>gnl|CDD|214330 CHL00001, rpoB, RNA polymerase beta subunit
MLRDGNEGMSTIPGFNQIQFEGFCRFIDQGLTEELSKFPKIEDTDQEIEFQLFVETYQLVEPLIKERDAV
YESLTYSSELYVPAGLIWKKSRDMQEQTVFIGNIPLMNSLGTFIINGIYRVVINQILRSPGIYYRSELDH
NGISVYTGTIISDWGGRLELEIDRKARIWARVSRKQKISILVLLSAMGLNLREILDNVCYPEIFLSFLND
KEKKKIGSKENAILEFYQQFACVGGDPVFSESLCKELQKKFFQQRCELGRIGRRNMNRKLNLDIPENNTF
LLPQDVLAAADYLIGMKFGMGTLDDIDHLKNKRIRSVADLLQDQFGLALNRLENAVRGTICGAIRRKLIP
TPQNLVTSTPLTTTYESFFGSHPLSQFLDQTNPLTEIVHGRKLSSLGPGGLTGRTASFRVRDIHPSHYGR
ICPIDTSEGINAGLIGSLAIHARIGHWGSLESPFYEISERSKEERMVYLSPSEDEYYMIAAGNSLALNQG
IQEEQVVPARYRQEFLTIAWEQIHLRSIFPFQYFSIGASLIPFLEHNDANRALMGSNMQRQAVPLSRSEK
CIVGTGLERQVALDSGVVAIAEHEGKIIYTDTDKIILSGNGDTLSIPLVMYQRSNKNTCMHQKPQVRRGK
CVKKGQILADGAATVGGELALGKNVLVAYMPWEGYNFEDAVLISERLVYEDIYTSFHIRKYEIQTHVTSQ
GPERITKEIPHLEAHLLRNLDKNGIVMLGSWVETGDILVGKLTPQEAEESSYAPEGRLLRAIFGIQVSTS
KETCLKLPIGGRGRVIDVRWIQKKGGSSYNPETIHVYILQKREIQVGDKVAGRHGNKGIISKILPRQDMP
YLQDGTPVDMVLNPLGVPSRMNVGQIFECLLGLAGDLLNRHYRIAPFDERYEQEASRKLVFSELYEASKQ
TANPWVFEPEYPGKSRLFDGRTGDPFEQPVTIGKAYILKLIHQVDDKIHARSSGPYALVTQQPLRGRSKQ
GGQRVGEMEVWALEGFGVAYILQEMLTYKSDHIRARQEVLGAIITGGTIPKPEDAPESFRLLVRELRSLA
LELNHFLVSEKNFQINRKEV
>gnl|CDD|214331 CHL00002, matK, maturase K
MEEFQGYLELDRSRQQDFLYPLLFQEYIYALAHDHGLNRSILLENSGYDNKYSLLIVKRLITRMYQQNHL
IISVNDSNQNPFLGHNKNFYSQMISEGFAVIVEIPFSLRLVSSLEEKEIAKSQNLRSIHSIFPFLEDKFS
HLNYVSDILIPYPIHLEILVQTLRYWIKDASSLHLLRFFLHEYCNWNSLITSKKSISFFSKENQRLFLFL
YNSYVCEYESIFVFLRKQSSHLRSTSSGVFLERIHFYGKIEHLVEVFRNDFQKTLWLFKDPFIHYVRYQG
KSILASKGTPLLMNKWKYYLVNFWQCHFHLWSQPGRIHINQLSNHSFDFLGYLSSVRLNPSVVRSQMLEN
SFLIDNAIKKFDTIVPIIPLIGSLAKAKFCNVLGHPISKPVWTDLSDSDIIDRFGRICRNLSHYYSGSSK
KKSLYRIKYILRLSCAKTLARKHKSTVRAFLKRLGSELLEEFFTEEEQVLSLIFPRTSSTSRRLYRERIW
YLDIICINDLVNHE
>gnl|CDD|176948 CHL00003, psbA, photosystem II protein D1
RRESTSLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNN
IISGAIIPSSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVA
YSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHG
SLVTSSLIRETTENESANLGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFT
ALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLA
>gnl|CDD|176949 CHL00004, psbD, photosystem II protein D2
MTIALGKFTKEENDLFDIMDDWLRRDRFVFVGWSGLLLFPCAYFALGGWFTGTTFVTSWYTHGLASSYLE
GCNFLTAAVSTPANSLAHSLLLLWGPEAQGDFTRWCQLGGLWTFVALHGAFGLIGFMLRQFELARSVQLR
PYNAIAFSGPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAAL
LCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGL
WMSAIGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHENLIFPEEVLPRG
NAL
>gnl|CDD|176950 CHL00005, rps16, ribosomal protein S16
MVKLRLKRCGRKQQAVYRIVAIDVRSRREGRDLEKVGFYDPIKNQTYLNVPAILYFLEKGAQPTETVYDI
LKKAEVFKELSL
>gnl|CDD|176951 CHL00008, petG, cytochrome b6/f complex subunit V
MIEVLLFGIVLGLIPITLAGLFVTAYLQYRRGDQLDL
>gnl|CDD|176952 CHL00009, petN, cytochrome b6/f complex subunit VIII
MDIVSLAWAALMVVFTFSLSLVVWGRSGL
>gnl|CDD|214332 CHL00010, infA, translation initiation factor 1
MKKENKIEMEGLVTESLPNGMFRVRLDNGCQVLGYISGKIRRNSIRILPGDRVKVELSPYDLTKGRIIYR
LRNKDSND
>gnl|CDD|176954 CHL00011, ndhD, NADH dehydrogenase subunit 4
MNYFPWLTIIVVLPIFAGSLIFFLPHRGNKVIRWYTLCICLLELLLTTYAFCYHFQLDDPLIQLKEDYKW
INFFDFHWRLGIDGLSIGPILLTGFITTLATLAAWPVTRNSRLFYFLMLAMYSGQIGLFSSRDLLLFFIM
WELELIPVYLLLSMWGGKKRLYSATKFILYTAGGSIFLLIGVLGMGLYGSNEPTLNFETLANQSYPVALE
ILFYIGFLIAYAVKLPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLIRINMELLPHAHSIFSPWL
VIVGAIQIIYAASTSLGQRNLKKRIAYSSVSHMGFIIIGIGSITDTGLNGAILQIISHGFIGAALFFLAG
TSYDRIRLVYLDEMGGIAIPMPKIFTMFSSFSMASLALPGMSGFVAELIVFFGIITSQKYLLMPKILITF
VMAIGMILTPIYLLSMLRQMFYGYKLFNVPNSYFFDSGPRELFISICILLPVIGIGIYPDFVLSLSVDKV
EAILSNYF
>gnl|CDD|176955 CHL00012, ndhJ, NADH dehydrogenase subunit J
MQGRLSAWLVKHGLVHRSLGFDYQGIETLQIKPEDWHSIAVILYVYGYNYLRSQCAYDVAPGGLLASVYH
LTRIQYGVDQPEEVCIKVFVPRKNPRIPSVFWVWKSADFQERESYDMLGISYDNHPRLKRILMPESWIGW
PLRKDYIAPNFYEIQDAH
>gnl|CDD|214333 CHL00013, rpoA, RNA polymerase alpha subunit
STQTLQWKCVESRVDSKRLYYGRFILSPLMKGQADTIGIALRRALLGEIEGTCITRAKIEGVPHEYSTIP
GIRESVLEILLNLKEIVLKSNLYGPQKASICVQGPKYVTAQDIILPPSVEIVDPTQHIATITEPIDLEIE
LKIEKGRGYRLKTPKNFQDGSFPIDAVFMPVRNVNYSIHSYGNGNEKQEILFLEIWTNGSITPKEALHEA
SRNLIDLFIPFLHAEEENLKLENNENRVTLLFTFHDRLTDLKKNKKEIALKQIFIEQLELSVRAYNCLKR
ANIHTLLDLLNYSQEDLLKIKNFGQKSAKEVLEALQKRFGIDLPKNK
>gnl|CDD|214334 CHL00014, ndhI, NADH dehydrogenase subunit I
MVTGFMNYGQQTIRAARYIGQGFMITLSHANRLPVTIQYPYEKLITSERFRGRIHFEFDKCIACEVCVRV
CPIDLPVVDWKLETDIRKKRLLNYSIDFGVCIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQIALG
RLPMSVIDDYTIRTISNSPQIKIVEEK
>gnl|CDD|176958 CHL00015, ndhE, NADH dehydrogenase subunit 4L
MMLEHVLILSAYLFSIGIYGLITSRNMVRALMCLELILNAVNINFVTFSDFFDSRQLKGDIFSIFVIAIA
AAEAAIGLAIVSSIYRNRKSTRINQSNLLKK
>gnl|CDD|214335 CHL00016, ndhG, NADH dehydrogenase subunit 6
MDLPEPIHDFLLVFLGSGLILGSLGVVLLTNPIYSAFSLGLVLVCISLFYILLNADFVAAAQLLIYVGAI
NVLIIFAVMFMNGPEYSKDFNLWTVGDGITSLVCTSLFFSLITTILDTSWYGIIWTTRSNQIIEQDLISN
VQQIGIHLSTDFLLPFELISIILLVALIGAITVARQEQVEET
>gnl|CDD|176960 CHL00017, ndhH, NADH dehydrogenase subunit 7
MTVPATRKDLMIVNMGPHHPSMHGVLRLIVTLDGEDVIDCEPILGYLHRGMEKIAENRTIIQYLPYVTRW
DYLATMFTEAITVNAPEQLGNIQVPKRASYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFREREL
IYDLFEAATGMRMMHNYFRIGGVAADLPYGWIDKCLDFCDYFLTGVAEYQKLITRNPIFLERVEGVGIIG
GEEAINWGLSGPMLRASGIQWDLRKVDHYECYDEFDWEVQWQKEGDSLARYLVRIGEMTESIKIIQQALE
GIPGGPYENLEARRFDREKDSEWNDFEYRFISKKPSPTFELSKQELYVRVEAPKGELGIFLIGDDSVFPW
RWKIRPPGFINLQILPQLVKRMKLADIMTILGSIDIIMGEVDR
>gnl|CDD|214336 CHL00018, rpoC1, RNA polymerase beta' subunit
MIDRYKHQQLRIGLASPQQIRAWAERILPNGEIVGEVTKPYTIHYKTNKPEKDGLFCERIFGPIKSGICA
CGNYRVIGDEKEDPKFCEQCGVEFTDSRVRRYRMGYIKLACPVTHVWYLKRLPSYIANLLDKPLKELEGL
VYCDFSFARPIAKKPTFLRLRGLFEYEIQSWKYSIPLFFSTQGFDTFRNREISTGAGAIREQLADLDLRI
IIDNSLVEWKELGEEGSTGNEWEDRKIGRRKDFLVRRIKLAKHFIRTNIEPEWMVLCLLPVLPPELRPII
QLDGGKLMSSDLNELYRRVIYRNNTLTDLLTTSRSTPGELVMCQKKLLQEAVDALLDNGIRGQPMRDGHN
KPYKSFSDVIEGKEGRFRENLLGKRVDYSGRSVIVVGPSLSLHQCGLPREIAIELFQPFVIRGLIRQHLA
SNIRAAKSKIREKEPIVWEILQEVMQGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADF
DGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVPSQDMLLGLYVLTIGNRRGIYANRYNPCNR
KNSTKEPYFSNSYDALGAYRQKRINLDSPLWLRWRLDQRIIASREVPIEVQYESLGTYHEIYEHYLIVKS
RKKEILSIYIRTTVGRILFNREIEEAIQGFSRA
>gnl|CDD|176962 CHL00019, atpF, ATP synthase CF0 B subunit
MKNVTDSFVSLGHWPSAGSFGFNTDILETNLINLSVVLGVLIYFGKGVLSDLLDNRKQTILNTIRNSEER
REEAIEKLEKARARLRQAELEADEIRVNGYSEIEREKENLINQAKEDLERLENYKNETIRFEQQRAINQV
RQQVFQLALQRALGTLNSCLNNELHLRTINANIGLLGAMKEITD
>gnl|CDD|176963 CHL00020, psbN, photosystem II protein N
METATLVAIFISGLLVSFTGYALYTAFGQPSKQLRDPFEEHED
>gnl|CDD|176964 CHL00022, ndhC, NADH dehydrogenase subunit 3
MFLLYEYDIFWAFLIISSLIPILAFLISGLLAPISKGPEKLSSYESGIEPMGDAWLQFRIRYYMFALVFV
VFDVETVFLYPWAMSFDVLGVSAFIEALIFVLILIVGLVYAWRKGALEWS
>gnl|CDD|214337 CHL00023, ndhK, NADH dehydrogenase subunit K
MNSIEFPLLDRTTSNSVISTTLNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPR
QADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCP
PKPEAVIDAITKLRKKISREIYEDRIRSQQENRCFTTNHKFHVVRSTHTGNYDQELLYQSPSTSEIPSET
FFKYKSSVSSHELVN
>gnl|CDD|176966 CHL00024, psbI, photosystem II protein I
MLTLKLFVYTVVIFFVSLFIFGFLSNDPGRNPGRKE
>gnl|CDD|214338 CHL00025, ndhF, NADH dehydrogenase subunit 5
MEHTYQYAWIIPFLPLPVPMLIGLGLLLFPTATKNLRRMWAFPSILLLSIVMIFSLNLSIQQINGSSIYQ
YLWSWTINNDFSLEFGYLIDPLTSIMLILITTVGILVLIYSDNYMSHDQGYLRFFAYLSFFNTSMLGLVT
SSNLIQIYIFWELVGMCSYLLIGFWFTRPIAANACQKAFVTNRVGDFGLLLGILGFYWITGSFEFRDLFE
IFNNLIYNNEVNLLFATLCAFLLFLGPVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARL
LPLFIVIPYIMNLISLIGIITALLGATLALAQKDIKRGLAYSTMSQLGYMMLALGIGSYRAALFHLITHA
YSKALLFLGSGSVIHSMEPIVGYSPDKSQNMVLMGGLRKYMPITKTTFLLGTLSLCGIPPLACFWSKDEI
LNDSWLYSPIFAIIAWSTAGLTAFYMFRIYLLTFEGHLRVHFQNYSGKKNSSFYSISLWGKEESKKINKL
LLLLTMNNNERVSFFSKKTYKIDGNVRNMIRSFITIFGNKKTFSYPHESDNTMLFPLLVLVLFTLFVGFI
GIPFNQEGIDLDILSKWLTPSINLLHQNSNNSVDWYEFLTNAIFSVSIAFFGIFIASFLYGPVYSSLQNL
DLINSFVKGGPKRIFLDKIINVIYNWSYNRGYIDAFYTISFIKGIRGLAELTHFFDRRVIDGITNGVGIT
SFFVGEGIKYVGGGRISSYLFLYLFYVSIFLLILYFFFSFI
>gnl|CDD|214339 CHL00027, rps15, ribosomal protein S15
MVKNSFISVISQEEKEENRGSVEFQVFSFTNKIRRLTSHLELHKKDYSSQRGLRKILGKRQRLLAYLSKK
NRVRYKKLISQLGIRELKTR
>gnl|CDD|214340 CHL00028, clpP, ATP-dependent Clp protease proteolytic subunit
MPIGVPKVPFRLPGEEDATWVDLYNRLYRERLLFLGQEVDDEIANQLIGLMVYLSIEDDTKDLYLFINSP
GGSVISGLAIYDTMQFVKPDVHTICLGLAASMASFILAGGEITKRLAFPHARVMIHQPASSFYEGQASEF
VLEAEELLKLRETITRVYAQRTGKPLWVISEDMERDVFMSATEAKAYGIVDLVAVNNEEE
>gnl|CDD|176970 CHL00029, rpl36, ribosomal protein L36
MKIRASVRKICEKCRLIRRRGRIFVI
>gnl|CDD|176971 CHL00030, rpl23, ribosomal protein L23
MDGIKYPVFTDKSIRLLEKNQYTFDVDSGSTKTEIKHWIELFFGVKVIAVNSHRLPRKKRRMGPIMGHKM
HYKRMIITLQPGYSIPLFREKRT
>gnl|CDD|176972 CHL00031, psbT, photosystem II protein T
MEALVYTFLLVSTLGIIFFAIFFREPPKVPTKK
>gnl|CDD|214341 CHL00032, ndhA, NADH dehydrogenase subunit 1
MIIDTTEVQAINSFSRLESLKEVYGLIWILVPILTLVLGITIGVLVIVWLEREISAGIQQRIGPEYAGPL
GILQALADGTKLLFKEDLLPSRGDIRLFSIGPSIAVISILLSYLVIPFGYHLVLADLSIGVFLWIAISSI
APIGLLMSGYGSNNKYSFLGGLRAAAQSISYEIPLTLCVLSISLLSNSLSTVDIVEAQSKYGFWGWNLWR
QPIGFIVFLISSLAECERLPFDLPEAEEELVAGYQTEYSGIKFGLFYVASYLNLLVSSLFVTVLYLGGWN
LSIPYIFIPELFEINKTGGVFGTTIGIFITLAKTYLFLFISITTRWTLPRLRMDQLLNLGWKFLLPISLG
NLLLTTSFQLLSL
>gnl|CDD|176974 CHL00033, ycf3, photosystem I assembly protein Ycf3
MPRSQRNDNFIDKTFTIVADILLRILPTTSGEKEAFTYYRDGMSAQSEGEYAEALQNYYEAMRLEIDPYD
RSYILYNIGLIHTSNGEHTKALEYYFQALERNPFLPQALNNMAVICHYRGEQAIEQGDSEIAEAWFDQAA
EYWKQAIALAPGNYIEAQNWLKITGRFE
>gnl|CDD|214342 CHL00034, rpl22, ribosomal protein L22
MMKKKSTTEVYALAKYIRMSAHKARRVIDQIRGRSYEEALMILEFMPYRACYPILKLVYSAAANASHNMG
LNKANLFISKAEVDEGPTLKRFRPRAQGRSYPIKKPTCHITIVLKDI
>gnl|CDD|214343 CHL00035, psbC, photosystem II 44 kDa protein
MKTLYSLRRFYHVETLFNGTLALAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLF
EVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETL
EESFPFFGYVWKDKNKMTTILGIHLILLGIGAFLLVFKALYFGGVYDTWAPGGGDVRKITNLTLSPSVIF
GYLLKSPFGGEGWIVSVDNLEDIIGGHVWLGSICILGGIWHILTKPFAWARRAFVWSGEAYLSYSLGALS
VFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEII
FGGETMRFWDLRAPWLEPLRGPNGLDLSKLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYV
SPRSWLATSHFVLGFFFFVGHLWHAGRARAAAAGFEKGIDRDFEPVLSMTPLN
>gnl|CDD|176977 CHL00036, ycf4, photosystem I assembly protein Ycf4
MNWRSEEIRRELITGSRRISNFFWAFILFLGSLGFLLVGISSYLGKNLIPFLPSQQILFFPQGIVMCFYG
IAGLFISSYLWCTILWNVGSGYNEFDKKEGIVCIFRWGFPGKNRRIFLRFLIKDIQSIRIEVKEGLNPRR
VLYLEIKGQRDIPLTRTGEPLTLREIEQKAAELAYFLRVPIEGF
>gnl|CDD|176978 CHL00037, petA, cytochrome f
MQNRNTFSWIKKQITRSISVSLMIYIITRTSISNAYPIFAQQGYENPREATGRIVCANCHLANKPVDIEV
PQAVLPDTVFEAVVKIPYDMQLKQVLANGKKGGLNVGAVLILPEGFELAPPDRISPEMKEKIGNLSFQPY
SPEKKNILVVGPVPGKKYSEIVFPILSPDPATNKDVHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNATA
AGIVSKILRKEKGGYEITIVDTSDGRQVVDIIPPGPELLVSEGESIKLDQPLTNNPNVGGFGQGEAEIVL
QDPLRVQGLLFFLASVILAQIFLVLKKKQFEKVQLAEMNF
>gnl|CDD|176979 CHL00038, psbL, photosystem II protein L
MTQSNPNKQNVELNRTSLYWGLLLIFVLAVLFSNYFFN
>gnl|CDD|176980 CHL00039, psbF, photosystem II protein VI
MTIDRTYPIFTVRWLAVHGLAVPTVFFLGSISAMQFIQR
>gnl|CDD|176981 CHL00040, rbcL, ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
MSPQTETKASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVW
TDGLTSLDRYKGRCYRIEPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRI
PPAYLKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQP
FMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMHDYLTGGFTANTSL
AHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLR
DDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVAN
RVALEACVQARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFETTDTL
>gnl|CDD|176982 CHL00041, rps11, ribosomal protein S11
RIGSRKSKRKIPKGVIHIQASFNNTIVTVTDVRGRVISWSSAGACGFKGARKGTPFAAQTAAENAIRTVI
DQGMKRAEVMIKGPGLGRDTALRAIRRSGLKLSSIRDVTPMPHNGC
>gnl|CDD|214344 CHL00042, rps8, ribosomal protein S8
MGNDTIADMLTRIRNANMVKKGTVRIPATNITENIVKILLREGFIENVREHRENNKYFLVLTLKYRGNKK
KPYITTLKRISKPGLRIYSNYKEIPRVLGGMGIVILSTSKGIMTDREARLKGIGGEILCYIW
>gnl|CDD|214345 CHL00043, cemA, envelope membrane protein
IGLIPRSITRTLSRFRKELTPNSESLVIQEFRMAKKKALTSLLYLASLVFLPWWISFSFKKSLEPWVTNW
WNTRQSEIFLNDIQEKRALEKFIELEELLLLDEMIKEYPETHLQKLRIGIHKETIQLAKIYNEDSIHTIL
HLSTNIISFAILSGLSILGKEELVILNSWLQEFLYNLSDTIKAFSILLLTDLCIGFHSPHGWELLIGSIY
KHFGFAHNDQIISLLVSTFPVILDTIFKYWIFRYLNRVSPSLVVIYHSMNE
>gnl|CDD|176985 CHL00044, rpl16, ribosomal protein L16
MLSPKRTKFRKQHRGRMKGISYRGNRICFGRYALQALEPAWITSRQIEAGRRAITRYARRGGKIWIRIFP
DKPVTMRPAETRMGSGKGSPEYWVAVVKPGRILYEMGGVSETIARAAIKIAAYKMPIKTQFIISE
>gnl|CDD|214346 CHL00045, ccsA, cytochrome c biogenesis protein
MIFITLEHILTHISFSLLSIVTLIYWITLLVDEIIGLYDSSEKGMIITFFCITGLLVTRWIYSGHFPLSN
LYESLIFLSWSLSIIHIVPYFKKKKNRLLGAITAPSAIFTQGFATSGLPTEMQQSTILVPALQSNWLMMH
VSMMILSYAALLCGSLLSIALLVITFRKNIDIFGKKNNLLNKSFSFSEIQYLNEKNNVLKNTSFFSSKNY
YKYQLIQQLDNWSYRIISLGFPFLTIGILSGAVWANEAWGSYWSWDPKETWALITWLIFAIYLHTRTNKG
WQGKKSAIVASIGFLIIWICYLGVNLLGIGLHSYGWFTL
>gnl|CDD|176987 CHL00046, atpI, ATP synthase CF0 A subunit
YDISGVEVGQHFYWQIGGFQVHGQVLITSWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAK
TQIGEEEYRPWVPFIGTMFLFIFVSNWSGALLPWKLIELPHGELAAPTNDINTTVALALLTSVAYFYAGL
SKKGLGYFGKYIQPTPILLPINILEDFTKPLSLSFRLFGNILADELVVAVLVSLVPLVVPIPVMFLGLFT
SGIQALIFATLAAAYIGE
>gnl|CDD|214347 CHL00047, psbK, photosystem II protein K
IFSLICICLNSALYSSSFFFAKLPEAYAIFNPIVDVMPVIPVLFFLLAFVWQAAVSFR
>gnl|CDD|214348 CHL00048, rps3, ribosomal protein S3
MGQKINPLGFRLGTTQKHHSLWFAQPKNYSEGLQEDKKIRDCIKNYVQKNIKYEGIARIEIQRKIDLIQV
IIYTGFPKLLIERKGRGIEELQINLQKELNSVNRKLNINITEVKKPYGEPNILAEYIAGQLENRVSFRKA
MKKAIELAEKADIKGIKIQISGRLNGAEIARVEWIREGRVPLQTLRAKIDYCSYPARTIYGVLGIKIWIF
KDEE
>gnl|CDD|176990 CHL00049, ndhB, NADH dehydrogenase subunit 2
IFMKAFHLLLFDGSFIFPECILIFGLILLLMIDLTSDQKDIPWLYFISSTSLVMSITALLFQWREEPMIS
FSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAL
ECLSLCSYLLSGYTKKDVRSNEATMKYLLMGGASSSILVYGFSWLYGLSGGEIELQEIVNGLINTQMYNS
PGISIALIFITVGIGFKLSLAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASALATRIFDIPFYFSSNEWH
LLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYIFMNLGTF
ACIVLFGLRTGTDNIRDYAGLYTKDPFLALSLALCLLSLGGIPPLAGFFGKLYLFWCGWQAGLYFLVSIG
LLTSVISIYYYLKIIKLLMTGRNQEITPYVRNYRRSPLRSNNSIELSMIVCVIASTIPGISMNPIIAIAQ
DTLF
>gnl|CDD|176991 CHL00050, rps19, ribosomal protein S19
MTRSLKKNPFVANHLLKKIEKLNTKEEKEIIVTWSRASTIIPTMIGHTIAVHNGKEHIPIYITDQMVGHK
LGEFAPTRNFRGHAKNDKKSRR
>gnl|CDD|176992 CHL00051, rps12, ribosomal protein S12
MPTIKQLIRNTRQPIRNKTKSPALRGCPQRRGTCTRVYTITPKKPNSALRKVARVRLTSGFEITAYIPGI
GHNLQEHSVVLVRGGRVKDLPGVRYHIVRGTLDAVGVKDRQQGRSKYGVKKPK
>gnl|CDD|176993 CHL00052, rpl2, ribosomal protein L2
MAIRLYKTYTPGTRNRSVDEQVKSNPRKNLIYGQHRCGKGRNNRGIITARHRGGGHKRLYRKIDFRRNKK
DIYGRIVTIEYDPNRNAYICLIHYGDGEKRYILHPRGLKIGDTIVSGTEAPIKIGNALPLTNIPLGTAIH
NIEITPGKGGQLARAAGAVAKLIAKEGKSATLKLPSGEVRLISKNCSATIGQVGNVDVNNKSLGKAGSKR
WLGKRPKVRGVVMNPVDHPHGGGEGRAPIGRKKPVTPWGKPALGRKTRKRKKYSDNLILRRRK
>gnl|CDD|176994 CHL00053, rps7, ribosomal protein S7
MSRRGTAKKRTAKPDPIYRNRLVNMLVNRILKSGKKSLAYRIVYRALKKIQQKTEKNPLSVLRQAIRNVT
PDVEVKARRVGGSTYQVPIEIGSTRGKALAIRWLLKASRKRSGRNMAFKLSSELVDAAKGSGNAIRKKEE
THRMAEANRAFAHFR
>gnl|CDD|176995 CHL00054, psaB, photosystem I P700 chlorophyll a apoprotein A2
MALRFPKFSQGLAQDPTTRRIWFGIATAHDFESHDDITEERLYQKIFASHFGQLAIIFLWTSGNLFHVAW
QGNFEAWVQDPLHVRPIAHAIWDPHFGQPAVEAFTRGGALGPVNIAYSGVYQWWYTIGLRTNEDLYTGAL
FLLFLSALSLIAGWLHLQPKWKPSVSWFKNAESRLNHHLSGLFGVSSLAWTGHLVHVAIPESRGEHVRWN
NFLDVLPHPQGLGPLFTGQWNLYAQNPDSSSHLFGTSQGAGTAILTFLGGFHPQTQSLWLTDIAHHHLAI
AVVFLIAGHMYRTNFGIGHSMKDILEAHIPPGGRLGRGHKGLYDTINNSLHFQLGLALASLGVITSLVAQ
HMYSLPAYAFIAQDFTTQAALYTHHQYIAGFIMTGAFAHGAIFFIRDYNPEQNEDNVLARMLDHKEAIIS
HLSWASLFLGFHTLGLYVHNDVMLAFGTPEKQILIEPIFAQWIQSAHGKTSYGFDVLLSSTNSPAFNAGR
SIWLPGWLNAINENSNSLFLTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCD
GPGRGGTCDISAWDAFYLAVFWMLNTIGWVTFYWHWKHITLWQGNVSQFNESSTYLMGWLRDYLWLNSSQ
LINGYNPFGMNSLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLAWAHERTPLANLIRWRDKPVAL
SIVQARLVGLAHFSVGYIFTYAAFLIASTSGKFG
>gnl|CDD|176996 CHL00056, psaA, photosystem I P700 chlorophyll a apoprotein A1
MIIRSPEPEVKILVDRDPVKTSFEKWAKPGHFSRTLAKGPDTTTWIWNLHADAHDFDSHTSDLEEISRKV
FSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLSDPTHIKPSAQVVWPIVGQEILNGDVGGGFRGIQITSG
FFQIWRASGITSELQLYCTAIGALVFAALMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSW
AGHQIHVSLPINQLLDAGVDPKEIPLPHEFILNRDLLAQLYPSFAKGLTPFFTLNWSEYSDFLTFRGGLN
PVTGGLWLTDIAHHHLAIAVLFLIAGHMYRTNWGIGHSLKEILEAHKGPFTGEGHKGLYEILTTSWHAQL
ALNLAMLGSLTIIVAHHMYSMPPYPYLATDYGTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTRY
NNLLDRVLRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPIFAQWIQNTHAL
APGATAPGATASTSLTWGGGDLVAVGGKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRL
IPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSISVVIFHFSWKMQSDVWGSISDQGVVTHIT
GGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLFFLGAHFVWAFSLMFLFSGRGYWQELIESIV
WAHNKLKVAPAIQPRALSIVQGRAVGVAHYLLGGIATTWAFFLARIIAVG
>gnl|CDD|176997 CHL00057, rpl14, ribosomal protein L14
MIQPQTYLNVADNSGARKLMCIRVLGASNRKYAHIGDVIIAVVKEAVPNMPLKRSEVVRAVIVRTCKELK
RDNGMIIRFDDNAAVVIDQEGNPKGTRVFGPIARELREKNFTKIVSLAPEVL
>gnl|CDD|176998 CHL00058, petD, cytochrome b6/f complex subunit IV
MGVTKKPDLNDPVLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPSMIGEPADPFA
TPLEILPEWYFFPVFQILRTVPNKLLGVLLMASVPAGLLTVPFLENVNKFQNPFRRPVATTVFLIGTAVA
LWLGIGATLPIDKSLTLGLF
>gnl|CDD|176999 CHL00059, atpA, ATP synthase CF1 alpha subunit
EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKAT
GKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR
GQRELIIGDRQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSP
ATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERA
AKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQ
IKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQSAPLTVEEQVATIYTGT
NGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLELFLLQEQT
>gnl|CDD|214349 CHL00060, atpB, ATP synthase CF1 beta subunit
INPTGPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRV
RAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDT
KLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYM
EMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSE
VSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSR
GLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARA
RKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVES
KLKK
>gnl|CDD|177001 CHL00061, atpH, ATP synthase CF0 C subunit
MNPLISAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVV
ALALLFANPFV
>gnl|CDD|214350 CHL00062, psbB, photosystem II 47 kDa protein
MGLPWYRVHTVVLNDPGRLISVHLMHTALVAGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLG
ITNSWGGWSITGETVTNPGIWSYEGVAGAHIVLSGLCFLAAIWHWVYWDLEIFRDERTGKPSLDLPKIFG
IHLFLSGVLCFGFGAFHVTGLYGPGIWVSDPYGLTGKVQPVNPAWGAEGFDPFVPGGIASHHIAAGTLGI
LAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYF
QQEIYRRVSAGLAENLSLSEAWSKIPEKLAFYDYIGNNPAKGGLFRAGAMDNGDGIAVGWLGHPIFRDKE
GRELFVRRMPTFFETFPVVLVDKDGIVRADVPFRRAESKYSVEQVGVTVEFYGGELNGVSFSDPATVKKY
ARRAQLGEIFEFDRATLKSDGVFRSSPRGWFTFGHASFALLFFFGHIWHGARTLFRDVFAGIDPDLDAQV
EFGAFQKLGDPTTR
>gnl|CDD|214351 CHL00063, atpE, ATP synthase CF1 epsilon subunit
MTLNLRVLTPNRIVWDSEVEEIILPTNSGQIGVLPNHAPIATALDIGVLRIRLNDQWLTMALMGGFARIG
NNEITILVNDAEKGSDIDPQEAQQTLEIAEANLEKAEGKKQKIEANLALKRARARVEAINAISS
>gnl|CDD|177004 CHL00064, psbE, photosystem II protein V
MSGSTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESRQEIPLITGRF
DPLEQLDEFTRSF
>gnl|CDD|177005 CHL00065, psaC, photosystem I subunit VII
MSHSVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPTDFLSVRVYLG
HETTRSMGLAY
>gnl|CDD|177006 CHL00066, psbH, photosystem II protein H
MATQTVEDSSRSGPRRTTVGNLLKPLNSEYGKVAPGWGTTPLMGVAMALFAVFLSIILEIYNSSVLLDGI
SVS
>gnl|CDD|177007 CHL00067, rps2, ribosomal protein S2
MTRRMWNINLEEMLEAGVHFGHQTRKWNPKMAPYIYAERNGIHIINLVQTARFLSEACDLVFDAASKGKK
FLFVGTKKQAADLVASAAIRARCHYVNKRWLGGMLTNWSTTKTRLQKLRDLRMEEKTGLFNRLPKKEAAI
LKRQLSRLEKYLGGIKYMTKLPDIVIIIDQQEEYTALRECRKLGIPTISILDTNCDPDLADIPIPANDDA
IASIKLILNKLTTAICEGRS
>gnl|CDD|214352 CHL00068, rpl20, ribosomal protein L20
MTRVKRGYIARKRRKKILKFASGFRGAHSRLFRTANQQKMKALVSSYRDRKKKKRDFRRLWITRINAAIR
ENGVSYSKFIHNLYKNQILLNRKILAQIAILDPNCFYTISNKIIK
>gnl|CDD|177009 CHL00070, petB, cytochrome b6
MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFASVQ
YIMTEVNFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVVLAVLTVSFGVTGYSLPW
DQIGYWAVKIVTGVPEAIPVIGSPLVELLRGSVSVGQSTLTRFYSLHTFVLPLLTAVFMLMHFLMIRKQG
ISGPL
>gnl|CDD|177010 CHL00071, tufA, elongation factor Tu
MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEY
ETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQ
VDDEELLELVELEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKIKRGENKWVDKIYNLMDAVDSYI
PTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGL
AGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTKEEGGRHTPFFPGYRPQFYVRTTDVTG
KIESFTADDGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGAGVVSKILK
>gnl|CDD|177011 CHL00072, chlL, photochlorophyllide reductase subunit L
MKLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWP
EDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYAD
YCIIITDNGFDALFAANRIAASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIR
VSRVKGKTLFEMVESEPSLNYVCDYYLNIADQLLSQPEGVVPKEVPDRELFSLLSDFYLNPIGNEGQKND
QENLLDFTIV
>gnl|CDD|214353 CHL00073, chlN, photochlorophyllide reductase subunit N
MSTKISETLTFECETGNYHTFCPISCVAWLYQKIEDSFFLVIGTKTCGYFLQNALGVMIFAEPRYAMAEL
EEGDISAQLNDYEELKRLCLQIKKDRNPSVIVWIGTCTTEIIKMDLEGMAPKLEAEIGIPIVVARANGLD
YAFTQGEDTVLAAMAHRCPEQEVSTSESKETKQKTQSSLFSNKEKSLVKYKTHPPLVLFGSLPSTVASQL
TLELKRQGIKVSGWLPSQRYTDLPSLGEGVYVCGVNPFLSRTATTLMRRRKCKLIGAPFPIGPDGTRAWI
EKICSVFGIEPQGLEEREEQIWESLKDYLDLVRGKSVFFMGDNLLEISLARFLIRCGMIVYEIGIPYMDK
RYQAAELALLEDTCRKMNVPMPRIVEKPDNYNQIQRIRELQPDLAITGMAHANPLEARGINTKWSVEFTF
AQIHGFTNARDVLELVTRPLRRNNNLENLGWTSLVKK
>gnl|CDD|214354 CHL00074, rps14, ribosomal protein S14
MAKKSLIQREKKRQKLVQKYHLKRRSLKKEIKKVSSLSEKWEIHGKLQSLPRNSAPTRLHNRCFLTGRPR
GNYRDFGLSRHVLREMAHACLLPGVTKSSW
>gnl|CDD|177014 CHL00075, rpl21, ribosomal protein L21
MMTYAIIEAGGKQLWVEPGRFYDINHFPLEPGTKILLNRVLLIRNESEILIGKPWLENATVKGRILHHFR
GKKITVYKMRPKKKTRKKQGHRQKLTRFLIDSISFNGK
>gnl|CDD|214355 CHL00076, chlB, photochlorophyllide reductase subunit B
MKLAYWMYAGPAHIGTLRVASSFKNVHAIMHAPLGDDYFNVMRSMLERERDFTPVTASIVDRHVLARGSQ
EKVVDNITRKDKEERPDLIVLTPTCTSSILQEDLQNFVDRASIESDSDVILADVNHYRVNELQAADRTLE
QIVRFYLEKARKQGTLDQSKTDKPSVNIIGIFTLGFHNQHDCRELKRLLQDLGIEINQIIPEGGSVEDLK
NLPKAWFNIVPYREVGLMTAKYLEKEFGMPYISTTPMGIVDTAECIRQIQKILNKLASDILEKKVDYEKY
IDQQTRFVSQAAWFSRSIDCQNLTGKKAVVFGDATHAASMTKILAREMGIRVSCAGTYCKHDAEWFKEQV
QGFCDEILITDDHTEVGDMIARVEPSAIFGTQMERHIGKRLDIPCGVISAPVHIQNFPLGYRPFLGYEGT
NQIADLVYNSFTLGMEDHLLEIFGGHDTKEIITKSLSTDSDLIWSPESQLELSKIPGFVRGKVKRNTEKF
ARQNGITNITVEVMYAAKEALSA
>gnl|CDD|177016 CHL00077, rps18, ribosomal protein S18
MDKSKRPFRKSKRSFRRRLPPIQSGDRIDYKNMSLLSRFISEQGKILSRRVTRLTLKQQRLITKAIKQAR
ILSLLPFLNNEKQFER
>gnl|CDD|214356 CHL00078, rpl5, ribosomal protein L5
MVQRLKSLYKEKIVPKLIEKFLYKNIHQVPKLKKIVINRGLGEASQNSKILESSIKELTIITGQKPIITR
AKKAIAGFKIREKMPVGVSVTLRGDKMYAFLDRLINLALPRIRDFQGLSPKSFDGHGNYNLGLKEQLMFP
EIDYDKIDQIRGMDISIVTTAKTDQEGLALLKELGMPFKDK
>gnl|CDD|214357 CHL00079, rps9, ribosomal protein S9
SKILYIGTGRRKTAVAQVRLVPGSGEIIINGKPAEEYLQYNPNYLNAIKAPLKLLGLENKYDIIVKVKGG
GLTGQAEAIRLGLARALCKINPENRKSLKKEGFLTRDARIKERKKYGLKKARKAPQFSKR
>gnl|CDD|177019 CHL00080, psbM, photosystem II protein M
MEVNILAFIATALFILVPTAFLLIIYVKTVSQND
>gnl|CDD|177020 CHL00081, chlI, Mg-protoporyphyrin IX chelatase
MVTNNLKKKERPVFPFTAIVGQEEMKLALILNVIDPKIGGVMIMGDRGTGKSTTIRALVDLLPEIEVVKD
DPFNSHPSDPELMSDEVREAIQNGETIETEKIKIPMVDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLL
AKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFG
MHAEIRTVKDPELRVKIVEQRTSFDKNPQEFREKYEESQEELRSKIVAAQNLLPKVEIDYDLRVKISQIC
SELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDIFKVITLCLRHRLRKDPLESIDSGDKVQKVFKEVFG
>gnl|CDD|177021 CHL00082, psbZ, photosystem II protein Z
MTIAFQLAVFALIATSFLLVIGVPVVFASPDGWSSNKNVVFSGTSLWIGLVFLVGILNSLIS
>gnl|CDD|214358 CHL00083, rpl12, ribosomal protein L12
MSTKINEIIEELKSLTLLEAAELVKQIEETFGVDASAPVGGGMMSAPAAAAAQAAEEVEEKTEFDVILEE
VPADKRIAVLKVVRSLTGLGLKEAKELVESLPKTIKEGISKEEAEEAKKQLEEAGAKVIIK
>gnl|CDD|177023 CHL00084, rpl19, ribosomal protein L19
MMKLQQLVKEIESEFLKKNLPKIRVGDTVKVGVLIQEGNKERVQFYEGTVIAKKNSGLNTTITVRKVFQG
IGVERVFLLHSPKLASIEVLRRSKVRRAKLYYLRNRVGKAARLKQKF
>gnl|CDD|214359 CHL00085, ycf24, putative ABC transporter
MNKSLKSLNSNLTKLVNQPYKYGFSTLIETERLPKGLNEDIVRLISKKKNEPIFLLIFRLKAYKKWKKMK
EPDWAFLKYPEIDYQDISYYSAPKLKKKLNSLDEVDPELLDTFEKLGISLNEQKRLANVAVDAVFDSVSI
GTTFKEELAKAGVIFCSISEAIQKYPELIKKYLGSVVPIGDNYFAALNSAVFSDGSFCYIPKDTKCPLEL
STYFRINNEESGQFERTLIIAEENSYVSYLEGCTAPQYDTNQLHAAVVELIALENAEIKYSTVQNWYAGD
ENGEGGIYNFVTKRGLCAGKNSKISWTQVETGSAITWKYPSCILIGDNSQGEFYSVALTNNYQQADTGTK
MIHIGKNTKSRIISKGISAGKSKNSYRGLVKIGPKALNSRNYSQCDSLLIGNKSQANTFPYIQVQNSTAK
IEHEASTSKIGEEQLFYFLQRGINLEEAISLLISGFCKDVFNKLPMEFALEADRLLSLKLEGSVG
>gnl|CDD|164492 CHL00086, apcA, allophycocyanin alpha subunit
MSIVTKSIVNADAEARYLSPGELDRIKSFVLSGQRRLRIAQILTDNRERIVKQGGQQLFQKRPDIVSPGG
NAYGEEMTATCLRDLDYYLRLVTYGIVAGDVTPIEEIGLVGVKEMYNSLGTPISGVAEGVRSMKSVACSL
LAGEDSAEAGFYFDYTIGAMQ
>gnl|CDD|164493 CHL00088, apcB, allophycocyanin beta subunit
MQDAITSVINAADVQGKYLDDNSVEKLRSYFQTGELRVRAAATIAANAATIIKEAVAKSLLYSDITRPGG
NMYTTRRYAACIRDLDYYLRYATYGMLAGDPSILDERVLNGLKETYNSLGVPIGATIQAIQAMKEVTASL
VGPDAGKEMGVYFDYICSGLS
>gnl|CDD|100206 CHL00089, apcF, allophycocyanin beta 18 subunit
MQDAITAIINRYDLTGKYLDKNAITQLNSYFSSASDRIKIVEIINAQASNIIKEASAQLFEEQPELLRPG
GNAYTTRRYAACLRDIEYYLRYASYAIVAGDTNILDERVLDGLKDTYNSLGVPIAPTVRSIELLKEIIKE
EIKSQNIDAHDYIDEPFQYMIKNLSEQDL
>gnl|CDD|164494 CHL00090, apcD, allophycocyanin gamma subunit
MSLVSQIILNADDELRYPTIGELESIQDYLKTGEKRIRIATILRDNEKEIIQKASKQLFQIHPEYIAPGG
NASGSRQRSLCLRDYGWYLRLITYGVLAGDKNSIEKIGIIGVREMYNSLGVPIIGMVDSIQCLKEAALEV
LSPEDVKIIEPYFDYIIQGMS
>gnl|CDD|164495 CHL00091, apcE, phycobillisome linker protein
MSVRASSGSPLVRPQLYRTASISTISQAEQQDRFLQLGELDQLVTYLNSGNKRLEIADILTKNANLIVSR
AADRIFVGGSPISYLERPQAAVTLTGDQSSQTKIQSLSGNIQGNFFRSLFNAGGATPAGFKPINVVRYGT
TRMRKSLRDLDWFLRYLTYAIVAGDPNILSVNIRGLRELIDNACSSAAAIVALREMRRVSLSIFTEDIEG
QELVKEYFDVVISEFEAPALTDKVRKRSSTDLQGLRLPQIYSQAGVSKPRFVMKPNLSSTEKNQVIKACY
RQIFERDIAKAYGLSLSELESKVKNGQISIKEFIRALGKSEIYRKQFYEPFVNSRVLELAFRHFLGRGPS
SLEEFQKYFAILSSRGLDGLVDALLNSKEYADYFGEETVPYLRQLGEEAQECRNWGAQIDLLNYSAPFRK
VPQFITLFSDYKQPLPDQHPYGRGNDPLSIQFGAIFPKETVNPRKRPALFGKDTRRILVRRGPGIYNQIS
NPNARQKSPGSLGPKIFKLSNVLSKNETSLEVIIKAAYLRVFGREVYEEEKIWLKPLENELRRRQISVRE
FVRQLAKSSVFRSLYWSPLYICKAIEYIHNRLLGRPTYGRQEINKYFDIAYKSGFYALIDALIDSPEYIE
TFGNNTVPYERYSTPAGLALRILRLSIIDSKSAKVISSKEARFIELGQAKESRSSSSIQSRIQQGVSLLR
DQSVVFKVNSHSDKENLEQVLRAAYRQIFERDLNSFIIGGEFLDIESAFLNGQISVRELVEKLGSSSLYG
KEFYQPYPNTKVIELGTKHFLGRAPNNQAEIRYYNQILASQGLAAFISTLVNSKEYRSVFGEDTVPYRRF
PTLPAANFPNTEKLYNRLTKQNRSIVVPSFKSVLGNQ
>gnl|CDD|177025 CHL00093, groEL, chaperonin GroEL
MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGV
ALIRQAASKTNDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDI
QAITQVASISAGNDEEVGSMIADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERM
EVVQENPYILLTDKKITLVQQDLLPILEQVTKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPG
FGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQARRIIVTKDSTTIIADGNEEQVKARCEQLRK
QIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAINATKAAVEEGIVPGGGATLVH
LSENLKTWAKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGYNAANNKFVNMY
EAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS
>gnl|CDD|214360 CHL00094, dnaK, heat shock protein 70
MGKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKGDLLVGQIAKRQAVINPENTFYSVK
RFIGRKFSEISEEAKQVSYKVKTDSNGNIKIECPALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVI
TVPAYFNDSQRQATKDAGKIAGLEVLRIINEPTAASLAYGLDKKNNETILVFDLGGGTFDVSILEVGDGV
FEVLSTSGDTHLGGDDFDKKIVNWLIKEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPF
ITATQTGPKHIEKTLTRAKFEELCSDLINRCRIPVENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKK
LLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKDILLLDVTPLSLGVETLGGVMTKIIPRNTTIPTKKSEV
FSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGILSVTAKDKGTGK
EQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEKKEKI
ENLIKKLRQALQNDNYESIKSLLEELQKALMEIGKEVYSSTSTTDPASNDDDVIDTDFSET
>gnl|CDD|214361 CHL00095, clpC, Clp protease ATP binding subunit
MFERFTEKAIKVIMLSQEEARRLGHNFVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVEKIIGRG
TGFVAVEIPFTPRAKRVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDLSKIRSLILN
LIGEIIEAILGAEQSRSKTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPG
VGKTAIAEGLAQRIVNRDVPDILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEV
HTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEIL
FGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSRVRLINSRLPPAARELDKELR
EILKDKDEAIREQDFETAKQLRDREMEVRAQIAAIIQSKKTEEEKRLEVPVVTEEDIAEIVSAWTGIPVN
KLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALA
SYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNL
LLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIETNSGGLGFELSENQLSEKQYKRLSNLVNEELKQ
FFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPL
RRAIMRLLEDPLAEEVLSFKIKPGDIIIVDVNDEKEVKILLINKDNLILNK
>gnl|CDD|214362 CHL00098, tsf, elongation factor Ts
SAELVKELRDKTGAGMMDCKKALQEANGDFEKALESLRQKGLASANKKSTRITTEGLIESYIHTGGKLGV
LVEINCETDFVARREEFQKLAKNIAMQIAACPNVKYVSLEDIPEEIINLEKKIESEKDDLQNKPEEIKEK
IVEGRIKKRLKELSLLDQPFIRDQSITVEELIKQNIAKLGENIQIRRFARFTLGEGEEKL
>gnl|CDD|214363 CHL00099, ilvB, acetohydroxyacid synthase large subunit
MMNQLTLREKTGAFALIDSLVRHGVKHIFGYPGGAILPIYDELYAWEKKGLIKHILVRHEQGAAHAADGY
ARSTGKVGVCFATSGPGATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYV
VRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVGLEKFDYYPPEPGNTIIKILGCRPIYKPTIKRIEQA
AKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTTLMGKGIFDEDHPLCLGMLGMHGTAYANFA
VSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVAIVGDVKKVLQELLELLKNSP
NLLESEQTQAWRERINRWRKEYPLLIPKPSTSLSPQEVINEISQLAPDAYFTTDVGQHQMWAAQFLKCKP
RKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQGMV
RQWQQAFYGERYSHSNMEEGAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIEDENC
YPMVAPGKSNSQMIGILKQSTTPVS
>gnl|CDD|214364 CHL00100, ilvH, acetohydroxyacid synthase small subunit
MKHTLSVLVEDESGVLTRIAGLFARRGFNIESLAVGPAEQKGISRITMVVPGDDRTIEQLTKQLYKLVNI
LKVQDITNIPCVERELMLIKINVNSQTRPEILEIAQIFRAKVVDLSEESLILEVTGDPGKIVAIEQLLEK
FGIIEIARTGKIALIRESKVNTEYLRYISEFTVL
>gnl|CDD|214365 CHL00101, trpG, anthranilate synthase component 2
MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYA
PYIPILGVCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSP
LEITAWTEDGLIMACRHKKYKMLRGIQFHPESLLTTHGQQILRNFLSLSS
>gnl|CDD|214366 CHL00102, rps20, ribosomal protein S20
MANNKSAIKRIKISERNRLRNKAYKSSVKTLIKKYLKNLEDYKTSPNSNNKKKVQETLSSVYSKIDKAVK
KGVFHKNTAARKKSKLAKALKKS
>gnl|CDD|214367 CHL00103, rpl35, ribosomal protein L35
MPKLKTRKAAAKRYKKTGNGKFLRRKAFKSHLLQKKSSKQKRKLSQTVCVSKGDSKSIKLMLPYL
>gnl|CDD|177033 CHL00104, rpl33, ribosomal protein L33
MAKGKDVRVTVILECTSCVRNGVNKESTGISRYITQKNRHNTPNRLELKKFCPYCYKHTIHKEIKK
>gnl|CDD|177034 CHL00105, psaJ, photosystem I subunit IX
MRDLKTYLSTAPVLSTLWFGFLAGLLIEINRFFPDALTFPFF
>gnl|CDD|177035 CHL00106, petL, cytochrome b6/f complex subunit VI
MLTITSYFGFLLAALTITSGLFIGLSKIRLI
>gnl|CDD|177036 CHL00108, psbJ, photosystem II protein J
MADTTGRIPLWLIGTVAGIAVIGLLGIFFYGSYSGLGSSL
>gnl|CDD|177037 CHL00112, rpl28, ribosomal protein L28; Provisional
MSKKCQLTGKKANNGYTVSHSHKRTKKLQKVNLQTKKIWSNTQNRWVKLKISTKAIKTLKKKL
>gnl|CDD|177038 CHL00113, rps4, ribosomal protein S4; Reviewed
MSRYRGPRLKIIRRLGALPGLTSKTPRPGSDLRNQSRSGKKSQYRIRLEEKQKLRFNYGLTERQLLKYVR
IARKAKGSTGQVLLQLLEMRLDNILFRLGMAPTIPAARQLVNHGHILVNGRIVDIPSYRCKPKDIITVKD
KQKSKNLIQNNLESSPREELPNHLTLDKLQYKGLVNQIIDRKWVGLKINELLVVEYYSRQT
>gnl|CDD|100224 CHL00114, psbX, photosystem II protein X; Reviewed
MTPSLSAFINSLLLGAIIVVIPITLALLFVSQKDRTTRN
>gnl|CDD|177039 CHL00115, rpl34, ribosomal protein L34; Reviewed
MTKRTLSGTKRKKVRKSGFRARMATAAGRKILNARRRKGRKKLALR
>gnl|CDD|214368 CHL00117, rpoC2, RNA polymerase beta'' subunit; Reviewed
MAERANLVFHNKVIDKTALKRLISWLIDHFGMAYTSHILDQLKTLGFQQATAAGISLGIDDLLTPPSKGW
LVQDAEQQSLILEKHYHYGNVHAVEKLRQSIEIWYATSEYLKQEMNPNFRMTDPLNPVYMMSFSGARGNA
SQVHQLVGMRGLMSDPQGQIIDLPIQSNFREGLSLTEYIISCYGARKGVVDTAVRTADAGYLTRRLVEVV
QHIVVRETDCGTTRGISVSPRNGMMIERILIQTLIGRVLADDIYIGSRCIATRNQDIGIGLANRFITFRA
QPISIRSPLTCRSTSWICQLCYGWSLAHGDLVELGEAVGIIAGQSIGEPGTQLTLRTFHTGGVFTGGTAE
QVRAPFNGKIKFNEDLVHPTRTRHGHPAFLCKIDLYVTIESEDIIHNVNIPPKSLLLVQNDQYVESEQVI
AEIRAGTSTLNFKEKVRKHIYSDSEGEMHWSTDVYHAPEFTYGNVHLLPKTSHLWILSGGVYRSSLVSFS
LHKDQDQINIHLSVERRYISRLSVINTNNGQVRHKLFSSDGKKEKRILDYSELNRIISNGHCNFIYPAIL
HENSDLLAKRRRNRFLIPFQSIQEREKELMPCGISIEIPINGILRRNSIFAYFDDPRYRTKSSGITKYGT
IEVDSIVKKEDLIEYRGVKEFKPKYQMKVDRFFFIPEEVHILPESSSILVRNNSIIGVDTQITLNIRSKV
GGLVRIEKKKKRIELKIFSGDIHFPGETDKISRHSGILIPPGTGKKNSKESKKIKNWIYVQRITPTKKKY
FVLVRPVVTYEIADGINLATLFPQDLLQEKDNLQLRVVNYILYGNGKPIRGISSIQLVRTCLVLNWDQDK
KSSSIEEARASFVEVRTNGLIRDFLRINLVKSPISYIRKRNDPSSSGLLVQSNNFLDSTNIYSKAEIQSQ
SLSQNQGTIRTLLNRNKESQSLLILSSSDCFRIGPFNGKKSKYHNIKESNPLIPIRNSLGPLGTVLQIAN
FSSSYHLLTHNQILVTKYLQLDNLKQTFQVKVLKYYLIDENGKIYNPDPCSNIILNPFNLNWYFLHHNYC
EETSTIISLGQFICENVCISKNGPHKSGQIIIVQVDSLVIRSAKPYLATPGATVHGHYGEILYEGDTLVT
LIYEKSRSGDITQGLPKVEQLLEARSIDSISMNLEKRLEGWNERITRILGIPWGFLIGAELSIAQSQISL
VNKIQKVYRSQGVQISDKHIEIIVRQMTSKVLVSEDGMSNVFLPGELIGLLRAERINRALEEAICYRPIL
LGITKASLNTQSFISEASFQETTRVLAKAALRGRIDWLKGLKENVILGGLIPAGTGFKGLVHRSKQHKNK
NLEIKKKNLFEGEMRDILFHHRELFDSCISKNFH
>gnl|CDD|214369 CHL00118, atpG, ATP synthase CF0 B' subunit; Validated
MIISILILILAEEGAGGLFDFNATLPLMALQFLLLMVLLNIILYKPLLKVLDERKEYIRKNLTKASEILA
KANELTKQYEQELSKARKEAQLEITQSQKEAKEIVENELKQAQKYIDSLLNEATKQLEAQKEKALKSLEE
QVDTLSDQIEEKLLIK
>gnl|CDD|177042 CHL00119, atpD, ATP synthase CF1 delta subunit; Validated
SNPLVSKIAQPYAEALLEFAKEKNIMEQITADIQLILTFLNESPELKKFLANPLISKNAKKEVIKKTFGS
QINENTLKFLMVLVDRGRIALLDAIIEKYLELVYKLASIKIAEVSTAVPLSSAQEEALIEKLKEMTNAKE
IKLVITVDPSLIGGFLIKIGSKVIDTSIKGQLKQLASHLDTVLE
>gnl|CDD|177043 CHL00120, psaL, photosystem I subunit XI; Validated
MANFIKPYNDDPFVGHLSTPITTSSFTRALLGNLPAYRRGLSPLLRGLEIGMAHGYFLIGPFYKLGPLRN
SDVALLAGFLSAIGLIIILTLCLTIYGVVSFQEEDSSGDDLQTKKGWRQFTSGFLVGAVGGAGFAYLLLS
NIP
>gnl|CDD|214370 CHL00121, rpl27, ribosomal protein L27; Reviewed
MAHKKGAGSTKNGRDSNAKRLGVKRFGGEKVSAGNILIRQRGTKFKPGLNVGCGKDFTLYALIDGFVKFK
KKNKKQKSINVINIVI
>gnl|CDD|214371 CHL00122, secA, preprotein translocase subunit SecA; Validated
MFNNLFNNKSKLNKYQTLVNQINLLEEELKNLTDTELRSKTNKLKKRLSNGQNLNKIIPESFALTREASF
RTLGLRHFDVQLIGGLVLNDGKIAEMKTGEGKTLVATLPAYLNALTGKGVHIVTVNDYLAKRDQEWMGQI
YRFLGLTVGLIQEGMSSEERKKNYLKDITYVTNSELGFDYLRDNMALSLSDVVQRPFNYCIIDEVDSILI
DEARTPLIISGQSKTNIDKYIVADELAKYLEKNVHYEVDEKNKNVILTEQGILFIEKILKIEDLYSANDP
WIPYILNALKAKELFFKNVHYIVRNNEIIIVDEFTGRIMPGRRWSDGLHQAIEAKENLPIRQETETLASI
TYQNFFLLYPKLSGMTGTAKTEELEFEKIYNLEVVCIPTHRPMLRKDLPDLIYKDELSKWRAIADECLQM
HQTGRPILIGTTTIEKSELLSQLLKEYRLPHQLLNAKPENVRRESEIVAQAGRKGSITIATNMAGRGTDI
ILGGNPEFKLKKELYDLLLSYKSNEKISTISQNFLNILNSLKNDLKFLSLSDFENLKILNEASEISIPKN
SYQLSLRFLYNELLEKYKKLQEKEKKIVKKLGGLYVIGTERHESRRIDNQLRGRAGRQGDPGSSRFFLSL
EDNLLRIFGGDKIQNLMQTLNLDDEPLESKLLSKSLDSAQKKVEEYYYDQRKQLFEYDQVLNKQRKAIYS
ERRKILESQSLRDWILAYGEQVIDDIITFLKSRKNPNNKFINLINKFKELLKLPLCFNKSDLNTLNSGEL
KKFLYQQFWISYDLKELYLEQIGTGLMRELERSLLLQQIDKSWKEHLQKMSLLREAIGWRSYGQKDPLIE
YKNEAFNLFINMINHIRHLVIYDLFRSSIL
>gnl|CDD|177046 CHL00123, rps6, ribosomal protein S6; Validated
MMSKLNKYETMYLLKPDLNEEELLKWIENYKKLLRKRGAKNISVQNRGKRKLSYKINKYEDGIYIQMNYS
GNGKLVNSLEKALKLDENVLRYLTFKK
>gnl|CDD|177047 CHL00124, acpP, acyl carrier protein; Validated
MTKNDIFEKVQSIVAEQLGIEKSEVTLDANFTRDLGADSLDVVELVMAIEEKFDIEIPDEDAEKISTLQE
AVDFISQKINKK
>gnl|CDD|177048 CHL00125, psaE, photosystem I subunit IV; Reviewed
MVKRGSKVRILRKESYWYNEIGTVATVDQSGIRYPVLVRFEKVNYSGTNTNNFSLDELVEVEEE
>gnl|CDD|177049 CHL00127, rpl11, ribosomal protein L11; Validated
MAKKKLAIIKLALPAGKATPAPPVGPALGQHGVNINLFCKEYNARTKDKIGLIIPVEISVYEDKSYTFIL
KTPPASVLLAKAAGIKKGSGEPNKKKVGSITIKQLEEIAQIKLPDLNTISLSKAIKIIEGTAKNMGISIK
>gnl|CDD|177050 CHL00128, psbW, photosystem II protein W; Reviewed
MAKIQFIKGIDEEVIPDVRLTRSRDGSTGTATFRFKNPNILDKSTAKQGEITGMYLIDEEGELSTRDVNA
KFINGKPQAIEAIYIMKNPEAWDRFMRFMERYAEDNGLTFTKA
>gnl|CDD|177051 CHL00129, rpl1, ribosomal protein L1; Reviewed
MKKLSRRTKELRSKIEKKLYSPEEAINLLKETATAKFIETAEAHISLNIDPKYADQQLRTTVTLPKGTGK
TIRIAVLTNEEKITEAKNAGADIVGSDDLIEEITKGNLDFDLLIATPDMMPKLAKLGRVLGPRGLMPSPK
SGTVTTDLASAINEFKKGKLEYRADKTGIVHVLFGKSNFTEEDLLENLQAIYESIEQNRPSGVKGKYWKS
FYICSTMGPSIQIDISLLR
>gnl|CDD|177052 CHL00130, rbcS, ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit; Reviewed
MRLTQGTFSFLPDLTDQQIEKQIQYAISKGWALNVEWTDDPHPRNSYWELWGLPLFDVKDPAAVMFEINE
CRKQKPNGYIKVNAFDASRGVESCVLSFIVNRPANEPGFYLERTEGEGRFIRYTIHSYATAKPEGSRY
>gnl|CDD|214372 CHL00131, ycf16, sulfate ABC transporter protein; Validated
MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKG
ESILDLEPEERAHLGIFLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMD
PSFLSRNVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHY
QRLLDYIKPDYVHVMQNGKIIKTGDAELAKELEKKGYDWLKQ
>gnl|CDD|177054 CHL00132, psaF, photosystem I subunit III; Validated
MKKFNLLFLLLAALLLFNPIAAFADVAGLTPCSESPAFQKRLNNSVKKLENRLAKYEANSPPALALQQQI
DKTKARFDKYGRSGLLCGTDGLPHLITDGRWSHAGEFTIPGLLFLYITGWIGWVGRKYLRAVSTTKNPTE
KEIIIDVPLALKIMSSGFIWPLSAWQEFTSGQLLAPNDEITVSPR
>gnl|CDD|177055 CHL00133, psbV, photosystem II cytochrome c550; Validated
MLKKFSSLFLLVFLLIFSIFVSSALAIELDEATRTVVLDSSGKTVVLTPEQVKRGKRLFNASCGACHVGG
ITKTNPNVGLDPEALSLATPPRDNIEALVDYMKNPTTYDGLESIAEIHPSIKSADIFPKMRSLTDEDLYA
IAGHILLQPKIVSEKWGGGKIYY
>gnl|CDD|177056 CHL00134, petF, ferredoxin; Validated
MATYKVTLLSEEEGIDVTIDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDD
QLEAGFVLTCVAYPTSDCTILTHQEEELY
>gnl|CDD|177057 CHL00135, rps10, ribosomal protein S10; Validated
MEIMTNAKIRIKLKSFNHELLNSSCKKIIDTASRTNATAVGPIPLPTKRRIYCVLRSPHVDKDSREHFEI
RTHKRIIDIYYPSSETIDSLMKLDLPPGVDI
>gnl|CDD|177058 CHL00136, rpl31, ribosomal protein L31; Validated
MPKKNIHPQWFPETKVYCDGQLVMTVGSTKPELNVDIWSGNHPFYTGSQKIIDTEGRVERFMKKYGLN
>gnl|CDD|177059 CHL00137, rps13, ribosomal protein S13; Validated
MVRIAGVDLPRNKRIEYALTYIYGIGLTSAKEILEKANIDPDIRTKDLTDEQISALREIIEENYQVEGDL
RRFESLNIKRLMEINCYRGRRHRLGLPVRGQRTRTNARTRRGAKKTVAGKKK
>gnl|CDD|177060 CHL00138, rps5, ribosomal protein S5; Validated
MLFLLKKMYNKKKNRKSNIKENKWEERVIQIKRVSKVVKGGKKLSFRAIVVIGNENGWVGVGVGKADDVQ
NAVKKAVTDAKKNLITIPLTKSNSIPHNITGIFGAAKVILRPSAPGSGVIAGGSVRIVLELAGIKNILAK
QLG
>gnl|CDD|214373 CHL00139, rpl18, ribosomal protein L18; Validated
KRERVRKKIKGTAERPRLSVFRSNKHIYAQIIDDTNGKTLVACSTLEPDVKSSLSSTSTCDASKLVGQKL
AKKSLKKGITKVVFDRGGKLYHGRIKALAEAAREAGLQF
>gnl|CDD|177062 CHL00140, rpl6, ribosomal protein L6; Validated
MSRIGKLPIKIPDNVNVSIDDQIIKVKGPKGTLSRKIPDLITIEIQDNSLFVSKKDESKKARALHGLYRT
LINNMVIGVSEGFEKKLELQGVGYRAQVQGKDLILNLGYSHPVKIKIPPGISVEVENNTNITIKGIDKEL
VGQFAAKIRSVRPPEPYKGKGIRYKGEVIRRKAGKAGK
>gnl|CDD|214374 CHL00141, rpl24, ribosomal protein L24; Validated
MKKKKKMHVKIGDTVKIISGSDKGKIGEVLKIIKKSNKVIVKGINIKFKHIKPNKENEVGEIKQFEAPIH
SSNVMLYNEESNI
>gnl|CDD|177064 CHL00142, rps17, ribosomal protein S17; Validated
MPVKEKIGIVVSNKMNKTIVVAVENRYKHPIYGKIITKTKKYLVHDEENECNIGDQVLIEETRPLSKTKR
WILKEILSKSSLSN
>gnl|CDD|177065 CHL00143, rpl3, ribosomal protein L3; Validated
MSIGLLGTKIGMTQIFDETGNAIPVTILKVGPCVITQIKTLTTDGYNAIQIGYKQVSTKKLTKPQLGHLQ
KSNVPPLKYLKEFRVKSSEEFEVGQPLTVDAFSVGQLVNVSGKSIGKGFAGLQKRHNFSRGPMTHGSKNH
RAPGSIGAGTTPGRVYPGKKMAGRLGNKKVTIKNLKILKVDSENNLLVLKGSVPGKPGNLLSISPSK
>gnl|CDD|177066 CHL00144, odpB, pyruvate dehydrogenase E1 component beta subunit; Validated
MSEVFLFEALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGA
AMTGLRPIVEGMNMGFLLLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSV
PGLQIVACSTPYNAKGLLKSAIRSNNPVIFFEHVLLYNLKEEIPDNEYLLPLEKAEVVRPGNDITILTYS
RMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEHL
FDELDAPIVRLSSQDVPTPYNGPLEEATVIQPAQIIEAVEQIITNKK
>gnl|CDD|177067 CHL00145, psaD, photosystem I subunit II; Validated
MTLNLQMPSPTFGGSTGGWLRAAEVEEKYAITWTSPKEQIFEMPTGGAAIMRNGENLLYLARKEQCLALG
TQLRTKFKINDYKIYRIFPNGEVQYLHPKDGVFPEKVNPGRVAVGSRDFSIGKNPNPASVKFTGKATYD
>gnl|CDD|214375 CHL00147, rpl4, ribosomal protein L4; Validated
MTIQKFLNYPVIDLTGKEKSETIKLKLNVLEKSGNYLLHRALVRQNNNQRQGTASTKTRSEVRGGGRKPW
KQKGTGRARAGSNRSPLWKGGGVIFGPKPKTYSNKLNKKERRLALRTLLYNKSNNITVVENFESSITNPK
TKAFINLLKKLNINLDQKILIIVPEKTENLYLSTRNLKNVELISADTLNIKSLLKAKQIIITKEALKIIE
EVYND
>gnl|CDD|214376 CHL00148, orf27, Ycf27; Reviewed
TMENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQ
EIRKESDVPIIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRRTNKKSFSSKIPNSSIIR
IGFLKIDLNKKQVYKNNERIRLTGMEFSLLELLISKSGEIFSRATILKEVWGYTPERHIDTRVVDVHISR
LRAKLEDDPSNPDLILTARGTGYLFQSIIE
>gnl|CDD|177069 CHL00149, odpA, pyruvate dehydrogenase E1 component alpha subunit; Reviewed
YPKKVNLPLTNSNENNINSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLA
ETDYVCSTYRDHVHALSKGVPPKNVMAELFGKETGCSRGRGGSMHIFSAPHNFLGGFAFIGEGIPIALGA
AFQSIYRQQVLKEVQPLRVTACFFGDGTTNNGQFFECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIP
EIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIEALTYRFRGHSLADPDELRSKQEKEA
WVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISDLKKYLFAD
>gnl|CDD|164542 CHL00151, preA, prenyl transferase; Reviewed
MATNSNLLTPIEEELLILEDNLKKLIGSGHPILYAAAKHLFSAGGKRIRPAIVLLVAKATGGNMEIKTSQ
QRLAEITEIIHTASLVHDDVIDECSIRRGIPTVHKIFGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLIS
KVITDFAEGEIRQGLVQFDTTLSILNYIEKSFYKTASLIAASCKAAALLSDADEKDHNDFYLYGKHLGLA
FQIIDDVLDITSSTESLGKPIGSDLKNGNLTAPVLFALTQNSKLAKLIEREFCETKDISQALQIIKETNG
IEKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEIANFIINRLN
>gnl|CDD|214377 CHL00152, rpl32, ribosomal protein L32; Validated
MAVPKKRTSKSKKRIRKNIWKRKAYKAALKAFSLAKSLSTGKSKSFFYQQTNK
>gnl|CDD|177071 CHL00154, rpl29, ribosomal protein L29; Validated
MSLPKITDIIDLTDSEISEEIIKTKKELFDLRLKKATRQNFKPHLFKHKKHRLAQLLTLLSSRLKSL
>gnl|CDD|177072 CHL00159, rpl13, ribosomal protein L13; Validated
MNKTFIPSKDYKNRKWYIIDAKDQTLGRLATKIASLLRGKNKPSYHPSVDTGDYVIVINAEKIKVTGNKT
SQKFYVRHSGRPGGLKIETFEELQNRLPNRIIEKAVKGMLPKGPLGRKLFTKLKVYKGESHPHVAQKPIK
INI
>gnl|CDD|214378 CHL00160, rpl9, ribosomal protein L9; Provisional
MSKKKIQVILKENIQKLGKSGTVIKVKSGYARNYLIPNKMAKVATQGSLKQQKMYQKILDLKLKEAKEKC
LKVKQLLEEIQKFSVKKKVGENNQIFGSVTEKEISQIIKNKTNIDLEKQNIELPEIKTIGIYNIEIKLTS
DVKANINLQILPE
>gnl|CDD|214379 CHL00161, secY, preprotein translocase subunit SecY; Validated
KLQSKKKDELLNRLLFTLGLLLLIRLGTFIPVPGIDHTQLYPSLSNNPLLNLLNTFSGGGFFVIGLFALG
ILPYINASIIIQLLTSIIPSLEKLQKEEGEAGRRKINQYTRYLTLGWAIIQSIGISFWLKPYLFNWNLLL
ALEIVLALTSGSMIVLWLSELITEKGLGNGSSLLIFFNIVSNLPKLLQSLLFSLSANITILSILLLLFLF
FITLIGIIFLQEAIRKIPLISAKQLGKSSRLASNSYLPLRLNQAGVMPIIFASALLVLPGYLTNILLNQF
LLPLLSLFLQLASFKILYLVLYFVLILFFSYFYSTIVLNPKDISENLQKMAVSIPGIRPGKATTKYLKKT
LNRLTLLGALFLAFIALLPNLIESVLNLSVFKGLGTTSLLILVGVAIDTSRQIQTYLISNNYENMYD
>gnl|CDD|214380 CHL00162, thiG, thiamin biosynthesis protein G; Validated
MNNMTDKLKIGNKSFNSRLMLGTGKYKSLKDAIQSIEASGCEIVTVAIRRLNNNLLNDNSNLLNGLDWNK
LWLLPNTAGCQTAEEAIRMAFLGRELAKQLGQEDNNFVKLEVISDPKYLLPDPIGTLKAAEFLVKKGFTV
LPYINADPMLAKHLEDIGCATVMPLGSPIGSGQGLQNLLNLQIIIENAKIPVIIDAGIGTPSEASQAMEL
GASGVLLNTAVAQAKNPEQMAKAMKLAVQAGRLAYLAGRMPKKKYAQASSPIEGISK
>gnl|CDD|214381 CHL00163, ycf65, putative ribosomal protein 3; Validated
MQKFTLKVLWLENNIGIAVDQIVGNGTSPLTSYFFWPRTDAWELLKLELESKPWISEDERIEILNKTTEI
INYWQENKKKYSLSEAQSKFPDFIFVGKF
>gnl|CDD|164550 CHL00164, psaK, photosystem I subunit X; Validated
MNALLLLSLVPQTSPWSASTAIIMILCNLLCIVAGRYAIQVRGLGPSIPISGLKGFGLPELLATTSLGHI
IGAGSILGLSYVGLIS
>gnl|CDD|214382 CHL00165, ftrB, ferredoxin thioreductase subunit beta; Validated
MKLNNEKSKPESLEAMRKFAETYAKRTNTFFCSDLSITAVVIEGLARHKDEYGAPLCPCRHYEDKKVEVS
AAYWNCPCVPMRERKECHCMLFLTPDNEFASQSQTISKKTLLQNII
>gnl|CDD|214383 CHL00168, pbsA, heme oxygenase; Provisional
MVTNLATQLREGTTKSHSMAENVSFVKSFLGGVIDKKSYRKLVANLYFVYSAIEEEIEKNKEHPLIKPIY
FQELNRKESLEKDLNYYYGDDWKSIIEPSPATKIYVDRIHKISAKKPELLIAHAYTRYLGDLSGGQILKK
IAQRAMNLSDSGGLAFYDFDNIEDDQEFKQIYKAALDNLPLSDDQIQNIIAEANIAFNLNMKMFQELNSS
FIKIITMLIKNTILSFLGKLKVMLAFND
>gnl|CDD|100270 CHL00170, cpcA, phycocyanin alpha subunit; Reviewed
MKTPITEAIASADSQGRFLSNGELQACNGRFQRAAASLEAARSLTSNAQRLIDGAAQAVYTKFPYTTQMP
GPTYASSAIGKAKCARDIGYYLRMVTYCLVAGGTGPMDEYLVAGLEEINRSFDLSPSWYVEALKYIKASH
GLSGQAANEANAYLDYAINALS
>gnl|CDD|100271 CHL00171, cpcB, phycocyanin beta subunit; Reviewed
MLDAFAKVVAQADARGEFLSNTQLDALSKMVAEGNKRLDAVNKINANASTIVTNAARSLFAEQPQLIQPG
GNAYTNRRMAACLRDMEIVLRYVSYAMIAGDSSVLDDRCLNGLRETYQALGVPGSSVAVAVQKMKEAAVS
LANDSSGVTVGDCSALISELASYFDRAAVAVV
>gnl|CDD|133617 CHL00172, cpeB, phycoerythrin beta subunit; Provisional
MLDAFSRVVTNSDAKAAYVGGSDLQALKKFISEGNKRLDSVNSIVSNASCIVSDAVSGMICENPGLISPG
GNCYTNRRMAACLRDGEIILRYVSYALLAGDPSVLEDRCLNGLKETYIALGVPANSSARAVSIMKASAVA
FINNTASQRKMSTAQGDCSALASEVASYFDRVTAAIS
>gnl|CDD|100273 CHL00173, cpeA, phycoerythrin alpha subunit; Provisional
MKSVITTTISAADAAGRFPSSSDLESVQGNIQRAAARLEAAEKLASNHEAVVKEAGDACFAKYSYLKNPG
EAGDSQEKVNKCYRDVDHYMRLVNYCLVVGGTGPVDEWGIAGAREVYRTLNLPTSAYVASFAFARDRLCV
PRDMSAQAGVEYAGNLDYIINSLC
>gnl|CDD|214384 CHL00174, accD, acetyl-CoA carboxylase beta subunit; Reviewed
DKRDIRNLISNQIFEIDNDSYMYDTKYSWNTQKYKHLWVQCENCYGLNYKKFLKSKMNICEQCGYHLKMS
SSDRIELLIDPGTWNPMDEDMVSLDPIEFHSDEEPYKDRIDSYQKKTGLTDAVQTGIGQLNGIPVALGVM
DFQFMGGSMGSVVGEKITRLIEYATNESLPLIIVCASGGARMQEGSLSLMQMAKISSALYDYQSNKKLFY
ISILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKRVIEQTLNKTVPEGSQAAEYLFDKGLFDLIVPRN
LLKGVLSELFQLHGFF
>gnl|CDD|214385 CHL00175, minD, septum-site determining protein; Validated
EQITTEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVL
YTAMDVLEGECRLDQALIRDKRWKNLSLLAISKNRQRYNVTRKNMNMLVDSLKNRGYDYILIDCPAGIDV
GFINAIAPAQEAIVVTTPEITAIRDADRVAGLLEANGIYNVKLLVNRVRPDMIQANDMMSVRDVQEMLGI
PLLGAIPEDENVIISTNRGEPLVLNKKLTLSGIAFENAARRLVGKQDYFIDLDSPSKGPLKRLQKFFLGS
S
>gnl|CDD|214386 CHL00176, ftsH, cell division protein; Validated
MKEQSKYAILISLPLIVEKFTVWDVFYYSSVEDGLKSPNNPDVVQNKASSRMTYGRFLEYLDMGWIKKVD
LYDNGRTAIVEASSPELGNRPQRIRVELPVGASELIQKLKEANIDFDAHPPVLKSNIVTILSNLLLPLIL
IGVLWFFFQRSSNFKGGPGQNLMNFGKSKARFQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTA
VGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVF
IDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITV
SLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAI
DRVIAGLEGTPLEDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRS
QILARIVGALGGRAAEEVVFGSTEVTTGASNDLQQVTNLARQMVTRFGMSSIGPISLESNNSTDPFLGRF
MQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYTILP
PKKTWKAW
>gnl|CDD|214387 CHL00177, ccs1, c-type cytochrome biogenensis protein; Validated
KNMKQKLLKLLANLKFAIILLLLIAIFSVIGTIIEQDQSIEFYKNNYPLSNPIFGFLSWKIILKLGLDHI
YKTWWFLSLLLLFGLSLLLCTLLQQLPSLKIARRWQFYTNKNQFKKLQISTNLKKFSLSKLAYKLKSKNY
SIFQQGNKIYAYKGLIGRIAPIIVHFSMILILIGSILGALSGFTAQEIIPKTEIFHIQNIISSGQLSKIP
QESARVNDFWITYTPEKSIKQFYSDLSILNSEGKEIKRKTISVNHPLKYKGLTIYQTDWNIIGLRIKIGN
SKIIQIPLIKIENNNNKIWLTWIPLNKQNQSGLTLVIKDLQGKISLYDNNGNFLGILELNEPINLNNTPI
TLIEIISSTGLQIKSDPGIPIIYVGFFLLMISILISYISYSQIWLIQKNNKLYIGGKTNRAKFKFELEFL
KIIKQF
>gnl|CDD|177082 CHL00180, rbcR, LysR transcriptional regulator; Provisional
TDLPFTLDQLRILKAIATEGSFKKAAESLYISQPAVSLQIKNLEKQLNIPLFDRSKNKASLTEAGELLLR
YGNRILALCEETCRALEDLKNLQRGTLIIGASQTTGTYLMPRLIGLFRQRYPQINVQLQVHSTRRIAWNV
ANGQIDIAIVGGEVPTELKKILEITPYVEDELALIIPKSHPFAKLKKIQKEDLYRLNFITLDSNSTIRKV
IDNILIQNGIDSKRFKIEMELNSIEAIKNAVQSGLGAAFVSVSAIEKELELGLLHWIKIENITIKRMLSI
ITNPNRYKSKASETFYNEILTLFNT
>gnl|CDD|177083 CHL00181, cbbX, CbbX; Provisional
TLVNLQEEYEKTQIQEVLDILDEELVGLAPVKTRIREIAALLLIDRLRKNLGLTSSNPGLHMSFTGSPGT
GKTTVALKMADILYKLGYIKKGHLLTVTRDDLVGQYIGHTAPKTKEVLKKAMGGVLFIDEAYYLYKPDNE
RDYGSEAIEILLQVMENQRDDLVVIFAGYKDRMDKFYESNPGLSSRIANHVDFPDYTPEELLQIAKIMLE
EQQYQLTPEAEKALLDYIKKRMEQPLFANARSVRNALDRARMRQANRIFESGGRVLTKADLVTIEAEDIL
KSRLFNL
>gnl|CDD|177084 CHL00182, tatC, Sec-independent translocase component C; Provisional
FNTPITNWNFNFLDIEDPDLEMPLSEHLEELRQRLFLSLSILLLLTIVCFINVKSIVEILQAPAKGIKFL
QLSPGEYFFSSIKISFYTGLLISSPFIIYQIILFILPGLTKKERKIILPLLISSLVLFGLGLIFAYFVLV
PAALNFFINYGSDVVEPLWSFDQYFDFILVLFFSTGLAFQIPIIQIVLGLLNIISSKQMLSAWRYVILVS
TIVGAILTPSTDPLTQLLLSLAILLLYFSGVIVLKLLKK
>gnl|CDD|177085 CHL00183, petJ, cytochrome c553; Provisional
KNLIIGFLISCFALISFSQPAFAADLDNGEQIFSANCAACHAGGNNVIMPEKTLKKDALEANSMNSIEAI
TYQVTNGKNAMPAFGGRLSDEDIEDVANYVLSQAEKGW
>gnl|CDD|177086 CHL00184, ycf12, Ycf12; Provisional
MNLEVIAQLTSLALIVLAGPLVIVLLALRKGNL
>gnl|CDD|177087 CHL00185, ycf59, magnesium-protoporphyrin IX monomethyl ester cyclase; Provisional
MQTSINKLQTKTPAKETLLTPRFYTTDFDEMANYDISSNIEEIEAILEEFRADYNQQHFIRDNEFNQSWS
NLDEKTKSLFVEFLERSCTAEFSGFLLYKELSRKLKDKNPLLAEGFLLMSRDEARHAGFLNKAMSDFNLS
LDLGFLTKSRKYTFFSPKFIFYATYLSEKIGYWRYITIYRHLEKNPEYRIYPIFKFFESWCQDENRHGDF
FAALLKSQPHLLNGWKARLWCRFFLLSVFATMYLNDLQRSDFYAAIGLDARQFDMHVIRKTNESAARLFP
VVLDVDNPKFFKYLDQCACANLKLIEIDQKESSWIWKKFIKIPLYCNLILNLIKLYLLKPIDSKAVWNTI
R
>gnl|CDD|177088 CHL00186, psaI, photosystem I subunit VIII; Validated
MTASNLPSILVPLVGLVFPAIAMASLFLYIQKDKIV
>gnl|CDD|214388 CHL00187, cysT, sulfate transport protein; Provisional
IGDFNFSLKFSSIYIISLSYIIFLLVLPILALLIKASQQPWSDFLQKATEPIALSAYSLTLSMALIAALI
NGFFGLLIAWVLVRYNFPGKRLLDAAVDLPFALPTSVAGLTLATVYGDNGWIGHLLSHLGIQIVFTKLGV
LLAMIFVSFPFVVRTIQPVLQEIEKELEEAAWSLGASPWQTFWKVIFPPLIPALLTGLALTFSRAIGEYG
SIVIISSNIPFKDLVASVLIFQSLEQY
>gnl|CDD|214389 CHL00188, hisH, imidazole glycerol phosphate synthase subunit hisH; Provisional
MMKIGIIDYSMGNLHSVSRAIQQAGQQPCIINSESELAQVHALVLPGVGSFDLAMKKLEKKGLITPIKKW
IAEGNPFIGICLGLHLLFETSEEGKEEGLGIYKGQVKRLKHSPVKVIPHMGWNRLECQNSECQNSEWVNW
KAWPLNPWAYFVHSYGVMPKSQACATTTTFYGKQQMVAAIEYDNIFAMQFHPEKSGEFGLWLLREFMKKA
>gnl|CDD|177089 CHL00189, infB, translation initiation factor 2; Provisional
QNYENNISISSENTIDLKNPLFIKNLKHSSYKIRLESDIKDSLLNLDINKKLHEKLDKKNKKFNKTDDLK
DSKKTKLKQKKKIKKKLHIDDDYDNFFDSKNNSKQFAGPLAISLMRKPKPKTEKLKKKITVNKSTNKKKK
KVLSSKDELIKYDNNKPKSISIHSPLTIQELSTLLCIPETEIIKSLFLKGISVTVNQIIDISIISQVADD
FGINIISEEKNNINEKTSNLDNTSAFTENSINRPPIVTILGHVDHGKTTLLDKIRKTQIAQKEAGGITQK
IGAYEVEFEYKDENQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPI
IVAINKIDKANANTERIKQQLAKYNLIPEKWGGDTPMIPISASQGTNIDKLLETILLLAEIEDLKADPTQ
LAQGIILEAHLDKTKGPVATILVQNGTLHIGDIIVIGTSYAKIRGMINSLGNKINLATPSSVVEIWGLSS
VPATGEHFQVFNSEKEAKLKIIKNKENNKKDTTKRITLSTTKTINKKDNKKQINLIIKTDTQGSIEAIIN
SISQIPQKKVQLNILYASLGEVTETDVEFASTTNAEILAFNTNLAPGAKKAARKLNIIIKEYQVIYDLLE
YIEALMEDLLDPEYKKVPIGEAEVKTVFPLAKRFVAGCRVTEGKITKNALIKVIRENKLIYEGKITSLKR
VKEDVEEAQEGNECGIFIEEFQLWQSGDKIHAFELIPKKKSL
>gnl|CDD|177090 CHL00190, psaM, photosystem I subunit XII; Provisional
MISDSQIFIALFLALTTGILAIRLGTALYQ
>gnl|CDD|214390 CHL00191, ycf61, DNA-directed RNA polymerase subunit omega; Provisional
MMNKYNSYDSNEILYKTEELLNAASNRYKITIQVANRAKRRRYEDIDIINDPSIKPIIRAILEMVDEINQ
PEIISD
>gnl|CDD|214391 CHL00192, syfB, phenylalanyl-tRNA synthetase beta chain; Provisional
MKISLKWLKELINLENIDLDTLINKLTLAGFEVEDILSVKIGGESDIILDISSTANRSDVLSIQGLSREI
SALFNSDPIKLKYYNPSISWFDKLKNLISNDSSKLNCSMFIAVIIENIEIKDSPKWLQNRLSSSGFKSLN
NLTDIQNYIMLETGQPIEIYDLDKIYSKNTTSSLALSSKFALQKSSFIASNSKNIELENNILVVQANNVI
ISIAGIISNEEIICDKNTKSILIEASIFDAAVIRKSSRKLGLRTDRSIRYEKSLKNDNLLEAYYRLVSLL
RILNPKLKCKFHFIYKKIKNSSRRIKLSYKKIKDILGPIKINTNTRYLSPKEITNALKRLNFKITYDSLK
LNWEVLIPSYRKDDIVREIDVIEEIARIYGFNNFLSKLPNIKFIGRLDIDYNTRDKIRSYLRNLGLTELI
HYSLVKQESFSKNEIKLKNPLIKDYSTLRSSLLPGLIEAVQENLKQGNSTLEGFEIGHVFNLDSSSIIEE
TELAGGIFGGIDIRSSWSEKAQSLNWFEAKGIIENFFQKLNLPIYWKKYSDLDEKINFHPYCTSEIFLSN
GQKIGIFGQLHPLLANKLNLNTEIYLFEINLDILQYSIQQNNLISYQPYSSYPKIIRDLSFIIKKSISIS
KIKELIYQNGDNLLESITLFDYYKGKSIPNGHTSLGLRLTFQSENKTLTNEEIDRIQQNLQKVLEKKLNA
EIRE
>gnl|CDD|177092 CHL00193, ycf35, Ycf35; Provisional
MSHFTKIKTSIQNLNLLKKALNDLNIEWKKENQVIKGYNGQTHNADLVIKQSNNYDIGFVWNGQEYELVA
DLSFWQQPWSVENFLDKLNQQYAYNSIIKESKKIGFEPIEYVNNKDGSIKLVLQRWNY
>gnl|CDD|177093 CHL00194, ycf39, Ycf39; Provisional
MSLLVIGATGTLGRQIVRQALDEGYQVRCLVRNLRKASFLKEWGAELVYGDLSLPETLPPSFKGVTAIID
ASTSRPSDLYNAKQIDWDGKLALIEAAKAAKIKRFIFFSILNAEQYPYIPLMKLKSDIEQKLKKSGIPYT
IFRLAGFFQGLISQYAIPILEKQPIWITNESTPISYIDTQDAAKFCLKSLSLPETKNKTFPLVGPKSWNS
SEIISLCEQLSGQKAKISRVPLFLLKLLRQITGFFEWTWNISDRLAFVEILNTSNNFSSSMAELYKIFKI
DPNELISLEDYFQEYFERILKRLKDINYEQVQKQKDL
>gnl|CDD|177094 CHL00195, ycf46, Ycf46; Provisional
MKFTDELKLLLKARYPIIYINTIEEDRLEYIIRKSIKLNLNRSIYSWDFVDGYTNNPNDNGFAKRNPLQA
LEFIEKLTPETPALFLLKDFNRFLNDISISRKLRNLSRILKTQPKTIIIIASELNIPKELKDLITVLEFP
LPTESEIKKELTRLIKSLNIKIDSELLENLTRACQGLSLERIRRVLSKIIATYKTIDENSIPLILEEKKQ
IISQTEILEFYSVNEKISDIGGLDNLKDWLKKRSTSFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIA
NDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGDSGTTNRVLATF
ITWLSEKKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSWKKYDIKK
LSKLSNKFSGAEIEQSIIEAMYIAFYEKREFTTDDILLALKQFIPLAQTEKEQIEALQNWASSGRIRLA
>gnl|CDD|177095 CHL00196, psbY, photosystem II protein Y; Provisional
MDTRLLVIAAPVLAAASWALFNIGRLAIQQIQRLSR
>gnl|CDD|214392 CHL00197, carA, carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
MKKMIPAILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLE
DIESVKIQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLN
LSYLRAKIKESPHMPSSDLIPRVTTSSYYEWDEKSHPSFYLADNKRPHSSYQLKIIVIDFGVKYNILRRL
KSFGCSITVVPATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKYNIPIFGICMGHQILSLAL
EAKTFKLKFGHRGLNHPSGLNQQVEITSQNHGFAVNLESLAKNKFYITHFNLNDGTVAGISHSPKPYFSV
QYHPEASPGPHDADYLFEYFIEIIKHSKSSKN
>gnl|CDD|214393 CHL00198, accA, acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
MSNRKPHVPDFMKPLAELESQVEELSKLAPKNDKVINNKLKSFQRKLRILKKEIFYSLTPLQRLHLVRQS
ERPTTLDYIPYILDEWIELHGDRGGSDDPALVGGIGKINGRTIVFLGHQRGRNTKENVLRNFGMPSPGGY
RKALRLMKHANKFGLPILTFIDTPGAWAGVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALG
IGIGDSIMMLEYAVYTVATPEACAAILWKDSKKSLDAAEALKITSEDLKVLGIIDEIIPEPIGGAQADPA
SASKILKKKLIRQLDFLKILSPSELKAHRYEKFRKLGAFYEI
>gnl|CDD|164575 CHL00199, infC, translation initiation factor 3; Provisional
MLEKYKNSKKLSRDLPLINERIRFPKVRVIDDSGEQLGIFTSEQAIQLAANQGLDLVLVSEKSDPPVCRI
IDYGKYKFTQEKRAKEAKKKQHNSSIKEVKMRYKIEEHDYKVRINQAFKFLQAGDKVKATLTFRGREIQH
LNLAINLLNKMAADLSSIAEIQQPPSQDGRNMIMILSPKKVD
>gnl|CDD|214394 CHL00200, trpA, tryptophan synthase alpha subunit; Provisional
MNTISNVFEKLDKQCALIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRAL
KQGINLNKILSILSEVNGEIKAPIVIFTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVC
NLYNIELILLIAPTSSKSRIQKIARAAPGCIYLVSTTGVTGLKTELDKKLKKLIETIKKMTNKPIILGFG
ISTSEQIKQIKGWNINGIVIGSACVQILLGSSPEKGLDQLSEFCKVAKKSIIS
>gnl|CDD|164576 CHL00201, syh, histidine-tRNA synthetase; Provisional
MAKIQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFT
DRSNRDITLRPEGTAGIVRAFIENKMDYHSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARA
DTEVIHLAMQIFNELQVKNLILDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSK
NLKTQEILDGAPKISDFLSLESTEHFYDVCTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDT
ICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAKDNIILPKQSIDVYIATQGLKAQKKGWEIIQFLEK
QNIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEISYLKKK
IAFNKKFNSY
>gnl|CDD|133644 CHL00202, argB, acetylglutamate kinase; Provisional
MLNNDERVQVLSEALPYIQKFRGRIMVIKYGGAAMKNLILKADIIKDILFLSCIGLKIVVVHGGGPEINF
WLKQLNISPKFWNGIRVTDKVTMEIVEMVLAGKVNKDLVGSINANGGKAVGLCGKDANLIVARASDKKDL
GLVGEIQQVDPQLIDMLLEKNYIPVIASVAADHDGQTYNINADVVAGEIAAKLNAEKLILLTDTPGILAD
INDPNSLISTLNIKEARNLASTGIISGGMIPKVNCCIRALAQGVEAAHIIDGKEKHALLLEILTEKGIGS
MLVV
>gnl|CDD|164577 CHL00203, fabH, 3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
MGVHILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDP
LEIDLIILATSTPDDLFGSASQLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADT
LSKWIDWSDRKTCILFGDGAGAAIIGASYENSILGFKLCTDGKLNSHLQLMNKPVNNQSFGTTKLPQGQY
QSISMNGKEVYKFAVFQVPAVIIKCLNALNISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKY
GNTSAASIPLALDEAIQNNKIQPGQIIVLSGFGAGLTWGAIVLKWK
>gnl|CDD|214395 CHL00204, ycf1, Ycf1; Provisional
LGNLVSLCMKIINSVVVVGLYYGFLTTFSIGPSYLFLLRARVMEEGEEGTEKKVSATTGFITGQLMMFIS
IYYAPLHLALGRPHTITVLALPYLLFHFFWNNHKHFFDYGSTTRNSMRNLSIQCVFLNNLIFQLFNHFIL
PSSMLARLVNIYMFRCNNKMLFVTSSFVGWLIGHILFMKWVGLVLVWIQQNNSIRSNVLIRSNKYLVSEL
RNSMARIFSILLFITCVYYLGRIPSPIFTKKLKETSETEERVESEEETDVEIETASETKGTKQEQEGSTE
EDPSPSLFSEEREDPDKIDETEEIRVNGKEKIKKDLFWFEKPLVTLLFDYKRWNRPFRYIKNDRFENAVR
NEMSQYFFYTCQSDGKERISFTYPPSLSTFWEMIQRKIPLFTLEKLSSDELYNQWIYTNEEKKNNLSNEF
LNRIEALDKESSSLNILEKRTRLCNDETKKEYLPKIYDPFLNGPYRGRIKKLFSPSIINETSIKNNIEGV
WINKIHGILLNNTDYQEFEQKIDTFNKKSLSTEINESLTLINKFGAEPKSSLNLKGLSLFSEPEQEKINS
EEEIKIFKFLFDAVITDPNDQTIIKKSIGIKEISKKVPRWSYKLIDELEQLEGENEENVPSDHQIRSRKA
KRVVIFTDNESNNDIYTNLKDNQNSDQKDEVALIRYSQQSDFRRGIIKGSMRAQRRKTVIWELFQANVHS
PLFLDRIDKLFFFSFDISGLMKKIFRNWNGKDAEFKISDSVEEKTKKKKKKEKKKEEEYKREEKARIEIA
EAWDSILFAQVIRGSLLVTQSILRKYIILPSLIIIKNIGRMLLFQFPEWSEDLKDWKREMHVKCTYNGVQ
LSETEFPKNWLTDGIQIKILFPFYLKPWHRSKLRSSHKDRMKKKKKKKNDFCFLTVWGMETELPFGSPRK
RPSFFEPIFKELKKKIRKFKKKYFLVLKILKERTKLFLKVSKETKKWIIKSFLFLKRIIKELSKRNPILL
FGLREIYELNETKKEKDSIISNQMIHESSVQIRSMEWTNSSLTEKKIKDLTDRTKTIRNQIEKITKEKKK
ITNTINISPNKTSYDSKIIESSKKIWQILKRRNTRLIRKSYYFIKFFIERIYIDIFLGIINIPRINTQLF
LESTKKIIDKYIYKNEENKEKINKKKQNTIHFISTIKKSLYNISNKNKNSKIFYDLSSLSQAYVFYKLSQ
TQVINLYKLRSVLQYNGTSFFLKNEIKDYFEAQGIFHSKLKHKNLLNSGMNQWKNWLRSHYQYDLSQIRW
SRLVPQKWRNRVNQDRMVQNKDLNKWDSYEKDRLIHYKKQNDFEANSLLNQKDNFKKDYRYDLLSYKSIN
YEDKKFQVNKNQEISYNYNTRKVNLFDMPEGIAINNYLGKGDILDIEKNPDRKYLDWRILNFSLRKKVDI
ESWVDTDSKSKKNTKTGVNNYQIIDKIDHQDFENNQANKKKNFFDWMGMNEEILNRPISNLEFWFFPEFV
LLYNTYKIKPWIIPIKLLLLNLNGNENVNKKINQKKKGFIPSNEKKSIEIENRNQEEKEPAGQGELESDK
EKKGNLESVLSNQEKNIEEDYAESDIKKRKNKKQYKSNTEAELDFFLKRYLRFQLRWNDFLNQRIINNIK
VYCLLLRLINPREIAISSIQRGEMSLDIMMIQKNLTLTELMKKGILIIEPVRLSVKNDGQFIIYQTIGIS
LVHKNKHQINQRYREKKYVDKKNFDESITKHQTITENRDKNHYDLLVPENILSPKRRRELRILICFNSKN
KNAVDRNSVFCNEKNVKNCGQVLDKKKDLDKDKNKLIKLKFFLWPNYRLEDLACMNRYWFNTNNGSRFSM
LRIHMYPRLKIR
>gnl|CDD|214396 CHL00206, ycf2, Ycf2; Provisional
MKGHQFKSWIFELREILREIKNSHYFLDSWTQFNSVGSFIHIFFHQERFIKLFDPRILSILLSRNSQGST
SNRYFTIKGVVLLVVAVLIYRINNRNMVERKNLYLTGLLPIPMNSIGPRNDTLEESFGSSNINRLIVSLL
YLPKGKKISESCFLDPKESTWVLPITKKCIMPESNWGSRWWRNWIGKKRDSSCKISNETVAGIEISFKEK
DIKYLEFLFVYYMDDPIRKDHDWELFDRLSPRKRRNIINLNSGQLFEILVKHWICYLMSAFREKIPIEVE
GFFKQQGAGSTIQSNDIEHVSHLFSRNKWAISLQNCAQFHMWQFRQDLFVSWGKNPHESDFLRNVSRENW
IWLDNVWLVNKDRFFSKVRNVSSNIQYDSTRSSFVQVTDSSQLKGSSDQSRDHFDSISNEDSEYHTLINQ
REIQQLKERSILWDPSFLQTERTEIESDRFPKCLSGYSSMSRLFTEREKQMNNHLLPEEIEEFLGNPTRS
IRSFFSDRWSELHLGSNPTERSTRDQKLLKKQQDVSFVPSRRSENKEIVDIFKIITYLQNTVSIHPISSD
PGCDMVPKDEPDMDSSNKISFLNKNPFFDLFHLFHDRNRGGYTLHHDFESEERFQEMADLFTLSITEPDL
VYHKGFAFSIDSYGLDQKQFLNEVFNSRDESKKKSLLVLPPIFYEENESFYRRIRKKWVRISCGNDLEDP
KPKIVVFASNNIMEAVNQYRLIRNLIQIQYSTYGYIRNVLNRFFLMNRSDRNFEYGIQRDQIGNDTLNHR
TIMKYTINQHLSNLKKSQKKWFDPLIFISRTERSMNRDPDAYRYKWSNGSKNFQEHLEHFVSEQKSRFQV
VFDRLRINQYSIDWSEVIDKKDLSKSLRFFLSKLLLFLSKKLLFLSKSLPFFFVSFGNIPIHRSEIHIYE
LKGPNDQLCNQLLESIGLQIVHLKKLKPFLLDDHDTSQKSKFLINGGTISPFLFNKIPKWMIDSFHTRIN
RRKSFDNTDSYFSMISHDQDNWLNPVKPFHRSSLISSFYKANRLRFLNNPHHFCFYCNKRFPFYVEKARI
NNYDFTYGQFLNILFIRNKIFSLCGGKKKHAFLERDTISPIESQVSNIFIPNDFPQSGDETYNLYKSFHF
PIRSDPFVRRAIYSIADISGTPLTEGQIVNFERTYCQPLSDMNLSDSEGKNLHQYLNFNSNMGLIHTPCS
EKYLPSEKRKKRSLCLKKCVEKGQMYRTFQRDSAFSILSKWNLFQTYMPWFFTSTGWKYLNLIFLDTFSD
LLPILSSSQKFVSIFHDIMHGSDISWRILQKKLGLKLPQWNLISEISSKCLHNLLLSEEMIHRESESPLI
WTHLRSPNVREFLYSILFLLLVAGYLVRTHLLFVSRASSELQTEFEKIKSLMIPSYMIELRKLLDRYPTS
ELNSFWLKNLFLVALEQLGDSLEEIRGSGGNMLLGGGPAYGVKSIRSKKKYLNINLIDIIDLIPNPINRI
TFSRNTRHLSHTSKEIYSLIRKRKNVNGDWIDDKIESWVANSDSIDDEEREFLVQFSTLTTEKRIDQILL
SLTHSDHLSKNDSGYQMIEQPGSIYLRYLVDIHKKYLMNYEFNTSCLAERRIFLAHYQTITYSQTSCGAN
SFHFPSHGKPFSLRLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVFLNKFLDNKPKGFLIDDID
IDDSDDIDDSDDIDRDLDTELLTMMNALTMDMMPKIDRFYITLQFELAKAMSPCIIWIPNIHDLNVNESN
YLSLGLLVNSLSRDCERCSTRNILVIASTHIPQKVDPALIAPNKLNTCIKIRRLLIPQQRKHFFTLSYTR
GFHLEKKMFHTNGFGSITMGSNARDLVALTNEALSISITQKKSIIDTNTIRSALHRQTWDLRSQVRSVQD
HGILFYQIGRAVAQNVLLSNCPIDPISIYMKKKSCKEGDSYLYKWYFELGTSMKKLTILLYLLSCSAGSV
AQDLWSLPGPDEKNGITSYGLVENDSDLVHGLLEVEGALVGSSRTEKDCSQFDNDRVTLLLRPEPRNPLD
MMQNGSCSIVDQRFLYEKYESEFEEGESEGALDPQQIEEDLFNHIVWAPRIWRPWGFLFDCIERPNELGF
PYWARSFRGKRIIYDEEDELQENDSEFLQSGTMQYQTRDRSSKEQGFFRISQFIWDPADPLFFLFKDQPF
VSVFSRREFFADEEMSKGLLTSQTDPPTSIYKRWFIKNTQEKHFELLIHRQRWLRTNSSLSNGFFRSNTL
SESYQYLSNLFLSNGTLLDQMTKTLLRKRWLFPDEMKIGFM
>gnl|CDD|214397 CHL00207, rpoB, RNA polymerase beta subunit; Provisional
INMNFALPDFLEIQRTSFCWFLNEGLNEELNIFSKIFDYTGNLELLLFGKNYKLKYPKYNLLSAKSYDSN
YSIQIYLPLKFINLKTNKIKFINYLIGNLPKMTQRGTFIINGLERVIVSQIIRSPGIYFKKEIKKNSNKI
YSATLIPNRGSWIKFELDKNKEIWIRIDKNRKKPLIIFLKALGLTDQDIYSRLTKSEFLKKLKPILLNSN
SYTNEEILLEIYKNLSPIEPATVNDANQNLFSRFFDPKNYDLGKVGRYKINNKLNLNIPERVRNLTYEDI
LSIIDKLINLKINKGNFDDIDHLKNRRVRSVGELLQNQFRIGLKRLERILRNRMTICDIDSLSKFNLINP
KPLIALIREFFGSSQLSQYMDQTNPLSELTHKRRISILGPGGLDKDRISFAVRDIHPSHYGRICPIETPE
GPNCGLIGSLATNARINKFGFIETPFYKVINGKVKKFGNPIYLTADSEDLYRIAPNDINLNKNNYFKKNI
IPVRYKQEFKTVNPSKVDFIAISPIQVFSIAESLIPFLEHNDANRALMGSNMQRQAVPLLYPEKPIVGTG
YEKQIALDSGMTIISLTEGIVVSVSAYKIIIQDDNNRYIHYYLQKYQRSNQNTCINYRPIVWVGEKINIG
QILADGSDIDNSELALGQNVLVAYMPWEGYNFEDAILINKRLVYEDLFTSIHIEKYEIELRQTKLGSEEI
TRNIPNVSEYSLKNLDENGIISIGSKVLAGDILVGKITPKGESDQLPEGKLLRAIFGEKAKDVKDTSLRM
PNGGYGRVIKVEIFSRSKGDELKFGYYLKIRVFIAQIRKIQVGDKLAGRHGNKGIISRILPRQDMPYLPD
GTPPDIILNPLGVPSRMNVGQLFECLLGLAGDNLNKRFKILPFDEMYGSEYSRILINNKLNQASIKNNEY
WLFNSYHPGKMVLRDGRTGYKFKNPVTVGIAYMLKLIHLVDDKIHARTTGPYSLVTQQPLGGKAQHGGQR
FGEMEVWALEAFGAAYTLKELLTIKSDDMQGRNETLNAIVKGQPIPKPGTPESFKVLMRELQSLGLDIEA
YKIENFLEGQRLEIEINLMENYKYFRK
>gnl|CDD|439772 COG0001, HemL, Glutamate-1-semialdehyde aminotransferase [Coenzyme transport and metabolism]. Glutamate-1-semialdehyde aminotransferase is part of the Pathway/BioSystem: Heme biosynthesis
KTPRSAELFERAKKVIPGGVNSPVRAFKSVGGTPLFIERAKGAYLYDVDGNEYIDYVGSWGPLILGHAHP
EVVEAVQEAAERGTSFGAPTELEVELAELICERVPSVEMVRFVNSGTEATMSAIRLARGYTGRDKIIKFE
GCYHGHSDSLLVKAGSGAATLGVPDSPGVPEAVAKDTLVLPYNDLEAVEEAFEEHGDEIAAVIVEPVAGN
MGVVPPEPGFLEGLRELCDEHGALLIFDEVITGFRVALGGAQGLYGVTPDLTTLGKIIGGGLPVGAFGGR
AEIMELLAPLGPVYQAGTLSGNPLAMAAGLATLELLKEPGVYERLEALGARLREGLREAAAEAGVPHTVN
GVGSMFGVFFTDEPVRNYADAKASDTERFARFFHAMLERGVYLAPSQFEAWFLSAAHTDEDIDKTLEAAE
EALKALAAA
>gnl|CDD|439773 COG0002, ArgC, N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]. N-acetyl-gamma-glutamylphosphate reductase is part of the Pathway/BioSystem: Arginine biosynthesis
IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLVFEPPDPDELAAGCDV
VFLALPHGVSMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKG
ARLIANPGCYPTAVLLALAPLLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRH
TPEIEQELSRLAGEDVKVSFTPHLVPMVRGILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEGRL
PETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAGQAVQNMNLMFGLPETTGLELVPLYP
>gnl|CDD|439774 COG0003, ArsA, Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism]
DMTRIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELGNEPTEVAVPNLYALEI
DPEAELEEYWERVRAPLRGLLPSAGVDELAESLPGTEELAALDELLELLEEGEYDVIVVDTAPTGHTLRL
LSLPELLGWWLDRLLKLRRKASGLGRPLAGILGLPDDPVLEGLEELRERLERLRELLRDPERTSFRLVTN
PERLAIAETRRALEELALYGIPVDGLVVNRVLPEEADDDAFLAARRERQQEYLAEIEEAFAPLPVVEVPL
LAEEVVGLEALRALAEELY
>gnl|CDD|439775 COG0004, AmtB, Ammonia channel protein AmtB [Inorganic ion transport and metabolism]
MAAAALLDSGDTAWMLVAAALVLLMTPGFALFEGGLVRSKNVLNVLMKNFADFALVSVLWVLVGYSLAFG
PGAGGFIGGPLGFFLSGVGPGSLAGTIPELVFFLFQMMFAAITAAIISGAVAERMKFSAYLIFSVLWSTL
VYPPVAHWVWGGGWLAQLGFLDFAGGTVVHIVGGWAALAGALVLGPRIGKYKGKPNAIPPHNLPLAALGA
FLLWFGWFGFNAGSALAANGLAGLAFVNTNLAAAAGALAWLLVEWLRKGKPDLLGAANGALAGLVAITPA
AGFVSPLGALVIGLIAGVICVFAVTFLKRKLKIDDPLGAFGVHGVGGIWGTLATGLFASPALGGAGLFYG
GGAAQLGVQLIGVLVVGVWAFVVSFIILKILKKTIGLRVSEEEEREGLDLSEHGERAYPEVKS
>gnl|CDD|439776 COG0005, XapA, Purine nucleoside phosphorylase [Nucleotide transport and metabolism]. Purine nucleoside phosphorylase is part of the Pathway/BioSystem: Purine salvage
IGIIGGSGLGDLLEDIEEVAVETPYGEHSGELVIGTLGGKRVVFLPRHGRGHYYEPHMINYRANIRALKA
LGVKRLIATNAVGSLNPDLKPGDLVLIDDHIDLTGGRPLTGFNGGGVRFVDMTDPYDPELRELLLEAAKE
LGIPLDEGVYVCTEGPRFETPAEIRMLRRLGADVVGMSTVPEAILAREAGLCYAGISLVTNYAAGISDEP
LTHEEVLEVAAAAAEKLRRLLKELIARLPAE
>gnl|CDD|439777 COG0006, PepP, Xaa-Pro aminopeptidase [Amino acid transport and metabolism]
ARLRALMAEAGLDALLLTDPSNFAYLTGFRGSPERLAALLVTADGEPVLFVDELEAERELVDASDLLEEL
RAIKSPEEIELMRKAARIADAAHEAALAALRPGVTEREVAAELEAAMRRRGAEGPSFDTIVASGENAAIP
HYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEV
DAAARDVLAEAGYGEYFPHGTGHGVGLDVHEGPQISPGNDRPLEPGMVFTIEPGIYIPGIGGVRIEDTVL
VTEDGAEVLTRLPRELLEL
>gnl|CDD|439778 COG0007, CysG, Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]. Uroporphyrinogen-III methylase (siroheme synthase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
KGKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINA
LLVELARAGKRVVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVT
FVTGHEKDGKLDLDWAALARPGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTL
ATLAELAAEAGLKSPALIVVGEVVALREKLSWFEA
>gnl|CDD|439779 COG0008, GlnS, Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDW
DEGPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLA
AGEPPVLRFKIPEEGVVFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHL
SNTPRQIWLYEALGWEPPEFAHLPLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDD
QEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRALDDEELAELLAPELPEAGIREDLERLVPLV
RERAKTLSELAELARFFFIEREDEKAAKKRLAPEEVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAG
VKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAIDKLA
>gnl|CDD|439780 COG0009, TsaC, tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal structure and biogenesis]. tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC is part of the Pathway/BioSystem: tRNA modification
MATILKIQPRLIEQAAEALRAGGVVAYPTDTVYGLGCDALNKEAVERIFAIKGRPRDKPLIVLVADLSQL
EEYAKEVPDAARRLAKAFWPGPLTLILPATKEVPDLLTGGRDTVAVRVPDHPVALALLRALGPPLASTSA
NLSGEPPPTTAEEVREQLGDRVDLILDGGPCGVGVPSTIVDLTGGEPEILRPGAIDVEELEEVL
>gnl|CDD|439781 COG0010, SpeB, Arginase/agmatinase family enzyme [Amino acid transport and metabolism]. Arginase/agmatinase family enzyme is part of the Pathway/BioSystem: Urea cycle
LGLPAVDLEEADIVLLGVPSDLGVSYRPGARFGPDAIREASLNLEPYDPGVDPLEDLGVADLGDVEVPPG
DLEETLAALAEAVAELLAAGKFPIVLGGDHSITLGTIRALARAYGPLGVIHFDAHADLRDPYEGNLSHGT
PLRRALEEGLLDPENVVQIGIRSNDPEEFELARELGVTVFTAREIRERGLAAVLEEALERLRAGDPVYVS
FDIDVLDPAFAPGVGTPEPGGLTPREALELLRALAASGKVVGFDIVEVNPPLDPDGRTARLAAKLLWELL
GGL
>gnl|CDD|439782 COG0011, YqgV, Thiamin-binding stress-response protein YqgV, UPF0045 family [Coenzyme transport and metabolism]
VIVEISVIPLGTGESVSEYVAEAIEVIRESGLKYEVTPMGTTIEGELDELMAVVKKAHEALFEAGAPRVS
TVIKIDDRRDKEGTMEEKVESVEEKLGR
>gnl|CDD|439783 COG0012, GTP1, Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis]
LKCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVD
IAGLVKGASKGEGLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEK
RLERLEKKAKSGDKEAKAELELLEKLKEHLEEGKPARSLELSEEEKKLLKELQLLTAKPVLYVANVDEDD
LAEGNPYVEKVREYAAKEGAEVVVICAKIEAELAELDEEERAEFLEELGLEESGLDRLIRAGYDLLGLIT
FFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFERGFIRAEVISYDDLIAYGSEAAAKEAGKLRLEGKDYVV
QDGDVIHFRFNV
>gnl|CDD|439784 COG0013, AlaS, Alanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Alanyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MMTSAEIRQKFLDFFESKGHTIVPSSSLVPKNDPTLLFTNAGMVQFKPYFLGQEKPPYPRATTSQKCVRT
GGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKEEAIAWAWELLTEVLGLPKERLWVTVYEDDDEAYDIW
KKEIGVPEERIIRLGKKDNFWEMGDTGPCGPCSEIFYDRGPEYGGGPPGSPGEDGDRYIEIWNLVFMQFN
RDEDGTLTPLPKKNIDTGMGLERIAAVLQGVHSNYETDLFRPLIEAAAELTGVKYGADEEDDVSLRVIAD
HIRAVAFLIADGVLPSNEGRGYVLRRILRRAVRHGRLLGIKEPFLYKLVPVVVEEMGDAYPELKEKQELI
EKVLKAEEERFLRTLERGLKLLDEAIAKLKAAGGKVLSGEDAFKLYDTYGFPLDLTEEIARERGLTVDEE
GFEAAMEEQRERARAAAKFSGDAAVDGVWRELLEEGGPTEFVGYDTLEAEAKVLALVKDGELVDSAKAGE
EVEVVLDRTPFYAESGGQVGDTGTIEGDGGVFEVTDTQKPPGGLIVHIGKVEEGELKVGDTVTAQVDAER
RRAIARNHSATHLLHAALREVLGEHVTQAGSLVAPDRLRFDFSHFEALTPEELAEIEDLVNEKIRENLPV
ETREMPLDEAKALGAMALFGEKYGDEVRVVSIGDFSRELCGGTHVSRTGDIGLFKIVSESSVAAGVRRIE
AVTGEAALEYLREQEALLKELAELLKAPPEELPERVEALLEELKELEKELEQLKAKLASAAADDLLAQAE
EIGGVKVLAARVEGVDAKDLRDLADDLKDKLGSGVVVLASVADGKVSLVAGVTKDLVKKGLKAGDLVKEV
AKIVGGGGGGRPDMAQAGGKDPSKLDEALAAVKEWLAEKL
>gnl|CDD|439785 COG0014, ProA, Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]. Gamma-glutamyl phosphate reductase is part of the Pathway/BioSystem: Proline biosynthesis
AYLEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENGLSEALLDRLKLT
EERIEAMAEGLRQVAALPDPVGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNA
VILRGGSEAIHSNRALVAVIQEALEEAGLPEDAVQLVPTTDREAVGELLTLDGYIDVIIPRGGAGLIRRV
VENATVPVIEHGDGNCHVYVDASADLEMAVDIVVNAKTQRPGVCNALETLLVHRDIAAEFLPRLAAALAE
AGVELRGDERTRAILPDVKPATEEDWGTEYLDLILAVKVVDSLDEAIAHINRYGSGHTEAIVTEDYAAAR
RFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELTTYKYVVRGDGQIRP
>gnl|CDD|439786 COG0015, PurB, Adenylosuccinate lyase [Nucleotide transport and metabolism]. Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis
LISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADDFEIDAERIKEIEKET
RHDVKAFVYALKEKVGAEAGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTP
MLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEAWPEVEERVAEKL
GLKPNPVTTQIEPRDRHAELFSALALIAGSLEKIARDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPI
DSENIEGLARLARALAAALLEALASWHERDLSDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMR
ANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLRELLAADPEIPAELSKEELEALF
DPANYLGAADEIVDRV
>gnl|CDD|439787 COG0016, PheS, Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]. Phenylalanyl-tRNA synthetase alpha subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAA
LEARKEELEAAELEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNF
EALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDESDATHSPMFHQV
EGLVVDKGISFADLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCFICGGKGCRVCKGTGWLE
ILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQFG
>gnl|CDD|439788 COG0017, AsnS, Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Aspartyl/asparaginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLENFEEAKKLTTESSVEV
TGTVVESPRAPQGVELQAEEIEVLGEADEPYPLQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAI
REFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKS
NTRRHLAEFWMIEPEMAFADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGRDVERLEKVPESPFPRITY
TEAIEILKKSGEKVEWGDDLGTEHERYLGEEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPG
IGEIIGGSQREHRYDVLVERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIP
FPRDPGRLTP
>gnl|CDD|439789 COG0018, ArgS, Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MNIKEELAEAIAAALAALGAGLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDAD
PLVEKVEIAGPGFINFFLSPAALAAVLKEILADGEDYGRSDAGKGKKVVVEYVSANPTKPLHVGHLRGAV
IGDALARILEAAGYDVTRENYINDAGTQIGKLALSLERYGEEEIEPESKPDGYLGDLYVKFHKEYEEDPE
LEDIARELLAKLEPGDEEALELWKKAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSGAVEEVVEELKEK
GLLYESDGALWVRLTEFGDDKDRVLVKSDGTYTYFTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLF
AALKALGYDPAKDLEHLLFGMVNLRDGEKMSTRAGTVVTLDDLLDEAVERAREIIEEKSEEEKEEIAEQV
GIDAVRYFDLSRSRDKDLDFDLDLALSFEGNTNPYVQYAHARICSILRKAGEELDGLAEADLSLLTEEEE
LALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEELRAARLALVAATAQVLK
NGLGLLGISAPERM
>gnl|CDD|439790 COG0019, LysA, Diaminopimelate decarboxylase [Amino acid transport and metabolism]. Diaminopimelate decarboxylase is part of the Pathway/BioSystem: Lysine biosynthesis
MTHFARDGELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGSGAKVLYAVKANSNLAVLRLL
AEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAELG
KRAPVGLRVNPGVDAGTHEYISTGGKDSKFGIPLEDALEAYRRAAALPGLRLVGLHFHIGSQILDLEPFE
EALERLLELAEELRELGIDLEWLDLGGGLGIPYTEGDEPPDLEELAAAIKEALEELCGLGPELILEPGRA
LVGNAGVLLTRVLDVKENGGRRFVIVDAGMNDLMRPALYGAYHPIVPVGRPSGAEAETYDVVGPLCESGD
VLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGEARLIRRRETYEDLLASEVL
>gnl|CDD|439791 COG0020, UppS, Undecaprenyl pyrophosphate synthase [Lipid transport and metabolism]
LYERALLPEIDPGNLPRHVAIIMDGNGRWAKKRGLPRIEGHRAGVEAVREVVEACAELGIKYLTLYAFST
ENWKRPKEEVSFLMGLLREYLRRELDELHKNNVRVRVIGDRSRLPESLQEAIEEAEELTKNNTGLTLNIA
LNYGGRWEIVDAVRKIARDVAAGELDPEDIDEETISRYLYTADLPDPDLLIRTSGEQRISNFLLWQLAYA
ELYFTDVLWPDFDKEDLLRAIRDYQRRERRFGGTSEQV
>gnl|CDD|439792 COG0021, TktA, Transketolase [Carbohydrate transport and metabolism]. Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway
MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSML
LYSLLHLTGYDLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRP
GHDIVDHYTYVIAGDGDLMEGISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGW
HVIRVEDGHDLEAIDAAIEAAKAETDKPTLIICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWP
PEPFEVPDEVYAHWRAAGERGAAAEAEWNERFAAYAAAYPELAAELERRLAGELPEDWDAALPAFEADAK
GVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDPSGRNIHFGVREHAMGAIMNGIA
LHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLASLRAIPNLDVIR
PADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAAEGVAKGAYVLADAEGTPDVILIATGSEVS
LAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGI
DTFGASAPAKVLFEEFGFTVENVVAAAKELL
>gnl|CDD|439793 COG0022, AcoB, Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]. Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGA
ALAGLRPVVEIQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHI
PGLKVVAPSTPYDAKGLLKAAIRDDDPVIFLEHKRLYRLKGEVPEEDYTVPLGKARVVREGTDVTIVTYG
AMVHRALEAAEELAEEGISAEVIDLRTLSPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEA
FDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVAAVRELLAY
>gnl|CDD|439794 COG0023, SUI1, Translation initiation factor 1 (eIF-1/SUI1) [Translation, ribosomal structure and biogenesis]. Translation initiation factor 1 (eIF-1/SUI1) is part of the Pathway/BioSystem: Translation factors
MKDKKDNSGLVYSTDPGREPEEEEEPAEELPPGDGIVRVRRETKGRKGKGVTVVTGLPLDDEDLKALAKE
LKKKCGCGGTVKDGEIEIQGDHRDKIKALLEKKGYKVKRAGG
>gnl|CDD|439795 COG0024, Map, Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]
IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSV
NEVVVHGIPSDRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGN
RLGDIGHAIQSYAESNGYSVVREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEV
KVLDDGWTVVTKDGSLSAQFEHTVAVTEDGPEILTLPDGG
>gnl|CDD|439796 COG0025, NhaP, NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion transport and metabolism]
MELLLLILLLLLLGLLSQWLARRLKLPAPLLLLLAGILLGPGLGLELDPELGDLEPLLELFLPPLLFEAA
LNLDLRELRRNGRPILRLAVVGVLLTTLAVALAAHWLLGLPLAAALLLGAILAPTDPVAVSPILRRLGVP
KRLRTILEGESLLNDATALVLFVLALAAALGGGFSLGEALLDFLLAILGGILVGLLLGWLLGRLLRRLPD
PLLEILLTLALPFLAYLLAEALHGSGVLAVVVAGLVLGNAGRRSLSPETRLQLLEFWETLEFLLNSLLFV
LLGAQLPLILLGALGLGGILLVLLALLVVRPLWVFLSLALRGSRLSWRERLFLSWGGPRGIVSLALALSL
PLHGGAGFPGRDLILALAFGVILLTLVLQGLTLPPLARRLGLREDEPEGEELEAALARAALLELLAAELL
ADDEEVVLRAARRARRRREAAELLSEEAEEELDEDLLRLLLALLRLRLLNALAAARLERLLLRRRVEELL
RLLERLLRERELEELR
>gnl|CDD|439797 COG0026, PurK, Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]. Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
QLGRMLALAAKRLGYRVHVLDPDPDSPAAQVADEHIVADYDDEEALREFAERCDVVTFEFENVPAEALEA
LEAEVPVRPGPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRRGGYDGKG
QVVIKSAADLEAAWAALGGGPCILEEFVPFERELSVIVARSPDGEVATYPVVENVHRNGILDESIAPARI
SEALAAEAEEIAKRIAEALDYVGVLAVEFFVTKDGELLVNEIAPRPHNSGHWTIEACVTSQFEQHLRAVC
GLPLGDTELLSPAVMVNLLGDDWEDPGWEALLALPGAHLHLYGKKEARPGRKMGHVTVLGDDLEEALERA
RAA
>gnl|CDD|439798 COG0027, PurT, Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]. Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis
MTTIGTPLSPNATKVMLLGSGELGKEVAIELQRLGVEVIAVDRYANAPAMQVAHRSYVIDMLDGDALRAL
IEREKPDFIVPEIEAIATDALVELEAEGFRVVPTARAVRLTMNREGIRRLAAEELGLPTSPYRFADSLEE
LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSPADIEAAWEYAQEGGRGGAGRVIVEGFVDFDYEITLLTVR
AVDGPTHFCEPIGHRQEDGDYRESWQPQPMSEAALAKAQEIAKKVTDALGGRGIFGVELFVKGDEVYFSE
VSPRPHDTGMVTLISQDLSEFALHARAILGLPVPEIRLVGPAASAVILAEGESWAPAFDGLAEALAVPGT
DLRLFGKPEAYGRRRMGVALATADDVEEAREKAREAAAKVKVV
>gnl|CDD|439799 COG0028, IlvB, Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]. Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVC
LVTSGPGATNLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEV
LRRAFRIATSGRPGPVVLDIPKDVQAAEAEEEPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAG
GGARRAGAAEELRALAERLGAPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFD
DRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIVGDAKAVLAALLEALEPRADDRAAWLARIAAWRA
EYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYGLPA
AIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGGRYSGTDLP
NPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEENPPGATLDEM
>gnl|CDD|439800 COG0029, NadB, Aspartate oxidase [Coenzyme transport and metabolism]. Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis
ERLKTDVLVIGSGIAGLSAALKLAERGRVTLLTKGELGESNTRWAQGGIAAVLDPGDSPELHIADTLAAG
AGLCDPEAVRVLVEEGPERIRELIELGVPFDRDEDGELALTREGGHSRRRILHAGDATGREIERALLEAV
RAHPNITVLENHFAVDLITDADGRCVGAYVLDEKTGEVETIRAKAVVLATGGAGQLYAYTTNPDVATGDG
IAMAYRAGARLADMEFVQFHPTALYHPGAPSFLISEAVRGEGAVLRNADGERFMPDYHPRAELAPRDVVA
RAIDAEMKKTGGDCVYLDISHLDAEFIRERFPTIYARCLELGIDITKEPIPVAPAAHYTMGGVATDLDGR
TSIPGLYAVGEVACTGVHGANRLASNSLLEGLVFGRRAAEDIAARLAESPLPPEIPEWDESVTDPDEEVL
IAHLRDELRRLMWDYVGIVRTAKGLERALRRLELLREEIEEYANFRVSRDLLELRNLLLVAELIVRAALA
RKESRGAHYRSDYPETDPAWRRHTVLRLDDD
>gnl|CDD|439801 COG0030, RsmA, 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]. 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification
MSKSRRYGLRPKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRR
LAAILRETFAAYPNLTVIEGDALKVDLPALAAGEPLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQK
EVAERLVAKPGSKDYGRLSVLVQYYADVEILFTVPPEAFYPPPKVDSAVVRLTPRPEPLVPVADEKLFFR
VVKAAFSQRRKTLRNSLKSLFSKERLEEALEAAGIDPTARAEELSVEEFARLANALKKRG
>gnl|CDD|439802 COG0031, CysK, Cysteine synthase [Amino acid transport and metabolism]. Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis
MRIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEA
TSGNTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAF
WPNQFENPANPEAHYETTGPEIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLL
SGGEPGPHKIEGIGAGFVPKILDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKR
LGPGKTIVTILPDSGERYLST
>gnl|CDD|439803 COG0033, Pgm, Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism]
LHPRAGQPAPPSDLIDVPRLVSAYYTIKPDPTTPFQDVKFGTSGHRGSSLKGSFNEPHILAITQAIFDYR
KAQGITGPLFLGGDTHALSEPAIQTALEVLAANGVGVVIVGQGGYTPTPAVSHAILKYNRGTSGAADGIV
LTPSHNPPEDGGIKYNPPNGGPADEDVTDAIEARANEILEYGLADVKRVPLDRAGTAMTVEVIDPVADYV
ELLESVFDFDAIRAAGFRIGFDPLGGATGPYWKAIAERYGLDLTVVNGVPDPDFRFMTLDWDGGIRMDPS
SPYAMASLIAGKDAPDFAAANDGDGDRHGIVTPRGGLMNPNHYLAVAIAYLFTHRPGWAALAGVGKTMVT
SSAIDRVAAALGRPLYEVPVGFKWFVNGLDAGSLGFGGEESAGASFLRRDGSVWTTDKDGLWAVLLAAEI
LAVTGKSPAEIYRELWARFGRPYYSRHDAEATDEQKARLAKLSGEQVGATTLAGEDIFAYLDPAPGNGAA
IGGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIDAEAADLVDAALAL
>gnl|CDD|439804 COG0034, PurF, Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]. Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis
MDKLHEECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEEDLERLK
GNIAIGHVRYSTTGSSSLENAQPFYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHL
IARELTKEDLEEAIKEALRRVKGAYSLVILTGDGLIAARDPNGIRPLVLGKLEDGYVVASESCALDILGA
EFVRDVEPGEIVVIDEDGLRSRQFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREAPVD
ADVVIPVPDSGRPAAIGYAEESGIPYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVL
VDDSIVRGTTSRRIVKMLREAGAKEVHFRIASPPIRYPCYYGIDTPTREELIAANRSVEEIREYIGADSL
GYLSLEGLIEAVGEPIEGFCTACFTGDYPTGIPDEEKKRLELLR
>gnl|CDD|439805 COG0035, Upp, Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]. Uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage
MLRVHVVDHPLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGKTTGKVLAGK
KLVIVPILRAGLGMLDGVLDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSL
VAAIDLLKKRGAKDIKIVCLIAAPEGIERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK
>gnl|CDD|439806 COG0036, Rpe, Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]. Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway
IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENP
DRYIEAFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPG
FGGQKFIPSVLEKIRRLRELIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAA
LREAAAAA
>gnl|CDD|439807 COG0037, TilS, tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]. tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification
KVRKAIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRLGFELVAVHVDHGLREESDEDAEFVAELC
EELGIPLHVVRVDVPAIAKKEGKSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGS
GLAGLAGMPPSRGGGVRLIRPLLYVSRKEIEAYAKENGLPWIEDPCNYDPRYTRNRIRHLVLPELEERNP
GFKENLARSAENLAEEEDLLDELAE
>gnl|CDD|439808 COG0038, ClcA, H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism]
RRRLLRLLLLAVLVGILAGLAAVLFRLLLELATHLFLGGLLSAAGSHLPPWLVLLLPPLGGLLVGLLVRR
FAPEARGSGIPQVIEAIHLKGGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGRLLRLS
PEDRRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLLFGNGPLFGVP
SVPALSLLELPLYLLLGILAGLVGVLFNRLLLKVERLFKRLKLPPWLRPAIGGLLVGLLGLFLPQVLGSG
YGLIEALLNGELSLLLLLLLLLLKLLATALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLLFPGLGLSP
GLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPLMIACVIAYLVSRLLFPRSIYTAQLER
>gnl|CDD|439809 COG0039, Mdh, Malate/lactate dehydrogenase [Energy production and conversion]. Malate/lactate dehydrogenase is part of the Pathway/BioSystem: TCA cycle
MKVAIIGAGNVGSTLAFRLASGGLADELVLIDINEGKAEGEALDLADAFPLLGFDVKITAGDYEDLADAD
VVVITAGAPRKPGMSRLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVDVMTYIAQKASGLPKERVIG
MGTVLDSARFRSFLAEKLGVSPRDVHAYVLGEHGDSMVPLWSHATVGGIPLTELIKETDEDLDEIIERVR
KGGAEIIEGKGSTYYAIAAAAARIVEAILRDEKRVLPVSVYLDGEYGIEDVYLGVPVVIGRNGVEKIVEL
ELTDEERAKLDASAEELKEEID
>gnl|CDD|439810 COG0040, HisG, ATP phosphoribosyltransferase [Amino acid transport and metabolism]. ATP phosphoribosyltransferase is part of the Pathway/BioSystem: Histidine biosynthesis
MMLRIALPKGRLLEETLELLKKAGIKLREEDSRKLIAETNDPDVEVLLLRPQDIPTYVEDGAADLGITGK
DVLLESGADVYELLDLGFGKCRLVVAVPEGSDYTSLADLRGLRIATKYPNLTRRYFAEKGIDVEIVKLNG
SVELAPLLGLADAIVDIVSTGSTLRANGLKEVETILESSARLIANRASLKDKREKIEQLLERLEGVLEAR
GKVYLMMNVPKEKLEEVVALLPGLESPTVSPLEDWVAVHAVVPEDEVWELIDKLKAAGARGILVTPIEKM
I
>gnl|CDD|439811 COG0041, PurE, Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]. Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase is part of the Pathway/BioSystem: Purine biosynthesis
PKVGIIMGSDSDWPTMKKAAKILDEFGIPYEVRVVSAHRTPDRLFEYAKTAEERGLKVIIAGAGGAAHLP
GMVAAKTTLPVIGVPVKSKALDGLDSLLSIVQMPPGVPVATVAIGGAKNAALLAAQILALKDPELAEKLK
AYREEQTEKVLAKDEELQEKL
>gnl|CDD|439812 COG0042, DusA, tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]. tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
GNLELPNPLILAPMAGVTDRPFRRLCRELGAGLLYTEMVSARALLHGNRKTRRLLDFDPEEHPVAVQLFG
SDPEELAEAARIAEELGADEIDINMGCPVKKVTKGGAGAALLRDPELVAEIVKAVVEAVDVPVTVKIRLG
WDDDDENALEFARIAEDAGAAALTVHGRTREQRYKGPADWDAIARVKEAVSIPVIGNGDIFSPEDAKRML
EETGCDGVMIGRGALGNPWLFREIDAYLAGGEAPPPSLEEVLELLLEHLELLLEFYGERRGLRRMRKHLL
WYFKGLPGARELRRRLSKAKSLAELLELLE
>gnl|CDD|439813 COG0043, UbiD, 3-polyprenyl-4-hydroxybenzoate decarboxylase [Coenzyme transport and metabolism]. 3-polyprenyl-4-hydroxybenzoate decarboxylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
MAYRDLREFLAALEKRGELKRIKEPVDPDLEITAITRRVLRAGGPALLFENVKGYGFPVLGNLFGSRERV
ALALGVPPDELGERLAEALKKEPIPPKVVSSAPCQEVVLTGDDVDLTKLPIPTCWPGDGGPYITLGLVIT
KDPETGWQNVGIYRMQVLDKNTLGMHWLPHRHGALHYRKAEERGKPLPVAVAIGADPATILAAVAPLPYG
VDEYEFAGALRGEPVELVKCETVDLEVPANAEIVLEGYIDPGERAPEGPFGEHTGYYSPVDPFPVFRVTA
ITHRKDPIYPSTVVGRPPEEDALLGIATEAIFLPLLRKAFPEVVDVYLPPEGCSRRLAVVSIKKRYPGHA
KRVMMAAWGLGQMMYTKFVIVVDDDVDPRDLNEVLWALATRVDPDRDVVIIPNTPGDPLDPSSPPPGLGS
KMGIDATRKWPEEGGREFPEPIEMPPEVKARVDELWKEL
>gnl|CDD|439814 COG0044, AllB, Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]. Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDI
ETGTRAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALAEAG
AVAFKVFMGSDDGNPVLDDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGLKGRPAEAE
EEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPP
LRTEEDREALWEGLADGTIDVIATDHAPHTLEEKELPFAEAPNGIPGLETALPLLLTELVHKGRLSLERL
VELLSTNPARIFGLPRKGRIAVGADADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGR
VVYEDGEVVGEPRGRFLRR
>gnl|CDD|439815 COG0045, SucC, Succinyl-CoA synthetase, beta subunit [Energy production and conversion]. Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
MNLHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKAGGVKLAKSPEEAR
EAAEEILGMTLVTHQTGPKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEET
PEKIIKVPIDPLVGLQPYQARELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLV
ALDAKVNFDDNALFRHPELAALRDLSEEDPLEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAG
GEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFGGITRCDVVAEGIVAALKEVGLKVPVVVRLE
GTNVEEGRKILAESGLNIIAADTLEEAAKKAVELAKGA
>gnl|CDD|439816 COG0046, PurL1, Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and metabolism]. Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain is part of the Pathway/BioSystem: Purine biosynthesis
MSTVDLEGGREALEEANRELGLALSDDEYDYIVEILGRNPTDVELGMFSQMWSEHCSYKSSNALLKSLPT
EGPRVLSGPGDNAGVVDIGDGLAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIFGMGARPIAGLDSLRF
GNLDQPPASPRYILIGVVAGIADYGNCFGVPTVGGEVRFDESYEGNPLVNAGGVGIIRADHIFKAKAPGV
GNKVVYVGGPTGRDGIGGATFASEELGEDSELDRPAVQVGDPFMEKRLIEAILELGDTGLIVGIQDMGAG
GLSSASSEMAAKGGLGAEIDLDKVPLREPGMSPYEIWLSESQERMLLVVKPEKLEEFEAIFERWRLPAAV
IGEVTDDGRLVVTDHGETVADLPLDFLAGGAPKYHRPAKRPAYLEPLDLPEPIDLEEALLRLLSSPNVAS
KEWLYRQYDREVGGNTVRDPGVADAAVVRVDGTYKGLAMSTGENPRYALLDPYAGARMAVAEAARNLAAV
GAEPLAITDCLNWGNPEKPEEMAQLVEAVKGLADACRALGIPVPSGNVSLYNETKDGKVAIPPTPVIGAV
GLVDDVRKTVTPDLKKEGDLLYLIGETKNELGGSEYAQVLGQLGGEPPDVDLEAEKALFEAVQELIREGL
ILAAHDVSDGGLAVALAEMAFAGGLGADIDLDALGDLRPDAALFSESQGRAVVQVAPEDAEAVEALLAEA
GLPAHVIGTVTGDDRLVIRRGGETLLSLSLAELRDAWEETLPRLRDN
>gnl|CDD|439817 COG0047, PurL2, Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]. Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
PKVAILVFPGSNCDRDMAAAFERAGAEAEDVWHSDLRTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSPIM
DAVREFARRGGLVLGICNGFQILTELGLLPGIWPALTRNRSLRFICRWVYLRVENNDSPFTSGMEAGEVI
PIPIAHGEGRYVADEETLAELEANGQVAFRYVDADGNVTYPANPNGSLNNIAGITNEDGNVLGMMPHPER
AVEPLLGPGESTDGLRIFRSAVKYFG
>gnl|CDD|439818 COG0048, RpsL, Ribosomal protein S12 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S12 is part of the Pathway/BioSystem: Ribosome 30S subunit
MPTINQLVRKGRKKKKKKSKSPALKGCPQKRGVCTRVYTTTPKKPNSALRKVARVRLSNGIEVTAYIPGE
GHNLQEHSVVLVRGGRVKDLPGVRYHIVRGALDTAGVKGRKQSRSKYGAKKPKA
>gnl|CDD|439819 COG0049, RpsG, Ribosomal protein S7 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S7 is part of the Pathway/BioSystem: Ribosome 30S subunit
MPRRGRAPKREVLPDPKYNSVLVTKFINKIMLDGKKSVAEKIVYGALDIIEEKTGEDPLEVFEKALENVK
PLVEVKSRRVGGATYQVPVEVRPERRQALAMRWIIDAARKRKEKTMAERLANELLDASNNRGAAVKKRED
THKMAEANKAFAHYRW
>gnl|CDD|439820 COG0050, TufA, Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]. Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors
MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEY
ETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDM
VDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTD
KPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLL
LRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVITLPEGV
EMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE
>gnl|CDD|439821 COG0051, RpsJ, Ribosomal protein S10 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S10 is part of the Pathway/BioSystem: Ribosome 30S subunit
MTKQKIRIRLKSYDHRLLDQSVKKIVETAKRTGAKVKGPIPLPTKILRVTVLRSPHVDKDSREQFEMRTH
KRLIDIHDPTDKTIRALMRLDLPAGVDIEIKLE
>gnl|CDD|439822 COG0052, RpsB, Ribosomal protein S2 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S2 is part of the Pathway/BioSystem: Ribosome 30S subunit
MAVVTMKQLLEAGVHFGHQTRRWNPKMKPYIFGERNGIHIIDLQKTVPLLEEAYNFVRDVAANGGKILFV
GTKKQAQEIIAEEAERCGMPYVNERWLGGMLTNFKTIRKSIKRLKELEKMEEDGTFEKLTKKEALMLRRE
REKLEKNLGGIKDMKRLPDALFVVDPKKEHIAVKEARKLGIPVVAIVDTNCDPDGVDYPIPGNDDAIRSI
KLITSKIADAILEGKQGRKAEAEEEEEEAEEFVEAEEEEAAEA
>gnl|CDD|439823 COG0053, FieF, Divalent metal cation (Fe/Co/Zn/Cd) efflux pump [Inorganic ion transport and metabolism]
GRRAALASLAANLLLAVLKLVAGLLTGSVALLADALHSLSDLVASLLVLLGLRLAAKPADEEHPYGHGKA
EYLASLIVAVLILLAGLFILYEAIERLLHPEPVEPSGLGLAVLLISIVVNEALARYLRRVGKKTGSPALK
ADALHDRSDALTSLGVLIGLLLALLTGWPWLDPIAAILIGLLILKVAYKLARESLSLLMDEALDEELVER
IRAIILSVPGVIGVHDLRTRKSGPRIFVDLHIEVDPDLTVEEAHDIADRIEAALREEFPGVADVTIHVEP
EEDD
>gnl|CDD|439824 COG0054, RibE, 6,7-dimethyl-8-ribityllumazine synthase (Riboflavin synthase beta chain) [Coenzyme transport and metabolism]. 6,7-dimethyl-8-ribityllumazine synthase (Riboflavin synthase beta chain) is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
TIEGDLPASGLRIAIVVARFNEDITDKLLEGALDALKRHGVSEENIDVVRVPGAFEIPLAAKKLAESGRY
DAVIALGCVIRGETPHFDYVANEVTKGLMQVSLDTGVPVGFGVLTTDTIEQAIERAGGKAGNKGAEAALA
ALEMANLLRQLR
>gnl|CDD|439825 COG0055, AtpD, FoF1-type ATP synthase, beta subunit [Energy production and conversion]. FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGM
EVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLL
APYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVF
GQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEM
GALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILD
PLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEQFTGIPG
KYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAEA
>gnl|CDD|439826 COG0056, AtpA, FoF1-type ATP synthase, alpha subunit [Energy production and conversion]. FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDN
VGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQ
PVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVE
TLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRP
PGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFN
AGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGERLVELL
KQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGKLDDEIEEKLK
AAIEEFKKTFAASA
>gnl|CDD|439827 COG0057, GapA, Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]. Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis
MTIRVAINGFGRIGRLVLRALLERGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNG
KKIKVLAERDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDY
DADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTST
GAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPL
VSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSNRMVDLAEYMAKLL
>gnl|CDD|439828 COG0058, GlgP, Glucan phosphorylase [Carbohydrate transport and metabolism]
LALNAEELFRAIDPELWETLGKRLEEAAADDWFLALAAAVRDYLSPRWFQTNRAYPDQKAKRVAYFSAEF
LLGRSLGNNLLNLGLYDEVREALAELGLDLEDLLEQEPDLPLGNGGLGRLAADFLKSASDLGLPAVGYGL
RYEYGYFRQRIDDGWQVERPDNWLRYGDPWELPRPEPAVEVKFGDEDGRTEDVLAVPYDVPIPGYRNNTV
NTLRLWKAEASEEVGLYLFDAGDYTDAVENKPEDRNITKVLYPGDSEEAGKELRLRQEYFLGSGGVRDLR
RLHLKTGGDLDGLPEPVVIHLNDTHPAFAILELMRLLVDEHGLSWDEAWEITRATFVFTNHTPVPEALER
WPVDLFERLLPRHLEIIGEINRRFLEEVRARPGDRERLLRLGIIDEGQFRMAHLALRGSHSVNGVSALHG
EVLRETMFADFYPLWPVPFTNVTNGVHPRRWLLLANPELAELITEYIGDGWITDLELLEKLEPIADDPAF
QEELWEVKQANKERLAAYIRERTGIVLDPDALFDGFAKRFHEYKRQLLNLLHDIERYNRILNNPNLDERP
RQFIFAGKAAPGDEMGKLIIKLINAVARVPNNDPRVEFRLKVVFLENYDVSLAEKLVPGADVWEQIPTAG
KEASGTSGMKFALNGALTLGTLDGANVEIYEEVGDENGFAFGLTAEEVEALRAKYNPRDYYEADPELRRV
LDQLASGYFSPDPEEFRALYDLLLGGDPYLVLADFASYVDAEEEVDPLYRRPERWVRMMILNIARLGKFS
SDRMIREYAERIWKLPAADNALARE
>gnl|CDD|439829 COG0059, IlvC, Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]. Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
MAKIYYDKDADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGSKSWKKAEEDGFEVMTVAEA
AKRADVIMILTPDEVQAAVYEEEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRRE
YEEGFGVPALIAVHQDATGKAKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAG
FETLVEAGYQPEMAYFECLHELKLIVDLIYEGGIANMRYSISNTAEYGDYTRGPRVITEEVKEEMKKVLD
DIQSGEFAKEWILENQAGRPNLNALRAEEAEHPIEKVGAELRAMMPWL
>gnl|CDD|439830 COG0060, IleS, Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
YKETLNLPKTDFPMRANLPKREPEILKFWEENDIYEKSREARAGRPKFVLHDGPPYANGDIHIGHALNKI
LKDIIVRYKTMRGFDVPYVPGWDCHGLPIELKVEKELGIKKKDIEKVGIAEFREKCREYALKYVDEQRED
FKRLGVWGDWDNPYLTMDPEYEESIWWALKKLYEKGLLYKGLKPVPWCPRCGTALAEAEVEYKDVTSPSI
YVKFPVKDEKALLLLEDAYLVIWTTTPWTLPANLAVAVHPDIDYVLVEVTGGERLILAEALVEAVLKELG
IEDYEVLATFKGAELEGLRYEHPFYYVVGYDRAHPVILGDYVTTEDGTGIVHTAPGHGEDDFEVGKKYGL
PVLNPVDDDGRFTEEAPLFAGLFVKDANPAIIEDLKERGALLAREKITHSYPHCWRCKTPLIYRATPQWF
ISMDKLRDRALEAIEKVNWIPEWGEGRFGNMLENRPDWCISRQRYWGVPIPIWVCEDCGELHRTEEVIGS
VAELLEEEGADAWFELDLHRPFLDETLKCPKCGGTMRRVPDVLDVWFDSGSMHFAVLENREELHFPADFY
LEGSDQTRGWFYSSLLTSTALFGRAPYKNVLTHGFVLDEDGRKMSKSLGNVVDPQEVIDKYGADILRLWV
ASSDYWGDLRFSDEILKEVRDVYRRLRNTYRFLLANLDDFDPAEDAVPYEDLPELDRWILSRLNELIKEV
TEAYDNYDFHRAYRALHNFCVEDLSNWYLDISKDRLYTEAADSLDRRAAQTTLYEVLETLVRLLAPILPF
TAEEIWQNLPGEAEESVHLADWPEVDEELIDEELEAKWDLVREVRSAVLKALEAARKEKLIRQPLEAAVV
LYADEELAAALESLGDLLAEELNVSEVELVDDAEDLGKDALKALDVEGISVTVEVEKADGEKCERCWHYE
VGWTPEHEGLCRRCVRRVQGL
>gnl|CDD|439831 COG0061, NadK, NAD kinase [Coenzyme transport and metabolism]
MKRIAIVAKPGKPEALEAAEELAELLEERGIEVVLDEDTAVPGVPLEELGEEADLVIVLGGDGTLLRAAR
LLAPLGIPILGINLGRLGFLTEIEPEELEEALERLLAGEYEVEERLLLEATVDRDGEVVHEALALNEVVV
LRGSIARMIELEVYIDGEFLEEFRGDGLIVSTPTGSTAYNLSAGGPIVHPGLDALVLTPIAPHTLSSRPL
VLPDDSEIEIEVLEDSRPAVLVADGQEVRDLEPGDRVEIRRSPKPVRLLRLKDHSFFERLREKLGWGGD
>gnl|CDD|439832 COG0062, Nnr1, NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism]
MKLLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPSAARRVLVLCGPGNNGGDGLVAARLL
AEAGYNVTVFLLGDPEKLSGDAAANLERLKAAGIPILELDDELPELAEADLIVDALFGTGLSRPLRGPYA
ELIEAINASGAPVLAVDIPSGLDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGI
PAAAEAPAALLLLADLLALLLPPRRRSHHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPP
AAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLL
LALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAVAAAAVVAGAAGVVVVAAAGG
GGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLAAAAALIALLL
AAALLLLLA
>gnl|CDD|439833 COG0063, Nnr2, NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism]
DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVA
AALPELMVIPLPEEDELLELLERADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPEL
LAALPAPTVLTPHPGEFARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGN
PGLATAGSGDVLAGIIAGLLAQGLDPFEAAAAGVYLHGLAGDLAAEERGRGLLASDLIEALPAALRELLE
>gnl|CDD|439834 COG0064, GatB, Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit [Translation, ribosomal structure and biogenesis]. Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MKYEVVIGLEVHVQLNTKSKIFCGCSTEFGAEPNTNVCPVCLGLPGALPVLNKKAVEYAIKAGLALNCEI
AERSKFDRKNYFYPDLPKGYQISQYDLPICEGGYLEIEVEDGEEKRIGITRIHLEEDAGKSIHEGGAGYS
LVDYNRAGVPLIEIVSEPDMRSPEEARAYLEKLRSILRYLGVSDGNMEEGSLRCDANVSVRPKGSEELGT
RVEIKNLNSFRFVERAIEYEIERQIELLESGGKIVQETRLWDEDKGETRSMRSKEEAHDYRYFPEPDLPP
LVISDEWIEEIRATLPELPDAKRERFVEEYGLSEYDARVLTSDKELADYFEAAVKAGADPKLAANWIMGE
LLRRLNERGLEIEESPVTPEQLAELIKLIDDGTISGKIAKEVFEEMLETGGDPEEIVEEKGLKQVSDEGA
LEAIVDEVLAANPDAVEDYKAGKEKALGFLVGQVMKATKGKANPKLVNELLKEKLGG
>gnl|CDD|439835 COG0065, LeuC, Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism]. Homoaconitase/3-isopropylmalate dehydratase large subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
MGMTLAEKILARHAGREVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVAVFDHNVPTK
DPKSAEQVKTLREFAKEFGITFFDVGDPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTT
DVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERM
TLCNMAIEAGAKAGIIAPDETTFEYLKGRPFAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVV
PVSELEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAG
AEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSPGSRTYLASPATAAASAIAGRITDPREL
>gnl|CDD|439836 COG0066, LeuD, 3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]. 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
EKFTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRYDRSPDPDFVLNQPRYQGADILVA
GRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAIEANPGDELTV
DLEAGTVTNGTGETYPFEIDPFRRECLLNGLDDIGLTLKHADAIAAFEAKRPAWL
>gnl|CDD|439837 COG0067, GltB1, Glutamate synthase domain 1 [Amino acid transport and metabolism]. Glutamate synthase domain 1 is part of the Pathway/BioSystem: Glutamine biosynthesis
MTENSGLPAAQGLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILI
QIPDAFFRAEAAELGIELPEPGEYAVGMVFLPQDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLG
ETARATEPVIEQVFVARPDGLDGDAFERKLYVARKRIEKAIRALGLDDEDFYICSLSSRTIVYKGMLTPE
QLGEFYPDLQDPRFESALALVHQRFSTNTFPSWPLAQPFRYLAHNGEINTLRGNRNWMRAREALLASPLF
GDDLEKLLPIVNPGGSDSASLDNVLELLVLGGRSLPHAMMMLIPEAWENNPDMDPERRAFYEYHSALMEP
WDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIPPEDIVEKGRLQPGKMLLVDLE
EGRIIDDEEIKAELAAAHPYGEWLKENRIRLEDLPEPEEEPAPDDDLLLRRQQAFGYTEEEELLLLLPMA
AGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLLEEEEA
RRRLLLLPPPLLNELLLLLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAEAAAAAAAAAVLLILII
DLSDDDSDAAPAPLAAAAAAHHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALEL
LLDGLLLGLEDAAAAAAAKKKKKKKKGKLKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGG
GGGGGGLDEEAEEEAARAAAAAAEPGGLLLGLGGGGGGEYGRRREGELHLLLQAATAAAAAAYRAYKYYR
FARYTALLDLLRLLLLLLLLLFEEEEEEEEPEEEEEEEESSAIAAASSAAASAAASAAAAAAAAGAGGGG
GGGGGGGGGGGEGRRASGGSGSSSSASVAAAGGGVVVGAGAAAAEGGGGGGGGGGGGGGGGGGGGGGVPG
IAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVVVAAAAGVAAAAAAAAAAAAVG
SSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLGGGGGGGGGAAALGAGALGG
GAAALVVVGCGVAMCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALLELLRLLEEG
LGVVELLLLLLLLLLLAKLLLLLLLLLLPLLPPDDPRDLALEEDDELLLLLALLLLLLALALALLAAVRV
ALRAALGRARRRGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG
GGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGAGGGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGG
GGGGGGGGGGGGGGGGGGGGGGGGGGLDLDVVLDEEEEEELEELLLLLEEEEEEELELEEEEAELLELAD
AALLLLLLVKVKAAVKVLLLLLLAAAAAAAEAAAAAAAAAEAAAAAAAEA
>gnl|CDD|439838 COG0068, HypF, Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, protein turnover, chaperones]
MKRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGEEEALEAFLEALRAEAPPLARID
SIEVEELPPEGFDGFRILESEAGGGGRTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIR
ALPYDRPNTSMAAFPMCPDCAAEYEDPADRRFHAQPNACPVCGPQLWLLDADGKPLAEGDDAIAAAAELL
RAGKIVAIKGLGGFHLACDATNEEAVARLRRRKRRPAKPFAVMARDLETARRLCEVSEAEEALLTSPARP
IVLLPKRPDSPLAPSVAPGLDTLGVMLPYTPLHHLLLDELGRPLVMTSGNLSGEPICIDNEEALERLSGI
ADYFLLHNRPIVNRVDDSVVRVIDGKPRFLRRARGYAPLPIPLPFELPPVLALGAELKNTFCLAKGDQAF
LSQHIGDLDNLETLEAFEETIEHLLRLYDVRPEVIACDLHPDYLSTRLAEELAERGLPLIEVQHHHAHIA
AVMAEHGLDGPVLGIALDGTGYGDDGTIWGGEFLLGDYAGFERVGHLRPFPLPGGDKAAREPWRMALALL
YEAGGEELLEPLLKRFSEKELALLRQMLERGINSPLTSSAGRLFDAVAALLGICDEISYEGQAAMELEAL
ADRAEEAEPYPFPLREIDGLLVLDWAPLLRALLEDLQAGVPPAEIAARFHNTLAEAIAELALRLAERTGI
DTVALSGGVFQNRLLLELLRARLEAAGFKVLLHRQVPPNDGGISLGQAAIAAARLEG
>gnl|CDD|439839 COG0069, GltB2, Glutamate synthase domain 2 [Amino acid transport and metabolism]. Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis
LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGGLLGLDLEEA
VKNYIKAIEKGLLKIMSKMGISTLASYRGAQIFEAVGLSRELVDIGIADVLTQHRHAILRNLPVGGRYRY
RFESIGPEIRQYFFESDGEEHPFNRETRSLLYQAAKNEEDYKPFGTLVDYQPGYEWTLRSLFPFKADRPP
IPIGEPVEPPYSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESPYHLGDGGGDAIKQIA
SGRFGVRDEDGEYLPNAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIE
DLAQLIFDLRELNPGAPVGVKLVSGAGVGTIAACKGVAKTGAYADFITIDGGEGGTGAAPLESIKHAGLP
WELGLAEVHQTLVGNGLRDRIRLIADGKLKTGRDVAIAAALGADEFGFARAFMVALGCIMARKCHLNTCP
VGVATQDPELRKGFVVEGKPERVVNYFRFTAEEVREILAALGVRSPDELIGRHDLLRVRDGEHWKAKGLD
LSPLLYKPELPEGVPRRCQEEQDHGLDKALDLELIAAAAAAAEEGKPVVLITNIRNNNRRVGGMLSGEIA
KRYGGAGLPDDTIILGFAGGAGQSFGAFGAGGGLLLLEGDDNDYVGKGGGGGGIIVPPPPGASFFPEENI
IIGNTGLYGATGGGAYFAGGAGERFAVR
>gnl|CDD|439840 COG0070, GltB3, Glutamate synthase domain 3 [Amino acid transport and metabolism]. Glutamate synthase domain 3 is part of the Pathway/BioSystem: Glutamine biosynthesis
GGGAGAMGAAAAAGGGGGGGGAGGDGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGG
GGGGGGGGGGGLGALLAGGGAFFAAGLAAGLLALAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLL
ALGVRAAALARREAELSELAARRRLRLRRLALLRRRRRRRRREFRRRSSSSLSSSSSSLYSLLLLVLLLL
LLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFFAPRTLAANNNNNNNNNNNNNNNRNAILNLSSRLEALS
LELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAAPAPRAAAPPAAAAAFAAAADLYAAAAA
AAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKGRELPGGGLLVGGGGGGL
LDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLLLLLLAEALEE
EEESGGAGAAAAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELL
LLELLLLLLALALLLLLLLLLLLLGDATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIR
DSALLLALLPALLALLLLHHHLLRALGRVLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALL
LLAYALLGLLEAAAYKAKAALKAGVKKKLKIGGSSISSSSGGGIIEGAGGGLGLLLELGGTTTTVGEGGG
GGEILGEGGAARHAAAADAAAAAALALGGGGGGGRGGGGEGHHGGHYHHLLQQLAARTAAALYDDYYAYE
DRADELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRFATGAMSGGSSSSEAHEELAIAMNRIGGKSNGG
GGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMAQGAKPGEGGQLPGHKVYPWIAR
LRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGVAKAAADVILISG
HDGGTGASPLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATA
PLVVLGCIMMRKCHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRR
DLLLVRRAVDHWKAKGLDLSPLLYKPDVPADVPRYCTEEQNHGLEGALDRELIEDARPAIENGEPVELEY
PIRNTDRSVGTRLSGEIAKRYGNEGLPEDTITLRFTGSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGG
KIIVRPPAGSTFVAEENIIIGNTCLYGATGGELYAAGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGVV
VVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMVELERLDEEEDEEELRELIEEHVEYTGSARAKEI
LDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAGLDADE
>gnl|CDD|439841 COG0071, IbpA, Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]
MVDIEETDDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEEEEEEGENYLRRERRYGSFERSFTLPDD
VDVDKIEASYENGVLTITLPKAEEAKPRKIEIKAG
>gnl|CDD|439842 COG0072, PheT, Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]. Phenylalanyl-tRNA synthetase beta subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MKLSLLWLLLLVEEAALLEELLLLLTGEGLEEEEVEGAAAVVVGVVVVVVVVEEPHPDADDLVVVVVDVG
GGEVLVVVCGAANVAVGVVVVAAPGGAVLPGGFKIKKAKIRGVESSGMLCSEEELGLGEDHDGIIVLPPD
APVGGDAREYLGLDDTVLEIDLTPNRADCLSVRGVARELAALLGAPLKLPAIEPEVPPAIDDPIPVEIED
PEACPRYAGRVIRGVKVGPSPLWMQERLRAAGIRPINNVVDITNYVMLELGQPLHAFDLDKLKGGIVVRR
AREGEKLTTLDGKERTLDPDDLVIADDEGPLALAGVMGGEDSEVTEETTDVLLESAYFDPVSIRRTARRL
GLHSDASYRFERGVDPALTVAALERATQLILEIAGGEVGPGIVDVYPEPPEPKTITLRLARINRLLGVEI
PAEEIEEILERLGFEVEEDGDGLTVTVPSWRFDIEIEADLIEEVARIYGYDNIPSTLPRAPLAGGGLTEA
QRLRRRVRRALAARGYQEVITYSFVSPEDADLFGLRREAVRLANPISEDLSVMRTSLLPGLLEAAAYNLN
RGQKDVRLFEIGRVFLPDEGEEPREPLHLAGVLTGNREPESWGGKARPVDFFDLKGDVEALLAALGVPKL
EFEAAEHPALHPGRSAEILLGGKVIGFIGELHPKVLKALDLPGPVYVFELDLDALLELARKVPKYKPISK
FPAVRRDLALVVDEDVPAADVLDAIRKAAGKLLEDVRLFDVYEGKGVPEGKKSLAFSLTLQDPDRTLTDE
EIDAAMDKIVAALEKKFGAELRG
>gnl|CDD|439843 COG0073, EMAP, tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis]
MKVSLSWLKEYVDLDLSPEELAEKLTMAGIEVEDFEKVGGLDGLRVGKVLEAEPHPNADKLLVLQVDVGE
ETRQIVCGAPNVYAGDKVPEALVGAQVPGVVNLKPRKIRGVESEGMLCSAEELGLGEDHDGILELPEDAP
PGDDAEYLLLLDDVIIEILTTPNRDDLLSVGGAAREAAALGGLLLKPPAPPVVEGTDDAVLVVVVDDDAC
DRYYGRVVRGVVNVVVPPPPWLRRLLRRGGRRRIINVVDINNVVLLLLGQPHHAFDDDDLGGGIVVRRRR
AEELLLLLLGDTTLLLDDLLLIDDDDDALAAAGGGGGGGGSSGSTTTTTLLLAAAAFFAAAGRRRRRRRL
SSRSSRRRRREDDDDPRVAAAAAAAALLLIILGGGGGVAGGVVDEGLPPPPPRIIRLRRRRRLLLLGIDI
DEEELLLLLLLLGFEVEGEGESVVVPPPRRRDDVIEEDEEEEEARRYYYYDLPPPPPPAPPAVPEPPAAR
RRLRRRRRLLLLLGLEEAVTYSSFSELLLALLLLFEAALLLLLPPSSLSSSLLLSLLLLLLLLVLLLLRR
RNRNRRLFEGGEVFFGFEGGGLELLLAELEAGGALLLGGGGGAALGLAADDADDLAGVLLLLALLLGLLA
LLALAAAAPAAAAPGAGGAGGLLLGGGGGLGGLLPVLLKLLLLLLLALLFEVLLDELLLPAAVLLALPLV
ARPLLRAIVVDVAAAVAAALAAVAAALALVVALLAVVLLVVVVDVGVGKVLKKLLLSLDLEVTLLDLEEL
ELT
>gnl|CDD|439844 COG0074, SucD, Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]. Succinyl-CoA synthetase, alpha subunit is part of the Pathway/BioSystem: TCA cycle
SILVNKNTRVIVQGITGKEGSFHTKQMLAYGTNVVAGVTPGKGGQTVLGVPVFDTVAEAVEETGADASVI
FVPPPFAADAILEAIDAGIKLIVCITEGIPVLDMVRVKRYAKAKGTRLIGPNCPGIITPGECKLGIMPGH
IFKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELFEEDPETEAIVMIGEIG
GSAEEEAAEYIKENMTKPVVAYIAGRTAPPGKRMGHAGAIISGGKGTAESKIEALEAAGVPVAESPSEIG
ELLKKALK
>gnl|CDD|439845 COG0075, PucG, Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]. Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis
RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTENDVVILTGSGTGAMEAALANL
VSPGDKVLVLVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVHNETSTGV
LNPLEEIGALAKEHGALLIVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEA
RKLPSYYLDLKLWLKYWEKGQTPYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLE
LFAEEEYRSPTVTAVRVPEGVDAAALRKRLKERYGIEIAGGLGPLKGKIFRIGHMGYVNPEDVLRTLAAL
EEALRELGVPVELGAGVAAAQEVLAE
>gnl|CDD|439846 COG0076, GadA, Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]. Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
EFRALLHQALDLAADYLAGLDRPVFGPSPEELRAALDEPLPEEGLPPEEALAELEDLVLPGSVDWNHPRF
LAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLPEGAGGVFTSGGTEANLL
ALLAARDRALARRVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAA
IDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERAD
SITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPADDGVPNLGDYTLELSRRFRALKLWATLRA
LGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCFRYKPAGLDEEDALNYALRDRLRARGRA
FLSPTKLDGRVVLRLVVLNPRTTEDDVDALLDDLREAAAE
>gnl|CDD|439847 COG0077, PheA2, Prephenate dehydratase [Amino acid transport and metabolism]. Prephenate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
MMRIAYLGPEGTFSHQAARKYFGPDAELVPCPSFEDVFEAVESGEADYGVVPIENSIEGSVNETLDLLLE
SDLKIVGEVVLPIHHCLLARPGTKLEDIKTVYSHPQALAQCREFLREHLPGAELVPVSSTAAAARLVAEE
GDPGAAAIASELAAELYGLEVLAENIEDNPNNTTRFLVLGREPAAPTGADKTSLVFSLPNRPGALYKALG
VFATRGINLTKIESRPIKGGLWEYVFFIDVEGHIDDPRVAEALEELKRLTEFLKILGSYPRADL
>gnl|CDD|439848 COG0078, ArgF, Ornithine carbamoyltransferase [Amino acid transport and metabolism]. Ornithine carbamoyltransferase is part of the Pathway/BioSystem: Arginine biosynthesis
TNLKGRHFLSLLDLTPEELRALLDLAAELKAKRKAGIPHRPLKGKTLAMIFEKPSTRTRVSFEVGMAQLG
GHAIYLDPGDSQLGRGESIKDTARVLSRYVDGIMIRTFGHETLEELAKYAGVPVINGLTDLFHPCQALAD
LLTIREHFGKLKGLKVAYVGDGNNVANSLLLAAAKLGMDVRIATPEGYEPDPEIVAKAKEIAAESGGSIT
ITHDPAEAVKGADVVYTDVWVSMGQEEEAEERIKAFKPYQVNEELMALAKPDAIFMHCLPAHRGEEVTDE
VIDGPQSVVFDEAENRLHAQKALLAWLLGG
>gnl|CDD|439849 COG0079, HisC, Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid transport and metabolism]. Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
SPYVPGGPIEEPEDIIKLSSNENPYGPPPKVLEAIAAALDALNRYPDPDATALREALAEYYGVPPEQVLV
GNGSDELIQLLARAFLGPGDEVLVPEPTFSEYPIAARAAGAEVVEVPLDEDFSLDLDALLAAITERTDLV
FLCNPNNPTGTLLPREELEALLEALPADGLVVVDEAYAEFVPEEDSALPLLARYPNLVVLRTFSKAYGLA
GLRLGYAIASPELIAALRRVRGPWNVNSLAQAAALAALEDRAYLEETRARLRAERERLAAALRALGLTVY
PSQANFVLVRVPEDAAELFEALLERGILVRDFSSFGLPDYLRITVGTPEENDRLLAALKEI
>gnl|CDD|439850 COG0080, RplK, Ribosomal protein L11 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L11 is part of the Pathway/BioSystem: Ribosome 50S subunit
MAKKVKGVIKLQVPAGKANPAPPVGPALGQHGVNIMEFCKEFNAKTKDEKGMIVPVVITVYSDRSFTFIV
KTPPASVLLKKAAGIEKGSGEPNKEKVGKITREQVREIAEIKMPDLNAKDLEAAVKIIAGTARSMGITVE
G
>gnl|CDD|439851 COG0081, RplA, Ribosomal protein L1 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L1 is part of the Pathway/BioSystem: Ribosome 50S subunit
MAKLSKRYKAAAEKVDRNKLYSLEEAVELVKETATAKFDETVEVAVRLGVDPRKADQMVRGTVVLPHGTG
KTVRVAVFAKGEKAEEAKAAGADYVGAEDLIEKIQGGWLDFDVVIATPDMMGKVGKLGKILGPRGLMPNP
KTGTVTMDVAKAVKEAKAGKVEFRVDKAGIIHAPIGKVSFDAEKLKENLKALLDALIKAKPASAKGTYIK
KITLSSTMGPGVKVDP
>gnl|CDD|439852 COG0082, AroC, Chorismate synthase [Amino acid transport and metabolism]. Chorismate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
FGKLFRVTTFGESHGPALGAVIDGCPAGLPLDEEDIQRELDRRRPGYSRGTTQRKEKDEVEILSGVFEGK
TTGTPIALLIENTDQRSKDYSEIKTRPRPGHADLTYALKYGFRDYRGGGRSSARETAARVAAGAIAKKLL
AELGIEIRSYVVQIGGIKAEEEELDLEEIEANPVRCPDPEAAEEMEALIDEARKEGDSLGGVVEVVATGV
PAGLGEPVFDKLDARLAKALMSIPAVKGVEIGDGFEAARMRGSEVNDEITPDGGGIRRKTNNAGGILGGI
SNGEPIVVRVAFKPTPSIPKPQRTVDLETKEPTELATKGRHDPCVVPRAVPVAEAMVALVLADALLEKFG
GDSD
>gnl|CDD|439853 COG0083, ThrB, Homoserine kinase [Amino acid transport and metabolism]. Homoserine kinase is part of the Pathway/BioSystem: Threonine biosynthesis
KSVKVRVPATSANLGPGFDSLGLALSLYDEVEVERSDEPGLEIEIEGEGADELPTDEDNLVYQAALALLE
KLGKEPPGLRIEIEKGIPLGRGLGSSAAAIVAGLVAANALLGLPLSKEELLELATEGEGHPDNVAPALLG
GLVLSRSDGEPVRVVRLPVPPDLKAVVVIPDFELSTKEARAVLPKQVPLKDAVFNSSRAALLVAALATGD
YELLGRAMEDRLHEPYRAKLIPGFDEVKEAALEAGALGAGISGAGPTVLALADDEEAEAVAEAMKAAFAE
AGIDARVYVLKIDNEGARVLES
>gnl|CDD|439854 COG0084, TatD, 3'-_5' ssDNA/RNA exonuclease TatD [Cell motility]
LIDTHCHLDFPEFDEDRDEVLARARAAGVERIVVVGTDLESSERALELAERYPNVYAAVGLHPHDAKEHD
EEDLAELEELAAHPKVVAIGEIGLDYYRDKSPREVQEEAFRAQLALAKELGLPVIIHSRDAHDDTLEILK
EEGAPALGGVFHCFSGSLEQAKRALDLGFYISFGGIVTFKNAKKLREVAAAIPLDRLLLETDAPYLAPVP
FRGKRNEPAYVPHVAEKLAELRGISLEELAEATTANARRLFGL
>gnl|CDD|439855 COG0085, RpoB, DNA-directed RNA polymerase, beta subunit/140 kD subunit [Transcription]. DNA-directed RNA polymerase, beta subunit/140 kD subunit is part of the Pathway/BioSystem: RNA polymerase
RWSFAKIKEPLELPNLLEIQLDSFNWFLEEGLQEIFDEISPIEDFTGNLSLEFGDYRLGEPKYTPEECKE
RDLTYAAPLYVKVRLVNKETGEIKEQEVFMGDFPLMTDSGTFIINGTERVIVSQLVRSPGVYFVEEEDKS
GKDLYSAKVIPSRGAWLEFETDKDGTIYVRIDRKRKIPVTVLLRALGLETDEEILEAFGDDPIQEYILAT
LEKDNTKTQEEALLEIYRKLRPGEPPTIERAEQLLDNLFFDPKRYDLAHVGRYKINKKLGLDVPPEDRVL
TAEDIVATIKYLLELHLGEREPDDIDHLGNRRVRLVGELLQNQFRVGLSRMERVVRERMTTQDVEAITPQ
SLINIRPVVAAIKEFFGSSQLSQFMDQTNPLSELTHKRRLSALGPGGLSRERAGFEVRDVHPSHYGRMCP
IETPEGPNIGLIGSLALYARVNEYGFIETPYRKVENGKVTDEIEYLTADEEENYYIAQANAPLDEDGNFL
EERVLVRYRGEEVLVPPEEVDYMDVSPKQIVSVATSLIPFLEHDDANRALMGANMQRQAVPLLRPEAPLL
HYPLQKFQRSNQGTCINQRPIVRVGDRVEKGDVLADGPATDNGELALGQNLLVAFMPWEGYNYEDAIIIS
ERLVKDDVLTSIHIEEYEIEARDTKLGPEEITRDIPNVSEEALRNLDEDGIIRIGAEVKGGDILVGKVTP
KGETELTPEERLLRAIFGEKAREVRDTSLRVPHGEKGKVIDVKVFSREEGDELPPGVNKLVRVYVAQKRK
IEVGDKLAGRHGNKGVISRILPQEDMPFLEDGTPVDIVLNPLGVPSRMNVGQVLETHLGWAAALLGRRVA
TPVFDGAPEEEIRELLEKAGLPPDGKEVLYDGRTGEPFDNPVTVGYMYYLKLHHMVDDKIHARSTGPYSL
ITQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQERLTIKSDDVCGRVKVYEAIVKGENIPEPGIPESF
KVLLKELQSLGLDVEVLSEDG
>gnl|CDD|439856 COG0086, RpoC, DNA-directed RNA polymerase, beta' subunit/160 kD subunit [Transcription]. DNA-directed RNA polymerase, beta' subunit/160 kD subunit is part of the Pathway/BioSystem: RNA polymerase
MAFVEDFDAIKIGLASPEKIRSWSYGEVKKPETINYRTFKPERDGLFCERIFGPCKDYECYCGKYKRMVY
KGVVCEKCGVEVTLSKVRRERMGHIELAMPVFHIWGLKSLPSRIGLLLDMSLRDLERVLYFESYVVIDPG
DTPLEKGQLLTEDEYREILEEYGDEFVAKMGAEAIKDLLGRIDLEKESEELREELKETTSEQKRKKLIKR
LKVVEAFRESGNRPEWMILDVLPVIPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLLELKAPDI
IVRNEKRMLQEAVDALFDNGRRGRAVTGANKRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPE
LKLHQCGLPKKMALELFKPFIYRKLEERGLATTIKSAKKMVEREEPEVWDILEEVIKEHPVLLNRAPTLH
RLGIQAFEPVLIEGKAIQLHPLVCTAFNADFDGDQMAVHVPLSLEAQLEARLLMLSTNNILSPANGKPII
VPSQDMVLGLYYLTREREGAKGEGMIFADPEEVLRAYENGAVDLHARIKVRITEDGEQVGKIVETTVGRY
LVNEILPQEVPFYNQVINKKHIEVIIRQMYRRCGLKETVIFLDRLKKLGFKYATRAGISIGLDDMVVPKE
KQEIFEEANKEVKEIEKQYAEGLITEPERYNKVIDGWTKASLETESFLMAAFSSQNTTYMMADSGARGSA
DQLRQLAGMRGLMAKPSGNIIETPIGSNFREGLGVLEYFISTHGARKGLADTALKTADSGYLTRRLVDVA
QDVIVTEEDCGTDRGITVTAIKEGGEVIEPLKERILGRVAAEDVVDPGTGEVLVPAGTLIDEEVAEIIEE
AGIDSVKVRSVLTCETRGGVCAKCYGRDLARGHLVNIGEAVGVIAAQSIGEPGTQLTMRTFHIGGAASRA
AEESSIEAKAGGIVRLNNLKVVVNEEGKGVVVSRNSELVIVDDGGRREEEYKVPYGGVLVVVGGGVVVGG
GIVAEWDPHTPPIIEEVGGGVVFDDIVEGGVIVEKTDEETGGLSIVVEDDKARRGGGKLLIRALKLLDAV
GLSLLLGGTDAAAAGVIIGGLDVVLGDGVAIGVGAAIARIPGLSGGTRDGTGGLARVAAAAEAKEAKEIA
AGAEIIGGVGFGKKTKKKRRLVITEEDGSPIEEEVVKKKRILVVE
>gnl|CDD|439857 COG0087, RplC, Ribosomal protein L3 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L3 is part of the Pathway/BioSystem: Ribosome 50S subunit
MMKGLLGKKVGMTQVFDEDGVVVPVTVIEAGPCVVTQVKTYEKDGYGAVQLGFGEKKEKRVTKPLLGHFK
KAGVEPKRYLREFRVDDVEEYEVGQEIKVDVFEAGQKVDVTGTSKGKGFQGVIKRHGFKGGPASHGSSKS
HRAPGSIGARQTPGRVFKGKKMAGHMGNERVTVQNLEVVKVDAERNLLLVKGAVPGPKGGLVIIRPAVKP
KKKK
>gnl|CDD|439858 COG0088, RplD, Ribosomal protein L4 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L4 is part of the Pathway/BioSystem: Ribosome 50S subunit
MKLDVLNLDGKKVGEVELSDAVFGIEPNEHLLHQVVVAQLANARQGTHKTKTRSEVSGGGKKPWRQKGTG
RARQGSIRSPQWRGGGVVFGPKPRDYSQKLNKKMRRLALRSALSAKAREGRLIVVDDFSLDAPKTKELAA
LLKALGLEGKVLIVLDEVDENLYLSARNLPNVKVLPADGLNVYDLLNADKLVLTKAALEKLEERLA
>gnl|CDD|439859 COG0089, RplW, Ribosomal protein L23 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L23 is part of the Pathway/BioSystem: Ribosome 50S subunit
KRPVITEKSTALAEKNNKYTFEVAPDANKTEIKKAVEKLFGVKVEKVNTLNVKGKKKRFGRRVGKRSDWK
KAIVTLAEGQKIDFFEGV
>gnl|CDD|439860 COG0090, RplB, Ribosomal protein L2 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L2 is part of the Pathway/BioSystem: Ribosome 50S subunit
MAIKKYKPTTPGRRFMVVVDFSELTKGKPEKSLLEPLKKSGGRNNQGRITVRHRGGGHKRKYRIIDFKRN
KDGIPAKVARIEYDPNRSARIALLHYADGEKRYILAPKGLKVGDTVVSGEDADIKPGNALPLKNIPVGTI
VHNIELKPGKGGQLARSAGTSAQLMAKEGKYATLRLPSGEVRKVLAECRATIGQVGNSDHENISLGKAGR
SRWLGIRPTVRGVAMNPVDHPHGGGEGRTSGGRHPVSPWGKPTKGYKTRKKNKRSDKFIVRRRKKK
>gnl|CDD|439861 COG0091, RplV, Ribosomal protein L22 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L22 is part of the Pathway/BioSystem: Ribosome 50S subunit
MEAKAKLRYVRISPRKARLVADLIRGKKVEEALAILEFSPKKAARIVLKVLKSAIANAENNNGLDVDNLV
VKEIFVDKGPTLKRFRPRARGRATRIRKRTSHITVVVSEK
>gnl|CDD|439862 COG0092, RpsC, Ribosomal protein S3 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S3 is part of the Pathway/BioSystem: Ribosome 30S subunit
MGQKVNPIGFRLGIIKDWDSRWYADKKDYADLLHEDLKIRKYLKKKLKNAGISKIEIERTANRVRVTIHT
ARPGIVIGKKGAEIEKLRKELEKLTGKEVQINIVEVKKPELDAQLVAENIAQQLERRVSFRRAMKRAIQR
AMRAGAKGIKIQVSGRLGGAEIARTEWYREGRVPLHTLRADIDYGFAEAHTTYGVIGVKVWIYKGEVLPK
KEEAAAAEAAEGGKPR
>gnl|CDD|439863 COG0093, RplN, Ribosomal protein L14 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L14 is part of the Pathway/BioSystem: Ribosome 50S subunit
MIQQGTRLKVADNSGAKEVMCIKVLGGSRRRYAGVGDIIVVSVKKATPEGKVKKGQVVKAVVVRTKKEIR
RPDGSYIRFDDNAAVLINDDGEPKGTRIFGPVARELREKGFMKIASLAPEVL
>gnl|CDD|439864 COG0094, RplE, Ribosomal protein L5 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L5 is part of the Pathway/BioSystem: Ribosome 50S subunit
MPRLKEKYKEEVVPALMKKFGYKNVMQVPKLEKIVINMGVGEAVQDKKLLESAVEDLTLITGQKPVVTKA
KKSIANFKLREGMPIGCKVTLRGDRMYEFLDRLINIALPRVRDFRGLSPKSFDGRGNYTLGIKEQIIFPE
IDYDKIDKIRGMDITIVTTAKTDEEARALLKALGFPFRK
>gnl|CDD|439865 COG0095, LplA, Lipoate-protein ligase A [Coenzyme transport and metabolism]. Lipoate-protein ligase A is part of the Pathway/BioSystem: Lipoate biosynthesis
RLIDSGSTDPAFNLALDEALLEEVAEGEDPPTLRLWRNPPTVVIGRFQNVLPEVNLEYVEEHGIPVVRRI
SGGGAVYHDPGNLNYSLILPEDDVPLSIEESYRKLLEPILEALRKLGVDAEFSGRNDIVVDGRKISGNAQ
RRRKGAVLHHGTLLVDGDLEKLAKVLRVPYEKLRDKGIKSVRSRVTNLSELLGTDITREEVKEALLEAFA
EVLGVLEPGELTDEELEAAEELAEEKYSSWEWNYGR
>gnl|CDD|439866 COG0096, RpsH, Ribosomal protein S8 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S8 is part of the Pathway/BioSystem: Ribosome 30S subunit
MSMTDPIADMLTRIRNAQMAGKKEVDVPASKLKGAILKVLKEEGYIKDFEVIEDGKKGKLRVELKYGING
EPVIKGIKRVSKPGLRVYVKKEELPRVLNGLGIAIVSTSKGVMTDKEARKKGVGGEVLCYVW
>gnl|CDD|439867 COG0097, RplF, Ribosomal protein L6P/L9E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L6P/L9E is part of the Pathway/BioSystem: Ribosome 50S subunit
SRIGKKPIPIPAGVEVTIDGNTVTVKGPKGELSRTLHPDVKVKVEDNKLTVTRPSDSKEARALHGTTRAL
INNMVEGVTEGFEKKLEIVGVGYRAQVQGKKLVLSLGYSHPVEYEIPEGITVEVPKQTEIVVKGIDKQLV
GQVAAEIRALRPPEPYKGKGIRYAGEVIRRKEGKKKK
>gnl|CDD|439868 COG0098, RpsE, Ribosomal protein S5 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S5 is part of the Pathway/BioSystem: Ribosome 30S subunit
MAPRKERIEEEESELEEKVVAINRVAKVVKGGRRFSFSALVVVGDGNGRVGVGLGKAREVPEAIRKAIED
AKKNMIKVPLVGGTIPHEVIGKFGAGRVLLKPASPGTGVIAGGAVRAVLELAGIKDVLAKSLGSSNPINV
VRATFDALKQLRSPEEVAALRGKSVEE
>gnl|CDD|439869 COG0099, RpsM, Ribosomal protein S13 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S13 is part of the Pathway/BioSystem: Ribosome 30S subunit
MARIAGVDLPGNKRVEIALTYIYGIGRTTARKILEKAGIDPDKRVGDLTDEEIAKIREVIENNHLVEGDL
RREVRMDIKRLKDIGCYRGIRHRRGLPVRGQRTKTNARTRKGPRKTVGVKKKKKK
>gnl|CDD|439870 COG0100, RpsK, Ribosomal protein S11 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S11 is part of the Pathway/BioSystem: Ribosome 30S subunit
MAKKKKKKTKKKKKKNVPSGIAHIHSTFNNTIVTITDLQGNVIAWSSAGTVGFKGSRKSTPYAAQVAAEK
AAKKAMEHGLKEVEVRVKGPGPGRESAIRALQAAGLEVTSIKDVTPIPHNGCRPPKRRRV
>gnl|CDD|439871 COG0101, TruA, tRNA U38,U39,U40 pseudouridine synthase TruA [Translation, ribosomal structure and biogenesis]. tRNA U38,U39,U40 pseudouridine synthase TruA is part of the Pathway/BioSystem: tRNA modification
MMRIKLTIEYDGTNFHGWQRQPNGRTVQGELEKALSKLLGEPVRVIGAGRTDAGVHALGQVAHFDTPSPI
PPERLVRALNALLPPDIAVLWAEEVPDDFHARFSAKSRRYRYRIYNRPVRSPFLRGYVWHVPRPLDVEAM
NEAAQLLLGEHDFSSFRAAGCQAKSTVRTIYRAEVEREGDLIVFEIEANGFLHNMVRNIVGTLVEVGRGK
LSPEWIKEILEAKDRTRAGPTAPAHGLYLVEVDYPEDFFL
>gnl|CDD|439872 COG0102, RplM, Ribosomal protein L13 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L13 is part of the Pathway/BioSystem: Ribosome 50S subunit
SAKPAEVERKWYVIDAEGKVLGRLASEIAKILRGKHKPTYTPHVDTGDFVIVINAEKVKLTGNKLEQKVY
YRHSGYPGGLKETTARELLAKKPERVIEKAVKGMLPKNKLGRKMLKKLKVYAGAEHPHAAQKPEVLEINA
>gnl|CDD|439873 COG0103, RpsI, Ribosomal protein S9 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S9 is part of the Pathway/BioSystem: Ribosome 30S subunit
MAMKVYYGTGRRKTAVARVRLKPGTGKITVNGKPLEEYFPRETLRMKVLQPLELTGTEGKFDVIVNVKGG
GISGQAGAIRHGIARALVEYDPELRPALKKAGLLTRDPRMVERKKYGLKKARKRPQFSKR
>gnl|CDD|439874 COG0104, PurA, Adenylosuccinate synthase [Nucleotide transport and metabolism]. Adenylosuccinate synthase is part of the Pathway/BioSystem: Purine biosynthesis
NVVVVGAQWGDEGKGKIVDLLAERADVVVRFQGGNNAGHTVVVGGKKFKLHLIPSGILRPGKTCVIGNGV
VLDPEALLEEIDGLEARGVDVRSRLRISERAHLILPYHRALDKAREEARGKKKIGTTGRGIGPAYEDKVA
RRGIRVGDLLDPEVLREKLEELLEYKNFLLEKLYGAEPLDFEELLEEYLEYAERLKPYVADTSELLNEAL
KAGKKVLFEGAQGTLLDIDHGTYPYVTSSNTTAGGACTGSGVGPTKIDRVIGVVKAYTTRVGEGPFPTEL
FDETGERLRERGHEFGTTTGRPRRCGWLDAVALRYAVRINGLTGLALTKLDVLDGLDEIKVCVAYELDGE
RIDEFPASLEDLARCEPVYEELPGWKEDISGIRSFEDLPENARAYVERIEELLGVPISIVSVGPDREQTI
VRR
>gnl|CDD|439875 COG0105, Ndk, Nucleoside diphosphate kinase [Nucleotide transport and metabolism]. Nucleoside diphosphate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
AMERTLVIIKPDAVQRGLIGEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGP
VVAMVLEGENAVAVVRKLMGATNPAEAAPGTIRGDFALSIGENAVHGSDSPESAEREIALFFSEEEIVSY
>gnl|CDD|439876 COG0106, HisA, Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis
IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAK
ATGLPVQVGGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQ
ETSGVDLEELAKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL
GVEGAIVGKALYEGKIDLEEALALAR
>gnl|CDD|439877 COG0107, HisF, Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]. Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis
LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAE
EVFIPLTVGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGWEV
YTHGGRKPTGLDAVEWAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHF
VEVFTEGGADAALAASIFHFGEITIAELKAYLAEAGIPVRL
>gnl|CDD|439878 COG0108, RibB, 3,4-dihydroxy-2-butanone 4-phosphate synthase [Coenzyme transport and metabolism]. 3,4-dihydroxy-2-butanone 4-phosphate synthase is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
MSLSSIEEAIEALRAGKMVIVVDDEDRENEGDLIIAAEFVTPEAINFMARHGRGLICLPLTEERADRLGL
PPMVDRNTDPYGTAFTVSVDAREGVTTGISAADRALTIRALADPDAKPEDFVRPGHVFPLRARPGGVLER
AGHTEAAVDLARLAGLKPAGVICEIMNDDGTMARLPDLEEFAKKHGLKIITIADLIAYRRR
>gnl|CDD|439879 COG0109, CyoE, Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism]
MSSASASSAASLRSTLRDYLALTKPRIILLLLFTALAGMLLAAGGLPDLLLLLLTLLGGALAAGAANALN
NYIDRDIDALMKRTKNRPLPTGRISPREALIFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLW
LKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLEALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLP
VVKGERRTKRQILLYTLLLVPVSLLPYLLGMAGLIYLVVALVLGAWFLYLAVRLYRRPDRKWARKLFKFS
ILYLTLLFLALLVDHLLLL
>gnl|CDD|439880 COG0110, WbbJ, Acetyltransferase, isoleucine patch superfamily [General function prediction only]
MKLLLLFGARIGDGVVIGPGVRIYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPID
DPATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER
>gnl|CDD|439881 COG0111, SerA, Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]. Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis
MKILILDDLPPEALEALEAAPGIEVVYAPGLDEEELAEALADADALIVRSRTKVTAELLAAAPNLKLIGR
AGAGVDNIDLAAATERGIPVTNAPGANARAVAEYALALLLALARRLPEADRAQRAGRWDRSAFRGRELRG
KTVGIVGLGRIGRAVARRLRAFGMRVLAYDPSPKPEEAADLGVGLVDSLDELLAEADVVSLHLPLTPETR
GLIGAEELAAMKPGAILINTARGGVVDEDALLAALDSGRLAGAALDVFEPEPLPADSPLWDLPNVILTPH
IAGSTEEAQERAARQVAENIRRFLAGEPLRNLVN
>gnl|CDD|439882 COG0112, GlyA, Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]. Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis
MLSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDE
VEQLAIERAKELFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVV
SYGVDPETGLIDYDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGL
HPSPVPGADVVTTTTHKTLRGPRGGLILCNEELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFK
EYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPRS
PFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREEVKELCKRFPLYPDL
>gnl|CDD|439883 COG0113, HemB, Delta-aminolevulinic acid dehydratase, porphobilinogen synthase [Coenzyme transport and metabolism]. Delta-aminolevulinic acid dehydratase, porphobilinogen synthase is part of the Pathway/BioSystem: Heme biosynthesis
TTRPRRLRRTPAIRRLVRETRLSPDDLIYPLFVVEGENEREPIPSMPGVYRLSLDLLVEEAEEAVELGIP
AVALFGVPELKDEDGSEAYNPDGLVQRAIRAIKAAVPELVVITDVCLDEYTSHGHCGILDDGYVDNDETL
EVLAKQALSQAEAGADIVAPSDMMDGRVGAIREALDEAGFTDVPIMSYSAKYASAFYGPFRDAAGSAPQF
GDRKTYQMDPANSREALREVALDIEEGADMVMVKPALPYLDIIRRVKDEFDVPVAAYQVSGEYAMIKAAA
QNGWLDEERVVLESLLSIKRAGADGILTYFAKEAARWLKEG
>gnl|CDD|439884 COG0114, FumC, Fumarate hydratase class II [Energy production and conversion]. Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle
MMETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKA
DAIVAAADEVIAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSS
NDTFPTAMHIAAALALEERLLPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEH
GIERIEAALPRLYELALGGTAVGTGLNAHPGFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGA
LKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSIMPGKVNPTQCEALTMVCAQVMGNDAAITFA
GSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEELLERSLMLVTALNPHIGYDK
AAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMTG
>gnl|CDD|439885 COG0115, IlvE, Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]. Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
RLIWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELL
EAIRELVAANGLEDGYIRPQVTRGVGGRGVFAEEYEPTVIIIASPLPAYPAEAYEKGVRVITSPYRRAAP
GGLGGIKTGNYLNNVLAKQEAKEAGADEALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRD
SVIELARELGIPVEERPISLEELYTADEVFLTGTAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTDIVR
GEAED
>gnl|CDD|439886 COG0116, RlmL, 23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]. 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification
FELFATCARGLEALLADELKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDD
LYEGAKAIPWEEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHV
HLLKDRATLSLDTSGESLHKRGYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIA
ANIAPGLNRDFAFEKWPDFDAELWQELREEAEARIKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIE
FEQADFRDLEPPAEPGLIITNPPYGERLGEEEELEALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLK
ASKRRKLYNGGLECRLLQY
>gnl|CDD|439887 COG0117, RibD1, Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and metabolism]. Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
ERYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLE
PCSHHGRTPPCADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMR
TGRPFVTLKLAMSLDGKIATANGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGEN
PPRRVVVDDLLLRPPPALLLVANDAALIIVTVTADAAAALAALAAEAGVVLLLVGGLLLLALLLLLLLLL
LLLLLLLLLLGGGGGLAAAALLAALLLDLLL
>gnl|CDD|439888 COG0118, HisH, Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]. Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis
MMIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAV
AGGKPVLGICLGMQLLFERSEENGDTEGLGLIPGEVVRFPASDLKVPHMGWNTVEIAKDHPLFAGIPDGE
YFYFVHSYYVPPDDPEDVVATTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK
>gnl|CDD|439889 COG0119, LeuA, Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]. Isopropylmalate/homocitrate/citramalate synthases is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
PDRIIIFDTTLRDGEQAPGVSFSVEEKLRIARLLDELGVDEIEAGFPAASPGDFEAVRRIAELGLDATIC
ALARARRKDIDAALEALKGAGVDRVHLFIKTSDLHVEYKLRKTREEVLEMAVEAVKYAKEHGLEVEFSAE
DATRTDPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHNDLGLAVANS
LAAVEAGADQVEGTINGIGERAGNAALEEVVMNLKLKYGVDTGIDLSKLTELSRLVSEITGLPVPPNKPI
VGENAFAHESGIHQDGILKNPETYEPIDPEDVGRERRIVLGKHSGRAAIAYKLEELGIELDDEELQEILE
RVKELADKGKREVTDADLEALVRDVLGEKPFFELESYRVSSGTGGIGGEEVETAAEGNGPVDALDNALRK
ALGKFYPLLLELELADYKVRILDGAVAVVAVV
>gnl|CDD|439890 COG0120, RpiA, Ribose 5-phosphate isomerase [Carbohydrate transport and metabolism]. Ribose 5-phosphate isomerase is part of the Pathway/BioSystem: Pentose phosphate pathway
MTQDELKRAAAEAALEYVEDGMVVGLGTGSTAAYFIDALGERVREGLDIVGVPTSEATAELARELGIPLT
DLDEVDELDLYIDGADEVDPDLNLIKGGGGALLREKIVAAASKRFIVIADESKLVDTLGAFPLPVEVIPF
ARSAVARELEKLGGEPVLREAGGGGPFVTDNGNLILDVHFGRIDDPEALEAELNQIPGVVEHGLFAGLAD
VVLVGTEDGVEVLER
>gnl|CDD|439891 COG0121, YafJ, Predicted glutamine amidotransferase YafJ [General function prediction only]
CRLLGYSGNVPTDLEFLLLDPEHSLVRQSGATREGPHADGWGIGWYEGDGEPRLYRDPLPAWSDPNLRLL
ARPIKSRLVIAHVRKATVGPVSLENTHPFRGGRWLFAHNGQLDGFDRLRRRLAEELPDELYFQPVGTTDS
ELAFALLLSRLRDGGPDPAEALAEALRELAELARAPGRLNLLLSDGERLYATRYTSDDPYPTLYYLTRTT
PDDRVVVVASEPLTDDEGWTEVPPGELLVVRDGLEVEV
>gnl|CDD|439892 COG0122, AlkA, 3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair]
PFDLDATLDDGTWRRLPDGPGVVRMRPGGDALEVELAEAVARLRRLLDLDDDLEAIAALAARDPVLAPLI
ERYPGLRLPRRPDPFEALVRAILGQQVSVAAARTIWRRLVALFGEPIEGPGGGLYAFPTPEALAAASEEE
LRACGLSRRKARYLRALARAVADGELDLEALAGLDDEEAIARLTALPGIGPWTAEMVLLFALGRPDAFPA
GDLGLRRALGRLYGLGERPTPKELRELAEPWRPYRSYAARYLWRS
>gnl|CDD|439893 COG0123, AcuC, Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites biosynthesis, transport and catabolism]
TALIYHPDYLLHDLGPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAAS
LDGGYGQLDPDTPVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAA
IAARYLLAKGLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQDPLYPGTGAADETGEGAGEGSNLNVP
LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELADHCGG
PVVSVLEGGYNLDALARSVAAHLETLLG
>gnl|CDD|439894 COG0124, HisS, Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MMKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVEKEMYTFEDR
GGRSLTLRPEGTAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAE
VIALAADLLKALGLKDFTLEINSRGLPEERAEALLRYLDKLDKIGHEDVLDEDSQRRLETNPLRAILDSK
GPDCQEVLADAPKLLDYLGEEGLAHFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGS
VCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLLLEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQEL
RAAGIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELL
AE
>gnl|CDD|439895 COG0125, Tmk, Thymidylate kinase [Nucleotide transport and metabolism]. Thymidylate kinase is part of the Pathway/BioSystem: Thymidylate biosynthesis
MKGKFIVFEGIDGSGKSTQIKLLAEYLEARGYDVVLTREPGGTPLGEAIRELLLGDNEDMSPRTELLLFA
ADRAQHVEEVIRPALAAGKIVICDRYVDSSLAYQGGGRGLDLEWIRQLNRFATGGLKPDLTILLDVPPEV
ALARARARGGELDRFESEDLEFHERVREGYLELAAKEPERIVVIDASQSIEEVHAEIREALAELLK
>gnl|CDD|439896 COG0126, Pgk, 3-phosphoglycerate kinase [Carbohydrate transport and metabolism]. 3-phosphoglycerate kinase is part of the Pathway/BioSystem: Glycolysis
TLDDLDLKGKRVLVRVDFNVPLDDGKITDDTRIRAALPTIKYLLEKGAKVILLSHLGRPKGKVDPKYSLK
PVAERLSELLGKPVKFVDDCIGEEAEAAVAALKPGEVLLLENLRFHPEEEKNDPEFAKKLASLGDVYVND
AFGTAHRAHASTVGIAKLLPSAAGFLMEKELEALGKALENPERPFVAILGGAKVSDKIGVIENLLEKVDK
LLIGGGMANTFLKAQGYDVGKSLVEEDKIDTAKEILEKAKEKGVKIVLPVDVVVADEFSADAERKVVPVD
EIPDDWMGLDIGPKTIELFAEVIKDAKTVVWNGPMGVFEMEPFAKGTRAVAKAIAESGAFSVVGGGDTAA
AVNKLGLADKFSHVSTGGGASLEFLEGKELPGVEALEDK
>gnl|CDD|439897 COG0127, RdgB, Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism]
KLVFATGNAGKLREIRALLAPLGIEVVSLSDLGLPEPEETGDTFEENALIKARAAAKATGLPALADDSGL
EVDALGGAPGVYSARYAGEGADDEANNEKLLKLLEGVDEDRRARFVCVLALADPDGEPLVFEGEVEGEIA
EEPRGEGGFGYDPIFIPDGYGKTFAELSPEEKNAISHRGRALRKLAEWLKE
>gnl|CDD|439898 COG0128, AroA, 5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]. 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDGG
TLRVTGVGGGLKEPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIES
RGGGYLPLTIRGGPLKGGEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFG
VEVEVEGYRRFTVPGGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEM
GADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELR
KLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLRAEGPVTIDDAECVAKSFPDFFELLES
L
>gnl|CDD|439899 COG0129, IlvD, Dihydroxyacid dehydratase/phosphogluconate dehydratase [Amino acid transport and metabolism, Carbohydrate transport and metabolism]. Dihydroxyacid dehydratase/phosphogluconate dehydratase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
MPKMRSDTVTKGRERAPARALLRATGLTDEDFGKPIIGIANSWNEIVPGHVHLDDLAEAVKEGIRAAGGV
PFEFNTIAVSDGIAMGHEGMRYSLPSRELIADSIETMVNAHCFDGLVCIPGCDKITPGMLMAAARLNIPS
IFVYGGPMLPGKYDGKDLDIVDVFEAVGAYAAGKISDEELKEIERNACPGCGSCSGMFTANTMACLTEAL
GLSLPGSGTIPAVSAERRRLAREAGRRIVELVEKDIKPRDILTREAFENAIAVDMALGGSTNTVLHLLAI
AHEAGVDLTLDDFDRISRRTPHLCDLKPSGKYHMEDLHRAGGIPAVMKELLDAGLLHGDCLTVTGKTLAE
NLADADIDRDQDVIRPLDNPYSPTGGLAILRGNLAPDGAVVKTAGVDESMLVFEGPARVFDSEEEAVEAI
LGGKIKAGDVVVIRYEGPKGGPGMREMLSPTSALKGMGLGKSVALITDGRFSGGTRGLSIGHVSPEAAEG
GPIALVEDGDIITIDIPARTLDLLVSDEELARRRAAWKPPEPRVTSGVLAKYAKLVSSASKGAVTDPP
>gnl|CDD|439900 COG0130, TruB, tRNA U55 pseudouridine synthase TruB, may also work on U342 of tmRNA [Translation, ribosomal structure and biogenesis]. tRNA U55 pseudouridine synthase TruB, may also work on U342 of tmRNA is part of the Pathway/BioSystem: tRNA modification
GILLLDKPAGMTSHDVVQKVRRLLGAKKVGHTGTLDPLATGVLPICLGEATKLSQYLLDADKTYRATIRL
GVETDTDDAEGEVVETSPVPRLTEEEIEAALASFTGEIEQVPPMYSAIKVDGKRLYELARAGEEVERPPR
PVTIYSLELLSFDAPELTLEVTCSKGTYIRSLARDLGEALGCGAHLSALRRTRVGPFTLEDAVTLEELEE
LAEGALDALLLPVDEALADLPAVELDEEEAKRLRNGQRLPLPGLPADGLVRVYDPDGRFLALGEIEDGRL
KPKRVFNL
>gnl|CDD|439901 COG0131, HisB2, Imidazoleglycerol phosphate dehydratase HisB [Amino acid transport and metabolism]. Imidazoleglycerol phosphate dehydratase HisB is part of the Pathway/BioSystem: Histidine biosynthesis
ETDISVELNLDGTGKSDISTGVGFFDHMLEQFARHGLFDLTVKAKGDLHVDDHHTVEDVGIVLGQALAEA
LGDKKGIRRYGHAYVPMDEALARVAVDLSGRPYLVFDVEFPREKIGDFDTELVEEFFRAFANNAGITLHI
RVLYGENAHHIIEAIFKAFARALREAVEIDPRRAGVPSTKGVL
>gnl|CDD|439902 COG0132, BioD, Dethiobiotin synthetase [Coenzyme transport and metabolism]. Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis
MKGLFVTGTDTDVGKTVVTAALAAALRAAGLRVGYYKPVQTGCEETDGGLRNGDAELLRRLSGLPLSYEL
VNPYRFEEPLSPHLAARLEGVPIDLDKILAALRALAARYDLVLVEGAGGLLVPLTEDLTLADLAKALGLP
VILVVRARLGTINHTLLTVEALRARGLPLAGIVLNGVPPPDLAERDNLETLERLTGAPVLGVLPYLADLD
PEALAAYLDLES
>gnl|CDD|439903 COG0133, TrpB, Tryptophan synthase beta chain [Amino acid transport and metabolism]. Tryptophan synthase beta chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
MSSLYSLPDEKGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERL
SEKLGGAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYM
GEEDIERQALNVFRMKLLGAEVVPVTSGSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDF
QSVIGREAREQILEKEGRLPDAVVACVGGGSNAIGIFYPFLDDESVRLIGVEAGGKGLETGEHAATLTKG
RPGVLHGARTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLKDTGRAEYVSVTDDEALEAFQLLSRTEG
IIPALESAHALAYALKLAPELSKDQIIVVNLSGRGDKDVDTVAKYLGLED
>gnl|CDD|439904 COG0134, TrpC, Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]. Indole-3-glycerol phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
PTILDKIVAHKREEVAARKARVPLAELEARAAAAPPPRDFAAALRAAGGPAVIAEIKKASPSKGLIREDF
DPAEIARAYEAGGAAAISVLTDEKFFQGSLEDLRAVRAAVDLPVLRKDFIIDPYQIYEARAAGADAILLI
AAALDDEQLKELLALAHSLGMDVLVEVHDEEELERALALGARLIGINNRNLKTFEVDLETTERLAPLIPA
DVLVVSESGIRTPEDVARLAAAGADAFLVGEALMRAPDPGAALRELL
>gnl|CDD|439905 COG0135, TrpF, Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]. Phosphoribosylanthranilate isomerase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
MTRVKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAALPPFVKKVGVFVNADPEEILE
IVEAVGLDAVQLHGDESPEYCAALRERLGLPVIKAIRVGDGADLEEAAAYAPVADALLLDAKVPGLYGGT
GKTFDWSLLAGLALPKPVILAGGLTPENVAEAIRLVRPYGVDVSSGVESAPGVKDPDKIRAFVEAVRA
>gnl|CDD|439906 COG0136, Asd, Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]. Aspartate-semialdehyde dehydrogenase is part of the Pathway/BioSystem: Lysine biosynthesis
YNVAVVGATGAVGRVLLELLEERDFPVGELRLLASSRSAGKTVSFGGKELTVEDATDFDFSGVDIALFSA
GGSVSKEYAPKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEALADHLPKGIIANPNCSTIQMLVALKPL
HDAAGIKRVVVSTYQAVSGAGAAAMDELAEQTAALLNGEEIEPEVFPHPIAFNLIPQIDVFLENGYTKEE
MKMVNETRKILGDPDIPVSATCVRVPVFRGHSEAVNIEFERPVSLEEARELLAAAPGVKVVDDPAENDYP
TPLDASGTDEVFVGRIRKDLSVPNGLNLWVVADNLRKGAALNAVQIAELLIKE
>gnl|CDD|439907 COG0137, ArgG, Argininosuccinate synthase [Amino acid transport and metabolism]. Argininosuccinate synthase is part of the Pathway/BioSystem: Arginine biosynthesis
KKVVLAYSGGLDTSVIIPWLKEKYGYEVIAVTADVGQGEDLEAIEEKALKLGASKAYVVDAREEFVEDYV
FPAIKANALYEGKYPLGTALARPLIAKKLVEIAREEGADAVAHGCTGKGNDQVRFELAIRALAPDLKIIA
PWREWDLKSREEEIEYAEEHGIPVPATKEKPYSIDENLWGRSIEGGELEDPWNEPPEDAYEWTVSPEDAP
DEPEYVTITFEKGVPVALNGEKLSPVELIEELNEIGGKHGVGRIDIVENRLVGIKSRGVYEAPGATILIT
AHRALESLTLDRETLHFKDILDQKYAELVYNGLWFSPLREALDAFIDETQKRVTGTVRLKLYKGNATVVG
RKSPYSLYDEDLATYEEDDVFDQKDAEGFIKLFGLPLRVAARVRKKK
>gnl|CDD|439908 COG0138, PurH, AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]. AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
VPIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPK
IHGGILARRDNPEHVAQLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHA
DVAVVVDPADYDAVLEELKANGGTSLETRRRLAAKAFAHTAAYDAAIANYLAEQLGEEEFPETLTLSFEK
VQDLRYGENPHQKAAFYRDPGAEGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCG
VAVGDTLAEAYEKAYACDPVSAFGGIIAFNRPVDAATAEAIAKIFLEVIIAPDFSPEALEILAKKKNLRL
LELGGLDPPAPGLDVKSVSGGLLVQDRDLGLIDPADLKVVTKRAPTEEELADLLFAWKVVKHVKSNAIVL
AKDGATVGIGAGQMSRVDSARIALEKAGERAKGSVLASDAFFPFRDGVEAAAKAGITAIIQPGGSIRDEE
VIAAADEHGIAMVFTGMRHFRH
>gnl|CDD|439909 COG0139, HisI1, Phosphoribosyl-AMP cyclohydrolase [Amino acid transport and metabolism]. Phosphoribosyl-AMP cyclohydrolase is part of the Pathway/BioSystem: Histidine biosynthesis
LEEGILDKLKFDEDGLIPAIVQDADTGEVLMLAYMNREALEKTLETGRATYWSRSRQRLWRKGETSGHVQ
KVKEIRLDCDGDALLLKVEQIGPACHTGRRSCFYRE
>gnl|CDD|439910 COG0140, HisI2, Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]. Phosphoribosyl-ATP pyrophosphohydrolase is part of the Pathway/BioSystem: Histidine biosynthesis
MSDVLDELEAVIEERKAADPEGSYTAKLFAKGIDKILKKVGEEAVEVVIAAKNGDKEELIYEAADLLYHL
LVLLAARGISLDDVLAELARRHGLSGLEEKASR
>gnl|CDD|439911 COG0141, HisD, Histidinol dehydrogenase [Amino acid transport and metabolism]. Histidinol dehydrogenase is part of the Pathway/BioSystem: Histidine biosynthesis
MMKILDDADLSAELKALLKRPAADDEDVEATVREILADVRARGDAALLEYTERFDGVDLESLRVSEEEIE
AAYAALDPELREALELAAENIRAFHEAQKPESWEVETEPGVVLGQRVTPIERVGLYVPGGKAPYPSSVLM
NAIPAKVAGVKEIVMCTPPPKDGKINPAVLAAAHLAGVDEIYKVGGAQAIAALAYGTETIPKVDKIVGPG
NIYVAAAKRLVFGGVGIDMPAGPSEILVIADETADPEFVAADLLSQAEHDPDAQAILVTTSEELAEAVEA
EVERQLATLPRAEIARKALEDNGAIILVDDLEEAIELANRYAPEHLELQTADPEALLERIRNAGAIFLGP
YTPESLGDYAAGPNHVLPTGGTARFSSGLSVDDFLKRSSVQEYSEEGLAKLAPAIETLAEAEGLEAHARA
VRIRLEKLG
>gnl|CDD|439912 COG0142, IspA, Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]. Geranylgeranyl pyrophosphate synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
MTLKDLLALLAEDLARVEAALEELLARSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRA
AAAVELIHTASLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDPERRLRALRIL
ARAARGMCEGQALDLEAEGRLDVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGL
AFQIRDDILDVTGDPEVLGKPAGSDLREGKPTLPLLLALERADPEERAELRELLGKPDLDEEDLAEVRAL
LRESGALEYARELARELAEEALAALAALPDSEAREALRALADYVVERDR
>gnl|CDD|439913 COG0143, MetG, Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVD
RIHAEFKELFEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGT
CPKCGAEDAYGDQCENCGATLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEENPDIQPE
VRNEVLSWLKEGLQDLSISRDFDWGIPVPGDPGKVFYVWFDALIGYISATKGYADDRGLPEDFEKYWPAP
DTELVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDAL
RYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMIHKYFDGKVPEPGELTEADEELLAEAE
AALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDEDPERLATVLYTLLEALRILAILLKP
FLPETAEKILEQLGLEGDELTWEDAGWPLPAGHKIGKPEPLFPRIEDEQIEALL
>gnl|CDD|439914 COG0144, RsmB, 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]. 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification
AAALAALRAEAAAAAAALALALLLLALLLLDRALAALLLLAALRLLRRRDRALLAALLAGLLRLLRLLLL
LLRLLLLLLLLLLLPLLAALLLVAAAQLLAARVAVDEAVGPGAAGLVNAVLRRVLREREALLAAADPVER
LAVRYSHPEWLVERLRAAYGPEEAEALLAALNEPPPLDLRVNTLKASREELLARLAEEGIEAEPTPLSPD
GLRLEGPGPVTALPGFREGLFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAV
DISEHRLKRLRENLARLGLSNVEVVVADARELLEWLPGKFDRVLLDAPCSGTGTLRRHPDIKWRRTPEDI
AELAALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGGYL
RLLPHRHGTDGFFIARLRKKA
>gnl|CDD|439915 COG0145, HyuA, N-methylhydantoinase A/oxoprolinase/acetone carboxylase, beta subunit [Amino acid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]
VGVDVGGTFTDVVAVDEDGRLRTHKVLSTPEDPSDGVLEGIRELLEDAGIPLAEIDLVVHGTTVATNALL
ERKGARTGLITTRGFRDVLEIGRQNRPDLYDLFIEKPEPLVPRRLRFEVRERIDADGEVLTPLDEAEVRA
AARELRAAGVEAVAVCFLHSYRNPAHERRAAEILREELPDVPVSLSSEVSPEIREYERTSTTVVNAYLSP
ILRRYLDRLEARLRERGFGGPLLIMQSNGGLASAEAAARRPVRTILSGPAGGVVGAAALARAAGFDNVIT
FDMGGTSTDVSLIEDGEPERTTETEVAGYPVRVPMVDIHTVGAGGGSIAWVDAGGRLRVGPESAGADPGP
ACYGRGGTEPTVTDANLVLGRLDPDNFLGGRMPLDVEAARAAIEKLADPLGLSVEEAAEGILRIANENMA
NAIRKVSVERGYDPRDFTLVAFGGAGPLHACALAEELGIPRVIVPPAAGVLSALGMLLADIRHDYVRSVE
APLDDADLAELNAAFAELEAEARAELAAEGVAAEDIRVERSADMRYAGQGHELTVPLPAGRLDAADLAAL
RAAFHAAHERRYGFALPDAPVEIVNLRVEAIGPVPKPELPRLPPGGDAAPAPKGTRPVYFDGGWVDTPVY
DREALPPGDRIAGPAIIEEPDTTTVVPPGWRATVDAYGNLILTRAAAA
>gnl|CDD|439916 COG0146, HyuB, N-methylhydantoinase B/oxoprolinase/acetone carboxylase, alpha subunit [Amino acid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]
LGTTVDPVTLEVIRNRLIAIAEEMGETLQRTAFSPNIKERLDFSCALFDADGRLVAQAPGIPVHLGSMPE
AVKAVIERFGNDGIRPGDVFITNDPYLGGTHLPDITVVTPVFHDGELVGFVASRAHHADIGGIVPGSMPP
DATEIFQEGLRIPPVKLVEAGELNEDVLRLILANVRTPDQNLGDLRAQIAANRVGERRLLELVERYGLDT
VEAAMDELLDYAERAVRAAIAALPDGTYRAEDFLDDDGVGDEPIKIKVTVTVKGDRITVDFTGTSPQVPG
NINAPLAVTRAAVLYALRCLLDPDIPLNAGCLRPIEVIAPEGSILNPRYPAAVVAGNVETSQRVVDAVFG
ALAQALPERVPAASQGTMNNLTFGGVDPRGEPFVYYETIGGGSGARPGGDGLDAVHTHMTNTRNTPVEVL
EARYPVLVERYELRPDSGGAGKYRGGLGVVREIRFLEPEMTVSLLGDRRRFPPWGLAGGGPGAPGRNVLV
RGDGDEEELGGKATVPLQPGDVVVIETPGGGGYGDPLERDPEAVLRDVRDGYVSPEAARRDYGVVLDPDG
AVD
>gnl|CDD|439917 COG0147, TrpE, Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism, Coenzyme transport and metabolism]. Anthranilate/para-aminobenzoate synthases component I is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
ARIPVYRELLALETPVSLFLKLADGPYAFLLESAEGGEKWGRYSFIGADPLATLTVRGGRVTIEGGGEVE
PSEGDPLDALRALLARFRLPPLPGLPPFTGGLVGYFGYDLVRYFERLPDLAPDDLGLPDAALGLYDRLLV
FDHLKGTRSNFTREEYLAAVERAKEYIRAGDIFQVVLSQRFSAPFEGDPLALYRALRRINPSPYMFYLRF
GDFAIVGSSPERLVRVEDGRVETRPIAGTRPRGATPEEDAALAEELLADEKERAEHLMLVDLARNDLGRV
CEPGSVKVPELMVVERYSHVMHLVSTVTGRLRPGLDALDALRATFPAGTLTGAPKIRAMEIIDELEPTRR
GVYGGAVGYLSFDGNMDLAIAIRTAVVKDGRAYVQAGAGIVADSDPEAEYQETLNKARALLRALEL
>gnl|CDD|439918 COG0148, Eno, Enolase [Carbohydrate transport and metabolism]. Enolase is part of the Pathway/BioSystem: Glycolysis
MSRIEDVHAREILDSRGNPTVEVEVTLEDGAVGRAAVPSGASTGSHEAVELRDGDKSRYLGKGVLKAVEN
VNEEIAPALIGMDATDQRAIDRAMIELDGTPNKSRLGANAILGVSLAVAKAAAAALGLPLYRYLGGVNAK
TLPVPMMNIINGGAHADNNVDIQEFMIMPVGAPSFSEALRMGAEVFHALKKVLKEKGLSTAVGDEGGFAP
NLKSNEEALELILEAIEKAGYKPGEDIALALDVAASEFYKDGKYHLKGEGKELTSEEMIDYYADLVDKYP
IVSIEDGLAEDDWDGWKLLTEKLGDKVQLVGDDLFVTNPKRLKKGIEEGAANSILIKVNQIGTLTETLDA
IELAKRAGYTAVISHRSGETEDTTIADLAVATNAGQIKTGSPSRSERVAKYNQLLRIEEELGDAARYAGR
SAFKRL
>gnl|CDD|439919 COG0149, TpiA, Triosephosphate isomerase [Carbohydrate transport and metabolism]. Triosephosphate isomerase is part of the Pathway/BioSystem: Glycolysis
MRKPLIAGNWKMNGTLAEAKALLAALAAALADLADVEVVVCPPFTYLAAVAEALAGSPIALGAQNVHWED
SGAYTGEISAAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTE
EVVARQLKAALAGLSAEQAANVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILY
GGSVKPGNAAELFAQPDIDGALVGGASLDAEDFLAIVRA
>gnl|CDD|439920 COG0150, PurM, Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]. Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis
MSMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKL
KIAQALDKHDTIGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGE
TAEMPGMYAPGEYDLAGFAVGVVEKDKIIDGSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDP
VPELGRTLGEALLEPTRIYVKPVLALLKAVDVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIF
DWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALLKAAGETAYVIGEVVAGEGEGVVL
>gnl|CDD|439921 COG0151, PurD, Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]. Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGP
EAPLVAGIVDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPI
VVKADGLAAGKGVVVAETLEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTA
QDHKRAGDGDTGPNTGGMGAYSPAPVVTEELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPK
VLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDEVELEWDDRAAVCVVLASGGYPGSYEKGDVITG
LEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERAYEAVEKIRFEGMFYRRDIGWRAL
KR
>gnl|CDD|439922 COG0152, PurC, Phosphoribosylaminoimidazole-succinocarboxamide synthase [Nucleotide transport and metabolism]. Phosphoribosylaminoimidazole-succinocarboxamide synthase is part of the Pathway/BioSystem: Purine biosynthesis
MPKLELLYEGKVKDVYATDDDTLLMVFKDRISAFDGVKPDPIPGKGEVLNQISAFWFELLEDIGIPTHFI
ETLSGREMLVKKLEMIPVEVVVRNYAAGSLWKRYQAGIALPLGLEEGTKLPEPIFEPSTKADEGHDPNIS
EEHIVALGLATEEEAEELRELALKINERLSELAAERGIILVDTKLEFGRDADGEIVLADEITPDSSRLWD
ADTYESLDKDRFRDWLGGNTSEAYIEVLERLTGEK
>gnl|CDD|439923 COG0153, GalK, Galactokinase [Carbohydrate transport and metabolism]
RLERLIEAFEEAFGEEPEGVFSAPGRVNLIGEHTDYNGGFVLPAAIDRGTYAAARPRDDRKVRVYSADFD
EEVEFDLDDLEPGEEDGWANYVRGVAWALQERGYKLGGFDLVIDGDVPLGAGLSSSAALEVAVALALNDL
FGLGLDPVELAKIGQRAENEFVGVPCGIMDQFASALGKKGHALLLDCRSLEYEYVPLPLEGYALVIVDTN
VKHSLADSEYNERRAECEAAAAILGVKSLRDVTLEDLEAARARLGDEVLRRRARHVVTENQRVLEAVEAL
RAGDLEAFGKLMNASHASLRDDYEVSCPELDTLVELALAEAGVLGARMTGGGFGGCTIALVPKDAVDEFI
EAVAEAYAEKTGLEPDFYVVKPSDGARRLA
>gnl|CDD|439924 COG0154, GatA, Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit or related amidase [Translation, ribosomal structure and biogenesis]. Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit or related amidase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MSDLAELSAAELAAALRAGEVSAVELVEAALARIEAVNPALNAFVTVDAERALAEARAADARRAAGEALG
PLAGVPVAVKDLIDVAGLPTTAGSKALADFVPPYDATVVARLRAAGAVILGKTNMPEFAMGGSTENSAYG
PTRNPWDPDRTPGGSSGGSAAAVAAGLVPLALGSDTGGSIRIPAAFCGLVGLKPTYGRVSRYGVVPLASS
LDQVGPLARTVADAALLLDVLAGPDPRDPTSAPAPVPDYLAALDRDLKGLRIGVPREYFGGDGVDPEVAA
AVEAAAAALEALGAEVVEVDLPDLDEALAAYYTIAAAEAAANLADLLRTRPEGFGPEVRRRILLGAYYSA
ADYLKAQRVRALLRRDFAAAFEDYDVLLTPTTPTPAPPIGELDADIDPALAMNYLLDRFTAPANLAGLPA
LSVPAGFTADGLPVGLQLIGPPGDEATLLRLAAALEQALGWHRRRPPL
>gnl|CDD|439925 COG0155, CysI, Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]. Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis
LYKYERIKREDVRSRLGTFAEQLGRFLTGEISEDDFRLRLKFHGLYQQRDPDGAFMLRVRIPGGVLTPEQ
LRALADIAREYGRGYLHLTTRQNIQLHWILLEDLPEILRELAEVGLTTIGACGDVVRNVTASPLAGVDPD
ELFDVRPYAEAISQHLLGHPEYTYLPRKFKIAFSGPPEDDADVEINDLGFIAVVKEDGLVGFNVLVGGGL
GRTPRLADVLGEFVPPEDLLDVAEAVVRVFRDYGDRDNRKKARLKYLVDDLGVEKFREEVEEEYLGFPLE
PAPRPLPAFARWDHLGVHEQKQDGLYYVGLSVENGRITDEQLRALADLAERYGSGEIRLTPNQNLILADV
PEEDLPALEAALRALGLATPPSGLRRDSIACPGLPTCKLAIAESKRLAPALADRLEEDLDGLHDDEPIRI
RISGCPNSCGRHYIADIGLVGKAKKGVVEAYQLYLGGGLGGDARLGRKYGPKVPADEIPDALERLLEAYL
AEREEGESFGDFVRRVGIEPLKELLYAAA
>gnl|CDD|439926 COG0156, BioF, 7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]. 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTG
SGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARL
SGAKVVRFRHNDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGV
LGETGRGLVEHFGLEDRVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAA
LEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVPVIVGDAERALALADALLERGIYVSAIRPP
TVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE
>gnl|CDD|439927 COG0157, NadC, Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]. Nicotinate-nucleotide pyrophosphorylase is part of the Pathway/BioSystem: NAD biosynthesis
IDELIRRALAEDLGYGDLTTEALIPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDR
VEAGDVLLEVEGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAV
RAGGGVNHRLGLSDAVLIKDNHIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLD
NMSPEELREAVALLRGRALLEASGGITLENIRAYAETGVDYISVGALTHSAPALDLSLRIEP
>gnl|CDD|439928 COG0158, Fbp, Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]. Fructose-1,6-bisphosphatase is part of the Pathway/BioSystem: Gluconeogenesis
MMKGTTLTQFLIEQQRRFPGATGELSALLNAIALAAKIISREVNKGGLAGILGAAGSENVQGETQKKLDV
IANEIFIEALEWGGHVAAMASEEMDDPIPIPEQYPRGKYLVLFDPLDGSSNIDVNVSVGTIFSILRRPSG
GGPVTEEDFLQPGSEQVAAGYVLYGPSTMLVLTTGNGVHGFTLDPSIGEFLLTHPNMRIPEDTKEYAINE
SNYRHWEPPVRRYIDECLAGKEGPRGRDFNMRWIGSLVADVHRILLRGGIFLYPADSRDGYPPGKLRLLY
EANPMAFLVEQAGGAATDGRQRILDIVPTSLHQRVPLILGSKEEVERVERYHAEPDAS
>gnl|CDD|439929 COG0159, TrpA, Tryptophan synthase alpha chain [Amino acid transport and metabolism]. Tryptophan synthase alpha chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
SRIDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERA
LANGVTLDDVFELVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAA
ADAHGLDLIFLVAPTTSDERIKKIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGF
GISTPEQAAEVAAYADGVIVGSALVKLIEEGGDDEALEALAAFVRELKAALR
>gnl|CDD|439930 COG0160, ArgD, Acetylornithine aminotransferase/4-aminobutyrate aminotransferase [Amino acid transport and metabolism]. Acetylornithine aminotransferase/4-aminobutyrate aminotransferase is part of the Pathway/BioSystem: Arginine biosynthesis
PKSAELLARRERYESRGYSRSYPVVIVRAEGAYLWDVDGNRYLDFLAGIGVLNVGHNHPRVVEAVKEQLD
KLTHTLTDYLTEAKVELAERLAELLPGPLLKKVFFGNSGAEAVEAALKLARAATGRPGVIAFTGAYHGRT
LGALALTGSSAPYKKGFGPLAPGVYHVPYPYPYRCPFGLSGEDCGEACLAYLERLLFDTQSGPDEVAAII
VEPIQGEGGFIVPPPGFLQALRELCREHGILLIADEVQTGFGRTGKFFAFEHFGVVPDIVTLAKSLGGGL
PLSAVVGRAEIMDAWGPGEHGGTFGGNPLACAAALAVLDVIEEEDLLENARELGAYLRERLEELAERHPI
IGDVRGRGLMLGVELVKDRGTKEPAPELAAAVVARAFERGLLLLTCGPYGNVLRFLPPLTITDEELDEGL
DILEEALAA
>gnl|CDD|439931 COG0161, BioA, Adenosylmethionine-8-amino-7-oxononanoate aminotransferase [Coenzyme transport and metabolism]. Adenosylmethionine-8-amino-7-oxononanoate aminotransferase is part of the Pathway/BioSystem: Biotin biosynthesis
DTASLLARDRAHLWHPFTQMKDFEALPPLVIVRAEGVYLYDADGRRYLDGMSGLWCVNHGHGRPEIAEAI
AEQLDKLAHVMFFGFTHEPAIELAERLAELAPGGLNRVFFTDSGSEAVETALKMARQYWRARGQPERTKF
ISRENGYHGDTFGAMSVGGLPGMHALFGPLLPGVLHVPAPYCYRNPFGESEEEFGARLADELEEAILEEG
ADTIAAFIVEPVVGAGGMIVPPPGYLKRLREICDKYGILLIADEVITGFGRTGKMFACEHAGVTPDIITL
AKGLTGGYLPLGATLVSDEIYDAFLDGDEAGAFMHGHTYSGHPLACAAALANLDILEEEDLLENVAAIGA
YLRAGLAELADHPLVGDVRGLGLIGAIELVADKATKEPFDPEGRVGARVYAAALERGLILRPLGDTIYLM
PPLIITEEEIDELVDALREALDEVLA
>gnl|CDD|439932 COG0162, TyrS, Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Tyrosyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MNLLLELIWRGLIEQITDEELREKLAGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGG
FTGMIGDPSGKSEERKLLTEEQVAENAETIKEQVFKFLDFDDNKAEIVNNSDWLGKLSFIDFLRDLGKHF
TVNRMLERDDVKKRLESGQGISFTEFSYPLLQGYDFVELYRRYGCDLQLGGSDQWGNILAGRELQRRYGG
EPQFGLTMPLLTGADGTKMGKSEGNAIWLDEEKTSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELE
AEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAFEALFGKGELPDDLPEVELSAAEGGIPLVDLLVE
AGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAGDLLHGGYLVLRVGKKKFALVKLK
>gnl|CDD|439933 COG0163, UbiX, Flavin prenyltransferase UbiX [Coenzyme transport and metabolism]. Flavin prenyltransferase UbiX is part of the Pathway/BioSystem: Ubiquinone biosynthesis
MKRIVVGITGASGAIYGLRLLEVLKALGVEVHLVISEAAKLVLAHETGLSLEELEALADVVYDNDDIGAP
IASGSFRTDGMVVAPCSMKTLAAIAHGLSDNLITRAADVTLKERRKLVLVPRETPLSLIHLENMLKLAEA
GAIILPAVPAFYHKPQTIDDLVDFVVGRILDLLGIEHDLYKRWGGEE
>gnl|CDD|439934 COG0164, RnhB, Ribonuclease HII [Replication, recombination and repair]
LRRGFRLVAGVDEAGRGPLAGPVVAAAVILPPDFPIEGLNDSKKLSPKKREELYEEIKERALAWAVGEAS
PEEIDELNILQATLLAMRRAVEGLSVKPDLVLVDGNRLPGLPIPVEAIVKGDAKSASIAAASILAKVTRD
RLMEELDEEYPGYGFAKHKGYPTKEHREALREYGPTPIHRRSFAPVKKLL
>gnl|CDD|439935 COG0165, ArgH, Argininosuccinate lyase [Amino acid transport and metabolism]. Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis
MSMKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAE
IEAGAFEFDPELEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEAL
LDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDR
ERTAELLGFDGPTENSLDAVSDRDFALEFLSAASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSI
MPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKDLQEDKEPLFDAVDTLKLCLRLFAGMIATL
KVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGKDLEDLTLEELQAFSPLIEE
DVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAALRA
>gnl|CDD|439936 COG0166, Pgi, Glucose-6-phosphate isomerase [Carbohydrate transport and metabolism]. Glucose-6-phosphate isomerase is part of the Pathway/BioSystem: Glycolysis
MTQTPAWQHLRRFERFSLEAAGLLLDYSKNRITDETLELLLELAEEEEAREALFAGEKINPTEGRAVLHG
ALRLPEAGEDVMPEVREELARIKAFAEKVRTGKRITDVVNIGIGGSDLGPRAVIEALKPYFRDGPRVHFV
SNVDPDYLAELLAGLDPETTLFIVISKSGTTQETLTNARVAREWLEKAGGEDAAKHFVAVTDNAGALRAF
GIDEGYNTFPFPDWVGGRYSVLSAVGLLPAAAIGIDFEELLAGAHAMDEHFRTAPLEENPPVLLALLGIW
YRNFKGAETEAVLPYDQRLERFPAWLQQLWMESNGKSVDRDGNPVGYGTGPVGEPGTTDQHSFGQLLHQG
TRDIPVTFIAVAEPHHDIPDLLLANLQGLALLAGKTLDEVLALAAEATPHALFPGNRPSNTILLPKLTPY
TLGALIALYEHAVFVQGVLWGINPFDQPGVELGKKLAFALLGKLGGEEAAAGDSTEALLKRLRA
>gnl|CDD|439937 COG0167, PyrD, Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]. Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINR
MGLNNPGVDAFLERLLPAKRYDVPVIVNIGGNTVEDYVELARRLADAGADYLELNISCPNTPGGGRALGQ
DPEALAELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVLANEA
GGLSGPALKPIALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRII
RGLEAYLEEKGFSSIS
>gnl|CDD|439938 COG0168, TrkG, Trk-type K+ transport system, membrane component [Inorganic ion transport and metabolism]
PAREGFLIVALVWLVGALLLALPFALSGGGLSFLDALFEAVSGVTTTGLTVVDTLDTLPKFGLLWRSLLQ
WLGGLGIIVLAVAILPLLGIGGRQLFQAELPNEKLLPRIVRTAKALWLIYLGLTLIGALLLWLAGMALFD
AIFHAFSAFSTGGFSTHDDSLGAFNSPAIELVIIVFMILGGLGFPVHYDLLRYRRFRRLFSDTELRLYLT
LILLVVGLLALFLWNNGTLGSLGEALRAALFQVVSILTTTGFATVDYGQWPPFSLLLLILLMFIGGSAGS
TAGGIKVTRFAVLLKAIRRELRRLIHPNAVRPVRIGGRRIPEEVIRKALAFFFLYLLLVVVGTLLLSLTE
GLDFLTALFEVASAFGNVGLSLGITGASLSDAGKLVLIFLMLLGRLEILTVLVLLTPRFRWREE
>gnl|CDD|439939 COG0169, AroE, Shikimate 5-dehydrogenase [Amino acid transport and metabolism]. Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
NGKTRLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVPPEDLAAAVAGLRALGIRGLNVTIPHKEA
AIPLLDELDPRARLIGAVNTVVFEDGRLIGDNTDGIGFVRALREAGVDLAGKRVLVLGAGGAARAVAAAL
AEAGAAEITIVNRTPERAEALAARLGVRAVPLDDLAAALAGADLVINATPLGMAGGDALPLPASLLAPGA
VVYDLVYNPLETPLLRAARARGARVIDGLGMLVHQAAEAFELWTGVRPPVEAMRAALRAL
>gnl|CDD|439940 COG0170, SEC59, Dolichol kinase [Posttranslational modification, protein turnover, chaperones, Cell wall/membrane/envelope biogenesis]
SGLKKELSRKIIHIGSGLVILLALYLFIGRWIALILLALLLVGYLIIELLRLRYPLILLSSILREVERKP
SLGTVYFALGILILVLLFPPEIAAAAILVLALGDGLAALVGKRFGKHKLPVGGGKSLEGSLAMFIVSFLI
LLLVLLLFSLLIALLIALVATLVEALSPKGDDNLTIPLASALLLYLLGLL
>gnl|CDD|439941 COG0171, NadE, NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]. NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis
LLLLLALLLLAAALLDAAAAAAAALAALAAAAAALLLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLL
LALAAGGGAALAGGGGGAGGGLLNGAALVLGGGDLLFFADDFLLLLLVVEEEEEEFVGGPPPPPAALGGA
GVLLILSSSSSAVGAAAAAAALAAALLSSLSSAAYYAAAGGGESTTDLARGGGGGLLLVVLLLVGGGDDD
FFDGGSAAVDDDDLLLLLRRRREEELLLARARDADGGRRVAAEAAPPPPEEEEMDLEEVYDALVLGLRDY
VRKNGFKGVVLGLSGGIDSALVAALAVDALGPENVLGVTMPSRYTSDESLEDAEELAENLGIEYEEIDIT
PAVEAFLEALPHAFGGELDDVAEENLQARIRMVILMALANKFGGLVLGTGNKSELAVGYFTKYGDGAGDL
APIADLYKTQVYALARWLNRNGEVIPEDIIDKPPSAELRPGQTDEDELGPYEVLDAILYAYVEEGLSPEE
IAAAGYDREWVERVLRLVRRNEYKRRQPPPGPKVSSRAFGRGRRYPIDSGRE
>gnl|CDD|439942 COG0172, SerS, Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MLDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEA
LIAEVKELKEEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHW
ELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGTGQLP
KFEEDLYKIEGDDLYLIPTAEVPLTNLHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFD
KVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISS
CSNCTDFQARRLNIRYRDEDGKPEFVHTLNGSGLAVGRTLVAILENYQQADGSVRIPEVLRPYMGGLEVI
E
>gnl|CDD|439943 COG0173, AspS, Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MYRTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDDSAEAFEKAEKLRSEYV
IAVTGKVRARPEGTVNPKLPTGEIEVLASELEILNKAKTPPFQIDDDTDVSEELRLKYRYLDLRRPEMQK
NLILRHKVTKAIRNYLDENGFLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVSGF
DRYFQIARCFRDEDLRADRQPEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLGVELPTPFPRMTYAEA
MERYGSDKPDLRFGLELVDVTDIFKDSGFKVFAGAAENGGRVKAINVPGGASLSRKQIDELTEFAKQYGA
KGLAYIKVNEDGLKSPIAKFLSEEELAAILERLGAKPGDLIFFVADKPKVVNKALGALRLKLGKELGLID
EDEFAFLWVVDFPLFEYDEEEGRWVAMHHPFTMPKDEDLDLLETDPGKVRAKAYDLVLNGYELGGGSIRI
HDPELQEKVFELLGISEEEAEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFPKTQSA
QDLMTGAPSEVDEKQLKELHIRLRPPEKK
>gnl|CDD|439944 COG0174, GlnA, Glutamine synthetase [Amino acid transport and metabolism]. Glutamine synthetase is part of the Pathway/BioSystem: Glutamine biosynthesis
MSKLTVEEVLAFLKERGVKFVDLQFTDINGVLRGKRVPASELEKALEEGIGFDGSSIEGFVEIGESDMVL
VPDPSTLRILPWRPEPTARVICDVYDPDGEPYEGDPRNVLKRVLARLAETGLTPYVGPELEFFLFDDDSD
EKGNRGLRPRDKGGYYDLAPLDRFEDFRREIVLALEAMGIPVETSHHEVAPGQHEINLRYADALTAADRV
VLFKYVVKEVARRHGLTATFMPKPFAGDNGSGMHVHQSLWDADGKNLFADPDGYAGLSELARHFIGGLLK
HAPALTAFTAPTVNSYKRLVPGYEAPVNIAWGYDNRSAAIRIPGGSPKATRIEYRVPDADANPYLAFAAL
LAAGLDGIENKLEPGEPVDGNAYELSPEERAGIPRLPRSLEEALDALEADEFLREVLGEDFVDHYIALKR
AEWEEFRRRVTPWERERYLE
>gnl|CDD|439945 COG0175, CysD, 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]. 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis
PLPATLDDLLEELNAELEAEAIEILREAAAEFGGRVVVSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYE
FPETYEFRDRLAERLGLDLIVVRPEDAFAEQLAEFGPPLFYRDPRWCCKIRKVEPLKRALAGYDFDAWIT
GLRRDESPTRAKEPVVEWDPVGGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVE
SGEDERAGRWWDEEKERKECGL
>gnl|CDD|439946 COG0176, TalA, Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]. Transaldolase/fructose-6-phosphate aldolase is part of the Pathway/BioSystem: Pentose phosphate pathway
MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAKAGIKDFVEDIREICDIVDGPVSAEVLATDTEGMIAE
ARRLAALYRPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGI
DGIALVREIYQIYKNYGARTRILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLAD
WEKL
>gnl|CDD|439947 COG0177, Nth, Endonuclease III [Replication, recombination and repair]
LERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPI
GLYRNKAKNIIALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLG
LVPGKDPEEVEKDLMKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG
>gnl|CDD|439948 COG0178, UvrA, Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]
MMMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQM
DKPDVDSIEGLSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDR
ILALPEGTRLQILAPVVRGRKGEHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLV
VKEDIRSRLADSVETALKLGDGLVIVEVVDEGEELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTC
DGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSSSYYFQLLEALAKHYGFDLDTPWKDLPEEQRDLILY
GSDEKIKFRYKNRGRRRTYEKPFEGVIPFLERRYRETYSEHVREELSRYMSETPCPACKGARLKPEALAV
KIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLTLDRSAGTLSGGE
AQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIIDIG
PGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIPL
GVLTCVTGVSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPAT
YTGVFDPIRELFAQTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNR
ETLEVKYKGKNIADVLDMTVEEALEFFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASE
LSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGG
EIVAEGTPEEVAKVKASYTGRYLKEYLEAAR
>gnl|CDD|439949 COG0179, YcgM, 2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) [Secondary metabolites biosynthesis, transport and catabolism]
APVPPGKIICVGLNYADHAAEMGNDVPEEPVLFLKPPSALVGPGDPIPLPAGSGKLDYEGELAVVIGKRA
RNVSEEDALDHVAGYTVANDVTARDLQRERGGQWTRGKSFDTFCPLGPWIVTADEIPDPQDLRIRLRVNG
EVRQDGNTSDMIFSVAELIAYLSQFMTLEPGDVILTGTPAGVGPLKPGDVVEVEIEGIGTLRNTVV
>gnl|CDD|439950 COG0180, TrpS, Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Tryptophanyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MSKKRVLSGIQPTGRLHLGNYLGALKNWVELQDEYECFFFIADLHALTTPQDPEELRENTREVAADYLAA
GLDPEKSTIFVQSDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKENVNAGLLTYPVLMAADILLY
KADLVPVGEDQKQHLELTRDIARRFNHRYGEVFPEPEALIPEEGARIPGLDGRKKMSKSYGNTINLLDDP
KEIRKKIKSAVTDSERLRYDDPGKPEVCNLFTIYSAFSGKEEVEELEAEYRAGGIGYGDLKKALAEAVVE
FLAPIRERRAELLADPAELDEILAEGAEKARAIAAKTLAEVREAMGLLYF
>gnl|CDD|439951 COG0181, HemC, Porphobilinogen deaminase [Coenzyme transport and metabolism]. Porphobilinogen deaminase is part of the Pathway/BioSystem: Heme biosynthesis
MTKTLRIGTRGSPLALWQAEHVADRLEAAHPGLEVELVPIKTKGDKILDRPLAKIGGKGLFTKELEEALL
DGEIDIAVHSLKDVPTELPEGLVLAAVLEREDPRDALVSRDGASLDDLPEGAVVGTSSLRRQAQLLALRP
DLEIVDLRGNVDTRLRKLDEGEYDAIILAAAGLKRLGLEDRITEVLDPEEMLPAPGQGALGIECRADDEE
LRELLAALNDPETRLAVTAERAFLAALEGGCQVPIGAYATLEGDELTLRGLVASPDGSEVIRAERSGPAA
DAEALGRELAEELLAQGAAEILAEIR
>gnl|CDD|439952 COG0182, MtnA, 5-methylthioribose/5-deoxyribulose 1-phosphate isomerase (methionine salvage pathway), a paralog of eIF-2B alpha subunit [Amino acid transport and metabolism]
DKVRTIWWDGGALVLLDQTLLPHEEEYVELTTVEDVAEAIRDMVVRGAPAIGVAAAYGVALAAREAAADD
REEFLAELEEAAEYLAATRPTAVNLFWALDRMLAALEELPSVEEIREALLAEALAIADEDVAANRAIGEH
GAELIPDGDTILTHCNAGALATVGYGTALGVIRAAHEAGKLIHVYADETRPLLQGARLTAWELMQDGIPV
TLITDNAAGHLMQRGKVDAVIVGADRIAANGDVANKIGTYGLAVLAKHHGIPFYVAAPTSTIDLSLPDGE
DIPIEERDPDEVTHVGGRRIAPEGVPVYNPAFDVTPAELITAIITEKGVIRPPYEENLAKLFP
>gnl|CDD|439953 COG0183, PaaJ, Acetyl-CoA acetyltransferase [Lipid transport and metabolism]. Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAA
LLAGLPESVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVD
PMINPGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEV
VVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVA
GVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLG
ASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV
>gnl|CDD|439954 COG0184, RpsO, Ribosomal protein S15P/S13E [Translation, ribosomal structure and biogenesis]. Ribosomal protein S15P/S13E is part of the Pathway/BioSystem: Ribosome 30S subunit
MPLTKEEKEEIIKEYGRHEGDTGSPEVQIALLTERINNLTEHLKEHKKDHHSRRGLLKMVGKRRRLLDYL
KKKDIERYRALIAKLGLRK
>gnl|CDD|439955 COG0185, RpsS, Ribosomal protein S19 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S19 is part of the Pathway/BioSystem: Ribosome 30S subunit
MRRSLKKGPFVDEKLLKKVEKANESGEKKVIKTWSRRSTILPEMVGLTIAVHNGKKFVPVYITEEMVGHK
LGEFAPTRTFVGHGGPGKGATRSSK
>gnl|CDD|439956 COG0186, RpsQ, Ribosomal protein S17 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S17 is part of the Pathway/BioSystem: Ribosome 30S subunit
MSEERVRRKTLTGVVVSDKMDKTVVVEVERRVKHPLYGKYVRRSKKYHAHDENNECKVGDTVRIMETRPL
SKTKRWRVVEIVEKAKE
>gnl|CDD|439957 COG0187, GyrB, DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair]
AKKSNYDASSIQVLEGLEAVRKRPGMYIGSTDERGLHHLVWEIVDNSIDEALAGYCDRIEVTLHADGSVT
VEDNGRGIPVDIHPKEGKSALEVVLTVLHAGGKFDGGSYKVSGGLHGVGASVVNALSERLEVEVKRDGKI
YRQRFERGKPVGPLEKIGKTDRTGTTVRFKPDPEIFETTEFDYETLAERLRELAFLNKGLTITLTDEREE
EPKEETFHYEGGIKDFVEYLNEDKEPLHPEVIYFEGEKDGIEVEVALQWNDGYSENIHSFVNNINTPEGG
THETGFRTALTRVINDYARKNGLLKEKDKNLTGDDVREGLTAVISVKLPEPQFEGQTKTKLGNSEARGIV
ESVVSEKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSALESSGLPGKLADCSSKDPEESE
LFIVEGDSAGGSAKQGRDREFQAILPLRGKILNVEKARLDKILKNEEIRDLITALGTGIGDDFDLEKLRY
HKIIIMTDADVDGAHIRTLLLTFFYRYMRPLIEAGHVYIAQPPLYRIKKGKKTYYAYSDAELDELLKELK
GKKKVEIQRYKGLGEMNPEQLWETTMDPETRTLLQVTIEDAAEADEIFSLLMGDKVEPRREFIEENAKFV
RNLDI
>gnl|CDD|439958 COG0188, GyrA, DNA gyrase/topoisomerase IV, subunit A [Replication, recombination and repair]
MSDPPPAERIIPVNLEDEMKRSYLDYAMSVIVGRALPDVRDGLKPVHRRILYAMHELGLTPDKPYKKSAR
VVGDVMGKYHPHGDSAVYDALVRMAQDFSMRYPLVDGQGNFGSIDGDPAAAMRYTEARLAKIAEELLADI
DKDTVDFVPNYDGSEQEPTVLPARFPNLLVNGSSGIAVGMATNIPPHNLGEVIDACIALIDNPDATIEEL
MEYIPGPDFPTGGIIVGREGIREAYETGRGSIRVRAKAEIEELKRGREQIVVTEIPYQVNKARLIEKIAE
LVKEKKIEGISDVRDESDRDGMRIVIELKRDANPEVVLNQLYKHTQLQTSFGINMLALVDGRPRVLNLKE
ILEAFLDHRREVVTRRTQFELRKAEERAHILEGLLIALDNIDEVIAIIRASKDPDEAKEALMERFGLSEI
QAEAILDMRLRRLTGLEREKIEDEYAELLKEIAELEDILASEERLLKIIKEELLEIKKKYGDERRTEIEE
AEGEIDIEDLIPDEDVVVTLSHKGYIKRTPLDTYRAQRRGGKGVSGMGTKEEDFVEHLFVASTHDTLLFF
TNKGRVYRLKVYELPEGSRTAKGKPIVNLLPLEPGEKITAVLPVKEFDEDKYLLFATKKGTVKKTPLSDF
SNIRKNGIIAINLKEGDELVGVALTDGDDDVLLATSNGKAIRFPESDVRPMGRTARGVRGIRLKEGDEVV
GMAVVDEEDDLLTVTENGYGKRTPLSEYRLQGRGGKGVITIKLTEKNGKLVGALVVNDDDELMLITSSGQ
LIRTPVSDIRVTGRNTQGVRLIRLDEGDKVVSVA
>gnl|CDD|439959 COG0189, LysX, Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]. Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
MMKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPELYRGEDLSEFDAVLPRIDPPFYG
LALLRQLEAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLD
GSGGRGVFLVEDEDALESILEALTELGSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTN
LARGGRAEPVELTDEERELALRAAPALGLDFAGVDLIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIA
DYLEARAAR
>gnl|CDD|439960 COG0190, FolD, 5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism]
MMAQILDGKAVAAEIREELKERVAALKAKGITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLP
ADTTQEELLALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPC
TPAGIMELLERYGIDLAGKHAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVG
KPGLITADMVKPGAVVIDVGINRVEDGKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER
QAGLR
>gnl|CDD|439961 COG0191, Fba, Fructose/tagatose bisphosphate aldolase [Carbohydrate transport and metabolism]. Fructose/tagatose bisphosphate aldolase is part of the Pathway/BioSystem: Glycolysis
MLVSLKELLDKAKEGGYAVPAFNVNNLETLQAILEAAEELNSPVILQVSEGAAKYAGLEYLAAMVRAAAE
EASVPVALHLDHGASFELIKRAIDAGFTSVMIDGSHLPFEENIAITKEVVEYAHAAGVSVEAELGVVGGE
EDGVDVDDAEALYTDPEEAAEFVEETGVDALAVAIGTVHGVYKGEPKLDFDRLKEIREAVPVPLVLHGGS
GVPDEEIREAIKLGVAKINIDTDLRLAFTAAVREYLAENPDKYDPRKYLKPAREAMKEVVKEKIRLFGSA
GKA
>gnl|CDD|439962 COG0192, MetK, S-adenosylmethionine synthetase [Coenzyme transport and metabolism]. S-adenosylmethionine synthetase is part of the Pathway/BioSystem: Methionine biosynthesis
RYLFTSESVTEGHPDKVCDQISDAILDAILAQDPNARVACETLVTTGLVVVAGEITTSAYVDIPEIVRET
IKEIGYTSSEYGFDADTCAVLTSIHEQSPDIAQGVDEALDELDEQGAGDQGIMFGYACNETPELMPLPIS
LAHRLARRLAEVRKSGELPYLRPDGKSQVTVEYEDGKPVRIDTVVVSTQHDPDVSQEQLREDIIEEVIKP
VLPAELLDDDTKYLINPTGRFVIGGPQGDAGLTGRKIIVDTYGGYARHGGGAFSGKDPTKVDRSAAYAAR
YVAKNIVAAGLADRCEVQLAYAIGVAEPVSIYVDTFGTGKVSDEKIEEAVREVFDLRPAGIIERLDLRRP
IYRKTAAYGHFGREDLDFPWEKTDKVEALKKAAG
>gnl|CDD|439963 COG0193, Pth, Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]. Peptidyl-tRNA hydrolase is part of the Pathway/BioSystem: Translation factors
MMKLIVGLGNPGPEYANTRHNIGFMVVDELARRHGVSFKKKKFKGLVAEGRIGGEKVLLLKPQTYMNLSG
EAVAALARFYKIPPEDILVVHDDLDLPPGKIRLKKGGGHGGHNGLKSIIAHLGTQDFPRLRIGIGRPGGK
GDVADYVLGKFSKEERELLDEAIDRAADAVELLLKGGLEKAMNRFNS
>gnl|CDD|439964 COG0194, Gmk, Guanylate kinase [Nucleotide transport and metabolism]
RGKLIVLSGPSGAGKTTLVKALLERDPDLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEW
AEVHGNYYGTPKAEVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEE
VIERRLAKAREELAHADEFDYVVVNDDLDRAVEELKAIIRAERLRRERQA
>gnl|CDD|439965 COG0195, NusA, Transcription antitermination factor NusA, contains S1 and KH domains [Transcription]
MSMMLLELLEALEELEKEKGIDKEILIEALEAALKKAYKKNYGNEVVVRVIIDGDTGEIRVYVVKEVVEE
VEDPREEILLEAAKEDDPDEEGGDIIEEEVPPDFFGRIAAQAAKQVIQQKRREAEREIIYEEFKDRGGEI
VGGVVQRVERGNVIVDLGKVEAILPRREQIPGENYRVGDRIRAYVLEVRKETRGPQIILSRTHPEFLKRL
FELEVPEIADGIVEIKAIAREPGSRAKIAVYSNDPRVDPVGACVGMRGSRVQAVVNELNGEKIDIILWSE
DPAQFIANALSPAKVSSVEVDEEEKSADVVVPDDQLSLAIGKGGQNVRLAAKLTGWKIDIKSESEAEEKR
EEE
>gnl|CDD|439966 COG0196, RibF, FAD synthase [Coenzyme transport and metabolism]. FAD synthase is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
MKIIRGLSELPADLRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKL
LTTLEEKLELLEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLR
ELGEEYGFEVEVVPPVTIDGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTAN
LALPEEKLLPADGVYAVRVRIDGRRYPGVANIGTRPTFDGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLR
DEKKFDSLEALKAQIAKDVEQARAILAKLK
>gnl|CDD|439967 COG0197, RplP, Ribosomal protein L16/L10AE [Translation, ribosomal structure and biogenesis]. Ribosomal protein L16/L10AE is part of the Pathway/BioSystem: Ribosome 50S subunit
MLMPKRVKYRKQQRGRIKGVAKRGNKFAFGNYGLKALEPGQITSRQIEAARIAITRYLKRGGKVWIRIFP
DKPLTKKPAETRMGAGKGKPEGWVAVVKPGRILFEIAGVSEEVAKEALRLAAHKLPIKTRIVVREE
>gnl|CDD|439968 COG0198, RplX, Ribosomal protein L24 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L24 is part of the Pathway/BioSystem: Ribosome 50S subunit
MKMKIKKGDTVIVIAGKDKGKRGKVLKVLPKKNRVIVEGVNIVKKHQKPNQQNPQGGIIEKEAPIHISNV
MLVDPKTGKPTRVGFKVLEDGKKVRVCKKSGEVI
>gnl|CDD|439969 COG0199, RpsN, Ribosomal protein S14 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S14 is part of the Pathway/BioSystem: Ribosome 30S subunit
MAKKSMIARNKKRPKPVRLRNRCELTGRPRGYYRKFGLCRICFRELAHRGEIPGVKKASW
>gnl|CDD|439970 COG0200, RplO, Ribosomal protein L15 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L15 is part of the Pathway/BioSystem: Ribosome 50S subunit
MKLNELKPAPGSRKKRKRVGRGIGSGKGKTAGRGHKGQKARSGGGVRPGFEGGQMPLYRRLPKRGFKNIF
RKEYAVVNLGDLNKLFEAGTEVTLEALKEAGLVKKKKDGVKILGNGELTKKLTVKAHKFSKSAKEKIEAA
GGKVEVIE
>gnl|CDD|439971 COG0201, SecY, Preprotein translocase subunit SecY [Intracellular trafficking, secretion, and vesicular transport]
MLSTLKNAFKIPELRKRILFTLGILIVYRLGSHIPVPGIDPAALAQLFAQQSGGLLGLLNMFSGGALSRF
SIFALGIMPYITASIIMQLLTVVIPKLEELQKEGEEGRKKITQYTRYLTVVLALLQAFGIALGLRSGPPG
GGLVIDPGILFYLLTVITLTAGTMFLMWLGEQITERGIGNGISLIIFAGIVARLPSALAQIFELVRTGEL
SILLLLLLLVLALAVIAFVVFVEQAQRRIPVQYAKRVVGRRMYGGQSTYLPLKVNMAGVIPIIFASSLLL
FPATIAQFFGGSSGWLQWIANYLSPGSPLYIVLYALLIIFFTYFYTAITFNPEEIADNLKKSGGFIPGIR
PGKPTAEYLDKVLTRLTLVGAIFLALIAILPEILGAITGVPFYFGGTSLLIVVGVALDTMKQIESQLLMR
HYEGFLK
>gnl|CDD|439972 COG0202, RpoA, DNA-directed RNA polymerase, alpha subunit/40 kD subunit [Transcription]. DNA-directed RNA polymerase, alpha subunit/40 kD subunit is part of the Pathway/BioSystem: RNA polymerase
LEFEKPRKIEVEEEISDNYGKFVLEPLERGYGTTLGNALRRVLLSSLPGAAVTSVKIEGVLHEFSTIPGV
KEDVTDIILNLKGLRLKLHSDEPKTLRLEKKGPGEVTAGDIELPSDVEILNPDLVIATLDEDAKLEMELT
VEKGRGYVPAEENKKEDLPIGVIPIDAIFSPVRKVNYTVENTRVGQRTDYDKLILEIWTDGSITPEEALA
EAAKILIEHLSLFVNLEEEAEEVEEEVEEEEEEIDPILLRPIEELELSVRSYNCLKRAGINTIGDLVQKT
EEELLKIRNFGKKSLEEIKEKLAELGLSLGMDLENWP
>gnl|CDD|439973 COG0203, RplQ, Ribosomal protein L17 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L17 is part of the Pathway/BioSystem: Ribosome 50S subunit
MRHRKKGRKLGRTSSHRKALLRNLATSLIEHERITTTLAKAKELRPYVEKLITLAKKGDLHARRLAFAYL
RDKEAVKKLFDEIAPRYADRPGGYTRIIKLGFRKGDNAPMAIIELVDRDEE
>gnl|CDD|439974 COG0204, PlsC, 1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]. 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis
LRSLFLLLRRFRYRLVRLWARLLLRLLGVRVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPRPVRF
VAKKELFKIPLLGWLLRALGAIPVDRSKRRAALRALRQAVEALKAGESLVIFPEGTRSPDGRLLPFKTGA
ARLALEAGVPIVPVAIDGTERALPKGFLPRPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLAEL
RAEAA
>gnl|CDD|439975 COG0205, PfkA, 6-phosphofructokinase [Carbohydrate transport and metabolism]. 6-phosphofructokinase is part of the Pathway/BioSystem: Glycolysis
MKRIGILTSGGDAPGLNAAIRAVVRTAIKYGIEVYGIRDGYEGLLEGDIIDLTREDVSGILQRGGTILGS
SRSKPFKTEEGREKALENLKKLGIDALVVIGGDGSLDGAAKLAEEYGIPVVGIPKTIDNDLPGTDYTIGF
DTAVNTAAEAIDRLRDTAASHERVFVVEVMGRHAGWLALAAGLAGGADLILIPEVPFDLDKLLEKLKERR
KRGKGYSIIVVAEGAGDEDGEAVLEADTDAFGHVRLGGIGEYLAKEIEERTGIETRVTVLGHLQRGGSPS
AFDRVLASRLGAAAVELLLEGKTGVMVGIRRGEIVLVPLEEVANKEKPVDPDSPLIQLARELGI
>gnl|CDD|439976 COG0206, FtsZ, Cell division GTPase FtsZ [Cell cycle control, cell division, chromosome partitioning]
MFELDDEEELKAKIKVIGVGGGGGNAVNRMIEAGLEGVEFIAANTDAQALENSKAPTKIQLGEKLTRGLG
AGANPEVGRKAAEESREEIREALEGADMVFITAGMGGGTGTGAAPVIAEIAKELGALTVGVVTKPFSFEG
KRRMRQAEEGIEELRKYVDTLIVIPNDKLLEVADKNTPLLEAFKKADDVLRQAVQGITDLITKPGLINLD
FADVKTVMSNGGVALMGIGEASGENRAEEAAEKAISSPLLEDVSISGAKGVLVNITGGSDLTLDEVNEAA
EIIQEEADPDANIIFGAVIDESLGDEIRVTVIATGFDSEAIVGEEETERPLEETEPAEDLDIPAFLR
>gnl|CDD|439977 COG0207, ThyA, Thymidylate synthase [Nucleotide transport and metabolism]. Thymidylate synthase is part of the Pathway/BioSystem: Thymidylate biosynthesis
MKQYLDLLRHILEEGTWKEDRTGTGTLSVFGYQMRFDLSEGFPLLTTKKVHWKSIIHELLWFLRGDTNIR
YLRENGVKIWDEWADENGDLGPVYGKQWRSWPTPDGGTIDQIAQVIDQLKTNPDSRRLIVSAWNPAELDE
MALPPCHALFQFYVADGKLSCQLYQRSADVFLGVPFNIASYALLTHMVAQVTGLEPGEFVHTIGDAHIYL
NHLEQVKEQLSREPRPLPKLKINPKVKSIFDFTFEDFELEGYDPHPAIKAPVAV
>gnl|CDD|439978 COG0208, NrdB, Ribonucleotide reductase beta subunit, ferritin-like domain [Nucleotide transport and metabolism]. Ribonucleotide reductase beta subunit, ferritin-like domain is part of the Pathway/BioSystem: Pyrimidine salvage
LDEPIINGLTTNRINWNPIKYPWAYELYKKQLANFWLPEEVPLSNDIKDWKKLSDDERHLIKRVLGFLTL
LDSIQGNNLVLALYPHVTAPEVRAVLSRQAFMEAIHAKSYSYILETLGLDIDEIFNWIEENPALQKKAEF
ILKYYDDLGTRETKKDLLKSLVASVFLEGIFFYSGFAYPLSLARRGKMKGTAEIIRLILRDESLHGNFGI
YLINTIREENPELFTEELKEEIYELLKEAVELEKEYADDLFPDGILGLNAEDVKQYIRYIANKRLMNLGL
EPLFEGDVNPFPWMSEGLDLNKKTDFFETRVTEYQKGGVESTFDED
>gnl|CDD|439979 COG0209, NrdA, Ribonucleotide reductase alpha subunit [Nucleotide transport and metabolism]. Ribonucleotide reductase alpha subunit is part of the Pathway/BioSystem: Pyrimidine salvage
QLRKEALGQYKSFSEKIKYVEEGLYDERLLEEDLEELAAAIDPERDRFFSYNALKTLYDRYLLKDEDGKP
LETPQDLFMRVAMGLAAAEKPEDREEWAKEFYDLLSSLRFLPATPTLFNAGTPRGQLSSCFVLPVEDSLE
SIFDALKDAALLSKSGGGVGFNFSRLRPKGSPIKGTGGVSSGPVPFMKVFDDAAVAVNQGGKRRGANMVY
LRVWHPDIEEFLDLKKNNGDERRRLHNFNISVWIPDLFMEAVEEDEDWTLFSPREVPDLYGLYGEEFEEA
YEEYEADGRVYKTIKARELWRKILESAWETGEPGILFKDTINRRNPLPHLGVIHSSNLCGEIPLLPYESE
DASCNLGSINLAKFVKDGEFDWEKLEETVRTAVRFLDNVIDINDYPVPEIEKANRRHRPIGLGVMGLADA
LAKLGIPYDSEEARELADEIMEFINYYAYKASAELAKERGAFPAFEGSKYAKGILPFDKYLDDLLIPTTL
DWDALREDIKKHGLRNSTLTAIAPTGTISLIAGTTSGIEPIFSLVYVRKVLDGGEFTVVNPYLVRALKEL
GLWDEELVEKIKEDGSVQDIDELPEELKELYVTAYEIDPEWHIDMQAARQKHVDQAISKTLNLPNDATVE
DLAELYLLAWKLGLKGIYYYRDGSRTGQVLSTGKK
>gnl|CDD|439980 COG0210, UvrD, Superfamily I DNA or RNA helicase [Replication, recombination and repair]
SDLLAGLNPEQRAAVEHPEGPLLVLAGAGSGKTRVLTHRIAYLIAEGGVDPEQILAVTFTNKAAREMRER
IEALLGRLARGLWVGTFHSLALRILRRHAELLGLPPNFTILDGDDQLRLIKELLKELGLDEKRFPPRELL
SLISRAKNEGLTPEELAELLAADPEWRAAAELYEAYQERLRANNALDFDDLLLLAVRLLEENPEVLEKYQ
NRFRYILVDEYQDTNPAQYELLRLLAGDGRNLCVVGDDDQSIYGFRGADPENILRFEKDFPDAKVIKLEQ
NYRSTQNILDAANAVIANNPGRLGKNLWTDNGEGEKVRLYVAPDEEEEARFVADEIRELHEEGVPLSDIA
VLYRTNAQSRALEEALRRAGIPYRVVGGLRFYERAEIKDLLAYLRLLANPDDDVALLRILNVPRRGIGAA
TLERLREAAREEGISLLEALRDLGELAGLSGRAAKALRRFAELLEALRAAAERLPLEELLEALLDESGYE
EELREEAGEEAERRLENLEELVDAAARFEERNPGASLEAFLEELALLSDLDAADEDEDAVTLMTLHAAKG
LEFPVVFLVGLEEGLFPHQRSLDDEEELEEERRLFYVAITRARERLYLTYAASRRLWGETQDNEPSRFLD
ELPEELLEWVRPKAEAAAAAASAAAALPASGAGAAALAAGAAAAAAAAGGGAAVAGAGLGRAAAAGGADG
GAAGAGGGLAAVALTVLPALL
>gnl|CDD|439981 COG0211, RpmA, Ribosomal protein L27 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L27 is part of the Pathway/BioSystem: Ribosome 50S subunit
MAHKKGGGSSRNGRDSNSKRLGVKRFGGQKVKAGNIIVRQRGTKFHPGKNVGMGKDHTLFALVDGVVKFE
RKGKGRKFVSVV
>gnl|CDD|439982 COG0212, FAU1, 5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism]
IAMDKKALRKELLARRRALSPEERAEASAAIAERLLALLEFRRAKTIALYLPIRGEVDTRPLIEALLARG
KRVALPVVVPDGRPLEFRRWTPGDPLEPGRFGIPEPVGDAPEVAPEEIDLVLVPLLAFDRRGYRLGYGGG
YYDRTLARLRPRPLTIGLAFDCQLVDELPVEPHDVPLDAIVTEKGV
>gnl|CDD|439983 COG0213, DeoA, Thymidine phosphorylase [Nucleotide transport and metabolism]. Thymidine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage
AVDIIRKKRDGGELTAEEIRFFIDGYTDGSIPDYQMAAFLMAVYFRGMTDEETAALTLAMRDSGDVLDLS
DIPGPKVDKHSTGGVGDKTSLVLAPLVAACGVPVPKMSGRGLGHTGGTLDKLESIPGFRTELSEEEFRRQ
VNEIGCAIIGQTGDLAPADKKLYALRDVTATVESIPLIASSIMSKKLAAGADALVLDVKVGSGAFMKTLE
DARELAESMVDIGNGAGRKTVALITDMNQPLGRAVGNALEVKEAIETLKGEGPEDLTELTLALGAEMLVL
AGLAKDLEEARAKLEEALASGKALEKFKEMVAAQGGDPDVVDDPELLPQAPVVREVKAPRSGYVSAIDAR
AIGLAAVLLGAGRATKEDPIDPAVGIVLLKKVGDKVEKGEPLATIHANDEADAEEAAERLRAAYTIGDEP
PEPPPLIYERI
>gnl|CDD|439984 COG0214, PdxS, Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]. Pyridoxal 5'-phosphate synthase subunit PdxS is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
LETGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIM
EAVSIPVMAKVRIGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGE
GAAMIRTKGEAGTGNVVEAVRHMRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFA
AGGIATPADAALMMQLGADGVFVGSGIFKSEDPEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDIS
TLPEEERLQERGW
>gnl|CDD|439985 COG0215, CysS, Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
TLKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDV
DDKIIKRAAEEGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGD
VYFDVRSFPDYGKLSGRNLDDLRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSA
MSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLL
KKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLYNALRRLEEALGAADSSAEEIEELREEFIAAM
DDDFNTPEALAVLFELVREINKALDEGEDKAALAALAALLRALGGVLGLLLLEPEAWQGAAEDELLDALI
EALIEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTTWRRK
>gnl|CDD|439986 COG0216, PrfA, Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]. Protein chain release factor RF1 is part of the Pathway/BioSystem: Translation factors
SMLDKLEALEERYEELEALLSDPEVISDQKRFRKLSKEYAELEPIVEAYREYKKLLEDIEEAKELLEEES
DPEMREMAKEELEELEARLEELEEELKILLLPKDPNDDKNVILEIRAGTGGDEAALFAGDLFRMYSRYAE
RKGWKVEILSASEGELGGYKEVIFRISGEGVYSRLKFESGVHRVQRVPETESQGRIHTSAATVAVLPEAE
EVDVEINPKDLRIDTFRSSGAGGQHVNTTDSAVRITHLPTGIVVECQDERSQHKNKAKAMKVLRARLYEA
EQQKQQAEIAAERKSQVGSGDRSERIRTYNFPQGRVTDHRINLTLYKLDEVMEGDLDELIDALIAEDQAE
KLAALE
>gnl|CDD|439987 COG0217, TACO1, Transcriptional and/or translational regulatory protein YebC/TACO1 [Transcription, Translation, ribosomal structure and biogenesis]
AGHSKWANIKHRKGAQDAKRGKIFTKLIREITVAAKEGGGDPEGNPRLRLAIQKAKAANMPKDNIERAIK
KGTGELDGANYEEITYEGYGPGGVAVLVECLTDNRNRTAAEVRHAFSKNGGNLGETGSVSFMFDRKGVIV
IPKEGVDEDELMEAALEAGAEDVEEDDDSFEVYTAPEDFGAVREALEEAGIEPESAELTMIPQTTVELDD
EDAEKVLKLIDALEDLDDVQNVYTNFDISDEVMEEL
>gnl|CDD|439988 COG0218, EngB, GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning]
MKIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDK
FYLVDLPGYGYAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIV
LTKADKLKKSELAKQLKAIKKALGKDPAAPEVILFSSLKKEGIDELRAAIEEWL
>gnl|CDD|439989 COG0219, TrmL, tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL, contains SPOUT domain [Translation, ribosomal structure and biogenesis]. tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL, contains SPOUT domain is part of the Pathway/BioSystem: tRNA modification
MLHIVLYEPEIPQNTGNIIRLCAATGARLHLIEPLGFSLDDKKLKRAGLDYWELVDLTVHDSWEAFLEAL
PGGRLFLFTTKGTKPYTDVDYQPGDVLLFGRETAGLPEEVLAAPADQRLRIPMRPGVRSLNLSNAVAIVL
YEALRQLGFPGLV
>gnl|CDD|439990 COG0220, TrmB, tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]. tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification
LTPFQQRVLEELLPLGLDLKGPLDWAELFGNDAPLVLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVA
KALKKAEEEGLTNVRLLRGDAVELLELFPDGSLDRIYLNFPDPWPKKRHHKRRLVQPEFLALLARVLKPG
GELHLATDWEDYAEEMLEVLSAHPGFENLAETGDYAPRPEDRPLTKYERKGLRLGRPIYYLIFR
>gnl|CDD|439991 COG0221, Ppa, Inorganic pyrophosphatase [Energy production and conversion]
MNLHDIPPGKNAPEEVNVVIEIPKGSRVKYEYDKETGALRVDRVLYTSMHYPANYGFIPQTLAEDGDPLD
VLVLTPEPTFPGCVIRARPIGVLKMEDEGGRDDKILAVPVDDPRYDHIKDISDLPPHLLDEIEHFFEHYK
DLEGKWVKVEGWGGAEEAKKEIEEAIERYKKKFG
>gnl|CDD|439992 COG0222, RplL, Ribosomal protein L7/L12 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L7/L12 is part of the Pathway/BioSystem: Ribosome 50S subunit
MALTKEEIIEAIKELTVLELSELVKALEEKFGVSAAAPVAVAAAAAAAAAAAAEEKTEFDVILKSAGDKK
IAVIKVVREITGLGLKEAKDLVEGAPKPVKEGVSKEEAEEIKKKLEEAGAKVELK
>gnl|CDD|439993 COG0223, Fmt, Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]
MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPAGRGRKLTPSPVKELALEHGIPVLQPESLKDPEF
LEELRALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDE
GLDTGDILLQEEVPIGPDDTAGSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGR
IDWSRPAEEIHRLIRALNPWPGAFTTLDGKRLKIWKARVLEEAGGGAPGTILAVDKDGLLVACGDGALRL
LELQPAGKKRMSAADFLRGYRLKPGERL
>gnl|CDD|439994 COG0224, AtpG, FoF1-type ATP synthase, gamma subunit [Energy production and conversion]. FoF1-type ATP synthase, gamma subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
MASLKEIRRRIKSVKSTQKITKAMKMVAASKLRKAQERAEAARPYAEKLREVLAALAAASPEYDHPLLEE
REVKRVGLIVITSDRGLCGGFNSNVLKAAEELIKELQAEGKEVELIVVGRKGRDFFKRRGINVVAEFTGL
SDKPSFEDAKEIAEELLDAFLAGEIDEVYLVYNRFVSAITQEPVVEQLLPLDPEELEEAEWETRADYIFE
PSPEEILDALLPRYLESQIYQALLESAASEHAARMTAMKNATDNAGELIDDLTLEYNRARQAAITQELSE
IVGGAEAL
>gnl|CDD|439995 COG0225, MsrA, Peptide methionine sulfoxide reductase MsrA [Posttranslational modification, protein turnover, chaperones]
PAGTETATFAGGCFWCVEAVFEQLPGVISVVSGYAGGHTPNPTYEEVCSGRTGHAEAVQVTYDPAVISYE
ELLEVFFEIHDPTQLNRQGNDRGTQYRSAIFYHDEEQKEIAEASIAALQASLDGPIVTEIEPAKTFYPAE
DYHQDYLAKNPNGYYCYRVGTGKVAKLRKLFPDKLKP
>gnl|CDD|439996 COG0226, PstS, ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and metabolism]
AASGTITIAGSSTVYPLAEAWAEAFQKANPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELEAA
KENGVELVEIPVAIDGIAVVVNPDNPVKNLTGEQLADIFSGKITNWNDIGGKLPDEPITVVGRSDGSGTT
DYFTEYLLGVGAEVREGVEGAEGNEGVVQAVAQTPGAIGYVGLSYAEQNKLKALAIDNKAGKFVEPTAEN
IAAGSYPLSRPLYIYVKKEPDAKAPAVKAFLDFVLSDGGQKIVEKLGYVPLPDAVVEKVRAALKA
>gnl|CDD|439997 COG0227, RpmB, Ribosomal protein L28 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L28 is part of the Pathway/BioSystem: Ribosome 50S subunit
MSRVCEITGKGPMFGNNVSHSNRKTKRRFLPNLQKVRVWVDSGRPVRLRVSTRCLRTIDKKGKVDRAL
>gnl|CDD|439998 COG0228, RpsP, Ribosomal protein S16 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S16 is part of the Pathway/BioSystem: Ribosome 30S subunit
MVKIRLARGGAKKRPFYRIVVADSRSPRDGRFIERIGFYNPLTNPARIKLDEERAQYWLSKGAQPTDTVA
KLLKKA
>gnl|CDD|439999 COG0229, MsrB, Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, chaperones]
MTYKVKKSDAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPS
FTKPIDPGAVEEKEDRSHGMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKEE
>gnl|CDD|440000 COG0230, RpmH, Ribosomal protein L34 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L34 is part of the Pathway/BioSystem: Ribosome 50S subunit
MKRTYQPSKRKRKRTHGFRARMSTKNGRKVLKRRRAKGRKRLTV
>gnl|CDD|440001 COG0231, Efp, Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ribosomal structure and biogenesis]. Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) is part of the Pathway/BioSystem: Translation factors
MISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREM
QYLYNDGDGYVFMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGV
KGDTATGGTKPATLETGAVVQVPLFIEEGDKIKVDTRTGEYVERAK
>gnl|CDD|440002 COG0232, Dgt, dGTP triphosphohydrolase [Nucleotide transport and metabolism]
DDIRSPFQRDRDRIIHSAAFRRLQDKTQVFPLPEGDHYRTRLTHSLEVAQIARSIARALGLNEDLVEAAA
LAHDLGHPPFGHAGEDALNELFRDLGGFEGNAQSLRILTRLEKRYAFGGLNLTYATLDGILKYPGPSLAA
PKPKPKGFYQSEKDVFDWVREELGLLALGRPRTLEAQIVELADDIAYSVHDLEDAIRAGLLSLEDLPELL
EYLGPLDERRRLGELRSRLIGRLVTDVIEASRENLFDGPLIAFSPEVAAALKELKKFLFERVYRHPEVLR
LELKGRRIIRELFDAFLEDPLELLPEEFRERYEAADDEYGRLRVVADYIAGMTDRYALRLYRRLF
>gnl|CDD|440003 COG0233, Frr, Ribosome recycling factor [Translation, ribosomal structure and biogenesis]
MIDEILKDAEEKMEKAIEALKEELAKIRTGRASPSLLDGIKVDYYGSPTPLNQVANISVPEARTLVIQPW
DKSMLKAIEKAIRKSDLGLNPSNDGNVIRIPIPPLTEERRKELVKVVKKEAEEAKVAIRNIRRDANDDLK
KLEKDKEISEDELKRAEDEIQKLTDKYIKKIDELLKAKEKEIMEV
>gnl|CDD|440004 COG0234, GroES, Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones]
KIKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEKPQEGEVVAVGPGKLLDNGKRVPLDVKVGDKVLFGKYA
GTEVKIDGEEYLILRESDILAVVEE
>gnl|CDD|440005 COG0235, AraD, 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]. 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle
MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDL
KPSSETPLHLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPGTEELAE
AIAEALGDRPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLVLSDEEIDKLARKFG
>gnl|CDD|440006 COG0236, AcpP, Acyl carrier protein [Lipid transport and metabolism]. Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
MPREELEERLAEIIAEVLGVDPEEITPDDSFFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVAD
LADYLEEKLA
>gnl|CDD|440007 COG0237, CoaE, Dephospho-CoA kinase [Coenzyme transport and metabolism]. Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
MLIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALA
EIVFADPEALKKLEAIVHPLVREEIERRLAAARGAPYVVLDIPLLFETGLEKLVDRVIVVDAPEEVQIER
LMARDGLSEEEAEARIAAQMPDEEKRARADFVIDNDGSLEELRAQVDALLEKL
>gnl|CDD|440008 COG0238, RpsR, Ribosomal protein S18 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S18 is part of the Pathway/BioSystem: Ribosome 30S subunit
MAKLRPRRRRFRRKKVCRFCADKIEYIDYKDVELLKKFISERGKILPRRITGTCAKHQRQLATAIKRARH
LALLPYVVDHL
>gnl|CDD|440009 COG0239, CrcB, Fluoride ion exporter CrcB/FEX, affects chromosome condensation [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism]
MKTLLLVALGGALGALLRYLLSLLLPRLFGSGFPWGTLAVNVLGSFLLGLLLGLLARRGLLSPELRLLLG
TGFLGGFTTFSTFSLETVRLLERGRYLLALLYVLLSVVLGLLAAALGLALARRLA
>gnl|CDD|440010 COG0240, GpsA, Glycerol-3-phosphate dehydrogenase [Energy production and conversion]. Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEEINETRENPRYLPGVKLPENLRATSDLEEALAG
ADLVLLAVPSQALREVLEQLAPLLPPGAPVVSATKGIEPGTGLLMSEVIAEELPGALRIAVLSGPSFAEE
VARGLPTAVVVASEDEEVAERLQELLSTPYFRVYTSDDVIGVELGGALKNVIAIAAGIADGLGLGDNARA
ALITRGLAEMTRLGVALGARPETFMGLAGLGDLVLTCTSDLSRNRRFGLALGKGKSLEEALAEMGMVAEG
VYTAKAVYELAEKLGVEMPITEAVYAVLYEGKSPREAVEALMARPLK
>gnl|CDD|440011 COG0241, HisB1/GmhB, Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]. Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis
MMKKAVFLDRDGTINEDVGYVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVH
AKMLELLAAEGGRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGC
KGILVLTGKGAEELAEALPDTVADDLAEAVDYLLAE
>gnl|CDD|440012 COG0242, Def, Peptide deformylase [Translation, ribosomal structure and biogenesis]
MAILPILQYGDPVLRKVAKPVTEFDDELRALIDDMFETMYAAPGVGLAAPQVGVSLRLFVIDVSDEDGKG
EPLVLINPEIVEASGETVEGEEGCLSVPGIRGEVPRPERVRVRYLDLDGEPVELEAEGLLARCIQHEIDH
LDGILFIDRLSPLKRERILKKLE
>gnl|CDD|440013 COG0243, BisC, Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]
MSLRDFKAAGAGAAALEAAGTKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALD
ERLYSPDRLTYPMKRVGPRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGGSAGRLSNEAAY
LAQRFARALGTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLR
EAAKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTVGFDELAAY
VAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGG
PFSLTGEAILDGKPYPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTW
LERDDIVTNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWGRTEEDYLRELLEATRGRGI
TFEELREKGPVQLPVPPEPAFRNDGPFPTPSGKAEFYSETLALPPLPRYAPPYEGAEPLDAEYPLRLITG
RSRDQWHSTTYNNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAP
HGWWYEPADDKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKAAA
>gnl|CDD|440014 COG0244, RplJ, Ribosomal protein L10 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L10 is part of the Pathway/BioSystem: Ribosome 50S subunit
MTREEKKAVVAELKEKLKEAQAVVLTDYRGLTVAQMTELRRKLREAGVEYKVVKNTLARIALEGTGFEGL
DDLLKGPTAIAFSYEDPVAAAKVLKDFAKENEKLVIKGGVLDGKVLDAEQVKALAKLPSREELLAKLLGL
LQAPATKLVGVLNAPPRKLARVLKAIAEKKEA
>gnl|CDD|440015 COG0245, IspF, 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase [Lipid transport and metabolism]. 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
MMRIGIGYDVHRFVEGRPLILGGVEIPHEKGLLGHSDADVLLHALCDALLGAAGLGDIGTHFPDTDPRWK
GADSRVLLREVVRLVREKGYRIGNVDVTIIAQRPKLAPHIEAMRANLAEALGIPVDRVSVKATTTEGLGF
TGRGEGIAAQAVALLEK
>gnl|CDD|440016 COG0246, MtlD, Mannitol-1-phosphate/altronate dehydrogenases [Carbohydrate transport and metabolism]
MKKLNRATLSALPAGVARPAYDRSALPPGIVHFGVGNFHRAHQAWYTDRLLNAGDFDWGIVGVGLRSGDA
LRDALAAQDGLYTLVERGPDGVEEARVIGSISEVLVAPEDPEAVLALLADPALRIVSLTITEKGYCLDPA
TGELDLDHPDIQADLANPAPPRSAPGKLTAALYRRRAAGLKPFTVLSCDNLPHNGDVLREAVLAFARLWD
PELADWIEENVTFPNTMVDRIVPATTDEDRARLAAELGYEDAAPVVAEPFRQWVIEDDFPAGRPPLEKAG
VQFVDDVAPYEEMKLRLLNGSHTALAYLGYLAGYETVAEAMADPLLRAFVRRLMLEEIIPTLPPPPGVDL
EAYADAVLERFANPAIRHTLARIALDGSQKLPQRLLPTLRDYLAAGRDPKRLALAVAAWLRYLRGVDDDG
EPIELSDPLADELAALAAAADDPADLVRAFLALEAIFGDDLADDPGFVEAVTAALEELLAKGARATLAAL
LA
>gnl|CDD|440017 COG0247, GlpC, Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion]
LSGGHGGGLKAEHGTGRFMAPFLELELGKIKYAFDPDNKLNPGKIGLLNPGVELLGDGDLHDKNLKTLPW
KELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELPLDLSEEVYEVLDLCLTCKACE
TACPSGVDIADLIAEARAQLVERGGRPLRDRLLRTFPDRVPAADKEGAEVLLFPGCFTNYFDPEIGKAAV
RLLEAAGVEVVLPPEELCCGAPALSKGDLDLARKLARRNIEALERLGVKAIVTTCPSCGLTLKDEYPELL
GDRVAFEVLDISEFLAELILEGKLKLKPLGEKVTYHDPCHLGRGGGVYDAPRELLKAIPGVEVVEMPEDS
GCCGGAGGYGFEEPELSMRIGERKLEQIRATGADVVVTACPSCRTQLEDGTKEYGIEVKHPVELLAEALG
>gnl|CDD|440018 COG0248, GppA, Exopolyphosphatase/pppGpp-phosphohydrolase [Nucleotide transport and metabolism, Signal transduction mechanisms]
APMRLAAIDIGSNSVRLLIAEVDEGGSFRILDREKEPVRLGEGLDATGRLSEEAIERALAALKRFAELLR
EYGVERVRAVATSALREAKNGDEFLDRVKEETGLPIEVISGEEEARLIYLGVLSGLPLSDGRGLVVDIGG
GSTELILGDGGEILFSESLPLGAVRLTERFFPDDPPTAEEFAAAREYIREELEPLAKELRKGGPDTLVGT
GGTIRTLARLLLALGRYDEKVHGYTLTREELEELIERLLSLTLEERAKLPGLSPDRADVILAGAAILEAL
MEALGIEEIVVSDRGLREGLLYDLLGRDGKKDDR
>gnl|CDD|440019 COG0249, MutS, DNA mismatch repair ATPase MutS [Replication, recombination and repair]
MSDMAKLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAEKASRLLDITLTKRGKGAGEPIPMAGVPY
HAAEGYLAKLVKAGYKVAICEQVEDPAEAKGLVKREVVRVVTPGTLTEDALLDAKRNNYLAAVARDKGRY
GLAWLDISTGEFLVTELDGEEALLDELARLAPAEILVPEDLPDPEELLELLRERGAAVTRLPDWAFDPDA
ARRRLLEQFGVASLDGFGLEDLPAAIAAAGALLAYLEETQKGALPHLRRLRRYEEDDYLILDAATRRNLE
LTETLRGGRKGSLLSVLDRTVTAMGSRLLRRWLLRPLRDRAAIEARLDAVEELLEDPLLREELRELLKGV
YDLERLLSRIALGRANPRDLAALRDSLAALPELKELLAELDSPLLAELAEALDPLEDLAELLERAIVDEP
PLLIRDGGVIREGYDAELDELRELSENGKEWLAELEARERERTGIKSLKVGYNKVFGYYIEVTKANADKV
PDDYIRKQTLKNAERYITPELKELEDKILSAEERALALEYELFEELREEVAAHIERLQALARALAELDVL
ASLAEVAVENNYVRPELDDSPGIEIEGGRHPVVEQALPGEPFVPNDCDLDPDRRILLITGPNMAGKSTYM
RQVALIVLLAQIGSFVPAESARIGIVDRIFTRVGASDDLARGQSTFMVEMTETANILNNATERSLVLLDE
IGRGTSTYDGLSIAWAVAEYLHDKIRARTLFATHYHELTELAEKLPGVKNYHVAVKEWGGDIVFLHKVVP
GPADRSYGIHVAKLAGLPASVIERAREILAELEKGEAAAAGKAAPDQLSLFAAADPEPSPVLEELKALDP
DELTPREALNLLYELKKLLKE
>gnl|CDD|440020 COG0250, NusG, Transcription termination/antitermination protein NusG [Transcription]
MSMEKRWYVVHTYSGYEKKVKENLERRIEGIEVFVPTEEVVEIKNGKKKTVERPLFPGYVFVRMDLTDES
WYLVRNTPGVTGFVGFGGKPAPLPDEEVERILARLEEGEEKPRPKVDFEVGDRVRITDGPFAGFEGTVEE
VDPEKGRVKVLVSIFGRETPVELDFSQVEKI
>gnl|CDD|440021 COG0251, RidA, Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]. Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation
MTRELINPPAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDD
VVKVTVYLTDMADFAAVNEVYAEYFGEGRPARTAVGVAALPKGALVEIEAIAALP
>gnl|CDD|440022 COG0252, AnsA, L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal structure and biogenesis, Amino acid transport and metabolism]
MMMPKILVLATGGTIAMRADPAGYAVAPALSAEELLAAVPELAELADIEVEQFANIDSSNMTPADWLALA
RRIEEALADDYDGVVVTHGTDTLEETAYALSLMLDLPKPVVLTGAQRPADAPSSDGPANLLDAVRVAASP
EARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEGRVRFYRRPPRRPESELDLAPALLP
RVAILKLYPGMDPALLDALLAAGVKGIVLEGTGAGNVPPALLPALKRAIERGVPVVVTSRCPEGRVNGVY
GGGRDLAEAGVISGGDLTPEKARIKLMLALGQGLDPEEIRRLFET
>gnl|CDD|440023 COG0253, DapF, Diaminopimelate epimerase [Amino acid transport and metabolism]. Diaminopimelate epimerase is part of the Pathway/BioSystem: Lysine biosynthesis
MTLPFTKMHGLGNDFVVIDARDQPLELTPELARALCDRHFGIGADGLLLVEPSDGADFRMRIFNADGSEA
EMCGNGARCFARYLYDKGLTGKDEFTVETLAGVLRVEVEEDGLVTVDMGPPRFEPAEIPLAGEEDTIDYP
LEVGGETLTGTAVSMGNPHAVIFVDDLDAADLETLGPLIEHHPLFPERVNVEFVQVLDPDHIRLRVWERG
VGETLACGTGACAAAVAAIRLGLLDRKVTVHLPGGDLTIEWDEDGHVYMTGPAETVFEGEIDLEAL
>gnl|CDD|440024 COG0254, RpmE, Ribosomal protein L31 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L31 is part of the Pathway/BioSystem: Ribosome 50S subunit
MKKGIHPEYREVVVTCSCGNEFLTRSTLEYPEIKVDVCSACHPFYTGKQKIVDTAGRVEKFNKRYGKFGK
KK
>gnl|CDD|440025 COG0255, RpmC, Ribosomal protein L29 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L29 is part of the Pathway/BioSystem: Ribosome 50S subunit
MKAKELRELSDEELKEKLKELKKELFNLRFQHATGQLENPHRIREVRRDIARIKTVLREKELAAA
>gnl|CDD|440026 COG0256, RplR, Ribosomal protein L18 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L18 is part of the Pathway/BioSystem: Ribosome 50S subunit
PRYKKKARRRRHYRVRKKISGTSERPRLVVFRSNKHIYAQIIDDTGGKTLASASTLEKELRKKLGSGGNT
EAAYLVGKLIAERAKAKGIEEVVFDRGGYLYHGRVKALADGAREAGLKF
>gnl|CDD|440027 COG0257, RpmJ, Ribosomal protein L36 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L36 is part of the Pathway/BioSystem: Ribosome 50S subunit
MKVRASVKKICRDCKVVRRKGRVYVICKKNPRHKQRQG
>gnl|CDD|440028 COG0258, ExoIX, 5'-3' exonuclease Xni/ExoIX (flap endonuclease) [Replication, recombination and repair]
MMPMKKLLLIDGSSLLFRAFYALPPLTNSDGQPTNAVYGFTNMLLKLLKEEKPTHLAVAFDAKGPTFRHE
LYPEYKANRPEMPEELRPQIPLIKEVLEALGIPVLEVEGYEADDVIGTLAKQAEAEGYEVLIVTGDKDLL
QLVDDNVTVLDPMKGVSELERYDPAEVEEKYGVPPEQIIDYLALMGDSSDNIPGVPGIGEKTAAKLLQEY
GSLENILANADEIKGKLREKLRENKEQARLSRKLATIKTDVPLPFDLEDLKLRPPDREALRELFEELEFK
SLLKRL
>gnl|CDD|440029 COG0259, PdxH, Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]. Pyridoxine/pyridoxamine 5'-phosphate oxidase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
MSDLADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDE
RGFVFYTNYESRKGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQ
SQPIASREELEARFAELEARFAGGDVPRPPHWGGYRVVPDRIEFWQGRPSRLHDRLRYTREDGGWTIERL
AP
>gnl|CDD|440030 COG0260, PepB, Leucyl aminopeptidase [Amino acid transport and metabolism]
MKISLSSASLAKLSADALVVGVFEGGDLSPAAAALDAALGGALAALLAAGGFKGKAGETLLLPGPPGLAA
ERVVLVGLGKAEELDAEDLRKAAAAAARALKKAGAKSVAVALPELPDDAEAAEAAAEGALLGAYRFDRYK
SKKKEPPPLEELTLVVPDAAAAEAALARAEAIAEGVNLARDLVNTPANDLTPEELAERAKELAKEHGLKV
EVLDEKELEKLGMGALLAVGQGSARPPRLIVLEYKGGGKAKPPVALVGKGVTFDTGGISLKPAAGMEEMK
KDMGGAAAVLGAMKAIAELKLPVNVVGLIPAVENMPSGNAYRPGDVLTSMSGKTVEVLNTDAEGRLVLAD
ALTYAAERFKPDLIIDLATLTGACVVALGPDTAGLFSNDDALADELLAAGEAAGEPVWRLPLWDEYREQL
KSDIADLKNIGGRFAGAITAALFLRRFVGDTPWAHLDIAGTAWNSGARPYRPKGATGFGVRLLVELLEDR
AE
>gnl|CDD|440031 COG0261, RplU, Ribosomal protein L21 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L21 is part of the Pathway/BioSystem: Ribosome 50S subunit
MYAIIETGGKQYKVEEGDVLKVEKLDAEAGDTVEFDKVLLVGDGGKVKVGAPYVEGAKVTAEVVEHGKGK
KVIVFKFKRRKGYRRKQGHRQPYTRVKITSINA
>gnl|CDD|440032 COG0262, FolA, Dihydrofolate reductase [Coenzyme transport and metabolism]. Dihydrofolate reductase is part of the Pathway/BioSystem: Folate biosynthesis
RKLILIVAVSLDGVIGGPDGDLPWLFPDPEDLAHFKELTAGADAVLMGRKTYESIAGYWPTRPLPGRPKI
VLSRTLDEADWEGVTVVSGDLEEALAALKAAGGKDIWVIGGGELYRQLLPAGLVDELYLTVVPVVLGEGD
RLFPELDAPSRLELVESEADSGFVHLTY
>gnl|CDD|440033 COG0263, ProB, Glutamate 5-kinase [Amino acid transport and metabolism]. Glutamate 5-kinase is part of the Pathway/BioSystem: Proline biosynthesis
REALAKARRIVVKIGSSLLTDEGGGLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGLPKRPK
TLPEKQAAAAVGQGLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINEND
TVATDEIRFGDNDRLAALVANLVEADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEITPEIEAMAGGAGS
GLGTGGMATKLEAARIATRAGIPTVIASGREPNVLLRILAGERVGTLFLPSGEPLSARKRWIAGALQPRG
RLVVDAGAVRALRERGKSLLPAGVTAVEGDFERGDVVEIVDPDGREIARGLVNYSSDELRRIKGRRSDEI
EAILGYKGRDEVIHRDNLVLL
>gnl|CDD|440034 COG0264, Tsf, Translation elongation factor EF-Ts [Translation, ribosomal structure and biogenesis]. Translation elongation factor EF-Ts is part of the Pathway/BioSystem: Translation factors
AAITAALVKELRERTGAGMMDCKKALTEADGDIEKAIEILRKKGLAKAAKKAGRVAAEGLVAVAVDGKKG
AIVEVNCETDFVAKNEDFQAFANEVAEAALAAKPADVEALLAAPLDGKTVEEAITELIAKIGENISLRRF
ARLEVGGVVGSYVHNGGKIGVLVALEGDADEELAKDIAMHIAAMNPKYLSREDVPAEVVEKEREIATEQA
REEGKPENIIEKIVEGRLNKFLKEVTLLEQPFVKDPKKTVGQLLKEAGAKVVGFVRFEVGEGIEKKEEDF
AAEVAAQAKG
>gnl|CDD|440035 COG0265, DegQ, Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]
GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDLPAAPLGDSDK
LRVGDWVLAIGNPFGLGQTVTAGIVSALGRSIGSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGIN
TAIISRSGGSQGIGFAIPINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELAEALGLPEPEGVLVARVEP
GSPAAKAGLRPGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGERPE
>gnl|CDD|440036 COG0266, Nei, Formamidopyrimidine-DNA glycosylase [Replication, recombination and repair]
PELPEVETVRRGLAPALVGRTITRVEVRSPRLRFPVPEDFAARLTGRRITAVERRGKYLLLELDGGLTLL
IHLGMSGRLRVVPPGEPPEKHDHVRLVLDDGTELRFADPRRFGALELLTPDELEVHPLLARLGPEPLDPD
FDPEYLAARLRRRRRPIKALLLDQSVVAGVGNIYADEALFRAGIHPLRPAGSLSRAELERLAAAIREVLR
EAIEAGGTTLRDYVNADGEPGYFQQRLYVYGREGEPCPRCGTPIERIVLGGRSTYYCPRCQR
>gnl|CDD|440037 COG0267, RpmG, Ribosomal protein L33 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L33 is part of the Pathway/BioSystem: Ribosome 50S subunit
MAGMREKITLACTECKGRNYTTTKNKRNTPERLELKKYCPKCRKHTLHKETK
>gnl|CDD|440038 COG0268, RpsT, Ribosomal protein S20 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S20 is part of the Pathway/BioSystem: Ribosome 30S subunit
MANIKSAKKRIRQNEKRRLRNRARKSRLRTAIKKVRKAIAAGDKEAAQEALKAAQSKLDKAASKGVIHKN
KAARKKSRLAKKVNALA
>gnl|CDD|440039 COG0269, UlaD, 3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism]
MMKPKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGA
LEAEMAFKAGADIVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWDPVERAKELEELGVDIVILHRGI
DAQAAGGSPLDDLKKIKELVGVPVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAID
KA
>gnl|CDD|440040 COG0270, Dcm, DNA-cytosine methylase [Replication, recombination and repair]
SKKLTVIDLFAGAGGLSLGFEKAGFEVVFAVEIDPDACETYRANFPEAKVIEGDIRDIDPEELIPDVDLL
IGGPPCQPFSVAGKRKGLEDPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFEEILKELEELGY
RVDYKVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTHLKPYVTVGDALEDLPDAHEARYLSETITAG
YGGGGRFLHPGEPRRLTVREAARLQGFPDDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAILKALEKL
>gnl|CDD|440041 COG0271, BolA, DNA-binding global transcriptional regulator BolA, affects cell shape, cell division and biofilm formation [Transcription, Signal transduction mechanisms]
MSRQERIEEKLTAALAPEHLEVIDESHLHAGHAGAGGESHFKVVIVSDAFAGKSRVARHRLVYAALADEL
AGGIHALAIHAYTPEEWQAR
>gnl|CDD|440042 COG0272, Lig, NAD-dependent DNA ligase [Replication, recombination and repair]
MTPEEAKERIEELREELRRHNYRYYVLDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLE
GFAKVRHAVPMLSLDNAFSEEELRDFDRRVRKFLGDEPVEYVCELKIDGLAISLRYENGRLVRAATRGDG
TVGEDVTANVRTIRSIPLRLKGDDVPEVLEVRGEVYMPKADFEALNEEREEAGEKPFANPRNAAAGSLRQ
LDPKITAKRPLDFFAYGLGEVEGLLPDTQSEALELLKEWGFPVNPERRVCKSIEEVLAYIEEWEEKRHSL
PYEIDGVVIKVNDLALQERLGFTSRAPRWAIAYKFPAEEATTKLLDIEVQVGRTGALTPVARLEPVFVAG
VTVSRATLHNEDEIERKDVRIGDTVVVRKAGDVIPEVVGVVLEKRPGDEKPFVMPTHCPVCGSPLVREEG
EAALRCTNGLSCPAQLKERLKHFASRKAMDIEGLGEKLIEQLVDAGLVKDPADLYRLTKEDLLGLERMGE
KSAQNLLAAIEKSKKTPLARFLFALGIRHVGETTAKLLARHFGSLDALMAASEEELAAVDGIGPVVAESI
VEFFAEPHNRELIERLRAAGVNMEEEEAEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSV
SKKTDYVVAGENAGSKLDKAEELGVPILDEAEFLELLG
>gnl|CDD|440043 COG0274, DeoC, Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism]
KELAKLIDHTLLKPDATEEDIEKLCEEAKEYGFAAVCVNPCYVPLAAELLKGSGVKVATVIGFPLGATTT
EVKVAEAKEAVADGADEIDMVINIGALKSGDYDAVEEEIAAVVEAAGGAVLKVILETGLLTDEEIRKACE
LAIEAGADFVKTSTGFGPGGATVEDVRLMRETVGGRVGVKASGGIRTLEDALAMIEAGATRIGTSSGVAI
LEGLEARSS
>gnl|CDD|440044 COG0275, RmsH, 16S rRNA C1402 N4-methylase RsmH [Translation, ribosomal structure and biogenesis]. 16S rRNA C1402 N4-methylase RsmH is part of the Pathway/BioSystem: 16S rRNA modification
MTAEFYHIPVLLEEVLEALAPKPGGVYVDGTLGGGGHSRAILERLGPGGRLIGIDRDPDAIAAAKERLAE
FGDRFTLVHGNFSELDEVLAELGIEKVDGILLDLGVSSPQLDDAERGFSFRRDGPLDMRMDPSQGLTAAD
VLNTYSEEELARILREYGEERFARRIARAIVEARKEKPITTTGELAEIIKRAVPAKARKGIHPATRTFQA
LRIEVNDELEELEEALEAALDLLKPGGRLAVISFHSLEDRIVKRFFREGSKGCECPPDLPVCECGHKPPL
KLLTKKPIVPSEEEIARNPRARSAKLRVAERI
>gnl|CDD|440045 COG0276, HemH, Protoheme ferro-lyase (ferrochelatase) [Coenzyme transport and metabolism]. Protoheme ferro-lyase (ferrochelatase) is part of the Pathway/BioSystem: Heme biosynthesis
MTPKTGVLLVNLGTPDSPEDVRPYLREFLSDRRVIEIPRLLWQPILAGIILPERPKKSAEAYESIGGGSP
LNVITRRQAAALQAELAERGDDVPVYLAMRYGNPSIEDALEELKADGVDRILVLPLYPQYSASTTGSYFD
DVARALKKLRWQPEIRFIRSYYDHPGYIEALAESIREALAELGREPDRLLFSAHGIPERYLDKGDPYPAQ
CEETARLVAEALGLPEDDWSLAFQSRFGPEPWLEPYTDDTLEELAKEGVKRVVVVPPGFVSDCLETLEEI
DIEARELFEEAGGEEFVRIPCLNDSPAFIEALADLVEERLAG
>gnl|CDD|440046 COG0277, GlcD, FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]
MLTAALLAALRAILAGRVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRG
GGTGLAGGAVPLDGGVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATI
GGNIATNAGGPRSLKYGLTRDNVLGLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATL
RLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALELMDRAALALVEAAPPLGLPEDGGALLLVEF
DGDDAEEVEAQLARLRAILEAGGATDVRVAADGAERERLWKARKAALPALGRLDGGAKLLEDVAVPPSRL
PELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERARAAAEEIFDLVAELGGSISGEHGI
GRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP
>gnl|CDD|440047 COG0278, GrxD, Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones]
MMDVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPT
IPQLYVKGEFIGGCDIIREMYESGELQKLLEEAGA
>gnl|CDD|440048 COG0279, GmhA, Phosphoheptose isomerase [Carbohydrate transport and metabolism]
MLDRIKQYFEESIEALQALAEALAEAIEAAAELLAEALLNGGKILVCGNGGSAADAQHFAAELVGRFERE
RPGLPAIALTTDTSVLTAIANDYGYDEVFARQVEALGRPGDVLLAISTSGNSPNVLRALEAARERGMTTI
ALTGRDGGKLAGLADIEIRVPSDSTARIQEVHLLIIHILCELIEAALFG
>gnl|CDD|440049 COG0280, Pta, Phosphotransacetylase (includes Pta, EutD and phosphobutyryltransferase) [Energy production and conversion]
KFFRPLIERAKAAPKRIVFAEGEDERVLRAAQEALDEGLAEPILVGRPEKIEARAEELGLDLSGFEIIDP
EDSPRYEEYAEAYYELRKRKGVTPEEARELVRDAAYFAAMMVRLGEADGLVKGAVGTTADLLRPVLQIIG
LRPGVKRVSHVFLMELPDRLLFITDTAVNIDPTAEQLADIAINAADTARAFGIEPKVALLSASEFGSPKG
PSTDKVREATKMARGQIPDLEVDGELQFDAALSPEAAKRKGPDSPVAGDANVLVFPDLEAGNILYKLLQR
LAGAEAIGPILLGLAKPVHLLSRGDSVRDIVNSIALAAVQ
>gnl|CDD|440050 COG0281, SfcA, Malic enzyme [Energy production and conversion]. Malic enzyme is part of the Pathway/BioSystem: Urea cycle
EDMERVETLEQEALEYHRIYDRGKILVYPTVPLHTQEDLSLAYTPGVAEACLEIAEDPRLAYGYTAKGNL
VAVVTDGTAVLGLGDIGPLAGMPVMEGKAVLFKAFAGIDAFPICLDTNDPDEFVEAVKALEPTFGGINLE
DIKAPNCFEIEERLREELDIPVFHDDQHGTAIVVLAALLNALKLVGKKLEDQKIVINGAGAAGIAIARLL
VAAGLSEENIIMVDSKGLLYEGRTDLNPYKREFARDTNPRGLKGTLAEAIKGADVFIGVSAPGAFTEEMV
KSMAKRPIIFALANPTPEITPEDAKAWGDGAIVATGRSDYPNQVNNVLIFPGIFRGALDVRATRITDEMK
LAAARALADLVDEEELGPDYIIPSPFDPRVSPAVAAAVAKAAIESGVARRPIDEDYREALEARM
>gnl|CDD|440051 COG0282, AckA, Acetate kinase [Energy production and conversion]
MKILVLNAGSSSLKFQLFDMDSEEVLAKGLVERIGLPGARLKHKDAGGEKVERELPIPDHAAALALVLEL
LTDHGIIKDLDEIDAVGHRVVHGGEKFSESVLIDDEVLAAIEELIPLAPLHNPANLAGIEAARELLPDLP
QVAVFDTAFHQTMPEVAYLYALPYELYEKYGIRRYGFHGTSHRYVAERAAELLGKPLADLRLITAHLGNG
ASLCAIKNGKSVDTSMGFTPLEGLVMGTRSGDIDPGVVLYLMRKEGLSADEVDDLLNKESGLLGLSGISS
DMRDLEEAAASGDERARLALDMFVYRIKKYIGAYAAALGGLDALVFTAGIGENSAEVRARVCEGLEFLGI
ELDPEANAARGGERVISTPDSRVKVLVIPTNEELMIARDTLRLLK
>gnl|CDD|440052 COG0283, Cmk, Cytidylate kinase [Nucleotide transport and metabolism]
PVIAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALARNLDIEFETDP
GGQRVFLNGEDVTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPGLVADGRDIGTVVFPDAELKI
FLTASAEERARRRYKELKEKGISVSLEELLADIKERDERDSTRAVAPLKPAEDAIVIDTTDLSIEEVVEK
ILALVRERLS
>gnl|CDD|440053 COG0284, PyrF, Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]. Orotidine-5'-phosphate decarboxylase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
KRSPLIVALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEGVEALKERGLPVFLDLKRHDIPNTVA
AAARAAAELGVDAVTVHAYGGRDMLEPALEAADESGKGVFAVTVLTSPGAADLQELGIEGPLYEVVLRLA
KLAKEAGLDGVVCSATEAAALRAALGPDFLLLTPGIRPQGGDAGDQKRVGTPAEAIAAGADYLVVGRPIT
YAGDPRAAAEAIREEIAA
>gnl|CDD|440054 COG0285, FolC, Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]. Folylpolyglutamate synthase/Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis
MTTYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVG
LYTSPHLVRFNERIRINGEPISDEELVEALEEVEPAVEEVDAGPPTFFEVTTAAAFLYFAEAPVDVAVLE
VGLGGRLDATNVIDPLVSVITSIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAA
ELGAPLYRAGRDFSVEEREGAVFSYQGPGGEYEDLPLPLLGAHQAENAALALAALEALRELGLPISEEAI
REGLANARWPGRLEVLSRGPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAP
LADEVIVTTPPSPRALDAEELAEAARELGLRVEVAPDVEEALEAALELADPDDLILVTGSLYLVGEVRAL
LGR
>gnl|CDD|440055 COG0286, HsdM, Type I restriction-modification system, DNA methylase subunit [Defense mechanisms]
DVLGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLDPKPGETVYDPACGSGGFLVEAAEYLKEHGG
DERKKLSLYGQEINPTTYRLAKMNLLLHGIGDPNIELGDTLSNDGDELEKFDVVLANPPFGGKWKKEELK
DDLLGRFGYGLPPKSNADLLFLQHILSLLKPGGRAAVVLPDGVLFRGAEKEIRKKLLENDLLEAIIGLPS
NLFYNTGIPTCILFLTKGKPERTGKVLFIDASK
>gnl|CDD|440056 COG0287, TyrA, Prephenate dehydrogenase [Amino acid transport and metabolism]. Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
FMRIAIIGLGLIGGSLALALKRAGLAHEVVGVDRSPETLERALELGVIDRAATDLEEAVADADLVVLAVP
VGATIEVLAELAPHLKPGAIVTDVGSVKGAVVEAAEALLPDGVRFVGGHPMAGTEKSGPEAADADLFEGA
PYILTPTEGTDPEALERVEELWEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVADLEDEEEILR
LAAGGFRDTTRIAASDPEMWRDIFLANREALLEALDRFIEELDALRDALEAGDGEALEELLERARAAR
>gnl|CDD|440057 COG0288, CynT, Carbonic anhydrase [Inorganic ion transport and metabolism]
MEALKRLLEGNRRFVAGKFPQDPERFEELAKGQHPFALVIGCSDSRVPPELIFDQGPGDLFVVRNAGNVV
PPYDPGVLASIEYAVEVLGVKLIVVLGHSGCGAVKAALDGLELEELGLIGNWLRHIRPAVERVRAELPAA
DGEERLDRLVELNVREQVENLRTSPIVREAVAAGKLKVHGWVYDLATGRVEFLDPEGGGFEPLP
>gnl|CDD|440058 COG0289, DapB, 4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]. 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis
IKIAVAGASGRMGRELIRAVLEAPDLELVAAIDRPGSPGQDAGELALGVPVTDDLEEALAKADVVIDFTH
PEATLENLEAALEAGVPVVIGTTGFSEEQLAELEEAAKGIPVLIAPNFSLGVNLLFKLAEEAAKYLGDDY
DIEIIEAHHRQKVDAPSGTALKLAEAIAEARGRDLDDVAVYGREGITGARKKGEIGIHSVRGGDIVGEHT
VIFAGEGERIEIRHDASSRESFAPGALLAARWLAGKPPGLYGMEDVL
>gnl|CDD|440059 COG0290, InfC, Translation initiation factor IF-3 [Translation, ribosomal structure and biogenesis]. Translation initiation factor IF-3 is part of the Pathway/BioSystem: Translation factors
MRPKKKKEPRINEEIRAPEVRLIGEDGEQLGIVSTREALRLAEEAGLDLVEISPNAKPPVCKIMDYGKFK
YEQQKKAKEAKKKQKVIEVKEIKFRPNIDEHDYETKLKNARRFLEEGDKVKVTVRFRGREMAHKELGEEL
LERFAEDLEDVAKVEQKPKLEGRQMIMVLAPKKKK
>gnl|CDD|440060 COG0291, RpmI, Ribosomal protein L35 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L35 is part of the Pathway/BioSystem: Ribosome 50S subunit
MPKMKTHSGAKKRFKVTGSGKIKRKKAGKRHLLTKKSTKRKRRLRGTTVVSKADAKRVKRLLPY
>gnl|CDD|440061 COG0292, RplT, Ribosomal protein L20 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L20 is part of the Pathway/BioSystem: Ribosome 50S subunit
ARVKRGVVARKRHKKILKLAKGYRGRRSRLYRVAKEAVMKALQYAYRDRRQKKRDFRRLWITRINAAARE
NGLSYSRFINGLKKAGIELNRKVLADLAVNDPAAFAALVEKAKAALA
>gnl|CDD|440062 COG0293, RlmE, 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]. 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification
MKMKRSKSSKRWLQRHLNDPYVKRAKKEGYRSRAAYKLLEIDEKDKLIKPGMRVVDLGAAPGGWSQVAAK
RVGGKGRVIALDLLPMEPIPGVEFIQGDFREDEVLDQLLEALGGRKVDLVLSDMAPNTSGHKSVDHARSM
YLVELALDFARKVLKPGGAFVVKVFQGEGFDELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGFKG
>gnl|CDD|440063 COG0294, FolP, Dihydropteroate synthase [Coenzyme transport and metabolism]. Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis
MTLGRTLDLSRPLVMGILNVTPDSFSDGGRYNDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEE
ELARVVPVIEALRAEFDVPISVDTYKAEVARAALEAGADIINDVSGLRFDPEMAEVAAEYGVPVVLMHMR
GTPQTMQRNPHYDDVVAEVRDFLEERIEAAEAAGIARERIILDPGIGFGKTLEHNLELLRRLDELRALGY
PVLVGVSRKSFIGALLGRPPEERLAGTLAAAALAAARGADIVRVHDVAETVDALKVADAIRRAR
>gnl|CDD|440064 COG0295, Cdd, Cytidine deaminase [Nucleotide transport and metabolism]. Cytidine deaminase is part of the Pathway/BioSystem: Pyrimidine salvage
MDDEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREI
KAIAVVADTGEPVSPCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL
>gnl|CDD|440065 COG0296, GlgB, 1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism]
LLGELDLYLFGEGRHYRLYEKLGAHPVEVDGVEGVRFAVWAPNARRVSVVGDFNGWDGRRHPMRRRGGSG
IWELFIPGLGPGDLYKYEIRGADGEVLLKADPYARYQELRPHTASVVVDPSAYEWQDDDWMGPRAKRNAL
DAPMSIYEVHLGSWRRKEGGRFLTYRELAERLVPYLKELGFTHIELMPVAEHPFDGSWGYQPTGYFAPTS
RYGTPDDFKYFVDACHQAGIGVILDWVPNHFPPDGHGLARFDGTALYEHADPRRGEHTDWGTLIFNYGRN
EVRNFLISNALYWLEEFHIDGLRVDAVASMLYLDYSREEGEWIPNKYGGRENLEAIHFLRELNETVYERF
PGVLTIAEESTAWPGVTRPTELGGLGFDAKWNMGWMHDTLRYMTKDPIYRKYHHNELTFSLVYAFSENFV
LPLSHDEVVHGKGSLLGKMPGDRWQKFANLRLLYAYMWTHPGKKLLFMGQEFGQWREWNYDEPLDWHLLD
YPPHAGLQRLVRDLNRLYREEPALHELDFDPEGFEWIDADDAENSVLAFLRKGKDGDDVLVVCNFTPVPR
ENYRIGVPRAGRWREILNSDAEEYGGSGVGNLGGVTAEEVPWHGRPYSLELTLPPLAAVVLKPEK
>gnl|CDD|440066 COG0297, GlgA, Glycogen synthase [Carbohydrate transport and metabolism]
MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIDDKLKDLEVVASLEVPLGGRTYY
ARVLEGPDDGVPVYFIDNPELFDRPGPYGDPDRDYPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQT
GLIPALLKTRYADDPFKRIKTVFTIHNLAYQGIFPAEILELLGLPPELFTPDGLEFYGQINFLKAGIVYA
DRVTTVSPTYAREIQTPEFGEGLDGLLRARSGKLSGILNGIDYDVWNPATDPYLPANYSADDLEGKAANK
AALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPG
RVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYGTVPIVRRTGGLADTVIDYNEATGEGTG
FVFDEYTAEALLAAIRRALALYRDPEAWRKLQRNAMKQDFSWEKSAKEYLELYREL
>gnl|CDD|440067 COG0298, HypC, Hydrogenase maturation factor HybG, HypC/HupF family [Posttranslational modification, protein turnover, chaperones]
MCLAIPGKVVEILDGDTALVDVGGVRREVSLALVPEVKVGDYVLVHVGFAIEKIDEEEAEETLELLEELG
AALEEVDA
>gnl|CDD|440068 COG0299, PurN, Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]. Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDA
ALLEALDAYGPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFV
DEEVDTGPIIAQAAVPVLPDDTEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDGE
>gnl|CDD|440069 COG0300, YqjQ, Short-chain dehydrogenase [General function prediction only]
MSLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVA
ALAEAVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVS
SVAGLRGLPGMAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLLSPEEVA
RAILRALERGRAEVYVGWDARLLARLLRLLPRLFDRLLRRAL
>gnl|CDD|440070 COG0301, ThiI, Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]. Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis
YKVILVRYGEIALKGKNRKRFEKRLVKNIRAALKDLGEVKVKREWGRIYVETDGEDAEEAIERLKKVFGI
VSFSPAVEVEKDLEDIKEAALELAKEELKGKTFKVRAKRAGKHFPFTSPELEREVGGALLENTPGLKVDL
KNPDVTIRVEVRDDKAYVYTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGP
YTSERAEEKVKDLARKLSRYGGHRVKLYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGAL
ALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIGMDKEEIIEIARKIGTYEISILPYEDCCTVFVPKH
PETKPKLEKVEKEEEKLDLEELLEEAVENAEV
>gnl|CDD|440071 COG0302, FolE, GTP cyclohydrolase I [Coenzyme transport and metabolism]. GTP cyclohydrolase I is part of the Pathway/BioSystem: Folate biosynthesis
DEPDREEIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVLNTTFEEGYDEMVLVKD
IEFYSMCEHHLLPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAV
VIEAEHMCMTMRGVRKPGSSTVTSAMRGVFREDPATRAEFLSLIRG
>gnl|CDD|440072 COG0303, MoeA, Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]. Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis
MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLR
VVGEIAAGSPPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAA
GDVLLPAGTRLTPADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLRE
AGAEVVDLGIVPDDPEALRAALREALAEADLVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPL
AFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLPPPPPPRVRARLAEDLPKKPGRTEFLRVRLER
DDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLLLDGL
>gnl|CDD|440073 COG0304, FabB, 3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]. 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDR
FTQYALAAAREALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMA
AGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRN
DDPEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARA
MRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIA
SVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGHNASLVFKRY
>gnl|CDD|440074 COG0305, DnaB, Replicative DNA helicase [Replication, recombination and repair]
NIEAEQAVLGALLLDNDALDEVADILKPEDFYRPAHRLIFEAILDLYERGEPIDLVTVAEELEKRGELEE
VGGAAYLAELAENVPSAANIEYYARIVKEKALLRRLIEAGTEIVELAYDEDEDVDELLDEAEQKIFEIAE
KRSSKGFVSISDILKEALERIEELYKNGGGITGVPTGFTDLDKLTGGLQPGDLIILAARPSMGKTAFALN
IARNAAIKEGKPVAIFSLEMSAEQLVMRLLSSEARIDSSKLRTGKLSDEDWERLSSAAGELSEAPIYIDD
TPGLTIAEIRAKARRLKREHGLGLIVIDYLQLMSGSGRSENRQQEISEISRSLKALAKELNVPVIALSQL
SRAVEQRTDKRPQLSDLRESGSIEQDADVVMFLYRDEYYNPDSEDKGIAEIIIAKQRNGPTGTVKLAFDG
EYTRFENLA
>gnl|CDD|440075 COG0306, PitA, Phosphate/sulfate permease [Inorganic ion transport and metabolism]
MMTLLLLIVVILLALFFDFNNGFHDAANAIATAVGTRALSPRTAVLLAAVFNFLGALLFGTAVAKTIGKG
IVDPGILTLEVVLAALLGAILWNLITWYLGIPSSSSHALVGGLVGAGLAAAGFGAVNWGVLLKIVLPWVL
SPLIGFLLGFLLMRLLYWLFRRANPRRVNRGFRRLQIVSAALMAFSHGANDAQKAMGIITLALLAAGLLS
GFEVPLWVILLCALAIALGTLLGGWRIIKTLGKKITKLDPLQGFAAETSSAATVLLASLLGIPVSTTHVI
TGSIMGVGAARRLSAVRWGVAGRIVLAWVLTLPAAALLAALLYLLLSLLG
>gnl|CDD|440076 COG0307, RibC, Riboflavin synthase alpha chain [Coenzyme transport and metabolism]. Riboflavin synthase alpha chain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
MFTGIIEEVGTVVAIEKKGGGLRLTIEAPLLLSDLKIGDSIAVNGVCLTVVEIDGDGFTVDVSPETLRRT
TLGDLKVGDRVNLERALRLGDRLGGHIVSGHVDGTGEVVSIEPEGNSWRLRFSAPPELAKYIVEKGSIAV
DGVSLTVNEVEGDRFSVNLIPHTLEVTTLGELKVGDRVNLEVDILAKYVERLLERRKA
>gnl|CDD|440077 COG0308, PepN, Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism]
MKRLTRLEAYRPPGYDVTHYDLDLDLDPATTRLSGTATITFTATEAPLDSLVLDLKGLEVTSVTVDGKPL
DFTRDGERLTITLPKPLAPGETFTLEIEYSGKPSNGGEGLYRSGDPPDGPPYLYTQCEPEGARRWFPCFD
HPDDKATFTLTVTVPAGWVAVSNGNLVSETELGDGRTTWHWADTQPIPTYLFALAAGDYAVVEDTFASGV
PLRVYVRPGLADKAKEAFESTKRMLDFFEELFGVPYPFDKYDQVAVPDFNFGAMENQGLVTFGEKVLADE
TATDADYERRESVIAHELAHQWFGNLVTCADWDDLWLNEGFATYMEQLFSEDLYGKDAADRIFVGALRSY
AFAEDAGPNAHPIRPDDYPEIENFFDGIVYEKGALVLHMLRTLLGDEAFRAGLRLYFARHAGGNATTEDF
LAALEEASGRDLSAFFDQWLYQAGLPTLEVEYEYDADGKVTLTLRQTPPRPHPFHIPLEVGLLGGKLTAR
TVLLDGEQTELVAKPDPVLLLRLDDELAFLLAHDSDPFNRWEALQALWRDGEADYLDALRALADTDPAVR
AEALALLGSDQLALARAALALAAELALLRALDDLLALAALAALPDPLDL
>gnl|CDD|440078 COG0309, HypE, Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones]
LAHGSGGKLMRELIEELFLPALGNEVLVGGEDAAVLDLGGGRLAFTTDSFVVSPIFFPGGDIGKLAVHGT
VNDLAVSGAKPLYLSVSLILEEGFPLEDLERIVESMAEAAREAGVSIVTGDTKVVERGGVDGPFINTTGI
GVVPKGRLISPSGARPGDKIIVTGGIGDHGTAILAAREGLELEGELLSDAAPLNDLVSVLLEAAPGGVHA
MRDPTRGGLAGALNEIAEASGVGIEIDEDAIPVRPEVRGICELLGLDPLYLANEGKLVAVVPPEDAEAVL
EALRAHGIDAAIIGEVTEGPPGRVVLKTAIGGERILDPPEGDPLPRIC
>gnl|CDD|440079 COG0310, CbiM, ABC-type Co2+ transport system, permease component [Inorganic ion transport and metabolism]
MHIPDGFLPPPVAAAGWAVAAPFLAYGLRKLKKELDEEKIPLLAVLAAFFFVASMINIPIPGGSSGHLVG
GGLAAILLGPWAAFLAITIVLLLQALLFGDGGLTTLGANIFNMAIPGPFVGYLVYRLLRKLGPRLALAAF
LAGALGVLLAALLTALELALSGPYPFAKFAGAMAVTHLPLGIIEGLITALVVSFLAKV
>gnl|CDD|440080 COG0311, PdxT, Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport and metabolism]. Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLRERIAA
GLPVFGTCAGLILLAKEIEDPDQPTLGLLDITVRRNAFGRQVDSFEADLDIPGLGDGPFPAVFIRAPYIE
EVGPGVEVLATVDGRIVAVRQGNILATSFHPELTDDLRVHEYFLEMVRGAK
>gnl|CDD|440081 COG0312, TldD, Zn-dependent protease PmbA/TldA or its inactivated homolog [General function prediction only]
MEDLAEKLLEAAKKAGADYAEVRLERSRSESVSVRNGEVEQAESSEDQGVGVRVIVGGRTGFASTSDLSP
EALREAVERAVAIARATPEDPVAGLADPAPLYDPWESVSLEEKIELLKEAEAAARAVDPRIVNVGASLSA
SEEEVLIANSDGFLIEYRRSRVSLSVSVIAEDGGDMQRGYDGTGGRGLEDLDDPEEVGREAAERALARLG
ARPIPTGKYPVVLDPEAAGLLLHEALGHALEGDRVLKGSSFLAGKLGEQVASPLVTIVDDPTLPGGLGSL
PFDDEGVPTRRTVLIEDGVLKGYLLDRYSARKLGLESTGNARRESYAHPPIPRMTNTYLEPGDKSLEELI
ASVKRGLYVTELGGGGVDPVTGDFSFGASEGYLIENGEITYPVKGATIAGNLPEMLKNIVAVGNDLELRP
GGCGKPGQSGSPSLLIDGLTVGG
>gnl|CDD|440082 COG0313, RsmI, 16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]. 16S rRNA C1402 (ribose-2'-O) methylase RsmI is part of the Pathway/BioSystem: 16S rRNA modification
LYLVPTPIGNLEDITLRALEVLKEVDLIAAEDTRTTRKLLKHLGIKKPLISLHEHNEAERAPELLERLKA
GKDVALVSDAGTPGISDPGARLVRAAHEAGIPVVPLPGPSAVLTALSASGLPGDRFAFEGFLPRKKKERR
KRLKELEAEPRTLIFYESPHRLAKTLEDLAEVLGPDRRLCVARELTKLFEEIRRGTLAELLAWLPDLPPK
GEFVLVIEG
>gnl|CDD|440083 COG0314, MoaE, Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]. Molybdopterin synthase catalytic subunit MoaE is part of the Pathway/BioSystem: Molybdopterin biosynthesis
MMRVRVTEEPFDLAAELAALRASDPEAGAVVTFVGTVRDHNDGRRVTALEYEAYPPMAEKELAEIAEEAA
ERWGLLDVAVIHRVGRLEPGEPIVLVAVSSAHRKEAFEACRFLIDRLKTRAPIWKKEIFEDGEEWVEARS
SDD
>gnl|CDD|440084 COG0315, MoaC, Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]. Molybdenum cofactor biosynthesis enzyme MoaC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
MSELTHLDEQGRARMVDVSDKAVTARTAVAEGRVRMSPETLALIREGGVKKGDVLAVARIAGIMAAKRTS
ELIPLCHPLPLTGVDVDFELDDDLSGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIE
DIRLLEKSGGKSG
>gnl|CDD|440085 COG0316, IscA, Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein turnover, chaperones]
PITLTDAAAKRIKRLLAKEGNPGLGLRVGVKGGGCSGFSYGLDFDDEPNEDDLVFEQDGVKVVVDPKSLP
YLDGTEIDYVEELLGSGFKFNNPNAKSSCGCGESFSV
>gnl|CDD|440086 COG0317, SpoT, (p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription]
MVSVRLSAIEARLEELLERLKAYLPPADIALIRRAYEFAEEAHEGQKRKSGEPYITHPLAVAEILAELGL
DAETIAAALLHDVVEDTDVTLEEIEEEFGEEVAELVDGVTKLSKIEFGSKEEAQAENFRKMLLAMAKDIR
VILIKLADRLHNMRTLKAMPPEKQRRIARETLEIYAPLAHRLGINQIKWELEDLSFRYLEPERYKEIAKL
LKEKRGEREEYIEEIIEELKEELAEAGIKAEVSGRPKHIYSIYRKMQRKGLSFEEIYDLYAFRIIVDTVD
DCYAALGIVHSLWKPIPGRFKDYIAIPKPNGYQSLHTTVIGPDGKPVEVQIRTEEMHEIAEYGVAAHWKY
KEGGGSGDSSYDEKIAWLRQLLEWQEEAGDSGEFLESLKLDLFPDEVYVFTPKGDVIELPRGATPLDFAY
AIHTEVGHRCVGAKVNGRLVPLSTPLKNGDTVEIITSKNAGPSRDWLNFVKTSRARSKIRQWFKKQRREE
NIELGRELLEKELKRLGLTLDDENLEKLAKKLGFKSLDDLLAAIGLGEISLRQVVNRLLPELEKEEPEEE
DEELLKKSKKKKSDSGVLIDGVDGLLVKLAKCCNPIPGDPIVGFVTRGRGVSVHRKDCPNLAELREREPE
RLIDVEWGEDSSGVFPVDIRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDGTATIRFTVEVRDLDH
LARVLRKLRKVPGVISVRRVRG
>gnl|CDD|440087 COG0318, MenE/FadK, O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]. O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAAL
RAGAVVVPLNPRLTAEELAYILEDSGARALVTALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTP
GDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFA
RYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEV
RIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMII
SGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPR
RVEFVDELPRTASGKIDRRALRERYAAGALEA
>gnl|CDD|440088 COG0319, YbeY, ssRNA-specific RNase YbeY, 16S rRNA maturation enzyme [Translation, ribosomal structure and biogenesis]. ssRNA-specific RNase YbeY, 16S rRNA maturation enzyme is part of the Pathway/BioSystem: 16S rRNA modification
MSIEIQNEDDFELDEALLERWLEAALEAEGLAEDAELSVRFVDDEEIRELNREYRGKDKPTDVLSFPYDE
LPEDGPPLLGDIVISVETAAREAKEQGHSFEDELAHLLVHGLLHLLGYDHETEEEAEEMEALEEEILAKL
GIPD
>gnl|CDD|440089 COG0320, LipA, Lipoate synthase [Coenzyme transport and metabolism]. Lipoate synthase is part of the Pathway/BioSystem: Lipoate biosynthesis
MSTLPDIRRPEARNPETPILRKPDWLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSRGTAT
FMILGDICTRRCRFCDVATGRPLPLDPDEPERVAEAVAEMGLKYVVITSVDRDDLPDGGAGHFAETIRAI
RELNPGTTIEVLIPDFRGREEALDIVVDARPDVFNHNLETVPRLYKRVRPGADYERSLELLKRAKELDPG
IPTKSGLMLGLGETDEEVLEVMRDLRAAGVDILTIGQYLQPSKKHLPVDRYVTPEEFEELKEIALELGFL
HVASGPLVRSSYHADEQAAKARAARG
>gnl|CDD|440090 COG0321, LipB, Lipoate-protein ligase B [Coenzyme transport and metabolism]. Lipoate-protein ligase B is part of the Pathway/BioSystem: Lipoate biosynthesis
NRPLIIRDLGLVDYEEAWAAQRRLTAARVAGDTPDELWLLEHPPVYTLGRSGKPEHLLAPGGIPVVQTDR
GGQITYHGPGQLVGYPILDLRRRGLDVRAYVRRLEEAVIDTLAEYGIEAERRPGAPGVWVDGRKIAAIGL
RVRRGVTYHGFALNVNPDLSPFSRIVPCGIADLGVTSLSDELGRPVTMEEVAEALIRHFAEVFGYELVEL
S
>gnl|CDD|440091 COG0322, UvrC, Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair]
MDPFDLKEKLKTLPTSPGVYLMKDANGEVIYVGKAKNLKNRVSSYFQKSDLSPKTRRMVSEIADIEYIVT
DTETEALLLENNLIKKHKPRYNILLKDDKSYPYIKITNEEFPRIFVTRGVKKDGGRYFGPYPSAGAVRET
LDLLQKLFPLRTCSDSLFKNRSRPCLLYQIGRCSAPCVGLISEEEYREDVEQARRFLEGKTKELIKELEE
KMEEAAEELEFERAARLRDQIRALEKVQEKQKVVLPDGGDADVIAIARDGGEACVQVFFVRGGRLIGRRS
FFLEKVLDEDDEELLEAFLAQYYLDRPSIPKEILVPEELEDAELLEEWLSERRGRKVKIRVPQRGEKKKL
LELAEKNAREALERKLAERERDEARQERALEELAEALGLPELPRRIECFDISHIQGTNTVASMVVFEDGK
PDKSDYRRFKIKTVEGGDDYASMREVLTRRYKRLLEEDEPLPDLILIDGGKGQLNAAREVLEELGLDDIP
VIGLAKRDEELFLPGDSEPIILPRNSPALYLLQRIRDEAHRFAITFHRKLRSKARLKSVLDEIPGIGPKR
RKALLKHFGSLKAIKEASVEELAAVPGISKKLAEAIYEYLHKE
>gnl|CDD|440092 COG0323, MutL, DNA mismatch repair ATPase MutL [Replication, recombination and repair]
MPKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLP
LAFERHATSKIRSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVEGGKVVEVEPAAAP
KGTTVEVRDLFFNTPARRKFLKSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIA
AIYGREFAENLLPVEAEREGLRLSGYIGKPEFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGR
YPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRSAVREALAQAALGQLHGTYILAENEDGLVLI
DQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEPFGPNTVAVRA
VPALLGEGDAEELLRDLLDELAEEGSSESLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLEATEN
PYTCPHGRPTWIELSLEELEKLFKR
>gnl|CDD|440093 COG0324, MiaA, tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]. tRNA A37 N6-isopentenylltransferase MiaA is part of the Pathway/BioSystem: tRNA modification
KPPLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPDEE
YSVADFQRDARAAIAEILARGKLPILVGGTGLYIKALLEGLSFLPPADPELRAELEAEAEELGLEALHAE
LAELDPEAAARIHPNDPQRIIRALEVYELTGKPLSELQKEKKEPPPYDVLKIGLDPDREELYERINRRVD
QMLEAGLLDEVRALLARGLDPDLPAMRAIGYRELLAYLDGEISLEEAIERIKRATRQYAKRQLTWFRRDP
DIHWLDPDEPDLLEEILELIKAFLEE
>gnl|CDD|440094 COG0325, YggS, Pyridoxal 5'-phosphate homeostasis protein YggS, UPF0001 family [Coenzyme transport and metabolism]
MMSIAENLAAVRERIAAAAARAGRDPEEVTLVAVSKTVPAEAIREAYAAGQRDFGENRVQEALEKIEALA
DLDIEWHFIGHLQSNKVKYVAELFDLIHSVDRLKLAEELNKRAAKAGRPLDVLLQVNISGEESKSGVAPE
ELPALAEAIAALPNLRLRGLMTIAPLTEDPEEVRPAFARLRELFDRLRAQGPGLDELSMGMSGDYEIAIE
EGATMVRVGTAIFGARP
>gnl|CDD|440095 COG0326, HtpG, Molecular chaperone, HSP90 family [Posttranslational modification, protein turnover, chaperones]
MAKETGEFQAEVKQLLDLMIHSLYSNKEIFLRELISNASDAIDKLRFLALTDPELKEEDGDLKIRIEVDK
EAKTLTISDNGIGMTREEVIENLGTIAKSGTREFLEKLKGDQKKDSDLIGQFGVGFYSAFMVADKVEVVT
RSAGEDAEAVRWESDGDGEYTIEEAEKAERGTEITLHLKEDAEEFLEEWRLREIIKKYSDFIPVPIKMEG
EEEETEEDETINSATALWTRSKSEITDEEYKEFYKHLFHDFEDPLFWIHLNVEGPFEYTGLLYIPKKAPF
DLYDRDRKGGIKLYVKRVFIMDDAEDLLPEYLRFVRGVVDSPDLPLNVSREILQEDRQLKKIRKAITKKV
LDELEKLAKNDREKYEKFWKEFGLVLKEGALEDFKNREKIADLLRFESTKEGGYVTLAEYVERMKEGQKK
IYYITGESREAAEQSPHLEIFKAKGIEVLLLTDPIDEFLISHLEEFDGKKFKSVDSGDLDLDKLEEKKES
EEEEEEFKPLLERFKEALGDKVKDVRVSARLTDSPACLVADEGDMSRRMEKMLKAMGQDMPEAKPILEIN
PNHPLVKKLAAEEDEELFKDLAELLYDQALLAEGGLLEDPAAFVKRLNKLLEKALG
>gnl|CDD|440096 COG0327, NIF3, Putative GTP cyclohydrolase 1 type 2, NIF3 family [Coenzyme transport and metabolism]. Putative GTP cyclohydrolase 1 type 2, NIF3 family is part of the Pathway/BioSystem: Folate biosynthesis
MTLSELVAALEELLPPALAESWDPNGLQVGEGRAEVTRIVTAVDATQAVIEEAIEAGADLLIVHHPLFWK
GEDSITAGTVKGRRLALLIKNDIALYAAHTPLDAHPELGNNAQLARLLGLEDVEPLGPSGGEGLGRIGEL
PEPMTLEELAARVKEALGLRGVRVVGDPDRPIRRVAICTGSGQSLIEEAAAAGADAYITGEIKEHTAHDA
REQGIALIDAGHYATERPGVQALAEWLAEAFGLEVEFIDIDNPP
>gnl|CDD|440097 COG0328, RnhA, Ribonuclease HI [Replication, recombination and repair]
KMIEIYTDGACRGNPGPGGWGAVIRYGGEEKELSGGLGDTTNNRAELTALIAALEALKELGPCEVEIYTD
SQYVVNQITGWIHGWKKNGWKPVKNPDLWQRLDELLARHKVTFEWVKGHAGHPGNERADALANKAL
>gnl|CDD|440098 COG0329, DapA, 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]. 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis
KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGR
VPVIAGVGSNSTAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTG
VDLSPETLARLAEIPNIVGIKEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVA
PELMVALYEAALAGDLAEARALQDRLLPLIRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAE
LRAALKELGLL
>gnl|CDD|440099 COG0330, HflC, Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones]
NKLILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDVPP
QEVLTKDNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTGRDEINAEI
REELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAII
EAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYRSLEALEEVLSPNSKVIVLPPDGNGFLKYLLKS
>gnl|CDD|440100 COG0331, FabD, Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]. Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
MKLAFLFPGQGSQYVGMGKDLYENFPVAREVFEEASEALGYDLSALCFEGPEEELNLTENTQPAILAASV
AAYRALEEEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAVPAGPGGMAAVLGLDDEE
VEALCAEAAQGEVVEIANYNSPGQIVISGEKEAVEAAAELAKEAGAKRAVPLPVSGPFHTPLMAPAAEKL
AEALAAVTFADPKIPVVSNVDAAPVTDPEEIRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLS
GLVKRIDPGVEVLAVEDPADLEALLE
>gnl|CDD|440101 COG0332, FabH, 3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]. 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDP
EDIDLIIVATVTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAE
TLSRIVDWTDRSTCVLFGDGAGAVVLEASEEGPGILGSVLGSDGSGADLLVVPAGGSRNPPSPVDEGDHY
LRMDGREVFKFAVRNLPEVIREALEKAGLTLDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGN
TSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAVLRW
>gnl|CDD|440102 COG0333, RpmF, Ribosomal protein L32 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L32 is part of the Pathway/BioSystem: Ribosome 50S subunit
AVPKRKTSKSRRRKRRSHDKLTAPALVVCPNCGEPKLPHRVCPSCGYYKGRQVIEV
>gnl|CDD|440103 COG0334, GdhA, Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]. Glutamate dehydrogenase/leucine dehydrogenase is part of the Pathway/BioSystem: Glutamine biosynthesis
EPEFLQAVLEQLDSAAPVLGLDPGILERLKEPERVIIVRVPVRMDDGSVQVFRGYRVQHNSALGPYKGGI
RFHPSVNLDEVKALAFWMTFKNALTGLPFGGGKGGIDFDPKGLSDGELERLTRRFMTELYRHIGPDTDIP
APDVGTGAREMAWMMDEYSRITGETVPGVVTGKPLELGGSLGRTEATGRGVVYFAREALKKLGLSLEGKT
VAVQGFGNVGSYAAELLHELGAKVVAVSDSSGGIYDPDGIDLDALKEHKEERGSVAGYPGAEFITNEELL
ELDCDILIPAALENVITEENAKRLKAKIVAEGANGPTTPEADEILAERGILVAPDILANAGGVTVSYFEW
VQNLQRYSWTEEEVDERLEEIMVDAFDAVFETAEEYGVDLRTAAYIAAFERVADAMKARGI
>gnl|CDD|440104 COG0335, RplS, Ribosomal protein L19 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L19 is part of the Pathway/BioSystem: Ribosome 50S subunit
MNLIKEIEAEQLKKDIPEFRPGDTVRVHVKIKEGNKERIQVFEGVVIARRGGGLNETFTVRKISYGVGVE
RTFPLHSPRIEKIEVVRRGKVRRAKLYYLRDLRGKAARIKEKRDAK
>gnl|CDD|440105 COG0336, TrmD, tRNA G37 N-methylase TrmD [Translation, ribosomal structure and biogenesis]. tRNA G37 N-methylase TrmD is part of the Pathway/BioSystem: tRNA modification
MRIDVLTLFPEMFEGPLGHSILGRALEKGLLELEVHNLRDFTTDKHRTVDDTPYGGGAGMVMKPEPLFAA
IEAAKAEGPKPRVIYLSPQGRPFTQALARELAKEEHLILLCGRYEGIDERVIEHLVDEEISIGDYVLSGG
ELAAMVLIDAVVRLLPGVLGNEESAEEDSFSDGLLEYPHYTRPAEFRGLKVPEVLLSGNHAKIARWRREQ
SLERTRERRPDLLEKAELTKEDRKLLEELKKE
>gnl|CDD|440106 COG0337, AroB, 3-dehydroquinate synthetase [Amino acid transport and metabolism]. 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
MQTLTVNLGERSYDIRIGRGLLDELGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVL
PDGEASKTLETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSV
GGKTGVNHPGGKNLIGAFHQPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLA
RDPEALEEAIARSCEIKAEVVAADERESGLRALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSA
RLGLLSEEDVERIRALLEALGLPTRLPALDPEALLAAMKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEEL
LRAAL
>gnl|CDD|440107 COG0338, Dam, DNA-adenine methylase [Replication, recombination and repair]
MKKIKPPLKWAGGKRRLLPQILPLLPKHFGRYVEPFVGGGAVFFNLDPSKKEVLNDINPDLINFYRVVKD
DPEELIELLRLTFVPNSREEYYRLREIFNESLDDLERAARFLYLNRTCFNGLYRVNSKGGFNVPFGRYKN
PYIPERLRAVSERLQRVEIENLDFEEVIKRADSPGDFVYLDPPYYPLSRTSLFTSYGKGGFTDEDHERLA
DLLKELRGGKVLLSNSDTPLIRELYKGFRIEEVEAKRSINSNGSKRGKVKELLIT
>gnl|CDD|440108 COG0339, Dcp, Zn-dependent oligopeptidase, M3 family [Posttranslational modification, protein turnover, chaperones]
MAAMTNPLLDPSTLPYGLPPFDAIKPEHFEPAFEAALAEARAEIEAIAANPEAPTFENTIEALERSGERL
SRVWSVFSHLNSVDTNPELRAAYNEVLPKLSAHSDEIGLNEALFARIKALYDSRDFLGLDPEQKRLLENT
LRDFVLSGAALPEEDKARLREINEELAELSTKFSQNVLDATNAWALVVTDEAELAGLPESAIAAAAAAAK
ARGLEGWLITLDNPSYQPVLTYADNRELREKLYRAYVTRASDGGEFDNRPIIAEILALRAEKAKLLGYAN
YAEYSLADKMAKTPEAVLDFLRDLAPAAKPAAERELAELQAFAAEEGGIFDLEPWDWAYYAEKLRQARYD
LDEEELKPYFPLDRVLDGLFEVAERLYGLTFKERKDVPVYHPDVRVFEVFDADGELLGLFYLDLYAREGK
RGGAWMDSFRSQSRLDGELQLPVAYNVCNFTKPVGGKPALLTHDEVTTLFHEFGHALHGMLTDVDYPSLS
GTNVPWDFVELPSQFMENWCWEPEVLALFARHYETGEPLPDELLDKLLAARNFNSGFATLRQLEFALLDM
ALHTLYDPEAGADVLAFEAEVLAEVGVLPPVPPRRFSTYFSHIFAGGYAAGYYSYKWAEVLDADAFSAFE
EAGIFDRETGQRFRDEILSRGGSRDPMELFKAFRGREPSIDALLRHRGLAAA
>gnl|CDD|440109 COG0340, BirA2, Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]. Biotin-(acetyl-CoA carboxylase) ligase is part of the Pathway/BioSystem: Biotin biosynthesis
RIEVFDEVDSTNDEAKELAREGAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPL
LSLAAGLAVAEALRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQPPFDPEE
LDQPATSLKEETGKEVDREELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEG
IAVGIDEDGALLLETADGEIRAVAAGEVSLR
>gnl|CDD|440110 COG0341, SecF, Preprotein translocase subunit SecF [Intracellular trafficking, secretion, and vesicular transport]
RLFPGNTNIDFMKKRKIWFAISAVLILASIVSLFTRGLNLGIDFTGGTLIEVSFEQPVDLEEVREALEEA
GLGDASVQTFGSDNDVLIRTPPLDGESAEEVEKVRAALKEAFGDVEIVRVEFVGPTVGKELTRKALLALL
VALIGILIYIAFRFEWRFAVGAVVALLHDVLITLGIFSLFGLEFDLTFIAALLTIIGYSLNDTVVVFDRI
RENLRKYRKMTLAEIINLSINQTLSRTINTSLTTLLVVLALLFFGGETLRDFALALLIGIIVGTYSSIFI
ASPLLLWLGKR
>gnl|CDD|440111 COG0342, SecD, Preprotein translocase subunit SecD [Intracellular trafficking, secretion, and vesicular transport]
MKAKFLLWRLLLLLLVVALSLVAPNGPAKPIKLGLDLQGGVHLLLEVDTDAALDEDGDGIREVTEEALDQ
AIEILRNRVNELGVSEPVIQRQGDDRIVVELPGVQDPAEAKELLGKTAKLEFRLVDDSADAQAAVPAGSE
LLPCRDGQPYLLLGPVVLTGDDLTDASAGFDQQTGQPVVSFTLDSEGAKKFADATRENVGKPLAIVLDGE
VISAPVIQEPITGGSAQITGSFTVEEAQDLALLLRAGALPAPLEIVEERTVGPTLGADSIEKGLIAGLIG
LLLVALFMLLYYRLPGLVANIALALNVVLLLGVLSLLGATLTLPGIAGIILTIGMAVDANVLIFERIREE
LRAGRSLRAAIEAGFKRAFSTILDANVTTLIAAVVLFVLGTGPVKGFAVTLILGILISMFTAVPVTRPLL
NLLLGRRRLKKLGI
>gnl|CDD|440112 COG0343, Tgt, Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]. Queuine/archaeosine tRNA-ribosyltransferase is part of the Pathway/BioSystem: tRNA modification
MAMKFELLATDPGKARRGRLTTPHGTIETPAFMPVGTQATVKALTPEELKEIGAQIILGNTYHLYLRPGA
EVIAKAGGLHKFMNWDGPILTDSGGFQVFSLAKLRKITEEGVTFRSHIDGSKHFLTPEKSMEIQRALGSD
IIMAFDECTPYPATYEYAKKSMERTLRWAERCKAAHKRLPDQALFGIVQGGMYEDLRKESAEALVELDFD
GYAIGGLSVGEPKEEMYEILEYTTPLLPEDKPRYLMGVGTPEDLLEAVARGVDMFDCVLPTRNARNGTAF
TSQGRINIRNARYKEDFRPLDPECDCYTCRNYSRAYLRHLFKAGEILGARLLTIHNLHFYLRLMREIREA
IEEGRFAEFKAEFLAKYGRG
>gnl|CDD|440113 COG0344, PlsY, Phospholipid biosynthesis protein PlsY, probable glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]
MMLLLLLLLLAYLLGSIPFGYLVGKLFGGIDIREHGSGNIGATNVLRVLGKKAGLLVLLLDALKGALAVL
LARLLGGGPLLLLLAGLAAVLGHNFPVFLGFKGGKGVATALGVLLALSPLVGLIALAVWLLVLLLTRYVS
LGSLVAALAAPILALLLGGPLALLLLALLLALLVIYRHRSNIKRLLAGTESKIG
>gnl|CDD|440114 COG0345, ProC, Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]. Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
MSMKIGFIGAGNMGSAIIKGLLKSGVPPEDIIVSDRSPERLEALAERYGVRVTTDNAEAAAQADVVVLAV
KPQDLAEVLEELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSE
EDRELVEALFSAVGKVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGA
AKLLLESGEHPAELRDRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKELGK
>gnl|CDD|440115 COG0346, GloA, Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism]
MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGAAPAPGGGGLH
HLAFRVDDLDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPPG
>gnl|CDD|440116 COG0347, GlnK, Nitrogen regulatory protein PII [Signal transduction mechanisms, Amino acid transport and metabolism]
MKKIEAIIRPFKLDDVKEALEEAGVPGMTVTEVKGFGRQKGHTELYRGAEYVVDFLPKVKIEIVVSDEDV
DKVVEAIIKAARTGKIGDGKIFVSPVEEAVRIRTGERGEDAL
>gnl|CDD|440117 COG0348, NapH, Polyferredoxin NapH [Energy production and conversion]
MSYPRLVKGRFRRLRRLVQLLFLLLFLLGPWLRWLGDPAVLLDLAERRFYLFGLFWDFYLLALLLIGAAL
ALFLLTLLFGRVWCGWVCPQGVLTELFSWLERKLGDRRLKLPWSLSKILRWLKYIILALWLLLALLTGLT
FFGYFSPIGTLLRLLLFGVLGLWLLLILLAAFLLLALFLRRQWCRYLCPYGAFQGLLSDLSTLRVRYDRG
DCIDCGLCVKVCPMGIDIRKGEINQSECINCGRCIDACPKDAIRFSSRGEKTR
>gnl|CDD|440118 COG0349, Rnd, Ribonuclease D [Translation, ribosomal structure and biogenesis]
LITTDEELAALCARLAQAPAVAVDTEFMRERTYYPRLCLIQLADGEEVALIDPLAIGDLSPLWELLADPA
IVKVFHAAREDLEILYHLFGILPKPLFDTQIAAALLGYGDSVGYAALVEELLGVELDKSEQRSDWLRRPL
SEEQLEYAAADVRYLLPLYEKLLEELEREGRLEWAEEECARLLDPATYREDPEEAWLRLKGAWKLNPRQL
AVLRELAAWREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAEAL
ALPEEELPEPPRRLPLSPGYKALLKLLKALLKEVAEELGVAPELLASRKDLEALARWGELADPPLLSGWR
RELFGEELLALLEGE
>gnl|CDD|440119 COG0350, AdaB, DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, recombination and repair]
TIRYAIFDTPLGPLLIAATDRGLCALSFGDDREEALLARFPAALREDPPLLAEAARQLDAYFAGERKDFD
LPLDLRGTPFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSL
GGYAGGLERKRALLELEGALAAA
>gnl|CDD|440120 COG0351, ThiD, Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]. Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis
LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAI
KIGMLGSAEIIEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEAL
LGIEITTLDDMREAAKALLELGAKAVLVKGGHLPGDEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSS
AIAALLAKGLDLEEAVREAKEYVTQAIRAALRLGMGHGPVNHFA
>gnl|CDD|440121 COG0352, ThiE, Thiamine monophosphate synthase [Coenzyme transport and metabolism]. Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
MTLPRLYLITDPDLCGRDLLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRV
DLALALGADGVHLGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPP
PLGLEGLAWWAELVEIPVVAIGGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA
>gnl|CDD|440122 COG0353, RecR, Recombinational DNA repair protein RecR [Replication, recombination and repair]
MYPPPLERLIEALSKLPGIGPKSAQRLALHLLKRDEEEAERLAEALLEAKEKVRHCSVCGNLTEEDPCSI
CADPRRDRSLICVVEEPADVLAIERTGEYRGLYHVLGGVLSPLDGIGPEDLNIDELLERLKEGGVKEVIL
ATNPTVEGEATAHYIAELLKPLGVKVTRLARGLPVGGELEYADEGTLARALEGRR
>gnl|CDD|440123 COG0354, YgfZ, Folate-binding protein YgfZ, synthesis and repair of Fe-S clusters [Posttranslational modification, protein turnover, chaperones]
MTSSFAEQRALLAGAALVDLSDRGVIRVSGPDALKFLQGQLTNDVRALAPGQARLAALLTPKGRVLADFR
VFRDGDGYLLDVPADLAEALLKRLKKYRLRSKVEIEDASDDLAVLGLAGPAAAAALAALGALADPAAHAV
ADGGTIRLPRPAPGYLLIVPAAAAAALWEALAAGAAPAGSAAWEALRIAAGIPRIGADTDEDFIPQELNL
DALGGVSFKKGCYPGQETVARMHYRGKVKRRLVLLHLDGSALPAPGTELLAGGRPVGTVTSAARHPEGGP
IALAVLRRDAADAGAELRVGGAAATVIVLPLPYRLPE
>gnl|CDD|440124 COG0355, AtpC, FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]. FoF1-type ATP synthase, epsilon subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
LKLEIVTPERVLFSGEVESVVAPGAEGEFGILPGHAPLLTALKPGVVRIRTEDGEEEYFAVSGGFLEVQP
NKVTILADTAERAEDIDVERAEEAKERAEERLEEAKDDIDYARAEAALARALARLRAAEKL
>gnl|CDD|440125 COG0356, AtpB, FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]. FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase
DTVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILV
SNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLFFPPFPWLAPLMLPIEIISELA
RPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAV
EE
>gnl|CDD|440126 COG0357, RsmG, 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]. 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification
LAELLEEGLAELGLELSEEQLEQLEAYLELLLKWNKKINLTAIRDPEELWERHILDSLALLPLLPKEGAR
VLDVGSGAGFPGIPLAIARPDLQVTLVDSLGKKIAFLREVVRELGLKNVTVVHGRAEELAPREKFDVVTA
RAVAPLPDLLELALPLLKPGGRLLALKGPDAEEELAEAPKALKVLEEVEELTLPGLDAERHLVVIKKIKR
T
>gnl|CDD|440127 COG0358, DnaG, DNA primase (bacterial type) [Replication, recombination and repair]
RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISF
LMEYEGLSFPEAVEELAERAGIELPEEEGSPEEREEASERERLYEALELAAKFYQEQLKNTPEGKAARDY
LKKRGLSDETIERFGLGYAPDGWDALLKHLKKKGFSEEELVEAGLVIEREDGGYYDRFRGRIMFPIRDLR
GRVIGFGGRVLDDGEPKYLNSPETPLFHKGRVLYGLDLARKAIRKEDRVIVVEGYMDVIALHQAGIKNAV
ATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALRALELLLKDGLQVRVLFLPDGEDPDELIRKEGA
EAFRELLENAKPLIEFLIERLLEGYDLDTPEGRAALLREALPLLAKIPDPILRELYLRELAERLGLDEEA
LDALARLKRRALEKRIEELKEELKEARGDEEEKKELRELLKKKLK
>gnl|CDD|440128 COG0359, RplI, Ribosomal protein L9 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L9 is part of the Pathway/BioSystem: Ribosome 50S subunit
MKVILLEDVKGLGKKGDVVEVKDGYARNYLIPQGLAVEATKGNLKQLEARRAALEAKEAEELAEAEALAE
KLEGLTVTIKAKAGEGGKLFGSVTTKDIAEALKAQGIEIDKRKIELPGPIKTLGEYEVTVKLHPEVTATI
KVNVVAE
>gnl|CDD|440129 COG0360, RpsF, Ribosomal protein S6 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S6 is part of the Pathway/BioSystem: Ribosome 30S subunit
MRHYEIVFILRPDLSEEQVEALVEKFKGIIEKNGGEIVKVEDWGKRKLAYPIKKKREGHYVLMNFEADPA
AIAELERQLRINEDVLRFLTVRLDEAEEEPSPMMKKE
>gnl|CDD|440130 COG0361, InfA, Translation initiation factor IF-1 [Translation, ribosomal structure and biogenesis]. Translation initiation factor IF-1 is part of the Pathway/BioSystem: Translation factors
MAKKEDLIEVEGVVEEVLPNARFRVRLENGHERLARISGKMRKNRIRILPGDRVLVEPSPYDLTKGRIVY
RYK
>gnl|CDD|440131 COG0362, Gnd, 6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]. 6-phosphogluconate dehydrogenase is part of the Pathway/BioSystem: Pentose phosphate pathway
AKADIGVIGLAVMGRNLALNIADHGFSVAVYNRTAEKTDAFLAEHGKGKNIVGTYSLEEFVASLERPRKI
LLMVKAGKPVDAVIEQLLPLLEPGDIIIDGGNSHFTDTIRREKELAEKGIHFIGMGVSGGEEGALHGPSI
MPGGSKEAYELVKPILEAIAAKVDGEPCVTYIGPDGAGHFVKMVHNGIEYADMQLIAEAYDLLRDGLGLS
NDEIAEVFAEWNKGELDSYLIEITADILRKKDPETGKPLVDVILDKAGQKGTGKWTSQSALDLGVPLPLI
TEAVFARYLSALKEERVAASKLLPGPEAAPFEGDKEAFIEDLRDALYASKIVSYAQGFALLRAASKEYGW
NLDLGEIARIWRGGCIIRARFLDDITEAYDKNPDLPNLLLDPYFADALKKAQPAWRRVVATAALAGIPVP
AFSSALAYYDSYRSARLPANLIQAQRDYFGAHTYERVDKEGFFHTEW
>gnl|CDD|440132 COG0363, NagB, 6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminase [Carbohydrate transport and metabolism]. 6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminase is part of the Pathway/BioSystem: Pentose phosphate pathway
KMRVIIFPDAEELAAAAAERAAERIAEAIAEKGRAVLGLAGGSTPLGLYEELARLHKEGGLDWSRVHVFN
LDEYVGLPPDHPQSNRRFMREALLDHVDIPPENIHIPDGEAEDPEAAAARYEALIAEAGGIDLQLLGIGE
DGHIAFNFPGSPFLSETDRVVTLDESTRQANARFFGSIPKVPPQAITLGIPTIMKAREILLLATGENKAE
AVAAALEGPVTEEVPASILQGHPNVTWFLDEAAASLLT
>gnl|CDD|440133 COG0364, Zwf, Glucose-6-phosphate 1-dehydrogenase [Carbohydrate transport and metabolism]. Glucose-6-phosphate 1-dehydrogenase is part of the Pathway/BioSystem: Pentose phosphate pathway
MTQMRPAEPCDLVIFGATGDLARRKLLPALYNLYRDGLLPEGFRIIGVARRDWSDEEFREEVREALEEFS
RKPFDEEVWERFLERLHYVSGDFTDPEGYERLKELLEELDEERTPGNRVFYLATPPSLFGPICENLGAAG
LATEGGWRRVVIEKPFGHDLASARELNDELGRVFDESQIYRIDHYLGKETVQNLLALRFANALFEPLWNR
NYIDHVQITVAETVGVEGRGGYYDGAGALRDMVQNHLLQLLCLVAMEPPASLDADAIRDEKVKVLRALRP
ITPEDVAENTVRGQYTAGWIGGEPVPGYREEPGVAPDSTTETFVALKLEIDNWRWAGVPFYLRTGKRLPE
RVTEIVIQFKPVPHSLFRETAEELPPNRLVIRIQPDEGISLRFNAKVPGLGMRLRPVSLDFSYSDAFGER
SPEAYERLLLDVMRGDQTLFMRRDEVEAAWRWVDPILEAWAEEPEPPPPYPAGSWGPEAADALLARDGRS
WREPD
>gnl|CDD|440134 COG0365, Acs, Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]
RWFVGGRLNIAYNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIY
LPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEE
LPSLEHVIVVGRTGADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYL
VHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVT
VFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISN
LPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWY
RTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLK
PGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLGDTSTLEDPEAL
DEIKE
>gnl|CDD|440135 COG0366, AmyA, Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism]
ADPDWWKDAVIYQIYPDSFADSNGDGGGDLKGIIEKLDYLKDLGVDAIWLSPFFPSPMSDHGYDISDYRD
VDPRFGTLADFDELVAEAHARGIKVILDLVLNHTSDEHPWFQEARAGPDSPYRDWYVWRDGKPDLPPNNW
FSIFGGSAWTWDPEDGQYYLHLFFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDKDEGL
PENLPEVHEFLRELRAAVDEYYPDFFLVGEAWVDPPEDVARYFGGDELDMAFNFPLMPALWDALAPEDAA
ELRDALAQTPALYPEGGWWANFLRNHDQPRLASRLGGDYDRRRAKLAAALLLTLPGTPYIYYGDEIGMTG
DKLQDPEGRDGCRTPMPWSDDRNAGFSTGWLPVPPNYKAINVEAQEADPDSLLNFYRKLIALR
>gnl|CDD|440136 COG0367, AsnB, Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]. Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
MCGIAGIIDFDGGADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLSEGGHQPMVSEDGRYV
LVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDR
FGIKPLYYAEDGGGLAFASELKALLAHPGVDRELDPEALAEYLTLGYVPAPRTIFKGIRKLPPGHYLTVD
AGGELEIRRYWDLEFVPHERSDSEEEAVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLS
KGPLKTFSIGFEDSAYDESPYARAVAEHLGTEHHEVTVTPEDLLDALPDLVWHLDEPFADPSAVPTYLLS
RLAREHVKVVLSGEGADELFGGYPRYREAALLLSPDFAEALGGELVPRLYAESGAEDPLRRMLYLDLKTY
LPGDLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELKLRGGRGKYLLRKALEGLLPDEVLDRPKQG
FPVPLGPWLRGPLREWLEDLLSDESLAARGLFDPDAVRRLLEEHLAGRRDHSRKLWSLLMLELWLRRF
>gnl|CDD|440137 COG0368, CobS, Cobalamin synthase CobS (adenosylcobinamide-GDP ribazoletransferase) [Coenzyme transport and metabolism]. Cobalamin synthase CobS (adenosylcobinamide-GDP ribazoletransferase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
ELRGFLLALQFLTRLPVPAPVDVDEEDLARAVRYFPLVGLLIGLLLALVLLLLSLLLPPLLAALLAVAAL
VLLTGGLHLDGLADTADGLGGGRDRERRLEIMKDSRIGAFGVLALVLVLLLKVAALASLAAAAALLALLA
APVLSRLAMVLLIATLPYARPEGLGAPFAGGVSRRALLLALLLALLLALLLLGWAGLLALLAALLAALLL
RRWARRRLGGITGDVLGAAQELTELAFLLALALLLG
>gnl|CDD|440138 COG0369, CysJ, Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]. Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis
WLSGYLAGLASRAAAAAAAAAAAAAGTPLTILYGSQTGNAEGLAEQLAERAKAAGLAVTLASLDDYKPKD
LAKEGLLLIVTSTYGEGEPPDNARAFYEFLHSKKAPKLDGLRYAVLGLGDSSYETFCQTGKDFDARLEEL
GATRLLPRVDCDVDYEEAAEAWLAAVLAALAEALGAAAAAAAAAAAAAPAYSRKNPFPATVLENRELTGR
GSAKETRHIEIDLPGSGLSYEPGDALGVWPENDPALVDELLARLGLDGDEPVTLDGEPLSLREALTEHLE
LTRLTPPLLEKYAELTGNAELAALLADEDKAALREYLAGRQLLDLLREFPAAELSAEELLELLRPLTPRL
YSISSSPKAHPDEVHLTVGVVRYEASGRERKGVASTYLADLEEGDTVPVFVEPNPNFRLPADPDTPIIMI
GPGTGIAPFRAFLQEREARGASGKNWLFFGDRHFTTDFLYQTELQAWLKDGVLTRLDLAFSRDQAEKIYV
QHRLLEQGAELWAWLEEGAHVYVCGDASRMAKDVDAALLDIIAEHGGLSEEEAEEYLAELRAEKRYQRDV
Y
>gnl|CDD|440139 COG0370, FeoB, Fe2+ transporter FeoB [Inorganic ion transport and metabolism]
MKMITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGTYSLSAYSPDE
KVARDFLLEEKPDVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVP
VVPTSARKGKGIDELKEAIIEAAEGKKPRPLRIDYPEEIEEAIEELEELLEEDGPYPSRWLAIKLLEGDE
EVLELLSELLELLEEIREELEEELGEDLESIIADARYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPV
LGIPIFLLIMFLVFQLTFTVGAPLMDLIDGGFGWLGDWVAALLPPGWLRSLLVDGIIGGVGGVLVFLPQI
AILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSGFGCNVPAIMATRTIESPRDRLITILVA
PFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTLLKGEPSPFVMELPPYRLPTL
KNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGESEDLENSYLGRIGKALEPVFAPLGFDWQIG
VALITGFAAKEVVVGTLGTLYGVGEDAEESASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRET
GSWKWTLFAVGYMTVLAYLVAFLVYQIGRLLG
>gnl|CDD|440140 COG0371, GldA, Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]. Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
RVIILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGECSEEE
IERLAEEAKEQGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSF
LAKNPDLVLVDTDIIAKAPVRLLAAGIGDALAKWYEARDWSLAHRDLAGEYYTEAAVALARLCAETLLEY
GEAAIKAVEAGVVTPALERVVEANLLLSGLAMGIGSSRPGSGAAHAIHNGLTALPETHHALHGEKVAFGT
LVQLVLEGRPEEIEELLDFLRSVGLPTTLADLGLDDETEEELLTVAEAARPERYTILNLPFEVTPEAVEA
AILAT
>gnl|CDD|440141 COG0372, GltA, Citrate synthase [Energy production and conversion]. Citrate synthase is part of the Pathway/BioSystem: TCA cycle
MSSEIDIRAKFTVDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEE
LAEFKAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSALGAFDPDADDIDPEARLEKAIRLIAKLPT
IAAYAYRYRRGLPPVYPDPDLSYAENFLYMLFGEEPDPEEARALDLLLILHADHEQNASTFTARVVASTL
ADLYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKI
LKEAAEELLEELGDDPLLEIAEELEEVALEDEYFIEKKLYPNVDFYSGIVYHALGIPTDMFTPIFAISRV
AGWIAHWLEQRADNRIIRPRQIYVGPEDRDYVPIEER
>gnl|CDD|440142 COG0373, HemA, Glutamyl-tRNA reductase [Coenzyme transport and metabolism]. Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis
MSLLVVGLNHKTAPVEIREKLAFSEEELEEALEELKAQPGVDEAVILSTCNRTEIYAVADDPHAGLEALI
EFLAEYHGLDVEELEPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYELAREAGTTGPVLNR
LFQKAFSVAKRVRTETGIGEGAVSVSSAAVELAKKIFGDLSGKTVLVIGAGEMGELAARHLAAKGVKRIT
VANRTLERAEELAEEFGGEAVPLEELPEALAEADIVISSTGAPHPVITKEMVERALKKRRHRPLFLIDLA
VPRDIEPEVGELPGVYLYDIDDLQEVVDENLEERQAAAPKAEAIIEEEVEEFLEWLKSREVVPTIRALRE
KAEAIREEELERALKKLPDLGEDEREVLEKLTRSLVNKLLHAPTVRLKEAAAEGEDDEYLEALRRLFDLE
EEEED
>gnl|CDD|440143 COG0374, HyaB, Ni,Fe-hydrogenase I large subunit [Energy production and conversion]
IVIDPITRIEGHLRIEVEVDDGVVTDAWSSGTMFRGFEIILKGRDPRDAWAITQRICGVCTTSHALASVR
ALEDALGIEPPPNARLIRNLILAAENLHDHLVHFYHLFALDWVDVVYALKADPKKTAASLSPWPKASPPY
FADVQDRLKPFVESGQLGIFANGYWGHPAYKLPPEVNLMAGAHYLEALEAQREAVEIHAIFGGKWPHPSN
LVPGGVTCAITLERLARLKSILDEFRDFVEQVYLPDLLAFARFYKDLAKLGGGLGNFLSYGDFPDPDNGW
GGARLFPPGVILNGDLGKVHPVDPDKITEDVTHSWYEDDGPLHPWEGETEPDYTDLDKDGKYSWVKAPRY
DGKPMEVGPLARQLVAYAAGHPLIKDLVDAALKALGLPPEALFSTLGRTAARALEAALLADAMEKWLDAL
VPNIKAGDTKTFEPPTWPKEAKGVGLTEAPRGALGHWIVIKDGKIANYQIVVPTTWNASPRDAKGQPGPY
EAALIGTPVADPEKPLEVLRTVRSFDPCLACAVHVIDPKGKELLRVKVL
>gnl|CDD|440144 COG0375, HybF, Hydrogenase maturation factor HypA/HybF, metallochaperone involved in Ni insertion [Posttranslational modification, protein turnover, chaperones]
MHELSIAQSILEIVEEEARENGAKRVTKVRLEIGELSGVEPEALEFAFEVLARGTIAEGAELEIEEVPAR
ARCRDCGKEFELEELFLRCPKCGSPDLEILSGRELRIKSIEVE
>gnl|CDD|440145 COG0376, KatG, Catalase (peroxidase I) [Inorganic ion transport and metabolism]
MSAEGKCPFMHGAAAAAAGGGTSNRDWWPNQLNLSILHQHSPKSNPMGEDFDYAEAFKKLDLDAVKKDLK
ALMTDSQDWWPADYGHYGPLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSWPDNANLDKARRLLWPI
KQKYGNKISWADLMILAGNVALESMGFKTFGFAGGREDVWEPEEDVYWGPETEWLGDERYSGDRELENPL
AAVQMGLIYVNPEGPNGNPDPLAAARDIRETFGRMAMNDEETVALIAGGHTFGKTHGAGDAEHVGPEPEA
APIEEQGLGWKNSFGSGKGEDTITSGLEGAWTPTPTQWDNGYFDNLFGYEWELTKSPAGAHQWVPKDGAA
ADTVPDAHDPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEEFADAFARAWFKLTHRDMGPKSRYLGP
EVPAEELIWQDPIPAVDHELIDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDKRGGANGARIRL
APQKDWEVNEPEQLAKVLAVLEGIQKDFNAAQSGGKKVSLADLIVLGGCAAVEKAAKDAGHDVTVPFTPG
RTDATQEQTDVESFAVLEPKADGFRNYLKKGYSVSAEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGG
SKHGVFTDRPGTLTNDFFVNLLDMGTEWKPSSDDEGLFEGRDRKTGEVKWTATRVDLVFGSNSELRALAE
VYASDDAKEKFVKDFVAAWTKVMNLDRFDLA
>gnl|CDD|440146 COG0377, NuoB, NADH:ubiquinone oxidoreductase 20 kD subunit (chain B) or related Fe-S oxidoreductase [Energy production and conversion]. NADH:ubiquinone oxidoreductase 20 kD subunit (chain B) or related Fe-S oxidoreductase is part of the Pathway/BioSystem: NADH dehydrogenase
LTTLDKLVNWARKNSLWPLTFGLACCAIEMMAAGASRYDLERFGAEVPRASPRQADLMIVAGTVTKKMAP
VLRRLYEQMPEPKWVIAMGACAISGGPYWDSYSVVQGVDKIIPVDVYVPGCPPRPEALLDGILKLQEKIR
RERLRGRKEYGE
>gnl|CDD|440147 COG0378, HypB, Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones]
AAENRALFAEKGVLAVNLMGSPGSGKTTLLEKTIRALKDRLRIAVIEGDIYTTEDAERLRAAGVPVVQIN
TGGCCHLDASMVLEALEELDLPDLDLLFIENVGNLVCPAFFPLGEDLKVVVLSVTEGDDKPRKYPPMFTA
ADLLVINKIDLAPYVGFDLEVMEEDARRVNPGAPIFEVSAKTGEGLDEWADWLREQLRAK
>gnl|CDD|440148 COG0379, NadA, Quinolinate synthase [Coenzyme transport and metabolism]. Quinolinate synthase is part of the Pathway/BioSystem: NAD biosynthesis
EELIERIRRLKKEKNAVILAHYYQRPEIQDIADFVGDSLELARKAAETDADTIVFCGVHFMAETAKILSP
EKKVLLPDLEAGCSMADMAPAEQLRAFKEEHPDATVVTYVNSSAAVKAESDIVCTSSNAVKIVESLPEDK
ILFAPDQNLGRYVAKKTGADMILWDGFCIVHERFTPEDIERLKAEHPDAKVLVHPECPPEVVELADFVGS
TSGIIKYAKESPAKEFIVGTEIGILHRLRKENPDKTFIPAPPAAICPTMKMNTLEKLYWALENEVNEITV
DEEIAEKARKALERMLEIS
>gnl|CDD|440149 COG0380, OtsA, Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism]
GSRLVVVSNRLPVPHVREDGSIRVKRSAGGLVTALEPVLRRRGGLWVGWSGGDADREAVEEPRGPVPPDL
GGYTLAPVDLSAEEVDGYYEGFSNETLWPLFHYRLDLPEFDREDWEAYRRVNRRFAEALAEEAEPDDVVW
VHDYHLLLVPAMLRELGPDARIGFFLHIPFPPPEIFRILPWREEILEGLLGADLIGFQTPRDARNFLDCV
RRLLGAEVDEGGTVRYGGRTVRVGAFPIGIDVEEFAELARSPEVRARAERLREELGGRKLILGVDRLDYT
KGIPERLRAFERLLERHPELRGKVTLLQIAVPSREDVPAYRELRREIEELVGRINGRFGTLDWTPIRYLN
RSLPREELAALYRAADVALVTPLRDGMNLVAKEYVAAQPDDPGVLVLSEFAGAAEELTEALLVNPYDIDG
MAEAIHRALTMPLEERRRRMRALRERVRRYDVHRWADDFLDALAAVRAAASPLA
>gnl|CDD|440150 COG0381, WecB, UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]
MMKVLTVVGTRPEAIKMAPVIRALKKRPGFEHVLVHTGQHYDYEMSDQFFEELGIPKPDYDLGIGSGSLA
EQTARILEGLEEVLEEEKPDAVLVHGDTNSTLAAALAAFKLGIPVAHVEAGLRSFDRPMPEEINRRLTDH
ISDLHFAPTELARENLLREGIPPERIFVTGNTVIDALLYVLERAEESDILEELGLEPKKYILVTLHRREN
VDDPERLENILEALRELAERYDLPVVFPVHPRTRKRLEEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLT
DSGGIQEEAPSLGKPCLTLRDTTERPETVEAGTNKLVGTDPERIVAAVERLLDDPAAYERMARAVNPYGD
GNASERIVDILLRYLG
>gnl|CDD|440151 COG0382, UbiA, 4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]. 4-hydroxybenzoate polyprenyltransferase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
RAYLRLLRLDRPIGILLLLWPTLWALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINER
KPNRPLASGRISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSLFLKRFTLLGNLVLGLL
FGLGILMGFAAVTGSLPLSAWLLALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIIAGVL
YALAVLLLLLLGLLAGLGLLYLLGLLAALLLLYLSQLWLLRPRKKDPARALKLFKLNMLLGLLLFLGIAL
>gnl|CDD|440152 COG0383, MngB, Alpha-mannosidase [Carbohydrate transport and metabolism]
AGMKKKKVHAVGHAHIDRAWLWPVEETRRKLARTFSTVLDLLEEYPEFVFDGSTAQLYDYLKEHYPELFE
RIKKLVKEGRWEPVGGMWVEPDTNLPSGESLVRQLLYGQRFFKEEFGVDMKVGWLPDSFGYSAQLPQILK
GAGIDYFVTQKGSWNDTNRFPYHTFWWEGIDGSEVLTHFFPNGYNSGLDPEELAGAWRNFEQKAVTDELL
LPFGYGDGGGGPTREMLERARRLNDLPGLPEVVISTPEDFFEALEEELPDLPVWQGELYLELHRGTYTSR
ADLKRLNRRAERLLREAEPLAALAALLGAEYPQEELDEAWKLLLLNQFHDILPGSSIDEVYREAEARYEE
ALEEAESLIDEALRAIAGAIDLPEDGDPLVVFNTLPWPRSEVVELPLYTPGKNFQLVDSDGKELPAQILE
DGKILFSAEDLPALGYKTLSLVEGEASPESSVSVSENVLENEFLRVEIDENGSLTSIYDKETGREVLAGR
GNQLQLFEDSPDAGDAWDIDPPYEDKPIELDELASIEVVESGPLRARLRVTRTFGRSTITQTITLRAGSP
RLDFKTEVDWQERDHLLKVAFPTDVRADEATAEIQFGVIKRPTHPNTSWEKARFEVPAHRWVDLSEGGYG
VALLNDGKYGYDVKDNTIRLTLLRSPVFPDPDADLGEHTFTYALYPHAGDWDEADVVQEAYELNTPLRVY
QQPPHEGGLPPEFSLLSLDGPNLVLSAVKKAEDGSGLILRLYEPSGERGTATLKFDFPLASAEEVNLLEE
PLEELEVEDNTVELELKPFEIKTLRLKR
>gnl|CDD|440153 COG0384, YHI9, Predicted epimerase YddE/YHI9, PhzF superfamily [General function prediction only]
MTLPFYQVDAFTDRPFGGNPAAVVLDADGLSDEQMQAIARELNLSETAFVLPPEDPADYRLRWFTPTGEV
PFCGHATLAAAHVLAEEGGLPGGRITFETKAGLLPVEVDGDGAWLEQDFPALPPEPVDPEELAAALGLSA
DDADLPPEVVSTGLPDLLVPLASEEALRALRPDFAALAALSGRLGARGVYVFAPGDDADADFVSRMFAPG
VGIPEDPATGSAAAALAAYLAEKGGKPPTELTAEQGSEMGRPGRLHVELDGDGRVRVGGRAVTVLEGELL
L
>gnl|CDD|440154 COG0385, YfeH, Predicted Na+-dependent transporter YfeH [General function prediction only]
DWFLLLLLLAVVLALLLPAAFEPLLPLLLALIMFGMGLTLSPEDFKRVLRRPRLVLLGLLAQFVLMPLLA
LALALLFGLPPELALGLLLLAACPGGVASNVFTSLARGNVALSVSLTAVSTLLAPFLTPLLVALLLGLQG
VEVDPLDMILSLLLIVLLPLVLGMLLRRLLPKWAERLKKPLPLVSRLAILLIVYAAFAANVDNLLSVGLL
VLLAVLLLNALGLLLGYLLARLLGLDRADRITIAFEVGMKNLGLALVLATTLFPGPLAALPAALYHLWQL
IVGALLARRWARRA
>gnl|CDD|440155 COG0386, BtuE, Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism]
MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQ
EPGSNEEIAEFCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGGDIKWNFTKFLIDRDGNVVA
RFAPTTKPEDPELEAAIEKLL
>gnl|CDD|440156 COG0387, ChaA, Cation (Ca2+/Na+/K+)/H+ antiporter ChaA [Inorganic ion transport and metabolism]
MSLLRRILPLLLLFVPIAALALFLLHGGRWGPVLVFILAALAIIPLAFAAVHHAEVLAHRLGEPFGGLLL
ATFGNAIEVILIISAMLAGEELPTLVRDTIFGAIMINLNGVLGLSLLLGGLRHKEQEFNLQGARAYLSVL
IPLAVLALVLPNFTTSTPGPTFSTAQLIFVAIVLLVLYGLFLLFQTVTHRDYFLPEDEGEEDEDEHEEPP
SKWSLLLSLGLLLVALVAVVLLSEILVGSIEEAVEALGLPEAFVGVIIAILVLAPEGLTAVRAARKNRLQ
LSLNIALGSALASIGLTIPALVLISLLTGQPLTLGFNPFELVLLALTVLVSNLTFSDGRTNWLEGAVHLA
LFAIYAFLFFFP
>gnl|CDD|440157 COG0388, Nit2, Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]
TMRIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPALAAL
AELARELGIAVVVGLPERDEGGRLYNTALVIDPDGEILGRYRKIHLPNYGVFDEKRYFTPGDELVVFDTD
GGRIGVLICYDLWFPELARALALAGADLLLVPSASPFGRGKDHWELLLRARAIENGCYVVAANQVGGEDG
LVFDGGSMIVDPDGEVLAEAGDEEGLLVADIDLDRLREARRRFPVLRDRRPDLY
>gnl|CDD|440158 COG0389, DinP, Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair]
RRILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGVVAAASYEARAFGVRSGMPLFQARRLCPDLVVL
PPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGSARLFGSAEAIARRIRRRIRRETGLTVSVGI
APNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKLARLGIRTIGDLAALPRAELR
RRFGKVGERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERLAERLRRQGLGAR
TVTVKLRTSDFRTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGVRLS
>gnl|CDD|440159 COG0390, FetB, ABC-type iron transport system FetAB, permease component [Inorganic ion transport and metabolism]
MNVIDLSLLDLALAALLVLIALALSRWLKLGLEKDLLIAAVRAVVQLLLVGYVLKYIFALNNPWLTLLML
LVMLLVAARTAAKRGKRRIPGLFWIVLLSILAGTLLVLLLFLLLVIRGAPWYTPQYLIPLAGMILGNAMN
AISLALDRLLSELRSRRGEIEARLALGATPRQAIAPIVREAIRAALIPTINSMATVGLVSLPGMMTGQIL
AGASPLEAVKYQILIMFMILAATALSVVLAVYLAYRRLFNERHQLRLDR
>gnl|CDD|440160 COG0391, CofD, Archaeal 2-phospho-L-lactate transferase/Bacterial gluconeogenesis factor, CofD/UPF0052 family [Carbohydrate transport and metabolism, Coenzyme transport and metabolism]
RRLARGPKVVAIGGGTGLSTLLRGLKRYTANLTAIVTVADDGGSSGRLRRELGVLPPGDLRNCLAALADD
EPLLSRLFQYRFSGGGDLAGHSLGNLLLAALTEITGDFVEAIDLLSKLLGVRGRVLPMTLDPVDLVAELE
DGRIVRGESAIAKAGGRIERVFLEPEDAPATPEALEAIEEADLIVLGPGSLYTSIIPNLLVPGIAEALRE
TKAPKVYVCNLMTQPGETDGYSAADHVRALERHLGGPFIDAVLVNNAPVPDELLERYAEEGAEPVELDRE
RLEELGVRVVRADLLDEDGPVRHDPEKLARALLE
>gnl|CDD|440161 COG0392, AglD2, Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis]
LRAANPWWLLLALLLTLLSYLLLALRWRLLLRALGVKLPFRRLFLVSFIGYFGNNIGPGALGGEAVRARL
LSRRGVPAGKAAAIVALERLTDLLGLLLLAGLGLLFGPGALPGLGNLPGALLLLLLGLALLAAVLLYLLL
LAFRPRLLLRLRRWKLLRKIREKLERFLEGLRRLRLSPRLLLLQLLLSLLDWLLAALILYFLLPALGVDV
SFLAVLAVFLLASLAGLLPPTPGGLGVFEAALLLLLSLFGVPAAAALAALLLYRLIYYLLPLLLGLLLLL
LLELRRRRK
>gnl|CDD|440162 COG0393, YbjQ, Uncharacterized pentameric protein YbjQ, UPF0145 family [Function unknown]
TTTNTIPGYEIVEYLGLVTGETVRSRNIGKDFFAGLRDLVGGESGAYEELLEEAREEALERMKEEARALG
ANAVVGVRFDTSEIGGGMLEVLAYGTAVKVEPE
>gnl|CDD|440163 COG0394, Wzb, Protein-tyrosine-phosphatase [Signal transduction mechanisms]
MMPKRVLFVCTGNICRSPMAEALLRHLAGGRVEVDSAGTEPGGPVDPRAVAVLAERGIDLSGHRSRQLDE
EDLPEFDLVITMCDSAAEELCPLFPGAAKLLLHWDVPDPYYGGLEAFREVRDEIERRIEALLAKLRR
>gnl|CDD|440164 COG0395, UgpE, ABC-type glycerol-3-phosphate transport system, permease component [Carbohydrate transport and metabolism]
MSATARRRRRRLGRILLYLLLILLALLFLFPLYWMVVTSFKPPAEIFSGPPSLLPSEFTLENYRAAFTDG
PFGRYLLNSLIVAVVSTVLSLLLSSLAAYALARFRFRGRKLLFLLILATLMIPGQVLLIPLYLLFRQLGL
LNTYWGLILPYLAFGLPFGIFLLRQFFRSIPRELEEAARIDGASEFRIFWRIVLPLSKPALATVAIFTFI
GAWNDFLWPLILLTSPDLRTLPVGLASFQGQYGTDWGLLMAAAVIATLPVLILFLFLQRYFVRGLTAGAV
KG
>gnl|CDD|440165 COG0396, SufC, Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones]
LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDILELS
PDERARAGIFLAFQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEG
FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKPDF
VHVLVDGRIVKSGGKELALELEEEGYDWLKEEAAA
>gnl|CDD|440166 COG0397, SelO, Protein adenylyltransferase (AMPylase) SelO/YdiU (selenoprotein O) [Posttranslational modification, protein turnover, chaperones]
MTLTTLNFDNSYAQLPPAFYSRVQPTPVPAPRLVALNEELAEELGLDPEALDSPEFAAVFSGNALPPGAE
PLAQAYAGHQFGHWAPQLGDGRAILLGEVVDPDGQRWDLQLKGAGRTPYSRGGDGRAVLRSSLREYLCSE
AMHALGIPTTRALALVTTGEPVYRETVEPGAVLTRVAPSHIRFGTFEYFAARGDLEELRQLADYTIARHY
PELADAENPYLALLREVVERTARLIAQWQRVGFIHGVMNTDNMSILGETIDYGPCAFMDAYDPGTVFNSI
DHQGRYAYGNQPAIALWNLARLAEALLPLIDEDEEAVELAQAALEGFEELFEAAYLAMMRAKLGLATEEE
GDAALIEDLLALMAANEADYTLFFRALSDLDADDALAPLRDLFADRAAFDAWLARWRARLAQEGRSDAER
AAAMRAVNPKYILRNHLAEEAIEAAEQGDYSPFERLLEVLRRPYDEQPEFEDYAAPPPDWARVYETSCSS
>gnl|CDD|440167 COG0398, TVP38, Uncharacterized membrane protein YdjX, related to fungal oxalate transporter, TVP38/TMEM64 family [Function unknown]
MKRLRRLLLLLLLLLALVLLYLLDPEALRAWIESLGPLAPLVFILLYALQTLLPLPGTVLTLAAGALFGP
WLGTLLSLIGATLGALLAFLLARYLGRDFVERLLGKPRLKRLDRLLERNGFLAVFLLRLIPVFPFDLVNY
AAGLTGVRLRTFLLATLLGMLPGTLVYVYLGAGLASLNSLGLLLALALLALLALLGLLLRRLRRRLKKR
>gnl|CDD|440168 COG0399, WecE, dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]
MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPG
DEVITPAFTFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAI
AKKHGLKVIEDAAQALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRD
RDAKYEHVELGYNYRMDELQAAIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHL
YVIRLDEGEDRDELIAALKARGIGTRVHYPIPLHLQPAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTE
EDVDRVIEAIREFL
>gnl|CDD|440169 COG0400, YpfH, Predicted esterase [General function prediction only]
GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAPRAPVPEGPGGRAWFDLSFLEGREDEEGLAAAA
EALAAFIDELEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAALAGT
PVFLAHGTQDPVIPVERAREAAEALEAAGADVTYREYPGGHEISPEELADARAWLAERLA
>gnl|CDD|440170 COG0401, YqaE, Membrane potential modulator PMP3/YqaE, plasma membrane proteolipid 3 (PMP3)/Esi3/RCI2/UPF0057 family [Energy production and conversion]
MDLLRIILAILLPPLGVFLTVGLGKTFWINILLTLLGWIPGIIHALWVIAKRK
>gnl|CDD|440171 COG0402, SsnA, Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]. Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
DLLIRGAWVLTMDPAGGVLEDGAVLVEDGRIAAVGPGAELPARYPAAEVIDAGGKLVLPGLVNTHTHLPQ
TLLRGLADDLPLLDWLEEYIWPLEARLDPEDVYAGALLALAEMLRSGTTTVADFYYVHPESADALAEAAA
EAGIRAVLGRGLMDRGFPDGLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAAL
ARELGLPLHTHLAETRDEVEWVLELYGKRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHC
PTSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRLAALLQRLRGGDPTALSAREALEMAT
LGGARALGLDDEIGSLEPGKRADLVVLDLDAPHLAPLHDPLSALVYAADGRDVRTVWVAGRVVVRD
>gnl|CDD|440172 COG0403, GcvP1, Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport and metabolism]. Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
DEFAMRYIPPTEEDRAEMLAAIGVDSLDELFDDIPAEIRLKRPLDLPEALSEAELLRHLRALAAKNKVLT
SFIGAGYYDHYVPAVVRNILERPEFYTAYTPYQPEISQGRLQALFEFQTMVAELTGMDVANASLYDGATA
AAEAMLMARRVTKRSNKVLVSEDVHPQTRAVLKTYAEPLGIEVVEVPDEDGVTDLEALKALLDDDVAGVL
VQYPNFFGVIEDLRAIAEAAHAAGALVIVAADPLSLGLLKPPGELGADIVVGEGQRLGVPLGFGGPHAGF
FATREKLVRQMPGRLVGVTVDADGKRAFRLTLQTREQHIRREKATSNICTNQALLALAASMYAVYHGPEG
LKEIAERIHQKAHYLAERLAALGVEVPFNGPFFDEFVVRLPKPAAEINAALLEKGILGGLNLRRVDDDTL
LVAVTETTTKEDIDALVEALAE
>gnl|CDD|440173 COG0404, GcvT, Glycine cleavage system protein T (aminomethyltransferase) [Amino acid transport and metabolism]. Glycine cleavage system protein T (aminomethyltransferase) is part of the Pathway/BioSystem: Glycine cleavage
FRPLRRTPLHDRHVALGAKFVDFGGWEMPVQYPGGVIAEHLAVREAVGLFDVSHMGKIEVTGPDAAAFLD
RLVTNDVSKLKPGRARYTLMLNEDGGIIDDLTVYRLGEDRFLLVVNAANAAKDLAWLEEHLPPDFDVTIT
DVTDDWALLAVQGPKAREVLAKLTDADLSALPFMSFREGTVAGVPVRVSRTGYTGEDGFEIYVPAEDAEA
LWDALLEAGEEFGVKPCGLGARDTLRLEAGYPLYGHELDETTTPLEAGLGWAVKLDKGDFIGKEALLRQK
EEGPRRKLVGLELDGRGVPRAGAPVLADGEVVGEVTSGTFSPTLGKSIALAYVPAGLARPGTELEVEIRG
KRVPAEVVKPPFYDPEGERLRG
>gnl|CDD|440174 COG0405, Ggt, Gamma-glutamyltranspeptidase [Amino acid transport and metabolism]
MVATAHPLASQAGLEILRAGGNAVDAAVAAAAALAVVEPHSSGIGGGGFALIYDAKDGKVTALDGRGTAP
AAATPDMYLDAGDEIPVRGPLAVGVPGTVAGWEAAHERYGTLPLAELLAPAIRLAEDGFPVSPRLAALLA
AAAERLARDPGAAAIFLPDGRPPKAGDILRQPDLAATLRRIAEEGADAFYRGEIAEAIVAAVQAAGGLLT
LEDLAAYRAEWREPLSGTYRGYTVYSMPPPSQGIALLQILNILEGFDLAALGPDSAEYVHLLAEAMKLAF
ADRDRYLGDPDFVDVPVEGLLSPAYAAERAALIDPDRATPSPRPGDPTGPESGDTTHLSVVDRDGNAVSL
TQSIYGGFGSGVVVPGTGFLLNNRGDDFSLDPGHPNALAPGKRPRSTMSPTIVLKDGKPVLVFGSPGGSR
IPQTVLQVLLNVLDFGMNPQEAVDAPRWHHQGLPDTLELEPRFPPAVIAALRARGHKVEVVPDWSGGAQA
ILRDPDGVLEGAADPRR
>gnl|CDD|440175 COG0406, PhoE, Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism]
MTRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEAL
GLPVEVDPRLREIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGGESLADVQARVRAALEELLARH
PGGTVLVVTHGGVIRALLAHLLGLPLEAFWRLRIDNASVTVLEFDDGRWRLVALN
>gnl|CDD|440176 COG0407, HemE, Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]. Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis
MTPKERLLRALRGEPVDRVPVWPLTTAALMRQAGRYLPEYCYDPELAAEVTLQPVRRFGVDAAILFSDIL
VEAEALGCKVDFGEGEGPVVEEHPIRDAEDVDALEVPDPEDGRLPYVLEAIRLLKEELGDEVPLIGFAGG
PFTLASYLVEGFEKLKKLMYRDPELVHALLDKLTDAVIEYLKAQIEAGADAVQIFDSWAGLLSPKDFEEF
VLPYLKRIVDALKERGVPVIIHFCGDGTPLLEDMAETGADALSVDWRVDLAEAKERLGDKVALQGNLDPA
LLLLNGTPEEVEAEVKRILDAGGGGPGHIFNLGHGIPPDTPPENVKALVEAVHEYG
>gnl|CDD|440177 COG0408, HemF, Coproporphyrinogen-III oxidase HemH, oxygen-dependent [Coenzyme transport and metabolism]. Coproporphyrinogen-III oxidase HemH, oxygen-dependent is part of the Pathway/BioSystem: Heme biosynthesis
MMEPDKEAVRAWFLDLQDRICAALEALDGKGRFEEDPWERPEGGGGRSRVLENGRVFEKGGVNFSHVHGE
FLPPSATAKRPELAGRRFFATGVSLVAHPRNPYVPTVHMNVRFFEASKPVWWFGGGADLTPYYPFEEDAV
HFHQTAKAACDPFGPDYYPRFKKWCDEYFYLKHRNEPRGVGGIFFDDLNEGDFEADFAFTQDVGDAFLPA
YLPIVERRKDTPYTERERDFQLYRRGRYVEFNLVYDRGTLFGLQTGGRTESILMSLPPLVRWEYDYQPEP
GSPEARLYEDFLKPRDWL
>gnl|CDD|440178 COG0409, HypD, Hydrogenase maturation factor HypD [Posttranslational modification, protein turnover, chaperones]
MKYVDEFRDPELARALAEAIRALADPTRPYRIMEVCGGHTHAIFRYGLRSLLPENIELIHGPGCPVCVTP
MGRIDAAIALARRPGVILCTFGDMLRVPGSRGSLLEAKAEGADVRIVYSPLDALKIARENPDKEVVFFAI
GFETTAPATAAAILQAKAEGLKNFSVLSNHVLVPPALRALLDDPELRIDGFIGPGHVSTVIGSKPYEFIA
EEYGKPIVVAGFEPLDILQAILMLVRQLEEGRAEVENQYTRAVREEGNPKAQALIAEVFEVRDAEWRGLG
EIPGSGLRLREEYAAFDAEKRFGVPVEEVPEPKGCRCGEVLRGLKKPTDCPLFGKACTPENPLGACMVSS
EGACAAYYRYGRLRDAA
>gnl|CDD|440179 COG0410, LivF, ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism]
MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL
PPHRIARLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERVYELFPRLKERRRQRAGTLSGG
EQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLE
RGRIVLEGTAAELLADPEVREAYLGV
>gnl|CDD|440180 COG0411, LivG, ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism]
SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG
LPPHRIARLGIARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPRARREEREARERAEELLERV
GLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIE
HDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPRVIEAYLGEEAAA
>gnl|CDD|440181 COG0412, DLH, Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]
MTTETVTIPTPDGVTLPGYLARPAGGGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGP
GDDPDEARALMGALDPELLAADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFY
GGLPADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAGHGFTNPGRPRYD
PAAAEDAWQRTLAFLA
>gnl|CDD|440182 COG0413, PanB, Ketopantoate hydroxymethyltransferase [Coenzyme transport and metabolism]. Ketopantoate hydroxymethyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
VTVPDLRKMKAGGEKIVMLTAYDAPFARLADEAGVDVILVGDSLGMVVLGYDSTLPVTLDEMIYHTKAVA
RGAKRALVVADMPFGSYQASPEQALRNAGRLMKEAGADAVKLEGGAEMAETIRALVEAGIPVMGHLGLTP
QSVNQLGGYKVQGRTEEAAEKLLEDAKALEEAGAFALVLECVPAELAKEITEALSIPTIGIGAGPDCDGQ
VLVLHDMLGLTDGFKPKFVKRYADLGGSIREAVRAYVEEVKSGSFPAPEHS
>gnl|CDD|440183 COG0414, PanC, Panthothenate synthetase [Coenzyme transport and metabolism]. Panthothenate synthetase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
MKIIRTIAELRAALAAWRAAGKRIGLVPTMGALHEGHLSLVRRARAEADVVVVSIFVNPLQFGPNEDLDR
YPRTLEADLALLEAAGVDLVFAPSVEEMYPEGFSTRVDVGGLSEVLEGASRPGHFDGVATVVTKLFNIVQ
PDVAYFGEKDYQQLAVIRRMVRDLNLPVEIVGVPTVREADGLALSSRNVYLSPEERAAAPALYRALQAAA
EAIAAGERDAAALLAAARAALAAAPFVRLDYVEIVDAETLEPVEEIDGPALLLVAARLGKTRLIDNIVLN
>gnl|CDD|440184 COG0415, PhrB, Deoxyribodipyrimidine photolyase [Replication, recombination and repair]
MMTALVWFRRDLRLHDNPALAAAAESGDPVIPVFILDPEQLGPHPLGAARRWFLHESLAALDASLRELGS
RLIVRRGDPEEVLPALARELGADAVYWNRDYEPYERARDAAVKAALREAGIEVHSFNDHLLFEPGEVLTG
SGTPYKVFTPFWKAWLKRLKRAPLPAPSALPALPIPPESDTLADLGLLPTDGLALLWPPGEAAALERLED
FLDDRLADYDETRDFPALDGTSRLSPHLAFGEISPRQVWHAALAALEEEGGEGAETFLSELAWREFYYHL
LYHFPDLATENFRPEFDAIPWRNDEELFEAWQEGRTGYPIVDAGMRQLNQTGWMHNRVRMIVASFLTKDL
LIDWRWGERWFMDTLVDGDLASNNGGWQWAAGTGTDAAPYFRIFNPVTQGEKFDPDGDYIRRWVPELADL
PAKYIHEPWKAPPLELKARLGKDYPAPIVDHKEARERALAAYKAAK
>gnl|CDD|440185 COG0416, PlsX, Acyl-ACP:phosphate acyltransferase (fatty acid/phospholipid biosynthesis) [Lipid transport and metabolism]
RMRIAVDAMGGDHAPEVIVPGALLALKEHPDLEIILVGDEEAIEPLLAKHPALRDRIEIVHASEVIEMDD
KPSQALRRKKDSSMRVALELVKEGEADACVSAGNTGALMAAALLVLGRLPGIDRPAIAAVLPTLKGPTVL
LDLGANVDCKPEHLVQFAVMGSAYARAVLGIENPRVGLLNIGEEEIKGNELVKEAYELLKESDLNFIGNV
EGRDIFKGTVDVVVCDGFVGNVALKTSEGTAKLILSLLKEEFKRSLLSKLGALLAKPALKRLKKRLDPRE
YGGAPLLGLNGIVIKSHGSSDAKAFANAIRQAAEAVENDVNEKIAERLAEL
>gnl|CDD|440186 COG0417, PolB, DNA polymerase B elongation subunit [Replication, recombination and repair]
MKIPGFLLDRSYRDEDGKPVIELWGRTEDGPSVLLDVTGFRPYFYVPLPDEEKLEELLRDIKEITEVEPV
KLKSFFGEPVPVLKIYTRDPRDVRELRDRLKEGGIDVYEADIRFHDRYLIDRFLTPGVWYEGEVEEDGGK
LDYEVKENPRLKPEDYRPKLKVLSFDIEVSTPRGFPDPERDGPIISIGLAGSDGEKKVLMLGREGVDFEV
EYFDDEKALLEAFFEIIREYDPDIIIGWNVDNFDLPYLQKRAERLGIPLDLGRDGSEPSWREHGGQGFAS
IPGRVVIDLYDALKSATYKFKSYSLDAVAEELLGEGKLIVDGGEIERLWDDDKPALAEYNLRDAELTLRI
FEKTLLLPFLIELSRITGLPLDDVGRAGSSAAFENLLLPEAHRRGYLAPNKGEIKGEAYPGGYVLDPKPG
LYENVLVLDFKSLYPSIIRTFNISPETLVEGGEEPCGDEDVAPGFGHRFCREPKGILPSILEELWDERDE
AKKKMKKAKPDSEEYRLYDALQQALKILMNSFYGVLGSEGCRFYDPELAESITARGREIIKQTIEKAEEL
GYKVIYGDTDSLFVWLPKASLEEAIEIGKELAEEINAWWPSGLELEFEKHYRRFFFPGSKKRYAGLTEDG
KIDIKGLEAVRSDWTELAKEFQQEVYERILKEEDVEKAVEYVRDVIEKLRAGEVDLDDLVIRKRLRKPLS
EYEKNVPPHVRAARKLDERGRPYQRGDKISYVITKGGGRVEPVELAKERESEIDYDYYIEKQLKPTADRI
LEAFGVSFDELKGGSKQLGLFDFF
>gnl|CDD|440187 COG0418, PyrC, Dihydroorotase [Nucleotide transport and metabolism]. Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
MMQTLTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGSDF
EPLMTLYLTDNTTPEEIARAKASGVVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEV
TDPDIDIFDREAVFIDRVLEPLRRRFPELKVVFEHITTKEAVDFVRAAGDNVAATITPHHLLYNRNAMLV
GGIRPHYYCLPILKRETHRQALRAAATSGNPKFFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVF
EEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVPESIPFGDDTLVPFRAGETLNWRVV
>gnl|CDD|440188 COG0419, SbcC, DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]
KLLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEAS
VELEFEHGGKRYRIERRQGEFAEFLEAKPSERKEALKRLLGLEIYEELKERLKELEEALESALEELAELQ
KLKQEILAQLSGLDPIETLSGGERLRLALADLLSLILDFGSLDEERLERLLDALEELAIITHVI
>gnl|CDD|440189 COG0420, SbcD, DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair]
MRFLHTADWHLGKPLHGASRREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRL
SEAGIPVVLIAGNHDSPSRLSAGSPLLENLGVHVFGSVEPEPVELEDGLGVAVYGLPYLRPSDEEALRDL
LERLPRALDPGGPNILLLHGFVAGASGSRDIYVAPVPLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSG
SPEPRSFSEAGGKGVLLVELDAGGLVSVEFVPLPATRRFL
>gnl|CDD|440190 COG0421, SpeE, Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]
EDGRVLVLDGVVQSTMELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEID
PEVVELAREYFPLLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRA
LKPGGVLVVNLGSPFYGLDLLRRVLATLREVFPHVVLYAAPVPTYGGGNVFLLAL
>gnl|CDD|440191 COG0422, ThiC, 4-amino-2-methyl-5-hydroxymethylpyrimidine (HMP) synthase ThiC [Coenzyme transport and metabolism]. 4-amino-2-methyl-5-hydroxymethylpyrimidine (HMP) synthase ThiC is part of the Pathway/BioSystem: Thiamine biosynthesis
MMTQMEYARKGIITPEMEYVAEREGVTPEFVRDEVAAGRIVIPANINHPELEPMGIGRGLRTKVNANIGT
SADTSDIEEEVEKLKWAIKWGADTVMDLSTGGDIDEIRRWILRNSPVPVGTVPIYQALEEAGGSVVDLTW
DDFFDVIEEQAEQGVDFMTIHAGVTLETLERLKKSGRVTGIVSRGGSILAAWMLHNHKENPLYEHFDELL
EILKEYDVTLSLGDGLRPGCIADATDRAQFAELITLGELTKRAWEAGVQVMIEGPGHVPLDQIEANVKLQ
KRLCHGAPFYVLGPLVTDIAPGYDHITSAIGAAIAAWAGADFLCYVTPAEHLGLPNVEDVKEGVIAYKIA
AHAADLAKGHPGARERDDAMSKARFELDWEDQFELALDPEKAREYRDETLPKDAHFCSMCGPFCAMKIVQ
EVLEYAAEKG
>gnl|CDD|440192 COG0423, GRS1, Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]. Glycyl-tRNA synthetase, class II is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MASEDTMEKIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSPII
MPPKVWEASGHVDGFTDPLVDCKECKKRYRADHLIEEYLAIEDAEGLSLEELEELIKENNIKCPNCGGKE
LTEVRQFNLMFKTNIGPVEDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNF
IFRTREFEQMELEFFVDPGTDNEWFAYWLALRKKWLLSLGIDPENLRFRDHLPEELAHYAKATWDIEYEF
PFGWGELEGIAYRTDYDLSRHQEYSGKDLTYFDPETGEKYIPHVIEPSFGVDRLLLAFLEHAYTEEEVDG
EERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKAFNVEYDDSGSIGRRYRRQDEIGTPFCVT
VDFDTLEDNTVTIRDRDTMEQERVPIDELKAYLAELLKGER
>gnl|CDD|440193 COG0424, Maf, 7-methyl-GTP pyrophosphatase and related NTP pyrophosphatases, Maf/HAM1 superfamily [Secondary metabolites biosynthesis, transport and catabolism]
PKLILASASPRRRELLEQLGLPFEVVPPDIDETPLPGESPEELVLRLARAKAEAVAARLPDALVLGADTV
VVLDGRILGKPADAEEARAMLRRLSGRTHRVHTGVALIDPGGRLWTRVVTTRVTFRPLSDAEIEAYLATG
EPLDKAGAYGIQGLGAALVERIEGSYSNVVGLPLIELLELLRELGVDLL
>gnl|CDD|440194 COG0425, TusA, Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ribosomal structure and biogenesis, Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones]
LDARGLSCPLPVLKTKKALEELKPGEVLEVLADDPGAVEDIPAWCRETGHELLSVEEEGGVYRILIRKGG
>gnl|CDD|440195 COG0426, NorV, Flavorubredoxin [Energy production and conversion]
QAVEIAHGVYWVGVLDWDRRLFEGEYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKK
IDYIIVNHQEPDHSGSLPELLELAPNAKIVCSKKAARFLPHFYGIPDFRFIVVKEGDTLDLGGHTLQFIP
APMLHWPDTMFTYDPEDKILFSGDAFGSHGASDELFDDEVDEHLEEEARRYYANIMMPFSKQVLKALKKV
RGLDIDMIAPSHGPIWRGNPKEILDWYRKWSSYQPEKKVVIVYASMYGNTEKMAEAIAEGLTEEGVKVKL
YDLEKTDPSEIITEIFDAKGIVIGSPTYNGGAFPPIADLLGYLKGLAPKNKLAGAFGSYGWSGEAVKLLE
EKLEDAGFEVVFEPLRVKFKPTEEDLKKCEELGTDLAQKL
>gnl|CDD|440196 COG0427, ACH1, Propionyl CoA:succinate CoA transferase [Energy production and conversion]
DRIEYRSKLVSAEEAASLIKSGDRVGVSTGAGEPKALPKALAARAEELFDVELVTGASLGPGALAEADLE
EHFRHRSPFSGGNLRKAINEGRVDYIPIHLSEVPRLLRSGFLPIDVALIEVSPPDEHGYFSLGTSVDNTP
AAVEKAKKVIAEVNPNMPRTLGDIFIHISKIDAIVETDEPLPELPFAPPDEVDRAIAEHIAELIEDGATL
QLGIGGIPNAVLAGLADSKDLGIHTEMLQDGMLDLIEAGVITNASKTIDPGKIVTSFALGSKRLYDFLDD
NPKVELRPVEYSNDPEVIARNLGVIAINSALEVDLYGQVNSESIGTRQYSGIGGQGDFARGAYLSKGGKS
IIALPSTAKGGKISRIVPMLKPGSHVTTTRHDVDYVVTEYGVADLRGKSPRERAEALIEIAHPDFREELR
EYAERAG
>gnl|CDD|440197 COG0428, ZupT, Zinc transporter ZupT [Inorganic ion transport and metabolism]
MSPLLLALLAGLLAGLATLLGALLALFFKRLSKRLLSLLLGFAAGVMLAASFFELLPEALELGEGPLLAA
LGFLLGALLLFLLDRLLPHEHRGAEPAKAHLRRGLLIALGITLHNFPEGLAIGVAFAADPALGLALALAI
ALHNIPEGLAVAAPLRAAGYSRRKALLLGLLSGLVEPLGALLGYLLLSLSPALLPYLLAFAAGAMLYVVV
DELIPEAHREGHSRLATLGLLLGFLLMMLLDVL
>gnl|CDD|440198 COG0429, YheT, Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]
MPLLSTSPFRPPWWLRNGHLQTIYPSLFRRRPALPYRRERLELPDGDFVDLDWSDPPAPSKPLVVLLHGL
EGSSDSHYARGLARALYARGWDVVRLNFRGCGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVG
FSLGGNLLLKYLGEQGDDAPPLKAAVAVSPPLDLAASADRLERGFNRLYQRYFLRSLKRKLRRKLALFPG
LIDLEALKRIRTLREFDDAYTAPLHGFKDAEDYYQRASALPFLPQIRVPTLILNAADDPFLPPECLPEAA
ELNPNVTLELTKHGGHVGFISGKSPGRRYWLERRILEFLDAHL
>gnl|CDD|440199 COG0430, RCL1, RNA 3'-terminal phosphate cyclase [RNA processing and modification]
MIEIDGSYGEGGGQILRTALALSALTGKPVRITNIRAGRPKPGLRPQHLTAVKAAAEICGAEVEGAELGS
TELTFRPGPVRGGDYRFDIGTAGSTTLVLQTLLPALALADGPSRLTLTGGTHVPWSPPFDYLERVFLPLL
RRMGAEAELELLRRGFYPAGGGEVTLTVEPSALLRPLDLLERGELLRVRGISLVANLPAHVAERQAEAAR
ERLGEAGLEVEIEVEVRPALGPGSGIVLWAEYEHGTEGFDALGERGKPAERVGEEAAEELLEFLASGAAV
DEHLADQLLLPLALAGGEGRFTVSELTDHLLTNIWVIEQFLGVRIEVEGEEGGPGRVTVK
>gnl|CDD|440200 COG0431, SsuE, NAD(P)H-dependent FMN reductase [Energy production and conversion]
MKILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLRDLDLPLYDEDLEADGAPPAVKALREAIAAA
DGVVIVTPEYNGSYPGVLKNALDWLSRSELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQV
SIPKAGEAFDEDGELTDEELAE
>gnl|CDD|440201 COG0432, YjbQ, Thiamin phosphate synthase YjbQ, UPF0047 family [Coenzyme transport and metabolism]
QEELTVETTRRRGFIDITDEVEEAVAESGIKEGLVHVFVPHTTASLTINENADPGVRRDLEAFLERLVPE
DDPYRHNLEGPDNMPAHLKASLLGSSLTIPVTDGRLALGTWQGIYLCEFDGRPRRRRVVVTVI
>gnl|CDD|440202 COG0433, HerA, Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair]
KPLPGSPVYLADDEELEELLGDGGGILIGKLLSPGVPVYLDLDKLLNRHILILGATGSGKSNTLQVLLEE
LSRAGVPVLVFDPHGEYSGLAEPGAERADVGVFDPGAGRPLPINPWDLFATASELGPLLLSRLDLNDTQR
GVLREALRLADDKGLLLLDLKDLIALLEEGEELGEEYGNVSAASAGALLRRLESLESADGLFGEPGLDLE
DLLRTDGRVTVIDLSGLPEELQSTFVLWLLRELFEARPEVGDADDRKLPLVLVIDEAHLLAPAAPSALLE
ILERIAREGRKFGVGLILATQRPSDIDEDVLSQLGTQIILRLFNPRDQKAVKAAAETLSEDLLERLPSLG
TGEALVLGEGIPLPVLVKIRLPESRPGGESPDLVREWE
>gnl|CDD|440203 COG0434, BtpA, Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis]
MNLKEIFGTKKPVIGMVHLLPLPGSPRYDGEGLEAIIERALRDARALQEGGVDGIIVENFGDAPFLKDDV
DPETVAAMAAVAGAVRKEVSVPVGVNVLRNDAIAALAIAAATGADFVRVNVFTGAYATDQGLIEGNAAEL
LRYRRRLGAEDVKILADVHVKHASPLGDRPLEEAARDTVERGLADAVIVSGARTGEATDLEDLKRVKEAA
PDVPVLVGSGVTPENVAELLSVADGAIVGSSLKRDGKTWNPVDPERVRRFMEAVRRLR
>gnl|CDD|440204 COG0435, ECM4, Glutathionyl-hydroquinone reductase [Energy production and conversion]
MGLLVDGKWHDDWYDTKDTGGRFVRQESQFRNWITADGSGGFPAEAGRYHLYVSLACPWAHRTLIFRALK
GLEDAISVSVVHPLMLEDGWTFSPDPGATPDPLNGARYLHELYTKADPDYTGRVTVPVLWDKQTGTIVNN
ESAEIIRMLNSAFDGLAGNDLDLYPEALREEIDALNDRIYDTVNNGVYRAGFATTQEAYEEAVDELFDAL
DWLEERLSDQRYLCGDRLTEADWRLFTTLVRFDAVYHGHFKCNRRRIADYPNLWGYLRDLYQLPGVAETV
DFDHIKRHYYGSHPTINPTGIVPLGPDLDLDAPHDRDRLGG
>gnl|CDD|440205 COG0436, AspB, Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]. Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
MKLSSRLARLPPSPIREVSALAAELKAAGEDVIDLGIGEPDFPTPDHIREAAIEALDDGVTGYTPSAGIP
ELREAIAAYYKRRYGVDLDPDEILVTNGAKEALALALLALLNPGDEVLVPDPGYPSYRAAVRLAGGKPVP
VPLDEENGFLPDPEALEAAITPRTKAIVLNSPNNPTGAVYSREELEALAELAREHDLLVISDEIYEELVY
DGAEHVSILSLPGLKDRTIVINSFSKSYAMTGWRIGYAVGPPELIAALLKLQSNLTSCAPTPAQYAAAAA
LEGPQDYVEEMRAEYRRRRDLLVEGLNEIGLSVVKPEGAFYLFADVPELGLDSEEFAERLLEEAGVAVVP
GSAFGPAGEGYVRISYATSEERLEEALERLARFLERY
>gnl|CDD|440206 COG0437, HybA, Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion]
LSMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPCVK
VCPTGATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPT
GALVFGDLDDPESEVSKRLAELPAYRLLPELGTKPSVYYLPKRN
>gnl|CDD|440207 COG0438, RfaB, Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]
MGRLVPRKGLDLLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPP
GDPEALAEAILRLLEDPELRRRLGEAARERAEERFSWEAIAERLLALYEELLA
>gnl|CDD|440208 COG0439, AccC, Biotin carboxylase [Lipid transport and metabolism]. Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
DIDAIIAAAAELARETGIDAVLSESEFAVETAAELAEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVP
GFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFL
EGREYSVEGLVRDGEVVVCSITRKHQKPPYFVELGHEAPSPLPEELRAEIGELVARALRALGYRRGAFHT
EFLLTPDGEPYLIEINARLGGEHIPPLTELATGVDLVREQIRLALGEPRILDP
>gnl|CDD|440209 COG0440, IlvH, Acetolactate synthase, small subunit [Amino acid transport and metabolism]. Acetolactate synthase, small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
RHTISVLVENEPGVLARVAGLFSRRGYNIESLTVGPTEDPGISRMTIVVEGDERVIEQITKQLNKLIDVI
KVVDLTDEESVERELALIKVKADGETRSEILRIAEIFRARIVDVTPDSLTIELTGDEEKIDAFIELLKPY
GILEVVRTGRVALSRGSKSL
>gnl|CDD|440210 COG0441, ThrS, Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MIKITLPDGSVREFEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEI
LRHSAAHLLAQAVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVS
REEAIELFKEKGEPYKVELIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEK
NKMLQRIYGTAFPKKKELDAYLHRLEEAKKRDHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDY
IREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFPTESDGEEYALKPMNCPGHILIYKSGLRSYRD
LPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEDYYVKL
STRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLP
ERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEVAK
KLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE
EIRSRSLEP
>gnl|CDD|440211 COG0442, ProS, Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MRASKLFIPTLKERPADAEVWSHQLMLRAGLIRKLASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVL
MPLLQPAELWEESGRWEGFGPELARVTDRLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFR
DEIRPRFGLLRTREFLMKDAYSFHATEEELDEEYQKMLDAYERIFERLGLPVRAVEADSGAIGGSESHEF
MVLADSGEDTIVYCDACDYAANIEKAEALAPPAERAEPTKELEAVATPGAKTIEEVAEFLGVPAEKTVKT
LVYKADGELVAVLVRGDHELNEIKLENLLGASELELATEEEIEAALGAVPGFLGPVGLGVPYIADRSVAG
MSNFVCGANEDDYHYTNVNWGRDFPVDEVADLRNVVEGDPCPDCGGLLQDGRGIEVGHIFKLGTKYSKAM
DATFLDENGKEQPVWMGCYGIGVTRLIAAAIEQHHDDKGIIWPPAIAPFQVVIVPINMKDEAVLEAAEEL
YAELKAAGIDVLLDDRDERPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKRRDTGEKEEVPLDELVETV
KELL
>gnl|CDD|440212 COG0443, DnaK, Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones]
AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKRQAVTNPGRTIRSIKRLL
GRSLFDEATEVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLE
VLRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALAD
YVAPEFGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLPFSGGKHLDVELTRAEFEELIAPLV
ERTLDPVRQALADAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLA
GDVKDLDVTPLSLGIETLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGR
FELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLGTGKEQSITIKEEIERML
>gnl|CDD|440213 COG0444, DppD, ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism]
LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGE
DLLKLSEKELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDP
ERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD
LGVVAEIADRVAVMYAGRIVEEGPVEELFENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSG
CRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLYEEEAP
>gnl|CDD|440214 COG0445, MnmG, tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]. tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification
MYYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEM
GRAADKTGIQFRMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVT
ADGIEFRAKAVVLTTGTFLNGLIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSI
DFSKLEEQPGDEPPPPFSFLTEKIHPPQIPCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIE
DKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQLAMLRSIPGLENAEILRPGYAIEYDYVDPT
QLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFILDRSEAYIGVLIDDLVTKG
TDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKSTRVTPNEEV
NEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKL
KRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA
>gnl|CDD|440215 COG0446, FadH2, NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism]
RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVT
LRDGETLSYDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELA
EALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDKVAVTLTDGEEIPAD
LVVVAPGVRPNTELAKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQ
GRVAAENILGGPAPFPGLGTFISKVFDLCIASTGTGRLLGAQ
>gnl|CDD|440216 COG0447, MenB, 1,4-Dihydroxy-2-naphthoyl-CoA synthase [Coenzyme transport and metabolism]. 1,4-Dihydroxy-2-naphthoyl-CoA synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
MSSEIFDPIRWRTVKDYTDITYHRAEGIARIAINRPEVRNAFRPETVDELYDALDHAREDPDVGVVLLTG
NGPSKDGGWAFCSGGDQRVRGRGGYVYEDGVGRLNILEVQRLIRFMPKPVIAMVAGWAIGGGHVLHVVCD
LTIASENARFGQTGPDVGSFDAGYGSAYLARQVGQKKAREIWFLCRQYSAQEALEMGLVNKVVPHAELEE
EAVEWAREILEKSPTAIRMLKAAFNADDDGLAGQQEFAGEATRLAYMTDEAQEGRDAFLEKRKPDFSKFP
W
>gnl|CDD|440217 COG0448, GlgC, Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism]
KVLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGK
PWDLDRKRGGVFILPPYQQREGEDWYQGTADAVYQNLDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIE
SGADITVACIEVPREEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDVLIELLEEDAPNSS
HDFGKDIIPRLLDRGKVYAYEFDGYWRDVGTIDSYYEANMDLLDPEPEFNLYDPEWPIYTKQKDLPPAKF
VRGGKVKNSLVSNGCIISGTVENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGV
VIGEDPEEDRKRFTVSSGIVVVGKGAV
>gnl|CDD|440218 COG0449, GlmS, Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis]
MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGIG
HTRWATHGAPSDENAHPHTSCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGG
GDLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLED
GEIAVLTRDGVEIYDLDGEPVEREVKTVDWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGRVV
LDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEFRYRDPVVDPGTLVIAISQ
SGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAALYLLALYL
ARARGTLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALKLKE
ISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELA
DDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE
>gnl|CDD|440219 COG0450, AhpC, Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms]
MMPLIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVI
GLSVDSVFSHKAWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEV
YPLSVGRNVDEILRVVDALQFVDKHGEVCPANWKPGDKVIIPPPDLVGKALERFPE
>gnl|CDD|440220 COG0451, WcaG, Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]
RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEFVRGDLRDPEALAAALAGVDAVVH
LAAPAGVGEEDPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVYGDGEGPIDEDTPLRPVSPYGASK
LAAELLARAYARRYGLPVTILRPGNVYGPGDRGVLPRLIRRALAGEPVPVFGDGDQRRDFIHVDDVARAI
VLALEAPAAPGGVYNVGGGEPVTLRELAEAIAEALGRPPEIVYPARPGDVRPRRADNSKARRELGWRPRT
SLEEGLRETVAWYRA
>gnl|CDD|440221 COG0452, CoaBC, Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]. Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
MLAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEA
EMGHIELARWADLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATL
RERGVHIIGPASGELACGDVGKGRMAEPEEIVEAIEALLAPKKDLAGKKVLITAGPTREPIDPVRFISNR
SSGKMGYALAEAAAARGAEVTLVSGPVALPTPAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYR
PAEVADQKIKKTDDPLTLELVKNPDILAELGARKKPGQFLVGFAAETENLLENARAKLARKNLDLIVAND
VSDAGAGFGSDTNAVTLLDKDGREEELPLMSKLEVARRILDEIAELLAA
>gnl|CDD|440222 COG0454, PhnO, N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only]
MSIRKATPEDINFILLIEALDAELKAMEGSLAGAEFIAVDDKGEPIGFAGLRRLDDKVLELKRLYVLPEY
RGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFEKELSLS
>gnl|CDD|440223 COG0455, FlhG, MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility]
TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAGEADLEDAIVQGPGGLDVLPGGSG
PAELAELDPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLL
RRRLGVRRAGVVVNRVRSEAEARDVFERLEQVAERFLGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDS
PAARAIRELAARLAGWPVPE
>gnl|CDD|440224 COG0456, RimI, Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis]
GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGF
EEVGERPNYYGDDALVMEKELA
>gnl|CDD|440225 COG0457, TPR, Tetratricopeptide (TPR) repeat [General function prediction only]
LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALE
LDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELD
PDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKK
LAILTLAALAELLLLALALLLALRLAALALYQYRA
>gnl|CDD|440226 COG0458, CarB, Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]. Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEK
PDGVIVQFGGQTALNLAVELEEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEE
ALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDG
EDNVIIVGIMEHIEPAGVHSGDSICVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYV
IEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGNDTGFEPTLDYVVVKEPVFPFEKFPGVDPVL
GPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLLSLVADDDKEEALLLARRLARLGFLIEATRGTA
EVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLLGAKSLGDSDGIIRRALAAKVPYVTTLAAAA
AAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS
>gnl|CDD|440227 COG0459, GroEL, Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]
MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGA
QLVKEVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDK
EELAQVATISANGDEEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKM
PAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGF
GDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAKRVEVDKDNTTIVEGAGNPKAIVILVGAATE
VEVKERKRRVEDALHATRAAVEEGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIA
ENAGLDGSVVVEKVRAAKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADK
PEKEEAA
>gnl|CDD|440228 COG0460, ThrA, Homoserine dehydrogenase [Amino acid transport and metabolism]. Homoserine dehydrogenase is part of the Pathway/BioSystem: Methionine biosynthesis
LENAEELARRLGLDLRVVGVAVRDGMKPRGIDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLA
ALEAGKHVVTANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTT
NYILTKMEEEGLSFSEALKEAQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRIT
AEDIAAAKELGYVIKLLAIAERTGGGVEARVHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAG
AEPTASAVLADLLDIARGLRAG
>gnl|CDD|440229 COG0461, PyrE, Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]. Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
MSYKEELAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGP
ATGGIPLAAAVARALGLPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGA
EVVGVAVIVDREEGAAENLEEAGVPLHSLLTLDDLLELLKEKGYIDPEELEALEAYREKPG
>gnl|CDD|440230 COG0462, PrsA, Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]. Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis
MKDLKIFSGNANPELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIEESVRGRDVFVIQSTSPPVNDNLMEL
LIMIDALKRASARRITAVIPYYGYARQDRKFRPREPITAKLVADLLEAAGADRVLTVDLHAPQIQGFFDI
PVDHLYAAPLLADYIKSKDLEDLVVVSPDVGGVKRARAFAKRLGAPLAIIDKRRPGANEVEVMNIIGDVE
GKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAAATHGVLSGPAVERLENSPIDELVVTDTIPLPEEKR
CDKIKVLSVAPLLAEAIRRIHEGESVSSLFD
>gnl|CDD|440231 COG0463, WcaA, Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]
MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGK
GAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVR
LLTNLPDSTSGFRLFRREVLEELGFDEGFLEDTELLRALRHGFRIAEVPVRYRAGESKLNLRDLLRLL
>gnl|CDD|440232 COG0464, SpoVK, AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLL
LALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYED
IGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARA
LAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNT
LLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAE
ATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEALEREDIFLKR
>gnl|CDD|440233 COG0465, HflB, ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones]
IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTKTRFTTYRVNDPELVD
LLEEKGVEVTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVT
FDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSD
FVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEG
VIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGAD
LANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADP
VHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARA
MVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLD
ALAEALLEKETLDGEELEEILAG
>gnl|CDD|440234 COG0466, Lon, ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones]
MSEEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDD
LYEVGTVAKILQLLKLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLEEEEEDDKELEALMRSLKEQ
FEEYVKLNPKIPPELLAALSNIEDPGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVL
ELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGEKDDGEDEIEELREKIEKAKLPEEVKEKAEKELKK
LERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKL
KGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKN
PVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRME
IIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVA
KKIAEGKKKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLT
GQLGDVMKESAQAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPV
RSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVL
KIALEKEPEPLPKKE
>gnl|CDD|440235 COG0467, RAD55, RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]
RVPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLLRRAESL
GLDLEEYIESGLLRIIDLSPEELGLDLEELLARLREAVEEFGAKRVVIDSLSGLLLALPDPERLREFLHR
LLRYLKKRGVTTLLTSETGGLEDEATEGGLSYLADGVILLRYVELGGELRRALSVLKMRGSAHDRTIREF
EITDGGIEVGE
>gnl|CDD|440236 COG0468, RecA, RecA/RadA recombinase [Replication, recombination and repair]
MAKKVASSEKEKALEAALSQIEKQFGKGSIMRLGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYG
PESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSG
AVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNP
ETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTRVKVVKNKVAPPFKEAEFDIMYGEGISKEGELLD
LAVELGIIEKSGAWYSYGGERLGQGRENAKQFLKENPELAEEIEAKIREKLGLGAVSEAAAAEEEEDEEE
E
>gnl|CDD|440237 COG0469, PykF, Pyruvate kinase [Carbohydrate transport and metabolism]. Pyruvate kinase is part of the Pathway/BioSystem: Glycolysis
MMRRTKIVATLGPASDSPEVLRKLIEAGMDVARLNFSHGDHEEHRERIELIREAAKELGRPVAILLDLQG
PKIRTGKFKEGPVELKKGDTFTLTTDDVEGDAERVSVTYPELPEDVKPGDRILLDDGKIELRVEEVEGDE
VVCEVVNGGVLSSRKGVNLPGVGLSLPALTEKDREDLKFALELGVDFIALSFVRSAEDVLEARELLEEAG
GRAPIIAKIEKPEAVENLDEIIEASDGIMVARGDLGVEIPLEEVPLIQKRIIRKARRAGKPVITATQMLE
SMIENPRPTRAEVSDVANAVLDGTDAVMLSGETAVGKYPVEAVETMARIAEEAEKSLDYRRILDRLRDEP
ERTITDAIARAAVELAEDLGAKAIVAFTESGSTARRISRYRPKVPILALTPNERTARRLALVWGVYPVLV
DDVESTDEMIEEAVEALLEEGLVKPGDLVVITAGVPVGVPGTTNTLKVHRV
>gnl|CDD|440238 COG0470, HolB, DNA polymerase III, delta prime subunit [Replication, recombination and repair]
QEEAWEQLLAAAESGRLPHALLLHGPPGIGKTTLALALARDLLCENPEGGKACGQCHSRLMAAGNHPDLL
ELNPEEKSDQIGIDQIRELGEFLSLTPLEGGRKVVIIDEADAMNEAAANALLKTLEEPPKNTPFILIAND
PSRLLPTIRSRCQVIRFRPPSEEEALAWLREEGVDEDALEAILRLAGGDPRAAINLLQALAGRKELLEDL
AALLSRDRALELLDALLKAEALELLDWLLKWLLDNLPLEYAGEDLARAYEALSEADRRLGRYANDRLLLE
ALLAKLGRL
>gnl|CDD|440239 COG0471, CitT, Di- and tricarboxylate antiporter [Carbohydrate transport and metabolism]
LGGFVLAAALEKTGLGRRIALLLLKRFGGSPLRLLLGLMLATALLSAFISNTARAAMMLPIALSIAAALG
SEKRSKFGSALLLPIAFAASIGGMGTLIGTPPNLIAAGLLEEATGIPISFFEWMLVGLPVALVGLLLLWL
VLYRLLPPEIKEVPGSKEVIREELAELGPLSRREKIALAIFALTVLLWITGSLHGIPIAVVALLGAVLLL
LTGVLTWKDAYKSIPWGVLLLFGGGLALGAALEKTGLAAWLADALLPLLGGLSPLLLLLLLALLTLLLTE
FASNTATAALLLPIAISLAQALGVNPLPLALAVAFAASCAFLLPVGTPPNAIVYGSGYYKFKDFLKVGLP
LNLIGLVVLLLLGPLWWPL
>gnl|CDD|440240 COG0472, Rfe, UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate transferase [Cell wall/membrane/envelope biogenesis]. UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate transferase is part of the Pathway/BioSystem: Mureine biosynthesis
LRLLLAFLLAFLLSLLLTPLLIRLARRLGLVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALLSNPE
LLLLLLGALLLGLIGFLDDLLGLSARQKLLGQLLAALLLVLLLLRITSLTIPFFGLLDLGWLYIPLTVFW
IVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDT
GSLFLGFALAALAILGRQEGASLLLLLLILGVPVVDTLSVILQRVLRGKRIFKADRAHLHHHLELLGWSE
RQVVLRFW
>gnl|CDD|440241 COG0473, LeuB, Isocitrate/isopropylmalate dehydrogenase [Energy production and conversion, Amino acid transport and metabolism]. Isocitrate/isopropylmalate dehydrogenase is part of the Pathway/BioSystem: TCA cycle
TYKIAVLPGDGIGPEVVAAALKVLEAAAERFGLDFEFEEADIGGAAYDKTGTPLPDETLEALRKADAILL
GAVGGPKWDDGVRPESGLLALRKELDLYANLRPAKLYPGLPSPLKPEIVEGIDLVIVRENTEGLYFGIGG
RIGTGTGEEVAIDTRVYTRKGIERIARYAFELARKRRKKVTSVDKANVLKLTSGLWREVVREVAKEYPDV
ELDHMYVDAAAMQLVRNPEQFDVIVTENLFGDILSDLAAGLTGSLGLAPSANIGDEGKALFEPVHGSAPD
IAGKGIANPIATILSAAMMLRHLGEEEAADAIEAAVEKVLAEGVRTPDLGGKAGTSEMGDAIIAAL
>gnl|CDD|440242 COG0474, MgtA, Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]
MATALKDWHALSAEEVLAELGTSEEGLSSEEAARRLARYGPNELPEEKKRSLLRRFLEQFKNPLILILLA
AAVISALLGDWVDAIVILAVVLLNAIIGFVQEYRAEKALEALKKLLAPTARVLRDGKWVEIPAEELVPGD
IVLLEAGDRVPADLRLLEAKDLQVDESALTGESVPVEKSADPLPEDAPLGDRGNMVFMGTLVTSGRGTAV
VVATGMNTEFGKIAKLLQEAEEEKTPLQKQLDRLGKLLAIIALVLAALVFLIGLLRGGPLLEALLFAVAL
AVAAIPEGLPAVVTITLALGAQRMAKRNAIVRRLPAVETLGSVTVICTDKTGTLTQNKMTVERVYTGGGT
YEVTGEFDPALEELLRAAALCSDAQLEEETGLGDPTEGALLVAAAKAGLDVEELRKEYPRVDEIPFDSER
KRMSTVHEDPDGKRLLIVKGAPEVVLALCTRVLTGGGVVPLTEEDRAEILEAVEELAAQGLRVLAVAYKE
LPADPELDSEDDESDLTFLGLVGMIDPPRPEAKEAIAECRRAGIRVKMITGDHPATARAIARQLGLGDDG
DRVLTGAELDAMSDEELAEAVEDVDVFARVSPEHKLRIVKALQANGHVVAMTGDGVNDAPALKAADIGIA
MGITGTDVAKEAADIVLLDDNFATIVAAVEEGRRIYDNIRKFIKYLLSSNFGEVLSVLLASLLGLPLPLT
PIQILWINLVTDGLPALALGFEPVEPDVMKRPPRWPDEPILSRFLLLRILLLGLLIAIFTLLTFALALAR
GASLALARTMAFTTLVLSQLFNVFNCRSERRSFFKSGLFPNRPLLLAVLLSLLLQLLLIYVPPLQALFGT
VPLPLSDWLLILGLALLYLLLVELVKLLRRRFGR
>gnl|CDD|440243 COG0475, KefB, Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism]
LLASLLLQLGLLLLAAVLAGLLARRLGLPSVLGYILAGILLGPSGLGLIEDSEALELLAELGVVLLLFLI
GLELDLKRLRKMGRRALGIGLLQVLLPFLLGFLLALLLGLSLAAALFLGAALAATSTAIVLKVLKELGLL
KTPLGQLILGVALFDDIAAILLLALVPALAGGGSVAGSLLLALLKALLFLALLLLVGRYLLRRLFRLVAR
TRSRELFLLFALLLVLLAAALAELLGLSAALGAFLAGLVLAESEYRHELEEKIEPFGDLFLPLFFVSVGL
SLDLSALLSNPLLALLLVLAAIVGKLLGAYLAARLFGLSRREALRIGLLLAPRGEFALVLASLGLSAGLI
SPELFAALVLVVLLTTLLTPLLLRLALRLAERAK
>gnl|CDD|440244 COG0476, ThiF, Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]. Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis
TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQ
ILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVK
LGIPLVSGAVIGFEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGI
GEPLAGRLLLFDALTMEFRTIKLPRDPDCPVCGE
>gnl|CDD|440245 COG0477, ProP, MFS family permease, includes anhydromuropeptide permease AmpG [Carbohydrate transport and metabolism, Amino acid transport and metabolism, Inorganic ion transport and metabolism, General function prediction only]
MSSTDAAPTRRRRRALLALALGTFLEGLDFTIVNVALPSIAADLGASSAQLGWIVSAYLLGRAIGLLLFG
RLGDRYGRKRVLLIGLLLFGLASLLCGLAPSPELLIAARALQGIGAGGLMPGALALIAELFPARERGRAL
GLWGAAIGLGLALGPLLGGLLVAALGWRWIFLINAPLGLLALVLRLRLPESRGLLLALLALALAALLLAA
LALALLALLLLLLLLLLALLALLLAGAALLLLLALLLLALLLLLALLLLAALLLLLLLLLLLALLLALLL
LLLLLLLLLLLALLL
>gnl|CDD|440246 COG0478, RIO2, RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms]
MVEKSPGGGPVALKFHREGRTSFRKVRRERADKEHYSWLYAARTRAEREFRALERLYPAGLPVPRPIAAN
RHAIVMERIEGVELARLKLEDPEEVLDKILEEIRRAHDAGIVHADLSEYNILVDDDGGVWIIDWPQAVPR
DHPNAEELLERDLENLLRSFRKKYGLEVDLDEVWAALLGGYES
>gnl|CDD|440247 COG0479, SdhB/FrdB, Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]. Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle
MTVTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRP
RLACQTHVRDLKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDNERLQSPEDREKADD
LAECILCGACVAACPNVWANPDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVC
PKGIPPTKAIAKLKREALKR
>gnl|CDD|440248 COG0480, FusA, Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]. Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
MAEYPLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDGNTVMDWMPEEQERGITITSAATTCE
WKGHKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREG
ADFDRVLEQLKERLGANPVPLQLPIGAEDDFKGVIDLVTMKAYVYDDELGAKYEEEEIPAELKEEAEEAR
EELIEAVAETDDELMEKYLEGEELTEEEIKAGLRKATLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSP
LDVPAIKGVDPDTGEEVERKPDDDEPFSALVFKTMTDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERI
GRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDEDHPIVLEPIEFPEPVISVAIEPKTKADEDK
LSTALAKLAEEDPTFRVETDEETGQTIISGMGELHLEIIVDRLKREFGVEVNVGKPQVAYRETIRKKAEA
EGKHKKQSGGHGQYGDVWIEIEPLPRGEGFEFVDKIVGGVIPKEYIPAVEKGIREAMEKGVLAGYPVVDV
KVTLYDGSYHPVDSSEMAFKIAASMAFKEAAKKAKPVLLEPIMKVEVTVPEEYMGDVMGDLNSRRGRILG
MESRGGAQVIKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEEVPANVAEKIIAKRKAEKE
>gnl|CDD|440249 COG0481, LepA, Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis]
MDQKNIRNFSIIAHIDHGKSTLADRLLELTGTLSEREMKEQVLDSMDLERERGITIKAQAVRLNYKAKDG
ETYQLNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSA
DPERVKQEIEDIIGIDASDAILVSAKTGIGIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSYRGVVV
YVRVFDGTLKKGDKIKMMSTGKEYEVDEVGVFTPKMTPVDELSAGEVGYIIAGIKDVRDARVGDTITLAK
NPAAEPLPGFKEVKPMVFAGLYPVDSDDYEDLRDALEKLQLNDASLTYEPETSAALGFGFRCGFLGLLHM
EIIQERLEREFDLDLITTAPSVVYEVTLTDGEVIEVDNPSDLPDPGKIEEIEEPIVKATIITPSEYVGAV
MELCQEKRGVQKNMEYLGENRVELTYELPLAEIVFDFFDRLKSITRGYASLDYEFIGYRESDLVKLDILI
NGEPVDALSFIVHRDKAYSRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVLAKCYGGD
ISRKRKLLEKQKEGKKRMKQVGNVEIPQEAFLAVLKVD
>gnl|CDD|440250 COG0482, MnmA, tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]. tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification
KRVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDASGSGGCCSLEDIEDARRVADKLGIPHYVVD
FEEEFKDRVIDYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEEKDGRYELLRG
VDPNKDQSYFLYRLTQEQLSKTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYL
PEKPGDIVDLDGKVLGEHDGLHYYTIGQRKGLGIGGGEPLYVVGKDPETNTVIVGQGEALYSRELTAEDV
NWISGEPPEEPLRCTAKIRYRQPPVPATLTPLEDGRVRVEFDEPQRAVTPGQSAVFYDGDRVLGGGIIER
TER
>gnl|CDD|440251 COG0483, SuhB, Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family [Carbohydrate transport and metabolism]. Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family is part of the Pathway/BioSystem: Gluconeogenesis
HPLLELALRAARAAGALILRRFRELDLEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGAS
EGRDSGYVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRV
SARTDLEDALVATGFPYLRDDREYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIA
AGALIVREAGGVVTDLDGEPLDLGSGSLVAANPALHDELLALLRE
>gnl|CDD|440252 COG0484, DnaJ, DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones]
DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAE
LLLATELAESAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLALLELALAAVLGLLLALA
>gnl|CDD|440253 COG0486, MnmE, tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]. tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification
TIAAIATPPGRGGIGIIRISGPDALEIADKLFGPKLAEPKPRTAHYGHIRDPDGEVIDEVLVLYFPAPHS
YTGEDVVEIHCHGGPAVLQRILELLLKLGARLAEPGEFTKRAFLNGKLDLTQAEAVADLIDAETEAAARQ
ALRQLSGALSRRIEELRERLLDLLALIEAAIDFPEEDVEFLDREELLERLEELREELEALLASARQGELL
REGIKVVIVGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIEERINIGGIPVRLIDTAGLRETEDEVEK
IGIERAREAIEEADLVLLLLDASEPLTEEDEEILEKLKDKPVIVVLNKIDLPSEADGELKSLPGEPVIAI
SAKTGEGIDELKEAILELVGEGALEGEGVLLTNARHREALERALEALERALEALESGLPLELLAEDLRLA
LDALGEITGEVTTEDLLDRIFSRFCIGK
>gnl|CDD|440254 COG0488, Uup, ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only]
LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEP
PLDDDLTVLDTVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLG
FPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRY
FLDRVATRILELDRGKLTLYPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQ
SRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPN
GAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRFL
FSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRY
FLDRVATRILEFEDGGVREYPGGYDDYLEK
>gnl|CDD|440255 COG0489, Mrp, Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning]
ALLAALELLLLREEAQALLLLLLLLLLLLRLEEAAAAAALAAAAPAAAAPAPLPPAPALLLLLLLLLGLL
LLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRML
GLENRPGLSDVLAGEASLEDVIQPTEVEGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTP
PGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNMVCPKGERYYGGGEEYGY
REYGDREIA
>gnl|CDD|440256 COG0490, KhtT, K+/H+ antiporter KhtSTU, c-di-AMP-binding regulatory subunit KhtT, contains RCK_C (TrkA_C) domain [Inorganic ion transport and metabolism, Signal transduction mechanisms]
AALALLLLLIILLLLLALAALLVAIVIVGVLGLILRGLLLLELALLLLLLGELLRLLTRLLIELVLLLAI
EEVKVPPGSPLVGKTLGELNLRQRTGVTVVAIRRGGEVILSPGPDTVLEAGDTLVVVGTREQLERLEELL
>gnl|CDD|440257 COG0491, GloB, Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only]
VYVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAA
LAEAFGAPVYAHAAEAEALEAPAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVP
DEKVLFTGDALFSGGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEELLAALGER
ANPFL
>gnl|CDD|440258 COG0492, TrxB, Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]
YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFPEGISGPELAERLREQAERF
GAEILLEEVTSVDKDDGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFR
GKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDGRVE
GVTLKNVKTGEEKELEVDGVFVAIGLKPNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKY
RQAATAAGEGAIAALSAARYLEPLK
>gnl|CDD|440259 COG0493, GltD, NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]. NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEV
CGRVCPAPCEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQL
ARAGHEVTVFEALDKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAV
FLATGAGKPRDLGIPGEDLKGVHSAMDFLTAVNLGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAE
SVTIVYRRTREEMPASKEEVEEALEEGVEFLFLVAPVEIIGDENGRVTGLECVRMELGEPDESGRRRPVP
IEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWA
IAEGRKAARAIDRY
>gnl|CDD|440260 COG0494, MutT, 8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX family [Defense mechanisms]
MTEILSSEPEHYRPAVVVVLLDDDGRVLLVRRYRYGVGPGLWEFPGGKIEPGESPEEAALRELREETGLT
AEDLELLGELPSPGYTDEKVHVFLARGLGPGEEVGLDDEDEFIEVRWVPLDEALALVTAGEIAKTLAALA
RLL
>gnl|CDD|440261 COG0495, LeuS, Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MQERYNPKEIEKKWQKYWEENGTFKADEDSSKPKYYVLDMFPYPSGRLHMGHVRNYTIGDVVARYKRMQG
YNVLHPMGWDAFGLPAENAAIKNGVHPAEWTYENIANMRRQLKRLGLSYDWSREIATCDPEYYKWTQWIF
LQLYEKGLAYRKEAPVNWCPVDQTVLANEQVIDGRCWRCGAPVEKKELPQWFLKITDYADELLDDLDKLD
GWPEKVKTMQRNWIGRSEGAEVDFPVEGSDEKITVFTTRPDTLFGATFMVLAPEHPLVKELATPEQNAAV
AAFIEEAKKKSEIERTSETKEKTGVFTGLYAINPLTGEKIPIWIADYVLMDYGTGAVMAVPAHDQRDFEF
AKKYGLPIKQVIAPEDGDDPDILEEAYTGDGVLINSGEFDGLDSEEAKEAIIEWLEEKGLGKRKVNYRLR
DWLISRQRYWGEPIPIIHCEDCGVVPVPEDQLPVELPEDVDFDPTGGSPLARAPEWVNVTCPKCGGPARR
ETDTMDTFVDSSWYYLRYTDPHNDEAPFDPEAANYWLPVDQYIGGIEHAILHLLYARFFTKVLRDLGLVS
FDEPFKRLLTQGMVLEVGKDGVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLFEMFAGPPERDLEWSD
SGVEGAYRFLNRVWRLVVDEAEALKLDVADLSEADKELRRALHKTIKKVTEDIERLRFNTAIAALMELVN
ALYKAKDSGEADRAVLREALETLVLLLAPFAPHIAEELWERLGHEGSVADAPWPEADEAALVEDEVTIVV
QVNGKVRGKIEVPADASKEELEAAALADEKVQKFLEGKTIRKVIVVPGKLVNIVVK
>gnl|CDD|440262 COG0496, SurE, Broad specificity polyphosphatase and 5'/3'-nucleotidase SurE [Replication, recombination and repair]
LLTNDDGIDAPGLRALAEALAELGEVTVVAPDREQSGAGHSLTLHRPLRVRKVELPGVGAYAVDGTPADC
VKLALNGLLDEKPDLVVSGINHGANLGDDVLYSGTVAAAMEGALLGIPAIAVSLAVGGDPADFETAARVA
RRLVEKLLENGLPPGTLLNVNVPDVPAEEIKGVKVTRQGRRHYAEEVEKRVDPRGRPYYWLGGEGLEEDA
EEGTDVAALAEGYISVTPLQLDLTAYEALDELKEL
>gnl|CDD|440263 COG0497, RecN, DNA repair ATPase RecN [Replication, recombination and repair]
MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDL
SDDPPLAAWLEENGLDLDDGELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDP
DAQRELLDAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEE
LEEERRRLSNAEKLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEA
ASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTVEELLAYAEELRAELAELENSDERLEELEAEL
AEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTPLEEPGPNGADQVEFLFSANPG
EPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEKLARLARNHQVLCVTH
LPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALAHARELLALAAS
>gnl|CDD|440264 COG0498, ThrC, Threonine synthase [Amino acid transport and metabolism]. Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
KLRCTRCGATFSDALLYLCPDCGGLLPDSYPALSREDLASRRGLWRYRELLPFDDEEKAVSLGEGGTPLV
KAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASSGNGSAALAAYAARAGIEVF
VFVPEGKVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSINPARLEGQKTYAFEIAEQ
LGRVPDWVVVPTGNGGNILAGYKAFKELKELGLIDRLPRLIAVQATGCNPILTAFETGRDEYEPERPETI
APSMDIGNPSNGERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEGEID
PDEPVVVLSTGHGLKFPDAVREALGGEPLAVPPDLEAVKAAVEE
>gnl|CDD|440265 COG0499, SAM1, S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism]
TAPMDYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGG
AEVRWASCNPLSTQDDVAAALAAAGIPVFAWKGETLEEYYWCIEQALDHGPNIILDDGGDLTLLLHKERP
ELLAGIIGGTEETTTGVHRLRAMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGK
TVVVAGYGWCGKGVAMRARGLGARVIVTEVDPICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITA
EHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRPQVDEYTLPDGRRIYLLAEGRLVNLAAATGHP
SEVMDMSFANQALAQIYLVKNGDKLEPGVYVLPKELDEEVARLKLEALGVKIDTLTEEQAEYLGSWVEGP
>gnl|CDD|440266 COG0500, SmtA, SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]
PWDSYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAA
KAGLGNVEFLVADLAELDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSASDAAAAL
SLARLLLLATASLLELLLLLRLLALELYLRALLAAAATEDLRSDALLESANALEYLLSK
>gnl|CDD|440267 COG0501, HtpX, Zn-dependent protease with chaperone function [Posttranslational modification, protein turnover, chaperones]
DPELYRLVEELAARAGIPMPEVYVMDSPAPNAFATGRGPNNARIVVTDGLLELLDRDELEAVLAHELGHI
KNGDILLMTLASGLLGLIGFLARLLPLAFGRDRDAGLLLGLLLGILAPFLATLIQLALSRKREYEADRAA
AELTGDPDALASALRKLAGGNLSIPLRRAFPAQAHAFIINPLKLSSLFSTHPPLEERIARLRELAAEGEY
>gnl|CDD|440268 COG0502, BioB, Biotin synthase or related enzyme [Coenzyme transport and metabolism]. Biotin synthase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
DLTREEALALLELPDEELEDLLAAADEVREHFFGNKVQLCGLINIKSGGCPEDCKYCGQSAHNKTGIERY
RLLSVEEILEAARAAKEAGARRFCLVASGRDPSDRDFEKVLEIVRAIKEELGLEVCASLGELSEEQAKRL
KEAGVDRYNHNLETSPELYPKICTTHTYEDRLDTLKNAREAGLEVCSGGIVGMGETLEDRADLLLTLAEL
DPDSVPINPLIPIPGTPLEDAPPLDPEEFLRTIAVARLLLPDALIRLSGGRETLLRDGQALALLAGANSI
MPGNKYLTTPGRSVEEDLAMIEDLGLEV
>gnl|CDD|440269 COG0503, Apt, Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]. Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage
EDLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYAL
GVPFVPARKPGKLPGETVSEEYDLEYGTGDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGA
EVVGIAFLIELGFLGGREKLRDYPVESLLTL
>gnl|CDD|440270 COG0504, PyrG, CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]. CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis
TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLD
LGHYERFLDINLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEESGADVVIVE
IGGTVGDIESLPFLEAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVC
RSERPLPEEIKRKIALFCNVPEEAVISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELV
ERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANGVKVNIKWIDSEDLEEENAEELLKGVDGILV
PGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEQ
KDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYREQLEKAGLVFSGTSPDGRLVE
IVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKKKK
>gnl|CDD|440271 COG0505, CarA, Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]. Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDF
ESDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIE
ELLEKARAAPGMEGLDLVKEVSTKEPYEWTEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSA
EEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANH
PVKDLETGRVEITSQNHGFAVDEDSLPATDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSA
YLFDRFIELME
>gnl|CDD|440272 COG0506, PutA, Proline dehydrogenase [Amino acid transport and metabolism]. Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
MTAALDEALRARAVALARRLVEAIRAAPEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIR
DKLAKSPSFLVNASTWGLMLTLVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVS
LDLLGEAVLTEAEAERYLDAYLEALEAIGAAGVDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLAR
AAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRI
RVRLVKGAYWDPEIVRAQVHGWPYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALA
GERGRPPDRFEFQMLYGMGEDLQRALAAVDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVAD
FDDDEDLLEFPREPPRFLAALAAPTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAAL
AAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA
EAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGLVALLPLGPLAAAAA
AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALT
LAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASL
LSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGG
PLVPGLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGA
GGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAAAAA
>gnl|CDD|440273 COG0507, RecD, ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair]
LLEIREAWAEQGIYRIGIFADFIARDDPIRAAALLSRAAGEGHTFPLEDLAAARLLGVAEDIEAALAALV
ESGPLVLDGRRYLTRLLEAEQRLARRLRRLARPALDEADVEAALAALEPRAGITLSDEQREAVALALTTR
RVSVLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKAAKRLSESTGIEARTIHRLLGLRPDSGRFRH
NRDNPLTPADLLVVDEASMVDTRLMAALLEALPRAGARLILVGDPDQLPSVGAGAVLRDLIESGTVPVVE
LTEVYRQADDSRIIELAHAIREGDAPEALNARYADVVFVEAEDAEEAAEAIVELYADRPAGGEDIQVLAP
TNAGVDALNQAIREALNPAGELERELAEDGELELYVGDRVMFTRNDYDLGVFNGDIGTVLSIDEDEGRLT
VRFDGREIVTYDPSELDQLELAYAITVHKSQGSTFDRVILVLPSEHSPLLSRELLYTALTRARELLTLVG
DRDALARAVRRDTARATGLAERLR
>gnl|CDD|440274 COG0508, AceF, Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]. Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVG
AVIAVIA
>gnl|CDD|440275 COG0509, GcvH, Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]. Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
MEIPDDLKYTEDHEWVRVEGDGTATVGITDFAQDLLGDIVFVELPEVGTEVEAGEPFGVVESVKAVSDLY
APVSGEVVEVNEALEDDPELVNEDPYGEGWLFKIKPSDPAELDDLLDAEAYAALLEEE
>gnl|CDD|440276 COG0510, CotS, Thiamine kinase or a related kinase [Coenzyme transport and metabolism]
RLHASPALLRFDLFARLERYLALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGRLY
LIDWEYAGLGDPAFDLAALLVEYGLSPEQAEELLEAYGFGRPTEELLRRLRAYRALADLLWALWALVRAA
QEANGDLLKYLLRRLE
>gnl|CDD|440277 COG0511, AccB, Biotin carboxyl carrier protein [Lipid transport and metabolism]. Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
LIELLEESGLTELEVEEGEYKVRIKRGGAAAAAPVAAPAAAAPAAAAPAAAAAAAAASGGGAVKSPMVGT
FYRAPSPGAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE
>gnl|CDD|440278 COG0512, PabA, Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]. Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAG
KIPILGVCLGHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDEL
EVTAWTEDGEIMGIRHRELPIEGVQFHPESILTEHGHQLLANFLELAGE
>gnl|CDD|440279 COG0513, SrmB, Superfamily II DNA and RNA helicase [Replication, recombination and repair]
MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR
APQALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGA
LDLSGVETLVLDEADRMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPEN
ATAETIEQRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQR
ERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDER
RLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRGGRPGPKGERKARRGKRRRRKR
>gnl|CDD|440280 COG0514, RecQ, Superfamily II DNA helicase RecQ [Replication, recombination and repair]
LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALM
KDQVDALRAAGIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEA
HCISQWGHDFRPDYRRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVV
PKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDE
VDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSP
PDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLGPPETFDGTEAAQKALSCVYR
TGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQLFGERKLERYGEAFL
>gnl|CDD|440281 COG0515, SPS1, Serine/threonine protein kinase [Signal transduction mechanisms]
MSALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIV
RVYDVGEEDGRPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL
TPDGRVKLIDFGIARALGGATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDG
DSPAELLRAHLREPPPPPSELRPDLPPALDAIVLRALAKDPEERYQSAAELAAALRAVLRSLAAAAAAAA
AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAA
LLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAL
AAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAAAALALA
>gnl|CDD|440282 COG0516, GuaB, IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]. IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis
LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLL
KKKKFLLLVDDDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGGDAMKKIKLTFDDVLLI
PGNSATVEPARALVDAGADLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMAIAIAADGGIGYIH
DNAKALAAGADAVMLGSLFAGTEEQPGEVILYQGRSVKRYRGMGSDAKKLVPEGIEGRVPYKGPLEDTLH
QLLGGLRSGMGYCGARTIEELREKARFVRITSAGLRESHPHDVDIE
>gnl|CDD|440283 COG0517, CBS, CBS domain [Signal transduction mechanisms]
MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVS
EVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA
>gnl|CDD|440284 COG0518, GuaA1, GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]. GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
KILILDHDPFGGQYPGLIARRLREAGIELDVLRVYAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLED
EPALIREAFELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADPLFAGLPDEFTVWMSHGD
TVTELPEGAEVLASSDNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADELAAEELLAEASLHDPEL
REAGRRLLRNFLREI
>gnl|CDD|440285 COG0519, GuaA2, GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]. GMP synthase, PP-ATPase domain/subunit is part of the Pathway/BioSystem: Purine biosynthesis
MDKEIIIVLDFGGQYQQLIARRRREEGVYSEIIPPDTAAEEIKAKGPPGIILSGGPSSVYEEGAPPDDPE
LFELGGPILGICYGGQLMLHLLGGGVVRAERREYGGALLLVDDESDLFAGGPEELQVWMSHGDRVTELPP
GFEVIASTENCPVAAIANEERKLYGVQFHPEVVHTEQGKEILKNFLFDICGCKGDWTMENFIEEAIEEIR
EQVGDGKVICALSGGVDSSVAAALLHKAIGDQLTCVFVDHGLLRKGEAEQVEETFKEHFGLNLIYVDASE
RFLSALKGVTDPEEKRKIIGEEFIEVFEEEAKKLGGAKFLAQGTLYPDVIESGSVKGPAATIKSHHNVGG
LPEDMKFKLVEPLRELFKDEVRALGRELGLPEEIVYRHPFPGPGLAIRILGEVTKEKLEILREADAIFIE
ELRKAGLYDKVWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSVDGMTADWARLPYEVLERISNRIINE
VKGVNRVVYDITSKPPATIEWE
>gnl|CDD|440286 COG0520, CsdA, Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]
DVEAIRADFPVLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVAR
FIGAASPDEIIFTRGTTEAINLVAYGLGRLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDG
ELDLEALEALLTPRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFY
AFSGHKLYGPTGIGVLYGKRELLEALPPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAI
DYLEAIGMEAIEARERELTAYALEGLAAIPGVRILGPADPEDRSGIVSFNVDGVHPHDVAALLDDEGIAV
RAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKLAEL
>gnl|CDD|440287 COG0521, MoaB, Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]. Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis
MSSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEG
VDLVLTTGGTGLSPRDVTPEATRPLLDKELPGFGELFRALSLEEIGPSAILSRAVAGIRGGTLIFNLPGS
PGAVREALEAILPELPHAVDLLNGVDHEC
>gnl|CDD|440288 COG0522, RpsD, Ribosomal protein S4 or related protein [Translation, ribosomal structure and biogenesis]. Ribosomal protein S4 or related protein is part of the Pathway/BioSystem: Ribosome 30S subunit
MARYTGPKCKLCRREGVKLFLKGERKCALERRPYPPGQHGQRRKKLSDYGLQLREKQKLRRIYGVLEKQF
RRYFEEAARRKGNTGENLLQLLERRLDNVVYRLGFAPTRAQARQLVSHGHILVNGKKVNIPSYQVKPGDV
IEVREKSKKLPRIKEALESAEQRGVPEWLEVDAEKLSGTVVRLPEREEIPVPINEQLIVELYSR
>gnl|CDD|440289 COG0523, YejR, Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only]
DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRDTDEEIVELSNGCICCTLR
EDLLPALRRLLRRGRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLADRTLH
ELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARP
GWLEELRDHEHDDGIRSFVFRSDRPFDPERLADFLEELGPGVLRAKGFLWLAGRPRRLVFQGVGGRLSLE
PLGPWPADDRRSRLVFIGRDLDEAALEAALDACLLTDA
>gnl|CDD|440290 COG0524, RbsK, Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]. Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLA
ELRAEGVDTSGVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLGGITLAS
EPPREALLAALEAARAAGVPVSLDPNYRPALWEPARELLRELLALVDILFPNEEEAELLTGETDPEEAAA
ALLARGVKLVVVTLGAEGALLYTGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANA
AAALVVTRPGAQPALPTREEV
>gnl|CDD|440291 COG0525, ValS, Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MELPKTYDPKEVEAKWYQYWEENGYFKADPDSDKEPFTIVIPPPNVTGSLHMGHALNNTLQDILIRYKRM
QGYNTLWQPGTDHAGIATQAVVERQLAEEGKSRHDLGREKFLERVWEWKEESGGTITNQLRRLGASCDWS
RERFTMDEGLSKAVREVFVRLYEKGLIYRGKRLVNWDPKLKTALSDLEVEHEEVKGHLWHIRYPLADGSG
YIVVATTRPETMLGDTAVAVHPEDERYKHLIGKTVILPLVGREIPIIADEYVDPEFGTGAVKITPAHDPN
DFEVGKRHNLPMINILDEDGTINENAGKYRGLDRFEARKAIVADLEELGLLVKVEPHKHSVGHSDRSGTV
IEPYLSDQWFVKMKPLAKPAIEAVEDGEIKFVPERWEKTYFHWMENIRDWCISRQLWWGHRIPAWYCPDG
EVYVARTEPEACAKAGSVNLTQDEDVLDTWFSSALWPFSTLGWPEKTEDLKYFYPTSVLVTGFDIIFFWV
ARMIMMGLHFTGEVPFKDVYIHGLVRDEQGRKMSKSKGNVIDPLDLIDKYGADALRFTLAALASPGRDIK
FDEERVEGYRNFANKLWNASRFVLMNLEGFDPGLDPDPEELSLADRWILSRLNKTIAEVTEALEKYRFDE
AAQALYDFVWNEFCDWYLELAKPRLYGGDEAAKRETRATLVYVLEQILRLLHPFMPFITEEIWQKLPPRK
EGESIMLAPWPEADEELIDEEAEAEFEWLKEVISAIRNIRAEMNIPPSKKLPLLLKGADEADRARLEENA
AYIKRLARLEEITILVDEKPEGAASAVVGGAEVFLPLEGLIDVEAERARLEKELAKLEKEIARVEKKLSN
EGFVAKAPAEVVEKEREKLAEAEAKLEKLEEQLARLK
>gnl|CDD|440292 COG0526, TrxA, Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]
MKAVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDEN
PEAVKAFLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK
>gnl|CDD|440293 COG0527, MetL1, Aspartate kinase [Amino acid transport and metabolism]. Aspartate kinase is part of the Pathway/BioSystem: Lysine biosynthesis
MALIVQKFGGTSVADAERIKRVADIVKKAKEAGNRVVVVVSAMGGVTDLLIALAEELLGEPSPRELDMLL
STGEQLSAALLAMALQELGVPAVSLDGRQAGIITDDNHGKARIDLIETPERIRELLEEGKVVVVAGFQGV
TEDGEITTLGRGGSDTTAVALAAALKADECEIWTDVDGVYTADPRIVPDARKLPEISYEEMLELAYLGAK
VLHPRAVEPAMKYNIPLRVRSTFNPDAPGTLITAEDEMEGPVVKGIASDKDIALITVSGVPMVDEPGFAA
RIFSALAEAGINVDMISQSSSETSISFTVPKSDLEKALEALEEELKLEGLEEVEVEEDLAKVSIVGAGMR
SHPGVAARMFSALAEAGINIRMISQGSSEISISVVVDEEDAEKAVRALHEAFFLDKE
>gnl|CDD|440294 COG0528, PyrH, Uridylate kinase [Nucleotide transport and metabolism]. Uridylate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
MSKPKYKRVLLKLSGEALAGEGGFGIDPEVLDRIAEEIKEVVDLGVEVAIVIGGGNIFRGASGAAKGMDR
ATADYMGMLATVMNALALQDALEKLGVPTRVQSAIEMPQVAEPYIRRRAIRHLEKGRVVIFAAGTGNPYF
TTDTAAALRAIEIGADVLLKATKVDGVYDADPKKNPDAKKYDRLTYDEVLAKGLKVMDATAFSLCRDNNL
PIIVFNMNKPGNLLRAVLGEKIGTLVSG
>gnl|CDD|440295 COG0529, CysC, Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]. Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDR
DENIRRIGEVAKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKAR
AGEIKNFTGIDDPYEAPENPELVLDTDKESVEESVEKILAYLEERGYIS
>gnl|CDD|440296 COG0530, ECM27, Ca2+/Na+ antiporter [Inorganic ion transport and metabolism]
ADLLVRGADALARRLGISPLVIGLTIVAFGTSLPELAVSVTAALDGSPDIAVGNVVGSNIANILLILGLA
ALIRPLAVDRRVLRRDLPFLLLASLLLLALLLDGTLSRIDGVILLLLYVLYLYYLIRRARKEPAWEEVEE
ELEEKPKMSLWKALLLLVLGLALLVVGARLLVDGAVEIARALGVSELVIGLTIVAIGTSLPELATSIVAA
RKGEDDLAVGNIIGSNIFNILLVLGIGALITPIPVDPAVLSFDLPVMLAATLLLLGLLRTGGRIGRWEGL
LLLALYLAYLALL
>gnl|CDD|440297 COG0531, PotE, Serine transporter YbeC, amino acid:H+ symporter family [Amino acid transport and metabolism]
MSRGESSELKRKLGLFDLVALGVGAIIGAGIFVLPGLAAGLAGPAAILAWLIAGLLALLVALSYAELASA
FPRAGGAYTYARRALGPLLGFLAGWALLLSYVLAVAAVAVAFGGYLSSLFPAGGSVLIALVLILLLTLLN
LRGVKESAKVNNILTVLKLLVLLLFIVVGLFAFDPANFTPFLPAGGGLSGVLAALALAFFAFTGFEAIAN
LAEEAKNPKRNIPRAIILSLLIVGVLYILVSLALTGVVPYDELAASGAPLADAAEAVFGPWGAILIALGA
LLSLLGALNASILGASRLLYAMARDGLLPKVFAKVHPRFGTPVNAILLTGVIALLLLLLGAASFTALASL
ASVGVLLAYLLVALAVIVLRRRRPDLPRPFRVPLPLIPILGILLCLFLLYLLGPGALLIGLVLLAIGLLL
YLLYRRRHPKLLKEAEEE
>gnl|CDD|440298 COG0532, InfB, Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]. Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
VPRPPVVTVMGHVDHGKTSLLDAIRKTNVAAGEAGGITQHIGAYQVETNGGKITFLDTPGHEAFTAMRAR
GAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDKPGANPDRVKQELAEHGLVPEEWGGD
TIFVPVSAKTGEGIDELLEMILLQAEVLELKANPDRPARGTVIEAKLDKGRGPVATVLVQNGTLKVGDIV
VAGTAYGRVRAMFDDRGKRVKEAGPSTPVEILGLSGVPQAGDEFVVVEDEKKAREIAEKRQQKAREKKLA
RQKRVSLEDLFSQIKEGEVKELNLILKADVQGSVEALKDSLEKLSTDEVKVNIIHSGVGAITESDVNLAA
ASNAIIIGFNVRPDAKARKLAEREGVDIRYYSIIYDLIDDVKAAMEGMLEPEYKEEILGRAEVREVFKVS
KVGTIAGCYVTEGKIKRNAKVRVLRDGVVIYEGELESLKRFKDDVKEVRAGYECGIGLKNFNDIKEGDII
EAFEMEEVKRTL
>gnl|CDD|440299 COG0533, TsaD, tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]. tRNA A37 threonylcarbamoyltransferase TsaD is part of the Pathway/BioSystem: tRNA modification
MLILGIETSCDETAAAVVDDGRGLLSNVVASQIDLHARYGGVVPELASRAHLENILPLVEEALEEAGVTL
KDIDAIAVTAGPGLIGALLVGVSFAKALALALGKPLIGVNHLEGHLLAPFLEDPPPEFPFLALLVSGGHT
QLVLVKGVGDYELLGETIDDAAGEAFDKVAKLLGLGYPGGPAIDKLAKEGDPKAFRFPRPMLDRPGLDFS
FSGLKTAVLNYIEKLKQKGEEQDKADIAASFQEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRER
LEELAEKRGIRLFFPPLELCTDNAAMIAAAGYERLKAGEFSDLDLNARPRLPL
>gnl|CDD|440300 COG0534, NorM, Na+-driven multidrug efflux pump, DinF/NorM/MATE family [Defense mechanisms]
LTEGPILKLLLRLALPIILGNLLQSLYGLVDTIFVGRLGTAALAAVGLAFPIFFLLIALGIGLGVGGTAL
VAQALGAGDREEARRVLGQALLLALLLGLLLTLLGLLFAPPLLRLLGADPEVLALARDYLRIILLGLPFL
LLFNVLNGILRGLGDTKTPMIIMLIGNVLNIVLDPLLIFGGGLGVAGAALATVISQAVSALLLLYYLFRK
RSLLRLRLRDLRPDRKILKRILRIGLPAGLQQLAESLGFLVLNALVARLGTAAVAAYGIALRIESLAFMP
ALGLGQAAQPLVGQNLGAGDYDRARRAARLALLLALGIGLLLALLLFLFPEPIIGLFTDDPEVIALAATY
LRIAALFQPFDGLQFVLSGALRGAGDTRFPMIISLLRLWLVRLPLAYLLAFLGLGLTGVWLALPIGEVLR
ALLLLLR
>gnl|CDD|440301 COG0535, SkfB, Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism]
RLQIELTNRCNLRCKHCYADAGPKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAK
ELGIRVNLSTNGTLLTEELAERLAEAGLDHVTISLDGVDPETHDKIRGVPGAFDKVLEAIKLLKEAGIPV
GINTVYPCPFLPELSLGNA
>gnl|CDD|440302 COG0536, Obg, GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, chromosome partitioning, Replication, recombination, and repair]
FVDEAKIYVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGDVILVADENLNTLLDFRYKRHFKAENGEN
GMGKNRTGKNGEDLVIKVPVGTVVKDAETGEVLADLTEDGQRVVVAKGGRGGLGNAHFKSSTNRAPRFAE
PGEPGEERWLRLELKLLADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRSFVIA
DIPGLIEGASEGAGLGHRFLRHIERTRVLLHVVDAAPLDGRDPVEDYEIIRNELEAYSPELAEKPRIVVL
NKIDLLDAEELEELKAELEKLGGPVFPISAVTGEGLDELLYALAELLEELRAEEAEEEEEVEE
>gnl|CDD|440303 COG0537, HinT, Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide transport and metabolism, General function prediction only]
MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKA
LRKALGPDGFNLGINNGEAAGQTVPHLHVHVIPRYEGDDNFMPVIGTKVDPEELEETARKLRA
>gnl|CDD|440304 COG0538, Icd, Isocitrate dehydrogenase [Energy production and conversion]. Isocitrate dehydrogenase is part of the Pathway/BioSystem: TCA cycle
MEGEKIKVEDGKLKVPDNPIIPFIEGDGIGPEITRAIWKVIDAAVEKAYGGKRDIEWKEVDAGEKARDET
GDWLPDETAEAIKEYGVGIKGPLTTPVGGGWRSLNVTIRQILDLYVCRRPVRYFKGVPSPVKHPEKVDIV
IFRENTEDIYAGIEWKAGSPEALKLIFFLEDEMGVTVIRFPEDSGIGIKPVSDEGTERLVRAAIQYALDN
KRKSVTLVHKGNIMKFTEGAFKDWGYEVAEEEFGDKFITEGPWEKYKGPKPAGKIVYKDRIADDMLQQIL
LRPGEYDVIATKNLNGDYISDALAAQVGGLGIAPGANIGDDGGAEFEATHGTAPKYAGKDSTNPGSLILS
GTMMLRHRGWLEAADLIEKAVEKTIESGKVTYDLARLMEGATELSTSEFGDAIIENLDK
>gnl|CDD|440305 COG0539, RpsA, Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S1 is part of the Pathway/BioSystem: Ribosome 30S subunit
MSESFAELLEESLKELKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDEPGELEVKVGDEVEVYV
EKVEDGEGEIVLSKKKADREKAWEELEEAFENGEPVEGKVKGVVKGGLIVDIGGVRAFLPASQVDVRPVR
DLDEYVGKTLEFKIIKLDRKRNNVVVSRRAVLEEEREEKREELLEKLEEGDVVEGTVKNITDFGAFVDLG
GVDGLLHISEISWGRVKHPSEVLKVGDEVEVKVLKIDREKERISLSLKQLQPDPWENIAEKYPVGDVVKG
KVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHPSDVVKVGDEVEVKVLDIDPEERRISLSIKQLA
>gnl|CDD|440306 COG0540, PyrB, Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]. Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis
MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLG
ADVINFSASTSSVSKGESLADTIRTLEAYGADAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQAL
LDLYTIREEFGRLDGLKVAIVGDLKHSRVARSNIKALSKLGAEVTLVAPPTLLPEEIEELGVEVTTDLDE
ALPDADVVYMLRIQKERFTDGLFPSYREYKRSYGLTAERLALAKPDAIVMHPGPRNRGVEIDSDVDDTPR
SVIFEQVTNGVAVRMALLYLLLGGEE
>gnl|CDD|440307 COG0541, Ffh, Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport]
MFENLSERLQGAFKKLRGKGRLTEENIKEALREVRRALLEADVNLKVVKDFIERVKERALGEEVLKSLTP
GQQVIKIVHDELVELLGGENEELNLAKKPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYR
PAAIEQLKTLGEQIGVPVFPEEDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAA
VNPDETLLVVDAMTGQDAVNVAKAFNEALGLTGVILTKLDGDARGGAALSIRAVTGKPIKFIGTGEKLDD
LEPFHPDRMASRILGMGDVLSLIEKAQEAIDEEEAEKLAKKLKKGKFDLEDFLEQLQQMKKMGPLKKLLG
MLPGMGKLKQLKDLDIDEKELKRIEAIINSMTPEERRNPDIINGSRKRRIAKGSGTTVQDVNRLLKQFEQ
MKK
>gnl|CDD|440308 COG0542, ClpA, ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones]
MNFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGR
LPKVSGSSGQPYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREA
LEELRGGSRVTSQNPESKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPG
VGKTAIVEGLAQRIVNGDVPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDE
LHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISI
LRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAAARVRMEIDSKPEELDELERRL
EQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL
EKELAELEEELAELAPLLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHERVIGQDEAVEA
VADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVSRLIGA
PPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSN
IGSELILDLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAE
RGITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGELV
>gnl|CDD|440309 COG0543, Mcr1, NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]
KVVSVERLAPDVYLLRLEAPLIALKFKPGQFVMLRVPGDGLRRPFSIASAPREDGTIELHIRVVGKGTRA
LAELKPGDELDVRGPLGNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALLARGRRVTLYLGARTPEDLYLL
DELEALADFRVVVTTDDGWYGRKGFVTDALKELLAEDSGDDVYACGPPPMMKAVAELLLERGVPPERIYV
SLERRMACGIGMCGGCVVPVGGGCKDGPVFDAAEVDW
>gnl|CDD|440310 COG0544, Tig, FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, protein turnover, chaperones]
MKVTVEKLEGLKRKLTVEVPAEEVEKAVDKALKKLAKKVNIPGFRKGKVPRSVVEKRYGKEVLEEALNEL
LPEAYEEAVEEEKLRPAGQPEIDVVELEEGKDLEFTAEVEVRPEVELGDYKGLEVEKPVVEVTDEDVDEE
LERLREQFATLVPVERAAEEGDRVTIDFEGTIDGEEFEGGKAEDYSLELGSGSFIPGFEEQLVGMKAGEE
KTFEVTFPEDYHAEELAGKTATFKVTVKEVKEKELPELDDEFAKKLGEFETLEELKADIRENLEREKKQR
ARAKLKDQVLDALVENNEFDLPEALVEREIDRLLEQAEQQLQQQGLQDTGKTEEELREEFREQAERRVKL
GLILDEIAKKENIEVTDEEVEAEIEEMAQQYGMPPEEVKEYLQNPGQLEQLRADVLEEKVVDFLLEKAKV
TEKE
>gnl|CDD|440311 COG0545, FkpA, FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones]
LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKR
RLVIPPELAYGERGAGGVIPPNSTLVFEVELLDV
>gnl|CDD|440312 COG0546, Gph, Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion]
IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLLGEDPDEELEELLAR
FRELYEEELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAK
PKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAGADYVIDSLAELLA
LLAE
>gnl|CDD|440313 COG0547, TrpD, Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and metabolism]. Anthranilate phosphoribosyltransferase, glycosyltransferase domain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
MMKELLKKLAEGKDLTREEAREAMRQIMSGEATPAQIGAFLTALRMKGETVEEIAGFADAMRELAVPVPL
PDGDVVDIVGTGGDGANTFNISTAAAFVAAAAGVPVAKHGNRSVSSKSGSADVLEALGVNLDLSPEQVAR
CLEEAGIGFLFAPLFHPAMKHVAPVRKELGVRTIFNLLGPLTNPAGPKRQLLGVYHPELVEPLAEVLQLL
GVKRALVVHGLDGLDEISLTGPTKVAELRDGEIEEYTLDPEDFGLPRAPLEDLRGGDAEENAEILRAVLA
GEGGPARDAVLLNAAAALYVAGKADSLAEGVELAREAIDSGAALAKL
>gnl|CDD|440314 COG0548, ArgB, N-acetylglutamate kinase [Amino acid transport and metabolism]. N-acetylglutamate kinase is part of the Pathway/BioSystem: Arginine biosynthesis
MESAIEKAEWLREALPYIQAFRGKTFVIKYGGEAMEDEELKAALAQDIALLKSLGIRPVLVHGGGPQINE
LLKRLGIESEFVNGLRVTDEETLEVVEMVLAGKVNKEIVALLSQGGGNAVGLSGKDGNLITARPLGVGDG
VDLGHVGEVRRVDPELIRALLDAGYIPVISPIGYSPTGEVYNINADTVAGAIAAALKAEKLILLTDVPGV
LDDPGSLISELTAAEAEELIADGVISGGMIPKLEAALDAVRGGVKRVHIIDGRVPHALLLELFTDDGIGT
MIV
>gnl|CDD|440315 COG0549, ArcC, Carbamate kinase [Amino acid transport and metabolism]
MKKRIVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAAKKK
VPPMPLDVCGAMTQGMIGYMLQQALRNELPKRGIDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEA
EELAKEKGWTFKEDAGRGYRRVVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVRDEDGGLKGVEA
VIDKDLASALLAEELDADLLLILTDVDKVYINFGKPDQRALDEVTVAEAKKYIEEGHFAAGSMGPKVEAA
IRFVEATGKRAIITSLEKAEEALAGKAGTRIVP
>gnl|CDD|440316 COG0550, TopA, DNA topoisomerase IA [Replication, recombination and repair]
KKLVIVESPAKAKTIAKYLGKDYVVTASVGHLRDLPKPELDVDVENDFEPKYEVIPGKKKQVKELKKLAK
KADEVILATDPDREGEAIAWHLLELLGDKKPVKRVVFNEITKKAIKEAFKNPRDIDMNLVDAQQARRILD
RLVGYNLSPLLWKKVKRGLSAGRVQSPALRLIVEREREIEAFVPEEYWTIEATFKTGGGEFTAKLVKIDG
KKILDEEEAEAILAALKGKTFTVTSVEKKPKKRNPPPPFTTSTLQQEASRKLGFSAKKTMSIAQRLYEVG
LITYMRTDSVRLSEDAVAAAREYIEALYGKEYLPEKPRVYKTSKNAQEAHEAIRPTGVTRTPESLSGDEF
KLYDLIWKRFLASQMPPAEYETTTVTIEVGGEEFRASGKVIKFPGFLKVYGEGKDDEEEEEEKRLPPLKE
GEKLKLKKIEPEQHFTKPPPRYTEASLVKAMEELGIGRPSTYASIIETLQDRGYVEREGKRLVPTELGFI
VIDLLEEHFPDLVDYEFTAKMEEKLDEIAEGKLDWKDVLEEFYKPFKELVE
>gnl|CDD|440317 COG0551, YrdD, DNA topoisomerase I, ssDNA-binding Zn-finger and Zn-ribbon domains [Replication, recombination and repair]
AEKEIAAALAAAKEAVKLVKKKKKKKKEGKKKGLAGALGLKKKLVDLLLKEKLKKLVENEKLIAELDIKD
LKKLKKDKKKKAKALAAALAAADDDAIEAAAAADEEEALKAAEALEAIRKAVVEEVKSRARKRAARAPAD
VAAAAAAAALARLLLLAAASRALRLLLLLAAGRLRLLSAVAAGLLELEELLKEFEEEEEEEAAEEEEEEE
EAKKKKEEDKKKKKKKKKKDKEEETKAIKKKKKAAEAVLAAKKAAKEAKAKKELPTTTTDALPEALATTS
LTAAAAASALAAALLEEEGELLYTGGYIRYTRTPKSSEADALAALEALKKIAEEPPDERAKKKKKKAKKK
KASEAKETTDHPPIPPTTAAALLELLEDRKLLLELLVRRRFAAAADLAKVEELTKVEEADEEELVEAEGG
LLEVLGEEEEDDEDEEEELLLPPLEEGEPLLLEELLLEKQTTTPPPRYTTELLLKKLEEEGGGGRGTTAT
IIILILKRRYVVLEEKKTTPTELLVEVVLLLLLPFPKLEDTTETAEEEEALLDKEEGKEDKVVEIREEEY
PFFKKLLEIAEEEGEEELSEEDEVLGEKCPKCGKPLVIKKGRYGKFLGCSNYPECKYTKPLPKPEVTGVK
CPKCGKKLVLRKSKKGKVFYGCSNYPKCKFTEWDKPVKEPCPKCGSPLVEKKTKKGCANKLCGYE
>gnl|CDD|440318 COG0552, FtsY, Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport]
FFERLKEGLSKTRSGLGEKLKSLFSGKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKD
PEELKEALKEELLEILDPVDKPLAIEEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFR
AAAIEQLEVWGERVGVPVIAQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRV
IKKLDPDAPHEVLLVLDATTGQNALSQAKVFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGV
GEGIDDLRPFDAEEFVDALFGEE
>gnl|CDD|440319 COG0553, HepA, Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair]
LLLLLLLLALGALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLL
ALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLV
LLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLE
LELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALAL
LLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANPFEDADLVITSYGLLRRD
IELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLK
AFRERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRR
ELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTD
TLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWW
NPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG
>gnl|CDD|440320 COG0554, GlpK, Glycerol kinase [Energy production and conversion]
MKKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISA
EDIAAIGITNQRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKI
KWILDNVPGARERAEAGELLFGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPR
SMLPEVRPSSEVFGETDPDLFGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRS
KNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQWLRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLG
APYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQ
ADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERERLYAGWKKAVER
TLGWAE
>gnl|CDD|440321 COG0555, CysU, ABC-type sulfate transport system, permease component [Inorganic ion transport and metabolism]
MSRRVLPGFGLTLGLTLLYLSLIVLLPLAALVLKAAGLGWAEFWAVLTSPRVLAALKLSLGTALIAALIN
LVFGLPLAWVLVRYRFPGKRLVDALVDLPFALPTAVAGIALLLLFGPNGWLGQLLAPLGIKVAFTPLGIV
LAQTFVSLPFVVRTVQPVLEELDPELEEAAATLGASRWQTFRRVILPLLLPALLTGFALAFARALGEFGA
VIFIAGNLPMKTEILPLLIYLKLEEGDYAGATAIALVLLLISFLLLLLINLLQRRSRR
>gnl|CDD|440322 COG0556, UvrB, Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair]
PFKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQL
YGEFKEFFPNNAVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVS
CIYGLGSPEEYLKMVLSLRVGEEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIR
IEFFGDEIERISEFDPLTGEVLGELDRVTIYPASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEA
QRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPPTLLDYFPDDFLLFIDESHVTVPQIRGMYNG
DRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEKSGGQVVEQIIRPTGLLDPEI
EVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTLERVEIIRDLR
LGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQR
AIDETNRRREIQEAYNEEHGITPQTIKKSIRDILEGTYEADEETEELVAEADAAKLSKEELEKLIKELEK
EMKEAAKNLEFEEAARLRDEIKELKKE
>gnl|CDD|440323 COG0557, VacB, Exoribonuclease R [Transcription]
YENSRETILAFLKEDAYKPLSKKELAKALGLKDEESREALKRRLRALEREGQLVKTRRGRYRLPEKLDLV
EGRVRGHRDGFGFVIPDDGEEDIFIPPRELNGALHGDRVLVRVTKEDRRGRPEGRVVEILERANTRVVGR
FEKEKGFGFVVPDDKRLLQDIFIPPDDLNGAKDGDLVVVEITRYPERRGPPEGRVVEVLGSPGDPGAEIL
IAIRKHGLPHEFPEEVLAEAEALPDEVPEADLKGRRDLRDLPLVTIDGEDAKDFDDAVSAEKLDNGGWRL
GVHIADVSHYVRPGSALDREARKRGTSVYLPDRVIPMLPERLSNGLCSLNPGEDRLAMSCEMEIDAKGEV
VSYEFYRSVIRSDARLTYEEVQAILDGKDEELREEYADLVPMLEELYELAKILRKAREKRGAIDFDLPET
KIILDEEGKPEDIVPRERNDAHKLIEEFMLLANEAVAEFLEKLKLPFLYRVHEEPDPEKLEALREFLANL
GLKLKGGDEPTPKDLQKLLEQVKGRPEEELLNTLLLRSMKQAVYSPENIGHFGLALEAYTHFTSPIRRYP
DLLVHRALKAYLEGKRSPGLQEYLEEELEEIAEHCSETERRADEAERDVVDLKKAEYMKDRVGEEFEGVI
SGVTSFGLFVELDELGVEGLVHVSSLGDDYYEYDERRQALVGERTGKRYRLGDRVEVRVVRVDLDRRQID
FELVEGGSEAP
>gnl|CDD|440324 COG0558, PgsA, Phosphatidylglycerophosphate synthase [Lipid transport and metabolism]. Phosphatidylglycerophosphate synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis
RPAFQRRLLNIPNQLTLLRILLVPVFALLLLLGGALLLALVLFLLAGLTDALDGYLARRLGQVSRFGAFL
DPVADKLLDAAALLGLVLLGLLPAWLALLILLRELLVSYLRARAAALGVVASYLGKAKTVLQLVAILLLL
LGLPLLGVLLWLAAVLTLLSGIQYLVAARRALRARRR
>gnl|CDD|440325 COG0559, LivH, Branched-chain amino acid ABC-type transport system, permease component [Amino acid transport and metabolism]
MDLFLQQLLNGLSLGSIYALIALGLTLIFGVMGVINFAHGEFVMLGAYVAYTLATLLGLPLWLALLLAVL
VAALLGVLLERLVIRPLRGAPPLALLLATIGLSLVLQGLVLLIFGADPRSFPALLSGSVELGGVSIPAYR
LFIIVVALVLLAALWLFLRRTRLGLAMRAVAQNREAARLMGINVDRVIALTFALGAALAGLAGVLLAPIY
SVSPTMGFLLGLKAFAAVVLGGLGSIPGAVVGGLLLGLAESLGAAYLPSGYKDVVAFVLLILVLLVRPQG
LFGRKERERV
>gnl|CDD|440326 COG0560, SerB, Phosphoserine phosphatase [Amino acid transport and metabolism]. Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis
RKMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESLRFRVALLAGL
PEEELEELAERLFEEVPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDG
RLTGEVVGPIVDGEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAADRER
GWPVLDLLGDR
>gnl|CDD|440327 COG0561, Cof, Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only]
MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALI
YDPDGEVLYERPLDPEDVREILELLREHGLHLQVVVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEV
IAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAADYVTGSNDEDGVAEALEKL
>gnl|CDD|440328 COG0562, Glf, UDP-galactopyranose mutase [Cell wall/membrane/envelope biogenesis]
MMYDYLIVGAGFFGAVFAERLAEELGKKVLVIDKRDHIGGNAYDEYDETGILVHKYGPHIFHTNNKRVWD
YLSRFTEFNPYQHRVLANVDGQLYPLPFNLNTINQLFGKKLTPDEARAFIAEQAEPIKEPRNLEEQALSL
VGRDLYEKFFKGYTEKQWGRDPSELPASIIKRLPVRFNYDNRYFNDTYQGMPKGGYTAMFERMLDHPNIE
VRLNTDFFEVRDEIPADHVVYTGPIDEYFDYRFGRLPYRSLDFEFETLDVEDFQGVAVVNYPDADVPYTR
ITEFKHFTGQQHPKTVITREYPRAYEEGDEPYYPINDEENQALYKKYRALAEKEPNVIFGGRLATYRYYD
MDQVIASALALFDKL
>gnl|CDD|440329 COG0563, Adk, Adenylate kinase or related kinase [Nucleotide transport and metabolism]. Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
MRIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAGTELGKKAKEYMDAGELVPDEIVIGLVKE
RLAQPDCANGFILDGFPRTVAQAEALDELLAELGIKLDAVIELDVDDEELVERLSGRRVCPNCGATYHVK
FNPPKVEGVCDKCGGELVQRADDNEETVRKRLEVYHEQTAPLIDYYRKKGKLVEIDGEGSIEEVTADILA
IL
>gnl|CDD|440330 COG0564, RluA, Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and biogenesis]. Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific is part of the Pathway/BioSystem: 23S rRNA modification
ILYEDEDLLVVNKPAGLVVHPGSGGDDGTLVNALRAHLGELSGVPRPGLVHRLDRDTSGLLLVAKTRKAA
RRLSEQFREREVEKRYLALVEGKPKEDEGTIDAPLGRDPKDRKKMAVVDEDGKPAVTHYRVLERFGGYSL
VEVRLETGRTHQIRVHLAHIGHPIVGDPLYGGDRSNRLLGLDRQALHAYRLGFPHPVTGEPLEFEAPLPE
DFQALLEK
>gnl|CDD|440331 COG0565, TrmJ, tRNA C32,U32 (ribose-2'-O)-methylase TrmJ or a related methyltransferase [Translation, ribosomal structure and biogenesis]. tRNA C32,U32 (ribose-2'-O)-methylase TrmJ or a related methyltransferase is part of the Pathway/BioSystem: tRNA modification
LDNIRVVLVEPQHPGNIGAAARAMKNFGLSDLRLVNPRGWPDEEARAMASGADDVLENARVVDTLEEALA
DCDLVVGTTARPRELRKPVLTPREAAEELLARAAGGKVALVFGRERSGLTNEELALCDALVTIPTNPEYP
SLNLAQAVQVVAYELRKAALEAPPLPPPPEPEPATAEELEGLYEHLEELLDAIGFLDPEKPEKLMRRLRR
LFGRARLTEREVRTLRGILRALERRLK
>gnl|CDD|440332 COG0566, SpoU, tRNA G18 (ribose-2'-O)-methylase SpoU [Translation, ribosomal structure and biogenesis]. tRNA G18 (ribose-2'-O)-methylase SpoU is part of the Pathway/BioSystem: tRNA modification
MTSPSNPRVKDLRKLRDKKYREEEGLFLAEGRHAVEEALKAGREIEELLVTEGALDRLAELLALAKAAGI
PVYEVSREVLDKLSGTETHQGVLAVVRPPEYADLEDLLAEAGEPPLLLVLDGVQDPGNLGAILRSAAAFG
VDGVILPKRRADPYNPKVVRASAGALFHVPVARVTNLADALEELKEAGFWVVGTDLDGEASLYEVDLPGP
VALVLGNEGKGLSRLVLEACDELVRIPMAGGVESLNVAVAAAILLYEAARQRRAK
>gnl|CDD|440333 COG0567, SucA, 2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes [Energy production and conversion]. 2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes is part of the Pathway/BioSystem: TCA cycle
MLMKAMDRSSFLSGANAAYIEELYEQYLEDPDSVDPSWRAFFDGLPDVPGARDFAHSPIREEFRKLAKNG
AGAAASAAADPEAARKQVRVLQLINAYRVRGHLFAKLDPLGLRERPYVPELDPAFYGLTEADLDTVFNTG
SLLGLETATLREIIAALKETYCGSIGVEYMHISDPEEKRWIQERLESTRNRPSFSAEEKKRILEKLTAAE
GFEKFLHTKYVGQKRFSLEGGESLIPALDELIERAGELGVKEIVIGMAHRGRLNVLVNILGKPPRDIFSE
FEGKSAEDVLGSGDVKYHLGFSSDVETPGGKVHLSLAFNPSHLEIVNPVVEGSVRARQDRRGDTDRDKVL
PILIHGDAAFAGQGVVYETLNMSQLRGYRTGGTIHIVINNQIGFTTSPRDARSSTYCTDVAKMVQAPIFH
VNGDDPEAVVFVARLALDYRQKFKKDVVIDLVCYRRHGHNEGDEPAFTQPLMYKKIKKHPTTREIYADKL
VAEGVITAEEADEMVDEYRAALDEGFEVVKEYKPNKADWLEGDWSPYRRLGEDWDDPVDTGVPLEKLKEL
GEKLTTLPEGFKLHPKVEKILEDRRKMAEGEKPLDWGMAEALAYASLLDEGYPVRLSGQDSGRGTFSHRH
AVLHDQKTGETYVPLNHLSEGQARFEVYNSLLSEEAVLGFEYGYALAEPNTLVIWEAQFGDFANGAQVVI
DQFISSGESKWGRLSGLVMLLPHGYEGQGPEHSSARLERFLQLCAEDNMQVCNPTTPAQYFHLLRRQMKR
PFRKPLIVMTPKSLLRHKLAVSSLEELAEGSFQEVIDDTDELDPKKVKRVVLCSGKVYYDLLEERRERGR
DDVAIVRIEQLYPFPEEELAAELAKYPNAKEVVWCQEEPKNMGAWYFIQHRLEEVLPKGQRLRYAGRPAS
ASPATGYMSVHKAEQKALVEEALGI
>gnl|CDD|440334 COG0568, RpoD, DNA-directed RNA polymerase, sigma subunit (sigma70/sigma32) [Transcription]. DNA-directed RNA polymerase, sigma subunit (sigma70/sigma32) is part of the Pathway/BioSystem: RNA polymerase
AYLREIGRVPLLTAEEEVELARRIQAGDEEAKRKLVEANLRLVVSIAKKYQGRGLPLLDLIQEGNLGLMK
AVEKFDPERGFRFSTYATWWIRQAITRAIADQWRTIRLPVHMAETLNKLRRAKRQLLQELGREPTPEEIA
EELGVPEEKVREMLRLAREPVSLDAPVGDDEDSELGDLLEDEEAPSPEEALEEELLREELREALDTLTER
EREILRLRFGLDDGEPHTLEEIGKEFGVSRERVRQIEAKALRKLRHPLRSRKLRDYLD
>gnl|CDD|440335 COG0569, TrkA, Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms]
LLILLLLLVLLFAMGIEGLVLLDALYGLLITLTTVTTLGGGLLDPVTLVAAIFLIGVVIIPLGYTLITFG
DAVLFGGLLEALRRRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVL
VIVGDATDEEVLEEAGIEDADAVIAATGDDEANILACLLAKELGVPRIIARANDPEYADLLERLGADVVI
SPERLAARRIARLLLRPGVLDVLELADGDAEIVEVTVPEGSPLVGKTLKELDLRERYGVTVVAIKRGGEV
IIPSGDTVLEAGDELI
>gnl|CDD|440336 COG0571, Rnc, dsRNA-specific ribonuclease [Transcription]
SEDLEELEERLGYRFKDPELLEQALTHRSYANEHGGLENNERLEFLGDAVLGLVVAEYLYRRFPDAPEGE
LSKLRAALVSEETLAEIARELGLGDYLRLGKGEEKSGGRRRPSILADAFEALIGAIYLDGGLEAARKFVL
RLFEPRLEEIAPGGAGKDYKTALQEWLQARGLPLPEYEVVEEEGPDHAKTFTVEVLVGGKVLGEGTGRSK
KEAEQAAAKAALEKLGKKE
>gnl|CDD|440337 COG0572, Udk, Uridine kinase [Nucleotide transport and metabolism]. Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
AARSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLD
LLNEHLEPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVR
LIRRIVRDGEERGRTAESVIEQYWATVRPGHEQYIEPTKEYADIVIPNGGPLNPVALDLLVARLLS
>gnl|CDD|440338 COG0573, PstC, ABC-type phosphate transport system, permease component [Inorganic ion transport and metabolism]
MSSSRLRPRRRRRRLGDRLFRGLLLLAALLSILILLLIVLFLLIESLPAFQEVGLLEFLTGTEWNPVSSN
GEFGILPLIVGTLLVSLIALLIAVPLGLGIAIFLSEYAPPRLRRILKPAIELLAGIPSVVYGFWGLFVLV
PLLRDLFPWPPSGFSLLTAGIVLAIMILPTITSLSRDALRAVPRSLREAALALGATRWETIRKVVLPAAR
SGIIAAVILGLGRALGETMAVLMVAGNAPQIPFSLFDPGRTLTALIALEFGEAPFGSLHYSALFALGLVL
FVITLLVNLLARLIVRRYREKYG
>gnl|CDD|440339 COG0574, PpsA, Phosphoenolpyruvate synthase/pyruvate phosphate dikinase [Carbohydrate transport and metabolism]. Phosphoenolpyruvate synthase/pyruvate phosphate dikinase is part of the Pathway/BioSystem: Gluconeogenesis
MTKYVYWFAEGGADDVDLVGGKGANLGEMTRLGLPVPPGFTITTEAYRRFLEENGLEEEIRELLADLDVD
DVDALAEASAEIRELILEAPLPEELEEEILAAYAKLEEKFGEDLLVAVRSSATAEDLPDASFAGQMDTVL
NVNGNEQLLEAIKAVFASLFTDRAIAYRRHNGIDHDDVGTAVNVQAMVFGNMSASGVMFTRDPSTGEKDV
VYIEALNGLGEDVVAGIVTPDPYYVDKPTILERTLGSKAIKMVYDGGTVEVPVPPEERNRPSLTDEEYLE
LARIALRLEKHYGDPQDIEWAIDDGKLYILQTRPITVLEGLITKEALLRVDPAQLDQLLHPRFDPKAKEE
GEVLAKGLPASPGAASGKVVFIADEAELARFQEGVILVRDETDPDDVPGMKAAAGIVTERGGMTSHAAIV
ARELGIPAVVGCGDATRVLKDGDEITVDGTTGEVK
>gnl|CDD|440340 COG0575, CdsA, CDP-diglyceride synthetase [Lipid transport and metabolism]. CDP-diglyceride synthetase is part of the Pathway/BioSystem: Phospholipid biosynthesis
LKQRIITALVLAPLVLAALFLGGWAFALLVALIALLGLWEWARLLGLKGIPPRLLGLLAGLLYIGLLFSF
LVLLRALPDGLWLLLLLLLLVWATDTGAYFVGRLFGKHKLAPRISPKKTWEGAIGGLVGAVLVGLLFALL
FGLGLSLWLLLLLGLLLAIASQLGDLFESLLKRDAGVKDSGNLLPGHGGVLDRFDSLLFAAPVVYLLLLL
L
>gnl|CDD|440341 COG0576, GrpE, Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein turnover, chaperones]
MEELEAELAELKDRLLRLQAEFENYRKRTEREREEARKYALEKLAEDLLPVLDNLERALAAAEEDEDVKS
LLEGVEMTLKQLLDVLEKHGVEEIEPVGEPFDPNLHEAVSQVPSPDVEPGTVVEVLQKGYRLGDRVLRPA
MVVVAKG
>gnl|CDD|440342 COG0577, SalY, ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms]
EYLRLALRSLRRNKLRSLLTVLGIAIGIALVIAILALGRGLRRSLLRDLDSLGFDLLTVSRTPGGSRATL
SYEDLREALRALPGVESVAPSSSGSATVRYGGGEPPSVRVLGVDPDYFRVLGIPLLAGRFFTAADDLGAP
PVVVIGEALARRLFGGEDPVGKTIRLNGRPFTVVGVVEAELRALLRRRDPGDDFEVQTLDEILAALYGVL
RTLTLLLGAIAGLALLVACIGIMNLMLASVTERTREIGIRKALGASRRDILRQFLTEALLLALLGGLLGL
LLALLLLRLLAALLGLPVSLDPWVLLLALALSLLVGLLAGLYPARRAARLDPVEALRSE
>gnl|CDD|440343 COG0578, GlpA, Glycerol-3-phosphate dehydrogenase [Energy production and conversion]. Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYLEQGEFRLVREALREREVLLRNAPHLVRPLPFLL
PLYKGGERPAWLIRAGLFLYDLLAGRKGLPRHRRLSRAEALALAPLLRPDGLRGGFEYYDAQVDDARLVL
ELARTAAERGAVVLNYTRVTGLLRDGGRVWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPKAP
RRVRPSKGSHLVVPRLFLPLDDALYIFQNTDGRVVFAIPWEGRTLIGTTDTDYDGDPDEPAATEEEIDYL
LEAANRYFARPLTRDDVVSTYAGVRPLLDDGGKDTSALSRDHVIEVGPAGLLSIAGGKLTTYRKMAEDAV
DAAARLLGLPRRPCWTADLPLPGGDAGFDAFVAALAAAPGLPEALARRLLRRYGTRAEEVLALAAEDPDL
GEPLGPGLPYLEAEVVYAVRHEMARTLEDVLLRRTRLGLLDADAAAAAAPAVAELMAAELGWDDARRAAE
VAAYRALLAAY
>gnl|CDD|440344 COG0579, LhgO, L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]
MMEMYDVVIIGAGIVGLALARELSRYEDLKVLVLEKEDDVAQESSGNNSGVIHAGLYYTPGSLKARLCVE
GNELFYELCRELGIPFKRCGKLVVATGEEEVAFLEKLYERGKANGVPGLEILDREELRELEPLLSDEGVA
ALYSPSTGIVDPGALTRALAENAEANGVELLLNTEVTGIEREGDGWEVTTNGGTIRARFVINAAGLYADR
LAQMAGIGKDFGIFPVKGEYLVLDKPAELVNAKVYPVPDPGAPFLGVHLTRTIDGNLLFGPNAVFVPKKE
DSLLDLFESLRFPNFWPMLAKNLLTKYLESVTSLSKEAFLEALRKYVPELPDEDLIPAFAGIRAQIIKPD
GDFVIEEADDPGSIHVLGIESPGATSALAIAEHVAELLPEKLEEKDWQPKRKMISFGELKEDPAYGEI
>gnl|CDD|440345 COG0580, GlpF, Glycerol uptake facilitator or related aquaporin (Major Intrinsic protein Family) [Carbohydrate transport and metabolism]
SLMKRLLAEFLGTFILVLLGCGVVAVLAGTKGGIGWLGIALAWGLAVLAGVYAFGHISGAHLNPAVTLAL
AVAGRFPWKDVLPYIIAQLLGAFLGAALVYLIYGGHFDATEDGGAKLGVFATSPAIGYSLGAAFLTEIIG
TFVLVFVILGITDKRAAPGGLAPLAIGLLVAAIGLSLGPLTGYAINPARDLGPRLFHALGKGGSDWGYLW
VPIVAPILGAALAALLYRALFG
>gnl|CDD|440346 COG0581, PstA, ABC-type phosphate transport system, permease component [Inorganic ion transport and metabolism]
LALLPLVWILGTVLVKGLPALSWEFLTSSPSPGPEGGGILPAIVGTLLLVLLATLIAVPLGVLAAIYLAE
YARGGRLARLIRFAIDVLAGVPSIVYGLFGYALFVLTLGLGFSLLAGALALALLMLPVVIRTTEEALRLV
PNSLREASYALGATKWQTIRKVVLPAALPGILTGVILAIARAAGETAPLLFTAGVSPFLPLSLFDPFATL
PVHIYNLASSPYPAAQELAWAAALVLLLLVLLLNLLARLLRRRFRKKLK
>gnl|CDD|440347 COG0582, FimB, Integrase/recombinase, includes phage integrase [Replication, recombination and repair, Mobilome: prophages, transposons]
TLTDTAKKKAKPKDKPYKLGDGGGLLLLVGPSGGKRWRYRYRFRGKRKRLALGVYPGVSLALARARRAEA
RALLALGIDPSPARKAAKAAAAAAAANTFEEVAEEWLEEKKPEWKEKTAAQVRRTLEKHIFPVLGDRPIA
EITPPDLLAVLRPIEARGAPETARRVRQRLRQVFRYAVARGLIERNPAADLKGALPKPKVKHHPALTPEE
LPELLRALDAYRGSPVTRLALRLLLLTGVRPGELRGARWSEIDLEAALWTIPAERMKTRRPHIVPLSRQA
LEILKELKPLTGDSEYVFPSRRGPKKPMSENTLNKALRRMGYGRFTPHGFRHTASTLLNEAGFPPDVIER
QLAHKDGNKVRAAYNRADYLEERREMMQWWADYLDALRAGA
>gnl|CDD|440348 COG0583, LysR, DNA-binding transcriptional regulator, LysR family [Transcription]
MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARR
ILAELEEAEAELRALRGGPRGTLRIGAPPSLARYLLPPLLARFRARHPGVRLELREGNSDRLVDALLEGE
LDLAIRLGPPPDPGLVARPLGEERLVLVASPDHPLARRAPLVNSLEALLAAVAAGLGIALLPRFLAADEL
AAGRLVALPLPDPPPPRPLYLVWRRRRHLSPAVRAFLDFLREALAE
>gnl|CDD|440349 COG0584, UgpQ, Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism]
PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLA
ELRQLDAGSGPDFAGERIPTLEEVLELVPGDVGLNIEIKSPPAAEPDLAEAVAALLKRYGLEDRVIVSSF
DPEALRRLRELAPDVPLGLLVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDP
EEMRRLLDLGVDGIITDRPDLLRAVLRE
>gnl|CDD|440350 COG0585, TruD, tRNA(Glu) U13 pseudouridine synthase TruD [Translation, ribosomal structure and biogenesis]. tRNA(Glu) U13 pseudouridine synthase TruD is part of the Pathway/BioSystem: tRNA modification
MERDLGLPYATGTPGIGGRLKASPEDFIVEEILGFEPSGEGEHLLLRIEKRGWNTLDVARRLARALGISR
RRVGYAGLKDRHAVTTQWFSVHLGKDEPDLSALELEGVEVLEVGRHRRKLRRGDLKGNRFTIVLRDVDGD
RERLEARLEEIAAQGVPNYFGEQRFGSDGPNLFVAKALLRGDYEGAGALRRLPRNLRSLFLSAAQSYLFN
RVLSERLERGLWNRPLAGDVLQLAGSGSWFVVEELDLETLQRRLARGDIHPTGPLPGRGTLLADGEAGEI
EREVLAEEGLLLEDLRLPERLGLKGERRALRLRPQDLSWEWDDDTLTLSFSLPKGSYATSVLRELMKVD
>gnl|CDD|440351 COG0586, DedA, Membrane integrity protein DedA, putative transporter, DedA/Tvp38 family [Cell wall/membrane/envelope biogenesis]
LLLDFLDALIAQWGYLGLFLLVFLESVGPPLPGESLLFLAGALAAQGELSLWLVLLAATLGALLGDLIGY
WIGRRLGRRLLRRLGRRFLKPERLDRAEAFFERHGGKAVFLGRFIPGVRTLVPLVAGAARMPYRRFLLYN
ALGALLWVGLLVLLGYLLGENLPLVLEYLGRYGLVVLAIVVVLLLPLVLRLLRKRRRARAA
>gnl|CDD|440352 COG0587, DnaE, DNA polymerase III, alpha subunit [Replication, recombination and repair]
MSPSFVHLHVHSEYSLLDGASRPEELVARAAELGMPALAITDHGNLFGAVRFYKAAKKAGIKPIIGCELY
VAPGSRDDAGYHLVLLAKNREGYRNLCRLLSRAYLEGFYKGKPRIDLEDLAEHSEGLIALSGCLAGEVGQ
ALLAGQYDEAEAALARLKDIFGDRFYLELQRHGLPEDRRVNAALLELARELGLPLVATNDVHYLNPEDAE
AHDVLLCIRTGKTLDDPGRRRFANAERYLKSPEEMAELFADLPEALANTLEIAERCNFSLDLGKYQLPKF
PVPEGETEEEYLRKLAEEGLERRYPEGIPEEYRERLEYELDVIEKMGFPGYFLIVWDFIRWARSNGIPVG
PGRGSAAGSLVAYALGITDVDPIRYDLLFERFLNPERVSMPDIDIDFCHERREEVIQYVYEKYGRDRVAQ
IATFGTMRARAAIRDVGRVLGLPYGEVDRLAKLIPNDPGITLEKALEEEPELRELYDSDPEVRRLLDLAR
KLEGLPRHLSTHAGGVVISDDPLTDLVPLERAAMGGRPVTQFDKDDVEALGLLKFDFLGLRTLTVIRDAL
DLIKENRGIDIDLADIPLDDPKTYELLQRGDTIGVFQLESRGMRSLLKRLKPDCFEDLVALVALYRPGPM
QGGMVPPYIRRKHGREPVEYPHPELEPILKETYGVIVYQEQVMQIAQVLAGFSLGEADLLRRAMGKKKKE
EMAKQREKFVEGAVANGYDEEFAEEIFDQIEKFAGYGFNKSHAAAYALLAYQTAYLKAHYPAEFMAALLN
SQPMGFYKPAQYVQEARRHGIEVLPPDVNESDWDFTVEPGGAIRLGLGAIKGVGEAAAEAIVAAREENGP
FTSLFDFCRRVDLRKLNKRVLEALIKAGAFDSLGPNRRQLLWALEAALDAAQQAQKDKASGQLSLFGGAG
DEEVAEPALPELPEWSEKEKLAAEKEALGLYLSGHPLDLYREELRRLGVTPAADLAELRDGRRVRVAGLV
TSRQRPGTKKGKRMAFVTLEDETGSIEVVVFPEVYERYRRLLLEDRLLLVRGKVQRRDGVVHLIAERIEV
>gnl|CDD|440353 COG0588, GpmA, Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]. Phosphoglycerate mutase (BPG-dependent) is part of the Pathway/BioSystem: Glycolysis
YKLVLLRHGESEWNLENRFTGWTDVDLSEKGRAEAKRAGRLLKEAGFLFDVAYTSVLKRAIRTLWIVLDE
MDRLWIPVEKSWRLNERHYGALQGLNKAETAAKYGEEQVHIWRRSYDVPPPPLDPDDPRHPGNDPRYADL
PPAELPLTESLKDTVARVLPYWEEEIAPALKAGKRVLIAAHGNSLRALVKHLDGISDEEIVGLNIPTGIP
LVYELDDDLKPIKKYYLDD
>gnl|CDD|440354 COG0589, UspA, Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms]
MYKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELEEELREEAEEALEEAAER
LEEAGVEVETVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV
>gnl|CDD|440355 COG0590, TadA, tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]. tRNA(Arg) A34 adenosine deaminase TadA is part of the Pathway/BioSystem: Pyrimidine salvagetRNA modification
MEDDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWR
LSGCTLYVTLEPCPMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAAL
LRDFFAAR
>gnl|CDD|440356 COG0591, PutP, Na+/proline symporter [Amino acid transport and metabolism]
MSTLDLIIIILYLLLLLGIGLYASRRTKSLEDYFLAGRSLGWWVLALSLGATWLSAWTFLGVPGLAYAYG
LSALWYALGYALGALLLALFFAPRLRRLGALTIPEFLEKRFGRGLRLLAAIIILLFLLGYLAAQLVALGK
LLEALFGIPYWLGILIGALIVLLYTVLGGLRAVAWTDVLQGILMLVGLILLLIVALSALGGFGELFAALP
APGLLSLFPGLGFTGWLAFLGLFLAIGLGYFGQPHIVQRFLAAKSEKEARKAALIGGLLYLLFYLLAALI
GLLARALFPDLPLADPDLALPLLILELLPPGLAGLLLAAILAAAMSTADSQLLAASSVFTRDIYKPFIKP
KASDKQLLRVSRLAVLVVGLLALLLALLFPSSILDLVLLAWGGLGAALLPPLLLGLFWKRATKAGALAGM
IAGLVVVLLWKLLGGPLGPFGWLYPILPGLLVSLLVFVVVSLLTKPPSEEVLEEFD
>gnl|CDD|440357 COG0592, DnaN, DNA polymerase III sliding clamp (beta) subunit, PCNA homolog [Replication, recombination and repair]
MKFTISREELLKALQLVSRVVPSRSTLPILSNILLEAEDGGLTLTATDLEISIRTSIPAEVEEEGSITVP
AKKLLDIVRKLPDGEVTLEVDGNKLTIKSGRSRFTLPTLPAEDFPELPEIEEENSFTLPADELKELIEKT
AFAASTDETRPYLTGVLLEIEGDKLRLVATDGHRLAVREIPLEEEAEEEFSVIIPRKTLNELAKLLDDSD
EEVEIALSENQIRFEFGNTTLTSRLIDGKFPDYERVIPKEFDTKVTVDRKELLEALKRVSLLANEKNRGV
RLSFSDGELTLSANNPEQGEAEEELPVEYEGEDLEIGFNAKYLLDALKAIDSEEVRLEFTDPNSPALITP
VDDEDYLYLVMPMRL
>gnl|CDD|440358 COG0593, DnaA, Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair]
LNPRYTFDNFVVGPSNRLAHAAALAVAEWPGKAYNPLFLYGGVGLGKTHLLHAIGNEALENNPGARVVYL
TAEEFTNDFINAIRNNTIEEFKEKYRSVDVLLIDDIQFLAGKEATQEEFFHTFNALREAGKQIVLTSDRP
PKELPGLEERLRSRLEWGLVVDIQPPDLETRIAILRKKAADRGLELPDEVLEYLARRIERNVRELEGALN
RLDAYALLTGRPITLELAREVLKDLLRAQKKEITIEDIQKAVAEYFGVSVADLLSKSRTREIARPRQIAM
YLARELTDLSLPEIGRAFGGRDH
>gnl|CDD|440359 COG0594, RnpA, RNase P protein component [Translation, ribosomal structure and biogenesis]
LKKRKDFQRVFRKGKRVSSRYFVLYYLPNDLDPPRLGFSVSKKVGNAVVRNRIKRRLREAFRLNKPELPP
GYDIVVIARPGAAELDFAELEKELEKLLK
>gnl|CDD|440360 COG0595, RnjA, mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis]
LKKDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLT
HGHEDHIGALPYLLKELNVPVYGTPLTLALLEAKLKEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHS
IPDSLGLAIRTPAGTIVHTGDFKFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVG
PTLEEIFAKAKGRIIVATFASNVHRIQQIIDAAKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDL
KEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIKPGDTVIFSSSPIPGNEKAVARVINELYRLG
AEVIYDSDAKVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKLAEEMGVPEENIFIAENGDVV
ELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVGGPDIVSRGFV
YVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV
>gnl|CDD|440361 COG0596, MenH, 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]. 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
MSTPRFVTVDGVRLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGY
TLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEA
LAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAF
AAALRDFLARL
>gnl|CDD|440362 COG0597, LspA, Lipoprotein signal peptidase [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport]
LLFLLLALLVLLLDQLTKLWVVANLALGESIPVIGGFFNLTYVENTGAAFGLLAGAGWLLIILALVVLVG
LLYYLRRLKKRSKLLALALGLILGGALGNLIDRLFYGYVVDFIDFHIGGWHWPIFNVADIAITIGVILLL
LDSLFGKKKKK
>gnl|CDD|440363 COG0598, CorA, Mg2+ and Co2+ transporter CorA [Inorganic ion transport and metabolism]
RELDALEELLDPEGFVWIDLDGPTDEELEWLAEEFGLHPLALEDALDIEQRPKLEEYDDYLFIVLRTLNY
NEEEEELETGPLSIFLGPNFLITVRERPLDAFDDVRERLERGPGLLPRGPDYLLYALLDAIVDRYFPVLE
ELEDELDELEDELFESPDNELLRRLYRLRRELVRLRRALAPLREVLSRLLRGESPLISEEDREYLRDVYD
HLERLLEMVDSLRERLSGLLDAYLSLISNRQNEIMKVLTIIAAIFLPPTFIAGIYGMNFEGMPELDWPYG
YPIVLGLMLLIAVLLYLYFKRKGWL
>gnl|CDD|440364 COG0599, YurZ, Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone decarboxylase family [General function prediction only]
EEVLKEVEEYVPRALEALAEFAPEFAEAFEALFGDVWARGALDPKTRELITLAALAALGCEPCLKAHVRA
ALNAGATREEIAEALLVAAVYAGFPAALNALRAALEVLEELGAA
>gnl|CDD|440365 COG0600, TauC, ABC-type nitrate/sulfonate/bicarbonate transport system, permease component [Inorganic ion transport and metabolism]
MTTSTRRRLRRLLLPLLSLALLLALWELAARLGLVPPFLLPSPSAVLAALVELLASGELWEHLLASLLRV
LLGFALAALLGVPLGLLLGLSRLLRRLLDPLLVFLRPIPPLALAPLLILWFGIGEASKIFVIFLGAFFPI
LLNTAAGVRSVDPELLELARSLGASRWQILRKVVLPAALPYIFTGLRIALGLAWIGLVVAELLGASSGLG
YLILDARQLLDTDLVFAAILVIGLLGLLLDLLLRLLERRLLRWR
>gnl|CDD|440366 COG0601, DppB, ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid transport and metabolism, Inorganic ion transport and metabolism]
MLRYILRRLLQAIPVLLGVSTLVFLLLRLLPGDPAAALLGPRATPEAIAALRAELGLDQPLLVQYLDWLG
GLLRGDLGTSFVYGRPVSDLIAERLPVTLELALLALLLALLIGIPLGILAALRRGSWLDRLITVLALLGI
SIPSFWLGLLLILLFAVKLGWLPVSGRVSPWEDFLDALRHLILPALTLALGSLAGIARLTRSSMLEVLGQ
DYVRTARAKGLSERRVLLRHALRNALIPVVTVLGLQLGGLLGGAVVVETVFSWPGLGRLLVDAILNRDYP
VVQGIVLLIAVLVVLVNLLVDLLYALLDPRIRLG
>gnl|CDD|440367 COG0602, QueE, Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]. Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification
TLPIVEIFYSIQGEGALAGRPAVFVRLAGCNLRCSWCDTKYAWDGEGGKRMSAEEILEEVAALGARHVVI
TGGEPLLQDDLAELLEALKDAGYEVALETNGTLPIPAGIDWVTVSPKLPSSGEEEDNRENLEVLRRADEL
KFVVADETDLEEAEELLARLDFRCPVYLQPVWGNKLEENTELLAEWCLAHPNVRLSPQLHKLLGV
>gnl|CDD|440368 COG0603, QueC, 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]. 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification
MMKKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGQRHRKELEAARRIAKALGVGEHKVIDLDFLGEI
GGSALTDDSIEVPEGHYAEEGIPSTYVPGRNLIFLSIAAAYAEALGAEDIFIGVNATDYSGYPDCRPEFI
EAFNAALNLGTKRPVRIHTPLMHLSKAEIVKLGLELGVPYELTWSCYNGGGRACGRCDSCRLRLEAFAEA
GIPDPTEYAARPE
>gnl|CDD|440369 COG0604, Qor, NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only]
MKAIVITEFGGPEVLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGVVV
AVGEGVTGFKVGDRVAGLGRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPG
ETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRALGADHVIDYREEDFAERVRALTGGRGVD
VVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFARDPAERRAALAELA
RLLAAGKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTVD
>gnl|CDD|440370 COG0605, SodA, Superoxide dismutase [Inorganic ion transport and metabolism]
ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEIIKKLSEELKRALRNNA
GGHWNHTLFWENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVS
TPNQDNPLMAGGTPLLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR
>gnl|CDD|440371 COG0606, YifB, Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones]
MLARVYSVALLGIEAPLVEVEVDISNGLPGFTIVGLPDTAVKESRERVRAALKNSGFEFPAKRITVNLAP
ADLPKEGSRFDLPIALGILAASGQIPAEALEDYVFLGELSLDGSLRPVRGVLPAALAAREAGIRRLIVPA
ANAAEAALVPGIEVYGASSLLEVVAFLRGEQPLPPAEPDAPPAEPPYEPDLADVKGQEQAKRALEIAAAG
GHNLLMIGPPGSGKTMLARRLPGILPPLTEEEALEVTAIHSVAGLLPPDGGLIRRRPFRAPHHTASAAAL
VGGGSIPRPGEISLAHNGVLFLDELPEFSRRVLEALRQPLEDGEVTISRANGSVTYPARFQLVAAMNPCP
CGYLGDPDRECRCSPRQIRRYLSRLSGPLLDRIDLHVEVPPVPYEELSSAPPGESSAEVRERVAAARERQ
LERFGGTGIRLNAQLPGRELRKYCRLDAEARALLERALERLGLSARAYDRILRVARTIADLAGSERIERE
HLAEALQYRRLD
>gnl|CDD|440372 COG0607, PspE, Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]. Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle
ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRS
AQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKGK
>gnl|CDD|440373 COG0608, RecJ, ssDNA-specific exonuclease RecJ, DHH superfamily, may be involved in archaeal DNA replication intiation [Replication, recombination and repair]
MSTGRRWILKPPDPELVEALAKELGLSPLLARLLANRGITTPEEAEAFLDPSLKDLHDPFLLKDMDKAVE
RLAEAIENGEKILIYGDYDVDGATSTALLVRFLRALGANVDYYIPNRFEEGYGLNPEAVERAAEQGVDLI
ITVDCGISSHEEVAYAKELGIDVIVTDHHLPGEELPPADAIVNPKRPDCDYPFKELAGVGVAFKLAQALR
RELRERPEPDLAELLDLVALGTVADVVPLTGENRILVKQGLKRLRATKRPGLRALLEVAGLDPKEITAED
IGFALGPRINAAGRLGDASLGVELLLTDDEEEARELAEELDELNRERKEIEAEITEEALAQIEELPDLED
PKVLVLYDEDWHPGVIGIVASRLKEKYHRPTIVLAIDEDGIAKGSARSIPGFDLYDALDACSDLLLKFGG
HAMAAGLTLKEENLEAFRERFNEVVAEQLAEEDLEPVLEIDGELPLSELTLELAEELEQLEPFGQGNPEP
VFLGRNVRVVSQRIVGKDGNHLKLTLRDGGRRLDAIAFNAGDKLEELPNAGKRVDIAYTLDI
>gnl|CDD|440374 COG0609, FepD, ABC-type Fe3+-siderophore transport system, permease component [Inorganic ion transport and metabolism]
SLSLGAVPISLSDVLRALLGPDGDPTADLIVWDLRLPRVLLALLVGAALAVAGALMQGLTRNPLADPGIL
GVSSGAALGAVLAIVLGGGLSALGLPLAAFLGALLAALLVYLLARRGGGLSPLRLVLAGVAVSALFSALT
SLLLLLADPEQLRSIVFWLMGSLAGASWDDVLLLLPVLLIGLLLALLLARALNALALGDETARSLGVNVE
RLRLLLLLLAALLTGAAVAVAGPIGFVGLVVPHIARLLVGPDHRRLLPASALLGALLLLLADTLARTILA
PAELPVGIVTALIGAPFFLYLLRRRR
>gnl|CDD|440375 COG0610, COG0610, Type I site-specific restriction-modification system, R (restriction) subunit and related helicases .. [Defense mechanisms]
MSKFSEAALEQAIIELLQELGYEYLSGPDIAPEDESEVLLEDNLRAALERLNPGLSDDEIERALRELTKP
ESNGLLEANKGFYDLLRNGVKVEYDGEEKTKTVRLIDFKNPENNDFLVVNQFTVSGGNYKRRPDVVLFVN
GLPLVVIELKNPLTQVTIKEAFNQIQRYRREIPGLFAYNQLFVISDGVEARYGTNTAPFEFFLPWKDGDG
NDLNPDGITDLDYLIEGLLSKERLLDIIRNFIVFDEDEGGLIKIVARYHQYFAVRKAVERVKEAEGDGKG
GVIWHTQGSGKSLTMVFLAQKLARLPDLDNPTVVVVTDRKDLDDQLFDTFKAFGRESVVQAESRADLREL
LESDSGGIIVTTIQKFPEALDEIKYPELSDRKNIIVIVDEAHRSQYGGLAKNMRDALPNASFFGFTGTPI
FKEDRTTLEVFGDYIHTYTITQAIEDGATLPLLYEYRLAKLKLDKEKIDEEFDELTEGLDDEEKEKLKAK
WALLEEVLGAPERIEQIAEDIVEHFEERTRPGKGKAMVVTSSREAAVRYYEAFDKLRPEWGYKPLKIAVV
FSGSANDDPEELKEHGNKEYEKDLAKRFKDPDDPLKLLIVVDMLLTGFDAPSLHTLYVDKPLKGHNLMQA
ISRVNRVFPGKPYGLIVDYRGIFENLKKALALYSEEDGKEDVLTDPEEALEELKEALDELRALFPEGVDF
SAFDPTEKLEALDEAVERFLGDEEARKEFKKLFKELSRLYNLLSPDDEFGDLELEKYRDDVSFYLALRAK
LRKLGEKLDLKEYEEKIRQLLDEAIDLERKEIKPRIKQNPVQYRKFSELLEEIIEEYNNGALDADEVLEE
LEELAKEVKEEEERAEEEGLNEEELAFYDALAENLGDEKLKELAKELDDLLKKNVTVDWRKRESVRAKLR
DAIKRLLRKYGYPKQDEAVEEVYEQA
>gnl|CDD|440376 COG0611, ThiL, Thiamine monophosphate kinase [Coenzyme transport and metabolism]. Thiamine monophosphate kinase is part of the Pathway/BioSystem: Thiamine biosynthesis
MGEFGLIERLFKRLALRGPDVLLGIGDDAAVLDPPGGRLVVTTDMLVEGVHFPLDWMSPEDLGWKAVAVN
LSDLAAMGARPLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPELTISVTAIGEVPG
GRPLLRSGARPGDLVYVTGTLGDAAAGLALLLRGLRVPLEAREYLLERHLRPEPRLALGRALAEAGLATA
MIDISDGLAADLGHIAEASGVGAEIDLDALPLSPALREAALGLDPLELALTGGEDYELLFTVPPEALEAL
EAAALGVPLTVIGRVTEGEGVTLDDADGRPIPLEARGWDHF
>gnl|CDD|440377 COG0612, PqqL, Predicted Zn-dependent peptidase, M16 family [General function prediction only]
LAPAAGAAPAAAPDVEEFTLPNGLRVILVPDPEAPVVSVRLWVRVGSRDEPPGKTGLAHFLEHMLFKGTK
KRSAGEIAEELEALGGSLNAFTSFDYTVYYLSVLSEDLELALELLADRLLNPTFDEEELERERGVVLEEI
RRYEDDPDGLAFEALLAALYGDHPYGRPIIGTEESIEAITREDLRAFYKRYYRPNNAVLVVVGDVDPEEV
LALVEKYFGDLPAGPAPPRPDPAEPPQTGPRRVVVDDPDAEQAHILLGYPGPARDDPDYYALDVLNEILG
GGFSSRLFQELREKKGLAYSVGSSFSPYRDAGLFTIYAGTAPDKLEEALAAILEELERLAKEGVTEEELE
RAKNQLLGSLALSLESNSGLASQLGRYELYGGDLDYLEEYLERIEAVTAEDVQAVARKYLDPDNLVVVVV
GPKKKAE
>gnl|CDD|440378 COG0613, YciV, 5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and metabolism]
WMKIDLHVHTTASDGSLSPEELVARAKAAGLDVLAITDHDTVAGYEEAAEAAKELGLLVIPGVEISTRWE
GREVHILGYGIDPEDPALEALLGIPVEKAEREWLSLEEAIDLIREAGGVAVLAHPFRYKRGRWLDDLLEE
LADAGLDGIEVYNGRHSPEDNERAAELAEEYGLLATGGSDAHGPEKPL
>gnl|CDD|440379 COG0614, FepB, ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism]
MRIVSLSPSATELLLALGAGDRLVGVSDWGYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSG
NDEEDYEQLEKIGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPT
VLYEIWSGDPLYTAGGGSFIGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEE
ALEALLADPGWQSLPAVKNGRVYVVPGDLLSRPGPRLLLALEDLAKALHPELFA
>gnl|CDD|440380 COG0615, TagD, Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]. Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILG
EEWDKFEDIEEIKPDVIVLGDDWKGDFDFLKEELEKRGIGCEVVYLPRTEGISSTKIKKRI
>gnl|CDD|440381 COG0616, SppA, Periplasmic serine protease, ClpP class [Posttranslational modification, protein turnover, chaperones]
AKARPPKVKPSIAVIDLEGTIVDGGGPPSGEIGLEDILAALRKAAEDPDVKAVVLRINSPGGSVAASEEI
RDALRRLRAKGKPVVASMGDVAASGGYYIASAADKIYANPTTITGSIGVIAQGPNFKGLLEKLGVEVEVV
TAGEYKDALSPFRPLSEEEREQLQALLDDIYDQFVEDVAEGRGLSLEEVREIADGRVWTGEQALELGLVD
ELGTL
>gnl|CDD|440382 COG0617, PcnB, tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and biogenesis]. tRNA nucleotidyltransferase/poly(A) polymerase is part of the Pathway/BioSystem: tRNA modification
RLSPNALKVLEALEEAGFEAYLVGGAVRDLLLGRPPKDIDIVTVATPEEVAALFRKALRTVPVGRDFGTV
TVVFGGEKIEVATARTERYYGDGRRPFVEFGDTLEEDLARRDFTINALAYDLNDGELIDPFGGLADLEAR
VIRTVGDPEERFREDPLRILRAVRFAARLGFTIEPETLAAIREMAGLLDRLSAERVWDELLKLLLSPHPS
RGLELLRETGLLEVLALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVREL
VELHLRFHGLGELRDSAVRRLLERGPEALEDLLLLRENGLEYPELQERLAELLEAAWRRFQPPVDGEDLM
ALGLKPGPEIGEILRALREAVLDGGIPNRREEALLRWLRRL
>gnl|CDD|440383 COG0618, NrnA, nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and metabolism, Signal transduction mechanisms]
EELAELLKKADRILILTHVNPDGDALGSALALALLLRALGKEVTIVYPGEIPHELAFLPGADEIVRLEDV
DLEYDLVIVVDTSSPDRIGDLAELLEKAKPVIVIDHHPSNDDFGDFNDVDPDAGATSEIIYELLKELGIE
IDPEIATALYTGIVTDTGSFRYSNTTPRDFRAAAELLEKGADLDLIARILYPSLSLEQLKLLGRALENLE
VLEDGKVAYSYLTKEDLEEFGATPDDTEGLVDYLLSIEGVEVAVVFGEVEDGEIKVSLRSKGRVDVGEIA
REFGGGGHARAAGATIPGLDLEEVVEKLLEAL
>gnl|CDD|440384 COG0619, EcfT, ECF-type transporter transmembrane protein EcfT [Coenzyme transport and metabolism]
MSTLDQYAPGDSFLHRLDPRTKLLLLLLLIIAAFLLPSPLVLLVLLLLALLLLLLAGIPLRRLLKRLLPL
LPFLLLLLLLLPLFVPGTVLFSLGPLTITREGLLLALLLALRLLALVLAALLLLLTTPPSDLLAALRRLG
VPPELALMLLLALRFIPVLLEEARRIREAQRARGGDFGKLRRRLRSLGPLLGPLLVRSLRRAERLALAME
ARGFGGGGKRTSLRELRFSRRDYLALALLLALLAALLLL
>gnl|CDD|440385 COG0620, MetE, Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]. Methionine synthase II (cobalamin-independent) is part of the Pathway/BioSystem: Methionine biosynthesis
LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFP
ERLDGYAFARNGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVR
DYKDREELLDDLAPAYREELKALEAAGARWIQIDEPALAEDLPDEYLDWAVEAYNRAAAGVPDTKIHLHT
CYGGYEDILEALAALPVDGIHLEFVRSRAGLLEPLKELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEAL
KYVPPERLWVSPDCGLKHRPVDLTREEAWAKLRNMVAFAREVRGE
>gnl|CDD|440386 COG0621, MiaB, tRNA A37 methylthiotransferase MiaB [Translation, ribosomal structure and biogenesis]. tRNA A37 methylthiotransferase MiaB is part of the Pathway/BioSystem: tRNA modification
MKKVYIVTLGCQMNQVDSERMAGLLEAAGYELVDDPEEADVVVVNTCSVREKAEEKSRQTIGRLAELKRK
NPDAKIVVTGCLAQREGEELLEEIPEVDLVVGPQDKHRLPELLEEALAGEKVVDISSEETFDDLPVPRRT
GRTRAFVKIQEGCNNFCTFCIIPYTRGRERSRPPEDILAEARRLAAQGVKEIVLTGQNVNSYGKDLYGKT
DLADLLRALAEIEGIERIRLSSSHPKDFTDELIEAMAESPKVCPHLHLPLQSGSDRVLKRMNRRYTREEY
LELVEKIREAIPDIAIRTDIIVGFPGETEEDFEETLDFVEEVRFDRLHVFPYSPRPGTPAAKMPDQVPEE
VKKERLARLMELQEEISAERNQRLVGKTVEVLVEGPSKKDDGQLIGRTENYALVVFPGDELLPGDFVDVK
ITEADEYDLIGELVE
>gnl|CDD|440387 COG0622, YfcE, Predicted phosphodiesterase, calcineurin family [General function prediction only]
KIAVISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGPDPPEVLDLLRELPIVAVRGNHDGAVLRGL
RSLPETLRLELEGVRILLVHGSPNEYLLPDTPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPG
SVGQPRDGDPASYAILDIDDGEWSVEFVRVPYDIEAAIREAGL
>gnl|CDD|440388 COG0623, FabI, Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]. Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis
GLLKGKRGLITGVANDRSIAWGIAKALHEEGAELAFTYQGEALKKRVEPLAEELGSALVLPCDVTDDEQI
DALFDEIKEKWGKLDFLVHSIAFAPKEELGGRFLDTSREGFLLAMDISAYSLVALAKAAEPLMNEGGSIV
TLTYLGAERVVPNYNVMGVAKAALEASVRYLAADLGPKGIRVNAISAGPIKTLAASGIPGFDKLLDYAEE
RAPLGRNVTIEEVGNAAAFLLSDLASGITGEIIYVDGGYHIMGM
>gnl|CDD|440389 COG0624, ArgE, Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]. Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis
AAVLAAIDAHLDEALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPPGRPNLVARRPGDGG
GPTLLLYGHLDVVPPGDLELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTL
LFTGDEEVGSPGARALVEELAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNA
IEALARALAALRDLEFDGRADPLFGRTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRA
LLAAAAPGVEVEVEVLGDGRPPFETPPDSPLVAAARAAIREVTGKEPVLSGVGGGTDARFFAEALGIPTV
VFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLAG
>gnl|CDD|440390 COG0625, GstA, Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]
MMKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAIL
EYLAERYPEPPLLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEA
RLAGGPYLAGDRFSIADIALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRALAAAEPDLA
>gnl|CDD|440391 COG0626, MetC, Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]. Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis
MGPATRAVHAGRDPDPQTGAVSPPIYLTSTFVFPSAEALAARFAGEEGGYIYSRYGNPTRRALEEALAAL
EGGEAALAFASGMAAISAVLLALLKAGDHVVASDDLYGGTRRLLDKVLARFGIEVTFVDPTDLAAVEAAI
RPNTKLVFLETPSNPTLEVVDIAAIAAIAHAAGALLVVDNTFATPLLQRPLELGADIVVHSATKYLGGHS
DVLGGAVVGRDEELAERLRFLQNALGAVLSPFDAWLLLRGLKTLALRMERHCENALAVAEWLEAHPAVAR
VYYPGLPSHPGHELAKRQMSGFGGMLSFELKGGREAARRFLDALKLFTLAVSLGGVESLITHPATMTHRS
LPPEERAALGITDGLVRLSVGLEDVDDLIADLEQALAAL
>gnl|CDD|440392 COG0627, FrmB, S-formylglutathione hydrolase FrmB [Defense mechanisms]
GGRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD
GGQASFYVDWTQGPAGHYRWETYLTEELPPLIEANFPVSADRERRAIAGLSMGGHGALTLALRHPDLFRA
VAAFSGILDPSQPPWGEKAFDAYFGPPDRAAWAANDPLALAEKLRAGLPLYIDCGTADPFFLEANRQLHA
ALRAAGIPHTYRERPGGHSWYYWASFLEDHLPFLARALG
>gnl|CDD|440393 COG0628, PerM, Predicted PurR-regulated permease PerM [General function prediction only]
MSRWRRLLLLLLLLLLLLLLLYLLRPFLLPFLLALVLAYLLNPLVRRLERRGLPRGLAALLVLLLLLLLL
VLLLLLLVPLLVSQLSELIENLPSYLDSLQEWLASLPEYLEELDPEQLQELLSSLLSSLSSLLGSLLSGL
LSLLSSLGGLLLNLVLVLILLFFLLLDGDRLRRWLLRLLPLRYRERVRRLLREIDRTLGGYLRGQLLVAL
IVGVLTGIGLLILGVPYALLLGVLAGLLNFIPYVGPILGAIPAALVALLQGPGLALLVLIVYLVVQQLEG
NVLRPKLVGRSVGLHPLVVLLALLGGGALFGILGLFLAPPLAAVLKVLLRELLERYLLSDELEEPE
>gnl|CDD|440394 COG0629, Ssb, Single-stranded DNA-binding protein [Replication, recombination and repair]
MNKVTLVGRLGKDPELRYTPSGTAVANFRLAVNRRYKDQDGEWKDETDWHRVVAWGKLAENAAEYLKKGD
KVYVEGRLRTRSWEDKDGQKRYTTEVVADEIQFLGSRPSGGGGGDD
>gnl|CDD|440395 COG0630, VirB11, Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport]
DLDLLAPATTDPAPAPTALARLREELDRKLLEELREEEVPEANFREPVLVVPEFLLGYEEEEVSYVVEYP
YLVVIDDEEIEEYLYYLVEEPPDSEEEEELLEEEERLLEELLLLEEEDALEDLEVLLLRELDSLLKDYKI
KVSEERLEKLLYYLLRDFVGYGKLDPLMRDPNIEDISCNGVGIPVYVYHRDYERIPTNIVFESEEELDNF
VVKLAQRSGKHISVARPIVDATLPDGSRIALTLGPEVSRRGSSFTIRKFREVPLTPIDLIEWGTLSPELA
AYLWLLLENGKSVLVAGGTASGKTTLLNALLSFIPPDAKIVTIEDTRELNLPHENWISLVTRESFGGEEG
DVTMFDLLKAALRQRPDYIVVGEVRGEEAYTLFQAMATGHGVLSTFHADSVESAINRLTSPPINVPRTLL
QALDLVVFQKRVRVGGKRVRRVTSIVEIVGYDPETGEIRTNP
>gnl|CDD|440396 COG0631, PTC1, Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms]
LEVAAASDVGRVRENNEDAFLVALDPGGGLFVVADGMGGHAAGEVASRLAVETLAELFQEALAPDPEDLE
EALREAIRAANRAILELAQEDPELAGMGTTLVAALIAGGRLYIAHVGDSRAYLLRDGELEQLTRDHSLVQ
ELVDAGRITPEEARTHPQRNVLTRALGTDDDVEPDISPLELEPGDRLLLCSDGLTDMVSDEEIAEILASA
GDPQEAAEALIELALEAGGPDNITVVLVRVEDADAES
>gnl|CDD|440397 COG0632, RuvA, Holliday junction resolvasome RuvABC DNA-binding subunit [Replication, recombination and repair]
MIAYLRGTLVEKGPDYVVIDVGGVGYEVFVPLSTLSALPEVGEEVKLYTHLVVREDALTLYGFATEEERE
LFRLLISVSGVGPKLALAILSGLSPEELARAIASGDVKALTKVPGIGKKTAERIILELKDKLGKLALAAG
AAAAAAAAASSALEEAVSALVALGYSPKEAEKAVAKVLKEGPDASVEELIRAALK
>gnl|CDD|440398 COG0633, Fdx, Ferredoxin [Energy production and conversion]
MPKVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGS
RLACQARPTSDLVVELP
>gnl|CDD|440399 COG0634, HptA, Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]. Hypoxanthine-guanine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage
MHDDIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYG
GGTESSGEVRILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPA
DYVGFEIPDEFVVGYGLDYAEYYRNLPYIYALKPEV
>gnl|CDD|440400 COG0635, HemN, Coproporphyrinogen-III oxidase HemN (oxygen-independent) or related Fe-S oxidoreductase [Coenzyme transport and metabolism]. Coproporphyrinogen-III oxidase HemN (oxygen-independent) or related Fe-S oxidoreductase is part of the Pathway/BioSystem: Heme biosynthesis
MSITSYPTGEAAALAALAPARPLSLYIHIPFCRSKCPYCDFNSHTTREEPVDRYLDALLKEIELYAALLG
GRPVSTIFFGGGTPSLLSPEQLERLLDALREHFPLAPDAEITLEANPGTVTAEKLAALREAGVNRLSLGV
QSFDDEVLKALGRIHTAEEALAAVELAREAGFDNINLDLIYGLPGQTLESWEETLEKALALGPDHISLYS
LTHEPGTPFAQRVRRGKLALPDDDEKADMYELAIELLAAAGYEQYEISNFARPGGESRHNLGYWTGGDYL
GLGAGAHSYLGGVRYQNVKDLEAYLAAIEAGGLPVARGEVLSEEDRLREFVILGLRLNEGVDLARFEERF
GLDLREYFAERLAELEEDGLLEIDGGRLRLTPKGRLLLNNIAAAFLDALE
>gnl|CDD|440401 COG0636, AtpE, FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy production and conversion]. FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K is part of the Pathway/BioSystem: FoF1-type ATP synthase
MEAAASAIGAGLAIGLAAIGAGIGIGLAGGKALEAIARQPEAAGKLQTTMFIGAALIEALAIYALVIALI
LLFAN
>gnl|CDD|440402 COG0637, YcjU, Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism]
MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAA
RKEELYRELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVAR
GKPDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL
>gnl|CDD|440403 COG0638, PRE1, 20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, chaperones]
MQPSQQSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIF
KIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGVRPFGVALLIG
GVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSASGD
GIDVAVITEDGFRELSEEE
>gnl|CDD|440404 COG0639, ApaH, Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal transduction mechanisms]
SLDLLRLDLLLLLLRRLLLLLHDLHLLAHAGHAGQWPLWDALTALLEAEDVERLLNWLRLLPLLYGMYYN
KPDRWSDDLQGLDRLRFIINAFTRMRFCTPDGRLDFKCKEPPETAPPGLKPWFDVPGRRTADYTIVFGHW
AALEGLGTPPNIYALDTGCVWGGKLTALRWEDKQRFQVPCPQ
>gnl|CDD|440405 COG0640, ArsR, DNA-binding transcriptional regulator, ArsR family [Transcription]
MSETKELEELAELFKALADPTRLRILRLLAEGELCVGELAEALGLSQSTVSHHLKVLREAGLVTSRREGR
WVYYRLADEALAELLEWLLELL
>gnl|CDD|440406 COG0641, AslB, Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones]
KALVLKPTSRCNLRCSYCYYSEGDEGSRRRMSEETAEKAIDFLIESSGPGKELTITFFGGEPLLNFDFIK
EIVEYARKYAKKGKKIRFSIQTNGTLLDDEWIDFLKENGFSVGISLDGPKEIHDRNRVTKNGKGSFDRVM
RNIKLLKEHGVEVNIRCTVTRENLDDPEELYDFLKELGFRSIQFNPVVEEGEADYSLTPEDYGEFLIELF
DEWLERDGGKIFVREFDILLAGLLPPCSSPCVGAGGNYLVVDPDGDIYPCDEFVGDPEFRLGNVFDGSLA
ELLDSPKLRAFGREKNVLLDEECRSCPYLPLCGGGCPANRYAETGDGFKPYSYYCELYKKLFEHALRLE
>gnl|CDD|440407 COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms]
LLLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLL
LLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELD
EEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDL
PDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFF
RTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPLA
>gnl|CDD|440408 COG0643, CheA, Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms]
MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDL
LDALRNGELALTPELIDLLLEALDALRALLDALEAGGEPPADISALLARLDASEEAIEEVVADEVEISPP
APAALEPAPAAAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDESLRE
LEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGD
PLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITA
EEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTL
AIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGREVIRLRGELLPLVRLGELLGLPGAEPEGERG
PVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVRSARARARA
AAA
>gnl|CDD|440409 COG0644, FixC, Dehydrogenase (flavoprotein) [Energy production and conversion]
AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPLERPVRGARFYSPGGKS
VELPPGRGGGYVVDRARFDRWLAEQAEEAGAEVRTGTRVTDVLRDDGRVVVRTGDGEEIRADYVVDADGA
RSLLARKLGLKRRSDEPQDYALAIKEHWELPPLEGVDPGAVEFFFGEGAPGGYGWVFPLGDGRVSVGIPL
GGPRPRLVGDGVLLVGDAAGFVDPLTGEGIHLAMKSGRLAAEAIAEALEGGDFSAEALAEYERRLRELLK
A
>gnl|CDD|440410 COG0645, COG0645, Predicted kinase, contains AAA domain [General function prediction only]
LILVCGLPGSGKSTLARALAERLGAVRLRSDVVRKRLFGAGLAPLERSPEATARTYARLLALARELLAAG
RSVILDATFLRRAQREAFRALAEEAGAPFVLIWLDAPEEVLRERLEARNAEGGDSDATWEVLERQLAFEE
PLTEDEGFLLVVDTSGLEEALAAL
>gnl|CDD|440411 COG0646, MetH1, Methionine synthase I (cobalamin-dependent), methyltransferase domain [Amino acid transport and metabolism]. Methionine synthase I (cobalamin-dependent), methyltransferase domain is part of the Pathway/BioSystem: Methionine biosynthesis
MRRAALLELLKERILILDGAMGTMLQAYGLTEGDFRGEKGCNELLNLTRPDVIREIHRAYLEAGADIIET
NTFGANRIKLADYGLEDRVYEINRAAARLAREAADEFSDRPRFVAGSIGPTGKLLSPLGNITFDELVEAY
REQAEGLIEGGVDLLLIETIFDTLEAKAAIFAAREAFEELGRDLPVMVSGTFDASGRTLSGQTPEAFATS
LEHLGPDAIGLNCALGPDEMRPHVEELSEVADTPVSAYPNAGLPNLVGGRTVYDETPEEMAEYAEEFAEA
GGVNIVGGCCGTTPEHIRAIAEAVKGLPPRKRPPPPPALRLSGLEPLTITQDSLFVNVGERTNVTGSKKF
ARLILEGDYDAALAVARQQVEAGAQVIDVNMDEGMLDGEAAMVEFLNLIASEPDIPRVPDMIDSSKWEVI
EAGLKGVQGKGIVNSISLKEGEEKFLELAKLVRRYGAAVVVMAFDEEGQADTAERKVEICARAYDLLTEE
VGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKLNLPHALVSGGVSNVSFSFRGNNPVREAIHA
VFLYHAIAAGMDMGIVNAGQLAIYEEIPEELLLLVEDVVLNRREDATERLLEIAEEVKGAGKAAEEEAEE
ERREEEEERLLELLLVGGIEIDEEDDEEAALLLAALELIIIELLLGGGMVVGGLGGGGGKLLLVVVVKAV
VKKKVAVALLKPEEEEKKKGGGKGGGVVVGVVVKVVVDDVDIIIVVVVVVVNNGIVVLVVVVIVVVALEA
AAAAEAAVILLVGGLVLLLLEEEVLAAAEAAAEAAVLLL
>gnl|CDD|440412 COG0647, NagD, Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism]
MSELADRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAE
DEIVTSGDATAAYLAERHPGARVYVIGEEGLREELEEAGLTLVDDEEPDAVVVGLDRTFTYEKLAEALRA
IRRGAPFIATNPDRTVPTEDGLIPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVG
DRLDTDILGANAAGLDTLLVLTGVTTAEDLEAAPIRPDYVLDSLAELLL
>gnl|CDD|440413 COG0648, Nfo, Endonuclease IV [Replication, recombination and repair]
MMLIGAHVSIAGGLLNAVERAAEIGANAFQIFTKNPRGWKAKPLDEEDIEAFREAMEEHGIGPVVVHAPY
LINLASPKPELREKSVAALRDELERCEALGAKYLVFHPGSHVGAGEEAGIARIAEALNEVLEETPGGVTI
LLENTAGQGTELGRTFEELAAIIDRVEDKERVGVCLDTCHAFAAGYDLRTPEGYDGVLDEFDRIIGLDRL
KVIHLNDSKNPLGSRKDRHAHIGEGEIGLEAFRRLVNDPRLAGIPFILETPKEDPGYAEEIALLRELLGE
>gnl|CDD|440414 COG0649, NuoD, NADH:ubiquinone oxidoreductase 49 kD subunit (chain D) [Energy production and conversion]. NADH:ubiquinone oxidoreductase 49 kD subunit (chain D) is part of the Pathway/BioSystem: NADH dehydrogenase
ELETEEMVLNMGPQHPSTHGVLRLVLELDGETVVDADPHIGYLHRGFEKLAENRTYTQIIPYTDRLDYLS
PMNNELAYVLAVEKLLGIEVPERAQYIRVILAELNRIASHLLWLGTYALDLGAMTPFLYAFREREKILDL
FEEVTGARMTHNYFRIGGVRRDLPDGFLEKVREFLDYFPKRLDEYEDLLTGNRIFKARTKGVGVLSAEDA
IALGVTGPVLRASGVDYDLRKDEPYSGYDELDFDVPVGTEGDCYDRYLVRMEEMRQSLRIIRQCLDKLPE
GPVMAKDPKIAPPPKEEMKTSMEALIHHFKLVTEGFKVPAGEVYAAVESPRGELGFYLVSDGGTKPYRVK
IRSPSFANLQALPEMLKGHMLADVVAILGSLDIVLGEVDR
>gnl|CDD|440415 COG0650, HyfC, Formate hydrogenlyase subunit HyfC [Energy production and conversion]
MMLILLALLQLLLALLLAPLLLGIIRKVKARLQGRRGPPILQPYYDLLKLLRKETVVPETASWLFRAAPY
VALAAMLLAALLVPVLTTGPPLSFSGDLIVLVYLLALARFFLALAGLDSGSPFGGIGASREMTLSALAEP
PLLLVLFALALLAGSTSLSDIVAYQAAHGPLLLSPSLLLAAIAFFIVLLAETGRIPFDIPETHLELHEGM
LLEYSGRHLALLELAAALKLFVLLSLFVNLFLPWGIALTLLLALLLFLLKLLVLAVLLAVIEASTARLRL
FRVPDFLWTAFLLALLALLLAVL
>gnl|CDD|440416 COG0651, HyfB, Formate hydrogenlyase subunit 3/Multisubunit Na+/H+ antiporter, MnhD subunit [Energy production and conversion, Inorganic ion transport and metabolism]
MSHLLILPVLLPLLAAALLLLLGRRRRLQRALSLLASLALLALALALLLQVLAGGPLVYALGGWPAPFGI
VLVADRLSALFLLLTALVALAVLLYSIGYMRHERRGRRFYPLFLLLLAGMNGAFLTGDLFNLFVFFEVML
LASYGLVALGGTKEALRAGLKYLILNLVGSALFLLGVGLLYGATGTLNMADLAARLAELDPGLLLAAFAL
LLVGFGIKAALFPLHFWLPDAYPAAPSPVSALLSGLLTKVGVYAILRVLTLLFGADPALFLGTLLLVLGL
LTMLVGALGALAQRDLKRLLAYSSVSQIGYILLGLGLGTPLGLAGALFHLLNHALAKALLFLAAGAIERA
TGTRDLDKLGGLGKRMPLTAAAFLIGALALAGLPPLSGFVSKWLLLQAALEAGAWLLAAVLLLSSLLTLA
YFVRIFGRAQ
>gnl|CDD|440417 COG0652, PpiB, Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones]
MKAAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP
GYTIPDEFDPGLKHKRGTLAMARAQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTD
PGDGPLEPVVIESVTIVED
>gnl|CDD|440418 COG0653, SecA, Preprotein translocase subunit SecA (ATPase, RNA helicase) [Intracellular trafficking, secretion, and vesicular transport]
MGKLLKKIFGSRNDRELKRLRKIVDKINALEPEMEALSDEELRAKTDEFKERLANGETLDDLLPEAFAVV
REASKRVLGMRHFDVQLIGGIVLHQGKIAEMKTGEGKTLVATLPAYLNALTGKGVHVVTVNDYLAKRDAE
WMGRLYRFLGLSVGVIVHGMDPEERRAAYAADITYGTNNEFGFDYLRDNMVFSLEDMVQRGLNYAIVDEV
DSILIDEARTPLIISGPAEDSTDLYYRINKLVPRLKRDGDYTVDEKARTVTLTEEGIEKVEKLLGIDNLY
DPENIELVHHLNQALRAHALFKRDVDYIVKDGEVVIVDEFTGRLMPGRRYSDGLHQAIEAKEGVKIQNEN
QTLASITFQNYFRMYEKLAGMTGTADTEAEEFREIYGLDVVVIPTNRPMIRKDEPDLVYKTEEEKFNAVV
EDIKERHEKGQPVLVGTTSIEKSELLSKLLKKEGIPHNVLNAKQHEREAEIVAQAGRPGAVTIATNMAGR
GTDIVLGGNPEFLAAAELADRGLEWEEAIAKIKAEWQAEHEEVLEAGGLHVIGTERHESRRIDNQLRGRS
GRQGDPGSSRFYLSLEDDLMRIFGSDRIKGMMDKLGMEEGEPIEHKMVSKAIENAQKKVEGRNFDIRKNL
LEYDDVMNDQRKVIYEQRREILEGEDLSETILDMREDVIEDLVDEYIPEGSYPEQWDLEGLEEALKELFG
LDLPIEEWLDEEGLDEEELRERLLEAADEAYEEKEEELGPEVMRELERVVLLQVLDRKWREHLDAMDHLR
QGIGLRGYAQKDPLVEYKREAFELFEEMLDSIKEEVVRYLFRVQVRSEEEREEVEEERRENHADPAGEEE
EEAPKQPVRKGPKVGRNDPCPCGSGKKYKHCHGKLA
>gnl|CDD|440419 COG0654, UbiH, 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]. 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLARGAP
IRGIRVRDGSDGRVLARFDAAETGLPAGLVVPRADLERALLEAARALGVELRFGTEVTGLEQDADGVTVT
LADGRTLRADLVVGADGARSAVRRLLGIGFTGRDYPQRALWAGVRTELRARLAAAGPRLGELLELSPRSA
FPLRRRRAERWRRGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAALRGRDDEAALARYERERRP
RAARVQRAADALGRLFHPDSPPLRLLRNAGLRLLDRLPPLKGGGLP
>gnl|CDD|440420 COG0655, WrbA, Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and conversion]
KILVINGSPRKNGNTAALAEAVAEGAEEAGAEVELIRLADLDIKPCIGCGGTGKCVIKDDMNAIYEKLLE
ADGIIFGSPTYFGNMSAQLKAFIDRLYALWAKGKLLKGKVGAVFTTGGHGGAEATLLSLNTFLLHHGMIV
VGLPPYGAVGGGGPGDVLDEEGLATARELGKRLAELAKKLK
>gnl|CDD|440421 COG0656, ARA1, Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism]
NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWND
NHGYDDTLAAFEESLERLGLDYLDLYLIHWPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLA
ETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHL
QRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERLGPDPD
>gnl|CDD|440422 COG0657, Aes, Acetyl esterase/lipase [Lipid transport and metabolism]
MDVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAA
LRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLTASPLRADLAGLP
PTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLPEARAALAEIAAFLRRALA
>gnl|CDD|440423 COG0658, ComEC, DNA uptake channel protein ComEC, N-terminal domain [Intracellular trafficking, secretion, and vesicular transport]
AGLLAALLLGDRSGLSPELWEAFRATGLAHLLAISGLHVGLVAGLVLLLLRRLGPPRRLAALLALLALLL
YALLAGFSPSVLRAALMLALVLLALLLGRRASSLRALALAALLLLLLDPLALLSPGFQLSFLAVAGLILL
YPPLRRRLARRLPRWLAELLAVSLAAQLATLPLLLYLFGQVSLVSLLANLLAVPLVSLIVVPGLLLALLL
LPLLPPLALLLLLLALLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL
LLLLLLLLLLLLLLLLLLLLLLGLLGGVGVGGGDGGLLLGGRGLLGVLGGLLLLLLLLLLLLLLLLLGLL
LVLLLLLLLALLLGLLLLLLAALLGLAAALLLLLALLALLALLALALLLGALVGLLVVLLLALRSLLLGG
GLLLLLLLLLLLLALALLLLLLALLSLLLLLLLLLALLLLLLGSLLLSLLLLLALASSALASLSSSSSGA
AVLAAAGAVALLASGGLAALAPGALGLLGGRGRRGTRRGGRLRRTRLLRRLVR
>gnl|CDD|440424 COG0659, SUL1, Sulfate permease or related transporter, MFS superfamily [Inorganic ion transport and metabolism]
GYRRSNLRGDLLAGLTVALVALPLALAFAIAAGLPPEAGLYAAIVGGIVYALFGGSRLLISGPTAALAVV
VAAAVAPLGSLALLLAATLLAGVLQLLLGLLRLGRLARFIPRPVIVGFLAGIAILIILGQLPHLLGLPAP
GGSFLEKLAALLAALGEINPPTLALGLLTLAILLLLPRLLKRIPGPLVAVVLGTLLVWLLGLDVATVGEI
PSGLPSFSLPDFSLETLRALLPPALTIALVGSIESLLTARAVDAMTGTRSDPNRELIAQGLANIASGLFG
GLPVTGSISRSAVNVKAGARTRLSGIVHALFLLLVLLFLAPLLAYIPLAALAAILIVVGIGLIDWRSFRR
LWRAPRSDFLVMLVTFLVTVFTDLLIGVLVGVLLSLLLFLRRVSRPHVVVLRVPGTHFRNVERHPEAETG
PGVLVYRLDGPLFFGNAERLKERLDALAPDPRVVILDLSAVPFIDATALEALEELAERLRARGITLELAG
LKPPVRDLLERAGLLDELGEERVFPDLDEALEAAEERAE
>gnl|CDD|440425 COG0661, AarF, Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport and metabolism, Signal transduction mechanisms]. Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family is part of the Pathway/BioSystem: Ubiquinone biosynthesis
MSALRRLRRLARIARVLLRYGLGELLDRLGLPRLRRLLTGEERREELRRRRAERLRLALEELGPTFIKLG
QLLSTRPDLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVHRARL
KDGREVAVKVQRPGIEEAIEADLRILRRLARLLERLSPEGRRLDPVEVVDEFARSLLEELDYRREAANAE
RFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGF
FHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELLLALLNRDYDRVAEALLELGFVPPDTDVDE
LERALRAVLEPYFGKPLKDISFGELLLELFELARRFPLRLPPELVLLQRTLLTLEGVGRQLDPDFDLWEV
AKPFLERLLRERLGPRALLKRLKREAPELAELLPRLPRLLERAALIIGSALLLLALLGLAALLGWLL
>gnl|CDD|440426 COG0662, ManC, Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism]
MQDVNIEELKAIGWGSYEVLGEGGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTIGDEEVEL
KAGDSVYIPAGVPHRLRNPGDEPLELLEVQAPAYLGEDDIVRED
>gnl|CDD|440427 COG0663, PaaY, Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only]
MMIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGY
PLTIGDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKV
VRELTEEEIAFLRESAENYVELARRYLAEL
>gnl|CDD|440428 COG0664, Crp, cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms]
FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGE
LSLLGGEPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERL
ARFLLELADRLDGRIDLPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERLA
>gnl|CDD|440429 COG0665, DadA, Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]
ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGASGRNAGQLRPGLAALADRALVRLAREALDL
WRELAAELGIDCDFRRTGVLYLARTEAELAALRAEAEALRALGLPVELLDAAELREREPGLGSPDYAGGL
YDPDDGHVDPAKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTERGTVRADAVVLAAGAWSARL
LPMLGLRLPLRPVRGYVLVTEPLPDLPLRPVLDDTGVYLRPTADGRLLVGGTAEPAGFDRAPTPERLEAL
LRRLRRLFPALADAEIVRAWAGLRPMTPDGLPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILG
GEPPLDLAPFSPDR
>gnl|CDD|440430 COG0666, ANKYR, Ankyrin repeat [Signal transduction mechanisms]
LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVA
LLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL
EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA
DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA
ALLDLLTLL
>gnl|CDD|440431 COG0667, PdxI, Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only]
MEYRRLGRSGLKVSRLGLGTMTFGGPWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK
GRPRDDVVIATKVGRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDE
LVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAG
GLLTGKYRRGATFPEGDRAATNFVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPG
ARSPEQLEENLAAADLELSAEDLAALDAALAAVPAP
>gnl|CDD|440432 COG0668, MscS, Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis]
EALAQLWSLLGLLLLLGELLLALLPKLLLALLILLIGWLLIRLLRRLIRRLLRRARRDRTLLPLLRNILK
ILIVIIAILLILSILGVNITSLLAGLGAAGLAIGLAAQDLLSNFIAGIFILLERPFRVGDWIEVGGVEGT
VEEIGLRSTRLRTLDGRLVTIPNSKILSSPITNYSRGPTRRVDVTIGVDYDTDIDKARELLKEILEELPR
ILKDPAVVGVTELGDSSVNLRVRAWTKPGDYWDVRRDIRERIKAALDEAGIEIPFPTRTVHLAEEA
>gnl|CDD|440433 COG0669, CoaD, Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]. Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFD
GLLVDFAREVGANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGD
VSGFVPPAVAEALKEKFAK
>gnl|CDD|440434 COG0670, YbhL, Integral membrane protein YbhL, putative Ca2+ regulator, Bax inhibitor (BI-1)/TMBIM family [Inorganic ion transport and metabolism]
MNNFDRNAGAAAAASDAGLRKVLRNTYGLLALGLLLTALVAYLGMALPGLAALLFGSPGLFWVLLIAPLG
LVFLLSKLANRANSAAALALLFAYTALMGLTLSPILLVYTGLSGPASIAQAFGGTAATFGGLSLYGYTTK
RDLSFLGSFLFMGLIGLIIASLVNIFLQSPALSLAISVAGVLLFSGLTLYDTQRIKHGYETNKQYIMAAL
SLYLDFINLFLSLLRLLGGRR
>gnl|CDD|440435 COG0671, PgpB, Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]. Membrane-associated phospholipid phosphatase is part of the Pathway/BioSystem: Phospholipid biosynthesis
LLLALLLALLLLLLLLADLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLAL
LLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGTAGGYSFPSGHAAAAFALALVLALLLPR
RWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALLRR
>gnl|CDD|440436 COG0672, FTR1, High-affinity Fe2+/Pb2+ permease [Inorganic ion transport and metabolism]
PWSAMLAAFLIVLREGLEALLVVGILLAYLRKTGRRDLLRWVWAGVGAALAASLLLAALLQYLISGLSGA
GQELFEGVIGLVAVAMLTWMVFWMHSKARSWKAELEGKVDAALSRGSLWGLALLAFLAVLREGFETVLFL
YALAAQAGGTSAVLLGALLGLALAVVIGYLLYRGGVRLPLRRFFRVTGVLLLLLAAGLLGKGVHELQEAG
LLPALQDPLWDTSALLPDDSWPGTLLKGLLGYYPRPTLEQLIAQLLYLVVVLGLFLRRARRAAAAARAA
>gnl|CDD|440437 COG0673, MviM, Predicted dehydrogenase [General function prediction only]
MDKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVRVYTDYEELLADPDIDAVVI
ATPNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSG
AIGEIRSVRARFGHPRPAGPADWRFDPELAGGGALLDLGIHDIDLARWLLGSEPESVSATGGRLVPDRVE
VDDTAAATLRFANGAVATLEASWVAPGGERDERLEVYGTKGTLFVDAIRGGEPPPVSLEDGLRALELAEA
AYESARTGRRVELPD
>gnl|CDD|440438 COG0674, PorA, Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha subunit [Energy production and conversion]. Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha subunit is part of the Pathway/BioSystem: Pyruvate oxidation
GKRVLMDGNEAVALGAIAAGCRVIAAYPITPSTEIAEYLAEWLAELGGVVVQAESEIAAIGAVIGASAAG
ARAMTATSGPGLSLMQEGLGLAAGAELPLVIVVVQRAGPSTGLPIKGDQSDLMQALYGGHGDTGWIVLAP
SSVQEAFDLTIIAFNLAEKYRVPVIVLFDGFLGSHEEPVELPDDEEVKILPRPEEYRPYALDEDPRAIPG
TAQPDVYFTGLEHDETEDPENAEKMVEKRMRKFEKIRDELPRVEYYGAEDAEVVIVAMGSTAGTAKEAVD
RLREEGIKVGLLRVRLLRPFPAEALREALKGVKKVAVVERNKSGQLALDVRAALGADRVVGGIYGLGGRP
FTPEEILAVIEELLKGAPKFTL
>gnl|CDD|440439 COG0675, InsQ, Transposase [Mobilome: prophages, transposons]
MLRTYKFRLYPTKEQEELLERTLGCCRFVYNYALAERRQAYKETGKSLSYYELQKLLTELKKEYPWLKEL
PSQVLQQALKRLDEAFKSFFKRKKKGKKAGFPRFKKKGRYRSFTYPQSGFKLKDGRLKLPKIGWVKIRLH
RPLPDDGKIKSVTISRKAAGKWYVSFVVEVEDVPELPPTGKVVGIDLGLKNFATLSDGEKIDNPKFLKKA
ERKLAKLQRRLSRKKKGSKNRRKARKKLAKLHEKIANQRKDFLHKLARKLVKEADVIVVEDLNVKGMKKN
KKLNKSISDAGWGEFRRQLEYKAEKYGIKVVEVDPAYTSQTCSSCGHVVKKLRLSVRTFVCPKCGTVHDR
DVNAAINILRRGLRQLGLAGHSGGTVRPLRD
>gnl|CDD|440440 COG0676, YeaD, D-hexose-6-phosphate mutarotase [Carbohydrate transport and metabolism]
MSLTILNLFGLSPSVSLRGPGGLPVLRIDNPGARATIALQGAHVLSWQPAGEEPVLWLSPAAAFEPGKAI
RGGVPVCWPWFGPHPSDPGLPAHGFARTRPWQLTEHREDDGGVILTLTLTDSEATRALWPHAFELELTVT
LGETLTLELTTTNTGDQPFSFTQALHTYFAVGDIEQVRVSGLEGARYIDKLDGGAEKQQEGPLTFTGETD
RVYLDPPAPLTIHDPGLKRRIRIAKSGSSSVVVWNPWAEKAASMADMPDDGYRTMVCVETANALDDAVTL
APGESHTLSQTISVEP
>gnl|CDD|440441 COG0677, WecC, UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]
KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGRLRATTDPEA
LAEADVVIIAVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKA
GEDFFLAYSPERINPGNKLHELRNIPKVVGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENT
YRDVNIALANELALICDRLGIDVWEVIEAANTKPGFLIFYPGPGVGGHCIPVDPYYLTWKARELGYHPRL
ILAAREINDSMPEYVVERVVKALNEAGKSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDV
HDPYVDEEEVEGEYGELVDLEEALEGADAVVLAVDHDEFDELDPEELRLKGAKVVVDTRGVLD
>gnl|CDD|440442 COG0678, AHP1, Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]
TIKVGDKLPDVTFKTRTADGPEDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDE
IACVSVNDAFVMNAWGKAQGAEGKITMLADGNGEFTKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLN
VEPAPGPFEVSDAETLLAQL
>gnl|CDD|440443 COG0679, YfdV, Predicted permease, AEC (auxin efflux carrier) family [General function prediction only]
MLTILSAILPIFLLIALGYLLGRRGLLPEEDAKGLSRLVFYVALPALLFSSLATADLSELLDLLSLLLAA
LLATLLLFLLALLLARLLKLDRAERGVLALAASFGNTGFLGLPLALALFGEEGLAYAALYDAVNNLLLNT
LGVILLSRGGGGGASSLKKVLKKLLRNPLIIAILLGLLLNLLGIPLPAPLDDTLDLLGGAAIPLALLALG
ASLALSRLKGDLKLVLLASLLKLLLLPLLALLLALLLGLDGLLLQVLVLLAAMPTAVNAYVLAERYGGDP
ELAASAVLLSTLLSLVTLPLWLALLGLL
>gnl|CDD|440444 COG0680, HyaD, Ni,Fe-hydrogenase maturation factor [Energy production and conversion]
MMKILVLGIGNPLRGDDGVGVRVAEALEERELPEGVEVIDGGTLGLELLELLEGADRVIIVDAVDSGAEP
GTVRRLEPEELPAGDASKLSTHQLGLAELLALARLLGDLPEEVVLIGIEPESLEFGEGLSPEVAAAVPKA
VELILEELAE
>gnl|CDD|440445 COG0681, LepB, Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport]
MSKKKKKKRELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGFGEPKRGDI
VVFKYPEDPSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDGDVEVPPGEEEVPGGG
GDNSNDSRSGDPDDGGGGVGVDGVGVGGVVDVVVPDVDSRLVDVGDGPP
>gnl|CDD|440446 COG0682, Lgt, Prolipoprotein diacylglyceryltransferase [Cell wall/membrane/envelope biogenesis]
LNMDPVLFSIGPLAIRWYGLMYALGFLLGLWLARRRAKRRGLDPDQVDDLLLWAVLGGIIGARLGYVLFN
PDYYLANPLEIFAIWEGGLSFHGGLIGGILAAWLFARKRKLPFLKLADAIAPGLPLGQAIGRIGNFINGE
LYGRPTDLPWGVVFPNGSGGLPRHPTQLYEALLELLLFALLLWLRRKKRPPGQLFGLYLILYGLGRFFIE
FFREDDAQLGYLGLTMGQLLSLPMILLGLALLVYARRRKKAAP
>gnl|CDD|440447 COG0683, LivK, ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid transport and metabolism]
ADPIKIGVLLPLTGPYAALGQPIKNGAELAVEEINAAGGVLGRKIELVVEDDASDPDTAVAAARKLIDQD
KVDAIVGPLSSGVALAVAPVAEEAGVPLISPSATAPALTGPECSPYVFRTAPSDAQQAEALADYLAKKLG
AKKVALLYDDYAYGQGLAAAFKAALKAAGGEVVGEEYYPPGTTDFSAQLTKIKAAGPDAVFLAGYGGDAA
LFIKQAREAGLKGPLNKAFVKAYKAKYGREPSSYAAAGYDAALLLAEAIEKAGSTDREAVRDALEGLKFD
GVTGPITFDPDGQGVQPVYIVQVKADGKFVVVET
>gnl|CDD|440448 COG0684, RraA, RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal structure and biogenesis]
PRLDAELLERLAAVSTATVSDALDRLLRGALDPGIRPLHPGARLVGPAVTVRYRPGDNLMLHEAIDLAPP
GDVLVIDAGGDTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRVGPGE
INVPVSIGGVTVRPGDLVVADDDGVVVIPAELAEEVLEAAEAIEAREEFIRERIRAGESLADLY
>gnl|CDD|440449 COG0685, MetF, 5,10-methylenetetrahydrofolate reductase [Amino acid transport and metabolism]
MKLEELLKAGKPVVSFEFFPPKTAEGEEKLWETAEELAPLDPDFVSVTYGAGGSTRDRTLAIAARIQQET
GLEPVAHLTCVGRNREELESILLGLAALGIRNILALRGDPPKGDGHPGGFLYASELVALIREMNGDFCIG
VAAYPEKHPEAPSLEADLDRLKKKVDAGADFAITQLFFDNDAYFRFVDRARAAGIDVPIIPGIMPITSFK
QLARFAELCGAEIPDWLLKRLEKAGDDEAVRAVGIEIATEQCEELLAEGVPGLHFYTLNRAEATLEILER
LGLL
>gnl|CDD|440450 COG0686, Ald, Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]. Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle
MIIGVPKEIKNNENRVALTPAGVRELVAAGHEVLVETGAGLGSGFSDEDYSAAGAEIVDTAEEVFAQADL
IVKVKEPQPEEYALLRPGQILFTYLHLAADPELTEALLEKGVTAIAYETVEDPDGSLPLLAPMSEIAGRM
AIQIGAEYLEKPNGGRGVLLGGVPGVPPAKVVILGGGVVGTNAARMALGLGADVTVLDINLDRLRRLDDI
FGGRVTTLYSNPANIEEALKEADLVIGAVLIPGARAPKLVTREMVKRMKPGSVIVDVAIDQGGCFETSRP
TTHDDPTYVVHGVVHYCVANMPGAVPRTSTYALTNATLPYLLALADKGWEQALREDPGLAKGLNTYKGKL
TNKAVAEAFGLPYTDLELLLAA
>gnl|CDD|440451 COG0687, PotD, Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]
MSRRSLLGLAAAALAAALAGGAPAAAAEGTLNVYNWGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAK
LRAGGSGYDVVVPSDYFVARLIKAGLLQPLDKSKLPNLANLDPRFKDPPFDPGNVYGVPYTWGTTGIAYN
TDKVKEPPTSWADLWDPEYKGKVALLDDPREVLGAALLYLGYDPNSTDPADLDAAFELLIELKPNVRAFW
SDGAEYIQLLASGEVDLAVGWSGDALALRAEGPPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFM
LSPEVAAALAEYVGYAPPNKAARELLPPELAANPAIYPPEEVLDKLEFWNPLPPENRELYTRRWTEIK
>gnl|CDD|440452 COG0688, Psd, Phosphatidylserine decarboxylase [Lipid transport and metabolism]. Phosphatidylserine decarboxylase is part of the Pathway/BioSystem: Phospholipid biosynthesis
PKHLLSRLMGPIAREGWPFIALLIRTFIKRYGIDLSEALPSSYTSFNDFFFRDLKPGARPIPDDPDAVVS
PADGKVSQIGEIEEDRLLQAKGHPYSLEELLGDSELAEKFEGGTFVSIFLSPFDYHRNHMPVDGTVVEVK
YIPGKFLSVNPLALRPKLFARNERVVIVIETEFGPVAVVQVGALIVRRIVTYVKEGDTLKKGEEMGLFKF
GSTVDLLLPKGAVEILVKPGQKVRAGETIGRLK
>gnl|CDD|440453 COG0689, Rph, Ribonuclease PH [Translation, ribosomal structure and biogenesis]
MRPDGRAPDQLRPVKITRGFTKHAEGSVLIEFGDTKVLCTASVEEGVPPFLKGSGQGWVTAEYGMLPRAT
HTRNRREAARGKQSGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVLQADGGTRTASITGAFVALADA
LNKLVEKGLLKENPLKDQVAAVSVGIVDGEPVLDLDYEEDSAAEVDMNVVMTGSGEFVEVQGTAEGAPFS
REELDALLDLAEKGIAELIALQKEALGE
>gnl|CDD|440454 COG0690, SecE, Preprotein translocase subunit SecE [Intracellular trafficking, secretion, and vesicular transport]
MAKKKTGKGKKIVKFFKEVRAELKKVVWPTRKELIQTTLVVLVFVLIFALFLWLVDLLFGWLVSLILG
>gnl|CDD|440455 COG0691, SmpB, tmRNA-binding protein [Posttranslational modification, protein turnover, chaperones]
MAKKPGIKVIAQNRKARHDYFIEETYEAGIVLTGTEVKSLRAGKANLKDSYARIKNGELWLINAHISPYE
QGNHFNHDPRRTRKLLLHKKEIDKLIGKVKEKGYTLVPLKLYFKDGRAKVEIALAKGKKLYDKRETIKER
DWKREKERALKRR
>gnl|CDD|440456 COG0692, Ung, Uracil-DNA glycosylase [Replication, recombination and repair]
MDVLLEPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHG
PGQAHGLSFSVPPGVPLPPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGK
GWETFTDAVIRALNARKEPVVFLLWGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAY
LEEQGKTPIDW
>gnl|CDD|440457 COG0693, YajL, Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms]
MMKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPPVTSKHGITVTADKTLDDVDPDDYDALVL
PGGHGAPDDLREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGATYVD
EEVVVDGNLITSRGPGDAPAFARALLELLA
>gnl|CDD|440458 COG0694, NifU, Fe-S cluster biogenesis protein NfuA, 4Fe-4S-binding domain [Posttranslational modification, protein turnover, chaperones]
AQAAALKLLPEEPGGELIRGEVAAPGAPAAAALLLAEAPEVEEDDDVVVVAAVFVAVTDELSGPLLELAI
IDAILAAAGGQLTLAAPDAAVAEVLSFHALTDAELEERIEEVLDEEIRPALASDGGDIELVDVEDGVVYV
RLGGACSGCPSSTMTLKNGIERALKERVPEVKEVEA
>gnl|CDD|440459 COG0695, GrxC, Glutaredoxin [Posttranslational modification, protein turnover, chaperones]
KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFIGGEHLGGFDEGELD
ALLA
>gnl|CDD|440460 COG0696, GpmI, Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and metabolism]. Phosphoglycerate mutase (BPG-independent), AlkP superfamily is part of the Pathway/BioSystem: Glycolysis
RKKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGA
GRVVYQDLTRINKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGV
KKVYVHAFLDGRDTPPKSALGYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGE
TAASAVEAIEASYARGETDEFVKPTVIVDYGKPVATIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDR
GKRPKLLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLAKAGLKQLRIAETEKYAHVTFFFNGGREEPFP
GEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIVLNFANPDMVGHTGVLEAAIKAVEAVDE
CLGRVVDAVLAAGGTLLITADHGNAEQMIDPDTGGPHTAHTTNPVPFILVGGDKGVKLREDGRLADIAPT
ILELMGLPQPAEMTGKSLIEK
>gnl|CDD|440461 COG0697, RhaT, Permease of the drug/metabolite transporter (DMT) superfamily [Carbohydrate transport and metabolism, Amino acid transport and metabolism, General function prediction only]
RLRGILLLLLAALLWGSSFVAIKLALAGLPPLQLAFLRFLLAALLLLPLLLLRGRRLPPLSRRDWLLLLL
RGLLGLALAFLLFFLALQYTPAALAALLLALAPLFVALLAALLLGERLSRRRWLGLLLGFAGVLLIVGPG
GGGGGGSLLGDLLALLAALSWALYTVLTRRLSRRLDPLTLTFWQMLVGALLLLPLALLTGLPLPLSAAAW
LALLYLGLFGTALAYLLWFRALRRLGASRAAPLTYLEPVFAVLLGWLLLGEPLTPLQLLGAALILAGVLL
AALRERRRAA
>gnl|CDD|440462 COG0698, RpiB, Ribose 5-phosphate isomerase RpiB [Carbohydrate transport and metabolism]. Ribose 5-phosphate isomerase RpiB is part of the Pathway/BioSystem: Pentose phosphate pathway
MKIAIGSDHAGFELKEAIKEYLEEKGHEVVDFGTYSEDSVDYPDFAIKVAEAVASGEADRGILICGTGIG
MSIAANKVPGIRAALCHDPYSARLAREHNDANVLCLGARVIGPELAKEIVDAFLATEFEGGRHQRRVDKI
SELEKENAK
>gnl|CDD|440463 COG0699, CrfC, Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, recombination and repair]
MIPVGVLDETIEDRADLRRRLDQARLDLADPSLRIVMAGTTSQGKSQLVNALLGRRLLPSGAGETTGVPT
EIKHAEGSSARLLPTAGSVADTKRWPGLDTEEIYNPIHQVSQTKKRRARGSNGPEVLRALVGLPHPLLRQ
GLVIVDTPGLGALVGSEAELTLAKLPDADAVLVVLDADAEVTASEMELLRRVIQNLRICPSVFVVLNKID
RRWRDLQPRQRTADQLHLQRADVSRVLPLSALLGLLAKVAGDKELNEESRFPGLEAILSEQILARAGELE
RPQVLGEFNSAVAQSGKLLSSELERAEREADELRQNYARWQAELGDELNDLTADVHHDLRTRFRTLRTAQ
RLLDSQDPTLRAPISQYLLEEHWDELFRNLANSLTTAGGDNFIWAFFRSVANDLAKSFAEAGRDNVLSAS
IFPRSELRPIAAMEAPQLLRLQQQQKQLIGLRGSGGVFMLGLTSSLVGLGLLNRRVIETLVQRLLRVFAE
LKARVRRWVDDLLLPFSQHPRDAKLLEQRMLRDHFLYIAEELERSLLESLQELIAALQQRLTEREQRYRE
LGRDLGIEQQDNLVGLAGVGRA
>gnl|CDD|440464 COG0700, SpmB, Spore maturation protein SpmB (function unknown) [Function unknown]
SLLSNWIIPLIILLILLYGLLKKVNVYEAFVEGAKEGFKTAVKIIPYLVAMLVAIGVFRASGALDLLIDG
LKPLLSLLGIPAEALPLALMRPLSGSGALGMMTDLMKTYGPDSFIGRLASTMQGSTETTFYVLAVYFGAV
GIKKTRYALPVGLLADLAGIIAAIFICYLFFG
>gnl|CDD|440465 COG0701, YraQ, Uncharacterized membrane protein YraQ, UPF0718 family [Function unknown]
LMSQLGEALTFFLYLLLEALPFLLLGVFLSGLIQVFVPPERLRRLLGGNGLLGVLLAALLGALLPFCSCG
VVPLARGLLKAGAPLGAAMAFLLASPLINPIAILLTAGLFGWKFALARVVAGLLVAIVIGLLIGRLGRER
ELEPAELSAGGGGAEAERSWKERLRRALREAWEEFKDVGPYLLIGVLIAALIQGFVPAEFLASLGGGNNL
LSVLLAALLGVPLYVCSEGDIPIAAALLAKGMSPGAALAFLMAGPALSLPELIMLRKVFGPRLLAAFLGL
VLVGAILAGLLFNLLL
>gnl|CDD|440466 COG0702, YbjT, Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only]
KILVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALAAAGVEVVQGDLDDPESLAAALAGVDAVFLL
VPSGPGGDFAVDVEGARNLADAAKAAGVKRIVYLSALGADRDSPSPYLRAKAAVEEALRASGLPYTILRP
GWFMGNLLGFFERLRERGVLPLPAGDGRVQPIAVRDVAEAAAAALTDPGHAGRTYELGGPEALTYAELAA
ILSEA
>gnl|CDD|440467 COG0703, AroK, Shikimate kinase [Amino acid transport and metabolism]. Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEEENA
VIATGGGAVLSPENRELLKEHGTVVYLDASPETLLERLRRDDNRPLLQGEDPRERLEELLAEREPLYREV
ADITVDTDGRSPEEVVDEILEALEE
>gnl|CDD|440468 COG0704, PhoU, Phosphate uptake regulator PhoU [Inorganic ion transport and metabolism]
EELEELRNDLLEMGGLVEEALEDAIEALLERDLELAEEVIEGDDEIDALEVEIEEECLRLIALQQPVASD
LRLIVAALKIATDLERIGDLAVNIAKRALRLAPEPPLKPLVDIEEMAELALEMLKDALDAFARRDVELAR
EVAERDDEVDELYRSIFRELLTYMMEDPRNIEQAIDLLLIARYLERIGDHATNIAERVIYLVTGEDVRHN
RPK
>gnl|CDD|440469 COG0705, GlpG, Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein turnover, chaperones]
RLPPVTLALIALNVLVFLLQLLLGGELLNWLALVPARLLLGELWRLLTSMFLHGGFLHLLFNMLALWVFG
PLLERRLGSKRFLLLYLLSGLGGGLLQLLFSPGSGYPLVGASGAIFGLLGALLVLGPRRRVLLLFIPIPA
LLFLLVWLLLGLLFGLLGGGGIAWEAHLGGLLAGLLLALLLRKLRRRRR
>gnl|CDD|440470 COG0706, YidC, Membrane protein insertase Oxa1/YidC/SpoIIIJ [Cell wall/membrane/envelope biogenesis]
IDYGWFGFIAKPLFWLLNFLHSLVGNWGLAIILLTLIVRLLLFPLTVKQYKSMAKMQELQPELKEIQEKY
KDDPQKLQQEMMKLYKEEGVNPLGGCLPMLIQMPIFIALYRVLRNSIELRHAPFLGIPDLSAPDPYYIFL
PILMGVTMFLQQKLNPAPAQDPQQKKMMYIMPLMFLFFFLSFPAGLVLYWVVSNLLTIGQQLIINRRLDK
KK
>gnl|CDD|440471 COG0707, MurG, UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]. UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis
MSKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKN
LKAPFRLLKALLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADR
VALAFPETKKYFPKKKAVVTGNPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALA
ALLEARLQVVHQTGKGDYEEVRAAYAAAIRPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKP
AILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPEKLAEALEELLEDPERLAKMAEAARALARPDAA
ERIADLILELAKG
>gnl|CDD|440472 COG0708, XthA, Exonuclease III [Replication, recombination and repair]
MKIASWNVNGIRARLPKLLDWLAEEDPDVLCLQETKAQDEQFPLEAFEAAGYHVYFHGQKGYNGVAILSR
LPPEDVRRGLGGDEFDAEGRYIEADFGGVRVVSLYVPNGGSVGSEKFDYKLRFLDALRAYLAELLAPGRP
LILCGDFNIAPTEIDVKNPKANLKNAGFLPEERAWFDRLLELGLVDAFRALHPDVEGQYTWWSYRAGAFA
RNRGWRIDYILASPALADRLKDAGIDREPRGDERPSDHAPVVVELD
>gnl|CDD|440473 COG0709, SelD, Selenophosphate synthase [Amino acid transport and metabolism]
MMEEIRLTQLSHGGGCGAKIGPGVLAQILAGLPPPSDPNLLVGLETSDDAAVYRLGDDQALVQTTDFFTP
IVDDPYDFGRIAAANALSDVYAMGGRPLTALAIVGFPIDKLPEEVLAEILAGGADKCREAGAPLAGGHSI
DDPEPKYGLAVTGLVHPDKVLRNAGARPGDVLILTKPLGTGILTTAIKAGLADGEDIAAAIASMTTLNKA
AAELARLYGVHACTDVTGFGLLGHLLEMARGSGVSAEIDLDAVPLLPGALELAEQGIVPGGTYRNRASYG
AKVEFAEGLDEAQRDLLFDPQTSGGLLIAVPPEAAEELLAALRAAGYAAAIIGEVTAGEGGAIEVR
>gnl|CDD|440474 COG0710, AroD, 3-dehydroquinate dehydratase [Amino acid transport and metabolism]. 3-dehydroquinate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
EGRPKICVPLVGATPEDLLAEAEAAARAGADLVELRLDYLEDPDLEELKELLEALREYGGLPLIFTFRTA
EEGGEFEGSEEERLELLRAAADSAGVDLVDVELDTLEDDVDDLIEAAREAGVKVIVSYHDFEKTPSAEEL
VEILEKMQELGADIVKIAVMAKSPEDVLRLLEATLEAKEELDRPVITMAMGELGKISRILGPLFGSALTY
ASVGEASAPGQIDVEELRELLELLEA
>gnl|CDD|440475 COG0711, AtpF, FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]. FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAE
IIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAA
QAALVDRFIAEL
>gnl|CDD|440476 COG0712, AtpH, FoF1-type ATP synthase, delta subunit [Energy production and conversion]. FoF1-type ATP synthase, delta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
MALSTIARRYAKALFELAKEKGALDEVEEELFALAALLAENPELRALLSSPVISAEEKKELLEALFGGKL
SPETLNFLKLLVENGRLALLPEIAEEFEELAAERRGIVVAEVTSAVPLSEEQLERLAAALEKKTGKKVEL
NVKVDPSLIGGVVVRVGDKVIDGSVRGRLNRLRRALKG
>gnl|CDD|440477 COG0713, NuoK, NADH:ubiquinone oxidoreductase subunit 11 or 4L (chain K) [Energy production and conversion]. NADH:ubiquinone oxidoreductase subunit 11 or 4L (chain K) is part of the Pathway/BioSystem: NADH dehydrogenase
IPLEHYLILAAILFAIGLYGVLTRRNLIVVLMSIELMLNAVNLNLVAFSRYLGDLDGQVFALFVIAVAAA
EVAVGLAIIVALYRNRGTIDVDDLNELKG
>gnl|CDD|440478 COG0714, MoxR, MoxR-like ATPase [General function prediction only]. MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MTEARLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLP
SDILGTYIYDQQTGEFEFRPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIA
TQNPIEQEGTYPLPEAQLDRFLLKLYIGYPDAEEEREILRRHTGRHLAEVEPVLSPEELLALQELVRQVH
VSEAVLDYIVDLVRATREHPDLRKGPSPRASIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHRLILS
PEADAEGVTADD
>gnl|CDD|440479 COG0715, TauA, ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism]
LAALAALALAACSAAAAAAEKVTLRLGWLPNTDHAPLYVAKEKGYFKKEGLDVELVEFAGGAAALEALAA
GQADFGVAGAPPALAARAKGAPVKAVAALSQSGGNALVVRKDSGIKSLADLKGKKVAVPGGSTSHYLLRA
LLAKAGLDPKDVEIVNLPPPDAVAALLAGQVDAAVVWEPFESQAEKKGGGRVLADSADLVPGYPGDVLVA
SEDFLEENPEAVKAFLRALLKAWAWAAANPDEAAAILAKATGLDPEVLAAALEGDLRLDPPLGAPDPARL
QRVADFLVELGLLPKDV
>gnl|CDD|440480 COG0716, FldA, Flavodoxin [Energy production and conversion]. Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis
ILIVYGSTTGNTEKVAEAIAEALGAAGVDLFEIEDADLDDLEDYDLLILGTPTWAGELPDDWEDFLEELK
EDLSGKKVALFGTGDSSGYGDALGELKELLEEKGAKVVGGYDFEGSKAPDAEDTEERAEEWLKQL
>gnl|CDD|440481 COG0717, Dcd, dCTP deaminase [Nucleotide transport and metabolism]. dCTP deaminase is part of the Pathway/BioSystem: Thymidylate biosynthesis
MILSDKEIRKLIEEGRIVIEPFDEEQVQPNSYDLRLGNEFRVFENHNSGVIDPKKRDLTEEIEIEPGDGF
ILPPGEFYLARTLEYVRLPDDLVAFLEGRSSLARLGLFVHTTAGVIDPGFEGRITLELSNTGPLPIKLYP
GMRIAQLVFFRLSGPAERPYGRGGKYQGQRGVTLSRIFKD
>gnl|CDD|440482 COG0718, YbaB, DNA-binding nucleoid-associated protein YbaB/EfbC [Transcription]
NMGGLMKQAQKMQEKMQEAQEELAELEVEGESGGGLVKVTVNGKGEVKSIEIDPSLLDPEDKEMLEDLIV
AAVNDALRKAEELAQEEMGKLTGGLNLPGL
>gnl|CDD|440483 COG0719, SufB, Fe-S cluster assembly scaffold protein SufB [Posttranslational modification, protein turnover, chaperones]
KLGLPTRRDEEWKYTDLSPLDLDDFAYAPKAVEVPEEIKATLPEAEAGRLVFVDGVFVAELSDELAPKGV
IFTSLSEALREHPELVKKYLGKVVPPDDDKFAALNTALWSDGVFIYVPKGVKVEKPLQLYFRINAEGTGQ
FERTLIVAEEGAEVTYIEGCTAPGDEASLHNAVVEIVVGDNARLRYSTVQNWSGNAYHFVTKRARVGRDA
RYEWTTGSLGSKLTRNYPSVILNGEGAEAELNGVALAGGGQHADTGTKVIHAAPNTTSRILSKGILDDRA
RGVFRGKIKVAKGAQKTDAYQSNRNLLLSDKARADTKPELEIYADDVKCSHGATVGQIDEEQLFYLRSRG
ISEEEARALLVNGFAAEVIEELPDEELREELNRLIELKLEGSV
>gnl|CDD|440484 COG0720, QueD, 6-pyruvoyl-tetrahydropterin synthase [Coenzyme transport and metabolism]. 6-pyruvoyl-tetrahydropterin synthase is part of the Pathway/BioSystem: tRNA modification
MYRITKEFRFSAAHRLPGHDGKCGRLHGHNYRVEVTVEGEELDETGMVVDFGDLKAALKEVIDRLDHRFL
NELPDLEGLNPTAENLARWIWDRLAPRLPGGVRLLRVRVYETPTNWAEYEGEL
>gnl|CDD|440485 COG0721, GatC, Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and biogenesis]. Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MSITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTES
LDREEALANAPETEDGYFKVPKVIE
>gnl|CDD|440486 COG0722, AroG1, 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase [Amino acid transport and metabolism]. 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
MMDQTDDLRIREIKPLITPAELKEELPLSEAAAETVAESRQAIRDILHGKDDRLLVVVGPCSIHDPDAAL
EYARRLKALAEELSDDLLIVMRVYFEKPRTTVGWKGLINDPHLDGSFDINKGLRLARKLLLDINELGLPA
ATEFLDPITPQYIADLISWGAIGARTTESQTHRELASGLSCPVGFKNGTDGNLQIAIDAIRAASAPHHFL
GIDKDGQSAIVQTTGNPDCHVILRGGKGGPNYDAESVAAAEEALAKAGLPPRLMVDCSHANSGKDHRRQP
EVAEDVAAQIAAGNRSIIGVMLESHLVEGNQDLPPGSPLVYGQSITDACIGWETTEELLRELAEAVRARR
A
>gnl|CDD|440487 COG0723, QcrA/PetC, Rieske Fe-S protein [Energy production and conversion]
AAAPVFVSPSAKAKAGAPVEVDLSDLPPGEGKVVEWRGKPVFVVRTPVRGDGEIVAVSAICTHLGCPVTW
NADEGGFDCPCHGSRFDPDGRVLKGPAPRPLPVPPLEVDDDKLLIGVG
>gnl|CDD|440488 COG0724, RRM, RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis]
SMKIYVGNLPYSVTEEDLRELFSEYGEVTSVKLITDRETGRSRGFGFVEMPDDEEAQAAIEALNGAELMG
RTLKVNEARPREERP
>gnl|CDD|440489 COG0725, ModA, ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]. ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis
RRLLLLALLLLALLLAGASAAAAAAELTVFAAASLKEALEELAAAFEKEHPGVKVELSFGGSGALARQIE
QGAPADVFISADEKYMDKLAKKGLILAGSRVVFATNRLVLAVPKGNPADISSLEDLAKPGVRIAIGDPKT
VPYGKYAKEALEKAGLWDALKPKLVLGENVRQVLAYVESGEADAGIVYLSDALAAKGVLVVVELPAELYA
PIVYPAAVLKGAKNPEAAKAFLDFLLSPEAQAILEKYGFEPPK
>gnl|CDD|440490 COG0726, CDA1, Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]
LVLSLDELLPALRWGPLPKKAVALTFDDGPREGTPRLLDLLKKYGVKATFFVVGSAVERHPELVREIAAA
GHEIGNHTYTHPDLTKLSEEEERAEIARAKEALEELTGKRPRGFRPPYGRYSPETLDLLAELGYRYILWD
SVDSDDWPYPSADAIVDRVLKYLKPGSIRPGTVEALPRLLDYLKAKGYRFVTLAE
>gnl|CDD|440491 COG0727, YkgJ, Uncharacterized protein YkgJ, contains CxxCxxCC motif [General function prediction only]
MSKIAELRFPCLGCGACCRGFRVSLTPAEIGRLAKHLGLSPEEFLERYLRYVLKGTEDGRCVFLDGETRR
CSIYEVRPSACREFPFVFEDGFGKTLKGDEACPGARARHGLERLKRELRL
>gnl|CDD|440492 COG0728, MurJ, Lipid II flippase MurJ/MviN (peptidoglycan biosynthesis) [Cell wall/membrane/envelope biogenesis]
LRAALIVAIGTLLSRILGFVRDILIAAAFGAGAVADAFFVAFRIPNLLRRLFAEGALSAAFVPVLAEALE
KEGEEEARRFASRVLTLLLLVLLVLTLLGILFAPLLVKLLAPGFDPEKFALAVALTRIMFPYILFIGLSA
LLGGVLNARGRFAAPALAPVLLNLVIIAGLLLLAPLFGPGIYALAWGVLLGGVLQLLIQLPALRRLGLRL
RPRFDLRDPGVRRVLKLMLPALLGVSVSQINLLVDTILASFLPEGSVSALYYADRLYQLPLGLFGVAIGT
ALLPRLSRAAAAGDLEEFRRTLSRGLRLVLLLTLPAAVGLIVLAEPIVRLLFERGAFTAEDTALTALALA
AYALGLPAFALVKVLARAFYARQDTRTPVRIAVIAVVVNIVLNLLLVPPLGHAGLALATSLSALVNALLL
LVLLRRRLGGLPLRGILRTLLKLLLASLVMGAVLWLLLRLLGDWLGGGLLGRLLALALLILVGAAVYFAL
LLLLGVRLRDLLR
>gnl|CDD|440493 COG0729, TamA, Outer membrane translocation and assembly module TamA [Cell wall/membrane/envelope biogenesis]
LLLLLALLLAAPAAAAPYEVEIDGLDGELRDNLRAHLSLLRLRDEPDLDPAELRRLARADPERIRAALRA
EGYYSPTVTIRLDGRDGPWTVTITVDPGPPVRIGKVDIELLGEAAQDPARRKLLAAWPLKPGDPLRHGAY
EAAKSALLDALRERGYPDARFTQSRAEVDPATNTADVTLTVDSGPRYRFGEITVEGLSRVPEDFLRRLAP
FKPGEPYSPDKLLELQQRLQSTGYFSSVRVTPDEDPAPDGTVPVTVTLTERKRRRIGFGLGYSTDTGPRL
SAGWEHRNLFGRGHRLRLELELSQPEQSLSADYRIPPLFPLGQYLSLGAGLEREDTDDYDSRSLTLGAGR
TRRLSDGWTRSLGLRLLYERFTDGDDDRTYTLLSPGLSWTRDRRDDPLDPTRGYRLSLELGPGSKLLGSD
TSFLRLYARGSWYRPLGERHRLAGRAELGAILGADFDDVPPSLRFFAGGDGSVRGYGYQSLGPRDGDGDV
IGGRSLAVGSLEYRYRVTENWGLAVFVDAGNAFNDFPFSDLKVGAGLGLRWYSPVGPIRLDLAYPLNDRD
DSSFRLYISLGQAF
>gnl|CDD|440494 COG0730, TauE, Sulfite exporter TauE/SafE/YfcA and related permeases, UPF0721 family [Inorganic ion transport and metabolism]
LMLLLLLLLAGFLAGFLDGLLGVGGGLITVPALLLFGLPPAVAVGTSLLAVVFTSLSGALAHRRRGNVDW
RLLLPLALGALIGALLGALLLLLLPADVLKLLFGVLLLLVALLMLLRPKPGAEPERRLPRRSPLLLLLLG
FVIGFLSGLFGIGGGFLLVPALVLLLGLPLKRAVATSLALIFVTALAGLIGFALLGYVDWPLALLLALGS
LLGAYLGARLARRLPPKLLRRLFAVVLLLVGLKLLLKALG
>gnl|CDD|440495 COG0731, Tyw1, Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal structure and biogenesis]. Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily is part of the Pathway/BioSystem: tRNA modification
MRRGGLCYKYVYGPVPSRRLGRSLGINLIPNKTCNFDCVYCQRGRTTDLTRERREFDDPEEILEELIEFL
RKLPEEAREPDHITFSGSGEPTLYPNLGELIEEIKKLRGIKTALLTNGSLLHRPEVREELLKADQVYPSL
DAADEETFRKINRPHPGLSWERIIEGLELFRKLYKGRTVIETMLVKGINDSEEELEAYAELIKRINPDFV
ELKTYMRPPALSRVNMPSHEELEEFAERLAELGYEVVS
>gnl|CDD|440496 COG0732, HsdS, Restriction endonuclease S subunit [Defense mechanisms]
TKKYYLRSPSFREYLRSLATGSTQPNLNKKDLKKLPIPLPPLEEQKRIVEILDSLFDKIAALEKEIEKLK
ELRDALLPKLFTGELRVR
>gnl|CDD|440497 COG0733, YocR, Na+-dependent transporter, SNF family [General function prediction only]
ASSKREQWSSRLGFILAAAGSAVGLGNIWRFPYVAGENGGGAFLLPYLLALLLIGIPLLIAEFAIGRRGR
KSPVGAFRKLAPGKKWEWIGWLGVLGAFLILSYYSVVAGWVLAYLFKSLTGAFGGLDAEDAGAFFGAFLS
SPGEVLIWHLLFLLLTALIVARGVQKGIEKASKILMPLLFVLLIILVIRALTLPGAAEGLKFLFTPDFSK
LTDPEVWLAALGQAFFSLSLGMGIMITYGSYLPKDEDLPRSALIVALLDTLVALLAGLAIFPAVFAFGLE
PAAGPGLAFVTLPAVFAQMPGGRLFGVLFFLLLLFAALTSAISLLEVVVAALIDKFGLSRKKATLIVGLL
IFLLGIPSALSFNVSVTIGLTFFDLVDFLVSNILLPLGGLLIAIFVGWVLGKEKLREELNAGSDIKLGKW
WRFLIRYVAPVALLIIFLNGLGLL
>gnl|CDD|440498 COG0735, Fur, Fe2+ or Zn2+ uptake regulation protein Fur/Zur [Inorganic ion transport and metabolism]
MEALEEAEELLREAGLRLTPQRLAILELLLESDRHLSAEEIYEALRKKGPSISLATVYRTLDLLVEAGLV
HRIEFGGGKARYELNEGDHHHHLICTKCGKVIELDDDEIEELLEELAEPHGFEIESHELEIYGLCPDCQK
>gnl|CDD|440499 COG0736, AcpS, Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism]
GIGIDIVEIARIERALERHGERFLERVFTPAERAYCQSRKRPAEFLAGRFAAKEAVSKALGTGIGKGVSW
RDIEVLNDPSGKPTVRLSGRAAELAAELGITRIHLSISHERDYAVAFVILEA
>gnl|CDD|440500 COG0737, UshA, 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms]
ATVTLTILHTNDLHGHLEPYDYFDDKYGKAGGLARLATLIKQLRAENPNTLLLDAGDTIQGSPLSTLTKG
EPMIEAMNALGYDAATLGNHEFDYGLDVLLELLDGANFPVLSANVYDKDTGEPLFKPYTIKEVGGVKVGV
IGLTTPDTPTWSSPGNIGGLTFTDPVEAAQKYVDELRAEGADVVVLLSHLGLDGEDRELAKEVPGIDVIL
GGHTHTLLPEPVVVNGGTLIVQAGSYGKYLGRLDLTLDDDGGKVVSVSAELIPVDDDLVPPDPEVAALVD
EYRAKLEALLNEVVGTTEVPLDGYRAFVRGGESPLGNLIADAQLEATGADIALTNGGGIRADLPAGPITY
GDVYTVLPFGNTLVVVELTGAQLKEALEQSASNIFPGDGFGGNFLQVSGLTYTIDPSKPAGSRITDLTVN
GKPLDPDKTYRVATNDYLASGGDGYPMFKGGKDVPDTGPTLRDVLADYLKA
>gnl|CDD|440501 COG0738, FucP, Fucose permease [Carbohydrate transport and metabolism]
MSKKNYRRALIAIYLLFFLWGFATALWGPLIPALKDAFGLSDAQAGLLLFAFFLGYLLASLPAGRLIDRF
GYKRGLLLGLLLMALGLLLFALAPSYPLLLLALFLLGLGLGLLDVAANPYVAALGPETAASRLNLLHAFF
SLGALLGPLLGGLLILLGLSLSWHLPYLILAVLLLLLALLFLRSKLPEIEEEEEEAAGSAASLKSLLKNP
RLLLGGLAIFLYVGAEGAIGDWLPLYLKDVLGLSEATAALGLSLFWGGMTIGRFLGGFLLKRFGPVRLLR
LSALLAAVGLLLALLAPGPWLALIGLALVGLGLSLMFPTIFSLALDGLGKRTAAAVSAVLIMGIVGGAIG
PPLIGFLADAFGLRAAFLVPLVCYLLILLLALALKRKRRKK
>gnl|CDD|440502 COG0739, NlpD, Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis]
AALALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGS
GAWPVKGRITSGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYT
TLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLPA
>gnl|CDD|440503 COG0740, ClpP, ATP-dependent protease ClpP, protease subunit [Posttranslational modification, protein turnover, chaperones]
YLVPMVVEQTPRGERAYDIYSRLLKERIIFLGGEIDDHVANLIIAQLLFLEAEDPDKDILLYINSPGGSV
TAGLAIYDTMQFIKPDVSTICLGQAASMGAFLLAAGTKGKRFALPNARIMIHQPSGGAQGQASDIEIQAR
EILKMRERLNEILAEHTGQPLEKIEKDTDRDTWMTAEEAVEYGLIDEVIESRKE
>gnl|CDD|440504 COG0741, MltE, Soluble lytic murein transglycosylase or regulatory protein s (may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis]
AAAAAAAAAALALAASAAAALALALLAAAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAAL
AAADALAAFAAIAALAAELLALAALLLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAG
ARGLMQLMPATARRLGLKLGLGPSPDDLFDPETNIRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRW
LRRNGDRDGEIIPYAETRNYVKKVLANYAIYRAG
>gnl|CDD|440505 COG0742, RsmD, 16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]. 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification
MRIIGGKARGRKLKVPKGPGTRPTTDRVREALFNILGPDIEGARVLDLFAGSGALGLEALSRGAASVVFV
EKDRKAAAVIRKNLEKLGLEDRARVIRGDALRFLKRLAGEPFDLVFLDPPYAKGLLEKALELLAENGLLA
PGGLIVVEHSKREELPELPAGLELLKERKYGDTRLSFYRREEE
>gnl|CDD|440506 COG0743, Dxr, 1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]. 1-deoxy-D-xylulose 5-phosphate reductoisomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
MKRIAILGSTGSIGTQTLDVIRRHPDRFRVVALAAGSNVELLAEQAREFRPEYVVVADEAAAEELREALA
GSGIEVLAGEEALIEVAALPEVDVVMAAIVGAAGLLPTLAAIRAGKRIALANKESLVVAGELVMAAAKEH
GAQLLPVDSEHSAIFQCLPGEDREGVERIILTASGGPFRGRPREELANVTPEQALAHPNWSMGRKITIDS
ATMMNKGLEVIEAHWLFDVPPDQIEVVVHPQSIIHSMVEFVDGSVLAQLGPPDMRLPIAYALAYPERIPS
GVPPLDLAKLGTLTFEPPDEERFPCLRLAYEALRAGGTAPAVLNAANEVAVAAFLAGRIGFLDIADVVEK
VLERHPPIAPPSLEDVLEADAWARRRARELIARLA
>gnl|CDD|440507 COG0744, MrcB, Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis]
MAKPRRGKRLLRRLLGLLLLLLAVLVLAALAGLVALYVADLPDPEELEDLALPQTSTIYDRDGTLIATLG
DENREWVPLDQIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLFLS
NERTLSRKLKEALLALKLERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGL
VKAPSYYDPYRNPEAAKERRNLVLDRMVEQGYITQAEADAAKAEPLTLVPPPNGAAAGKYPYFVDYVRRE
LEELLGEDDLYRGGLKIYTTLDPKLQKAAEKAVKNVLPEGKPGGLQAALVVVDPKTGEVLAMVGGRDYGK
SQFNRATQAKRQPGSTFKPFVYAAALEQGYTPATTVDDEPVTFPGGGWSPKNYDGRYRGPVTLREALANS
LNTPAVRLAQEVGLDKVVDTARRLGITSPLDPNPSLALGTSEVSPLEMASAYATFANGGVYVEPHAITKV
TDADGKVLYEAKPKCEQVISPEVAYLMTDMLQDVVTSGTGRAARLPGRPVAGKTGTTNDNRDAWFVGYTP
QLVTAVWVGNDDNSPMGYVTGGSLPAPIWRDFMEAALEGLPVEDFPKPSGVVRIDEPSPTPSGTEPTETS
>gnl|CDD|440508 COG0745, OmpR, DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription]
MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR
PSDIPIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVLRVGDLLDLAAREVTR
DGEPVELTPKEFRLLELLMRNPGRVVSREQLLEEVWGYDYGDDRTVDVHISRLRKKLEDDLIET
>gnl|CDD|440509 COG0746, MobA, Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]. Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis
MTMPITGVILAGGRSRRMGQDKALLPLGGRPLLERVLERLRPQVDEVVIVANRPERYAALGVPVVPDDPP
GAGPLAGILAALEAAPAEWVLVLACDMPFLPPDLVRRLLEALEEGADAVVPRSGGRLEPLFALYRRSLLP
ALEAALAEGERSLRALLERLDVVYVPFEDLDDAFFNVNTPEDLARAEE
>gnl|CDD|440510 COG0747, DdpA, ABC-type transport system, periplasmic component [Amino acid transport and metabolism]
MDPALSTDAASANVASLVYEGLVRYDPDGELVPDLAESWEVSDDGKTYTFTLRDGVKFHDGTPLTAEDVV
FSLERLLDPDSGSPGAGLLANIESVEAVDDYTVVITLKEPYPPFLYLLASPGAAIVPKHALEKVGDDFNT
NPVGTGPYKLVSWVPGQRIVLERNPDYWGGKPKLDRVVFRVIPDAATRVAALQSGEVDIAEGLPPDDLAR
LKADPGLKVVTGPGLGTTYLGFNTNKPPFDDVRVRQALAYAIDREAIIDAVLNGLGTPANGPIPPGSPGY
DDDLEPYPYDPEKAKALLAEAGYPDGLELTLLTPGGPDREDIAEAIQAQLAKIGIKVELETLDWATYLDR
LRAGDFDLALLGWGGDYPDPDNFLSSLFGSDGIGGSNYSGYSNPELDALLDEARAETDPAERKALYAEAQ
KILAEDAPYIPLYQPPQLYAVRKRVKGVEPNPFGLPDLADVSLA
>gnl|CDD|440511 COG0748, HugZ, Putative heme iron utilization protein, contains PNPOx domain [Inorganic ion transport and metabolism]
DEEADEEAAEEARTLLRSARSGALATLDADGYPFASYAPFALDDDGSPYILISGLAEHTRNLLADPRASL
LLIEDESKAGDPLARPRLTLQGRAERVEDSEEWEAARARYLARFPKAALYADLPDFSLFRLTPERGRLVG
GFGRAYWLSGEDLLGADAAEAGAVEHMNDDHAAGHPDAAWRMTGIDPEGFDLRAGDRVLRLPFPEPVTDA
GELRAALVALA
>gnl|CDD|440512 COG0749, PolA, DNA polymerase I, 3'-5' exonuclease and polymerase domains [Replication, recombination and repair]
AGLVAFDTETTSLDPMDAELVGISFAVEPGEAAYIPLAHGAPEQLDLDEVLAALKPLLEDPAIPKIGQNL
KYDLHVLARYGIELAGVAFDTMLASYLLNPGRRRHGLDDLAERYLGHETISYEELAGKGKKQLTFDQVPL
EEAAEYAAEDADITLRLHEVLKPELEEEGLLKLYEEIELPLVPVLARMERNGILVDRELLAELSAELAKR
LAELEQEIYELAGEEFNLNSPKQLGEILFEKLGLPVGKKTKTGYSTDAEVLEKLAEDHPIPALILEYRQL
SKLKSTYVDALPKLINPDTGRIHTSFNQTVTATGRLSSSDPNLQNIPIRTEEGRRIRKAFVAPEGYVLLS
ADYSQIELRILAHLSGDEGLIEAFREGEDIHAATAAEVFGVPLEEVTSEQRRRAKAINFGIIYGMSAFGL
ARQLGISRKEAKEYIDRYFERYPGVKDYMEETVEEAREKGYVETLFGRRRYLPDINSSNRNRRSFAERAA
INAPIQGSAADIIKLAMIRVDRALKEEGLKSRMLLQVHDELVFEVPEDELEEVKELVKEVMENAVELSVP
LVVDVGVGKNWDEAH
>gnl|CDD|440513 COG0750, RseP, Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription]
MSFLLTILAFILVLGVLVFVHELGHFLVARLFGVKVEEFSIGFGPKLFSKKRGETEYGIRAIPLGGYVKM
AGMDPESEVAPEDDPRAFNSKPVWQRLIIVLAGPLANFLLAIVLFAVLFMTVGVPVLTPPVVGEVVPGSP
AAKAGLQPGDRIVAINGQPVTSWDDLVDIIRASPGKPLTLTVERDGEELTLTVTPRLVEEDGVGRIGVSP
SGEVVTVRYGPLEALGAGVKETWDMIVLTLKGLGKLITGKVSAKNLSGPIGIAGIAGEAASSGLASFLSF
LALLSINLGVLNLLPIPALDGGHLLFLLIEAIRGRPVSEKVQEPIQRIGFALLLGLMVFATYNDIVRLF
>gnl|CDD|440514 COG0751, GlyS, Glycyl-tRNA synthetase, beta subunit [Translation, ribosomal structure and biogenesis]. Glycyl-tRNA synthetase, beta subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MMKDLLLEIGTEELPAKFLPKLLEQLAELLAAGLKEARLSFGEVEVYATPRRLAVLVEGLAEKQPDREEE
VKGPPVKAAFDADGNPTKAALGFARSQGVDVDDLERRETDKGEYLFARKTIKGRPTAELLPEILPEAIAK
LPFPKSMRWGDGDVRFVRPVRWLVALLGDEVVPFEILGLKSGRTTRGHRFLGPGPIEIASADDYEETLRE
GYVIADFEERRELIREQLEAAAAELGGTADIDEDLLDEVTNLVEWPTALLGSFDEEFLELPQEVLITTMK
EHQRYFPVLDADGKLLPYFITVSNGESKDPENVIAGNERVLRARLADAKFFYEEDLKKPLEDRVEKLKKV
VFQEKLGTLADKVERIEALAAAIAEQLGLDEEAALAERAALLAKADLVTQMVGEFPELQGIMGRYYALHD
GEPEEVALAIEEHYLPRFAGDALPSTLVGAIVALADKLDTLVGIFGIGLIPTGSKDPFALRRAALGILRI
LIEKGLPLDLSELLDAALALYGEQLDAEEVVEEVLDFFLERLRNLLQEEGISYDVVDAVLALGPDDPLDA
DARAKALAAFRALPEFEALAAANKRVANILKKAEGEVSAEVDPALLEEPAEKALYEALEELEPEVEALLA
AGDYEEALAALAALRPPVDAFFDNVMVMAEDEALRANRLALLARLRALFLRVADISKLVK
>gnl|CDD|440515 COG0752, GlyQ, Glycyl-tRNA synthetase, alpha subunit [Translation, ribosomal structure and biogenesis]. Glycyl-tRNA synthetase, alpha subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MTFQDIILTLQKYWAEQGCVILQPYDMEVGAGTFHPATFLRALGPEPWNVAYVQPSRRPTDGRYGENPNR
LQHYYQFQVILKPSPDNIQELYLGSLEALGIDPKEHDIRFVEDNWESPTLGAWGLGWEVWLDGMEITQFT
YFQQVGGIDCDPVSGEITYGLERLAMYLQGVDNVYDLVWNDGVTYGDVFLQNEVEQSAYNFEYADVEMLF
RLFDDYEAEAKRLLEAGLPLPAYDYVLKASHTFNLLDARGAISVTERASYILRVRNLARAVAEAYLEQRE
ELG
>gnl|CDD|440516 COG0753, KatE, Catalase [Inorganic ion transport and metabolism]
GQYADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFE
VTEDISKYTKAKFFQEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIR
DAIKFPDFIHAQKRDPDTNLPQHDTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAE
GERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDP
LDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVPGIDFSPDKMLQGRLFSYADTQRYRL
GPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSLGGPREDPGFKEPPLKVDGDKVRYRSESDD
HFSQAGLLYRSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVDPELGARVAEALGLDLPEAKAL
>gnl|CDD|440517 COG0754, Gsp, Glutathionylspermidine synthase, CHAP domain [Amino acid transport and metabolism]
MRRITIPPRPDWRAKAEELGFVFHTLDGEPYWDESAYYVFSLAEIEELEEATNELHQMCLEAVDHVVKDE
RLLARLGIPEALWPLIRESWERRDPSLYGRFDLAYDGRGPAKLLEYNADTPTSLYEAAVVQWLWLEDQGL
GLPPGADQFNSLHEALVERWKELAARLPGGPLHFACDEDSPEDRGTVAYLQDTAREAGLDTKFIYIEDIG
WDEEGRFVDLDGRPIEFLFKLYPWEWMLREEFGLALLRAGVRWIEPAWKLILSNKAILPLLWELFPNHPN
LLPAYFEPDPGLLTGYVRKPLFGREGANISIVDPGGELEETDGPYGEEGFIYQAYAPLPKFDGNYPVIGS
WVVGDEAAGIGIREDDGLITDDLSRFVPHIILD
>gnl|CDD|440518 COG0755, CcmC, ABC-type transport system involved in cytochrome c biogenesis, permease component [Posttranslational modification, protein turnover, chaperones]
LYLLLSGRAPLSNLYESLLFFAWATVLLWLVFERRDLRLLGAFVLLLALLLLAFLFADPEITPLVPALDS
RWLYIHVPAAWLSYGAFALAAVLSLLYLVWRRFLKKLARPSLKLLDRLAYAAAPIGFPFLTLGLITGAIW
AKPAWGRYWGWDPKETWALILWLLYAGYLHLRLAIGWRGRAAAVLAIVGFVNVPIIYFGVNWWLSGLHSY
AGL
>gnl|CDD|440519 COG0756, Dut, dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]. dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis
KVKIKRLDEDAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKH
GITLLNSPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGS
TGR
>gnl|CDD|440520 COG0757, AroQ, 3-dehydroquinate dehydratase [Amino acid transport and metabolism]. 3-dehydroquinate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGVDG
IIINPGAYTHTSVALRDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALA
ELLSK
>gnl|CDD|440521 COG0758, Smf, Predicted Rossmann fold nucleotide-binding protein DprA/Smf involved in DNA uptake [Replication, recombination and repair]
SDERLAWLALSRVPGVGPVTLRRLLAHFGSAEAALEALPSELARLGLGEKAAEAIRARPDLADAERELEW
LERLGIRLLTPGDPDYPALLREIPDPPPLLYVRGDLDLLDRPAVAIVGSRNASAYGRRVARELAAELAEA
GFTVVSGLARGIDAAAHRGALEAGGKTIAVLGTGLDRIYPAEHRKLAERIAENGALVSEFPPGTPPLRGN
FPRRNRIIAGLSLGVLVVEAAERSGSLITARLALEQGREVFAVPGSITSPRSAGCNRLIRQGAKLVTSAE
DILEELGWLLEALPQEAPAPLDELDPEEKRVLDALGPEPVSIDELARRTGLPVAEVLAALLELELKGLVE
RLPGGRYSRL
>gnl|CDD|440522 COG0759, YidD, Membrane-anchored protein YidD, putatitve component of membrane protein insertase Oxa1/YidC/SpoIIIJ [Cell wall/membrane/envelope biogenesis]
KSLMKRLLIGLIRFYQRFISPLLGPRCRFYPTCSEYALEAIERHGLLKGSWLTLKRILRCHPWHPGGYDP
V
>gnl|CDD|440523 COG0760, SurA, Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones]
DQFDSPEEVRASHILVKVPPSEDRAKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRG
QLVPEFEEAAFALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELRKK
AKI
>gnl|CDD|440524 COG0761, IspH, 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase IspH [Lipid transport and metabolism]. 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase IspH is part of the Pathway/BioSystem: Isoprenoid biosynthesis
PMKILLAKPRGFCAGVDRAIEIVERALEKYGAPVYVLGEIVHNPQVVERLEAKGVVFVEELDEVPDGATV
IFRAHGVSPEVREEAEERGLKVIDATCPLVTKVHKEVRRLAKEGYTIVIIGHKGHPEVEGTMGQAPGKVV
VVESPEDVEALPVRDPEKLAVVSQTTLSVDDTAEIVEALKERFPEIRGPVKDTICYATQNRQDAVKELAK
EVDLMLVVGGKNSSNTNRLVEVAKEAGPPAYLIETAEELDPEWLEGVKTVGITAGASTPEWLVEEVIDRL
RELGPEEVE
>gnl|CDD|440525 COG0762, Ycf19, Cytochrome b6 maturation protein CCB3/Ycf19 and related maturases, YggT family [Posttranslational modification, protein turnover, chaperones]
MLALLGLLSLLLNIYFWLIIIRAILSWVPPFGYNPIGRFLYQLTEPLLRPIRRIIPPLGGIDLSPIVAIL
ILQLLQRLLLGLLA
>gnl|CDD|440526 COG0763, LpxB, Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]. Lipid A disaccharide synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis
MKIFIVAGEASGDLLGANLIRALKARDPDAEFVGIGGPRMQAAGLESLFDMEELSVMGFVEVLKHLPRLL
RLRRQLKRAILAEKPDVVILIDYPGFNLRLAKRLKKAGIPVVYYVSPQVWAWRPGRVKKIARAVDHVLAI
FPFEPEFYRKHGVPVTFVGHPLADEIPLEPDRAAARARLGLDPDKPVIALLPGSRRSEIKRLLPVFLEAA
KLLAARRPDLQFVVPLAPSLRRELIEAALADWPLPVTLVDGQTYDAMAAADAALVASGTATLEAALLGVP
MVVAYKVSPLTYWIAKRLVKVPYISLPNLLAGREVVPELLQDDATPENLAAALLRLLDDPAARAAQLAAF
AELRQLLGEGGASERAAEAILELLEKRA
>gnl|CDD|440527 COG0764, FabA, 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and metabolism]. 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase is part of the Pathway/BioSystem: Fatty acid biosynthesis
IEEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLL
KSEGLEGKGRLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVE
K
>gnl|CDD|440528 COG0765, HisM, ABC-type amino acid transport system, permease component [Amino acid transport and metabolism]
MFFDFSVLLDYLPLLLEGLLVTLLLTVLAIVLGLVLGLLLALARLSPNPVLRWLATAYVEFFRGTPLLVQ
LFFIYFGLPLLGIDLSPFVAAVIALTLNSAAYLAEIVRAGIQSVPKGQWEAARALGLSRWQTMRRIILPQ
ALRIILPPLGNEFISLLKDTSLVSVIGVPELTRAAQQIASRTFRPFEVYLVAALIYLVLTLPLSLLARRL
ERRLARGR
>gnl|CDD|440529 COG0766, MurA, UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]. UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis
MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGG
TLTIDASNINSTEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEI
EHGYIEARAGRLKGARIYLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAG
TDTITIEGVEKLHGAEHTVIPDRIEAGTFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDG
IRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGTSVITETVFENRFMHVDELNRMGADIKLDGH
TAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRGYENLEEKLRALGADIERV
>gnl|CDD|440530 COG0767, MlaE, Permease subunit MlaE of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis]
LGRAVLRFLAFLGRLLLFLARVLRRLFRPRFRWRELLRQIYFVGVGSLPIVALTGFFIGAVLALQGAYQL
RQFGAESFVGDLVALSLVRELGPLLTALLVAGRVGSAIAAEIGTMRVTEQIDALEVMGIDPIRYLVLPRV
LAGVIALPLLTILADVVGILGGYLVAVLLLGISPGAYLSSLQDFVDPSDVLVGLIKALVFGFIIALIGCY
QGLNAKGGAEGVGRATTRAVVTSIVLILVLDFLLTVLFF
>gnl|CDD|440531 COG0768, FtsI, Cell division protein FtsI, peptidoglycan transpeptidase (Penicillin-binding protein 2) [Cell cycle control, cell division, chromosome partitioning, Cell wall/membrane/envelope biogenesis]
MKRKKEKRLFRRRLLLLFLLVLLLFLLLVGRLFYLQVVEGDEYAELAEENRIRTVPIPAPRGLIYDRNGN
VLATNVPVYSLYADPEEVKDPEETAEKLAKLLGLDPEELRKKLKKKSRFPVYLKRNLSPEEAARIRALKL
PGVYVEAEYKRYYPYGELAAHVLGYVGEINGGDGIGKSGLEKAYEDLLRGTPGKRRVEVDARGRVIRDLG
EEKPPVPGKDLVLTIDSDLQKIAEEALKKAVEEYKAKSGAVVVMDPKTGEILAMASYPSFDPNLFVGGPD
EPLRNRAVQGTYEPGSTFKPFTAAAALEEGVITPDTTFDCPGYYRVGGRTIRDWDRGGHGTLTLTEALAK
SSNVGFYKLALRLGIDKLYDYLKKFGLGQKTGIDLPGEASGLLPSPKRWYPGETATMSIGQGLSVTPLQL
AQAYAAIANGGVLVKPHLVKEIVDPDGEVVKEEPEVLRRVISPETAETVREGMEGVVNEPGGTARRAAIP
GYRVAGKTGTAQVVDIGNGGYYKGRHIASFVGFAPADNPRYAVAVVVENPGGGAYGGTVAAPVFREIMEA
YLRLLGPP
>gnl|CDD|440532 COG0769, MurE, UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]. UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
GITYDSRKVKPGDLFVALPGARVDGHDFIAQAIARGAVAVVTEAPGALLAAGVPVIVVPDPRAALALLAA
AFYGHPSQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGLIGTVGNGIGGELIPSSLTTPEALDLQRLL
AEMVDAGVTHVVMEVSSHALDQGRVDGVRFDVAVFTNLTRDHLDYHGTMEAYFAAKARLFDQLGPGGAAV
INADDPYGRRLAAAAPARVITYGLKADADLRATDIELSADGTRFTLVTPGGEVEVRLPLIGRFNVYNALA
AIAAALALGIDLEEILAALEKLKGVPGRMERVDGGQGPTVIVDYAHTPDALENVLEALRPHTKGRLIVVF
GCGGDRDRGKRPLMGEIAARLADVVIVTSDNPRSEDPAAIIADILAGIPGAGKVLVIPDRAEAIRYAIAL
AKPGDVVLIAGKGHETYQIIGGVKIPFDDREVAREALAE
>gnl|CDD|440533 COG0770, MurF, UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]. UDP-N-acetylmuramyl pentapeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
ILLTLAEIAEATGGRLIGDPDLVVTGVSTDSRKIKPGDLFVALKGERFDGHDFVAQALAKGAAAALVSRP
LPADLPLIVVDDTLKALQQLAAAHRARFNIPVIAITGSNGKTTTKEMLAAVLSTKGKVLATPGNFNNEIG
VPLTLLRLPEDHEFAVLEMGMNHPGEIAYLARIARPDIAVITNIGPAHLEGFGSLEGIARAKGEIFEGLP
PGGVAVLNADDPLLAALAERAKARVLTFGLSEDADVRAEDIELDEDGTRFTLHTPGGELEVTLPLPGRHN
VSNALAAAAVALALGLDLEEIAAGLAAFQPVKGRLEVIEGAGGVTLIDDSYNANPDSMKAALDVLAQLPG
GGRRIAVLGDMLELGEESEELHREVGELAAELGIDRLFTVGELARAIAEAAGGERAEHFEDKEELLAALK
ALLRPGDVVLVKGSRGMGLERVVEALKEGAA
>gnl|CDD|440534 COG0771, MurD, UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]. UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
DLKGKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAELEAPGVEVVLGEHPEELLDGADLVV
KSPGIPPDHPLLKAARAAGIPVIGEIELAYRLSPAPIIAITGTNGKTTTTTLIGHILKAAGLRVAVGGNI
GTPLLDLLLEPEPPDVYVLELSSFQLETTPSLRPDVAVILNITPDHLDRHGSMEAYAAAKARIFANQTPD
DYAVLNADDPLTRALAEEAKARVVPFSLKEPLEGGAGLEDGKLVDRASGEELLPVDDLRLPGRHNLENAL
AALAAARALGVPPEAIREALRSFKGLPHRLEFVAEINGVRFINDSKATNPDATLAALESFDGPVVLIAGG
LDKGADFSPLAPAVAERVKAVVLIGEDAEKIAAALAGAGVPVVIVETMEEAVAAAAELARPGDVVLLSPA
CASFDQFKNYEERGDVFKEAVRELA
>gnl|CDD|440535 COG0772, FtsW, Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell cycle control, cell division, chromosome partitioning]
MALGLLLRRLRKIDWLLLLLVLLLLGIGLVMVYSASSALAARKGGDPFYFFKRQLIWLLLGLVLMLVVSR
IDYRRLRRLAYPLYLLGLVLLLLVLLFGTEVNGARRWISLGGFSFQPSEFAKLALILFLASYLSRKRDKL
KDLKGLLPPLLLIGLPVGLILLQPDLGTALVLFAIFLGMLFVAGLPWKYLLGLLLLGVAAAVLLILLKPY
QRARILAFLDPWADPLGAGYQIIQSLIAIGSGGLFGKGLGNGTQKLGYLPEAHTDFIFAVIGEELGFIGA
LLVLLLFLLLIYRGLRIALRARDPFGRLLAAGIASLIFFQAFINIGMVTGLLPVTGVPLPFISYGGSSLL
ANMIALGLLLSISRRRRRAER
>gnl|CDD|440536 COG0773, MurC, UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]. UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis
LDKIMHIHFIGIGGIGMSGLAEILLALGYKVSGSDLAESPMTERLEALGIPVFIGHDAENIDDADLVVVS
SAIPRDNPELVAARERGIPVLSRAEMLAELMRGKRSIAVAGTHGKTTTTSMLAHILEEAGLDPTFLIGGI
LNNFGTNARLGDGDYFVAEADESDGSFLHYSPDIAVVTNIEADHLDIYGDLEAIKEAFHEFARNVPFYGL
LVLCADDPGLRELLPRCGRPVITYGFSEDADYRAENIRIDGGGSTFDVLRRGEELGEVELNLPGRHNVLN
ALAAIAVALELGVDPEAIAEALASFKGVKRRFELKGEVGGVTVIDDYAHHPTEIAATLAAAREKYPDRRL
VAVFQPHRYSRTRDFLDEFAEALSLADEVILLDIYAAREKPIPGVSSEDLAEAIRKRGKDVVYVPDLDEL
VEALAEIARPGDVVLTMGAGDIGGLGEKLLE
>gnl|CDD|440537 COG0774, LpxC, UDP-3-O-acyl-N-acetylglucosamine deacetylase [Cell wall/membrane/envelope biogenesis]. UDP-3-O-acyl-N-acetylglucosamine deacetylase is part of the Pathway/BioSystem: Lipid A biosynthesis
MKQRTLKKPVSLSGVGLHSGKKVTLTLRPAPANTGIVFRRTDLPGQPEIPARADNVVDTRLCTTLGKGGV
RVSTVEHLMAALAGLGIDNALIEIDGPEVPIMDGSAAPFVELIQEAGIVEQDAPRRFIRIKKPVRVEDGD
KWAELLPYDGFRIDFTIDFDHPAIGRQSASLDLSPESFVREIARARTFGFLKDVEALRAAGLALGGSLDN
AIVIDDDGVLNPEGLRFPDEFVRHKILDAIGDLALLGAPLLGHFIAYKSGHALNNALLRALLADPS
>gnl|CDD|440538 COG0775, MtnN, Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB [Nucleotide transport and metabolism, Coenzyme transport and metabolism]. Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB is part of the Pathway/BioSystem: Menaquinone biosynthesis
MTIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDA
VINTGVAGGLDPDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPALFEADPALLEAAKEAAKESGLKV
VTGTIATGDRFVWSAEEKRRLRERFPGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKAPNDFDEF
LEEAAKNAAELLRALLRKLRS
>gnl|CDD|440539 COG0776, HimA, Bacterial nucleoid DNA-binding protein IHF-alpha [Replication, recombination and repair]
MTKSELIEAIAEKTGLSKKDAEAAVDAFLDEITEALAKGERVELRGFGTFSVRKRAARTGRNPKTGEEIK
IPAKKVVKFKPGKELKDAVNGS
>gnl|CDD|440540 COG0777, AccD, Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]. Acetyl-CoA carboxylase beta subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis
MSWFKKLKPKIKTTSKKREVPEGLWTKCPSCGEILYRKELEENLYVCPKCGHHFRISARERLELLLDEGS
FEELDADLVPVDPLKFKDSKKYKDRLKEAQKKTGLKDAVVTGTGTINGIPVVVAVMDFSFMGGSMGSVVG
EKITRAIERAIEKKLPLIIFSASGGARMQEGILSLMQMAKTSAALARLSEAGLPYISVLTDPTTGGVTAS
FAMLGDIIIAEPGALIGFAGPRVIEQTIREKLPEGFQRAEFLLEHGFIDMIVHRKELRDTLARLLALLTK
>gnl|CDD|440541 COG0778, NfnB, Nitroreductase [Energy production and conversion]. Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation
LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEANQEWVA
DAPVLIVVCADPDRSEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEEPVA
LLALGYPAEELNPRPRKPLEEVV
>gnl|CDD|440542 COG0779, RimP, Ribosome maturation factor RimP [Translation, ribosomal structure and biogenesis]
MSGLEERLEELLEPVLEELGLELVDVEVVKEGKRWVLRVYIDKDGGVTLDDCAAVSRALSAVLDVEDPIP
GAYTLEVSSPGLDRPLKKPRDFERFIGRLVKVKLREPIDGRKKFTGRLLGVDDDGVTLEVDGKEVEIPLD
DIAKARLVIEF
>gnl|CDD|440543 COG0780, QueFC, NADPH-dependent 7-cyano-7-deazaguanine reductase QueF, C-terminal domain, T-fold superfamily [Translation, ribosomal structure and biogenesis]. NADPH-dependent 7-cyano-7-deazaguanine reductase QueF, C-terminal domain, T-fold superfamily is part of the Pathway/BioSystem: tRNA modification
MTELDGLCLDGLDEIDPYSPDPALLETFPNPHPGRDYEITLTSPEFTSLCPVTGQPDFATIVIRYVPDKK
CVELKSLKLYLVSFRNHGIFHEQCVNRIFDDLVAACKPRWLRVYARFTPRGGIDINPFRSSGK
>gnl|CDD|440544 COG0781, NusB, Transcription antitermination protein NusB [Transcription]
ELALQALYQVELSGAYANEILEEFLEDEELSEADRAFATELVYGVLRNQEELDALIAPYLKDWPLERLDP
VDRAILRLAAYELLYLDDVPYKVAINEAVELAKKFGTEDSPKFVNGVLDKIAKELRAE
>gnl|CDD|440545 COG0782, GreA, Transcription elongation factor, GreA/GreB family [Transcription]
MMKKNYLTPEGYEKLKAELEELKTVERPEIAEAIAEARAEGDLSENAEYDAAKEEQGFIEGRIRELEKRL
ANAEVIDPSKLDTDKVFFGATVTLEDLEDGEEETYTIVGPDEADPKKGKISIESPLGRALLGKKVGDEVE
VTTPGGEREYEILEIE
>gnl|CDD|440546 COG0783, Dps, DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and metabolism, Defense mechanisms]
KTPIGLDEEAREKVAEALNQLLADLYVLYLKTKNAHWNVKGPNFFSLHELFEELYDELREAIDEIAERIR
ALGGVPPGTLAEFAKLSTIKEEPEGVVDAREMVEALLEDYEALIKTLREAIELADEAGDEGTADLLTDIL
RELEKRAWMLRAHLED
>gnl|CDD|440547 COG0784, CheY, CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms]
PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRR
IRALPRLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA
>gnl|CDD|440548 COG0785, CcdA, Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
MLLSLLLAFLAGLLSFLSPCVLPLLPGYLSYLTGLSRASRRRALLRALLFVLGFSLVFVLLGALASALGS
LLGQYQDLLRIVAGVLLILFGLVLLGLLKIPFLQREARINLRRKAGLLGAFLLGLAFGLGWTPCIGPILG
AILALAATSGSVLRGALLLLAYALGLGLPFLLLALFAGRLLGRLRRLRRHLRW
>gnl|CDD|440549 COG0786, GltS, Na+/glutamate symporter [Amino acid transport and metabolism]
TILLDMFQTLALAILLLLIGRFLRKKVKFLQKLNIPAPVIGGLLFALLGPILLGTGGLEITFDTTLQSLL
MLVFFATIGLGASFKLLKKGGKPLVIFLALAQVLAVLQNVVGVGLALLLGLDPLLGLLAGSISLTGGHGT
AAAWGPTFEDLGIEGATELALAAATFGLVAGGLIGGPLARRLIRKGKLKPSADDDSLPEEVRTGFEDEER
GRKTSIDPLLLHLALILLAMGLGYLLSELLKSLTGLSLPLFVGAMIVGIILRNILDRLGKYKVDDRAIDR
IGGVSLDLFLAMALMSLKLWELADLAGPLLVILVAQVVLMVLFAYFVTFRLMGKDYDAAVIAAGHCGFGL
GATPTAIANMRAVTPRYGPSPKAFLVVPLVGAFFIDIANAPIITLFLNLLK
>gnl|CDD|440550 COG0787, Alr, Alanine racemase [Cell wall/membrane/envelope biogenesis]. Alanine racemase is part of the Pathway/BioSystem: Mureine biosynthesis
SRPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELR
EAGIDAPILVLGGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDTGMNRLGFRPEE
APALAARLAALPGLEVEGIMSHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYP
EAHFDMVRPGIALYGLSPSPEVAADLGLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIG
YADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTDIPDVKVGDEVVLFGEQGITADELAEAAGTIS
YEILTRLGPRVPRVYVGE
>gnl|CDD|440551 COG0788, PurU, Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]. Formyltetrahydrofolate hydrolase is part of the Pathway/BioSystem: Purine biosynthesis
MTTYILTLSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFEAPGLDFDLEALRAAFAPL
AERFGMDWRLHDSDRRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPLAEWFGIPFHHI
PVTKETKAEAEARLLELLEEYDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYER
GVKLIGATAHYVTADLDEGPIIEQDVERVDHRDTPEDLVRKGRDVEKRVLARAVRWHLEDRVLVNGNKTV
VF
>gnl|CDD|440552 COG0789, SoxR, DNA-binding transcriptional regulator, MerR family [Transcription]
IGEVARLTGVSVRTLRYYERIGLLPPPERTEGGYRLYSEEDVERLRFIRRLRELGFSLAEIRELLDLLDD
GEEEVRELLEEHLAELEAQIAELQALRAEL
>gnl|CDD|440553 COG0790, TPR, TPR repeat [General function prediction only]
LALAAAAAAAAAAAAAALAAAAAAAGAAAAAAAAAAAAAALAAAAGAAAAAAAAAAAAAAGGAEAQYNLG
LMYAEGRGVPKDYEKALEWFEKAAEQGDAEAQYNLGLMYEEGLGVPQDYAKALEWYEKAAEQGDADAQYN
LGLLYLNGEGVPKDPAKAAEWYRKAAEQGDADAQYNLGVLYENGRGVPKDPAKALEWYRKAAEQGDADAQ
YNLGRLYLNGEGVEKDLEKALRWLRKAAEQA
>gnl|CDD|440554 COG0791, NlpC, Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis]
ASVASALAAALAAAAAALAAVAAAGALAAADAAVAAALVAAAAAVLAAAALLAGPAAAVAGAAAPAVGSA
GAAAAAAAAKAGSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCSGLVQYVYRQAGI
SLPRTSADQAAAGTPVSRSELQPGDLVFFRTGGGGISHVGIYLGNGKFIHASSSGKGVRISSLDSPYWKS
RYVGARRV
>gnl|CDD|440555 COG0792, YraN, Predicted endonuclease distantly related to archaeal Holliday junction resolvase, YraN/UPF0102 family [Replication, recombination and repair]
RRRELGRRGEDLAARYLERKGYRILARNWRCRGGEIDLIARDGDTLVFVEVKTRRSARFGGPAEAVTPRK
QRRLRRAAEAYLARHPGLADLPVRFDVVAVTGDGREIEHIENAFDA
>gnl|CDD|440556 COG0793, CtpA, C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones]
QLFDEVWRLIRDNYVDEYDDRDLAEGALNGMLGELGDPHSYYLDPEEYEDFQESTSGEFGGLGAELGEED
GKVVVVSVIPGSPAEKAGIKPGDIILAIDGKSVAGLTLDDAVKLLRGKAGTKVTLTIKRPGEGEPITVTL
TRAEIKLPSVEAKLLEGKIGYIRIPSFGENTAEEFKRALKELKKQGAKGLILDLRNNPGGLLDEAVELAD
LFLPKGPIVYTRGRNGKVETYKATPGGALYDGPLVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKG
SVQTVFPLPDGGALKLTTARYYTPSGRSIQGKGVEPDIEVPLTPEDLLKGRDPQLEKALEL
>gnl|CDD|440557 COG0794, GutQ, D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]
MTDAEDILESAREVLEIEAEALAALAERLDESFEKAVELILNCKGRVVVTGMGKSGHIARKIAATLASTG
TPAFFLHPAEASHGDLGMITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVL
DLPVEREACPLNLAPTTSTTATLALGDALAVALLEARGFTAEDFARFHPGGSLGRRLLLRVSDLMMPGVE
PPVVVPDALLEEALKELGMTGVGGGAVVDDGGGLDGDLTDGDLRRRLLDDLDLTDVMTTTMTTPTTPPLA
AAAAAAAAALLIEEIIVVVVVVVVVGVLVGGLLLLLL
>gnl|CDD|440558 COG0795, LptF, Lipopolysaccharide export LptBFGC system, permease protein LptF [Cell wall/membrane/envelope biogenesis, Cell motility]
MKILDRYLLREFLKTFLAVLLVLLALFVLIDLVELLDDAAEGGLPLGLVLLYLLLRLPYFLYLLLPLALL
LAVLLTLGRLARDSELVALRASGVSLWRLLRPVLILALLLALLTFLLSEYVAPWANQQAEELRAEALSRS
DLSLLKPGLFLRDDGNRVIYAESVDPDGKTLRNVFIYEFDDDGRLTSIITAESARFEDDGSWRLEDGTRY
ELDPDGDFRVTRFDEYDLPLPLTPEDLAVLLKKPEELSTSELLEYIEYLKRSGLDAPRYRAELHWRLALP
LAALVMALLAVPLSLRPPRSGGRGLRLLIGILLGFLYYLLLSLAGSLGESGKLPPLLAAWLPNLLFLLLG
LYLLLRA
>gnl|CDD|440559 COG0796, MurI, Glutamate racemase [Cell wall/membrane/envelope biogenesis]. Glutamate racemase is part of the Pathway/BioSystem: Mureine biosynthesis
NAPIGVFDSGVGGLTVLREIRKLLPNEDIIYFGDTARFPYGEKSEEEIRERTLEIVEFLLEQGVKLIVIA
CNTASAAALDALRERYDIPVVGVIPAIKPAAAATRNGRIGVLATPATVKSGAYQRLIARFAPDVEVISQA
CPGLVPLVEEGLLDGPETRALVREYLAPLLAAGIDTLVLGCTHYPLLKPLIQEVLGPGVTLIDSAEAVAR
RVKRLLEEHGLLNPEGAPGTVRFYTTGDPEAFARLARRFLGEPISVEKLDL
>gnl|CDD|440560 COG0797, RlpA, Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane/envelope biogenesis]
LLLLALLLAGASGKPYTVRGKTYYPLAEASGYTETGLASWYGDKFHGRKTASGERYDPNALTAAHKTLPL
GTYVRVTNLENGRSVVVRVNDRGPFVKGRIIDLSYAAARKLGMLGKGVAPVRVEVLGPASLAG
>gnl|CDD|440561 COG0798, ACR3, Arsenite efflux pump ArsB, ACR3 family [Inorganic ion transport and metabolism]
MRKRLSFFERYLTLWIFLAMAAGLLLGYLFPGVFQALASLEVATVNIPIAILLWLMIYPMMAKVDFEELG
KVFRNPKGLGLTLVINWLIKPFLMFALAWLFLPDAPEYIAGLILLGLAPCTAMVIVWTGLAKGDVEYALV
LVALNLLLQVLLFPPYVWLLLGVSDVTVPWGTLALSVLLYVVIPLAAGFLTRRLLLRRKGREWFEERFLP
KLSPISLLGLLLTIVLLFALQGETILENPLDILLIAIPLLIQFAINFALSYLLGRLLGLPYEDAAPLAFT
GASNNFELALAVAIALFGLNSGAALATVVGPLIEVPVMLSLVKVALRTRKWFPKS
>gnl|CDD|440562 COG0799, RsfS, Ribosomal silencing factor RsfS, regulates association of 30S and 50S subunits [Translation, ribosomal structure and biogenesis]
MTMDSEELLKLIAKALDDKKAEDIVVLDVRGLSSIADYFVIASGTSDRQVKAIADEVEEKLKEAGIKPLR
VEGLDEGEWVLLDYGDVVVHIFQPEVREFYNLERLWGDAPRID
>gnl|CDD|440563 COG0800, Eda, 2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]. 2-keto-3-deoxy-6-phosphogluconate aldolase is part of the Pathway/BioSystem: Entner-Doudoroff pathway
SKMELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVGPDALVGAG
TVLTPEQARAAIAAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEALGP
AYLKALKGPLPDVPFMPTGGVSPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWAAITERAREAVAAVRA
ARA
>gnl|CDD|440564 COG0801, FolK, 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (folate biosynthesis) [Coenzyme transport and metabolism]. 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (folate biosynthesis) is part of the Pathway/BioSystem: Folate biosynthesis
RVYLALGSNLGDREANLRAALEALAALPGIRVLAVSSVYETPPVGFTDQPDFLNAVVLLETDLSPEELLD
ALQAIEAELGRVRKERWGPRTLDLDILLYGDLVIDTPRLTLPHPRMHERAFVLVPLAEIAPDLVHPVLGK
TVAELLAALPDQGGV
>gnl|CDD|440565 COG0802, TsaE, tRNA A37 threonylcarbamoyladenosine biosynthesis protein TsaE [Translation, ribosomal structure and biogenesis]. tRNA A37 threonylcarbamoyladenosine biosynthesis protein TsaE is part of the Pathway/BioSystem: tRNA modification
LPSEEETEALGARLAALLKPGDVILLEGDLGAGKTTFVRGLARGLGVTGEVTSPTFTLVNEYELGRLPLY
HFDLYRLEDPEELEDLGLEEYLDGDGVCLIEWPERIEGLLPEDDLEITIEYLGEDGRRITLTAHGPRGER
LLEALA
>gnl|CDD|440566 COG0803, ZnuA, ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and metabolism]
MKRLLLALLLLAALLLAGCSAAASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTP
SDIAKLAKADLVVYNGLGLEGWLDKLLEAAGNPGVPVVDASEGIDLLELEEGHDHGEPDPHVWLDPKNAK
KVAENIADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPGRKLVTSHDAFGYLARAYGLEVV
AIQGISPGSEPSPADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVKVLYLDSLGGPGGPGDTYL
DMMRHN
>gnl|CDD|440567 COG0804, UreC, Urease alpha subunit [Amino acid transport and metabolism]
MAKISRKAYADLYGPTTGDRVRLADTDLFIEVEKDLTTYGDEVKFGGGKVIRDGMGQSQTTRAEGALDLV
ITNAVILDHWGIVKADIGIKDGRIVGIGKAGNPDTMDGVDPDLVIGPGTEVIAGEGLILTAGGIDTHIHF
ICPQQIEEALASGITTMIGGGTGPAEGTNATTCTPGPWNIARMLEAADALPMNIGFLGKGNASSPEALEE
QIRAGACGLKLHEDWGATPAAIDACLSVADEYDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTFHTEGAG
GGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDMLMVCHHLDPSIPEDVAFAESRIRPETIAAEDV
LHDLGAISMMSSDSQAMGRVGEVITRTWQTAHKMKKQRGPLPGDSGRNDNFRVKRYVAKYTINPAIAHGI
SHEVGSVEVGKLADLVLWDPAFFGVKPELVIKGGMIAWAQMGDPNASIPTPQPVHYRPMFGAYGKALAAT
SVTFVSQAALEAGIAERLGLRKRLLPVKNTRNIGKADMVLNDATPDIEVDPETYEVRVDGELLTCEPATE
LPLAQRYFLF
>gnl|CDD|440568 COG0805, TatC, Twin-arginine protein secretion pathway component TatC [Intracellular trafficking, secretion, and vesicular transport]
MSEAEDGEMPLLEHLEELRKRLIRSLIAFLVGFIVGFFFADPIYDFLAAPLKAALPEGVKLIATGPTEPF
FTYLKVALLAGLILALPVILYQLWAFIAPGLYRHERRLALPFVLASVLLFLAGAAFAYFVVLPLAFKFLL
SFAPEGVEPLLDISEYLSFVLKLLLAFGLAFELPVVLVLLNRLGIVTPETLRKKRRYAIVGIFVLAAILT
PPDVISQLLLAIPLILLYELSILIARLVERRRAKREAAE
>gnl|CDD|440569 COG0806, RimM, Ribosomal 30S subunit maturation factor RimM, required for 16S rRNA processing [Translation, ribosomal structure and biogenesis]. Ribosomal 30S subunit maturation factor RimM, required for 16S rRNA processing is part of the Pathway/BioSystem: 16S rRNA modification
MKMEDLVVVGRIVKAHGVKGEVKVKSFTDDPERFFDYGPVFLEDPDGELRPLTVESVRPHKGGLLVKFEG
VDDREAAEALRGAELYVPRDDLPELEEDEFYWHDLIGLEVVDEDGEELGKVTDVLETGANDVLVVKGPGG
KEVLIPFVDEFVPEVDLEAGRIVVDPPEGLLDL
>gnl|CDD|440570 COG0807, RibA, GTP cyclohydrolase II [Coenzyme transport and metabolism]. GTP cyclohydrolase II is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
MLLSSIEEIIEDIRAGKMVILVDDEDRENEGDLIMAAEFVTPEAINFMARHGRGLICLTLTEERCEQLLL
PLMVNNNGTPFGTAFTVSIEAAEGVTTGISAADRARTIQAAVAPDAKPEDLVQPGHIFPLRAQPGGVLVR
AGHTEAAVDLARLAGLEPAGVICEIMNEDGTMARLPDLEEFAKEHGLKIGTIADLIAYRLRNESLVERVA
EARLPTEFGEFRLHAYRDTIDGQEHLALVKGDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKR
IAEEGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRL
LTNNPRKVVGLEGYGLEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD
>gnl|CDD|440571 COG0809, QueA, S-adenosylmethionine:tRNA-ribosyltransferase-isomerase (queuine synthetase) [Translation, ribosomal structure and biogenesis]. S-adenosylmethionine:tRNA-ribosyltransferase-isomerase (queuine synthetase) is part of the Pathway/BioSystem: tRNA modification
KLSDFDFDLPEELIAQYPAEPRDASRLLVLDRKTGEIEHRRFRDLPDYLRPGDLLVFNDTRVIPARLYGR
KETGGKIEVLLLRELDEDLWLALVRPAKKLKPGTKLYFGDGLVAEVLENTEDGGRTLRFLYDGDFLELLE
RLGEMPLPPYIKRKDEEEDRERYQTVYAKEPGAVAAPTAGLHFTPELLERLKAKGVEIAFVTLHVGLGTF
RPVKVEDIEEHKMHSEYYEVPEETAEAINAAKAAGGRVIAVGTTSVRALESAADADGTLKPFSGWTDIFI
YPGYRFKVVDALITNFHLPKSTLLMLVSAFAGRELIMAAYQHAIEEKYRFFSYGDAMLIL
>gnl|CDD|440572 COG0810, TonB, Periplasmic protein TonB, links inner and outer membranes [Cell wall/membrane/envelope biogenesis]
PEEARRRGIEGTVTVRFTIDADGRVTDVEVVKSSGHPLLDEAALRAVRRWRFKPAKQNGKPVRVKTVPIR
>gnl|CDD|440573 COG0811, TolQ, Biopolymer transport protein ExbB/TolQ [Intracellular trafficking, secretion, and vesicular transport]
SLLELFLQGGLVMIPLLLLSVLSWAIIIERLLFLRRARRRARKFLRAFLELWSAGDLDEAIELCEARNSP
LARILAAGLRELKSGGGREAIERALEEAASRELPRLERGLSFLATIGSIAPLLGLLGTVWGMINAFQAIA
AAGQADLAVVAGGISEALITTAAGLAVAIPAVIAYNYFSRRIDRLVAELEEFAEELLAL
>gnl|CDD|440574 COG0812, MurB, UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]. UDP-N-acetylenolpyruvoylglucosamine reductase is part of the Pathway/BioSystem: Mureine biosynthesis
EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLGRLKGI
EVDDGVLVTAGAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTG
EVRTLSAEECGFGYRDSIFKRERYIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNP
PGDSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII
>gnl|CDD|440575 COG0813, DeoD, Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]. Purine-nucleoside phosphorylase is part of the Pathway/BioSystem: Purine salvage
MMTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSI
SIYAYELITEYGVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVE
AAKELGIKVHVGNVFSSDLFYREDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTG
EETTAEERQTTFNDMMEIALEAALKL
>gnl|CDD|440576 COG0814, SdaC, Amino acid permease [Amino acid transport and metabolism]
MSKKAMKWRKSDLGWVLLIAGTAIGAGMLALPIAAGGGGFWPSLLLLLLAWPLMYLSHLLLLEVNLSSPP
GADITTVVEEYLGKGGGILIGLLYFFLLYPLLLAYISGGGNILASFLVNQLGLTIPRWLLSLIFILVLGA
IVWLGTRLVDRVNRILVFPKIIAFLLLSLYLIPHWNLANLLNSALPSYLKYLWLALPVLLTSFGFHPIIP
SLVKYYRKDAKKLRRAILIGSLIPLVIYLFWVFSCLGSLPPEEFAEAKAQNISLLSALANVFNSPLISYL
GPLFAFFAIATSFLGVYLGLFDFLADLFKKKKSKKGRLKTALLTFLPPWIVALLNPSIFILALGYAGPII
AILLFILPALLVWKVRARFPLKYRVPGGKLSLIFVILFGLLAISAQILSLF
>gnl|CDD|440577 COG0815, Lnt, Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]
PFGLWPLAFVALAPLLLLLRGARSPRRAFLLGWLFGLGFFLAGLYWLYVSLHVFGGLPAWLAPLAVLLLA
AYLALFFALAAALARRLRRRGGLLRPLAFAALWVLLEWLRGWLFTGFPWLRLGYSQADFSPLAQLAPLGG
VYGLSFLVVLVNALLALALLRRRRRLAALALALALLLAALRLSPVPWTEPAGEPLRVALVQGNIPQDLKW
DPEQRREILDRYLDLTRELADDGPDLVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRRDGGG
GRYYNSALLLDPDGGILGRYDKHHLVPFGEYVPLRDLLRPLIPFLDLPLGDFSPGTGPPVLDLGGVRVGP
LICYESIFPELVRDAVRAGADLLVNITNDAWFGDSIGPYQHLAIARLRAIETGRPVVRATNTGISAVIDP
DGRVLARLPLFTRGVLVAEVPLRTGLTPYARWGDWPALLLLLLALLLALLLR
>gnl|CDD|440578 COG0816, YqgF, YqgF/RuvX protein, pre-16S rRNA maturation RNase/Holliday junction resolvase/anti-termination factor [Translation, ribosomal structure and biogenesis, Replication, recombination and repair, Transcription]
RMGRILGLDVGTKRIGVAVSDPLGIIATPLETIKRKKGEPDLARLAKLIKEWEVDALVVGLPLNMDGSEG
PRAQRARKFARRLAGRFGLPVELVDERLTTVEAERALIEAGVSRKKRKGVIDQIAAVIILQSYLDS
>gnl|CDD|440579 COG0817, RuvC, Holliday junction resolvasome RuvABC endonuclease subunit RuvC [Replication, recombination and repair]
ILGIDPGLRRTGYGVIEVDGNRLRLVASGVIRTPPKLPLPERLLEIYEGLTELIEEYKPDEVAIEEVFFN
KNPKSALKLGQARGVALLAAAQRGLPVAEYTPLQVKKAVTGYGRADKEQVQAMVKRLLGLDEIPKPDDAA
DALAIAICHAHR
>gnl|CDD|440580 COG0818, DgkA, Diacylglycerol kinase [Lipid transport and metabolism]
KSKKKLRRLIKSFGYALRGLKAAFRTERNFRIHLVLAVLVIPLAFFLGLSAVEWALLILAIGLVLIAELL
NTAIEAVVDLVSPEYHPLAKRAKDIAAAAVLLAALLAVVVGLIILLPKLL
>gnl|CDD|440581 COG0819, TenA, Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism]
MSFSERLREAAAPIWEAILEHPFVQGLADGTLPREAFRHYLVQDYLYLEHFARALALAAAKAPDLEDMRF
LAGLAAGLLEVELALHERYAAELGISEEELEATPPSPTTRAYTSYLLAAAASGDYAELLAALLPCEWGYA
EIGKRLAERPLPPDHPYAEWIETYASEEFQELVEWLIALLDRLAATASEAERERLEEAFRTASRLEYAFW
DMAYRLER
>gnl|CDD|440582 COG0820, RlmN, Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 [Translation, ribosomal structure and biogenesis]. Adenine C2-methylase RlmN of 23S rRNA A2503 and tRNA A37 is part of the Pathway/BioSystem: 23S rRNA modification
LLGLTLEELEEFLAELGEKPFRAKQIFRWLYQKGVTDFDEMTNLPKALREKLAENFEIGLLEVVREQVSA
DGTRKYLFRLADGNLVETVLIPYEDRGTLCVSSQVGCAMGCSFCATGKQGLVRNLTAGEIVGQVLLARRD
LREGGRRVTNIVFMGMGEPLLNYDNVLKAIRILNDPEGLGISARRITVSTSGLVPGIRRLADEGLPVNLA
VSLHAPNDELRDELMPINKKYPLEELLEACRRYPEKTGRRITFEYVLLKGVNDSPEDARELARLLKGLPC
KVNLIPFNPVPGSPYKRPSPERIEAFADILEKAGIPVTVRRSRGDDIDAACGQLRAKV
>gnl|CDD|440583 COG0821, IspG, 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism]. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE is part of the Pathway/BioSystem: Isoprenoid biosynthesis
MPSSPIPRRKTRQVRVGNVAIGGGAPISVQSMTNTDTADVEATVAQIKALAEAGCEIVRVAVPDEEAAAA
LPEIKKQLPVPLVADIHFDYRLALEAAEAGVDKLRINPGNIGSDEKVREVVEAAKERGIPIRIGVNAGSL
EKDLLEKYGDPTPEALVESALEHARILEELGFDDIKISLKASDVQDTIAAYRLLAERCDYPLHLGVTEAG
TGRKGTVKSAAGLGILLAEGIGDTIRVSLTADPVEEVKVAQEILKSLGLRSRGPEVISCPTCGRTEIDLI
QLAEEVEERLRDIKEPLKVAVMGCVVNGPGEAKEADIGIAGGGGEGLLFKKGEIIRKVPEDEIVEELLEE
IEKYVAERYGEGA
>gnl|CDD|440584 COG0822, IscU, Fe-S cluster assembly scaffold protein IscU, NifU family [Posttranslational modification, protein turnover, chaperones]
DLDDLYSEKILDHAKNPRNVGELEDADGSGEGGNPLCGDTVTLYLKVDDGRIEDAKFEGFGCAISQASAS
MLTELVKGKTLEEALALTDEFGDLAALGGLPKFPARVKCALLAWDALKAALADYRAKK
>gnl|CDD|440585 COG0823, TolB, Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport]
LAFTLSRDGNSDIYVVDLDGGEPRRLTNSPGIDTSPAWSPDGRRIAFTSDRGGGPQIYVVDADGGEPRRL
TFGGGYNASPSWSPDGKRLAFVSRSDGRFDIYVLDLDGGAPRRLTDGPGSPSWSPDGRRIVFSSDRGGRP
DLYVVDLDGRKRRLTPAS
>gnl|CDD|440586 COG0824, FadM, Acyl-CoA thioesterase FadM [Lipid transport and metabolism]. Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis
MTLFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPA
RYGDELTVETRVVRLGGSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPDELRAALEALLAA
>gnl|CDD|440587 COG0825, AccA, Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]. Acetyl-CoA carboxylase alpha subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis
NYLDFEKPIAELEAKIEELRALAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTL
DYIEAIFTDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRL
MKLAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDR
VLMLEHSIYSVISPEGCASILWKDASKAPEAAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENL
KEALLKALKELKGLSPEELLEQRYEKFRAIGRFLE
>gnl|CDD|440588 COG0826, RlhA, 23S rRNA C2501 and tRNA U34 5'-hydroxylation protein RlhA/YrrN/YrrO, U32 peptidase family [Translation, ribosomal structure and biogenesis]. 23S rRNA C2501 and tRNA U34 5'-hydroxylation protein RlhA/YrrN/YrrO, U32 peptidase family is part of the Pathway/BioSystem: 23S rRNA modification
MKKPELLAPAGSLEALKAAVEAGADAVYIGGKRFNARARAGNFSLEELAEAVEYAHERGKKVYVTLNTLL
HDEELEELEEYLDFLAEAGVDAIIVQDLGVLELAREIAPDLPLHASTQANVTNSEAVKFLKELGASRVVL
ARELSLEEIKEIREKTDVELEVFVHGALCIAYSGRCLLSSYLGGRSANRGACAQPCRWPYTLIDEEPGEY
YPILEDEHGTYILSPKDLCLLEHLPELIEAGVDSLKIEGRMKSPEYVATVVRAYRQAIDAYLAGPENYEF
DEEWLEELEKLFNRGFTTGFFRNPLKVGDGL
>gnl|CDD|440589 COG0827, YtxK, Adenine-specific DNA N6-methylase [Replication, recombination and repair]
MDAEKIEKLFNLLDESAQVLQNELDTSYLEALIETLENLLDGEVEGKPTEEAKKKLKKNYQKLQLESLSK
EEIRKALQLALLKGMKESVQPNHQMTPDAIGLLIGYLVEKFTKKEGLRILDPAVGTGNLLTTVLNQLKKK
VNAYGVEVDDLLIRLAAVLANLQGHPVELFHQDALQPLLIDPVDVVISDLPVGYYPNDERAKRFKLKADE
GHSYAHHLFIEQSLNYLKPGGYLFFLVPSNLFESDQAAQLREFLKEKAHIQGLIQLPESLFKNEAAAKSI
LILQKKGEGTKQPKEVLLAQLPSFKNPEAMKKFLEQINKWFKENKKN
>gnl|CDD|440590 COG0828, RpsU, Ribosomal protein S21 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S21 is part of the Pathway/BioSystem: Ribosome 30S subunit
MIEVKVRENESIDSALRRFKRKVEKEGILRELRRREHYEKPSEKRKRKKAAARRRQRKRLRK
>gnl|CDD|440591 COG0829, UreH, Urease accessory protein UreH [Posttranslational modification, protein turnover, chaperones]
MTAAPAQLPAGAQGWRGRLRLGFARRGGRTVLARLYHSGPLRVQRPFYPEGPGVCHVVLLHPPGGLVGGD
RLRIDITVGAGAHALLTTQAATKVYRSDGGYARQDVRLTVGAGARLEWLPQETILFDGARLRQRTRVDLA
PGARLLGWEIVVLGRPARGERFAFGRLRSRLEIRRDGRLLWAERLRLDGDAALLDSPAGLGGAPVFATLV
AVGPDADEALLEALRALLAEAPGVRAGASALPDGGLVVRLLGPDAEALRRALRAAWQALRPALLGRPPAL
PRIWKT
>gnl|CDD|440592 COG0830, UreF, Urease accessory protein UreF [Posttranslational modification, protein turnover, chaperones]
TDALALLRLLQLADPALPVGAFAYSHGLETAVEAGLVRDAASLEAWLRDQLRQGLGRLDAPLLARAYRAA
AAGDLAALAELDALLLALRESAELRLESRQMGRALLRLLRALWPDPLLAAYLAAIPAPGHYPVAFGLAAA
ALGIPLEEALLAYLYSWVSNLVSAAVRLVPLGQTAGQRLLARLAPLIEAAAERALALPLDDLGSFAPLLD
IASMRHETQYSRLFRS
>gnl|CDD|440593 COG0831, UreA, Urease gamma subunit [Amino acid transport and metabolism]
MHLTPREQEKLLIFTAAELARRRRARGLKLNYPEAVALISDEVLEGARDGKSVAELMEEGRTVLTRDDVM
PGVPEMIPEVQVEATFPDGTKLVTVHDPIRPA
>gnl|CDD|440594 COG0832, UreB, Urease beta subunit [Amino acid transport and metabolism]
GEIIVADGDIELNAGRETITLTVANTGDRPIQVGSHYHFFEVNPALEFDREAARGMRLDIPAGTAVRFEP
GQTREVELVPIGGARRVYGFNGLVNGPLDDE
>gnl|CDD|440595 COG0833, LysP, Amino acid permease [Amino acid transport and metabolism]
SSGSEKQNKLKRGLKSRHLSMIALGGVIGTGLFLASGYTISQAGPGGALLAYLLGGLMVYFLMTSLGELA
VAMPVSGSFQTYATRFIDPAFGFAVGWNYWLNWAITVAAELTAAGIIMQYWFPDVPVWIWSLLFLALIFL
LNALSVKAFGESEFWFSLIKVITVIAFIIVGLLMIFGIIGGHAPGFSNFTTGDGPFPGGFLAILGVMMIV
GFSFQGTELIGIAAGESENPEKTIPKAIRQVFWRILLFYILAIFVIAALIPYTDAGVAESPFTLVFERAG
IPYAADIMNAVILTAVLSAGNSGLYASTRMLWSLAKEGMAPKIFAKLNKRGVPLNALLATMAVGLLALLS
SFFGAGTVYLWLLSISGLTGFIAWLGIAISHYRFRRAYVAQGGDLEDLKYKAPLFPFGPIFAFILCLIVI
IGQAFDPEQRIALYIGIPFFLACYLGYKLKKKTKLVPLEEMDLSPED
>gnl|CDD|440596 COG0834, HisJ, ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms]
LRVGVDPDYPPFSFRDEDGKLVGFDVDLARAIAKRLGLKVEFVPVPWDRLIPALQSGKVDLIIAGMTITP
EREKQVDFSDPYYTSGQVLLVRKDNSGIKSLADLKGKTVGVQAGTTYEEYLKKLGPNAEIVEFDSYAEAL
QALASGRVDAVVTDEPVAAYLLAKNPGDDLKIVGEPLSGEPYGIAVRKGDPELLEAVNKALAALKADGTL
DKILEKWFGEDVP
>gnl|CDD|440597 COG0835, CheW, Chemotaxis signal transduction protein CheW [Signal transduction mechanisms]
LEAGANELQYLTFRLGGERYAIPIEKVREILPLPPITPVPGAPPWVLGVINLRGRVVPVIDLRALLGLPP
TEDTERTRIIVLEVGGRVVGLLVDSVSGVVRIDPDDIEPPPELLSGGLAPFITGVAKLDDRLILLLDLEK
LLAEEELAALA
>gnl|CDD|440598 COG0836, CpsB, Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]
SMIYPVILAGGSGTRLWPLSRESYPKQFLPLLGEKSLLQQTVERLAGLVPPENILVVTNEEHRFLVAEQL
PELGPANILLEPVGRNTAPAIALAALLIAKRDPDAVLLVLPADHLIEDEEAFREAVRAAVEAAEAGKLVT
FGIKPTRPETGYGYIEAGEALGGAGAYKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELER
HAPEIYAALEAAVAAAGTDLEVRLDAEAFAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELL
EKDENGNVVLGDVLLIDSSNSLVRSEGRLVAVIGVEDLVVVDTPDALLVAPKDRAQEVKKIVEALKE
>gnl|CDD|440599 COG0837, Glk, Glucokinase [Carbohydrate transport and metabolism]. Glucokinase is part of the Pathway/BioSystem: Glycolysis
MTAPTPILVADIGGTNARLALAEGGGGLELLEIRRYPSADYASLEDALRAYLAELGLPRPRAACLAVAGP
VDGDRVKLTNLPWSISAAALRAALGLERVLLINDFEALAYALPALSPDDLVQLGGGEPDPGGPRAVIGPG
TGLGVAGLVPDGGGWIVLPSEGGHVDFAPRDERELELLRYLRRRYGHVSAERVLSGPGLVNLYRALAALD
GAPPAPLSPAEITAAALAGSDPLAVEALELFCRILGRVAGNLALTLGARGGVYLAGGIAPRILPLLDRSG
FREAFEDKGRFSALLADIPVYVITHPQPGLLGAAAYAAQL
>gnl|CDD|440600 COG0838, NuoA, NADH:ubiquinone oxidoreductase subunit 3 (chain A) [Energy production and conversion]. NADH:ubiquinone oxidoreductase subunit 3 (chain A) is part of the Pathway/BioSystem: NADH dehydrogenase
MLSDYLPILIFLLVALGLALAMLLLSRLLGPKRPNPEKLSPYECGIEPVGDARIRFSVRYYLVALLFVIF
DVEVVFLFPWAVVFRELGWFGLIEMLVFIAILLVGLIYAWKKGALEW
>gnl|CDD|440601 COG0839, NuoJ, NADH:ubiquinone oxidoreductase subunit 6 (chain J) [Energy production and conversion]. NADH:ubiquinone oxidoreductase subunit 6 (chain J) is part of the Pathway/BioSystem: NADH dehydrogenase
ETILFYIFAALAVASALGVVTSRNPVHAALYLVLTFLSVAGLYLLLGAEFLAAVQVIVYVGAVMVLFLFV
VMLLDLDKEELREGFRKYRPLAALVGLLLLAELAYVLLSTSWAAAPAAAAAAVGNTKALGELLFTDYLLP
FELASVLLLVAMIGAIVLARRE
>gnl|CDD|440602 COG0840, Tar, Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]
LLILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLL
ALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLAL
AALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPL
RELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELA
AGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETA
ETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIE
ELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVN
QAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL
>gnl|CDD|440603 COG0841, AcrB, Multidrug efflux pump subunit AcrB [Defense mechanisms]
MNLSRFFIRRPVAAIVLSLLILLAGLLAYLRLPVEQFPDIDPPTVTVSTTYPGASPEEVESTVTTPIEEA
LNGVEGIKYITSTSSEGSSSITVEFELGTDIDEALVDVQNAVDRARSDLPEDVEPPGVTKVNPSDFPVMV
LALSSDDLDELELSDYAERNIKDRLERVPGVGQVQIFGGREREIRIWLDPDKLAAYGLTLADVANAIRAQ
NVDVPAGRIGGGDREYTVRTNGRLKTPEEFENIVIRTNDGSVVRLGDVARVEDGAEDYRSIARLNGKPAV
GLAIQKQPGANALEVADAVRAKLEELQASLPEGVELTIVYDQSEFIRASIEEVVKTLLEAILLVVLVVFL
FLRSWRATLIPAVAIPVSLIGTFAVMYLLGFSLNILTLFALVLAIGIVVDDAIVVVENIERHMEEGLSPL
EAAIKGAREVAGAVIASTLTLVAVFLPLAFMGGITGQLFRQFALTVAIALLISLFVALTLTPALCARLLK
PHPKGKKGRFFRAFNRGFDRLTRGYGRLLRWALRHRKLTLLVALALLALSVLLFGRLPTEFFPEEDQGQI
IVSVQLPPGTSLERTEAVVRQVEEILLEVPEVESVFSVVGFSGGGSGSNSGTIFVTLKPWDERDRSADEI
IARLREKLAKIPGARVFVFQPPAGGLGSGAPIEVQLQGDDLEELAAAAEKLLAALRQIPGLVDVRSDLQL
GKPELQLDIDREKAAALGVTVADVASTLRAALGGRYVNDFNRGGREYDVRVQAPEEDRNSPEDLENLYVR
TPDGEMVPLSSVATIEEGTGPSSINRYNGQRSVTVSANLAPGVSLGEALAAIEELAAELKLPPGVSIEFT
GQAEEEQESFSSLGLAFLLALLLVYLVLAAQFESFIQPLIILLTVPLALIGALLGLLLTGTPLNIYSQIG
LIMLIGIVVKNAILLVDFANQLREEGMSLREAILEAARLRLRPILMTSLATILGLLPLALGTGAGAEFRQ
PLGIAVIGGLLFSTLLTLFVVPVLYVLLDRLRRRL
>gnl|CDD|440604 COG0842, YadH, ABC-type multidrug transport system, permease component [Defense mechanisms]
YLAFLVPGLLAMSLLFTALMLTALSIAREREQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLV
ALLFFGVPLRGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLP
GWLQAIAYLNPLTYFVEALRALFLGGAGLADVWPSLLVLLAFAVVLLALALRLFRRRLRG
>gnl|CDD|440605 COG0843, CyoB, Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]
EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIF
FFATPFLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEAS
PGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLL
LLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVA
IAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFV
IGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFI
GFNLTFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAGGNPW
GARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE
>gnl|CDD|440606 COG0845, AcrA, Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms]
MKVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQL
AAAQAQLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDG
VVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPA
VDPATRTVRVRAELPNPDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPV
TLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVVEAAAP
>gnl|CDD|440607 COG0846, SIR2, NAD-dependent protein deacetylase, SIR2 family [Posttranslational modification, protein turnover, chaperones]
MTKIERLAELLREAKRIVVLTGAGISAESGIPDFRGPDGLWEKYDPEEVASPEAFRRDPELVWAFYNERR
RLLRDAEPNAAHRALAELEKAGKLVFVITQNVDGLHQRAGSKNVIELHGSLHRLRCTKCGKRYDLEDVLE
DLEGELPPRCPKCGGLLRPDVVWFGEMLPEEALERALEALAEADLFLVIGTSLVVYPAAGLPEYAKRAGA
PLVEINPEPTPLDSLADLVIRGDAGEVLPALVE
>gnl|CDD|440608 COG0847, DnaQ, DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair]
RFVVLDTETTGLDPAKDRIIEIGAVKVDDGRIVETFHTLVNPERPIPPEATAIHGITDEDVADAPPFAEV
LPELLEFLGGAVLVAHNAAFDLGFLNAELRRAGLPLPPFPVLDTLRLARRLLPGLPSYSLDALCERLGIP
FDERHRALADAEATAELFLALLR
>gnl|CDD|440609 COG0848, ExbD, Biopolymer transport protein ExbD [Intracellular trafficking, secretion, and vesicular transport]
MALSRRRRRREMAEINLTPLIDVMFVLLIFFMVTAPFLTPQGLKVDLPKASAAPPPKEPEPLTVSIDADG
QIYLNGEPVDLEELEARLKAALAANPDPEVVIRADKDVPYGDVVKVMDALRKAGITKVSLATEPKGG
>gnl|CDD|440610 COG0849, FtsA, Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]
AKSNIIVGLDIGTSKVVALVGEVDPDGKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGV
KIESVYVGISGGHIKSQNSRGVVAISGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIK
DPVGMSGVRLEVDVHIVTGPKTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGG
TTDIAVFKDGALRHTAVIPVGGDHITNDIAIGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRP
PREISRKELAEIIEARVEEIFELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILGLPVRIGRP
DGIGGLPEAVRDPAYATAVGLLLYAAKNQEERFEPVKEKKKGGLFGRIKRWF
>gnl|CDD|440611 COG0850, MinC, Septum site-determining protein MinC [Cell cycle control, cell division, chromosome partitioning]
MSKQPVELKGTKFGLVVLLLDSADFEELLEELKEKLEQAPGFFKGAPVVLDLGNRLLTEEDLEELVELLR
EYGLRPVGVRGGVPELAEAAAAAGLPVLPERAAAAPEAAPAPEEAPTLVIRRPVRSGQQIYAPGDLVVLG
DVNPGAEVIADGNIHVYGPLRGRAHAGASGNTEARIFALSLEPELLRIAGVYARAEDLPAELRGKPEQAY
LEDGKIVIEPLSL
>gnl|CDD|440612 COG0851, MinE, Septum formation topological specificity factor MinE [Cell cycle control, cell division, chromosome partitioning]
MSLLDFFRGRKKSSADVAKERLQLVLAHDRAGLSPDYLEQLKKEILEVISKYVEIDEDAVEVSLEREDDL
SALEANIPLPRVKR
>gnl|CDD|440613 COG0852, NuoC, NADH:ubiquinone oxidoreductase 27 kD subunit (chain C) [Energy production and conversion]. NADH:ubiquinone oxidoreductase 27 kD subunit (chain C) is part of the Pathway/BioSystem: NADH dehydrogenase
MSELEELLEALEEKFGDAVLEVEEARGELTLTVPPEDLVDVARFLRDDLGFDHLSDLTGVDYPERGDRFE
VVYHLLSLTHNRRLRLKVFVPRDDPVVPSVTDVWPGANWHEREAYDMFGIVFEGHPDLRRILLPEDWEGH
PLRKDFPLEGYVEVRYDEELKRLE
>gnl|CDD|440614 COG0853, PanD, Aspartate 1-decarboxylase [Coenzyme transport and metabolism]. Aspartate 1-decarboxylase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
MLRTMLKSKIHRATVTEADLNYEGSITIDEDLLDAAGILPYEKVQIVNVNNGERFETYVIPGERGSGVIC
LNGAAARLVQPGDLVIIIAYAQMDEEEAKTHKPKVVFVDEDNRIVEIGN
>gnl|CDD|440615 COG0854, PdxJ, Pyridoxine 5'-phosphate synthase PdxJ [Coenzyme transport and metabolism]. Pyridoxine 5'-phosphate synthase PdxJ is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
TRLGVNIDHVATLRNARGGNYPDPVRAALLAEEAGADGITVHLREDRRHIRDRDVRRLRELVQTELNLEM
APTEEMLDIALRVKPDQVTLVPEKREELTTEGGLDVAGQADRLKPVIARLKDAGIRVSLFIDPDPEQIEA
AAELGADRVELHTGPYADAFDEAEREAELARLRAAARAAHELGLGVNAGHGLNYDNVAPIAAIPGIEELN
IGHALIARALFVGLEEAVREMKALM
>gnl|CDD|440616 COG0855, Ppk, Polyphosphate kinase [Inorganic ion transport and metabolism]
DPSRYINRELSWLAFNERVLEEAEDPRVPLLERLKFLAIFSSNLDEFFMVRVAGLKRQIEAGVTKRSPDG
LTPAEQLEAISERVHELVEEQYRIFNEELLPELAEEGIHILRRDELTEEQRAWLRDYFEEEVFPVLTPLA
LDPAHPFPFLSNKSLNLAVRLRGKDAGGSKFAIVKVPRVLPRFIRLPSELGKHRFVLLEDIIRAHLDELF
PGYEVLGAYQFRVTRNADLEVDEDEAEDLLEAIEKELKRRRFGDPVRLEVDADMPEELLEFLLEELGLDE
EDVYRVGGPLNLTDLMQLPDLDRPDLKYPPFTPRPPPRLREGGDIFAAIREKDILLHHPYESFDPVVRFL
RQAAADPDVLAIKQTLYRTSGDSPIVDALIEAAENGKQVTVLVELKARFDEENNIRWARRLEEAGVHVVY
GVVGLKTHAKLCLVVRREGDGLRRYVHLGTGNYNEKTARLYTDLGLLTADPEIGADVTRLFNFLTGYSRP
PKYKKLLVAPFTLRKRLLELIDREIENAKAGKPARIIAKMNSLVDPEIIDALYEASQAGVKIDLIVRGIC
CLRPGVPGLSENIRVRSIVGRFLEHSRIYYFGNGGDEEVYISSADWMTRNLDRRVEVLFPILDPTLKQRI
IEILDIQLADNVKAWELDPDGSYVRVKPAEGEPPFRAQEALMEYASAKGRGSALA
>gnl|CDD|440617 COG0856, PyrE2, Orotate phosphoribosyltransferase homolog [Nucleotide transport and metabolism]
MKNIDELIEKAAELKSKGLSTGEIADELNVSRETATWLLTRAKKGSGEPAPKDIHVDWSSIGRSSNRLRY
IAQAMADMLLEELGDEEVDLVVGIAKSGVPLATLVAEELGTELAIYHPAKHQWEIEDLGGSFSRNFASVE
GKRCVIVDDVITSGTTMTETIEAIREHGGEPVACVVLVDKRGIDEIDGVPVYSLIRVVRVG
>gnl|CDD|440618 COG0857, PtaN, BioD-like N-terminal domain of phosphotransacetylase [General function prediction only]
MMKSIYIASTEPGSGKTSVALGLARALQRKGLRVGYFKPIGQSLVGGGERDEDVELIREHLGLDLPYEDA
SPVTLDEVETLLAEGDPDELLERIVERYEALAAECDVVLVEGSDPTGVGSPFELSLNARIAKNLGAPVLL
VASGGGRTPEELVDALLLAADEFRGEGARVLGVIINRVPPEKLEEVREALRPFLEGSGIPVLGVIPENPE
LAAPTVRDLAEALGAEVLNGGELLDRRVESVVVGAMSVPNALERLREGALVITPGDRSDILLAALLAALS
GTPSIAGLILTGGLPPDPAVLRLAEGLGQTLPILSVELDTYTTAERLERVRGRIRADDPRKIELALELFA
EHVDVDWLLSRLGLPRSRLSPPAFFYYLLERAARAAKRIVLPEGGEDRRILAAAICLLRRIAACVLLGGP
EEIIRVAAAQGGLLLDGIEIIDPPDSRLRYVAAEVYLRRRKKKGVTVAAAQLEDDVVLYTGMMMVHEGDG
LGMGSGATTTTTTTIPPQLIITKTGPGVVSSSSFFLMLLQVVVVGDCACAPNPPPEELALAAIISSSSAA
AAGFGPEPAMISLSSSTSGSGGGVDVVKVATATALVRRRDLLLDGPGPYQAAAAADVVVAKAKPSPVAGA
AAAFVFPFLDTNNTNNTAKARQASAGAVAPGPQGLGLPVNDLDLSRGVVDIDITIALTIIAAQQQAA
>gnl|CDD|440619 COG0858, RbfA, Ribosome-binding factor RbfA [Translation, ribosomal structure and biogenesis]
AESQRQLRVAELIQRELAEILQRELKDPRLGLVTVTEVEVSPDLSHAKVYVSVLGDEEEREEVLKALNKA
KGFIRSELGKRLRLRYTPELRFVYDDSLEYGARIDELLDEARKEDDEE
>gnl|CDD|440620 COG0859, RfaF, ADP-heptose:LPS heptosyltransferase [Cell wall/membrane/envelope biogenesis]
PQPPMRILIIRLSALGDVLLATPALRALKRAYPDAEIDLLVEPRFAPLLELNPYVDEVIPFDKKRRKGLA
ELLKLLRQLRAERYDLVIDLQGSLRSALLARLAGAPRRIGFDKELRSLLLNHRVPLPPDQHEVERYLALL
AALGIPLPDPRPDLPLPEEDRAEARALLARLGLPGKPYIVLHPGASWPAKRWPAERFAELARALAARGLR
VVLLGGPGERELAEEIAAALGPPVINLAGKTSLRELAALLARADLVVGNDTGPMHLAAALGTPTVALFGP
TDPARWGPYGDRHRVLRADLPCSPCGKRECPLGHHPCMADISPEEVLEALEELLAR
>gnl|CDD|440621 COG0860, AmiC, N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis]
LDLKASLALAAAPAAARKGPPLKGKVIVIDPGHGGKDPGAIGPNGLKEKDVNLDIALRLAELLEAPGAKV
VLTRDDDTFVSLSERVAIANKAKADLFISIHANAAPNPSARGAEVYYYSGSQTSAESKKLAEAIQKELVK
ALGLKDRGVKQANFYVLRETDMPAVLVELGFISNPEDEALLKSPAYQQKLAEAIADGILRYFGK
>gnl|CDD|440622 COG0861, TerC, Tellurite resistance membrane protein TerC [Inorganic ion transport and metabolism]
MDLLLFGPEAWLALLTLYLLEIVLSIDNAFVIALIFRKLPPEQQKKALFWGILGALVLRIILIFLGAWLL
SFPWILYLGGLFLLWTAIKLLHEKEEEDEENENGKRAATPLWLAVVQIELADLVFSLDSVPAAFGITQDP
FLVFTGNIFAILGLRFLAFLLAGLLDRFPYLKYLAAAILGFIGVKLILEDLHFHIPKGYISLAVIFSVLA
LGILASLLKRRKAKA
>gnl|CDD|440623 COG0863, YhdJ, DNA modification methylase [Replication, recombination and repair]
RLICGDCLEVLKELPDESVDLIVTDPPYNLGKKYGLGRREIGNELSFEEYLEFLREWLAECYRVLKPGGS
LYVNIGDRYISRLIAALRDAGFKLRNEIIWRKPNGVPGPSKRRFRNSHEYILWFTKGKKYTFNVDAVKSI
EDGRNPSDVWDIPGVTPKERKGHPTQKPVELLERLILASSNPGDIVLDPFAGSGTTLVAAERLGRRFIGI
EIDPEYVEVARRRLEEATGLEFEELA
>gnl|CDD|440624 COG0864, NikR, Metal-responsive transcriptional regulator, contains CopG/Arc/MetJ DNA-binding domain [Transcription]
MKRISVSLPDDLLEELDELVEEEGYSNRSEAIRDAIREYLAERKWREGDGEVVGVLTIVYDHHKRELSER
LTDIQHEYRDLIISSLHVHLDHDNCLEVIVVRGEAEEIRELADKLRGLKGVKHGKLVLLPAE
>gnl|CDD|440625 COG1001, AdeC, Adenine deaminase [Nucleotide transport and metabolism]
GREPADLVIKNGRLVNVFTGEILEGDIAIAGGRIAGVGDYIGEATEVIDAAGRYLVPGFIDGHVHIESSM
VTPAEFARAVLPHGTTTVIADPHEIANVLGLEGVRYMLEAAEGLPLDIFVMLPSCVPATPGLETAGAVLG
AEDLAELLDHPRVIGLGEVMNFPGVLNGDPRMLAKIAAALAAGKVIDGHAPGLSGKDLNAYAAAGIRSDH
ECTTAEEALEKLRRGMYVMIREGSAAKDLPALLPAVTELNSRRCALCTDDRHPDDLLEEGHIDHVVRRAI
ELGLDPVTAIQMATLNAAEHFGLKDLGAIAPGRRADIVLLDDLEDFKVEKVYADGKLVAEDGKLLVDLPK
YPYPPWARNTVKLRPLTAEDFAIPAPGGVKVRVIGVIPGQIITEHLEAELPVEDGEVVPDPERDILKIAV
VERHGGTGNIGLGFVKGFGLKRGAIASTVAHDSHNLIVVGTNDEDMALAANRLIEIGGGIVVVKDGKVLA
ELPLPIAGLMSDEPAEEVAEKLEALRAAARELGCTLEEPFMTLSFLALPVIPELKLTDRGLVDVTTFEF
>gnl|CDD|440626 COG1002, YeeA, Type II restriction/modification system, endonuclease and methylase domains [Defense mechanisms]
FANDSNSLDKAFFGEELLLAGLEEGAAVANKLIGRELEEQAIALALLEAGIIQLDSLLKTSRLSKKTGVG
FKTLTRLLNVAALLAITDLNLILLLKLLEALLKALLLAEEAAAALLLLTLALNDPDTDALFELLAALLAE
FREDFELLFAKFLPLNSSLLFELRLAFATLLILLLRLELEITLYVNTVLKDDNGKRRTGLLDPLFYLFAF
LDATDLSSDWTKINPDIFGSMFEAVLDPEERSKLGMHYTSVPNIMKVVRPLFLDPLRAEWEAAGAWEALL
EKIEAERELLNLLKRLASIRVLDPACGSGNFLVIAYKELKAIEGEVLIRLEELDGLSQFHRKSTIIPNNF
YGIEINPFAAEIARLALWIAELQWNYRYRGQLAPFLPLLNDDNNIECGNALRLRDGNAADWRFVCPETGG
EDYIIGNPPFLGQKEQREELKDDYVAVFPGKVPGSADYVAYWFEKAADYLRAGRGRFGFVTTNSICQGEQ
RKVLWPLLFATGLEIFFAIPDFPWANASDNAAVRVSIVGLSKGKPAGPKTLFSELEGVLFGREVGNINAY
LTAGADVTVAKRLKPNSELGKMFYGNKPGGGGAFIISREEAEELLAEDPGNEKVIKPFLGGRDLIRGPRR
YCLWIIDFGLSLEEAKSYPAIFERLEKVVKPERDKSRRAATRKKWWLLARNPHEFREAKAGLSRYIATPR
VSKERPFGWLDSGTIPDDKAFAIADDDLYLLGILSSRLHRVWILAVGGGLGNDPRYSNTLCFNTFPFPKL
TEKQKEDITALAEEILLAPEKMPSDLRAAHQELDEAVERAYGWRRFLNDTERLEKLFALYTEMTAKEK
>gnl|CDD|440627 COG1003, GcvP2, Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport and metabolism]. Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
VSLPEPEADAASLLPEALLRKSPVFLPEVSETEVLRHYTRLSQKNLGLDTGMIPLGSCTMKYNPKINEEP
ATLPGFANLHPFQPEETVQGYLELMYELEEWLAEITGMDAVSLQPNAGAQGEYAGLLAIRAYHESRGEGH
RNEILIPDSAHGTNPASAAMAGFKVVVVKSDEDGNVDLEDLKAKVGDRTAALMLTNPSTHGVFEEDIKEI
CDIVHEAGGLVYYDGANLNAIVGLARPGDMGFDVCHLNLHKTFSTPHGGGGPGSGPVGVKEHLAPFLPGP
PVVKDGDKYRLDYDRPKSIGRSAAFYGNAGVLVRAYAYIRMMGAEGLREATEVAVLNANYLAARLKDHYP
VLYTGNGRCAHEFILDLRPLKKETGVTTLDIAKRLLDYGFHAPTMYFPLIVPETLMIEPTESESKEELDR
FIDAMIAIREEAREDPEPLKNAPHTTPVRRLDEVYADRNLVLTWREEE
>gnl|CDD|440628 COG1004, Ugd, UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]
MKIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLRFTTDL
AEAVAEADVVFIAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRG
AGVDFDVVSNPEFLREGSAVEDFLRPDRIVIGVDSERAAEVLRELYAPFVRNGTPIIVTDLRSAELIKYA
ANAFLATKISFINEIANLCEKVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELG
YDLRLLEAVEEVNERQKRRLVEKIREHLGGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARV
RAYDPVAMENARRLLPDDITYADDAYEALEGADALVILTEWPEFRALDFARLKALMKGPVIFDGRNLLDP
EELRAAGFTYYGIGRP
>gnl|CDD|440629 COG1005, NuoH, NADH:ubiquinone oxidoreductase subunit 1 (chain H) [Energy production and conversion]. NADH:ubiquinone oxidoreductase subunit 1 (chain H) is part of the Pathway/BioSystem: NADH dehydrogenase
MSLLLAPLLITLIKALVILVFLLLLAAYLTWAERKVLARMQDRIGPNRVGPFGLLQPLADGLKLLFKEDI
IPAGADKFLFLLAPILAFIPALLAFAVIPFGPGLVLADLNVGLLYVLAVSSLGVYGIILAGWASNNKYSL
LGALRAAAQMISYEIPLGLSLLGVVLLAGSLNLSEIVEAQAGGLWFILPQPLAFVVFFIAALAETNRAPF
DLPEAESELVAGYHTEYSGMKFALFFLAEYANMFLVSALATTLFLGGWLGPFPILPLGGLPGILWFLLKT
LFFIFFFIWVRATLPRYRYDQLMRLGWKVLLPLSLVNLVLTAAVVLLFG
>gnl|CDD|440630 COG1006, MnhC, Multisubunit Na+/H+ antiporter, MnhC subunit [Inorganic ion transport and metabolism]
MELLLALVIGVLFAIGVYLLLRRNLIKVIIGLSLLSNAVNLLLFAMGGLTGGAPPILGEGPPAAPYADPL
PQALVLTAIVIGFAVTAFLLALAYRIYQLYGTDDVDELREDER
>gnl|CDD|440631 COG1007, NuoN, NADH:ubiquinone oxidoreductase subunit 2 (chain N) [Energy production and conversion]. NADH:ubiquinone oxidoreductase subunit 2 (chain N) is part of the Pathway/BioSystem: NADH dehydrogenase
SLDLLALLPEIILLLGALVLLLLDLFLPRRSRRLLAGLALLGLLLALALLLLALGGGTGTAFGGMFVVDG
FALFFKLLILLAALLVLLLSRDYLERRGLLRGEFYALLLFATLGMMLMASANDLLTLFLGLELLSLSLYV
LVAFRRDDRRSSEAALKYFLLGALSSGFLLYGISLLYGATGSLNLAGIAAALAAGGANSPLLLLGLVLVL
AGLAFKLSAVPFHMWTPDVYEGAPTPVTAFLATAPKIAAFAALLRLLVEAFPGLAADWQLLLAVLAVLSM
TVGNLAALAQTNVKRMLAYSSIAHAGYLLLGLAAGTPLGVSAALFYLLAYLFMNLGAFAVILLLSRKGGE
AEEIEDLAGLARRSPLLALAMTIFLLSLAGIPPTAGFFGKFYVFSAAVEAGLYWLAVIAVLNSVISAYYY
LRVVKAMYFDEPEEEAPISAPPGLRVALVIAALLVLLLGIFPGPLLDLAAAAA
>gnl|CDD|440632 COG1008, NuoM, NADH:ubiquinone oxidoreductase subunit 4 (chain M) [Energy production and conversion]. NADH:ubiquinone oxidoreductase subunit 4 (chain M) is part of the Pathway/BioSystem: NADH dehydrogenase
MGMPLLSLLILLPLLGALLLLLLPRRNARLARWVALAVSLLTLLLSLYLLAGFDPGTGGFQFVESYPWIP
SLGISYHLGVDGISLPLVLLTALLTPLAILASWNEIKKRPKLYYALLLLLEAGMIGVFLALDLFLFYVFW
ELMLIPMYFLIGIWGGERRIYAAIKFFLYTLAGSLLMLVAILALYFLAGALTFDIAELAAAPLPLTAQLL
LFLAFFIAFAVKVPMFPFHTWLPDAHVEAPTAGSVLLAGVLLKMGGYGLLRFALPLFPEASAYFAPLLAA
LGVIGIIYGALVALAQTDLKRLIAYSSVSHMGFVLLGIFALNPLGLQGAVLQMVSHGLITAALFLLVGVL
YDRTHTRDIADLGGLAKRMPVLAALFLLAALASLGLPGTSGFVGEFLVLLGAFQVNPWLAILAALGLILT
AAYLLWMYQRVFFGPLKEELAELPDLNPRELAVLAPLAALILLLGLYPQPLLDLIEPSVEALLARVGA
>gnl|CDD|440633 COG1009, NuoL, Membrane H+-translocase/NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit [Energy production and conversion]. Membrane H+-translocase/NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit is part of the Pathway/BioSystem: NADH dehydrogenase
LQLLWLIPLLPLLGALLAGLLGRRLGRRAAGWLAALAPLAAFVLSLLLFPAVLGGEVVVELYTWIPVGSL
GLDFGFRLDGLSLLMLLLVTGVGLLVHIYSIGYMSGDPGLARFFAYLLLFMAAMLGLVLSDNLLLLFVFW
ELVGLCSYLLIGFWYEKPSARRAARKAFLVTRVGDLGLLLGILLLGAIAGTLNFSELLAAAPTILSSPLL
TLILLLLLLGAFGKSAQFPLHFWLPDAMEGPTPVSALLHAATMVKAGVYLLARLSPLFALSPVWLTVVAI
IGAITALFAALIALAQTDIKRVLAYSTVSQLGYMFLALGVGAYVAALFHLLTHAFFKALLFLGAGSVIHA
TGTRDIRKMGGLRKKMPITAITFLIGALSLAGIPPFAGFFSKEAILEAALEAGGLGPLLLAVALLGAFLT
AFYSFRLFFLVFFGKPRPKTPKHPHESPWLMTLPLVVLAVLSLVLGLLLPGLLEGLLAPAAVLGGELHLA
HGLLLNALPLLLSLLGIALGYLLYLKRPLPALAERLKPLYRLLANKWYFDELYDALFVKPVRALARFLWF
DRYVIDGIVNGLARLTLFSGRLLRRLQTGYLQFYALTILLGVVVLLLL
>gnl|CDD|440634 COG1010, CobJ, Precorrin-3B methylase [Coenzyme transport and metabolism]. Precorrin-3B methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
PMRGKLYVVGLGPGSAELMTPRARAALAEADVVVGYGTYLDLIPPLLPGKEVHASGMREEVERAREALEL
AAEGKTVAVVSSGDPGVYGMAGLVLEVLEEGGAWRDVEVEVVPGITAAQAAAARLGAPLGHDFCVISLSD
LLTPWEVIEKRLRAAAEADFVIALYNPRSRKRPWQLERALEILLEHRPPDTPVGIVRNAGRPDESVTVTT
LGELDPEEVDMLTTVIIGNSQTRVIGGWMITPRGYPRKYD
>gnl|CDD|440635 COG1011, YigB, FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism]
IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALWRRYERGEITFAELLRRLLE
ELGLDLAEELAEAFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVV
SSEEVGVRKPDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAEPRPDYVI
SDLAELLELL
>gnl|CDD|440636 COG1012, AdhE, Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]. Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
MTTPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAI
LLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRRE
PLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSE
VGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNA
GQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELL
TGGRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLA
RARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL
>gnl|CDD|440637 COG1013, PorB, Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]. Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
VLKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAA
AVATGIKLANPDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTT
TTPYGKPEPPKDPAEIAAAHGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDPSKTI
EWAKEGMWPLYEYDPGEKLRLTYEPKDKIPVGEFLKNQGRFEELIEEIQKPV
>gnl|CDD|440638 COG1014, PorG, Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma subunit [Energy production and conversion]. Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma subunit is part of the Pathway/BioSystem: Pyruvate oxidation
MAMDLEIRIAGVGGQGVVTAGKILAKAAMREGYYVQGYPSYGSEQRGGPVVSHVRISDEPIRSPLIDEAD
VLIALDPEELDRVLDGLKPGGVLIVNSSLVPPEVWRLPQEALERKDIRVYVIDATKIAKELLGNARVANT
VMLGALAALLGLPLEALEEAIEETFGKKGEKVVELNLKAFEAGYEAAKEVFALAAAPAPLVLLAGNAAAA
LGAAAGGAAFAAAYPITPSTSLIEAAAAAAAKVGGVVAEEEAAAAAAAAAAAAAAAGAAAAAAGGGGGAA
LATEGLGLAGMTETPVVAVAAPRPGPGTGTPTEEEQGLLLLAAGGGGGEAPALALAPDTEEELLFAAAAA
FALAEYAQALLLLLLLQLLVLLLTDLLLLLLDLLRRRAGLGAEEAEARRKLLAAEGRAARAAGGGGGGGG
GGGL
>gnl|CDD|440639 COG1015, DeoB, Phosphopentomutase [Carbohydrate transport and metabolism]
MKRAILIVLDSVGIGEAPDAAKFGDEGANTLGHIAEAVGGLNLPNLARLGLGNIAPLAGLPPVEEPLGAY
GKMAEVSAGKDTTTGHWEIAGLPVEFPFPTFPDGFPEELIDEFEERTGRGVLGNKPASGTEIIEELGEEH
MRTGKPIVYTSADSVFQIAAHEEVFPLEELYRLCEIARELLDGEYAVGRVIARPFVGEPGNFVRTANRHD
YALKPPGPTLLDRLKEAGGDVIAVGKISDIFAGRGITESVKTKGNADGMDKTLEAMDEAFGGLIFTNLVD
FDSLYGHRRDVAGYAKALEEFDARLPELLAALRPDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPGLK
PGGNLGTRETFADIGATIADHFGVPPPGHGTSFLS
>gnl|CDD|440640 COG1017, Hmp, Hemoglobin-like flavoprotein [Energy production and conversion]
LSPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLFNGDMGEQRKALAAALAAYARNLDNLEAL
LPALERLGRKHVSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVMIAAEAE
>gnl|CDD|440641 COG1018, Fpr, Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]
AGFRPLRVVEVRRETPDVVSFTLEPPDGAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITV
KRVPGGGGSNWLHDHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFRPVT
LVYGARSPADLAFRDELEALAARHPRLRLHPVLSREPAGLQGRLDAELLAALLPDPADAHVYLCGPPPMM
EAVRAALAELGVPEERIHFER
>gnl|CDD|440642 COG1019, CAB4, Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]. Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
YMKVAVGGTFDPLHDGHRALLERAFELGGDVIIGLTSDELAKKTKKRPVRPYEERRENLEAFLEKLAPDR
EYEIRKLDDPYGPALEDEDFDALVVSPETEPGAEKINEIRRERGLKPLEIVVVPHVLAEDGKPISSTRIR
NGEIDEHGRLLKDR
>gnl|CDD|440643 COG1020, EntF, EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism]
AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRA
LRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLL
LLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAY
WRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYS
GQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEE
LQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLF
DAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAARTP
DAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAY
PAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTG
RPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAAL
AELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETT
VDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFV
ADPFGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAP
GDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAA
APPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAA
AAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLA
LLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLL
LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALL
ALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL
>gnl|CDD|440644 COG1021, EntE, EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism]
MLEGFTPWPEEFAARYREAGYWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLAL
GLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDRHRGFDYRAL
ARELQAEVPSLRHVLVVGDAGEFTSLDALLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYL
YSVRASAEICGLDADTVYLAALPAAHNFPLSSPGVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTAL
VPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEGLVNYTRLDDPEEV
ILTTQGRPISPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRT
PDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAEL
RRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA
>gnl|CDD|440645 COG1022, FAA1, Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]
MSEFSDVPPADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAI
LSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHI
VVLDPRGLRDDPRLLSLDELLALGREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLS
NARALLERLPLGPGDRTLSFLPLAHVFERTVSYYALAAGATVAFAESPDTLAEDLREVKPTFMLAVPRVW
EKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLAGKSPSLLLRLKHALADKLVFSKLREALGGRLR
FAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKIAEDGEILVR
GPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASP
LIEQAVVVGDGRPFLAALIVPDFEALGEWAEENGLPYTSYAELAQDPEVRALIQEEVDRANAGLSRAEQI
KRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA
>gnl|CDD|440646 COG1023, YqeC, 6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]
MQIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPAPRVVWLMVPAG
EITDQVIEELAPLLEPGDIVIDGGNSNYKDDIRRAEELAEKGIHFVDVGTSGGVWGLENGYCLMIGGDKE
AVERLEPIFKALAPGAENGYLHCGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASEFDLDLAEVAEVW
RRGSVIRSWLLDLTADALAEDPKLEGISGYVEDSGEGRWTVEEAIELGVPAPVITAALFARFRSRQEDSF
ADKVLAALRNQFGGHAVKKK
>gnl|CDD|440647 COG1024, CaiD, Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]. Enoyl-CoA hydratase/carnithine racemase is part of the Pathway/BioSystem: Fatty acid biosynthesis
VLVEREGGVATITLNRPEKLNALSLEMLAELAAALDEAEADPDVRVVVLTGAGKAFCAGADLKELAAAAD
PEEARAFARGLQRLFRALRRLPKPVIAAVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGLIPGGGG
TQRLPRLVGLARAKELLLTGRRIDAEEALELGLVNRVVPDDELLAAALALAARLAAGPPLALAATKRALN
AALEAPLDEALELEAEAFAELFASEDAREGIAAFLEKRK
>gnl|CDD|440648 COG1025, Ptr, Secreted/periplasmic Zn-dependent peptidases, insulinase-like [Posttranslational modification, protein turnover, chaperones]
MKKLTLSLFFLLLLLLAAAPSAQAAQGWQPLAETIIKSPNDPRQYRAITLDNGLKVLLVSDPQADKSAAA
LAVPVGSFDDPDDQQGLAHFLEHMLFLGTKKYPEPGEYQEFISKHGGSHNASTATERTNYYFEVENDALE
EALDRFADFFAAPLFDPEYVDRERNAVNAEYTLKRSDDGRRIYQVHKETLNPAHPFSRFSVGNLETLSDK
PGSKLRDELLAFYQRYYSANLMKLVLYSNQSLDELEKLARQTFGAIPNRNLSVPPITVPLYTPEQLGIII
HIVPLKPRRQLRLEFPIPNNQAYYRSKPLTYISYLLGNEGEGSLLDWLKKQGLAESLSAGGGISGRNFGD
FSISVSLTDKGLAHRDEIIAAVFAYIELIRQQGIQEWYFDEQAQLLELAFRFQEKTRPMDYVSWLSDNML
RYPVEDVLDADYLMDGFDPAAIRARLAQLTPENARIWLISPDVPTDKTAYWYDTPYSVDPITQEQLAKWQ
QASQNPALSLPELNPYIPDDFSLIKLDKESAKPELLVDEPGLRLWYMPDQYFAEPKADIYLSLRNPQAVD
SARNQVLTRLLDYLLNDALNELSYQASVAGLSYSLYAHQGGLTLSASGFTQKQPKLLEALLDQLASFEPT
EERFAQAKSQLLRQLDNAEKAKPYSQLFSPLSRLLQPPYFEREELLAALESITLQDLRAFREQLLQQLHL
EMLVVGNLSEEQAKQLADSLKKQLAPNGTGEEPRRQVVDLDKSGSLNLEKACDHTDSALLIYYQSGYDSL
ASMALSSLLGQIISPWFFNQLRTEEQLGYVVGAGYMPLGRQPGLGFYVQSPVASPAYLLERIDDFLKQFE
ERLLALSEEEFAQYKQGLINQLLEPDQNLSEEAQRLWVDIGNGDFEFDTREKLIAAVKKLTRADLIDFFQ
QAVIAPQGLRLLSQSQGTKHSKADELKGWKTITDISAFQKTLPVKE
>gnl|CDD|440649 COG1026, Cym1, Zn-dependent peptidase, M16 (insulinase) family [Posttranslational modification, protein turnover, chaperones]
MTLKVGKTHHGFELLREEYIEELNSTAYLFRHEKTGARLLHLANDDDNKVFSIAFRTPPEDSTGVAHILE
HSVLCGSRKYPVKDPFFELLKGSLNTFLNAMTYSDKTAYPVASRNEKDFYNLMDVYLDAVFFPNLDPLIF
AQEGWRYELEEPDSPLTYKGVVYNEMKGAMSSPDSVLWRALQKSLFPDTTYGYNSGGDPEVIPDLTYEQF
LAFHKKYYHPSNAYIYLYGDIDAEEHLAFLDEEYLSRFERLEVDSEVPDQKRFSAPREVEETYPVAEEED
TENKTYLSLNWLLGESTDLEESLALQLLSYVLLGNSASPLKKALLDSGLGKDVSGGLEDSLRQPVFSIGL
KGSEPEKAEAFEKLILETLEKLVEEGIDKELLEAALNQLEFSLREIDGGSYPYGLQLILRALDSWLYGGD
PLALLRYEPALEKLREKIKDPGYFENLIRKYLLDNPHRVLLTLKPDPGLAERKEAAEKEKLAAIKASLSE
EEKQAIIEQTKALKERQEQEDSPEALATLPKLTLEDIPKEVKEIPLEEEELGGVPVLFHDLFTNGIVYLD
LYFDLPALPEELLPYLPLLTDLLGELGTGKYDYLELSNEIAAYTGGISASTSVYTNIDDVQEYRPYFVVS
GKALARNLDKLFELLKEILLNTRFDDKKRLRELVAQIKARLEQSLTGSGHSLAMSRASSYFSPAAAYSEQ
LSGLSYYRFLKDLEENLDEKLEELAEKLQELADKLFNRPNLLISVTGEEEELEAFKKALEAFIASLPAGT
AAPFKYPFDAEPKNEGWITSSQVNYVAKAYNFVPLGHEYAGALLVLAGILRNGYLWNKIRVQGGAYGGGA
SFDSLSGNFRFYSYRDPNLKETLDVYDEAPDWLRNFDLSERELEKAIIGTISSLDKPLSPAGKGKRAFHR
YLSGRTPEDRQKFRDEILSTTLEDLRRVAELYLDVLKEASIAVIGNEEKIEEAKDLFDEIIKLL
>gnl|CDD|440650 COG1027, AspA, Aspartate ammonia-lyase [Amino acid transport and metabolism]
RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGLLDKEKADA
IVAACDEIIAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTND
VYPTAIRLALLLLLRELLEALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRW
RLYEAAELLREVNLGGTAIGTGLNAPPGYIELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKR
LAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTVTMAAEA
GQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYVENSIGLVTALNPYIGYEKAAE
IAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG
>gnl|CDD|440651 COG1028, FabG, NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]. NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis
MTRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAV
EALVAAAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNI
SSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARI
PLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDGGLTA
>gnl|CDD|440652 COG1029, FwdB, Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]
MPKVVKNVVCPFCGCLCDDLEVEVEGGKIVVVKNACAIGAAKFERAVSDHRITSPRIRGKEVSLEEAIDK
AAEILANAKRPLIYGLSSTDCEAMRAGLALAERVGAVVDNTASVCHGPSLLALQDVGWPTCTLGEVKNRA
DVIIYWGCNPVHAHPRHMSRYSVFPRGFFTPKGRKDRTVIVVDPRPTDTAKVADLHLQVKPGRDYEVLSA
LRALVRGKELSPEEVAGIPVEDLEELAERLKNAKYGVIFWGMGLTQSPGKHLNVDAAIELVRDLNRYTKF
SILPLRGHYNVAGANQVASWQTGYPFRVDFSRGYPRYNPGETSAVDLLARGEVDALLWVASDPGAHFPPD
AVEHLAKIPTIVIDPHGTPTTEVADVVIPVAIPGIEHGGTAYRMDNVPLPLRKLRDSPLPSDEEVLKAIE
ERVKELKG
>gnl|CDD|440653 COG1030, NfeD, Membrane-bound serine protease NfeD, ClpP class [Posttranslational modification, protein turnover, chaperones]
MKKLLLLLLALLLALAAPASAAAAAKKVYVIPIDGAIGPATADYLERALEEAEEEGADAVVLELDTPGGL
VDSAREIVDAILASPVPVIVYVASGARAASAGAYILLASHIAAMAPGTNIGAATPVQIGGGIDEAMEEKV
INDAVAYIRSLAELRGRNADWAEAMVRESVSLTAEEALELGVIDLIAEDLDELLATLGTAGAEIVEYEPT
WRERLLSFLTNPNVAYILLLIGILGLIFELYTPGFGVPGVIGAIALLLAFYGLYLPANYAGLLLFLLGII
LLILELFVPGFGILGIGGIIALVLGLLLLFDTDVPGLGVSALLIVAIALVIAIFLAFVLGKVLRARKRKP
VTGAEELIGKEGVALTDLRPSGKVRIDGERWDAVSEGEFIEKGEKVRVVGVEGLRLVVRPVEE
>gnl|CDD|440654 COG1031, TM1601, Radical SAM superfamily enzyme with C-terminal helix-hairpin-helix motif [General function prediction only]
MKVLIIDGYVDEPACFGVPPYISPYPRYIAGALVDAGVEEDITYLTIDQLRKDPSLWEDVNKADLVVVIA
GMTVPGKYLGGTPITLEEIQRIAWLARGPKILGGPIRFGYGLEGGTAAETLRFDLDFDYLAKGDPEAALY
DYLSGGLEGFPDRRRDYEEIDRWAVLGAFIVEQHPNYPYLICEIETSRGCPRRVGGCSFCTEPLYGRPEF
RPPEGVVEEVEALYDAGVRHFRLGRQADILAYGGKGGGDGPKPNPEALEELYSGIREVAPDLKTLHIDNV
NPGTIARYPEESREALKTIVKYHTPGDVAAFGLESADPVVIKANNLKVTPEEVLEAIRIVNEVGGWRGYN
GLPKLLPGINFVHGLPGETKETFELNYEFLKRVLDEGLLVRRINIRQVMAFPGTPMWETGADIARKHKKL
FKKYKEWVREEIDLPMLRRVVPPGTVLRDVILEYHDGGITFGRQLGSYPLLVGIPGELPLGDVIDVVVVD
HGMRSVTGVPYPLDVNTASLDELTAIPGIGKKRAGKIIAGRPFRSLEELKKVVGDESLDDLLKFV
>gnl|CDD|440655 COG1032, YgiQ, Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only]
MKVLLVYPPKYPVPPLGLAYLAALLEEAGYEVRIVDLNAEDRSLEDLLKPLREDPDLVGISLYTPQYPNA
LELARLIKERNPGVPIVLGGPHASLNPEELLEPFADFVVIGEGEETLPELLEALEEGRDLADIPGLAYRD
DGRIVQNPPRPLIEDLDELPFPAYDLLDLEAYHRRASIETSRGCPFGCSFCSISALYGRKVRYRSPESVV
EEIEELVKRYGIREIFFVDDNFNVDKKRLKELLEELIERGLNVSFPSEVRVDLLDEELLELLKKAGCRGL
FIGIESGSQRVLKAMNKGITVEDILEAVRLLKKAGIRVKLYFIIGLPGETEEDIEETIEFIKELGPDQAQ
VSIFTPLPGTPLYEELEKEGRLYDWEKYEDLLEAVLAPRLSGDR
>gnl|CDD|440656 COG1033, MMPL, Predicted exporter protein, RND superfamily [General function prediction only]
ERLMERLARFILRHRKLVLLLFLLLTLLLAYGAPKLEVDTDFESLLPEDDPSVQAYDEFEEEFGGDDTVV
VAVEGKDDIFTPETLEALRELTEELEEIPGVDSVTSLTNVRATEGTEDGLTVEPLIPDELPASPEELAEL
REKVLSSPLYVGRLVSPDGKATLIVVTLDPDPLSSDLDRKEVVAEIRAIIAKYEDPGVEVYLTGFPVLRG
DIAEAIQSDLAIFFPLALLLILLLLFLFFRSLRGVLLPLLVVLLAVIWTLGLMGLLGIPLSPLTILVPPL
LLAIGIDYGIHLLNRYREERRKGLDKREALREALRKLGPPVLLTSLTTAIGFLSLLFSDIPPIRDFGIVA
AIGVLLAFLTSLTLLPALLSLLPRPKPKTRRLKKPPELGRLLAKLARFVLRRPKVILVVALVLAVVSLYG
ISRLKVEYDFEDYLPEDSPIRQDLDFIEENFGGSDPLEVVVDTGEPDGLKDPEVLKEIDRLQDYLESLPE
VGKVLSLADLVKELNQALNEGDPKYYALPESRELLAQLLLLLSSPPGDDLSRFVDEDYSAARVTVRLKDL
DSEEIKALVEEVRAFLAENFPPDGVEVTLTGSAVLFAAINESVIESQIRSLLLALLLIFLLLLLAFRSLR
LGLISLIPNLLPILLTFGLMGLLGIPLNIATAVVASIALGIGVDYTIHFLSRYREERRKGGDLEEAIRRA
LRTTGKAILFTSLTLAAGFGVLLFSSFPPLADFGLLLALGLLVALLAALLLLPALLLLLDPRIAKKR
>gnl|CDD|440657 COG1034, NuoG, NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]. NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGM
VVKTDSPKVKKARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLIL
LDMNRCILCTRCVRFCDEIAGDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKA
RPWELKKTPSICPHCSVGCNIRVDVRGGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRK
DGELVEASWEEALAAAAEGLKALKKAENSVGAALLGALPDAAAILEAAEAGKLKALVLLGADPYDLDPAA
ALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRA
LANALGAGLPYDSLEEVRAELAAEAPATVSAEG
>gnl|CDD|440658 COG1035, FrhB, Coenzyme F420-reducing hydrogenase, beta subunit [Energy production and conversion]
EVYAARAKDPEIRKKGQSGGVVTALLAYLLEEGLVDGVVVVGRDDPWKPEPVLATTPEELLAAAGSKYTQ
SPLLEALKEAKLEGGKRVAFVGTPCQIAALRKLQKKDPVLLDNIVLTIGLFCGGNFSPEGLEKFLEELLG
VDPEDVTKLDFWKGKFEIETKDGEVKEIPLKELEDSGYFRRPSCRSCKDYTAELADISVGDVWGIGDPDG
WSTVIVRTEKGEELLEKAVDAGYLELSPLEEAGNLAAVQKLAKRKKKRAKKLLERRGLE
>gnl|CDD|440659 COG1036, AfpA, Archaeal flavoprotein [Energy production and conversion]
MKKPRIAWGITGSGHYLKESLEIMKELKKVYDIDVFLSKAGEEVLKMYGLWDDLLKEFGRVFRDKGASSP
PVGRFYLGKYDTLVIAPATSNTVAKIVLGIADTLVTNAVAQAGKGRVPSIVFPCDTEPEVETEAPGGKKV
KLYPRKIDLENVEKLRKMEGTTVLESPEELEEAL
>gnl|CDD|440660 COG1038, PycA, Pyruvate carboxylase [Energy production and conversion]. Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
MKKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEII
RVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGP
VDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPK
HIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFL
VDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSLDDPEIGIPSQEDIRLNGYAIQCRITT
EDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDSLLVKVTAWGRTFEEAIRKMRRALREF
RIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVNGPPGVKGRPK
PDFPKPKLPKVDLGAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLKI
APATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVR
AFVKEAAEAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKEL
EKAGAHILAIKDMAGLLKPYAAYKLVKALKEEVDLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASM
SGLTSQPSLNSLVAALEGTERDTGLDLDALQELSNYWEAVRKYYAPFESGLKAPTAEVYKHEMPGGQYSN
LRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTPSSKVVGDMALFMVQNGLTPEDVYEKGKDLDFPDS
VVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPVDFDALRAELEEKLGREPSDRDVLSYLLY
PKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPDEDGMRTVFFELNGQ
PREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPR
DGTVKEVLVKEGDQVEAGDLLIEL
>gnl|CDD|440661 COG1039, RnhC, Ribonuclease HIII [Replication, recombination and repair]
MSNIVLKLTDKQIEKLKQYYQKGLTPSEPPYAVFAAKKPGTTITAYKSGKVLFQGKGAEDEAEFWGTKLE
PEILGKAKSEVTTLPANLAFLSHIGSDEVGTGDYFGPLTVAAVYVDKEQIELLKELGVKDSKKLTDDKIR
KLAPQIRETIPYSLLILNPEKYNELQAKGWNLNKLKAWLHNQAIENLLKKIAKPDGILIDQFAEPKVYFK
YLKKEKNIVRENLYFRTKAESDHLAVAAASIIARAAFLKEMDKLSKEAGITLPKGASAKVDQAAAKIIKK
FGEEALRKIAKLHFANTEKALK
>gnl|CDD|440662 COG1040, ComFC, DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only]
LRSLLRALLDLLFPPRCLLCGAAPGGGLCPDCRAKAAFRYEGPLRRLILALKYRGRLDLARLLARLLARA
LREALLPRPDLIVPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLLRRVRATPSQAGLSRAERRRN
LRGAFAVRPPARLAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLARTPR
>gnl|CDD|440663 COG1041, Trm11, tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]. tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification
MKYFFYPGSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEH
YGYEDADVIRGDARDLPLADESVDAIVTDPPYGRSSKISGEELLELYEKALEEAARVLKPGGRVVIVTPR
DIDELLEEAGFKVLERHEQRVHKSLTRYILVL
>gnl|CDD|440664 COG1042, PatZN, Acyl-CoA synthetase (NDP forming) [Energy production and conversion]
MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPP
DLAVIAVPAETVPDVVEECGEKGVKAAVVISAGFAETGEEGAALEQELLEIARRYGMRLLGPNCLGLINP
ATGLNATFAPVPPLPGNIALVSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTR
VILLYLEGIRDGRRFLSAARAAARGKPVVVLKSGRSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVD
DLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADALEDLGLELAELSEETQAALRAVLPPFASVGN
PVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALIEAAKGSGKPVLASWMGGDSVA
EARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPASEDFDPDRERARAIIEAALAEGRGVLTE
AEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAEAVRAAFE
EILARVRAARPDARIDGVLVQPMVPGGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEAL
AREMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLA
PPAPPAPR
>gnl|CDD|440665 COG1043, LpxA, Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]. Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis
MAMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQD
LKYKGEPTRLEIGDNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGH
VEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRA
LKRAYRLLYRSGLTLEEALEELEAELPDSPEVRELLDFIRASKRGIIR
>gnl|CDD|440666 COG1044, LpxD, UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]. UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis
SFTLAELAELLGGELVGDGDLEITGVAPLEEAGPGDLSFLANPKYAKQLATTKASAVIVPPDFAAALPGL
ALIVVDNPYLAFAKLLQLFYPPPAPAPGIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVV
IGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVIGADGFGFAPDEDGGWVKIPQLGRVVIGDDVEIG
ANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIAGHLTIG
DGVIIGAQSGVTKSIPEGGVYSGSPAQPHREWLRNAAALRRLPELAKRLKELEKK
>gnl|CDD|440667 COG1045, CysE, Serine acetyltransferase [Amino acid transport and metabolism]. Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis
MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHP
GATIGRGFFIDHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGD
NAKIGANSVVLKDVPPGSTVVGVPARIVKRKGSK
>gnl|CDD|440668 COG1047, SlpA, Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones]
IEKGDVVTLHYTLKLEDGEVFDSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERD
PELVQTVPREQFPEDEELEVGMQVEFQTPDGQEVPGTVTEVDDDTVTVDFNHPLAGKTLTFDVEVVEV
>gnl|CDD|440669 COG1048, AcnA, Aconitase A [Energy production and conversion]. Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
SMDSFKARKTLTVGGKPYTYYSLPALEEAGGDISRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPK
ARGDDEIPFRPARVLMQDFTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDAL
EKNLELEFERNRERYQFLKWGQQAFDNFRVVPPGTGIVHQVNLEYLAFVVWTREEDGETVAYPDTLVGTD
SHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVG
KFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTGRSEEQIELVEAYAKAQGLWRD
PDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPVGEELDKPVRVEVDGEEFELG
HGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLERAGLLPYLEALG
FNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALAGT
VDIDLTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYD
WDPDSTYIRRPPFFEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKD
FNSYGSRRGNHEVMMRGTFANIRIKNLLAPGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEY
GTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESLGLTGDETFDIEGLDEGL
APGKTVTVTATRADGSTEEFPVLHRIDTPVEVEYYRAGGILQYVLRQLLAA
>gnl|CDD|440670 COG1049, AcnB, Aconitase B [Energy production and conversion]. Aconitase B is part of the Pathway/BioSystem: TCA cycle
MLEAYRKHVAERAALGIPPLPLNAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAA
IAKGEATSPLISPEKAVELLGTMLGGYNVQPLIELLDDAELAPEAAEALSHTLLVFDAFHDVEEKAKAGN
AYAKQVLQSWADAEWFTSRPELPEKITVTVFKVPGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPGPL
KTIAELKAKGHPVAYVGDVVGTGSSRKSATNSVLWHMGEDIPFVPNKRTGGVVLGGKIAPIFFNTAEDSG
ALPIECDVSKLNTGDVIDIYPYEGKITKENGEVISTFELKPDTLLDEVRAGGRIPLIIGRGLTDKAREAL
GLPPSDVFRRPEAPADSGKGYTLAQKMVGKACGVEGVRPGTYCEPKMTTVGSQDTTGPMTRDELKELACL
GFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFISSRGGVSLRPGDGIIHSWLNRMLLPDTVGTGGDSHTR
FPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPYYAIKQGLLTVEKKGKK
NIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCTIKLSKEPVIEYLRSNIALLKWMIAEGYGDARTL
ERRIAAMEEWLANPELLEADADAEYAAVIEIDLNEIKEPILACPNDPDDVKLLSEVAGTKIDEVFIGSCM
TNIGHFRAAGKLLEGKGNLPTRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMGNQARVADG
ATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGRLPTVEEYMEYVKKIDPMADDIYRYLNFDQIEEY
QEKADVVIPVIA
>gnl|CDD|440671 COG1051, YjhB, ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism]
MTKVPKVAVDAVIFRKDGRVLLVRRADEPGKGLWALPGGKVEPGETPEEAALRELREETGLEVEVLELLG
VFDHPDRGHVVSVAFLAEVLSGEPRADDEIDEARWFPLDELPELAFTPADHEILE
>gnl|CDD|440672 COG1052, LdhA, Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, Coenzyme transport and metabolism, General function prediction only]. Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
KPILVLDPRTLPDEVLERLEAEHFEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLI
ANRGVGYDNIDLAAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLLGRD
LSGKTLGIIGLGRIGQAVARRAKGFGMKVLYYDRSPKPEVAELGAEYVSLDELLAESDIVSLHCPLTPET
RHLINAEELALMKPGAILINTARGGLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDHPLLSLPNVVLTP
HIASATEEAREAMAELALDNLLAFLAGEPPPNPVNP
>gnl|CDD|440673 COG1053, SdhA, Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]. Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHTAAAQGGINAAGTNVQKAAGEDSPEEHFY
DTVKGGDGLADQDLVEALAEEAPEAIDWLEAQGVPFSRTPDGRLPQFGGHSVGRTCYAGDGTGHALLATL
YQAALRLGVEIFTETEVLDLIVDDGRVVGVVARDRTGEIVRIRAKAVVLATGGFGRNYEMRAEYLPEAEG
ALSTNAPGNTGDGIAMALRAGAALADMEFVQFHPTGLPGDGGLISEGARGKPGGILVNKEGERFMNEYAP
RDVVSRAILEEIDEPAYLVLDLRHRRRLEEYLEAGYLVKADTIEELAAKLGIDAAELAATVARYNAAAKA
GVDPRGTCLGPIKEGPFYAIPVRPGVHYTMGGLRVDADARVLDADGTPIPGLYAAGEAAGSVHGANRLGG
NSLGDALVFGRIAGRHAAEYAKA
>gnl|CDD|440674 COG1054, TrhO, tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis]
MKPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFA
DLEFKESEADGHPFPRLKVKLKKEIVTMGLPDVDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEI
GTFKGAIDPDTDTFREFPEWVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLE
EVPEEGSLWEGECFVFDERVAVDHNLEPGVIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADKYECCS
DECTEEQRARYERQRQLRLAKERL
>gnl|CDD|440675 COG1055, ArsB, Na+/H+ antiporter NhaD or related arsenite permease [Inorganic ion transport and metabolism]
MMILALAIFVLTYLLIILEPRGLNRAVAALLGAALLLLLGVVSLEDALEAIDWNTILFLLGMMIIVAILD
ESGFFEWLAIKLARRAKGSPRRLLWLLGLLTALLSAFLDNDTTALLLTPVVLAIARRLGLNPVPFLIAIV
FAANIGGAATPIGNPTNIMIASAGGLSFLDFLANLFPPSLVSLLVTLLVLYLLFRKELPAAPDLEDDPKE
AIKDRRLLRISLLVLALLLVGFVLHSFLGLPPALIALLGAAVLLLLARVDVREVLKKVDWSTLLFFIGLF
VVVGGLENTGLLDLLAELLASLTGGNLLLAALLILWLSAILSAVVDNVPLVAALLPLIPDLGATGNPEPL
WLALALGATLGGNLTPIGSAANVIVLGIAEKKGIKISFGEFLKVGLPLTLLTLLIALLYLLLLYF
>gnl|CDD|440676 COG1056, NadR, Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]. Nicotinamide mononucleotide adenylyltransferase is part of the Pathway/BioSystem: NAD biosynthesis
MMKRGLFIGRFQPFHLGHLAVIKWALEEVDELIIGIGSAQESHTPRNPFTAGERIEMIRAALKEEGLSRV
YIVPIPDINNNSLWVSHVKSLVPPFDVVYSNNPLVGRLFKEAGYEVLLPPLFEREEYSGTEIRRLMLEGE
DWESLVPPAVAEVIEEIDGVER
>gnl|CDD|440677 COG1057, NadD, Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]. Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis
MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRF
EVSDIELERPGPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDE
LEELEALKPGGRIILLDVPLLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR
>gnl|CDD|440678 COG1058, CinA, ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair]
KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGP
TPDDLTREAVAEALGVPLVLDPEALALIEERFAKRGREMTENNLKQALLPEGAELLPNPVGTAPGFSIEN
NGKVVIFLPGVPSEMKPMFEEEVLPRLKKLFSGEPIVSRTLRTFGIGESDLAELLEDLEARFPNVTIGSY
PSDGEVRLRLTARGTDEEEAEAALEALEEELRERLGDYI
>gnl|CDD|440679 COG1059, ENDO3c, Thermostable 8-oxoguanine DNA glycosylase [Replication, recombination and repair, Defense mechanisms]
LEEIEEIYNEIKDLIEERIEEFKRLWKEGSEEDLFSELCFCILTANSSAEGGIKAQKELGDNGFFNLSEE
ELEEKLREVGHRFYNTRAEYIVEARKLFGKLKDLIKSFKDPFEAREWLVKNVKGIGYKEASHFLRNIGFF
DLAILDRHILRNLKEYGLIEEIPKTLTKKRYLEIEEKLREISEKLGIPPGELDLYLWYKETGKVFK
>gnl|CDD|440680 COG1060, ThiH, 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]. 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis
EILEKALAGERLSLEDALALLSPAAADLEELAELADELRRRRFGNTVTFVVNRPINLTNVCVNGCKFCAF
SRDNGDIDRYTLSPEEILEEAEEAKALGATEILLVGGEHPDLPLEYYLDLLRAIKERFPNIHIHALSPEE
IAHLARASGLSVEEVLERLKEAGLDSLPGGGAEILDDEVRHPIGPGKIDYEEWLEVMERAHELGIRTTAT
MLYGHVETREERVDHLLHLRELQDETGGFTEFIPLRFRPANTPLYLERPGVSDRELLKLIAVARLFLPNI
GNIQASWVSLGTRLRQLALSLGANDLGGTSMEENIVRAAGGEEGDERSVEELIRLIREAGRIPVERDTLY
R
>gnl|CDD|440681 COG1061, SSL2, Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]
VLLRGIAERGADKLRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEA
GDEASGTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRRELL
EQWAEELRRFLGDPLAGGGKKDSDAPITVATYQSLARRAHLDELGDRFGLVIIDEAHHAGAPSYRRILEA
FPAAYRLGLTATPFRSDGREILLFLFDGIVYEYSLKEAIEDGYLAPPEYYGIRVDLTDERAEYDALSERL
REALAADAERKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEA
FRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDFVGNDVPVLE
ELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLA
LALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEELAALLLKELL
RAALAA
>gnl|CDD|440682 COG1062, FrmA, Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion]
GGPLEIEEVELDEPRPGEVLVRIVAAGLCHSDLHVRDGDLPVPLPAVLGHEGAGVVEEVGPGVTGVAPGD
HVVLSFIPSCGHCRYCASGRPALCEAGAALNGKGTLPDGTSRLSSADGEPVGHFFGQSSFAEYAVVPERS
VVKVDKDVPLELAALLGCGVQTGAGAVLNTAKVRPGDTVAVFGLGGVGLSAVQGARIAGASRIIAVDPVP
EKLELARELGATHTVNPADEDAVEAVRELTGGGVDYAFETTGNPAVIRQALEALRKGGTVVVVGLAPPGA
EISLDPFQLLLTGRTIRGSYFGGAVPRRDIPRLVDLYRAGRLPLDELITRRYPLDEINEAFDDLRSGEVI
RPVIV
>gnl|CDD|440683 COG1063, Tdh, Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]. Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
MKALVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGE
GVTGLKVGDRVVVEPNIPCGECRYCRRGRYNLCENLQFLGIAGRDGGFAEYVRVPAANLVKVPDGLSDEA
AALVEPLAVALHAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGADAV
VNPREEDLVEAVRELTGGRGADVVIEAVGAPAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELT
LRGSRNYTREDFPEALELLASGRIDLEPLITHRFPLDDAPEAFEAAADRADGAIKVVLDPD
>gnl|CDD|440684 COG1064, AdhP, D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism]
MKAAVLTEPGGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVG
PGVTGFKVGDRVGVGWVDSCGTCEYCRSGRENLCENGRFTGYTTDGGYAEYVVVPARFLVKLPDGLDPAE
AAPLLCAGITAYRALRRAGVGPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKLELARELGADHV
VNSSDEDPVEAVRELTGADVVIDTVGAPATVNAALALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRG
SLIGTRADLQEMLDLAAEGKIKPEVETIPLEEANEALERLRAGKVRGRAVLD
>gnl|CDD|440685 COG1066, Sms, DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and repair]
MAKTKTVYVCQECGYESPKWLGRCPECGAWNTLVEEVVAKAKKGRAASGAAGRASKPVPLSEVEAEEEPR
ISTGIGELDRVLGGGLVPGSVVLIGGEPGIGKSTLLLQVAARLAKKGGKVLYVSGEESASQIKLRAERLG
LLSDNLYLLAETDLEAILATIEELKPDLLVIDSIQTMYSEELESAPGSVSQVRECAAELIRLAKETGIAV
FLVGHVTKEGSIAGPRVLEHMVDTVLYFEGDRHSRYRILRAVKNRFGSTNEIGVFEMTEKGLREVSNPSE
LFLSERDEPVPGSAVTVTMEGTRPLLVEVQALVSPSSFGNPRRTAVGLDSNRLAMLLAVLEKRAGLPLGD
QDVYVNVVGGLKITEPAADLAVALAIASSFRDRPLPPDTVFFGEVGLTGEIRPVSRIEQRLKEAAKLGFK
RAIVPKGNKKKLKPKGIEIIGVSTLEEALEALF
>gnl|CDD|440686 COG1067, LonB, Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones]
SLLSESLLLLLLLLALLDAILSLPTEALDALALALLLDPRALRFRLLGALGLGRLPLGLGRALEGLGTGL
LIRLLLENREAAGPEGDGKLYLEALLLEEKAAALLAAALRLYLGEFLELLLPEALELLEGEAEELLEDLD
ELEREEIEEKIEELEEELRELLRQLPQWEREAREKLRELNREVALFAVGPLIEELKEKYADLPKVLEYLE
AVKEDILENLEDFLPEEEEEEPLAEALLREKFFRRYRVNLLVDNSETQGAPVIYEDNPTYQNLFGRIEYR
AEMGALVTDFTLIKPGALHRANGGYLILDAEDLLSNPFAWEALKRALRSGEIRIESLGEELGLISTVSLE
PEPIPLDVKVILIGDRELYYLLYEYDPEFRELFKVKADFDDEMPRTDENIRAYARFIASICREEGLRPFD
RSAVARLIEYSSRLAEDQEKLSTRFAEIADLLREADYWARKAGAELITAEHVEQALDAKEYRSNRIEEKI
QESILDGTILIDTEGEKVGQINGLSVLDLGDYSFGRPSRITATVYLGKGGVIDIEREVELSGPIHSKGVL
ILSGYLGARYAQDKPLSLSASLVFEQSYGGVDGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQ
PIGGVNEKIEGFFDVCKARGLTGKQGVIIPAANVKNLMLRDEVVEAVKAGQFHIYAVEHVDEAIELLTGL
PAGERDEDGRYPEGSVNGRVQARLKELAELAKKFSKKKKKKK
>gnl|CDD|440687 COG1069, AraB, Ribulose kinase [Carbohydrate transport and metabolism]
EKYVIGVDFGTDSVRAVVVDAADGEELASAVHPYPRWVIGLYLPPPPDQARQHPLDYLEALEAAVREALA
QAGVDPADVVGIGVDATGCTPVPVDADGTPLALLPEFAENPHAMVILWKDHTAQEEAERINELAKARGED
YLRYVGGIISSEWFWPKILHLLREDPEVYEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAHEGGY
PSEEFFAALDPLLDGLADRLGTEIYPLGEPAGTLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGVEPG
TLVKVMGTSTCHMLVSPEERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEE
RGISLHPLLTEEAAKLPPGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTR
AIIERFEEEGVPIDEIIACGGIATKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEE
AMAAMGSGFDKVYTPDPENVAVYDALYAEYLQLHDYFGRGRN
>gnl|CDD|440688 COG1070, XylB, Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]. Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEE
IAAIGVSGQMHGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWL
KENEPEIFARIAKVLLPKDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPP
GEVAGTLTAEAAAETGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRV
HTFCHAVPGRWLPMGATNNGGSALRWFRDLFADGELDDYEELNALAAEVPPGADGLLFLPYLSGERTPHW
DPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLG
RPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDELYERYRELYPALKP
LFER
>gnl|CDD|440689 COG1071, AcoA, TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]. TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
LVQVLDPDGTEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRP
GDWIFPTYRDHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAA
LAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAG
YGIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERDPI
ERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYAEPPPHLAEQRAELAA
>gnl|CDD|440690 COG1072, CoaA, Panthothenate kinase [Coenzyme transport and metabolism]. Panthothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
MSDTDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRL
HRATSAFLGQADKKTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLM
DRKGFPESYDRRGLLRFLARVKSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEPNPWL
FVSDFFDFSIYVDADEEDLREWYVERFLKLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLA
ENILPTRSRADLILRKGADHSVERVRLRK
>gnl|CDD|440691 COG1073, FrsA, Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]
IFPPSDKVNKEDVTFKSRDGIKLAGDLYLPAGASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAF
DYRGYGESEGEPREEGSPERRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDS
PFTSLEDLAAQRAKEARGAYLPGVPYLPNVRLASLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSE
DLYEAAAEPKELLIVPGAGHVDLYDRPEEEYFDKLAEFFKKNL
>gnl|CDD|440692 COG1074, RecB, 3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair]
MSEPPWTDAQRRALDPLGGSVLVEASAGSGKTYTLVARYLRLLLERGLDPEEILVVTFTRAAAAEMRERI
RERLAEAADLEDPDLEELARARRRLARALENLDRAAISTIHSFCQRLLREFAFEAGLDPNFELLDDAEAL
LLEEAVDDLLREAYAPLDALALARLLDAFGRDDDSLEELLLALYKLRSRPDWLEELAELDEALEALREAL
LKAKEALAALREALAAAAAPLLAALLRLLAAVLARYERRKRERGLLDFDDLLHRALRLLRDEDAPWVAER
LRERYRHILVDEFQDTSPLQWEILRRLAGEALADGRTLFLVGDPKQSIYRFRGADPELFLEARRALEGRV
DGERLTLTTNFRSTPEVVDAVNALFAQLMGAGFGEIPYEPVEALRPGAYPAVELWPLEPDDVSEEDARER
EARAVAARIRRLLAEGTTVEGGGRPVRPGDIAVLVRTRSEAAAIARALKAAGIPVAASDRLSLFESPEVR
DLLALLRALLNPEDDLALAAVLRSPLFGLSDEDLAALAADRKGESLWEALRAYERLARALERLRALRELA
RRLGLAELLERLLEETGLLERLLALPGGERRLANLLHLDELLQLALEYEQTGGPGLAGFLRWLERLIEDG
GDEEKRRLESDADAVRIMTIHKSKGLEFPVVFLPALRERARAEELAEELRLLYVALTRARDRLVLSGAVK
KKDAEKESSWLARRGTLVHRLLEHLDFSAPAELRAALARLLARGGLDEEEAEALAEALLAFLATPLLAEL
FAAAEVLREVPFLLPDLYRGLGGLLKGRIDLVFEDDGRVYIVDYKTNRLGPDDEEYLPERYRLQLALYAL
ALERLLPGRPVRAGLYFTDRGRLVEI
>gnl|CDD|440693 COG1075, EstA, Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism]
YAATRYPVVLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDSAEQLAAFVDAVLAATGAEKV
DLVGHSMGGLVARYYLKRLGGAAKVARVVTLGTPHH
>gnl|CDD|440694 COG1076, DjlA, DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]
MQLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRLAAGLPEEEQRLALQKAAAINEAYETLKDPRGID
LAAPA
>gnl|CDD|440695 COG1077, MreB, Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]
MLFGLFSKDIGIDLGTANTLVYVKGKGIVLNEPSVVAIDKKTGKVLAVGEEAKEMLGRTPGNIVAIRPLK
DGVIADFEVTEAMLKYFIKKVHGRRSFFRPRVVICVPSGITEVERRAVRDAAEQAGAREVYLIEEPMAAA
IGAGLPIEEPTGNMVVDIGGGTTEVAVISLGGIVVSRSIRVAGDELDEAIIQYVRKKYNLLIGERTAEEI
KIEIGSAYPLEEELTMEVRGRDLVTGLPKTITITSEEIREALEEPLNAIVEAIKSVLEKTPPELAADIVD
RGIVLTGGGALLRGLDKLLSEETGLPVHVAEDPLTCVARGTGKALENLDLLRRVLISSD
>gnl|CDD|440696 COG1078, YdhJ, HD superfamily phosphohydrolase [General function prediction only]
MKIIRDPVHGYIEVDELELDLIDTPEFQRLRRIKQLGLAYLVYPGAEHTRFEHSLGVMHLARRALDRLRR
KGVEIDEEERELVRAAALLHDIGHGPFSHAFEEVLLTGVDHEEITLRIIEENEINGILEKHGIDPELVAD
IIKGEYPNKFLRQLISSQLDADRMDYLLRDSYYTGVSYGNIDLERLIRMLRVVDDELVVEEKGIYAVESF
LIARYLMYWQVYFHKTSRAAEVMLRRALERAKELYDEGELENPLDLEDFLRLDDYDLLSALKEWQDHPDP
ILSDLARRLLNRKLFKRVILIVDKNGKIRELSEVSPLVNALAGSKRVKKLRVYYPKELRE
>gnl|CDD|440697 COG1079, NupQ, ABC-type guanosine uptake system NupNOPQ, permease subunit NupQ [Nucleotide transport and metabolism]
MSDMDILASLLAATLRAATPLLLAALGGLFSERAGVLNIGLEGMMLMGAFAGFAVAYLTGSPWLGLLAAA
LAGALLALLHAFLTITLRANQIVSGLALNLLALGLTAFLGRLLFGQGGQTPSIPGLPPIPIPGLSDIPVL
GPLLFGQSPLVYLALLLVPLVWWVLYRTRFGLRLRAVGENPAAADALGINVYRIRYLAVLIGGALAGLGG
AYLSLGYVGSFTEGMTAGRGFIALAAVIFGRWRPLGALLAALLFGFADALQLRLQALGIGIPSQLLLMLP
YVLTILVLAGFSGRARAPAALGKPYVKEE
>gnl|CDD|440698 COG1080, PtsA, Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate transport and metabolism]
LKGIAASPGIAIGKAFLLREEDLEVPEYTISPEDVEAEIARLEAALAKAREELEALREKAPEDLGEEEAA
IFDAHLLLLEDPELIEEVEELIREGRYNAEWALKEVIEELAAQFEALDDEYLRERAADIRDVGRRVLRNL
LGVEAPDLSDLPEPVILVAHDLTPSDTAQLDPSRVAGFVTDLGGRTSHTAILARSLGIPAVVGLGDALLL
VKDGDLVIVDGDAGVVIVNPDEETLAEYRERQAEYAAERAELARLRDLPAVTLDGVRVELAANIGLPEDA
AAALENGAEGVGLFRTEFLFMDRDDLPTEEEQFEAYRAVAEAMGGRPVTIRTLDIGGDKPLPYLPLPKEE
NPFLGLRAIRLCLDRPELFRTQLRAILRASAHGNLRIMFPMISSVEELRQAKALLEEAKAELRAEGIPFD
EDIPVGIMIEVPAAALIADQLAKEVDFFSIGTNDLIQYTLAVDRGNEKVAYLYDPLHPAVLRLIKMVIDA
AHKAGKPVGVCGEMAGDPLATPLLLGLGLDELSMSPSSIPAVKAIIRRLDLAEARALAEKALALDTAEEV
RALLEEFLAEL
>gnl|CDD|440699 COG1082, YcjR, Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism]
MKLGLSTYSLPDLDLEEALRAAAELGYDGVELAGGDLDEADLAELRAALADHGLEISSLHAPGLNLAPDP
EVREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAWDRLAERLRELAELAEEAGVTLALENHE
GTFVNTPEEALRLLEAVDSPNVGLLLDTGHALLAGEDPVELLRKLGDRIKHVHLKDADGDQHLPPGEGDI
DFAAILRALKEAGYDGWLSLEVESDPDDPEEAARESLEYLRKLL
>gnl|CDD|440700 COG1083, NeuA, CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis]
MKILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLRP
AELAGDTASTIDVILHALEWLEEQGEEFDYVVLLQPTSPLRTAEDIDEAIELLLESGADSVVSVTEAHHP
PYWALKLDEDGRLEPLNPDPHNRPRRQDLPPAYRENGAIYIFKREALLENKSRFGGKTGAYEMPEERSVD
IDTEEDFELAEALLKKRK
>gnl|CDD|440701 COG1084, Nog1, GTP-binding protein, GTP1/Obg family [General function prediction only]
MPFEKIPTVPTADELIDKAFRRAARAGRAKRGLEKGREAEESRLRTAANILSDNLENIVRKFPDFDELHP
FYRELADILVGVDELKKSLSAVSWASRKIKEISREYIRKIRRADSDEARKLRKEAFGRIASVVRRIDDDL
LFLNEARNKLRKLPDIDPDLPTIVVAGYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQ
VIDTPGLLDRPLSERNEIERQAILALKHLADVILFLFDPSETCGYSLEEQLNLLEEIRSLFDVPVIVVIN
KIDLSDEEELKEAEEEADIKISALTGEGVDELLDELIEALEEEPELPPEE
>gnl|CDD|440702 COG1085, GalT, Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism]
PPPDMPELRYDPLTGEWVLIAPHRAKRPWDGPVEKPEDPPEYDEDCPLCPGNERATPPEIPPPGWDVRVF
PNKFPALSPEAPDAREGDGLYDAMPGRGRHEVICFSPDHDLSLAELSVERIRDVLEAWRDRTAELGADPR
IRYVQIFENRGAEAGASLPHPHGQIIAYPFVPPRIARELRGARAYYEEHGRCLLCDILAQELAAGERVVA
ENEHFVAFVPFAARWPFETWILPKRHVSDFEELTDEERDDLARILKRVLRRLDNLLGDFPYNMGLHQAPV
DGEERDHYHWHLEIYPRLRSATVLKFLAGFELGAGAFINDVTPEQAAERLREVSEV
>gnl|CDD|440703 COG1086, FlaA1, NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones]
LLLRLLLRLLLRRLRRRGRNKRRVLIVGAGEAGRQLARALRRNPDLGYRVVGFVDDDPDKRGRRIEGVPV
LGTLDDLPELVRRLGVDEVIIALPSASRERLRELLEQLEDLGVKVKIVPDL
>gnl|CDD|440704 COG1087, GalE, UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis]
MKILVTGGAGYIGSHTVVALLEAGHEVVVLDNLSNGHREAVPKGVPFVEGDLRDRAALDRVFAEHDIDAV
IHFAALKAVGESVEKPLKYYRNNVVGTLNLLEAMREAGVKRFVFSSSAAVYGEPESVPITEDAPTNPTNP
YGRSKLMVEQILRDLARAYGLRYVALRYFNPAGAHPSGRIGEDHGPPTHLIPLVLQVALGKREKLSVFGD
DYPTPDGTCVRDYIHVVDLADAHVLALEYLLAGGGSEVFNLGTGRGYSVLEVIDAFERVTGRPIPYEIAP
RRPGDPAALVADSEKARRELGWKPKYDLEDIIADAWRWQQKNPNGYRD
>gnl|CDD|440705 COG1088, RfbB, dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis]
MMRILVTGGAGFIGSNFVRYLLAKYPGAEVVVLDKLTYAGNLENLADLEDDPRYRFVKGDIRDRELVDEL
FAEHGPDAVVHFAAESHVDRSIDDPAAFVETNVVGTFNLLEAARKYWVEGFRFHHVSTDEVYGSLGEDGP
FTETTPLDPSSPYSASKAASDHLVRAYHRTYGLPVVITRCSNNYGPYQFPEKLIPLFITNALEGKPLPVY
GDGKQVRDWLYVEDHCRAIDLVLEKGRPGETYNIGGGNELSNLEVVELICDLLGKPESLITFVKDRPGHD
RRYAIDASKIRRELGWKPKVTFEEGLRKTVDWYLDNRDWWEPLKSGAYREERY
>gnl|CDD|440706 COG1089, Gmd, GDP-D-mannose dehydratase [Cell wall/membrane/envelope biogenesis]
KTALITGITGQDGSYLAELLLEKGYEVHGIVRRSSTFNTERIDHLGIDDRLFLHYGDLTDSSSLIRIIQE
VQPDEIYNLAAQSHVGVSFEQPEYTADVTALGTLRLLEAIRILGPKTRFYQASSSEMFGLVQEVPQSETT
PFYPRSPYAVAKLYAHWITVNYREAYGLFACNGILFNHESPRRGETFVTRKITRAVARIKLGLQDKLYLG
NLDAKRDWGHAPDYVEAMWLMLQQDKPDDYVIATGETHSVREFVELAFAEVGLDWEWKVYVEIDPRYFRP
AEVDLLLGDPSKAKKKLGWKPKTSFEELVREMVEADLELLK
>gnl|CDD|440707 COG1090, YfcH, NAD dependent epimerase/dehydratase family enzyme [General function prediction only]
KILITGGTGFIGSALVAALLARGHEVVVLTRRPPKAPDEVTYVAWDPETGGIDAAALEGADAVINLAGAS
IADKRWTEARKQEILDSRVDSTRLLVEAIAAAANPPKVLISASAIGYYGDRGDEVLTEDSPPGDGFLAEV
CRAWEAAAAPAEEAGTRVVLLRTGIVLGPDGGALPKLLPPFRLGLGGPLGSGRQWMSWIHIDDLVRAILF
LLENPDLSGPVNAVAPNPVTNAEFTRALARVLHRPAFLPVPAFALRLLLGEMAELLLASQRVLPKRLLEA
GFTFRYPTLEEALRDLLG
>gnl|CDD|440708 COG1091, RfbD, dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis]
RILVTGANGQLGRALVRLLAERGYEVVALDRSELDITDPEAVAALLEEVRPDVVINAAAYTAVDKAESEP
ELAYAVNATGPANLAEACAELGARLIHISTDYVFDGTKGTPYTEDDPPNPLNVYGRSKLAGEQAVRAAGP
RHLILRTSWVYGPHGKNFVKTMLRLLKEGEELRVVDDQIGSPTYAADLARAILALLEKDLSGIYHLTGSG
ETSWYEFARAIAELAGLDALVEPITTAEYPTPAKRPANSVLDNSKLEATLGIKPPDWREALAELLAELA
>gnl|CDD|440709 COG1092, RlmK, 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]. 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification
KVRLKPGKERRLRRGHPWVFSNEIDRVEGELEPGDLVEVEDADGRFLGRGYYNPHSQIAVRLLSRDPDEP
IDAAFFANRLRKALALRRKLAKREGTNAYRLVHGEADGLPGLIVDRYGDVLVVQEYSAGMERRRDEILEA
LVEVLGPEGIYLRSDVRVRQLEGLPQYEGVLYGEAPEEVEVEENGLKFLVDLTDGQKTGLFLDQRENRAR
VAELAKGKRVLNLFSYTGGFSVHAAAGGAKSVTSVDLSATALEWAKENAALNGLDDRHEFVQADAFDWLR
ELAREGERFDLIILDPPAFAKSKKDLFDAQRDYKDLNRLALKLLAPGGILVTSSCSRHFSLDLFLEILAR
AARDAGRRVRIIERLTQPPDHPVLPAFPEGEYLKGLLLRVLP
>gnl|CDD|440710 COG1093, SUI2, Translation initiation factor 2, alpha subunit (eIF-2alpha) [Translation, ribosomal structure and biogenesis]. Translation initiation factor 2, alpha subunit (eIF-2alpha) is part of the Pathway/BioSystem: Translation factors
VMKRKELPEEGELVVGTVKEVKDFGAYVTLDEYEGKEGFIHISEVASGWIKNIRDYVREGQKVVCKVLRV
DPKRGHIDLSLKRVNEHQRREKIQEWKNEQKAEKLLEIAAEKLGKSLDEAYEEVGWKLEDEYGSLYDAFE
EAAIEGPEALEDAGLPEEWIDAIVEIAKENIKVPKVKISGYVELTSLAPDGVERIKKALKAAEENIEPED
VDVEITYVGAPRYRIEVTAPDYKTAEKALKKAAEKAIKAIKKLGGEGEF
>gnl|CDD|440711 COG1094, Krr1, rRNA processing protein Krr1/Pno1, contains KH domain [Translation, ribosomal structure and biogenesis]
MQYVKIPKDRIGVLIGKGGETKKEIEEKTGVKLDIDSETGEVTIEPGEDPLAALKARDIVKAIGRGFSPE
KALRLLDDDYMLEVIDLPDVGKSPNALDRIKGRIIGREGRTRRIIEELTGVDISIYGKTVAIIGDFDQVE
IAREAIEMLIDGRIHPTVYEFLEKARRELKRRRLELY
>gnl|CDD|440712 COG1095, RPB7, DNA-directed RNA polymerase, subunit E'/Rpb7 [Transcription]. DNA-directed RNA polymerase, subunit E'/Rpb7 is part of the Pathway/BioSystem: RNA polymerase
MYKLVELEDVVRIPPSLFGEPLEEAALEILREKYEGRVDKDLGIIVAVLDVKVIGEGKIVPGDGATYHDV
EFDALTFKPELQEVVEGEVVEVVEFGAFVRIGPIDGLLHISQIMDDYVDYDEKNGRLIGKESKRTLKVGD
VVRARIVAVSLNEKSPRDSKIGLTMRQPGLG
>gnl|CDD|440713 COG1096, Csl4, Exosome complex RNA-binding protein Csl4, contains S1 and Zn-ribbon domains [Intracellular trafficking, secretion, and vesicular transport]
MKVKEGDFVLPGDVLAVIEEFLPGEGTYEEDGKIRAAVVGKVVIDDKNRVISVKPKKKPPPVPKKGDIVI
GEVVDVRESMALVKIYAIEGNERELPSSFSGIIHISQVSDSYVKDLSDEFRVGDIVRAKVISTLPPIQLS
IKEPDLGVIKAKCSKCGSPLVKDGDKLKCPNCGNVEKRKLSTDYGKGEIRK
>gnl|CDD|440714 COG1097, Rrp4, Exosome complex RNA-binding protein Rrp4, contains S1 and KH domains [Intracellular trafficking, secretion, and vesicular transport]
KIYVEDRKIVVPGDLLAEGEYKPGSGTYVEGGKIYSTVLGLVEIKDDKVSVIPLEGKYIPKVGDLVIGKV
TDVGPSNWEVDINSPYQALLPVSEVPGRPFNVESDDLRKYLDIGDYILAKVKNFDRTRDPLLTMKDKGLG
KIEGGRIVEISPSKVPRVIGKKGSMINMLKKETGCEIIVGQNGRIWIKGPDEEGEELAIEAIKKIEREAH
TSGLTDRIKEFLEEEKGERGVSSE
>gnl|CDD|440715 COG1098, YabR, Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function prediction only]
MSIEVGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIADGYVKDINDYLKVGDEVKVKVLSIDEDGKIS
LSIKQAEEKPKRPPRPRRNSRPKAGFESFEDKLSKFLKDSDERLSDLKKRTESKRGGRGR
>gnl|CDD|440716 COG1099, COG1099, Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only]
MRIIDPHIHMTSRTTDDYEAMAAAGVVAVIEPAFWLGQPRTSAGSFRDYFDSLVGWERFRAAQFGIKHYC
TLGLNPKEANNRRLAEEVLELLPRYLDKEGVVAIGEIGLDDQTPEEEEVFREQLELARELDLPVLVHTPH
RDKKEGTRRILDVLRESGLDPERVLIDHNNEETVKLVLDTGFWAGFTIYPSTKMSPERAVDILEEYGTER
ILVNSAADWGPSDPLAVPKTALEMLRRGIDEEDIRKVVYENPLAFFGQSG
>gnl|CDD|440717 COG1100, Gem1, GTPase SAR1 family domain [General function prediction only]
MGEKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTNGVTIDKKELKLDGLDVDLVIWDTPGQDEFRETR
QFYARQLTGASLYLFVVDGTREETLQSLYELLESLRRLGKKSPIILVLNKIDLYDEEEIEDEERLKEALS
EDNIVEVVATSAKTGEGVEELFAALAEILRGEGDSLD
>gnl|CDD|440718 COG1101, PhnK, ABC-type uncharacterized transport system, ATPase component [General function prediction only]
MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV
TKLPEYKRAKYIGRVFQDPMMGTAPSMTIEENLALAYRRGKRRGLRRGLTKKRRELFRELLATLGLGLEN
RLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNME
QALDYGNRLIMMHEGRIILDVSGEEKKKLTVEDLLELFEEIRGEELADDRLLLG
>gnl|CDD|440719 COG1102, CmkB, Cytidylate kinase [Nucleotide transport and metabolism]
MVITISREPGSGGTTIAKRLAEKLGLPLYDGEILREAAKERGLSEEEFEKLDEKAPSLLYRDTAEEDEID
RALDKVIRELARKGNCVIVGRLADWILRDRPNVLKVFLTAPLEVRVKRIAEREGISEEEAEKEIKKRDKS
RAKYYKYYYGIDWGDPSNYDLVINTSRLGIEEAVDLILAAIEAREKKE
>gnl|CDD|440720 COG1103, COG1103, Archaeal Cys-tRNA synthase (O-phospho-L-seryl-tRNA:Cys-tRNA synthase) [Translation, ribosomal structure and biogenesis]
LDKYNIEIRRVEEGYINIDPIQRGGRLTPEARKALIEWGDGYSVCDYCRGRLDKIKKPPIAEFHEDLAEF
LNMDEVRVTPGAREGKFAVMHSLVEKGDTVVLDGLAHYTSYLAAERAGLNVREVPNSGYPDYKITPEAYA
EKIEEVIRETGKPPALALLTHVDGNYGNLHDAKKIAKVAHQYDIPLLLNGAYTVGRMPVDGKKLGADFVV
GSGHKSMAASAPSGVLATTEEYADKVFRTSKMRGDVTGRTFGIKEVEMLGCTLRGAPLVTMMASFPHVVE
RVKHWDEEVKKARWFVEELERIEGTKQLGEKPRNHDLMRFETPSFDEIAQTHKKRGYFLYDELKKRGITG
IKPGLTKVFKLSTYGLSREQLEYVADAFKEIAEKYGLEVN
>gnl|CDD|440721 COG1104, NifS, Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism]
MMMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSG
GTEANNLAIKGAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPD
TALVSVMHANNETGTIQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVG
ALYVRKGVRLEPLIHGGGQERGLRSGTENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIP
GVVINGDPENRLPNTLNFSFPGVEGEALLLALDLAGIAVSSGSACSSGSLEPSHVLLAMGLDEELAHGSI
RFSLGRFTTEEEIDRAIEALKEIVARLRKLS
>gnl|CDD|440722 COG1105, FruK, 1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]
ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELL
DEEGIPTDFVPIEGETRINIKIVDPSDGTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPP
GVPPDFYAELIRLARARGAKVVLDTSGEALKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELL
ERGAENVVVSLGADGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGA
AAALSPGTGLPDREDVEELLAQVE
>gnl|CDD|440723 COG1106, COG1106, ATPase/GTPase, AAA15 family [General function prediction only]
MLISFSIENFRSFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVEPF
LLDSESKNEPSEFEILFLLDGVRYEYGFELDKERIISEWLYFLSTAAQLNVPLLSPLYDWFDNNISLDTS
SDGLTLLLKEDESLKEELLELLKIADPGIEDIEVEEEEIEDLVERKLIFKHKGGNVPLPLSEESDGTKRL
LALAGALLDALAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTHSTELLDAFLELLRRDQ
IWFVEKDKDGASELYSLEDFKVRKDENLEKGYLQGRYGAIPFLEDLELRG
>gnl|CDD|440724 COG1107, COG1107, Archaea-specific RecJ-like exonuclease, contains DnaJ-type Zn finger domain [Replication, recombination and repair]
MGSCIICGKPVDGEICDSCHEEDVVYELDPGCTPDDLEPGRYYRGTVDGVADFGVFVDLNDHVTGLLHRS
ELDQDWEVGDEVFVQVKEVRDNGNVDLGWVSIDSYETVEVEKELPRTTIGDLEDRVGETVRIEGEVVQVK
QTGGPTIFTVRDETGTVDCAAFEEAGVRAYPEVEVGDIVRVTGEVERRRGELQIETESLEVLEGEEAEAV
RERLEEALDERAEPADVEPLVESEALEKLRPDLRDAAKAIRRAVLEGRPIVVRHHADADGYCAGVAIERA
VLPLIREVHGDPDAEYHYFKRRPSKAPFYEMEDVTRDLTFALEDRERHGQKLPLVVLVDNGSTEEDVPAY
ELLKVYDIPIVVVDHHHPDEAVDDYVDAHVNPYLVGGDYDITTGMLATELARMINPDVTDDLRHLPAVAG
WGDRSEAPEAEDYIDLAEDAGYDEEDLRDIAEALDLEAFYLRYNDGRELIDDLLFVGDEDRHRELVEHLS
EQARRKLDTQLEAAMPHVKHEELPNGAHLNVLDVEAYAHRFTFPPPGKTLGELHDRKVERTEGEPVITIG
YGPDFAVLRSTGVRLDIPEMVEELAEEIPGAGVSGGGHLVVGSIKFVEGMREAVLDALVEKIAEAE
>gnl|CDD|440725 COG1108, ZnuB, ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and metabolism]
YDFMQRALLAGLLVGLACGLLGVFLVLRRMSLIGDALSHAALPGVALAFLLGLSPLLGALVAGLLAALLI
GLLRRRSRLKEDTAIGIVFSGGFALGVLLISLVPGSAVDLMSYLFGSILAVSRSDLLLLAVLAAVVLLLL
LLFYRELLLVSFDPELARASGLPVRLLHLLLLVLLALTVVAALQAVGALLVSALLIIPAATARLLTRSLR
RMLLLAVLIGVLSSVLGLYLSYYLDLPTGPTIVLVAGLLFLLSLLFSPRR
>gnl|CDD|440726 COG1109, ManB, Phosphomannomutase [Carbohydrate transport and metabolism]
MTYKKLFGTDGIRGIVGEELTPEFVLKLGRAFGTYLKEKGGPKVVVGRDTRLSSPMLARALAAGLASAGI
DVYDLGLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRA
EAEEIGKVTRIEDVLEAYIEALKSLVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDG
NFPNHNPNPEPENLEDLIEAVKETGADLGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGPGGT
VVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRETGAVLGGEESGGIIFPDFVPTDDGILAALLLL
ELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKIGAVMEKLREAVEDKEELDTIDGVKVDLEDGGWVLV
RPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEAL
>gnl|CDD|440727 COG1110, TopG2, Reverse gyrase [Replication, recombination and repair]
GGAMLLAVYRRMCPNCGGPISDDRLSKGLPCEKCLPEKLKVEDLEEVAEALEELGTLKGLKKLYNLEEEL
EEFEEFFEKATGSRPWSAQRTWARRLLLGKSFAIIAPTGVGKTTFGLVTSLYLAKKGKKVYIVVPTTPLV
LQVEERLKAFAEKAGVNVRIVAYHSKLSKKEKKEVLEKIESGDFDILITTSAFLARNFDILKKYKFDFIF
VDDVDSVLKSSKNIDRVLKLLGFSEEDIELALELIKLRRRLAKLLQNEEKLEKLREEIEELEKKLEELKR
ERIGVLIVSSATGRPRGKRVKLFRELLGFEVGGRAEGLRNVVDSYILPDEDLEEKLVELVKKLGKGGLVF
VPIDLGKEYAEELAEELNENGIKAELYTSKNKEAIKKFERGEIDVLVGVASYYGVLVRGIDLPHRIRYAV
FAGVPKHKFSLKLELPSPRRLLRLLSVLREVLEEEVREKAESLLAYLRRILRRLSPAEIQKLAEELLEGG
VLPEAAEVIKEAKEFLREKLSREDVLEKLEESEDVSLVREGGKLYILVPDVATYIQASGRTSRLYAGGIT
KGLSVVIVDDEKLFEGLKRRLRWYLEEFEFKPLEEINLDELLKEIDEDRKKVREILEGKVKPEKKDLVKT
ALVIVESPNKARTIASFFGKPSRRRIGGLRVYEVSIGDYLLLITASGGHVFDLVTEAYARGFYGVLVENG
RFIPVYDTIKRCLDCGEQFTDEVEVCPRCGSPNIVDSLEIVEALRELATEVDEVLIGTDPDTEGEKIGWD
VYNLLRPYAKNIKRIEFHEVTRKAILEALKNPREIDENLVEAQIVRRIEDRWIGFTLSQKLWKVFGNRNL
SAGRVQTPVLGWIIERYEESRKSKKYLIILTLENGRLELSIEDLKEAEEVRKALEKEVKVKVKKVEEEEE
ELNPLPPYTTDTLLRDASRRLGLSAEETMRLAQDLFESGLITYHRTDSTRVSDAGIAVAKEYISERFGEE
YFKPRRWGEGGAHEAIRPTRPLDAEDLRRLIEEGVIELPIPLTRRHLRLYDLIFRRFMASQMRPAKVEKV
KLRVSLELPGGEIEEERIVEIIEDGFLLIYPPIKVEPELKEGEYKVTEVKIRKVPKVPLYTQGDLVREMK
ERGIGRPSTYAKIVETLLRRGYVVESKKGKKLVPTKLGIEVYNYLSENFPDLVSEERTRELEEKMDEIEE
GEADYQDVLEELYNELRELVLSPESELGA
>gnl|CDD|440728 COG1111, MPH1, ERCC4-related helicase [Replication, recombination and repair]
TIERRLYQLNLAASALRKNTLVVLPTGLGKTAVALLVIAERLHKKGGKVLFLAPTKPLVEQHAEFFKEAL
NIPEDEIVVFTGEVSPEKRKELWEKARIIVATPQVIENDLIAGRIDLDDVSLLIFDEAHRAVGNYAYVYI
AERYHEDAKDPLILGMTASPGSDEEKIEEVCENLGIENVEVRTEEDPDVAPYVHDTEVEWIRVELPEELK
EIRDLLNEVLDDRLKKLKELGVIVSTSPDLSKKDLLALQKKLQRRIREDDSEGYRAISILAEALKLRHAL
ELLETQGVEALLRYLERLEEEARSSGGSKASKRLVSDPRFRKAMRLAEEADIEHPKLSKLREILKEQLGT
NPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQASKEGDKGLTQKEQIEILERFRAGEFNVLVATSV
AEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGRVVVLIAKGTRDEAYYWSSRRKEKKMKSILKK
LKKLLDKQEKEKLKESAQATLDEFESIKELAEDEINEKDLDEIESSENGAHVDWREPVLLQVIVSTLAES
LELRELGEKVDDEVNLILEIDRVDVVDDGSVLRVSRLLVEIGELDGKTRVIIASYGDEYFDAILRLTSKI
KLPSLVSDISVDIPDLPIVEIVGEAVLCKKEDGSREARFIKKERDLKGIRLAEGETLNDPLIELLRQQLY
GEALREETETAAVVRILA
>gnl|CDD|440729 COG1112, DNA2, Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]
ELALLLDAARALLALLALALLALLLALALLLDLLLLLLLAAALLLLALALALLLLALRALELLDLLAALA
LLLLLLLLDAELLLLALRALLLLLAAELLLLLLLLLLLAALLLALAALLLALALLLLALALLALLALLLA
ELLDLLAALAALAALLAALLLLLLLLAALLLLDLRLLALLELLLAAALALALLALLALALEDELALLLLL
LLLALLLLLALLLLLDALLLLLAALALLALALLLALLLLLLALLLLAALALLRAALRLDLLAALELLAAL
SLALLALLAALALALLLLAALALLLALALAALLALLALLALLAARLAAALAALLLLLLLEELALLAALLL
LLELALLRLLAALLLALALLLLLALEELLLLALLRLLAEGLALLLLLLLAALLRLARALLLLALLLAAAA
AALAALLLLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIE
EHPEELEKLIAELREAARLRRALRRELKKRRELRKLLWDALLELAPVVGMTPASVARLLPLGEGSFDLVI
IDEASQATLAEALGALARAKRVVLVGDPKQLPPVVFGEEAEEVAEEGLDESLLDRLLARLPERGVMLREH
YRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDSPLVFIDVDGVYERRGGSRTNPEEAEAVVELVREL
LEDGPDGESIGVITPYRAQVALIRELLREALGDGLEPVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRNF
GFLNGGPRRLNVAVSRARRKLIVVGSRELLDSDPSTPALKRLLEYLERA
>gnl|CDD|440730 COG1113, AnsP, L-asparagine transporter or related permease [Amino acid transport and metabolism]
MSTSAAASEEEGLKRGLKNRHIQMIALGGAIGTGLFLGSGKAIALAGPAVLLSYLIAGLIVFLVMRALGE
MAVANPVSGSFSDYAREYLGPWAGFVTGWLYWFFWVLVGMAEATAVGIYLQFWFPDVPQWVWALVFLVLL
TAINLLSVKLFGEFEFWFALIKVVAIVAFIVVGLLLIFFGFGLPGGPPAGLSNLWDHGGFFPNGIGGVLA
ALQIVVFAFGGIELVGIAAAEAKDPEKTIPKAINSVIWRILLFYVGSLFVILALVPWNQIGAGGSPFVTV
FSLLGIPAAAGIMNFVVLTAALSSLNSGLYSTSRMLYSLAERGDAPKFFGKLSKRGVPVRAILLSAVVLL
IGVVLNYLLPEKAFTFLLSISGFGALFVWLMILVSQLKFRRRLPREGAAALKFKMPGFPYTSYLTLAFLA
AVLVLMAFDPDTRIALIVGPVWLALLVVGYFLVRRRRA
>gnl|CDD|440731 COG1114, BrnQ, Branched-chain amino acid permease [Amino acid transport and metabolism]
MKKLSTKDILVIGFMLFALFFGAGNLIFPPFLGQLAGSNWWPAILGFLITGVGLPLLGIIAVAKSGGGLE
DLASRVGPWFGLIFTVLIYLAIGPLFAIPRTAAVSFEMGIAPFLPESQLSLLIFSIIFFALVLLLSLNPS
KLVDRIGKILTPALLILLAILIIKAIISPLGPIGAPTGAYQSNPFSKGFLEGYQTMDALAALVFGIVIIN
AIRSKGVTDKKEIAKYTIKAGLIAGIGLALIYGGLAYLGATSSGLFGGAENGAEILSAIVQHLFGSFGSI
LLAIIVTLACLTTAVGLITACAEYFSELFPKLSYKTWVIIFTLFSFLVANLGLDQIIAISVPVLMFIYPI
AIVLILLSLLNKFFKNSKLVYRGAVIVTLIFSLLDGLKALGLSLGALTSFLNYLPLYSLGLGWLLPALIG
FVIGLLIDKLKKK
>gnl|CDD|440732 COG1115, AlsT, Na+/alanine symporter [Amino acid transport and metabolism]
MDALNEILNAINDFLWGPPLIILLLGTGLYFTIRLGFVQFRKFGHAFRLLFGKKKDKGGEGGISSFQALA
TALAATVGTGNIAGVATAIALGGPGAVFWMWVTALLGMATKFAESTLAQKYREKDEDGEYRGGPMYYIEK
GLGKKWLAVLFAIFLIIAAGGIGNMVQANSIASALENAFGIPPWITGIVLAVLVGLVIFGGIKRIAKVAE
KLVPFMAVLYILGALIILILNIDQIPAAFALIFKSAFGPQAAAGGFAGATVMAAIRQGVARGLFSNEAGL
GSAPIAAAAAKTDHPVRQGLVQMLGVFIDTIVVCTMTALVILLTGVWNPGGGLTGAALTQAAFSSVLGGW
GGYFVAIALFLFAFSTIIGWYYYGEKNLEYLFGSKKAILVYRILFLLMVFVGAVASLDLVWALADIFNGL
MAIPNLIALLLLSGVVVKELKDYFAQLKAG
>gnl|CDD|440733 COG1116, TauB, ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism]
MSAAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV
DGKPVTGPGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLS
GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVV
VLSARPGRIVEEIDVDLPRPRDRELRTSPEFAALRAEILDLLREEAERAA
>gnl|CDD|440734 COG1117, PstB, ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]
MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVE
GEILLDGEDIYDPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAAL
WDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVT
HNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYITGRFG
>gnl|CDD|440735 COG1118, CysA, ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism]
MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNL
PPRERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQ
RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQG
RIEQVGTPDEVYDRPATPFVARFLGCVNVLRGRVIGGQLEADGLTLPVAEPLPDGPAVAGVRPHDIEVSR
EPEGENTFPATVARVSELGPEVRVELKLEDGEGQPLEAEVTKEAWAELGLAPGDPVYLRPRPARVFLP
>gnl|CDD|440736 COG1119, ModF, ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism]
DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRGG
EDVWELRKRIGLVSPALQLRFPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPF
GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGI
THVLLLKDGRVVAAGPKEEVLTSENLSEAFGLPVEVERRD
>gnl|CDD|440737 COG1120, FepC, ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism]
MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR
RELARRIAYVPQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSG
GERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVL
LKDGRIVAQGPPEEVLTPELLEEVYGVEARVIEDPVTGRPLVLP
>gnl|CDD|440738 COG1121, ZnuC, ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]
MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP
RRARRRIGYVPQRAEVDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGEL
SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVL
LLNRGLVAHGPPEEVLTPENLSRAYGGPVALLAHG
>gnl|CDD|440739 COG1122, EcfA2, Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only]
IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNL
RELRRKVGLVFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQK
QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDG
RIVADGTPREVFSDYELLEE
>gnl|CDD|440740 COG1123, GsiA, ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones]
MTPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDG
RDLLELSEALRGRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYP
HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIA
DRVVVMDDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVRA
VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQD
PYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALA
LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE
EVFANPQHPYTRALLAAVPSLDPA
>gnl|CDD|440741 COG1124, DppF, ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism]
MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT
RRRRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLS
GGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVA
VMQNGRIVEELTVADLLAGPKHPYTRELLAASLAFERA
>gnl|CDD|440742 COG1125, OpuBA, ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism]
MIEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLD
PVELRRRIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEYRDRYPHELSGG
QQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM
REGRIVQYDTPEEILANPANDFVADFVGADRGLRRLSLLRVEDLMLPEPPTVSPDASLREALSLMLERGV
DWLLVVDEDGRPLGWLTLEDLLRALA
>gnl|CDD|440743 COG1126, GlnQ, ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism]
MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKK
DINKLRRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGG
QQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMD
GGRIVEEGPPEEFFENPQHERTRAFLSKV
>gnl|CDD|440744 COG1127, MlaF, ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis]
MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDIT
GLSEKELYELRRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPS
ELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIAD
RVAVLADGKIIAEGTPEELLASDDPWVRQFL
>gnl|CDD|440745 COG1129, MglA, ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]
AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRF
RSPRDAQAAGIAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGD
LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRV
TVLRDGRLVGTGPVAELTEDELVRLMVGRELEDLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEI
LGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIREN
ITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDE
PTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEEAIMAAA
TGGAAAA
>gnl|CDD|440746 COG1131, CcmA, ABC-type multidrug transport system, ATPase component [Defense mechanisms]
IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE
VRRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRL
GLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIV
ADGTPDELKARLLEDVFLELTGEEAR
>gnl|CDD|440747 COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]
MSKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGL
ALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLP
QLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGI
RVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDL
VAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYP
GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVP
QDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARA
LLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEE
LLARGGLYARLYRLQFGEE
>gnl|CDD|440748 COG1133, SbmA, Peptide antibiotic transporter SbmA/BacA, ABC-type permease family [Defense mechanisms]
MFKSFFPRPKLFFLSAAIWSLLAVLFWYAGGEGLGASLGLPPAAAGAPPPIGAARFWTPDFLWFYAYYAL
CVGLFAGFWFFYSPHRWQRWSILGSALIIFVTYFSVQVSVAINAWYGPFYDLIQKALSKPGSVTIADFYG
QMLTFLGIALIAVTVGVLNAFFVSHYVFRWRTAMNDYYMAHWPRLRHIEGASQRVQEDTMRFASIVEGLG
VSFIDAVMTLIAFLPVLWALSQHVTELPIIGEVPYSLVWAAIFWSLFGTVLLALVGIKLPGLEFRNQRVE
AAYRKELVYGEDDAERAQPPTVRELFSNVRRNYFRLYFHYLYFNVARYLYLQADNIFPLFILVPSIVAGK
ITLGLMQQISNAFGQVRSSFQYLVNSWTTIVELLSIYKRLRAFEAAIDDEPLPEIDQE
>gnl|CDD|440749 COG1134, TagH, ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism]
MSSMIEVENVSKSYRLYHEPSRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLK
LIAGILEPTSGRVEVNGRVSALLELGAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFI
DQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVR
RLCDRAIWLEKGRLVMDGDPEEVIAAYEALLAGRE
>gnl|CDD|440750 COG1135, AbcC, ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]
MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLT
ALSERELRAARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQ
LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDR
VAVLENGRIVEQGPVLDVFANPQSELTRRFLPTVLNDELPEELLARLREAAGGGRLVRLTFVGESADEPL
LSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDAAIDAALAYLREQGVVVEVLG
>gnl|CDD|440751 COG1136, LolD, ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]
MSPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQ
DISSLSERELARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDH
RPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR
ADRVIRLRDGRIVSDER
>gnl|CDD|440752 COG1137, LptB, ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis]
MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL
PMHKRARLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGG
ERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIIS
EGKVLAEGTPEEILNNPLVRKVYLGEDFRL
>gnl|CDD|440753 COG1138, CcmF, Cytochrome c biogenesis protein CcmF [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
IPELGHFALILALALALVQAVLPLIGARRGDARLMASARPAALAQFLLVALAFAALVYAFVTSDFSVAYV
AQNSNSALPLLYKISAVWGGHEGSLLLWVLILALWGAAVALFSRRLPPELRARVLAVLGLISVGFLLFIL
FTSNPFERLLPAPADGRGLNPLLQDPGLAIHPPLLYLGYVGFSVPFAFAIAALITGRLDAAWARWVRPWT
LAAWLFLTLGIALGSWWAYYELGWGGWWFWDPVENASLMPWLTGTALLHSLAVTEKRGALKSWTVLLAIL
TFSLSLLGTFLVRSGVLTSVHAFASDPERGVFILAFLAVVIGGSLLLFALRAPRLKSGGRFSLVSRESAL
LLNNLLLVVAAAVVLLGTLYPLILEALGGGKISVGPPYFNAVFVPLMLPLLLLMGIGPLLRWKRADLARL
LRRLLVPAVAALVAALLLPALLGGRSLLALLGLGLAAWVIAGTLLELVRRLRLRGEPALRRLRRLPRSRY
GMYLAHLGVAVTVIGIAGSSAYSVERDVRLAPGESVTLGGYTFTFEGVREVEGPNYTAVRATFTVSRDGK
PVATLHPEKRFYPVRGMPTTEAAIDTGLLRDLYVVLGEPLEDGAWAVRVYYKPLVRWIWLGGLLMALGGL
LALSDRRYRVGAPARAAAAA
>gnl|CDD|440754 COG1139, LutB, L-lactate utilization protein LutB, contains a ferredoxin-type domain [Energy production and conversion]
MSKASSEDFKERAREALADEQLRKALDRATDTLRAKRAKAVAELPDWEALREAARAIKDHALANLDEYLE
QFEANATANGGHVHWARDAEEANRIVLDIAREKGAKKVVKSKSMVTEEIGLNEALEAAGIEVVETDLGEY
IVQLAGEPPSHIVMPAIHKNREQIAELFHEKLGTEPLTDDPEELTRAAREHLREKFLEADVGITGANFAV
AETGTIVLVTNEGNARLCTTLPKVHIAVMGIEKLVPTLEDLEVFLRLLPRSATGQRITTYTSLITGPRRP
GEGDGPEEFHLVLLDNGRSAMLADPEFREALRCIRCGACLNVCPVYRRVGGHAYGSVYPGPIGAVLTPLL
HGLEKAADLPYASTLCGACTEVCPVKIPIPELLLELRERIVEEGLTPPAEKLAMKAWAWVMSNPKLYRLA
LRLARRALKLLPRGGGIRRLPGPLGGWTKGRDLPAPAKESFRDWW
>gnl|CDD|440755 COG1140, NarY, Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and metabolism]
MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELDR
NGKLRLRAGGRLKKLANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPMKIEWGP
NWDDDLGGSFEYASKDPNLEGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLV
DQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEE
AASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDDWIEAAQRSPVYKLAKEWKVALPLHPEYRTLPM
VWYVPPLSPVVDAVEAGGHDGDADGLFPAIDSLRIPVEYLANLFTAGDEEPVEAALRRLAAMRAYMRAKN
VGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGFDFGGGCP
>gnl|CDD|440756 COG1141, Fer, Ferredoxin [Energy production and conversion]
MKVTVDRDTCIGCGLCVALAPEVFELDDDGKAVVLDEEVPEELEEDVREAADACPVGAITVEE
>gnl|CDD|440757 COG1142, HycB, Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]
MNKFIIADPEKCIGCRTCEAACAVAHEGEEGEPFLPRIRVVRKAGVSAPVQCRHCEDAPCAEVCPVGAIT
RDDGAVVVDEEKCIGCGLCVLACPFGAITMVGEKSRAVAVKCDLCGGREGGPACVEACPTGALRLVDV
>gnl|CDD|440758 COG1143, NuoI, Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]. Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
EDKCIGCGLCVRVCPVDAITIEDGEPGKVYVIDPDKCIGCGLCVEVCPTGAISMTPFELAVEDREE
>gnl|CDD|440759 COG1144, PorD, Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]. Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
PQGGAITEPGGTAAYKTGGWRVERPVVDEDKCIGCGLCWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAE
VCPVKAIEMVPEEK
>gnl|CDD|440760 COG1145, NapF, Ferredoxin [Energy production and conversion]
AALLLDLKEALSPKLKVLYAVVTGILGKIILNVIAGALLKAVALGGLLPIIGILAKEAFDALKDVLGILG
AIVIGIGAGEIVRVGIAAADLNLKAVALVLLLALAVAGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALA
EAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKDGKPQIVV
DPDKCIGCGACVKVCPVGAISLEPKEIE
>gnl|CDD|440761 COG1146, PreA, NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism]
MMPVIDTDKCIGCGACVEVCPVDVLELDEEGKKALVINPEECIGCGACELVCPVGAITVEDDEPEEQ
>gnl|CDD|440762 COG1148, HdrA, Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]
MARIGVFVCHGINIGGVVDVPAVAEYAKTLPGVVYAEDNLYLCSQDGQELIKDDIKEHGLNRVVVAACSP
RTHEPLFRETLREAGLNPYLFEMANIREQCSWVHMDEPEAATEKAKDLVRMAVAKAKLLEPLEPIKVPVN
KRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHKTFPGLDCPQCILEPLIAEVEANPNIT
VYTGAEVEEVSGYVGNFTVTIKKGPREEIEIEVGAIVLATGFKPYDPTKLGEYGYGKYPNVITNLELERL
LAAGKILRPSDGKEPKSVAFIQCVGSRDEENGLPYCSRVCCMYALKQALYLKEKNPDADVYIFYRDIRTY
GKYEEFYRRAREDGVRFIRGRVAEIEEDEGGKLVVTVEDTLLGEPVEIEADLVVLATGMVPSEDNEELAK
LLKLPLDQDGFFLEAHPKLRPVETATDGIFLAGAAHGPKDIPESIAQATAAAARAIQLLSKGELGVEPSV
AEVDPEKCTGCGRCVEVCPYGAISIDEKGVAEVNPALCKGCGTCAAACPSGAISLKGFTDDQILAQIDAL
LVP
>gnl|CDD|440763 COG1149, COG1149, MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only]
VKRKIPVIDEEKCIGCGLCVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGAITLEEREAGKI
>gnl|CDD|440764 COG1150, HdrC, Heterodisulfide reductase, subunit C [Energy production and conversion]
NLKKCYQCGTCTASCPVARAMDYNPRKIIRLAQLGLKEEVLKSDSIWLCVSCYTCTERCPRGIDIADVMD
ALRNLAIRE
>gnl|CDD|440765 COG1151, Hcp, Hydroxylamine reductase (hybrid-cluster protein) [Energy production and conversion]
IDPAVQEMLEKAKEDGIETVFDRFEAQQPQCGFGLQGMCCRQCEQGPCRITPKTPRGVCGKTADTIVARN
LLRYVAKGAAAHADHAREVALTLKAAAEGADYEIKDEEKLRFVAEALGITTEGKDLIEIALELADALLED
FGKAGGEPATWLEAKAPEERIESWRELGIEPRGIDREIVEALARTHTGVDLDPVNLLLLALRTGLADWGG
MALLDEANDILFGTPEPTEVEVNLGVLKEDGVNILVHGHDPKLSEAIVEAARDLEELAKQTGAKGINVYG
ICCTGGEMLPRHGYPEKKYVHLAGNYGSAEFAIFTGAIDAMVVDTNCIMPPLASVAECYYTDRITTTGVV
GIPGAEHIEFDEEGALEDASEIIEKAIENFKPREDEKVYIPQEKGEIVVGFSHEAVLAALGSADPLIDAI
KSGKIRGFVLVVGCDGRKPGRDYNYYTLFKELIPNDVLVLTTGCAKYRLNKLGLGDIEAAELAGEGLKEV
CEALGIPPVLDMGQCNDNYRALVLALALAEALGVDINDLPLAGSAPEWYEQKAVAIGLYLLALGVKIHLG
PTPPAFGSPNVLKVLTEDFEDITGGTFTVEEDPKKAADKIIAHIEEKRKALGI
>gnl|CDD|440766 COG1152, CdhA, CO dehydrogenase/acetyl-CoA synthase alpha subunit [Energy production and conversion]
AELFDDCVMCGLCTLACPEEIPGFIDDPIIRKVGVPLVDGTIPGVAALVGCANDPEEAAKIAKELQEKGL
IVFLSGTLIEQLPEAFDGRLVPLGSCTSVVHAVGFAIRAALIFGGIPPGNYEEILDYILNRVGAFVVALG
EYSQRAAAAAAGAIRLGFPVITDQDVPEPIPEHLLSRLEDYEEGVQTALELRGIKITRTEIDIPVAYGPA
FEGER
>gnl|CDD|440767 COG1153, FwdD, Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]
MKVLLITGRTIFQGVAIEGGKFSDEYFDACAVCELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDL
HPGLVFIPMGPWANAVVPPETHSTGMPDFKGVPVEVEPTDEEVLSAEELMQKAGGLG
>gnl|CDD|440768 COG1154, Dxs, Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]. Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVW
DVGHQAYPHKILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKV
VAVIGDGALTGGMAFEALNNAGHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLL
KKLPGIGPPLYELARRAKEGLKGLVVPGTLFEELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVT
KKGKGYAPAEKDPDKFHGVGPFDPETGEPKKSKSSAPSYTDVFGDTLVELAEKDPRIVAITAAMPEGTGL
DKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQVIHDVALQNLPVTFAIDRAG
LVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRGNGPGVELPAELEPL
PIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVTVE
EGVLAGGFGSAVLEFLADAGLDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG
>gnl|CDD|440769 COG1155, NtpA, Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]. Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 is part of the Pathway/BioSystem: A/V-type ATP synthase
MMTKGKIVKINGPLVTAEGMGGAKMYEVVYVGEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGE
PLSVELGPGLLGNIFDGIQRPLDKIAEKSGDFIPRGVDVPALDREKKWDFTPTVKVGDKVSAGDILGTVQ
ETPLIEHKIMVPPGVSGTVKEIAPEGEYTVEDTIAVLEDEDGEEHELTMYQKWPVRRPRPYKEKLPPSEP
LITGQRVIDTFFPIAKGGTAAIPGPFGTGKTVTQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPELID
PKTGRPLMERTVLIANTSNMPVAAREASIYTGITIAEYYRDMGYDVALMADSTSRWAEALREISGRLEEM
PGEEGYPAYLASRLAEFYERAGRVKTLGGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDASLA
YARHYPAINWLTSYSLYLDDLAEWYDENVDPDWSELRNEAMDLLQEEAELQEIVRLVGEDALPDEDRLTL
EVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLSEIKELPLREKIARMKYS
PENELLEKFDELEKEIDEEIEEL
>gnl|CDD|440770 COG1156, NtpB, Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]. Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 is part of the Pathway/BioSystem: A/V-type ATP synthase
MMKKEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTK
VRFLGEPLELPVSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLN
TLVRGQKLPIFSGSGLPHNELAAQIARQAKVRGEEEKFAVVFAAMGITHDEANFFREEFEETGALDRVVM
FLNLADDPAIERIITPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYS
DLASLYERAGRIKGRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLS
RLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEEALSETDKKYLKFADAFERRFVNQGFDE
NRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPKKRAKE
>gnl|CDD|440771 COG1157, FliI, Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport]
LDRLARLLARLEELPPVRVSGRVTRVVGLLIEAVGPDASIGELCEIETADGRPVLAEVVGFRGDRVLLMP
LGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEP
LDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEDDLGEEG
LARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYP
PSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLA
SISRVMPDIVSPEHRALARRLRRLLARYEENEDLIRIGAYQPGSDPELDEAIALIPAIEAFLRQGMDERV
SFEESLAQLAELL
>gnl|CDD|440772 COG1158, Rho, Transcription termination factor Rho [Transcription]
AEDDGLIPVEGVLEILPDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDAVTGQVRPPKEGEKYFALL
RVESVNGEDPEEARKRPDFDNLTPLYPDERLRLETTPDDLSTRVIDLVAPIGKGQRGLIVAPPKAGKTTL
LQDIANAITANHPEVHLIVLLIDERPEEVTDMQRSVKGEVIASTFDEPAERHVQVAELVIERAKRLVELG
KDVVILLDSITRLARAYNLVVPASGRTLSGGVDANALYKPKRFFGAARNIEEGGSLTIIATALVDTGSRM
DEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINKSGTRREELLLSPEELEKVWILRRALSGMDPVEAME
FLLDRLKKTKSNAEFLESMNKTT
>gnl|CDD|440773 COG1159, Era, GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]
FRSGFVAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIHKPKRKLGR
RMNKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELL
DFAEIVPISALKGDNVDELLDEIAKLLPEGPPYYPEDQITDRPERFLAAEIIREKILRLLRDELPYSVAV
EIEEFEEREGLLRIRATIYVERDSQKGIIIGKGGSMLKKIGTEARKDIEKLLGKKVFLELWVKVKKNWRD
DERALRELGY
>gnl|CDD|440774 COG1160, Der, Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]
MSPVVAIVGRPNVGKSTLFNRLTGRRDAIVDDTPGVTRDRIYGEAEWGGREFTLIDTGGIEPDDDDGLEA
EIREQAELAIEEADVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGPKREADAAEFYSLGLGE
PIPISAEHGRGVGDLLDAVLELLPEEEEEEEEDDPIKIAIVGRPNVGKSSLINALLGEERVIVSDIAGTT
RDSIDTPFERDGKKYTLIDTAGIRRKGKVDEGIEKYSVLRTLRAIERADVVLLVIDATEGITEQDLKIAG
LALEAGKALVIVVNKWDLVEKDRKTREELEKEIRRRLPFLDYAPIVFISALTGQGVDKLLEAVDEVYESA
NKRISTSKLNRVLEEAVERHPPPAVKGRRLKIYYATQVGTRPPTFVLFVNDPELLPFSYKRYLENQLREA
FGFEGTPIRIEFRKRKNP
>gnl|CDD|440775 COG1161, RbgA, Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis]
MQIQWFPGHMAKARRQIKEILKLVDLVIEVVDARIPLSSRNPMLDELVGNKPRLLVLNKADLADPSVTKQ
WLKYFEKQGVDALAISAKKGKGIKELIEAIRELAPEKGIKRRPIRVMIVGIPNVGKSTLINRLAGKKVAK
TGNKPGVTKGQQWIKLDDGLELLDTPGILWPKFEDPEVGYKLAATGAIKDEVLDLEEVALFLLGYLARRY
PELLKERYKLDELPRTKLELLEAIGRKRGCLLSGGEVDLEKAAEILLTDFRSGKLGRITLETPEEVELR
>gnl|CDD|440776 COG1162, RsgA, Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]
LMPGRVIKVHGGRYYVETEDGERYRCRLRGKLRKKGISPVVGDWVEIEPDDDGEGVIEEILPRKNLLVRP
AVGRDKEQVIAANIDQVLIVVALAEPDFNLRLLDRYLVAAEAAGIEPVIVLNKADLADDEELEELLAIYE
ALGYPVLAVSAKTGEGLDELRELLKGKTSVLVGQSGVGKSTLINALLPDADLATGEISEKLGRGRHTTTH
AELYPLPGGGWLIDTPGFREFGLWHIEPEELAHYFPEFRELAGQCRFRDCTHLHEPGCAVKAAVEAGEIS
PERYESYLKLLEELEERKRR
>gnl|CDD|440777 COG1163, Rbg1, Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]
AMTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVG
FPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRN
ADLILIVLDVFELEQYDVLKEELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLDLDEEDIKKILREYG
IVNADVLIREDVTLDDLIDALMGNRVYKPAIVVVNKIDLADEEYVEELKSKLPDGVPVIFISAEKGIGLE
ELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGSTVGDVCEKIHRDFVERFRYARVWGKSAKHPGQRV
GLDHVLEDGDIVEIIIKK
>gnl|CDD|440778 COG1164, PepF, Oligoendopeptidase F [Amino acid transport and metabolism]
MTALPTRSEVPEEYTWDLSDLYPSDEEWEADLEELEELIEEFEALYKGKLALSAETLLEALELYEELSEL
LGRLYSYASLRYDEDTTDPEAQALLSRAQELLAELSAALSFFEPELLALDEEKLEALLEEEPELAEYRFY
LEELRRQKPHTLSEEEEKLLAELSETGGAAWNILYDLTNADLRFPTVEDEDGEEVELTHGQYLNLLESPD
REVRKAAFEALYKAYKKYENTFAATLNTLVKDRLFLARLRGYDSALEAALLANRIPREVYDALIEAVREN
LPLLHRYYKLKAKLLGLDKLHMYDLYAPLVKDVDKKITYEEAKELVLEALAPLGPEYAEIAKRAFEERWI
DAYPRPGKRSGAFCSGTPYGVHPYILLNYTGTLRDVFTLAHELGHAVHSYLARDNQPYLNSDYPIFLAET
ASTFNEMLLFDYLLKNATDPEEKLALLNQKLEDFRATVFRQTMFAEFEREVHEAREEGGELTAEELNELY
LELQKEYYGDAVEIDDGYPYEWARIPHFYHSPFYVYQYAFGLLAALALYARILEEGEGFVERYLELLKAG
GSDYPEELLKKAGVDLTDPEFWQAALDVIEELIDELEALL
>gnl|CDD|440779 COG1165, MenD, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport and metabolism]. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
SDKNSNTLWARVLVEELVRLGVRHVVISPGSRSTPLTLAFARHPDLRLHSHVDERSAAFFALGLAKASGR
PVALVCTSGTAAANYYPAVIEAFYSGVPLIVLTADRPPELRDCGANQTIDQVGLFGNHVRWSADLPLPEA
DPDALRYLRRTINRALAAALGPPPGPVHINVPFREPLYPDPDEEDPLAAGGPWIRVTPPEPAPSPEALAQ
LADELERAKRGLIVAGPLPPPEELAEALAALAEALGWPVLADPLSNLRHPNVISTYDLLLRNPEFAELLQ
PDLVIRFGGPPVSKRLKQFLRRHPPAEHWVVDPSGEWRDPFHSLTRVIEADPEAFLEALAERLPPADSAW
LARWLAAEQKARAAIDEYLAEDPLSEGAVARRLLEALPEGSTLFVGNSMPVRDLDLFARPLPKGVRVYAN
RGASGIDGTVSTALGAALASGKPTVLLTGDLSFLHDLNGLLLLYELPPNLTIVVVNNDGGGIFSMLPGAK
FEPEFERFFGTPHGLDFEHLAAMYGLDYARVSSWEELREALAEFLPSDGPRVLEVRTDREENAELLKALF
AAVAAAL
>gnl|CDD|440780 COG1166, SpeA, Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]
PMMDWTIEDARELYNIDRWGEGYFDINEKGHVTVRPDGDPGPSIDLYELVEELRERGLSLPVLLRFPDIL
RDRVERLNEAFAKAIAEYGYQGRYRGVYPIKVNQQRHVVEEIVRAGKPYNFGLEAGSKPELMAVLALLDD
PGSLIICNGYKDREYIRLALLGRKLGHKVIIVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQ
NSGGERSKFGLSASEILEVVERLKEAGMLDCLQLLHFHLGSQIPNIRDIKRAVREAARFYAELRKLGAPI
EYLDVGGGLGVDYDGSRSNSDSSMNYSLQEYANDVVYAIKEVCDEAGVPHPTIISESGRALTAHHSVLIF
NVLDVERAPPEPPPPAPPEDAHELLRNLWETYESLTPRNLQECYHDALQYKEEARSLFNLGYLSLEERAL
AEQLYWAICRKIRELLDPLEYHPEELDELNEKLADKYFCNFSLFQSLPDSWAIDQLFPIMPIHRLDEEPT
RRAVLADITCDSDGKIDQFIDGQGVKSTLPLHPLKPGEPYYLGVFLVGAYQEILGDLHNLFGDTNAVHVR
LDEDGGYEIEHVVEGDTVAEVLSYVQYDPEDLLERYRRQAEQAVRAGRLTPEERQRLLEEYEAGLRGYTY
LED
>gnl|CDD|440781 COG1167, ARO8, DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]. DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis
MLIRLDRDSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRP
GSGTFVAARLPAPAPAPRAAAAVAAPALRRLLEAAPGVIDLGSGAPDPDLFPLAALRRALRRALRRLPPA
LLGYGDPQGLPELREAIARYLARRGVPASPDQILITSGAQQALDLALRALLRPGDTVAVESPTYPGALAA
LRAAGLRLVPVPVDEDGLDLDALEAALRRHRPRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIE
DDYDSELRYDGRPPPPLAALDAPGRVIYIGSFSKTLAPGLRLGYLVAPGRLIERLARLKRATDLGTSPLT
QLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLPDGLRVTGPPGGLHLWLELPEGVDAEALAAA
ALARGILVAPGSAFSADGPPRNGLRLGFGAPSEEELEEALRRLAELLRELA
>gnl|CDD|440782 COG1168, MalY, Bifunctional PLP-dependent enzyme with beta-cystathionase and maltose regulon repressor activities [Amino acid transport and metabolism, General function prediction only]
MKYDFDTIIDRRGTGSVKWDGLEDRFGGEDVLPMWVADMDFATPPAVIEALKERVEHGVFGYTAPPDEYY
EAIIDWLKRRHGWEIDPEWIVFTPGVVPGLALAIRAFTEPGDGVLIQTPVYPPFFKAIENNGRELVENPL
ILEDGRYRIDFDDLEAKLDPGVKLLLLCNPHNPTGRVWTREELERLAELCERHDVLVISDEIHADLVLPG
HKHTPFASLSEEAADRTITLTSPSKTFNLAGLKASYAIIPNPALRARFARALEGLGLPSPNVLGLVATEA
AYREGEEWLDELLAYLRGNRDLLAEFLAEHLPGVKVTPPEATYLAWLDCRALGLDDEELAEFLLEKAGVA
LSDGATFGEGGEGFVRLNFACPRAVLEEALERLAKAL
>gnl|CDD|440783 COG1169, MenF, Isochorismate synthase EntC [Coenzyme transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]. Isochorismate synthase EntC is part of the Pathway/BioSystem: Menaquinone biosynthesis
PRFYWASPDRGEGLAGLGEAARFEAPGPDRFAALAAAWQALLADAALAGTGPRAFGGFAFDPDSPAPAAR
LVLPRLLLRRSRRGVPDPAEWREAVAQALEAIRAGELDKVVLARALDLTLDEPIDPRALLARLRRRNPDC
YTFAVELGAGDGFVGASPERLVRRRGGQLTTEALAGTAPRGADPEEDAALAAALLASEKDRREHALVVDS
IREALAPLCSSLDVPEEPELLRLRNVQHLATPITGTLDPGVSALDLAAALHPTPAVGGTPREAALALIRE
LEPFDRGWYAGPVGWVDADGDGEFAVAIRSALIDGNRARLFAGAGIVAGSDPEAEWAETEAKLRTMLRAL
GLE
>gnl|CDD|440784 COG1171, IlvA, Threonine deaminase [Amino acid transport and metabolism]. Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
MTALMPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEE
RARGVVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAE
EEGATFVHPFDDPDVIAGQGTIALEILEQLPDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGA
AAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEP
AGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAEILERGLVGEG
>gnl|CDD|440785 COG1172, AraH, Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component [Carbohydrate transport and metabolism]
MSATTTTARSLLRRLLPELGLLLALVLLLVVFSILSPGFLSPGNLSNILRQAAILGILALGMTLVIITGG
IDLSVGSVVALSGVVAALLLVALGLPILLAILLALLVGALLGLLNGLLVAKLRIPPFIVTLGTMFIARGL
ALLLTGGRPISGLPDAFRALGQGSLLGIPVPVLIALVVALVAWFLLRRTRFGRYIYAVGGNEEAARLSGI
NVRRVKILAYVLSGLLAGLAGILLAARLGSAQPNAGSGYELDAIAAVVIGGTSLTGGRGSVLGTLLGALI
LGVLNNGLNLLGVSSYWQQIVKGAIILLAVLLDRLRRRRRAR
>gnl|CDD|440786 COG1173, DppC, ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid transport and metabolism, Inorganic ion transport and metabolism]
PRSRWRRAWRRLRRNPLAVIGLVILLLLVLLALFAPLLAPYDPTAQDLAARLQPPSAAHWLGTDQLGRDV
LSRLLYGARISLLVGLLAVLIALVIGVLLGLLAGYFGGWVDAVLMRLVDVLLAFPSLLLAIALVAVLGPG
LLNVILALGLTGWPGYARLVRAQVLSLREREYVEAARALGASPLRIIFRHILPNVLPPLIVQATLGIASA
ILAEAGLSFLGLGVQPPTPSWGTMLSEGRNYLLTAPWLALFPGLAIVLTVLAFNLLGDGLRDALD
>gnl|CDD|440787 COG1174, OpuBB, ABC-type proline/glycine betaine transport system, permease component [Amino acid transport and metabolism]
MNLSLIEWLADNRDGILALLLEHLLLVLLALLIALLIAVPLGILITRRRRLAGLVLGVANILQTIPSLAL
LALLIPLLGIGPAPAIIALVLYALLPILRNTYTGLRSVDPAVVEAARGMGMTPWQRLWRVELPLALPVIL
AGIRTAAVQNIGTATLAALIGAGGLGDLIFDGLQLNNTALILAGAILVALLALLVDLLLALLERLLTPRG
LR
>gnl|CDD|440788 COG1175, UgpA, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism]
MTTTTSAAARRRRRRRRLAAYLFLLPALLLLLVFVLYPLLYTLYLSFTDWNLLGPPPEFVGLDNYARLFT
DPRFWNALGNTLLFTVVSVPLQLVLGLLLALLLNRKLRGRGFFRTLFFLPWVISPVVVALIWKWLFNPDY
GLLNALLGALGLEPINWLGDPSLALPAVIIVTVWKGTGFNMLIFLAGLQSIPRELYEAARIDGASPWQRF
RRITLPLLRPTILFVLVLSTIGALQVFDLVYVLTGGGPGNSTTTLVLYIYQTAFQQFDFGYASAIAVVLF
LIILVLTLLQLRLLRRRE
>gnl|CDD|440789 COG1176, PotB, ABC-type spermidine/putrescine transport system, permease component I [Amino acid transport and metabolism]
MSAALRRRLRPLLLLLPALLWLLLFFVLPLLLLLVYSFTTRDPYGGVVPGFTLENYARLFTDPLYLKVLL
RTLWIALLTTLICLLLGYPIAYFLARAPPRWRNLLLLLVILPFWTSFLVRTYAWIVLLGRNGLLNSLLLA
LGLIDEPLRLLYTEFAVVIGLVYVYLPFMVLPLYAALEKIDPSLLEAARDLGASPWQTFRRVILPLSLPG
IIAGSLLVFIPALGAFVTPALLGGGKVLMIGNLIYQQFLSALNWPLAAALAVVLLLIVLLVLLLYLRLLR
RRRLLGG
>gnl|CDD|440790 COG1177, PotC, ABC-type spermidine/putrescine transport system, permease component II [Amino acid transport and metabolism]
SSRLGRLLLRLFLALVLLFLYLPILVLVLYSFNDSWFLTFPPEGFTLRWYAELFSDPRLLDALLNSLLIA
LLSTLLATVLGTPAALALARYRFRGRRLLLALLLLPLVVPGIVLGVALLLLFSALGLSGGLWGLILAHVV
FTLPFVVLVVLARLQGFDPSLEEAARDLGASPWQTFRRVTLPLIAPGILAGALLAFTLSFDEFVITLFLA
GPGVTTLPVYIYSMIRRGISPEINALSTLLILLSLLLLLLAERLRRRGERRR
>gnl|CDD|440791 COG1178, FbpB, ABC-type Fe3+ transport system, permease component [Inorganic ion transport and metabolism]
MSTRPRRRPRLLLLLLALLLALLVLLPLLALLLRAFTDGLANFWALLSDPYLWRALGNTLLLALLVTLLS
LLLGVPLAWLLARTDFPGRRLLRWLLLLPLALPPYVVALAWIALFGPNGLLNTLLRALFGLEPPDIYGLG
GIILVLVLFNYPYVYLLLRAALRSIDASLEEAARSLGASPWRAFRRVTLPLLRPAIAAGALLVFLLCLAD
FGTPLVLGGGYTTLTTAIYQAWLGDFDLGAAAALALVLLLLVLLLLLLERRLRRRRRYATVGGRARRPRR
VKLGRWRWLALALCLLLVLLGLLLPLLALLLWSLTKALDDNLTLDNYRFVLLDPSLLRALLNSLLLALLA
ALLAVLLALLLAYLVRRRRGRLARLLDRLAMLPYAVPGIVLGLGLLLLFNRPLPLLLYGTLAILVLAYVV
RFLPFALRSLEAALAQIDPSLEEAARSLGASPLRTLRRVTLPLLRPGLLAAALLVFVTSMKELSATLLLR
PPGFETLAVLIYQLASSGRYGEAAALALLLVLVSLLPVLLLERLLGRR
>gnl|CDD|440792 COG1179, TcdA, tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]. tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification
MDMERRFSRTERLYGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHA
LDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADELLSEDYDYVIDAIDSVSAKAALIAWCRRRG
IPIISSMGAGGKLDPTKIRVADLSKTSNCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRKPQADGTVCDTG
GTGLKCAGPGSISFVPAVFGLIAAGEVIRDLLGKAAR
>gnl|CDD|440793 COG1180, PflA, Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones]
EEVRGRIYGISPFSTVDGPGSIRLSVFTQGCNLRCPYCHNPEISQGRPDAAGRELSPEELVEEALKDRGF
LDSCGGVTFSGGEPTLQPEFLLDLAKLAKELGLHTALDTNGYIPEEALEELLPYLDAVNIDLKAFDDEFY
RKLTGVSLEPVLENLELLAESGVHVEIRTLVIPGLNDSEEELEAIARFIAELGDVIPVHLLPFHPLYKLE
DVPPPSPETLERAREIAREYGLKYVYIGNVPG
>gnl|CDD|440794 COG1181, DdlA, D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]. D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
MRVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIGIDVEDLPAALKELKPDVVFPALHGRGGEDGT
IQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPA
REGSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNGGPRALPPIEIVPENGFYDYE
AKYTDGGTEYICPARLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMTPTSLL
PKAAAAAGISYEELIERIIELAL
>gnl|CDD|440795 COG1182, AzoR, FMN-dependent NADH-azoreductase [Energy production and conversion]
MMKLLHIDSSPRGEGSVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAAFFTPAEGRTPEQ
QAALALSDELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITA
RGGVYSGGPAAGMDFQTPYLRTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELAAAL
>gnl|CDD|440796 COG1183, PssA, Phosphatidylserine synthase [Lipid transport and metabolism]
MSRPRRRAIYLLPNLFTLLNLFCGFLAIVAAIEGDFELAALLILLAAVFDGLDGRVARLLNVQSEFGAEL
DSLADMVSFGVAPALLLYQWGLLPLGGLGWLAAFLFAACSALRLARFNVKTDDDKNYFVGLPSPAAALLV
ASLVLLGLELGLPGLPNPWVLLALTLLLALLMVSPIPYPSFKRLSLKRRVPLPLLLLVVLAVALLVLYPW
LALFLLFLLYLLSGPVLALYRLRRLKR
>gnl|CDD|440797 COG1184, GCD2, Translation initiation factor 2B subunit, eIF-2B alpha/beta/delta family [Translation, ribosomal structure and biogenesis]. Translation initiation factor 2B subunit, eIF-2B alpha/beta/delta family is part of the Pathway/BioSystem: Translation factors
MERVAETAEEIREMEIHGAARIARAAAEALRDLAERSRAADPEEFRRELEAAARALRRARPSAASLPNAV
RRVLARVADGETVEEAREAVLEAADEFIERAEEAKERAAEIAAKRIRDGDTILTHSNSSTVLAAIEAAVP
QGKDIRVYVTESRPRYQGRITARELAEAGVPVTLIVDSAARHFLKEVDRVVVGADTITADGAVVNKIGTS
PLALAAREAGVPVTVAAETYKFSPETFELVEIEERDPSEVYDEEPEGVTVRNPAFDVTPPDLIDAIITER
GVLPPEAIYTVIRELLGWALREPW
>gnl|CDD|440798 COG1185, Pnp, Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ribosomal structure and biogenesis]
KKEFELGGRTLTLETGKLAKQADGAVLVRYGDTVVLVTVVASKEPREGIDFFPLTVDYQEKFYAAGKIPG
GFFKREGRPSEKEILTSRLIDRPIRPLFPKGFRNEVQVIATVLSVDPENDPDILAMIGASAALAISDIPF
NGPIGAVRVGYIDGEFVLNPTVEQLEESDLDLVVAGTKDAILMVEAEAKEVSEEVMLEAIMFGHEAIKKL
IEAQEELAAEAGKEKREYEPPEVDEELKAAVKELAEDKLKEAYQIPDKQEREEALDAIKEEVLEALAEEE
DEEDEKEVKEAFKKLEKKIVRRRILEEGIRIDGRKLDEIRPISCEVGVLPRTHGSALFTRGETQALVVAT
LGTLRDEQIIDGLEGEESKRFMLHYNFPPFSVGETGRMRGPGRREIGHGALAERALEPVLPSEEEFPYTI
RVVSEILESNGSSSMASVCGSSLALMDAGVPIKAPVAGIAMGLIKEGDKYAVLTDILGDEDHLGDMDFKV
AGTRDGITALQMDIKIDGITREILEEALEQAKEGRLHILDKMLEAISEPREELSPYAPRIITIKIPPDKI
RDVIGPGGKVIRKIIEETGAKIDIEDDGTVKIAATDGEAAEKAIERIEGITAEPEVGEIYEGKVVRIMDF
GAFVEILPGKDGLVHISELADERVEKVEDVLKEGDEVKVKVLEIDDQGRIKLSRKA
>gnl|CDD|440799 COG1186, PrfB, Protein chain release factor PrfB [Translation, ribosomal structure and biogenesis]. Protein chain release factor PrfB is part of the Pathway/BioSystem: Translation factors
AILTIHAGWAEMLLRMISPEIEIPESDLRIDTYRASGAGGQNVNKVSSAVRLTHDIASSSLPDSRLTPGG
IVVKAQEERSQHQNREDALKRLKALLYEAELEPKERRATKPTRGSKKRRLWGKQIRSMVKDLRGNVDDGD
>gnl|CDD|440800 COG1187, RsuA, Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ribosomal structure and biogenesis]. Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 is part of the Pathway/BioSystem: 16S rRNA modification
EGMRLQKFLANAGVGSRREAEELIEAGRVTVNGKVVTELGTKVDPGDEVTVDGKPLKLPEEPVYLLLNKP
AGVVSTTKDPEGRPTVFDLLPEARKERLFPVGRLDKDTEGLLLLTNDGELAHRLTHPKYGVEKEYLVRVD
GPVTEEDLERLREGVELEDGPTKPAKVEILSGEANTWLRITLTEGRNRQVRRMFEAVGLPVVRLKRVRIG
PLTLGDLPPGEWRELT
>gnl|CDD|440801 COG1188, HslR, Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain [Translation, ribosomal structure and biogenesis]
AAERMRLDKWLWAARFFKTRSLAAEACDGGRVRVNGQRAKPSREVKVGDVLTIRQGGRERVVRVLALSER
RGPAPEAQLLYEELTPSPAPREEAAAAAPRPRGAGRPTKKDRRELDRFRG
>gnl|CDD|440802 COG1189, YqxC, Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis]
ERLDVLLVERGLAESREKAQRLIMAGRVLVNGQVVDKPGTKVPEDAEIEVKGEELPYVSRGGLKLEGALD
AFGIDVAGKVCLDIGASTGGFTDCLLQRGAAKVYAVDVGYGQLAWKLRQDPRVVVLERTNARYLTPEDLP
EPPDLVVIDVSFISLTLVLPALLALLKPGGELVALVKPQFEVGRERVGKGGVVRDPALHAEVIEKVLAAA
AELGLRVLGLTPSPITGPDGNIEFLLWLRKGGGPDPDI
>gnl|CDD|440803 COG1190, LysU, Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]. Lysyl-tRNA synthetase (class II) is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MSEEEDLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEEETGDEVSVAGRIMAKRD
MGKASFADLQDGSGRIQLYLRRDELGEEAYELFKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSL
RPLPEKFHGLTDPETRYRQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAA
RPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDM
MDLTEELIREAAEAVLGTTKVTYQGQEIDLSPPWRRITMVEAIKEATGIDVTPLTDDEELRALAKELGIE
VDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRDDPGLTERFELFIAGREIANAFSELN
DPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFPLM
RPEKK
>gnl|CDD|440804 COG1191, FliA, DNA-directed RNA polymerase specialized sigma subunit [Transcription]. DNA-directed RNA polymerase specialized sigma subunit is part of the Pathway/BioSystem: RNA polymerase
DLEELLRRYQEGDEEAREELIEEYLPLVKKIASRLAGRLPAELDDLIQVGLIGLIEAIDRFDPSKGVSFE
TYAVPRIRGAILDYLRDEDWVPRSVRELARKIEEAIEELEQELGREPTDEEIAEELGISLEEVQEALEAA
NAYQLLSLDEPLEDGDDLLDLLESGDPEEELEHEELREALAEAIEQLPERERLVLSLYYFEELTLKEIAE
VLGVSESRVSRLHKKALARLREYLKE
>gnl|CDD|440805 COG1192, ParA, ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility]
MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLE
DAIVPTEIPGLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAA
DSVLIPVQPEYLSLEGLAQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDT
VIPRSVALAEAPSAGKPVFEYDPKSKGAKAYRALAEELLERLE
>gnl|CDD|440806 COG1193, MutS2, dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]
MNEKTLEKLEFDKILELLAEYAVSELGKELARKLRPSTDLEEVERLLAETAEARRLLRLEGGLPLGGIPD
IRPLLKRAEEGGVLSPEELLDIARTLRAARRLKRFLEELEEEYPALKELAERLPPLPELEKEIDRAIDED
GEVKDSASPELRRIRREIRSLEQRIREKLESILRSASYQKYLQDAIITIRNGRYVIPVKAEYKGKIPGIV
HDQSASGQTLFIEPMAVVELNNELRELEAEERREIERILRELSALVREYAEELLENLEILAELDFIFAKA
RYALELKAVKPELNDEGYIKLKKARHPLLDLKKVVPIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTL
MAQSGLPIPAAEGSELPVFDNIFADIGDEQSIEQSLSTFSSHMTNIVEILEKADENSLVLLDELGAGTDP
QEGAALAIAILEELLERGARVVATTHYSELKAYAYNTEGVENASVEFDVETLSPTYRLLIGVPGRSNAFE
IARRLGLPEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEE
EKEEILEKAREEAEEILREARKEAEELIRELREAQAEEEELKEARKKLEELKQELEEKLEKPKKKAKPAK
PPEELKVGDRVRVLSLGQKGEVLEIPKGGEAEVQVGILKMTVKLSDLEKVEKKKPKKPKKRPAGVSVSVS
KASTVSPELDLRGMRVEEALPELDKYLDDALLAGLPEVRIIHGKGTGALRKGVREYLKRHPYVKSFRLGE
PGEGGDGVTVVELK
>gnl|CDD|440807 COG1194, MutY, Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair]
MDMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPED
EVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNV
KRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAF
AEGRQEELPVKKPKKKKPERYGAALVIRDDGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPEALERWLRE
ELGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK
>gnl|CDD|440808 COG1195, RecF, Recombinational DNA repair ATPase RecF [Replication, recombination and repair]
RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSFRTARDAELIRFGADGFRVR
AEVERDGREVRLGLGLSRGGKKRVRINGKPVRRLSDLAGLLPVVLFSPEDLRLVKGGPSERRRFLDRLLF
QLDPRYLDALSRYERALKQRNALLKQGREADLALLDVWDEQLAELGAAIIAARLAFLERLAPLFAEIYAA
LSGGKEELELRYRSGWLYESAELEEALLEALAENRERDLARGRTLVGPHRDDLEFTLNGKPAKKFASQGQ
QKSLVLALKLAQAELLKEETGEAPILLLDDVFAELDEERREALLELLADLGGQVFITTTDPEDFPALLER
AK
>gnl|CDD|440809 COG1196, Smc, Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]
MRLKRLELAGFKSFADPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSS
SRKPLGRAEVSLTFDNSDGTLPIDYDEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSI
IGQGMIDRIIEAKPEERRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAE
KAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE
LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE
EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE
EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA
ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA
AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA
RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL
AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE
RLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLETFDAVNENF
QELFPRLFGGGEAELLLTDPDDPLETGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFC
VLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLYGVTMQEPGVSRVVSVDLEEAEEL
AEA
>gnl|CDD|440810 COG1197, Mfd, Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and repair, Transcription]
GGGRLTLSGLPGSARALLLAALARALGRPLLVVTADEREAERLAEDLRFFLPDLPVLLFPAWETLPYDRF
SPSPDIVSERLATLRRLASGKPGIVVTPVRALLQRLPPPELLAAASLSLKVGDELDLEELRERLVAAGYE
RVDQVEEPGEFAVRGGILDIFPPGSEHPVRIEFFGDEIESIRTFDPETQRSLEKVDEVELLPAREFPLDE
EAIERFRERLRELFGLDPKLDELYEALSEGIAFAGIEYYLPLFYEELATLFDYLPEDALVVLDEPERIEE
AAEEFWEEIEERYEARRHDRGRPLLPPEELFLDPEELFAALKRRPRVTLSPFAALPEGAGVVNLGARPLP
SFAGQLEALLEELKRLLKDGGRVLLAAESEGRRERLLELLRDHGIPARLVESLAELSPGGVAITVGPLEH
GFELPDAKLAVITESELFGERVKRRRRKKKRSADAFIRDLSELKPGDYVVHVDHGIGRYLGLETLEVGGA
ERDYLVLEYAGGDKLYVPVDQLDLISRYVGSEGEAPKLDKLGGSDWQKAKAKAKKAVRDIAAELLKLYAE
RAARKGFAFSPDTPWQREFEAAFPYEETPDQLRAIEEVKADMESPRPMDRLVCGDVGFGKTEVALRAAFK
AVMDGKQVAVLVPTTLLAQQHYETFKERFAGFPVRVEVLSRFRTAKEQKETLEGLADGKVDIVIGTHRLL
SKDVKFKDLGLLIIDEEQRFGVRHKEKLKALRANVDVLTLTATPIPRTLQMSLSGIRDLSIIATPPEDRL
PVKTFVGEYDDALIREAILRELLRGGQVFYVHNRVEDIEKVAARLQELVPEARIAVAHGQMSERELERVM
LDFYEGEFDVLVCTTIIETGIDIPNANTIIIERADRFGLAQLYQLRGRVGRSHRRAYAYLLYPPDKVLTE
DAEKRLEAIQEFTELGAGFKLAMHDLEIRGAGNLLGEEQSGHIAEVGFDLYLQMLEEAVAALKGGKEPEE
EWEPEINLGVPALIPEDYIPDVRQRLELYKRIASAESEEELDELQEELIDRFGPLPEEVENLLAVARLKL
LARRLGIEKIDAGGKGIRIEFSPNTPLDPEKLIRLIQKQPGRYKLDGDDKLVITLDLEDPEERLEALEEL
LEALAKLAKE
>gnl|CDD|440811 COG1198, PriA, Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair]
MKIAEVALPVPLDRPFDYLVPEGLELVQPGSRVLVPFGRRQVVGIVVGLKEESDVDPAKLKPILAVLDDE
PLLPEELLELLRWVADYYLCPLGEVLRLALPAGLRQGYPARIKTERYVRLTLGEELPKRAPKQRRVLEAL
REHGGPLTLSELAKEAGVSRSVLKALVKKGLLEIEEREVDRDPFAPDVPAEPPPTLNEEQQAAVEAIRAA
AGGFSVFLLHGVTGSGKTEVYLQAIAEVLAQGKQALVLVPEIALTPQTVERFRARFGARVAVLHSGLSDG
ERLDEWRRARRGEARIVIGTRSALFAPFPNLGLIIVDEEHDSSYKQEDGPRYHARDVAVVRAKLEGAPVV
LGSATPSLESLYNAQKGRYRLLELPERAGGAPLPEVELVDMREEPLEGGRILSPPLLEAIEETLERGEQV
LLFLNRRGYAPFLLCRDCGWVAKCPNCDVSLTYHRSRRRLRCHYCGYEEPVPKQCPECGSDSLRPFGPGT
ERVEEELAELFPDARVLRMDRDTTRRKGALEKLLEAFARGEADILVGTQMLAKGHDFPNVTLVGVLDADL
GLNSPDFRAAERTFQLLTQVAGRAGRAEKPGEVLIQTYNPEHPVIQALLNHDYEAFYEEELAERKAAGYP
PFGRLALLRASGKDEEAAEEFAQALARALRALLSADGVEVLGPAPAPIARLRGRYRWQLLLKAPSRAALQ
QLLRALLALLEKPLPRKVRWSIDVDPQS
>gnl|CDD|440812 COG1199, DinG, Rad3-related DNA helicase DinG [Replication, recombination and repair]
ADDGLLALAFPGFEPRPGQREMAEAVARALAEGRHLLIEAGTGTGKTLAYLVPALLAARETGKKVVISTA
TKALQEQLVEKDLPLLRKALGLPLRVALLKGRSNYLCLRRLEQALQEGDDLDDEELLLARILAWASETWT
GDRDELPLPEDDELWRQVTSDADNCLGRRCPYYGVCPYELARRLAREADVVVVNHHLLFADLALGEELLP
EDDVLIIDEAHNLPDRARDMFSAELSSRSLLRLLRELRKLGLRPGLKKLLDLLERLREALDDLFLALEEE
EELRLALGELPDEPEELLEALDALRDALEALAEALEEELERLAELDALLERLEELLFALARFLRIAEDEG
YVRWLEREGGDVRLHAAPLDPADLLRELLFSRARSVVLTSATLSVGGPFDYFARRLGLDEDARTLSLPSP
FDYENQALLYVPRDLPRPSDRDGYLEAIAEAIAELLEASGGNTLVLFTSYRALEQVAELLRERLDIPVLV
QGDGSREALLERFREGGNSVLVGTGSFWEGVDLPGDALSLVIIVKLPFPPPDDPVLEARREALEARGGNG
FMYAYLPPAVIKLKQGAGRLIRSEEDRGVVVLLDRRLLTKRYGKRFLDSLPPFRRTRPEELRAFLERLD
>gnl|CDD|440813 COG1200, RecG, RecG-like helicase [Replication, recombination and repair]
MAPLDTPLTYLKGVGPKRAKLLAKLGIRTVGDLLFHLPRRYEDRTRLTPIAELRPGETVTVEGTVVSVEV
VRRRRRRRILEVTLSDGTGSLTLVFFNQPYLKKQLKPGTRVLVSGKVERFRGGLQMVHPEYELLDEEEAE
LAGRLTPVYPLTEGLSQKTLRKLIRQALDLLAPDLPEPLPEELRARYGLPSLAEALRNIHFPPSDEDLHP
ARRRLAFEELLALQLALLLRRARRRKRKGPALPGDGELLEAFLAALPFELTGAQKRVIAEIAADLASPHP
MNRLLQGDVGSGKTVVALLAMLAAVEAGYQAALMAPTEILAEQHYRSLSKLLEPLGIRVALLTGSTKAKE
RREILAALASGEADIVVGTHALIQDDVEFKNLGLVVIDEQHRFGVEQRLALREKGEAPHVLVMTATPIPR
TLAMTLYGDLDVSVIDELPPGRKPIKTRVVPEERRDEVYERIREEIAKGRQAYVVCPLIEESEKLDLQAA
EETYEELREAFPGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNATVMVIENAERFG
LSQLHQLRGRVGRGSAQSYCLLLYDAPLSETARERLEVMRETNDGFEIAEEDLELRGPGEFLGTRQSGLP
DLRIADLVRDADLLEAAREDAEELLEEDPELASHPALRRWLGLRFRDEDYLEVG
>gnl|CDD|440814 COG1201, Lhr, Lhr-like helicase [Replication, recombination and repair]
MSAEDVLSLLHPAVRAWFAARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDELARRPRP
GELPDGLRVLYISPLKALANDIERNLRAPLEEIGEAAGLPLPEIRVGVRTGDTPASERQRQRRRPPHILI
TTPESLALLLTSPDARELLRGVRTVIVDEIHALAGSKRGVHLALSLERLRALAPRPLQRIGLSATVGPLE
EVARFLVGYEDPRPVTIVDAGAGKKPDLEVLVPVEDLIERFPWAGHLWPHLYPRVLDLIEAHRTTLVFTN
TRSQAERLFQRLNELNPEDALPIAAHHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVIQ
VGSPKSVARLLQRIGRAGHRVGEVSKGRLVPTHRDELVECAAALEAARAGEIEARRPPRNPLDVLAQHIV
AMAAGGPFDVDELYAEVRRAYPYRDLTREDFDAVLDFLAGGGPSLRAYERYARIVRDRVDGRLGARRGAA
RLARTNIGTIPDRGMLKVRLVRGGRRLGELEEEFVEELRPGDVFVLGGRSLRIERIRGMRVYVRPAPGKP
PTVPSWFGERLPLSTELARAVGAFLRELAEWEAARAWLREYGLDEPAARALREYLEEQRAATSALPTDDT
LLVERFRDEEGDWHLVVHPFEGRRVHEALGLLLAYRLSRRFGIPLGFAANDYGFVLRLPDPVPLLDLLRL
FDPDNLEDDLEAALNGSELFKRRFRECAARALLIPRRYPGKRKSLRQQQASSDLLLDVLREYPDHPLLRE
TYRECLEDLLDLPRLRELLERIEGGRIRVVEVELDRPSPFAFPLLVERGRDAVLAERRAADLLRLDERLL
AELLGEADRE
>gnl|CDD|440815 COG1202, COG1202, Superfamily II helicase, archaea-specific [Replication, recombination and repair]
MTLFLHPQKGEYLVVPIRDGERLFRGKLELKETPAGPRPGKFRVKRGSQEEPRPPDEFVELLRRAERIRI
SQQTSAEFEEMLDGYQLEAKVVRTCRFCLLEGRYTPLTEKTAIKYGGEYICPDCAKEELERELSFSGGFT
GAAQDRLEELLLEVRDLDRVLNLLSGRLDPDLTKFDEISATTDEVDTVPVDDLDLPPELKDLLEGRGEEL
LPVQSLAVENGLLEGKDQLVVSATATGKTLIGELAGIKNALEGKGKMLFLVPLVALANQKYEDFKDRYGD
GLDVSIRVGASRIRDDGTRFDPNADIIVGTYEGIDHALRTGRDLGDIGTVVIDEVHMLEDPERGHRLDGL
IARLKYYCPGAQWIYLSATVGNPEELAKKLGAKLVEYEERPVPLERHLTFADGREKIRIINKLVKREFDT
KSSKGYRGQTIIFTNSRRRCHEIARALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDF
PASQVIFDSLAMGIEWLSVQEFHQMLGRAGRPDYHDRGKVYLLVEPGKSYHRSMEMTEDEVAFKLLKGEM
EDVAVEYDEEAAVEETLANVVVGGGKAKRLNDRMLGEIPTKHALGKLLEYGFIDGLEPTPLGRAVARHFL
GPEEAFLILDGVRKGDDPLEIVAELELFDEEYLKNARQLSRALGTNVPSRAFHTLDILSSGLEKLDPKLR
DQLLDFAKDLDCGCEDERKFSEKILELRAEGLDPSQISRILEDEYGIYAYPGDILSYLDNSVRTLEAVER
IARKPELAKEAKRLKRKIEG
>gnl|CDD|440816 COG1203, Cas3, CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]. CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
LALLAKEALLGALALAALLLLLLALLLAALLLLLLAALLLALLLALLLLAALELALLLLLLLLLLLLLLL
LLLDLLLDDLAFLFLLLLIDADWLDSANFDMARQALDHLLAERLERLLPKKSKPRTPINPLQNEALELAL
EAAEEEPGLFILTAPTGGGKTEAALLFALRLAAKHGGRRIIYALPFTSIINQTYDRLRDLFGEDVLLHHS
LADLDLLEEEEEYESEARWLKLLKELWDAPVVVTTIDQLFESLFSNRKGQERRLHNLANSVIILDEVQAY
PPYMLALLLRLLEWLKNLGGSVILMTATLPPLLREELLEAYELIPDEPEELPEYFRAFVRKRVELKEGPL
SDEELAELILEALHKGKSVLVIVNTVKDAQELYEALKEKLPDEEVYLLHSRFCPADRSEIEKEIKERLER
GKPCILVSTQVVEAGVDIDFDVVIRDLAPLDSLIQRAGRCNRHGRKEEEGNVYVFDPEDEGGGYVYDKPL
LERTRELLREHDEILPEDKRELIEEYYRELYELLPDELDSFKEIL
>gnl|CDD|440817 COG1204, BRR2, Replicative superfamily II helicase [Replication, recombination and repair]
MKVAELPLEKVIEFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGKAL
YIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDL
VVVDEAHLIDDESRGPTLEVLLARLRRLNPEAQIVALSATIGNAEEIAEWLDAELVKSDWRPVPLNEGVL
YDGVLRFDDGSRRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAE
ELLEVSEETHTNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR
DTKRGGMVPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDEADELFERYILGEPEPIRSKLANESALRT
HLLALIASGFANSREELLDFLENTFYAYQYDKGDLEEVVDDALEFLLENGFIEEDGDRLRATKLGKLVSR
LYIDPLTAAELVDGLRKADEEFTDLGLLHLILILRDWIN
>gnl|CDD|440818 COG1205, YprA, ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair]
MARLEELLERLRASPRYGDQIVHVRTIPAREARYAPWPDWLPPELRAALKKRGIERLYSHQAEAIEAARA
GKNVVIATPTASGKSLAYLLPVLEALLEDPGATALYLYPTKALARDQLRRLRELAEALGLGVRVATYDGD
TPPEERRWIREHPDIVLTNPDMLHYGLLPHHTRWARFFRNLRYVVIDEAHTYRGVFGSHVANVLRRLRRI
CRHYGSDPQFILASATIGNPAEHAERLTGRPVTVVDEDGSPRGERTFVLWNPPLVDDGIRRSALAEAARL
LADLVREGLRTLVFTRSRRGAELLARYARRALREPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVS
TNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVAGDDPLDQYYVRHPEELFERPPE
AAVIDPDNPYVLAPHLLCAAAELPLTEGDLELFGPEARELLDALVEEGLLRRRGDGWYWTGDDRPARDVS
LRGAGGENVVIVDATTGRVIGTVDLPRALRELHPGAIYLHQGETYRVEELDLEERKAYVRPVDVDYYTRA
LSETDIRILEVLEERELGGVTVHFGEVEVTEQVTGYKKRRLYTGEVLGEVPLDLPPRTLRTKAVWLTIPP
DLLEAAGLDPEDFPGALHAAEHALIGLLPLFALCDRWDIGGVSTPLHPDTGAPTIFIYDGYPGGVGLAER
GYERFEELLEATRDLIASCPCEDGCPSCVQSPKCGNGNEPLDKAAALRLLEALLGGAP
>gnl|CDD|440819 COG1206, TrmFO, Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and biogenesis]. Folate-dependent tRNA-U54 methylase TrmFO/GidA is part of the Pathway/BioSystem: tRNA modification
MKPVTVIGGGLAGSEAAWQLAERGVPVRLYEMRPVKMTPAHKTDGFAELVCSNSLRSDDLTNAVGLLKEE
MRRLGSLIMAAADAHRVPAGGALAVDREGFSAAVTEKLENHPNITVVREEVTEIPEDGPVIIATGPLTSD
ALAEAIQELTGEEYLYFYDAIAPIVDADSIDMDKAFRASRYDKGEADYLNCPMTKEEYEAFYEALLAAEK
VELKDFEKEKYFEGCLPIEVMARRGRDTLRFGPMKPVGLTDPRTGKRPYAVVQLRQENAEGTLYNLVGFQ
TKLKWGEQKRVFRMIPGLENAEFVRYGVMHRNTFINSPKLLDPTLQLKARPNLFFAGQITGVEGYVESAA
SGLLAGINAARLLLGKEPVPPPPTTALGALLNYITGADPKDFQPMNVNFGLLPPLEKRIRDKKERKEAYA
ERALEDLEAWLAELGL
>gnl|CDD|440820 COG1207, GlmU, Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis]
SPLAVVILAAGKGTRMKSKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADLDVEF
VLQEEQLGTGHAVQQALPALPGDDGTVLVLYGDVPLIRAETLKALLAAHRAAGAAATVLTAELDDPTGYG
RIVRDEDGRVLRIVEEKDATEEQRAIREINTGIYAFDAAALREALPKLSNDNAQGEYYLTDVIAIARADG
LKVAAVQPEDPWEVLGVNDRVQLAEAERILQRRIAERLMRAGVTIIDPATTYIDGDVEIGRDVVIDPNVI
LEGKTVIGEGVVIGPNCTLKDSTIGDGVVIKYSVIEDAVVGAGATVGPFARLRPGTVLGEGVKIGNFVEV
KNSTIGEGSKVNHLSYIGDAEIGEGVNIGAGTITCNYDGVNKHRTVIGDGAFIGSNTNLVAPVTIGDGAT
IGAGSTITKDVPAGALAIARARQRNIEGWVRPKKKKK
>gnl|CDD|440821 COG1208, GCD1, NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis]
KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFG
VRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRY
GVVELDGDGRVTRFVEKPEEPPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGY
WLDIGTPEDLLEANALLLSGKAPVVIWP
>gnl|CDD|440822 COG1209, RmlA1, dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]
MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQ
LGIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDP
ERYGVVEFDEDGRVVSLEEKPKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKL
VVELLGRGFAWLDTGTHESLLEANRFVLTIEKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGP
YLLRLLDSNRARVK
>gnl|CDD|440823 COG1210, GalU, UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]
MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRS
YELEATLEAKGKEELLEEVRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPC
LKQMIEVYEETGGSVIAVQEVPPEEVSKYGIVDGEEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTP
EIFDILEKTKPGAGGEIQLTDAIAALAKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFRE
YLKELLKE
>gnl|CDD|440824 COG1211, IspD, 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]. 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVR
VVAGGATRQDSVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDD
GRVTETVDRSGLWAAQTPQGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPE
DLALAEALLRSRER
>gnl|CDD|440825 COG1212, KdsB, CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]. CMP-2-keto-3-deoxyoctulosonic acid synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis
MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASKGADRVVVATDDERIADAVEAFGGEVVMTS
PDHPSGTDRIAEAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDPEADMATLATPITDEEELFN
PNVVKVVTDKNGRALYFSRAPIPYPRDAFAEDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLR
ALENGYRIKVVETDAPPIGVDTPEDLERVRAL
>gnl|CDD|440826 COG1213, COG1213, Choline kinase [Lipid transport and metabolism]
KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGPDV
TFVYNPDYDETNNIYSLWLAREALDEDFLLLNGDVVFDPAILKRLLASDGDIVLLVDRKWEKPLDEEVKV
RVDEDGRIVEIGKKLPPEEADGEYIGIFKFSAEGAAALREALEALIDEGGPNLYYEDALQELIDEGGPVK
AVDIGGLPWVEIDTPEDLERAEELFA
>gnl|CDD|440827 COG1214, TsaB, tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal structure and biogenesis]. tRNA A37 threonylcarbamoyladenosine modification protein TsaB is part of the Pathway/BioSystem: tRNA modification
MLILAIDTSTEACSVALLDDGEVLAEREENDGRGHSERLLPMIDELLAEAGLTLSDLDAIAVGIGPGSFT
GLRIGVATAKGLALALGIPLVGVSSLEALAAQAPRAGAGLVLVAIDARRGEVYWAVYDADDGELERLGEP
RVLAPEELAEPLAGGPVLFVGDGAEAYAELLAEALAVLADALALPSAAALARLAAARLAAGEAEDPADLE
PLYLRDPDAEPPAERKA
>gnl|CDD|440828 COG1215, BcsA, Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility]
LLLLLALLALLYLLLLALARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGS
TDETAEIARELAAEYPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG
VGASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWA
RGGLQLLLKHRPLLRPRRLLLFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHL
LYGLLLLLAALRGKKVVWKKTPR
>gnl|CDD|440829 COG1216, WcaE, Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism]
MRPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRVRVIRNPENLGFA
AARNLGLRAAGGDYLLFLDDDTVVEPDWLERLLAAACLLIRREVFEEVGGFDERFFLYGEDVDLCLRLRK
AGYRIVYVPDAVVYHLGGASSGPLLRAYYLGRNRLLFLRKHGPRPLLRLALLRGLRLRLRGR
>gnl|CDD|440830 COG1217, TypA, Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms]
MMREDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVK
INIVDTPGHADFGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDE
VVDEVFDLFIELGATDEQLDFPVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLV
TNLDYSDYVGRIAIGRIFRGTIKKGQQVALIKRDGKVEKGKITKLFGFEGLERVEVEEAEAGDIVAIAGI
EDINIGDTICDPENPEALPPIKIDEPTLSMTFSVNDSPFAGREGKFVTSRQIRERLEKELETNVALRVEE
TDSPDAFKVSGRGELHLSILIETMRREGYELQVSRPEVIFKEIDGKKLEPIEELTIDVPEEYSGAVIEKL
GQRKGEMTNMEPDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIMNHVFDGYEPYKGEIPGRRNGSLIS
METGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNMRASGSDEAIRLTPP
RKMSLEQALEFIEDDELVEVTPKSIRLRKKILDENERKRAAKKKKK
>gnl|CDD|440831 COG1218, CysQ, 3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism]
LEALLEAAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAI
PYEERKSWDRFWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGG
GERQPIRVRDRPPAEPLRVVASRSHRDEETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTME
WDTAAGQAILEAAGGRVTDLDGKPLRYNKKEDLLNPGFIASGDHAAILAA
>gnl|CDD|440832 COG1219, ClpX, ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones]
MAGDSKKELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEEEAEEELKKLPKPKEIKAFL
DEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIA
DATTLTEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLK
ILEGTVANVPPQGGRKHPQQEFIQIDTTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKSKKEKDEGE
LLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEAL
EAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVITKEVVEGKAKPILVYK
>gnl|CDD|440833 COG1220, HslU, ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones]
MSELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRL
AKLANAPFIKVEATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPK
KKAGSNNPFEEEEEEEEEEEEISRTREKFRKKLREGELDDREIEIEVEESSSPGVEIMGPPGMEEMGMNL
QDMFGNLMPKKKKKRKVKVKEARKILTQEEAAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSG
PDVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGAFHVSKPSDLIPELQGRFPIRVELDSLTEED
FVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEVNERTENIGARRLHTVMEKLLEDISFE
APDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL
>gnl|CDD|440834 COG1221, PspF, Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms]
MKRKEKILNYLKELTKNLSLEKKSEGFTAEEIAEKLGISRNNVSHELNELVKEGKLIKINGRPVLFLDKE
AFEEQFGTKLKSEYSFVELLAEKENNEEEEDPFDNLIGANGSLKNAIEQAKAAILYPPKGLHTLILGPTG
VGKSFFAELMYEYAIEIGVLPEDAPFVVFNCADYANNPQLLMSQLFGYVKGAFTGADKDKEGLIEKADGG
ILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGETEKTRKANVRIIFATTEDPESSLLKTFLRRIPMVIKLP
SLEERSLEERLELIKHFFKEEAKRLNKPIKVSKEVLKALLLYDCPGNIGQLKSDIQLACAKAFLNYITNK
KEEIEITLSDLPENVKKGLLKLKENREELDKLSEYLEEYLIISPDTEKKLISEEDEYELPYNFYEIIEDK
YEELKSEGLSEEEINKIISKDIESYFKKLIFKLDKSNISEELLLIVVDEVIVNVVEIFEEAEKKLLRYNS
SNLFIALSLHLLSTLLRIKKGKKIINPQLNEIKKKYYEEFILAAEAIKIIEEELKILIPDEEEGFILLLL
IELKEEKSLSENVIVVVVIAHGGAAASSSMAVVNLLLLEVAVAAIDDPPLEVVDVLIEEKTIVVIINKGK
GGLLLLLDDGGSLFGIIIIEEEGIIIVTVVIVSTTTVLEAAARKKLLELDLDEIIVLEELLKNPLESKKI
KISTSKKKKIIVTTIAITTGEAGGILILILIIELLDKDLILIIIEILLIIIKEEILEKIIEEKKEVIIIV
IISIIPLIIPPIILLLALKLIILIEILVLLEILIDKEKIENIIKELLSLLNIIIVLLIIDILILI
>gnl|CDD|440835 COG1222, RPT1, ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones]
GNDLLTIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPA
ESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPF
IRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF
ESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEG
FSGADLKAIVTEAGMFAIREGRDTVTMEDLEKAIEKVKKKTETATN
>gnl|CDD|440836 COG1223, COG1223, Predicted ATPase, AAA+ superfamily [General function prediction only]
LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDS
LIGSYLGETARNLRKLFDFARRAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGLPSGSVVIA
ATNHPELLDSALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKT
ALKKAILEDREKVTKEDLEEALKQRKERKKEPKKEG
>gnl|CDD|440837 COG1224, TIP49, DNA helicase TIP49, TBP-interacting protein [Transcription]
MSEIREIEKVKEFERISAHSHIRGLGLDENGKAKFVADGLVGQVEAREAAGIVVKMIKEGKMAGKGILIV
GPPGTGKTALAVAIARELGEDTPFVAISGSEIYSAELKKTEFLMQALRKAIGVRVREKRKVYEGVVKEIK
IRYARHPYNPYVKVPREATITLATKDEEKTLTVGEEIAQQLVELGIRKGDVIWIDAETGRVSKLGRAKGE
GAKTYDIETKRIVEVPSGPVKKEKEIVRTLTLHDLDLYLAAQRAAFSALFGFFEEREIPSEVRKQVDELV
KKWIEEGKAELVPGVLFIDDAHMLDIEAFSFLTRAMESELAPIIILATNRGITKIRGTDIESPHGIPLDL
LDRLLIIPTRPYTEDEIREIIKIRAEEEDIELSDDALEELTKIGVERSLRYAVQLLEPAYIIAKRRGRSK
VTVEDVEEASKLFADVKESVEYVKEYEELFLK
>gnl|CDD|440838 COG1225, Bcp, Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]
APDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKK
FAEKYGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLEALLAELK
>gnl|CDD|440839 COG1226, Kch, Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism]
LGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAALALAALLLLLLLAGGGGFFLLLLLAAAALL
LLLLLAAALLLLLVLLLLLLLLLLLLLLALLLLLLALAAREEEAEAAEDAIDLEGHVIIAGFGRVGQIVA
RLLRAEGIPFVVIDLDPERVEELRRFGIKVYYGDATRPDVLEAAGIERARALVVAIDDPEAALRIVELAR
ELNPDLKIIARARDREHAEELRQAGADEVVRETFESALQLARHALEALGVPEEEAARAIQEFRRRDYER
>gnl|CDD|440840 COG1227, PPX1, Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion]
MMKILVFGHKNPDTDSICSAIAYAYLKNQLGEDAEAVRLGEPNPETAFVLDYFGVEAPELIEDVAAGKKV
ILVDHNELAQSVDGIDEAEILEIIDHHRIGDFETAAPLYIRIEPVGCTATIIAKLYKENGVEIPKEIAGL
MLSAILSDTLLFKSPTTTDEDREAAEELAEIAGVDIEAYGLEMFKAKSDLSGKSAEELLRMDAKEFEMGG
KKVGIGQVETVDPEEVLDRKDELEAAMKKVKAEKGYDLVLLLVTDILNEGSTLLVVGDDVAVVEKAFGVT
LENNTVWLPGVVSRKKQVVPPLTEAFA
>gnl|CDD|440841 COG1228, HutI, Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism]
KKAPAQAGTLLITNATLVDGTGGGVIENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDA
HTHLGLGGGRAVEFEAGGGITPTVDLVNPADKRLRRALAAGVTTVRDLPGGPLGLRDAIIAGESKLLPGP
RVLAAGPALSLTGGAHARGPEEARAALRELLAEGADYIKVFAEGGAPDFSLEELRAILEAAHALGLPVAA
HAHQADDIRLAVEAGVDSIEHGTYLDDEVADLLAEAGTVVLVPTLSLFLALLEGAAAPVAAKARKVREAA
LANARRLHDAGVPVALGTDAGVGVPPGRSLHRELALAVEAGLTPEEALRAATINAAKALGLDDDVGSLEP
GKLADLVLLDGDPLEDIAYLEDVRAVMKDGRVVDRS
>gnl|CDD|440842 COG1229, FwdA, Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]
MELIIKNGRVYDPANGIDGEVMDIAIKDGKIVEEPSDPKDAKVIDASGKVVMAGGVDIHTHIAGGKVNVG
RMMRPEDHRADPRPRTGLTRSGSGFSVPSTFATGYRYAEMGYTTVFEAAMPPLNARHTHEEMADTPIIDK
GAYPLLGNNWFVLEYLKEGDQEKAAAYVAWLLRATKGYGIKVVNPGGVEAWKWGKNVLDLDDPVPYFGVT
PREILKGLARANEELGLPHSLHVHCNNLGVPGNYETTLDTMKAAEGLKPKEQVLHLTHVQFHSYGGEGWR
DFSSGAAEIAEYVNKHPNITIDVGQVTFGETTTMTADGPMEYDLHKLAGLKWANMDVELETGCGVVPFIY
RPKNFVNALQWAIGLELFLLVKDPWRVFLTTDHPNGGPFTRYPRLIALLMSKKFRDEMLAKLHPWAAARS
TLASIDREYSLYEIAIMTRAGPAKALGLADRGHLGVGADADIAIYDINPDDKDYEDIEKMFSKPAYVIKD
GEVVVKDGEIVATPQGRTHWVDPKVDENPEIEKDLREKFDRYYTVNLENYPVSDEYLPNPVRIE
>gnl|CDD|440843 COG1230, CzcD, Co/Zn/Cd efflux system component [Inorganic ion transport and metabolism]
MGHGHGHSHHHAAASSERRLLIALALTLGFMVVEIVGGLLSGSLALLADAGHMLSDALALGLALFAYRLA
RRPADARFTFGYKRAEILAALANALLLLVVAGYILYEAIQRLFNPPPVAGGGMLVVAVIGLVVNLVSAWL
LHRGSKHDLNLRGAYLHVLADALGSVAVIVAALVILFTGWTWLDPLLSLLIALLILRSAWGLLRESLRIL
LEGVPDGIDLEEVRAALEALPGVADVHDLHVWSLSSGENALTAHVVVDDGADADAILDEIRELLAERFGI
EHVTIQIETEACAD
>gnl|CDD|440844 COG1231, YobN, Monoamine oxidase [Amino acid transport and metabolism]
MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHT
NLLALARELGLPLEPFPNENGNALLYLGGKRVRAGEIAADLRGVAELLAKLLRALAAALDPWAHPAAELD
RESLAEWLRRNGASPSARRLLGLLGAGEYGADPDELSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAA
ELGDRIRLGAPVTRIRQDGDGVTVTTDDGGTVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGA
AIKVFLQFDRPFWEEDGLYGGISLTDLPIRQTWYPSNGPDGGAGVLLGYVGGDDARALAALSPEERVAAA
LEQLARIFGVYAAEPVDYVSTDWGRDPWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEWPGWV
EGALESGERAAAEILARLGG
>gnl|CDD|440845 COG1232, HemY, Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]. Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVDGFRIDRGPHSFLTRDPEVLELLRE
LGLGDELVWPNTRKSYIYYGGKLHPLPQGPLALLRSPLLSLAGKLRALLELLAPRRPPGEDESLAEFVRR
RFGREVYERLVEPLLEGVYAGDPDELSADWAFPRLKRLELEHGSLIKGALALRKGAKAGEVFGYLRGGLG
TLVEALAEALEAGEIRLGTRVTAIEREGGGWRVTTSDGETIEADAVVSATPAPALARLLAPLPPEVAAAL
AGIPYASVAVVALGFDRPDLPPPDGFGWLVPRDEGVPILAVTFSSNKWPHRAPDGKVLLRLEVGGAGDPE
LWQLSDEELVALALADLRKLLGIDAEPVDTRVVRWPKAYPQYTVGHLERVAAIREALAALPGLYLAGRAY
DGVGLPDCIRSGREAAERILAEL
>gnl|CDD|440846 COG1233, COG1233, Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism]
MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFERPGFRFDVGPSVLTMPGVLERLFR
ELGLEDYLELVPLDPAYRVPFPDGRALDLPRDLERTAAELERLFPGDAEAYRRFLAELRRLYDALLEDLL
YRPLLSLRDLLRPLALARLLRLLLRSLRDLLRRYFKDPRLRALLAGQALYLGLSPDRTPALYALIAYLEY
AGGVWYPKGGMGALADALARLAEELGGEIRTGAEVERILVEGGRATGVRLADGEEIRADAVVSNADPAHT
YLRLLGEEALPARYRRRLERFRYSPSAFKLYLGLDGPLPGLAHHTIHLSEDYEAAFDDIFRGRLPEDPSL
YVSIPSLTDPSLAPEGKHTLWVLVPVPYGLEDAWDELKEEYAERILARLERYAPGLRDRIVAREVLTPLD
FERYLNLVGGAIYGGAHTLDQSAFFRPSNYRTPIPGLYLVGASTHPGGGVPGVLISGRLAARRILKDLKR
A
>gnl|CDD|440847 COG1234, ElaC, Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis]
MKLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLP
GLLSTRSLAGREKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGGFTVTAFPLDHPVP
AYGYRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVK
RLVLTHFSPRYDDPEELLAEARAVFPGPVELAEDGMVIEL
>gnl|CDD|440848 COG1235, PhnP, Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]
MKVTFLGSGSSGGVPQIGCDCPVCASTDPRYGRTRSSILVEADGTRLLIDAGPDLREQLLRLGLDPSKID
AILLTHEHADHIAGLDDLRPRYGPNPIPVYATPGTLEALERRFPYLFAPYPGKLEFHEIEPGEPFEIGGL
TVTPFPVPHDAGDPVGYRIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDDPEPGHLSNEEALE
LLARLGPKRLVLTHLSPDNNDHELDYDELEAALLPAGVEVAYDGMEIEL
>gnl|CDD|440849 COG1236, YSH1, RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis]
MKLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLL
VKEGFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGGVRVTF
HPAGHILGSAQVELEVGGKRIVFSGDYGREDDPLLAPPEPVPPADVLITESTYGDRLHPPREEVEAELAE
WVRETLARGGTVLIPAFALGRAQELLYLLRELKKEGRLPDIPIYVSGMAIRATEIYRRHGEYLRDEAQDP
FALPNLRFVTSVEESKALNRKGPAIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLR
GAKEVKIFGEEVPVRARVERLFGLSAHADWDELLEWIKATGKPERVFLVHGEPE
>gnl|CDD|440850 COG1237, COG1237, Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only]
SMKITVLVDNTAGDEGLLAEHGLSALIETEGKRILFDTGQSDVLLKNAEKLGIDLSDIDAVVLSHGHYDH
TGGLPALLELNPKAPVYAHPDAFEKRYSKRPGGKYIGIPFSREELEKLGARLILVKEPTEIAPGVYLTGE
IPRVTDFEKGDPGLYVKEDGGLVPDPFLDEQALVIKTDKGLVVITGCSHAGIVNILEYAKEVTGGKRIYA
VIGGFHLLGASEERIEKTIEALKELGVEKIYPGHCTGLEAIAALKERFGDRFIELGVGSVIEF
>gnl|CDD|440851 COG1238, YqaA, Uncharacterized membrane protein YqaA, VTT domain [Function unknown]
MLRRLYDWTRWALHRYGLWGLFLVSFLEATFLPIPSEVLLVPMLLAGPERAWLLALVATLGSVLGGLVGY
AIGRFLFEAVGRPLLERYGKEEKLERAQAWFRRYGFWALLLAGWTPIPGDVLTIAAGVLRLPLWPFLLAS
LIGRGARFFLVALLLLWFGPPI
>gnl|CDD|440852 COG1239, ChlI, Mg-chelatase subunit ChlI [Coenzyme transport and metabolism]
MMRTVFPFTAIVGQEEMKLALLLNAVDPGIGGVLIRGEKGTAKSTAVRALAALLPPIEVVKGCPYNCDPD
DPDELCPDCRERLAAGEELPTETRPVPVVELPLGATEDRVVGSLDLEKALKEGEKAFEPGLLARAHRGIL
YVDEVNLLDDHLVDVLLDAAAMGRNTVEREGVSVSHPARFVLVGTMNPEEGELRPQLLDRFGLSVEVEGP
RDPEERVEIVRRRLAFEADPEAFAAEYAEEQAELRERIAAARELLPEVTIPDELLRYIAELCIALGVDGH
RADIVIARAARALAALEGRTEVTAEDIRRAAELALPHRLRRDPFEEPGLDEEPPPPPGDEEDEE
>gnl|CDD|440853 COG1240, ChlD, vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism]
DLALALLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLL
AVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENRLEAAKGALLDFLDDYRPRDRVGLVAFGGEA
EVLLPLTRDREALKRALDELPPGGGTPLGDALALALELLKRADPARRKVIVLLTDGRDNAGRIDPLEAAE
LAAAAGIRIYTIGVGTEAVDEGLLREIAEATGGRYFRADDLSELAAIYREID
>gnl|CDD|440854 COG1241, Mcm2, DNA replicative helicase MCM subunit Mcm2, Cdc46/Mcm family [Replication, recombination and repair]
EESDLVDKFEEFLRRYKYRDEILELAQEYPEKRSLVVDYNDLYSFDPDLADDLLENPDEVLEAAEEALRE
IDLEPYDVSLGDAHVRITNLPETVPIRDIRSDHIGKLISVEGIVRKATEVKPKITEAAFECPRCGTETYV
PQTGEKLQEPHECPGCGRQGPFKLLPEKSEFIDAQKIRIQEPPEDLPGGQQPQSIDVILEDDLVGEVRPG
DRVTVTGILRIEQRTSGRGKSTIFDLYLEANSIEVEEKEFEEIEITEEDEEKIKELSKDPDIYEKIIASI
APSIYGYEEIKEAIALQLFGGVPKVLPDGSRIRGDIHILLVGDPGTAKSQLLRYAARLAPRGVYTSGKGS
TAAGLTAAAVRDDFGTGRWTLEAGALVLADGGLACIDELDKMREEDRSALHEAMEQQTISIAKAGIVATL
NARCSVLAAANPKYGRFDPYEPIAEQIDLPPTLLSRFDLIFVLRDKPDEERDRELARHILKVHRAGELLE
QEIEEETEEVKPEIDPDLLRKYIAYARRNVFPVLTEEAKDLIEDFYVDMRKKGEDEDSPVPITARQLEAL
IRLAEASARMRLSDTVTEEDAERAIRLVDSCLKDVGVDPETGKFDIDVIETGTSKSQRDKMKLIKDIIKE
LEEESSGGAPIEDVIEEAEEEGIDREKAEELIEKLKRKGEIYEPKPGHYKKV
>gnl|CDD|440855 COG1242, YhcC, Radical SAM superfamily enzyme [General function prediction only]
DKRYNTYSDYLKERFGEKVYKLPLDAGFTCPNRDGTLGRGGCTFCNEAGSGDEALSRSLSIKEQIEEGKE
FIRKKYKAKKFIAYFQAYTNTYAPVEVLKELYEEALAHPDVVGLSIGTRPDCLPDEVLDLLAELNERGEV
WVELGLQSAHDKTLKRINRGHDLAEFIDAVRRLRKRGIKVCTHLILGLPGETREDMLETAKILSALGVDG
VKLHPLHIVKGTPLAKMYERGEFKLLSLEEYVDLVVDFLERLPPDIVIHRLTGDAPRELLLAPNWSLKKW
EVLNAIDKELERRGTYQGKLY
>gnl|CDD|440856 COG1243, ELP3, tRNA U34 5-carboxymethylaminomethylation enzyme Elp3 (RNA elongator complex protein 3), contains radical SAM and acetyltransferase domains [Translation, ribosomal structure and biogenesis]
KKPVRTISGVAIIPVFTPPAGCPGKCVFCPQGKITPQSYTGQEPAALRARQNDYDPYKQVRARLEQLLAI
GHPVDKVELAFMGGTFTALPRDYQEWFLKRALDAMNGFDSPTLEEAQRRNETAEGRIVGIRLETRPDYID
EEILDRLLEYGVTKVELGVQSLDDEVLKRSNRGHTVEDVIEATRLLRDAGFKVGYHLMPGLPGSTPEKDL
ETFRELFEDDFRPDMLKIYPTLVIKGTELYELYKRGEYKPLTLEEAVELLAEIKLKFIPRYVRVIRIGRD
IPAKEIVAGPKHPNLRQLVESRLEEEGIKCRCIRCREVGHNDDPEDIELRREDYEASGGKEHFLSFEDKD
IDILIGFLRLRFPKTALVRELHVKGNGSWQHRGYGKRLLEEAEEIAREEGYKKLAVISGIGVREYYRKLG
YERDGPYMSKDL
>gnl|CDD|440857 COG1244, RaSEA, Archaeosine formation enzyme, radical SAM superfamily [Translation, ribosomal structure and biogenesis]
MSDMAELNKRIREIRPRKRPVDPDKPAAVWIEKDRLDGEVVDSLTIILRTRGCPWARAGGCTMCGYVADS
APGPVSAEDLIAQIDHALEKYDGSEAFVVKIYTSGSFLDPREVPPEAREAILERLAEDGVKKVIVESRPE
FVTEETLEEFREILGGKRLEVAIGLETSNDEIREKCINKGFTFKDFERAAELLKEAGIGVKAYLLLKPPF
LSEKEAIEDAIRSVEDAAPYADTISLNPTNVQKGTLVERLWKRGEYRPPWLWSVVEVLKEAKATVDARVL
SDPVGGGSKRGPHNCGKCDREVIDAIERFNLTQDIEVLEELDCDCKKEWEKVLELEDLSYGMPLTR
>gnl|CDD|440858 COG1245, Rli1, Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis]
MMRIAVVDRDRCQPKKCNYECIKYCPVNRTGKEAIEIDEDDGKPVISEELCIGCGICVKKCPFDAISIVN
LPEELEEDPVHRYGENGFRLYGLPVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVL
KRFRGTELQDYFKKLANGEIKVAHKPQYVDLIPKVFKGTVRELLEKVDERGKLDELAEKLGLENILDRDI
SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLAD
YVHILYGEPGVYGVVSKPKSVRVGINQYLDGYLPEENVRIRDEPIEFEVHAPRREKEEETLVEYPDLTKS
YGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYISPDYDGTVEE
FLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ
RLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGVHGHASGPMDMREGMNRFLKELGITF
RRDEETGRPRINKPGSYLDREQKERGEYYYYE
>gnl|CDD|440859 COG1246, ArgA, N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]. N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis
MTIRPATPDDVPAILELIRPYALEEEIGEFWVAEEDGEIVGCAALHPLDEDLAELRSLAVHPDYRGRGIG
RRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIDKEDLPYAKVWQRDSVVMEKDLE
>gnl|CDD|440860 COG1247, MnaT, L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism]
EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLG
PFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEV
GTLPEVGFKFGRWLDLVLMQKRL
>gnl|CDD|440861 COG1249, Lpd, Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]. Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGI
SAGAPSVDWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGGETLTADHIVIATGS
RPRVPPIPGLDEVRVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPE
ISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGV
ELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPE
IASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGFVKLIADAETGRILGAHIVGPHAGELIHEAA
LAMEMGLTVEDLADTIHAHPTLSEALKEAALALLGR
>gnl|CDD|440862 COG1250, FadB, 3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]. 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis
EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAALARI
TPTTDLAALADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHF
FNPVPLMPLVEVIRGPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASP
EDIDAAMRLGFGFPMGPFELADLVGLDTALAVLEVLYEALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYD
Y
>gnl|CDD|440863 COG1251, NirB, NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]
KMRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENG
IDLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALA
PGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEI
EGDDRVTGVRLADGEELPADLVVVAIGVRPNTELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPG
PVYGRRVLELVAPAYEQARVAAANLAGGPAAYEGSVPSTKLKVFGVDVASAGDAEGDEEVVVRGDPARGV
YKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAALPLKELK
>gnl|CDD|440864 COG1252, Ndh, NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]
MKRIVIVGGGFAGLEAARRLRKKLGGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAG
VRFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAA
FERAERRRLLTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPDKVRITLVEAGPRILPGLGEKLSEAAE
KELEKRGVEVHTGTRVTEVDADGVTLEDGEEIPADTVIWAAGVKAPPLLADLGLPTDRRGRVLVDPTLQV
PGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAV
ADVGGLKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL
>gnl|CDD|440865 COG1253, TlyC, Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only]
MSLLLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLA
GLLAGALGEAALAALLAPLLGSLGLPAALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVA
PPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFE
FGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYEGDLDDIVGVVHVKDLLRALLEGEPFD
LRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEIVGEIRDEYDEEEPEIV
KLDDGSYLVDGRLPIDELNELLGLDLPEEEDYETLGGLVLEQLGRIPEVGETVEVDGLRFEVLDMDGRRI
DKVLVTRLPEEEEEE
>gnl|CDD|440866 COG1254, AcyP, Acylphosphatase [Energy production and conversion]
MKRVRIIVSGRVQGVGFRAFTRRQARRLGLTGWVRNLPDGSVEVVAEGEEEAVEAFLEWLRKGPPAARVE
DVEVEEEEPTGEFEGFEIR
>gnl|CDD|440867 COG1255, MTH1000, Predicted small methyltransferase MTH1000, UPF0146 family [General function prediction only]
MMERAIAEYIADRLANYDRVVEVGIGRRPDVAAALAERGVDVTATDVNPRAVPEGVNFVRDDVFDPDLSL
YEGADAIYAIRPPPELQRPILELARKVGADLLFTTLGGEQPAVPPNGVERINYGGGTLYVARR
>gnl|CDD|440868 COG1256, FlgK, Flagellar hook-associated protein FlgK [Cell motility]
SLFSALNIALSGLNAAQRALDVTSHNIANANTPGYSRQRVVLSAAGPTATGAGQVGTGVRVTGIRRIRDE
FLDAQLRSANSDLGYAEARADALSQLEALLGEPSDTGLSTALDDFFNALQELASNPESSAARQAVLEAAQ
ALADRFNSLSSQLQDLRADADSQIASTVDEINSLLSQIADLNKQIVKAEAGGQDANDLLDQRDQLLDELS
ELVGVTVVEQDDGTVNVSTGNGQTLVDGDTASELSFTPSAGDPGGLSTVTLDDSGVPSDATSSITGGSLG
GLLELRDETLPEYQAQLDELARGLADAFNAVHAQGYDLNGNPGGDLFDIDPSITGGTLTPFDTVGAGNIS
VNPAVIGDPSLLAAANSDGGGAGDNTNALALAALQDAKLVFDSGGSGTLSDYYASLVSDLGVDAQQAKTE
AEAQEALLDQLENQRQSVSGVNLDEEMANLIKFQQAYQANARVITTADEMLDTLLNIVG
>gnl|CDD|440869 COG1257, HMG1, Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism]. Hydroxymethylglutaryl-CoA reductase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
RISGFSKLSVEERREFLAEFTGLSDEELEHLGNYSGLPQELADGMIENVIGTFQLPLGVAGNFLINGKDY
LVPMATEEPSVVAAASRGAKLIRESGGFKTTVLGDGMIGQPQFVDVGDARAAREWILENKEEILEAAESA
DPSMTKRGGGLRDIEVRVLLGNMVVLHLIVDTGDAMGANMVNTATEAVAPWIEELTGGEVLLRILSNYAT
GKLVRAEVTIPVEVLGKVLKVSGEEVAEKIVLASNFAGADPYRAATHNKGIMNGIDAVVIATGNDWRAVE
AGAHAYAARDGRYESLTTWKDEDGDLYGSITLPLAVGTVGGGTGLHPLAKEALKILGVPSAKELAEIIAA
VGLAQNLAALRALATEGIQKGHMKLHRRNIAIAAGATGEEIEKVARLFKEKTVSVDAAK
>gnl|CDD|440870 COG1258, Pus10, tRNA U54 and U55 pseudouridine synthase Pus10 [Translation, ribosomal structure and biogenesis]. tRNA U54 and U55 pseudouridine synthase Pus10 is part of the Pathway/BioSystem: tRNA modification
MDILEKARRILAEGPLCDHCLGRQFAKLSFGLTNAERGRALRTALALELDEPYEPVEPEECWVCEGLFDR
FDEWAERAAEALEGVEFETFLVGTRVPPLVEENEEELWEEAGLEAAEPLKSELNREVGKRVGALTGKEVD
FKRPDVVAILDLAEDRVELQVNPLFIYGRYRKLERGIPQTEWPCRECRGSGCERCGGTGKQYPESVEELI
GPPVIEAFDGEDAVFHGAGREDIDARMLGTGRPFVIEVKEPRRRDVDLDELEAEINEFADGKVEVEGLRF
ATREMVERVKESKASKTYRALVEFEGPVSEEKLKEALEELEGATIEQRTPTRVLHRRADLVRERTVYEIK
LELLDDRHAELEIHGEGGLYVKELVSGDEGRTEPSLAGLLGVQAEVTELDVLGVEGEDEPF
>gnl|CDD|440871 COG1259, COG1259, Bifunctional DNase/RNase [General function prediction only]
MIELEVVGVRVDPPSGSPVVLLKEEDGRRVLPIWIGPFEAQAIALALEGEKPPRPLTHDLLKNILEALGA
RLERVVIDDLKDGVFYARLVLKDGGEEVEIDARPSDAIALALRTGAPIYVAEEVLDEAGIPLEEEEEE
>gnl|CDD|440872 COG1260, INO1, Myo-inositol-1-phosphate synthase [Lipid transport and metabolism]
MRKIRVAIIGVGNCASSLVQGIEYYKDGEIDVPGLMHVDIGGYKPGDIEVVAAFDIDARKVGKDLSEAIF
AKPNNTIKFADVPKTGVRVRRGPVLDGLGGHLREYIEESSEEAPEDVVKELKESGADVLVNYLPVGSEEA
SRFYAEAALEAGVAFVNAIPVFIASDPEWAELFEEAGLPIIGDDIKSQVGATILHRTLAELFAERGVKVL
RTYQLNIGGNTDFLNMLERERLESKKISKTSAVTSILGYDDAPIHIGPSDYVPWLGDRKVAYIRIEGRGF
GGVPMNLEVKLEVWDSPNSAGVVIDAIRLAKLALDRGIGGPLYEPSAYFMKSPPVQYTDDEARAKQEEFI
EGELER
>gnl|CDD|440873 COG1261, FlgA, Flagellar basal body P-ring formation protein FlgA [Cell motility]
LLEARLWGRLSVGVRCDGKGWTVYVPARVAVYGEVVVAARPLARGEVITADDLRLEEGDLARLPGGALTD
PDELVGKVARRSLRAGQPLRASDLRAPPLVKRGQTVTIVARGGGFSVSAEGRALENGALGDRIRVRNLSS
GKVVSGRVVGDGTVEVGL
>gnl|CDD|440874 COG1262, YfmG, Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones]
PESFAGNAVGLEMVLIPGGTFLMGSPEGEGAFDNERPRHRVTVSPFYIDKYEVTNAEYRAFVGWTLADGR
NNPLYSDFGGPDHPVVHVSWYDAQAYCRWLGKKTGKGYRLPTEAEWEYAARGGDGRPYPWGDDLPPELAN
YAGNDGRGSTAPVGSFPPNPFGLYDMAGNVWEWTADWYDPPYPGAPADGPVGPENGGQRVLRGGSWATPP
DHLRSAYRNFFPPDARWQFVGFRLARDL
>gnl|CDD|440875 COG1263, PtsG1, Phosphotransferase system IIC components, glucose/maltose/N-acetylglucosamine-specific [Carbohydrate transport and metabolism]
AKKKKNPLFRFLQKIGGIFMPPIPVLPAAGLLLGLGALLTNPGLLGEGSFLSGTYQILNAAGDAVFYFLP
LLFAIGAAKGFGGNPALAAVIGYLLVHPTLLNAYAVAGGYISFLGIPTLIGYQGGVFPGILAGWLAAYLE
KFLKKKLPDALGFFFVPILTLLIMVPLALLVIGPIWPPIGNGIAAGLGWIYGLAGAIGGFIYGFLYRLLV
PTGLHHGLNPIFWFLLGGTGDDGLFPILAAAMFGQPGAALAVYLKAKPNKKVKGLAISAALTAFLTGITE
PAEFGFNLVAPKLFIAHAIGGGLGGAIAGLLGVKAFSFGVGGLIDFPSILNPGATNLLLYLIGLVIAFVY
YFVFTFLIGREDEEEEEKLATKADAKKEEAEAAAAALGGGGGLLLLEADITVLLLTLVDVVIVVVKDVVK
LAAAGAVVVGVGGVGAVGGVGGGGVVIVIVIIILVVVLEGLGE
>gnl|CDD|440876 COG1264, PtsG2, Phosphotransferase system IIB components [Carbohydrate transport and metabolism]
KELAKDILEALGGKENIVSVDHCATRLRVTVKDPSKVDEAALKKLGVKGVVKNGGQVQVIIGPGVDKVAD
EIEKLL
>gnl|CDD|440877 COG1266, YdiL, Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, chaperones]
LLWLLLFLLVVVILAPIAEELLFRGYLLGRLRRRFGPWLAILLSSLLFGLLHLPNLLGFLPAFLLGLVLG
LLYLRTGSLWVPILLHALNNLLALLLL
>gnl|CDD|440878 COG1267, PgpA, Phosphatidylglycerophosphatase A [Lipid transport and metabolism]. Phosphatidylglycerophosphatase A is part of the Pathway/BioSystem: Phospholipid biosynthesis
LRNPAHLLATGFGSGLSPKAPGTWGSLAALPLYLLLLGLGLWLLLLLLLLLFLIGIWACGKTERDLGVHD
PGEIVIDEVVGMWITLLFLPAGWLWLLAAFVLFRLFDILKPWPIRWLDRRLKGGLGIMLDDVLAGIYALL
VLALLAWL
>gnl|CDD|440879 COG1268, BioY, Biotin transporter BioY [Coenzyme transport and metabolism]
SRMKTRDLALVALFAALLAVLAQISIPLPFGPVPITLQTLAVLLAGALLGPRRGALSVLLYLLLGALGLP
VFAGGRGGLGYLLGPTGGYLLGFILAAFVIGLLAERGWDRSFLRLLLAMLAGLLVIYALGVLWLALVAGL
SLAKALAAGVLPFLPGDLIKAVLAALIAPALRR
>gnl|CDD|440880 COG1269, NtpI, Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion]. Archaeal/vacuolar-type H+-ATPase subunit I/STV1 is part of the Pathway/BioSystem: A/V-type ATP synthase
MAIVKMKKVSLIGLKSDKDEVLEALQELGVVHIEDLDEELEEEEGLKPGEPDEELEELSELLSRLRSALS
ILGPYLEEKGGLKPKKEVTLEELEEELEEELEEIEEEVNELEERLEELEEELEELEELIEALEPWGDLDI
DLEELRGTKYLSVRVGTVPKENLEKLKKALEILADYVEVVSSDKEDEVYVVVIVPKEDEEEVEEVLRSLG
FERLEIPELEGTPSEALEELEEEIEELEKEIEELEKELEELAEKYREDLLALYEYLEIEKEKAEAPLKLA
TTENLFVLEGWVPEEEVEELEKALEKATGGRVYVEEEDPEEDDEPPTLLKNPKFVKPFELLVEMYGLPKY
GEIDPTPFFALFFPLFFGMMFGDAGYGLLLLLAGLLLLKKFLSKGLKKLGKLLLYLGISTIIFGLLYGSF
FGFELLAGLLPALWLDPLEDPNTMLVLSLAIGVIHLLLGLILGIYNLLKRGDYKDALLDQGGWLLLLLGL
LLLVLGLVLGGPLPLTTIGLVLLIIGLVLLLLFGGRSGKNIGGRLGEGLFGLYEITGYLSDVLSYIRLFA
LGLASAGLAMVVNTLAGMVGGGPIVGIIGGILILILGHLLNIALEGLGAFVHSLRLQYVEFFGKFYEGGG
KPFKPFKLKRKYTKI
>gnl|CDD|440881 COG1270, CbiB, Cobalamin biosynthesis protein CobD/CbiB [Coenzyme transport and metabolism]. Cobalamin biosynthesis protein CobD/CbiB is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MTLMTLLLLLLALLLDLLLGDPRRRPHPVVLFGRLISRLERRLNRPGRSPAQRRLAGALAVLLLVLPVLL
LAWLLLRLAYRLHPWLGLLLEALLLYLALAGRSLADHARAVARALEAGDLEAARRALSMIVGRDTDNLDE
AGIARAAVESVAENTSDGVVAPLFWFALGGLPGALAYKAVNTLDSMWGYKNERYRYFGWAAARLDDLLNW
IPARLTALLIALAAGLGSPRRALRIWRRDARKHPSPNAGWPEAAMAGALGVRLGGPNVYGGVVVERPWLG
DGRRPPTAEDIRRALRLLRRAALLWLLLAALLALLLAL
>gnl|CDD|440882 COG1271, AppC, Cytochrome bd-type quinol oxidase, subunit 1 [Energy production and conversion]
MDALLLSRLQFAFTISFHILFVPLTIGLALLLAIMETLWLRTGDEVYLRLTRFWGKLFAINFAVGVVTGI
VMEFQFGTNWSGFSRFVGDVFGAPLAYEGLTAFFLEATFLGIMLFGWDRVSPKLHLLATWLVALGTNLSA
FWILAANSWMQTPVGFEIVDGRAELTDFWAVIFNPSFPYRFVHMVLAAYLTGAFFVAGVSAWYLLRGRHV
EFARKSLKIALVFALIAAPLQAVSGDLSGLNVAEHQPAKLAAMEGLWETEEGAPLSLFGIPDEEAEENRY
AIEIPGLLSLLATHDFDGEVPGLNDFPPDDRPPVAIVFWSFRIMVGLGFLMLLLALLGLWLRRRGRLEES
RWLLRLAVLMGPLPFIAIEAGWIVTEVGRQPWIVYGLLRTADAVSPVSAGEVLFSLILFTLVYLLLFVAE
VYLLRRLIRKGPEEEEPEPAPD
>gnl|CDD|440883 COG1272, YqfA, Predicted membrane channel-forming protein YqfA, hemolysin III family [Intracellular trafficking, secretion, and vesicular transport]
MSTSAPYSRVEEIANAITHGIGALLAIAGLVVLIVLAALSGDAWAIVSFSIYGASLILLYLASTLYHSLP
SPRAKRVLRRLDHSAIYLLIAGTYTPFALIALRGPWGWTLLGIVWGLALLGIVLKLFFPGRPRWLSTLLY
LAMGWLAVFAIPPLLAALPPAGLWLLLAGGLLYTVGAVFYALKRLPGFHEIWHLFVLAGSACHFVAILLY
VLP
>gnl|CDD|440884 COG1273, YkoV, Non-homologous end joining protein Ku, dsDNA break repair [Replication, recombination and repair]
MMRAIWKGAISFGLVNIPVKLYSATESHDISFHQLHRKDGGRIRYKRVCEVTGKEVEYEDIVKGYEYEKG
RYVVLEDEELEALPPESTKTIDIEQFVPADEIDPIYFDKPYYLAPDKGGEKAYALLREALRKTGKVAIAR
VVLRGRERLAALRPRGDGLVLETLRYPDEVRDADEFPDLPEDVKVDPKELDMAKQLIESLTGDFDPEKYK
DEYREALLELIEAKIEGKEVVAPPEEEPEGANVIDLMEALKASLEAAKKKRAAAKAKKAPAKKAARKKA
>gnl|CDD|440885 COG1274, PepCK, Phosphoenolpyruvate carboxykinase, GTP-dependent [Energy production and conversion]. Phosphoenolpyruvate carboxykinase, GTP-dependent is part of the Pathway/BioSystem: Gluconeogenesis
MTAATIPGLAPAPTTHEKLLAWVAEVAALTQPDRVVWCDGSQEEYDRLCDELVEAGTFIRLNPEKRPNSF
LARSDPSDVARVEDRTFICSEKEEDAGPTNNWMDPAEMKATLTGLFDGCMRGRTMYVIPFSMGPLGSPIS
KIGVEITDSPYVVVSMRIMTRMGTAVLDVLGADGEFVPCLHSVGAPLAPGQKDVPWPCNDTKYIVHFPET
REIWSYGSGYGGNALLGKKCFALRIASVMARDEGWLAEHMLILKLTSPEGKKYYVAAAFPSACGKTNLAM
LIPTIPGWKVETIGDDIAWMRPGEDGRLYAINPEAGFFGVAPGTSEKTNPNAMATLKGNTIFTNVALTDD
GDVWWEGMTDEPPAHLIDWQGNDWTPDSGRPAAHPNSRFTVPASQCPSIAPEWEDPAGVPISAILFGGRR
ATTVPLVTEARDWEHGVFLGATMGSETTAAAEGAVGVVRRDPFAMLPFCGYNMGDYFQHWLDMGRKLGPD
KLPKIFYVNWFRKDEDGKFLWPGFGENSRVLKWIVERVEGKAEAVETPIGWVPRYEDLDLDGLDFSEEDF
EELLAVDPEEWKAELPLIEELFAKFGDRLPAELRDELEALRSRLA
>gnl|CDD|440886 COG1275, TehA, Tellurite resistance protein TehA and related permeases [Defense mechanisms]
MSTAPRSRLRNLPPAWFALVMGTGGLGLAWRLAAALLPGPAAIAEVLLALAALLFLVLLLLYLLKWLRYP
AAVRADLRHPVRGSFFPTIPMALLLLGTGLLPLAPALALVLWLLGVALHLALTVYFPYRLFTGEKFEIEH
ITPAWFIPVVGNIVVAVAGALLGPLLELSYAFFGVGLFLYLVLLPLVLYRLIFHKPLPEALRPTLWILLA
PPAVGLLAYLALGGGPLDGFALILWGFGLWWLLLLLLLTPRLLRLPFSPSWWAFTFPLAAYATATLRLAE
ATGLPFLAVLALALLVLATLVWLYVLVRTLRALARGKLFVPEP
>gnl|CDD|440887 COG1276, PcoD, Putative copper export protein [Inorganic ion transport and metabolism]
AALLAVLTQTSFGRAWLVRLLLAALLALLLLLAVRSRAGAALLLLLALLALLTLALTGHAAASEGHALAV
LADALHLLAAAVWVGGLLALLLLLRRLRRGAALAAALRRFSRLALVAVALLALSGVVNAWLRLGSLSALL
TTPYGRLLLAKLALVAVLLALAALNRRRLVPRLEAGPRALRRLRRSIRAELVLGLLVLGLAAALATTPPP
VAAAAAAALTGPTLPPPPPLSALLTTWPLDLLLLLAALAAALVLALLLVALRRRGDGWPPVRTVALLAGL
LA
>gnl|CDD|440888 COG1277, NosY, ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones]
ILAIARKEFRDLFRSPRFYVLLALFLLLALLLAYLGGAASGFLGLGLALLASLFSLLSLLLPLLAPALGM
DAISGERESGTLELLLTLPISRWEIVLGKFLGALLVLLLALLITFLLALLLGLLLFGSPPPDLGAILGFY
LGLLLLGLAFLAIGLFISALTRNQIVAAILAIALWLLLVILLAWIVLFLALAYLRFKRRDL
>gnl|CDD|440889 COG1278, CspC, Cold shock protein, CspA family [Transcription]
MATGTVKWFNAEKGFGFITPDDGGEDVFVHISALQRSGFRTLREGQRVEFEVEQGDKGPQAVNVRVL
>gnl|CDD|440890 COG1279, ArgO, Arginine exporter protein ArgO [Amino acid transport and metabolism]
MLSAFLQGFLLGLSLIVAIGAQNAFVLRQGLRREHVLPVALICALSDALLIALGVFGVGALLAASPWLLT
VLRWGGAAFLLWYGLRALRRALRGGAALDAAEGAALSLRKAILTALAVTLLNPHVYLDTVVLLGSIAAQY
GGDERWAFALGAILASFLWFFGLGYGARLLAPLFARPRAWRVLDLLIGLVMWAIALKLLLGLLA
>gnl|CDD|440891 COG1280, RhtB, Threonine/homoserine/homoserine lactone efflux protein [Amino acid transport and metabolism]
MSLELLLAFLLAALVLALTPGPDNLLVLSRGLRRGRRAGLAAALGIALGDLVHILLAALGLAALLAASPL
LFTVLKLAGAAYLLYLGWKLLRSAGRPLAAEAAAAASARRLFRQGFLLNLLNPKAILFFLAFLPQFVDPG
APLLLQLLLLGATFLLVSLLWLLLYALLASRLRRRLRSPRALRWLNRVAGLLLIGFGLRLALSRR
>gnl|CDD|440892 COG1281, HslO, Redox-regulated molecular chaperone, HSP33 family [Posttranslational modification, protein turnover, chaperones]
DDYLVRFLFEDGDVRGEAVRLTETVQEALARHDYPPPVTALLGEALAAAALLGATLKFDGRLTLQIQGDG
PLGLLVADADSDGEVRGYARNPEVELPLNEKGKLDVGELVGNGYLAVTIDPGLGEPYQGIVPLVGGELAE
DLEYYFAQSEQLPTRVWLGVLVDEDGWRAGGLLLQLLPGADEEAIDDEDAWERAVALAATLTISELLDPG
LTPEELLYRLFHEEDVRVFEPQPVRFRCSCSRERVENALKSLGREELEDMLEEDGGIEVTCEFCNEKYRF
DPEELEELFAE
>gnl|CDD|440893 COG1282, PntB, NAD/NADP transhydrogenase beta subunit [Energy production and conversion]
MSNTLITLAYLVAAVLFILGLKGLSSPETARRGNLLGAVGMLIAVVATLLLPGIVNYGLILAAIAIGGAI
GAVLARKVEMTAMPQLVALFNGFGGLAAALVAAAELLEPGALAGALPAIHLIEIVLGVLIGAVTFTGSLI
AFGKLQGLISGKPITFPGQHLLNLLLLLAIVALGVLFVVSPGSLLLLLLLTVLALLLGVLLVLPIGGADM
PVVISLLNSYSGLAAAAAGFVLGNDLLIIAGALVGASGAILTYIMCKAMNRSLINVLFGGFGGGGAAAAG
AAEQGEVKEISAEDAAILLAYASSVIIVPGYGMAVAQAQHAVRELADLLEERGVEVKFAIHPVAGRMPGH
MNVLLAEANVPYDQLLEMDEINPEFAQTDVALVIGANDVVNPAARTDPGSPIYGMPILEVDKAKTVIVIK
RSMGPGYAGVENPLFYKDNTRMLFGDAKKSVEELVKAL
>gnl|CDD|440894 COG1283, NptA, Na+/phosphate symporter [Inorganic ion transport and metabolism]
MSILLILLNLLGGLALFLFGMKMMSDGLQRAAGDRLRRILARLTSNRLKGVLAGALVTALLQSSSATTVM
VVGFVNAGLMTLAQALGVILGANIGTTLTAQLIAFDLSALAPPLIAIGVILFLFGKRRRLRQIGRILIGF
GLLFLGLDLMSEAMEPLRDSPAFRALLASLSGNPLLGVLVGALLTALVQSSSATVGLLLALAAQGLIPLE
AALALVLGANIGTTITALLASIGANVAARRAALAHLLFNLIGVLIFLPLLPPFAALVAWLSPDPARQIAN
FHTLFNLLNALLFLPFIGPLARLLERLIPDKEEEEEPARPKYLDPSLLETPSLALAQARREVLRMGDLVE
EMLRRALELLREGDEKLAEEIRKLEDAVDRLEREIKLYLAKLSRESLSEEESRRLAELLHIANDLERIGD
IIENLAELAEKKIEKGLEFSEEGLEELRELHERVLENLRLALSALASGDLELARKLLEEKEEIRRLEREL
RKRHLERLREGRCSIETGSLHLDLLRDLERINDHLANIAYPVLEEAGELL
>gnl|CDD|440895 COG1284, YitT, Uncharacterized membrane-anchored protein YitT, contains DUF161 and DUF2179 domains [Function unknown]
MKKKIKLKKKLKDYLLIILGALLYAIGLNFFLIPNNLADGGVTGIAIILSYLFGLPVGILLLLLNIPLFI
LGYKFLGKRFGIKTIYGVLLLSLFLDLLPPIIPPLTDDPLLAAIFGGVLLGIGLGLVFRGGGSTGGTDII
AMILNKKTGISIGKILLIIDAIIILLAGFVFGWETALYSLIALFITSKVIDFVIEGFNQKKAVFIISDKP
EEIAEAILEELGRGVTILKGEGGYTGEEKKVLYTVVSRRELAKLKRIVKEIDPNAFVIVSDVSEVLGEGF
KKRKI
>gnl|CDD|440896 COG1285, SapB, Magnesium uptake protein YhiD/SapB, involved in acid resistance [Inorganic ion transport and metabolism]
DTMDWLEILLRLLLALLLGGLIGLERELRGKPAGLRTHILVALGAALFVLLSLYLFEDYLGGVRADPSRV
AAQVVSGIGFLGAGVILKEGGSVRGLTTAATIWVTAAIGLAVGAGLYLLAILATLLVLLVLTLLRPLERR
IPRRPRRRTLRVTEDDEGDLRELLELLEENGLRIRSLEIEDDEDEIAPEKDLEELLSE
>gnl|CDD|440897 COG1286, CvpA, Colicin V production accessory protein CvpA, regulator of purF expression and biofilm formation [Nucleotide transport and metabolism, Cell wall/membrane/envelope biogenesis]
MTWIDIIILAILLLSALLGLRRGFVREVLSLAGWIAAFFVALRFYPPLAPLLTLYIPDPALRNAVAFALL
FIVVLIVGSLLGSLLSKLVKASGLGGLDRLLGAVFGLLRGVLIVVVLLLLLALTPLPQQPWWQESRLAPL
LESLAPWLSPLLPDDLAELIE
>gnl|CDD|440898 COG1287, Stt3, Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, protein turnover, chaperones]
MSEKTSVLDKLKRLLHLPALLLILALALWIRLLPYDNVFRDGGVYLGGNDPWYHLRQIEYILANGPSTLP
FDPLTWYPWGRDIGQFGPLFDQLIALLALILGLGSPSQSSVYTVAAWFPPIFGALTVIPVYLLGRRLGGR
KAGLLAALLLALSPGQLSRSLLGFADHHVAELFFSTLAVLFLVLALKRAKREKRDLEALKRPLLYAVLAG
VALGLYLLTWGGYVLFVGILALFALLQLLLDLLRGRSPEYLAIVGAVSFAVAALLVLPFIPRLGFSGTGL
SLLQPLLALALAAGTVFLAWLARELERRDLPRLYYPAALVGLVAAGLALLAVLLPRVLAALIPGLRRFFG
ASALAATIAEAQPLTLSDLFSSFGIAFFLALIGLLLLLYRPLRERRPELLFLLVWALFSIYAAFTQVRFL
YYLAVAVAILAAIGLGELLDRLDLDKKKREAKKNINGVKILAVALIVLLLLIPLSASIALSGGSSFGPGG
INDDWIDALEWLKENTPEPGVYPDGAYGVLSWWDYGHWITVLGERIPVANPFQQGITGAANFLLAPSESE
AEAILDALHADGLGVRYVIVDDEMATGKFYAMATWAGDPSDYYQTLYPPSGVTVYTERYYNTMLARLHLF
DGSGDEAAAVSVVTVPGYVESGSSPAEAGVVTQDAATALALGAGGNAVAALLSSIYVTSSTGVSSLAIGG
DVTSATSTSGGAVVGLPGDTVTAEVTTSYSVPYYTPGGYSGVYTSVTSTVSVPYVVLTVTVTSNVIVLGY
GGLG
>gnl|CDD|440899 COG1288, YfcC, Predicted membrane transporter YfcC, affects glyoxylate shunt [General function prediction only]
METKKKKKKKFKFPHAYVILFIIIVLAAILTWIIPAGEYDRVEDGRTVVVPGSYHYVEQNPQGLFDIFTA
PIKGLVEAADIIFFILIIGGAFGVINKTGAIDAGIGALVRKLKGKEKLLIPVLMLLFALGGTTFGMAEET
IAFYPILVPLAIALGYDAITGVAIIFLGAGIGFAASTINPFTVGIAQGIAGLPLFSGIGLRLVIFVVFTL
IAIIYVMRYAKKVKKDPEKSLVYDDDEEFRKRFLKDDDEDPEFTGRHKLVLLVFALGFVIMIYGVLKLGW
YFPEMAALFLVMGIVAGIIGGLSENKIAEAFVKGAKDLLGGALIIGLARGILVIMEDGKILDTILYGLSN
LLSGLPPVLFAIGMFIVQSLLNFFVPSGSGQAALTMPIMAPLADLVGVTRQTAVLAFQFGDGLTNLITPT
SGVLMATLAIAGVPYDKWLKFVWPLFLILFLLAIVFLIIAVLIG
>gnl|CDD|440900 COG1289, YccC, Uncharacterized membrane protein YccC [Function unknown]
PRQALAEAYRALADLRALADALLRALLRNLRRLKRLRANLSPDSPAFRHALRLALAALLALLIALLLGLP
HPYWALLTVLIVLQPSYGATLSRALQRILGTLLGALAGLLLLALFPQPLLLLLALALVLGLCFFALLTRS
YAFALAGITAAVVLLFALLGPGVFDVALARVLDTLIGILIALLVSYLLWPRWARRRLRARLARALRANAR
YLRALLSQGDPADDLALRAARRRLAAALAALEALLQRALSEPPRGRRRELRALLALNHRLLSLLSALGAR
>gnl|CDD|440901 COG1290, QcrB/PetB, Cytochrome b subunit of the bc complex [Energy production and conversion]
MSTTKKASGLADWLDERLPLASLVREHLEYPFPKNWNFSYWFGELALYSFVIQILTGIFLTMYYKPSASE
AFASVEYIMRDVPGGWLIRYMHHWGASLFFAAVYLHMFRGFFYGAYKKPRELNWIIGVLLLLLTMAEAFT
GYSLPWDQLSYWGARVITGLFGAIPVIGTWLVTWLFGGEFPGDATLNRFFALHVLLLPALLLALVVLHLW
LLHRHGHNNPPGPERKKTEKVDGVPFHPYYTVKDGFGFFVFLGVFALLAFFFPINPPPNYGPANPLATPA
HIQPDWYFLPFYGILRAIPGSAKLGGVIAMGLAILVLFLLPFLDRSPVRSPRYRPVRTALGVAFIVFFIV
LTILGANPPIATLLGSINTVTYFAFFLIVLPILAFIEKTKPLP
>gnl|CDD|440902 COG1291, MotA, Flagellar motor component MotA [Cell motility]
MATIIGLVVGLGAVLGGFLLEGGSLGALIQPPSLLIVFGGTLGAVLISFPLKVLKAALKALKKAFKGKKA
DYEELIELLVELAEKARKEGLLALESDIEEIDDPFLRDGLRLVVDGTDPEEIRELLETEIEAMEERHEAG
AKVFEAMGDYAPAFGIIGTVLGLIQMLGNLDDPSALGPGIAVALVTTFYGVLLANLFFLPIANKLKRRSE
EEVLLREMIIEGLLAIQAGENPRIIEEKLRSFLPPSERPSFEEEELKG
>gnl|CDD|440903 COG1292, BetT, Choline-glycine betaine transporter [Cell wall/membrane/envelope biogenesis]
MSDKNKEKFKKKIDPPVFIPSALLILAFVLWGLLFPEAAGAVLNAAFSWITTNFGWFYLLLVLLFVVFCL
YLAFSKYGKIRLGGDDAKPEFSTFSWFAMLFSAGMGIGLVFWGVAEPLYHFLSPPPGVEPGSPEAARWAM
AYTFFHWGLHAWAIYALVGLALAYFAYRRGLPLTISSALYPLLGDRIYGPIGKVIDILAVFATVFGVATS
LGLGALQINAGLNYLFGIPNSLTVQIIIIAVITALFTISAVSGLDKGIKRLSNLNMVLALLLLLFVLIVG
PTLFILNLFVQSLGDYLQNFVPMSLWTDAYGDTGWLGGWTVFYWAWWIAWAPFVGLFIARISRGRTIREF
VLGVLLVPTLFTFLWFSVFGGTAIHLELNGGGDLAEAVAAGVEAALFALLEQLPLGTILSVLAIILVIIF
FVTSADSGSLVLAMLTSGGDEEPPRWQRIFWGVLIGLVAAVLLLAGGLSALQTASIITALPFSFVLLLMC
VSLVKALREDPRRLRSAEAEAA
>gnl|CDD|440904 COG1293, RqcH, Ribosome quality control (RQC) protein RqcH, Rqc2/NEMF/Tae2 family, contains fibronectin-(FbpA) and RNA- (NFACT) binding domains [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones]
MAFDGIDLAALVNELREKLLGGRIDKIYQPDKDELLLKLRTPGKRYKLLISAHPGYARIHLTEEPPENPD
TPPMFCMLLRKHLEGGRITSIEQIGFDRIVEFDFEKRDELGDLVEKTLIVELMGKHSNIILVDEEGKIID
ALKRVSPDQSRVRTVLPGEPYEPPPSQDKLNPLELSEEEFAELLSESDGDLVRTLATNFLGLSPLLAEEI
CYRAGLDKDTPTDELSEEDLEALYEALQELLEELENGEFKPTIYYEEDGKPVDFSPFPLTHYEGLEKESF
DSFSEALDEYYSEKAERDRVKQLAEDLRKKVENELEKLERKLEKQEEELEEAEKAEKYREKGELLTANLY
QVEKGMKEVTLPNYYEEVTIPLDPRLSPSENAQRYYKKYKKLKRKKEGAEEQLEETEEELEYLESVLAQL
EQAEDEDLEEIREELIEQGYLKKKKKKKKKKKKWYEKPRWFISSDGFLILVGRNNRQNDELTKKYARKND
IWFHAKDIPGSHVIIKTEGKEPPEETLEEAAQLAAYYSKARKSGSVPVDYTEPKQVSKPKGAKPGFVIYG
NRKTLYVTPDEEVEKLAI
>gnl|CDD|440905 COG1294, AppB, Cytochrome bd-type quinol oxidase, subunit 2 [Energy production and conversion]
LPLIWFLLIGVLLIGYVILDGFDLGVGILLPFAGKDDEERRVMINSIGPVWDGNEVWLVLGGGALFAAFP
LAYATLFSGLYLPLLLILLALIFRGVAFEFRSKADSPRWRRLWDWAFFIGSLLPAFLLGVALGNLLQGVP
FDADGDYTGGFFDLLNPFALLGGLASVALYLLLGATFLALKTEGELQERARRLARRLALATLVLFALVSL
WTPLAAPALFANWFSYPWLWPLPLLAVLAALLAVRALRRGREGLAFLASALLIALAVAGLGISLFPYLLP
SSDPASSLTIWDAASSPYTLKIMLVVALIFLPIVLAYTAWVYRVFRGKVTAEE
>gnl|CDD|440906 COG1295, BrkB, Uncharacterized membrane protein, BrkB/YihY/UPF0761 family (not an RNase) [Function unknown]
MSKLPRLPRLRRLLRLLKRAVRRFLEDDGTLLAAALAYYTLLSLFPLLLLLFALLGLFGDPALQEQLLDL
LSNLLPGEAADLIQDTLEQLLSNGRGGLLSIGLLVLLWSASGLFSALERALNRIWGVKEKRSFLRRRLLS
LLLTLLLGLLLLLSLALSVLGPALLSFLGDLLLGEPLLGLLRLLRWLLPLLLLVLLFALLYRFLPNRRVR
WRDALPGALLAALLWELASYLFSLYVSNFSSYNATYGSLGAVIILLLWLYLSALILLLGAELNAVLERRR
GLRAEPRAA
>gnl|CDD|440907 COG1296, AzlC, Predicted branched-chain amino acid permease (azaleucine resistance) [Amino acid transport and metabolism]
FRAGLRDALPILLGYIPFGLAFGVLAVQAGLSVWEAVLMSLLVFAGASQFAAVGLLAAGAPLLAIVLTTL
LVNLRHLLYGASLAPYLRGLPLRKRLLLAFLLTDESFALAMARFERGELRRAYFLGLGLTLYLSWVLGTL
LGALLGSALPDPLAWGLDFALPALFLALLVPQLKGRATLVAALVAAVVALLAALLLPGGLGILVAALAGA
AAGALLERLRRRRAA
>gnl|CDD|440908 COG1297, OPT, Predicted oligopeptide transporter, OPT family [General function prediction only]
MSPGPEYKPYVPAGKNLPELTLRAVILGALLGVVFTAANAYLGLKVGLTFSASIPAAVISMAVLRALKRG
STILENNIVQTIASAAGSLAAGVIFTLPALLMLGYWQGFPYWQTFLWALLGGILGVLFAIPLRRALIVDE
DLPFPEGTAAAEVLKAGEKGGEGGSGAKLLLLGGLIAALYKLLRDGLGLIPESVSLWFKIGLAKLTFGLD
LSLALLGVGYLVGLRVGLSMLLGGLLAWGVLIPLLSAFGGIALPAGVSLADAASAIWSSYVRWIGAGAMA
VAGLWTLIKLLKPIVRGFKSSLAALKKKKGGGAVPRTERDLPMKWVLIGILALLVLLVVLFQYFFAWGIP
LLGALLAVVLGFLFAAVAGYMAGLVGSSNNPVSGMGIATQLIAALLLLALGLTGPGGVAAALMVAAVVCG
AAAIAGDNLQDLKTGYLVGATPWKQQVAQLIGVIVGALVIGPVLNLLNPAYGFGSEALPAPQATLMAAVA
EGIFGGPLPWTLILIGAVLGVVLILLDELLPRKRRFRLPPLAVGLGIYLPLSLSLPIFIGGLIAWLVDRR
AKEALAEAAERRGVLLASGLIAGEALMGVLLAILIVLGGPLALPEGFGSLAQWLGLVVFALLCAYLYRRA
LKA
>gnl|CDD|440909 COG1298, FlhA, Flagellar biosynthesis protein FlhA [Cell motility]
LAVPLGVIAILAMMILPLPPFLLDLLLAFNIALSLLILLVALYIKRPLDFSVFPTLLLITTLFRLSLNVA
STRLILLEGHEGTDAAGKVIEAFGEFVVGGNYVVGLVVFLILVIINFVVITKGAGRIAEVAARFTLDAMP
GKQMAIDADLNAGLIDEEEARRRREEIQREADFYGAMDGASKFVRGDAIAGILITLINIIGGLIIGVLQH
GMSFGEAAQTYTLLTIGDGLVSQIPALLISTAAGIIVTRAGSEGDLGEQLSGQLFANPKALYIAAGVLGL
LGLIPGMPHLPFLLLAALLGGLAYRLKKRQKEEEAEEAAAAAEAEAAAEPAEESVDDLLPVDPLELELGY
GLIPLVDESQGGDLLDRIKGIRRQLAQELGFVVPPVRIRDNLQLKPNEYRIKIKGVEVARGELRPDRLLA
INPGGVTGELPGIPTKEPAFGLPAVWIDPEQREEAELLGYTVVDPSTVIATHLSEVIKRHAAELLGRQEV
QQLLDRLKKEYPKLVEELVPKLLSLGELQKVLQNLLRERVSIRDLRTILETLADYAPRTKDPDLLTEHVR
QALGRQIVQQYAGPDGELPVITLDPELEQLLLESLQQTEQGSYLALDPGLAQRLLQSLAEAVEKLEAQGE
PPVLLVSPQLRPYLRRLLERFLPDLPVLSYNEIPPDVEIESVGTVG
>gnl|CDD|440910 COG1299, FrwC, Phosphotransferase system, fructose-specific IIC component [Carbohydrate transport and metabolism]
AAASKKKVIVVATTTAGATAAAAAAAAAAAAAAAAGGVIVVVVGGGGGGGGNLLTTEEEAAAAAIIIAAA
DDVEDRFFGKKGKVVVVVAGGAAKKELLIIAAAAAAAAVYAAGGAAAAAESEEKKKSGGSGIYKHLMTGV
SYMLPFVVAGGILIALSFLFGIYAFDPGDVSEGTLAAALFQIGGAAFGLMVPVLAGYIAYSIADRPGLAP
GFIGGLLANNIGAGFLGGIIAGFLAGYVVLWLKKKIKLPKSLEGLKPILIIPLLGTLITGLLMIYVIGPP
IAALNTALTNWLNSMSGSNAVLLGAILGAMMAFDMGGPVNKAAYAFGTGLLASGIYAPMAAVMAAGMVPP
LGLALATLLFKKKFTEEEREAGKAAFILGLSFITEGAIPFAAADPLRVIPSNMIGSAVAGALSMLFGVTL
PAPHGGIFVLPLVSNPLLYLLAIAIGTVVTALLLGLLKKPVEKKEEAAE
>gnl|CDD|440911 COG1300, SpoIIM, Stage II sporulation protein SpoIIM, component of the engulfment complex [Cell cycle control, cell division, chromosome partitioning]
DREAAWARLEWLKRLEELRRLRRLSGAEPDELALLYRRAATDLSYARTRYPDSALVAYLNQLVARAHQAI
YGTRRELWRRLLRFFLKEFPAALRRNRRLYLFAALLFLLGALFGAILVASDPEFQRSLLGPEFLEQLEEG
YSEGSAASMFGQIFTNNIKVALLAFALGILLGIPTIFVLFFNGLVLGAVAGFLVAKGLLDLFFAFILPHG
ILELPAIIIAGAAGLRLGWALLFPGTRSRLDALKEAGRRYVKLVLGLVPLLLVAALIEGFVTPSLLPLWL
KILIGALALALFLAYFLLYGRRA
>gnl|CDD|440912 COG1301, GltP, Na+/H+-dicarboxylate symporter [Energy production and conversion]
FKLSLTLQILIALVLGILLGLLLPELVAAVLKPLGDIFINLLKMIVVPLVFFSIVVGIASLGDLKKLGRI
GGKTLLYFLVTTTIALVIGLVVANLFQPGAGLNLDLADAAAAEAAEAPSLLDFLLNIIPSNIFEAFAEGN
MLQIIFFAILFGIALAALGEKGKPLLDFFESLSEVMFKIVGWVMKLAPIGVFALIAATVAKYGLDALGSL
GKLVLTVYLALLLHLFVVLPLILRLLTGLSPLKFLRAIRPALLLAFSTSSSEATLPVTMEKAEEKLGVSK
SVASFVLPLGATINMDGTAIYQAVAALFIAQAYGIDLSLGQQLTIVLTAVLASIGAAGVPGAGLVMLAAV
LSAVGLPLEGIALILGIDRILDMARTAVNVTGDAVATVVVAKWEGELDREKLNAAL
>gnl|CDD|440913 COG1302, YloU, Uncharacterized conserved protein YloU, alkaline shock protein (Asp23) family [Function unknown]
MAEEELGKITIADEVIAKIAGIAALEVYGVVGMAGGFADGIAELLGRKNLTKGVKVEVGEDQVAIDLYVV
VEYGVNIPEVAENVQENVKYAVEKMTGLEVVEVNVHVQGVRFPEEEEE
>gnl|CDD|440914 COG1303, TRM56, tRNA C56-2-O'-methylase, SpoU family [Translation, ribosomal structure and biogenesis]
EIVVLRLGHRPERDKRITTHVALTARAFGADGIILAGNDEKVEESVEDVVDRWGGPFEVEYGVSWKKVIR
DWKEEGGKVVHLTMYGEPVDDVIDEIREREKDLLVVVGAEKVPGEVYELADYNVAVGNQPHSEVAALAIF
LDRLFEGRELDREFEDAKLRVIPSERGKKVVEKE
>gnl|CDD|440915 COG1304, LldD, FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]. FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRL
AAPFLIAPMGGGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDD
LLRRAEAAGADALVLTVDTPVLGRRERDLREGFSQPPRLTPRNLLEAATHPRWALGLASLAAWLDTNFDP
SLTWDDIAWLRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGR
IPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAEL
RRALLVL
>gnl|CDD|440916 COG1305, YebA, Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones]
LAGLVLAALLAALSGPLAPAPTGLLVTAGAGRGGGVASVVPGGGTELLAGPGELLSASYDPELRALAAEL
TGGATTPYEKARALYDWVRDNIRYDPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVSGY
LPGEPPPGGGRADDAHAWVEVYLPGAGWVPFDPT
>gnl|CDD|440917 COG1306, COG1306, Predicted glycosyl hydrolase, alpha amylase family [General function prediction only]
VVVFLPLGARTARGGTITLPRTLTVAALAALAAAGVAGDVEAVAAAAGEASDVVESAAAAVRSRARARAA
NRSSSGLTVSAPPPAVRGIYLTAYSAGSPSRRDKLLDLIDETELNAVVIDIKDDDGNVTYDSEVPLAREI
GAVRKYIKDPRALVKTLHENGIYVIARIVVFKDPVLAEARPDLAVKTKDGGVWRDGKGLAWVNPYNKEVW
DYNIDIAKEAAELGFDEIQFDYVRFPEGGGNKKLVYSPPGNGESRVEAITDFLAYAREELRPYGVFVSAD
VFGYVATSPGDMGIGQDLEKIAENVDYISPMIYPSHYGPGEFGIANPDLEPYEIVYNSLKDARERLETLG
SPAKVRPWLQDFTASWLGYQPYGPAEVRAQIRALYDAGIDEWLLWNAGNRYTEGALY
>gnl|CDD|440918 COG1307, DegV, Fatty acid-binding protein DegV (function unknown) [Lipid transport and metabolism]
MKIAIVTDSTADLPEELLEKYGIEVVPLTVIIDGEEYRDGVDITPEEFYEKLREGKELPKTSQPSPGEFL
EAFEELLEEYDEIISIHLSSGLSGTYQSARLAAEELEDFKVHVIDSKSASMGLGLLVLEAARLAEEGKSL
EEIVERLEELREKTRTYFVVDTLEYLRKGGRISKAAALLGSLLNIKPILTVEDGKLVPVEKVRGRKKALK
RLVELAEERAKDLKPVRVAISHAGAPEEAEELKEELEERFPVKEILISEIGPVIGAHTGPGALGVAFL
>gnl|CDD|440919 COG1308, EGD2, Transcription factor homologous to NACalpha-BTF3 [Transcription]
MFGGMNPRKMKQMMKQMGIKVEEIDAEEVIIRTKDKEIVFENPQVTVMKAQGQETYQIVGEPEEVEKGAE
EAEVEIPEEDVELVAEQTGVSEEEAREALEEANGDLAEAILKLEEE
>gnl|CDD|440920 COG1309, AcrR, DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription]
RRRREATRERILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALE
EALAAEDPRERLRALLRAYLEFLAENPALARLLLAEAAELPELRAALRALLRRLRALLAELLRAGGLLAD
VDPDALARALLALLDG
>gnl|CDD|440921 COG1310, Rri1, Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif [Posttranslational modification, protein turnover, chaperones]
MLVLPRELLDAILAHAEAAYPEECCGLLLGKGGGDKRVTRVYPARNVAESPETRFEIDPEDLLAAEREAR
ERGLEIVGIYHSHPDGPAYPSETDRAQAAWPGLPYLIVSLPDGGPELRAWRLRDGRF
>gnl|CDD|440922 COG1311, HYS2, Archaeal DNA polymerase II, small subunit/DNA polymerase delta, subunit B [Replication, recombination and repair]
MSAKDIDREVEVLSDITGKSTCTGEVEDFVAYFRDRYEKLKKILRGRVNARPIESIAKLKKGGEEVSIIG
MVSDIRSTKNGHWIVELEDPTGTIPVLVMKDRDLFELAEELLLDEVIGVEGTLSNDGGLFFADEIIFPDV
PRTHEPNRSDREVYAVFISDVHVGSKTFLEDAWERFIDWLNGEEDNEIASRVKYLLIAGDLVDGIGIYPG
QEKELDIVDIYEQYEEFAEYLKEIPKDIKIVIIPGNHDAVRLAEPQPALPEEYRKIFYAENVTFVGNPAM
VTLEGVKVLMYHGRSLDDVIAEIPGASYDKPAKAMKELLKRRHLAPIYGGRTPIAPEKEDYLVIDEVPDI
FHTGHVHKLGVGKYRGVLLINSGTWQSQTEFQKSVNIVPTPGIAPIVDLKTLKVTVLDFSE
>gnl|CDD|440923 COG1312, UxuA, D-mannonate dehydratase [Carbohydrate transport and metabolism]
MKMTWRWFGPNDPVTLEDIRQIGATGIVTALHHIPVGEVWPVEEIAERKAEIEAAGLEWSVVESVPVHED
IKLGLGDRDRYIENYKQSLRNLAAAGIKTVCYNFMPVLDWTRTDLAYPLPDGSTALRFDQADFAAFDLFI
LKRPGAEADYSEEVVADAKERFEAMSEAEKARLTRNIIAGLPGWEEEYTLEEFRELLAAYKGIDEEKLRE
NLKYFLEEVIPVAEELGIKMAIHPDDPPWPIFGLPRIVSTEEDLRRLLDAVDSPANGLTLCTGSLGARPD
NDLPAMARRFGDRIHFAHLRNVKREGDGSFYEAAHLDGDVDMVAVVKALLDEEARRRADFDIPMRPDHGR
MILDDLGRKGRPGYGLIGRALGLAELRGLWEAIEKMLK
>gnl|CDD|440924 COG1313, PflX, Radical SAM superfamily enzyme PflX [General function prediction only]
AYELLESCTLCPRNCGVNRLAGEKGFCGAGRKAKVASAGLHFGEEPPLSGTNGSGTIFFSGCNLRCVFCQ
NYEISQEGEGKEISVEELAEIMLELQEQGAHNINLVTPTHYVPQILEALKIAKEKGLRLPIVYNTSGYES
VETLRLLDGIVDIYLPDFKYADDELAKRYSGAPDYPEVARAAIKEMHRQVGDLVFDEDGIAKRGLIVRHL
VLPGNLAGSKKVLRFIAEELSPDTYVSLMSQYTPAYKAREYPELNRRITREEYEEALDYARELGLENGFI
QELDSSESFIPDFDL
>gnl|CDD|440925 COG1314, SecG, Protein translocase subunit SecG [Intracellular trafficking, secretion, and vesicular transport]
MYTVLLVLHVIVAILLIGLVLLQSGKGAGLGAAFGGGASGTLFGARGAANFLTRATAILAVLFFVLSLVL
AYLASRGSSASSVLDQSAPAP
>gnl|CDD|440926 COG1315, FapA, Flagellar assembly protein FapA, interacts with EIIAGlc [Cell motility]
VDFAELIEEEAIKKALNNAKGEEVKIAERRDAKIEIEISEDKMEAYLTLTPPEGGKPLTKEEILEALKEA
GIVYGIDEEAIEKLLENPYGEKILIARGKPPVDGEDGRIEYLFDLDKERKPKEDEDGRVDFRELGLIINV
KKGDVLARKIPPTPGEPGKTVTGEPIPAKPGKDIPLKAGKGTELSEDGNTLVAAIDGQPVLENGKISVDP
VLEVKGDVDLSTGNIDFDGSVIIKGDVLSGFSVKATGDIEVGGVVEGATIEAGGDIIIKGGIIGKGKGVI
KAGGNVTAKFIENATVEAGGDIIVSDYIMHSNVKAGGSVIVGGRKGVIIGGSIRAGEGIEAKTLGSPAGT
KTEIEVGEAKIIVTKTVYPGVKIQIGNASYRIKEEIGGVTFYLEDGEIKIS
>gnl|CDD|440927 COG1316, Cps2a, Anionic cell wall polymer biosynthesis enzyme TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan teichoic acid transferase) [Cell wall/membrane/envelope biogenesis]
MSKILRILLAVNILLLGSDSREGDRGGGRSDTIMLAHIDPDTKKVTLVSIPRDTYVDIPGYGKDKINAAY
AYGGPELLVKTVENLLGIPIDYYVVVDFDGFKKLVDALGGVEVCVPKPMDYGDPYLGIDLPAGTQTLDGE
QALAYVRFRHGDPDGDLGRIERQQQFLKALLKKLLSPGTLTKLPKLLDALSKNVTTDLSLSDLLSLAKAL
RKLDGGNIEFVTLPGEGSYIDDGVSYVLPDEEAIQALLQALLADDPPAEAAPSA
>gnl|CDD|440928 COG1317, FliH, Flagellar biosynthesis/type III secretory pathway protein FliH [Cell motility, Intracellular trafficking, secretion, and vesicular transport]
MEELEALREEAREEGYAEGYEEGLEEGRAEAEAEIAEALEQLQALLEQLQAPLEELDEELEEELVELALA
IARKVIGRELALDPEAILALVREALAALREAEEVTIRVNPDDLELVREALDELLGEGGWRLVADPSLARG
GCRIETDDGEIDASLETRLEELREALLEELEE
>gnl|CDD|440929 COG1318, COG1318, Predicted transcriptional regulator [Transcription]
MEIPLKPVGKEEIDQLETRLFLKTLFRPEVLGGLKKLVERLTWLPSLAVAAYAVAREEAGKTVSEIAEEL
GRTEQTVRNHLRADTKAGGLVKLAYEKLKEGELKLEIPWARIKGLEELKEKGKELEEKLEKVKELLHEIK
EAL
>gnl|CDD|440930 COG1319, CutB, Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit [Energy production and conversion]. Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
MAPFEYHRPTSLEEALALLAEHGPDARVLAGGTDLLPLMKLRLARPEHLVDINRIPELRGIEEEGGGLRI
GALVTHAELAASPLVRERYPLLAEAARAIASPQIRNRGTIGGNLANADPAADLPPALLALDATVELAGPD
GERTIPAADFFLGPGETALEPGELITAVRLPAPPAGAGSAYLKVGRRASDAIALVSVAVALRLDGGTIRD
ARIALGGVAPTPWRAREAEAALAGKPLSEEAIEAAAEAAAAAADPIDDVRASAEYRRHLARVLVRRALAE
AAERA
>gnl|CDD|440931 COG1320, MnhG, Multisubunit Na+/H+ antiporter, MnhG subunit [Inorganic ion transport and metabolism]
ILEILVAVLLLLGALFALVGAIGLLRLPDFYTRLHAATKATTLGLGLILLGVALYFGSGAVSLKLLLIIL
FLLLTAPVAAHLLARAAYRSGVPPWEKTVVDELAEDLDRE
>gnl|CDD|440932 COG1321, MntR, Mn-dependent transcriptional regulator MntR, DtxR family [Transcription]
MMMLSESEEDYLKAIYELSEEGGPVRTSDIAERLGVSPPSVTEMLKKLEEKGLVEYEPYGGITLTEEGRE
LALRIVRRHRLLERFLVEVLGVDWDEAHEEAERLEHVLSDETIERLDAFLGFPEEDPHGDPIPDA
>gnl|CDD|440933 COG1322, RmuC, DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair]
LLLQERLTGEFENLANEILEEKLEKFQEQNEERLDQLLKPLRETLDEFEKKLEETEKRRAESFGSLSERL
EQLDEAQQQLSQEVGNLTRALKNKKTRGNWGEVQLERILEDAGLPEGCEYEEQVSLSNEDGSRLRPDVIV
RLPGGKWLVIDAKFPLEAYERLVEAEDEEEREAALKAHARSVRKHIKDLSEKDYWDLIPPETPDFVLMFL
PIEGAYAEALERDPGLIEEAFEKRVVLVSPTTLMALLRTVQMGWRQEAQEENASEIAELLGALYDEFGRF
GERLEKLGKHLDQAQKDYNQAVGKLTGNLLRRARKLEELGAEEKKELPELLEEAREEAEDEE
>gnl|CDD|440934 COG1323, TmcAL, tRNA-Met C34-N4-acetylcytidine synthase TmcAL [Translation, ribosomal structure and biogenesis]. tRNA-Met C34-N4-acetylcytidine synthase TmcAL is part of the Pathway/BioSystem: tRNA modification
MKAVGIIAEYNPFHNGHLYHIEEAKKLTGADVVIAVMSGNFVQRGEPAILDKWARAKMALKNGVDLVIEL
PVVFAVQSAEYFAYGAVSLLDALGVVDHLCFGSESGDIELLKEIAKILIEEPEEFKELLKKYLKKGLSYP
KARSLALEELLGDELAEDLSSPNNILGLEYLKALKKLNSPIKPLTIKRIGAGYHDEELTGKIASATAIRK
ALLEGDLEKLKNYVPPATYEILKEEIKEGRGPVSWEDFFPLLLYKLLTSSPEELANIYDVSEGLENRIKK
AARKAGSFEELIELIKTKRYTWTRIQRILLHILLGITKDDLESFLKKGPPYIRVLGFNKKGRELLKEIKK
KASLPIITKVSKYKKSLLELDIRATDLYSLLYPNPKPRKGQDFTRPPIIIK
>gnl|CDD|440935 COG1324, CutA1, Divalent cation tolerance protein CutA [Inorganic ion transport and metabolism]
SDYILVLTTAPDEEEAERIARALVEERLAACVNILPPITSVYRWQGKIEEDEEVLLLIKTTAERYDALEA
RIKELHPYEVPEIIALPIEAGNPAYLDWIREETR
>gnl|CDD|440936 COG1325, COG1325, Exosome subunit, RNA binding protein with dsRBD fold [Intracellular trafficking, secretion, and vesicular transport]
KIHYIELRVFCHATEDEDKVLEALLNLLPEEDDEIEREESEGHYGNPILILSARLEKKDAIREVLKRLIS
LLSEEDLEELLDELDERVDEDGKLYLRLDKQAAYLGEVRLSDGGDVIKIRIKVEAYPAKREKAIENLREL
LE
>gnl|CDD|440937 COG1326, COG1326, Uncharacterized archaeal Zn-finger protein [General function prediction only]
MSDMPERVAVVCPSCSPDEETVHEVLKEKGGNVTVRCTECGHVHKVTIEEPKPVEVKVIVSQDGESFTTT
VELPPDEIIEVGDEFVVDDEEAIMPVRITSIELGGGKRVEEAKAEDIETLWTRAVDNVRVKVSVHRGGET
RSLKVEVPGDYEFTVGETIEFGGEEFRIEAIKTRDDATRDRRGDTVEAKDIKRIYGRDERRRAWSAW
>gnl|CDD|440938 COG1327, NrdR, Transcriptional regulator NrdR, contains Zn-ribbon and ATP-cone domains [Transcription]
MRCPFCGHEDTKVIDSRPSEDGTAIRRRRECLACGKRFTTYERVELVPLMVIKKDGRREPFDREKLLRGL
LRACEKRPVSAEQIEAAVDRIERELRASGEREVPSREIGELVMEELKKLDEVAYVRFASVYRSFKDVDDF
REELEELLKEKEK
>gnl|CDD|440939 COG1328, NrdD, Anaerobic ribonucleoside-triphosphate reductase [Nucleotide transport and metabolism]. Anaerobic ribonucleoside-triphosphate reductase is part of the Pathway/BioSystem: Thymidylate biosynthesis
MMLKVIKRDGRVVPFDPEKIANAIKKAAKAVGGEDRDEELAEEIADEVEKELERLGGGGTITVEEIQDIV
EKVLMESGHPEVAKAYILYREQRTRLREARTTLVDDIELLDEYDDWRVNENANKSYSFSTQRDLIAGEVS
KEYALNKILPPEVADAHRNGDIHIHDLDYLPRMTNCCLWDLRDLLKNGFNGGNGKVEPPKHIQTALAQMA
QIIATVQSEQAGGQAFSRFDTYLAPYVRKDKLEGKTYKEIKQAMQSLEYNLNTLPSRRGQTPFTSITFGL
GTPEDFSWEMRMINKAILEVRIEGDGEGRTFIFPKLIFNITEGFNWEPEDPNYDLLQLAFECTAKRGYPY
FLNYDNSDELYKGSFKRSMGCRLFLDGWENGEELNRGRGNLGVVTLNLPRIAYEAKGDEEKFFEILDERL
DLAKEALEIKRKRLQKLAKAGLAPILYQTGAYLGRLKPDDSIDELFKNGFSTIGYIGLNEMLLNFTGKHH
IESEEAKAFALEILKHMRERADEWQEETGYLYSLYATPAESLTYRFAKLDKKRFGDIIGVTDKPYYTNSF
HLPVRKTIDPFEKLDFEDEYQPLYTGGTISYVELGELQPNPEALEAVVRYAYDNYRIGYLGINPPFDICP
KCGYLGGEHDECPKCGNEDTVEVIRRTCGYLGNVQPWNDGK
>gnl|CDD|440940 COG1329, CdnL, RNA polymerase-interacting regulator, CarD/CdnL/TRCF family [Transcription]
FKVGDKVVYPMHGVGVIEAIEEKEIAGEKKEYYVLRFPYDDMTIMVPVDKAESVGLRPVISKEEVEKVLD
VLKGRETVKPTNWSRRYREYEEKIKSGDIFEIAEVVRDLYRRDKEKKLSAGERKMLENARQLLVSELALA
LGIDEEEAEELIEEA
>gnl|CDD|440941 COG1330, RecC, Scaffold subunit RecC of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair]
MLHLYHSNRLEVLADLLAALLAAQPLADPFAPEVILVQSPGMARWLQLELAERFGIAANIEFPLPASFIW
QLFRAVLPDVPEESPFSKEALTWRLMRLLPELLDEPEFAPLARYLGDDEDQRKRYQLAGRLADLFDQYLV
YRPDWLAAWEAGEDVDGPLPDDQAWQAALWRALVAETGALQSAWHRANLYQRFIAALRSGEPRPAGLPER
VFVFGISALPPVYLEVLQALARHIDVHLFLLNPCREYWGDIVDARELARLAARSDDDDLLEVGNPLLASW
GKQGRDFLDLLAELEDESQEIDAFVDPPPDTLLHQLQADILELRPPAEGASKRPLAPDDRSLQVHACHSP
LREVEVLHDQLLALFADDPTLTPRDILVMVPDIEAYAPYIQAVFGQAPPDPRRIPFSIADRSARQENPLL
AAFLQLLDLPQSRFTASEVLDLLEVPAVARRFGLDEDDLERLRRWVAEAGIRWGLDAAHRARLGLPATEQ
NTWRFGLDRLLLGYAMGEEAGLWQGILPYDEVEGLDAELLGRLAEFLDRLAAWRQRLAEPRTLAEWLERL
RALLDDFFAPDEEDEWALAQLRRALAELAEQAAEAGYDEPLPLAVVRDALAARLDGRPTRQRFLAGGVTF
CTLMPMRSIPFRVVCLLGMNDGDFPRQQPPLGFDLMARHPRRGDRSRRDDDRYLFLEALLSARERLYISY
VGRSIRDNSERPPSVLVSELLDYLAQGFALPGDSGERLRAHLVVRHPLQPFSPRYFEPGSPRLFSYDAEW
LAAARALGQPRAPAPPFLAQPLPPPEPEEEVTLDDLLRFLRHPVRAFLRQRLGVRLPEEEEELEDAEPFE
LDGLERYQLRQRLLEALLAGDDPAELFARLRARGLLPPGAFGELLLERLLEEVAALAAALRPLLAGPPLE
SLDVDLDLGGVRLTGWLDGVRGDGLVRWRPGKLKAKDLLRLWLEHLALCAAGPPGGESVLVGRDGVWRLA
PLPPEEARALLAELLALYRQGLRQPLPLFPKTAWAWAEACYDGKTQEKALEAARQAWEGGDFVPGEGDDP
YLQRVFRGLDPLELDERFAALAERLLLPLLAHLEAAE
>gnl|CDD|440942 COG1331, YyaL, Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only]
MTNRLANETSPYLLQHADNPVDWYPWGEEAFAKAKREDKPILLSIGYSACHWCHVMEHESFEDPEVAALL
NEHFVNIKVDREERPDIDAIYMTAVQAMTGQGGWPLTVFLTPDGKPFFGGTYFPPEPRYGRPGFLDLLEA
IAEAWREDREEVEEQAEEITEALAEAASAAPPAAELDEELLDRAVEALLRSFDPEYGGFGGAPKFPQPPN
LEFLLRYAARTGDEEALEMVELTLDAMARGGIYDHLGGGFHRYSVDAEWLVPHFEKMLYDNALLLRLYAE
AYQLTGDPLYRRVAEETLDFLLREMTSPEGGFYSALDADSEGEEGKFYVWTPEELREVLGPEDAELFAEY
YGVTEEGNFEGKNILHLRRDLEELAEELSEEELEERLEAAREKLLAAREKRPRPGRDDKILTSWNGLMIA
ALAEAGRVLGDPEYLEAAERAADFILDNLWDPDGRLLRSYRDGEAGIPGFLEDYAFLIEALLALYEATGD
PRWLERALELADEALEHFWDPEDGGFFFTADDAEDLIVRPKEIYDGATPSGNSVAARNLLRLAALTGDER
YRERAERALRAFAGLLARYPLAHASLLLALDELLAGPLEVVIVGDEPAAELLRALLRRYLPNRVVLALPP
EDDLPLLAGRPAVDGKPTAYVCRGFTCSLPVTDPEELLELLK
>gnl|CDD|440943 COG1332, Csm5, CRISPR-Cas system type III CSM-effector complex subunit Csm5, RAMP superfamily Cas7 group [Defense mechanisms]. CRISPR-Cas system type III CSM-effector complex subunit Csm5, RAMP superfamily Cas7 group is part of the Pathway/BioSystem: CRISPR-Cas system
MNIFKYTLKLETLSPVHIGSGEKLSPFEYVIEGGKLYILDQEKLFEFLSERELLDEYLEFIENNNPKLFS
LQKFLKKNGLDDKDIKEFYRYKISSNRNDINRNEIRRFIKNGNGRPYIPGSSLKGAIRTALLYHLLKKNN
EELEIVLNKIREKLNKRFKKAAQALEKELFGKRSGDPNYDLFRALKVSDSNPISPDELEIYEKKIINLKK
GGKKGIPIYRECIKPGVKFSFSITLDSKLLKRFKNERGSKESLEDLVEACNEFYRDLIEEELAFFKKVLG
LNSLLKFYEKLKQKIEAAEEFLLRLGWGSGFLSKTLGLLLDDEDEEEIRKIFGLKKREKDNFPFPKTRRV
VFDNGRPNYYPLGWIKLEIEE
>gnl|CDD|440944 COG1333, ResB, Cytochrome c biogenesis protein ResB [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
MSPALGLRGWLRWAWRQLTSMRTALFLLLLLAVAAIPGTLLPQRSPDPAGVTQYLADYGPTLGPILDRLG
LFDVYSSWWFSAIYLLLFISLIGCSIPRLPPHWKALRAQPPRTPRRFLKRLPHHAELTVDASPDEVLERA
AALLRKRGYRVREREDDGGVSVSAEKGYLRELGNLVFHLSLLGILIGVALGSLFGYRGQVIVVEGETFAT
LVGYDSFDGDQLLPFSVRLDDFTVEYYDNGQPKDFQSDVTVTEGGGGEVKEATIRVNHPLRYDGYRVYQS
GYGYAPSVTVRDKDGGVVFGGPVPFLPQDSSIKVPDNGLPEQLGLEFFLPTAALDGDGVPTSKSPDPNNP
ALVLKVYRGDLGLDTGVPARSFLAPGQTVELPDGLGTITFDGFGVKRFTGLQVSKDPGQPLVLLGAILLL
LGLILSLYVRRRRVWVRVTPDGDGGTVVEVAGLARKNDAGLEKEFDRLAAALDQAEEED
>gnl|CDD|440945 COG1334, FlaG, Uncharacterized conserved protein, FlaG/YvyC family [General function prediction only]
MDISSISSSSAPSSASSQSVPPSSSEVAETQAALAEEAAAPEKAEEEVSKEELEKAVEKLNEFLQSLNTS
LEFSVDEDTGRVVVKVIDKETGEVIRQIPPEEVLDLAAKLRELVGLLVDEKA
>gnl|CDD|440946 COG1335, PncA, Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction only]. Nicotinamidase-related amidase is part of the Pathway/BioSystem: Pyrimidine degradation
ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPG
TPGAELVPELAPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVT
VVEDACASRDPEAHEAALARLRAAGATVV
>gnl|CDD|440947 COG1336, Cmr4, CRISPR-Cas system type III CMR-effector complex subunit Cmr4, RAMP superfamily Cas7 group [Defense mechanisms]. CRISPR-Cas system type III CMR-effector complex subunit Cmr4, RAMP superfamily Cas7 group is part of the Pathway/BioSystem: CRISPR-Cas system
AALLFLYALTPLHVGTGQRLGVVDLPIQRERHTGFPIIPGSSLKGALRSYAEALYGKEDEELVCALFGPE
PDEGSDHAGAVSFGDARLLLFPVRSLKGVFVWVTCPYLLRRLGRDLGLAGISEPLDEGEALVAKDLLEGG
KVVLEELELKVKKNPKLKALADWLAKLLPDDELLKKRLVVVSDDDFSYLVNSALEVQTRVRIDPETKTVE
EGALWYEEALPRETVLYSLVLARDSRNGKDSLDAEDVLEKLKELLDGEYLQIGGKETVGRGLVRLKLVG
>gnl|CDD|440948 COG1337, Csm3, CRISPR-Cas system type III CSM-effector complex subunit Csm3, RAMP superfamily Cas7 group [Defense mechanisms]. CRISPR-Cas system type III CSM-effector complex subunit Csm3, RAMP superfamily Cas7 group is part of the Pathway/BioSystem: CRISPR-Cas system
LRNRIKITGTIELLTPLHIGSGKGGGIGGVDNPVIRDPDGRPYIPGSSLKGVLRSLLERLLRSLGGDVCE
KGEKSCPVCRLFGSPGEGLASRLIFSDAYLDEEALTEIRTGVAIDRVTGTAADGALRDYEVVPAGTKFEG
EIELENLDEEELGLLLLALKLLEEGDDRLGGGKSRGLGRVKLELLEVTVRDLKNGYEKELDLEQLEELLK
KL
>gnl|CDD|440949 COG1338, FliP, Flagellar biosynthesis protein FliP [Cell motility]
MRRRLLALLLLLALLLLPAPALAQPGLPSLSLTLGGAGGGQTYSLSLQILLLLTVLSLAPAILLMMTSFT
RIIIVLSFLRQALGTQQTPPNQVLIGLALFLTFFVMAPVFDQIYDDALQPYLAGEITQEEALERASEPLR
EFMLKQTREKDLALFADLAGEPPPETPEDVPLRVLIPAFVISELKTAFQIGFLIFLPFLVIDLVVASVLM
SMGMMMLPPVMISLPFKLLLFVLVDGWNLLVGSLVRSFG
>gnl|CDD|440950 COG1339, Rfk, Archaeal CTP-dependent riboflavin kinase [Coenzyme transport and metabolism]. Archaeal CTP-dependent riboflavin kinase is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
GYDELATLKLLALLGALKGPVKISSSELAKRLGISQQTASRRLQELEDAGLIERDLVGDGQWVKITEKGE
ELLRREYADYRRIFEIKDSLELTGTVVSGLGEGRYYISLPGYKEQFREKLGFEPYPGTLNVKLDDESVRK
RRRLESLDGIIIDGFEDEGRTFGGVKCYPAKINGIPAAVIVPERTHHPEDVLEIIAPVKLRDELGLKDGD
EVTIEVELE
>gnl|CDD|440951 COG1340, COG1340, Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]
SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELN
EKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVE
KIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE
ADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGE
KLTTEELKLLQKSGLLE
>gnl|CDD|440952 COG1341, Grc3, Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and biogenesis]
MEVVLGAGASYEPVEGEEVPEEWEELLEEILSSGPGRIMVLGPVDSGKSTLTTLLANKLLAEGLKVAIID
ADVGQSDLGPPTTVSLGLVREPVLSLSELKAEKLRFVGSISPSGHLLRIVAGVKRLVERAKERGADRIVI
DTDGWVRGPAAREYKAALIEALKPDLIVVLGREDELEPILAKFPGIKVIRLPVPPVVRERSREERRLYRE
EKYRRYFEGAKLREVSLEDVKILGTPLFNGEPLDEEELSSVLYAEKSGDKLILVSEVEKLKRRLGVKEVY
ILPPGELRGLLVGLIDGDGFLLGLGILKEIDFEEGKIKILTPYEDGEVRGIRLGRIRLDEEFEELGRLDP
LVA
>gnl|CDD|440953 COG1342, COG1342, Predicted DNA-binding protein, UPF0251 family [General function prediction only]
MPRPKKCRRVCFLPEVRCFKPAGIPLRELEEVVLTVDELEAIRLVDLEGLTQEEAAEKMGVSRPTFQRIL
KSARKKVADALVNGKAIRIEGGNYELCEG
>gnl|CDD|440954 COG1343, Cas2, CRISPR/Cas system-associated endoribonuclease Cas2 [Defense mechanisms]. CRISPR/Cas system-associated endoribonuclease Cas2 is part of the Pathway/BioSystem: CRISPR-Cas system
MWVLVVYDIPDDKRRRKVAKLLKKYGFRVQYSVFEGELTEAELAELKKRLKKIIDPEEDSVRIYPLTDKQ
FGKVEVLGKKKDPEQLLIL
>gnl|CDD|440955 COG1344, FlgL, Flagellin and related hook-associated protein FlgL [Cell motility]
MRISTNMSALNALRNLNRTQSDLAKLQEQLSSGKRINSASDDPAGAAIALRLRSQIRGLEQYQRNANDAI
SRLQTAEGALGEITDILQRARELAVQAANGTLSDEDRAAIAAELEQLLDQLLSIANTTDFNGRYLFAGTA
TDTPPFQVDYQGDAGQRTAALGALDAALDNVSSARAELGARQNRLESAINNLSDLSENLTAALSRLEDAD
MAEAITRLTKLQTLLQAALAALAQANQLSLLDLLR
>gnl|CDD|440956 COG1345, FliD, Flagellar capping protein FliD [Cell motility]
MASISSLGLGSGLDTDSLVSQLMAAERAPLTRLTQQQTSLEAQISAYGTLKSALSSLQDALSALKKSSTF
NAKKATSSNESAVTATATSGAAAGSYSIEVTQLAQAQSLASAAFASATTTLGTGTLTITVGDGKTVTITI
DANDTLADIADAINAAGAGVTASIVNDGSYRLVLTSKKTGAANAITVSVSGDGALSALLGFDPASGMTET
QAAQDAKLTVNGITITSSSNTFTDAIDGVTLTLKKVTGGPVTLTVSTDTDAIKKAIKDFVDAYNELIDTI
NSLTKYTKDEETAKAGALLGDSTLRSLQSQLRSALSSPVSGGGSYKSLSDIGITTDKDGKLELDETKLDK
ALAEDPDAVAKLFTGDGKTTGIATRLDDLLDSYTGSDGTITSRTDGLNKQLKDLDDQIERLEDRLEAREA
RYRKQFTALDTAMSQLNSQSSYLTQQLASL
>gnl|CDD|440957 COG1346, LrgB, Putative effector of murein hydrolase [Cell wall/membrane/envelope biogenesis]
MVYLLASPLFGLTLTLAAYLLAKKLYRRTGSPLLNPVLIAIVLLIALLLLTGIPYETYFEGGQFIHFLLG
PATVALAVPLYEQRHLIRKYWLPILLGLLVGSVVAIVSAVLLAKLLGLSPELLLSLAPKSVTTPIAMGIS
ESIGGIPSLTAVFVIITGILGAVLGPPLLKLLRIRDPVARGLALGTAAHGIGTARAFEIGEEEGAFASLA
MGLNGILTALLAPLLAPLLL
>gnl|CDD|440958 COG1347, NqrD, Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrD [Energy production and conversion]. Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrD is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase
MAFSKKNKKVLTDPLFDNNPITLQILGICSALAVTTKLKTALVMSIAVTLVTAFSNLFISLIRNHIPSSI
RIIVQMTIIASLVIVVDQVLKAYAYDISKQLSVFVGLIITNCIVMGRAEAFAMKNPPWPSFLDGIGNGLG
YGLILLIVAFFRELFGSGTLFGFQVLPLVNYGGWYQPNGLMLLPPSAFFIIGLIIWALRSWKPEQVEK
>gnl|CDD|440959 COG1348, NifH/CfbC, Nitrogenase ATPase subunit NifH/coenzyme F430 biosynthesis subunit CfbC [Coenzyme transport and metabolism, Inorganic ion transport and metabolism]
MMRQIAIYGKGGIGKSTTSSNLSAALAEMGKKVMQIGCDPKADSTRLLLGGKRIPTVLDTLREKGEDVEL
EDIVFEGFGGVKCVEAGGPEPGVGCAGRGIITAIELLEELGAYEEDLDVVIYDVLGDVVCGGFAMPIREG
YADEIYIVTSGEFMALYAANNICKGIKKYANRGGVRLGGIICNSRNVDGERELVEEFAERLGTQIIAFVP
RSNIVQRAELNGKTVIEYAPDSEQADEYRELAKKILENKKLVIPKPLSDEELEELLLEYGILEKED
>gnl|CDD|440960 COG1349, GlpR, DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, Carbohydrate transport and metabolism]
MLAEERRQKILELLRERGRVSVEELAERLGVSEETIRRDLAELEEQGLLRRVHGGAVLVSSAAAEPPFAE
RETLNAEEKRAIARAAASLIEDGDTIFLDAGTTTLALARALPDRRNLTVVTNSLNIANELAERPNIEVIL
LGGELRPSSGSLVGPLAEEALRRFRADKAFLGASGIDAEGGLTTFDEEEAEVKRAMIEAARRVILLADSS
KFGRRALARVAPLSEIDVLITDAGPPPELLEALEEAGVEVIVAE
>gnl|CDD|440961 COG1350, COG1350, Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport and metabolism]. Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
EQTKILLDESEIPTQWYNILADLPEPLPPPLHPGTGEPVTPEDLAPIFPMELIEQEMSTERWIEIPEEVR
EIYRLWRPSPLYRARRLEKALGTPAKIYYKYEGVSPAGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWG
SALSFACALFGLECTVYMVKVSYEQKPYRRSMMETYGAEVIPSPSDLTEAGRKILAEDPDTPGSLGIAIS
EAVEDAATRDDTKYALGSVLNHVLLHQTVIGLEAKKQLEKAGEYPDVVIGCAGGGSNFAGLAFPFLRDKL
RGKKDVRFIAVEPAACPTLTRGVYAYDFGDTAGLTPLLKMYTLGHDFIPPPIHAGGLRYHGMAPLVSQLY
HDGLIEAVAYPQLEVFEAGVLFARTEGIVPAPESAHAIKAAIDEALKCKEEGEEKTILFNLSGHGHFDLA
AYDAYLAGKLEDY
>gnl|CDD|440962 COG1351, ThyX, Thymidylate synthase ThyX, FAD-dependent family [Nucleotide transport and metabolism]. Thymidylate synthase ThyX, FAD-dependent family is part of the Pathway/BioSystem: Thymidylate biosynthesis
MKVRLIDYTPDPEDLIAAAARVSYSSKSLRELLKELSEEKAEKLIRRLLRHGHESPFEHASFTFAIEGVS
RAVTHQLVRHRIASYSQQSQRYVKLDDKEYYIPPEIAKNEELLEEYEEAMEKAFEAYEELLERGVAREDA
RYVLPNATETKIVVTMNLRELLHFLKLRCCSHAQWEIRELAEAMLEELKKVAPLLFE
>gnl|CDD|440963 COG1352, CheR, Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]
MAELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALT
INVTEFFRDPEHFEALREEVLPELLARRRAGRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAGWRVEILA
TDISEEALEKARAGIYPERSLRGLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPPPFGRFDLI
FCRNVLIYFDPELQRRVLRRFHDSLAPGGYLFLGHSESLGGLSDLFEPVDKKGRFIYRKRAA
>gnl|CDD|440964 COG1353, Cas10, CRISPR/Cas system-associated protein Cas10, large subunit of type III CRISPR-Cas systems, contains HD superfamily nuclease domain [Defense mechanisms]. CRISPR/Cas system-associated protein Cas10, large subunit of type III CRISPR-Cas systems, contains HD superfamily nuclease domain is part of the Pathway/BioSystem: CRISPR-Cas system
DRLKFLLVSGDISGIQDFIFQKRALKDLRGRSFLLSLLTEAAALELLEKLGLDNIIYPGGGRFLALLPEE
TAEALEEIEKAINEWLLEIFKGQLELALAAVELSANDLLGGNYSELYRKLERKLEARKLRRFSLDFAPLF
EELGKGGGRKCSLCGRRPAVVEEKKEGERLCALCRLIKRKYLIRKFPSTSDIAALPFLEKLEEKLKELYL
LNDGELLEERLLANYVPKKKLEEPKTLEELAEKSGEGIPYLAVLKADGDNMGKIFSGEKEATPSRHATLS
RALSLFFKKAVNEIVEELRHNGYVIYAGGDDVLAIGPWDEALEFARELREAFEEYTGNLNPEITLSAGIV
IAHPKYPLYRALELAEELLKKAKKVSEKGKNALAIFLLKRSGEELTTVVPWDLELEELLEEKLKELELSR
SFLYKLLELLEELEEDNNLWRAELAYLLARNKEEKLEEKEKLLKELAKLLRELDLLL
>gnl|CDD|440965 COG1354, ScpA, Chromatin segregation and condensation protein Rec8/ScpA/Scc1, kleisin family [Replication, recombination and repair]
PDALEVKLDNFEGPLDLLLHLIRKQKLDIYDIPIAEITDQYLAYIEAMRELDLELAAEFLVMAATLLEIK
SRMLLPRPEEEEEEDEEDPREELVRRLLEYKAFKEAAEELAERERLGRDVFPRGVPEEERFVERLLPDVD
LEDLLEAFARVLRRAELVPVHHIEREEVSVEEAMEEILRRLREGGRVSFSELFADEESRSEVVVTFLALL
ELVKEGLIELEQEEPFGPIYIRRREEA
>gnl|CDD|440966 COG1355, Mho1, Predicted class III extradiol dioxygenase, MEMO1 family [General function prediction only]
MAMVRPPAVAGSFYPADPEELRAQIESFLAEAPPPAAKGRPKALIVPHAGYIYSGPVAAHAYAALAESGK
PDTVVILGPNHTGLGRGIAVTSAGAWETPLGDVPVDRELADALAELSGLVEVDELAHAREHSLEVQLPFL
QYLLPDFKIVPILVGDQSPETAEELAEALAELLKEGRDTLIVASSDLSHYGPYEEAREKDRETIEAILAL
DPEGLYRVVREENISACGYGPIAALLEAAKKLGAKKGELLDYATSGDVSGDKSSVVGYASIVFY
>gnl|CDD|440967 COG1356, COG1356, Transcriptional regulator [Transcription]
MFDAKYSLLTRRQAEVLALRERGLTQQEIADILGTSRANVSSIEKSARENIEKARETLAFYETLDAPVRI
TIEEGTDLYDVPKLVYDEADEAGVKVRYDAPELMKLLRDAAGDAIKGRRVKEDIEVGVTRDGEVRVRVS
>gnl|CDD|440968 COG1357, YjbI, Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown]
DLSGADLSGADLSGADLSGADLSGANLSGALSGANLSGANLSGANLTGANLSGADLSGADLSGANLSGAD
LSGANLTGADLSGANLANLSGANLSGANLSGANLRGANLSGANLSGADLSGADLSGANLSGADLSGANLS
GANLSGADLSGADLSGANLSGANLSGANLANLEGADLK
>gnl|CDD|440969 COG1358, Rpl7Ae, Ribosomal protein L7Ae or related RNA K-turn-binding protein [Translation, ribosomal structure and biogenesis]. Ribosomal protein L7Ae or related RNA K-turn-binding protein is part of the Pathway/BioSystem: Ribosome 50S subunit
DKILNLLGLARRAGKLVSGEEQVLKAIRKGKAKLVIIAEDASENTKKKLLDLCEEYGVPVVEVGTKEELG
KAIGKVGRAVVAITDEGFAKKLLELLEE
>gnl|CDD|440970 COG1359, YgiN, Quinol monooxygenase YgiN [Energy production and conversion]
ITVIAKLTVKPGKRDEFLAALRELVEATRAEPGCLSYELYRDPDDPNRFVLYERWEDEAALEAHLASPHF
KAFLAALAPLLAEPPEVRVYE
>gnl|CDD|440971 COG1360, MotB, Flagellar motor protein MotB [Cell motility]
EEEGHHGGAWLVTYADLMTLLLAFFVLLWALSSALEENLLSGQVEVRITEEGLVIEIQDRVLFDSGSAEL
TPEGRELLDKIAAVLAEVPNRIRVEGHTDNVPISTARFPSNWELSAARAAAVVRYLIEGGVPPERLSAVG
YGDTRPLAPNDTPEGRARNRRVEIVILRRAAEEA
>gnl|CDD|440972 COG1361, MJ0795, S-layer protein MJ0795, predicted component of type IV pili-like system [General function prediction only]
LLVLLLLAALLAGPAAAVAVSGSPDLSVTVSDSNEVAPGEEVTLTVTITNDGTLTARNVTVELEGDYPFE
VKSGEQSVGGSLPPGQSVTVTFTVTVPEDAEPGTYPIPVTVSYSYGYTDRTETETYTVTVKVEGEPRFEV
VSVTSPDSLTPGDTGTLTLTIKNTGTGTAKNVTVTLTSPSGDLTDLEPGPRPATNVVVVLSSPVSPVGSN
SVALGTLEPGESATFTFKVDVSEDAEPGPYPLPLTVTYRDEDGDTYSDTVTIGVYVAPKADFEVENVEST
ITAGETVTITITVTNTGNETAKNVVARLSADDPLSSLDDEAFIGDLAPGESATVTFTVSASSDATPGTYP
ITVTIRYDDDDGNTQLSDTITVPVEVTEPSSGGLLTVLAIIIGLLIVAVGGYLYRRRKK
>gnl|CDD|440973 COG1362, LAP4, Aspartyl aminopeptidase [Amino acid transport and metabolism]
EEKEEAEAFAEDLLDFLDASPTERHAVAEIARRLEAAGFTELDETEKWKLKPGDKYYVVRNGKSLIAFVI
GKEPLETGFRIVGAHTDSPRLDLKPNPLYEDEGYAQLGTEVYGGPLLYTWLDRPLSLAGRVVLKDGSKVE
VRLVDFDDPVLRIPDLAIHLDREVNKGLELNKQEDLNPLLGSGDEEKEKKADLLKLLAEKYGIEEEDILS
ADLELVPAQKARDVGLDREFIASYRLDNLVSAYAGLEALLDAENPEKTAVLALFDHEEIGSETATGAQSP
FLEDVLERILAALGGSEEDLRRALANSFMLSADVAHAVHPNYPEKHDPTNAPLLGGGPVIKKNANQRYAT
DAESAAVFRRLCEKAGVPWQTFVGRSDMGGGSTIGPITATRLGIRTVDVGVPLLSMHSPRELAGKADVYY
LYKALKAFFE
>gnl|CDD|440974 COG1363, FrvX, Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism]
MDYLLELLKELTEAPGPSGFEDEVREYIKEELEPLGDEVETDRLGNLIATKKGKGDGPKVMLAAHMDEIG
FMVKHITDNGFLRFTPLGGWDPRVLEGQRVTIHTRDGDIPGVIGSKPPHVLTPEERKKPVDIEELFIDIG
ASSKEEAEALGIRVGDFVVFDPEFEELTNSGFIKSKALDDRAGCAVLLELLKALKDEDLPVTVYFVFTVQ
EEVGLRGASTAAYDIKPDEAIAVDVTPAGDTPGVNEEAVTKLGKGPAIRAKDSSGIYDPGLRRFLIELAE
ENGIPYQRDVLPGGGTDAGAAHLAGEGVPTALIGIPTRYIHSPYERIHLDDLEATVKLLVAYLESLDAET
VEG
>gnl|CDD|440975 COG1364, ArgJ, Glutamate N-acetyltransferase (ornithine transacetylase) [Amino acid transport and metabolism]. Glutamate N-acetyltransferase (ornithine transacetylase) is part of the Pathway/BioSystem: Arginine biosynthesis
MAVVSPLGGLTAPKGFRAAGVAAGIKKKGRKDLALIVSDVPATAAGVFTTNRVCAAPVLVCREHLAGGKA
RAIVVNSGNANACTGEQGLEDARAMAAAVAEALGIPPEEVLVASTGVIGEPLPMDKIEAGIPAAVAALSA
DGWEDAAEAIMTTDTFPKEAAVEVEIDGKTVTIGGIAKGSGMIHPNMATMLAFITTDAAISPALLQALLK
EAVDRSFNRITVDGDTSTNDTVLLLANGAAGNPPITEDDPDYAAFAEALTEVCQDLAKQIVRDGEGATKL
IEVRVTGAASDEEARKVAKAIANSPLVKTAIFGEDPNWGRILAAVGYSGADFDPDKVDIYLGDVLVAENG
GPVDYDEEAAAAVMKQDEITIRVDLGRGEGSATVWTCDLTYDYVKINADYRT
>gnl|CDD|440976 COG1365, COG1365, Predicted ATPase, PP-loop superfamily [General function prediction only]
HVEAYMDIFVKKYRLKLSLKALERLRDSNISEEAYERLRELLEKRLNGPKEFLKRSKEKNPKVVVAFSGG
VDSSASLIIAKWIGFDVEAVTVKSTIILPQMFKKNIKELCKKLNVKHEFIEIDLGEIIEDALKGKFHPCG
RCHSLIEEAVEDYAKKNGIKIVIFGDLLSVGYLSIYKKDGIVRLNLPAFLALDKDEIREILGNNGIELSM
KYGCPLLREAHKRHPSLRKFSIQRVLREVRAGVLEPGEALKLILDI
>gnl|CDD|440977 COG1366, SpoIIAA, Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction mechanisms]
SIPVEVRDGVLVLPLIGELDAARAPELREALLEALETGARRVVLDLSGVTFIDSSGLGALLSLAKAARLL
GGRLVLVGVSPAVARVLELTGLD
>gnl|CDD|440978 COG1367, Cmr1, CRISPR-Cas system type III CMR-effector complex subunit Cmr1, RAMP superfamily Cas7 group [Defense mechanisms]. CRISPR-Cas system type III CMR-effector complex subunit Cmr1, RAMP superfamily Cas7 group is part of the Pathway/BioSystem: CRISPR-Cas system
MPRLTLTFTLELVTPLFLGGADPQTAELRPPSIKGVLRFWWRALAGGRLGKDLEELRKLESEIFGSTFGL
REKKNRKKKTRKALKPGSSFTLTLTFPPEEVKEELEAALWLWSLFGGLGARSRRGFGSLKIVEIEGDKEL
KEKLRKLLKKLGEIPKDLPDFPAFKGTRLYVVKPKDALEKLGNFLREFRGKWPEADAIRRLTRKKFPRAV
FGLPRGDKYDRRASPLILSIHRGNGKYYPVILLLPSIILKPGGSKDLDALEAFLEKLKKKEI
>gnl|CDD|440979 COG1368, MdoB, Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis]
FFLLFLLLLSLRLVFLLFNFDLSLGEILQAFLYGLRFILYLLLLLLLLLLLLLPLLFRRPKLRWIYLLLV
LLLLLLLLVADILYYRFFGDRLNFSDLDYLGDTGEVLGSLLSSYDLLLLLDLLLLLLLLLLLYRLLKKLR
KSLPWRKRLALLLLLLALLLLGIRLGEDRPLNLSDAFSRNNFVNELGLNGPYSFYDALRNNKAPATYSEE
EALEIKKYLKSNRPTPNPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQG
GRTSRGEFAVLTGLPPLPGGSPYKRPGQNNFPSLPSILKKQGYETSFFHGGDGSFWNRDSFYKNLGFDEF
YDREDFDDPFDGGWGVSDEDLFDKALEELEKLKKPFFAFLITLSNHGPYTLPEEDKKIPDYGKTTLNNYL
NAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENPLERYRVPLLIYSPGLKKPKVIDT
VGSQIDIAPTLLDLLGIDYPSYYAFGRDLLSPDTDPFAFRNGGFITDDYVYVLKTGELTEEDKELEEEAL
AYLQLSDYLYGNDLLR
>gnl|CDD|440980 COG1369, POP5, RNase P/RNase MRP subunit POP5 [Translation, ribosomal structure and biogenesis]
KHLPPTLRPRKRYIAFEIISEAEIDRRELERAIWEAALNLLGDLGSAKADPRVIYFDFDGGRGILRCRRG
YVDEVRAALALVTEINGKPVIIRPLGTSGTIKAAKEKYLG
>gnl|CDD|440981 COG1370, ArcTGT, tRNA-guanine transglycosylase, archaeosine-15-forming, contains TGT and PUA domains [Translation, ribosomal structure and biogenesis]
MSDDDLERLRTIADYQFGRGAGEALFPDDITIERSKKTGRIRQVYLDGKRLATLRATDGRFTLTIEGARR
LHEALPFPKYRVVVDDESAPFVREGKNVFAKFVIDVDPEIRPGDEVLVVDEDDELLAVGRALLSGEEMKD
FKRGVAVKVREGVKKEK
>gnl|CDD|440982 COG1371, ARCH, Archease, activates RNA ligation by RtcB (tRNA splicing) [Translation, ribosomal structure and biogenesis]
MGYEFLDHTADVGIEAYGPTLEEAFANAALALFALMVDTSKVEPREEREIEVEAEDLEDLLVDWLNELLY
LFDTEGLLFSRFEVEIEENGGYRLEATARGEPLDPERHEFKVEVKAVTYHELRVEQEDGGWRAQVVVDV
>gnl|CDD|440983 COG1372, Hop, Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, transposons]
LLGLKETEIVLVATLVTDALRLKLLELKEEGIELLKLELDLEELGEVLAEALVRAIDGASLILLAAGGGV
LLVALTGLGREAAAGLALAGGDTGTGVCLTGDTLVLTADGRLVPIGELVGSGEDVEVLSLDLDTGKLVWA
PVTKVFKTGVKPVYRIRTRSGREIRATPDHPFLTLSGWKEAGELKPGDRVAVPRHLPSFGEEELPDSLDE
ELAYLLGLLLGDGSLSKRGAGRFTNADEELLEDVAEAAEELFGRADEGPRVEARRATVYEVRVSSKPLAE
LLEELGLFGKRSGEKRIPDFVFRLSREQIRAFLRGLFDADGSVSNRGGRIRLSTTSRRLAEQVQLLLLRL
GIVSRIYERRRPDGKGRTAYRLRISGGDNLRRFAERIGFGSSRKQERLAELLAALRRRKDDLVRARELAN
GRRLSRERLRRLALEDEALEALADSDVYWDEVVSIEPVGEEDVYDLTVPGTHNFVANGIVVHNSGGALDD
VGAAVLDEDLLGGEPEEGEAGGAAEDKDRAKTGATTLAAGDLLVERDVEAEPEEIEDVISGEGRILERAA
LLAVALDELEDELEEARAAAALKAKKAELAALLKETEPLVETEEEEEALLLEGAREIELLLEGRAEGLLE
AEALLAEPEKKLLEVDIQEEALVLAGLIGLRGEGLLEVAVEDLAAASVALIKKGLAAEARALVAAVREAA
LKDLRLLEARERAEDELELDELLKEIEAVRGVELLLALRAEDGELEAPLDAKEEDLLAALGIDYDIGGIE
LVLADGEQAAVAVDVSRPIRAGKELLEEAAAEEDIGAGRAAELEPIGIQGASELPKVEEAEEGRALLELA
EVVLSLLLERAVRAVEEARALSLEEG
>gnl|CDD|440984 COG1373, COG1373, Predicted ATPase, AAA+ superfamily [General function prediction only]
VMIMIKRKILDKLLKLLDNRKAVVITGPRQVGKTTLLKQLAKELENILYINLDDPRLRALAEEDPDDLLE
ALKELYPGKTYLFLDEIQRVPEWEDALKRLVDDGRNGRFILTGSSSLLLSKELAESLAGRIESLELYPLS
FREFLEAKGESLDDLLPLSEEHDELLELLEEYLLRGGFPEAVLLDDERDKRRWLKSYIETILERDIPKRA
GIRDPELLRRLLRSLASNLGQLFSYSKLANDLGISKKTVKRYLDYLEDAFLIFRLPPYDLNLKKRLRKSP
KLYLVDTGLLNALLGLDPEELLLDSEDLGALLENFVFLELLRRGYEVYYWRTKDGAEVDFVLEKGGKIIP
IEVKYGENTRERELKSLKKFRDKYGPAKGIVITLGDEGRLEIDGILVIPLWKLLL
>gnl|CDD|440985 COG1374, NIP7, Rbosome biogenesis protein Nip4, contains PUA domain [Translation, ribosomal structure and biogenesis]
MEPKLRRLSKEELKLIKKELEKYGDKDLLEEFNLLVLEGKFKDVYAVTEEVWEIIENLPKRPYSAGLHIG
EIGKEKFRPSLEGAQLLARYCEKNYVVVNEKGEKLFLYGRDVFKESIIEYPWKGNGRVVVLNKNGEPLGI
GRIRFEKGRKFIKNIVDVGWYLRRGG
>gnl|CDD|440986 COG1376, ErfK, Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis]
IVVDLSEQRLYVYEDGGLVRTYPVSVGRPGFPTPTGTFRVLRKAENPTWTPPAEMPAGMPGGPDNPLGPY
ALYLSDGGYGIHGTPWPSSIGRNVSHGCIRLSNEDAKWLYDRVPVGTPVVV
>gnl|CDD|440987 COG1377, FlhB, Flagellar biosynthesis protein FlhB [Cell motility]
MAEEDDGEKTEEPTPKRLRDAREKGQVARSRELTTALVLLAGLLLLLFLGPSLAERLGELLRSLLSFARA
LALDPADLLALLGALLLEALLALLPLLLVLALAALLANLLQGGFLFSTKALKPKFSRLNPISGLKRLFSL
RALVELLKSLLKLLLVGGVAYLVLRGELPELLALAALPLAAALALLGDLLLKLLLAVLLALLVIAAIDYP
YQRWEHEKKLRMTKQEVKDEHKESEGDPEVKGRIRQLQREMARRRMMAAVPKADVVITNPTHYAVALKYD
PGKMGAPVVVAKGADEVALRIREIAREHGVPIVENPPLARALYATVEVGQEIPEELYQAVAEVLAYVYQL
KR
>gnl|CDD|440988 COG1378, YrhO, Sugar-specific transcriptional regulator TrmB [Transcription]
ELIELLEKLGLSEYEAKVYLALLELGPATASELAKASGVPRSRVYDVLESLEEKGLVEVSEGRPKRYRAV
PPEEALERLLEEREEELEELREELEELYEELREPEEELVWVVKGREAILERLRELIASAEEEILIVLSPP
ELLLEELEEALEEALERGVKVRVLVSPEVLEVPERLEEEGEEVRVLPGLPGRLLIVDDKEALISVSEPDG
EETAIWIEDPELAALLRELFETLWEKAE
>gnl|CDD|440989 COG1379, YqxK, PHP family phosphoesterase with a Zn ribbon [General function prediction only]
MRFFADLHIHSGYSRATSKDLTLENIAEWARRKGIDLVGTGDFTHPAWLEELKELLEEAEGGGFRYGGVR
FILGAEIETIYKKKTRKVHHLIYLPDLEAAEEFSEWLSKIVGNIHLDGRPILGLDARELLEIVLELGGLF
IPAHIFTPWKSLYGSKFDSLEECFGDLTDHIDAVELGLSSDPDMADRISELDRYTFLSNSDAHSPAKLGR
EANLFDLTELSFEEIRKALKTKDGRGILANYGFFPELGKYHRTGCRKCGVRLEPEETRALGGRCPVCGKP
LTKGVLDRIEELADREEPVHPPHRPPYIYLVPLAEIPGEILGVGPKTKKVQRAYEKLLEAFGTEMDILHE
APLEELAKVVGEKLAEAIVRAREGKVIIQPGGGGEYGKIRLFEPGELERLSG
>gnl|CDD|440990 COG1380, YohJ, Putative effector of murein hydrolase LrgA, UPF0299 family [General function prediction only]
MLRQLAILLLFQLLGELLSRLLGLPIPGSVIGMLLLFLLLALGIIKLEWVEPGADFLLRHLSLLFVPAGV
GVMNYLDLLSAEGLPILLAIVVSTLLVLAVTGLVVQLLLRRKEKKGERKA
>gnl|CDD|440991 COG1381, RecO, Recombinational DNA repair protein RecO (RecF pathway) [Replication, recombination and repair]
MSLYKTEAIVLRTRPYGETDLIVTLFTREHGRISAVAKGARRPKSRLRAVLQPFTPLDLSWYKGRELGTL
TQAELIGSFAALRLDLLALAAASYLAELLDRLLPEEEPHPELFDLLLAALDALAEGEDPELLLRRFELRL
LAELGYGPDLDRCAVCGEPLEDLYYFSPEEGGALCPRCSAGGPALALSGETLLLLRALLRGDLDDLGALS
LSPETLRELLRLLRAYLRYHLGRRPLKSRELLEQL
>gnl|CDD|440992 COG1382, GimC, Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]
MMQNLPPEVQNQLAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKLPDDAEVYKSVGNLLVKTDKE
EVIKELEEKKETLELRLKTLEKQEERLQKQLEELQEKLQEALSGAGGGGGA
>gnl|CDD|440993 COG1383, RPS17A, Ribosomal protein S17E [Translation, ribosomal structure and biogenesis]. Ribosomal protein S17E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MGNIRPTYIKRIARELLEKYPDLFTEDFEENKKLVEELTDVESKRVRNRIAGYITRKVKKRKR
>gnl|CDD|440994 COG1384, LysS, Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]. Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MSDDAPDSKAWPFEEADKLLKRLEKKGKEPVVFETGYGPSGLPHIGTFGEVARTTMVRRALRELGIPTRL
ICFSDDMDGLRKVPDNVPNQEMLEKYLGKPLTRIPDPFGCHESFGEHFNARLRAFLDSFGFEYEFISATE
LYKSGRFDEALLRALENYDKIREILLPYLGEERRATYSPFLPICPKCGRVLQTPVIEVDAEAGTVTYRCE
GCGHEGETPVTGGNGKLQWKVDWAMRWAALGVDFEPFGKDHAAGSVDSGSKIAREVLGGEPPEGFVYELF
LDENGEKISKSKGNGLTVEEWLEYAEPESLRYFMFRKPKKAKDLDFDVIPKLVDEYDRFERKYFGEEDQE
EEERLANRVYHIHVGNPPKEMPLPVPYRFLLNLAQVANAEDKEVLWGFLRRYAPDATPETHPRLDERVER
ARRWARDFVPPTKKFRLPEELPDVELDDKERAALEDLAERLEALEDWDAEEIQNEVYEVGKEHGFELRDW
FKALYEVLLGQEQGPRLGSFLALLGKEFVIALIRR
>gnl|CDD|440995 COG1385, RsmE, 16S rRNA U1498 N3-methylase RsmE [Translation, ribosomal structure and biogenesis]. 16S rRNA U1498 N3-methylase RsmE is part of the Pathway/BioSystem: 16S rRNA modification
MRMPRFFVPPELAAGDTVTLDGEEAHHLVRVLRLKPGDEVILFDGRGGEYLAEITEIGKKSVTLRILEQL
EREPEPPLRLTLAQALPKGDRMDLIVQKATELGVDRIVPVITERSVVKLDGERAEKKLERWQKIAIEAAE
QSGRARLPEVAPPVSLAELLAELPAGDLRLVLHEEEAKASLKELLPPGGSVALLIGPEGGFSEEEIELLR
AAGFQPVSLGPRILRTETAALAALAALQALLGDWG
>gnl|CDD|440996 COG1386, ScpB, Chromosome segregation and condensation protein ScpB [Transcription]
MERAELKAIIEALLFAAGEPLSLEELAELLGLDEEEVEEALEELAAEYASRGRGIELVEVAGGYRLQTRP
EYAPYVRRLLKEEKPKRLSRAALETLAIIAYRQPVTRAEIEEIRGVNVSGVIRTLLERGLIREVGRKEVP
GRPILYGTTEKFLDYFGLKSLDDLPPLEELEEAGELELLEE
>gnl|CDD|440997 COG1387, HIS2, Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and metabolism, General function prediction only]. Histidinol phosphatase or related hydrolase of the PHP family is part of the Pathway/BioSystem: Histidine biosynthesis
MRGDLHTHTTYSDGEGTIEEMVEAAIELGLEYIAITDHSPSLFVANGLSEERLLEYLEEIEELNEKYPDI
KILKGIEVDILPDGSLDYPDELLAPLDYVIGSVHSILEEDYEEYTERLLKAIENPLVDILGHPDGRLLGG
RPGYEVDIEEVLEAAAENGVALEINTRPLRLDPSDELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALA
RRAGLTKEDVFNTLRKEELLKL
>gnl|CDD|440998 COG1388, LysM, LysM repeat [Cell wall/membrane/envelope biogenesis]
GLLLALSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKA
ALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGL
SSDTIRPGQKLKIPAS
>gnl|CDD|440999 COG1389, COG1389, DNA topoisomerase VI, subunit B [Replication, recombination and repair]
AAIAEELAEKQKEISVAEFFEKNKQLLGFDSPARALYTTVKEAVDNSLDACEEAGILPDIKVSIERVDGK
DIYRVTVEDNGPGIPPEQIPKVFGKLLYGSKFHVLRQSRGQQGIGISAAVLYAQMTTGKPVEVISKTGGS
EPAYYFELKIDTKKNEPVILEKEEVDWDRWHGTRVELELEGDYVRGKQSIYEYLKRTAIVNPHARITFID
PDGEVYTFPRATEKLPKPPKEIKPHPHGVELGTLKRMISNTKKRTLKEFLVNSFSRVGDKTAEEILKKAG
LDPDKPPKKLSREEAEKLVEAFKKVKFMAPPTDCLSPIGEELIEKGLKKILNPEFVAAVTRKPKVYSGHP
FIVEAGIAYGGDIPPDGKPEILRFANRVPLLYDQGSCVITKAVESIDWKRYGLSQPGLPAGPLVILVHVA
STKVPFTSEGKEAIADVPEIEKEIRLALQEVARKLKKYLSKKEREKEAKEKLRIIEKYIPEIARKLAEIL
GKPVPDIEEKLAKIMGKVLEKEEVEEEKVTITVKNYTVKE
>gnl|CDD|441000 COG1390, NtpE, Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]. Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
MMSLEKIIEEILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELE
ARKELLEAKEELIEEVFEEALEKLKNLPKDPEYKELLKKLLKEAAEELGSGDLVVYVNEKDKELLEELLK
ELKKKGLEVSEEDIDILGGVIVESEDGRIRVDNTFESLLERLKEELLKEIAEILFG
>gnl|CDD|441001 COG1391, GlnE1, Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, chaperones]
MTAPLPAALQAALERLLARLLEALAALLALDPALRALLAAVLAASPFLARLLRRDPELLARLLASGPLPR
PLDAADLLARLAAALAAAADEAALMRALRRFRRREMLRIAWRDLAGLADLEEVTAALSALAEAAIQAALD
WLYRELAARYGTPLDADGEPQGLVVLGMGKLGGRELNFSSDIDLIFAYPEDGETDGRRSLSNQEFFTRLG
QRLIKLLDERTADGFVFRVDMRLRPDGDSGPLALSFAALEDYYQSQGREWERYAMIKARPVAGDLEAGEE
LLALLRPFVYRRYLDFGAIESLREMKRQIRAEVRRRGLGDNIKLGRGGIREIEFIVQTFQLIRGGREPEL
RQRSTLEALDALAELGLLPAEAADELAEAYRFLRRVEHRLQMLDDQQTHTLPEDEEDRARLARAMGFADW
AAFLAALDAHRQRVHRHFAALFGDPEELSSEDGPLNLLWTGDLDDEETLETLAQLGFEDPEAAAERLRAW
RHGRRVRTLSERARERLDRLMPRLLEALAETPDPDEALLRFLDLLEAIPRRTAYLALLAENPAALKRLAR
LCGASPWLAEYLARHPILLDELLDPRFLYEPPDRAALRAELRQRLARAPEDDEEQQLDALRQFKQAQVFR
IAAADLAGALPVMKVSDHLTALAEAILEAVLRLAWQELAARHGRPRHREGPGFAVIGYGKLGGKELGYGS
DLDLVFLYDDDDEAAETDGERPIDASQFYARLAQRLIHALTTRTAAGILYEVDMRLRPSGNSGLLVTSLD
AFEDYQRNEAWTWEHQALTRARVVAGDPALGARFEAIRREVLTRPRDPAKLREEVREMREKMRAELGSKS
AGRFDLKQDRGGIVDIEFIVQYLVLAHAHEHPELLRNSDNIRLLEALAEAGLLPAEDAEALADAYRLLRR
LQHRLRLQEQPARVPPDELEAERAAVRALWQRVFGEPA
>gnl|CDD|441002 COG1392, YkaA, Phosphate transport regulator YkaA, distantly related to PhoU, UPF0111/DUF47 family [Inorganic ion transport and metabolism]
LFPKEKSFFDLLEEHAEKVVEAAELLVELLEDYEDVEELAEEIKELEHEADEIKREIREELNKTFITPFD
REDILELASALDDIADYIEDIAGRLVLYKIEELDEELLELAELLVEAAEELVEAVKELRELLKKAEEVLE
LIIEINRLENEADDLYREALAKLFESEKDPIEVIKLKEIYELLEDIADRCEDVADRLEIIVLKNA
>gnl|CDD|441003 COG1393, ArsC, Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and metabolism]
MITIYGNPNCSTSRKALAWLEEAGIEYEFIDYLKTPPTAEELKELLAKLGLGVEELLNTRGTTYRELGLK
DKALSEEEALALMLEHPSLIKRPIVVTGDKALVGFPPEEVLALLG
>gnl|CDD|441004 COG1394, NtpD, Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]. Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 is part of the Pathway/BioSystem: A/V-type ATP synthase
AAKVKPTKMELLRLKRQLKLAKRGHKLLKDKRDALIREFLKLIDEAEELREELEELLEEAYEALALANAR
MGIEAVEELALSVPRVLEVEVSTRNIMGVEVPVLESEEFKEERPYGLLGTSAWLDEAIEALEELLELLLE
LAELETALRRLAEEIRKTQRRVNALEKVLIPRLEETIKYIRMKLEEREREEFVRLKKVKKKL
>gnl|CDD|441005 COG1395, COG1395, Predicted transcriptional regulator [Transcription]
MSREALIENVIALLERAGFVVSERCNIRPRSFDLVARRGDELLLIKVLYNIDSLSEETAEELKRLAKYLD
ASPLIIGERTRDEELEDGVVYERHGIPAVSPETLYDYFVEGEPPLIYAAPGGLYVKIDGEKLRELREERG
LSLGELASELGVSRRTISKYERGEMDASIEVALKLEEILGEPIVKPIDILEGAEDLEEAEPTPEDPEEEE
ILEVLSRLGFDVHPTKRAPFDAVAKDEDNTLLTGISKDTEKLEKRARLMSKISEVTGSRSVFIVEKKTKR
ESIEGTALIEEEELEKIDDPEELIDLIRERKEE
>gnl|CDD|441006 COG1396, HipB, Transcriptional regulator, contains XRE-family HTH domain [Transcription]
MSTLKKALGERLRELRKARGLTQEELAERLGVSRSTISRIERGRRNPSLETLLKLAKALGVSLDELLGGA
DEELPEALLSEEE
>gnl|CDD|441007 COG1397, DraG, ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones]
LLDRARGALLGLAIGDALGAPVEFYSREEIRARYGPITDYVGGGNLPPGEWTDDTQMALALAESLLEAGG
FDPEDLARRFLRWLRTGPGRDIGPTTRRALRNLRRGGAGESGEGSAGNGAAMRIAPLGLAYAGDPEEAAE
LARASAALTHGHPRAIAGAVAYAAAVAAALRGADLEEGYVVETLPAALWALLRADDFEEALLLAVNLGGD
TDTTAAIAGALAGALYGLEAIPERWLEPLERRDRLEELAERLAALA
>gnl|CDD|441008 COG1398, OLE1, Fatty-acid desaturase [Lipid transport and metabolism]
MTTATPAPPEKGRINWVTVLFFVLLHLLALLAAVPYAGVGFSWSAVALALVLYVLTGLGITVGYHRLFSH
RSFKTPRWLEYLLAILGALALQGGPLWWVADHRRHHRHSDTEGDPHSPKLRGFWWSHMGWMLREDPTPND
YRYAPDLAKDPELRWLDRYYLLLQLALGLLLPALLGGLLGGGWSGLLWGGFVRTVLLHHGTWFINSLAHV
WGYRPFETRDTSRNNWWLALLTFGEGWHNNHHAFPTSARHGLRWWEIDPTWWLIRLLEKLGLAWDVRRPP
AERIAA
>gnl|CDD|441009 COG1399, YceD, 23S rRNA accumulation protein YceD (essential in plants, uncharacterized in bacteria) [Translation, ribosomal structure and biogenesis]
MSKLKMKIDLAELKAGKGLEFEGEVDLAELERLADLPALGPVRVDLRLEKVGGGVLLTGTVEGTVTLPCD
RCLEPFEYPLDVEFEELFVFDEEEAEEEDEVILLEGDEIDLEELIEEELLLALPMKPLCPEDCKGLCEGA
NLNEGECGCEEEKIDPRWAALKKLKKKKE
>gnl|CDD|441010 COG1400, SEC65, Signal recognition particle subunit SEC65 [Intracellular trafficking, secretion, and vesicular transport]
MKDMKEIVIWPAYFDASLSRSEGRRVPRELAVEKPTLEEIAKAAKKLGLNPEVERDKKYPRRWWEKSGRV
VVEKDGSKSELLKKIAEKLKKLREKQ
>gnl|CDD|441011 COG1401, McrB, 5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms]
LLRPVLEFKFLIVGLRLKPLESEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEEL
SAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLE
LADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEET
LEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGGEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGKY
EPTPGIFLRFCLKAEKNPDKPYVLIIDEINRANVEKYFGELLSLLESDKRGEELSIELPYSGEGEEFSIP
PNLYIIGTMNTDDRSLALSDKALRRRFTFEFLDPDLDKLSNEEVVDLLEELNEILEKRDFQIGHRALLLL
DGLLSGDLDLLLLLLLLLLELLLLLLDKLDLLGMAEFEDRLELSEYLPLLLRASLED
>gnl|CDD|441012 COG1402, ArfB, Creatinine amidohydrolase/Fe(II)-dependent FAPy formamide hydrolase (riboflavin and F420 biosynthesis) [Coenzyme transport and metabolism]. Creatinine amidohydrolase/Fe(II)-dependent FAPy formamide hydrolase (riboflavin and F420 biosynthesis) is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
RLAELTWPEVEAALKEDDVAILPVGSTEQHGPHLPLGTDTLIAEAVAERVAERLPGVLVLPTIPYGVSPE
HLGFPGTISLSPETLIAVLRDIGESLARHGFRRIVLVNGHGGNVAALKEAARELRAEHPGMLVVVLNWWR
LAPPGLALSEGEETGGGHAGELETSLMLALRPELVRMDRAADGPPAGLPIGLLSRDLTPSGVLGDPTLAT
AEKGEALLEAAVEALVELLRELAAAP
>gnl|CDD|441013 COG1403, McrA, 5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms]
RRPGREWPALRRAVLKRDNGRCQYCGRPFSGDALEVDHIIPRSRGGTDTWENLVLLCRRCNRRK
>gnl|CDD|441014 COG1404, AprE, Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones]
LVAAALALVAALVAAALAAAAAAAAALAAALLVVLAAGVAVAAAAAALVAAAAAAAVAAALAAPLAPAAL
AAPAPLPVPAAAPAAVRAAQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDFVDG
DGDPSDDNGHGTHVAGIIAANGNNGGGVAGVAPGAKLLPVRVLDDNGSGTTSDIAAAIDWAADNGADVIN
LSLGGPADGYSDALAAAVDYAVDKGVLVVAAAGNSGSDDATVSYPAAYPNVIAVGAVDANGQLASFSNYG
PKVDVAAPGVDILSTYPGGGYATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAPGPY
YGYGLLADGAAGATSAGAGLAAAAGAAGAAAAATAAAVSVASAGAATAAADAAAGATAAALAAGSTGATA
AGLLAAAALSTLAAVAAAVVVTTGTSTEALVAVGGT
>gnl|CDD|441015 COG1405, SUA7, Transcription initiation factor TFIIIB, Brf1 subunit/Transcription initiation factor TFIIB [Transcription]
MSTTESEEEETSVCPECGGENLVTDTERGETVCEDCGLVVEEDVIDRGPEWRAFDSEERDERSRTGAPLT
LARHDKGLSTEIGWQDKDAYGKSLSGRKRRQLARLRKWQNRSRVSSSKERNLVQALSEIDRLASALGLPD
SVRETAAVIYRKAVEKGLLRGRSIEGVAAAALYAACRQAGVPRTLDEIAEVSRVDRKEIARAYRLLNREL
GLKVPPIDPIEYIPRIASELGLSEEVERRAREILEKAKEKGLTSGKNPAGLAAAALYLAALLLGEKVTQK
EVAEVAGVTEVTIRNRYKELLEALGIEVE
>gnl|CDD|441016 COG1406, CheX, Chemotaxis protein CheX, a CheY~P-specific phosphatase [Cell motility]
MKAELINPFIEATIEVLKTMLGLEVEVGKPYLKEDPVPSGDVSGVIGLTGDIKGSVIISFPEETALKIAS
AMLGEEVEEIDEMVKDAVGELANMIAGNAKTELSEKGYDIDISPPTVITGENHSISHPSGGPVLVIPFTT
EGGKFEIEVALEEGK
>gnl|CDD|441017 COG1407, COG1407, Metallophosphoesterase superfamily enzyme [General function prediction only]
MEIELAGETLVLLPEGALYWPAERTLVVADLHLGKESAFRRRGIPLPPYDTRETLERLEALIERTGPDRL
IILGDLFHDFGGPSRQEWEELERLLALHAGVEVILVRGNHDPGLPDLLEDLGGEVVDEELVLGGLLFRHE
PEPEAADGEIAGHEHPAVRLRDRVGRSLRLPCFLRDGRRLVLPAFGAFTGGLDVNPPAFSPLLRRGGAEA
YLLDGTRLGPLARL
>gnl|CDD|441018 COG1408, YaeI, Predicted phosphohydrolase, MPP superfamily [General function prediction only]
LALALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKIN
ALKPDLVVLTGDLVDGSVAELEALLELLKKLKAPLGVYAVLGNHDYYAGLEELRAALEEAGVRVLRNEAV
TLERGGDRLNLAGVDDPHAGRFPDLEKALAGVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIR
LPGIGALLTPVRLGRKYVAGLYREGGTQLYVSRGLGTSGPPVRFGCPPEITLITLKSA
>gnl|CDD|441019 COG1409, CpdA, 3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]
FRFAHISDLHLGAPDGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVV
PGNHDIRAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAK
PVIVFLHHPPYSTGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL
PPGYRVIEVDGDGLTVEVRRVDGG
>gnl|CDD|441020 COG1410, MetH2, Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]. Methionine synthase I, cobalamin-binding domain is part of the Pathway/BioSystem: Methionine biosynthesis
MGTMIQLLKLRELDADGAMFTDLQLDLKGNNDLLGLTGPNEILEIHRPELEAGADIIETNTGADAAITAA
DGAAEALLAEYNGAAAALALEAAAAAAAAAAAAARAVAGAPGPTGGTASPGPDVPGLGFRNFDFDELVEA
YAEAGLGLGGGGADLLLTETIFDTLNAAAAAAAAAAAAEEEGVPIPVMVTGTITDGSGRTLSGQTAEAFL
ESLGHAAPGSNGLNCALGAEELRPYLEELSRIPPSAVSNAPNAGLPNGFGEYDETPEEMAAALAEFAEEG
GVNIVGGCCGTTPEHIRAIAEAVAGLKPRPREKPPPAVLSGLEPVPIGQDSPFVNIGERTNVTGSKKFRE
LILEGDYDEALEVAREQVEAGAQILDVNVDEPGRDEVAAMVRFLNLLASEVRVPLMIDSSKPEVIEAGLK
CYQGKPIVNSISLEEGEERFEEVAPLAKKYGAAVVVLAIDEEGQADTAERKLEIAERIYDLAVEEYGFPP
EDIIFDPLVFTVATGIEEHRNYAVETIEAIRLIKEELPGAKTSLGVSNVSFGLPGNVREALNSVFLYHAI
KAGLDMAIVNPGQLEPYDDIPPELRELAEDVLLNRRPDALERLIELFEGVKGAKAKKADLEWRELPVEER
LKHAIVKGIKEGIEEDTEEALAEGARPLEIINGPLMPGMNVVGDLFGAGKMFLPQVLKSAEVMKAAVAYL
EPFMEKEKGESSSKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIG
LSGLMTTSLDEMKEVAEEMRRRGLDIPVLIGGAALTRAYTAVKIAPAYDGAVVYAKDASRAVRVADKLLS
KERREAFVAEIKAEYEKLRERHAARKKKLLSLEEARSNVDSDYPPPTPPFLGTRVLKDIPLAELVPYIDW
TPFFQQWGLKGKYLDGEEARELFPDAQAMLDRIIEEKWLTARAVYGYFPANSEGDDIEVYDDESSEELAR
FHFPRQQRGPNLCLADFVAPKESGERDYVGFFAVTAGIGIEELAAELEAAGDDYDAIMLHALADRLAEAF
AEYLHERVRKEWGYAPDEALTNEDLIKEKYRGIRPAPGYPACPDHTEKRKLFDLLDAERIGVTLTESFAM
HPEASVSGIYFHHPEAKYFNV
>gnl|CDD|441021 COG1411, COG1411, Uncharacterized conserved protein related to proFAR isomerase (HisA) [General function prediction only]
MRIIPVIDLKNGLVVHAKSGNRAEYRPIESPLCPSSDPLEVARALLELYGFRELYIADLDAIQGRGDNLE
VIRALAAPGLELWVDAGIRDPDDLLALLALARVRPVIGTETLDDLETLEELLAAPERIVLSLDFRGGQLL
GPDALWLDPEEILEELNELWPRRVIVLDLARVGTGSGPDLELLERLRARSPDHRLIAGGGVRDVEDLEAL
EKAGASGALVATALHDGRI
>gnl|CDD|441022 COG1412, Fcf1, rRNA-processing protein FCF1 [Translation, ribosomal structure and biogenesis]
VKVLLDTNALMMPAQFGVDVFEELDRLLGKYEFIVPEAVLEELEKLSRGAKGKEKRAARVALDLAERCEI
VETEGGYADDAILELAKENGVIVATNDKELRRRLLEAGIPVIYLRQKKKLLIT
>gnl|CDD|441023 COG1413, HEAT, HEAT repeat [General function prediction only]
VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEA
LGRIGDPEAVPALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRLG
>gnl|CDD|441024 COG1414, IclR, DNA-binding transcriptional regulator, IclR family [Transcription]
DRSGVQSLERALAILEALAEAGGGLSLSELARRLGLPKSTVHRLLATLEEEGYVERDPEGGRYRLGPRLL
ELGSAALRRLDLRRLARPVLEELAEETGETVHLAVLDGDEVVYVARVEGPRPVRVSSRVGSRLPLHATAS
GKALLAFLPEEELEALLARAGLPRFTPNTITDPAALRAELAEIRERGYAVDDGELEPGVRAVAAPVFDAD
GRVVAALSVSGPSSRLTEERLEELAPALRAAAREISRALGYRP
>gnl|CDD|441025 COG1415, COG1415, Uncharacterized conserved protein, DUF763 domain [Function unknown]
MMRTGIADLPLHGGHVPPWLFERMVRLGRAIVEAIVEEYGPDEVLRRLSDPFWFQAFGCVLGMDWHSSGI
TTVVLGALKEGLNPLSKELGIYVCGGKGKHSRKTPDELEALGERFGLDGEELVRASRLVAKVDNAAVQDG
YQLYHHSFIVTEDGKWAVIQQGMNEETRTARRYHWLSEGLKSFVEEPHTAIAGDKQGEVLNLTDRESAEA
RKAILDLLREGPDKILRELARLKAMLGATLQPALPHLYMPAHHDVRPSDVDLRRLEKVLRAAYERQPEDF
EELLLLPGVGPKTLRALALIAELIYGAPASFRDPARYSFAHGGKDGHPYPVPRKVYDETIEVLEEAVEKA
KLGRKEKLEALKRLSRLARRLERPA
>gnl|CDD|441026 COG1416, COG1416, Intracellular sulfur oxidation protein, DsrE/DsrF family [Inorganic ion transport and metabolism]
MRKFLLLLLALAAAAAAAAAAADAPYKVVFHVDSADPAKLNAALNNAANLLNAYGAPEDVEIEVVAHGPG
IKLLLKDNNPLAERIAALAEKGVKFVACGNTLKARGIDKDDLLPGVEVVPSGVVELAELQQEGYAYIKP
>gnl|CDD|441027 COG1417, COG1417, Uncharacterized conserved protein, DUF22 domain [Function unknown]
EMVRIVGRKGGIIKREKVKAEPYDFTRAHRGKWEPIIADEDVEVRAGEVKKIKIKEIEIPPNTIAVPCAY
ARHALGHVLDVGEEGPRPVEEERTIDHAYFLAVEDGEIKKGDLLGVLNLLPIMFTE
>gnl|CDD|441028 COG1418, RnaY, HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only]
LPELIKLVKYLRTSYGQHDLQHSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHEVEGSHAEIGA
ELARKYLESLGFPEEEIEAVVHAIEAHSFSGGIEPESLEAKIVQDADRLDALGAIGVARAFAIGGQAGRE
LRDPEDTAINHFYEKLLKLKDLMATELARDIAKKREEFMEEFPVTVIRETR
>gnl|CDD|441029 COG1419, FlhF, Flagellar biosynthesis GTPase FlhF [Cell motility]
MKIKKFVAKDMREALRKVKEELGPDAVILSTRKVKKGGFLKKVEVTAAVDEDEAEKAPAAAAAPAAASAA
AEEEELEELRRELAELKELLEEQLSGLAGESARLPPELAELLERLLEAGVSPELARELLEKLPEDLSAEE
AWRALLEALARRLPVAEDPLLDEGGVIALVGPTGVGKTTTIAKLAARFVLRGKKKVALITTDTYRIGAVE
QLKTYARILGVPVEVAYDPEELKEALERLRDKDLVLIDTAGRSPRDPELIEELKALLDAGPPIEVYLVLS
ATTKYEDLKEIVEAFSSLGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRVPEDIEVADPERLA
RLLLGGLEEEE
>gnl|CDD|441030 COG1420, HrcA, Transcriptional regulator of heat shock response [Transcription]
LDERQREILRAIVEDYIATGEPVGSRTLAKRYGLGVSPATIRNEMADLEELGLLEQPHTSAGRIPTDKGY
RLYVDSLLEVKPLSEEERRAIEAFLSQRAGDLEDLLQRAARLLSQLTNYAAVVLAPKLERARLKHIELVP
LSERRVLVVLVTDSGRVENRVIELPEGLSEEELEELSNYLNARLAGLTLSEIRERLLEELEQELAEYDDL
LRALLEALLEALSEEDEERLYVSGTSNLLRQPEFSDLEKLRELLELLEEKEVLLRLLDEAESAEGVQVFI
GSENGLEGLKDCSVVTAPYRVGGKVVGTLGVIGPTRMDYERVIPLVDYTARYLSRLLSK
>gnl|CDD|441031 COG1421, Csm2, CRISPR-Cas system type III CSM-effector complex small subunit Csm2 [Defense mechanisms]. CRISPR-Cas system type III CSM-effector complex small subunit Csm2 is part of the Pathway/BioSystem: CRISPR-Cas system
MSNDKKKKALGKLKDLDAKLLIDKAEEIGKELKNKKLTTSQIRKFYDEVKRIKNKVKQEELFEELLPELA
LLKPKLAYAAGREKEVKEFVEVLDKAIDKVKDSEDFFERFVDFFEAIVAYHKFYGGKE
>gnl|CDD|441032 COG1422, YidC, Archaeal YidC/Oxa1-related membrane protein, DUF106 family [Cell wall/membrane/envelope biogenesis]
MFLAMVGALLLMAGYSIPSIRNAIGGVLDVVLGPLLAFLPFYAVILILALLTGLYSTLIQKYLMDWEKMG
KYQERMKAFQKERREAQERGDDEALKKLQEEQMEMMGDQMGMSKEQFKPMVWIMVITIPIFLWLYWFIGN
GAVGHAEAVVVFPFAGEVNLTDGVLGPFPAWIVWYFLCSLAFSQIIRKALNIGMFPTK
>gnl|CDD|441033 COG1423, COG1423, ATP-dependent RNA circularization protein, DNA/RNA ligase (PAB1020) family [Replication, recombination and repair]
IKEVAEKLGLSEERLEKLLEKGKLRREEFEGIEYLRFRDDVRGIERGTVIFDDGEVVRGYPKIPRALVLE
PGLKKHFIGPVAVEEKMNGYNVRIAKIGGEILAFTRGGYVCPFTTDRARDLLDLEFFDDHPDLVLCGEMV
GPENPYVPHDYPEVDDLAFFVFDIRDKETGRPLPVEERRELAEEYGLPQVRLFGEFDPDDVEEIKEIIER
LDKEGREGVVLKDPDMRVKPLKYTTSYSNIGDLRYAFRFPFDLGRDFFFSRIVREGFQSVEFGESDEELR
ERALELGEAILEPMVEAIRKVAEGERVGERFTLRFRSPETAEEFLEHLRRLGVDIEIESDEREDGYWVVE
FRKVYPSTTDKIRSYLEGGLWPD
>gnl|CDD|441034 COG1424, BioW, Pimeloyl-CoA synthetase [Coenzyme transport and metabolism]. Pimeloyl-CoA synthetase is part of the Pathway/BioSystem: Biotin biosynthesis
EMLYSVKMRASKGHEKGGKHISGAERIVTEEELEEIVNALLERALNHSRGKPDFINIKVEKVDESDILYI
PPLPVKTIEVSSVEEGRKLARELLEKAGISEEAIEKAIELLKNGSNMRGAMLLDADSGERLEPDKERGVR
VSRMDWTPSAELKEALLRLGLGGNRFREALVLASKVASAPGIIAELCWSDDPDYTTGYVASKKLGYVRIT
NLKEKGSENGGRVFFVDGSRDIEKLIDYLEKQPVLVRGVG
>gnl|CDD|441035 COG1426, RodZ, Cytoskeletal protein RodZ, contains Xre-like HTH and DUF4115 domains [Cell cycle control, cell division, chromosome partitioning]
EALETIGELLRQAREAKGLSLEDVAERTKISVSYLEAIEEGDFDALPGPVYVRGFLRSYARALGLDPEEL
L
>gnl|CDD|441036 COG1427, MqnA, Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and metabolism]. Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) is part of the Pathway/BioSystem: Menaquinone biosynthesis
KLRIGAVSYLNTLPLYYGLERGGLLPDVELVKGVPSQLNRMLAEGELDVGLISSIEYARHADDYLILPDL
SISADGPVGSVLLFSRVPLEELDGKTVALTSESRTSVALLKILLAEYYGVRPEYVPGPPDLEAMLEGADA
ALLIGDRALRAAARGRFPYVYDLGEEWKELTGLPFVFAVWAVRRDAAEANPVAELHEALLEAKERGLAHL
DEIAEEAARRLGLPPELLEDYLRNLRYDLGEEERKGLRLFYEYAAELGLLPEVPELRF
>gnl|CDD|441037 COG1428, Dck, Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism]
MKPRYIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKD
LRQFGGNVVSDRSIYKDAIFAKLLHEMGTLSDREFDLYRQLFDNLTEDLPKPDLVIYLQASVDTLLERIK
KRGRDYEQNIDLDYLERLNEAYEEWFEHYDASPVLIIDTDELDFVNNPEDLELLLEQIEEKLKGR
>gnl|CDD|441038 COG1429, CobN, Cobalamin biosynthesis protein CobN, Mg-chelatase [Coenzyme transport and metabolism]. Cobalamin biosynthesis protein CobN, Mg-chelatase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
PELIDLYADKVLRVVRLLGGRRYWEYLLEALEEAKANGAPLVVLGGPDPELMSLSTVPPEVAARLWRYLA
EGGPENLRNLLRYLADTYLGTDVPYEPPVELPWEGIYHPDAPRVFEDLEEYLEWYATDPDRPTVGILFYR
SHWLAGNLAVVDALIRALEARGLNVIPVFCSSLRDEVVEEYFLEDGKPRVDALINTTSFSLGRPAAAAGV
ELLKKLNVPVLQAITSSSSREEWEASPQGLSPLDVAMQVALPEFDGRIITVPISFKERERDPDGVVRYVP
IPERIERVARRAARWARLRRKPNSEKKVAIILHNYPPGEARIGNAVGLDTPESVVRLLRAMKEAGYDVGN
LPESGDELIELLLAGGTNDGRWLTLEELVRKAAQLVPAEEYREWFATLPEAVREAVIERWGEPPGEIMVY
EGYIVIPGIRFGNVFVGVQPPRGFGEDPSAIYHDPDLPPPHQYLAFYRWLREVFGADAVVHVGTHGTLEW
LPGKSVGLSAECYPDIALGDLPNIYPYIVNNPGEGTQAKRRSYAVIIDHLTPPMTRAGLYGELAELEELL
DEYYEAKSLDPARLPALREQIWELAKELNLDKDLGLDEEPDDDEFDEFLEELHGYLCELKEAQIRDGLHI
FGEAPEGERLVELVVAILRLPNGDVPSLREALAAALGLDFDPLLADPGEPRRTNGDLVDELEELARELVE
ALLENGFDVAELLEELLGGANEDLRAVLLFICLELVPRLAQTTDEIDNLLRALDGGYVPPGPSGAPTRGR
PDVLPTGRNFYSVDPRAIPTKAAWEVGKKLADQLLERYLQEHGEYPESVGLSLWGTETMRTGGDDIAQIL
ALLGVRPVWDEASGRVTGLEVIPLEELGRPRIDVTVRISGFFRDAFPNLIELLDDAVRLVAALDEPDEQN
YVRKHVLEDLAELLAEGLDEEEAERRATYRIFGSKPGAYGAGVQLLIEAGNWEDDEDLADVYINWGGYAY
GKGVWGVPAPEAFERRLSRVDVTVKNQDSREYDLLDSDDYYQYHGGMTAAVRALSGKNPESYVGDSSDPD
NVKVRTLKEEIRRVFRSRVLNPKWIEGMKRHGYKGAFEMAATVDYLFGWDATTDVVDDWMYEEVAETYVL
DEENREFFRENNPWALQEIAERLLEAIQRGLWQADDEVLEELRELYLEIEGDLEEREGDE
>gnl|CDD|441039 COG1430, COG1430, Uncharacterized conserved membrane protein, UPF0127 family [Function unknown]
MLLALLLLALAAAALPTGELTINTAGLAIDVEVADTFEERARGLMFRKSLPEDEGMLFVFDEPRCRSFWM
KNTRFPLDIIFLDADGRIVSIAENLPPCSWTSYPSGGPARYVLELPAGWAARLGIKVGDRLEIEPLSS
>gnl|CDD|441040 COG1431, PIWI, PIWI domain, catalyzes dsRNA-guided hydrolysis of ssRNA, involved in RNA silencing, RNA metabolism and antiviral defense [Translation, ribosomal structure and biogenesis, Defense mechanisms]
IPKVPHAISVPTEVAFRVGVDVWRRLELVPSAILVVIRRAGIETREGLRNIGLLLDSWVADLGSFLLEID
RPVIDLKESPLDKVEISSDIAVILKENAYDKRRIALAKSGEEEVSRLRDYASILLLSLTFDEDRARGEKF
FRVLTNASTKKPVGDDLHPTARQLKVEKRLLADAKVDELPARLLLVYQSISLQNIISVGGSRLLAQRLEQ
VSLGKVRVRLIKLAIRRKVRDPKELRDSAQYLAKEKDRELFELDGRSRLKSFETEALKEEFLRKLSKKLK
SLSGIKLNIITKKSGPESKEALSEALKQLANEQGPDLVLVFIPQSDKADDDEESFDLYYEIKALLLRRGI
PSQFIREDTLKNSNLKYILNNVLLGILAKLGGIPWVLNEPPGPADLFIGIDVSRIKAGTQRAGGSAVVFD
SDGELLRYKLSKALQAGETIPARDLEDLLKESVDKFEKSAGLKPKRVLIHRDGRFCDEEVEGLKEFLEAF
DIKFDLVEVRKSGSPRLYNNENKGFDAPERGLAVKLSGDEALLVTTGVKTERKGTPRPLKIVKHYGQTSL
EDLASQILKLTLLHWGSLFPYPRLPVTIHYADKIAKLRLRGIRHPSKVEGDRLYFL
>gnl|CDD|441041 COG1432, LabA, NYN domain, predicted PIN-related RNAse, tRNA/rRNA maturation [General function prediction only]
KRVAVFIDGDNLYAAARDLGFDIDYEKLLEELAEYGRLVRARAYGDDTDERQQGFIDALRENGFEVILKP
LQQFRTSGKNAVDVELAVDAMELAYTPNIDTFVLVSGDSDFTPLVERLRERGKRVEVVGVEGKTSDALRN
AADEFIDLDDLREEILREPREREA
>gnl|CDD|441042 COG1433, NifX, Predicted Fe-Mo cluster-binding protein, NifX family [Posttranslational modification, protein turnover, chaperones]
MKIAIPSDGGSRVSPHFGRAPYFLIYDVEDGEIVLVEVIENPGEAGGGAGGLLAQLLAELGVDVVIAGGI
GPGALEALEAAGIKVYTGAEGTVEEALEAYLEGELEEA
>gnl|CDD|441043 COG1434, ElyC, Lipid carrier protein ElyC involved in cell wall biogenesis, DUF218 family [Cell wall/membrane/envelope biogenesis]
MLSKLLLLLLLLGRRRLLLLLALLLLLLLSPVGFWLLRPLERYADPPQPADAIVVLGGGVYDGRPSPVLL
ERLDAAARLYRQGPAPRIIVSGGQGPGEGVSEAEVMARYLLALGVPAERILLEDRSRNTWENARFSAALL
RERGIRRVILVTSAYHMPRALALFRRAGLEVIPAPTDFTSPPFLPSARALERSRLALREYLGLLWYRLRG
RL
>gnl|CDD|441044 COG1435, Tdk, Thymidine kinase [Nucleotide transport and metabolism]. Thymidine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
RRMGKLEFIYGPMFSGKSEELLRRAHNYEEAGQKVLLFKPAIDDRYGEGKIVSRIGLSREAIPVDDDTDI
LELVREGPDVDVVLIDEAQFLDPEQVDQLARLADRLGIPVICAGLDTDFRGEPFPGSPRLLALADEVTKL
KAICVVCGRKATMNQRLVDGGPAVYEGEQVLIGGNESYEARCRRHYREPMKE
>gnl|CDD|441045 COG1436, NtpF, Archaeal/vacuolar-type H+-ATPase subunit F/Vma7 [Energy production and conversion]. Archaeal/vacuolar-type H+-ATPase subunit F/Vma7 is part of the Pathway/BioSystem: A/V-type ATP synthase
KIAVIGDRDTVLGFRLAGIEVFVVEDPEEAEEALEKLLEDEDYGIIIITEDLAEKLPEEIRRYKEESVLP
LIVEIPDRHGSLGIPDSIRELVKRAIGIDIL
>gnl|CDD|441046 COG1437, CyaB, Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) [Signal transduction mechanisms, General function prediction only]
IEVEVKVRVIDLEEVRERLEELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRRGGGRATLTYKGPKLD
EGSKTREEIETEVDDGEAMEAILEALGFRPVATVEKTREIYKLGGVTVTLDEVEGLGPFVEIEGEAEDEV
EAAREAIEEVLAELGLDPDDIIRKSYLELLLEK
>gnl|CDD|441047 COG1438, ArgR, Arginine repressor [Transcription]
MKKAARQAKIKEIISEEEIETQEELVELLKEEGFNVTQATVSRDLKELGLVKVPNADGGYVYALPEEGGP
NPEERLKRLLRELVVSIDHSGNLVVIKTLPGAAQAVASAIDSLGLPEILGTIAGDDTILVIPRSEEDAEE
LAERLLKLLEGK
>gnl|CDD|441048 COG1439, Nob1, rRNA maturation endonuclease Nob1 [Translation, ribosomal structure and biogenesis]
MMMYVLDASAFIAGYPLDGELYTTPSVIEELKDIKSRLRLEALEGGGLRIREPDPESIEKVKKAARKTGD
LEELSKTDISVLALALELDATLVTDDYALQNVAKHLGIKVEPIATKGIKEVRKWRYRCTGCGREFDEPEE
ECPICGSPLKRKRKK
>gnl|CDD|441049 COG1440, CelA, Phosphotransferase system cellobiose-specific component IIB [Carbohydrate transport and metabolism]
KKILLVCAAGMSTSLLVKKMKKAAKERGIDVEIEAVSAGELEDVIDDYDVVLLGPQVRYMLDEIKKIADE
KGIPVAVIDMQDYGMMDGEKVLDQALELLK
>gnl|CDD|441050 COG1441, MenC, O-succinylbenzoate synthase [Coenzyme transport and metabolism]. O-succinylbenzoate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
MRHATLYRYSIPMDAGVILRNQRLKTRDGLLVRLQEGGREGWGEIAPLPGFSQETLEQAEQQALAWLQRW
LAGDLLDEKSLLPSVAFGLSCALAELEGELPEAANYRAAPLCSGDPDELIARLNQMPGEKVAKVKVGLYE
AVRDGMVVNLLLEAIPDLRLRLDANRSWTLDKAVQFAKYVNPEHRSRIAFLEEPCKTPEESREFARETGI
AIAWDESVREPDFRVEAEPGVAAIVIKPTLVGSLQRCRQLIEQAHQLGLQAVISSSIESSLGLTQLARLA
AWLTPDTAPGLDTLDLMQAQLLRPWPGSDLPLVALDSLEIVWQWT
>gnl|CDD|441051 COG1442, RfaJ, Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis]
MNKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVD
DELLKDLPVSKHISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTG
SQKKRAKRLGLPDDDGYFNSGVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLP
PRYNYQYSLYYELKDKSNKKELLEARKNPVIIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKA
LRYKQLRKKAKHLRYLKGIKN
>gnl|CDD|441052 COG1443, Idi, Isopentenyldiphosphate isomerase [Lipid transport and metabolism]. Isopentenyldiphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
EELVDLVDEDGRPIGTAERAEVHRKGLLHRAFSVFVFNSDGRLLLQRRALTKDHWPGLWDNTVCGHPRAG
ETYEEAAVRELEEELGITVDDDLRPLGTFRYRAVDANGLVENEFCHVFVARLDGPLTPQPEEVAEVRWVT
LEELLALLEAGPEAFTPWFRLY
>gnl|CDD|441053 COG1444, TmcA, tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]. tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification
LDLLRALRAEARRAGHRRLLVLSGDDEWCRAQAEALLEALPGDWLWVGERPPLGVEHIPPSAARRLLGRE
FDHVVFDAHDGFDPNALGALSGTVRGGGLLVLLTPPLDEWPQRPDPDSLRLAVPPEPIVTPRFIRRLQRK
LREHPGVAIWDQDSPLIDPELPAKARFPRPAYEGCLTADQAAALAALERLAERKRVLVLTADRGRGKSAA
AGLAAARLAAEGGRVLVTAPSKAAVEELFEFAGELLEALGVKYRELTGAGGRVRFVAPDALLERPPDADL
LLVDEAAAIPVPLLEKLLAAFPRVVFTTTVHGYEGTGRGFLLRFCARLDESTPGWRELTLDEPIRWAAGD
PLERWLFRALLLDAEPAVLQLVDAPPGEVEYERLDQDELLADEELLRQLFGLLVLAHYRTSPDDLRRLLD
APNQHFRALRTGGKVVGVAWLAEEGGLDAELAEAVWAGRRRPRGNLVPQSLAAHLGLPEAATLRGWRIVR
IAVHPALQRRGLGSRLLAEIREEAKEEGLDWLGVSFGATPELLRFWQRNGFVPVHLGTTRNASSGEYSAM
VLKPLSEAGEALVDRAARRFARDLPNLLSDPLRDLDPDVARALLRALPADADPELSDEDWRELAGFAFGH
RPYEASLDALRRLLLAYLLDPRADLSPREERLLVAKVLQGRSWEEVAEELGLSGRKALLRALRDAVAQLL
DAY
>gnl|CDD|441054 COG1445, FrwB, Phosphotransferase system fructose-specific component IIB [Carbohydrate transport and metabolism]
KIVAVTACPTGIAHTYMAAEALEKAAKELGHEIKVETQGSVGVENELTAEDIAAADAVILAADIEVDMER
FAGKPVIEVSVKDAIKDPEALIEKALAAA
>gnl|CDD|441055 COG1446, IaaA, Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism]
MKMSRRALIIHGGAGTIARSAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNA
GKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLEL
VDPLYFFTEKRWKQWKKALEYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAG
TYADNEVGAVSATGHGEYFIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKLGGDGGLIAVDKDGNIAA
PFNTEGMYRAYIDGDGELVVAIYKD
>gnl|CDD|441056 COG1447, CelC, Phosphotransferase system cellobiose-specific component IIA [Carbohydrate transport and metabolism]
EEIAMEIILHAGNARSLAMEALKAAKEGDFEEAEELLKEADEELLEAHKVQTELIQKEAGGEKVEVSLLL
VHAQDHLMTAMTEKDLAKELIELYKKLEKL
>gnl|CDD|441057 COG1448, TyrB, Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]. Aspartate/aromatic aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
MFEHLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETETTKSYLPIEG
DAAFNDAVQKLLFGADSPAVAAGRVATVQTPGGTGALRVGADFLKRAFPDATVWVSDPTWPNHRAIFEAA
GLEVKTYPYYDAETGGVDFDGMLADLKQLPAGDVVLLHGCCHNPTGADLTPEQWQEVAELLKERGLIPFL
DIAYQGFGDGLEEDAAGLRLFAEAGPEFLVASSFSKNFGLYRERVGALSVVAADAEEADRVLSQLKALIR
TNYSNPPDHGAAIVATILNDPELRALWEAELAEMRERIKAMRQQLVDALRAKGPSRDFSFIARQRGMFSY
LGLSPEQVDRLREEFGIYMVGSGRINVAGLNESNIDYVAEAIAAVL
>gnl|CDD|441058 COG1449, COG1449, Alpha-amylase/alpha-mannosidase, GH57 family [Carbohydrate transport and metabolism]
MAKPLYVVFYWHMHQPYYRDPYFGDYLNPWVFLHVAKDCYLPMAAILLEYPKFKVTFNISPTLLEQLEDY
IPEVIPRYRELAETGQVELLAEPYYHPIAPLLLDFGDPEDFREQVKMHRELFKELFGVKPTGFWNTELAV
SDEILELLAEMGFKWIATEGAVLVRSLGWRSPNYLYRPYRVEGGSGLKLLFRDYRLSDDIGFRFSNWSYP
LAADKFASWLEAIPRGEGPGDVVNIALDGENFGEHYPNNGYEFLRALYQALSEHPGIEFVTPSEVLEKFP
PVDELELPPQLPTGSWADGDFSTWIGNPMQNEAWDLLYEAREAVRAAGEADEEQRALALEDLRYLEGSDW
FWWMGTKHFSDGEVHSYFDQLFRKHLASPYRLLGEPSPYDLIPAFINYMGVLRDFQERVF
>gnl|CDD|441059 COG1450, PulD, Type II secretory pathway component GspD/PulD (secretin) [Intracellular trafficking, secretion, and vesicular transport]
AAAAEPVTLNFRDADLRDVLRALYADAEDLAKVLRSLLGGAAGVSVVADPRTNSLIVRATPEQLREIEEL
IEQLDVPRRQVLIEAKIVEVSLSDLRELGIDWSALGGNGGGVNFGGTGSLGSLAAAGSLGGGLNLGLLGG
GNFGALLNALESNGDANVLSSPSILTLNNQEAVIKVGQTVPYVTGSTTTSSTGNPTTTIEYVDVGITLKV
TPQINEDGTVTLDINPEVSSVTGSTTGGGNGLPTINKREISTTVRVKDGQTVVLGGLIRDEESESESKVP
LLGDIPLLGRLFRSTSKSKEKTELVIFITPTIIRDGEDAQALTEEYDRLRALQ
>gnl|CDD|441060 COG1451, YgjP, UTP pyrophosphatase, metal-dependent hydrolase family [General function prediction only]
MSLLTRTILLGGREIPYELRRSKRKRLRLRVPPDGRVRVTAPLRVSLAEIEAFVRSKADWILKKLARLRE
RARQPPREFVDGESLPYLGRRYRLRVVEGARGSVRLDGGRLLVPVPGGDPEQIRRALEDWYRRQARELLP
ERLARYAARLGVKPPRVRIRDMKTRWGSCSSKGRIRLNWRLIMAPPEVIDYVVVHELAHLREMNHSPRFW
ALVERLMPDYRERRKWLKENGAALHR
>gnl|CDD|441061 COG1452, LptD, LPS assembly outer membrane protein LptD (organic solvent tolerance protein OstA) [Cell wall/membrane/envelope biogenesis]
AQDAAQALSVPDLAPDDDAPVLIEADSLEYDQDDGTVTAEGNVEIRQGDRRLKADRVTYDQKTGTVTAEG
NVRLTDGGNVLTGDEAELNLDTKDGFIENARYQLVDRGGRGAAERIKRTGDNRTRLENATYTTCPPGDPD
WQIRASRIILDQEEKVGTARNARLEIKGVPVFYLPYLSFPDPDKRKSGFLIPSFGSSSRLGFELSLPYYW
NIAPNYDATLTPRYMSKRGLQLGGEYRYLFKSGSGELSIRGEYLPDDRLGDNDDRGLLRWQHSFDLNKGW
RFGADVNRVSDDDYLRDFDSSLGSSSDDYLTSSASLSRTYGDNWNLSLRAQHFQTLRDSDDDSPYQRLPQ
LDFNYVYRPLLGGEFSLDAEATNFTRDDSDFQDGPDGTRLHLEPSWSLPLSRPGGLFLTPKAGLRATAYQ
LDNDSDPDTLDGSVSRVLPTFSLDSGLPFERDFSLGGGGTQTLEPRLQYLYVPYRDQSDIPNFDSALLDF
DYANLFSDNRFSGYDRIEDGNQLTLGLTSRLLDKDGGRERLRLSVGQSYYFADQRTLADDSGSTKLSDLV
AEASLRPNDGLSLTARAQYDPYTGRVNRGNAGLRYRPDRRNLNLGYRYLRDDPDYGYSDDIEQLDLSGSW
PLTDNWSVVGRYRYDLTDNRLVETLLGLEYDDCCWALRLVYRRYYTSGSDLEYDTSFFFQLELKGLGSLG
SN
>gnl|CDD|441062 COG1453, COG1453, Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]
MQYRRLGKTGLEVSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGYGDSEEFLGKALKGPRDKV
ILATKLPPWVRDPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKPGGALEALEKAKAEGKIRH
IGFSTHGSLEVIKEAIDTGDFDFVQLQYNYLDQDNQAGEEALEAAAEKGIGVIIMKPLKGGRLANPPEKL
VELLCPPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADNLEPLTEEELAILERLAEELGELLK
DFCTGCGYCMPCPQGINIPEVFRLYNLARAYGMREYAKERYNALGPGAKASACIECGACEERCPQGLDIP
ELLKEAHELLGGLPV
>gnl|CDD|441063 COG1454, EutG, Alcohol dehydrogenase, class IV [Energy production and conversion]
MMFTFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPN
PTVETVEAGAAAAREFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAG
TGSEVTPFAVITDPETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPL
TDALALEAIRLIARNLPRAVADGDDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLAN
AILLPHVLRFNAPAAPERYAEIARALGLDVGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPE
LAELALADRCLANNPRPLTEEDIEAILRAAY
>gnl|CDD|441064 COG1455, CelB, Phosphotransferase system cellobiose-specific component IIC [Carbohydrate transport and metabolism]
MNKFIDFLEKKLMPVAAKIGNQRHLRAIRDGFISTMPLIIVGSLFLLIANLPIPGWADFMAFGEPWAAIL
GIPYNGTFGIMSLFVAFGIAYSLAKSYKLDPLSAGLLSLAAFLILTPFTVDDTGVIPTSYLGAQGLFTAI
IVGLLSVEIYRFLIKKNITIKMPDGVPPAVSRSFAALIPGLIILIIFWIINLLLQFTTGTDLPELIYTLL
QAPLVSLGDSLPGVLLIVFLIQLLWFFGIHGANIVGPILQPIWLANLAENAAAFAAGQALPHIITEQFFD
VFVLIGGSGATLGLVIALLLFSKSKQLKAVGKLSLVPGIFNINEPIIFGLPIVLNPILFIPFILAPLINA
TIAYFATALGLVPPPVVLVPWTTPPPIGAFLATGGDWRAAILQLVNLVISVLIYYPFFKAYEKQLLKEEK
EEA
>gnl|CDD|441065 COG1456, CdhE, CO dehydrogenase/acetyl-CoA synthase gamma subunit (corrinoid Fe-S protein) [Energy production and conversion]
MALTPLEIYKLLPKTNCKECGEPTCMAFAMKLAKGKAKLEDCPPLSEEALEKLEEALAPPIREVKIGTGD
KAVKIGGETVLFRHEKTFFNPTAIAIDVSDTMDEEEIDERVKKINKFKFERVGEKLKLDMVAVRNSGDPE
KFAAAVKKVAETDLPLILCSEDPEVLKAALEVVADRKPLLYAATKDNWEEMAELAKEYKVPLAVKAPDLE
ELKSLVEKLQALGYKDLVLDPGGRNLKDTLANFTQIRRAAIKGDRPFGYPIIAFPNEEDPYWEAVLASVF
IAKYADIIVLHDLEPWALLPLLTLRQNIYTDPQKPVAVEPGIYEIGNPDENSPVLITTNFALTYFTVEGD
IESSKVPCYLLVVDTDGLSVLTAWAAGKFTAEKIAKFIKESGIEEKVKHRKLIIPGLAAVLSGDIEELTG
WEVLVGPRESSGIPAFLKKLWP
>gnl|CDD|441066 COG1457, CodB, Purine-cytosine permease or related protein [Nucleotide transport and metabolism]
MSTTSRRSNRAETVEDYGLEPVPESERHGSPRSLFWVWFGANVALATFVIGALLGLGLGFWQALLAILLG
NLIGFLLGALIAYIGARTGLPTMLLSRAAFGYRGSTLPSLLNALTTIGWFAVEAAIAAQALAALLGGLGI
PLVLAYLIVGLLVILLAIFGYRAISRLQRWAVPLLLVLFVLLVVLALSHPGLSALLAYPPGSSPLSFGAA
VSVVAGLFISWAPYAADYSRYLPRKTSGRAVFWATFLGFVLGGVLLMLLGALLAAAAPGAADPVGALGAL
LPTGLGVPALLVVILSQWTINVLNLYSASLALSNLFPRLGRVVATLVVGVIGTLLALLGFLDAFENFLLL
LGVVLPPWGGIMLADYFLVRRGRYDPDALFDRRGRYGGVNWVGLIAWLLGSVVGILFVNTPGLFGPALAD
LSWLVALVVAAVLYLLLARYYLARPEAA
>gnl|CDD|441067 COG1458, COG1458, Predicted RNase MK1237, contains PIN domain, UPF0278 family [General function prediction only]
MLKQRFVLDTSAFTDPELREVLGDETLEEAVRRILDLIARARLKLGISCYMPPSVYNELMRFLERNGCPE
EVIAKLDTWIVKKTPDRYEVKIPAEIFYEYVEEMRERINKGLRVAEEAVREAAEEGLELLSKEEEIEREE
IGKIIRKLREKYREALRKGILDSAEDLDVLLLAKELDAAVVTSDEGIIKWAEKLGLRFVDARTFPTMLEE
YLRHVKREE
>gnl|CDD|441068 COG1459, PulF, Type II secretory pathway, component PulF [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
PTFRYKALDADGKKVKGEIEADSEAEARAQLREQGLTPLSVKEKKEGLAARLFRRKVKAKDLALFTRQLA
TLLRAGLPLLEALEILAEQTENPRLRKVLADIREDVEEGASLSEALAKHPKVFPPLYVNMVRAGEASGNL
DEVLERLADYLEKQEELRKKIKSALIYPAIVLVVAIGVVLFLLTFVVPQFAGIFESFGAELPLLTRILIA
LSDFLQNYWWLLLLGLVLLVVGFRRLLRTPKGRLRLDRLLLKLPVIGPLIRKAALARFARTLATLLSSGV
PLLEALEIAAEVVGNRVLREALEEARERVREGESLSEALEASGLFPPLVVQMIAVGEESGALDEMLEKVA
DFYEEEVDRAVDRLTSLLEPLLIVVLGGIVGFIVLAIYLPIFSLGSLVG
>gnl|CDD|441069 COG1460, RpoF, DNA-directed RNA polymerase, subunit F [Transcription]. DNA-directed RNA polymerase, subunit F is part of the Pathway/BioSystem: RNA polymerase
MIVKEILEEEYLTLPEAKEILEKIEEERAEDEELSYELRRTIEYLNKFSKLDPEKARELVEELVELEGLK
EETAVKIANILPRTRDELRAILAKERYTLSEEELDEILEIVKKY
>gnl|CDD|441070 COG1461, YloV, Predicted kinase related to dihydroxyacetone kinase [General function prediction only]
IDGKALRRMFRAAAANLEANKEEINALNVFPVPDGDTGTNMLLTMRSAAKELEKLESDSVGEVAKALARG
ALMGARGNSGVILSQLLRGFAKGLEGKEELDAADLAAALQRAVETAYKAVMKPVEGTILTVARAAAEAAE
EAAKETDDLAEVLEAAVEAAKEALARTPELLPVLKEAGVVDAGGQGLVVILEGFLAALTGEEIEEPEEAS
ELEELVNAVHEPSAQAHIETEDIEFGYCTEFLLKGDEFDVEELRARLSELGDSLVVVGDDDLVKVHVHTN
DPGAVLEAGLKYGRLHKIKIDNMREQHEEILEKEEEAAEEPKKKRGVVAVAAGDGLAELFKSLGVDVVIE
GGQTMNPSTEDLLDAIESVNAEEVIVLPNNKNIIMAAEQAAELARDKKVVVIPTKSIPQGLAALLAFDPE
ASLEENVEAMTEAAAAVRTGEVTYAVRDTLIDGGEIKKGDVLGLVDGEIVVVGKDLEEVALKLLDRMLDE
DGELVTILYGEDASEEEAEALAEHLEEKYPDVEVEVYDGGQPLYPYLISVE
>gnl|CDD|441071 COG1462, CsgG, Curli biogenesis system outer membrane secretion channel CsgG [Cell wall/membrane/envelope biogenesis]
MKKSILALLLLALLALLLAGCATTESSTPVEVEPPVLANATPYAQDLVALPYPGPKPRVAVGDFDDQTGQ
NGSSGSDAVGQGASDMLITALQQSGRFTVVERENLSNLLAERKLAGSGRIRAGTAAQLGQLLGADYLITG
GITEFDRNTSGGGGGARLFGIGGSGKYQVAYVTVDLRLVDVRTGEVVYSVTGSGEISSSEVSAGGFGFVG
GGLLEAGTGGYDNTPNGKAVRAAIEEAVNNLVAGLEAGAWRPADLAVSGGQVV
>gnl|CDD|441072 COG1463, MlaD, Periplasmic subunit MlaD of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis]
MRRRSRELKVGLFVLVGLALLVGLALWLGGLGLFGDTYTYTAVFDDVGGLKVGSPVRYAGVKVGRVTSIE
LDPDGYRVRVTLRIDPDVPIPADSVATIRSSGLLGEKYVELSPGGDSGPPLADGDVIPLESPVDLEDLLS
QLSPLLEALDPGALLDNLNTLTDTLADAAAQLDALLDNLNTLSDTLAERRDDLRALLASLNALSAQLDGL
LADNRGTLGKLLANLEALLDNLARTSDNLEELLEDLERNPAALLFGPKLP
>gnl|CDD|441073 COG1464, NlpA, ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion transport and metabolism]
MKKLLALLLALALALALAACGSSSAAAAAADKKTIKVGATPGPHAEILEVVKPELAKKGIDLEIVEFTDY
VQPNEALADGEIDANYFQHIPYLDNFNKENGYDLVPVGKTHIEPMGLYSKKYKSLDELPDGATIAIPNDP
TNQGRALLLLQKAGLIKLKDGVGLLATVKDITENPKNLKFVELDAAQLPRSLDDVDAAVINGNYALEAGL
DPTKDALFLEDKDSPYANIIVVREDDKDDPAIKKLVEAYQSDEVKKFIEEKYKGAVVPAW
>gnl|CDD|441074 COG1465, AroB2, 3-dehydroquinate synthase, class II [Amino acid transport and metabolism]
MMKEVWIKADGGDEERKARVTAALESGVDGVLVDEEDVERVRELGRVKVVAEDPDGDIVVADLSTLRRKG
GEDGAYVEITDKEDEEFAAELAKAADYVIVEGEDWTIIPLENLIAQLQGSETKLIAGVKDAEEAELALGT
LEKGVDGVLLDPDDPAEIKKTVRLLKAEREKLELVEATVTSVEPVGMGDRVCVDTCSLMEPGEGMLVGSS
SSGLFLVHSETEESPYVASRPFRVNAGAVHAYVRVPGGKTRYLSELKAGDEVLIVDADGNTREAIVGRVK
IEKRPLLLIEAEVDGKKISTILQNAETIRLVGPDGKPVSVTELKPGDEVLVYVEEGGRHFGMAVEETIIE
K
>gnl|CDD|441075 COG1466, HolA, DNA polymerase III, delta subunit [Replication, recombination and repair]
KKLAPVYLLYGEEPLLIDEAADALRAAALAEDDGFNRTRLDGAETDWAELLDEAQTLSLFGERRLVIVRN
AEFLKKPGEGLEALEAYLANPPPDTVLVLTAGKLDKRKKLFKALEKAGVVVECYPLKERELPAWIRQRLK
AAGLRIDPDAAQLLAERVGGDLLALAQELEKLALYAGDGGTITLEDVEALVGDSAEFNVFDLADALLAGD
AARALRILRRLLAEGEEPVLILAALARQFRLLLQVKALLAQGKSLAEIAKELGVPPFRVKLALRALRRWS
LERLARALQLLAEADLALKGGAADP
>gnl|CDD|441076 COG1467, PRI1, Eukaryotic-type DNA primase, catalytic (small) subunit [Replication, recombination and repair]
MDEKTREFLKGRFRDYYRRADLELPPDLEEREFGFIPFDDTTMVRHLSFKSLGELRDFLVRNVPRHVYYS
AAYYEDPGAPTMEEKGWLGADLIFDLDADHLPGCDPVSMSYAEMLEAAKDEALKLLDFLEDDFGFDEDDI
KIVFSGGRGYHVHVRDEDVRELGSDERREIVDYVRGIGLDIERLGRRSPPLPTDGGWRGRVARELIELLD
ELRELKDALERLTSLDGIGEGRAETLLGALRIEALRSGNVDVGPVVRRLFEELLEDVVEELSAEIDEPVT
TDIHRLIRLPGSLHGKSGLRVVPLTRDELDDFDPLVDAVVFGDREVKVEVTKPPKVELLGESFGLEEGEV
EVPEYAAVFLMCRGVAEIAGE
>gnl|CDD|441077 COG1468, Cas4, CRISPR/Cas system-associated exonuclease Cas4, RecB family [Defense mechanisms]. CRISPR/Cas system-associated exonuclease Cas4, RecB family is part of the Pathway/BioSystem: CRISPR-Cas system
TEEDMKITGSAIQYYLYCPRKLWLIHVIGLEWEENERVALGRLLHERVYKRLERLRREVPLDSERLGLTG
KIDLVEFEDGELVPVEYKKSKPKPWEADRMQLCAYALLLEEMLGIPVPKGYLYYPEERKREEVELTEELR
EEVEEAIEEIREILESEKPPPPTKSKKKCKKCSYREFCLPRETS
>gnl|CDD|441078 COG1469, FolE2, GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]. GTP cyclohydrolase FolE2 is part of the Pathway/BioSystem: Folate biosynthesis
TLPDVQSSPDDRNIPLDRVGIKGVRLPVRIADKDGGPQHTVATFDMYVDLPADQKGTHMSRFVEVLDEHL
EEALSVESLEALLEEMAERLYAERAEVEMRFPYFIRKKAPVSGLSGLEDYDVTLEAELDRDGEFRKTLGV
EVPVTSLCPCSKEISRQLAQERGIPYGAHNQRSHATISVELDEDEDVWIEDLIDLAESAASTPVYTLLKR
PDEKAVTELAYENPKFVEDAVRDVAAALVEDPRIADFRVEVENFESIHNHDAYAEIERDKR
>gnl|CDD|441079 COG1470, COG1470, Uncharacterized membrane protein [Function unknown]
VAAAGLVASSTVAAGALAALLDLTTPLVGSTVALTSTASALSGERTTLAALAATGGLVTATPVSPTSATL
TLSVEVPSNATVGTYLPITVTVAPYGLTLSVESPSLEVAPGETVTYTVTLTNTGDEPDTVSLSAEGLPEG
WTVTFTPDTSVSLAPGESKTVTLEVTPPANAEPGTYPVTVTATSGEDSSSASLTLTLTVTGSYELELSST
PTGRTVTPGESATFTVTVTNTGNGADLTNVTLSASAPSGWTVSFEPETIPSLAPGESATVTLTVTVPADA
TAGDYTVTVTATSDETASATLRLTVETSSLWGWIGYLIRKYGGLGATGSLLVASVSLVVGAVVGTLTTPL
LLTGFAGNGLLSAATAPLLLLLGLTLSLLSDVLVFTVGSAGVSAAAATAETSALTALGVGATGAVGSGSA
SASVKVTGGAAVATGLTDATTLPGAGSTATLALPGGGGITSTLSLGTLPLGGSTT
>gnl|CDD|441080 COG1471, RPS4A, Ribosomal protein S4E [Translation, ribosomal structure and biogenesis]. Ribosomal protein S4E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
GGSRHLKRLAAPKFWPISRKEYKWTVKPSPGPHPKERSIPLLVVLRDVLKYADTAREAKKIISEGKVLVD
GRVRKDYKFPVGLMDVISIPKTGEYYRVVPDEKGRLKLIPISEEEAKLKLCKIENKTTVKGGKIQLNLHD
GRNILVDVENDYKTGDSLVISIPEQEILDHIPFEEGNLALIVGGKNAGEIGKIVEIKKGKGSKPNTVTIE
DKDGEKFETIEDYVFVIGEEKPVIKLGEE
>gnl|CDD|441081 COG1472, BglX, Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism]
MTLEEKIGQLFQVGVTGEGAELIREGHVGGVILFDPAQWAELTNELQRATRLGIPLLIGTDAEHGVANRP
AGGATVFPQAIALAATWDPELAERVGRAIAREARALGINWNLAPVVDINRDPRWGRNFESFGEDPYLVGR
MAAAYVRGLQGNGVAATAKHFAGHGDEETGRHTGPVDVSERELREIYLPPFEAAIKAGVASVMTAYNALN
GVPATLSKWLLTDLLRGEWGFDGLVVSDWGAMGGLAEHYDPAEAAVLALNAGLDLEMPGGKAFIAALLEA
VESGELSEERIDEAVRRILRLKFRLGLFDDPYVDPERAAEVVGSPEHRALAREAARESIVLLKNDNGLLP
LAALAAGGALAADAAAAAAAAAAAAAAAAAAAAAAAAAALLEAAAGADAALALAAAAAALLLVAAAALVA
VVALAAALAVLLLLVLGVAVGVGAVLLAGGGGAAAAAAGGGGG
>gnl|CDD|441082 COG1473, AbgB, Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]. Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
KILALIDALAPELIALRRDLHAHPELSFEEFRTAAYVAEELRELGIEVTTGVGGTGVVAVLKGGKPGPTI
ALRADMDALPIQEQTGLPYASKNPGVMHACGHDGHTAMLLGAAKALAELRDELKGTVRLIFQPAEEGGGG
AKAMIEDGLLDRPDVDAIFGLHVWPGLPVGTIGVRPGPIMAAADSFEITIKGKGGHAAAPHLGIDPIVAA
AQIVTALQTIVSRNVDPLDPAVVTVGIIHGGTAPNVIPDEAELEGTVRTFDPEVRELLEERIERIAEGIA
AAYGATAEVEYLRGYPPTVNDPELTELAREAAREVLGEENVVDAEPSMGSEDFAYYLQKVPGAFFFLGAG
NPGTVPPLHSPKFDFDEKALPIGAKALAALALDLLA
>gnl|CDD|441083 COG1474, CDC6, Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]
MIFEDLLWDESIFRDREVLSPDYVPDRLPHREEEIEELASALRPALRGERPSNVLIYGPTGTGKTAVAKY
VLEELEEEAEERGVDVRVVYVNCRQASTRYRVLSRILEELGSGEDIPSTGLSTDELFDRLYEALDERDGV
LVVVLDEIDYLVDDEGDDLLYQLLRANEELEGARVGVIGISNDLEFLENLDPRVKSSLGEEEIVFPPYDA
DELRDILEDRAELAFYDGVLSDEVIPLIAALAAQEHGDARKAIDLLRVAGEIAEREGSDRVTEEHVREAR
EKIERDRLLEVLRGLPTHEKLVLLAIAELLKDGEDPVRTGEVYEAYEELCEELGVDPLSYRRVRDYLSEL
EMLGLIEAEVSSKGRRGRTREISLSVDPEVVLEALEEDL
>gnl|CDD|441084 COG1475, Spo0J, Chromosome segregation protein Spo0J, contains ParB-like nuclease domain [Cell cycle control, cell division, chromosome partitioning]
MKEGEEIREIPIDKIVPSPYNPRRTFDEEALEELAASIREHGLLQPILVRPLGDGRYEIIAGERRLRAAK
LLGLETVPAIVRDLDDEEALELALIENLQREDLNPLEEARAYQRLLEEFGLTQEEIAERLGKSRSEVSNL
LRLLKLPPEVQEALREGKLSLGHARALAALSDPERQEELAEKIIEEGLSVRETEELVKALAKDLARLERR
LSELGTKVKIELEKKGKISLEDLDRLLERLG
>gnl|CDD|441085 COG1476, XRE, DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription]
MKKKLGNRLKELRKERGLTQEELAELLGVSRQTISAIENGKYNPSLELALKIARALGVSLEELFSLEE
>gnl|CDD|441086 COG1477, ApbE, FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones]
MGTTVSITLYGPDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERAL
EISELSDGAFDPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGG
IAKGYAVDRAAELLRAAGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPRDPGAVLAVLELSDGAVATSG
DYERYFEIDGKRYSHIIDPRTGYPVEHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLPGLEAL
LIDRDGKVFASPGF
>gnl|CDD|441087 COG1478, CofE, F420-0:Gamma-glutamyl ligase (F420 biosynthesis) [Coenzyme transport and metabolism]
MSLEVIPVKGLPEIRPGDDLAALIAEALPAAGLRDGDVLVVASKIVSKAEGRLVDLADVTPSERAIELAK
KYGKDPRRVELILRESDRVVAERGPTLIVETRHGFVCANAGIDASNVPGGTVLLLPEDPDASARRLRAGL
RERTGKRVGVIITDTFGRPWRLGQTGVAIGAAGIPPLRDYRGKKDLFGRELEVTVIAVADELAAAANLVM
GEADEGTPVAVVRGLPVLVDDGPGARELVRPPEEDLFRLGLREAL
>gnl|CDD|441088 COG1479, GmrSD, DNAse/DNA nickase specific for phosphorothioated or glycosylated phage DNA, GmrSD/DndB/SspE family, contains DUF262 and HNH nuclease domains [Defense mechanisms]
IKATEKSLGELLSGNGRFVIPDYQRPYVWTEEQVEDLLDDILRGFENNDSEYFLGSIVLWETDNETAGVG
KYEVIDGQQRLTTLTLLLAALRDLLKEDGDAKDIERLYLLNKEPEEERYKLELSEEDREWFPDLLDGESP
ETDSQRNLLEAYEFFEERLEELLEELEALLDYLLYKLPVVEIELEDEDDAYEIFETLNSRGKPLSPADLL
KAYLLARLDEDDLYREYWDPIEEELGEDDFLRHYGLLELLEELEELLEDLLLLLLLLLLLELLELLLLLL
LLLLLLLLALGLLLLDLLLLELLLLLLLELLELLLLLLLAALLLLLLLLLLLLLALLLLLLLAELLLLLA
LLSIALLLLLLLLLALLLVLLLILLALLELLLELLSRELLLLLALLLLLISALLLRLALTLLLLLLALDL
VLLLLLLLLLLSLLLKDLLLLLLLLLLLLLLLLIKALLLALEALDLLKLLRLSLLLLLKLLLSLLLLNLL
LNLLLLASLKKALDLLELLLLLLAEEAEPLLLLLLLGALLAALRELLLLALNAA
>gnl|CDD|441089 COG1480, PgpH, Cyclic di-AMP-specific phosphodiesterase PgpH, HD superfamily [Signal transduction mechanisms]
MKKLLKRLLKKQSKLYRLLLFLLFVLLLTLLLFPKVGPFKYDLQVGQIAPEDIVAPRDFSYEDEEATEEE
REEAAESVPPVYDLDPEVAEEVLEKLEELFDAIREIRSDAELSLEEKVAELKERLGLSLSDEELETLLSL
SDEDLQKLKEEILQILEEIYSEGIREDDLETAREELRSQLESSDLSSELRNLLVELLRQLLKPNLVYDEE
ATEKAREEAAAAVEPVRGTIKKGEVIVRKGEVVTEEQYEKLESLGLLRESGNNWLILLGLALLVLLLLLL
LLLYLRRFRPEILRNNKKLLLLALIILLTLLLAKLVSLIDSLLPYLVPVAAAPMLLAILFDARLALFVSV
LLALLLGFIVGNSFEFLLLQLIGGIVAILSVRRLRRRSDLFRAGLLIGLVNILVILALGLIQGGSLSLEI
LWSLLLAFLNGLLSAILAIGLLPLLESLFGITTDIKLLELSNPNHPLLKRLLLEAPGTYHHSLMVANLAE
AAAEAIGANPLLARVGAYYHDIGKMKRPLYFIENQMGGENPHDKLSPSLSALIIISHVKDGVELARKYKL
PKEIIDFIRQHHGTTLVKYFYHKAKEENGGEEVDEEDFRYPGPKPQSKETAIVMLADSVEAAVRSLKEPT
PEKIEGLVRKIIKDKLEDGQLDECDLTLKDLEKIKKSFVKVLTGIYHSRIEYPELKKKKKKK
>gnl|CDD|441090 COG1481, WhiA, DNA-binding transcriptional regulator WhiA, involved in cell division [Transcription]
MSFSAEVKDELARLEVEKKCCRKAELAALLRMNGSLHISNGRLVLEIETENAAIARRIYKLLKELYGIDT
ELLVRKKMRLKKNNVYIVRVPQEGGEELLRDLGLLDERGRLVRGIPPELVKSECCKRAYLRGAFLAGGSV
NDPEKSYHLEIVCPSEEAAEALVGLLNRFGLNAKIRERKGGYVVYLKEGEAISDFLNLIGAHQALLEFEN
VRIVKEVRNSVNRLVNCETANLNKTANAAVRQIENIERIEEILGLDNLPEHLREIAELRLENPDASLKEL
GELLDPPLSKSGVNHRLRKLLEIAEKLRE
>gnl|CDD|441091 COG1482, ManA, Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism]
MMYPLRFKPIFKEKIWGGRRLKEVFGKDLPEGKIGESWEISAHPNGVSVVANGPLAGKTLDELVEEHPEE
LLGEKVYARFGDEFPLLIKFLDAKDDLSVQVHPDDEYAKEHEGGSYGKTEMWYILDAEPGAEIYLGFKEG
VTKEEFREALENGDIEDLLNRVPVKKGDFFLIPAGTVHAIGAGILVLEIQQTSDITYRVYDYDRLDLDGK
PRELHIEKALDVIDFERKPDEVVQPTVVEEEGNREERLVECPYFTVERLELDGEVTLDTEDSFHILSVVE
GEGTIESDGEPYELKKGETFLLPAAVGEYTIRGEAKLLKSYVPD
>gnl|CDD|441092 COG1483, COG1483, Predicted ATPase, AAA+ superfamily [General function prediction only]
LKPWFDVCTPHPDVLKGTLQQAEFAADLDQVVRGEAPDEYQDPEEFFERTYLTEGLRDLLAEVLRRLSGD
KGGDPVIRLQTAFGGGKTHTLLALYHLAKGGPALSDLPGVEEILDEAGIPELPGKVRVAVFVGTELDPSQ
GRGKPDGPTIKTLWGELAWQLGGEEGYALVAEADESGTAPGGDVLRELFGGRPCLILIDELVAYARQLRA
VKVLDSGLFDQLLTFLQALTEAAKGVPNAVLVVSLPASALEAGGEEGQEALDRLEKVFGRVESAWRPVSD
EEIFEIVRRRLFESIDDEAAADAVARAYADLYRANRAELPSEAREADYRERIKAAYPFHPELFDRLYEKW
STLPRFQRTRGVLRLLALVVHRLWEKGDKDPLIHPGHVPLDDPRVRNELTSYLEDNWEPVIDADIDGPNS
HAQRLDREWPNLGKYPLARRVARTIFLGSAPGRGAANRGLTEPELRLGVAQPGEDIGNFGDALRRLTDRA
TYLYSDGGRYWFSTQPNLNKLIADRARQVDDEDVDEEIRERLRKVFGGGDFGVHVFPESSADVPDDADLR
LVVLPPDAAHSRSEDSAAPEAAEEILENRGSSPRTYRNTLVFLAADEDRLERLRDAARRLLAWESIVDDP
ERLNLDELQRKQLKERLKEAEQALREAVRETYKWLLYPSQDAAGKLRWEEIRLSGASSLAERISKKLRSD
ELLITEPIRLRKGDHVSTKDLWEDFARYLYLPRLKDPDVLRKAIRAGVASGDFGGLRTGDDLPLLLLLDV
AAAAADATQALEAAAAAAAAPPTVLPSEDGGLGGELPVDEVPVGAPVGSSGDAAPTPPSTTGAARLAADR
PGAVAETASEAVAAVALLLVATDTAIVAIEPDADVEASAEELVLVAREQSETGEADEDEGTGEEVVTSEG
SLEIPGEAVLALGRSDETAGAIVAEGKTGLKAGGEVPETGGGGGESTVLVALVVAVSAEELAELTVEAVE
RDKLTAGTGLSK
>gnl|CDD|441093 COG1484, DnaC, DNA replication protein DnaC [Replication, recombination and repair]
MLMEELKELLKALKLPGMAEALDELLAQAACDELSYEEFLALLLEAEVAEREQRRIERRLKAARFPAAKT
LEDFDFDAQPGLDRRQILELATLDFIERGENLILLGPPGTGKTHLAIALGHEACRAGYRVRFTTAPDLVN
ELKEARADGRLERLLKRLAKVDLLILDELGYLPLDAEGAELLFELISDRYERRSTIITSNLPFSEWGEVF
GDPTLATAILDRLVHHAHIIELKGESYRLKEA
>gnl|CDD|441094 COG1485, ZapE, Cell division protein ZapE (Z ring-associated ATPase), AFG1 superfamily [Cell cycle control, cell division, chromosome partitioning]
MMMSPLERYQALLAAGGLQPDPAQEAAVARLDRLYDELLAYRPRKSGLLGRLFGRKRKPEPPKGLYLWGG
VGRGKTMLMDLFFESLPVERKRRVHFHRFMQEVHARLHALRGQADPLPPVADRIAAEARLLCFDEFHVTD
IADAMILGRLFEALFARGVVLVATSNIPPDDLYKNGLQRARFLPFIALIKQHLDVLNLDSGTDYRLRRLE
GAPVYHTPLDAEADAALDAAFARLTGGAPEEPETLEVNGREIPVPRAAGGVAWFDFADLCGGPRGQADYL
ELARRFHTVILSDVPVMGPDNRNEARRFITLIDELYDRRVKLIASAAAPPEELYTGGRGAFEFERTASRL
IEMQSEEYLALPHRP
>gnl|CDD|441095 COG1486, CelF, Alpha-galactosidase/6-phospho-beta-glucosidase, family 4 of glycosyl hydrolase [Carbohydrate transport and metabolism]
MKIAIIGGGSTYTPELLLGDLLRYPELPVSEIALYDIDEERLEIVGRLARRMAAEAGAPIKVEATTDRRE
ALKGADFVINQIRVGGLEARELDERIPLKYGVIGQETTGPGGIARALRTIPVMLDIARDMEELCPDAWLL
NYTNPAGIVTEALLRYGPGIKVVGLCHSPIGTQRRLAKLLGVPPEEVDYDYAGLNHLGWFTRVYVDGEDL
YPELLEAVAELPENIEDRPVRFELLRRLGYLPNEYLPYYYKRDEAVEKWLIPEGTRAEYVRRCEEELFEE
YRDALDGKPEELLERGGAGYSEYAVDLIEALATGKPRRIIVNVRNNGAIPNLPDDAVVEVPCLVDANGIR
PLAVGPLPPQLAGLIRQVKAVEELTVEAALEGDRELALQALLLDPLVPSLDVAKALLDELLEAHKEYLPE
FKR
>gnl|CDD|441096 COG1487, VapC, Ribonuclease/mRNA interferase VapC, contains PIN domain [Defense mechanisms]
YLLDTNVLIDLLRGRPPAVLAWLAELEAGELAISAITLAELLYGARRSPDAKRRAALEAFLEAFPVLPFD
AEAARRAGELRAALRRAGRPIGLADLLIAATALAHGLTLVTRNTKDFERIPGLKVEPW
>gnl|CDD|441097 COG1488, PncB, Nicotinic acid phosphoribosyltransferase [Coenzyme transport and metabolism]. Nicotinic acid phosphoribosyltransferase is part of the Pathway/BioSystem: NAD biosynthesis
MDNLALLTDLYKLTMAQAYLPEGTANRRAVFELFFRRLPFGRGYVVFAGLQRFLKYLENLRFTEEDIAYL
RSLGVFDEDFLDYLADFRFPGDIRAVPEGTVVFPGEPLLTVEGTLPEAQLLETLLLNILNYPTLIATKAA
RIVQAAGGRPLHDFGLRRAHGLEAAVAAARAAYLAGFAGTSNVLAGRYYGIPSVGTMAHSFVQAHDDELE
AFRAFAEAYPDGTTLLVDTYDTLSGVPNAIELAKELLARGGLLGIRLDSGDLAYLSKQARELLDEAGLPD
VRIIASDDLDEYRIAALLEQGAPIDVFGVGTRLVTSSDRPTLGFVYKLVAVEGDGEWRPVIKLSETPGKK
SKPGRKQVYRRDEDGKATADLVALEDEPLPGEPEPLLVPVFRDGKLVYELPSLEEIRERAAAQLAELPEE
LKRLRNPPAYPVDLSEALWDLKEQL
>gnl|CDD|441098 COG1489, SfsA, DNA-binding protein, stimulates sugar fermentation [Carbohydrate transport and metabolism, Signal transduction mechanisms]
MKFPPPLVEGTLIKRYNRFLADVELDDGEEVTAHCPNTGRMTGLLTPGARVWLSPSDNPKRKTPYTLEAV
EVGGTWVGINTALPNRLVEEALEAGLIPELAGYDTIRREVKYGNSRIDFLLEGPGRPDCYVEVKSVTLVE
DGLALFPDAVTERGQKHLRELAALVEEGYRAVLLFLVQRPDAERFAPADHIDPEYAEALREAAAAGVEVL
AYRCEVTPEGIRLGRELPVVL
>gnl|CDD|441099 COG1490, Dtd, D-aminoacyl-tRNA deacylase [Translation, ribosomal structure and biogenesis]
MRAVIQRVSEASVTVDGEVVGEIGKGLLVLLGVEKGDTEEDADWLARKILNLRIFEDENGKMNLSLLDVG
GELLVVSQFTLYADTRKGRRPSFSKAAPPEEAEPLYEYFVEALRELGLPVETGVFGADMQVSLVNDGPVT
ILLDSKK
>gnl|CDD|441100 COG1491, COG1491, Predicted nucleic acid-binding OB-fold protein [General function prediction only]
GGDGKPDKYEEYAYVLDYLPHGRPDDKRPQYRKEPIAQAIGEDEFTLLELVPKDDADIEIGERVYIGKGK
RDKIVSVKRRIEYDDLTSTAKSELPYVVEEIVKENEKRFVDFFNEAQPITLRLHQLELLPGIGKKLMWAI
LEERKKKPFESFEDLEERVKGLHDPKKVIVKRILEELKDDDLKYRLFVR
>gnl|CDD|441101 COG1492, CobQ, Cobyric acid synthase [Coenzyme transport and metabolism]. Cobyric acid synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MAKALMVQGTTSDAGKSLLVAALCRILARRGYRVAPFKAQNMSLNSAVTADGGEIGRAQALQAEAAGVEP
SVDMNPVLLKPEGDTGSQVIVQGKPVGNMSARDYYEYKPRLLEAVLESLDRLAAEYDLVVIEGAGSPAEI
NLRDRDIANMGFAEAADAPVILVGDIDRGGVFASLVGTLALLPEEERARVKGFIINKFRGDPSLLEPGLD
WLEERTGVPVLGVLPYLEDLRLPAEDSLALESRRGSKGGGRLRIAVIRLPRISNFTDFDPLAAEPGVRLR
YVRPPEELGDADLVILPGSKNTIADLAWLRESGLDDAIRAHARRGGPVLGICGGYQMLGRRIADPDGVEG
GAGEVPGLGLLPVETVFAPEKTLRQVTGTLLGPLSGAPVSGYEIHMGRTTGPDGARPLLRRDGREPDGAV
SADGRVWGTYLHGLFDNDAFRRALLNALREKKGLSPLAAGAVDYAARREAALDRLADHVEEHLDLDALLA
LLG
>gnl|CDD|441102 COG1493, HprK, Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction mechanisms]
TLHGVLVDVGGRGVLITGPSGSGKSELALELIKRGHRLVADDRVELRREGGGRLIGRAPELLRGLIEVRG
LGILDVPTLFGAGAVRPEARIDLVVDLVEWDDKEYERLPLEEETTEILGVEVPLLTLPVRPGRNLAVLIE
VA
>gnl|CDD|441103 COG1494, GlpX, Fructose-1,6-bisphosphatase/sedoheptulose 1,7-bisphosphatase or related protein [Carbohydrate transport and metabolism]
LELVRVTEAAALAAARWMGRGDKNAADQAAVDAMRRALNTVDIDGTVVIGEGEKDEAPMLYIGEKVGTGE
GPEVDIAVDPLEGTTLTAKGLPNAISVLAVAERGSLLHAPDMYMEKIAVGPEAKGVIDLDAPVEENLRAV
AKALGKDVSDLTVVVLDRPRHEELIEEIREAGARIKLISDGDVAGAIATALPGTGVDILMGIGGAPEGVL
AAAALKCLGGEMQGRLWPRNDEERARAKEMGIDLDRVLTLDDLVKGDDVIFAATGVTDGDLLKGVRFFGG
GARTHSLVMRSKTGTVRFIEAEHRLDKKPRL
>gnl|CDD|441104 COG1495, DsbB, Disulfide bond formation protein DsbB [Posttranslational modification, protein turnover, chaperones]
SSGRLLLLLLALAALALLLGALYFQYVLGLEPCPLCIYQRIAMYGLALLALLAALLPPRRGLRLLLLLAL
LLALAGAGLAAYHVGLQWGPWPGPPSCGCGLEYFPSWPDWLPSLFAGTGDCDEVQWTFLGLSMPGWNLIA
FALLALLALLALL
>gnl|CDD|441105 COG1496, YfiH, Copper oxidase (laccase) domain [Inorganic ion transport and metabolism]
LTFPDWPAPPGVRHGFTTRLGGVSQGPYDSLNLGLHVGDDPEAVAENRRRLAAALGLPPDRLVWLNQVHG
TRVVVVDAPDPDGAIPEADALVTNEPGVALAVLTADCVPVLFADPEGGVVAAAHAGWRGTVAGILEKTVE
AMEALGARPEDILAWIGPAIGPCCYEVGEEVAEAFLAADPDAARAFRPGAGGKYLLDLPGLARLRLLAAG
VPNIEGGGLCTYCDPDRFFSYRRDGKTGRMASLIWL
>gnl|CDD|441106 COG1497, MJ0558, Predicted transcriptional regulator MJ0558, contains a CRP-type HTH domain [Transcription]
MDVLRSKREATRFQILVEIAERQPAVRQGEIADKLGVTPQAVSEYIKELVEEGLVEKEGRGRYRVTKEGV
EWLLENAEDLRRFADHVLEDVIGSVSVWAAIAAEDIEEGETVSLYMEDGLLYATPGEKGGATGVATTDAE
AGEDVGVTGLEGVIDLEPGEVTVVKVPRVREGGSRAVDLDRLKELIESADLVAAAGVEALVALRKAGIEP
DVFFGAGEVAIEAARRGLDVLVVATDDMLGRVTDRLRDEGLEYEVVDLVKS
>gnl|CDD|441107 COG1498, SIK1, Box C/D ribonucleoprotein Nop56/Prp31/SIK1 subunit [Translation, ribosomal structure and biogenesis]
MKIYVTLTWFGILALDEDGKIVDYELFPKDEIVEELLKIEEELIELIEKLKDEVVVELKKLGLEAAVEAI
NEGGAEFRRDLPELAVEAGFAEDEEEYYDLLHEVTLEATRRKVREAAQARDLQIIQAIRALDDIDKTANL
LAERLREWYGLHFPELDTGVKDHEEYARIVAELGPRENITKENLAEKIAEAAKKSMGADLSDEDLEIIKS
LAERILDLYDERKSLEEYIERVMPEVAPNLTALAGPVLGARLISLAGGLERLAKLPASTIQVLGAEKALF
RHLRGGAPPPKHGVIFQHPAIHGSPRWQRGKIARALAAKLAIAARIDHYSGEIGPELKEELEKRIEEIKA
RY
>gnl|CDD|441108 COG1499, NMD3, NMD protein affecting ribosome stability and mRNA decay [Translation, ribosomal structure and biogenesis]
MSRGFCPRCGREVEELVDGLCKDCYLEEFPLVDAPDRVEVTVCPRCGAVRRGGRWVDPGAEDYEEVAIEA
VEDALKVHEEAEDVEIEVEPEQLDPNTIRVHVTVTGRVRGEPVEEEVTVPVRIKREVCPRCSRIAGGYYE
AIVQVRADGRKPTEEEREEAEEIAEEVVDKLAKGDRLAFITKVEELKEGLDIYLGSTKAGRKIARAIVEE
LGGSVSESPKLVGEDKDGKEVYRVTYSVRLPEFRPGDIVEYEGKPYLVRSVSGGGLKGRDLETGERYEAS
WEEAPDAKVLGKREDAEEATVVSVEDNEIQVLDPETYETVTIPRPDYLDAEEGDEVPVLKIEGRLYILPD
EE
>gnl|CDD|441109 COG1500, Sdo1, Ribosome maturation protein Sdo1 [Translation, ribosomal structure and biogenesis]
MVSLDDAVIARLESHGERFEILVDPDLALEYKEGKDVDIEDVLAVEEIFKDARKGERASEESLKKVFGTT
DVLEIAKEIIKKGEIQLTAEQRREMIEEKRKQIINYIARNAIDPQTKLPHPPQRIELAMEEARVHIDPFK
SVEEQVKEVVKALRPIIPIKFEKAKIAVKIPPEYAGKAYGEISKFGTIKKEEWQNDGSWIAVVEIPAGMQ
NEFIDKLNKLTKGEAEVKILKV
>gnl|CDD|441110 COG1501, YicI, Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism]
MAYTKIYENKGVYKVVIGEIAPPIEFPLETSESSDKLRSETGKLIVQQGNKTYVRKQLDLGEQIYGLGER
FTTLHKRGRIVVNWNLDHGGHKDNGNTYAPIPFYVSSKGYGVFVNSASYVTFDVGSAYSDLVEFTVPGDS
LEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYYDQDQVLAFADEFRDRGFPLDVIHLDIR
WMDKYYWGDFEWDPRRFPDPKAMVKELHDRGVKLVLWINPYVAPDSAIFAEGMANFVKIASGTVFVGKMW
PGTTGLLDFTRPDAREWFWAGLEKELLSIGVDGIKLDMNEGWPTDVATFPSNVPQQMRNLYGLLEAKATF
EGFRTSRNNRTFILTRSGFAGGQRYPVIWTGDNTSSWESLEDQLTQGLNLSLSGVPFWTPDIGGFFGSPS
RELWIRWFQVGAFSPFARIHGWASSTEPWFFDEEAKQIVKEYAQLRYRLLPYIYSLFAKASTDGTPVIRP
LFLEFPDDPTTRFIDDQYMFGEYLLVAPIFAGTESRLVYLPKGKWYDFWTGELIEGGQWITVTAPLDRLP
LYVRDGSIIPLGPVSLRPSMQKIDGIELRVYGSGETAYTLYDDDGETVS
>gnl|CDD|441111 COG1502, Cls, Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and metabolism]. Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis
KAAPLAAGLPLVGGNRVTLLVDGDEAFAALLEAIEAARRSIDLEYYIFDDDEVGRRLADALIAAARRGVK
VRVLLDGIGSRALNRDFLRRLRAAGVEVRLFNPVRLLFRRLNGRNHRKIVVIDGRVAFVGGANITDEYLG
RDPGFGPWRDTHVRIEGPAVADLQAVFAEDWNFATGEALPFPEPAGDVRVQVVPSGPDSPRETIERALLA
AIASARRRIYIETPYFVPDRSLLRALIAAARRGVDVRILLPAKSDHPLVHWASRSYYEELLEAGVRIYEY
EPGFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYDPEFAAQLRARFEEDLAHSREVTLEEWRKR
PLRRLRERLARLLSPLL
>gnl|CDD|441112 COG1503, eRF1, Peptide chain release factor 1 (eRF1) [Translation, ribosomal structure and biogenesis]. Peptide chain release factor 1 (eRF1) is part of the Pathway/BioSystem: Translation factors
SSRKRYELKKTLEELKKLSGRGTELLSLYIPPDPPISDVVNQLREELSQAKNIKSKQTRKNVQDALERII
ERLKLYKKPPENGLAIFAGAVPTDMLTYVIEPPEPVRTFRYRCDSRFYLEPLEDMLEEKERYGLLVIDRR
EARIGLLRGGRIEELDELESEVPGKHRKGGQSQRRFERLIEEAAHEFFKEVAEAANELFLRDKLKGLIIG
GPGPTKEEFLEGDYLHHRLRKKVLGLFDVSYTGEAGLRELVEKAEDLLKEQEREEEKELVEEFFEELAKG
GLAVYGLEEVLEALEMGAVDTLLISEDLRKPGVRCPCCGCLGEEECPCCGCGGEVEEEEDLVDELVELAE
QQGAEVEVISTDFEEGEQLLKAFGGIAAILRYRI
>gnl|CDD|441113 COG1504, COG1504, Uncharacterized conserved protein, DUF498 domain [Function unknown]
MKIEEYSFGSIVIDGKTYEKDVVIYPDGKVERRWRKYGTGHKLSLEDLEELLEEGVEVVVVGTGQYGRLK
VDPEVKELLKEKGIEVIILPTPEAVELFNELLSEGKKVLALFHLT
>gnl|CDD|441114 COG1505, PreP, Prolyl endopeptidase PreP, S9A serine peptidase family [Amino acid transport and metabolism]
KKRLTYPATRRDDVVDTTAVADPYRWLEDDDSPETLAWVKAQNAVTRAYLAAIPRREALRARLLELLNYD
RIPAPFKRGGRYYNFWNDGLQNQGVLRVRDGLDPEWEVLLDPNALSEDGTWVLGAWSLSPDGRRLAYSLS
EGGSDARVVRVFDVATGEFVEDGFEWEKKSGVAWLDGTGFVYSRYGEPEGSLTDSGYPRKVYYHRRGTPQ
SEDELVFEGPPDDPERYVGVSVSEDGRYLLISRALGFYRNELYLLDLPDGELVPLDLPFDADYSGVVNGG
WLYLLTRLDAPRGRLVAIDLAAPGPRNWTEFIPEAEAVLEGVSWTGGRLVLSYLDDVVSRVRVYDLDGKL
VREVPLPGLGSVSGFSGDDDGDELFYSFTSFLTPPTLYRYDLGTGESELLKKPPAPFDASDYEVEQVFAT
SKDGTRVPYFIVHKKGLKLDGPNPTLLYGYGGFNISLTPSYSASGLAWLERGGVYAVANLRGGGEYGPAW
HQAGLKENKQNVFDDFIAAAEDLIARGYTSPERLAIQGGSNGGLLVGAALTQRPELFGAVVCAVPLLDML
RYHKFTAGASWIAEYGDPDDPEEFAYLYAYSPYHNVKAGVAYPATLFTTADHDDRVHPAHARKFAARLQA
AQAGDNPVLYREETEGGHGAGAPTSQRAEEAADIYAFLWRNLG
>gnl|CDD|441115 COG1506, DAP2, Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]
TFKSADGTTLPGWLYLPADGKKYPVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWG
GDEVDDVLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREY
TERLMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEG
HGFSGAGAPDYLERILDFLDRHLK
>gnl|CDD|441116 COG1507, COG1507, Uncharacterized conserved protein, DUF501 family [Function unknown]
MTTPPFEPVSEADLAIVAAQLGRPPRGVVGVAARCPCGYPQVVKTAPRLPDGTPFPTLYYLTCPRLTAAV
SRLEASGLMKEMTERLAADPELAAAYRAAHESYLARREALGDEAGEGVPEIAGVSAGGMPTRVKCLHALV
AHALAAGPGVNPIGDEALELLEDWWPPGRCACVEE
>gnl|CDD|441117 COG1508, RpoN, DNA-directed RNA polymerase specialized sigma subunit, sigma54 homolog [Transcription]. DNA-directed RNA polymerase specialized sigma subunit, sigma54 homolog is part of the Pathway/BioSystem: RNA polymerase
MMKQSLQLRQSQQLVLTPQLQQAIKLLQLSTLELEQEIEQELEENPLLEEEELENPAAAEESLQEHLLEQ
LRLLPLSERERAIAEYLIGSLDDDGYLRVSLEEIAEDLGVSEEEVEAVLKLLQSLDPAGVGARDLQECLL
LQLRRLPRDDPLALRIIRDHLDLLAKRDYKKLAKKLGVSEEELQEAIALIRSLNPKPGRAFSSEETQYIV
PDVIVRKVDGEWVVELNDDALPRLRINREYAELLKRADDKEAKEYLKEKLQEARWLIKSLEQRQETLLKV
AEAIVERQRDFFEHGEEALKPLTLKDIAEELGLHESTVSRVTTNKYVQTPRGIFELKYFFSSGVSTDDGE
EVSSTAIKALIKELIAAEDKKKPLSDQKIAELLKEQGINIARRTVAKYREQLGIPSSSQRKRL
>gnl|CDD|441118 COG1509, EpmB, L-lysine 2,3-aminomutase (EF-P beta-lysylation pathway) [Amino acid transport and metabolism]
MITRSVTEEQWNDWQWQLRNAITDPEELLRLLGLSEEELEALEAVAKVFPLRVTPYYLSLIDPGDPDDPL
RRQVLPSAEELEDAPGESLDPLGEDDDSPVPGLTHKYPDRVLLLVTGTCAVYCRYCFRRRFVGDDDNKPS
KEEWEAALDYIRAHPEIRDVLLSGGDPLMLSDERLEWLLERLREIPHVERIRIGTRLPVVLPQRITDELL
EILKKYHLPLVIVTHFNHPREITPEAAEALRRLRDAGIPLLNQSVLLRGVNDDAETLAELSEKLFRAGVR
PYYLFQLDLVQGAAHFRVPVARGLEIMEELRGRLSGYAVPRYVRDAPGGGGKVPLLPNYLIREDG
>gnl|CDD|441119 COG1510, GbsR, DNA-binding transcriptional regulator GbsR, MarR family [Transcription]
MSEKLEEAKERFIEAFGEMGERWGLPRSAGRIYALLYLSDEPLTADELAEELGVSKSSVSTALRELEDWG
LVRRVRKPGDRKDYFRAEKDVWELFRRVFRERLRREIDPTLELLREALEELEDSEEAEEARERLEELRDF
YEFLERLLEALLKRWEEDLRKEDK
>gnl|CDD|441120 COG1511, YhgE, Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]
FKRELKRLFKNKLALIALIALILVPLLYAGLYLWAFWDPYGNLDNLPVAVVNEDKGATVDGKTVNLGDEL
VDELKDNDSFDWQFVSEEEAEKGLKDGKYYAVIVIPEDFSANLASLLSDDPEKATITYYTNEANNYLASK
ITDTAATTVVDQVNSQVTETYAETVSPVALKTEALNPVPNYGSGLAPFFLSLALWVGALLLFLLLRPLVD
RAGASLDRLNELFLK
>gnl|CDD|441121 COG1512, YgcG, Uncharacterized membrane protein YgcG, contains a TPM-fold domain [Function unknown]
MKKLLLLLLLLLLFALPALAQDVPPVPALTGYVVDYAGLLSPAEEAALEQKLAALEDKTGAQIVVVTVPS
LGGEDIEDYATRLFRKWGIGQKGKDNGVLLLVAKDDRKVRIEVGYGLEGALTDAIAGRIIDETIIPAFKD
GDYYGGILAGVDAIIAVLAGEYLPDPEAEETDSSGDAFGLLFIGVIFLFFLLSILLGGGGGGGGGFGVGI
GGILIGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG
>gnl|CDD|441122 COG1513, CynS, Cyanate lyase [Inorganic ion transport and metabolism]
RAEVTEKILAAKKAKGLTWADIAEAIGRSPVWTTAALLGQMSLPEEEAEKLAELLGLPEEAAAALQEVPY
KGSLDPAVPTDPLIYRFYEIVQVYGPTLKELIHEKFGDGIMSAIDFSMDVEKVEDPKGDRVVITMSGKFL
PYKKW
>gnl|CDD|441123 COG1514, ThpR, RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and biogenesis]
MRLFIALPPPEELREALAALRARLKAAPGGRWVRPENLHLTLAFLGEVDEERLEALAEALARAAAGAPPF
ELRLDGLGAFPRPRPRVLWLGVEPSPELLALHRRLRAALARAGLPPERRPFVPHVTLARGKRPAPPLAPA
LAELRDFEFPEFTVDEFVLYESELTPDGPRYEVLAEFPLGG
>gnl|CDD|441124 COG1515, Nfi, Deoxyinosine 3'-endonuclease (endonuclease V) [Replication, recombination and repair]
KPLHPWPLSLEEARALQRELAARVVLEDDLGEPRLVAGVDVSYEDGGDRAVAAIVVLDYPTLEVVERAVA
RGPVTFPYIPGLLSFRELPALLAALEKLKVEPDLLLVDGQGIAHPRRLGIASHLGVLLDVPTIGVAKSRL
CGEFEEPGEERGSWSPLVDDGEVIGAVLRTRDGVKPLYVSPGHRISLETALELVLACTPGYRLPEPTRLA
DRLARRLRREL
>gnl|CDD|441125 COG1516, FliS, Flagellin-specific chaperone FliS [Cell motility, Intracellular trafficking, secretion, and vesicular transport]
ENSVATASPHQLILMLYDGALKFLARAKGAIERGDIEEKGEAISKAQDIISELRASLDMEKGGEIAKNLD
ALYDYMIRRLLEANLKNDAEILDEVIRLLEELRDAWKEIAKQA
>gnl|CDD|441126 COG1517, Csx1, CRISPR/Cas system-associated protein Csx1, contains CARF domain [Defense mechanisms]. CRISPR/Cas system-associated protein Csx1, contains CARF domain is part of the Pathway/BioSystem: CRISPR-Cas system
AKRLLIATWGNPKNWREVKYVLEDNREREVESKTSLVALAKALNPDRVIILALDSLATYLDLQKGEPSSY
EDLLSEVKEKVEEYVKESSEFGNNIEVVVLPGVGTFGEDEFRGNPTDFFSYALYKLLKKLEEVDEPLEIV
LDITHGINYMPTLALRAARLAASLLALANKKEVKLEVYNSDPYVKDEEPILNIHEIESETITPVQLLSEI
TSRLLSKYPDNVRKIKREFKKNLREVLSNLSKALKALSYGLPLLLLYLLREIEELEKLERALDKLEELEE
ENITVTLREEGKKVEDYDLIIRELAYLALLLSLLKLYLESRIVKSDDGEVPLDELKKLADKYFSSPVIRI
IIKNELSKIKNAIEASSLIKGEWISLAELLEKIKGESKENCDIDKRNFIAHAGLERNITEVKKDGDKICI
RYNEECLERIKKALKKRGE
>gnl|CDD|441127 COG1518, Cas1, CRISPR-Cas system-associated integrase Cas1 [Defense mechanisms]. CRISPR-Cas system-associated integrase Cas1 is part of the Pathway/BioSystem: CRISPR-Cas system
TLYITEPGAYLSRKGNTLVVEKEDEEKKRVPLEDIEQIVLFGEVSLSTALLRFLAENGIPVHFLDYYGRY
LGRLLPRESGGNVLLRRAQYQAYLDEEKRLALARSIVRGKIRNQRAVLRRYGRRRKEDLEEAIERLEELL
KRLEEADSIDELRGIEGNAARIYFSALDGLLPEDFRFEGRSRRPPRDPVNALLSFGYTLLYSDVLSAIYA
AGLDPYIGFLHEPRPGRPSLALDLMEEFRPILVDRLVLSLINRGQITPKDFEKELGGVLLTEEGRKKFLE
AFEERLQETIKHPFLGRKVSYRRLIRLQARKLAKHLRGELDEYPPFVLR
>gnl|CDD|441128 COG1519, KdtA, 3-deoxy-D-manno-octulosonic-acid transferase [Cell wall/membrane/envelope biogenesis]. 3-deoxy-D-manno-octulosonic-acid transferase is part of the Pathway/BioSystem: Lipid A biosynthesis
MMRFLYNLLLYLLLPLLLPLLLWRARRGREYRERLGERLGFYPAPRPGGPLIWFHAASVGEVEAALPLIE
ALRARYPDLKILLTTTTPTGAEVAKKLLPDADIHQYLPLDLPGAVRRFLDHWRPDLAILVETELWPNLLA
AAKRRGIPLVLVNARLSERSFRRYKRLGGLARPLLSRFDLILAQSEADAERLRALGAPPERVTVTGNLKF
DRVPPPADPAELAALRAALGEGRPVWVAGSTHPGEEEILLDAHRKLRKRHPDLLLIIAPRHPERFDEVAA
LLKKAGLSVARRSEGEAPLADTDVLLGDTMGELGLLYALADVAFVGGSLVPRGGHNPLEPAALGKPVLFG
PHTFNFAEAAELLIAAGAAIQVADAEELAAAVLALLADPELRAAMGAAARAVVEANRGATDRTLAALEPL
LPQA
>gnl|CDD|441129 COG1520, PQQ, Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis]
LLLLLLLLSGFSSEDDEPPPAPLPEFEPSVKVKQLWSASVGDGVGKGYSRLAPAVAGDRVYAADADGRVA
ALDAATGKELWRVDLGEPLSGGVGADGGLVVVGTEDGEVIALDADDGEELWRARLSSEVLAAPAVAGGRV
VVRTGDGRVYALDAATGERLWSYQRPVPALTLRGTSSPVIVGGAVLVGFANGKLVALDLANGQPLWEQRV
AQPRGRTELERLVDVDGTPVVDGGVVYAVAYQGRLAALDLRSGRVLWSRDLSSYTGLAVDGNNLYVTDDD
GRVWALDRRNGAELWKQDALLYRGLTAPVVLGDYVVVGDFEGYLHWLSRDDGSLVARLRVDGSGIRAAPV
VVGDTLYVQTRDGTLAALRL
>gnl|CDD|441130 COG1521, CoaX, Pantothenate kinase type III [Coenzyme transport and metabolism]
MLLAIDIGNTRIKWGLFDGGELLASWRLATDRRTADELAELLRQLLAALLPDIEGVIISSVVPPLTEALE
ELLRKYFGVPPLVVGPGVKTGLKNAYDNPEELGADRIANAVAARELYGGPLLVVDFGTATTFDVVDADGE
YLGGAIAPGLGLSLEALHQRTAKLPLVELEKPPSVIGKNTVEAIQSGVVYGYAGLIEGLIERIKEELGED
PKVIATGGDAPLLAPELKTIDIVDPDLVLEGLRLIYERNK
>gnl|CDD|441131 COG1522, Lrp, DNA-binding transcriptional regulator, Lrp family [Transcription]
MELDEIDRRILRLLQEDGRLSFAELAERVGLSESTVLRRVRRLEEAGVIRGYGAVVDPEKLGLGVTAFVE
VKVPPHRLDEFAEALAAIPEVLECYLVTGDYDLLLKVVARDMEELERFLLERLAALPGVRRTETSFVL
>gnl|CDD|441132 COG1523, PulA, Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism]
MRVWPGRPYPLGATWDGDGVNFAVFSAHATRVELCLFDEDGDEETARIPLPERTGDVWHGYVPGLGPGQR
YGYRVHGPYDPERGHRFNPNKLLLDPYARAIDGPLRWDDALFGYRIDLSFDPRDSAPFVPKSVVVDPAFD
WGGDRPPRTPWEDTVIYEAHVRGFTKLHPDVPEELRGTYAGLAHPAVIDYLKRLGVTAVELLPVHAFVDE
RHLVEKGLTNYWGYNTLGFFAPHPRYASSGDPGGQVDEFKTMVKALHAAGIEVILDVVYNHTAEGNELGP
TLSFRGIDNASYYRLDPDDPRYYIDYTGCGNTLNLNHPRVLQLILDSLRYWVTEMHVDGFRFDLASTLGR
EPDGFDPDSPFLDAIAQDPVLSQVKLIAEPWDIGPGGYQVGNFPPGWAEWNDRYRDTVRRFWRGDPGTLG
ELATRLAGSSDLFEHSGRRPYASINFITAHDGFTLADLVSYNEKHNEANGEDNRDGHNDNRSWNCGVEGP
TDDPEILALRRRQIRNLLATLLLSQGTPMLLAGDEFGRTQQGNNNAYCQDNEISWLDWDLDEADRDLLAF
VRRLIALRRRHPVLRRRRFFTGRPIEGDGLPDVAWLRPDGEEMTEEDWDDPGARALGVLLAGRAIPIGDD
DLLVLFNAGHEPVEFTLPEGPGGRRWRLVLDTALPDPEPEGPVAGATYTVPARSVVVLRA
>gnl|CDD|441133 COG1524, AtaC, c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms]
MKRGLSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAP
AHTTLLTGLYPGEHGIVGNGWYDPELGRVVNSLSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFWPSF
EGSGLIDAARPYPYDGRKPLLGNPAADRWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAA
LREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVPPDIDLNRLRLAGLLAVRAGESAHLYLKDGADA
EVRALLGLPARVLTREELAAGHFGPHRIGDLVLVAKPGWALDAPLKGSHGGLPDEEMRVPLLASGPGFRP
GVRNVDVAPTIARLLGLPDG
>gnl|CDD|441134 COG1525, YncB, Endonuclease YncB, thermonuclease family [Replication, recombination and repair]
MRKLLLALLLALAALAAAAAAATLTAGVVRVIDGDTLRVRDDGKGERVRLAGIDAPELGQPCGPEQPCGE
EARQALRALLAGKTVTLEPDEGRDRYGRLLAYVYVDGRDLNEELVREGLAWAYRRYSPDKYADRYLAAEA
EARAARRGLWSDAFPVPPEWRRRK
>gnl|CDD|441135 COG1526, FdhD, Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and conversion]
ATKRVPVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESI
EVDEDEGGIVVRVELAPGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLD
ALREAQPLFRRTGGVHAAALFDPDGELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMV
QKAARAGIPILVSVSAPTSLAVELAEEAGLTLIGFARGDRFNVYTHPERI
>gnl|CDD|441136 COG1527, NtpC, Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]. Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 is part of the Pathway/BioSystem: A/V-type ATP synthase
MASVTNYAYINARIRAMESKLLKEEDYERLLEAESLEEIARFLKETGYGEELDELAERESGRDLLEKALN
RNLAKTYRKLLEFAPGELKEFVKLYLLRYDIHNLKVILRGKYSGEDLEEIRELLIPAGELSEEDLKKLLE
AKSVEELVEALEGTPYYEALEEALEEYEETGDLFPIENALDRAYYENLLELAKKKGKDRKLLLEYLGTEI
DLLNLRTILRLKRYGLSPEEIEAYLIPGGYRISEKELKELAEAEDVEELLEALEGTPYGKLLSELEELEE
TGSLSEFERALDRYLLEYAKKLSKYYPFSIGPVLAYLLAKENEVKNLRIIAEGKRYGLSPEEIRERLR
>gnl|CDD|441137 COG1528, FtnA, Ferritin [Inorganic ion transport and metabolism]
MLSEKMEKALNEQINLEFYSSYLYLAMAAWCDEKGLPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVEL
PAIDAPPNEFESLLEVFEAALEHEQKVTKSINELVDLAREEKDYATENFLQWFVKEQVEEEALARTILDK
LKLAGDDGSGLFMLDKEL
>gnl|CDD|441138 COG1529, CoxL, Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]. Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
MSDPADFRIIGKPVPRVDGPAKVTGRARYTDDIRLPGMLYAAVVRSPHAHARIKSIDTSAALALPGVVAV
LTGEDLPGLKFGLPGPDPDQPPLADDKVRYVGEPVAAVVAETREAARDAAELIKVEYEPLPAVVDPEAAL
APGAPLVHEELPGNVAAEWRGERGDVDAAFAEADVVVEATYTTPRLAHAPMEPRAAVAEWDGDGRLTVWA
STQGPHLVRRALARALGLPPEKVRVIAPDVGGGFGGKLDVYPEEVLAALAARKLGRPVKLVLTREEDFLA
DTHRHATVQRVRLGADKDGKITALRHDVVADTGAYASFGEAVLPLGATMATGPYAIPNVRVEARAVYTNT
PPTGAYRGPGRPQAAFALESAMDELAEELGMDPVELRLRNLIRPGDFPPTGQPYDSGRLAECLEKAAEAF
GWGERRARPAEARAGKLRGIGVAAYIEGSGGGGDPESARVRLNPDGSVTVYTGATDIGQGHETVLAQIAA
EELGVPPEDVRVVLGDTDLTPYGGGTGGSRSTAVGGSAVRKAAEKLREKLLELAAHLLGADPEDLEFEDG
RVRVPGRSVSLAELAAAAYYGGLEATGTYDPPTYPTYSFGAHVAEVEVDPETGEVRVLRVVAVHDCGRVI
NPLLVEGQVEGGVVQGIGQALYEELVYDEDGQLLNANFADYLVPRAADVPEIEVIFVETPDPTNPLGAKG
VGEPGTIGVAPAIANAVYDATGVRIRDLPITPEKVLAALRE
>gnl|CDD|441139 COG1530, CafA, Ribonuclease G or E [Translation, ribosomal structure and biogenesis]
KEILINATPQETRVALVEGGRLVELDIERPGREQLVGNIYKGKVTRVLPGLQAAFVDIGLERHGFLHVKD
ISPEYFSLGKEDSGKRPNIQDVLKEGQEVLVQVVKEPRGTKGARLTTFISLAGRYLVLMPNNRHVGVSRR
IEGEEERERLKELLSELKVPEGMGLIVRTAAEGASEEELQWDLDYLLKLWEAIQEAAKSAKAPFLIYQEL
DLIIRALRDYFRPDIGEILVDSREAYEKAKDFISLVMPDLADRVKLYTGERPLFDRYQIESQIESALERR
VWLKSGGYLVIDQTEALTTIDVNSGRFTGGRNIEETAFKTNLEAADEIARQLRLRDLGGIIVIDFIDMED
EEHQREVENRLKEALKKDRARTQIGGISRFGLVEMTRQRLRPSLGESLCEPCPRCEGRGTIKSVETVALE
ILREIEREARKENTREVLVQAPPEVAAYLLNEKRQELAELEKRYGVSIKLIPNPSLETEQYDIVRLRDDE
>gnl|CDD|441140 COG1531, COG1531, Uncharacterized conserved protein, UPF0248 family [Function unknown]
MIKELLNRILWDPRYDREDYEIVYLDRGAPGGLKEIPGSEIVRVDRGYIVLDDGTVIPYHRILEIRYKGE
VIWRRGEK
>gnl|CDD|441141 COG1532, COG1532, Predicted RNA-binding protein [General function prediction only]
CESNAYLLKDGNEELLMEDVDKIEPEGDKILLEDIFGEQKEIKGRIKEIDLVDHKIILEE
>gnl|CDD|441142 COG1533, SplB, DNA repair photolyase [Replication, recombination and repair]
LEEKAKSILNRNKSPDLPFDYSINPYRGCEHGCIYCYARPTHAYLLDFETKIVVKVNAAELLRKELRRPG
KPTPIALGTNTDPYQPIERRTGLTRELLEVLAEYNHPLEIVTKSALVLRDLDLLAELAHRGLVRVAFSLT
TLDEELARKLEPRTPSPERRLEAIRKLAEAGIPVGVMFAPIIPYLTDWEEEYEALLEAAAEAGALSAEYI
TLRLPPEVKELFREWLEEHFPDLAEKVRSLKFGQRGRGKGRYADELRQRFREALRRYGLYYR
>gnl|CDD|441143 COG1534, YhbY, RNA-binding protein YhbY [Translation, ribosomal structure and biogenesis]
MLTGKQRRYLRALAHHLKPVVQIGKNGLTEAVLAEIDRALEAHELIKVKVLQNDREDRKEIAEEIAEATG
AELVQVIGKTLVLYRPSPEKKKIEL
>gnl|CDD|441144 COG1535, EntB1, Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism]
PTAADLPANKVSWTLDPARAALLIHDMQNYFLRPYDPDEPPIRELVANIARLRDACRAAGIPVVYTAQPG
DQTPEDRGLLNDFWGPGLTAGPEGQEIVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGV
YAHIGCLATAVDAFMRDIQPFVVADAVADFSREEHRMALEYVAGRCGVVVTTDEVLEALRAAGP
>gnl|CDD|441145 COG1536, FliG, Flagellar motor switch protein FliG [Cell motility]
MADAAAARKLSGVEKAAILLLALGEEAAAEVLKHLSPEEVQKLTLEMARLGNVSPEEVEAVLEEFYELLR
AQSGILVGGIDYARELLEKALGEEKAASILDRITGSAGRRPFERLRWMDPRQLANLIRNEHPQTIALILS
HLDPDQAAEVLSLLPEELRADVVLRIATLEGVSPEALKELEEVLERKLSSVGSQKSSKVGGVKAAAEILN
RMDRSTEKEILEALEERDPELAEEIRDLMFVFEDLVRLDDRSIQRLLREVDNDDLALALKGASEELREKI
FSNMSKRAAEMLREDLEAMGPVRLSDVEEAQKEIVAIARRLAEEGEIVLGRGGGDEY
>gnl|CDD|441146 COG1537, PelA, Stalled ribosome rescue protein Dom34, pelota family [Translation, ribosomal structure and biogenesis]
MKILEEDEKRGEIKLVPETLDDLWHLSHIIEPGDLVYADTTRRVKQSSDKLRPDKGERKPVRLGIRVEKV
EFHPFTNRLRISGVIEEGPDFGPLGSHHTLNVEPGDELSIIKEKWKKDQLERLEEAVEASKKPKVLIVAV
DEGEAAIALVRQYGVEELATITSGSSGKRYPSKRSREEFFEEIAKALKNVASDVDAIIVAGPGFTKEDFA
KYLKEKYPELAKKIVVEDTSSGGERGVYEVLRRGAVDEILEESRIARESELVEELLERIAKDGKVAYGLD
EVKEAAEYGAVETLLVLDELLRSEDREDVDELLNSVESMGGKVVVVSSEFEPGKQLKALGGIAALLRYKI
Q
>gnl|CDD|441147 COG1538, TolC, Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]
TLDELIERALANNPDLRAARARVEAARAQLRQARAGLLPSQELDLGGKRRARIEAAKAQAEAAEADLRAA
RLDLAAEVAQAYFDLLAAQEQLALAEENLALAEELLELARARYEAGLASRLDVLQAEAQLAQARAQLAQA
EAQLAQARNALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDLRAAEAQLEAAEAEIGVA
RAAFLPSLSLSASYGYSSSDDLFSGGSDTWSVGLSLSLPLFDGGRNRARVRAAKAQLEQAEAQYEQTVLQ
ALQEVEDALAALRAAREQLEALEEALEAAEEALELARARYRAGLASLLDVLDAQRELLQAQLNLIQARYD
YLLALVQLYRALGGGWE
>gnl|CDD|441148 COG1539, FolB, Dihydroneopterin aldolase [Coenzyme transport and metabolism]. Dihydroneopterin aldolase is part of the Pathway/BioSystem: Folate biosynthesis
MDRIFLEGLRVYAYHGVYDEERELGQRFVVDLELELDLRKAAASDDLADTVDYAEVAEAIKELVEGEHFN
LIETLAERIADRLLAEFPRVEAVRVRVRKPDAPIGADSVGVEIERSRK
>gnl|CDD|441149 COG1540, PxpA, 5-oxoprolinase subunit A [Amino acid transport and metabolism]
MRIDLNSDLGESFGAWTMGDDEALLPLVTSANIACGFHAGDPLVMRRTVRLAKERGVAIGAHPGYPDLAG
FGRRNMDVSPEELYADVLYQIGALQAFARAAGTRVQHVKPHGALYNMAARDEALARAVAEAVKAVDPDLI
LLGLAGSELERAAEEAGLRVAREAFADRAYTPDGTLVPRREPGAVIHDPEEAAARVLRMVTEGTVTAVDG
KDIPVRADSICVHGDTPGAVELARAIREALEAAGIEIAPF
>gnl|CDD|441150 COG1541, PaaK, Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism]
SEMYWNPIETLSREELEALQLERLRATVARAYENSPFYRRKFDEAGVDPDDIKSLEDLAKLPFTTKEDLR
DNYPFGLFAVPLEEIVRIHASSGTTGKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFGYGLFT
GGLGLHYGAERLGATVIPAGGGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRDLSLKKGIF
GGEPWSEEMRKEIEERWGIKAYDIYGLTEVGPGVAYECEAQDGLHIWEDHFLVEIIDPETGEPVPEGEEG
ELVVTTLTKEAMPLIRYRTGDLTRLLPEPCPCGRTHPRIGRILGRADDMLIIRGVNVFPSQIEEVLLRIP
EVGPEYQIVVDREGGLDELTVRVELAPGASLEALAEAIAAALKAVLGLRAEVELVEPGSLPRSEGKAKRV
IDR
>gnl|CDD|441151 COG1542, COG1542, Uncharacterized conserved protein, DUF505 domain [Function unknown]
MVIKKEHAEALLKLLEEEEKGTEITEVLPEEEETVLELELAGLVRLETPLKIELTYAGRKLAEILDDLIE
KGKLPSPEEWPEDFRWIGSEIIAMIEAAEKAGRVGPLAEEALMERGLAEEVRDETKKEYKALTEYGKALL
EIYRETHPRLEIDAELAEFIRKMPKGPAEKSTLPYGGHEPHLLEAMRLIAYSVPTSDVFAFTALGQAVKK
ALTLGGFGEGTVLSEDILEALADAVDEEELTDAELEELQSLGLIDDEGELLPAGEALLEVYRLWKKGVEE
PVWSFALEEDEVEILKAIDELWKKHETNPEELPTFDEIRKEMEWYEKNFDLREALYSLESFGLIKTEEDE
KGKLVYYLTEWGEKVLEDQRKNFREISADAVKAITITEKEFSAPNVEWVEKAREEGLVGTGEPTDSGRLY
AELAEEIERKPHLTRYELQVLHKIPEKGIFVDELYKLFDEGDEEEIRWALEKLEARGFIEILPDGNVILT
EAGELMKRALSGVPEGFGNPVNPLIYRVLKAIREVGTLYVKEKKVRILPKNIKEAIKYSGLDPETFEKAL
ELARAAGFIGKNSINEAGLLLLEAVEKLNPKEEV
>gnl|CDD|441152 COG1543, COG1543, Predicted glycosyl hydrolase, contains GH57 and DUF1957 domains [Carbohydrate transport and metabolism]
MKGYLALVLHAHLPYVRHPEHEPFLEEDWLFEAITETYLPLLNMFERLERDGVPFRLTMSLTPPLLEMLA
DPLLQERYVRYLEKLIELAEKEVERTKGDPEFHYLARFYLDRFKEALRIFEERYGGDLLGAFKKLQDSGY
LEIITCAATHGYLPLLGVYPEAVRAQIKVGVDTYERHFGRKPRGIWLPECAYYPGLDEILAEYGIRYFFV
DSHGILYADPRPRYGVYAPVYTPSGVAAFGRDPESSKQVWSAEEGYPGDPDYREFYRDIGYDLDYDYIKP
YIHPDGIRVNTGIKYYRITGKTDDKEPYDPEWAREKAAEHAGNFVFNREKQLEYLASLMDRPPIVVAPYD
AELFGHWWFEGPQFLEFLFRKLAYDQDEVELITPSDYLDEYPENQVVTPPESSWGEGGYHEVWLNGSNDW
IYRHLHKAEERMIELARRFPDADGLERRALNQAARELLLAQSSDWAFIMTTGTAVEYAVRRTKEHLNRFN
RLYEMLESGKIDEEWLEELEEKDNIFPDIDYRVYRSEA
>gnl|CDD|441153 COG1544, RaiA, Ribosome-associated translation inhibitor RaiA [Translation, ribosomal structure and biogenesis]
KINITGRNVEVTDALREYVEEKLEKLEKYFDRIISADVTLSVEKNRRFKVEITLHVPGPVLRAEAEAEDM
YAAIDLAVDKLERQLRKYKEKLKDHRRRRAP
>gnl|CDD|441154 COG1545, COG1545, Uncharacterized OB-fold protein, contains Zn-ribbon domain [General function prediction only]
FWRALAEGRLLGQRCPACGTVYFPPRPVCPHCGSEDLEWVELSGRGTVYSYTVVHRPPPPFEDEVPYVVA
LVELDEGVRVLGRLVGVDPEDVRIGMRVRVVFRPIDEDGRTLPVFR
>gnl|CDD|441155 COG1546, PncC, Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]. Nicotinamide mononucleotide (NMN) deamidase PncC is part of the Pathway/BioSystem: NAD biosynthesis
LESLAEVVGELLRERGLTLATAESCTGGLIAAALTDVPGSSAVFDGGFVTYSNEAKEELLGVPAETLEKH
GAVSEEVAREMAEGARRLSGADIAVAVTGIAGPGGGTPGKPVGTVYIALAGPGGVVVRRLHFGGDREAVR
EQAVRAALDLLREL
>gnl|CDD|441156 COG1547, YpuF, Predicted metal-dependent hydrolase [Function unknown]
MDDHTRLPRALREGVRLFNAGDYFEAHEVLEELWKEAGEPEKDFLQGLIQLAVALYHLRRGNWRGARRLL
GRALEYLEGYPPDYRGVDVEEL
>gnl|CDD|441157 COG1548, MfnF, Methanofuran synthetase MfnF, hydantoinase/oxoprolinase family [Coenzyme transport and metabolism]
MNMKIIGWDIGGANLKAALLDGGRVVAVVQHYCPLWKGLDRLDEALAELLAKLGSADRHAVTMTGELADC
FADRAEGVRFIVDAVEEAFPCGPVRFYAGDGGFVTPEEAAAHPLDVASANWLASARLAARLIPDGLLVDI
GSTTTDIIPIKDGRVAARGRTDAERLASGELVYTGVLRTPLMALADSVPFRGRWTPVSAEYFATTADVYR
LLGELDEEADTCPTADGRGKSVEASARRLARMVGADLEEISEEDWRALAQYFAEAQLRQITEAVERVLSR
AALPALAPVVGAGIGRFLAAELARRLGRPYIDLAELLGKEASDCAPAVAVALLAERYLS
>gnl|CDD|441158 COG1549, ArcS, Archaeosine tRNA-ribosyltransferase, contains uracil-DNA-glycosylase and PUA domains [Translation, ribosomal structure and biogenesis]
MEYFEVHKRDGAARIGELRLEDPVRTPALVDDVLVDAGSLWAAEDDLTVLPHRALPPGTPDEVVESFAVD
YPDVDGPSAAVVSPETAVEGADAYVLSNAGGLVGHARAFVDAIVKLREAIPPDTALYLPGVATPSNVALL
VYLGVDLFDDTRAKLAGTQGIYLTPEGEYFLDDLDELPCACPACQGPREFDREDLAEHNRNALEAELALV
RERIRAGRLREYVEGQARHDPWLTAALRLLDREYDYLEERTPVVRGSELLANSDESLRRPEVQRFAERVT
ERYRPPFKDVLVLLPCSAKKPYSTSQSHRQFIDAIGSARYRVHEVILTSPLGVVPRELELTYPAAHYDIP
VTGEWSEEEIEFVAEVLERYLEKNDYPRVIAHVPGDYREICERVAEKLGIDIEYTVVGHPTSPESLSNLK
EALEGEEKYSKRERRHNTVRAIADYQFGKGAGDALFPDDIVVKGRYPKLQVFRGKEQLATLVPQYGMLSL
TLEGAERLVDSPTYRVEIDDFVPKGSVLAPGVVDADPRIRPGDEVVVEGPKAFGVGRAAMSGPEMVESTR
GVAVKVRHVKKR
>gnl|CDD|441159 COG1550, YlxP, Stress-induced protein YlxP, DUF503 family [Function unknown]
VIGVLELELRLPGAHSLKEKRSVVKSLIDRLRNRFNVSVAEVGDQDLWQRAVIGVAVVSNDRAHVESVLD
KVERFIESNPEAEILDVEREILG
>gnl|CDD|441160 COG1551, CsrA, sRNA-binding carbon storage regulator CsrA [Signal transduction mechanisms]
LVLTRKVGESIVIGDDIEITVLEIKGGQVRLGIEAPRDVPIHREEIYERIQEENKEAAEAS
>gnl|CDD|441161 COG1552, RPL40A, Ribosomal protein L40E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L40E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
DMAKFEEAEKRRLNKKICMRCGARNPIRATRCRKCGYKNLRPKKKERRAK
>gnl|CDD|441162 COG1553, DsrE, Sulfur relay (sulfurtransferase) complex TusBCD TusD component, DsrE family [Inorganic ion transport and metabolism]
MKYLLIVNGPPYGSQAAYSALRFAEALLEKGHEVDRVFFYQDGVLNANALQKPPSDEYNLVQMWQELAAQ
HGVELVVCGACALRRGITDEENLIEGFELSGLGELAEATLEADRVITF
>gnl|CDD|441163 COG1554, ATH1, Kojibiose phosphorylase YcjT [Carbohydrate transport and metabolism]
VDPWSLVEEGFDPEDEGLRESLFSLGNGYLGTRGNFEEGYSGDTPGTYLAGVYERDPTRVGEWKYGYPEY
GQTLVNAPNWLGIRLRVDGEPLDLATGELLDYERELDMREGVLTRSFVWRDPAGRRVRVESRRFVSMADR
HLAAIRYEVTPLNFSGPITIRSALDGRVTNEDDDPRRYRALDEKHLEPLEKEAEDDRALLVARTRQSGIR
VATAARHRVENGENVEAEREVEEEEDLVAETYTVDLKPGETLRLEKYVAYHTSRDHAISELADAAERALA
RARETGFDELLAEQREAWADFWERADVEIEGDPEAQQAIRFNLFHLLQTASGRDEDLGIGAKGLTGEGYG
GHYFWDTEIFVLPFLLYTDPEVARNLLRYRYNTLDAARERARELGLKGALYPWRTINGEECSAYWPAGTA
QYHINADIAYAIWRYVRATGDEEFLAEYGAEVLVETARFWASLGHFDEEKGRYHIHGVTGPDEYHAGVNN
NAYTNVMARWNLRYAAEALDKLPEERYAELAEKLGLSDEEVAKWKDIADKMYLPYDEELGIIPQFDGFLD
LEEWDVEDYPADYLPLLLHYHPDRIYRYQVIKQADVLLAFYLFGDEFTLEEKRRNFDYYEPRTVHDSSLS
ACVHAIVAAELGDRELAYEYFLRAARLDLDDLQGNTTEGLHIASMAGTWMALVRGFGGMRVRDGRLSFNP
RLPEEWESLSFRIRYRGRRLRVEVTHDEVTYTLESGEPLTIKVRGEEVTLTPGEPVTVPLP
>gnl|CDD|441164 COG1555, ComEA, DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]
APASASAAAGGKVDINTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVEDLLEVKGIGPKTLEKLKPY
LT
>gnl|CDD|441165 COG1556, LutC, L-lactate utilization protein LutC, contains LUD domain [Energy production and conversion]
SAREAILARIRAALGRPPPPPLPRGEPPLFRLLSADDLVELFVERLEAVGGEVVRVTTEAELPAALAELL
AEAGLKRIVVPEPGLPAALQLAWDPLEELEDPAALEDADVGITGAEFGIAETGTIVLDSGPDQGRALSLL
PEHHIVVVPASQIVPTMHEAYARLREKAGLPRNITFISGPSKTADIEQTLVLGAHGPRRLHVILVE
>gnl|CDD|441166 COG1558, FlgC, Flagellar basal body rod protein FlgC [Cell motility]
MSLFSAFDIAGSGLTAQRLRLNVIASNLANANSTRTSDGGPYRRKQVVFEAVLDRAGSGAAGVRVAGIVE
DDSPFRLVYDPGHPDADADGYVRYPNVNVVEEMVDMISASRSYEANVEVINTAKSMLLKTLEIGR
>gnl|CDD|441167 COG1559, MltG, Endolytic transglycosylase MltG, terminates peptidoglycan polymerization [Cell wall/membrane/envelope biogenesis]
KRKKILLLLALLLLLLLLAGAFYVQQYLLAPLPGPGEEVVVEIPPGASLSQIADQLEEAGVIKSARAFRL
AARLNGYAGKIKAGEYELKPGMSAAEILDKLRSGKVVQVKVTIPEGLTLEQIAARLAKAGLLDGEDFLAA
AEAFLAALGLPGESLEGYLFPDTYEFPPGTTAEEILKRMVARFDKVLTEAWAARAKDLGLTPYEVLTLAS
IVEKETGVAEERPKVAGVFYNRLKKGMRLQSDPTVIYGLGDFGGRLTRKDLETDSPYNTYKNKGLPPGPI
ANPGRAAIEAALNPAKTDYLYFVADGDGGHVFSKTLAEHNRNVRKYRRWLRER
>gnl|CDD|441168 COG1560, LpxP, Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and metabolism]. Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) is part of the Pathway/BioSystem: Lipid A biosynthesis
LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETL
RLWRLSPERLRKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRGYPVTAVYRPLKNPLLDR
LIRRGRERFGGELIPRKDGVRALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVPAATPTGPARLARRTG
APVVPVFARRLPDGRGYRLEIEPPLEDFSEDVEADTQRLNRALEAWIREHPEQWLWLHRRW
>gnl|CDD|441169 COG1561, YicC, Uncharacterized stationary-phase protein YicC, UPF0701 family [Function unknown]
MIRSMTGFGRAEAETDGGTLTVEIRSVNHRYLDLSLRLPRELRALEPEIRELIRKRLSRGKVEVSLSLER
AGAAAAALRINEALLKAYLEALKELAEELGLAGPISLDDLLRLPGVLETEEEEEDLEELWAALLAALDEA
LDDLVAMREREGAALAADLLERLDAIEELVAEIEERAPEVVEAYRERLRERLEELLEGVELDENRLEQEV
ALLADKADITEELDRLKSHLKQFRELLEKGGPVGRKLDFLMQEMNREANTLGSKSNDAEITQLVVELKVE
IEKIREQVQNIE
>gnl|CDD|441170 COG1562, ERG9, Phytoene/squalene synthetase [Lipid transport and metabolism]
LAAAYAYCRAITRRHSRSFYLASLLLPPELRRAVYALYAFCREADDIVDEVSDPAEREARLDWWRAELDA
AYAGGPADHPVLAALADTVRRYGLPRELFLDLIDGMEMDLTKTRYATFAELEDYCYRVAGVVGLLLLRVF
GADDPEALAAADALGVALQLTNILRDVGEDARRGRVYLPLDDLARFGVTEEDLLAGRASPALRALLRFLA
ARARALLREALAGIPALPRRARRAVLLAAALYRAILDKIERRGYDVLRRRVRLSRLRKLWLLWRALLR
>gnl|CDD|441171 COG1563, COG1563, Uncharacterized MnhB-related membrane protein [General function prediction only]
MILLIDLILLALLVISAIAAVLQKDLLAAVILFGIFSLLAALLFVLLGAPDVALTEAAVGAGLSTVLFLL
ALRKTGRVEKG
>gnl|CDD|441172 COG1564, ThiN, Thiamine pyrophosphokinase [Coenzyme transport and metabolism]. Thiamine pyrophosphokinase is part of the Pathway/BioSystem: Thiamine biosynthesis
MKALILAGGELPDPELLKELLEKADFIIAADGGALHLLELGIKPDLIIGDFDSISEEELEQYKEKGVEII
IFPPEKDETDTELALRYALERGADEILILGATGGRLDHTLANLSLLARYAEKGIRIVLIDENNEIFLLPP
GSLTLEGPPGTYVSLIPLSDPVTGLTLEGLKYPLDNATLTFGSSLGISNEAIGDEATISVESGILLVIL
>gnl|CDD|441173 COG1565, MidA, SAM-dependent methyltransferase, MidA family [General function prediction only]
MALAHSTALAALIRARIAAAGGPIPFARYMELALYHPGLGYYSTGRDKFGAAGDFITAPELSPLFGELLA
RQLAQVWEALGAPAPFTLLELGAGRGTLAADILRALRALLPGFYAALRYHIVELSPDLRARQQETLAAFA
PARVRWLDSLEELPEDFSGVVLANEVLDALPVHQFVRTGGGWRERGVGLDDGGLVFGLRPLSDPELLAAL
PALLAPLPEGYVTEVNLAAEAWLATLAARLARGAALLIDYGYPASEYYHPQRSGGTLQCYYRHRAHDDPL
ANPGLQDITAHVDFTALAEAAEAAGLEVLGYTTQGLFLLALGLLERLAALSAGDPAAALALRAAVKRLTL
PAEMGELFKVLALGKGLDPPPLPGFS
>gnl|CDD|441174 COG1566, EmrA, Multidrug resistance efflux pump EmrA [Defense mechanisms]
MKALKKRRLLALVLLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKG
QVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALY
KKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTI
RAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKV
TSISPGAGFTSPPKNATGNVVQRYPVRIRLDNPDPEPLRPGMSATVEIDTE
>gnl|CDD|441175 COG1567, Csm4, CRISPR-Cas system type III CSM-effector complex subunit Csm4, RAMP superfamily Cas5 group [Defense mechanisms]. CRISPR-Cas system type III CSM-effector complex subunit Csm4, RAMP superfamily Cas5 group is part of the Pathway/BioSystem: CRISPR-Cas system
MKMKIYKLKFKPPLHFGTPGIGLEESSEFLHSDTLFSALCWALALLYGEEDLEELLEEFKENPPFRLSSA
FPYIGEEYFLPKPLLPPKLLPDDGLSEDRKKLKKIKYIPLELFEKLLKGEKDEALDEEIKGSFKKPPLFK
IQERPRVAIDRLTGTGQLYYVGQVFFAEGAGLYFLADFEEESREKFEAALRLLGDEGLGGDRSIGLGKFE
VEFEEIELDEAEEGNAYMLLSLYSPTDEELENDLERAYYQLVTRGGYIGSPLAGRSPRKKPVYMFKEGSV
FKKKPEGKLLDVSPDEGGHPVYRYGYALTLPVR
>gnl|CDD|441176 COG1568, BpsA, Aminopropyltransferase BpsA, N(4)-bis(aminopropyl)spermidine biosynthesis [Secondary metabolites biosynthesis, transport and catabolism]
MKIIGKIVKVAENTKIGEGERIVEQILRALYSGPISFWELIRLSDLPLPVVAEILKELLKEGLLEREGGG
IRLTEKGKELVENLGIKPLKDLTCPLCEGRGIVLDEEFEELLEKFKEIAKNRPEAIVDYDQGFVTPETTV
RRAALMDSRGDLEGKRILVLGDDDLTSIALALTGLPRRITVVDIDERLLDFINEVAKEEGLDIEAVHYDL
RNPLPEELRGKFDVFFTDPPETLEGLKLFLSRGVEALKGEGGAGYFGLTHSEKSPEKWLEIQKLLLNMGL
VITDIIPDFNEYEGAEIYHEEYRAWKLAPVKVDVIWYTSDLYRLETTSGPKPLIEGIKFDEEIYTDEEAS
TTVR
>gnl|CDD|441177 COG1569, COG1569, Predicted nucleic acid-binding protein, contains PIN domain [General function prediction only]
MRVVLDTNVLVSALLSPDGAPARLLRAALAGRFTLLVSAAILEELERVLARPKFKLSPEEREELLAALLA
LAELVEPTPLWRPICRDPDDNKFLELAVAGGADYLVTGDKDLLSLARFFGIRILTPAEFLELLRPK
>gnl|CDD|441178 COG1570, XseA, Exonuclease VII, large subunit [Replication, recombination and repair]
SNEKILSVSELNRYIKRLLERDFGNVWVEGEISNLKRHSSGHLYFTLKDEDAQIRCVMFRGRARRLKFRP
EDGMKVLVRGRVSVYEPRGDYQLIVEDIEPAGLGALLAAFEQLKEKLAAEGLFDPERKRPLPFLPRRIGV
VTSPTGAAIRDILTVLRRRFPAVEVLLYPVLVQGEGAAAEIAAAIERANARPEVDVIIVARGGGSLEDLW
AFNDEAVARAIAASPIPVISAVGHETDFTIADFVADLRAPTPTAAAELAVPDRAELLARLDQLRARLRRA
LRRRLERERQRLDRLRRRLVLASPERLLEQRRQRLDELEQRLRRALRRRLERKRQRLEALAARLEALSPL
ATLARGYAIVRDADGKVVRSAAQVKPGDRLTIRLADGELEATVTEVEKEQ
>gnl|CDD|441179 COG1571, TiaS, tRNA(Ile2) C34 agmatinyltransferase TiaS [Translation, ribosomal structure and biogenesis]. tRNA(Ile2) C34 agmatinyltransferase TiaS is part of the Pathway/BioSystem: tRNA modification
RVIIGIDDTDSREGGCTTYLAANIAEELEKEGGLVDYPRLVRLNPNVPYKTRGNAAVALEFAVDPEEKEK
LLEIARDLVEEYSEDDESTNPGIVVLEGDIPEELKEFYRKALREVVTIDEAEKVAEKNGIEIIGFKGGRG
IIGALAAIGAWLDPLEKLAVLELAPTVEIERDLEPGWYEVPPSARRHLAKPLVRGGFDA
>gnl|CDD|441180 COG1572, COG1572, Serine protease, subtilase family [Posttranslational modification, protein turnover, chaperones]
VFDGVLVLESLSTADALSLEAGTALAAAVSSATLLGAGLATGTTATLVATNLGAGATSTGTAAADGDAAL
GSLSTTSTNTASSTNVLSTDVGTGPNTGAQTATATGGYADGNAGESNENNNTVAVLISSGKPDLVVTSVT
APSTLTPGTTITVSVTVNNQGSAPANGSSVDFDASDTLLGSFTVASLTLAAGASYTFNPTLTLPVTASGN
YYLLVVADPDNYVLETNETNNTTAAAEITVSGTPPDLTVTSVTAPSTVVEGDTITVSATVKNQGTAAAGA
TTVAFYLSGDPVGTASVGALAAGASYTVTVTITLPANAGTYYLLAVVDPDNQVAESNETNNVASSAITVV
GPPPPDLVVTSVSAPSTATAGSSVTVSVTVKNQGTAAASGFTVTLYLSGDATTDLTYVGSLAAGASYTVT
ISVTTASGQYYLLVVADPDNYVGESNENNNVFAVSINVN
>gnl|CDD|441181 COG1573, Udg4, Uracil-DNA glycosylase [Replication, recombination and repair]
RAAAAAAETLEELREAVAACRRCPLVETRTQPVFGEGDPDARLMIVGEAPGAGEDRTGRPFVGRAGQLLD
KMLAAAGLAREDVYITNAVKCRPPGNRKPTPEEIAACRPFLEREIALIRPKVIVALGATAAQALLGAGER
ITRLRGKWHELPGGIPLLPTYHPSYLLRNPTTKREAWEDLLAARALLGE
>gnl|CDD|441182 COG1574, YtcJ, Predicted amidohydrolase YtcJ [General function prediction only]
MKLAAAAADLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIDLGGKTVLPGFID
AHVHLLGGGLALLGVDLSGARSLDELLARLRAAAAELPPGEWILGRGWDESLWPEGRFPTRADLDAVSPD
RPVVLTRVDGHAAWVNSAALELAGITADTPDPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELR
AALRAALRELASLGITSVHDAGLGPDDLAAYRELAAAGELPLRVVLYLGADDEDLEELLALGLRTGYGDD
RLRVGGVKLFADGSLGSRTAALLEPYADDPGNRGLLLLDPEELRELVRAADAAGLQVAVHAIGDAAVDEV
LDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELGVIASMQPTHATSDGDWAEDRLGPERAARAYPF
RSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGRGLGPEERLTVEEALRAYTIGAAYAAFEEDEK
GSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEAE
>gnl|CDD|441183 COG1575, MenA, 1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]. 1,4-dihydroxy-2-naphthoate polyprenyltransferase is part of the Pathway/BioSystem: Menaquinone biosynthesis
AWLEAARPRTLPAAVAPVLLGTALAYYETGSFNWLLFLLALLAALLLQIGVNLANDYFDYKKGTDTEERV
GPSRVIVSGLLSPKQVLRAALLLLALALLLGLYLVLLSGWPLLLLGLLGILAAIFYTGGPFPLGYRGLGE
LFVFLFFGLVAVLGTYYVQTGTLSWAALLASLPVGLLSAAVLLANNLRDIETDRAAGKRTLAVRLGRKRA
RRLYAALLLLAYLLILLLVLLGLLPPWALLALLSLPLALKLVRRVLRGAKPEALIPALKNTALLNLLFGL
LLALGLLLGR
>gnl|CDD|441184 COG1576, RlmH, 23S rRNA pseudoU1915 N3-methylase RlmH [Translation, ribosomal structure and biogenesis]. 23S rRNA pseudoU1915 N3-methylase RlmH is part of the Pathway/BioSystem: 23S rRNA modification
MKITIIAVGKLKEKWLKEGIEEYAKRLPRYGKLELIEIPDEKRPKNADEEQIKEKEGERILAAIPPGAYV
IALDERGKQLTSEEFAEKLEKWRDSGRSDLAFVIGGADGLSPEVRARADLKLSLSKMTFPHQLVRLILAE
QLYRAFTILRGHPYHR
>gnl|CDD|441185 COG1577, ERG12, Mevalonate kinase [Lipid transport and metabolism]. Mevalonate kinase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
APGKLILFGEHAVVYGQPAIAVAVDRRATVTVEPSDDDKLRIESPDLGGTLDLDPLADAALRYIKAAIEA
ALEYLGLPLKGFDIEIDSEIPRKRGLGSSAAVAVAVIRALAAFYGVELSKEELFKLALEAEKIVHGNPSG
LDTAASTYGGPIYYQRGDRAEPLELPKNLPLVVGDTGVPASTKELVAKVRKLKERNPELYEAFLEEIGDL
VEEAIEALEEGDLEALGELMNENHGLLRALGVSTPELDRLVEAARKAGALGAKLTGAGGGGCVIALA
>gnl|CDD|441186 COG1578, DUF89, House-cleaning carbohydrate phosphatase, DUF89 family [Defense mechanisms]
KIHPECIPCLLRQALRAARLATDDEELQKRILREVLEILAELFDPDLTPPEIATEVHRIIYELLGNDDPY
KELKERSNELALELLPELKERIESSEDPLETALKLAVAGNIIDFGVKGVSFDLEETIKEVLEKPFAIDDT
EELKERLKKAKRVLYLGDNAGEIVFDKLLIEELKKLGLEVTYAVRGGPILNDATLEDAKEAGLDKVARVI
TTGSDAPGTVLEECSEEFKELFDEADLIISKGQGNYETLSEEKDKPIFFLLKAKCEVVARDLGVPVGDLV
FK
>gnl|CDD|441187 COG1579, DR0291, Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only]
AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE
VEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL
EEKKAELDEELAELEAELEELEAEREELAAKIPPELLALYERIRKRKNGLAVVPVEGGACGGCFMELPPQ
ELNEIRAADEIVRCPNCGRILYREEE
>gnl|CDD|441188 COG1580, FliL, Flagellar basal body-associated protein FliL [Cell motility]
MAEAKKGGKKKLILIILALVVLLLAAGGGAYFLLGSGAAAEAAEAAAAEPKPPPVYVPLDPFTVNLADGG
RDRYLKVGITLEVADEKAAEELEKHMPEIRDALLMLLSSKTAEDLSTPEGKEKLREELLERINEVLGKEG
KVEDVLFTEFVVQ
>gnl|CDD|441189 COG1581, AlbA, DNA/RNA-binding protein AlbA/Ssh10b [Transcription]
ENVVFIGKKPVMNYVLAVLTQFNNGAKEVIIKARGRAISRAVDVAEIVRKRFLGGVKIKDIKIGSEELES
EDGKTRNVSTIEIVLAK
>gnl|CDD|441190 COG1582, SwrD, Swarming motility protein SwrD [Cell motility]
MIKLTRLNGEEFVLNADLIERIEATPDTVITLTNGKKYVVKESVDEVIEKVIEYRRRIGAL
>gnl|CDD|441191 COG1583, Cas6, CRISPR/Cas system endoribonuclease Cas6, RAMP superfamily [Defense mechanisms]. CRISPR/Cas system endoribonuclease Cas6, RAMP superfamily is part of the Pathway/BioSystem: CRISPR-Cas system
MRIKLKLESDKKIILPINYNYLLQSFIYNLLSESDPELAKFLHDKGFGKRRFKLFTFSRLFGKKFKINKE
GIIIFGGPVSLYISSPDPEFIENLYNGLLKNKEFRLGDNRFEVEEVEVLPEPEITNEVVFKTLSPIVVRS
TNNGKKKTYYLSPEDEEFSELLKENLKKKYEALYGEEPDEEEFDIEPLKVKKKVVKYKGTYIKGWLGPFK
LEGDPELLKFAYDAGLGEKNSQGFGMV
>gnl|CDD|441192 COG1584, SatP, Succinate-acetate transporter SatP [Energy production and conversion]
AVKDKTANPAPLGLFGFAMTTFLLSLHNAGWFPGSALPVLAMALFYGGLAQLIAGIMEFKKGNTFGATAF
TSYGAFWLSLAGLLLLPKFGLAAAADAAALGWYLLAWGIFTLFMTIATLKTNKALQVVFLLLDILFFLLA
LGDFTGSAALTTIAGYEGLICGLLAWYLAAALVLNETFGRTVLPLGK
>gnl|CDD|441193 COG1585, YbbJ, Membrane protein implicated in regulation of membrane protease activity [Posttranslational modification, protein turnover, chaperones]
MSALPWLIWLILGLLLLIAELLTPGFFLLWFGLGALAVGLLALLGLSLWLQLLVFAVLSLLLLLLWRRLL
KRRLRSDAPLLNTRVDALIGRTATVVEPIDNGRGRVKLGGEEWRARSEDDLPAGTRVRVVAVEGNTLIVE
PVE
>gnl|CDD|441194 COG1586, SpeD, S-adenosylmethionine decarboxylase [Amino acid transport and metabolism]
KFLGKHLIADLYGCDPELLNDAERLEEILVEAAEAAGATVLGVAFHKFEPQGVSGVVLLAESHISIHTWP
EYGYAAVDVFTCGDDIDPEKALEYLKEAFGADKVEVTELKRGFTRDIK
>gnl|CDD|441195 COG1587, HemD, Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]. Uroporphyrinogen-III synthase is part of the Pathway/BioSystem: Heme biosynthesis
LAGKRVLVTRPAPQAEELAALLEALGAEVVELPLIEIEPLPDPAALRAALERLGDYDWVIFTSANAVRAF
FEALEELGLRLAGLKIAAVGPKTAAALRAAGLKVDLVPEGFTSEGLLELLQALAGKRVLIPRGDGGREDL
AETLRAAGAEVDEVEVYRTVPPDDLPEELLEALAAGEIDAVLFTSPSTVRNLLELAPDAGLAALARVRIA
AIGPRTAEAARELGLKVVI
>gnl|CDD|441196 COG1588, POP4, RNase P/RNase MRP subunit p29 [Translation, ribosomal structure and biogenesis]
MITPENILRHELIGLEVEVVESTNPSLVGISGRVVDETKNTLVIETEDGVKRVPKSGATFEFTLPDGESV
TVDGSLLLGRPEERLKKLIKKKWR
>gnl|CDD|441197 COG1589, FtsQ, Cell division septal protein FtsQ [Cell cycle control, cell division, chromosome partitioning]
MSKLRLRRKRRRRRRLRLLLLLLLLLLALLVWLLLFSPLFPVREVEVEGNSHVSAEEIRAALGILLGGNL
FTLDLDAIRERLEALPWVKSASVRRRWPDTLVIEVTEREPVARWNTGGGYYLVDADGVVFEAVSAEPPAD
LPLLTGPDGSEKAVLALLELLAALPELRLQISEISLSSRGRWTLTLDDGVEVRLGRSEDLAEKLARLAAL
LPQLLAGKGIAYIDLRYPDGPAVRLKEEAAE
>gnl|CDD|441198 COG1590, Tyw3, tRNA(Phe) wybutosine-synthesizing methylase Tyw3 [Translation, ribosomal structure and biogenesis]. tRNA(Phe) wybutosine-synthesizing methylase Tyw3 is part of the Pathway/BioSystem: tRNA modification
NTMMWEERKKEALERLEEDLEIGYVDPDIIDLLDKINSLPDYYTTSSCSGRITVVDAPYPWDKENSKIVF
KWHRPVTVDELLEALKKPSERRLWLIVQGPILHVYTRDLEEAKKLLKIAREAGFKHSGIKSISDKGVIVE
IRSGERMDVPLRENGKLIVDEEYLKRIVDVANEKLLKGKRRLKRLYEALRSLLP
>gnl|CDD|441199 COG1591, COG1591, Holliday junction resolvase Hjc, archaeal type [Replication, recombination and repair]
MMNKRKGSRAERELVNKLWEAGFAVIRAPASGSATKRPLPDIVAGKGGKILAIEVKSRSKDKIYIEKEQV
EKLLEFARRFGGEPFIAVKFKRKGWRFFPPEDLEETDGGNYKIDKETALEGLDLEELVGKIEQKTLDEFL
>gnl|CDD|441200 COG1592, YotD, Rubrerythrin [Energy production and conversion]
MSLKGTKTEKNLLAAFAGESQARNRYTAFAKKAKKEGYPQIARLFRATAEAEKEHAKNHFKLLKGAAGPV
GIGDTAENLKAAIEGETYEWTEMYPEFAKVAEEEGFKEAARSFRYAAEAEKIHAERYKKLLENLEAGKVF
KKDEEVVWVCPVCGYIHEGKEAPEKCPVCGHPKSYFELFA
>gnl|CDD|441201 COG1593, DctQ, TRAP-type C4-dicarboxylate transport system, large permease component [Carbohydrate transport and metabolism]
MIGLLLFGLLLVLLLLGVPIAFALGLAGLAGLLLLGDLPLSVLAQRMFSGLDSFPLLAIPLFILAGELMN
RGGISRRLFDFANALVGHLRGGLAHVNVLACALFAAISGSSVATAAAIGSILIPEMKKRGYDKGFAAGLT
AASGTLGILIPPSIPMIIYGVLTEVSIGKLFLAGIVPGLLLALLLMIVIYIIARRRGYPRGERASWRERL
RALRDALPALLLPVIILGGIYGGIFTPTEAAAVAVVYALLVGVFVYRELTLKDLPEALLETARTTAMIML
IIAGASVFGWFLTLEGIPQALAEWILGLGLSPWVILLLINLLLLVLGMFMDGLSAILILVPILLPIATAL
GIDPVHFGIIMVVNLEIGLITPPVGLNLFVASGIAGVPLEEVFRGVLPFLLAMLVVLLLLTYFPALSLWL
PRLLGG
>gnl|CDD|441202 COG1594, RPB9, DNA-directed RNA polymerase, subunit M/Transcription elongation factor TFIIS [Transcription]. DNA-directed RNA polymerase, subunit M/Transcription elongation factor TFIIS is part of the Pathway/BioSystem: RNA polymerase
KFCPKCGSMMKPKDGVLVCPKCGYEEPRDEEAEAKYVSTEEQEDKEIIVVEEEEVEGLPTTKVICPKCGN
DEAYWWLKQTRSADEPETRFFRCTKCGHTWREY
>gnl|CDD|441203 COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 family [Transcription]. DNA-directed RNA polymerase specialized sigma subunit, sigma24 family is part of the Pathway/BioSystem: RNA polymerase
MSSDEELLERLRAGDEAAFEELYERYRPRLYRYARRLLGDRADAEDLVQETFLRLWRKLDSFRGRGSFRA
WLYRIARNLAIDHLRKRRRRRELLDELAEELPDEAADPEEALEAEELLEALLAALERLPPRQREVLVLRY
LEGLSYAEIAEILGISEGTVKSRLSRARKKLREALEEEGAL
>gnl|CDD|441204 COG1596, Wza, Periplasmic protein Wza involved in polysaccharide export, contains SLBB domain of the beta-grasp fold [Cell wall/membrane/envelope biogenesis]
MRLLLLALLLAGCAAVPPDYRLGPGDVLRITVWGEPELSGEVTVDPDGTISLPLIGPVKVAGLTLEELEE
EIEERLAKYLKDPQVTVSVAEYRSRRVYVLGEVNRPGRYPLSSGLTLLDAIALAGGLTERADLRNVQLIR
GGKEVVYTVDLYDLLLGGDPSQNIRLQPGDVIFVPEAGRRVF
>gnl|CDD|441205 COG1597, LCB5, Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only]
AMMRALLIVNPASGRGRAARLLERLVAALRAAGLEVEVLETESPGDATELAREAAAEGADLVVAAGGDGT
VNEVANGLAGTGPPLGILPLGTGNDFARALGIPLDPEAALEALLTGRTRRIDLGRVNGRYFLNVAGIGFD
AEVVERANRALKRRLGKLAYVLAALRALLRYRPFRLRIELDGEEIEGEALLVAVGNGPYYGGGLRLAPDA
SLDDGLLDVVVVRPLSRLRLLRLLPRLLRGRHLRHPGVRYFRAREVEIESDRPLPVQLDGEPLGLATPLE
FEVLPGALRVLVPAD
>gnl|CDD|441206 COG1598, HicB, Antitoxin component HicB of the HicAB toxin-antitoxin system [Defense mechanisms]
KYPAIIEKDEDGGYVAEVPDLPGCVTQGDTLEEALENAKEALELHLEALLEDGEPIPEPSSIEET
>gnl|CDD|441207 COG1599, RFA1, ssDNA-binding replication factor A, large subunit [Replication, recombination and repair]
DIEEHYEELADALGVSKEEFEVKISDLSPGDRDVNVEGRVLEIGEERTFDRKDGSEGRVQSGVIGDETGR
IRFTLWDDKADLELEEGDVVRIENAYVREFNGGPELNLGERTTIEKLDEDVEVIPDEERTPIGDIEPGGT
VSVTGTIVSVRPGSGFIKRCPECNRVLQDDGQCREHGKVRGEYDLRIKAVLDDGTGTIRVVLWGELTEEL
YGIDLGDAIEIADDALDQGVVAEEIREKLLGRYYRVRGNLSDRYGLLADSIELSADDPAERAEELLAEVE
GD
>gnl|CDD|441208 COG1600, QueG, Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]. Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification
MSDLMELKEEIKAWARELGFDLVGIAPADPLPEAEERLEEWLAAGYHGEMGYMERHIEKRADPRELLPGA
KSVISLALNYLPEEEVSDPDRGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERA
LAERAGLGWIGKNTNLITPEFGSWFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDAR
RCISYLTIELKGPIPEELRPKMGNRIYGCDDCQDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEA
EFRERFGGSAIRRIGRERLLRNAAIALGNSGDPAAVPALEALLDDPSPLVREHAAWALGRLGGRE
>gnl|CDD|441209 COG1601, GCD7, Translation initiation factor 2, beta subunit (eIF-2beta)/eIF-5 N-terminal domain [Translation, ribosomal structure and biogenesis]. Translation initiation factor 2, beta subunit (eIF-2beta)/eIF-5 N-terminal domain is part of the Pathway/BioSystem: Translation factors
DMDYEELLDRAYEKLPEKVGSGERFEVPEPEVRIEGNRTIIRNFSDIADALNRDPEHLLKYLLKELGTAG
SIEGGRAILQGKFSPEDINALIDRYVKEYVICPECGSPDTRLVKEGRVLMLKCEACGARRPVK
>gnl|CDD|441210 COG1602, NreA, Archaeal DNA repair protein NreA [Replication, recombination and repair]
MRLDEYELCVRCKGRKRLCGLPSCPILERFRSVESKFSKIVSGDSIFGSSPPSVFVGRYGYPKVSIGPLV
PPGDEGDASIYETPEEWYGLSIEDILSYRSSLVRGNTRVDVDDVHDPDKLLEEIQEVAISDRPVDVEVGL
KKPPKPDLKFDDVLTPMGPSAPAEKIDLTENPKVPRKVEKLVYDDDLKAEDAIIELYRRGFDVYYIQRIL
SAGLLGRGKNRRLVPTRWSITAVDDTIGKYLRGEIRDYPSIDEVEVYSGEYLGNRFWVILAPGSWSFELV
EAWAPGSVWNPDGSEVWIESDYEGYEGRKGYAETAGGYYAARLAVLEHLASRRRQAKALVLREITPEYWA
PVGVWQVREGVRNALEGEPGKFETLEEALRYVSKRLRVPLKDWLRKSKLLKGIRKQRTLDDFLK
>gnl|CDD|441211 COG1603, RPP1, RNase P/RNase MRP subunit p30 [Translation, ribosomal structure and biogenesis]
MKMYDLAVHAYPDGDSTVARLALTAKRLGYDGIVVRNHSDARADYDAEAIREEYGIDVVRGVEIRADNPS
KLSGAVGNYRPKVDVVAVHGGDEKINRAAVENPRVDVLAHPMTARDGGFNHVLAKAAAENGVAVEFDLGP
LLRARGGRRVRALQRLRKLLELVRKYDFPLVVSSGARSHLDLRAPRELIALGELFGFEEEEAEEGLSEWP
RIAERNRRRESFIEPGVEVGE
>gnl|CDD|441212 COG1604, Cmr6, CRISPR/Cas system CMR subunit Cmr6, Cas7 group, RAMP superfamily [Defense mechanisms]. CRISPR/Cas system CMR subunit Cmr6, Cas7 group, RAMP superfamily is part of the Pathway/BioSystem: CRISPR-Cas system
ISNLGLYFDKYLPEEKKEENKSSLKREILEELVKAKGDLDLYKELFERQERLLESLGYRVITLEAKTKSR
LVVGLGNPSPLEVGLALHHTYGVPYIPGSSIKGVVRAAAEELLAEADEDDEAIDKLFGTEPGDEEASAGK
VIFFDAYPVPGDGPLLEVDVITPHYGEYYQGEEPPEDWDSPVPVPFLTVAPGVTFRFAIAIRREELGKDL
LKLALELLKEALEELGIGAKTAVGYGRFE
>gnl|CDD|441213 COG1605, PheA, Chorismate mutase [Amino acid transport and metabolism]. Chorismate mutase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
MSESESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDP
EFVEAIFREIISESIALQEKLLAEVAYLGPEGGFTGQAAGKHFGGSAASLPAAAIDEVFREVEAGGAAYG
VVPVENSTEGGVVETLDLLLASPLKI
>gnl|CDD|441214 COG1606, COG1606, ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]
LEEKLERLKAILKELGSVLVAFSGGVDSTLLAKVAHDVLGDRVLAVTADSPSLPERELEEAKELAKEIGI
RHEVIETDELEDPEFVANPPDRCYHCKKELFSKLKELAKELGYAVVADGTNADDLGDYRPGLRAAKELGV
RSPLAEAGLTKAEIRELARELGLPTWDKPSSACLASRIPYGEEITPEKLRRVERAEAFLRSLGFRQVRVR
HHGDLARIEVPPEELERLLEEELREEIVEKLKELGFRYVTLDLEGYRSGSMNEVL
>gnl|CDD|441215 COG1607, YciA, Acyl-CoA hydrolase [Lipid transport and metabolism]
PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVE
LYARVVRVGRTSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALR
RRELRL
>gnl|CDD|441216 COG1608, COG1608, Isopentenyl phosphate kinase [Lipid transport and metabolism]
MIVLKLGGSVITDKDKPETVRRDALERIAREIAAALDLDLVIVHGGGSFGHPVAKKYGLHGTLGTEDAEG
VSETHRAMRELNRIVVDALLEAGVPAVSVPPSSFAVRDNGRILSFDTEPIKEMLEEGFVPVLHGDVVFDA
ERGFTILSGDEIVVYLAKELKPERVGLATDVDGVYDDDPKGKLIPEITRSNFDEVLDALGGSAGTDVTGG
MAGKVEELLELAKPGVEVYIFNGNKPGNLSAALRGEEVRGTRIR
>gnl|CDD|441217 COG1609, PurR, DNA-binding transcriptional regulator, LacI/PurR family [Transcription]
RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPD
LSNPFFAELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAG
IPVVLIDRPLPDPGVPSVGVDNRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLP
PDPELVVEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLA
RYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLLPPELVVRESTAPAP
>gnl|CDD|441218 COG1610, YqeY, Uncharacterized conserved protein YqeY, may have tRNA amino acid amidase activity [General function prediction only]
MSLKERLNEDLKAAMKAKDKVRLSTLRMILAAIKNREIDERRELDDEEVLAVLQKMVKQRRESIEQYEKA
GRPDLAEKEEAEIAILEEYLPKQLSEEELEAAVDEAIAETGASSMKDMGKVMGALKPKLAGRADGKAVSA
LVKALLS
>gnl|CDD|441219 COG1611, PpnN, Nucleotide monophosphate nucleosidase PpnN/YdgH, Lonely Guy (LOG) family [Nucleotide transport and metabolism]
SVCVFGGSRTGPDPPYYEAARELGRLLAERGFTLVTGGGPVGLMGAVADGALEAGGRSIGVIPHFLVERE
VANPYLTELIVVDYMHERKAMMLELADAFVALPGGFGTLDELFEVLTLAQLGKHPKPIVLLNGNGFWDPL
LDWLDHMLEEGFISPEDLDLLLVVDDPEEALDALEAYEPPYASK
>gnl|CDD|441220 COG1612, CtaA, Heme A synthase [Coenzyme transport and metabolism]
MTSSARSRRALRRLALLTLVLTFLLVVLGGAVRLTGSGLGCPDWPLCYGSLIPPTSEAGWQAAFKPEMPL
EEFKAWIEFGHRLLAGLLGLLILLLAVLAWRRRRRRRRLRWLALLLLLLVGLQGALGGWTVTSGLSPYVV
ALHLLLALLILALLLWLALRLRRPDGPLAAAVPRRLRRLALAALVLLLLQILLGALVAGNYAGLACPDFP
LCNGQWLPHDAEPFLNFENPVAVQFIHRLGAYLLLLLLLALALRLRRSRAPRALRRAALLLLALLLLQVL
LGIATVLLGLPLLLAVLHQAGAALLLGALVYLLLRLRR
>gnl|CDD|441221 COG1613, Sbp, ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and metabolism]
MKRSQSSLLLAALLALALAACAASSAAAAAADVTLLNVSYDPTRELYKEINPAFAKHWKAKTGQTVTIKQ
SHGGSGKQARAVIDGLEADVVTLALAYDIDAIAKAGLIPPDWQKRLPNNSSPYTSTIVFLVRKGNPKGIK
DWDDLVKPGVSVITPNPKTSGGARWNYLAAWGYALKKYGGDEAKAKEFVTKLYKNVPVLDSGARGATTTF
VQRGIGDVLLAWENEALLALKEFGKDKFEIVVPSVSILAEPPVAVVDKNVDKKGTREVAEAYLEYLYSPE
AQEIAAKHGYRPRDPEVAAKYAAQFPKLKLFTIDDVFGGWDKAQKTHFADGGIFDQIYAP
>gnl|CDD|441222 COG1614, CdhC, CO dehydrogenase/acetyl-CoA synthase beta subunit [Energy production and conversion]
GERIRKDDMYVELGGPKTPAFELVRMKEMDEVEDGKIEVIGPDIDDMEEGSRLPLGIVVEVAGRKMQEDF
EPVLERRIHEFLNYIQGLMHLGQRDIIWIRISKEAVEKGFRLKHIGKILHAKFKQEFGPIIDKVQVTIYT
DEEKVKELLEEAREIYEARDERLKGLTDEDVDTFYSCTLCQSFAPTHVCVVTPERPGLCGAINWLDGKAA
YEIDPEGPNQPIEKGEVIDEVLGEYSGVNEFVKKASQGEVERVNLYSIMEYPMTSCGCFECIAAYIPEVN
GIMIVNRDYKGMTPNGMPFSTLAGQTGGGKQTPGFMGISKNYIRSRKFLQADGGWARIVWMPKELKEELK
ERIPKRAEELGIEDFIDKIADETDATTIEELLEFLEEKGHPALGMKPIL
>gnl|CDD|441223 COG1615, COG1615, Uncharacterized membrane protein, UPF0182 family [Function unknown]
RRALLITLVVLVVLLVLFSRLAGFYTDWLWFDSLGYTSVFTTQLLTRIGLFVVGFLLMALFVFLNLWLAY
RLRPVYAPASPEQDPLDRYREVIEPRRRLVLIGVPVVLGLFAGLAASGQWQTVLLFLNSTPFGITDPIFG
LDIGFYVFTLPFYRFLLSFLFALVILALIAALVTYYLYGGIRLQGRGGRLSRAARVHLSVLLGLFLLLKA
VGYWLDRYELLYSDRGVVTGAGYTDVNAVLPAKTILAVIALICAVLFFANAFRRRWRLPAIGLALLVVSS
LLLGGIYPALVQQFQVKPNELEKEAPYIERNIDATRAAYGLDDVEEEDYPATTTLTAGDLREDAETIANI
RLLDPRPLSPTFTQLQQIRNYYQFPDTLDVDRYTIDGKYRDVVVAARELNLDGLPDNAQTWVNRHLVYTH
GYGVVAAPVNEVTADGQPEFLIKDIPPTGDLDLGVYEPRIYFGELTPDYVIVGTPKPREFDYPSGDGNVY
TTYEGKGGVPLGSFFNRLLFAIKFGDPNILLSDAITSDSKILYNRNPRERVEKVAPFLTLDSDPYPAVVD
GRLVWIVDAYTTSDNYPYSQPVSLSEATADSLTGQALPNGGVNYIRNSVKATVDAYDGTVTLYAWDEEDP
VLKTWSKIFPGLFKPLSEMPADLRSHLRYPEDLFKVQRELLARYHVTDPGVFYNGEDFWQVPNDPTEGEE
QLQPPYYLTMKLPGQDKPEFSLTSPFTPANRNNLIAWLAARSDGENYGKLRLLELPKDTLVYGPGQVENR
INQDPEISQQLTLWNQGGSRVIRGNLLTLPIGGGLLYVEPVYLQASGESSYPELKRVIVAYGDKVVMADT
LDEALDQLFGGDSGAPAGDPGTSTPETPTPPPGGGTASAALAEALQEAQDAYEDAQAALKSGDWAAYGEA
LKELQDALERLEAAQG
>gnl|CDD|441224 COG1617, Cgi121, tRNA threonylcarbamoyladenosine modification (KEOPS) complex, Cgi121 subunit [Translation, ribosomal structure and biogenesis]. tRNA threonylcarbamoyladenosine modification (KEOPS) complex, Cgi121 subunit is part of the Pathway/BioSystem: tRNA modification
MKIVGGRVTIDDLDAFLKKLRAIAEEHGVTVQAFDADYVAGRRHLERAVEHALRAFERGRNIARDLGVEI
LLYAAGRRQISRALEMGVKEGENRVVVVVLGDDDEAAAEELSELLEEDDLTLSEEKEERLREFFDITDAE
LEAVGEERLEDLVLERVALLDVEK
>gnl|CDD|441225 COG1618, THEP1, Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism]
MKIFITGRPGVGKTTLLLKVVEELRDEGLRVGGFITPEVREGGRRVGFKLVDLATGEEAILASVDIDSGP
RVGKYGVDPEALEAIAVEALERALEEADLIVIDEIGKMELKSKGFREAIEEALDSDKPVLATVHKRSHPF
LDEIRERGGVEVLEVTPENRDALPEEILELLREEL
>gnl|CDD|441226 COG1619, LdcA, Muramoyltetrapeptide carboxypeptidase LdcA (peptidoglycan recycling) [Cell wall/membrane/envelope biogenesis]
MIKPPPLKPGDTIAVVAPSSPVDPERLERAIERLESLGLKVVLGPHVLARHGYLAGTDEERAADLNAAFA
DPEVKAILCARGGYGAIRLLPYLDYDLIRANPKWFIGYSDITALHLALYAKTGLVTFHGPMLASDFGEEE
DEYTLESLRRALFGEEPEIQPPPNPGWKTLRPGKAEGRLIGGNLSVLASLLGTPYLPDLEGKILFLEDVG
EAPYRIDRMLTQLKLAGVLDRVAGIILGRFTDCDPDEDYGETLEEVLRDRLGDLGIPVVYGLPFGHTPPN
LTLPLGARAELDADAGTLTLLEPA
>gnl|CDD|441227 COG1620, LldP, L-lactate permease [Energy production and conversion]
MSLGLSALLALLPILVLFVLLVVLRWPAHKAMPIGLLVALLVALFVFGMPAGLALAATLQGALFGLPILW
IVFGAILLYNTTVESGAFDVIRRSFASISPDRRVQALLIAFLFGAFLEGAAGFGTPVAITAPLLVGLGFP
PLAAAGLALIANTAPVAFGAVGTPIIVGAQVTGLDALEIGAMVGRQLPILSLLIPFLLVWILDGWRGIKE
VWPAALVAGLSFAVPQFLTANFLGPELPDIIAGLVGLAALVLFLRFWKPKEIWDFAPEEEWPAEEEDAEK
LSAMSLLKAWSPYLLLIVLLVLTRLPPPVKALLNSTTLKIPWPGLLGAGTTGASYSFNPLYAPGTAILLA
ALITILLLRMSPGQAKRAFKETLKQLRGPILTLAFVLALAYVMNYSGMPATLGLALAAATGAAFPFFAPF
LGWLGVFITGSDTSSNALFGGLQFTTAEQLGLSPTLIVAAQSVGGVMGKMISPQNIVAAAAAVGLVGKEG
EIIRKTLIPSLILLLLVGLLVLLQAYVLIP
>gnl|CDD|441228 COG1621, SacC, Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]
ADDPYRPQYHFTPPAGWMNDPNGLVYFDGEYHLFYQYNPYGPVWGPMHWGHATSTDLVHWEHLPIALAPD
EEYDSGGCFSGSAVVDDGNLVLFYTGNVRDGDGGRRQYQCLAYSTDGRTFTKYEGNPVIPNPPGGYTKDF
RDPKVWWDDGKWYMVLGAQTGDGKGTVLLYTSPDLKNWTYLGEFGEGDGAFGYMWECPDLFPLDGKWVLI
FSPQGGGPEGGSQTGYFVGDFDGETFTPEEFQELDYGFDFYAPQTFSDPDGRRILIGWMGNWEYAYPTDE
DGWAGAMTLPRELTLRKDGRLYQRPVPELESLRGDEVTLENVTLDPGSNTLPGLDGDAYELELEIDPGSA
GEFGLRLRADGGEETVIGYDPENGRLTLDRSKSGLTDEGGGGIRSAPLPADGTLKLRIFVDRSSVEVFVN
DGEAVLTSRIFPTEGDTGISLFAEGGTATIKSLTVWELK
>gnl|CDD|441229 COG1622, CyoA, Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion]
MKRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADP
AQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIATVNELV
LPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVV
VSPEEFDAWLAEQKASAAT
>gnl|CDD|441230 COG1623, DisA, c-di-AMP synthetase DisA, contains DisA_N, linker and DNA-binding domains [Signal transduction mechanisms]
KEERLREILALVAPGTPLRDGLERILRARTGALIVLGDDEEVESIVDGGFELDVEFSPTRLYELAKMDGA
IVLSSDAKRILYANVQLVPDPSIPTSETGTRHRTAERVAKQTGFLVIAISQRRNIITLYKGGLRYVLEDI
GVILSRANQALQTLEKYKSRLDEVLTNLSALEFEDLVTLRDVAAVLQRLEMVRRISEEIERYILELGTEG
RLISLQLEELVAGVEEERELLIRDYLPELDERDPEEILEELASLSSEELLDLSLIARALGYGGGSDALDQ
PVSPRGYRLLSKIPRLPSAVIENLVEHFGSLQKLLAASIEELDDVEGIGEVRARAIREGLSRLAEQSILD
RYV
>gnl|CDD|441231 COG1624, DisA, c-di-AMP synthetase, contains DisA_N domain [Signal transduction mechanisms]
ILDILLVAFLLYKLYKLIRGTRAVQLLKGILVLLLLYLLAELLGLETLSWLLSNFITVGVIALIIIFQPE
IRRALEQLGRGRFFRRRSEEEEEKVIDEIVKAVKELSKRKIGALIVIERETGLDDYIETGIKLDAEVSSE
LLINIFIPNTPLHDGAVIIRGNRIVAAGCILPLSENPDISKELGTRHRAALGISEVTDALVIVVSEETGS
ISLAKNGKLTRNLDPEELRELLRELLSPKEEKKSK
>gnl|CDD|441232 COG1625, NifB, Fe-S oxidoreductase, related to NifB/MoaA family [Energy production and conversion]
MKIRGAKISKVEPGSIAEELGIEPGDRLLSINGQPIRDIIDYRFLTADEELELEVEKADGEIWELEIEKD
YDEDLGLEFETALFDGLRQCRNKCIFCFIDQLPPGMRESLYFKDDDYRLSFLYGNYITLTNLTEEDWDRI
IEQRLSPLYVSVHATNPELRKRMLGNPRAGDILEQLKRLAEAGIEMHAQIVLCPGINDGEELERTIRDLA
SLYPAVLSVAVVPVGLTKFREGLYPLRPFTPEEAREVIDQVEAWQKKFRKELGTRFVYLSDEFYLLAGRP
LPPAEHYEDFPQLENGVGMIRLFLDEFEEALEKLPRKLAKPRRVTIVTGVSAAPALQPLVERLNEIKGLE
VNVLPIKNDFFGETVTVTGLLTGQDIIAQLKGKDLGDLLLLPSVMLKAGEDVFLDDMTVEELEEALGVPV
IVVENDGEDLVDALLGLGRGE
>gnl|CDD|441233 COG1626, TreA, Neutral trehalase [Carbohydrate transport and metabolism]
MELPEPDESYVSDPGQTLREHIDALWPVLTRTPDEPNEGSSLLPLPHPYVVPGGRFREIYYWDSYFTMLG
LAESGRWDLARDMVDNFAYLIDRYGHIPNGNRTYYLSRSQPPFFALMVELLAEHTGDEWLRRYLPQLEKE
YAFWMDGADSLAPGQAYRRVVRLPDGTVLNRYWDDRDTPRPESYREDVETAKQSPERPAEEVYRDLRAGA
ESGWDFSSRWLADGKDLATIRTTDIVPVDLNALLYHLETTLAKAYALAGDPAKAAEYRARAERRKEAINR
YLWDEERGFYFDYDFVTGKQTAVLSAAAFYPLFAGIATPEQAARVAETLEPQLLKPGGLVTTLVNSGQQW
DAPNGWAPLQWMAVKGLRNYGYDDLAREIARRWLALVERVYERTGKLVEKYNVVDPSLEAGGGEYPLQDG
FGWTNGVYLALLALLGEP
>gnl|CDD|441234 COG1627, MJ0835, Uncharacterized conserved protein MJ0835, predicted component of type IV pili-like system, DUF1515 family [General function prediction only]
MAEDIEGKIKRLLGKISAESKPKMPKPKPTKPPSKKPSRIPERRKRTLIGALVFVIIIIFIAYAGYYYLQ
SKPYQELENAKAAKIAEVNAYFKGELPNDPQKQALIAKIQAAQTPEELLAIDVKAKAYKELKQYKNQQIN
QIKDMYGPYLSLSLTANSLVRKINSAKSKEEVDEIFPDSYLEELWKEYYLKQIDSTPTQYVIVKYSGESQ
IMSKDEAKEIVSKADLSELKNYKIEPVSLVKIAIVISRKQCAGGLIQPGDSVDVYLKNTSTIFYGIVDSS
YVILGDISYSESQSVSNSVSSTSSTSGATVLLTSYSPGISDSQLTSNQYGSSQSSSSSSSISYSLNVNLP
GILKATAAGKLDEPDIKEKLGNYGWKLNDIERNTNIFDENTNYLVIIEVPSEFVPDIIQNKNSIYIVKPT
Q
>gnl|CDD|441235 COG1628, COG1628, Endonuclease V homolog, UPF0215 family [General function prediction only]
RGIRVLGIDDSPFEGGDGRSTLAGVVMRGDRVIDGVAFGRITVDGLDATDAIIELVDSLKFRPDVRVVLL
DGITFAGFNVVDLERLHEETGLPVIAVTREEPDGDAIESALRKHFPDDEERLELYRRLGPREPVSVTGGT
LYVQAVGISPEEAAELVRAFTLEGRIPEPLRVAHLIARAVRRGESRGRA
>gnl|CDD|441236 COG1629, CirA, Outer membrane receptor protein, Fe transport [Inorganic ion transport and metabolism]
LEEVVVTATRTDESLQDVPGSVSVISREQLEDQPATDLGDLLRRVPGVSVTSAGGGAGQISIRGFGGGGN
RVLVLVDGVPLNDPSGGDGGLSYIDPEDIERVEVLRGPSSALYGSGALGGVINIVTKKPKDGKGGEVSAS
YGSYGTYRASLSLSGGNGKLAYRLSASYRDSDGYRDNSDSDRYNLRAKLGYQLGDDTRLTLSASYSDSDQ
DSPGYLTLAALRPRGAMDDGTNPYSNDTDDNTRDRYSLSLEYEHLGDGLKLSASAYYRYDDTDLDSDFTP
TPADGGTLEQTDFDNRTYGLELRLTYDLGFGGKHTLLVGLDYQRQDLDGSGYPLDLGSGSLPTLTSGADD
DGTTTSLALYAQDTYKLTDKLTLTAGLRYDYVSYDVDDTVTGTDSASGSRSYSAFSPSLGLTYQLSPNLS
LYASYSRGFRAPTFGELYANGTDPYSVGNPDLKPETSTNYELGLRYRLLDGRLSLSLALFYSDVDNEILS
VPLPNDSGFSTYYTNAGKARSYGVELELSYQLTPGLSLNASYSYTDAKFDDDTDGSADLDGNRLPGVPPL
TANLGLTYEFPGGWSLGLGVRYVGDRYLDDANTQGAPGGYTLVDLGAGYRFGDNLTLSLGVDNLFDKKYA
TSLSVRASNVRGFL
>gnl|CDD|441237 COG1630, NurA, ssDNA and dsDNA 5'-3' nuclease NurA, repair of double-stranded DNA breaks [Replication, recombination and repair]
MLRLLLESLLRKKDIILSKLKNINENIEKKDVEEKWNELPEENPSDCNVAAVDGSRNKRRLSGFILYAVS
AYAVGFGDGVEKSKLSYELGVLSPYKHVEDRLRLYMETLELKLALLALENGEIDLILMDGSLSGLLIRPP
PYTEDLVEKFEEKLDEIYKEIEKKLKEGGKSNEIIIYSNEVEELLEEALRRPGGKDEELDAAKIYLEYLE
YLYSLKKLLEKFKKNLVYVAKTSYSNELFKSNIPDIAILDAYTREPGYSEPLDSNLGKKVKEKKSFPDVG
KRLREFYKNLGIYLFYVRLERGGNILKIESPKDRKEKIEEILSLLKEISANGYPYPLKKAHETVKITRKE
MEAIIKALGIFLKSGREVLG
>gnl|CDD|441238 COG1631, RPL42A, Ribosomal protein L44E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L44E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MKMPKKIRTYCPYCKKHTEHEVERVKKGKRSGLAWGQRRYRRKTKGYGGKPSPVPKGGAKPTKKVDLRYR
CSECGKAHLREGFRAKKFELV
>gnl|CDD|441239 COG1632, RPL15A, Ribosomal protein L15E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L15E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MAKSMYSYIREAWKRPKEGYVGELQWERLQEWRREPSVVRIERPTRLDRARALGYKAKQGIVVVRVRVRK
GGRRKPRPNAGRRPKRMGVNKITPAKSLQRIAEERAARKYPNLEVLNSYWVGEDGKYKWYEVILVDPHHP
AIKNDPDLNWICDPSHRGRAFRGLTSAGKKGRGLRNRGKGTEKTRPSIRANERRGK
>gnl|CDD|441240 COG1633, YhjR, Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism]
SLLEILKEAIAMEEEAIEFYLELAEKAKDPELKKLFEELAEEEKKHAELLEKLYEKLGGKPVAPPEEESQ
PGLAELMDKLDGSVSDAEALELAIATEKDAIEFYRELAAKVGDPEIKKLFEELAADEKEHAALLEGLYDR
L
>gnl|CDD|441241 COG1634, FolK, 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase MptE (tetrahydrofolate and tetrahydromethanopterin biosynthesis) [Coenzyme transport and metabolism]
MDFEEWEPVYEAILDDFGYDREEDERAADILSSLLKEARPFDLDELKDLIRGKTVAVVGAGPSLEEELKR
AREAGVVIAADGATSALLEAGIRPDIVVTDLDGDPETLLEANRKGSIVVVHAHGDNIERLRRYVPRFKNV
IGTTQAEPLGNVYNFGGFTDGDRAVFLADEFGAKKIVLVGFDFDDPVGKYSPSVDEIKRKKLEWAKRLLE
WLERRRGERFEVLDGRR
>gnl|CDD|441242 COG1635, THI4, Thiazole synthase/Archaeal ribulose 1,5-bisphosphate synthetase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism]
LDEVKITRAIVEEYFEKLLDYLEVDVAIVGAGPSGLTAAYYLAKAGLKVAVFERKLSLGGGMWGGGMMFN
KIVVQEEAKEILDEFGVRYKEYEEGLYVADSVEAVSKLAAAACDAGAKIFNLVSVEDVVVRDNRVAGVVI
NWTPVEMAGLHVDPLTIEAKAVVDATGHDAEVVRVLARKGPLLLGEVPGEKSMWAEEGEKLVVENTGEVY
PGLYVAGMAANAVFGLPRMGPIFGGMLLSGKKAAELILEKLKKD
>gnl|CDD|441243 COG1636, QueH, Epoxyqueuosine reductase QueH (tRNA modification) [Translation, ribosomal structure and biogenesis]
NGMMKLLLHSCCAPCSTYPLEYLREEGFDVTGFFYNPNIHPYEEYEKRLEELKRFAEKLGIPFIEGDYDP
EEWLRRVKGLEDEPERGERCRLCYDMRLERTAKYAKELGFDAFTTTLLISPYKNHELINEIGERAAKEYG
VPFLYSDFRKKGGYKRSIELSKELGLYRQQYCGCIYSERERYKKRKKKGRER
>gnl|CDD|441244 COG1637, NucS, Endonuclease NucS, RecB family [Replication, recombination and repair]
MRLVIARCSVDYEGRASSHLPLGDRLIIIKPDGSVLVHSDGGYKPVNWQPPPCTLEVEEEDGVLVVRSVR
RKPDERLEIRIDEVYHLSAHDLGDDPGLVKDGVEADLQELLAENPELIEEGFRLIRREYPTAIGPVDLLA
RDADGNLVVIELKRRRAGIDAVEQLTRYVELLNRDPLLAPVRGILVAPSITPQARTLLEDRGLEFVELD
>gnl|CDD|441245 COG1638, DctP, TRAP-type C4-dicarboxylate transport system, periplasmic component [Carbohydrate transport and metabolism]
MKRKLLAAALAAALALAAAAAAAAAVTLKLAHVLPPGHPWGKAAEKFAEEVEERTGGRIKVEVFPGGQLG
KEPEVLEAVRDGAVDMAAVSPGYLSGFVPEFGVFDLPFLFRDYEHADKVLDGELGPELLEELEKKGLKVL
GWWDNGFRQLTTSKKPIRSPEDLKGLKIRVPGSPVLAAMFEALGANPVPMPFGEVYTALQTGVVDGQENP
LSSIYSAKLYEVQKYLTLTNHAYSPFVLVMNKDFWDSLPPEQQAALLEAAAEAAAYQRELARELEAEALA
ELKAAGVTVVELSPEDRAAFREAAKPVYDEWAEEVGAELLDAIRAALAK
>gnl|CDD|441246 COG1639, HDOD, HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms]
EELLKGILELPPLPEVALRLLELLADPDASLAELARLISQDPALTARLLRLANSAYYGLGRKITSVEQAV
VLLGLDTVRNLALALALRQLFSAKLPAYGLDLRRFWRHSLAVAAAARALARRLGLLDPEEAFLAGLLHDI
GKLVLLSLFPEEYAELLALAEADGLSLAEAEREVLGTDHAELGAALARKWGLPEELVEAIRYHHDPEAAG
EHRRLAALVHLANRLARALGEEDPALPEAALALL
>gnl|CDD|441247 COG1640, MalQ, 4-alpha-glucanotransferase [Carbohydrate transport and metabolism]
RAWGILLHLYSLPSARNWGIGDFGDLYRFVDFLAEAGQDFWQILPLHATFPPYGDSPYSPSSRFAGNPLY
IDLEALPEFGLLSAADLAALAPLRDADRVDYDAVAALKLAALRLAFERFRARADAERRAAFEAFCAEEGE
WLEDYALFMALKEHFGGRGWREWPEELRDRDPPAVAAFRAELADEIEFHKFLQWLFFRQWAALKAYANAA
GIGLIGDLPIGVAPDSADVWANPELFALDAVAGAPPDYFSPTGQLWGNPPYDWDALAETGYAWWIDRLRA
NLRLADALRIDHFRGLERLWWIPAGEETAANGAWVKYPGEDLFGILALERGRLPVIAEDLGTVPPEVREL
LDRFGLPGMKVLQFEFDDPDGPFLPHNYPRNAVAYTGTHDNPTLAGWWEGLDLDLREERAEREEERAALL
RYLGRDPEDMEEELVWALIRLLAASVAALAIVPLQDLLGLEARMNLPGTVDGYNWRWRLPVDLEDLFADP
EARRLLAALTELYGR
>gnl|CDD|441248 COG1641, LarC, CTP-dependent cyclometallase, nickel-pincer nucleotide (NPN) cofactor biosynthesis [Coenzyme transport and metabolism]
MKILYLDCFSGISGDMLLGALLDLGVDLEALQEALASLGLDGYELEVEKVKRNGIRATKVDVDLDEHHHH
RHLAEIRAIIEASDLPERVKELALAIFRRLAEAEAKVHGVPVEEVHFHEVGAVDAIVDIVGAAIALDLLG
IDRVYCSPLPVGSGTVKCAHGILPVPAPATLELLKGVPVYGGGIEGELVTPTGAAILAALADEFGPPPAM
TIEKIGYGAGTRDLPDRPNVLRLVLGETAEEGLERDTVVVLETNIDDMTPEVLGYLMERLLEAGALDVFL
TPITMKKGRPGVLLTVLCRPEDAERLAEILFRETTTLGVRRRPVERYILPREIETVETPYGEVRVKVADL
GGGIVNVKPEYEDCRRIARETGLPLREVYRAALAAAEELLSD
>gnl|CDD|441249 COG1643, HrpA, HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]
MSLITYPPDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARA
AAERMAEELGEPVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNAD
LLLALLLDLQPALRPDLKLLVMSATLDAERFARLLGDAPVIESSGRTYPVEVRYRPLPADERDLEDAVAD
AVREALAEEPGDILVFLPGEREIRRTAEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLAT
NIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA
RRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARALLQELGALDADGRLTPLGRAL
ARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGSDLLARLNLWRRLREQQREFLSYLRLR
EWRDLARQLRRLLGEGANEEPADYEAIGLLLALAYPDRIARRRGEGGRYLLARGRGAALFPGSPLAKKEW
LVAAELVGGAAEARIRLAAPIDPEWLEELAAHLIKRYSEPHWDKKRGRVVARERVRLGALVLVSRPLPGP
DPEAAREALLRALRREGLDLLPWSKAARQLRARVEFLERKLGERWPDVSDEALLATLEDWLAPYLTGVRS
LKDLKRLDLLAALRALLPWEQQQRLDELAPTHLTVPSGSRLPLDYSADGPPVAVRLQELFGLAETPGVAD
GRVPVPLHLLSPAGRPLQVTWDLPGFWRGSYAEVRKELRGRYPKHPWPDDPAAAAPTRRTKRRMPR
>gnl|CDD|441250 COG1644, RPB10, DNA-directed RNA polymerase, subunit N (RpoN/RPB10) [Transcription]
MIIPVRCFTCGKVIGHKWEEFKRRVEAGEDPGKVLDDLGVKRYCCRRMLLSHVELIDEVIPY
>gnl|CDD|441251 COG1645, COG1645, Uncharacterized Zn-finger containing protein, UPF0148 family [General function prediction only]
MSERSSDDAIKKMAELLLKGATMLSEHCPVCGSPLFRKDGEVFCPVCGKEVVVKEEEEEKPEVKTREVLD
ELEEILEEKLNSLAKELKEESDPERQKEILEALEKLLEILEKLKRL
>gnl|CDD|441252 COG1646, PcrB, Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism]
GKVEKYLLEKLDWKGWLHVTLIDPDKELSDEEAELAEAACESGTDAILVGGSLGVTEENLDELVSAIKEA
YDVPVILFPGNPEQVSPGADAILFPSVLNSRNPYWIIGAHVEAAPLVKKLGLEVIPEGYIVLNPGTTVAY
VTNARPIPLDKPDVAAAAALAEEYLGMPIVYLEYGSGAGEPVDPEMVKAVKKALEDTPLIYGGGIRSPEK
AREMAEAGADTIVVGNAIEEDPDLALETVEA
>gnl|CDD|441253 COG1647, YvaK, Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]
MKILGAEPFFLEGGRKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLE
DVEEAYEILKAGYDKVIVIGLSMGGLLALLLAARYPDVAGLVLLSPALKIDDPSAPLLPLLKYLARSLRG
IGSDIEDPEVAEYAYDRTPLRALAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSP
DKELVWLEDSGHVITLDKDREEVAEEILDFLERLAA
>gnl|CDD|441254 COG1648, CysG2, Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and metabolism]. Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) is part of the Pathway/BioSystem: Heme biosynthesis
MDYFPIFLDLEGRRVLVVGGGEVAARKARLLLKAGARVTVVAPEFSPELAALAEEGRIELIKRAFEPEDL
DGAFLVIAATDDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLR
ERLEALLPPEYGDLAELLGRLRERVKARLPDGAERRRFWERLLDGPLAELLRAGDEEEAEALLEELLAEA
A
>gnl|CDD|441255 COG1649, YddW, Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown]
MKKLLLLLLLLALSLLGCSAPAPAAAPSPKREIRGVWLTTVDLSVLKQKAELIEILDRLKELGFNAVFFQ
VRPAGDALYPSAIEPWSEYLTGTQGKDPGYDPLAFAIEEAHKRGLEVHAWFNPYRAAPNTDVSPLAPSHI
AKKHPEWLTKYRDGGKLWLNPGHPEVRDFILDLVLEVVTRYDVDGIHFDDYFYPSEFGYDDATYALYGQE
TGFDNPKDLSWADWRRDNVNRFVRRLYQAIKAVKPDVKFSISPFGIWRNSPTGLFAYDDLYQDWRTWVKE
GWVDYIVPQLYWPDGNSAADFEKLLDWWAQQAKGRKVPLYIGIGLYKVPPEEILRQIQLNRDLPGVAGVV
FFSYESLWNNPGLADALRQGLYRTPALVPAMPWLDGTGVLLSWQAPAEELAEALARLAVVPSSASLDLAA
ASLASFILAFAILTVAGAINAAYQVAVTYNR
>gnl|CDD|441256 COG1650, COG1650, D-tyrosyl-tRNA(Tyr) deacylase [Translation, ribosomal structure and biogenesis]
MIAIVVSRADPASVNIAEHLLELLDWEEREDDDGGGTYYRSDGFELREFDELHIYLDGLDEAFGIDPDLI
IFASRHSSETGRPLLTVHFTGNFGEAEYGGKPGELAIAAPAAMKALLRALKEHAEPEGYDVSMEATHHGP
TDLGKPSLFVEIGSTEEEWRDPDAAEAVARAILDLLEVGPKRCRVAVGFGGGHYAPRFTRLALETDVAFG
HIAPKYALEALDEEVLRQAIEKSGADLALIDRKGLKSGERPRLEELLESLGLEVVKE
>gnl|CDD|441257 COG1651, DsbG, Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones]
KVTVVEFFDYQCPYCARFHPELPELLKKYVDGKVRVVYRPFPLLHPDSLRAARAALCAADQGKFWAFHDA
LFANQPALTDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSGAVP
YEELEAALDAAL
>gnl|CDD|441258 COG1652, XkdP, Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism]
VAAAAAAAALAALLPAVSAAAATVLALAAAAALAVVAGLGAAVGAGGALAAALPLAAGLAAAVAAAAAAA
VLIAPVAVMRAGAAAKLSPAVTVAEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRFYGDPARWPEIAEA
NRDQIKNPDLIYPGQVLRIPALE
>gnl|CDD|441259 COG1653, UgpB, ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism]
MRRLALALAAALALALAACGGGGSGAAAAAGKVTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESVP
YDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTYDGKLYG
VPFNTDTLGLYYNKDLFEKAGLDPPKTWDELLAAAKKLKAKDGVYGFALGGKDGAAWLDLLLSAGGDLYD
EDGKPAFDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDFD
VGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAKWDALQAVLLGQKTPEEALD
AAQAAANAALARA
>gnl|CDD|441260 COG1654, BirA, Biotin operon repressor [Transcription]
MMSSTRLKLLRLLADGEFHSGEELAEELGVSRAAVWKHIKALRELGYEIESVPGKGYRLAEPPDLLDPEE
IRAGLSTKRLGREILYVISSTSTNLLALELAAQGGDAGTVVAAEQQRGGRGRRRRSWSSPGGGGLLYSLL
LRPPIAPALLSLLLLAAAVAVAAALAEGGGLVKWKKWPNDLLKKGKKILGILEEEGGDADGVVIVVGGGG
NNNNSNPEEEPQELAELATSLLLILRLRLLRLLLLLLLLLLELLELLGFLEFFFLWERLDWELLRVLKLV
VVVVEIGGGGGGGGALGGGLLGLLLLGGGGGGGEGSLSAVVVLL
>gnl|CDD|441261 COG1655, COG1655, Uncharacterized conserved protein, DUF2225 family [Function unknown]
MVKEISPLYDKKVTCPVCKKEFKTKKVRSSKIRVGKRDSDFCPHYEGVNPLLYEVWVCPHCGYAAFEKDF
EKLSPAQKEKIKEKISSKWKPRDFSGERTLEEAIEAYKLALLCAQLKKAKTSKLAGLCLRLAWLYRDLGD
EEQEKRFLKKALELYEKAYENEDFPDKGMDEDTLLYLIGELSRRLGNYEEAKRWFSRVIGDKGAKNKPKI
IDMAREQWQLIREEKKEK
>gnl|CDD|441262 COG1656, Mut7-C, Uncharacterized conserved protein, contains PIN-related Mut7-C RNAse domain [General function prediction only]
PRFLLDVMLGKLARWLRMLGFDTLYANDIDDDELLAIAREEGRILLTRDRGLLKRAEVTRGVLLRSTDPE
EQLAEVLRRFGLDLELDRPFTRCLRCNGPLEPVDKEEVADRVPPYVRERYDEFWRCPKCGKVYWRGSHWR
RMRERLERLLKRSAA
>gnl|CDD|441263 COG1657, SqhC, Terpene cyclase SqhC [Lipid transport and metabolism]
SIAPASASASSASNAEDRSLLDAAIAAAQALLLQQQDDGGWWGGELEADVTIAAEYILLHHFLGPDDEEL
EAKIARYLRRQQNDDGGWPLYHGGPGDLSTTVKAYFALKLLGDDPDAPHMVRAREFILARGGAARANVFT
KIWLALFGQYPWRGVPALPPEIMLLPRWFPFHIYKFSYWARTVIVPLLILYARKPVAPLPPGVGIDELFV
EPPEQVDYYFPAPRDRSPWSRFFLALDRLLRAYERLPPKPLRRRALRKAEDWILERLEGDGGLGGIFPAM
VNSLMALLALGYPPDHPVVRRALEALEKLLVETEDGARCQPCVSPVWDTALAVQALQEAGLPEDHPALER
AADWLLSKQILVKGDWAVKRPDVEPGGWAFQFANDHYPDVDDTAVVLMALLRLRLPDEPRYREAIERAVE
WILGMQSRDGGWGAFDKDNTKEWLNKIPFADHGALLDPPTADVTARCLEMLGQLGLTEDHPAIRRAVAYL
RREQEPDGSWFGRWGVNYIYGTWSVLTGLNAAGVDPDDPAIRRAVAWLLSIQNADGGWGEDCRSYEDPRY
VGLGPSTASQTAWALLALLAAGEADSPAVARGIAYLLSTQREDGSWDEEYFTGTGFPRVFYLRYHLYRQY
FPLWALARYRNLRG
>gnl|CDD|441264 COG1658, RnmV, 5S rRNA maturation ribonuclease M5, contains TOPRIM domain [Translation, ribosomal structure and biogenesis]
MTDRSKIKEVIVVEGKDDTAALKRAVDADIIETNGSAISEETLELIKVAAEKRGVIILTDPDRAGERIRK
RISEHLPGAKHAFIDREKARKKKGIIGVEHASPEAIRRALSKVRTEKEEEEEEFSLEDLLDAGLLGGGGA
KKRRERLGEELGIGYGNGKQLLKRLNMFGITREEFEEALEEIEE
>gnl|CDD|441265 COG1659, CFP29, Bacteriocin, linocin/CFP29 family [Defense mechanisms]
DYLKRELAPISDEAWEEIDEEAVETLKRHLAGRRFVDVYGPLGWGLSAVGTGRLTPIEEAPVDGVRAGVR
KVLPLPELRVPFTLSRRDLDNVERGAKDLDLSPLADAARKIALAEDRAIFNGYAAAGIEGLLTASGNPTV
KLWADPGNAPDAVAEALSKLREAGVEGPYALVLSPDLYTALSRTYDGGYPEIEHIKRLVDGKIVWAPALE
GAVLVSTRGGDFELTIGQDLSIGYLSHDAENVELYLTESFTFRVKTPEAIVVLEL
>gnl|CDD|441266 COG1660, RapZ, RNase adaptor protein RapZ for GlmZ sRNA degradation, contains a P-loop ATPase domain [Signal transduction mechanisms]
KPMRLVIVTGLSGAGKSTALRALEDLGYYCVDNLPPALLPKLVELLAQSGGGIRKVAVVIDVRSRDFFAD
LPEALDELRARGIDVRILFLDASDEVLVRRYSETRRRHPLAGDGSLLEGIERERELLAPLRERADLVIDT
SDLSVHQLRERIRELFGGEEESGLTVTVESFGFKYGIPLDADLVFDVRFLPNPHYVPELRPLTGLDAPVA
DYVLSQPEVQEFLDKLLDLLEFLLPGYEREGKSYLTIAIGCTGGQHRSVAIAERLAERLREKGYRVSVRH
RDLGRE
>gnl|CDD|441267 COG1661, AF0104, Predicted DNA-binding protein with PD1-like DNA-binding motif, PPC/DUF296 domain [General function prediction only]
KYREGSIGRVFVLRLDPGEDLLESLEAFAEEEGIKAAIVSGIGALRDATLGFYDQEEKEYEEIEFDGPLE
VVSLSGNISLDDGKPFVHLHAVLGREDGQTLGGHLLEGTVGFTLEVVITELDGIELERKFDPETGLNLL
>gnl|CDD|441268 COG1662, InsB, Transposase and inactivated derivatives, IS1 family [Mobilome: prophages, transposons]
KLQRAISEELKILIDRVEIELIGLALLARGVGLSISALIITVNTKLVAVYVQLKVPNLSDKRLVEVDELW
TFVGSKKNKVWIWYAVDRDTGRIVAFVVGDRDKKTARKLWEKLKPFEIAVIYTDGWKAYASLIPEKRHVV
SKGYTNHIERNNLTLRHRLKRLVRKTICFSKSLEMHDKAIKLFFHYYNFGLVP
>gnl|CDD|441269 COG1663, LpxK, Tetraacyldisaccharide-1-P 4'-kinase (Lipid A 4'-kinase) [Cell wall/membrane/envelope biogenesis]. Tetraacyldisaccharide-1-P 4'-kinase (Lipid A 4'-kinase) is part of the Pathway/BioSystem: Lipid A biosynthesis
MMRLPRFWYKRGLLAWLLLPLSLLYGLVVALRRALYDRGILKSYRLPVPVIVVGNLTVGGTGKTPLVIAL
ARLLQARGYRPGVLSRGYGGKSKGPLLVDPGSTAAEVGDEPLLLARRTGVPVAVGPDRVAAARALLAHPG
VDVIILDDGFQHYALARDLEIVVVDGARGFGNGRLLPAGPLREPLSRLKRADAVVVTGCPAASKEAIKKR
LRPGQPVFFMRLVPGALVNLSTGERLPLEDLKGKRVLAVAGIGNPERFFATLRALGLEVVETLAFPDHHA
FTAADLEALAAEAKALGAAPLLTTEKDAVKLPAFALREPLWYLPVEAEFDDDEAFEELLLAKLKKLRRR
>gnl|CDD|441270 COG1664, CcmA, Cytoskeletal protein CcmA, bactofilin family [Cytoskeleton]
MFKKKSAAESEGITTVIGEGTTIKGDITSEGDLRIDGTVEGDITAEGTLVIGEGGVVEGDIEADNVVING
TVEGNITASEKLELLSTARVEGDITAGSLEIEEGAVFEGKCEMGEDEAAPAASPAPAAS
>gnl|CDD|441271 COG1665, AF1967, Predicted nucleotidyltransferase AF1967 [General function prediction only]
MKVRLRDFIETKDGWIFAVVTYDHPEDRILSFLRYVPDENGDRELNGKRYRKVDFEEAYEFLRENRPEYL
YYDPVDVDVHVVPVEDVKRILRPEERLKEILEEPSNELEEKVRKLVDILHDAGVPYGKMGVTGSLLPGLQ
NEASDIDFVVYGLDWFKKAREALKRAKEDGKLEALDEDMWKKVYNKRIPELSFEEFVWHEKRKGNRGMID
GTYFDLLATRDWDEIKGYPEVRGKDLGKIKIEATVTDDSFAFDNPAVYKVDHAEIDEVLSFTHTYAGQAL
EGEVIEARGKLEEVGGEKRLVVGTTREAKGEYIKSL
>gnl|CDD|441272 COG1666, YajQ, Cyclic di-GMP-binding protein YajQ, UPF0234 family [Signal transduction mechanisms]
MPSFDIVSEVDMQEVDNAVDQANKEIATRFDFKGSKASIELKDKTITLTADSEFQLKQVLDILRSKLVKR
GIDLKALDYGKVEKASGKTVRQEVKLKQGIDQELAKKIVKLIKDSKLKVQAQIQGDQVRVTGKKRDDLQA
VIALLKGADLDLPLQFTNFR
>gnl|CDD|441273 COG1667, AF1501, Uncharacterized conserved protein AF1501, DUF2226 family [Function unknown]
MWFPVDEDKEVGSLGNLEEIISSSTPSTGYVRILTREGEAIYDAFIFVEGGKIVGAYLGDIRSLEELSAE
EALEELRILEDSVVDVYELDEDLFETILELNDECKLKEPSLPIEVEIATEEIFTEEVSREELLKKYGIKE
PSEESIENILEDYFKSSDDFEELKRMLRMEGVVDVLVYLKVKEEEGVDERILEFIRKDIDEALSETIRDI
GKRI
>gnl|CDD|441274 COG1668, NatB, ABC-type Na+ efflux pump, permease component NatB [Energy production and conversion, Inorganic ion transport and metabolism]
MNKLWLVAKKELKERLRDKSFLISTLLLPLLLVPLLGLGMLFMSGNDDEPLKVAVVDESGAPALAEALKE
AAVNFEVVPEVADEEEAEAAVEDGEIDAVLVIPEDFSLENPATVELYSDSSPDSSAVSRLESALSQALLA
LRLAALGLDPEQLQALLAPVSVETVDLSKASPEEGAGYILGYLLPFLLYMFIFTYGSMIADSVAEEKESR
TLEILLSSVSPRQLLLGKILGIGLVGLTQALLWLVGGLIGLLLASGLGLSALSGLNLSPGLLLLFLLFFL
LGYLLYAALFAALGALASSFKEAQQYLSPLTLLLMIPFFVAMFVLSNPDGPLATVLSLIPFTSPILMPLR
LALGEVPWWEILLSLALLLATAVLLLWLAARIYRREILMYGKKPSLKELLKW
>gnl|CDD|441275 COG1669, MJ0435, Predicted nucleotidyltransferase MJ0435 [General function prediction only]
MNREEILEILREVIEELAERYGVSRLGLFGSVARGEAREDSDIDLLVEFDEPTSLFDLFELEEELEELLG
RKVDLVTLDGLSPRLRERILKEGVLL
>gnl|CDD|441276 COG1670, RimL, Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones]
PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDKED
GELIGVVGLYDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVL
EKLGFRLEGTLRDALVIDGRYRDHVLYSLLREE
>gnl|CDD|441277 COG1671, YaiI, Uncharacterized conserved protein YaiI, UPF0178 family [Function unknown]
MKIWVDADACPVVKEIIFRVAERYGIPVTLVANQSHRIPPSPYIETVVVDAGFDAADDYIVNRAEPGDLV
ITQDIPLAARVLEKGALVLNPRGELYTEENIGELLAMRDLMAKLRRSGGRTGGPKPFSKEDRQRFANALD
RLLARAKRR
>gnl|CDD|441278 COG1672, COG1672, Predicted ATPase, archaeal AAA+ ATPase superfamily [General function prediction only]
DFFDREEELEELEKLYESDGGELVVVYGRRRVGKTSLIKEFLKEKPAIYFDAREESERESLRDFSEALAE
ALGDPLSKKEFESWEEAFEYLAELAEGKRLVIVIDEFQYLVKLDPSLLSILQYLWDELLSDSNVSLILCG
SSIGMMEELLLDYKSPLYGRRTGEIKLKPFSFEESKEFLPEGFEYSEEELEEAYSVLGGIPGYLTLFGNE
GKSLEENIEELLLSPTSLLYEEPENLLREELREPARYFSILKAIASGATRLSEIASALGISSSSLSRYLK
NLIDLGIIEKEVPVEKSKKGRYRIADPFLRFWFRFVYPNRSLIE
>gnl|CDD|441279 COG1673, COG1673, Predicted RNA-binding protein, contains PUA-like EVE domain [General function prediction only]
EMRYWIAVASRENWKVGKEKGFWGVPHRKKALLKRVKPGDKLIYYVPGESFGGKTLCQAFVAIFEVVSEP
FEDEMPIFKSGDEFFPYRVKVKPVKILEEPVPIKPLIDKLSFIKNKRKWGGYLRQGLREIPEEDFKLIVS
ALK
>gnl|CDD|441280 COG1674, FtsK, DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning]
LLLLLLLLALLAGLLLLLLLLLLLLLLLLLLLLLLALLLGLLLLLLGLLLLLLALLLLLLAGLLLLGLLL
GLLLLLGLLLLLLLLLGLLGAALLALLALALALLLGALGLLALAAAALGALALLLLAAAEALALAVLPPL
DLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDI
ALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAK
MPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANAL
KWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKGEEEEGLEPLPYIVVIIDELADLMMVAGKEVEEAI
ARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLP
PGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDEGGDDDEDDELFDEAVELVVETQK
ASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL
>gnl|CDD|441281 COG1675, TFA1, Transcription initiation factor IIE, alpha subunit [Transcription]
MVEEDLNDEVLREYLEELVGEEGLKILEALLEEGEVTDEELAEETGIKLNDVRRILYKLYEKGLAVYRRE
KDEETGWLTYYWRLNLDNIPEFLEKRKKKVLEKLKERLEYEESNEFYICPNCCTRYTFDEAMEYNFKCPE
CGEMLEYVDNSELIEALKERIKELEEELGRAS
>gnl|CDD|441282 COG1676, SEN2, tRNA splicing endonuclease subunit SEN34 [Translation, ribosomal structure and biogenesis]. tRNA splicing endonuclease subunit SEN34 is part of the Pathway/BioSystem: tRNA modification
PTPIRGTLLGDRVVVWDIDAARELYEEGFYGKPLDKSPLQLSLIEALYLLEKGKLEVYDDGKELSFEELL
EIARKVDPEFDRKYLVYRDLRDRGYVVKTGFKFGSDFRVYERGPGIEDHSPYLVHVVPEGTEFSPRELSR
AVRLAHSVRKRMVFAVVDDEGEIEYYKFEWLKP
>gnl|CDD|441283 COG1677, FliE, Flagellar hook-basal body complex protein FliE [Cell motility]
MSPISAINAYAQLQALAAQAAPSAAAAAPAAGGASFGDVLKDALDDVNQTQQEAEALAQAFATGKSVDLH
DVMIAMQKASLSLQLTVQVRNKLVEAYQEIMRMQV
>gnl|CDD|441284 COG1678, AlgH, Putative transcriptional regulator, AlgH/UPF0301 family [Transcription]
SMESLKGHLLIAMPSLGDPNFARSVVYLCEHNEEGAMGLVLNRPLDLTLGDLLEQLDIEPLAAADQPVFF
GGPVEPDRGFVLHSPDGLWESSLEISDGLYLTTSLDILEALAAGEGPEKILVFLGYAGWGPGQLEQELAE
NSWLVVPADPDILFDTPPEDRWRAALRRLGIDPALLSNEP
>gnl|CDD|441285 COG1679, AcnX1, Mevalonate 5-phosphate dehydratase subunit 1, aconitase superfamily (modified mevalonate pathway) [Lipid transport and metabolism]
MKLTDEEEAMLDGEHGEAKQKAMEILVALGEALGAERLVPITSAHISGVSYKTIGDAGLEFLEELADMGA
KVRVPTTLNPIGMDLENWEEMGVPEEFAEKQRRIIDAYERMGVRPTFTCTPYLLGNIPRFGEHVAWAESS
AVIYANSVLGARTNREGGPSALAAAITGRTPLYGLHLDENRRPTVLIDVDAPLEGVSDWGALGYLVGRLA
GDRVPVITGLPRRPTEDQLKALGAAMAASGAVALFHVVGVTPEAPTLEAAFGGRAPVETITITKADLREV
YEELNTGEDDVDLVALGCPHLSLEELRELARLLEGRKVKKGVPLWVCTSRAVKAAADRMGYTAIIEAAGG
KVLTDTCMVVSPAEPMGYKVLATNSGKAAHYLPGLCGVKVRFGSLAECVEAAVTGRWEGEL
>gnl|CDD|441286 COG1680, AmpC, CubicO group peptidase, beta-lactamase class C family [Defense mechanisms]
MKFAAAAPAAGLSADLAALDAALDAALAEGGIPGAAVAVVRDGKVVYEKAYGVADLETGRPVTPDTLFRI
ASVTKSFTATAVLQLVEEGKLDLDDPVSKYLPEFKLPDDAKRDITVRHLLTHTSGLPDYEPDPYDAADVA
RPYTPDDLLARLAALPLLFEPGTRFSYSNLGYDLLGEIIERVTGQPLEDYLRERIFEPLGMTDTGFGLPD
AEAARLAPGYEADGEVHDAPAWLGAVAGAGGLFSTARDLARFGQALLNGGEWDGKRLLSPETLAEMTTPQ
VPSGDAGGGYGLGWWLNDDGGSGSFGHGGATPGFSTFLWVDPERGLGVVVLTNRDDPGAGDRAALLEALL
AALLG
>gnl|CDD|441287 COG1681, FlaB, Archaellin (archaeal flagellin) [Cell motility]
MFESKFRKDERGQVGIGTLIVFIAMVLVAAVAAGVLINTGGFLQQKAQETGEESTQQVSSGLEVVGAVGG
VGDTTSGTIDYINITVKLAAGSSPVDLSQTTITYSDGSGTVTLVYGGSTSDSSTDSSNNADGTFTIIVIQ
DEDGSDNNVLLEPGDRATLTINTTSGEGLGLSPGDTVTIEITPESGATTTIERTVPSSLTDSVVELY
>gnl|CDD|441288 COG1682, TagG, ABC-type polysaccharide/teichoic acid/polyol phosphate export permease [Carbohydrate transport and metabolism]
RALRDLWRYRELILALVRRDLKARYRRSVLGLLWALLNPLLMLLVYTFVFGVLLRAPSGGVPYALFLLAG
LLPWNFFSEALNRGSGSIVANAGLIKKVYFPREILPLARVLSALVNFLISLVVLLVVLLLFGVPPSWTLL
LLPLALLLLLLFGLGLGLLLAALNVFFRDVQQIVGLLLQLLFFLSPVFYPLSTLPEPLRWLLLLNPLTHI
IELFRAALLGGYLPDWLSLLYALLVSLVLLLLGLLLFRRLRRRFADVL
>gnl|CDD|441289 COG1683, YbbK, Uncharacterized conserved protein YbbK, DUF523 family [Function unknown]
MPKILVSACLLGEPVRYDGGHKRDPFVEELAKYGEFVPVCPEVAGGLPTPRPPAEIVGGDGEVRVVQTKT
GEDVTEAFLAGAEEALKLAREHGIDGAILKSKSPSCGSGRKIYDGTFSGTLKKGVGVFAALLKENGPLVV
EEEGRLNDP
>gnl|CDD|441290 COG1684, FliR, Flagellar biosynthesis protein FliR [Cell motility]
LLAWLAAFLLVFVRIGAFLMVAPVFGSRSVPVRVRLGLALALALLLAPVLPPVLPPVPLSSLGLLLLLLQ
ELLIGLALGFVARLVFAALQLAGQIIGMQMGLSFASVFDPQSGVQSPVLGQFLYLLALLLFLALDGHLLL
IRALVESFELLPVGGAPLSGDALELLVRLFGQMFALALQLALPVIAALLLVNLALGLLNRAAPQLNVFFV
GFPLKILVGLLLLALTLPLLLPVFERLFEEALEALLGLLRLLG
>gnl|CDD|441291 COG1685, AroK2, Archaeal shikimate kinase [Amino acid transport and metabolism]. Archaeal shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
MKGRATAPGAGTIINAIATGKGSAFGIDLKTTAEVELTDGGGIKGEIAGNPDADTRLIERCVELVLERFG
DGNGGTVRTESEIPTASGLKSSSAAANATVLATLDALGEDMDDLDALRLGVEAARDAGVTITGAFDDACA
SMLGGVTVTDNTEDELLKREEVDWDVLIFTPPERAFSADADVERCKLIAPMAELAFDLALEGDYWEAMTL
NGLAYCAALGFDPEPALEALEAGALGVSLSGTGPSYVAVVDRDNLDEVKDAWSKREGKVILTTINNKGAR
VI
>gnl|CDD|441292 COG1686, DacC, D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]
MKKLLLLALLLLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALK
AGKISLDDKVTVSEEAARTGGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNA
KAKELGMTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNGRGITLRNTNRLL
GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYGFPKGEALKAEVVLD
GPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR
>gnl|CDD|441293 COG1687, AzlD, Branched-chain amino acid transport protein AzlD [Amino acid transport and metabolism]
MTTGYLLAAIAVMALATFLTRALPFLLFPRLKPPPLVQYLGRVLPAAIMGILVVYCLKDVDFAAAPYGLP
ELIAIAVTVALHLWKRNALLSIFAGTALYMLLVQLVFV
>gnl|CDD|441294 COG1688, Cas5, CRISPR/Cas system-associated protein Cas5, RAMP superfamily [Defense mechanisms]. CRISPR/Cas system-associated protein Cas5, RAMP superfamily is part of the Pathway/BioSystem: CRISPR-Cas system
MKVLKVDLKGPTASFRKPFTSKSQPTYPLPPPSTVIGMLAAALGRDKDSYFEVMKVAIQGLYPAKTVDLE
RNYVLTKNGRGSKEGGRTPIGREYLFNPRLRIYIVGEDEELLEELKEALEKPVYTLSLGRSEDLVSVEEV
EVVEAEEVEEEKVLTNTYVPLDLAKGLNKEGIPYALPREREVVYELNGSEVEVKEEVEVYKDGDEYVVWL
>gnl|CDD|441295 COG1689, AF1543, Class II terpene cyclase family protein AF1543 [General function prediction only]
MTSLRFDLARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAVRILKLLGEEVPNRDKTIEFLESCQDEEG
GGFALYTTSYGLMALALLGIDPPDEQEALEYLSDALPTKFAGGASDLEETYLAVALLEALGASEPEREKI
REFLLSLRRPDGGFGGKKPNLEDTYWALAALRRLGRDLPPADRVIAFILACQNEDGGFSKTPGSYSDLEA
TYYALRALKLLGEPPKNVDKLLEFIASCQNSDGGFRRSPEGGISTLEYTYYALAVLKWLKRL
>gnl|CDD|441296 COG1690, RtcB, RNA-splicing ligase RtcB, repairs tRNA damage [Translation, ribosomal structure and biogenesis]
LKRIDDYTWEIPKGGMRVPARIWASEVLLEDKALEQLANVATLPGIVKHVAAMPDVHLGYGFPIGGVAAT
EGVISPGAVGVDIGCGMRLLRTDLTAEDLPDKLKELRDALERAVPSGVGSHGIKLSKRELDEVLREGARW
AVEKGYGLEEDLERIEEGGRLEGADPPKVSERAKERGRPQLGTLGGGNHFIEVQVVDEIYDEEAAEAFGL
EEGQVWVMIHSGSRGLGHQIATDYIRLAKKAMKKYGIKLPDRDLAYAPLGSPEGQDYLAAMAAAANYAFA
NRQVIMHLVREAFREVFGKDLGLELVYDVHHNYAKREEHDGREVLVHRKGATRAFPPGHPEEYRRTGQPV
LIPGSMGTASYILRGKGNAESFGSASHGAGRVMSRTAAKRRFTGEDLREELAERGILVEARKDAGVAEEA
PGAYKDIDEVVEAQEEAGLVEVVARLRPLVVVKG
>gnl|CDD|441297 COG1691, COG1691, NCAIR mutase (PurE)-related protein [Nucleotide transport and metabolism]
MDPEALRELLEAVKSGELSVDEALEKLKDLPFEDLGFAKIDHHRELRTGFPEVIYGEGKTPEQIVEIARA
LLERGGNVLVTRASPEKAEALKAAFPEAEYDELARILVIGRGPPPPTGGKVAVVTAGTSDIPVAEEAAVT
AEAMGNEVERIYDVGVAGIHRLLSHLEELRDADVIIVVAGMEGALPSVVGGLVDVPVIAVPTSVGYGASF
GGLAALLSMLNSCAPGVSVVNIDNGFGAGYLAALINRR
>gnl|CDD|441298 COG1692, YmdB, 2',3'- and 3',5'-cNMP phosphodiesterase YmdB, calcineurin family [Signal transduction mechanisms]
MRILFIGDVVGRPGRRAVKEHLPKLKKEYKLDFVIANGENAAGGFGITEKIAKELFDAGVDVITLGNHAW
DKKEILDFIDREPRLLRPANYPPGTPGRGYTIFEANGKKVAVINLMGRVFMPPLDCPFRAADRLLEELKK
ETDAIIVDFHAEATSEKQAMGWYLDGRVSAVVGTHTHVQTADERILPGGTAYITDVGMTGPYDSVIGMDK
EEVIRRFLTGLPVRFEVAEGPATLNGVVVEIDDKTGKAVSIERIRIGGDLPEAL
>gnl|CDD|441299 COG1693, COG1693, Repressor of nif and glnA expression [Transcription]
MTDDLERKLIEILRILSESDEPIGSRRIADELQERGYDISERTVRYHLRILDERGLTKKVGYKGRRLTEK
GRKELERALVSDRLGFVSSRIEELAYRVTFDPETGKGDVIVNISLVDKEDLEDALEILKAVFDSGLSVSP
RVKILEEGEEIGGLTVPEGKVGIATVCSITLDGVLLKRGIPVNPRFGGLLEIENGKPVRFTDLISYEGTS
IDPLEIFISRGMTSVTEALETGSGKILANIREIPLAAREEARELLEKLKDAGFGGVLDVGEPNEPLLGVP
VEPGKVGIVVYGGLNPIAALEEAGIPVETKALSGLIDISEMEEIEEL
>gnl|CDD|441300 COG1694, MazG, NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms]
KELQKRVRAFIKERGWGQYHSPKNLAAALTEEVGELAEAFQWLTGEQSKKDPEKKEELAEELADVLIYLL
CLANQLGIDLEEAFEEKMEKNEKRY
>gnl|CDD|441301 COG1695, PadR, DNA-binding transcriptional regulator, PadR family [Transcription]
MKRQLRKGTLELLILALLAEGPMYGYEIIKELEERSGGFWKVSEGTLYPALKRLEKEGLVESEWEESEGG
PRRKYYRLTEAGREELAEWLEEWEKLAEALEA
>gnl|CDD|441302 COG1696, DltB, D-alanyl-lipoteichoic acid acyltransferase DltB, MBOAT superfamily [Cell wall/membrane/envelope biogenesis]
MLFNSLEFLLFLPIVLLLYWLLPRSRRLRNLLLLVASLFFYAWWDPRFLLLLLLSTLVNYLLGLLIERSR
DKRRRKLLLILGIVLNLGLLGFFKYFNFFLESLNALLGALETDLPLLDILLPLGISFYTFQAISYLVDVY
RGKIKPERNFLDYALFVSFFPQLVAGPIVRAKDLLPQLRKRRTFDYENFARGLRLFLLGLFKKVVIADNL
APYVDPVFDNPESLSGLEAWLGALAYTLQIYFDFSGYSDMAIGLALLFGFRLPENFNSPYFARSITEFWR
RWHISLSTWLRDYLYIPLGGNRKGKLRTYLNLFITMLLGGLWHGAGWTFVIWGALHGLYLVLERLWRKLR
LKLPRLSRLGRLLGWLLTFLLVVFAWVFFRAPSLSDALSILKAMFGLGFGLPELAAYLLLLLLLLLALLL
VIHLPRLKKLGALERLLRRLPAWLRWALYALLLLAILLLGPSGYNPFIYFQF
>gnl|CDD|441303 COG1697, Spo11, DNA topoisomerase VI, subunit A [Replication, recombination and repair]
KKDDERRKKALKKLKELAEKIYDQIEKGEIPVLEIPSRTLSNIEYDEKKGVLKLGDKKSVRSFLNVKQAK
KFMQTLLVASFIKELLEENKTSTLRELYYISKHWILKENTFDEQDESDALIEDLEVATGVLREEFHIRPE
EKGSVVGPLTIRDGTRGDEIDCSKVGEGGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEGFWKKY
NAILVHLKGQPARATRRFLRRLNEELGLPVYVFTDGDPWGYYIYSVIKYGSIKLAHESERLATPDAKFIG
VTPSDIEEYDLPTDKLKDKDIKRAKELLKDPWFQTDYWQKEINLFLKLKKKAEQQALAKKGLDFVTDTYL
PEKLEEGGWL
>gnl|CDD|441304 COG1698, COG1698, Uncharacterized conserved protein, UPF0147 family [Function unknown]
MAKMKDNEEKIKQAIQILDQIINDTSVPRNIRRAATEAKEILKNEKESPGVRAANAISILDEISNDPNMP
SHTRTLIWQVVSQLETIR
>gnl|CDD|441305 COG1699, FliW, Flagellar assembly factor FliW [Cell motility]
IETTRFGEIEVDEEKIITFPEGLPGFEDLKRFVLLPDEEDSPFFWLQSVDDPDLAFVVIDPFLFFPDYEF
ELSDEELAALGLESPEDVLVLVIVTVPEDPEKITANLKAPIVINVKNRLGKQVILEDSRYPIRHPLFEE
>gnl|CDD|441306 COG1700, AQ645, Predicted anti-virus defense system component AQ645, contains DUF2357 and PD-(D/E)xK nuclease domains [Defense mechanisms]
FVSSNHSLEARSDRILATPPRTRSPHILLATDSSETDVLVTTLHVTEVADKESLYKLVVASVKADMGVLN
FGNEVGFTDLLDGRLQIEVFPSKLDYKEDYKEMLREVNDEMANLAFELLSPTYQGAGTSQTRAPSLLEFF
ALLRELFEDLPAALERILRNPHHRLVTEHELVPSEKAKRIDSRTLKELRKHPELLQKSAILGKGYLPRRI
LETRKEVSLDTPENRFVKHALESIRQRLERLRKALEEEKRNTQSAPDPAILRELDEMQRRLQRLLRHTFF
REVGELTRLPSNSLVLQMAPGYREVYRYYLMLRLGLKLDWGDVFNLSVKDVALLYEYWCFLKLRKILREL
YGVEVASQDLIKVDRNGLFVNLRKGRESKFTFENPGTGERITLSYNRTFSRPSFGSPTVAQRPDYVLEIE
KEGSGPAYHYVFDAKYRLEPAAEGSEYKEIENTPGPKEDDLNKMHRYRDAIVAEYERRTFGAYVLYPGDE
EEEFANHKFYKSILVGIGAFPLLPGATELLEQFLKRLLNEELVRELLLERLLSSEWTVAQRTLLLVIVEK
AKDPELSLRNRVVHQLLVKLARLGELRSKTYEDPLYKGKAKFAYIQYYAQLQLRSKHGFIEVRLLIRAYA
STKTALIEKIVEILSPPSKSRDLYSLKQLAALPELIKKKQYELTELAFSSLLRLLGVNELLELALELEEA
LKLTLDEDRLLLDSVPVVEEKCLL
>gnl|CDD|441307 COG1701, aPPS, Archaeal phosphopantothenate synthetase [Coenzyme transport and metabolism]. Archaeal phosphopantothenate synthetase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
MMDIPKDHPRYESLLTREKLVEGVEKGIVAPQGLIAHGRGEAFDYLLGEKTTPSALEAERAAAAALLLAK
HPVISVNGNTAALVPEEIVELAEAVGAKIEVNLFYRTEERVEAIAEHLREHGAKEVLGLDEDARIPGLDH
ERAKVDPDGIYSADVVLVPLEDGDRTEALVKMGKTVIAIDLNPLSRTARTATITIVDNITRAVPNITEFA
RELKGADREELEEIIRSFDNKENLAEALEEIRERLKRLADE
>gnl|CDD|441308 COG1702, PhoH, Phosphate starvation-inducible protein PhoH, predicted ATPase [Signal transduction mechanisms]
EEMTELTLELPDNERLAALFGPFDENLRLIERALGVKIVARGNELKISGEEEAVERAERVLEELYELARK
GNPLTPEDVELALRMARAGEEEELAELLDDVIVITTRGKPIRPKTPGQKRYVDAIRKNDIVFGIGPAGTG
KTYLAVAMAVAALKRGEVKRIILTRPAVEAGEKLGFLPGDLKEKVDPYLRPLYDALYDMLGPEKVERLIE
RGVIEIAPLAYMRGRTLNDAFVILDEAQNTTPEQMKMFLTRLGFGSKMVITGDITQIDLPRGQKSGLVEA
LEILKGVEGIAFVYFTSKDVVRHPLVQRIVEAYEKYEAKKEAKRE
>gnl|CDD|441309 COG1703, ArgK, GTPase of the G3E family (not a periplasmic protein kinase) [Posttranslational modification, protein turnover, chaperones]
LDVEELVEGLLAGDRRALARAITLVESRRPEHLARELLKALLPHTGKAHRIGITGVPGAGKSTLIDALGL
RLRERGKRVAVLAVDPSSPFTGGAILGDRTRMEELARDPGVFIRSSASRGSLGGLARATREAILLLEAAG
FDVIIVETVGVGQSETDVAGMADTFLLLLLPGAGDELQGIKAGIMEIADIIVVNKADGDGAERAVRELRG
ALHLLRPAEPGWRPPVLTTSALTGEGIDELWEAIEEHRAYLKESGELEERRREQARRWLWELVRERLRER
FREQPEVRARLDELEEAVLAGELDPYAAADELLEALL
>gnl|CDD|441310 COG1704, LemA, Magnetosome formation protein MamQ, lipoprotein antigen LemA family [Cell wall/membrane/envelope biogenesis]
MKKTLIILLAILVLLVLWGISIYNRLVRLRERVKAAWSQIDVQLQRRADLIPNLVETVKGYAAHEKETLE
AVTEARAKATSAQIGDPAELAQAEGQLSGALGRLLAVAENYPDLKANQNFLDLQEELEGTENRIAVARRR
YNDAVRDYNTKIRSFPSNLVAGMFGFKPKEYFEAEEAEREAPKVSFD
>gnl|CDD|441311 COG1705, FlgJ, Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility]
LASLDSSSASSSAGAAAQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALGGGAS
ALSSAAALALKSAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAA
QKAAKKYGVPASVLIAQAALESGWGKSELDGSPSNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARF
RAYDSYAESFRDYARLLKNNPRYAGALANAKDYEAFAKALQKAGYATDPKYADKLISIIESYNLTQ
>gnl|CDD|441312 COG1706, FlgI, Flagellar basal body P-ring protein FlgI [Cell motility]
MLRRLLLLLALLLLLAAAAAAAAVRIKDIASVQGVRDNQLVGYGLVVGLDGTGDSTTQTPFTEQSLANML
ERLGVNVPPTNLQLKNVAAVMVTAELPPFAKPGQRIDVTVSSIGDAKSLRGGTLLMTPLKGADGQVYAVA
QGNLVVGGFGASGDGSSVTVNHPTVGRIPNGAIVEREVPTDFGDGGSLTLNLRNPDFTTARRIADAINRR
FGPGTARALDARTVRVRAPADPSGQRVAFLAEIENLEVEPDAPARVVINERTGTVVMGQNVRISPVAVAH
GNLTVTITETPQVSQPNPFSGGQTVVVPRTQIDVEEEGGRLFVLPEGASLQDLVRALNALGATPRDLIAI
LQALKAAGALQAELEVI
>gnl|CDD|441313 COG1707, AF1403, Uncharacterized protein, contains ACT and PBP-like DUF5612 domains, MJ1458 family [General function prediction only]
MLIALTIIAENKPGVLRDITGVIAEHGGNITYTQQFVEDDGKALIYMEIEGVDDIEDLLSELRALPSVRE
VEVHKSLEEIYGKRVIIIGGGAQVAQVALGAISEADRHNIRGERISVDTIPLVGEENLAEAVRAVARLPR
ASILVLAGSLMGGEITEAVDELKEEGIPVISLNMAGSVPDVADLVVTDPVQAGVMAVMAISDTAVFDINR
VRGRVF
>gnl|CDD|441314 COG1708, MJ0604, Predicted nucleotidyltransferase, MJ0604 family [General function prediction only]
MSTLLRELLEEIVEALRRGPEVAAVYLFGSYARGDARPDSDIDLLVVVDDPPLPDERLELLADLLRELGL
PVDLVVLTPAELELRLFLREILREG
>gnl|CDD|441315 COG1709, COG1709, Predicted transcriptional regulator,contains XRE-type HTH domain [Transcription]
MMDYPREELAEKIAGEITLSDDPGETLRKWREDFGISQTELARELGVSPSVISDYESGRRKSPGIAFVKK
FVEALLEIDEERGGKVIRQLARVLSAGFDSDAILDIREYSSPVPLEEFVDAIDGTLVVSGDLDRRIYGYT
VIDSIKAILELSSEEFYRLYGWSTERALIFTNVSTGRSPMVAIRVSPLKPAAVVLHGPDKVDPLAIKLAE
IEGIPLIVTTLDIEELLKRLRELK
>gnl|CDD|441316 COG1710, MJ1475, Predicted DNA-binding protein MJ1475, contains C-terminal HTH domain [General function prediction only]
MKIRVVSSKEEIRKLDENEVEVHLAFRPSNEDIFSLVERCPNVKVIQCPPSYYRTVSKSVIMFLEMQGIK
LLEGDVWGHRKDINEYYEISPKVYDRIKELRNEGKSDEEISDKLGRETKLPIDTLYYLLKKKSDS
>gnl|CDD|441317 COG1711, COG1711, DNA replication initiation complex subunit, GINS family [Replication, recombination and repair]
MDLDELRSILRKERKSDSLQEIRPDFYEDVAEYIAELEEERDRAASDDPSSPEVRRLTDEIETAREVVEA
IFERRIGKIVKLALRAAAGMTSDGLTPEERELYDDLVDAIESNREEVLDPLAGPETTEAPEIAPEEPETI
EEPAEPSPEAEPEDEEPEAPEEPAGKAEINEEYVVVRILEDVPPFAGVDGRNYTLHKEDVVTLPELNADV
LVKRNAALKINL
>gnl|CDD|441318 COG1712, AspD, L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism]
MRIGLIGCGAIGSEVAEALADAGVELVAVYDRDPERAEALLASLGARVVSDVDELLAADPDLVVEAASQA
AVREHGPAVLEAGKDLMIMSVGALADEELLERLEAAAREGGARIYLPSGAIGGLDALKAARIGGLDSVTL
TTRKPPKSWKGTPAEKLIDLDALTEPTVIFEGSAREAARLFPKNANVAATLALAGIGFDRTRVRLVADPA
ATRNIHEIEAEGDFGEFEIRVENVPSPDNPKTSYLAALSAVRALRNLVAPIVI
>gnl|CDD|441319 COG1713, YqeK, Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal transduction mechanisms, General function prediction only]
MDREEILEKLKERLSPKRYEHTLGVAETAVELAERYGVDVEKAELAGLLHDYAKELPPEELLELAKEYGL
DLDELEEYNPELLHGPVGAYLAKEEFGITDEEILNAIRYHTTGRPNMSLLEKIIFLADYIEPGRDFPGVE
ELRKLAKQDLDEAVLEALDNTIKYLIEKGRLIHPRTIEARNYLL
>gnl|CDD|441320 COG1714, YckC, Uncharacterized membrane protein YckC, RDD family [Function unknown]
MSIETPEAVALELRYAGLGRRLLAFLIDLLILFALLLLLALVLLLGLLGALLGLLLLLGFLVAFLYFVLF
ETLRRGQTLGKRALGLRVVDLDGGPISFGQALLRNLLRILSILPLGLGLLWALFDKRRQRLHDLLAGTVV
VRE
>gnl|CDD|441321 COG1715, Mrr, Restriction endonuclease Mrr [Defense mechanisms]
GRKALAAYEEIRAELAEELLERLRSLSPYEFEELVAELLRRMGYGSVEVTGRSGDGGIDGIAKEDRLGGD
RIYVQAKRYKGNTVGRPEVREFAGALAGEGADKGIFITTSRFTKDAREEARRLGRRIELIDGDRLAELLI
EYGVGVQTERIDEDYFE
>gnl|CDD|441322 COG1716, FHA, Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]
MARLVVLEGPLAGRRFPLDGGPLTIGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFVNGQ
RVTEPAPLRDGDVIRLGKTELRFRLS
>gnl|CDD|441323 COG1717, Rpl32e, Ribosomal protein L32E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L32E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
TPELSEETKRLLKLRKKQKRKKPEFKRQDWWKYKRLGDSWRKPRGIDNKQRLQLKGKPPLVKVGYRSPKA
VRGLHPSGFEEVLVHNVKDLEGLDPETQAVRIASTVGLRKREEIEEKAKELGIKVLNPTVVE
>gnl|CDD|441324 COG1718, RIO1, Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms]
MKDRRLDREIDKLRKRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLARRPGG
ELVAAKIYRTATSSFKRMAQYIEGDPRFMGKGSFGRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGN
VLLMEFIGDDGVPAPRLKDVELEPEEAEELYEQLIEYIVRLYKAGLVHGDLSEYNILVDDGGPVIIDLPQ
AVDVAHPNAKEFLERDVENIARFFARFGPELDPEELLKEIWA
>gnl|CDD|441325 COG1719, COG1719, Predicted hydrocarbon binding protein, contains 4VR domain [General function prediction only]
MAAEEDFLVALFRALEEELGIAAARVLYRAGKRIGKELAERFKEEADLLEALKEFWKLSGWGILEIDELS
EGPLVITVEDSPECRGLPNSGKPVCHFLAGLLAGFFSELLGKEVEVRETECEAMGDDYCRFEVRPKE
>gnl|CDD|441326 COG1720, TrmO, tRNA (Thr-GGU) A37 N6-methylase [Translation, ribosomal structure and biogenesis]. tRNA (Thr-GGU) A37 N6-methylase is part of the Pathway/BioSystem: tRNA modification
EITLRPIGVIRSPFKEKFGIPRQPRLAPGAEGEIELFPEYAEALRGLEGFSHLWLLYWFHRARRWRLTVR
PRLGGNERRGVFATRSPHRPNPIGLSVVRLLGVEGNRLHVRGLDLLDGTPVLDIKPYVPYADAIPDARSG
WAEEAPEELLAV
>gnl|CDD|441327 COG1721, YeaD2, Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown]
RLSVERSLPPRLSVGEEVEVTLTLRNSLGPGTLRYTLRPRRGVYRLGPVTVRVRDPLGLFERRRTVAAPA
ELTVYPLLAALRRLELRARRRVRGVLAGEHRSRRRGDGTEFAELREYQPGDDLRRIDWKATARTGELYVR
EFEEERELTVVLLLDTSASMRFGSGGPSKLDLAVEAAASLAYLALRQGDRVGLLTFGDRVRRYLPPRRGR
RHLLRLLEALARLEPAGETDLAAALRRLARRLPRRSLVVLISDFLDPEELGIDVVDVRTDEPLVAALLRY
LRLKRRG
>gnl|CDD|441328 COG1722, XseB, Exonuclease VII small subunit [Replication, recombination and repair]
DKKELSFEEALAELEEIVERLESGELPLEESLALYERGVALAKRCQKKLDEAEQKVEKLLEDEDGELEEP
FDPE
>gnl|CDD|441329 COG1723, Rmd1, Mitochondrial translation protein, Rmd1/RMND1/DUF155 family [Translation, ribosomal structure and biogenesis]
MMMLRCRAYCLGERIDLKRLEEALKLSTKYRWRDPLILRVGEGGFVVLFRYGVVVFFGVSEDEEADFLDE
LKPFVEEPLEEPESEEFEIEIGPDEEDRVEEDHIILPDLDPERLLLVSDVLAQSVALARYEERVAALFDE
IEPLAQELAKKGKLPLSRKELLKKIGKLLLIKHRIILRVEILDKPEFFWENPELERLYLRLEDEFELKER
YEALNRKLEIIHETLETLLDLLQHRHSSRLEWIIIILIVVEIVLTLYEKFF
>gnl|CDD|441330 COG1724, YcfA, Predicted RNA binding protein YcfA, dsRBD-like fold, HicA-like mRNA interferase family [General function prediction only]
MPKLPSMKGRELIKALEKLGFVLVRQKGSHHILKHPDKGRTVTVPRHPGKELPPGTLRSILKQAGLTREE
FL
>gnl|CDD|441331 COG1725, YhcF, DNA-binding transcriptional regulator YhcF, GntR family [Transcription]
IRIDFDSGVPIYEQIADQIKEAIASGELKPGDRLPSVRELAAELGVNPNTVAKAYRELEDEGLIETRRGK
GTFVAEDARELLEERREEFLEEALRELVAEARRLGLSLEELLEL
>gnl|CDD|441332 COG1726, NqrA, Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrA [Energy production and conversion]. Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrA is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase
IKIKKGLDLPIKGAPEQVIEDGPASKTVALLGEDYVGMKPKMLVKEGDRVKAGQPLFEDKKNPGVKFTSP
VSGTVVEINRGEKRVLLSVVIEVDGDEQETFEKFGASDLASLSREQVKENLLESGLWTAIRQRPFSKVAA
PDSTPKAIFVSAMDTNPLAADPEVIIAGQEEAFQAGLTALSKLTDGKVHVCVAPGSSLPFAGLKGVEVHT
FSGPHPAGLVGTHIHFLDPVNKGETVWTINYQDVIAIGKLFLTGKLDTERVVALAGPEVKKPRYVRTRLG
ASLDELVAGELKDGENRVISGSVLTGRKATGPDGYLGRYHNQVSVLPEGREREFLGWLRPGFNKFSVTRA
YLSWLFPKKKFDFTTNTNGSERAMVPTGNYEKVMPLDILPTQLLKALIAGDTDEAEALGCLELDEEDLAL
CTFVCPSKYEYGPILREGLDLIEKE
>gnl|CDD|441333 COG1727, RPL18A, Ribosomal protein L18E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L18E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
KTNPRLVSLIRDLKKASRENDAPIWRDVAERLEKPRRNRAEVNLSKINRYAKEGDTVVVPGKVLGSGKLS
KKVTVAAFSFSETAAEKIEEAGGECLTIEELVKENPKGSGVRII
>gnl|CDD|441334 COG1728, YaaR, Uncharacterized conserved protein YaaR, TM1646/DUF327 family [Function unknown]
MKINDLKRTNLSSKKSRKSKKKAEKSKSSFSDVLEKQEEKLSKEELDELLEEIDEQGERLARSPTLRDLK
KYKKLVKEFLKEAVKNGYKLKEESSWDRRGRSRVYTIVKKVDEKLEELTEELLSEEKDRLDILAKIGEIR
GLLIDLYT
>gnl|CDD|441335 COG1729, CpoB, Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning]
KALLKAGDYDEAIAAFKAFLKRYPNSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDAL
LKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARARLARL
>gnl|CDD|441336 COG1730, GIM5, Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones]
MSDGEGEEELQQLLQQLQELEAQIEALQQQIELLQASIEELDAAIETLEALKSGEGSEVLVPLGGGAFVK
AKVKDKDKVIVSLGAGVAVEKDLDEAIEYLEKRIKELEKALEKLEEELQELEEEYEELEQQLQQLQQQAQ
QQQMQ
>gnl|CDD|441337 COG1731, RibC2, Archaeal riboflavin synthase [Coenzyme transport and metabolism]. Archaeal riboflavin synthase is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
MKKIGIADTTFARVDMGSAAIDELKKLLPSVKIVRYTVPGIKDLPVAAKKLIEEEGCDIVIALGMPGPKE
KDKMSAHEASTGLIMAQLMTNKHIIEVFVHEDEAEDEKELAWLAEDRAREHAENLVKLLFKPEKLTREAG
TGLRQGYEDAGPIRG
>gnl|CDD|441338 COG1732, OsmF, Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system (osmoprotectant binding protein) [Cell wall/membrane/envelope biogenesis]
MKRLLLLALALAAALALAGCGLASAAAAGDTIVVGSKNFTEQEILAEIYAQALEAAGLKVERKLNLGGTE
VVRQALKSGEIDLYPEYTGTALTTYLKEDPITDPEEVYEAVKEALPEKNGLTWLDPAGFNNTYALAVTKE
TAEKYGLKTISDLAKVAGELTLGADPEFAERPDGLPGLKKAYGFEFKEVKPMDTGLTYTALANGQVDVAD
AYTTDGRIAALDLVVLEDDKNFFPPYNAAPLVRKEVLEKYPELAEVLNKLSGKLTTETMQELNYQVDVDG
EDPADVAREFLKEK
>gnl|CDD|441339 COG1733, HxlR, DNA-binding transcriptional regulator, HxlR family [Transcription]
KKKDLKEADCPVRRALDVIGGKWKLLILRALLDGPRRFGELRRSLPGISQKMLTQRLRELEEDGLVERTV
YPEVPPRVEYSLTEKGRSLLPVLDALAEWGEEHLPEIE
>gnl|CDD|441340 COG1734, DksA, RNA polymerase-binding transcription factor DksA [Transcription]
MSDEQLEEFRERLLEEREELLEELEETEEELLSGDLSAYDPDPADRATEEEERELELALRDRERKLLRKI
DAALERIEEGTYGICEECGEPIPLERLEARPTATLCIECKERQERRERR
>gnl|CDD|441341 COG1735, Php, Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction only]
MGFVRTVLGPIPPEELGVTLMHEHLFVDLPGVRQDPPADDDELDDVEAAVEELERFKAAGGRTIVDATPI
GLGRDPEALRRISEATGLNIVAATGFYKEPFHPEWVLGASVDELAELLIREITEGIDGTGVRAGVIKIGT
SYGGITPDEEKVLRAAARAHRETGAPISTHTEAGTMGLEQLDLLEEEGVDPERVVIGHMDRNPDLDYHRE
LADRGAYLEFDGIGRDKYYPDEERVELIAELIERGYADQILLSHDVGRKSYLKAYGGPGYDYILEVFLPR
LRRRGVTEEDIDTLLVDNPRRLFAF
>gnl|CDD|441342 COG1736, DPH2, Diphthamide synthase subunit DPH2 [Translation, ribosomal structure and biogenesis]
MLYDIDLDRIIEEIRERGAKRVALQFPEGLKRRAPEIAEKLEEETGVEVIISGDPCYGACDLATDEAKGA
DLLVHFGHSPMPEYYKEPVIFIEAFSDVDVDEVLEKALEELKGKKIGLVTTVQHVHLLDEVKEILEEHGF
EVVIGKGDGRITYPGQVLGCNFSAARNVDVDAYLFVGGGNFHPLGVALSTGKPVLALDPYTGEVREVDEE
AERILRKRYAAIAKAMDAKTFGIIVSTKIGQYRPELAKRLKKLLEKHGKKAYLITMDEITPDRLLNFGID
AYVNTACPRIAIDDQGRFPKPVLTPGEFEIVLGLRKWEDYEFDEILGV
>gnl|CDD|441343 COG1737, RpiR, DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription]
MMSAMSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPEL
KLALAQELAEGLSSYERLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIF
GVGASAPVAEDLAYKLLRLGKNVVLLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGA
KVIAITDSPLSPLAKLADVVLYVPSEEPTLRSSAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEAL
LSELRE
>gnl|CDD|441344 COG1738, YhhQ, Queuosine precursor transporter YhhQ, DUF165 family [Translation, ribosomal structure and biogenesis]
MLVSFAYRKTRGLIGLAALFVTVLILSNILVQKLVSLFGGFVLTAGAFLFPLTFLATDILTEVYGKKAAR
RVVWLGFLANLLASLLIQLALLLPPAPFWTGQEAFEAVFGFVPRIVLASLLAYLVGQLLDVYVFHRLKKR
TGGKHLWLRNNGSTLVSQLIDTLIFFTIAFYGVFPWEVLLEIILSQYLFKLLVALLDTPFTYLVVRWLKR
REGLDVYDEA
>gnl|CDD|441345 COG1739, YIH1, Putative translation regulator, IMPACT (imprinted ancient) protein family [General function prediction only]
MDSYKTIAAPAEAEIEIKKSRFIAYAAPVESEEEAKAFIAEIRKEHPDATHNCWAYRIGAPGEIQRASDD
GEPSGTAGKPILEVLQGRGLTNVLVVVTRYFGGIKLGAGGLVRAYGGAAAEALEAAGIVEKVPQVELTLT
VDYALLGKVERLLKQHGAEILDQDYGEDVTLTLAVPEDEAEAFEERLTDLTRGRAEIE
>gnl|CDD|441346 COG1740, HyaA, Ni,Fe-hydrogenase I small subunit [Energy production and conversion]
MSKEETLYEKLRRRGVSRRDFLKFCAATAAALGLPPSAAPRVAEALETKPRPPVIWLHGQECTGCTESLL
RSSHPTVEDLILDMISLDYHETLMAAAGHQAEEALEEAMEKYKGKYILVVEGSIPTGDGGIYCTIGGKTF
LEILKEAAEGAAAVIAVGSCASFGGVPAAKPNPTGAVGVSDVLKDKPVINVPGCPPNPDVITGTLAHYLT
FGKLPELDALGRPKFFYGRRIHDNCERRPHFDAGEFAEEFGDEGARKGWCLYKLGCKGPVTYNNCPTRRW
NGGVSWPVQAGHPCIGCSEPGFWDKGSPFYERLPDIGIPGIEANADKIGAGALGAAAAGIGAHAAASAVK
GRLAKKLKKEGEEE
>gnl|CDD|441347 COG1741, YhaK, Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only]
RPTDLGGGLKVRRYLPSRDRRGFGPFRVLDHDGPAPPGYGAGFPPHPHRGMETVTYVLEGELEHRDSLGN
GGVIRPGDVQWMTAGSGIVHSERNPSEGGPLHGLQLWVNLPPADKGLAPRYQHIPDIPEVELGGGRLRVI
AGPLDGVDGPVKIHQDALLYDIRLDAGATLTLPLPPGREAYLYVIEGSVTVNGETLEAGDLAVLSDGDEL
TLTADEDARVLLLGGEPLDEPIVMWGPFVMNTKEEIEQAKEDW
>gnl|CDD|441348 COG1742, YnfA, Uncharacterized inner membrane protein YnfA, drug/metabolite transporter superfamily [General function prediction only]
EMLKTLLLFILAALAEIGGCYLPWLWLREGKSAWWLLPGALSLALFAWLLTLQPAAAAGRVYAAYGGVYI
AASLLWLWLVDGVRPDRWDLIGAAICLIGAAIILFAPR
>gnl|CDD|441349 COG1743, COG1743, Adenine-specific DNA methylase, contains a Zn-ribbon domain [Replication, recombination and repair]
MTDQTRPKKLIEVALPLEAINEEAAREKSIRHGHPLSTLHLWWARRPLAAARAVLLASLLDDPSDIDPEE
FLTELGIGPERELVAWENSPNEEVLEEARAEIREAWGGELPTVLDPFAGGGSIPLEALRLGLEVVASDLN
PVAVLILKATLEYPPKFGEGLAEDVRRWGEWIREEAEKRIGELYPTDPPGCEATVIAYLWARTVTCPNCG
AEVPLVSSWWLAKKKGKEAAVCPIVDPEPKRVDFEVVEGKKKCGEEFDPSDGTVRRGKATCPHCGTTIPG
DYIRDQAKAGRMGQRLYAVVYEGPSGGRGYRAPTEEDLEAAEKAEEELEEKWDLDWVPDEEIPEGSRTFR
PIRYGMTKWRDLFNPRQLLALTTLSELIREAREEILREAGATEYAEAVATYLALAVSKLLDYNSRLCRWD
SGREKIRNTFGRQAIPMVWDFAEANPLGDSSGGFSWALEKVVKALEYLVAPVEGYGGNGTVLQGDATDLP
LPDGSVDAVVTDPPYYDNVPYAELSDFFYVWLRRSLGDIYPDLFSTELTPKAEELVANPYRFGGKDKAEE
FFEEGMTEAFAEMRRVLKPDGPLTVYYAHKSSEAWETLLEALIDAGFTITATWPVRTEMPGRLHARGKNA
LASSIVLVCRKREADAETGSWRDVRRELRREAPEALEELQKGGIAGVDLIQAAIGPALEVFSRYYPVLEA
DGEPVSVREALEEINRAVDEALLEELLGEGEFDPDTRFYLLWWEQYGAAEGPYDEARKLARAVGTDVDDL
KRAGIVEKKGGKVRLLTPDELPDDWDPEDDRTVWDALHALIRALEKGGEEAAAKLLAKLGLKAEAFRELA
YALYTVLPRWAEEAEAYNDLLTSWDRQGTLD
>gnl|CDD|441350 COG1744, Med, Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC superfamily, includes NupN [Signal transduction mechanisms]
AAAEKLKVALVYVGGIGDKSFNQAAYEGLEAAEKELGVEVKYVESVPEADYEPALRQLAEQGYDLIIGVG
FGFADALLKVAKEFPDVKFAIIDGYVDGAPNVASYFFREEEGSYLAGVLAALMTKTGKVGFVGGMPIPEV
IRFINGFALGAKYVNPDIKVLVVYTGSFSDPAKGKEAALALIDQGADVIFQAAGGTGVGVIQAAKEAGKV
YAIGVDSDQSALAPDVVLTSAVKRVDVAVYDAVKAVLDGTFKGGDYVLGLKEGGVGLAPDEDFGDLVPAE
VKAKVEELKAKIISGEIKVP
>gnl|CDD|441351 COG1745, COG1745, Uncharacterized metal-binding protein MJ1132, UPF0058 family [Function unknown]
HKEELIHLHQLLVEVKKYFEEEGNEEEDFKEYEELGISPTHIHKSKTEHKAAIFVLGNGIASAMSEDEFE
SAGRISKRLKELADRAEKEI
>gnl|CDD|441352 COG1746, CCA1, tRNA nucleotidyltransferase (CCA-adding enzyme) [Translation, ribosomal structure and biogenesis]. tRNA nucleotidyltransferase (CCA-adding enzyme) is part of the Pathway/BioSystem: tRNA modification
DLEDVLEEVLERIKPTEEERERLEEVADELIERIEEAAKELGIDAEVVLVGSTARGTWLSGDRDIDIFVL
FPPDLPREELEEYGLEIGHAVLPDFEGEEEYAEHPYVTGTIDGFDVDLVPCYRVESATKIRSAVDRTPFH
TRYIKERLDDGLADDVRLLKQFLKGIGVYGSELKTRGFSGYLCELLVIEYGSFENVLEAAADWRPPVVID
PENHGTKKFDDPLVVIDPVDPERNVAAALSLENLARFIHAAREFLEDPSEEFFFPPPPEPLSAEELREHL
ERRGTTPVAIVFEKPDLVDDVLYPQLRKSLRGLVKLLEREGFDVLRSGAWADEERAVLLFELEVAELPAV
KRHEGPPVWVREHAERFIDKYADDEAYGPFIEGGRYVVERERKYTTAEELLRSELFDVSLGKHVEEALEE
GYEVLVGEEILELAEEFGEFLAEYLDPK
>gnl|CDD|441353 COG1747, COG1747, Uncharacterized N-terminal domain of the transcription elongation factor GreA [Function unknown]
MSEEIEQKITELLNEEKWTRATANNYSVSKFKELDDLIDEVKDEGKTEVKELCDEHLKHSKNSIIALYIS
GIISLSRQSLDDSNLLNLIDIFSENHKWAIVEHLCNKILEYGENKHALRTLAECYEKLGNKELYGVWERL
VKVDYEEADIVKKLAEKIEEENKEKAIEFYKKAIYRFINNKDFSKFKELWEELCENDPVDGDFFLRILRK
IKGSDLATRFGQLLEDLYPLWKKIEDWDESIEILKLILDLDSNSPWAREELIECLKKKYKDHSLLEEYLK
LSGLRNKWRNFQGAISDFEKLIHFDKGNFVFHRSWGVGEIMSISFNGDKVVIDFAVKKGHDMSFAMAFKS
LKPLSKDHILVRKFTDPDELEKKIKKDPPWALKELLKSFDGPATAAEIKEELVPLVIPESEWSKWWQKAK
KKLKKDPRIGVPPKKKDPYVLRDTPVSHEEKLQEKFKAQKDFNDRIQLAYEFLRDSDSESEAFEEMLDYF
TEALKNSGLVDAQEIQAYLLLEDLLAKLPFGNKALEPSFAELIKSVDDLEEVFEKIEIAELKKRFLDLVR
KHRSNWREIFIKLLFTSPGKLRKYIIKELLEEGKREELSKKLKRLLDNPKDNPEVFIWVFKNIHAKEWEL
EGISDEELLEAFLRLLDYLKAEPENRKLNKKLYNILFKRDELVRDLIENADEEFIKEFYLLLKKVPDFSD
HDKKILRSLIEEVHPSLAFEDEKSEEDVRLSTTTLFIRDTEAKQLLIEKEIEQIETLAEVENAIEIERLR
ELEKYALEAEAKLLLEARVNSLLDLATLALLADTKSALTKDVGFKRKVKIGNGVTVKLEEESILGPWESG
PILAIISYTALSGESKKKHLLKELLGKEIKNSKRDYFTIKEEIEEVDDAY
>gnl|CDD|441354 COG1748, Lys9, Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]. Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis
YEVTLADRSLEKAEALAASGPKVEAAQLDASDPEALAALIAGADLVINALPPYLNLTVAEACIEAGVHYV
DLSEDEPETEAKLALDELAKEAGVTAIPGCGLAPGLSNVLAAYAADRFDEIDSIDIRVGGLPGYPSNPLN
YGTTWSPEGVIREYTNPARAIEDGKWVEVPPLSERETIDFPGVGRYEAYNTDGELETLPETYPGVKTVRF
KTGRYPGHLNHLKVLVDLGLTDDEPVEVEGVEVSPRDVLKAILPDPLPLGPTDKDVVVIGVVVKGTKDGK
RETYVYNLVDHEDAETGSTAMAYTTGVPAAIAAELLLEGKIPKPGVVNPEQLDPDPFLEELAKRGIPIEE
EE
>gnl|CDD|441355 COG1749, FlgE, Flagellar hook protein FlgE [Cell motility]
MMMSFNTGVSGLNAASTALDVIGNNIANSNTVGFKSSRAEFADLVAQSLSGANPTQVGGGVRVASVAQIF
TQGSLQSTGNALDLAISGNGFFVVSDSGGQTYYTRAGSFSLDKDGYLVNSSGLYLQGYPADADGTIPDTG
GGLEPIQIPTGQLPAKATTKVTLGGNLPADATVPTAPFDPTDPTTYNFSTSVTVYDSLGNSHTLTLYFTK
TGANTWTVYVTVDGADVTGGTGATGTGTLTFDSNGKLTSPTSGGPGTLTLTVNGAAPQTITLDLSGLTQY
ASSFSVTSLTQDGYAAGTLTGVSIDDDGVVTATYSNGQTRPLGQIALATFANPQGLQKLGGNLWAETANS
GEPLLGTAGTGGLGSIQSGALESSNVDLAEELVNMIVAQRAYQANAKVITTSDEMLQTLVNLKR
>gnl|CDD|441356 COG1750, COG1750, Predicted archaeal serine protease, S18 family [General function prediction only]
MKSKLLASLLLLLLLASPLAAQSNSAVRSVTIYAPAVSGTGEGVVINITVTVTYPGSGRVYVSTSPLTGP
DTQASARIAALVASLLAGVDLSSYDVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMIN
PDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQAILTGYNTQVGETVDLVEYGKELGVKVIEVSTIADALQ
YFT
>gnl|CDD|441357 COG1751, PK, Ligand-binding C-terminal domain of pyruvate kinase, DUF1867 [Carbohydrate transport and metabolism, Signal transduction mechanisms]
EKSIMYFEKPGKENTEATLELAVERAKELGIKHIVVASTSGETALKALEALKGKDVNLVVVTHHVGFREP
GEDEMDPEVREELEKAGVKVLTGTHLLSGVERAISNKFGGVYPVEIIAETLRLFGQGVKVCVEIALMAAD
AGLIPVGEEVIAVGGTGRGADTAVVIRPAHSNNFFDLKIREIICKPREK
>gnl|CDD|441358 COG1752, RssA, Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only]
APARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRR
DLFDLSLPRRLLRLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLA
DAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNPPLRKLPSLLDILGRALEI
MFNSILRRELALEPADILIEPDLSGISLLDFSRAEELIEAGYEAARRALDE
>gnl|CDD|441359 COG1753, VapB3, Predicted antitoxin, CopG family [Defense mechanisms]
MTKTISISDEVYERLKRIKREDESFSDVIERLLKERKEDLLEGFGTLSDEEADELEEAVKESREEFDERL
DERDEE
>gnl|CDD|441360 COG1754, COG1754, Uncharacterized C-terminal domain of topoisomerase IA [Function unknown]
KSAAVLVVVVVVVVKVPAAKKVLPKYAKKKKGVKAVLKKADVAKADDKVVDDDDKKDDVDDDKKKKKKLL
KAAAKKKKALALALAADDEDEELLAADDELEEEKVIKLLLLELAVERVARAAAVRAAAAEAARLAALLRR
RLVLRRLVRRLLVRLLLLRLVLLLLRLLVARRAARRRRRRRRRRARRRELERRRERARAAEAEEAAAAAA
AAADAGRAAAARDGKGGGKLAAGGAAAAAAAAAAAAAAAAALAEAAAAAAVREPPTPTTTTTAQAATTTT
TRAAAARTTRSAQQAARRTRLGGEGTYTTTTTTTTTTSAAAAAAAAAAAALAAAAAAAYAPPPPYYYKKK
AAAAAAAAAAAAAAAARRPPAARAALLSDDRLLLELLLLRRTAAAAAAAAAATATTTAAAAAAGAGAVGT
AAAGAVFFFGGFLLFAEEEDDDEEDDDDDDLPALEEGLPLLKEGVLADQHFTQPPPRYTEAPLVKRMEEL
GIGRPSTYASILSTLADRIYVRLDKRRLIPEDKGRLVTAFLFSFFRRYVEYDFTADLEEFLDDVSDGELD
WKAVLRRFWRDFSAAYDETGDLRISEVLDALEDLGEIDPREINSCPLGTGGLSLRVGRYGPFIECSNYEP
RRASIPECLAPDELTPEKAEELLEAPADGPRVLGTDPETGKPIVLKDGRFGPYVQLGEPEKEDKPKPKRA
SLPKGMSPETVTLEDALKLLSLPRVVGEHPETGEEITAQNGRFGPYLKHGKDYRSLKSEDDVFTITLNRA
LELLAQPKARGRRAAAPPLKELGEHPVSGKPVVVKDGRYGPYVTDGKTNATLPKDDDPESLTLERALELL
AEKRAKGPAKKKKAAKKAAAKKAAAKKTAAKKAAAKKAAAKKAAAKKAAKKA
>gnl|CDD|441361 COG1755, YpbQ, Uncharacterized conserved protein YpbQ, isoprenylcysteine carboxyl methyltransferase (ICMT) family [Function unknown]
MMLWFLLLFLLVFLQRLAELVISRRNEKWLLARGAVEYGAGHYPLMVVLHTLFLASLILEALLRGRPFLP
PLSWIGLALFLLAQALRYWVIRSLGRRWTTRIIVLPGAPLVTSGPYRYLRHPNYFLVVLELAALPLLFGA
WITALLFSLLNALLLAVRIRAEEKALKELTA
>gnl|CDD|441362 COG1756, Emg1, rRNA pseudouridine-1189 N-methylase Emg1, Nep1/Mra1 family [Translation, ribosomal structure and biogenesis]
MLKLILAESALELVPKELWNHPAVVKNARRRGKRPSEILLDSSLHHAAMKRLPEAEKRGRPDIVHISLLE
ALESPLNKEGKLRVYVHTIDDKVIFVGPETRIPKNYNRFVGLMEQLFKEGRVPPNGKPLLELENMSLSEL
LEEINPSRVILLSEKGEKVSPEEIASEALEENPCVVIGGFPHGDFSESTKKKADKVYSIYDEPLEAWTVA
SRILYAYEKLLGLL
>gnl|CDD|441363 COG1757, NhaC, Na+/H+ antiporter NhaC/MleN [Energy production and conversion]
MLAGFNPPVTDKLKSREKPNFYAIVWEALLPILVLIVVLVVGVLLYTGLALHIGLLIGLIVAALLGLRKG
LSWKEIEEGIIEGIKSMLPAILILLLAGALIGVWIALGTVPYLIYYGLGLLSPSLFPAAAFLLCAIISFA
TGTSWGTFGTLGPALMGIAAALGIPLAITAGAVLSGAVFGDKCSPISDTTILSSAGAGCDLFDHVRTMLP
YALPAAVIALVLYLVLGLGYSGDEQIEEILTALESSFNISPLLLLPPVVVIGLALKKVPAIPAWLILLAL
AFGGILEKTGILEVILEALLKKVKSVGGLILSTVLLAIGVNLLTGDQYLSIILPGRMFKKAYEKRGLAPK
NLSRTLEDSGTVTSPLIPWNTCGAFMAGTLGVSTLEYLPYAFFNWLSPLVTIIYAFTGIGKKLDEEEK
>gnl|CDD|441364 COG1758, RpoZ, DNA-directed RNA polymerase, subunit K/omega [Transcription]. DNA-directed RNA polymerase, subunit K/omega is part of the Pathway/BioSystem: RNA polymerase
MARPTVEDLLEKVDNRYELVLLAAKRARQLAEGAEPLVEPDSDKPVVIALREIAEGKITIEILE
>gnl|CDD|441365 COG1759, PurP, 5-formaminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate synthetase (purine biosynthesis) [Nucleotide transport and metabolism]. 5-formaminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate synthetase (purine biosynthesis) is part of the Pathway/BioSystem: Purine biosynthesis
MISRDEILEILEGYDKDKITIATLGSHSALDILDGAKDEGFRTIAVCQKGREKPYRRFKRVADEFIVVDK
FSDILSEEVQEKLRELNAILVPHRSFVAYVGYDNIENSFKVPIFGNRNLLRWEERRGEKNKLLEKAGIRI
PKKYESPEDIDRPVIVKLPGAKGGRGYFIASSYEEFKEKSEELIKQGVIDEEDLKNASIEEYVIGVHFNF
NYFYSPLEGRVELLGIDRRYESNIDGLVRLPAKQQLELNIDPSYTVVGNIPAVLRESLLEKVFEMGEKFV
EAAKKLVPPGIIGPFCLQSVVTKDLEFVVFEVSARIGGGTNVYMGVGSPYSKLYWGEPMSMGRRIAREIK
EAIEKDRLEKIVT
>gnl|CDD|441366 COG1760, SdaA, L-serine deaminase [Amino acid transport and metabolism]
AAELLEYCEEEGLSIFDIIGENEMALRPEEEIRAGLDRIWDVMKECVEIGPSTSSHTAGALRIGRRARKL
LRYGEKPLPGDVLDWVNIYALASFEENAAGGGTVTAPTAGALGVIPAVLLYYQEFLGADDERIRDALLTA
AAIGILIKFTASISGAEGGCQAEVGSASAMAAASLVELLGGGPIQIENAAEIALEHILGLTCDPVGGLVQ
IPCIERNALAAVKAINIARMALARDGLMVIELDEVIEAMRETGRDMPEKLKETSLGGLAVTYIVE
>gnl|CDD|441367 COG1761, RPB11, DNA-directed RNA polymerase, subunit L/RPAC2 [Transcription]. DNA-directed RNA polymerase, subunit L/RPAC2 is part of the Pathway/BioSystem: RNA polymerase
MELKIIKKTDNELEIEIEGEDHTLLNLLKEELLKDPGVDFATYDIKHPLISEPVLRIKTDGGIDPLEALK
EAAKRIIEECDEFKKEFE
>gnl|CDD|441368 COG1762, PtsN, Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate transport and metabolism, Signal transduction mechanisms]
MMLSDLLTPELILLDLEASSKEEAIEELAELLAEKGYVLDKEEYLEALLEREELGSTGIGPGIAIPHARP
EGVKKPGIAVARLKEPVDFGAMDGEPVDLVFLLAAPEDDSEEHLKLLAELARLLSDEEFREKLLNAKSPE
EILELLKEAE
>gnl|CDD|441369 COG1763, MobB, Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]. Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
MPVLGIVGYSGSGKTTLLEKLIPELKARGLRVGTIKHAHHDFDIDTPGKDSYRHREAGADEVLVASPERW
ALMTELPEEPSLDELLARLDDVDLVLVEGFKHEPLPKIEVHRAEEGKPLLYPEDPNIIAVASDAPLPTGL
PVFDLNDPEAIADFILEWLKRK
>gnl|CDD|441370 COG1764, OsmC, Organic hydroperoxide reductase OsmC/OhrA [Defense mechanisms]
MKRLYTATATWTGNRGDGTVSSEDGGLDLPLSSPPEFGGDGTGTNPEELLAAAYAACFMLALLAVAAQAG
VTVESYEVTAEVTLGKDDDGGFAFTGITLRLRVTVPGLDREKAEELVEKAHEVCPISNALRGNITVELTL
>gnl|CDD|441371 COG1765, YhfA, Uncharacterized OsmC-related protein [General function prediction only]
TRWEGGFRAEVETRGHTVVIDEPPELGGTDTGPSPVELLLAALAGCTAITVRMIAKKKGIDLEGLEVEVE
GDRDEEPKGFTKIRVTITVDGDLSEEQLERLLELAEKYCPVSDTLRNGVEITTELE
>gnl|CDD|441372 COG1766, FliF, Flagellar biosynthesis/type III secretory pathway M-ring protein FliF/YscJ [Cell motility, Intracellular trafficking, secretion, and vesicular transport]
MAEALKEILQQLLEFLAKLGARRKIALLGAAAAVVALLVALVLWASRPDYRPLYSNLSDKDAGAIVEALD
QAGIPYKLSDDGGAILVPADQVHEARLKLAAQGLPKGGGVGYELFDKNQGFGTTQFMENVNYQRALEGEL
ARTIESLDGVESARVHLALPKRSVFVREQQPPSASVVLTLRPGRALSPEQVAAIVHLVASSVPGLKPENV
TVVDQNGRLLSSGDDDDSGLALAATQLEYKRRVEQRLRRRIESLLEPIVGPGNVRVQVTADLDFDRVEQT
EETYDPDSGVVRSEQTSEESSTGSGAGAGGVPGALSNQPPAPAAAGAGAGSSSSSSRTEETRNYEVDRTV
RHTVQPPGRIKRLSVAVVVDGKYTTDADGKVTYVPLSAEELAQIEALVRSAVGFDAARGDSVTVVNMPFA
GPEELELPELPFWEQPWFLEDLMTLIKYLLLALVALLLLLFVVRPLLRRLLRPEEEAAAAAADALELPDE
AVALSEEEIAGEEDLPDEGREYEDLLKRLRELAEEDPEEVAQVLRSWLAEE
>gnl|CDD|441373 COG1767, CitG, Triphosphoribosyl-dephospho-CoA synthetase [Coenzyme transport and metabolism]
MTTSLAERIARAAQLALLLEVSLTPKPGLVDRRDDGHDMDFETFLASAAALAPYFERAAEAGAAGALLGR
LPLGIAAERAMLAARATGGVNTHLGAIFLLGPLAAAAGRLLARSLTAEALREGVAEVLAGLTVDDAAAFY
RAIRLANPGGLGADELDVRRGLTLGEAMRLAYGRDGIAGEAASGFPTVFELALPALRRALARGGDLEDAL
LQALLALLAEVPDTNILRRGGLEGAEEVQQRAREVLAAGGVATPAGLEALEELDAELIARNLNPGGSADL
LAATLFLALLEGLEA
>gnl|CDD|441374 COG1768, DR1119, Predicted phosphohydrolase, DR1119 family, metallophosphatase superfamily [General function prediction only]
MRIYAIGDLHLSFAPDKPMDVFGERWENHPEKIAENWRETVGPDDTVLIPGDISWAMKLEEALPDLDWID
ALPGRKVLIKGNHDYWWSSISKLRKLLPPSLHFLQNNAFVYGDVAICGTRGWICPGDDEFTEHDEKIYER
ELGRLELSLEAAKKLGGKKIIVMLHYPPFNDKGEPSEFTELLEEYGVDKCVYGHLHGEGHKNALEGEING
IRYHLVSADYLDFKPLKILD
>gnl|CDD|441375 COG1769, Cmr3, CRISPR-Cas system type III CMR-effector complex subunit Cmr3, RAMP superfamily Cas5 group [Defense mechanisms]. CRISPR-Cas system type III CMR-effector complex subunit Cmr3, RAMP superfamily Cas5 group is part of the Pathway/BioSystem: CRISPR-Cas system
MMWLLLEPLDVLFFRDGRPFSAGGGAWAESLFPPPPSTLAGALRSALLSALGVDFADFAPEELKALLGTP
DELGALRLRGPFLARRDGGGGELLFPAPADLVVKKEDKSELVRLRPLDEPECDLGSVDLPELLALKPAEK
AKPVGGGWLTAEGLLAYLQGELPSPEDLVKASDLWKTEPRVGIAIDPGTRTAKEGMLYQTEGLRLRDGVG
LAVEVEGPDDSLPKPGLLRLGGEGRLARVEELEELFELPEPPEALIIAKGRRFRLYLLTPAIFERGWRPG
GLDEDLRLNGVRVRLVAAAVGRPLPISGWDLARKRPKPLRRAVPAGSVYFFELLEGDAEALLEKLHGGSI
SDEEQDRREGFGLALIGVWND
>gnl|CDD|441376 COG1770, PtrB, Protease II [Amino acid transport and metabolism]
MTRAAAAAPTPPVAKKRPHTRTHHGDTRVDDYAWLRDREDPEVLAYLEAENAYTEAVMAPTKPLQETLFA
EMKGRIKEDDSSVPYRDGGYWYYSRTEEGKQYPIYCRKPASGAGEEVLLDGNALAEGHDFFSLGGLSVSP
DGRLLAYSVDTVGSERYTLRIKDLETGEDLPDVIENTSGGLVWAADNRTLFYTRVDETLRPYQVWRHRLG
TDPAEDVLVYEEKDERFFVGVGKTRSGRYIVIGSGSTTTSEVRLLDADDPTAEPRLVAPREEGVEYSVEH
AGDRFYILTNDDAPNFKLVRAPVDAPSRENWQELIPHRPGVLLEGVDAFKDHLVVSERENGLPRIRVRDL
DDGEEHEIAFDEEAYTAGLGGNPEFDTDTLRYSYSSLTTPSSVYDYDLATGERTLLKQQEVPGGFDPADY
VSERLWATARDGTKVPVSLVYRKDTKLDGSAPLLLYGYGSYGISIDPSFSTSRLSLLDRGFVYAIAHIRG
GGELGRRWYEDGKLLKKKNTFTDFIACAEHLIAQGYTSPGRIVAMGGSAGGLLMGAVANMAPELFAGVIA
QVPFVDVLTTMLDPSLPLTTGEWDEWGNPLNDKEAYDYMKSYSPYDNVKAQAYPAILVTTGLNDSRVQYW
EPAKWVAKLRELKTDDNPLLLKTNMDAGHGGASGRFDALKEVALEYAFLLDLLGIA
>gnl|CDD|441377 COG1771, COG1771, Uncharacterized conserved protein, contains N-terminal Zn-finger domain [Function unknown]
MDESELIARSNKFLDDIKRDKPKLDDLKSFDSVIKIYFTLNSNLEILEDLKEKMELRGFDTPYRSVGKYK
EIDSEDLYEIDRHAQYFRRKASEKKNILERVKSAIASHKIALGHLEEYYELKCGRKEIKVKELKDGSSKV
KAIVNESGIGRLEIIPYLPYSGDYLVLLSQLSPWVREAFKKILNILREEKRGVVKSITLRLEVFENGKWK
FKRIKIDDDSDYEGELRKRYGKAVRIESLQFHKTKNKLINDHYVRDNLALAYLSLYEDKPIKLLLWDIFR
YYLLTSEDRRERSGPFPSIRPTLDRNHLKWFDVPFRDVVELLDLNEKIFKIGNGSELLIRKFELEKKLKK
LNIKLNPYALGGVILYLISDWDEEKVAEIFGIDKKEVEEALKKIAIIGILKDKFVEIKKFEKFGKPKSDK
AKKFLELLKG
>gnl|CDD|441378 COG1772, COG1772, Uncharacterized conserved protein, DUF531 domain [Function unknown]
MLTLGLYNTYDPIKVHEAHYRAIARAAPICYAFGFHLALFGFPFDMTPKELVEYVADKTTIGESGKYLRE
LAEKGRFHLFDLPKKGFPPQFGEVVATTSKPDEKKAITPEDVAEMILRGKSFLLLIGLGRKGLPKEVFKI
AKYHLDITGGGVSLETCTAIGAIPAAIAGLVEG
>gnl|CDD|441379 COG1773, NorV, Flavorubredoxin [Inorganic ion transport and metabolism]
MKKYQCKVCGYVYDPAEGDPENGIPPGTPFEDLPDDWVCPVCGAGKEDFEPVE
>gnl|CDD|441380 COG1774, YaaT, Cell fate regulator YaaT, PSP1 superfamily (controls sporulation, competence, biofilm development) [Signal transduction mechanisms]
MPEVVGVRFKKAGKIYYFDPGDLELKVGDKVIVETERGLEIGEVVLTPREVREEEVVEPLKKVLRKATEE
DLEKYEENREREKEAFEICREKIKEHGLDMKLVDVEYTFDGSKLIFYFTAEGRVDFRELVKDLAREFRTR
IELRQIGVRDEAKMLGGIGPCGRELCCSTFLTDFEPVSIKMAKEQNLSLNPTKISGQCGRLMCCLNYEHD
TYEEALKDLPKVGSKVETPEGEGKVVKVDILKETVTVRLEDGGEVEVPLEEVKEIKKAK
>gnl|CDD|441381 COG1775, HgdB, Benzoyl-CoA reductase/2-hydroxyglutaryl-CoA dehydratase subunit, BcrC/BadD/HgdB [Amino acid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]
MSDEKKIMKYFKVLKELAAKYYEELKEAKEEGKKVVGWFCSYVPEELIHAAGAVPVGLEGGSDEPIEAAE
KGLPRNLCSYIKSSLGFALTGKLPFPDLVVGETTCDGKKKMYELLARDVPVYVMDLPQNKDDEEAVDYWK
EELKELIEFLEELTGRKIDEEKLREAIKLYNEARKLLRELYELRKAKPPPISGFDLLLVMAAAFFMDKEE
ATELLEELLDELEERIAEGIGAVPEEKPRILWTGIPPWPPNRKLLKLIEEAGAVVVADDYCTGSRYFETD
VDEPEDPLEALARRYLSNIPCSCNTPNERRLELLLKLAKEYKADGVIYHSLKFCKPYSVEYPLLKKALEE
AGIPVLSLETDYSDSDEGQLRTRIEAFLEMLGER
>gnl|CDD|441382 COG1776, CheC, Phosphoaspartate phosphatase CheC, specific for CheY-P [Signal transduction mechanisms]
LSEEELDALREIGNIGAGNAATALSTLLGKKVDLSVPRVEIVPIEELPEELGDPEEPVVGVVQEFTGGIS
GEALLLFPEESAKKLADLLLGGDGDSDELDEMELSALSEIGNILTGSFLTALANLLGLTIDISPPELAVD
MAGAILSSLLAELGQEDDYALVIETEFTIEDLEIDGHLLLLPDPESLEKLLEALGVLLE
>gnl|CDD|441383 COG1777, COG1777, Predicted transcriptional regulator, ArsR family [Transcription]
MSDDEDLDRLLDALGNPTRRRILALLSEEPAYVSELARELGVSRQAVYKHLRKLEEAGLVESYREGREDG
RARKYYRLSAFRLEVTLTPDLFARLARELEAYRRELSGRLARI
>gnl|CDD|441384 COG1778, KdsC, 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only]
LLERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPAVRRRAE
ELGITHVYQGVKDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTT
KPGGRGAVREVCELILKAQGKWDALLAAYL
>gnl|CDD|441385 COG1779, Zpr1, C4-type Zn-finger protein [General function prediction only]
MEEKEEETEVKCPVCGGKTLKVIWQTYNIPYFGEVLIITGRCSSCGYRFSDVMILEQKEPVRYTLKVEKE
EDLNARVVRSSSGTIRIPELGLEIEPGPASEGFITNVEGVLNRFEEVVETACKWAEDEEEKEKALEILEK
IEEAKDGKRPFTLIIEDPLGNSAIISDKAKKEKLTEEEAEKLKTGMIIIDV
>gnl|CDD|441386 COG1780, NrdI, Flavodoxin NrdI, NrdF-interacting activator of class Ib ribonucleotide reductase [Nucleotide transport and metabolism]
PMLIYYSSLSGNTRRFVEKLGLPAQRIPIRESDPPLEVDEPFVLVTPTYGGGGGRGEVPKQVIRFLNDPD
NRKLLRGVIGSGNRNFGDNYCLAGDIIAAKYNVPLLYKFELSGTPEDVERVREGLEEFWKQQSST
>gnl|CDD|441387 COG1781, PyrI, Aspartate carbamoyltransferase, regulatory subunit [Nucleotide transport and metabolism]
MEDKELQVSAIKNGTVIDHIPAGKALKVLKILGLDGTGERVTVGMNVPSKKLGKKDIIKIENRELSDEEL
NKLALIAPNATINIIRDYEVVEKKKVELPEEIEGVLKCPNPNCITNNEPVESRFYVVDKEPLKLRCHYCE
KIFSEDEIAEN
>gnl|CDD|441388 COG1782, COG1782, Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only]
MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERERNNDAFPFDPEELDAVVLTHAHLDHSGLL
PLLVKYGYRGPIYCTPPTRDLMALLLLDSAKIQEEEAEYANKKRYSGHPPVEPLYTEKDVEKALKHFITL
DYGEVTDIAPDIKLTFYNAGHILGSAIVHLHIGDGLHNIVFSGDLGRGKTPLLRPPTPFPRADTLIMEST
YGGRLHPSREEAEEELAKVINETIERGGKVLIPAFAVGRTQEILYVLNELMREGKIPEVPVYLDSPMAIE
ATAIHTAYPEYLDEELRDLIFKGENPFLFENLHYVESVEESKEINDSDEPAIIIATSGMLTGGRILHHLK
HLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETIPVRAEVETIDGFSGHADRNELLNWLRRLKPK
PKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL
>gnl|CDD|441389 COG1783, XtmB, Phage terminase large subunit [Mobilome: prophages, transposons]
MTTLQKEINPKFYPLLWDSKHRYRILKGGRGSGKSSFIALKLILKAMEDPKRNILVIRKVQNSLRDSVYE
QLKWAIERLGLSDYFKITKSPLEITYKPTGSKIIFRGLDDPNLDKIKSITGIAIIWVEEATEFSEESFDQ
LLPTLRGPGLFSEIWFTFNPESPYHWVYKRFFDNEVPPDTLVHHSTYLDNPFLPEQLIREIEDLKETDPD
YYRHIWLGEWVGSEGLVFPNWEVHEFDDEEIPPFDRLYFGLDFGFANDPTALVRCGLDAKDKVLYIFDEY
YYVGLTDDEIAKLLKDFIPGYRKEPIYADSAEPESIAELRRYGFRIRGAKKGPGSVEDGIRKLAQLRKIY
IHPRCPNTIREFRLYSWDTDKTGEVLPEPVDENDHAIDALRYALEDYIRRRGLGFDRA
>gnl|CDD|441390 COG1784, COG1784, TctA family transporter [General function prediction only]
MDPELLLLLLAAVLAGVLLGTISGLVPGLHVNNFALLLAALSPALLGLLPPLLVAVAILAAGVVHTFLDI
VPSLFLGVPDADTALSVLPGHRLVLEGRGREAVRLSALGSALAVVLALPLAVPLTWLLPALYPTLDAYLG
LVLLAVVALLILTERSWRARLGALLVFLLSGILGIFTLDLLPTGPLGAGSVLLPLLSGLFGAPVLLDSLG
GGGEIPPQKDAKIALSRRTILRGAFAGSLAGAIVGWLPGVSAAIAAVLALLFVPGDRGDREFIVATSGVN
TANAVFALFALYAIGRPRSGVMVAISELLGGFDPPSLPLLLAVIALAALLGYLLTIVLGDLYLRVVGRLD
YRKLSIGVLALLVVLVYLFTGPFGLAVLIVATAIGLLPPRLGIRRVHLMGVLILPVILYYL
>gnl|CDD|441391 COG1785, PhoA, Alkaline phosphatase [Inorganic ion transport and metabolism, General function prediction only]. Alkaline phosphatase is part of the Pathway/BioSystem: Folate biosynthesis
MMKKLLLALALLLAAAAAAVAAAAAAKKAKNVILFIGDGMGLSQITAARIYKGGPGEDGRLAFDQFPVTG
LVTTYSADSLVTDSAAAATALATGVKTYNGAIGVDPDGKPLETILELAKAAGKATGIVTTARITHATPAA
FYAHVPSRNNYDEIAEQLLDSGVDVILGGGRRYFLPKGTGGKRKDGRDLIEEAKAKGYTVVTTKEELAAL
DAGGGKLLGLFADSHMPYEIDRDNDFPDEPSLAEMTKKAIDVLSKNPKGFFLMVEGGRIDWAGHANDAAG
AIEETLAFDKAVGVALDFAKKNPDTLVIVTADHETGGLTLGGPILDLVKNYKALDADGVKNGLGDLTYGK
NQRAGVGWTSGGHTGEDVPVYAYGPGAELFSGTIDNTDIFKKMAKALGLKL
>gnl|CDD|441392 COG1786, AcnX2, Mevalonate 5-phosphate dehydratase subunit 2, swiveling domain (modified mevalonate pathway) [Lipid transport and metabolism]
TLKGRKIVGGKAEGEALVSDEPISFLGGVDPKTGVVIDPGHPLYGQSIAGKILVFPTGKGSTVGSYVLYE
LKKNGTAPAAIIFREADPILALGAIVAGIPLVDLFDEDPFEAIKTGDRVRVDADEGTVEVL
>gnl|CDD|441393 COG1787, COG1787, Endonuclease, HJR/Mrr/RecB family [Defense mechanisms]
RKEKRKIRSGLEELDNMDGREFEKYLAKLLRKLGYDVEVTPGSGDFGADLIATKDGERIAVQCKRYKSPV
GNKAVQEVVAAKAYYGADKAVVVTNSYFTKSAKELAKSNGVELIDRDDL
>gnl|CDD|441394 COG1788, AtoD, Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism]
MDKVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVDGLGLLIGAGQVKK
VIASYVGGVGLNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEGKETREIDGE
EYVLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIF
VDAVVEVPGGARDKRI
>gnl|CDD|441395 COG1790, COG1790, Uncharacterized conserved protein, DUF483 domain [Function unknown]
MEAVEELEELLKKIQELREGLSENRNFLGKHIQRLDDFQFNYIISRLDKQIEIVKKYSPKVRPAIDPMVS
TELGVYRGLDDEEVGKLLGYPECCIESFSEDFRFGIDSEHLKEIEEIKIDKNSYAIILPSGFIPCSLKCS
KAIKRGLIGFVSKEEFRKILKLEEELITELPHFHSAYDEYYEKILLKG
>gnl|CDD|441396 COG1791, Adi1, Acireductone dioxygenase (methionine salvage), cupin superfamily [Amino acid transport and metabolism]
MATLRIYPDDGPEQPTTITDLEEIARELAPLGVRFERWDAGQDLLTDAEKEEVLAAYRSEIERLKAERGY
QSVDVISLHPDTPNLDALRAKFLSEHTHTEDEVRFFVAGEGLFGLHLGGKVYEVLCEAGDLISVPAGTEH
WFDMGPSPRFKAIRLFTNPEGWVAHYTGSDIADRFPRLEE
>gnl|CDD|441397 COG1792, MreC, Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]
MKPLFFFRNRLLLLLLLLVLLALALIVLDNRDRLLEPVRQALGDVLSPVQRLASAPVGGVSGVSDNFRSL
FNLREENERLKEENAELRAELQRLEELEAENARLRELLDLKERLDYKFVAAEVIGRSPDPWSNTITIDKG
SNDGVKPGMPVIDAKGLVGQVTEVSPNTSRVLLITDPNSRVPVQVQRTGVRGILSGDGSNGLLELRYLPR
DADVKVGDLVVTSGLGGVFPKGLPVGTVTSVERDPGGLFKTIYVKPAADFDRLEEVLVLKNKPEEEPAPE
EA
>gnl|CDD|441398 COG1793, CDC9, ATP-dependent DNA ligase [Replication, recombination and repair]
EELRRAAFATEAEEATAKRLEAKALLFVIQKHDATRLHYDFRLELDGVLKSWAVPKGPSLDPADKRLYGI
VGDLTWEPEGGLTKGTLFELAGEKLAGRWYLVRLGERVSDWLLVPPMLATLVDSPPDGGDWAYEPKWDGY
RVQAHRDGGEVRLYSRNGEDITDRFPELVEALRALPADDAVLDGEIVALDEDGRPPFQALQQRLGRKRDV
AKLAREVPVVFYAFDLLYLDGEDLRDLPLSERRALLEELLAGAPPPLRLSPHVIDWGEGEALFAAAREAG
LEGVMAKRLDSPYRPGRRSGDWLKVKCPRTQDLVVGGATPGKGRRAGGFGSLLLGVYDPGGELVYVGKVG
TGFTDAELAELTERLRPLTRERSPFAVPSDGRPVRWVRPELVAEVAFDEITRSGALRFPRFLRLREDKPP
EEATLEELEALLAAQ
>gnl|CDD|441399 COG1794, RacX, Amino acid racemase YgeA [Cell wall/membrane/envelope biogenesis]
MMKTIGILGGMGPEATADYYRKINEATPARLDQDHSAEILLNSPDFPDRTAAILAGDWEDPAPLLAEAAR
RLEAAGADFIVIPCNTAHYVADEIQAAVSIPLLHIADATAEAIRARGIKRVGLLGTRGTMESGFYQDRLE
AAGIEVIVPDEEDQELVHRIIYDELKAGIITEESRAALLEIIERLAARGAEAVILGCTELPLLLDQEDSP
VPLIDTTDIHARAAVDLA
>gnl|CDD|441400 COG1795, Fae, Formaldehyde-activating enzyme (5,6,7,8-tetrahydromethanopterin hydrolyase) [Energy production and conversion]
SKIIMMLIGEALVGDGNEVAHIDLIIGPRDGPVGTAFANALANQSAGHTPLLAVLAPNLPVKPATLMVPK
VTIKNAKQANQMFGPAQAAVAKAVADAVAEGVIPKDEADDLVIIVSVFIHPEADDDKKIYRYNYEATKLA
IKRAMAGEPSIDEVLANKDRAKHPFAGFKVG
>gnl|CDD|441401 COG1796, PolX, DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair]
MDNKEIARILEEIADLLELKGENPFKIRAYRRAARAIENLPEDIEELVAEGDLTEIPGIGKAIAAKIEEL
LETGRLEELEELREEVPPGLLELLRIPGLGPKKVKKLYEELGITSLEELEAAAEEGRIRELPGFGEKTEE
NILKGIELLRKRGGRFLLGEALPLAEEILAYLRALPGVERVEVAGSLRRRKETVGDIDILVASDDPEAVM
DAFVKLPEVKEVLAKGDTKASVRLKSGLQVDLRVVPPESFGAALQYFTGSKEHNVALRQLAKERGLKLNE
YGLFDVGGERIAGETEEEVYAALGLPYIPPELREDRGEIEAAEEGRLPELVELDDIRGDLHHHTTWSDGG
ASIEEMAAAAAARGYYYIAITDHSSSLVVAGGLDEERLLQQEEEIDALNERLDGIILLLGGEEDILDDGG
LDDDDDLLLEDDDVVAAVHHSFLLQDEEMTRRRLAAANEPVVVIIHHPTGRLLLRRRPYYVDDEAIIAAA
AAAGALEEENNAPRRLLLLDDLARAAAEGGVVIIIIDDAHHTDLLLDLMGGGVAARRRWWLEKDVNNNTL
LLELLLL
>gnl|CDD|441402 COG1797, CobB, Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]. Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MSIPRLVIAAPHSGSGKTTVTLGLLAALRRRGLKVQPFKVGPDYIDPGYHTLATGRPSRNLDPFLMGEEG
VRELFARGSAGADIAVIEGVMGLYDGLDGDSGSGSTAHLAKLLGAPVVLVVDASGMSRSAAALVLGFRAF
DPDVRIAGVILNRVGSERHEELLREAIEHYTGIPVLGALPRDEELELPSRHLGLVPAAEREELEEALDRL
AELVEEHVDLDALLELARSAPPLPAPPSPLFAPPPGPRVRIAVARDEAFNFYYPENLELLEAAGAELVFF
SPLRDEALPEDVDGLYLGGGFPELFAEELSANRSMRESIREAAEAGMPIYAECGGLMYLCRSITDFEGKG
YPMVGVLPGDAVMTKRLQGLGYREATALGDSPLGPAGERIRGHEFHYSTLTPEGDLRPAYRLRRGRGIDG
GRDGFVYGNVLASYLHLHFASNPEWAERFVAACRAYRRS
>gnl|CDD|441403 COG1798, DPH5, Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]
MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIGTDLEKLEELIGKEIVVLDREDVEDNPEEIL
EEAKEKDVVFLTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAIGLTGLQNYKFGKTVTIPFPYE
GFVPTSPYDTIKENLERGLHTLVLLDIKADKNRYMTANEALELLLEIEKKRREGVISDDTLAVVVARAGS
PDPKIVAGKLSELANYDFGEPPHSLIIPGRLHFMEAEALKALAGA
>gnl|CDD|441404 COG1799, SepF, Cell division protein SepF/YlmF, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning]
MGLFDKLKNFFGLEDEEEYEEYEEPEEEEPAPAKPAKKKANVVPLHSATSSQSKIVVVEPRSYEDAQEIA
DHLRNGKPVIVNLERMDDDQAKRIVDFLSGLVYALDGSIQKVGNKIFLLTPSNVEVSGEIKEELAEKGFF
NW
>gnl|CDD|441405 COG1800, COG1800, Predicted transglutaminase-like protease, UPF0252 family [General function prediction only]
MKKNLSPPISCELCALNESELSTIKKLASQLKGNDSKETIWNILEWEEENIEYDYSKAEVPPSYIQTPSE
TLKKKKGICSDYAVLTAALLLNLNYSPVYILVIEFNSTIGHAAAAVEINGTLFVLDQHLPPIEIGTYIKY
LAKNDLKIIAEITVYRVSKEEGGIFSQLDNVFKYIDLEYIDTYPDIINRIEERLKKDKQLSNVEELEGRI
TKLKFPVYRRYYNPIFHEQYVEYITMIIDEEIRENIKKFSYIEVTKEQEDLIISLY
>gnl|CDD|441406 COG1801, YecE, Sugar isomerase-related protein YecE, UPF0759/DUF72 family [General function prediction only]
MIRIGTSGWSYPDWRGVFYPEGLPAKDELEYYARHFNTVEINSTFYALPSPETVARWAAQTPDGFRFSVK
APRFITHERRLADAEELLERFLESLEPLGDKLGPLLFQLPPSFKFDPERLEAFLALLPRGLRHAVEVRHP
SWFTPEVLALLREHGVALVIADSPRVPPIAVTTADFVYVRLHGRNERYDYGYSPEELDEWAERIRAWAAE
GRDVYVYFNNDAEGHAPANALALAELLGAAG
>gnl|CDD|441407 COG1802, GntR, DNA-binding transcriptional regulator, GntR family [Transcription]
MTSPSPLRRESLAEQVYEALREAILSGELPPGERLSEAELAERLGVSRTPVREALRRLEAEGLVEIRPNR
GARVAPLSPEEIRELYEVRAALEGLAARLAAERATPADLARLRALLEELEAAAAAGDVAAYLELDREFHR
ALVEAAGNPRLAELLRRLRARLRRYRRLSLRSPGRLEESLAEHRAILDALEAGDAEAAAAALRAHLERAR
ERLLEALAAAAA
>gnl|CDD|441408 COG1803, MgsA, Methylglyoxal synthase [Carbohydrate transport and metabolism]
MTIALIAHDNKKDDLVEFAKAHKDILSKHELVATGTTGKLIEEATGLEVTRLLSGPLGGDQQIGALIAEG
EIDAVIFFRDPLTAQPHEPDVKALLRLCDVHNIPLATNLATAELLITSLLRG
>gnl|CDD|441409 COG1804, CaiB, Crotonobetainyl-CoA:carnitine CoA-transferase CaiB and related acyl-CoA transferases [Lipid transport and metabolism]
PAMTGPLAGIRVLDLSRVLAGPFATMLLADLGADVIKVERPGGGDPTRGWGPPFDGESAYFLSLNRNKRS
ITLDLKSPEGRELLRRLVARADVLVENFRPGVLERLGLGYEALRAINPRLIYCSISGFGQTGPYADRPGY
DLIAQAMSGLMSLTGEPDGPPVRVGVSVADIAAGLYAAIGILAALLHRERTGRGQVVDVSLLDAALALLA
NQAAEYLATGEVPERTGNRHPGIAPYGVYRTADGWVAIAAGNDRQWRRLCEALGRPDLADDPRFATNAAR
VANRDELDALLAAWFATRTRAEWLELLEAAGVPAAPVNTLAEVLADPQLAARGMFVEVDHPDGGPVRQPG
PPPRFSGTPGRVRRPAPALGEHTDEVLAELGYSAEEIAALRAAGVIG
>gnl|CDD|441410 COG1805, NqrB, Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrB [Energy production and conversion]. Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrB is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase
MGLRKFLDKIEPHFEKGGKLEKWYPLYEAFDTFLYTPGTVTKGGVHVRDAIDLKRIMITVVLALFPALLF
GMYNVGYQANLALGALGAAPDDWRGALISLLGGHDPASFWDNFLYGALYFLPIYIVSYVVGGFWEVLFAV
VRKHEVNEGFLVTGMLFPLILPPTIPLWQVALGISFGVVIGKEVFGGTGKNFLNPALTGRAFLFFAYPAQ
MSGDKVWVAVDGFSGATPLGQAAAGGLDAVGTGAGYSWMDAFLGFIPGSIGETSTLAILIGAAILIVTGI
ASWRIMLGVFIGMIATSLLFNLIGSDTNPMFAMPWYWHLVLGGFAFGMVFMATDPVSAAMTNKGKWIYGF
LIGFMTVLIRVVNPAYPEGMMLAILFANVFAPLIDHFVVQANIKRRLKRAKV
>gnl|CDD|441411 COG1806, PpsR, Regulator of PEP synthase PpsR, kinase-PPPase family (combines ADP:protein kinase and phosphorylase activities) [Signal transduction mechanisms]
MMKKRTVFLVSDSTGETAETVARAALSQFPGVEFEIHRFPFVRTEEKADEVLEEINEAPPIVFYTLVDPE
LREILEEFCRELGIPCVDLLGPFLDALESELGVKPSREPGLQHGLDEEYFKRIEAIEFALAHDDGQDPRG
LDEADVILVGVSRTSKTPTSMYLANQGIKVANYPLVPEVPLPEELFEVDRKKIVGLTIDPERLNQIRRER
LKSLGLRPNSRYASLERIREELEYAERLFRRLGCPVIDVTNKSIEETAAEILQLLGLRRRSY
>gnl|CDD|441412 COG1807, ArnT, PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA [Cell wall/membrane/envelope biogenesis]
MSKTLSARPLLLLLLLALLLRLLGLGSLPLWDPDEARYAEIAREMLESGDWLTPTLAGEPYFDKPPLIYW
LIALSYKLFGVSEFAARLPSALLGLLTVLLVYLLARRLFGRRAALLAALLLLTSPLLLLFGRLATPDALL
LLFWTLALYALLRALERRRLRWLLLAGLALGLGFLTKGPVALLLPGLALLLYLLLTRRWRRLRRLRLLLG
LLLALLLALPWYIANDWATGPAFLEYFFGYENLVPLLFFSLSATKLPRYLLPLLPALALLAAAGLARLRR
RRRALLLLALVLLLALLIALLLALAALAL
>gnl|CDD|441413 COG1808, AF0785, Uncharacterized membrane protein AF0785, contains DUF389 domain [Function unknown]
DLSEDRISREELYERAEEESRLSGTYLVLLVLSTIIATIGLLLNSPAVIIGAMVIAPLMGPILALALGLV
LGDRELLRRSLKTLLVGLLLAIAVAALLALLLPLTEATSEILARTSPTLLDLLVALAAGAAGALALTRGK
SSALVGVAIAVALVPPLATAGIGLAWGNWDLALGALLLFLVNLVGINLAALLVFLLLGYRPRRWREKKRA
R
>gnl|CDD|441414 COG1809, ComA, Phosphosulfolactate synthase, CoM biosynthesis protein A [Coenzyme transport and metabolism]
MNFLLFPLPERTEKPRKTGLTMVIDKGLGLRETEDLLEVAGPYIDFVKLGFGTSALYPNDVLEEKIKLYR
SAGIPVYPGGTLFEAAVLQGKFDEYLRLAKKLGFTAVEVSDGTIDLSHEEKCEIIRKAAKLGFTVLSEVG
KKDPDKILSPYKWIELIKEDLEAGAWKVIVEARESGTNVGIYDEDGEVREGLVEEILSKIPPEKIIWEAP
QKKQQVWLIKLFGPNVNLGNIAPNEVIALETLRLGLRGDTFRLFLPDETGA
>gnl|CDD|441415 COG1810, COG1810, Uncharacterized conserved protein, DUF166 domain [Function unknown]
MKIGVIYSGKYGERLIGNLLNYSFSDFIVGVIELPEPLPEFIDEPEEYLPDEIPEADIIIAYGLHPDLTY
ELPEIAAEAGVKAVIVPGEDPKWAGPGLKKQLEEICEEYGIEIEFPKPFCALEENGDPVIDEFLSKFGKP
ELEIEVENGKIKDVDVLRSAPCGSTWFVAKKLKGKDIEEAPEKAGLAHHSYPCRASMERDFELGDTILHK
AGYIHKEAVEKALKKEKEEN
>gnl|CDD|441416 COG1811, YqgA, Uncharacterized membrane protein YqgA, affects biofilm formation [Function unknown]
MMLGTIVNVAAIILGGLLGLLLGKRLPERLKETVMQGLGLAVLLIGIQMALKTKNILIVILSLVLGGIIG
ELLDIEKRLERLGEWLERKFGRGGEGSFAEGFVTASLLFCVGAMAIVGALQDGLTGDHSILFTKSILDGF
TAIIFASTLGIGVAFSAIPVLLYQGSLTLLAGLISPLLTPAMIAELTAVGGLLILAIGLNLLGIKKIKVA
NLLPALFIAPLLSLLWSLL
>gnl|CDD|441417 COG1812, MetK2, Archaeal S-adenosylmethionine synthetase [Coenzyme transport and metabolism]. Archaeal S-adenosylmethionine synthetase is part of the Pathway/BioSystem: Methionine biosynthesis
MRNIVVEELNQTPVEDQEVEIVERKGIGHPDSICDGIAEAVSRALSKEYLERFGTILHHNTDKTLLVAGQ
SAPKFGGGEVIEPIYILLVGRATTEVKGEKIPVEEIALEAAKEWLRENLRFLDPERHVIVDVKIGEGSAD
LVDVFERGKKVPLANDTSFGVGYAPLSETERIVLETERYLNSKEFKKKYPEVGEDIKVMGLREGDKITLT
VACAMVDRYVSDLDEYIAVKEEVKEEVLDLASKYTDRDVEVHVNTADDPERGSVYLTVTGTSAEMGDDGS
VGRGNRVNGLITPNRPMSMEATAGKNPVNHVGKIYNLLSNEIAERIVKEVDGVREVYVRLLSQIGKPIDE
PLVASVQVITEDGVDLSDVKSEVEEIIDEELANITKITERLIEGKISTF
>gnl|CDD|441418 COG1813, aMBF1, Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and HTH domains [Translation, ribosomal structure and biogenesis]
MAKESTGELVEDYGERIREAREARGLSQEELAEKLGVSESTIRRIERGEATPSLDTLRKLEKALGISLAE
>gnl|CDD|441419 COG1814, Ccc1, Predicted Fe2+/Mn2+ transporter, VIT1/CCC1 family [Inorganic ion transport and metabolism]
EERHRSERSGWLRAAVLGANDGLVSTAALVAGVAGAGASPSAILLAGLAGLVAGALSMAAGEYVSVSSQR
DTEEAELARERRELAEDPEGEREELAEIYRARGLSPELAEQVAEELTAHDAAWLDAHAREELGIDEEELA
SPWQAALASFLAFAVGALLPLLPYLLAPGAAALPVSAVLTLLALALTGALKARLGGASPLRAALRTLLIG
ALAAAVTYLVGLLFGVAVG
>gnl|CDD|441420 COG1815, FlgB, Flagellar basal body rod protein FlgB [Cell motility]
MSILFDKTFGLLEKALDLRSLRQEVIASNIANADTPGYKARDVDFEAALKAALGGGSAGLALATTNPRHI
PGSAGSSVSPEVLYRTPTQPSLDGNTVDLDEEMAKLAENALQYQAALTFLNKKFSMLKTAIKGGR
>gnl|CDD|441421 COG1816, Add, Adenosine deaminase [Nucleotide transport and metabolism]. Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRAAYDFRDLQSFLDTYDAGAAVLQTEEDFRRLA
YEYLEDAAADGVRYAEIRFDPQLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFE
TLELALRYRDRGVVGFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIG
HGVRAIEDPALVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDE
YELAAEAFGLSDADLAQLARNAIEASFLPEEEKAALLAELDAYFAA
>gnl|CDD|441422 COG1817, COG1817, Predicted glycosyltransferase [General function prediction only]
MKILFDINHPAHVHFFKNAIRELEERGHEVLVTAREKDVTTDLLDAYGIDYEVLGKHGDSLYSKLLELIE
RELRLLRLARRFDPDVLVGIGSPYAAHVAFLLGIPSIVFYDTEHAKLVNRLTLPFADVILTPSVFPKDLG
DKHVRYNGYHELAYLHPDRFKPDPSVLKELGLDPDEPYIVVRFVAWKASHDVGKKGFSDEILRELIEELE
EYGTVFISSEGELPAELEKYRIPVPPADIHDLLAYADLFIGDGGTMATEAALLGTPAIRVNSFVMGYFDE
LEIKYGLVYNFTDEEEALEKAEELLSDPNLKERWQKRRERLLKDKIDVTDFIVDFIENYPES
>gnl|CDD|441423 COG1818, Tan1, tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure and biogenesis]. tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain is part of the Pathway/BioSystem: tRNA modification
MNLIVTTPRGRERDAIEELRDILEEGDPNAEVVPTGFSGVLLVKTSLDPYEAVEKLKEEPWEPRYILRVI
PVDRVVKTDLEEIVEAAKELAKKKIPEGETFAVRCEKRGKSKLSSREVIRAIGEAIKRGAKVDLENPDWV
VLVEILGDKAGISVLKPEDIFS
>gnl|CDD|441424 COG1819, YjiC, UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]
RILFVTLGGRGHVNPLLALARALRARGHEVTFATGPDFADLVEAAGLEFVDWRPDLVVSDPLALAAALAA
EALGIPVVSLTPPELEYPRPPDPANVRFVGPLLPDGPAELPPWLEEDAGRPLVYVTLGTSANDRADLLRA
VLEALADLGVRVVVTTGGLDPAELGPLPDNVRVVDYVPQDALLPRADAVVHHGGAGTTAEALRAGVPQVV
VPFGGDQPLNAARVERLGAGLALPPRRLTAEALRAALRRLLADPSYRERAARLAAEIR
>gnl|CDD|441425 COG1820, NagA, N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]
AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEPDAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPE
ALRTIARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGGAGILGIHLEGPFLSPEKKGAHPPEY
IRPPDPEELDRLLEAAGGLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVT
HLFNAMSPLHHREPGVVGAALDDDDVYAELIADGIHVHPAAVRLALRAKGPDRLILVTDAMAAAGLPDGE
YELGGLEVTVKDGVARLADGTLAGSTLTMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAP
GKDADLVVLDDDLNVRATWVGGE
>gnl|CDD|441426 COG1821, MfnD, Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme transport and metabolism]
MKILVFEYITGGGLADEPLPPSLLAEGRAMLDALLADLARLPGVEVVTTRDARLAPPALPRTSVPVRSGE
DFSALWRRLAAEADAVLVIAPETDGILARLTRIVEAAGKRNLGSSPEAIALAADKLLTAELLAAAGIPTP
PTFPADDAPPLLAGPWVVKPDDGAGSEGTRLFDDPAALRAREARGAGLIVQPYIEGEAASLSLLCGRGGA
LLLSINRQRIEVDGGRFSYLGGTVPAEHPRKEELQALAQKVAEALPGLRGYVGVDLILTADGPVVVEVNP
RLTTSYVGLRAALGENLAALLLDLLAGGLPPERQPVEVHLEGE
>gnl|CDD|441427 COG1822, MJ0419, Uncharacterized membrane protein MJ0419, predicted role in archaeal polysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis]
VIRFILMSIISAFLVFIITASIFIFFIIFMQLLILNDELGIEEKELKSRIKKLFPGFNSFDSISISFVLF
IIGIIFQILNLIWVGGIPLFNPSLRYFLNVKFTILSYLLFLGSANILSSSKYDRKRYIIYSIIGFVLLVL
LGYRTPVIALLLSVLITLYYSKKISVKEVLLLALLLFIILLGMGYVRLYSEWQGWTLNPIELLLYRAGFT
MSVLDKIVYNFNGVTHGKLHYSALPGSSPGPRAIIGKLTLGRYGVSITPTIFGPVLLDFGILGVLFQMFI
LGFLLGIGYKIQKKLKGIYLGLYSILLAYCLIGIETGILDLLVILYYFISILICIYVILLNKKR
>gnl|CDD|441428 COG1823, TcyP, L-cystine transporter TcyP, sodium:dicarboxylate symporter family [Amino acid transport and metabolism]
MMNLLVIINLAIFLALIGLLYRMQKKHVSFSKRVFTGLGLGILFGLILQLIYGAGSPVIKQSIDWFNIVG
NGYVRLLQMIVMPLVFVSILSAITKLKNASSLGKISGLIIGILLGTTAIAALVGILVALLFGLTAEGLTQ
GAAETARGEALEERLGEVEDLSLPQQILSFIPTNPFADLTGARPTSTIAVVIFAAFLGIAALGLRRKKPE
QAETFLKGIDALQAIVMRLVRLVLRLTPYGVLALMTKVVATSDFADILNLGKFVVASYVALIIMFIVHLL
LLALAGLNPLTYFKKVWPVLTFAFTSRSSAGTIPLNIETQTKRLGVPEGIANFAASFGATIGQNGCAGIY
PAMLAVMIAPTVGINPLDPSFILTLIAVVTISSFGVAGVGGGATFAALIVLSAMGLPVALAGLLISIEPL
IDMGRTALNVSGSMTAGTVTSRLLGQLDKDIYNSDEEVELEEA
>gnl|CDD|441429 COG1824, MgtE2, Permease, similar to cation transporters [Inorganic ion transport and metabolism]
MTVRWTVRRIVRESLPVLLVLAVGGIIAGLVLEGMEELLLAYPGLLVLVPAFLGTRGNLGGILGARLSTA
LHLGLLEPRLRPDRRLLNNILATLILALLISPLIGVLAWLVAVLLGRGSLGLLTLVGIALLAGLLLALLL
IVVTYYVAIASYRFGLDPDNVVIPVVTTLGDVFGVLFLILVARLVLGL
>gnl|CDD|441430 COG1825, RplY, Ribosomal protein L25 (general stress protein Ctc) [Translation, ribosomal structure and biogenesis]. Ribosomal protein L25 (general stress protein Ctc) is part of the Pathway/BioSystem: Ribosome 50S subunit
MESITLKAEKREETGKGAARRLRREGKVPAVIYGGGKEPVSISVDAKELRKLLRKEGENTLITLDIDGKK
EKVLIKDVQRHPVKDEILHVDFLRVSAGEKVTVEVPVHFVGEAAGVKVGGGLVLTLHELEVEALPPDIPE
PIEVDVSDLGLGDSISVHDLDLPLLVGVVEDPDVVVVVVVTP
>gnl|CDD|441431 COG1826, TatA, Twin-arginine protein secretion pathway components TatA and TatB [Intracellular trafficking, secretion, and vesicular transport]
MFGIGFWELLIILVVALLVFGPKKLPELARSLGKAIREFKKAANEVKEELDEELKEEELRKSEKEAEELK
KA
>gnl|CDD|441432 COG1827, NiaR, Transcriptional regulator of NAD metabolism, contains HTH and 3H domains [Transcription, Coenzyme transport and metabolism]
MDGEERREKILEILKESKEPISGSELAKKFGVSRQVIVQDIALLRAKGEPIIATPRGYILLKAESSKGFT
RVIACKHTPEEIEEELNTIVDNGGTVLDVIVEHPVYGEITGSLMISSRRDVDKFLKKLKESKAEPLSSLT
GGVHLHTIEADSEETLDRIEEALKEKGFLIE
>gnl|CDD|441433 COG1828, PurS, Phosphoribosylformylglycinamidine (FGAM) synthase, PurS subunit [Nucleotide transport and metabolism]. Phosphoribosylformylglycinamidine (FGAM) synthase, PurS subunit is part of the Pathway/BioSystem: Purine biosynthesis
MFKARVEVTLKPGVLDPQGEAIKRALKRLGYEGVEDVRIGKYIELELDAEDEEEAEEEVEEICEKLLANP
VIEDYEIELEEA
>gnl|CDD|441434 COG1829, COG1829, Archaeal pantoate kinase [Coenzyme transport and metabolism]. Archaeal pantoate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
ARAFVPGHITGFFSPHIGEDPLKTGSRGAGLALSPGVTTTVSEAEGSETKITLNGEPVDIPVSERVLEKL
GDRPVRVEHESPLPLGYGFGVSGAGALGTALALNRALGLGLSSNEAAQIAHEAEVEAGTGLGDVVAQAHG
GVVIRLKPGAPGIGRVDRIPVRDIRVIVVVLGELSTKEVLSDDTRRINAAGEKALERLLEEPTLETFMEL
SRRFAREAGLLSPEVREAIEALEAAGGGASMAMLGETVFALVEEEEVEEAVEGLSDAGYDVIVCRIDPAG
ARLLR
>gnl|CDD|441435 COG1830, FbaB, Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]. Fructose-bisphosphate aldolase class Ia, DhnA family is part of the Pathway/BioSystem: Glycolysis
DMGKKIRLSRIFNAGTGRLVIVAVDHGVEHGPNPGLEDPEEIVRLAAEGGADAVALTKGILERLARKYAR
DIPLILKLNGSTSLGYPDPNDKVLVGSVEDAVRLGADAVGVTIYVGSEYEAEMLEELARVVEEAHRYGLP
VLAWPYPRGPAVKDETDPDLVAHAARIAAELGADIVKTKYPGDPESFREVVAACPVPVVIAGGPKTPDDE
DFLEMVRDAIDAGAAGVAVGRNIFQRPNPEAMLRAISAIVHEGASVEEA
>gnl|CDD|441436 COG1831, COG1831, Predicted metal-dependent hydrolase, urease superfamily [General function prediction only]
MKELDLPILDNHLHLDPVKGLGLEAVKDFRRAGGTHIALVNKPSWHYGIEPTDGEDYRKVFEITVREAEK
ARETGVKAWPVLGVHPAEIDRLVDRGMSPEEALELMKKGLDLAAEYVKEGKAVGIGEVGRPHYDVSPEVW
EASNEVLRHALELAKDLDCAVQLHTESAGEETVTDIAELAEKVGLPPERVVKHHAPPRVAEAEELGLFPS
VPAKKEALEEAAEQGPRFLMESDYIDDPKRPGAVLGPKTVPRRTRWLLEEGLIDEEAVYKIHVENPEKVY
GVEPE
>gnl|CDD|441437 COG1832, YccU, Predicted CoA-binding protein [General function prediction only]
MDNPDDEEIREILKSAKTIAVVGLSPNPERPSYYVAKYLQRHGYRVIPVNPGAKEILGEKVYASLADIPE
PVDIVDVFRRSEAVPEIVDEAIAIGAKVVWLQLGVVNEEAAERAEAAGLDVVMDRCPKIEHARLGGGL
>gnl|CDD|441438 COG1833, COG1833, Uri superfamily endonuclease [General function prediction only]
MKLPADKGTYVLVLKLDEPLTITVGALGEFEFPAGYYAYVGSALGPGLRARVERHLRKEKKLHWHIDYLL
GHAEVELLGVVVIPSDERLECALARALSELPEIPVPGFGASDCKCPSHLFYFPDNPELLEAVRAAFEELG
LE
>gnl|CDD|441439 COG1834, DdaH, N-Dimethylarginine dimethylaminohydrolase [Amino acid transport and metabolism]
RVLMCRPDHFGVEYAINWMDPLREWAGPPPDAERAVAQWDALVDALEALGVEVHRLPPVPGLPDMVFTRD
AGLVIGDGAILARMRHPERRGEEAAYREWLEELGIPVVRLPEPGVFEGGDVLLDGDTLLVGYGFRTNRAG
IEWLARLLGYEVVPLELVDPRFLHLDTAFCPLAPGLALVYPEAFDPESLALLKEPGWDLIEVPEEEAAWL
GCNVLSLGGRRVVSPAGNPRLNAALRAAGFEVIEVDLSEFLKGGGGFHCLTLPL
>gnl|CDD|441440 COG1835, OafA, Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains [Cell wall/membrane/envelope biogenesis]
ASSSRRRLPSLDGLRGLAALLVVLYHAFLLFPPGPLGGLLSGGFLGVDVFFVLSGFLITRSLLRRLERGG
FSLRRFYLRRFLRIYPAYLVVLLLTGHLWSLSVELQFYLLFPLLLLLLRRLRRRLLALLALLALASLLLL
ALLLTGDPSAAYFLTLTRLWEFLLGALLALLYRRLRRLRRLLALAGLALLLAALLLLDGAPFPGFGLLPL
LAALLVLAAAAGSGLLSRLLSSRPLVFLGDISYSLYLWHWPVLVLLLALLGRLLGPAPLLLLLLALALSL
ALAALSYRLVERPARRLKRRLARRARAAA
>gnl|CDD|441441 COG1836, COG1836, Cytidylyltransferase family enzyme [General function prediction only]
AVLLNPLLLALALSLLLGYLAYRKKLLTLSGALAAVLLGTLIIGLGGWGWFLLLLLFFILGSLLTKYGYK
RKEALGIAEEKGGARGAGNVLANGGVALLAALLYAATPDDSPLFLLAFAGSLATALADTWASEIGVLSGK
RPRLITTLKPVPPGTSGGVSLLGTLAGLLGALLIALLAWLLGLIDSLLGLLIVVLAGFLGTLVDSLLGAT
LQNKYGWLTNDGVNFLATLIGALLAALLALLLG
>gnl|CDD|441442 COG1837, YlqC, Predicted RNA-binding protein YlqC, contains KH domain, UPF0109 family [General function prediction only]
MKELVEFLVKPLVDHPDDVSVTEEEGERTVVLELRVAPEDLGKVIGKQGRTAKAIRTVLSAAAAKEGKRV
RLEIVD
>gnl|CDD|441443 COG1838, FumA, Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain [Energy production and conversion]. Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain is part of the Pathway/BioSystem: TCA cycle
MATIRLNTPLTEEDVRKLKAGDRVLLSGTIYTARDAAHKRLVELLDRGEPLPVDLKGQVIYYVGPAPAKP
GYVIGSAGPTTSTRMDKYTPELLEELGLKGMIGKGGRSPEVIEAMKKHGAVYLAAVGGAAALLAKAIKKV
EVVAYEDLGPEAIWKLEVEDFPLIVAIDSKGNSLYEQGRAKARARLAALE
>gnl|CDD|441444 COG1839, COG1839, Adenosine/AMP kinase [Nucleotide transport and metabolism]
MELEVVDIEKPEGVNVILGQSHFIKTVEDLYEALVTSVPGIKFGLAFCEASGPRLVRYEGNDEELIELAV
KNALAIGAGHSFVIFLRNAYPINVLNAIKNVPEVCRIFCATANPLEVIVAETEQGRGILGVVDGFSPKGV
ETEEDIKERKEFLRKIGYKL
>gnl|CDD|441445 COG1840, AfuA, ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]
LLEAFEKKTGIKVNVVRGGSGELLARLKAEGGNPPADVVWSGDADALEQLANEGLLQPYKSPELDAIPAE
FRDPDGYWFGFSVRARVIVYNTDLLKELGVPKSWEDLLDPEYKGKIAMADPSSSGTGYLLVAALLQAFGE
EKGWEWLKGLAANGARVTGSSSAVAKAVASGEVAIGIVNSYYALRAKAKGAPVEVVFPEDGTLVNPSGAA
ILKGAPNPEAAKLFIDFLLSDEGQELLAEEGYEYPVRPDVEPPEGLPPLGELKLIDDDDKAAENREELLE
LWDEAV
>gnl|CDD|441446 COG1841, RpmD, Ribosomal protein L30/L7E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L30/L7E is part of the Pathway/BioSystem: Ribosome 50S subunit
MKKLKVTLVRSTIGRPPDQRATLKALGLRKINHTVELPDTPAIRGMINKVKHLVTVEE
>gnl|CDD|441447 COG1842, PspA, Phage shock protein A [Transcription, Signal transduction mechanisms]
GIFKRLSDIIRANINALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW
EEKARLALEKGREDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKA
RAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEAAAELAAGDSLDDELAELEADSEVEDEL
AALKAKM
>gnl|CDD|441448 COG1843, FlgD, Flagellar hook-capping protein FlgD [Cell motility]
MATSSSSSVLSSLSTSSTSSSSSSSSSLGKDDFLKLLVAQLQNQDPLNPMDNTEFIAQLAQFSTVEQIEN
LNTTLESLASSLTSSQALQASSLIGKEVLVEGNTISLDGGSASGGFELPSAADSVTVTITDANGNVVRTI
DLGAQSAGVHTFTWDGTDDDGNALPDGTYTFSVEATDDGEPVTATTLVYGKVTSVTLSGGGPVLNLGGGG
SVPLSDVTEIRDP
>gnl|CDD|441449 COG1844, COG1844, Uncharacterized conserved protein, DUF356 domain [Function unknown]
MMSFALIRADNYDKILNALADLERYGGLKIRGKPRIIEPEYADNILVSVLGVPLRKKCKSAALVEVDENA
GKAISRLRKIHPPAHIVVVSPRHDVYEELLRKFGKLPELKGYYSPKSSDSSDRKKEY
>gnl|CDD|441450 COG1845, CyoC, Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]
AHDVEAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPDWPAGAELLDLPLPLINTLLLLLS
SFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLH
VIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL
>gnl|CDD|441451 COG1846, MarR, DNA-binding transcriptional regulator, MarR family [Transcription]
MSDEPDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVS
RLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLA
EN
>gnl|CDD|441452 COG1847, Jag, Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General function prediction only]
MADFLEELLDIMGLDGDIEIEVEGDRLTVDISGEDLGLLIGRRGETLDALQYLTNLAVNRKTGERSRVIL
DVEGYRERREEELEELARRAAEKVKRTGKPVELEPMSPYERRIIHDALADDPGVETESEGEEPYRRVVIS
PKR
>gnl|CDD|441453 COG1848, VapC, VapC family ribonuclease, toxin component of the VapBC toxin-antitoxin module, contains PIN domain [Defense mechanisms]
MILLDTNVLIYALEGDSPFHERARELLERAEEGEEELYTSPLVLAEVLYVLTRPGGLSLEEARELLEALL
SNIEVVPVDEEILEEAAELLAKYGLRLNDALHLATALEHGADALVTFDRDFARVPGLEVVDPEE
>gnl|CDD|441454 COG1849, COG1849, Uncharacterized conserved protein [Function unknown]
SMSADLEEKVEKYIRMLEEALEKVEPAPPEGSPLYKAAEDFLEMAESYLEDAKYFLEKGDLVTALACISY
AEGWLDAGRRLGLFDVPWDS
>gnl|CDD|441455 COG1850, RbcL, Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate transport and metabolism]
DYVDPDYIPDDDDILATYRITPETGVDPEEAAAAIAGEQSTGTWTEVPTETDELRERLAARVYSIEELPE
VGGGYRRALVTIAYPLENFGGNLPNLLSTVAGNLFGLKAVSGLRLLDLEFPESFLAAFPGPKFGIEGTRE
LLGVYDRPLLGTIIKPKVGLSPEETAELVYELALGGVDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEE
ETGEKKMYAFNITADTDEMLRRADLAVELGANAVMVDVNTVGLSAVQTLREEHIGLPIHAHRAGHGAFTR
SPLHGISMRVLAKLWRLAGADHLHVGTPVGKMEGDDEEVLAIADALLQPWGGLKPVFPVPSGGQHPGQVP
ELYDALGTDLILQAGGGIHGHPDGPAAGARALRQAWEAAVAGIPLEEYAKTHPELAAALEKWGKKAP
>gnl|CDD|441456 COG1851, COG1851, Uncharacterized conserved protein, UPF0128 family [Function unknown]
MMLNTLVFETLGQPEKEREFKIKSLKRWGFDLVLGKKDGKETYFVSKVGEREEGDKYEEGGKEYEIEEVL
KELPKNAKLFARIEMEEGRAYLVFWLREEDENFEILRVPARTLLLAFLKKHKLNHLIKALRNVGLATELV
KQRGVEGKPLPYEELPPVARRFLREAKKVEKDTGFGRVALAYFGENKEGDHRYRLSWLLPTIALFDVDIA
EKVDKILAELK
>gnl|CDD|441457 COG1852, COG1852, Predicted redox protein with CxxCxxC motif, DUF116 family [General function prediction only]
MIIKLLFPKLRLLTLDLLYPLAKALGRLFGIDKDIVDRSFIELNNKLVRSKFKKVPPEKRLILLPHCLQS
SDCPAKITPDGLNCKRCGRCDIGDLKELAEKYGYKVFIATGGTFARKIIKEYRPKAIIAVACERDLTSGI
QDVSPIPVIGVLNERPNGPCFNTSVDVEEVEEAIKLFL
>gnl|CDD|441458 COG1853, RutF, FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]. FMN reductase RutF, DIM6/NTAB family is part of the Pathway/BioSystem: Pyrimidine degradation
MPDAFRDALGRLAPGVAVVTTRDADGRPNGMTASSFTSVSLDPPLVLVSVAKSSDTLENIRETGEFVVNV
LSEDQAELANRFAGRSGRGVDKFAGAGLTTASGEVGAPLLAEAPAWLECRVVDVIELGDHTLFIGEVVAV
HVDEDVDGRPLLYLGGRYRR
>gnl|CDD|441459 COG1854, LuxS, S-ribosylhomocysteine lyase LuxS, autoinducer biosynthesis [Signal transduction mechanisms]
MPKVESFTLDHTKVKAPYVRVAGVDKGPGGDVITKFDLRFCQPNREVLPTAALHTLEHLLAGFLRNHLDG
IIDISPMGCRTGFYLILIGEPSSEEVADALEETLEDVLEAEGEVPAANEVQCGNYRDHSLEGAKEIARKV
LEKGIEWID
>gnl|CDD|441460 COG1855, PilT, Predicted ATPase, PilT family, contains N-terminal PIN domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
MKIVPDTSVIIDGRISELIESGEYRGATIIIPEAVVAELEAQANQGREIGFSGLEELQKLRELAEEGGIE
LEFVGERPSLEQIKLAKGGEIDALIRDVALELGATLITSDRVQAEVARAKGIDVIYLKPEVEEFGPLEIE
EFFDEDTMSVHLKEGVPPMAKRGKPGEWRLVKIRDEPLTREELEEIAREIIERAKRDPDGFIEIERPGAT
VVQLGNYRIAIARPPFSDGIEITAVRPIVKLSLEDYNLSEKLKERLKERAEGILIAGAPGAGKSTFAQAL
AEFYADKGKIVKTMESPRDLQVPPEITQYTPLEGSMEKTADILLLVRPDYTIFDEVRKTEDFEVFADMRL
AGVGMIGVVHATRPIDAIQRFIGRVELGMIPQIVDTVIFIENGEIEKVYDLEFTVKVPTGMTEEDLARPV
IEVRDFETGELEYEIYTFGEQVVVVPVKKEEEEKSGVWKLAEEEIEREIRRYAPGHVEVEIISDNKAVVY
VPEDDIPAVIGKGGKRISEIEKKLGIDIDVRPLEEEPSEELGEGVGVTIEETKKHLVIIVPEYAGKTVDV
YAGDEYLFTATVGRKGEIKVSKNSAIAKELERAIDSGEQITVRPV
>gnl|CDD|441461 COG1856, COG1856, Uncharacterized conserved protein, radical SAM superfamily [General function prediction only]
MADLVELLQAAWEIRKANFPRKIFFYAPGFKHYETSEFNSRNKFPAISVTGGYCALNCDHCGGHYLEGMI
PASTPEELVRVVEELKEKGAKGLLISGGSDKRGKVPLDKFLDALRRIKDKTGLKINVHTGLVDEEIARGL
KEAGVDAVSLDVIGDDETIREVYGLDKTVDDYLRSLELLKKAGLKVVPHIVIGLHYGKILGEYEALEMLS
EYGPDALVLVVLMPTPGTPMANVPPPSPEEVARVLAYARLLLPDLPLSLGCARPRGKYRVELDRYAVDAG
VNGIAFPSEGTVELAKELGREIVYSEECCSLVVG
>gnl|CDD|441462 COG1857, Cas7, CRISPR-Cas system type I effector complex subunit Cas7, RAMP superfamily [Defense mechanisms]. CRISPR-Cas system type I effector complex subunit Cas7, RAMP superfamily is part of the Pathway/BioSystem: CRISPR-Cas system
MSKFLSLTVRFLVNAESLNYGESVGNYTELKKVPVVVKDGYKVEYVPYISGQALRHAYQRALVELAKERG
LPLAEVCKQGEFLKFGGDKGVVQFFEEAIIKDYVVEDLFGFLKTEEGKAVKRTSPVRVSYAIPLEPFKGA
LDAQFHTRYGLADRIGEEQNIFQVEIHSALYTYTITLDLDRIGVDENDERGEIVLDNEERKKRVKALLDA
LKLLLRGFGAKGSRFLPDLSPLFLVAGVSDVKNPFFLPGIKLDYIEEIKERLEKFKKAIKEKTVFGYVKG
FFNNEGEEIKSKKVSSVEELFEKLKEKVLEYYG
>gnl|CDD|441463 COG1858, MauG, Cytochrome c peroxidase [Posttranslational modification, protein turnover, chaperones]
PEKVELGKKLFFDPRLSGNGTISCASCHNPALGFTDGLPTSIGVGGQLGPRNAPTLLNAAFNGAQFWDGR
AASLEEQALGPILNPVEMGMSLEEVVARLKADPEYRALFKAAFGDDPITFDNIAKAIAAFERTLVSPNSP
FDRYLRGDKAALTEQEKRGLNLFFGKAGCASCHNGPLFTDNSFHNIGLPENYGGPPDADLGRYAVTGDPA
DRGKFKTPSLRNVALTAPYMHDGSFATLEEVVDFYNKGGGANPNLDLLLKGLNLTDEEIDDLVAFLKTLT
DEY
>gnl|CDD|441464 COG1859, KptA, RNA:NAD 2'-phosphotransferase, TPT1/KptA family [Translation, ribosomal structure and biogenesis]
MDDKRLERLSKFLSYILRHFPEEIGLELDEEGWVDVDELLAALRRRGRWLTREHLEAVVATNDKGRFEIS
GDRIRANQGHSVPVDLDLPPAEPPEVLYHGTAPRFLDSILEEGLKPMSRHHVHLSADRETARKVGSRHGK
PVVLEVDAAAMRAAGHKFYRSGNGVWLTDHVPPEYLTVVED
>gnl|CDD|441465 COG1860, COG1860, Predicted metal-binding protein, contains two cysteine clusters, UPF0179 family [Nucleotide transport and metabolism, Replication, recombination, and repair]
MTKITLIGSRLAKEGTEFVYLGEAPECEGCKLKKVCLNLEKGRRYRVVGVRENQVHDCPVHDGGVRAVEV
EEAPITANVPSKKAIEGSKITLEGPKCDNIDCPSYELCNPEGLKEGEKYKIVEVLGEPPECPLGRSLKLV
ELAPV
>gnl|CDD|441466 COG1861, SpsF, Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]
MMKIVAIIQARMGSTRLPGKVLKPLGGKPVLEHVIERLKRSKLIDEVVVATTTDPADDPLVDLAKELGVP
VFRGSEDDVLSRYYQAAEAYGADVVVRITGDCPLIDPALIDELIAAFLESGADYVSNSLPRTYPRGLDVE
VFSFAALERAWEEAKLPSEREHVTPYIYEHPDRFRIGNVEPPEDLSDLRLTVDTPEDLELIRAIYEALYP
KNPDFSLEDVLDLLDKNPELAAINAHVEQKEGYEK
>gnl|CDD|441467 COG1862, YajC, Protein translocase subunit YajC [Intracellular trafficking, secretion, and vesicular transport]
MNPALAQAGGGSGLMSLLPLVLIFVIFYFLMIRPQQKRQKEHKEMLSSLKKGDEVVTIGGIHGTVVKVDD
DTVTLEIADGVKVKVERSAIARVLPKGTAKAA
>gnl|CDD|441468 COG1863, MnhE, Multisubunit Na+/H+ antiporter, MnhE subunit [Inorganic ion transport and metabolism]
MKRLLPHLLLSLLLALVWLLLSGSFSPGNLLLGLLLALLVLLLFRRLPPPRLPYLRRPLRLLRLLLYFLW
DIVVANIDVARRVLRPRLPIRPGIVAVPLRLRSDLGITLLANSITLTPGTLTVDVDDDRRTLYVHALDVD
DPEALIEEIKGRYERRLLEIFE
>gnl|CDD|441469 COG1864, NUC1, DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism]
DDAGYDPDFLLLGLPSLARALSTNNYLLCYTGYSLSYNESRRTPNWVAYNLDGSWLGKSLKRSDDFRPDP
RLPSGYRATLADYTGSGYDRGHLAPSADRTFSKEANSETFLMTNISPQAPDFNQGIWARLENYVRDLARK
GGEVYVVTGPVFDDGDLKTIGSGGVAVPTAFWKVVVDPDKNTGTLRAIAFLLPNTALSSGPLRTYQVSVD
EIEKLTGLDFFPNLPDDLEAALEAKVDP
>gnl|CDD|441470 COG1865, CbiZ, Adenosylcobinamide amidohydrolase [Coenzyme transport and metabolism]
MSTGFEVRREDGVLVVRFPGPRRVLSTAVLNGGLREARAVFNHQVPEDYDRTDPEEYLAEVLARLGLPPG
DTVGLLTAADMENAAIAEESFGGLSVTAVVTAGVSNAVRAGADPASYYEPRPPPPGTINIIVLINAPLSD
GALVNAVITATEAKTAALQELGIGSRYSGGLATGTGTDAIAVAAPPDGEPLTYAGKHTKLGELIGRAVYE
AVREALRRQNGLTP
>gnl|CDD|441471 COG1866, PckA, Phosphoenolpyruvate carboxykinase, ATP-dependent [Energy production and conversion]. Phosphoenolpyruvate carboxykinase, ATP-dependent is part of the Pathway/BioSystem: Gluconeogenesis
MSTTPTFGLEKYGIKNLGEVYYNLSPAELVEEALRRGEGVLTSTGALVVDTGKFTGRSPKDKFIVKDPST
EDTIWWGNVNQPISPEKFDALYARVLAYLSGKELFVQDLYAGADPEYRLPVRVITEYAWHALFARNMFIR
PTEEELANFEPDFTIINAPGFKADPERDGTNSETFIILNFTKKIVLIGGTEYAGEMKKSIFSVMNYLLPL
KGVLPMHCSANVGKDGDTALFFGLSGTGKTTLSADPNRKLIGDDEHGWSDNGVFNFEGGCYAKTINLSAE
AEPEIYNAIRFGAVLENVVLDPETREPDYDDGSLTENTRAAYPIEHIPNAVIPSRGGHPKNIIFLTADAF
GVLPPISKLTPEQAMYHFLSGYTAKVAGTERGVTEPQATFSACFGAPFMPLHPTVYAELLGEKIAEHGVN
VWLVNTGWTGGPYGVGKRMSIKYTRAMIDAALDGSLDNVEFETDPIFGLAVPTSCPGVPSEILNPRNTWA
DKAAYDAQAKKLAGMFIENFKKFEDHVSEEIRAAGPKLK
>gnl|CDD|441472 COG1867, TRM1, tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]. tRNA G26 N,N-dimethylase Trm1 is part of the Pathway/BioSystem: tRNA modification
MDLMEITEGKVKILVPDPEKYSRFEPAWAPVFYNPRMELNRDISVAALRAYRERLKREISYLDALAASGI
RGLRYALEVGIKVTLNDIDPEAVELIRENLELNGLEDVEVYNRDANALLHELGRRFDVVDLDPFGSPAPF
IDSALRAARKGGLLCVTATDTAPLCGAHPKSCIRRYGAVPLNTEYHHEMGLRILLGAIARTAARYDKGIE
PLLSHATDHYVRVYLEVERGAKKADEALEELGYIYHCPSCLYREAEKGLLAHEECPLCGSELVTAGPLWL
GPLHDKEFVEEMLEEADDLELGTAKRARKLLETLREELDIPPTYYDQHELCKRLKISAPSMDEFIEALRE
AGYKASRTHFSPTGFKTDAPLDEIREAIRELSS
>gnl|CDD|441473 COG1868, FliM, Flagellar motor switch protein FliM [Cell motility]
MSDVLSQEEIDALLSAVSSGEVDAEEKEEEEEKKVKPYDFRRPDRFSKERLPTLEIIHERFARLLRTSLS
NLLRRNVEISVASVEQLTYGEFIRSLPVPTSLNIFRLEPLRGSALLEIDPSLVFALVDRLLGGDGRPHAI
EGREFTEIEQRIIERLLELLLEDLEEAWAPVYPLEPELERSETNPQFAQIVSPNEVVVVVTFEVEIGDRS
GMINICIPYSTLEPIRDKLSSRFQSDRKERDERWRERLREELEEAEVELSAELGETEITLRELLNLKVGD
VIPLDKKVDDPLTVYVGGVPKFEGKPGVSNGRLAVKITEIIEEEEE
>gnl|CDD|441474 COG1869, RbsD, D-ribose pyranose/furanose isomerase RbsD [Carbohydrate transport and metabolism]
MKKTGILNSELSRVLARLGHTDTIVIADAGLPIPPGVERIDLALTPGVPSFLDVLDAVLSELQVEKAILA
EEIKEKNPELHEALLELLPGIEIEYVSHEEFKELTKQAKAVIRTGECTPYANIILVSGV
>gnl|CDD|441475 COG1871, CheD, Chemotaxis receptor (MCP) glutamine deamidase CheD [Signal transduction mechanisms]
MSNAGMKEIKVGPGEYYVSTDPDTLITTGLGSCVAVCLYDPVAKIGGMNHFMLPDSSGAKAAGNPAKYGD
TAMELLINELLKLGARRERLEAKIFGGANMFSGLSSDSLNIGERNVEAAREYLAEEGIPIVAEDVGGNYG
RTVEFDPATGRVLVKTLGGGEKEL
>gnl|CDD|441476 COG1872, YggU, Uncharacterized conserved protein YggU, UPF0235/DUF167 family [Function unknown]
MDALREDGDGLILAVRVQPGASRDAIVGVHGGALKVRVTAPPVDGKANAALIKLLAKALGVPKSRVEIVS
GETSRNKRVRI
>gnl|CDD|441477 COG1873, YlmC, Sporulation protein YlmC, YlmC/YmxH family, contains PRC-barrel domain [General function prediction only]
ASELIGKEVITSDGERLGKVKDVEIDLETGKIEALVVPPGNKFFGFLGDGEKEVVIPWEAVKKIGDDVIL
>gnl|CDD|441478 COG1874, GanA, Beta-galactosidase GanA [Carbohydrate transport and metabolism]
FTFLLDKPFLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIGYFAWNLHEPEEGVFDFDWLDRFIDLL
HEAGLKVILRTPTAAPPAWLLKKYPEILPVDADGRRRGFGSRRHYCPSSPVYREAARRIVRALAERYGDH
PAVIMWQVDNEYGSYDYCDACAAAFRDWLRERYGTLDALNEAWGTAFWSQRYTDWDEIEPPRLTPTTANP
SLRLDFRRFSSDQVLEYLRAQRDILREAGPDVPVTTNFMGPFPGLDYWKLARDLDVVSWDNYPDGSAADP
DEIAFAHDLMRGLKGGGPFMVMEQWPGWVNWGPYNPAKRPGQLRLWSLQALAHGADGVNYFQWRPSRGGT
EYDHDAPLDHAGRPTRKFREVRELGAELARLPEVPGSRVTARVALLFDWESWWALEIQSPPLGQDLGYVD
LVRALYRALRRAGVTVDIVPPFADLSGYKLLVAPALYLVSDALAERLLAYVENGGRVNYGPRSGIVDEKD
RVRLGGYPGILRDLLGVRVEEFDPLPPGEPVPLSGGYTGWLWYELLPLDGAEVLARYADGFYAGRPAVTR
NTFGKGVAWYNGTNLDDWLLAALLARLLAEAGLYPVDLPEGVEAVRRVG
>gnl|CDD|441479 COG1875, YlaK, Predicted ribonuclease YlaK, contains NYN-type RNase and PhoH-family ATPase domains [General function prediction only]
MSMKKTYVLDTNVLLHDPNAIFRFEEHDVVIPMVVLEELDKFKKGMSELGRNARQASRLLDELRAKGNLD
EGVPLPNGGTLRVELNHKDSELPAGLPLDKNDNRILAVALNLQEEYPGRPVILVSKDINLRIKADALGLE
AEDYRNDKVLDIDLLYTGVKELPVSDEEIDSLYEGGRIDLPELPELYPNQFVILESENPFKSALGRVDGD
TAKLVLLKDLGDRSVWGIKPRNREQRFALDLLLDPDIDLVTLLGKAGTGKTLLALAAGLEQVLEEKRYRK
IIVTRPTVPVGEDIGFLPGTEEEKMAPWMQAIYDNLEFLVSSDEKKGEWGRSIDELLDRGRIEIESLTFI
RGRSLPNQFVIIDEAQNLTPHQVKTIITRAGEGTKIVLTGDPAQIDNPYLDEHSNGLTYVVERFKGWPLS
GHITLTRGERSRLAELAAELL
>gnl|CDD|441480 COG1876, LdcB, LD-carboxypeptidase LdcB, LAS superfamily [Cell wall/membrane/envelope biogenesis]
LVNKDHPLPADDLVPLPGGGHRLRKEAAAAFEAMQAAAKKDGIDLVIVSGYRSYERQEALYNRKVARYGI
EAALRYSAPPGTSEHHTGLAIDIGDPDPGTDLEEEFEETPAGKWLAANAAKYGFILRYPKGKEDITGYAY
EPWHWRYVGVEAAKEIFEKGLTLEEYLG
>gnl|CDD|441481 COG1877, OtsB, Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism]
APRLLLFLDFDGTLAPIVPDPDAARPPPELRELLRRLAARPGGAVAIVSGRDLADLDRLLGPLGLPLAGS
HGAERRLPGGEWEVLPLAAEAPEWLDALRAALEALAARTPGVLVEDKGASLALHYRQAPPEEAEELRAAL
RELAARLGPGLEVLPGKKVVELRPAGVDKGRAVRALLAELPFGRAPVFIGDDVTDEDAFAALPAGGLGIK
VGSGPTAARYRLADPAEVRALLARLAEARRAA
>gnl|CDD|441482 COG1878, COG1878, Kynurenine formamidase [Amino acid transport and metabolism]
KIIDLSHPISPGMPVYPGDPPPEIEPVATLEEGDGFNVSRITMGTHTGTHIDAPAHFIPGGRTIDELPLE
RLVGPAVVIDVSGKADYLITVEDLEAWEAQGGEIPPGDIVLLRTGWSKRWGTEAYLNHFPGLSPEAAEWL
VERGVKLVGIDTLSIDPPEDEDFPVHRALLGAGIYIIENLTNLDELPAGGFTLIALPLKIKGGDGSPVRA
VAIVPE
>gnl|CDD|441483 COG1879, RbsB, ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism]
KRLALLAAVLALALALAACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVD
AEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAA
GRLAAEYLAKALGGKGKVAILTGSPGAPAANERTDGFKEALKEYPGIKVVAEQYADWDREKALEVMEDLL
QAHPDIDGIFAANDGMALGAAQALKAAGRKGDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVD
AALKLLKGKEVPKEILTPPVLVTKENV
>gnl|CDD|441484 COG1880, CdhB, CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion]
DPWQIATIAGPKTAKAVKPEVAAKMIKKAKRPLLIVGPEALDDEELLERAIEIAKKAGIPIAATGHSIKG
FVERGVEPAKYINIHELTNFLKDPEWKGLDGNGQYDLVIFLGFKYYYASQVLSGLKHFAPHLKTIAIDRY
YHPNADMSFGNLKPEDWLAALDELIDNL
>gnl|CDD|441485 COG1881, PEBP, Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family [General function prediction only]
FTLTSPAFADGGPIPDKYTCDGENVSPPLSWSGAPEGTKSFALIVEDPDAPTGGGFWHWVVYNIPADVTE
LPEGAGSADLPAGAVQGRNDFGEAGYGGPCPPPGDGPHRYVFTVYALDVELDLPPGATRAELLFAMEGHV
LARATLTGTYE
>gnl|CDD|441486 COG1882, PflD, Pyruvate-formate lyase [Energy production and conversion]. Pyruvate-formate lyase is part of the Pathway/BioSystem: Pyruvate oxidation
ESFLAGPTERTKRLREKLLEAKPLIDIERARLFTESYKETEGLPVIIRRAKAFSHILEHKPIYIKDDELI
VGLQTDKPRKRPIFPEGGIRWVEDELDALPTRPQDGFEISPEDKEIFREIAPYWKGKTHNDGVFDAYPEE
IRKARKAGIITGLPDAYGRGHIIGDYRRVLLYGLDGLIEEAKEKLAELDLTDPEDIEKIDFYKAMIIVCE
AVIRLAERYAELARELAEKETDPKRKAELLEIAEICGFVPANPARTFWEAVQWVWFVYLAAIKEQNGAAM
SLGRFDQYLYPYYERDLEEGRLTEEEAQELLDCFWIKLREVRFLRTPEYAELFAGYPTWVTLTIGGMTPD
GRDAVNELSYLILETLRNLPLPEPNLTVRWSEKLPEGFLKKAAEVISIGTGSPQYENDDLMIPMLLNKGV
TLEDARDYGIAGCVEPMVPGKQMQFFGAGRINLAKALEYALNNGVDEKTGKQVGPETGDPTDFLTYDEVM
EAFKKQLDYLADLYVNALNIIHYMHDKYAPEPFLSALHDDCIERGKDLNEGGARYNFGAIGIAGLSVVAD
SLSAIKKLVFDKKKVTMDELLEALAANFEGYEELRQLLLNAPKYGNDDDYVDEIAVELVETFMDEIRKYK
TYRGGTYTLSILTITSNVPYGKKTGATPDGRKAGEPLADGASPMHGRDKNGPTAVLKSVAKLPYEKATDG
ILLNQKFSPSALGGEEGIENLVSLLRTYFDLGGHHIQFNVVDRETLLDAQKHPEKYPDLTVRVAGYSAYF
VELSKEQQDDIIARTEHEF
>gnl|CDD|441487 COG1883, OadB, Na+-transporting oxaloacetate/methylmalonyl-CoA decarboxylase, beta subunit [Energy production and conversion]
MMEDLLNLFQSTGFANLTWGNLVMILVGLLLIYLAIKKKYEPLLLLPIGFGMILANIPLSGLMEILQGGL
LQYLYNFGISNGLFPPLIFMGIGAMTDFGPLLANPKSLLLGAAAQFGIFATLLGALALGFTLKEAASIGI
IGGADGPTAIFVASKLAPHLLGPIAVAAYSYMALVPIIQPPIMKLLTTKKERKIRMKQLRPVSKLEKILF
PIVVTILVGLLLPSAAPLIGMLMLGNLLRESGVVERLSDTAQNELINIVTIFLGLTVGATMEADTFLNPK
TLGILVLGLVAFAIGTAGGVLFAKLMNLFSKGKINPLIGAAGVSAVPMAARVAQKVGQEEDPSNFLLMHA
MGPNVAGVIGSAVAAGVLLSLLG
>gnl|CDD|441488 COG1884, Sbm, Methylmalonyl-CoA mutase, N-terminal domain/subunit [Lipid transport and metabolism]
KLRKKPERKLEFTTLSGIPVKPVYTPADLADLDYLEDLGFPGEFPYTRGVYPTMYRGRPWTMRQYAGFGT
AEETNARYRYLLAAGQTGLSVAFDLPTLRGYDSDHPRAYGEVGKAGVAIDSLEDMEILFDGIPLDKVSVS
MTINGPAPPLLAMYIAAAEEQGVDPEKLRGTIQNDILKEYIARNTYIFPPEPSMRLIGDIFEYCAKHVPK
FNSISISGYHIREAGATAVQELAFTLADGIEYVEAALARGLDVDDFAPRLSFFFNIGMDFFEEVAKFRAA
RRIWARIMKERFGAKNPRSMMLRFHTQTSGWSLTAQQPLNNIVRTTLQALAAVLGGTQSLHTNAYDEALA
LPTEESARIALRTQQIIAEETGVTDTVDPLGGSYYVESLTDELEERAWAYIEEIEELGGMLKAIETGYPQ
REIQEAAYRYQARIDSGERVIVGVNKFRLEEEPPIELLRVDPEVRERQIERLKELRAERDNAAVEAALAA
LREAARSGGNLMPLIIDAVRAYATLGEISDALREVFGEYREPI
>gnl|CDD|441489 COG1885, COG1885, Uncharacterized conserved protein, UPF0212 family [Function unknown]
MPDYRVVLEAAWLVRDVETVDDAIGIAISEAGKRLNPDLDYVEIEVGDTACPSCGEELESAFVVADTALV
GLELEMKVFNAESEEHASRIAKSEIGKALRDIPLEVLEVEEI
>gnl|CDD|441490 COG1886, FliN, Flagellar motor switch/type III secretory pathway protein FliN [Cell motility, Intracellular trafficking, secretion, and vesicular transport]
LALAALLLALLLALAALALLLALALALPVLLAALLALLLALLLLAPLLLLAAAGAALLLGLLDLLLEVGG
LLLLGSDEEPAEFEPLEDAPEAEEEPENLDLLLDVPVEVTVELGRTRLTLRELLKLGPGSVIELDRLAGE
PVDILVNGRLIARGEVVVVDDRFGVRITEIVS
>gnl|CDD|441491 COG1887, TagB, CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism]
KLLLLLRRLYYRLSRLLPVKKNIILFESRNGRSYSDNPKALFEYLRKNHPDYEVVWVVDDDSKRLPKEGV
KVVKRGSLKYLYALARAKYLVSNHYFPFPSYFRKRKGQKYVQLWHGTPLKKIGLDDPPRYLKRVLREYRN
WDYLLSSSEESTEIFRRAFGYPEGEVLETGYPRNDVLFDADREELREELRERLGIPEDKKVILYAPTWRD
DEDNFDDYLDLDLERLAELLGDDYVLLVRLHPFVKDSLDEKYSDRIIDVSDYPDINDLLLASDVLITDYS
SVMFDFALLDRPIIFYAYDLEEYRDERGFYFDYEEDAPGPVVTTFEELIDAIEDILENGDEYAEKYKAFR
ERFFPYDDGNASERVVDAI
>gnl|CDD|441492 COG1888, COG1888, Uncharacterized conserved protein, DUF211 domain [Function unknown]
AGIRRLVLDVLKPHEPSIVEFAKALADLEGVDGVNITVVEVDVETENLKVTIEGDDIDFEEIEEAIEDLG
GVIHSIDEVVAGKRIVEE
>gnl|CDD|441493 COG1889, NOP1, Fibrillarin-like rRNA 2'-O-methylase NOP1 [Translation, ribosomal structure and biogenesis]
MEELFEGVYRVEFDGEKRLATKNLVPGKRVYGERLIKIEGVEYREWDPRRSKLAAAILKGLKELPIKEGS
KVLYLGAASGTTVSHVSDIVPEGPVYAVEFAPRVMRDLLEVAESRPNIIPILADARKPEEYAHVVEKVDV
IYQDVAQPNQAEIAIKNADFFLKKGGYLLLAIKARSIDVTKDPKEIFKEEIRKLEERGFEILEIIDLEPY
HKDHLMVVARKK
>gnl|CDD|441494 COG1890, RPS3A, Ribosomal protein S3AE [Translation, ribosomal structure and biogenesis]. Ribosomal protein S3AE is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MARKRARRVKDKWKEKKWYTVYAPEFFGEVEIGETPADDPEKLIGRVVETTLGDLTGDFSKQNIKLYFKI
NDVEGDKAYTEFIGHELTRDYLRSLVRRGSSKIDAIVDVTTKDGYKVRVKPVAFTTKRANTSQKHAIRKI
MRDIVEEKAKELTFDEFVQEIVFGKLSSDIYKEAKKIYPLRRVEIRKSKLLARPEEEAPEEEVAEAVE
>gnl|CDD|441495 COG1891, MfnB, 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate synthase MfnB [Coenzyme transport and metabolism]
MTKLLVSVRSLEEALLALEGGADIIDLKNPAEGALGALFPWVIREIVEAVGGRKPVSATIGDLPMKPGTI
SLAALGAAATGVDYVKVGLFGGDDAEEALEALAPLVRAPGKRVVAVLYADAGRPLDLLALAAAAGFDGVM
LDTADKDGGSLFDFLDEEELAEFVALARALGLLCGLAGSLRFEDIPRLLRLGPDYLGFRGALCEGGDRNS
AIDPELVAALRALLHGA
>gnl|CDD|441496 COG1892, PpcA, Phosphoenolpyruvate carboxylase [Carbohydrate transport and metabolism]
MRKIPRTMSTQHPDNASVPFWAESPVIEGEDEIEEAYYAFSHLGCDEVMWDAEGKDVDTFVVRKLLSRYP
EFFKNKILGKDIFLTYRVPNPSVEKAERKVLAETLESIPRSYDVARVFYGEPVPPIFEVILPMTTSAEEL
IRVYRYYEKAVAGKEEIELYDGDITVKDWIGEFYPKKIEVIPLIEDKDSLLNIDKIVGEYLKDKKPEYQR
VFLARSDPAMNYGLISAVLLVKYALSKLYKLEEELGIPIYPIIGVGSLPFRGNLSPDNVEKVLNEYPGVY
TFTIQSAFKYDYPEKEVKKAIEKINNTKRKEPESIDEEEIILDIIEKYSSEYQKIIEALAPLINDVALYL
PRRRARKLHIGLFGYSRSTGGVTLPRAISFVAALYSIGLPPEILGLSSLSKLTEEELDVLKENYKNLKED
LSEAARYFNPEVLELLKSIWKIDKETIKMIKEDIKYAEKLLGIKIGPKDYESRKHALLTSLILLALKEGK
FEEAKKYILEMALIRKFLG
>gnl|CDD|441497 COG1893, PanE, Ketopantoate reductase [Coenzyme transport and metabolism]. Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
MKIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEALRENGLRLESPDGDRTTVPVPAVTDPEELGPAD
LVLVAVKAYDLEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHT
GGGRLVLGELDGGPSERLEALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADP
EARALARALMREVLAVARAEGVPLPEDDLEERVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLA
RRLGVPTPVNEALYALLKALEAGRA
>gnl|CDD|441498 COG1894, NuoF, NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) [Energy production and conversion]. NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) is part of the Pathway/BioSystem: NADH dehydrogenase
KKQTRVLLRNCGIIDPESLEDYIARGGYQALRKALTEMTPEEVIEEVKDSGLRGRGGAGFPTGLKWSFVP
KAPGDPKYLVCNADEGEPGTFKDRSLLEGDPHQLIEGMIIAAYAIGATKGYIYIRGEYPLAIERLEKAIE
EAREAGLLGKNILGSGFDFDIEVHRGAGAYICGEETALLESLEGKRGQPRLKPPFPAVSGLWGKPTVVNN
VETLANVPHIIRNGAEWFASIGTEKSKGTKLFSLSGHVKNPGLYEVPMGTTLRELIYDIGGGIRGGRKLK
AVQPGGPSGGCLPAEHLDTPMDYESLAAAGSMLGSGGMIVMDETTCMVDVARFFLEFYAHESCGKCTPCR
EGTGWMLEILDRIEAGEGTEEDLDLLEDLADTIKGTSLCALGDAAPNPVLSTLKYFRDEFEAHIKDKR
>gnl|CDD|441499 COG1895, HEPN, HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms]
LVATLLEKAEEKLAAAKLLLENGLYEDAINRAYYAMFHAAKALLLSKGLSPKTHSGVISAFGEHFVKTGK
IDLELGRFLSRAFQLRQNADYGGEAEPTEEEAKEYIEQAEEFLEEIKAYL
>gnl|CDD|441500 COG1896, YfbR, 5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and metabolism, General function prediction only]
QLDFLAELDRLKLIKRWGLLRNSRPENVAEHSWHVALIAHLLADIANEGVDPERVAKMALLHDLVEIDTG
DIPTPVKYANEAKKEIERAAAERLFGLLPEELREEFRALWDEFEAGETPEARFVKAADKLEALLQALEEI
GAGNKENTFEQAYERLLKKIKE
>gnl|CDD|441501 COG1897, MetA, Homoserine O-succinyltransferase [Amino acid transport and metabolism]. Homoserine O-succinyltransferase is part of the Pathway/BioSystem: Methionine biosynthesis
MPIKIPDDLPAFEILRKENIFVMDEERAAHQDIRPLKIGILNLMPKKIETETQLLRLLGNTPLQVEVTLL
RMDSHESKNTPQEHLETFYKTFDEIKDEKFDGLIITGAPVEHLDFEEVDYWDELKEIMDWAKTHVTSTLH
ICWGAQAALYHHYGIPKYPLPEKLFGVFPHRVLDPNHPLLRGFDDRFYVPHSRYTEVRREDIEAVPGLEI
LAESEEAGVYLAASKDGRQVFVTGHPEYDRDTLKKEYKRDVAKGLPPPIPKNYFPDDDPAKEPLNRWRSH
AHLLFSNWLNYYVYQETPYDLEKIGEGVD
>gnl|CDD|441502 COG1898, RfbC, dTDP-4-dehydrorhamnose 3,5-epimerase or related enzyme [Cell wall/membrane/envelope biogenesis]
MKVIETAIPGVLLIEPKVFGDERGFFFETFNAEEFAEAGLDFDFVQDNHSRSRKGVLRGLHFQLPPHAQA
KLVRVVRGAVFDVAVDLRKGSPTFGQWVGVELSAENGRQLYIPEGFAHGFLTLSDDAEVLYKVTDYYAPE
AERGIRWNDPDLGIDWPLPLEPILSEKDAAAPTLAEA
>gnl|CDD|441503 COG1899, DYS1, Deoxyhypusine synthase [Posttranslational modification, protein turnover, chaperones, Translation, ribosomal structure and biogenesis]
MSGTREELLGEPVKDIDIKPGMSVSELIDAMGKTGFNARRLAEAADILEEMLKDKDCTVFLTLAGAMVPA
GLRGIIADLIRNGMVDVIVTTGANLDHDIAEALGGKHYKGSFDADDEELREEGINRIYDVFIPEESYRVI
EEFVREILEELEKKKPYSSREFLYELGKYLDEKEDEDSILYAAYENGVPIFVPAITDSSIGLQLWMHRQE
GSDLKIDAFKDVRELTDIVFKAKKTGALIIGGGVPKNFTIQTNPFLEILGLDRGGLDYAVQITTAPPDDG
SLSGATLREAISWGKVKPDAKKVTVYGDATIALPLLVAALLER
>gnl|CDD|441504 COG1900, HcyBio, Sulfur incorporation enzyme MA1821 (anaerobic homocysteine biosynthesis), HcyBio/DUF39 family [Amino acid transport and metabolism]
MKTIAEINEKIRKGKAVVVTAEEMIDIVKELGVEKAAKEVDVVTTGTFGPMCSSGAFLNFGHSDPPIKMR
KVWLNGVPAYAGLAAVDLYLGATQPSEDDPPGEFEYGGGHVIEDLIAGKSVHLRATGYGTDCYPRKEIET
TITLDDINQAYLFNPRNAYQNYNVAVNSSDRTLYTYMGPLLPNLGNATYSTAGALSPLLNDPYLRTIGIG
TRIFLGGGIGYVAWEGTQHNPLVKRLENGVPLGPAGTLAVIGDLKQMSPEWLRGASFKGYGVSLMVGVGI
PIPVLNEEVARYTAVSDEDIVAPVVDYSIPRRVRPTLGLVSYAELKSGKIEIEGKEVPTAPLSSYKKARE
IAEELKEWIESGEFLLTEPVAPLPSDRSFKPLDIRG
>gnl|CDD|441505 COG1901, TrmY, tRNA pseudouridine-54 N-methylase [Translation, ribosomal structure and biogenesis]. tRNA pseudouridine-54 N-methylase is part of the Pathway/BioSystem: tRNA modification
MRQFVVIGHKAPTDPDFSLDDLPGGAGRLDILCRCVNSAFFLSHGIRRDVRVYLVLLGGPDPPKTIRFEG
SELRYLNPDERSTAALIRKALEKREGAIGEQERESTPGVYVRRGGFEDLLDELAEDGTLYYLHEDGEDIR
DVEFPEDPVFVLSDHIGFTEEEEALLEELGAEKISLGPKSLHADHCITVVHNELDRRGYG
>gnl|CDD|441506 COG1902, FadH, 2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion]
MMKMPKLFSPLTLGGLTLKNRIVMAPMTRGRADEDGVPTDLHAAYYAQRARGGAGLIITEATAVSPEGRG
YPGQPGIWDDEQIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDLPGGWPPVAPSAIPAPGGPPTPRALT
TEEIERIIEDFAAAARRAKEAGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVR
AAVGPDFPVGVRLSPTDFVEGGLTLEESVELAKALEEAGVDYLHVSSGGYEPDAMIPTIVPEGYQLPFAA
RIRKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRPLLADPDLPNKAAAGRGDEIRPCIGCNQCLPT
FYGGASCYVDPRLGR
>gnl|CDD|441507 COG1903, CbiD, Cobalamin biosynthesis protein CbiD (cobalt-precorrin-5B C-methyltransferase) [Coenzyme transport and metabolism]. Cobalamin biosynthesis protein CbiD (cobalt-precorrin-5B C-methyltransferase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MSELYVSKNGKKLRTGYTTGSCAAAAAKAALLALLTGEFPDEVEITLPKGIRLTFPVEDVEIDGGSASAA
VIKDAGDDPDVTHGALIFARVRLTPGPGIVIDGGEGVGTVTKPGLPLPVGEPAINPVPRRMIEEAVREVL
AELGYGGGVEVTISVPEGEELAKKTLNPRLGIVGGISILGTTGIVRPMSEEAWKASIRQEIDVARANGLD
HVVLTTGNRGEKFARELLGLPEEAFVQMGNFVGYMLKEAVRHGFKKVLLVGHIGKLVKLAAGIFNTHSRV
ADVRLEILAALAALAGAPPELVEAILAANTAEEALELLEEAGLDAVFDLIAERAAERARERLGGDIEVEV
VLFDRDGGILGRSEGADE
>gnl|CDD|441508 COG1904, UxaC, Glucuronate isomerase [Carbohydrate transport and metabolism]
DEDFLLPTETARRLYHDYAKDLPIIDYHCHLDPKEIAENKPFENPTELWLGGDHYKWRAMRANGVDEEYI
TGEADDREKFRAWAETVPLFRGNPLYHWTHLELKRYFGIDELLSPETADEIYDEINEKLATPEFRPRALL
ERFNVEVLCTTDDPLDDLEYHKAIAADGFKGRVLPTFRPDKALNIEKEGFADYLEKLGEASGVDITSFDG
LLAALRKRRDFFHAHGCRASDHGLETARTADLSEAEAEAIFAKALAGETLSAEEAEAFRTAMLTELARMY
AEDGWVMQLHPGALRNNNTRMFARLGPDTGFDSIGDTEYAEALSPLLDALGNEPQLPKTILYTLNPTDNR
ELAPLAGNFPDGGIAGKVQLGSAWWFLDQKDGMERQREALTETGLLSNFVGMLTDSRSFLSYARHDYFRR
ILCNLLGRLVEEGELPEDEALLGEIVEDICYNNAKRYFKL
>gnl|CDD|441509 COG1905, NuoE, NADH:ubiquinone oxidoreductase 24 kD subunit (chain E) [Energy production and conversion]. NADH:ubiquinone oxidoreductase 24 kD subunit (chain E) is part of the Pathway/BioSystem: NADH dehydrogenase
MSERELSEELLAEIDEIIAKYPRKRSALIPILHLVQEEFGYLPEEAIEEIAEALGLPPAEVYGVATFYSM
FRLKPVGKHVIRVCTGTACHLRGAEELLEALEEKLGIKPGETTADGKFTLEEVECLGACGLAPVMMVNDD
VYGRLTPEKVDEILDELRA
>gnl|CDD|441510 COG1906, COG1906, Predicted GntP-related membrane permease AF0261, DUF401 family [General function prediction only]
MMELLKVLLAFALIIVLLRKKVNLGIAILAGSLILALLFGLGPLALLGALLKTLTSPNTLELILIVALIM
ILGSLMRKTGLLDRMVEALSKLFRSPRLSLAFIPALIGLLPMPGGALFSAPMVKEAGEELNLSPEKKAFI
NYWFRHIWEYIWPLYPGIILASSIAGISLSKLILLNWPITLLAILAGYLFLFRPLRKEKKPAEEDSKERR
RALKELLKSLLPILVVVLLVLLFGLPLLIALLLGLLVLVILNRKPLKNFKEVLKKALKWKILLLVLGVMI
FKEILEASGAVESLSEELLSLGIPVLVIIILLPFIVGLLTGITVAFVGIAFPLLLPLIGSSNSILPLLML
AYASGFAGVMLSPVHLCLILTAEYFKADLGKVYKYLLPPALLLLALGLLYFLLLGFL
>gnl|CDD|441511 COG1907, bRFAP, Beta-ribofuranosylaminobenzene 5'-phosphate synthase (methanopterin biosynthesis) [Coenzyme transport and metabolism]
PRMVRVTAPARLHLGFLDLNGALGRRFGGIGLALDEPRTVVEAEPADELEVEGPEAERARAYAERLLEAL
GVPGGVRITVEEAIPRHVGLGSGTQLALAVAAALARLYGLPLSVRELARLLGRGGRSGIGVAAFERGGFI
VDGGHPTERTVPPLIARHDFPEDWRFLLVIPDAGRGLHGEEEVDAFRRLPPLPPEDADELCRLVLMQLLP
ALAEGDLEAFGEAINEIQRLGGDYFAPAQGGVYRSPAVEEVLELLREAGAEGVGQSSWGPTVYGITDSEE
EAEAIAAALRALLDRGVGGEVIVTRARNRGAEIREE
>gnl|CDD|441512 COG1908, FrhD, Coenzyme F420-reducing hydrogenase, delta subunit [Energy production and conversion]
EEEFEPKILAFVCNWCAYAAADLAGVSRLQYPPNVRIIRVPCSGRVDPAFILKALSKGADGVLVLGCHPG
DCHYIKGNYRARRRVELLKELLEELGLEPERVRLEWVSAAEGEKFAEVINEFVERIKELGPNPLKGF
>gnl|CDD|441513 COG1909, DPCK, Archaeal dephospho-CoA kinase [Coenzyme transport and metabolism]
MLRLPEELREELKEPFGPLYTDAEDLLEDVREELKKAKPLITVGDVVTYNLLEAGIVPDLAIVDGKTKRE
PVDEEVRTGYRVLEVKNPPGTITEELIEAIKEALESGEPTLILVDGEEDLAVLPAILLAPEGSVVVYGQP
GEGMVLVKVTEEAKERARELLDKFEGDEE
>gnl|CDD|441514 COG1910, YvgK, Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism]
PLLYKLLGLLAPLREKVEAALSRKLVSSLGVLEFLRVKLGLVGGLRVAEPLVRGAGVITSLVAADGLLKI
PEPSEGLEAGLEVEVELLRPELPLLTLVIIGSHDPLLDILLRLLEKRESGAGLASSYVGSLGGLEALARG
EADIAGIHLLDEETGEYNIPYVRRYLPGRPAVLINLARREQGLIVAKGNPKGIKGLEDLARPDLRFVNRQ
KGSGTRVLLDELLRRLGIDPEDINGYEREEYTHLAVAAAVASGEADVGLGIEAAARAFGLDFIPLAEERY
DLVIPREALFDPPVQALLEILRSPEFRERAAALGGYDLSDTGKVIYEA
>gnl|CDD|441515 COG1911, RPL30E, Ribosomal protein L30E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L30E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MMDIEKALRDAVKTGKVVLGSKQTIKAIKLGKAKLVILAANCPPEIREDIEYYAKLSNVPVYVYPGTSVE
LGALCGKPFRVSALAIIDPGESDILAL
>gnl|CDD|441516 COG1912, COG1912, Stereoselective (R,S)-S-adenosylmethionine hydrolase (adenosine-forming) [Coenzyme transport and metabolism, Defense mechanisms]
IITLLTDFGLKDPYVGAMKGVILSINPDARIVDITHDIPPFNIRAAAFILAQAYPYFPPGTVHLAVVDPG
VGTERRAIAVETEGHYFVGPDNGLLSLVAEELGPEEVVEIDNPDYRPPVSSTFHGRDVFAPAAAHLASGV
PLEELGPPIDDSLVRLPLPEPVVEDDGIEGEVIYIDHFGNLITNIPAELFEGLGKFEVRVGGRTIEPIVR
TYADVPPGELLALFNSSGLLEIAVNQGSAAELLGLKVGDPVRIEFKK
>gnl|CDD|441517 COG1913, COG1913, Predicted Zn-dependent protease [General function prediction only]
MKILLVPLGDVPPDLLDELAEELREVFGLPVEVLPPLPLPLEAYDPERGQYDAEALLDFLSRLKEEDGDK
VLGVTDVDLYAPGLNFVFGLAYLGGRVAVVSTARLRPEFYGLPPDEELFLERVLKEAVHELGHLFGLGHC
PNPRCVMHFSNSLEELDRKPPSFCPSCRRKLRRKL
>gnl|CDD|441518 COG1914, MntH, Mn2+ or Fe2+ transporter, NRAMP family [Inorganic ion transport and metabolism]
PRKRSRLRRLLALLGPGLLVAAAYIDPGNLATYTQAGAQFGYSLLWVILLSNLLAIVLQEMSARLGIVTG
KGLAELIRERLGRWLGWLLLILLELANLATDAAEIAGAALALNLLFGIPLLLGAVITALLAILLLLRGGY
RRLERVLKVLVALMLLAFVVTAFLAHPDWGEVAKGTLVPSLPGSGSLLLAIAILGATVMPYNLFLHSSLV
QEKGWTGKEDLRYARLDTVVGMLLAGLVNLAILLLAAAVLHGTGIGVDSAAQAAQALEPLLGEWAAILFA
LGLLAAGFSSTITATLAGAYVMAGFLGWRIGLWLRRFYLVTRLLTLIGALIVLLLGGDPVKLLVLSQVLN
GLLLPFALIPLLLLTNDKDLMGEYRNGRWLNVLGWLIVLLIVVLNLYLLVSTLFG
>gnl|CDD|441519 COG1915, COG1915, Uncharacterized conserved protein AF1278, contains saccharopine dehydrogenase N-terminal (SDHN) domain [Function unknown]
MMFSREVELEGHIIDSGILPKVLDLIMDMGGSFEILDFDVGKKKDDPSYARLRVSAPDEEHLDEILSELH
RLGAVLVDAPDAKLEPAPKDGVAPDGFYSTTNYPTYVRINGEWILVENSRMDCVIVVDPEDGRARCVEFR
DVKKGDLVVVGEEGIRVHPPERPREGGDTFAFMSGGVSSERPFSLDIRQIAEELREEKAEGGKILWVGGP
AVVHTGARDALARLIREGYVDALLAGNALATHDIEAALFGTSLGVDLYTGESVPGGHRHHLDAINEIRRA
GSIKAAVESGVLKSGIMYECVKNNVPFVLAGSIRDDGPLPDVITDVYEAQDAMREHLRGADMVIMLATML
HSIATGNMLPSYVKTVCVDINPATVTKLSDRGSLQAVGIVTDVGDFLPLLARELDKLEK
>gnl|CDD|441520 COG1916, COG1916, Pheromone shutdown protein TraB, contains GTxH motif (function unknown) [Function unknown]
MDESPITRIELDGKEIILLGTAHVSQESVEEVREVIEEEKPDAVAVELDESRYQALKDPDAWKDLDIFKV
IKEGKAGLLLANLALSAFQKRLGEQFGIEPGAEMKAAIEAAEERGAPVALIDRDIQITLKRAWRNMGFWE
KLKLLAGLIASLFSREEISEEEIEKLKEGDVLEALFEEFAEFSPKLKEVLIDERDAYLAHKLREAPARGK
KVVAVVGAGHLPGIERYLEEPETLPDLAELEEVPPKSRWPKIIGWLIPALILALFALGFFSGGLELGLQA
LLSWVLINGGLAALGALLAGGHPLSILTAFVAAPLTSLNPLIAAGWFAGLVEAWLRKPTVGDFERLRDDV
TSLKGWWRNRVFRVLLVFALTNLGSSIGTFIAGFRILRLLFG
>gnl|CDD|441521 COG1917, QdoI, Cupin domain protein related to quercetin dioxygenase [General function prediction only]
MRLAEIALTGVSVRVLADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDV
VFIPPGVPHAFRNLGDEPAVLLVVFSPGL
>gnl|CDD|441522 COG1918, FeoA, Fe2+ transport protein FeoA [Inorganic ion transport and metabolism]
MTLSELKPGEKARIVRISGDGELRRRLLELGLVPGTEVEVVRKAPLGGPLVVRVGGTRIALRREEAAKIL
VEP
>gnl|CDD|441523 COG1920, COG1920, 2-phospho-L-lactate guanylyltransferase, coenzyme F420 biosynthesis enzyme, CobY/MobA/RfbA family [Coenzyme transport and metabolism]
RAVVPVKRLARAKSRLSPVLSPEEREALARAMLRDVLAALLAAGGVDRVVVVTTDPEAAALARALGAEVL
VDPPERGLNAAVNAALAAARERPADPVAVLPADLPLLTPADLAALLAAARAGDVVIVPDRDGGGTNALLA
RPPDPFRPRFGGGSFARHRAAAARAGLSVEVVDSPRLRLDVDTPEDLVELLLHGVGPHTAAYLRS
>gnl|CDD|441524 COG1921, SelA, Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis]
AAEVEARLSALERPGLRPVINATGTVLHTNLGRSPLSEEAVEAVAEAARGYSNLEYDLETGKRGSRYDHV
EELLCELTGAEAALVVNNNAAAVLLALAALAAGKEVIVSRGELVEIGGSFRIPDVMALSGAKLVEVGTTN
RTHLRDYEAAITENTAALLKVHTSNYRIVGFTEEVSLAELAELAHEHGLPVIVDLGSGSLVDLSKYGLPH
EPTVQEYLAAGADLVTFSGDKLLGGPQAGIIVGKKELIERIKKNPLGRALRVDKETLAALEATLRLYLDP
EKAAEEIPTLRMLTRPQEELRARAERLAEALNALLGVTVEIVPDESQVGGGSLPVEELPSAAVALDPAGL
SAEELAKALRRGDPPIIGRIEDGRLLLDLRTLLPDEEEIIAEALRELLA
>gnl|CDD|441525 COG1922, WecG, UDP-N-acetyl-D-mannosaminuronic acid transferase, WecB/TagA/CpsF family [Cell wall/membrane/envelope biogenesis]
MPRVNILGVPVDALTMEEAVERILEALEEGRPGYVVTANAEHLMLARRDPELREALNRADLVLPDGIGVV
WAARLLGRPLPERVTGSDLMPALLERAAEKGLRVFLLGGKPGVAEKAAANLRQRYPGLRIAGTHHGYFRF
PEEEEAIIERINASGPDILFVGLGAPKQEKWIARNRDRLPVAVIIGVGGAFDFLAGTVKRAPRWMQRLGL
EWLYRLLQEPRRLWRRYLLPNPLFLLLVLRQKLR
>gnl|CDD|441526 COG1923, Hfq, sRNA-binding regulator protein Hfq [Signal transduction mechanisms]
MKKPINLQDQFLNQLRKERIPVTIFLVNGVKLQGKIKSFDNFTVLLERDGKQQLVYKHAISTIVPAR
>gnl|CDD|441527 COG1924, YjiL, Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism]
QGMIYLGIDIGSTTTKAVLLDEDGEILASAYLPTGGDPLEAAKEALKELLEEAGLKREDIAGVVATGYGR
VLIGAAFADKVVTEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKLEDGVVVDFAMNDKCAAGTGRFLEVM
ARRLGIPIEEFGELALKAKNPVDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVGI
GEPVVFQGGVAKNDGVVRALEKELGKEVIVPPIPQLMGALGAALLAREKVKKGK
>gnl|CDD|441528 COG1925, PtsH, HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport and metabolism]
MLEREVTIVNKLGLHARPAAKLVQLASKFDSEITVEKGGKEVNAKSIMGLMSLGAKKGDEVTITAEGPDA
EEALDALAALIESGFGEE
>gnl|CDD|441529 COG1926, COG1926, Predicted phosphoribosyltransferase [General function prediction only]
MFRDRTDAGRQLAERLAAYRGEDPVVLALPRGGVPVAAEVARALGAPLDVLVVRKIGAPGNPELAIGAVA
EDGVVVLNEDLIRRLGISEEYIEAEKAREREELERRRRRYRGGRPPPDLKGRTVILVDDGIATGATMRAA
LRALRRQGPARIVVAVPVAPPDTLEELRREADEVVCLETPEPFRAVGQFYEDFPQVSDEEVIALLAQAR
>gnl|CDD|441530 COG1927, Mtd, F420-dependent methylenetetrahydromethanopterin dehydrogenase [Energy production and conversion]
VVKIGIIKLGNIGTSVVIDLLLDERADREDIEVRVVGSGAKMGPEEAEDVVEKLKEWDPDFVIVISPNAA
APGPTKARELLKESDIPCIIISDGPGKKEAKDALEEQGFGYIIVKADPMIGARREFLDPVEMASFNSDVL
KVLATTGAFRLVQEELDKVIEQVKAGKSEIELPKIVITPEKAVEAAEFSNPYAKAKAMAALEIAEKVADI
NVKGCFMTKELEKYIPTVASAHEMMRAAAKLADEAREIEKSNDTVLRTPHAKDGKLLSKTKLMEKPE
>gnl|CDD|441531 COG1928, PMT1, Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones]
MTAALPPARLVPPMPGDRLRGWLGTLLVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNGYERNWP
DPGPFFVVHPPLGKWLIALGEWLFGYVNPFGWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLAL
DGLHLVLSRTALLDIFLMFFVLAAFGCLLLDRDQVRRRLAAAVAAGRAPSRWGPRLGFRWWRLAAGVLLG
LACGVKWSGLYFLAAFGLLTVAWDAGARRAAGVRRPWLGALLRDGIPAFFALVIVPLLTYLASWTGWFAS
DTGYDRHWAAQNPGSGLGWVPDALRSLWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYYETGQT
GTLGCGAGKCVRAVLAIGNPALWWLGLPALLWLLWRWIARRDWRAGAVLVGYAAGWLPWFLYLDRTMFFF
YAIPFVPFLVLALALVLGLILGPARASERRRLGRLVVGLYVGLVVANFAFFYPILTGLPIPYDEWQARMW
FPSWI
>gnl|CDD|441532 COG1929, GlxK, Glycerate kinase [Carbohydrate transport and metabolism]. Glycerate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
KIVIAPDSFKGSLSALEVAEAIAAGIRRVFPDAEVVKLPMADGGEGTVDALVAATGGERVTVTVTGPLGR
PVEASYGLLGDGKTAVIEMAAASGLPLVPPEERNPLLTTTYGTGELIRAALDAGARRIIIGLGGSATNDG
GAGMLQALGARFLDADGRELPPGGAALARLARIDLSGLDPRLAEVEITVACDVDNPLLGPNGAAAVFGPQ
KGATPEMVEELDAALAHFADVLERALGKDVADIPGAGAAGGLGAGLLAFLGAELRSGIDLVLELLGLDEA
LAGADLVITGEGRLDSQTLHGKAPAGVARLAKKAGVPVIALAGSLGDDAEELYEAGIDAVFSIVDGPMSL
EEALANAAELLERAAENIARLLK
>gnl|CDD|441533 COG1930, CbiN, ABC-type cobalt transport system, periplasmic component [Inorganic ion transport and metabolism]
MKKKKKNLLLLLLVVALAVLPLFLGGGAEFGGADDQAEEAIEEIAPDYEPWFEPLWEPPSGEIESLLFAL
QAAIGAGVIGYYLGYYRGRRKARKEAEDA
>gnl|CDD|441534 COG1931, COG1931, Predicted RNA binding protein with dsRBD fold, UPF0201 family [General function prediction only]
DVRVEAPVRPTEDEDKVLDAIRNIFPEEELEIEEGGGYKRIVGESDLHSLEKFHELLREQRILDTARSVL
FKGIKGDTFSFMLNKQAAFVGRVSFVVGEESPLGPIHVTVEVDDPVERVIDWLAPPTEDGRPVDEDDMPD
D
>gnl|CDD|441535 COG1932, SerC, Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and metabolism]. Phosphoserine aminotransferase is part of the Pathway/BioSystem: Serine biosynthesis
MRVYNFSAGPAKLPEEVLEQAQAELLDWNGSGMSVMEMSHRSKPFKAIVEEAEADLRELLGIPDGYEVLF
LQGGATAQFAMVPMNLLRGGKKADYLVTGEWSKKAIKEAKKYGEVNVVASSEDDNFGYIPKPEEWQLSPD
ADYVHYTSNETITGVEFHELPDVGDVPLVADMSSDILSRPVDVSKFGLIYAGAQKNIGPAGLTVVIVRPD
LLGRAERAIPSMLDYKTHADNDSMYNTPPTFAIYLAGLVLKWLKEQGGLAAMEKRNAEKAALLYDWIDAS
DFYTNPVDPEDRSRMNVTFDLADEELDAAFLAEAKAAGLVGLKGHRSVGGMRASIYNAMPLEGVEALVDF
MDEFERRH
>gnl|CDD|441536 COG1933, PolC, Archaeal DNA polymerase II, large subunit [Replication, recombination and repair]
EEVKEAELEEELAEEGEEEIAAELGAERAGEARAGLAAELEAKVRAVLKLLEAAAALEAGIDAEAGAGAL
ALTEGVVAAAGQGAEAAAIKAAGGGAVEGSIVRRGGGGRVRGGEAEEEALAGEVRRKVLEIEDYDRLSEV
DEEVREEELLLAEEEDEEEEEEEEVEDEEADEVEEDDEEEGGLGLELRALVLVVGRDLKADKAEGGNVLL
TDLDGEGEEGEDDEGDEGKDEDGEEAVLRDEGGGPLEPLVGGRVGDLAREKGGTLAALVAGGGRILAGLL
LGDGAVTLGEALGVAVVGGAPSEGGGVGLEGVVVVLRGGSLVVLGVVAAVKITGRVEEEIVVKEEDDLDE
REIDLDDELLGPGEPEELLVAELLEEPDGEELSGEVEEEEEELDELEEEAEESREEGDEDEEELTEREED
ALSLKLELERELEGLLTEEEEELLELLEELLLELLDEELEDELILELLILLEEEEEEELILDLLLELDLS
ELKKGLKLLSDREVAPFDLESGGLVALKSRMVRPRRRERRDLSDRRRTLEPAGEVGPPIGDVGLLGRGLR
GAADTDLKEAAGVGLFKEPILRLECCECGEPSCEICIECGLEKPYCLICCCPDESGRDECPCCGCGREPS
TSSRKDFPLKKRLAAAEENGRERALDPLKGVKGLTSRDKTPEPLEKGILRAKHDVSVFKDGTVRYDMTDL
PLTHFRPSEIGVTVEKLRELGYTEDILGKPLESEDQLVELKVQDIIISEDAAEYLLRVAKFIDDLLEKYY
GLEPFYNAEDREDLIGHLVIGLAPHTSAGVVGRIIGFTLAVVGYAHPYFHAAKRRNCDGDEDCVMLLLDG
LLNFSRSFLPDKRGGLMDAPLVLTSRIDPSEIDDEAHNMDVVSRYPLEFYEATLEMADPKEVEDLIDIVE
DRLGTDGQYEGFGFTHDTSDIAAGPDLSAYKTLGSMMDKMDAQLELARKIRAVDETDVAERVIESHFLPD
LIGNLRAFSRQEFRCLKCGAKYRRMPLTGKCRKCGGNVILTVHEGSVNKYLETAKKVAEEYDVRDYTKQR
LEILERSIESLFENDKNKQSGLADF
>gnl|CDD|441537 COG1934, LptA, Lipopolysaccharide export system protein LptA [Cell wall/membrane/envelope biogenesis]
LLLLALLLLLLAAPALAQKADRDQPIEIEADRLEVDDKKGTAVFTGNVVVTQGTLTLRADKLVVYYDKAG
GIERIEATGNVTFRQKRDGGQEVEATADRAEYDVATDTVVLTGNAVLTQGGNTVTGDRITYDLKTGRATA
EGGGGGGRVRAVLQPKQKKDKKPA
>gnl|CDD|441538 COG1935, COG1935, Uncharacterized conserved protein, DUF473 domain [Function unknown]
MEYAALTGISRRVIEELKRNRLRTIELRSAHNFFALLKLNPGDLVFLTSVSLEDLTRGTEGIIAEVLKIE
ISTHRVVQSGDLYYEEREMTAARIQLKLVGLGRVREVKSNEIGKPTKVDVEEISCYEAG
>gnl|CDD|441539 COG1936, Fap7, Broad-specificity NMP kinase [Nucleotide transport and metabolism]
MRIAITGTPGTGKTTVAKLLAERLGLEVIHLNDLVKEEGLYTEVDEERDSLVVDEDALAEELEELKEGDV
IIEGHLAHLVDVDRVIVLRCNPEVLEERLEERGYSEEKIRENVEAEALDVILSEAVERFGEEKVYEIDTT
GRTPEEVADEILAIIKGEREPSPGSVDWLEYLE
>gnl|CDD|441540 COG1937, FrmR, DNA-binding transcriptional regulator, FrmR family [Transcription]
HEDKKKLLNRLKRIEGQVRGIIRMIEEDRYCIDILTQLAAVRSALNKVGLELLEDHLRHCVVEAIESGDR
EEKIEELLKLLK
>gnl|CDD|441541 COG1938, COG1938, Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]
EPDLEGPVLIEGFPDAGLVGSIATDHLIETLDMEEVGSIDSDELPPVVTFEDGRPRPPLRLYANEDRDVL
LLVGDVPEPPRRWEEFAAAVLDWAEELGVSEVVSLGGIPADVPHTRPIVTGVATDEELLERLEEGIEPLE
EGVPTGILGLLLNEAEERGIPAVGLLAEVLAQSPDPKAAAALLEALEKLLGLDIDTDELLEEAEEIEEQI
EELAEQDEEARAEEQYDAELPEEMYL
>gnl|CDD|441542 COG1939, MrnC, 23S rRNA maturation mini-RNase III [Translation, ribosomal structure and biogenesis]. 23S rRNA maturation mini-RNase III is part of the Pathway/BioSystem: 23S rRNA modification
SEKDVKQLSPLALAYIGDAVYELYVRTYLLLKGNTKVNDLHKLAVKYVSAKAQAKLLRKLLPLLTEEELD
IVRRGRNAKSGTVPKNADVQTYRYATGFEALIGYLYLTGQTERLEELLELAIEEIEEEEK
>gnl|CDD|441543 COG1940, NagC, Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription]
NPDAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAELIEELLAEAGISRGRILGI
GIGVPGPVDPETGVVLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLT
LGTGIGGGIVINGKLLRGANGNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELGGAEKLTA
EELFAAARAGDPLALEVLDEAARYLGIGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPA
REDPRIVPASLGDDAGLLGAAALALE
>gnl|CDD|441544 COG1941, FrhG, Coenzyme F420-reducing hydrogenase, gamma subunit [Energy production and conversion]
MAKPKVATYWLAGCSGCQLSFLDLDERLLDLLELVEIVYFPEASDVKEIPEPVDVALVEGSIRNEENEER
LKEIREKSKILVALGACAVTGGIPALRNLYDLEELLERVYGETPSTNPQIPGEELPELLDRVRPLSEVVK
VDYELPGCPPDPDQILEVLTALLEGRLPELPGYSVCVECKRRENVCLLVQGYPCLGPVTRAGCGALCPSA
GRPCRGCRGPTEDDNGAALLSALASLGLDDEEILREFYRFNLPASLLREKVK
>gnl|CDD|441545 COG1942, PptA, Phenylpyruvate tautomerase PptA, 4-oxalocrotonate tautomerase family [Secondary metabolites biosynthesis, transport and catabolism]
PIINIKLFEGRTPEQKRALAKAVTDAVVEVLGKPPESVSVVIEEVPPENWGIGGKLLS
>gnl|CDD|441546 COG1943, RAYT, REP element-mobilizing transposase RayT [Mobilome: prophages, transposons]
MARSRRLHVPGLTYHITFRTKYRRPVFTDDEDRERLLELLREIAERYGVEILAYVLMPDHVHLLVTLPPD
LSLSKIMRRLKGRSSRRINRRYLREGHLWQRRYFAHTVGDEADLLTIRRYIHNNPVRAGLVEEPEDWP
>gnl|CDD|441547 COG1944, YcaO, Ribosomal protein S12 methylthiotransferase accessory factor YcaO [Translation, ribosomal structure and biogenesis]
VVSPEETLERVRPLLSPLGIGRVADITGLDRLGIPVYSAVRPNARAAGALSVSQGKGLTPEQARASALME
AIERYSAERQGDEPLVRASYAELGAEDRALDPEDLLLPSDESPFDPDRPIDWVPGWDLTSGEPVLVPAEA
VYYPYPLPPPGPRFFRASSNGLAAGNTLEEAILHGLLELIERDAFALWWYNRLPGPRIDLDSFDDPALRE
LLDRFRAAGIEVWLLDLTSDLGVPVVAAVARDPDGDPPLLAFGAGAHLDPEIALLRALTEAAQSRLTFIS
GARDDLPAEYRRAADYERVRRLEDHAYLDASGPTVPFADLPDLSTDDLREDLAALLDRLAAAGLDVLVVD
LTRPDLGLPVVRVIVPGLEPFTFGFDRGGPRLYDVLAEAELNPAPFP
>gnl|CDD|441548 COG1945, PdaD, Pyruvoyl-dependent arginine decarboxylase [Amino acid transport and metabolism]
PKKIFITKGVGEGPTELNAFDAALLDAGIGNYNLVRVSSILPPGAEIVPVEEGPDLLPPGAILPVVYARI
TSNEPGELIAAAVGVAIPKDPSGPGYISEHHGFGTEEEAEEYAEDMAAEMLALRGWEIGETKVITVEARV
EKDGCWTTAVAAAVLWYS
>gnl|CDD|441549 COG1946, TesB, Acyl-CoA thioesterase [Lipid transport and metabolism]
ALMELLDLLDLERLEDGLFRGEISPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDG
PIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELLIAGVL
PLRFFAFLRPFDIRPVEGPLPFAPPSGEPRQRVWMRARDPLPDDPLHAALLAYASDATPPATALLSWLGP
PLPAASLDHAMWFHRPFRADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR
>gnl|CDD|441550 COG1947, IspE, 4-diphosphocytidyl-2C-methyl-D-erythritol kinase [Lipid transport and metabolism]. 4-diphosphocytidyl-2C-methyl-D-erythritol kinase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
SLTVKAPAKINLFLHVTGRRPDGYHELETVFQFIDLGDTLTIEPADDGSISLTGPGAGVPTDEDNLVYRA
ARLLQEATGIPPGVDIHLEKRIPVGAGLGGGSSDAAATLRALNRLWGLGLSREELAELAAKLGADVPFFL
YGGTALAEGRGEKLTPLPPLPELWLVLVKPGVGVSTAEVYRALDLTRDTPPPDIDALLAALAAGDAALAA
LLRNDLEPVAFKLYPEIAEVLEALLEAGALAARMSGSGSTVFGLFEDEEAAEAAAAALPARGGVFVARTL
N
>gnl|CDD|441551 COG1948, MUS81, ERCC4-type crossover junction endonuclease [Replication, recombination and repair]
PVRIVVDSREKNSGVPRLLSRLGVEVRVKTLEVGDYVVSDRVAVERKTVRDFVNSLIDGRLFEQASRLAE
AYERPVLIIEGDLLYEERNIHPNAIRGALASLALDFGIPVLPTRDAEDTAELLVTLARREQEEEKREVSL
HGKKKPKTLREQQLYVVESLPGIGPKLARRLLEHFGSVEAVFNASEEELMKVEGIGEKTAERIREVLDSE
YKGE
>gnl|CDD|441552 COG1949, Orn, Oligoribonuclease (3'-5' exoribonuclease) [RNA processing and modification]
DDNLVWIDLEMTGLDPETDRIIEIATIVTDSDLNILAEGPVLVIHQSDEALDGMDDWNRRMHTKSGLIDR
VRASTVTEAEAEAQTLAFLKQHVPAGKSPLCGNSIGQDRRFLARYMPELEAYFHYRNLDVSTLKELARRW
YPEVLAGPKKKGGHRALADIRESIAELRYYREHFFVL
>gnl|CDD|441553 COG1950, YvlD, Uncharacterized membrane protein YvlD, DUF360 family [Function unknown]
MMRFLIRWLVNALALLIAAYLLPGIEVDSFGTALIAALVLGLLNALVKPILVLLTLPLTILTLGLFLLVI
NALMLWLAAWLVPGFHVDGFWAALLGALVLSIVSSLLSSLLGDDKD
>gnl|CDD|441554 COG1951, TtdA, Tartrate dehydratase alpha subunit/Fumarate hydratase class I, N-terminal domain [Energy production and conversion]. Tartrate dehydratase alpha subunit/Fumarate hydratase class I, N-terminal domain is part of the Pathway/BioSystem: TCA cycle
MREIDPEDLTEAVAELIIEASYYLPPDVLEALKEALEKEESPNAKDVLAQILENAEIAAEGKLPICQDTG
TAVVFVKIGQDVPIDGDLEEAINEGVRRAYKEGPLRKSVVDPLTRKNTGDNTPAVIHIEIVPGDKLEITV
APKGGGSENKSALKMLNPSEGLEGVKKFVLETVKEAGGNPCPPGIVGVGIGGTAEKAAKLAKKALLRPLD
ERNPDPRLAELEEELLEAINKLGIGPQGLGGKTTALDVKIERAPRHIASLPVAVNINCWATRHATAVIDG
DGPFELESP
>gnl|CDD|441555 COG1952, SecB, Preprotein translocase subunit SecB [Intracellular trafficking, secretion, and vesicular transport]
MAEENNAAQQQQQPQFQIQRQYVKDLSFENPNAPAIFQEQWQPEIDVQLNVNARKLAENVYEVVLTVTVT
AKLGDKTAFLVEVKQAGIFTIRNIPEEQLEPLLGIECPRILFPYAREIVSDLVRRGGFPPLMLAPINFDA
LYQQRLQQQAAQAAAAQA
>gnl|CDD|441556 COG1953, FUI1, Cytosine/uracil/thiamine/allantoin permease [Nucleotide transport and metabolism, Coenzyme transport and metabolism]
MTETETATDEAPAPGYDPRLYNEDLAPTPAEKRTWGWYNIFALWMGMVHSVPGYTLAAGLFALGLSWWQA
LLALLLGNLIVLVPMNLNGHAGTKYGIPFPVLARASFGVRGANIPALLRGLIAIGWFGIQTYLASQALDA
LLLKLFPGLASLGGAHSFLGLSALGWISFLLFWALQLLIFWRGMEAIRKFEDWAGPLVYVVMLALAIWAL
SKAGGFGPILSLPSKFLSGGAFWAVFFPALTLMVAYWATLALNFPDFTRFAKSQRAQVRGQFLGLPVNML
LFSFIGVVTTSATVVVFGEAIWDPVELVARIDSPFAVVLALLTFLIATVGINIVANFVSPAYDFSNLFPK
KISFRRGGLITAVIGLLITPWNLYNSPEGIFYFLGGLGALLGPVFGILIADYYLVRRQRLDVDDLYSEDD
GRYWYRNGWNPRAVIALVVGAVISLAGALVPALAPLYDYSWFVGAALGGVLYLALMRRRPRAV
>gnl|CDD|441557 COG1954, GlpP, Glycerol-3-phosphate responsive antiterminator (mRNA-binding) [Transcription]
LAENPIIPAVRDLKDLEKALKSDVEVIFLLNGDIGNLKSIVKRLKQAGKKVFVHIDLIEGLSNDEYGIEY
LKQEIKPDGIISTKSNLIKAAKKEGLLTIQRLFLIDSSALETGIKLIEKSKPDAIEILPGIMPKVIKEIK
KETGIPIIAGGLIRTKEDVEAALAAGAIAVSTSNKELW
>gnl|CDD|441558 COG1955, ArlJ, Archaellum biogenesis protein ArlJ/FlaJ, TadC family [Cell motility]
RYLLLILLPLALFFLLVVLGLILGLLLPLLVFLLAVIYPKLKASSRKRKIDNDLPYAVTYMYALSTGGLS
RREIFRRLAEEEEVYGELAKEFRRIVRLVDLWGYDLLTALRRVAKRTPSDLLADFLDRLASVLRSGGDLE
EFLESEQETLMEEYETEYERALETLELLAELYVTLLVSGPLFLIIILVVPILTGGDSLTLLLLLVYLLIP
LVSLGFIVLIYTLLPKDPIWYRLKELRSPEQTLIRNPYRALAISVPLALVLVLLLLLLGFGLTPPVDLPD
DLLLAALLTPLLPPGIVAEREERKIKKRDEEFPDFLRALGSSNEAGLTLEEALKTLARKDFGPLTPEIRR
LYKRLNLGIDLTRALRRFAARTGSPLIQRFVELLVDAIEAGGDPKEVGEILASNAERLVLLRRERRQSMR
TYVGVIYGLFAVFLFILVILLEIFLDLLAGLSTSLASASSAAGGLGSFGSIDVELLRYLFFHAILIQALL
SGLVAGKVGGGSIAAGLKHSVILLWIGYVVFIVVP
>gnl|CDD|441559 COG1956, MsrC, GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, Signal transduction mechanisms]
EATSKEEDYDELLAQLSALLAGETDLIANLANISALLFEALPDYNWVGFYLVDGGGELVLGPFQGPPACT
RIPFGKGVCGTAAAEGETQLVPDVHAFPGHIACDSASRSEIVVPIFKDGEVIGVLDIDSPTPGRFDEEDQ
AGLEALAALLAEALDA
>gnl|CDD|441560 COG1957, URH1, Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]. Inosine-uridine nucleoside N-ribohydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARP
LVRPLVTAEHVHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPEL
AERIKRIVIMGGAFFVPGNVTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALG
TPLGRFLADLLDFYLDFYRERYGLDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRG
VTGRPPNARVALDVDAERFLDLLLERLARL
>gnl|CDD|441561 COG1958, LSM1, Small nuclear ribonucleoprotein (snRNP) homolog [Transcription]
MSERPLKVLEKSLGKRVLVKLKDGREYRGKLKGYDQHMNLVLEDAEEIDDGEVVRKLGTVVIRGDNVVFI
S
>gnl|CDD|441562 COG1959, IscR, DNA-binding transcriptional regulator, IscR family [Transcription]
RLSTKTDYALRALLYLALHPGGEPVTSKEIAERQGISPSYLEKILQKLRKAGLVESVRGPGGGYRLARPP
EEITLGDVVRAVEGPLALVECVSGPPDCPVEEACALHGVWEEAEDAILEVLDSVTLADLVEDAEAREVAE
R
>gnl|CDD|441563 COG1960, CaiA, Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]. Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELA
LVLEELARADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTA
VRDGDGYVLNGQKTFITNAPVADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGE
LFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAV
QHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLER
LYRDARILTIYEGTNEIQRLIIARRLLGRPG
>gnl|CDD|441564 COG1961, SpoIVCA, Site-specific DNA recombinase SpoIVCA/DNA invertase PinE [Replication, recombination and repair]
MMRAAGYARVSTDDQEGLSLERQREALRAYAEKAGWEIVRIYVDEGVSGTSKDRPGLQRLLADLRAGKFD
TLVVWKLDRLGRNLADLLELVEELKERGVRLISLTEGIDTSTPMGRLLLTILAAFAEFERELISERTRAG
LAAAKARGKYLGRPPYGYRDPKKLVIDEEEAEVVRRIFELYLEGKSLREIARELNERGIPTWSRSTVYRI
LKNPVYGGLGVYGLGKKIVTEKGERKVRRRRKRRVIREEEERVRRRELAAKRARRLLKGKLLRGLRGRKK
RGGGRKRRRGGGRRLCGRLGRLRKGGRLRRCRLGRRLKASARKLARGKLKEALLLEVLLELLELLLDLAL
LLLLEELAALLELLAAELELELEEERAQALLELKLLLL
>gnl|CDD|441565 COG1962, MtrH, Tetrahydromethanopterin S-methyltransferase, subunit H [Coenzyme transport and metabolism]
FKFDKEQEVYDIGGVKIGGQPGEYPTVLIGSIFYNGHKIVEDEKKGIFDKEAAEALINRQEELSDETGNP
AMVDIVGETPEAMKKYIDFVAEITDAPFLIDSSVPEVRIAAAKYATEIGLADRAIYNSINMSIKEEEIEA
LKESDVKAAIVLAFNPMDPSVEGRMKILEEGGGGQDKGLLEIAEECGIENPLVDTAVTPLGSGSGFSARA
ILAVKAKFGYPVGSAPHNAPSAWKWLREKKKEEAFAACDAGSNLVAQTLGADFILYGPIENAPEVFPAVA
MADIMIAEAAKDLGGEPPDENHPLNKLF
>gnl|CDD|441566 COG1963, YuiD, Acid phosphatase family membrane protein YuiD [General function prediction only]
MEILSNRPLLAALLAWFVAQFLKVIINLIKTRKFDWSLLFSTGGMPSSHSALVTALATAVGLTEGFDSPL
FAIAAVFALIVMYDAAGVRRAAGKQAKILNQLIEELFQLVEEKIKEERLKELLGHTPLEVFVGALLGILV
ALLLYFLF
>gnl|CDD|441567 COG1964, MoaA2, C-terminal domain of the GTP 3',8'-cyclase MoaA, radical SAM superfamily (molybdenum cofactor biosynthesis) [Coenzyme transport and metabolism]
KTRPYLFYETTTSLCPECLKVVDAKIVEEDGKVYMEKRCPEHGEFRDLYWSDAEYYRRFEEYNKPGEGPL
NFNTETEYGCPYDCGLCPDHEQHTCLALIEVTNRCNLNCPICFANSGPGYGYEPSLEEIEKMLDALVREE
GEPDVVQFSGGEPTVHPDLFEILDLAKERPIKHVMINTNGIRIAKDPDFAERLAEAGPLFEVYLQFDGLS
DEPYRRLRGADLLEVKLKAIENLRKAGISTTLVPTLVKGVNDHEIGDIIRFALQNPCVRGVTFQPVAFAG
RIPQFDPEEDRITLPDVRRLIEEQTDGLFTPEDFYPVPCCHPHCGAMTYALKDGGKVIPLTRFIDVEGLL
EGLANTIAFEEDKALLKKSLPKLFSESKSPESIAENLKDLLCCLPKGVEALAELHENVFRIGIMHFMDAY
NFDVERVKKCCIHYVTPDGRIIPFCTYNLFLYRDEVEEKFSKPLREWKARRKE
>gnl|CDD|441568 COG1965, CyaY, Fe-S cluster assembly protein CyaY, frataxin homolog [Inorganic ion transport and metabolism]. Fe-S cluster assembly protein CyaY, frataxin homolog is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MTESEFHQLADALLEAIEEALDRDDDADIDCERSGGVLTLEFDNGSKIIINRQEPLRQIWLAAKSGGFHF
DYDDGKWIDTRSGEELFALLSRALSEQAGEPVTLAA
>gnl|CDD|441569 COG1966, CstA, Carbon starvation protein CstA (peptide/pyruvate transporter) [Energy production and conversion, Amino acid transport and metabolism]
MNALWLVLAALVIYAIGYRFYGKFIARKVFGLDPNRPTPAHRLNDGVDYVPTNKWVLFGHHFASIAGAGP
IVGPILAAQFGWLPALLWILIGNVFAGAVHDFGALFASVRNDGKSIGEIAGKYIGKRAGVLFLIFIFLLL
LLVLAVFALVVANALANSPWAAFTVALTIPIAILMGLYLYRLPGNVLEASIIGVVLLYLAIVLGPYVPFT
LSGTTWVIILFVYGFIASVLPVWLLLQPRDYLSSFLLIGMIIGLAIGIIIANPEIQMPAFTGFVDGTGPV
GAGPLFPFLFITIACGAISGFHSLVSSGTTSKQLDNESDARFVGYGGMLGEGFLALMALIAATALFPGVY
AAYESLAAAAGVGGGAPTFAVGMANILSGLGIPMAFGYHFAILFVALFALTTLDTGTRLGRFMLQELFGI
VQLKRTKWLPNRYVATAIAVALWGYLLYGGGINTLWPLFGIANQLLAALALLTATVWLIKMGKYAWVTLI
PMVFMLVVTLTALLWKLFSNFLPAFGNYLLAILAAILLVLALIL
>gnl|CDD|441570 COG1967, COG1967, Uncharacterized membrane protein [Function unknown]
RIGEFIYKYYIGPIVAVALPGYTAVPTLTYAVILLLALYGVYALLRRLDIPVDRRFVLALAPFMLLGGAL
RVLEDAGAIPPPLSPLFITPAIYFTVFVVAGAALLVSVLLERAGLVDRYERPLAAVGTVALVVTLGYLLW
LGLTTGTFYPFVPVIVLVLATVVTALTWLLLRRFAPEVNAGTGPLGLLVVFGHALDGVSTAVGIDWLGYG
EKHPVPRAIIEFTGALPTAELTGTAWLFVLVKLAVALPVVWLFNEYVEESPRLANLLLIAVAAVGLGPGT
RNMLRFTFGV
>gnl|CDD|441571 COG1968, UppP, Undecaprenyl pyrophosphate phosphatase [Lipid transport and metabolism]
MDLLQAIILGIVQGLTEFLPVSSSGHLILVPALLGWEGDPGLAFDVVIQLGTLLAVLVYFRKDILRLLRG
LFRSLRRDDPDARLALLIIVATIPAAIIGLLFKDFIESLLRSPLVVAIALIVGGLLLLLAERLGRRKRTL
EDLTLKDALLIGLAQALALIPGVSRSGATITGGLLLGLSREAAARFSFLLAIPAILGAGLLELLKLLKAL
SSVDLGPLLVGFVVAFVVAYLAIKWLLRYLKRHSFKPFAIYRIILGIVLLILLLL
>gnl|CDD|441572 COG1969, HyaC, Ni,Fe-hydrogenase I cytochrome b subunit [Energy production and conversion]
MSETVRKLKRVYVWEAPVRLWHWVNALCIVVLSVTGYYIGSPPPSPSGEASDHFVMGYIRFIHFAAAYIF
AVGFLGRLYWAFVGNRYARWLFFIPLWNKKWWKELWEELRWYLFLEKEPPKYVGHNPLAQLAYFGFFLLS
LFMIVTGFALYGEGLGPGSWAPTLFGWVIPLFGGSQDVRTWHHLGMWLIIAFVIIHVYAAIREDIMSRQG
IISSMISGWKFFKDDRPP
>gnl|CDD|441573 COG1970, MscL, Large-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis]
MLKEFKEFAMRGNVIDLAVGVIIGAAFGKIVTSLVNDIIMPLIGLLTGGVDFSNLFIVLKGAVKEAGAVT
INYGAFINAVINFLIIAFVIFLVVKAINKLKKKEEAAPAAPAPPKEEELLTEIRDLLKAQRC
>gnl|CDD|441574 COG1971, MntP, Putative Mn2+ efflux pump MntP [Inorganic ion transport and metabolism]
MSLLELLLLAIALSMDAFAVSIAYGLRKKRIRIALRIALIFGLFQALMPLLGWLLGSLLSGYIGAVAHWI
GFLLLILIGLKMIYEALKEEEEEEPKSGRISGKELLLLAIATSIDALAVGISLALLGVNILLTALLIGLV
TFIMSFLGVLLGRRLGSLLGKKAEILGGLILILIGLKILL
>gnl|CDD|441575 COG1972, NupC, Nucleoside permease NupC [Nucleotide transport and metabolism]
MNILIGLLGIAVLLGIAWLFSENRKAINWRTVGIGLALQLLLAFLVLKVPAGRAAFEALSDGVNKLLSYA
NEGTAFVFGGLAGPGLPGGFVFAFQVLPPIIFFSALISILYYLGILQFIVRGIGWVLSKILGTSGAESLS
AAANIFLGQTEAPLVIKPYLAKMTRSELFTVMTGGMATVAGSVLAAYASMLGVPAKYLLAASVMAAPAAL
LIAKILVPETEEPETDGVVEVEEEKEPANFIDAIAEGALDGLKLALNVGAMLIAFVALIALVNGILGGLG
GLFGGLSLQRILGYLFAPLAWLIGVPWSEALQAGSLMGTKLVLNEFVAYLDLAKLLAGALSPRTVAIVTY
ALCGFANFSSIGIQIGGIGALAPERRSDIARLGLKALLAGTLASLLSATIAGLFLG
>gnl|CDD|441576 COG1973, HypE2, Hydrogenase maturation factor HypE [Posttranslational modification, protein turnover, chaperones]
MDIEGFARRGLRKGADEPELEEKLADRILEIKNISREYARRLAKAVIEEVKNTLGLKGDLLTYPPSGVTM
GEFGVGSRGTGDFYAHRKIAEIIGSTSAVVDSDELDDAGVVKAGGVYIVVTVDGIHSRLSDFPFLAGFHV
TRATLRDVYVMGARPVALLSDIHVADDGDVAKIFDYTAGITAVSELTGVPLVTGSTLRIGGDMVIGDRMT
GCVGAVGVSEHLTARKQARPGDVILMTEGAGGGTISTTALYYGMHDVVDETINIKFLKACEALLESGLLK
EIHAMTDVTNGGIRGDAHEISKTAGVRLVFDEEKIRSLVNPRVLEMLEDLEIDYLGVSLDSLLIIAPPEV
AEEIIRVVRSAGVKIDEIGRVEEGGGAVLIVDGEERDFTPRFRESAYTPIKKVVGEETPRDFEEMKKKVD
RAAEEAIEKKERVVERLKKKG
>gnl|CDD|441577 COG1974, LexA, SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms]
MKKLTKRQREILDFIKEYIRERGYPPSQREIAEALGLSSSAVHRHLKALEKKGYLRRDPGKSRAIELLPA
SPEVVGLPLLGRVAAGFPIPAEENIEEYLDLPEELVKNPGATFALRVKGDSMIDAGILDGDLVIVDRQLE
AENGDIVVALIDGEATVKRLYKEGGRVRLQPENPAYPPIIIEGDDVEILGVVVGVIRRL
>gnl|CDD|441578 COG1975, XdhC, Molybdoenzyme maturation factor PaoD (Mo cofactor insertion), XdhC/CoxF family [Posttranslational modification, protein turnover, chaperones]
RDVLEALAALLAAGEPVVLATVVETRGSAPREPGAKMLVTADGRIAGTIGGGCLEADVIERAREALADGE
PRLLRYGLGPEDAWDLGLCCGGTVEVLLEPLDAADALAALAAALAAREPVALVLDLAGGLGEDGVFVEVL
GPPPRLLIFGAGHVARALARLAAALGFRVTVVDPRAEFAPPERFPGADEVVADDPEDALAALALDPGTAV
VVLTHDHALDLAALEAALRSPAAYIGLIGSRRKRARRRERLREEGVSEAQLARLHAPIGLDIGAKTPEEI
AVSILAELIAVRRGASGAALREA
>gnl|CDD|441579 COG1976, TIF6, Translation initiation factor 6 (eIF-6) [Translation, ribosomal structure and biogenesis]. Translation initiation factor 6 (eIF-6) is part of the Pathway/BioSystem: Translation factors
MIRRLSVFGSPNIGVYARANDKYALVPPDLPEKKVEKIEEVLGVEVIETTIAGSRLIGSLAVGNSNGILV
PSIVTDEELERLKEALDLNVEVLPSKITALGNLILANDKGALVHPDLSDEAVKKIEDVLGVEVVRGTIAG
VKTVGSAAVATNKGVLVHPDATDEELKFLEDVLKVPVDVGTVNFGSPFVGSGLVANSKGYLVGEDTTGPE
LGRIEDALGFI
>gnl|CDD|441580 COG1977, MoaD, Molybdopterin synthase sulfur carrier subunit MoaD [Coenzyme transport and metabolism]. Molybdopterin synthase sulfur carrier subunit MoaD is part of the Pathway/BioSystem: Molybdopterin biosynthesis
KVTVRYFAALREAAGKSEEEVELPEGATVGDLLEALAARYPGLAERLLRRRVRVAVNGEDVRLDTPLKDG
DEVALFPPVAGG
>gnl|CDD|441581 COG1978, YkuK, Predicted RNase H-related nuclease YkuK, DUF458 family [General function prediction only]
MMFWSPTKGELSFEEVFEDIKEFIEKEPKAGYKLIIGTDSQVKGGETKFVTAIVIHRVGKGARYFYRKKR
ERKIRSLRERIFYETSLSLEVASKLTELLKKYGGADLELEIHLDIGTNGKTRDLIKEVVGYVEGMGFEAK
IKPDSFAASSVADKYTK
>gnl|CDD|441582 COG1979, YqdH, Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]
MNNFTFYNPTKIIFGKGQIAKLGEEIPKYGKKVLLVYGGGSIKKNGLYDQVKAALKEAGIEVVEFGGVEP
NPRLETVRKGVELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDILTGKAPVEKALPLGTVLTLP
ATGSEMNSGSVITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDA
PLQDRFAEGLLRTLIEEGPKALKDPEDYDARANLMWAATLALNGLIGAGVPQDWATHMIEHELSALYDID
HGAGLAIVLPAWMRYVLEEKPEKFAQYAERVWGITEGDDEERALEGIEATEEFFESLGLPTRLSEYGIDE
EDIEEMAEKATAHGMTALGEFKDLTPEDVREILELAL
>gnl|CDD|441583 COG1980, FbpA, Archaeal fructose 1,6-bisphosphatase [Carbohydrate transport and metabolism]
MKITLSVIKADIGGVGGHTRPHPELLEAAEEVLAEAKKKGLLIDFYVTHCGDDIQLIMTHTKGVDNEEIH
GLAWDAFKEATEVAKELKLYGAGQDLLKDAFSGNVKGMGPGVAEMEFEERPSEPVIVFMADKTEPGAFNL
PLYKMFADPFNTAGLVIDPSMHDGFRFEVMDVYEHKKVELSTPEELYDLLALIGAPGRYVIKRVYSKSDG
EIAAVVSTERLNLIAGKYVGKDDPVAIVRAQSGFPAVGEVLEPFAFPHLVAGWMRGSHNGPLMPVSLNDA
VPTRFDGPPRVIALGFQLKEGKLVGPVDLFDDPAFDYARRKALEIADYMRRQGPFEPHRLPPEEMEYTTL
PAVLEKLKDRFED
>gnl|CDD|441584 COG1981, HemJ, Protoporphyrinogen oxidase HemJ (unrelated to HemG or HemY) [Coenzyme transport and metabolism]
LYLWLKALHIIAVVSWFAGLFYLPRLFVYHAEADDGSEERERFKIMERRLYRIIMTPAMILTWVFGLWLL
FLYGWLSAGWLHAKLALVLLLSGYHGWCGRLLKRFAAGRNTRSHRFYRIFNEVPTLLLIAIVILVVVKPF
>gnl|CDD|441585 COG1982, LdcC, Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]
YMDQLLTPLFDALKKYAERGPVSFHVPGHKGGRGFGREFYDFFGENVFRLDLTELPGLDDLHDPEGVIKE
AQELAAEAFGADRTFFLVNGTSSGNKAMILAVCGPGDKVLVPRNCHKSVIHGLILSGAIPVYLNPEIDNE
LGIIGGITPEAVEEALIEHPDAKAVLITNPTYYGVCYDLKAIAELAHEHGIPVLVDEAHGAHFGFHPDLP
RSAMEAGADLVVQSTHKTLGALTQSSMLHVKGGRVDHERVNEALMLLQSTSPSYLLMASLDVARRQMAGE
GEELLDEALELAIEARKEINKIPGLYVFGPEDLGAPGVYDLDPTKLTIDVPGLGISGYEVAEYLREEYGI
QVELADLYNILFLLSLGDTKEDIERLVAALKELKRLYDKNAPLEEVLPLAFPPLPELVMSPREAFFAETE
LVPLEEAVGRIAAEMVIPYPPGIPLLMPGERITEEVIDYLRALEEAGGRFPGFEDPELRTIRVVKE
>gnl|CDD|441586 COG1983, PspC, Phage shock protein PspC (stress-responsive transcriptional regulator) [Transcription, Signal transduction mechanisms]
RKKLYRSRDDRVIAGVCAGLAEYFGIDPTLVRLIFVLLTLFGGAGILLYLILWLLLPEAPTAAEK
>gnl|CDD|441587 COG1984, PxpC, 5-oxoprolinase subunit C/Allophanate hydrolase subunit 2 [Amino acid transport and metabolism]
MMLEVLKPGLLTTVQDLGRPGYQHLGVPPSGAMDRLALRLANRLVGNPEGAAALEITLGGPTLRFEEDTV
IALTGADMPATLDGRPVPPWRPVAVKAGDVLTLGAPRAGARAYLAVAGGIDVPPVLGSRSTDLRAGLGGL
EGRALQAGDVLPLGAPAAAAPGRGLPAELLPGEEVTLRVVPGPQDDWFTEEAIERFFSSEWTVTPQSDRM
GYRLEGPPLERAHPSEILSEGIVPGAIQVPPDGQPIVLLADRQTTGGYPKIATVISADLPRLAQLRPGDT
VRFVP
>gnl|CDD|441588 COG1985, RibD, Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]. Pyrimidine reductase, riboflavin biosynthesis is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
TGRPYVTLKLAMSLDGKIATADGESKWITGEAARRDVHRLRARADAILVGAGTVLADDPSLTVRLPGLGR
QPLRVVVDSSLRLPPDARLFDDAAPTLVLTTEAADAERRAALEAAGAEVIVLPGDGRVDLAALLAALAER
GIRSVLVEGGPTLAGSFLAAGLVDELILYIAPKLLGGDGPTLVGGPGLETLADAPRLRLVSVRRLGDDLL
LRYRPRR
>gnl|CDD|441589 COG1986, YjjX, Non-canonical (house-cleaning) NTP pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism, Defense mechanisms]
KVAVGSTNPVKINAVEEAFERLFPNAEVEGVDVPSGVSDQPMGDEETRQGAINRARNALEAADADFGVGL
EGGVDEFEGGLYLFAWAAVIDGDGRVGIGRSASFPLPPEVAERLLQGEELGPVMDELFGTENIKQKGGAI
GLLTNGLVTRTDLYEQAVILALIPFLNPELY
>gnl|CDD|441590 COG1987, FliQ, Flagellar biosynthesis protein FliQ [Cell motility]
MTPELVIDLGRQALWTALLLSAPLLLVALVVGLVISIFQAATQIQEQTLSFVPKLLAVLLVLLLLGPWML
STLVDFTRRLFSRIPGLI
>gnl|CDD|441591 COG1988, YbcI, Membrane-bound metal-dependent hydrolase YbcI, DUF457 family [General function prediction only]
MDSLTHILLGAALGAAALGRKLGPALSRAALLAGALGSLLPDIDVPKSKLGRRLSDPISYLFGHRGFTHS
LLFLLLLALLLALLLRLLFPKASFLRLFLAFFLGYLSHLLLDALTSYGVQLLWPFSKKRFALPLIFIKTA
IDPLLTLLLLAGLLLALLL
>gnl|CDD|441592 COG1989, PulO, Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, Intracellular trafficking, secretion, and vesicular transport]
MEPLLLILLAFLLGLLIGSFLNVVIYRLPRGESIVFPRSHCPHCGHPLRWYDNIPVLSYLLLRGRCRYCG
APISLRYPLVELLTGLLFLLLALRFGLSLQLLAALLLLSLLLALSFIDLDTQLLPDSLTLPLLWLGLLLS
LLGGFVSLLDALLGALAGYLLLWLIYWLFKLLTGKEGMGGGDVKLLAALGAWLGWQALLLILLLASLLGA
LVGLILLLLGRKGRKTPIPFGPFLALGGLIALLFGDQIISWYLGLF
>gnl|CDD|441593 COG1990, Pth2, Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]
MEMKQVIVVRKDLKMSKGKLAAQVAHAAVSAALDALKKDKEWFEEWKDEGQKKVVLKVNSEEELFELKEK
AERLGLPTALIRDAGLTELEPGTVTCLGIGPAPEEKIDKITGDLKLL
>gnl|CDD|441594 COG1991, MJ0832, Uncharacterized conserved protein MJ0832_1, predicted component of type IV pili-like system, UPF0333 family [General function prediction only]
MTSLKFIKSNRGQISLEFSLLVLAILLAAIITSYYLIPSSYGAGKSNIDSIALLAKAAVSKLKTVLVAAA
DEGTRKTVYLKYPPGTWDGNNIEIYIYIGNGVNGTSNNYNFVKNYTIIVVTIPPKEVNVVVNWND
>gnl|CDD|441595 COG1992, COG1992, Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) [General function prediction only]
GGGGGGGADAKTAAALGAGGGGTTTAVTVTATTTVTGVGSDPPPPVEVQQQAVAADDDVDDAKTGMLMTA
TIVEVVAVVVKSRDKPLVVVVVPVAVAAAGLGLLLAEAELAKLLLPLLATVTPNEPEVEELLLPTIRSLL
AEARAARLALQEEGADALGVKGGHVSGDAVVDVLEDERDVETFRHPRLVTEATHGSGCTFSAAIAALLAK
GLSLEEAVRGAKLFLLHAIRYGLLVGKGVGPVNHLADLRLEAERERVLEEVRRALERLESNEGFAKLIPE
VGSNLVYALPYARSIEDVAAVPGRIVRVGGRVTVVGPPEFGASSHVARVLLAAMKFDPEIRAAINIRYDE
EILEALEDLGLKVVEFDREEEPEEVEGSTMPWGIAEAIEKAGDVPDVIYDRGGVGKEPMIRVLGRDAEEV
VEKVLEILRRLA
>gnl|CDD|441596 COG1993, COG1993, PII-like signaling protein [Signal transduction mechanisms]
KLLRIYIGESDRHGGKPLYEAIVERARELGIAGATVFRGIEGFGAHGRLHTARFLELSDDLPVVIEIVDT
EEKIERFLPRLDELVKDGLVTLEPVEVGRYG
>gnl|CDD|441597 COG1994, SpoIVFB, Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, protein turnover, chaperones]
MGIPVRLHPSILIFALALFLSVLLHELAHALVARRLGDPTAKITLNPLKGGWAKINRNFRNPRDEALVAL
AGPLANLLLALLFALLLRLLPALGLGPLALLLGYLALINLVLAVFNLLPIPPLDGGRILRALLPRRTARR
ATRLEPYGFLILLLLIFLGLLLGNIWLSPLLNLLI
>gnl|CDD|441598 COG1995, PdxA, 4-hydroxy-L-threonine phosphate dehydrogenase PdxA [Coenzyme transport and metabolism]. 4-hydroxy-L-threonine phosphate dehydrogenase PdxA is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
TKPRIAITMGDPAGIGPEIILKALADPRILELCRPVVIGDPKVLERAAKQLGLDLPLREIDSPAEAAANP
GTLNVLDVGNDAAPVEPGKPSAAAGRAALESLERAVELALAGEIDALVTAPINKEAINAAGFPFPGHTEF
LAELTGTKDVVMMLAGEGLRVALVTTHIPLRDVPDAITPERILETIRLLHRALRRDFGIAKPRIAVAGLN
PHAGEGGLFGREEIDIIAPAIEAARAEGIDVSGPLPADTLFHRAARGEYDAVLAMYHDQGLIPLKLLGFD
RGVNVTLGLPFIRTSVDHGTAFDIAGKGIADPGSLIAAIRLAARLARNRR
>gnl|CDD|441599 COG1996, RPC10, DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]. DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger is part of the Pathway/BioSystem: RNA polymerase
EAMVEYKCPRCGAEVELDEGTPAIRCPYCGSRIFIKERPPVVKRVKAI
>gnl|CDD|441600 COG1997, RPL43A, Ribosomal protein L37AE/L43A [Translation, ribosomal structure and biogenesis]. Ribosomal protein L37AE/L43A is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MMKKTKKVGSAGRFGPRYGRKLRKRVADIEEKMRAKHTCPECGSKRVKRVATGIWECRKCGYKFAGGAYV
PETPAGKTVGRAIKRAT
>gnl|CDD|441601 COG1998, RPS27ae, Ribosomal protein S27AE [Translation, ribosomal structure and biogenesis]. Ribosomal protein S27AE is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MAKGKKAAVHEYYKVEDGKIKRKRKFCPRCGSGVFMAEHKDRWHCGKCGYTEFKKK
>gnl|CDD|441602 COG1999, Sco1, Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones]
MRRTLTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGGDDVQVLFISVDPERD
TPEVLKAYAEAFGAPRWIGLTGDPEEIAALAKAFGVYYEKVPDGDYTFDHSAAVYLVDPDGRLRGYYPAG
EDPEELAADLKALLEE
>gnl|CDD|441603 COG2000, COG2000, Uncharacterized Fe-S cluster-containing protein [General function prediction only]
MIGKTWLLPGLNCGACGYKTCRDFAAAVYQGKAELEMCPFYMRERFESNSNLVVEELPNGGDILGVEADF
VLYPLPGEPSAREIFLPFRPDEKLEIKKGDIIRGRPLGAGCPITHFAKVLEYDPVTGLITVHVVGPLHRR
GGEEKEVKDLGAYKVEAFEGIVEVIGKQPKVGQRIRFLPGHCMMQKVHSGLVGEVTAETEGLRVRIEGID
LK
>gnl|CDD|441604 COG2001, MraZ, MraZ, DNA-binding transcriptional regulator and inhibitor of RsmH methyltransferase activity [Translation, ribosomal structure and biogenesis]
MFLGTYEHKLDAKGRLSIPAKFRDVLAEELGGGLVLTRGLDGCLELYPLEEWEKLEEKLEALPLFSPEAR
DFQRLFLGGATEVELDKQGRILIPPNLREYAGLEKEVVLVGAGNRFEIWDPEAWEAYLAEAEEDFAELAE
ELGD
>gnl|CDD|441605 COG2002, AbrB, Bifunctional DNA-binding transcriptional regulator of stationary/sporulation/toxin gene expression and antitoxin component of the YhaV-PrlF toxin-antitoxin module [Transcription, Defense mechanisms]
MKTVKVTSKGQITIPKEIREALGIKEGDKLEVIVDGDGIVLKPVKPPVEELRGLLKGLSLEELEEAIREA
>gnl|CDD|441606 COG2003, RadC, DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, recombination and repair]
MKIKDLPHRERPRERLLAKGAAALSDAELLAILLRTGTPGKDAVELAKELLARFGSLRGLLRASVEELRK
IKGIGEAKAAQLKAALELGRRLLREELEERPVISSPEDVADYLRARLAHLPREVFRVLFLDTKNRLIADE
ELSIGTLNHTPVYPREVFKRALRLNAAAIILAHNHPSGDPEPSRADIELTRRLKEAGELLGIRLLDHIII
GDGGYVSFAEEGLL
>gnl|CDD|441607 COG2004, RPS24A, Ribosomal protein S24E [Translation, ribosomal structure and biogenesis]. Ribosomal protein S24E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MEIEILEERENPLLNRREVKFTVTHEGATPSRKEVREKLAAMLNVDKELVVVDKLKTEFGKGESKGYAKV
YDDEERAKKIEPEYILKRNKIKEEEEE
>gnl|CDD|441608 COG2005, ModE, DNA-binding transcriptional regulator ModE (molybdenum-dependent) [Transcription]
MSMKLRLKLWLELDGGVFLGPGRIELLEAIDETGSISAAAKAMGMSYKRAWDLIDAMNNLLGEPLVERQT
GGKGGGGARLTPEGRRLLALYRRLEAEAQRALAALFEELFALLRSKTS
>gnl|CDD|441609 COG2006, COG2006, Uncharacterized conserved protein, DUF362 family [Function unknown]
MSKKVAIVRCEDYEVREAVREALELLGGIERFVKPGDRVLIKPNLLWAKPPEKGATTHPEVVEAVVRLLK
EAGAKEVIVGDSPGVGDTRKVYEASGYEEVAEELGVELVDLNEERYVEVEIPGGKVLKELRIAKPVLEAD
VVINLPKLKTHGQTTVTLAVKNLFGVVPGLEKAEFHRREDLHEMIADLARAIKPDLTIVDGIVGMEGNGP
SGGTPRELGLILASTDPVALDAVAARLLGFDPEEVPYLRLAAERGLGTGDLEDIEIVGEPLEEVRVKDFK
LP
>gnl|CDD|441610 COG2007, RPS8A, Ribosomal protein S8E [Translation, ribosomal structure and biogenesis]. Ribosomal protein S8E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MMIWQGRSTRKPTGGRKRPARKKRKYELGREPTETKVGEEKRKIVRVRGGNTKVRLLRANYANVADPKTG
KVKKAKILNVVENPANPNYVRRNIITKGAIIETELGKARVTSRPGQDGVVNAVLIEE
>gnl|CDD|441611 COG2008, GLY1, Threonine aldolase [Amino acid transport and metabolism]
MMIDFRSDTVTGPHPEMLEAMAAANVGDDVYGEDPTVNRLEERVAELFGKEAALFVPSGTMANQLALRAH
TRPGDEVICHETAHIYVDEGGAPEALSGVKLLPVPGEDGKLTPEDLEAAIRPGDVHFPQPGLVSLENTTE
GGTVYPLEELRAIAAVAREHGLPLHLDGARLFNAAAALGVSLAEITAGVDSVSFGLTKGLGAPGGAVLAG
DPEFIEEARRWRKRLGGLMRQAGFLAAQGLAALEDDLERLAEDHAMARRLAEGLAALPGVRVPEPVETNI
VFVILPDELAERLREKGVLFYPWGPGAVRLVTHWDTTEEDVDAFLAALAELLA
>gnl|CDD|441612 COG2009, SdhC, Succinate dehydrogenase/fumarate reductase, cytochrome b subunit [Energy production and conversion]
AEVKKNRPLSPHLQIYRLPLTMIVSILHRITGVALFLGLPLLVWWLAASASSPEAFAAVQAFLGSPLGKL
VLLGLTWALLYHLLAGIRHLLWDFGYGFELETARRSAWVVLVLSVVLTVLLGVVLWGL
>gnl|CDD|441613 COG2010, CccA, Cytochrome c, mono- and diheme variants [Energy production and conversion]
GGLLGGALGALLGGGGLSDEGAGAAGAGGVAAAGAGLAGALVDGAAAAAALGAAAAAAAAAAALALALLL
ALLLAAAAADAPAADAEALARGKALYEQNCAACHGADGKGGLGAAPNLTDDALYGGDPEALVETILNGRP
GGAMPAFGGQLSDEEIAALAAYLRSLSGN
>gnl|CDD|441614 COG2011, MetP, ABC-type methionine transport system, permease component [Amino acid transport and metabolism]
MLTMWSELWPLLLQATGETLYMVGVSTLIAVLLGLPLGVLLVLTRPGGLLPNPVLYRVLGVIVNIFRSIP
FIILLVALIPLTRLIVGTSIGTTAAIVPLTIAAIPFFARLVENALREVDPGVIEAAQAMGASPWQIIFKV
LLPEALPSLILGLTVTLISLIGYSAMAGAVGGGGLGDLAIRYGYQRFDTDVMLVTVVILIVLVQIIQFLG
DRLARRLDHR
>gnl|CDD|441615 COG2012, RPB5, DNA-directed RNA polymerase, subunit H, RpoH/RPB5 [Transcription]. DNA-directed RNA polymerase, subunit H, RpoH/RPB5 is part of the Pathway/BioSystem: RNA polymerase
MMKKFNVLDHELVPKHEILSEEEAEEVLKEYGIKPEQLPKIKASDPAVKAIGAKPGDVIKIIRKSPTAGE
AVYYRLVVEG
>gnl|CDD|441616 COG2013, AIM24, AIM24 protein, required for mitochondrial respiration [Energy production and conversion]
DYEIEGPNFQVLEVELDPGESVIAEAGAMVAMSGNVDFETKMGDGGLLGALKRALTGESLFLTTFTAEGG
PGEVALAPPYPGDIIVLDLDGESIIVQKGAFLAAESGVEIDIKFQKGLGAGLFGGEGLFLLKLSGTGTVF
LHSYGEIIELELAPGEPLVVDTGHVVAWSGSLDYDIERVGGLKSSLFSGEGLVATFTGPGKVWVQSRELS
>gnl|CDD|441617 COG2014, COG2014, Uncharacterized conserved protein, contains DUF4213 and DUF364 domains [Function unknown]
LELYDELIDELLPRLEDLTVEDVVIGLGWTLVELSDGSVGLAYTPLEETRSCALPWAGDLIGKPARELAE
LLLSWNPLERSLGLAAINALSNSPLDAEPKGLEDGDAFDLLPIKKGKKVAVVGYFPPLLEKLRKKGAELT
VLERNPRRPGDLPDPAAEELLPEADVVIITGTTLVNKTLDRLLELAKNAREVVLVGPSTPLLPELFFGYG
VDALAGVVVTDPDRALRAIAEGGGTRHFGKGVRKVVLKL
>gnl|CDD|441618 COG2015, BDS1, Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism]
TAPKPASEATAAANAAVAKSLPFEDTQDFEDARRGFIATLDDLVIRNADGRVVWDLDAYDFLEDGDAPDT
VNPSLWRQAQLNNIHGLFEVTDGIYQVRGFDLANMTFIEGDTGWIVIDPLTSVETAAAALALYRKHLGDR
PVKAVIYTHSHVDHFGGVRGVVDEEDVKSGKVPIIAPEGFMEHAVSENVYAGNAMGRRAQYMYGTLLPRG
PKGQVDAGLGKTTSTGTVGLIPPTDTITKTGEELTIDGVRMEFQLTPGTEAPAEMNFYFPDFKALCMAEN
ATHTLHNLYTLRGAQVRDALAWSKYLDEALELFGDRAEVMFASHHWPTWGNERIVEYLTNQRDAYKYLHD
QTLRLANQGYTPDEIAEVIKLPPSLAKDWYTRGYYGSVSHNVKAVYQRYLGWYDGNPANLNPLPPEEAAK
RYVEAMGGADAVLAKARAAFDAGDYRWAAELLNHLVFADPDNQEARELLADALEQLGYQAESATWRNFYL
TGALELRHGVPKSPTPNTASPDMIAAMPTEMLFDYLAVRLDGPKAAGKDLTINLIFTDTGEKYLLELRNG
VLTYRKGPQADDADATLTLTRADLLALLLGKTTLDDLVASGGAKVEGDAAALARLLGLLDPFDPDFNIV
>gnl|CDD|441619 COG2016, Tma20, Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ribosomal structure and biogenesis]
KVMKRHHLSKKEIKELLEELEERLGVDLSGDNVEVAETDDFEIYLVDGEPLLFKVDDEPFPTLRGLLKYP
PEKPVVTVDMGAVKFVSNGADVMRPGIVEADGEIKEGDIVVIVEEKHGKPLAVGRALVDGEEMVEGKKGK
AVKNLHHVGDKLWE
>gnl|CDD|441620 COG2017, GalM, Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism]
MITEPDGELYTLENGGLRAVIPEYGATLTSLRVPDKDGRDVLLGFDDLEDDPPWAYGGAILGPYANRIAD
GRFTLDGKTYQLPINEGPNALHGGARDRPWEVEEQSEDSVTLSLTSPDEEGYPGNLELTVTYTLTDNGLT
ITYTATNLGDKPTPFNLGNHPYFNLPGEGGGDIDDHRLQIPADEYLPVDEGLIPTGELAPVAGTPFDFRE
PRPLGDGGFDHAFVGLDSDGRPAARLTDPDSGRRLEVSTDEFPGLQVYTGNFLDPGRDGVCLEPQTGPPD
APNHPGFEGLIVLAPGETYSATTRIRFSV
>gnl|CDD|441621 COG2018, COG2018, Predicted regulator of Ras-like GTPase activity, Roadblock/LC7/MglB family [Signal transduction mechanisms]
EQAEKLDWLLDDLVERVPGVRGAVLVSADGLLIASSLGLDDDDAERLAAMAAGLLSLARRAARELGAGEV
EQVVVEGERGYLLVTAAGDGAVLAVLADPDADLGLVRYEMRRLAERLGELLTP
>gnl|CDD|441622 COG2019, AdkA, Archaeal adenylate kinase [Nucleotide transport and metabolism]
VLNKVREKLKEDYKIVNFGDVMFEVAKEEGLVKDRDEMRKLPVEEQKELQKEAAEKIAEMAKEGNVIIDT
HAVIKTPGGYLPGLPKWVLRELNPDVIVLIEADPEEILRRRLKDPTRKRDIESEEEIEEHQDVNRAAAMA
YAVLTGAPVKIVENREGKLEEAAEELVEVLRK
>gnl|CDD|441623 COG2020, STE14, Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein turnover, chaperones]
MGLVLILLGLLLRLWAVLTLGRSWTTLVPPRKAHRLVTTGPYRYVRHPMYLGFLLLLLGLALLLGSLLAL
LLALLLLLLYVLRIRREERRLRARFGEEYRAYAARVPRLIPRL
>gnl|CDD|441624 COG2021, MET2, Homoserine O-acetyltransferase [Amino acid transport and metabolism]. Homoserine O-acetyltransferase is part of the Pathway/BioSystem: Methionine biosynthesis
GPLTLESGATLPPVTLAYETYGTLNADKSNAVLICHALTGDSHAAGPHPPDDPKPGWWDGLIGPGKAIDT
DRYFVICSNVLGGCYGSTGPASINPATGKPYGLDFPVVTIRDMVRAQKRLLDHLGIERLAAVIGGSMGGM
QALEWAVSYPDRVRRAIVIATAARLSAQNIAFNEVQRQAIRADPNWNGGDYYDGEGPRRGLALARMIGHI
TYRSDDELNRKFGRRLQDGEDPFGFDGRFQVESYLRYQGEKFVRRFDANSYLYLTRAMDYFDLGRGRGSL
AAALARIKARFLVISFTSDWLFPPEESREIAEALPAAGKDVSYAEIDSDYGHDAFLLEIEQLGPLIRAFL
ARIAR
>gnl|CDD|441625 COG2022, ThiG, Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and metabolism]. Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis
MMDDPLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPGGDNLLDYLDPLGVTL
LPNTAGCRTAEEAVRTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPV
LAKRLEDAGCAAVMPLGAPIGSGLGLLNPYNLRIIIEQADVPVIVDAGIGTPSDAAEAMELGADAVLLNT
AIARAGDPVAMARAFKLAVEAGRLAYLAGRMPKRDYASASSPLTGFLHQ
>gnl|CDD|441626 COG2023, RPR2, Ribonuclease P protein subunit RPR2 [Translation, ribosomal structure and biogenesis]
IARERIEILFELAEEAAREGNPELARRYVELARRIAMKYRVRLPRELKRRFCKKCDAPLVPGVNARVRLK
GGRVVITCLECGWIRRYPYK
>gnl|CDD|441627 COG2024, SepRS, O-phosphoseryl-tRNA(Cys) synthetase [Translation, ribosomal structure and biogenesis]. O-phosphoseryl-tRNA(Cys) synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
MRFDPEEIKELARKDFEKAWHEGKEVLKPPGLNERYPRLKYEYGKPHPVFDTIQRLREAYLRMGFDEMMN
PLIVDEQEVYKQFGPEALAVLDRCFYLAGLPRPNVGISDERIEKIEEILGRDISEEEIEKLRKILHAYKK
GEIDGDDLVHEISEALNVDDALVVKILDEVFPEFKELKPESSRLTLRSHMTSGWFITLSSLWERKPLPIK
LFSIDRCFRREQAEDASRLMTYHSASCVIADEDVTVDDGKAVAEGLLSQFGFEKFRFRPDEKRSKYYVPD
TQTEVYAYHPKLDGWVEVATFGIYSPTALAEYGIPYPVMNLGLGVERLAMILYGAEDVREMVYPQFYEWE
LSDRELARMIKVDEVPVTPEGREIARAIVETCEEHADEPSPCEFLAWEGEFFGRNVKVYVVEPEENTKLC
GPAAFNEVVVYDGNILGVPDTEKWKEAFEEGVSTGIRYIDAFAALAAARIEEAAASGETETEVRVRIVKS
PSDINLKIEELAMRYITSKNKKIDVRGPVFLTVRAEIE
>gnl|CDD|441628 COG2025, FixB, Electron transfer flavoprotein, alpha subunit FixB [Energy production and conversion]
GVLVFAEHRDGELKPVSLELLGAARELADKLGGEVTAVVLGAGVEALAEELAAYGADKVLVVDDPALAHY
LAEPYAAALAALAEKYKPEIVLAPATTRGRDLAPRVAARLDTGLTADCTALEIDGGGLVATRPAFGGNAM
ATIKCPDDPQVATVRPGVFEPAEPDGSATGEVEEVEVELDEADLRVKVVEREEKASGRVDLTEADVVVSG
GRGLGSKENFELLEELADALGAAVGASRAAVDAGWLPHDRQVGQTGKTVAPKLYIAVGISGAIQHLAGMK
DSKTIVAINKDPEAPIFKVADYGIVGDLFEVVPALIEALKKRK
>gnl|CDD|441629 COG2026, RelE, mRNA-degrading endonuclease RelE, toxin component of the RelBE toxin-antitoxin system [Defense mechanisms]
MYKVEFTPRALKDLKKLDKKVQKRIKKKIEELAENPRPGGKKLKGSLKGLYRLRVGDYRIIYEIDDDELV
VLVLAIGHRRDVYRK
>gnl|CDD|441630 COG2027, DacB, D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]
LLALLLLLALLASAAALPAALDALLADPGLGGASVGVVVVDLDTGEVLYSRNADRPLTPASTMKLLTTAA
ALELLGPDYRFKTTVYADGTIRDGVLNGNLYLVGGGDPTLSSEDAAGLWDLAAQLKAAGIRRINGDLVLD
DSLFDGPALAPGWFWDDLGRGYGAPPSALMVNENAVRLTLRPGAAGGPARVSVEPPLAGVTIDNQVKTAA
GSGDTLDVYRAPGGNRLVLTGTLPAGCGEFTLSLAVPDPALYAARAFAAALAAAGITVTGKVRRGTAPAG
ARLLAEVQSPPLAELVRDMNKESDNLYAEALLRTLGAERTGAPGSFAGGAAAVRAFLAELGIDTSGLVLV
DGSGLSRYNRVTARALAQLLQAAARSPWLPEFLASLPVAGVDGTLRNRFKGTPAAGRVRAKTGTLTGVSA
LAGYVTTADGRRLAFSILVNNYNASAAEARAALDALLAALARCG
>gnl|CDD|441631 COG2028, ASCH, ASCH domain, putative RNA-binding protein, DUF365 family [General function prediction only]
MKVIFYASREDQGFVGEAEIERVEYFENPMEILEKYGDRLFLTEEELRKYERDRKRWGSRGRRKKPWLVL
ELENIKKYKRVVKPKRFITVGGKYLTEDEYEEIRRQD
>gnl|CDD|441632 COG2029, COG2029, Uncharacterized conserved protein, DUF366 domain [Function unknown]
MKTIFLEEEIDYDGSQLRPLWAYRNFGIQGDSIVVFRGPCRVKLENMVDLEDVLAKKPIYSDDMLHFIVE
HFDVPDLEKAVLRQRLLVAIIKEVLEEYGGVKLRRDGDDLYVDGKKLSVSIATASPVSTKIHLGINVTSE
GTPVPAVGLEDLGIEDIEELAERVASAYAEEIEKIELDRCKVRGVP
>gnl|CDD|441633 COG2030, MaoC, Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism]
YFEDLEVGDVLPHGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDL
PGTAVANLGLQEVRFLRPVRVGDTLRARVEVLEKRESKSRGIVTLRTTVTNQDGEVVLTGEATVLVPRRP
>gnl|CDD|441634 COG2031, AtoE, Short chain fatty acids transporter [Lipid transport and metabolism]
MLARLGRFFTRLVERYLPDPFVFAILLTLVVFVLALVLTGASPLAVVKAWGDGFWSLLTFTMQMALVLVT
GYALASSPPVKRLLDRLASLPKTPRQAIVLVALVSMLASWINWGFGLVVGALLARELARRVKGVDYPLLV
AAAYSGFLVWHGGLSGSAPLLIATPGHFLEKIIGVIPTSETIFSPYNLVIVAVLLVVLPLLNYLMAPKEE
EVVTIDPELLVDEEEEAAKETAPMTPAERLENSRLLSLLIGLLGLAYLVYYFATKGFALNLNIVNFLFLF
LGLLLHGTPRSYLRAVAEAVKSAAGILIQFPFYAGIMGIMTASGLAAVISEWFVSIATPTTFPLFTFLSA
GLVNFFVPSGGGQWAVQGPIVMPAAQELGVDLGKAAMAVAWGDAWTNMIQPFWALPLLGIAGLKARDIMG
YCVVQLLVSGPVISLGLLFLPY
>gnl|CDD|441635 COG2032, SodC, Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism]
MKKLLALLAAAALLLAACAQSAAAAKTATATLVDTGDGKVVGTVTFTETPGGVLVTVELSGLPPGEHGFH
IHEKGDCSAPDFKSAGGHFNPTGTKHGGPNPDGPHAGDLPNLYVDADGTATLEVLAPRLTLGGLNDLDGR
ALIIHAGPDDYSTQPSGNAGARIACGVIKAA
>gnl|CDD|441636 COG2033, SORL, Desulfoferrodoxin, superoxide reductase-like (SORL) domain [Energy production and conversion]
KRLEFYKCEKCGNIVEVVHGGGGPLVCCGEPMELLVANTADAAKEKHVPVIEAEGFGVKVKVGEVPHPMT
EEHYIEWIELYTGDGVGRKELKPGDEPEATFKVKDKSGTLTAREYCNLHGLWESE
>gnl|CDD|441637 COG2034, COG2034, Uncharacterized membrane protein, DUF131 family [Function unknown]
MMGELLVLIGILLIFLGFLLVFLGILLSASKSGKGNVEAGGVIMIGPIPIVFGSSPGIALLALILAIVLM
IIYILLYLLS
>gnl|CDD|441638 COG2035, COG2035, Uncharacterized membrane protein, DUF368 family [Function unknown]
MKRTLKDYLLNFLKGMAMGAADVVPGVSGGTIALILGIYERLIASISSINPKALKLLLRGGFKAAWRKIN
GRFLLPLGIGILIGILSLAKLIEYLLEHYPILTWSFFFGLILGSIPVLYKQIGKWKAKHILALLIGAVLA
FLITFLPPASLSPPNLLFLFLAGAIAICAMILPGISGSFILLLLGLYEPVLDAVSDLDLPVLAVFGLGAV
VGLLLFSKLLSWLLKHYRSATLAFLLGLMIGSLRAIWPWKETLETLLDLPGGDSQLLLAILLFILGIALV
LLLEKLEKKKK
>gnl|CDD|441639 COG2036, HHT1, Archaeal histone H3/H4 [Chromatin structure and dynamics]
ELPVAPVDRIIKKAGAERVSEDAVEALAEILEEYAEEIAKEAVELAKHAGRKTVKAEDIELAAKLLN
>gnl|CDD|441640 COG2037, Ftr, Formylmethanofuran:tetrahydromethanopterin formyltransferase [Energy production and conversion]
MEINGVEIEDTFAEAFPMKATRVIITAATEKWARIAATEATGFATSVIGCGAEAGIERELSPDETPDGRP
GVAILIFAMSKKKLEKQLLNRIGQCVLTCPTTAVFNGLPDAEERIPLGKKLRFFGDGYQISKEIGGRRYW
RIPVMDGEFLCEETTGYVKGVAGGNFLILGRDQAAALAAAEAAVEAIRKVPGVITPFPGGIVRSGSKVGS
KYKFLGASTNDAYCPTLRGKVEDSELPEGVGAVLEIVIDGLDEEAVAEAMRAGIEAACKVPGVVRISAGN
YGGKLGPHHFHLHELL
>gnl|CDD|441641 COG2038, CobT, NaMN:DMB phosphoribosyltransferase [Coenzyme transport and metabolism]. NaMN:DMB phosphoribosyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MSLLEETLPAIPPLDEEAMAAAQARLDNLTKPPGSLGRLEELAVQLAGIQGTLPPRLDRPAVVVFAADHG
VAAEGVSAYPQEVTAQMVRNFLAGGAAINVLARQAGADLRVVDVGVAADLPPLPGLIDRKVARGTGNFAK
GPAMTREEAEAALEAGIEIADELIAAGADLLGTGEMGIGNTTPAAALLAALTGLPPEEVVGRGTGLDDEG
LARKIAVIRRALARHRPDPADPLDVLAKVGGFEIAAMAGAMLGAAARRVPVVVDGFISTAAALVAVRLAP
GVRDYLIFSHRSAEPGHRLALEALGLEPLLDLGMRLGEGTGAALALPLLRAAVALLNEMATFEEAGVSGK
E
>gnl|CDD|441642 COG2039, Pcp, Pyrrolidone-carboxylate peptidase (N-terminal pyroglutamyl peptidase) [Posttranslational modification, protein turnover, chaperones]
MKVLVTGFEPFGGEPVNPSWEAVKRLDGREIGGAEVVAAVLPVVFGKSLEVLVEAIEEHRPDAVLALGQA
GGRAAITIERVAINVDDARIPDNDGNQPIDEPIVADGPAAYFSTLPIKAIVAALRAAGIPASVSNTAGTY
VCNHVMYRLLHLLATKGPPIRAGFIHVPYLPEQAAAKPGTPSMSLEDIVRALEAAIEAALEAL
>gnl|CDD|441643 COG2040, MHT1, Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) [Amino acid transport and metabolism]
MNPLRLPLLMGRILLLDGGMGTELERRGGDLLDPLWSAFALLEAPELVRAVHRDYFAAGADVITTNSYQA
SPDGLAELGYSAEEAERLNRRAVALAREARDEYTPGPPVLVAGSVGPYGDEYRPDYGLSAEEAEAYHRPR
IEALAEAGVDLLAAETIPSLAEAIAIARAAAEAGKPVWISFTVEDDGRLRSGEPLAEAIAAVDTDPGPAA
VGVNCSHPEHFEAALEALAAWTGRPIGVYANAGEMSDAELKTWGGLDDGDPEELAEQAAEWVAAGARIIG
GCCGTGPRHIAAIARALRAAG
>gnl|CDD|441644 COG2041, MsrP, Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and protein-methionine-sulfoxide reductases [Energy production and conversion]
MSIKELSRRRFLKGGALAFPVRTAGGVPEIDPADWRLRVDGLVEKPLTLTLDDLLALPLEERIYRLHCVE
NWSGGVAPWTGVPLRDLLERAGPKPGAKYVLFESADPGYTESLPLDEALDPDTLLAYGMNGEPLPPEHGA
PLRLVVPGLYGFKSAKWLVRIEVTDEDPPGYWETRGYHFYANI
>gnl|CDD|441645 COG2042, Tsr3, Ribosome biogenesis protein Tsr3 (rRNA maturation) [Translation, ribosomal structure and biogenesis]
MKLYVYYLGQDDPKKCTARKLERFGLAKLVRSIRKIPRGGIVLDPFAEKALSPADRDIVEKRGIVALDCS
WEKAEEVFFKRKRGNHRRLPFLLAANPVNYGKPFKLSSVEALAAALYILGEKEQAEEILSKFKWGHTFLE
LNKELLEDYAKAKDSEEIVEIQNEYLDDIL
>gnl|CDD|441646 COG2043, COG2043, Uncharacterized conserved protein, DUF169 family [Function unknown]
MDYKELAEKLKELLRLKTSPVAVKLIKDEEEIPEGVKRPGEKLRHCQAVGMARREGWTVYATAEDLGCPG
GAAALGLKELPEKLKSGELYFGLGYFSSLEAAKRTVEAMPRLPPGKYYAIVVAPLEKAEFEPDVVVIYGN
PAQAMRLVQAYLYKTGGRLEFSFAGNQSVCADATAYPYLTGKPNISLGCSGSRKFGGIEDDEMVVGIPAE
KLEELVEGLEATAKGYPKKRKKAIPKK
>gnl|CDD|441647 COG2044, COG2044, Predicted peroxiredoxin, DsrE/DsrF-like family [General function prediction only]
MAEKLVILLTSGPDDPERATMAFVLAAAAAAMGAEVTIFLTGEGVRLAKKGVAEKIRAPGGPPLADLLEE
AIEAGVKVYVCEPCLKARGLTEEDLIPGVEIAGAADFAELALEADARVLTF
>gnl|CDD|441648 COG2045, ComB, Phosphosulfolactate phosphohydrolase or related enzyme [Coenzyme transport and metabolism]
MKKIRVCLTPELIDPYDLEGDVVVVVDVLRATTTIVTALANGARAVIPVASVEEARALAARLEGALLAGE
RGGLKIEGFDLGNSPLEYTPEVVAGKRLVLTTTNGTRALARAAGAKRVLIGSFLNASAVAEYLLRLAEDV
AIVCAGWKGRFSLEDTLCAGAIADRLLDRLEDVELSDEALAALALYRAAKDDLLEALRQSSHGRRLLRLG
FEEDLEYCAQLDASDVVPVLRDGRLVLASG
>gnl|CDD|441649 COG2046, MET3, ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]. ATP sulfurylase (sulfate adenylyltransferase) is part of the Pathway/BioSystem: Cysteine biosynthesis
MSKLIPPHGGKLVNRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVVE
NMRLADGLLWPIPITLDVSEEDAAGLKEGDEVALRDEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAH
PGVAKLYERGDVYLGGPITLLNRPKHPDFPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQKR
ALETVDGLLIHPLVGETKPGDIPAEVRVRCYEALLENYYPKDRVLLSGLPLAMRYAGPREALLHAIIRKN
YGCTHFIVGRDHAGVGDYYGPYDAQEIFDEFPPGELGIEPLKFEEAFYCKKCGGMATSKTCPHDKEDRVS
LSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQPFGE
>gnl|CDD|441650 COG2047, COG2047, Proteasome assembly chaperone (PAC2) family protein [General function prediction only]
MEEIEIEYDEEPELRDPVLIEGLPGAGHVGKLAAEHLIEELDAEKVAEIYSEEFPPQVVVDEDGTRELPT
NEFYYARPPGGRDLLLLTGDHQPTEPEGWYELCEEVLDIAEELGVRRVYTLGGYLTGEPHTPPPVLGAAT
DEELAEELEEAGVEFSEGYGGIVGASGLLLGLAKLRGIDAACLMGETPGYLVDPKAALAVLEVLEKLLGI
EVDLEELEERAEEMEEVVDELKEMLEEQKDAEQASGEDLAAYL
>gnl|CDD|441651 COG2048, HdrB, Heterodisulfide reductase, subunit B [Energy production and conversion]
MKYAYYPGCSLPGTAPEYEKSTRAVAKALGIELVELPDWNCCGASSAHSVDELLWLALAARNLALAEKMG
LDIVTPCNACYGSLKEANHELKEDPELREKVNEILAEAGLEYKGTVKVRHLLEVLYEDVGLEKIKEKVKK
PLKGLKVAPYYGCHLLRPSEIAGFDDPENPTSLDELVEALGAEPVDYPYKTECCGASLRLSNPEVSLKLT
GKILESAKEAGADAIVTACPLCHLNLDMYQPEINKKFGTEFNIPVLYFTQLLGLALGLSPKELGLDKHIV
DPEPL
>gnl|CDD|441652 COG2049, PxpB, 5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]
MRMAMRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAAL
AARLRALLAELDAAAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGF
PYLGGLDPRLATPRRATPRTRVPAGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPALLRPGD
RVRFVPISEEEFDALRGEV
>gnl|CDD|441653 COG2050, PaaI, Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism]
MSDPLERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSA
LPPGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP
>gnl|CDD|441654 COG2051, RPS27A, Ribosomal protein S27E [Translation, ribosomal structure and biogenesis]. Ribosomal protein S27E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
KKILIPEPRSKFLKVKCPDCGNEQIVFSHASTVVRCLVCGTTLAEPTGGKAKILGEIVEV
>gnl|CDD|441655 COG2052, RemA, Regulator of extracellular matrix RemA, YlzA/DUF370 family [Cell wall/membrane/envelope biogenesis]
LINIGFGNIVSADRIIAIVSPESAPIKRLIQEAKERGKLIDATYGRKTRAVIITDSGHVILSAIQPETIA
QRLEGKEE
>gnl|CDD|441656 COG2053, RPS28A, Ribosomal protein S28E/S33 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S28E/S33 is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MSEVTEEDGVPAEVIEIIGRTGMTGEVTQVRVRILEGRDKGRIITRNVKGPVRVGDILMLRETEREARKL
KKR
>gnl|CDD|441657 COG2054, MfnE, 5-(aminomethyl)-3-furanmethanol-phosphate kinase MfnE (methanofuran biosynthesis) [Coenzyme transport and metabolism]
MSSMWVVKLGGSLLDSPELLEWLAALLAREGGGRVVIVPGGGPFADAVREAQRRWGLDDEAAHWMAILAM
EQYALLLADLLPGLVLADSLAEIRAALARGRIPVLLPYRLLRSADPLPHSWDVTSDSIAAWLAGRLGAER
LVLVKSVDGIEGKISAKELAAFGVVDPAFPRFLAEAGIECYVVNGRDPERLRAALRGEPVVGTLIR
>gnl|CDD|441658 COG2055, AllD, Malate/lactate/ureidoglycolate dehydrogenase, LDH2 family [Energy production and conversion]. Malate/lactate/ureidoglycolate dehydrogenase, LDH2 family is part of the Pathway/BioSystem: TCA cycle
MRVSAEELRALVARVLLAAGVSEEDAAAVADVLVEADLRGIDSHGVARLPRYVERLRAGGINPNAEPEVV
RETPATAVVDGDNGLGQVAARRAMELAIEKAKEHGIGAVAVRNSNHFGALGYYAEMAAEAGLIGIAFTNS
PPLVAPWGGREPLLGTNPIAFAAPRGGGPPFVLDMATSVVARGKIEVAARKGEPIPEGWAVDADGNPTTD
PAAALEGGALLPLGGHKGYGLALMVELLAGVLSGGGFGPEVSSFYDDGGPPGLGHFFIAIDPAAFGGLEA
FKARMDALLDALRASPPAPGGDPVRLPGEREAAARAERLAEGIPLPDALWAELRALA
>gnl|CDD|441659 COG2056, YuiF, Predicted histidine transporter YuiF, NhaC family [Amino acid transport and metabolism]
MNAVVIAVLVMLVLSLLRVNVVLALIIAALVGGLVAGLSLEETISAFIDGLGGGAEIALSYALLGAFAVA
ISKSGLTDLLAKKIIKLLGGEPSKRKTGVKWLLLLILLLMAIMSQNLIPVHIAFIPILIPPLLSVMNKLK
LDRRAVACVLTFGLKAPYMLLPVGFGLIFHGILLDNMNDNGLDVTAADVPKAMAIPALGMVVGLLIAVFI
SYRKPREYEDVEIEGASEEEEVVISTKKIVVALLAIVAALVVQLYTDSLILGALAGFIVFFLTGVIKWKE
ADDVFTEGMKMMAFIGFVMIAAAGFANVLKATGAVESLVESSAALIGGNKALAAFLMLLVGLLITMGIGS
SFSTIPIIAAIYVPLCLSLGFSPLATIALIGTAGALGDAGSPASDSTLGPTSGLNADGQHDHIWDTVVPT
FLHYNIPLLIFGWIAAMVL
>gnl|CDD|441660 COG2057, AtoA, Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism]
AYTTRELMAVRAARELRDGEVVNLGIGLPTLAANLAPLTHAPDVTLQSENGLLGPGPAPLPGSVGDPDLI
NAGKQFFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIGDYDKPGKRLPGMGGAMDLAAGAKRVIV
VMEHSKRKFVEKCDLLTGPGVVDGPRRVITDLAVFDFDPEKGLVLRELHPGVTVEEVQENTGFELIVADD
VPETPPPTEEELALLRELDPTGLRL
>gnl|CDD|441661 COG2058, RPP1A, Ribosomal protein L12E/L44/L45/RPP1/RPP2 [Translation, ribosomal structure and biogenesis]. Ribosomal protein L12E/L44/L45/RPP1/RPP2 is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MEYVYAALLLHEAGKEINEDNLKKVLEAAGVEVDEARVKALVAALEGVDIEEAIKQAAAAPVAAAAAAAA
PAAAEEKEEEKKEEEEEEKSEEEAAAGLGALFG
>gnl|CDD|441662 COG2059, ChrA, Chromate transport protein ChrA [Inorganic ion transport and metabolism]
APMPSLLELFLAFLKIGLLSFGGGYAVLPLLQREVVEKRGWLTEEEFLDGLALAQALPGPIAINLATFIG
YLVAGILGALVATLGFFLPSFLLILLLAPFYERFRDNPWVQAALAGIKAAVVGLIAAAALRLAKKALKDW
LTLAIALAAFVLLLFFKVPPILVILAAALLGLLL
>gnl|CDD|441663 COG2060, KdpA, K+-transporting ATPase, KdpA subunit [Inorganic ion transport and metabolism]
MMLSGILQIALFLALLLLLAKPLGRYMARVFEGERTWLDPVLGPVERLIYRLAGVDPDEEMSWKQYALAL
LLFNLVGFLLLYALLRLQGWLPLNPQGLPGMSPDLAFNTAISFVTNTNWQHYSGETTLSYLSQMLGLTVQ
NFLSAATGIAVAIALIRGFARKSTKTLGNFWVDLTRSTLYVLLPLSLVLALLLVSQGVPQTLAGYVTVTT
LEGATQTIAMGPVASQEAIKQLGTNGGGFFGANSAHPFENPTPLSNLLEMLAILLIPAALVFTFGRMVGD
RRQGWAIFAAMLVLFVAGLAVAYWAEQAGNPALAALGVQSGGNMEGKEVRFGIAASALFAVVTTAASCGA
VNAMHDSLTPLGGLVPLFNMQLGEVVFGGVGSGLYGMLLFVILAVFIAGLMVGRTPEYLGKKIEAREMKM
ASLAILVHPLLILGGTAIAVVTPAGLAGISNPGPHGFSEVLYAYTSAAANNGSAFAGLSANTPFWNLTLG
IAMLLGRFLPIIPVLAIAGSLAAKKRVPESAGTLPTDTPLFVGLLIGVILIVGALTFFPALALGPIAEHL
SLLAG
>gnl|CDD|441664 COG2061, COG2061, Uncharacterized conserved protein, contains ACT domain [General function prediction only]
LLLLLDEEAAAAALAVVVVTTPLLLSSSSSLSVGLVVLLKEENLQTTGSFKRRGAYKLIALLLEEEEKGG
VAAAAAGNAAQAAAAAAALGGISAIVVMPPPPPLPKVAATRGGGAVVVVVGGDDDAAAAAAAALQEEEGG
FFHHPDDDDDVIAGGGGGGLEILELLPDVVVVVVGGGGGGGGGGAAAAAKAKRPPIVIVGVQAEAAAAAP
SSLAAGIEVVPGGGTTIADGIAVVKPGGLTFIIIRKVVDDVVVVVEEEIAAALLLLLERKKKVVEGAAAA
AAAAALKKKPLRGKKVVVVLSGGNIDDLLLLRIIIKGLLAAGRRLVLLVVLPDRPGQLLRVLQPIAELGA
NIISVVHERENSKTPRGEVEVEVVLETRGEEHLEEIIAALREAGYNVRRVG
>gnl|CDD|441665 COG2062, SixA, Phosphohistidine phosphatase SixA [Signal transduction mechanisms]
LILVRHAKAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLP
PKVEVEDELYDADPEDLLDLLRELDDGETVLLVGHNPGLSELAALLAGGEPLDGFPTGGLAVLEFDIDDL
GPGKGRLVWFLTP
>gnl|CDD|441666 COG2063, FlgH, Flagellar basal body L-ring protein FlgH [Cell motility]
LLLLLALLLAGCASVPPEPVVDDPAYAPVMPAPPPAAPPANGSLFQAGGSRPLFEDRRARRVGDILTVVI
VENTSASKSASTSRSRSSSVSLGIPTLFGLPGSLLGGPNLSVSASSSSSFKGKGSASRSNSLTGTITATV
VEVLPNGNLVVRGEKEVRVNQGLEYIRLSGIVRPEDISPDNTVSSTKIADARIEYGGRGALADAQQPGWL
QRFFDSVL
>gnl|CDD|441667 COG2064, TadC, Flp pilus assembly protein TadC [Extracellular structures]
LLLLGLLYVFLLPTPLALLLALLAALLGFLLPDLWLKRRAKKRQKEIRRELPDALDLLAVCVEAGLSLDA
ALRRVAEELGASSGPLAEELARVLAELRAGRSRREALRNLAERTGVDEVRSFVTALIQAERYGTSIAEAL
RVQADEMREKRRQRAEEKAAKLPVKMLVPLILFILPALFIVLLGPAVIQIM
>gnl|CDD|441668 COG2065, PyrR, Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide transport and metabolism]. Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage
KKKKEILDAADIDRALTRIAHEIIERNKGLEDLVLVGIQTRGVPLAERLAERIEEIEGVKVPVGSLDITL
YRDDLRRRPPRPVVNETEIPFDIDGKTVVLVDDVLYTGRTVRAALDALMDFGRPAKIQLAVLVDRGHREL
PIRADYVGKNVPTSRSERVEVRLKEIDGEDAVVIVEPA
>gnl|CDD|441669 COG2066, GlsA, Glutaminase [Amino acid transport and metabolism]
LEEIYEKVRPYLGEGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALED
LGGEEVWERVGVEPSGDPFNSIVQLELENGIPRNPMINAGAIVVTSLLPGRSGDERFERILDFLRRLAGN
RELSVDEEVYASEKATGDRNRALAYLLKSFGNLENDVEEVLDLYFRQCSIEVTCRDLARMGATLANGGVN
PVTGERVISPEVARRVLALMLTCGMYDASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGN
SVRGVKALERLSTELGLSIF
>gnl|CDD|441670 COG2067, FadL, Long-chain fatty acid transport protein [Lipid transport and metabolism]
LLLALALLLASGSAQAAGFQLNEQGARALGMAGAGVAALADDASAVFYNPAGLAFLKGTQLSLGLTLIDP
DVDFTGTGTGSDGSADGPVFVVPNFYYVYPLNDRLAFGLGVYAPFGLGTDYDDDWPGRYLATKSELKTIN
INPSVAYKVNDKLSVGAGLDLVYGDAELKRAVDFAGLAPSDGSAELKGDDWGFGFNLGLLYKPTDNLRLG
LSYRSKVKMDLDGDATFSGPASLGLFADTAGSADLDLPATLSLGVAYKLTDKLTLAADVTWTNWSSFDEL
AITFDNPVGSPDSVLPFNWKDTWVYALGAEYKLNDKLTLRAGYAYDESPVPDETRNPLIPDGDRHWLSLG
AGYKLSKNLSLDLAYAYLFGKDRTINNTSTPGNLNGTYKASANILGLSLSYKF
>gnl|CDD|441671 COG2068, MocA, CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]
MSKVAAIILAAGASSRMGRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVV
VNPDWEEGMSSSLRAGLAALPADADAVLVLLGDQPLVTAETLRRLLAAFRESPASIVAPTYDGRRGHPVL
FSRRLFPELLALTGDQGARALLRRHPDRVRLVPVDDPGVLLDIDTPEDLARLLAR
>gnl|CDD|441672 COG2069, CdhD, CO dehydrogenase/acetyl-CoA synthase delta subunit (corrinoid Fe-S protein) [Energy production and conversion]
MAFEIPKEKYTGKIREVTLGTREKTVTIGGETALPFYHFEGEMPNKPVIAMEVFDIPPEDWPEALKEPFG
DVLNDPAAWAKKCVEEYGADMICLHLISTDPNGKDKSPEEAAKVVKEVLQAVDVPLIIGGSGNPEKDAEV
LEKVAEAAEGENLLLGSATEDNYKTIGAAAMAYGHSVIASSPLDINLAKQLNILLTELGVPLDRIVMDPT
TGALGYGIEYSYSIMERIRLAALQGDKMLQMPMICGVGTEAWKAKEAWAPEEDDPEWGDQEERGILWEAV
TALTLLLAGADILIMRHPESVKTLKEIIDTLMGSNEY
>gnl|CDD|441673 COG2070, YrpB, NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only]
LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNLTPEALREEIRKIRELTDGPFGVNLIVHPANPR
FEELLEVVLEEGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVREARKAEKAGADAVVAEGAEAGGHRG
ADEVSTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPAHEAYKQALVDAK
EEDTVLTRSFTGRPARALRNSFTREGLDLEAECLYPILEALTAGKRLRAAAAEGDLEKGLLWAGQGAGLI
RDILPAAELVARLVAEAEAALA
>gnl|CDD|441674 COG2071, PuuD, Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism]
ITADLRTAGGYPAHYLPEDYVRAVRAAGGLPVLLPPVGDEEDLDELLDRLDGLVLTGGADVDPALYGEEP
HPELGPIDPERDAFELALIRAALERGKPVLGICRGMQLLNVALGGTLYQDLPDQVPGALDHRQPAPRYAP
RHTVEIEPGSRLARILGEEEIRVNSLHHQAVKRLGPGLRVSARAPDGVIEAIESPGAPFVLGVQWHPEWL
AASDPLSRRLFEAFVEAARAR
>gnl|CDD|441675 COG2072, CzcO, Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism]
TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTWRDNRYPGLRLDTPSHLYSLPFFPNW
SDDPDFPTGDEILAYLEAYADKFGLRRPIRFGTEVTSARWDEADGRWTVTTDDGETLTARFVVVATGPLS
RPKIPDIPGLEDFAGEQLHSADWRNPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRTPPWVLPR
PNYDPERGRPANYLGLEAPPALNRRDARAWLRRLLRAQVKDPELGLLTPDYPPGCKRPLLSTDYYEALRR
GNVELVTGGIERITEDGVVFADGTEHEVDVIVWATGFRADLPWLAPLDVRGRDGRSGPRAYLGVVVPGFP
NLFFLGPNSPSGHSSLTLGAERQARYIARLIAHMRRRGAAAIEVRPEAEDAFNARLQRRAARTV
>gnl|CDD|441676 COG2073, CbiG, Cobalamin biosynthesis protein CbiG [Coenzyme transport and metabolism]. Cobalamin biosynthesis protein CbiG is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MKIAIIALTENGLELARRLAEALPGADLYVPEKLAEEGAVPFDGSLKELLAELFKEYDAIVFIMATGIVV
RLIAPLLKDKKTDPAVVVVDEKGRFVISLLSGHLGGANELARRIAEILGATPVITTATDVNGLPAVDTLA
KKLGWRIENFEDVKAVNAALVNGEPVGLYQDAGLPPPLPKNVKLVDEDYEAAVVVTDRVLELPLPVLVLR
PKVLVLGIGCRRGTSAEEIEEAIEEALAEAGLSPKSIAAIATIDLKKDEPGLLELAKELGVPLVFFSAEE
LNEVEVPNPSEFVKKTVGVGGVAEPAALLASGGGELIVEKQKYGGVTVAIARED
>gnl|CDD|441677 COG2074, Pgk2, 2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and metabolism, Lipid transport and metabolism]
RRMKRPRIILIGGASGVGKSTIAAELARRLGIPRVISTDSIREVMRPIISKELVPTLHTSSYEAYKSLSE
EEIIAGFLDQAEAVSPGIEAVIERALKEGESLVIEGVHLVPGFLAELKFNGGNVVMLVLLVSDEELHRER
FYSRARYTHANRPGERYLDHFERIRRIQDYLVEQAREHGVPVIENIDLDETVDRILEAITEAFSRGG
>gnl|CDD|441678 COG2075, RPL24A, Ribosomal protein L24E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L24E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MVETRTCSFCGREIEPGTGKMYVRNDGTVLWFCSSKCEKNMKLGRDPRKLKWTRKYRKGKEKR
>gnl|CDD|441679 COG2076, EmrE, Multidrug transporter EmrE and related cation transporters [Defense mechanisms]
AWLYLLLAGLLEVVWTLALKLSDGFTRLLPSVLTVVGYALSFYLLSLALKTLPVGTAYAVWTGIGAVGTA
LVGILLFGEPLSLARLLGIALIIAGVVGLKLFSGS
>gnl|CDD|441680 COG2077, Tpx, Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]
MATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEE
AAKLDNVVVLTISADLPFAQKRFCGAEGIDNVVTLSDFRDRSFGKDYGVLIKEGPLLGLLARAVFVLDEN
GKVVYTELVPEITDEPDYDAALAALKAL
>gnl|CDD|441681 COG2078, AMMECR1, Predicted RNA modification protein, AMMECR1 domain [General function prediction only]
ELSDEEGARLVRLAREAIEAYLEGGELLPPPEDLPEALKERRGVFVTLKKDGELRGCIGTLEPVRPLAEA
VIENAIAAAFEDPRFPPVTPEELDDLTIEVSVLSPPEPIEDLLEELEPGRDGLIVEKGGRRGLLLPQVAW
EGLWDPEEFLAHLCRKAGLPPDAWKDPDVKVYRFEVEVFKEREP
>gnl|CDD|441682 COG2079, PrpD, 2-methylcitrate dehydratase PrpD [Carbohydrate transport and metabolism]
TERLAEFAAGLRYEDLPAEVVERAKRRLLDTLGVALAGLREPPVRALRAAAAALGGPGGATVLGTGGRLS
PEDAALANGTAAHALDFDDTHLAAIGHPSADVIPAALAVAEALGASGRDLLTAIVAGYEVQGRLGLAVGP
SHYRRGWHHTGTLGTFGAAAAAARLLGLDAEQTAHALGIAASQAAGLRQYLRFGTMTKPLHAGFAARNGV
LAALLARAGFTGPPDILEGPFGFFAAFAGGEFDPEALTDGLGERWEILETSFKPYPACRHTHAAIDAALA
LRAEHGLDPDDIERIEVETHPAALRIIGDPDPATPEDAKFSLPYCVAVALLDGRLGLDDFEDERLADPDV
RALAAKVTVVEDPELDARYPAARPARVTVTLKDGRTLEAEVDYPKGHPENPLSDEELEAKFRALAAPVLG
AARAERLLDAVRRLEDLPDVAELLAL
>gnl|CDD|441683 COG2080, CutS, Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and conversion]. Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
MMMITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGK
EITTIEGLAEDGELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYV
RIVRAVKRAAAALRG
>gnl|CDD|441684 COG2081, YhiN, Predicted flavoprotein YhiN [General function prediction only]
IVIGAGAAGLMAAITAAERGARVLLLEKNPKVGRKILISGGGRCNFTNSEPLPEFLNYYGGNPHFLKSAL
SRFTPEDLIAFFEGLGIETKEESSGRVFPDSSKASDILRALLAELREAGVEIRLRTRVTGIEKEDGGFGV
ETPDGETVRADAVVLATGGLSYPKLGSTGDGYRLAEQFGHTITPLRPALVPLTLSEHFFKRLAGLSLKNV
ALSVGGKKIASFRGELLFTHRGLSGPAILQLSSYWRDALKKGGATLTIDLLPDLDLEELDARLARPREKN
GKKSLKNVLRGLLPKRLAALLLELADPDKPLAQLSKKEREALAALLKAWPLTPTGTRGYDEAIVTAGGVD
TKELDPKTMESKKVPGLYFAGEVLDVDGPTGGYNLQWAWSSGYAAGQAAAAW
>gnl|CDD|441685 COG2082, CobH, Precorrin-8X methylmutase CbiC/CobH [Coenzyme transport and metabolism]. Precorrin-8X methylmutase CbiC/CobH is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
DYIRDPAEIERESFAIIRAELDLSRFSEDEEPVVVRLIHATGDFDLADLLRFSPGAVEAGRAALRAGAPI
VTDVEMVAAGINKRRLPALGNEVICLISDPRVAELAKAEGITRSAAAMRLAAERLEGAIVAIGNAPTALF
ELLELIEEGAPRPALIIGVPVGFVGAAESKEALMASGVPYITVRGRKGGSAIAAAAVNALLYL
>gnl|CDD|441686 COG2083, COG2083, Uncharacterized conserved protein, UPF0216 family [Function unknown]
MTGNSVIDRILEKELRRINSHLPAERKSLKELLEEEKPSIRLRDGSEHYFDKEELERLASILPEYLWDLL
KLPIIIEYDPSVGEGGYRVRGRWEVEAISILLGIDREEEGRLWLYRPEVEKLRRKLPTLTQITFSVE
>gnl|CDD|441687 COG2084, MmsB, 3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism]
MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAA
VEEVLLGEDGLLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGD
EAAFERARPVLEAMGKRIVHVGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGA
AGSWVLENRGPRMLAGDFDPGFALDLMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSA
LIKLL
>gnl|CDD|441688 COG2085, COG2085, Predicted dinucleotide-binding enzyme [General function prediction only]
IGIIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAELGPGARAGTNAEAAAAADVVVLAVPYEAVP
DVLESLGDALAGKIVIDATNPLPERDGFILDPPGGGSAAELVAALLPGARVVKAFNTIGAAVLADPARPA
GGRRDVFVAGDDAEAKAVVAALIEDLGFDPVDAGPLANARRLEPLTPLLINLARTAGLELGFRLL
>gnl|CDD|441689 COG2086, FixA, Electron transfer flavoprotein, alpha and beta subunits [Energy production and conversion]
MKILVCVKQVPDTNVKIRVDPDGGTLDREGVPSIINPYDEYALEEALRLKEKGGGEVTVVSMGPPQAEEA
LRKALAMGADRAILVSDDAFAGADTLATAKALAAAIKKIGGPDLVLCGKQAIDGDTGQVGPMLAELLGLP
QVTYVSKLEVEGGTVTVERELEGGLETVEVPLPAVVTVDKGLNEPRYPSLKGIMKAKKKPIEVLSAADLG
LDPAKVGLKGSPTKVVKVFAPPARRAGEIIEGDPEEAAAELVEKLKEEAKV
>gnl|CDD|441690 COG2087, CobU, Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase [Coenzyme transport and metabolism]. Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MLTLVLGGARSGKSRFAEKLAAASGKPVVYIATAQAFDEEMAERIARHRARRPAGWTTVEEPLDLAAALA
ALAPPGDVVLVDCLTLWLTNLLFAEDAWEEEDVEAEIDELLEALRALPGPVVLVSNEVGLGIVPENPLGR
RFRDLLGRLNQRLAAAADEVYLVVAGLPLKLK
>gnl|CDD|441691 COG2088, SpoVG, DNA-binding protein SpoVG, cell septation regulator [Cell cycle control, cell division, chromosome partitioning]
EITDVRIRPVEPEGKLKAFASVTFDDCFVVHDIKVIEGKNGLFVAMPSRKTPDGEYRDIAHPINKEAREK
IEDAVLEAYEEALE
>gnl|CDD|441692 COG2089, SpsE, Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope biogenesis]
HPPFIIAEIGVNHNGDLELAKELIDAAAEAGADAVKFQTYTADTLTSDSAPKAFYQSGSLWGGESLYELY
KRLELPWEWHKELKEYCKELGIIFFSTPFDEESVDFLEELGVPAYKIASGEITNLPLLRYIAKTGKPIIL
STGMATLEEIEEAVEALREAGNDQIALLHCTSAYPAPPEDVNLRAIPTLKEAFGVPVGLSDHTLGIEVPI
AAVALGASVIEKHFTLDRSLPGPDHAFSLEPDELKAMVEAIRNAEKALGSGIKGPTPSEKKNRRVARRSL
VAARDIKAGEVITEENLRVKRPGTGLSPKYLDEVLGKKAKRDIKAGTPLTWDDLE
>gnl|CDD|441693 COG2090, COG2090, Uncharacterized conserved protein, DUF371 domain [Function unknown]
MVMEEVIRARGHENVRATHRSTFEITKDDYLTPRGDCIIGVEADKAAADLSEEFKEALRDPDATITVTLE
VGGLSDTITGRGHPDLTLEHPRDIVIRKSDYVDDRTLAIRADKAAADLDRDLVEALADGATLTVTIIVED
>gnl|CDD|441694 COG2091, Sfp, Phosphopantetheinyl transferase [Coenzyme transport and metabolism]
PLLSTIPGEVHVWFIRLDEEDLDELLALLSEDERARAARFRSEKRRRRFLAGRALLRELLARLLGLPPAD
LEFAYDPHGKPYLADPGLHFSLSHSGGLAAVAVSRGGPVGVDIERIRPRIDLALARRFFSPEERAWLAAL
PQDDRLEAFTRLWTLKEALLKATGTGLSLPLRALAVE
>gnl|CDD|441695 COG2092, EFB1, Translation elongation factor EF-1beta [Translation, ribosomal structure and biogenesis]. Translation elongation factor EF-1beta is part of the Pathway/BioSystem: Translation factors
MGDVAAVIKVMPESPEVDLEELKEKIKKKLPEGYEIKGIEEEPIAFGLKALKLYVVMPDTEGGTDALEEA
LSSVEGVESVEVESVSRLS
>gnl|CDD|441696 COG2093, Spt4, RNA polymerase subunit RPABC4/transcription elongation factor Spt4 [Transcription]. RNA polymerase subunit RPABC4/transcription elongation factor Spt4 is part of the Pathway/BioSystem: RNA polymerase
KPEKACRNCKRLVPEDGDVCPVCGSTDLSEDWSGYVIILDPEKSEIAKKLGITKPGKYALKVR
>gnl|CDD|441697 COG2094, Mpg, 3-methyladenine DNA glycosylase Mpg [Replication, recombination and repair]
MTRPLPRDFFARDALEVARDLLGKVLVRETDGGTVAGRIVETEAYLGPDDPASHAYRGRTPRNAVMFGPP
GHAYVYFIYGMHWCLNVVTGPEGEPSAVLIRAGEPVEGIELMRARRGKARKDRDLANGPGKLCQALGIDR
AHNGLDLTDDPLWLEDGEPVPPEEIVAGPRIGISYAADLPWRFWIKGNPFVSR
>gnl|CDD|441698 COG2095, MarC, Small neutral amino acid transporter SnatA, MarC family [Amino acid transport and metabolism]
DLSLFLSAFVTLFAIIDPIGNVPIFLSLTKGLSPAERRRIALRASLIAFVILLVFALAGQLILSFFGISL
PAFRIAGGILLFLIALDMLFGKPSGEKETEAEEAEDKEDIAVVPLAIPLLAGPGAIATVILLAAQAPGLL
GLLAVLLAILLVLLLTYLILLLAGRILRLLGETGINVLTRLMGLILAAIAVQMILDGIKGLFPGLA
>gnl|CDD|441699 COG2096, PduO, Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]. Cob(II)alamin adenosyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MKIYTRTGDKGTTGLGGGSRVSKDDPRVEAYGTVDELNSAIGLARALLLDEDLRELLERIQNDLFDLGAD
LATPGEKRPPLRITEEDVERLEEEIDELNAELPPLKSFILPGGSPAAAALHVARTVCRRAERRLVALAEE
EPVNPEVLKYLNRLSDLLFVLARVANKRAGVAEVLWKPGK
>gnl|CDD|441700 COG2097, RPL31A, Ribosomal protein L31E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L31E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MSEEDFEERVYTIPLRKVKLAPRTKRADRAIKLIREFLARHMKVEEEKVKIDPSLNEKIWSRGREKPPRK
VRVRAVKFEEGEVEVELAE
>gnl|CDD|441701 COG2098, MptD, 7,8-dihydroneopterin aldolase MptD (tetrahydrofolate and tetrahydromethanopterin biosynthesis) [Coenzyme transport and metabolism]
FKNPTDRERACFEAGIKLGALYHQFAGTPVSPESAESLEKAIEESIENQPFVEDVKVSIDRDRLEAKDNE
YGYTELTGRMLDVEIVVRYGGTEVVARMRYIEELGYPLMYIEDVEEV
>gnl|CDD|441702 COG2099, CobK, Precorrin-6x reductase [Coenzyme transport and metabolism]. Precorrin-6x reductase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MMMILILGGTTEARALAEALAAAGIPVIVSLATRTGAPLLPEPGGPVRVGGFGAEGLAAYLREEGIDAVI
DATHPFAAQISRNAAAACAELGIPYLRLERPAWQAPPGDLWIEVDDLEEAAAALPELGGRVFLTTGSKEL
AAFAALPPQHRLLARVLPPPEVLEKCEALGLPPKNIIAMRGPFSLELERALLRQYGIDVLVTKNSGGAGG
TDAKLEAARELGIPVIMIRRPPLPYGEVVSDVEEALAWLKR
>gnl|CDD|441703 COG2100, COG2100, Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function prediction only]
MERLIGRTTGRPLYYITSGIPLIGHIAFGVIDRGTNVLQVRPTTGCNLNCIFCSVDAGPHSRTRQAEYIV
DPEYLVEWFEKVARFKGKGVEAHIDGVGEPLLYPYIVELVKGLKEIKGVKVVSMQTNGTLLSEKLIDELE
EAGLDRINLSIDTLDPEKAKKLAGTKWYDVEKVLELAEYIARETKIDLLIAPVWLPGINDEDIPKIIEWA
LEIGAGKKWPPLGIQKYEPHKYGRKPPGVKVWSWKEFYRWLRELEEEYGVKLILSPEDFGIHKRKRLPKP
FRKGEVVKVEIVLPGWLKGEVLGVAKNKDRVITVIGVKKVPPIGDRVKVKIIRDKDNIYVAKPV
>gnl|CDD|441704 COG2101, SPT15, TATA-box binding protein (TBP), component of TFIID and TFIIIB [Transcription]
KPTIEIENIVASGSLGQELDLEKLAEDLPNAEYNPEQFPGLVYRLKEPKTAALIFRSGKMVCTGAKSEED
LIEAVEKVIEKLRKLGIEIPDEPEITVQNIVASADLGREINLNALAIGLGLENIEYEPEQFPGLVYRLDD
PKVVLLLFSSGKLVITGAKDEEEAERAVDKLRERLEELGL
>gnl|CDD|441705 COG2102, Dph6, Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and biogenesis]
VVVSWSGGKDSALALYRALQEGYEVVGLLTTVPEDFDRVMFHGPNLELLEAQAEALGIPLIEIELSGSNE
EYEEELEEALKELKAEGIEGVVFGDIFLEDQRDYRERVCEELGLEAVFPLWGRDTEELLEEFIDAGFEAI
IVCVDAEGLDESWLGRELDEELLEELPAYGVDPCGEGGEFHTFVLDGPLFKKPIEIEEGEIVWRGGFGFL
DIE
>gnl|CDD|441706 COG2103, MurQ, N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis]
MMDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVG
AGTSGRLGVLDASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIA
ASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLS
TAAMIRLGKVYGNLMVDVRATNAKLRDRAIRIVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEE
AEALLARAGGFLRKALAALGA
>gnl|CDD|441707 COG2104, ThiS, Sulfur carrier protein ThiS (thiamine biosynthesis) [Coenzyme transport and metabolism]. Sulfur carrier protein ThiS (thiamine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis
MKITVNGEPREVPEGTTLADLLEELGLDPKGVAVAVNGEIVPRSQWASTVLKEGDRVEIVTAVGGG
>gnl|CDD|441708 COG2105, YtfP, Predicted gamma-glutamylamine cyclotransferase YtfP, GGCT/AIG2-like family [Amino acid transport and metabolism]
MLLFVYGTLRRGESNHHLLRGARFLGPATLEGRLYDLGAYPALVPDGGGRVYGELYEVDDALLAALDELE
GAPNLYRRELVPVETGDGTVEAWVYVYNPEVSGLPRIPSGDWLA
>gnl|CDD|441709 COG2106, MTH1, Predicted RNA methylase MTH1, SPOUT superfamily [General function prediction only]
KLSVAIPSSLLSEEPDLREKTRKIGYIARAAAIFRVDRIVIYPDREGERRRDGEFIETVLRYLATPPYLR
KRLFPLRDELRYAGVLPPLRIPSHTGSKSPKVGDLRQGLVTRVDGKVRVDIGLGHPISLPGKLPEGERVT
VRISSREPVRAEPVDEPEIYWGYEVKRTDSLRELLEEYDAGLVIATSRKGEPITVSLAELAERIKSAGGV
LVVFGSPYRGLPEILGVENLDPLFDLVLNTIPNQGTETVRTEEALFATLAILNLLE
>gnl|CDD|441710 COG2107, MqnD, 1,4-dihydroxy-6-naphtoate synthase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and metabolism]. 1,4-dihydroxy-6-naphtoate synthase (menaquinone biosynthesis, futalosine pathway) is part of the Pathway/BioSystem: Menaquinone biosynthesis
MMTITLGHSPDPDDAFMFYALAHGKVDTEGFEFEHVLEDIETLNRRALKGELDVTAISFHAYPYIADDYA
LLRSGASLGRGYGPLVVAKKPMSLEELKGKRIAVPGRYTTAYLLLRLALPKAFEVVEMPFDEIMPAVLSG
EVDAGLIIHEGQLTYAEYGLVKVLDLGEWWEEETGLPLPLGGNVIRRDLGEEVARKIEEALRKSIKYALA
HPDEALEYAMKYARELDEEVIDKFIGMYVNEYTVDLGEEGRRAVRTLLERAYEKGLIPKPKEPDFL
>gnl|CDD|441711 COG2108, COG2108, Uncharacterized radical SAM domain-containing protein [Function unknown]
MINKGNPGTGLYYGYLSPGCRLCRKGAKLVLFITGLCNRNCFYCPLSEERKGKDVIYANERPVESDEDVI
EEARRMGALGAGITGGEPLLVLDRTLEYIRLLKEEFGPDHHIHLYTNGILADEDVLRKLADAGLDEIRFH
PPQELWGLLGTPYLESIKLAKEYGLDVGVEIPAIPGEEEELKKLLEFLDEAGVDFLNLNELEFSETNAEA
LRERGYTLKDDISNAVKGSEETALELLEYAEDNLKLKVHYCSSVFKDAVQLRNRLRRIAKNTARPYEEIT
EDGTIVYGIIEGGDLEELAERLGELGVPEELYEIKDGRIELAPWLLEELADELPGLGGEAYIVERYPTAD
GLVVERIPLAE
>gnl|CDD|441712 COG2109, BtuR, ATP:corrinoid adenosyltransferase [Coenzyme transport and metabolism]. ATP:corrinoid adenosyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MVDARIAAATEEKGLVQVYTGNGKGKTTAALGLALRALGHGLKVGVVQFIKGGWDTGELKALERLPGVEF
HQMGEGFTWETQDREEDIAAAREGWERAKELLASGEYDLVILDEINYALKYGLLDVEEVLELLKNRPEHQ
EVVLTGRNAPPELIELADLVTEMKEVKHPFDAGIKARKGIEF
>gnl|CDD|441713 COG2110, YmdB, O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis]
IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKQGGCPTGEAVITPAGNLPA
KYVIHTVGPVWRGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFL
EEHPSLEEVRFVLFDEEDYEAYRRALAR
>gnl|CDD|441714 COG2111, MnhB, Multisubunit Na+/H+ antiporter, MnhB subunit [Inorganic ion transport and metabolism]
LLLLLLLLLLLLLLLLLALLLLLLLLLLLLALAAAALAALLALLAALALLLAATAAAAALALLLLLLLLA
ALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLGALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLSLL
LLLLLLLLLLLAAAAAAAAAALLGGGGGALLLLLLLLLLLGLLALAAAAALALLLLLLLPLLLALALAAA
AAAAAAAAALLFFLFLAAAAAAAAAAAALAAAAAAAVAVVALLLLLALVAGLLLLLLLLLLLLLLLLLLL
GLLGALLLLLLLLLLLLLLLLLLLLLLLLLLLGLLLAAAAAAAAALLALLLLLALALLLLLALALAAGLG
LRLLLLLLLRLLAALLAAAAAAALAAAAALLLLLLLLLLALLLALGLLGLLLLLAALLAAAALLAAAAAA
ALALALLGGALAAAPAAAAAALLLLLLLLLALLLLALLLLLLLLLALLLLLLLAVAALVALLLLLLLLLL
LLLVLVLLLLLLLLLLLLLLLLLLLLRAAARAALLALAAAAAGAAAYALALGLLLVAAASTTGGGGGGLL
LGLLGVVVVVVVLVLVLLLLALGLVLLLLLARLGALALLLLLLLALLVAAAAASLILSRLTRVLLPGILG
FSVYLFFRGHNAPGGGFTGGLVEALALILLYLALGRLWVEERLPVDALILIGVGLLLAALTGLAALLFGG
PFLTSAFLPLAGGLNLVNAILFDFGVFDTVGGITVLILAALGRLRRREGR
>gnl|CDD|441715 COG2112, COG2112, Predicted Ser/Thr protein kinase [Signal transduction mechanisms]
MDSDEELIRLLCYPRSESELEERLEELKSLGITSIYSGGTLIGGLRLLGKGYRGVVFLGKLGGKKVALKI
RRTDSPRPSLKKEAEILKKANGAGVGPKLYDYGRDFLVMEYIEGEPLKDWLENLDKEELRKVIRELLEAA
YLLDRIGIDHGELSRPGKHVIVDKGRPYIIDFESASISRKPSNVTSALSYLFLGSNIAKRIKKILGLDKE
KLRELLKLYKKNPSK
>gnl|CDD|441716 COG2113, ProX, ABC-type proline/glycine betaine transport system, periplasmic component [Amino acid transport and metabolism]
MKKLLLLLLAAALALALAGCAAAAAAPGSCKTVTIADVGWTSATATTAVAKQILEELGYEVELVELDVPV
TYQGLANGDIDVFLEAWLPTTHADYDEAYGDGKVEDLGTNYEGAKQGLAVPKYVAEPGIKSIADLKKYAD
LFDGKIYGIEPGWGCNRVIEEAIKAYGLDDFELVEGSEAAMLAALARAYKRGEPIVFYGWTPHWMFAKYD
LKYLEDPKGAFGPNFPAETVHTVARKGFAEDNPEAAKLLENFKFTLEDINALMAAIENDGADPEEAAKEW
LKANPDVVDGWLPGVTA
>gnl|CDD|441717 COG2114, AcyC, Adenylate cyclase, class 3 [Signal transduction mechanisms]
AALAALLLLLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLL
LLGLLLLALLLGLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLA
LALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAG
GEELRLGGERREVTVLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFG
APVAREDHAERAVRAALAMQEALAELNAELPAEGGPPLRVRIGIHTGEVVVGNIGSEDRLDYTVIGDTVN
LAARLESLAKPGEILVSEATYDLLRDRFEFRELGEVRLKGKAEPVEVYELLGAKEAA
>gnl|CDD|441718 COG2115, XylA, Xylose isomerase [Carbohydrate transport and metabolism]
MKEYFPGIPKIKYEGPDSDNPLAFRHYDPDEVVAGKTMKEHLRFAVAYWHTFCWTGSDPFGGGTRERPWD
PGGDPMERAKAKADAAFEFFTKLGAPYYCFHDRDLAPEGATLAERNKNLDEIVDYFKEKQKETGVKLLWG
TANLFSHPRFMNGAATNPDPDVFAYAAAQVKKALDATKELGGENYVFWGGREGYETLLNTDMKRELDHLA
RFLHMAVDYAKKIGFKGQFLIEPKPKEPTKHQYDFDVATVIGFLRTYGLEKDFKLNIEVNHATLAGHTFE
HELAVAADAGKLGSIDANRGDYQLGWDTDQFPTNVYETTLAMYEILENGGFTTGGLNFDAKVRRTSFDPE
DLFYAHIGGMDTFARGLKIAAAILEDGELEALLAERYASWDSGIGKDILAGKLSLEDLAAYALAEGFDPA
PRSGRQERLENLVNEYLLG
>gnl|CDD|441719 COG2116, FocA, Formate/nitrite transporter FocA, FNT family [Inorganic ion transport and metabolism]
DYLSPAEIAERAVEAGEKKLNRSPLKLLISGILAGAFIGFGFLLAITVTAGLPGLGPGLAKLLGGLVFPL
GLILVVLGGAELFTGNTLTPVLAVLAKKISWGKLLRNWGVVYLGNLIGALLFALLLALSGVLGPGAVGAA
LLAIAEHKVSLPFLEAFVRGILCNWLVCLAVWMAYAAKDVTGKILAIWLPIFAFVAGGFEHSVANMFEIP
LGILLGADLTWGDFILWNLIPVTLGNIVGGAVFVGLLYYFQYRREREE
>gnl|CDD|441720 COG2117, COG2117, Predicted subunit of tRNA(5-methylaminomethyl-2-thiouridylate) methyltransferase, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]. Predicted subunit of tRNA(5-methylaminomethyl-2-thiouridylate) methyltransferase, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification
KAAVLYSGGKDSSLAALLLERFYDVELVTANFGITDSWKHAREAAEALGFPHRVLELDRGVLEEAVDMII
EDGYPRNGIQYVHEHALEALADLEYDAIADGTRRDDRVPKLSRSEAQSLEDRHGVDYIRPLSGFGRKAVD
RLVERLLEVEEGPSEEIPKADYETELRELIRERHGEDAVEEIFPEHEQSRVIGRKK
>gnl|CDD|441721 COG2118, PDCD5, DNA-binding TFAR19-related protein, PDSD5 family [General function prediction only]
MSPDDDELEELRRRKLEELQRQQAAQQAAEAQEQAQQQAEAQKQAILRQILTPEARERLNNVKLVKPEFA
EQVEQQLIQLAQSGRLQGPIDDEQLKELLRELTPDRREFKIERR
>gnl|CDD|441722 COG2119, Gdt1, Putative Ca2+/H+ antiporter, TMEM165/GDT1 family [General function prediction only]
MMEAFLTSFGLVALAELGDKTQLLALALATRYRPWPVLAGILAATLLNHALAVALGSWLASLLPPDYLRW
VAALLFLAFGLWLLRPDKLDEEEAKAAEKSRFGPFLTTFVAFFLAEMGDKTQLATIALAARYGAPLAVWL
GTTLGMMLASALAVLLGRKLAKRIPLRLIHRIAAALFLLFGLVTLLEALGGL
>gnl|CDD|441723 COG2120, LmbE, N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism]
RVLVVAAHPDDEELGCGGTIARLAAAGHEVTVVTLTDGEAGSPGGPPLREELAEIRRAEARAAAAILGVS
DVEFLGYPDGGLEGPLEELRRALARLIREVRPDVVLTPDPGDGHPDHRAVGRAVLAAARLAGLPKILGPR
LYLYEVPSDTEPDVAVDITDVLERKLAALAAHASQLDPLFAIRALARLRGAQAGVEYAEAF
>gnl|CDD|441724 COG2121, COG2121, Uncharacterized conserved protein, lysophospholipid acyltransferase (LPLAT) superfamily [Function unknown]
MKLLKKLARSPLLLRLLGWLLAGYLRLLFRTLRVEVEGEEALDRLLASGKPFILAFWHGQLLMAPFLFRG
KKIAVLVSRSRDGELIARVLERLGFGTVRGSSSRGGAAALREMLRALKEGYSVAITPDGPRGPRRVVKPG
IIYLARKSGAPIVPVAVAASRRWRLKSWDRFVLPLPFSRVVIVYGEPIYVPPDADEEELEALRLELEAAL
NALTARADALLGRAP
>gnl|CDD|441725 COG2122, COG2122, Uncharacterized conserved protein, UPF0280 family, ApbE superfamily [Function unknown]
RLPQAEGLDGFHVQHGETDLTIGADGDELVEAAKAAIARFRTQLEEYIAELPEFRTSLEPLPVPPLAPPI
VRRMAAAARPAGVGPMAAVAGAVADEVGEALLEAGSKEAIVENGGDIALHLDRPVTVGIYAGNSPLSGKL
GLRIPPGDGPLGICTSSGTVGHSLSFGIADAVTVLARDAALADAAATAIGNAVDLPDDVEKALEAGREIP
GIDGALLILGDKIGVWGDLPELVPARVDED
>gnl|CDD|441726 COG2123, Rrp42, Exosome complex RNA-binding protein Rrp42, RNase PH superfamily [Intracellular trafficking, secretion, and vesicular transport]
MSSPIIPEIKRDYILSLLKKGKRIDGRGLDEYRPIEIETGVIEKAEGSALVKLGNTQVLAGVKVEPGEPF
PDTPNEGVLIVNAELLPLASPTFEPGPPDENAIELARVVDRGIRESKAIDLEKLVIEPGKKVWMVFIDIY
VLDYDGNLFDASSLAAVAALLTTKVPKVEVGEDGVVVDKGEDTPLPVNTLPVSVTMAKIGDYLVVDPTLE
EESVMDARITITTDEDGNIVAMQKGGSGSFTEEEIDKAIDIALEKGKELRELLK
>gnl|CDD|441727 COG2124, CypX, Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]. Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis
MTATATPAADLPLDPAFLRDPYPFYARLREYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLP
EVLRPLPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRIREIADELLDRLAARGPVDLVEEFARP
LPVIVICELLGVPEEDRDRLRRWSDALLDALGPLPPERRRRARRARAELDAYLRELIAERRAEPGDDLLS
ALLAARDDGERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEPELLPAAVEETLRL
YPPVPLLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDRPPNAHLPFGGGPHRCLGA
ALARLEARIALATLLRRFPDLRLAPPEELRWRPSLTLRGPKSLPVRLRPR
>gnl|CDD|441728 COG2125, RPS6A, Ribosomal protein S6E (S10) [Translation, ribosomal structure and biogenesis]. Ribosomal protein S6E (S10) is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MAEFKVVVSDPKTGKSYQIEVKGQDANRLIGKKIGDEVDGSAVGLPGYKLEITGGSDKSGFPMRPDLPGP
GRKRILLSGGVGFKPKRDGERRRKTVRGNEISDDIVQINAKVVEYGEKPLEELLGEEEEEAEE
>gnl|CDD|441729 COG2126, RPL37A, Ribosomal protein L37E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L37E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MSKGTPSMGKRNKGKTHIRCRRCGRNSYNVRKKYCASCGFGKSKRIRSYSWQ
>gnl|CDD|441730 COG2127, ClpS, ATP-dependent Clp protease adapter protein ClpS [Posttranslational modification, protein turnover, chaperones]
MSPDTEPEEETETKTKPPPPYKVVLLNDDVNTMEFVVEVLQKVFGMSEEQAEQLMLEVHTKGKAVVGVGT
REIAETKVEQVHDYGLQATIEPAE
>gnl|CDD|441731 COG2128, YciW, Alkylhydroperoxidase family enzyme, contains CxxC motif [Inorganic ion transport and metabolism]
MSPELLKAFLALSGALMAKGGLSPRERELVALRVSQINGCAYCLDAHTAIARKAGLDEERIDALRAWRES
PLFDPRERAALAFAEALTRTPGGVSDADVAALRAGFSDAEIVELVLAIALFNMSNRLNNALGTPPDPPFA
AL
>gnl|CDD|441732 COG2129, COG2129, Predicted phosphoesterase, related to the Icc protein [General function prediction only]
KILAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNHDDPE
VLDALEESGVHNLHGRVVEIGGLRIAGLGGSRPTPFGTPYEYTEEEIEERLAKLREKDVDILLTHAPPYG
TTLDRVEDGPHVGSKALRELIEEFQPKLVLHGHIHESRGVDKIGGTRVVNPGSLAEGYYALIDLEDRSVE
L
>gnl|CDD|441733 COG2130, CurA, NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]
MMTTNRQIVLASRPEGEPTPEDFRLEEVPVPEPGDGEVLVRNLYLSVDPYMRGRMSDAKSYAPPVELGEV
MRGGAVGEVVESRHPDFAVGDLVLGMLGWQDYAVSDGAGLRKVDPSLAPLSAYLGVLGMPGLTAYFGLLD
IGKPKAGETVVVSAAAGAVGSVVGQIAKLKGCRVVGIAGGAEKCRYLVEELGFDAAIDYKAGDLAAALAA
ACPDGIDVYFDNVGGEILDAVLPLLNTFARIAVCGAISQYNATEPPPGPRNLGQLLVKRLRMQGFIVFDH
ADRFPEFLAELAGWVAEGKLKYRETVVEGLENAPEAFLGLFEGENFGKLLVKV
>gnl|CDD|441734 COG2131, ComEB, Deoxycytidylate deaminase [Nucleotide transport and metabolism]
KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLREKLGIPSG
ERGECCRTVHAEQNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELAKELLKE
AGVEVRQLELEEEE
>gnl|CDD|441735 COG2132, SufI, Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis]
PLPIPPLLESGGGREYELTAQPATVELLPGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVH
WHGLRVPNAMDGVPGDPIAPGETFTYEFPVPQPAGTYWYHPHTHGSTAEQVYRGLAGALIVEDPEEDLPR
YDRDIPLVLQDWRLDDDGQLLYPMDAAMGGRLGDTLLVNGRPNPTLEVRPGERVRLRLLNASNARIYRLA
LSDGRPFTVIATDGGLLPAPVEVDELLLAPGERADVLVDFSADPGEEVTLANPFEGRSGRALLTLRVTGA
AASAPLPANLAPLPDLEDREAVRTRELVLTGGMAGYVWTINGKAFDPDRPDLTVKLGERERWTLVNDTMM
PHPFHLHGHQFQVLSRNGKPPPEGGWKDTVLVPPGETVRILFRFDNYPGDWMFHCHILEHEDAGMMGQFE
VVP
>gnl|CDD|441736 COG2133, YliI, Glucose/arabinose dehydrogenase, beta-propeller fold [Carbohydrate transport and metabolism]
LLAALLLAGCSPAGALPAPTPTLPPGFTVEVVADGLDHPWGLAFLPDGRLLVTERAGRIRLLDDDGKLST
PVADLPVFAGGEGGLLGVALDPDFATNGYLYVAYTDPGGAGTRVARFTLSDGDTLTSEEVILDGLPAGGG
NHNGGRLAFGPDGKLYVSVGDRGNACEARGNAQDLNSLRGKILRIDPDGSIPADNPFVGTPGARPEIYAY
GHRNPQGLAFDPETGELWATEHGPDGGDELNRIEPGGNYGWPYCEGGQNYDPIGDSTPDAGLTDPVATWP
PGHAPSGLAFYTGDAFPAEYRGGLFVADLGSRRVVRVPLDGDGKVVGEEDFLTGAGGRPRDVAQGPDGAL
YVLDDNDGRIYRITY
>gnl|CDD|441737 COG2134, Cdh, CDP-diacylglycerol pyrophosphatase [Lipid transport and metabolism]
MQMRRALRLLIALLILLLAAAAAWPWLGAANSDALWKIVSQQCVPNQQQNGNPAPCAEVDLAAGYVVLKD
RNGPLQYLLIPTARISGIESPLLLEPATPNYFAQAWQARDLLSQRYGKPIPDDALSLAINSAYGRSQNQL
HIHISCLRPDVRAQLDAQAPQIGSQWQPLPGGLLGHRYLARRVTEEELAQRSPFRLLAEEVPGARDHMGR
YGLALAPLPDGDFVLLATRRDLLTLNRASAEELQDHDCAILKSLP
>gnl|CDD|441738 COG2135, SRAP, ssDNA abasic site-binding protein YedK/HMCES, SRAP family [Replication, recombination and repair]
MCGRYALTATPEELAERFGAEDAPGGDLEPRYNIAPTQPVPVVRETDDGPRELRLARWGLVPSWAKDPKK
GPRLINARAETVAEKPSFRAAFRRRRCLIPADGFYEWRKEGGKKQPYYIHRKDGEPFAFAGLWERWRDPD
GEWLLTFTILTTEANGLMAPIHDRMPVILPPEDWDAWLDPDLTDEELLALLRPYPAEELEAYPVSRAVNS
PRNDGPELIEPV
>gnl|CDD|441739 COG2136, IMP4, rRNA maturation protein Rpf1, contains Brix/IMP4 (anticodon-binding) domain [Translation, ribosomal structure and biogenesis]. rRNA maturation protein Rpf1, contains Brix/IMP4 (anticodon-binding) domain is part of the Pathway/BioSystem: 16S rRNA modification
LITTSRKPSQRTRSFCKDLSRVLPNSVYVNRGKKSLRDLLEEALELGADRLVIIGERKGNPGRLRFYDVE
GNELLSIGLILIGVKLSREIPGNVRIYNASSLVVKASEPVVSGAGELADLLSELLGFEAIESSYDVIVLI
RGDEKGIFEIEFLKSDGGPVGPLLRIKGVKLGD
>gnl|CDD|441740 COG2137, RecX, SOS response regulatory protein OraA/RecX, interacts with RecA [Posttranslational modification, protein turnover, chaperones]
KEDTEKKARNRALRLLARRERSRKELRRKLARKGFDEEEIEEVLDRLKEEGYLDDERFAESYVRSRLRRK
GYGPRRIRQELRQKGIDEELIEEALEELDEEDELEAARELARKKFGSLKPLDPAKEKQKLARFLARRGFS
SDLIRRVLRELLEE
>gnl|CDD|441741 COG2138, SirB, Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]. Sirohydrochlorin ferrochelatase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MMKTALLLVAHGSRDPEGAEEFEALAARLRARLPGLPVELAFLELAEPSLEEALDALVAQGATRIVVVPL
FLAAGGHVKEDIPEALAEARARYPGVRIRLAPPLGPDPRLADLLAERLAEALARPDTAVVLVGRGSSDPD
ANADVAKLARLLAERLGPVETAFLGTGPSLEEALERLRALGARRVVVLPYFLFPGVLTDRIADQVAGADV
VAEPLGPHPELADLVLDRYR
>gnl|CDD|441742 COG2139, RPL21A, Ribosomal protein L21E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L21E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MKRSHGFRSKTRKKLSKDPRERGTPPLSRLLQEFEEGDKVHIKIDPSVHKGMPHPRFHGKTGTVVGKRGR
AYKVEVKDGGKEKTLIVRPEHLKPQK
>gnl|CDD|441743 COG2140, OxdD, Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]. Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis
MTLAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINT
GDEPLVFLAVFDDDAGSDYGTISLSGWLAHTPPEVLAVDNPRYDK
>gnl|CDD|441744 COG2141, SsuD, Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase SsuD and methylene tetrahydromethanopterin reductase) [Coenzyme transport and metabolism, General function prediction only]. Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase SsuD and methylene tetrahydromethanopterin reductase) is part of the Pathway/BioSystem: Pyrimidine degradation
AERLGFDRVWVADHHFPPGGASPDPWVLLAALAAATSRIRLGTGVVVLPLRHPLVVAEQFATLDHLSGGR
LDLGVGRGWGPDEFAAFGLDHDERYERFEEALEVLRRLWTGEPVTFEGEFFTVEGARLVPRPVQGPHPPI
WIAGSSPAGARLAARLGDGVFTAGGTPEELAEAIAAYREAAAAAGRDPDDLRVSVGLHVIVAETDEEARE
RARPYLRALLALPRGRPPEEAEEGLTVREDLLELLGAALVGTPEQVAERLEELAEAAGVDEFLLQFPGLD
PEDRLRSLELFAEEVLPLLRR
>gnl|CDD|441745 COG2142, SdhD, Succinate dehydrogenase, hydrophobic anchor subunit [Energy production and conversion]
MVYRTPLKRARGLGSAKSGTHHWLLQRVTAVALVVLVLWFLFFLLSLPGADYAEVAAWFASPFWAILTLL
FLLSALYHAWLGLRVVIEDYVHGTGLRLALLLLLTLALVALAAAGVFALLRIAL
>gnl|CDD|441746 COG2143, SoxW, Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones]
MKKLLLLLLLLLLLAAAAAAQEISFLLDLEEDLALAKAEGKPILLFFESDWCPYCKKLHKEVFSDPEVAA
YLKENFVVVQLDAEGDKEVTDFDGETLTEKELARKYGVRGTPTLVFFDAEGKEIARIPGYLKPETFLALL
KYVAEG
>gnl|CDD|441747 COG2144, COG2144, Selenophosphate synthetase-related protein [General function prediction only]
MMDLAALAAELRNFPGVTRKRDIADVVRALGLASSGGTAAAFGDDAAAIPDGDGYLLLAAEGIWPKFVEA
DPWFAGYCSVLVNVSDIAAMGGRPLAVVDALWSSDEEAAAPVLAGMRAASRKFGVPIVGGHTHPDTPYNA
LAVAILGRAKKLLTSFTARPGDRLIAAIDLDGRYHPPFPYWDATTGKPPERLRAQLELLPELAEAGLVTA
AKDISNPGIIGTLGMLLECSGVGATIDLDAIPRPEGVDLERWLKAFPSFGFLLTVPPENVDEVLARFAAR
GITAAVIGEVTDSRRLTLRDGGERATFFDFSKEPLTGCGPKAA
>gnl|CDD|441748 COG2145, ThiM, Hydroxyethylthiazole kinase, sugar kinase family [Coenzyme transport and metabolism]. Hydroxyethylthiazole kinase, sugar kinase family is part of the Pathway/BioSystem: Thiamine biosynthesis
MEQIAEALEAVREKKPLVHCITNYVVMNDTANVLLAIGASPAMADAPEEVAEMAAIASALVINIGTLTPE
QVEAMLLAGKAANEAGKPVVLDPVGVGATPYRTETARRLLKELKPTVIRGNASEIAALAGEGGGGKGVDS
TDSSDDALEAAKALARKYGTVVAVTGETDYVTDGERVYRVSNGHPLMTKVTGTGCMLGALIAAFLAVEED
PLEAAVAALAVMGIAGELAAEKAQGPGSFRVALLDALYLLTPEDLAERARIEEV
>gnl|CDD|441749 COG2146, NirD, Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]
MSEVKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFD
LRTGECLGGPATEPLKTYPVRVEDGDVYVDLPE
>gnl|CDD|441750 COG2147, RPL19A, Ribosomal protein L19E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L19E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MMDLSAQKRLAADILGVGVNRVWIDPERLDEIADAITREDIRELIKEGVIKAKPKKGNSRGRARERKEKR
KKGRRRGPGSRKGKKGARTPKKERWMKKIRALRRYLKELRDDGEIDRSTYRKLYRKAKGGEFRSVAHLKS
YIEEHGLL
>gnl|CDD|441751 COG2148, WcaJ, Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane/envelope biogenesis]
RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLL
LLIAAAVVVVIIVLLALLLRELLLLLLLLLLRLLGVVAELGRVSLSELGGLPLLSVRGPPLSGYQRVLKR
LFDIVLALLGLILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDAEKLLGAVFKLK
NDPRITRVGRFLRKTSLDELPQLWNVLKGDMSLVGPRPELPEEVELYEEEEYRRRLLVKPGITGLAQVNG
RNGETFEERVELDLYYIENWSLWLDLKILLKTVLVVLKGKGA
>gnl|CDD|441752 COG2149, YidH, Uncharacterized membrane protein YidH, DUF202 family [Function unknown]
MSERSPRLVYDRGELPDPRFHLANERTFLAWIRTALALIAFGFAIERFGLFLRPLALSLPGLSRVLGLAL
VLLGALLAVLAYIRYRRVERALRRGEPLPSSRLALLLAVAVALLGLLLLVYLLLRA
>gnl|CDD|441753 COG2150, COG2150, Predicted regulator of amino acid metabolism, contains ACT domain [General function prediction only]
MWDEILEKFEDYPSQQKVIRLLLERGFSVNEEGKVYCGDIEIPITQIARAAGVDRRVVDSTIEAILEDPE
LRRIFSNIRPMPSLSDVAPLLGLGVIEIEPDDADYPGILAAVANVLADHGISIRQIVSEDPEFTEEPKLT
IITEGPIPGDVIEELRKLPGVKRVSIY
>gnl|CDD|441754 COG2151, PaaD, Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, chaperones]
SEETAEPLEEEVWEALKTVYDPEIPVNIVDLGLIYDVEVDDDGRVKVTMTLTTPGCPAADVIPDDVEEAL
EEVPGVEDVEVELVWDPPWTPDRMSEEARLKL
>gnl|CDD|441755 COG2152, COG2152, Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism]
NGILKRYPGNPILTPNDMPRWEVNAVFNPGAVRFNGKFLLLYRVEGRDGKSHLGLARSDDGINFRRDDEP
ILFPETDYEDTGVEDPRITKIDGRYYITYTAYSGAGARIGLARTKDFKTWERLGLIFPPDNKDAVLFPEK
INGKYALLHRPSDGFHTGGPDIWISYSPDLEHWGDHRIVMGPRPGTWDSLKIGAGPPPIKTEEGWLLIYH
GVRNTAAGLVYRLGAALLDLEDPSKVIARSPEPILEPEEEYERVGDVPNVVFPCGAVVDEDGTVYIYYGA
ADTRIALATATLDELLDYLKNTPE
>gnl|CDD|441756 COG2153, ElaA, Predicted N-acyltransferase, GNAT family [General function prediction only]
AEELYDALALRREVFVVEQGVPPYLELDGKDEDARHLLAYDDGELVATARLLPPGDGEAKIGRVAVLPEY
RGQGLGRALMEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAGIPHIDMRKPLS
>gnl|CDD|441757 COG2154, PhhB, Pterin-4a-carbinolamine dehydratase [Coenzyme transport and metabolism]
MAEPPLTDEEIAAALAELPGWELEDGALERTFKFKDFAEALAFVNRVAELAEAEDHHPDISNRYNRVTVT
LTTHDAGGLTENDFILAAKIDALAAALGA
>gnl|CDD|441758 COG2155, YuzA, Uncharacterized membrane protein YuzA, DUF378 family [Function unknown]
MKTLDRIALILVIIGALNWGLIGLFQFDLVAALFGGQASALSRIIYILVGLAGLYSLSLLFRIRKKPERE
>gnl|CDD|441759 COG2156, KdpC, K+-transporting ATPase, KdpC subunit [Inorganic ion transport and metabolism]
LRQLRPALRLLLVLTLLTGLAYPLAVTGIAQLLFPGQANGSLIEVDGKVVGSALIGQPFTDPRYFHGRPS
ATGDSPYNAAASGGSNLGPTNPALLKRVEERIAALRAANPGAPAPVPADLVTASGSGLDPHISPAAALYQ
VPRVAKARGLPEAQVRALVAEHTEGRQLGILGEPRVNVLKLNLALDAL
>gnl|CDD|441760 COG2157, RPL20A, Ribosomal protein L20A (L18A) [Translation, ribosomal structure and biogenesis]. Ribosomal protein L20A (L18A) is part of the Pathway/BioSystem: Archaeal ribosomal proteins
EMKVFRVKGTFKAGDGWQKFTKEVRALNEKVAREKVYSEIGSKHKLKRTQIKIEEVEEISPEEVTDPVVK
KLAKL
>gnl|CDD|441761 COG2158, COG2158, Uncharacterized conserved protein, contains a Zn-finger-like domain [General function prediction only]
MREKLKKVEESYKFFSNRDCEYYPCHFEGQNCLFCYCPLYPCGDEECGGNWIYSSDGGGVWSCSDCTLPH
EPEVYDFILKKLKELGDWPGDPEAKKKELKKVRRKTL
>gnl|CDD|441762 COG2159, LigW, 5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism]
MMIIDVHTHLGTPEERLADMDEAGIDKAVLSPTPLADPELAALARAANDWLAELVARYPDRFIGFATVDP
QDPDAAVEELERAVEELGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYY
AAPLILSGVAERFPDLKFILAHGGGPWLPELLGRLLKRLPNVYFDTSGVFPRPEALRELLETLGADRILF
GSDYPHWDPPEALEALEELPGLSEEDREKILGGNAARLLGLDA
>gnl|CDD|441763 COG2160, AraA, L-arabinose isomerase [Carbohydrate transport and metabolism]
MNDLKNLEVWFVTGSQHLYGPELLEQVAEYSQEIAEKLNASGKIPVEVVDKGVVDTPEEIRAACLEANAD
EDCDGVITWMHTFSPAKMWIPGLQALQKPLLHLHTQPNRAIPWDTIDMDFMNLNQSAHGDREFGFIFTRM
GIPRKVVVGHWQDPEVWEEIGDWMRAAAAWHDLRHLRVARFGDNMRGVAVTEGDKVEAQIKFGYHVNTYE
VGDLVEYVNAVSDAEVDALVAEYEETYDVAPELRKGGERRESLRRAARIELGLRKFLEDGGLGAFTYYFE
DLGGLKQLPGLAVQRLMADGYGFGGEGDWKTAALMRIMKVMGAGLPGGGSFMEDYTYDFEPGDDLVLGAH
MLEVCPSIAAGKPRLEVHPLGIGGKGDPARLVFTVKPGPATNLSLVDMGDRFRLLVNEVESVEPPEPLPK
LPVARARWKPKPDLRTFAEAWILAGGAHHTALSQGHTAEQLEDFAELLGIELVVIDEDTTLRQFKNELRW
NEAYY
>gnl|CDD|441764 COG2161, StbD, Antitoxin component YafN of the YafNO toxin-antitoxin module, PHD/YefM family [Defense mechanisms]
MTTISYSEARKNLASLLDQVVEDHEPVIITRRNGPAAVLISAEDYESLQETLYLLSSPANAERLLESLAE
LEAGEVSLDELIE
>gnl|CDD|441765 COG2162, NhoA, Arylamine N-acetyltransferase [Secondary metabolites biosynthesis, transport and catabolism]
TAFDLDAYLARIGYSGPPAPTLETLRALHRAHVRAIPFENLDVLLGRPISLDPDALFDKLVRRRRGGYCY
ELNGLFAALLEALGFDVTLLAARVRWGGPGGPGPPRTHMALLVTLDGERWLVDVGFGGGTPLEPLPLEDG
TEQDQPGGTYRLVRSDDGEWVLQRRVDGGWRPLYRFDLEPQELADFEVANWYTSTHPDSPFVGNLLVARA
TPDGRVTLRGRRLTRRRGGGEEERTLLSAEELAAVLRERFGLDLDD
>gnl|CDD|441766 COG2163, RPL14A, Ribosomal protein L14E/L6E/L27E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L14E/L6E/L27E is part of the Pathway/BioSystem: Ribosome 50S subunit
PEIEIGQVVRSKAGRDAGRYFVVVDIIDDNFVLVADGDKRKVEKPKKKNIKHLQPTDKVIEEIKEKLLEG
GRVTNAEIRKALEELGLE
>gnl|CDD|441767 COG2164, COG2164, Uncharacterized protein with cyclophilin fold, contains DUF369 domain [General function prediction only]
MKIRITIGDVELEAELDDTPTARAIWDALPFESTANRWGDEIYFEIPVDVPLEENAREVVEVGDIAYWPP
GNALCIFFGPTPISRGGEIRPASPVNVIGRIVGDVSDLKSVKDGERVRVERA
>gnl|CDD|441768 COG2165, PulG, Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
MKLRRRRRRQRGFTLIELLVVIAIIGILAALALPALQGARERARRAELRSNLRQIQQALERYRLDNGRYP
SSLTGLLADVRGGGYLGSNGLPPAGTPCD
>gnl|CDD|441769 COG2166, SufE, Sulfur transfer protein SufE, Fe-S cluster assembly [Posttranslational modification, protein turnover, chaperones]
MTMSLPEALDEIVEEFALLDDWEDRYRYLIELGKKLPPLPEELKTEENKVPGCQSQVWLVAELDDGKLHF
RADSDAPIVRGLIALLLAGLSGLTPEEILAVDPDFFEELGLTEHLSPSRSNGLAAMLKRIKRQARAYLAA
>gnl|CDD|441770 COG2167, RPL39, Ribosomal protein L39E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L39E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MARNKPLGKKLRLAKALKQNRRVPAWVIVKTNRKVRRNPKRRNWRRSKLKV
>gnl|CDD|441771 COG2168, TusB, Sulfur transfer complex TusBCD TusB component, DsrH family [Translation, ribosomal structure and biogenesis]
MLHTVSKSPFETNDLDSCLRLLTPGDALLLIQDGVYAALKGSRALALLLAAPIKVYALKEDLEARGLTAQ
ISDGVKLIDYAGFVELTEKHDKQISW
>gnl|CDD|441772 COG2169, AdaA, Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair]
MTTDLLDDDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKR
CRPDLAPGSPPRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLR
ARQLLQTGLSVTDAAYAAGFGSLSRFYEAFKKLLGMTPSAYRRGGAGAAIRFAPTPCSLGLLLVAASARG
VCAILLGDDPEALLRDLQDRFPAAELIGGDAAFEQLVAEVVGFVEGPLLGLDLPLDLRGTAFQQRVWQAL
RAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIPCHRVVRADGALSGYRWGVERKRALLEREA
AAAAAAAA
>gnl|CDD|441773 COG2170, YbdK, Gamma-glutamyl:cysteine ligase YbdK, ATP-grasp superfamily [Posttranslational modification, protein turnover, chaperones]
MSLEFASSEPLTLGVEEELQLVDPETGDLVPRADEVLAALRGDLGGRVKPELLQSQVEIATGVCTTLAEA
RAELRALRRALAAAAARLGLRLAAAGTHPFADWRDQPITDKPRYRRLAERYGYLARQMLICGLHVHVGVP
DRDEAVRVLNRLRPWLPHLLALSASSPFWQGRDTGYASYRLLVFQRLPTAGLPPYFASWAEYERYVDDLV
RTGVIEDIKMIYWDIRPSPRFPTVEVRVCDVPLTVEEAVALAALVRALVRTLLRELDAGEPLPPVPPWLL
RENKWRAARYGLDGELIDPGTGREVPARDLLRELLERLRPVAEELGCLDELELLRRILRRGTGADRQRAV
FARTGSLRAVVDLLVAETAAGLP
>gnl|CDD|441774 COG2171, DapD, Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]. Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis
MADLGTVIDAAWENRAELTPLADREVREAVEEVIAALDAGPLRVAEPNLDGEWVVNEWVKKAILLSFRLE
DNRVLEGGGVTYHDKVPLKFDYFKPAGVRIVPGARVRLGAYLAPGVVLMPSFVNIGAYVDEGTMVDTWAT
VGSCAQIGKNVHLSGGAGIGGVLEPLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTKIY
DRVTGEVYYGRVPAGSVVVPGSLPGKDGDYGLYCAVIVKRRDEKTRSKTSLNELLRDN
>gnl|CDD|441775 COG2172, RsbW, Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]
SLSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGDPDGPVEVELELDPDGL
EIEVRDEGPGFDPEDLPDPYSTLAEGGRGLFLIRRLMDEVEYESDPGGTTVRLVKRL
>gnl|CDD|441776 COG2173, DdpX, D-alanyl-D-alanine dipeptidase [Cell wall/membrane/envelope biogenesis]
MKRLKPAQAECPEGLVDIADVDPGIRLDLRYATPDNFTGRPVPYGAPRCYLRRPAAEALAKAQAELAAQG
LRLKIFDAYRPQSAQQHFWDALPDDLRMKYPDVDKAELFVRGYVADPARGSPHSRGAAVDLTLVDATGKE
LDMGTGFDEFSPRSHPDYPGLTAEARANRRLLREAMEAAGFTNYPTEWWHFDLGDEMPYPVLDFPVE
>gnl|CDD|441777 COG2174, RPL34A, Ribosomal protein L34E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L34E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
RPRYRSRSYRRVYVRTPGGRTVIHYERRKPSKARCAICGRPLNGVPRGRPVEIRKLSKTEKRPERPYGGY
LCPKCLRKLIKAEARSSS
>gnl|CDD|441778 COG2175, TauD, Taurine dioxygenase, alpha-ketoglutarate-dependent [Secondary metabolites biosynthesis, transport and catabolism]
SSLTIRPLTPAIGAEITGVDLAAPLSDATVAELRAALLEHGVLVFRGQPLTDEQQVAFARRFGELEIHPT
RPYNLPGHPEIFDVSNDPADGYTNAGLPWHTDGSFRERPPKGSILYCVEVPPEGGDTLFADMAAAYEALP
EELKELLEGLRAVHSFNKDYGRGRPDPEELREEDDASVPPVEHPVVRTHPETGRKVLYVNEGFTTRIVGL
SPEESRALLDELFAHATRPEFTYRHRWQPGDLVIWDNRRTLHGATADYGPGRRVLHRVTIAGDVP
>gnl|CDD|441779 COG2176, PolC, DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]
MSLDLEDLTYVVFDLETTGLSPKKDEIIEIGAVKVENGEIVDRFSTLVNPGRPIPPFITELTGITDEMVA
DAPPFEEVLPEFLEFLGDAVLVAHNASFDLGFLNAALKRLGLPFDNPVLDTLELARRLLPELKSYKLDTL
AERLGIPLEDRHRALGDAEATAELFLKLLEKLEEKGITTLR
>gnl|CDD|441780 COG2177, FtsX, Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning]
MRLLYALREALRGLRRNPLMTLASILVIALALLLLGLFLLLLLNANQLASQLEDEVEISVYLKDDATEAQ
IAALEEKLRALPGVASVRYISKEEALEELKEWLGESDLLELLDENPLPASIEVKLKPEDPEDLEALAAAL
EALPGVAEVDYDREWVERLFALLNLLRLVGLVLAALLLLAAVLLIGNTIRLAIYSRREEIEIMKLVGATD
GFIRRPFLLEGALLGLLGGLLALLLLALLYLLLVSALADGLAFLSLLSLGGLLLLLLLLLLLLGALLGAL
GSRLAVRRYLRV
>gnl|CDD|441781 COG2178, COG2178, Predicted RNA- or ssDNA-binding protein, translin family [General function prediction only]
KLKEIIEEIREELEEKDEAREEALKLSREIIRLSGNAIRAIHRGELEEAEELLDEARELVEELKELLKEY
PDLYYSGYVQDALQEYVEASILYAIIRGEEIPSPEELGVPPAAYLLGLADAIGELRRHILDLLRKGDLEE
AERLLEIMEEIYEELMTFDYPDALTPGLRRKTDVARGLIERTRGDLTLAKRQKKLEKALKKFEKR
>gnl|CDD|441782 COG2179, YqeG, Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only]
LKLLKPDEYVKSIYDIDPEKLKEKGIKGLILDLDNTLVPWDEPEATPEVIEWLEELKEAGFKVCIVSNNS
EKRVKRFAEKLGIPYIARAKKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKPLVD
KEFWFTRINRFLERRILKRLKKKG
>gnl|CDD|441783 COG2180, NarJ, Nitrate reductase assembly protein NarJ, required for insertion of molybdenum cofactor [Energy production and conversion, Inorganic ion transport and metabolism, Posttranslational modification, protein turnover, chaperones]
MEAQRMKTLKALSLLLDYPDEELLAALPELRAALAEAAAREALAAFLDHLAALDLLDLQEEYVETFDRGR
RTSLYLFEHVHGESRDRGQALVDLKELYRAAGLELDDGELPDYLPLVLEFLATLDPEEARALLGDIRHGL
ELLRARLEERGSPYAALFDALLALLPAAAEAEAAVARLIAE
>gnl|CDD|441784 COG2181, NarI, Nitrate reductase gamma subunit [Energy production and conversion, Inorganic ion transport and metabolism]
FLFGIYPYIALAVFVVGSIYRYRRDQYGWTSRSSQLLEKRLLRWGSPLFHFGILFVFAGHLVGLLTPGSW
TDALGISEHLYQLLAVVLGGIAGVLALIGLLILLYRRLTDPRVRATSTPSDYFILLLLLAQLLLGLLTTL
VSAGHLDGDYRETVSPWFRSLLTFQPGAAELMAGVPLIFKLHILLGMTLFALFPFTRLVHVWSAPVGYLF
RPYQVVRSRRRRNLRIGPAL
>gnl|CDD|441785 COG2182, MalE, Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]
MKRRLLAALALALALALALAACGSGSSSSGSSSAAGAGGTLTVWVDDDEAEALEEAAAAFEEEPGIKVKV
VEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKDDFLPAALDAVTYDGKLYG
VPYAVETLALYYNKDLVKAEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFYPFLAAFGGYLFGKDGD
DPKDVGLNSPGAVAALEYLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADLKKALGIDYGVA
PLPTLAGGKPAKPFVGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVKAD
PLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPAEALDAAQKQIEAAIAQ
>gnl|CDD|441786 COG2183, Tex, Transcriptional accessory protein Tex/SPT6 [Transcription]
MMMDIIQRIAQELGLRPKQVEAAVELLDEGATVPFIARYRKEATGGLDEVQLRTIEERLTYLRELEKRRE
TILKSIEEQGKLTPELKAKIEAADTKQELEDLYLPYKPKRRTKATIAREKGLEPLADLLLAQPTGDPEAE
AAKYINEEKGVADVEAALDGARDILAERISEDAELRGKLRELLWKEGVLVSKVKKGKEEEGAKFRDYFDY
SEPLKKIPSHRILALNRGEKEGVLKVKLEPDEEEAEAYIARRFIKDQGRPADEWLKEAVRDAYKRLLAPS
LERELRNELKEKAEEEAIKVFAENLRDLLLAAPAGGKVVLGLDPGFRTGCKVAVVDETGKLLDTATIYPH
PPQNKWEEAAKTLAALIKKYKVELIAIGNGTASRETEQFVAELIKELDLKVQYVIVSEAGASVYSASELA
REEFPDLDVTVRGAVSIARRLQDPLAELVKIDPKSIGVGQYQHDVNQKKLKRSLDAVVEDCVNAVGVDLN
TASAPLLSYVSGLNPTLAKNIVAYRDENGAFKSRKELLKVPRLGPKAFEQAAGFLRIRDGDNPLDNSAVH
PESYPVVEKILKDLGVSVKDLIGNKELLKKLDPEKYADELFGLPTLRDILKELEKPGRDPRPEFKTPTFR
EGVLKIEDLKPGMILEGTVTNVTDFGAFVDIGVHQDGLVHISQLSDRFVKDPREVVKVGDIVKVKVLEVD
LKRKRISLSMKLDDEAGAA
>gnl|CDD|441787 COG2184, FIDO, Fido, protein-threonine AMPylation domain [Signal transduction mechanisms]
GDMFDPYLYPGTTVLRNKLGITDAAELDEAEAELTALRAAELFERPPPGVFDLAHLKAIHRRLFGDVYDW
AGQIRTVNISKGGTRFAPPSFIERELEALFDDLREENYLRGLDREEFAERLARFHGELNVIHPFREGNGR
TQRLFFDQLARQAGYPLDWSRVDKEEYLEALIAADNGDYSPLKALFRDALTPARES
>gnl|CDD|441788 COG2185, Sbm, Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and metabolism]
EAFAEKTGRRPRVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVSSL
DGGHLELVPELIELLKEAGAGDILVVVGGVIPPEDIEALKAAGVDAVFGPGTDLEEIIEDLLEL
>gnl|CDD|441789 COG2186, FadR, DNA-binding transcriptional regulator, FadR family [Transcription]
KPIRRRSLAEQVAEQLRELILSGELKPGDRLPSERELAEQLGVSRTTVREALRALEALGLVEVRQGGGTF
VREPSPWALLDPLALLLALDDASLRDLLEARLALEPEAARLAAERATDEDLARLEAALAEMEAAADDGEA
FAEADLAFHRAIAEASGNPLLALLLESLRELLRRSVRLTLRSPEARERSLAEHRAILDAIRAGDPEAARA
AMRAHLEAVRERLREALAERAR
>gnl|CDD|441790 COG2187, COG2187, Aminoglycoside phosphotransferase family enzyme [General function prediction only]
MTDAADQAALIAFLSDPAAYPHPVEPVELIETHISWVFLTGDYAYKLKKPVDFGFLDFSTLEKRRHFCEE
ELRLNRRLAPDLYLGVVPITRTADGLALGGDGEPVEYAVKMRRFPQEALLDRLAARGELTPALIDALART
LAAFHARAPTAPDISAFGGPEAVRANLDENFEQLRAYLGDLLDAAQLAALRAWTRAFLARLAPLLEARRR
AGFVRECHGDLHLGNICLIDGKPVLFDCIEFNERLRWIDVLYDLAFLLMDLEARGRPDLANRFLNRYLEA
TGDYEGLALLPFYLSYRAAVRAKVAAFRLADPADEAERAAALAEARRYLDLALRYLAPPPP
>gnl|CDD|441791 COG2188, MngR, DNA-binding transcriptional regulator, GntR family [Transcription]
SSPVPLYLQIADALRERIESGELPPGDRLPSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTFVA
EPKIEYPLSRLTSFTEELRARGREPSTRVLSAERVPADEEVAEALGLPPGAPVLRIERLRLADGEPVALE
TSYLPAALFPGLLEEDLETGSLYELLEERYGLRITRAEQRIEAVLADAEEAELLGVPPGAPVLVIERVTY
DADGRPVEYSRSYYRGDRYRFVVELRRR
>gnl|CDD|441792 COG2189, Mod, Adenine specific DNA methylase Mod [Replication, recombination and repair]
GLTWPGKREALLAANTPIAKTLRPCPEESVDFDTTENLLIEGDNLEALKLLQESYAGKVKCIYIDPPYNT
GNDFFAYNDNFETESNGRFHSSWLSMMYPRLKLARELLSEDGVIFVSIDDNEVHYLKLLLDEIFGEENFV
ATIIWKKKSSGKNDAKFFSRTHEYILVYAKNKSYLKFNGLPRTEEQLKRYKNPDNDPRGRWRSVPLTAPG
GRPNLFYPIEHPSTGKEVYPGRGWRWSKETMEELIADGRIYFGKDGNGVPRRKRYLDEVKKGVVPTTIWD
DIGTNQNGTKELKELFGGKVFDTPKPEKLLKRIIEIATNPGDLVLDFFAGSGTTAHAVMKLNAEDGGNRR
FILVQLGEYADTVTKERLRRVIDGISKGVGQGGGGFRYYELATALTSEAALALKRARLDIAALRKERARR
KLKLERVEKEGTSALKVLADVLDDVDDDELKAVLAVELLLLALDDAVEDLVLTDLALLLLVLLLLLLLDL
L
>gnl|CDD|441793 COG2190, NagE, Phosphotransferase system IIA component [Carbohydrate transport and metabolism]
KKSKTLTIYAPVSGEVVPLSEVPDPVFASKMMGDGVAIEPTGGKVVAPVDGTVTSVFPTKHAIGLTSDDG
LEVLIHIGIDTVKLNGEGFTVLVKEGDKVKAGDPLIEFDLDAIKAAGYSLITPVVVTNSDEYKSVELTKS
GQVKAGDPLLTVKL
>gnl|CDD|441794 COG2191, FwdE, Formylmethanofuran dehydrogenase subunit E [Energy production and conversion]
KPDLEELLEKAVEFHGHLCPGLAIGYRAAEAALELLGIERSEDEELVAIVETDACGVDAVQVLTGCTLGK
GNLIYRDYGKMAFTFVDRKTGKAVRVVLKPEKREKAPEFAELRKKVVPGEFEEDREELIEAILEAPEEEL
FSIEEVDVELPEKARIFESVICEVCGEPVMESRARLKDGKIVCIPCAGGKYY
>gnl|CDD|441795 COG2192, COG2192, Predicted carbamoyl transferase, NodU family [General function prediction only]
MYILGISAFYHDSAAALVVDGEIVAAAEEERFTRIKHDKAFPRNAIRYCLAEAGITLADVDAVAFYWKPL
LKFERLLETYLARAPRGLRSFLRALPGWLREKLFLKRLLRRELDGPRPKVLFVEHHLAHAASAFFPSPFE
EAAVLTIDGVGEWATTSIGHGRGGRIELLKEIRFPHSLGLLYSAFTYYLGFKVNSGEYKVMGLAPYGKPR
YVDLLLRELIDLKDDGSFRLNMDYFNYATGLRMTSEKLEELFGGPPRRPEDPLTQRHADLAASVQAVLEE
VVLHLARHLHERTGSRNLCLAGGVALNCVANGRILREGPFEDVWVQPAAGDAGTALGAALAVAHQLLGQP
RVDAMRGAYLGPSFSDEEIEAALRAAGLPYERLEDDLAEAVAELLAEGKVVGWFQGRMEFGPRALGNRSI
LADPRRPEMQDRLNLKIKFRESFRPFAPSVLAERAAEYFELDQPSPYMLFVAPVRPEKRSRIPAVTHVDG
TARVQTVDRETNPRYHALLEAFERLTGVPVLLNTSFNVRGEPIVCTPEDALRCFMRTGLDALVIGDFLLE
KPDQPAWP
>gnl|CDD|441796 COG2193, Bfr, Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism]
GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQ
DLGKLRIGEDVEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIE
KIGLQNYLQSQM
>gnl|CDD|441797 COG2194, OpgE, Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis]
KFLLPRLSPLKLILLLALYFALFLNLPFWGRLLAILPLDGVNLLFLLSLPLLLLAALNLLLSLLAWRYLF
KPLLILLLLISAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIR
YRPLLRELGQRLALLLLALLVIVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLP
LQPLGADAKLAAAGAKPTLVVLVVGETARADNFSLNGYARDTTPELAKEKNLVSFRDVTSCGTATAVSVP
CMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRDNQSGCKGVCDRVPTIDLTADNLPPLCDGGECLD
EVLLDGLDEALADLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFTPTCDTNDLQNCSREELVNAYDNTILY
TDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTHVPMIMWLSDGYAQRYG
IDFACLKARADKPYSHDNLFHTLLGLLDVRTSVYDPELDILAPCRRA
>gnl|CDD|441798 COG2195, PepD2, Di- or tripeptidase [Amino acid transport and metabolism]
NPERLLERFLEYVKIPTPSDHEEALADYLVEELKELGLEVEEDEAGNVIATLPATPGYNVPTIGLQAHMD
TVPQFPGDGIKPQIDGGLITADGTTTLGADDKAGVAAILAALEYLKEPEIPHGPIEVLFTPDEEIGLRGA
KALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIKLAARFLAALPLGR
IPEETEGNEGFIHGGSATNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGVGVVEVEIEDQY
PNWKPEPDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESME
KAWELLVEILKLIA
>gnl|CDD|441799 COG2197, CitB, DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription]
MIRVLIVDDHPLVREGLRALLEAEPDIEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRLL
TPREREVLRLLAEGLSNKEIAERLGISERTVKTHVSNILRKLGVRNRTELVLLALRLGLLD
>gnl|CDD|441800 COG2198, HPtr, HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms]
LALLLLALLLLLLLLLLLLLLLLALLALLLLLLLAALALLLLLLLLLALLALLLLLVALALLLALLLLLL
GVLLLLLDLLELLLLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLL
LLALLLLLLLLLVLAALLLLLLLALLLALLLLVLLVLLLLLLLLLLLLLLLLLLLLLLLLALTLAALLEL
LAAELALEALLAELAAEAAAALAAELALAELAALLLLLLLLLLLLILLLLLLLLLLLLLLLLLLLLLLLL
LLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLA
LLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSLLLLLLLLLLL
LLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLL
LLLLLLLLLLLLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLAL
LLGLGLLLGLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLL
LLLLLLLLLLLLLLLLLLLLLLAVLLAAAAAAAALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAA
IAAAAAAAAAAAAAAAAAAAALLAALLLLLLLLLLLLLLLLLLLLAAAAAAAASPAAPALPVLDLEALRR
LGGDPELLRELLELFLEELPELLAELRQALAAGDLEALARLAHKLKGSAGNLGAPRLAELAAELEQAARA
GDLEEAEELLAELEAELERVLAALEALLAEE
>gnl|CDD|441801 COG2199, GGDEF, GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms]
VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLL
LLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARAR
REGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAE
ALAERLREALEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY
>gnl|CDD|441802 COG2200, EAL, EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms]
LLLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLL
LLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLA
LELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLL
LLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGG
GAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARARRRLALESELREALEEGELRLYYQPIV
DLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDLRLSVNL
SARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSL
SYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGY
LFGRPLPLEELEALLR
>gnl|CDD|441803 COG2201, CheB, Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains [Signal transduction mechanisms]
MPFKVVAIGASTGGPEALEEVLSALPADFPAPIVIVQHMPPGFTSSLAERLNRLTALPVKEAEDGERLEP
GHVYIAPGGRHLEVERSGGYRLRLSDGPPVNGHRPSVDVLFRSLAEVYGERAVGVILTGMGSDGAEGLKA
IKEAGGLTIAQDEESCVVYGMPRAAIEAGAVDEVLPLEEIAAALLRLLRRRAA
>gnl|CDD|441804 COG2202, PAS, PAS domain [Signal transduction mechanisms]
TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLE
LLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLR
LLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYE
LELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRDITERKRAEEAL
>gnl|CDD|441805 COG2203, GAF, GAF domain [Signal transduction mechanisms]
LLSVLALALAREVAAAELLEELATLLLALLLLALQALERVLETTELALALELLLERLTELRAAARLAAEA
AEAALLLILLIDALVLLSLVATAGLVLELADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGR
LRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALDLEE
LLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLGEGLAGRALRTGEPVVVNDAST
DPRFAPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARLY
EALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEG
LLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLL
LLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLEREL
LTLVGVLLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTV
LVVLAAVEDSALLLRLALALASLVLLRALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLG
VARLLQLSVLEV
>gnl|CDD|441806 COG2204, AtoC, DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms]
SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRA
LDPDLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSGLIGRSPAM
QEVRRLIEKVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAF
TGAVARRIGKFELADGGTLFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEEL
VEEGRFREDLYYRLNVFPIELPPLRERREDIPLLARHFLARFAAELGKPVKLSPEALEALLAYDWPGNVR
ELENVIERAVILADGEVITAEDLPEALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG
>gnl|CDD|441807 COG2205, KdpD, K+-sensing histidine kinase KdpD [Signal transduction mechanisms]
ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSPEERRELLEIIRESAERLLRLI
EDLLDLSRLESGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANL
LDNAIKYSPPGGTITISARREGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEGGTGLGLAIVKRI
VEAHGGTIWVESEPGGGTTFTVTLPLAES
>gnl|CDD|441808 COG2206, HDGYP, HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms]
LLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLLLALLALLLLLLLLLALLALLLALLALLLLLL
LLLLLLSLLLAVALLLAELLLLLAALESLLAELFEELRLGLLEELKKLVEELDELLPDALLALLAALDAK
DPYTYGHSVRVAVLALALARELGLSEEELEDLGLAALLHDIGKIGIPDEILNKPGKLTDEEFEIIKKHPE
YGYEILKKLPGLSEVAEIVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPEE
ALEELRKGAGTQFDPELVEAFIKVLGIYPPVVEIDL
>gnl|CDD|441809 COG2207, AraC, AraC-type DNA-binding domain and AraC-containing proteins [Transcription]
LRLLILLLLLLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLL
LLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLL
LLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAK
RLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRARA
>gnl|CDD|441810 COG2208, RsbU, Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, Transcription]
LVLALLRAALLLLLELLLAAALLLLLLLLLAALLALELLALLLALLLLLLALLLLLLLLLALRLALLLLA
LLLALLLLAALLLLALLALALLLALLAALLLVLLLLLLLLLGLLAVALLLLLALLLLLALLLLALLLGLL
LLLLLLLLLAALLLALALALALALLLLLALAAALALLAALLLENARLEEEEKNRRLERELELARRIQRSL
LPPRLPEVPGLDIAARYRPADEVGGDFYDVFPLDDGRLAVVIGDVSGHGVPAALLMAMLRSALRALAREG
LDPAEVLERLNRALYEDLGGGRFVTAFLGVLDPETGRLTYANAGHPPPLLLRADGEVEELDGGGLPLGLL
PDAEYEEHEIPLEPGDRLLLYTDGLTEARNGDGELFGEERLLELLAENADLPAEELLDALLEALEEFRGG
GPQEDDITLLALRRR
>gnl|CDD|441811 COG2209, NqrE, Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrE [Energy production and conversion]. Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrE is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase
MEHLLSLFIKSIFIENMALAFFLGMCTFLAVSKKVKTAFGLGIAVIFVLTITVPLNWLIYNYLLKPGALA
WAGLADVDLSFLGLITFIGVIAAMVQILEMVLDKFSPALYNALGIFLPLITVNCAILGGSLFMVERDYNF
GESVVYGFGSGLGWALAIVALAAIREKLKYSDVPAGLRGLGITFITTGLMALAFMSFSGIKL
>gnl|CDD|441812 COG2210, YrkE, Peroxiredoxin family protein [Energy production and conversion]
KKKLTIIVFSGDLDKAYAALILANGAAAMGKEVTIFFTFWGLNALRKDKKDSLKKPLGNPMFGMMMPKGP
PKLPLSKPGMGGLGTKMMKKRMKKKGVASLEELLELAKELGVKLYACQMSMDLMGIKKEELIDGVEIGGA
ATFLEEAEEADINLFI
>gnl|CDD|441813 COG2211, MelB, Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism]
TAAKKKLSLKEKLAYGLGDLGLNLAFGLLSAYLLYFYTDVLGLSAALVGLILLVARLWDAITDPLIGALS
DRTRTRWGRRRPWILIGAIPLALSFVLLFTAPDLSPTGKLIYALVTYLLLGLAYTLVNIPYSALGAELTP
DYEERTRLSSWRFAFAGLGGLLASVLPPPLVAAFGGDAALGYRLTALIFAVLGLLAFLLTFFGTKERPVP
EEEKVSLKESLKALLKNRPFLLLLLAYLLFFLALALVAALLLYYFKYVLGLSAALVGLLLALYFLAALLG
APLWPRLAKRFGKKKAFIIGLLLAALGLLLLFFLGPGNLWLLLVLAALAGIGLGAILVLPWAMLADVVDY
DEWKTGRRREGLYFGIFTFAIKLGQALAGALAGLLLALFGYVAGAAQSPSALTGIRLLFFLLPAVLLLLA
ALLLLFYPLTRERHAEIRAELAARRAA
>gnl|CDD|441814 COG2212, MnhF, Multisubunit Na+/H+ antiporter, MnhF subunit [Inorganic ion transport and metabolism]
MMTTVLLIALALLALALLLALYRLIRGPTLADRVLALDTLGTNAVALLALLGILTGRPLYLDVALVLALL
GFVGTVAFARFLER
>gnl|CDD|441815 COG2213, MtlA, Phosphotransferase system, mannitol-specific IIBC component [Carbohydrate transport and metabolism]
TTAMKKGSARAKVQKFGRFLSGMVMPNIGAFIAWGLITALFIPTGWLPNETLAKLVGPMITYLLPLLIGY
TGGKMVYGVRGGVVGAIATMGVIVGADIPMFLGAMIMGPLGGWVIKKFDKLIEGKIKAGFEMLVNNFSAG
ILGMLLAILAFFAIGPVVEGLSNALAAGVEWLVNAGLLPLASIFIEPAKVLFLNNAINHGILTPLGIQQA
AETGKSILFLLEANPGPGLGILLAYMFFGKGSAKQSAPGAIIIHFFGGIHEIYFPYVLMKPLLILAVIAG
GMTGVFTFVLFGAGLVAPASPGSIFAVLAMTPKGSYLGVILGVLVAAAVSFLVASIILKRSKSKEDEDDL
EAATAKMEAMKGKSSSVASALTAAAAVGAADASNVKKIVFACDAGMGSSAMGASVLRKKVKKAGLDIEVT
NTAINNLPDDADLVITHKDLTERAKQKAPNAQHISVDNFLNSPKYDELVEKLKKQNDDS
>gnl|CDD|441816 COG2214, CbpA, Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]
MPDLKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEELFQRLNEAYEVLSDPERRAEYDR
ELGQSGKGSASQPSAAAQRLA
>gnl|CDD|441817 COG2215, RcnA, ABC-type nickel/cobalt efflux system, permease component RcnA [Inorganic ion transport and metabolism]
MEFHRALSGALRALREDPPGAGLLLLGLSFLYGVFHAAGPGHGKAVISSYLATHRATLRRALLLSLASAL
LQGLVAILLVGVLLVLLNLSARELTQASPWLEKASYALIALLGLWLLWRALRRLRRALRPAHVHDHHDCG
CGHAHLPDPEELAAAGSWRSALALILAIGLRPCSGAILVLLFALALGLFLWGVAAVLAMALGTALTVSAL
ALLAVYARRLAVRLSGGGSRWAARLLRGLELAGGLLIILLGLLLLLAALPA
>gnl|CDD|441818 COG2216, KdpB, K+ transport ATPase, ATPase subunit KdpB [Inorganic ion transport and metabolism]
MMSKKRKKRSLFDPALLRRALKDAFRKLDPRVQIRNPVMFVVEVGAILTTVLTILDLLGGGGGPAGFNLQ
ITLWLWFTVLFANFAEALAEGRGKAQADSLRKTRTDTVARRLVDDGTEEEVPASELRKGDVVLVEAGDII
PGDGEVIEGVASVDESAITGESAPVIRESGGDRSAVTGGTRVLSDWIVVRITANPGESFLDRMIALVEGA
KRQKTPNEIALTILLAGLTLIFLLVVVTLPPFAAYAGAPISVTVLIALLVCLIPTTIGGLLSAIGIAGMD
RLVQANVIAMSGRAVEAAGDVDTLLLDKTGTITLGNRQASEFIPVPGVSEEELADAAQLASLADETPEGR
SIVVLAKERGGLRERDLAPLGAEFVPFTAQTRMSGVDLPGGREIRKGAADAIKAYVRELGGTVPAELDAI
VEEIARSGGTPLVVAEDARVLGVIYLKDIVKPGIKERFAELRRMGIRTVMITGDNPLTAAAIAAEAGVDD
FLAEATPEDKLALIRREQAEGRLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAGNMVDLDSDPTKLI
EIVEIGKQLLMTRGALTTFSIANDVAKYFAIIPALFAAAYPQLGALNIMGLASPQSAILSAVIFNALIIP
ALIPLALRGVKYRPMSAAALLRRNLLIYGLGGLIVPFIGIKLIDLLLSALGLA
>gnl|CDD|441819 COG2217, ZntA, Cation-transporting P-type ATPase [Inorganic ion transport and metabolism]
ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYEAEPAD
ADAAAEEAREKELRDLLRRLAVAGVLALPVMLLSMPEYLGGGLPGWLSLLLATPVVFYAGWPFFRGAWRA
LRHRRLNMDVLVALGTLAAFLYSLYATLFGAGHVYFEAAAMIIFLLLLGRYLEARAKGRARAAIRALLSL
QPKTARVLRDGEEVEVPVEELRVGDRVLVRPGERIPVDGVVLEGESSVDESMLTGESLPVEKTPGDEVFA
GTINLDGSLRVRVTKVGSDTTLARIIRLVEEAQSSKAPIQRLADRIARYFVPAVLAIAALTFLVWLLFGG
DFSTALYRAVAVLVIACPCALGLATPTAIMVGTGRAARRGILIKGGEALERLAKVDTVVFDKTGTLTEGK
PEVTDVVPLDGLDEDELLALAAALEQGSEHPLARAIVAAAKERGLELPEVEDFEAIPGKGVEATVDGKRV
LVGSPRLLEEEGIDLPEALEERAEELEAEGKTVVYVAVDGRLLGLIALADTLRPEAAEAIAALKALGIRV
VMLTGDNERTAEAVARELGIDEVRAEVLPEDKAAAVRELQAQGKKVAMVGDGINDAPALAAADVGIAMGS
GTDVAIEAADIVLMRDDLRGVPDAIRLSRATMRIIRQNLFWAFGYNVIGIPLAAGGLLSPWIAAAAMALS
SVSVVLNALRLRRFKPK
>gnl|CDD|441820 COG2218, FwdC, Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]
MSTLTLTLKAEPELRLEASGITPDALAGKSAAEIAALPVWEGNRKVPLGDLFDVEGDDGDTKIVIEGDLS
RVKRIGAGMTAGEIIVEGDVGMYLGAGMKGGKITVNGNAGSFAGAEMKGGEIEINGNAGDFLGAAYRGDW
RGMSGGTIIVKGNAGDRLGDRMRRGTIIIEGDAGDFAGSRMIAGTIIVKGNAGRRPGYGMKRGTIVVAGK
PEELLPTFVDCGTHELVFLRLLAKAPFAELDGRRFRRYAGDLAVKGKGELLVKA
>gnl|CDD|441821 COG2219, PRI2, Eukaryotic-type DNA primase, large subunit [Replication, recombination and repair]
MNRLLARYPFLAEAREYVEEAGVSLEELLSSDAYKPAVERARERVERALEDGEIGKPDSDERSTEEELLS
YPIARILVSLLDDRILIRRYALAEAKRAEERLQDDLNEDDEDLIDILEEFGLNAAVREDDDGFRIHVSDY
LRLAARLHDPEWRLVNRELSDGEVYLSKEELVRLLREAVRERIADGLPLDVPDEICEALEDEVDEIKELL
AERKSTLREIGTVEPELFPPCMKALLDRLRKGENLPHSARFALASFLLNIGMDVDEIVELFKVAPDFDEE
KTRYQVEHIAGDGSGTEYSPPSCETMKSYGLCVNPDDLCEGISHPLSYYRRKLRDADKDSDWRERK
>gnl|CDD|441822 COG2220, UlaG, L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism]
PGGMKITWLGHATFLIETGGKRILIDPVFSGRASPVNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRAL
KRTGATVVAPLGVAAWLRAWGFPRVTELDWGESVELGGLTVTAVPARHSSGRPDRNGGLWVGFVIETDGK
TIYHAGDTGYFPEMKEIGERFPIDVALLPIGAYPFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDEDPL
ERFAAALAAAGVRV
>gnl|CDD|441823 COG2221, DsrA, Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism]
PYGIIGTWPPKIDEEKCIGCGLCVAVCPTGAISLDDGKLVIDEEKCIGCGACIRVCPTGAIKGEKPKKF
>gnl|CDD|441824 COG2222, AgaS, Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis]
AREIAQQPEAWRRALAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPS
ELVVYPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKS
VAATKSFTTMLLALLALLAAWGGDDALLAALDALPAALEAALAADWPAAALAALADAERVVFLGRGPLYG
LAREAALKLKELSAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIG
AEDDAAITLPAIPDLHDALDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV
>gnl|CDD|441825 COG2223, NarK, Nitrate/nitrite transporter NarK [Inorganic ion transport and metabolism]
SGRWRVLLLATLAFFLAFGVWYLWSVLAPPLAEEFGLSAAQLGLLFAIPVLVGALLRIPLGFLVDRFGPR
RVLLIGLLLLGIGLLLLALAVSYWLLLLLGLLLGIGGGGSFAVGIALVSKWFPPDRRGLALGLAAGGGNL
GAAVAAFLAPLLIAAFGWRNAFLILGILLLVVAVLAWLFLRDPPAGAAAAAKASLRDQLEALRDPRFWLL
SLLYFGTFGSFIGFSSWLPPYLVDQFGLSAATAGLLAALFALLGALGRPLGGWLSDRIGGRRVLLIVFAL
MALGLLLLALALGSLWLFLVLFLLLGLALGGGNGAVFALVPDIFPTKNAGAVYGLVGAAGGLGGFLGPLL
FGALLDATGSYTAAFLVFAVLALVALVLTLLLYRRPRRAAAA
>gnl|CDD|441826 COG2224, AceA, Isocitrate lyase [Energy production and conversion]. Isocitrate lyase is part of the Pathway/BioSystem: TCA cycle, glyoxylate bypass
MMTRQQTAAELEKDWATNPRWKGIKRPYTAEDVVRLRGSVQIEHTLARRGAERLWELLHTEDYVNALGAL
TGNQAVQQVKAGLKAIYLSGWQVAADANLAGQMYPDQSLYPANSVPAVVRRINNALLRADQIQHAEGKDD
IDWFAPIVADAEAGFGGPLNAFELMKAMIEAGAAGVHFEDQLASEKKCGHLGGKVLVPTQEAIRKLNAAR
LAADVMGVPTLIIARTDAEAATLLTSDIDERDRPFLTGERTAEGFYRVKNGIEQAIARGLAYAPYADLIW
CETSTPDLEEARRFAEAIHAKFPGKLLAYNCSPSFNWKKNLDDATIAKFQRELGAMGYKFQFITLAGFHA
LNYSMFELARGYAERGMAAYVELQEAEFAAEKRGYTATKHQREVGTGYFDEVATAISGGQSSTTALKGST
EEEQF
>gnl|CDD|441827 COG2225, AceB, Malate synthase [Energy production and conversion]. Malate synthase is part of the Pathway/BioSystem: TCA cycle, glyoxylate bypass
TQTTPSGVEITGPLGPRYEEILTPEALAFLAELHRRFAPRRQELLAARAERQARIDAGELPDFLPETASI
REGDWKVAPIPPDLQDRRVEITGPVDRKMVINALNSGAKVFMADFEDANSPTWDNVIEGQINLRDAVRGT
ISFTSPEGKEYRLNDKPATLIVRPRGWHLPEKHVLVDGEPISGSLFDFGLYFFHNAKALLARGSGPYFYL
PKLESHLEARLWNDVFVFAQDELGIPRGTIKATVLIETIPAAFEMDEILYELRDHSAGLNCGRWDYIFSY
IKTFRNHPDFVLPDRAQVTMTVPFMRAYSELLVKTCHRRGAHAIGGMAAFIPIKNDPEANEAALAKVRAD
KEREANDGHDGTWVAHPGLVPVAMEVFDAVLGDRPNQLDRLREDVSVTAADLLDVPEGTITEAGLRNNIS
VGIQYLEAWLRGNGAVPIYNLMEDAATAEISRSQVWQWIHHGATLDDGRKVTAELVRQLLAEELAKLRAE
VGEERFEAGRFDEAAELFEELVLSDEFPDFLTLPAYERLD
>gnl|CDD|441828 COG2226, UbiE, Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]. Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis
FDRVAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLN
VEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA
GFE
>gnl|CDD|441829 COG2227, UbiG, 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]. 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
MSDPDARDFWDRRLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELN
VDFVQGDLEDLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN
>gnl|CDD|441830 COG2229, Srp102, Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport]
MAFINVAAREITVKIVYAGPFGAGKTTFVRSISEIEPLSTEGRLTDASLETKTTTTVAFDFGRLTLGDGL
RLHLFGTPGQVRFDFMWDILLRGADGVVFLADSRRLEDSFNAESLDFFEERLEKLPFVVAVNKRDLPDAL
SLEELREALDLGPDVPVVEADARDGESVKETLIALLELVLARLDARAGL
>gnl|CDD|441831 COG2230, Cfa, Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism]
HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLA
RRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYF
AKVARLLKPGGRLLLHTP
>gnl|CDD|441832 COG2231, HP0602, 3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair]
MNTKEDLLEIYERLLEHYGPQHWWPAETPFEVIVGAILTQNTSWKNVEKAIANLKEAGLLDPEALAALDP
EELAELIRPSGFYNQKAKRLKNLARWLVERYGGGLEKLKALPTEELREELLSLKGIGPETADSILLYAFN
RPVFVVDAYTRRIFSRLGLIEEDASYDELQRLFEENLPPDVALYNEFHALIVEHGKEYCKKKPKCEECPL
RDLCPYGGQE
>gnl|CDD|441833 COG2232, PylC, Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism]
MSSPPDLLIAGFSARALAQSARRAGYRVYAVDLFADLDTRALAERWVRLDAESCGFDLEDLPAALLELAA
ADDPDGLVYGSGFENFPELLERLARRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPETRFEPPPDPGP
WLVKPIGGAGGWHIRPADSEAPPAPGRYFQRYVEGTPASVLFLADGSDARVLGFNRQLIGPAGERPFRYG
GNIGPLALPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFD
AHLRACRGELPEVPRPKPRRVAAKAILYAPRDLTIPDDLSWPPWVADIPAPGTRIEKGEPVCTVLAEGPT
AEAARALLERRAEEVRRLLE
>gnl|CDD|441834 COG2233, UraA, Xanthine/uracil permease [Nucleotide transport and metabolism]. Xanthine/uracil permease is part of the Pathway/BioSystem: Pyrimidine degradation
MSSTASSGLVYGVDERPPLGQTLLLGLQHVLAMFGATVLVPLIVGGALGLSAAQTALLISAALFVSGIGT
LLQLLGTGGRLPIVLGSSFAFIAPIIAIGAAYGLAAALGGIIVAGLVYILLGLLIKRIRRLFPPVVTGTV
VMLIGLSLAPVAINMAAGGPGAPDFGSPQNLLLALVTLAVILLLSVFGKGFLRRISILIGIVVGYIVALL
LGMVDFSPVAEAPWFALPTPFPFGLPTFDLGAILTMLPVALVTIAETIGDILAVGEITGRDITDPRLGRG
LLGDGLATMLAGLFGGFPNTTYSENIGVIALTGVYSRYVVAVAAVILILLGLFPKLGALIATIPSPVLGG
ATIVLFGMIAASGIRILVNVDFSNPRNLLIVAVSLGLGLGVTGVPGALATLPATLGPLFLSGIALGALVA
ILLNLLLPGKKEEEEEPAE
>gnl|CDD|441835 COG2234, Iap, Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism]
ALAAAGGGGGTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDEVVVLGAHYD
SVGSIGPGADDNASGVAALLELARALAALGPKPKRTIRFVAFGAEEQGLLGSRYYAENLKAPLEKIVAVL
NLDMIGRGGPRNYLYVDGDGGSPELADLLEAAAKAYLPGLGVDPPEETGGYGRSDHAPFAKAGIPALFLF
TGAEDYHPDYHTPSDTLDKIDLDALAKVAQLLAALVYELANADERWP
>gnl|CDD|441836 COG2235, ArcA, Arginine deiminase [Amino acid transport and metabolism]
MMPLGVHSEIGKLRKVLLHRPGLELERLTPDNLDELLFDDIPWLERAQKEHDAFAKVLRDRGVEVLYLED
LLAETLADPEAREWFLDRFLDESGVGSGLAEALREYLDSLSPEELAEKLIGGITKDELPFDKPKSLVDLV
LGPDDFLLDPLPNLYFTRDPSAWIGGGVTLNSMYWPARRRETLLMEAIYKHHPRFAGADVPVWYGDRRDG
PATIEGGDVLVLSNGVVAIGISERTSPQAIERLARNLFADGAAERVLAVQIPKSRAFMHLDTVFTMVDRD
KFTVYPGIVGTLRVFSLTPGDDGGLDIREEEESLLDVLAKALGLDKLRLIPTGGGDPIAAEREQWNDGNN
TLAIAPGVVVAYDRNTVTNELLRKAGIEVIEIPGSELGRGRGGPRCMSMPLVRDDL
>gnl|CDD|441837 COG2236, Hpt1, Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]. Hypoxanthine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage
MDKFKKEYLSWDEIHELSRRLAEQILESGFRPDVIVAIARGGLVPARILADALGVPDLASIRVSSYTGTA
KRLEEPVVKGPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPSSKFKPDYYAEE
TDAWIVFPWELDE
>gnl|CDD|441838 COG2237, COG2237, Uncharacterized membrane protein [Function unknown]
MRTLVLCVDRDDDIGRKAGVETPVVGREAVIEAAVKLALADPEDSDVNALFGALKVYDELKAKGEDVEVA
VVSGDEDVGVKADRKIAEQLDEVLAKYDPDSAIVVSDGAEDESVLPIIQSRVPIDSVKRVVVRQARNLES
TYYLIKQALADPEYRKTFLVPLGLLLLIYPLLLLAGYPGVALGVIVALLGLYLLYRGFGLDELVDGALER
LRESLYSGRVSFVTYVVAALLILVGIVLGYLSLSSLYTTSGLGLLVLALAFVYGAVPWLAAAALTASLGR
LLDEYLRGRFIRWRYLNLPFFVVAIGLVVYGFSGYFLEIAGVISLSSLQRLALFLIGGIVVALIGVLLFA
YVRSRAGEEEEEKPS
>gnl|CDD|441839 COG2238, RPS19A, Ribosomal protein S19E (S16A) [Translation, ribosomal structure and biogenesis]. Ribosomal protein S19E (S16A) is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MVTVYDVPADLLIERLAEYLKEVDEIEPPEWAEFVKTGVHKERPPEQEDWWYVRAASLLRKVYLDGPVGV
ERLRTEYGGKKRRGVAPEHFRKGSGSIIRKILQQLEKAGLVEKTKGKGRVVTPEGRSLLDKLAYEVLKEL
VEDRPELEKYA
>gnl|CDD|441840 COG2239, MgtE, Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism]
ETEELLEELRELLEEGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVQE
ELLEELSDEELAELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFV
AVREDWTVGEALRYLRRQAEDPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADD
DQEEVARLFERYDLLALPVVDEEGRLVGIITVDDVVDVIEEEATEDILKLAGVSEDEDLFASVLKLARKR
LPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAGMGGNAGSQSLTVVVRGLALGEITLSDWWRV
LLKELLVGLLNGLILGLVVGLVAYLWFGNPLLGLVVGLALVINVLVAALAGSLLPLLLKRLGIDPAVASG
PFITTITDVVGFFIYLGLATLFL
>gnl|CDD|441841 COG2240, PdxK, Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]. Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELG
VLLEFDAVLSGYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLAD
IITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPL
LPFSPNGTGDLFAALLLAHLLRGKSLEEALERAAAFVYEVLERTAAAGSDELLLEAALDELV
>gnl|CDD|441842 COG2241, CobL, Precorrin-6B methylase 1 [Coenzyme transport and metabolism]. Precorrin-6B methylase 1 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MPWLTVVGIGPGGPDGLTPAAREAIAEADVVVGGKRHLELFPDLGAERIVWPSPLSELLEELLALLRGRR
VVVLASGDPLFYGIGATLARHLPAEEVRVIPGISSLQLAAARLGWPWQDAAVVSLHGRPLERLLPALAPG
RRVLVLTDDGNTPAAIARLLLERGFGDSRLTVLENLGGPDERITRGTAEELADADFSDLNVVAIECR
>gnl|CDD|441843 COG2242, CobL, Precorrin-6B methylase 2 [Coenzyme transport and metabolism]. Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
ALVLVGGGGGGGGGLGAAAAAAAAAAAALVGGGRLLLLLLALLAAAALAWPPPLAALLLLLLARRGVVVV
VLASGDPGFGGGGGTLLRLLLAEEVRVIPAPSSFSLAAARLGWALAEVVVVSLLGRALLLLLLALLPGAR
LLLLLLDGAAPAAAAALLLLRGGGGSLLLVLEGLGGGEERRRTGAAAAAAAADAAALNVVALLVVAGPGA
RLPRTPGLPDEAFERDKGPITKREVRALTLAKLALRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERD
PERAALIRANARRFGVPNVEVVEGEAPEALADLPDPDAVFIGGSGGNLPEILEACWARLRPGGRLVANAV
TLETLALALEALAELGYGGELVQVQVSRLKPLGGGTGFRPANPVTIISAEKPE
>gnl|CDD|441844 COG2243, CobF, Precorrin-2 methylase [Coenzyme transport and metabolism]. Precorrin-2 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MMGKLYGVGVGPGDPELLTLKAVRALREADVIAYPAKGAGKASLAREIVAPYLPPARIVELVFPMTTDYE
ALVAAWDEAAARIAEELEAGRDVAFLTEGDPSLYSTFMYLLERLRERGFEVEVIPGITSFSAAAAALGIP
LAEGDEPLTVLPGTLLEEELERALDDFDTVVIMKVGRNFPKVREALEEAGLLDRAWYVERAGMPDERIVP
GLAEVDIEEAPYFSLILVR
>gnl|CDD|441845 COG2244, RfbX, Membrane protein involved in the export of O-antigen and teichoic acid [Cell wall/membrane/envelope biogenesis]
LKKLLKNTLWLLLGQLLGALLGFLLLPLLARLLGPEEYGLFALALSIVALLSVLADLGLSTALVRFIAEY
REEELRRLLSTALLLRLLLSLLLALLLLLLAPFIAALLGEPELALLLLLLALALLLSALSAVLLALLRGL
ERFKLLALINILSSLLSLLLALLLALLGLGLWGLVLKYSLPLLLSGLLGLLLTNLDRLLLGALLGPAAVG
IYSAAYRLASLLLLLITALSQVLFPRLSRLLAEGDREELRRLYRKALRLLLLLGLPLALGLALLAPPLLS
LLFGPEYAEAAPVLPILALGALFLALSGVLSNLLLALGRTRLLLIISLIGAVLNLVLNLLLIPRYGLVGA
AIATLLSYLVLLLLLL
>gnl|CDD|441846 COG2245, COG2245, Uncharacterized membrane protein, contains DUF996 domain [Function unknown]
MMDLSTAKILGGIGAILALLGFLPGIGGILSIVGLVLILVALNEISKAVNDERIFSNYLYSFILGIIGIV
VIVLLLIGLAFFSLFSGFPYALLHEFLSIIGTILLGFIILYILFIISAYFLKKSYELLAKYTGVGLFRTA
GLLYFIGAILTIILIGFIILLIAWILEIVAFFSLPDKIESE
>gnl|CDD|441847 COG2246, GtrA, Putative flippase GtrA (transmembrane translocase of bactoprenol-linked glucose) [Lipid transport and metabolism]
RALRRLLRQLLRFGLVGGLGTLVDLGVFYLLVELLGLPPLLANVIAFVVAVIVNFLLNRRWTFRSRGGRS
RLREFLRFLLVSLVGLALNLGLLALLVYVLGLPYLLAKLIGIVVGTVFNFLLSRRWVFRKKRE
>gnl|CDD|441848 COG2247, LytB, Putative cell wall-binding domain (amidase enhancer), LytB superfamily [Cell wall/membrane/envelope biogenesis]
AAAAASVLDGGGVTSAAVGSVADAGVTDSTATTSATSVAGGAAAAADPGVAAVVVAVGADTAAAVAAAAV
AAATAAAAAVSAAGVAVDAAAAAAAAAAAAAAASAAAVAAAAGAADAGLLTLLGTDSAAAAGVTVVAAVA
LTAVVVAVGLGTASATVAAAAAGGVGRAAGGRAAAAAAAAAAAAAGGAAGAVAIAKAGDSADTVVLARGD
NFADALAAGPLAAALNAPILLTPSDSLPPATLAELKRLGPKKVYILGGTAAVSEAVEDQLKALGITVERI
AGADRYETAAAIAKELGPDADTVVLASGEDFPDALSAAAAAAAAAAAAAAAAAAVAAAAAAAAAAAAVAA
AAGAALVAASAAAAAAAAAAGVAAAVAAGGAAGAAADAGAAAAAAAAAAAAAAAAAAAAAAAAAAAVAAA
GAAAAAAAAGGGAAAALLAAAGAGALAAAAAGAAVATGGSAVATAGDVVAVG
>gnl|CDD|441849 COG2248, COG2248, Predicted hydrolase, metallo-beta-lactamase superfamily [General function prediction only]
MKIIPLAFDSLGVRSMATFVETKDVRILIDPGVSLAPRRYGLPPHPRELERLEELREEIQEYAKKADIII
ITHYHYDHHDPGEEIPKEIYRGKVLLIKDPEENINRSQRRRAPRFLKAIKGIAKEIEYADGKEFRFGDTT
IEFSPPVPHGADGSRLGYVVMVLIEDGDKSLLFTSDVQGPPNDEALEFILEKKPDVLIIDGPPTYLLGYR
VSEESLEKSIKNLEELIREGLKTLIIDHHLLRDLNYRERLKEVYEAAKDLGVKVLTAAEFLGVEPELLEA
RRRELYKRENKEAEIPEGLA
>gnl|CDD|441850 COG2249, MdaB, Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction only]
KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADFYRDGPLPIDVAAEQELLL
WADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGG
PIEELLFRGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA
>gnl|CDD|441851 COG2250, HEPN, HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms]
LRRAERDLEAAELLLEEGRYDLACFHAQQAAEKALKALLLALGGEPPKTHDLRELLELLEKLLPEPEELR
DLLRLLDKAYIPARYPDALPEGPEEYTREEAEEALELAEEVLEFVEKLLKE
>gnl|CDD|441852 COG2251, COG2251, Predicted nuclease, RecB family [General function prediction only]
MFLLDDRMLLSASDLLAYLRCPRRLLLDLDRALLPPPDPPDPMLLRLARLGDAHEARVLARLRAEGRGVV
EIERPEYPADDLEAAAAATLEAMRQGVDVIYQAVLFDGTLLGRADFLVRVPGPSDFGDWSYEVVDTKLAR
RAKPEALLQLAAYADLLAAIGGPVPETAHLVLGDGGRYSVRLADLLPVMRERRARLLALLAAHQEPEVFW
GRPRCSLCGWCDHCAAEAEAEDDLSLVAGVTPSQRAKLQAAGITTIDALAAADPPQRVPGLGKQTAARLR
AQARLQVEQRAGEPAYEVLDPEGLAALPAPSPGDLFFDFEGDPLLPEYWGLEYLFGVLVVDRRGTEKFRP
FWAHDRAEERRAFEQFLDLVAERRAAYPDAHIYHYAPYEVTALKRLAARYGTREAEVDALLRGGRLVDLY
PVVRKSVRLPVESYSIKALEPLYGFEWRDGDVADGGDSVVWYAQWLETGDRGAEAAELLEAILDYNEDDC
RSTRRLRDWLLEFRAEAG
>gnl|CDD|441853 COG2252, NCS2, Xanthine/guanine/uracil/vitamin C permease GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family [Nucleotide transport and metabolism]
MRSMLERFFKLSERGTTVRTEILAGLTTFLTMAYIIFVNPSILSAAGMDFGAVFTATALAAAIGTLLMGL
YANYPFALAPGMGLNAFFAYTVVLGMGVSWQTALGAVFISGIIFLLLTLTGLREAIINAIPESLKLAISA
GIGLFIAFIGLKNAGIVVANPATLVTLGDLTSPPVLLALIGLLLTAVLMARKVKGAILIGILATTILGII
LGVTPLPSGIVSLPPSLAPTFGQLDFSGALSLGLLPVVFTFLFVDFFDTMGTLIGVASRAGLLDEDGNLP
RLGRALLADAIATVAGALLGTSTVTTYVESAAGVAAGGRTGLTAVVTGLLFLLALFFSPLASAVPAAATA
PALIIVGVLMMSSVRKIDWDDFTEAIPAFLTIIMMPLTYSIANGIAAGFISYVLLKLATGKAKEVHPLMW
VLAALFVLYFIFLAI
>gnl|CDD|441854 COG2253, COG2253, Predicted nucleotidyltransferase component of viral defense system [Defense mechanisms]
MMIFRELLRNLARELGLDRDYIEKDYLLERILPALSKSPLADKLVFKGGTALRKFYGDLPRFSEDLDFTL
LGDFLSLEEIKKLLEEIEEALEGEGLEVEIKEPKEEGDYDRIRIRYPGALGGARQRIKIEINTRERVVLP
PEERPLPPLYEDLDDPPFEIRVYSLEELLAEKLRALLDRSRPRDLYDLWYLLRQEGDLDFDLLREALEKY
CKSRDFEELLAEKLELRKQWKNDLKPFLPALDFDEVVEELLELLKK
>gnl|CDD|441855 COG2254, Cas3, CRISPR/Cas system-associated endonuclease Cas3-HD [Defense mechanisms]. CRISPR/Cas system-associated endonuclease Cas3-HD is part of the Pathway/BioSystem: CRISPR-Cas system
MTCCAFKGEETLEEHIRGVLNFLEKLKRSYIPVLSRRLGIDEEEVRDAVKIAVILHDIGKAAEAYQKKFS
NRKRSFFGHEFLSAYFAYKALRKLIKSKNLKFIAALAVMLHHEAMIGGAIRSLGNLKLNALPDLLDELDL
VLEDFSSLADLLEELGGEGSGVIDKVEDYTFDDVIRELRELSVRLLAPPESRKLRRLVYLLLLPLVVADN
LAASLNREGKETKF
>gnl|CDD|441856 COG2255, RuvB, Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair]
MAEEDRLSSSASEEEDALERSLRPKRLDEYIGQEKVKENLKIFIEAAKKRGEALDHVLLYGPPGLGKTTL
AHIIANEMGVNIRITSGPAIEKPGDLAAILTNLEEGDVLFIDEIHRLSRVVEEILYPAMEDFRLDIVIGK
GPAARSIRLDLPPFTLVGATTRAGLLTSPLRDRFGIVLRLEFYTVEELAEIVKRSARILGVEIDEEGALE
IARRSRGTPRIANRLLRRVRDFAQVKGDGVITLEIADAALELLEVDELGLDEMDRRILETIIEKFGGGPV
GLETLAAALGEERDTIEDVYEPYLIQQGFLQRTPRGRVATPKAYEHLGLKPPEDAGT
>gnl|CDD|441857 COG2256, RarA, Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair]
MDDAAAEASAANAPLAERMRPRTLDEVVGQEHLLGPGKPLRRAIEAGRLSSMILWGPPGTGKTTLARLIA
NATDAEFVALSAVTSGVKDIREVIEEARERRAYGRRTILFVDEIHRFNKAQQDALLPHVEDGTITLIGAT
TENPSFEVNSALLSRCRVFVLKPLSEEDLEQLLERALADDERGLGGYKLELDDEALEALARLADGDARRA
LNALELAVLSAPPDGVIEITLELVEEALQRRALRYDKDGDEHYDLISAFIKSIRGSDPDAALYWLARMLE
AGEDPRFIARRLVIMASEDIGLADPQALQIAVAAAQAVERLGMPEGRIALAQAVIYLATAPKSNAAYLAI
NAALADVREGGSLPVPLHLRNAPTKLMKELGYGKGYKYPHDYPGGYVGQQYLPDELKGRRYYEPTERGFE
RKIKERLEKLRKLRRGARE
>gnl|CDD|441858 COG2257, YlqH, Type III secretion system substrate exporter, FlhB-like [Intracellular trafficking, secretion, and vesicular transport]
MSKEKKKRKKAVALKYDGEKDNAPKVVAKGKGELAEKIIELAKEHGVPVHEDPELVELLSQLDLGDEIPP
ELYQAVAEILAFIYRLDGKAPEGKP
>gnl|CDD|441859 COG2258, YiiM, N-hydroxylaminopurine reductase YiiM, contains MOSC domain [Nucleotide transport and metabolism, Defense mechanisms]
MGKVLAVNIGKESGIPKRPVEGAVLVAGLGLEGDAQADRKHHGGPDRAVTLYAAEHYDAWAAELGRDLPP
GAFGENLTTEGLDLSDLPIGDRLRIGEALLEVTQPRKPCHKLEARLGGPGLAKAMCQMGRGGIYARVLEG
GEVRAGDEVELLERPEPGVTVA
>gnl|CDD|441860 COG2259, DoxX, Uncharacterized membrane protein YphA, DoxX/SURF4 family [Function unknown]
SLLSTLADLGLLLLRLLLGLLFLAHGLQKLFGFDGTAGFFASLGLPLPALLAYLAGLAELVGGLLLILGL
FTRLAALLLAGFMLVAIFVVHLPNGFWAMGGGEKNLLLAGGLLALALLGPGRYSLDALLGRRLR
>gnl|CDD|441861 COG2260, Nop10, rRNA maturation protein Nop10, contains Zn-ribbon domain [Translation, ribosomal structure and biogenesis]. rRNA maturation protein Nop10, contains Zn-ribbon domain is part of the Pathway/BioSystem: 16S rRNA modification
MKSLIRKCPSCGRYTLKDTCPVCGGPTVVPHPPRFSPEDKYGKYRRKLKKR
>gnl|CDD|441862 COG2261, YeaQ, Uncharacterized membrane protein YeaQ/YmgE, transglycosylase-associated protein family [General function prediction only]
MGIIGWIIIGLIAGWLARAIMPGGQGGGLIGTIVLGIVGAFVGGWLGGLLGIGLVGGFSLGSLIVAVIGA
IILLFIYRLIRGRRR
>gnl|CDD|441863 COG2262, HflX, 50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]
MFEREERGERAILVGVDLPGSDEDAEESLEELAELAETAGAEVVGTVTQRRDKPDPATYIGKGKVEELAE
LVEELEADLVIFDDELSPSQQRNLEKALGVKVIDRTGLILDIFAQRARTREGKLQVELAQLQYLLPRLVG
MWTHLSRQGGGIGTRGPGETQLETDRRLIRDRIARLKRELEKVRKQRELQRKRRKRSGIPTVALVGYTNA
GKSTLFNRLTGADVLAEDKLFATLDPTTRRLELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREAD
LLLHVVDASDPDFEEQIETVNEVLEELGADDKPIILVFNKIDLLDDEELERLRAGYPDAVFISAKTGEGI
DELLEAIEERLPEDRVEVELLLPYSDGDLVAWLHEHGEVLSEEYDEDGTLLTVRLPPEDLARLEAYLVE
>gnl|CDD|441864 COG2263, COG2263, Predicted RNA methylase [General function prediction only]
KRELEIILEKLPGFSNPKVELEQYPTPAELAAELLHLAYLRGDIEGKTVLDLGCGTGMLAIGAALLGAKK
VVGVDIDPEALEIARENAERLGVRVDFIRADVTRIPLGGSVDTVVMNPPFGAQRRHADRPFLEKALEIAA
VIYSIHNAGSLDFVERFAADRGGEITHVFRAEFPIPRTFEFHRKRRRRIEVEVYRIERK
>gnl|CDD|441865 COG2264, PrmA, Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]
MKWIELTITTPEEAAEALSDALEELGAEGVEIEDAPPGLWERVGVKAYFPEDEDLEELLAALAEALGELG
APEITVEEVEEEDWVEEWKKYFKPIRVGDRLVIVPSWEEYEPDPGEIVIEIDPGMAFGTGTHPTTRLCLE
ALEKLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLED
GPYDLVVANILANPLIELAPDLAALLKPGGYLILSGILEEQADEVLAAYEAAGFELVERRERGEWVALVL
RKKA
>gnl|CDD|441866 COG2265, TrmA, tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]. tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification
EILELTIEDLAHGGDGVARHDGKVVFVPGALPGERVRVRVTKVKKSFARAKLVEVLEPSPDRVEPPCPHF
GRCGGCQLQHLSYEAQLELKQRVVREALERIGGLPEVEVEPIIGSPEPWGYRNRARLSVRRTDGRLRLGF
YARGSHELVDIDECPLLDPALNALLPALRELLAELGARRGELRHLVVRAGRDYLTERLGGLTFRISPGSF
FQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGL
KNVEFVAGDLEEVLPELLWGGRPDVVVLDPPRAGAGPEVLEALAALGPRRIVYVSCNPATLARDLALLVE
GGYRLEKVQPVDMFPHTHHVESVALLE
>gnl|CDD|441867 COG2266, COG2266, GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]. GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MAGGKGTRLGGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKTREYLKERGVEVIETPGEGY
VEDLNEALESISGPVLVVPADLPLLTPEIIDDIIDAYLESGKPSLTVVVPAALKRELGVSPDTTFEIDGE
LVPTGINIVDGSDGEQEETNLVLDDPRLALNVNTPEDLKLAEKLL
>gnl|CDD|441868 COG2267, PldB, Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]
MTRRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSD
GPRGHVDSFDDYVDDLRAALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLL
GPSARWLRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGARHELLNEPAREE
VLAAILAWLER
>gnl|CDD|441869 COG2268, YqiK, Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]
METLGILIIIGVIVVVLLLLLIILARFYRKVPPNEALVITGRGGGYKVVTGGGAFVLPVLHRAERMSLST
MTIEVERTEGLITKDGIRVDVDAVFYVKVNSDPEDIANAAERFLGRDPEEIEELAEEKLEGALRAVAAQM
TVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDARIAEAEAER
ETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQ
RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAW
NKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSAVAEALAPLLESLLEETGLDLPG
LLKGLTGAGAAAPAGEPAE
>gnl|CDD|441870 COG2269, EpmA, Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis]
ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIGPDGGGRPLYLHTSPEFAM
KRLLAAGSGPIYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAGFAPAERLS
YQEAFLRYLGIDPLTADLDELAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQA
ALARISPDDPRVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAG
LPDCSGVALGFDRLLMLALGAERIDDVLA
>gnl|CDD|441871 COG2270, BtlA, MFS-type transporter involved in bile tolerance, Atg22 family [General function prediction only]
MSAAPKASRREILAWALYDWANSAFSTVITTFVFPPYFTSVAALGDPAAATALWGYALAIAGLLVALLAP
VLGAIADRSGRKKPFLAFFTLLGVLATAALFFVAPGGLWLGLLLFVLANIGFEGSLVFYNAFLPDIATPE
EIGRVSGLGWALGYLGGVLLLLINLALFLKPEAFGLPDAGEAVRISFLLTALWWLLFALPLFLFLPERPR
PGPAPPRGAVRAGFRELRRTLRELRRYRDLLRFLLAYFFYRDGVQTVIAFAGIYAAGVLGFSTTELIVFG
LLVQIVAALGALLFGRLDDRIGPKRVILVSLVIWIVVCLAAYFLTTALAFWILGLLIGLVMGGIQALSRS
LLARLIPPGREAEFFGLYALSGKAASFLGPLLFGLVTQLTGSQRLGILSLIVFFVIGLVLLLRVKVPRGR
AAAG
>gnl|CDD|441872 COG2271, UhpC, Sugar phosphate permease [Carbohydrate transport and metabolism]
ARAPSRYRWRILALLFLAYFLNYLDRSNLSVAAPPLQADLGLSAAQLGLLASAFFLGYALGQIPAGLLAD
RFGRRRVLAIGLLLWGLATLLFGFATSFWQLLLLRFLLGLGEAGFFPAALKLIAEWFPPKERGRALGIFN
AGGPLGGALAPPLLGWLLAAFGWRAAFLILGLPGLLLALLRFWLLALAYFLVYFALYGFLTWLPTYLVEV
RGLSLAQAGLLLSLPFLAGIVGSLLGGWLSDRLGRRRKLVLAIGLLLAALALLLLALLPSPALAIALLFL
AGFGLGGAFGLLWALAAELFPKKARGTASGLVNTFGFLGGALGPLLVGYLLDATGYQAAFLLLAALALLA
ALLALLLLRETRK
>gnl|CDD|441873 COG2272, PnbA, Carboxylesterase type B [Lipid transport and metabolism]
MKRLLAAAAAAAPVVRTEAGRVRGVVEGGVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPAC
PQPPRPGDPGGPAPGSEDCLYLNVWTPALAAGAKLPVMVWIHGGGFVSGSGSEPLYDGAALARRGVVVVT
INYRLGALGFLALPALSGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLA
SPLAKGLFHRAIAQSGAGLSVLTLAEAEAVGAAFAAALGVAPATLAALRALPAEELLAAQAALAAEGPGG
LPFGPVVDGDVLPEDPLEAFAAGRAADVPLLIGTNRDEGRLFAALLGDLGPLTAADYRAALRRRFGDDAD
EVLAAYPAASPAEALAALATDRVFRCPARRLAEAHAAAGAPVYLYRFDWRSPPLRGFGLGAFHGAELPFV
FGNLDAPALTGLTPADRALSDQMQAYWVNFARTGDPNGPGLPEWPAYDPEDRAVMVFDAEPRVVNDPDAE
ERLDLWDGVV
>gnl|CDD|441874 COG2273, BglS, Beta-glucanase, GH16 family [Carbohydrate transport and metabolism]
MKLLLLLALLLAALAAAGAASSAPAAAGWTLVFSDEFDGTSLDTSKWTYDTGGPGWGNGELQYYTDENVS
VENGNLVITARKEPYGGGGRPYTSGRITTKGKFSFTYGRFEARAKLPKGQGLWPAFWMLGGDIDGGWPAS
GEIDIMEFVGKDPNKVHGNVHYGGYNGGEGIGASYDLPFDASDDFHTYAVEWTPDSIRWYVDGVLVHTVT
PADVGGPWPFDQPFYLILNLAVGGNWPGAPDTTGFPATMEVDYVRVYQL
>gnl|CDD|441875 COG2274, SunT, ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms]
RRKVPFVLQMEAADCGLACLAMIARYYGRPVSLEELREALGVSRDGLSLLGLLRAARRLGLRARGVRLDL
EELAELPLPAILHWDGNHFVVLEGVDGDKVTIADPATGRRKLSLEEFAESWTGVALLLEPTPEFDKRGEK
PFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEG
LLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVESIREFLTGSLLTALLDL
LFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKAL
GAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNIL
SGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPV
LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFL
FSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNP
RILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARK
GLYAELVQQQL
>gnl|CDD|441876 COG2301, CitE, Citrate lyase beta subunit [Carbohydrate transport and metabolism]
LPMRLRRSLLFVPGDRPRRLAKALASGADAVILDLEDAVAPDEKDAARENVAEALAELDFGGPEVFVRIN
ALDTPWGLDDLAALVGAGLDGIVLPKVESAEDVRALAALLTELEAEGGSIPLMALIETARGLLNAAEIAA
ASPRVEALVFGAEDLAADLGARRTRDGDELLYARSRIVLAARAAGLAAIDGVYTDFRDLEGLRAEARRAR
ALGFDGKTAIHPSQIAVINEAFAPSEEEVAWARRILAAFEEAEAKGVVSLDGKMVDRPHLRRARRILARA
RAIGVRPE
>gnl|CDD|441877 COG2302, YlmH, RNA-binding protein YlmH, contains S4-like domain [General function prediction only]
MDREKILQHFRKEEREFIDRVLDWAEQVEKTYEPKLTDFLDPREQKIAESLLGRLTDLKVRFFGGYEGAE
RKRLLIAPDYYEPEEEDFPIALLEIKYNFKFVTLSHRDVLGALLGLGIKREKIGDILVGEDGAQVIVAKE
IADFLLLNLTKIGRVPVKVEEIDLEELIIPEEKWKEITTTVSSLRLDAVASAGFGLSRSKAAELIESGKV
KVNWKVVDKPSFEVKEGDLISVRGFGRLKVLEIGGKTKKGRIRITLKRYK
>gnl|CDD|441878 COG2303, BetA, Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]. Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
MLEEYDYVIVGAGSAGCVLANRLSEDAGLRVLLLEAGGRDDDPLIRMPAGYAKLLGNPRYDWRYETEPQP
GLNGRRLYWPRGKVLGGSSSINGMIYVRGQPEDFDLWAQLGNQGWGYDDVLPYFKRAEDNERGADAYHGR
SGPLPVSDPPLPNPLSDAFIEAAEELGIPRADDFNGGACEGCGFCQVTCRNGARWSAARAYLPPALKRPN
LTVRTGALVTRILFDGGRATGVEYRDDGEEHTVRAAREVILAAGAINSPQLLLLSGIGPASHLREHGIPV
VHDLPGVGRNLQDHLEVSVVFRFKEPVTLNKSLRKARIGLQYLLTRSGPLTSNVAEAGGFFRSDPGLERP
DLQFHFLPLGLTPRWGKKALHDGHGFTAHVEQLRPESRGRVTLDSADPLGAPLIRPNYLSDENDRRVLVA
GVRLAREIAAQPALAPYRGEEILPGPDVQSDEELAFIRARAYTIYHPVGTCRMGTDPDSVVDPRLRVHGV
ENLRVVDASVMPTITSGNTNAPTIMLAEKAADMILGDYLKN
>gnl|CDD|441879 COG2304, YfbK, Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only]
AEAGFAAADTVPLSTSSADVDAASSSNRRRLLVGGEPPPAAAVRLEELVNFFPYDYPLPTGRLAQSPWNP
QTRLLLVGLQPPKAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV
LLPPTPATDRAKILAAIDRLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANVGITDPEELL
KLAEEAREEGITLTTLGVGSDYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDF
PLPYGTLKL
>gnl|CDD|441880 COG2306, COG2306, Predicted RNA-binding protein, associated with RNAse of E/G family, DUF402 domain [General function prediction only]
PKGIVRLVDIYRVEPLGLGPRFHYLESWLLPDLGYRWLQFHPRDGHYSVTVMFDEHGRDQDFYLDIVRIT
GVDGGVWRTTDLYLDLVVLPGGEAELLDEDELEEALAAGLISKEQADLALRTAHRLLEGIAAHGF
>gnl|CDD|441881 COG2307, Alpha-E, Uncharacterized conserved protein, Alpha-E superfamily [Function unknown]
DMLSRVAENLFWMGRYLERAENTARLLRVNLRLLLDPPAEGAEEEWRSLLAALGDPEGFAARYDEADPEN
VLRFLLFDPDNPGSIASCLRAARENARSVRDRLSTEMWEALNELYLELRELLARGLSRADLLEFLDWVKE
RLAAFRGLADETMLRDEGWRFLRLGRRLERADNTARLLDVKLHVLEVGSALDYYQWEALLRSVSALETYR
RRYRGRISPEPVLDLLLLDPDFPRSLAFCLDRLERHLAALPGSYGGGLLSEAERLLGRLLARLRYADIEE
LLDDGLHEFLDDLQDRLNELSDAISRTYFSHAAA
>gnl|CDD|441882 COG2308, COG2308, Circularly permuted ATP-grasp protein [General function prediction only]
LLAGYRPPPGFYDEMFDADGAPRPHWRPLLEALEALGPEELARRQAAADRLLRENGVTFNVYGDPGGTER
PWPLDLIPRIISAAEWAQLEAGLKQRARALNAFLADIYGEQRLLKDGVLPAELVLGSPGFLRPCVGIKPP
GGVYLHIYGVDLVRDPDGRWWVLEDNTRAPSGVGYALENRRVMSRVFPELFRDLRVRRLADYFRALRDTL
RALAPRGVDDPRVVLLTPGPYNSAYFEHAYLARYLGVELVEGRDLTVRDGRVYMRTTGGLKRVDVIYRRV
DDDFLDPLEFRPDSALGVPGLLEAYRAGNVALANAPGSGVADDKALYAFVPAIIRYYLGEEPILPNVPTW
WCGDPDERAYVLDNLDELVVKPADGSGGYGMLIGPALSAAEREALRARIRANPRNYVAQPTVSLSTAPTL
VDGGLEPRHVDLRPFALAGGDGYRVMPGGLTRVALREGSLVVNSSQGGGSKDTWVLSDEPVAPTSLLPPS
LAPRRRRSSLLSSRAANNLWWGGRYEEREETLRRLLRALLLRLEEGDDPPAPLAALLLLALLLALLLPGP
PAPGALAEALAAALLLALLILDRFSLDGASALALLLAAARRRLLLRRRLDDLSRRLLLRLRDLALASGLA
LENLAAELLLLLLLLGLLLARLAGGAMLLRRRRRRRARLRRLRRLLELGDSLLLLRLLLALLSAEEELLL
ELLLLLLLLRSTLRRRRRLRLLLLLLLLLLLLLLLSLLLLLLLLLLLLLLLLLLLLLALDLLAALLAELA
ALLALLLDLLLA
>gnl|CDD|441883 COG2309, AmpS, Leucyl aminopeptidase (aminopeptidase T) [Amino acid transport and metabolism]
RLEKYAELLVKYGLNLQPGEKVLIVADIEAAPLARALAEAAYEAGAKPVVVWSDPELTRARLEHASEEQL
EFIPPWEAAAMEEADAVIAITSPSNPDLLSDVDPEKIAAHTKARKPALKPVRERIRVGKTRWCVTAYPTP
AWAQKAFMSLEALEDFIFKACRLDWEEHAELLEKLADLLNEADEVRITGPGTDLTVSLAGRKWIGGAGIT
EPGFFANLPTGEVFTAPVEDSVNGTVVFDKPLSYQGNLIEGIRLTFEDGKVVEATAEKGEEVLKKLLDTD
EGARRLGELALGTNSPISRLFGNTLFDEKIGGTVHLALGDAYPECLGGGNDSAIHWDFVIGSGEIYIDGE
LIFRDGEFVI
>gnl|CDD|441884 COG2310, TerZ, Stress response protein SCP2 [Signal transduction mechanisms]
MAISLQKGQNISLTKEAPGLTKVRVGLGWDPAKTDGGDFDLDASAFLLDANGKVRSDEDFVFYNNLKSPD
GSVRHTGDNRTGEGDGDDEQITVDLSKVPADVEKIVFVVTIYDAEARGQNFGQVSNAFIRVVDAATGEEL
ARYDLSEDFSGETAMVFGELYRHGGEWKFRAVGQGYNGGLAGLATDY
>gnl|CDD|441885 COG2311, YeiB, Uncharacterized membrane protein YeiB [Function unknown]
MTTSAAPVAPSERILALDALRGFALLGILLVNIPLFALPFAAYLNPAAPGPPSGLDRVVWALLFLLVDGK
FYPLFALLFGAGLALQLRRAERRGRDFRRLYLRRLLWLLLFGLLHAVLLWPGDILLAYALLGLLLLLLRR
LSPRTLLIWAAVLLLLGLLLLLLLGYALTAGPAEAAAAGLAAAIAAYASGSYLEALAFRLTELGLLLFLL
LGRGPPVLGLFLLGMALGRRGLLEGPERHRRLLRRLAVIGLAVGLPLALLGLLLPSLLLLLLLLLRYLGG
LLLALGYAALILLLAQRLRPGRLLRALAAVGRMALTNYLLQSVIGTLLFYGYGLGLFGRLGRAALLLLAL
AIWAVQLLFSHLWLRRFRRGPLEWLWRRLTYGRRQPLRR
>gnl|CDD|441886 COG2312, YbfO, Erythromycin esterase homolog [Secondary metabolites biosynthesis, transport and catabolism]
MTAPPASASLVAWLREAAIPLQTTDLDDLDPLLDRIGDARVVGLGEATHGTHEFYRLRARITRRLVEEKG
FRAVAVEADWPDALRVNRYVRGGGDGDPREALKAFSTWMWRNEEVLALVEWLRAYNADLPHGDKVGFYGL
DLYSLWESIDAVLAYLDRVDPEAAAEARERYACLDPYGRDPQSYGRAAPSGERESCEEEVVELLEELQER
RAEYAARDGAEEYFDAEQNARVVANAEEYYRAMYRGGPESWNLRDRHMAETLERLLEHLGPGAKAVVWAH
NSHIGDARATDMGARGEVNIGQLLRERFGDDYVLIGFGTYRGTVIAADDWGGPMEVKTVPPARPGSYEAL
LHQVGPPRFLLDLRAAPEAEVREWLREPRLERAIGVIYRPETERASHYFPASLPEQFDALIHIDETTALT
PLPAEA
>gnl|CDD|441887 COG2313, PsuG, Pseudouridine-5'-phosphate glycosidase (pseudoU degradation) [Nucleotide transport and metabolism]
NKYLRISPEVAAALAAGRPVVALESTIISHGMPYPQNLETAREVEAIVREAGAVPATIAVLDGKIKVGLS
DEELERLAQAKDVAKVSRRDLPVALARGRSGATTVAATMILAALAGIRVFATGGIGGVHRGAEETFDISA
DLQELARTPVAVVCAGAKSILDLPLTLEYLETLGVPVIGYGTDEFPAFYSRSSGLPVPYRVDSPEEIAAI
LRAKWALGLPGGVLVANPIPEEDALDAEEIDAAIAEALAEAEAQGIRGKAVTPFLLARIAELTGGRSLEA
NIALVKNNARLAAEIAVALAALA
>gnl|CDD|441888 COG2314, TM2, Uncharacterized membrane protein YozV, TM2 domain, contains pTyr [General function prediction only]
AELPKSEKSKLVAGLLAIFLGGFGIHRFYLGKTGTGIIYLLFFWTGIPGIIGLIDGILYLTMSDEEFNRR
YNVGKKGWF
>gnl|CDD|441889 COG2315, MmcQ, Predicted DNA-binding protein with #double-wing# structural motif, MmcQ/YjbR family [Transcription]
MTIEELRAYCLSLPGATEDFPFGPDALVFKVGGKMFALLGLDGGRPRVNLKCDPELAEELREQYPGITPG
YHMNKKHWNTVYLDGSLPDDELRELIDHSYDLVVAKLPKKKRAEL
>gnl|CDD|441890 COG2316, COG2316, Predicted hydrolase, HD superfamily [General function prediction only]
MMTREEALELLKEYTKSENLIKHALAVEAVMRALARRFGEDEEKWGIAGLLHDIDYEKTPDPEEHCLKGA
EILRERGVPEEIIRAILSHNDYTGVERETLMEKALYAADELTGLITAAALVRPSKSLSDVEVKSVKKKFK
DKSFAAGVNREVIKSGAEELGLELDEFIELTLEAMQEIADELGLA
>gnl|CDD|441891 COG2317, YpwA, Zn-dependent carboxypeptidase, M32 family [Posttranslational modification, protein turnover, chaperones]
MMTAYEELLERLRRISALGHAAALLGWDQETMMPEGGAEARAEQLATLSGLAHELLTDPELGELLAALEA
EEDLDDDEAANLREMRRDYERATKLPAELVEELSRATSEAEHAWREARAANDFAAFAPYLEEVVELKREE
AEALGYGGHPYDALLDDYEPGMTVAELDALFAELREELVPLVEKILASQAQPDPSFLEGPFPEEAQRALS
RELLEALGYDFDRGRLDVSVHPFTTGLGPGDVRITTRYDENDFLSALFSTIHETGHALYEQGLPPALYGT
PLGEGRSMGIHESQSRLWENQVGRSRAFWEHLYPLLQEHFPEQLGDVSLEDFYRAINRVEPSLIRVEADE
VTYPLHIILRYELERALIEGDLEVADLPEAWNEKMEEYLGITPPNDAEGCLQDVHWSGGSFGYFPTYTLG
NLYAAQLFAAARKDLPDLDELIARGDFSPLLDWLRENIHQHGSRYTPDELIERATGEPLNPEYFLDYLEE
KYGELY
>gnl|CDD|441892 COG2318, DinB, Bacillithiol/mycothiol S-transferase BstA/DinB, DinB/YfiT family (unrelated to E. coli DinB) [Secondary metabolites biosynthesis, transport and catabolism]
LLRYNEWANRRLLKALEALPEEELDWKPGAGFRSIGELLNHILVVDRIWLARLTGEPPPPAALDAELFPT
LAELLAALEEADARLLEFLASLTDEDLDETVTFFSGDGEGEMTRGEILLHVFNHETHHRGQLTVYLRQLG
IEPPS
>gnl|CDD|441893 COG2319, WD40, WD40 repeat [General function prediction only]
ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGAL
LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSA
DGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV
AFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL
LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSD
DGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT
>gnl|CDD|441894 COG2320, GrpB, GrpB domain, predicted nucleotidyltransferase, UPF0157 family [General function prediction only]
PIELVPYDPEWPEQFEREAARIRAALGDRALRIEHIGSTAVPGLAAKPIIDILVVVADLEDLDALVEALE
ALGYERLGEDGIPGRRFFRKGDGGRTHHLHVREAGSPEWRRHLLFRDYLRAHPEAAAEYAALKRELAARY
PDDRDAYTEAKTPFIEEILARALAWA
>gnl|CDD|441895 COG2321, YpfJ, Predicted metalloprotease [General function prediction only]
MRWNDRRDSSNVEDRRGSGGGGGGLAIGGGIGGLVILLIGLLLGGDPSGLLGGGGGGGQSQQQQQRTGAD
ANDELDCFVSVVLASTEDVWTQIFPAAGKTYRPPKLVLFSGATQTACGTASSAVGPFYCPADQKVYLDLS
FFDELRTRFGAPGDFAQAYVIAHEVGHHVQNLLGILDKVQRARQRASEAGANSLSVRLELQADCYAGVWA
HHAQQTLGPLEPGDIEEALNAASAIGDDRLQKQAQGRVVPESFTHGSSAQRVRWFKRGYESGDPAACDTF
SAASL
>gnl|CDD|441896 COG2322, YozB, Predicted membrane metallochaperone YozB (3H, Sco1 fusion), DUF420 family [General function prediction only]
MRSRARKRYNALIAVLSIVIPALVAGLFGGPPPDLPGADLSFLPHINAVLNGLTAVLLLAGWRAIKRGNI
EAHRRAMLTAFVLSALFLVSYLLYHALGGSTSFGGPGAIRYVYLFILITHILLAIVVVPLVLYTLYLALT
GRFTRHRKIARWTFPIWLYVSVTGVVVYLMLYPYYPS
>gnl|CDD|441897 COG2323, YcaP, Uncharacterized membrane protein YcaP, DUF421 family [Function unknown]
APMLPLLEIVLRTVIIYLALLLLLRLMGKRQLSQLTPFDFVVTIALGSIAGNAILGPDVSLLGGLIALLT
LVLLQYLLSYLSLKSRKFRRLIDGKPTVLIKDGKILEENLRKARLTEDDLLSALREKGIFSLSDVEYAIL
EPNGQLSVIKKSDKQPVTPYPLIIDGEILEDVFLAELDSGK
>gnl|CDD|441898 COG2324, COG2324, Uncharacterized membrane protein [Function unknown]
MKELTALERVRLNRFTIAVVFGLAGLLLLLPGLLPEPLAGNVVYLLLGTLAMLLYAVRGLGDRRALAFLL
LAFLLGLAIELLGVSTGFPFGEYSYGSGLGPKLLGVPLTIPLSWFPLVLNSYLLARLLLGRRARRPWLRL
LLGALLMVAWDLVLDPAAVALGFWVWEGGGPYFGVPLSNYLGWFLVGLVFVLLLDLLLRRKPNKPLLLRR
RSLSFPLDLYLSFFLFFGGINLWAGLWLPAALGLLFGLLLLLLARTD
>gnl|CDD|441899 COG2326, PPK2, Polyphosphate kinase 2, PPK2 family [Energy production and conversion]
VDLTKKLDKEEYEAELAALQAELVKLQEWLYATGRRVLIVFEGRDAAGKGGTIKRVTEGLNPRGVRVVAF
KAPTEEERAHDYLWRYWRHLPAAGEIGIFDRSWYERVLVERVMGFCTDEEWERRYEEINEFERMLVDDGI
ILLKFWLHISKEEQKKRFKERLDDPLKRWKLSPEDLEEREKWDDYTKAYEEMLARTSTPHAPWYVVPADD
KRYARLNVIRTLLEALEYLDLDYPDPDIVA
>gnl|CDD|441900 COG2327, WcaK, Polysaccharide pyruvyl transferase family protein WcaK (colanic acid biosynthesis) [Cell wall/membrane/envelope biogenesis]
MKILLSGYYGFGNLGDEALLEALLQLLRKRLPDAEITVLSGNPEETRKRYGVRAVPRRNFLEILRALRRA
DLVISGGGGLLQDVTSLRSLLYYLGLVLLAKLLGKPVVIYGQGIGPFKSPLSRRLLRRVLNRADLISVRD
EASAELLKDLGVKKPPIELTPDPAFLLPPEPVDKEAPLERPVVGVNLRPWRGLEEDYLEALAAALDRLIE
RTGYKVVLLPHQYGQEDDLAIAEELAAKLKERVVVLDEELDPDELLSLIARADLVIGMRLHALIFALSAG
VPVIALSYDPKVRGLMEDLGLPDYVLDLDDLDPEELLAAVEELLANREELREKLAEKLAELRARARENLE
LLLKLLK
>gnl|CDD|441901 COG2329, HmoA, Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and metabolism]
MIVVINRFRVKPGQEEEFEEAFAERRELLAEQPGFLGFELLRSLEDPGEYLVVSYWESEEAFRAWFRSSE
HRAAHAKGREILAGPPRVEHYEVVAEVE
>gnl|CDD|441902 COG2331, COG2331, Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only]
MPIYEYRCESCGHEFEVLQKMSDDPLTVCPECGGPLRRLISAPGFVFKGSGFYVTDSRSGSKKSSSSSSG
SGSSSCG
>gnl|CDD|441903 COG2332, CcmE, Cytochrome c biogenesis protein CcmE [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
MTPRRKKRLKLVVAGLVALGAAVALVLYALRDNIVYFYTPSEVAAGKAPPGRRIRVGGLVVPGSVQRDPD
GLTVRFVVTDGGATVPVRYTGILPDLFREGQGVVAEGRLDPDGVFEADEVLAKHDENYMPPEVADALKKA
GVWQGGAA
>gnl|CDD|441904 COG2333, ComEC, DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport]
LRVTFLDVGQGDAILIRTPDGKTILIDTGPRPSFDAGERVVLPYLRALGIRRLDLLVLTHPDADHIGGLA
AVLEAFPVGRVLVSGPPDTSETYERLLEALKEKGIPVRPCRAGDTWQLGGVRFEVLWPPEDLLEGSDENN
NSLVLRLTYGGFSFLLTGDAEAEAEAALLARGPDLKADVLKVPHHGSKTSSSPAFLEAVRPRVAVISVGR
DNRYGHPHPEVLERLRAAGIRVYRTDRDGAITVTSDGDGLRVE
>gnl|CDD|441905 COG2334, SrkA, Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]. Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis
DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRRYVLKLYRPGRWSPEEIPFELALLAHLAAAGLP
VPAPVPTRDGETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALADFPRPNARDLAWWDE
LLERLLGPLLPDPEDRALLEELLDRLEARLAPLLGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYG
PRLYDLAIALNGWADGPLDPARLAALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVRAKDPAF
ERYLRRQIALAWAALEA
>gnl|CDD|441906 COG2335, FAS1, Uncaracterized surface protein containing fasciclin (FAS1) repeats [General function prediction only]
MKKLLLLAALALLAACASSAAAEGAAMAPTKNIVETAANNPDFSTLVAALKAAGLVDTLSGEGPFTVFAP
TDAAFAALPAGTLDALLKPENKATLTKILTYHVVPGKVTAADLKDGKTLTTLQGQTLTVTVSGGGVTVNG
ANVITADIEASNGVIHVIDKVLLP
>gnl|CDD|441907 COG2336, MazE, Antitoxin component MazE of the MazEF toxin-antitoxin module [Defense mechanisms]
MTTKIRKWGNSLGVRIPKALLEQLGLKEGDEVELEVEDGRIVIRPVRRPRYTLEELLAGITPENAHEEYD
WGKPVGKEVW
>gnl|CDD|441908 COG2337, MazF, mRNA-degrading endonuclease MazF, toxin component of the MazEF toxin-antitoxin module [Defense mechanisms]
TPKRGDIVLVDLDPTVGSEQGKRRPALVVSNDAFNRYSPTVIVAPITSNIRKGYPFRVLLPPGENGLKKD
SVVLVDQIRTVDKSRLGKKIGRLSEELLEEVLAALKLLLGL
>gnl|CDD|441909 COG2339, PrsW, Membrane proteinase PrsW, cleaves anti-sigma factor RsiW, M82 family [Signal transduction mechanisms]
VAVLLLGLALLLLVVLLLASLGNPAMLILLLLALVPALALLAFFYWLDRYEPEPLRLLLLAFLWGALVAV
PAALLLNTLFGLLLPTEGDLGLFLGAFLVAGLVEEFAKGLAVLLLLYRRREFDEPLDGIVYGAAVGLGFA
FVENILYLFRAFAEGAGGLLQTAILRALLSPFGHALFTAITGYGLGLAKFSPSRGRRVLALLGGLLLAVL
LHGLWNFLLSLGGGVYLLVLVPLVLFLWALLLRKIRREQRL
>gnl|CDD|441910 COG2340, YkwD, Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell cycle control, cell division, chromosome partitioning, General function prediction only]
LLLALLLAAAAAAPAALSALEQEVLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDG
SSPFDRLKAAGYSYRAAGENIAAGYSTAEEAVDGWMNSPGHRANILNPDFTEIGVGVAYGGDGGVYWTQV
FGRP
>gnl|CDD|441911 COG2342, COG2342, Endo alpha-1,4 polygalactosaminidase, GH114 family (was erroneously annotated as Cys-tRNA synthetase) [Carbohydrate transport and metabolism]
VGILLAVLVALSLAAEPTNAALENWSYQLYYGNVDLDEIALSNFDLVVIDPDRDGPDGPYSAEEIQKLKE
NGKKVLAYLSIGEAEDYRPYWDKLVPPDWLGGENPEWPGEYLVDYWSPEWQDLLLEYLDRILDAGFDGVF
LDTVDAYEYWALQDRAELAKAMVDGVADLANYARARNPDFLIIPNNGFALLDYDKYLPYIDGVLVEDVFY
DGDEPVSEDEWEWRLKYLQRLRKRGKPVLTVDYVDDEDRIADAYARARKEGFIPYVADRSLDRIVP
>gnl|CDD|441912 COG2343, COG2343, Uncharacterized conserved protein, DUF427 family [Function unknown]
MESVWDYPRPPRIEPSSRRVRVRWNGVVIAESDRAVRVEETGLPPVYYFPPEDVRMELLEPSDTTTFCPW
KGTASYYSVVVGGEVNEDAAWSYPEPKPEAAAIAGYVAFYPGRVDVCEVDGER
>gnl|CDD|441913 COG2344, Rex, NADH/NAD ratio-sensing transcriptional regulator Rex [Transcription]
MMKKKKIPEATIKRLPLYLRYLEELKEEGVERISSKELAEALGVTAAQVRKDLSYFGEFGKRGVGYNVEE
LIEEIEKILGLDREWNVALVGAGNLGQALANYNGFEKRGFKIVAAFDVDPEKIGTKIGGIPVYHIDELEE
VVKENKIEIAIITVPAEAAQEVADRLVEAGIKGILNFAPVRLKVPEDVVVENVDLSVELQTLSYFLNNKE
EEES
>gnl|CDD|441914 COG2345, COG2345, Predicted transcriptional regulator, ArsR family [Transcription]
MTDTPALAALADPTRRRILELLKRAGPVTAAELAEALGLTPNAVRRHLDALEEEGLVERETERRGRGRPA
KLYRLTEAGRARFPRAYDDLAVALLDALRELLGEDAVERLARARGRRLAARYRPALAGAGSLEERLEALA
ELLSEEGYMAEVEEEDDGFQLCEHNCPFLEVAEEHPVVCELELGLFEGLLGALVAERTATLADGDRRCTY
RIPPRAA
>gnl|CDD|441915 COG2346, YjbI, Truncated hemoglobin YjbI [Inorganic ion transport and metabolism]
SPEPTLYERIGGEEAIRALVDRFYDRVRADPLLGPIFPEADLEEHREKLADFLSQVLGGPGLYSGRRMRA
RHAPLPITEEHFDRWLELMREALDELGVPPELAEELLARLERIADDMVNR
>gnl|CDD|441916 COG2348, FmhB, Lipid II:glycine glycyltransferase (Peptidoglycan interpeptide bridge formation enzyme) [Cell wall/membrane/envelope biogenesis]
MTFLTEIDREEWDAFVASHPGGNFLQSPEWAEVKANLGWEPERLGVKDDGELVAAALVLIRKLPLGGSLA
YIPRGPVLDYSDAELLGAFLEELKAYAKKKRAIFLRIDPDVPEREWDDELIELLAALGFRHQGFRKGFED
IQPRFTFVLDLTGDEEELLASMSKKTRRNIRKAEKKGVEVREGGREDLDEFYELYKETAERDGFSLRSLD
YFEDLLDALGDAGRARLYLAEHEGEPLAAALVVYSGDEAYYLYGGSSDEYRKLMANYLLQWEAIRWAKER
GCTRYDFGGISGDLDPDHPLYGLYRFKKGFGGEVVEYIGEFDLPLNPLLYKLYRLALKLRRKLR
>gnl|CDD|441917 COG2350, YciI, YciI superfamily enzyme, includes 5-CHQ dehydrochlorinase, contains active-site pHis [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]
MLFAVILTDKPDSLEERDALRPAHLAYLKELYEEGRLLAAGPLLDDDTGGLIIAEADSREEAEALAAADP
YVKAGVVASVEVREWKPVLGALA
>gnl|CDD|441918 COG2351, HiuH, 5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide transport and metabolism]
MGRLSTHVLDTARGRPAAGVRVELYRLDGDGWTLLAEGVTNADGRIDALGGEALAAGTYRLVFDTGDYFA
ARGVPPFLPEVPVRFGIADPEEHYHVPLLLSPWGYSTYRGS
>gnl|CDD|441919 COG2352, Ppc, Phosphoenolpyruvate carboxylase [Energy production and conversion]. Phosphoenolpyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
MTSLLSAEAPDKDAPLREDIRLLGRLLGEVLREQEGEELFDLVERLRQLAIALRRGDPEAREELAALLAG
LSPDEAVRVIRAFSIYFQLANIAEDNHRIRRRRARERAGSAPQPGSLAAALARLKEAGVSAEQLQELLDR
LLIEPVFTAHPTEAKRRTVLEKLRRIALLLEELDRPRLTPREREELEERLRREITLLWQTDELRLEKPTV
ADEIRNGLHYFRETLFDVVPELYRELERALAEHYPDLDPPLPPFLRFGSWIGGDRDGNPFVTAEVTRETL
RRQREAALEHYLEELHELGRELSLSARLVGVSPELLALLEADRELLPEVAPDASERRPDEPYRRKLTLIR
ARLAATLDRLTGLLAGRHAVVPAGPYASAEELLADLRLIRDSLRAHGGALLADGRLRPLIRAVETFGFHL
ATLDIRQNSDVHEEAVAELLAAAGVGADYAALDEAERVALLLEELASPRPLISPYAELSEETREELAVFR
VAAEARREYGPEAIGTYIISMTESVSDLLEVLLLAKEAGLVDPAAGGGRCPLDVVPLFETIEDLRAAPEI
MRALLSLPVYRALLAARGNVQEVMLGYSDSNKDGGFLASNWELYKAQRALVEVAREHGVRLRLFHGRGGS
VGRGGGPTYEAILAQPPGTVNGQIRITEQGEVISSKYANPEIARRNLEQLVAAVLEASLLPREEAEPDPP
EWEEAMEELSAASRAAYRALVYETPGFVDYFREATPIDEIAELNIGSRPASRKGSRSIEDLRAIPWVFSW
TQSRFMLPGWYGVGSALEAFLEEDPEGLALLREMYREWPFFRTLLSNVEMVLAKADLAIARRYAELVEDE
ELRERIFGRIEAEYERTVEAVLAITGQDELLDRNPVLARSLRLRNPYLDPLNHLQVELLRRLRAGGDEED
EELLRALLLTINGIAAGLRNTG
>gnl|CDD|441920 COG2353, YceI, Polyisoprenoid-binding periplasmic protein YceI [General function prediction only]
MKKLLLLAALAALAAAAAAGTYTIDPAHSSVGFSVKHLGVSTVTGRFKKFSGTITFDPADPEAGSVEVTI
DVASIDTGNAKRDKHLRSADFFDVAKYPTATFVSTSVEATGDGTYEVTGDLTIKGVTKPVTLPVTLTGAG
DRAGFSATTTIDRSDFGIGYGSPLGGVLVGDEVEIEIDLEAVKQ
>gnl|CDD|441921 COG2354, MutK, Membrane protein MutK/YedI, may be involved in DNA repair [Replication, recombination and repair]
MASGLLALLDDIAALAKLAAASLDDVAAMAKKAAKKTAGVVGDDLAVTPQYVTGVRADRELPVVWAIAKG
SLRNKLILVPAALLLSAFAPWAITPLLMLGGAYLCFEGAEKVAHKFLHHKEEDEEHLAALADAAVDPAAL
EKEKVKGAIRTDFILSAEIMVIALGTVADAPFWTQAAVLAVVAILITVGVYGLVALIVKLDDVGLYLARR
GSAAAARALGRGLVAAMPKLMKALSVVGTAAMFWVGGGILVHGLPELHHLIHHLAEAVAHAVPALGGVLA
WLVPTLLSAVVGLVAGAVVVAVVTLVPKLRGKKAA
>gnl|CDD|441922 COG2355, COG2355, Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism]
HERMPVIDGHCDLLLRLLEPGRDLTERSPDGHVDLPRLREGGVGAQFFAVFVPPEYRPASALARALEQID
ALHRLVAASPDRLRLARTAADLEAALAEGKIAALLGIEGAEALGGDLDNLDVLYRLGVRYIGLTWNGDNR
LADGATDPDTDGGLTDFGREVVREMNRLGMIVDVSHLSDKTFWDVLELSKAPVIASHSNARALCDHPRNL
TDEQLKAIAERGGVIGINFVPAFLSPDGPDATLDDVVDHIDHIVELVGIDHVGLGSDFDGIGEGPEGLED
VSDLPNLTEALLKRGYSEEDIEKILGGNFLRVLREVLAA
>gnl|CDD|441923 COG2356, EndA, Endonuclease I [Replication, recombination and repair]
KETDENNDGNVSCGYQRADRWNREHVVPASWFGHGKSDPMETDLHHLRPADGEVNSDRSNFPFGEVGGAA
SKYGQCGMKVDFKGRVFEPRDEVKGDVARAYFYMATRYELRISVLSRGQLQLLLAWHKQDPVDAWERERN
NRIASIQGNRNPFIDHPELADRIWG
>gnl|CDD|441924 COG2357, YjbM, ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport and metabolism, Signal transduction mechanisms]
MSLLEEEIREFLADYERFLPPYEAALEELKTKLEILLDEFEKHGGSPIEHVTSRVKSPESIIEKLRRKGL
PLTYENILEEITDIAGIRIICYFVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVRVPVFL
SDGPKGVPVEIQIRTIAMDFWAELEHKLRYKYDGEIPEEIKRRLKRAAALLELLDEEMSEIRDEIEEAQK
EFEDKEAIAEESLAALLLLLEDLGVDLDFILAIELSELFLLDLELELAKLLRIAEEIAILRLLDLLESLG
RDRLLD
>gnl|CDD|441925 COG2358, Imp, TRAP-type uncharacterized transport system, periplasmic component [General function prediction only]
ALAGAAAAAAPQFLTIGTGGTGGTYYPIGGAIAKVVNKELPGIRVTVQSTGGSVENLRLLRAGEADLAIV
QSDVAYDAYNGTGPFEGGPLDNLRALASLYPEPVHLVVRADSGIKSLADLKGKRVSVGPPGSGTEVTAER
LLEAAGLTYDDVKVEYLGYGEAADALKDGQIDAAFFVAGLPTGAVTELAATTDIRLLPVDDEAIAKLLEK
YPYYAPATIPAGTYPGQDEDVPTVAVPAVLVTRADLPEDLVYELTKALFENLDELKAAHPAAKELTPETA
LDGLPVPLHPGAARYYKEKGLLK
>gnl|CDD|441926 COG2359, SpoVS, Stage V sporulation protein SpoVS, predicted DNA-binding, AlbA superfamily [Function unknown]
MEVLKVSSKSNPNSVAGAIAGVLREDGEVEIQAIGAGAVNQAVKAIAIARGYLAPEGIDLVCVPAFVDVE
IDGEERTAIRFIVEPRKK
>gnl|CDD|441927 COG2360, Aat, Leu/Phe-tRNA-protein transferase [Posttranslational modification, protein turnover, chaperones]
FPPPEQALSDPDGLLAVGGDLSPERLLAAYRQGIFPWFSEGEPILWWSPDPRAVLPPDEFHISRSLRKTL
RKGRFEVTVDTAFEAVIRACAAPRPGQEGTWITPEMIEAYTELHRLGYAHSVEVWQDGELVGGLYGVALG
RAFFGESMFSRVSDASKVALVHLVAHLRAWGFRLIDCQVLTPHLASLGAREIPRAEFLALLAEALAQPAP
PWQFD
>gnl|CDD|441928 COG2361, HEPN, HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms]
MSMRRDRAYLEDILEAIERIEEYTEGLDFEDFLEDELTQDAVIRNLEIIGEAAKRIPDEFREKHPEIPWR
QIAGMRNRLAHGYFGVDLEIVWDTVQNDLPELKEQIEAILEELEE
>gnl|CDD|441929 COG2362, DppA, D-aminopeptidase [Amino acid transport and metabolism]
MKVYISADMEGIAGVVSWEQVRPGGPEYERARRLMTAEVNAAIEGAFAAGATEVVVNDSHGSMRNLLPEE
LPPRARLIRGKPRPLSMMEGLDESFDAVFFIGYHARAGTPRGVLAHTYSGRAIARVRINGEEAGEFGLNA
ALAGEYGVPVVLVSGDDALCEEARELLPGIVTVAVKEGIGRYAAISLSPEEARELIREAAKEALARARAA
KPLKLPGPVTLEVEFKSPALADLASLLPGVERVDGRTVRFTADDYLEAYRALLALTALASGARF
>gnl|CDD|441930 COG2363, YgdD, Uncharacterized membrane protein YgdD, TMEM256/DUF423 family [Function unknown]
MMMRLFLILGALLGALAVALGAFGAHGLKGRLSPEALATFETAVRYQMYHALALLALGLLAQRLPSRLLR
LAGWLFLLGILLFSGSLYALALTGIKLLGAITPIGGLLFILGWLLLAIAALRLKRR
>gnl|CDD|441931 COG2364, YczE, Uncharacterized membrane protein YczE [Function unknown]
MKKKRLLKRLLVLLLGLFLLGLGIALTIKAGLGTSPWDVLHYGLSLLTGLSIGTVTIIVGLLVLLLWILL
LRKRPGLGTILNMFLIGLFIDLFLWLLPFLTPESLLLRILLLLIGIVLLALGVALYIGAGLGAGPRDGLM
LALSKRTGWSFGVVRTGIEVTVLLIGWLLGGPVGIGTVIAALLIGPLIQFFLPLLGKLLRKLTPRPA
>gnl|CDD|441932 COG2365, Oca4, Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms]
PLEGAVNFRDLGGYPTADGRRVRWGRLYRSGALSRLTDADLARLADLGIRTVIDLRSPAEVARAPDRLPP
GVRYVHLPVLPDDAEALLEELRDGDLTPGDAEEFMLELYRAFVDPDAADAYRAAFRALADAENGPVLFHC
TAGKDRTGVAAALLLLALGVPRETIMADYLLTNEYLAPLRARLLAALRAALGDEDPELLAPLLGVRPEYL
EAALDAIDERYGSVDAYLEEGLGLTDAELEALRARLLE
>gnl|CDD|441933 COG2366, PvdQ, Acyl-homoserine lactone (AHL) acylase PvdQ [Secondary metabolites biosynthesis, transport and catabolism]
RRLLAALLLLLLLAAGGLYWLLRRSLPDYDGELALPGLSAPVEIVRDEWGVPHIYAENDEDAFFALGYVH
AQDRLFQMDLLRRAAAGRLSELFGPAALETDRFFRTLGLRRAAEAELAALDPETRAALEAYAAGVNAYIA
ELRHGALPPEFKLLGYKPEPWTPEDSLAVLKLMAFDLSGNLRDELLRARLLAKLGPDRLADLFPDYPGDA
PIIPPEALDPAALPPALALAALAAALSPLLPPLPPGIGSNNWAVSGSRTASGKPLLANDPHLGLSAPSIW
YEAHLESPGLNVIGATLPGVPGVIIGHNEHIAWGLTNFGPDVQDLYIEELNPDNPNQYRYDGGWEPFETR
TETIKVKGGAPVTLTVRETRHGPVISDDLPDPEGTALALRWTALEPGDRTLLAFLRLNRARNVEEFRAAL
RRFGAPAQNFVYADADGNIGWQAAGRIPIRPPGDGRLPLPGWDGEYEWQGYLPFEELPQVVNPASGYIAT
ANNRPVDADYPYYLGGDWAPGYRAQRIRELLAAREKHTVEDMKALQLDTVSLFARRLLPLLLAALDAAPL
ADPRLAEALDLLAAWDGRMDADSAAAALFAAWLRELLRALFADELGPEAFDAFLLPLSDRALERLLEDPD
SPWWDDIRTPAVETRDDILLAALADALAELEKRLGSDPADWRWGKLHTLTFRHPLGGAVPPLRRLFNVGP
LPVGGGSDTVNATGYDGAGGPFAVTHGPSYRMVVDLGDPDKSRFILPGGQSGHPLSPHYDDQAELWARGE
YRPLLFDRAAVEAAAVSTLTLTPAG
>gnl|CDD|441934 COG2367, PenP, Beta-lactamase class A [Defense mechanisms]
MRLLALLLLAAAAAAPASALEAELAALEAALGGRVGVYVLDLDTGETVGINADERFPAASTFKLPVLAAV
LRQVDAGKLSLDERVTLTPEDLVGGSGILQKLPDGTGLTLRELAELMITVSDNTATNLLLRLLGPDAVNA
FLRSLGLTDTRLDRKEPDLNELPGDGRNTTTPRDMARLLAALYRGELLSPESRARLLDWLARQTGRDRLR
AGLPEGWRVAHKTGTGGGVRNDVGIVWPPDGKPYVLAVFTKGPDADAARAEALIAEIARAVYDYLR
>gnl|CDD|441935 COG2368, YoaI, Aromatic ring hydroxylase [Secondary metabolites biosynthesis, transport and catabolism]
IRTGEEYLESLRDGREVYIDGERVEDVTTHPAFRNAARSVARLYDLQHDPEYRDLMTYTSPETGERVNRF
FLIPRSKEDLVKRREAIREWARLTGGCMGRSPDYLNAFLMTLAADADFFAEGDTDFAENARRYYEYVQEN
DLFLTHAITDPQGDRSKPPSEQEDPDVYLHVVEETDDGIVVRGAKMLATGAALADEILVGPTGPLGPGDK
DYAVAFAVPMNTPGLKLICRESYEDGAASPFDYPLSSRFDENDAIVVFDDVLVPWERVFLYGDVELANRL
YAETGFAVYHRHQYVVRKAVKLDFLIGLAALIAEANGIDKFPHVQEKLGELIAYRETFKALLIAAEAEAE
PDPGGTYLPNRSLLNAARVLAPRAYPRIVEILRELAGGGLITLPSEADFENPEIRPYLDKYLRGSNIDAE
ERVKLFRLAWDLTGSEFGGRHELYERFYAGSPEAMRIAIYRQYDKEPKKALVDRLLGEY
>gnl|CDD|441936 COG2369, COG2369, Uncharacterized protein, contains phage Mu head morphogenesis gpF-like domain [Mobilome: prophages, transposons]
NDLGKARELPPEEAIAYFRQKLNLPTEDWRDVWQAAHARAFTVAKAIRLDLLNDIRAALTQALEEGTTLE
EFRKDLEPILAKKGWGGGSKRRARTIYRTNLRTAYAAGRWARMQELGVKEARPYWRYRAVGDERTRPSHR
ALDGKVLPLDDPFWGTHYPPNGWNCRCTVRALSEDDLERRGLKEDSAPEGIDPGFDYNPGK
>gnl|CDD|441937 COG2370, HupE, Hydrogenase/urease accessory protein HupE [Posttranslational modification, protein turnover, chaperones]
MKKTSRLLLAAALLLLASPALAHHGHGGHGGFLSGLAHPLTGLDHLLAMVAVGLWAALLGGRAGWLLPLA
FVAAMLLGALLGLAGLALPGVETGIAASVLVLGLLLALARRLPLAAAAALVALFALFHGYAHGAEIPGAA
SALAYLAGFVLATALLHLAGIALGLLLRRRAAARLLLRAAGAAIAAAGLALLAGAL
>gnl|CDD|441938 COG2371, UreE, Urease accessory protein UreE [Posttranslational modification, protein turnover, chaperones]
LRATEILGNGAALAAAAVDTVTLDYDERQKRRLRLTTDDGREVGLDLPRGTVLRDGDVLVLEDGRLVVVR
AAPEPVLVVRAADPLDLARLAYHLGNRHVPLQIEEDRLRIPPDHVLEDMLEGLGLT
>gnl|CDD|441939 COG2372, CopC, Copper-binding protein CopC (methionine-rich) [Inorganic ion transport and metabolism]
MRRLARLLAALLLALLLLLLAAAPASAHAVLVSSSPADGATVTAAPTEVTLTFSEPVEPGFSTVTVTDPD
GERVDVGDPTVDGAKTLTVPLPAPLPPGTYTVSWRVVSADGHPVSGSFTFTVGAP
>gnl|CDD|441940 COG2373, YfaS, Uncharacterized conserved protein YfaS, alpha-2-macroglobulin family [General function prediction only]
AALPATLPLTPPLLLAALAALALLALLALLLGAALPLSPPPALALAIAALVLPAAPLLALLLAPLLLALA
AAASALALAATLLALSLLSAAALLLLALLAALALAVRAAALAASSALAAAAAALALAAALLAAALLALLA
ALAAAAALALALALAAAAAAALAALLAAAAAALLALAALAAELAALLALALVLAAALLAPAALSEVALLL
EPDLKGKLNKRVTTALPLSELLALLKPGVYLVVARFPGDYSYNGESRATQWFLVSDLGLTAKRGDDGLLV
FVTSLSTGKPVAGAEVELYDRNGQVLATATTDADGLARFPAGDRGEGGRAPALLVARKGGDFAFLDLDDG
PALDLSDFDVGGRAPPGGLDAFLFTDRGIYRPGETVHLKALLRDADGKAPAGLPLTLELTDPDGKEVRRQ
TLTLNEFGGYSFSFPLPEDAPTGTWRLELYVDPKPALGSKSFRVEEFKPPRFKVDLTLDKEPLKPGDPVT
VTVDARYLFGAPAAGLKVEGEVTLRPARTAFPGYPGYRFGDPDEEFEPEELDLGEGTLDADGKASLSLPL
PDAPDAPGPLRATVEASVFESGGRPVTRSATVPVHPADFYVGIRLPLFDGDPEGAPATFEVVAVDPDGKP
VAGKGLKVELYREEWRYVWYKSDDGGWRYESQEKEEPVAEGTLTTGADGPASLSLTPVEWGRYRLEVKDP
DGGLATSVRFYAGGNASWGAERPDRLELSLDKESYKPGETAKLLIQSPFAGRALVTVERDGVLETQWVDV
KGGGTTVEIPVTEDWAPNAYVSATLVRPGDSTANDMPARAYGVAPLPVDPPARRLKVELTAPEKLRPGET
LTVTVKVKGAAGKAAEVTLAAVDEGILNLTGYKTPDPLDFFYGKRALGVETRDLYGRLIGAFGGAAGALR
SGGDGALGRGGNPKPPRKRFKPVALFSGPVKTDADGKATVSFDLPDFNGTLRVMAVAWSDDRFGSAEATV
TVRKPLVVRPSLPRFLAPGDRFELPVDVFNLTGKAGTVTVTLEASGGLTLEGEATQTVTLAAGGRATVRF
PLKAPDAGDAKVTVTATGGGESDAREVELPVRPANPLVTRATSGVLAPGESWTLPLDLPGGLRPGTGSLT
LSLSSSPPLDLAGLLRYLLRYPYGCTEQTTSRALPLLYLSDLAEALGLKGDKDAELRARIQAAIARLLSM
QNSDGGFGLWPGGSESDPWLTAYATDFLLEAREAGYAVPDDALDRALDYLRNYLRNPWEIEYDDAYRLAV
RAYALYVLARAGKADLGDLRYLYDRRKDALSPLAKAQLAAALALLGDKARAEELLAAALARLRETGARDY
WYGDYGSPLRDQALALALLAELGPDAPLAPKLARWLAKALKSGRWLSTQETAWALLALAAYARAAGASPD
FTATLTLDGKTLPLTGRGPLARVTLPAAELLAGPLTITNTGDGPLYYTLTLSGYPAEGPPPAASNGLEIE
RRYYDLDGKPIDPASLKQGDLVVVRLTVTAPSGRVENVAVVDPLPAGFEIENPRLATSGDLGDWLGDSWQ
PDHQEFRDDRVVAAFDLDPAGTYTFAYLVRAVTPGTFVLPPAQAEDMYRPEVRARSAGGRVTVVA
>gnl|CDD|441941 COG2374, COG2374, Predicted extracellular nuclease [General function prediction only]
IHGQTVTGVVTAVGFYLIFVFTGFYGLLSPTVVTVPVTLGLTGVLFGNYRQPTETFVNPRPEAPVGGDLR
VATFNVENLFDTDDDDDDFGRGADTPEEYERKLAKIAAAIAALDADIVGLQEVENNGSALQDLVAALNLA
GGTYAFVHPPDGPDGDGIRVALLYRPDRVTLVGSATIADLPDSPGNPDRFSRPPLAVTFELANGEPFTVI
VNHFKSKGSDDPGDGQGASEAKRTAQAEALRAFVDSLLAADPDAPVIVLGDFNDYPFEDPLRALLGAGGL
TNLAEKLPAAERYSYVYDGNSGLLDHILVSPALAARVTGADIWHINADIYNDDFKPDFRTYADDPGRASD
HDPVVVGLRLPP
>gnl|CDD|441942 COG2375, ViuB, NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ion transport and metabolism]
MTTTTPARVRRPLRLRELTVVRVERLSPHMRRVTLGGEDLAGFASPGPDDHVKLFFPPPGGGEPVLPTLD
DGLALPGEERPVMRTYTVRRFDPEAGELDIDFVLHGDGGPASRWAARARPGDRVGILGPGGSFVPPPDAD
WYLLAGDETALPAIARILEALPADARGTAVIEVPDAADEQPLPAPAGVEVTWLHRGGAPPGSALLDAVRA
LELPDGDVYAWVAGEASAVRALRRHLRDERGLPRDRVRASGYWRRGRAED
>gnl|CDD|441943 COG2376, DAK1, Dihydroxyacetone kinase [Carbohydrate transport and metabolism]. Dihydroxyacetone kinase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
MKAVADVIAENRKFLNDLDAVVGDGDHGINMARGFDAVRAALDAAPADPGVVLRAAGMKVASVVGGGSGG
LVGTGFLDAAVALKGETSPTADQVAAALRAADEGIQGRGVAYTGDKTNFDAAAPAAEAIEEAVAAGTAAA
AALDEAAAAAEKGAEATRSMGAALGRATYPGERSPGHPDPGATSVALLLNGLGASLDAKLDEDAPV
>gnl|CDD|441944 COG2377, AnmK, 1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis]
KPMLVIGLMSGTSLDGIDAALVEFDGEGKVELLAAETVPYPEELRARLLALCAPASLSLEELAELDRALG
RLFAEAVLALLAKAGLSAEDIDAIGSHGQTVRHRPEGRPGFTLQIGDGALLAELTGIPVVADFRSRDVAA
GGQGAPLVPAFHQALFSDPGEPRAVLNIGGIANITYLPPGGPVIAFDTGPGNALLDAWVQRHGGKPYDKD
GAWAASGKVDEALLARLLADPYFALPPPKSTGRELFNLAWLEQLLAGFGLSPEDVQATLTELTAASIADA
IRRLPPPPDRVLVCGGGAHNPTLMERLQALLPGVPVVTTDELGIDPDAKEALAFAWLAVRTLRGLPGNLP
SVTGAKRPVILGA
>gnl|CDD|441945 COG2378, YobV, Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains [Transcription]
MSRLERLLALLQLLQSRRGVTAAELAERLEVSERTIYRDIDALRELGVPIEAERGRGGGYRLRDGYRLPP
LMLTEEEALALLLALRLLAALGGAPLAEAAASALAKLEAVLPERLRERLEALAERVGVDPPPEVDPEVLE
TLREAIRERRRLRIDYRSGRGEPTERTVEPYGLVFYGGRWYLVAWCELRDDIRTFRLDRIRSLELTDERF
EPPPDFDLAEYLAEGFGVFAGGPEPVTVTLRFSPEAARYLRERHPSQEIEELPDGSVRVTLTVADLDELA
RWLLSFGADVEVLEPEELREAVREEARRLLARYE
>gnl|CDD|441946 COG2379, GckA, Glycerate-2-kinase [Carbohydrate transport and metabolism]. Glycerate-2-kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
SADLRALLLAIFDAAVAAADPDRAVRRALPELLPPKGRVVVVGAGKAAAAMAAALEEILGDRLTEGLVVT
RYGHAVPLERIEVVEAGHPVPDEAGLAAARRILELVSGLGEDDLVLALISGGGSALLELPAEGITLEDKQ
AVNRALLASGADISEMNTVRKHLSAIKGGRLAAAAAPARVVTLIISDVPGDDLDVIASGPTVPDPTTFAD
ALAILERYGIELPASVRAHLERGAPETPKPGDPRFARVENHIIASNRDALEAAAEAARALGYNALILSDA
LEGEAREVAKVLAAIAREVARHGQPFKKPCVLLSGGETTVTVRGNGRGGRNQEFALALALALAGLPGITA
LAADTDGIDGPTDAAGAIVDGDTLARARALGLDPRAYLANNDSYGFFAALGDLIVTGPTGTNVNDLRAIL
I
>gnl|CDD|441947 COG2380, NurA2, NurA-like predicted nuclease, RNAse H fold [General function prediction only]
MRFRVDPWDPGYGAPFEAEEAAPSSAEVDLDVELPADRWRPITPAPPVSPPDVVLFVDGVRRIEARLWID
DPGGTATPGLAASYAAGAVRCDGGPAELAGVRVRRGLFTASPSAGDLPTGGLRYEPHAASGDGPEALRAA
LQRALRALEVELATRLRAAGEDDLLVVDGPLRGRSRLPRAVGYVKTHHRAYLPPELAALVPELAPGERTP
VFLLGTSWDRHSWYLRLPGAPGAPWAGIVRVECSADLGLAEAVALADLSAALLPRFASVPYKDPRAPQNL
VPIAGLERELRRRLGDARLLRRALRAAAARLAA
>gnl|CDD|441948 COG2382, Fes, Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]
GATALLLALAAAGLAALLLLAALAGAAPPGLLVASAVVVVRVLPAAAAAARLLAPVVAAAVVVLGGPPPA
TDDKDVPHGTVETVTYPSKALGRTRRVWVYLPPGYDNPGKKYPVLYLLDGGGGDEQDWFDQGRLPTILDN
LIAAGKIPPMIVVMPDGGDGGDRGTEGPGNDAFERFLAEELIPFVEKNYRVSADPEHRAIAGLSMGGLAA
LYAALRHPDLFGYVGSFSGSFWWPPGDADRGGWAELLAAGAPKKPLRFYLDVGTEDDLLEANRALAAALK
AKGYDVEYREFPGGHDWAVWRAALPDFLPWLFKD
>gnl|CDD|441949 COG2383, COG2383, Uncharacterized membrane protein, Fun14 family [Function unknown]
MDDQLDVDLTQLGLQLGFGAVIGFAVGYALKKVAKIVLVLVGLYLASLFYLESQGIITVNWDALQALLDG
ATQQARGAGGSLLDGLLSNLPFGAGFAAGFLLGFKKG
>gnl|CDD|441950 COG2384, TrmK, tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]. tRNA A22 N1-methylase is part of the Pathway/BioSystem: tRNA modification
KLSKRLQAIASLVPKGARVADIGTDHAYLPIYLVKNGIIKKAIAGDVNEGPLEKAKKNVKKYGLEDKIEV
RLGDGLEVLEPGEVDTIVIAGMGGELIADILEAGKDKLKSVKRLILQPNTGAEELRRWLYENGFRIIDEE
LVEEDGKIYEIIVAEPGEEKLELSELELEFGPLLLEEKNPLLKEYLEREIEKYQRILEQLEKSKTEEAAE
KIEELEKKIKAIEEVLKC
>gnl|CDD|441951 COG2385, SpoIID, Peptidoglycan hydrolase (amidase) enhancer domain SpoIID [Cell wall/membrane/envelope biogenesis]
KVLLSLLLTLALLLALGASLLVLPAAGKVAASSSLGVLILGPVGGLGLKKGDLGLLSLEGSGALILPALS
GKVVLSIDGLISVNGRDYRGSLEVYPNGGGLTLVNEVPLEEYLKGVVAAEMPASWPLEALKAQAVAARTY
ALRNLLRHAHDGYDLCDTTHCQVYKGLEEETPKIRKAVEATRGEVLTYNGEPIDAVFHSTSGGYTENAED
VWGSDLPYLRSVPDPYDKESPKYRWTKTFSLAELAKALGKKLGDVGDIKDIKVLERTPSGRVKKLKIVGD
KGTKTISGEEIRRALGKLRSTLFTVEKKGDGFTFTGKGYGHGVGMSQWGANGMAKQGKSYREILKHYYPG
TELEKLY
>gnl|CDD|441952 COG2386, CcmB, ABC-type transport system involved in cytochrome c biogenesis, permease component [Posttranslational modification, protein turnover, chaperones]
MLRAFLALLRRDLRLELRRRGGLLNPLLFFLLVVVLFPLAFGPDPALLARIAPGILWVAALLAALLSLDR
LFAADYEDGTLEQLLLSPVPLEAIVLGKLLAHWLLTGLPLLLLAPLLALLLGLPAEALGLLLLTLLLGTP
GLSLIGTLGAALTVGLRRGGLLLALLVLPLYIPVLIFGVGATAAALAGLPVSGWLALLGAFDLLALALAP
LAFAAALRI
>gnl|CDD|441953 COG2388, YidJ, Predicted acetyltransferase, GNAT superfamily [General function prediction only]
MEITHNEEKGRFELEVDGELAGELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVP
LCPFVAAYFERHPEYADL
>gnl|CDD|441954 COG2389, COG2389, Uncharacterized metal-binding protein, DUF2227 family [Function unknown]
MPSGRTHDRITLWSLPVVAGLTYYLTRSPELTLLFAGGFLFGGLMFGPDLDIYSRQYQRWGWLRWIWLPY
QKLLRHRSFLSHGPIIGTILRLLYLGLWLLLLGILGLAILQLLGGITWNWQALVQLLGRSLRLYPQELLA
LFLGLELGAMSHSISDWLGSAYKRLRKKKKGRRRKRKS
>gnl|CDD|441955 COG2390, DeoR, DNA-binding transcriptional regulator LsrR, DeoR family [Transcription]
RAAWLYYVEGLTQREIAERLGISRRTVSRLLAEAREEGLVRISITDPLAGLLELERELRERFGLKEVIVV
PGDSDDDEEVLRALGRAAAEYLERLLKDGDVIGVGWGRTLAAVAEALPPLPLPDVTVVPLRGGLGEDVEA
QANEIARRLAEKLGGEYYLLPAPAIVDSAETREALLEEPSIREVLELARRADVALVGIGSADPDSTLARR
GYLSEEELAELRAAGAVGDICGRFFDADGRIVDTPLNDRTIGISLEDLRRIPRVIAVAGGEEKAEAILAA
LRGGYINVLITDEATARALLE
>gnl|CDD|441956 COG2391, YedE, Uncharacterized membrane protein YedE/YeeE, contains two sulfur transport domains [General function prediction only]
MTPFTPWMALLGGLLIGLGLALLLLGNGRIAGISGILSGMLDPAKVLGFLDRAWRFVFGGGLVVGPLLYR
LVAPHLPAITITIDPPRLVIGGLLVGIGTRLGGGCTSGHGVCGLGRLSPRSLVATLAFMAGGFLTVFLVR
HLL
>gnl|CDD|441957 COG2401, MK0520, ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only]
MARYNPFFVLMRVTKVYSSVLDLSERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKS
TLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAVELLNAVGLSDAVLWLRRFKELSTG
QKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIF
VGYGGVPEEKRR
>gnl|CDD|441958 COG2402, COG2402, Predicted nucleic acid-binding protein, contains PIN domain [General function prediction only]
MIFVDTGALIALFNRRDQYHEAAVELLESLLEGELPLVTTDYVLTETLTLLSRRLGREAAVKFLDRLRES
GGLEIVPLTEEDFERALELFEKYADKPLSLTDASSVALMERLGIDEILTFDRDFDQYGFTLLPTD
>gnl|CDD|441959 COG2403, YjiA, Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion transport and metabolism]
MRRRVIIMGAAGRDFHNFNVFFRDNPEYEVVAFTATQIPGIEGRRYPPELAGELYPDGIPIYPEEELEEL
IRELRVDEVVFAYSDVSHEEVMHKASRVLAAGADFRLLGPKETMLKSSKPVIAVCAVRTGCGKSQTSRKV
ARILKERGLKVVVVRHPMPYGDLEKQAVQRFATYEDLDKHECTIEEREEYEPHIDRGNVVYAGVDYEAIL
REAEKEADVILWDGGNNDFPFYKPDLHIVVADPHRPGHELSYYPGEVNLRMADVVVINKVDTADPEDIET
VRENIRKVNPKAEIIEAASPVTVDDPELIRGKRVLVVEDGPTLTHGGMPYGAGYVAARKYGAAEIVDPRP
YAVGSIKETYEKYPHIGPVLPAMGYGPEQLKDLEETINRVDCDVVVIGTPIDLSRLIKINKPVVRVRYEL
QEIGGPTLEDILDEFLEKLGL
>gnl|CDD|441960 COG2404, DhhP, Oligoribonuclease NrnA/c-di-AMP phosphodiesterase DhhP, DHH superfamily [Translation, ribosomal structure and biogenesis, Signal transduction mechanisms]
MDPKILIITHTDLDGVGCAALARRAFGDPVKLYFASPGKLDEILERILEYLKKGELVFITDLSPNKETLE
EIEELLEELKEKGAKVVWIDHHKWAEELANALREAGVWLVVDTSTCAAGLVYEYLHPEGDEFLEELVEVV
RDRDLWLWEDPESKDLNRLLFWLGDEEYKERLLEKLANGPLLDDEVEEALLEYRNEELERIEKALKRVVI
REINGYKVGVVYAPRGSQSELGNLLLERNGADFAVIVNPKGKVSLRSRGFVDVSEIAKKLGGGGHPNAAG
AKLDIELLELILSAILRAIEEKKAARK
>gnl|CDD|441961 COG2405, COG2405, Predicted nucleic acid-binding protein, contains PIN domain [General function prediction only]
MMIVVSDTSPLIYLAKIGRLDLLPELFGEIIIPEAVYEEIEAGGAPEPGAEELERPGWLEVVEVEDESLV
ELLRKGLDAGEAEAIALALELGADLLLIDDRAARKVAKKLGLKVTGTLGILLRAKERGLISSEEAKPLLD
RLIEAGFRLSPELYEEVLRLLGEL
>gnl|CDD|441962 COG2406, DPS, Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, recombination and repair]
MGKVGREILVGVDVDELIELLNKAYADEWLAYYYYWIGAKNVKGLMGEGIKEELEDHAEEELNHAELLAE
RIYELGGTPPLDPEEWAELSGCGYDLPEDPTDVRAILEQNLKAERCAIKVYNELCNMTKGKDPVTYDLAL
DILEEEVEHEQDLEDLLGDLESGHF
>gnl|CDD|441963 COG2407, FucI, L-fucose isomerase or related protein [Carbohydrate transport and metabolism]
PKIGIIPVSREFFPMELAKEARKLIVEALREDGEVEVVIADGTVETVAEAAKCAEKFKKEGVDGVIVVLP
NFGYEDETADAARLLDVPVLIWAFPDEEGKMAGRRDGACGLLAALANLRQRGIPAFLIYGHQDPDDESVA
EKLLRFARAARAVAGLRGLRIGSIGGRPMGFYTSRVNEDKLLERLGIRVEEIDLSELLRRAEKYDDDEVE
KALEWIKENADVYGNLPDEQLEKVAKLYLALRDLMEENGLDAIAIQCWPELQDNYGPNPCFAESLLNDSG
IPVACEVDILGALSMLILKLASGTPVLFADVRNYWPDDDDIIHLFHCGNTALSFAGESTITELIAHEILE
ATVYFEGGGGSLEGRTKPGPVTFARLNTDDGGPRLYIAEGEFVDLPLETFGTYGVVRIPGAFRLVYSVLE
NGFAHHGAIVYGHIGADLIEAAKYLGIPVYMHNVPEEKIFRP
>gnl|CDD|441964 COG2409, YdfJ, Predicted lipid transporter YdfJ, MMPL/SSD domain, RND superfamily [General function prediction only]
VARHRWLVLLAWLVLLVALGVLAPQLGGSLSSNGFFLPGSESQRAADLLAEAFPESDGASAVVVVEAPDG
TLTDPAFRAAVAALVARLRADPGVAGVQDPWDDPAAGLVSEDGKAALVTVTLDGDAGDEAAEAVDALRDA
VAAAPAPGLTVYVTGPAALAADLNEAFEEDLGRAELITLPVALVVLLLVFRSLVAALLPLLTAGLAVGVA
LGLLALLAAFTDVSSFAPNLLTMLGLGVGIDYALFLVSRYREELRAGEDREEAVARAVATAGRAVLFSGL
TVAIALLGLLLAGLPFLRSMGPAAAIGVAVAVLAALTLLPALLALLGRRVFWPRRPRRRRAAAPESGFWR
RLARAVVRRPVPVLVAAVAVLLALALPALGLRLGLPDADSLPADSPSRQGYDALAEHFPPGSNGPLTVVV
ESDDDLDPADLAALDALAAALAAVPGVASVQPPTRPEGTDGDAARLQVVPDGDPDSPEAIDLVDRLRDAA
APALEGAEVLVGGTTAVNIDISDALADDLPLVIPVVLGLIFLLLLLLFRSVVAPLKAVLTNLLSLGAALG
VLVLVFQHGWLLLGFTPGPLDSFVPLLLFVILFGLGMDYEVFLVSRIREEYDRGGGTREAVIRGLARTGR
VITSAALIMAAVFAAFATSPLVFLKQIGFGLAVGVLLDAFVVRMLLVPALMALLGRWNWWLPRWLDR
>gnl|CDD|441965 COG2410, COG2410, Predicted nuclease (RNAse H fold) [General function prediction only]
KTFAGIDLAGKPKRPSGVAVISGNPTIAVLTLYSDEEIIELCLLKKPVVVAIDAPLSLPEGGGFREVDRE
LRRLGIRVLPPSLRGMRKLTERGIRLASILESQGVEVIETHPTSALKSLGLSRKDYSRRELLSRLGIDLP
SLSSKDELDAVIAALTAYAYAKGKAIAIGASDGEIVLPKEGIKKPL
>gnl|CDD|441966 COG2411, ASCH, Predicted RNA-binding protein, contains PUA-like ASCH domain [General function prediction only]
MKHLNFKPKYLDAILSGRKTATIRLGDKRYKPGDEVYVTSGGRKIAKARITSVRVKKLSELTDEDARLDG
FSSVEELIEALRKIYGDISPDDEVTVIEFEVVE
>gnl|CDD|441967 COG2412, COG2412, Uncharacterized conserved protein, DUF424 domain [Function unknown]
MKMYLKIHRTEGGVLVAVCDEELLGKTFREGGLSLTVSEEFYGGELVDEEEALKALKEATIANLVGERAV
ELAIEEGLVDEDSVLEIGGVPHAQVFRM
>gnl|CDD|441968 COG2413, COG2413, Predicted nucleotidyltransferase [General function prediction only]
MVREKVERTGERREVVYDEEHWELLREKRRRAIEILEALESFGLESIVHGSVARGDVHPGSDIDVFIPEP
VPSYKVELALESAGFKIYEKEIVQATPRSTPKAYIVLDPEEEVVVSFPLAKLRPRELEFYRFGGKLDLDG
LRRGKRVPGVNKRLVLIEPTEEGHIESPVIGRESEVARILGVSIETVLERVRVLTRRDEVGRTGVFLKYE
LPPDEPFEEALRELARRNPLFRRRLSEKGL
>gnl|CDD|441969 COG2414, YdhV, Aldehyde:ferredoxin oxidoreductase [Energy production and conversion]
MYGYAGKILRVDLSTGTIKVEPLPEEWARKYLGGRGLGAKLLYDEVPPGVDPLSPENKLIFATGPLTGTP
APGSGRYTVVTKSPLTGTIGDSNSGGYFGAELKFAGYDAIVIEGKAEKPVYLYIEDGKVEIRDASHLWGK
DTYETEEALKEELGDNASVAAIGPAGENLVRYACIMNDGGRAAGRGGVGAVMGSKNLKAIVVRGTKKVEV
ADPEEFKELVKEALKEIKENPVTQGLRKYGTAVLVNIANELGALPTRNFQEGYFEGAEKISGEALAEKYL
VKRRGCYGCPIACGRVVKVKEGPYKGLAGEGPEYETIAALGSNCGIDDLEAVAKANELCNELGLDTISAG
NTIAFAMELYEKGLITKEDTGGLELRFGDAEAALELIEKIAYREGFGDLLAEGVKRAAEKLGKGEELAMH
VKGLELPAYDPRGAKGMGLGYATSNRGACHLRAYPIAPEVLGIPEKVDPLSTEGKAELVKWFQDLTAVFD
SLGLCKFTTFALGPEDYAELLNAATGWDVTPEELLKIGERIYNLERLFNLREGFTRKDDTLPKRLLEEPL
PEGPAKLDVEELEEMLDEYYELRGWDEEGVPTRETLKELGLDEVAEDLEK
>gnl|CDD|441970 COG2419, TRM10, tRNA (A,G)9-N-methylase TRM10 [Translation, ribosomal structure and biogenesis]. tRNA (A,G)9-N-methylase TRM10 is part of the Pathway/BioSystem: tRNA modification
KKPGEALLELLKEKGIERLGLLRHLKKGRFRRDIFQEIAVRLLVGKYGVCEEEEYGAVVWEFNGREVKLL
AGGGEEPSDAAYVRPEPEVTPEELSEKLPPYPLFIVDLSLWDKHTPKEKKKLRLQLAATLGTVRRYLWDR
HLALTNAPEEFREWLNKFFPLFRVTIYELPTDEILKELGADRVVLLDPNAEEDLTEEDVLNADAFIIGGI
VDKGRPRPGATRKLAELIGLVKRRRIELRGSVIGVPDRINKIVEILLRARYEGGSLEEAIISVMSPRDAR
WRLRKEIPKRARRGKKYLVVPKELYEELKEWLPLTWRDFVKALRRAGFEVLERPR
>gnl|CDD|441971 COG2421, FmdA, Acetamidase/formamidase [Energy production and conversion]
AMHTLPATETVHHGRFDPDLPPVLTVKPGDTVTIETLDCFGGQIKSEDDADDVRDLDFSGVHPLTGPIYV
EGAEPGDVLAVRILDIEPRRDWGVNATIPGFGFLPDEFPEERVKIWEIDGERGTARFLPGVRIPLRPFIG
TIGVAPAEEGAVSSVPPGEHGGNMDIKDLTAGSTLYLPVFVPGALLSLGDLHAAQGDGEVCGTAIEVAGT
VTLRVDLIKGGGLPWPRLETDDYWITIGSGPDLDEAARNAVREMIDLLSEEFGLSEEEAYMLLSVAGDLR
ISQVVDPNKTVHAKIPKAIFDKDG
>gnl|CDD|441972 COG2423, OCDMu, Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid transport and metabolism]. Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family is part of the Pathway/BioSystem: Proline biosynthesis
MLILSAEDVAALLDMDDAIDAVEEAFRALARGRVVMPPRTVLDLPEAGGTLLLMPAYIPGGGAFGVKVVS
VFPGNPARGLPTVQGTVLLFDAETGEPLALLDGTLLTALRTAAASALAARYLARPDARTLGIIGAGVQAR
TQLRALAAVRPIERVRVWGRDPEKAEAFAARLAAEGLPVEAADDLEEAVADADIIVTATPSREPVLRGEW
LRPGTHINAVGADTPGKRELDPALLARARVVVDSREQALAEAGELQHALAAGLISEDDIVAELGEVLAGR
APGRTSDDEITVFKSVGLALQDLAAARLVYERARAAGLGTEV
>gnl|CDD|441973 COG2425, ViaA, Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown]
GVPDAAAAARLAALLLAPAPATALLLAGLLRAALALGLALALRAALLALLLLLLRAALALLTLLAGLVLL
ALDALLLAALLAALLDALLLAVLLLALLLLAALLLLAAPASAAVPLLEGPVVLCVDTSGSMAGSKEAAAK
AAALALLRALRPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGGTDIAPALRAALELLEEPD
YRNADIVLITDGEAGVSPEELLREVRAKESGVRLFTVAIGDAGNPGLLEALAD
>gnl|CDD|441974 COG2426, COG2426, Uncharacterized membrane protein [Function unknown]
LMLPKELIVFLISMLPVVELRGAIPLGIALGLPPLLAFLLAVLGNLLPVPFLLLFLRPVLKWLRRKPIFK
KFFEWLVERAKKKSKKIEKYGFLGLALFVAIPLPGTGAWTGSLAAYLLGIDFKKAFLAILLGVLIAGIIV
TLLSLGGISLLV
>gnl|CDD|441975 COG2427, YjgD, Uncharacterized conserved protein YjgD, DUF1641 family [Function unknown]
MAKPITEEELATEELEELLEKLAENADALAELLELLAELKESGLLDALNGLLEAREDVLKILVDALNDEE
VTNLIENLMSLLELLSKLDPEDLVKLLNKLVDALKEAAEALAEPEPVGLFGLLRALRDPDVQRGLGFLLA
FLKALGKSLKEEA
>gnl|CDD|441976 COG2428, Sfm1, Rps3 or RNA methylase involved in ribosome biogenesis, SPOUT family [Translation, ribosomal structure and biogenesis]
MKKPLIVIEHLEPELSPWLLLEYRHVSRLAGKDRLVFTNVPEEYHKILSKLGIVVSESVVELVGSLLIDP
SRVIILDPKAEKELTPEDLSEAKYVVVGGILGDHPPRGRTRELITSRLKGAKARNIGPGQFSIDGAVYVA
KLILRGKRLEEIEYVDGPTIELDEFVEVELPYAYPLVEGKPLISPGLIEYLKRGLPEEEEREL
>gnl|CDD|441977 COG2429, Gch31, Archaeal GTP cyclohydrolase III [Nucleotide transport and metabolism]. Archaeal GTP cyclohydrolase III is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
MIQVTLIQIDNYGPWTVTPGPRREWDLQTLQSRLYADLQQLFGARGGYVFFTRFDNMIAVTNGLDLEDHA
EIQESIRNRYPVTVSMGIGTGETPYEALENATEALQEAGSAQDEDRREVLADDRGDDDVQIAHFDVNDAT
GKYTDRLSAYDTFILIEQLYAKLMEYLREHGSLSFFVGGDNFIAVCPDLSKADYEDAIDHVKEEVGVELK
VGIGIGKTARDAGMLAKHALEEIREKRTSGKVEELS
>gnl|CDD|441978 COG2430, COG2430, Uncharacterized conserved protein, DUF432 domain [Function unknown]
MSMFGRYEPFKIEIGGIEISIEKEGGILRYRRYCDGGVVEKLIVSGGGRILINPIEPVNLPKYITKYLLI
RFEKPIVVPPGSSVTIYLKFPVEIGVFVGSKGSYELIDVFSLGKPKYALYGSPENGVICRYWKSEVYSEP
PEDPLGEGVIKLVIVNNSDEWVEVSKIVFPAYGLKLYYNEDKAYYMSINMTIKSRNVAEVEFTRKPPREG
LKKSLELYPARIILVKFLMEWGL
>gnl|CDD|441979 COG2431, LysO, Lysine export protein LysO/YbjE, DUF340 family [Amino acid transport and metabolism]
MKESLILLGAVVLGILLGLFLLLLLALPDSLSTYALYLLLFLVGIQLGNSGISLRQIKSLNRRGLLIPLA
VILGSLLGGALAALLLGLPLKEGLAIASGFGWYSLSGILITDAYGPVLGSIAFLNNLLRELLAILLIPLL
ARRGPLAAIAVGGATSMDTTLPVIQKSGGKEYVPIAIVSGFILSLLVPILIPLFLS
>gnl|CDD|441980 COG2433, COG2433, Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]
VFGVDIQSGSPRGDAPSYALVILDDGKIVKRDEVSLRKLLRLIWEEKPDIVAVDNIYELAADKDELVRFL
RMLPPGTKLVQVTGGERPEPLSRLARRHGIPFGKLDPMEEAEACARLAALGVGYEVSAFEDKTKIKVSRG
RSPGKGGWSQNRYTRRIHGAVKRAAREIESILDEAGLDYDLEVREGYGGLSRAVFTVYAPREELPVSPSR
GGDVRVRIEPVRRDKIEFEPLKKRRKYLIVGIDPGTTTGIAVLDLDGEVLDLYSSRTMDRAEVIEWISER
GKPVIVATDVTPMPETVEKIRRSFNAVLYTPKEDLSVEEKLHLAREYGYDNDHERDALAAALKAYDAYKN
KFERVEKKVPPDVDRDEVKARVIRGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEE
QVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEE
LKRKLERLKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYGLKEGDVVYLRDASGAGRSTAELLAEAGP
RAVIVPGELSEAADEVLFEEGIPVLPAEDVTIQEVDDLAVVDEEELEAAIEDWEERAEERRREKKAEMLE
RLISEYRAERRKGL
>gnl|CDD|441981 COG2440, FixX, Ferredoxin-like protein FixX [Energy production and conversion]
LFLNNYNVDEDQPHIKVKDPDICIARCLAKPCTRYCPAGVYEIVGDGRLQINYENCLECGTCRIKCPTQN
ITWVYPEGGGGVNYRFG
>gnl|CDD|441982 COG2441, COG2441, Predicted butyrate kinase, DUF1464 family [General function prediction only]
MMRVAGIDPGTKSFDLVVLEDGRVVLEKSIPTEEVASNPEIVVEELEELGPVDAIAGPSGYGLPLKRAEE
ITDRDLFEMTLVRKDDVGALVYIGLRKLVRLLKESKLPVYFIPGVIHLPTVPAWRKINRIDMGTADKLAV
AALALAEEARREGVDYSEVNFIVVEIGYGYNAAIAVKNGRIVDGIGGTSGFPGYLSIGAMDGELAYLLGR
FSKKDLFRGGLADLAGTSSPEEFIKRADPNCEEAFEAFIESIVKDVAALLASVKPDRVYLSGRFSRIPDL
RKYLEERLEDKFEVRKLKGLPAAKAKEAAQGAAIIADGLAGGKYKELVEHLELREARGTVLDYVTHPGLL
REKLRKEYRKL
>gnl|CDD|441983 COG2442, COG2442, Predicted antitoxin component of a toxin-antitoxin system, DUF433 family [Defense mechanisms]
LLDRITIDPEILGGKPCIRGTRIPVETILELLAAGMSPEEILEDYPDLTLEDIYAALAYAAAHLEEIE
>gnl|CDD|441984 COG2443, Sss1, Preprotein translocase subunit Sss1 [Intracellular trafficking, secretion, and vesicular transport]
MAIKIQEKLKELLKDYKRVLKLARKPDKEEFLQIAKITGLGILLIGLIGFIIYLIMTLLPGGV
>gnl|CDD|441985 COG2445, YutE, Uncharacterized HEPN domain protein YutE, UPF0331/DUF86 family [General function prediction only]
RERIEEKLEYIEEYLARLEELAELSPEEFLSDPTEQDAVERNLQLAIEAAIDIGNHIIAGFGLRDPGSYR
DIFDILAEEGVISEELAEKLKKMVGFRNILVHDYLEIDLEEVYEILKEHLDDLEEFIKEIRK
>gnl|CDD|441986 COG2450, SepFarc, Predicted archaeal cell division protein, SepF family [Cell cycle control, cell division, chromosome partitioning]
MMGFLKKILGGTSKPRSEEDYVELDLDDYEEAEGEAKVYVKVAEIEDLEDVPAIKDEVYDGNIVIADITR
LKTDDETLERILKELKQVARDVGGDIVGLGDDQIIITPTGVKISREKIGGGE
>gnl|CDD|441987 COG2451, Rpl35A, Ribosomal protein L35AE/L33A [Translation, ribosomal structure and biogenesis]. Ribosomal protein L35AE/L33A is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MKGVILSYRRGKNTQYNNQVLIKVLGVNDRKEASKLIGRKVIWRDPTGNKYKGKIVRVHGTKGVVRARFK
PGLPGQALGDTVEII
>gnl|CDD|441988 COG2452, COG2452, Predicted site-specific integrase-resolvase [Mobilome: prophages, transposons]
LTPGEAAELLGVSPKTLRRWEKEGKLPAIRTPGGHRRYPESEVERLERRTVIYARVSSADQKDDLERQVE
RLEEYATAKGYQDEVIKDVGSGLNYKRKGLLKLLERIEVERVVVEHKDRLARFGFELLEALCEAYGVEIV
VVNQESPEQELVEDLIAIITSFSARLYGLRSYKKAVKE
>gnl|CDD|441989 COG2453, CDC14, Protein-tyrosine phosphatase [Signal transduction mechanisms]
SWIIPGLLAGGPLPGGGEADLKREGIDAVVSLTEEEELLLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAV
DFIDEALREGKKVLVHCRGGIGRTGTVAAAYLVLLGLSAEEALARVRAARPGAVETPAQRAFLERFAKRL
>gnl|CDD|441990 COG2454, COG2454, Predicted nuclease, contains PIN domain [General function prediction only]
PEALEKLREAAEDLRYLLNRGYPKKSALNLVGNRYRLSKRQRLALYRCVHSDEEIALRKSKLVPLEALKG
KELAIDGFNVLITLESALSGGPLFLCDDGFIRDLAGVHGTYKIVEETEEALELIGEALKELGPKKVIFLL
DAPVSNSGELAGLIRELLEEYGINGEVELVKNPDKELKEASGIVATSDSVILDRVERWFDLAAEIIEEYI
PDAWVVDLSP
>gnl|CDD|441991 COG2456, COG2456, Uncharacterized conserved protein, DUF2304 domain [Function unknown]
MILIQIILIIFALALIVYVIRRLRKARLSAIRRLFWLAFWLVAILAAIFPGILTRVANLLGVGRGLDLLL
YLLIVLLLYLLFRLYLRISKLERKITKLARELALREAELPDLEGKDET
>gnl|CDD|441992 COG2457, COG2457, Uncharacterized conserved protein, DUF447 domain [Function unknown]
MIYETIVTTLDADGRPNAAPMGIIVKGDELVLRPFKGSTTYENLLATGEAVVNVTDDPRVFAGSLFGRLD
PEDFPLVPAERVDGPRLKDALAHIELEVTSIEDDSERPVLELRVVHIGIHRPPFRGFNRAQAAVIEAAVL
ATRLHLLPKEKILEEIAYLRIAIEKTGGPREKEAWEWLMEKVE
>gnl|CDD|441993 COG2461, COG2461, Uncharacterized conserved protein AF0170, contains SAB, hemerythrin HHE, and PAS domains [General function prediction only]
MSDEERKELLKEIIKRLHEGESLEEVKEEFKELFKGVSPSEIALAEQELIKEGIPVEEIQKLCDVHAALF
RGSLEEEEEPELPPGHPVHTLKKENDAIRKLLEELKELLPELEKAEDEDSKEEILNKLLELLNKLREIDK
HYARKENLLFPYLEKYGITGPPKVMWGVDDEIRDLIKELRKLLEEEEGDIEEFKEKLEELVEEIEEMIFK
EENILFPMALELLSEEEWKEIYEESDEIGYCLIEPPEEWKPEEEPVYLKEEEAELDRDGEIDLDTGYLTV
EQLNAILNTLPVDITFVDENDIVRYFSDGKERIFPRTKSIIGRKVQNCHPPKSVHIVEKILEDFKSGKKD
EAEFWINMGGKFVYIRYFAVRDENGEYLGTLEVTQDITPIRELEGEKRLL
>gnl|CDD|441994 COG2469, CheF, Archaeal chemotaxis protein CheF [Signal transduction mechanisms]
MSEGESKIADFVGRFVQVVKDGRKLNDAEWVSGRILLSNKRLVLATNDGKRTIPLSSVFDVAVGYDVPQD
LAFFSDYVTIAYGEDEDRRVALIEGAETVEKFETVLFRALLNGTTVLVKHPAVVGGVVQDTEWEKARLKV
DEEAVRFAGPDGSFVEIDLDDVGDVERGERTVDGEERPVLEVEHTDDGTSVTTYIAGSSRKMNLLGRLLR
LEYEELEEDLEDIDLSEEEKEVLMALYSGVSPFELPDFLGMDVDEVEEILDRLIEKGLVEEVRTRTEVAL
TPRGRNIASEAIEDV
>gnl|CDD|441995 COG2501, YbcJ, Ribosome-associated protein YbcJ, S4-like RNA-binding protein [Translation, ribosomal structure and biogenesis]
EYITLGQLLKLAGLVESGGEAKALIAEGEVKVNGEVETRRGRKLRPGDVVEVGGETIRVVA
>gnl|CDD|441996 COG2502, AsnA, Asparagine synthetase A [Amino acid transport and metabolism]. Asparagine synthetase A is part of the Pathway/BioSystem: Asparagine biosynthesis
MMKLIIPKGYKSLLDLRETQIAIKKIKDFFQKELAKELNLTRVSAPLFVRPETGLNDDLNGVERPVSFDI
KDMGDAEAEIVHSLAKWKRMALKRYGFEPGEGLYTDMNAIRRDEELDNLHSIYVDQWDWEKVITKEDRNL
EFLKETVRKIYKVIKRTEDYLLEKYPQLKPKLPEEITFITSQELEDMYPDLTPKEREDAIAKEYGAVFIM
GIGGVLKSGEPHDGRAPDYDDWSLNGDILVWNPVLDRALELSSMGIRVDEEALKKQLKIAGCEDRLNLPF
HKMLLNGELPLTIGGGIGQSRLCMFLLRKAHIGEVQASIWPEEMIEECEKNGIHLL
>gnl|CDD|441997 COG2503, COG2503, Predicted secreted acid phosphatase [General function prediction only]
MKKLKLSIAALLLLLALAGCATTPAPAAAAAAQQNLPDQNLMAVLWMQTSAEYRALAYQAYNLAKLRLDA
ALAQPSGGKPPAVVLDLDETVLDNSPYQAWLIKNGKSFDPKTWDEWVKEAQATAVPGAVEFLNYANSKGV
TVFYISNRKAEEKAATLANLKALGFPVVDEDHLLLKTDGSDKEARRQAVAKRYRIVMLVGDNLGDFADAF
DKKSNAERRALVEQNAAKFGTKWIVLPNPMYGSWESALYDNYYKLSPEEKLQLRRDALK
>gnl|CDD|441998 COG2508, PucR, DNA-binding transcriptional regulator, PucR/PutR family [Transcription]
LALLLLLAALLAAAALAARLAALARAAALLLVLLAAALAALAAGAALLLRVVRLVLALELADLLLLLLGL
LLLLLAGAGAALEAAAAYLALALLRERAAARRLRAELLDDLLEGRLEEDLAARAALVSYREARRALRLAR
ALPGGGRVVRYDDLGLYRLLLALADPEALRAFVERVLGPLLEYDAEHGTDLLETLRAYLDNGGNVSATAR
ALHVHRNTVRYRLRRIEELLGRDLDDPEDRLELQLALRLLRLLGAAR
>gnl|CDD|441999 COG2509, COG2509, FAD-dependent dehydrogenase [General function prediction only]
MIRTNLKLPLDDEEALKAAIAKKLGIPSLKYDVVIVGAGPAGLFAALELAEAGLKPLVLERGKDVEERTC
PVAEFWRKGKCNPESNIQFGEGGAGTFSDGKLNTRSKDPQGLIRYVLEIFVKFGAPEEILYAAKPHIGTD
KLPKVVKNIREYIEELGGEIRFNTRVTDILIEDGRVKGVVTNDGEEIEADAVILAPGHSARDWFEMLHRL
GVKLEAKPFDIGVRVEHPQELIDRIQYGKFAGHPLLGAAEYKLVYQTKNYGRGVYTFCMCPGGFVVAEAS
EPGLVVVNGMSYSDRKSENANFALLVSVTPTDFPGGPLAGIEYQRSIERLANELGGGNYKAPAQRLGDFL
AGRRSTELGSVEPTYKPGVTPGDLSLVLPYRILDALREALEAFDKKIPGFASDDALLYGVETRTSSPVRI
PRDEDLETNIKGLYPAGEGAGYAGGIVSAAVDGIRVAEAIAEKLGP
>gnl|CDD|442000 COG2510, RibN, Riboflavin transporter RibN, EamA domain [Coenzyme transport and metabolism]
SWLLLALLSAFFAGLTAIFAKIGLKGIDPNLATFIRTLVALIFLLLILLVTGKLGELPELSPKSWLFLLL
SGLATGLSWLFYFRALKLGPASIVAPIDKLSPVFTVLLSVLFLGERLTLKQIIGILLIVAGVILLSLK
>gnl|CDD|442001 COG2511, GatE, Archaeal Glu-tRNAGln amidotransferase subunit E, contains GAD domain [Translation, ribosomal structure and biogenesis]
MSELDYEELGLKVGLEIHQQLDTKTKLFCNCPTELREPESDREFTRYLRPTKSELGEIDRAALEESKKGR
KFEYLAYPDTTCLVEADEEPPHELNREALEIALAIALLLNMNIVDEVHVMRKIVIDGSNTSGFQRTALVA
LGGYIETEGGKVGIQTICLEEDAARKIEETGDGVVYSLDRLGIPLVEIATAPDIRSPEQAREVALRIGML
LRSTGKVKRGLGTIRQDVNVSIAGGARVEIKGVQDLDLIPKIVEYEVKRQVNLLEIRDELRERGASVEDI
EIVDVTDVFKDTKSKVIKKALKKGGKVLAVKLPGFAGLLGREIQPGRRLGTELADYAKFWGVGGIFHTDE
LPNYGITEEEVEALREALGAGEEDAFVIVADEEEKAKKALEAVIERAKEALEGVPEETRAALPDGTTRYL
RPLPGAARMYPETDIPPVEIDEEELEEAKKNLPELPEEKVERLVKEYGLNEELAEQIVDSERLDLFEELV
EKKGVDPTLIASTLTSTLTELRREGVDVENLTDEHIEEVFDLVAEGKIAKEAIEEILEALAENPDLSAEE
AVEELGLGGLSEEEVEEIIDEVVEENADQVKEKGMGAFGPLMGEVMKELRGKADGKLVSEILREKIQKRL
>gnl|CDD|442002 COG2512, COG2512, Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain [General function prediction only]
MLVVAALLLYPELLEDERRVLELLRENGGRMTQSEIVKETGWSKSKVSRLLSRLEERGLIEKERVGRENV
VELPEDEPEA
>gnl|CDD|442003 COG2513, PrpB, 2-Methylisocitrate lyase and related enzymes, PEP mutase family [Carbohydrate transport and metabolism]
SKRARFRALLASGGILVLPGAWDALSARLAEQAGFEALYLSGAGVAASLLGLPDLGLLTLTEVLEHARRI
ARAVDLPVIADADTGFGNALNVARTVRELERAGVAGIHIEDQVGPKRCGHLPGKEVVPAEEMVERIRAAV
DARRDPDFVIIARTDARAVEGLDEAIERAKAYAEAGADVIFVEALTSLEEIRRVAAAVDVPLLANMTEGG
KTPLLTAAELAELGVRRVSYPVSLLRAAAKAAERALRELREDGTQAALLDAMQTFAELYELLGYDEYEAL
EKRYFKFK
>gnl|CDD|442004 COG2514, CatE, Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism]
ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVLEEAPGAPPRPGAAGLDHVAF
RVPSRADLDAALARLAAAGVPVEGAVDHGVGESLYFRDPDGNLIELYTDRPRFEHVGDLETDVLGFRLSD
P
>gnl|CDD|442005 COG2515, Acd, 1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism]
RFPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQ
SNHARATAAAAAKLGLKCVLVLRGEEPTPLNGNLLLDRLLGAELHFVSRGEYRDRDEAMEAVAAELRARG
GKPYVIPEGGSNPLGALGYVEAAAELAAQLAELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGIS
VLKGADFLRERVAELARATAALLGLVSRADIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTG
KAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGYAE
>gnl|CDD|442006 COG2516, COG2516, Biotin synthase-related protein, radical SAM superfamily [General function prediction only]
LQSLGVRDPPAGPSDHKALTISGETVRVSVGTATALGYSKIAFLHGPTVLALTVLQGCIRNCQFCGIARS
LAAGRDRTIRVKWPTYDLEQLAEVAKAAVELDGVKRMCMTTGTPPGSDRGAAESARAIKAAVDLPISVQC
EPPDDDAWLERLKDAGADRLGIHLDAATPEVFERIRGGKARVSWERYWEAIEEAVEVFGPGQVSTHLIVG
LGETEEEIVELCQRLIDMGVYPFLFAFTPIPGTPLEDHPAPPIAFYRRIQLARYLIDKGLRSEDIFRFDD
GGQVVDFGVELLRLINSGKAFMTAGCPGCGACNRPYYNERPG
>gnl|CDD|442007 COG2517, COG2517, Predicted RNA-binding protein, contains C-terminal EMAP domain [General function prediction only]
MWDTANDYRILVAEKAVELLERIVENVKLPGPWNKKEALKLAKEIKSEIQRLKYSYMPPTELAKSPEVKK
LKEKAEEIIEALLGEEWLEKFLEREKTEENIAEIRYFLNTLYGLPARLKLGEINDPLYAVDIEVGEVISV
SKHPSADKLWVCNVNCGKRAYTVVTNDLDVRKGEVVAVALLPPREFMGVVSEGMFLGAPLKDVKGEKGEL
PPGINLEALGEVRAIVYAILKS
>gnl|CDD|442008 COG2518, Pcm, Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones]
VQQLRPRGVTDPRVLDAMRAVPRELFVPEALRELAYADRALPIGHGQTISQPYIVARMLEALDLKPGDRV
LEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDGALGWPEHAPFDRIIVTA
AAPEVPEALLEQLAPGGRLVAPVGEGGVQRLVLITRTGDGFERESLFEVRFVPLRGG
>gnl|CDD|442009 COG2519, Gcd14, tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]. tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification
EGDRVLLTDPKGRKYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVTTSKGKEFLVLRPTLYDYVLSMKR
GTQIIYPKDAGYIIARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFG
LPDNVELKLGDIREGIDEGDVDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALRESGF
TDIEAVETLLREWKVEGLAVRPEHRMVGHTGFLVFARKL
>gnl|CDD|442010 COG2520, Trm5, tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]. tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification
LCVKVPKKEAERVRRRLREEGLLDKDRKIKVDGDYVYIPVTEPPEDGEVVEQEFPEREPPSLKELLEGGL
PEELLELLPSSYDIIGDIAIIKIPDELEEYKEEIAEAILESHPNVKTVLAKASGVEGEFRVPELELLAGE
GRTETIHRENGCRFKLDVAKVYFSPRLATERLRIAELVKPGERVLDMFAGVGPFSIPIAKRSGAKVVAID
INPDAVEYLKENIRLNKVEDRVTPILGDAREVAPELEGKADRIIMNLPHSADEFLDAALRALKPGGVIHY
YEIVPEEDPFERAEERIEEAAEEAGYEVEILEKRRVKSYSPGVYHVVVDVRVS
>gnl|CDD|442011 COG2521, COG2521, Predicted archaeal methyltransferase [General function prediction only]
MPHYSKGPLLTGYEARALLAARRKAGEVEVSLDLGLTRSKVELDGEGVVFPDGQRLDLDELEKIAKDRST
IYVVDDGELYPVEIFSEGYYKLVPTGDGAPTLEINGIHMHRIKGTDPLEDARRKVKLVGVRRGDRVLDTC
TGLGYTAIEALKRGAREVITVEKDPNVLELAELNPWSRELANERIKIILGDASEVIKTFPDESFDAIIHD
PPRFSLAGELYSLEFYRELYRVLKPGGRLFHYTGNPGKKKRGRDVPRGVAERLRKAGFKRVRRVEEAQGV
LAVKR
>gnl|CDD|442012 COG2522, AF0184, Predicted transcriptional regulator, contains XRE-type HTH domain [Transcription]
MKLPCEIAVREVLPAIRALLAKELVERGLSQSEIAKLLGITQAAVSQYLSGKRGASERIEFDEEIKELIE
ELAEGLASGKPEDALAEICRLCRELLKRG
>gnl|CDD|442013 COG2524, COG2524, Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]
LLVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAA
AVRVVAEKELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKA
LAEGRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL
>gnl|CDD|442014 COG2602, YbxI, Beta-lactamase class D [Defense mechanisms]
MKKLLLLLALLLLLACPANAAAAAANVIERPDLAKLFDEAGVEGTFVLYDLKTGKYIVYNKERAETRFSP
ASTFKIPNSLIALETGVIKDENEVFKWDGVKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKY
LDKLNYGNADISGGIDTFWLDGSLKISALEQIDFLKRLYRNKLPFSKRTQDIVKDIMIVEKTPNYTLYGK
TGWGFRDDPDIGWFVGWVEKNDNVYFFATNIDIPDEADLPKRKEITRKILKQLGLLP
>gnl|CDD|442015 COG2603, SelU, tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal structure and biogenesis]. tRNA 2-selenouridine synthase SelU, contains rhodanese domain is part of the Pathway/BioSystem: tRNA modification
MSKRITLDDFLELLDDDPLIDVRSPVEFAEGHIPGAINLPLLDDEERAEVGTCYKQQGPFAAIKLGHALV
SGKLAAHREEAWAFAPKHPRPLVYCWRGGLRSGSVAQWLREAGIDVPRLEGGYKAYRRFVLDELERLPAP
LPLIVLGGPTGSGKTRLLHALAAQGAQVLDLEGLANHRGSSFGRIGLGPQPSQKDFENLLAIALLKLDPA
RPVVVEDESRRIGRVHLPDALYEAMRQAPLVLLEAPLEERVERLLEDYVDLMLADPEYLKEALDRIRKRL
GGERYQELLALLEAGDHEEWIEELLEEYYDPMYRYSLEKKADRIVFRGDAEEVLAFLAALS
>gnl|CDD|442016 COG2604, COG2604, Uncharacterized conserved protein [Function unknown]
DLLIVFGLGLGYHIEALLEKLPEKRLIVIEPDLEIFKLSLETIDLSELLSDKRLYLLVGDDLEEIFDLLN
SLIDIFGKNINLIILPSYLKLYPEEYLELKKLLKEYIKKKLINLGTYFDFGLLWLENFLKNLPYILKSPP
IKDLKNKFKGKPAIIVSAGPSLDKNIELLKELRDKALIIAVGTALKALLKNGIKPDFVVSIDPGEANYKH
FKGEFLKDIPLIFSSTVHPEILKLYKGPKLFFKSGGFPLAKWFEGLELGLLESGGSVANTALDLAVKLGC
KPIILIGQDLAYTDGKTHAKGSVYEEKDDELLEELEDYLEVEGNFGEEVKTTRVLLSYRKWFEQFIAKYP
EIKFINATEGGAKIEGTEPLPLEEVIEKYLKKEIDKRIKKKKNKYDKKKVLKKLEELLKELKKIKKLLEK
ALELLEKLLEELEKKKLDKIDKELKKNELLASIVQPFLIKEEEEKLLRIIKKNKELYEGLLELLELLEKA
L
>gnl|CDD|442017 COG2605, COG2605, Predicted kinase related to galactokinase and mevalonate kinase [General function prediction only]
IISRAPLRISFAGGGTDLPPYYLEHGGAVLNAAIDKYAYVTLEPRFDGKIRLSSSDTERVETVDEDDDIP
HPVIREALKLFGIGDGLEITTDSDAPAGSGLGSSSALTVALLNALHALLGLPLSPYDLARLAYEIERNDL
GEPGGKQDQYAAAFGGFNFIEFGPDGRVIVNPLRISPEILNELESNLLLFYTGITRESSDILKEQVKNVE
DGDEATLEALHEMKELALEMKEALLKGDLDEFGELLNEGWELKKRLASGISNPAIDEIYELARKAGALGG
KLLGAGGGGFLLFYAPPERREAVREALSKAGLRVVPFSFDKEGSQVWR
>gnl|CDD|442018 COG2606, EbsC, Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal structure and biogenesis]
TPVRRALDAAGIPYEVVEHPEPAATAEEAAEALGVPPEQIAKTLVFRGDGGPVLAVVPGDRRLDLKKLAA
ALGAKKVEMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARL
TGATVADIARPA
>gnl|CDD|442019 COG2607, Atu1564, Predicted ATPase, AAA+ superfamily [General function prediction only]
MTDEELLARLERLLEALERLLPPPPGGPDFAAADAFRWRRRGGGGRLEPVPHPDPIRLDDLVGIERQKEI
LIRNTEQFLAGLPANNVLLWGARGTGKSSLVKALLNEYADQGLRLIEVDKEDLADLPDIVELLRGRPERF
IIFCDDLSFEEDETSYKALKAVLEGGLEARPDNVLIYATSNRRHLMPEYMSDNERPVDGEIHPGEAVEEK
LSLSDRFGLWLGFYPPDQDEYLAIVRHLAAHFGLDIDDEELRREALQWALTRGGRSGRVAWQFIDDLAGR
LGLALD
>gnl|CDD|442020 COG2608, CopZ, Copper chaperone CopZ [Inorganic ion transport and metabolism]
MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKA
E
>gnl|CDD|442021 COG2609, AceE, Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion]. Pyruvate dehydrogenase complex, dehydrogenase (E1) component is part of the Pathway/BioSystem: Pyruvate oxidation
MSMDGLPSQLPDIDPQETQEWLESLDAVIEEEGPERARYLLERLLERARRSGVGLPFSATTPYINTIPVE
QEPPYPGDEELERRIRSIIRWNAMAMVVRANRKGGGLGGHISSFASAATLYEVGFNHFFRGPDHPGGGDL
VYFQGHASPGIYARAFLEGRLTEEQLDNFRQEVDGKGLSSYPHPWLMPDFWQFPTVSMGLGPINAIYQAR
FMKYLHNRGLKDTSDRKVWAFLGDGEMDEPESLGAISLAAREKLDNLIFVINCNLQRLDGPVRGNGKIIQ
ELEGVFRGAGWNVIKVIWGSEWDPLLAKDTDGALVKRMNETVDGDYQTYKAKDGAYVREHFFGKYPELKA
LVADMSDEDIWRLNRGGHDPRKVYAAYKAAVEHKGQPTVILAKTIKGYGMGEAGEGRNITHQQKKLDLDD
LKAFRDRFNIPISDEQLEELPYYKPAEDSPEMKYLHERRKALGGYLPQRRTKAEPLEVPELSAFAALLKG
SGKREISTTMAFVRILNDLLKDKEIGKRIVPIVPDEARTFGMEGLFRQIGIYSPVGQLYTPVDADQLLYY
KESKDGQILQEGINEAGAMSSWIAAGTSYSTHGVPMIPFYIYYSMFGFQRVGDLAWAAGDQRARGFLIGA
TAGRTTLNGEGLQHQDGHSHLLASTIPNCVSYDPAFAYELAVIVQDGLRRMYGEQENVFYYITVMNENYA
QPAMPEGVEEGILKGMYLLKEGEGKGKPRVQLLGSGTILREVLAAAELLAEDWGVAADVWSVTSFNELRR
DGLDVERWNLLHPEEEPRVPYVTQCLAGAEGPVVAATDYMRAVPDQIRPWVPGRYTVLGTDGFGRSDTRE
ALRRFFEVDRYSIVVAALKALADEGKIDASVVAEAIKKYGIDPDKPNPLTA
>gnl|CDD|442022 COG2610, GntT, H+/gluconate symporter GntT or related permease, GntP/DsdX family [Carbohydrate transport and metabolism]
MMLLLGLLLAIALLILLIIKFKLHPFLALLLAALLVGLLAGMPLAKIVTSIMTGFGGTLGSIGLVIGLGA
MLGKLLEDSGAAERIADTIIKKFGEKRAPLALVLAGFILGIPVFFDVGFVILAPLAFSLARRAGISKLLI
GLALAAGLSTTHMLVPPTPGPLAAAGILGADLGAVILLGLIVAIPALIVGYLYAKWLGKKAPVPAPEGLA
GEEDEEEEDDEELPSFGLALLPILLPIVLILLGTIADLLPKDSALVQVLAFIGDPIIALLIGVLVAILLL
RRGLSREELMKILNEGLKPAGLILLITGAGGAFGAVLAASGIGDAIADALSGLGLPPLLLAFLIAALLRG
ATGSATVAMITAAGILAPLLLALGVSPELLVLAIGAGSGGLSHVNDSGFWLVKEYFGLTVKETLKTWTVM
TTIIGVVGLVLVLILSLLFG
>gnl|CDD|442023 COG2703, COG2703, Hemerythrin [Signal transduction mechanisms]
LEWSDELSVGIPEIDEQHKELFELINELYDALESGKGREELAELLDELLDYTEEHFAREEALMEEYGYPD
LEEHKAEHRRFLEELEELRERLEAGDLELARELLEFLKDWLVNHILKEDKKYARYLKKKGAG
>gnl|CDD|442024 COG2704, DcuA, Anaerobic C4-dicarboxylate transporter [Carbohydrate transport and metabolism]
MFWLQLLVVLAAIFIGARLGGIGLGLAGGLGLAILVFGFGLKPGSPPIDVMLIIMAVITAAAALQAAGGL
DYLVQIAEKLLRKNPKRITFLAPLVTYLFTVLAGTGHVVYSLLPVIAEVAKKNGIRPERPLSIAVVASQI
AITASPISAAVVALLAILAPHGVSLLQILAVTIPATLIGVLVAALVSLRRGKELDDDPEYQERLADGEVR
KYIYGETLLDKELPPGAKLSVLIFLLGIVAVVLLGAFPSLRPGFIDDGKGKPLSMTSAIQMVMLTAAALI
LLVCKVKPAKIANGSVFKAGMVAVIAIFGIAWMGDTFFSAHMAEIKEALGDLVQAYPWLFAVALFLVSVL
LYSQAATTKALMPLGLALGIPPPVLIASFPAVYGYFFLPTYPTLLAAINFDRTGTTRIGKYVLNHSFMIP
GLIGVVVSVAVGFLLASLIL
>gnl|CDD|442025 COG2706, Pgl, 6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism]
MKRLLLSTFVYVGTYTSGESEGIYVFRLDTATGELTLLGLVAALGNPSFLALSPDGRFLYAVNEVDDGGV
SAFRIDPADGTLTLLNTVSSGGASPCHLSVDPDGRFLFVANYGGGSVSVFPIDADGSLGEPVQVIQHEGS
GPNPERQEGPHAHSVVFDPDGRFLYVPDLGTDRIYVYRLDPATGKLPEPPEVSLPPGSGPRHLAFHPNGR
FAYVINELDSTVSVYAYDAATGTLTLIQTVSTLPEDFTGENWAADIHISPDGRFLYVSNRGHNSIAVFAI
DADGGKLTLVGHVPTGGKWPRDFAIDPDGRFLLVANQKSDNITVFRIDADTGKLTPTGRSVPVPSPVCVA
FL
>gnl|CDD|442026 COG2707, YeaL, Uncharacterized membrane protein, DUF441 family [Function unknown]
MESTLILLVLLLLGLLGKNNSVTIAALVLLLLKLLPLDKVFPFLEKKGLNLGIIILTIAVLVPIASGKIG
LKDLLKSFKSWKGLLAILVGILVAWLGGRGVDLLSSQPEIVVGLVIGTIIGVAFFKGVPVGPLIAAGITA
LILKLIRLF
>gnl|CDD|442027 COG2710, NifD/CfbD, Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and metabolism, Inorganic ion transport and metabolism]
NRKALGVNPAKGCQPLGAKLALLGIKDAIPLVHGSQGCAAYSRVTRGRHFKEPIPLFSTDMTEDDVVFGG
EKNLEEAIKNIIERYKPKLIFVYTTCLTETIGDDIEAVIKEAREELGIPVVPVSTPGFVGSHSTGYHIAV
EAIVEQLVGTGEPKTPGKINLIGGYNLIPGDLWEIKRLLEEMGLRVIALPDLGGTTVEEIADAGRAKLNL
VLCSRSGNYAARYLEEKYGIPYLEFVSPIGLEATDEFLRKLAELFGKPVPEVIARERGRLVDALADYHFY
LGGKKVAIYGDPDLLWGLASFLLELGMEPVAAVTTTGSPEDYERIKELLEELPEGTVIDDGDLEELEELL
KELKPDLLIGGSKGKYLARKLGIPLLRVGFPIYDRVGLQRRPYAGYRGALNLLEDIANALLSPVWE
>gnl|CDD|442028 COG2715, SpmA, Spore maturation protein SpmA (function unknown) [General function prediction only]
MLNYIWLGMILIGIVVALINGRFEAVTKAAFDSAKTAVEIAIGLIGVMALWLGIMKIAEKAGLIDKLARL
LRPLFRRLFPEVPKDHPAMGAIVMNLSANMLGLGNAATPLGLKAMEELQKLNPDKDTASNAMITFLVLNT
SSITLIPTTVIAIRAQAGSANPTDIVGPTLLATFISTLAGIIADKIFQRINLRRPST
>gnl|CDD|442029 COG2716, GcvR, Glycine cleavage system regulator GcvR [Amino acid transport and metabolism]
MQHLVITAIGPDRPGIVAALARAVSEHGCNILDSRMARLGGEFAGILLVSGPWDAIAKLEAALPALAAEL
GLLVTVKRTEPHEAPPAGLPYVVEVVGNDRPGIVAEVTQFLAERGINIEDLSTKTYPAPMSGTPLFSAQI
TVHVPAGLDIDALRDALEDLADELNVDISLEPIK
>gnl|CDD|442030 COG2717, MsrQ, Heme-binding membrane subunit of periplasmic DMSO/TMAO and protein-methionine-sulfoxide reductases [Energy production and conversion]
TARRLPWLKPLVFLLALLPLLWLVWLALTGGLGADPVEALIHFTGDWALRLLLATLAITPLRRLTGWPWL
LRLRRMLGLWAFFYALLHLLAYLWLDLGFDLALIWADIVKRPYITVGFAAFLLLLPLALTSTNAAIRRLG
RRWKRLHRLVYLAAVLAVLHFFWLVKSDVTEPLLYAAILALLLAWRLPKARRRRRRAAAA
>gnl|CDD|442031 COG2718, YeaH, Uncharacterized conserved protein YeaH/YhbH, required for sporulation, DUF444 family [General function prediction only]
MSIIIDRRLNLKRKSAVNRQRFLRRVKEAIKKAVADAVSEESIIDSDGGEKIKIPIRDLSEPRFRHGSGG
KREHVGPGNGEFVVGDRIGRPPGGGGGGGKGQAAGDGEGEDDFEFELSREEFLDLLFEDLELPNLVKKQL
AEIEEEKTRRAGFRKKGSPSNLDKKRTLREALKRRIAEGRIKRIPFIDPDDLRYRRWEKVPKPESNAVMF
CLMDVSGSMGEFEKDLAKRFFFLLYLFLRRKYEKVEIVFIRHHTEAKEVDEEEFFHSGESGGTIVSSALE
LMLEIIEERYPPSDWNIYAAQASDGDNWSSDNPRCVELLEELLPLCQYFGYGEITPYERGSTLWREYERI
ADEFPNFAMVRIREKEDIYPVFRELFKKEEAEAAA
>gnl|CDD|442032 COG2719, SpoVR, Stage V sporulation protein SpoVR/YcgB, involved in spore cortex formation (function unknown) [Cell cycle control, cell division, chromosome partitioning]
MSTGSDWTFELLERYDEEIEEIAKEFGLDFYPNQIEVITAEQMLDAYASVGMPTRYPHWSFGKQFEQLEK
SYRRGLSGLAYEIVINSNPCIAYLMEENSLTMQKLVIAHAAYGHNDFFKNNYLFRTWTDARSILDYLAFA
KNYIARCEERYGVDAVEAFLDACHALMNHGVDRYKRPPKLSLAEERERQREREEYLQRQYNDLWRTLPEL
EEQDKEEAAKRRRFPEEPEENLLYFLEKNAPLLEPWQREILRIVRKEAQYFYPQRQTKVMNEGWATFWHY
TIMNELYDEGLLTDGEMIEFLHSHTNVVAQPPFDSPYYSGINPYALGFAMFRDIERICENPTDEDREWFP
DIAGSGDWLEKLFEARRNFKDESFIRQFLSPKLIRDFKLFSFLDDDREPELEVSAIHDERGYRKVREQLA
RQYNNGGREPNIQVVDVDYRGDRELTLRHRVHEGRPLDLDYAEEVLKHLARLWGRPVHLETVDEDGKVLL
SYDGKPHSRRKL
>gnl|CDD|442033 COG2720, YoaR, Vancomycin resistance protein YoaR (function unknown), contains peptidoglycan-binding and VanW domains [Defense mechanisms]
GVAGGGVLAAAALALALLLAAAALALVLAVPSVVVLGGAVALAGAAVGVGGDGSAALAAALASAALAATE
LVVLLLTLAVLTDTAALVAAALLAAAVAAAAAAVAVEGGGDAGLGLAAAAALADLAAAGGALAAPLEPSL
DEEKLRAALEEIAAELERPPKDARLRIEGGKPVIVPEVDGRKLDVEKLLAALLAALTGGERTVELPVAEV
EPKVTTEDLEALGIKEVIGEFTTPFDGSQANRTTNIRLAAEKLNGTLVKPGETFSFNKTVGPRTAANGYK
EAPVIVNGKLVPGVGGGVCQVSTTLYNAALFAGLEIVERHPHSYPVSYYPAGRDATVAYGYIDLKFKNDT
DYPVLIQAYVTGGSLTVEIYGTKPYDTVEIETEVTNVTPPKTVYKEDSLPPGEECVPQEGAPGFTVTVYR
VVYDNGKVVKREIFTSTYDPWPAVVCGPP
>gnl|CDD|442034 COG2721, UxaA, Altronate dehydratase [Carbohydrate transport and metabolism]
MKLLIIHHDDDVVVAVVDLAGGGEGTVGGGGVTLLEDVPAGHKKAAADIAAGGEVVKYGVVIGGAAADIP
AGGWVHHHNNNLAAAPELDDYAYATWPAPDVPLEGRTFMGYRRPDGRVGTRNYVLILPTVGCSNRVARRI
AEAFERPDFPNVDGVVALTHPYGCGQLGEDLELLRRTLAGYARHPNVGGVLVVGLGCENNQIDRLAEEIG
ARDGKPVEFLTIQEVGGTRDTIEAGVRLARELLQEANEDRREPVPLSELVVGLKCGGSDGFSGITANPAL
GYASDLLVAAGGTVILSETPELFGAEHLLARRAATPEVAEKLVDLVNWYEDYAAAHGVDLGNNPSPGNKA
GGLTTIEEKSLGAIAKGGTSPIVDVLDYAEPPTKKGLVFMDTPGNDPESVTGLAAAGANLVLFTTGRGTP
FGNPIAPVIKIATNTALAERMPDDIDFDAGTILDGEETIEEAGEELFELILDVASGRLTKAEILGHGEFV
IWKLGVSL
>gnl|CDD|442035 COG2723, BglB, Beta-glucosidase/6-phospho-beta-glucosidase/beta-galactosidase [Carbohydrate transport and metabolism]
KRKRFPKDFLWGAATAAYQIEGAWNEDGKGPSIWDTFSRTPGKVVNGDTGDVACDHYHRYKEDIALMAEL
GLKAYRFSIAWPRIFPDGEGEVNEAGLDFYDRLIDELLAAGIEPFVTLYHWDLPQALEDYGGWLNRDTAD
AFADYAETVFERFGDRVKYWITFNEPNVSAFLGYLLGGHAPGRKDLKAALQAAHHLLLAHALAVKALREI
GPDAKIGIVLNLTPVYPASDSPEDVLAARRADALFNRWFLDPLLRGEYPADLLELLEEHGILPEITPGDL
EIIKNPVDFLGVNYYTPTVVKADPGGESPFFGNFFVGVVNPGLPTTDWGWEIDPEGLRDLLNRLYDRYGL
PLYITENGAGADDEVEEDGRVHDDYRIDYLREHLAAVHRAIEDGVDVRGYFVWSLIDNFEWANGYSKRFG
LVYVDYDTQKRTPKKSFYWYKEVIA
>gnl|CDD|442036 COG2730, BglC, Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]
AAMGPRLRGVNLGNWLELWFETLWGNITEEDIDAIADWGFNTVRLPVSWERLQDPDNPYTLDEAYLERVD
EVVDWAKARGLYVILDLHHAPGYQGWYDAATQERFIAFWRQLAERYKDYPNVLGFELLNEPHGATWADWN
ALAQRAIDAIRATNPDRLIIVEGNNWGGAHNLRALDPLDDDNLVYSVHFYGPFVFTHQGAWFAGPTYPAN
LEARLDNWGDWAADNGVPVFVGEFGAYNDDPDASRLAWLRDLLDYLEENGIGWTYWSFNPSGDTGGLLDR
GTGDWGDDRGLLKAL
>gnl|CDD|442037 COG2731, EbgC, Beta-galactosidase, beta subunit [Carbohydrate transport and metabolism]
MIIGNLSNLDRYAGLPPALKKALEFLKETDLAALPPGRYEIDGDNIFANVQEYETKPAEERKAEAHRKYI
DIQILLSGEERIGYAPLENLEVSEPYDEEKDIQFYEDIEPESFLTLQPGDFAIFFPEDAHKPGCAVGE
>gnl|CDD|442038 COG2732, BarS, Barstar, RNAse (barnase) inhibitor [Transcription]
TVVIDGSEIRDEEDFYRQLARALDFPDYFGRNLDALWDCLTGGVELPVELVWKNAEASRRRLGEDFEALI
EVLEEAEEELEGDLRFNLRD
>gnl|CDD|442039 COG2733, YjiN, Uncharacterized membrane-anchored protein YjiN, DUF445 family [Function unknown]
MTTPSRALRRMKRLATGLLLLAAALFLAALALPDRGPWLGYVRAFAEAAMVGALADWFAVTALFRHPLGL
PIPHTAIIPRNKDRIGDSLGDFVEENFLSPEVIREKLRRVDPARRLGDWLADPENAERLARELARLLPGA
LDVLDDERVQAFIERALRRRLRGIDLAPLLGRLLEALTEDGRHQELLDLLLDRLAEWLADNETREFLAEL
IREWVREESPSWLPKLPDDWVDDKLADRIVRALLSLLEEVRADPDHPLRQAFDRWLREFIDRLQHDPETA
ARVEELKRELLDHPALREYLGDLWESLRAWLLEDLADPDSALRRRLAAALQSLGERLAEDPALRARLNEW
LRDAAARLVERYRDEIGRLISDTVKRWDAEELSRKIELKVGRDLQFIRINGTLVGGLVGLLLYALSQLLG
G
>gnl|CDD|442040 COG2738, YugP, Zn-dependent membrane protease YugP [Posttranslational modification, protein turnover, chaperones]
MFFDPYIILLIPALLLSLWAQAKVKSTFKKYSKVPSSSGLTGAEVARKMLDDNGLYDVRVESVPGQLTDH
YDPRNKVVRLSEDVYNGRSVAAAAVAAHEVGHAIQHAEGYAPLKLRSALVPVANFGSNLSWILILIGLLL
GSPGLLLIGIILFAAAVLFQLVTLPVEFDASRRALAWLESGGILTQEELPGAKKVLNAAALTYVAAALVA
LLQLLRLLLIFGGRRD
>gnl|CDD|442041 COG2739, YlxM, Predicted DNA-binding protein YlxM, UPF0122 family [Transcription]
LEKTVRINLLFDFYGELLTEKQREYLELYYNDDLSLGEIAEELGISRQAVYDNIKRAEKILEEYEEKLGL
VEKFQKRQKLLEEIKELLEELEESEDDEELEKLIEELEELEE
>gnl|CDD|442042 COG2740, YlxR, Nucleoid-associated protein YlxR, Predicted RNA-binding, DUF448 family [General function prediction only]
MMKAKKIPLRTCIGCRERKPKKELIRIVRSPDGEVVPDPTGKLPGRGAYLCPDRECLEKAVKKRAFARAL
KAKVPEDLYDELEELLERRALRR
>gnl|CDD|442043 COG2746, YokD, Aminoglycoside N3'-acetyltransferase [Defense mechanisms]
PVTRESLAADLRALGVRPGDTVLVHSSLSSLGWVCGGAQAVIEALLDVVGPEGTLVMPTQSGDNSDPATW
ENPPVPEEWWETIRAEMPAFDPATTPTRGMGAIPETFRTWPGVVRSDHPQASFAAWGPDAEEITADHPLD
YGLGEGSPLARLYELDGKVLLLGVGYDTNTSLHLAEYRADAPGKRTVRYGAPILEDGERVWVEFEDIDTD
SDDFEEIGEAFEAEGIVRKGKVGNADSRLFDARDLVDFAVDWLEEH
>gnl|CDD|442044 COG2747, FlgM, Negative regulator of flagellin synthesis (anti-sigma28 factor) [Transcription, Cell motility]
MKINGTGPLSVTAVNPYQKAAATAASAGKAAAAASAAAASDSVELSSAAKQLQQLEELASSPDIDAERVA
EIKQAIANGTYKVDAEKIADKLLAFERELLG
>gnl|CDD|442045 COG2755, TesA, Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism]
MKAAAGKPLRIVALGDSITAGYGASRERGWPALLARRLAAADVRVVNAGISGATTADLLARLDRDLLALK
PDLVVIELGTNDLLRGLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYLNERIEAYNAAIR
ELAAEYGVPLVDLYAALRDAGDLPDLLTADGLHPNAAGYRLIAEAVLPALK
>gnl|CDD|442046 COG2759, MIS1, Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]
MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEG
KTTTTVGLGQALNRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLL
AALIDNHIHQGNELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGVPREDGFDITVASEVMAILCLAT
DLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVHGGPFANIAHGCN
SVIATKLALKLADYVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVAKDELTEENL
EALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGVRVALSEVWAKGGEGAEELA
EAVVEACEEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQ
YSLSDDPKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDIDEDGKITGLF
>gnl|CDD|442047 COG2761, FrnE, Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones]
PLKIDIFSDVVCPWCYIGKRRLEKALAEFGDDVEIRWRPFELNPDMPPEGEDRREYLLAKGSPEQAEQMR
AHVEEAAAEEGLPFDFDRIKPPNTFDAHRLLKAAELQGKQDALLEALFEAYFTEGRDIGDREVLLDLAAE
VGLDAEEFRADLESDEAAAAVRADEAEARELGVTGVPTFVFDGKYAVSGAQPYEVFEQALRQALA
>gnl|CDD|442048 COG2764, PhnB, Zn-dependent glyoxalase, PhnB family [Energy production and conversion]
SVTPYLVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELRIGGSVLMLSDAPPDSPAAEGNGVSLSL
YVDDVDALFARLVAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMINTP
>gnl|CDD|442049 COG2766, PrkA, Predicted Ser/Thr protein kinase [Signal transduction mechanisms]
MTGMDLLERLAERYRREAALEWEGSFAEYLDLVREDPRVARTAAQRLLDMIDSAGTETVDEPGDEIRRYR
FFDDPFNDGEHAFFGLEETLERIVDYLRSAARGLGERKRILLLHGPVGSGKSTLARCLKRGLEEYSRTDE
GALYTFEWNFPSADDDIKGSPMHEHPLHLFPPEEREDLLEELNERDDHYGIRIEGELSPWCRKRLEALLE
EYGGDILKVLEHVRVERLVVSERDRVGIGTFEPGDEKNQDISELTGDVDLRKLAEYSESDPRAFSYDGEL
NQANRGLLEFVEMLKAPIKFLYPLLTATQEGNVKLTKFAAIDIDEVILAHSNESEYAAFRNNKKNEALKD
RLILVKVPYLLRVSEEVKIYEKLLTNSDLRGRHIAPHTLEVAALFAVLTRLKEPENAGLSLVEKMRLYDG
ESLPTGFKAKDVKELRDEAGVDEGMSGISPRYVRDILSNALNSDTDEVCLNPLDVLNELEEGLKQHPVFS
EEERERYLNFIEVVREEYLEFVKKEVQKAYLLSYEEYGQELFDRYVDHVDAWIQDEKVRDPITGEEEDPD
ERLMRSIEEQLGIPENAKKDFRREIINAILRYARDNPGEKFDYTSYERLREAIEKKLFEDVKDLLKVTSP
FTAKPDTETQKKIEEVVDRLIEEYGYCEASARLLLEYVMRVRARG
>gnl|CDD|442050 COG2768, COG2768, Uncharacterized Fe-S cluster protein [Function unknown]
HSLGKPYVDEEKCIGCGACVKVCPVGAISIEDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEEDEEFQEK
MAEY
>gnl|CDD|442051 COG2770, HAMP, HAMP domain [Signal transduction mechanisms]
LLLLLLALLLLLLLLLLLLLLAGALLVLALISLRLLLALLLLLLLLLALLLLLLLLLLLLLAALVLLALL
LAAALLLLLLLLSLVALAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALLLALAL
LALLLGLAAARLLLAALLALAAALALALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAA
LLLLLLLALLALLLALLLALLLARRITRPLRRLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRMADS
LRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADL
LLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALA
LLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELL
LLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLALAA
VEAAALLLAALLLAAVAALLELAALLLLLLAAAEALAALELELAAAAEAALAEAELLEVAAAAEAGAALL
A
>gnl|CDD|442052 COG2771, CsgD, DNA-binding transcriptional regulator, CsgD family [Transcription]
LLLLALALLLLALLLLLLALLALLLLLLLAALLLLLALLLLAALLLLAAAAAALAAALAAALLLGLLLLL
LIALLLLLLLLLALLLLLALLALLAALLARLAALLLALALAALLLAALARLLARAPGLTPREREVLRLLA
EGLTLKEIARILGISERTVRTHLKRIYRKLGVSSRAELVALALRLGLI
>gnl|CDD|442053 COG2801, Tra5, Transposase InsO and inactivated derivatives [Mobilome: prophages, transposons]
ELAEEEELRKEEELLRRLLLLLRLLLLRRRVLRRVSRRRRRLLRLLRRRRARSRRRRRLRRPRSYRADED
AELLERIKEIFAESPRYGYRRITAELRREGIAVNRKRVRRLMRELGLQARRRRKKKYTTYSGHGGPIAPN
LLFTATAPNQVWVTDITYIPTAEGWLYLAAVIDLFSREIVGWSVSDSMDAELVVDALEMAIERRGPPKPL
ILHSDNGSQYTSKAYQELLKKLGITQSMSRPGNPQDNAFIESFFGTLKYELLYRRRFESLEEAREAIEEY
IEFYNHERPHSSLGYLTPAEYEKQLAAAA
>gnl|CDD|442054 COG2802, LON/PUA, Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown]
ADLPMELPLFPLGAVLFPGGRLPLHIFEPRYLDMVRDCLAGDRPFGVVLIREGREVGGPPPLYDVGTLAR
ITDFEELEDGRLDITLRGVQRFRILEELQEDDPYRVAEVEWLPDEPDLPVPEELEALRERLLRLLRRYPE
LAGLEADPDLDDPEWLSNRLAELLPLDPEEKQALLEAPDLLERLELLLALLERE
>gnl|CDD|442055 COG2804, PulE, Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
GALSLLLRLGDLLVEAGLISEEQLLAALAEQKKTGKPLGELLVELGLVTEELLAEALAEQLGLPFVDLDE
LEIDPEVLELLPEELARRHRVLPLRLEGGTLTVAMADPLDLEALDELRRLTGRPVEPVVATESDIERALD
RLYGSESSIEELLEELAEDLTSEEEDLEDLLEEADDAPVVRLVNAILEDAIKEGASDIHIEPYEKRLRVR
FRIDGVLREVLRLPKSLAPALVSRIKIMANLDIAERRLPQDGRIKLRLGGREIDLRVSTLPTVYGEKVVL
RILDKSAALLDLEQLGFSPDQLERLRRLIRRPHGIILVTGPTGSGKTTTLYAALNELNTPERNIITVEDP
VEYQLPGINQVQVNPKIGLTFASALRSILRQDPDVIMVGEIRDLETAEIAVQAALTGHLVLSTLHTNDAP
SAITRLLDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEPDPEELERLGLPPEELAPLTFYRGVGCEH
CNGTGYKGRTGIYELLVIDDELRELIAEGASAAELREAARKEGMRTLREDGLEKVLQGITTLEEVLRVTG
E
>gnl|CDD|442056 COG2805, PilT, Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures]
MAMDLDELLKLAVEQGASDLHLTVGSPPMLRIDGELVPLDDPPLTPEDLEALLKEILTEEQRERLEEEGE
LDFSYSLPGLGRFRVNIFRQRGGVAAVLRLIPSEIPTLEELGLPPVLKELAELPRGLVLVTGPTGSGKST
TLAAMIDYINETRAKHIITIEDPIEFVHKHKKSLINQREVGRDTPSFANALRAALREDPDVILVGEMRDL
ETIEAALTAAETGHLVFATLHTNSAAQTIDRIIDVFPPEEQAQIRSQLAESLRGVISQRLLPRADGGGRV
AAREILVNTPAVRNLIREGKTHQIPSLIQTGKKLGMQTMDQSLAELVKEGLITEETALAYAS
>gnl|CDD|442057 COG2807, CynX, Cyanate permease [Inorganic ion transport and metabolism]
MSTTSSSARRSRRAGRWLLLLAIVLVALNLRPAITSVGPLLPEIRADLGLSATQAGLLTTLPLLAFGLFA
PLAPRLARRFGLERTLLLALLLLAAGLLLRSLAPSVALLLAGTALIGAGIAVGNVLLPGLIKRWFPDRVG
LMTGLYTAAMGLGAALAAGLTVPLAAALGWRGALAVWALLALLALLLWLPLLRRRPAAAAAAPAAASLRS
LWRSPLAWLLTLFFGLQSLLYYAVVAWLPPILRDAGLSAATAGLLLSLFQLAGIPGSLLVPLLADRLGDR
RPLLLLLGLLGLAGLLGLLLAPGSLPWLWAVLLGLGQGGLFPLALTLIGLRARTPAEAAALSGMAQSVGY
LLAALGPLLVGALHDATGSWTAALLLLAALAVLMLVAGLLAGRPYVEDA
>gnl|CDD|442058 COG2808, PaiB, Predicted FMN-binding regulatory protein PaiB [Signal transduction mechanisms]
YIPPHFRETDPEELRALIRAHPFATLVTAGDGGPLATHLPLLLDEDAGEGGVLIGHVARANPQWRALAAG
GEVLVIFQGPHAYISPSWYPSKRVVPTWNYVAVHAYGRLEVIDDPEELRALLERLTARFEAGRPEPWSVD
DAPEDYIDRLLRGIVGFEIEITRLEGKFKLSQNRPAADRAGVIAGLEASGDPAARALAAL
>gnl|CDD|442059 COG2810, COG2810, Predicted type IV restriction endonuclease [Defense mechanisms]
MTAPADLQSLVERILRNLDYLSLRSANEAATRQEFIDPLLEALGWDIDNPEEVIPEERVEGGRPDYALRL
NGKRKLFVEAKKPGVNLKDKPARQARSYAWSSGVRWAILTNGREWRVYDAQEKTSPRPIELDTALEARLL
LLEYEELSSELDLILSRIIVDTDLLARLTLGLLDSELKERKLLSDSDPLLLEIDARLKETLGTAIKSTVL
SGPILTDLREDRELSVVGLSKSLDELLEELELKKDADEVLKGLGPPDRKYSGRSLRRSKSEVLGIKDDIA
ISIYLLLLPLVTLELVLKLIEDRLSIGEIGHLQSREILNEVKVLREELLRNILEVTGSRA
>gnl|CDD|442060 COG2811, NtpH, Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]. Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase
MDRPEVLKEIKEAEEEADEIIEEAKEEREERIAEAREEAEEIIEQAEEEAEEEAQERLEEAREEAEAEAE
EIIEEGEKEAEALKKKAEDKLDKAVELLVEEFEEAVHA
>gnl|CDD|442061 COG2812, DnaX, DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]
MSYQVPQTFDDVVGQEHVVRTLKNALASGRLAHAYLFTGPRGVGKTTLARILAKALNCENGPTGEPCGEC
ESCRAIAAGSHPDVIEIDAEASNIGVDDIRELIEKVSYAPVEGRYKVYIIDEAHMLTTEAFNALLKTLEE
PPPHVVFILATTEPQKLLPTILSRCQRFDFRRLPPEEIAEHLAKIAEREGIEIEPEALALIARAADGSMR
DALSLLDQAIAFGLLDRRELLLDLLEALLAGDVAALLALAEELAKRGRDLKRFLDDLLSLLRDLLLLKLG
PDAELLVNEDERERLQELARRLSPERLLRAIQILLEARRELERNVNPRLALEMLLLRLAR
>gnl|CDD|442062 COG2813, RsmC, 16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]. 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification
APAASDWPRTITVRLAGRDLTFVTLPGVFSRDRLDIGTRLLLEHLPEPLGGRVLDLGCGYGVIGLALAKR
NPEARVTLVDVNARAVELARANAAANGLENVEVLWSDGLSGVPDGSFDLILSNPPFHAGRAVDKEVAHAL
IADAARHLRPGGELWLVANRHLPYERKLEELFGNVEVLARNKGFKVLRAVK
>gnl|CDD|442063 COG2814, AraJ, Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism]
MPATPRRRWLALLALALGAFLSGLGIGIVLPALPLIAADLGASPAQAGLVVTAYLLGAALGAPLAGRLAD
RFGRRRVLLLGLLLFALGSLLCALAPSLWLLLAARFLQGLGAGALFPAALALIADLVPPERRGRALGLLG
AGLGLGPALGPLLGGLLADLFGWRWVFLVNAVLALLALLLLLRLLPESRPAARARLRGSLRELLRRPRLL
LLLLLAFLLGFGFFALFTYLPLYLQEVLGLSASAAGLLLALFGLGGVLGALLAGRLADRFGRRRLLLIGL
LLLALGLLLLALAGSLWLLLLALFLLGFGFGLLFPLLQALVAELAPPEARGRASGLYNSAFFLGGPLA
>gnl|CDD|442064 COG2815, PASTA, PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis]
LLLLVLLLLALVGAGWLFTSPGEEVTVPDVVGMTVDEAEAALEEAGLKVEVEEEYSDDVPAGTVISQDPA
AGTKVKKGSTVTLTVSKGPEKVTVPDLVGKSLDEAEAALEAAGLKVGEVEEEYSDDVPKGTVISQSPAAG
TEVPKGTTVTLVVSKGPEPVTVPDLVGLTLEEAKAALEAAGLKVGVVEEEYSDDVPAGTVISQSPAAGTK
VEKGSTVTLT
>gnl|CDD|442065 COG2816, NPY1, NADH pyrophosphatase NudC, Nudix superfamily [Nucleotide transport and metabolism]
MSAPLAFAGSPLDRAAELRADPDWLAAWADPRVLVVDGGRLLLLEDGGELLLPAGEAADLGPPAEAVFLG
LDDGRPVFAVDLPAELELPEGAEFVDLRELGGLLDPRDAGLAARAVALLNWHRTHRFCGRCGAPTVVAAA
GWARRCPACGAEHYPRTDPAVIVLVTDGDRILLARQARWPPGRYSLLAGFVEPGETLEQAVRREVFEEVG
VRVKNVRYVGSQPWPFPSSLMLGFTAEADSGEITVDGDEIEDARWFSRDELPAALAGLLLPPPGSIARRL
IEAWLAGP
>gnl|CDD|442066 COG2818, Tag, 3-methyladenine DNA glycosylase Tag [Replication, recombination and repair]
MPDGMKRCPWAGSDPLYRAYHDTEWGVPVHDDRALFEKLCLEGFQAGLSWITILRKREAFRAAFDGFDPE
KVAAYDEADVERLLADPGIIRNRLKIEATINNARAFLALQEEFGSFSAYLWSFVDGKPIVNRPKTLAEVP
ATTPLSDALSKDLKKRGFKFVGPTTCYAFMQAVGMVNDHLVGCFRRGEVAA
>gnl|CDD|442067 COG2819, YbbA, Predicted hydrolase of the alpha/beta superfamily [General function prediction only]
LIALGQTEYFTLESPILGEDRRIRVYLPPGYDAPEKRYPVLYMLDGQNLFDALAGAVGTLSRLEGGIPPA
IVVGIGNGDDGERRLRDYTPPPAPGYPGPGGPGGGADAFLRFLEEELKPYIDKRYRTDPERTGLIGHSLG
GLFSLYALLKYPDLFGRYIAISPSLWWDDGALLDEAEALLKRSPLPKRLYLSVGTLEGDSMDGMVDDARR
LAEALKAKGYPGLNVKFEVFPGETHGSVAWAALPRALRFL
>gnl|CDD|442068 COG2820, Udp, Uridine phosphorylase [Nucleotide transport and metabolism]. Uridine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage
MKESELPDGSQYHLGLKPGDVADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVIST
GIGGPSAAIAVEELAALGAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELT
RALVEAAEELGVDYHVGITASTDGFYAEQGRELRVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGH
RAGSVLAVSANRVTGEFSKDPEEAVERAIKVALEALKKLIE
>gnl|CDD|442069 COG2821, MltA, Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis]
MRRLLLLLALLLLAACATQPPPPGAAAPDARLQPVSFSDLPGWADDDLAAALPAFRRSCRRLARRPAASA
YGITAADWRAACAAARQLPAADPAAARAFFEREFQPYQVVGPDGGGNGLFTGYYEPELEGSRTRTAEYRY
PLYRRPPDLVTVDLGSFELKGKRLRGRLEGGRLVPYPTRAEIEAGALAGRGLELAWVDDPVDAFFLQIQG
SGRVRLPDGSLIRVGYAGKNGHPYTSIGRLLIDRGELPLEQMSMQAIRAWLRANPEELRELLNQNPSYVF
FRELPGPDAGPLGALGVPLTPGRSIAVDPSLIPLGAPVWLETTLPDANFSGKPLRRLMIAQDTGGAIKGA
VRADLFWGTGDEAGERAGRMKHPGRLWVLLPKGAAPPL
>gnl|CDD|442070 COG2822, EfeO, Iron uptake system EfeUOB, periplasmic (or lipoprotein) component EfeO/EfeM [Inorganic ion transport and metabolism]
FELLDGVRVVGERENIAPGLSRTLTVTLGPGTYQTACPGMLGNPRGTFTVTGGEAAAAAAADTAADLAGA
TAEYKAYVKGQVDALVTATEAFAAAVKAGDLAAAKALYAPARLHYERIEPVAESFGDLDPAIDAREDDLE
EDPEWTGFHRIEKDLWEGGSTDGLKPVADQLVADVKELKARVRTLEITPEDLANGAAELLEEVATSKITG
EEERYSHTDLWDFAANVEGAQKAFELLRPLLEKKDPALAATIDARFAAVQALLDAYRDGDGYVSYDALTK
AQRKALSAAVNALAEPLSQLAAAVG
>gnl|CDD|442071 COG2823, OsmY, Osmotically-inducible protein OsmY, contains BON domain [Cell wall/membrane/envelope biogenesis]
MKGVAAVATDRRTTGTQVDDATIEAKVKAALLADPGLDAADINVTVYNGVVTLTGQVPSEAEKDRAEEIA
RGVPGVKSVVNELRVGPPSRSNDTWITTKVKAALLADKDVPSTNIKVVTENGVVYLMGLVTQAEADAAAE
IARNVSGVKKVVNLFEV
>gnl|CDD|442072 COG2824, PhnA, Uncharacterized Zn-ribbon-containing protein [General function prediction only]
MLSRLPPCPKCNSEYTYEDGDMLYCPECGHEWAKAAAAEAEEDALVVKDANGNVLQDGDTVTLIKDLKVK
GSSFVAKRGTKVKNIRLVDGDHDIDCKIDGFGAMVLKSEFVKKA
>gnl|CDD|442073 COG2825, HlpA, Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones]
MKKLLALLALALALALSAAAAAQLKIGVVDVQRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQ
EKLQKEAATLSEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQELLQPILEKIQKAIKEVAKEEGYDL
VLDKSAVLYADPGLDITDEVLKKLNKKYPKK
>gnl|CDD|442074 COG2826, Tra8, Transposase and inactivated derivatives, IS30 family [Mobilome: prophages, transposons]
MRSYKHLTLEEREEIEALLKAGLSVREIARRLGRSPSTISRELKRNSGRRGYRAEGAQRLAEDRRRRPKR
KRKLATTPELRAYVEEKLRKKWSPEQIAGRLKREDDPGMRVSHETIYRYIYAGGLRKDLYRPLRRKRKRR
RPRGRTRKRRGKIPDRRSISERPAEVEDRAEPGHWEGDLIIGKRGKSALLTLVERKSRFVILLKLPDKTA
ESVADALIRLLRKLPAFLRKSITTDNGKEFADHKEIEAALGIKVYFADPYSPWQRGTNENTNGLLRQYFP
KGTDFSTVTQEELDAIADRLNNRPRKCLGYKTPAEVFAEELAALA
>gnl|CDD|442075 COG2827, YhbQ, Predicted endonuclease, GIY-YIG superfamily [Replication, recombination and repair]
MMYYVYILRCADNGTLYTGVTNDLERRLAEHNSGKGAKFTRKRRPVKLVYYEEFEDRSEALKREKQIKKW
SRAKKEALIEGD
>gnl|CDD|442076 COG2828, PrpF, 2-Methylaconitate cis-trans-isomerase PrpF (2-methyl citrate pathway) [Energy production and conversion]
MMQIKIPCVLMRGGTSKGVFFLASDLPADPAARDRLLLAVMGSPDPRQIDGLGGATSLTSKVAIVSPSTR
PDADVDYLFAQVSVDKPVVDWSGNCGNILAAVGPFAIEEGLVDAQDGETTVRIWNVNTGKIIVAHVPTPD
GQVQYEGDFEIDGVPGTAAPIALEFLDPAGSVTGALLPTGNAVDTIDVGGGIEVTCIDAGMPVVFVRAAD
LGLTGTELPAELDADPALLARLEAIRLAAGVRMGLGDVSRPVTPKIALVAPPRDYGTSSGTVKADDIDIL
VRYFSPGKCHHAMAVTGAVCIATAAAIPGTVVNELAGGGADRGEVRIGHPSGTLSVGAEVDGDGGGWTVT
KAGVLRTARRLMEGEVYVPADAL
>gnl|CDD|442077 COG2829, PldA, Outer membrane phospholipase A [Cell wall/membrane/envelope biogenesis]
ALERDSADNPFNLTPYKPNYFLPGTYTSNPNKEPYSPVSWAINLDNTEAKFQISFKTPLWRDLLGDNGDL
YFAYTQRSFWQLYNSDDSSPFRETNYEPELFLGFPTDYKLGGWRLRGLGLGFNHQSNGRSGPLSRSWNRV
YLRLGFERGNLTVSLRPWYRIPEDADDDDNPDIEDYMGYGDLTLGYRWGDHEFSLTLRNNLRSDNKGALQ
LDWSYPLSRNLRGYVQYFNGYGESLIDYNHRQTRIGIGVSLND
>gnl|CDD|442078 COG2830, COG2830, Uncharacterized conserved protein, DUF452 domain [Function unknown]
MKTKWLKREGSENLILFFAGWGMDPEPFRHLALPENYDVLICYDYRDLSLEEFDFSAYREIRLVAWSMGV
WVAERLLAGLIPFESAIAINGTLAPVDDEYGIPPAIFKGTLDNLSEKNRLKFYRRMCGDKELLSRYLKLP
PQRSLEEQKEELAALYEQILQRPGTDILWDKAIIGEKDRIFPAQNQLNYWQQRPCRITVLEGGHFPFYHF
KSWEELLD
>gnl|CDD|442079 COG2831, FhaC, Hemolysin activation/secretion protein [Intracellular trafficking, secretion, and vesicular transport]
ALALLLLLLLAAAAAAQAAAAAPDAGQLLRQQQQQQQLQPAPDVPPLPPPAAPAAPPAAEGPCFTIKRIR
VEGNTVLPEEELQALLAPYLGRCLTLADLNALADAITNLYRDRGYITSRAYLPPQDLSDGVLRIQVVEGR
VGRIRVEGNSRLSRAYLRSALPLAEGKPLNLRDLEQGLLLLNRLPGVQVTAELRPGTEPGTSDLVVTVEE
AKPFRGSLGLDNSGSPSTGRYRLGASLSLDNLLGLGDQLSLSYSRSLDGDGSRSYSLSYSVPLGYWGLTL
GLSYSRYRSRVGGPFGTLDISGKSQTYGLRLSYPLIRSRDQKLSLSLGLDYKDSRNYLLGTEIEVQRRRL
SVLRLGLSYTRRLGGGVLSLSLSFSQGLDWLGATPAPDASRGPDGRFTKLRLSASRVQPLPQDFSLLLRL
DGQYSSDPLLSSEQFSLGGRYSVRGYDEGELSGDNGWYLSNELRWPLPRLSLLGGLQLYAFLDAGRVWNN
SALPGQLNGRTLAGAGLGLRLSLGKNLSLDLDYARPLGDPDGDTDNRRLYFSLSYSF
>gnl|CDD|442080 COG2832, YbaN, Uncharacterized membrane protein YbaN, DUF454 family [Function unknown]
MSRMMRILYIALGWLSLGLGVIGIFLPLLPTTPFLLLAAWCFARSSPRLHRWLLNHPRFGPYIRDWREHR
AIPRRAKILALLMMALSLAISLFLVPPLWVRILLAAVLLAVAIYILRRPTPPPEE
>gnl|CDD|442081 COG2833, COG2833, Uncharacterized protein, contains ferritin-like DUF455 domain [Function unknown]
MTLREAALAVLLTADPAEKLALTRALAAAWRAGRLALDPDPGPAAPPDRPGRPARPELVPPRDVPRRSLG
TPEGRAALLHAIAHIEFNAINLALDAVLRFPGMPRAFYDDWLRVAAEEARHFRLLRERLAELGYDYGDFP
AHDGLWEMAEKTAHDLLARMALVPRVLEARGLDVTPGMIEKLRAAGDEEAAAILDIILRDEIGHVAIGNR
WFRYLCEQRGLDPEETYRELLRRYFPGRLKGPFNREARRAAGFSEDELDPLAALE
>gnl|CDD|442082 COG2834, LolA, Outer membrane lipoprotein-sorting protein [Cell wall/membrane/envelope biogenesis]
MKKRLLLLLALLLLLALAGAAQSAEEILDKLQAKLNSIKSLSADFTQTVTDAGGNEPQTSSGKFWLKRPG
KFRWEYTKPYEQLIVSDGKTVWIYDPDLNQVTVIPLSDATPLALLLGDFSDLLKDFTVTLLGEETGRKAY
VLELTPKDKDSGFGKITLWFDKETLLRKLEIYDADGQRTTITFSNVKTNPPLPDSLFTFDPPKGVEVIDQ
R
>gnl|CDD|442083 COG2835, Trm112, RNA methyltransferase activator Trm112/YbaR [Translation, ribosomal structure and biogenesis]
MDPRLLEILACPVCKGPLELDKEEGELVCTACGLAYPIRDGIPVLLPDEARPLSEDEEFS
>gnl|CDD|442084 COG2836, DsbD, Uncharacterized membrane protein, DsbD domain [Function unknown]
MIELSLLAAFLLGLLGSGHCVGMCGPIVLALSLALPPGRRRRLRQLLLYNLGRILSYALLGALAGLLGAG
LALLGSLSPAQQVLSILAGLLLILLGLYLLGWWRGLARLERLGPRLWRRLQPLLRRLLPVKSPGGAFLLG
LLWGLLPCGLVYSALLAAAASGSALQGALVMLAFGLGTLPALLAAGLLAGRLSRRLRRRVRRLAGLLLIL
LGLLTLLRGLALLGCH
>gnl|CDD|442085 COG2837, EfeB, Periplasmic deferrochelatase/peroxidase EfeB [Inorganic ion transport and metabolism]
TEADLDDIQAGILTPPQAHAIFLAFDLKDGADRAALRALLRRLTALAARLTSGAPALRLPPAGLTVTVGF
GPSLWDRLGLAPRPAELAPFPEFPGDGLDAPATGGDLLLQICADDPDVLFHAARQLLRALRGAATVRWEQ
DGFRYFPTGRNLFGFVDGTENPKGEDEADEVVLVGDEDPAWFAGGSYVVVRRIRHDLEAWDRLSLEEQEK
VIGRTKDDGAPLDGGPEFDDPDFAADAGVIPADSHVRRANPRDDGNELRILRRGMPYGDGLDPAGELDAG
LLFIAYQADPARQFEMLQRMLGGDPDGNYDRLLDFTTPVGGAYFFVPSGDFLGQ
>gnl|CDD|442086 COG2838, IcdM, Monomeric isocitrate dehydrogenase [Energy production and conversion]. Monomeric isocitrate dehydrogenase is part of the Pathway/BioSystem: TCA cycle
KMSKIIYTKTDEAPALATYSLLPIVKAFTKAAGIEVETRDISLAGRILANFPEYLTEEQRVPDALAELGE
LAKTPEANIIKLPNISASVPQLKAAIKELQAKGYALPDYPEEPKTDEEKEIKARYDKVLGSAVNPVLREG
NSDRRAPKAVKNYAKKNPHSMGAWSSDSKTHVAHMSEGDFYGNEKSVTLDKATTVKIEFVAADGTVTVLK
EKLPLLAGEVIDATVMSKKALRAFLAEQIADAKEKGVLFSLHLKATMMKVSDPIIFGHAVKVFFKDVFEK
HGDTFKELGVNPNNGLGDLYAKIEKLPEDKRAEIEADIEAVYAKRPALAMVDSDKGITNLHVPSDVIIDA
SMPAMIRDSGKMWGPDGKLQDTKAVIPDRSYAGVYQEVIDFCKKNGAFDPTTMGTVPNVGLMAQKAEEYG
SHDKTFEIPADGTVRVVDAAGNVLLEHAVEAGDIWRMCQTKDAPIRDWVKLAVNRARASGTPAVFWLDEN
RAHDAELIKKVETYLKDHDTTGLDIRIMSPVEATRFTLERIRRGEDTISVTGNVLRDYLTDLFPILELGT
SAKMLSIVPLMNGGGLFETGAGGSAPKHVQQFVEENHLRWDSLGEFLALAVSLEHLAEKTGNAKAKVLAD
TLDAATGKFLDNNKSPSRKVGELDNRGSHFYLALYWAQALAAQTEDAELAAKFAPVAKALAENEEKIVAE
LNAAQGKPVDIGGYYHPDDEKASAAMRPSATLNAIIDAL
>gnl|CDD|442087 COG2839, YqgC, Uncharacterized conserved protein YqgC, DUF456 family [Function unknown]
IILWILAILLFLVGLAGTVLPVLPGPPLIWAGLLLYGFADGFAELGWTFLIILGVLTLLSFVLDYLAGAL
GAKKFGGSKWGIWGATIGLIVGLFLFGPFGIIIGPFLGAFIGELLARRDLKQALKAGIGTLVGFLLGTVA
KLVLALAMIGWFLIAVFL
>gnl|CDD|442088 COG2840, SmrA, DNA-nicking endonuclease, Smr domain [Replication, recombination and repair]
RRKRRLSDDDRALFRQAMGDVKPLKQDNRVRPERPPPKPTPAQRARREAAALAELDPVDLAPDEPLSYRR
PGVQPGVLKKLRRGKYPPEARLDLHGLTVEEAREALAAFLAEAQRRGLRCVLIIHGKGLGSPGGRPVLKS
QVPRWLRQHPEVLAFHSAPPRHGGSGALYVLLRRSRR
>gnl|CDD|442089 COG2841, YdcH, Uncharacterized conserved protein YdcH, DUF465 family [Function unknown]
EFPEYRDLIHALKQSDAHFARLFDEYHELDKEIHRLETGVEPISDEELEELKKERLRLKDELYAMLKAAK
A
>gnl|CDD|442090 COG2842, COG2842, Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]
MTKKTQAAVAKEIGNEKLEAKIARWEAPSFVETKNVRRFAEALDEARALPGIGVVYGESGVGKTTAAREY
ANRNPNVIYVTASPSWTSKELLEELAEELGIPAPPGTIADLRDRILERLAGTGRLLIIDEADHLKPKALE
ELRDIHDETGVGVVLIGMERLPAKLKRYEQLYSRIGFWVEFKPLSLEDVRALAEAWGELTDPDLLELLHR
ITRGNLRRLDRTLRLAARAAKRNGLTKITLDHVRAAALMLGEGP
>gnl|CDD|442091 COG2843, CapA, Poly-gamma-glutamate biosynthesis protein CapA/YwtB (capsule formation), metallophosphatase superfamily [Cell wall/membrane/envelope biogenesis]
PPADTITLAAVGDVMLGRGVDQALPRYDFDYPFGDVKPLLRAADLAIGNLETPLTDSGTPYPSKGYHFRA
PPEYADALKAAGFDVVSLANNHSLDYGEEGLLDTLDALDAAGIAHVGAGRNLAEARRPLILEVNGVRVAF
LAYTYGTNEWAAGEDKPGVANLDDLERIKEDIAAARAGADLVIVSLHWGVEYEREPNPEQRELARALIDA
GADLVIGHHPHVLQGIEVYKGKLIAYSLGNFIFDQRGNPRTDDGLILRLTLEKGKVTSVELIPTRIDRYG
RPRPASGEEAARILERLERLSKDFGTKLEL
>gnl|CDD|442092 COG2844, GlnD, UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms]
AAALAALREALAEGRAALRERFRAGADGRELVRARAALVDQLLRALWDLAGLTEPERLALVAVGGYGRGE
LAPHSDIDLLFLLPDKPTPALEEVIEAFLYLLWDLGLEVGHSVRTVDECLREAREDITVRTALLEARLLA
GDEALFEELRERFRADVFWDSRAFFEAKLAEQRERHAKYGDTRYNLEPNIKEGPGGLRDLQTLLWIAKRH
FGVRSLEELVKKGLLTEEEYRELRRAEDFLWRVRFALHLLAGRAEDRLLFDLQREVAERLGYQDTEGNRA
VERFMQRYYRTAKAVGRLNEILLQRLEEAILKPPGLRRPRPINEGFQLRNGRLEVADPDVFERDPVALLR
LFLLAAQHPEGLGIHPDTLRLLRRALRLIDDAFRRDPEARRLFLEILRQPRGITRALRRMNEYGVLGRYI
PEFGRIVGQMQFDLFHVYTVDEHTLRVVRNLRRFERGELAEEFPLASELIAELPKPELLYLAALFHDIAK
GRGGDHSELGAEDARRFCPRHGLSPEDTELVAWLVRHHLLMSHTAQRRDISDPEVIRDFARLVGSEERLD
YLYLLTVADIRATGPKVWNSWKASLLRELYRATLRALRGGLEPPDREERIEERKEEALALLADQGWDEEE
IEALWARLPDDYFLRHDPEEIAWHARLLLRADDSGKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGAL
AALGLNILDARIHTTRDGYALDTFIVLDPDGEPIDDPDRLERIEQALEEALSGEVPLPEPLARRLSRRLR
HFPVPPRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQ
KLTDPERQEALREALLEALDEEAE
>gnl|CDD|442093 COG2845, COG2845, Peptidoglycan O-acetyltransferase, SGNH hydrolase family [Cell wall/membrane/envelope biogenesis]
MSTSRLVRLLLLLLLAKLPDADRVLVIGDSLAQGLAPGLQRALADQPGIRVINLSKQSTGLVRPDFFDWP
KTIRELLAEEKPDVVVVMLGANDRQDIRDGGGRLKFGSPEWEEEYRRRVDALLRALRAHGVPVIWVGLPP
MRSPRLSADMAYLNDIYREEAEKAGVIFVDTWDGFVDEDGKYTAYGPDVDGQRVRLRANDGIHFTPAGAR
KLAFFVEKEIRRLLGEAGA
>gnl|CDD|442094 COG2846, RIC, Iron-sulfur cluster repair protein YtfE, RIC family, contains ScdAN and hemerythrin domains [Posttranslational modification, protein turnover, chaperones]
MTLLTITPDQTVGDLVAENPGAAAVFRRFGIDFCCGGDRSLAEACEEKGLDPEELLAELNALANEEEEPE
IDWKSWPLDELIDYIVNTHHRYLREQLPELIRLAEKVERVHGDRHPELIGLAELFEELKEELESHMKKEE
QILFPYIRKLEEAKTAEHFGTIENPIAVMEHEHDDAGEKLEEIRELTNDYTPPEDACNTYRALYAGLEEL
EEDLHQHIHLENNILFPRALALEKELK
>gnl|CDD|442095 COG2847, COG2847, Copper(I)-binding protein [Inorganic ion transport and metabolism]
MKRLLLLAALLALAAAPALAHEAAAGDLTVSDAWVRATPPGAPVTAAYMTLTNTGDEDDRLVGASSPAAG
RVELHETVMEDGVMKMRPVEGLPIPAGGTVELKPGGYHLMLMGLKQPLKAGDTVPLTLTFEDGGTVTVTA
PVRPA
>gnl|CDD|442096 COG2848, COG2848, Uncharacterized conserved protein, UPF0210 family [Cell cycle control, cell division, chromosome partitioning]
MLNIEEILETIRMIEEENLDIRTVTMGISLLDCADSDIEKLCEKIYDKITRYAKDLVKVAEEIEREYGIP
IVNKRISVTPIALVAAASDAEDYVEIAKTLDKAAKEVGVDFIGGFSALVHKGMTKGDRALIDSIPEALAE
TERVCSSVNVASTKAGINMDAVALMGEIIKETAELTADRDGIGCAKLVVFANAPEDNPFMAGAFHGVGEP
DCVINVGVSGPGVVKAALEKVKGADLGELAETIKKTAFKITRVGELVGREAAKRLGVPFGIVDLSLAPTP
AVGDSVAEILEEMGLERCGAPGTTAALALLNDAVKKGGAMASSHVGGLSGAFIPVSEDAGMIEAVEAGAL
TLEKLEAMTCVCSVGLDMIAIPGDTPAETISAIIADEAAIGMINNKTTAVRIIPVPGKKVGDEVEFGGLL
GRAPVMPVNPFSSAKFINRGGRIPAPIHSLKN
>gnl|CDD|442097 COG2849, YwqK, Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms]
KKKEGLLKISKYLLSLKLKYELGDTLLEKNGYKSGVKEKTEDSYNEGGKLIKKKLGKGLGKYKKGKLGEW
KTYYPNGQLKSEGTYKNGKLEGEWKEYYENGKLKSEGNYKNGKLHGEWKEYYENGKLKEEGNYKNGKKDG
VWKYYDENGKLVKEEEYKNGKKV
>gnl|CDD|442098 COG2850, RoxA, Ribosomal protein L16 Arg81 hydroxylase, contains JmjC domain [Translation, ribosomal structure and biogenesis]
ISPEQFLRDYWQKKPLLIRGAFPDFVDPLSPDELAGLACEEDVESRLVSNDGQGRWQLRHGPFDEEDFAA
LPERGWTLLVQGVDHWHPEVAALLRAFRFIPDWRLDDLMISYAPPGGGVGPHFDSYDVFLLQGEGRRRWR
IGDQPDDDPELVPDLPLRILADFEPEIDWVLEPGDMLYLPPGFAHDGVALEECMTYSIGFRAPSWAELLS
ELADYLADDLLGDQRYRDPDLQARADPGEIPAAALDRLRAMLLDLLDDPELLARWLGEFLTEPK
>gnl|CDD|442099 COG2851, CitM, Mg2+/citrate symporter [Energy production and conversion]
MLALLGFLMIAVFMYLIMTKRLSPLVALILVPIIFALIAGFGPAEIGEFILDGIKSVAPTAVMFLFAILY
FGIMIDAGLFDPLIRRILRLVGGDPVKVVVGTALLAAIVHLDGDGATTFLITIPAMLPLYKRLGMSPLVL
ACLVALAAGVMNMLPWGGPTARAAAALGVDVSELFVPLIPVQIVGLVWVLAVAYLLGRRERKRLGVAGLA
GEAEGSEADAELTDEERELRRPKLFWFNLLLTLALIVLLVLGILPPAVLFMIGFAIALLVNYPNLKDQKE
RIAAHAGNALMVASIIFAAGVFTGILSGTGMLDAMANSLVSIIPDSLGPYLPLITGLLSMPLTFLFSNDA
YYFGVLPVLAEAAAAYGIDPVEIARASLIGQPVGHPVSPLVPATYLLVGLAGVDLGDHQKFSFKWAWGTS
LVMLAVAVLTGAIPL
>gnl|CDD|442100 COG2852, YcjD, Very-short-patch-repair endonuclease [Replication, recombination and repair]
LRRNDTPAERRLWQRLRNRQLRGLKFRRQVPIGGYIVDFYCPEARLAIEVDGGYHGSPEQRERDRRRDAY
LERLGWRVLRFWNEDVLRNPEGVLEEILAALEER
>gnl|CDD|442101 COG2853, MlaA, Lipoprotein subunit MlaA of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis]
MKTRLLRLLLLLLAALLLAGCASTPEPAAADPNDPLEPFNRAMFAFNDVLDRYVLRPVAKGYRAVVPDPV
RTGVSNFFSNLGEPVSFVNNLLQGKPKDAGTDLGRFLINTTFGLGGLFDVASEMGLPKHDEDFGQTLGVW
GVGSGPYLVLPLLGPSTVRDTVGLVVDTFLDPLSYVDDSAVRYALTALEGVDTRARLLDAEDLLEEASLD
PYAFVRDAYLQRRRFLIGDGNPPEDE
>gnl|CDD|442102 COG2854, MlaC, Periplasmic subunit MlaC of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis]
EDPDALVKQVADEVLAILKADKAEIKGDPEALRALVEEILLPYFDFERMARLVLGRYWRQATPEQRQRFT
EAFRQLLVRTYAGALLEYSGQKIEVLPERPLPDGDRVVVRTEIISPGGPPIPVDYRLRKKDGGWKVYDVV
VEGVSLVTTYRSQFASIIRRKGIDGLIAKLKEKNAKLAKAK
>gnl|CDD|442103 COG2855, YeiH, Uncharacterized membrane protein YadS, UPF0324 family [Function unknown]
MSALLARLRRLLPGLLLVALIALAALFLAELLPGLGALLLAILLGMLLGNLLGLPARLKPGIAFASKKLL
RLGIVLLGFRLTLQQILALGPSGLLLIVLVVALTFLLGYWLGRLLGLDRKLALLIAAGTSICGASAIAAT
APVIKAKEEDVAVAVATVFLFGTLAMFLYPLLGHLLGLSDAQFGLWAGGTIHDVAQVVAAGAAVGEEALD
IATIVKLTRVLLLAPVVLVLALYFRRRGAKGGGGGKRKPRFPWFVLGFLAASLLNSLGLLPAAVLAALKT
LSTWLLTLAMAALGLGTSLRKLRKVGGKPLLLGLILWLFLAVLSLALILLLF
>gnl|CDD|442104 COG2856, ImmA, Zn-dependent peptidase ImmA, M78 family [Posttranslational modification, protein turnover, chaperones]
IVLNSNLSPERQRFTLAHELGHLLLHRGGETDLFLSSDDKIEREANAFAAELLMPEEALRELLKEKLSED
LEELAKRFGVSEEALLYRLKELGLIDEPGLGLILL
>gnl|CDD|442105 COG2857, CYT1, Cytochrome c1 [Energy production and conversion]
ALPGAALAAGGGVHLDKGPFGTFDKASLQRGAQVFVNYCSACHSLKYVRYRRLADLGLSEDQVKANAAEF
GPAKPGDLMPSPMPNAAAAAWFGAAPPDLSLIARAREGGADYIYTYLRGFYRDPSRPTGWNNTVFPNVAM
PHPLWLQGQVTYVDGLTPAEYDQMARDVVAFLMWAAEPHLEERKRLGVWVLLFLLVFTVLAYLLKKEYWK
DVH
>gnl|CDD|442106 COG2859, SIMPL, Outer membrane channel-forming protein BP26/OMP28, SIMPL family [Cell wall/membrane/envelope biogenesis]
MKTKKSALILALILALGLIIAGYLLGNGLKKFKKADRTVTVKGLAEREVKADLAVWPISFSVTGNDLSEA
YAKLERDKAKVRAFLKSKGIPEDEISFSAPSITDKYAQQYGDNGTNEIFRYTLTQTVTVRSKDVDKVRKA
SRKITELINQGVVLTSNPPEYLFTKLNDLKPEMIAEATKDARERAEKFAEDSGSKLGKIKSASQGVFQIT
ARDSNEDGGIYDTSSIIKKVRVVSTVEYYLE
>gnl|CDD|442107 COG2860, YadS, Uncharacterized membrane protein YeiH [Function unknown]
TLLYILDLIGTFAFAISGALAAVRKRLDLFGVLVLAFVTALGGGTLRDLLLGRTPVFWLQDPRYLLVALA
AALLVFFFARLLERLRRLLLVLDAIGLALFAVIGAQKALAAGLPPLIAVLLGVITAVGGGVLRDVLANEV
PLVLRKELYATAALLGALVYVLLLALGLPPTLAALIAAAVVFALRLLAIRFGWSLPVFR
>gnl|CDD|442108 COG2861, YibQ, Uncharacterized conserved protein YibQ, putative polysaccharide deacetylase 2 family [Carbohydrate transport and metabolism]
AAKAKAVGAAAAVLAALATAAAAPAAAPLAALLLAAALAAALAGGPEPVSAEPEVPGSAPSPPAKEPAPE
DAEKELAAAPDPALLEESPFGPPVIAADGLRPWDAYARPFPAAAAAPKIAIVIDDLGYSLSGTRRALALP
GPVTLAFLPYAPYSRELAELARAAGHEVLLHLPMEPLSPKNDPGPGTLLTGMSEEEIRRRLRWALARVPG
AVGVNNHMGSRFTSDEEAMRPVMEELKKRGLFFLDSRTSPRSVAPKVAKELGVPVARRDVFLDNVQDEAA
IDKQLAKLEKIARKNGSAIAIGHPHPETLEALKEWLPELEARGIELVPVSALLK
>gnl|CDD|442109 COG2862, YqhA, Uncharacterized membrane protein YqhA [Function unknown]
MMKKLERLFERLLFASRWLLAPLYLGLILALLVLFVKFFVELWHLLPHLFSLSETDIILGVLGLIDLVLI
ANLLLIVIFGGYENFVSKIDLAEHPDRPEWLGHVDFDDLKLKLAKSIVAISSIHLLKTFLNAENITDLDL
LWQVAIHLTFVVSALYLAHTDRLSSKSHKA
>gnl|CDD|442110 COG2863, CytC553, Cytochrome c553 [Energy production and conversion]
MKLALLAAPAAAGDAARGKAYAAACAACHGADGEGNPGGGAPRLAGQHAEYLVAQLKAFRSGARKNGVMP
AIAKGLSDEDIKALAAYIASLKAPPGAA
>gnl|CDD|442111 COG2864, FdnI, Cytochrome b subunit of formate dehydrogenase [Energy production and conversion]
GRSGRKILRFSLFERINHWLVAISFILLALTGLALFFPKFFWLTPLFGGPQWARILHRFAGVVFFVGFVL
HFVYWLRHNLPNKKDLKWLKKIGGFLGGKEEEHPPAGKYNAGQKLDFWAVILGGLVLGVSGLILWFPYFA
QYFPIWVMRIALLVHAIAAILLIAAIIVHIYAATLGVEGALRAMFTGYVDEEWAKEHHPLWYEELKAKGK
LEERSAE
>gnl|CDD|442112 COG2865, COG2865, Predicted transcriptional regulator, contains HTH domain [Transcription]
EELKELLAGGESETLEFKESLNEPDEILKTVCAFANTEGGTLLIGVDDDGEIVGLDDPDKLLERLENLIA
DNISPPIRPDVEEVEIDGKRVLVIEVPPGPSKPYYLKGKGGAYIRVGSSSRPL
>gnl|CDD|442113 COG2866, MpaA, Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis]
MKLLILPATYKEVSSYDRYYTYEELLALLAKLAAASPLVELESIGKSVEGRPIYLLKIGDPAEGKPKVLL
NAQQHGNEWTGTEALLGLLEDLLDNYDPLIRALLDNVTLYIVPMLNPDGAERNTRTNANGVDLNRDWPAP
WLSEPETRALRDLLDEHDPDFVLDLHGQGELFYWFVGTTEPTGSFLAPSYDEEREAFAEELNFEGIILAG
SAFLGAGAAGTLLISAPRQTFLFAAALDIGGGGDVSAGELVAGTLLTAGGAGLGLELLVVRGTSALSLVL
KLVGAKTAELESALEAEKTVLELAELLEAASEDLLALAAVTATDAKGADLAVAGDEK
>gnl|CDD|442114 COG2867, PasT, Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis]
MPTISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEVVAELTVSFKGLRESFTTRNTLDP
PERIDFELVDGPFKHLEGRWRFEPLGEGGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR
>gnl|CDD|442115 COG2868, YsxB, Uncharacterized conserved protein YsxB, DUF464 family [Function unknown]
MIKVTIYRNKDGKIVGFEVSGHAGYAEYGEDIVCAAVSALSQTAVNGLEELLGVEPEYEVDDGYLKVELP
DLDEEQDEKAQLLLETMLLGLKTIAEEYPEYIK
>gnl|CDD|442116 COG2869, NqrC, Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrC [Energy production and conversion]. Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrC is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase
MAMNKDSNGYTILVALVLCLVCSVLVSGAAVGLKPIQEENKALDKQQNILSAAGLLEPGSAEEVEELFAK
YIEPRVVDLDTGEFVEDVDAETFDQRKAAKDPALSLPPEEDIAGIKRRERYAPVYLVKDEDGKVEKYILP
VYGKGLWSTIYGFLALEADGNTVKGLTFYHHGETPGLGAEIENPKWQAQFVGKKIFDEDGFVAIRVVKGG
ADPKDEHEVDGLSGATLTSNGVTNMLKFWLGENGYGPFLKKLREGEL
>gnl|CDD|442117 COG2870, RfaE, ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis]
MSRERLKELLPRFSRARVLVVGDVMLDRYWYGDVERISPEAPVPVVRVEREEERPGGAANVAANLAALGA
QVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTKTRVIAGGQQLLRLDFEDRFPLSAELEAR
LLAALEAALPEVDAVILSDYGKGVLTPELIQALIALARAAGKPVLVDPKGRDFSRYRGATLLTPNLKEAE
AAVGIPIADEEELVAAAAELLERLGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVFDVTGAGDTVIAT
LALALAAGASLEEAAELANLAAGIVVGKLGTATVSPEELLA
>gnl|CDD|442118 COG2871, NqrF, Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]. Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase
MTEILLGVVVFTAIILLLVGLILFAKSKLVPSGEVKITINGDGKEIEVEEGQTLLDALLRQGIFLPSACG
GGGTCGQCKVKVLEGGGDILPTETFHLSDRERKEGYRLACQVKVKSDMEIEVPEEVFGVKKWEATVVSNE
NVTTFIKELVLELPEGEEIDFKAGQYIQIEVPPYEVDFKDFDIPEEEKFGLFDKNDEEVTRAYSMANYPA
EKGIIELNIRIATPPMDVPPGIGSSYIFSLKPGDKVTISGPYGEFFLRDSDREMVFIGGGAGMAPLRSHI
FDLLERGKTDRKITFWYGARSLRELFYLEEFRELEKEHPNFKFHPALSEPLPEDNWDGETGFIHEVLYEN
YLKDHPAPEDCEAYLCGPPPMIDAVIKMLDDLGVEEENIYFDDFGG
>gnl|CDD|442119 COG2872, AlaX, Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis]
MTELLYLEDSYLKEFEATVTAVTEEGGVVLDRTAFYPTGGGQPGDTGTLVWDGKEIRVVDVRKEDGEIVH
VLEGAPLPEVGDEVTGEIDWERRYRHMRLHTALHLLSAVVYREYGAPVTGGQIGEDRARIDFDLPEFDEE
DLEEIEAEANELIAADLPVRIYWITREELEAIPGLVRTMSVLPPPGVGRVRIVEIGGVDLQPCGGTHVAN
TGEIGRIKITKIEKKGKGNRRVYFTLGE
>gnl|CDD|442120 COG2873, MET17, O-acetylhomoserine/O-acetylserine sulfhydrylase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]. O-acetylhomoserine/O-acetylserine sulfhydrylase, pyridoxal phosphate-dependent is part of the Pathway/BioSystem: Methionine biosynthesis
MTEKKYGFETLALHAGQEPDPTTGARAVPIYQTTSYVFDDAEHAADLFALKEPGNIYTRIMNPTTDVLEK
RIAALEGGVAALATASGQAAITLAILNLAEAGDHIVASSSLYGGTYNLFAHTLPRLGIEVRFVDPDDPEA
FEAAIDPNTKAIFGETIGNPALDVLDIEAIAEIAHEHGVPLIVDNTFATPYLCRPIEHGADIVVHSATKY
IGGHGTSIGGVIVDGGNFDWAANGKFPELTEPDPSYHGLVYTEAFGNAAFITKARVQLLRDLGAALSPFN
AFLLLQGLETLSLRMERHVENALKVAEFLEAHPKVAWVNYPGLPSHPYHELAQKYLPKGAGGVLTFGLKG
GREAGKKFIDSLKLFSHLANIGDAKSLVIHPASTTHSQLSEEEQAAAGVTPDLIRLSVGIEDIDDIIADL
DQALAAAT
>gnl|CDD|442121 COG2874, FlaH, Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]
EIISTGNDELDKRLGGGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGLSVTYISTELTTKEFIKQMKS
LSYDISDYLLRGRLLFLPVHPLGFEWNSKQRKDLLKRLMKYIASNLWEADVIIIDSLSALLRNAEESAIL
DFITFFKNLVDLGKTIILTVHPSALDEDILTRLRSIADVYLKLSLASVGGRVVKVLEVVKFRGARGQVGN
TISFDVDPGFGIKIEPISVA
>gnl|CDD|442122 COG2875, CobM, Precorrin-4 methylase [Coenzyme transport and metabolism]. Precorrin-4 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MKGTVYFVGAGPGDPDLITVKGRRLLEEADVVLYAGSLVPPELLAYCKPGAEIVDSASMTLEEIIALMKE
AAAEGKDVVRLHSGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRA
EGRTPMPEGESLASLAAHGATLAIYLSAHRIDEVVEELLEGYPPDTPVAVVYRASWPDEKIVRGTLADIA
EKVKEAGITRTALILVGPALGAEDFARSKLYDPGFSHGFRPAKKES
>gnl|CDD|442123 COG2876, AroGA, 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase [Amino acid transport and metabolism]. 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
ALPGVEKVVRVSKPYKLASREFKPEDTVVDVGGVKIGGGELVVIAGPCAVESEEQILETAKAVKAAGAKI
LRGGAFKPRTSPYSFQGLGEEGLKLLAEAREETGLPVVTEVMDPRDVELVAEYADILQIGARNMQNFELL
KEVGRTGKPVLLKRGLSATIEEWLMAAEYILSEGNPNVILCERGIRTFETATRNTLDLSAVPVLKELTHL
PVIVDPSHATGRRDLVPPMAKAAVAAGADGLMIEVHPDPEKALSDGPQSLTPEEFAELMEELRKLAEAVG
RRL
>gnl|CDD|442124 COG2877, KdsA, 3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase [Cell wall/membrane/envelope biogenesis]. 3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase is part of the Pathway/BioSystem: Lipid A biosynthesis
IGGIEVGNDKPLFLIAGPCVIESEDLALEIAEKLKEITDKLGIPYIFKASFDKANRSSIDSFRGPGLEEG
LKILAEVKEEFGVPVLTDVHEPEQAAPVAEVVDVLQIPAFLCRQTDLLVAAAKTGKVVNVKKGQFLAPWD
MKNVVEKVREAGNDNILLTERGTSFGYNNLVVDMRSLPIMRETGYPVVFDATHSVQLPGGQGGSSGGQRE
FVPVLARAAVAVGVDGLFMETHPDPDKALSDGPNMLPLDKLEELLEQLKAIDELV
>gnl|CDD|442125 COG2878, RnfB, Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]. Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
MSTILIAVLVLGGLGLVFGLILGYASKKFKVEEDPRVEEIDALLPGANCGQCGYPGCRPYAEAIAEGEAP
INLCPPGGAAVAEKLAELLGVEAGPLDPEVAVVRCNGGCEKAKPKYEYDGIKDCRAAVIGGPKGCEYGCI
GCGDCIKACPFDAIVGAAKGMHTVDEDKCTGCGLCVEACPVDCIEMVPVSPTVVVSSWDKGKAVRKVVGC
IGLCCKKCCPAAAITVNNLAAIIDYKKCTCCGCCEKCCPTAIIA
>gnl|CDD|442126 COG2879, YbdD, Uncharacterized short protein YbdD, DUF466 family [Function unknown]
MLARLRRALRRLRQTARLMVGVPDYDRYVAHMRRHHPDQPPMTEREFFRERQDARYGGPGGRCC
>gnl|CDD|442127 COG2880, COG2880, Predicted DNA-binding protein, potential antitoxin AbrB/MazE fold [General function prediction only]
MSKVIEAIYENGVLKPLEKVDLPEGEEVKIIIRREIRELLEKYKGILKVDEEELEELLEERED
>gnl|CDD|442128 COG2881, Yip1, GTPase-interacting Yip1 domain [General function prediction only]
MTTGGPRALVRTWKEVLLRPRRFFRKMPSPGGQAPPLVFALVVALIYALLSLLWNLLLMGPSAIPGGFPA
LGGLAGLAAALLLLILAPIFAPIGLFLVAAILHLILRLFGGDRGGFEETLRVVAYASAPCVLAIIPLIGL
IIAGIWSAYLLIVGLREVHGISTGRAALAVLLPALLLFGLGFGLIFAGAGL
>gnl|CDD|442129 COG2882, FliJ, Flagellar biosynthesis chaperone FliJ [Cell motility]
MKRSFRLQTLLDLAEKEEDEAARELGQAQQALEQAEEQLEQLEQYREEYEQRLQQKLQQGLSAAQLRNYQ
QFIARLDEAIEQQQQQVAQAEQQVEQARQAWLEARQERKALEKLKERRREEERQEENRREQKELDELASR
RF
>gnl|CDD|442130 COG2884, FtsE, Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]
MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK
RREIPYLRRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSG
GEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLEL
EDGRLVRDEARGV
>gnl|CDD|442131 COG2885, OmpA, Outer membrane protein OmpA and related peptidoglycan-associated (lipo)proteins [Cell wall/membrane/envelope biogenesis]
LSEAALGASALAIDAAGGLLSGAALLLALLGVLGSAGGLLSLADDLAEASAGAAGGAAAGAEAGGLSAGL
ELLDAGSLSATAAAGAAALLVLLAALGALGAGLAALLLAIAAAASAAAADALALAAGAAAALGALGASAA
AAAAALAAAKALGDSAAAALDAAAKAEAAAAAAALLPAAVAEVVLLSNVYFDFDSAELTPEAKAALDELA
ALLKENPDLRIEIEGHTDSRGSDAYNLALSERRAEAVKDYLVSKGIPASRITAVGYGESRPVASNDTEEG
RAKNRRVEIVVLKK
>gnl|CDD|442132 COG2886, COG2886, Predicted antitoxin, contains HTH domain [General function prediction only]
MKTITIELPDDLLLALRLTPEEFERELRLELAVKLYEEGRLSLGKAAELAGMSRAEFLELLGRRGIPVFN
YDEEDLEEDLENLEE
>gnl|CDD|442133 COG2887, Slr0479, RecB family exonuclease [Replication, recombination and repair]
RRLSPSRIETLLRCPLRYYARYILGLRDPLEPPPDAADRGTLVHAVLERFYKLPADELPAEELLALLEEA
WAELGFEDPWAAALWLERAERLLEAFLEWERAPAGLEPVAVEVEFELELPGGVRLRGRIDRIDRLPDGRL
VVVDYKTGKAPSTKDEAGEDPQLALYALALERGFEGLVPAGARLVYLGDLGKKKVLDPLEEELEEAEERL
EELAAAIADPEGPFPARPNPPLCRYCDYRHLCRVGEWG
>gnl|CDD|442134 COG2888, COG2888, Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 family [General function prediction only]
PVCPSCGREIAPEGGVAFYCPNCGEALIIRCPKCRKQSNALYFCPKCGFEGP
>gnl|CDD|442135 COG2890, HemK, Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis]
MTIRELLRWAAARLAAAGVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPL
AYILGEAEFYGLEFKVDPGVLIPRPETEELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVT
AVDISPDALAVARRNAERLGLEDRVRFLQGDLFEPLPGDGRFDLIVSNPPYIPEDEIALLPPEVRDHEPR
LALDGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVAR
RP
>gnl|CDD|442136 COG2891, MreD, Cell shape-determining protein MreD [Cell wall/membrane/envelope biogenesis]
MPRRQLLNPWLIWLSLLLALLLEILPLPGELLPFRPDWLLLVLVYWSLALPRRVGVGTAFVLGLLLDVLY
GSLLGQHALALSLVAYLALRLHQRLRNFPLWQQALIVLLLLLLAELLVFWIRLLLGGTLPGWSYFLSALL
SALLWPWLYLLLRKLRRRFKDRRVR
>gnl|CDD|442137 COG2892, Pcc1, tRNA threonylcarbamoyladenosine modification (KEOPS) complex, Pcc1 subunit [Translation, ribosomal structure and biogenesis]. tRNA threonylcarbamoyladenosine modification (KEOPS) complex, Pcc1 subunit is part of the Pathway/BioSystem: tRNA modification
MMMHRAELEFEYDDEERARAIYRSLLPEVGEIDDDRSRVTISLDGNTIVIEIEADDLSALRAALNSWLRL
IKVAEEILEIAK
>gnl|CDD|442138 COG2893, ManX, Phosphotransferase system, mannose/fructose-specific component IIA [Carbohydrate transport and metabolism]
IVIATHGPLAEGLLSSAEMILGEQENVEAVDLYPGDDPEDLREKLEEAIAELDSGDGVLILTDLFGGTPS
NVAARLLAKHENVEVIAGVNLPMLLEALTYREDLSLDELVEKALEAGREGIKSLSE
>gnl|CDD|442139 COG2894, MinD, Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning]
MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRL
KQALIKDKRFENLYLLPASQTRDKDALTPEQMKKLVEELKEEFDYILIDSPAGIEQGFKNAIAGADEAIV
VTTPEVSSVRDADRIIGLLEAKGIRKPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIV
SSNRGEPVVLDEKSKAGQAYRNIARRLLGEEVPLRDLEEEKKGFFSRL
>gnl|CDD|442140 COG2895, CysN, Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]. Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
MSTDIEAYLAQHENKDLLRFITCGSVDDGKSTLIGRLLYDTKSIFEDQLAALERDSKKRGTQEIDLALLT
DGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHS
YIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGLEDITFIPISALKGDNVVERSENMPWY
DGPTLLEHLETVEVAEDRNDAPFRFPVQYVNRPNLDFRGYAGTIASGTVRVGDEVVVLPSGKTSTVKSIV
TFDGDLEEAFAGQSVTLTLEDEIDISRGDVIVAADAPPEVADQFEATLVWMDEEPLLPGRKYLLKHGTRT
VRATVTAIKYRIDVNTLEHEAADSLELNDIGRVTLRLAEPIAFDPYADNRATGSFILIDRLTNATVGAGM
IRGALRRAAN
>gnl|CDD|442141 COG2896, MoaA, GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and metabolism]. GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) is part of the Pathway/BioSystem: Molybdopterin biosynthesis
MTSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTG
GEPLLRKDLPELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDL
DKVLAGIDAALAAGLTPVKINAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAA
EILERLEARFPLEPLPARGGGPARYYRVPGGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEV
DLRALLRSGASDEELAEAIREAIARKPEGHGFDEGDFPQPKRSMSAIGG
>gnl|CDD|442142 COG2897, SseA, 3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism]
LAAHLDDPDVVILDVRWDLPDGRAAYEAGHIPGAVFLDLDTDLSDPRSPGRHPLPSPEAFAALLGALGIS
NDTTVVVYDDGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLA
DADEVLAALGDPDAVLVDARSPERYRGEVEPIDPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAAL
GIDPDKPVITYCGSGVRAAHTWLALELLGYPNVRLYDGSWSEWGSDPDLPVE
>gnl|CDD|442143 COG2898, MprF2, Lysylphosphatidylglycerol synthetase MprF, lysyl-tRNA-binding C-terminal domain [Lipid transport and metabolism]
LLALLYKLLLLLLLALLLAAGSAVSVALGGGGLLGGAGRGRVYGAALLALFYGGAAVLALGVALLSLLLL
LLLALLSLLSLALLALLLLVLLLLLLLGLLLLLLLALLLALVLLRARRIRIGLLALALPLLLALLLLLLS
ALALLAAAAALLLILLLLGALLSFAAFAALFVAAVLAGIVSGVPGGLGVFGVVLLALLGALGLPALLALL
LLLRYRLYLLPLLLLLLLLLFLLLLARAAALAVALLRLLRPARPRPAPTAEDLERARALLRRYGGDSLSY
LALLGDKSYFFSPDGRAFIAYRVVGGVAVALGDPIGDPEDWAELIWEFLEFADRHGWRPAFYQVSEEDLP
LYRDAGLRALKLGEEAVVDLAEFTLEGKKRKDLRQAVNRAERAGYTVEVVRPPELSPALLAELRAISDEW
LAGKGLPEKGFSLGRFDEDYLPRVRLAVARDADGRVVAFASFVPVYGREGWSLDLMRRRPDAPNGVMEFL
FASLILWAKEEGYERFSLGMAPLSGVGERGGAGPVERLLRLLYRHGERFYGFEGLRRFKEKFQPEWEPRY
LAYPGGLSLPRILLALARAEGPGLRRKL
>gnl|CDD|442144 COG2899, TerC2, Uncharacterized TerC-related membrane protein, DUF475 domain [Inorganic ion transport and metabolism]
MKTLRYFRWSFLVTAVGLVLAFWYGGWTALFIVAILAVLEISLSFDNAVVNATVLKRMSPFWQKRFLTWG
ILIAVFGMRLVFPLLIVAVAAGLGPVEALDLALNDPDEYARILTDAHPQIAAFGGAFLLMVFLNFFFDEE
KDVHWLRWIERPLAKLGKLDAIEVAVALLVLLVFSYLLPAEEALTVLIAGILGLLTYLLVEGLGGLFEGE
EEGAAKAAGKAGLGGFLYLEVLDASFSFDGVIGAFAITNDIFIIALGLGIGAMFVRSLTIYLVEKGTLDE
YRYLEHGAHYAIGALAVIMLLSILVHIPEVVTGLIGVVFIGAALWSSIRRNRREAAAAAA
>gnl|CDD|442145 COG2900, SlyX, Uncharacterized coiled-coil protein SlyX (sensitive to lysis X) [Function unknown]
LEERLEELEIRLAFQEDTIEELNDVVARQQREIDRLQRQLRLLAERLKELEPSLGASPAEEEPPPHY
>gnl|CDD|442146 COG2901, Fis, DNA-binding protein Fis (factor for inversion stimulation) [Transcription]
MNASDTASSPPLRDCVRQALENYFADLDGEPPSDLYDMVLAEVEKPLLETVLEHTRGNQSRAAEMLGINR
NTLRKKLKQYGLL
>gnl|CDD|442147 COG2902, Gdh2, NAD-specific glutamate dehydrogenase [Amino acid transport and metabolism]
MTSEASKAELLEAVAELIAERLPAAQAPLVAAFARQYYRHVPPEDLAARSPEDLYGAALSHWQLAQQRKP
GEPKVRVFNPDLEEHGWQSTHTVVEIVTDDMPFLVDSVTMELNRLGLTIHLVVHPVLAVERDADGELVEV
LPADEAPADGLRESLIHIEIDRQTDPEALEELEAELERVLADVRAAVEDWPAMRARLLEIAAELEAAPPP
VDADEVAEAAAFLRWLADDHFTFLGYREYDLVGEDGDDVLRPVPGSGLGILRDDSVRVRGRSLSALPPEA
RAFAREPDLLILTKANSRSTVHRPAYLDYIGVKRFDADGEVIGERRFLGLFTSTAYNESVRDIPLLRRKV
EAVLERSGFDPGSHSGKALLNILETYPRDELFQISEDELLETALGILHLQERRRVRLFLRRDPFGRFVSC
LVYVPRDRYNTELRLRIQAILAEAFGGESVEFTTYFSESVLARVHFIVRVDPGELPDVDVAELEARLAEA
ARSWEDDLREALVERFGEERGNRLARRYADAFPAGYREDFSPRTAVADIERLESLSEEGPLAMSLYRPLE
ADPGELRLKLYHRGEPIPLSDVLPVLENMGLRVIDERPYEIEPADGEPVWIHDFGLEYPGGGEIDLDEVR
ELFEDAFAAVWRGEAENDGFNRLVLAAGLTWREVAVLRAYARYLRQIGFPFSQDYIEDTLARHPAIARLL
VELFEARFDPARDDDDREERAAALREEIEAALDEVASLDEDRILRRFLNLIQATLRTNFYQRDADGQPKP
YLSFKLDPRKIPDLPLPRPMFEIFVYSPRVEGVHLRGGKVARGGLRWSDRREDFRTEVLGLVKAQMVKNA
VIVPVGAKGGFVVKRLPAPGDREAWLAEGIACYKTFIRGLLDITDNLVGGEVVPPEDVVRHDGDDPYLVV
AADKGTATFSDIANGISAEYGFWLGDAFASGGSVGYDHKKMGITARGAWESVKRHFRELGIDIQTEDFTV
VGIGDMSGDVFGNGMLLSEHIRLVAAFDHRHIFIDPNPDAAASFAERKRLFELPRSSWADYDKSLISKGG
GVFSRSAKSIPLSPEMRAALGIEVDSLTPNELIRAILKAPVDLLWNGGIGTYVKASTESHADVGDRANDA
LRVNGSELRAKVVGEGGNLGLTQLGRIEYALNGGRINTDAIDNSAGVDCSDHEVNIKILLNRLVADGDLT
LKQRNKLLAEMTDEVAELVLRDNYRQTQALSLAEAQAAERLGEHARFIRALERAGRLDRALEFLPSDEEL
AERRAAGQGLTRPELAVLLAYAKIVLKDELLASDLPDDPYLARELVRYFPKPLRERFADEIAEHPLRREI
IATQLANDMVNRMGITFVFRLQEETGASAADIARAYVIAREVFGLPALWAAIEALDNKVPADVQLEMLLE
VRRLLRRATRWFLRNRRQPLDIAAVIERFRPGVAALRPALPELLPGEEREALEARAAELVEAGVPEDLAR
RIAALPYLYSALDIVEVAEETGRDVAEVARVYFALGDRLGLDWLREQISALPVDDRWQALARAALRDDLY
AQQRALTAAVLRSTDPGEDAEERVEAWLEANAAALERWRQMLAEIRASGTLDLAMLSVALRELRDLA
>gnl|CDD|442148 COG2904, QueFN, NADPH-dependent 7-cyano-7-deazaguanine reductase QueF, N-terminal domain [Translation, ribosomal structure and biogenesis]
NMNTLEDSPLGKKTAYPDQYDPSLLFPIPRSLNRDELGLDADALPFVGVDIWTAYELSWLNPKGKPQVAI
AEFRVPADSPNLIESKSFKLYLNSFNQTRFASAEEVQATLQKDLSAAAGGPVKVTLFPLDDFAGQPIGEL
PGECIDDLDIEIDDYQPNPALLLAAAEEEEVEETLLSLLLKSNCLVTTQPDWGSVQIYYYGPIIDRELLL
LYLVSFRQHNEFHEQCVERIFIDLMRRCQPLKLTVYARYRRRGGLDINPRRSNSEPAPPPNRRRRRQ
>gnl|CDD|442149 COG2905, COG2905, Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms]
VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEV
MTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSEEL
>gnl|CDD|442150 COG2906, Bfd, Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism]
MYVCLCNGVTDRQIRAAIAEGATSLEELRAALGAGTQCGSCVPEARELLAEALA
>gnl|CDD|442151 COG2907, Ppro0129, Predicted flavin-containing amine oxidase [General function prediction only]
MARMRIAVIGSGISGLTAAWLLSRRHDVTLFEANDRLGGHTHTVDVDLDGRTVPVDTGFIVFNERTYPNL
TALFAELGVPTQPSDMSFSVSLDGGGLEYAGSNLNGLFAQRRNLLRPRFWRMLRDILRFNREAPALLEAG
SDDDLTLGEFLDRNGYSEAFRDHYLLPMGAAIWSCPPDDMLDFPARFFVRFFHNHGLLSVTDRPQWRTVK
GGSREYVRRLTAGLKDRIRLNTPVRSVRRDADGVEVRTADGEEERFDHVVFATHSDQALALLADPTPAER
ELLGAIRYQPNEAVLHTDTSLMPRRRRAWASWNYLLDREDGTRPVSVTYWMNRLQGLPAPTPVFVTLNPT
RPIDPEKVLARFTYEHPVFDLAAIAAQKRLPELQGRNRTWFCGAYWGYGFHEDGLRSALRVAEALGARLP
WAV
>gnl|CDD|442152 COG2908, LpxH, UDP-2,3-diacylglucosamine pyrophosphatase LpxH [Cell wall/membrane/envelope biogenesis]
MRTLFISDLHLGTPGPQAITAALLDFLRSIAHDADALYLLGDIFDFWIGDDDVWPPGHNRVLQKLLELAD
KGTPVYYIPGNHDFLLGDYFAKELGATLLPDPIHLTLDGKRFLLLHGDGLDTGDKGYQLLRKLVRNPWLQ
WLFLGLPLWSRLALAAKLRRKSKAANQDKAVKIIDVFEQAVAELARERGVDGVIHGHTHRPAIHELDGGV
RYINLGDWVESGTALVEDGDGLELLRWP
>gnl|CDD|442153 COG2909, MalT, ATP-, maltotriose- and DNA-dependent transcriptional regulator MalT [Transcription]
ALVLDDYHLIDDIHLAFLLRHLPPNLHLVLASRTDPLARLRARLELRADDLRREEAAALLRRRLLPLSEE
DAARLAERTEGWARLALDPEEALALLERLLALAEAAGRLLLRALALRALGDREEALAALRRRLLAEGLSN
KEIAERLFISVNTVKTHLRNIYRKLGVRSRTEAVARARELGLLA
>gnl|CDD|442154 COG2910, YwnB, Putative NADH-flavin reductase [General function prediction only]
KIAVIGATGRVGSLIVREALARGHEVTALVRNPEKLPDEHPGLTVVVGDVLDPAAVAEALAGADAVVSAL
GAGGGNPTTVLSDGARALIDAMKAAGVKRLIVVGGAGSLDVAPGLGLDTPGFPAALKPAAAAKAAAEELL
RASDLDWTIVRPAALTDGERTGRYRLGGDGLLVDASSISRADVAVALLDELEDPAHIRQRFTVAY
>gnl|CDD|442155 COG2911, TamB, Autotransporter translocation and assembly protein TamB [Intracellular trafficking, secretion, and vesicular transport]
GLSGGGLTLRDDGVDLEADRLRLDWSPLALLRGRLCIDELALSASLDGDRLRLDNLDLDAPEGALSGLLD
LVQATLDAEGLDLASSALDDLDLRSGGNRLTLSGNLSAASLDGDLDLDAPDLADLAALLPGLAGSLSGDG
LDSLSLDADGTLAQHRLDLDAKGEPASLSLALSGGLDRDDGGTLSRLDFLNTGRWGLAAPATLSYDDGRV
TLGPLCLAGGGSLCLSGTLGGTLDLQLRLKNLPLALLNPFLPDDLGLSGTLNGDADLSGGLANPQGDASL
SLSGDLTLNDGLGGLPLGLGDLTLNARLANGRLTLDLTLDGGGLGTLSLSGSVPLADGLPPSAPLDGNLR
LDNLDLALLNPLLPGVLERLSGQLNGDLRLSGTLAAPQLNGQLTLDDGRLKLPALGVRLTDINLRLRFDG
DRLTLDGLTADSGGGTLTLSGTVDLDGLSWPADLTLKGDNLRVLNPPDYTATVSGDLTLTGTPDGPTLSG
NVTVPRARITLPELPPSAVSLSDDVVVVNRPPEPVPEEEAAGLPLDLDLNVNLGDDVRVRGFGLDARLGG
DLRLTGTPGGAPRLTGEINLVRGRYNAYGQRLTIERGSITFNGPPLDPYLDIEAVRTVDDVTAGVRVTGT
ASNPKITLFSDPALPQDEILSLLLFGRGLDSLSGGDAAQLASAAASLLGGGGGGLLGQLGSALGLDDLSI
DTGGSGDGTSVTVGKYLTDRLYVSYGVGLFDGLSEVTLRYRLTRRLSLEAQSGTGNGVDLLYRFEF
>gnl|CDD|442156 COG2912, SirB1, Regulator of sirC expression, contains transglutaminase-like and TPR domains [Signal transduction mechanisms]
MKSIALFDEQIDLAEAALLIAQDEYPDLDIEQYLAQLDALAAELRERLPAEADPLERLEALNQLLYGELG
FAGNDEDYYDPDNSYLNKVLDRRRGIPISLGILYLELARRLGLPLYGVNFPGHFLLRVDLPDGPVFIDPF
NGEILSEEELEELLKGLLGPPAELEPEFLAPASNREILARMLRNLKAAYLREKDWERALRVVERLLLLDP
DDPYEIRDRGLLYAQLGCYQAALEDLEYFLEQCPEDPDAELIKEQLEELRRKLH
>gnl|CDD|442157 COG2913, BamE, Outer membrane protein assembly factor BamE, lipoprotein component of the BamABCDE complex [Cell wall/membrane/envelope biogenesis]
MRKLRLLLLALLLALLLAGCSSFVYKIDIQQGNVVTQEDLAQLKPGMTKEQVRYLLGTPSLTDTFHPNRW
YYVYSFRRGGKEVEQRVLAVYFDDDGRVARIEGDGKTPTSAELLEQLLGNGRVNPADE
>gnl|CDD|442158 COG2914, PasI, Putative antitoxin component PasI (RatB) of the RatAB toxin-antitoxin module, ubiquitin-RnfH superfamily [Defense mechanisms]
MMEMIRVEVAYALPDKQVLLRLEVPEGTTVEQAIEASGILERFPEIDLAKNKVGIFGKLVKLDTVLRDGD
RVEIYRPLIADPKEARRRRAAK
>gnl|CDD|442159 COG2915, HflD, Regulator of phage lambda lysogenization HflD, binds to CII and stimulates its degradation [Mobilome: prophages, transposons, Signal transduction mechanisms]
KNYQDQTLALAGIFQAAALVQQLARTGQCDEEALEASLNSLLNTDPDSTEDVYGGLANLRLGLRTLLAQL
GGNRGGRDAELTRYALSLLHLERKLAKNPDMLSQLGERIEQAERQAEHFGLLHENVIANLADIYSDTISP
LGPRIQVTGEPEYLQQPDNAAKIRALLLAGIRAAVLWRQVGGSRWQLLFSRKKLLQAAKQLLARLT
>gnl|CDD|442160 COG2916, Hns, DNA-binding protein H-NS [Transcription]
MSEDLRELSLEELEELIEKLEKVIEELEKRERAEALAEIKELAAEYGISLEELLGALAAKKAKKKRAKVP
AKYRDPNGPGKTWTGRGRKPKWIKAALAAGKSLEDFLIK
>gnl|CDD|442161 COG2917, YciB, Intracellular septation protein A [Cell cycle control, cell division, chromosome partitioning]
MKLLLDFGPLILFFVAYKLYGIYVATAVLIVATLLQLAILWIRTRKVEKMQLITLVLVVVFGGLTLLLHD
ETFIKWKPTIIYWLFALVLLGSLLFGKPLLKRMLGKALQLPDEGWRRLNLAWALFFLFLAVLNEYVARTF
STDTWVNFKLFGLMGLTLLFTLAQGPYLSRHLPEEEEEEEE
>gnl|CDD|442162 COG2918, GshA, Gamma-glutamylcysteine synthetase [Coenzyme transport and metabolism]
MSPDLSRRLAWLAAPAHPSLLKGILRGIERETLRVTPDGRLAQTPHPAALGSALTHPWITTDYSEALLEF
ITPVFDDIDELLAFLRDIHRFVYRHLGDELLWPLSMPCFLPGEEDIPIAQYGSSNIGRMKTVYRRGLKNR
YGRLMQTIAGVHYNFSLPEAFWQALQGLEGDSESLQDFISAGYFGLIRNFRRFGWLIPYLFGASPAVCKS
FLKGREHPLEEFDKGTLYLPYATSLRMSDLGYQNKAQSGLKICYNSLDSYVDSLRRAIRTPSPEYEKIGV
KVDGEYRQLNTNILQIENEYYSPIRPKRVTRSGEKPSQALLRRGVEYIEVRSLDINPFSPIGIDEEQIRF
LDLFLLWCLLADSPPISAEELAEIDDNFNRVVLEGRKPGLTLQRGGEEIPLQDWGKELLDDLQPVAELLD
AAHGGGAYQAALAAQRAKLDDPELTPSARILAEMRENGEGFGEFGLRLAKQHREYLRAEPLSAETEAEFE
AEAEESLAEQAEIEAADTLSFDEFLARY
>gnl|CDD|442163 COG2919, FtsB, Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning]
RMRLLRTLVLLLLLAYLQYHLWFGDGGLLAYRELRQEIAELEAENAKLKARNAELEAEVADLKDGPDYIE
ERAREELGMVKPGETFYRVPDPEKAA
>gnl|CDD|442164 COG2920, TusE, Sulfur transfer complex TusBCD TusE component, DsrC family (tRNA 2-thiouridine synthesizing protein C) [Translation, ribosomal structure and biogenesis]
TLEVNGKTIETDEEGFLLDPEDWSEEVAEALAREEGIELTDEHWEVIRFLREYYAEYGISPAIRELVKAL
GKKFGPKGNSKYLYELFPGGPAKQACKIAGLPKPTGCV
>gnl|CDD|442165 COG2921, YbeD, Putative lipoate-binding regulatory protein, UPF0250 family [Signal transduction mechanisms]
STKEEPLIEFPCDFPIKVMGLADDDFVDAVVEVVQRHAPDFDPETISVRPSSKGKYLSVTVTITATSREQ
LDALYRALTAHPLVKMVL
>gnl|CDD|442166 COG2922, Smg, Uncharacterized conserved protein Smg, DUF494 family [Function unknown]
MFDVLVYLFENYIDPDVEACPDQDELARELSAAGFEDDEIDKALDWLEGLAELQESPAPAAASSGSIRIY
TDEEQERLDTECRGFLLFLEQAGVLDPETRELVIDRAMALDDEEISLDDLKWVVLMVLWNQGQELAYLIM
EELLFDDDEGTLH
>gnl|CDD|442167 COG2923, DsrF, Sulfur transfer complex TusBCD TusC component, DsrF family [Translation, ribosomal structure and biogenesis]
MKKLLFVFRQAPHGSAAAREGLDAALAAAAFDQDVSVLFIDDGVYQLLKGQQPEAIGQKNYIATFKALPL
YDIEKVYVCAESLEERGLSEDDLVLDVEVLSRAELRELLAEADVVLTF
>gnl|CDD|442168 COG2924, YggX, Fe-S cluster biosynthesis and repair protein YggX [Inorganic ion transport and metabolism, Posttranslational modification, protein turnover, chaperones]
MSRTVFCVKLGKEAEGLDFPPYPGELGQRIFENVSKEAWQEWLKHQTMLINEYRLNLMDPEARKFLEEQM
EKFLFGEGADKPEGYVPPSA
>gnl|CDD|442169 COG2925, SbcB, Exonuclease I (degrades ssDNA) [Replication, recombination and repair]
QPTFLWHDYETFGADPRRDRPAQFAGIRTDADLNIIGEPLVLYCKPADDYLPHPEACLITGITPQLALEK
GLPEAEFAARIHAEFSQPGTCGVGYNSIRFDDEVTRYLFYRNFYDPYAREWQNGNSRWDLLDVVRACYAL
RPEGIEWPENEDGRPSFKLEHLTAANGIEHENAHDALSDVYATIALAKLIKQKQPKLFDYLFSLRDKRKV
AALIDLPAMKPLLHVSGMFPAERGCTALVVPLAWHPTNKNAVIVCDLAGDPSPLLDLDAEELRERLFTRR
ADLPEGVERLPLKLVHINKCPVLAPAKTLRPEDAERLGIDRDQCLRHLALLRAHPDLREKVRAVFAREPF
APSDDVDLQLYGGFFSDADRRLMEIIRALSPEQLAALNPAFEDPRLPELLFRYRARNFPETLSEEEQQRW
QAHRRARLTDGAGGALTLEEFFEELEELAEEHQDDPRKQALLKALYDYAEQLAP
>gnl|CDD|442170 COG2926, YeeX, Uncharacterized conserved protein YeeX, DUF496 family [Function unknown]
FQNVLEFVRMFRRKNKLKREIADNEKKIRDNQKRVLLLDNLSEYIKPGMSIEEIQAIIANMRSDYEDRVD
DYIIKNAELSKERREISKKLKDIKKAKIEK
>gnl|CDD|442171 COG2927, HolC, DNA polymerase III, chi subunit [Replication, recombination and repair]
MTRVDFYHLTRVSDREALACRLAEKALRAGWRVLVLCPDEEQAEALDELLWTFRPDSFLPHGLAGEGLAA
DQPVLLTTDEENPNGADVLINLDGAVPDFFSRFERVIEIVDGDEEAKQAARERWKAYRAAGYELTY
>gnl|CDD|442172 COG2928, COG2928, Uncharacterized membrane protein [Function unknown]
RLMKRLRRYFLTGLLVLLPLAITLYVLWWLFGWLDGLLGPLLKLLLPELGFYIPGLGLVVLLLLILLIGL
LARNFLGRRLLRLGERLLNRIPLVRSIYNAVKQIVETLLSDSGDSFRKVVLVEYPRKGIWTIGFVTGETP
GEVAAKLGEDMVAVFVPTTPNPTSGFLLIVPREDVIELDMSVEEALKFIISAGVVSPESKPAKAALAA
>gnl|CDD|442173 COG2929, COG2929, Uncharacterized conserved protein, DUF497 family [Function unknown]
MEFEWDEAKAAANLAKHGVSFEEAEEVFFDPPLLVVEDPRHSYGEDRFIAIGLIDGGRLLVVVFTERGDA
IRIISARKANRKERKRYEQRLR
>gnl|CDD|442174 COG2930, SYLF, Lipid-binding SYLF domain, Ysc84/FYVE family [Lipid transport and metabolism]
MKRRKLLLLALLLLALAAAAAASAAAAAKAAEIDARADATLQELYPDVPGPRELLEKAKGVLVFPNVIKA
GFIVGGAYGEGVLLVRGPSTPAYYSLAGGSVGLQIGAQSYDLVLVFMTDEALDKFRKSGWTLGADASVAA
GPVGAGASADTTATLKAPVYAYSRSKAGLFAGASLEGSKITRDDDANR
>gnl|CDD|442175 COG2931, COG2931, Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism]
GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGG
GGGGGGDGGGGGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGND
TLTGGAGNDTLYGGAGNDTLYGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGG
DDGLDGGDGDDGLGGGGGDDTLGGGGGGDGGGGGGGDDGLGG
>gnl|CDD|442176 COG2932, COG2932, Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: prophages, transposons]
VPLYDGEASAGGGAFNEVEEPVDKLEFPGLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTEIRDGGIY
VVRTDGELLVKRLQRRPDGKLRLISDNPAYPPIEIPPEDADEIEIIGRVVW
>gnl|CDD|442177 COG2933, RlmM, 23S rRNA C2498 (ribose-2'-O)-methylase RlmM [Translation, ribosomal structure and biogenesis]. 23S rRNA C2498 (ribose-2'-O)-methylase RlmM is part of the Pathway/BioSystem: 23S rRNA modification
MNRLLLYCRPGFEKECAAEITDKAAELGVFGYARAKPNSGYVLFECYQPEDAEELARELPFRELIFARQW
FVVLAELEDLPPEDRITPILEALRELLPRFGELWVETPDTNEGKELSKFCRKFTVPLRAALRKAGLLLAK
ENAGAPRLHLFFLDGDTAYVGYSYPGNSSPWPMGIPRLRFPADAPSRSTLKLEEAFHVFLPRDEWEERLR
PGMRAVDLGAAPGGWTWQLVRRGMFVTAVDNGPMAPSLMDTGQVEHLREDGFKYRPPKPVDWLVCDMVEK
PARVARLMADWLVNGWCREAIFNLKLPMKKRYEEVRECLERLRERLAEAGIPYELRAKQLYHDREEVTVH
LRRRPK
>gnl|CDD|442178 COG2935, Ate1, Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein turnover, chaperones]
MTHPPLRSLQFYLTAPHPCSYLPGRQARKLFTDPSGPLAAELYDALLRAGFRRSGNILYRPHCPGCRACV
SVRIPVADFRPSRSQRRVLKRNADLTVRVLPPEFTEEHYALYRRYLAARHADGGMDPMSREQYAAFLEDS
WVDTRLVEFRLDGRLVAVALTDVLPDGLSAVYTFFDPDLARRSLGTYAILWQIELARRLGLPYLYLGYWI
EGSRKMAYKARFRPLERLIGGGWQRLDPPE
>gnl|CDD|442179 COG2936, COG2936, Predicted acyl esterase [General function prediction only]
MKRAAPADVYVKEDVWIPMRDGVRLAADIYRPKDAEGPVPVILERTPYGKRDGTAGRDLGPHPYFAERGY
AVVVQDVRGTGGSEGEFDPYRVDEQTDGYDTIDWLAKQPWSNGKVGMIGISYGGFTQLAAAADRPPALKA
IVPQAPTSDRYDDDHYHGGAFLLGFNLGWAATMGAYKERPPDPADARWRELLPDDYADRLEHLPLSDADA
LGEQLPFWEDWLAHPDYDAFWQERSLLEDLDRIKVPVLAVGGWYDVFLNGTLRLYEALRAPAGVPRKLVI
GPWTHGPWARGQLGPLFGATAIDFLQEALRWFDHWLKGIDNGIEDEPPVRVYVMGAGRWRTEDDWPPPGA
RPTRLYLGPGGGLSTEAPAAAAGPDTYVYDPADPVPTTGGELLGPEGPADQRFAEARPDVLVFTTAPLTE
DLEIAGPPTARLFVSSDAPDADFVVRLIDVAPDGRSTNVTDGILRLRYRDSFEKPEPLVPGEVYEVTIEL
WPTAHVFKAGHRIRVQVSSSNFPRYDRNPNTGVPIYTATDFVKATQTVHHGPAHPSRLELPVVPG
>gnl|CDD|442180 COG2937, PlsB, Glycerol-3-phosphate O-acyltransferase [Lipid transport and metabolism]. Glycerol-3-phosphate O-acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis
MLLRLPLKLLVKSKVIPEDTAELELDPSKPVVYVLPYRSLSDLLVLRRQCRKLGLPDPIQLVPVSVLWTF
VRFGEPVSLRELLDEGGSDERLARKLARVLRVHFRRQRRAVIGPDLKHRRDLIERLLRSPAVRKAIEEEA
KSKGISEEKARKEARRYLREIAADFSYSAIRFLDRVLRWLWNRLYDGIRVDNLERLRELAKGHEIVYVPC
HRSHMDYLLLSYVLYHNGLVPPHIAAGINLNFWPLGPILRRGGAFFIRRSFKGNKLYSAVFREYLAELFE
RGYSVEYFIEGGRSRTGRLLPPKTGMLSMTVQAFLRGARRPVVFVPVYIGYERVLEVGSYAKELRGGEKK
KESLGGLLRALRKLRRRFGRVYVNFGEPISLSEYLDQHVPDWRESEDLRPEWLRPAVDKLAFEIMVRINR
AAAVNPVNLVALALLASPKRALTEAELLAQLDLYLDLLRNVPYSLSVTLPELTPEELLEHLLSLGLIEVE
KDGLGDVISIDDEQAVLLTYYRNNILHLFALPALIASALLANRRISRAELLELVRLLYPLLKAELFLRWD
AEFEEVLDEELDELVRQGLLEREGDTLRRPPARFRQLQLLAHVLRETLERYAIVLSLLAKLGSGTLDRKE
LEKESLLLAQRLSLLHGINAPEFFDKALFRNFIQTLREQGYLDDDEDGKDEKLEELADDARELLSPELRQ
TIQRIAR
>gnl|CDD|442181 COG2938, SdhE, Succinate dehydrogenase flavin-adding protein, antitoxin component of the CptAB toxin-antitoxin module [Posttranslational modification, protein turnover, chaperones]
MLDEARRKRLRWRCRRGMLELDLLLGRFADAHLDTLSDAELDAFERLLELEDPDLFDWLMGRKPPPDEEL
AALVARIRAFHQAR
>gnl|CDD|442182 COG2939, Kex1, Carboxypeptidase C (cathepsin A) [Amino acid transport and metabolism]
MKKRRALLLAALLALAALAAAAAAQAAADKAAGPAPALPADADVVTEHSVTIGGKTIAYTATAGTLPLRD
EDGKPIASVFYTAYTRDGADAATRPVTFAFNGGPGSASVWLHLGALGPKRVKFDDDGDAPPPPYGLVDNP
YSLLDVTDLVFIDPVGTGYSRALGGDKPKDFWGVDADIEALAEFIRTWLTRNNRWNSPKYLIGESYGTTR
AAGLARALQERHGVYLNGVILVSPALDFGTLRFAPGNDLPYALYLPSYAATAWYHGKLPPQGKDLEAFLA
EAEAFALGEYLPALAKGDRLSPAERAAIAAKLARLTGLSEDYVLRANLRIDTGRFRKELLRDEGLTVGRL
DSRYTGPDPDPAGERPDYDPSLDAILGAYTAAFNDYLRNELGYKTDLPYELLSYDVVRPWDWGHGERGYP
NVAEDLRQAMAQNPYLRVLVASGYYDLATPYFAAEYTLDHLPLPGELRDRISFKYYPGGHMMYLREPSLA
ALNDDLRAFIRAALPA
>gnl|CDD|442183 COG2940, SET, SET domain-containing protein (function unknown) [General function prediction only]
MAMLHPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHTYLFELDDDGVIDG
ALGGNPARFINHSCDPNCEADEEDGRIFIVALRDIAAGEELTYDYGLDYDEEEYPCRCPNCRGT
>gnl|CDD|442184 COG2941, Coq7, Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) [Coenzyme transport and metabolism]. Demethoxyubiquinone hydroxylase, CLK1/Coq7/Cat5 family (ubiquinone biosynthesis) is part of the Pathway/BioSystem: Ubiquinone biosynthesis
LSFLDRLIIEFDRALRTLFGPARASRPRPAAGVPEAELSAAERRHAAGLMRVNHAGEVCAQALYQGQALT
ARDPEVRAALEEAAAEETDHLAWCEERLRELGSRPSLLNPLWYAGSFALGALAGLLGDKWSLGFVAATER
QVEAHLDSHLARLPAQDPKSRAILEQMREDEAEHADIALEAGAAELPAPLRGAMKAGSKVMTWTAYRI
>gnl|CDD|442185 COG2942, YihS, Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate transport and metabolism]
ADWLRAELLDDLLPFWLPRSIDPEGGGFFGCLDDDGTPYDDADKGLVLQARQVWTFALAYLLLGRPEYLE
LAEHGLDFLREHFRDPEHGGWYWSLDADGKPLDDRKQAYGHAFALLALAEAYRATGDPEALELAKETFEL
LERRFWDPEHGGYAEAFDRDWSPLRPYRGQNAHMHLLEALLALYEATGDERWLERAEEIADLILTRFADP
EGGRLLEHFDPDWSPDPDYNRPRGVSPGHDIEWAWLLLELAALLGDAWLLELARKLFDAALEYGWDDERG
GLYYELDPDGKPVDDDKLWWVQAEALVAALLLYQLTGDERYLDWYRRLWDYIWAHFIDHEYGEWFGELDR
DGEPLTDLKGGPWKGDYHNPRALLEVLRRL
>gnl|CDD|442186 COG2943, MdoH, Membrane glycosyltransferase [Cell wall/membrane/envelope biogenesis, Carbohydrate transport and metabolism]
RPARTWPRAAALRRLLVFGLALATTALATWLMAGVLSAGGLTVLEWVLLALFALLFAWIALGFWTALIGF
LLLLRGRDPYSLSAPFAARPPPPLTARTAILMPVYNEDPARVFAGLRAMYESLAATGQLDHFDFFILSDT
TDPDIWAAEEAAWAALRARLGGGGRIFYRRRRRNTGRKAGNIADFCRRWGGAYDYMLVLDADSLMSGETI
VRLVRRMEANPRAGLIQTLPVLVGRETLFARLQQFAARVYGPLFAAGLAWWQGGEGNYWGHNAIIRVRAF
AEHCGLPVLPGRGPFGGHILSHDFVEAALMRRAGWEVWLAPDLGGSYEESPPTLIDFAKRDRRWCQGNLQ
HLRLLGAPGLHPVSRFHFLTGIMSYLSSPLWLLFLLLGTALALQAALIRPEYFPEPFQLFPVWPVFDPER
ALALFVLTMALLFLPKLLGLLLALLRGEARRAFGGALRLLLSVLLETLFSALLAPIMMLFHTRFVIGILL
GRDVGWKAQRRDDGALPWREALRRHWPHTLLGLALGAAAYWLSPSLLLWLLPVLLGLVLAIPLSVLTSSP
SLGRALRRAGLFLIPEETAPPPVLRRARELLAEPAAAAADGFAQAVADPALNALHCALLPPRAPAARAEL
VEQALEALSAAEKLALLSDPELLARLARLWS
>gnl|CDD|442187 COG2944, YiaG, DNA-binding transcriptional regulator YiaG, XRE-type HTH domain [Transcription]
MTKKPLTPEEIRALRERLGLSQAEFAALLGVSVSTVRRWEQGRRKPSGAALKLLRLLEKHPELL
>gnl|CDD|442188 COG2945, COG2945, Alpha/beta superfamily hydrolase [General function prediction only]
KVLINGPAGRLEGRLDLPEGPPRGVALILHPHPLFGGTMDNKVVYTLARALVAAGFAVLRFNFRGVGRSE
GEFDEGRGELDDAAAALDWLRAQNPLPLWLAGFSFGAYVALQLAMRLPEVEGLILVAPPVNRYDFSFLAP
CPAPTLVIHGEQDEVVPPAEVLDWARPLSPPLPVVVVPGADHFFHGKLDELKELVARYLPR
>gnl|CDD|442189 COG2946, NicK, DNA relaxase NicK [Replication, recombination and repair]
MKRDGSSNSVLIDYLRFTFKETDDLEEILEEILGLKDYFSHERKGFYGYEESYSLGDIVGFVGFGEGQNG
TVLVELSGTGCRQAEEYLEAGWYDRLFDWLQDPGGKITRIDLAIDDFDGELSIEQAVSKYKKGLFISRGR
RPKYELVGTDWENGKGKGRTLYIGSRESGKYWRIYEKGKELGDKESSWVRFELRLKNEKAVIPVDILLNP
GEYLAGAYNIYARFVDAEPEDSNEKIPLTVKPAKISLERTLRWLRRQVGPTLNMLKEIDGLDAEEIVEDL
VRDGKKLPKRLEKIIEQQVTDA
>gnl|CDD|442190 COG2947, EVE, Predicted RNA-binding protein, contains EVE domain [General function prediction only]
AYWLMKSEPDVYSIDDLVADGTTPWDGVRNYQARNFLRAMKVGDLVFFYHSNKEPGIVGIAEVVREAYPD
PTQFDTPRWVMVDVKFVRKLPRPVTLAELKADPALADMALVRQSRLSVMPVTEEEWEIILALGGL
>gnl|CDD|442191 COG2948, VirB10, Type IV secretory pathway, VirB10 component [Intracellular trafficking, secretion, and vesicular transport]
PKPEDLRLRAEPPRVTRLSRKVLIGLAGVAVLLLGGALIYLSTRGAQRRLQELEAARRSPLFVQGGGGAA
AAQAAAAGAAGPAGAAGAAGGSADPNGQDRKNAFLNQLQDTRTVSARATRLPDSPYLLPAGTVIPAVLET
GINSDLPGQITAQVTEDVYSATGRVLLIPQGSRLIGEYDSGVSFGQSRVLVVWTRLITPDGVSIDLDSMP
GTDALGRAGLEGQVDNHWWERFGAALLLSLLGDGAELAASSDEGDLSTAIRENTAQSLSQAAQQILERNL
NIPPTLTIRQGTRVRVIVARDLDFSSPYR
>gnl|CDD|442192 COG2949, SanA, Uncharacterized periplasmic protein SanA, affects membrane permeability for vancomycin [Cell wall/membrane/envelope biogenesis]
MKKRLRRLLKILLALLLLALLLLLAINVWVSLSTAGRIYTDVEELPARPVALVLGASVYPDGTPNPYLAD
RLDAAAELYKAGKVKYLLVSGDNSTKSYNEPRAMRRYLIKRGVPAEDIVLDYAGFRTYDSCVRARKVFGV
DRATIVTQRFHLPRALFIARALGIDAIGVAADDVSYRSGLKVRLREVLARVKAFLDLYLLRREPRFLGPP
EPIV
>gnl|CDD|442193 COG2951, MltB, Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis]
MRRLALAAALALACASAAAAAAAAAADFAAWVAAFRQEAAAAGISRATLDAALAGATPDPRVIELDRRQP
EFTKPWWDYLARFVSPARIARGRAFLRQHAALLARIEQRYGVPAEIIVAIWGVETNYGRYMGNFPVLDAL
ATLAFDGRRAEFFRGELIAALKILQRGDIDPDQMKGSWAGAMGQTQFMPSSYLRYAVDFDGDGRRDLWNS
PPDALASTANYLKKHGWQRGQPWGYEVRLPAGFDYALAGLKPRRTLAEWAALGVRPADGRPLPADGPASL
LLPAGANGPAFLVTPNFYVITRYNRSDLYALAVGHLADRIAGAFVA
>gnl|CDD|442194 COG2952, COG2952, Uncharacterized conserved protein, DUF507 domain [Function unknown]
MRLKLGHVPYIANEIVRDLLNSGDIEVEKGPEEVKKDIESVLEEYLKKERELEEKAKEILEENGEEIEFE
NVDYRQAFWRIKKKLAEERGIILNGEERLNDIAHQILEMLMHSDLIEEVVEDNVIRNKIFPILKKYLKVE
EEIDDEVREKIKNYKKKLIEGTEEWEIEYERLYEEELRKRGLL
>gnl|CDD|442195 COG2954, CYTH, CYTH domain, found in class IV adenylate cyclase and various triphosphatases [General function prediction only]
MALEIERKFLVKGDPWRALATRGTRIRQGYLSTDPERTVRVRIKGDQAFLTIKGKGSGLSREEFEYEIPL
ADAEELLELCEGPVIEKTRYLVPHGGHTWEVDEFEGENAGLVVAEVELPSEDEPFELPDWLGEEVTGDPR
YYNSNLAKHPYSQWSAE
>gnl|CDD|442196 COG2956, LapB, Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]
LLLPVAAALGWYFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLE
RDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLG
PENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPD
YLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEGLEAALALLERQLRRH
>gnl|CDD|442197 COG2957, AguA, Agmatine/peptidylarginine deiminase [Amino acid transport and metabolism]
PAEWEPQEATWLAWPHREDDWGGGLEPVRAAFAAIARAIARFEPVTILVPDEDAEEARALLGEDLANVRL
VEAPTNDAWARDTGPIFVVNDDGELAAVDWRFNGWGGKYPPWDLDNQVARKVAELLGLPLYRSDLVLEGG
SIEVDGEGTLLTTESCLLNPNRNPGLTRAEIEAELKRYLGVEKVIWLPGGLAGDDTDGHIDTLARFVAPG
TVVLVVCDDPDDPNYAVLQANLEELKAATDADGRPLEIVPLPMPGPLYEDGERLPASYANFLIANGAVLV
PTYGDPADAAALAILQELFPGREVVGIDARALIWGGGSIHCITQQQPA
>gnl|CDD|442198 COG2958, COG2958, Uncharacterized conserved protein [Function unknown]
KLTLKELILEVLEDNPKEPFTAREIAEKIVETYPYECQDKKLNSRGKTPVAEIGAQIYVDAKKNPEVKFI
KVSGRPRLYYLKKNEDELEVDAAEIEEEESKAKKKKEKKTYSERDLHPLLSYYLYNELNLYTKTIDHERS
KNSGKGGNKWLHPDIVGVYFLDKEWHNEVRDCVKLGKGNSIKLWSFEVKKEINRSNLRESFFQAVSNSSW
ANEGYLVAAEISDDDTLKELRRLSASFGIGVIKLDTENPDESQILIPAKEREEIDWDTINRLVEENPDFK
KFIELVKIYYQTGKVRKKDWD
>gnl|CDD|442199 COG2959, HemX, Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis HemX, COG0755, no evidence of involvement in heme biosynthesis) [General function prediction only]
MTENNPVETAAESASAPAASTASAPAPPALWLALLALLLALAAGGGGYYLGWQQLQQQQAELAQLAQQLA
ALQQQAQELRALAQQLQELLQQLAARLAQLEQRLAELQQQLAALQQLLQSLSGSSRDDWLLAEAEYLLRL
AGQQLQLEGDVKTALAALQSADARLARLNDPSLLPVRRAIARDIARLRAVPQVDIDGIALRLDALANQVD
NLPLASDVAPAAAPAAAAAEASASISDWQQNLWEKSWDELRDLVRIRRRDQPVAPLLSPEQAFFLRENLR
LRLLNARLALLRRQEELYQQSLAAAQTWLRRYFDTDSPATQAFLAELDQLQAQSISVELPDILESLAALR
KLLAQRVRALL
>gnl|CDD|442200 COG2960, UbiK, Ubiquinone biosynthesis accessory factor UbiK [Coenzyme transport and metabolism]
MQDPKFFDDLAKLLSDALPAAQGPRREVEKNVRAQLQSALSKLDLVTREEFDVQRAVLARTREKLEALEA
RLAELEAKLAAAA
>gnl|CDD|442201 COG2961, RlmJ, 23S rRNA A2030 N6-methylase RlmJ [Translation, ribosomal structure and biogenesis]. 23S rRNA A2030 N6-methylase RlmJ is part of the Pathway/BioSystem: 23S rRNA modification
MLSYRHAFHAGNFADVLKHAVLVLLLDYLKRKDKPFRYIDTHAGAGLYDLDSEEAQKTGEYRDGIGRLWQ
AADLPPLLADYLDLVRALNPDGGLRYYPGSPLIARALLRPQDRLRLFELHPTDAALLRANFAGDRRVRVH
HRDGFEGLKALLPPPERRGLVLIDPPYEVKDEYQRVVDALAEALKRFATGTYAIWYPIKDRAEVDRLLRA
LKALGIRKILRAELTVRPDDDGLGLTGSGMLVINPPWTLDEELRELLPWLAELLAQDGGASFRLEWLV
>gnl|CDD|442202 COG2962, RarD, Membrane protein RarD, contains two EamA domains, drug/metabolite transporter family [General function prediction only]
MMSEMRKGVLAALLAYLLWGLLPLYFKLLAPVPALEILAHRILWSLPFLLLLLLLTRRWGELRRLLRDPR
LLLLLLLAALLIAVNWLLFIWAVNNGHVLEASLGYFINPLVSVLLGVLFLKERLRRLQWLAVGLAAAGVL
VLTVGYGSLPWIALVLALSFGLYGLLRKKLPVDALTGLTLETLLLLPLALAYLLWLAATGTGAFGSAGPG
LTLLLLLAGVVTAVPLLLFAAAARRLPLSTLGLLQYIAPTLQFLLAVFVFGEPFTPARLITFGLIWLALA
LFSLDGLRRRRRARRAA
>gnl|CDD|442203 COG2963, InsE, Transposase InsE and inactivated derivatives [Mobilome: prophages, transposons]
MSKKRRRYSPEFKAEAVRLVLEGGASVAEVARELGISPSTLYRWVRQYREGGLGGFPGDGRTTPEQAEIR
RLRKELRRLEMENDILKKAAALL
>gnl|CDD|442204 COG2964, YheO, Predicted transcriptional regulator YheO, contains PAS and DNA-binding HTH domains [Transcription]
MSKEDKELLESYIPIADGLAALFGPNCEVVLHDLEDPEHSIVAIANGHVSGRKVGDPITDLGLELLKDGA
YEDPDVIGNYETRTKDGRLLKSSTIFIRDEKGKPIGALCINFDLSKFEAAQNFLDSFLPTDDSEEEPPEN
FASDVEELIDEIIDEALAEVGKPPSALSKEEKIEIVRELDEKGIFLIKGAVDYVAKRLGISRATVYNYLR
EIKK
>gnl|CDD|442205 COG2965, PriB, Primosomal replication protein N [Replication, recombination and repair]
MMNRLVLSGTVVERPALRYTPAGIPVLEFVLEHRSEQQEAGLPRQVECEIPAVASGELAEKLARLPLGSQ
VRVTGFLARKSRGSRQLVLHIQQIELID
>gnl|CDD|442206 COG2966, YjjP, Uncharacterized membrane protein YjjP, DUF1212 family [Function unknown]
MSEDEAELREVLDLALRAGELLLESGAETYRVEDTMLRIAAALGLDEVEVFVTPTSITVSLEDGDEPITR
VRRVRPRGINLEKLAEVNRLSRDLVAGELDLEEARRRLDEIKRAPPRYPRWLVVLAAGLAAAAFALLFGG
GWLDFLVAFLAGALGGLLRRLLARRGLNPFFVEALAAFVATLIALLLARLGLGLNPDLIIIGSILPLVPG
VPLTNAVRDLIAGDLVSGLARLAEALLIALAIAFGVALALSLLGLLGLPPLPPPPLLPLPPWLLLLLAAA
AAAAAFAVLFAARRRLLLLAAALAAAAAAARLLLLLLGGGGSAAAAAAAAVAVGGLLAARRRRRPPPVVL
VPAAVLVVPPGGGLYLRLLLLLGGGGAGAAAALLLAAAAAALLAGLLGAALAVLLRRLL
>gnl|CDD|442207 COG2967, ApaG, Uncharacterized conserved protein ApaG affecting Mg2+/Co2+ transport [Inorganic ion transport and metabolism]
YGIKVSVETEYLPEQSDPEEGRYVFAYTITIENLGDVTVQLLSRHWIITDANGKVQEVEGEGVVGEQPVL
APGESFEYTSGCVLETPVGTMQGSYQMVDEDGERFDVPIPPFSLAAPRA
>gnl|CDD|442208 COG2968, YggE, Uncharacterized conserved protein YggE, contains kinase-interacting SIMPL domain [Function unknown]
MKKKLLALALALALLAGAPAQAEAPDEPTITVSGEGEVEVAPDIATVSLGVETEGKTAAEALAENAERMA
AVIAALKAAGIAEEDIQTSNLSVQPEYDYDKDGKPKLTGYRASNTVTVTVRDLDKLGEVLDAAVAAGANR
INGVSFGLSDPEALRDEARKAAVADARAKAEALAKALGVKLGRVLSISEGGSGGRPVPMMRAAMAMAAAA
AASTPIEPGEITVSASVTVVFELE
>gnl|CDD|442209 COG2969, SspB, Stringent starvation protein B, binds SsrA peptide [Posttranslational modification, protein turnover, chaperones]
MQMTSTRPYLIRALYEWIVDNGLTPYLLVDADYPGVQVPREYVKDGQIVLNISPSAVGNLQLGNDAISFS
ARFGGVPRDIYVPVAAVLAIYARENGQGMAFEPEEYYEEEADEAPPDDDPEPPEPPPKKGRPSLRVVK
>gnl|CDD|442210 COG2971, BadF, BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism]
PYILGVDGGGTKTRAVLVDADGEVLGRGRAGGANPQSVGLEEALASLREALEEALAAAGDPADIEAVGFG
LAGAGTPEDAEALEAALRELFPFARVVVVNDALAALAGALGGEDGIVVIAGTGSIAAGRDGDGRTARVGG
WGYLLGDEGSGAWLGREALRAALRALDGRGPPTALTEAVLAEFGLDDPEELIAWVYRGPAPPADLASLAP
LVFEAAEAGDPVARAILEEAADELAELARALLERGALPVVLAGGVAAAQPLLREALRARLAAGGAEIVPP
AGDPVDGALLLALRLLGA
>gnl|CDD|442211 COG2972, YesM, Sensor histidine kinase YesM [Signal transduction mechanisms]
LSKSLSLLSIVLLLLILLLLVLLILLLSLLLIILLLLLLLILLLLLLILLLLLLLLLLLLLLLLLLLLLL
LLLLLLLALLLILLLLLLLLLLLILLLSLLLLLALILLLALLLLLSILLLILGLLLIILLLLSLLGWTLV
SLIPKSELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDLVRLEVSGNDE
IGILARSFNEMVERIKELIEEVYELELEKKEAELKALQAQINPHFLFNTLNSIRWLAELEDPEEAEEMLE
ALSKLLRYSLSKGDELVTLEEELELIKSYLEIQKLRFGDRLEVEIEIDEELLDLLIPKLILQPLVENAIE
HGIEPKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEELSSKGEGRGIGLRNVRERLKLYYGE
EYGLEIESEPGEGTTVTIRIPLEEE
>gnl|CDD|442212 COG2973, TrpR, Trp operon repressor [Transcription]
MYSQREEEDWQQFVELLQQAFDEDDLQPLLQLLLTPDEREALGTRVRIVKELLRGEMSQREIAQELGVSI
ATITRGSNSLKTADPELKAWLEQQLLEDK
>gnl|CDD|442213 COG2974, RdgC, DNA recombination-dependent growth factor RdgC [Replication, recombination and repair]
MWFKNLQLYRLTPPWPLSAEELEEALAEHAFTPCGSQDMQSFGWVPPLGRSGEALVHSVGGQILLCLRKE
EKLLPASVVKEELEEKVAEIEAEEGRKPGRKEKKELKEEVIDELLPRAFSRSSRTYAWIDPKNGWLVVDA
ASAKKAEEVLSLLRKSLGSLPVVPLATQQSPAAAMTEWLASGEAPAGFTLGDECELKSPGEDGAVVRCKR
QDLDSDEIRAHLEAGKQVTKLALTWDDRISFVLTEDLSIKRLKFLDVLLEQADDIDGDDAAERFDADFAL
MTGELSRLLPDLIEALGGEAEP
>gnl|CDD|442214 COG2975, IscX, Fe-S-cluster formation regulator IscX/YfhJ [Posttranslational modification, protein turnover, chaperones]
MKWTDTEDIAIALYEKHPDVDPLTVRFTDLHRWVLELPGFDDDPERSNEKILEAIQMAWIEEAE
>gnl|CDD|442215 COG2976, YfgM, Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal transduction mechanisms]
MAYYLTEEEQLEAIKKWWKENGKAIIVGVVLGLAAVFGWRYWQSYQESQAEEASALYEQLLEALAAGDAA
AAAAAAEKLIDDYGGTAYAALAALLLAKAAVDAGDLDKAAAQLQWVLDNAKDPALKALARLRLARVLLAQ
KKYDEALATLDAVKPEAFAALYAELRGDILLAQGDKAEARAAYQKALAALPEDAPLRQLLQMKLDDL
>gnl|CDD|442216 COG2977, EntD, 4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites biosynthesis, transport and catabolism]
PDAFDDALFAQLGPPEPAALARAVPKRRAEFLAGRLCARRALAELGVPPAPILIGEDRAPLWPAGVVGSI
SHSDGYAAAVVAPASDVRGLGIDIEPLLDEPLAEELLPSILTPAERALLAALSPLPFAHALTLLFSAKES
LYKALYPLVGRYFGFDDAELVALDPEAGTFTLRLLQDLSPGFPAGRRFEGRFALRDGLVLTLVAL
>gnl|CDD|442217 COG2978, AbgT, p-Aminobenzoyl-glutamate transporter AbgT [Coenzyme transport and metabolism]
MSTSKKKGLFQRFLDGIERVGNKLPHPFTLFVILALIVIVLSAILSALGVSVVHPGTGETIAVVNLLSGE
GLRRILTSMVKNFTGFPPLGLVLVAMLGVGVAEKSGLISALLRKLVLKAPKKLLTPAVVFVGILSNIASD
AGYVVLIPLAAMIFYAVGRHPLAGLAAAFAGVSGGFSANLLIGGTDPLLAGITQEAAQIIDPNYTVNPLA
NYYFMIASTFVLTIVGTLVTDKIVEPRLGKYDGDEDLDEEEELEPLTAEEKKGLRWAGIAALAFIALLAL
LVLPEGSPLRNPDGSLLPSPFMKGIVPLIFLFFLIPGIVYGIAAGTIKNDKDVPKMMSKSMSTMGGYIVL
AFFAAQFIAYFNWSNLGTILAVKGAEFLKSLGLTGIPLIIGFILLTAFLNLFIGSASAKWAILAPIFVPM
LMLLGYSPELTQAAYRIGDSSTNIITPLMPYFPLILAFAQRYDKKAGIGTLISLMLPYSIAFLIVWTLLL
IVWYLLGLPLGPGAPIFY
>gnl|CDD|442218 COG2979, YebE, Uncharacterized membrane protein YebE, DUF533 family [Function unknown]
MDAKKLLDQLLGSGQGGLGGLGQAKGGAGGLLGGLGGGAAAGGLAGLLLGSKKGRKMGGSALKYGGLAAL
GGLAYKAYQNWQAGQAAQAAAPADSAFEPATRLPAAPAEQRALLLLRAMIAAAKADGHIDEAERARIEGQ
LDEAGLDAEERAWLEQELAKPLDPDALAAAARTPEQAAEVYLASLLAIDPDTFAERAYLDELARALGLDP
ALVAELEAQA
>gnl|CDD|442219 COG2980, LptE, Outer membrane lipoprotein LptE/RlpB (LPS assembly) [Cell wall/membrane/envelope biogenesis]
MMMRRLLALLLLLLAVLLLAGCGFHLRGTTQLPPEFKTLYLQSSDPYSPLTRALRRQLRANGVRLVDDPA
DADAVLRILSESRERRTLSVNANGRVAEYELTYTVRFQVRDPDGKELIPPQTVSVRRDYSYNPNNALAKE
AEEELLRREMRRDAAQQLLRRLAAVKPAEAAA
>gnl|CDD|442220 COG2981, CysZ, Sulfate transporter CysZ [Amino acid transport and metabolism, Inorganic ion transport and metabolism]
MIKNFLSGIGYLLRGLRLIRSPGLRRFVLIPLLINLLLLVGLFWLLLGLLDDLIDWLTPFLPDWLSWLRW
LLWPLAVLLLLLLGFFLFTPVANLIAAPFYGLLAEKVEARLTGRPLPDSLVSLLKDLPRGLRRELRKLGY
LLLRAIPLLLLGFIPGVGQTVAPVLWFLFNAWLLGREYFDYPAERRRLSFREARRLLRRHRGLALGFGAV
VALLLLIPLLNLLVMPAAVAGATLLWVERLRAKRLPSP
>gnl|CDD|442221 COG2982, AsmA, Uncharacterized conserved protein AsmA involved in outer membrane biogenesis [Cell wall/membrane/envelope biogenesis]
KRLMKRLLIILAILLVLLVAALVALPLLFDWNRLRPLIERQVSEATGREVTIDGDLSLSLFPWPGVTLGD
VTLSNPDGFGGPPLASAERLELDLALLPLLSGELEVDEITLDGPVINLERDADGRANWDFLLAAAAAAAD
AEASAWSLDIGRLEITDGRLVYDDAASGADLTLDDLNLTLSGPSLDGPFRLSGSGRLNGQPLTLDGKIGG
LLALGPYPLKLDLRSGDLRLSLDGTVDLAGLDGQLALSGPSLRDLLALLGVTLPEPGPFSLSGRLTADGD
RLRLEDLKGTLGDSDLTGDLSVTGGDRPALTGDLASDRLDLDDLLPAAPAAAAAGAPAAARGLPDAPLDL
SALRALDADVRLSADSLKLGGLPLGDLAAHLTLDDGRLDLDPLSAGLYGGTLSGSLTLDARGDPPRVALK
LSLSGVDLGPLLPDLAGFDRLSGTLNGDLDLSGTGNSVAALLASLNGSASLSLGDGAISGLNLEQLLRNA
G
>gnl|CDD|442222 COG2983, YcgN, Uncharacterized cysteine cluster protein YcgN, CxxCxxCC family [General function prediction only]
AMMRPPFWETKTLEEMTDEEWESLCDGCGKCCLHKLEDEDTGEIYYTNVACRLLDTETCRCSDYENRFQK
VPDCVKLTPENLREFDWLPPTCAYRLLAEGKPLPDWHPLVSGDPESVHEAGISVRGRVVSEDDVDEDDLE
DHIIDWPL
>gnl|CDD|442223 COG2984, COG2984, ABC-type uncharacterized transport system, periplasmic component [General function prediction only]
KPKKIGILQISEHPALDAAREGFKDGLAEAGYGKNLKLDYQNAQGDQATAAQIAAKLVADKPDLIVAIGT
PAAQAAANATKDIPVVFTAVTDPVGAGLVKSLEKPGGNVTGVSDLLPIEKQLELIKKLLPDAKRIGVLYN
PSEANSVAQVEELKKAAKKLGLELVEATVTSSNEIQQALQSLAGKVDAIYVPTDNTVVSALEAIAKVAAR
AKIPVFGGDDSSVKAGALAGYGIDYYELGRQAAEMALRILKGEKPADIPVETPKKFELVINLKTAKALGI
TLPE
>gnl|CDD|442224 COG2985, YbjL, Uncharacterized membrane protein YbjL, putative transporter [General function prediction only]
MELFELLVANPELALFLVIALGYLLGKIKIGGFSLGVAGVLFVGLLIGHFGVTLHIPHFVKSLGLALFVY
AIGLQVGPGFFASLKRDGLKLNLLAVVVVVLGLLVALALAKLFGLDPGLAAGLFAGALTNTPALGAAQDA
LGKLGLSKQLSANPAVGYAVAYPFGVIGIILFVALLPKLFRIDLDAEAKKLEAGEGSAYPPLVTRAYRVT
NPNLVGKTVAELEALLGTRVVISRIRRGGEIIVPTPDTVLQEGDIVLVVGTREALEAAEALLGEEVDDSE
LLDSDLDVRRIVVTNKEVAGKTLGELNLRNRFGVVITRVRRGGVELPATPDTVLQLGDRLTVVGPKEDVE
RVAKLLGNSERKLSETDLLPLGLGIVLGLLLGSIPIPLPGIPPLSLGLAGGPLIVGLLLGRLGRTGPLVG
YMPPSANLLLRELGLALFLAVVGLSAGPGFVETLQESGLLLFLLGALVTLVPLLVVLLVGRYVLKLNYLI
LLGALAGAMTSPPALAAANEAAGSDAPALGYATVYPLAMILLILLGQLLVLLL
>gnl|CDD|442225 COG2986, HutH, Histidine ammonia-lyase [Amino acid transport and metabolism]
MMTTVTLDGGSLTLEDVVAVARGGAKVELSPEARARIEASRAFVEEIAAEGKPVYGVNTGFGALADVRIP
PEDLEELQRNLIRSHAAGVGEPLPEEVVRAMMLLRLNSLARGYSGVRPEVVERLVALLNAGVTPVVPEKG
SVGASGDLAPLAHLALALIGEGEVFYKGERMPAAEALAEAGLEPLTLGAKEGLALINGTQVMTALAALAL
FDAERLLDLADVAAALSLEALLGSDAPFDPRIHALRPHPGQIAVAANLRALLAGSELVESHRNCRRVQDP
YSLRCAPQVHGAVRDALAYAREVLEIELNSVTDNPLVFPDEGEVISGGNFHGQPVALAMDFLAIALAELA
NISERRIARLVDPALSHGLPPFLVPDPGLNSGFMIAQYTAAALVSENKTLAHPASVDSIPTSANQEDHVS
MGTIAARKLRRIVENLEQVLAIELLAAAQALDLRGPLKLSPGTEAAYAAVREVVPFLDEDRPLAPDIEAA
AELIRSGALLAAV
>gnl|CDD|442226 COG2987, HutU, Urocanate hydratase [Amino acid transport and metabolism]
MTTYGRIYGYRFRPEREIRAPPGTELPAKGWQQEAALRMLMNNLDPEVAEHPEELVVYGGTGRAARNWAQ
YDLIVKYLKELEDDETLLVQSGKPVGVFRTHPDAPRVLIANSNLVPNWANWEDFEELEALGLTMYGQMTA
GSWIYIGPQGIVQGTYETFANAARKHFGGDLAGKLFLTAGLGGMGGAQPLAATMAGGVGLIAEVDPSRIE
KRLEQGYLDEVADDLDEALARAKEAKAKKEPLSIGLLGNAADVLPELVRRGIVPDLVTDQTSAHDPLNGY
LPAGLSFEEANELRAEDPEEFKELVKESMARHVEAMLEFQARGAYFFDYGNNIRQEAYDAGVKDAFDFPG
FVPAYIRPLFCYGKGPFRWVALSGDPEDIYKTDEAALELFPQDRDLHRWIRMARENVLFQGLPARICWLG
YGERAKIALAFNEMVRKGELKAPIVIGRDHLDVGSVASPNRETENMKDGSDAVADWPLLNALGNTARGAT
WVSLHHGGGVGIGYSIHAGFVIVADGSEEADERLKRVLTNDPGMGVARHADAGYEEAIETAKERGVTLPM
LVDDELL
>gnl|CDD|442227 COG2988, AstE, Succinylglutamate desuccinylase [Amino acid transport and metabolism]
EDFLALTRWLDEGVLELTPHAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLILGNPA
AMRAGRRYLDEDLNRLFGGRHLQNPESYEAARAKELEQAVGPFFAAGGRVRLHIDLHTAIRNSGHERFAV
YPFRGRPFDLALLAYLAAAGPEAVVLHHAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEE
ALRALLSGAELPEHPAQDLDLYRVVQQIIKHGDDFMLHPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEE
RIVFPNEAVYYGQRAALLLTPKELI
>gnl|CDD|442228 COG2989, YcbB, Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis]
MRRLLLALLAGALAALPAAAAAPADALAQAIRALAAALPAAEALDYDDALAAFYAARGYRPLWTDDGGPT
ARARALLAALAEAALHGLNPADYDLAALQALLAAPADLAALDLLLSDAFLRYARDLRGGRVDPRRIDPDW
DLPPPSLDLAALLQQALAAGDLAAALRSLAPQHPQYAALRQALARYRAIAAAGGWPPVPAGPTLRPGDSD
PRVPALRERLAALGDLPADAPSDSDVYDAELVEAVKRFQARHGLKADGVIGPATLAALNVSPEERIRQLA
LNLERLRWLPRDLGDRYILVNIPDFRLEYVENGKVVLSMRVIVGKPDRQTPVFSSEISYVVFNPYWNVPR
SIARKEILPKLRRDPGYLARNGYEVVDSNGRVVDPSSIDWSAVSAGNFPYRLRQPPGPGNALGRVKFMFP
NKYAIYLHDTPSKSLFNRDMRAFSHGCVRVEDPRDLAEWLLADQPGWSRERIEEALASGKTTTVNLKEPI
PVHLVYFTAWVDEDGRVQFRDDIYGRDARLLAALQKAKA
>gnl|CDD|442229 COG2990, VirK, Outer membrane protein VirK/YbjX involved in antimicrobial peptide resistance, DUF535 family [Function unknown]
MSNILQLFFSLPSGKLYPGKIWKKRRKRLKFLLRSLLHPRATKRLLDFLAQQPLLAALLKAQPRLPCKLH
RPYLDKGFSAKQRLDAIVDHYRFLEQLLPSALLQALLSEKGLTLAELTGKEGEDFSLYLSSNPGLDKEGE
LTLELRDAEGQLLYSLTFSLVQDNGKRTLFIGGLQGPKREVPHELIKQATKACHGLRPKRLLVEALCLLA
RVLGIEQILAVSNKGHIYRSLRYRLKKSKKLHADYDEFWQELGGEPKDDGYFQLPLQIERKPLEEIASKK
RAEYRKRYELLDELEQQIAELLRALQR
>gnl|CDD|442230 COG2991, NqrM, Na+-NQR maturation protein NqrM [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]. Na+-NQR maturation protein NqrM is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase
MTTFLLTFGVFLLVVLAMAIGVIFGRKPIKGSCGGLGALGIEKECDCGEPCDERKKKMAKEAAAAAD
>gnl|CDD|442231 COG2992, Bax, Uncharacterized FlgJ-related protein [General function prediction only]
MKKKITALLLLLAALTLLLAACSEVPRLTLTALPDFSAIKDVDEKKQAFFRYLLPLILAENERILAERER
LLALQAKLLKSLSPEEQAWLSALAKKYRVKNDLLDEADLEELLKRVDIIPPSLVLAQAANESGWGTSRFA
REGNNLFGQWCFSKGCGLVPKQRDEGANHEVAKFDSPQASVRSYMLNLNTHPAYKDLRQIRAQLRAEGKP
LTGLALAEGLENYSERGEAYVEELRSMIRYNNLERYDEAQLAD
>gnl|CDD|442232 COG2993, CcoO, Cbb3-type cytochrome oxidase, cytochrome c subunit FixO [Energy production and conversion]
GEMWHEKLERNPGLLTVLTLLAVSIGGLVEIVPLFFIKSTIEPVEGVKPYTPLELAGRDIYIREGCYNCH
SQMIRPFRDEVERYGHYSLAGESVYDHPFQWGSKRTGPDLARVGGKYSDEWHRAHLIDPRSVVPESIMPA
YPWLAENKLDGEDIAAKMRALRTLGVPYTDEDIANAPADLKGQADPIADDLKDFDGEPPEDTEMDALIAY
LQRLGTDVKFATADAAA
>gnl|CDD|442233 COG2994, HlyC, ACP:hemolysin acyltransferase (hemolysin-activating protein) [Posttranslational modification, protein turnover, chaperones]
ERLNEAEALGAVVWLMMQSPLHRHYPLSDLEWRILPAIQLGQFKLYFDEDGRPIAFVSWAWLSEEAEAKL
LTDDRELTAEEWNSGDRLWIIDFIAPFGHARQMLRDLRKNLFPGEKIRALRHRPDKGSIRKVMRFKGSQV
SKE
>gnl|CDD|442234 COG2995, PqiA, Intermembrane transporter PqiABC subunit PqiA [Cell wall/membrane/envelope biogenesis]
MSDASLVGVLQGLIACPHCDLLLRRPPLPPGERARCPRCGAVLHRRKPNSLQRTLALLLAALILYIPANL
LPIMTTSLLGLSSEDTILSGVIALWQSGSYPVALLVFIASILVPLLKLLALLYLLLSVRRGRRRSPPGRT
RLYRLVEFIGRWSMLDVFVVGILVALVKLGGLASVTPGPGAWAFAAVVVLTMLAAMSFDPRLIWDALEEA
R
>gnl|CDD|442235 COG2996, CvfB, Predicted RNA-binding protein YitL, contains S1 domains, virulence factor B family [General function prediction only]
VVRETDFGYYLDGGEGGEILLPKKEVPEDLEIGDEVEVFVYLDSEDRLIATTRKPKAQVGEFAWLKVVDV
TKIGAFLDWGLEKDLLVPFSEQPRPMKKGDKYLVYLYLDKTGRLVATLKLEKFLDEDSPPYKKGDEVDLL
VYRLTDLGYFVIVNNKYLGLIHKSEVFEELRLGEKLKGRVKKVREDGKIDLSLQPRGYEKIDDDAEKILE
YLEENGGFLPLNDKSSPEEIKKVFGMSKKAFKRALGGLYKEGKIEIEDDGIRLK
>gnl|CDD|442236 COG2998, TupB, ABC-type tungstate transport system, permease component TupA [Inorganic ion transport and metabolism]
MKRRLLLLLLLLLLALALAGAAAAAAESLRLATTTSTEDSGLLDYLLPAFEKKTGIEVKVVAVGTGQALE
LGRRGDADVLLVHAPSAEEKFVAEGYGVNRRDVMYNDFVIVGPADDPAGIKGAKDAAEALKKIAEAKAPF
VSRGDDSGTHKKELRLWKAAGIDPSGDWYRETGQGMGATLNMAAEKGAYTLTDRGTYLAFKNKLDLEILV
EGDPRLFNQYGVIAVNPEKHPHVNYELAQAFIDWLTSPEGQKIIASFGVDGEPLFFPNAGKE
>gnl|CDD|442237 COG2999, GrxB, Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones]
MKLYIYDHCPFCVRARMIFGLKNIPVELIVLLNDDEETPIRMIGKKMVPILEKDDGSYMPESLDIVHYID
ELDGKPILTGPVRPEIAAWLKKVSSYVNRLLYPRWAKAPLPEFATPSARAYFINKKEASIGDFEELLANT
PELIAELNQDLEELEPLIKSPSAVNGELSLDDIILFPLLRSLTIVKGIQFPPKVRAYRDRMSKKTGVPLL
DDVAV
>gnl|CDD|442238 COG3000, ERG3, Sterol desaturase/sphingolipid hydroxylase, fatty acid hydroxylase superfamily [Lipid transport and metabolism]
QFLLAFLLLDFVYYWLHRLSHRVPLLWRFHAVHHSSERMNLLTALRFHPLEILLSALLFLLPLALLGFPP
EAVLLYLALNLLYQFFNHSNIRLPLDGPLEYVFVTPSHHRVHHSRNPEYLDKNYGGILSIWDRLFGTYRP
EEREPIRYGLTGPPRPRN
>gnl|CDD|442239 COG3001, FN3K, Fructosamine-3-kinase [Carbohydrate transport and metabolism]
QAIAEALSEALGPPFEITSVRPVSGGDINQAYRVTTDGRRVFVKLNPASPLGMFEAEAAGLRALAATGTI
RVPEVIGVGTTGDHAFLVLEYLELGPPTAGAWERLGRQLAALHQATAPRFGWDRDNFIGSTPQPNTWTDD
WAEFFAEQRLGPQLQLAAEKGLLFAADRERIERLVERLPELLAPHEPQPSLLHGDLWSGNVLFTADGEPV
LIDPAVYYGDREVDLAMTELFGGFPDAFYDAYQEVWPLDPGYEERKPLYQLYHLLNHLNLFGGSYLSQAE
RILDRLL
>gnl|CDD|442240 COG3002, MpsB, Na+-translocating membrane potential-generating system subunit MpsB, UPF0753/DUF2309 family [Energy production and conversion]
MNTLAGSEFDLREALEEACHRIPPQWPLDDFVAVNPLHGLQDLPFAQAAARLARLFGARVTLPRAEYREA
YASGRITDADLEAALAEAGGALSLEELKAALLQPPPAPPPALPLLRDLLKRLTGIDWDQLVHPQISRWCA
AYFDQGQALWQPPGRGKGLYAAWRELATHDLTPLLMGLRGLRARVAALPEDAEAAIAWALERLGLPEAAW
EDYLHALLLSLGGWAGWARYLEWQAELAGRRDITLRDLLAIRLAWEAALLDEKRGALEAAWRAALAAQAA
PAVEATEALEVDEIWQEALERAYQRELLAGLAAAPTPAPPAERPAVQAAFCIDVRSEVFRRALEAVDPGI
ETLGFAGFFGVPIAYRPLGSDAARPQCPVLLAPKYLVKEVPLEAAAADRARRRRLRAARAWKRFKRSAVS
GFSFVETLGLLYAGKLLGDSLGPSRPVALPDAFGLMAKERPRTRPRLENEDENGLQIGFTLDERAALAEG
VLRAMGLTRGFAPLVLLVGHGSSSVNNPHAAALDCGACGGQTGEVNARVLAALLNDPEVRAGLAERGIDI
PEDTVFVAALHDTTTDEITLFDLDLLPASHRADLARLQRWLAQAGDLARRERARRLGLAPTKSPEALLAD
VRRRARDWAEVRPEWGLAGNAAFIVAPRSRTRGLFLDGRAFLHSYDWRQDPDGAVLELILTAPMVVAHWI
NLQYYFSTVDNERFGSGNKLLHNVVGLIGVFEGNGGDLRTGLPWQSVHDGERWVHEPLRLLVVIEAPPEA
IDAVIARHPAVRELVDNGWLHLFALDPEGREFRRYRGGGGWEPYEPDEE
>gnl|CDD|442241 COG3004, NhaA, Na+/H+ antiporter NhaA [Energy production and conversion, Inorganic ion transport and metabolism]
LRRFLRSEAAGGILLLLAAVLALIWANSPLAESYEALLHTPLGLGIGSLHLDLSLLHWINDGLMAIFFFL
VGLEIKRELLVGELSSPRKAALPIIAALGGMVVPALIYLAFNAGTPEAARGWAIPMATDIAFALGVLALL
GSRVPASLRVFLLALAIVDDLGAILVIALFYTSGLSLLALLLAAAALALLALLNRRGVRSLWPYLLLGVV
LWYAVLKSGVHATLAGVLLALTIPARPRVGGEEEAESPLERLEHALHPWVAFLILPLFAFANAGVSLSGL
SLAALTSPVTLGIALGLVLGKPLGIFGFSWLAVKLGLARLPAGVSWRQLYGVGLLAGIGFTMSLFIAELA
FPDPELLDAAKLGILLGSLLAAVLGYLLLRLRLRRKR
>gnl|CDD|442242 COG3005, NapC, Tetraheme cytochrome c subunit NapC of nitrate or TMAO reductase [Energy production and conversion]
KRKPWSLLLLLLVGFVLGVGFWGGFNTALELTNTPEFCVSCHVMEPVYEEWQHSSHYSNASGVRATCNDC
HVPHGFVNKYARKAIDGSKDVYGFTTGTIPTPIKFEAHRLEVDSENCRRCHSFLVMDISKQSARAAKAHQ
KAEEEGKTCIDCHKGVAHGLP
>gnl|CDD|442243 COG3006, MukF, Chromosome condensin MukBEF, kleisin-like MukF subunit [Cell cycle control, cell division, chromosome partitioning]
MSEFSQTVPELVGWVKQNDFSLSLPTERLAFLLAIAVLNSERFDGELSEGELIDAFRYVSKGFEQSDETL
TVRANNAINDLVRQRLLSRFTSEMTEGESIYRLTPLGIGITDYYIRQREFSTLRLSIQLSIVADELQRAA
EAAEEGGDEFHWRRNVFAPLKYSVAEIFDSIDLTQRAMDEQQNQVKEDIAALLNQDWRAAISSCEQLLSE
TSGTLRELQDTLEAAGDKLQAQLLRIQEAVMGRAELEFVDQLIFDLQAKLDRIISWGQQAIDLWIGYDRH
VHKFIRTAIDMDKNRVFSQRLRQSIQDYFDHPWALTYANAERLLDLRDEELALRDEEVTGELPAELEYEE
LSDVNEQLAERIEEHLAVFKEQGKPLDLGLVLRDYLAQYPRSRHFDVARILVDQAVRLGVASADFSGLQP
EWQPINDYGAKVQAHVIDQY
>gnl|CDD|442244 COG3007, COG3007, Trans-2-enoyl-CoA reductase [Lipid transport and metabolism]
MIIKPKVRGFICTTAHPVGCEANVREQIDYVKAQGPIANGPKKVLVIGASTGYGLASRITAAFGSGADTI
GVFFEKPPTEKKTGTAGWYNTAAFEKAAKEAGLYAKSINGDAFSDEIKQKVIELIKEDLGQVDLVVYSLA
SPRRTDPDTGEVYRSVLKPIGEPYTGKTIDTDKDEVSEVTIEPATEEEIADTVKVMGGEDWELWIDALKE
AGVLAEGAKTVAYSYIGPELTWPIYRHGTIGRAKEDLDRTAKAINAKLKALGGEAYVSVNKALVTQASSA
IPVMPLYISLLYKVMKEKGTHEGCIEQIYRLFAERLYGDAPPLDEEGRIRLDDWELRPDVQAEVKALWPQ
VTTENLKELTDYAGYKHEFLKLFGFGVDGVDYDADVDPEVLIPL
>gnl|CDD|442245 COG3008, PqiB, Intermembrane transporter PqiABC subunit PqiB [Cell wall/membrane/envelope biogenesis]
MTDNNPPEPEAKVRRRRRISPVWLVPIVALLIGAWLLYQAYSERGPEITITFDSAEGIEAGKTKVKYKGV
DVGTVESVRLSDDLSHVIVTARLNKDAEPLLREDTRFWVVKPRISLSGVSGLDTLLSGAYIGLDPGKSGE
PQREFTGLEEPPLVTPDAPGLRFVLRADDLGSLSVGSPVYYRGIPVGRVESYELDPDGRGVTIQVFIEAP
YDKLVTTNTRFWNASGVDVSLGASGLKVNTESLASLLSGGIAFDTPDGSEDGEPAKEGTVFTLYPDEAAA
QESPYGERVEYVLYFDDSVRGLSVGAPVEFRGIRVGTVTSVPLEYDPDTQRFRIPVLIRIEPERLGLRGS
RFWASEEDWRQLLEPLVARGLRAQLKTGNLLTGQLYVDLDFYPDAPPAELDREAGYPVLPTVPGGLDQIQ
LQVSGILDKLNKLPLEEIGENLYRTLANLDSTLASASGLLASLNLTQVLPELQDTLASLQKTLAGGIGLS
PDSPLYQDLQQALQELTRAARSLRLLADTLPRHPNSLIFGRPEVKDPQPKAA
>gnl|CDD|442246 COG3009, PqiC, Intermembrane transporter PqiABC lipoprotein subunit PqiC [Cell wall/membrane/envelope biogenesis]
MKRPLRLLLLLLLALLLAACASSPPTRYYTLPPPAAPAAAAAAAAAPVIEVGPVSLPDYLDRPQIVYRTG
DGRLVIAENHRWAEPLSDQLTRALAANLAARLPGARVAAQPWPLAGRPDYRLRVDVTRFDGRPDGQAVLS
AQWSLRRGGGGGPLLSRRFSIEEPLAGDGYDALVAALSQALAQLADQIAAALAALPAA
>gnl|CDD|442247 COG3010, NanE, Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism]
NELLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRD
YPDSDVYITPTLEEVDALAEAGADIIALDATRRPRPDGETLAELIARIHEEPGALVMADISTLEEALAAA
ELGADIVGTTLSGYTGETKGTDGPDLELLKELVAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAIT
RPELITKRFVDALKKA
>gnl|CDD|442248 COG3011, YuxK, Predicted thiol-disulfide oxidoreductase YuxK, DCC family [General function prediction only]
MPAPPPPKPIVLYDGVCPLCNREVRFLLRRDRAGRFRFVPLQSEDGQLAAPGLDPEDLLDSLHLIDEDGR
VYTGSDAVLRILRALGGPWRLLAALLRLPGLRPLRDRLYRLVARNRYRLFGKKDACRLPTPEL
>gnl|CDD|442249 COG3012, YchJ, Uncharacterized conserved protein YchJ, contains N- and C-terminal SEC-C domains [Function unknown]
PSNSPCPCGSGKPYADCCGPYHAGAAPAPTAEALMRSRYSAFVLGDADYLLATWHPSTRPALLRLEIEAW
APGTQWLGLEILATEAGPDDDEGTVEFVARYREGGRAGRLHERSRFVREDGRWYYVDGEVAPKPGRGSGK
KFKK
>gnl|CDD|442250 COG3013, YfbU, Uncharacterized conserved protein YfbU, UPF0304 family [Function unknown]
MEMTNAQRLILSNQYKIMALLDPENAEDYRRLATILERGYGLQYRWELDKLFGELSEEECREVIDILEMY
HALQESYENLDDADKSELDARRLEFLGFDGNTEGEYLSYVRFLVEDEGRFPEFDKKGHDLNSHTPMLDKY
QRMLTVWRACPRQYKHLSVEEIQQILNA
>gnl|CDD|442251 COG3014, COG3014, Uncharacterized conserved protein [Function unknown]
MKSNKLLVLALALLLSGCATSYSARTQDLRQALESGDYQQALKLLEKNKKEKSGRDRLLYLLEKGMVLHL
AGDYEESNKAFEEAERLIEDLETRVSSVAEEAGSLLTNDNARPYRGEDYEKVMIHTYKALNYLQLGDLEG
ALVEARRANERQRRAKEKYEKEIEEAEKEAKKQGLKNRYSDLGKYYNGYQNAFALYLSGLLYEADGDLND
AFISYRRALELYPDNPQLKEDLLRLAKKLGFTDELERYEKRFGDKEPPKPGEGEVVVIYENGLAPVKKEV
RIDLPLFLGGDLGYVRIALPKYVERPPAYSPLSVSADGQTGKTETLADIDALAAKTLKDRMPGILARALA
RAAAKKGAQYAARKKNGELGGLLTGIANAATEQADTRSWQTLPAEIQVARVPLPAGEHTLTLKAGGGNGE
VTVFTVEVPPGRTTLVYVR
>gnl|CDD|442252 COG3015, CutF, Uncharacterized lipoprotein NlpE involved in copper resistance [Cell wall/membrane/envelope biogenesis, Defense mechanisms]
MKKILLLLLLAALLLAGCNNRSQTETATVKATAVADAHNAENSLDWAGTYRGVLPCADCEGIETTLTLNA
DGTYVLTETYLGKKDGPFTSKGTFTWNRDGDKIVLTDSNGEKRYYRVGENTLEMLDMDGNPITGPLADNY
TLKKVDK
>gnl|CDD|442253 COG3016, PhuW, Putative heme-binding protein PhuW [General function prediction only]
MKRLLILLLALLLAACAASTSAPQDHPLAGQIYDLATGKALSLAQLLAELADADVVLLGEKHDNPAHHRL
QLELLQALHAQGPQLALGMEMFERDQQPALDRYLAGEISEAELLEAAEWDRGWPNYWELYRPLVEFAKEH
GLPLLALNLPRELVRKVAREGLEALPPEERAYLPLDIDLPDPAYRALLAEIMGGHGALPEEQLERFVAAQ
QLWDATMAESIAAALKAHPGRPVVLIAGSGHVRYGLGVPLRLARRLPGLKVVVLLPVEQGEPEELDPAGI
ADYVWFT
>gnl|CDD|442254 COG3017, LolB, Outer membrane lipoprotein LolB, involved in outer membrane biogenesis [Cell wall/membrane/envelope biogenesis]
MSKLRRLLLLLLLLLLLAGCATLPPRPTTSPTSPAWQAHQQQLQQLQQWQLRGRIAVRSPQQRGSARFNW
QQQGDRYRLLLSGPLGQGVLELEGDPGGVTLTDSDGKTYQAADAEALLQQLTGWSLPVSQLRYWVRGLPA
PAAPAEYTLDAQGRLASLNQDGWQIDYLRYQTVGGPALPKRIELTRGDLRIKLVIDQWQL
>gnl|CDD|442255 COG3018, FlgP, Flagellar basal body lipoprotein FlgP, LPP20 family [Cell motility]
MKKRLLLLLLALLLLTGCSPVNWEPVDPWEPPVLTAVGYGAIAPQRGLSPAQARLMAMRAAKLDAYRNLA
EQVYGVRIDSSTTVRDLVLQNDSVRTSVDGVIRGARVVSSYPVGDGTYETELELDLDGVFRLYVKEVKYY
>gnl|CDD|442256 COG3019, COG3019, Uncharacterized metal-binding protein, DUF411 family [Function unknown]
MKSRRTLLAAALALALLAALAGAAAAAAAPAITVYKSPTCGCCGAWVDHLEANGFEVTVVDTDDLAAVKQ
RLGVPPELASCHTAVVGGYVIEGHVPAADIKRLLAERPDAIGLAVPGMPVGSPGMEMGDRKDPYDVLLFG
KDGSTSVFARYR
>gnl|CDD|442257 COG3021, YafD, Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily [General function prediction only]
MTKRRLLALLWAALLLLLATLLPLGLGADHWLIRLLDFFRPQLAVLALLLLLLALLRRRWALAAAALLLL
LVQAALILPYTLPAPKSAPAGGPDLRVLTANVLFGNADAEALAALVREEDPDVLVLQETTPAWEEALAAL
EADYPYRVLCPLDNAYGMALLSRLPLTEAEVVYLVGDDIPSIRATVELPGGPVRLVAVHPAPPVGGSAER
DAELAALAKAVAALDGPVIVAGDFNATPWSPTLRRLLRASGLRDARAGRGLGPTWPANLPFLRLPIDHVL
VSRGLTVVDVRVLPVIGSDHRPLLAELALP
>gnl|CDD|442258 COG3022, YaaA, DNA-binding protein YaaA associated with the oxidative stress response [Replication, recombination and repair]
LILLSPAKTKDFGSPLDLDELTFPELLEEREELIDALRKLSADELAKLMGISDKLAELNVERFQDWNAPL
TTAPARPAILAYTGVVYDGLDAASLSEEALAYAQEHLRILSGLYGLLRPLDLIPPYRLEMGTKLPGLRGK
NLYAFWGDRLTDALNEELGDELVVNLASNEYFKAVDPKALKARVITPVFKEEKNGKRKVISHYAKKARGL
MARYLIENRIEDPEELKAFDREGYRFDEELSTEDELVFVR
>gnl|CDD|442259 COG3023, AmpD, N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis]
MKGYTIDTGARFVPSPNFDERPAGAEIDLIVIHYTAGPPGGGALDWLTDPALRVSAHYLIDRDGEIYQLV
PEDDRAWHAGVSSWRGRTNLNDFSIGIELENPGHGWAPFTEAQYEALAALLRDLCARYGIPPDHIVGHSD
IAPGRKTDPGPAFPWARLAALLARYGY
>gnl|CDD|442260 COG3024, YacG, Endogenous inhibitor of DNA gyrase, YacG/DUF329 family [Replication, recombination and repair]
MTKVPCPICGKPVEWSPENPYRPFCSKRCKLIDLGRWLSEEYRIPGEPLDDDEEDPEE
>gnl|CDD|442261 COG3025, PPPi, Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and metabolism]
MAREIELKLLVDPEALPALRQHPLLAGLAVGEPATRRLENTYFDTPDLDLRRAGIGLRVRREGGRWEQTL
KTAGQVVGGLHQRPEWEVPLPSPEPDLSLLPDEPLPELLDAAALGAALQPVFTTDFERTTWLLTLADGSL
IEVALDQGEIRAGERREPICELELELKSGDPAALFALALELAEALPLRLSSLSKAERGYRLAAGAPAAPV
KALPVALDPDMTAEEAFRAILRACLAHLQANEEALLRGDDPEAVHQMRVAL
>gnl|CDD|442262 COG3026, RseB, RseB, negative regulator of sigma E activity [Signal transduction mechanisms]
MKRLLLALLLALLLASASAAAAAAAADAEALLQRMAQAARQLNYEGTFVYQRGGQIESLRIRHAVDDGGE
YERLESLDGPPREVIRRGDEVSCFLPDLKPVSLESRHIVDSFPALLPADLERLSEYYDFRLGGRERVAGR
DAQVVRLVPRDGLRYGYRLWIDEETGLLLKSDLLDRDGEVLEQFAFTSLELGDPIDDSALKPSLAGAKLW
RPPLLALPPADAAASGWQLGWLPPGFKLVSQSRRPLPGSGEPVEHLLYSDGLASVSVFIEPADEGSPPLE
GLSRQGATTAYSRRVGGYEVTVVGEVPAATAKRIADSVRFKA
>gnl|CDD|442263 COG3027, ZapA, Cell division protein ZapA, inhibits GTPase activity of FtsZ [Cell cycle control, cell division, chromosome partitioning]
MSMNRVTVTILGREYRLACPEGEEEHLREAAAYVDEKMREIREKGGVLGTERLAVLAALNLADELLKLKE
ELEELEERLEELEEKLDEALEELE
>gnl|CDD|442264 COG3028, YjgA, Ribosomal 50S subunit-associated protein YjgA, DUF615 family [Translation, ribosomal structure and biogenesis]
MSRKPLDDEDEEDERPSKSQLKREMHALQDLGEELVELSPDQLAKLPLPEDLRDAIAEARRITKHEARRR
QLQYIGKLMRREDLEPIRAALDKLKNGSAQETAAFHRLERWRDRLIAEGDDALTELLEEYPQADRQQLRQ
LIRNARKEAAANKPPKAYRELFQYLRELLEAAEA
>gnl|CDD|442265 COG3029, FrdC, Fumarate reductase subunit C [Energy production and conversion]
MSKRKPYVREMKATWWKKLPFYRFYMLREGTAVFVAWFSLVLLYGLFALSQGPEAWAGFVAFLQNPLVLL
LNLIALAAALLHTVTWFELAPKAMNIIIGGERVPPKPIVAGLWAATAVVSVVILALAL
>gnl|CDD|442266 COG3030, FxsA, FxsA protein affecting phage T7 exclusion by the F plasmid, UPF0716 family [General function prediction only]
MFRLLLLLFLLLPLLEIALLIQVGSAIGVLPTLLLVVLTAVLGLLLLRRQGLRTLRRLQQALAQGELPAR
ELLDGALLLLAGALLLTPGFLTDALGLLLLLPPVRRLLRRLLLRRVVVRVRSAGTGPRPGDGDVIEGEFE
REDD
>gnl|CDD|442267 COG3031, PulC, Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular transport]
MTRLALARVLTLLLVLTDAPETRLNLTLLGVVASSDPERSFAIIAEGGGKQKSYRVGDEIPGGATLVAVY
RDRVILSNNGRLETLMLDGEDYAAPAAAAAAPASSPAASSAAASAGGQEELEVSRDELLANPNELLDYIR
LSPVREDGKLVGYRVNPGRPGSLFSKLGLQPGDVITSINGQDLTDPAQALELLQQLRDASEVTLTVERNG
QPVTLTYNLR
>gnl|CDD|442268 COG3033, TnaA, Tryptophanase [Amino acid transport and metabolism]
MMMKTPAEPFRIKMVEPIRMTTREERERALKEAGYNTFLLRSEDVYIDLLTDSGTGAMSDRQWAAMMLGD
ESYAGSRSFYRLEDAVRDIFGFKYVLPTHQGRAAENILFPVLVKPGDVVPSNMHFDTTRAHIELAGARAV
DLVIDEALDPESDHPFKGNMDLDKLEALIEEVGAENIPFVMMTITNNSAGGQPVSMANIREVRELADKYG
IPLVLDAARFAENAYFIKQREEGYADKSIKEIVREMFSYADGFTMSAKKDGLVNIGGFLALRDEELFEKA
RNLVILYEGFPTYGGLAGRDMEALAVGLYEGLDEDYLRYRIGQVEYLGEKLDEAGVPVVTPAGGHAVFVD
AKRFLPHIPQEQFPAQALAAALYLESGIRGVEIGSLSLGRDPDTGEQVPAPLELVRLAIPRRVYTQSHMD
YVAEALIELYERRESIKGLRIVYEPPVLRHFTARLEPVSD
>gnl|CDD|442269 COG3034, YafK, Murein L,D-transpeptidase YafK [Cell wall/membrane/envelope biogenesis]
MMRLLLLLALLALAALLPPALLSPPSPVLIVVDKSERRLELWKGDDGRGKLLKTYPICLGSGPLGPKRRE
GDRRTPEGFYFITRRNPNSKYHLAFGISYPNAYDRARGRGRSTGGGIMIHGTPSGDYHRPPDWTDGCIAL
TNEDIEEIYALVREDGTPVVIFP
>gnl|CDD|442270 COG3036, ArfA, Stalled ribosome alternative rescue factor ArfA [Translation, ribosomal structure and biogenesis]
MSKYQHGRGQIKDNALKALVTDPLFRQRVEKNKKGKGSYQRKAKHGKKEGWEASGKQFFTLGFLL
>gnl|CDD|442271 COG3037, UlaA, Ascorbate-specific PTS system IIC component UlaA [Carbohydrate transport and metabolism]
MSILNFIVNNILGQPAILIGLIALIGLLLQKKPFSDVISGTIKTIVGFLILSAGAGILVGSLTPFGEMFN
KAFGLQGVVPNNEAIVAAAQEKYGSEVALIMLFGFIINILLARFTKFKYIFLTGHHMLYMACLLAVILVV
AGLSGWELIIVGGILLGLYWAVSPALAQPFMRKITGNDDFAIGHFGTLGYWLSGKIGKLVGKKEKSTEDI
KLPKWLSFLRDSTVSTALTMTIFYLIIALFAGPDYVEELSGGTNFIVYALLQALTFAAGVYILLQGVRMF
LAEIVPAFKGISEKLVPGAKPALDCPVVFPYAPNAVLIGFLSSFIGGLVGMLLLGLLGLVVIIPGVVPHF
FDGATAGVFGNATGGRRGAIIGGFVNGILITFLPALLLPVLGSLGFAGTTFGDADFAVVGIILGLIAKLF
GGIGIIIIIV
>gnl|CDD|442272 COG3038, CybB, Cytochrome b561 [Energy production and conversion]
MSLRNTPTRYGLVARALHWLMALLIIGLFALGLLMVDLPRGDPLRLFLYSLHKSLGVLVLLLVLLRLLWR
LTNPPPPLPPSMPRWQRLAAHLVHLLLYLLMLAVPLSGWLMSSASGRPVSLFGLFTLPALVPKNEALADL
AGELHELLAWLLLALIALHVAAALKHHFIDRDGTLRRMLPGRR
>gnl|CDD|442273 COG3039, IS5, Transposase and inactivated derivatives, IS5 family [Mobilome: prophages, transposons]
MKQQLFAADERYAKKKKQTRPLLFLEEMIDVVPWALLLDIIEPRYPKGKGGRPPYPLERMLRILFLQQWY
NLSDPAMEDALYDRLSFRRFAGLDLSDRVPDETTILRFRHLLEEHGLGEALFEEVNAQLSEKGLILRKGT
IVDATIIAAPSSTKNKDRQRDPDAHQTKKGNQWYFGYKAHIGVDADSGLIHTVVTTAANVHDVTHLDELL
HGEETDVYADKGYQGAEKREELKARGIRWHIARKPGRNKPLSELQKRRNRRKAKVRAKVEHPFGVIKRLF
GYKKVRYRGLAKNTAQLFLLAALYNLKRARRLLLAG
>gnl|CDD|442274 COG3040, Blc, Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis]
MKRLRLLLALAAALLLAGCASAPPPPVTPVPPVDLDRYLGTWYEIARLPHRFERGCVNVTAEYSLREDGT
IKVINRGRKGFDGEWKEAEGKARVVDDPTNAKLKVSFFGPFYGDYWILALDPDYQYALVGGPDRDYLWIL
SRTPTLPDAVYQELLARARALGYDTSKLIRVPQTPPQV
>gnl|CDD|442275 COG3041, YafQ, mRNA-degrading endonuclease YafQ (mRNA interferase), toxin component of the YafQ-DinJ toxin-antitoxin module [Translation, ribosomal structure and biogenesis, Defense mechanisms]
MLKIVYTKQFKKDLKKLKKRGPDIEKLKKVLRLLAEGNPLPPSLRDHALKGNLKGYRECHINPDWRLIYR
IEDDVLILVRIGSHSELF
>gnl|CDD|442276 COG3042, Hlx, Putative hemolysin [General function prediction only]
MKRALLLLLLAAALLLAGCSSSQPNAPPPPQIGMANPASVYCVQQGGTLEIRKQLDGGQVGMCQLPDGRR
CEEWALYRGDCP
>gnl|CDD|442277 COG3043, NapB, Nitrate reductase cytochrome c-type subunit NapB [Energy production and conversion, Inorganic ion transport and metabolism]
MKKLILLALALLAALALAGAAQAAEEVLSLRGSAELDAEAVAPPLKKPPKDDKRIARNYVNQPPLIPHSI
DGYQITKNANKCLSCHSRENAKETGAPKISVTHFMDRDGKVLADVSPRRYFCTQCHVPQADAKPLVENTF
KPVDGLGKKK
>gnl|CDD|442278 COG3044, COG3044, Predicted ATPase of the ABC class [General function prediction only]
MKNKEELRKLLKRIDGKGYKAYKDIKGTYDFGDFTLFIDHVQGDPFASPSKIRVRIPQSIAGFPAELYDS
PVRRIALEDYLTRSFAQAIRKLASGRRGTGKSGLIAIDRPGQEVLERTAVLINEDYVEARFSVGLPARGR
RILGREAAKLLFEELPRIVEASLLYENLDAEALERHVELVEDQEYLRQQLKERGLVAFVADGSILPRESG
VSDRPLKENAVPFQSPESLEVEFELPNGGTITGMGIPEGITLIVGGGYHGKSTLLKALERGVYNHIPGDG
REYVVTDPDAVKIRAEDGRSVEGVDISPFINNLPQGKDTRRFSTENASGSTSQAANIMEALEAGARLLLI
DEDTSATNFMIRDARMQALVAKEKEPITPFIDRVRQLYEDLGVSTILVMGGSGDYFDVADTVIMMDEYRP
RDVTEEAKAIAEEYPTGRKAEGGAPFGPITPRVPLPESLDPRRGKKVKIKARGLDEIQFGRETIDLSAVE
QLVDPSQTRAIAAALRYARKRYLDGRRSLREILDLIEEDIEEKGLDVLSPFRGHPGDLARPRRFELAAAL
NRLRTLKVK
>gnl|CDD|442279 COG3045, CreA, Periplasmic catabolite regulation protein CreA (function unknown) [Signal transduction mechanisms]
MKRLLLLALAAALALLAAAAAAAEEIGEVSTVFKLLGPNDKIVVEAFDDPKVPGVTCHVSRAKTGGIKGL
LGLAEDPSDASIACRQTGPITFGDKLKQGEEVFSERRSLLFKSLQVVRIYDAKRNTLVYLVYSDKLIEGS
PKNSISTVPIMPWGP
>gnl|CDD|442280 COG3046, COG3046, Uncharacterized conserved protein related to deoxyribodipyrimidine photolyase [General function prediction only]
MRTLRLILGDQLNPDHSALREADPADDVVLMAEVRQEATYVPHHKQKIALFFSAMRHFADELRAAGWRVD
YVRLDDPDNTGSLAGELARAIAEHGPDRLEVTEPGEYRLLQQLEALAASLGIPVEVLPDEHFLCSREEFA
AWAKGRKQLRMEYFYREMRRRTGILMDGDQPVGGKWNFDADNRKPPPGDLSPPAPLRFEPDAITQEVLEL
VERRFVDHFGDLDPFRWPVTRAQALQALDHFIEHRLPHFGDYQDAMLTGEPFLFHSLLSFALNLGLLDPR
EVIEAAEAAYRAGDAPLNSVEGFIRQILGWREYVRGIYWLEMPDYAERNALGATRPLPEFYWTGETDMNC
LAQAIGQTLDHAYAHHIQRLMVTGNFALLAGVDPQEVHEWYLAVYIDAYEWVELPNTLGMSQFADGGLLA
SKPYAASGNYINRMSDYCKGCRYDPKKKTGEDACPFNALYWDFLDRHRDRLAGNPRMAMMYRNLDRMSDE
ERQAIRERAEAFLARLDA
>gnl|CDD|442281 COG3047, OmpW, Outer membrane protein OmpW [Cell wall/membrane/envelope biogenesis]
KKTLLALAAAAAAALAAGPAMAQDAGDWIVRAGAAGVDPDSSSGDLTGGTVPGTDVDVDNNTTPGLTFTY
FFTDNIAVELLLGTPFKHDVSGAGSLAGLGKLGSVKHLPPTLTLQYHFGPDSKFRPYVGAGVNYTRFFDE
KLTAALGGTDLKLDDSWGPAAQAGVDYALDDNWFLNADVKYIDIDTDATLNGGGATVKGDVKLDPWVVGV
GVGYRF
>gnl|CDD|442282 COG3048, DsdA, D-serine dehydratase [Amino acid transport and metabolism]
MAGKTMAQLIADFPLLEDLIALEEVLWFNPNYTPAAEALPDVGLTAADVADAEARLQRFAPYLAKAFPET
AASGGIIESPLVPIPAMQKALEERYGQPIPGRLLLKCDSHLPISGSIKARGGIYEVLKHAEKLALEAGLL
KEEDDYSKLASDEFRAFFSQYSIAVGSTGNLGLSIGIMSAALGFQVTVHMSADAKQWKKDLLRSKGVTVV
EYEGDYSVAVEQGRKQAEADPNCHFVDDENSRDLFLGYAVAALRLKKQLAEAGIVVDAEHPLFVYLPCGV
GGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLATGLHDKISVQDIGLDNRTAADGLAVGRASGFVG
RAMERLLSGVYTVEDDELYRLLALLADTEGIRLEPSALAGMPGPLRLLGSAGQAYLERHGLTEKMANATH
LVWATGGSMVPEEEMEAYLAKGKALL
>gnl|CDD|442283 COG3049, YxeI, Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]
AEMCTRIVYKTKDGTVITGRTMDWGFDLGSNLVVFPRGYERDGEVGPNSLKWTSKYGSVGMGAYDGYPLT
ADGMNEKGLAAALLYFPGYADYPKRDKEGKPNLAPSEFVQWVLDNFATVEEVKEALKKINFVNDPVPGLG
RVAPLHLSISDATGDSAVIEYIDGKLVIHDNPVGVMTNSPTFDWQLANLRNYINLSPKQPEPVKLGGLTL
TPFGQGSGTLGLPGDYTSPSRFVRAAFLKNALPKPADEEEAVASVFHILRNVSIPKGIVRPDEPNISYTQ
WTSVADLKNKTYYFETYDNPNIFWVDLKKLDFSKGAEVKKLDLDPNEQLIGDVNKKF
>gnl|CDD|442284 COG3050, HolD, DNA polymerase III, psi subunit [Replication, recombination and repair]
MSRRDWLLQQLGITQWVLRRPAVLQGEIAISLPDNIRLVIVAEELPALNDPLLSDVLRALALTPDQVYCL
TPEQVAMLPEDIRCNCWLLGVDEPLNLAGAQLHSPSLSELYANAQAKRALWQQICQHEHDFFPHAD
>gnl|CDD|442285 COG3051, CitF, Citrate lyase, alpha subunit [Energy production and conversion]
GGLKPFQGAFATKPEGRRAAPKVRSVPPGEDKLVASLEEAIEKSGLKDGMTISFHHHFRNGDYVVNMVME
AIAKMGIKDLTLAPSSLFPVHEPLIEHIKNGVITRIETSGLRGPLGEAISKGLLKKPVVIRSHGGRARAI
ESGELHIDVAFIAAPSADEYGNANGVSGKSACGSLGYAMVDAQYADKVVAVTDNLVPYPNTPASIPQTQV
DYVVKVDSIGDPAKIVSGATRITKNPRELLIAKYAAEVIEASGYFKDGFSFQTGAGGASLAVTRFLREKM
RKKGIKASFALGGITGYLVDMLEEGLFKKLLDVQSFDLEAVESLKENPNHQEISASMYANPHNKGAAVNQ
LDVVILSALEVDTDFNVNVLTGSDGVIRGASGGHQDTAAGAKLTIIVAPLVRGRIPTIVDKVTTVVTPGE
TVDVLVTERGIAVNPRRPDLIEKLKKAGLPVKTIEELKEEAEKLTGKPKPIEFTDRVVAVVEYRDGSVID
VVRQVKE
>gnl|CDD|442286 COG3052, CitD, Acyl-carrier protein (citrate lyase gamma subunit) [Energy production and conversion]
MEIKKEAVAGTLESSDLMVTVEPADGGGIEIELTSSVEKQFGDQIRAVVRETLARLGVTGAKVIIEDKGA
LDCVIRARLETALERALGSEE
>gnl|CDD|442287 COG3053, CitC, Citrate lyase synthetase CitC [Energy production and conversion]
NPKELKAVREFLEQNGLTLDEDIDYTVGIYDDGKLIATGSLAGNVLKCVAVDPDYQGEGLSLQLITELIN
LAYERGIFHLFLYTKPENEKLFESLGFYPIASVDPDVVLLENGPPGIQDYLKKLRKLRQPGGKIGAIVMN
ANPFTLGHRYLVEQAASECDWLHVFVVSEDRSLFPFEDRLELVKQGTADLPNVTVHPGGDYIISRATFPS
YFLKDKGVVDEAQTELDLRIFRKYIAPALGITHRFVGTEPFCPVTAIYNQAMKRWLPPAGIEVVEIPRKE
KDGEAISASRVRKLLAEGDLEAIRKLVPETTYAYLQSHEAKEIIAKIKKG
>gnl|CDD|442288 COG3054, YtfJ, Predicted transcriptional regulator YtfJ [General function prediction only]
MKKKTLLALLLLLLPFFASAHNIQLGQPLPPVGVADKGELVLNGDKFSYQPWNSAQLAGKVRVIQHIAGR
SSAKEMNAPLIEAIKAANFPHDKYQTTTIVNTDDAIWGTGSFVRSSLEDNKKEFPWSQFVLDSNGVVRKA
WQLKEKSSAIIVLDKQGKVQFAKEGALSPEEVQQVIALINQLLKK
>gnl|CDD|442289 COG3055, NanM, N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis]
ATWSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELAPLPGPPRHHAAAVAQD
GKLYVFGGFTGANPSSTPLNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGGNVAWVE
VYDPATGTWTQLAPLPTPRDHLAAAVLPDGKILVIGGRNGSGFSNTWTTLAPLPTARAGHAAAVLGGKIL
VFGGESGFSDEVEAYDPATNTWTALGELPTPRHGHAAVLTDGKVYVIGGETKPGVRTPLVTSAEVYD
>gnl|CDD|442290 COG3056, YajG, Uncharacterized lipoprotein YajG [Function unknown]
MKKLKLLLLLLAALLLAGCASSPQTLTLTPKVPPSQNPIGQGATVSLTVVDQRPSQYLGSRGGGYGELST
LTASNDLRLLLQQALEQGLEAQGFRVGANNANANLTVELEELYADVEQGNLRYNITSKADLQVVVQGGNG
TFTKNYRASRSQEGAFSPSNEKIEEALNEVLSDVLQDMLNDPELSNFLKQNA
>gnl|CDD|442291 COG3057, SeqA, Negative regulator of replication initiation SeqA [Replication, recombination and repair]
MKTIEVDDELYRYIASQTQHIGESASDILRRLLNLPSSQQPAVVPQTSSVTTSEAAAVVPKAASVATPED
RVRAVRELLLSDEFAEQKKAVNRFLLILSTLYRLNPEAFAQATESLKGRTRVYFAQDEETLLASGSSTKP
KQIPGTPYWVITNTNTGRKRSMLEQVMQSMGFPAELIEKVCGTI
>gnl|CDD|442292 COG3058, FdhE, Formate dehydrogenase maturation protein FdhE [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
MSIRILPPEQLEQSSGAIPPLLLPNPAKLFARRAARLRQLAEGHPLADYLRFLAALADAQQEALAALPPL
PLPDAAALARAAEHGMPPLDAAGLPRDPAWRELLDALLAALAAAGEAPEPARAALERLRAADEAELEALA
DALLAGDFAGVDAALAPFVWAALQVYWTQLAAQLDAKALAPLGWQRGLCPVCGSLPVASVVRIGGKEGLR
YLHCSLCETEWHMVRVKCSNCESTKKLSYFSLEGEEAAVKAETCDDCHSYLKILYQEKDPQVEPVADDLA
SLALDLLMEEEGFARSGLNPFL
>gnl|CDD|442293 COG3059, YkgB, Reactive chlorine resistance protein RclC/YkgB, DUF417 family [Defense mechanisms]
MTSMKALLQLLARLDRLGIHLLRAGLVIVFLWIGGLKFTQYEADGIVPFVANSPLMSWLYSVFGTYGFSY
LLGVVELTIGLLLALGPWSPKLGLLGGLLAVGTFLVTLSFLFTTPEVWVPSLGGFPALSGAGQFLLKDIV
LLAASLVLLSDSLRRLLARRKA
>gnl|CDD|442294 COG3060, MetJ, Transcriptional regulator MetJ (met regulon) [Transcription, Amino acid transport and metabolism]
AKWNGEYISPYAEHGKKSEQVKKITVSIPLKVLKVLTDERTRRQVNNLRHATNSELLCEAFLHAFTGQPL
PTDEDLRKDNPDKIPAEARELMEEMGIDIEDWEELDD
>gnl|CDD|442295 COG3061, OapA, Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning]
MGRMNPLPRKHRRLLGLLSALLLLALLLPSPDASASRVSQPLVPLALTAEADAPAAAAPAAPAAPEGEWQ
EYTVQSGDTLSQIFRRLGLSASDLYALLAAEGDAKPLSRLKPGQELRFQLDADGQLQALRYEVSRLETLL
FTRQGDGFQRKRVTELSDGSFSADAALASLETLELAAAAGILSDFIAAALDAGAGDAGLVELEIILDDDI
DFADLLFAADRFTGDYFRVYAEGEGGDGGYIGAGGFRAAKFRRRAVRFRRSSSSSSYRRRPHRLSRRRRL
RRGPDAAAPSGSSNAAGGGGHKITRRGGGGGGAAVGVGTGTPTTGAGLGVVRGGRGGGGGVVVGQIGRGG
TYGGTGLHLHKHGHKGGGVVGQGVTIGTLGGTGPTTGPHLHYEFVQNGVRVAPLTVKLPAAPPLAAAAAA
AFKAL
>gnl|CDD|442296 COG3062, NapD, Cytoplasmic chaperone NapD for the signal peptide of periplasmic nitrate reductase NapAB [Posttranslational modification, protein turnover, chaperones]
MSDEMHISSLVVQARPERLEAVAAALAALPGVEVHASSEEGKLVVVIEAESQGALLDTIEAIRALPGVLS
VSLVYHQFEEEEELEE
>gnl|CDD|442297 COG3063, PilF, Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]
LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALEKALKLDPNNAEALLNLAELLL
ELGDYDEALAYLERALELDPSALR
>gnl|CDD|442298 COG3064, TolA, Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]
AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAE
LAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEE
RKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAA
AADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV
VAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAA
AAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVEL
RVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADLLLLGG
>gnl|CDD|442299 COG3065, Slp, Starvation-inducible outer membrane lipoprotein Slp [Cell wall/membrane/envelope biogenesis]
MLSRLMRLLLLLLAALLLAGCATVPEAIRGASPTPLSLSAVLAAPEAYVGQEVRWGGVIVSVENLEDRTR
LEVVAYPLDSSGRPDLGDPSQGRFLARVPGFLDPADYAKGRLVTVVGTVTGSETGKIGEAPYRYPVVDAD
GYHLWPVRQQVVYPYYYDPYYWGYGPGPGYGW
>gnl|CDD|442300 COG3066, MutH, DNA mismatch repair protein MutH [Replication, recombination and repair]
MLLITPPQSEQELLERAQALAGLTLGELAAQAGIPVPANLKRDKGWVGQLLELALGATAGSKPEQDFPHL
GIELKTIPIDAQGKPLETTFVCVAPLTGNSGLTWETSHVRHKLSRVLWIPVEGERDIPLAERRIGSPLLW
SPSAEEEAILRQDWEELMELIVLGRVEEITARHGEVLQLRPKAANSKALTEAIGEEGEPIKTLPRGFYLK
KSFTAQILARYFLLP
>gnl|CDD|442301 COG3067, NhaB, Na+/H+ antiporter NhaB [Energy production and conversion, Inorganic ion transport and metabolism]
MSLGRAFAKNFLGQSPDWYKLTILAFLIINPILFFTVGPFVAGWLLVAEFIFTLAMALKCYPLQPGGLLA
IEAVLIGMTSPEHVYHEVEANLEVILLLMFMVAGIYFMKQLLLFVFTKLLLGIRSKILLSLAFCLAAAFL
SAFLDALTVTAVIISVAVGFYSVYHKVASGKGFHDDHDHTDDDHVDELHREDLEQFRAFLRSLLMHAAVG
TALGGVMTMVGEPQNLIIAEQAGWDFGEFFLRMAPVTIPVLICGLLTCVLLEKFKWFGYGAKLPESVRQI
LADFDREEDAKRTKQDRAKLIVQAIIAVWLIVGLALHLAEVGLIGLSVIILATAFNGVTDEHAIGKAFEE
ALPFTALLVVFFAVVAVIIDQHLFTPIIQWVLSLEGEQQLAMFYLANGLLSMISDNVFVATVYINEVKAA
LDAGTITREQFDLLAVAINTGTNLPSVATPNGQAAFLFLLTSALAPLIRLSYGRMVWMALPYTIVLTLVG
LLAVEFLL
>gnl|CDD|442302 COG3068, YjaG, Uncharacterized conserved protein YjaG, DUF416 family [Function unknown]
LKNPIFKRLEKLEPWQQLAFMAALCERMLPNYQLFCEATGFGDAKVYRNILDLVWESLTVKKAKINFDRQ
LEKLEEIIPDAEDFDSYGVYPAIDACVALSELLHSLLDGDLEEAVEVSQLSLGTVAAFIEAQEGEELSDE
ELKEHPLMQDELDFQWELLRLLEECEERDIELIKGLRALAREEGVSNIGISL
>gnl|CDD|442303 COG3069, DcuC, C4-dicarboxylate transporter DcuC [Energy production and conversion]
MMGLIIALVVVILVGYLIIKKYNAQLVLLLAGLLLLLIAVILGLGPILPAKKSTGSVFFDIFEAIKKLMS
SRLAGLGLIIMALGGFAAYMDHIGASDALVRLLTKPLKKIKSPYLLLPLAFILGQLLSLAIPSAAGLAAL
LMATLYPVLVRLGVSPAAAAAVIATTAGIDLGPGSGDNVLAAELAGMDVMDYFFGYQLPISIPTILVVAV
LHYFVQRYFDKKEGYVAEAEEEEDEAKEEESKAPLFYALLPILPLVLLLVFSKLVIPSIKLDVVTAMLIS
LFIALLIERIRKRDAKKVFAGTKVFFDGMGKAFASVVGLIVAAGVFAAGLKAIGAIDALISSAQSSGLGG
IIMMLVMVLITFLAAILTGSGNAAFFAFAELVPPIAAKFGINPVALGLPMQLAAGLGRTMSPVAGVVIAV
AGIAGVSPFEVVKRTAIPMIVGLIVVLVLTLILF
>gnl|CDD|442304 COG3070, TfoX, Transcriptional regulator of competence genes, TfoX/Sxy family [Transcription]
MASSEELVERVRELLAPLGPVTARRMFGGYGLYVDGKMFALVSDDELYLKADEELREAFEAAGCEPFTYE
KRGRPVTLGYYLVPEELLDDPDELLEWARLALEAALRAKPKKKK
>gnl|CDD|442305 COG3071, HemYx, Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown]
MRRLLWLLLLLAAAVLLAALLEGLLALAEGRYARAEKLLSKAAEHSEAPLLAYLLAARAAQALGDYERRD
EYLAQALELAPEAELAVLLTRAELLLDQGQAEQALATLEALRAGAPRHPQVLRLLLQAYRQLGDWEELLE
LLPALRKHKALSAEEAQALERRAYLGLLRQAARDAEALKALWKALPRAERRDPELAAAYARALIALGDHD
EAERLLREALKRQWDPRLVRLYGRLQGGDPAKQLKRAEKWLKKHPNDPDLLLALGRLCLRNQLWGKAREY
LEAALALRPSAEAYAELARLLEQLGDPEEAAEHYRKALALALG
>gnl|CDD|442306 COG3072, CyaA, Adenylate cyclase, class I [Signal transduction mechanisms]
PDLDDGMRKDLKTLRQRFLALNQLRLERALSAMSSRQQQVLDLLPLLFHYNHPLLPGYVSGDVPAGIANF
TPDKRQLQALQRLARSFDYKQRAQHEPPILGLYLMGSTGSIAQSESSDLDIWVCHDPDLDAEARALLQQK
CELIEQWAASLGVEVHFFLMDENRFRHGERESLSGENCGSAQHLLLLDEFYRTAILLAGKRPLWWLVPPE
EEHNYDEYVQTLLAKGFINPDEWLDFGGLGTIPAEEYFGAGLWQLYKGIDSPYKSVLKLLLLEAYSSEYP
NTQLLSLEFKQAVYAGELDLDELDPYVMMLRRVTRYLLERNDLKRLELVRRCFYLKVNEKLSRPPRERSK
SWRRELLERLVREWGWSEERLALLDNRAQWKIEQVREERNELVDELMQSYRNLIQFARRNNISSSISPQD
IGILGRKLYAAFERLPGKVTLINPGISPDLSEENLTFIQVPEGRANRAGWYLYNQSLTPADIIGRQPLKY
SRSLVELVAWCYFNGLLTASTRLHLHPGGSDLDEYELQQLVADLRQHFPVPLPAPSNEALSRPCEIRHLA
LFINLGVDPTAHLSRRGIHFDSSRSDALSFGGARENLVGSIDLVYRNSWNEVRTLHFEGDDALLDALKTL
LGKMHQDAAPPPSIDVFCYSQTRRGAIANRVEQLFNECISLRLGGTRQPNRRYLLRVAGQYYGLFFERRG
VSVQKLENAVDLYRALSENKLSYSPLVLDRHALEDHPLPPVIDSFASEGLIQFFFEDNGDGFNIYILDEN
NSLEIYRQCEGDKEELLRPLNRFYRSSQDRRTYGSSFINFNLPQFYQIVRNDGGELQVEPFRSPLAASDA
NYYEVQAIGDEGDDSLFEFYCDCQEFESLELEGDLLLVAAVAILLRRRRRRPYPYYITDDDLLSALELDE
QLEQQTVQTLQYLKYLEALE
>gnl|CDD|442307 COG3073, RseA, RseA, negative regulator of sigma E activity [Signal transduction mechanisms]
MNEMQKEQLSALMDGELDELEDRRLLDALAQDAELRQTWARYHLIGDVLRGELLAVLSLDFAARVAAALA
DEPTVLAPAAAPEARKLRRWLRPLGQVAVAASVALVAVVGVQQYNGPGDAAPVLATVPVSGSASPVSLAV
PSQVLEQDRRLNAYLQAHQQRAGANA
>gnl|CDD|442308 COG3074, ZapB, Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning]
MSLELLEELEAKVQQAVDTIELLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQERIR
SLLGKIDEV
>gnl|CDD|442309 COG3075, GlpB, Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]
MKFDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAGQSALHFSSGSLDLLGYLPDGEPVADPFDALADLPEQ
APEHPYSLLGADAVREALAQFEALLGDAGLPYQGSTDRNHLRVTPLGTLKPTWLSPASVPAGPLSDWRKI
LVVGIEGFLDFQPQLAADNLKRAGFEVRAVTIDFPGLDNPSEFRAVNIARVLDDPENREALAEELKPLAG
GADAVGLPAVLGLDDSAAVLAELEQALGVPVFELPTLPPSVPGIRLHDALRRAFEQAGGRIMPGDPVVRA
EAEDGRVTAVYTRRNHGDIPLRADHVVLATGSFFSGGLVADRDRIREPVFDLDVPQPEDRYDWYRDDFFA
PQPYLRFGVATDARLRPLAKGGPVFENLYAAGAVLGGYDPIREGCGAGVALATALHAAEQILAEA
>gnl|CDD|442310 COG3076, RraB, Regulator of RNase E activity RraB [Translation, ribosomal structure and biogenesis]
PSELEEQQEETREIIEALLEDGSDPDALYTIEHHFSFEDFDKLEKAAVDAFKLGFEVTDAEELELEDGET
LFCFDIISESELDAELIDAQVEQLLPLAEKFGVEYDGWGTYFED
>gnl|CDD|442311 COG3077, RelB, Antitoxin component of the RelBE or YafQ-DinJ toxin-antitoxin module [Defense mechanisms]
MMATANVNVRIDEELKEEAEAVLEELGLTPSDAIRMFLKQVVREGGLPFELKLPNAETLAALEEARKGKG
EPRFDSVDELFE
>gnl|CDD|442312 COG3078, YihI, Ribosome assembly protein YihI, activator of Der GTPase [Translation, ribosomal structure and biogenesis]
MSRPKKTRKIGKIMPAAPKGKRKTREELDQEARERKRKKKHKGLKAGSRQNEAEKQKKNNQQKQAKDPRI
GSKKPVPLGVEENAPAKVKKPKPKEEKKPKLSPEQELAKLENDERLDALLDRLEAGETLSAEDQAWVDET
LDRIDELMEELGIEDDDDEEEEEKQEDLLRLLKRGDPKDFK
>gnl|CDD|442313 COG3079, YgfB, Uncharacterized conserved protein YgfB, UPF0149 family [Function unknown]
NTLPDYDELADLLQQLGLGVSPAELHGLLCGLLCGGARLDDESWLALLLDLLNDGEALPEELLAALTELY
EQTLEQLADDDFSFELLLPDDDAPLFERADALAEWCQGFLLGLGLAGPKLSKLSEEVQEALRDLAEIAQL
DYDEDEDDEEDEQALEEVVEYVRVAALLLFEELGPPPPPAEDKPTLH
>gnl|CDD|442314 COG3080, FrdD, Fumarate reductase subunit D [Energy production and conversion]
MMNRNPKRSNEPIFWGLFGAGGMVSALVGPVLILITGILVPLGILPADALSYERVHAFAQNWLGKLVLLG
VIALPLWHAAHRIHHTLHDLGIHAGTAGKLVCYGVAALGSVLAAILLLTI
>gnl|CDD|442315 COG3081, NdpA, dsDNA-binding nucleoid-associated protein YejK/NdpA [Replication, recombination and repair]
MSMAISHIILHQLEKEEEEGQATLVLRDSELPVDEAVEELLEELHRAYNAKSGKGYGRFSDDEEESPFAA
LLRDYLEGELDFVAFSQQAAEQLKLELDKYPFAEGGYLLFAHYQLLATDYLLIALLKHKEGVTVDEELEL
SETEYLDLSKLDLAARIDLTEWQTGPESNRYLSFIKGRGGRKVSDFFLDFLGCEEGVDAKAQTQQLLQAV
EDYCEQEQLDKEERQEYRKKVYEYCKEQDKAGEPVALEELSEELDEENPEAFYEFVREQDYELEEEFPPD
RRTLKKLTKFSGSGGGLSISFDSKLLGERIFYDPETDTLTIKGLPPNLKDQLKRRLKED
>gnl|CDD|442316 COG3082, YejL, Uncharacterized conserved protein YejL, UPF0352 family [Function unknown]
PIQSKYSDKQVEKLLNDLIAVLEKHKAPVDLSLMVLGNMVTNIINTSVPPAQREALAEKFAQALKSSVKT
>gnl|CDD|442317 COG3083, YejM, Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms]
LISWGHWFALFNILLALLIGSRYLFIADWPGTLLGRLYLLVSWLGHFSFLVFALYLLLLFPLSFLVPSQR
LFRGLSVILATAGLTLLLVDTEVFQRFHLHLNPLVWDLLFNPDQGELARDWQLLFIPVPLIFLLEMLLAT
WSWRKLRSLERRRFGKPVAALFLVSFLASHLIYIWADANFYRPITMQRANLPLSYPMTARSFLEKHGLLD
AQEYQQRLEEQGNPEASSLNYPLHPLQFSDPAKPPNILLIVVDSLRADMLDPEVMPNLYAFAQRSLRFTN
HYSSGNSTRAGLFGLFYGLPGNYWDSILAERTPPVLIDALQQQGYQFGLFSSAGFNSPLFRQTIFSDVSL
PRLHTPGGPAQRDRQITAQWLQWLDQRDSDRPWFSYLFLDAPHAYSFPADYPKPFQPSEDCNYLALDNES
DPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQNYWGHNSNFSRYQLQVP
LVIHWPGTPPQVISKLTSHLDIVPTLMQRLLGVQNPASDYSQGEDLFDPQRRRDWVLAGDYRNLAIITPD
RITVLDPSGNYQVYDRDYRPLKDAKPPLGLLLQVLTELKRFYA
>gnl|CDD|442318 COG3084, YihD, Uncharacterized conserved protein YihD, DUF1040 family [Function unknown]
MKCHRLNELIELLQPAWQKEPDLNLLQFLQKLAEEAGFDGPLSELTDDVLIYHLKMRGSDKDEMIPGLKK
DYEDDFKTALLRARGIIKD
>gnl|CDD|442319 COG3085, YifE, Uncharacterized conserved protein YifE, UPF0438 family [Function unknown]
KMTESFLSTKRFFDDKHFPRGFSRSGDFTIKEAQLLERYGHAMKALESGEREPETEEEQRFVAVCKGERE
PESEFEKVWLKYLKRINRKKRFHTLSGSPPQADSEDDYSDSDDDDD
>gnl|CDD|442320 COG3086, RseC, RseC, positive regulator of sigma E activity [Signal transduction mechanisms]
MIEETGTVVAVEGGTAWVETQRKSACGSCAAKSGCGTGLLSKLFPSKEHRLEVPNPLGLKVGDRVEVGIP
ESSLLKAALLVYLLPLLGLLLGALLGQALGPGGSELLAALGGLLGLALGFLLARRLSRRLAKKSKYQPVI
LRILPPSSV
>gnl|CDD|442321 COG3087, FtsN, Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning]
PETALAAILLAAAALLLELSAEAAAAASDNLRLAAGSAAAPALAEDALVASAAKAGLAETGAKAGAILAA
AALAALNAAAAALAAASAAAAAAAAPAAAAAEAAAAPAGMAKKEAAAAPAAKKPYYVQVGAFRSRANAER
LRARLALLGLEARVVEVEVGGGTWYRVRVGPFSSRAEAEKAREKLKAAGIDALVVRVK
>gnl|CDD|442322 COG3088, NrfF, Cytochrome c-type biogenesis protein CcmH/NrfF [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
MRRLLLLLALLLAAPAAAVIPDEQFDDPALEARARELSKELRCPVCQNQSIADSNAPLARDLRREVRERL
AAGKSDEEIVDYMVARYGEFVLYKPPLKGATLLLWLGPFLLLLLGLGVLVRFLRRRRAAAAAAPLSAEEQ
ARLAALLKE
>gnl|CDD|442323 COG3089, YheU, Uncharacterized conserved protein YheU, UPF0270 family [Function unknown]
MIIPWQQLSPETLDNLIEEFVLREGTDYGEQEVSLEQKVAQVRRQLKRGEAVIVFDELHESVNIMPKEQF
RALGRQ
>gnl|CDD|442324 COG3090, DctM, TRAP-type C4-dicarboxylate transport system, small permease component YiaM [Carbohydrate transport and metabolism]
LRLLKRLLDRLERLEEALAALLLAAMVLLVFAQVVLRYVFNSPLPWTEELARYLFVWLVFLGAAYAVRRG
GHIRVDLLVDRLPPRARRVLDLLALLLVLAFLALLAWYGWELVLRSWERGQTSPALGIPMWWVYLALPVG
FALMALRLLLRLLRLLRGREPELAEEEE
>gnl|CDD|442325 COG3091, SprT, Predicted Zn-dependent metalloprotease, SprT family [General function prediction only]
PIMLQQELQRRVEQILQLAEEYFGRPFPHPEVRFNLRGTTAGRAHLQSHEIRLNPKLLEENGEEFLIEVV
PHELAHYHLYQEFGRVRPHGKEWRELMEKVGGLPPRRTHRFDVSSVQGKRYLYRCACGQHQLSRRRHNNV
LRGARYRCRKCGGKLKLVE
>gnl|CDD|442326 COG3092, YfbV, Uncharacterized membrane protein YfbV, UPF0208 family [Function unknown]
MGFFKTLKDGQRYMKTWPVEKKLAPIFPENRVIKATRFAIKFMPPLAVFSLVWQYALGGPEQLPQAVATA
LFALSLPLQGLYWLGKRANTPLPPSLLSWYREIRQKLIEAGIALAPVVAKPTYQELADLLKRAFKQLDKA
FLDDL
>gnl|CDD|442327 COG3093, VapI, Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense mechanisms]
MNKRNPIHPGEILREEFLEPLGLSQTELAKALGVSRQRISEILNGKRAITADTALRLARAFGTSAEFWLN
LQAAYDLWLARQKAGEE
>gnl|CDD|442328 COG3094, SirB2, Uncharacterized membrane protein SirB2 [Function unknown]
MMYLALKHLHLTLVALSILLFILRGLWMLRGSALLQARWVRILPHIIDTLLLLSGIGLAVILHQYPFTAP
WLTAKLIGLIAYIVLGTVALKRGRTKAVRWLAFLLALLVFAYIVAVALTKQPLLFL
>gnl|CDD|442329 COG3095, MukE, Chromosome condensin MukBEF, MukE localization factor [Cell cycle control, cell division, chromosome partitioning]
SSTNIEQFMPAKLAQAIANPLFPALDSQLRSGRHIGIDELDNHAFLMDFQDELELFYRRYNVELIRAPEG
FFYLRPRSTTLIPRSVLSELDMLVGKVLCYLYLSPERLANEGIFSLQELYEELLSLADESKLLKLVNQRS
TGSDLDKQKLQEKVRTSLNRLRRLGMVTFVGNDSSKFRISESVFRFGADVRSGDDPREAQLRLIRDGEAV
TLEQELSLQDTLDEELDSEEEEEEEQAEDEEE
>gnl|CDD|442330 COG3096, MukB, Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning]
IERGKFRSLTLVNWNGFFARTFDLDELVTTLSGGNGAGKSTTMAAFVTALIPDLTLLHFRNTTEAGATSG
SRDKGLHGKLKPGVCYAALDVVNSRGQRLLVGVRLQQVAGRDKKVDIKPFIIQGLPEDVKPTDLLTETLD
GRQARVLPLNELKEKAEELEGVQFKQFNSITDYHAFMFDLGVTPKRLRSSSDRSKFYRLIEASLYGGISS
AITRSLRDYLLPENSGVRKAFQDMEAALRENRMTLEAIRVTQSDRDLFKHLITEATNYVAADYMRHANER
RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIE
RYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ
ALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVER
SQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA
ELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTA
AMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVLLSEIYDDVTLEDAPY
FSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRYS
RFPEVPLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAA
LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAQA
FIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLG
ENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQAD
AEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAV
LRLARDNDVERRLHRRELAYLSADELRSMSDKALGALRLAVADNEHLRDALRLSEDPRRPERKVQFYIAV
YQHLRERIRQDIIRTDDPVEAIEQMEIELARLTEELTSREQKLAISSESVANIIRKTIQREQNRIRMLNQ
GLQNVSFGQVKGVRLNVNIRETHAQLLDALSEQQEQHQDLFFSNRLTFSEALAKLYQRLNPHIDMGQRSP
QTIGEELLDYRNYLELEVEVNRGADGWLRAESGALSTGEAIGTGMSILLMVVQSWEEESRRLRGKDISPC
RLLFLDEAARLDAKSIATLFELCERLDMQLLIAAPENISPEKGTTYKLVRKVFNNQEHVHVVGLRGFGQE
>gnl|CDD|442331 COG3097, YqfB, Uncharacterized conserved protein YqfB, UPF0267 family [Function unknown]
MPNDITFFERFEPDILAGRKTITIRDESESHFKPGQILRVGTYEDDRYFCTIEVLSVTPVTLDELTEEHA
RQENMTLDELKQVIREIYPGEDQLYVIEFKLV
>gnl|CDD|442332 COG3098, YqcC, Uncharacterized conserved protein YqcC, DUF446 family [Function unknown]
MTMHDQVAQLLLQLEAALRALGLWQSEPPSPEALASTQPFCVDTLSFEQWLQWVFIPRMRALLEAGQPLP
TRFAIAPYAEEALKGRPPGVAPLLALLRQLDALLSGESA
>gnl|CDD|442333 COG3099, YciU, Uncharacterized conserved protein YciU, UPF0263 family [Function unknown]
SMDLMNLLSEDELIDTAYDIFLELAADNLDPADILLFNLQFEERGAVELVDPGDDWEEEVGFDVDPEEFA
EVWIGLVNEEDEIDDVFARILISRDPDEKFCHILWKR
>gnl|CDD|442334 COG3100, YcgL, Uncharacterized conserved protein YcgL, UPF0745 family [Function unknown]
MLCAIYKSPKKDETYLYVEKRDDFSRVPEALLQMFGKPEFVMDLLLTPERKLARADAEKVLAALEEQGFY
LQMPPPEENLLKDHL
>gnl|CDD|442335 COG3101, EpmC, Elongation factor P hydroxylase EpmC (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis]
MTHQYQDLIELFNQCFAESYNTRLVKGDDEPIYLPADEECPYHRIVFAHGFFASALHEIAHWCIAGEERR
LLEDYGYWYCPDGRDAEQQAEFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGDAEPDREAFKRAVHAQV
LRYLEQGLPERAARFIQALAAFYGTPLPLTAADFPLPELL
>gnl|CDD|442336 COG3102, YecM, Uncharacterized conserved protein YecM, predicted metalloenzyme [General function prediction only]
SAKFIEELQDLFADLPRFEQKIQQLAQRLGLDLSQYQADHIALRCNQNATAERWRQGLLQCGTLLSENEI
NGRPICLFELHQPLQVGPWQIDCVELPYPGDKHYPHEGWEHVELVLPGDPETLVEQWVPRALALLPDLLS
PGIKLKTSSPKGEGERLPNPTLAVTDGGVTIKFHPYSIKEIVASEQA
>gnl|CDD|442337 COG3103, YgiM, Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only]
AAAETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRYSNGKTGWVSSRYLTVTPSAR
ERLPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYRGTGWV
>gnl|CDD|442338 COG3104, PTR2, Dipeptide/tripeptide permease [Amino acid transport and metabolism]
TTSAPQRTFFGHPKGLYTLFFTEMWERFSFYGMRAILVLYLTASLADGGLGLSEADAAAIYGAYTALVYL
TPLLGGWLADRLLGQRRAILLGGILMALGHFLLALPGGVTLFYLGLALIAVGNGLFKPNISSLVGQLYDP
GDPRRDAGFTIFYMGINIGAFLAPLLCGYLGEKYGWHYGFGAAAIGMLIGLIIFLLGRKYLGDIGLEPDN
PLSKKERLIAVALGALLLVLVLAGLLSNANIANYLLYVIAIIAYFIFILRSKKLTKEERKRLLAILILFL
FSIVFWALYEQAGTSLNLFADRNVDRSLFGFEIPPSWFQSLNPLFIIILAPVFAALWTKLGKRGKEPSTP
TKFALGLLLLGLGFLVMALAALLAGAGGKVSPLWLVLAYLLLTIGELCLSPVGLSMITKLAPARFAGQMM
GLWFLATALGNLLAGLLAGLYAVPGYTAYFLLLGGIALVAGVVLLLLSPKLRRLMHGVE
>gnl|CDD|442339 COG3105, YhcB, Uncharacterized membrane-anchored protein YhcB, DUF1043 family [Function unknown]
MESMIWLYAIIGLVVGIIIGFLLMRLLNRKVRQQQKLEQELDEAKAELEQYRQEVNEHFARTAELLDNLA
QDYRKLYQHLAKSAERLLPDEPEKDNLFAASLTELELSNDESPPEEPPRDYAPGASGLLSEEYGLEKKP
>gnl|CDD|442340 COG3106, YcjX, Ras-like GTP-binding stress-induced protein YcjX, DUF463 family [Signal transduction mechanisms]
DEALKALQDELADLANRLLDRHLRLAVTGLSRSGKTAFITSLVNQLLHGGSGARLPLFSAAREGRLLGAK
RVPQPDLAVPRFDYEEHLAALTGEPPQWPESTRGISELRLAIRYRSASGLRRHLGETATLYLDIVDYPGE
WLLDLPLLEQSYAEWSQQQLALLQRPPRAELAKPWLAALATLDPAAPADEATLARLAAAYTDYLHACKAE
LGLSLLQPGRFLLPGDLEGAPALQFFPLPGLDPLAAAPKGSLYAMLERRYEAYKQHVVKPFYRDHFARFD
RQIVLVDCLQALNAGPEAFADLERALTQILESFRYGKSSLLSRLFSPRIDKLLFAATKADHVTPDQHDNL
ESLLRQLVQEAIRRAEFEGAEVDTMALAAVRATREGTVEHGGETLPAIRGTPLAGGEEVALFPGEVPERL
PDADFWQEQGFRFPRFRPPPLELDAGLPLPHIRLDRALQFLLGDKLA
>gnl|CDD|442341 COG3107, LpoA, Outer membrane lipoprotein LpoA, binds and activates PBP1a [Cell wall/membrane/envelope biogenesis]
MLPILTKRTSVSRLLLLLLLALLLAGCASTSTAPQTPAADLQGEATASAEYYLQQAEQSQPEEKADYQLL
AARALLQEGQLAQARALLAQLPPQQLSPEQQLEYQLLLAELALAQGDPEAALALLSQLSLASLSPEQQAR
YYQLRAQAYEQQGDPLAAARARIALEPLLTDGQARQENQDQIWQLLSQLPPAQLQSLAINADEPVLQGWL
ELALIYRQNGGDPDQLQQALNDWQQRYPQHPAAKLLPTELQQLLALQPAQPKKIALLLPLSGRLAPAGQA
IRDGFLAAYYADLSAGGSRPQLRFYDTNSADIAALYQQAQQDGADFVIGPLLKENVDALAALPSLPVPTL
ALNQPDDPRAPPNLYQFGLSPEDEARQAAERAWQDGHRRALVLAPDGSWGDRVAEAFAQRWQQLGGQVVD
VQYYDPQADLSQAIKSLLGIDQSEARIRQLKRLLGLSLEFEPRRRQDIDAIFLVATPEQARLIKPQLDFH
YAGDLPVYATSRSYSGNPDPDQDRDLNGVQFSDMPWLLDPNPPLRQQLEQLWPNADGSLARLYAMGVDAY
RLAPRLNQLRQIPGYRLNGLTGTLSLDPDGRIERQLSWAQFRNGRPVPLP
>gnl|CDD|442342 COG3108, YcbK, Uncharacterized conserved protein YcbK, DUF882 family [Function unknown]
MTRSLLSRRAFLRAAAALALKRLNFFLRDWRTNEVAPIDPRLLDLLWALRRRLGSPEPIQIISGYRSPAT
NAMLRRRSRGVAKNSLHMLGKAADIRIPGVSLSQLRRAALALGRGGVGYYPRSGFVHVDTGPVRSWGG
>gnl|CDD|442343 COG3109, ProQ, sRNA-binding protein ProQ [Signal transduction mechanisms]
MENTQKPKKLESPKEVIAYLAERFPACFDLEEPKPLKIGIFQDLAARLPDDELSKTQLRRALRRYTRSWR
YLKAVKEGAQRVDLDGNPAGEVTEEHAEHAREQLAERKAKVAARRAAEQAAKAAAAKAAKPKKPAAERRM
LEKLAALKVKFGK
>gnl|CDD|442344 COG3110, YccT, Uncharacterized conserved protein YccT, UPF0319 family [Function unknown]
MKLRLALAALLALLLSASAFAATLKLPPDIELLVVDGQKVSSSLLKGADSLELDNGEHQLVFRYSKIVRS
GGDRRLYTSDPLIVTFDAENGQDLTISLPKLENEREAKAFAKDPQVTLVDKNGQPIPAKQDVLKQEGFQL
GRDYEKELAEYNAAGGPASVAAFAAAPAATATQLAQANAPVVTAQSENDAEQMLQYWFQQADKETRKRFL
IWAKQ
>gnl|CDD|442345 COG3111, YdeI, Predicted periplasmic protein YdeI with OB-fold, BOF family [Function unknown]
MKKTLALAALLALASAPAFAADGGFKGPPSAQDGGFTGPSDAAVTTVAQALAMRDDAWVTLEGNIVKQLG
DDKYLFRDATGTIKVEIDDKVWNGQTVTPKDKVRISGEVDKDWNKVEIDVKRIQK
>gnl|CDD|442346 COG3112, YacL, Uncharacterized conserved protein YacL, UPF0231 family [Function unknown]
MDYEFRRDLTGQVRARFSMGHEALGRWLNEEVGGDLAKLDELLAAIDQLKGSERQEWQLIGKEYSLLLDR
DEVMVRANQLAFEEDEELEEGMSYYDEESIAFCGLEDFEELLQAWQEFIQTR
>gnl|CDD|442347 COG3113, MlaB, Binding protein subunit MlaB of the ABC-type intermembrane phospholipid transporter Mla, contains STAS domain [Cell wall/membrane/envelope biogenesis]
MSEALLWNAEGGTLRLSGELTRDTVLALWAQLLALLAAGGAVEIDLSGVTRVDSAGLALLLELLREARAQ
GKTLRLTGVPEQLRTLAALYGLDELLP
>gnl|CDD|442348 COG3114, CcmD, Heme exporter protein D [Intracellular trafficking, secretion, and vesicular transport]
MQFDSWSEFFAMGGYGFYVWLSYGITLLVLLGLVLLPRRRRRRLLKELRRRQRREQRIKAARQQE
>gnl|CDD|442349 COG3115, ZipA, Cell division protein ZipA, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning]
QELRLILIILGAIAIAALLLHGLWRSRKERRSSFRDKPSKRDVLLDDDGIGEVRVVAAEAPERVEPEASF
DAEDEVREPDQEEVDPLLDDEADIEAAPAEPVRWAGTAAAVEPAPEQEAYEEAGPAGESAEQEDAPAEEP
EAEAPAEEALAAELCAEPEEVIVLNVVAREGQPFAGEDLLQALEQAGLRFGEMGIFHRHLDPDGSGPVLF
SLANMVKPGTFDPDNMEDFSTPGVSLFMQLPGPGDALQAFDLMLETAQRLADELGGVVLDDQRSPLTPQT
IEHYRERIREFERRMRLA
>gnl|CDD|442350 COG3116, FtsL, Cell division protein FtsL, interacts with FtsB and FtsQ [Cell cycle control, cell division, chromosome partitioning]
MTRAGKLLLLLLLLVLASALAVVYSRHQSRQLFAELERLQAERDQLEVEWGRLQLEQSTLAAHSRIERIA
REKLGMRLPTPAQTVVVK
>gnl|CDD|442351 COG3117, YrbK, Lipopolysaccharide export system protein LptC [Cell wall/membrane/envelope biogenesis]
MSKRLRRLLLLLLLLLLALLTWWLEQPEPPPPAAVQPHEPDYTAENFTLTRFDADGRLSYRLTADKMEHY
PDDDTTELTNPVLTLYDEDGPPWTITADRGKLNKDGKELYLYGNVVVTRLAGAGPALTLTTEELTVDPDT
QDASTDDPVTITGGGSTITGVGMRANLRTQTLELLGNVRGTYE
>gnl|CDD|442352 COG3118, CnoX, Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones]
AVVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGV
RSIPTLLLFKDGQPVDRFVGALPKEQLREFLDKVL
>gnl|CDD|442353 COG3119, AslA, Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]
MKRLLLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSP
VCSPSRASLLTGRYPHRTGVTDNGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYLTDLLTDKAIDF
LERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPLPPNLAPRDLTEEELRRARAAYAAMIEEVD
DQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALV
SLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTGRWKLIRYYDDDGP
WELYDLKNDPGETNNLAADYPEVVAELRALLEAWLKELGDPPL
>gnl|CDD|442354 COG3120, MatP, Macrodomain Ter protein organizer, MatP/YcbG family [Replication, recombination and repair]
MKYQQLENLEAGWKWKYLVKKHREGENITRYIEQSAAQEAVQQLLTLENEPVKVLEWIKEHMNPALDNRL
KQTIRARRKRHFNAEKQHTRKKSIDLEYLVWQRLSALAQRRGMTLSETIVQLIEEAERKEKYASQMSSLK
QDLKALLKK
>gnl|CDD|442355 COG3121, FimC, P pilus assembly protein, chaperone PapD [Extracellular structures]
MKRLLRLLLLALLLLLASAAAAAGISISPTRVIYPAGDKEASLTLTNTGDTPYLVQSWVDDWDQDAGPDK
ATAPFVVTPPLFRLEPGKSQTVRIIRTGPPLPQDRESLFRLNVDEIPPKDASEEGKNTLQIALRTRIKLF
YRPAGLKGSPEDAAEKLTWSLVGNGLTVTNPGPYYVTLSDLSLGAGGKKLKKGLGMVLPGSTRRWPLPAG
ASLAAGGKVTWATINDYGGAVPLEATL
>gnl|CDD|442356 COG3122, YaiL, Uncharacterized conserved protein YaiL, DUF2058 family [Function unknown]
MANSLQDQLLKAGLVDKKKAKKAKKEKRKQRKQARKKGAEAVDEAKAAAERAQAEKAERDRELNRQRQAE
AERKAIAAQIRQLIEQNRLNRKDGEIAYNFTDGGKIKRIYVTAAQRKQLAAGRLAIVRLDGRYELVPAAV
AEKIAERDPSAVVLLNDASEAEPDEDDPYADYQIPDDLMW
>gnl|CDD|442357 COG3123, PpnP, Pyrimidine/purine nucleoside phosphorylase YaiE/PpnP, UPF0345/DUF1255 family [Nucleotide transport and metabolism]
QFDNVTVMKKANVYFDGKVKSRTFIFADGSKKTLGVMLPGEYTFGTGAPEIMEVVSGELEVKLPGSDEWQ
TYAAGESFEVPANSSFDLKVAEPTAYLCS
>gnl|CDD|442358 COG3124, AcpH, Acyl carrier protein phosphodiesterase [Lipid transport and metabolism]
MNFLAHLHLSGDDPSSLLGNLLGDFVKGKPYEHYPPDIQAGIRLHRRIDSFTDSHPLVREARQRFRPEYR
RYAGIILDIFFDHFLARHWSQYSDEPLEEFAQRAYALLEQNLPILPERFQRLLPYMIQEDWLESYAELEG
IERALNGMSRRLRRPNPLAGAVEELEEHYDELEQDFLQFFPDLMAFAKQKLSELSE
>gnl|CDD|442359 COG3125, CyoD, Heme/copper-type cytochrome/quinol oxidase, subunit 4 [Energy production and conversion]
MSHHHHHEGASHGSLKSYLIGFVLSVILTAIPFWLVMTGALSPGTTLAVILGLAVVQIVVHLVYFLHMNT
SSEGRWNLLALIFTVLIVVIVVGGSLWIMYHLNYNMMPG
>gnl|CDD|442360 COG3126, YbaY, Uncharacterized lipoprotein YbaY [Function unknown]
MMKRLLLLLAGLAAALALAGCADKSAAAAAAAAQATVTGTVTYRERIALPPDAVLTVTLEDVSLADAPAK
VLAEQTIEPAGQVPFPFSLPYDPADIDPGHRYAVSARITVDGRLLFITDTAYPVLTDGAGKPVDLVLVPV
PR
>gnl|CDD|442361 COG3127, YbbP, Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport and catabolism]
MSSLRLALRLAWRDLRAGELRLLLLALVLGVAAVAAVGSFSDRLQAGLARQARELLGGDLVLRSDQPLPA
AWLAQARALGLRVSRTVEFRSMARAGDGSQLVEVKAVDGAYPLYGELELAPAPPLADALAGGPAPGEVWV
DPRLLARLGLKVGDTIRLGDATFTIAGVLTREPDRGGGGFSLAPRVLINLADLEATGLIQPGSRVRYRYL
VAGPDADLEALRAWLEPALPAGQRVRTVEDARPELGRALDRAEQFLLLVALLALLLAGVAVANAARRYVA
RRLDTIALLRCLGASRRQIFRIYLLQLLLLGLLGSLLGLLLGALLQALLAALLADLLPVPLEPALSPLPL
LLGLLVGLLVLLLFALPPLLRLRRVPPLRVLRRDLEPARPRAWLALLLALAGLAALALWLSGDLRLALIF
LGGLLVALLLLALLAWLLLRLLRRLPRRLGPALRLALANLHRPPARTAAQVLALGLGLMLLLLLALVRGD
LLASWQAQLPEDAPNYFLINIQPDQVDAFRAFLAAQGVAALELYPMVRGRLVAINGQPVAELAYDDDRAR
WVLRREFNLTWSATLPEGNRLVAGEWWPALDAGEPLVSVEEGLAERLGLKLGDTLTFNVAGREVTATVTS
LRKVDWDSMRPNFFVVFSPGALEGAPATYITSFYLPPAAEAALLRALVRAFPNVTVIDVDAILDQVRDIL
DQVSLAVEFLAGFALLAGLLVLAAALAASRDERTREAALLRTLGASRRQLRRALALEFALLGLLAGLLAA
LLAELAGWALARFVFDLPFSPPWWLWLAGLLGGALLVLLAGLLGARRVLRQPPLEVLREE
>gnl|CDD|442362 COG3128, PiuC, Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction only]
LLHIPNVLTPEEVAQIRALLAAAEWVDGRVTAGWQAAQVKNNLQLPEDSPLARELGELVLAALGRNPLFF
SAALPLRIFPPLFNRYEGGMHYGNHVDNAIRGLPGTGQRVRTDLSFTLFLSDPDEYDGGELVIEDTYGEQ
SVKLPAGDMVLYPSTSLHRVTPVTRGERLASFFWIQSMVRDDAQRELLFDLDQAIQSLRARGGDDPEVDR
LTGVYHNLLRMWAEV
>gnl|CDD|442363 COG3129, RlmF, 23S rRNA A1618 N6-methylase RlmF [Translation, ribosomal structure and biogenesis]. 23S rRNA A1618 N6-methylase RlmF is part of the Pathway/BioSystem: 23S rRNA modification
LHPRNRHRGRYDFPALIKSCPELAPFVFLNPYGDESIDFANPKAVKALNKALLKHFYGIKHWDIPDGYLC
PPIPGRADYIHYLADLLAESNNGVIPTGKKIKVLDIGTGANCIYPIIGNREYGWRFVGSDIDPVALASAQ
KIIDANPGLKGKIELRLQKNPKNIFKGIIKPGERFDLTLCNPPFHASAEEAAAGTQRKLKNLGKKKAKKP
VLNFGGQSNELWCEGGELAFIKRMIKESKQFAKQVLWFTSLVSKKENLPPLYKALKKLGATEVKTIEMAQ
GQKQSRFVAWTF
>gnl|CDD|442364 COG3130, Rmf, Ribosome modulation factor [Translation, ribosomal structure and biogenesis]
MKRQKRDRLERAYQRGYQAGVTGRSKELCPYQGDVARSAWLGGWREGREDRWDGLTG
>gnl|CDD|442365 COG3131, MdoG, Periplasmic glucan biosynthesis protein OpgG [Cell wall/membrane/envelope biogenesis]
MDRRDLLKSAAALAALAAPALAAPAAAPAAAAGAAQPFSFDTLVERARALAAKPYVPPPPPLPDALAALD
YDQYRAIRFRPDRALWRGDGLPFELQFFHLGFLFKEPVRINEVEDGQAREIPFDPDLFDYGKDSPAPALP
GDLGFAGFRLHYPLNRPDYKDELAVFLGASYFRAVGRGQQYGLSARGLAIDTALPGGEEFPRFTEFWLER
PAPGADSLTVYALLDSPSVTGAYRFVIRPGEETVMDVEATLFPRKDVERLGIAPLTSMFLFGENDRRRFD
DFRPEVHDSDGLAIWTGNGEWIWRPLNNPPRLQVSSFADENPRGFGLLQRDRDFDHYQDLEARYERRPSL
WVEPLGDWGKGAVQLVEIPTDDETNDNIVAFWVPEAPPKAGQELSFAYRLHWGADPPVPPPLARVVATRT
GRGGVPGQPRPPGARKFVVDFAGGPLAALPADAPVEAVVSASRGEISNVVVEPNPETGGWRLAFDLDPEG
AEPVELRAFLRLGGQPLSETWLYQWTPPA
>gnl|CDD|442366 COG3132, YceH, Uncharacterized conserved protein YceH, UPF0502 family [Function unknown]
MMLPPLSPLEARVLGCLIEKEVTTPDQYPLSLNALVTACNQKSNRDPVMNLSEAEVQDALDELRAKGLVR
EVSGFGSRVAKYEHRFCNVLKLSPQELALLCLLLLRGPQTPGELRTRTERLHEFADVSEVEAVLEELAER
EGPLVVKLPRAPGKRESRYAHLLSGEVDLAALAAAAAAPAAESSALEARVAALEAEVAELRAELAELRAE
LGA
>gnl|CDD|442367 COG3133, SlyB, Outer membrane lipoprotein SlyB [Cell wall/membrane/envelope biogenesis]
MKKLLLAAALLAALLLAGCANSSYSGDVYSRGQARQVQTVEYGTVVSVRPVTIQGSNSGLGTVGGAVLGG
VAGSQVGGGRGRALATVAGAVAGGVAGNAIEKGVTRTQGVEITVRLDNGETIAVVQEADPQFRVGQRVRV
VGGGGTTRVSPR
>gnl|CDD|442368 COG3134, YcfJ, Uncharacterized conserved protein YcfJ, contains glycine zipper 2TM domain [Function unknown]
MKKSLLVGAVLAALAAAGAAAAAGYAAADSFPDYARVVSVTPIYETVRTPRQECWDETVTERAPVQDGNS
IAGTVIGAIAGGVLGNQVGGGSGRKAATAAGAVAGGYAGNQIQGNMQRGDTYYRTVRRCETVYDYEERLV
GYDVTYRYNGREYTTRMDYDPGDRIRVRVSVTPADS
>gnl|CDD|442369 COG3135, BenE, Predicted benzoate:H+ symporter BenE [Secondary metabolites biosynthesis, transport and catabolism]
MARSLLRDLSLSAVSAGFVAVLVGYTSSFAIVFQAAQAAGATPAQAASWLWALGLGMGLTSIGLSLRYRM
PIVTAWSTPGAALLATSLAGGSLPEAVGAFLVAGLLILLTGLTGLFGRLMARIPAPIAAAMLAGVLLRFG
LAAFTALATAPLLVLPMLLVYLLGRRLAPRYAVLAALLVGLAVAALQGQLHLSALALALAAPVFVTPEFS
LSALLGLALPLFLVTMASQNLPGIAVLRAAGYRPPVSPLITVTGLASLLLAPFGGHAINLAAITAAICAG
PEAHPDPARRYIAAVAAGVFYLLLGLFAGTVVALFAALPAALIAALAGLALLGTIGGSLAAALADEKERE
AALVTFLVTASGVSLFGIGSAFWGLVAGLLALLLLRRRRRR
>gnl|CDD|442370 COG3136, GlpM, Dual-topology membrane protein YdgC, GlpM family [Function unknown]
MGLLLKALLGALVVVLIALLSKTKNYYIAGLVPLFPTFALIAHYIVGSERGVEALRTTILFGMWAIIPYF
AYLLALYYFIGRMRLPLALAGAVLCWLVAAWVLILLWTRFHG
>gnl|CDD|442371 COG3137, YdiY, Putative salt-induced outer membrane protein YdiY [Cell wall/membrane/envelope biogenesis]
MKKRLAAALALALLLASAAAAAQIPNGPAEEKKGWSGSAELGASATSGNTDSTSLNAALRLTYETGDWRH
SLGASALYGESNGVTTAERYFAGAQYDYKLSERFYLFGLARYERDRFSGYDYRATLGAGYGYQLINTDRH
SLSVEAGPGYRYEEYTDGGEDESEAILRLGLDYRWKLTDNASFTQDLSVEPGSDNTRVNSETGLTVKLTG
SLALKLSYTVRYNSDPPPGVKKTDTTTSVSLVYSF
>gnl|CDD|442372 COG3138, AstA, Arginine/ornithine N-succinyltransferase beta subunit [Amino acid transport and metabolism]
LVIRPARPSDLDALLALARESGPGFTSLPPDRERLAARIERSERSFAGEVDEPGEEGYLFVLEDTETGEV
VGTSAIEAAVGLDEPFYSYRVGTLVHASRELGVHNRVETLTLSNDLTGASELCGLFLDPEYRKGGNGRLL
SRSRFLFIAQHRERFADRVIAELRGVSDEDGRSPFWEALGRHFFGMDFAEADYLSGIGNKQFIAELMPKY
PIYVPLLPEEAQAVIGQVHPDTRPALALLEKEGFRYEGYVDIFDGGPTLEARTDDIRTVRESRLLTVAIG
DDAPADGEPYLVANTRLADFRAVLAPADLDGDGQLRLSAEAAEALGVSEGDAVRVVPL
>gnl|CDD|442373 COG3139, yeaC, Uncharacterized conserved protein YeaC, DUF1315 family [Function unknown]
MNFEQLIASMTPEIYERLKTAVELGKWPDGRALTEEQRELCLQAVMLYQARHNPEEQHMGIGPRGEIVCK
SKQELKQQFGDEEEPIARIKPD
>gnl|CDD|442374 COG3140, yoaH, Uncharacterized conserved protein YoaH, UPF0181 family [Function unknown]
MFNGLPALTHEQQQQAVERIQQLMAQGMSSGEAIALVAQEIREEHQGEQVVVRFDDED
>gnl|CDD|442375 COG3141, YebG, dsDNA-binding SOS-regulon protein YebG, induction by DNA damage requires cAMP [Replication, recombination and repair]
AVEIKYVVDRDGEEKMTFTSKKEADAYDKMLDLAENLAELLEQSPVGLDEEQAEELALYLAENKDALAKA
LKGKKLPLSEAEKEAEAAADKKKSTPIKAA
>gnl|CDD|442376 COG3142, CutC, Copper homeostasis protein CutC [Inorganic ion transport and metabolism]
MMLLEVCVDSVEDALAAEAGGADRIELCSALAEGGLTPSYGLIKAAREAVDIPVHVMIRPRGGDFVYSDD
EFEVMLRDIRAARELGADGVVFGALTPDGEIDLERLKRLVEAAGGLPVTFHRAFDVVPDPLEALEQLIDL
GVDRVLTSGGAATAEEGLDLLKELVEQAGGRIEIMAGGGVRPENVPELVAATGVREVHLSARVRVPSSMT
NPGVSMGGEFSRSPTDAEKVRALRAALDAL
>gnl|CDD|442377 COG3143, CheZ, Phosphoaspartate phosphatase CheZ, dephosphorylates CheY~P [Cell motility, Signal transduction mechanisms]
MSLEDAKELVDALEAGDEAAAEQVDELAAAREDELFQEIGQLTRELHDALRELGLDPRLEEAASSEIPDA
RDRLDYVVEMTEQAANRTLNAVEAAQPLQDRLREEAAALLARWQRLFARELSLDEFRELVKDTRAFLGEV
PELTDALRAQLTEIMMAQDFQDLTGQVIKKVVNLLQEVESRLVQLLLEFGPEEEAAPADAREDASLLNGP
QINGEGTDVVSSQDDVDDLLSSLGF
>gnl|CDD|442378 COG3144, FliK, Flagellar hook-length control protein FliK [Cell motility]
ALAQADAEALLAALAALEASASLQAAAAAEKAQVALAAAAAAAAPAAAATALAGAGTAALSASLASAAEA
LAAAETSSAVSAPAALSANASAPSAAAALAAPLGQLSPQWAQQLAQRVQLMANQGVQEAEIRLNPEELGP
LEIKLTVEGGQATAQFVAENAEVREALEAALPRLRQALAEQGLQLGQVSVSQGSSDQQGQQQQQNQQSGQ
GQGRQGGASDEAAAAARGGVDLFA
>gnl|CDD|442379 COG3145, AlkB, Alkylated DNA repair dioxygenase AlkB [Replication, recombination and repair]
TLFDDPRPENLELPDGGAVYLPGFLSPEEADALLAALRAEAPWRQPVIPIFGKTMSVPRLNAWYGWVGAG
YRYSGTDPEPPPWPPALLALKRRVEAAAGFPFNSCLLNLYRDGQDRMGWHQDDEEELGFNPPIASVSLGA
TRRFRFGHKERKDPTRSLPLEHGDLLVMGGPTQLAWQHGVPKTKKGTGPRINLTFRRIGP
>gnl|CDD|442380 COG3146, COG3146, Predicted N-acyltransferase [General function prediction only]
DLTIRVLSSIAEIPAAAWDALAGPDNPFLRHAFLSALEESGSVGPRTGWQPQHLTLWDDGRLVAAAPLYL
KSHSYGEYVFDWAWADAYERAGLRYYPKLLSAVPFTPVTGPRLLVAPGEDEAALRAALVAALRQLARRNG
LSSLHVLFPDEDEAAALEEAGLLLRLGVQFHWHNRGYADFDDFLAALSSRKRKNIRRERRKVAEAGITIR
TLTGDEITEADWDAFYRFYQDTYDRKWGSPYLTRAFFELLGETMPDRVLLVLAERDGRPIAGALNLRGGD
TLYGRYWGCLEEVPFLHFEACYYQGIEYAIAHGLQRFEPGAQGEHKLARGFLPVPTYSAHWIAHPGFRQA
VADFLERERAAVAAYIEELNEHLPFRKG
>gnl|CDD|442381 COG3147, DedD, Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning]
PAEEAAAAPAAAAAPAAPAAAAAPAPAAAAAAAAPKPAAKPAAPKPAAAAAAAPAAKAAAPAGGGWVVQL
GAFSNEDNAKELVAKLRAAGYPAYTEPVTTGGGTLYRVRVGPFASRAEAEAALAKLKKLTGLKGFVVRYK
>gnl|CDD|442382 COG3148, TapT, tRNA U47 aminocarboxypropyltransferaseTapT/TuaA/ YfiP, DTW domain [Translation, ribosomal structure and biogenesis]
RSMARGSRVPRCPRCLLPQSLCLCALIPPLDTRTRVLLLQHPKEAKKPKNTGRLIALSLPNTELFVGERF
EPDPALLALLADPQRQPYLLFPGEDAAPLRVVAPPAAGKPPLLILLDGTWRKARKMFRLSPWLDALPRLS
LPPPPPSRYRLRKAPREGQLSTLEAAALALALLEGPEAAQPLLAAFDAFVERYLAGRGRRPRERNRRASR
R
>gnl|CDD|442383 COG3149, PulM, Type II secretory pathway, component PulM [Intracellular trafficking, secretion, and vesicular transport]
MNALLERLKAWWQQLSPRERRLLLAGAAVLLLALLYLLVWQPLLRAREQAQAQLAALQAQLAWMQQQAAE
AQALRASPGGAAPAGGSLLQAVDRSARRAGLTLTRLQPQGDRVQVWLDQVPFDALLRWLAELEQQYGVRV
EELDLERADAPGLVSVRLTLERGGA
>gnl|CDD|442384 COG3150, YcfP, Predicted esterase YcpF, UPF0227 family [General function prediction only]
TMLLYLHGFNSSPQSAKAQLLAAYFAEHGPDIEFICPQLPPSPAAAIAQLEALIAGLPGEPLALIGSSLG
GFYATWLAERYGLRAVLINPAVRPARLLADYLGEQTNYYTGERFELTPEHLDELRALEVPPLTRPERYLL
LLQTGDEVLDYREAVAKYAGARQTVEEGGDHAFSGFERYLPAILAFLGLA
>gnl|CDD|442385 COG3151, yqiB, Uncharacterized conserved protein YqiB, DUF1249 family [Function unknown]
MMSLLRPRYVPDLAALMALCEANYARLLRLLPDLDEVGDSYVSSVGGGLDLHLEVLERSPYTTTLELTQL
FPDLPGLPDPDLTVRLYHDARLAEVLSCQQIRRLQPRYGYPNPKMHQLDEKWQLNRFLGEWLDYCLRQGH
SFTSL
>gnl|CDD|442386 COG3152, yhaH, Uncharacterized membrane protein YhaH, DUF805 family [Function unknown]
EAYKRFFKKYFSFSGRASRSEYWWFVLFNLLVSLVLAILDALLGSSGAILLGLLAALYALALLIPSLALT
VRRLHDTGRSGWWLLLLLIPFIGIIVLLVLLFLPGTPGPNRYGPDPKA
>gnl|CDD|442387 COG3153, yhbS, Predicted N-acetyltransferase YhbS [General function prediction only]
IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGPALLL
GPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDEVFLAK
EL
>gnl|CDD|442388 COG3154, UbiT, Ubiquinone biosynthesis accessory factor UbiT, lipid carrier SCP2 domain [Coenzyme transport and metabolism]
TRLVPRLPALLALPLRLLPFPPLSLLLAALLNRLLRRPLLFGRLDFLEGRRLRIEVTDLPLRFLLTLDDG
RLRVVRAAGEADVTISGPLADLLLLAARKEDPDTLFFQRRLVIEGDTELGLALKNLLDAAELDLLPGPLR
RLLRRLARFVERGLALPRPAA
>gnl|CDD|442389 COG3155, ElbB, Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms]
KKVAVILSGCGVYDGSEIHEAVLTLLALDRAGAEYQCFAPDIEQHHVINHLTGEEMGEKRNVLVESARIA
RGNIKPLAELNAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAFHEAGKPIGAICIAPALL
AKLLGAGVKLTIGNDADTAAAIEAMGGEHVECPVDEIVVDEENKVVTTPAYMLAASISEAAEGIEKLVKK
VLELA
>gnl|CDD|442390 COG3156, PulK, Type II secretory pathway, component PulK [Intracellular trafficking, secretion, and vesicular transport]
MSRRRRRQRGVALITVLLIVALLAALAAALAERQRLELRRAENLLDRQQARWYALGAEALARARLADDAK
DNVDHLGEPWAQPLPPFPLDGGEVSGRIRDEQGCFNLNALVDPDGEVNPYAQQVFRRLLEALGLDEYEAE
ALADAIVDWIDSDDLPRPGGAEDDYYLALGPPYRPANGPFASVSELRLVKGMTPELYARLAPYVTALPGD
TKINVNTAPPEVLAALLGGLSLDDAQALLAARPEKGFADVADFLALLGLAGLDLLKDQLTVSSDYFLLEA
TVRLGDGRLRLRSLLQRSGGGGVTVLR
>gnl|CDD|442391 COG3157, Hcp, Type VI protein secretion system component Hcp (secreted cytotoxin) [Intracellular trafficking, secretion, and vesicular transport]
MAVDAYLKIDGIKGESTDKGHEGWIEVLSFSHGVSQPTDGTTSSGGGRGAGKRSHSDLTFTKEIDKASPL
LYKACASGKHLKKAELKFYRANGGKEEEYLTITLENVIISSVSPSGSGGEGTPLETVSLSYAKITWTYTP
QDADGGIGGEVTDGWDLKANKK
>gnl|CDD|442392 COG3158, Kup, K+ uptake protein Kup [Inorganic ion transport and metabolism]
MTSAASPASHGKKSLAALALGALGVVYGDIGTSPLYALKEAFSGAHGLPVTPENVLGVLSLIFWSLILVV
SVKYVLFVMRADNRGEGGILALMALAQRALGDGPRRRAVLVLLGLFGAALFYGDGVITPAISVLSAVEGL
EVATPALEPYVVPITLVILVGLFAVQRRGTARVGKLFGPIMLVWFLVLAALGLVHIVQHPEVLAALNPLY
AVAFFLEHGWIAFLALGAVVLAVTGAEALYADMGHFGRRPIRLAWFFLVLPALLLNYFGQGALLLADPEA
IENPFFLLAPDWALLPLVILATLATVIASQAVISGAFSLTRQAIQLGYLPRLRIRHTSEEEEGQIYIPAV
NWLLLVAVLLLVLGFRSSSNLAAAYGIAVTGTMLITTLLAFVVARRLWKWPLWLALLVLGFFLVVDLAFF
AANLLKIPDGGWFPLLIGAVLFTLMTTWKRGRRLLAERLREDALPLDEFLESLEKSPPVRVPGTAVFLTS
DPDGVPLALLHNLKHNKVLHERVVLLTVVTEDVPRVPPEERVEVEDLGDGFWRVTLRYGFMETPDVPRAL
ALCRKQGLKFDPMDTSFFLSRETLVPSKKPGMARWREKLFAFMSRNAASATDFFRIPPNRVVELGTQVEI
>gnl|CDD|442393 COG3159, YigA, Uncharacterized conserved protein YigA, DUF484 family [Function unknown]
LTEEDVAAYLLAHPDFFERHPDLLAALRLPHPHGGAVSLVERQLERLRERNRRLEDRLRELIAIARENEA
LFNRLHRLVLALLEARSLDDLLAALADSLREDFGVDAVALRLFSDAADLPGLPLALPVSAALRAFAGRLG
GGRPYCGRLRGPEAALLFGDAAAEVGSVALIPLGLGGPLGLLALGSRDPQRFQPGMGTLFLEFLAEVLSR
ALRRWLER
>gnl|CDD|442394 COG3160, Rsd, Regulator of sigma D [Transcription]
MLNQLESAQERWGGVHELIDRWLEERQQLLVAYCKLAGLKPFKEDLTALDEKALQRFCQLLVDYLSAGHF
EIYERIIEEAEGFGDGALALAEQLYPRLEATTEQALDFNDKYDEADIDDDNLLELDQDLSRLGEALEERF
ELEDQLIELLHNSHAEAVAA
>gnl|CDD|442395 COG3161, UbiC, 4-hydroxybenzoate synthetase (chorismate-pyruvate lyase) [Coenzyme transport and metabolism]. 4-hydroxybenzoate synthetase (chorismate-pyruvate lyase) is part of the Pathway/BioSystem: Ubiquinone biosynthesis
MSIALALLAPHWQPAPPLLSQLPPALRDWLLTDGSLTRRLEALTGGPFSVEVLRQGFVPADADEAPLLGL
PAGERVLVREVLLRGDGQPWVYARSVIPLSTLPGAWRELLRLGNRPLGELLFADPELRRDPLEVGRLEPA
HPLARRGLAAPGPLWARRSRFRLGGPPLLVTEVFLPA
>gnl|CDD|442396 COG3162, YjcH, Uncharacterized membrane protein, DUF485 family [Function unknown]
MSTPEEDYERIQASPEFQELVRRRRRFAFPLTAIFLVWYFGFILLIAFAPGFLATPVGGVITVGIPLGLG
QFVSTFVLTGIYVRRANREFDPLAEEIREEVEKG
>gnl|CDD|442397 COG3164, YhdR, Uncharacterized conserved protein YhdP, contains DUF3971 and AsmA2 domains [Function unknown]
MSKPLRRLLRRLLRILLLLLAVLLVLLALLLSLLRLLLPLLDDYRPQLEAWLSQALGVPVTIGSLSASWQ
GLGPVLELRDVRLLDPDGRPALRLPRVELALDLWRSLLHGRPRFRRLTLDGLQLDLRRDADGRWSVAGLP
VSGGGDGDDLDALLDWLLQQGRFSLRDSRLRWLDPSRGPPLTLSIVNLRLRNGGRRHRLEGRASLPAALG
GPLDLRADLRGPDPGDWRGWSGQLYLQADDVDLAPWLPRDLPDNLGLQSGRGSLRAWLDLRDGRLTSATA
DLALSDLSLRLAEDLPPLALQRLSGRLRWQRQGDGWQLDLPDLRLATDGQAWPLGDLSLRWQPAAGQGEE
LRLRADRLDLAALAPLLPLLPLLPPALRELLAALQPRGRLRDLRLDWPLEAPERYRLSARLQDLSWQAWG
GLPGVSGLSGTLSGDEQGGRLTLDSQDATLDLPGVFREPLPLDRLSGRLAWQRDGDGWRLSSDDLRLANA
DLAGSGRFRLQLPLGDGPPVLDLLAGLSRADAAAAWRYLPLPAMGEDLRDWLDGAIVAGQVDNATLLLRG
DLADFPFDPNEGVFQVYADLRDATLDFQPGWPALTDLDGDLLFDNNGLEIRADSGRLLGVRLSNVTARIP
DLSADKPVLTIDGDASGPGADVLDYLQQSPLADSLGGALDELQASGPVSLDLKLDIPLDGGGDVKVDGDV
RLANNDLRLKPLDLTLTQVRGRLRFTEGGLSAEGLQARLLGGPVTLSIATGGQAGDGQVRVDLSGRASAA
GLRAWLPLPLPLLRRLSGSAPWQAELSIPLPGGGQYELTLTSDLKGLALDLPAPLGKAAGEALPLRLEVS
GDPESFRDRLDLSLGDLLNARLLLDKGGGRLLRGALALGSGAPPLPPAPGLSVSGRLPELDLDAWLALLS
ALAGDASGSASPLLPTRIDLRADQLDLGGQTLHDVRLSARRQGGGWRLQLDSPELAGTLTWPPAAGAGPL
RARLDRLHLPALEASEAGSAAGEPLADADVDPRSLPALDLVVDDLRLGGRDLGRLELEARPDGDGLRLDK
LRLDSPDARLTGSGDWRQDGGGSRTRLKGKLDSKDLGKLLARFGYPSPIRGGSGKLDGDLSWPGSPWQFD
LASLSGSLSLDLGKGQFLKVEPGAGRLLGLLSLQSLPRRLTLDFSDVFSKGFAFDSIRGSAQIADGVART
DDLLIDGPAADVLMSGSADLVRETLDLRVVVTPEISASLPLAAAFAGNPVVGAAVFAAQKVLGDPLDKIT
SIRYRVTGSWDDPKVTEVSRFPKEAAAPA
>gnl|CDD|442398 COG3165, UbiJ, Ubiquinone biosynthesis protein UbiJ, contains SCP2 domain [Coenzyme transport and metabolism]
LLPPLLLAALETALNRLLALDPAARARLARLAGKVLRLELTELSLPLYLVFSEDGLDVLGAWEGEADCTL
TGSLSALLRLADAQDLTALIASGELRIEGDAQLAQQLSRLLDQLDWDWEEDLSRYVGDVAAHRLAQGARK
LLRWLRRAARRLQQNLAEYLTEESRLLPGRLEVADFADEVDALRDDVDRLEARLARLEAKLAAS
>gnl|CDD|442399 COG3166, PilN, Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]
MIRINLLPWREERRKRRKRRFLALLVLALLLALAVLFLVYLYLQGQIAQQQARNAALQQEIAKLDKQIAE
IKELKKQKAELLARLQVIEQLQQSRPPWVHLLDELARLLPEGVWLTSLSQQGGTLTLTGVAQSNARVAEF
MRNLEASPWFSDVELVEIEAKDDGKGLVSFTLTVKLKRPAEEEEA
>gnl|CDD|442400 COG3167, PilO, Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]
MALDLNNLDLREIGSWPLPVKILLLLLLVLLVLALGYFFLISPQLEELEELEAEEAQLKQELEKKQAKAA
NLPALKAQLEELEQQLGELLKQLPSKAEVPALLDDISQAALGSGLEFELFKPGPEVPKEFYAELPISIRV
TGTYHQLGAFVSDVANLPRIVTLHDITISPAKDGSGTLSMEATAKTYRYLDEEEAAAQEAAA
>gnl|CDD|442401 COG3168, PilP, Type IV pilus assembly protein PilP [Cell motility, Extracellular structures]
MRLLLLLLLLLLLSGCGDSDLDDLEQWVAEVKARPKGPIEPLPEIKPYEPFVYSAAGLRDPFSPPKLEAA
QEAAAKGSGLQPDLNRPKEPLEAYPLDSLKMVGTLGKGGGLWALIRAPDGSVYRVKVGNYLGQNFGRITA
ITEDEIELREIVPDGAGGWVERPATLALQEK
>gnl|CDD|442402 COG3169, COG3169, Uncharacterized membrane protein, DMT/DUF486 family [Function unknown]
PPILLTILLLILSNVFMTFAWYGHLKFLKSKPLWIAILISWGIAFFEYCLQVPANRIGYGVFSLAQLKII
QEVITLVVFVPFAVLYLKEPLKWNHLWAFLCILGAVYFIFRK
>gnl|CDD|442403 COG3170, FimV, Type IV pilus assembly protein FimV [Cell motility, Extracellular structures]
MKRALLASSAYALGLGELTVQSALGEPLRAEIELTDVSAEEADSLRVRLASAEAGLRFAVERRADGRPVL
RVTSSRPVNEPFLDFLVEVNWPSGRLVREYTLLLDPPAYAAAAAAPAAAPAPAPAAPAAAAAAADQPAAE
AAPAASGEYYPVRPGDTLWSIAARPVRPSSGVSLDQMMVALYRANPDAFIDGNINRLKAGAVLRVPAAEE
VAALSPAEARQEVQAQSADWAAYRARLAAAVEPAPAAAAPAAPPAAAAAAGPVPAAAEDTLSPEVTAAAA
AEEADALPEAAAELAERLAALEAQLAELQRLLALKNPAPAAAVSAPAAAAAAATVEAAAPAAAAQPAAAA
PAPALDNPLLLAGLLRRRKAEADEVDPVAEADVYLAYGRDDQAEEILKEALASEPERLDLRLKLLEIYAA
RGDRAAFEALAAELYALTGGGRALDPDNPLYAPGAAAAAEDAPAAEAEDDSPAEEPAASAAAAAELGDEE
GARELLEEVLAEGNDALL
>gnl|CDD|442404 COG3171, YggL, Uncharacterized conserved protein YggL, DUF469 family [Function unknown]
MAKNRSRRLRKKLHVDEFQELGFEVSWTFPEGTSEEQIDAFVDAFIDEVIEPNGLAFGGSGYLQWEGLVC
LQRYGSCTEEDRALVEAWLEARPGVKDVEVSELFDAWYDE
>gnl|CDD|442405 COG3172, NadR3, Nicotinamide riboside kinase [Coenzyme transport and metabolism]. Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis
PEVRPSFVKKIVLLGAESTGKTTLARALAAHYNTPWVPEYGREYLEEKGRALTYDDLLAIARGQLALEDA
AAKRANKLLFCDTDALTTKVYSELYFGKCPPWLEALAAQRRYDLYLLLDPDIPWVADGLRDGPEVREEFQ
QLLREELEERGIPYVVISGDYEERLEQALAAIDELLAK
>gnl|CDD|442406 COG3173, YcbJ, Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only]
EELDEAALRALLAAQLPGLAGLPEVEPLSGGWSNLTYRLDTGDRLVLRRPPRGLASAHDVRREARVLRAL
APRLGVPVPRPLALGEDGEVIGAPFYVMEWVEGETLEDALPDLSPAERRALARALGEFLAALHAVDPAAA
GLADGRPEGLERQLARWRAQLRRALARTDDLPALRERLAAWLAANLPEWGPPVLVHGDLRPGNLLVDPDD
GRLTAVIDWELATLGDPAADLAYLLLYWRLPDDLLGPRAAFLAAYEEATGDLDDLTWWALADPELAALGR
RALE
>gnl|CDD|442407 COG3174, MgtC, Membrane component of predicted Mg2+ transport system, contains DUF4010 domain [Inorganic ion transport and metabolism]
MDLLAPLLELLLRLAIALAIGLLIGLEREWSKRGEEEGSRFAGIRTFALIGLLGGLSALLAEELGPWLLA
VGLLAVALLLAVAYLRKARQEGDPGLTTEVALLLTFLLGALAVLGDPLLAVALAVVVTLLLALKEELHGF
ARRLSEEELRAALKFLLLSLVILPLLPNRPIGPWGALNPREIWLMVVLISGISFVGYVAVRLLGARRGLL
LTGLLGGLVSSTATTLSLARRARENPALSRLAAAGILLASAVMFLRVLVIAAVVNPALLPALAPPLLAAA
VVGLAVALLLWRRSKREAEDVEPELGNPFELKTALKFGLLFAVILLLSAAAQEWFGDAGLYALAAISGLA
DVDAITLSLARLAADGSLSATTAAIAILLAALSNTLVKAGLAAVIGGRRLGRRVALGLLLALAAGLAALL
LLG
>gnl|CDD|442408 COG3175, COX11, Cytochrome c oxidase assembly protein Cox11 [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
MSDAQPLRRRNRRLVLKLLLVVVGMFGFGFALVPLYDVFCEVTGINGTTQRAAAAANSQVDLSRTITVRF
DANVNPGLPWEFKPEQRSVTVHPGETATVFYEATNLSDRPIVGQAIPSVTPGQAGAYFNKIECFCFTEQT
LAPGETVEMPVVFYVDPELPKDVKTITLSYTFFDVTGPAAAAAAAAAAA
>gnl|CDD|442409 COG3176, COG3176, Putative hemolysin [General function prediction only]
LIAARSSPLGRLLIRLLERLLGLGRLNRLYDQYARTPAELRGAQFLRYVFEELGARLEVPEGDLDRIDAD
GHLLVVANHPLGILDGLALLKLVGTVRPDYRILANDLALRIPGGFYSELEFPVDPFNLETLKAARRHLLE
GGRSCVFPAGRVSGARRVIDLLWSGLAAKLARKAGAPVVPVYFDGRNSGLFYLFGSIHPTLRTAALPREL
LRKRGHLIELRVGRPIPPLELDLDLDPAELPPLLRGYTYALGADPDFNTADVRLNPRYRR
>gnl|CDD|442410 COG3177, COG3177, Fic family protein [Transcription]
TPELLKLLAEADEALGRLDGLPEELRELLRKLLIEEAYASSAIEGNTLTLDEVRSLLEGGLTGGPPLRDE
REVLNYVEALEYLLELLRGEPLTEELILELHRILLKGLRGEDKEPGEYRTGQVGIGAVYVPPPPEEVPEL
MEELLDWLNEEDELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGLLSQPLLPLSRIIEEDR
DEYYDALEAVRETGDLTPWIEFFLEAILEAAEEALALLERLLELARGRLNERQRKLLELLFENPVLTASE
LAELLGVSRRTARRDLKDLVELGILEKVGGGRNTRY
>gnl|CDD|442411 COG3178, COG3178, Predicted phosphotransferase, aminoglycoside/choline kinase (APH/ChoK) family [General function prediction only]
MDDREAALRAFLARALGWADATLEPLAGDASFRRYFRLTLGDRSAILMDAPPEKEDVRPFVAIARLLRAA
GLSVPEILAADLEQGFLLLEDLGDTTLLDALDAGENADELYRAAIDALARLQAAPAPADLPPYDEALLLR
ELDLFPDWYLPRHLGLPLDDAERAELEAAFEALLDSLLAQPRVLVHRDFHSRNLMVLPDGRPGLIDFQDA
VLGPPAYDLVSLLRDAYVDWPEELVEALLDRYLAAARAALPPFDFAAFLRAYALMGLQRHLKILGIFARL
ALRDGKPGYLADIPRVLRYLRRVLAHYPELAPLARWLDELVLPALQV
>gnl|CDD|442412 COG3179, GH19, Chitinase, GH19 family [Carbohydrate transport and metabolism]
GFLITEAQLRAIFPGASFALAQGYAPALNAALPEFGITTPLRLAHFLAQIAHESGGLRYLEENLNYSALQ
VFGRYPDGAPEAIANRVYGGRKDLGNTAPGDGWRYRGRGLIQLTGRANYRAAGDALGLDLVNNPDLLADP
EVAARSAAWFWATRGLNALADAGDFGEVTRRINGGLNGLDDRRARYQRAKAVL
>gnl|CDD|442413 COG3180, AbrB, Uncharacterized membrane protein AbrB, regulator of aidB expression [General function prediction only]
MSRRPPSLLRWLLTLALAAAGGLLFSLLGLPAPWLLGPMLAVALAALAGAPLRLPRRLRNAGQAVLGVMI
GSSFTPEVLAQLARWWPSLLLLTVLTLALSLLGGWLLRRLGGLDRATALLGSAPGGLSEMVALAEEYGAD
VRLVALMQYLRVLLVVLLVPLVARLLGGGGAGAAAALGPAAPPLSLLGLLLLLALALAGGLLGRRLRLPA
GALLGPLLLSAALHLTGLVTAALPPWLLAAAQVLIGWSIGLRFTRETLRELLRLLPAALLSTLLLIALCA
LFAWLLALLTGLDLLTALLATAPGGLDEMAIIALALGADVAFVTAHQLLRLLLVLLLAPLLARLLARRRP
RR
>gnl|CDD|442414 COG3181, TctC, Tripartite-type tricarboxylate transporter, extracytoplasmic receptor component TctC [Energy production and conversion]
MKTTRRALLALAAALALALAAAAAAAAAYPSRPIRLIVPFAAGGGTDIVARLLAEKLSKALGQPVVVENR
PGAGGTIGAAAVARAAPDGYTLLLGSSGTLAINPALYKKLPYDPLKDFTPVALLATDPLVLVVNPDSPAK
TLAELIAAAKANPGKLNYGSSGVGSSDHLAGELFKKAAGIDMTHVPYKGGGPALTDLLGGQVDAMFDSLS
EALPQIKAGKLRALAVTSPERSPALPDVPTLAEAGLPGFEASSWRGLFAPAGTPPAVVAKLNAALAKALA
DPEVRERLAALGLEPVGSTPEEFAAFIAAEIARWGEVIKAAGIK
>gnl|CDD|442415 COG3182, PiuB, PepSY-associated TM region [Function unknown]
SSLRKLLRRLHLWLGLLAGLFLLILALTGALLVFKPEIDRWLNPELLAVAPGGPPLSLDELLAAARAAYP
GARVTSITLPAEPDRAARVRVRDPEGEGRTVYVDPYTGEVLGTRDEGSTFFRFLYRLHRSLLLGDTGRLI
VGLAALLLLVLLISGLVLWWPRRRRWKDFFTFRWGAGGRRFWLDLHNVLGVWALPFLLVIALTGLVWSLA
DWLRAALAALGGGTPAAEAEPPASASAPAGAPPLSLDAALAAARAALPDAEPRRISLPGDPGGVYTVRGR
DPGELTPRGRDTVYFDPYTGEVLAVRDFADYSAGAKLLEWLYPLHTGRFGGLPGRILYFLLGLALALLIV
TGLLLWWKRRRKKRAPPAARAPRLVLLVG
>gnl|CDD|442416 COG3183, COG3183, Predicted restriction endonuclease, HNH family [Defense mechanisms]
DLEEPKGFTEGAKKEVTHKRYERNPKLRKKAKEHAGGKCEVCGFDFEFVYGELGEGYIEVHHLIPLSEIG
EGGVDPIEDLVPLCPNCHRMLHRGRPPLSIEELKKLLKRRKA
>gnl|CDD|442417 COG3184, COG3184, Uncharacterized conserved protein, contains DUF2059 domain [Function unknown]
MKKILAALLLALLLAAAPPAFAQDSPAHLAAARKLLELTGAEKMFDQMLPQLAEQLKQQLAQANPELWKD
LDEVVQEKALALAARRDELEDEMAPIYAKHFTEEELKAIIAFYESPAGKKLLEKMPALMQESMQAGQQWM
QKLAPELMARLQEELKERGAAKP
>gnl|CDD|442418 COG3185, HppD, 4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only]
LDGIEFVEFAVGDAEQLAFLLEALGFTLVARHRSKAVTLYRQGDINFVLNAEPDSFAARFAREHGPGVCA
IAFRVDDAAAAYERALALGAEPFEGPGPGELRIPAIRGIGGSLHYFVDRYGYGGIYDPDFEPLPGDAAPA
GAGLTRIDHIGIAVPRGDLDEWVLFYEDVLGFEEIREEDIEDPYQGVRSAVLQSPDGKVRIPLNEPTSPD
SQIAEFLEKYRGEGIQHIAFATDDIEATVAALRARGVRFLDIPDNYYDDLEPRVGAHGEDVAFLHPKGIL
VDRDTGGVLLQIFTKPVGGTFFFELIQRKGGEGFGEGNFKALFEAIEREQIRR
>gnl|CDD|442419 COG3186, PhhA, Phenylalanine-4-hydroxylase [Amino acid transport and metabolism]
METNAQLARDPAYLARYTDPQGYIDYTAEEHAVWRRLYRRQVALLPGRACDEYLDGLEKLGLPADRIPQL
DEVNERLKALTGWRVVAVPGLIPPDAFFELLANRRFPVATFIRTPEEIDYLPEPDIFHEVFGHVPLLTNP
VFADFLQAYGEAGLKASKLDSELALLARLYWFTVEFGLIGTPEGLRIYGAGILSSPGESEYALESDEPNR
IPFDLERVMRTPYRIDIYQPTYFVIDSFDQLFEVLEEDFAALYDRAKFAPAFPPGGLLGGDKVIARGTG
>gnl|CDD|442420 COG3187, HslJ, Heat shock protein HslJ [Posttranslational modification, protein turnover, chaperones]
ASAAAPLAGTEWVLVSIDGKPVPDGRPPTLTFDEDGRVSGSAGCNRFSGSYTLDGGTLTFGPLASTRMAC
PDALMELEQAFLAALEAVASYRIDGDTLTLTDADGKELLR
>gnl|CDD|442421 COG3188, FimD, Outer membrane usher protein FimD/PapC [Cell motility, Extracellular structures]
RSRRRRLALLLLLLLALAAAAAAAAVEFNPAFLDGDDAAAIDLSRFSRGNYVPPGTYYLDVYVNGQPLGR
GDITFVADRDDGRLQPCLTPELLEQLGLKLDALPALLAADGQCVDLSAIPGASVRFDFATQRLDLSVPQA
ALPYQARGYVPPSLWDDGIPALLLNYDLNASRSRGRSGSASESRYLGLNSGLNLGAWRLRNNSSYSYSSG
GGSGWQRLDTYLQRDIPALRSQLTLGDSYTSSDWFDSVRFRGVQLASDFRMLPDSLRGYAPVVRGIAASN
ATVTVRQNGYVIYQTTVPPGPFEINDLPPTGGAGDLDVTVTEADGREQTFTVPFASVPQLLRPGLSRYSL
AAGRYRRNGSFDYGPPFAQGTLRYGLSNGLTLYGGAEAAEDYQAGGLGAGFNLGALGALSADVTQSRARL
PDDDTGSGQSYRLGYSKSFDETGTNFSLAGYRYSTRGYRDLSDALDARDSGGDNSSYRPRSRFQATLSQS
LGDGGSLYLSYSQQDYWDGSGRTRSYSLGYSNSLRNISYSLSASRSRNGGGRRDRSVSLSLSIPLGNRSS
ASYSLSRDNGGGTSQQVGLSGSAPEDGGLGYSLSAGYGSGGDGNSGSANLSYRGSYGTLSAGYSYSRGYR
QVSAGASGGLVAHAGGVTLSRRLGDTFALVDAPGAAGVPVNNERGGRTDRRGYALVPYLTPYRRNRVSID
PLDLPDDVELDNTEQRVVPTRGAGVLVRFPTRRGRRALLTLRDADGKPLPFGAEVTDEGGQEVGIVGQDG
QVYLSGLPPQGTLTVKWGDGAQQCRASYTLPASADGQGIPRLPLTCR
>gnl|CDD|442422 COG3189, YeaO, Uncharacterized conserved protein YeaO, DUF488 family [Function unknown]
MMIRIKRVYDPPEPDDGYRVLVDRLWPRGVSKEDAALDLWLKDLAPSTELRKWFHHDPERWEEFRRRYRA
ELDANPAALDLLAALARHGTVTLLYAAKDEEHNHAVVLREYLEERLAKL
>gnl|CDD|442423 COG3190, FliO, Flagellar biogenesis protein FliO [Cell motility]
MKRLAAAAAPAPSSGGSLLQVLLALLLVLALILGLAWLLRRLGGRGGGGGALRVVASLSLGPRERLVLVE
VGGRQLLLGVTPQQITLLHELPAPEEAEELEAAPAPPSFAQLLKRALKRLRS
>gnl|CDD|442424 COG3191, DmpA, L-aminopeptidase/D-esterase [Amino acid transport and metabolism]
GLPPGPLNAITDVPGVRVGHATDIGDVRTGVTVILPHGGAVAGVDVRGGAPGTRGTDLLDPLGLVERVHP
IVLTGGSAVGLDAADGVMRWLEERGPGFDVGTGTVVPIVPEAVLFDLYLGDIRGRPVDAEHGYAALDAAS
SGPVAEGNVGAGTGATVFGFKGGIGTASRVLPGGYTVGALVAVNAFGDVVDLRTGVPFGDTLALKGPAPP
PPGANTTIGVVATDAPLTKAQLKRLARRAHDGLARTIGPVHTNGDGDIVFAFSTGNVIPAPVPDDLDPLF
AAAAEAVEEAILNAVLAAETVTGRDVPAL
>gnl|CDD|442425 COG3192, EutH, Ethanolamine transporter EutH, required for ethanolamine utilization at low pH [Amino acid transport and metabolism]
MSINEIIIYIMMIFMVLGAIDKILGNKFGLGEEFEEGFMAMGPLALAMVGIIALAPVLAEFLSPVIGPLY
TALGADPSMFATTILANDMGGYPLAEELAQDPEAGLFAGLILGSMMGATIVFTIPVALGIIEKEDHKYLA
LGVLIGIITIPIGCLAGGLVAGFDIGMVLRNLIPVIIFAVLIALGLWFAPDKMIKGFLVFGKFMVAVITI
GLAAAIVEYLTGIPIIPGMAPLFEAIEIVGKIAIVLAGAFPLVYLITKVFKKPLEKLGKKLGINEVGAAG
LLATLANNIPMFGMMKDMDPRGKVINVAFAVSAAFVFGDHLGFTAGFQPDMIFPMIVGKLVGGILAIIVA
LLLTRKEAKKLEKKDAA
>gnl|CDD|442426 COG3193, GlcG, Heme-binding protein HbpS, GlcG/HbpS family [Signal transduction mechanisms]
TKPSLTLEDARKIAAAALAKARELGVPVAIAVVDAGGNLLAFLRMDGAPLGSIDIAIGKAYTAAAFGRPT
GELEERAQPGPPLLGLNTSNGPGLVPFGGGVPIKVDGEVIGAIGVSGGTSEQDEAIAQAGLAALG
>gnl|CDD|442427 COG3194, AllA, Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism]
MSTSATLPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFGGEGRAGISIFRAQPRALPL
RITMLERHPLGSQAFIPLSGKPFLVVVAPPGGGPDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDF
LVVDRSGTGEDCEEHDLDTPLEIE
>gnl|CDD|442428 COG3195, PucL, 2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) decarboxylase (uric acid degradation) [Nucleotide transport and metabolism]
PMTLDELNALSREEFVAALGGCFEHSPWVAERAWAARPFASAEALHAAAARAVRAASEEEQLALLRAHPD
LGGKAAGAGRLTAESTSEQAGAGLDDLTDEERARLAALNAAYEARFGFPFIIAVRGRSKAEILAALERRL
ANDPETEFAEALAQIRRIARLRLEDLLAA
>gnl|CDD|442429 COG3196, CbrC, Colicin E2 tolerance protein CbrC, UPF0167 family [General function prediction only]
MNMPLPKFRYHPDPLATGSFVASDGVCQCCGKARGYIYTGPFYSVEEVDYLCPWCIADGSAAAKFDGEFQ
DDAGLEGEPIDDEKLEELCERTPGYISWQQEQWLAHCNDACAFLGYVGIEELKALLDELAALLEDYALRG
EFWEDLLEYLHKDGDPQGYLFRCLHCGKHRLWVDFD
>gnl|CDD|442430 COG3197, FixS, Cytochrome oxidase maturation protein, CcoS/FixS family [Posttranslational modification, protein turnover, chaperones]
MEILYLLIPLSLLLGLLALAAFIWAVKSGQFDDLEGPAVRILFDDDDPKPPPKEKKEKKK
>gnl|CDD|442431 COG3198, COG3198, Uncharacterized conserved protein [Function unknown]
MSSSNQMAKPWYKQFWPWFLIALPLAVVVAGLVTLYLAISNADSLVVDDYYKEGKAINQDLERDQLAAAL
GLSAQLRLDDDGVELRLTLNGPAELPEALRLTLIHPTLAERDQTVVLQRDGDGRYRGQLPEPLAGRWYVQ
LEPEDGDWRLQGEVTLPQGNAVVLGPRL
>gnl|CDD|442432 COG3199, COG3199, NAD kinase [Nucleotide transport and metabolism]
MMKIGIIANPIAGMGGAVGLKGSDGEIRRAVARGAVPRAPERANIALRLLLGLKERVLIMTDSGGMGEDV
LRELGFEVEVLYDMPPVTTTAEDTRRAARAMLEAGVDLIVFLGGDGTARDVAKAVGDSVPVLGIPAGVKI
HSGVFAVTPEAAEETIAGLANELAGLVAAEVVDIDEAAFRNGRLRARLYGYMKVPVELRYVQAVKQGGSE
SEELVLEDIAAYLVDVMEDDTLYIIGPGSTTAAIMDELGLENTLLGVDAVWDGELLASDVTEAQLLFLTF
AEPAKIGVSPIGGQGHIFGRGNQQISPGVIRRVGKENIIVVATKSKLIALDGRELLVDTGDPELDEELSG
YIRVITGYDGPRLVDVA
>gnl|CDD|442433 COG3200, AroG2, 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, class II [Amino acid transport and metabolism]. 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, class II is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
MASRWTPDSWRSKPAKQQPTYPDAAALAAVEAELASLPPLVFAGEARRLKAQLAAVARGEAFLLQGGDCA
ESFAEFTADNIRDKFKVLLQMAVVLTYGASKPVVKVGRIAGQFAKPRSSDTETRDGVTLPSYRGDIVNGF
EFTPEARRPDPQRMLRAYHQSAATLNLLRAFTQGGFADLHQVHQWNLGFVRNSPAGERYEELADRIDEAL
RFMEACGIDSETTPQLREVDFYTSHEALLLDYEEALTRIDSRTGDWYDTSAHMLWIGERTRQLDGAHVEF
LRGIRNPIGVKVGPSTTPDDLLRLIDRLNPENEPGRLTLITRMGADKVRDHLPPLVRAVKAEGRKVVWSC
DPMHGNTIKSSSGYKTRRFDDILDEVRGFFEVHRAEGTHPGGVHLELTGDDVTECLGGARAITEEDLADR
YETACDPRLNAEQSLELAFLVAEMLRE
>gnl|CDD|442434 COG3201, PnuC, Nicotinamide riboside transporter PnuC [Coenzyme transport and metabolism]
LFEWLLAQLTLGGTPMSWLELIAVLFGLLSVWLAARRNIWNWPFGIISTLLYAYLFFQAKLYGDALLQVY
YFIMSIYGWYQWKRGRDNEGEVPVRRLSLKEWLLLIAAGVLGTLLLGYLLKAFTDSAVPYLDAFTTVLSL
VAQWLMARKYVENWLLWIVVDIVSVPLYFYKGLYLTAILYAVFLVLAIYGYRNWRKSAKQQKA
>gnl|CDD|442435 COG3202, TlcC, ATP/ADP translocase [Energy production and conversion]
SSPLSRLLARLFPIRPGELKKFLLLFLLFFLILFAYYILRPIRDALFLTGLGAEVLPWLKTGTAPVALLA
VPLYSKLVNRLSRRRLFYVVYLFFLLFLLLFAFLLYPNRDAIIRKWVGRLFYVWVELFNLFVVSLFWSFA
NDIFNTREAKRLFGLIGAGGTLGGILGGFLTSLLAKFLGLANLLLVAAVLLLIALLLLRYLNRRVPRLPD
AAAKATKKKKIKGGLLEGLKLILKSPYLLLIALLVLLYNIVITLVEFQWKDIVKEAYPDPAELAAFFGFF
DLIVNLLTLLLQLFVTSRLLRRLGVGVALLITPVIILVGGLLFFLFPALAVGAIQNVLSRALKYSLFDPT
REMLYIPLDRELKYKGKAFIDTVVYRLGKSLGGWILIGLLSLLGLSAPYLAVIFIVLALLWILAAFKLGR
EYKRLLKESL
>gnl|CDD|442436 COG3203, OmpC, Outer membrane porin OmpC/OmpF/PhoE [Cell wall/membrane/envelope biogenesis]
TLLALAVAAALAGAAHAQSSVTLYGRVDAGVEYVDNGGGSLTRLTSGGDSGSRLGFKGSEDLGGGLKAIF
QLESGFNADTGTSGGGGRLFGRQAYVGLKGDDFGTLTLGRQYTPLYDVVGAFDPFGDSGDAGNLAGDDNL
AGTGRADNAIKYRSPNFGGLTFGAQYSFGEDAGSSSNGRGYGAGLTYANGPLSLGAAYQQSNDAQGATAG
GDDADAWGLGASYDFGNLKLAAGYGQTKNDDAGGAGNAKADGYELGASYPFGPALTLSASYGYTDAKDGA
DDDDANQYALGADYALSKRTSLYAEYGYNDNDGNANFTAAAGDTDDGVAVGLRHKF
>gnl|CDD|442437 COG3204, YjiK, Uncharacterized Ca-binding beta-propeller protein YjiK [General function prediction only]
MKKSSIILALLLLLLLAAAAPSIDLDEASLWLPDYRLDIEPKLLPGELDEISGLTYNPDTGTLFAVQDEP
GEIFELSLTGKVLRRIPLGGFGDYEGIAYLGDGRYVLVSEGTQTLYEVTLDDGTTVLRADVKSLKLGLSE
KGNKGFEGLAYDPKNNRLFVAKERDPDGIYEFDLDSKKLTGSPDKALKGVKDPSALAIDPITGHLLILSD
ESKLLLELDRDGKVVSALSLDKGFDFPQPEGIAFDPDGNLYIVSEPGGGKNLFYVFKKNAK
>gnl|CDD|442438 COG3205, COG3205, Uncharacterized membrane protein, DUF2061 family [Function unknown]
METHKRSMAKTISWRVIHFSVTFLVAYLLTGSLALAGAIALVEPLVKTVAYYFHERLWNRIRWG
>gnl|CDD|442439 COG3206, GumC, Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]
MNESSSAPPEEEDEIDLRDLLRILRRRKWLILLVFLLVLALALLYALLLPPVYEASATLLVEPQSSDVLL
SGLSSLSASDSPLETQIEILKSRPVLERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNVIEI
SYTSPDPELAAAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDL
SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELA
ELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE
AELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPAVVPLKPVSPKKLLILALGLLLGLLLG
LGLALLLELLDRTIEEELELLLLLGLPLLGPLPPLKSKRERRRARLALLLLAAALAALLALLLALLLLLL
LLLLLLLVSSSSGGGSSSTSSALAAASAAAAAAAALLLLLLLLLLLDLLLLLLLLLLLLLLLLGGLLLLL
LLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLLSDDLILDLVPLLAALLAAAVLA
VLVVVLLLVVALVALARLALLAAALLLLLVLVVVGGVVLGGVVYGYYYYYYYYYYYY
>gnl|CDD|442440 COG3207, Dit1, Pyoverdine/dityrosine biosynthesis protein Dit1 [Secondary metabolites biosynthesis, transport and catabolism]
SMDSTSAEEIADIILAELLQYRRVLPASDPCISSEEQEGFAVQLPRIAAFVEAGEPITFILPAFPCKSPN
PAKVLGHLPDLGERLSLRFLDSLCQRIQSVYSPGARITICSDGHVFSDLIGVPDDHIDAYQDELRNLIHE
LGASHLSVFNLEDFYPFTLSFDQLRERLVKSYAESLEELKERVRTDEEGLRLYRGITRFLYEDGLTPDYT
GSNSALQKDAKLRAYGVIQRSRAWGNLLAERFPDAIRLSIHPQPAGSKKFGIHLLDTRDDWLTPWHGVAV
NVDGQFVLMKRSDAEELGGVLVTIDGRPSHYVI
>gnl|CDD|442441 COG3208, GrsT, Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism]
PRPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLTSLEELADDLAEELAPLL
DRPFALFGHSMGALLAFELARRLERRGRPLPAHLFVSGRRAPHLPRRRRPLHDLSDAELLAELRRLGGTP
EEVLADPELLELFLPILRADFRLLETYRYTPGPPLDCPITALGGDDDPLVSPEELAAWREHTTGPFRLRV
FPGGHFFLRDHPAELLALIRAALAALA
>gnl|CDD|442442 COG3209, RhsA, Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only]
ETSLGLVGGTTGASSTLLAATNAGGGTAVTNAGSTVLLAKGGLSTAAAAGGAATLTARSASTTDVVGTLT
GAGGTSAGGVTALGDASAAGGGYVGGAAAGGGATLTGLAAATASAGRLVSTGAGAGGTVTAATGGTLGAT
AGSATTGSTDGGRGGVAVTGLAGGGASAYGLTLGGAAAGPATGVGTGAVTLATGLAGSALLALGSGAILG
GLAGAYSGSATTATGTALGTPASVAATVTGSATGAAGAGAAVATAATTLGGTTGAGTGASGAGLDASTGT
GGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTTGTAAVSGAADAGTTTTTGTGTGGTTTTVG
GGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTTGVGAGTTTTSTTGGDGGPA
TAAGALTAGGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGTGGGTLTSGS
AGATTLGTDTTLDDTLGGTTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTST
GTGGTGTVTTTGDGTGGASTTTGTTGGTATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGL
ERATASTGSTTGGTTGTGVTTTGTTTTRATGTTGTGTGVTAGLTTLATGGTTVGGGTGTTSTATTGATTG
GTETGTTVTTLAGGTTTRLGTTTTGGGGGTTTDGTGTGGTTGTLTTTSTTTTTTAGALTYTYDALGRLTS
ETTPGGVTQGTYTTRYTYDALGRLTSVTYPDGETVTYTYDALGRLTSVITVGSGGGTDLQDRTYTYDAAG
NITSITDALRAGTLTQTYTYDALGRLTSATDPGTTESYTYDANGNLTSRTDGGTTTYTYDALGRLVSVTK
PDGTTTTYTYDALGHTDHLGSVRALTDASGQVVWRYDYDPFGNLLAETSGAAANPLRFTGQEYDAETGLY
YNGARYYDPALGRFLSPDPIGLAGGLNLYAYVGNNPVNYVDPLGLAALLGTTGLGGGAGVGAGAAGGGAA
AAGGSAGAGAAGGGAGGAGAGGAGGGAGAGAGAAAGAAGGAGGGAGASGAGGG
>gnl|CDD|442443 COG3210, FhaB, Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport]
GSGGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGG
VGNTSASTGGIGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTV
TTLGGTTTGNTVLSTSGAGNNTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLA
NAGGGTAGGVASANSTLTGGVVAAGTGAGVISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGT
NATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGG
NNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATGNTGTTIAGNGGS
ANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGI
GTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASG
SNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGG
GAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLN
NAGNTLTISTGSITVTGQIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGT
TLTLANANGNTSAGATLDNAGAEISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGA
GGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNG
AVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTS
ANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNA
SGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASK
VGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAAT
EGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGA
TAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAA
VNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGR
DGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGG
STAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEAG
TGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAEGTNAEYG
GTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTDATLAGL
GGATTAAAGNVATGDTAP
>gnl|CDD|442444 COG3211, PhoX, Secreted phosphatase, PhoX family [General function prediction only]
MSDHDDDVVEARLSRRQFLKGGLAAAAAAALGGPLAACASAAAAGAPSGLGFTPVAPSTLDDLVVPEGYS
YRVLIRWGDPLFDGAPAFDPDGQTAAAQAKQFGYNHDGMAFFPLPGSSDRGLLVVNHEYTNPELLYPGGG
AARTAEQVRKEMAAHGVSVVEVRRDADGKWEVVRDSPYNRRITANTPMELTGPAAGHDLLKTSADPDGTS
VLGTLNNCAGGVTPWGTYLTCEENFNGYFGDAPNRFGWVVEIDPADPTSTPVKHTALGRFKHEGAAVDPA
ADGRVVVYMGDDERFEYLYKFVSDGKYDPGDRAANSGLLDEGTLYVARFNGDGTGEWLPLVHGDPPLTPA
DGFASQADVLINTRLAADAVGATKMDRPEDIEVNPVTGKVYVALTNNSRRGDGGVDAANPRAGNRYGHII
ELDEAGGDHAATTFTWDLFLLGGDPADADFAGGNTTGGDGFSSPDNLAFDPRGNLWIQTDGSTSGLGNND
GLWAMLVDGPETGELKRFLSGPVGAEITGPTFTPDGRTLFVNVQHPGETSAITGPGSNWPDGDGARPRPS
VVVITRKD
>gnl|CDD|442445 COG3212, YkoI, PepSY domain containing protein, regulator of zincin peptidase activity [Posttranslational modification, protein turnover, chaperones]
MGAIISLEQALEIALARVPGRVLEVELERDDGRLVYEVEILTPDGRVYEVEVDAKTGEVLKVEEDD
>gnl|CDD|442446 COG3213, NnrS, Nitric oxide response protein NnrS [Signal transduction mechanisms]
MSTLPRPPRGPPLLSLGFRPFFLLGALFAVLAMLLWLLALAGGLPLPGALPPLLWHAHEMLFGFAPAVIA
GFLLTAVPNWTGRPPIRGRPLALLVLLWLAGRLAFLLGGALPPLLAAALDLAFLLALALALARPLIRARN
WRNLAFLAALLLLALANALFHLAALGGDPALALLGLRLGLGLLLLLILLIGGRVIPFFTANALPGYQPVP
PPWLDNLALGLLLLALLLWLLGPDAALTAVLALAAALLHLVRLARWRGWRTLREPLLWILHLGYAWLPLG
LLLLGLAALGPVLGSAALHALTVGAIGTMILAMMTRVSLGHTGRPLVADRLTVLAFALLQLAALLRVLAP
LLLPAAYLLLLLLAALLWIAAFGLFLLRYGPILLRPRADGRPG
>gnl|CDD|442447 COG3214, YcaQ, DNA glycosylase YcaQ, repair of DNA interstrand crosslinks [Replication, recombination and repair]
MATRTLSLAQARRLALAAQGLLRPRPRPAGKRGLLRAIRRLGLVQIDSINVVARAHYLVLFSRLGPYDPA
LLDRLLWADRRLFEYWAHEASLLPVEDYPLLRWRMRRAREGGWKRWARWAEEHPALIDEVLARIRAEGPL
TARDLEADLQRGSGGWWDWSPSKRALEYLFRTGELMVAGRRGFERVYDLTERVLPAEVLAAPTPDEEEAA
RWLVRRAARALGVATARDLADYFRLKPAEAKAALAELVEEGELEPVEVEGWDRPAYLHPDARLPRPVTRT
ALLSPFDPLVWDRKRAERLFGFDYRIEIYVPAAKRQYGYYVLPFLLGDRLVGRVDLKADRKAGVLRVQAL
WLEPGVRLTAALAAALAAELRRFARWLGLERVVVTRGPGDLAPALAAALA
>gnl|CDD|442448 COG3215, PilZ, Type IV pilus assembly protein PilZ [Cell motility, Extracellular structures]
MSDPAARRPGILSLAIKDKAALYAAYMPFLKNGGLFVPTNRPYKLGDEVFLLLTLPDDPEKLPVAGKVVW
ITPPGAQGGRPAGIGVQFSDDDKEAARNKIEALLAGLLSSDRPTHTM
>gnl|CDD|442449 COG3216, COG3216, Uncharacterized conserved protein, DUF2062 family [Function unknown]
MPRRLLKRLLPRPEGLRRRLRYFGHRLLRWHLNPRSIARGVAIGVFIGFLPFFGLQMLLAAALALLLRGN
LPAAVAGTWISNPLTMPPIYYFAYKLGAWLLGTPPLAFALFELSLSWSALLELLLEIGLPLLLGSLILGL
VAALLGYFLVRRLWRRWRRRRRRRRAARA
>gnl|CDD|442450 COG3217, YcbX, N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and metabolism, Defense mechanisms]
MGRVSRLYRYPVKSLAGEALESATLTAGGLPGDRRWALVDADGRFLTQRRHPRLALLRARLDEDGGLTLT
APGGESLTVDLDDDAGDAAAAWLSEYLGRPVRLVRLPPESRRGPPVGFADGYPVLLISTASLADLNARLG
APVDMRRFRPNLVVDGLEPFAEDDWVGRRLRIGEVRLRVVKPCSRCVVTTVDPETGERDPEPLRTLARYR
GADGHVDFGVNAIVLEGGTIRVGDEVEVLE
>gnl|CDD|442451 COG3218, COG3218, ABC-type uncharacterized transport system, auxiliary component [General function prediction only]
MTPRRLLRLLLLLLLALLLAGCSSLPAPPPPTLYDLTPPLPAAAAAGPLPAQLLVAEPTAPGALDSDRIV
VRPDPGQLQYYAGARWADPPPRLLQDLLVEALEASGRFRAVGRPGSGLAADYRLEGELRDFEQDFDGGAP
RAVVELRARLVDDRDGRVVASRRFEARVPAASADAAGVVAALNQALDQLLAEIVAWLAAQLA
>gnl|CDD|442452 COG3219, COG3219, Uncharacterized conserved protein, DUF2063 family [Function unknown]
MPSLQQLQRAFAAHLRDPDAAPPPGGIEARRLAIYRRLVFNNLEGFLSSGFPVLRALLGDERWEALVRAF
FAEHPSRSPYFRDIGEEFLDFLAEEAPARPGDPPFLAELAHYEWAELAVFVAEDAPPAAAIDPEGDLLDL
RLVLSPLAWLLAYAYPVHRIWPAFQPEEPPAGPTFLLVWRDPDDEVRFLELNPLTARLLELLAEQGLTLA
AALEALAEELGHDPEALLEDGAALLAQLLAQGLILGPRA
>gnl|CDD|442453 COG3220, COG3220, Uncharacterized conserved protein, UPF0276 family [Function unknown]
MTTPLPPLGVGLGLRPEHYDDLLATRPDVDFFEVHPENYMGAGGPPLAQLERLRERYPLVLHGVGLSLGS
ADPLDPDHLARLKALADRLEPAWVSEHLAWSSAGGVHLGDLLPLPYTEEALDHVAARIRQVQDALGRPLL
LENPSSYLAFPGSEMSEAEFLAELVERTGCGLLLDVNNVYVNAVNHGFDPLAYLDALPLERVGEIHLAGH
SEEADGLLIDTHGAPVPDPVWALLEEALARFGPVPTLLERDGNIPPLAELLAELARARAILARAAA
>gnl|CDD|442454 COG3221, PhnD, ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion transport and metabolism]
VLPSESPADLLARWQPLADYLEEELGVPVELVPATDYAALIEALRAGQVDLAFLGPLPYVLARDRAGAEP
LATPVRDGSPGYRSVIIVRADSPIKSLEDLKGKRFAFGDPDSTSGYLVPRALLAEAGLDPERDFSEVVFS
GSHDAVILAVANGQADAGAVDSGVLERLVEEGPDADQLRVIWESPPIPNDPFVARPDLPPELREKIREAL
LSLDEDPEGKAILEALGLEGFVPADDADYDPIRELLKALG
>gnl|CDD|442455 COG3222, COG3222, Uncharacterized conserved protein, glycosyltransferase A (GT-A) superfamily, DUF2064 family [Function unknown]
MSAKTALIVFAKAPEPGKVKTRLAPALGPEGAAELYRALLEDTLAVAAALPAGDVEVAYAPDLDEAAFDA
WLPAGFTLIPQGGGDLGERMANAFADAFARGYEPVVLIGSDCPDLTPALLAEAFEALEEHDAVLGPAEDG
GYYLIGLRRPHPELFENIPWSTDTVLADTLARLRELGLSVALLPPLWDVDTPEDLARLAAELPALSRAAL
L
>gnl|CDD|442456 COG3223, PsiE, Phosphate starvation-inducible membrane PsiE (function unknown) [General function prediction only]
MKKHHKLDRLIAKLLQLILNIGLFVIGIALVIALAKETYEMVLLLSSGYVLLEDILLFFLYFEFIAMIVK
YFKSGYHFPLRYFIYIGITALIRLIIVDHKDPLDTLLLSGAILLLAIALLIVRYGRLKFP
>gnl|CDD|442457 COG3224, COG3224, Antibiotic biosynthesis monooxygenase (ABM) superfamily enzyme [General function prediction only]
MPATEPVTVVITRRVRPGREAEFEAWLREITALAARFPGFLGVGVIRPSGGSDEWVILLRFDSEENLDAW
LESPERRAWLEEGEPLLEGEERVERRTGLEGWFTPPGAPAAAPPPRWKQALVTWLVLFPLVLLLNLLLGP
LLAGLPLLLRVLIGTAISVALLTYVVMPRVTRLLRPWLHPKPR
>gnl|CDD|442458 COG3225, GldG, ABC-type uncharacterized transport system involved in gliding motility, auxiliary component [Cell motility]
GLNALLFLLLVLAILVLLNYLASRYYFRFDLTEDKRYTLSPATKNLLKNLEEPVTITVFLSGDDLPAEFR
RLRREVRELLEEYQRYNGNIKLEFIDPDEDPELARQLAEFGIQPTNLTQGQKLIFPGAVVEYGGKTEVVP
LLKNDLNSIEFLEYELTNAIRKLTRTKKPKVGFLTGHGELSLDRDLSDFVEALEEKGYDVAPLNLDSAAE
IPEDADVLVIAGPTKAFSEEEKYALDQYLMRGGKLLWLLDPVNAELDSLAFPRDLGLDDLLFKYGVRLNP
GLVVDLSSAGIPLGYLPWPYFPLVTNYGNHPITKNLNLAVLFPFASSIDTLKNKGIKKTPLLRTSPQSWL
ETDPASILGTVRLEFDPETFDIKGPLPLAVALEGKFPSAFKNRIKPGELKESSKEQRVVVIGDGDFLSNQ
FLGQYGNKDFLLNAVNWLADDEGLISIRPKEIKDRPLDLSKIQEEKLFWQFNILLPLLLLGFGLLIWWRR
RRRY
>gnl|CDD|442459 COG3226, YbjK, DNA-binding transcriptional regulator YbjK [Transcription]
PRRRRGEERRERILEAALRVIARDGVRGVTHRAVAAEAGVPLGSTTYYFRTRDELLAAAFERLAEREAAR
LRALLAAADDLEDAAEALADLLAELLPADRDRLLARYELYLEALRDPELRALLRRWRDRLREALARLLAA
LGSPDPPETARALVALIDGLTLHALLDPDPLTREELRAALRRLLRALLPAP
>gnl|CDD|442460 COG3227, LasB, Zn-dependent metalloprotease (Neutral protease B) [Posttranslational modification, protein turnover, chaperones]
MKKALAAALALSSSLSAAPASAASAEAAAKAYLAANKAAFGSADDDLVLRRVRTDENGTTHVRYQQTYKG
LPVFGGDLVVHLDANGKVKAVNGALRAGLEVLSTTPKLSAEAALAAALAALGAKSAKATSAPKPELVVYA
ADGKARLAYEVVVTGTDAGTPSRPHVFVDANTGAVLDSWDDIHTALATGTGRTVYGGTVTLDTTQSGGTY
YLRDPTRGIKTYDANNGTSLPGTLFTDEDNVWGNGTNGADAAVDAHYGAGVTYDYYKNWFGRNSIDGAGG
GLISRVHYGLNYVNAFWDGSQMVYGDGDGVTFGPLTGSLDVVGHELTHGVTEYTSGLVYSGESGALNESF
SDIFGALVEFYANGPADPNDWLIGEDIWTPGSGDALRYMDNPSKDGQPDDYWDGSIDNGGVHYNSGILNH
AFYLLAEGGTHRGNGSTVTGIGIDKAGKIFYRALTDYLTSSTTFADARTATLQAAKDLYGASSAEVAAVA
AAWDAVGVGAATGPPPTTTTTTTTASTSSSGSSSSVTGSGSVVVASTTTTTGSSGGTGGSAGALSAGTTS
TSTSSSSTSTTSSSTTTTTAAAAAAGGTSTILVTGSTGSSTSTTTTTT
>gnl|CDD|442461 COG3228, MtfA, Mlc titration factor MtfA, regulates ptsG expression [Signal transduction mechanisms]
MLRWLRRWRRRRRLARAPFPALWRAILARVPFLAGLSAEERARLRELAQLFLAEKRFEGVGGLEVTDEMR
LLIAAQACLPLLGLGLDWYDGLHEILVYPGAFVVRREEQDEAGVVHEGDEVLSGEAWERGPVVLSWPDVQ
AGFRNPRDGHNVVIHEFAHKLDMLDGAADGVPPLHPRMDYAPWAQVFSAAYEALQRRVDAGEETLIDPYA
ATNPAEFFAVASEYFFEAPELLAEKHPALYELLARFYRQDPAA
>gnl|CDD|442462 COG3230, HemO, Heme oxygenase [Inorganic ion transport and metabolism]
AAAAAPSLLARLRAATRALHERLDALVMLLDPFLTLEDYARFLRAQYGFHAPLEALLAAAALAALLPDLA
ERRRLALLEADLADLGLPPPAAAAAALPALTSLAAALGALYVLEGSTLGGAVLLKRLRRALGLDPDFGAR
FLAGYGDGTGAMWRAFLAALDAAALTEEEADAAIAGARAAFARFEAWLEAAF
>gnl|CDD|442463 COG3231, Aph, Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis]
GPRLPPALRELLGGYRWEPVTIGESGAKVFRLADGGRPTLYLKIEPAGPAAELEDEADRLRWLAGQGLPV
PEVLDFGEDDGGAWLLTTAVPGRPAASVSEALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEAR
ARVAAGLVDPDDFDEERRGRPPEELLAELLAERPAEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVA
DRYQDLALAARSLRENLGEGWVEPFLDAYGIAPDPERLAFYRLLDEFF
>gnl|CDD|442464 COG3232, HpaF, 5-carboxymethyl-2-hydroxymuconate isomerase [Amino acid transport and metabolism]
PHLIIEYSANLADELDIPALLEALHQALAASGLFPLGDIKVRAIPLDHYLVGDGGPDDAFVHVTLRILAG
RSDEQKQALSEALFAALRAHLAPVFARYVALSVEIREIDRASYAKRNNIHA
>gnl|CDD|442465 COG3233, COG3233, Predicted deacetylase [General function prediction only]
MPMSARLLVSLHDVSPATLDEVAELLAELDARGVPLSLLVVPRFHGKYPLAEDPEFVAWLRARRARGDEL
ALHGYDHADDGPDYLHRRVYTRREAEFAALPEHEARLRLEAALALLERLGLPTKGFVPPAWLMSPGALQA
LRELGFRYTADLRGIYDLETGRAIRAPVLTWSARSAWRRWLSRALNAAARRRARRGGLVRLAIHPKDLRY
PGGRQALLDALDAALEEGREPVTYADLLARSAAA
>gnl|CDD|442466 COG3234, yfaT, Uncharacterized conserved protein YfaT, DUF1175 family [Function unknown]
MDRGEFRAAKEVQLTAALDTSDGASDGFPDFLALDPEDSEAFRAWFVRIALEQIRQPSPRWPEEQRDCAG
LVRFAYREALKKHDGKWLKANGYDGPIIEDVSKYNYPELPLSGTQIFRILAGRWQQGDGAFSAFASARAL
IQFNSRFVSRDLNQALPGDLLFFDHPEDDMPYHLMIYMGDGIVYHTGPVGETDGELRAVRLEDLMRWKDP
RWRPREDNPNFLGVYRLKFLS
>gnl|CDD|442467 COG3235, COG3235, Uncharacterized membrane protein [Function unknown]
MNLPADLLPSWLLWLAWLLYLLLLLLALRRAPWRRLRRDKSRQHLFLGAVVALFLLWLLRAGIKPGLSFH
FLGATALTLMFGWRLALLAGSLALLGLTLFGAADWAALGLNGLLMVALPVLVSYLLYRLVYRYLPRNLFV
YIFVNGFFGAALTILLAGLAAALLLWLSGAYSWDYLLDNYLPYLPLLAFPEAFLNGMLITLLVVYRPEWV
RTFDDRRYLDG
>gnl|CDD|442468 COG3236, RibX, N-glycosidase YbiA/RibX (riboflavin biosynthesis, damage control), NADAR superfamily [Coenzyme transport and metabolism, Defense mechanisms]
SGARLKYIFFYGHTEPYGCFSNFSPAPFEVDGVTWPTAEHYYQAQKFGDTEIREKILAAKTPAEAKKLGR
KVKGFLRADWEAVKFDIMREANLAKFSQHPDLRELLLATGDRVLVEASPKDYIWGIGGDWRGLNLLGFIL
MEVREELR
>gnl|CDD|442469 COG3237, yjbJ, Uncharacterized conserved protein YjbJ, UPF0337 family [Function unknown]
MNKDKIKGKWKQLKGKAKEAWGKLTDDDLLEAEGKADQLKGKLQEAYGDAKDAAKKAVDDWKDKL
>gnl|CDD|442470 COG3238, ydcZ, Uncharacterized membrane protein YdcZ, DUF606 family [Function unknown]
MMMLLLLLLALLAGALLALQAAINGRLGQALGSPLAAALISFLVGTLVLLLLLLFLRGLPGLPALAPVPW
WLYLGGLLGAVYVFLSALLVPRLGVALTILLVIAGQLIGSLLIDHFGLFGLPKRPLTLTRLLGLALMLAG
VVLIQLGR
>gnl|CDD|442471 COG3239, DesA, Fatty acid desaturase [Lipid transport and metabolism]
MTTATPLTPADEAELRALRARLRALLGRRDWRYLLKLALTLALLAALWLLLSWSWLALLAALLLGLALAG
LFSLGHDAGHGSLFRSRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYL
FQHLLRFFLLGLGGLYWLLALDFLPLRGRLELKERRLEALLLLLFLAALLALLLALGWWAVLLFWLLPLL
VAGLLLGLRFYLEHRGEDTGDGEYRDQLLGSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRI
LKELCPEYGLPYTEGSLLRSYREVLRLLRRLGLPARPAP
>gnl|CDD|442472 COG3240, COG3240, Phospholipase/lecithinase/hemolysin [Lipid transport and metabolism, General function prediction only]
MKKRLAAALALLALLLAACGGAASAAAFSRIVVFGDSLSDTGNLFNLTGGLPPSPPYFGGRFSNGPVWVE
YLAAALGLPLTPSSAGGTNYAVGGARTGDGNGVLGGAALLPGLAQQVDAYLAAAGGTADPNALYIVWAGA
NDLLAALAAVGATPAQAQAAATAAAANLAAAVGALAAAGARHILVPNLPDLGLTPAAQALGAAAAALLSA
LTAAFNQALAAALPALGVNIILFDVNSLFNEIIANPAAYGFTNVTDACLSGTVSALLCVANPDTYLFWDG
VHPTTAAHRLIADYAYSALAAPGQL
>gnl|CDD|442473 COG3241, BlueCu, Azurin [Energy production and conversion]
MKKLLLALAALLLAAGELATAAKATPAAAAAAADCEITIEANDAMKFDKKEITVKAGKEVTLTLKNTGKL
PKDAMGHNWVLTKPGDDQAVGAAGAAAGADNNYVPPDDDRVIAHTKLIGGGESDTITFTAPKEPGDYPFF
CSFPGHWALMKGTLIVEK
>gnl|CDD|442474 COG3242, yjeT, Uncharacterized conserved protein YjeT, DUF2065 family [Function unknown]
MMDDLLLALGLVLVIEGLLPFLFPGAWRRMLRQLAQLPDGQLRFIGLVSMVAGLVLLWLVRG
>gnl|CDD|442475 COG3243, PhaC, Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism]
AAAGDSLAAAAAAAAAAAALLAAPARLLLAQAALAQRLLALWQAAAARLAGGGAAPPPIPPPPDDRRFDP
DWWWNPPFDFIKQAYLLLAQWWLDAVADVEGLDPKTRRRVRFYTRQILDAMSPSNFLATNPEALKETLET
GGESLVRGLENLLEDLERGAISQTDESAFEVGENVATTPGKVVYRNDLMELIQYAPTTEKVHKTPLLIVP
PWINKYYILDLQPGNSLVRYLVDQGFTVFLISWGNPDAEDRDLGLDDYVEDGILAAVDAVREITGEDKVN
LLGYCLGGTLLAIYAALLAARGPDRVASLTLLATPLDFSEPGELGVFIDESQLADLEALMAAKGYLPGRL
MAGAFSLLRPNDLIWSYYVNNYLLGENPPPFDLLYWNADSTRLPGRMHSQYLRDLYLENRLAKGELELGG
RPVDLSDITVPVLVVAGEEDHIAPWRSVYALAQLVGGKDVTFVLAPGGHIGGIVNPPGKPKRSYWTNDRL
PGDPDEWLAGAEEHPGSWWPDWADWLAERSGKKVPARAPGSGPPLEDAPGTYVKE
>gnl|CDD|442476 COG3245, CytC5, Cytochrome c5 [Energy production and conversion]
MKKSLLAALALALRIAPVGAVALAAAAAAAAARSGEAVYNATCAACHATGVAGAPKLGDKAAWAPRIAKG
MDTLLKHAINGFNAMPPKGGCADLSDDEVKAAVDYMVN
>gnl|CDD|442477 COG3246, COG3246, Uncharacterized conserved protein, DUF849 family [Function unknown]
MRKVIITCAITGAIHTKSMNPALPVTPEEIAEDAIAAAEAGAAIVHLHVRDPDGRPSQDPELFREIVERI
REACPDVIINLTTGGGGGMTVEERLAHLAELKPEMASLDMGSMNFGLGDRVFENTPADIEELAREMQERG
VKPEIECFDTGHLYNAARLIDRGLLKGPLHFQFVLGVPGGMPADPENLLAMVDRLPDGATWSVAGIGRHQ
LPLAAMAIALGGHVRVGLEDNLYLDKGVLAKSNAELVERAVRIAEELGREVATPAEAREILGLKGA
>gnl|CDD|442478 COG3247, HdeD, Acid resistance membrane protein HdeD, DUF308 family [General function prediction only]
LSEALKRNWWWLLLLGILLILLGILALVWPGATLLALVILFGILLLVSGIVQLVAAFRARGWGGRGWLLL
LGILYIVAGILLLFNPLAGALVLTLLIGIWLLVSGILRIVAAFRLRKEVPGWGWLLLSGILSLLLGILLL
FWPFSGLWVLGLLLGIYLIFSGIALIALALRLRKAAKA
>gnl|CDD|442479 COG3248, Tsx, Nucleoside-specific outer membrane channel protein Tsx [Cell wall/membrane/envelope biogenesis]
MKKITLLAAALLLALLLLSAPAAAAAADWSDTSLNYLYGEDFRVGPGDVDDTYLTLEHASGWGYGDNFFF
VDVLKSFGGDPADDGGSEFYGEISPRLSLGKLTGKDLSFGPVKDVYLAAGYNFGEGNAGRQRTYLLGLGF
DLDVPGFGYLSLNLYARYNDENYGAANENSWDGYQLTPVWFYPFSIGGSDLSYDGFIDYIFGSDLTAANI
LFQPQLRYDLGKALGWKKDRLYVGVEYRYWHNKYGIKDGADVKTTGNGPYLLVKYHF
>gnl|CDD|442480 COG3249, COG3249, Uncharacterized conserved protein, DUF2066 domain [Function unknown]
RRLLLLLLLLLLSSPAQAAEVSGLYEAEVPVASQSEEERNAAIAQALAQVLVKVSGDRDVLNNPGIAQAL
RNAERYVQQYRYRQDEGESSSFQLLLVVRFDPQAVDRLLREAGLPVWGENRPLVLVWLAVEDGGGRRLVG
SDSDPELLQALKQAAKRRGLPLLLPLLDLEDQAAVSVSDVWGGFEEPIAAASARYGADAILAGRLSRTGD
GQWQADWQLLLGGQVQSWSSQGGSLAQALAAGVDGVADRLAKRYAVVPSSGAEGRVRIQVTGVDSLADYA
RLLSYLESLSVVRDVRVVSVQGDTVTFELDLLGDVEQLAQALALDRRLVPVADPASPANELVYRWLP
>gnl|CDD|442481 COG3250, LacZ, Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]
GGWKFRLGDAPEGAKPDFDDSGWDPITVPGDWELDLYGLPDPFVGPWYLYNGVGWYRRTFTVPASWKGKR
VFLHFEGVDTAAEVWVNGKKVGYHEGGFTPFEFDITDYLKPGENVLAVRVDNPSDGSYLEGQDWWRTSGI
YRDVWLEATPKVHIEDVFVTPDLDDGSATLTVEVELENESDAGVTVEVTLLDADGKVVATATAKVTLAAG
EENTVTLTLTVPNPKLWSPEDPNLYTLVVTLKDDGKVVDTVSTRFGFRTIEIDGDGGFLLNGKPVFLKGV
NRHEDWPDDGRAVTDEAMRRDLELMKEAGFNAVRTSHYPEDPEFYDLCDELGLLVWDEAPFEWHGMLGDD
PEFLEAVEAELREMVRRDRNHPSIILWSGGNESGGGPNFAALYEWVKELDPTRPVRFLSEYGHAMPNSLG
GGYHQPSDFEEYQALQALEEYWEAFRRRPRLAGGFIWQLNDYWPEPRDNDGNFCSWGLVDYYDRTPKPAY
YEVKSAWQPVLVSDGMLHILLPHWNDGKEGELPYSSTVADLYTPYVRPQENGNRTDVRWLTLTNGKGKGL
LVSGVPLLSGSALAYLTEDLLAAKEEGLLLAADLTTLLLDLADLGGGGNSGGGLLLLGGLLVEKDLSLAA
LLLAAAEL
>gnl|CDD|442482 COG3251, MbtH, MbtH family protein, regulates adenylation domains of NRPSs [Secondary metabolites biosynthesis, transport and catabolism]
MSNPFDDDDGTFLVLVNDEGQYSLWPAFRAVPAGWRVVGGPGSREECLAYIEEHWTDMRPLSLREAMAEQ
A
>gnl|CDD|442483 COG3252, Mch, Methenyltetrahydromethanopterin cyclohydrolase [Coenzyme transport and metabolism]
MISLNRLALELVDELLDFAEELRVEVHELDNGATVIDAGVNAPGGLEAGLLLAEICLGGLGTVSLRPGDV
DGAWPPAVEVSTDHPVLACLGSQYAGWSLSVGKFFALGSGPARALAGKEELFEELGYRDDADFAVLVLES
DKLPPEEVAEKVAEACGVDPENLTLLVAPTASLAGSVQVAARVVETALHKLHELGFDLTKIVSGSGSAPL
APVAPDFLTAMGRTNDAILYGGRVHLTVRGDDDAAEDLADKLPSSASRDYGRPFAEIFKEADYDFYKIDP
MLFSPAEVTVNNVETGKTFRAGEINEDLLAESFGL
>gnl|CDD|442484 COG3253, HemQ, Coproheme decarboxylase/chlorite dismutase [Coenzyme transport and metabolism, Inorganic ion transport and metabolism]
MSEAPTEEGWYTLHSFFKVWPAWRRLPDEEREEAAAEFEELLEELEAEGGLRGLYDVSGLRADADLMFWH
HAPTLEDLQAAEREFRRTALGRYLEPTWSYVSVTRPSEYNKDSHLPAFLAGRELPPRKYVCVYPFVKSRE
WYLLPFEERREMMAEHGMIGRKYAGKVRQNTTGSFGLDDYEWGVALEADDLHDFVDLVYELRFDEARAHV
REFGPFYTGRRLDPEELLAVL
>gnl|CDD|442485 COG3254, RhaM, L-rhamnose mutarotase [Cell wall/membrane/envelope biogenesis]
KRYAFVMDLKPGLIAEYKRRHAAIWPELLAALKEAGIRNYSIFLDGNLLFGYMEVDDFEAAMAALAADPV
NQRWWALMADIQETLPDAKPSEKWVPLEEVFHLD
>gnl|CDD|442486 COG3255, SCP2, Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism]
DEWAEALCEKLNAADAAAGWDGVVQFVITGEGGGAYYLVIDDGKCTVSEGDDDDADVTLTASYEDWKKLL
TGELDPMTAFMTGKLKVEGDMGLAMKLMSLFKAL
>gnl|CDD|442487 COG3256, NorB, Nitric oxide reductase large subunit [Inorganic ion transport and metabolism]
SYKKLWWALALVLVVSFAVLGYGGVEIYRQAPPIPDKVVSPDGEVLFTKDDILDGQQVFQSYGLMQYGSI
WGHGAYLGPDWTADWLHREAEAMLDYYAQQRYGKPYAALSAEEQAALRARVKRELRTNRYDAATGTLTLS
PARAAAIEQVAAYYTDLFGDGPEEYALPEGTIPDPEEARQLAAFFFWTAWAAVTNRPGEDYSYTNNWPYE
PLVGNTPTADNLVWSILSVILLLAGIGALLWIYGRLGHEEEEPEPPDADPLDDVPLTPSQRAAGKYFLVV
AALFLVQVLFGGLTAHYYVEGDFFYGIPLAQLLPFNVARTWHTQLAIFWIATGWLGAGLFLAPLISGREP
KGQKLGVNLLFWALVVVVVGSLLGYWLGIMGKLGGDLNFWLGHQGREYLELGRFWQIGLVVGLLLWLFLV
FRTILPALKRGRKTGLLHLLLLSAVAIALFYLAGLFYGPHTNLSVDEYWRWWVVHLWVEGFFEVFATAVV
AFLLVKLGLVSRKSAERALYFEVILFLGGGIIGTGHHYYWIGTPTYWMALGAVFSALEVVPLVLLGVEAW
ENYRLRRRAGWMFPYKWAFLFFVAVAFWNFLGAGVFGFLINLPIVNYYEHGTNLTAAHGHAALFGVYGML
AIGLMLFALRYLRPRAAWNEKLLKWAFWLLNIGLALMVFLSLLPAGILQLWASREHGYWYARSQEFLQQP
LLQTLRWLRLPGDVVFILGALLLAWDVLKLLRRERKAT
>gnl|CDD|442488 COG3257, AllE, Ureidoglycine aminohydrolase [Nucleotide transport and metabolism]
TYYAPKGGLPPQTDLLTTRAVFTEAYAVIPPDDIVTSVLPGWENTRVWILARPLSGATFSQYIVEVAPGG
GSDRPEPDPGAETFLFVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNAGDEPARFHWIRKRYEPVE
GLEAPEAFVGNEADVEPTPMPGTEGATTRFLLPEDLRFDMHVNIVTFEPGGSIPFVETHVMEHGLYVLEG
KGVYRLNNDWVEVEAGDFIWMRAYCPQACYAGGPGPFRYLLYKDVNRHPELG
>gnl|CDD|442489 COG3258, TsdA, Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion transport and metabolism]
MRKLALLAAAAARRGEELFTNGLSCASCHLDAGTKPWGVAAAYPAYRARNGKVVTLEDRINGCFTRSMNG
KPLPLDSAEMKALVAYLRWLSRGLPVGVKLDGRGLPKLPKPAASADVERGKALYAERCASCHGADGEGQG
RADGQYGFPPLWGGDSYNDGAGMARLGTLADFIKGRNMPLGKPGSLSDDEAWDVAAYVRSLPRPVPRKTD
VPAVRK
>gnl|CDD|442490 COG3259, FrhA, Coenzyme F420-reducing hydrogenase, alpha subunit [Energy production and conversion]
MTRRITIDPVTRVEGHGKITIFLDDDGKVKDARLHIVEPRGFEKFLEGRPYEEVPDITARICGICPVAHH
LASAKALEAAFGVEPPPTARKLRRLLYCGEWIQSHALHFFFLAAPDFLGYRNVLGLAKKHPELVKRGLRL
RKLGNEIIELLGGRAIHPVNAVPGGFSKAPSEEERDELLERLEEALEFAEEAVDLFKDLFLKNKDEVDFP
DFDTEFMGLVDDGEYPLYDGRLRIVDSDGKILEFDPADYLDHIAEEVVPWSYAKFPYLKGLGYDGIYRVG
PLARLNLNDDILTPLAQEALEEFGLRFGPPVHNPFAYHWARLIEILYAAERAIELLEDPEITGPPLRVPV
GPRAGEGVGVVEAPRGTLIHHYTVDEDGLITKANLIVPTTQNNAAIEEDVRQVAKALLDGGEPDEGLLNR
VEMAIRAYDPCISCATHALGQMPLKLELVDADGELIDE
>gnl|CDD|442491 COG3260, HycG, Ni,Fe-hydrogenase III small subunit [Energy production and conversion]
KVLGRSLWIRHVDAGSCNGCEIEILALLTPRYDLERFGIKFVASPRHADVLLVTGPVTRNMREALLRTYE
AMPEPKVVVAVGDCACSGGVFRDSYAVLGGVDKVIPVDVYIPGCPPRPEAILDGLLKALGRLEEKLK
>gnl|CDD|442492 COG3261, HycE2, Ni,Fe-hydrogenase III large subunit [Energy production and conversion]
LALAALALLLALDLAAGGALFGLRLEAEDELLLLLLLAAGVLLLLPTPPPSSSAPAAAAARRERARERLG
GEEGGGPPRRRLLLPDGWPPLPPPPLRPPPPPRGPPPPPPEEPEMKVEGEGVHEIPVGPVHAGLIEPGHF
RFSVEGERILDLEIRLGYVHRGIEKLAEGRDYEQALYLAERICGICSVAHALAYCQAVEKAAGIEVPPRA
QYLRVILLELERIHSHLLDLGALANDVGFETLFMQCWRLRERVLDLNEALTGNRVLRGINVPGGVRRDLD
PEQLKAILERLDELEEEVKELVDLFLNDPSVLDRLVGTGVLSKEDARDLGAVGPVARASGVDRDVRRDHP
YAAYDELDFKVVTETEGDVYARALVRLEEIFESLDLIRQALEKLPEGPIRVPVPGLPPDGEGLGRVEAPR
GELVHYVRTDGDGRLERVKIRTPSFANWPALELALRGNIVADFPLINKSFDPCYSCTDR
>gnl|CDD|442493 COG3262, HycE1, Ni,Fe-hydrogenase III component G [Energy production and conversion]
MTRPEELRARFGGSILERRWVRPNEVWVEVDREDLPELAEFLAEGGGGRLAALWGNDERELGGGFAVYYV
FALEGEGALVTLKVSVPKDDPVFPSITDLFPAASWYEREIRDLFGIVPEGHPDPRRLVLHDDWPEGIYPL
RKDFKGGPRPAPAPAEEYFRPVEGEGIEVVVVGPVHAGIIEPGHFFFSVGGEIVIRLEELLYYVHKGEEK
LEEGEEGRAGLVLAEAAGGDSGAAAAAAAAAAAEAAAAAAIPPRAALLRLLRLLLERLELHLGLLGLGGL
DAGGAGAAGAAALLRRRLERLLEALLLRRGRRGGGGGGGGGRDDDDLLADLILELLLDLEEEEEELEELA
DLLSRLIDRLDTTGGLALKAAAAGGVGGAAGRASGGRGDRRRRAPYAAYDDVDLRVVVLTVGDVDVRRAR
VREELEEISRLIIILLDLLLLGPGGLLVGGEPAPAEGGGGGGGLRGGGGEGVRGGGGDAIRRRRWRRPSA
ANWPNPPALILPNINDDFPLNNSINSLSYGSSD
>gnl|CDD|442494 COG3263, NhaP2, NhaP-type Na+/H+ and K+/H+ antiporter with C-terminal TrkAC and CorC domains [Energy production and conversion, Inorganic ion transport and metabolism]
MDTLNLILLIGALLLLLSILASKLSSRLGVPLLLLFLGIGMLAGEDGLGGIQFDDAELAQLIGSLALAVI
LFDGGLRTRWSSFRPVLAPALSLATLGVLLTAGLTGVFAHWLLGLSWLEGLLLGAIVSSTDAAAVFSILR
SKGLNLKERLASTLELESGSNDPMAVFLTIALIELITGGGASGWSLLLLFVLQMGLGALVGLAGGWLGVW
LLNRIRLPAEGLYPVLVLALALLAFGATALLGGSGFLAVYLAGLVLGNRRLPHKKSILRFHDGLAWLAQI
GMFLMLGLLVFPSRLLPVALPALLIALFLIFVARPLAVFLSLLPFRFSWREKLFISWVGLRGAVPIVLAT
FPLLAGLPGAQLIFNVVFFVVLVSLLVQGTTLPPVARKLGLEVPPEPKPLTRVELELLEELDAELVEYRV
PPGSPAVGKTLRELRLPEGALVVLIVRDGELLVPRGSTRLQAGDQLLVLAPPEDLEALERLFAAVSRAGT
LAEWFGDRVRLG
>gnl|CDD|442495 COG3264, MscK, Small-conductance mechanosensitive channel MscK [Cell wall/membrane/envelope biogenesis]
MEESALLELLFLIGGISISLPNLLLALLILVVTYLLARLLSRLLERRLLRRTRLDPGLRYLISKLIRYLI
IVLGLLIALSALGIDLTALAALAGALGVGIGFGLQDIVSNFISGLILLFERPFRVGDWIEIGGTEGTVEE
IGLRSTRIRTFDGEEVIIPNSELITNPVINWSLSDPRRRVEIPVGVAYGSDLEKVRELLLEAAREHPRVL
KDPAPSVLFTEFGDSSVNFELRFWVNDPRDRLRVRSDLNEAIKKAFREEGIEIPFPQRDVHLRNPPGEVP
E
>gnl|CDD|442496 COG3265, GntK, Gluconate kinase [Carbohydrate transport and metabolism]. Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHL
AAGEGAVLACSALKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPD
EDAIVVDIDQPPEEIVAQILAALG
>gnl|CDD|442497 COG3266, DamX, Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning]
GLLGETLSTLALALLLLSLSLVLGDLGLLLLLLLRALLSALELLLATGLRLLLLAGLLLLLIRLLSEAVD
LGALASAALLLALASLALLGILLLALLALLLDLLLLADLLRAAALLLLKLLLLLLTLLLLVLLLLLALLL
ALLLDLPLLTLLIVLPLLEEQLLLLALQDIQGTLQALGAVAALLGLRKAEEALALRAGSAAADALALLLL
LLASALGEAVAAAAELAALALLAAGAAEVLTARLVLLLLIIGSALKAPSQASSASAPATTSLGEQQEVSL
PPAVAAQPAAAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPTAAKPVVTETAAPAAPAPEAAAAAAAPA
APAVAKKLAADEQWLASQPASHYTLQLLGASSEAALEAFAAKHSLKGNLWVYPTTRNGKPWYVVVYGSYA
SRAEAKAAVAALPAELRASKPWVRSIAQVQQELKK
>gnl|CDD|442498 COG3267, ExeA, Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
MYLEFFGLKEKPFSLTPDPRFLFLSPSHREALARLEYALAQGGGFVVLTGEVGTGKTTLLRRLLERLPDD
VKVAYIPNPQLSPAELLRAIADELGLEPKGASKADLLRQLQEFLLELAAAGRRVVLIIDEAQNLPPETLE
ELRLLSNLETDSRKLLQIVLVGQPELRERLARPELRQLRQRITARYHLRPLDREETAAYIEHRLKVAGGE
GDPLFTPEAIEAIYRASGGIPRLINNLCDRALLAAYAEGKKVVDAEIVREA
>gnl|CDD|442499 COG3268, COG3268, Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown]
MTEREFDIVVYGATGYTGRLVAEYLARRGLRPALAGRNAAKLEAVAAELGAADLPLRVADLDDPASLAAL
LAGTRVVLNTVGPFARTGEPLVEACLAAGTHYLDLTGEPDWVRRMIDRYDAAARAAGARIVPACGFDSVP
SDLGAALLQERLPEADRLTLAVRAKGGFSGGTAASMLEALAAGGADRRNGRLVRVPYALRTREDFPDGGP
QQGAWTAPWGDVNTAVVRRSNALLNYEEYMAVPKGAARALALAAGLGALLAAAVPPLRRLLKRVLPKPGE
GPSEEERERGRFVVWGEARTAGGRRVRARVRGPGGYGLTAKMLAEAALRLLADDPVRGGFLTPATAFGAA
LVLRLLAVAGLTFEVEEL
>gnl|CDD|442500 COG3269, COG3269, Predicted RNA-binding protein, contains TRAM domain [General function prediction only]
AAFEAAEALLAAGGDVVAKVFIGEGGGPLDDLVEEEFRYVLLRGAAASRRESSKRRSVGKPEAQELTPPV
EEGEEYEVEIEDIGKKGDGIARVEGFVIFVPGAEVGDRVKVKITKVKRNFAFAEVVERL
>gnl|CDD|442501 COG3270, Ncl1, Ribosome biogenesis protein, NOL1/NOP2/FMU family [Translation, ribosomal structure and biogenesis]
APPLLELFQLMMLLLLEEEAAFAAALRLLRRSSLRVLLLKAAEDLALRLLAPPPLLPPPPWPEGGGYEED
EELGGPLGLAAAALYYLQEAAAASSALPVAALPGLLLLLAAAAGGAAATAAAAAQGGLLLNLLNIILALE
LLASSVEVLHANIVVVVNTNTPLAELAGFVFFDALDADADASLLGGGFPREGAAAKEADPLRKASAEIQL
EIEAAAAAALLLGGGALLLTTTTEPSEEEEEEEELLLLLEELDLALEPAVEEGAGEGGDPEAAAALTELL
GLHRFPPHGEGGGGFFAALKKKAGDEPSPKKKKKKKKPKQAKEVLRAFAEEGLPLPEVGRLWERGGKLYL
LPEELPDLSGLKVLRIGLKLGEIKKKRFEPSHALALALGPEATKNVVELDAEEALRYLKGEDIELEDGDK
GWVLVTYDGYPLGWGKYVGGRLKNHYPKGLRR
>gnl|CDD|442502 COG3271, C39G, Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, secretion, and vesicular transport]
MKRATLLLSLLLLLAGSPAGSVLPGSGGGYSVPVKSLKELRFRNVVRQQYDYSCGAAALATLLNYHYGRP
VSEAEVLEGMLTHGDQRRRGFSLLDMKRYLEALGLRADGYRLTLDDLAQLGIPAIVLINLGGYKHFVVVK
GVDDGRVLLADPALGNRSLSREEFEKMWDGNVLFVVPPK
>gnl|CDD|442503 COG3272, YbgA, Uncharacterized conserved protein YbgA, DUF1722 family [Function unknown]
RLVQPKTGDDDTTEMLAFFSAFLAQLLDVDGGYIKSKKSPSCGGERVRVYYEEGGPPAKKGVGLFARALM
ERFPLLPVEEEGRLNDPVLRENFLTRVFALARWRELLAEGLTIKALVEFHSRHKYLLMAHSQKAYRELGR
LVANAKKRPLEELAEEYEELLMEALAKPATRKNHTNVLQHIFGYFKKQLSSDEKQELLELIEDYRQGLVP
LIVPLTLLKHYLRRYPDPYLAQQTYLNPYPEELGLR
>gnl|CDD|442504 COG3273, COG3273, Uncharacterized protein, contains PhoU and TrkA_C domains [General function prediction only]
VGMMALELVEYEPVLVKLLLVEMKDTAELLIDLAYSAVLDESDALAEEVLELELRMDVLQLLARMSLLLA
ARALEEAELLAPVLGVVAAAVAISAAAGDIAKVVLEDIGLPEAMRAALPEAVETLVRATVAASSALAGRT
LLLILLETETGVRVIAIRRGDDWLLNPGPTTILRADDLVLLRGPEGGILEVYLAATGDLYERPRPPEDSI
VEMKNLSELAVDLAYSSVLFDSEELAEEVRELEEEVDALKSRLEAWVLRAARRVDDPVALRGLLHLASST
EVISDAALDIAEGVLRGLEDHPVVAEAVRESDERIVRVTVPPGSPLVGKTLGELKLETETGVRVIAIRRG
GGWIYDPDGDTRLRAGDVLIVKGTREGLERLEELAGG
>gnl|CDD|442505 COG3274, WecH, Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis]
MPSSKKKRIVYLDLLRVLAIFAVVLIHVTAPFVSSPGLIGSLNWWVANLLDSLSRFAVPLFFMISGALLL
DRKKEDLKDFYKKRLRRILIPLLFWSLIYLLFFTFLGGFSFNSLSEFLKNLLTGGVSYHLWFLYMIIGLY
LFTPLLRKLVRKASKRELLYFLLLWLILSLLLPYLNTLLGIDLFFTLTLFLGYLGYFLLGYYLARYKARL
KKRRLIALLLFLVGLALTFLGTYLLSLQTGKFNELFYSYLSPNVVLMSVALFLLLKNLSFRSSKLSRLLS
RLSKYSFGIYLIHPLVLDLLTKLGLNLLNINPLLGIPLVALLTFVLSLLIVLLLRKIPLLRKLVG
>gnl|CDD|442506 COG3275, LytS, Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms]
LLALLLLLLLLLLLLLLLLLLLSLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL
LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLILILLALLL
SLQEEELELEELEKELLEAELKALKAQINPHFLFNTLNSIYSLIREDPEKARELLLKLSDLLRYSLYESD
KELVPLEEELEFLENYLELEKLRFGDRLQVEIDIDEELLDLLIPPLLLQPLVENAIKHGISSKEGGGTIS
ISIEVEGDRLVIEVENNGVGIQPKKKKKGSGIGLKNVRERLELLYGDKYSLEIESTDGGGTKVTLKIPLK
KE
>gnl|CDD|442507 COG3276, SelB, Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]. Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
MIIGTAGHIDHGKTTLVKALTGIDTDRLKEEKKRGITIDLGFAYLPLPDGRRLGFVDVPGHEKFIKNMLA
GAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWLELVEEEIRELLAGTFLED
APIVPVSAVTGEGIDELRAALDALAAAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELE
LLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSAP
RPLKHWQRVHLHHGTAEVLARVVLLDREELAPGEEALAQLRLEEPLVAARGDRFILRDYSPRRTIGGGRV
LDPNPPKRKRRSPERLAWLEALAKGDPAELLAALLALAPGGLSLAELARLTGLSEEELAALLEELGARVV
VLGGGDRLLVSAAALEALKERLLAALAEFHEKNPLRPGLSREELRRRLLPRLPEKLFDALLEELLAEGEL
VLTGGWLHLPGHKVTLSAEEEALWQRLLPLLAAGGFPPPWLRELAAELGLEEEAVRELLRLLLRLGELVK
VVDDLFYLAAALAALAALLAALLAETGAAAAADRRDLLGGRRKLLLLLLEFFDRRRRRRRRGRRRRLRRD
>gnl|CDD|442508 COG3277, GAR1, rRNA processing protein Gar1 [Translation, ribosomal structure and biogenesis]. rRNA processing protein Gar1 is part of the Pathway/BioSystem: 16S rRNA modification
MKRLGTVLHIAKQGLLIVRLDAADLPPIGSPVVDKSLKRVGKVVDVFGPVDSPYAAVKPDSKVSLEKLVG
EKLYVR
>gnl|CDD|442509 COG3278, CcoN, Cbb3-type cytochrome oxidase, subunit 1 [Energy production and conversion]
MEMEKFSYDDKIVRQFAIATVVWGVVGMLVGVLIAAQLAFPALNFDLPWLTFGRLRPLHTNAVIFAFGGN
ALFATSYYVVQRTCKARLFSDKLAWFHFWGWQLIIVLAAITLPLGITQSKEYAELEWPIDILIAVVWVAY
AINFFGTIAKRREPHIYVANWFYIAFIVTVAMLHIVNNLAIPVSLFKSYSVYAGVQDAMVQWWYGHNAVG
FFLTAGFLGMMYYFVPKQAGRPVYSYRLSIVHFWALIFIYIWAGPHHLHYTALPDWAQTLGMVFSIMLIA
PSWGGMINGLLTLSGAWDKLRTDPILKFLVVALTFYGMSTFEGPMMSIKSVNALSHYTDWTIGHVHSGAL
GWVGFITFGALYYLVPRLWGTELYSKKLVNWHFWLATIGIVLYIAAMWVAGITQGLMWRAYNEDGTLTYS
FVETVTAMHPYYVIRAIGGLLYLSGALIMAYNLWMTIRGGKAVAAEPAEAPALA
>gnl|CDD|442510 COG3279, LytT, DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms]
MMKILIVDDEPLARERLERLLEKYPDLEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLR
ELDPPPPIIFTTAYDEYALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKDRIFVKS
GGKLVKIPLDDILYIEAEGNYVKIHTKDKKYLVRKTLKELEEKLPPKQFFRVHRSYIVNLDKIKEIEKNF
NGEVVLKNGEEIPVSRRYKKEFKEW
>gnl|CDD|442511 COG3280, TreY, Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism]
MRIPRATYRLQFHAGFTFDDAAALVPYLARLGISHLYASPILKARPGSTHGYDVVDHNRINPELGGEEGF
ERLVAALRAHGMGLILDIVPNHMAVGPDNPWWWDVLENGPASPYADFFDIDWEPPDPELRGKVLLPVLGD
PYGEVLEAGELKLDFDPEEGGFVLRYYDHRFPLAPGTYPRILAEALARELLSLLTALRHLPARRREKEEI
KRRLAELYASPEVRAAIDRALAEFNPGDPESFDALHALLERQHYRLAYWRVAADEINYRRFFDVNELAGL
RVEDPEVFEATHALILELVAEGLVDGLRIDHIDGLADPRGYLRRLREALGGPAYIVVEKILEPGERLPAD
WPVAGTTGYDFLNQVNGLLVDPAGEAALTRLYERFTGETADFDELVREAKRLILETSLAGELNRLARLLA
RIARADRRTRDFTLNALRRALRELLAAFPVYRTYVNPGGLSAEDRRYIEEAVERARRRLPDLDPAALDFL
EDLLLGEEPGGLSEEERARRLEFVMRFQQLTGPVMAKGVEDTAFYRYNRLLSLNEVGGDPDRFGLSPAAF
HAANQERARRWPHAMLATSTHDTKRGEDVRARLNVLSELPEEWAEAVRRWRRLNAPLRRRLDGGPAPDPN
DEYLLYQTLVGAWPLDLLDAEGLAAFAERLQAYMLKALREAKVHTSWTDPDEAYEEAVLAFVRALLDPPE
NNPFLADFLPFVQRIAPAGALNSLAQTLLKLTAPGVPDIYQGTELWDFSLVDPDNRRPVDFAARARLLAE
LDAREEEGALLAELLANWRDGRIKLFLTARLLRLRRRHPELFAEGDYLPLEVTGERADHVVAFARRHGGR
AVVVVAPRLLARLLGEGALPLGAEGWGDTRVVLPEGLPGRWRDVLTGETVEEGGSLPLAELLARLPVALL
VREDG
>gnl|CDD|442512 COG3281, Ble, Predicted trehalose synthase [Carbohydrate transport and metabolism]
KLDVDYYVDDADAIFDDGSGDIDGDGDGGGLDGLLDLLLDLADLLPLDPPLLPDDDFDPDDDDYDDYDDY
DDSRDDYDRGEARRFIVDAAHRRLRVIRILLVLVAAPRAPRRPQARRARRASPESRDDDVADDTDTDDEY
TRAIADDDDNANAFAEWFPEAFFHHFYFFHPPDLDLNFELVERVLLLLDDLLDLLDDLVRLLRLLPENEE
EEEEETEEELERERLLKLRAERAALLEARAELAEEAEAPEEDDDAEGAFALFPLMAFAFPIPPRMYMAII
LEDIDPITDILIQTPEPDLPEQWALFLRLRDELTLERVTDAERDYLYRRRARRRRARRRLLLRRRRRLLL
LLRRRRLLLLLGLLLLLLGGGLPGYGDGDGGGDNIGGGLRDGRSTPPQRSPSRRGGFSRADPPRLVLPVI
VDPLYEYAAVNVEASLRLLLLLLLLRRRRLRLRRRRLRFGLGRFRLLLLENRRLLALLAELEVEVELVLA
RLLLLLAAVLLELLPLEGVVPLPLELGLLLPLPLLLPLGLLLAPLGFLVFLLALLPLEPLEVLPVLVALP
LPLLLVLLGLLLALLARARRALLELLLAPLLLARRRSGGGARAAIRALLLLAAALLLGGGRLLLGELRFR
PTPALAELLPADLPVRRLSGEQSNTSVIYGDRLILKLFRRLEPGINPDLEMGRFLTEAGFPNVPPLLGSV
EYRDPDGEPTTLAVLQEFVPNQGDAWSYTLDSLRRFLERVLLADEEVAEEIGDFLALARLLGRRTAELHA
ALASPTDDPAFAPEPFTPDDQRSLAQRMRRRLRRALALLPRRLPALPEEVQELAEELLARREALLARLAA
LAAAKIGAPKQRIHGDYHLGQVLRTGDDFVIIDFEGEPARPLAERRAKDSPLRDVAGMLRSFDYAAAAAL
RRATGVRPEDRERLEPWADAWRRRARAAFLDGYLEAAGGAGLLPADPRELRALLDAFLLEKALYEVVYEL
RNRPDWLPIPLRGLLRLLEELAGL
>gnl|CDD|442513 COG3283, TyrR, Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid transport and metabolism]
MRLEVTCEDRLGITRELLDLLVERNIDLRGIEIDPSGRIYLNFPELDFEQFQHLMPEIRRIPGVTDVRTV
PFMPSEREHLELDALLEALPDPVFSIDLKGKIELANPAALSLLGLSEEELIGQPLSELLKGFNFSRWLES
NEPRPQSERVVINGQDYLADILPIYLPDEEGKSILAGAVVTLKSAARLGEQLQALQVNDDSGFDHIVASS
PKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAP
GAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDL
AELVQEGEFREDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWP
GNVRQLENALYRAVSLLEGDELTPEDLQLPEYAASAGLLDDLLEGSLDEIVKRFERSLLRRLYPSYPSTR
KLAKRLGVSHTAIANKLREYGIGK
>gnl|CDD|442514 COG3284, AcoR, Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]
MPSARHLREARWFLSGGRLPAGGVRPLIARSWQRCREYGLDPDRPPAPRVLSGAELRELRERNEELLRAA
RPVLERLYEQLAGSGSVVLLTDADGVILDTLGDPRFLDRARRVGLAPGADWSEEARGTNAIGTALAEGRP
VTVHGAEHFLEANHGLTCSAAPIFDPDGRLLGVLDISGPARSSQPHTLALVRAAARRIENRLFLRSFRRE
WRLRLHFLPEFLGSLSEGLLAFDEDGRIVAANRAARRLLGLADAALLGRPLEELFGLDLEALPDGARRAP
ASPRPLRLRDGRRLGALLRLRPARRAARAAPAGAPAPAALAALAGGDPAMRRALRRARRLADRDIPVLIL
GETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEPGAFTGARRKGRPGKIEQADGGTL
FLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAAGRFREDLYYRLNGLTL
TLPPLREREDLPALIEHLLRELAAGRGPLRLSPEALALLAAYPWPGNVRELRNVLRTALALADGGVITVE
DLPDELRAELAAAAPAAAAPLTSLEEAERDAILRALRACGGNVSAAARALGISRSTLYRKLKRYG
>gnl|CDD|442515 COG3285, LigD, Eukaryotic-type DNA primase [Replication, recombination and repair]
ASAAAELEVGGREVRLTNPDKVLFPEAGITKGDLADYYAAVAPVMLPHLRDRPLSLVRYPDGIGGECFFQ
KHAPKGAPDWVRTVPVPSPSGRTADYLVVDDLATLLWLAQLGALEFHPWGSRADDLEHPDRLVFDLDPGP
GVGFADVVEAALLVRELLDELGLTSFPKTSGGKGLHVYVPLEPRYDWDEVRAFARALARELERRAPDLVT
AEMSKEKRGGKIFIDYLQNARGATTVAPYSLRARPGAPVSTPLTWDELDDGLDPDDFTIRTVPERLAELG
DPWADLLDAAQSLPALLERL
>gnl|CDD|442516 COG3286, COG3286, Uncharacterized conserved protein, DUF2067 domain [Function unknown]
MPLVKRVIVIKVPDGEEAEEFLERISSKIKSVDYVYIEIKGNRLKIEIQGDKDEIKEAWRRIRELYRKLR
LYKDGRGLYEYSLEDIVREAGYTIPPELLVDTLKLLGYKAELDEDDVIKTNAPLEEIVELARRLSEAYAE
IRFQVRGSSARRVIAAVSILTGVDPEEVIEEALEKGLLEEDEDGKIVLKKDWRLALKELLKKLKG
>gnl|CDD|442517 COG3287, FIST, FIST domain protein MJ1623, contains FIST_N and FIST_C domains [Signal transduction mechanisms]
MKTFVGVGHSTAADPAEAGRAAEEALAQLGAADPALVLVFASPDYDLEALLAALRAAFPGAPIIGCSTAG
EISPGGVLEGSVVLLAFSFDKFRVGVAVGDGLSDDSREAGRELARRLLAALGPDPDLRFALLLSDGLSGN
EEELLEGLYSALGPDVPIFGGSAGDDLRFEKTYVFHNGEVLSDAAVVALLGTSLPVGVGSSHGWKPTGPE
MVVTKAEGRVVYEIDGEPAAEVYARYLGDDAEELPASFLLFPLGVRIGGGEYLVRSPLAVEEDGSLTFAG
DIPEGSVLRLMEGNPDDLIEAAERAAEAALARLGGKPEAALLFDCVGRRLVLGQRVEEELEAVSELLGAP
VAGFYTYGEIGPFGGGGNQHHNQTLTGVAFGE
>gnl|CDD|442518 COG3288, PntA, NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]
MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIVDAELLGADIVLK
VRPPSAEELAALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKA
VLLAAPALHTFFPLMSTAAGTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKF
VELAIDANGAGGYAKELSEEEKAKQAELLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVD
LAAEQGGNCELTVPGETVTKNGVTIIGPTNLPSRLPAHASQLYAKNLLNFLELLVKDGALALDLEDEIVA
GTLLTHDGE
>gnl|CDD|442519 COG3290, CitA, Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms]
LLLLLLLLLLLLILLILILILLLLLLIILLLILLLVLLLLLFLLFVIILLLLLLILLLILLLLLLLLLAA
LLLKLLEEIARLVEEREAVLESIREGVIAVDRDGRITLINDAARRLLGLDAIGRPIDEVLAEVLETGERD
EEILLNGRVLVVNRVPIRDDGRVVGAVATFRDRTELERLEEELEGVKELAEALRAQRHDFRNHLHTISGL
LQLGEYDEALEYIDEISEELQELIDSLLSRIGNPVLAALLLGKAARARERGIDLTIDIDSDLPDLPLSDT
DLVTILGNLLDNAIEAVEKLPEEERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTKLGEGR
GLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE
>gnl|CDD|442520 COG3291, COG3291, Uncharacterized conserved protein, PKD repeat domain [Function unknown]
FTATPTSGCAPLTVQFTDTSSGNATSYEWDFGDGTTSTEANPSHTYTTPGTYTVTLTVTDAAGCSDTTTK
TITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDT
GLTGSTGTASDTATVTTSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGV
TTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGT
STNGTGGLGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSSTGTVF
>gnl|CDD|442521 COG3292, COG3292, Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]
KRLLLLLLLLLLSLFAQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRH
DPGDPNSLPSNYIRALLEDSDGRLWIGTDGGLSRYDPKTDKFTRYPLDPGLPNNSIRSIAEDSDGNIWVG
TSNGLYRYDPKTGKFKRFTLDGLPSNTITSLAEDADGNLWVDSDGNLWIGTDGNGLYRLDPNTGKFEHIT
HDPDPNSLSSNSIYSLFEDREGNLWVGTYGGGLNYLDPNNSKFKSYRHNDPNGLSGNSVRSIAEDSDGNL
WIRLWIGTYGGGLFRLDPKTGKFKRYNPNGLPSNSVYSILEDSDGNLWIGTSGGGLYRYDPKTGKFTKFS
EDNGLSNNFIRSILEDSDGNLWVGTNGGLYRLDPKTGKFTNFTHDPDKNGLSSNYINSIFEDSDGRLWIG
TDGGGLYRYDPKTGKFKHFTTKDGLPSNTIYSILEDDNGNLWNFNSASNLGLLSLLGGLLGGLNLGNAIK
LPLSNLGLLLTLLLLGINLSLVRSLISLLTLLLLALLLLLSLLLLLLLLLLLLLLLLLLLLLLLLLILLL
LLLRLLLLLLLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLL
LLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLLLLLLLLALLLLLLLLL
ALKLLLLLLLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLLILLVLE
LLLELALGLILLLKLLLLLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKIDLLDILELI
LLELELGLLLGLLLLLLLEILLLSLVELLLELLEGIILALDLLLGSLSLVILLGLNELLLAELEEIDALL
IELLLEEEVLLALI
>gnl|CDD|442522 COG3293, COG3293, Transposase [Mobilome: prophages, transposons]
MRKRHPVDLTDAQWARIEPLLPGPDKGGRPRHDDREVVNAILYVLRTGCPWRDLPRDFGPWRTVERRFRR
WRRLGRWERLAEALLAAVIDASSVRAHQ
>gnl|CDD|442523 COG3294, COG3294, Metal-dependent phosphatase/phosphodiesterase, HD supefamily [General function prediction only]
MSTEVLDRPIAEHLFPDGRLKITLEEIKNDPEIQAYLEAANVNALKRLGYNDHGPVHARIVANRALEILE
LLKEAGVEPSGAKDGGGYPEDEAELAALAAYLHDIGNVVHRDDHEQSGAILAAPILDRILMDIYDTEKRV
RLKAEILHAIGNHDEETEPLTIEAAALIVADKSDMERGRVRNPYDLGTFDIHDRSNYAIERVELRVGEEK
PIRLELEMDTSAGVFQYFEILLPKMAASFLGCYFELVAVVTGENGTRLL
>gnl|CDD|442524 COG3295, COG3295, Uncharacterized conserved protein [Function unknown]
MTRAALFPPRRSRRAFWLKWLRQWHWYSSALCLVGMLLFAVTGITLNHAAWIEAEPQVTERELTLPEALL
AQLAAEGSAPLPLALAEWLRQELGLSGAGREAEWSDDEIYVSLPGPGGDAWASIDRETGAVEVERTDRGW
IAYLNDLHKGRNTGAAWSWFIDIFAVACLLFSLTGLLLLQLHARRRPSTWPLVGLGLVLPLLLALLFIH
>gnl|CDD|442525 COG3296, Tic20a, Uncharacterized Tic20-related protein, DUF4870 domain [General function prediction only]
MSDPPPLPTQEDRTWAMLAHLSGLLGLIIPFGGFIGPLIIWLLKKDRSPFVDEHGKEALNFQITLLIYYI
VSGILTLVLIGFLLLIALGILNLVFPIIAAIKANNGEPYRYPLTIRFIK
>gnl|CDD|442526 COG3297, PulL, Type II secretory pathway, component PulL [Intracellular trafficking, secretion, and vesicular transport]
MSERLIIRLPSQPDDPIEWLLWSADGQEIASGELADAEALAELPARAAARRVVLLVPASDVLLTRVTLPA
KARRQLRQALPFALEEQLADDVESLHFALGPRQGDGRVWVAVVDREWLQAWLDALEAAGLPVDRIVPDAL
ALPLPEGGWSVLLLGDQWLVRTGEWQGFAVEADLLPLLLAAALEEAESKPAALPLLESYSPLPELEALEL
AEQPLGDPLQLLAQGLAASAINLLQGEFAPRSRRSRLWRPWRPAAALAALLLVLQLVGLGVEAWQLRQQA
AALRAEIEALYRQAFPGVKRVVDPRRQMERQLARLRGGAGGSDLLPLLAALAPALAAVPGLKLQSLRYDA
DRGELRLQLTAASFEALEQLRQALEAAGLQVEIGSANQEGGGVEGRLTLRSKAS
>gnl|CDD|442527 COG3298, COG3298, Predicted 3'-5' exonuclease related to the exonuclease domain of PolB [Replication, recombination and repair]
MNPVLVFDIETIPDVAGGRRLYGLDAGLSDADVAEAAFQLRREETGSDFLPLHLHRIVAISCVLRDGDGF
KVWSLGDPDDDEAELIQRFFDGIEKYTPQLVSWNGGGFDLPVLHYDGIAKLLGFPGKLGMDGSKVWPAYQ
DGEIDEIRDYCETDVLNTYLVYLRFQLMRGLLSPREYAAEIELVRETLAAGAGPHWQEFLAAWAAAGELA
Y
>gnl|CDD|442528 COG3299, JayE, Uncharacterized phage protein gp47/JayE [Mobilome: prophages, transposons]
RPTLEEILARMLADIKSIGGDIDLSEGSPLGQLLAAVAAELADLYQLLEWILRQIFPDTADGEYLDRHAA
ERGITRKPATKATGTVTFTGTPGTVIPAGTVVQTEDGVTYVTTEDVTIDADGTATVPVEAEEAGAAGNVP
AGTILTLVTPIPGVQSVTNPEALTGGADEETDEELRARLLASVRRPPTGGNAADYRAWALEVPGVGRAKV
YPLWNGPGTVKVVIVDGGDDAAVQAYIDPKRPIGADVTVVAPTEVPINVTVTLTPDSGYTLAAVRAAIKA
ALAAYFNRLPIGETVSLSRIEAAILSIPGVTDLTINGPTANITIGENEIPVLGTVTVTVV
>gnl|CDD|442529 COG3300, MHYT, MHYT domain, NO-binding membrane sensor [Signal transduction mechanisms]
TCLAGSHDPWLVALSVLIAVLGSYTALDLARRARAASGRARRAWLALAALALGGGIWSMHFIAMLAFRLP
VPVGYDPPLTLLSLLVAILASGLALALASRRRLSRLRLLLGGLLMGLGIAAMHYTGMAAMRMAGAISYDP
ALVALSVLIAVVASTAALWLAFRLRSLRRRLGAALVMGLAICGMHYTGMAAATFVPDPGAPAPAPGLSPT
LLALAVAVVTLLILGLALLASLLDDARRRARAARELASLRLLAALALAGLLLTGLLLALEARGALAALLG
AALDELLLDLLLLLDLDGDAALLLALGELLADLLLALVAARVVARVRLVARVGGDERDEIVAEDRLRRAE
AEAAADAARLALAAAASALSLDALLLLALLAAAALALALAALLALRALAAADALTVEADASSAAAELLLA
AALLLLLLLLLLLLLLLARD
>gnl|CDD|442530 COG3301, NrfD, Nitrite/polysulfide reductase, membrane component NrfD/PsrC [Inorganic ion transport and metabolism]
MTEYDVFHQLVWGWPIAIYLFLGGLGAGAFLLAALLDLLGRPESRALRRAGALIALVFLAIGLLLLVLDL
GRPLRFWKLLLNPNPTSWMSWGVWLLSLFGLLALLYAALLLKKELRLPLLEKLRRALALLGALLALLLAA
YTGFLLSAAKARPLWNTPLLPVLFLVSALSTGAAALLLLALLFGKEPSEELHLLHRLDVALILLELVLLA
AFLVGLHLGGAAAAAAAEALLTGRYAPLFWGGVVGLGLLLPLLLELAALKLKRSKGLLALAALLVLVGGL
LLRYLILYAGQLTPLSP
>gnl|CDD|442531 COG3302, DmsC, DMSO reductase anchor subunit DmsC [Energy production and conversion]
MHPEWPLVLFTVLSQAGVGLFLALALALLLGLLSPASRKRLLRALLLALVLLGVGLLASTFHLGHPLRAW
RAFSNLRTSWLSREIVAAVLFFALAGLYALLAWLGKLPGGLRKLLGLLAALLGLALVFAMAMIYQIKTVP
TWNTPLTPLNFLLTALALGALLAALLLALAGVDLRALKALALLALLALVLALAVLVAYLARLASIGSATQ
TAAALLTREFGHLLALRLVLLALGFVLPLLPLLRGSTAALALLALAFALVLAGELVGRWLFYALAVHVGM
LY
>gnl|CDD|442532 COG3303, NrfA, Formate-dependent nitrite reductase, periplasmic cytochrome c552 subunit [Inorganic ion transport and metabolism]
MKKKSLLFAVAALVVFLLGLLLVSIAERKAEAKTPFTPVVEIADGEPDPEVWGKNYPRQYDSYKKTAETT
FTSKYGGSEPYDKLEEDPRLVVLWAGYAFSKDYNEPRGHAYALEDQRETLRTGADGPQPGACWTCKSPDV
PRLIKEMGEDAYYKGPWAELGAEIVNPIGCADCHDPKTMELRITRPALIEALKALGKDFNKATRQEMRSL
VCAQCHVEYYFKGDGKYVTFPWDKGLTVEDIEAYYDEIGFSDWTHPLSKAPMLKAQHPEFETWSQGIHAK
AGVSCADCHMPYVREGGKKYSDHHVGSPLKNIERACQTCHRQSEEELRARVETIQDRVKELRLRAEDALV
KAHFEAKAAWEAGATEEEMKPALELIRHAQWRWDFVAAENSMGFHAPQEALRILGDAIDLARQARLKLAR
ALAKAGVTEPVPIPDISTKEKAQKAIGLDMEKEQAEKEEFLKTV
>gnl|CDD|442533 COG3304, YccF, Uncharacterized membrane protein YccF, DUF307 family [Function unknown]
MRLLGNIIWFVFGGFWLALGWLLAGLILCITIIGIPFGLACFKIAGLALWPFGKEVVDRPDGAGALSLLG
NIIWFIFAGWWLALGHLVTGLALCITIIGIPFGIQHFKLAPLALAPFGKRIVPSDVARAA
>gnl|CDD|442534 COG3305, COG3305, Uncharacterized membrane protein, DUF2068 family [Function unknown]
AIAVFEAAKGLLLLLAALGLLLLLHRDLQQLLEELLEHLHLDPANHYPEILLEKADLLTPGTLHLIALGA
LAYALLRLVEAYGLWRGKRWAEWLALVSTAIYLPFEIYELIRHPSWLKLGVLLINLAVVAYLARVLRRFR
RRGGATAY
>gnl|CDD|442535 COG3306, COG3306, Glycosyltransferase involved in LPS biosynthesis, GR25 family [Cell wall/membrane/envelope biogenesis]
MKIFVINLDRSTERREHIEAQLARLGLDFEFFDAVDGRDLSEEELARYDRAKALRRYGRPLTPGEIGCFL
SHRKAWQKIVESGLPYALILEDDVILSPDFAEVLEALAWLPADWDIVKLETSKRKVFLGRRKIKKLGGYR
LVRPYSPPLGTAGYLISRKAAKKLLALLEPIDRPVDDFLFRFWLHGLRVYQVRPALVIQDSGLLGSTIEA
ERRRKKRKRRLWDKLRRELRRLFYRLRL
>gnl|CDD|442536 COG3307, RfaL, O-antigen ligase [Cell wall/membrane/envelope biogenesis]
TFGNPNHLAAYLALALPLLLALLLLLKRRRLRRLLALLALLLALLALLLTGSRGAWLALLVGLLLLLLLY
KRKLRLRRLLLLLLAALLLLLLALILVSPPLAERLLEILGKDSSLGGRLEIWKAALEMIKEHPLLGVGYG
NFWYAYPAYQPAGYIWNAGHAHNEYLEILAETGILGLLLLLLLLLVLLRRALRRLRRSRLALALLALLLA
LLVHGLTESPLFSPASALLFWLLLALLLA
>gnl|CDD|442537 COG3308, COG3308, Uncharacterized membrane protein [Function unknown]
MTKPTKSARRLRLLALASLLALILLLLAWELWLAPLRPGGSWLALKALPLLLPLPGLLKGRPYTYAWASF
LILLYFLEGVVRAWSDPGLSRWLALLEVLLSVLLFVAALLYARWRGRALGLAAKKLK
>gnl|CDD|442538 COG3309, VapD, Virulence-associated protein VapD, endoribonuclease [Defense mechanisms]
MYAIAFDLDTNCLKKHYHGESYNNAYADIRKVLEKHGFEWTQGSVYLSDEGINAAHLVLAIQELAKQFSW
FKPSVRDIRAFRIEEWSDLTFIVKGVTQ
>gnl|CDD|442539 COG3310, COG3310, Uncharacterized conserved protein, DUF1415 family [Function unknown]
PSDEQVIAATRRWLERAVIGLNLCPFAKAVHVKGQIRYVVSEATDPEALLEDLLEELQLLDETPPEEIET
TLLIHPNVLADFLDYNDFLDLADALLEQLGLEGVYQLASFHPDYQFAGTEPDDAENYTNRSPYPTLHLLR
EASIERALAAYPDPEAIPERNIATLRELGLEGWKALLAACFKAD
>gnl|CDD|442540 COG3311, AlpA, DNA-binding transcriptional regulator AlpA [Transcription, Mobilome: prophages, transposons]
MSLPPDRLLRLKEVAELLGVSRSTIYRLIKKGEFPKPVKLGGRSVRWRESEVEAWLAARIAASR
>gnl|CDD|442541 COG3312, AtpI, FoF1-type ATP synthase accessory protein AtpI [Energy production and conversion]. FoF1-type ATP synthase accessory protein AtpI is part of the Pathway/BioSystem: FoF1-type ATP synthase
LYGRKPARKLLLLQLLVVLLVALLALVLWGPQAALSALLGGLIAVLPNAYFALRAFRYAGARAAKRVVRS
FYRGEALKFLLTIVLFALAFKLVKPLNPLPLFVGYLLVLVVQWLAPLLLNRKNK
>gnl|CDD|442542 COG3313, YdhL, Predicted Fe-S protein YdhL, DUF1289 family [General function prediction only]
MMMEQPVPSPCIGVCSLDPEDGVCRGCGRTLDEIARWSKMSDEERRAVLRRLPQRRAAL
>gnl|CDD|442543 COG3314, SpoVV, Spore dipicolinate transporter SpoVV/YjiH/YlbJ, contains nucleoside recognition GATE domain [Cell cycle control, cell division, chromosome partitioning, Amino acid transport and metabolism]
MESKYDTKDLLKFIIPSLIGIFLFFIPISINGKSTIPLDHLATWIQESLGSALPTLLLALIVIGAILPLI
AKLWKPSNVSPVWSLLRVLGAVFAVMVLFKYGPEAIFSAATGGLLLWVLLPSLLPFFIIAALFLPLLLGF
GLVEFIGVLLEPIMRPLFKLPGRSAFDAAASWVGGYPVGALLTSRLYEEGYYTKREAARIATFFSTVSPL
FMIVVAAVGGLMDPFLAHYLTVLLVGFIVAFITPRIPPLSRKPDTYYEGRKPQPEEPEGGNLFKRALKEA
LEAAEKARSLGKLLGDAVKNSLNMLLGIGPFIMAFGVLALILAEYTPIFDWLGYPFYPLLELLGLPEAAE
AAPAIISGFAEMFLPAILASEIASLLTRFVIAILSVSGLIYFSQVGSLLLGTDIPLRFKDLFIIFLLRTI
LSLPITALIAHLLF
>gnl|CDD|442544 COG3315, YktD, O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, transport and catabolism]
ESRRPDPLFRDPYAARLVGAIGYDFSRLLAGRGLRLGVAARTRFFDDLLRAALAAGIAQVVILGAGLDTR
AYRLDNPGGVRWFEVDLPEVIALKRRLLPELGPPARLRLVAVDLRDPDWPDALPAAGFDPSRPTLFIAEG
VLMYLTEEAVRALLRRIAALFPPGSELAFDYVPPLALKGSKKHPAVRKLRRDLGAPFKFGIDPDDPAELL
EEPGWRLVEELSPLELLARYLPLRPLRAPRLVHARF
>gnl|CDD|442545 COG3316, Rve, Transposase (or an inactivated derivative), DDE domain [Mobilome: prophages, transposons]
MVDFKGRRFPPEIILLAVRLYLRYGLSLRDVEEMLAERGVDVSHSTIYRWVQKFAPLIAKRLRRRRPPLS
DSWHVDETYIKIKGKWHYLYRAVDAEGRILDFLLSPRRDTKAAKRFLRKALKKYGLKPRVIVTDKLPSYG
AALRELKPEGGLGVEHRQVKGLNNRIERDHRTLKRRERPMRGFKSFRTAQRFLSGFEAYYNFRRPHRSLN
GATPARVARAAASKWGELILLAAAF
>gnl|CDD|442546 COG3317, BamC, Outer membrane beta-barrel protein assembly factor BamC [Cell wall/membrane/envelope biogenesis]
KLSVRLVLLLLLVLLLAGCSSLQRYFRSGKVDYLSAPKLPPLEVPPDLTAPSQDDRYDIPAGGAATGSEY
DIRPPAQVLPLVDGVRIERSGDQRWLVVDASPEQLWPQLREFWQENGFTIASEDPAAGVMETDWAENRAK
IPDFIRRTLLDGLYSTGERDRFRTRVERGVGGTTEIYVSHRGMEEVGDQKDSTVWQPRPADPRLEAEMLN
RLMVYLGADEEQAAAALAAAQVGGIRVQLGKDADGLPVLIVRAPFDRAWRRVGLALDRVGFTVEDRDRSQ
GLYYVRYVDPDDGEKPGFWSRLFGSDPELKAGDYRVQVGDLGNRTSVTVLDAKGKPLTSDTADRILSLLQ
AQLR
>gnl|CDD|442547 COG3318, YecA, Uncharacterized conserved protein YecA, UPF0149 family, contains C-terminal Zn-binding SEC-C motif [Function unknown]
LEEALACGPDLWALAIPRRAEPKVGRNDPCPCGSGKKYKKCCGAN
>gnl|CDD|442548 COG3319, EntF2, Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism]
AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLA
AALALAALAALAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAA
AAAAAAALAAAAGLGGGGGGAGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLL
LLLLLLALLLLLLLALLAAAALLALLLALLLLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLAL
LLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGG
GGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAA
LAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLAA
LLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLR
LLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAGGSGPPLFCVHPAGGNVLCYRPLARALGPDRPV
YGLQAPGLDGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQGEEVALLVLL
DSYAPGALARLDEAELLAALLRDLARGVDLPLDAEELRALDPEERLARLLERLREAGLPAGLDAERLRRL
LRVFRANLRALRRYRPRPYDGPVLLFRAEEDPPGRADDPALGWRPLVAGGLEVHDVPGDHFSMLREPHVA
ELAAALRAALAAAEA
>gnl|CDD|442549 COG3320, Lys2b, Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]. Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis
RTVLLTGATGFLGAHLLRELLRRTDARVYCLVRASDEAAARERLEALLERYGLWLELDASRVVVVAGDLT
QPRLGLSEAEFQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVAG
PADRSGVFEEDDLDEGQGFANGYEQSKWVAEKLVREARERGLPVTIYRPGIVVGDSRTGETNKDDGFYRL
LKGLLRLGAAPGLGDARLNLVPVDYVARAIVHLSRQPEAAGRTFHLTNPQPLSLG
>gnl|CDD|442550 COG3321, PksD, Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism]
AADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAYYDPDPDAPGKTYVRWGGFLDDV
DEFDALFFGISPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAI
DAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESF
ILFSKGGMLSPDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAP
NGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPADQPCAIGSVKSNIGHL
EAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTN
AHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLDLADVAYTLATGRAHFEH
RLAVVASSREELAAKLRALAAGEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYETEPVFRAALDE
CDALLRPHLGWSLREVLFPDEEESRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACV
AGVLSLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAGYDGVSIAAVNGPRSTVVSGPAEAVE
ALAARLEARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGEALDADYWV
RHLRQPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQCLAAAGDAVVLPSLRRGEDELAQLLTALAQL
WVAGVPVDWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLA
LAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAA
AAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAA
LAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAA
AAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALA
GLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALA
ALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAAL
AALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA
>gnl|CDD|442551 COG3322, CHASE4, Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms]
MSLRRKTLLAILLLLLLLLALLYLVSRLILLSSFSELEEQAAERDVERVLNALDAELDQLARLVADWAVW
DDTYEFVQDGDPEWIESNLGDWTFENLGLDLVLVLDPDGRLVYSKGYDLEDGELVPLPEALAPLLARARA
LLRHASPDSSVSGLLRLDGGPALVAARPILPSDGPGPPRGTLVFGRYLDEAFLARLAERTGLDLTLSPAD
PPAPPDQVVEPLSDDTIAGYVPLRDIDGQPVLLLRWTPPRPIYQQGRALLRYLLPALLLLGLLLALLALL
LLRLVLLLLLLLLRLVLSRLLLLLLRLLLLELLRALELLLLLLRRLLLLLLLLRLLLLLLDLLAALNLLL
LLRALAERLVALALLALLLLGLLGLLAALRRLGLLAILALAEEAARLLLLALAIAGELLIGIEVLLALGL
ELAGSAIALARAAAALALLLAAAAAARLAARAASGLLRDLLEADELEDRLRRALLAEAAALLLLALLALE
LLLALGDAALEILLAILLLGLVLEAQLAELERLLLLGEAGGELLEEIALLAALLAGLLLAVLLSLLLRLL
LLIDALVALAEAAAGLLEALLEEEVELRRALLEAEELLLIALALLSLGLALALDDGGRGLAGLLLLFRLS
GIGLLLLRRLLGDDLLGLLAALIDLILALAGSLLLLTLAAAAEATAVVLVAELLEGALLLQALALISLLE
LLLLLLLLELQLLEQVLSAPAALA
>gnl|CDD|442552 COG3323, YqfO, PII-like insert in the uncharacterized protein YqfO, YbgI/NIF3 family [Function unknown]
IIKIIIILEEEAAPPLAAEEDDNGGLLGGGGLVVVVVLLVLLDLEEEVVEEAAEAGALIIIHHHPLLFKL
LKKLGTDKPVGRIIKKIIKAIIIIAAAHTNDDDAAGGNNDLLAALLLLLLLILLLKKEEKLYKLVVFVPE
EHAEAVREALFAAGAGHIGNYDHCSFQTEGTGTFRPLEGANPFIGEVGELERVEEVRIEVIVPESLLKKV
LKALKKAHPYEEPAYDIYPLENLGGGGGGGGGLLEEPELEEFFLLLKKKLLLTGVRVVVGLKKKVKKVVA
VGGGGGGAAAAAAAAAAADVVTTDDKYHHDHAAAEAGLILIDGGHHEEEEEKLLLKLLLLKKKAKAAALV
EEETNPVTNY
>gnl|CDD|442553 COG3324, VOC, Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only]
MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGDYAEFDTDGGQVGGLMPGAEEPGGPGWLLYFA
VDDLDAAVARVEAAGGTVLRPPTDIPPWGRFAVFRDPEGNRFGLWQPAA
>gnl|CDD|442554 COG3325, ChiA, Chitinase, GH18 family [Carbohydrate transport and metabolism]
SATASVSDTAAAATATSGKRVVGYFTQWGIYGRNYLVKDIPASKLTHINYAFANVDPDGKCSVGDAWAKP
SVDGAADDWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTWSKGFSDAAATPASRAAFVDSCVDLLRKYN
FDGIDIDWEYPGSGGAPGNVYRPEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGPDKLDGIELP
KVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGR
GWTGVTGGNNGLYQPATGPAPGTWEAGVNDYKDLKALYLGSNGYTRYWDDVAKAPYLYNGDTGTFISYDD
PRSIAAKADYVKDKGLGGVMFWELSGDTADGTLLNAIGEGL
>gnl|CDD|442555 COG3326, YsdA, Uncharacterized membrane protein YsdA, DUF1294 family [Function unknown]
MRLPLILLLYLLLINLLTFLLYGIDKRAARKGRWRIPEKTLLLLALLGGWPGALLGQQLFRHKTRKKSFR
IGFWLIVLLNLALLAWLLSF
>gnl|CDD|442556 COG3327, PaaX, DNA-binding transcriptional regulator PaaX (phenylacetic acid degradation) [Transcription]
MTPAVDDDLDQRPMRARSLLFTLYGDYLRPRGGWIWLGSLVRLLEPLGVSERAVRTALSRLVKRGWLESE
RRGRRSGYRLTPRGRRRLEEGDRRIYAFRPPTWDGRWTLVVFSVPESERELRHRLRRELTWLGFGTLAPG
VWIAPGPLAEAVRELLAELGLADYVTVFRAEHLGPGDLAELVARAWDLDELAARYREFLARFRPLLEALR
AGALDPEEAFALRTLLVHEWRRFLFRDPGLPAELLPADWPGARARELFRELYARLAPPAERHVDEVLETA
D
>gnl|CDD|442557 COG3328, IS285, Transposase (or an inactivated derivative) [Mobilome: prophages, transposons]
KTLTKELLEELLSELLEGDDLFDDLLRELLKELLEQALEAELDAHLGAEKYERTGGERGNSRNGYRERTV
KTRVGELELRVPRDRDGSFEPQLLPKYQRREQALEEVIIELYAKGVSTRDIEEALEELYGTGLSKSTVSR
ITDKLDEEVEAWQNRPLEERYPYVYLDAIYLKVREDGRVVNKAVYVALGVNEDGRKEVLGLWVGESESAA
FWLEVLRDLKNRGLKDVLLVVSDGLKGLPEAIEAVFPGARWQRCIVHKIRNSLKYVPKKDRKAVAADLKA
IYQAPTKEAAEAALDAFAEKWGKKYPKAAKSLEENWDELLTFFDFPAEIRRHIYTTNPIERLNREIRRRT
KVVGIFPNEEAALKLVYLALQEASKKWTMGIRRWKGMEALAQLAILFEDR
>gnl|CDD|442558 COG3329, COG3329, Uncharacterized conserved protein Alr0986 [Function unknown]
MDFLELLLANLLSPAVLFFVLGILAALLKSDLEIPEAIYKFLSIYLLLAIGLKGGVELAHSGLTEVLLPL
LAALLLGVLIPLIAFFILRRLGKLDRVDAAAIAAHYGSVSAVTFAAALAFLESQGISYEGYMVALLALME
SPAIIVALLLARRARSKKRATGEKVSWGELLHESLLNGSVVLLLGGLVIGLLTGPEGVEKIEPFFVDLFK
GVLALFLLDMGLVAARRLGDLRKVGLFLLAFGILMPLVNGLLGLGLGKLLGLSLGGAVLLAVLAASASYI
AVPAAMRLALPEANPSLYLTASLGITFPFNITIGIPLYLALAQALAG
>gnl|CDD|442559 COG3330, COG3330, Uncharacterized conserved protein BH1414 [Function unknown]
MTKSKSEPSSEEESEELEPAKLAPVDEDLGDLPDSYGEDRIVLLPRDPQWLYAYWDISPDTKERLRSQGG
HSSRLVLRLYDVTDIDFDGQNAHSVQEIEVDEEARNWYINVPEPDRDYRVELGYLTPDGRFLPLARSNIV
RTPRASPSDSIDERWMTIEEEYELLYRLSGGVGPSSPSILQELFERSSGSLYSST
>gnl|CDD|442560 COG3331, YotM, Penicillin-binding protein-related factor A, putative recombinase [General function prediction only]
MTINYPNGKKYTPKKKKKKWISYGNRGMTLEEDINETNEYYLERGIAVIHKKPTPIQIVKVDYPKRSAAV
ITEAYFRQASTTDYNGVYQGRYIDFEAKETKNKTSFPLKNIHEHQIEHMEQVEKQGGIAFLIIRFSKLDE
TYLLPAEDLIKFWDRAKNGGRKSIPYEEIEEEGYEIPSGYGPRLDYLEAVDKLLFER
>gnl|CDD|442561 COG3332, Tango2, Uncharacterized stress-responsive protein, TANGO2 (Transport and Golgi organisation 2) family, contains NRDE motif [General function prediction only]
MCLIAFAWQPHPDYPLVLAANRDEFYARPTAPPARWPDAPGVLAGRDLEAGGTWLGVNRHGRFAALTNRR
DPSGPPAGARSRGELVLDFLAGESAPAAYLALLALDAAAYNGFNLLVGDADRLFYLSNRGDALVRRLAPG
VHGLSNALLDTPWPKVARLKAALAAALAPDDPDPDALFALLADRTPAPDAELPDTGVGLEWERLLSSIFI
HGPGYGTRSSTLLALDADGRVEFAERRFDADGPPCGTRRFRFTLLSR
>gnl|CDD|442562 COG3333, COG3333, TctA family transporter [General function prediction only]
MDMLDNLLQGFAVALTPQNLLLILLGVLLGTIVGALPGLGPTMAVALLLPLTFGMDPTSALIMLAGIYYG
AMYGGSITAILLNIPGTPASAATTLDGYPMAKQGRAGKALGIAAIASFIGGLIGTIVLIFLAPPLAKVAL
KFGPPEYFALALLGLTAIASLSGGSLLKGLIAGLLGLLLATVGIDPITGVPRFTFGSPELLDGIDLVPVL
IGLFAISEVLRLLERGRAGAEAKAKLGGLLPTLKELKRSWPTILRGSLIGTFIGILPGAGATIASFLSYA
EAKRLSKHPEKFGKGAIEGVAAPEAANNAAAGGALIPLLTLGIPGSATTAVLLGALLIHGIQPGPLLFTE
NPDLVYGLIASLFIANILLLVLGLPLIRLFVKLLRIPRRILYPIILVLCVIGAYAINNSVFDVWLMLAFG
VLGYLMRKLGFPVAPLVLGFVLGPMAEENLRRALLLSGGDLSIFFTRPISLVLLALAVLSLLLPLLRRLR
RRR
>gnl|CDD|442563 COG3334, MotE, Flagellar motility protein MotE, a chaperone for MotC folding [Cell motility]
SSEAALLEELEERREELDAREAELDEREAELEALEKELEERIAELEELEAELEALLKRREEAEEEDLKRL
VKIYENMKPKAAAAILEEMDDEVAAGILSRMKPRKAAAILAEMDPEKAAELTELLAGRS
>gnl|CDD|442564 COG3335, COG3335, Transposase [Mobilome: prophages, transposons]
RLKLRVRKAAALLAARGLSSAGLALALALRARALKRRLGRRRLKVRLGPRALGSDLARPQELLLKALQQL
GLKLRAALRELLERLEERAAATSSSRGRRRRRGRRKGKQRKKRRAAKKAKAGKRRRGERLALLRKLSAGA
AVLVVLDAGDPTSGGGKRTNLIGALNLDGGLAVMVFDGSINGEVFIAFLEQLLLPYLKPGIVVILDNASF
HKSKAVREWLEEAGIELLFLPPYSPDLNPIERLWSKLKALLRKNRAFRSKDELKAAVRSFLDRISPDPER
VRNWFRHAGYAA
>gnl|CDD|442565 COG3336, CtaG, Cytochrome c oxidase assembly protein CtaG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
MLTGLLRLLTAWRFDPLLLLLLLLAAALYLRGVRRLRRRGDRWPVGRTVAFLAGLALLYLATGSPLDVYG
HVLFSAHMVQHMLLMMLAPPLLVLGAPVTLLLRALPRRLHSRVARVLTHPLVALLLFVGSFYVWYFPPLF
DAALRSHWGHLLMHVHFLLAGLLFWWPLLGPDPGPRRLPYLLRLLYLFATMPFHAFFGALLMFSTTLLYP
WYTALPRPWGLSPLADQQLGGGIMWIPGEIPYLVVLLALFVRWLRSDRREARRAADRDGDPE
>gnl|CDD|442566 COG3337, Cmr5, CRISPR-Cas system type III CMR-effector complex small subunit Cmr5 [Defense mechanisms]. CRISPR-Cas system type III CMR-effector complex small subunit Cmr5 is part of the Pathway/BioSystem: CRISPR-Cas system
MQTLEQQRAAFAYEKVKEVKEDKKVKKKYKSLVKKLPAMILQNGLGQTLAFLLSKGKKNKEDAHKALYEH
LAEWLKKRDPDVPDLNGKEDLLEALISADLAEYRRATREALALLNWLKRFAEALLKEEEEED
>gnl|CDD|442567 COG3338, Cah, Carbonic anhydrase [Inorganic ion transport and metabolism]
MKKRLLLALLLAAALPAAAAAAASAPHWSYEGETGPEHWGELSPEFATCATGKNQSPIDIRTAIKADLPP
LKFDYKPTPLEIVNNGHTIQVNVDPGSTLTVDGKRYELKQFHFHTPSEHTINGKSYPMEAHLVHKDADGE
LAVVGVLFEEGAENPALAKLWANLPLEAGEEVALDATIDLNDLLPEDRSYYRYSGSLTTPPCSEGVLWIV
LKQPITVSAEQIEAFARLYPNNARPVQPLNGRLILES
>gnl|CDD|442568 COG3339, YkvA, Uncharacterized membrane protein YkvA, DUF1232 family [Function unknown]
MKKSDFWDGKLKKLARRLPFLRRLLLLYYAGRDPRVPWKAKLLIAAALAYFVSPIDLIPDFIPVLGYLDD
LAVLALALALVIKEIPPEVREEAWEGAEDLFEAR
>gnl|CDD|442569 COG3340, PepE, Peptidase E [Amino acid transport and metabolism]
LLLTSGGTFNGSEYEYLDEALLELLGKGRPKVLFIPTASVGGDHDAYTAKFYEAFSKLGVKVSVLHLFSP
TFEDPVEALLEADVIFVGGGNTFNLLALWREHGLDDILREAVEAGTVYAGVSAGSNCWFPTIRTTNDGPP
PLRSFDGLGLVPFSINPHYDDEDMGETREPRIHEFLASNPLPPVYALDDGTALHVRGGKLEVVGEGAYRV
FR
>gnl|CDD|442570 COG3341, Rnh1, Ribonuclease HI-related protein, contains viroplasmin and RNaseH domains [General function prediction only]
KKKKFYAVWKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTKEEAEAALNGNYEDYKGKKKKLSEIELDSI
AVYVDGSCSGNPGVYEYGGVDTKTGKETFSELFHDGPFAEGTNNAGEFLAAVHALAYLKKKGSKLPIYSD
YRGAISWVKGKWKTKLERTQAYKELFDLIEKKNTYENPFVKVKTHSGDKWNEIPDDLARKALG
>gnl|CDD|442571 COG3342, COG3342, Uncharacterized conserved protein, Ntn-hydrolase superfamily [General function prediction only]
TFSIVARDPETGAFGVAVASSSPAVGARVPWARAGVGAVATQSFTNPALGPRGLALLAAGLSAEEALAAL
LAADPGREYRQLGVVDADGRTAAFTGAECLGWAGHATGDGYAVAGNMLAGEEVVEAMAAAFEAAAGPLAE
RLLAALEAGEAAGGDARGVQSAALLVVDPEGWPYVDLRVDDHEDPIAELRRLLEVYRPQFEAYVTRALD
>gnl|CDD|442572 COG3343, RpoE, DNA-directed RNA polymerase, delta subunit [Transcription]. DNA-directed RNA polymerase, delta subunit is part of the Pathway/BioSystem: RNA polymerase
LKELSKEQLKELSMIELAYEILEEKGEPMSFRDLIKEVAELKGLSDEELKERIAQFYTDLNIDGRFVSLG
ENRWGLREWYPVDQIDEEIA
>gnl|CDD|442573 COG3344, YkfC, Retron-type reverse transcriptase [Mobilome: prophages, transposons]
MSLRRITEKAKPDPGARFTSLLEKILSRENLLEAYKRVKANKGAAGIDGVTVEDFEEYLEENLYDLRERL
RSGSYRPQPVRRVEIPKPDGGVRPLGIPTVRDRVVQQAVKQVLEPIFEPDFSDSSYGFRPGRSAHDALKK
AREYINEGYRWVVDADIKKFFDNVDHDLLMKRLRRRIKDKRVLRLIRRWLKAGVMEDGVVEEREEGTPQG
GPLSPLLANIYLHELDKELERRGHRFVRYADDFVILCRSKRAAERVLESLTERLEKLGLELNPEKTRIVR
PGDGFKFLGFSFRRGKGLGFKFRPRKSKRKKKRKRRRRTRRRSRKRRRRIRRLLRRLLLGWRRYLLLAEL
KRLLNALLRGRRRYYRRLWRKRRKKLRRRLRLLLLRRARRRRAKRRARGRKRRWRIAASALLSPLLLAHY
LLLLLLVLLSRYAL
>gnl|CDD|442574 COG3345, GalA, Alpha-galactosidase [Carbohydrate transport and metabolism]
MVLAYSDGGLDGASRRLHRYVRARLAPGPPDKPRPVGWNSWEAYYFDFTEEKLLALADAAAELGVELFVL
DDGWFGGRRDDTAGLGDWLVDPEKFPNGLKPLADRIHALGMKFGLWVEPEMVNPDSDLYREHPDWVLKDP
DGEPVEGRNQYVLDLSNPEVRDYLFEVLDRLLAEWGIDYIKWDFNRDLTEAGSLPGERQGEGLHRYVLGL
YRLLDRLRA
>gnl|CDD|442575 COG3346, Shy1, Cytochrome oxidase assembly protein ShyY1 [Posttranslational modification, protein turnover, chaperones]
MTAPLRPRWLGLLLLALVLAAVLVALGFWQLQRAEEKEALIARIEARLAAPPVPLPELLAWPAAFPADDE
YRRVTVTGRYLPDHQVLLDNRTLDGRPGYEVLTPLRLDDGRAVLVNRGWVPAGADRAALPRVPAPPAGEV
TVTGRLRPPEPRGSFLPGNDPPEGQVQSIDLAALAAALGLPLAPYVLDLDAESPGGLRPWPPPVLDPGRH
LGYALQWFALALAALGLYVYLARRERRERRADAAE
>gnl|CDD|442576 COG3347, RhaD, Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism]
MKNLWDDAEAAALVGEELALLVYRSRLLGADPRLVNHGGGNTSVKTTETDLTGEEVEVLWVKGSGGDLAT
IEPAGFAALRLDPLRALRELGVLSDDEMVNLLRHCLFDLNAPAPSIETLLHAFLPHKHVDHTHPDAVIAI
ANAPDGEELTREIFGDRVGWVPYVRPGFDLALALAEAFRANPGAEGVVLGKHGLFTWGDTAKESYERTIE
LINRAEEYLAAHGAAVPAAKYASLPAPERRALAAALAPVLRGAVSRERRMIGHFRDSPAVLEFVNSADLA
RLAQLGTSCPDHFIRTKIRPLVLDADPDADDLDALKARLEAAVAAYRAEYRAYFERHAAGDSPAMLDPNP
RVVLVPGVGMFGFGKDKKEARIAADFYENAINVMRGAEAVGRYVPLPEQEAFDIEYWLLEQAKLQRMPKP
KPLAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGADAVDATDVDVTAEAA
VAAAFGFAGLDIGGSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGLGGSSV
FAVSKNAAAAAYGAAAAATAKAAAQHLLRALAAEGGANGINANRVNPDAVLDGSAIWASAARAERAAAYG
IGNLLLEEVYRKRVALAVLVLAEDIAEAAAFFASDGGNKATGGR
>gnl|CDD|442577 COG3349, COG3349, Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only]
MMPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFPDPDTGLPIDNGQHVLLGCYRNTLD
LLRRIGAADNLVGPEPLQFPLPGGRRWTLRAPRLPAPLHLLRALLRAPGLSLADRLALLRLLTACRERRW
RELDDISVADWLRRHGQSPRLIRRLWEPLLLAALNTPPEQASARLALTVLRETLLAGPAASDLLVPRGPL
SELFVDPALAYLEARGGEVRLGTRVRALEFDGGRVTGLVLADGETVPADAVVLAVPPEVAARLLPELARL
PELGLLAPLEYSPIVNVHLWLDRPVTLGPPPFAGLVGSTSQWVFDRGAGDGGQGGVLSVVISAADRLLDL
SREELAAEVWAELAALLPAAREALPVWSRVVREKRATFAATPGSDRLRPGARTPIPNLFLAGDWTATGLP
ATMEGAVRSGRRAANAILARLGRPA
>gnl|CDD|442578 COG3350, YHS, Heavy metal-bindng TRASH/YHS domain, predicted Cu/Ag metallochaperone [Inorganic ion transport and metabolism]
MKGVAMVIDPVCGMTVDPGSAAYTAEYDGKTYYFCSEECRDKFKANPEKYLPQYGG
>gnl|CDD|442579 COG3351, FlaD, Archaellum component ArlD/FlaD/FlaE [Cell motility]
DGGSKPYLETLPEDYVAELVVFEWLEFLVERVGYNGAADALDYYEEIGWISEDVRDELLDYLRGFDPGNE
VPDWEPPSKLTVDDHTRSLLYIERLAGRKIDRDLLDRLEREVDGIKRG
>gnl|CDD|442580 COG3352, FlaC, Archaellum component ArlC/FlaC [Cell motility]
GEDNEAIEELEERINEIENELPKISSTISTVRKENEEIKETVDKIDENVKDLLSLYEVVSNQVNPFVGDV
SGEAAGKGGGLGGSKEDGSEDDDDEDDLADAEEEDEDDEDLAEDDEDDDDDIDGDTDDEDLDDDEDEGDD
ENDDEDDDEDEDDDADDSSDDDGEEEEDEDSEDDEDDDDDEDDGEEEGDDEGEELDSVVTLDDADEEEGD
DIGNLAEGDDEDYEDDDGDESDDEGSDDDDAAEDEPDYAPDIDLLPEDDDAELSEEEDEE
>gnl|CDD|442581 COG3353, FlaF, Archaellum component FlaF, FlaF/FlaG flagellin family [Cell motility]
MGFSVSGSAAIIFIGVLIAFGILYTAASNSFERVSDANDDQYDRALERLNTAITITSATYDSSSSTLTVN
VTNTGSTTLSVSDTDVLVDGTYVTDSTTVVDGDSSTDLWLPGETLTITVTTDSTGPHRVKVVTENGVADT
EVVS
>gnl|CDD|442582 COG3354, FlaG, Archaellum component FlaG, FlaF/FlaG flagellin family [Cell motility]
MASVSASHLILFIASLLIAAGVAGTLTTEVTNISDSVEDRGDDVSEQIRTDIAIISDPGSAVYDDTNETV
TFYVKNTGSRTLPADPTAIDVLVDGEYVTPVNVTVVDGGDSVWRPGDVLEITVTVTDDLSPGDHRVTVVV
NGDEESFEFRT
>gnl|CDD|442583 COG3355, COG3355, Predicted transcriptional regulator [Transcription]
MSDSIEMLVRLEPDLEDVLECVYGLSETDAEVYLILLENGEPLTVEELAEALDRSRSTVYRSLQKLLEAG
LVEREKRNLEGGGYPYVYYAIDPEELKEKLVDDLDEWYEKVGELIEEFEEEKADPLAITWE
>gnl|CDD|442584 COG3356, COG3356, Predicted membrane-associated lipid hydrolase, neutral ceramidase superfamily [Lipid transport and metabolism]
MTAVSRILARLSRYIFRAPSWYISLAIIILIAAIIGAVSFDSILEDAWFGIFLFGVPAIIAALLTTPFID
ILGGRLTLNRSLLLALFSLLIWLLIYLIGILISVVLGKPLGLDALVLGLALIFAFRLLVLYAVSRASLIK
AALPASIQPLAIALVLVLYSGTLSDPPTFFLKLIVLSLVFALAAYLFIVVIDRPFRRSLGVSALDFLQAF
LAHLTEGSRELEEFFEEIGEERDVPVTVIRFRREGKNKARFVLPDIHPGPFGEIGGSNLPYRLAKRFDGS
AMVMHGTATHDFNLVSEREVDKILDAVKNALEKIEYSSTASKPVRVQSGDARVTGQRFGDTALLVLTRSP
KGMDDIPYAVGLELMAEAKKRGFEDVLLVDAHNCMGGEAGELPGSEDAFDLIKAAKKALKELREAPQYPL
KVGYARSETPWSREDGIGPLGIQVLVLEVGGQKTAYVLIDGNNMEPGLREKIRDALSKLGVDEVEVMTTD
THVVNTVRGSLGYNPVGSAIDPEEIIKWVLELVKEAIADLEPVEAGMATERAEVKVFGNDRFETLASTVN
ASVSITKALAAAIFLLAILLSFLAFFYL
>gnl|CDD|442585 COG3357, COG3357, Predicted transcriptional regulator, contains HTH and Zn-ribbon domains [Transcription]
TTRERIAELLRESPLTASELARILGISEKEVYEHLEHIAKSLKRKDERLLVAPPECRDCGFVFFDDRLNK
PSRCPRCKSERIEEPRFRIEEK
>gnl|CDD|442586 COG3358, COG3358, Uncharacterized conserved protein, DUF1684 family [Function unknown]
MTKTLLAYAAATDADDYAAEWEAWRAERDAEFADPPGSPLPAPARKAFKGLDYFPPDPAWRVEARFEPTP
DPETVEIPTTTGGTVEYERPGTVEFELDGKEYRLTAYQSAYGGGLFLPFRDATSGKETYGGGRYLDLTIP
DDDGTVVLDFNRAYNPPCAYSPYYTCPLPPAENRLPVAVEAGEKAYRK
>gnl|CDD|442587 COG3359, YprB, Uncharacterized conserved protein YprB, contains RNaseH-like and TPR domains [General function prediction only]
DARDAYFFAELLPSEDLLFFDIETTGLSGGGTVIFLIGLADGEGDGFVVRQYFGEDPGEEAALLEAFLEW
LADYKLLVTYNGKSFDLPFLKTRFTLHRLPPPLPEFPHLDLLHPARRLWKNRLPSGGLKTVEELLGIERE
DDLPGYEAPRLYRRYLRTGDPEALETLLEHNREDVLNLATLLEHLYNRLLEDTFAPAE
>gnl|CDD|442588 COG3360, COG3360, Flavin-binding protein dodecin [General function prediction only]
SMHVYKVIELVGSSPKSWEDAVQNAIARASKTLRNIRWFEVVEQRGHVEDGKIAEYQVNLKVGFRLED
>gnl|CDD|442589 COG3361, YqjF, Uncharacterized conserved protein YqjF, DUF2071 family [Function unknown]
APLPVGRPFLTQRWRDLLFLHWPVDPEVLAPLLPAGLELDTFDGSAWVSLVPFRMEDVRPRGLPAVPGLS
TFPELNVRTYVRRDGRPGVYFFSLDAPRRLAVLVARTLFGLPYYWARMRVRRDGDRVRYRSRRRGPGPRG
ARFRATYRPGGPPFPAEPGSLEHFLTERYRLYTRRDGRLLRGEVHHPPWPLQPAELTILDNTLFAAAGLP
APDGPPLVHYSPGVDVRVGPPRRLR
>gnl|CDD|442590 COG3363, PurO, Archaeal IMP cyclohydrolase [Nucleotide transport and metabolism]. Archaeal IMP cyclohydrolase is part of the Pathway/BioSystem: Purine biosynthesis
MYVGRFIVVGPSEDGRAVAAYRVSSRSFPNRNRVERDDGLTVGPTDDAPLTDNPYISYNCVRVVGGIAVV
TNGSHTDPIAEKLELGYPARDALAESLLARDYEKDDYNTPRIAGVVGGDGEAYLGIVRSDALLVEEVDRQ
AGEGTLVATYEKDGPPLPSFEGEDAEEAADEIWDSLDFEHPVCAAGATIDGDGFETAIYNKEE
>gnl|CDD|442591 COG3364, COG3364, Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only]
MPHKCTKCGKIFEDGSKEILKGCPSCGGKKFLYVKEEKRAKDVEEEKSAEKIIEEVDELLEVEPSLKEIP
EEDGDRIESIRILGPGSYELNLESLLERDEIVMALKEEGTYAIDLPSMFKKKKKKKK
>gnl|CDD|442592 COG3365, COG3365, Uncharacterized conserved protein, DUF2073 family [Function unknown]
MDDGVQIDLISKERLEKMTSMEKIRLILDKVREGKIVVLEEGLTPEEESKLIEMTMTEIDPDGFSGIEIE
TYPAKETSDKSFLGRLLGKKSSRRLTVIGPANQLKTLKKDKDLISALVSLK
>gnl|CDD|442593 COG3366, COG3366, Uncharacterized membrane protein [Function unknown]
SLIIDLLLLVLDLLVRILPLIFIGLFLANLIVELGLVQKLSRLARPLTRFANLPDECGASFLVAFVSPTA
ANSMLAEFYKEGKISDRELILASLINSFPAFLRHLFTYQLPVLLPLLGVVGLIYVGLRLLIGLLKTLIGL
LAGRLLLRPRNVSIPEPEPEEKRSLREALKKALKKTKKRLRRIVPITLPVYFLVFFLIETGFFDYLTELV
APLASLLGLPPEAIPVITAYFASPIAGYAAAGPLLNEGSLTPKQAVITLLLGNVLSSPVRALRHSLPYYV
GIFGPKLGLKLIAISTGLRILSIILVLLVLLL
>gnl|CDD|442594 COG3367, COG3367, Uncharacterized conserved protein, NAD-dependent epimerase/dehydratase family [General function prediction only]
LMIKKPALLLLGGAFDPLDAKTAHGLVRYSPYDIVGVIDSTGAGADAGEVLDGKRGIPIVASLAEALAAG
ADTLVIGIAPAGGVLPEEWRAVILEALEAGLDIVSGLHEFLSDDPELAALAKRHGVTLIDVRKPPKDLPV
ATGRIREVSGKRVLTVGTDCAVGKMTTALELERALRARGIKADFIATGQTGIMIAGYGIPLDAVVADFVA
GAVEQLVPEAAEDPDWDVIEGQGSLFHPAYSGVTLGLLHGSQPDALVLCHEPGRKHIRGFPHYPIPPLEE
EIDLYEALARLNPDAKVVGIALNTSGLSEEEARAAIAEYEAELGLPATDPLRFGADKLVDALLALFP
>gnl|CDD|442595 COG3368, COG3368, Predicted permease [General function prediction only]
MNLEIVKVIYREVHYRIMKDNPRLSNSPKKIKKQLKFSLNIKLTYGSQSLAYLFFGIMLASSIFISSNTD
AISSFFSILFILPFIFSLYSTSVFFAYVASNDLFEPLKSLPIKVGGRYLSVLLFIDSLPAIFFVLPSIAV
LLVGNLYTILLSLLWAFAAILLGHSLGLLLFIISSGKGKGHSLKSLLKILGIFLFLGIFYLLIYDQEYLL
RNYESYIAILPYYSIAFPFSALTIIYPFFSLLLLLLYLAIFAVIYYYLILRLWESLLEGEEVEGKESTKY
KIKSGSPLLAFLKKDFKIIFRKTQNLTGFLVPLYIVIPFIFGVIKIGKFPLSLAFIIIFAIGFFSTFSAD
MLLKIELEGIEFLRSLPIKKRSFAMGKALFMSIIPSAISIAVLILAFAYNGLSSLFLLPIAFLIPLLTSS
INMLYKKHPKGTEINYPSLGFLDGIVLLILSGIIFGIIAIPLFFLSIPLSYIISSIIDLIIGLLLIWKL
>gnl|CDD|442596 COG3369, COG3369, Uncharacterized conserved protein, contains Zn-finger domain of CDGSH type [Function unknown]
MSEVKITVAKNGPLLVEGDVEIVDADGNEYEEGKRYALCRCGLSKNKPFCDGSHKGTGFEPEGEAAEY
>gnl|CDD|442597 COG3370, COG3370, Uncharacterized conserved protein AF1964, DsrE/DsrF-like family [General function prediction only]
MAKLLVLITSGDDEEKAKMALMYALNSLKKNWWEDVKVIFWGPSVKLLAEDEEEVQELIKELIKAGVKVS
ACKACADNLGVTEKLEKLGIEVEYAGEPLTELLKEGYQVLTF
>gnl|CDD|442598 COG3371, COG3371, Uncharacterized membrane protein [Function unknown]
MRMDSRRLAGLLGIIAPIIALLGILIAIALNPWFSITKNALSDLGSPVGPTAWIFNGGLIVTGLLVLLFA
IALLRVSNKVERAGSALLILAGLGLALVGVFPEGTGRPHLFVALWFFLLGSLAAIVYGIGLLLSGRKPRG
ILSVLLGVISLGILWILALYARIPPGVAGPERVGAYPILIWVIALGGYLLGRRK
>gnl|CDD|442599 COG3372, COG3372, Predicted nuclease of restriction endonuclease-like (RecB) superfamily, implicated in nucleotide excision repair [General function prediction only]
MLTSDLLRVRRRGGTIVPKFLDIDRELLELAAELIAIFEAHVGETRGELEEALEELEGESTDYKLVRGLA
KLLEDRCTFETVAPLDPEELRRAVFEAAAAVLGVPSEEEREAVLARVADRLGVSPEELEAGLYADLEENQ
ILTEFDAPTPEALLHRYNLALAQGILYRATEVRIRASDNDPGEYKLLFRYLKFLRLMYEIERDDDGGYTL
TIDGPTSLFKSTTRYGLALAKLLPALLHCEEWELRATIDDRGTERKERTFTLSSEDGLVSHYPAGKPYDS
MVEADFAERFEALDTDWTLEREPEPLPLGGSVMIPDFALEHPDTGRRVYLEIVGFWTPEYLEKKLEQLRR
AEDVNLLLAVSERLNVSEGVEIEAVPARVVWFKGKLSPKDVLEVLERYEEELV
>gnl|CDD|442600 COG3373, COG3373, Predicted transcriptional regulator, contains HTH domain [Transcription]
MEGESSIFIDPHIYRSLNKSKVRKKILLYLYSIYPEATYLSEISRRVRSDPSNVRGALEGMGKRYNGESS
LIELGLVECIERKGVKIYSLTEYGKRVVEYLRDYDRDYRPFL
>gnl|CDD|442601 COG3374, COG3374, Uncharacterized membrane protein [Function unknown]
MAMFIDPLTLMLMALAAGLLLLAYYVYKNAGGKAIDEALKSLGAPFLAVGLFALITGLWMTFTWPLPGSY
NILFGDPYLLFGILLLAAGIAIYKGWDLRYLGILALFLGLYLIVYGVAIYNLGLTKEPLAAGGLYILTGL
AGILSPPVYLKPDNVGKVLAYIAAILLILAALIAAFIGYEAVYGHLAGFGKWPPWPG
>gnl|CDD|442602 COG3375, COG3375, Predicted acetyltransferase, GNAT superfamily [General function prediction only]
MAAGVEIRELTTPAELEAVQRLQRSVWGSPPNEPVPVHLLRALAHAGGYVLGAFDGGELVGFSFGFPGFR
PGGLYLHSHMAGVLPEYRGRGVGYALKLHQREWALERGVTLITWTFDPLQARNAYFNLAKLGAIAREYLP
NFYGEMRDGINRGLPTDRLLVEWDLDSPRVRAALAGRPEPLEDAGAVVALERGADGLPVVGEVPLDAPVV
LVAVPADIEALRRTDPALARRWRLATREALGALFAAGYRVTGFDRDGEGWYVLVRRSLDAL
>gnl|CDD|442603 COG3376, HoxN, High-affinity nickel/cobalt permease [Inorganic ion transport and metabolism]
MTATAARSLRRRLAALFAALAALHVLGWGLLLAAFAAYPVLLGLALLAYTFGLRHAFDADHIAAIDNTTR
KLMQEGKRPVSVGFFFSLGHSTVVILAALLIAAGARAAQDDIPALHEIGGLIGTLVSGLFLLLIALLNLV
ILLGIWRVFRRVRRGEYDEEELDELLASRGLLARLFRPLFRLVSKSWHMYPVGFLFGLGFDTATEIGLLA
LSATAAAAGLPWWAILVFPLLFAAGMSLVDTLDGVLMSGAYGWAFSNPLRKLYYNLTITGLSVVVALVIG
GIELLGLLADKLGLTGGFWDWIAGLNLGNLGYAIVGLFVLTWLVSLLIWRLGRYDERESAAP
>gnl|CDD|442604 COG3377, YunC, Uncharacterized conserved protein YunC, DUF1805 family [Function unknown]
MMEVEPIELEGGTFLGVKVELPKTPLLTIKGEKGYIMCGALDVEALNKRGIVAARVSGVKTIEDLLNAPV
ESVTTAAEELGIEPGMTGREALEKM
>gnl|CDD|442605 COG3378, COG3378, DNA primase, phage- or plasmid-associated [Mobilome: prophages, transposons]
YVPETGKWYVYDGGRWEEDDGEVRRLIKELLRAILAKWAKKSRSSRRIKAVLELLKAELPDELDADPNLI
NVKNGVLDLRTGELRPHSPEDYLTKVLPVEYDPDAKCPRWLKFLDEIFPGDKELIDLLQEALGYCLTGRT
SEQKFFFLYGPGGNGKSTFLNLLTALLGKDNASSASLETLTENRFDLARLKGKRLNIASELEEGYRLDES
LLKALTGGDPITARRKYKDPFSFKPTAKLLFATNHLPRIRDTDDGIWRRLLIIPFNVTFPEEERDPNLKE
KLLEELPGILNWALEGLLRLLENGGLTEPESVKEATEEYREESDPLGAFLEECCELDPGARVPKKDLYEA
YREWCEDNGEKPLSKRTFGKELKKLGFEYEKRRTNGGKRRGYRGIRLKDDSDS
>gnl|CDD|442606 COG3379, COG3379, Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only]
MGDMPRVLVIGLDGAPPDLLDPWIARGELPNLARLAEEGAYGRLRSTIPPITPPAWTSMMTGRNPGEHGV
YGFRDREPGSYDTRVANSRDVRAPTLWDILSRAGKRVTVLNVPVTYPPRPVNGVMVSGFLTPDLLGDATY
PPELADELEALVGDYRIDVNAKLRPDDKEELLEDLYETLEKRFEAARHLLEEDDWDLFMVVFMGTDRVQH
FLWHYYDPDHPLYDPDGPYRDAILDYYRALDRYIGELLELAGDDTTVVVVSDHGFGPLDGEVNINEWLEE
EGYLSLKDDPPDRLREPTPLSADDIDWSRTRAYSLGGYYGRIFLNLKGREPQGIVPPAEYEAVRDELIAD
LEALRDPETGEPVVTRVVRREEAYRGPHGDIAPDLVVIPDDGFWRSIGVGSPKVFDPPTGPRTGTHRPDG
IFLAAGPGIAPGARLEDADLYDVAPTILALLGLPVPRDMDGRVLVEAFARLR
>gnl|CDD|442607 COG3380, COG3380, Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]
MSMPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRMATRRLDGGRFDHGAQYFTARDPRFQALV
EEWLAAGLVAPWTFDFVVLDADGLVSPRDDGEPRYVGVPGMNALAKHLAAGLDVRLGTRVTALERDGDGW
RLTDEDGEEYGPFDAVVLAIPAPQAAALLEPSLAPELAAALASVRYRPCWAVMLGFDQPLDPDWDAAFVD
DGPLAWIARDSSKPGRPGEEAWVLHASPEWSREHLDDDPEEVAAALLAAFAELLGLPLAEPDWAQAHRWR
YALPEAPLGAPFLWDADLGLGLCGDWCAGGRVEGAWLSGLALARALLARLA
>gnl|CDD|442608 COG3381, TorD, Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational modification, protein turnover, chaperones]
MTETTAELEARAALYRLLARLFYREPDEELLEALASGELLDDLPADEELAEALAALASAAAEDDLEELAA
EYTRLFIGPGRPPAPPYESVYLDEEGLLFGESTLEVRAFYRALGLELDEDFKEPEDHIALELEFMAYLAE
REAEALELLEAQREFLEEHLLPWAPRFLDDLEAHAETPFYRALAELLRAFLEADREELEELLEEA
>gnl|CDD|442609 COG3382, B3/B4, B3/B4 domain (DNA/RNA-binding domain of Phe-tRNA-synthetase) [General function prediction only]
MKFSIDPEVFELFPGLRIGVIVAKGVDNTESPPELEALLQEAEEEARARLTLEPLKELPVIAAWREAYKK
FGIDPKRYRPSAEALLRRVLKGGGLPRINPLVDLYNAVSLRYLLPIGGYDLDKIEGDLRLRLARGGESFL
PIGGDEEEPPEPGEVVYADDEGVFCRRWPWRDSERTKVTEETKNALFIIEGLPGVSAEDLEAALDELAEL
LERYLGGEVVKTRILDADNPEFE
>gnl|CDD|442610 COG3383, YjgC, Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]
SNPMKKVKTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRG
GEFREVSWDEALDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMAS
AVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLAD
LHLQIKPGTDLALLNGLLHVIIEEGLVDEDFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAAR
LIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRDMGALPNVLPG
YRDVTDPEHRAKVADAWGVPPLPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLE
FLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAELARRLGYGF
DYDSPEEVFDEIARLTPDYSGISYERLEALGGVQWPCPSEDHPGTPRLFTGRFPTPDGKARFVPVEYRPP
AELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVV
LRARVTDRVRPGTVFMPFHWGEGAANALTNDALDPVSKQPEYKACAVRVEKVAE
>gnl|CDD|442611 COG3384, LigB, Aromatic ring-opening dioxygenase, catalytic subunit, LigB family [Secondary metabolites biosynthesis, transport and catabolism]
MGRLPALFISHGSPMNALEDGALTAALRRLGRRLPRPDAILVVSAHWETRGTTVTAAARPETIYDFYGFP
PELYELQYPAPGDPELAERVAELLAAAGLPVRLDPERGLDHGTWVPLRLMYPDADIPVVQLSLDPTLDPA
EHYALGRALAPLRDEGVLIIGSGSLVHNLRALRWGPGDAIPSPWAEEFDDWLLEALAAGDHDALLDYRPA
PYARLAHPTEEHLLPLLVALGAAGDDAKARVFHDGVEYGSLSMRSVQFGV
>gnl|CDD|442612 COG3385, InsG, IS4 transposase InsG [Mobilome: prophages, transposons]
MSKRNSLSLLDQVLRKLLLKFPSEGKELKARLSLLQIRERLVALLLVTISLRLLLADGSSRTLAGFKRSY
SVAMSESISPSSLNQRLTAELLRDLFEHLLDELAQVTPTLGHRLWIFRDVLILDSTTIRLHLSLFDWAAF
RTTKAGVKLHVLLNLTTQLPEFIAITDGKTHDVKQLKTLPWPKGSIVVFDRGYYDYRLFARIDENGGFFV
TRLKKNANYRVVEELRVPRGRGILSDQLVELTGAGTQKKYPKKLRLVGVRDEETGKYHEFLTNNFDLSAE
TIADLYRSRWEIELFFKELKQHLKIKAFLGTSENAVEIQIWTALITYLLLRYLKKLAKESWSFSQLARLL
LLNLFEYLGIWLLELLRPPAPDPPKRRNQLALFKA
>gnl|CDD|442613 COG3386, YvrE, Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]. Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
KLADAGFRLGEGPVWDPDGRLYWVDIPGGRIHRYDPDGGAVEVFAEPSGRPNGLAFDPDGRLLVADHGRG
LVRFDPADGEVTVLADEYGKPLNRPNDGVVDPDGRLYFTDMGEYLPTGALYRVDPDGSLRVLADGLTFPN
GIAFSPDGRTLYVADTGAGRIYRFDLDADGTLGNRRVFADLPDGPGGPDGLAVDADGNLWVALWGGGGVV
RFDPDGELLGRIELPERRPTNVAFGGPDLRTLYVTTARSLPLAGALFRVRVDVPGL
>gnl|CDD|442614 COG3387, SGA1, Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and metabolism]
MSAPIEDYGLIGNGRTAALVDRDGSIDWLCLPRFDSPSVFAALLDDEKGGRFSIAPEGPWRSTQRYLPDT
LVLETRFETDDGVLEVTDFMPRFPYDRPPDLVRRVEGVSGEVRIRVFFRPRFDYGRTDPWVTRGSNGIRY
VGGPDTLRLTSNVPLGSDSAIRAEFTLEAGETVYFVLGYGESLEEPPLPEDAEEALERTEEYWREWVSRL
TYPGPWREAVIRSALTLKLLTYEPTGAIVAAPTTSLPEEIGGERNWDYRYCWLRDAAFTLYALLRLGYTE
EAERFFRWLLRAVAGDGGYLQPMYGIDGERGLPERELDHLSGYRGSRPVRIGNAAALQIQLDVYGEVLDA
LYQYYKDGGDLDEDLWRLLRALADFLARHWPEPDAGIWEERGEPRHFTYSKVMCWVALDRAARLAELLGL
PAPAERWRALADEIRAEILERGWDEERGAFVQAYGSDTLDASLLLLPLVGFLPPDDPRVVSTVEAIEREL
RVDGLVYRYRTDDGLGGPEGPFLICTFWLVEALARIGRLDEARELFERLLAYANPLGLLSEEIDPETGEP
LGNFPQAFSHLGLINAALRLSRALD
>gnl|CDD|442615 COG3388, COG3388, Predicted transcriptional regulator [Transcription]
MFDRLEEEVELLERHLEVLKAVIENQPIGIIKLSEETGLPEHKVRYSLRVLEQEGLIEPSPEGAVTTDDT
EEFLEELDEGLDELIERLEEIKEEGKSIL
>gnl|CDD|442616 COG3389, COG3389, Presenilin-like membrane protease, A22 family [Posttranslational modification, protein turnover, chaperones]
MSSRTREYVPVGGMVGLFLLVQLGALALVPPFEEAGYQAVEDPEDPTNSLLYIGAILVATALMLAAFKYD
LQWLIRALIVLASGLLSWYVFSALVPPLVTVGLVNVLALLLAAAVGAALYVYPEWYVIDAAGVLMGAGAA
ALFGISFGLLPALVLLSVLAVYDAISVYGTEHMLDLAEGVMDLKIPVLLVIPTTLSYSFLDDDFPEGEGS
AEDDAEEADETDDADEDDPGERDAFFIGLGDAVMPTILVASAAFFLPAPTLGVPGLALNLPALGAMVGTL
VGLLVLLWMVMKGRAHAGLPLLNGGAIGGYLLGALASGVPLLEALGL
>gnl|CDD|442617 COG3390, COG3390, Replication protein A (RPA) family protein [Replication, recombination and repair]
MPTREVARRVFAAEFNDATLSFKESDDERAPNYVLTPTGARVNRVFVVGVLTEKEDVGDDSEYWRGRVVD
PTGAFVVYAGQYQPEAAAFLEEIEPPAFVAVVGKPRTYETDDGRVYVSVRPESITVVDAETRDRWVVDTA
ERTLDRIEAFAEALSRGDALRDALKEAGVSEGLAEGIPLAIEHYGTDPEYYRALRILAALALEVVAGERD
EVEALDLAPDEEGADLEAGLSDDDAEDETDLASEAQEELDEEVDADDEDALEDALGEEEESAEEKEEA
>gnl|CDD|442618 COG3391, YncE, DNA-binding beta-propeller fold protein YncE [General function prediction only]
ALVASSLLVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADA
DGADAGADGRRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTA
TGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSNTVSVIVSVIDTATGKVVATIPVGGGPVGVAVSPDGR
RLYVANRGSNTSNGGSNTVSVIDLATL
>gnl|CDD|442619 COG3392, COG3392, Adenine-specific DNA methylase [Replication, recombination and repair]
MYPTIRYIGSKRKLLPFIEEVISEVVIEGESFLDLFAGTGVVSRAFKKHGKRVIANDLEYYSYVLNKAYI
ENNSEPLFEKLGPYEELLAYLNRLPPEDGFISENYCPAGSGERLYFSDENAKKIDAIREEIEELKLDGIN
ENEYAILLASLIYAADKVANTAGVYGAYLKDWLKRAEKPLELEPPEFIDNGKENEVFNGDANELIKKIEA
DLVYLDPPYNSRQYGSNYHLLETIARYDKPEIKGKTGLRDWREYRSPFCSKRGALDAFEDLISNAKAKYI
LLSYNSEGLISLEEIIEILSKYGKVEVFEIDYKRFRGGRNRNSKKNRVTEYLFLLKKR
>gnl|CDD|442620 COG3393, COG3393, Predicted acetyltransferase, GNAT family [General function prediction only]
ELVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERL
GFRPVGEYATVLFRKP
>gnl|CDD|442621 COG3394, ChbG, Chitooligosaccharide deacetylase ChbG, YdjC/CelG family [Carbohydrate transport and metabolism]
KKLIVNADDFGLSPGVNEAIIEAHREGILTSTSLMVNGPAFPEAAALARENPGLDVGLHLTLTSGRPLTP
PEEVPSLVDEDGRFFPSLGRLGVRAFLGRADLDEVEAELRAQIERFLAAGLPPTHLDSHQHVHLHPGVLE
AVLDLAKEYGLPAVRLPREPAPAILRRPGLAALARGARRRARRAGLPTNDGFFGLFYSGKMTEERLLRLL
DALPPGVTEIMCHPGFVDPELRAISSYTYPREAELAALTSPEVKEALEERGIELITYRDLR
>gnl|CDD|442622 COG3395, OtnK, D-threonate/D-erythronate kinase OtnK and related C4-acid sugar kinases, YgbK/DUF1537 family [Carbohydrate transport and metabolism]
KLGVIADDFTGATDVAVQLARAGLRTVLLLGVPTLALADDADAVVIATKSRSLPPEEAVARVREALAWLK
AAGARLVYKKFDSTLRGNIGAETDALLDALGADAAVVVPAFPENGRTTVGGHLFVGGVPLHETEMARDPV
TPMTESDLPRLLAEQTKGPVGLVDLADVRAGAEALRAALAALAAEGARIVVVDAVTDADLDAIAEALADL
AERVLVVGSSGLAAALAAAPAALPPAGGPVLVVVGSCSPVTRRQLAALLAEPGVPVVELDVERLLDGEAE
AEVERALAWALAALAAGRTVLIYTSRDPEDVADAQERLGRLAAGERIEAALAEIARRLLEEAGVRRLIVA
GGDTSGAVLKALGIRGLRILGEIAPGVPLGRAIGGDFDGLPVVLKGGNFGDEDFFARALEGLEGK
>gnl|CDD|442623 COG3396, YdbO, 1,2-phenylacetyl-CoA epoxidase, catalytic subunit [Secondary metabolites biosynthesis, transport and catabolism]
MTTEKIEPRDWMPEEYRKALIRYLLRLADDELILAQRLSEWCGRAPTLEEDIALANIAQDELGHARLLYT
LAEELEGAGRDEDDLAYLRDEGEFRNSLLVEQPNGDWADTIARQFLFDAAAILLLEALARSSDAPLAAIA
AKICKEESYHLRHGEEWVIRLGDGTEESRERMQAALDRLWPYTLELFGPDDVEEALAAAGIKVDNDELRQ
EWLATVVPVLEEAGLTVPDEPVARGGGRQGRHTEHLGYLLAEMQYLQRAYPGAT
>gnl|CDD|442624 COG3397, COG3397, Predicted carbohydrate-binding protein, contains CBM5 and CBM33 domains [General function prediction only]
MMRRRRLLLAAALAALLALLLAAGPASAHGYVESPASRAYLCYLDGGEDAAPQNPACWAAVAAGPQAQYE
WQSVLREGPKGFPQAGIPDGQLCSAGRARFSGLDLQRGDWPKTPVTAGANFTFTWTATAPHATTYWRYYI
TKQGWDPTQPLTWSDLELVPFCTVTDPGARPGGTYTHTVNLPAGRSGRHVIYAVWQRSDTAEAFYNCSDV
NFGGGGGTPPWTAAGTSVEITTPPTPPPPSTPATTPTPSTTTTGSGGATTVATSTTAGGAVTTTTTVVNT
GAGATGGEAATTTD
>gnl|CDD|442625 COG3398, COG3398, Predicted transcriptional regulator, contains two HTH domains [Transcription]
RFWALFLGYRRITRKNVLDNDTRRRIYEYIRENPGIHFREIVRDLGLNRGTLRYHLRRLEREGKITSEKD
GGRTRYFPNSGTYSEEEKKILAYLRRETPRRILLYLLENPGATNKELAEELGISRSTVSWHLKRLEEDGL
VERERDGRNVRYYLNPPER
>gnl|CDD|442626 COG3399, COG3399, Uncharacterized conserved protein [Function unknown]
MMSYPLLLTLHLLAAIAFIGTVFFEVLILEGVRKRLPRETMREVERAIGKRARRIMPWVVLVLYLSGLGM
AWQHRAALAHPFASSFGLLLTLKILLALSVLGHFLTAMTLMRRGKLTGRRSRYIHLSVFCHMLLIVLLAK
AMFYLHW
>gnl|CDD|442627 COG3400, COG3400, Uncharacterized protein AQ_414, contains TrkA and USP-like domains [General function prediction only]
MKKILIIADGIVAKHFLERLRETYVGENSYIVVYYNEAIIPEKDPENFEFIKFDPTSFVKLKKILKKEFS
QIIIVMKDKDETEETYKNIRELDPKVRIVVLDFWDLDFEELDDENINLVNPNELLANRLIDFLPNVPVVA
QNIGLGEGEIMEVLVPFGSSFVYRHIGSIEQKNWRIAAIYRNNKLILPNPSLMIQPNDRLLIVGDPEVLK
SVYRAIKKEIGQFPAPFGSNIYLYIDMNYMNQEEIKKLVKEALYLHRKLKAKKLIIRVINPSIIKLLEKI
KNLEGEFIIVEIDYRNTSFSALLKEDLKQYDIGLIVVSRKLFKKKYYRKALYDLKIPVLKLGEESFSKLK
ESVVLLLDEEDIEFISSTIFDLSSQLKLPLELYDYEEPRGQKKTEILEHFENLAKIFEKKIEIEQKEGNP
IRELKKKENILQILPFTKKLLKREFISIFSTDVEYLYFKLKKNSQLFIPVEE
>gnl|CDD|442628 COG3401, FN3, Fibronectin type 3 domain [General function prediction only]
TGSSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTG
GRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGT
YALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVA
ATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRSNSGDGPFTKVA
TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS
SDADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASA
ASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLS
VTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSS
VSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLLVL
>gnl|CDD|442629 COG3402, YdbS, Uncharacterized membrane protein YdbS, contains bPH2 (bacterial pleckstrin homology) domain [Function unknown]
LSPRAVKVWRLRALIGALILLAVLAVLALLLDFPPWLGWVLLALVVVLAVLSLVLAPPLRYRRWRYEVRE
DDLYIRRGVLFRRRTVVPYGRIQHVDTEQGPLERLFGLATVTVTTAGSSGDVTIPGLPEEEAERLRDRLA
ALA
>gnl|CDD|442630 COG3403, YcgG, Uncharacterized conserved protein YcgG, contains conserved FPC and CPF motifs [Function unknown]
MSRLLTKEDLEERGPLPDWLADLYEEFRAFILDPPFPCVFAKSALKKGQLRYGFVDDLTSGDDLLALADD
LLEYLELYRDEGSKFTSLVVFFEPPEELSEEEYEERLWEILQYLHDHDPAPWPEDVSTDPDDPHWSFSFG
GEPFFVVGLHPAYSSRKSRRFPYPAIVFNPRWQFEGLRGETGRGERARDKIRERDEAYDGLSINPDLGDY
GDGDSEWRQYSGGDRNVPEPWKCPFHRKRE
>gnl|CDD|442631 COG3404, FtcD, Formiminotetrahydrofolate cyclodeaminase [Amino acid transport and metabolism]
MMLLDLTIKEFLEELASKSPAPGGGSAAALVGALGAALGSMVANLTIGKKKYADVEEEMKEILEKAEKLR
EELLALIDEDAEAFNEVMAAYKLPKETEEEKAARSEAIQEALKEAAEVPLEVARLCLEVLELAEELAEKG
NPNAISDAGVAALLARAALKGALLNVKINLKSIKDEEFVEELRAEAEELLKEAEELADEVLAIVEEKLG
>gnl|CDD|442632 COG3405, BcsZ, Endo-1,4-beta-D-glucanase Y [Carbohydrate transport and metabolism]
LRRLLLLLAAGLALFAEAGASAAAAKLWPAWEQFKRRYIQGDGRVIDTGNGNISHSEGQGYGMLLAVQAN
DRATFDRLWRWTKTNLARGDDGLFAWRWGPDGSWGVLDPNSASDGDLDIAYALLFAGRRWGDPDYLAEAR
AILQAILRKEVVPVPGLIVLLPGDWGFDGGGSWVTNPSYFPPPAFRVFARAAPDAFWAELADSSRALLEK
AAHPPTGLPPDWVALDGTGGPQPAPGFPPRFSYDAIRVPLRLAMDAAWFGDPLAKALLAPMAAFWASQGR
SNPPAGVDLDGGPLAEGYHSVGFVAALAVAALAADGAAQAFVDRLWNTPLPTGPDDYYDASLYLLGLLAL
SGNYRFCLP
>gnl|CDD|442633 COG3407, MVD1, Mevalonate pyrophosphate decarboxylase [Lipid transport and metabolism]. Mevalonate pyrophosphate decarboxylase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
MAMGSATARAHSNIALIKYWGKRDEELNLPANPSLSLTLDAFYTTTTVEFDKDLAEDEFILNGEPQKGKF
LPKISKFLDRVRALAGKSYHARIESENNFPTAAGLASSASGFAALALAANSAEGLDLDDRKLSRLARLGS
GSACRSIFGGFVEWGKGEDDEDSYAVPIPAEDWDLADIILVVDKGEKKVSSREGMKTAETSPFYPAWVEQ
AEEDLEKLKEAIKAGDFEALGEIAESNALRMHATMMTSNPPFIYWKPNTLEVINAVRELREEGLPVYFTL
DAGPNVKVLCPEEDAEKVAAFLAAELVNGQVIVDKPGPGARL
>gnl|CDD|442634 COG3408, GDB1, Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism]
VRALRRAADQLRTNTPGDGPTVIAGYPWFSTDWGRDTLIALPGLLLLDPELARGILRTLARYQEEPGKIP
HEVRDGEEPYYGTVDATPWFIIALGEYYRWTGDLAFLRELLPALEAALDWILRGDRDGDGLLEYGRSGLD
NQTWMDSKVDSVTPRSGALVEVQALWYNALRALAELARALGDPELAARWRELAERLKESFNERFWNEELG
YLADALDGDGRPDDSIRPNQLFAHALPTGILDPERARAVLRRLVSPELLTPWGLRTLSPGDPAYNPMAYH
NGSVWPWLNGLYAEGLLRYGFREEARRLLEGLLDALEEFGLGRLPELFDGFDGYPRGCIPQAWSAAEVLR
LLQ
>gnl|CDD|442635 COG3409, PGRP, Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis]
ASAPTLRLGDSGEDVRELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGLPVDGIVGPATWAALRA
>gnl|CDD|442636 COG3410, BH3996, Uncharacterized conserved protein, DUF2075 family [Function unknown]
ALRAGEDFRDDLGEYVELESLEWSNAVRRDLGHELVESWAASDPVLLEDLVDVLDVLADILIILRLPAIG
DDVDIVILLLLNLDEVVSLVREDERTLAESRELKLLDVSVVLDLLRSRLLDLLSYAAAYSALLLSVAALA
NNLDIAAALTLDLRNYYELEDDQLLFRSDYLGIEKAPLKLKGEDEKLVEGFKLIKKDGLELELLLLISIS
IRLISKLLSESLKLTLLGEQLLLKIDDLKKVVEAILALAAESLKEVGKLVLVSGGGGGTTKVVLLALLLR
LLSLRLLALLLLLVNAAPRLKYLKLLSSGKKGKLIKNDFKRSVSLIDRLSKLDLAAIDVADRALLLLSGS
LLGLNENQGELLDEAIKSVFFVVDVQQVVQLELKTSERIIEAAALLRGATVGRLLLEQQFRGGGSADYDV
WDDDLGIRETANPLPKDDDYDFRVFDDPQEMYEAIKKKNKEGGLSRMVAGYCWPWPSKKDGLAYDIEIGG
FRLPWNLTDDRPSALWAEDPDSIDEVGCIYTAQGFELDYVGVIIGPDLVYRDGRIVVDPEKYADKAAKGR
KKLKESDEDADRIIRNTYNVLLTRGMKGTYVYATDPELREYLRELVSGS
>gnl|CDD|442637 COG3411, COG3411, 2Fe-2S ferredoxin [Energy production and conversion]. 2Fe-2S ferredoxin is part of the Pathway/BioSystem: 2Fe2S
MSKYRHHVLVCTGSCGAAGAEEVLDALKEELKERGLDGDVRVTKTGCLGRCEQGPVVVVYPEGVWYGNVT
PEDVPEIVEEHLLGGRPVERLLLPDP
>gnl|CDD|442638 COG3412, DhaM, Phosphotransferase subunit DhaM of the dihydroxyacetone kinase DhaKLM complex, contains PTS-EIIA, HPr, and PEP-utilizing domains [Signal transduction mechanisms]
IVIVSHSAKLAEGVVELARQMAGGDVPIAAAGGTDDGGIGTDADKIAEAIEEADSGDGVLVLVDLGSAVM
NAEMALELLDEELRERVRLADAPLVEGAVAAAVAASAGADLEEVAAEAEEALEAKK
>gnl|CDD|442639 COG3413, DmsR, Predicted transcriptional regulator, contains HTH domain [General function prediction only]
VELLDRTDDRALYRLSVSLLEALAEHGGVVLSPRATDGGWRWRVLFPDREDLREFVEELRERGIDVELVR
LRELDRPTRSSLLDGLTDRQREALETAYEMGYFEVPREATLEELAEELGISKSTLSEHLRRAERKLLEAL
LDE
>gnl|CDD|442640 COG3414, SgaB, Phosphotransferase system, galactitol-specific IIB component [Carbohydrate transport and metabolism]
MKKILVVCGSGLGTSTMLKMKIEKVLKELGIDAEVEHCDVSSAKSKADDADLIVTTTDLAEELGIPVINV
IPLLNGIDKDEIKEKLLEALKELG
>gnl|CDD|442641 COG3415, Csa3, CRISPR-associated protein Csa3, CARF domain [Defense mechanisms]. CRISPR-associated protein Csa3, CARF domain is part of the Pathway/BioSystem: CRISPR-Cas system
SRLTLTEEERRDLEKLLRKTKDAREARRLRAVLLLAEGLSVREIAERLGVSRSTVYRWLKRYREGGLAGL
KDRPRGGRPSKLSDEQRERLLELLREKSPDQGSRWTLAELAELLEEEFGVEVSPSTVRRLLKRLGLSYKK
PRPRAPKQDPEAVEKFKKELEALLAKPAKAEVAGVDEGDEIGALRRAAGGRLLAPGGRVRRTGASVRRGR
ALLFLALGLALGLRIGLTIDALLAGALLLFLRLLAERALALLLLLLLLLLLSPSKAVARAAKLLKLELLR
LLFLPPSASLLLALEALLRELRERNLLRLAHASLLLLFAAARDAR
>gnl|CDD|442642 COG3416, COG3416, Uncharacterized conserved protein, DUF2076 domain [Function unknown]
MTPEERQLIDGLFDRLKQAEGQPRDPEAEALIAEALRQQPAAPYYMAQTILVQEAALKQAQQRIQELEAQ
LAQLQQQQPQSSGGFLSGLFGGGQRPPPAPQPSQPGPQQQPAPPSGPWGQAAPQQPGYGQPQYGQPAAGP
SGGGGFLGGALQTAAGVAGGVLLANALTGMFSGSHPGEGVGGGGGEPGGAGEETVINNYYGDDAGGDNND
AGFQDNDYDASGDDGGFDDFGGDDDSF
>gnl|CDD|442643 COG3417, LpoB, Outer membrane lipoprotein LpoB, binds and activates PBP1b [Cell wall/membrane/envelope biogenesis]
MKKKKLLLVALAALLLAGCASTPVTYVDPNEVEDVSGKWNSTDWQAAAEPMVDSMLSSPWVAKTAGGRPV
LLVDSVKNKTNEHIDTETATKDIRRALINSGKFRFVSAGQLAQARQELGLQRDDSLVSRSTAIGLGREVG
ADYVLYGSISSIVDSPGKGKVVYYQFTLQLMDVQTGEIVWSGEKEIRKTG
>gnl|CDD|442644 COG3418, FlgN, Flagellar biosynthesis/type III secretory pathway chaperone FlgN [Cell motility, Intracellular trafficking, secretion, and vesicular transport]
TAQELAALLEQELEALQELLELLEEEQQALVARDVDALQELTEEKSQLLATLEQLDQQRRQLLAALGLSA
DYAGMEAWLADDPALAALWQELLELTRRCRELNQVNGQLIERRLRRNQQALDILRGAAAAPSLYGADGQT
RSASSGGRKIGAA
>gnl|CDD|442645 COG3419, PilY1, Type IV pilus assembly protein, tip-associated adhesin PilY1 [Cell motility, Extracellular structures]
VPSALAAASPVVNSTNLTLSSSSTSTAASLAGGAGGSTLLSAGSATATSAGTASTASASASAVTTSTGST
SDGSGATAAATASVGSTVSATTASASSGSTGSLGGSSAQSGSANSTSTYVASDSASTNGSTSSGTSAAAA
STNTASSGTANAATTNTGAGASTGNSTSTATTTTATSTTLTGDGVTGTSDATSNSYATGANNNGANTGVG
VAADASTTGVTSASSSNNAAVNGRGKYFSASDPEELVAALQSALSDILARSSSFAAVAVSSSRLQSDNQV
YQASFDPTDWTGNLKAYKLDASTGAISATPLWSAAEKLPARSPASRNIYTWNGSTGALVPFTWANLSAAQ
KAALGSGASGLTDALGANLVNYLRGDDSNEEDDGGLFRTRTSLLGDIVNSSPVYVGAPDFGYADSGYGAF
VTAYANRTPVVYVGANDGMLHAFNAGDTGEELFAYVPSAVLPNLARLADPDYGGNHRYFVDGSPTVGDVY
IGGAWRTVLVGGLGRGGRGYYALDVTDPASFAAPKVLWEFTDADGDADLGYTWSKPVIAKLNDGRWVVIF
GNGYNSASDSDGRAVLFVVDADTGALLKKIDTGAGSAADPNGLSDPAAVDSDGDGTADRVYAGDLGGNLW
RFDLSSSTPSNWSVTGTPLFTATDSSGNAQPITAAPDVARHPTGGGLMVYFGTGKYLEPLDLTSTVTQSF
YGIWDDGTTTATTTITRSDLVQQTITSDGTGTTTEVTTVSNNAVDWATKKGWYIDLPTSGERVLSDPLLV
GGVVIFTTYIPSVSDPCSPGGTGWLYALDYLTGGALTNSVFDTNGDGVVDAADSRSVVVSGIGLPPTPVV
VNGKEVTSGSDGGIESVKINESGGGPRGRVSWRELRN
>gnl|CDD|442646 COG3420, NosD, Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism]
LALLLLLLLLAGAAAAATAPGDSLQAAIDAAPPGDTIEVPPGTYEGNIVIDKPLTLIGEGGAVIDGGGKG
TVITITADNVTVRGLTITGSGDSLTDDDAGIYVRGADNAVIENNRIENNLFGIYLEGSDNNVIRNNTISG
NRDLRADRGNGIHLWNSPGNVIEGNTISGGRDGIYLEFSDNNVIRNNTIRNLRYGIHYMYSNDNLVEGNT
FRDNGAGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIEGNTISGNGKGIFIYNSNRNTIRGNLFAG
NGIGIHLTAGSEGNRIYGNNFIGNRTQVKYVGGRDNEWSADGRGNYWSDYTGFDLDGDGIGDV
>gnl|CDD|442647 COG3421, ResIII, Type III restriction endonuclease [Defense mechanisms]
KKKTVRKINEKRFLLLQKLDQSEIVLFAEEFPITITLNLNENIRKRLYEEEAFYLKNYIENEPFIKNKPK
HLLFNMATGSGKTLIMAGLILYLYKKGYRNFLFFVNTNNIIYKTRENFLNPQSPKYLFNEKIEIDGENVA
IKEVDNFPEADENDINIKFTSIQKLHNDLNTPRENSLTYEDFEDKKLVLISDEAHHLNASTKSKKKTEKE
EEKSWEYTVNRILKANPDNILLEFTATIDLSNKEIYKKYKDKIIYRYDLKQFREDGYSKDVKRLQSDYED
QERMLNAVLLSEYRRKLAERNGINIKPVILFKSKKIKESKEAYDEFLQLIKNLSADDIEKLIKFSTGKNE
NGSEILENAFDYFRKNDISLNSLVREIKRDFSEENVINVNSKDDSEKEKQILLNTLEDPDNPIRAIFAVD
KLNEGWDVLNLFDIVRLYDTRDGKGGKPGKTTISEAQLIGRGARYYPFELEEGQDKFKRKFDNDPSNELR
ILETLHYHTINDPRYIDELKSALKEMGLPPDEDEEIELKLKPEFKETDFYKKGKVFYNEKVEKSRDDIDG
IDDLIINKTYKYGLKTGSLILITIFFDEETAKDQATLQKTKDIKISDIDDRIIRKALSRLDFFRFDNLKK
YFPDLESLKEFLHSEKYLGGIEITITGEVFSIKDLTADEKLQILLKILAEIAKYIDKNYKEYIGTKEFIP
YPIKEVFKDKKIRVYVNDTSDKEHGDGAQNDDKNQKLQLDLINEDWYVYNENYGTSEEKKLVKYIAKRLE
ELKEKYSEIYLIRNEEALKLYEFKDGEAFEPDFILFLKDKENEDLTYQVFIEPKGGHLLEQDEWKEDFLK
EIEKEQKIIFGENDEYKIIGLPFYNDDDRENEFEKAFKALLLA
>gnl|CDD|442648 COG3422, YegP, Uncharacterized conserved protein YegP, UPF0339 family [Function unknown]
AAKFELYRDKDGEFRFRLKAANGQIIASSEGYASKAAAENGIESVKKNAPDAEVVDLT
>gnl|CDD|442649 COG3423, SfsB, Predicted transcriptional regulator, lambda repressor-like DNA-binding domain [Transcription]
MRKKKDWHPADIKAALRKRGTSLAALAREAGLSSSTLSNALTRPWPKGERAIAEALGVPPEEIWPSRYA
>gnl|CDD|442650 COG3424, BH0617, Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism]
SARILSIATAVPPHRYTQEEIAEFAAELFGLDERDRRRLRRLFENSGIETRHSVLPLEWYLEPPSFGERN
ALYIEEALELAEEAARRALDKAGLDPEDIDHLVTVSCTGFAAPGLDARLINRLGLRPDVRRLPVGGMGCA
AGAAGLRRAADFLRADPDAVVLVVCVELCSLTFQRDDDSKDNLVANALFGDGAAAVVVSGDPRPGPGPRI
LAFRSYLIPDTEDVMGWDVGDTGFRMVLSPEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKV
LDAVEEALGLPPEALAHSREVLREYGNMSSATVLFVLERLLEEGAPAPGERGLAMAFGPGFTAELVLLRW
E
>gnl|CDD|442651 COG3425, PksG, 3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]. 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
MKVGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDRAGIDP
SDIGAVYVGTESGPDASKPIATYVHGALGLPPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIAS
DIARYGPGSAGEYTQGAGAVAMLVGADPRIAEIEGGSGSYTTDVMDFWRPNGSDYPLVDGRFSEPAYLDH
LEEAVKDYKEKTGLKPDDFDYFVFHQPFGKMPKKAAKKLGRKAGREIQEDFEEQVEPSLIYSRRIGNTYT
GSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGTVTPGIEERLRRPGVEEQLANRRYLSYAEYEK
LRGKILPEDAEDVTLPGEFVLTGIKDHERIYE
>gnl|CDD|442652 COG3426, Buk, Butyrate kinase [Energy production and conversion]
MYRILVINPGSTSTKIAVFEDEKELFEETIRHSAEELAKFESIADQLEFRKEAILEFLKEHGIDLSELDA
VVGRGGLLKPIEGGTYRVNEAMLEDLKNGKYGEHASNLGALIAYEIAEELGIPAYIVDPVVVDELEDVAR
ISGLPEIERKSIFHALNQKAVARRAAKELGKKYEELNLIVAHLGGGISVGAHKKGRVIDVNNALDGEGPF
SPERAGGLPVGDLVKLCFSGKYTKEELKKKLVGKGGLVAYLGTNDAREVEKRIEEGDEKAKLVYEAMAYQ
IAKEIGAMAAVLKGKVDAIILTGGLAYSKRLVDLIKERVSFIAPVEVYPGEDEMEALAEGALRVLRGEEE
AKEYEGE
>gnl|CDD|442653 COG3427, CoxG, Carbon monoxide dehydrogenase subunit CoxG [Energy production and conversion]
MELSGSFTVPAPPEQVWAALNDPEVLAACIPGCESLEVVGDTEYEATVKVKVGPVKATFKGEVTLSELDP
PESYTLTGEGKGGRAGFAKGTATVTLEPDGGGTRLTYDADADVGGKLAQLGRRLIDGVAKKLADQFFENL
AAKLE
>gnl|CDD|442654 COG3428, YdbT, Uncharacterized membrane protein YdbT, contains bPH2 (bacterial pleckstrin homology) domain [Function unknown]
MSEPWRRLHPLSILVRLLKALALLLPVLLLLLAGVGAGGGLLWVLLIALVLLLLLLLVSYLRWRTTRYRI
TDDRLIVRSGVLSRKRREIPLDRIQSVDVSQPLLHRLFGLGTVRIETAGGGESEVELDALSVPEAERLRR
LLLERAAGAAEEEAEAAAPEEVLYRLSPRDLLLAGLTSGGLLLLLALVGALYSQLADEAGLLLVLLLLLL
GWLLSVVGTVLRYYGFRLTRSGDGLRIRRGLLTRRSVTIPLDRIQAVRIKQPLLRRLFGWARLEVEVAGY
GEEEGGSSVLLPLAPRDEALRLLAELLPELEELTRHPRRARWLAPLRYRRLGYALTGDYLVVRSGFLTRR
TVVVPRDRIQSVRLSQSPFQRRLGLATVRVDTAAGPGSYTVPDLDAEDARALAAWLLPRL
>gnl|CDD|442655 COG3429, OpcA, Glucose-6-phosphate dehydrogenase assembly protein OpcA, contains a peptidoglycan-binding domain [Carbohydrate transport and metabolism]
MIIDLPDTTTSKIAKELVELREEGGAVALGRVLTLVVVTDEGDVEEAIEAANAASREHPCRVIVVVRGDG
EGAARLDAQIRVGGDAGASEVIVLRLYGELARHLDSLVLPLLLPDAPVVAWWPGEAPENPAEDPLGRLAQ
RRITDSAAAPDPLAALARRAEHYTPGDTDLAWTRLTPWRALLAAALDQPPYEPVTSVTVEGAPDSPSADL
LAAWLASRLGVPVTRVVTPGGPGITRVRLERASGDIELTRPDGRVATLSQPGQPDRRVALPRRTLADLLA
EELRRLDPDEVYEEALAAGLPLLGARDAAAAA
>gnl|CDD|442656 COG3430, COG3430, Archaeal flagellin (archaellin), FlaG/FlaF family [Cell motility]
MTMKKGMSDERAVSPVIGVILMVAITVILAAVIGVFVFGLGDDVSEPAPQASLSVEFVGDGDSVTITHEG
GDPVNVDDLKVSVDGTTITLS
>gnl|CDD|442657 COG3431, COG3431, Uncharacterized membrane protein, DUF373 family [Function unknown]
MKKLFRLILPWFSDDRFVRLLEKVIDLVVIVLAILLFLVILVGVADLFYSLYQLLLTGLFPLDFIEIFGD
FLNVLILIELFRNLIIYLREHRISVRLVVETAIVAVLREIIILDVKEISPLDLLALAALLLALGILYWLV
VKYPPREEGI
>gnl|CDD|442658 COG3432, COG3432, Predicted transcriptional regulator [Transcription]
MKRRSRLEIIADILEALKNEGAKKTRIMYKANLSYDRLKKYLDLLEEKGLIEKEDDGGRRIYRITEKGRE
FLEKYEEIKELLE
>gnl|CDD|442659 COG3433, AcpA, Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]
IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFI
PVPYPAQPGRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAG
VGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAAS
PAPALETALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTL
AAWWALLAAAQAAAA
>gnl|CDD|442660 COG3434, YuxH, c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms]
MMDVFVARQPILDRDQRVVGYELLFRSGLENSAPDVDGDQATARVLLNAFLEIGLDRLLGGKLAFINFTE
ELLLSDLPELLPPERVVLEILEDVEPDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADIIKIDVL
ALDLEELAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKGKKLPPSQLTLLQLL
NELNKPDADLDEIEEIIKRDPALSYKLLRYVNSAAFGLRRKITSIRQAIVLLGLRQLRRWLSLLLLASLS
DSGKPPELLETALVRARFCELLAEKLGPKEEADEAFLVGLFSLLDALLDQPMEELLEQLPLSDEIKDALL
GREGPLGPLLALAEAYERGDWEAVERLAEELGLSPEQVNEAYLEALAWADELLSALA
>gnl|CDD|442661 COG3435, COG3435, Gentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism]
LVPPEPRPKAVPHLWRYADLRPLLLRAGRLVTAERAERRVLVLENPGLGGKSAATPTLYAGIQLLLPGEV
APAHRHTQSALRFVIEGEGAYTVVDGERVPMERGDFVLTPSWTWHDHGNEGDEPMIWLDGLDIPLVELLE
AGFFEDGPDDVQPVTRPEGDSEARYGHGGLRPYEFLRDTVSSPLLHYPWERTREALERLAALEEPDPYGG
AALRYVNPATGGDVMPTIGAFMQLLPPGFHTRPHRHTGSAVYHVVEGSGRSIVGGERFDWGEGDLFVVPS
WAWHSHASADEDAVLFSFSDRPVQEALGLYREERLE
>gnl|CDD|442662 COG3436, COG3436, Transposase [Mobilome: prophages, transposons]
EEEEEELILLLLLLERLRLRRLRERESRLESQPELQLLELEEEAEEEEEAAEEAEAKTTKKKPKPGRKPM
PEHLPREEVLHEPTDMRKIDGLAAIGEEVSEELDLDPGALFVFRNRRDKYKCLYCDGTGLVYAPAPAKRL
EKGLAGPGLLAHILVSKFVDHLPLYRQEEIFARLGVELSRSTLLNWVGRAAELLEPLLEGLDERLLAAPV
LHADETPVQVLDEGKGKTVTASYWWVYRDGRPSRGPVVYDAYRSRRGARAGLVLDGGLGGGLGDDYADGY
AALLRLAELGCAAAARRRRKAAAAALKKLAKKAAAAAAGLAAEEALLRIEELRKEERLRERRRERRPRRL
LLLKALLLLLLLLLPLLPPGKALLYAALARAARLLALLDRLLDLLRNNDENNAERNALRRRNNLFA
>gnl|CDD|442663 COG3437, RpfG, Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms]
MRTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLR
LLRADPSTRDIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYL
KLAAPLHDIGKIGIPDAILLKPGKLTPEEWEITHAHIGAEILSGSLLPLLQLAAEIHERWDGSGLSARDA
LTSKKLEEALEEIR
>gnl|CDD|442664 COG3439, COG3439, Uncharacterized conserved protein, DUF302 family [Function unknown]
KKLLGLITVESPKSFDETVERLEEALKEEGFGVLAEIDVSATLKELGLDLRPYRILGFCNPKLATRLLQA
DPEIGLLLPCRVLVYEDEDGKVWVSYMDPSALAKLFGNPELKEVAEEVEEALEKILEA
>gnl|CDD|442665 COG3440, COG3440, Predicted restriction endonuclease [Defense mechanisms]
AEQLLDALFLEEEPDELERTERERLVKRRVRQGAFRKAVLEAYDGRCAVTGLDIPPLLEAAHIKPWSDHG
GRDDVSNGLLLCPNHHALFDRGLITIDDDYRILVSPRLKEESDLIRELKELHGRKLRLPEHERFRPDPEY
LAWHRENVFK
>gnl|CDD|442666 COG3442, COG3442, Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction only]
ELTIGHLYPDLLNLYGDRGNVLALKRRAEWRGIDVEVVEVNPGDDLPFDDVDIVFIGGGQDREQEIVADD
LLRIKDALRAAIEDGVPVLAICGGYQLLGHYYETADGERIPGLGILDVYTVAGKKRLIGNVVVETELNGE
FGTLVGFENHSGRTYLGPGVKPLGRVLYGYGNNGEDGTEGARYKNVIGTYLHGPLLPKNPALADRLIALA
LERKYGELIELAPLDDTLEEKAREAILKRLR
>gnl|CDD|442667 COG3443, ZinT, Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism]
HGHSHGHPHTEAEKKAYEGYFDDKDVKDRSLSDWEGDWQSVYPYLQDGTLDPVFEHKAKKDGDKTAEEYK
AYYTKGYATDVDRIVIEGNTVTFHKNGKVKSCEYKYDGYKILTYKSGNRGVRYLFECKDADAGAPKYIQF
SDHIIAPEKSAHFHIYWGNDQEALLEEMDNWPTYYPYQLSGDQIVDEMLAH
>gnl|CDD|442668 COG3444, AgaB, Phosphotransferase system, mannose/fructose/N-acetylgalactosamine-specific component IIB [Carbohydrate transport and metabolism]
MAIVLARIDDRLIHGQVATAWTKELGANRIIVVNDEVAKDPLRKTLLKMAAPPGVKVSVLTVEKAIEVLK
KPKYDKQKVFLLFKNPEDALRLVEGGVPIKEVNVGGMAFREGKKQITKAVSVDEEDVEALKELAEKGVEV
EIQKVPSDSKVDLKDLL
>gnl|CDD|442669 COG3445, GrcA, Autonomous glycyl radical cofactor GrcA [Coenzyme transport and metabolism]
MIKGIQITKSANAALLNSFWLLDEEKNEARCLCAKDDYAEDQVVALAELGQFEYREVPVEAPPRVEGGQH
LNVNVLRRETLEDAVKHPEKYPQLTIRVSGYAVRFNSLTPEQQRDVITRTFTESL
>gnl|CDD|442670 COG3447, MASE1, Integral membrane sensor domain MASE1 [Signal transduction mechanisms]
MSSSSALGTPGRPLLRLLLLALLYFLLALLGLLLARPPGGVSPIWPPAGVALAALLRFGRRAWPGILLGA
LLANLLAGLTGDPLLLALLIALGNTLEALLAAWLLRRLLGFSPPLQRLRDVLRFLLAAALLAPLISALLG
ALALALAGLLPGSPFLSSWLTWWLGDALGILLVTPLLLAWRRPRLRRLRRRRLLEALALLALLLLVSWLV
FGLLGYPLAFLLFPLLLWAALRFGLRGAALAVLLLALIAILATALGLGPFASLSPNQSLLLLQLFLAVLA
LTGLLLAAALAERRRQRLRERELALRAALELLALGLLLAALDDALLLLNARGLLLLALSLAALLLLRLAL
LLLLLALDALLLLLADDDRGELRGDLLRRRGATRLGAVVARLLRRSGGRGEEVVVLLVIAQVEEALELAL
RERREERLLERLALALELLAITAALLAAALLLALADLLLLLLAEAAQLLARALLLGLDRLLADAALAALA
ALADLLGALLSAGLRRRGGRRLGARLIRSLLSRVLAELGAVELLLALIADLTEVALGAEALERLLERLLL
ALLGLGLAVAALLATLGLLLALLAALALSGAAALLALGAALLLAAAILGLAAALLALLRLLGERARLLET
RRLVGAL
>gnl|CDD|442671 COG3448, COG3448, CBS-domain-containing membrane protein [Signal transduction mechanisms]
AMTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERL
LDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE
>gnl|CDD|442672 COG3449, SbmC, DNA gyrase inhibitor GyrI/SbmC [Replication, recombination and repair]
MMKLRTREADQRRRILLVLIALHDDLDLLLLALLLAFAFHFFFFHRRRRFRALIGRRARLLLRRRLLAAL
ALLLLSSSAIIAAAAAASGYSSSASFRRFFRAFGGSSRSRRRRAKAKLLALPPLDPPRLEPMMDVEIKEL
PPRRVAYLRHRGPYEEIGEAFERLIAWAKARGLLPPDSRTIGIYYDDPDITPPEKLRYDACVTVPEDVAL
PGGVEVKTIPGGRYAVLRHKGPYEDLGAAWDWLYGEWLPASGYELRDRPCFEIYLNDPRETPEGELITDI
YLPLKP
>gnl|CDD|442673 COG3450, COG3450, Predicted enzyme of the cupin superfamily [General function prediction only]
LDADAVEPESDPPAPERILEGDPSARTWNLFTSPDGGVSAGVWECTPGKFRWDYDEDEFCYILEGRVTVT
DDDGEPVEFGAGDSFVFPAGFKGTWEVLETVRKHYVIR
>gnl|CDD|442674 COG3451, VirB4, Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport]
MYLEIGDRYGRVLSIKGYPSETSPGLLDPLLQLPCEFIVTQSFTPLDKDEALKKLKRKRRRLESKRKSEQ
ALVDDDAESQAEDAEEALDELQSGGERLGEVHLTLTVFADDLEELEEAVREVESALQSAGFTLVRETLNQ
EEAFLSSLPGNFDYRLRRRLLTTSNLAALFPFHSFELGDPWGIYLLNTRSGTPVFFDFHDGLDNGNTLIL
GPSGSGKSFLLKLLLLQLLRYGARIVIFDPGGSYEILVRALGGTYIDLSPGSPTGLNPFDLEDTEEKRDF
LLELLELLLGREGEPLTPEERAAIDRAVRALYRRADPEERTTLSDLYELLKEQPEAKDLAARLEPYTKGG
SYGWLFDGPTNLDLSDARFVVFDLTELLDNPELRPPVLLYLLHRIWNRLRKNNDGRPTLIVIDEAWLLLD
NPAFAEFLEEWLKTLRKYNGAVIFATQSVEDFLSSPIAEAIIENSATKILLPQPKADIEDYAELLGLSER
ELELIRSAGRGKRDFLIKQGNGSVVFRLDLSPEELALLSTKPEEVAILDELRAEHG
>gnl|CDD|442675 COG3452, CHASE, Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms]
MKLSALLLLRRRPLLLALLAFLLLLAVGAVLERLLREQEEQQLRAEVLQELSAIRARLEGELNARLSLLR
GLAALVEANPGISQEEFERLARNLLEDYPGIRNIALAPDGVIRYVYPLAGNEAALGLDLRTDPEQRAAAL
RARESGQLVLAGPVNLVQGGRGLIGRLPVFLDGGDDRFWGFVSAVIDLDRLLDSAGLDDAQDGYQIALRG
RDGDGAEGEVFYGDAALFDQDPVTLEVNLPGGSWQLAAAPKGGWLASPRNALPLRLAGLLISLLLALLVY
LLRQLLLLRLLLLLLRLELIAAALLLLLLALDLLLELLLLLRLAEALLQERLRALALLAALEDLLLLKFD
RDLLDLLLLLELEAILALLLLLRRLLRSREARGGLGGDLVRVGGVIDGRVAVILIIEALELAEARLAALD
QERDASDVALGAALVVLEALLIIALLRELALLAGALLARKSLLLALDLAAESERLRYLELLLGDALRERI
RRALLRLQLLSLDLSALAAVLGAESLAGLLISVFIDARILEAERLELALVAGEVALEELLLRLLGEILLL
RAELILALLDAKSGLSALELSGLLAGRAALDSLLLLLALALRQLDESALFILEELLLRLIIDLRIERLLL
LLLGGEILLGELALLLLLLVLIILILLSVEEAGLILALSLLLALLLLAILDAAVSLLATLLLLFQLLLLL
LIILEGLLAELVAEALRLALALAQLLLRLLLAELLQLLLLLLGLILLELLLRLDGLLVELIALRLEILIL
TLLILDADEILADQT
>gnl|CDD|442676 COG3453, COG3453, Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family [General function prediction only]
IRKITDRLSVSGQPTPEDLAALAAAGFKTVINLRPDGEEPDQPAAADEAAAAEAAGLEYVHIPVTGGAIT
DEDVEAFAAALAAAPGPVLAHCRSGTRSSALWALYQAGKGGMSPEEALAAAAAAG
>gnl|CDD|442677 COG3454, PhnM, Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase PhnM [Inorganic ion transport and metabolism]
MMTELVITNARIVLPDEVIDGSVVIEDGRIAAIDEGASAAPGAIDAEGDYLLPGLVDLHTDNLERHIEPR
PGVRWPLDAALLAHDAQLAAAGITTVFDALSVGDEPDGGRRLENARALADAIAALRAAGLLRADHRLHLR
CEVTSPDALELLEELLDDPRVDLVSLMDHTPGQRQFRDLEKYRAYYAGKYGLSDEEFDALVARRRALRAR
YAAANRAALVALARARGIPLASHDDDTAEHVAESAALGVAIAEFPTTLEAARAARAAGLAVLMGAPNVVR
GGSHSGNVSAAELAEAGLLDILSSDYVPASLLAAAFRLAEDGGLDLPEAVALVTSNPARALGLDDRGEIA
PGKRADLVRVRRLDGVPVVRAVWVAGRRVYRAG
>gnl|CDD|442678 COG3455, DotU, Type VI protein secretion system component TssL/VasF/DotU [Intracellular trafficking, secretion, and vesicular transport]
SSDPSLALRGAGLNPLVDAASPLLLLVVRLRQGAEPPDPAALRQRLVEEIRRFERRLRAAGYSPEDIEAA
RYALCALLDEAVLNTPWGGRSEWSRHPLQSTFFNETWGGEKFFELLERLLQEPAAHLDLLELYYLCLLLG
FEGRYRVEGGREELEALRRRLYQLIRRLRGEPPAPLSPHWQGPDAARKRLRRRLPLWVLAAVAALVLLLL
YLGLSYRLNSQTDPVLAQLNQLL
>gnl|CDD|442679 COG3456, COG3456, Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport]
MPLTLRIINSPDLESGSAASATFGRGGGTIGRSADCDWVLPDPDRSVSRRHAEIRFRDGAFCLTDLSTNG
TFLNGSDHPLGPGRPVRLRDGDRLRIGDYEIRVEISGEDEGADDPLAAAPEPAVSSPSNLSDTEAAPDAA
LAFSFSLDPLEALDEAATEAPATADDPPSLLPEDWLPSAAPVADEAAAQAIDQLPSAAAPAPEPEPAADA
DHALLAALLRGLGLDLELLDSQDAEDFLEELGRLLRAAVEGLLDLLRARAEFKNEFRLDQTMLRPIENNP
LKFSPDYEEALALLLAPKSPGFLSAPAAVAESLRDLRLHQLALLAAIQAALRALLDAFSPEALERRFERR
LFGSRKAKAWDMYEAYYQELSSERQQGFEKLFGEVFAQAYDRALRELKREGE
>gnl|CDD|442680 COG3457, YhfX, Predicted amino acid racemase [Amino acid transport and metabolism]
IPPPTLVIDLDKIRENARRLVELAAKHGIELYGVTKQFGGNPEIAKALLDGGIKGIVDSRIKNLKKLKRA
GIPHPGHLLRIPMLSEVEEVVRYADISLNSELETARALSEAAKKQGKVHKVILMVDLGDLREGGFPEELV
DTVEEILKLPGIELAGLGTNLPCFGGVLPTEENLGTLLELAELLEAKFGIKLPIVSGGNSTSLPLLAEGT
LPKGINHLRPGEALLLGTDPLNARPIPGLEQDAFVLVAEIIELKEKPSVPIGEIGRDAFGNAPEFGDRGI
RKRAILAIGRQDVDPEGLTPIDYGIEILGASSDHLILDVTDSKEDYKVGDTVVFCLRYQAFLTRSTSAYV
EKIYSG
>gnl|CDD|442681 COG3458, Axe1, Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism]
MPTADLPLEELRAYRPTLPEPADFDAFWDATLAEARAVPLDPELTPVETGLPGVEVYDVTFTGFGGARIY
GWLLRPKGEGPLPAVVEFHGYGGGRGLPHEDLDWAAAGYAVLVMDTRGQGSSWGDTPDPGGYSGGALPGY
MTRGIDDPDTYYYRRVYLDAVRAVDALRSLPEVDGKRIGVTGGSQGGGLALAAAALDPRVKAAAADVPFL
CDFRRALELGRAGPYPEIRRYLRRHREREPEVFETLSYFDAVNFARRIKAPVLFSVGLMDPVCPPSTVFA
AYNALAGPKEILVYPFNGHEGGGPEQQDRQLAFLRELL
>gnl|CDD|442682 COG3459, COG3459, Cellobiose phosphorylase [Carbohydrate transport and metabolism]
NGYGGFDDDGREYVITGPDTPAPWINVLANPDFGFLVSETGGGYSWYKNSRENRLTRWRNDPVSDPPGEY
FYLRDEETGDYWSPTWQPVRKPLDEYECRHGFGYTRFEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSD
RPRRLSVTSYVEWVLGNARDDTANFQVTLSTGEVDPEGGAILARNPYNERFNGRVAFFAVSEPVSSFTGD
REEFLGRYGSLANPAALERGKLSNSVGAGLDPCAALQVDIELAPGEEKELVFLLGQGENKEEARALIARY
RDPDAVDAALAEVKAYWDELLGAVQVETPDPALDLMVNGWLLYQTLACRLWARSAFYQSGGAYGFRDQLQ
DSMALVHARPELAREQILLAASRQFPEGDVQHWWHPPTGRGVRTRFSDDLLWLPYAVAAYIKETGDFSIL
DEVVPFLDGPPLPPGEEDAYDLPTVSGEEATLYEHCKRAIDFSLNRLGPHGLPLIGRGDWNDGMNLVGEG
GKGESVWLAWFLYYALKEFAPLAEARGDEERAERYRAEAEELREAIEKHAWDGEWYRRAYFDDGTPLGSK
ENEECKIDLIAQSWAVLSGAADPERARKAMDSVDKYLVTEYGGLILLLTPPFDKYDPDPGYIKGYPPGVR
ENGGQYTHAAPWAIMAEALLGDGDRAYELYSMINPINHNDEADRYKVEPYVYAADVYGVDPHFGRGGWSW
YTGSAGWMYRAATEYILGIRPEGDGLRIDPCIPSDWPGFSVTRRFRGAVYHITVKNPDGVSKGVKSITVD
GKPIEGNLIPLVDDGKEHEVEVVL
>gnl|CDD|442683 COG3460, PaaB, 1,2-phenylacetyl-CoA epoxidase, PaaB subunit [Secondary metabolites biosynthesis, transport and catabolism]
MSAASATEWPLWEVFVRSKPGLPHRHVGSLHAPDAEMALQNARDVFTRREEGVSIWVVPSDAITASSPEE
KDAFFDPAADKVYRHPTFYEVPEKVEHM
>gnl|CDD|442684 COG3461, COG3461, Uncharacterized conserved protein [Function unknown]
SEQYHEPVEELSEETRDMHRAIVSLMEELEAVDWYNQRVDATKDPELKAILAHNRDEEIEHAAMLLEWLR
RNDPGWDEELRTYLFTEGPITELEEAAEAAGEEGAAPSASSLGIGSL
>gnl|CDD|442685 COG3462, TM0315, Uncharacterized protein, contains short C-terminal (SHOCT) domain [Function unknown]
MMGWGGWGWGMGGFLMLLFWLLLIVLIVYLLVRLLRGRGGGPSDGGSEEDSALEILKERYARGEIDEEEY
ERRKKDLLET
>gnl|CDD|442686 COG3463, COG3463, Uncharacterized membrane protein [Function unknown]
MTKLALRKDPPLRLLLALAAIFFLVFFLLSLLRHYLFQSAAYDLGIFDQAFWNTSHGRPPISSLKGFHLL
GDHFSPILLLLAPLYALFPSPYTLLVIQAVALALGALPLYRLARRRLGSPRLALLIAAAYLLYPAVFGAN
LFDFHPEALAPPFLLGALLALERRRWRLFALLLVLILLVKEDLGLTVAGLGLWLLLRRRRRRLGLALIVL
SLAWFLLATKVIIPLFSGDEAKRAAVGRYSYLGNSVGEIIWNLLTNPGLLLSELFSLDKLEYLLLLFLPL
AFLPLLSPLSLLAALPLLALNLLSDNPSQWSLTHQYSLPLIPFLFLAAIDGLARLKKWRRLARAILLWSL
IAFLLAPYGYFLKPLDRAAAAREAIALIPPDASVLTTNNLAPHLSHRRNIYLVPDEDYVLLDLRSPGWPS
SESEEALVDRLLNDGEYGLVAQEDGVVLLKRNARLKASLPRSRRGTLIEAILAVGLPAPPVAAIALATLL
LPITLALVGSSAILPLNTYLLLALLLDPAPDIALLLLTASSTPVAAVVLADLEFTPLVLSRLVL
>gnl|CDD|442687 COG3464, COG3464, Transposase [Mobilome: prophages, transposons]
LELMSVKRVAELLGVSWDTVWRILKRAVERLLARPDFSGPRVLGIDEFALRKGHKYVTVIVDLDTGRVLD
ILPGRSKETLKAFLKELGEEERAQVEVVAMDMSAAYKAAVKEALPNAVIVADRFHVVKLLNEALDKVRRR
EQRELRGRRGRERRPLKRSRYLLLKNPENLTEKQKERLDELLSASPELKRAYELKEALRDLFRAKDPEEA
RRALDRWIERARRSGLPEFKKLAKTLRRWRDGILNYFDHRISNGPVEGINNKIKLIKRRAYGFRNFENFR
ARILLAC
>gnl|CDD|442688 COG3465, YwgA, Uncharacterized conserved protein YwgA [Function unknown]
MLLEHAKLMKLLSAAGEIVGRKKLQKMIYILKKMGVPFGEKYQFHFYGPYSEELTLRLEELCNLGFIKEQ
KEGKGSYYQYRYSITEAGKEFLNKADAEMPDLKEVIDLLNGQSSRFLELVSTVLYFDDLPKESEVIDKVH
ELKPKQNYTDEEIEEAIRFIEELRWICL
>gnl|CDD|442689 COG3466, ISA1214, Putative transposon-encoded protein [Mobilome: prophages, transposons]
MRRVEIRKQTFVLPEEVEVVFEKVVTPFGNSAKVDVPKEYIGKRVYVIVLDDDE
>gnl|CDD|442690 COG3467, NimA, Nitroimidazole reductase NimA or a related FMN-containing flavoprotein, pyridoxamine 5'-phosphate oxidase superfamily [Defense mechanisms]
MRRKDRELDREEIRALLDEARVGRLATVDDGRPYVVPVNYVYDGDTIYFHTAKEGRKLDNLRRNPRVCFE
VDELDGLHSTNYRSVVVFGRAEEVEDPEEKARALRLLLEKYAPGRWRPFSDKELDATAVIRIDPEEISGK
RRAG
>gnl|CDD|442691 COG3468, AidA, Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport]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>gnl|CDD|442692 COG3469, Chi1, Chitinase [Carbohydrate transport and metabolism]
SSSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTA
ATSSTTSTTATATAAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASA
TSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTP
GLPKHVLVGYWHNFDNGSGYIRLSDVPDKYDVINVAFAEPTGATNGTVTFTLDPGSSSPGGYTDAQFKAD
IAALQAQGKKVLLSIGGANGTVQLNTAAAADNFVNSVIALIDEYGFDGLDIDLEGGSNSLNAGDTDTPVI
TNLISALKQLKAKYGPGFVLTMAPETPYVQGGYVAYGGIWGAYLPVILALRDILTLLHVQYYNSGSMLGL
DGQVYSQGTVDFLVAMADMLLEGFPVAGNSNGFPGLRPDQVAIGLPASPSAAGGGYVSPANVNKALDCLT
KGTNCGSYKPRGTYPGLRGLMTWSINWDASNGYEFSNNVGAYLD
>gnl|CDD|442693 COG3470, Tpd, Uncharacterized conserved protein probably involved in high-affinity Fe2+ transport [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism]
MKKLLSALALALALLLLAGAAGAAEYPIGEPVEKGGMEIAAVYLQPVDMEPAGMMLSASESDIHLEADIH
ATKGNPNGFGEGEWVPYLTVKYELTKQGSGKVQKGTFMPMVASDGPHYGDNVKLDGPGKYKVTFTIKPPS
ANGFGRHVDKETGVGPWFKPFTVEYDFTYAGI
>gnl|CDD|442694 COG3471, COG3471, Predicted secreted (periplasmic) protein [Function unknown]
MKRLLRLLAALLLALLAASPALAQAAAPPGNVVQLSASASREVANDLLTATLYAEAEGKDAAALAAQVNQ
AMNAALALAKKYAGVKVSTGNYSTYPRYDKKGKITGWRGRQELRLESKDFAALSQLAGQLQEQLALSGVS
FSLSPEAREKAEDELIAQAIAAFQARAQLIAKALGASGYRIVEVNLNSSGGPYPRPMMMRAAAAAAAAAA
APPPLEAGKSTVSVTVSGSIELK
>gnl|CDD|442695 COG3472, COG3472, Uncharacterized conserved protein domain, often C-terminal to DUF262 [Function unknown]
LLVILLSILLLLPLLLVIQILDELRKRQLVDLIDKGRLLLLLLSRGILLRLLLLGGLEEGPLLLLPVESL
LPLLLLLQGLLILLLLLLLPLLVKLLLSLRELRNLLRGVLDLQQPLRRRRIADDDDLLPDSDDVDDADID
IEDDRLDRSLIDDDLLLDEDEDEVLLLIVLRNSELLEDRSLLELYLETDELKRLLLDSEVVLESIILLLS
VDVVVVEVVILIIEAVVALLKELLALGLLLTFLDLADDAFAAGFDLRDDWDEREEELAEKGLYDVSPTDF
LRALALLATKSAKRRDLLNLETEEYEEWWDKLKDGLEKALNFLRNSAGIFSSRLLPYRTQLVPLAAYLAL
LGEKGLDAELRDKLRRWFWCSVFTGRYSSSTETRFAQDIKEVRDWINGDSGPFPRTLEDAIFAELDRLLT
LRSRSSAAYKGILALLAKLGARDFLSGQKIDLSNLFDNKLEIHHIFPKAYLKKQGISRSLYNSIANRTPL
SARTNRKIGDKAPSEYLAELEEKAGEEELDEILASHLIPEDLELLRADDYEDFLEARRELLAEAIERAMG
KLIDDE
>gnl|CDD|442696 COG3473, COG3473, Maleate cis-trans isomerase [Secondary metabolites biosynthesis, transport and catabolism]
MTTDGLGWRARIGLIVPSSNTTVEPEFPRMLPEGVTLHFSRIPVPEIVTPEELAAMADDLDAAARLLADA
RVDVIAYACTSGSFLIGPDGDRELCARITEATGVPVTTSAGALVAALRALGARRIALVTPYTDEVNERVV
AYLEAAGFEVVAVRGLGLPDNAEIARVSPEELRDLAREVDAPDADAIFISCTNLRTLDVIAELEAELGKP
VLSSNQATAWHALRLAGLDDRVPGWGRLLREA
>gnl|CDD|442697 COG3474, Cyc7, Cytochrome c2 [Energy production and conversion]
GDAAAGEKLFNRKCAACHSVDGGAGNRVGPNLNGVVGRKAGSVEGFAYSDALKASGLVWDEETLDAWLAD
PKAFVPGTKMPFAGLKDPEDRADLIAYLKTL
>gnl|CDD|442698 COG3475, LicD, Phosphorylcholine metabolism protein LicD [Lipid transport and metabolism]
MKELDTSTLRELQLVELEILKEFDRICEKHGIRYFLDGGTLLGAVRHKGFIPWDDDIDIGMPREDYERFL
KIAPEELPEKYFLQNADTDPNYPNPFAKLRDKNTTIIEKSELNLDIDHGIFIDIFPLDGVPDDKLERKKQ
KRKTRFYRRLLFLKKRAKISPGKKLKKLLKKLLYFLLKLISPRFIYKKLEKLARKYNNEDSDYVGYLSSR
YDYKKEIFPKEEFFPLIRVEFEGIEFPVPKNYDKYLTRLYGDYMQLPPEEKRVNHH
>gnl|CDD|442699 COG3476, TspO, Tryptophan-rich sensory protein TspO/CrtK (mitochondrial benzodiazepine receptor homolog) [Signal transduction mechanisms]
SWLALILFLAAVLAAGALGGLLTPSDGEWYASLNKPSWTPPNWVFGPVWTVLYILMAVAAWLVWRAAGSS
ERRLALALFALQLVLNALWSPLFFGLHSLGLALIVILLLWLLILATILAFWRVSRLAALLLLPYLLWVSF
ATYLNAAIWRLN
>gnl|CDD|442700 COG3477, YagU, Uncharacterized membrane protein YagU, involved in acid resistance, DUF1440 family [Function unknown]
LFTQTKPNRRRYGVALWAGIIGGIISAFVKWGWEVPFPPRTPERDRTNPPQELLQDLGIPIDPTHLTYTY
SGHVVNWGSFIVHFLFSIVFAVLYCVVAEIFPKIKLWQGAAFGIVITVVFHGILMPLLGLVPPLWNLPFY
EHFSEIFGHIVWMWSIEIVRRDLRNRITREPDAEVP
>gnl|CDD|442701 COG3478, YpzJ, Predicted nucleic-acid-binding protein, contains Zn-ribbon domain [General function prediction only]
MMKKNYGCPKCGNTEYEVDEIAATGGGLSKIFDIQNNKFTVVSCKNCGYTEFYKAQTSTGSNILDLFFG
>gnl|CDD|442702 COG3479, PadC, Phenolic acid decarboxylase [Secondary metabolites biosynthesis, transport and catabolism]
MPTFPQHDLSGFVGKHFIYTYDNGWEYEIYVKNAHTIDYRIHSGMVGGRWVKDQRVDIVRLGEGIYKVSW
TEPTGTDVSLDFNLNDRVLHGTIFFPRWVVDHPEKTVCFQNDHLDLMREYRDAGPTYPTEVIDEFATITF
IEDCGADNEDVISCAPSELPAGYPDRLN
>gnl|CDD|442703 COG3480, SdrC, Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms]
MTLRRRSWTLLVALLLLVVLLLLLALLPVPYVIESPGPTYDTLGEVDGKPVISVEGAETYPTSGSLRLTT
VSVTGGATLFEALYAWLDPDYAVVPREEVYPPGESDEEYNQQNAAQMESSQENAIAAALRAAGYPVTEGV
YVASVLEGSPADGVLQPGDVITAVDGKPVTTAEDLRDALAAKKPGDTVTLTVTRDGKEKTVTVTLVKLPD
DDGRAGIGISLVTKVDFPFDVDIDLGDIGGPSAGLMFALGIYDQLTPGDLTGGKKIAGTGTIDADGTVGP
IGGIDQKVVAARRAGATIFLAPASNCAEAVGTIPTGLKVVPVDTLDDALDALEALRAGGDLPTC
>gnl|CDD|442704 COG3481, YhaM, 3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily [Translation, ribosomal structure and biogenesis]. 3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily is part of the Pathway/BioSystem: 23S rRNA modification
MMKRKFIKDLKPGEEVDGFFLIKSKELRTTKNGKPYLSLTLQDKTGTIEAKIWDASEEDIEEFQPGDVVK
VRGKVQEYQGRLQLKITRIRLADEEEVDPSDFLPSSPKDIEEMYEELLELIDSIENPYLKRLLRAILDKE
FRERFLTAPAAKSNHHAYIGGLLEHTLSVARLAKALADLYPELNRDLLIAGAILHDIGKVRELSGPPGTE
YTDEGQLLGHIVLGVEMIEEAAAELGDFPEELLLLLKHMILSHHGELEWGSPKRPKTPEAEILHYADNLD
AKMNMFERALEKVEPGGEWTEYIRALDRRFYKPKLE
>gnl|CDD|442705 COG3482, COG3482, Uncharacterized conserved protein [Function unknown]
MKIVVFLGPSLSAAEARAILDATYLPPAARGDLLRAVREGPRAIGIIDGVFEQVPAVWHKEILWALSQGV
RVFGAASMGALRAAELAPFGMIGVGAIFEWYRDGELEDDDEVAVAHAPAEDGYRPLSEPLVNIRATLAAA
VAAGVISAEEADALLAAAKALFYPERTYPRILAAAGEALSAEELAALLAFLPSGRVDQKREDALALLRAL
RERAAS
>gnl|CDD|442706 COG3483, TDO2, Tryptophan 2,3-dioxygenase (vermilion) [Amino acid transport and metabolism]
AAVRPLEEGITTDFSGRMSYGDYLQLDTLLSAQHPLSDHHDEMLFIIQHQTSELWFKLILHELRAARAAL
RADDLPPAFKMLARVSRIQEQLNAQWDVLATMTPSEYLAFRDALGQSSGFQSYQYRQIEFLLGNKNAAML
KPHEHDPEAHAELEAALEAPSLYDEALRLLARRGFPVPAEVLERDWTQPYEPDPAVEAAWLEVYRDPERH
WDLYELAEKLVDLEEAFQRWRFRHLKTVERIIGFKRGTGGSSGVAYLRKALDLTFFPELWSVRTEL
>gnl|CDD|442707 COG3484, COG3484, Predicted proteasome-type protease [Posttranslational modification, protein turnover, chaperones]
TYCVGIKLDDGLVFASDTRTNAGVDNISTFRKMHVFEVPGERVIVLMTAGNLATTQAVVSLLEEDLEAPA
GPNLLTAPSMFEAARYVGEALREVQAEDAEALEAAGVDFNASFILGGQIKGEPPRLFLIYPEGNFIEATE
DTPFLQIGETKYGKPILDRVLTPDTSLEDAAKCALVSFDSTMRSNLSVGLPIDLLVYERDSLEIGEQRRI
EEDDPYFQEIREQWSEALREAFDELP
>gnl|CDD|442708 COG3485, PcaH, Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport and catabolism]
ETPSQTEGPFYVDGLPLPLGADLARDAPGEPIRVTGRVLDGDGRPVAGALVEIWQADADGRYSHQDDGPL
DPNFNGRGRFTTDADGRYRFRTIKPGPYPIPNHPGRPAHIHFSVFAPGFERLTTQLYFPGDPYNASDPVF
GVRDTLIARFEPEDGALVYRFDIVLQGPGET
>gnl|CDD|442709 COG3486, IucD, Lysine/ornithine N-monooxygenase [Secondary metabolites biosynthesis, transport and catabolism]
MDDTKVYDLIGIGIGPFNLGLAALLDELPDLDALFLERKPEFDWHPGMLLEGATLQVPFLKDLVTLADPT
SPFSFLNYLKEHGRLYDFYNRENFFPLRREYNDYCRWAAEQLDNVRFGTEVEAVEYDDDAGAFRVTVRDG
TGERETYRARNLVLGTGTRPYLPECFRGLPGERVFHSSEYLHRKEDLQAAKRVTVVGSGQSAAEIFLDLL
RRQDGPGAELTWVTRSPGFFPLDYSKFTNEIFSPEYVDYFYALPEEVRDRLLAEQKLLYKGISPDLINEI
YDLLYERSVGGDPPRVRLLPNSEVTAVERAGGGYRLTLRHLETGERFELETDAVVLATGYRPRLPAFLEP
LADRIRRDEDGRLRVDRDYRVDWDGPRTGRIFVQNAEEHTHGIAAPDLSLGAWRNAVIINSLLGREVYPV
EARIAFQQFGVPAAAAAAPA
>gnl|CDD|442710 COG3487, IrpA, Imelysin-like iron-regulated protein IrpA, duplicated M75 peptidase-like domain [Function unknown]
MKRLLLLAALAAALLLAACSAAAAAATAAAVLATYADIAHAAYEDSLTTAKALQTAIDALLAAPSEETLA
AARAAWLAARVPYQQTEVFRFGNAIVDDWEGQVNAWPLDEGLIDYVDGSYGESDENPLATANIIANPSIT
IGGKTIDASTITPELLASLNEAGGVEANVATGYHAIEFLLWGQDLNGTGPGAGNRPYTDYVTGNCTNGNC
DRRAQYLKAATDLLVSDLEEMVAQWAPGGAYRAALEALDPKAGLRKILTGMGSLSYGELAGERMKVALML
NDPEDEHDCFSDNTHNSHYYNALGIRNVYLGRYTRVDGSVVSGPSLSDLVAAKDPALAAELKAKLDATVA
ALEAIKDAAEAGEAFDQMIAEGNAEGNALVQAAIDALVDQTRSIERAAAALGLDGIEFEGSDSLDN
>gnl|CDD|442711 COG3488, COG3488, Uncharacterized conserved protein with two CxxC motifs, DUF1111 family [General function prediction only]
SLLALLALLALAAACTAPTTDFSAPEPFEALPGGATTVYDTSRNAFSQPAANLSFEERLDFVVGNSLFRK
PWVSAPSSTTARDGLGPLFNARSCQACHIKDGRGHPPEGPGEDAVSMLLRLSIPGADAHGGPLPDPVYGG
QLQDFAIPGVAAEGRVVISYEEVTVTLADGETVTLRKPTYSFTDLGYGPLHPDTMLSPRVAPPMIGLGLL
EAIPEADILALADPDDADGDGISGRPNRVWDPETGATRLGRFGWKAGQPSLRQQSAGAFAGDMGITSPLF
PSEDCTAAQTACLAAPNGGEPEISDELLDLVTFYSRNLAVPARRDVDDPQVLRGKQLFYQAGCAACHTPK
FVTGRLAPFPELSNQTIWPYTDLLLHDMGEGLADGRPEFLASGREWRTPPLWGIGLTETVNGHTRFLHDG
RARTLLEAILWHGGEAEASRDRFVALSKADRAALLAFLESL
>gnl|CDD|442712 COG3489, IrpA2, Imelysin-like iron-regulated protein IrpA, duplicated M75 peptidase-like domain [General function prediction only]
MKKIKLALALALLLLLSACSPSDSTDSSDEFDRAAMLTNLADNVIIPAYQDFATAAAALATATDAFCAAP
SEATLAAARAAWRDAYLAWQKVEPFRFGPAEENNRRERINFWPDRRGLIEALIASGALTPYDLAGSSVAA
QGLPALEYLLFGEGADDLAITTAENAARRCAYLKAIAANLAALATELLTAWTPPGGYRAQFVAAGGDNPL
YPDAKEALNELVNALITGLEKVKDQKLGIPLGLFSAGTAKPELAEAWRSGNSLALLKANLEALQALFNGG
SDGTGLDDYLDALGAKDLADSINAQFDAARAALEALPAPLEEALADDRAALEALYDELKALVRLLKVDLA
SALGLTLGFNDNDGD
>gnl|CDD|442713 COG3490, COG3490, Uncharacterized conserved protein, DUF1513 domain [Function unknown]
MMMMDRRQFLAGLGAALALLPRLAWAAAAGAPALLSAARDADGSYAAAGLDADGRILFRVPLPARGHGVA
AHPDRPEAVAFARRPGTFALVFDCRTGRVLQRLTAPEGRHFYGHGVFSPDGRLLYTTENDFETGRGVIGV
YDARDGYRRIGEFPSHGIGPHELLLMPDGRTLVVANGGIETHPDTGREKLNLDTMRPSLVYLDARSGALL
EQHELPDDLHQLSIRHLAVAADGTVWFALQYEGDPGDAPPLVGLHRRGGALRLLEAPEEELRRLRGYIGS
VAADADGGLVAVTSPRGGRVALWDAATGRLLGAAPLPDVCGLAAAADGFLASSGRGQLVRLDAGGATLLR
LRLPGLAWDNHLVRL
>gnl|CDD|442714 COG3491, PcbC, Isopenicillin N synthase and related dioxygenases [Secondary metabolites biosynthesis, transport and catabolism]
STSFSSIPVIDLSPLRSGDPADRAAFAAELGEACREVGFFYVTGHGIPAELIDRLYAAARRFFALPEEEK
LKYAIPGSPGQRGYTPFGGETAKGAKPPDLKEFFDIGRELPPDDPDAGPPLYGPNQWPEELPGFREAVLA
YYAALEALGRRLLRAFALALGLPEDYFDDLFDDPNSILRLIHYPPQPAPPPPGQVGAGAHTDYGLLTLLL
QDDVGGLQVLTRDGEWIDAPPVPGAFVVNIGDMLERWTNGRLRSTPHRVVNPAAGRERYSIPFFLHPNPD
AVIEPLPSCVTADDPARYEPITAGDYLKERLAEIGLYRKA
>gnl|CDD|442715 COG3492, COG3492, Uncharacterized conserved protein, DUF1244 family [Function unknown]
MDDQTRTELEAAAFRRLVAHLDERTDVQNIDLMNLAGFCRNCLSKWYREAAEERGVELDKDEAREIVYGM
PYAEWKAKYQTEATPEQLAAFEAAQA
>gnl|CDD|442716 COG3493, CitS, Na+/citrate or Na+/malate symporter [Energy production and conversion]
AVKTNTRAWAKLKKFKIGGIPLPLFLILAAVVLAAVYTGKLPSDMIGGFAVLMVLGFLLGEIGKRIPILK
SIGGGAILALFVPSYLVYYGLLPENVIKSVTTFMKTSNFLYFYIAALIVGSILGMNRKLLIKGFARYFPP
ILGGVIGAALVGTLVGMLFGLSFYHTFFYIVLPIMGGGIGEGAIPLSLIYAAILGQPQAEYFSQLIPALT
LGNIFAIICAGLLNKLGKKRPKLTGNGQLLRGNSDDLEEEEKETPLDVKLMGAGLLLAISLFLVGVLLSK
LIGIPAPALMILLAVLLKLFNLVPPELEEGAKQLYKFFSKNLTYPLLVGIGVAYTPLDELVAAFTPAYVV
TIVATVLGAVLGGFFVGKLVGFYPIEAAITAGLCMSGMGGTGDVAILSASNRMNLMPFAQISTRIGGAIT
LILASILLSLLL
>gnl|CDD|442717 COG3494, COG3494, Uncharacterized conserved protein, DUF1009 family [Function unknown]
GKLGLIAGGGRLPLLVAEAARAAGREVVVVALRGEADPELAAYAPHYWVRLGQLGKIIKALKREGVTEVV
MAGKVTRPRLFSDLRPDLRALRLLARLKDRGDDTLLRAVVRELEEEGFRVLGAHEILPDLLAPAGVLTRR
KPDEEERADIAFGFEVAKALGRLDIGQTVVVKDGAVLAVEAIEGTDAMIRRAGELRRGGGGVLVKVAKPG
QDLRFDLPTIGPRTIENAAEAGLAGIAVEAGKTLILDREEVIALADAAGIFIVGV
>gnl|CDD|442718 COG3495, COG3495, Uncharacterized conserved protein, DUF3299 family [Function unknown]
MKRLRALLLALLASAAAAEARELDWEDLIPEDDLEALPEDLHDLSDDDPRAEALLDRMQQASDSAPVVPE
LDGKAVRIPGFVVPLEDEEGKVTEFLLVPYFGACIHVPPPPPNQIVYVKLPKGVKLDDLYDPVWVTGTLK
VERTESDLATAGYSLEADSVEPYEEP
>gnl|CDD|442719 COG3496, COG3496, Uncharacterized conserved protein, DUF1365 family [Function unknown]
MASALYEGQVRHRRFRPVRHRFRYRVFMLLLDLDELDALFRRSRLFSRNRFNLLSFRDRDHGGDPGGPLR
AWVRELLAEAGGERPDGRVRLLTQPRVLGYVFNPVSFYYCYDADGQLRAILAEVNNTFGERHSYLLPVDD
GIGAGIRLRADKAFHVSPFMPMDGRYRFRFSPPGDRLRVHIDNYDGGGKLLDATLSGRRRPLTDASLLRA
LLRYPLMTLKVVAGIHWQALKLWLKGVPFHPHPAPPAEEVSRSPP
>gnl|CDD|442720 COG3497, COG3497, Phage tail sheath protein FI [Mobilome: prophages, transposons]
GLEALEAADEKLGVKPRILIAPGLSSLPAVAAALLAHCEKLRAFAILDAPGDGTTLADAIAYRGNFGYDS
RRAALYYPWVKVFDTNATVTVPPSGHAAGLYARVDAERGVWKSPSNKEINGVTGLSRPVGFDLQLTDTEA
NLLNPKGINTIRNFPGRGFRVWGNRTLSSDPEWRFINVRRTFDFIEESIAEATQWAVDEPNTPALWDDIR
ESINAFLRTLWRQGALLGGKVWCDEETNTAEDIAAGKLVIDIGFAPVPPAEFITFRIRQTDGY
>gnl|CDD|442721 COG3498, COG3498, Phage tail tube protein FII [Mobilome: prophages, transposons]
LPRKLKNFNVYVDGNSYLGVAEEVTLPKLTRKTEEYRGGGMDGPIEVDLGMEKLEAEFTLGGYDPDVLKL
FGLNPGDAVQLTFRGAYQDDDTGEVVPVEVVMRGRLKEIDPGTWKPGEKTETKVTFSLTYYKLTVDGKEL
IEIDKLNNIYKVNGVDQLADIRAALGL
>gnl|CDD|442722 COG3499, COG3499, Phage protein U [Mobilome: prophages, transposons]
DFVFELSTAPYQELQRSTSYRWASHARIGRRPALQFTGPGLDTITLSGVLYPELTGGRAELDALRAMADA
GKALPLVDGNGRVLGWFVIESISETQSEFDADGTARKIEFTLTLKRYDEDLAN
>gnl|CDD|442723 COG3500, gpD, Phage protein D [Mobilome: prophages, transposons]
MSTTGSVRTPRFRIKVNGKDITADIAPRLLSLTVTDNLGGEADTLELTLDDGDGRWDDLFLPRRGAELEI
SLGYGGEGLLFKGIFTVDEIEFSGPPDTLTIRARDADVRLSLRTRRSRSWEDTTLSDIVRQIAGRHGLTP
KVDATSIKIEHIDQTNESDLDFLTRLAERNGAVVKVKDGKLVFKPPGAGESASPVLTLTGSDLISFSFRL
DARGQYTGVTARWWDPKTKKLIEATASAPKLGSGADVLRLRHTPAASQAEAKAAAKAKLRKLQRGKVTGS
VTLAGNPDLRAGSPVELSGFGPRFDGKYYVTSVTHTLSSGGYTTELELERPPFGEG
>gnl|CDD|442724 COG3501, VgrG, Uncharacterized conserved protein VgrG, implicated in type VI secretion and phage assembly [Intracellular trafficking, secretion, and vesicular transport, Mobilome: prophages, transposons, General function prediction only]
MSLSQSNRLLTLETPLGDDALLVLRFSGEEALSRPFEFELELLSEDADLDLDALLGKPATLTLRTADGPE
RYFHGIVTEFEQLGTDGGLARYRLTLVPWLWLLTLRRDSRIFQDKSVPDIVEEVLAEYGLAAFEFRLSGS
YPPREYCVQYRESDLDFVSRLLEEEGIYYYFEHEEGGHTLVLADDPSAHPPLPGATLPYHPRSGADEEED
SITRWRVRRRVRPGKVTLRDYDFKKPAADLEASASSPRDGDEGDLEVYDYPGRYTADPAEGERLARLRLE
ALRARAVRVEGESNVRGLAPGRRFTLTGHPRADLNGEYLVTSVTHEGSQNLYSGAGGEDGGYRNRFTAIP
ADVPFRPPRRTPKPRIAGPQTATVVGPAGEEIHTDEYGRVKVQFHWDREGKKDENSSCWVRVAQPWAGAG
WGGHFIPRVGQEVLVAFLDGDPDRPIVTGRVYNGANMPPYTLPANKTRSGIRTRSSPGGGFNELRFDDKA
GQEEIFLHAEKDMNTLVDNDETITVGNDRTEEVGTDETGTVAGNQGLTVSGDQTVVVGGNQTLVVGGART
LVVGGNLAAVVGGAAATAGGAQATLVAGALLLLAAGGALTTVGGGGTTTGGGAAATAGGGGAGAAAGGAA
TAAAGAAATSAAGGASSAAAAAGGAAGAGGGGLAAAGGGGAAAAGGAGAGGAGGGAGALAAGAAAVAAAA
AGGAGGGAAAGGIIGAGGTGIGGGGATAGGGAGASGGGAAAGA
>gnl|CDD|442725 COG3502, COG3502, Uncharacterized conserved protein, DUF952 family [Function unknown]
MMMIYHIAPAAEWEAAEAAGEYRGASLDADGFIHFSTAEQVAETANKHFAGQEDLVLLAIDPDALGAALR
WEPSRGGALFPHLYGPLPLDAVVWVRPLPLGPDGRFVLPELLR
>gnl|CDD|442726 COG3503, COG3503, Uncharacterized membrane protein, DUF1624 family [Function unknown]
TSRLASIDALRGLAMVLMALDHVRDDLHFFGLVPTDLATTPPWRWFTHLCAPLFLFLAGVSLYLAHSRGI
RWRALSRFLLKRGLWLILLALLITLFTWLFFPDSFIYFGVLHAIGVSMILLALLLRLPRWALLLLGLAII
AGHNLLDGIHFDSPWLLWLGLHTRGPPTLDYYPLLPWFGVMLLGYALGRLFYPGGARRRLLRKYPPSRLL
RPLAVLGRHSLFIYLLHQPVLHGLLLLAALLLGPNAGDFALYPLCRWFCRYKARRRDWWLSYL
>gnl|CDD|442727 COG3504, VirB9, Type IV secretory pathway, VirB9 components [Intracellular trafficking, secretion, and vesicular transport]
ALVTPRPGAYDNRIRVVPYNPGAVYRVYTAPGYVTDIELEPGEEIESVAAGDTVRWQVGPTKGNHLFVKP
TEPGLDTNLTVVTNRRTYHFELRSTADRATYMYRVRFRYPDDEAAALAAAAAAAAAAAAAPVAPGVDPEP
LNFNYTISGDAALRPVRVFDDGRFTYIRFPAGNGELPAIFVVGPDGEESLVNYRVRGNYVVVDRVFPAAV
LRLGDEVVCIENTGFGPAK
>gnl|CDD|442728 COG3505, VirD4, Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport]
HVLVIGPTGSGKTVGLVIPNLTQLARGESVVVTDPKGDLAELTAGFRRRAGYDVYVFDPFDPERSHRWNP
LDEIRDPADAQELAEALIPALGGGGGGDPFWREAARALLAALILALAEEGRRTLADVYRLLSEPEEELRE
LLEALPESPHPPVADTLAAFLNAAEKTRSSVLSTLASALELLSDPEVAALTSGSDFDLRDLIREKGTLYL
VLPPDDLSTLAPLLRLLLSQLIRALLRRAERSGRLPRPVLLLLDEFANLGRLPSLETLLATGRGYGIRLV
LILQSLAQLEAIYGEEGAETILGNCGTKIFLGVNDPETAEYLSELLGKRTVERRSESRSRGSRSRSRSEQ
ERPLLTPDELRRLPDGEAIVLVRGGPPIRAKKIRYYKDPEPAPAFEPRDAEA
>gnl|CDD|442729 COG3506, Ree1, Regulation of enolase protein 1 (function unknown), concanavalin A-like superfamily [Function unknown]
MKILPSKLRWLNEPARWSVTDGALTVTTDPGTDFWRRTHYGFVRDNGHFLLAEVDGDFTFEVKVTGDFKE
LYDQAGLMVRVDEENWIKAGIEYVPDGVPRLGSVVTNGYSDWSTGPVPGDPKSVWLRLSRRGDALRIQYS
LDGKTWTLLRLAPLPPAAPVKVGLMACSPTGEGFTVRFSDFSLTPPDWKDLHDGS
>gnl|CDD|442730 COG3507, XynB2, Beta-xylosidase [Carbohydrate transport and metabolism]
MKKLLLLLLLLLAAAAALGNTYTNPVLPGDYPDPSIIRVGDTYYLYGTSFEYFPGLPIFHSKDLVNWELV
GHALDRLPQWADPYSGGIWAPDIRYHNGKYYLYYTAVDGGKNRSGIGVATADDPEGPWSDPGPLVCPGGN
GIDPSVFVDDDGKAYLVYGSGGGGIYVAELDPDTGKLLGEPKTLAPGGEGGWIEGPHIYKRNGYYYLFYS
EGGTCNSGYAVRVARSKSPTGPYEDAPGNPILTQRSDGGIQGPGHGSLVETPDGEWYLVYHAYRPPGGLG
RETFLDPVTWNEDGWPVVGPGTGEPPQPLPAPESDDFDGPLGLQWSLGYLRLTRQFTATTKLRAGLVLYG
N
>gnl|CDD|442731 COG3508, HmgA, Homogentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism]
NEMATYALPGALPRKRHTPQRAPDGLYAEELLGGEGFTGPRSWLYHIRPPTAHGDFEPVEDGPKTADDGP
LRPRHLRWNPLPPDGGDFVDGRRTLLGNGDVAIHLYAANESMDRFFRNADGDELIFVHEGSGRLETEFGH
LEVEPGDYVVIPRGTTYRVELDDGPARGLVIENYGAPFRLPERGQLGEHAPYNERDFRTPVAAYEDDEGE
FEVVVKFRGRLWRATYPHSPLDVVGWDGNLYPYKFNIRDFEPITGIRFHPPPSIHTTFTAPNFVVCSFVP
RWLDVHPGAIRPPYYHSNVDSDEVMFYVDGDFDSRKGIEPGGISLHPCGIPHGPHPGAFEAAINKGKKET
DELAVMFDTRRPLRLTEAALEVEDPDYADSWQ
>gnl|CDD|442732 COG3509, LpqC, Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism]
MRRLRRLAALAALLALLPAAAAAGDFERTFTVGGGTRTYRLYVPAGYDGGAPLPLVVALHGCGGSAADFA
AGTGLNALADREGFIVVYPEGTGRAPGRCWNWFDGRDQRRGRDDVAFIAALVDDLAARYGIDPKRVYVTG
LSAGGAMAYRLACEYPDVFAAVAPVAGLPYGAASDAACAPGRPVPVLVIHGTADPTVPYAGAEETLAQWA
ALNGCAATPTRTEVTDGGGYTRTRYSDCAGGAEVELYTVEGGGHAWPGGGAAGPYTDPRGIDASEEIWRF
FGAH
>gnl|CDD|442733 COG3510, CmcI, Cephalosporin hydroxylase [Defense mechanisms]
EEFEQERRERIASLGSDEALDDLSEEWLRASYKNKYSYNFSWLGRPIIQYPQDMVAYQEIIWELKPDLII
ETGIAHGGSLIFSASMLALLGMKGKVLGIDIDIRPHNRAAIEAHPLAPRIELIEGSSTAPEIVEQVKALA
KPGERVMVILDSNHTHEHVLAELEAYAPLVTPGSYLVVFDTIIEDLPVDMFPDRPWGPGNNPKTAVEEYL
KEHPEFEIDKSIEHKLLITVAPDGYLKRI
>gnl|CDD|442734 COG3511, PlcC, Phospholipase C [Cell wall/membrane/envelope biogenesis]
ANRTGTLTDIKHVVVLMQENRSFDHYFGTLPGVRGFGDPNPIPQPDGKPVFTQLPDPNGALPNLPFRLDT
TQTNAQRTGDLPHSWYDEQAAWNGGKMDGFVAAKDAGGLTMGYYDRADLPFYYALADAFTLCDNYFCSVF
GGTTPNRLYLVSGTTPPYGNAGGPDVYNVDADPSSATTLPPQTWTTIGDRLEAAGVSWKWYQGGWDNALA
GPHHNPLQYFAQFANATPDRASHLYDRLDDFRADVAAGTLPAVSFIKPPGAYSEHPGYSDPADGAAYIAD
VLDALTASPVWSKTAIIITYDENGGFFDHVPPPVPPSSTDGEGGDGDPYGLGPRVPMLVISPWAKGGWVD
HTVFDHTSVLRFIEKRFGLPELNIPWRRAVAGDLTSAFDFAR
>gnl|CDD|226043 COG3512, COG3512, CRISPR-associated protein, Cas2 homolog [Defense mechanisms]
MSEYKFMRMILMFDLPTDTAAERKAANKFRQFLLKDGYQMLQFSVYSRILKGRDSNQKHIGRLREHLPNE
GNIRCLEVTEKQFARMKLLLGELVFNEKKVNSDQLLLFLGEAFDES
>gnl|CDD|442735 COG3513, Cas9, CRISPR-Cas system type-II protein Cas9 [Defense mechanisms]. CRISPR-Cas system type-II protein Cas9 is part of the Pathway/BioSystem: CRISPR-Cas system
MDKYILGLDLGINSVGWAVLELDEDGEPGEIIDAGVRIFDDGEDPKSGESLAAARREARGARRRRRRRKH
RLRRLKRLLVEEGLLPADDAERKALLPLNPYELRAKALDEKLSPEELGRALFHLAQRRGFKSNRKTDSKD
NESGKVKDAIKELRERLEAKGARTVGEYLYRRLQENGKVRNRKGDYDFYIPREDLEDEFEAIWAAQAEFG
PALLTEELRDELLEIIFFQRPLKSGKKLVGKCTFEPDEKRAPKASPLFQRFRILQKLNNLRIVDDGGEER
PLTLEERQKIIDLLENKKKLTFKKLRKLLGLPDGVIFKGFNYEDDDRAKLKGDKTYAKLAKIFGKAWLNE
FDPEILDDIVEALTLFKDDEELKEWLKKLYGLDEEQAEALANLPLPDGYGNLSLKALRKILPLLEEGLDY
DEAVKAAGYDHSSLEILDRLPPIGEEKRKGSIRNPVVHRALNQLRKVVNALIRKYGKPDEIHIELARDLK
KSKKERKEIQKRQRENEKAREKAREEIAEEGGGEPSRRDILKYRLWEEQNGRCPYTGKPISISDLLDGSV
EIDHILPRSRTLDDSFNNKVLCLADANREKGNRTPYEALGGDEAEKWEEILARVENLKLIPQKKKKRFLK
KELDRDDDEGFIARQLNDTRYISRLAAEYLKSLYPFEDKGKRKVRVVPGQLTAMLRRAWGLNKILSDDGE
KNRDDHRHHAIDALVIACTTQGLLQRLAKASREREDAEKAEEHFPPPWDGFRQDVAEAVDEIFVSHAPRR
KVTGQLHKETIYSTGEGKVVLRKPLTSLKLKDLEKIVDPKKA
>gnl|CDD|442736 COG3514, COG3514, Uncharacterized conserved protein, DUF4415 family [Function unknown]
MSKKSKTDLKALTAEEDEEITAAAAIDPSDAPELTDEFFARARKRRRGRPKAAPPKVQVTIRLDPDVLEW
FKATGPGWQTRINAALRDYLK
>gnl|CDD|442737 COG3515, TssA1, Type VI protein secretion system component TssA1/VasJ/EvfE, contains ImpA_N domain [Intracellular trafficking, secretion, and vesicular transport]
MDIEALLAPISGDAPCGEDLRYDPDFDALKEARRGDDEQQQGDWVIELKPADWREVERLAEELLTTRSKD
LRVAVWLAEALLRLDGLAGLADGLELLAGLLERFWDDLHPQLDEDDPEERVNALAWLNDPRLLLAPLRLA
PLTEGRGGELSLRDYEQARDLERLPARAAAIPPTLERLEAALADTSAAFLQALLAALEAALAALEALEAA
LDERLGDDAPDLSPLRKALEEILAALRRLAAARGAPAPAAEAAAPAPAAAPAAAAPAAAAAAAPGPIQSR
EDALRQLREVADYFRRTEPSSPVPYLLERAVRWGGMPLAELLRELIPDALSQLERLLGIRPE
>gnl|CDD|442738 COG3516, TssB, Predicted component TssA of the type VI protein secretion system [Intracellular trafficking, secretion, and vesicular transport]
MSESKQKFLSRVRKPRVQITYDVETGGAEEKKELPFVMGVLGDLSGKPEEPLPPLKERKFVEIDKDNFDD
VMKAIAPRLAFSVPNTLSGDGGELNVDLTFESMDDFSPEAVARQVPPLRKLLEAREALADLKGKLDGNPA
LEKLLEKVLQDPELLQALAAELGAEAEAEED
>gnl|CDD|442739 COG3517, COG3517, Predicted component TssB of the type VI protein secretion system, VipA/VipB/TssB family [Intracellular trafficking, secretion, and vesicular transport]
EGSLLDQILAQTRLPPSDEARDIAKAAVATLVAQVLEGTVTVSKDLKALIDAMIAEIDELLSEQLNEILH
HPEFQKLESSWRGLHYLVDNTETDENLKIRVLNVSKEELLKDFEKAPEFDQSGLFKKVYEEEYGTFGGEP
YGALIGDYEFDHSPEDIALLRKMSKVAAAAHAPFIAAASPSLFGLDSFTELSNPRDLAKIFETPEYAKWR
SFRESEDSRYVGLTLPRFLLRLPYGPDTNPVEGFNFEEDVDGADHEKYLWGNAAYALATNLTRAFAKYGW
CAAIRGVEGGGLVEGLPTHTFETDDGGVDLKCPTEVAITDRREKELSDLGFIPLVHRKNTDYAAFFSAQS
LQKPKEYDDPDATANARLSARLPYIFAVSRFAHYLKVMQRDKIGSFKEREDLERELNDWISQYVTGDDNA
SQETKARYPLREARVEVEEVPGKPGWYRAVLFLRPHFQLEGLTVSLRLVAELPK
>gnl|CDD|442740 COG3518, COG3518, Predicted component of the type VI protein secretion system [Intracellular trafficking, secretion, and vesicular transport]
MARLRPRRRLQPSLLDRLTDDEPDRSRESPLSRVVSLEQLRESVRRDLEWLLNTRRGEASLLAAYPEVRR
SVLNYGLPDLSGASLGSPDDREAIERAIRQAILRFEPRLRRVSVTVLPDDDDSPNTLRFRIEAVLWADPA
PEPVRFDTVLDLETGRVSVSDL
>gnl|CDD|442741 COG3519, VasA, Type VI protein secretion system component VasA [Intracellular trafficking, secretion, and vesicular transport]
MDDELLRYYNRELAYLRELGAEFAERYPKIAGRLGLSGDEVADPHVERLLEGFAFLTARVQQKLDDEFPE
LTEALLEVLYPHYLRPIPSMSIVQFTPDPAAGDLTEGFTIPRGTELLSRPVDGTRCRFRTAYDVTLWPLE
ITDARLESAPAALPLLGLPAGAAAVLRLRLRTSGGLPLADLGLDRLRFYLDGEPSLASALYELLFAHVVG
VVVRPGGGDPAPVRLPADALRPVGFDDDEALLPYPARSFPGYRLLQEYFAFPEKFLFFDLTGLEALLLRA
AGDEFELVILLDRAPPRLELAVDADNFRLHCTPVINLFPKRAEPIRLDHRQHEYPLVPDRRRPLDYEVYS
VDRVTGVRAGGGEEREFRPFYSFRHGGGGDAPGAYYHLRRRPRTRSSYPGTETFLSLVDLDEAPYLPEDE
TLSVELTCTNRDLPELLPVGGQGDFTLEDSAPVASIRCLTGPTPPRRPPLGGALAWRLISHLSLNYLSLA
DGEDGAEALRELLRLYDFTDDAASRRQIDGIVSVESRPVTRRLPGPGPRGFVRGLEITLTLDESAFSGEG
AFLFGSVLERFFALYASINSFTQLVLRSTQRGEIKRWPPRAGQRPLL
>gnl|CDD|442742 COG3520, COG3520, Predicted component of the type VI protein secretion system [Intracellular trafficking, secretion, and vesicular transport]
MATTDRRAAPDLIERLLAEPWRFDFFQAVRLLERLAPRRPPLGRAARPRDEPVRFRQSPSLGFPPSEIAS
VEPDEGDGPPRLTVNFLGLFGPNGPLPLHYTEYLAQRERHGDPALRAFLDLFNHRLLSLFYRAWRKYRPP
VSFERGGDDRFSRYLLALAGLGTPGLRERLAVPDSALLAYAGLLARRTRSAEGLEALLSHYFGVPVRIEE
FVGRWVPLPPDQQTRLGGGQNARLGQSAVLGSRVWDRQGKFRIRIGPLSLAQYLRFLPGGDLLTALRALV
RFYLGDELDWDLRLVLKAEEVPPARLGGARGARLGWTSWLGSRPAAPDADDVTLSLERYQG
>gnl|CDD|442743 COG3521, COG3521, Predicted component of the type VI protein secretion system [Intracellular trafficking, secretion, and vesicular transport]
MKKRLKRLARLLLLLLLLLLLAGCGSTQKVTVIFYKQPTTLHLTLTAAPDLNPDANGRPSPVVVRVYQLK
DDSAFESADFFALLDDDEEALGADLLSVKELTLLPGESKTLDLPLDPEARYIGVVALFRDPDGARWRLVI
PVPELDSDGKLTIELGGNAITLVPEKEV
>gnl|CDD|442744 COG3522, COG3522, Predicted component of the type VI protein secretion system [Intracellular trafficking, secretion, and vesicular transport]
MSKINKVVWSEGMFLRPQHFQQQDRYLEHLLRARLRALSPYPWGFSELELDEDALALGKLALRRASGVFP
DGTPFDAPDADPLPPPLDLPELFVRNQTVYLALPLRRPGGANVAFEEAADSLARYRAEEEEVRDLNSGGG
EPAEVQVARLNLRLLLESEDRDGYVTLPVARILERRADGGVVLDESFIPPLLSISASPVLAGFLRELLGL
LQARAEALAGRLREPGEFGVADVADFLLLQTLNRAEPLLRHLLRLPQLHPERLYRELLRLAGELATFSSE
SRRPPDLPAYDHDDLGASFAPLMDLLRQLLSTVLEQRAIAIPLEERRPGIWVARLDDRRLLENADFVLAV
RADLPAEELRERFPAQVKVGSVEDIRDLVNSALPGIPLRPLPVAPRQIPYHAGYVYFELDRSGPLWQQML
QSGGIALHVPGDFPGLELELWAVRRS
>gnl|CDD|442745 COG3523, IcmF, Type VI protein secretion system component VasK [Intracellular trafficking, secretion, and vesicular transport]
MLLRFLTSRWVLSLLGLLALALLIWFGGPLLAIGDYRPLESVLVRLLAIAVILLLWLLVWLVRRWRARRA
NRALEDALAEQAEEKAAADPSREEIEALRERFQEALATLKKSRLGQGGGRRALYELPWYLIIGPPGAGKT
TALVNSGLKFPLADKFGKAAIRGVGGTRNCDWWFTDEAVLIDTAGRYTTQDSDAEVDRAEWLGFLDLLKK
HRPRQPINGVIVAISLADLLTQSPEEREQHAKALRQRLQELRERLGIRFPVYVLFTKADLLAGFSEFFAD
LDKEEREQVWGFTFPYDEKQEFDLLAEFDAEFDELLERLNERLLDRLQQERDPERRALIFGFPQQFAALK
EALAEFLEELFEPNRYQTPPLLRGVYFTSGTQEGTPIDRVMGALARNFGLSRAALPAQSGSGRSYFLKDL
FSKVIFPEAGLAGRNRRWERRRRWLRRAAYAAAALALLGLLGGWTWSYLNNRRLLAEVEAKVDAYRALAA
ALLVADTDLAALLPALNALRDLPAGYGYRRDDPPLSAGLGLYQGDKLGPAARAAYLRALEQLLLPRLALR
LEEQLRQAPADPEELYEALKAYLMLGDPEHRDADFLKAWMARDWRELLPGNTRAELRAALERHLDALLDL
GGDPSAPPLPLDEALVAQARAELRRVPLAQRVYARLKARALATRLPDFTLADAVGPQAALVFTRSSGKPL
TLGIPGLFTREGYHEVFLPAIDELAEELARDDWVLGLSAEDDLSEADREQLQREVRQLYLADYIAEWRAF
LGDLRLAPFTSLAQAIAALRVLSSPDSPLRRLLRAVADETTLTRPSEAAAGGAAAKGLLAAAKARLLSAR
GRLGRLLGADAAAAAAQVPGQPVDRHFAPLHRLVEANDGGPAPLDDYLQALNELYTYLTAIANAPDPGKA
ALKLAKASGGGSDLISALKAEAGRLPEPLRRWLGSLADQAWSVVLGGARAHLNRRWRAEVYPFCRQAIAG
RYPFAPRSSRDVALADFARFFGPGGILDSFFQQNLKPFVDTSGRPWRFRPWDGQGLGLSPAVLAQFQRAA
AIRDAFFAGGGAEPSVRFQIKPVSLDPGISRFTLEIDGQLLRYRHGPQRPVSVVWPGPGGSNGARITLTP
LDGTSPSSLSYEGPWALFRLLDKAQLTTVSPDSFTVTFTVDGRSVTYELRADSVNNPFALPLLRGFRCPE
SL
>gnl|CDD|442746 COG3524, KpsE, Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]
QRARRRPRRKLLLLLFLLFVLLPTLLAALYYGLIASDQYVSEARFVVRSAEGQSGSDGLGGLLGGTGFSS
SSQDSYIVQDYLRSRDAVERLDAELDLRAHYSRPGIDPLSRLDPDASIEDLYKYYRRRVKVEYDSTSGII
TLEVRAFDPEDAQAIAEALLAESEELVNQLSERAREDAVRFAEEEVERAEERLRDAREALLAFRNRNGIL
DPEATAEALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDS
LASLLAEYERLELEREFAEKAYTSALAALEQARIEAARQQRYLAVIVQPTLPDEALYPRRLYNILLVFLI
LLLLYGIGSLLVASIREHRD
>gnl|CDD|442747 COG3525, Chb, N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]
MKKWALYFLLLLLLLLSCAANAAVAAAALSIIPTPVSVTVGEGSFTLSAGTTIVADGPELKAAAELLADR
LKRATGLPLSVAAAAAGAAIVLAIKDPSLGPEAYRLTVTPKGITITAADPAGVFYGLQTLLQLLPAAAEK
GGSWSLPAVEIEDAPRFGWRGLMLDVARHFFPKEFVKRLIDLMALYKLNVFHWHLTDDQGWRIEIKKYPE
LTEVGAWRGHTLIGHDPQPFDGKPYGGFYTQEDIREIVAYAAARGITVIPEIDMPGHARAAIAAYPELGC
TGKPYSVRSVWGVFDNVLNPGKESTYTFLEDVLDEVAALFPSPYIHIGGDEVPKGQWEKSPACQALMKEL
GLKDEHELQSYFIRRVEKILASKGRKMIGWDEILEGGLAPNATVMSWRGEDGGIEAAKAGHDVVMSPGSY
LYFDYAQSDDPDEPYAWGGFLPLEKVYSFDPVPEGLTAEEAKHILGVQANLWTEYIPTPERVEYMLFPRL
LALAERAWSPPEDKDWDDFLNRLQRHLPRLDALGVNYRPPAPGAKVEGKLTLNTELPGLEIRYTTDGSNS
PPYTAPVAVSGTVKARTF
>gnl|CDD|442748 COG3526, COG3526, Predicted selenoprotein, Rdx family [General function prediction only]
MMKPRVEIEYCTQCGWLLRAAWMAQELLTTFGEELGEVALVPGTGGVFEVRVDGELIWDRKEDGGFPEAK
ELKQRVRDRIAPERDLGHSDRKS
>gnl|CDD|442749 COG3527, AlsD, Alpha-acetolactate decarboxylase [Secondary metabolites biosynthesis, transport and catabolism]
AAAAEHPENTLYQYSTLSALMAGVYDGTITIGELLKHGDFGIGTFNGLDGELIVLDGKVYQARADGSARE
VPDDEKTPFAVVTFFEPDKTVTLENPMTREELEELIDKLLPSKNLFYAVRIDGTFSYVKTRSVPKQEKPY
PPLVEVAKNQPEFTFENVKGTLVGFYTPEYFQGINVPGYHLHFISDDRKFGGHVLDFRLESGTVEIQEID
DLELHLPETEDFLKADLSPEDLDEEIEKAEG
>gnl|CDD|442750 COG3528, COG3528, Uncharacterized conserved protein, DUF2219 family [Function unknown]
MKSLKSLLLLLLLLAALAAQADAPDADNAGTFSLQLDNDLFAGTDRYYTNGLFLSYTSPNDKLPGWLRWL
ARLFDGDGKKRVGLSLGQNIYTPSDIEATDPQPDDRPYAGYLYGGLSLISLTDNSLDRLSLTLGVVGPAA
LAEEVQNGVHKLIGSDEPEGWDNQLENEPGFNLSYERSWRLLRSSGGGLGFDLSPHAGAALGNLFTYASA
GLTLRLGQNLPSDFGSARIRPGLPGNAAFSPTRGFEWYFFAGVEGRYVAYDITLDGNTFRDSPSVDKRPL
VGDLEAGFALRWGGFRLSYSQVFRTKEFKGQDRGHSFGSLSLSYRF
>gnl|CDD|442751 COG3529, COG3529, Predicted nucleic-acid-binding protein, contains Zn-ribbon domain [General function prediction only]
MTKMKKRFIAGAVCPKCQAMDTLVLWRENGVEVRECVSCGYTETQPDEEVEAATEAEEQVIGIFKPE
>gnl|CDD|442752 COG3530, COG3530, Uncharacterized conserved protein, DUF3820 family [Function unknown]
MMMDPEDLIELANTKMPFGKYKGRLLIDLPEPYLVWFARKGFPKGKLGQLLALMYEIKLNGLEGLLRPLR
KRF
>gnl|CDD|442753 COG3531, COG3531, Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, protein turnover, chaperones]
KPKLHYIYDPLCGWCYGFAPVIEALAEALGDRLDVELLSGGLFPGSNRRPMDPEMRAYIQPHWQRIAQLT
GQPFGEAYNDLLRDGTFVLDSEPACRAVLAARELAPERELAMLHAIQRAFYVEGRDISDPEVLAELAAEL
GLDAEAFAAALASEETRQHIQQEFALARQLGVQGFPTLVLEQGGQLYLLPRGYGDPEALLAALEQL
>gnl|CDD|442754 COG3533, HybA1, Beta-L-arabinofuranosidase, GH127 family [Carbohydrate transport and metabolism]
AKLRPVPLSDVRLTDGFWGERQELNREYTLPHQWEQLEPDGLLANFRIAAGLKKGEYGGWEFDDHDVGKW
LEAAAYAYARTGDPELEARLDYVIDELAAAQEPDGYLGTYFTIEGGEKRWVLRLSHELYNAGHLIEGAVA
HYRATGKRKLLDVAIRLADWIDDTFGPLPDQLQGMLGHGGIEEALVELYRVTGDKRYLDLAKRFIDRRGR
LPLRGGEYFQDHDPLREQTDAVGHAVRAIYLYAGAADVAAETGDEEYLDALERLWDNVVNRKMYITGGNG
SRHDGEAFGPDYDLPNDTAYAETCASIGMLKLNRRLLLLTGDAKYADVYERALYNHILSGQSLDGGGFFY
FNPLRSGGYHERQPWFGCACCPGNGARTLASLGGYIYATSDDGLYVNLYIGSTLNWKLDGKGVKLRQETN
YPWDGKVRITVDPAKPGEFTLRLRIPGWAKGATVKVNGKPVDAEVEPGSYATINRTWKKGDVVELDLPMP
VRLVEANPRVPDDRGKVAVKRGPLVYCAESGDNGGDLDDLRLPDDAPLEAEYAPDLLGGVVVLKGEGLVS
GDPLTYRTPGGKPVDLTLIPYYAWANRGPGEMRVWLP
>gnl|CDD|442755 COG3534, AbfA, Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism]
RITIDPDFPIGTIDRRIYGHFAEHLGRCIYGGIYVGPDSPIADEDGFRKDVVEALKELGVPVLRWPGGCF
ADGYHWEDGIGPREKRPRRLNLAWGGVTETNSFGTHEFMDWCELLGAEPYLAVNLGSGTVQEARDWVEYC
NHPGGTPLSDLRRANGREEPWKVKYWGLGNEPWQCGGHMTAEEYARLAREYATAMRNVDPSIELVACGSS
GDDYEWTETVLEHAYDLVDGISLHYYYGNKGSATGFDEGDWASTLASALDMDEFIEKHSAIMDKYDPKKR
VGLSFDEWGVWYDVEPGTAPGFLEQQYTLRDALVAGLLLNIFLRHADRVKMANLAQLVNVLQPIILTDGG
KAWLTPTYHVFAMYSVHQRGTALPVEVDSPTYDTGGKFGDVPAVDASASRDEDGELTVFLVNRDPTEAVE
VEVDLRGFEAKVVEGRVLTADDLDAHNTFENPDRVVPRAFKGAKLEGGTLTVTLPPLSVVVLRLKLG
>gnl|CDD|442756 COG3535, COG3535, Uncharacterized conserved protein, DUF917 family [Function unknown]
MMRLLTEEDIEDLARGAAVLGTGGGGDPYIGKLLARQAIEEGGPVELVDPDELPDDALVVPVAMMGAPTV
LVEKLPSGEEAVRAVRALEEYLGRKIDAVMPIEIGGVNSLIPLAVAARLGLPVVDADGMGRAFPELQMTT
FYLAGVPATPMVLADEKGNVVILETIDNAWAERLARAVTVAMGGSAAVALYPMTGAQVKRAAIPGTLSLA
LELGRAIREAREAGADPVEALLAALGGRVLFKGKVTDVERRTEGGFDRGTVTIEGLDEDAGRTLTVEFQN
ENLVAWRDGEVLATVPDLICVLDAETGEPITTERLRYGQRVAVLALPAPPLWRTPEGLEVVGPRAFGYDI
DYVPVEEL
>gnl|CDD|442757 COG3536, COG3536, Uncharacterized conserved protein, DUF971 family [Function unknown]
MMTTPWPTEIRLHQASRVLEITFDDGHRFRLPAEYLRVYSPSAEVQGHGPGQEVLQPGKRDVNITGIEPV
GNYAVRLTFDDGHDSGIYSWDYLYELGRNQEALWQDYLDRLAAAGLSRDPPMPP
>gnl|CDD|442758 COG3537, COG3537, Putative alpha-1,2-mannosidase [Carbohydrate transport and metabolism]
MKRLLLLAALALLASCAAAAAAAAADLTDYVNPFIGTGGHGNTFPGATVPFGMVQLSPDTGANGWDWCSG
YHYSDSTIRGFSHTHLSGTGCGDYGDILVMPTTGEVKLDPDSGYASRFSHANETASPGYYSVTLADYGIT
AELTATERAGFHRYTFPAGDEAHLLLDLGHGLNKVTDSEVKVVDDRTITGYRTSGCGWAGNYRVYFVAKF
DKPFTSVGTWDDGTVTPGSTEASGKGVGAYLTFDTKAGEQVTVKVAISFVSVEGARANLEAEIPGWDFDA
VRAAARAAWNKELGKIEVEGGTEDQKRTFYTALYHSLLAPNLFSDVDGRYRGFDGKVHTAEGFTYYTNFS
LWDTYRALHPLLTLLAPERAGDMVNSLLAQYRQGGWLPRWSLPGNETNCMIGYHSDPVIADAYLKGIRGF
DAEAAYEAMLKNATVPPPDDAVGRKGLEYYLKLGYVPYDKIHESVSRTLEYAYDDFAIAQLAKALGKKED
AEYFLKRAQNYRNLFDPETGFMRGRNADGSWRTPFDPFAWGDDFTEGNAWQYTWSVPHDVAGLIELMGGR
EAFVAKLDSLFATPPTFDDSGHDITGGLIGQYAHGNEPSHHIPYLYNYAGQPWKTQEVVREILDTLYTDT
PDGLPGNEDNGQMSAWYVFSALGFYPVNPGSGEYVLGSPLFDKATIHLPNGKTFTIEAPNNSDKNRYIQS
VTLNGKPYTKTWITHSDIMAGGTLEFTMGATPNKTWGTAPEDAPPSLSAG
>gnl|CDD|442759 COG3538, COG3538, Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown]
MIKTPSVRPPAAERKFTSKAVEKAIARVKKKIKDPELAWLFENCFPNTLDTTVEFGTIDGDPDTFVITGD
IPAMWLRDSTAQVWPYLPLAKEDPALKQLIAGLINRQTKCILIDPYANAFNKDPNGSEWQDDLTDMKPGV
WERKWEIDSLCYPIRLAYLYWKATGDTSPFDEDWRKAMRLILKTFKEQQRHEGRGPYRFQRTTSRATDTL
PRDGYGTPVKPTGLIWSGFRPSDDACTYGYLIPSNLFAVVSLRQLAEIATEVLKDTALAAEARALADEVE
AAIKKYAIVEHPKYGKIYAYEVDGFGNYLLMDDANVPSLLSLPYLGYCDADDPVYQNTRKFVLSEDNPYF
FKGKAAEGIGSPHTGPDYIWPIALIMRGLTSTDDAEIRECLDTLKATDAGTGFMHESFHKDDPTKFTREW
FAWANTLFGELILKLAGEKPKLLKS
>gnl|CDD|442760 COG3539, FimA, Pilin (type 1 fimbrial protein) [Cell motility]
MKKLLLALLLALALSAAAAAAADGTVNFTGTVVAPTCTINTGSKDQTVDLGTVSTSDLNGVGSTSGPKPF
SIKLTNCDAGTSNSVKVTFTGTADSANPGLLANTGSGGASGVGIQLLDSDGTPIPLGTPSSAVTLTSNGS
ATLPFYARYVATGATVTAGSFNATATFTIDYQ
>gnl|CDD|442761 COG3540, PhoD, Phosphodiesterase/alkaline phosphatase D [Inorganic ion transport and metabolism]
LSRRSFLKGAAAAAAALALGAAPAAAAAAARDPFTLGVASGDPTPDSVVLWTRLAPDPPARPVPVRWEVA
TDESFRRVVRSGTVTATPERDHTVKVDVTGLEPGTRYFYRFRAGGETSPVGRFRTAPAPGAPDRLRFAFA
SCQNYEGGYFTAYRAMAEEDPDFVLHLGDYIYEDGPGPYGLPGLWRPEPSKEAETLADYRGRYAQYRSDP
DLQALHAAVPWIATWDDHEVANNWAGGGAEHDRYTEGDFAARRAAALQAFYEYMPIRRPGPDGDDGRIYR
RFRYGDLADLFMLDTRSYRDPQPCLQCPEADDPDRTLLGAEQLAWLKDGLAASTATWKVIAQQVPMGRLV
PDGAEGVAYNLDAWDGYPAERARLLDFIKDNGIRNVVVLTGDVHYAWASDLKPDRADPQGPTVGVEFVTG
SITSGGFGPGLDDATLNPHVKFVNAPQRGYGLVTVTPDSWTADFRVVTVTLPDEAGRPGLQP
>gnl|CDD|442762 COG3541, YcgL, Predicted nucleotidyltransferase YcgL [General function prediction only]
MRERILDKLERIEREHGVRVLLAVESGSRAWGFPSPDSDYDVRGIYVHPKEWYLGLEPPRDVIERPIGDE
LDLVGWELRKFLRLLLKSNPNVLEWLFSPIVYRETPFGEELRALAPRFLSRRAYHHYLGYAKSQLRKYLK
GELVRLKKYFYVLRPLLAGIWLLETGEIPMEFSELLELLAELLAEIDELLARKRGGEESELGPRLEELRA
FIERLLAELEAAAKKALPERPDRAALDALLRELLRARWG
>gnl|CDD|442763 COG3542, CFF1, Predicted sugar epimerase, cupin superfamily [General function prediction only]
MMMTAEELIEKLGLEPHPEGGYYRETYRSAERIPAAALGGGRAASTAIYFLLTAGEFSHWHRVDSDEIWH
FYAGDPLELHLIHPDGTYETVVLGPDLAAGQRPQLVVPAGTWQAARLLGGGGYALVGCTVAPGFDFEDFE
LAPRDELLA
>gnl|CDD|442764 COG3543, COG3543, Uncharacterized conserved protein, DUF1284 domain [Function unknown]
MMIRLRGHHLLCLLGFRGKGYSPAFVENMDAIIERLRKPGEEIEIVDGPDDICAPCPNNRDGHCTNESKV
RERDRKVLEDLGLEPGEVLTWDEILQRIRKAFSSGDIREICGGCEWLSLCYCKAGLGKLK
>gnl|CDD|442765 COG3544, COG3544, Uncharacterized conserved protein, DUF305 family [Function unknown]
MIPHHQQAVEMASGADFDRLFLQLMIAHHQGAIDMAQAELEHGKDPEVRELAQDIIAAQTAEIAQMRALL
AALGA
>gnl|CDD|442766 COG3545, YdeN, Predicted esterase of the alpha/beta hydrolase fold [General function prediction only]
LIVPGLGGSGPDHWQSWWERELPTVRRVEQPDWDRPDLDDWLAALDAAVAAADGPVVLVAHSLGCLAVAH
WAARLPRKVAGALLVAPPDPERPGFLPELDAGFAPIPRAPLPFPSIVVASRNDPYVSFERAERLARAWGA
ELIDLGAAGHINAESGFGEWPEGLALLAEL
>gnl|CDD|442767 COG3546, CotJC, Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and metabolism]
MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMRDPKYKDLLMDIGTEELGHVE
MVATTIALLLEGAPPELAPEDPPLAAIKGGGNPQHFIVHGGGALPVDSNGVPWTAAYVQASGNLVADLLS
NIAAEQRARLVYERLYEMTDDPGVKDMLGFLLAREIVHQQRFGKALEELQGKFPEKKKYEDQEFSYKYFN
FSTGDYSDRGPWNGGPPPGGEFEYVDGPEGGPPDLPEDPEEFA
>gnl|CDD|442768 COG3547, COG3547, Transposase [Mobilome: prophages, transposons]
METVIFVGIDVSKDTFDVAVVDEDGKVVLKVFRFANDRAGLLALLAWLKKLGPPCLVGMEATGGYHHWLA
RFLAAAGHEVVVVNPRQVKAFRKGRRAKTDRIDAEAIARAARRGRLRPVPVPSEEQQALRALVRRREQLV
KERTALKNRLRGLLLEFGIVWGPTGRALLKRLLELEAESLPPALRELLRSLLERIAALEEQIKELEKEIE
ELIKQDLDEKARLLLSIPGIGPITAATLLAEIGDIGRFRSARQLAAYAGLVPRQHSSGGKRGRGRISKRG
NRYLRRALYEAALSALRHNPRLKAWYQRLLAEGKPKKVAIVALARKLARIIWAVLKDGTPYDPPYAAAA
>gnl|CDD|442769 COG3548, COG3548, Uncharacterized membrane protein [Function unknown]
MKKVDEEAERGKERLEAFSDGVFAIAITLLVLELKVPEGSDGELLAALLELWPSFLSYVLSFIVIGIYWN
NHHRLFRYVKRVDGRLLWLNLLLLFFISLLPFTTALLGEYPFAPLAVALYGLNLLLIGLAYLLLWRYAIR
HGLLDSGLAKALIRGIDRKGLISPLLYLLAIVLAFFSPWLALILYLLLALLWLIPDRRIERRL
>gnl|CDD|442770 COG3549, HigB, Plasmid maintenance system killer protein [Defense mechanisms]
IKSFKDKGLERFFEGGRTKGIPADIARKLRRKLDMLDAATSLEDLRVPPGNRLEALKGDRKGQYSIRVNG
QWRICFRWEDGDAEDVEIVDYH
>gnl|CDD|442771 COG3550, HipA, Serine/threonine protein kinase HipA, toxin component of the HipAB toxin-antitoxin module [Signal transduction mechanisms]
ARRTLDVYLNGRLVGTLTRDDDGRISFEYDPDWLAPDGFPLSPSLPLREGPYPFPGGGLPGFFADLLPDG
WGRRLLARRLGISSLDPFDLLAAVGRDCVGALRFLPEGEGPEPPPEPEPLSLEELAEALRDLLEGEAPAL
GELLGGRSSLGGAQPKAALLREDGRWALPAGGTPTTHILKFPSGRLPDLVENEYLCLRLARAAGLPVAET
RLLRFGGRPALLVERFDRTADAGRRLHQEDFCQLLGLPPGQKYESPSYEDLARLLRRLSALPAADLEELF
RRMVFNVLIGNTDDHAKNFSFLYDPGGRWRLAPAYDLVPTYPYPRDDKLAMAIGGKKFDDITLRHLLAFA
EAFGLSERAALEIIEEVAEAVPAAWPEVAAELGVPEELLDRIADALRE
>gnl|CDD|442772 COG3551, COG3551, Uncharacterized conserved protein [Function unknown]
MSAASTPKRKALIVLGMHRSGTSLLAGLLQLLGVDLGQDLMPADEDNPKGYFEDRDIVALNDELLAALGS
SWDDPRPFPEEWLAAPALEALRARAAELLAEEFGDAPLWGIKDPRTCLLLPFWLELLPELGVDPRFVLVV
RNPLEVAASLARRDGFPLEKALLLWLRYNLDALRATRGLPRVFVDYDRLLADPRAELARIASALGLPLPE
AALAAAIDAFLDPDLRHHRATGEDLSDPRLPLARELYEALRRL
>gnl|CDD|442773 COG3552, CoxE, Uncharacterized protein CoxE, contains von Willebrand factor type A (vWA) domain [Function unknown]
AANLVGFARALRRAGLPVGPGETLDALRALEVVGLGDREDLYWALRATLVKRPEDLPVFDALFDLFFRAP
GLREKLLALLLPAAPGERARLAEALAAGDGPDEAREEFREELEEDARLTASAVEVLRHRDFAQLSAAELA
EARRLIRRLARRLARRRSRRRRPARRGGRIDLRRTLRASLRTGGEPIRLARRRRRRRPPRLVLLCDVSGS
MSPYARFLLRFLHALARQFSRVEAFVFGTRLTRVTRALRHRDPDRALARASAEVPDWSGGTRIGEALAEF
NRRWARRVLGRRTVVLILSDGLDRGDPELLAEEMARLRRRARRLIWLNPLLRWPGYEPLARGMAAALPHV
DDFLPVHNLASLEALARALAR
>gnl|CDD|442774 COG3553, COG3553, Uncharacterized conserved protein, DUF2218 domain [Function unknown]
MLTSTARVATDNASRYLKQLCKHFAHKVPVEFDETQGRIAFPFGTCTLTADDDALTLRLEAEDAEQLERL
EDVVARHLDRFAFREELTVDWQRA
>gnl|CDD|442775 COG3554, COG3554, Uncharacterized conserved protein [Function unknown]
RTLTWRRLDGPGLEHLRLQRSGDGIRAEGVVIGAADGEPFSLSYRLRCDADWRTRRLDVRGTTAGGERQL
SLERDGDGHWLVDDGAERPELDGCLDVDLSFTPFTNTLPIRRLGLAEGESAEIPVAYVSLPDLTVRPVRQ
RYTRLAPGRYRYESLDGGFTADLTVDEDGLVLDYPGLFRRV
>gnl|CDD|442776 COG3555, LpxO2, Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones]
YRFSGLPTTPFFDRAQFPWLAELEANWPTIRAELLALLAEIEALPPYHDISFDQANIFFDRGWKRFYLYW
YGERHPSNCALCPKTAALLEQIPGVKAAMFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNDDRCRIRVDG
ETYSWREGEAVLFDDTYEHEAWNDTDETRVVLFCDVWRPMLSPWERAVNRLFAAILMRSAFVPNARKNLK
KWNKRLYYLL
>gnl|CDD|442777 COG3556, COG3556, Uncharacterized membrane protein [Function unknown]
MLLDALLAYLHHLAIFVLAAALAAEAALLRPELTAAVVKRLARLDAVYGISALLVLATGLLRVFWGGKGA
DFYLHNPLFHAKVGLFVLVGLLSIYPTLTFLRWRKALRAGAAPVPSPAEVRRVRRLIRIELHLLVLIPLL
AALMARGVG
>gnl|CDD|442778 COG3557, YgaC, Uncharacterized conserved protein associated with RNAses G and E, UPF0374/DUF402 family [Function unknown]
MELPKEGEVVRIQSYKHDGSLHRVWDETVVLKDSEGVLIGANDGTLVTESDGRTWVTREPAICYFPADAW
FNIIFMIRPDGIYYYCNIASPFVWDGEALKYIDYDLDVKVFPDGTYRLLDEDEFEEHRVRMGYPAEIDAI
AEAAVDELLAWIRERKGPFDPEFVDRWLERYLRVKKR
>gnl|CDD|442779 COG3558, COG3558, Uncharacterized conserved protein, nuclear transport factor 2 (NTF2) superfamily [Function unknown]
ETRPPLPPFTRETAIQKVRLAEDAWNSRDPERVALAYTPDSRWRNRAEFLQGREEIVAFLTRKWARELDY
RLIKELWAFDGNRIAVRFAYEWHDDSGQWFRSYGNENWEFDENGLMRRRHASINDLPIAESERKFHWPLG
RRPDDHPGLSELGL
>gnl|CDD|442780 COG3559, NodJ, Putative exporter of oligosaccharides and polyketide antibiotics DrrB/NodJ, ABC-2 family [Intracellular trafficking, secretion, and vesicular transport]
MKSALTGTGTLLRLALRRDRVRLPIWILGLALLVAATAAAFEGLYPTEAERAALAATMANPAMRALFGPG
FGLYTLGGMVAWEMGLFLALLAALMSILLVVRHTRAEEESGRAELLRAGVVGRHAPLTAALLVALGANLL
LGLLTALGLVALGLPAAGSLLFGAALAAAGLVFAGVAAVTAQLTESARAASGLALAVLGVAYLLRAVGDV
SNSWLSWLSPLGWAQQTRPFADNRWWPLLLLLALAAVLLALAFALAARRDLGAGLLPARPGRARASPGLR
SPLGLAWRLQRGSLIGWAIGLAVLGLAYGSLAGSVGDLLEDNPALAELLARLGGGASLVDAFLATLLGIL
AILAAAYAVQAVLRLRAEETSGRAEPLLATAVSRTRWLASHLAVAALGSAVLLLVAGLGLGLGAAAVTGD
PGSLGRLLGAALAQLPAVLVVLGLAVLLFGLLPRLAGLAWLVLAYSFVVGYLGPLLDLPQWVLDLSPFGH
VPQLPAEDFDWAPLLVLTALAAALVALGLAGFRRRDLAG
>gnl|CDD|442781 COG3560, FMR2, Fatty acid repression mutant protein (predicted oxidoreductase) [General function prediction only]
DFLEAIKNRRSIYALGKNLPISDEEIEEIIKEAVKHTPSAFNSQSSRVVVLFGEEHDKLWDITKETLRKI
VPAEAFAPTEEKINSFAAGYGTVLFFEDQDVVKGLQEQFPLYADNFPVWSEQSSGMAQYAVWTALAEEGI
GASLQHYNPLIDEAVAKEWNIPASWKLRAQMPFGSIEAPAGEKEFIPDEERFKVFK
>gnl|CDD|442782 COG3561, COG3561, Phage anti-repressor protein Ant [Mobilome: prophages, transposons]
MNTSPNMNELIPVTIDGNGEQVVSARELHEFLEVKTDFSTWIKRRIEEYGFIEGQDFISFLSKTSNKSRG
GRPSKDYALTLDMAKELAMVERNEKGRQARQYFIECEKKLKSPAPEMARALLQAQQRRLAAALLKKLEQA
EELAQERQLNKALPAVYIAEENAINIILLLGLAKQKIGGRLKLGRLRRLLRLGQLLNLLGLLQTNNTYLI
LDGTQYQTRKGKLNTLQRSTR
>gnl|CDD|442783 COG3562, KpsS, Capsule polysaccharide modification protein KpsS [Cell wall/membrane/envelope biogenesis]
MSATLTALSGRRFLFLQGPHGPFFRRLARALRAAGHRVWRVNFNAGDRLFWRGPGAIDYRGTLDDWPAFL
ADLLRRHGITDIVLFGDCRPYHRAAIAVARALGIRVHVFEEGYLRPDWITLERGGVNGHSRLPRDPDAYR
RAALALPEPPLPPPVGGSFRRRAFYDVLYHLANMFLRPLYPHYRHHRPLHPLAEYLGWLRRLLRKPLYRR
RERAALARLRAGGGPYFLVPLQLEHDSQIRAHSPFASMEEFIEEVLASFARHAPADAHLVIKHHPLDRGL
RNYRRLIRRLARRLGVADRVHYVHGGHLPTLLRHARGVVTVNSTVGLSALWHGLPVKVLGRAVYDIPGLT
SQGPLDEFWAAPQPPDRELFRAFRRYLLETTQVNGGFYSREGRRAAVRQVVDRLLAPEDPYPAPRQQARA
V
>gnl|CDD|442784 COG3563, KpsC, Capsule polysaccharide export protein KpsC/LpsZ [Cell wall/membrane/envelope biogenesis]
MKGRLGVFSGGILRIPRLRRFLGLAGYDLRLGLPGPADAVAGWGRKPSARRARAYAARHGLPLIRLEDGF
LRSLGLGRAGEPPLSLVVDDLGIYYDATRPSRLEQLLATAPLDDAALLARARAAIARIRAARLSKYNHAP
PFLPPPPDPGYVLVVDQTAGDASVRYGGADAASFLEMLAAALAENPGARILVKTHPDVLAGKKQGYLTAA
DADDRVRLLTEDVSPWSLLEGADAVYTVTSQMGFEALLAGKPVRCFGMPFYAGWGLTDDRHPCPRRRRRR
TLAQLFAAAYILYPRYLDPYTGQLCELEDVIDWLAAQRRAWRRDRGGLVAVGFSLWKRAFLKPFLGRPGG
RLRFVRSPKKAARLALASGRKLLVWGSKAPEELELAAQRGAPVLRMEDGFLRSVGLGSDLVPPLSLVLDD
LGIYYDPTRPSDLERLLNTAAFSPAELARAEALRQRLVEAGLSKYNLGGRTPLPRLPAGRRVILVPGQVE
DDASIRLGSPGIRTNLDLLRAVRAANPDAYIIYKPHPDVVAGNRKGAVPEAEALRLADLVVTDADIVSLL
DAVDEVHTMTSLAGFEALLRGKRVVTYGQPFYAGWGLTRDLLPVARRTRRLSLDELVAATLIAYPRYVDP
VTGLPCPPEVAVDRLAEQRAPLPGPLGWLRRLLRKLQGLLASLAH
>gnl|CDD|442785 COG3564, COG3564, Uncharacterized conserved protein, DUF779 family [Function unknown]
MMVERVSATPAALALIRRLKAKHGPLMFHQSGGCCDGSAPMCYPAGEFRVGDSDVLLGEIGGVPFYISRS
QFEYWKHTQLTIDVVPGRGGGFSLEAPEGVRFLTRSRLFTDEELAALEPVPRG
>gnl|CDD|442786 COG3565, COG3565, Predicted dioxygenase of extradiol dioxygenase family [General function prediction only]
MMLPPFHLAFPVTDLDAARRFYGDVLGCEEGRSSDTWVDFDFFGHQLVAHLAPPFAFTAATNPVDGHDVP
VPHFGVVLDWDDWHALAERLKAAGVEFVIEPYIRFEGQPGEQATMFFLDPSGNALEFKAFKDESQVFAK
>gnl|CDD|442787 COG3566, COG3566, Uncharacterized conserved protein, DUF2213 domain [Function unknown]
MKVLAFDRAELGSVRSETAEGYLLVVDAPIARAGVQPYYGREIPGWEKDPDRVIRVYRPPEELFSAETLA
SFNGKPVTLDHPPEFVTADNWKELAVGTVGNDARFEGDYLVADLTIKDAEAIAAIEDGKRELSCGYDADY
DMTPGTPDGQPYDGVQRNIRGNHVALVDKGRAGPDCRIGDSDPAGAKKMQAGGMKMLKILLDGFKYEVAD
EVAEALEALEAQLDDAEAKAADAEAEIGDAAGDLEAELDALDEEIEKLEAELDEAEKKAMTAAKLDAAIA
ARAALVADAKALGPGVDFTGKSDRAIKRAVIKAAGGDFDVDDKSDAYIDAAFDAAVEDAKAKNLGSAAAN
DLATKAAAANAAKVNRLNMK
>gnl|CDD|442788 COG3567, COG3567, Uncharacterized conserved protein, DUF1073 domain [Function unknown]
MSKKPSAKRAATADGRENFLAGLGVGTARDSLAGQYGYPFVSLPRYQLEAAYRSNWIARKIVDIPAEDMT
RKWIEIKGDEDDKKKKKIEAAEERLKLWDKLKDALKRARLYGGAAILIGIKDGQDLSQPLDVEKIGKGGL
KGLIVLDRWQLTPGEYNRIDPLSPDYGKPEFYYVNGTTQGDQRVHPSRVIRFDGAPLPDELKSAENFWGI
SLLEALYDDLLDADSTSGGVAQLIYKAALRVLKTPDLREALAMGGTEELLKRLDLINQMKSNEGLALLDK
EEEFEVKSYSFAGLDDLLRQFAEQLSGAADIPLTRLFGQSPGGLNATGDGDLRNYYDRIAARQEGRLRPP
LTRLLEILQRSALGEIPPDITFEFNPLWQMSEKEKAEIAKTTADADAIYLDAGVITPDEVREALRNEPVS
TGYSGISDEDLEEAEDDPLTEGEPEEDKIGAAV
>gnl|CDD|442789 COG3568, ElsH, Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only]
AAAAAATLRVMTYNIRYGLGTDGRADLERIARVIRALDPDVVALQENAILSRYPIVSSGTFDLPDPGGEP
RGALWADVDVPGKPLRVVNTHLDLRSAAARRRQARALAELLAELPAGAPVILAGDFNDIDYILVSPGLRV
LSAEVLDSPLGRAASDHLPVVADLELP
>gnl|CDD|442790 COG3569, Top1, DNA topoisomerase IB [Replication, recombination and repair]
MKAEAARAAGLRYVDDSEPGITRRRRGKGFSYRDPDGRPVTDAATLARIRALAIPPAWTDVWICPDPNGH
LQATGRDAAGRKQYRYHPDWREVRDETKFDRLLAFGRALPRIRRRVARDLRRRGLPREKVLAAVVRLLDR
TLIRVGNEEYARENGSYGLTTLRKRHVKVDGDTVRFRFRGKSGKEHEVTLRDRRLARLVRRLQDLPGQEL
FQYRDEDGERHPVDSGDVNAYLREITGEDFTAKDFRTWAGTVLAAEALAEAGPAESERARKKNVVAAVDA
VAERLGNTPAVCRKSYVHPRVLAAYEDGRLIAYLRRRAARERDRRGLSRAERALLALLERAARRA
>gnl|CDD|442791 COG3570, StrB, Streptomycin 6-kinase [Defense mechanisms]
MSIDIPDALARRIRRGEAGRAWLAALPALLEELLDRWGLTPDGPPAHGSSSLVLPVRRADGTPAVLKLSP
PDEEAAREARALRWWDGRGAVRLLAADPDRGALLLERLDPGRSLADLPRRDDEATRILADLLRRLHVPAP
PGLPPLADWFARLFAAAPARWRLADPVPRRLLARAAALARELLASPAEDVLLHGDLHHGNVLAAGRRGWL
AIDPKGLIGDPAFDLANLLRNPLDELPLATDPARLRRRVDLLAEAAGLDRDRLLAWALARAVLSALWALE
DGEAEDAERALAVAEALAALL
>gnl|CDD|442792 COG3571, COG3571, Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]
MTEGPEDPRATLLLAHGAGAGMDSPFMVALAEALAAAGIAVARFEFPYMVAGRRPPDRAPVLDAAWRAVI
AALRARLAGLPLVIGGKSMGGRVASMLAAEGGGAAGLVCLGYPFHPPGKPEKLRTEHLADLTVPTLIVQG
ERDPFGTPEEVAGYPLPPAIELVWLPGGDHDLKPRKRSGRTQEDHLAAAADAVAAWLARLLR
>gnl|CDD|442793 COG3572, Gsh2, Gamma-glutamylcysteine synthetase [Coenzyme transport and metabolism]
MSRDSSDSTPIESRDQLVAYFAAGEKPREDWRIGTEHEKFGFRKDDLKPVPYEGPRGIEALLEGLQERFG
WEPIYEGGNLIGLKRDGASISLEPGGQFELSGAPLETIHETCAELNQHLAEVREIAEPLGIGFLGLGFQP
KWTRADIPWMPKGRYKIMREYMPKVGTLGLDMMLRTCTVQVNLDFSSEADMVRKMRVSLALQPLATALFA
NSPFTEGKPNGFLSYRSHIWTDTDPDRTGMLPFVFEDGFGFERYVDYALDVPMYFVKRDGKYIDAAGQSF
RDFLAGKLPGLPGERPTLGDWADHLSTLFPEVRLKRFLEMRGADGGPWARLCALPALWVGLLYDEGALDA
AWDLVKDWTAEEREALRDEVPRLGLKAPFRGRTLRDLAREVLAIARAGLKRRARLNGNGRDETIFLAPLE
EIVESGRTPAEELLELYHGAWNGDVDPVFEEYAY
>gnl|CDD|442794 COG3573, COG3573, Predicted oxidoreductase [General function prediction only]
MAAMDADVIVVGAGLAGLVAAAELADAGRRVLLLDQEPEANLGGQAFWSFGGLFLVDSPEQRRLGIKDSP
ELALQDWLGSAGFDRPEDHWPRRWAEAYVEFAAGEKRAWLHALGVRFFPVVGWAERGGYLAGGHGNSVPR
FHITWGTGPGVVEPFIRRVRAAAAAGRVTFRFRHRVDELIVEDGAVTGVRGEVLAPSDAERGAASSRDVV
GEFELRAQAVIVASGGIGGNHELVRRNWPARLGPPPKTMLSGVPAHVDGRMLDIAEAAGARLINRDRMWH
YTEGIPNWDPIWPGHGIRILPGPSSLWLDATGRRLPAPLFPGFDTLGTLEHIRATGYDYSWFVLNQKIIE
KEFALSGSEQNPDLTGKDLRLVLKRLLKGAPGPVEAFKDHGEDFVVADTLEELVAGMNALTGEPLLDAAT
LRRQIEARDRQIDNPFSKDAQIRAIRNARRYRGDRLIRTAKPHRLLDPKAGPLIAVRLNILTRKTLGGLQ
TDLDSRVLDADGQPIPGLYAAGEAAGFGGGGVHGYRALEGTFLGGCIFSGRAAGRAIAAAL
>gnl|CDD|442795 COG3575, COG3575, Uncharacterized conserved protein [Function unknown]
EQEQRLLAIILADPLRMAILRRVRALGLPDWWLGAGFVRNTVWNVLHGRPPRTGIKDIDVIYFDPSDLSY
EAEDALEARLRALFPDVPWEVKNQARMHLWYEEYAPYTSSEDAISRWPETATAVGVRLDADGQLELYAPF
GLDDLFAGRVRPNPLFPNREIYEQRVKRWLERWPELRVVP
>gnl|CDD|442796 COG3576, COG3576, Predicted flavin-nucleotide-binding protein, pyridoxine 5'-phosphate oxidase superfamily [General function prediction only]
MAITPAVALQELYGSPAARALRKVLDRLTPHERAFIAASPFFFLATVDADGWPDVSPRGGPPGFVRVLDD
RTLAFPDRRGNRRYDSLGNILENPRVGLLFLDPGRRERLRVNGRARIVTDPALLARLAVEGKRPERVIVV
TVEEVYFNCPKAITRSGLWDPEAWVPRAALPSPGEILAAALAPDVDAEA
>gnl|CDD|442797 COG3577, COG3577, Predicted aspartyl protease [General function prediction only]
LLALLGLFFGGRGVRAQLNPGQAPVSTGGGEVVLKRDRDGHFVVEGTINGQPVRFLVDTGASTVVLSESD
ARRLGLDPEDLGRPVRVQTANGVVRAARVRLDSVRIGGITLRNVRAVVLPGGELDDGLLGMSFLGRLDFE
IDGDRLTLRPRY
>gnl|CDD|442798 COG3579, PepC, Aminopeptidase C [Amino acid transport and metabolism]
AKEITPDLLAKFQEDFAADPANRVAQNAVAQNGINKAALNREVAAGYDFTFSIELKTGPVTNQKSSGRCW
MFAALNFLRSELIKKGKLKDFELSQNYTFFWDKLEKANYFLENIIATADEPLDDRLVQFLLSTPFGDGGQ
WDMVVNLIKKYGVVPKSVMPETNYSSNTAEMNAVLNKKLRKDAKELRELVAAGASEKELSARKEEWLKEV
YRILDIYLGEPPEKFDYEYKDKDGKFHRDGEYTPQEFAKKYVGLDLDDYVSLINAPTADHPYYKTYTVEY
LDNVVGGRPVKYLNVPIEELKEAAIAALKDGEPVWFGCDVGEQGFRKNGIADVPLYDYEELFGVDFAMDK
AERLDYGESTDTHAMVITGVDLDQNGKPTRWKVENSWGDDNGYKGYFYMSDAWFDEYTYEVVVHKKYLPK
EILKKLDQEPIVLPPWDPMG
>gnl|CDD|442799 COG3580, COG3580, Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function prediction only]
LFDYKPLPPEKAMRGTIGIPRALNYYEYYPFWKTFFTELGFEVVLSPPTNKEIYEKGIEIASDEACYPAK
LAHGHVADLLDKGVDYIFYPRIVSEPKEDEGADNHYNCPKVQGYPEVIKANIDEEEKGIPFISPFLNLDD
KELLAKRLYEELGKGLGISKKEIKRAVEKAWEAQRAFRRDLRKKGEEILEELKENGEKGIVLLGRPYHIY
DPEINHGIPELLRSLGVAVLTEDSLPHLGEDLSARPLRKNLQWTYHSRLLGAAKFVARHPNLDGIQLTSF
GCGPDSVTTDLVEEILERSGKPYLLLKIDEHSNEGGVKTRLEAFLDALKERKKKEAKALEFTK
>gnl|CDD|442800 COG3581, COG3581, Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function prediction only]
KKTMTILFPHMGPIHFRLLKAAFRGLGYEVEVLPPPDKETLELGLKYVNNDACYPLKIVLGQLIEALESG
KYDPDATAIVMTGTGGPCRAGNYIELLRKALKDAGYPDVPVISLNPQGLEFNPGFKLTLKLLKRAWKAIV
YGDLLEKLLYRTRPYEKNKGSADRLYEKWLEKLEEALESGSLKELKKLLKEIVKEFDAIPLDEDEKKPRV
GIVGEIYVKLEPFANNNIEKFLEEEGAEVVRPPLSDWILYNLYNRKFKAKELGGSKKSRLKKKLAIKVLE
KYRKPIKKALRKSLRFEPPPDIKELAEAAKPYLSLGNIGGEGWLLIGEMVELIKEGYDGIICLQPFGCMP
NIVAKGILKKLRRDYPEIPILTLDYDEGASEVNQLTRLEAFLDLAKRRREKKEEEAL
>gnl|CDD|442801 COG3582, CUZ1, CDC48-associated ubiquitin-like protein CUZ1, contains AN1-type Zn-finger (protection from As/Sb toxicity) [Defense mechanisms]
MAKCDICGKEENLPYQCRYCGGTFCSEHRLPENHDCPGLDDWNDPKGVFDSGFDDSVSGKGSGRSGIKTI
KTLLSTVLLTGLLAFLGGLLGSNLLTISVLFLAIIWITSFVLFGALGFLAQLFVSVFFFRFEITTVIVLF
VSVLFFLLLGFVGLAGNFGGLVFLLVFGGVLLGVLASAGALGALGLLLTLALLLLKLLLAGVAPFLVGAA
AAIAAGAGVVVGLVIAGGIGLGFLLFLAAALALLGIGYIVGGGVGLGGGGGGGGGGGLGGGGGGGGGGG
>gnl|CDD|442802 COG3583, YabE, Uncharacterized conserved protein YabE, contains G5 and tandem DUF348 domains [Function unknown]
ALRRRRKLLLAAVAAVLVTLAGGGGAYAAAKKTVTLDVDGEERTVTTFAGTVGEVLEEAGITVGEHDVVS
PALDTPLTDGDTGELTITVKRAKPVTVVVDGKTRTVTTTATTVGEALAEAGITLGEDDRVSPALDAPLTD
GMTITVTRVTTKTVTEEEPIPFETVRKEDPSLPKGETKVVQEGVPGVKEVTYRVTYENGKEVSREVVSEK
VTKEPVDEVVAVGTKPRPAPAPVPAGSGSGGGGSSTGSGGYGGLAASSATTAASGGGTGAPGGGGAARPT
AGAVAGVVVVGGGGGGGPGGGGGGGAAAGGGGGGGGGGAIDGAEGGSSAAAGGGR
>gnl|CDD|442803 COG3584, COG3584, 3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]. 3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases is part of the Pathway/BioSystem: 3D
TVTATAYTAGPECTGKGGGITASGTRLRPGGVIAVDPDVIPLGTKVYIEGYGYAVAEDTGGAIKGNRIDI
YMPSVSEALNWGRRTVTVYILE
>gnl|CDD|442804 COG3585, MopI, Molybdopterin-binding protein MopI [Coenzyme transport and metabolism]
MTSSRNNQFGGVVSIIAGGVVNEVVLLLLGGGTIIAAITTASSAELLGLVGGKEVAALKKASVVILATDD
AMKLSARNQLKGTVTRIERGAVNSEVVLDLGGGTTLTAVITNESVEELGLKEGDEVTALFKASSVILAVD
A
>gnl|CDD|442805 COG3586, COG3586, Uncharacterized protein domain, C-terminal to COG1479 DNAse/DNA nickase [General function prediction only]
LNIFFAKKSLKKDKNDLLLKSIKELLLLLLKRELKLDEERLLLLFGLLLVGSRFSLYLLRIDTLANDEEI
GTEVIIEYKRDINNSVILQGWKYLLLLLWNKADFLLLYNENLLLLLKRNDVSDSQSRVDFSSPSGGGIQK
EAINFKDLAIELWEEIREINRTRSLLLLAKVVSAASTKPVVSEAGEIAAVVKEIKVYTEDEHLELASEEL
RELYEALREYILALGDDVEEKPLKLYIAYKRSKNFVDIVPQKKRLKLYLNLDPDELEDPKGFTRDVSNIG
HWGTGDVEVTLKSDEDLEYAKPLIKQAYEKQMG
>gnl|CDD|442806 COG3587, PM0699, Restriction endonuclease, type III RM system [Defense mechanisms]
MKLKFKPQDYQTDAVEAVVDLFAGQPKCRSNFTVDPGREQGQLGLEEDELGFGNRLQLTDDQLLENIQKV
QLRNGLPPSESLEKGGYNFTVEMETGTGKTYVYIRTIFELNKRYGWSKFIIVVPSIAIREGVYKSLQITE
EHFKELYGKKPARYFIYDSKKLGQVRNFASSSGIQVMIINIQAFNKSGKDANRIYRELDDFGGRRPIDVI
AATRPIVIIDEPQSVDGKKTKEALASFNPLFTLRYSATHKDKHNLVYRLDAVDAYNKKLVKKIEVAGITV
KGAGNDAYLYLESIENSKKPPTARIELDVKTKSGSVKRKTRTVKKGDDLYELSGGREQYKGYIVSEIDAE
KGNEYIEFTNGEVLRLGEAIGDVDEDALRRIQIRETIKEHLDKELRLFPKGIKVLSLFFIDEVAKYRDYD
EDGNPVKGEYARIFEEEYKKLINEPKYQTYLKDIEIDVEKVHNGYFSIDKKGRLKDTKVKRRGETSDDED
AYDLIMKDKERLLSFDEPLRFIFSHSALREGWDNPNVFQICTLKESDSEIKKRQEIGRGLRLCVNQNGER
MDGFADINVLTVIASESYEDFAEGLQKEIEEDLGIRFGKAEEHYFAGKVVTDEDGEEVPLGEEEAKAIYK
YLVKNGYIDDKGKITDKLKEALKDGTLALPEELEPYAEQIIALLKSVAGKLEIKNARKRKVVKLNKANFL
KKEFQELWNRINHKTTYRVDFDSEELIKKCIKALDKNLRVSKLRYTVTKGEQDIGKAGVKAEESETETVD
VDENSQVLPDLLGKLQDETNLTRKTIVEILKGISGRFADFKNNPEEFIEKASRLINEQKATLIVDGIKYD
KLGDRYDQEIFTEEELTGYLSKNAVKAKKSVYDYVVYDSDVERKFAEDLDTSEEVKVYAKLPRGFKIPTP
VGNYNPDWAILFEEDGVKHLYFVAETKGSMSSLDLREIEKAKIECARKHFKALSNDDVKYDVVDSYEELL
EIV
>gnl|CDD|442807 COG3588, Fba1, Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]. Fructose-bisphosphate aldolase class 1 is part of the Pathway/BioSystem: Glycolysis
NTEELNATALAMVANGKGFLAALDQSGGSTPKALAAYGVEETEYSRREEMFDLVHAMRERIITSPAFTGD
KISGAILFEETMDQKIDGTPTFDYLWEKKGIVPGIKVDKGLKDLAPGVQLMKGLDGLDERLARAKELGAF
GTKWRSVIKIANAAGIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALP
EDEGVMLKMVIPGKDNLYQALVEHPAVPRVVFLSGGQSREEATAHLNANNGLIASFSRALQEGLLAAWSG
EEFNAALAQAIDGIYDASIEKA
>gnl|CDD|442808 COG3589, COG3589, Uncharacterized conserved protein, DUF871 domain [Function unknown]
LGISIYPGHSTLEEDKAYIELAAKYGFTRIFTSLLIPEDDKEKILERFKELIAYAKKLGMEVIADVSPAV
FEQLGISYDDLSFFKELGITGLRLDYGFTGAEEALMSHNPYGLKIELNASTITEYLDNIMSYGANKDNLE
GCHNFYPRPYTGLSRDFFLKCNKWFKKYGIRTAAFVPSQGATRGPWPLYEGLPTLEEHRNLPPLVQAKHL
FATGLIDDVIIGNAYASEEELKALSALNRDVIELKVELEEDISEVEKEILLEEVHTNRGDAAEYVIRSTE
SRVKYKDETIPPHNTVERKRGDITIDNELYGRYKGELQIALKDLPNDGKVNVVGRIIEEELFLLDYIKPW
QKFRFK
>gnl|CDD|442809 COG3590, PepO, Predicted metalloendopeptidase [Posttranslational modification, protein turnover, chaperones]
MKKLLLLLALLLALAACAAAAAAGTSGIDLANMDTSVRPGDDFYRYVNGGWLKTTPIPADRSRWGSFNEL
RERNEARLRAILEEAAAAPAAAGSDEQKIGDLYASFMDEAAIEALGLAPLKPDLARIDAIKDKADLAALL
AALHRAGVGGLFGFGVDADLKNSTRYIAYLGQGGLGLPDRDYYLKDDEKSAEIRAAYVAHVAKMLELAGY
DEADAAAAAEAVLALETALAKAHWSRVELRDPEKTYNPMTVAELAKLAPGFDWDAYLKALGLPAVDEVIV
GQPSFFKALDKLLASTPLEDWKAYLRWHLLDSAAPYLSKAFVDANFDFYGKTLSGQKEQRPRWKRAVALV
NGALGEALGQLYVERYFPPEAKARMEELVANLRAAYRERIENLDWMSPETKAKALEKLAAFTPKIGYPDK
WRDYSGLEIKRDDLVGNVLRASAFEYQRELAKLGKPVDRTEWGMTPQTVNAYYNPTMNEIVFPAAILQPP
FFDPKADDAVNYGGIGAVIGHEITHGFDDQGSQFDGDGNLRNWWTPEDRAAFEARTKKLVAQYDAYEPLP
GLHVNGKLTLGENIADLGGLSIAYDAYKLSLKGKEAPVIDGFTGDQRFFLGWAQVWRSKARDEALRQRLA
TDPHSPGEFRVNGPVRNLDAFYEAFDVKPGDKMYLAPEDRVRIW
>gnl|CDD|442810 COG3591, eMpr, V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones]
AVGRLETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGTATATRFRVPPGWVA
SGDAGYDYALLRLDEPLGDTTGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLSLDCSGRVTGVQGNRLSYD
CDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADRANTGVRLTSAIVAALRAWASA
>gnl|CDD|442811 COG3592, YjdI, Uncharacterized Fe-S cluster protein YjdI [Function unknown]
MKEKIKEYSGEEITVVWDPELCIHSGNCVKGLPEVFDPKRKPWINPDNASTEEIIEQIDRCPSGALSYRR
N
>gnl|CDD|442812 COG3593, YbjD, Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair]
MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPE
IEIELTFGSLLSRLLRLLLKEEDKEELEEALEELNEELKEALKALNELLSEYLKELLDGLDLELELSLDE
LEDLLKSLSLRIEDGKELPLDRLGSGFQRLILLALLSALAELKRAPANPILLIEEPEAHLHPQAQRRLLK
LLKELSEKPNQVIITTHSPHLLSEVPLENIRRLRRDSGGTTSTKLIDLDDEDLRKLLRYLGVTRSELLFA
RKVILVEGDTEVILLPALARKLGKDLDEEGISIIPVGGKSNLKPLAKLLKALGIPVAVLTDGDEAGKAET
IEKLKEKGE
>gnl|CDD|442813 COG3594, NolL, Fucose 4-O-acetylase or related acetyltransferase [Carbohydrate transport and metabolism]
MTSAKKRDPWIDNAKGILIILVVLGHAIGPLIGDGDWLRALYLFIYSFHMPLFFFISGYFSKPSRNGFKK
FLKKKFKRLLVPYLIFQLIYSLFKFLVEGGEPLDLSLLLLLLDPNGALWFLPALFVWRLLLPLLRRLRRW
PLLIALAIGLLAGYLPSIGLPLSLDRTLVFLPFFLLGYLLRKYHLERLRRLRVLLLAVAVFLAAALLGFN
RYLLLGSRSYGNWYGPLLRLLVALLGILLVLALLALLPRRRTWLTYLGRNTLYIYLLHGF
>gnl|CDD|442814 COG3595, YvlB, Uncharacterized conserved protein YvlB, contains DUF4097 and DUF4098 domains [Function unknown]
EEALSAEIAAAVSVIAVVAGSIVVGLKTSRGSVDASSGGSVRRTVALGVDTGAALGGVDGVGGNGLAGAS
YLRVTSSGDVRVSGVDDVSVKTSSGDVTVEDLSGDLTVKTVSGDIELSGLTGDEVELETVSGDITVKDGV
GGDVEAKTVSGDITVDGASGSVEAKTVSGDIRLTLEGAVAGRVKLKTVSGDVEVGLPEGTGADLDLSTVS
GDIRVDLPDVEVGKDGKRFSGTIGDGTVTIRAETSSGDIVIRRA
>gnl|CDD|442815 COG3596, YeeP, Predicted GTPase [General function prediction only]
MSTEVSSLTERLEALKRLPQVLRELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVG
RPCTREIQRYRLESDGLPGLVLLDTPGLGEVNERDREYRELRELLPEADLILWVVKADDRALATDEEFLQ
ALRAQYPDPPVLVVLTQVDRLEPEREWDPPYNWPSPPKEQNIRRALEAIAEQLGVPIDRVIPVSAAEDRT
GYGLEELVDALAEALPEAKRSRLARLLRAKAIDRYTLLAAAAALLAAALLALLALLLAALAAAPVALAGL
GPAALKTALVASLAELALRAAAGAAAAAAELSATASAS
>gnl|CDD|442816 COG3597, COG3597, Uncharacterized conserved protein, DUF697 family [Function unknown]
ARGLLLVVVGGLGSAGKTSLVGALLLTVGGLVGTGMGTTTAAETYALKLVLLVLLLLLTDTGGILEAGAA
GTLAELLALLLAVEADLLLVVDDDDLRASELEILRALVLIGKKSLLLLVKLDLLEEALQEALLALLVLRE
VVEIAAAAVAAAVAALQADALVAEELFEPEADIDLLLKRLAAALLAEGLLLLAAAILLAAQLLLEEAAAA
AAGQRRRAAARRIILRYAIAAAAVGAVPIPFADLLALAALQAKMVAELAKIYGVELSRERAKELLASLGG
GLGGLGLVRQLLRSLLKLIPGAGTVVGGAIQAATAAALTYALGRVAIEYFEKGGTFDPEGLKEVFKEAFQ
KAKRFLKEFKQEAKARA
>gnl|CDD|442817 COG3598, RepA, RecA-family ATPase [Replication, recombination and repair]
PRRWLVPGLLPEGGVTLLAGPPGTGKSFLALQLAAAVAAGGPWLGRRVPPGKVLYLAAEDDRGELRRRLK
ALGADLGLPFADLDGRLRLLSLAGDLDDTDDLEALERAIEEEGPDLVVIDPLARVFGGDENDAEEMRAFL
NPLDRLAERTGAAVLLVHHTGKGGAGKDSGDRARGSSALRGAARSVLVLSREKGEDLRVLTRAKSNYGPE
IALRWDNGGRLALEEVAALTAGAGEVELKELVGGVARTGTDSELEEGLLEVPLAEAESAGEDAELAAKAV
ADEKDAARAVARLKAGGGKSKKVREGRLAAGRE
>gnl|CDD|442818 COG3599, DivIVA, Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning]
MKLTPLDIRNKEFKKGFRGYDEDEVDEFLDEVAEDYERLIRENKELKEKLEELEEELEEYRELEETLQKT
LVVAQETAEEVKENAEKEAELIIKEAELEAEKIIEEAQEKARKIVREIEELKRQR
>gnl|CDD|442819 COG3600, GepA, Uncharacterized phage-associated protein, contains DUF4065 domain [Mobilome: prophages, transposons]
MSISALDVANYFLSKANEDGGSLTPLKLQKLLYYAQGWHLALYGRPLFDEDFEAWKYGPVVPELYDEYKD
FGSNPIPEPKEFDDSELSEEEKEILDEVWEKYGKYSAWELSELTHSESPWKKARKGLGAEGSNNVISDED
IKEYFK
>gnl|CDD|442820 COG3601, FmnP, Riboflavin transporter FmnP [Coenzyme transport and metabolism]
SKTRKLVTIALLSALSFVLMFIEFPLIPAPPFLKYDFSDVPALIGGFAFGPVAGIIVELIKNLLHLLTTG
SGTGPIGELMNFLAGLSFVLPAAYIYKKKKTRKGAILGLVVGTVVMTIVMVLLNYFVILPLYAKFLGFPL
EAVDLLTLILPAILPFNLIKGVINSVVTLLVYKRLSPILK
>gnl|CDD|442821 COG3602, ACT-3, ACT domain, ACT-3 family [Signal transduction mechanisms]
MSGETDLDELLASMTPVLNPGEYVFCTLPADQLPALELEPLATFREAEGLTLVLPRETADAAGLPYSFPF
RWITLTVHSSLEAVGLTAAVATALAEAGISCNVVAAYYHDHIFVPEDDAEQALAVLEALSAAAKA
>gnl|CDD|442822 COG3603, ACT-7, ACT domain, ACT-7 family [Signal transduction mechanisms]
KLTLKLLPGEYAVCRLPPDAPIPAWALGSGFVSITRTPDELSIVCPEERVPAGVRAERGWRALKVEGPLD
FSLTGILASLSSPLAEAGISIFAVSTFDTDYLLVKEADLDRAVAALRAAG
>gnl|CDD|442823 COG3604, FhlA, FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms]
ALLALRLLGLPLLLLLALALLLLVLLLLALLLRGDLLASALVLEESLELLALALSEALLAAQARQAALAA
RERQLFLGVPLRVGGEVLGVLTLDSRRPGAFSEEDLRLLETLASLAAVAILGETGTGKELVANAIHELSP
RADKPFVKVNCAALPESLLESLQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVF
PIRLPPLRERREDIPLLAEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGG
VLDADDLAPGSREALEEVEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGIK
>gnl|CDD|442824 COG3605, PtsP, Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms]
EMLKALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRATEGLNPEAVGKVRLP
LGEGLVGLVAERGEPLNLADAASHPRFKYFPETGEEGFRSFLGVPIIRRGRVLGVLVVQSREPREFTEEE
VEFLVTLAAQLAEAIANAELLGELRAALAELSLAREEEREAAVEAAIL
>gnl|CDD|442825 COG3607, COG3607, Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only]
MPRIIFVNLPVADLERSRAFYEALGFTFNPQFSDEGAACFVLGEGIVLMLLPREKFATFTGKPIADATGF
TEVLLALNVESREEVDALVAKALAAGGTVLKPPQDVGGMYSGYFADPDGHLWEVAW
>gnl|CDD|442826 COG3608, COG3608, Predicted deacylase [General function prediction only]
RLPLSRLASGTPVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELRGTVILVPVANP
PGFLQGSRYLPIDGRDLNRSFPGDADGSLAERIAHALFEEILPDADYVIDLHSGGIARDNLPHVRAGPGD
EELRALARAFGAPVILDSPEGGDGSLREAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGML
DGEAPPPPLAPPVLARGSEWVRAPAGGLFEPLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGR
RTNPLVNPGDALFHIA
>gnl|CDD|442827 COG3609, ParD, Transcriptional regulator, contains Arc/MetJ-type RHH (ribbon-helix-helix) DNA-binding domain [Transcription]
ETMSISLPDELEDFIDEQVESGRYASASEVIREALRLLEEREAKLEALRAALDEGLASGEAEPFADDVLA
ELRARAR
>gnl|CDD|442828 COG3610, YjjB, Uncharacterized membrane protein YjjB, DUF3815 family [Function unknown]
DLLLPLLLQLLAAFVAAVGFAVLFNAPRRALLWAGLGGALGWLVYLLLLDLGLGPVLATFVAALVVGLLA
ELLARRLKAPATVFTVPGIIPLVPGSGAYRAMYALVEGDYLAALSNGLEALLIAGALAAGLLLGSLLARP
RRRKRRLKRR
>gnl|CDD|442829 COG3611, DnaB2, Replication initiation and membrane attachment protein DnaB [Replication, recombination and repair]
MNQHWKELLPKDGYVVRLSGPLSDEDRKVLTLLYQPLIGAEAYSLYMTLWSELESNSEQSEEQTHYDLMN
LLNLSLPEIYQARKKLEAIGLLKTYKKEDEEGRQYIYELLPPLSPDQFFNDPLLSVLLYNKVGEERYQQL
KERFSKQKLDLEGYEEVTASFTDVFQSVSPSESQLVLEDGSSLKKEEKSKGPVLDDDSFDFELLFQLLSN
RMIPKKILTKEVKELILKLAFLYGIDELDMAKLILWAIDEDGQIDIEELRKAARDFYQREHGQQLPQLVE
KTEPQTKRATKGPSTKEEQLIKLLEEISPIQFLEDLSNGGEPTSQDLKLIEELMEQQGLPPGVINVLIYY
VLLKTDMKLPKNYVEKIASHWARKGVKTAEEAMEYAKQEHKKYQEWQKKKQNKGKRRPVRKEKLPDWLKE
EKKEEEQKKKSDKEESEEEREELLERLKKLRNKKK
>gnl|CDD|442830 COG3612, COG3612, Predicted DNA-binding protein AF1194, contains HTH domain, DUF2240 family [Function unknown]
MMSLRVAVAAPFRQKGKDSLTEKEFVFALSLDRKWMSPDQAKRLIDVAVEEGLLSREDGYLVPAFDPSEV
EVPEGFKPDESILRERSPFERLLDAIVASAGIEKQEAVAEINELQEELGGVTIEAAALLYAREEGVDVSD
LADKVREELLKKG
>gnl|CDD|442831 COG3613, RCL, Nucleoside 2-deoxyribosyltransferase [Nucleotide transport and metabolism]
LAGPLFSPDERERNERLKALLREHGFEVFSPQDDQAEEEGLAAEETAEAIFQADLAAIRRADLVVANLDG
AEPDSGTAFEIGYAYALGKPVIGYTTDDRPLGERGLPDNLMLAGSILAVRLVTTDFEDLLAALAEALAAR
LY
>gnl|CDD|442832 COG3614, CHASE1, Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms]
MSRSRSLLRRRLLPLLVLLLGLLLTALAWWAVRRAEEQRARARFERLADELASALEERLDAYEQVLRGLA
GLFAASDDVTRAEFRRYVASLDLLRRYPGIQGLGWAPRVPAAERAAFEAAARAEGFPDFRIRPAGERDEY
FPITYIEPLDARNRRALGFDMASEPVRRAAMERARDTGRPAASGPVTLVQETDGQPGFLLYLPVYRGGAP
PDTVAERRAALRGFVYAPFRMDDLLAGVLGRLADRDLDLRLYDGTDPGPPQLLYDSSPAAPAAAAPALSA
TRTLEVAGRTWTLEFRPTPAFEAALRSWLPWLVLLGGLLLSLLLALLLLSLARRRRRAEALAAARAALRA
LRAAELRLRALLRRALLALLRNALALALLLAALLLLLARLLLLLAALLLLLARALSAADLLLLQADLLLL
RLLLLLRRRLLLVRDLRLGRGLGLGVVLLLDAILLDLLALAELELAAARAEVALAEALLALLVVLLLALL
LALLRLLLALAELAATAAREAAGAALLLDREAALLDAALEALLDLLGLLVLLLLAELLLRLGALLLGRAL
LGGVGAGEGLVIIAELAALELELLRLEA
>gnl|CDD|442833 COG3615, TehB, Tellurite resistance protein TehB, SAM-dependent methylase, cupin superfamily [Inorganic ion transport and metabolism]
MLRLPENLICYKRTPVFTKDTLPAALLEKHNTKAGVWGKLTVLEGELRYRGLDEDGEEPEEEVVLAAGQP
GVIPPQQWHRVEPLSDDVEFQLEFYCAPEDYFEK
>gnl|CDD|442834 COG3616, Dsd1, D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]
DNLADLDTPALVLDLDALERNIARMAARAAAHGVRLRPHGKTHKSPELARRQLAAGAWGITVATLAEAEV
LAAAGVDDILLAYPLVGPAKLARLAALARAGARLTVLVDSVEQAEALAAAAAAAGRPLRVLVELDVGGGR
TGVRPPEAALALARAIAASPGLRLAGLMTYEGHIYGADDAEERRAAAREELARLAAAAEALRAAGLPCPI
VSGGGTPTFDFVADLPGVTELRPGSYVFHDAGYYRYGVCFPFDPALSVLATVVSRPEPGRAILDAGSKAL
SGDRGDDGLPVPLDLPGARVEGLSEEHGVLRLPAAADLRVGDRVRFIPNHACPTVNLHDELYVVDGGRVV
DVWPTAA
>gnl|CDD|442835 COG3617, COG3617, Prophage antirepressor [Mobilome: prophages, transposons]
MNNLITVFNFEGHEVRTVEIDGEPWFVAKDVARALGYSNPSDALKHLDDDEKTKLELDTPGGPQEMLFIS
ESGLYRLILRSRKPEAKRFKRWVTDEVLPSIRKTGS
>gnl|CDD|442836 COG3618, COG3618, Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only]
GIIDAHHHVWDPDRGRYPWLPDRSYPPRDATPEDYLALLDALGVDRAVLVQASFYGADNRYLLDAAARHP
DRLRGVAWVDLDAPDAAAELARLAAAGVRGVRFNLQGEPDGWLLDPAFRRGLARLAELGLHFDLLVDPRQ
LPALAPLLARLPDLPVVIDHLGKPDIAAGDDPWFAALLALAARPNVWVKLSGLYRESDAGWPYADLRPYA
RALLEAFGPDRLMWGSDWPVTLLAPDYGELLDLLEELLPDLSEAERRAILGDNAARLYGLAA
>gnl|CDD|442837 COG3619, YoaK, Uncharacterized membrane protein YoaK, UPF0700 family [Function unknown]
MKRKKGRERTPRENLRLALLLAFVAGFVDAVGFLALGGVFTSHMTGNVVLLGIALAGGDWAGALLALLAI
LAFVLGAALSGLLIRRARRRLRRWYALLLLLEAVLLLLAGLLGLSLPDLLAVLLLAFAMGLQNATFTKIS
GAVVRTTHVTGNLTDLGIELGRLLRGKRREARADRRKLLLYLLLILAFLLGAVLGALLFLRLGFAALLLP
AALLLALALLYLLRDRRR
>gnl|CDD|442838 COG3620, AF2118, Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription]
VRDLMSRDVVTVSPDDTLGEALRLMRKELGLSQLPVAELVGVSQSDILRIESGKRDPTVSTLEKIAEALG
KELSAVLVVDDGKLVGIITRRDLLK
>gnl|CDD|442839 COG3621, PATA, Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only]
MSANKPFRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLY
EEEGKEIFPKSRWRKLLSLRGLFGPKYDSEGLEKVLKEYFGDTTLGDLKTPVLIPSYDLDNGKPVFFKSP
HAKFDRDRDFLLVDVARATSAAPTYFPPAQIKNLTGEGYALIDGGVFANNPALCALAEALKLLGPDLDDI
LVLSLGTGTAPRSIPYKKVKNWGALGWLLPLIDILMDAQSDAVDYQLRQLLGDRYYRLDPELPEEIALDD
NAENIEALLAAAEKLI
>gnl|CDD|442840 COG3622, Hyi, Hydroxypyruvate/dehydroerythronate isomerase, Hyi/OtnI family [Carbohydrate transport and metabolism]
MPRFAANLSMLFTELPFLDRFAAAAAAGFDAVEFLFPYDRPAEEIAAALKKHGLTLVLFNLPAGDWAAGE
RGLAALPGREAEFRAGVDRALEYAAALGCKNLHVMAGNRPRGLDDEAALATFVENLRYAADLAAPHGITL
LIEPLNSRDHPGYFLDTTAQAVAIIEAVGSPNLKLLYDIYHMQIMEGDLIRTIRRHLPRIGHVQIADVPG
RHEPGTGELNYPAIFKALDALGYDGWVGCEYKPRGDTEAGLGWLKAYRVA
>gnl|CDD|442841 COG3623, SgaU, L-ribulose-5-phosphate 3-epimerase UlaE [Carbohydrate transport and metabolism]
YRLGIYEKALPNTLSWPEKLALAKELGFDFVEISIDESDERLARLDWSDEERRELRDAMEETGIRIPSMC
LSAHRRFPLGSADPAVRERALEIMEKAIDLASDLGIRTIQLAGYDVYYEPSDEETRQRFIEGLKKAVELA
ARAGVMLAIEIMDTPFMNSISKAMELVKEIDSPWLQVYPDIGNLSAWGNDVADELELGIGHIVAIHLKDT
LPGQFRDVPFGEGCVDFVAAFKTLKRLGYRGPFLIEMWNEDAEDWVAEIRQARDFLEQKLDEAGLAV
>gnl|CDD|442842 COG3624, PhnG, Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG [Inorganic ion transport and metabolism]
MTESADTAARQRWMRVLARAPPAELEALWAALGALPEVEWLRAPETGLVMVRGRAGGTGAPFNLGEATVT
RAAVRLADGTVGHAYVLGRDKRHAELAAVLDALLQTPAHRAALEAALLAPLAAARAARRAARAAEAAATK
VDFFTMVRGE
>gnl|CDD|442843 COG3625, PhnH, Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH [Inorganic ion transport and metabolism]
PGFADPVHDAQRAFRALLDAMARPGTIVTLPGALAPPAPLSPAAAAVLLTLADHDTPVWLDPALAADAVR
AWLRFHTGAPLVDDPEEADFALIADGAALPPLARFAQGTAEYPDRSATLIVEVESLAGGPGLRLTGPGIK
GERRLAPPGLPAAFWAALAANRALFPLGIDLILTCGGRLAALPRTTRVEV
>gnl|CDD|442844 COG3626, PhnI, Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI [Inorganic ion transport and metabolism]
MYVAVKGGERAIANAHRLLAERRRGDPAVPELSVDQIREQLRLAVDRVMAEGSLYDPELAALAIKQARGD
LIEAIFLLRAYRTTLPRFGYSEPLDTAAMRVERRISATFKDLPGGQVLGPTFDYTHRLLDFALLAEGEPP
FAPPEAEALPEPMPRVTDLLRAEGLIEPEPDADDAEPFDITREPLVFPAPRSARLQALARGDEGFLLALA
YSTQRGYGRNHPFAGEIRVGYVEVELVPPELGFAVEIGEILVTECEMVNQFKGSADEPPQFTRGYGLVFG
HSERKAMSMALVDRALRAGELGEEVTAPAQDEEFVLSHSDNVEATGFVEHLKLPHYVDFQSELELLRRLR
AEHAAAQADRADQTQEAAE
>gnl|CDD|442845 COG3627, PhnJ, Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase PhnJ [Inorganic ion transport and metabolism]
MTTAMDAGYNFAYLDEQTKREIRRAILKAVAIPGYQVPFASREMPIARGWGTGGLQVTLSLIGPDDVLKV
IDQGSDDTVNAVNIRRFFARTTGVATTTDTEEATLIQTRHRIPEEPLREDQILVLQVPIPEPLRFVEPSE
TETRRMHAEADYGRMWVKLYEDIVRFGEIATGYDYPVMVNGRYVMDPSPIPRFDNPKLHMSPALQLFGAG
REKRIYAVPPYTDVESLDFEDHPFEVEDFDGRACALCGATDSFLDEVIDDDTGERMYVCSDTDYCAERRA
AAEAAPDEAD
>gnl|CDD|442846 COG3628, COG3628, Phage baseplate assembly protein W [Mobilome: prophages, transposons]
MSEPGFDRATGRVAMVSGEEHIRQSIRIILTTPPGERVMRPDFGSGLHDLLFEPNNPATALLIRAAVAEA
LLRWEPRIEVESVDVTPDPEEDGKLLITIDYTVRATNQRFNLVYPFYLG
>gnl|CDD|442847 COG3629, DnrI, DNA-binding transcriptional regulator DnrI/AfsR/EmbR, SARP family, contains BTAD domain [Transcription]
PLRFRLLGPLEVRVDGRPVPLGGPKQRALLAYLALRAGRPVSRDRLADLLWGDDPPASARANLRTYVSRL
RRALGPAGGDLLVTRGGGYRLDVDPDEVDLHRFERLVARARAAAGDPAAAAALLREALALWRGPPLAGLP
FEPWLEAERARLEELRLAALEALAEALLALGRHAEALAELRRLVAAHPLRERLHRLLMRALYRAGRRAEA
LAAYRRLRRRLADELGVEPGPELRALHRRILRGD
>gnl|CDD|442848 COG3630, OadG, Na+-transporting oxaloacetate/methylmalonyl-CoA decarboxylase, gamma subunit [Energy production and conversion]
MTNSELLLEGLNLMLLGMGFVFVFLTLLVFAIKLMSKLINRFFPEPEPAPVATPSASAAPTADDPELVAA
ITAAIHHHRR
>gnl|CDD|442849 COG3631, YesE, Ketosteroid isomerase-related protein [General function prediction only]
TNRELVRRFYAAFNAGDVDALLALLAEDVVWEDPGGPGAGTYRGKEAVRAFFARLAAAFEDLRFEVRRVV
ADGDRVVVEGTVRGTVLATGKPYENRYADVFTVRDGKIVRVREYFDTAALAAALGA
>gnl|CDD|442850 COG3633, SstT, Na+/serine and Na+/threonine symporter SstT [Amino acid transport and metabolism]
MSTSSLLRKWNRGSLVKQILIGLVLGILLALLSPEAAKSVGLLGTLFVGALKAVAPILVFVLVMSAIANH
KQGQKTNMKPIIVLYLLGTFLAALVAVVASFLFPTTLTLVAAAADLTPPGGIGEVLKTLLLNVVDNPVNA
LANANYIGILAWAIGLGLALRHASDTTKTVLSDLSDAVSKIVRWVIRFAPLGIFGLVASTVATTGFSALL
GYAHLLAVLVGCMLFVALVVNPLIVFLKIRRNPYPLVFTCLRESGITAFFTRSSAANIPVNMALCEKLGL
DEDTYSVSIPLGATINMAGAAITITVLTLAAVHTLGIEVDLPTALLLSVVAAVSACGASGVAGGSLLLIP
LACSLFGISNDIAMQVVAVGFIIGVIQDSAETALNSSTDVLFTAAACYAEERKEGK
>gnl|CDD|442851 COG3634, AhpF, Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]
MAMLDDELKAQLKEYLEKLKNPVELVLFLDDCEKSEELRELLEEIASLSDKISLEVYDKDDVERAPSFAI
LRDGEDTGIRFAGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQ
ALNLMAVLNPNITHEMIDGAEFPDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKLDT
>gnl|CDD|442852 COG3635, ApgM, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate transport and metabolism]. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type is part of the Pathway/BioSystem: Glycolysis
KYILLIGDGMADRPIEELGGKTPLEAARTPNMDRLAREGICGLMDTVPPGMPPGSDVANLSLLGYDPEKY
YTGRGPLEAAGMGIELGPGDVAFRCNLVTLDEDGVMVDRSAGHISTEEAAELIEALNEELGGVEVRFYPG
VSYRHLLVLRGGGLSDKVTDTPPHDIGGKPIADYLPLPEGKKTAEILNELMEKSYEILADHPVNRKRVEE
GKPPANSIWLWGAGKRPALPPFKEKYGLKGAVISAVDLIKGIGKLAGMDVIDVPGATGYLDTNYAGKAEA
ALEALKDYDFVYVHVEAPDEAGHDGDLEEKVKAIERIDRRVVGPLLEGLEKFEDYRILVTPDHPTPISLR
THSGDPVPFLIYGPGVRPDDVTRFDERSAAKGGLGRIRGHELMPLLLN
>gnl|CDD|442853 COG3636, PA5055, Uncharacterized Zn-binding protein, DUF971 domain [Mobilome: prophages, transposons]
MMKTKLRDFDLAEYLKDPEDAAAYLNAALEEGDPAELLAALGDVARARGMSQLAKEAGLSRESLYKALSP
KGNPTLDTLLKVLKALGLRLTV
>gnl|CDD|442854 COG3637, LomR, Opacity protein LomR and related surface antigens [Cell wall/membrane/envelope biogenesis]
MKKLLLAALAAGVQAGYNFQFDNFVLGVEGDYSYSDIDGDSSGTTGSGDLDYLSLRARAGYDFNDRFLPY
ATAGVAYARVKVTGNTGSGTSGSDSDTRFGWTVGAGVEYALTDNWSLRLEYRYTDLGDADFDGGGSVDVD
LDSHTVRVGLNYRF
>gnl|CDD|442855 COG3638, PhnC, ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism]
PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAL
RGRALRRLRRRIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKA
YQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLA
RRYADRIIGLRDGRVVFDGPPAELTDAVLREIYGGEAEE
>gnl|CDD|442856 COG3639, PhnE, ABC-type phosphate/phosphonate transport system, permease component [Inorganic ion transport and metabolism]
LLLLALLALLVWSLWGLEFDLGRLIDGLPNLADFLSRFFPPDWSYLPDLLSALLETLAIALLGTLLGAVL
ALPLAFLAARNLAPNPWVRLLARRLLNVLRAIPELVWALIFVAAVGLGPFAGVLALAIHTIGFLGKLFAE
AIEEIDPGPVEALRATGASRLQVIRYGVLPQVLPQFLSYTLYRFEINIRAATVLGLVGAGGIGLLLNEAI
RLFQYDEVAAILLVILVLVLLIDLLSARLRRRLI
>gnl|CDD|442857 COG3640, CooC, CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones]
MKIAVAGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEVEADLIKPLGEMRELIKERTG
APGGGMFKLNPKVDDIPEEYLVEGDGVDLLVMGTIEEGGSGCYCPENALLRALLNHLVLGNYEYVVVDME
AGIEHLGRGTAEGVDLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGNKVREEEDEEFLRELLGLEL
LGFIPYDEEVREADLEGKPLLDLPDSPAVAAVEEIAEKL
>gnl|CDD|442858 COG3641, PfoR, Membrane regulatory protein PfoR, PTS_EIIC_2 domain (does not regulate perfringolysin expression) [Signal transduction mechanisms]
FLKRKNIKISVKRFFIKVLNGMALGLFVSLIPGAILGTIGKLLGIAFLIQIGTIAQSLLGPAIGVAIAYQ
LKAPPLVLFSAAIAGAIGSGAVKFTDGGIVLIGIGDPIGAFLAAIIAVEIGKLVSGKTKLDIILTPLVTI
LVGGLIGLLILPYVGPITTAIGNLINWATELQPLLMGILIAVVFGILLTSPISSAAIAIALGLSGLAAGA
ANIGCCAQMVGFAVMSYRENGIGGLLAQGLGTSKLQMPNIVKNPKIWIPPTLAAAILGPIATVLFKIQGT
PESAGMGTSGLVGPINALATMGSSLMNLLGILLLHFVLPAVLSFIIYYLFRKLGWIKPGDLKLEL
>gnl|CDD|442859 COG3642, Bud32, tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]. tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification
ERTRREARLLRELREAGVPVPKVLDVDPDDADLVMEYIEGETLADLLEEGELPPELLRELGRLLARLHRA
GIVHGDLTTSNILVDDGGVYLIDFGLARYSDPLEDKAVDLAVLKRSLESTHPDPAEELWEAFLEGYREVG
PAEEVLRRLREIELRGRYL
>gnl|CDD|442860 COG3643, GluFT, Glutamate formiminotransferase [Amino acid transport and metabolism]
MMKIVECVPNFSEGRDKEVIEAIVDAIRSVEGVKLLDYSPDADHNRTVVTFVGEPEAVKEAAFNAAKKAA
ELIDMTKHKGEHPRMGATDVIPFVPIRNVTMEECVELARELGKRIGEELGIPVYLYEEAATRPERKNLAD
IRKGEYEGLKEKIKDPEWKPDFGPAELHPTAGATAVGARMFLIAYNVNLNTDDVEIAKKIAKAVRESSGG
LRYVKAIGVYLEERGIAQVSMNLTDYTKTPLYRVFELVKREAARYGVNVVGSELVGLVPLEALLDAAEYY
LQLENFDEDQILENRLLELGLDE
>gnl|CDD|442861 COG3644, COG3644, Uncharacterized conserved protein, DUF2239 domain [Function unknown]
MSDSPSPTYTAFAGHRRIASGSLAEVALAVKAALDAGPAAPVLVFDDATGRQVDLDLRGSDAEVLARLAP
PAAAAAEASAPRGRGRPKLGVVAREVTLLPRHWEWLAAQPGGASVALRKLVDEARRAAAGRDRRRQAQEA
AYRFMSAMAGDLPGFEEASRALFAGDRARFAALIAAWPADVRDHALRLAAAAFAPASAA
>gnl|CDD|442862 COG3645, KilAC, Phage antirepressor protein YoqD, KilAC domain [Mobilome: prophages, transposons]
VAAAFEGASVALVIGIIIEIVSLENMEVRVDNESLGLGLAVKTSRRIEIRIGLVLAALESLKLVTKLVGR
RLLGLPVLLELLLALAEAALLELAERLEAAVLLAKRLAERAAERLLAAEEAEAQPELAELEEEKEALEQQ
LAEAAPKAEFYDRIVTSKGSISVRQAAKLLGIGENRLFAWLRENGILYRRGSGRWLPYQKYIDAGYFEVK
TGTYTDPDGNEHVSTQTRVTPKGRAYLAELLAEEGALPA
>gnl|CDD|442863 COG3646, pRha, Phage regulatory protein Rha [Mobilome: prophages, transposons]
MNQLELVTIKNGEPVTSSREIAELFGKRHKNVLRDIRKLISDLESPEFGQLNFEESTYEDSQNGRERPEY
LLTKDGFTLLVMGFTGKKAAEFKAAYIDRFNEMEEQLKQQSALPQTLTEALRALAEQEEEKEAALLLGLA
LAAAAARALAEQSEAEQTGVKLLLALRAKKEETAKLVDVLRKLGILRLSKRLKKKELKRRNLLLERGELR
R
>gnl|CDD|442864 COG3647, YjdF, Uncharacterized membrane protein YjdF [Function unknown]
MSERSRRLLLLLLALFLLVLIWSAIAPKDRATWLLEVAPVLIGLPLLIATYRRFPLSNLSYTLIFLHLLL
HTIGGHYTYAEVPLGDWLQDLFGLSRNHYDRLGHFAQGFLPAYPAREILLRRTPVRGGGWLFFLVVCVCL
AISAFYELIEWWVALISGGEAADAFLGTQGDIWDAQKDMLLALLGALLALLLLSRWHDRQL
>gnl|CDD|442865 COG3648, UriC, Uricase (urate oxidase) [Secondary metabolites biosynthesis, transport and catabolism]
MSAIVLGTNQYGKAEVRVVRVYRDGPRHEIRDLNVSVALRGDFLAAHLEGDNSHVLATDTQKNTVYAFAK
EHGVGSPEEFLLRLARHFVDTYEWVTGARVEIEEYAWDRIPVDGEEHDHSFVRSGQEVRTAVVTVDGDGT
WVVSGLKDLVVLKSTGSEFHGFPRDEYTTLPETTDRILATSVTARWRYSDPDPDWDASYEQVRDILLETF
AETHSLSLQQTLYAMGKAVLEAFPEIAEVRFSAPNKHHFLVDLSPFGLDNPNEVFHAADRPYGLIEATVL
RDDAPEA
>gnl|CDD|442866 COG3649, Cas7, CRISPR-Cas system type I effector complex subunit Cas7, RAMP superfamily [Defense mechanisms]. CRISPR-Cas system type I effector complex subunit Cas7, RAMP superfamily is part of the Pathway/BioSystem: CRISPR-Cas system
MTTIKNRYEFLFLFDVKNGNPNGDPDAGNRPRIDPETGRGLVTDVRLKRKIRDYLQDAKDGYDIFVQEGA
VLNGKHKSAYERLEDILEKKKKKKKDAEDLREWMCENFIDVRLFGAVMSTKGNSGQVRGPVQFTFARSLH
PVEPQEIQITRVAATEEKDAEGKDQGTMGRKHRVPYGLYAFHGFINANLAEKTGFTEEDLELLWEALWNM
FEHDRSASRGGMEPRLLIVFEHKSPLGNAPAGKLFDLVKVERKDGDEPPRSFEDYEVDVDELPEGLEVNR
LIEGVRYWVD
>gnl|CDD|442867 COG3650, COG3650, Uncharacterized membrane protein [Function unknown]
ALLAGVLLALLAALGAALATGLPAALTADLVAEKEETGTPAAFMQLLLVGGGGEAEAKGGTGSLSSQVLQ
LDTALDAAAAALGAPTPKAKGLPFRAFGNEPFWSLEIDGGGLVFSTPGGEEITLPYTEPQTAGGATVYRA
ETDGGSLTLTIRPGECSDGMSDRVYPYTATLTLGGRTLQGCGRLGG
>gnl|CDD|442868 COG3651, COG3651, Uncharacterized conserved protein, DUF2237 family [Function unknown]
MSKDEARNVLGEPLEPCSTDPLTGFYRDGCCNTGPEDLGSHTVCAVMTAEFLAFSKARGNDLSTPRPEFG
FPGLKPGDRWCLCAARWLEALEAGVAPPVVLEATHERALEVVPLETLKQHAVDL
>gnl|CDD|442869 COG3652, COG3652, Predicted outer membrane protein, contains DUF4142 domain [Function unknown]
MKTRGALALAALALAATPAAAAAAAAAAAAALSETDADFLAKAAQAGLFEIEAGKLALQKSTNPEVKAFA
QMMVDDHTKANEELKALAAKKGVTLPTELSADQQAKLDKLSKLSGAAFDKAYVDQQVAAHEKAVALFEKY
AAPGKDAELKAFAQKTLPTLQAHLEMAEALAKKLGK
>gnl|CDD|442870 COG3653, COG3653, N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism]
MFDLLIRGGTVVDGTGAPPFRADVAIKGGRIVAVGDLAAAEAARVIDATGLVVAPGFIDIHTHYDLQLLW
DPRLEPSLRQGVTTVVMGNCGVSFAPVRPEDRDRLIDLMEGVEGIPEGLDWDWESFGEYLDALERRGLGV
NVASLVGHGTLRAYVMGLDDRPPTPEELARMRALLREAMEAGALGLSTGLIYVPGTYASTDELVALAKVV
AEYGGVYQSHMRDEGDGLLEAVDELIRIGREAGVPVHISHLKAAGKPNWGKADEVLALIEAARAEGLDVT
ADVYPYPAGSTGLGALLPPWAAAGGLDERLARLRDPATRARIRAEIEEGLPDNLLGRGGWDNILISDSPP
NEPLVGKSLAEIAAERGVDPADAALDLLLEEDGRVLIVYFIMSEEDVRELLRHPWVMIGSDGGLGGKAHP
RAYGTFPRVLGHYVRERGVLSLEEAVRKLTSLPADRLGLKDRGLLRPGYRADLVVFDPATLADRATFDLP
AQRADGIRAVIVNGVVVVEDGKPTGARPGRVLRGGGAA
>gnl|CDD|442871 COG3654, Doc, Prophage maintenance system killer protein [Mobilome: prophages, transposons]
MTRYLSLEDVLAIHDRLLAEYGGLPGVRDEGLLESALARPRQTFFGEELYPDLFEKAAALLYGIAKNHPF
VDGNKRTAFAAALVFLDLNGYELDADDDEAVDLVLAVAAGELDEEELAAWLRKHLEPLSP
>gnl|CDD|442872 COG3655, YozG, DNA-binding transcriptional regulator, XRE family [Transcription]
MIYVKLDELLAERGMTKKELAEATGISRATLSRLKNGKAKAVRLDTLEKICKALDCQPGDLLEYVPDEE
>gnl|CDD|442873 COG3656, COG3656, Predicted periplasmic protein [Function unknown]
ALAALLAAPAAAAELKVTVEIPRLDVAEYHRPYVAVWIEDADGSPVRTLAVWYDTKKNEGTKWLKDLRQW
WRKSGRSLDMPVDGVSGATRPPGEHTLVWDGKDDAGNPLPPGKYTLVVEAAREVGGRELVRQPFTWPGKA
AQTAEAKGSSELGAVSLELKP
>gnl|CDD|442874 COG3657, COG3657, Putative component of the toxin-antitoxin plasmid stabilization module [Defense mechanisms]
REYYTIDGTEPFDEWLASLKDRRARARILARLDRLELGNFGDVKPVGEGVSELRIDFGPGYRVYYAQRGD
VLVLLLCGGDKSTQQKDIKKAKELAKEYKERKK
>gnl|CDD|442875 COG3658, CytB, Cytochrome b subunit of Ni2+-dependent hydrogenase [Energy production and conversion]
MSPTMAKVRVWDLPVRLFHWLLAALFLGAWLTGEGEGMDWHVWLGYALLALLLFRLLWGFVGSRYARFSD
FVPGPRAVLAYLRGLLRGRPPRYLGHNPLGALMVLALLLLLLLQALTGLFATDDAFWGPLAGLVSSDTSE
WLEELHELLANLLLALVALHVAAVLFYSLLHRENLVRAMITGRKRAPAEDPIPAS
>gnl|CDD|442876 COG3659, OprB, Carbohydrate-selective porin OprB [Cell wall/membrane/envelope biogenesis]
MRRLRRRLLAAAALALALAAAPAAAADGAAPSVATRPHLLGDWGGLRSWLADHGITFDLDYTGEVAGNVS
GGLRRGARYAGQLDLGLDLDLEKLAGWPGGTFHATVTNRHGRNLSADRLGDLQGVQEIYGGGVTTRLTEL
WYEQSLLDDRLDIKAGRLNVGSDFAASPLACNFQNLSFCGNPALNNLPSGGSNYPYSTWGARVRYRPTPD
LYLQAGVYDGNPAGYGRNRSGFDWGFSGSTGALLPVELGWKPNFGKDGLPGHYKLGGWYDTARFPDLYYD
VNGNPLALSGGPARTHRGRWGVYALADQMLWRPGGDPDRGLGLFGRAGVSDGDTNPIDYYADAGLVYKGP
FPGRPDDTIGLGFAYARLSSRLRAAQRDANAAGGGGTPVQRHETVLELYYGIQVTPWLTLQPDLQYIIHP
GGTSRIKNALVLGLRTTVTF
>gnl|CDD|442877 COG3660, ELM1, Mitochondrial fission protein ELM1 [Cell cycle control, cell division, chromosome partitioning]
MSKSAAPLRIWVLTDGKAGHENQALGLAEALGRPPEVKRVEPRGPWRWLAPRLPPGPLRALGGRDSDPLA
PPWPDLVISAGRRTAPPLLALKRASGTRTVQIMDPRLPPSHFDLVIVPEHDRLRGPNVLVTLGALHRVTP
ERLAAARAAWAPRLAALPRPRVAVLIGGPSRHYRFDPADAARLAEQLAALAPAEGGSLLVTTSRRTPPAA
LAALREALAGLPAVIWDGTGPNPYLGLLALADAIVVTADSVSMVSEAAATGKPVGVLPLPGGSGRFARFH
DALRAAGRARPFEGRLEDWRYEPLDETDRIAAEILERLGARRAA
>gnl|CDD|442878 COG3661, AguA2, Alpha-glucuronidase [Carbohydrate transport and metabolism]
LLASSNAQAEDGYDLWLRYDPIEDAALREAYRAAISRIVVLGDSPTLQSAADELQRGLSGLLGKAPPVVS
KATRDGALVLGTPDDSPLIAKLLLEEDLAALGEEGYLIRTVRVKGKGVTVIAANTDVGVLYGVFHLLRLL
QTGQPLDKLNIVSSPKIQLRMLNHWDNLDGTVERGYAGFSIWDWDNLPDYIDPRYRDYARANASIGINGT
VLNNVNANARLLTPEYLPKVAALADVFRPYGIKVYLSVNFAAPIEIGGLKTADPLDPEVRAWWKEKADEI
YRYIPDFGGFLVKANSEGQPGPQDYGRTHADGANMLAEALAPHGGIVMWRAFVYNCERKTDRAKAAYDEF
KPLDGKFRDNVIVQVKNGPIDFQPREPFSPLFGAMPKTPLMMEFQITQEYLGQQTHLVYLAPLWKEVLDF
DTYAKGKGSTVAKVVDGSLFGHKLTGIAGVANIGDDRNWTGHPFAQANWYAFGRLAWNPDLSSEEIADEW
IRLTFGNDPKVVETIKAMMLGSREAYVNYTTPLGLHHMMGPGHHYGPGPWVDGYERADWGTVYYHRADSD
GIGFDRTATGSNALAQYAPPVAELYESLETCPEELLLWFHHVPWDYKLKSGKTLWQELYDTYFEGVEQVR
EMQRTWESLKGKIDPERFEQVLERLEIQEKEAKWWRDACNLYFQRFSGIPDPAGREIP
>gnl|CDD|442879 COG3662, COG3662, Uncharacterized conserved protein, DUF2236 family [Function unknown]
MTAAADADGGGPRGDPGLFGPDSVTWRVHGDPRSMLLGGIRALLLQALHPGVGAGVADHSRFRTDPLGRL
RRTAAYVATVTYGDTEEAEAAAARVRRIHARVRGTDPDGRPYSALDPELLLWVHATFVDSFLRAYERFGG
PLTDAEADRYYAESARAARLLGVPDRDVPATRAEFRAYFDAMRPELEVTERAREVLRFLLRPPPPPLPRP
ALRPAGRLLRAATVGLLPPWARELLGLPWTPRDERAFRRLLRAVRAAVRLLPRRLRYAPLAPLRRARARL
RLARAPA
>gnl|CDD|442880 COG3663, Mug, G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair]
LPPVLAPGLRVLILGSNPGLASLAAGFYYAHPRNRFWPILGAAGGTDPRLDYPERKAFLLEHGIGLWDVV
ARCTRRAGSLDSAIRNAGPNDLAALLRYRPRIKTVAFNGKTAYRLFFKLVAPQPETIGGIELWVLPSPSP
ANARFSLEEKLAAWREL
>gnl|CDD|442881 COG3664, XynB, Beta-xylosidase [Carbohydrate transport and metabolism]
LLRTLLGPLAAAAPPPVAITVDLAKVAGPMKPLWAWFGYDEPNYTYMKDGKKLLSEGAGLSPVFRYIRFH
GLFHDDMGVYREDADGNPVYNFTYVDKIFDFLLELGMKPFVELGFMPEALASGPQTVFWWKGNVTPPKDY
AKWADLVRAFVRHLIDRYGIDEVRSWYFEVWNEPNLSGFWKGTQEEYFKLYDYTARAVKSVDPRLRVGGP
ATAGGAAAWLPDFLEHCAKNGVPVDFVSTHAYGTDPGFDGQLSMNPDAVLRDVEKVRKLIAASAFPNLPL
HITEWNTSYTPRDPYHDTAFYAAYIAKSLKRAGDLADSMSYWTFSDIFEEAGPPTQPFHGGFGLLNTNGI
KKPVYHAFRMLNRLGGERLAVGDDDAVATRDDDGRVAVLVWNYHDDDPAGPARTVELTLTGLPAGKYRLT
VYRVDEEHGNAYAAWLEMGSPQQPTREQIAELKAAAELQTSPEVVVVADGKLTLDLTLPRNSVVLIELTP
>gnl|CDD|442882 COG3665, YcgI, Uncharacterized conserved protein YcgI, DUF1989 family [Function unknown]
MTTPLPPADPLWEETVPAGSGWSFEVKRGQTLRIIDLEGNQVVDLLAFNADDPSERLSAPDTRKAQGTAY
LTTGDVLYSDMGRPLLTIVEDTVGRHDTLGGACSAESNTVRYGDRNDGHRNCRDNFLLALAKYGLGKRDL
PPNINFFMNVPVDADGGLSFDPGLSRPGDYVELRAEMDLLVVLSNCPHPLDPCNGYNPTPIHVEVWDAEP
PAADNATPENR
>gnl|CDD|442883 COG3666, COG3666, Transposase, IS1182 family [Mobilome: prophages, transposons]
MRGFRDYDRQQSLLLPVSLEDLVPEDHPLRAIDALVDELDFILSELEKLYSADTGRPAYDPEMLLKLLLY
GYLEGIRSSRQLEEACRYNLAFRWLLGLELDDPVPDHSTISRFRKRLLKSDVLEKLFAQVVLQAREEGLI
SGEHVAIDGTKIEANASKKSFVEKKALEK
>gnl|CDD|442884 COG3667, PcoB, Uncharacterized conserved protein involved in copper resistance [Inorganic ion transport and metabolism]
MKRPLAAALALLLLLLASPALAQDMDHAAQMQGSAPVPDARDPDAYADGYPRLLAMHDEHIFGFVLVDRL
EYRRGDGGDALAWDGQAWYGGDYNRLWLKSEGEGSSGGRLEEAEVEALYSRAISPFWDLQAGVRYDFGPG
PDRTWAAFGVQGLAPYWFEVDATAYLSEDGDLAARLEAEYDLLLTQRLILQPRAELNLYAQDDPERGIGS
GLSDVELGLRLRYEIRREFAPYVGVEWERKFGDTADLARAAGEDTSETRFVAGVRFWF
>gnl|CDD|442885 COG3668, ParE, Plasmid stabilization system protein ParE [Mobilome: prophages, transposons]
MKVRWTPEAEADLEEIYDYIAEDWGPEAAERYLDEIEEAIELLAEFPELGRPRPELRVPGLRELVVGPYV
IFYRVDDDTVEILRVLHGRRDLPALL
>gnl|CDD|442886 COG3669, AfuC, Alpha-L-fucosidase [Carbohydrate transport and metabolism]
MKKKLLLALLLLAAAQASLAPQKEKVPQLWFQDAKFGIFIHWGLYSVPGGAEWYMRYGKIPKFGYKDLAK
LFNPEKFDADQWARLAKDAGAKYVVLTAKHHDGFCLWDSKYTDYNVVDNSPWKRDVVKELAEACRKEGLK
FGLYYSPWDWHHPDYPYGPKPPDWPEYLEYWLNQLKELLTNYGPIDELWFDGAWPNGKRQEWDSPELYAL
IRNLQPEAVINDRLGLPPGPDYVTPERGIPTEIPPGPWETCTTIGPSWGYHEDDKYKSPEELIDILVDSV
SKGGNLLLNIGPDADGTIPEEDVERLKEIGAWLKVNGEAIYGTRPKVAGLDEDTRFTTKGNALYAIVLGW
PENGIVLQELALGQRVKSVELLGTGKRIRFEQTDKLRITIPEKAPSEFAVY
>gnl|CDD|442887 COG3670, COG3670, Carotenoid cleavage dioxygenase or a related enzyme [Secondary metabolites biosynthesis, transport and catabolism]
TTPFSDNPWLKGFAPLREEFDATDLPVEGEIPADLRGTLYRNGPGPLERGGQRYYHWFDGDGMIHAVRFE
DGRASYRNRFVRTEGYQAEQAAGRALYGGFGTPPPGGLWARLFDGPLKNTANTNVLAHGGKLLALWEGGR
PYELDPDTLETLGEDDLDGKLPGDAFSAHPKIDPRTGELVNFGYSFGLSPTLTLYRIDADGKLVRLGSIP
LPGPAMIHDFAITENYLIFFDPPLRFNPLRLLLGGRSFSDALEWDPELGTRILVIPRDDGSDVRWFETEP
FFVFHFANAYEDGGEIVVDLVRYDDFPVNQPLFEVLRGEDTPTAAPGRLWRWRLDLKTGTVREERLDDRS
CEFPRIDPRRVGRPYRYGYAAAADPGGGNPLFDGLAKFDLETGTLQTWDFGPGRYPGEPVFVPRPGAAAE
DDGWLLTVVYDANEDRSELLILDARDLEAGPVARLHLPHRVPFGFHGTWV
>gnl|CDD|442888 COG3671, COG3671, Uncharacterized membrane protein [Function unknown]
MNDPPPAPLPPKLESLRTLALIIYILYLLGFVTGITAIVGVIIAYVKRDDAAGTWLESHFRWQIRTFWIG
LLWLVIGGLLTFILIGFLILLAAWIWVIYRIVKGWLALNDNKPMPNP
>gnl|CDD|442889 COG3672, COG3672, Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, chaperones]
LAAALLLGLAAAAAAAQFAATGGATSAPYGHYEFCKRYPAECAVRVREWRLVELTLDEWAKLRAVNRFVN
RRIRPVTDIDHWGVEDYWATPLEFLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRDLPLGQGHAVL
TVRTDAGDLVLDNLTDAILPWSQRYDLLPRQSFNGPGLWVSIGRGRGSLVGSVRMRA
>gnl|CDD|442890 COG3673, COG3673, Uncharacterized conserved protein, PA2063/DUF2235 family [Function unknown]
MPKRLVVCCDGTWNSPDQGYPTNVVKLYRALRPDDDGARQIVYYDPGVGTDGRKWDRLLGGAFGRGLDRN
IRDAYRFLARNYEPGDRIYLFGFSRGAYTVRSLAGLIARCGLLRPEHATELVDEAYRLYRDRSPRRPDLD
EARRFRRKYCHRRVPIEFLGVWDTVGALGIPLPLLRLANRRYEFHDTTLSPSVRHARHALAIDERRKAFA
PTLWDEPPPGPPQRVEQVWFAGVHSDVGGGYAERGLSDIALVWMLEEAEAAGLRLDPLALRERLPADAPP
PAAAPLGGALKGFGPRRRRRPRRDRLEALRVVARRPVLRRRRPAAALRRRAARPLDLLLARRRPAAA
>gnl|CDD|442891 COG3675, Lip2, Predicted lipase [Lipid transport and metabolism]
MASLCKLAYPVTQGDPEVFGFILRSDDEVIVAFRGTESLTDWLTNLNAAQVPYPFAKTGGKVHRGFYRAL
QSLRELLEDALRPLSPGKRLYVTGHSLGGALATLAAADLERNYIFPVRGLYTFGQPRVGDRSFAKYYNLH
VPNSYRIVNNNDIVPLLPPVWMGYDHVGKLLWLDSLRKDMLTDHSMDNYIHHTDLSQLLTYAYEAAVLRA
FKRTGVTMLLAEGDGRVADVRLAWALSDLQIVIEHIVRRVLELLDALGVSPDESLA
>gnl|CDD|442892 COG3676, COG3676, Transposase and inactivated derivatives [Mobilome: prophages, transposons]
RNGSYRVYQRYLCKNCGRTFNDKTKTIFAHSKTKLRKWSFLIYLFLRFNTLLRQLELESSHSAARLLRHV
EQFARFLDARRILLFGPVEIDESGEVEVDESYFGGKRKGKRGRGAAGKVPVFGILKRNGKVYTVPVPDAK
RATLLPIIREKVEPGSTVYTDEFRSYDALDVSGFTHERVNHSKEFADGRNHINGIENFWSQAKRWLRKYN
GVSKKKFPLYLKECEFRFNHRKEPQLLKALKKWLKKRLL
>gnl|CDD|442893 COG3677, InsA, Transposase InsA [Mobilome: prophages, transposons]
MSTAEELLEQIRWPNGPVCPHCGSTRIVKNGKTRNGRQRYRCKDCGRTFTVTTGTIFEGSKLPLWLQAIR
LLLNGISLRQIARVLGVSYKTVWRWLHRIREALDELVDEVDEGEGLVGEEDEKTKSKRRRKRGKKLVKGL
KKGVVVKVRARGARKSKLAVRLELADLLLRRIILAALVAPLATDLAVGVDSKKHELLELARHTRRRRYRR
LVRKAERFSKKSRNRILASWTVRHHYVYVLH
>gnl|CDD|442894 COG3678, CpxP, Periplasmic chaperone Spy, Spy/CpxP family [Posttranslational modification, protein turnover, chaperones]
MKLKLLALLLALALALGAASAFAAGPPGGPRGGRGLRRMLEGLNLTEEQRQQIRAIRQQYRKQMRALRQQ
LREAREELRALLAADKFDEAAVRALADKIAALRAQLAVERAEARNQMYKVLTPEQRAKLAELMQERGEKH
G
>gnl|CDD|442895 COG3679, YlbF, Cell fate regulator YlbF, YheA/YmcA/DUF963 family (controls sporulation, competence, biofilm development) [Signal transduction mechanisms]
MNIYDKANELAEAIRESEEYKALKEAKEAVEADEEAQKLIREFQKLQEELQEKQRFGQEHTEEEMKKLQE
LKRELDLNPVIAEYLEAEQRLQQLLDDINKIIAEAVSEGYNP
>gnl|CDD|442896 COG3680, COG3680, Uncharacterized protein, contains GIY-YIG domain [Function unknown]
MDKKFPPEVIEKLGYYVYALIDPRDNKPFYIGKGKGNRVFAHLREAIASNESESAKLERIREIKKAGLDV
EHYILRHGLDEKTAFEVEAALIDLLGIVEAKLTNIVRGHGSDAFGRMTLEELIRRYAAPPLPPIDHPVLL
IKINKTYRSSLSAEELYEATRGAWVLGKDRREKVKYALAVYQGLVREVYEIDKWLPATTEPYSTRETEEN
RKQGRWEFVGRIAPDELRDLYLGKSVRKYRKRGAQNPIRYVGA
>gnl|CDD|442897 COG3681, CdsB, L-cysteine desulfidase YhaM [Amino acid transport and metabolism]
MDTELYQTLIEILKEEVVPALGCTEPIAVALAAAKAREVLGGEPEKIEVKVSGNIYKNGMGVGIPGTGMK
GLEIAAALGAVGGDPEKGLEVLKDVTPEDVEKAKELLDEGRVTVELKETDEGLYIEATVKTGDHSARVVI
EGSHTNIVLIEKNGEVLFEKESSAASEESLLEDLKKLSIKDIYDFAEEVDLEDIAFILEGIEMNMAIAEE
GLKGKYGLGIGKTLLKQIEKGLLGDDLLSRARALTAAASDARMSGCPLPVMSNSGSGNQGITATLPVVVY
AEHLGASEEKLARALALSHLVTIYIKSYIGRLSALCGAVVAGAGAAAGIAYLLGGDYEQIEGAIKNMLAN
LSGMICDGAKPSCALKVSTAVSAAILAALMALDGIVVTGGDGIVGEDVEETIRNLGRLASEGMKETDKEI
LEIMLKKQK
>gnl|CDD|442898 COG3682, CopY, Transcriptional regulator, CopY/TcrY family [Transcription]
KMKKLTEAELEVMQVLWELGPATVREVLEALPEERGWAYTTVLTLLRRLEEKGFLSREKEGRAYVYRPLV
SREEYQAQELRDLLDRFFGGSLKALVAAFVEEEKLSPEELEELRKLLDEKKKKKK
>gnl|CDD|442899 COG3683, COG3683, ABC-type uncharacterized transport system, periplasmic component [General function prediction only]
MTRLRRALRALLALLLLLLAAGPALAHPHVFIDARLEVVFDPDGQLTGVRHTWTFDEFYSAFLLQDLDKD
GDGKLTPEELAKLAAENMENLAEFHYFTYLKAGGKKVAFGPPTDYSLEYKDGRLTLTFTLPLAEPVPLAG
GPLTLEVYDPTYYVAFTYAEDDPVTLVGAPAGCTLEVVRPDPDAALVAYAQSLDEADFPDLPDEDPDLGA
QFAQRVTVTCP
>gnl|CDD|442900 COG3684, LacD, Tagatose-1,6-bisphosphate/sulfofructosephosphate aldolase [Carbohydrate transport and metabolism, Inorganic ion transport and metabolism]
MKLTPGKLRGLKRLSDPDGVIAALAIDQRGSLKKMLAKARGEEVTYEEIEEFKELVSEELTPYASAILLD
PEYGLPAAKARPGNAGLLLAYEKTGYDATEPGRLPDLLDGWSVKRIKEAGADAVKLLLYYDPDEPAEINE
HKHAFVERIGSECRAEDIPFFLEPVTYDANGEDEKSAEFAKVKPEKVIESMKEFSKPRYGVDVLKVEVPV
NMKYVEGFAGGEAAYTREEAAAAFREQSEATDLPFIYLSAGVSAELFQETLEFACEAGAKFSGVLCGRAT
WQDAVEVYAKPGEAAAREWLRTEGVENIEELNEVLAETATPWTEKYGGKE
>gnl|CDD|442901 COG3685, YciE, Ferritin-like metal-binding protein YciE [Inorganic ion transport and metabolism]
MAIKTLEDLFVHELRDIYAAEKQLLKALPKMARAATSPELKAAFEQHLEETEGQVERLEQVFERLGEKPS
GKKCDAMEGLIAEGQEILEEFADDEVLDAALIAAAQKVEHYEIAAYGTLIALAEQLGLDEAADLLEQTLD
EEKATDEKLTELAESLLNREAAGEE
>gnl|CDD|442902 COG3686, COG3686, Uncharacterized conserved protein, MAPEG superfamily [Function unknown]
MTIELWCLLLAALLPLVQVALAKLARNRQLGGYDWNAGPRDWLAPLSGWAARANRAQQNAFEALPLFAAA
VLVAHLTGASSATTALLAIAFLAARVLYVPAYLAGLPPLRSLVWAVGFLCTVALFVAALL
>gnl|CDD|442903 COG3687, COG3687, Predicted metal-dependent hydrolase [General function prediction only]
MNAAARTPAAVEIKPRRLDFDFDEDVPRYWFGGDPFLTHFFNALSALFPEGERFFIRSVRHFRDQITDPE
LKADIKGFIGQEAMHSREHEKFNEALAAQGYPVDRLEKRLKRLLKRLEKRLPPRLQLAITAALEHFTAIL
AELLLENPELLEGADPEMRALWLWHAIEEIEHKAVAFDVYQAVGGSYFLRVLGMLLATVLFFGFIFLGTA
YLLKQDGKLFRPKTWRRGLKFLFGRPGLLRRLLPPYLDYFRPGFHPWDHDNRALLEAWLAELADEGGPAA
AAAA
>gnl|CDD|442904 COG3688, Rae1, EndoRNase involved in mRNA decay, NYN (Nedd4-BP1/Rae1/YacP nuclease) family, contains PIN domain [Translation, ribosomal structure and biogenesis]
EILLVDGYNVIGAWPELKELKDDSLEAARDKLIEILANYAAFTGYEVIVVFDAHYVPGSEEKEEKYGGVE
VVFTKEGETADSYIERLVAELRNRPRRVTVVTSDRAEQRTVFGRGALRISARELLREVEEAKREIRKKIK
KKKPKRNTLKDRLDPEVLEKLEKLRRGK
>gnl|CDD|442905 COG3689, YcgQ, Uncharacterized membrane protein YcgQ, UPF0703/DUF1980 family [Function unknown]
RNFLDWVRDIYDNPDAYTGKTVKVTGFVYRDPDLPENQFVLARFVITCCAADAYPVGLLVKGPGADSLPN
DTWVEVTGTLSTETYPYGKRVPVLKVTSIEPIPKPKNPYVY
>gnl|CDD|442906 COG3691, YfcZ, Uncharacterized conserved protein YfcZ, UPF0381/DUF406 family [Function unknown]
MSDAIKKCKAEETAACCCVDVGTIIDNSDCTASFEAVYASEAEAEAALAALTEKARAVESEPCEISSEIT
PVEDGVLLKADFTFSCQAETLIFQLGLR
>gnl|CDD|442907 COG3692, YifN, Uncharacterized conserved protein YifN, PemK superfamily [Function unknown]
MALKFHPKVGEILMCDFSTGFVPPEMVKRRPVVVISPKLRNRPGLCTVVPLSTTPPRPVEPYHYRLPRNP
LPDKFDNRPSWAKCDMIYTVSFDRLDRVRDGKRRYRTPVLSPEDLRRIQRAVLKALGLGSLT
>gnl|CDD|442908 COG3693, XynA, Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism]
ALALAALDAAAAPGAASLKDLAADKGFLFGTAVNAGQLDDPAYRELLAREFNSVTPENEMKWGSIEPERG
EFNFSAADAIVAFAKANGMKVRGHTLVWHSQTPDWVFEDALSKEELRARLEEHITTVVGRYKGKIYAWDV
VNEAIDDDGSLRNSPWYQALGPDYIADAFRWAREADPDAKLFYNDYNIEGGPAKRDAYLELVKDLKARGV
PIDGVGLQGHLGLDYPSPEEIEAALDRFAALGLPIHITELDVRVLPLPDLTEEDDAAQADRYRDLFDAFL
SHPAVTGVTFWGLTDGYSWRPGFRTGYPLLFDEDYQPKPAYDAVLDAL
>gnl|CDD|442909 COG3694, COG3694, ABC-type uncharacterized transport system, permease component [General function prediction only]
MMRYLRLYLLFLKASLKSQLEYRANFLLGLLGSLLWLALGLLFLLVIFRHFPSIGGWSFYEVLFLYGLFL
LSFGLADTFFPNLWRLPEYIRTGTLDFLLLRPVNPLFQLSTRRFDLWRLGDLLVGIILLIYALSKLGIDW
TPLDVLLFILLLLSGVLIFYSLWLLLASLSFWFVRSENLTELFYGLSEFGRYPLSIYPGAIRFFLTFVIP
VAFVSYYPALALLGRPDPLWLALLAPLAAVVLLLLARLFWRFGLRRYTSAGS
>gnl|CDD|442910 COG3695, Atl1, Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like DNA-binding domain [Transcription]
MEMEEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSPGH
AGGAEEQRELLEAEGVPVVDDGRVDLKRYRWDPD
>gnl|CDD|442911 COG3696, CusA, Cu/Ag efflux pump CusA [Inorganic ion transport and metabolism]
MLNRIIRFSLRNRLLVLLLTLLLAAAGIYSLRRLPIDAFPDITNVQVQVITEAPGLSPEEVEQQVTYPIE
TALNGLPGVKEVRSISRFGLSVVTVIFEDGTDIYWARQLVLERLQQVREQLPAGVTPELGPISTGLGEIY
QYTLESDPGKYSLMELRTLQDWVIRPQLRSVPGVAEVNSFGGFVKQYQVLVDPAKLRAYGLTLDDVIEAL
ERNNANVGGGYIERGGQEYLVRGIGLIRSLEDIENIVVKTRNGTPVLLRDVAEVRIGPAPRRGAATLNGE
GEVVGGIVLMLKGENALEVIEAVKAKLAELKPSLPEGVKIVPFYDRSDLIDRAIHTVTKNLLEGALLVIL
VLFLFLGNLRAALIVALAIPLSLLFAFIVMRLFGISANLMSLGGLAIDFGIIVDGAVVMVENILRRLEEN
RAAGTPRERLEVVLEAAREVRRPIFFATLIIILVFLPIFTLEGVEGKLFRPMALTVIFALLGALLLSLTL
VPVLASLLLRGKVPEKENPLVRWLKRLYRPLLRWALRHPKLVLAVALVLLVLALALFPRLGSEFLPELDE
GDLLVMATLPPGISLEESVELGQQVERILKSFPEVESVVSRTGRAEDATDPMGVNMSETFVILKPRSEWR
SGRTKEELIAEMREALEQIPGVNFNFSQPIQMRVDELLSGVRADVAVKIFGDDLDVLRRLAEQIEAVLKT
VPGAADVQVERVTGLPQLDIRIDRDAAARYGLNVADVQDVVETAIGGKAVGQVYEGERRFDIVVRLPEEL
RDDPEAIRNLPIPTPSGAQVPLSQVADIEVVEGPNQISRENGRRRIVVQANVRGRDLGSFVAEAQAKVAE
QVKLPPGYYIEWGGQFENLQRATARLAIVVPLALLLIFLLLYLAFGSVRDALLILLNVPFALIGGVLALW
LRGMPLSVSAGVGFIALFGVAVLNGVVLVSYINQLRAEGLDLREAIIEGALERLRPVLMTALVAALGLLP
MALSTGPGSEVQRPLATVVIGGLITSTLLTLLVLPALYLLFGRRRLRRAAA
>gnl|CDD|442912 COG3697, CitX, Phosphoribosyl-dephospho-CoA transferase (holo-ACP synthetase) [Coenzyme transport and metabolism, Lipid transport and metabolism]
MPEMASGKEVSLEELLAAREQRAARQQELLEKYQQPLISLTLNIPGPVKDSPLLRRIFNEALQALEELLE
QNGWPVLEQQVLNLPTGPEAFLAVDADAEELKRAMIELEESHPLGRLWDIDVLDPDGESISRRDLGLPPR
RCLICGQPAKVCARSRRHSLEELLAKIEEIINDYFA
>gnl|CDD|442913 COG3698, YigE, Uncharacterized conserved protein YigE, DUF2233 family [Function unknown]
LLLALLLAAAPAAAVACEDLTFEGARYTVCTVDPAREDLRLFWKDDDGEPYGSFSALAAALAAKGKRLAF
AMNAGMYHPDRSPVGLYVENGRELVPLNTASGPGNFGLLPNGVFYLGDGRAGVIETRAFLAAGPKCRYAT
QSGPMLVIDGALHPRFLPDSTSRKIRNGVGVSADGRVVFAISEEPVNFYDFARLFRDRLGCPNALYLDGT
ISRLYAPELGRNDQGFPFGPIIGVVEKAP
>gnl|CDD|442914 COG3700, AphA, Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction only]
MKKVTLALSALALALSLSSSAFAAGPKVPYTQEGTTVAQLAQQAPIHWVSVEQIENSLKGKPPMAVGFDI
DDTVLFSSPGFYYGKQKFSPGSYSYLKNQKFWDKMNNGWDEFSIPKEVARALIAMHLKRGDQIYFITGRT
ATKTETVTKTLQKDFNIPAKNMNPVIFAGDKPGQYDKTQWIKKHNIKIHYGDSDDDILAAREAGIRGIRV
LRASNSTYQPLPQAGGYGEEVIVNSEY
>gnl|CDD|442915 COG3701, TrbF, Type IV secretory pathway, TrbF component [Intracellular trafficking, secretion, and vesicular transport]
MSFYGRTPEPETPYQKARQEWDERIGSARVQARNWRLMAFGCLLLALVLSGGLVWQSSQSKVVPYVVEVD
KLGEAQAVGPADAAYKPDDAQVAYHLARFIENVRSVSPDPVLVRQNWLRAYAFLTDRAAAKLNEYARGND
PFARAGKETVSVEVTSVVRASPDSFQVEWTETSRDRNGSLPSTERWTAILTIVLQPPRTEEQLRKNPLGL
YITDFSWSRELVQ
>gnl|CDD|442916 COG3702, VirB3, Type IV secretory pathway, VirB3 component [Intracellular trafficking, secretion, and vesicular transport]
EEDPLFKGLTRPAMFLGVPLVPFVLNVMVSLILFIWTGSLLYLLLAIPLHFVLRLICRRDPRFFRLLLLR
LRTRPRTRNRRFWGGNSYSPLPYRRRR
>gnl|CDD|442917 COG3703, ChaC2, Gamma-glutamylcyclotransferase ChaC2 (glutathione degradation) [Inorganic ion transport and metabolism]
ASLNRTLAGRPGGGDLWVFGYGSLIWNPGFEFVERRPARLHGWHRSFCLRSTVHRGTPERPGLVLGLDRG
GSCRGVAFRVPPEDAEAVLAYLWRREMVTGVYLPRWLPVRLADGRRVEALAFVADRDHPQYAGGLSLEEQ
ARIIAQAVGPSGSNADYLLNTAEHLRELGIRDPHLEALARLVRALLAAAT
>gnl|CDD|442918 COG3704, VirB6, Type IV secretory pathway, VirB6 component [Intracellular trafficking, secretion, and vesicular transport]
FFQDLLTALDNILNTFVTNAFSNLAGALTPILTALLTLYIILYGYAFLTGRIREPVSELVIRILKIALIL
ALALNWGFYQTYLFDLFTGGPDELAAAITGASGSGSTVASALDAVLSKLLSAASAIWDKAALLISGGILL
GLLGLIVLVGTLLLILVAVAVYLLAKIALALLLGLGPIFIAFLLFEATRRLFDGWLKQLLNYALQPVLVA
AVLALLLALIDSVLYALLGFSVNTDLLVAAAIGLLGGLALAVVVGLATALVSAASKGSASGGSGSGAAAG
GGAGGASSAAGAAPGRASSA
>gnl|CDD|442919 COG3705, HisZ, ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]
LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLQTFKLVDQLGRTLGLRPDMTPQ
VARIAATRLANRPGPLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGL
EDFTLDLGHVGLFRALLEALGLSEEQREELRRALARKDAVELEELLAELGLSEELAEALLALPELYGGEE
VLARARALLLDAAIRAALDELEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAYAPGVGDPLARGG
RYDGLLAAFGRARPATGFSLDLDRLLRALPAA
>gnl|CDD|442920 COG3706, PleD, Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription]
PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRAD
PRTADIPIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVARYGGEEFAILLPGTDLEGALA
VAERIREAVAELPSLRVTVSIGVAGDSLLKRADALYQAR
>gnl|CDD|442921 COG3707, AmiR, Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription]
MRGLRVLVVDDEPLRRADLREGLREAGYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQI
SEERPAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRELRALRRELAKLREALE
ERKLIERAKGILMERRGLSEDEAYRLLRKQAMDRRVKLAEVAEAILAAAELLKG
>gnl|CDD|442922 COG3708, YdeE, Predicted transcriptional regulator YdeE, contains AraC-type DNA-binding domain [Transcription]
MEYRIVEKPAFKLVGLSARTSNSDEEANEEIPALWQRFLPEGLAEIPNLSNPGGLYGVCTDYESDEGEFD
YLAGVEVSSFDEVPEGLETLEIPAGTYAVFTHKGPMPEALQETWQYIYSEWLPSSGYERADGPDFEVYDE
RDDPSPDSEVEIWIPIK
>gnl|CDD|442923 COG3709, PhnN, Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]
MSGPGRLIYVVGPSGAGKDSLLAAARARLAADPRLVFARRYITRPADAGGEDHDALSEAEFARRAAAGAF
ALHWQAHGLRYGIPAEIDAWLAAGRDVVVNGSRAVLPQARARYPRLLVVLITASPEVLAQRLAARGRESA
EEIEARLARAAEFLPDGPDVLVIDNDGPLEDAGARLLALLRAARARAA
>gnl|CDD|442924 COG3710, CadC1, DNA-binding winged helix-turn-helix (wHTH) domain [Transcription]
MRYRFGDFRLDPARRELLRDGEPVRLSPRAFDLLLLLLEHPGRVVSRDELLAAVWPGRVVSDNSLTQAIS
RLRKALGDDGLEPRLIRTVPRRGYRLVAPVEVEAPE
>gnl|CDD|442925 COG3711, BglG, Transcriptional antiterminator [Transcription]
ILKILLKNNNVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQKEKLLQLL
EKSEDPLSPKERVAYILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIK
LEGSELDIRKALAELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIA
IAIKRIKKGKYIKLDNPLLWEIKKPKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNELS
EIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFE
LAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKESKKKRVLVVCSSGIGTSRLLKSRLKKLFPEIE
IIDVISYRELEEIDLEDYDLIISTVPLEDKPVIVVSPLLTEEDIEKIRKFLKQIKKKLAKILFELLLLLL
LLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVIAIPIIIIIIIAIIVLAAEEPGVIK
LILVLLLLLILIILLEDDEALLVILLLLLLLIESSLLLLLLLELLLELELELLILLLL
>gnl|CDD|442926 COG3712, FecR, Periplasmic ferric-dicitrate binding protein FecR, regulates iron transport [Inorganic ion transport and metabolism, Signal transduction mechanisms]
MSAEDLDALLEEALSGEATAEEAALRARPSRRRLLRWLAAAAALALALAGLWLPTPLPALTADYRTATGE
RRTVTLPDGSRVWLNAGSALRYPVAFSGDEREVELLEGEAYFEVAKDPARPFIVHTGGGRVRVLGTRFNV
RADDDAVRVTVLEGKVRVSPGGAGQSVVLKPGQQAVFDADGKLAVSAVDAEAATAWRQGRLVFDNTPLAE
VLAELERYYGVKIVLADPALADLRVSGTFPLDDLDEVLEALALTLPIRYEREGDKIIIS
>gnl|CDD|442927 COG3713, OmpV, Outer membrane scaffolding protein for murein synthesis, MipA/OmpV family [Cell wall/membrane/envelope biogenesis]
MKRRLRLALLLALALLAAAPAAAQAEPSGDWELSLGAGAGVAPPYRGSDDYRVLPLPVISYRGDRFFADG
LDGLGYYLLDDDGFRLGLSLGYRPGRDSDDSDALRGLGDRDGTVEAGLFAEYRLTDWLRLRAELRTDVLG
VSNGLVADLGLSYRFRLGGRWTLTPGAGATWASSKYNDYYYGVSPAEAAASGLPAYDAGSGLKSPGLGLS
ATYRLTENWSLTAFARYTRLGGDAADSPLVDRRTQFTAGLGVSYRF
>gnl|CDD|442928 COG3714, YhhN, Uncharacterized membrane protein YhhN [Function unknown]
MKASRLLLLAFLLSALLYLDALYRGPRWLRWLFKPLTMLLLLLLAWQAPALSPYGYLILAGLLFSLLGDV
LLLLPGDRFLYGLGAFLLAHLLYIIAFLRQRRGLSFRWPLALLLLAIGAALLALLWPHLGELRIPVLVYI
LVILVMAWAAGERYFQLSTDSSFLVLAGALLFVLSDSLLAINRFRRPFPAAGLLIMATYFLAQFLIVRGL
LRHRA
>gnl|CDD|442929 COG3715, ManY, Phosphotransferase system, mannose/fructose/N-acetylgalactosamine-specific IIC component [Carbohydrate transport and metabolism]
MEISLIQAILIGLVAFLAGIDGLLGQFQLHRPLVAGLLVGLILGDVKTGLIIGATLQLIYLGVVNIGGAV
PPDPALAGIIGTALAILSGQDPETAIALAVPVGLLGQVLDILVRTINSFFVHKADKYAEEGNFKGIERLH
LLGPLLQFLLRAIPVFLALYFGADAVQALLNAIPAWLTHGLSVAGGMLPAVGFAMLLKMMGKKKLWPFFF
LGFVLAAYLKLPLLAIAIIGVAIALIYYQLKKKKNAAAAAASGDDDEDF
>gnl|CDD|442930 COG3716, ManZ, Phosphotransferase system, mannose/fructose/N-acetylgalactosamine-specific IID component [Carbohydrate transport and metabolism]
TTEEEKKLTKKDLRKVFWRSFFLQASWNYERMQALGFAYSMLPALKKLYKDKEELKEALKRHLEFFNTEP
QLGTFILGITAAMEEERANGADIDDEAINGIKTGLMGPLAGIGDSIFWGTLRPILGAIGASLALQGNILG
PILFLLLFNIIRFLIRYYLFKLGYKLGTKAITDLLEGGLLQKLTEGASILGLFVVGALIASYVKINTPLV
FSIGGVVITLQDILDKIMPGLLPLLLTLLVYWLLKKKVSPTKIILGLIVIGIVGSALGILA
>gnl|CDD|442931 COG3717, KduI, 5-keto 4-deoxyuronate isomerase [Carbohydrate transport and metabolism]
EVRYATHPDDVKRYDTEELREEFLIEDLFVPDEINLVYSHYDRMIVGGAVPVTKPLALETGDELGAEYFL
ERRELGIINIGGPGTVTVDGEEYELGNKDALYVGRGAKEVTFASADAANPAKFYLNSAPAHKAYPTKKIT
IADANPVELGSLETSNERTIYQYIHPDVVESCQLVMGMTELKPGSVWNTMPAHTHDRRMEVYFYFDLPED
QRVFHFMGEPQETRHLVVANEQAVISPPWSIHSGAGTSNYTFIWGMAGENQDYTDMDHVPMTDLR
>gnl|CDD|442932 COG3718, IolB, 5-deoxy-D-glucuronate isomerase [Carbohydrate transport and metabolism]
MSDLLIKPGSPADGGRVQDVTPESAGWEYVGFRVLRLAAGESLELETGDREVCLVLLSGKATVTVDGQTF
GELGGRMSVFEGPPDAVYVPPGSAFTVTAETDLEVAVCSAPAKGGLPARLIAPEDVPVELRGAGNNTRQV
HNILPPDFPADSLLVVEVITPGGNWSSYPPHKHDEDNPPEETYLEETYYHRLNPPQGFGFQRVYTDDRSL
DETMAVRDGDVVLVPRGYHPVAAAPGYDLYYLNVMAGPGRSWKFTDDPDHAWIRDTWAGQDVDPR
>gnl|CDD|442933 COG3719, RnaI, Ribonuclease I [Translation, ribosomal structure and biogenesis]
MRVPALRWLAALLLLLLAAAAAAAAAARGGRAGDFDYYVLALSWSPGFCATEGDARGKPQCRAGRAYGFV
LHGLWPQYERGWPSYCGTPEPALSRATRAALADVMPSAGLARHEWKKHGTCSGLSPDDYFALARRLREAV
NIPAVGRALNIGKTVTAAEVEAAFDAANPGLAPDAIAVTCRRGRLTEVRICLSKDLKPRPCGLADVRRGC
RAGFILVPPVRY
>gnl|CDD|442934 COG3720, HemS, Putative heme degradation protein [Inorganic ion transport and metabolism]
ATLYQRWRALRAENPKLRARDAAARLGISEAELLAARVGHGVTRLRPDWRALLPALEALGEVMALTRNES
AVHEKVGVYENVSLGGHAGLVLGPDIDLRLFLSHWAHGFAVEEETARGVRRSLQFFDAQGDAVHKVYLRE
ESDVAAWEALVARFRAEDQSPLLEVEPAPPPEAAKPDAEIDVAALRQEWRAMTDTHQFFGLLKKHGLSRL
QALRLAGDDLARRVDNDALRQLLEAAAADGLPIMVFVGNRGCIQIHTGPVEKVKPMGPWLNVLDPGFNLH
LREDHIAEAWVVRKPTKDGIVTSLELFDADGELIAQLFGQRKEGQPERAQWRELVEAL
>gnl|CDD|442935 COG3721, HugX, Putative heme iron utilization protein [Inorganic ion transport and metabolism]
MEELQQALRALLAENPDGVLEAIARELGVSELEVVAALPEEMATLVPGERFDEILQELAGWGEVTTIVHT
EDSIFEVKGPLPKGKHGHGYYNLHGKGGLHGHLKADNCAAIALVSRPFMGKESHSVQFFNAEGEAMFKIF
LGRDEKRQLLPEQVERFRALKA
>gnl|CDD|442936 COG3722, MtlR, DNA-binding transcriptional regulator, MltR family [Transcription]
EESMAFEDEILERLNEATTVRGFLIAAVELLAEAVDQLIQRVFRKDDYAVKYAVEPLLEGSGPLADLSVR
LKLLYGLGVISREEYEDIELLIALREELNHDGKEYRFTDDEILGPIKALHCVQDLPPLPLFPPADDKDSL
LYQMQQQRYEQMIRSTLILAITELIERLSVESPF
>gnl|CDD|442937 COG3723, RecT, Recombinational DNA repair protein RecT [Replication, recombination and repair]
MSNQLAKKATKKKPDTVKALLKQMKKEFELALPKHYSPERFLRSALTALQNTPALAKCDPTSILNALMQA
AQLGLEPNALGQAYLVPYGNTEVQFQIGYKGLIDLARRSGQIKSIYAHVVYEGDEFEYEPGLEKELEHKP
SFEGDRGEIIGAYAVAKLKDGGYKFEVMTKEQIEKHRDKSKAYKKKKSGPWKTDFEEMAKKTVIRRLLKY
LPLSSELQEAIAADESVEYDIRQDVDPVEAEEEGEAEAEAEAAENAEEGEEVDE
>gnl|CDD|442938 COG3724, AstB, Succinylarginine dihydrolase [Amino acid transport and metabolism]
KAFEVNFDGLVGPTHNYAGLSFGNVASTSNAGQVSNPREAALQGLAKMKALADLGFKQGVLPPQERPDLP
TLRRLGFSGSDAQVLAKAAKQAPALLSAASSASSMWTANAATVSPSADTADGRVHFTPANLNNKFHRSIE
APTTGRILRAIFADERHFAHHPALPQVAHFGDEGAANHTRLCADYGEPGVELFVYGRSAFDPSAPAPKRF
PARQTLEASQAVARLHGLDPDRVVFAQQNPAVIDAGVFHNDVIAVGNQNVLFYHEQAFLDQEAVLDELRA
KLGGLHFIEVPEAEVSVEDAVKSYLFNSQLLTLPDGSMALIAPEECRENPAVWAYLEELVASNNPIDEVK
YFDLRQSMRNGGGPACLRLRVVLTEAELAAVNPAVLLNDALFARLNDWVDRHYRDRLTPADLADPQLLDE
SRTALDELTQILGLGSIYPFQRA
>gnl|CDD|442939 COG3725, AmpE, Membrane protein AmpE required for beta-lactamase induction [Defense mechanisms]
MTLLTLLLALLLERLFKLGARWQRDHWFQRWLRRLERRPSLARWSSLLGLLLAVLLPVLVVALLLWLLSG
VLFGLLTLLLWVLVLLYCLGPGDLRADVRAYLKAARRGDRQAAYHMAEELLGIHGPADDSEEELLRQVQE
ALLWRNFRRYFAVLFWFVVLGPAGALLYRLLRLYARWLARHHLPAARSGADRLLHWLDWIPARLLALSYA
LVGNFVAALPAWRASLGDRHTSAADVLTAVARAALELDPEADDGARGVAELEAAVSLLKRALLVWLAVVA
LLTIAGWLV
>gnl|CDD|442940 COG3726, AhpA, Uncharacterized membrane protein Smp affecting hemolysin expression [Function unknown]
MMIKAKLKKRLHRTLIVLICLALLVILLQGASYFSLGSQLALSNQVENLARLLVRQAAFSASPLLVNNDK
NERLTALLNQLTKESRILDASVYDADGELLAQSGEALSVRDRLGLDGPLAGSYFRQQIVEPIFGKDGPLG
FLRVTLDTHVLATEQHQVDNTTNLLRLMLLLALLIGILLARTLLRFRRTRQSPFLLTASKPVKEEDEK
>gnl|CDD|442941 COG3727, Vsr, G:T-mismatch repair DNA endonuclease Vsr, very short patch repair protein [Replication, recombination and repair]
ADVLTPETRSRNMSAIRGKDTKPELALRRALHALGLRYRLHRKDLPGKPDIVFPKYRVAIFVHGCFWHGH
PGCRLATTPKTNTEFWRAKIERNVERDRRVNAALEAAGWRVLRVWECELKKKLALCVEALLERLEEWLRS
R
>gnl|CDD|442942 COG3728, XtmA, Phage terminase, small subunit [Mobilome: prophages, transposons]
KLTDKQERFCDEYLKDLNATQAAIRAGYSEKTASVIGSRLLKKPKIKAAIDELKKERAERTEITADEVLQ
RLTDIAFADITDYVEFGDDTLEVKKKIKLKDRLKALELLGKYYGLFTDKVEHKGEEDELED
>gnl|CDD|442943 COG3729, GsiB, General stress protein YciG, contains tandem KGG domains [General function prediction only]
MADTAKRGGSGVEKGNFAKDRERASEAGRKGGQHSGGNFANDPERASEAGRKGGQHSHGGKRSS
>gnl|CDD|442944 COG3730, SrlA, Phosphotransferase system sorbitol-specific IIC component [Carbohydrate transport and metabolism]
MDFLVKLAEGFIGLFQAGGETFVGLVTGILPTLIVLLTAMNALIKLIGEERVNKLAQKAGKNPITRYTVL
PVLAVFFLTNPMAYTFGRFLPEKYKPAFYDAAVSFCHPITGLFPHANPGELFVWLGIAAGITKLGLSLGD
LAIRYFLVGLVVILIRGIVTEFITAYVAKRQGITL
>gnl|CDD|442945 COG3731, SrlB, Phosphotransferase system sorbitol-specific IIA component [Carbohydrate transport and metabolism]
MIYQTTITEIGEEAADFLEEGMLILFGENAPDDLADYCVIHEVGELKGEIKVGDVLKIGGQEYTITAVGD
VANKNLRELGHITLKFDGATEAELPGTIHLEGKELPAIKVGTTITIE
>gnl|CDD|442946 COG3732, SrlE, Phosphotransferase system sorbitol-specific IIB component [Carbohydrate transport and metabolism]
MMMYKAVKIEKGSGGWGGPLVITPTEEKNKIVSVTGGGIPPVADKIAELTGAEAVDGFKTSVPDEEIACV
VIDCGGTARCGVYPKKRIPTINITPTGKSGPLAKYITEDIYVSGVKVDNISLADGEEEAAEATAAEEAAP
AQSAKKSKYDTAKKITEQTAKGGKDGLIAKIGRGMGKVVGTFYQAGRETIDTVIKTILPFMAFVSMLIGI
ILASGIGDWIANVLSPLAGNLIGLLIISLICSLPFLSPLLGPGAVIAQVIGVLIGVEIGKGNIPPQLALP
ALFAINTQVGCDFIPVGLSLGEAKPETVEVGVPAVLYSRFITGPPAVLIAWLASFGLYS
>gnl|CDD|442947 COG3733, TynA, Cu2+-containing amine oxidase [Secondary metabolites biosynthesis, transport and catabolism]
MTETLTGDLSAQAAAVPHPLDPLTAEEITAAVAILRAAGLLGETTRFASVELAEPPKAEVLAFEPGDPVD
RRAFVVLLDRATGATYEAVVSLTAGEVVSWEEIPGVQPPILLEEFEEAEEIVKADPRWQAALAKRGITDF
DLVMVDPWSAGYFGIPEERGRRLLRVLSFVRSDPEDNPYAHPIEGLVAVVDLNTMEVVRVEDHGVVPVPP
EPGNYDPELVGPLRTDLKPLEITQPEGPSFTVDGNEVSWQNWSFRVGFNPREGLVLHQVTYNDGGRERPI
LYRASLSEMVVPYGDPSPTHYWKNAFDAGEYGLGRLANSLELGCDCLGEIHYLDAVLADSDGEPVTIPNA
ICIHEEDYGVLWKHTDFRTGRAEVRRSRRLVVSFIATVGNYDYGFYWYFYQDGTIEVEVKLTGIVFTGAV
PPGEDPPYGTLVAPGLYAPNHQHFFNARLDMDVDGERNSVYEVDTVAVPIGPDNPYGNAFTTEATPLETE
SEAARDADPATGRYWKIVNPNKTNRLGEPVGYKLVPGGNPTLLADPDSSIAKRAGFATKHLWVTPYDPDE
RYAAGDYPNQSPGGAGLPAWTADDRSIENEDVVLWYTFGVTHVPRPEDWPVMPVDYAGFKLKPVGFFDRN
PALDVPPEPPAACHPG
>gnl|CDD|442948 COG3734, DgoK, 2-keto-3-deoxy-galactonokinase [Carbohydrate transport and metabolism]
MSTAPALIAVDWGTSNLRAWLLDADGQVLAERKSDAGILRLAPGGFEAALLELLGDWLAAAGDLPVVACG
MVGSRQGWVEAPYLPCPAGLADLAAGLVRVPLDPGLPVWIVPGLRQRSGGPPDVMRGEETQILGALALLP
EGDGLLCLPGTHSKWVRVDDGRITGFRTFMTGELFALLSQHSILGRSLPEDGAWDPAAFLAGVAAALSAA
GLLHALFSVRALGLLGGLSAEEAASYLSGLLIGAELAAARRYWGPGQPVTLVGSGALCALYARALEALGI
SVTLLDADDATLAGLWAIARALGLLA
>gnl|CDD|442949 COG3735, TraB, Uncharacterized conserved protein YbaP, TraB family [Function unknown]
MRRRLLLLLLAALLLLALAAAAAAAQAGPLLWKVSKGGKTSYLFGTIHVLDPRDYPLPPAVEEALAAADT
LVLELDPDDPDALALQALMKLMLLPDGKTLSDLLSPEEYARLEALLAALGLPLAALARLKPWFAALLLSL
AALQKAGLDPETGVDMYLLKLAKAAGKPVVGLETVEEQLALLDSLPEEEQAEMLRETLDELEKGEAQLET
LVDAWRAGDLAALEALLREDMAAYPEFYEALLDDRNRNWAPRIEALLKEPGTVFVAVGALHLPGEDGVLA
LLRARGYTVERVK
>gnl|CDD|442950 COG3736, VirB8, Type IV secretory pathway, component VirB8 [Intracellular trafficking, secretion, and vesicular transport]
MSNKAKPAEALKAYFAEARSWEADRYEKALRSRRRAWIVAGAALLLALLSVLAIAALLPLKTVEPYVVRV
DKSTGAVTVVTPLTEKQLTYNEAVDRYFLARYVRARESYDPATLQEDYDTVALLSSPDVQREYRALFSST
NPQSPDNVYGKGARRRVKILSISFLNDNTAQVRFTRTERDDTGGGTQTTHWIATITFRYVNAPLSEEDRL
INPLGFQVTSYRVDPEYLPN
>gnl|CDD|442951 COG3737, COG3737, Uncharacterized protein, contains Mth938-like domain [Function unknown]
MKLHLDHPPGRNTITAYGDGGFRINGMRYRGSLLVLPDGLVEDWPVTSFEDLTAAHLEPLLALKPEVVLL
GTGARQRFPPPALLAALREAGIGVEVMDTGAACRTYNILLAEGRRVAAALI
>gnl|CDD|442952 COG3738, YiijF, Uncharacterized conserved protein YijF, DUF1287 family [Function unknown]
MMRRLLLLALLALLLLSSLAFAQPNFAQKLVAAAREQTGVTVTYDPAYVSIDYPNGDVPADTGVCTDVVI
RAYRALGIDLQKLVHEDMKANFSAYPKIWGLKRTDRNIDHRRVPNLQTFFSRHGASLPISDNAADYQPGD
IVTWRLPGNLPHIGIVSDRKSADGRRPLVVHNIGAGPQEEDVLFDYKITGHYRYPPK
>gnl|CDD|442953 COG3739, YoaT, Uncharacterized membrane protein YoaT, DUF817 family [Function unknown]
MTSPASRLLARAPLRGLRRFLVEFLLFGLKQAWACLFGGLFFALLALTKLIWPGDAGLARYDFLLLAALL
IQILMLAFRLETWDELKVILLFHVVGTAMEIFKTSIGSWSYPEEGYLKIGGVPLFSGFMYAAVGSYIARA
WRLFDLRFTHYPPFWLTVLLALAIYLNFFTHHFIGDLRWVLFAAVVLLFWRTTVYFRVGRRRRRMPLLLA
FFLIAFFIWLAENIGTFFGAWQYPNQLGAWSLVHLGKLGSWFLLVIISFVIVALLKRPKARIHVPAPAA
>gnl|CDD|442954 COG3740, COG3740, Phage head maturation protease [Mobilome: prophages, transposons]
MEKPRKFAALEIRAVTDDDDGTIEGYASVFGSPSELDRFGEVIAPGAFAKSLAERGSDVPMLWQHDPAKP
LGRWDELREDDKGLRVEGRLLPDTPRARDVYALIKAGAIDGLSIGFRVVKDEWERDGGTGVRTILEVDLW
EVSVVTFPAYPDARVSARKSALEAAEAEALRLARALRRARALR
>gnl|CDD|442955 COG3741, HutG, N-formylglutamate amidohydrolase [Amino acid transport and metabolism]
MDPPFEVHRPTAQTSPLVLSSPHSGTDYPPDFLARLRLDARALRRDEDWHVDRLYDFAPALGATLLRANF
SRAVIDLNRDPDELDPYMFEGPRGQAGLGLIPRTTFDGEPIYRRRPDVAEAERRIERYWRPYHAALAALL
ARLRARFGYAVLIDCHSMPSVIPRLFGGRLPDFVLGDRDGASCAPALTAAVEAALAALGYSVVRNGPFKG
GYITRHYGRPARGVHALQIEIARRLYMDEAPFEPDPAGAARLRADLAALLAALAAWARSRAAE
>gnl|CDD|442956 COG3742, VapC, VapC family ribonuclease, contains PIN domain [Defense mechanisms]
MVVDTSALVAILLGEPEAEALAAALEAAPPRLISAVTVLEAAIVLARRRGPEARRELDALLAELGIEVVP
VDAAQARLAREAYRRYGKGRGHPARLNFGDCFAYALAKALGAPLLFKGDDFSHTDIEPA
>gnl|CDD|442957 COG3743, H3TH, Predicted 5' DNA nuclease, flap endonuclease-1-like, helix-3-turn-helix (H3TH) domain [Replication, recombination and repair]
AAAAAAGAAKPAALAAPRAGKADDLKKIKGIGPKIEKKLNELGIFTFAQIAAWTPEDIAWVDEELGGFKG
RIERDDWVEQAKLLAAGKWTEL
>gnl|CDD|442958 COG3744, COG3744, PIN domain nuclease, a component of toxin-antitoxin system (PIN domain) [Defense mechanisms]
MKLLLDTHALLWWLLGDERLSPAARELIEDPANELYVSAASLWEIAIKVRLGKLDLPEDLDEWLEELLEE
LGFELLPITPEHALAAAQLPLHHRDPFDRLLIAQALVEGLPLVTADRKIAAYGVKTIW
>gnl|CDD|442959 COG3745, CpaB, Flp pilus assembly protein CpaB [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
MKLKRLLLLLLALLLALLAAFLARRYLSGAEAPAAAAVPTVPVVVAARDIPAGTPLTADDLAVVEWPADA
VPEGAFTDPEELVGRVARVPIEAGEPILASKLAAPGERGGLSAVLPPGMRAVTVPVDEVSGVGGFLRPGD
RVDVILTLRSDDGGDGGQTVTRTLLQNVRVLAVGQTAGEDAAEGKPAVARTVTLEVTPEQAEKLALAQST
GTLSLALRNPDDEAPVDTAGVDLADLLGEPARAAPAAAPVRVIGAEVEV
>gnl|CDD|442960 COG3746, OprP, Phosphate-selective porin [Inorganic ion transport and metabolism]
AAAAADGVKVKFKEGGLEIKSADGGFSFKLGGRLQADYGGFDGDNTNGGDLGDGFELRRARLGFEGKLFK
DWDYKLEYDFAGNSGGTVGLLDAYLGYKGLPPLRLRVGQFKEPFGLERLTSSNYLTFMERSLATDAFAPN
RRLGVGLSGRLGDLNWTLAAGVFGGDGGGDSDGDDGKGVAGRVTWAPINSAGEVLHLGASGSYRDPDGDA
SLRFRSRPEARLTGTRFVDTGVIAGADSVTRYGLEAAWVYGPFSLQGEYYRSTVDRDGGGPDLTFDGWYV
QASYFLTGESRPYNRKGGVFGRVKPKHPFGKGGWGAWELAARYSHLDLNDGGIRGGRQDAWTLGLNWYLN
PNVRFMLNYIHADFDRPANGGGDGDDGDAFGLRAQVDF
>gnl|CDD|442961 COG3747, COG3747, Phage terminase, small subunit [Mobilome: prophages, transposons]
RGRKPKPTALKLLKGNPGKREINKREPKPPTDVPEPPKWLSEEAKKEWKRIAPELIAMGILTNLDLAALA
AYCQAYARYREAEEEIAEEGLTYETESGYLKKNPAVAIKNDATKQMRRLAAELGLTPASRARLAIPKPQE
EEEDDPFA
>gnl|CDD|442962 COG3748, COG3748, Uncharacterized membrane protein [Function unknown]
MEAYLLEWLNLLLRWLHVITAIAWIGSSFYFVWLDNSLRPPPDLLPKGVGGELWAVHGGGFYHVQKYLVA
PAQLPEHLHWFKWEAYTTWLSGFALLVVVYYFGAELYLIDPSVADLSPWQAIAISLGSLVAGWLVYDGLC
RSPLGRRDTLLGALLFVLLVAAAWGATQVFSGRAAFLHVGAMIATIMSANVFFVIIPGQRKVVAALKAGR
TPDPKYGKRAKQRSVHNNYFTLPVLFLMLSNHYPLTYAHPYNWLILALIFLAGALIRHFFNLRHAGKGKP
WWLWAGAALLLALIVWLAPKPDPAEAAAAAAAAAAVSFAQVQAIVQQRCSMCHAAEPTWEGFAAAPKGVM
LDTPEQIARHAQRIYQQAVVSKAMPLGNVTQMTDEERALLGAWIEAGARG
>gnl|CDD|442963 COG3749, COG3749, Uncharacterized conserved protein, DUF934 family [Function unknown]
MPKLIKDGQIVDDDWTLLRDDEPLPEGKVIVPLARWLAERDALLARNGPLGVWLAPDDDVEELAPDLDRL
ALIAVDFPKFTDGRGYSQARLLRERYGYTGELRAVGDVLRDQLFYMLRCGFDAFELRADQDLEAALAALN
DFSVAYQPAVDEPRPLFRRRA
>gnl|CDD|442964 COG3750, COG3750, Uncharacterized conserved protein, UPF0335 family [Function unknown]
MSDAGGVAADQLRSFIERIERLEEEKKAIADDIKEVYAEAKGNGFDVKVLRQIIRLRKMDPDEREEEEAL
LDLYKAALGMA
>gnl|CDD|442965 COG3751, EGL9, Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones]
AALADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAGIGRGLDHQVNEWIRRDSILWLDEKLA
SAAQARYLAALEELREALNSPLFLGLFEYEGHFARYPPGGFYKRHLDAFRGDLNRRLSLVLYLNPDWQPE
WGGELELYDDDGSEEEVTVAPRFNRLVLFLSEEFPHEVLPVGRERLSIAGWFRTR
>gnl|CDD|442966 COG3752, COG3752, Steroid 5-alpha reductase family enzyme [General function prediction only]
MTMSLLSLLLLALAALLAVMLLAWLVSLRTRNASIVDVAWSLGFVLVALVYALLGDGDDARRLLVAALVT
LWGLRLGGHLARRNRGKGEDPRYAALRERWGRGFALFSLFFVFLLQALLVWLVSLPVLAAAASPAPAPLG
WLDVLGAALWLVGFAFEAVADAQLARFKADPANKGKVCDTGLWRYSRHPNYFGEWLVWWGLALFALAAPP
GWWTLIGPLLMTLLLLKVSGIPLLEKHMLESRPAYREYQRRTSAFFPWPPKRSR
>gnl|CDD|442967 COG3753, YidB, Uncharacterized conserved protein YidB, DUF937 family [Function unknown]
GLLDSLLGAALGGAGQSGLLQALLQLLEQQGGLGGLLEKFQQGGLGDIVQSWVGTGENQPISADQLEQAL
GSDTLQQLASKTGLDPDEALSALAQLLPQAVDKLTPNGELPDAGDLAGGLGLL
>gnl|CDD|442968 COG3754, RgpF, Lipopolysaccharide biosynthesis protein [Cell wall/membrane/envelope biogenesis]
MRRVALFAFYLPQADELLLTNDSIFGPIAPLSPLFDRMEPENDDWWGLGEWTNKPLFPGHLQSYFLVFRK
RALASPAFRDFWYDLRLIEDKDDVIRRYEAGLARALGIAGFCYHYWFDGKRLRTRLLERPWDELLENGGF
PFLKRELLRDPS
>gnl|CDD|442969 COG3755, YecT, Uncharacterized conserved protein YecT, DUF1311 family [Function unknown]
MKKLLLLALLLLASLSALAQAADCDNAQTQAEMNACAAKEYQKADKELNKAYKALMKRLSAPEAKAALRK
AQRAWIKYRDAECAFAAAAYEGGSIAPLAYASCLARLTQERTKELESLLEC
>gnl|CDD|442970 COG3756, YdaU, Uncharacterized conserved protein YdaU, DUF1376 family [Function unknown]
SAMPYYPLYIGDYLADTRHLSAEEHGIYLLLLDAYWARGGPLPDDDARLARLIGARSPEEWAAVEAVLAE
FFELRDGGWRNHRLEEEIAKARAKAEKRSEAGRKGARKRQKKKEADRQSNADAF
>gnl|CDD|442971 COG3757, Acm, Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis]
LLALGGAAYPVHGIDVSHYQGDIDWAAVKAAGIDFAYIKATEGTDYVDPKFARNWAGARAAGLPRGAYHF
FRPCSDAAAQADNFISTVPRDPGDLPPVLDLEENGYYGLSPAQLRAWLKAFLDEVEAHTGRKPIIYTSPS
FYNDYLGNSDFSDYPLWIARYGSSPGYLPGRNWTFWQYTSSGRVPGISGNVDLNVFNGSRDELKALAL
>gnl|CDD|442972 COG3758, Ves, Various environmental stresses-induced protein Ves (function unknown) [Function unknown]
MSMRILRAADLPRMPWKNGGGETREIARFPEGAGLDDFDWRLSIATVAQDGPFSAFPGIDRTITLLEGDG
LRLTVDGQGEHTLDEPFQPFAFSGDAPVSARLLGGPVRDFNLMTRRGRARARVRVLRLAGTLPLHADAGT
GLLYVLAGAWTVALGGEAITLEAGDTLLLEAPAPLLTLTPLSGDGRLLLVELTPRA
>gnl|CDD|442973 COG3759, COG3759, Uncharacterized membrane protein [Function unknown]
MSILALILIALVALLHVYILVLEMFAWTTPRGRKVFGLTPEFAEATKVLAANQGLYNGFLAAGLIWGLFL
GDPAAGFALVLFFLGCVVVAGIYGALTASRKILLVQGLPALLALVLLLLA
>gnl|CDD|442974 COG3760, ProX, Predicted aminoacyl-tRNA deacylase, YbaK-like aminoacyl-tRNA editing domain [General function prediction only]
PLTEQELYALLDELGIPYETVEHPPVFTVEEAEALRGDLPGAHTKNLFLRDKKGTRFYLVVVPEDKRVDL
KALSKQLGSGRLSFASPERLEEYLGVTPGSVTPFGLINDTENRVTVVLDADLLEAELINCHPLVNTATLK
ISTDDLLRFLEATGHEPLIIDL
>gnl|CDD|442975 COG3761, NDUFA12, NADH:ubiquinone oxidoreductase NDUFA12 subunit (Leigh syndrome) [Energy production and conversion]. NADH:ubiquinone oxidoreductase NDUFA12 subunit (Leigh syndrome) is part of the Pathway/BioSystem: NADH dehydrogenase
MSFLLRIFTWWNGQTLGTRLFTWRKGEKVGEDEFGNRYYRTKDGKALGRERRWVIYNGYAEASRVPPEWH
GWLHHTTDEPPTEEPYPPRPWEKPHQPNLTGTPLAYRPKGSLLRGGRRPAATGDYEAWTPEA
>gnl|CDD|442976 COG3762, COG3762, Uncharacterized membrane protein [Function unknown]
FLSPAELARIEAAIAAAERRTSGEIRVVIERRSPLRRLLRRADARERALEVFLELGMWDTEDRNGVLIYV
SLAEHRVEIVADRGINAKVPQAFWQEIVDAMTAHFRQGRFAEGLVAAIEAVGELLAEHFPAQEDDVNELP
DEIVVL
>gnl|CDD|442977 COG3763, YneF, Uncharacterized conserved protein YneF, UPF0154 family [Function unknown]
MSTWLWILIIIVALLAGLAGGFFIARKYMKKYLKKNPPINEDMIRAMMMQMGQKPSEKKINQMMNQMKKQ
K
>gnl|CDD|442978 COG3764, SrtA, Sortase (surface protein transpeptidase) [Cell wall/membrane/envelope biogenesis]
RRVLGELLILAGLIGRLEIPKIGVDLPIVEGTDEDTLAKGAGHYPGTALPGEVGNAVLAGHRDTPGGTVF
RRLDELKPGDEIYVETADGTYTYRVTSIEVVDPDDVEVLAPTGKPLLTLITCTPFGSNTDRLIVYAELVS
TTPK
>gnl|CDD|442979 COG3765, WzzB, LPS O-antigen chain length determinant protein, WzzB/FepE family [Cell wall/membrane/envelope biogenesis]
MSSEESKQLYPNQYPPSQDDEIDLFELLRTLWQGKLWIIGITLLFALLALVYAFLLPQKWTSTAIVDPPT
VNELGGYYSQRQFLRNLDVKSVDPPVISSELFNEFIKQLSSYDLRREFLLQSDYYKQLQEGDEKEDAALL
DELINNISITPPDDKKKSSPYTNYSVSFTAETPEDAQQLLRGYIDFANQRVLKELNEELQGAIAARLQSL
KAQIKRLEEVAKAQRQRRIERLKYALKIAQAAGIKKPVYSNGQTPAVKLDPSYLFLLGTDALQAELEILK
ARGDDYPLNADLYQLQAQLAQLNALPIDDVGFQPFRYLRTPEEPVKKDKPKRALILVLGALLGGMLGVGV
VLIRHALRSRKKAK
>gnl|CDD|442980 COG3766, YjfL, Uncharacterized membrane protein YjfL, UPF0719 family [Function unknown]
MMFLLAGLLAFLLYFAVALLLLIVFLAVYELITPYKEWELIRQGNLAAALALGGALIGFAIPLASAIAHS
VSLLDFLIWGVVALVVQLLAYFLVRLLTPDLSEEIEEGNVAAGILLGAISIAVGLLNAACMTY
>gnl|CDD|442981 COG3767, COG3767, Uncharacterized low-complexity protein [Function unknown]
MKKNTKKPLALALGAALAASAAASPASAAENPFAMQELSSGYQLAEAEKKAAEGKCGEGKCGADKKKKKE
GKCGEGKCGADKKGDAKAAEGKCGEGKCGAKK
>gnl|CDD|442982 COG3768, YcjF, Uncharacterized membrane protein YcjF, UPF0283 family [Function unknown]
MSEEPKKPRAFDLDDAPEPAAAPLVPEQTFEDDAFIEEPEGDAAEPPAALAPRRRSRWGRLFWGALGALV
SLAVGLAAVDFIRDLFARSDWLGWAALALAALAVLALLGILLRELRGLRRLRRIDRLRERAAAALASDDL
GAARAFCEKLAALYGGRPDTAPGRARLQEHLGDIHDDRELLRLAERELLAPLDAQARREISRAAREVAVV
TAVSPLALVDMAFVLWRNLRMIRRIAELYGGRPGYLGRLRLFRAVLAHLAVTGASAVGDDLGQQVLGHGL
AAKLSARLGEGVGNGLLTARLGIAAMEVCRPLPFTADERPKLGDFRKELLTGLKKKKKK
>gnl|CDD|442983 COG3769, YedP, Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and metabolism]
MPPLLVFTDLDGTLLDHDTYSWAAALPALARLKARGIPVILNTSKTAAEVEPLRQELGLSDPFIVENGAA
IFIPKGYFAFPSGTADIDGYWVIELGKPYAEIRAVLEQLREELGFKFTGFGDMSAEEVAELTGLSLEQAA
LAKQREFSEPLLWLGSDEALERFIAALAALGLTVLRGGRFLHLMGGADKGKAVRWLVEQYRQRFGKNVVT
IALGDSPNDIPMLEAADIAVVIRSPHGAPPELEDKPRVIRTPAPGPEGWNEAILDLLE
>gnl|CDD|442984 COG3770, MepA, Murein endopeptidase MepA (D-alanyl-D-alanine-endopeptidase) [Cell wall/membrane/envelope biogenesis]
MKRLLLAALALALLAGLANAAAAATPAKQLFGAVTTPSAGAPQAIGSYANGCLAGAVALPEDGPGWQVMR
LSRNRNWGHPELIAFLERLSRKAAQQGWPGLLVGDMSQPRGGPMLSGHASHQIGLDADIWLTPMPRRRLS
RAERENISAISMVRADGLRVDPRNWTPQHAALIKLAASDPRVARIFVNPAIKKALCRTAGGDRSWLRKVR
PWWGHDYHFHVRLRCPAGSPGCEDQAPPPAGDGCGAELAWWFSDELNKPKPKKPKPPPKPRPLTLADLPA
ACQAVLAA
>gnl|CDD|442985 COG3771, YciS, Lipopolysaccharide assembly protein YciS/LapA, DUF1049 family [Function unknown]
MKYILIFLLVLAIFIIALTLGAQNDQVVTFNYLIAQGEFRLSTLLAILFGAGFILGWLICGLFYLRLKLK
LRRLKRKLKRLEQQLEELRTSPVKDS
>gnl|CDD|442986 COG3772, RrrD, Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis]
MMKTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHTGKDVKPGDTITEEEAEALLAADLAKAEAAVRRL
VKVPLTQNQFDALVSFAYNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERAL
CLGGLY
>gnl|CDD|442987 COG3773, CwlJ, Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, chromosome partitioning, Cell wall/membrane/envelope biogenesis]
IAYSDSDLDLLARAIYAEARGEPYEGQVAVAAVVLNRVRSPRFPNTICGVVYQPGQFSPVCDGQINRPPE
EEARRAARDALNGWRRDPTGGALYFHNPATVTPSWARSRPKTARIGNHVFYRPR
>gnl|CDD|442988 COG3774, OCH1, Mannosyltransferase OCH1 or related enzyme [Cell wall/membrane/envelope biogenesis]
PMIPKIIHQTWFGDKELPELVQRCIASWKKLNPDWEYRLWDDENFDDFIKEHGPEYLEAYYKLKKGAARA
DLFRLLLLYKYGGIYLDIDVECLKPLDPLLDGDDLFLGYEDPPPGIISNGFIAAEPGHPFLKKALE
>gnl|CDD|442989 COG3775, SgcC, Phosphotransferase system, galactitol-specific IIC component [Carbohydrate transport and metabolism]
MDIILEIFQYILDLGAAVMLPIIIFIIGLILGVKPKKAFRSGLTVGIGFIGINLVIGLLTDSLGPAAQAM
VENTGLNLPVIDVGWPAAAAIAWGSPVGLIIIPLGIIVNIIMLLLKWTKTLNVDIWNYWHFAFTGALVYA
VTGSLILGLAAAAIQAVIELKLADWTAPRVQKYYGLPGISIPHGMSASFAPIAIPLNKLLDKIPGLNKIK
IDPETLQKKFGIFGEPMVIGFILGLLIGILAGYDVKKILTLGITLAAVMVLFPRMVKLFMEGLLPISEAA
REFMKKRFKGRELYIGLDSAVLVGHPATLSTALLLIPITLLLAVILPGNKVLPFADLANIPFMVAMAVPV
TKGNIFRMLIIGIIVLPIGLYIATALAPLFTELAKSAGFAIPEGASLISSLSDGGPPFTWLIVKAFSLLN
IIGIGVLVIIYLGLAWYYRKKRKRNYLKEAA
>gnl|CDD|442990 COG3776, YhhL, Uncharacterized conserved protein YhhL, DUF1145 family [Function unknown]
MLINLGRLLMLFVWGFLLLNLVHPFPKPLNIFLNVALGFMVLMHGLQLLLLKGTLPKDGPKLSKWDQLRI
FLFGVFELLAWQKKLKAQQKA
>gnl|CDD|442991 COG3777, HTD2, Hydroxyacyl-ACP dehydratase HTD2, hotdog domain [Lipid transport and metabolism]
MALDLEHLRDWIGRTETRTDVITPALARRLAATLDRDPPAPAAGDPLPPLWHWCYFLPAAPQSELGPDGH
PARGGFLPPVPLPRRMWAGGRLEFHAPLRVGDEVTRTSTIADVTEKEGRSGPLVFVTVRHEISQDGGLAL
TEEQDIVYREAPAPGAPPPPPPAAPPAAAWSRTVTPDPVLLFRYSALTFNGHRIHYDRPYATEVEGYPGL
VVHGPLQATLLLELARRAPGRRPARFSFRGVSPLFDGEPFTLNGRPTGDGAAELWARDPDGRLAMQAEAE
L
>gnl|CDD|442992 COG3778, YmfQ, Uncharacterized conserved protein YmfQ in lambdoid prophage, DUF2313 family [Mobilome: prophages, transposons]
TAEDYAAALLALLPPGSAWPRDNGPVLAALLAGLAPALARVDARADDLLGEADPRTAVELLPDWERVLGL
PDPCAGGAQTLQERRAAVVAKLTATGGLSIPYFIRLAASLGYTITITEYRPFRAGLSRCGDPLYPEDWRF
AWRVNVPGVTVTRFRTGQSAAGEPLRVWGDAVLECLLRRLKPAHTVVIFAYEE
>gnl|CDD|442993 COG3779, YegJ, Uncharacterized conserved protein YegJ, DUF2314 family [Function unknown]
MKKLRLLLLLKTAVARRMDDDPIVLVAGDDPAMNAAIEKARATLDYFWRELSWEIVPALDLFAVKVAFAQ
EDGPGVEHMWITDVNFDGDTISGTLANEPGYLTNVRAGDPVSFPRDDISDWMYVRDGKMYGGFTIRAMRK
GMSAEEAAEHDAAWGLDF
>gnl|CDD|442994 COG3780, COG3780, DNA endonuclease related to intein-encoded endonucleases [Replication, recombination and repair]
MRRLRELSQEELEEAIDYVQELREEGLSYSQIISEIEKELGVKISKSTVSRWCKGIHSPFNKIKIVNLSP
SPDLAYIIGVYFGDGSITADEGYKYRIRLKVVDKEFAEAFANALKRIGANPPEPFPNRDGRWVVEASSKV
LYQFLKKPKEELFEVAERYPAEFLRGFFDSEGCVVSAKKDKRGYITVYNYDLELLEFVRYLLKKLGIEST
IYLPKKKGTEVPIRGKTYHYNKDYYELRIYRRESIETFYNKIGFTIERKKQRLEEYLRRLGRL
>gnl|CDD|442995 COG3781, YneE, Predicted membrane chloride channel, bestrophin family [Inorganic ion transport and metabolism]
MIVRKRPNWFRLLFVLRGSVLPKILPRLLLLLLLSVLVVLLYQVLFGLWVSLPIAPFTLLGTALALFLGF
RNNAAYDRWWEARKLWGALVNDSRNLARQVLALLPDEEDREERRRLVRRLIAFAHALRHHLRGEDPWEEL
ERLLPAEELERLKAAKNPPNAILLLIGRELAELRRRGRIDDIQLLALDRTLNELSDIQGGCERIKNTPIP
FAYSLLLHRFVYLFCLLLPFGLVDSLGWLTPPVVALIAYTFFGLEAIGEELEDPFGNDPNDLPLDAICRT
IEINLLEMLGETDLPPPLQPVNGVLL
>gnl|CDD|442996 COG3782, COG3782, Uncharacterized conserved protein, DUF1853 domain [Function unknown]
MPTNHLRHPLVRDLAWLLLSPPLLDGADAFHPALPLPAALLAWLQQLDRDPAPLLAHLAIPKSLRLGHYF
ERLWAFALEHAPDYELLAHNLQIRDGKRTLGELDFLLRDDNGQLIHLELAIKFYLGDPSGSNEIDRWIGP
NRKDRLDLKLEKLKEHQLPLSHHPEAQQALAALGLEVIKQQALFKGQLFYPYGDTNALPAPLNPDHLRGF
WIRLSDFPALFPASRWYILPKLDWLAPPRTNVAWLSFAELLALLEDHFAAKTSPVDGTWLEKSRGFVVPD
WWPERA
>gnl|CDD|442997 COG3783, CybC, Soluble cytochrome b562 [Energy production and conversion]
MRKTLLALLAVSLLLFSSAAFAADVEDDMDTMAKNYKTVLKADDAAEFKQALTKMRAAALDAKKGTPPKL
EGKAPDSPEMKDYRHGMDKLIGQIDQALKLADAGKLDEAKAAAEKLKDTRNEYHKKYR
>gnl|CDD|442998 COG3784, YdbL, Uncharacterized conserved protein YdbL, DUF1318 family [Function unknown]
MKKLLAILFLLLLLALLLLSAPAFALTPALDEAKAQGLVGETPDGYLGVVKADPAEAQALVAAINADRKA
VYQEIAAKNGITLEEVAKLAGQKLIERAPPGEYVQGINGQWVKK
>gnl|CDD|442999 COG3785, HspQ, Heat shock protein HspQ [Posttranslational modification, protein turnover, chaperones]
MKMIAAKFGIGQVVRHRLFGFRGVIFDVDPEFSNTEEWYEAIPEDRPLKDQPWYHLLAENEESPYHAYVS
EQNLVPDESGEPVEHPQLDELFESIRDGLYAPRLRLN
>gnl|CDD|443000 COG3786, COG3786, L,D-peptidoglycan transpeptidase YkuD, ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope biogenesis]
MRRLLAAAAPADAQQLIVVTAPPWDSTRATLRFERDGGRPFPCALGRGGITADKREGDGATPAGVFRLRG
AFGRADRARPGTALPYRPITPDDGWCDDPASPDYNRPVRLPFPASHERLRRDDPLYDLVVVIDHNDDPRV
PGRGSAIFLHVWRPGGGPTAGCVALSRADLRRLLAWLDPGTRPVIVLLP
>gnl|CDD|443001 COG3787, YhbP, Uncharacterized conserved protein YhbP, UPF0306 family [Function unknown]
MMDDLLARISRFLAKQHVLTLATTSDDGPWCANVFYAFDEDNLRLYFLSSPDTRHGQNMAENPRVAGTIF
GQPKTVALIKGVQFEGEARLLEGEEEERARALYYRRFPFARAMKAPLWRLRLDELKMTDNRLGFGKKLEW
QRDSGR
>gnl|CDD|443002 COG3788, YecN, Uncharacterized membrane protein YecN, MAPEG domain [Function unknown]
MTLPITALYAALLALLLLVLSLRVVRLRRKYRVALGDGGDPELQRAIRAHGNFVEYVPLALILLLLLELN
GAPAWWLHLLGIALLLGRLLHAYGLSRSKGPSPGRAIGMLLTFLVLLALAVLLLVYLLGGL
>gnl|CDD|443003 COG3789, YjfI, Uncharacterized conserved protein YjfI, DUF2170 family [Function unknown]
RMTMWTIHELADALNGSALFTGGEFDCEPIDGEEPVLQVTMSEYGDLPIFVTVTGEQILVETYLWPEDEV
KDRAEFNEALLRLNKLMPLSSFGIETVKGGDYYVLFGALSASSSLEDIVHEIETLADNAIDAAEALEEYL
KE
>gnl|CDD|443004 COG3790, YbgE, Predicted membrane protein, encoded in cydAB operon [Function unknown]
MSDMIDSLYQLTDKGPLRALSLILALALAGCVLWDPSRFAARTGGLSHWLGLLLIWAVCAGFIHGVGFRP
RRWLWRLLFSPLLAYLILIAGLYYFFLG
>gnl|CDD|443005 COG3791, COG3791, Uncharacterized conserved protein [Function unknown]
MMTLTGSCLCGAVRFEVDGPPLRVGACHCSICRKATGSAFAAVALVPADAFRLTSGEDALTTYRSSATAE
RHFCPTCGSPLFYRRRGGPGLVAVNAGLLDDPDGLPPTAHIFTSSKPPWVEIPDGLPQFEGL
>gnl|CDD|443006 COG3792, COG3792, Uncharacterized conserved protein, DUF596 domain [Function unknown]
DRILEASFGLPLSALWGYIKDAYGGDSDSFEERKEDFFFLLEELLDDGKLKLASHGKFLEGTTEEQVERF
RKAWPDSEEELEYDIDGLWFFTECPGGAVWILEDGYEE
>gnl|CDD|443007 COG3793, TerB, Tellurite resistance protein TerB [Inorganic ion transport and metabolism]
AELTSEVKRFSPNREFLEALVAGCALVAAADGDIDPEERQKIAALIQSLPELAPFDADELIAAFEAIVDL
LEFRAEALEELAKLLKGDPELAELVLRLAVDVAAADGVFDPEEKAVLEEICQALGLDP
>gnl|CDD|443008 COG3794, PetE, Plastocyanin [Energy production and conversion]
MAFEPATLTVKPGDTVTWVNTDSVPHNVTSDDGPDGAFDSGLLAPGETFSVTFDEPGTYDYYCTPHPWMV
GTIVVG
>gnl|CDD|443009 COG3795, YCII, 5-chloro-2-hydroxyhydroquinone dehydrochlorinase TtfG, YCII superfamily [Secondary metabolites biosynthesis, transport and catabolism]
MKYLLLIYADEEAEAGLSPEEMEALMAAMGAFNEELAAAGVLVAGEGLQPPSTATTVRVRDGKPVVTDGP
FAETKELLGGFYLIEVEDLDEAVEWAARCPAARGGGTVEVRPVMEAPD
>gnl|CDD|443010 COG3797, COG3797, Uncharacterized conserved protein, DUF1697 family [Function unknown]
MTTYIALLRGINVGGKNKVPMADLRALLEELGFTDVRTYIQSGNVVFSSDETDAAELAARIEAAIEERFG
FDVPVIVRTAEELRAILAANPFPAAADDDPKRLYVTFLSEPPDAEAVEALEALDAGPERVAVGGRALYLY
YPDGYGKSKLTNALLEKKLGVPATTRNWNTVRKLLELAEA
>gnl|CDD|443011 COG3798, COG3798, Uncharacterized conserved protein, DUF2171 domain [Function unknown]
MIDASQIKEHMEVVGSDGVHVGTVDHVEGDRIKLTKDDSHDGQHHYIPLSWVASVEGDKVRLSRTAEEAV
AQWEEEP
>gnl|CDD|443012 COG3799, Mal, Methylaspartate ammonia-lyase [Amino acid transport and metabolism]
MKIKDVLASPGLTGFYFDDQKAIKAGAKHDGFTYVGEPVTPGFTSIRQPGESISVMLILEDGQVAYGDCA
AVQYSGAGGRDPLFLAEDFIPVIEKEIAPRLIGRDLTSFRELAEEFDELRIDGKRLHTAIRYGVSQALLD
AVAKARKTTMAEVIADEYGTPLALEPVPIFAQSGDDRYTNADKMILKGVDVLPHGLINNVEEKLGKDGEK
LLEYVKWLKDRIRELGGPDYKPVFHIDVYGTIGLAFDNDVDRMADYLARLEEAAAPFKLRIEGPMDAGSR
EAQIEALAALREELDDRGVKVEIVADEWCNTLEDIKAFVDAGAADMVQIKTPDLGGINNSIEAVLYCKEK
GVGAYLGGTCNETDRSAQVCVHVALATGADQMLAKPGMGVDEGLMIVYNEMNRTLALLKARKT
>gnl|CDD|443013 COG3800, COG3800, Predicted transcriptional regulator [General function prediction only]
LQLLAKLLGLSLSYLNLIENLKKNPRALLLLLLAELLLVDYDDLVSLLLDLLLALLALLLDSLLLDELPL
ELFGLLLALLAAAAAAAPAALAAALRAAAERAAAYALGREGASAEPFPLEEVRDFFEAHDNYFPELDEAA
EALAAELGLDPGDLYAALAERLRERHGITVRILPLEALGGLLRRYDPHRRTLLLSERLDPAQRAFQLAHQ
LALLEQGDLIDALLASAGFSSEEARRLARIGLANYFAGALLMPYGRFLRAAEALRYDIELLARRFGVSFE
QVCHRLTTLQRPGARGVPFFFLRVDRAGNISKRFSATGFHFARFGGACPLWNVHEAFETPGRILTQLAEM
PDGRRYLCIARTVSRPGGGYGAPGRRFAIGLGCEIRHAGRLVYADGLDLDDPAAATPIGVGCRLCERPDC
PQRAFPPLGRRLKVDENRRGVSPYRFA
>gnl|CDD|443014 COG3801, COG3801, Uncharacterized conserved protein [Function unknown]
MATVDDVRRLALALPEVEEGTSYGTPAFRVRGKVFARLGPDGDTLVLKADLDEREALVAADPDVFFTTPH
YGGYPWVLVRLDRVDPDELRELLEEAWRLVAPKRLAAALDAAAP
>gnl|CDD|443015 COG3802, GguC, Uncharacterized conserved protein GguC, FAA hydrolase family [Function unknown]
MRLIQFRDADGQRRVALVEGGAARLLNGAASTYELALAAIAAGRSLAALVEARGLGEAVDYAALLAEGRL
LPPIDHPDPAHLLVTGTGLTHLGSADTRDAMHAKAQADEEELTDSMKMFRMGLEGGKPAAGQVGVQPEWF
YKGDGSIVVAPGAPLPSPAFALDGGEEPEIAGLYVIGPDGTPYRLGFALGNEFSDHVTERQNYLYLAHSK
LRPCSFGPELLVGELPAHVEGTSRILRDGEVLWEKPFLSGEANMSHSLANLEHHHFKYALFRRPGDVHVH
FFGTATLSFADGIRTQPGDVFEIEAPPFGLPLRNPLAVAAAEAAPVTVKAL
>gnl|CDD|443016 COG3803, COG3803, Uncharacterized conserved protein, DUF924 family [Function unknown]
MMATPQEVLDFWFGEAGPKLWFAKDPAFDAEIRERFLALHEAAAAGELDHWRETPEGRLALIILLDQFPR
NIFRGTPRAFATDALALALAQEAIARGFDRALPPVERAFFYLPFMHSESLADQERAVALFEALGDEADNL
DYARRHRDIIARFGRFPHRNAILGRESTPEELAFLAQPGSS
>gnl|CDD|443017 COG3804, COG3804, Uncharacterized conserved protein [Function unknown]
KIRVVQWGTGNMGRGAIRAILAHPGLELVGAIDHSPAKVGKDAGELAGLGRPLGVKATDDADAVLALDAD
VVVYATDSRLEEAVDDLERLLEAGVNVVTTAEELAYPWATSPELAARLDAAAKEGGVTLLGTGINPGFVN
DLLPLALTGLCRRIDKIRVQEIVDLSTYGEALAEAMGFGLTPEEFEEGIAAGPGVGHVGFGESVRMIADA
LGLELDEIEESLEPIVAEEDIETAGGTIPAGTVAGMRFTVTGYVDGGPVIELEHIWRVGPELEPDGDGDR
VEIEGEPNITLTIEPEIPGGIATAARAVNAIPAVIAAPPGLVTMLDLPLPRGRLGLLR
>gnl|CDD|443018 COG3805, DodA, Aromatic ring-cleaving dioxygenase [Secondary metabolites biosynthesis, transport and catabolism]
MTPRPTNDIAGYHAHVYFDEASREAAAALREEAGERFGVRVGRWHEKPVGPHPKWSYQLAFLPEQFDEVV
PWLMLNRGGLDILVHPLTGDDLADHTDHALWLGESLELNLSRLR
>gnl|CDD|443019 COG3806, ChrR, Anti-sigma factor ChrR, cupin superfamily [Signal transduction mechanisms]
AAVNDDAFDRRLARIDAPPAAPAAAAGRPPVLPRPLRRAVGLDDLPWRSPGPGVRRARLDRGGEGGRATS
LLRIAPGSAFPEHTHRGGEETLVLEGAFSDEHGDYGAGDFIRADPGSEHQPVADPDEGCICLVVLDAPLR
FTGGLGRLLNPFGRIHY
>gnl|CDD|443020 COG3807, SH3, SH3-like domain [Function unknown]
LLLAAAAAQLGPVSGLPAPRFVSLKSDEVNLRDGPSTKYPILWVYKRRGLPVEVIAEFGNWRRVRDPEGD
EGWVHQSLLSGRRTVIVTGDLANLRASPDENAAVVARLEPGVVLRLLECDGGWCKVRADGYKGWVRQSLL
WGVYPGEIID
>gnl|CDD|443021 COG3808, OVP1, Na+ or H+-translocating membrane pyrophosphatase [Energy production and conversion]
VLKQPAGTERMQEIAGAIQEGAMAYLKRQYKTLAIFAVVIAVLLALLLGGGGWLTAIAFLIGAVFSALAG
YIGMRVATRANVRTANAARKGLNKALKVAFRGGAVMGLLVVGLGLLGLSLLYLIFGGFLETAPEVLVGFG
FGASLIALFARVGGGIYTKAADVGADLVGKVEAGIPEDDPRNPAVIADNVGDNVGDVAGMGADLFESYVV
TIVAAMVLGALAFGAALGVALVLLPLLIAAVGIIASIIGIFFVRTKEGANPMKALNRGTYVTAVLSAVAT
YFVTYLLLPGSGFGWLGLFLAVLIGLVAGALIGLITEYYTSTEYRPVREIAEASETGPATNIISGLAVGM
ESTALPVLVIAAAILVAYLLAGGGFAPGLYGIALAAVGMLSTTGITVAVDAYGPIADNAGGIAEMSGLPP
EVREITDALDAVGNTTKAITKGFAIGSAALAALALFAAYIEEVGIALGEALLLSLDLLNPPVLVGLFIGG
MLPFLFSALAMQAVGRAAGAMVEEVRRQFREIPGIMEGTAKPDYARCVDISTKAALKEMILPGLLAVLAP
IAVGFLLGPEALGGLLAGAIVSGVLLAIFMANAGGAWDNAKKYIEDGNLGGKGSEAHKAAVVGDTVGDPF
KDTAGPSLNILIKLMNIVSLVIAPLFVALS
>gnl|CDD|443022 COG3809, COG3809, Predicted nucleic acid-binding protein, contains Zn-finger domain [General function prediction only]
EAMLCPKCGAPMRVVERSGVEIDYCPSCGGVWLDRGELEKLLEAEEAGAARRKSFLSDL
>gnl|CDD|443023 COG3811, YjhX, Uncharacterized conserved protein YjhX, UPF0386/DUF2084 family [Function unknown]
MNISKAEQRVLHVLAQGGRILHERDENGKITEVECVTREGWRLSDCTLAVFKKLKRKRLIASRGGGPYRI
TRRGLEAVRAQLDNR
>gnl|CDD|443024 COG3812, COG3812, Uncharacterized conserved protein, DUF1993 domain [Function unknown]
MSLSLYDASVPVFIRMLGNLSAILDKAEAHAAAKGIDPAVLLQARLAPDMFPLARQVQIACDFAKGAAAR
LAGVEAPSFEDTETTFAELQARIAKTIAFLESLSPAQIDGAEEREITLKLGGKELTFTGQDYLLSFALPN
FYFHVTTAYAILRHNGVELGKRDYLGALRL
>gnl|CDD|443025 COG3813, COG3813, Uncharacterized conserved protein, DUF1272 domain [Function unknown]
MLELRPNCECCDKDLPPDSPDARICSFECTFCADCAETVLDNVCPNCGGGLVPRPIRPAAALAKYPASTK
RVHKPVGCAAHAA
>gnl|CDD|443026 COG3814, SspB2, SspB-like protein, predicted to bind SsrA peptide [Posttranslational modification, protein turnover, chaperones]
MAEDLIRYDLLVQDALRGVVRKVLEEVAREGLPGEHHFYITFDTDAPGVEISDRLRERYPEEMTIVLQHQ
FWDLKVTEDGFSVGLSFGGVPERLVIPFDAITGFVDPSVQFGLQFEVAEEDDDEEEEEDDPEDAEPAEED
DAPEDDDPPPPEGGAEVVSLDAFRKK
>gnl|CDD|443027 COG3815, COG3815, Uncharacterized membrane protein [Function unknown]
AGLIYFLFFPLCHQLPERSFFINGRQMPVCARCTGIYLGLLIGLLLALLLGKLLPLPSLLLALLLLLPML
IDGFTQLLGLRESTNALRFITGLLFGIGLALFLYPILVELILKVR
>gnl|CDD|443028 COG3816, COG3816, Uncharacterized conserved protein, DUF1285 family [Function unknown]
YSAPPDLDGLAALAARAGAGRGLPPVELWNPPFCGDIDMRIARDGTWFYEGTPIGRPALVRLFSSILRRE
GDGRYYLVTPVEKVGIQVEDAPFLAVEMEVEGEGGDQVLTFRTNVGDVVTAGPDHPLRFERDPETGEPSP
YVHVRRGLEARLNRSVFYELVELAEERDIDGEDWLGVWSGGAFFPL
>gnl|CDD|443029 COG3817, COG3817, Uncharacterized membrane protein [Function unknown]
MILLEFLYILIGLILLATAVRSLRDKTNPKRIGTALFWGLLGLTFLFGDFLPAIIVGVLVILMALLAGFG
QVGIGSYKETSEEEREASAKRLGNKLFIPALLIPVVTVIGALLLKHLPIGGTPLLDTKLGTLVGLGIGCV
VALIVALILTKPKPKQAVREGRRLLDAVGWAAILPQLLAALGAVFAAAGVGDVIAHLVSSVIPEGNRFAA
VIAYCVGMALFTMIMGNAFAAFPVITAGIGIPFLIAQHGANPAVVGAIGMTAGYCGTLMTPMAANFNIVP
AALLELKDKYGVIKAQAPTALALLVVNIVLMYFLAF
>gnl|CDD|443030 COG3818, COG3818, Predicted N-acetyltransferase, GNAT superfamily [General function prediction only]
MTNPIVIRDAREHDLDAVLALNNAAVPAVSPLDAARLARLHEQAAYARVAEVDGEVAGFLLAFGPGADYD
SPNYRWFAERYDNFLYIDRIVVAPSARGRGLGRALYADVFSYARARGVPRVTCEVNLEPPNPGSLAFHAR
LGFREVGQQRVAGGKKRVSLLAKELCSY
>gnl|CDD|443031 COG3819, COG3819, Uncharacterized membrane protein [Function unknown]
MWPLIGILIIVVGFALRLNPLLVVLVAGIVTGLVAGMSPVEILEALGKAFVDNRYMSLFLLTLPVIGLLE
RYGLKERAQRLISKIKGATAGRLLILYLLIRQLTAALGLTSLGGHPQFVRPLIAPMAEGAAEAKYGELPE
KEREKIKAMAAATDNVGNFFGEDIFVAAGGVLLIKGFLEELGIDVEPLHIALWAIPTAIIAFIIHGIRLL
LLDRRLRREYKKKAAAASAA
>gnl|CDD|443032 COG3820, COG3820, Uncharacterized conserved protein, DUF1013 family [Function unknown]
MTQPLMPKATAVWLVDNTALTFEQIADFCGLHPLEVQAIADGEVAQGIKGLDPIANGQLTREEIERAEAD
PNYRLKLAESKVPVPERKRKGPRYTPVSKRQDRPDAIAWLLRNHPELKDAQISKLVGTTKPTIQAIRDRT
HWNSANIKPRDPVTLGLCSQIDLDAAVQKAAKRRPREEEEEGGRTLLPAEETLAPEAAEDEARAEEEEEL
DADSVFAKLKSLKGDDED
>gnl|CDD|443033 COG3821, COG3821, Uncharacterized membrane protein [Function unknown]
MTRLTLLSLLDLLALAWFLLCWLGYGWFAERRPKRRPSLSAVMHRYRRAWMRQMLTRDNRIFDAQILGNL
QQGTSFFASTSLLAIGGLLALLGATDRLLGLAADLPFAGPTSRALWELKLLLLLLIFVYAFFKFTWSLRQ
FNYCAILIGAAPNDPEADEPEAEAFAARAARVNILAARSFNRGLRAYYFALAALGWFLGPWLFIAATLAV
VAVLYRREFASDALAALLDG
>gnl|CDD|443034 COG3822, YdaE, D-lyxose ketol-isomerase [Carbohydrate transport and metabolism]
MKRSEINRIIREAEAFFEEHGIVLPPFAYWSPDEWKARDAEADEIRDEKLGWDVTDFGLGDFDRTGLTLF
TLRNGSLEDAGYGKPYAEKLMIVREGQTTPMHFHWPKMEDIINRGGGTLVLELYNSDPDGTIDTSPVTVV
VDGVERTYTAGEELRLAPGESVTLPPGTYHWFWAEGGDVLIGEVSTVNDDLTDNIFLDPIGRFPEIEEDE
PPLHLLVSDYPRFL
>gnl|CDD|443035 COG3823, COG3823, Glutamine cyclotransferase [Posttranslational modification, protein turnover, chaperones]
AIAVAAAAAPEVYTYEVVNTYPHDPTAFTQGLEFHDGTLYESTGLYGQSSLRKVDLETGEVLQRVDLPDR
YFGEGITILGDKLYQLTWQSGVGFVYDLATFELLGTFPYPGEGWGLTNDGKRLIMSDGSSTLRFLDPETF
AEVRTIQVTDNGRPVDRLNELEYVDGKIYANVWQTDRIVRIDPATGAVTGVIDLSGLLPEVKRTPGEDVL
NGIAYDPETDRLFVTGKLWPKLFEVRL
>gnl|CDD|443036 COG3824, COG3824, Predicted Zn-dependent protease, minimal metalloprotease (MMP)-like domain [Posttranslational modification, protein turnover, chaperones]
APSLEEFEALVAEALDALPEEFRALLDNVVILVEDFPDDEVLEELGLEDPPDLLGLYEGVPLTERSVSYS
GELPDRITLYRRPILDYWAEREELVEEVRHTLVHEIGHHFGLSDEDLHELGW
>gnl|CDD|443037 COG3825, CoxE2, Uncharacterized CoxE-like protein, contains von Willebrand factor type A (vWA) domain [Function unknown]
MFIDFFYELRAAGVPVSLREYLTLLEALDAGLAGSSLDDFYYLARAILVKDERHFDRFDQAFAAYFKGLE
TLDDELAREIPEEWLRKPLEKHLSEEEKAQIEALGLEELMETLKERLEEQKERHQGGNKWIGTGGTSPFG
HSGYNPEGVRIGGESRNRSAVKVWDKREFRDLDDDVELGTRNIKVALRRLRRFAREGAADELDLDGTIRA
TARNAGELDIVMRPERRNAVKVLLLLDVGGSMDPHIRLCEELFSAARSEFKHLEYYYFHNCVYEGVWKDN
RRRHRERIPTWDVLHKYGSDYKLIFVGDASMSPYEITHPGGSVEHWNEEPGAVWLQRLADHFPHAVWLNP
EPERYWGYTQSIGMIRELFEDRMFPLTLDGLERAMRELSR
>gnl|CDD|443038 COG3826, COG3826, Uncharacterized conserved protein [Function unknown]
MMTAIAARIAALDWAAIAAELDEQGCALLPGLLTPEECRALAALYDDDALFRSRVVMARHGFGRGEYKYF
AYPLPELVAALRTALYPRLAPIANRWNEALGIDARYPATLAEFLARCHAAGQTRPTPLLLRYGAGDYNCL
HQDLYGEHVFPLQVVILLSEPGRDFTGGEFVLTEQRPRMQSRAEVVPLRQGDAVIFATNHRPVRGTRGYY
RVNMRHGVSRVRSGERHTLGIIFHDAA
>gnl|CDD|443039 COG3827, PopZ, Cell pole-organizing protein PopZ [Cell cycle control, cell division, chromosome partitioning]
MSQGAQEPSMEAERLLSEEAAEAVASAFAALASAILSNGARTLEDLVREMLRPMLKEWLDENLPQLVERL
VREEIERVARG
>gnl|CDD|443040 COG3828, COG3828, Type 1 glutamine amidotransferase (GATase1)-like domain [General function prediction only]
MKAAKKKKVLVFSGGFRHDIEAGVPALKELLEENGFEVDVTEDAADFTPENLAKYDLVVFNNTTGDVLTD
EQQAALEDYVEAGGGFVGIHAATDTFRDWPWYGELVGGQFVSHPPIQEATVTVEDPDHPITKGLPDEFTV
TDEWYNFLRDPRPDVTVLATTDESTYPGGGMGGDHPVAWTREYGKGRVFYTALGHDEESFEDPGFRTLLL
RGILWAAGGKVA
>gnl|CDD|443041 COG3829, RocR, RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms]
AEELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLEVLK
TGKPVTGVIQKTGGKGKTVIVTAIPIFEDGEVIGAVETFRDITELKRLERKLREEELERGLSAKYTFDDI
IGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFVAVNCAAIPENLLESELF
GYEKGAFTGAKKGGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPVDVRIIAA
TNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLL
AYDWPGNVRELENVIERAVVLSEGDVITPEHLPEYLLEEAEAASAAEEGSLKEALEEVEKELIEEALEKT
GGNKSKAAKALGISRSTLYRKLKKYGIK
>gnl|CDD|443042 COG3830, ACT, ACT domain, binds amino acids and other small ligands [Signal transduction mechanisms]
MSMKALITVTGKDRPGITAAVSGVLAEHGVNILDISQTVIHGYFTMGMLVDLPESSASFEELQKDLEAAG
EELGVEVRVQHEDIFDYMHRIGRQGVVRYILTLLARAITAEAIAAVAAIVAINGLNIDRITRLSGRLELD
SGPDADVACVELAARGLAEDVAAAVAVALALARELRRDIAFQDDDRFRRRRRILVFDMDATLEEVEVEVE
LA
>gnl|CDD|443043 COG3831, WGR, WGR domain, predicted DNA-binding domain in MolR [Transcription]
MRLYLERIDPAGNSARFYELEVEPDLFGGWSLTRRWGRIGTKGQTKTKTFASEEEALAALEKLVAEKLRK
GYREVGAGAASAR
>gnl|CDD|443044 COG3832, YndB, Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and metabolism]
ADAEDRTITIEREIDAPPERVWRAWTDPELLARWFGPKGWATVAEFDLRVGGRFRFRMRGPDGEEFGFEG
EVLEVEPPERLVFTWGFEDDPEGESTVTVTLEPEGGGTRLTLTHTGFSAEDRDAVLAEGMEEGWTESLDR
LK
>gnl|CDD|443045 COG3833, MalG, ABC-type maltose transport system, permease component MalG [Carbohydrate transport and metabolism]
MSRRKSRKRRRRLKLGLRHLVLIILAIIALFPILWVVSASFNPGGSLYSSSLIPENFTLENYKKLFTETP
FLRWFLNSLIVAVVTAIISVFLAALAAYAFSRFRFKGRKAGLLALLLLQMFPAFLALVALYLLLSALGLL
NTLLGLILVYLGGAIPFNTWLMKGYFDTIPKELDEAAKIDGASHFQIFFRIILPLAKPILAVVALLSFIG
PWNDFILASVLLRSPENYTLAVGLYSFVSDQRNTNWGVFAAGAVLVAIPIVILFLFLQRYLVSGLTAGGV
KG
>gnl|CDD|443046 COG3835, CdaR, Sugar diacid utilization regulator CdaR [Transcription, Signal transduction mechanisms]
DPNLPIRFDGEVVGVIGITGEPEEVRAYGELAKTAELLLEQAREQLEWERRLREEFLDDLLSGNLEDEEE
LLERAKRLGIDLDRPRVVLVIELDSEDDESKDLERLRRALRALRRDLLVALSGDRLVVLLPAESEWRDEE
LRELAERLLEELEREGGLRVRIGVGRPVPGLAGLARSYREARRALELGRRLGPEGRVYFYDDLGLERLLL
QLRDDDELAEFLEEVLGPLLEYDKHGGELLETLRAYFENNGNISETAEALFIHRNTLRYRLKKIEELTGL
DLRDPEDRLLLYLALLLRRLL
>gnl|CDD|443047 COG3836, HpcH, 2-keto-3-deoxy-L-rhamnonate aldolase RhmA [Carbohydrate transport and metabolism]
MRKNRLKQRLRAGEPVIGTWLSLPSPAVAEILAGAGFDWVLIDLEHGPNDLETLLALLRAAAAAGVAPLV
RVPSNDPALIKRALDAGAQGVLVPMVETAEEARAAVAATRYPPLGIRGVGGPARAARYGRVADYLARAND
ETLVIVQIETAEAVENLDEIAAVPGVDGVFIGPADLSASLGHPGQPDHPEVQAAIERVIAAARAAGKPAG
ILAGDPEDARRYIALGARFVAVGSDVG
>gnl|CDD|443048 COG3837, COG3837, Uncharacterized conserved protein, cupin superfamily [Function unknown]
IVNLDDLPGPEAGRRYRRLGDALGLTRLGVNLITLPPGASSSPYHAHSAEEEFVYVLEGELTLRIGGEEY
VLEPGDSVGFPAGVPHRLRNRGDEPARYLVVGTRAPYPDSFDYWD
>gnl|CDD|443049 COG3838, VirB2, Type IV secretory pathway, VirB2 component (pilin) [Intracellular trafficking, secretion, and vesicular transport]
MKFLSMPLRRRLLLLALAALLLLLASPAFAAGSGMPWEGPLQQIVNSLTGPVAKAIAVIAIIVAGLMLAF
GELNGGFRRAIQVVLGISIAFGASSIVLSFFSFGGGILI
>gnl|CDD|443050 COG3839, MalK, ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]
MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL
PPKDRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQ
RVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDG
RIQQVGTPEELYDRPANLFVAGFIGSPPMNLLPGTVEGGGVRLGGVRLPLPAALAAAAGGEVTLGIRPEH
LRLADEGDGGLEATVEVVEPLGSETLVHVRLGGQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAETGR
RL
>gnl|CDD|443051 COG3840, ThiQ, ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]
MLRLDDLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE
RPVSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVAL
ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAA
DGPTAALLDGEPPPALAAYLGI
>gnl|CDD|443052 COG3842, PotA, ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism]
MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT
GLPPEKRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQ
QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMN
DGRIEQVGTPEEIYERPATRFVADFIGEANLLPGTVLGDEGGGVRTGGRTLEVPADAGLAAGGPVTVAIR
PEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLGDGQELVVRVPNRAALPLEPGDRVGLSWDPEDVVV
LPA
>gnl|CDD|443053 COG3843, VirD2, Type IV secretory pathway, VirD2 component (relaxase) [Intracellular trafficking, secretion, and vesicular transport]
MSDDDDFRRRPGRRRSRRAARARPFVAQAAAAAARAGGGVSRSGRGGGGRRGRFGRGRRASSRARRLLTS
RSRRVVVKARVVRHAGKGSAPLAAHLRYLQRDGVTRDGERGQLYGADTDRADGRAFAERCEDDRHQFRFI
VSPEDAAELEDLKAFTRDLMRQMEADLGTKLDWVAVDHWNTGHPHVHIIVRGVDDDGKDLVIARDYISHG
MRERASELVTLELGPRTELEIRRALEREVDAERWTRLDRALLREADDGGVVDLRPEPGPRDPEDRALLVG
RLQKLERLGLAEEIGPGQWRLAPGAEATLRELGERGDIIKTMHRALTERGIERGPADYVIHDEAPAAPII
GRLVDRGLADELGDRAYLVVDGIDGRTHHVRLPDGDATGDAPPGAIVEVRPREDAPGARRRTLAARADLD
LGRQSTAAHATWDDRQSRAREPAHLRRLEAGRRRRVALRRRADGEWLIADDLRRRGRVRAARRLRLLLRR
RELLLLALLLALEAGTGATDLDRELVVGGGGRQRRALAGRRAAMADDGGGQLLVPQPLSLEERGRLRVRG
LRRRGGGLDELGRRRRALGGELAAPAAEAPVRAGGEGTGRRTVGTTSGSLALREGARDFTLVPLRLVLWR
PVGQSGSGRGRGGGGSWGSGRG
>gnl|CDD|443054 COG3844, Bna5, Kynureninase [Amino acid transport and metabolism]
FETTRAFARALDAADPLAAFRDRFHLPDDGVIYLDGNSLGLLPKAAAARLAEVLEEEWGELLIRGWNEAP
WFDLPERLGDKLARLVGAAPGEVVVMDSTTVNLHKLLVAAYRPRPGRTKILSEADNFPTDRYALEGQARL
HGLDEELRLVEPRDGETLRPEDIEAALDDDVALVLLSHVNYRTGQLFDMAAITAAAHAAGALVGWDLAHS
AGAVPVDLHDWGVDFAVGCTYKYLNGGPGAPAFLYVHERHQDRLLQPLAGWWGHATPFAMEPGYEPAPGA
RRFQLGTPPILSMAALEASLDLFEEAGMDALRAKSLALTDYLIFLVEERLAPLGLELITPRDPARRGSQV
SLRHPEAYAIFQALIERGVIGDFREPDVIRFGPTPLYTSFEDVWRAVEILREILEEGEWEKFENERGAVT
>gnl|CDD|443055 COG3845, NupO, ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism]
MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR
IRSPRDAIALGIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVE
DLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADR
VTVLRRGKVVGTVDTAETSEEELAELMVGREVLLRVEKAPAEPGEVVLEVENLSVRDDRGVPALKDVSLE
VRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPD
MSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILARELSRD
PKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEAT
REEIGLLMAGVKEE
>gnl|CDD|443056 COG3846, TrbL, Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and vesicular transport]
MNDTGVIDRFLDRFTTYIDSGFGLLGGEVAFLFWTLIVIDMTLAGLFWALGDIGDFIARLVRKTLFVGFF
AWILGNFPNLAGIIFDSFAGLGLKAGGSSLTAADLLRPGRVADVGFDAAAPLLDAISDLMGPVSFFSNFD
TIAVLLIAWLLVLIAFFILAVQLFVTLIEFKLTTLAGFVLLPFGLSNKTSFLAERVLGNVVSSGIKVLVL
AVIVGIGSTLFDQFTAALSGGEPTIDEAMVIVLASLILLGLGIFGPGIAAGLVSGGPQLGAGAAAGTGAA
AGGAAVAAGAAAAAAAGGAAAAGGAAAARGGASAAGGAKAAYSLGSAGSGSGAAGVAAGMGGVGRAGGSA
AASPAGKAAFAQAAGFADSYRAGSRAAWAATGGAAARGAGLTASAPAKGGAPAWARRMKRRQAATHGATL
AAHALRSGDSGGSGASPSLSEKD
>gnl|CDD|443057 COG3847, Flp, Flp pilus assembly protein, pilin Flp [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
MKKLLKRFLKDESGATAIEYGLIAALIAVAIIAAVTTLGTALNGLFTSIATALTGANG
>gnl|CDD|443058 COG3848, PykA2, Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms]
KCNAAGKPVITATQMLDSMMRNPRPTRAEAADVANAIFDGTDAIMLSGETAAGKYPVEAVVTMVRIAERA
EEDLEYREQRVPRAKESSTTITDAISHAVATTAADLGAAAIITATESGATARMVSKYRPKAPIIAVTPSE
RVARQLSLVWGVYPLLVEESASTDEMFAVAVALALEAGLVKDGDLVVITAGVPVGVSGTTNLLKVHVVGD
VLAKGQGIGRGSVTGKAVVARSAEEALEKFEEGDILVVPSTDAEFVPAIEKAAGIITEEGGLTSHAAIVG
LELGIPVIVGAEGATEILKDGQVVTVDAERGVVYRGAVNVL
>gnl|CDD|443059 COG3850, NarQ, Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms]
LRELLLLALALLRLLLALLALLLLALLLLSLLALLLLLERTLLRLLSLLASAGLLAALLAALLLLLSLGL
LALLLALLLLLLLLLLAALLSLLLLLLLLLLLLLLLLLLLLAAAINRKLALLRLLLALLLALLLAYLLRR
RIVRPLRRLTQAAERIARGDFDARVPVSGRDELGTLARAFNRMADELQELYAELEEEEELEAELELLALL
DELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASALLL
LELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQ
AALEAAAAGAALAAAAAAAGLARALAQAGADAAEALGLLAEASEGAAGQGAGLVDVEGGVAGEGGLVVLI
VSIIAGGEAIARGEALAARGLAAAAALA
>gnl|CDD|443060 COG3851, UhpB, Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction mechanisms]
MQRLILSLFAFFLYSLAWFCLWAISFYLVRDPELAVLFLPFGLRLGLLLLTPRRYWPALLLAEWALLAWL
AIELGLLGLLWVLLASLLSLPAVALARRYWRRLYWQRLLVLLALVLLTALLNTLVSLLLGTSAAQVLLGS
LTGGLLLAPFCYLIWEYLFQQSKPIRLRTSHLLWYLLLFALSILLQLQLTAELRRFALFCLAIPIIFLAY
RYGWQGAVLATLLNSVALIAARQISSFHPLADLLLFLAAQSLTGLLLGAAIQRQRQLNQQLEQELRENRA
LARQLVSAEESERREIARELHDEIGQNITAIRTQASILKRLAPQPEIEQSAQSIESLALRIYDTTRRLLD
RLRPAVLDELGLEEALRELPRELAFEEPGISCQLDLRGDPSLLDDTLQLTLYRLVQEALTNILKHAEASQ
IRISLSQDKRLLSLEIRDDGIGLPPELRAKGFGLRGMRERVRALGGDFRLSSAPKGTRLSVLLPTPAASN
EAG
>gnl|CDD|443061 COG3852, NtrB, Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]
ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLERAL
AEGQPVTEREVTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLRDITERKRLERELRRAEKLAAVGELAA
GLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVL
ERVLELLRAEAPKNIRIVRDYDPSLPEVLGDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVERQVTLGG
LRPRLYVRIEVIDNGPGIPEEILDRIFEPFFTTKEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRI
YLPLEQAEEEP
>gnl|CDD|443062 COG3853, YaaN, Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms]
MSDETTEPEPALTLEDLLAPPAPVPEVPEQAAGMVDPEEAEVDLSKLSAEADAFVEALAAQIDLSDVNAI
LQYGAKAQRKLAAFSNRMLDRVKTKDLGEVGDSLSELRRTLEDLDPSELDDLKKKGLLGKLFPKGGNKLE
KYFAKYQSAQTQIDKISVALEKGQDELLKDNAMLDQLYEKNWEYFKELNQYIAAGELKLEELEAKIPALA
AEAEASGDPEDAQALNDLEQVLFRLEQRVHDLLLQRAVSIQGAPQIRLVQKNNQELIEKIQSAITTTIPL
WKNQVAVALALARQKLALDAQKAVNDTTNELLLKNAEMLKQNSIEIAKEAERGVVDIETLKQAFENLIAT
IDETLQIQDEGRAKRAQAEQELERLEEELKQYLLRARAR
>gnl|CDD|443063 COG3854, SpoIIIAA, Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning]
DLEEILAILPPTIREALEKLPDPVLDKLEEIRLRLGRPLELRFPGGEYFLSEAYPVTREDLERTLNRISN
YSLYALEEELRQGYITIPGGHRVGIAGTVVRESGIVKRIKDISGLNIRIAREVKGTADPILPYIISGGRI
YNTLIISPPGCGKTTLLRDIARVLSDGLLGFPGKRVGVVDERSEIAGCYGGIPQPDIGIRTDVLDGCPKA
EGMIMAIRSMSPEVIVVDEIGREEDAEALREAANAGVQLIATAHGNSLEDLLKRPTLSDLIGGGVFERYV
TLSRREGPGTVETILDRKADVLVEMLERD
>gnl|CDD|443064 COG3855, Fbp2, Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]. Fructose-1,6-bisphosphatase is part of the Pathway/BioSystem: Gluconeogenesis
MIKEDLKYLKLLSKQYPTIAAASTEIINLEAILNLPKGTEHFLSDIHGEYEAFSHVLRNASGVIKRKIDE
IFGNTLSEKEKKELATLIYYPEEKLELIKKEEEDLDEWYKVTLYRLIEVCRVVSSKYTRSKVRKALPKDF
AYIIEELLHEDSDDSDKEEYYNEIIDTIIELGRADEFIIALSNLIQRLVVDHLHIVGDIYDRGPGPDIIM
DTLMEYHSVDIQWGNHDILWMGAAAGSRACIANVIRISARYNNLDTLEDGYGINLLPLATFAMEVYKDDP
CTLFMPKLAEDDEYDEKEIRLIAKMHKAIAIIQFKLEGQIIKRHPEFGMEDRLLLDKIDYEKGTITIDGK
EYPLKDTNFPTIDPKDPYELTPEEEEVIDKLVSSFLNSEKLQKHIRFLYSKGSMYLVYNGNLLFHGCIPL
NEDGSFKEVTIEGKKYSGKALLDKLDQLAREAYFARDGSEEKKYGMDFLWYLWCGPDSPLFGKDKMTTFE
RYFIADKETHKEKKNPYYKLRDNEEICDKILEEFGLDPEKGHIINGHVPVKVKKGESPIKANGKLLVIDG
GFSKAYQKTTGIAGYTLIYNSYGLQLVSHEPFESTEKAIEEETDIVSTTRVVEKELKRKRVRDTDIGKEL
QEQIDDLKKLLEAYRKGLIKEKIK
>gnl|CDD|443065 COG3856, Sbp, Small basic protein Sbp (function unknown), DUF1290 domain [Function unknown]
WLPLLGLILGIIIGLFLPFTIPVAYSPYLSVAILAALDSVFGGIRAYLEGKFDNRVFISGFFSNALLAAL
LVYLGDQLGVDLYLAAVVAFGVRIFQNLAIIRRLLLKK
>gnl|CDD|443066 COG3857, AddB, ATP-dependent helicase/DNAse subunit B [Replication, recombination and repair]
RFILGRAGSGKTTYLLEEIKEELKEGKPIILLVPEQMTFQAERALLKRLGLGGSIRAQVLSFSRLAWRVL
QETGGATRPLLSDAGKRMLLRKILEEHKDELKVFARAADKPGFIEQLAELITELKRYGITPEDLEEAAEL
LKEKLRDLALIYEAYEEKLAGRYIDSEDLLRLLAEKLEKSEFLEGAEIYIDGFTDFTPQELELLEALLKK
AKEVTITLTLDPDELDLFSATGETYERLLELAKENGVEVEFKKSPELAHLERNLFAYPPEEEPEGIEIIE
AANRRAEVEAVAREIRRLVREEGYRYRDIAVVVRDLEAYAPLIERVFAEYGIPYFIDEKRPLSHHPLVEL
ILSLLELVRSNFRYEDVFRLLKTGLLRPLSREEIDRLENYVLAYGIRGRRWLERYLEEEEELTDEEEEDL
ERLNELRDRLLEPLLPLRERLKKAKTVREWAEALYEFLEELGVPEKLEEWREAEEAGDLEEAREHEQAWN
ALIELLDELVEVLGDEKLSLEEFLRILESGLEELTFGLIPPSLDQVQVGGLDRARGLDFKAVFVLGLNEG
VFPARPREDGLLSDEERERLNELGLELPPTSRERLLEERFLFYRALTRASERLYLSYPLADEEGKALLPS
PLIDRLRELFPELEERSLLEEELEYIGTPESALSELAAALRQLELAPLWWDVYKWLLKLSVSRLETYAAC
PFQFFLRYGLKLKEREEYELDAPDRGTLFHAVLERFYKELKEEGLDWADLSDEELEELLEEAVEELAPEL
QNGILLSSARYRYLLERLKRLLKRARRWLEEEARRSGFEPVALELSFGPEGGLPPLELELPNGRKIRLRG
RIDRIDRLESDGRYLRIIDYKSGSKKFDLDDVYYGLALQLPLYLDAALENLEGKEAEPAGALYFHLKNPK
LKAKKPLKKLKMKGLLLDDPEVLEIIPLKKDGSFKNSKVLSEEEFEELLDHVRELLKEAGEEILAGDFAI
NPYRTKDRTACQYCPYKSICRFDESLEGNEYRKLKKKEG
>gnl|CDD|443067 COG3858, SleL, Spore cortex hydrolase SleL/YaaH, N-acetylglucosaminidase of GH18 family [Cell cycle control, cell division, chromosome partitioning]
VQNGDTLDSIAPFWVSVANGDG
>gnl|CDD|443068 COG3859, ThiT, Thiamine transporter ThiT [Coenzyme transport and metabolism]
MKKKRTRMLVEIAIFAALAVVLSYIKLFKMPQGGSVTLSMLPIILIAFRWGLKAGLLAGFLYGLLQLLLG
PYILHPVQVLLDYPLAFGALGLAGLFRKKVQKKKRLLGIILGTLVGGFLRFLCHFISGVVFFGSYAPEGQ
NPWLYSLIYNGSYMLPELIITLIVLLILLKRLPKLLKPK
>gnl|CDD|443069 COG3860, COG3860, Uncharacterized conserved protein, DUF2087 family [Function unknown]
LLDLLLLLASESLLALAAALLLSAASASTAALLLFLLRLKAKAALLLLLAALLLAELLLARAAALAAPRE
AAAADARAAITEAEREKVLRRFFDEDGRLKRIPAKRKKRLVVLEHLASRFEPGRKYSEKEVNEILKRIHE
DYATLRRELVDYGLLTRTADGSVYWRIEEE
>gnl|CDD|443070 COG3861, YsnF, Stress response protein YsnF (function unknown) [Function unknown]
ANDDDEQTIPLYEERLVVGKRRVETGEVRVRKHVVTEEVTVTVPVRREEVVVERVPVDRAVTAAPGAAFQ
EETIEIPLYEERPVVSKEAVVVEEVRVRKEVVTETETVSETVRREEVDVERDGDLRIDDDDLE
>gnl|CDD|443071 COG3862, COG3862, Uncharacterized conserved protein with two CxxC motifs [Function unknown]
KKELTCIVCPKGCRLTVEVEDGEIIKVTGNTCPRGEEYAKQELTNPKRILTTTVKVEGGELPLVPVKTSK
PIPKEKIFDVMKELKKIEVKAPVKIGDVIIENILGTGVDIIATRNVE
>gnl|CDD|443072 COG3863, YycO, Uncharacterized conserved protein YycO, NlpC/P60 family [Function unknown]
MKKLLLFLAVCLTALSLGNKANDDLAPLQPGDILLTKSPSTLSGNHGHAGIYIGDGQVVEAVGDGVRIIP
LETWLDRYDTVAVLRVVKTSEAQRTAAANYAYSQVGKPYNYNFVKNVDDKKFYCSQLVWAAYKDAGGIDL
DSNGGLWVSPDDLLDSPDVYTVYTYK
>gnl|CDD|443073 COG3864, COG3864, Predicted metal-dependent peptidase [General function prediction only]
MSGPADAETKLEAARLRLLLEDPFLGALLLALRHVEDDAVPTAAVDGRWTLYYNPAFFARLSLEELAFVL
AHEVLHLALRHLARRKGRDPLLWNLACDYAINDYLDEAGLGLPPGAVTLERLGLEEGLSAEEIYRELRED
LRPEPKDQLCGSPADGHDRQWELPDLSPEEREELREEWARAIAQALEAARGRGKLPGGLRRLLAALLQPP
LPWRRLLRRFLARALRDEPDYSYARPSRRQGARLILPGLRRRRRPRVVVAIDTSGSISDEELGRFLGEVA
AILRALGAVRITVLQCDAAVQRVGKFEPEGLLREIRLKGGGGTDFRPVFEYAERAGPRPDLLVYFTDGEG
PFPERPPPYPVLWLLPGEGLSAPPPWGRVVRLGE
>gnl|CDD|443074 COG3865, COG3865, Glyoxalase superfamily enzyme, possible 3-demethylubiquinone-9 3-methyltransferase [General function prediction only]
MQKITPCLWFDGQAEEAAEFYVSVFPDSRITAVTRYPEDGPGGPAGSVLTVEFTLAGQPFMALNGGPLFK
FNEAVSFQVNCEDQAEVDRLWDALSAGGEESQCGWLKDRFGLSWQIVPRRLGELLADPDPAKAQRAMQAM
MQMKKIDIAALEAAAR
>gnl|CDD|443075 COG3866, PelB, Pectate lyase [Carbohydrate transport and metabolism]
MKLLLVLLLALAASAATAGAATAVPDAAAAAAPAPEGFASVNGGTTGGAGGTVVTVTTLADLRAALEASG
PRIIVVSGTIDLSKSPLKVNSNKTIAGQGDGATITGGGLNIKGASNVIIRNLRFRNGDDGGGSGGDAIGI
EGAHNVWIDHCTFSWGYDGLLDIKRGSDNVTVSWNIFAEGKGDHGKGMLIGSSDSDTTGKLRVTFHHNLF
ANNDSRNPRVRFGQVHVYNNYFYNWGNNYGIGSGGGAQVLVENNYFENVKGPLATSDGSSLLDPGYLYAR
GNVFDNSTGTAPAGSGTVFTPPYSYTLDPASDVKTLVLAGAGAGKL
>gnl|CDD|443076 COG3867, GanB, Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism]
MKKLTIARILLLLGLLLLACASNPAAKEAADFIKGADLSYLNEMEDCGGKFYDEDGVPKDPLQILKDHGV
NLVRLRLWVDPYWAAPYGGGYNDLADVLAMAKRAKAAGMKVLLDFHYSDFWADPGKQNKPKAWANLSFDQ
LKDAVYDYTYDVLTALKAAGLLPDMVQVGNEINNGMLWPDGKTEQGPGNWDRLAALLNAGIRAVRDVAAS
PDIKVMLHLAQGGNNGLFRWWFDNLTKRGVDFDVIGLSYYPYWHTGSLDDLGANLNDLASRYGKDVMVVE
TAYPWTLENGDGAPNIFGTDDPYAGGYPATPQGQADFLRDLIQAVKAVPNGGGLGVFYWEPAWIPVPGTG
WAGEGSSWENQALFDFDGKALPALDAFKAPAT
>gnl|CDD|443077 COG3868, COG3868, Predicted glycosyl hydrolase, GH114 family [Carbohydrate transport and metabolism]
MRRRRLLLLVLLALLLAGCAAAAAAAWWRPPPGATWQWQLYGPLDTLYDVDVYVVDPFDTTAATIAALKA
AGRKVICYVSVGEVEPWRPDAADFPAAVLGKNLDGWPGERWLDIRSPDWLAFIMEARLDLCWAKGFDGVE
PDNLDSYQNDTGFPLTAADQLAYNRRLARAAHARGLAIGLKNGFEQVPRLADYFDFAVAESCFGYDECGR
YVEPFRAAGKPVFAIEYTDPGDRAFARACAARIAALGFSPLVKDRDLDALGRLGYVPDYCDV
>gnl|CDD|443078 COG3869, McsB, Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones]
MSLDFLLSALSEWMEGSGPESDIVLSSRIRLARNLAGFPFPHRASEEEAEQVLSLVREALLSLSFQELGK
FELIKLEDLSPLERQVLVEKHLISPELAENPGGRAVLLSEDESVSIMVNEEDHLRIQCLLPGLQLEEAWE
LANKIDDALEEKLDYAFDEKFGYLTSCPTNVGTGLRASVMLHLPALVLTGQINRVLQALNQLGLTVRGLY
GEGSEALGNIFQISNQITLGKSEEEIIENLESVVRQIIEQERNAREALLKENRLELEDRVWRSYGILKYA
RLISSKEALNLLSDVRLGIDLGIIPGISPEVLNELMILTQPAHLQKLAGRELDPEERDIKRAELIRERLK
KLK
>gnl|CDD|443079 COG3870, DarA, Cyclic di-AMP receptor DarA/PstA [Signal transduction mechanisms]
MKLVIAIVQDEDANKLIDALVEAGFRATKLASTGGFLREGNTTLLIGVEDERVDEVLEIIKENCKSRKQF
VTPPSPMAGSGDSYIPYPVEVEVGGATVFVLDVERFEKF
>gnl|CDD|443080 COG3871, YzzA, General stress protein 26 (function unknown) [Function unknown]
TTDDEELEEKLWELLEDIRTAMLATVDADGRPHSRPMWFQVDVDDGTLWFFTSRDSAKVRNIRRDPRVSL
SFADPGDDRYVSVEGTAEIVDDRAKIDELWNPLAEAWFPDGPDDPDLVLLRVTPERAEYWDS
>gnl|CDD|443081 COG3872, YqhQ, Uncharacterized conserved protein YqhQ, DUF1385 family [Function unknown]
MMMKKPSYGGQAVIEGVMMRGPKKTAVAVRRPDGEIVVEEEPLKSLPKRSKLLKIPFLRGVVALIESLVL
GIKALNFSAEIAEEEEEEEKLSKWEMALTVVLSLLFAIGLFVVLPTLLAGLLGRLVGNSFLFNLIEGIIR
LAIFLGYIWLISRMKDIKRVFQYHGAEHKTINAYEAGLELTVENVRKYSRLHPRCGTSFLLIVMIVSIFV
FSLLGWPPLWLRILSRILLLPVVAGISYEILRLAGKHRDNPLVRILIAPGLWLQKLTTREPDDDQIEVAI
AALKAVLEEEEEEEEEEE
>gnl|CDD|443082 COG3874, YtfJ, Uncharacterized spore protein YtfJ [Function unknown]
MMEHPIEELMKTTMESLKKMVDVNTVVGDPIETGDTTIIPVSKVSFGFGAGGGEGKSKKGGKLGFGGGSG
AGVSITPVAFLVIKGDGVRLLPVKGNSLLDKLIDMVPEIIDKIKSKKEKKKKEEKEKEEESEE
>gnl|CDD|443083 COG3875, LarA, Nickel-dependent lactate racemase [Cell wall/membrane/envelope biogenesis]
MKISLPYGKGTLDLEIPDENLVGVLEPNEVPPLEDEEEAVREALDNPIGSPPLEELVKGGKKVVIIVSDI
TRPVPSKIILPPLLEELNEAGIPDEDITILVATGTHRPQTEEELREILGEEIVDRYRIVNHDARDKEDLV
YLGTTSRGTPVYVNKLVVEADLVILTGFIEPHYFAGFSGGRKSILPGVASRETIQANHSLMLDPKARTGN
LEGNPVHEDMEEAARMAGLDFILNVVLDSDKEIVAAVAGDPEKAHRAGCEFVRELYGVPIPEKADIVIAS
AGGYPKDINLYQAQKALDNAEAAVKPGGVIILVAECREGLGEDSFEEWLREAKTPEEVLERIRKEFTLGG
HKAQALARILEKAEVILVSDLDDELVRKMFMIPAKTLEEALDLALKKKGPDAKVAVMPDGGLTLPVVK
>gnl|CDD|443084 COG3876, YbbC, Uncharacterized conserved protein YbbC, DUF1343 family [Function unknown]
KVKTGADRLLAEYLPLLKGKRVGLVTNPTSVDRDLTHLVDLLLAPGVNLVALFGPEHGFRGDAQAGEKVG
DGVDPKTGLPVYSLYGKTRKPTPEMLKGIDVLVFDIQDVGVRFYTYISTLHYVMEAAAENGKPVIVLDRP
NPIGGLYVEGPVLDPGFESFVGMHPIPVRHGMTVGELARMFNGEFGIKCDLTVIPMEGWRRDMWYDDTGL
PWVPPSPNLPTLDSALLYPGTCLFEGTNVSEGRGTTRPFEVFGAPWIDGERLAERLNALGLPGVRFRPFS
FTPTFPKHAGKLCYGVQLHVTDRDAFRPVRTGLALLIALYRLYPDKFKFFDPSRNLFFDKLAGTDKLREQ
IEAGASPEEIRASWQPDLEAFKKRRKKYLLYP
>gnl|CDD|443085 COG3877, COG3877, Predicted DNA-binding transcriptional regulator with XRE-family HTH domain, DUF2089 family [Transcription]
MMYPVPTKCPVCGGELIVTRLKCPSCGTTIEGEFELCKFARLTPEQLEFVELFLKCRGNLKEVEKELGIS
YPTVRNRLDEIIAALGYEPEEEEEEDERKEILDKLEKGEISAEEALKLLK
>gnl|CDD|443086 COG3878, YwqG, Uncharacterized conserved protein YwqG, DUF1963 family [Function unknown]
AELRERLEKLAKPAIRLSPTPKEPTPLGASKFGGVPYLPKGMEWPTDSDGQPLSFLAQINFAELPPLDGL
PATGILQFFIDLDDDPWGLDFTDQDGFRVIYYPEPEEELTRAEYYPADYVFGEYALSFSKELELPSPEDY
RFEELFGEDEDEDAWEDYYDLLDELYDDGAGHKIGGYPSFTQGDPRDECEEAEDWRLLLQLDSDDDAGIM
WGDSGVLNFFITEEDLANRDFSRVWYNWDCS
>gnl|CDD|443087 COG3879, YlxW, Uncharacterized conserved protein YlxW, UPF0749 family [Function unknown]
MKERRRRKRWRLLVAVVCLLLGFLLAVQVRTTRGPDLLRATREEDLVALLDELQEENERLEAEIAELRAE
VDELESGAASSDAALEALQEELEKLRILAGLTPVTGPGIVVTLDDAPGDAEGGENPNDLVVHDQDLLDVV
NELWAAGAEAISINGQRIVATSAIRCAGNTILVNGRPLSPPYVIKAIGDPDTLEAALNIPGGVLDQLRKA
YGIGVTVEKEDEVTIPAYTGPVDLRYAKPV
>gnl|CDD|443088 COG3880, McsA, Protein-arginine kinase activator protein McsA [Posttranslational modification, protein turnover, chaperones]
MLCERCKKRPATVHLTQIINGEKTEVHLCEECAKEKGEFSFGFDEPFSLHDLLSGLLNFDSGQSSEKAPE
DELVCPTCGMTYSEFKKTGRLGCPDCYETFRDELEPLLRRIHGNTTHVGKVPKRAGGRLRIKREIEELKE
ELQEAVEKEEYEEAAELRDEIRELEKELGEEGE
>gnl|CDD|443089 COG3881, YrrD, Uncharacterized conserved protein YrrD, contains PRC-barrel domain [Function unknown]
MRKSSELIGLPVISLETGKQLGRVKDLVFDPEEGRVAGFLVESGGLFKGAKVIPFEDVVSIGEDAVTVDS
SSAIEKLEELPELNELLKKKIDLIGKKVITEKGELLGTVEDVYFDEETGKIVGYEISDGLLADLLKGRKI
LPAEQIVTIGKDVIIVPEEAE
>gnl|CDD|443090 COG3882, FkbH, Predicted enzyme involved in methoxymalonyl-ACP biosynthesis [Lipid transport and metabolism]
MTLAREIARLVAALRGKTRKCLVLDLDNTLWGGVLGEDGIDGIRLGQGAPGEAFLAFQEVIKTLDRRGIL
LAIASKNDEEDALEVLEEHPDMVLKEEDFAAPQINWNPKSENIREIAKELNIGLDSFVFIDDNPFEREEV
RAALPEVLVIDAPADPAEYAAALLALPEFEPLSLTEEDRKRREMYRANAKREELEESVGSLEEFLASLEM
RLTIRPADEADLPRVAQLTQRTNQFNLTTRRYSEEELAAFLADPGHLVLVARLTDKFGDYGLVGVVLVRR
EGDVWEIDLLLMSCRVLGRGVETALLNHLVELARAAGAKRLVAEYVPTAKNRPVRDFYRFLGFEEIEEDG
GLTVFELDLSSAPPPPEHIRVTEEE
>gnl|CDD|443091 COG3883, CwlO1, Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown]
ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL
QAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKA
DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA
AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAAS
AAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGG
GGGGGGGSSSGGGGGGVGLSVGGGYVGGA
>gnl|CDD|443092 COG3884, FatA, Acyl-ACP thioesterase [Lipid transport and metabolism]
YEKEYRVRYYEVDFNGRLRLPALLNYLQDAATEHAEALGFGIDDLEEKGLAWVLSRYQIEIDRYPRWGEK
ITVETWPSGYNRFFAYRDFRILDEDGELLARATSIWVLIDLETRRPVRIPDEILEPYGLEEERALPRPPR
KLKKPEDDEEEKEFTVRYSDIDTNGHVNNARYLEWALDALPLEFLKNHRLKRLEINYLKEVRLGDTVEVR
SARDEDGRTLHRIVGDDDGKELARARIEWRKL
>gnl|CDD|443093 COG3885, COG3885, Aromatic ring-opening dioxygenase, LigB subunit [Secondary metabolites biosynthesis, transport and catabolism]
MSIVGAGLVPHPPIIIPEVGGGEEKKIQKTIEAMKELARRIAEAKPDTIVIITPHGPVFRDAVAISPGER
LKGDLARFGAPEVSFEVENDLELAEEIAKEAEKEGIPVATLDEALAKRYGISLELDHGTLVPLYFLNKAG
FDYPLVHITPGGLSYEELYRFGKAIAEAAEALGRRVVVIASGDLSHRLTPDGPYGYHPEGPEFDRKVVEL
LEKGDVEGLLTLDEELIEKAGECGLRSFIIMLGALDGLEVSSEVLSYEGPFGVGYGVAAFEPG
>gnl|CDD|443094 COG3886, COG3886, HKD family nuclease [Replication, recombination and repair]
SLLAGFIDPIRPSTPLSSPKLLTNGKDEPSLLSELKKELKSADSFDISVAFITWSGLRLLLDALKELLER
GVKGRILTSTYLGFTEPKALRELLDLPNIEVRVSYDRKTRFHAKAYIFERTGYGTAIIGSSNLTRSALTD
NLEWNVKLSSAEDPDLIEKFRAEFESLWEDSEFVTLDPWIDKEEERYRRALKKEQRSDQPSPEEEEEPPP
PPPQQQQALLLLLARRRRRGRRLLLVVAAGTTTGTAAAAAAAFRRRLRALFRLLRLLILERAALLVSKRF
KSLRGLGGGGKGLLLGDGFATTSLTLSQSSLLSLLKSFLFDDDIIDIDDDVAAAAAAHAAAAFLFFFLLL
LLLLLLLPTDTDDDDLDDLNLDEEFDLRRALEELLLLLLLFFLLLDYFDDDDIDDDDDDDDGLDLREDEL
ELLNLVDYARDRYRRRKRLKRLLIIEAAKALAKFAAAAFAKAAALAAAASALAEAAARERAEDLAEDLEL
LDIITDDIFLVVILIIIVNIVVLLIPTLIIIIFIQLLLLLLRLLGLRKLRLLLDLLGFDNNLNLLIILLL
GLTLLNKNLLRRRLRGALLLSLFPGLESLEDILILIKILSDIIRLLLLLLKLKKLLLLRLLLLRRRLLEL
DELLLLRDDLLDLLLFLESLDDLSLKLKLEKKELLDLLEELLRKELKLLLLLLLLLLLLLLLLLLLLLLL
LLLLLLLLLLLLRRLLSLLSLEESVLSLLLLLSALLKKLKLSKALPLLIKLSVKLSLSNLLLELLKKFLL
KEELKDILLELLNKLLLRADLLLLLLYLRRARKDVLLEKNALLSDARALYYKELLILLTLALLTKYKDTG
STTKTKNYFNSLEESSSSSDSTRSIDSSEDRLQLLLLIKRRRKLLLDLLLKLDAGGGGGYLEVLLGDKLE
LGERLEGAVKKKKVKVAKLLVLKVLLKLDVA
>gnl|CDD|443095 COG3887, GdpP, Cyclic di-AMP phosphodiesterase GdpP, contains GGDEF-like and DHH domains [Signal transduction mechanisms]
MKKKLKKRKLRPLLLVLLLLLLLLLIILLFYNWIIGLLGLLLLILLLYYNIKAERKRRRELEKYIETLSY
RVDKAGKEALLELPIGIVLLDEDGEIEWYNPYFSEIFGDEDLLGKSLEDIFPELNLDKLKEEEGEEPFTI
TIGDRYYRVYYKKVKDEEEDLRLLYFFDVTEYEELKKEYEEERPVIGIIFIDNYDEVTQSMDESERSLLN
SEVTRKLNDWANEYGGFLKRYSSDRYLAVMNEKILEKLEEDKFSILDEIREITSGNNIPVTLSIGIGYGG
DSLAELGELAQSALDLALGRGGDQVVVKDGDKVRFYGGKTNAVEKRTRVRARVIAHALRELIKESDNVFI
MGHKNPDMDSIGAAIGVLRIAKMLGKEAYIVLDEVNPSIDRLMEEIKEEEEYEDLFISPEEALELITKNT
LLVVVDTHRPSLVESPELLEKAEKVVVIDHHRRGEEFIENPVLVYIEPYASSTSELVTELLQYQPDKIKL
SKLEATALLAGIVVDTKNFTLRTGVRTFEAASYLRRNGADTILVKQLFKEDLDTYIARAELISSAEIYRD
GIAIAVGPEDIEYSQVIAAQAADELLNIKGIEASFVLTKRSDGKIGISARSLGEINVQVIMEKLGGGGHL
TNAGAQLKDVTIEEAKEQLKEAIDEYLEEGEE
>gnl|CDD|443096 COG3888, COG3888, Predicted transcriptional regulator [Transcription]
MMSLREKILRILKNYGGEGIPQSELVRLLGASKSRVSEILSELEKEGLIARKKVIGKSKRVWLREYYPEP
DDKVLRIGILRASEYPFLLSFVKKLKEKGIDVEVKVYDNALSLTRDLAEGKIDLALSPLITQLIFSILYR
NIKIVGGGASGGSGIVGNPSGNGIVGSSELSSMELWRREFIKRLGLIEIIYFKSPEELIKSLESGEVGYI
AIWEPYYSILERNGYKVVFSDLFELEPCCTLAVNNSLNSEDLEKIKKIYREAIEEFLSSKDRWLEYYSKL
TGIDYSLVKKAVKNYDFDPELDMEELKRNLEKIGIEIPDNSIEFEAVI
>gnl|CDD|443097 COG3889, COG3889, Extracellular solute-binding protein, contains Ig-fold domain [General function prediction only]
MKKLLVVLVALLLALLLLSILSPANTAFAQAQEKGPAVDKVIFIVYSDEEQALEEVESGDIDLYFFGIPP
SLAQKLKSRPGLDVYSAPGGSYDLLLNPAPPGNGKFNPFAIKEIRFAMNYLIDRDYIVNEILGGYGVPMY
TPYGPYDPDYLRYADVIAKFELFRYNPEYANEIITEAMTKAGAEKIDGKWYYNGKPVTIKFFIRVDDPVR
KQIGDYIASQLEKLGFTVERIYGDLAKAIPIVYGSDPADLQWHIYTEGWGAGAFVRYDSSNLAQMYAPWF
GNMPGWQEPGFWNYENDEIDELTQRLATGNFTSLEERWELYRKALELGIQESVRIWLVDQLDPYVANSNV
KGVANDLGAGLRNPWTLRNAYTPGGTLTIGVRSVFQGPWNPVGGFNDVYSVDIARALYDPASFPHPFTGE
PIPFRVEWKVETGGPGGKIEVPADAIIWDPTSQKWVTVGPGTTAKSKVTFDYSDGLGRKWHDGQPITLAD
ILYAYYFAFEWATDPNDPTYDSAYAPSAKPFLDTIKGFRIIDDDTIEVYVDYWHFDPNYIASWAAFWPLS
MPWEIYAAMEKAVADGKLAFSRDKADSKNVDWLSLVAPDDVEIIKAALQEAINEGYIPYALKLVGLVTEE
EANARYQAAIDWINTYGHAWISNGPFYLDSYDPVAQTIELKAFRDPTYPFKPGYWLEFGKPVIPEIESVD
VPTIVVPGQPATITVSVTFAGYPYDIGSVKYFLIDPNGKIVAVGDAAPVAPGTFTITLPAEVTAKLSPGS
YTLVVIAYSELVALPAIYTTSFIVTPAVTIAVSTTIQTLTDTDTTTTTSAKTTPSLTTAATTTTTSTTTS
TTSVTTTAAALASAATAAIVVGVVAVAVAIATAILAVR
>gnl|CDD|443098 COG3890, ERG8, Phosphomevalonate kinase [Lipid transport and metabolism]. Phosphomevalonate kinase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
MDIIMFSAPGKVLWIGSYSVVFGGLSHVIAINKRVRCEFKESDSWIFETKYGKFDEKGNELIFSVFNYFK
QKFGNLPRLDVYLDNDNFFQIDGKKTGLGSSSAVTVALTACLYLILNGRLDKDEIFKLAQEANYRRQGGI
GSGFDIATAVFGSVVYFRFTDIPKVDSLIEPLRLGNYYMMLGFTGRSSKTVNSVKKFNEKRNLEKFKELM
KFIDEENIMAIKLLKLGKIDEALEHSKLARKDLNLLAGEVVGVSAENELPRSLIKLAEENGALIALSPGA
GGETFFALGPNLERVKEKWKKRGIIVINLKEDEGLKFES
>gnl|CDD|443099 COG3892, IolC, Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]
ARMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFL
REELEREGVDTSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGT
HLSHPRTRAAVLKALRYARAHGGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVG
TEEEFHIAGGSTDTLAALRAVRRVSTATLVCKRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGD
AFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAMPTWEELDYFLARGSRVPRPDKDAELNHLHR
VTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQVAAGAGLRGGIGVLIDDRYGQ
DALNAATGRGWWIGRPVELPGSRPLRFEHGRDIGSQLVEWPQEHVVKCLVFYHPDDPAELRLEQEAQLRR
LYDACRRSGHELLLEVIPPKDGPVDDDTVARAIQRFYNLGIKPDWWKLEPMSAAAWQAIDALIAERDPYC
RGVVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLW
RAARQAAAAA
>gnl|CDD|443100 COG3893, COG3893, Inactivated superfamily I helicase [Replication, recombination and repair]
MSVFTIPPGAPFLDALAAGLLARLAGDPLALARVTILLPTRRAARALREAFLRLLGRALLLPRIRPLGDL
DEDELLLDLPPAISPLERRLLLARLVRRWADALVPASPADALDLADSLARLMDELETEGVDLEALADLVP
DDLAGHWQRTLDFLKIVTEAWPAILAERGLIDPAARRRALLEALAARWRAAPAGPVIAAGSTGSTPATAR
LLAAVARLPQGAVVLPGLDLDLDEAAWAALAEDHPQYGLKRLLDRLGVTREDVRPWGATPALPARARLLS
EALRPAETTDAWRDLGAAALAGLTLIEAADPEEEALAIALALREALEEPGRTAALVTPDRALARRVAAEL
ERWGIEVDDSAGWPLSTTPAGALLRLLLELAAEPLAPVALLALLKHPLVRLGLGRGDHRRAVRALELALR
RGGRPAPGLAGLRAALARARPDDAEAAAALLDRLEAALAPLLALFAAGKRPLADWLAALRALLEALGADE
EGGEDALWAGEAGEALLELLAELAAAAGAGGPLSAAEYPALLRALLEGTTVRPPGGPHPRVQILGLLEAR
LQRFDAVILGGLNEGVWPPAPRPDPWLSRPMRRALGLPTPERRIGLAAHDFAQALGAPEVVLSRARRSDG
APTVPSRWLQRLEALLGGAALAAMGARWLAWARALDRPAPVAPAARPAPKPPVARRPRLSSVTIETLLRD
PPYAYYARRLLLLLLLPPLADPPAAARGGLLHHALLEFFEREPPALPADAAAALLLALAEALLALAAAPA
AAAAWWARRLRRAAAFAAAEEERRRALAREEAEEEGGRLALLEGGLLLLLRRRDRDDDDGDGDGGDDDKT
TTTGPPAKKLLLDLQLLLLLLAAAAGAGGGAGAAAAALALALLLLLLLGGPEGEALLELAAADLAALAAA
LALAAAALLAQGAAELAALAALALARDRAAALGDLADAAELAAAPEGEEEAAEGA
>gnl|CDD|443101 COG3894, COG3894, Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain [Function unknown]
MPKVKVTFLPSGKRVEVEAGTTLLDAAREAGVDIDAPCGGRGTCGKCKVKVEEGEFSPVTEEERRLLSPE
ELAEGYRLACQARVLGDLVVEVPPESRLDKQKILKEGLEREIELDPAVRKYYVELPEPTLEDPRSDWERL
KRALRKQGGLDDLTIDLSVLRKLPEVLREGDWKVTVTLHGGNEIIDVEPGDTTERLYGLAVDIGTTTVVA
YLVDLNTGEVLAVASAYNPQISYGEDVISRISYAMENPDGLEKLQRAVVETINELIEELCEEAGIDPEDI
YEAVVVGNTTMHHLFLGIDPRYLGRAPYVPAFSEPPSLKARELGLEINPGARVYLLPNIAGFVGGDIVAG
VLASGLHKSEELTLLIDIGTNGEIVLGNKDRLLACSCAAGPAFEGAGISCGMRAAPGAIERVRIDPDTLE
PRYKVIGDGPPRGICGSGLIDAVAELLRAGIIDRSGRFNRDLDTPRIREGEGGPEFVLAWAEETGIGRDI
VITQKDIRNLQLAKAAIYAGIRTLLEEAGLDFEDLDRVYLAGAFGNYLDPESAITIGLLPDIPLEKVKSV
GNAAGAGARLALLSREARREAEEIARKVTYIELSTEPDFQDEFVAALFLPHTDLDLFPSVK
>gnl|CDD|443102 COG3895, MliC, Membrane-bound inhibitor of C-type lysozyme [Cell wall/membrane/envelope biogenesis]
MKKLLLLLAALLLAGCASAAPPADPAPATQTVHYQCEDGKPLTVTYINNDNSLAVLRLDGETLVLKQVVS
ASGARYSDGQYVFWSKGDEATLERNGDDVVLNDCKLVK
>gnl|CDD|443103 COG3896, COG3896, Chloramphenicol 3-O-phosphotransferase [Defense mechanisms]
MEMKGRIIILNGASSSGKSSIARALQELLPEPWLHLSIDTFVDMLPPRLLRGIDGPGGAIDVGPILRRLI
RGMHRAIAAFARAGNNVIVDDVLLEGAWLQDLLRALSGLPVLFVGVRCPLEELERRERARGDRPIGLARS
QAERVHAGVIYDLEVDTSALSPEECAERILARLKARPSPSAF
>gnl|CDD|443104 COG3897, Nnt1, Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones]
MSEDFIRANTRLETVLVPEIRLHLAADAHPLWDATEEALGESGAPPPFWAFLWPSGQALARYLLDHPEVA
GKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPPAAGGFDLIL
GGDVLYERDLAEPLLPFLDRLAAPGGEVLIGDPGRGYLPAFRERLEALAGYEVVTRELEDTEKVKRGRVL
RLRRGA
>gnl|CDD|443105 COG3898, HemYx, Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to HemY-type protoporphyrinogen oxidase) [Function unknown]
MIRILLFLALVAALALGAAWLADRPGTVSITWLGYEIETSLLVAAIALLVLAAAVWLLWRLLRFLLGSPT
ALSRYFRRRRRRKGYQALSRGLIAVAAGDGRLARRKAAKAERLLDRPPLTLLLEAQAAQLAGDREAARRA
FEAMLEDPETRFLGLRGLMVEALRRGDTEAALALAEEALALAPKLPWAQDALLELQAAAGDWDGALATLD
AALKAGLLDKDVARRRRAVLLTARARELEEGDPDEARELAIEALKLAPDLVPAAVLAARLLIAQGKLRKA
AKVLEKAWRAQPHPDLAAAYAELRPGDSALDRLKRAETLAALNPDHPESRLALAEAALAAGDFGEARRAL
GPLLEERPTARVCLLMAEIERGEHGDDGRVREWLARALRAPRDPAWVCDACGTVSDDWAPVSPVCGRLDA
FEWKTPPERLAAPPAEAEMLPLIVGLPAAEAEAAAPPAEAVPDDPVEE
>gnl|CDD|443106 COG3899, COG3899, Predicted ATPase [General function prediction only]
LALLLLGLRLAVARLRGLLLALAAALALLAAALLLLLLLALRLALLLLALALLLLLLLALLLLLALLLAL
LLLALLLLALALLRLLAAERLALLLALALALLAALLLLLALALLLLALLALALLALLLALLLAAGVLGLL
LGGLLLAALAALLALAALAAAAAAAAAAAAARAARLRRARAARLAALALRALLLLVLLLLLLLLLLGLLL
AAAAALAAAAAAAAAAAPAAPVVLVAALLLALAALLALLLLAARLLGLAGAAALLLLGLLAAAAAGRRLL
ARRLIPQPLVGREAELAALLAALERARAGRGELVLVSGEAGIGKSRLVRELARRARARGGRVLRGKCDQL
ERGVPYAPLAQALRALLGQLPEDELAAWRARLLAALGANGRLLADLLPELELQPAPPELDPEEARNRLFR
ALLRLLRALAAERPLVLVLDDLHWADPASLELLEFLLRRLRDLPLLLVGTYRPEEVPPAHPLRLLLAELR
RAGAGVTRLELGPLSREEVAALVADLLGAAELPAELAELLVERTGGNPFFLEELLRALLEEGLLRFDGGG
WRWDAALAALALPDTVVDLLAARLDRLPPAARRVLRLAAVLGRRFDLELLAAVLGLSEAELAAALEELVA
AGLLVPRGDAGGGRYRFRHDLVREAAYASLPPEERRALHRRIARALEARGPEPLEERLFELAHHLNRAGE
RDRAARLLLRAARRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLER
ALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFIL
HWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAA
AALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAA
AAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALA
AAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAAL
AALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAA
AAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA
>gnl|CDD|443107 COG3900, COG3900, Predicted periplasmic protein [Function unknown]
MIKPLRALLLALALLLAAAAAAAAAAAAAPAAKAIDPDADEILKAMSDYLASLKSFSVDADTTYDVVLDS
GQKIQFSASGEVTVRRPDKLRVDRTGDGADREFYYDGKTFTLYGKALNVYATAEAPGTIDEALDKLRDKY
GIELPLADLLYSDPYDALLDRVTSAKYVGSSKVGGVECDHLAFRNDDVDWQIWIAQGDQPLPRKLVITYK
NVPGAPQYSATFSDWKLNPSLPDDTFTFTPPAGAKKIDFLPLDAAADGKK
>gnl|CDD|443108 COG3901, NosR, Transcriptional regulator NosR of nitric oxide reductase [Transcription]
MRSLLLLALLLLLLLLAAAAAAASTLPDFLARVPCAEVFPGATRFGEREGDPPVAPVYKGGELLGYVFLT
TDFVDTPGYSGKPINTLVGIDTDGRIVGVKLLKHSEPILLIGIPESKLRAFIEQYVGLDVKDEIEVGGSR
DEGAHGLDIISGATVTVMVINDSIMRSALKVARQLGIGAPAVRGPAREIDPDAGEPLDWATLVGDGSVRR
LRLTVGQVNAAFAGTGDARADERPTGDPDDTFIDLYFALLNVPTIGRSLLGEAEYANLMARLKPGEHAIL
VAGRGRYSFKGSGYVRGGIFDRIQLIQGGDSFRFRDLDHLRLYDLAAAGAPEFTESAIFRIRADAGFDPA
YPWRLQLLVQRATGALEKVFTTFDLGYWLPAAYLEGPPPAEVAAPAPLWQRIWKDRAVEIALLGAMLLVL
TVVFFFQDRLTRRPRLVHWFRYGFLAFTLLVLLLGWGGQLSVVVVVVLLFLFLFFFLFFFFLLLPFLFLL
WLWAAAALLLLGGGGGGGGLCCGGLLQLQLLQNARRLLRRKLQVPLLLLLALLLLKLLILLLLLLLSLSS
AALAEAEAEEEPEFFTTAIIFVRLWFWVFVVFLLLLLLLLLFFFFFRRLCLLGLALAAAALARRRLWRRR
RRECCCGCCCCCCKCCCIVIIIDGIIIINECCCCCCLCCRRCQDDPLCPPRIKKKKRKRKRAAAPAPAAA
PAAPAAPPPPPPV
>gnl|CDD|443109 COG3903, COG3903, Predicted ATPase [General function prediction only]
AAAAAAAAAAAAAAALALLALAAAAAAAAAAAALAAALEALRAALALLLLLLAALALALAALALLLAAAA
LLLRLLLLLLAARLLARLAAAAAAALARAAAAALALLLRLRLAARRLLLARALAAAALAAAAAAAAAAAA
APAPPPPAPPPPAPLAALARRAAALAAAARALLSAARLVTLTGPGGVGKTRLALEVAHRLADRFPDGVWF
VDLAGVTDPALVLAAVARALGVRDAPGRDPAARLRAALADRRLLLVLDNCEHVVDAAAALVRPLLPAAPG
LRVLATSREPLGLPGERVLPLPPLAVPPPGAEALASEAVALFVERAGAARPGFALDAAEAAAVAEICRRL
DGLPLAIELAAARLRTLSLAELAARLDDRLRLLTGGRRDAPPRHRTLRAALDWSYDLLSPAERRLLRRLS
VFPGGFTLEAAEAVCGGDGPADVLDLLAALVDKSLLEVEGGGGGPRYRLLETVREYAAERLAEAGERAAA
RRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWFLRGL
LREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALA
AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAA
AALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAA
ALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAA
AAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAA
AAAAAALAAAAAAAAAAAAAAAA
>gnl|CDD|443110 COG3904, COG3904, Predicted periplasmic protein [Function unknown]
MRRVLVALAALAALLLAPAAALAAPMTFEVVGPGCGCWIVAEGEITPGDAARLEALLETRGPGVATVVLN
SPGGSVAEALALGRLIRARGLDTAVPAGAYCASACVLAFAGGVERYVEPGARVGVHQPYLGGGDALPAAE
AVSDTQRATARLARYLREMGVDPELLELALSTPPDDMRYLTPEELLRYGLVTGPLPA
>gnl|CDD|443111 COG3905, PutA1, Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription]
STTTTTVRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREEWREALIQEGLAAADAGEFVSHEEVE
>gnl|CDD|443112 COG3906, YrzB, Uncharacterized conserved protein YrzB, UPF0473 family [Function unknown]
MAEEEEEIITLVDEEGNEVLFEVLFTFESEGFGKEYVILYPAGEEEDEEEEVQAFRYEEDEDGEEGELVP
IEDDEEWDMVEEVLNTLLEEEEEE
>gnl|CDD|443113 COG3907, COG3907, Membrane-associated enzyme, PAP2 (acid phosphatase) superfamily [General function prediction only]
MTTSSLRNSASRRFHLLLLLLLLLLLLLLFELTGLDLWLARLFYDPEGGQFPLRDNWLLELLLHDGGKWL
VILVAVLLLLLLLASFKRPRLRRYRRRLLYLLLSLALGLLVVSLLKSHTGRPCPWDLVEFGGDAPYVPLF
EPGPAGAGPGRCFPAGHASAGFALLALYFLLRRRRPRLARLGLAAGLALGLLMGLAQMLRGAHFLSHTLW
SAWICWLVALLLYWLLLRRPALEAAA
>gnl|CDD|443114 COG3908, COG3908, Uncharacterized conserved protein, DUF2093 domain [Function unknown]
MNRFERPSGGGEAKLRYLDGDFRVLRPGAFVRCAVTGEPIPLDELRYWSVDRQEAYASAEAALQRLLEAG
GKP
>gnl|CDD|443115 COG3909, CytC556, Cytochrome c556 [Energy production and conversion]
MKKTLLALALAALLAAALAAAAAAAPEDAIKARQAAMKAMGKNMGTLGAMAKGEVPYDAAAAAAAAATLA
ALAKLPPALFPEGSDKGKTEAKPEIWEDPADFKAKADKFEAAAAALAAAAGTGDLAALKAAFGAVGKTCK
ACHDDFRAKK
>gnl|CDD|443116 COG3910, COG3910, Predicted ATPase [General function prediction only]
MPYLRRVSLKREKVPDRDAYPFNLPAVRNLEGLEFHPPVTFFVGENGSGKSTLLEAIAVAAGFNPEGGSK
NFRFSTRESESALGEYLRLSRGLPKPRDGFFLRAESFFNVATYLDELAAEGPGILDSYGGRSLHEQSHGE
SFLALFENRFRGNGLYLLDEPEAALSPSRQLALLALIHDLVREGSQFIIATHSPILMAYPGATIYEFDED
GIREVAYEDTEHYQLTRRFLNNPERFLRH
>gnl|CDD|443117 COG3911, COG3911, Predicted ATPase [General function prediction only]
MMTRRIVITGGPGSGKTTLLNALARRGYACVPEAGREIIREQQAIGGDALPWTDPAAFAELMLEGRLRQY
REAEALSGPVFFDRGIPDVLAYLRLLGLPVPEHLETAAAAFRYDRTVFILPPWPEIYTQDAERKQSFEEA
LRTYEALVETYRALGYELIEVPKGSVEERVDFILSRLGLL
>gnl|CDD|443118 COG3913, SciT, Regulator of T6SS expression TagF, TagF/ImpM/SciT family (unrelated to teichoic acid polymerase TagF of B.subtilis, COG1887) [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport]
ARIGWFGKLPSRGDFVRRRLPRALIAAWDRWLQQGLAASREQLGPRWLDLYLTAPIWRFALPPGVGGEQA
VAGVLMPSVDRVGRYFPLTVAAALPADEPLPFPLALARLWFEQLEAAALAALRDGADAEQLLQALAALPP
PLLADPAAILALLGDFLETQTLESLEADLAAAWRQLLLALLLQPVAATSLWWTSGSDGVPPRTLLHLGLP
DPALFAALLAGL
>gnl|CDD|443119 COG3914, Spy, Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]
AAAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAA
AAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALA
LNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELD
PDNADAHSNLLFALRQACDWEVYDRFEELLAALARGPSELSPFALLYLPDDDPAELLALARAWAQLVAAA
AAPELPPPPNPRDPDRKLRIGYVSADFRRHAVGYLLEPLLEHHDRSRFEIYAYSTGPDDDALTQRLRAAA
DHWRDIPGLSDEEAAELIRADGIDILVDLSGHTAGNRLGVFALRPAPVQVSWLGYPGTTGLPAIDYFIAD
PYVLPPGAEAYYSEKLVRLPGSYLCYQPNDRAPEVAPLPTRADLGLPEGAVVFGSFNNLYKITPEVFALW
ARILKAVPNSVLLLKGGGLPEARERLRAAAAARGVDPDRLIFLPRLPRAEHLARYALADLFLDTFPYNGG
TTTLEALWMGVPVVTLAGETFASRVGASLLTALGLPELIATSEEEYVALAVALATDPELLAALRAKLRER
RQTSPLFDTPRFARDLEAAYRQMWQRWC
>gnl|CDD|443120 COG3915, COG3915, Uncharacterized conserved protein [Function unknown]
MKLLRLLALLLALLLLPAAAAAALPAPAGPVILTVSGKIGNTNAGGAATFDLAMLEALPQTEITTTTPWT
DGVQTFRGVLLRDLLAAVGAKGTTLRAVALNDYAVEIPISDLEEYGVILAYRMDGKPMSVRDKGPLWLIY
PYDDYPELQTEVYYSRSVWQLKRIEVE
>gnl|CDD|443121 COG3916, LasI, N-acyl-homoserine lactone synthase LasI (autoinducer biosynthesis) [Signal transduction mechanisms]
FEIISADNLHLHPELLDEMFRLRHRVFVEELGWEVPVPDGLEIDQYDDPSAHYLLAHDEDGRVVGCVRLL
PTTGPYMLEDVFPDLLDGGPAPRRPDIWEISRFAVDKDFRRRLGERARRPRVALALFLAMVEYALENGIT
HLVAVMEPRLERLLRRLGWPFEPLGPPVEIGGERAPAYLIDVDEETLARLRISGVLADALR
>gnl|CDD|443122 COG3917, NahD, 2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and catabolism]
TIDFYFDFSSPYAYLAATRLEALAARHGAEVRWRPVLLGAVFKATGGTPPAERIPAKGRYRLRDLARWAR
KLGLPFRFPPHFPVNPLLAARAALAAQDAGAAAAFVRAVFRAVWAEGRDIADPAVLAAIAAAAGLDAAAL
LAAAQSPAVKARLRANTEEAVARGVFGAPTFVVDGELFWGQDRLDFLEAALAGGGA
>gnl|CDD|443123 COG3918, COG3918, Uncharacterized membrane protein [Function unknown]
MSMTLLLALLIGVVAGLRAMTAPAALSWAARLGWLPLSGTPLAFLGSPLTAGVLTLLAAGELVGDKLPST
PSRTVPPQLGARIVSGALAGAALAAAGGARVGGALAGAIGAVAGTYGGYAARRRLAAAFGPDLPAALLED
AVAIALALLIVAALR
>gnl|CDD|443124 COG3919, COG3919, Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]
AMTMRFRVVVLGGDINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPGDDPEAFVDALLE
LAERHGPDVLIPTGDEYVELLSRHRDELEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDS
ADDLDALAEDLGFPVVVKPADSVGYDELSFPGKKKVFYVDDREELLALLRRIAAAGYELIVQEYIPGDDG
EMRGLTAYVDRDGEVVATFTGRKLRHYPPAGGNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDP
RDGEYKLIEINPRFWRSLYLATAAGVNFPYLLYDDAVGRPLEPVPAYREGVLWRVLPGDLLLRYLRDGEL
RKRLRELLRRGKVVDAVYALDDPLPFLRALRR
>gnl|CDD|443125 COG3920, COG3920, Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms]
LLLALLLLLLLALAALLLLAALLLLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVA
LAAAVGAAAALLALLVLLLLLLLAAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLL
LAILALAELAVALAELAAALLLLAEELAALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLL
ALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITE
RKRAEEELEASLEEKELLLRELHHRVKNNLQVVSSLLRLQARRADDPEAREALEESQNRIQALALVHELL
YQSEDWEGVDLRDYLRELLEPLRDSYGGRGIRIELDGPDVELPADAAVPLGLILNELVTNALKHAFLSGE
GGRIRVSWRREDGRLRLTVSDNGVGLPEDVDPPARKGLGLRLIRALVRQLGGTLELDRPEGTRVRITFPL
AELAA
>gnl|CDD|443126 COG3921, COG3921, Uncharacterized conserved protein, contains Extensin-like_C domain [Function unknown]
MRRPLLLLLLLLLALAALAACGAPRAPAPERNPWAPLALADPPGPATRAKLARLRADEAACLARLRRAGV
RFEPLPPISGGPGGCGIDDPVRVSAVGGGVALSPAATLSCPLAAALARWVREVVQPAARRRFGSPVVRIE
HAGSYSCRNRNGRRGARLSEHAFGNALDIAGFVLADGRRISVLRDWRGGGAEAAFLRAVRDGACGRFGTV
LGPGYNAAHADHFHLDLARRRSGYRYCR
>gnl|CDD|443127 COG3923, PriC, Primosomal replication protein N'' [Replication, recombination and repair]
MKTSQLLQTLEQQLDQLAQQIAPLADHRTLQARFDRQLFSTRSTRLQDYLQEARQNLAQLEQAVEANRTQ
QVAFLAERLVAQIAALQRELATQSLRKQEPRSASKPILDLYQKLAQHQEYERRLLAMIRDRESQLEQATT
LAEQQRLQKELAALEGRLARCRQALARIERQIERRERGF
>gnl|CDD|443128 COG3924, YhdT, Uncharacterized membrane protein YhdT [Function unknown]
EMDKRFKQANKEALWALGLTLLYFIWWYLFAYGLGSGTGIFGLPLWFELSCILGPLLFIVLCWLMVKFIF
KDIPLEDEDEEI
>gnl|CDD|443129 COG3925, FruA, N-terminal domain of the PTS fructose-specific IIB component [Carbohydrate transport and metabolism, Signal transduction mechanisms]
MKTLLITDASLGNAKAYLAKQMLSAAAAKAGLTLVENPAEADLVIVFGDAIPNDPALNGKKVYLGDAEEA
LNAPEAFLAQAKAEAKPYQAPAAAAAAPVSASGKKIIVAVAACTTGVATTFMAAAAEEEEKKKQGWWVVV
ETRGVGGGGNIIPEEEEAAADVVVAAADIDVDLKKFKKKKMYRTTTGLALKKTQEEDDAAFAEAIFYQGQ
QTGTASASASEKEKGGHLLLLLTHLLMMVVVVVGGGLLIALSFFFFIAFGKVAKAAGGALAAGGGGGGGA
AMVLLIAGAAAAAIAFAPGLGGGLGGGLGGAGAGSGGGGGIGGGIAAGAAAAKVKLLLSLPLKLEALKLI
LIIILLLSLILGLVIGIIIVVPVAALAAALSLWLTGMGGANAAVLGVLLGAMMGMMMGGGGGAVAYAAAV
GLTLSQASAAAAAAMAAAMAPPMPALGAAAAARRKKRKKEQEGGAAGAALGLCGIIEGAGAAAAPDAARP
IVCIAIGGAGGGAASMAISAAAGALHGGGLLLLIIPIIPPPLGILLALLIAGLVGGLLAALLKKVEKAPE
AAA
>gnl|CDD|443130 COG3926, ZliS, Lysozyme family protein [General function prediction only]
NFDQALDFILKHEGGYVNHPADPGGATNYGITQATLRAYRGLRDVTAGDVRALTREEAKAIYRRDYWDRP
RGDELPQGLAAEVFDFAVNSGPGRAIKLLQRALGALPDVTVDGIIGPKTLAALNAADPAVLIDAYCDARL
AYYRSLVERRPSQEKFLRGWLRRVESL
>gnl|CDD|443131 COG3930, COG3930, Uncharacterized conserved protein, DUF1704 domain [Function unknown]
MYRPHFAALGRRAYLAAVLELDDRLVELQKPIRILDAINPINIEQEKERFFASKFRELPEFRYRPLPFDP
EALKRELYSLRLEIIEDPPLGKLLRRKIDEYSRVIQMLEARGTPDFYYNSLRLYGSPSDKLIDNARFILD
LADEELLEEPEEKTLSAEEAAARLQERLDRYFPGFPVRVEVSDDIVADAMVGGDRLKIRKNARFSERDLE
ALEHHEIGVHVLTTLNGRAQPLKILSKGLPGYTETQEGLAVLSEYLSGGLTPARLRRLALRVIAVDMAED
GADFLDTFRLLREQYGLSREDAFTITLRVFRGGGFTKDALYLRGLVEVYNFLRSGGDLPLLFVGKVALED
LPVLQELVDRGLLRPPKYLPPWLRDLNSNNPRLDRIRAHYK
>gnl|CDD|443132 COG3931, HutG2, Predicted N-formylglutamate amidohydrolase [Amino acid transport and metabolism]
TSLAPDDPAPVEVINPDGRSPVLLVCDHASNAVPAALGDLGLPAADLERHIAWDIGAAGVARALAERLDA
PLVLSRYSRLVIDCNRPPDDPTLIPELSDGTVIPGNRGLSAAERAARLAAIYRPYHDAIAALLAARLARG
RPPVIVSIHSFTPVYKGVPRPWHIGILHDRDPRLADPLLAALRAEGDLVVGDNEPYSGADGVDYTLDRHA
EARGLPNVLIEIRQDLIADEAGQAAWAERLARLLRAALAALG
>gnl|CDD|443133 COG3932, ExoD, Exopolysaccharide synthesis protein ExoD [Cell wall/membrane/envelope biogenesis]
MTTPDRPRRLSEILDRLAEAAPGERVTLGDLLDALGERSFGPLLLLLALPFLLPLPGPGVSTIFGLPILL
IAAQMLLGRRHPWLPGFLARRSIPREKLRKALKRLRPWLRRLERLLRPRLTFLTSPPGRRLIGLLCLLLA
LLLMLPIPFTNTLPALAILLLALGLLERDGLLVLAGLVLGLAAVALVASVLYALVAAGAALLSWLK
>gnl|CDD|443134 COG3933, LevR, Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription]
KELSKKTESKVTNLNEAIAKARDLKELIKSKLLKESTGLLKLLALLLLLKRLSELLLELKKLKKEKKTLK
KERSLLEKKKNKLNLKEEKKEKLDFKALIGLSLSLLSAAAAAKAAKPPPPLGLLTLLLGGTGGGKSAFAG
YMYAFAAKIAELAAPFVFFNFANAAYNPNLLLLLLFGLGGGAGGGAGADGGGLGGAAGAGGGLLDLLDEL
PLEGEEQEELFFLLGKGLFRGEGGESRSRRVRIIRATTETEESLLLTTLTRRIRIIIILPRLPILERRER
ERLLLLLFEFEEEEIRIIKILIVLLLALLLLLLYVNNLGQLGLLKLLIKAAAAAALAKAIKEATIILRLL
SKLLKLLLLLLLNERLLLLELKILIEPLDIFFDSSASSDESDESEEDENLYEIIEIKKKLLLELGIDEEE
INIIIEIDIDVHLLKFIYDDNKNFNKEELAKIVDEDIINVVEEILELAEKKLGRKFSENFIYALSLHLSS
FIERIKEGKEIINPNLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTLFLVSLNENNESGKVG
VIVLAHGYSTASSMAEVANRLLGTNIFEAIDMPLDMSPEDILEKLKEYVKKIDTGKGVLLLVDMGSLTTF
GEIIEEETGIPVKTIDMVSTPLVLEAGRKALLGMSLEEIYESLKNFNPYEKIISKNKPEKNKKKAIITTC
FTGEGTAVKIKDLLEKSLPEDEDNIEIIPLDYLELEEFKEKIDEIFKEYEILAIVGTIDPEIPDIPFISL
EDLISGEGIEKLQKLLGGELDAEEIEEINNEIIKNFSLESLIESLTILNPEKIINELEDFISRLENLLGI
KLDNDVKIGLILHIACMIERLVTGEEILTYPNKEEFIQENESEYAVIKEAFSPIEEKYNIKIPDSEIAYI
YDILKN
>gnl|CDD|443135 COG3934, COG3934, Endo-1,4-beta-mannosidase [Carbohydrate transport and metabolism]
LDGKPYFFLGVNYWPRAGGFHMWRDWDPDRVRRELDDLAALGLDVVRVFLLWEDFQPNPGLINEEALERL
DYFLDAAAERGLKVVLTLFNNWWSGHMSGYNWLPSWVGGWHRRNFYTDPEAVEAQKAYVRTLANRYKDDP
AILGWELGNEPRNFGDPASPEAALAWLREMAAAIKSLDPNHLVSSGDEGDYWEVDDHPFVPAHAAPLIDY
LTVHLYPFNWGWVDRPRSTDKAAYLIELARALGKPVVLEEFGAPRDSPQASEEDRAEFYRTVLEAALTLA
GAAGANWWCFHDFDDLGDPPYEDQPLFGLFDSDGRPKPTAEVIREFARELK
>gnl|CDD|443136 COG3935, DnaD, DNA replication protein DnaD [Replication, recombination and repair]
LFEFYEQNFGRPLSPFEIEKINKWLDEDGFSPELILEALKEAVENGKRNFKYIDRILKNWKKKGIKTVED
AEAYEKKFKKRKKKKTSKSKSNFEQKPDWYDKE
>gnl|CDD|443137 COG3936, YfiQ, Membrane-bound acyltransferase YfiQ, involved in biofilm formation [Carbohydrate transport and metabolism]
MKLSIKETFYLRGILCLSIVLHHIITMTTLKSDVSLNQVEVLFIFRLLLMFATPVFIFLSEFLLAYSYKQ
NYPKGFLKKRLQYIFIPYLIIALIYAIYESLIKTNADFVDSFLTNIFLGNWHGWFILVIFQFYLLFYLFF
KFLKKYNPAVVVLLSLLINYVYLAYFNNFGAKTIFLGWLFYFVLGYYMGKNYERFLKFLEKYRIFIVIFA
ILAFGFFIYGALSGNLTEVTSKRFDLIPYTISVIFLVFLLLMKVKLVPKFLNFISNYSFEIYLIHPLILI
LLGSFFVSLEDSPLLYVLLVFLLTVGSAILVSKLLNKLPFGKLIVGKIKKPKLV
>gnl|CDD|443138 COG3937, PhaF, Polyhydroxyalkanoate synthesis regulator phasin [Secondary metabolites biosynthesis, transport and catabolism, Signal transduction mechanisms]
MEDLLKKLLLAGLGAASLTKEKAEELVDELVEKGELTEEEAKKFVDELVEKGEEEKEELEEKIEEQVEEA
LEKLGLATKEEVDELEERIDRLEKQLRELENKK
>gnl|CDD|443139 COG3938, PrdF, Proline racemase/hydroxyproline epimerase [Amino acid transport and metabolism]
MRSSRTITTIDAHTEGEPTRVVTGGVPPLPGNTMLEKRRYFAENYDWLRRLLMFEPRGHADMSGALLVPP
TRPDADFGVIFMETSGYLPMCGHGTIGVATVLLETGLVPMTEPVTEVVLDTPAGLVRARAEVEDGKVESV
TFENVPSFVYALDVEVEVPGLGTVTVDIAYGGNFYAIVDAQQLGLDLEPENARELIRLGLEIRDAANEQL
EVVHPENPDINGVSHVEFTGPPTDPDADARNAVVFGPGAIDRSPCGTGTSARMALLHARGELKVGETFVH
ESIIGSRFTGRILEETTVGGYPAIIPEITGRAWITGFNQFVLDPDDPLPEGFLLR
>gnl|CDD|443140 COG3940, COG3940, Beta-xylosidase, GH43 family [Carbohydrate transport and metabolism]
NPLIEQGADPWVYKHDGYYYFTATVEYDRIVLRRSKTLAGLATAEPVVVWTPPASGPMSKNIWAPELHFI
DGKWYIYFAAGDGEDNNFNHRMYVLENASADPLTGPWTEKGQIKTPWDSWAIDATVFEHNGKLYLVWSGW
EGDINGNQNLYIAEMSNPWTLSGPRVLLSKPEYDWEKIGFKVNEGPAVLKHNGKVFITYSASATWDPNYC
LGLLTADAGADLLDPASWTKSPEPVFQTSPENGVYGPGHNSFTKSPDGKEDWIVYHARSYPEIGCDPNRH
TRAQKFTWNADGTPDFGTPVPDGTPLPKP
>gnl|CDD|443141 COG3941, HI1514, Phage tail tape-measure protein, controls tail length [Mobilome: prophages, transposons]
QAARAFKRELDGLSRSGKSAAGKLESSFSRAAGGIAAAFGLNAAAGFGKSGVKTAAEFEQLQISLNTLLG
SAEKAAEALAWLKEFAADTPFELAGLTDAYKKLLAFGLDAEPTRGILTALGDAAAALGGSQEQLEGATLA
LGQMWAKGKLQGEELNQLAERGVPAWKLLAKAMGVTVAELQKMVEKGKLGAEDAIPALLDAMGKRFGGAA
AAQMKTLSGMVSNLGDAWTEFLAAVGDSGAFDALKNGLQGLLELLDELAEDGFAKGVSAALITAFEAAKT
AYEVADALGKVLAAIVGLAALGLATALAAVLLAAGALALAQALAAALAGAAAAAADAILALAVLVAAAAA
AAATAGGTLGSAATALEALAAFAALSSASLEGTVSAVADAADLSREAANLLAAAANALAAAKAFGAIAVT
FAGLADELLLTAAAAAAAAREALALAAAGGLGRAAAATAAIAVLDYEAEAGQKASKLAKAGTDTQAELQL
ASEGLAKKVALSLLKLALAAATTSLAQAAATAATDEGVTAIAADGLAEADLSTAGSSNAAGNAAAGQAEL
IAEAAGAGSDAGLKEAAEAAVAQNAAAAAATAQASAADLKALEAEKKAAEARAAKEQLVSAAAGAQAALN
GAEAGGELLEIQKLAAELVAKAKKALEAELQVKAKQLAAAALTEKAAALAADQAEKASAQLGAAKKEATA
SAIVSGRAAGEKGKLAASQGQAELQAAKVLAANAAQEVAAAEAAAAEQAAAKALAGAETQLAAAAKKVAD
LAKLAKAAEAENEALAAAADAILESQGIQSLANKQAELEAEKAGNLALAKQVIEIKNLALKDL
>gnl|CDD|443142 COG3942, COG3942, Surface antigen [Cell wall/membrane/envelope biogenesis]
ARAASLGDGYPPNVVDPWNGYPYGQCTWYAAWRRAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGA
VAVFTPGVAGPYGHVAVVESVNSDGSILVSEMNWGGPGIYSTRTISAGNASSYGFIHPK
>gnl|CDD|443143 COG3943, RhuM, Uncharacterized protein RhuM, Salmonella virulence factor [Function unknown]
RMSTSEILIYQTEDGETKIEVRLEDETVWLTQKQMAELFGVDVSNISKHLKNIFEEGELDEEATVRKFLT
VASEGKREVTRNVKHYNLDAIISVGYRVNSKRATQFRQWATQVLKEYLIKGFVLDDERLK
>gnl|CDD|443144 COG3944, YveK, Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]
EMDLREYLRILRRRWWLILLLTLLGALAALASSFLITPVYQASTTLLVSTSSGSDASDLYQGIQTAQQLV
NTYAELLKSPAVLEEVIDELGLDLSPEELAKKISVTSPPDTQVITITVTDTDPERAADIANAVAEVFAEE
VKELMKVDNVTVLDPATVPASPVSPNPKLNLAIGLVLGLLLGVGLAFLRELLDTTIRSEEDIERLLGLLL
GGAVPAARSARPLLLLLADASPRAAAARRRRRNLLFALAAVDARTVVVVSSSLSEGKSTTTAALALALAA
AAAGVVLVLADLDRRRRVALLGLLEGAGL
>gnl|CDD|443145 COG3945, COG3945, Hemerythrin domain [General function prediction only]
MSATEILRAEHRNIRRLLAVLEKLLDRLEEGEEVDFELLRDILDYIREFADRCHHPKEEDILFPRLEERG
GEAAGPIAVLLAEHEQGRQLTRELEEALEAYLAGDVVARDELAAALRAYIALLRQHIAKEENVLFPLAER
LLSDEDWEELGEAFEEVEDPLFGEGVHERYEALVERLEKA
>gnl|CDD|443146 COG3946, VirJ, Type IV secretory pathway, VirJ component [Intracellular trafficking, secretion, and vesicular transport]
MKRLIRLVLLAALLLAAAAATLAYAPWTVSLSDLPLVELPAKGPADTLAVFYSGDGGWRDLDKSVAEALA
AQGVPVVGVDSLRYFWSERTPEQTAADLARIIRHYRARWGKKRVILVGYSFGADVLPFAYNRLPPALRAR
VSLVALLALSKTADFEIHVEGWLGAGGDGLPVAPELAKLPAAKVQCIYGTEEDDSACPALKAPGVEVIKL
PGGHHFDGDYEALAKRILAAL
>gnl|CDD|443147 COG3947, SAPR, Two-component response regulator, SAPR family, consists of REC, wHTH and BTAD domains [Signal transduction mechanisms, Transcription]
AVPYVVKPAQPEELLN
>gnl|CDD|443148 COG3948, COG3948, Phage-related baseplate assembly protein [Mobilome: prophages, transposons]
ATIDLSQLPAPDVVETLDFETILAERKADLEALYPEVTGTTLLESDPLRKLLEVNAYRELLLRQRINEAA
KANLLAYATGADLDHLGALFGVERLVIQPADTTARPPVAAVMESDDDLRERIQLAPEGFSVAGPEGAYEF
HALSADGRIADVSVISPAPGEVTVYVLSREGDGTPSAELLAAVLAALSAEDVRPLTDRVTVQAATIVDYQ
IDATLYLYPGPDAEAVLAAARAALEAYVAQQHRLGRDIVPSAIYAALHVAGVQRVELTSPAADVVLDDTQ
AAYCTGITVTVGGVDD
>gnl|CDD|443149 COG3949, YkvI, Uncharacterized membrane protein YkvI [Function unknown]
MSKKFKRILKIAAAYIGTVIGAGFASGQEILQFFTSYGIWGLLGILLATLLFALVGALILELGRRLKAYS
YRELFKYLFGPYLGKLFDILYLLFLFGVLAVMLAGAGAILEEQFGLPYWLGSLIMAVLVLLTVLLGLEGV
VKVNSFIVPLLIIFVILIAIYSLFTNGGSISALAAIASSIPTASGNWLLSALLYVSYNLALAVAVLVPLG
GEIKSRKEAVAGGLLGGLGLGLLALLINLALLANYPEIADAEIPMLYLAGQIGPWLGLIYSVVLFLAIYT
TAVGNLYGLAARISEVGTKRYKIIALILLLLAFPLSFFGFSNLVSKLYPLFGYLGLVLLVILLLGWIKKK
KK
>gnl|CDD|443150 COG3950, COG3950, Predicted ATP-binding protein involved in virulence [General function prediction only]
MRIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGE
FGDSAKLILYYGTSRLLLDGPLKKLERLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDE
LDEKLEAVREALNKLLPDFKDIRIDRDPGRLVILDKNGEELPLNQLSDGERSLLALVGDLARRLAELNPA
LENPLEGEGIVLIDEIDLHLHPKWQRRILPDLRKIFPNIQFIVTTHSPLILSSLEDEEVIVLERDE
>gnl|CDD|443151 COG3951, FlgJ1, Rod binding protein domain [Cell motility]
MSISSSLSSSLALDAQSLNALKAAAKADDDAALKEAAQQFEALFLQMMLKSMRKAVPEDGLFGSQAEDMF
RDMLDQQLAKELAKGGGLGLADMIYRQLSRQQEAAAA
>gnl|CDD|443152 COG3952, LABN, Uncharacterized N-terminal domain of lipid-A-disaccharide synthase [General function prediction only]
LNMGDLAQILFVNEAIPLWWLLLGFVGQALFTLRFVVQWIYSERAKRSVLPVGFWYLSLLGSLLLLIYAI
FRKDPVFILGQSFGLFIYIRNLYLIRKEKKRAPAA
>gnl|CDD|443153 COG3953, SLT, SLT domain protein [Mobilome: prophages, transposons]
KNDGGGIVGKGGVAGNKVGGVKGKSKNGLSFFASGASGSGLNGDTSVAAGAANKNLGTGPAGGFITSIGG
GALVGGSGGAETRGVGTGGAAASGAGPTSGGGAAAAGIGAGGAGNWLGNQAASGSSGAIGVAGGGKKVAG
AANKAAKASSKAVAKGKTKAVKGGGGISSGSGGGAQAATGKGGGGLGKGASKALGGAGAGAGGGGGVGGG
AGGWGIDIRQAAALGVPVSEAWVDGILRIIQHESGGNPNAINLWDSNAAAGTPSKGLMQVIPPTFNAYKL
PGHGNIYNPVDNILAGINYAKSRYGSSDNVPGLASLGQGGGYHGY
>gnl|CDD|443154 COG3954, PrkB, Phosphoribulokinase [Carbohydrate transport and metabolism]
MSVKHPIIAVTGSSGAGTTTVKRAFEHIFRREGINAAIVEGDSFHRYDRAEMKAAMAEAEAEGRHFSHFG
PEANLFDELEELFREYGETGTGKRRHYLHNDEEAAPYGQPPGTFTPWEDLPEGTDLLFYEGLHGGVVTDE
VDVAQHVDLLIGVVPIINLEWIQKIHRDTAERGYSTEAVTDTILRRMPDYVHYITPQFSRTDINFQRVPT
VDTSNPFIARDIPTPDESLVVIRFRDPKGIDFPYLLSMIHGSFMSRANTLVVPGGKMGLAMELILTPLIH
QLMERRRRA
>gnl|CDD|443155 COG3955, COG3955, Uncharacterized conserved protein, DUF1919 family [Cell wall/membrane/envelope biogenesis]
LLIGIIRRKINKFFRKNFNFKNYQKLKNKEFTIISNNCWGGFIYHDLGLPFNSPFVNLFLYPDDFIKYLK
NIDYYLSQELTFIKESPVYEKNYPVGKLGDIEIHFMHYHSEEEAREKWNRRKKRINLDNLFIKMTDRDGN
SEEDLKEFDKLPFKNKVVFTHKPYNELKSAVYIKGYEWQCKVGFNGWNGKKYYDLTYLQFDYVNWLNKSK
DI
>gnl|CDD|443156 COG3956, YabN, Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only]
MENREKPLYAFERLLEIMARLRDPDGCPWDREQTHESLRPYTIEEAYEVADAIERGDLDELKEELGDLLL
QVVFHAQIAEEEGAFDFDDVIDGISEKLIRRHPHVFGDVEVEDAEEVLANWEKIKAQEKAEKGEGRKSVL
DGVPRSLPALMRAYKLQKKAARVGFDWPDVEGVLDKVEEELAELKEALASGDQEAIEEELGDLLFALVNL
ARHLGIDPEEALRRANRKFERRFRYIEAAAAEQGKSLEDLSLEEMDALWQEAKKAEKE
>gnl|CDD|443157 COG3957, XFP, Phosphoketolase [Carbohydrate transport and metabolism]
TDPLSPEELEKIDAYWRAANYLSVGQIYLLDNPLLREPLKPEHIKPRLLGHWGTTPGLNFIYAHLNRLIR
KYDLNMIYIAGPGHGGPAMVANTYLEGTYSEIYPDITQDEEGMRRLFKQFSFPGGIPSHVAPETPGSIHE
GGELGYSLSHAYGAAFDNPDLIVACVVGDGEAETGPLATSWHSNKFLNPARDGAVLPILHLNGYKIANPT
VLARISDEELEALFRGYGYEPYFVEGDDPAAMHQRMAAALDTAIEEIRAIQKEAREGGDATRPRWPMIVL
RTPKGWTGPKEVDGKPVEGTWRAHQVPLADVRDNPEHLALLEEWLRSYRPEELFDEDGRLRPELAALAPK
GDRRMGANPHANGGLLLRDLRLPDFRDYAVDVPKPGTVRAEATRVLGKYLRDVMKLNPDNFRIFGPDETA
SNRLQAVFEVTDRQWMAEILPEDEHLAPDGRVMEVLSEHQCQGWLEGYLLTGRHGLFSSYEAFIHIVDSM
FNQHAKWLKVSRELPWRRPIASLNYLLTSHVWRQDHNGFSHQDPGFIDHVVNKKADVVRVYLPPDANTLL
SVADHCLRSRDYVNVIVAGKQPAPQWLTMDEAIKHCTRGIGIWDWASNDDGGEPDVVLACAGDVPTLETL
AAVDILREHFPELKIRVVNVVDLMKLQPPSEHPHGLSDEEFDALFTTDKPVIFAFHGYPWLIHRLTYRRT
NHDNLHVRGYKEEGTTTTPFDMVVLNDLDRFHLVIDVIDRVPRLGSKAAHLKQRMEDKLIEHRAYIREHG
EDMPEIRDWKWPDLK
>gnl|CDD|443158 COG3958, TktA2, Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]
MEKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK
IPFVSTFAPFLTGRAYEQIRNDIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPAD
AVETEAAVRAAAEHDGPVYLRLGRGAVPVVYDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELL
AKEGISARVINMHTIKPLDEEAILKAARKTGAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRF
GESGSPEELLEKYGLDAEGIVAAAKELL
>gnl|CDD|443159 COG3959, TktA1, Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]
TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGH
AAPALYAVLAEKGYFPKEELATFRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMALAAKLDGKDY
RVYVLLGDGELQEGQVWEAAMAAAHYKLDNLIAIVDRNGLQIDGPTEDVMSLEPLAEKWEAFGWHVIEVD
GHDIEALLAALDEAKAVKGKPTVIIAHTVKGKGVSFMENRPKWHGKAPNDEELEQALAELEAELGDY
>gnl|CDD|443160 COG3960, Gcl, Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism]
ARMRAVDAAVAVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHVLARHVEGASHMAEGYTRAKAGNIGV
CIGTSGPAGTDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVLEPAQVPR
VFQQAFHLMRSGRPGPVLIDLPIDVQMAEIEFDIDTYEPLPVYKPAATRAQIEKALDMLNAAERPLIVAG
GGIINADASDLLVEFAELTGVPVIPTLMGWGSIPDDHPLMAGMVGLQTSHRYGNATLLASDFVLGIGNRW
ANRHTGSLDVYTKGRKFVHVDIEPTQIGRVFAPDLGIVSDAKAALELFVEVARERKAAGKLPDRSAWAAE
CQERKRTMLRKTHFDNVPIKPQRVYEEMNKAFGRDTRYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPL
GWTIPAALGVVAADPDRPVVALSGDYDFQFMIEELAVGAQFKLPYIHVVVNNSYLGLIRQAQRGFDMDYC
VQLAFENINAPELGGYGVDHVKVAEGLGCKAIRVTDPEEIAPAFEEAKALMAEHRVPVVVEVILERVTNI
SMGTEIDNVNEFEELAESPADAPTAIAL
>gnl|CDD|443161 COG3961, PDC1, TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]. TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
MPMTYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGA
LVTTYGVGELSAINGIAGAYAERVPVVHIVGAPGTRAQRRGPLLHHTLGDGDFDHFLRMFEEVTVAQAVL
TPENAAAEIDRVLAAALREKRPVYIELPRDVADAPIEPPEAPLPLPPPASDPAALAAAVAAAAERLAKAK
RPVILAGVEVHRFGLQEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCV
LCLGVVFTDTNTGGFTAQLDPERTIDIQPDSVRVGGHIYPGVSLADFLEALAELLKKRSAPLPAPAPPPP
PPPAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTSLFGAADLRLPEGATFIAQPLWGSIGYTLPAALGA
ALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGYTIERAIHGPDGPYNDIANWDYAKLP
EAFGGGNALGFRVTTEGELEEALAAAEANTDRLTLIEVVLDKMDAPPLLKRLGKA
>gnl|CDD|443162 COG3962, IolD, TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism [Carbohydrate transport and metabolism]
MMKTIRLTVAQALVRFLANQYVERDGEEQPLFAGVFGIFGHGNVAGLGQALEQDPDELPTYQGRNEQGMA
HAAIAYAKQKNRRRIMACTSSIGPGATNMVTAAALATANRLPVLLLPGDTFATRQPDPVLQQLEHFHDPT
ISVNDAFRPVSRYWDRITRPEQLMSALPRAMRVLTDPAETGAVTLALPQDVQAEAYDYPESFFAKRVHRI
RRPPPDPAELARAVELIRAAKRPLIIAGGGVRYSEATEALRAFAEATGIPVAETQAGKGALPWDHPLNLG
GIGVTGTLAANALAAEADLVIGVGTRLQDFTTGSKTLFANPDVRFVNINVARFDAYKHDALPVVADAREG
LEALTEALAGWRYPAAWTDEAAELKAEWDAEVDRLYAPTNGGLPTQAQVIGAVNEAAGPDDIVVCAAGSL
PGDLHKLWRTRDPGTYHVEYGYSCMGYEIAGGLGVKLAEPDREVYVMVGDGSYLMLNSELVTSVQEGKKI
IVVLLDNHGFGCINRLQMSTGSQSFGTELRDRDTETGRLDGGLLPVDFAANAASLGAKAYRVTTIAELRA
ALERAKAADRTTVIVIKTDPKTMTPGGGSWWDVGVAEVSERESVRAARAEYEEARAKQRRYL
>gnl|CDD|443163 COG3963, COG3963, Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism]
RLKSRLSDELLFLREFLRNPRTVGAIAPSSRALARAMASEVDWSGAGPVVELGPGTGVFTRAILARGVPD
ARLLAVEINPEFAEHLRRRFPRVTVVNGDAEDLAELLAEHGIGKVDAVVSGLPLLSFPPELRRAILDAAF
RVLAPGGVFVQFTYSPRSPVPRKLLRRGFEAVRSGFVWRNLPPARVYVCRKPR
>gnl|CDD|443164 COG3964, COG3964, Predicted amidohydrolase [General function prediction only]
DLLIKGGRVIDPANGIDGVMDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTHVFPGGTDY
GVDPDGVGVRSGVTTVVDAGSAGAANFDGFRKYVIDPSKTRVLAFLNISGIGLVGGNELQDLDDIDPDAT
AAAAEANPDFIVGIKVRASKGVVGDNGIEPLKRAKEAAKEAGLPLMVHIGNPPPPLDEVLDLLRPGDILT
HCFNGKPNGILDEDGKVRPSVREARKRGVLFDVGHGGASFSFKVAEPAIAQGFLPDTISTDLHTRNMNGP
VFDLATVMSKFLALGMPLEEVIAAVTWNPARAIGLPELGTLSVGADADITIFDLREGPFGFTDSEGETLE
GDRLLEPEATVRGGKVVYDLNGIAAP
>gnl|CDD|443165 COG3965, COG3965, Predicted Co/Zn/Cd cation transporter, cation efflux family [Inorganic ion transport and metabolism]
SRTEQRLLKLSIAGTLLFAVLGIVFGLLSGSQAILFDGVYSLIDAGMTLLSLLVARLIARPDSRRFQFGY
WHLEPLVLAIKGLILLLLCLYALVNAVGSLLDGGREIEFGLALVYALVATVGCFGIALYLRRANRRLRSE
LVRLDAKAWLMDGLLSAALLVAFILAYLLQGTGLAWLAPYVDPAILALLSLVFLPVPLRIVRQALREVLL
MAPPEELDARVREVMEAIVARYGFLDYRSYVAKVGRKLFIEIYFLVPPDFPARTIEELDAIRDEIADALG
DEGPDRWLTISFTADPRWAE
>gnl|CDD|443166 COG3966, DltD, Poly-D-alanine transfer protein DltD, involved in esterification of teichoic acids [Cell wall/membrane/envelope biogenesis]
MKKRLKAIFGPLILALVLLAGLLFFPTKKIKLISEKTVKNAATSLSPNVFKGRTIKQKALSDPRYVPFFG
SSELSRFDAFHPSVLAEKYNRDYTPFLLGRGGTQSLTHALNMQSMGDELKNKKVVFIISPQWFVKKGVDP
GAFQSNFSPLQAYNFLFNDKISEETKRYAAKRLLKLDSVKSDAILKKLLEKIAAGKKLSKVDKVYLKLYR
SMLEKEDLLFSYFILDGYKKKIDPQLKKLPKTYNWEELDKLAEEEGKKRTNNNPFGIDNSFYKKRIKPKL
KKLKGSQKNFDYLKSPEYGDLQLVLDVFKKLGAKVLFVIPPVNGKWYDYTGLSKEMRQQFYKKIKYQLES
QGFNVADLSKDGYDPYFMQDTIHLGWKGWVAVDKALDPFLKEKKPANYKINDYFLSKDWQQLK
>gnl|CDD|443167 COG3967, DltE, Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism]
MKLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPGLHTIVLDVADPASIAALAE
QVTAEFPDLNVLINNAGIMRAEDLLDEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSG
LAFVPLAVTPTYSATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGDPRAMPLDEFADEVM
AGLETGKYEILVGRVKLLRFAERLGPYAAFAIMNAA
>gnl|CDD|443168 COG3968, GlnA3, Glutamine synthetase type III [Amino acid transport and metabolism]
MSTLRFQAIEEATNRKPVPVTAPMEKVSEIFGSNVFNDAVMRERLPKEVYKSLKKTIEEGEPLDREIADV
VAAAMKDWAIEKGATHYTHWFQPLTGLTAEKHDSFISPDGDGKAIEEFSGKELIQGEPDASSFPSGGLRA
TFEARGYTAWDPTSPAFIKETGNGTTLCIPTVFISYTGEALDKKTPLLRSMEALDKAATRVLKLFGDKDV
KKVTSTLGPEQEYFLVDKALYNARPDLVLTGRTLFGAPPPKGQQLEDHYFGSIPERVLAFMKDLERELWK
LGIPAKTRHNEVAPGQFELAPIFEEANLAVDHNQLLMEVMKKVARRHGLVCLLHEKPFAGVNGSGKHNNW
SLSTDTGVNLLDPGKTPHENLQFLTFLVAVIKAVDKYADLLRASIASAGNDHRLGANEAPPAIISVFLGD
QLTDVLDQIEKGKKLSSKEKGKLKLGVDTLPELLKDNTDRNRTSPFAFTGNKFEFRAVGSSASIAGPNTV
LNTIVAEQLDEFADELEALIAKGEDKDEAILKVLREYIKEHKRIRFNGNGYSDEWVKEAEKRGLPNLKTT
PDALPALLSEKNIELFEKHGVLSERELESRYEILLEQYIKTINIEARTMGDMARNHILPAAIKYQNELAE
NVAGLKEIGLEADAKAQTELLKEISELISELKKAVDALEEARKKANAIEDAREKAIAYRDEVLPAMDELR
YHADKLELLVDDELWPLPKYRELLFIR
>gnl|CDD|443169 COG3969, YbdN, Predicted phosphoadenosine phosphosulfate sulfurtransferase, contains C-terminal DUF3440 domain [General function prediction only]
MKKYLDENVYEAAQERIEWIFDEFDRVCVSFSGGKDSGVLLHLAAEVARKNGRKIDVLFIDWEAQYSATI
DHVEEMFERYEDVVRFYWVCLPLTTRNAVSQFQPEWYCWDPGKKEDWVRPMPEHDVITDPNFFPFYRYGM
EFEEFVPAFGRWLSGKHPTACLVGIRADESLNRYLAIASQRKLRYYKDKPWTTAPFGNAYNAYPLYDWKT
EDIWTANAKFGYDYNRLYDLMYQAGVPLSQMRVCEPFGDEQRKGLWLYHVLEPETWAKLVGRVNGANFGA
IYGGTKALGYRKISLPEGHTWRSYALFLLDSMPERTAEHYRNKIAVSLRWWQKRGGPLDEIPDDQDKDIE
GTKDIPSWRRICKCILKNDYWCRSLSFGPTKSEIYRRYALREKYKRILWGIL
>gnl|CDD|443170 COG3970, COG3970, Fumarylacetoacetate (FAA) hydrolase family protein [General function prediction only]
DQATLVGRVWRPGVGGGPRVVVVRGGRVYDLTAAAPTVSDLLEAPDPAAAVRAAAGERLGSLDDLLNSLG
APRDPADPRLLAPVDLQEVKAAGVTFARSMLERVIEEQAAEGLWSQYLEVYIGPDPEIFTKATPLRSVGP
GAPVGIRPDSEWNNPEPELVLVVNSRGEIVGATLGNDVNLRDIEGRSALLLPQAKDNNASCAIGPFIRLF
DETFTLDDVRDLEIRLTIEGEDGFVLEGSSSMAEISRDPEELVAQTLGRHHQYPDGFVLFTGTLFAPTQD
RDGPGQGFTHKPGDVVEISIPGLGTLVNTVVLSDEAPPWTFGIRALMRNLAARGL
>gnl|CDD|443171 COG3971, MhpD, 2-keto-4-pentenoate hydratase [Secondary metabolites biosynthesis, transport and catabolism]
TAATIEALAEALAEARRTRRPIPPLPDRYPPLTLEDAYAIQDALVARRLAAGRRVVGWKIGLTSKAMQEQ
LGVDEPDYGPLFDDMVLPDGATIPLSRFIQPRVEAEIAFVLGRDLPGPGVTLADVLAATDAVAPAIEIVD
SRIADWKIGLADTIADNASSGGFVLGPPPVDPDDLDLRNVGVVLEKNGEVVATGAGAAVLGHPLNAVAWL
ANKLAARGIPLKAGDIVLTGSLTPAVPVKPGDTVRADFGGLGSVSVRFV
>gnl|CDD|443172 COG3972, COG3972, Superfamily I DNA and RNA helicases [Replication, recombination and repair]
EKTPKVEKIERLLLAVEHLKKGLGGVRFLDVNDDGEDYAIELLKGLEEELAAKLEKVGLVLILLIKLDLD
EVLVASSGAEQVVLDGVRALFEVLLQVDRESVRNLTEDHLRSLRLLAASRRDFLFALLLPEIPPAPFVQA
LRLLNLVSLEDFFLPLIAVLDLQQERIARSIPDGPQRIRGVAGSGKTVLLAAKAAYLALKHPGWRILVTC
FNRSLADHLRDLIPRFLRRFSNGEPEDNVKLIVFHAWGGKLLKQYGIPPLTFSQPNEAFDEACKALLEAI
QGEIIPPIYDAILIDEAQDFEPEFLRLLYQLLKPPKKRLIWAYDEAQNIYGRKIPSAGGIPAGIGRDTIL
KKNYRNTRPILTFAHAFGMGLLRPPGLLQGDAEDYEVERPGDKVTLIRPPEPAGRKGPLPEFKKYDDRAE
ELEAIAEEIKKNLRDEGLRPSDIAVIYLGNNEAKELGDRLAAALERQGIDSYIAGARSDPNFFWKDGGVT
ISTIHRAKGLEAPVVIIVGLDQLAKGESLERLRNLLYVAMTRARGWLVVSGSGESMAELYDELREVLNST
YPSPE
>gnl|CDD|443173 COG3973, HelD, DNA helicase IV [Replication, recombination and repair]
MSELDPELAEEQAHLDEVYARLDELRAEAEERLAEARKEGWGGTPQALSERDAFAAHAERRLARLDRLED
SPYFGRIDFQEEGEDDGETIYIGRIGLTDEDDGEPLVVDWRAPIASPFYDATPGPASYEAPGGTIPGGVV
RRRQYRIRGGKLTGVFDEVLDPDAAALIGDEALQAALSRNRDGRMKDIVATIQAEQDRIIRADLRGVLVV
QGGAGSGKTAVALHRAAYLLYTHRERLERGGVLIVGPNRLFLDYISQVLPSLGEEGVVQTTFGDLVPELL
GVEATAEEDPEVARLKGSLRMAEVLDRAVRDLEREVPFEDIRVEGGEVILSAEEIAEAFYRARRSLPHNK
RRERLRERLLDALKDQLAAELGKLWDEERDELRRELRRSKPVRAALNRLWPFLDPAELYRDLFSDPELLA
RAAGWLSPEERALLLRPTRELKKGRWTVADVALLDELAELLGGPDRTWTYGHVVVDEAQDLSPMQWRVLK
RRFPSASFTIVGDLAQAIHPYRGAESWEEVLEPLGGDRARLVELTKSYRSTAEIMEFANRVLRAAGPDLP
PPESVRRHGEPPRVVRVPSEAELAAAVVEAVRELLAEGEGTIAVICKTAREAEALYAALKAGLPVTLIDD
ESEELEAGVVVLPAYLAKGLEFDAVVVVDPDEIVYESPRGRRLLYVALTRATHRLTVLHTGELPPLLAG
>gnl|CDD|443174 COG3975, COG3975, Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only]
MTKSLLALLLAAAPAAATIHYRVDAPDPAAHLFEVTLTIPVPDAGGLTLSLPVWIPGSYLIREFAKNLVG
LKATDANGKPLAWEKLDKNTWQVHTPGGGALTVRYQVYAFDLSVRTAHLDATHGFFNGTSVFLYVAGYED
QPVQVTLTLPEAGWQVATALPPASGDGFGTFRAANYDELVDSPVEAGRFKRLEFEAGGVPHRLAVWGDPN
LDLERLIADLKKIVEEQIALFGEAPYDRYLFLLHLTDDGYGGLEHRNSTALICPRDDLTDWDGYRRFLGL
LSHEYFHSWNVKRIRPAALEPFDYDQENYTRLLWVFEGFTSYYDDLLLVRSGLISPEQYLDLLAKTITRV
LRTPGRLVQSLAESSFDAWIKYYRPDENSPNRSVSYYTKGALVALALDLTIREETGGKKSLDDVMRALWQ
RYGKTGIGYTEDDVQAALEEVAGYDLADFFDRYVYGTEDLPLAELLAPFGLKLVYEDAPSLKPSLGLRVS
ADGGGLVVTSVLWGSPAYKAGLSAGDELLAIDGLRVTADNLDDALAAYKPGDPIELLVFRRDELRTVTVT
LAAAPADTYKLERVEGATPAQKARLAAWLGP
>gnl|CDD|443175 COG3976, COG3976, Uncharacterized conserved protein, contains FMN-binding domain [General function prediction only]
MKKLLAILLALGLALALAASAASSAAAKYKDGTYTGTAQGFNGDVTVEVTVSDGKITDIEVLEHGETPGI
GDKAIEELPDEIVEAQSLDVDAVSGATLTSKAIKEAVEDALEQAGG
>gnl|CDD|443176 COG3977, AvtA, Alanine-alpha-ketoisovalerate (or valine-pyruvate) aminotransferase [Amino acid transport and metabolism]
LSQFGEKFTRLTGIRQLMDDLGEALRSGPDMIMLGGGNPAIIPEVEQLFRDCLAELLASGELGELVGNYD
SPQGKDPFIEALAKLLNQRYGWNLTPENIALTNGSQSAFFYLFNLFAGRTADGSLKKILLPLAPEYIGYA
DAGLEPDLFVAYKPTIELLDDHLFKYHVDFEQLEIDEDTGAICVSRPTNPTGNVLTDEELARLDELARQH
NIPLIIDNAYGPPFPNIIFTEATPIWNENIILCMSLSKLGLPGERTGIVIADEEIIQALSNFNTIISLAP
GRLGPALAAELIESGDLLRLSENVIRPFYQQKAEVAVATLRRALPDLPWRIHKPEGAIFLWLWFKDLPIS
SQELYQRLKARGVLVVPGHYFFPGLDEDWPHTHECIRISYTQDDEEIERGIQILAEEVRRAYAE
>gnl|CDD|443177 COG3978, IlvM, Acetolactate synthase small subunit, contains ACT domain [Amino acid transport and metabolism]
MMQYQLTIEARRRPGALERVLRVVRHRGFEVRSMNMEANDGDGLNIELTVSSDRPIELLTRQLEKLYDVE
SVEVL
>gnl|CDD|443178 COG3979, COG3979, Chitodextrinase [Carbohydrate transport and metabolism]
QAPTAPTGLTASNVTSSSVSLSWDASTDNVGVTGYDVYRGGDQVATVTGLTAWTVTGLTPGTEYTFTVGA
CDAAGNVSAASGTSTAMFGGSSTTLGSAEGVADTSGNLAASGAFFGVTTPPTPSSTLVVDGTTTVNAAAT
ANGGTGGSGGTTTIITTGVEGGGGSKTAQSLNAITAAGTAALNGGVVGGADEVLTCSAVKDDGSGGAGAG
NTYWALNTLGVSDTPSGTTATGGTVGITSAYGAGVSGNAAVNVNAGFVVGNVGGAAGNTGTTSGTATSDA
ATNDVGDAAVTGLNDGAANGPTGGYGATGTTVAGAAGVGGTKSGTGALGLSGAGGAGAAVSGTATGDDDA
GADDSTAGVSGAGSTTAPD
>gnl|CDD|443179 COG3980, SpsG, Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis]
MKILFRADASSEIGTGHVMRCLALAEALRERGAEVTFLCRDDSGSLIELLKERGFPVILLPAPSWEDDAE
ELLELLKDLQPDWLVVDHYALDAEYEKALKALGKKLVVIDDLGDRAHPADLVINQNLGASAEDYRGVPPG
TKLLLGPEYALLRPEFLALRPASRRISEEVRRILVTFGGSDPDNLTLKVLRALLQLDPDLKITVVVGPGY
PHLDELRALAAERPLNIELHRNVKDMAELMAQADLAISAAGTTTYELAALGLPTIVVAVADNQRAIAEAL
EENGAAINLGLGEELTDEELANALDELLLDPERRARMSRKARSLVDGRGAERIVEAILELLN
>gnl|CDD|443180 COG3981, COG3981, Predicted acetyltransferase [General function prediction only]
MMELVRPTLEDEESYLEYLAEFLKEHIDGSGYLVSFEDFEAWLERLLDEEKGEELPEGWVPATTYWLVDE
DGRIVGAINLRHELNEFLLRVGGHIGYGVRPSERGKGYATEMLRLALEEARELGLDRVLITCDKDNIASR
KVIEANGGVLEDEVVDEEDGRPVRRYWIDL
>gnl|CDD|443181 COG4001, COG4001, Uncharacterized conserved protein [Function unknown]
MENRGGIGALIATFRRILNNPLTRFLLRRLSKDCEKCGRPRLEVALSHYAGERVSCCIKCRFASKIVKKI
IKKGIKAFGVDEDEVKEALSDPYWRRGLATVLKGIILYGVVKPQKVPAPFFVVWWNTTMCNLRCCHCYQE
AGKPLPDELTTEEKLKVIDDLDRAGVVAIALSGGEPTIHPDFFRILYAAASRGIYVAAATNGTLIAAEKA
LEKKKAGGGYVVISSDGDAAPHEHDDFRRGGGGWRRAAVAANNAAVLGMNVAATTTTTTNNEDEVIDLLL
LAEEIGGKRVVFFFFVPGGGGKENIDDDLPPVEEEEFMRKIAYEMKRRPMIQVTTTAPQYVVVAESESGG
KSVAPHHHGGSEEIIREAIAEFGGGGGGGRIYAIIPEGGVVPPCFFPPPVVGLRRIEFDDIWETWEKEFL
LLRRRNLLLGNCCCCCYRCRCGGGRRRAAYYYYDDLTDPPGCIYNDIWKNKEIVAVKRKSLKEKEEIRPK
E
>gnl|CDD|443182 COG4002, COG4002, Predicted methyltransferase MtxX, methanogen marker protein 4 [General function prediction only]
MRALLNRARVAIGIGENSEKVLESAEKASGDAEVVLVGDTGLTDLEIVRTDEPEKELVDLLASGKVDAAV
RGTLSASKTLRLLKKALGVEKLERAALLETADGRRFLLAPVGIDEGWTVADKVELAELAAELIRRLGLEP
KVAVLSGGRLGDLGRSPRVDRSLAEAELVARLLKEKGIGAKHYEILIEDAVKDANVIIAPDGISGNLIFR
TLVLLGGGKGYGAPVLNIDKVFVDTSRASEGYTRAIMLASALAKIKKK
>gnl|CDD|443183 COG4003, COG4003, Uncharacterized conserved protein, DUF2095 family [Function unknown]
MEYDKEEFRKKFPNLAREIEEEKGLRIEVKVGEEDPWSGYLPTVIDYLRRCKTVEEALEVINYLEKRGEI
SEEEAEELKSILEEKGLRSFGGRKEDGYYYREGLR
>gnl|CDD|443184 COG4004, COG4004, Uncharacterized protein, contains DUF5611 domain [Function unknown]
MQEYPVKRGFKPDLERIKELLKECFGEVKEEGGHYVISYGALKRIEVWIEGKKLVVDTESDKSADDEVIL
DTNKRFNDFLEKATGYTAKERKKRAKKEVKE
>gnl|CDD|443185 COG4006, Csm6, CRISPR-Cas system-associated protein Csm6, contains CARF domain [Defense mechanisms]. CRISPR-Cas system-associated protein Csm6, contains CARF domain is part of the Pathway/BioSystem: CRISPR-Cas system
MRRVIISTVGTSLLTNALREEAKKLAELSPDQEIIERLKGDEAWEELLDFLREDPRRASAELNSLYKLLE
KLLRLGEDDELVLLASDTEAGRLCAEILKEYLEEKGINVEVYVVEGLGTKDAEDFQEGLRNLVRWIAEEI
KNYRDRGYRVYFNATGGFKAEIAFATLVGMLYGAPVYYIHESFSELIELPPLPITLDPELLEKLLGEILE
ALEESGLGYELSPWGRLFL
>gnl|CDD|443186 COG4007, COG4007, Predicted dehydrogenase related to H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase [General function prediction only]
MKVAVYGAGNQNLYVNKLNLPEKFGGEPPYGGSRMAIEFAKAGHDVVLAEPNRDVLTDEHWKKVEDAGVK
VTSDDIEAAKEAEIAILFTPFGKRTFEIAKTILPHLPENAVIANTCTVSPVVLYYVLERELRLERKDVGI
SSMHPAAVPGTPQHGHYVISGKATDGKEIATEEQIEKCVELAKSCGKEAYVVPADVSSAVADMGSLVTAV
ALAGVLDYYTVGTKIIKAPKKMVEKQILMTLQTIASLVETSGVEGLLKALNPELLVKSAKSMHLLDNQED
LDAALKILSKLDETLPEEIEEAEIKPTYLVAAQALVKELKTLIGGAAAEGAIRRSMKKLFE
>gnl|CDD|443187 COG4008, COG4008, Predicted metal-binding transcription factor, methanogenesis marker domain 9 [Transcription]
IALAPVAFALLIAIAVVAAITAGAVVAGAGDLDAYSILAASKGVARAIAEAISDEPMELIERVLRELGRE
ELFLINVVAATLEPGILAAAALLIALALLEKSAHCIQAAAAQAGLGEAIEGDAPRLGQVMLVDAIRGLKL
SVVTKKLVIVLIALARAGVVAVVKIIAGAADLDVAGADLDAIKGADIAAIDLLRLINSLTDIGNDSNMIF
ILADDISVARARMDDPSLGVGLVASLLRYLDELMGWYNAPKHICRGGDLRGLAFCCPPVKPCPLHPALKK
LGLSPEEFVKIKMEFAKGTPLEYGDSTCFGSLVWCCKISKPCPLRDGVLEQIGLSPDEYMRLKKELAEEI
LKKSFKDEEET
>gnl|CDD|443188 COG4009, COG4009, Uncharacterized conserved protein, DUF749 domain [Function unknown]
MFVATLLGIFTVKELPEEYEDFVRVKAALEKRELKDDDEIAILNIEGTTSYHVLFLDSYNSIEEIKEELK
EMGAKLNHDSEEILEGHLNR
>gnl|CDD|443189 COG4010, COG4010, Uncharacterized conserved protein, DUF2096 domain [Function unknown]
MKALPLDQQWVVLNELLSDLRKRGIEVPEEVFEDLRLANAIINFYKLDPHDPDRAKELKRAEKELNRVQE
ILLDLAENIGEDYRKKWLEKLKKASRGEKVYRFPLIKSKFEVGAPPGFEFIRVKLKEPIQEERLQEIAEY
HGVIIEFSEDDKIVIYGDKDRIKRALKEFSPFFKE
>gnl|CDD|443190 COG4012, AF0413, Uncharacterized protein, DUF1786 family, actin-like ATPase superfamily [General function prediction only]
MKILAIDVGSGTQDILLYDEGKEVENCPKLVLPSPTQIVAERIRKATAAGRDIFLTGYLMGGGPVSRAVR
AHLAAGLRVYATPSAALTINDDLERVKEMGIEIVEEPPEGAEEVELGDIDMEALKAALASFGVELPDKVA
VAVQDHGYSPGQSNRIFRFEYWEEFLEEGGRLEKLVYDEDPPEYFTRMKAVRESLKEPGVVVMDTGPAAV
LGALYDPRVAAENGAIVVNIGNGHTLAALVKDGRIVGLFEHHTRMLTPEKLKELLEKLADGTLTNEEVFN
DGGHGAYVKPPIGFDGFEPIVVTGPRRELLKDLGLKVYFAAPLGDMMLTGCFGLLAALKRLKGIA
>gnl|CDD|443191 COG4013, COG4013, Uncharacterized conserved protein, DUF2097 domain [Function unknown]
MKEIELIMTPDELIEYIRNNVKEGDYVELYYGRVHIPGTVVSINDCRLRLDLDGELISGLIEVDLEEIKD
DLIELVHEPEDSEKKIVIEAI
>gnl|CDD|443192 COG4014, COG4014, Uncharacterized protein MTH814, DUF2098 family [Function unknown]
MEVDINGKEITVGSYVRYINTGTVGKVVDIKEEDGGTWVLLDSTGLYYRVDTLEPADEKEYRKEEKEAGK
EDVIERLKKEREKFEEVDLTDQSCEGGG
>gnl|CDD|443193 COG4015, COG4015, Predicted dinucleotide-utilizing enzyme of the ThiF/HesA family [General function prediction only]
NIEELERKLVPKGEVSLIGLGRLGFRVALNLIEVHRGGPEKITVFDGQKISENDIIHRMLGAKIGEYKVD
FLKRLFGPDNSRKVVAIPENITEDNLDLITGDVVCIEIAGGDTLPTTAAIIKYAHERGIKTISTNGVFGI
GEEEIKVVDIEEADPNPPVEFLREEGIEGHILVGTGKLIRDWEPITPYVLDRIAKVMTIEILKLLKEKLK
N
>gnl|CDD|443194 COG4016, HcgF, Iron-guanylylpyridinol (FeGP) cofactor biosynthesis protein HcgF, CinA family [Coenzyme transport and metabolism]
MIRVATAECFTHGKIGREIHAFARGYPDNYGWSLDRELGNVSVVASLFIPTLSGVKSLLNIEPPEPDEVI
DGIKVYNEEGDLEVALLMAKAVKEITNADIGIGTTAGIGRGAIAIVTDNNKYLFTSDVYADLRKSDAKNI
LERQKSGIKKTLRLFESILKEEYLPEFVEKII
>gnl|CDD|443195 COG4017, HcgC, Iron-guanylylpyridinol (FeGP) cofactor biosynthesis protein, methyltransferase HcgC [Coenzyme transport and metabolism]
MEYGITETVKTIRSKITIKDIVKEIVEKKANAIKYWLEGEEFEPKNALIFGAYLTGAYIANALSKKCEVT
VVDIHPHLKDLLNPGVKFKLSLREGPSRNWDLIIDTTGIGGISPEFLSKFNPKVLIVEDPKSDGSDKTIR
KIDNTMERLESIEAAKKGILKTSGLNSKTSGTMTLTVDTLRDSMAEAEELDGVLYATPNLEFYERILFHE
RDPKKFLEELEKPALTVSSLTDVDCDEILSKNLSRIKSFVIEF
>gnl|CDD|443196 COG4018, HcgG, Iron-guanylylpyridinol (FeGP) cofactor biosynthesis protein, fibrillarin family [Coenzyme transport and metabolism]
MKDLIKEAVNDLDAAWELRKMKKDIIEIVDAVSDLSREETIKLGSNFKRFPLGCDLTEILVGTCASDLEK
IDLLGNCILSDRIGAPIHVCAYAFADIAEKEGMRPIELMKEVRENTEVPLDLDHFGKYGPMRFPKEITGC
MGQCYNEGPPFKGCPRGRIHKRLIDKEKEALKEKEEWVKLSSSVAVNLTSEQGAEGHAAPLDEAEEVAEL
AKKYGKGVEAIMFVGDGYDDLITGFKAAIEMGVDVFVIEGGPFNRAKDRLDAFARAVAAARILAPGKVVA
TNGAYEDECRIGLRSGLNAIISGFPKNHHGYMCGYSPGTARRGNFGLPRVLKIIKEEVKDGPTRVPIQRE
ELEALARAVKFLGPENIYPNKIGDTYIGDAHWVCLLNSPLYERVNVKKTVEDIVSMAEDGLNGDKVALLG
GRFISWGIAKALDGYVDEILISDVDPWVEKATVKNLREELKANIYRGNGDDKKAYKNADASIICSTIPEI
VRKIKNKIPDAITLI
>gnl|CDD|443197 COG4019, HcgB, Iron-guanylylpyridinol (FeGP) cofactor biosynthesis protein HcgB, guanylyltransferase [Coenzyme transport and metabolism]
LEELIKKAYIESLEGTRRGDKEEEVEAIREYILNAKNIVVPTNNEKKFKVINDVLSRFGLPEAEHLEIPT
NSADLTRMPALTKALMALDISDADLVIARGRLGVPGSGSMLVIMDSKGRILTASLSPSHVIHKKSIEEAV
KKEMIEALKRIGFT
>gnl|CDD|443198 COG4020, MK0078, Predicted ATPase/kinase of ASKHA (acetate and sugar kinases, HSC70, actin) superfamily [General function prediction only]
MFIGIDHGTTAIRFAILDDGEGSHFKISREEAKSFSESSILEEIEKRVPLEEIELIAVTYSMGDGISKIT
PIEKVKNRGVISIEGAGKHTGGGTRVFDEIKNSGIPAVVIPGIHRGSPTDPRFKVYSHQASPEKIGIAYN
ALCTGFENFIVSDISSNTVTLLVADGKIVGAIDACIFAPGTLHGPLDLEAIRDIDAGKITANEAFSHAGV
LKIAPYKDRDELLEAYSKGEKKALLALDTLALFAAMEIASLLLLLKDYIAGVVLAGSVAEMPEVAEKIKE
LLDRKVLVLDEWSAAIGCALIARDVFKGKREILGIEVDL
>gnl|CDD|443199 COG4021, Thg1, tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]. tRNA(His) 5'-end guanylyltransferase is part of the Pathway/BioSystem: tRNA modification
MRVREIFHDLRVLPGLPVVVRLDGRGFTRLTKELGFEKPFDERFRDAMVETAEHLMKESGFSPVYAYTFS
DEISLLFDELPFDRRVEKLDSVLAGEASAAFTLALGEPVAFDCRIIPLPNELVVDYFRWRQEEAWRNALN
AYCYWTLRKEGMSPREAAARLKGMKVAEKHELLFQRGINFNDLPAWQRRGIGVYWEEYEKEGYNPVTGEK
VLTTRRRLVVDWELPLFSKEEYRAF
>gnl|CDD|443200 COG4022, COG4022, Uncharacterized conserved protein, DUF2099 domain [Function unknown]
MDEHIIEALGKARVVVRDGKVVEVGEPKIRWCPLFKKFRGIKEITKEAVKKNIEFRIKDFGMFTPDRVLE
MDRDFVGFGASEILSTALRRGLIDAAVIVCDGAGTVITTNPELVQGIGGRMSGLVETEPIPEVIERIEER
GGIVLDPETASIDQVAGVRKAIELGYKKIAVTVADAEDAKKIRELESEGVDLIIIGVHTTGISREEAEEL
LKYADIVTACASKTIREIAGKKALLQAGTAVPIFALTQKGKELILERAKEIDSPILINTTKLPVLPEEKQ
PRPLV
>gnl|CDD|443201 COG4023, SBH1, Preprotein translocase subunit SecG (Sec61beta) [Intracellular trafficking, secretion, and vesicular transport]
MKKKKKGGGLMSSAGLVRYFEEDTKGIKIDPKTVVAIGIALGVIVIILNILLPLW
>gnl|CDD|443202 COG4024, COG4024, Uncharacterized conserved protein, DUF2100 domain [Function unknown]
IRVEQSEELIKKAVSTISKLKDKKKISYKDAKEGKIDVEEFKKAIYRLIEADEFLYKSAPEHELNGEDAK
EFCRLLIAAQKHINNILADFGVEEETEKELDKDALYIVSNKKLKKKLKDKGVDLNIVVTGGPLVPEDMRE
INPNIPEKALEGIEKKIEIAKNEIERKIEKFKPEKIVVVVEDDKSGELLYKRAKELYNAEKIVVEDIKD
>gnl|CDD|443203 COG4025, MTH423, Uncharacterized conserved protein MTH423, predicted component of type IV pili-like system, DUF2101 family [General function prediction only]
MEKLYTIGERVEKIRGSEKKVLLPSPSDDPPKSIIKRIAKRDRTPHEVTVLKLQLSFLLFLVLSILYVFN
FISLILILPLAVIYFLYLRYILIRNRRVMYPEDFEAYRDFFLMYIGLGSIAFLSNVGYLLVRVFPFEVYP
YLTYLGFILLAVLAFRHWFRVKYGRDYTYGVVEEVGGNLVKVKVHDDIRANVKPGYYIVEASGFVEEGEI
VKLLVEERGMSLRGARPVRIIEVYWW
>gnl|CDD|443204 COG4026, COG4026, Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only]
MTEKKPVDVRIIVEGASDVEVVSKALQNLALGSEYNITISSIIPTTNVEIAKSAVAGADLVLIATDADRV
GRELAEKFFEELKGMVGHVERMKLPLGHDVEYVDVELVRKEIKNAIIRAGLKSLQNIPEYNELREELLEL
KEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLLE
VFSLEELWKELFPEELPEEDFIYFATENLKPGKIIVGQGYIAAESKEDAEEWLKIIKLALILVESEKEEL
EFNKDEN
>gnl|CDD|443205 COG4027, COG4027, 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase [Nucleotide transport and metabolism]
MFTIVVRARKDADAVKAAVERFYPGWGIEVESLGGARSPEEIEDGLREIIEDDYFYILLLGREDKELAGE
LVEEIPPNVVVRVVPRKRVRNARLEELYWEIERARARFRLRVGWDNDAYLFEPVPPGRRPEGLEVEPDYD
IFLGVGRFRKNLSKLLGEDPGENPLVLRKTGGRHVVYSGPRPVAELHISDEGVPTVVKWIDVKTEDSESE
SLVLEANLEEAFEYEVSALGLLRVGGDVDTVPVPGKGGKDSALALLLVTTDYGRDNVKAVYVDTGTDFVD
SVVYVEGVALKLGVEEVIPYEGVDRGLLHRKGWCEMRKEEKVTLAVGEKLEVLVVGDVADGELRRRRESR
RVEERRPVKRPLRYDPPLFKWVVMPLKLWVAGHVQLLILLYGFFLNPLYYYGFYRIGCYLCLLLRLLELL
VLMLGPESRRELRKK
>gnl|CDD|443206 COG4028, COG4028, Predicted P-loop ATPase/GTPase [General function prediction only]
MRLLVAGLLRVDSGKTTFSLGLLERLGEVGLDAVGFKPRAGHNYWYDHDTLRRSLELGRLVGKDAYRLAD
ASGEDRPPEIINPVHRLWRPPDPEKYRNIRLYLGLLGRPDRTFVLDRVTRCLNGEEDPHYVVNATAERLP
KSLPEVLEELLPLLDAIPVESVEELRNLLMSSRYLPAFDSCAALLLERYDVVVIESYNDAAAPTPGSLAV
DAVAVVAPGRARIYDGDRYKKACEVASGSPRPWVLRVSEVFELLKPLKTVDLPPLESDERGRVADAYDPA
YDALLAAA
>gnl|CDD|443207 COG4029, COG4029, Uncharacterized conserved protein MJ0498 [Function unknown]
GTVTKYVVISSDSNVTPSDLARKIYELSLGVTIKETCFGAMITGPEEEVDKVVEELRNLDPNHIFVKDRG
FPPGDPRRCRAHRGGGRPGFHQLEAEVELLPLISKALDALEKGEPAVEPEKKKKLPVDKLKEIIEEEL
>gnl|CDD|443208 COG4030, COG4030, Predicted phosphohydrolase, HAD superfamily [General function prediction only]
MKFFITDCEGPLTLNDNAYELSAAFIPNGDKFFEIISRYDDVLAYVLKRPGYKAGDTLKLILPFLKAFGA
TNDSLIKFSKDNLRFVPGAEEALRYLKETMPTFIISTSYEHYLKALCEVLGFPFENTYSTELDLDKYELS
EEEKKILLELADEILKLPDIELDEEEVKTVEYLDDIFWRKIPKTEAGKLLEEVSPVGGNEKAYAVLDIIE
KTNIDLDETFYVGDSITDVQVLRLVRDNGGLAVSFNGNEYAVREANIAVLSETATVVAVLASIFYETGKE
GVFDLAESYNREYLETIDFNLKNDLKKKPEVYRVTRDNVEQLIEKSEAMRKKVRGESIGALG
>gnl|CDD|443209 COG4031, COG4031, Uncharacterized metal-binding protein, DUF2103 family [Function unknown]
MRVLDRRGERALEVVEAPPAEKIGGSHSTLIGGRQGRKAIRTVAGHPHVKKIIPGPIDAGGKGSRGGLRA
KVTRADDNGNVRLLLRDGSSVQENRVVTTAGDRETGERVRADLNEALREAELQ
>gnl|CDD|443210 COG4032, COG4032, Sulfopyruvate decarboxylase, TPP-binding subunit (coenzyme M biosynthesis) [Coenzyme transport and metabolism]
MSWAEAVVDALKEAGIDFVAYVPCSVLKPLINLLEADPDIRHVPVTREEEAVGIAAGAYLGGKRPVVLMQ
NSGLGNSINALASLNLTYRIPLLMLVSWRGEPGEDNPAQVPMGRITPPLLDAMGIPYFVLDTPEDVEPVI
ARAIEHAFETGRPVAVLLSPGLWGGKAL
>gnl|CDD|443211 COG4033, COG4033, Uncharacterized conserved protein MJ0453 [Function unknown]
MGCIENLNYEILLKNATFKECEEYIRKNCKEVYEVPPGYKILGVRLIGIPPIPVGIDGDDIIFPYTKPCY
GTFVLRVEDAPEEIERLRENLK
>gnl|CDD|443212 COG4034, COG4034, Uncharacterized conserved protein, DUF1152 domain [Function unknown]
MTLPPLFLRLFGARRVLVAGAGGGGDVVSALPLALALRRLGKRVHLGNVVWERYVVDPVPGPIPLEELVN
AEWLGDDVAIVNPDSYAIRGGRKYFPQLARWLRALGPPVVAADIKGGVKGLARALRELAELLGIDAIIGV
DVGGDILARGDEEGLGSPLADSISLAALAELEEPSLLAVIGFGSDGELSHEYVLERIADIAREGGYLGAF
GLDRDDAELLEDAVKHVNTEASRIPLAAFRGEYGEVKIRTGTREVFVNPLMALYFFLDLEAVARRSPLAK
LVAGTESLEEANERLNELRAEVRRRGRRR
>gnl|CDD|443213 COG4035, EhaL, Energy-converting hydrogenase Eha subunit L [Energy production and conversion]
MNEVYFIYLIYIISFIIGSFLGLEYSYKKYPEPFVEKRIDKLALILAIIGWTLLLNSGLISWVSINITIG
CFLIGFPLGMRPGYGRYETVIGIAIALLIWLLTLGL
>gnl|CDD|443214 COG4036, EhaG, Energy-converting hydrogenase Eha subunit G [Energy production and conversion]
PEIMSSLYHPALLVGFIVGIIALFAISREKDDLHRLLLTDLVEIAMLVVIAAVGTDLAEALILPGLVVGL
AELLAVSEILISREGLRKGKPPPRPLDMEVLRTAPPFLAIILVVYGIILSGFTGGAVAGLGLLFYFLSRR
VRGLEWEGIEGISGIAWALWIVGFIGFFLFPQYWLLALMLAGLGILIKVGSKLGLIGTMMG
>gnl|CDD|443215 COG4037, EhaF, Energy-converting hydrogenase Eha subunit F [Energy production and conversion]
MKKISKIWNYLSNPENLPRLFAGFLALVLIIGLLLPLTYNEDQLYPKPAPQSQIDAKSPLAPYDRGGIPL
EEPADIKSQYPQNEPNLGKITAYLTPISIWLSDTTMYFGTTIVSHPGGILDEILYYTRGLDTVLESSILF
VAFAIASWLFRNREED
>gnl|CDD|443216 COG4038, EhaE, Energy-converting hydrogenase Eha subunit E [Energy production and conversion]
MLLMTAEFYLGLFLLIIGTIGTAFGPRVKDPVVRLINLEVPAVGVLLIFLAYNETLALLTFIAVTAITTL
VLVRAIERREEMEE
>gnl|CDD|443217 COG4039, EhaD, Energy-converting hydrogenase Eha subunit D [Energy production and conversion]
MNDLLLLVSAALALLGAIGAILLRDPIDKIIMLALLEAGLIGLIVAFGYLDVAIASSLLEPISTIILLLA
LIKIEEVRKSKKKYGA
>gnl|CDD|443218 COG4040, EhaC, Energy-converting hydrogenase Eha subunit C [Energy production and conversion]
MDIAIAIIGVIAVLMVLRVLLEKDRARKLLYLNVMNFAIAALIALYIKTPMGAIAAIAYFIGSTLESNAI
AYTIARGEEEE
>gnl|CDD|443219 COG4041, EhaB, Energy-converting hydrogenase Eha subunit B [Energy production and conversion]
MMLEILHIAIAAVICWLNFVTIDTFFGLPEKPGVKGADAIGRSIEKRGGDLNGGFFMGNIVCSPDASAGT
LLAACGVYLMGIEGGLIAALLVYIGNRLCADPGYAGTTGALTATFIIYLFSFAGISPEYFIAGMVIAIFT
IQGISHPYASRLLGKIARKMGRY
>gnl|CDD|443220 COG4042, EhaA, Energy-converting hydrogenase Eha subunit A [Energy production and conversion]
MIYGNVILIILYAVAVISSIIVGAALRLPLLPERPIRDSWETSALFPTPVIALGLTAIVIKLFVYGIIGL
ILGAVIGIISALFSKYAEKIFPRPEDG
>gnl|CDD|443221 COG4043, ASCH, ASC-1 homology (ASCH) domain, predicted RNA-binding domain [General function prediction only]
MTHKMGLEEEYFELIKSGKKTIEGRLNDPKRKKIKVGDKIVFINLETGESLTVRVTDVRRYPTFKEMLEE
EGLEKVLPDGTSLEEMVKIYYKIYSKEKEKKYGVLAIEIELIG
>gnl|CDD|443222 COG4044, COG4044, Uncharacterized conserved protein, DUF2110 domain [Function unknown]
MVVLATKCYVEGDARERALDSLRSLVGNELGDLDVEWEVGVRDDDFPSVTVEGEDATVARNLLREEWGEI
TPHLEPGETYVGTLESWDEDGFVLDAGEPVRIPADELGLGPGSPEQIRERFGLVQHLPLRFVYGEDIPAR
LADAERDRLYEWTRGTGRVNVNSATRGEVRATVNRAGHAQDIVTVERLGLLEQSVVCTEGTDPPGLLASI
GPYLPAELLCVV
>gnl|CDD|443223 COG4046, COG4046, Uncharacterized protein, contains DUF1512 domain [Function unknown]
MDAQTSLSGLSDWISLISQLIWFIIFILLFPGYGQRIQIYIWSRDIEKKLNKLKSYADEARNKTIEYLKK
LGAKDPESLIDRLIEFFVIEPVSIEPTGIIRRLKHLLRTREDRIRSEVESLLPNIDEVERSNIETALEIA
NALNMIYKVVRHYLLLGKKTNNWYLIMQLQMLMPMIMEIAEAYRKALDAFLKGQPIGDGAGPLVAGRLML
NSKAEKWEIAKDTVASETEFEGRRLYVVKAEGPGSTVGRPGEAVEKLVEELGGKVSLIITVDAALKLEGE
ETGSIAEGVGAAIGDPGPEKIAIERVATKYGIPLYAVIIKMSMEEAITAMRKEIADAVDKVVERVKEIIK
ERTKPGDTVIVVGVGNTVGVAQ
>gnl|CDD|443224 COG4047, COG4047, N-glycosylase/DNA lyase (8-oxoguanine DNA glycosylase) [Replication, recombination and repair]
MRVDSERIEELAEILSELGIEFADVIEENVDPQYKALEKLAKNLGNDEFLKLVVANALVSYQLSMRGEEW
WKEFSEYFSGRPTNDDIVEAYIEFLSNSRGNRRLREAKIKRIEKVEPFLEELIEDPLVYYEDLSKLREEL
AKALGSKRESKTIVFAVKMFYYACRAAGGEVPYPMEIPIPVDSRIAKLTITSGIVEGLAGELMRRREEAI
EAWRKVSRESGIPPLHLDSILWLPGGGIRDELKRLLEELRDKLARLLPESALELLKELLYLICPS
>gnl|CDD|443225 COG4048, COG4048, Uncharacterized conserved protein, DUF2111 domain [Function unknown]
LKISEDSTAEDLEPLAMAIHELVGRLPVTMRSKNKPGVRIEDGKVVDDNYTGPVLEEVLKTGKIIRVTPK
SGPYKGVPVVVAPIKDEDGEVIAAIGVVDITGIFDLLSLFRRYPEI
>gnl|CDD|443226 COG4049, COG4049, Uncharacterized conserved protein, contains archaeal-type C2H2 Zn-finger [General function prediction only]
MVRLKAIKVEDRDGEEFFRCPRCGMVFRKSKDYSRHVNKSHGHLFKKEKRKWKKFKKQLLLID
>gnl|CDD|443227 COG4050, COG4050, Uncharacterized conserved protein, DUF2112 domain [Function unknown]
AKVFIYPPNSLILSDLVERFGHEPLSLMKEIREKVTTPGIDSPPLNITPEDPKKGLKYAAVEVPSGVRGR
MALIGPLIEEAEAAIIVEDAPFAFGCVGCARTNELTKFLIRQKDIPILELKYPTNEEEAKDFVAKIKEFL
ESLPGGKDK
>gnl|CDD|443228 COG4051, COG4051, Uncharacterized conserved protein MJ0802, methanogenesis marker protein 17, contains DUF2113 domain [Function unknown]
MEPLEYFEVECTEEEGAEAYREIARDVLSDLGLLRAIGRLRIYIDPEVPLFIAAGRLRKGPPPVTLGDVA
DVEAEEGEVTISISDETYLPDLLRKLWEKYGRDNVDQPDRFTIIVEVPEEEIEEIEELVVADPSETLKKD
LIDALIRIAPEGFRVRRHYLDGNRFTFVASEETLKPEWIDEAHEMIEEMMGGG
>gnl|CDD|443229 COG4052, COG4052, Uncharacterized conserved protein related to methyl-CoM reductase subunit C, methanogenesis marker protein 7 [General function prediction only]
MLEPLTYEGGVYKHDEILELIEDLGGYVIQKHVIQQEVVLTMLVPKEDIELIEELAKELLGKLTEAPLAG
TEIAVVSPTLARHHLPHSACDIAEYLRRYGAKTNMIGLARGFGKRIAQINDEERDLINEHDLAVFSLGNF
EDCIKNKKPKLFEGIDIPIVVTGGPELDTEDDPGADAYVGGIGRIAHRLRRGEEIRALDELVEEVEEVLD
KKREEIAKDPLSVSPARVMKEIEEQVPEIEEVLSPAPITLQLDGLRVKLPYDEYHEKIENVEVDEGIRLG
DVADITPSKMKDYILIKIKPESEVGFEI
>gnl|CDD|443230 COG4053, COG4053, Uncharacterized conserved protein [Function unknown]
MKIVSIGADISDNDVSCSKELIENIEKDIKKLIDKGAVKAALTNITGDDIVITAFVEENLLETVNKAIFD
ILRKNAEGFGDLAGISDDPEGAGEGISYAEAKARQSEYGDAIIIAFDTYGGESFVNEVALSVIEAAKGMV
YDVGGSVSNEPKEIPGVGYVGDETDDPVVVATVEDLEQVGVVAGAILGAALGFKNVYLVKRGTPSNVLPG
SVIYSVTAFLNGNVIDLYVPIERKTRILR
>gnl|CDD|443231 COG4054, McorB, Methyl coenzyme M reductase, beta subunit [Coenzyme transport and metabolism]
MAKYEDKIDLYDDRGKLLESNVPLEAISPLVNPAIKKIVDLTKRTVAVNLAGIENALKTGKVGGKANQIP
GRELDLDIVANADAIAEKIKEMVQVEEDDDTNVKLINGGKQLLVQVPSARLDAAAEYDAATLSTAAATTQ
AIIDTFDVDMFDASMVKAAVWGRYPQTVDYMGANVASILSIPQNNEGLGYALRNIMANHVVAMTKKNTMQ
AAALASILEQTAMFEMGDAIGPFERAHLLGLAYQGLNANNLVYDLVKANGKTGTVGTVVQSLVERAIEDG
VIKVGKKLPSGYKVYETKDPALWNAYAAAGLLAATMVNCGAARAAQGVSSTLLYFNDLLEHETGLPGVDF
GRVMGTAVGFSFFSHSIYGGGGPGIFNGNHVVTRHSKGFAIPCVAAAMALDAGTQMFSPESTSGLIGDVY
GEIDEFREPIKYVAEGAAEIKDK
>gnl|CDD|443232 COG4055, McorD, Methyl coenzyme M reductase, subunit D [Coenzyme transport and metabolism]
MSAMTDAEYPQVEIFPERLLKPETTEKLLNEIYSLDGIRRVVIHGPRLPKTVPYGPARGTPVNHPDRKVI
EVGGEEVELTVQVGRIILELEDEDVIEKIEEICEEVLPFSYEIREGRFMKTRPTVSDYAKYGPDADPRLL
GLVDPKSKSEPVVCIIKGTE
>gnl|CDD|443233 COG4056, McorC, Methyl coenzyme M reductase, subunit C [Coenzyme transport and metabolism]
MMIGRETQVVDCRESMGLGKGGGLAQRGTISECGRPDVIAVAMSPGRRHITKPVCEITYGLREEGIQTSV
LVLNAGSGVPDDAPSAGLGATFGLTPKEIEQIERHKVAVIHLGNVRSHIIYKARLILRNVDIPAIVVCQA
PVDFEDFAKIGVKTRLVMPPEDKIRTKGTVMEIVTGVTRGETCPREKLNEIVKKVKKTLKSITR
>gnl|CDD|443234 COG4057, McorG, Methyl coenzyme M reductase, gamma subunit [Coenzyme transport and metabolism]
MAYKPQYYPGTTSVAENRRKHMDPNYELEKLREISDEDIVLIMGHRAPGEDYPSVHPPLEEMGEPECPIR
ELVEPTEGAKAGDRVRYIQFADSMYNAPAQPYDRAYMYMIRFRGVDPGTLSGRQIVEARERDLEKYAKEL
IETEMFDPALTGIRGATVHGHSLRLDENGLMFDALQRYVLDEKDGHVVYVKDQVGIPLDRPVDVGKPMSE
EELKKRTTIYRLDGVPMRDDKEVVEVVQRIHELRTKYGFMPK
>gnl|CDD|443235 COG4058, McorA, Methyl coenzyme M reductase, alpha subunit [Coenzyme transport and metabolism]
MAKATKKLFLKALKKKFKEDPTEKKTKFYKFGGWKQSERKREFVEAAKKIAEKRGIPMYNPDIGVPLGQR
QLMPYQVSGTDTFVEGDDLHFVNNAAMQQMWDDIRRTVIVGLDTAHEVLEKRLGKEVTPETINEYLETLN
HAMPGGAVVQEHMVETHPGLVDDCYVKVFTGDDELADEIDPQFVIDINKLFPEEQAEQLKAAIGKSTWQA
VRVPTIVGRTCDGGTTSRWSAMQIGMSFISAYKMCAGEAAVADFAYAAKHAEVINMGTMLPARRARGPNE
PGGIPFGFLADIVQTSRVYPDDPAKVSLEVVAAGAMLYDQIWLGSYMSGGVGFTQYATAAYTDNILDDFV
YYGVDYVEDKYGGLAKAKPTMDVVKDIATEVTLYGLEQYEKYPALLEDHFGGSQRAAVLAAAAGISTAFA
TGNANAGLNGWYLSMLLHKEGHGRLGFYGYDLQDQCGAANSLSYRSDEGLPLELRGPNYPNYAMNVGHQG
EYAGIAQAAHAARGDAFALNPLIKVAFADKNLPFDFAEPRKEFAKGALREFEPAGERSLIIPAK
>gnl|CDD|443236 COG4059, MtrE, Tetrahydromethanopterin S-methyltransferase, subunit E [Coenzyme transport and metabolism]
MDPLIGMGVLALMGALATIAGAAEDLESDVGSQSNPNSQVQLAPQMGYPHRIFNKAISGEPPSYALWCAI
GGTVAWALMTAFGLNVVLALALGALVAALVHGVYATTAYLGRTASQARFGQPVYLDVVRSHTPVIMGHAF
IATFCIVTISYLMTTVLGHPFPLPLLALIWGITVGAIGSSTGDVHYGAEREYQNYEFGSGLPIANSGNIV
RKAEAGLRNSIDNSWFCAKFGGPATGLCFGLTVFLSGWRTTVFDPFGGITAGWGAVIAGLIIVLILAIIN
RKIEVWARKKYGPYKE
>gnl|CDD|443237 COG4060, MtrD, Tetrahydromethanopterin S-methyltransferase, subunit D [Coenzyme transport and metabolism]
MDIATNILYLILITIGGLLIGFGVHFVPVGGAPAAMAQATGIGTGTVQLAAGAGLTGLIGAAWMAEQTDS
ILLILASGAVGAMLMIAITMLVGNWIYVYGVGVPPASAKVKKDPITGDRQDEYVSQGTEGHGIPTVSFVS
GVIGGLLGGLGGALIYYALLEVYNANPGLISPIAVGLAGIFAVGIFFVNAVLASYNIGGTIEGFHDPKFK
RWPRAVVASLVASAVCAIIAVLIIGGL
>gnl|CDD|443238 COG4061, MtrC, Tetrahydromethanopterin S-methyltransferase, subunit C [Coenzyme transport and metabolism]
MSAGGGGVAAGAIPHNKLMAFGIVGGLVGIYLAYFLPVLGPYFSFIGGLGAICAIVWGADAVRRVASYGL
GTGVPSIGMLALGMGVIAALFGLAVGKAFGPGLAGPIVALIIAAIIGLIIGILANKIIGMKIPIMVQSMT
ELAGAGALAILGFSAAITGTFSFDGILTSVIGTGYIAVIFILGAMAILHPFNACLGPNEKQDRTLMLAAE
CGFLSMIIAGIVSLAFIGASAIVSIVVGLIGWYIAYKKFVKLSKRDAAAVLGTGLLPKEEE
>gnl|CDD|443239 COG4062, MtrB, Tetrahydromethanopterin S-methyltransferase, subunit B [Coenzyme transport and metabolism]
MSIVKIAPELHLVLDPETGLVAEERGDVIVYSMDPINEQIDKLEKYADDLVNSLDPRTPPLNSYPGREGV
YYIAGIYTNMFYGFIIGLVISALLAL
>gnl|CDD|443240 COG4063, MtrA, Tetrahydromethanopterin S-methyltransferase, subunit A [Coenzyme transport and metabolism]
MADKKEPAEGWPPVKGDYVVGDPESPVAVVTLGSHLEEAPIDAGAAIAGPCKTENLGIEKVVANVISNPN
IRFLILCGTEVKGHLTGQSLLALHENGVDEKGRIVGAKGAIPFLENLPDEAVERFQEQVELVDLIGTEDP
GTITAKIKECKAKDPGAFPEEPMVVEVGEAGREEEEEAGGFVPQAAEIALIEARIRLIEEHVTNIGRLNK
FIAGVYAGKIEGIMIGLVSSLVLLGLLLFG
>gnl|CDD|443241 COG4064, MtrG, Tetrahydromethanopterin S-methyltransferase, subunit G [Coenzyme transport and metabolism]
MAEDEKESIPSVVVDPDDYNEVLERLDEIEEKVEFVNSEIYQRIGKKIGRDIGILYGLVIGLIIFLVYIL
LSPIFLILS
>gnl|CDD|443242 COG4065, COG4065, Uncharacterized conserved protein MJ1451 [Function unknown]
MGFFSRFFRSPKPHIAESPPVRLPELKSKPYFIVASVEVGNTTTKCILTATNLETGKTYIINKTVRMTRD
VRPPKPGEEVFGRTLDGVELTRESVAELVRDTLLEAHKKANLDIKDDLHFVVRSTGVVAGFDSPEEVGEF
IKALADGCLMAGVPPRKMTPPMSKENIPEKFRKYSKLDKVVFDGAVAGVVPPTGSTGVEIVANEMEGELA
TAGIKEGAKWTDVDFRNPCISIDFGTTLDGRITSDELPYAKTIGNFCGLAGAIPDAIIRGTGLVDEKTGT
ALDIFGEKSPDSLTLKLKGKKAKEYAERIHEHIDIEEVPKDRKRYGSVPVNPDAAEESGVVLIGCDVGEN
GSDLPKLSEIGAEIYKKHGLPTLFAVIDRVMARVALRLVDVAVEEGLVFENTAIGITGRAGITGNKPKLI
LEGLEELGLYDKPEENVVFVDDGLARGAAVMARCMNSLGTPKNPLGGVRGGKCILGRRIKLQK
>gnl|CDD|443243 COG4066, COG4066, Uncharacterized conserved protein MTH_811, UPF0305 family [Function unknown]
MKIEEICARLASAMTRGELGEILKKEASKYSIFDLMKIRGFLEKEIRYLPPDYRKEYSPYFFEYLFETHH
EIKLDKRSGIFEEIDEPILKEFLEMIPEQCKDEPTPGEPRFRKLYYLVSGYLIFVLKEPGHPVGMPFPGG
FKVEEKGGKYYCPVKDKQKDVPFALCNFCPAKQDEEL
>gnl|CDD|443244 COG4067, COG4067, Uncharacterized conserved protein [Function unknown]
MKAAAPAADKLIIGWREWVALPELGIPAIKAKIDTGARTSSLHAFNIEEFERDGEDWVRFTVHPPQGDTD
TEVECEAPVVRRRKIKSSGGHAERRPVVETPLCLGGQTWEIEFTLTDRSDMNYPMLLGRTALRGRFLVDP
SRSFLQGKPC
>gnl|CDD|443245 COG4068, COG4068, Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only]
MMVKIPPHKHCRVCGKAIPPDERFCSEECEEKYQEEQKKQKKKQIIFFAALIVILIVIVVLGFF
>gnl|CDD|443246 COG4069, COG4069, Uncharacterized conserved protein, DUF2117 domain [Function unknown]
MKIGVVIHGPEIIDSGYAKKILKLLSRLGEVKAKLGGTMGKTAVIDAGLEDVIDISRKLKPSQSIEKLFE
DNDIVCLLNHGKSLETGHTFGNIVVSRLNNDKPLIQIERPGESDGTIIPWNKKALPHAEKLSKDLGLKIS
EPISVVNGIEIEKEGSRVIRKISGVSPGENIMVNGIVVGKATSSEVEIVAENGFITDIIGGEIKEHGVEK
LHKYEKRVDLEKAWIKTGLLRRSPVKARKVRKKNSSLEKGGRVVLIDHAAEDVFELIKGADLVVTIGDDT
TAIAGDILYRFGIPIIGITDGDRDEVLKEPFIFPGSMILRLKPGYDDIVGKKIKKELFRGKKSAVFENLE
ELKEEVIELAKESIESVIEY
>gnl|CDD|443247 COG4070, MJ1412, Cyclophilin family protein MJ1412, methanogenesis marker protein 3 [General function prediction only]
MKVEVNGKEKTLPEGSTLKDALPASGAPYKEGTSVGIIKPTEEREEETNEYRIKTTKGEIVIELLDPTDS
AKIWKENYKEFEGLRVRWTTRDAVAFGPFPSDIPPSREEGRYERGDVIFGLGGFDPDNTYLIFSKDRHTA
DYGAPEGGVFGRVVSGRGVLDRLTEGDRILSIEPVIEWTSTGNSIVTTDLSTPLEDGMEIFTYVEVELDP
ESPESVEHFLALTRDGTFKVDYESSTFIGDDRLLGEEVPYENFEPRREGAVTVRTAGKGAGRVYIYREDR
PSSPAHTVVGHVTRGIELVKLAKEGDKITVKTVPERIMLLGMTQKEAEEFLEKLGIKQVRDGYTGDDAVV
VKQDPETTMEILKEGEVETFGVPKDKIISIELYDDLAPKSVDYFRKATGLKHKPVGTLPVFFAFPGTYLF
KFEGDAPKYKELIPENTPEKKVKAGEIGITNQSRKHHGLVGVRLEDNDEFGPTGEPFSGTNIIGKVLDLE
KLKKLKEGDTVYIREVKR
>gnl|CDD|443248 COG4071, COG4071, Gamma-glutamyl ligase family protein MJ1361 [General function prediction only]
MSLEVDGMTYRRIPIKTRYIKPNENFIEIIEEYAGILLQDGDFLVISEKVIATAQGRLVDESEYKPSFLA
KLLSYYWSKYLWGYGLGPLLGIKKRTIKNLRKMPKEARRHKQVALRECGLIHALKPASEAGVDLSNVPGT
YVSLLPENPKKVAKEISKKIKERLGKDVTVIIVDTDATYRILGKSFTSLPIAIEGIISDTGVLGYLLGNL
GKKLGPTPLAIIRKISVEELLKIANIAEDSQKKNTETVYDMMKKFDTFEITEEMLNSIEHTPAVIVRPP
>gnl|CDD|443249 COG4072, COG4072, Uncharacterized conserved protein, DUF2118 domain [Function unknown]
KIPRLYVEGKLESDKVIIEKGGNLAIFLAKDEEYPGGGKFFGKVIYERFLEYVDLVEKKVTRDFIIVYPY
DYRTGFYLKKGDKLELIPVEGYRVTPIVDEGDRVREGDRLAAITTRKGEVRYIRSPVKGIVVYVYEIPWE
KPENYVVYILPE
>gnl|CDD|443250 COG4073, COG4073, Uncharacterized conserved protein MJ0501 [Function unknown]
MFLKIYGGGGPVRLFVGGLHGDEWKDTSDILKKLKPPDSGTLAIIPVVDRGKYISTLDEDYYQTMGKKII
DLVEKYKPEIYIELHSYSGENFDKLTDPDRLDRTGVPPLSVLEEGVLLGSVSPHIRRKYFPKEALCLTFE
IPKDNDLSKEFYAKILRVIKESKSRDDFIEFLKKRYPKQAEKAIEDYREFYGLNYPPF
>gnl|CDD|443251 COG4074, Mth, 5,10-methenyltetrahydromethanopterin hydrogenase [Energy production and conversion]
MKVAILGAGCYRTHAASGITNFSRACEVAEEVGKPEIAMTHSTITMGAELKHLAGVDEVVVSDPVFDNEF
TVIDDFDYEEVIEAHKEGNPEKIMPKIREKVNEVAKELPKPPKGAIHFTHPEDLGLKVTTDDREAVEDAD
FIITWLPKGDMQPAIIEKFADDIKEGAIVTHACTIPTTKFYKIFEDLGGRDDLNVTSYHPGAVPEMKGQV
FIAEGYASEEAIETLYELGKKARGNAFKLPAELLGPVCDMCSALTAITYAGLLSYRDAVTQILGAPAGFA
QMMAKESLEQITALMEKVGIDKMEEALDPGALLGTADSMNFGPLAEILPTVLKVLEKRKK
>gnl|CDD|443252 COG4075, COG4075, Uncharacterized conserved protein MJ1244, distantly related to nitrogen regulatory protein PII [Function unknown]
MKVLLKLFVESENLGKAINALTEGGITGFYLIEYKGMSPQDWKGFLLKEDPESAIKAIRDLAEDAVLIGT
VVDEEKVEKIEKLIEEKLANERYTIIEIPIEGIKVNGP
>gnl|CDD|443253 COG4076, COG4076, Predicted RNA methylase [General function prediction only]
DYLMQFFVPRWHHPMLNDVERNDAFKAAIERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDI
AAVARRIIAANGLSDRITVINADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIP
ERITNAAQPVESPVDAEGFEDWQFDGFDFRLFGFLLYAEPLLHLTRLVRTPLLLLLLPTAFDEFPFDLAS
QRATSAQRQLETSHGNEKVL
>gnl|CDD|443254 COG4077, COG4077, Uncharacterized conserved protein MJ0491 [Function unknown]
MILHEVAGKIMGSLEAFKGSKPLFDKEEILIVRGMSRDKIDFEKYNSILEYLEEKLKAEGFDIASEEGKN
FVEKIDENIRSTVEVPTEPDIFGFERLKESFEDMGCECDYKLGKKGNLGVFVVMWKDKSGKGPKFVEVVV
SNLES
>gnl|CDD|443255 COG4078, EhaH, Energy-converting hydrogenase Eha subunit H [Energy production and conversion]
MYIPSIGGNFLGIIPFGDIVFYLSPFTLILFLVALAFTALVILSKPEKQVEIAFGTDGDKAKEVSLKELK
IRRFMAIVCGLATAGAMLTGDLFNFTLFLALIGIVNIGIVAAVKNEHVLNAAYQYGLIAMIATLPLFGGA
ALILATTGTLSIFELAKTGGPVPLYAKLLLALGVIGETGMAPFYAAKAEMFRAPGAPYILMIHLSSLLIF
VRVIEILLTI
>gnl|CDD|443256 COG4079, COG4079, Uncharacterized conserved protein, DUF2121 domain [Function unknown]
MSLIIAYYGKKGAVIAGDKRRIAFRGDEEKRKILEEELYSGEIKTDEELYKKAEELGVNLKITDDRKKVR
KIGDVLVGEVGSIGTHDTKRRRIYATKGACAIVELTGSKITNKKRGGSGIIVFGNRYTKEIAEEELKKEW
KPKMSLQDIEDLIEEIFKKVSERTPSVSKEYDIYIVNKKLDNKQAKALEEAIEEDIKNLFKYREQLREKM
IDFGKVIKIASKIVKEGEVGEIVRVDGKNGEVKLYDDVIAIDKNWVVAGPGEKVFMEVENPGEVEDGDIV
VIENEVLKVKGTDEPVACDYIICRK
>gnl|CDD|443257 COG4080, COG4080, SpoU rRNA methylase family enzyme [Translation, ribosomal structure and biogenesis]
MMEVIVVLHNPSSVQRLVDFAKTVFGFGIKTLVITKVIGAAAQSGVPEAFKLALKLGKSLIVLPDLKDAI
ELLRPDVVYLLSDSGAEELDFEELLKDNGRVLIVFSGGESGFSKKELELGEPVKIKGVESDLGPVGLAAI
FLYKLLKLKQQ
>gnl|CDD|443258 COG4081, COG4081, Uncharacterized conserved protein MJ0452 [Function unknown]
TPTMMKALIVLGCPEVPVQTPLALYLSHKLKKKGHEVTVAGNPAALKLLKVADPEGHYLGETVDLDSCID
EIAEGKRDYDLCIVFVHNDAGVTYAATMSAILNAKLIAIVFGEDAEELAELIEFPCEIIVARAVHNPMPL
KVKIDEVLEWLV
>gnl|CDD|443259 COG4083, COG4083, Exosortase/Archaeosortase [Intracellular trafficking, secretion, and vesicular transport]
MGPMTDVLAWISIALFLASALLPGRRDYARYVAAGGWVLFGVFWLLLVPHYAFEENSYVEPVLALAAVPF
CLYTAYLLLRGRDSLFVLTRAVAIMGLIYLPFATIPALREWLIETVTDQTHWLLGLLGYPPELTGWNTFL
FDGNGYTVEIILACTGIGSIAIFLGLIAAVRAPLRRKLRAFAVAVPVIYILNLFRNVFVIIAYGEQWFQW
FPDIASNLFGYVSFFWAHNVIAQLLSVVALVGITYLVVRILPELLDIIEDLLYLYTGEEYDLREALGLER
DR
>gnl|CDD|443260 COG4084, EhaM, Energy-converting hydrogenase A subunit M [Energy production and conversion]
MLSKIDMNYEELYLEMKYRILKSNRWMEDVIVPISKELKISVEEVEEILMKKLDMSSLYELHAYAEQAKM
GCLGRKVHIDLGLCWLSDFFGLISKEDADLIRKKVVEDVLLHKKPYKEALEEGRALIIELLKE
>gnl|CDD|443261 COG4085, YhcR, DNA/RNA endonuclease YhcR, contains UshA esterase domain [RNA processing and modification]
ILNEEKITIVCLTTALLGISSLIIFPLQPGEITIAEIREGLGEYVTVEGVVTAVKVARDGGILFLKLQDG
TGGINVYAFGDVAEELLNYGPFPEIKEGDKVRVTGRVTEYKGRYEIILNDPSDIKLIPKYG
>gnl|CDD|443262 COG4086, YpuA, Uncharacterized conserved protein YpuA, DUF1002 family [Function unknown]
MKKLIKLILAALLLALGLLSPTTAFADAAWGKPIVTLGADLTESQKQEVLKLLGVDDLDDAKIITVTNAE
EHKYLGGYIPKAQIGSRAYSSAKITLTDKGSGLNVEITTDNITWVTPEMYANALLTAGIEDADVYVAAPF
PVSGTAALTGIYKAYEVATGEKLDEERKEVANEELVVTSELAEEIGYSDEKANELLAEIKEEIAKQKPAT
REEIENIVNNVANNLNINLSDEQIQQLVDLMEKISNLNIDWNQVKSQLDDLSDKIKDKLGSEEDKGFLDK
IKNFFSSLIDAISSLFSS
>gnl|CDD|443263 COG4087, COG4087, Soluble P-type ATPase [General function prediction only]
MIEIEIPGRGTLELKHLVLDYNGTLAVDGKLIPGVKERLEELAEKLEIHVLTADTFGTVAKELAGLPVEL
HILPSGDQAEEKLEFVEKLGAETTVAIGNGRNDVLMLKEAALGIAVIGPEGASVKALLAADIVVKSILDA
LDLLLNPKRLIATLRR
>gnl|CDD|443264 COG4088, Kti12, tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms]
MDSPMLLILTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFLVNESFPKETYEEVVEDVRTTTAD
NALDNGYSVIVDGTFYYRSWQRDFRNLAKHKAPIHIIYLKAPLETALRRNRERGEPIPERVIARMYRKFD
KPGTKDRPDLVIDTTEDSVSETLDAILKAIETWGIRLLS
>gnl|CDD|443265 COG4089, COG4089, Uncharacterized membrane protein [Function unknown]
MRRLIYMPFSPLFLLLLLLLLLLLVLIFFGLAHRAFDRLGLSDSQALLLLLLSLIGSFINIPLYRIKSEV
PPPEERYVRFFGIPYRVPVPRERKTVVAVNVGGALIPLLLSLYLLYRAGTPAELLRALLAIAIVAAVVYL
LARPVPGVGIAMPLLIPPLVAALIAYLLGPERSARVAYIAGTLGTLIGADLLNLRKIRRLGPGVVSIGGA
GTFDGIFLSGILAVLLAEL
>gnl|CDD|443266 COG4090, COG4090, Uncharacterized conserved protein MTH_862 [Function unknown]
MEKIEESKGIGGMLRPFKELVKDKKSEKIVFVGSPGVCTPFAELLAYAIRDTEKEQYFIPDLDIEKARKL
ELTDVGMQLGDKADPHNADVVVLLGGLAMPKIGVTPEDVKELIEKVEGKKIIGVCFMSMFEKAGWTDKID
FDYIIDADIDVDVLK
>gnl|CDD|443267 COG4091, COG4091, Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism]
NLDRLLAARAAEGRPIRVGLIGAGQMGRGLLAQIRRMPGMEVVAIADRNPERARAALREAGIPEEDIRVV
DTAAEADAAIAAGKTVVTDDAELLIAADGIDVVVEATGVPEAGARHALAAIEAGKHVVMVNVEADVTVGP
LLKRRADEAGVVYTGADGDQPGLIMELYDFARALGFEVVAAGKGKNNPLDDYATPDTQAEEAERKGMNPK
MLASFADGTKTMVEMAAVANATGLVPDVRGMHGPPARVDELPDVFRPKEDGGILERGGVVDYVVGLSVAP
GVFVIVTADDPYVRHCLNYYKLGDGPYYSLYRPYHLCGLETPLSVARAVLRGEATGAPLGRPVAEVVAVA
KRDLKAGEVLDGIGGYTVYGKLEPAEVARAENLLPIGLAEGCRLKRDVKKGEVITYDDVELDEGSLIVRL
RREQDALFA
>gnl|CDD|443268 COG4092, COG4092, Predicted glycosyltransferase involved in capsule biosynthesis [Cell wall/membrane/envelope biogenesis]
MSHDSDITVIIPLRLSEDRLDVIERLARLDETLPNNIVFLIVDDGSEADFASEIRNICALLGLRYVYLET
DSKPFSRARARNYGAEYAETDLILFCDVDCLLSDDFYEKVLEEIKLLKLETNIEDFLVLPVVYLTKDATE
LFFEQFETLKKKFFLQPLLRFLKEDYEKFASGSSIIVFNRDDFLAIGGNDERFVGHGYEDFEFLIRLLSL
AKILPMPDEFTLDYTNRSIIEYKGFRAYLALYGIEALQKGLILFHLYHEKRKSSDYYKEKQRNRERFNEA
LKTYVSDKEEPLQLDDLHQEKTLVLFSKHLRQYDKPGTITYPALSIFDPRELLFLARDLLREVIVIERTA
LFGTIYYKEDVAYNSYNNINERFLQEQFSDDEGAKSRDFIEELKAGDSTLEQMDDYATTRRKLADLASVK
SPLLSQNNDLEDDEAKEMFILGEQQYPEFSDSLSETIPANPDIVFVAKPHPLSPGDHLEFVPNLILHARE
DNIPCLLVIKSFTLEYESGVGLLSILHQNPVATLGNAFLNMSGAGYRIGSGQD
>gnl|CDD|443269 COG4093, COG4093, Uncharacterized conserved protein, DUF2125 domain [Function unknown]
MRRLTRRRSRRGLFLPAVLLVLLAALWSGYWFYAASRLEAAVDAWLARRAAEGWQAECADLSVGGFPFRF
ELTCTDPRLADPGTGVAWSAPRLRAAAQVYQPGHVIAELPGPQRLSLPPGGTLTATWDDLRASLRLDGGA
LDRLSLVAEDLTLTGSAGAPPPLLSAERLELHLRRNPDTPDTYDLALSATGLALPAADRGALDPAGLLRL
DASLDGTLDGPWDLLDALEAWRPAGGRIDLARLSLQWGDLRLTASGTLSLDADGRPDGELTLRAEGWEEL
LDLLVAAGPLPAGLAATLEAALGALARPSGPGALDLPLTFRDGRVSLGPIPLGPAPPLY
>gnl|CDD|443270 COG4094, COG4094, Uncharacterized membrane protein [Function unknown]
MLLLILGLLLFLGAHSVPSVPPLRARLIARLGERGYKGLYSLVSLAGLVLLIWGFGRARYDPGVPLWPPP
PWTRHLALLLMLVAFILLVAAYFPPNPLSIGARAKPDPYEPGIKRITRHPMLVGVKLWALAHLLANGDLA
SLLLFGGFLAWALAGRISIDRRKRRRLGEAWEALRARTSVIPFAGSARGDLIAVVLGLALYAAFLLWLHP
WLIGVSPLP
>gnl|CDD|443271 COG4095, SWEET, Sugar transporter, SemiSWEET family, contains PQ motif [Carbohydrate transport and metabolism]
DLIEIIGLLAGILTTISFLPQVIKTWKTKSTKDISLGMYLIFTTGVALWLIYGILIGDLPIILANAITLV
LALIILVLKLRYR
>gnl|CDD|443272 COG4096, HsdR, Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms]
DLSEAETRKKLIDPALKEAGWDVDDQILREVRPTAGRNVVIGEWPTRGGKGYADYVLFGDDGKPLAVVEA
KRTSKDVSAGLQQAKLYADGLEKQYGQVPFIFATNGREIWFWDDRDPYPREREVDGFPSPEELWELLKRR
KGTARKRLATEPYNDGIALRYYQIEAIRRVEEAIAKGQRRALLVMATGTGKTRTAIALIYRLLKAGRAKR
ILFLADRNALVDQAKNAFKPFLPDLDAFTKLYNKSKDIDKSARVYFSTYQTMMNRIDGEEEEPGYRQFPP
DFFDLIIIDECHRGIYSKWRAILDYFDALQIGLTATPKDTIDRNTYEYFNGNPVYTYSLEQAVADGFLVP
YKVIRIDTKFDREGIRYDAGEDLSDEEGEEIELEELEEDREYEAKDFNRKVVNEDTTRKVLEELMEYLDK
PGGDRLGKTIIFAKNDDHADRIVQALRELYPELGGDFVKKITGDDDYGKSLIDNFKNPEKYPRIAVTVDM
LDTGIDVPEVVNLVFMRPVKSRIKFEQMIGRGTRLCPDLFPGKTHFTIFDFVGNTELFADPSFPLRIFEP
RREREKFWDLLGGEDPAKLAVHLADALDPDKVTIPVVAEAVQLLDDVPDLRDLLKFIDKDKRQIIYTDFE
DELLEAEEGYGKKLKAEDYRDKFEAFLREHKEIPALQKLRNRLTREDLKELEEELEEQGLGEEDLAEAYG
EVGNELADLIDLIRHIAGLDQPLLTRRERVERAFKRFLAGHKYTEEQREFLERILDHLADNGVIELEDLD
EAPFTQDGGPGGIDGLFGGVDELDEALEELNEALYA
>gnl|CDD|443273 COG4097, COG4097, Predicted ferric reductase [Inorganic ion transport and metabolism]
MKRLRALLLIALYALLVLLPLLWLLADPLPAPAGGRGLRTALGQLTGLLALALMSLQFLLAARPPWLERP
FGGLDRLYRLHKWLGILALVLALAHPLLLLGPKWLVGWGGLPARLAALLTLLRGLAELLGEWAFYLLLAL
VVLSLLRRRLPYELWRLTHRLLAVAYLLLAFHHLLLGGPFYWSPPAGVLWAALAAAGLAAAVYSRLGRPL
RSRRHPYRVESVEPEAGDVVELTLRPEGGRWLGHRAGQFAFLRFDGSPFWEEAHPFSISSAPGGDGRLRF
TIKALGDFTRRLGRLKPGTRVYVEGPYGRFTFDRRDTAPRQVWIAGGIGITPFLALLRALAARPGDQRPV
DLFYCVRDEEDAPFLEELRALAARLAGLRLHLVVSDEDGRLTAERLRRLVPDLAEADVFFCGPPGMMDAL
RRDLRALGVPARRIHQERFEFR
>gnl|CDD|443274 COG4098, ComFA, Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair]
MEELQEFLYGRLLLREELPFSLELLQALLLRGYVQTLPAIKKEPGKWRCQRCGNTDRKLFAFPCARCGQG
CYYCRNCIQMGRVSSCTPLYYWPGPNKKEPKSNPLTWEGTLTPAQQKASDELLEAIKKKEEHLVWAVCGA
GKTEMLFPAIAEALKQGGRVCIATPRVDVVLELAPRLQQAFPGVDIAALYGGSEEKYRYAQLVIATTHQL
LRFYQAFDLLIIDEVDAFPYSGDPMLQYAVKRARKPDGKLIYLTATPSKALQRQVKRGKLKVVKLPARYH
GHPLPVPKFKWLGNWKKRLRRGKLPRKLLKWLKKRLKEGRQLLIFVPTIELLEQLVALLQKLFPEERIAG
VHAEDPERKEKVQAFRDGEIPILVTTTILERGVTFPNVDVAVLGADHPVFTEAALVQIAGRVGRSADYPT
GEVIFFHHGKTRAMKRAIREIKRMNREAKKR
>gnl|CDD|443275 COG4099, COG4099, Predicted peptidase [General function prediction only]
MKKLLLLLLLLGCAAQDGFEARTFTDPSDGDTLPYRLYLPKGYDPGKKYPLVLFLHGAGERGTDNEKQLT
HGAPKFINPENQAKFPAIVLAPQCPEDDYWSDTKALDAVLALLDDLIAEYRIDPDRIYLTGLSMGGYGTW
DLAARYPDLFAAAVPICGGGDPANAANLKKVPVWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPG
VGHNSWDPAYANPDLYDWLFAQKRP
>gnl|CDD|443276 COG4100, YnbB, Cystathionine beta-lyase family protein involved in aluminum resistance [Inorganic ion transport and metabolism, General function prediction only]
EEILELVEEAEEELAPVFKEIDEIAEYNQLKVLKAFQKNRVSDSHFAGTTGYGYDDIGRDTLERVYADVF
GAEDALVRPQIVSGTHAIALALFGVLRPGDELLSITGKPYDTLEEVIGIRGEGQGSLKEFGISYRQVPLT
EDGKIDLEAIKKAINEKTKMVLIQRSRGYSWRPSLTIEEIGEIIKFVKSINPDVICFVDNCYGEFVETRE
PTEVGADLMAGSLIKNPGGGLAPTGGYIAGRKDLVELAAYRLTAPGIGKEVGATLGQNRLMYQGLFLAPH
VVGEALKGAIFAAAVFEKLGFEVSPKPDEPRSDIIQAIKLGSPEKLIAFCQGIQKASPVDSHVTPEPWDM
PGYEDPVIMAAGTFIQGSSIELSADGPIREPYIVYLQGGLTYEHVKLAILSALQALLEK
>gnl|CDD|443277 COG4101, RmlC, Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only]
MSTLTIDWAHAGVRVVRPGLDATTAGKQGLDYFEGISAETVGSTGLWMGLVTIPPGARAKAHHHGEHETA
IYVLSGRAETRYGERLEHRVVTEPGDFIFIPPGVPHQEINLSDTEPAVAVIARTDPNEQESVVNLPELDA
LVPERA
>gnl|CDD|443278 COG4102, COG4102, Uncharacterized conserved protein, DUF1501 family [Function unknown]
LSRRDFLKASAAAGAGGLALPGLLAALAAAAAAAGDKALVVVFLRGGNDGLNTVVPKGDAAYYAARPTIA
IPAPGLLPLDGFFGLHPALAGLKPLYDAGKLAVVRAVGTPNPNRSHFDAQDIWETGSPSSAGVGSGWLGR
LLDALAGYFQAVAVGGTLPLALRGPAARVLALAPPGLRLFDPARLALLAALYADDEAAALAAAYEQALRL
ATSLREAFLSKEPAATRARYPRGSFGRQLLLAARLIEAGVRVVTVSLGGWDTHGNQGGRLARLLPELDQA
LAALLDDLGQRGLLDDTLVVVMSEFGRTPRENGSGGTDHGPGGSMLLAGGGVKGGRVYGATPGLGEAPDL
DGDLKPTVDVRDLAATLLHWLGLDPAKLLGVFPGLTDFEPLGLLA
>gnl|CDD|443279 COG4103, TerB2, Tellurite resistance protein TerB [Inorganic ion transport and metabolism]
MLGKLKSFFDRLTRAPEPEALPEGDFELALAALLVEVARADGEVSEAERDAIRRLLARRFGLSPEEAAEL
IELAEELEAEAVDLYRFTSVINDHLDYEERLQLIEALWEVAYADGELDEYEEALIRRIADLLGVSHRDFI
AARARAEAR
>gnl|CDD|443280 COG4104, PAAR, Zn-binding Pro-Ala-Ala-Arg (PAAR) domain, involved in Type VI secretion [Intracellular trafficking, secretion, and vesicular transport]
MPKPAARLGDKTSHGGPVISGSPTVLIGGRPAARVGDKVSCPKHGPDTIAEGSPTVLINGKPAARVGDKT
ACGGTIISGSPTVLIGG
>gnl|CDD|443281 COG4105, BamD, Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope biogenesis]
MKKLLKLLLLLLLALLLAGCSSFKKALKSWDAEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSPYAEQ
AQLMLAYAYYKQGDYEEAIAAADRFIKLYPNSPNADYAYYLRGLSYYEQSPDSDRDQTSTRKAIEAFQEL
INRYPDSEYAEDAKKRIDELRDKLARKELEVARYYLKRGAYVAAINRFQNVLEDYPDTPAVEEALYLLVE
AYYALGRYDEAQDAAAVLGKNYPDSPYLKDAEKLLKKIGKELKK
>gnl|CDD|443282 COG4106, Tam, Trans-aconitate methyltransferase [Energy production and conversion]
PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVRFVVADLRDLDPPEPFDLVVSN
AALHWLPDHAALLARLAAALAPGGVLAVQV
>gnl|CDD|443283 COG4107, PhnK, ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism]
MTNEEQPLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVY
YRDRDGGPRDLFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERLMAAGERHYGDIRARALEW
LERVEIPLERIDDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLS
MIVVTHDLGVIRLLADRTMVMKNGRVVESGLTDQVLEDPQHPYTQLLVSSVL
>gnl|CDD|443284 COG4108, PrfC, Peptide chain release factor RF-3 [Translation, ribosomal structure and biogenesis]. Peptide chain release factor RF-3 is part of the Pathway/BioSystem: Translation factors
SELAEEIARRRTFAIISHPDAGKTTLTEKLLLFGGAIQLAGAVKARKARRHATSDWMEIEKQRGISVTSS
VMQFEYRGYVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINK
LDREGRDPLELLDEIEEVLGIDCAPMTWPIGMGKDFKGVYDRYTDEVHLFERGAGGATEAPEEIEGLDDP
ELDELLGEDLAEQLREEIELLDGAGPEFDLEAFLAGELTPVFFGSALNNFGVRELLDAFVELAPPPRPRE
ADEREVEPTEEKFSGFVFKIQANMDPAHRDRIAFMRICSGKFERGMKVKHVRTGKKIRLSNPQQFFAQDR
ETVEEAYPGDIIGLHNHGTLRIGDTLTEGEKLEFTGIPSFAPELFRRVRLKDPMKAKQLRKGLEQLAEEG
AVQVFRPLDGNDPILGAVGQLQFEVVQYRLKNEYGVEVRLEPLPYSTARWVTADDPKDLEEFKRKNRSNL
AKDRDGRPVFLFPSEWNLRYAQERNPDIKFHATREHAA
>gnl|CDD|443285 COG4109, YtoI, Predicted transcriptional regulator containing CBS domains [Transcription]
TKHIISTSYDTFKEILLVEDIMTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL
GKDDDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQKI
>gnl|CDD|443286 COG4110, TerA, Tellurium resistance protein TerA/TerD [Defense mechanisms]
VLALGGNGAGIIIAGASGVVVLASALVFAAARLGADGSDGVSGDDVVGGGEGRGSGAAADSVGVAVAIGD
LALVFALLEVVVIAAAADGGAGAGISLAGQVLLAALLGSLVGRVDASGTRAEAALLLLLLYRRRRWWKGR
VGGAGFGGGAGLLALAGGVVVAAAPAPPPPAPAPPPPPAPPVSLSKITLTKAGPSISLTKQGAGFGEIRV
NLNWNQRPKQKKGFLGKLLGGNKGIDLDLGCLYELKDGSKGVIQALGNAFGSLNRPPYIQLDGDDRTGAV
SGGENLHINGDHWDEIKRILIFAFIYEGAPNWDATDGVVTLKPPGGPPIEVRLDEGDNNARMCAIALIEN
DGGELKVTREVRYFGGHSELDRAYGWGLRWTAGSK
>gnl|CDD|443287 COG4111, COG4111, Uncharacterized conserved protein [Function unknown]
ALPGGFVREHESLEDAARRWLAEQTGLELGYLEQLYTFGDPDRDPRGRVISVAYLALVREEELRADDADD
AAWFPVDELPPLAFDHRRILATALERLRAKLEYTPIGFELLPEKFTLSELQRLYEAILGRKLDKRNFRRK
ILSLGLLEETGEKQTGGAGRPAKLYRFDKE
>gnl|CDD|443288 COG4112, YmaB, Predicted phosphoesterase YmaB, NUDIX family [General function prediction only]
DEKVLVVPRELLFELGHFQGFLKVEVERFLEIILTHGEFRPRGDAEEDPSFKQIIPYVVFKNEDEIFVYK
RGSGQGEKRLHNKLSIGVGGHINPEDAADPEEAFKNGMRRELEEEVDIEGNYSLRYVGLINDDSTEVGRV
HLGVVFLIELDSPEVTVREKDLFEGGWISLEELKEYYEELETWSQLALDALFGL
>gnl|CDD|443289 COG4113, VapC, RNA interferase (RNase) VapC, contains PIN domain [Defense mechanisms]
IVVDASALVKWLLPEEGSEEALRLLERAADELVAPDLALYEVANVLWKAVRRGRLTEEEAEEALELLLEL
PIEVVPVTELLERALELARRHGLTAYDAAYLALAERLGAPLVTADRRLARAARAL
>gnl|CDD|443290 COG4114, FhuF, Ferric iron reductase protein FhuF, involved in iron transport [Inorganic ion transport and metabolism]
RAAASLWSKRYFGLLTPPVLYALLVLDRALDLSLENVRLELHEDGRPWAFYLPDEGLPLPGLSPEERIES
LLADHLAPLIEALAAVTGISPRLLWENAAVYIYWLLEELLELLGDAARAAADAQALLDEATLPDGRRNPL
YRFVRPKTPDAGAPVRVRRTCCLRYRLPGVGYCGTCPLLKRRERDAL
>gnl|CDD|443291 COG4115, COG4115, Toxin component of the Txe-Axe toxin-antitoxin module, Txe/YoeB family [Defense mechanisms]
MKLVFTPQAWEDYLYWQKTDKKLLKRINELIKDIKRNPFEGIGKPEPLKGDLSGYWSRRINDEHRLVYRV
DDDTIKILQCRYHY
>gnl|CDD|443292 COG4116, YjbK, Predicted triphosphatase or cyclase YjbK, contains CYTH domain [General function prediction only]
SQEIEIEFKNLLTKEEYNRLLEHFNFKEEEFFTQTNYYFDTPDFDLKKHGSALRIRTKNDSYELTLKQPA
EVGLLETNDPLSLEEAKALIEGGQLPSGEVADILKELGIDPEELKYFGSLTTTRAEIPYKEGLLVLDHSF
YLDQEDYELEFEVTDEEQGKKVFDELLKEFNIPKRPAKNKIARFYDALKKS
>gnl|CDD|443293 COG4117, YdhU, Thiosulfate reductase cytochrome b subunit [Inorganic ion transport and metabolism]
MAALPMRKVYLHPLWVRLWHWLNALLIILLILSGLQIHNAHPLFGWLAGARQWHFAAAWLLVLNGLFYLF
WNLATGHWRRYLPTRKDLPRNALRDIRYYLRGRFPGKTPWRKYNPLQKLAYLGVMFLLLPLLVLTGLAMS
KPVQLPWLVDLFGGLQTARTIHFLAAFLLVAFVIVHVYLVTTVGHLRNLKAMITGYEEVDEEEE
>gnl|CDD|443294 COG4118, Phd, Antitoxin component of toxin-antitoxin stability system, DNA-binding transcriptional repressor [Defense mechanisms]
MKTVTVREAKAHLSELLDRVEAGEEVVITRRGKPVARLVPVEPPRRPRALGLLKGRLSDDFDEPL
>gnl|CDD|443295 COG4119, COG4119, Predicted NTP pyrophosphohydrolase, NUDIX family [Nucleotide transport and metabolism, General function prediction only]
MMKRSAGILLYRRRDGGLEVLLVHPGGPFWARKDEGAWSIPKGEYEPGEDPLAAARREFAEETGVPAPDG
PFIPLGEVRQKSGKVVTAWAVEGDLDPAAIVSNTFELEWPPRSGRMQEFPEVDRAAWFSLEEAREKLVKG
QRPFLDRLLALLA
>gnl|CDD|443296 COG4120, COG4120, ABC-type uncharacterized transport system, permease component [General function prediction only]
MSLNLLIGALEQGLIYAIMALGVYITFRILDFPDLTVDGSFPLGAAVAAVLIVAGVNPFLATLAAFLAGA
LAGLVTGLLHTKLKIPPLLAGILTMTALYSINLRIMGKPNIPLLGEDTIFTLLPDLGLPGDWAKLLVLLV
IVLVIKLLLDWFLKTELGLALRATGDNPQMARALGINTDRMKILGLALSNGLVALSGALVAQYQGFADVN
MGIGTIVIGLASVIIGEVLFGSRSILRRLLAVVLGSILYRLIIALALQLGLPPNDLKLITALIVAIALAL
PQLKKKLKRKKRKRKA
>gnl|CDD|443297 COG4121, MnmC, tRNA U34 5-methylaminomethyl-2-thiouridine-forming methyltransferase MnmC [Translation, ribosomal structure and biogenesis]. tRNA U34 5-methylaminomethyl-2-thiouridine-forming methyltransferase MnmC is part of the Pathway/BioSystem: tRNA modification
MKRKLQPATLTTADGSGTPYSPEFDDVYHSKHGALQESRHVFLEGNLLPERWQGRSPFVILETGFGTGLN
FLATWQAWREDAPRNARLHFISVEKYPLTPEDLARALAAWPELAPLAEQLHAQWPPLVPGCHRLELDGGR
VTLTLLFGDARELLPQLDQNGRADAWFLDGFAPAKNPEMWTEELFAKLARLLKPGGTLATYTAAGAVRRA
LQAAGFEVEKLPGFGGKREMLRARKPPRPPPLSAP
>gnl|CDD|443298 COG4122, TrmR, tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]. tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification
MPEQGRLLYLLARLLGAKRILEIGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIARENFARAGLADRI
RLILGDALEVLPRLADGPFDLVFIDADKSNYPDYLELALPLLRPGGLIVADNVLWHGRVADPARRDPSTR
AIREFNEYLREDPRLESVLLPIGDGLLLARKRG
>gnl|CDD|443299 COG4123, TrmN6, tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]. tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification
ERLDGFLFKQFRIIQPRCGYRFGTDAVLLAAFAPVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQ
PEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPGSFDLVVSNPPYFKAGSGRKSPDEARAIARHEDA
LTLEDLIRAAARLLKPGGRFALIHPAERLAEILAALRKYGLGPKRLRPVHPRPGKPAKRVLLEARKGGRA
GLRILPPLVIHDEDGEYTPEVKALLRDF
>gnl|CDD|443300 COG4124, ManB2, Beta-mannanase [Carbohydrate transport and metabolism]
SAALLLAAAATAALVSLASLLAAAAAAALAAATASIVSATGAAGAGPSSGLGGGTAKLGGAVAGAGGQGA
GGGGRGGALGGADNGAGAASGQLAAATTEYKLGAAALVTLASGLLAATPVSGAGGTNGLKPGGIAHGAYD
AYLDRIADFLKSLQAGVPVIFRPGHEMNGGWFWWGAGADPEDYKALWRHVVDYLRNTGGLPNLIWVWSPN
GGFPSSADYLDYYPGDDYVDIVGLDGYNDGPTDPWQSFDELLDPGYDELRAFARAHGKPIAITETGPEPD
PYDKAAWITDLLDALRAKYPKISYFIWFNGDDDWRVDPSPNSAAAFKKFY
>gnl|CDD|443301 COG4125, COG4125, Uncharacterized membrane protein [Function unknown]
MRSLKERIRHAVLFELIALLISAPLLAWLFGKSLGDMGALAVVLSTIAMLWNYIYNWLFDRWERRQRGVR
RTLRVRILHALGFEGGLLLILVPLIAWWLGISLWEALLLDIGLLLFFLVYTFVFNWAYDRLFPLPRSARA
AAAA
>gnl|CDD|443302 COG4126, Dcg1, Asp/Glu/hydantoin racemase [Amino acid transport and metabolism]
MMRILVINPNTSAAMTERIAAAARAVAAPGTEIEAVTAAFGPASIESRYDEALAAPGVLEAAARAEAEGA
DAVVIACFGDPGLEAARELVDIPVVGIAEAAMHAAALLGRRFSVVTTLPRTVPRIEELVRRYGLADRCAG
VRALDGPVLELEGDPERALARLAEAAREAVEEDGADVIVLGCAGMAGLAAALQARLGVPVIDGVAAAVKL
AEALVRLGLSTSKVAYAKPPPKALTGL
>gnl|CDD|443303 COG4127, COG4127, Predicted restriction endonuclease, Mrr-cat superfamily [General function prediction only]
MTRYWLVRAGRGGELYDEFLENGVVAIGWDELGDLSPIASREELKAALDEVYPDAKPGARANAAGQLWRF
VNEIQKGDLVVTPDKNKRLYAIGEVTGDYEYDPSDDDEYPHRRKVKWLKETIPRDALSQALLNSLGSFLT
VFRVSRYAEELEALLEGKSAPGEAEEEAEEETEDPAFDIEEIARDFI
>gnl|CDD|443304 COG4128, Zot, Zona occludens toxin, predicted ATPase [General function prediction only]
MMITLITGVPGSGKSYEAVWFLIIPALKKGRRVITNIPGLKILERIAEHLGLAVPDTAELINVDTDDPDG
LEKMARWFHWAPDGALIVIDEAQRVWPPRGKGSKPPDVVQAFATHRHHGWDIVLITQNISLIHSFIRALI
ERHYRHRKLDGLGLRNRYEWPEHDGNPGKKTSHDKATSKRYKYPKDVFGLYKSATTGTEVKTDKPKSIFK
SPKFLFALPLFVIGFGYASYFIYSFFSKEGDDPPAPNTPSASASAAAAPVAVPGGSVPTGNVPLVP
>gnl|CDD|443305 COG4129, YgaE, Uncharacterized membrane protein YgaE, UPF0421/DUF939 family [Function unknown]
MKRRRALRRIGLRTLKTALAAALAWLIAELLGLPYPFFAAIAAVLCLQPTVGRSLRRALERILGVLIGAL
VGVLFFLLLGYGPWQLGLAVLLAILLAVLLKLGEGIVLAAVTALLVLLLGSPDDSLGYALNRLLDTLIGV
GVALLVNLLLLPPDPERRLRRAAAELLEELADILRELLRLRDASDAEEALKRLRELQ
>gnl|CDD|443306 COG4130, COG4130, Predicted sugar epimerase, xylose isomerase-like family [Carbohydrate transport and metabolism]
MMILIRFALNHMIAPRLSLEAFFALARRLGLNAVELRNDLPGNEITDGTPAAEVRALAAAYGIEILSINA
LYPFNVWSDERAAEAEALAAYAQACGAKALVLCPLNDGTDVRTGERQANLVAALRALKPILEEYGITGLV
EPLGFPISSLRSKAEAVEAIRAVGGEDPFKLVHDTFHHHLAGETQFFPEWTGLVHISGVEDPRVAVADMR
DEHRVLVDEADRLGNIAQIRALLAAGYRGPYSFEPFASEVHALADPEAALRASMDYIRSALA
>gnl|CDD|443307 COG4132, COG4132, ABC-type uncharacterized transport system, permease component [General function prediction only]
MTTASRRRRRKWLAWLGLLPFFLFVLLFLLLPTVWVVIGAFQDDDGGFTLANYAELTSPFYLQAFWNSIW
LSLASALIGAVIGLLLAYALRRGGPGWLRRAVLAFSGVASNFAGVPLAFAFIATLGRNGLVTLLLKQLGI
DLYDGFNLYSFWGLILVYLYFQIPLMVLLLYPALDGLRREWREAAALLGASRWQYWRRVALPVLAPSLLG
TFLLLFANAFGAYATAYALTGGNYNLVPIRIGALISGDVLLDPNLGAALALGMIVIMALVMALYQWLQRR
SRRWLR
>gnl|CDD|443308 COG4133, CcmA, ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones]
MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR
EDYRRRLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRV
ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGDFK
>gnl|CDD|443309 COG4134, YnjB, ABC-type uncharacterized transport system YnjBCD, periplasmic component [General function prediction only]
MRRLALALALLALLLAACSAALAAADWQAIEAEARGQTVYFNAWGGDPNINDYIDDWVAPQLKERYGITL
EHVKLADTADAVNRVLAEKQAGKDDGGSVDLIWINGENFAAMKEAGLLFGPFAEKLPNWAYVDTEKPTVT
TDFGVPVDGYEAPWGMAQLVFIYDSARVPNPPRSLAELLEWAKANPGRFTYPAPPDFTGSTFLKQALYEL
TGDPDALQQPVDEAKFAKVTAPLWAYLDELHPYLWRQGKTYPASNAALDQLLADGEIDMAMSFNPAEASS
AIANGELPPTVRTFVFDGGTIGNTHFLAIPFNAPNKAGAMVVANFLLSPEAQARKADPAVWGDPTVLDLD
KLPAEQRAAFDALPLGPATLSPEELGNALPEPHASWVEAIEEEWLKRYGAK
>gnl|CDD|443310 COG4135, YnjC, ABC-type uncharacterized transport system YnjBCD, permease component [General function prediction only]
ARSLLLRLAPALTLLLLLGPVLAGLAGTLLPAFGYLPALGGTGFSLAPWRALFAWPGLGRSILLSLFTGL
AATLLALLLALLILAAFYGTRLFRRLERLLSPLLAVPHAAAAIGLAFLIAPSGWLARLLSPWLTGWDRPP
DLLLVQDPYGLSLILGLVLKEVPFLLLMSLAALPQLNVRRSLAVARSLGYGRATAWLKVVLPQLYPQIRL
PVFAVLAYSLSVVDVALILGPTTPPTLAVLIWQWFNDPDLSLRLQAAAGALLQLLLVLAALLLWRLLERL
VARLGRRWLSSGRRGLGDPALRRLGLALMLLIALLSLLGLALLLLWSFAGRWRFPDALPSSWTLRFWQRA
APGLLEPLGNTLLLALASALIALVLVLACLEAEARRGRRPGRRALWLLYLPLLVPQIAFLFGLQVLLLRL
GLDGTWLAVIWAHLVFVLPYVFLSLAGPWRALDPRYAQVAASLGASPWRVFWRVKLPLLLRPILTAAAVG
FAVSVAQYLPTLLIGAGRVATLTTEAVALASGGDRRVIAVYALLQALLPLLGFALALLIPALLFRRRRGM
RHGR
>gnl|CDD|443311 COG4136, YnjD, ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only]
MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRRLTA
LPAEQRRIGILFQDDLLFPHLSVGENLAFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRA
RVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGNWQ
H
>gnl|CDD|443312 COG4137, YpjD, ABC-type uncharacterized transport system, permease component [General function prediction only]
MSLLLLALLAALLYLAAALLLLRRLLRRRPPLRRLALLLLALALLLHGLALYLRIFTAGGLNLGFFNALS
LVAWLIALLYLLESLRFPLDGLGPFVLPLAALALLLALLFPGEHILPLLLSPWLLLHILLALLAYSLLAI
AALQALLLLLQERQLKHKRLGGLLRRLPPLLTLERLLFRLIAAGFVLLTLTLLSGFLFSEDLFGQHLRWD
HKTVLSLLAWLVFAVLLWGRWRLGWRGRRAARWTLAGFLLLLLAYFGSRFVLEVILHRF
>gnl|CDD|443313 COG4138, BtuD, ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]
LQLNDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARH
RAYLSQQQSPPFAMPVFQYLALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAV
LLQVWPTINPEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGK
LVASGETAEVMTPENLSEVFGVKFRRLEVEGHRWLIPT
>gnl|CDD|443314 COG4139, BtuC, ABC-type cobalamin transport system, permease component BtuC [Coenzyme transport and metabolism]
MQLPQRQRRRDRRWLLLLLLLLLLLFVLSLCAGEVWIPPTQWLSEAWQLFVWQLRLPRTLAAVLVGASLA
VSGAVMQALFENPLAEPGLLGISNGAGVGLVLVVLLGGGLLPPWLLSLAAIAGALLVTLLLLAFARRRLS
NARLLLIGVALGIICSAIMTWAVYFSSSLDLRQLMYWMMGSFGGVDWRQLWLLLALLPVLLWLCLQGKPL
NLLLLGENQARQLGLSVHRWRNLLVLATGLLVGVSVALAGPIGFVGLVVPHLLRLLGTTDHRFLLPACAL
AGAALLLLADIIARLALSSAELPIGVVTATLGAPVFIWLLLRRRKIR
>gnl|CDD|443315 COG4143, TbpA, ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism]
MKRRTFLLAAALALALALAGCSGAAAAAKPTLTVYTYDSFASEWGPGPWLKAAFEAECGCTLEFVAPGDG
GELLNRLRLEGANPKADVVLGLDNNLLARALDTGLFAPHGVDALDALALPLAWDPDDRFVPYDYGYFAFV
YDKTKLLNPPESLEDLVDPEYKDKLVVQDPRTSTPGLAFLLWTIAAYGEDGALDYWQKLADNGVTVTKGW
SEAYGLFLKGEAPMVLSYSTSPAYHVIAEGDKDRYAAALFDEGHYRQVEGAGVLAGAKNPELARKFLDFL
LSPEFQAEIPTRNWMYPAVEDVELPEAFDEYAPVPEKPLTFDPDEIAANRDAWIDEWQRAVSG
>gnl|CDD|443316 COG4145, PanF, Na+/panthothenate symporter [Coenzyme transport and metabolism]
MMNLAILIPLLIYLLLVLGIGIYASRKRSKGSFLEEYFLGSRSMGGFVLAMTLAATYTSASSFIGGPGAA
YKYGLGWVLLAMIQVPTAFLTLGVLGKKFAILGRKYNAVTLADWLRARYQSKALVLLAALLLLLFFIAFM
VAQFVGGARLLETVTGISYTTGLLIFGVTVVLYTTIGGFRAVVLTDAIQGIIMLVGTVLLLIGVISAGGG
IENIMSTLAAIDPNLVSPTGPDGFLPRPFVISFWILVGFGVIGLPHTAVRCMAYKDSKSLHRAMIIGTIV
VGLLMFGMHLIGVLGRAVLPDLTVPDQVIPTLMVKVLPPFLAGIFLAGPLAAIMSTVDSLLLQASSTIVK
DLYLNYINPKASENEKKLKRLSKLVTLVLGLIVFLLALNPPDLIIWLNLFAFGGLEAAFFWPLVLGLYWK
RANATGAIASMLVGVASYFLLYYGNPKIFGFHAIVPSLLISLIAFLIGSLLGKPPDEERLELFF
>gnl|CDD|443317 COG4146, YidK, Uncharacterized membrane permease YidK, sodium:solute symporter family [General function prediction only]
MGLSTLDYIVFLLYFLLVAGIGYWVSRKKKEKTSEDYFLAGRSLTWWVIGASLIATNISAEQLIGLNGSG
YATGLAVAAYEWMAAIALIILALFFLPFYLKSGIYTMPEFLEKRYDRRTRTILSILFLVSYVFVNLPSVL
YAGALALNTIFGVPLWISVIGLGIIAGIYTIFGGLKAVAYTDVIQGIGLIIGGLLITVLGLDAVGDGSVL
AGWSALLKVPPEKFNMIGPADDPDLPWLGIFTGMPILNLFYWGTNQYIVQRALGAKNLKEAQKGVLFAGF
LKLLIPFIVVLPGIIAFVLFPDGLDNPDQAYPTLVKNLLPVGLKGLVAAALFAAIMSSLASALNSSSTLF
TLDIYKKYFNPNASEKQLVKVGRIATVVLAVIAILIAPLIGNADGLFQYIQEVTGFFSPPILAVFLLGLF
WKRVTAKAAKVALIAGIVLSILLK
>gnl|CDD|443318 COG4147, ActP, Na+(or H+)/acetate symporter ActP [Energy production and conversion]
MLALLEQLGMNLLAIGIFLVFVTFTLYITIWAARRTKSTSDFYVAGRGVTGVQNGLAIAGDYMSAASFLG
IAGLIALSGYDGLIYSIGWLVGYVLLLLLLAEYLRNFGKFTVPDFLGDRFYSRPARLVAAISTLVVSFFY
LIAQMVGAGVLISLLLGVDYEVAVVIVGVLMIVYVVLGGMKGTTWVQIIKAVLLIFAYTVPAVLVLAQFG
FNPLPLLAKAAEVHDLGAAYLEPGGLVKSPLDFISLGLALMLGTAGLPHILMRFFTVPDAKEARKSVGWA
LGFIGLFYLTAPALGFGARALVGPLPEWFDTGLIGAADGGGNMAVLALAEIAGGGNWLLGLVAAGAFATI
LAVVAGLLLAIASAISHDLYANVIKGKATEKEELRVARIAAVVIGVVAILLGINAPPQNVAFLVALAFAL
AASANFPVLLLSIFWKRFNTRGAVAGMLVGLISALVLIVLSPFVWVLGVDAALFPLENPGLVSMPLGFLV
AIVVSLLTPEPPAEDQELVEEQEVRSPTGIGAAKAS
>gnl|CDD|443319 COG4148, ModC, ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]. ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
MMLEVDFRLRRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGI
FLPPHRRRIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQ
RVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQG
RVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAHDPDYGLTRLALGGGRLWVPRLDLPPGTRVRVRI
RARDVSLALEPPEGSSILNILPGRVVEIEPADGGQVLVRLDLGGQTLLARITRRSADELGLAPGQTVYAQ
IKSVALLR
>gnl|CDD|443320 COG4149, ModB, ABC-type molybdate transport system, permease component ModB [Inorganic ion transport and metabolism]. ABC-type molybdate transport system, permease component ModB is part of the Pathway/BioSystem: Molybdopterin biosynthesis
LSPEDWSALWLSLKVALIATLLLLLLGIPLAWWLARTRFRGKGLLEALVTLPLVLPPTVLGFYLLLLFGR
NGPLGQLLEELFGISLVFTWTGAVLASVVVSLPLMVQPLRAAFEAVDPRLEEAARTLGASPWRVFFRVTL
PLAKPGILAGAVLAFARALGEFGATLMFAGNIPGKTQTLPLAIYDAVEAGDYAAAHALSLILLAISFVVL
LLLNLLNRRRRRR
>gnl|CDD|443321 COG4150, CysP, ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and metabolism]
MKMKKLLLAGAAALALAAPAAAAATELLNSSYDIARELFAALNPAFVAQWKAQTGDDLTIKQSHAGSSKQ
ARAILQGLKADVVTFNQVTDVQILHDKGNLIPADWQARLPNNSSPYYSTMAFLVRKGNPKNIKDWDDLAR
DDVKLVFPNPKTSGNGRYTYLAAWGYALEAFGGDEAKTREFMKKFLANVAVFDTGGRGATTTFVERGIGD
VLITFESEVNNIRKQYGADGYEVVVPPVSILAEFPVAVVDKNVEKNGTEEAAKAYLNYLYSPEAQRILAG
FNYRVNDEAVAAEFADRFPEVKLFTVEDVFGGWDQVMKTHFASGGELDQLLAAG
>gnl|CDD|443322 COG4152, YhaQ, ABC-type uncharacterized transport system, ATPase component [General function prediction only]
MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR
RRIGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQL
IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS
GSVDEIRRQFGRNTLRLEADGDAGWLRALPGVTVVEEDGDGAELKLEDGADAQELLRALLARGPVREFEE
VRPSLNEIFIEVVGEKAE
>gnl|CDD|443323 COG4154, FucU, L-fucose mutarotase/ribose pyranase, RbsD/FucU family [Carbohydrate transport and metabolism]
MLKGIDPLLSPELLKVLAEMGHGDEIVLADANFPAESLARRVVRLDGHSAPELLEAILSLFPLDTFVDDP
VVRMEVVGGPDEVPPVWAEYQAIIAKAEGRPVPIERLERFAFYERAKKAYAVVATGETRLYGNIILKKGV
IPP
>gnl|CDD|443324 COG4158, COG4158, Predicted ABC-type sugar transport system, permease component [General function prediction only]
MTTSPPAPAAPSAAPAAARRFRLRSLLQAVGMLPVLILLCIGFELLTPNFLTVQNLSNIARQASINIVLA
AGMTFVILTGGIDLSVGSILAASAVVAVLVSLLPGLGLLGIPAALLVGLLFGLINGLLIAFLKLPPFIVT
LGSLTALRGAARLLANGTTVFNPDLPFAWIGNGYLLGIPWLVVIALAVVLASWFILRRTVLGVHIYAVGG
NAQAARLTGIKVWRVLLFVYAVSGLLAGLGGVMSAARLYAANGLQLGQGYELDAIAAVILGGTSFVGGIG
SIWGTLIGALIIAVLNNGLILLGVSDFWQFIIKGLVIIIAVALDRYRQRGSART
>gnl|CDD|443325 COG4160, ArtM, ABC-type arginine/histidine transport system, permease component [Amino acid transport and metabolism]
MDLDLLFEYLPLLLSGLPLTLQLLALSLLLGFLLAVPLALARASGNRLLRWPARGYIYVFRGTPLLVQLF
LIYYGLGQFEWVRESWLWPLLRDPWFCALLALTLNTAAYTAEIFRGAIRAVPKGEIEAARALGMSRWQTF
RRIILPSALRRALPAYSNEVILMLKATALASTITVMDLTGVARRIYSRTYDPFEPFLIAALIYLVITFLL
TRLFRLLERRLLRHLRPRR
>gnl|CDD|443326 COG4161, ArtP, ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]
MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQ
KPSEKAIRLLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPL
HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQ
VVYMEKGRIIEQGDASHFTQPQTEAFAHYLSH
>gnl|CDD|443327 COG4166, OppA, ABC-type oligopeptide transport system, periplasmic component [Amino acid transport and metabolism]
MKKRKALLLLALALALALAACGSGGKYPAGDKVNDAKVLRLNNGTEPDSLDPALATGTAAAGVLGLLFEG
LVSLDEDGKPYPGLAESWEVSEDGLTYTFHLRPDAKWSDGTPVTAEDFVYSWKRLLDPKTASPYAYYLAD
IKNAEAINAGKKDPDELGVKALDDHTLEVTLEAPTPYFPLLLGFPAFLPVPKKAVEKYGDDFGTTPENPV
GNGPYKLKEWEHGRSIVLERNPDYWGADNVNLDKIRFEYYKDATTALEAFKAGELDFTDELPAEQFPALK
DDLKEELPTGPYAGTYYLVFNTRRPPFADPRVRKALSLAIDREWINKNVFYGGYTPATSFVPPSLAGYPE
GEDFLKLPGEFVDGLLRYNLRKAKKLLAEAGYTKGKPLTLELLYNTSEGHKRIAEAVQQQLKKNLGIDVT
LRNVDFKQYLDRRRNGDFDMVRAGWGADYPDPGTFLDLFGSDGSNNYAGYSNPAYDALIEKALAATDREE
RVAAYRAAERILLEDAPVIPLYYYTNARLVSPYVKGWVYDPLGVDFKAAYIEK
>gnl|CDD|443328 COG4167, SapF, ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]
MSALLEVRNLSKTFKYRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEI
LINGHKLEYGDYKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLP
EHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHL
GIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTKRLIESHFGEALTADAWRR
>gnl|CDD|443329 COG4168, SapB, ABC-type antimicrobial peptide export system, permease component SapB [Defense mechanisms]
MLIYLLRRLNLLLITLLILSLISFSLLYRDPLNPLSDASLFSGYLFYLQNLLQGDFGISSINGEPILEQL
LTVFPATLELCFLAFLLALLIGIPLGILAGIYRGKWLDKLISSLSLLGFSIPVFWLALLLILFFSLNLGW
LPVSGRYNLLYEIPPVTGFALIDAWLSDSPYRLKAIQSALQHLILPTLVLAVAPTTEVIRLTRQSTEEVM
NQNYIKAAATRGLSRFTIIRRHVLRNALPPIIPQLGLQFSTMLTLAMITEVVFSWPGIGRWLINAIRQQD
YAAISAGVIVIGTFVIIVNILSDILGALLNPLKRKEWYALR
>gnl|CDD|443330 COG4170, SapD, ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]
MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRW
NGIDLLKLSPRERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKWWQRFKWRKKRAIELL
HRVGIKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGT
SILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALLRSMPDFRQPLPHKSRLNTLPG
SIPPLQHLPIGCRLGPRCPYAQKKCVETPRLRKIKGHEFACHFPLNMEEKK
>gnl|CDD|443331 COG4171, SapC, ABC-type antimicrobial peptide export system, permease component SapC [Defense mechanisms]
MPSDNIYEEERIPSPLKQIWQSFRKNPLAMIGLYGFLFLILLALFGPLLAPYSPDQQFIGALLLPPSWDD
NGDVSFFLGTDDLGRDILSRLLYGARYTFGSALLVVLAAAIIGGIIGILAGMSRGLKSSILNHLLDTLLS
IPSLLLAIIIVALLGPGLENAMLAITLALLPQFIHAIYQAVHQELKKEYVLAARLDGASNWQLLRYSILP
NILEVLVTELTRALSIAILDISALGFLGLGAQLPSPEWGAMLGDSLELIYLAPWTVILPGLAIMFSVLIV
NLVGDGLRRALNKGVE
>gnl|CDD|443332 COG4172, YejF, ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism]
MMSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGS
ILFDGQDLLGLSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLER
VGIPDPERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMAL
LLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPPLLEARD
LKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLD
GLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARH
RYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVR
ALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE
>gnl|CDD|443333 COG4174, YejB, ABC-type microcin C transport system, permease component YejB [Secondary metabolites biosynthesis, transport and catabolism]
MGAYILRRLLLMIPTLLGIMLINFVIVQFAPGGPVEQVIAQLQGTGGGATGRISGGGGDAGGGAAAGGGS
KYRGARGLDPEFIAELEKQYGFDKPAHERFLLMLKNYLRFDFGESYFRDISVIDLILEKLPVSISLGLWS
TLLTYLISIPLGIRKAVRDGSRFDVWTSTVIIVGYAIPGFLFAILLIVLFAGGSYFDWFPLRGLTSDNWD
QLSWWGKILDYLWHLTLPVTAMVIGGFATLTLLTKNSFLDEIRKQYVLTARAKGLSERRVLYGHVFRNAM
LIVIAGFPAAFIGAFFTGSLLIETIFSLDGLGLLGFEAVVNRDYPVVFGTLYIFTLIGLVLKLISDLTYV
LVDPRIDFEAREV
>gnl|CDD|443334 COG4175, ProV, ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism]
MPKIEVRNLYKIFGKRPERALKLLDQGKSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLV
RCLNRLIEPTAGEVLIDGEDITKLSKKELRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAER
RERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQ
AKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDVDRSKVLTAGSVMR
PPEAVVSEKDGPRVALRRMREEGISSLYVVDRDRRLLGVVTADDALEAVKGEKDLEEILLTDVPTVSPDT
PLRDLLPLVAESPYPLAVVDEDGRLLGVISRGSLLAALA
>gnl|CDD|443335 COG4176, ProW, ABC-type proline/glycine betaine transport system, permease component [Amino acid transport and metabolism]
MDEPEDPKIPLGDWVDAAVDWLTDNFGGFFDAISDVLEGLLDGLEDLLLALPWWVVILLVAALAWRLRGW
RLALFTALGLLLIGNLGLWEEAMQTLALVLVAVLIALLIGIPLGILAARSDRVSRIVRPVLDFMQTMPAF
VYLIPAVMLFGIGKVPGVIATVIFALPPAIRLTNLGIRQVPKELVEAADAFGATPWQLLFKVQLPLALPT
IMAGVNQTIMLALSMVVIASMIGAGGLGQEVLRALQRLDIGLGFEAGLAIVILAIILDRITQALG
>gnl|CDD|443336 COG4177, LivM, ABC-type branched-chain amino acid transport system, permease component [Amino acid transport and metabolism]
SPYYLSLLTLILIYAILALGLNLLLGYTGLLSLGHAAFFGIGAYAAALLTTHLGLPFWLALLLAGLVAAL
LGLLIGLPALRLRGDYLAIATLAFAEIVRLLALNLESLTGGADGLSGIPRPTLFGLDLGSPLAFYYLVLA
LLVLVLLLLRRLVRSRFGRALRAIRENEIAAEALGINVTRYKLLAFVLSAALAGLAGALYAHYVGFVSPE
SFSFLLSIEILLMVVLGGLGSLLGPVLGAVLLVLLPELLRSLPEYRLLIFGLLLILVVLFRPRGLAGLLR
RLRRR
>gnl|CDD|443337 COG4178, YddA, ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only]
RSLLRQFWRLARPYWRSEEKWKAWGLLALLLLLTLASVGLNVLLNFWNRDFYDALQARDAAAFWQQLGVF
ALLAAISILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFTET
TLSLSLGLLSSVVTLISFIGILWSLSGSLTFTLGGYSITIPGYMVWAALIYAIIGTLLTHLIGRPLIRLN
FEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRRLIRRQRNLTFFTTGYGQLAV
IFPILVAAPRYFAGEITLGGLMQAASAFGQVQGALSWFVDNYQSLAEWRATVDRLAGFEEALEAADALPE
AASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI
ARPAGARVLFLPQRPYLPLGTLREALLYPATAEAFSDAELREALEAVGLGHLAERLDEEADWDQVLSLGE
QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG
SWQLLPAEAPA
>gnl|CDD|443338 COG4181, YbbA, Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism]
MSSSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVR
LAGQDLFALDEDARARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRL
DHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA
ARCDRVLRLRAGRLVEDTAATAA
>gnl|CDD|443339 COG4185, COG4185, Predicted ABC-type ATPase or kinase [General function prediction only]
MAMPRLYIIAGPNGAGKSTFARTILPEELGGLEFVNADLIARGLSPFNPETAAYEAGRLALERREELLAA
GRSFAFETTLSGPSKLDLIREAKAAGYRVRLIFVGLDSPELAIARVAQRVAEGGHDVPEDKIRRRYPRSL
ANLAEALPLADRAYVFDNSGEKPRLVAEKEDGQIVLLDIDDLPDWAKPALLAALERS
>gnl|CDD|443340 COG4186, COG4186, Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily [General function prediction only]
MIYFTSDTHFGHANIIKFCPRPFASVEEMDEALIANWNATVGPDDTVYHLGDFAFGGSAEEAREILRRLN
GRKHLIRGNHDGKLLLRLPAGFASVQDYAEIKLGGRRLLLCHYPLRTWNGADRGAWHLHGHVHGNRLLKP
TRRSINVGVDAWDYRPVSLEEILERLD
>gnl|CDD|443341 COG4187, RocB, Arginine utilization protein RocB [Amino acid transport and metabolism]
MKKWQTKEQLEELLCELVSIPSVTGTEGEKEVAEFIYEKLSELPYFQENPEHLGLHPLPDDPLGRKNVTA
LVKGKGESKKTVILISHFDVVDVEDYGSLKPLAFDPEELTEALKEIKLPEDVRKDLESGEWLFGRGTMDM
KAGLALHLALLEEASENEEFPGNLLLLAVPDEEVNSAGMRAAVPLLAELKEKYGLEYKLAINSEPSFPKY
PGDETRYIYTGSIGKLMPGFYCYGKETHVGEPFSGLNANLLASELTRELELNPDFCEEVGGEVTPPPVSL
KQKDLKEEYSVQTPHRAVAYFNVLTLERSPKEILEKLKKIAEEAAEKILEHYKEQYEKYCKLTGEPFVPL
PWKVKVLTYEELYEEAVKKYGEDFVEAIEEIAEKLNNGELDDREFSIKLVEELAELCKDKAPMIVIFFAP
PYYPHVNNRGESEKDPLILKAVEEVLEYAKEKFGETLEIKHFFPGISDLSYVGLPEDEEGIEALEDNMPG
WGKGYSLPFEEIRKLNIPVINIGPYGKDAHKWTERLYKPYSFEVLPDLLEKTIEELLKKS
>gnl|CDD|443342 COG4188, COG4188, Predicted dienelactone hydrolase [General function prediction only]
LLALLALLLAAAAAASPLRQPGPFAVGVQTLTLRDPSRDRPLPVDVWYPATAPADAPAGGPFPLVVLSHG
LGGSREGYAYLAEHLASHGYVVAAPDHPGSNAADLSAALDGLADALDPEELWERPLDLSFVLDQLLALNK
SDPPLAGRLDLDRIGVIGHSLGGYTALALAGARLDFAALRQYCGKNPDLQCRALDLPRLAYDLRDPRIKA
VVALAPGGSGLFGEEGLAAITIPVLLVAGSADDVTPAPDEQIRPFDLLPGADKYLLTLEGATHFSFLDPC
TPGAAILPEPDPPGPDRAAIHEYLNALSLAFFDAYLKGDPAAWLTT
>gnl|CDD|443343 COG4189, COG4189, Predicted transcriptional regulator, ArsR family [Transcription]
MVVLDDEESLEVLKALASETRLRILRLLAEEPLNVNELAEALGLPKSTVSYHIRKLEEAGLIRTEYKPGK
RGRQKICYLRVDKILIVLPGLDESDRE
>gnl|CDD|443344 COG4190, COG4190, Predicted transcriptional regulator, contains HTH domain [Transcription]
MKTLKIGIASLEEFRARALAAARGADAGEKPEPAEPVLSFESPESLARVLTPKRLELLRAIAEEGPESIR
ELARRLGRDVKNVHRDLKTLEELGLVELEEDGRAKRPVVPYDEIEIDFPLR
>gnl|CDD|443345 COG4191, COG4191, Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms]
ALRLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLA
LLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEKLA
ALGELAAGIAHEINNPLAAILGNAELLRRRLEDEPDPEELREALERILEGAERAAEIVRSLRAFSRRDEE
EREPVDLNELIDEALELLRPRLKARGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINAIDAMEEGEGGRI
TISTRREGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVGKGTGLGLSISYGIVEKHGGRIEVESEPGG
GTTFTITLPLA
>gnl|CDD|443346 COG4192, COG4192, Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms]
MKKLLKRLGIGARLLLAFALSALLTLVASLVALFSWNSLSNQIRYILDDSLPKLQASLKLEENSNELVAA
LPEFAAATNTTERSQLRNQLNTQLADIEELLAELEQLTQDAGDLRAAVADLRNLLQQLDSLLTQRIALRR
RLQELLEQINWLHQDFNSELTPLLQEASWQQTRLLDSVETTESLRNLQNELQLLLRLLAIENQIVSLLRE
VAAARDQADVDNLFDRLQYLKDELDRNLQALKNYPSTITLRQLIDELLAIGSGEGGLPSLRRDELAAQAT
LEALAEENNSILEQLRTQISGLVGNSREQLVALNQETAQLVQQSGILLLAIALLSLLLAVLINYFYVRRR
LVKRLNALSDAMAAIAAGDLDVPIPVDGNDEIGRIARLLRVFRDQAIEKTQELETEIEERKRIEKNLRQT
QDELIQAAKMAVVGQTMTSLAHELNQPLNAMSMYLFSAKKALEQENYAQLPTSLDKIEGLIERMDKIIKS
LRQFSRKSDTPLQPVDLRQVIEQAWELVESRAKPQQITLHIPDDLMVQGDQVLLEQVLVNLLVNALDAVA
TQPQISVDLLSNAENLRVAISDNGNGWPLVDKLFTPFTTTKEVGLGLGLSICRSIMQQFGGDLYLASTLE
RGAMVILEFN
>gnl|CDD|443347 COG4193, LytD, Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism]
TGYVTNGNADTVVDKTSTSATDAVNVATTAQLQAGATKTPTTGVTGGNVSTASYVGNVTGIVTTSYGNAY
AAASAQKSSAGTLVGAGNVGIIKYYKKSGVVSIKAGGNSLTKASVGEKSYSITNGKYTNTTDSLVYVTYA
KYFGPESYYTYLLSLLYKQLSSVGGVAVYVDADWLNVIPTESVPGGNLKHNSYNHSLKSAAAKQYSYSWM
YYDGGGWYSASGSDIAYYMDPRNFLNDEYNYFQFLDLRYSSNYSAEELNKYLKGTFTKGILIGKGQAFIE
AAKKYGVNPLYLASHALLETGNGTSKLAKGVEVNGKTYYNLFGIGAYDSNPLENGAKYAYKQGWTSPEKA
IVGGAKFIGSNYINNTGYGQNTLYKMRWNPVNPGTNHQYATDPFWAEKIAGHMYRAYKKLKDYNLYFDIP
VYK
>gnl|CDD|443348 COG4194, COG4194, Uncharacterized membrane protein, DUF1648 family [Function unknown]
MNSILILLLVILLFLGLLQAITPYLTRRTIVFGVRVPEERVKDPEIKAIKKRYRRRVLLLGILAAILSIL
LIALLSLLLLVALFVLIILSFLLYLLFHRKVKALKKQEGWYKGSKQVVVVDTSFRKRKKPVPWLWFLLPL
LIIIATLVVGLLGYPSLPDRIPTHWGFSGEPDAWAPKSPGSVFSPVLIQLGMTALLLFINVVILRSKPQL
DPANPAASAERNLKFRRAWSILLLITSILLNLLLLLIQLSVWGPIAPLPLLLILVLIPVLLILLGALVLS
LRVGQGGSRLKRNVEEEADSGLMDRDDDRYWKLGLFYVNPDDPAIFVEKRFGVGWTLNFARPLAWLILAG
IIAVPILIILLVILLP
>gnl|CDD|443349 COG4195, YjqB, Phage-related replication protein YjqB, UPF0714/DUF867 family [Mobilome: prophages, transposons]
MKKRLEKEASAATDKYSSFTELKENEVEGVDYRIRTRDRGSDVLVMAPHGGGIEPGTSELARAIAGGDYS
YYLFEGLKPSGNRELHVTSTNFDEPLALAMVAESDYVLSIHGCAGDEETTYVGGLDRALAEAIKEALTRA
GFTVKSAPPRLAGTSPENICNRGKSGEGVQLELSTGLRKALFKDFTLLGRARTTEVFYDFVAAVREALSD
LYPL
>gnl|CDD|443350 COG4196, COG4196, Uncharacterized conserved protein, DUF2126 family [Function unknown]
MMIIVALHHHTTYYYDRRVVLLPPVIRLRPAPHHRTTILSYSLKIEPPHHFFNWQQDPFGNNLARVVFPE
KTTEFLVVVVLVAAMVVINPFFFFFEEEAAEFPFFYYELLLKELLPYLLEEELGPLLLAFLASIDRKPPR
TIDFLVVLNNRLQQRIIYYIRREPGVQTPEETLLLAGGSCRDSSWLLVQLLRRLGLAARFVSGYLLQLLA
DDKSLDGPPGGEEDFTDLHAWWEVYLPGAGWWGLDDTSGLLAGEGHIPLAATPPPPSAAAIIGGADDCEV
EFFFFMMVVRRIHEDPRVTKPYTDEQWQAIDALGHKVDADLAAGDVRLTMGGEPTFVSIDDMESPEWNTA
ALGPTKRELADDLIRRLRDRFAPGGLLHYGQGKWYPGEPLPRWALSLYWRKDGEPIWRDPSLLADEDKDY
GATAEDAERFAEALAERLGLDADYVLPAYEDPAYYLWRERRLPVNVDPLDAKLDDPEERARLARVFERGL
DKPVGYVLPLQRWQAQGGRWRSGRWFLRRGRLFLIPGDSPMGLRLPLDSLPWVPPADYPYIHPRDPFAPR
GPLPDYAELRQRYAGPVPAEAGPAQDRVPAAVESAEGVVRTALCVEPRDGRLHVFMPPLERLEDYLELVA
AIEATAAELGLPVVIEGYEPPRDPRLNVLRVTPDPGVIEVNIHPAASWDELVEITETLYEEARQSRLGTE
KFMLDGRHTGTGGGNHVVLGGATPADSPFLRRPDLLRSLITYWQNHPSLSYLFSGLFIGPTSQAPRVDEA
RHDSLYELEIAFAQIPEPGAGEVPPPWLVDRLLRNLLVDVTGNTHRAEFCIDKLYSPDSPTGRLGLLEFR
AFEMPPHARMSLAQQLLLRALVARFWKEPYRGPLVRWGTELHDRFMLPHFVWQDFLDVLADLRRAGYPFD
PEWFAPFFEFRFPRYGEVQVGGVELELRQALEPWHVLGEEGAAGGTARYVDSSVERLQVKVTGLTPDRYV
VTCNGRRVPLRPTGTAGEFVAGVRYRAWQPPSALHPTIPVHAPLVFDLVDTWNGRSLGGCTYHVAHPGGR
NYDTFPVNAYEAEARRLARFEDHGHTPGPVDPPPEEPNPEFPLTLDLRRPP
>gnl|CDD|443351 COG4197, YdaS, DNA-binding transcriptional regulator YdaS, prophage-encoded, Cro superfamily [Transcription]
LEKAIEALGSQSALARALGVSQQAVSQWLNGKRRVPAERCLAIERATGGAVTREELRPDLDWAYLWPE
>gnl|CDD|443352 COG4198, COG4198, Uncharacterized conserved protein, DUF1015 family [Function unknown]
MAEIKPFRALRPNPEKAAEVAAPPYDVISSEEARALAAGNPYSFLHLILPEIDLPTDPYGENVYAKAAEN
LEEWIEEGVLVQDEEPAYYIYEQTMGGRTQTGLVAAVSVEDYENGVIKKHELTRPDKEEDRLRLLRATGA
NTGPVFLLYRDNEEIDALLDEVKKNEPLYDFTDEDGVRHRLWVIDDPEVIAQITEAFAADPALYIADGHH
RYASALRYAAERREKNPDHTGDEEYNYFLMVLFPDPQLKILPYNRVVKDLNGLSPEEFLEKLEEYFEVEE
LGDEPYKPSKKHEFGMYLDGKWYLLTLKPETYDKPDPVRRLDVSILQDLILEPILGIDDPRTDKRIDFVG
GIRGLEELKRRVDSGEYAVAFSLYPTSIEQLMAVADAGLVMPPKSTWFEPKLRSGLVIHELD
>gnl|CDD|443353 COG4199, RecJ, ssDNA-specific exonuclease RecJ [Replication, recombination and repair]
KTKWKIKKEKDEKKEEKEESELLLSLLVLLLLLLRGLLETEEAAEELELHELFLHDDLLLLMMLMAVARE
RIAIIEEAIIIIEGDDDDDGDDTTSVVSTTLLLLGALLDYYIPNRFRFGGGPGEAGPAEAAAGGAGLIII
VTVIIAVNGVIAAAEEKGLDIIIDDHHHPEHEEPLADAIAPPPPPPPPPPFGELAGGGVAAAVAAALLLG
LPLLLLLLLALLTAAADLVLLLENRRLLRRLLLLKLLSTERLGLLLLKAALLLASIIEEEEEGFGGGPIL
NAAARLGRAAAAVALLLLLDEEEEEEAAELAEAQNEERQEIVKIIEAEAIEEEEEAEEKDDNVVVVVAEG
GWNGGVGVVVSVVVVKYRRPPLILLIDDEEKGKAGGGSSSISFFLFLLELSLERLLLLFGGGGGAAAAAL
LLEDVEDLLRLLLELAALLELLEEDLPPELIDDLLLISDEIIIIIIEEELLLPPGGGPPPPPKFVLLEIA
INKRRIGGANKHLKKLLTGEGELLDAGGFFGGGLLEEELPDTIIVVVGGLSINEWNNRRKPQLMIQDIAV
NEWQLFDYRGKRDAEKWLPILPKEKTVFVAFHEETIKKFQSYIYYEEIVLVDDEEGEEDDLDVKYLVLLD
LPDSLEQLEELLETLQPERIYALFYQEESHYFSGMPTREQFKWLYKFLKKRKQFDLRKHGPQLAKHKGWS
KETLKFMTKVFFELGFVTIEDGVISINENPEKRDLTESPTYQLRQEQIELEKKLLYSSYSELKQWFESQM
EESS
>gnl|CDD|443354 COG4200, EfiE, Predicted lantabiotic-exporting membrane pepmease, EfiE/EfiG/ABC2 family [Defense mechanisms]
MMLRLLRAELLKLKRSLIWLLVLLLPLLSALLGLFNYLLNYEILQPYNDGDGWLSLWTQSFLFWSFFFLP
LLIALLASLLARLEHKNGNWKQLLTLPVSRAKLYLAKLLVVALLLLLSQLLFFVLYLLSGLLLGLSGSIP
WGELLKWLLLGWLASLPLIALQLWLSLRFRSFAAPVGIGIVGTIAGLLASVTGSGLGYYYPWSLPVLGMR
SNGLGDLSSVSLVLFLLVSLLYFVLFLILGILWFKRRDVR
>gnl|CDD|443355 COG4206, BtuB, Outer membrane cobalamin receptor protein BtuB [Coenzyme transport and metabolism]
VVVTATRLEQSKSDLTGSVTVIDAEELERSGATSLADALRRVPGVQVSSSGGPGSAASISIRGLGSNQTL
VLIDGVPLNDPSLGGVDLSLIPPDDIERIEVLKGAASALYGSDAIGGVINITTKKGKKGFKGSVSASYGS
FGTRRLSASLSGGAGKFSYSLSASYRRSDGYRYNDPDLRNNDGYENTSLNARLGYKLGDNGSLSLSGGYS
DSERGYPGAVGSDRNLRLSLSLEYKLSDGWSLLLLAYYYYDRDYEDGGGDSAGTSNTDGARAGLSY
>gnl|CDD|443356 COG4208, CysW, ABC-type sulfate transport system, permease component [Inorganic ion transport and metabolism]
MSSAARARSATTEPPWVRWLLIGLALLFLALFLVLPLAAVFAEAFSKGWGAYLAALTDPDALSAIRLTLL
VAAIAVPLNLVFGVAAAWAITRFEFRGKRLLITLIDLPFSVSPVVAGLIYVLLFGAQGWFGPWLEAHDIK
IIFAVPGIVLATIFVTFPFVARELIPLMQEQGTDEEEAALTLGASGWQTFWRVTLPNIKWGLLYGVILCN
ARAMGEFGAVSVVSGHIRGETNTLPLHVEILYNEYNFVAAFAVASLLALLALVTLVLKTLLEWRTARRLA
A
>gnl|CDD|443357 COG4209, LplB, ABC-type polysaccharide transport system, permease component [Carbohydrate transport and metabolism]
MSTTAAKAKRKKKKRKKSFLKRLKRDWQLYLMLLPGLIYLLIFSYLPMYGIVIAFKDYNPFKGIFGSPWV
GLKNFKFLFSSPDFWRVLRNTLLISLLKLVFGFPLPIILALLLNELRSKRFKKTVQTISYLPHFLSWVVV
AGIVYQFLSPDTGLVNQLLRALGGEPINFLTEPKYFRPIYVFSGIWKEAGWGSIIYLAAITGIDPELYEA
AAIDGAGRWQQIWHITLPGIRPTIVILLILNIGNILNVGFEQIYLLYNPLNYSTSDVIDTYVYRIGLQNG
DYSYATAVGLFKSVVGLILVLIANKIAKKLGEESLF
>gnl|CDD|443358 COG4211, MglC, ABC-type glucose/galactose transport system, permease component [Carbohydrate transport and metabolism]
EKKIKKKKIKNFLLNNAIYIVLLLLIIAIIIINPNFLSLRNIRNILTQSSTRMIIALGVAGLIVTQGTDL
SAGRMVGLAAVISASLLQSGDYAGKFFPNLPELPIIVPILIAIAIGALFGLINGFFVAKLKVPPFIATLG
TMLIVYGINSIYTDRPGAQPIGGLDESFTNFAQGSINIGGFGIPYLIIYAIIVIVIMWFIWNKTKFGKNM
YAVGGNPEAAEVSGVNVFKTLIIVYALAGALYGFAGFLEAARTGSATNNYGNGYELDAIAACVVGGVSFS
GGIGKISGVVIGVLIFTVINYGLTFIGVNPYWQYIIKGLIIIAAVALDIRKYLKKK
>gnl|CDD|443359 COG4213, XylF, ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism]
GKIKIGVSLPTKTSERWIRDGDNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGT
ALAAVLEKAKAAGIPVIAYDRLILNSDVDYYVSFDNVKVGELQGQYLVDGLPLKGKGNIELFGGSPTDNN
ATLFFEGAMSVLQPYIDSGKLVVVSGQWTLGWDPETAQKRMENLLTANGNKVDAVLAPNDGLAGGIIQAL
KAQGLAGKVVVTGQDAELAAVQRILAGTQYMTVYKDTRELAEAAAELAVALAKGEKPEVNGTYDNGKKDV
PSYLLEPVAVTKDNVKETLIDSGYYTAEQV
>gnl|CDD|443360 COG4214, XylH, ABC-type xylose transport system, permease component [Carbohydrate transport and metabolism]
MSTTAAPGGAVRSLRRLLGGDLRSLGMIIALVVIWIVFQILTGGTFLTPRNLSNLLLQNSYIGILAIGMV
LVILLGHIDLSVGSVSGFVGAVAAVLMVNWGLPWWLAILAALLVGALIGAWQGFWVAYVGIPSFIVTLAG
MLAFRGLTLLVLGGGTIAPFDPTFQAIGNGFLPDILGTLSWVLGAVAVAAYVALQLRSRRRRRRYGLPVE
PLWLFVLKLALLAVLILGAVYLLNSYRGIPIVVLILLVLVVVYTFVLTRTVFGRHIYAVGGNPEAARLSG
INVRRVTFSVFVNMGVLAALAGIVFAARLNSATPSAGTGFELDAIAAAVIGGTSLFGGVGTVYGAVIGAL
VMGSLNNGMSLLGVDSDWQQIVKGLVLLLAVAFDVLSRRRRGA
>gnl|CDD|443361 COG4215, ArtQ, ABC-type arginine transport system, permease component [Amino acid transport and metabolism]
MSMLTLLMFGLQGWGPALLAGALVTLELALLSLLLGLVLGLLGALAKLSGNRPLRWLATGYTTVVRGVPD
LLLILLLYFGGQILLNALADLFGYDGFIEINPFVAGVLALGFVFGAYATEVFRGAFLAVPKGQIEAARAY
GMSRWQVFRRILLPQMWRYALPGLGNNWLVLLKDTALVSVIGLVDLVRQAQEAAGSTREPFTFYLAAALI
YLALTTVSELVLARLERRASRGVRRAAG
>gnl|CDD|443362 COG4218, MtrF, Tetrahydromethanopterin S-methyltransferase, subunit F [Coenzyme transport and metabolism]
MAEEGVPTSNKPNMGAIDSVVEDIRYRAQLIARNQKLDSGVMATGIIGFAIGFLFALLLVVLPVLIMG
>gnl|CDD|443363 COG4219, MecR1, Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms]
WLAGVLLLLLRLLISLLRLRRLLRRARPVTDEELLELLERLARRLGIRRPVRLLESDRITSPFSFGLLRP
VILLPAGLEELSEEELEAILAHELAHIRRRDLLDNLLAELLLALFWFNPLVWLARRRLRLDRELACDAAV
LKAGGDRKAYAETLLKLAERRSQPALALAFGGSKSTLKKRIKMLLKSKSKRRSRLKLLLALLLALLLALA
LLSAPEAAAEPEEAAAAAALEAASAAASEAALALAEAAAVAAKVASVEDAEALIAEALAKDKEEKTAEAA
VKASSEADVEEEAAVELDAAEKAAAAAAAGLSAGAGEEGSGVADEAEAAIEAEELAK
>gnl|CDD|443364 COG4220, Nu1, Phage DNA packaging protein, Nu1 subunit of terminase [Mobilome: prophages, transposons]
MAEKLGKEVNKAELAELFGVSDRTIDQWARRGIPVVSRRGRYDLAAVVRWYIERLREKAAGRGSDDQVAD
LDAERARLARAQADKAELKNAVMRGELVPAEEVERALSRVAREVRANLLAVPSRLARRLPHLTAADIDVL
DREIRKALNELADYDDKLPADLDEYDRADD
>gnl|CDD|443365 COG4221, YdfG, NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]. NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation
MSDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAV
AAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIA
GLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPL
TPEDVAEAVLFALTQPAHVNVNELVLRPTA
>gnl|CDD|443366 COG4222, COG4222, Uncharacterized conserved protein, contains a phytase-like domain [Function unknown]
MKKLLLAAALLALLAAQAAAAVSLTLLGEAVLPAGTADFQGTPVGGLSGIDYDPADGTFYAISDDGSGAN
SPDYTLRFYTLRIDLDGGIGKVEVTGTTFLKDPDGVPFPGLPEGRYLTGADLDPEGIRVDPDGTFWISSE
FGPFIREFDADGKLLRELPPPGKFLGLPDAPEAGRRNNRGFEGLALSPDGKTLYAALESPLIQDGPKATA
DGGSPLRILEFDLATGKTGAQYAYPLDPIPPGKFADNGIGDILALDDTRFLVLERDFGEGPGNFKRIYKV
DLSGATDVSGIDSLKGAGITPVRKTLLLDLADLGLPFDNIEGMALGPRLDGDRTLVVVNDNNFPFSGQDT
QFLLLELKKA
>gnl|CDD|443367 COG4223, COG4223, Uncharacterized conserved protein [Function unknown]
EIAALEAAVAELPAQLTALEQRLAALEAAPAAAAATAALEARLAALRAALAAAREAVAAAAAAALEARLA
ALEAKAAAPEAEAAAAARAAALALAAAALRAAVERGQPFAAELAALEALAPDAPALAALAAFAATGVPTL
AALRAEFPAAARAALAAARAPEADASWLDRLLAFARSLVTVRRVGPVEGDDPDAILARAEAALAAGDLAG
ALAELEALPEAAQAAAAPWIAKAEARLAADAALQALAAQALAALGGAGQ
>gnl|CDD|443368 COG4224, YnzC, Uncharacterized conserved protein YnzC, UPF0291/DUF896 family [Function unknown]
MLMKEKIDRINELAKKAKEEGLTEEEKKEQKKLRQEYLKNFRGSFRNQLENIKVVDPEGNDVTPEKLKEI
QRKKG
>gnl|CDD|443369 COG4225, YesR, Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism]
VADSQLKRYWDIDPGKFPKWDYTQGVTLYGLLKLAEATGDKKYLDYIKRWFDFFIDEGNTYKLPPYNLDD
IAPGLALLELYEQTGDPKYLKAADTLADWQLNTQPRTSEGGFWHKKIYPNQLWLDGLYMAVPFLAQYGKL
TGDPKYFDDAAKQFLLTTKYLFDPETGLYYHGWDESREQKAGGSPAFWGRGNGWVAMALVDLLDLLPEDH
PDRPELLALLKEMAAALAKYQDESGLWHQVLDDPGNYLETSATAMFTYALAKGVNKGYLDKKYLPAAEKA
WNGLLKKIDEDGSLTGVCVGTGLGGSLEYYISEPIRTNDPYGVGPFLLAGSEMLKL
>gnl|CDD|443370 COG4226, HicB, Predicted nuclease of the RNAse H fold, HicB family [General function prediction only]
NMMTYKGYTASVEYSPEDGEFVGKVLGIPDLISFEGESVEELEKAFREAVDDYLEDCKELGEEPEKPYSG
KFNVRIPPELHRALAIAAAEEGVSLNQWVVEALSEALAHE
>gnl|CDD|443371 COG4227, ArdC, Antirestriction protein ArdC [Replication, recombination and repair]
MAAAKPRKDIYQEVTDRIIAALEAGTLPWRKPWNSSGAGLGLPLNAATGRPYRGINVLLLWMAAEERGYT
SPRWLTFKQAKELGGQVRKGEKGTLVVYYKRFEKEDEDEEDEEGEEVERRIPFLKAYTVFNAEQIDGLPE
EYYPLPEPLPESERIERAEAFIAATGADIRHGGDRAFYSPSTDRIQMPPREQFKDAEDYYATLLHELGHW
TGHKSRLNRDLGGRFGSEAYAFEELVAELGSAFLCAELGIAPEPRENHAAYIASWLKVLKEDKRAIFRAA
SKAQKAADYLLGLQPEAAEEEAA
>gnl|CDD|443372 COG4228, COG4228, Mu-like prophage DNA circulation protein [Mobilome: prophages, transposons]
MSSWRDKLQPASFRGVPFDVESADDSGGRRVAVHEYPYRDGPDVEDLGRKAREIRITAVVIGDDYLAQRD
ALLDALEQPGPGELVHPYFGSLQVQVGEYSVRHSAEEGGYATFDLTFVEAGEGAFPAALPDTQDALLAAA
DAALDAAGADFAAAFSVLAVADGALADVLALAGALSGLVGALSRLAGPAAGLKSSLTDLLAAPAALAAAL
TGLVDGLASLASSPADAIGALRSLSAGLSSDWDGNPAASPVPTPSATPSRPAAAQNQAAVAALVRRAALA
ELARAAAELLEAETETQVLSPDDAQAVRDALQAALDAERADAADAGDDAVYEALRDLRLALLQDLAARAA
ALPPLVTRTVPATLPALVLAHRLYGDAARADELVRRNGIRHPGFVPGGDLLEVLAR
>gnl|CDD|443373 COG4229, Utr4, Enolase-phosphatase E1 involved in merthionine salvage [Amino acid transport and metabolism]
MMIRAILTDIEGTTSSISFVHDVLFPYARERLPAFLREHAEDPEVAAALAAVRAEAGEPDADLEELIAVL
LRWIDEDRKATPLKALQGLIWEEGYEAGDLKGHVYPDVAPALRAWHAQGLRLYVYSSGSVAAQKLLFGHS
DAGDLTPLFSGYFDTRIGPKREAASYRNIAEALGLPPEEILFLSDVVEELDAAREAGLQTCQLVRPGDPT
DDPGGHPVVASFDEIEL
>gnl|CDD|443374 COG4230, PutA2, Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]
APFALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGL
LLLLELSSLSSEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLL
TALESSLSLASGLLRLLGRLGRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGE
AAAAAADAAAYAYAYAAAAAAAIAAAGGGSGGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLAL
LALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGGGGGVGQAVQAYAKALLLVLDLLARRRRRRR
RRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLAAQPAFAPQFATHAAATAAAA
AAAGGGGEFEFQCLHGMGEYLYDQVGRGKLGRPCRIYAPVGSHEDLLAYLVRRLLENGANSSFVNRIADE
DVPVEELIADPVEKARALGGAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSAALAAAAEKQWQAAP
LIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEA
HRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTVLRGRGVFVCISPWNFPLAIFTGQ
VAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTE
TARLINRTLAARDGPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIAD
RVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTL
IEIDSISDLEREVFGPVLHVVRYKADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNR
NIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVTVNTTAAGGNASLLALGDWLASLLGALTLPG
PTGERNTLTLRPRGRVLCLADSLEALLAQLAAALATGNRAVVAADLALAGLPAVLLPPFDAVLFEGRLRA
LRQALAARDGAIVPVIDAGYDLERLLEEAGGNASLM
>gnl|CDD|443375 COG4231, IorA, TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion]
RNITVKILDNRTTAMRYVIDEDKCTGCGACVKVCPADAIEEGDGKAVIDPDLCIGCGSCVQVCPVDAIKL
EKRVPE
>gnl|CDD|443376 COG4232, DsbD, Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones]
PAALILLLAFLGGLLLNLTPCVLPMLPIKSSIIVGQGGKSRRRAFLLSLAYVLGMALTYTLLGLLAALLG
GAVGWGFQLQSPWVLGALALLFVLLALSMFGLFELQLPSSLQNRLAALSNGGGLLGAFFMGVLAALVATP
CTAPFLGGALGYALQTGDALLGLLALFALGLGMALPLLLLGLFPGLLKLLPKPGAWMETVKQVFGFLLLA
TAIWLLSVLLPQAGLDAVALLLWALLLLALALWLLGALRLPHDSSGRRLSVRKGLGLLLLLAGLALLLGA
LSGADPLQPLAAGAAAAAAAAGLAWQADLEAALAEARAEGKPVFVDFTADWCVTCKENERTVFSDPEVQA
ALADDVVLLKADVTDNDPEITALLKRFGRFGVPTYVFYDPDGEELPRLGFMLTADEFLAALEKAKG
>gnl|CDD|443377 COG4233, COG4233, Thiol-disulfide interchange protein, contains DsbC and DsbD domains [Posttranslational modification, protein turnover, chaperones, Energy production and conversion]
MRRRRLLAALLALALAAAAAAAAAASAWVTSPHVEVRLVAGGDAVAPGGTLRAGLRLRLAPGWHTYWRNP
GDAGIPPSFDWSLSEGVAAGEIQWPAPKRFPDGGLTNYGYEGEVVLPVELTLPDPGGPVTLRAKVDWLVC
EDICVPEEAELSLDLPVGAATDAAAAALFAAALAAVPVPAPAAAVDVRAAVDPIDGGRLTLRLTLPAGGA
SDPDFFPEGPGGIDFAAPQTLRRDGGRLTLTLPLSGGPKAAPGSPLRLTVLDGGRAVEISLCAAAAAAAA
LAAAALAGLLALALALLLLLLLLLLALLLLLLLLLLLALLLLLLLSLLLLLAAGALLAALLLALAAGLAL
GGAALGGLLLGLLALGLLAAALFALLLLGLLLLLLALLLGLLLLLLLLGLLGGLALGGGFAGGLAALAGA
AAGAAAAAAAALAAAAAAAAAAAAAAGALLAALLALAALLLLALLLLALLLLLLALLLLLLPLLLAPLLL
LLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLALLALLLLLLLVGLLLLLAGLAALLAAAAAAAALALAL
LLAALVLAAAAAAAAALAASAAALAVAAAAAAAAAAVAAVVAVVAAAAALVVAAVAAAVAAATVVVAAAA
AALVAVVVAAVVTRAVADGAALPRVGRVGLAPLLLGPRAGVLLPLPPPLLL
>gnl|CDD|443378 COG4235, NrfG, Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEA
EELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARLLEASIAEA
>gnl|CDD|443379 COG4237, HyfE, Hydrogenase-4 membrane subunit HyfE [Energy production and conversion]
MLGTQLINLLAGLLLLTSFLMLAQRRLKALIRLYALQSLLLALLAALLGYTTGAPELYIIALLTLVLKVI
LIPWLLLRAIRKLGIRREVEPLLGPPLSLLIGAALVALSYFVALPIVLLAESLTRLALAVALAVVLIGLL
LMVTRRKAISQVVGFLVMENGLFLAALLLTYGMPLIVELGILLDVLVAVLIMGILAFRIRETFDSLDTDR
LERLKG
>gnl|CDD|443380 COG4238, Lpp, Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis]
MNRKLLLGAAILSSLLLAGCSNNSKIDQLSSDVQSLNAKVDQLSNDVSALRADVQAAKEEAARANQRLDN
QATSYKK
>gnl|CDD|443381 COG4239, YejE, ABC-type microcin C transport system, permease component YejE [Secondary metabolites biosynthesis, transport and catabolism]
MMRLSPLNRRRWRRFKANRRGYWSLWIFLVLFVLSLFAELIANDKPLLVSYDGELYFPVLKDYPETTFGG
DFETEADYRDPFVQELIEAKGWALWPPIPYSYDTINYDLPSPAPSPPSAENWLGTDDQGRDVLARLIYGF
RISVLFGLALTVISSVIGVAAGAVQGYFGGRVDLLFQRFIEIWSSMPELYLLIILSSIFQPSFWLLLGIL
LLFGWMGLVGVVRAEFLRARNLEYVRAARALGVSDRRIMFRHILPNAMVATLTFLPFILSGAITTLTSLD
FLGFGLPPGSPSLGELLAQGKNNLQAPWLGLSAFVVLALMLSLLVFIGEAVRDAFDPRKTFR
>gnl|CDD|443382 COG4240, Tda10, Pantothenate kinase-related protein Tda10 (topoisomerase I damage affected protein) [General function prediction only]
MSTSVYPAIRQFCQQHQLPEDFLETLWRLWLPLAEQLADHRQQLGRPLIVGINGGQGSGKSTLAAFLALI
LEQLGLRVAVLSIDDLYLTRAERQALAEQVHPLLITRGVPGTHDVELGLQVLDQLRAGKPGQPVSLPRFD
KSADDRAPDRQWPEIVGPVDIVLFEGWCVGARPQDEAALAQPVNPLEAEEDPDGVWRRYVNQQLAGDYLP
LWERLDRLIMLKAPDFRLVYQWRLEQEQKLIARGDGKGGMSDAQIERFVQHYQRLTHPALFILPARADLV
VELDADHRITAVYLPQSS
>gnl|CDD|443383 COG4241, YybS, Uncharacterized conserved protein YybS, DUF2232 family [Function unknown]
MPMNKTRALTEGALLAAIAVVLLLISVYVPVLGLILLFLLPLPIIVLGVRHGLKSGLLALVVALILTFLF
IGPLFALPLALLFGILGVVLGYLIKKKKSAFETLLAGTLAFLISTVILFLLSQLLFGINPFDELINAMKE
SFNEAIELYESMGMSEEQLEQMREQLEEMIELLKLLLPAILIIASFLLAFINYLVARKILKRLGYKVPKF
PPFREWRLPRSVLWIYIIVLLLLLFGDPEEISLLYIIGLNLLVILSFLFLLQGLSFIFYYLKKKKLPKFV
RILIVILLILLPLLLYLVRILGIIDLGFDLRKRIKKKK
>gnl|CDD|443384 COG4242, CphB, Cyanophycinase and related exopeptidases [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]
MKRLFAAADAPTKPKGALLIIGGGEDKDEILRRFVELAGGKDARIVVIPTASSEPEEVGERYRRAFERLG
AKSVEVLDIDSREDANDPEVVERLREATGVFFTGGDQLRLTDLLGGTPLLEAIRDRYARGGVIAGTSAGA
AIMSETMIAGGTSGEALRKGNVDLAPGLGFLPGVIIDQHFAQRGRLGRLLSAVARNPDLLGIGIDEDTAI
VVDPDGTAEVIGSGAVTVVDGSEATEEAKPGEPLSLSNLRLHVLSAGDRFDLKTRKVVPSEGKLPS
>gnl|CDD|443385 COG4243, COG4243, Vitamin K epoxide reductase (VKOR) family protein, predicted involvement in disulfide bond formation [General function prediction only]
MTSTRRRSRWLAWLLLVLALIGLLASFYLTLEKLTLLAPGGVLSCDINPVVSCGSVLNSPQASVFGFPNA
LLGLAAFAVVITLAVALLAGARLPRWLWLALLAGALAGVVFSVWLIYQSLFVIGALCPYCLVVWAVTIPL
FVLTTLGNLRRGWLDLGRLAV
>gnl|CDD|443386 COG4244, COG4244, Uncharacterized membrane protein [Function unknown]
MQLSLPLESRGLPLGHPLHPLLVHFPIALLLLALLFDLAGLLTGDPFLARAAFWLLLAGALGAVLAALAG
LLDLLAVPGGYRARRTLWLHGLLGVALLALAAANLLLRLGDRKRAQVSPLGLALSLLGVLLVGVTGWLGG
ELVYRHGVGVAPLPELERE
>gnl|CDD|443387 COG4245, TerY, Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown]
NPMRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALETVEVSVITFDGEAKVLLPLTDLEDF
QPPDLSASGGTPLGAALELLLDLIERRVQKYTAEGKGDWRPVVFLITDGEPTDSDWEAALQRLKDGEAAK
KANIFAIGVGPDADTEVLKQLTDPVRALDALDGLDFREFFKWLSASVSSVSRSVGP
>gnl|CDD|443388 COG4246, COG4246, Uncharacterized conserved protein, contains a phytase-like domain [Function unknown]
MRRRFRLALAAAGLALAALAPAAAAAPAAPAAPEPIAVSARPIAAFRPRDAATRFGALEFLGGLVLTSDD
PRFGGLSGLRLSPDGTRFLAVSDRGTWLTGRIVRDGDGRLTGLADVRIAPLLDSDGRPLARKGRADSEGL
ALDPGGTAYVSFERVHRILRYPLGPDGPGAPARPLPVPPAFRKLPSNGGLEALAILPDGSPLAGRLLAIA
ERSLDDDGNLPAWILGGPWPGAFTVPRSGGFDPTDAAFLPDGDLLLLERRFSLLDGFGMRLRRIALADIR
PGAVVDGEVLLEADMGYQIDNMEGLAVWRDADGETRLTLVSDDNFSFLQRTLLLEFRLPD
>gnl|CDD|443389 COG4247, Phy, 3-phytase (myo-inositol-hexaphosphate 3-phosphohydrolase) [Lipid transport and metabolism]
MKKLLTLLALALLLLAACAASAQPAPLPAVTATVETEPVAGGGDAADDPAIWVNPADPAKSLVLGTDKKG
GLYVYDLDGKILQFLPVGRPNNVDVRYGFKLGGKTVDLAVASDRTNNKLRLFRIDPDTGPLTDLGGIPTG
LREPYGLCLYKSPKDGKLYAFVNRKDGRVAQYRLVDDGGGKVTATLVRTFGLPSQPEGCVVDDETGYLYV
GEEDVGIWKYDADPDAGKGGELIAAVGGGGLVADVEGLAIYYGGDGTGYLLASSQGDNTFAVYDREGPNA
YVGSFRIGADGGIDGVSETDGLDVTSVPLGPGFPNGLFVVQDGRNRPPNQNFKLVDWEDIAAALGLPL
>gnl|CDD|443390 COG4248, YegI, Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding domains [General function prediction only]
MTVLRLTDSDGEPITLGDELGRGGEGDVYFLPDRPGYVAKIYHKPTDEARAEKLRVMVAHPPEDPFAEYG
HISIAWPTDLLEGANGGIVGFLMPRIKGARPLHKFYSPKTRRQQFPLFDWLFLLRTARNLAAAVAALHAA
GYVHGDVNPSNILVSDTALVTLIDTDSFQVRDPGKVYRCVVGTPEFTPPELQGKSFARVDRTEEHDRFGL
AVLIFQLLMEGRHPFSGVYQGDGDDPTLEERIAMGHFVYHPNRRVLIRPPPRAIPYEILHPYLQELFERA
FIDGHHNPQLRPSAKEWEAALAEAEDLLQPCATNPQHWYSNHLPSCPWCGRSRRGGGRDPFPSIQAIAAL
PRPPPPPRPRPPLPVLNLYSGRVPGAFKPDNHRLMVYSGQALADWHGARKINPNEALTYLKRGPVGYFLA
QYGKWWLVNEQLPAMIDLQTSAAIALGAKVELLEGQQILLSCGEGGRLLVVQMQSL
>gnl|CDD|443391 COG4249, COG4249, Uncharacterized conserved protein, contains caspase domain [General function prediction only]
AAAAAAAEKRVALVIGNSAYQDLPPLPNAVNDAEALAEALREAGFDEVILLTDATRAEIRRALRDFFAKA
QPGDVALFYFAGHGIQDDGENYLLPVDASPDDLESTAISLSELLDALAESPAKKVLVILDACRSGPFARG
GRRSAGPSSSRGLAELAAGRGTLVLTASAPGQVALEGPEGGHGVFTYALLEGLRGPADGDGGITLEELFK
YVRRRVRELTGGKQTPWFISSLGGDFVL
>gnl|CDD|443392 COG4250, DICT, DICT sensory domain found in diguanylate cyclases and two-component systems [Signal transduction mechanisms]
MRISGSILQELLDALPETRFTVYFKSSLVALSRAIEDRALRVDGKGLLIAGFQRESFYRQEADRYRRLAD
RSLQVHVYAAPDTEFPDHDNVTVHALEPADELAQEWFLVIDGPDYKAALLAEERSPGLPEMDQERRFYGF
WTFDPELVDEAADLLLDRIGSYRPELAAKLEQADPFVS
>gnl|CDD|443393 COG4251, COG4251, Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms]
LLLLALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLL
LLLVLAALALLLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEEL
ALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELL
LLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTAELERSNE
ELEQFAYVASHDLREPLRKISGFSQLLEEDYGDKLDEEGREYLERIRDAAERMQALIDDLLAYSRVGRQE
LEFEPVDLNELLEEVLEDLEPRIEERGAEIEVGPLPTVRGDPTLLRQVFQNLISNAIKYSRPGEPPRIEI
GAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGE
GATFYFTLPKAPA
>gnl|CDD|443394 COG4252, CHASE2, Extracytoplasmic sensor domain CHASE2 (specificity unknown) [Signal transduction mechanisms]
LLALLLLLLLVLLLRLLGLLQRLELAAYDLLFRLRPPEPPDPRIVIVAIDEASLAELGRWPWPRAVLAQL
LDKLAAAGPRAIGLDILFDEPDRPDGDAALAEALARAGNVVLGAKFSSGDEEGELEGGVAPPPELAAAAA
GVGFVNVVPDPDGVVRRVPLLVRYGGQTYPSLALALARVYLGAEGIELKLTPEALRLGDLVIPLDAGGYI
LLNYRGPPGTFPTVSAADVLDGRVPPDLFKGKIVLIGATAPGLGDLFPTPFSGQRMPGVEIHANAISQLL
SGRLLRRPPWWVELLWILLWGLLGALLLWRLRPLRLLLALLALLAALLGISYLLFLYQGLWLPLVPPLLA
LLLAYLLVTAYRALLRERRRLRRRRRRRLSLLLLLLLLLLLLLLLLLGGLGGEEELLLLLLLDLSFFTTL
SEELAPLLLLLLLLLLLLLLLAIIIGGGGGDGDGDGDAAVAAAGALPAEAAAAAAAAAAAAAALLRLLLL
AELAAAELGLGIGGGGGGGGGGGGGGGGGGGGRGAGVGAAVDLVALAEGLELLKLLTILISLIEALTAAL
LLARLPLLLLLLVVVKGKVRLIELLLLLLADAAEALAALLALAAAAAL
>gnl|CDD|443395 COG4253, COG4253, Uncharacterized conserved protein, DUF2345 family [Function unknown]
LLLLLLALSLLLLLLLLLLLALLLLRLLLLLLLLALLLLALLRLALLLGLLVLRLLLLALLLGLLLLLLD
LLLLVLLSAALLLLSVLRSELRLALLLLDLLALTLLAAALLVLLALLLSLAGLPQRRQLSALALALVLAV
LSRLQAFSRRALDELLALLLLRLRRRRALLRLRLADAALVRSTVEELLSRRHGDEVAFADDRLTERRASA
EAASRADAAALRDLRLALRLARRAATAADDAQTTDDARLTADDSAADAGSLSGSGGDGGAAGGSLAEATS
SLRVPAASVSLARYQRARRAAAAAAAADARAGGADAAGGVGTGGGRRLAAGLAGAAAEEEEAVGAEARAR
RRRLLRAARAAIRLLAAAALALLALGRGALAGRSPAAAAGPGIVGGTDRRARRRATAFVDRAAGPPPRTQ
RARRPLLPRPRGAGGPPPRVVSTRAGDTPSADDDDGGRRVVRDDRRVAWVGGGESWGAGGGAGAGGGVGG
GVVPLLGDGDVVIAAEGGGPPAPGGGAPAAHSAAHLDHSSGALSGGNSRNTGGNGLNLLDDDDDEGQQRS
ATQSGKTQLLLLLLVLLQQQRRGRGGERRGGFELATDAGGALRAAAGLLLSATGQRNAQGTQLDMAEALA
QLEQALELAKSLSDAAAQAQALLLDTAEALKALLDALKGWEAAQGAGLGGTLPALSQPVLLLSAPAGIAL
TTPQSTQLSAGENLALTAGQDTNIAAGKSLTVAAGEGISLFAQKGGIKLIAAKGKVEIQAQSDALELLAK
KDVTITSTAGRITITAKKEILLTAGGAYIRIEGGNIELGTPGKITVKAASHSFTGPASASAALPSLPKGA
LDEQFVLRHDATGEPLANQPYRITLADGSVVEGVTDAQGKTELLGTPAPESVKIELLEDE
>gnl|CDD|443396 COG4254, COG4254, Uncharacterized peptidoglycan binding protein, contains LysM and FecR domains [General function prediction only]
MKKLRGDTLLALAALLLALAALNALAAAAAAARVVAVSGEVTAVRADGKWRPLKVGDPLFEGDRIRTGAN
SRAQLRFADGSRLRLGPNSELRIDELRYDPGTGSGDTVLELLKGAVRSIVGKIGKGGSRFEVRTPTAVAG
VRGTEFRVSVDGDGQTRVEVLEGAVAVSNAAGQVVTVPAGQGTVASAGGAPVALLPAPALARLAGID
>gnl|CDD|443397 COG4255, COG4255, Uncharacterized conserved protein [Function unknown]
MMHLHLLLPGLLPPAAAARELLRGLALPALARLLARADRTRFAPSLPHEAWLARLFGLPGADGDLPVAAL
TALADGGDAGGGAWLRADPVHLRPDRDHLVLLDPGQLALSEAEARALLAALNPLFAEDGLQLEAPTPDRW
YLRLPAPPDLATAPLDRVLGRDIDIWLPRGPDARRWRRLLNEVQMLLHTHPVNQAREARGLPPVNSLWLW
GGGALPAAAQSPLARVWSDDPLLRGLARAAGVPAQPLPASFAALLAAEGDALVVLDALRAPALYGDWAAW
REALQALEADWFAPLLAALRRGRLDSLTLTGERSGRTFTLTRRDLWRFWRRPRPLAALL
>gnl|CDD|443398 COG4256, HemP, Hemin uptake protein HemP [Coenzyme transport and metabolism]
NASAAATSTPAAAPAAAAAPAPPRIDSRELLGGGREVRIEHNGQRYRLRITRNGKLILTK
>gnl|CDD|443399 COG4257, Vgb, Streptogramin lyase [Defense mechanisms]
AASAVDITEYPVPAPGSGPRDVAVDPDGAVWFTDQGGGRIGRLDPATGEFTEYPLGGGSGPHGIAVDPDG
NLWFTDNGNNRIGRIDPKTGEITTFALPGGGSNPHGIAFDPDGNLWFTDQGGNRIGRLDPATGEVTEFPL
PTGGAGPYGIAVDPDGNLWVTDFGANAIGRIDPDTGTLTEYALPTPGAGPRGLAVDPDGNLWVADTGSGR
IGRFDPKTGTVTEYPLPGGGARPYGVAVDGDGRVWFAESGANRIVRFDPDTELTEYVLPS
>gnl|CDD|443400 COG4258, COG4258, Predicted exporter [General function prediction only]
MTLSRRRRLLALLLWLLLLLALLALLASRLRFDTDILALLPADETDEQALLADQLREGPLSRQILVLISG
GDPAQLAAAARALAAALRASGLFASVQNGIPADLEALRDFLFPHRYLLLPAADRERLTADGLRAALQDRL
DQLYSPAGGVSKQLLLRDPLGLSRRLLEKLQPLGSRPRLRDGVLVSRDGTWALLLAETRASGFDTDAQQQ
LVAALRAAFAALNAAFPGAQLLLTGAGLFAVAAAQQIKHDISTIGLISLLGILLLLLLVFRSLRPLLLGL
LPVAVGALAGLAAVSLVFGSVHGITLGFGSSLIGVAVDYSLHYLTHRRAAGEWDPRAALRRIWPTLLLGL
LTTVLGYLALLFSPFPGLRQLGVFAAAGLLAAALTTLLWLPLLLPRAAPRPPAPALALLARLLARWPRRL
RWLLALLAVLALASLLGLNRLKWNDDLRALNPVPAALLAQEARLRALLGAPDVSQYLVVYGPDAEQALQR
NEALLPRLDALVAQGAIAGYQSLSRLLPSAATQQARQALLPDLAALRPRLAEALAGLGFRPDAFAPFLAD
LEAARAAPPLTPEDLLASPLAAALRLLLLGRKDGQWAALVPLRGVDDAAALRAAAAGLPGVRLVDRKAES
SSLFGRYRNDALWLLLLALLLILLLLLLRLRSLRRALRVLLPPLLAVLLTLAILGLLGIPLNLFHLIALL
LVLGIGIDYALFFTEGLLDKGELARTLLSILLAALTTLLGFGLLAFSSTPALRSFGLTVLLGILLALLLA
PLLAPRRRPRRAA
>gnl|CDD|443401 COG4259, COG4259, Uncharacterized conserved protein, DUF4810 domain [Function unknown]
MKKSKLLALLLAALLLAGCASPPKPLYYWGNYQDTVYQYYKEPETSPEEQIEALEKDIEKAKAKGKKVPP
GLHAHLGLLYAKTGNDDKAVEQFEAEKALFPESAPFMDFLLKKLKGKKK
>gnl|CDD|443402 COG4260, YdjI, Membrane protease subunit, stomatin/prohibitin family, contains C-terminal Zn-ribbon domain [Posttranslational modification, protein turnover, chaperones]
MGLFGFLKDQFIDVIEWTDDSPDTLVYRFPGYDNEIKNGSKLTVREGQGAIFVNEGKIADVFEPGRYTLD
TSNLPSLTTLKRWKFGFESPFKQEVYFVNTKEITDNKWGTPNPITFRDPEFGAPVRLRAFGTYSYRIVDP
LLFYKEVVGTDGVFTTDEIDEQLRSEIVTALSDALAESGIRYLDLAANTDELAQALNEALAPDFEERGLE
ITSFGIENISLPEEVQKAIDKRSSMAALGDLNAYVQYQAAEAMEAAASNEGGAAGAGMGMGMGMAMGGMM
AQALQQPGQPQQQQPAAAAAAPAQDPGKFCAQLGELLDAGKFCPECGDAKKAELLGW
>gnl|CDD|443403 COG4261, COG4261, Predicted acyltransferase, LPLAT superfamily [General function prediction only]
SAHWAGQKERGSRLGLRLFVWIARRLGRRVARLLLYPVVLYFFLFAPKARRASRAYLRRLLGRSGPPGWR
DVYRHFLAFAQTILDRVALLSGRIDLFDIDVDGEELLRALLAQGRGGILLGAHLGNFEVLRALARRRPGL
KINVLMHTEHAQKINRLLEALNPKSAINIIQVGEDPSTMLELKEALDRGELVAILGDRTPGGEKTVEVDF
LGAPAPFPQGPFLLAALLKVPVYLVFGLKEGGNRYHLYFEPFADFLDLPRKEREAALQELLQRYAARLEH
YCRKAPYQWFNFYDFWQDDE
>gnl|CDD|443404 COG4262, COG4262, Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only]
MSTRPRPKRRLLLLAVFVVGACGLVYELLLGRLASYLLGDSVLQFSIVIGVFLFAMGLGSYLSRRVADRL
LRAFIRLELLLALLGGLSALLLFALFAFLLGALFLLALYLLVLLIGLLIGAEIPLLMRLLERRREELGSA
VGRVYAADYLGALVGSLLFPFLLLPALGLVRTALLFGLLNAAVALVLLWLFRKRLRRKALLAAAALVLAA
LLVGLVFADPIESSAEQKLYGDPVVYSEQTPYQRIVVTRDKDDRRLYLNGNLQFSSLDEYRYHEALVHPP
MAAHPRPRRVLVLGGGDGLAAREVLKYPDVESVTLVDLDPEVTDLAKTNPFLRELNGGALNDPRVTVVNA
DAFQFLRETDEKYDVIIVDLPDPSNFSLGKLYSVEFYRLVRRHLAPGGVLVVQATSPYFAPKAFWCIAKT
LEAAGF
>gnl|CDD|443405 COG4263, NosZ, Nitrous oxide reductase [Inorganic ion transport and metabolism]
KDEKPGLSRRGFLGTAAVAGAGAGLAACKGAGGAAAAAAAALAAAAADAAGKVYVAPGELDEYYGFWSGG
HSGEVRVYGLPSMRELKRIPVFNPDPATGWGYTNESKKVLGTGHDGGGFYPWGDTHHPHLSYTDGTYDGR
YLFINDKANTRVARIRLDTFKTDKIIEIPNVQGNHGLRFQKTPNTEYVFAGGEFSVPLPNDGVPLDDKEK
YRGLFTFVDADTMEVAWQVLVDGNLDNAGKDYSGKWAFSTCYNSEKGNTLLEMSQAERDWIVVFNWKRIE
EAVKAGKFKTIGGSKVPVLDGRKGSGLTYYIPVPKSPHGVNVSPDGKYIVASGKLSPTVTVISFSKIDDA
FAGKVLKPRDAVVAEPELGLGPLHTEFDGKGNAYTTLFLDSQVVKWNIGDAIRAYKGEKVWYVVDKLDVH
YQPGHLHTSMGETKEADGKYLVALNKFSKDRFLPVGPLLPENAQLIDISGDKMKLVHDGPTFGEPHDAII
VHRSKIKPKKVYDRDDPFFPYAVKQAKEAKVIRDGNKVRVYMTSIAPHFGPDEFEVKQGDEVTVHVTNLD
QVEDLTHGFAIPGYNINMEIMPQETASVTFVADKPGVYWYYCTWFCHALHMEMRGRMLVEP
>gnl|CDD|443406 COG4264, IucA, Siderophore synthetase component IucA/IucC/SbnC [Inorganic ion transport and metabolism]
LTLDAWQAANRALLRKLLNELLRERLLAPEPEGELEDDGGGVYRLPLPAGGVEYRFPARRRSAFGRHRFD
PGSIYRTEDGAWRPLDALQLLALLLEELGIDDETLAELLEELLNSLANDALALAHRRLSAADLAAALDFI
ELEQALTEGHPLHPAPKSRIGFSAEDYRRYAPEFGGPFRLHWLAVHRDLARFGSAEGLDYDELLAEELGP
DTLARFAAELAALGLDPDDYVLLPVHPWQWENLLAPLFAAEIARGRLVPLGEGGDEYLPTQSIRTLYNAS
RPSKPYVKLSLSVLNTNSVRGLSPKELERGPAISRWLAELLAQDPYLRDPGFTILREPAGIGYRHPDYEE
GAGYQYREMLGAIWRENPFPLLEPGERAIPMAALLHDDPDGRPLLAALIERSGLREAAEAWFRRYLDVVL
PPLLHLLYRYGIALEAHGQNSVLVLDDGVPVRLLLRDFQGVRLSEPRLPELGEALPDLVERRVLLTVPDE
ELRLRIFYYLFVNNLRELIAALAEHGLLDEERFWRLVREVLEAYQARHPELAERFARFLLFAPTLPRKCL
LRTRLRNNGELDDLAPSLAVYGTLPNPLAA
>gnl|CDD|443407 COG4266, Alc, Allantoicase [Nucleotide transport and metabolism]
DLPDFTRLVDLASRRLGGSVLAANDEFFAEKENLLKPEPPVFIPGKFGDKGKWMDGWETRRRREPGHDWA
IVRLGAPGVIRGVDVDTAHFTGNYPPAASVEACSVEGYPDPEELADAEWTELLPRSPLGGDSHNLFEVAS
ERRWTHVRLNIYPDGGVARLRVYGEPVPDPRLLDAGGLVDLAALENGGRVVACSDMFYGSPSNLLMPGRG
RNMGDGWETRRRRDPGNDWVIVRLAAPGVVERIEVDTAHFKGNAPDRASLQGADAPGGTDASLITQSMFW
FELLPRTKLQPDTRHRFRELAAAGPVTHVRLNIFPDGGVSRLRLFGRLTEA
>gnl|CDD|443408 COG4267, COG4267, Uncharacterized membrane protein [Function unknown]
MAGIGFELRKLLRKDSLLSLLRAYGYAGIISSGPWLLSILGLLLIGILSLSVVVPREERELFQVSVTYLF
AFSLILTGPFQLVFTRYVADRLYEKRYEDILPNLIGALLLTTLLAGLLGLLFVFLLFSELSLLYRLLALA
LFVLLSLIWIAMIFLSALKDYKAIVLSFALGYGVTVLLALLLRPLGLEGLLLGFTLGQFVLLFLLLALIL
RYFPSNRLISFDFLKYFRKYPSLVFTGLFYNLGLWIDKFIFWFGPDTGEVVIGPFRASPIYDLPIFLAYL
TIIPGMAVFLVRVETDFYERYRKYYDAVREGGTLEEIEKARDEMVRVLRQGLFEIFKVQGLITLLILLLG
PTLLPLLGISPLYLPLFRILVVGAGLQVLLLAILNILFYFDDRRGALLLTALFLVLNLVLTLISLKLGPA
FYGYGFALASLLTFLVALIRLRRKLKNLEYETFMLQPIFVKG
>gnl|CDD|443409 COG4268, McrC, 5-methylcytosine-specific restriction endonuclease McrBC, regulatory subunit McrC [Defense mechanisms]
MTKITVFEHQRLRVDDPESAFEALLLEGSRYLRRGRKGLKAGNYVGVIQLGGLTIEILPKIPIRNLLYML
SYAYNLPLRQFGSANLGTEDEDLLDLLAELFLRELERLLRRGLIRDYVRREENLPVLRGRIDVAEQIRRN
LGRRGRLACRYDEFSEDNPENRILKAALRLLLRLTRNSELRRRLRRLLAAFDEVSDLRITRADFSKVRFN
RLNARYRPLLELARLILRNLSPTEEAGDQKLLSLLFDMNRLFERFVAKFLRRALPPGLRVSAQDSSKFLL
DDGGSRLSLRPDIVLRRGGKKTLVIDTKYKLLDLQYDKYGISSADLYQLFAYAKAYGAKRGLLLYPSTEE
EPQPLIVFQFGEGIRLRVVTLDLDAPWSDIREQLDELL
>gnl|CDD|443410 COG4269, YjgN, Uncharacterized membrane protein YjgN, DUF898 family [Function unknown]
MSDTAPAAAPARPHPFRFTGSGGEYFGIWIVNLLLTIVTLGIYSAWAKVRRRRYFYGNTELAGDRFEYHA
TGKEIFIGRLIALVLLVAYYLAGQFSPALGLVLFLLFLLLLPWLIVRSLRFRARRTSWRGVRFGFTGSYG
GAYKVFLLWPLLALLTLGLLLPWATARLRRYLVNNTRFGGARFSFEASGGPFYKIYLLALLLLLLFLAVA
GLLLGAVFAALLESLASAILGAFLLGYLGLYLGYLLAFAYYRARLRNLVWNHTTLGGHRFRSTLSAGRYL
WLLLSNLLLTLFTLGLARPWAKVRLARYRAEHTTVEGDGDLDALVAQAADEGSALGEGLADAFDLDLG
>gnl|CDD|443411 COG4270, COG4270, Uncharacterized membrane protein [Function unknown]
MAMRMWKTALRYLLAALFIFAGVLHFVKPKEFLAIVPPWLPAPRLLVYLSGVAEIALGIGLLIPRTRRAA
GWGLAALLVAVFPANIYMALNGIDAFGLPDWALWIRLPLQPVLIAWALWVTRAA
>gnl|CDD|443412 COG4271, COG4271, Predicted nucleotide-binding protein containing TIR -like domain [General function prediction only]
AAVAEKKRKVFIVHGRDSLVAEALARLLEKLGLEPIIWNEQFNAGRTIIEKLEEASDQVDFAIVLMTPDD
EGRLRGELVGQPRARQNVIFELGLFIGRLGRERVLLLKEGGVELPSDLAGVTYIRFDGGRIGAWKIELAR
ELKAAGIRIDINK
>gnl|CDD|443413 COG4272, COG4272, Uncharacterized membrane protein [Function unknown]
MEDRDIELIIGNLLRIGVLISAAVVLLGGILYLIRGGGEYPDYSVFRGEPSSLRSLGGILSGLLALDGLA
IIQLGLLLLIATPVLRVALSLLAFAKEKDYLYVAITLIVLAILLFSIFLGPAG
>gnl|CDD|443414 COG4273, COG4273, Uncharacterized conserved protein, contains metal-binding DGC domain [Function unknown]
MTEENSKLPLVYSCSGCSNVGQLANQVAVRLDREGPAEMSCLAGVGGGVPGLVKSARSGRPIIAIDGCPL
ACAKKCLERAGVKPDRHIVLTELGIKKRGSLDFDLEEVEKVAEAVKEILKKL
>gnl|CDD|443415 COG4274, COG4274, Uncharacterized conserved protein, contains GYD domain [Function unknown]
MPTYIILGRYTDEGVKNLKESPDRAEAVRKLIEALGGKLKSFYATLGEYDFVVIVEAPDDETAAAAALAL
GAAGNVRTETLRAFPPDEFREALKKLG
>gnl|CDD|443416 COG4275, ChrB1, Chromate resistance protein ChrB1 [Inorganic ion transport and metabolism]
FAIDAAELARLRGLFDRSADYADLLAELDAARATLAALAAAEALRQLRKLRAEFEARRAIDFFPGEAQKQ
AGAAAALLEAALAAALSPGEPHAVAGAIARLDPADYRGMKWVTRERPKVDRIACPWLIRRFIDPEAEFLF
VPPPEVCPVAEDAIPFDIPGAEFSHVGERCTFDTLLAKFGLDDPALLRLAAIVRGADTGRLDLAPEAAGL
EAILAGLSRNIKDDDELLEAGMPLYDALYAWFRDAQEETHNWPP
>gnl|CDD|443417 COG4276, SRPBCC, Ligand-binding SRPBCC domain [General function prediction only]
MPTFERETRIPAPLEEVFDFHSRPDNLERLTPPWMGERILSGVPGGLELGDRVTYRLRHFGIPQRWTSEI
TEVEPPHYFVDEQVKGPFKSWRHEHRFEEVGGGTLMTDRVEYELPLGLLGRLAHGLFVKKYLERIFAYRH
RVLKELLESHAKY
>gnl|CDD|443418 COG4277, COG4277, Predicted DNA modification or repair protein, contains radical SAM and helix-hairpin-helix domains [General function prediction only]
MKMDLLEKLAILADAAKYDVSCASSGSKRRNSGGGLGSTEGSGICHSYTPDGRCISLLKILLTNFCIYDC
AYCVNRRSNDVPRARFTPEEVVDLTLEFYRRNYIEGLFLSSGIIKSPDYTMERLVRVARKLREEHRFNGY
IHLKTIPGASPELIEEAGLYADRLSVNIELPTEASLKLLAPEKDKESILKPMGQIRDRIEEAKEERKKFR
KAPRFAPAGQSTQMIVGATPESDRDILKLSESLYKKYRLKRVYYSAFSPVPDDSRLPALTKPPLLREHRL
YQADWLLRFYGFSADEILDEEDPNLDLDIDPKLAWALRNRERFPVDVNRADYEMLLRVPGIGVKSAKRIL
AARRHGRLRFEDLKKLGVVLKRAKYFITCAGKYPGRILLDPDDLRARLLSGKKPAPEQLSLFDA
>gnl|CDD|443419 COG4278, COG4278, Uncharacterized conserved protein [Function unknown]
MTLLWARIQALDLAPDPFVARLARENGWSAEQAERVIEEYRRFLYLCAKAPGHPLMPSQVVDEVWHEHIL
YTRSYAEFCQRVLGRFLHHTPTEGGGSERAKFQDALERTLRLYEEEFGPEPPERLWPALDPDCSQCASGI
>gnl|CDD|443420 COG4279, COG4279, Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown]
MSRYKRGAFGRTWWGKRWLEALESYDDSNRLPRGRSYARNGRVLSLKIEPGRVTARVQGSRPEPYRVSIR
LPPFSDEDWDRVIATLAGRAGFLAALLAGEMPEEIEEAFEAAGLSLFPSSPRDLRTDCSCPDWANPCKHI
AAVYYLLAERLDEDPFLLFQLRGRDREELLAALRERRAGGALAPAGSASETAY
>gnl|CDD|443421 COG4280, COG4280, Uncharacterized membrane protein [Function unknown]
MNWSIFLAAFLASLVELVEAFTIVLAVGVTYGWRPALLGAAAGLLLVLALVATLGPALVLLPLNYLRLVI
GVLLLLFGYRWLRKAIRRFKGLRALHDEEAAFAKETEELREDSAVKANWLAFLTVFKVVLLEGLEVALIV
VALGPASGSYSSALLGALLALLLVLVLGAVLHAPLAKVPENTLKFVVGILLFSFGTFWLGEGLGAEWPGG
DLALLLLFALYLGINYLIVRWLKRRKPASVR
>gnl|CDD|443422 COG4281, ACB, Acyl-CoA-binding protein [Lipid transport and metabolism]
MSDLQAAFEAAVARVKTLTERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKD
EAMQQYIDLVNSLLGKQ
>gnl|CDD|443423 COG4282, SMI1, Cell wall assembly regulator SMI1 (Killer toxin-resistance protein 4) [Cell wall/membrane/envelope biogenesis]
MASVAESWERIEAWLAEHAPDLLAALRPGASEADIAALEAALGVELPEDLRALYRIHNGQGDDALPGLFG
NYRLLSLEEILDEWEVWKELLDDGEFDDLSEPDGGIRPVWWHPGWIPFAADGGGDHLCVDLDPGPGGTRG
QVIEFDHDEGEREVVAPSLAELLEDYADALEAGEYVYDEDDGEDGRLD
>gnl|CDD|443424 COG4283, DfsB, Uncharacterized conserved protein DfsB/IRC4, DUF1706 (PF08020) domain [General function prediction only]
PRPTSKEELLEAINKNFEKLIALLDSIPEEEADEPFDFGGRDRSVRDVLAHLIGWHELLLKWYEDEQAGE
PVDFPAEGYKWNTLGELNQKFYAKYQDLSLEELLALLNASHQEILALIESLSDEELFGKKRRPWTGKWTL
GRYIQSNTSSPYDWARKKIRKWKKAQA
>gnl|CDD|443425 COG4284, QRI1, UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism]
LIEKLEPHGQEHLLRFWDELSEAQQKMLEAQIEEIDIDVFQHLYRQLVLAEGATGLIPESDIEPAPVTDL
PLTDLDEVDRDRAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLAAR
RRYGVPLPLYIMTSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALDADLGPVLLPADPELELCPPG
HGGIYTALLASGLLDKLLERGIRYLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHL
ARVDGRLILREYSQLPDEEAEAFTGELRHPYGNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDES
GKPTSPNVIKFETFMFDAIPLFDGAVAIEVDREERFAPVKNTNGSDSPPLFY
>gnl|CDD|443426 COG4285, COG4285, Uncharacterized conserved protein, conains N-terminal glutamine amidotransferase (GATase1)-like domain [General function prediction only]
MKARPTPRPRVLVYRGPGASDDCVEALVRALKQLNLGFKVRYVTAEDITAGTLANADLLIQPGGGDLPYY
KALGGEGNAAIREFVENGGGYLGICAGAYLASKYVGFGLGTDARVVGNREFFPGVAVGPLGRPGADVSLT
ESTAVLVRWRGDTLTIYYQGGPYFEPAPDGPGYTVLATYADGSPAIVSGTYGKGRVVLSGPHPEATPGLE
EMIPAGVLWAA
>gnl|CDD|443427 COG4286, COG4286, Uncharacterized conserved protein, UPF0160 family [Function unknown]
MTPMLLVTHSGGFHADDVFAVAILTLLFPDAELVRTRDPEWIAPADIVFDVGGVYDPATGRFDHHQRGAP
LREDGIPYSSFGLIWKHYGRDYCRALGVPEADADAIAAAIDKGLVLPIDAVDNGAVTPSVAPLGGLTLSV
LLEAFNPVWDDEAPEAEDAAFLEAVAIARAVLERAIARAAAKLRAEAIVLQAIAAAGDKRILVLPRGMPW
RSAVFKAGDHLLFVVYPRGEGDWTVQTVPPEPGSFEQRADLPAAWAGLSDEALAAVTGVPDAVFCHNGRF
IAGAKSREGALKMARLALEEAA
>gnl|CDD|443428 COG4287, PqaA, PhoPQ-activated pathogenicity-related protein [General function prediction only]
LALALLLLAAGAAAAAAVTPETALKDYVNNRDPPLKWELKDTTTLGGVTVYELLLTSQKWRPITWKHQLT
IFVPKEVLPDGALLFITGGSNKPEQPNWPPPGDFDPELLAAIARKTKAIVALLSQVPNQPLFGGLREDAL
IAYTWHQFLKDPDYTWPLLFPMVKSAVRAMDAVQEFLKQELGKEIKRFVVTGASKRGWTTWLTAAADPRV
KAIAPMVIDVLNMPASLEHQYKVYGGYSIAIEDYVKLGIPQQLGTPAGKALMQMVDPYSYRARLTMPKYI
VNGSNDDYWVPDAIKHYYDDLPGEKALRYVPNAGHGLGDGKQAVEALSAFFGRTLQGRPLPQVSWKLDET
GKGARLTVASSEAPVKAKLWTATSEDRDFRGVRWTSRPLKLKEGGAVSVTVTYPKKGWQAFFVELTYKDG
NGPYTVSTRVYVLPDDKVPT
>gnl|CDD|443429 COG4288, COG4288, Uncharacterized conserved protein [Function unknown]
MMSAIGKRRWAIPDGYIPPRSTGPEPELTSHEALCVLNAGDEDAHVEITIYFEDREPVGPYRVTVPARRT
RHVRFNDLIDPEPIPLGVPYASVVESDVPVVVQHSRLDTRQAENALLSTIAYP
>gnl|CDD|443430 COG4289, COG4289, Uncharacterized conserved protein, DUF2264 domain [Function unknown]
MKRAPPNPIAGNPLWTRADWVALLDKLLEPVLPYASPGGARVRLPGEPAHYGRKVAYLEGFARTLWGLAP
WLAGGGDADPEGKLRELYRKGIANGTDPASPDYWGRFTDYDQRLVEAAALALALLLAPEWLWDPLDEATK
ERVVAWLKQVRGIKPPDNNWLLFRVMVEAFLLSVGGPYDRERIEYALARHEEWYVGDGWYSDGPGFHFDY
YNSWAIHPYLLLYAQLAGDADPLAAERAARYRERARRFAEDFERLFGPDGTFPPFGRSLTYRFAAFAPLA
ALALAGVEALPPGQVRGALSAVLRWFLEQPAFDRDGWLTIGYHGPQPAMAENYSSPGSPYWALKAFLPLA
LPADHPFWTAPEEPLPAEKAWSAGQDAPLDHALALS
>gnl|CDD|443431 COG4290, COG4290, Guanyl-specific ribonuclease Sa [Nucleotide transport and metabolism]
MRRRLGLAALLLAALLLAGCTASAPGSAPTSSSGLPTVALSELPPEARDTLALIEAGGPFPYRKDGVVFG
NRERLLPAKPRGYYREYTVPTPGSRDRGARRIVTGGDGEAYYTDDHYASFRRIR
>gnl|CDD|443432 COG4291, COG4291, Uncharacterized membrane protein [Function unknown]
MARSMIALLRLLRARPRLLISLAVGLVVALLLPASLSLVTRLLIGWNAGALLYLVLTWLVMWRADPERTR
RRARREDEGRAVVLLLVLLAALASLVAIVLELASAKDLSGAGKVLHLALAVATVVLSWLLVHTMFALHYA
HLYYSDDEDGRGGLDFPGDEEPDYWDFLYFSFTIGMTAQTSDVAITSRAMRRLVLLHSLLSFFFNTVILA
LTVNLAAGLLG
>gnl|CDD|443433 COG4292, LtrA, Low temperature requirement protein LtrA (function unknown) [Function unknown]
MTSTRARRPLLRARDPAEEHRRVTWLELFFDLVFVFAVTQLSHLLAEHLTWAGLLEFLLLFFAIWWAWVG
TTWFTNRFDPDDPPVRLLLLVQMAGALVMAAAIPEAFGDRGLVFALAYVVMRVGRALLYLRAARHDPALR
RNALRYAAWLAVSAVLWLAGALLPGPARLALWAVALLIEYLGPLLAFSRTGGWPVHGEHLAERYGLFVII
ALGESILATGAGLAEAPWTAPTLLAALLGFVLTFALWWLYFDRVAEAALHALARAADPGRLARLAYTYGH
LPLVAGIVATAVGLELVVAHPTGHLPGAAALALAGGVALYLLGLALFRRRVLGRVSRSRLLGAAALLLLA
PVAAALPPLALLALLAAVLVAVAVWETRGLRRRPRAAA
>gnl|CDD|443434 COG4293, COG4293, Uncharacterized conserved protein, DUF1802 family [Function unknown]
TTHALKEWAVAVEALEAGRQIILLRKGGIHEEPGGFQVEHERFLLYPTYEHQKPELLKPEYADLLDPVLS
GWHPGTVRIRSWAEVTDVFEVSDEEALAALEPFHIWTEEFIRDRLKWKPKKPLHVLLLRVYRLPEPVEIP
YRPEYGGCKSWIDLPEPISLEGSAPVLDDEAFERRAAEIREIL
>gnl|CDD|443435 COG4294, Uve, UV DNA damage repair endonuclease [Replication, recombination and repair]
MIIRLGYVCINLSLNASPSKTMTLANYSKLDREARLERLERIARQNLENLLRILRYNIAHGIGLFRISSD
LIPLATHPVVGWDWWKEFAEEFEEIGEFAKEHGMRVSFHPDQFTVLNSPREEVVENSIADLEYHARVLDA
MGLDEEAKIVIHVGGVYGDKEAALERFIENFKRLPDAVKKRLVLENDDKTYTAADVLELCEELGIPMVFD
VHHHRCNPDGESLEELLPRIFATWKDEDGPPKIHYSSPKSEKRPRAHADYIDPDDFLPFLKALKGLRDID
VMLEAKDKDLALLKLMEELKELRGVKRIDGATF
>gnl|CDD|443436 COG4295, COG4295, Predicted RNA repair component, a phosphatase of H2Macro superfamily, DUF2263 family [General function prediction only]
MSRERRKAIAQETLEILERGSYINPSGETVDIAEAVEAAVAGTRLYTPEDLLALTDKTPPAYKTRIEVTN
ETTLAAARRLVEGGGDVACLNFASAKNPGGGFLGGAQAQEESLARSSALYACLLRAPEYYAFHRAQRSLL
YSDRMIYSPGVPVFRDDDGDLLDEPYLVSFLTSPAPNAGAVRRNEPERADEIEEVLRERIRKVLAVAAHH
GHRTLVLGAWGCGVFRNDPADVAGAFAEALAERFAGAFERVVFAVLDRSPEQPNLTAFRERFGR
>gnl|CDD|443437 COG4296, COG4296, Uncharacterized conserved protein, DUF2262 domain [Function unknown]
LEEILKEYLKPVVIEDEVLGEFTLDKQSGSFEGSIEWLGNEISLSLDNEDEETITKALATAKDLFANQEE
WDKKLRDYAAKELLELANDWLDDDEEAPEITAEEFAKRIRLEEITVDPDGSFEFYYDDGDLFWGHVILVS
GNLNGGLTDADIAG
>gnl|CDD|443438 COG4297, YjlB, Uncharacterized conserved protein YjlB, cupin superfamily [Function unknown]
MTRADIEPETFLFEDDGWVPNNPRLPVLIYRGALPEDDDPAAAFEALFEANGWPNSWRNGVFDYHHYHST
AHEVLGVASGSARLQLGGEGGREVEVKAGDVLVLPAGTGHKRLSASEDFLVVGAYPPGQDYDICRGEPEE
RPAALARIAAVPLPATDPVTGKDGPLLRLW
>gnl|CDD|443439 COG4298, YiaAB, Uncharacterized conserved protein, YiaAB domain [Function unknown]
AQKDTPAWILQVWASFAVALGLTAIGIWYLPVDLWTKGYLGMGILFLVTSTFTLAKTLRDRHEADRLINR
IEEARTEKLLAEHDPFKL
>gnl|CDD|443440 COG4299, COG4299, Predicted acyltransferase, DUF1624 domain [General function prediction only]
PSKRLLSLDVLRGLTIALMILVNNPGSWSHVYAPLLHAEWHGFTPTDLVFPFFLFIVGVAMPFSLSKRLA
KGAPKSALYRKILKRSLILFLLGLFLNWFPFFLKDFSEIRIPGVLQRIALAYLFAALLYLYLSRKTQLII
AAGLLLGYWLLLAFVPVPGFGAGPLSPEGNLAAYIDRLLLGKGHLYKGEGKTFDPEGLLSTLPAIVTVLL
GYLAGRLLRSKKSNREKVLKLLIAGVLLLLLGLLWNLVFPINKKLWTSSFVLLTGGLALLLLALFYWLID
VKGYRKWTFPFVVFGMNAIFIYLLSELVARLLGLIKVGGTATSLFGWLYQNLFQPILGPYNASLLFALAF
VLLWWLILYWLYKKKIFIKV
>gnl|CDD|443441 COG4300, CadD, Cadmium resistance protein CadD, predicted permease [Inorganic ion transport and metabolism]
MNWLITTILTAIGAFAATNIDDIVILTLFFAQVNGRFRPRHIVIGQYLGFTALVLASLLGAFGALILPEE
WIGLLGLLPIALGIRALLNREREEEDEEAVELESSESSFLASLLSPQTYTVAAVTIANGGDNIGIYVPLF
ASLSLAELLVILAVFLVLVGVWCLLAYKLARRPAIAEILERYGRWLVPFVLIGLGIYILVESGTFGLLLL
L
>gnl|CDD|443442 COG4301, COG4301, Uncharacterized protein, contains predicted SAM-dependent methyltransferase domain [General function prediction only]
SSASDLRAEPADAAFAADVLAGLSATPKTLPPKYFYDARGSELFEQITELPEYYPTRTELAILRRHAAEI
AALLGPGATLVELGSGSSTKTRLLLDALGRPAAYVPIDISGEALEEAAERLAADYPGLEVHPVVADFTRP
LALPAGLAAGRRLVFFPGSTIGNFTPEEALAFLRRLRALLGPGDGLLIGVDLVKDPAVLEAAYNDAAGVT
AAFNLNLLRRINRELGADFDLDAFEHRAFYNPEEGRIEMHLVSLRAQTVRIGGLTFEFAAGETIHTENSY
KYTLEGFQALAAAAGFEPVRVWTDPKGWFSLHLLRA
>gnl|CDD|443443 COG4302, EutC, Ethanolamine ammonia-lyase, small subunit [Amino acid transport and metabolism]
MSEDIRPQILVPNPVNPDPWARLRAFTPARIGLGRAGTSLPTRALLRFQLAHAAARDAVHSPLDVEALAA
QLAALGLPLLTVHSAAADRDEYLRRPDLGRRLSDESRALLAELCPGPPDVQIVVADGLSATAVEANAAPL
LPALLPGLKAAGWSLGPPVFVRQGRVALGDEIGEALGARVVVVLIGERPGLSSADSLGAYLTYAPRPGRT
DAERNCISNIRPGGLPPAEAAAKLAWLLKEALRRKLSGVALKDESDALLLDAAGP
>gnl|CDD|443444 COG4303, EutB, Ethanolamine ammonia-lyase, large subunit [Amino acid transport and metabolism]
IYKTTLGGTTYQFKDLKELLAKANPERSGDELAGVAAESAEERVAAKMVLADLPLKDFLNEPVVPYEEDE
VTRLIIDTHDAAAFAPIKHLTVGEFREWLLSDATTGEALARLAPGLTPEMVAAVSKLMRNQDLILVAKKC
RVVTRFRNTIGLPGRLSTRLQPNHPTDDPRGIAASILDGLLYGSGDAVIGINPATDSVESVTRLLKLLDE
VIQRYEIPTQSCVLAHVTTQMEAIERGAPVDLVFQSIAGTEAANRSFGIDLALLDEAREAALSLGRGTVG
PNVMYFETGQGSALSANAHHGVDQQTLEARAYAVARRFDPLLVNTVVGFIGPEYLYDGKQIIRAGLEDHF
CGKLLGLPMGCDVCYTNHAEADQNDMDNLLTLLAAAGCNFIMGVPGADDVMLNYQSTSFHDALYLRELLG
LRPAPEFEAWLEKMGIMDENGRLTPRAGDPSLFLKLLGLL
>gnl|CDD|443445 COG4304, COG4304, Uncharacterized conserved protein, DUF2247 domain [Function unknown]
LYPIPYDFIDNKIRLTWSDILWGIENNLLSSDVAVEYAEEILEKEENSDRELELAFLIPKESNEIRPVLE
ELAEEETKADDSAIREKWLYLVLSWLFKNRKNFSDPLGEVEKIYADFDYPEEIESFVRYMPPSDPSLHSR
EENINRLYKNWEEYLKEEKIKLKG
>gnl|CDD|443446 COG4305, YoaJ, Peptidoglycan-binding domain, expansin YoaJ [Cell wall/membrane/envelope biogenesis]
MRLLSWLVLVALLGLLACGAAGPAAAAAPPGATHSGEATYYDADGGGNCSFDPIPADLLVAALNPTDYAN
SAACGACLEVTGPKGSVTVRVVDRCPECAPGDLDLSPEAFAKIADLEAGRVPITWRLVSCPVSGNVSYRF
KEGSSQWWTAVQVRNHRNPIAKLEVRSGGQWVALPREDYNYFVAESGMGPGPFTIRVTDVYGQVLEDTLP
PLSPGVVQDGKVQFPA
>gnl|CDD|443447 COG4306, COG4306, Uncharacterized conserved protein, DUF2321 domain [Function unknown]
MGTYDVAQVCLNGHVTTSSVNTSPELRQNFCSKCGEETITQCPSCSTPIRGDYHVEGFFGLGDPYLAPSY
CHNCGKPFPWTERKLEAA
>gnl|CDD|443448 COG4307, COG4307, Uncharacterized conserved protein, DUF2248 family [Function unknown]
MKLFRCPNCGQLLFFENTRCLSCGHPLGFDPDALAMSALEPDGDGTWRALAADGRRYRFCANAEHAVCNW
LVPADDPGALCRACRLNRTIPDLSDPENLERWARIEAAKRRLLYSLLRLGLPVPSRAEDPEHGLAFDFLA
DPPGGEPVMTGHANGVITINLAEADDAERERRRVQMGEPYRTLLGHFRHEIGHYYWDRLVRDGGRLEAFR
ALFGDERADYAAALQRHYANGPPADWQENFISAYATAHPWEDWAETWAHYLHIVDTLETAAAFGLALDPR
LPDEGPLTADLDFDPYAAADFDRLLEAWLPLTFALNSLNRSMGQPDLYPFVLSPPVVEKLAFVHRLVRAA
AAGA
>gnl|CDD|443449 COG4308, LimA, Limonene-1,2-epoxide hydrolase LimA/EphG [Secondary metabolites biosynthesis, transport and catabolism]
MTSPIDVVRAFLAAWSRLDVDAALSLLADDAVYHNVPLPPVRGRDAVRAFLEGFLRGAAGFEVRIHHIAA
DGGTVLTERVDRFRLGGLRVEFPVCGVFEVDDGKITLWRDYFDLADLLK
>gnl|CDD|443450 COG4309, COG4309, SirA-like two-layered alpha/beta sandwich domain, DUF2249 family [General function prediction only]
ACGSSDDAVPTLDVRGIPPRERHAAIFGAFDALAPGESFVLVNDHDPKPLLYQLEAERPGAFTWEYLERG
PEVWRVRITRRAA
>gnl|CDD|443451 COG4310, COG4310, Uncharacterized conserved protein, cotains an aminopeptidase-like domain [General function prediction only]
AMHALARRLFPICRSITGDGVRETLEILGEHIPLEIHEVPSGTQVFDWTVPKEWNIRDAYIKDPDGERVV
DFAESNLHVVGYSVPVDATMSLEELKPHLHTLPDQPDAIPYRTSYYKRRWGFCLSHNQREALPDGDYEVV
IDSTLEPGHLTYGELVLPGESDEEVLLSTHICHPSMANDNLSGPAVATFLARRLASRPDRRYSYRFLFIP
ETIGSITWLSRNEDELKRIKHGLVLTCVGDPGDFTYKRSRRGDAEIDRAAEHVLRHSGPEYKVYDFLPYG
YDERQYCSPGFDLPVGSLMRSKYGEYPEYHTSADNLDFVSPEGLAESLDLLLAIIEVLEANRVYLNLNPK
GEPQLGKRGLYPTIGGKSDARQAQMALLWVLNLSDGEHSLLDIAERAGLPFDELAEAADALLGAGLLEEV
EP
>gnl|CDD|443452 COG4311, SoxD, Sarcosine oxidase delta subunit [Amino acid transport and metabolism]
LLITCPYCGPRDESEFTYGGEAHIARPDPPAAASDEEWADYLFLRDNPKGVHRERWYHAAGCRKWFNVER
DTVTHEILGTYLAGEPRPAGAAEA
>gnl|CDD|443453 COG4312, COG4312, Predicted dithiol-disulfide oxidoreductase, DUF899 family [General function prediction only]
MTLPPVVSREEWLAARKALLAKEKELTRARDALAAERRRLPWVRVDKDYVFDGPDGPVSLADLFDGRSQL
IVYHFMFGPGWEEGCPGCSFFADHVDGHLAHLNARDVTLVAVSRAPLAEIEAYKRRMGWTFPWYSSAGSD
FNYDFGVSFTPEQLAGVEYNYRREPFPSGELPGLSVFLRDGGEVFHTYSTYGRGVEQLGGTYNYLDLTPK
GRQEDWEDSPMDWVRHHDEYGPA
>gnl|CDD|443454 COG4313, SphA, Sphingosine uptake channel SphA-related outer membrane channel [Cell wall/membrane/envelope biogenesis]
MKKSSRRLLLAAALAAALLAAGPAQATEGGLGHYPLGVEGFLAGALPPPGFYFLNYYYYYSADALRDNNG
DKLPAGFDATVDANALRLIYVTDTKVLGANYGFSAIVPLVSLDVDANVGGVSDSRTGLGDIYLGPLILGW
HPSPNLHVVAGLDIYAPTGSYDPNRLANPGLNYWTFDPTLAFTYLFDDGWELSAKLGYDFNTKNPDTDYQ
SGQEFHLDYALGKHFGKGWRLGLVGYYYKQLTDDSGPGARLDGFRGRVFALGPGVGYDFPPGGFSLSLKW
YHEFGARNRPEGDALWLRLSIPF
>gnl|CDD|443455 COG4314, NosL, Nitrous oxide reductase accessory protein NosL [Inorganic ion transport and metabolism]
MMRRLLLAALALLLLLAGCGGGADAAAPEPVALTGDDRCPVCGMTIADHPGPKAQIVYKDGKPLFFDSVR
CMFAYLLEPEQRRDIAAIYVTDYSTAGEWIDARKATYVVGSDVPGPMGAELVPFADEEDAEAFAAEHGGK
VLRFDEITPDLVESLG
>gnl|CDD|443456 COG4315, COG4315, Predicted lipoprotein with conserved Yx(FWY)xxD motif (function unknown) [Function unknown]
TAASTELGPVLVDADGMTLYTFDKDTAGPGKSACDGACAANWPPLLADGDAKASGLDTGDFGTITRADGT
KQWTYKGWPLYYYAGDKKPGDTKGDGVGGVWHVVKPDG
>gnl|CDD|443457 COG4316, COG4316, Uncharacterized conserved protein, DUF2251 domain [Function unknown]
MLYLTLEDEITVGEPKVVESHSPEGHLAVVFEDDGDTGYFYALDLSQEGQPILDALHIYNVEDVSDRHIP
SVVQICWSEDGYKAALLINGYPHAVFDFAAKRGYCRNGFPPPDLGMWSKEEHEWTDELVEFWLG
>gnl|CDD|443458 COG4317, XapX, Xanthosine utilization system component, XapX domain [Nucleotide transport and metabolism]
MKEYLLSLLAGLLVGVLFSLLKVPSPAPPVLAGLVGILGILLGEQLVPWLRRL
>gnl|CDD|443459 COG4318, COG4318, Uncharacterized conserved protein [Function unknown]
MRSVLAAAPCRPDARPGDLLQVPLADLRPTQMTVGLREVAYKRARWRAKSKKKLDAYLKKHMIPVVIGPG
GRLYLTDHHHLLRALLEEGVKTVLVRVLADLSSLDKDAFWRVMDARGWVHPYDEKGRRRPPAQLPKSLAD
LRDDPYRSLAGFLRDAGGYAKDTTPFSEFLWADFLRRRIDRKDVDKDFAAALKEALRLARSPEASYLPGW
CGPTA
>gnl|CDD|443460 COG4319, YybH, Ketosteroid isomerase homolog YybH [General function prediction only]
MKRSAEDEAAIRALLAAFAEAFNAGDADALAALYAEDAVFFDPGGPPVRGREAIRAAWAAAFAAGPRVTF
EVEDVRVLVSGDVAVVTGRWRLTGTDPDGEPVELAGRYTLVFRKQADGRWKIVHDHASGVP
>gnl|CDD|443461 COG4320, COG4320, Uncharacterized conserved protein, DUF2252 family [Function unknown]
MSPRVPRSSHADWAPAARRRDPVDLLEEQNAGRDPELLPLKYGRMAASPFAFFRGTAHLFAADLAGTPNT
GPRVWICGDAHLENFGLFASPERLLVFDLNDFDETLPGPWEWDLKRLAASLVLAARENGLSDKEARKLVR
AFVRAYREAMARFAGMDTLDVWRIDADNTRGLVRKLLEKARRRTRARLLDKLTEVVDGERRFRDDPPLLV
PVSDAERAAVRAALAAYRATLPPDRRYLLDRYRVKDVARRVVGVGSVGTRRYVVLLEGADDDDPLILQVK
EARPSVLAPYLPPSQPAFEHEGERVVAGQRLMQAASDPFLGWTTIGGRDFYVRQLRPMKGSLDLEDLSPE
RLEDYARLCGRALARAHARSGDDSGYSIAAAIAGYLGKSDEFDDAIADFALAYADQVERDHAAFVAAVRA
GRLPAASA
>gnl|CDD|443462 COG4321, COG4321, Predicted DNA-binding protein, contains ribbon-helix-helix (RHH) domain [General function prediction only]
MCEIGADPELYRPVKRSVRLAGHRTSVRLEPAFWDALEEIAAREGLSLNALIAEIDDERGEVGNLASALR
VFCLRYLRLRAAGPGPARAGPPI
>gnl|CDD|443463 COG4322, COG4322, Uncharacterized protein, contains DUF2272 domain [Function unknown]
MPRSLLAAALLLLLAACAGAAAPQAACPDFAARPPPSPAAQRIVAIACREWRLFGRPVIDDDGRLASLGL
TEEEDPALWQRVGRYWRAVGKSDLTGQDCRAFLVDTPWSAAFISWVMRKAGVAGDRFPFSPAHSDYINAA
IRGADGPGAAFRARDPAEYSPRPGDLLCAGRGRSRVDGLRAFLDAPTTGGLPSHCDIVVAVNPGGRELEA
IGGNVRDSVSMRLLPLDRDGRLAPRPGNRRPWFVVLQNR
>gnl|CDD|443464 COG4323, COG4323, Uncharacterized conserved protein, DUF962 domain [Function unknown]
MEKRFTSFAEFYPFYLSEHSNPTCRRLHFVGTTLVLALLALALATGNPWWLLAAPLVGYGFAWVGHFFFE
KNRPATFKYPLWSLMGDWVMFFDMLTGRLRFELERAG
>gnl|CDD|443465 COG4324, COG4324, Predicted aminopeptidase [General function prediction only]
MRRRAKRLLRALLLLLLALLLSGCATLGYYWQAVSGQLSLMRARRPIDEVLADPATPPALRERLQLAQRI
RAFASTELALPDNASYRRYADLGRPYVVWNVVAAPELSLTLKTWCFPVAGCVSYRGYFDEADAEAEAAEL
RAQGLDVYVGGVPAYSTLGWFNDPLLSTFIRWPEGELARLIFHELAHQVLYVKGDTAFNESFATAVEREG
VRRWLAQHGSAAARAEYARRDQRREQFRALLLATRDRLEALYASDLSDAQKRAAKAAIFAQLRADYAALK
ARWGGYAGYDRWFAQPLNNARLAAVATYHQLVPAFEALLEQEGGDLPRFYAAVRELAALPAEERKAALQA
LAAAA
>gnl|CDD|443466 COG4325, COG4325, Uncharacterized membrane protein [Function unknown]
MRARLRKLWRRLRSSLWFRPALIALLAILLALLALLLDRALGDDLLELLPWLFIGGADGARTLLSTLAGS
MLTVTTFSFSITVVALQLASSQFSPRLLRNFMRDRGTQNVLGTFIGTFVYSLVVLRAVRTGYYDGGRFVP
QLSVLVAILLALLSVGALIYFIHHLSRSIQVDNIIDRVERETRKAIDRLLPEPSLGARTPLPDPLPEDAT
PVRAPRSGYVQAIDVDALLKLAEEHDLVIRLLVRPGDFVVPGTPLARVWGGKALVDDELAEALRRAFVIG
RERTFEQDPRFGLRQLVEIALRALSPGINDPGTAIDCIDRLGRLLAELAARPLPSPVRRDEDGRPRVVVP
PLSFEDLLDDAFDQIRRYGAGDPEVLLRLLKALAALAEVAPDPERRAALRRHAELLLERAERALSLEEDR
ARLRRRAAALRQALGRR
>gnl|CDD|443467 COG4326, Spo0M, Stage 0 sporulation-control protein Spo0M [Cell cycle control, cell division, chromosome partitioning]
MMFKKLLASVGIGGAKVDTVLDNPTVRPGETLTGEVHIKGGDVDQEIDGIYLSLVTRVEVEVDDGEYKTT
VEFARYRLAGPFTIAAGEEREIPFSLPLPWETPITAVYGPLGGMPVWVRTELDIAGAVDPGDLDPLEVEP
LPLQEAVLDAFERLGFRLRKADLEAGRLRGVRQQLPFYQEIEFRPSGQYAGRLDEVELTFVADPDGLDVL
LEVDRRGGGGLLSEDGDDSYGRFTVSHDDADTTDWAAQLEQWLRQVAR
>gnl|CDD|443468 COG4327, COG4327, Uncharacterized membrane protein, DUF4212 domain [Function unknown]
MADMNLPEPATAYWRRNLRLIAILLVIWFLVSFGFGLFARELNQIRFGGFPLGFWFAAQGSILVFVVLIF
VYAWRMNRLDRKYGVDE
>gnl|CDD|443469 COG4328, COG4328, Predicted nuclease (RNAse H fold) [General function prediction only]
MMRFVGIDLAWTPRNPTGLCVLEDDADGRLLDLPRLRSDDEILAWIDRYVSGEPALIAVDAPLIVPNATG
MRPAERLLGRYFGRYHAGAYPANRGRPFAFPRGARLGRFLEALGFDHDPTIRPQRHGRYQIEVFPHPALV
ALFPLERILKYKKKPGLAFRRAELLRLAEILEILAEAEPPLDLSSPLWAELATAVEDALRGAELKAVEDK
LDALLCAYIAAYWWYWGPERNLVLGDLATGYIVAPALPTQRAARARSV
>gnl|CDD|443470 COG4329, COG4329, Uncharacterized membrane protein, DUF2243 domain [Function unknown]
MSTSSATASRDRRRLVWAGILLGLGLGGFVDGIVFHQLLQWHHMLSSVYPPTTVSGLRLNLLSDGLFHAF
TWVATVAGLFLLWRARRRRDVPWSGRRLWGGVLLGAGLFNLVDGVVDHKLLGIHHVRYGVNQLAWDLGWL
ASGVLLLVAGWLLLRRGRRRDARRA
>gnl|CDD|443471 COG4330, COG4330, Uncharacterized membrane protein, DUF1361 domain [Function unknown]
MKKLLILLLALALLTILCLFLLLARALLTGSLFFLFLIWNLFLAWIPLLLSLWLFRFKKRRSLLWWLLFL
VWLLFLPNAPYLLTDLIHLIEDPNYPLWYDLLLLLSFALTGLLLGVLSLLNIHRYLRRRGGKKLAWLFIL
IIHLLSGFGIYLGRFLRFNSWDILTNPFSLLRDIFDSLTNKKAWLFTLLFGLFLAVLYLVFKQLTLGLIL
RSRR
>gnl|CDD|443472 COG4331, COG4331, Uncharacterized membrane protein, DUF2127 domain [Function unknown]
MTSSKGERPETLLDRVFEISLLLKGLDGLAELVGGLLLLFVPPAQILRLAHLLTQRELLEDPHDTVANHL
LHAASHLSDGSQHFAAFYLLSHGVVKLVLVVALLRKKLWAYPWAIVVLGLFIVYQLYRYVVTHSIGLIVL
TVFDLVIIVLTWREYRRVRAEAASARARRRS
>gnl|CDD|443473 COG4332, COG4332, Uncharacterized conserved protein, DUF1062 domain [Function unknown]
MNLKVIWTVTPTGLPRIKRRCSKCGSKREFRCSGKFRVNANGKLLDVWLIYKCTKCDYTWNRTIFERVNV
RSIDPELLERFHSNDPELARRYAFDPALLRRNGAELDWFPEFRIEGDVPDSPADAEVVEVELRFEYPFPL
RLDRLLAEKLGLSRSRVERLIDSGRIRSNPELNLKKRKLRNGFTITIDLGAETDRA
>gnl|CDD|443474 COG4333, COG4333, Uncharacterized conserved protein, DUF1643 domain [Function unknown]
MRARLKSDVKSEAIFSPCGRYRYRLTRVWDPGKPPLLFIMLNPSTADELVDDPTIRRCERFARRWGYGGL
IVVNLFAYRATDPKDLRAAPDPVGPENDAAILEAAAEADKVVAAWGNHGALRGRGAEVLELLREAGKKLH
CLGLTKSGHPRHPLYLPYDTKPIPWDL
>gnl|CDD|443475 COG4334, COG4334, Uncharacterized conserved protein, DUF2255 domain [Function unknown]
MSTWTPEELARIDAADELHVAPFREDGTLRTPTWIWVVRVGDDLYVRSYNGRESRWYRAALRQGAGRIRA
GGVEKDVTFEPVSDEALNDAIDAAYRAKYARSRYLGPMVGPGARAATLRVVPRD
>gnl|CDD|443476 COG4335, AlkC, 3-methylpurine DNA glycosylase AlkC [Replication, recombination and repair]
AAGLKATLALALKAALAAALLAAFAAFDADLFFAFAAEAFLALELKLRERQLLLALRLRLPAALLEALLP
LVAAEALALLRADGEGISGFAYLPLPDYVAEYGLDHFERSLAALEELTQRFTAEFAIRPFLLRDPERTLA
QLLAWSKDPDEHVRRLASEGTRPRLPWAMRLPALKKDPSPVLPILEALKDDPSEYVRRSVANHLNDISKD
HPDLVIDTAARWLGEASPETDWIVRHALRTLIKQGDPEALALLGFAPAAEVTVSGFLVSPKVVLGGELLF
FSFLLNNTSAAQQLLVVDYVVHYKKAGGKTSKKVFKLTELLLPPGETVTIRKHSFFRITTTRYYYGGHHV
VELVNNGEELAAGFFLLLA
>gnl|CDD|443477 COG4336, YcsI, Uncharacterized conserved protein YcsI, UPF0317/DUF1446 family [Function unknown]
MTAADLAAMSPAEARAAIRAGEFTGPTAGLAPGYVQANLVILPKDWAYDFLLFCQRNPKPCPLLDVTEPG
SPELPALGPDADIRTDLPRYRVYRDGELVEEVTDITDLWRDDLVTFLIGCSFSFEEALLAAGIPVRHIEE
GRNVPMYRTNIPCRPAGRFSGPMVVSMRPIPAADVIRAVQITSRFPAVHGAPVHIGDPAAIGIADLAKPD
FGDAVEIRPGEVPVFWACGVTPQAAIMAAKPPFAITHAPGHMLITDVPDSELAVL
>gnl|CDD|443478 COG4337, COG4337, Uncharacterized conserved protein [Function unknown]
MKLLSTLALAALLLAAATPAAAATPAVNAAITEEEVLAAQKAWGEGLVAIGKAYEEGGDYKALASEVIDA
LYGYDLGPVLFKPTLASEPQFRTTKEGALSYFVGGNPAFPEDKGFALKPWTKVRFENAAIIIDGDSAIAM
GNYFFTDADGKETKVEYTFGYKKDDDGKLRIVLHHSSLPYSP
>gnl|CDD|443479 COG4338, COG4338, Uncharacterized conserved protein, DUF2256 family [Function unknown]
MPRRKKSDLPSKICAVCGRPFTWRKKWARDWDEVKYCSERCRRNKKKAGDSA
>gnl|CDD|443480 COG4339, COG4339, Predicted metal-dependent phosphohydrolase, HD superfamily [General function prediction only]
QLLERWQALLQEEAEALVAELLARYSEPHRHYHNLRHLQAVLAALDELAELAEDPDAVRLAAWFHDAVYD
TGAGDNEERSAELAREFLTSLGVPEEVIERVARLILATKMHPPAPDDLDEQILCDADLAILGADPERYAE
YSKAVRKEYAHVPDKDYRAGRRKVLIKFLARPHIYYTPYARERWEAQARANLARELERLEKE
>gnl|CDD|443481 COG4340, COG4340, Predicted dioxygenase, 2-oxoglutarate and Fe-dependent (2OG-Fe) dioxygenase superfamily [General function prediction only]
TKLRRQGYALLPAADLRALLGLSGADLEALAPSWNDLPPDPYLKDGGRYRRRRYSRFIVSGGTLTRLPHR
PHFQSKDYNPLHGGIERWFEPLEDAILANPLLQRLLRAFAALFSLLEGERPWHIEVHQFRIEATPDGIGR
PTPEGIHRDGVDFVAVHLVGRHNIEGGETRIYDADGELPVRFTLLEPLETLLVDDRRVFHGVTPIQPLDP
ARPGHRDVLVLTFRALGFQGP
>gnl|CDD|443482 COG4341, COG4341, Predicted HD phosphohydrolase [General function prediction only]
LLPDRILDLLERRGDEDYGGEPVTQLEHALQTATLAERDGADEELVVAALLHDIGHLLHDLGEDLDGGDD
NHEEIAAAILRPFFSEEVTWPVRLHVAAKRYLCATDPGYFAHLSEASVRSLALQGGGMDADERAAFRAHP
YFEDAVRLRRWDDAAKDPGYDTPPLEHFEPMVRRVLARPAGS
>gnl|CDD|443483 COG4342, COG4342, Phage integrase/recombinase [Mobilome: prophages, transposons]
MRAGGFEPPPSGLRVIILTEGLLEEFLEWLVKRVSEKTAKDYISALDRYLSILTPEDLREIELAKEKKNL
VKALRNLANFLVERGIISEEVAEKIKEVLKVKRSGVDLYVPTDEEIREALKYLKEKDEEVYLLYKLLLFS
GLRLSEALRLLNNFDPEKLVCEDGIARYPLGWSRGSKRAFYAYFPAEFARELEKLDITSYRTVKDRLRRK
GLVSAKYIRKWVANKMIELGIPEEVIDFIQGRAPLSVGEKHYLNLVGLADEWYPKYVDWLKRVLEGLE
>gnl|CDD|443484 COG4343, Cas4, CRISPR/Cas system-associated exonuclease Cas4, RecB family [Defense mechanisms]. CRISPR/Cas system-associated exonuclease Cas4, RecB family is part of the Pathway/BioSystem: CRISPR-Cas system
YFLTRSEVKRLLRRLLPLRREDPVDEELRGWNWDEPPVKPRYYLGLSVSEVAYSYCPTGRDVYLRRVLGV
RGEPSEALVLGRLVHEAFAEAFREAKRLIYSGVEPYRAIEELQEEARERLSECLDLEELFRYVEKLYKFE
ANRLLAELQEVLAKQPYLGEDSLVTLAIPVAVEYKVDGSPLGLSPNLSVDALVGGGIVVELKTGEPRDFH
RLALAGYALAIESWYEIPVDYGCLVYVSFRNDRVRIKRDPVYISDELRREFLEERDEAADMVEEGRDPGL
APNCPPTCPFYEVCHG
>gnl|CDD|443485 COG4344, COG4344, Predicted transciptional regulator, contains HTH domain [Transcription]
LDELSPDPLDLYILKHLKKAGVDYAKSIARNLEIPLEEVRDYLKKLEELGLLERVEGSTIKRTEAKFKLS
SEVHKHHTYYRLSREGELLLRELREK
>gnl|CDD|443486 COG4345, PF1044, Predicted DNA binding protein, Pae2254/DUF2258 family [General function prediction only]
MSLGPNKFELSTGLVIAARYADKLRRVAFAALRKLVKKGKIEPKEIARAAAELNKLLYEILVNKLKIDKL
DVVRIRVEYEVDDKEIKLNFDTLRIERFVPEEEVSKAVEKV
>gnl|CDD|443487 COG4346, COG4346, Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase [Posttranslational modification, protein turnover, chaperones]
MSRKRLKLISILIALAVLISLYTYYTASTFKAPGGNGYVSDEVWYVSAARNILRKVFGLTPRYPYPDKEN
INTYLNLEHPPLGKYIIALSMLLLGDKPLYWRLPSIILGALIVILVFLTARRLSGNIVAGLIASLLLALD
PLLRVMSSIAMLDIYVAFFTALALYFAVSGRLLLSSIALGLAAASKYSGLFLLIPLLLYLREIEKSPIKR
FLYGILIPLAVFLIVSIPLIIYFGFGRWLQEFLGALKWHTTSRPPGPPASTPWDWFLGVNPFPLYYNPDL
YASTNPVIMILALVSTLLLFPAYLKDKKLAIASVFLWSIFLGYALVYLLGNHTLYSFYVVQLAPLAAVYL
AVSLFLLIKWDYLISWAGLLSLLVRLVLK
>gnl|CDD|443488 COG4347, YpjA, Uncharacterized membrane protein YpjA [Function unknown]
MSLMRWIRYILPNRRFLWLLLIINLLGTIYGYWWYGPQLAETPPYFWPFVPDSPTATLFFTLALALWLLG
RPLPLLEALAFVTLIKYGLWTVVMLLLFADLGGSLLWMYWMLILSHLGMAVEALLYARYYRFSRRALAVA
AVWTLLNDVVDYVFGIHPHLTYLPQYLDLAGYFTVWLSVLAVFLALALRVKRKLES
>gnl|CDD|443489 COG4352, RPL13, Ribosomal protein L13E [Translation, ribosomal structure and biogenesis]. Ribosomal protein L13E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MEPPRPIVKKPRLRKYGGVDPGVREGRGFSIGELEAAGLTVEEARKLGIPVDKRRKSVHEWNVEALKKYL
EKLGYVPS
>gnl|CDD|443490 COG4353, COG4353, Acetyltransferase superfamily protein, DUF1122 family [General function prediction only]
SLELEIESVDVSQGRFKEEFNFDLYLGGKPLGTLKYFLGRPYYRPWIEIFDYNPWFRGSGLERELFKFIS
NFLPPGGRLFVEYVRDKETRYMLQRGYPPALTRLGFSLLKAGFTWFKDWYFPEGGNEGGPKIQANKPLDE
EERIRQLRELLEEVEEFIGREEIDDLIEKALERAKKIREEGYE
>gnl|CDD|443491 COG4354, COG4354, Uncharacterized conserved protein, contains GBA2_N and DUF608 domains [Function unknown]
MKNLSPSPSWPVLPYTVRYASDDGPWIAMPLGGIGAGCIGLGGRGDLNDWEIDNGPHKFGFLPACQFAIF
EEDEGGKAQARALEGPLPPYDGSGTEGSPAPNHGLPRFEKGTFKALYPRSWVEYEDPVFPVQVTCEAFSP
IIPGNYQESSYPVAVFEWTVHNPTDKPITLSIALSWQNFVGWFTNAIKSPKVKVRWGGSDGNFNEWREDN
GLVGILMTSEGVDPDSEGEGQMALATITNPGVSYRTRWNPGAWGGDGLDFWDDFSADGSLPDREDETPAE
AGEQPAGALAVRFTLAPGETREIPFVLAWDFPNREFWWGVNYYRRYTNFYATQGKDAWAVARTALKHLDE
LEEQTLAFQEPLLRSDLPDWVKEALLNNLYTLRSGTCLRTEDGQFAVWEGLDDDEGSCYGSCTHVWNYSF
ALAFLFPELEKSMREVEFARAIDDEGAMPFRLGLPLEHPWEDCNLAADGQMGFVLQVYRDWLLSGDDEFL
RECWPAVKKALEYAWIGWDADQDGVPEGAQHNTFDWELYGPNPYCGGLYLAALEAAAEMAEYLGDEEFAK
TYRQWLEQGSKWYDENLWNGEYYIQDIDSGASEEYQLGEGCLADQLCGQFYAHLLGLGDLVPPENIRSAL
KSIYKYNFRKFFREHFNNGRSYALGDEFGLANGTWPDGRPENPFPYPLEVWTGIEYGAAAFMIQEGMKEE
GLKLIEAVRDRYDGNKRNPFNEPECGSHYARAMASWALYLALSG
>gnl|CDD|443492 COG4357, COG4357, Uncharacterized conserved protein, contains Zn-finger domain of CHY type [Function unknown]
MIHGIEVRGVVVDDETRCAHYHSELDVIAIKFACCGKYYPCYRCHEELADHEAEPWPRERFDEKAVLCGV
CGTELTINEYLEADSCPACGAAFNPGCALHYHLYFET
>gnl|CDD|443493 COG4359, MtnX, 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (methionine salvage) [Amino acid transport and metabolism]
KPVIFCDFDGTITEKDVIDAILERFAPPGWEEIEDDWLAGEISSRECLGRQFALLPASKEELDALLENIE
IDPGFKEFVQFCRERGIPLYIVSDGLDFYIEPILERYGLSDVPIYANRLVFDGGGIRIEFPYADPDCSNG
CGTCKCAVIRKLKSDGYKVIYIGDGRSDFCAAKLADLVFAKGKLLEYCRENGIPHTPFETFADVIAYLK
>gnl|CDD|443494 COG4360, APA2, ATP adenylyltransferase (5',5'''-P-1,P-4-tetraphosphate phosphorylase II) [Nucleotide transport and metabolism]
ILLMPGTLWQRILEQTEHALASGALQPIPTEYEFIEDAGIRFLVRIVSNLARKDAAKKKQGGTRGPDFNP
FLPYEPDLFVGDISDTHVCLLNKFNVVDHHLLIVTRAFEEQESLLTLADFAALAACLAEIDGLGFYNGGK
IAGASQRHKHLQLVPLPLAPDGLAIPIEPALASAQFPGSIGTIPSLPFRHAFARLDPDWLSSPLAAAAAL
LEAYRRLLQALGLGAGDAQQSPPYNLLATREWMLIVPRSQESFEGISVNALGFAGSLLVRNPEQLDWLKQ
LGPLTLLAAVAFA
>gnl|CDD|443495 COG4362, COG4362, Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism]
TEQEALLAEAEEFLRQCYKELGKSEEEVERRLAEVRAEIAATGTYTHTYEELEYGARVAWRNSNRCIGRL
FWRSLQVRDRRHVTTPEEVFEALVEHLRFATNGGKIRPTITVFAPDQPGRPGVRIWNHQLIRYAGYETED
GSVLGDPASVEFTDACQRLGWRGPRTAFDVLPLVIQVGGEPPRLFEIPRDLVLEVPITHPEYPWFAELGL
RWYAVPAISNMRLEIGGIDYPAAPFNGWYMGTEIGARNLADEDRYNLLPKVAERMGLDTSSNRTLWKDRA
LVELNIAVLHSFKKAGVTIVDHHTASQQFLTFEQREEKAGREVTGDWSWLIPPMSGATTHVFHRYYDNEI
LKPNFFYQDD
>gnl|CDD|443496 COG4365, BshC, Putative cysteine ligase BshC/YllA (bacillithiol biosynthesis) [Secondary metabolites biosynthesis, transport and catabolism]
MKIEEIPFETGYFSKLILDYLNEKEELKPFYDYFPSDEESFEARLKELQSSRTEDREVLVEVLKEQYKRL
GASEKTLENIELLADPNTFTVVTGQQAGLFTGPLYTIYKIISTINLAKELKEKLPEPVVPVFWIAGEDHD
FDEINHFYLLGKKLQWNKIKLEEEPGAKGAVGRLSLDKEGLEEVLEEFFKELGETEFTKELLELLKEAYL
ESETLADAFARLMNELFGEYGLVILDADDPELKKLEAPFFKRELEEQESIFKAVSETSEKLEELGYKPQI
QVNPREINLFYLKDGERERIEREGGRFKVKNTDIRFSKEELLEELEEHPERFSPNVVLRPLYQEVLLPNL
AYIGGPGEIAYWAQLKDAFEAFGVPMPILLPRNSFTLVERKIEKKLEKLGLSVEDVFLGLEELKNKWVRE
QSNIDIDALFEEAKEQLEEQFEPLRELAEKIDPSLLGLVEANEVKQLKQLDYLEKRLLKAEKRKHEDELR
RIDKIQNELFPNGSLQERVYNFFPFLNKYGPDLIDELLELLLPLEGEHYIVYL
>gnl|CDD|443497 COG4367, COG4367, Uncharacterized conserved protein, DUF2316 domain [Function unknown]
MSLNIEQRKQTRQELQANFRLSGLTIEEVAEDLGTTTSKLESVLSLDGQDPEDVWILRDYLNDKIKENGK
EPVPFSALTGDYRQYWFLDAKLIERG
>gnl|CDD|443498 COG4370, COG4370, Uncharacterized conserved protein [Function unknown]
MKRLLFLSNGHGEDLIAVRILQALQQLAPGLEIAALPLVGEGKAYRRLGIPIIGPTQTMPSGGFIYMDGR
QLLRDLRGGLLGLTLRQLQAVRRWAKQGDLILAVGDIVPLLFAWLSGRPYAFVGTAKSEYYERDEQGSWS
GSVYLPWERWLMRSRRCLAVFPRDPLTAEDLQQQGIPAFFLGNPMMDGLEPTGKDLPLLPDSLTIALLPG
SRLPEAYRNLQLILEAVEALIKVFPGRPVQFLAAIAPSLDLEPLQEILASQGWQPQGGPPEALTFQKGNA
ELILTQDAFADCLHQADLAIAMAGTATEQAVGLGKPVITIPGEGPQFTYAFAEAQTRLLGPSVILVEKPE
QVAEAVQRLLQDPDYLQRIAENGRERMGPPGASRRIAECLLNRLLG
>gnl|CDD|443499 COG4371, COG4371, Uncharacterized membrane protein [Function unknown]
MRIGGYGYGGGFGFGFGGLFSILIFIAIANFLVRSFRRAGGGGGGELGYSDNPQVSVARLQVGLLASARE
LQRELNRLAETADTGTPEGLAQVLQEASLALLRHPEYWVYASAESQQTSLEQAEAKFNQLALAERSKFTE
ETLSNVNGQLRQATAKATTLAAEEPGEYIVVTLLVATRGKLELPKINSADDLRQALRQLGSIGSDRLLAV
EVLWTPQAEGDTLTTDDLLAAYPDLKLV
>gnl|CDD|443500 COG4372, COG4372, Uncharacterized protein, contains DUF3084 domain [Function unknown]
GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ
ARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE
LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIE
SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI
AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL
LDNDVLELLSKGAEAGVADG
>gnl|CDD|443501 COG4373, COG4373, Mu-like prophage FluMu protein gp28 [Mobilome: prophages, transposons]
MTAPLEELPASGASLPADADPDAPGVLLPYQQRWIADESPLKIAEKSRRTGLTWAEAADDVLTAAAARSA
GGMNVFYIGYNKDMAREFIDACAMWAKAFNLAASEIEEFVFEDQGEDKDILAFRIRFASGFRIQALSSNP
SNLRGKQGNVVIDEAAFHEDLAELLKAALALLMWGGKVRIISTHNGVDNPFNELIRDIRAGKKDYSVHRI
TFDDAVADGLYERICLVTGKPWSPEAEAAWRADIRADYGDDADEELDCIPKDGGGAYLPRALIEACMSAD
IPVLRWEGPDDFNLRPELEREAEMADWCEEHLEPLLDALDPGLRHALGEDFARSGDLSVIWPLEIQQDLR
RRVPFLVELRNVPFDQQEQILFYILDRLPRFAGGALDATGNGQYLAEAAAQRYGAERVEEVMLSEAWYRE
NMPPFKAAFEDGTLTIPKDEDVLDDLRAVQLVRGVPRVPDGRTKGADGGKRHGDSAIALALAYYASRQDG
GPIEYASVPRRRAAARMFGRGG
>gnl|CDD|443502 COG4374, COG4374, PIN domain nuclease, a component of toxin-antitoxin system (PIN domain) [Defense mechanisms]
MSKVVLDASALLALLRQEPGAERVAALLGGAVISAVNLAEVVTKLAERGVPADEIRQALAALGLEVVPFD
EEQALLAAELRPATKAAGLSLGDRACLALALRLGLPVLTADRAWSKLDLGVEVRLI
>gnl|CDD|443503 COG4377, YhfC, Predicted metal-dependent membrane protease YhfC, DUF2324 family [General function prediction only]
MTVSPLSIIFMAVALLISILLPVVLFLWLRKRLKVSWKPFGVGALIFFLFQLVLELPLHQLVLKPNGTLA
LSSTNPLLYALYGALAAGLFEETGRYIAFKFLLKRYRRWEDALGYGLGHGGLEAILLVGLSLLNNLILAL
LINSGDLSTLASLPAEQLQLEAQLEALAATPSWEPLLGGLERIFALALHIALSVLVLQAVRRGRFLWLVL
AILLHALIDAPAVLLQAGVLTNIVVVEAVVFLLALLSLVFILRIKERRPGSAGPS
>gnl|CDD|443504 COG4378, COG4378, Uncharacterized conserved protein, DUF2325 domain [Function unknown]
MSALVVGADRLGNIPDVLEELGFTEIIHWSGRKKSDQKKSIPSGTDLVIVLTDFVNHNLMKKVKEQAKKR
GIPVVFCRRSWSSLEQAL
>gnl|CDD|443505 COG4379, COG4379, Mu-like prophage tail protein gpP [Mobilome: prophages, transposons]
SDTVSLRVGGQIYGGWTSVSIDRDLERPAGSFELELTEPWGGALPRPVKPGAACEVRIGGDLVLTGYVDD
VDPSYDAGGHTVSVSGRDKTGDLVDCSAPHPTGQWKGVTLLDIAAQLAKPFGITVIAEADTGAALPKVSI
EPGETAFEALERAARARGLLLWSDPDGTLVLTRPGSGRAVATLVLGRNVLSASLRFSIRDRFSEYTVLGQ
SHAGGDSWAAEAGAHAVKATAKDPEVTRYRPLVIVAEDVDTAAAAQARARWERARRRGRSFTLTYTVQGW
RDSDGKLWQPNQLVRVTDPPHGIDGDFLIMEVTFSLDDGGGTTTELTLMPPGAFDPEAEPKKKRSARGKK
A
>gnl|CDD|443506 COG4380, COG4380, Uncharacterized conserved protein, DUF799 domain [Function unknown]
MKRLLKLLLLLLLALLLSGCATPPKPYDYTAFKESKPRSILVLPPVNKSPDVKAPYSVLSTVTQPLAEAG
YYVFPVALVDETFKQNGLTDAADIHAVPPAKLREIFGADAVLYVTITEYGTSYQVLSSVTTVSAEAKLVD
LRTGKTLWSGSATASSSEQNNNSGGGLLGMLVSAAVKQIVNTATDKYHDIAGIANARLLSAGRPNGLLYG
PYSPNYGKD
>gnl|CDD|443507 COG4381, gp46, Mu-like prophage protein gp46 [Mobilome: prophages, transposons]
MDIALVWDNPGTGDYALGGGDLLTDDTLATAVYISLFTDRRADPDDELPDGTGDRRGWWGDSYADRPLGS
RLWLLRREKDTSRVLLLARQYAEEALQWLIDDGRARSITVTAERPRPGWLLLTIEVTLPDGTKQTFQFRV
AWEGI
>gnl|CDD|443508 COG4382, gp16, Mu-like prophage protein gp16 [Mobilome: prophages, transposons]
MTDMRKRLIAKIHIAKRQLGLDDDTYRALLQRVTGKTSSKDMTDAELEKVLAELKRKGFKPKSKKKKHGG
RPAAAKVRRALLAKIRALWAEMGKAGFLRDKSWAYANAFAKRMFGVDRVEWLDDDQLRKVIEALKKWARR
HGKKADWERG
>gnl|CDD|443509 COG4383, gp29, Mu-like prophage protein gp29 [Mobilome: prophages, transposons]
MSQILDQTGRPIKKAALTQEIAAATLAGVRDIWSGHPSRGLTPARLAPILRAAGQGDLTAQLELAEDMEE
RDPHVFAVLQTRKRAVLGLEWRVEPASDSAADKKAADFVREWLERLELEDLLFDLLDAIGKGFSVLEIIW
ETDGGLWLPKDIEWRPPRWFRFDPDGGNTLRLRTKDGSAEGEPLPPFKFVVHRHKAKSGNPYRAGLLRVL
AWPYLFKNYGVKDWAEFLEKYGLPLRVGKYPPGASQDEKDTLLRALAAIGSDAAAIIPEGMEIEFLEAAK
SGSADPYEALADWCDRQISKAILGQTLTSEADGGSRALGNVHNEVREDILDADARQLAATLNRDLIRPLV
ALNFGPQARYPRFEFDTEEPEDLKALAERDKKLVDMGLRIPQSYVRDKYGIPEPKDGEEVLGPAAPAPAP
AQPPAKPRAALGAPAAFAAAEPDAAPAAQDALDALADQLAEEAAPAMAPLLEPVRAALAAAESLEELRDR
LAALYPELDTEALAELLARALFAAELAGRAEVEDEA
>gnl|CDD|443510 COG4384, gp45, Mu-like prophage protein gp45 [Mobilome: prophages, transposons]
MRVINRVLAPLARALRGLVFRGVVTLVNDSLKIQNLQVSGLAGETLDDVERFQNYGFTSVPPAGAEAIVL
PLGGDRSHGVAIAVEDRSYRLKGLKAGEVALYHDEGHKIVLKRGGVIEIDCCKTVEVNATEKVTFDTPLL
ETTGNITAQGDINGVSTDGDVVAGGISLKGHTHPGDSGGTTGPPN
>gnl|CDD|443511 COG4385, gpI, Bacteriophage P2-related tail formation protein [Mobilome: prophages, transposons]
MSDATSLLPPNADPLERALAAALARLEDLPVPLRLLWNPDTCPAALLPWLAWALSVDGWDEAWSEAVKRA
LIKAAIEIHRHKGTPAAVRRVLEALGYDIEVTEWWEYGGPPYTFRLDLTVLEAGITEETYAELRRLINDA
KPVRSHLDGLDISLD
>gnl|CDD|443512 COG4386, gpL, Mu-like prophage tail sheath protein gpL [Mobilome: prophages, transposons]
MTISFNTIPSDIRVPGFYIEFDNSLAVRGTPANPQRVLIIGQMLATGTAAALVPVRVTSDSQAAALFGRG
SMLALMVAAARKANPYGELWVIALADAAAGVAATGTITITGTATAAGVLSLYIGGQRVQVAVAAGDTAAT
IATALAAAINAVTDLPVTAAVDATGVVTLTARHKGETGNDIDLRLNYYGGESTPAGLTVTITAMAGGAGN
PDLAAALAALGDEWYDFIVSPYTDAASLTALRDELDDRWGPMEQLYGHGYTAKRGTLGALTTFGGTRNDP
HITVAGTNGSPSPPWEWAAAYAAVAASSLEEDPARPLQTLELKGLLPPADADRFTRTERNSLLYDGISTL
EVGPGGTVQIERAITTYTKNAYGVPDPSYLDIETIRTLDYVRRALRSRITLKFPRHKLADDGTRFGPGQA
IVTPPVIRAELLAVYRELEELGIVENVDAFKDGLIVERDGQDPNRLNVLIPPDVVNQLRVFAGRIQFRL
>gnl|CDD|443513 COG4387, gp36, Mu-like prophage protein gp36 [Mobilome: prophages, transposons]
MAYATLADLIARFGEDELIQLTDRDGTGAVDEAVVEEALADASAEIDGYLAGRYALPLATVPAVLVRLAC
DIARYRLYSRRATGTEEVRKRYKDALKFLEKIAKGKVSLGLPGVGEPAESSGGVRVTSRERVFTRDSLKG
YI
>gnl|CDD|443514 COG4388, COG4388, Mu-like prophage I protein [Mobilome: prophages, transposons]
MKTTKLATLLAALSAELPASGDGAPEWIQLLPAGRFRARDGRGPWTLDDAAAAAVIAAFAARGTDLVIDY
EHQTLLAAPNGQPAPAAGWIKELEWREDGLWARVEWTERAAALIAAKEYRYLSPVFLYDATGRVLELLSA
ALTNTPALDGLTALAAAEAAMLSTQEETPMNDLLKKLLAALGLGADATEEQILAALTALKADAGAAAAAL
KELAEALGLPADLEEVVAALSAKTATPDLAKFVPVATYAALQTELAALKAKAAEAEAEALVDAALADGKI
TPAERDWATALAKQDPAALKAFLAAAPVIAALTGTQTGGKPPGPAEGAAALSAEELAVAKALGISEEDYA
KTKKAEAK
>gnl|CDD|443515 COG4389, COG4389, Site-specific recombinase [Replication, recombination and repair]
LEALLARADAAPLADRLLWLIRLVDWLRPGDAADTAAAIARLRALLDLLERNPELRAALRRLLRRLLREL
DQISLLADSGILPRTGFFSELGRRLGEKLLPPPPDTDDLSDLFSLLFPREDDAEWLAAIPDETWLRLFAL
LAFDESEDDRAAAHWRQELLDALQVLSSRIAALGLEPELRRRMPELELEDSPFLALNREVEALLEAYRAG
LDSAAALEDLRHLRVLLDQCRAAVDRVRKHLEENGVSVSLVFLLERLRQRLDRLELLLDLLLADRGEDPA
RALVRLLKELVRAENRRRSVRALFRSNTELLARKVTERAAETGEHYITRTRKEYRAMLRSAAGGGLIIAF
TALLKILLGALGLAPFWEGLLASLNYALGFVLIHLLHFTLATKQPAMTAAALAAALDDTDGDSAGLEKLV
DLVARLTRSQFAAILGNVGVVVPVALLIALLWAALFGAPLISPEKAEHLLHSLDPLGSLTLLYAAIAGVL
LFLSGLIAGWYDNWFVYHRLPERLAHHPRLRRLLGAARARRLADYVEHNLGGLAGNFSLGFLLGLTPAIG
VFFGLPLDIRHVTFSSGNLAAALVALGFDALGWPAFWWAVAGILLIGLLNLGVSFSLALRVALRSRGVRF
RDRRRLLRAVWRRFRRRPLSFFLPPRSPAPAAAPAGE
>gnl|CDD|443516 COG4390, COG4390, Uncharacterized conserved protein, DUF2322 domain [Function unknown]
MNFADNLATLPSIDHLAALELLDADGQVVATIENKPGKAGSLAVYNALAQKFGAIDAAAAEEGLELFAEH
TADARANPGKHPNIDRLLAVIEGGLTLRVKPVPA
>gnl|CDD|443517 COG4391, COG4391, Uncharacterized protein, contains Zn-finger domain [Function unknown]
NAPETIEVTAKDVSCPGPEGWLGHPRVFLDIGETGEVECPYCGTLYVLKDGLKA
>gnl|CDD|443518 COG4392, AzlD2, Branched-chain amino acid transport protein [Amino acid transport and metabolism]
MSDSEIWLLILGMALVTYLPRYLPLLLLGRLRLPPWLRRFLRYVPVAVLAALIAPGVLLPDGQLDLSLDN
PRLLAALVAVLVAWLTRNLLLTIVAGMAVFFLLRLLL
>gnl|CDD|443519 COG4393, COG4393, Uncharacterized membrane protein [Function unknown]
MSYFFPAEKRKAKARKRNSRRWLLAVLAAVAVIAVALTYLDFYASRPPELSPAEPVLAEDGKVVIPLEQV
KDGKLHRFQYIADDGTEVRFFVIKKSDGSYGVAFDACEICGDTGYYQEGNQVVCKNCGVRFNIATIGFKG
GCNPVPLPYKVDGGKITISKADLEAGANYFK
>gnl|CDD|443520 COG4394, EarP, Elongation factor P Arg32-rhamnosyltransferase EarP [Translation, ribosomal structure and biogenesis]
TARLRWDIFCRVIDNYGDIGVCWRLARQLAAEHGQQVRLWVDDLAAFARLCPELDPDLAEQTVDGVEVRH
WTADFPDVAPADVVIEAFACELPEAYLAAMAAREPPPVWINLEYLSAEDWVEGCHGLPSPQPSLGLTKYF
FFPGFTARTGGLLREADLLARRDAFQADPAAQAAFLARLGIPPQPGELLVSLFAYENPALAALLDAWAAS
PQPVRLLVPEGRALAAVAAWLGVEPLAAGDRFQRGALTVHVLPFLPQDDYDRLLWACDLNFVRGEDSFVR
AQWAGRPFVWHIYPQEDDAHLAKLDAFLDRYCAGLPPEAAAALRAFWRAWNGGQDAAQAWPALAAHLPAL
QRHARAWAQRLAAQGDLATQLVQFVE
>gnl|CDD|443521 COG4395, Tim44, Predicted lipid-binding transport protein, Tim44 family [Lipid transport and metabolism]
MKSFGAFLLDILILALIAAFLILRFLRSGRRTGFERPAAAGLAAIAAAPPGFDVEAFLRGAKAAFEMIQA
AWDAGDLEDLRELLTPEVYAEFQAAIAEREAAGETNETTFVGILDAELVDAELEGDEAEVTVRFVGELRE
ATRDADGEVVEGDPAAAEEFREVWTFARPLGSGDPNWLLAGIQQAE
>gnl|CDD|443522 COG4396, Gam, Mu-like prophage host-nuclease inhibitor protein Gam [Mobilome: prophages, transposons]
ARLKAAAVVPQTREEVNEAIKEIGDIQRELTRIEAKMNDEIAAIKARAEAKIAPLKARIKELEKGIQTFC
EANRDELTGKTKSANLITGEVGWRLRPPSVKIRKKTLDAVLEALKRLGLKRFIRTKEEVNKEALLAEPEE
ALEIVGITIVQGVEDFYIEPFEEELEQKA
>gnl|CDD|443523 COG4397, gpT, Mu-like prophage major head subunit gpT [Mobilome: prophages, transposons]
MIINAANLQALFTGFKTAFQKGLGAAPSQWNKIATTVPSTTASNTYGWLGQFPGLREWVGDRVIKNLSAH
GYTIKNKKFESTVGVDRDDIEDDQLGIYGPLFQEMGRAAAEHPDELVFGLLKAGFTTLCYDGQNFFDTDH
PVGDGTGNATSVSNMGGGSGTPWYLLDTSRALKPLIFQERKDPEFVAKTDPNDENVFMRDEFVYGVDARC
NAGFGFWQLAYGSKQTLTAANYAAARAAMMGMKGDGGRPLGIRPTLLVVPPSLESAARKLLNAELIAGGA
TNEWKGTAELLVSPWL
>gnl|CDD|443524 COG4398, FIST, Small ligand-binding sensory domain FIST [Signal transduction mechanisms]
MRLFASAHATHPDWEAAAEEVLAQLRAQLAGAPDLGLLFISDAYADEAPRLLPLLRERLGVPHWVGCVGG
GVIGTGQEYEDEPALSLMLADLPGVQFRPFHLVAPLLPDLDSPPVGGFDAPTALLHADPFSPDLPDLLEG
LAEAYPGGPLVGGLASGRGAPGQNLFAAGEVYEGGLVGVAFSGNVTLETRVSQGCRPIGPPHQVTEAERN
VILELDGRPALDVLLELLGELLEDDLELAQGSLFVGLARDEFKASLDGGDFLVRNLLGVDPRRGAIAIGD
RVRPGQRLQFCLRDAQAAREDLERLLAEIREELEPGRRPRGALYFSCLGRGGGLFGEPNAELQLIREALG
DIPLAGFFANGEIGPVGGRNFLHGYTGVLTLFRSPS
>gnl|CDD|443525 COG4399, YheB, Uncharacterized membrane protein YheB, UPF0754 family [Function unknown]
MDFLLILLLPLIGALIGYFTNWLAIKMLFRPYKPIYIGGFRLQGLIPKRREELAKSIGEVVEEELLTPEE
ILEKLLTGELKDRIRELIKLALREILDDKALPGLLGPLLQFFLGEPDSIRDRIQYDKLKNILAKEVEEYL
EELLEDIVEYILEALDIEQLVEERVNALSPEELEELILPIAKKELKAIIVLGAVLGFIIGLLQGLIVLLL
>gnl|CDD|443526 COG4401, AroH, Chorismate mutase AroH [Amino acid transport and metabolism]. Chorismate mutase AroH is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
MMVRGIRGATTVEENTPEAILEATRELLEEILERNDLDPEDIVSVIFTVTPDLDAAFPAAAARELGWTDV
PLLCAQEMDVPGSLPRCIRVLIHVNTDKSQSEIKHVYLRGAKKLRPDLAQAQ
>gnl|CDD|443527 COG4402, COG4402, Uncharacterized conserved protein, DUF2330 domain [Function unknown]
MRLALRLLLALALLAAAALLAAPAAAAACGGYVAPADTSLVNTAERVVLARDGDRTTLTMQIDYQGDPKD
FAWVVPVPVEAQVEVGDDAIFERLDAATAPRLVEYFDPDPCSRMPGPAAAPGAAGPDSGSAAAGGVTVEA
QFTVGPYDIVILSATDSGGLETWLRENGYAIPPGAQPALDPYIRQGMKFFAAKLNPGEGGVGDLRPVRVT
YPSPKPMLPIRLGAANAGPQQDLTVYVLGEGRAEPTNYRTVKIPSNALVPDFVKEGSFYKALFQKAYAKE
GGRAAFLEYAWDMSSCDPCSADPLSPENVFLTRLHVRYTRDRFPEDLTFQETSNRQNFQ
>gnl|CDD|443528 COG4403, LcnDR2, Lantibiotic modifying enzyme [Defense mechanisms]
AEARALAAPLSAAAVAAALAAAAALAAEAPADAARALAAAAALASAASARTRAAAAGPAAADLYDGAAGI
ALFLAELARLTGDERYRELARAALRPLRRLLREELAGAMGPGLFTGLGGIAYALAHLGELLGDPRLLEDA
LALAALLEELIAADESLDVISGAAGAILALLALYRATGDPAALDLAIRCGDRLLAAAVRDDGGRAWPTPE
PAGRPLTGFAHGAAGIAYALLRLAAATGDERYLEAAREALAYERSLFDPEGGNWPDLREPDDGPRFRTAW
CHGAAGIGLARLALLRALGDPELREDLERALETTLRRGFGRNDSLCHGDAGNLELLLRAARATGDPELLE
AARRLAALLLARAERAGPLGLPGLPRGVESPGLMTGLAGIGYGLLRLAAPERLPS
>gnl|CDD|443529 COG4405, YhfF, Predicted RNA-binding protein YhfF, contains PUA-like ASCH domain [General function prediction only]
MPDDASLEAFWPDALAANPEVAAEEPPEAWAFGDSPELADELAALVLAGKKTATSSALADYEAEGEPLPK
VGDLSIVLDGDGEPVAIIRTTEVEVVPFDEVTEEFAAAEGEGDRSLEYWRKAHEAFFTRELAEIGREFSE
DMPVVCERFEVVYPLE
>gnl|CDD|443530 COG4408, COG4408, Uncharacterized conserved protein [Function unknown]
MGRVLILGTGPVAIQLAVDLKLHGDGRLGIAGRPSTRSERFFQALARTPGQIQVGIQNEQHRALEGKVTI
DHFFKDYAQVTGEWDTLILAVTADAYYDVLQQIPWEVLKGVKCVILVSPTFGSNLLVRNYLNKAGCDAEV
ISFSSYLGDTRWIDEEQPNRVLTTAVKKRLYLGSTHAGSPALERLCAVLAQLGIDLEPMDTPLEAETRNI
SLYVHPPLFMNEFSLNAIFGETPPPKYVYKLYPEGPITPALIRDMRLLWKELMALLNRLGVKSVNLLRFM
NDDNYPVRPESLSRRDIESFEQLPPIHQEYLLYVRYTALLVDPFSEPDEQGRYFDFSAVPFRRVFIDEEG
LWDIPRMPKEDYYRTKIIQGIARALDVPCPTIDSLLARYETALKAFADTHGGEQLSPAFLVQDFDEDLAM
ICSQIESTR
>gnl|CDD|443531 COG4409, NanH, Neuraminidase (sialidase) NanH, contains C-terminal autotransporter domain [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]
MIYNLALSDLLLLALTAVAALTETAVFTSGDDGYASYRIPALVTTPKGTLLAFADARYNGSGDLPGDIDI
VMRRSTDGGKTWSPPQVILDYGEGGGLSAGVGDPAPVVDRKTGRIFLLADWMPGNDGEGWSGSEPGTDPK
GTRQLWVTYSDDDGKTWSEPRNITPQVKDPDWRFLATGPGHGIQLKNGEHKGRLVFPAYYSDGGKPSAAV
IYSDDHGKTWKLGESANDKANTNEAQVVELSDGRLMLNMRNQSGGGKRAVATSKDGGETWSEVTFDPALP
EPVCQASIIRYDKGDGKDVLLFSNPASPKGRKNGTVRLSYDDGKTWPYSKVIEPGGSAYSCLTVLDDGTI
GLLYERGDAGNIVFARFPLDWLTQKK
>gnl|CDD|443532 COG4412, COG4412, Bacillopeptidase F, M6 metalloprotease family [Posttranslational modification, protein turnover, chaperones]
QYYEEQSGGRYTVDGTVTDWVKVPYNEARYGANICGGDDNGPWALVRDALNAWQIKADLADYDQWDRYDL
DGDGNFNEPDGYIDHFQIVHAGVGEEAGGGALGEDAIWSHRWYAGGNYGIPGPASNKLGTGIWVGDYTIQ
PENGGVGVFAHEYGHDLGLPDLYDTSSGGGNPVGFWSLMSSGSWLGKGEGTEPTGMGAWDKLQLGWLDYE
TVDAGQKGTVTLGNGKNAQAVRVNLPDKETTLVGPASGSKAYWSGYGDNLDNTLTRPIDLTGATSATLTF
KAWYDIEEDYDYGYVEVSTDGGATWTPLPGNVTGTPDPNGSGLGPGITGTSNGWVDLSFDLSAYAGQTVQ
LRFRYVTDGGVAEDGFYVDDIAVTADGTTVFSDDAEYGDNGWTLNGFTRTDGTYTKAYDHYYLAEWRNYI
GYDKGLAGPDWVEHMPYQDGLLVWYWDTSYGDNNVGVHPGEGLLLPVDAHPEPLYWSDGTAARTRVQIYD
AAFSLQKTDPFTLHYNGAPGYVRGLPAVPVFDDS
>gnl|CDD|443533 COG4413, Utp, Urea transporter [Amino acid transport and metabolism]
NPLLDFIRALLRGIGQVFFQNNALTGLLILAAIALASPRLGLGALLGVLIATLTARLLGFDRAEIRAGLY
GFNGALVGLALGFFFGPSPASWVLLVLGAALSALVTAALSRLLIPWGLPALTLPFVLVTWLLLLAAYKFG
GLPVSPLLPPALPAPASATNGLTLPDLVEALFKGVGQVFFQDSWVAGLLILAGLAIASRIAALLALIGSV
LGLLVALLLGAPPASIALGLYGFNAVLTAIALGGVFLKPSPRSFLYALLGAILTVFLQAALTVLFAPLGL
PVLTAPFVLATWLFLLALKLLP
>gnl|CDD|443534 COG4416, Com, Mu-like prophage FluMu protein Com [Mobilome: prophages, transposons]
MMQEIRCGHCNKLLAKAGEYGRLQIKCPRCKTLNHFKAASPPPSPDRARATKQRHRLPP
>gnl|CDD|443535 COG4420, COG4420, Uncharacterized membrane protein [Function unknown]
MAKESGELSELERRLDEPLERRIEIIRNLRERFEEDLTAGGRLADAIARFGGSWTFLILFTVFLVVWIAL
NLLAPPGLAFDPYPFILLNLVLSLQAAYQAPLILMSQNRQADRDRVRAELDYQVNLKAEAEIEYLHRKLD
ALRLALGEVATRDFERSELQQEQLLEELEERLEES
>gnl|CDD|443536 COG4421, COG4421, Capsular polysaccharide biosynthesis protein [Cell wall/membrane/envelope biogenesis]
LPPPRRLEGPVALLAGLGSGNYGHWLIDVLPRLWLLRQAGELDDIDPILVPPDLPPFQRESLALLGIPEE
KIIEIDRGPPVRVERLIVPSPLGGESGVHRVPPWLLRFLRERLLPAATPPPAPPRRIYISRRDASRRRIL
NEEELEALLEKYGFEIVDPEELSFAEQIALFAEAEVIVGPHGAGLTNLVFCRPGTKVIELFPPGYVNPYF
WLLAALLGLRYYYLLGESVGPSPDNGLHADFRVDPDALEEALAELLAD
>gnl|CDD|443537 COG4422, COG4422, Bacteriophage protein gp37 [Mobilome: prophages, transposons]
MADNSKIEWTDATWNPVTGCTKVSPGCDNCYAERMAKRLKAMGGEKYEWGFRVRLHPERLEQPLRWKKPR
RVFVNSMSDLFHEDVPDEFIDRVFDVMRATPQHTFQVLTKRPERMRELLPSLDWPPNVWLGVSVENQKEA
DRRIDHLRKTPAAVRFLSCEPLLGPLGLLDLTGIDWVIVGGESGPGARPMHPEWVRSIRDQCAAAGVPFF
FKQWGGWGPDVGKKAAGRLLDGRTWDEMPEV
>gnl|CDD|443538 COG4423, COG4423, Uncharacterized conserved protein [Function unknown]
MALNIKDPEVDRLARELAALTGESKTEAVRRALEERLARLRRERRAAPLRERLRAILERAAALPGLDDRS
ADEILGYDELGLP
>gnl|CDD|443539 COG4424, LpsS, LPS sulfotransferase NodH [Cell wall/membrane/envelope biogenesis]
MTTRPFRSYVICATPRSGSTLLCELLNATGVAGCPGEYFNPPFIPEWARGFLLGDRDRDPDEYLRAIRRA
GTTPNGVFGFKLFWDQLPRLLQRALRLLAAFPDLKFIHLTRRDKLAQAVSLVIAQQTGQWHSDADDALAP
TAPPEYDAEEIARLLEALQDFEARWEAWFARTGITPLEITYEDLAADPVEVLNRVLDFLGVDPPLAPLRP
ALKKQADEPSDEWVARFREEAEALAALD
>gnl|CDD|443540 COG4425, COG4425, Uncharacterized membrane protein [Function unknown]
MTAPRRRLRRLLRSLSFTGLLLGLLFFALSLTPSLLPRPWLFQGVLSGVSAAIGYGLGVLLAWLWRYLEL
PEPSPRARRRARWVLAAACLVVAVVFLWLAARWQNSIRALMGMPPVESAHPLLVAAVALAVFALLLLLAR
LLRRLVRWLARRLGRVLPRRVANVVGVVVVVVLVWSLVNGVLVRGALRAADSSFAALDALTEPGVEQPTD
PLRSGSPASLVSWESLGRQGRRFVASGPTAADIAAFTGRPAKEPIRVYAGLNSADTPEERAALALAELER
TGAFDRSVLVVVTPTGTGWVDPAAADALEYLHGGDTATVAMQYSYLPSWLSLLVDREYGREAGRALFEAV
YGYWSTLPEDSRPKLYVFGESLGSFGSEAAFDGLDDLGDPVDGALWVGPPFFSPLWRELTDRRDPGSPEW
LPVYRDGRVVRFANQPGDLARPGAPWGPPRIVYLQHASDPVVWWSPDLLWREPDWLREPRGPDVSPDLRW
YPVVTFLQVAADMAVATGVPPGHGHVYAEEYVDAWAAVTEPPGWTPADTERLRALLAALA
>gnl|CDD|443541 COG4427, COG4427, Uncharacterized conserved protein, DUF2332 domain [Function unknown]
MTELERLAAAFRRQAEACAAGGSPLYARLARAVADDLELLALLAGWPGDPEGDAVPLRLLGALHALVLSG
RAHELAAYYPSVGGDPDDDALWPAFRDFLLEHDDELRALLDTRTPQTNEVGRSAVLLPALLWIAARTGGP
LALLEIGASAGLNLLWDRYAYRYGGRGVVLGPADSPVRLAPAWRGPPPPLPAPPRVASRAGCDLNPLDLA
DPDDRLWLRAYVWPDQPERLARLEAAIALARADPPRLVRGDAVDWLPERLAEVPAGVTLVVFHTIVWQYL
PAETRARLLAALAEAGARARPLAWLSLEPDGVGPGAGDFALTLRLWPGGEQTTALGRADPHGRWVEWLAA
>gnl|CDD|443542 COG4430, YdeI, Uncharacterized conserved protein YdeI, YjbR/CyaY-like superfamily, DUF1801 family [Function unknown]
MNPEVPVLYFESAAEWRAWLEANHDTETGKWLVFYKKGSGKPSYTYNEAVKEALCFGWIDGVLKKLDDES
YLQRFTPRRPKSQWSRVNKERVERLIAEGRMTPAGLEAIEAAKADGRWAAYEVEELEVPEDLQAALDANP
AAKAFFEALTPSYRRAYLLWISSAKRPETRAKRIEKIIEMLARGKKLNP
>gnl|CDD|443543 COG4443, COG4443, Uncharacterized conserved protein [Function unknown]
MAEIKYEIVEEIGVLSESSKGWTKELNLVSWNGREPKYDIRDWSPDHTKMGKGITLTKEELKELKDILNE
>gnl|CDD|443544 COG4445, MiaE, tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) [Translation, ribosomal structure and biogenesis]. tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) is part of the Pathway/BioSystem: tRNA modification
MSLLTPIMLFLKCPTPPAWVEAALANLDELLIDHAHCEKKAASTAMSLIFRYPDKPELVRKMSALAREEL
EHFEQVLEIMKKRGITLGRLRADRYANGLRKLVRTSEPERLLDRLLVGALIEARSCERFALLAPHLPDEE
LAKFYRSLLRSEARHYQDYLKLARQYFDEEDVDERLEELLEAEAELIASLDPEFRFHS
>gnl|CDD|443545 COG4446, COG4446, Uncharacterized conserved protein, DUF1499 family [Function unknown]
AALRACAGTPPENLVVDGRLAPCPASPNCVSSQSADEDHDIAPLTLDGSPEEAFARLLAIIESLPGTKIV
EETEGYLEAEFTSRLFGFVDDVEFRLDPDGTVIHVRSASRVGYSDLGVNRRRIEALRAALEALGG
>gnl|CDD|443546 COG4447, COG4447, Uncharacterized conserved protein related to plant photosystem II stability/assembly factor [General function prediction only]
ADGNRLWAVGASGGILRSTDGGKTWTPLSDGLPGLSLRAVAFSDPNTVWVGTGPGGIYRSTDGGKTWTEV
NSGPDNPRLFAIAFSDPNTGYAAVGGIYRTTDGGKTWTKVSSGLPVDLNDVAFLDPGTLYAAGEGGLIYR
STDGGEYRSTDGGKTW
>gnl|CDD|443547 COG4448, AnsA2, L-asparaginase II [Amino acid transport and metabolism]
MTMAAVVLVEVTRGGLVESRHRGSAVVVDADGRVVASLGDPDAPVFPRSSAKPLQALPLLESGAADAFGL
TDEELALACASHSGEPEHVEAVRSMLAKAGLDEDALRCGPHWPLDEAARDALIRAGEGPTRLHNNCSGKH
AGMLATCVHLGWPTDGYLDPDHPLQQAIRETVEELTGEPVADATGVDGCGAPVFALPLTGLARAFARLAT
AEGGSPARATAARRVADAMRAHPELVAGTGRFDTDLMRAVPGRLVAKTGAEGVYAAALPPDGLGVALKID
DGATRAAEPVVAALLRRLGVLDAEEPAALAALARPPVLNGGGEVVGEIRPAFALAA
>gnl|CDD|443548 COG4449, COG4449, Predicted protease, Abi (CAAX) family [General function prediction only]
PLLSLILSRLLRAVRTLPSLRDWLVALLILLIYAAIALPLGFITGFLQWSPWAASPLSLLAVILILLLFP
AIGEELLFRGLLLPHPVELASGLNWWLWILLSLVLFVLYHPLNALTFYPAGRPTFLNPRFLLLAGLLGLA
CTIAYLLTGSLWPAVIIHWLVVVVWLLLLGGYEKLL
>gnl|CDD|443549 COG4451, RbcS, Ribulose bisphosphate carboxylase small subunit [Carbohydrate transport and metabolism]
MSRTQETFSYLPPLLDAEIVAQVRYLLAQGWAIGIEHADDRRFRTTYWQMWKLPMFDSTDEAEVLAELEA
CRKEHPGEYVRLIGIDPKAKRRVLEFIVQRPN
>gnl|CDD|443550 COG4452, CreD, Inner membrane protein CreD involved in colicin E2 resistance [Defense mechanisms]
METLWMKRSLLLKLLIIGLLILLLLIPLGMIRGLVRERQSRRDEAVAEIAQSWGGEQTLLGPVLVVPYTE
TVTEEDENGKKTVVREREGYLYLLPEKLNVDGDLKPEERKRGIYEVPVYTADLTLKGRFDLPDLLAALGI
DGETILWGKAYLVLGISDLRGIRGVPKLRVNGQALAFEPGTGLSDGLGSGLHAPLPLAALAAGQPLDFSF
KLNLNGSGSLSFVPLGKTTEVTLTSNWPHPSFTGAFLPDEREVTDDGFSASWQVSSLARNYPQSWTGDQL
ADEDLALSSFGVSLIEPVDVYQKSDRAVKYAILFIGLTFVAFFLFEVLKKLRIHPVQYLLVGLALVLFYL
LLLSLSEHIGFALAYLIAALACVGLIGFYLSAVLRSWRRGLLFGAVLALLYGFLYVLLQLEDYALLLGSL
GLFAILALVMYLTRKIDWYGLGAAKSKAS
>gnl|CDD|443551 COG4453, COG4453, Uncharacterized conserved protein, DUF1778 family [Function unknown]
TTATKTARINLRISPEQKALIDRAAALSGKTLTDFVLEAALEAAEEVLLDQRLIRLSEEDFEAFLAALDN
PPAPNPRLKRALKRYAPWE
>gnl|CDD|443552 COG4454, COG4454, Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction only]
MKRTLALLLALALALLATAALAAGDSHASAIGKPGDAAKVTRTITVTMGDTMRFTPDSIEVKAGETVRFV
VTNPGKLKHEFVLGTFAELAEHAKVMAKMPDMEHGDPNEVELAPGETGELVWTFTKAGTFEFACLIPGHY
EAGMTGKIVVK
>gnl|CDD|443553 COG4455, ImpE, Protein of avirulence locus involved in temperature-dependent protein secretion [General function prediction only]
MMTAEELLKAGSLDDALAALQAQVRAKPADADLRAFLFQLLCLAGDWERALTQLKLAAELDPQALPMAAL
YRQAIRAEQAREEVFAGGATPLFLGEPPEWVALLLEALQALRQGDAAQAAALRAQALELAPATPGTIDGT
AFDWIRDGDDRLGPVLEVITNGRYYWVPFSAIASLEFEPPADLRDLVWRPAELTLVDGGEGVGLIPARYP
GSPASADDALRLGRETDWQELGDGLYRGLGQRMWLTDDGEYPLLDLRELEFDAAEA
>gnl|CDD|443554 COG4456, VagC, Virulence-associated protein VagC (function unknown) [Function unknown]
RTAKLFKNGRSQAVRLPKEFRFPGDEVEIRREGDTLILRPKPKSWDSLFASLEPFSDDFMAEREQPPPQE
REEL
>gnl|CDD|443555 COG4457, SrfB, Virulence factor SrfB-related protein [Secondary metabolites biosynthesis, transport and catabolism]
MLAELTDYKQEITLIPNSGIQFLDFGLDLDARPELSGRFVRRSANGPLLRLLYDEESDKFLLPAPPGGAP
EVVDPEYSISLEQSLKLLDGVWLPLPFLRFNPPRRFDQGPDNWARVRIVELETPDDDGNTHRVTLAFDTK
LVADDQNTAYLAPTEEDVRNGASFALAWRNDEMAWFLDQTWVDGWLREVFKEFARERERRSEEDIEDALR
QFEHQAHYLNLLSLLGSQLRVPEIKIVTTTLQDIVPAIPVDLVLDVGNSRTCGILIEDHPQENDGLKQSY
ELQLRDLSRPELVYNEPFESRVEFAQARFGKEHFSVESGRRDAFVWPSIVRVGPEASRLAQRREGTEGST
GLSSPKRYLWDEDPYEQGWRFNQAYDKSDREPLATAAPLMRLINDRGEPLYQLPEDERLPVFSPHYSRSS
LMTFMLSEVLAQALMQINSPAQRLRMGHSDAPRRLRSIILTLPSAMPKPEREIFRSRMEQAIGLVWKSMG
WHPGDDDFSTPEDKEKSWVPVPEVQVEWDEATCGQLVYLYNETQVNFGGRIEEFFASLARPDKQPDGEAP
GRTLRIASIDIGGGTTDLAITDYRLDDGVGSNVKITPEQLFREGFKVAGDDILLDVIQRYVLPALQAALK
KAGVADAASLLSRLFGGEGRSDQDAVLRQQLTLQVFMPLALAILSAYEQYDPLDRSAEISATFGELLELQ
PPTDKVLDYVNQAIRREPAGAPPFDLLDVPLQIDLSDLHEAFLSGRMSICKPLRALCEVISHYDCDVLLL
TGRPSRLPGVQALFRHLQPVPPNRILPLHGYRTGGWYPFHKNGRIDDPKSTAAVGAMLCLLSLDLRLPNF
YFKAGDFQPYSTVRYLGLLDNNNTLKDENVYYRDIDLDDPDYTLDAEASFEMRGPVRLGFRQLDNERWPA
SPLYTLTINNPELARKIAGDGVLRVTLAVDKAKGRKEAGPERFEIADAELSDGTPVPLRDLRLKLNTLAD
SGSGDSHYWLDSGSVYIK
>gnl|CDD|443556 COG4458, SrfC, Virulence factor SrfC-related protein [Secondary metabolites biosynthesis, transport and catabolism]
MKPLTSSQLSQQWQAVYQGADKAIDWIDSTRQSAPRLDIEADSLILKLRRARNKARRLGDVSAKPMAVGF
FGLSQAGKSYLISALAAGENGKLETDLGGQTLDFIKHINPPGGKEATGLVTRFTRQAAVGDAAYPVELRL
LSEIEIAKILANAFFNDFDQEKVNYELDEQHIAALLKELAMRRQPEPVPGITEDDVVALWDYLNRHFGKR
QKPLDAHFWPSAIELAPYLSIDDRAQLFSLLWGEIEELTAAYIQLAHTLQSLGHAERVLAPLSVLVDESD
GGLSQANSIMNVDMLERLNTPADLPVQVRPVVDGRAGKPVELSLAELAALTAELIFPLANPPREPLFEQV
DLLDFPGYRGRLDLESIDDVKAENEEESNPLAQLLLRGKVAYLFERYTDNQEMNALVVCTASSKQSDVKD
VGPVLDRWIKKTQGETPQQRSRRKPGLIWALTMFDGRITQGLNLTEDLLKESWGGMLKLTMLERFGNFDW
MKNWDGQPFDNTFLVRKPGMKTPFIELDAEGEVAESQQPKLALLRQTFNEDEAVQRHVANPGDAWDAMLA
LNDGGMERMADYLSAEANPEVKLGRIAEQLNELQRELVENLLGNWYQPGGEDELAKKQRIAEMLLKALQT
RTGVHGELLERLLPPRDELRRLYLQQQEQQPDEANEAADSADSSEPFGIGDDIDLFSDDPPTPATPAAPA
EAAKKGHEARFARAVFRYWVNHLRNLPENEALLELLGLSKPTIELLVDELITASIRLKLEEQLSQALLET
EQAGVRREQLADRQVSRALTVLGDFVAWLGFLQIPEEQRPDSRVNRGQKIFAKPPKQASFGASQRLPKLS
DTPENYTAFYIYDWLVGLAEMIIQNAGHSAGREISPEQNEQLGRILDLIKAAQL
>gnl|CDD|443557 COG4459, NapE, Periplasmic nitrate reductase system, NapE component [Energy production and conversion]
STSTSDASTKREELRAFLFLAVVLFPILAVGLVGGYGFIVWMLQLFFGPPGP
>gnl|CDD|443558 COG4460, COG4460, Uncharacterized conserved protein, DUF4440 domain [Function unknown]
MSLMNPYIREVIDLHVLIERWFGGDAGEGALDALLARFSPDFSMVTPSGQRLDRDALGAFFRAARGARPG
LRIEIDDLEVLAEWGDGAVVRYRETQTLPGGRTVRRSTAVFRRDGGGVRWRHLHETWVAA
>gnl|CDD|443559 COG4461, LprI, Lysozyme inhibitor LprI [Defense mechanisms]
MKLRLALLLALLLAAAAAAAASFDCAKASSPVEKAICADPELSALDRRLAALYQQALAAAAAGDRAALRA
EQRAWLKQRNACGKDRACLEDAYQERIAELQAVYGLVPA
>gnl|CDD|443560 COG4463, CtsR, Transcriptional regulator CtsR [Transcription]
MANLSDIIEAYLKQLLEESGDGVIEIKRNELADRFNCVPSQINYVLSTRFTPERGYLVESKRGGGGYIRI
VKVRLDDDDDLLDHLIELIGDSISQQEAEDIIERLLEEGLITEREANLMLAALDRRTLGLPLPLRDELRA
RILKAMLLTLLYEE
>gnl|CDD|443561 COG4464, YwqE, Tyrosine-protein phosphatase YwqE [Signal transduction mechanisms]
MIDIHSHILPGIDDGAKTLEESLAMAREAVALGITKIVATPHIMPGYYDNTPETIREAVEELQEALKEEG
IPLEILPGAEVRLDPDLLELLESGELLTLGGSRYLLVELPYNSIPPYLEELIFELQLKGYTPIIAHPERY
PYLQEDPERLYELVERGALFQVNAGSLTGYFGKKVKKTAEKLLEEGLVHFLASDAHNLRHRPPRLAEALE
ALEKLFGSEKADRLLEENPRALLEGEPIE
>gnl|CDD|443562 COG4465, CodY, GTP-sensing pleiotropic transcriptional regulator CodY [Transcription]
MMSLLEKTRKINKLLQKSAGEPVDFKEMAEVLSEVLDANVYIVSRKGKILGYALLEEFECDRMEDEMLEE
KRFPEEYNEKLLKINETKANIPIDSDLCVFPVEERCLFPNKLTTIVPIYGGGERLGTLILARFDEEFTDE
DLILAEYGATVVGMEILREKAEEIEEEARKKAVVQMAIGTLSYSELEAVEHIFEELDGKEGLLVASKIAD
RVGITRSVIVNALRKLESAGVIESRSLGMKGTYIKVLNDKLLEELKKLK
>gnl|CDD|443563 COG4466, COG4466, Uncharacterized conserved protein Veg, DUF1021 family [Function unknown]
MMMPNTLAEIKKELESHVGKRVKLKANKGRKKIVEREGVLEETYPSVFVVELDQEENAFRRVSYSYSDVL
TETVELTFCDDEEKIKI
>gnl|CDD|443564 COG4467, YabA, Regulator of replication initiation timing YabA [Replication, recombination and repair]
MDKKELFDRLSELEEQLGELLKELGELKDEVAELLEENARLRIENEHLRERLEELEKKKEKKAEKDIGEG
YDNLARLYEEGFHICNLHFGSRRNDEDCLFCLSFLNK
>gnl|CDD|443565 COG4468, GalT2, Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism]
MMINQAIERLVEYAIKNGLIEEEDRIYARNRLLELLGLDEPEEPEVEEENEESLPEILDELLDYAVENGL
IEDTVTERDLFDTKIMGLLTPRPSEVNRKFWELYAESPKAATDYFYKLSKDSNYIRTDRIAKNIKWKTPT
EYGDLEITINLSKPEKDPKAIAAAKNAKQSSYPKCLLCKENEGYAGRLNHPARQNHRIIPLTLNGEDWGF
QYSPYVYYNEHCIVLSEEHRPMKIDRATFERLLDFVEQFPHYFIGSNADLPIVGGSILSHDHFQGGRYTF
PMEKAPIEEEFTLKGFPDVEAGIVKWPMSVIRLRSEDKERLVEAADKILEAWRGYSDESVDILAYTDGTP
HNTITPIARRRGGKYELDLVLRNNRTSEEHPLGIFHPHAEVHHIKKENIGLIEVMGLAVLPGRLKEELEE
VKKYLLGEKKDIEENEVLAKHAEWAEELKAKYPTLTKENVEEILKEEVGKVFERVLEDAGVFKRDEEGRA
AFKRFIESL
>gnl|CDD|443566 COG4469, CoiA, Competence protein CoiA, contains predicted nuclease domain [General function prediction only]
MLFALDENGELVSAAQDSKEELRQAKKGEEFYCPGCGSPVILKAGSKKIPHFAHKSKSSCDYFSEGESEE
HLQGKLLLYEWLQRQGIEVELEYYLPEIKQRADVLVEFGGKKIAIEFQCSPISIEELKERTEGYKSAGIE
VIWILGG
>gnl|CDD|443567 COG4470, YutD, Uncharacterized conserved protein YutD, DUF1027 family [Function unknown]
MIKIDGRQYELVENYREAFDEEAFKERYSDILDKYDYIVGDWGYEQLRLKGFYKDQNKKATFDTKISTLQ
DYLYEYCNFGCAYFVLKKVNP
>gnl|CDD|443568 COG4471, YlbG, Uncharacterized conserved protein YlbG, UPF0298 family [Function unknown]
FMMQKRQGLIVWLYSLKQAKQLRRYGHVHYVSKKMKYAVLYVDQDDIEETMEKLERLPFVKKVEPSYRPD
IKTEFENAKPDKAKEYDYKIGL
>gnl|CDD|443569 COG4472, COG4472, Uncharacterized conserved protein, UPF0297 family [Function unknown]
DETMKFNFDKEEEEDVKEILTEVYEALEEKGYNPINQIVGYLLSGDPAYITSHNNARNLIRKLERDELLE
ELVKSYLKEKG
>gnl|CDD|443570 COG4473, EcsB, Predicted ABC-type exoprotein transport system, permease component [Intracellular trafficking, secretion, and vesicular transport]
MNLNDLWKKRLSAHIKELSKYLRYIFNDHFVIVLLFLLGAGGYYYSQWLKTLPPDFPAALLVAVILGLVL
TLSPVRTLLKEADLVFLLPLEKKMKPYFKKALRYSFISQLYLLLLVLAILAPLYFQTTGLSGSSYLLLLL
LLLLLKAWNLLLEWQELRFRDGKGRRLDRLLRFILNGVAVYLLLYGAPLLALVIAVLLAVLYYYLLKKKT
KQKLLPWELLIEKEQNRMMRFYRFANLFTDVPHLKGSVKRRRYLDWLLSRIPFKQKNTYLYLYARTFLRS
GDYFGLYVRLTIIGALIIYFVPNPWVSLIVALLFLYLTGFQLLPLYTHHRTNVWTDLYPVPEEQRKKAFV
KLLRQLLIIQAIIFSLAFLLSLGDLLGALIILIGGLVFVLLFTIVYLPKRLK
>gnl|CDD|443571 COG4474, YoqJ, Uncharacterized SPBc2 prophage-derived protein YoqJ [Mobilome: prophages, transposons]
MMKTLAVTGYRSFELGIFKDDDPKIEVIKKALKKRLIELLEEGLEWVIIGGQLGVELWAAEVVLELKEEY
PDLKLAVITPFEEQEERWNEENQEKYQKILEQADFVKSVSQRPYEGPGQFKQRNQFMLDHSDGALLVYDE
ENEGSPKYFYEKAKKYGENHDYPILLITFDDLQDIAEELQENDP
>gnl|CDD|443572 COG4475, YwlG, Uncharacterized conserved protein YwlG, UPF0340 family [Function unknown]
LEQIKEQLEAALEELLEQAPLKPGQLFVVGCSTSEVLGERIGTAGSLEVAEAIFEGLLEVLKKRGIYLAF
QCCEHLNRALVVEREAAEKYGLEEVSVVPVPHAGGSMATAAYRQFKDPVVVESIQAHAGIDIGDTLIGMH
LKPVAVPVRLSVKEIGEAHVTAARTRPKLIGGERAVYEREE
>gnl|CDD|443573 COG4476, YktA, Uncharacterized conserved protein YktA, UPF0223 family [Function unknown]
SYPLDLDWSTEEIIDVVNFFSAVEKAYEKGVEREDLLEAYRRFKEVVPSKSEEKQLFREFEEASGYSLYR
VVKKAKETEKGKIKMK
>gnl|CDD|443574 COG4477, EzrA, Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning]
MMIYIIGIIVLIIALYGAGYIMRKKHYKEIDRLEERKLEIMNRPVLDELSKVKKLNLSGQTEEKFEEWRQ
KWDEIVTKQLPEIEELLFDAEEAADKFRFKKAKKALDEIEQLLDEIEEEIEEILEELEELLESEEKNREE
IEELKEKYRELRKTLLAHRHSFGPAAEELEKQLEELEPEFEEFEELTESGDYLEAREILEQLEEELNALE
ELMEEIPPLLKELQTELPDQLEELKSGYREMKEQGYVLEHLNIEKEIEQLEEQLKEALELLEELDLDEAE
EELEEIEEEIDELYDLLEKEVEAKKYVDKNQEELEEYLEHLKEQNRELKEEIDRVQQSYRLNENELEKVR
NLEKQIEELEKRYDEIDERIEEEKVAYSELQEELEEIEEQLEEIEEEQEEFSEKLKSLRKDELEAREKLD
ELKKKLREIKRRLEKSNLPGLPEEYLEMFEEASDEIEELSEELNEVPLNMDEVNRLLEEAEEDIETLEEK
TEELVENATLTERLIQYANRYRSDNPEVAAALTEAERLFREYDYEKALEIAATALEKVEPGALKRIEESY
KEEKETS
>gnl|CDD|443575 COG4478, COG4478, Uncharacterized membrane protein [Function unknown]
LKQILLSLSLPLFILSLSIAITINFSPLLYYFEIDKLNIPEDVGLSKEDLLENYSYLIDYLNGPWLGDLK
LPDFPFSERGLLHFADVKNLFLLAYLILLILLILSIIFLRRLKKKRRLWFLLRPFIITLLLPLALGVLAA
INFDKFFTLFHKLFFNNDYWLFDPATDPIINLLPEEFFLHCFILIFILFLVAAILLYILGWLLKKK
>gnl|CDD|443576 COG4479, YozE, Uncharacterized conserved protein YozE, UPF0346 family [Function unknown]
RRSFYQYLMTYRGPKKKDPKSDFANDAFLDHSFPKQSDDYDELSDYLELNGDYLGALSVFDELWEEYLER
>gnl|CDD|443577 COG4481, COG4481, Uncharacterized conserved protein, DUF951 family [Function unknown]
KYQLGDIVEMKKPHPCGSNEWEIIRTGADIKIKCLGCGHIVMLPRSKFEKKVKKVLKK
>gnl|CDD|443578 COG4483, YqgQ, Uncharacterized conserved protein YqgQ, DUF910 family [Function unknown]
KTLYDVQQLLKRFGIIIYTGDRLADLELMEDELKELYKAGLIDKEEYLKAKLILRREHRIEKKKG
>gnl|CDD|443579 COG4485, YfhO, Uncharacterized membrane protein YfhO [Function unknown]
MKKIRKKKILKKKLLLLLSFLLPLLIMLIVFAFRGIYPFGDSFLLAGDGGSQYIPFFAYLREALLSGPGS
LFYSFSFGLGGNFYGLLAYYLGSPFNLLLLLFPASFLPYAILFLTLLKIGLAGLSFYYYLKKLFKINRWA
ALIFSTLYALSGFVFANSLNIMWLDALILLPLLLLGLERLIREKKPGLYILALALSLISNFYFGYMICIF
LVLYFLYRLIIQHKKDIKSRLKLFLRFIVSSLLGGLISAILLLPTVLALLQNGRSYTEFSVSLFYEYPLF
DLLSKLFPGSFDFTQMDGLPNIYVGLLVLLLAILFFFTKKIYKKKKLRLFALLLFLFLSFSLSPLNSAWH
GFSAPQWFPYRWSFLFSFLLILLAAEALERLKEIKLKQLLIALILVIILLLILFLYEKTYEYLTLNSLLL
TLLFLALYLLLLLLRKKKKKSRVLAVLLLLLVLVELGINAYYSLGGIGYISSSEYASYYKEQQKLIDEIK
KDDSDFYRIEKTFDRTKNDPMLYGYNGISHFSSILNGNILDFLGDLGFPSESNSRYRYLGNTLLLDSLLG
VKYLISKKDTGKKDLYGFKLLDSSGNYIVYENPNALPLGFTTDNIISESKLEDLNPLDNQNALLNGLVGE
DADYSFTPAEITTVSANITTTNGRLTVKQKDGGITLTLTVPKNGDYYLYLPLKLPDKNNVTVTVNGYEIT
RKSTGRDNQLLNLGYFEKGETDTITIQLKKNGTYSLDNLGLYTLDYDALKKAAAKLKKNALTLTKFSDNK
ITGTINAKEDGYLFLSIPYDKGWKAKVDGKKVKIKKVNGGFMGVPVPKGKHTIELTYRPPGLKLGLIISI
LGLLLLILYILYFRKKKKKK
>gnl|CDD|443580 COG4487, COG4487, Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]
MNEIKCPNCGTVFKLDESLYADIVKQRRAEFEKELAERLADAAKREAALELAEAKAKAQLQEQVAEKDAE
IAELRARLEAEERKKALAVAEEKEKELAALQEALAEKDAKLAELQAKELELLKKERELEDAKREAELTVE
KERDEELDELKEKLKKEEEEKQLAEKSLKVAEYEKQLKDMQEQIEELKRKKEQGSTQLQGEVLELEFEEL
LATAFPNDYFEKVSKGSKGADYIFRVNDEAGQECGSIMFEMKRTKNWNEDWLKKLDKDRREKKAEYAVLV
SLLEPKGEYNFGIVDGMYVVRPQFFIPLITLLRNALLKSLKYKQELEGVRTKMEMLYQYLDGTNFEEQLE
AFKEAFSSMQDDFDKEYRLASKQWKKREKQIDKVIKNTEKMKGSLQGIAGNKAQDIKKLTRGTMKAKFEE
LKKAE
>gnl|CDD|443581 COG4492, PheB, ACT domain-containing protein, UPF0735 family [General function prediction only]
MKKEKKFYLVREDILPEAILKVVEAKELLESGEVKTVNEAVKKVGISRSAFYKYKDYVFPFYEMSKGKII
TLSLLLEDEPGVLSSVLNIIAEAGGNILTINQSIPIQGIANVTISIETSDMTIDIEELLEELRELEGVRK
VEILGRE
>gnl|CDD|443582 COG4493, YktB, Uncharacterized conserved protein YktB, UPF0637 family [Function unknown]
TFNGFTEEDFDVFTIEGLDERMEALRERIRPKFEALGEEFAPYLSALTGEEMFPHVAKHARRTVNPPNDT
WVAFAPNKRGYKKLPHFQIGLWEDHVFIWFAIIYESPDKEEIAERLLENLDDLKALPDDFVWSLDHTKPD
ATPLSELDDEDLEKLLERLRDVKKAEFLVGRHIPRDDALLMSGEEFLALIEETFETLLPLYKLALSVT
>gnl|CDD|443583 COG4495, COG4495, Uncharacterized conserved protein, DUF4176 domain [Function unknown]
MDKMDKLLPIGSVVRLKGGTKKLMIIGRIQQNEGEETIFDYVGCPYPEGNVGPEKTYLFNHEDIDEVVFE
GYEDEEEERFQELLKKALKELEEKKKK
>gnl|CDD|443584 COG4496, YerC, Predicted DNA-binding transcriptional regulator YerC, contains ArsR-like HTH domain [General function prediction only]
MNSKLKDEALDQLFEAILSLKDPEECYAFLEDLCTPAELKALAQRLEVARLLREGKTYREIAEETGASTA
TISRVKRCLNYGAGGYRLVLDR
>gnl|CDD|443585 COG4499, YukC, ESX protein secretion system component YukC [Intracellular trafficking, secretion, and vesicular transport]
MEEKKKTYLEDQLEYQFKKEDDRWTLTFQKSKIKLKDELELQLLKEISPEFVPKEITVTEDELIITYQPP
SNLKSFEDIKKKDRSSKLRFALNLAQLEEHLNSRLTLILHPENLVFDKNLTPYFLHRGVKESLPPYELDE
ERFLKEYKALVIALFSKKYSFDELYLGSLETAKLSPFEKKILQAETLEALLEFLEKQYEKELEAKEKNMA
KVPKKKWKIFKYLSIGLIALLVPLIIPLVYLLFFKQPFQEAYLAANAAFLKNDYSQVITTLEDYDPEKMP
YVVKYELAYSYIQTESLSEEQKENILNNITLQSDPDYLLYWIYIGRGELDEALDIARYLDDNDLIMYALI
KKREQIKNDPDLSGEEREQKLKELEAELDEYLEEYEEAKEEEEEVEEEEEKAAEEKLKQEEEKEKKEDEE
AAKAEKEDKTKETKK
>gnl|CDD|443586 COG4502, YorC, 5'(3')-deoxyribonucleotidase [Nucleotide transport and metabolism]
MKPRIAVDMDGVLADFYAAFLDIYNKEYGTNLTLEDLDGWDLWELVPPEHRERIREFLNEPGFFRDLPPI
PGAQEVLKELSDKYEVYIVTAAMEFPNSLEEKYEWLDEHFPFIPWQNIIFCGDKSLVGGDYLIDDNPKNL
EEFKGKGILFDAPHNRHITGYPRVNNWKEVEALLLSL
>gnl|CDD|443587 COG4506, YwiB, Uncharacterized beta-barrel protein YwiB, DUF1934 family [Function unknown]
KKPVLISIKSTQRQGGEEETIELETEGKLYKKGGSYYLRYEESEESGMEGTTTTLKIEEDRVTLIRSGAV
NMRQVFEPGKRTEGQYETPYGSLEMETKTKKLEVDLTEKGGEIEIEYDLELNGQLVGNYKLEITIK
>gnl|CDD|443588 COG4508, Dut2, Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily [Nucleotide transport and metabolism]. Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily is part of the Pathway/BioSystem: Thymidylate biosynthesis
MNLKKLFEMQKELDDRIEEEHGLEGEDLFDKKYLALLVELGELANETRCFKFWSKKPPSPKEVILEEYVD
GLHFILSLGLELGYDLLELAAPMEAELKSLTEQFLDVYEAITAFAKNLTKKNYQELFALFLQLGYALGFT
EEDIEKAYLGKNELNHFRQDNGY
>gnl|CDD|443589 COG4509, COG4509, Uncharacterized conserved protein [Function unknown]
MKKKKIIRRILLLLALAVLLFSAGLIGDIYLEYKEADKEYEELAQVVVKEESEEAEEDEELRVDFDALRE
INPDIVGWIYIPGTEIDYPVVQGDDNDYYLHHDFDGEYSRAGSIFLDYRNKPDFSDRNTIIYGHNMKDGS
MFGDLKKYKDQDFFDEHPTFYIYTPEGTYTYEIFAAYVVDTDFDYYRTDFSDDEDFEAFLDEIKKRSVVK
TDVDVTKADKILTLSTCSYEFDDGRLVVVAKLVKE
>gnl|CDD|443590 COG4512, AgrB, Accessory gene regulator protein AgrB [Transcription, Signal transduction mechanisms]
MMIEKLADKIANYLKKELNLDEEDEEVLKYGLELILGALIKIILILLIALLLGVLPETLIALLAFGLLRL
FSGGAHAKTYLRCLIFSLLIFLLIGLLAKYLPPILLIVLIILIFIISLLLIIKYAPVDTENKPITSKKRR
KKLKKLSIIILLILFLISLLYLTGNNIISLAILLGILLQAFTLTPLGYKLIRKLDNIL
>gnl|CDD|443591 COG4517, COG4517, Uncharacterized conserved protein, DUF1820 domain [Function unknown]
MAKKPIYRVTFLNQGKVYELYAREVYQSDLYGFIEIEEFVFGERSSLVVDPSEEKLKTEFAGVKRSYIPM
HAIIRIDEVEKEGTAKISELDSGGKVTPFPSPPYTPGK
>gnl|CDD|443592 COG4518, gp41, Mu-like prophage FluMu protein gp41 [Mobilome: prophages, transposons]
MAVMTFELKHGLKVGEETQREVTLRELTAGDVIDAQLASERVVITNNGPVLYKSPALMGYELLRRQIASI
GKIQGPLSLKQLKKLHPEDLELLQAKADELDAALASEEVADRGRSDAAGG
>gnl|CDD|443593 COG4519, COG4519, Uncharacterized conserved protein [Function unknown]
MSISKTNPSFYRRLYLAWLIDSGRPNVPALMEATGMPRRTAQDTLKALPGLGIECEFVQDGVRNNDGYYR
ISDWGPIDRAWVAEHLAEIAAALGYP
>gnl|CDD|443594 COG4520, LipA17, Surface antigen [Cell wall/membrane/envelope biogenesis]
MKKRKLVVALAAALALAGCATTSNKEQVGTVLGALAGGLLGSQIGGGKGRLAATIAGALLGALIGGEIGA
SLDESDRAAAAEAEYRALETAPSGQPVSWRNPDTGNSGTVTPTRTYQVGGQYCREYTHTVTIGGRTETAR
GTACRQPDGSWQIVS
>gnl|CDD|443595 COG4521, TauA, ABC-type taurine transport system, periplasmic component [Inorganic ion transport and metabolism]
MKFKRLLLLAALALAGCALAAAAAAAAKEVTIGYQTIPNPELVAKADGALEKALGAKVNWRKFDSGADVI
TALASGDVDIGSIGSSPFAAALSRGLPIEVIWIADVIGDAEALVVRNGSGITSPKDLKGKKIAVPFGSTS
HYSLLAALKHAGIDPSDVTILNMQPPEIAAAWQRGDIDAAYVWDPALSELKKSGKVLITSAELAKWGAPT
FDVWVVRKDFAEENPDFVAAFLKVLADAVADYRADPAAWPAAKAIAKLLGADPEDAPAQLAGYTFPTAAE
QLSADWLGGDGGAAKALKDTADFLKEQGSIDAVLADYSGYVNPSYLEAALKM
>gnl|CDD|443596 COG4525, TauB, ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]
MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP
VTGPGADRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMR
QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSP
GPGRIVERLELDFSRRFLAGEDARAIKSDPAFIALREELLDIIFAQEEAEAA
>gnl|CDD|443597 COG4529, YdhS, Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]
MTGARKRIAIIGGGASGTALAIHLLRRAPEPLRITLFEPRPELGRGVAYSTDSPEHLLNVPAGRMSAFPD
DPDHFLRWLRENGARAAPAIDPDAFVPRRLFGEYLRERLAEALARAPAGVRLRHIRAEVVDLERDDGGYR
VTLADGETLRADAVVLATGHPPPAPPPGLAAGSPRYIADPWPPGALARIPPDARVLIIGTGLTAIDVVLS
LAARGHRGPITALSRRGLLPRAHPPGAPLPLKFLTPEALEELPLFFAARTARDLLRALRADLAEAEAGGV
DWRAVIDALRPVLQALWAALSAEERRRFLRHLRPYWDVHRHRMPPESAARLLALIAAGRLEVLAGRLEDI
EAAEGGFVVTGAGDGETLEVDVVINATGPEPDLRRDADPLLRSLLARGLARPDPLGLGLDVDPDGRVLDA
DGRASPRLFALGPLARGTLWETTALPEIREQAAALARRLLASLAEA
>gnl|CDD|443598 COG4530, COG4530, Uncharacterized conserved protein [Function unknown]
MAKPELGTKRTCPSCGARFYDLNKDPIVCPKCGTEF
>gnl|CDD|443599 COG4531, ZnuA, ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion transport and metabolism]
LASAAAAAAPRVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLE
PFLEKPLETLAPDAKVVELLELPGLTLLPFREGGDFEHHDHHDEHHHHHHHHDDHHDHHHGGYDPHLWLS
PENAKAWAAAIADALSELDPENAATYQANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRF
GLNALGAITLNPEIQPGAKRLAEIREKLKELGAVCVFAEPQFNPALVETVAEGTGVRTGVLDPLGADLEP
GPDLYFQLLRQLADSLASCL
>gnl|CDD|443600 COG4533, SgrR, DNA-binding transcriptional regulator SgrR of sgrS sRNA, contains a MarR-type HTH domain and a periplasmic-type solute-binding domain [Transcription]
MRSLRLLQQFQRLWQHSGGQPQETTLQELAELLFCSRRHVRTLLNQMQEAGWLSWQAEAGRGKRSRLTFL
YTPEELQQQRAEQLLEQGKIEQALQLVGLDPDALRQLLQSHLGGSWRQGRPILRIPYYRPLENLLPGTPL
RRSEQHLARQIFSGLTRINEENGEPEPDLAHHWQQLSPGLHWRFYLRPALHFHNGRELTAEDVISSLERL
RALPALRPLFSHIARITSPHPLCLDITLHQPDYWLAHLLASVCAMILPPEWQTLPDFARPPIGTGPFRVV
ENSPNLLRLEAFDDYFGYRALLDEVEIWILPELFEQLLSCQHPVQLGQDETELASLRPVESRLEEGCYYL
LFNQRSGRLSDAQARRWLSQLIHPIALLQHLPLEYQRFWTPAYGLLPGWHHPLPAPEKPVPLPTKLTLAY
YEHVELHAIAQALQELLAQQGVELEIRFYDYKEWHGGAQLAKADLWLGSANFGEPLEFSLFAWLREDPLL
QHCLSEDQFAHLQATLDAWRQQEDLTQRLLALEEWCQQLMREGWITPLFHHWLQLSGQPSVRGVRLNTLG
WFDFKSAWFPPPEP
>gnl|CDD|443601 COG4535, CorC, Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion transport and metabolism]
MSDDRPSSGSSKRSWLERLSQLFSGEPEDREELLELLRDAEERELIDADTLSMIEGVLQVSELRVRDIMI
PRSQMVVIDIDQPLEEILPVVIESAHSRFPVIGEDRDEVIGILLAKDLLRYLAQDAEEFDLRDLLRPAVF
VPESKRLNVLLREFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQIVGEIEDEHDEDEDEDNIRPLSDGSYR
VKALTPIEDFNEYFGTDFSDEEFDTIGGLVAQEFGHLPKRGESIEIDGLRFKVLRADSRRIHLLRVTRLP
PAAEPDAE
>gnl|CDD|443602 COG4536, CorB, Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion transport and metabolism]
MDDISLSLLIGILVLLLLLSAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGN
NLVNILASSLATVIAIRLFGDAGVAIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLY
PLVWLVNLIVRGLLRLFGVKPDADASDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIM
VPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYRGDIDNIVGVLHVRDLLRALRKGDLSKEDLRKIAREP
YFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILEEIVGEITDEHDPDAEEIRPQEDGSYL
VDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFEILQVQDNRIKTVRIRPLP
>gnl|CDD|443603 COG4537, ComGC, Competence protein ComGC [Mobilome: prophages, transposons]
MKKKKRKLKKEKGFTLIEMLIVLLIISILLLIAVPNLTKQRETAQEKGCEANIKMVQSQVELYELDHGTY
PASLEELVDEGYLKEKQPTCPNGGEYTIDSNGEVVASN
>gnl|CDD|443604 COG4538, SnoaL, Uncharacterized conserved protein, contains SnoaL-like domain [Function unknown]
ATMTPEDVVQRQLDAYNARDIDAFLATYADDAEVYRFPGTLLAKGREAIRERYAERFANEPDLHAELVSR
IVLGNKVIDHELVTGLFGGGPVEVVAIYEVEDGLIARVWFIRG
>gnl|CDD|443605 COG4539, MPO1, 2-hydroxy fatty acid dioxygenase MPO1 (alpha-oxidation of fatty acids) [Lipid transport and metabolism]
MRSLDDLLAEYAEYHRNPTNIATHFIGVPLIVFSVLALLWRIPLPVGGLPLTWATLAALAALLYYLRLSL
RLGLGMLLLLALCLLLAELLAAALPTALWLWIALGLFVVGWIGQFIGHKIEGKKPSFLDDLQFLLIGPLF
VLAELLFALGLRY
>gnl|CDD|443606 COG4540, gpV, Phage P2 baseplate assembly protein gpV [Mobilome: prophages, transposons]
RLANLIRTGTVAAVDADPGRVRVRTGDLLTDWLPWLTPRAGGVRDWWPPSVGEQVLLLSPGGDLEDGVVL
PGLYSDADPAPSDSPDAHVTRFPDGAVIEYDRATGALTVTGIGTATVTASGSVTLTAPTVTLDAPVVTIT
GNVTVSGDVTAGGVSLNNHTHGGVQSG
>gnl|CDD|443607 COG4541, COG4541, Uncharacterized membrane protein [Function unknown]
LDPGTLLAILAMAAVTYLTRIGGYLLLRRVPLSPRVEAALEALPGAVLIAVVAPAAVSGGPAELLALAVT
ALVALRRLSLLPAVLAGVAAVALLRALLG
>gnl|CDD|443608 COG4542, PduX, PduX protein involved in propanediol utilization and related proteins [Secondary metabolites biosynthesis, transport and catabolism]
MTMGTARCPGSCGELLQGWIGGREFLVTCPIDLYSTVTVEPGPGGIPAERPKARRAAELTLEHLGLPPLG
GRIELRSDIPVGKGMASSTADIAATARAVARALGKELSPEELARLAVAIEPTDSTMFPGLVLFDHREGRV
LEPLGPLPPLDILGLDSGGTVDTLAFNRRDLAELNRAEEPEIERALALLREALRTGDLALLGEAATLSAR
ANQRILPKPELEELLALAEELGALGVNVAHSGTVLGLLFDPGDHDVEKLAEALRRRLLRLGYPRIGLVRI
INGGIR
>gnl|CDD|443609 COG4544, COG4544, Uncharacterized conserved protein [Function unknown]
MSAARTALAALRRRIWRGEGLAAAARAVLPTGFAALDAALPGGGLPRGALHEILGPAPGIGELGLLLPLL
ARLAQAGGPVLWIAPPYDLYAPGLAAAGLDPERLLLVRARRPADALWAAEEALRSGACGAVVAWLERLDL
TASRRLQLAAEAGGVLGFLLRPARAAGQPSAAALRWRVSPAPSAGRPRWRVELLKRRGGPPGSWILEWDD
AGLSLALAAALADRPAAARA
>gnl|CDD|443610 COG4545, COG4545, Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones]
MKLILYGSELCPDCAPAKEELKELGIDYEFVDITESLANLKEFLKLRDTRAAFDDAKANGYIGIPCLVLE
DGEITLDLEELLDFFGP
>gnl|CDD|443611 COG4547, CobT2, Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]. Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MMPKESPAEPFKRALAATLRAIAGDPELEVSFSADRPGLSGDRARLPEPPRRLTAEEVAIARGAADALAL
RLRHHDAALHARLAPQGPEARAVFDALEQARVEALGARRMAGVAANLDAMLEDRYRRAGYARITDRADAP
LADALALLVRERLTGRPPPPSARKLVDLWRDWIEEKAGADLDRLAELLDDQAAFARAVRDLLRDLDLAEE
LGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAEDAEASGDDAEEGESEAAEAESDEMAEEAEG
EDSEEPGEPWRPNAPPPDDPADPDYKVFTTAFDEVVAAEDLCDPEELDRLRAYLDQQLAHLQGVVSRLAN
RLQRRLMAQQNRSWEFDLEEGILDAARLARVVADPTQPLSFKQEKDTEFRDTVVTLLIDNSGSMRGRPIT
VAAICADILARTLERCGVKVEILGFTTRAWKGGQSREKWLAAGKPANPGRLNDLRHIIYKSADAPWRRAR
RNLGLMMREGLLKENIDGEALLWAHNRLLARPEQRRILMVISDGAPVDDSTLSVNPGNYLERHLRQVIEE
IETRSPVELLAIGIGHDVTRYYRRAVTIVDAEELGGAMTEQLAELFDE
>gnl|CDD|443612 COG4548, NorD, Nitric oxide reductase activation protein [Inorganic ion transport and metabolism]
ALLLAAELRLLLLLLLAARALLAAALAALAAAAEALAAAALLLELLLALLAALRLALLREAAARALALLL
GALRLAALLSAGLLELALDALPLGRAEPEADAADALDALRDERALDAAADELGDEAPEALGEEPEAPDAA
ASELSAAGYPEWDYRKQRYRPDWCTVLERRPPEGDPAFLDATLARHRRLIRRLRRQFEALRPQRVRLRRQ
EDGDELDLDAAIRALADRRAGGEPDPRIYMRRRRKERDLAVLLLLDLSLSTDAWVGSGRRVLDVEREALL
LLAEALEALGDPFAIYGFSSDGRHRVRYYRIKDFDEPYDDAVRARIAGLEPGYYTRMGAAIRHATALLAA
QPARRRLLLVLTDGKPNDIDVYEGRYGIEDTRQAVREARRAGIHPFCITIDPEADDYLPRIFGRGGYTVI
DDVERLPERLPQLYRRLTR
>gnl|CDD|443613 COG4549, YcnI, Uncharacterized conserved protein YcnI, contains cohesin/reeler-like domain [Function unknown]
MKRSLLRAAAALAAAAAAALLAAGAASAHVTVEPKEAAAGSYYKLTFRVPHGCDGAPTTKVEVQLPEGVT
SVKPMPKPGWTVEVVKGKLAKPVDVHGTEVTEAVTEVTWTADGGLPDGQFDEFVLSAGLPDDGTTLYFPA
VQTCSDGEVVRWIEIPAAGQDEPEHPAPVLTLTAAAAAG
>gnl|CDD|443614 COG4550, YmcA, Cell fate regulator YmcA, YheA/YmcA/DUF963 family (controls sporulation, competence, biofilm development) [Signal transduction mechanisms]
MLYSKDEILAKAKELAEMIAETEEVERFKQAEAKINENQKVQELIAEIKALQKQAVNFQHYGKPEALKKA
EAEIDALQEELDEIPIVQEFKQSQVEVNDLLQLVTHTISNTVTDEIEVETGGDVLDGETGGCGCG
>gnl|CDD|443615 COG4551, COG4551, Predicted protein tyrosine phosphatase [General function prediction only]
MMNVLFVCSRNRWRSPTAEQVFRNHPGVEVRSAGTSPDARVPVTAELIEWADVIFVMEKKHRNRLSKRFG
RLLKGKRVICLDIPDDYQFMDPELVELLESKVPPYLRLL
>gnl|CDD|443616 COG4552, Eis, Predicted acetyltransferase [General function prediction only]
MEIRPLTEDDLDAFARLLAYAFGPEPDDEELEAYRPLLEPGRVLGVFDDGELVGTLALYPFTLNVGGARV
PMAGITGVAVAPEHRRRGVARALLREALAELRERGQPLSALYPFEPGFYRRFGYELAGDRRRYTIPPESL
PLRPDAPGRVRRVDPDDAELLAALYERFARRRPGALDRDEAWWERVLRDLGGEPLRAAVHYDEDGEPDGY
VLYRVKDGGDGGTLEVRELVALTPEARRALWRFLASHDSQVDRVRWRLPVDDPLPLLLPDPRAAKTTIRP
GLMLRIVDVPAALEARGYPAGDGDLVLEVTDPLLPWNAGRFRLEVDDGRATVERTDAEADLTLDIRALSA
LYLGGVSPAALARAGRLTEGDPEALAALDALFPGRAPYLSDYF
>gnl|CDD|443617 COG4553, DepA, Poly-beta-hydroxyalkanoate depolymerase [Lipid transport and metabolism]
MLYQLYELQRAALAPARAAADAAARLLSNPLNPLSYTPGGRRLAAALELFERLTRRYGKPEFGIDSVTVD
GREVPVTEEVVLEKPFCRLLHFKRDLDGGAKPQPKVLIVAPLSGHYATLLRGTVETLLPDHDVYITDWHD
ARDVPLSEGRFDLDDYVDYVIEFLRHLGPDTHVVAVCQPTVPVLAAVALMAADGDPAQPRSMTLMGGPID
TRVSPTAVNDLATEKPLEWFERNVIHTVPAPYPGAGRRVYPGFLQLTGFMSMNLDRHVKAHWDLFKHLVK
GDGDSAEAHRDFYDEYLAVLDLTAEFYLETIETVFQEHALPKGELTHRGRPVDPSAIRRTALLTVEGELD
DISGVGQTEAAHDLCSGLPPDMKRHHLQPGVGHYGVFNGRRWREEIYPRVRDFIRAHAAAAA
>gnl|CDD|443618 COG4555, NatA, ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism]
MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR
EARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKK
VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV
VAQGSLDELREEIGEENLEDAFVALIGSEEGEA
>gnl|CDD|443619 COG4558, ChuT, ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism]
MKRLALALLLLALAALAAGASVAAAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVG
YMRQLSAEGILSLKPTLVLASEGAGPPEVLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGE
ALAARLEADLAALAARVAAIGKPPRVLFLLSRGGGRPMVAGRGTAADALIRLAGGVNAAAGFEGYKPLSA
EALIAAAPDVILVMTRGLESLGGVDGLLALPGLAQTPAGKNKRIVAMDDLLLLGFGPRTPQAALALAQAL
YPAAA
>gnl|CDD|443620 COG4559, COG4559, ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]
MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSP
WELARRRAVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQ
RVQLARVLAQLWEPVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRI
LLLHQGRLVAQGTPEEVLTDELLERVYGADLRVLAHPEGGCPQVLPRA
>gnl|CDD|443621 COG4564, COG4564, Signal transduction histidine kinase [Signal transduction mechanisms]
TKLLLLLLLALLALAALSLETLRQALLEERKAELRALVELAVSIIAALYAAGELSEEEAKEQALAALRAL
RFGGDGYFFVYDYDGTMLAHPINPELVGKNLLDLKDANGKYLIRELIEAAKKKGGGFVEYLWPKPGSGKP
EPKLSYVKKFPPWDWVIGTGVYLDDIEAAFAAAALELLLLLALLLALALALLLLVLAALAGLLLASALEG
ELNLAGALAALLLAAAAELLAALLLIGAAAGALLALAEAVAAVLAEALAAAAAAAAASAAASSAALAAAA
AEAEAALAASEASAAAALAAAAAAAAAAAAAAAAAEAAAAAAAAAAAAAAAAASVADVAALAAAAAAAAA
IAALAAAAAAAAAAAAAAAAIAAAAAAAAAAAAAAAAAAAEAAAAAAAAATAAAALEAVAAAAAAAAAAA
AAEAAAAEVEAAAAITAIILEAAAAAAAAIEAEEAAAVAAAAALAAEAAAAAAAAAEAAAAAAAAEAASA
VVSAAAAAAAAGAAAALALA
>gnl|CDD|443622 COG4565, CitB, DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms]
MKMIRVLIVEDDPMVAELLRRYLERLPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRE
LRARGPDVDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEEDLPEA
>gnl|CDD|443623 COG4566, FixJ, DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription]
TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGS
PLPVIFLTGHGDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRAELRARLASLTP
REREVLDLVVAGLSNKQIARELGISPRTVEVHRANVMEKLGARSLAELVRLALALG
>gnl|CDD|443624 COG4567, COG4567, DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription]
SAEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEAL
RERDPDARIVVLTGYASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPPENPMSLDRLEWEH
IQRVLAECDGNISATARALGMHRRTLQRKLAKRPPRR
>gnl|CDD|443625 COG4568, Rof, Transcriptional antiterminator Rof (Rho-off) [Transcription]
NEEYQPISCDDYDYLEIACLRRYPVKLTLKNGETIEGKARDTLTRKKVEYLVLETDGETRELRLDHIASF
SALELGPHFSTVVFSPS
>gnl|CDD|443626 COG4569, MhpF, Acetaldehyde dehydrogenase (acetylating) [Secondary metabolites biosynthesis, transport and catabolism]
MMEKLKVAIIGSGNIGTDLMYKLLRSEHLEPVLMVGIDPESDGLARARRLGVATSAEGIDGLLAAPDDID
IVFDATSAKAHARHAPLLREAGIRAIDLTPAAIGPYVVPPVNLDEHLDAPNVNMVTCGGQATIPIVAAVS
RVAPVEYAEIVATIASKSAGPGTRANIDEFTETTARAIEEVGGAKRGKAIIILNPAEPPLIMRDTVYCLV
EDDADEDAIRASVHEMVAEVQAYVPGYRLKQEPQFDGNRVSVFLEVEGAGDYLPAYAGNLDIMTAAAVRV
AERLAQRLLAGEAAA
>gnl|CDD|443627 COG4570, RusA, Holliday junction resolvase RusA (prophage-encoded endonuclease) [Replication, recombination and repair]
MMIKFTLPGPPSPKGRPRTKRGRRYTPEKGKAYRNLVALAARQQMPKKPLEGPVAVEIKFYFPPDRRKPD
LDNLLKAILDALTGAGVWKDDSQVVDLIVEKRYDDKGPRVEVEIEELEEE
>gnl|CDD|443628 COG4571, OmpT, Outer membrane protease [Cell wall/membrane/envelope biogenesis]
MKKKLLVALFLLAPLALPALANAATVEPEFTPDSVSFSLSLGVLSGESKEYVYDPDGGRKLSQLDWKIDN
APIIKGGLSWDPLPWLSLGASGWTTLGSGSGYMDDYDWLNPGQTDWTDWSSHPKTRLNYANEFDLNAKGW
LLKENNYSLGVLAGYQEDRFSWTARGGSYIYSDNGFRDDVGTFPDGEKGISYKQRFKVPYIGLTGSYRYG
NWEFGGLLKYSPWVRARDNDHHYLRDLTFKDKFKNSNYYSLSLNAGYYVTPNLKFFVEASYSRYTEAKGD
TTIYDLTTGTSSYGGDAAGIDNYSYTVSLGLKYRF
>gnl|CDD|443629 COG4572, ChaB, Cation transport regulator ChaB [Inorganic ion transport and metabolism]
MPYNSPSDLPESVRSHLPEHAQEIFREAFNSAWEEYKDPEDRRGDESREEVAHKVAWAAVKKKYEKDEGG
KWSKK
>gnl|CDD|443630 COG4573, GatZ, Tagatose-1,6-bisphosphate aldolase non-catalytic subunit AgaZ/GatZ [Carbohydrate transport and metabolism]
NPLLDLVARHKAGEPVGIYSVCSAHPLVIEAALRRALEDGSPVLIEATSNQVNQFGGYTGMTPADFRDFV
LGIADEVGFPRERLILGGDHLGPNPWQHLPAEEAMAKAEELVAAYVAAGFTKIHLDCSMSCAGDPVPLSD
EVVAERAARLAAVAEAAAREAGGEAPVYVIGTEVPVPGGAQEALDELAVTTPEAARATLEAHRAAFAAAG
LEDAWERVIALVVQPGVEFDHTNVIDYDPEKARALSAVLEDHPGLVFEAHSTDYQTPEALRALVRDHFAI
LKVGPALTFALREALFALDAIEDELIPAEQRSNLREVLEQVMLAQPGYWQKYYHGDEAEQRLARHYSYSD
RIRYYWPDPEVQAAVERLLANLEGVPIPLPLLSQYLPAQYERVREGELAPDPRALVLDKIRDVLRDYAAA
CGP
>gnl|CDD|443631 COG4574, Eco, Serine protease inhibitor ecotin [Posttranslational modification, protein turnover, chaperones]
MKKLLLALASLLAAASASANADAAAQPLEDLAPFPAAEKGMVRHVIQLPPQENENDFKVELIIGKTMEVD
CNRHFLGGELEEKTLEGWGYDYYVVSKVGGPASTLMACPDQPKREAFVTLGGDPALVRYNSKLPIVVYVP
KGVEVRYRIWKADDEIQPAVKK
>gnl|CDD|443632 COG4575, ElaB, Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD/DUF883 family [Translation, ribosomal structure and biogenesis]
MANTKTTTSVEDSKEDLEADLKALVDDLEELLKSTADDAGEKAAELREKAEAALDEARERLSEAEDAAVE
RAREAADAADDYVHENPWQSVGIAAGVGLLLGLLLARR
>gnl|CDD|443633 COG4576, CcmL, Carboxysome shell and ethanolamine utilization microcompartment protein CcmK/EutM [Secondary metabolites biosynthesis, transport and catabolism, Energy production and conversion]
MQLARVIGTVVATRKHPSLEGLKLLVVQPLDLDGEPTGEPVVAVDTVGAGVGEWVLVVSGSAARQAFGDK
DAPVDAAIVGIIDEVEVDGD
>gnl|CDD|443634 COG4577, CcmK, Carboxysome shell and ethanolamine utilization microcompartment protein CcmL/EutN [Secondary metabolites biosynthesis, transport and catabolism, Energy production and conversion]
MGKALGLIETKGLAAAIEAADAMLKAANVELVGYEKIGSGKVTVIVRGDVAAVKAAVDAGAAAAERVGEL
VSSHVIPRPHPEVEAA
>gnl|CDD|443635 COG4578, GutM, DNA-binding transcriptional regulator of glucitol operon [Transcription]
MSMWIALILLAALAWLLQLALGWWQIRRFNRAFGELRNKGRVGIGRSKGRFKPGVIVLLAVDRNGRVVDA
LIMKGVTVFARFKPLEELEGLDLDEIEPDLIFPKDKLLAKALLAALEQIDRVRAGKE
>gnl|CDD|443636 COG4579, AceK, Isocitrate dehydrogenase kinase/phosphatase [Signal transduction mechanisms]
MFPPMSSALAQRIAQTILDGFDAHYRLFREITARAKQRFEQADWHGVQRASRERIELYDERVRETVARLR
QELGADALDRELWQQVKLAYIGLLTDHPQPELAETFFNSVFCRIFHRRYFDNDFIFVRPAISTEYIESDR
PVYRSYYPADGGLRATLRRILADFPFALPFEDLERDVRLIARALRERLGARLRLGANFQIQVLNSLFYRN
KGAYLVGRIINGDGEIPFVLPLLHNEKGGLYVDAVLTDEDDISILFSFARAYFMVDMEVPSAYVQFLRSL
MPRKPRAELYTAIGLQKQGKTEFYRDFLHHLAHSSDQFIIAPGIKGMVMLVFTLPSYPYVFKVIKDRFAP
PKDVTREQVKEKYRLVKQHDRVGRMADTQEFSNVAFPRARFSPELLAELRKEAPSLLEEDGDELVIKHLY
IERRMTPLNLYLEEASDEQAEAAVEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEIEYLTD
CNFRRIPPPRNPEDEMSSEPWYSVGPNDVFPEEFGTFLLGDPRVRAAFMEHHGDLLDAAYWQGLQQRIRA
GHVEDVFPYPRERRFRRRY
>gnl|CDD|443637 COG4580, LamB, Maltoporin (phage lambda and maltose receptor) [Carbohydrate transport and metabolism]
MKKMKLLTLALAVAAALLAAQAQAVDFHGYLRSGIGASSDGGEQQCFQLPGAGSKYRLGNECDTYAELGL
GQELYKEDGKTFYVDSMLAYSNDQSNDWESTNGDDGDFALRQAYVQAKGLIPALPGATFWAGKRYYQRHD
VHINDFYYWNISGPGAGIENIDLGFGKLSYAWTRNDENDGSNSGDQDVNVNRHDVRLAGIKVNPGGKLEL
GVDYGRANGTDGQKDAKNGWMLTAEHTQGNFLGGFNKLALQYGTGAGALQGLGGTGDTSADNDAKSWRVI
DHGVWQLTDRFSGMYVAVYQKDDDRDDGDGQTWYSVGVRPVYAWTENFKLLLEVGYDRVKPQDGDTRRLT
KFTLAPTWSAGPGFWSRPELRLFATYAKWNEAAQGAATGTFGGDTSGVTFGVQVEAWW
>gnl|CDD|443638 COG4581, Dob10, Superfamily II RNA helicase [Replication, recombination and repair]
MTLSPARADARLEALADFAEERGFELDPFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALARGRR
SFYTAPIKALSNQKFFDLVERFGAENVGLLTGDASVNPDAPIVVMTTEILRNMLYREGADLEDVGVVVMD
EFHYLADPDRGWVWEEPIIHLPARVQLVLLSATVGNAEEFAEWLTRVRGETAVVVSEERPVPLEFHYLVT
PRLFPLFRVNPELLRPPSRHEVIEELDRGGLLPAIVFIFSRRGCDEAAQQLLSARLTTKEERAEIREAID
EFAEDFSVLFGKTLSRLLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTK
LSKFDGERHRPLTAREFHQIAGRAGRRGIDTEGHVVVLAPEHDDPKKFARLASARPEPLRSSFRPSYNMV
LNLLARPGLERARELLEDSFAQFQADRSVVGLARRARELERALAGVVERLACDLGDLQEYFALRQPLSPL
EALERESPAYALDVVSVPEATLEDPRPVLLAQDRRARGEAAAAMKAAIEYDERMERLEEVLRPHPLHECP
LERAFELYRETHPWVRDIELRPKSVARDFDRFCELLREYGYLDDLTLTSEGLLLRYLYDAAEALRQGVPD
DLDPEELAALISWLVEEVRRVDSSEWERLPSPANRRAFVLVNALFRRLELLERRHGLPELDPGLAGAWAS
GADLAEVLDATDLDAGDFVRWVRQVIDPDPELRRTARAAVDLIRRGVVAYS
>gnl|CDD|443639 COG4582, ZapD, Cell division protein ZapD, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning]
STMILYEYPLNERIRTLLRLEFLFQQLKHFLAGDDPWDHHAALRTLFEILDVLERADLKSELLKELERQK
QKLEALRGNPGVDEEALDALLDELDQLSAALRALAGKIGQSLRENEWLMSIRQRLSIPGGTCSFDLPAYH
YWLHQPPEQRRQDLQQWLAPLLPLRDALTLVLRLLRESGRPRKVTAENGFYQQNLGGRPAQLLRVRLDAE
LGLYPEISGNKYRFAIRFMPLDSEERPRQVEEDVPFELACCAL
>gnl|CDD|443640 COG4583, SoxG, Sarcosine oxidase gamma subunit [Amino acid transport and metabolism]
GVTLREVPPLGLVSLRARPGQEALAAALKAALGLALPAPPRVAAAGGRAALWLGPDEWLLLAPYGAAEDL
AAALAAALAGLHAAVVDVSDGRTVFELSGPRARDVLAKLCPLDLHPRAFPVGAAARTVLAHVGVVLWRTG
EDRFRLLVRRSFADYLWHWLEDAAREYGA
>gnl|CDD|443641 COG4584, COG4584, Transposase [Mobilome: prophages, transposons]
MLTMEQIREIRRLLREGLSIREIARELGISRNTVRKYLRRAEEWPELYPRRRPRPSKLDPYKEYIDEWLE
EGPRVTAKRIWEELKEEHGYTGSYSTVRRYVRRLRPEYPKEAFVRLEHPPGEQAQVDWGEATVPPITGER
RKVYVFVAVLGYSRYKYVEAYPSQTQEDLLEAHVRAFEFFGGVPREIVYDNLKTAVTKADRGEPVLNERF
LAFAAHYGFEPRPCRPRRPKEKGKVENAVGYVRRNFLAPRPRFTSLEELNAALLEWLERVANRRIHGTTG
ESPAERFAEEEEALLPLPPPPPPAVRYETVRVVKDDVVVVDGNRYSVPPYSVGRRVVVVVVVDRVVVIVV
GEVVAAHHRRRHRRGKRRDPPHYLLPLLLRPRAAPPAAALAAALLAEAPEELRLLLLALLRARGRLARLL
LLLLLLLLLELAAAAAAAAAALAAALAALLLSLLRLARLADLEPLLLLQPLPALALPAAPLTLR
>gnl|CDD|443642 COG4585, ComP, Signal transduction histidine kinase ComP [Signal transduction mechanisms]
LLALALLGALALLVGALLGLLLALVLLRARRAERAAELERELAARAEEAREEERRRIARELHDGVGQSLS
AIKLQLEAARRLLDADPEAAREELEEIRELAREALAELRRLVRGLRPPALDDLGLAAALEELAERLLRAA
GIRVELDVDGDPDRLPPEVELALYRIVQEALTNALKHAGATRVTVTLEVDDGELTLTVRDDGVGFDPEAA
PGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLAAA
>gnl|CDD|443643 COG4586, COG4586, ABC-type uncharacterized transport system, ATPase component [General function prediction only]
IIEVENLSKTYRVYEKEPGLKGALKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG
ILVPTSGEVRVLGYVPFKRRKEFARRIGVVFGQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVE
LLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILL
TSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRGGEVIEREGNRVR
LEVDPRESLAEVLARLLARYPVRDLTIEEPPIEEVIRRIYKEG
>gnl|CDD|443644 COG4587, COG4587, ABC-type uncharacterized transport system, permease component [General function prediction only]
MMTMRKYLALFRIGFRRMLAYRANFLAGILTNLVPGLILYFLWSAVYASGGEIGGYSLAQMITYFLLAQV
LRALTSVWVDWEIAEEIRSGDIAYDLLRPVDYLLYWLARDLGERLFRLLFRLLPVLLVALLLFGLALPAS
LLAWLLFLLSLLLAFLINFLIQYLIGLLAFWTEEISGILRLKNVLVLFLSGLLIPLDLFPEWLQTILLWL
PFPYIVYFPASILLGRLSGAEALRGLLIQLFWLVVLLLLGRLLWRRGLRRYVVQGG
>gnl|CDD|443645 COG4588, AcfC, Accessory colonization factor AcfC, contains ABC-type periplasmic domain [Cell wall/membrane/envelope biogenesis]
AAAAVINVYGPGGPAPALKEAAEAFEKKTGVKVEVTAGPTPKWIDKAKKNADIIFGGSEQMMTAFAEAYP
GAFDSKDVEPLYLRPAAILVRPGNPKNIKGFEDLLKPGVKIVVVNGAGQTGVWEDIAGRTGDIETVQAFR
SNIVAYAPNSGAARKAWTQDPDIDAWITWNIWQKANPDLADLVEIEPDYRIYRDTNVALTKKGKADAEAQ
AFVDFLKSPEAQAIFKKWGWKR
>gnl|CDD|443646 COG4589, YnbB, Predicted CDP-diglyceride synthetase/phosphatidate cytidylyltransferase [General function prediction only]
LNARIRAWWVMVAVFWLAFLLGPTGALVLFALISFLALREFITLTPTRRGDHRALFWAFVVLPLQYYLVG
IGWYGLFTVFIPVYVFLLLPVRSALAGDTERFLERVAKIQWGLMLCVFCLSHAPALLTLPIPRGALLLLF
LVLVVQLNDVGAYLWGKLFGKRKLAPKISPNKTWEGLLGGVLTATLLGALLYWLLTPFSLWQALLLGLLI
SIAGFFGDLVMSAIKRDAGVKDSGNLIPGHGGILDRLDSLIFAAPVFFHLLRYFFYL
>gnl|CDD|443647 COG4590, COG4590, ABC-type uncharacterized transport system, permease component [General function prediction only]
MSTASPPPSLLPSSPARLRRRRWRLLKDKLARYGVTAGGIGVIVALLLIFFYLLYVVLPLFRSASVEPVA
QYSLPGAAAGATLALGMEEQNEVGYRFTDDGEVVFFSLADGEVLSEVQLPLPEGAQITSFAAAAPSSGLV
AYGLSDGQALVVKHDYKVSYPNNVRTITPSLEYPLGEEPLVLDEQGQALTQLAVQVGDDGLTVAAVTADG
RLLLTRFSKEENFLTGEVTLEREDYELPSLPGDVTQLLLDPDQRNLYVADGQGELSVYDIRDPDNPELRE
VVNLVAAGAEITALAFLLGGISLLVGDSDGSVSQWFPVRDEDNNRSLTKIRDFDASPAPITAIAPEHRRK
GFVAVDANGNLGIFHTTSERTLLSEKLSDGPLSALAISPRANGLLVEDSDGQLHFFEVDNEHPEVSWSAL
WQKVWYEGYPEPDYVWQSSSASDDFEPKFSLVPLTFGTLKAAFYAMLFAVPLAIAGAIYTAYFMSPKMRG
VVKPTIEIMEALPTVILGFLAGLWLAPFVEENLPGVFSLLLLLPLGILLFAYLWSRLPESIRNRVPEGWE
AALLIPVILLVGWLCFALSPPIENAFFGGDMRQWLTNELGITFDQRNALVVGIAMGFAVIPTIFSIAEDA
IFSVPKHLTQGSLALGATPWQTLTRVVLLTASPGIFSAVMIGLGRAVGETMIVLMATGNTPVMDFNIFEG
MRTLSANIAVEMPESEVGSTHYRVLFLAALVLFVFTFVFNTLAEIVRQRLRKKYSSL
>gnl|CDD|443648 COG4591, LolE, ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall/membrane/envelope biogenesis]
MNLLKIALRNLFRNKRRTLLTILGIALGVAKASDEVVLGEGLAKKLGLKVGDTITLISPDGSPKTRRFTV
VGIFESGGYELDGSLVYVPLETAQELLGLGDQVSGILVKLKDGADAEAVAAALEAALPGLEVKTWRELNA
ALFSALKTEKLILLLILLLILLVAAFNIVNTLLMSVLERTREIGILKALGASRRQIRRIFLLEGLLLGLI
GGLLGLLLGLLLALLLNALLGILLPFIFALPVSLSPSDVLLALLLALLISLLASLYPARRAARLDPVEAL
RGE
>gnl|CDD|443649 COG4592, FepB, ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism]
MARRRLAAAAALLAAALLLAGCSSADSTASGTSTAAAGGWPRTVTTEKGTVTLPAKPQRIVSTSVTLTGS
LLAIDAPVVASGATTPNNVTDDQGFFRQWADVAKERGVKRLYIGLEPNAEAIAAAAPDLIIGSATGGDSA
LDLYDQLSAIAPTLVVNYDDKSWQELATQLGEATGHEAQADAVIAAFDARVAEVKAAITLPPQPVSALVY
NEDGGANLWTPESAQGQLLQALGFTLAPLPAELATSTSQGKRGDIVQLSGENLAAALTGPTLFLFAADDK
DVDALKADPLLAHLPAVQAGRVYALGPDSFRLDYYSASNLLDRLEKLFGS
>gnl|CDD|443650 COG4594, FecB, ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism]
MKKLLLLLILLLALLLLAACGSSSSDSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLEWSFADALLALG
VTPVGIADDNDYDRWVPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSRHEAIYDQLSKIAPTVL
FKSRNGDYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQFRADGLRLYTP
NSFAGSVLAALGFENPPKQSKDNGYGYSEVSLEQLPALDPDVLFIATYDDPSILKEWKNNPLWKNLKAVK
NGRVYEVDGDLWTRGRGPLAAELMADDLVEILLKKK
>gnl|CDD|443651 COG4597, BatB, ABC-type amino acid transport system, permease component [Amino acid transport and metabolism]
MTTATDPPPPSPRLSSLLYDPRVRSILFQVLALALVVALVWYLVSNTLANLAARGIATGFGFLDRTAGFD
ISQSLIPYSPTDTYGRAFLVGLLNTLLVAVLGIVLATILGFLVGIARLSSNWLVSKLATVYVEIFRNIPL
LLQIFFWYFAVLEALPSPRQSLSLFDGVFLNNRGLYLPAPVFEPGFGWVLAALLAAIVAAFVLRRWARRR
QEATGQRFPVWWISLALLVGLPLLAFLLLGAPLSLDYPELKGFNFRGGLTLSPEFVALLLALSLYTAAFI
AEIVRAGIQAVSKGQTEAARALGLRPGQTLRLVVLPQALRVIIPPLTSQYLNLTKNSSLAVAIGYPDLVS
VFAGTTLNQTGQAIEIIAITMAVYLTISLLISLLMNWYNRRVALVER
>gnl|CDD|443652 COG4598, HisP, ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]
MTDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGE
EIRLKPDRDGELVPADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLA
KVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVV
THEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSSSLK
>gnl|CDD|443653 COG4603, NupP, ABC-type guanosine uptake system NupNOPQ, permease component NupP [Nucleotide transport and metabolism]
MSRLRLERRLLRLRSLLIPLLAVLLALLVGALLILLAGANPLEAYSALFQGAFGSPYGLGETLVKATPLI
LTGLAVAVAFRAGLFNIGAEGQLYLGALAAAAVGLALPGLPGPLHLPLALLAGALAGALWAAIPGLLKAR
FGVNEVITTLMLNYIALYLVNYLVRGPLRDPGSGFPQTPPIPESARLPRLLPGTRLHLGLLIALLAAVLV
WVLLNRTTLGYELRAVGLNPRAARYAGINVKRLIVLAMLISGALAGLAGAVEVLGVQGRLTPGFSPGYGF
TGIAVALLGRNNPLGIILAALLFGALYVGGDAMQRALGVPSEIVDVIQGLIILFVLAADFLIRYRLRRRR
RKRAAK
>gnl|CDD|443654 COG4604, CeuD, ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism]
MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS
RELAKRLAILRQENHINSRLTVRELVAFGRFPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQ
RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMK
DGRVVAQGTPEEIITPEVLSDIYDTDIEVEEIDGKRICVYFR
>gnl|CDD|443655 COG4605, CeuC, ABC-type enterochelin transport system, permease component [Inorganic ion transport and metabolism]
MRTTARRRLLLLALLALLAAALFLFYGLPGNWDYILPRRGTKLAAMLLVAIAIAVSTVLFQTITNNRILT
PSIMGFDSLYVLIQTLLVFFLGSAGLAALNPLLNFLLEVALMVGFSLLLYRWLFRGGRRNLHLLLLVGVV
LGTLFRSLSSFLQRLIDPNEFDVLQDRLFASFNNVNTDLLLIAAVIVLLALLLLWRLRRRLDVLALGRDQ
AINLGVDYRRVVRRLLILVAVLVAVSTALVGPITFLGLLVANLAYQLFGTYRHRYLLPAAALIGVIALVG
GQFVVEHVFNFSTTLSVIIEFVGGIYFLYLLLRKRRL
>gnl|CDD|443656 COG4606, CeuB, ABC-type enterochelin transport system, permease component [Inorganic ion transport and metabolism]
MKKLRLLILLLLVLSILSLFIGVSDVSLSDLLSLDPEALQILLISRLPRTLAILLAGASLSVAGLIMQQL
TRNRFVEPTTAGTMESAKLGILVALLLFPGASLLGKMLVAFVFALAGTLLFLAILRRIPFKDALLVPLVG
LMLGGVISAITTFFAYRFDLLQSLSSWLQGDFSGVLRGRYELLWLSAPLAVLAYLYADRFTIAGMGEDFA
TNLGLNYRRVVNLGLVIVALITAVVVVTVGSIPFLGLIVPNIVSLYMGDNLRRTLPWVALLGAGFVLACD
ILGRLIIYPYEIPIGTVVGVVGSAIFLYLLLRRRRRAA
>gnl|CDD|443657 COG4607, CeuA, ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism]
MKKTLLAALALAAALALAACGSSSAAAASAAAAETVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGV
EVAGVPKGLLPDYLSKYADDKYANVGTLFEPDLEAIAALKPDLIIIGGRSAKKYDELSKIAPTIDLTVDG
EDYLESLKRNTETLGEIFGKEDEAEELVADLDAKIAALKAAAAGKGTALIVLTNGGKISAYGPGSRFGPI
HDVLGFKPADEDIEASTHGQAISFEFIAEANPDWLFVIDRDAAIGGEGPAAKQVLDNELVKQTTAWKNGQ
IVYLDPDAWYLAGGGIQSLTEMLDEVADAL
>gnl|CDD|443658 COG4608, AppF, ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]
AAMAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEP
TSGEILFDGQDITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAEL
LELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLT
YLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQALLSAVPVPDPERRRERIVLEGDVP
SPLNPPSGCRFHTRCPYAQDRCATEEPPLREVGPGHQVACHLAEEGSGV
>gnl|CDD|443659 COG4615, PvdE, ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism]
MNLLRLLLRESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQL
LLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALVLGCLA
YLAWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKLNRRRRRAFF
DEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFVLVLLFLRGPLS
QLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDEGFTLGP
IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR
LLGLDGEADPARARELLERLELDHKVSVEDGRFSTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDP
EFRRVFYTELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAALAAS
>gnl|CDD|443660 COG4618, ArpD, ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport]
MSRASAGRSELRAALRACRRAFLSVGLFSFFINLLMLTPPLYMLQVYDRVLTSRSVDTLLMLTLLALGLY
AVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRAALRGGGGAAAQALRDLDTLRQFLTGPGLFALFDL
PWAPIFLAVLFLFHPLLGLLALVGALVLVALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAM
GMLPALRRRWQRANARALALQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIAASIL
MGRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMPLPRPKGRLSVENLTVVPPGSKRPILRG
VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG
TIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVV
LDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLARP
AAA
>gnl|CDD|443661 COG4619, FetA, ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]
LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP
EWRRQVAYVPQEPALWGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLA
LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL
>gnl|CDD|443662 COG4623, MltF, Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms]
LLLLLPACSSEPGDLEQIKERGVLRVLTRNSPTTYFIYRGGPMGFEYELAKAFADYLGVKLEIIVPDNLD
ELLPALNAGEGDIAAAGLTITPERKKQVRFSPPYYSVSQVLVYRKGSPRPKSLEDLAGKTVHVRAGSSYA
ERLKQLNQEGPPLKWEEDEDLETEDLLEMVAAGEIDYTVADSNIAALNQRYYPNLRVAFDLSEPQPIAWA
VRKNDPSLLAALNEFFAKIKKGGTLARLYERYFGHVKRDTRAFLRRIEGRLPPYDPLFEKYAEEYGLDWR
LLAALAYQESHWNPRARSPTGARGLMQLMPATAKELGVDDRLDPEQSIRAGAKYLRWLYDRFPEAIDEPD
RWWFALAAYNAGPGHVQDARRLAKKQGLDPDRWFDVEKSQPKYYDTGYARGRETVNYVPNIRAYYDIYKR
L
>gnl|CDD|443663 COG4624, Nar1, Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]
LLLLLRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISC
IQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGKAEIDEEKCISCGQCVAVCPFGAITEK
SDIEKVKKALKDPEKVVAQVAPAVRGQFGGTVTPGKLVAALKKLGFDDVFETAFGADLTIMEEAKELLER
LKKGKLPMITSCCPAWVKLIEKYYPELLPNLSPCKSPMQAFGALIKTYYAPDIKVVFIGPCIAKKFEAKR
PEMKGDVDYVLTFRELARMIKEAGIDLANLEEEEFDNESSGAGRIFGVTGGVMEAALRTAYELLPDGLEL
KVAVVSGLKNCRKLLEEIKAGKIDYHFIEVMACPGGCIGGPGQPIPPGSLEKRRKRVALYAKEAPIRKSH
ENPEILDLYREFLGKPLSEKAHELLHTHYR
>gnl|CDD|443664 COG4625, COG4625, Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown]
GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGG
GGGAGGGGGGGGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGG
GGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGG
GGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGG
GGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGA
GGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTGGGGAGGGGGAA
GGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTYTGTTTV
NGGGNYTQSAGSTLAVEVDAANSDRLVVTGTATLNGGTVVVLAGGYAPGTTYTILAVAAALDALAGNGDL
SALYNALAALDAAAARAALDQLSGEIHASAAAALLQASRALRDALSNRLRALRGAGAAGDAAAEGWGVWA
QGFGSWGDQDGDGGAAGYDSSTGGLLVGADYRLGDNWRLGVALGYSRSDVDVDDRGSSGDSDSYHLGLYG
GYQFGALYLDGGLGYGWNDYDTDRTIAFGGLSRTATADYDGDTASAFLEAGYRFDLGGLTLTPFAGLAYV
RLRTDGFTETGGAAALSVDSQSTDSLRSTLGLRASRTFSLGGGVTLTPSGRLGWRHEFGDDDPSTTASFA
GAPGAAFTVAGAPLARDALVLGAGLSARLSDGLSLGLGYDGEFGSGYTDHGGSAGLRYRF
>gnl|CDD|443665 COG4626, YmfN, Phage terminase-like protein, large subunit, contains N-terminal HTH domain [Mobilome: prophages, transposons]
MSEPYWDTATDYAEDVVDGEIIAGKLIKLACQRHLDDLKRPPYYFDEEKAERAIRFIKLLKHTKGPLAGK
PFELEPWQKFIVGAIFGWVDKDTGLRRFREAYLLVPRKNGKSTLAAGIALYLLLADGEPGAEVYSAATTR
DQAKIVFKEAKAMIKASPELAKRFKIQDNAKTITHPKTGSKIKALSADADTLDGLNPSFAIVDELHAHKD
RDLYDVIKSGMGARPQPLLIIITTAGDDPEGPCYEEYEYARKVLDGEIEDDRFFPIIYELDEDDDWTDPE
NWIKANPNLGVSVSLEYLRDEARKAKESPSKRADFLTKHLNIWVGLSADAWLDMDDWEACAEPVDLEDLR
GRPCYGGLDLSSTDDLTALALVFRDDDGKWYVLSHFWIPEDTLEEREKEDGVPYRDWAEQGLLTITPGNV
IDYEEVAEWILELAERFDLKEIGYDPWGATYLVQALEEEGFPLVEVRQGFKTLSPPIKELERKLLDGKLV
HGGNPLLRWCVSNVVVKEDANGNIKPTKKKSRGKIDGAVALIMAVGRAMLNEEARGELNSVYEDRDILV
>gnl|CDD|443666 COG4627, COG4627, Predicted SAM-depedendent methyltransferase [General function prediction only]
SLSPLKLNIGCGPKRLPGWLNVDIVPAPGVDIVGDLTDPLPFPDNSVDAIYSSHVLEHLDYEEAPLALKE
CYRVLKPGGILRIVVPDLEHVARLYLAEYDAALDVAELRLAGPIDPLGIILGERLAGLAARHSVLFRTGF
TRLALTARRSAAGARAALAER
>gnl|CDD|443667 COG4628, COG4628, Uncharacterized conserved protein, DUF2132 family [Function unknown]
EQPNNPLHGVTLEQILTELVDHYGWEELGERININCFKNNPSIKSSLKFLRKTPWAREKVEALYLYTLKR
KPRA
>gnl|CDD|443668 COG4630, XdhA, Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism]
IRFLLNGELVELSDVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVVGELDDGGLRYRAVNACILFL
PQLDGKALVTVEGLAGPDGALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYERGPAPDRADIEDALSGNL
CRCTGYRPIIDAARAMAEAPAPDPFAADRAAVAAALRALADGETVELGAGGSRFLAPATLDELAALLAAH
PDARLVAGATDVGLWVTKQLRDLPPVIFLGRVAELRRIEETDDGLEIGAAVTLSDAEAALAAHFPELAEL
LRRFASRQIRNAGTLGGNIANGSPIGDSPPALIALGAELVLRSGDGRRTLPLEDFFLGYRKTDLQPGEFV
EAIRIPLPAAGQRLRAYKVSKRFDDDISAVCAAFALTLDDGTVTEARIAFGGMAATPKRARAAEAALLGQ
PWTEATVAAAAAALAQDFTPLSDMRASAEYRLAVAANLLRRFFLETQGEAPATRVA
>gnl|CDD|443669 COG4631, XdhB, Xanthine dehydrogenase, molybdopterin-binding subunit XdhB [Nucleotide transport and metabolism]
MSKALSPPPAAGAVGKSLPHESARLHVTGEARYIDDLPEPAGTLHAAPGLSPVAHARILSIDLSAVRAAP
GVVAVLTAADIPGENDIGPIIHDEPLLADGEVEYVGQPVFAVVAESREAARRAARLAKIEYEELPAILTI
EEALAAGSFVLPPHTLRRGDADAALAAAPHRLEGEFEIGGQEHFYLEGQIALAIPGEDGGMLVHSSTQHP
SEVQHLVAHVLGVPMHAVTVEVRRMGGGFGGKESQAALFAALAALAARKTGRPVKLRLDRDDDMVMTGKR
HPFRIDYEVGFDDDGRILGLDITLAARCGWSADLSGPVADRAMFHADNAYYLPAVRITGHRCKTNTQSNT
AFRGFGGPQGMLAIERVIDDIARALGLDPLDVRRRNFYGPAERNTTPYGQPVEDNILHELVDELEESSDY
AARRAAIAAFNAASPVLKRGLALTPVKFGISFTATHLNQAGALVHVYTDGSVQLNHGGTEMGQGLHTKVA
QVVADELGVPLERVRITATDTDKVPNTSATAASSGSDLNGMAAQDACRQIRERLAAFAAELLGVEPEDVR
FADGRVRVGGQSLSFAELVKAAYLARVSLSATGFYKTPKIHWDRATGQGRPFYYFAYGAAVSEVEIDTLT
GEYRVLRVDILHDVGRSLNPAIDIGQIEGGFVQGMGWLTTEELVWDDKGRLLTHAPSTYKIPAASDRPED
FNVALLERPNREDTIYRSKAVGEPPLMLGISVFEALRDAVAAVGDYRVSPPLDAPATPERVLMAVEAVR
>gnl|CDD|443670 COG4632, NAGPA, Sugar-P-sugar glycosidase (uncovering enzyme, UCE), NAGPA superfamily [Carbohydrate transport and metabolism]
SALGLLGGLVVVNGAAGGALLVRKLVVLLIGGALGATALALAVSVTGLNALLAAAELALALSALTTLTLA
GAATAAVLLAAPLLSLLAGVTAGPGAPVTGGLLVRAAAGALVGALALGRLVDVLTLVTTPARGNRPVAPG
GLFDPGGKPTGIIISNGKVISPNKDGPARDVLGIDKDGKLIVGDPVTIDLEKLPAGVEEAVGGGPLLVKN
GKVVVDADEAAFGNGRAPRTAIGITADGTLLLVVVDGRQPGSIGATLAELAQLLKELGAVDALNLDGGGS
TTLVYNGKVVNRPSDGKERPVANALGVFPK
>gnl|CDD|443671 COG4633, COG4633, Plastocyanin domain containing protein [General function prediction only]
MLLVNLLGLALIGLILWWFWLSKPKSAKAAVENGVQEVTITVDGGGYSPSRITVKAGIPVRLNFTRKDPS
GCAEEVVFPDLGISQDLPLGKTVTIEFTPLKPGEYPFTCGMGMYRGTIVVE
>gnl|CDD|443672 COG4634, COG4634, Predicted nuclease, contains PIN domain, potential toxin-antitoxin system component [General function prediction only]
MKFLLDENLSPRLVEWLREAGHDVLHVRDLGLPGASDEEILEYARREGRIIVTKDKDFGELLALSGAPPP
GIILLRLGNLSPEELAELLRRVLERIEEFLLEGALIVVEPDRI
>gnl|CDD|443673 COG4635, HemG, Protoporphyrinogen IX oxidase, menaquinone-dependent (flavodoxin domain) [Coenzyme transport and metabolism]
MKVLILYASRDGQTRKIAERIAEVLREAGHDVDLVDLEDAPDLDLAGYDAVVIGASIRYGKWLPEAVRFV
RRHRDALAARPVAFFSVSLTARKPEKRTPETNAYLRKFLAKTGWQPDLVAVFAGALDYPRYGFFDRLMIR
LIMKMTGGETDTSRDGEYTDWDAVRAFAREFAALLAARR
>gnl|CDD|443674 COG4636, Uma2, Endonuclease, Uma2 family (restriction endonuclease fold) [General function prediction only]
MTAALPPGKRLTVEEYLALLPEDERYELIDGELIEMPPPGGRHGRIAGNLARLLRNWLRGRGLRVFDSDT
GVRLPNGSVRYPDVAVVCGERLDREERESYLEGAPDLVVEVLSPSTARYDRGEKLALYARAGVPEYWLVD
PEQRTVEVYRLPEGEYELLTYEGGDTLSSLPVLPGLELDLEELFEAV
>gnl|CDD|443675 COG4637, COG4637, Predicted ATPase [General function prediction only]
MITRIRIKNFKSLRDLELPLGPLTVLIGANGSGKSNLLDALRFLSDAARGGLQDALARRGGLEELLWRGP
RTITEPIRLELEFAEEDERDLRYELELGLPEPGGRPEVKEERLWLKRGSGGRPFLDFRPKGRAVGGEPER
LDSPESLLSQLGDPERFPELRALREALRSWRFYDFHPAPLRQPQPAGRTPVLAPDGSNLAAVLATLRETH
PERFERILEALRDAFPGFEDIEVEPDEDGRVLLEFREKGLDRPFPARELSDGTLRFLALLAALLSPRPPP
LLCIEEPENGLHPDLLPALAELLREASERTQVIVTTHSPALLDALEPEEVLVLEREDDGETRIRRLSDLE
LPEWLEGYSLGELWARGLLGP
>gnl|CDD|443676 COG4638, HcaE, Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit [Inorganic ion transport and metabolism, General function prediction only]
ASRLPAAFYTDPEIFELELERIFRRGWYYVGHSSELPEPGDYLTRTILGEPVVLVRDKDGEVRAFHNVCP
HRGAPLSEGRGNGGRLVCPYHGWTYDLDGRLVGIPHMEGFPDFDPARAGLRSVPVEEWGGLIFVWLGPDA
PPLAEYLGPLAEYLDPYDFGELKVAGRETYEVNANWKLVVENFLDGYHVPFVHPGIILFLFPNLMILDYP
DHLVVRTVTPVSPDRTRVFVTFYVPKDALDPEARADLEAFWGRVFEEDREIVERQQRGLRSLAYPGPYLS
RSPAEGGVRHFRRWLRRL
>gnl|CDD|443677 COG4639, COG4639, Predicted kinase [General function prediction only]
MLSLVVLIGLPGSGKSTFARRLFAPTEVVSSDDIRALLGGDENDQSAWGDVFQLAHEIARARLRAGRLTV
VDATNLQREARRRLLALARAYGALVVAVVLDVPLEVCLARNAARDRQVPEEVIRRMLRRLRRPPLPEEGF
RVVYV
>gnl|CDD|443678 COG4640, YvbJ, Uncharacterized protein YvbJ, contains N-terminal Zn ribbon domain [Function unknown]
MKFCPNCGHKLEDGVKFCPNCGTPLTSKVKQARQAKQKQAQSAVSNTAVKKKITKKKKIIIASIAVILIL
LIGFYYLGKNYYSPEAQVDRFLEAVKNNDAEALAKLLVTNDSNLKITKDEAKALITYFKENPSYLKELLS
DLKSAAESLNKSEILQLKKDGKKFLFFDKYKVVVKPKYLTVKTNLKGAKLFLNGKKIGTSDSDNFSKKLG
PLIPGTYTLKAKGKNDGGELEGEEEIDLLENENNNQSIDLSLKGKYVTVKSNLPDADLYINGKKIGKLVS
GSKTVGPYPWDGSVTVYAKKTFPGGTIKSDEVKISDSSDGSTVTLDFPNVLDEDTAEEELVKAYYKDYVY
ALNANDASDLTNYFDEGSNNFYKDVKEYIKQKMKKGISFDLSSVEVQTGDDTYKVSFTAKYDFYSSDGEE
ITQEFTYGYILKYDEDGKGYQIVDI
>gnl|CDD|443679 COG4641, COG4641, Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]
MKILWNGHATYYRGLLRALAALGHEVTFLEPDDPWHDPLYAAELLDAFRPDLVLVISGVELVAALRARGI
PTVFWDTDDPVTLDRFRELLPLYDLVFTFDGDCVEEYRALGARRVFYLPFAADPELHRPVPPEARFRYDV
AFVGNYYPDRRARLEELLLAPAGLRLKIYGPGWPKLALPANVRRGGHLPGEEHPAAYASSKITLNVNRMA
ASPDSPTRRTFEAAACGAFLLSDPWEGLEELFEPGEEVLVFRDGEELAEKLRYLLADPEERRAIAEAGRR
RVLAEHTYAHRARELLAILEELG
>gnl|CDD|443680 COG4642, COG4642, Uncharacterized conserved protein [Function unknown]
GGSVAEDGAGGGGDATALGGGGEGGLAAAGGEGGGGLGTLPGGGGYGGGADGGGGGGGGTGVAGGGGGEG
GVTAAGGGGGGGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGG
IYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGT
YTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYADGSVYEGEWKN
>gnl|CDD|443681 COG4643, COG4643, Uncharacterized domain associated with phage/plasmid primase [Mobilome: prophages, transposons]
MSTNVKEVKAAARGRWPDILAALGLDPPALHGPCPCGGKDRFRFDDKRGRKSGWYVCNQCGPPAGDGLDL
LMKVFGWDFKEAALGLDAKGRELTPEERAAARARAAAARAAREAEREARQAAAARRAAALWAEARPATPG
DHPYLARKGLAAHGLRFHPALLLPGGALLVPLTDADGELVTLQRIYLDGEKRFLKGGRKKGAFIRIGPLP
PPGGTLLIAEGYATALSVHEATGLPVVAALDAGNLLPVAQALRERYPVAELIIAADNDRNTDGNPGQAAA
EEAARAVGGLVALPPFPPKKGTDFNDLHQARGLEAVRAAFEAALYQPAGQTAAAVALALAAVGSATAEVA
AALALAPSAVEGVGLSEDDAAIAADLRWGAALRPSLGAAAGLRLLLAAEAGEDAAKKAALALTKLASLAA
QLPLDGLSLSDALDG
>gnl|CDD|443682 COG4644, COG4644, Transposase and inactivated derivatives, TnpA family [Mobilome: prophages, transposons]
AGLPALLLLPDAALTLLLRLLLLEARLLDVAAAAARGELLGGKIGKLLLKLPALDPPPPEAALRAALRRL
LPLPPLIILLLLVDVDTGTGFFFFFTSLGRGRKPDDDRRLLLALLAAGGNNGLLPKMARASPGLSRDQLA
WVARWYIREETLRAANAAIVNAQHRLPLAALWGDGTTASSDGQKFEVGVRNLLAGYSNRYYGREPGVTIY
THVSDQYAPFHSQVIPATEREAAYVLDGLLRNETDLKPDEHYTDTHGYSDHVFALCHLLGFRFAPRIRDL
KDRKLYRPDPPTRYEHLDPLIGGTINWDLIEEHWDDILRLAASIKLGTVSASTILRRLGSYSRQNPLYKA
LRELGRIERTLFLLDYLDDPELRRRIQAGLNKGEARNALARAIFFGRLGEIRDRTREEQEKRASALNLVA
NAIVLWNTLYLQRALEELRAEGDEIPDELLAHLSPLGWEHINLTGDYDFDLERKLGGLRPLRAPLALLLA
>gnl|CDD|443683 COG4645, OpgC, Predicted acyltransferase [General function prediction only]
MSAPAPAAPAPMGRDLRLDFFRGLALVFIFINHIPGNVLERLTHRNFGFSDAAEGFVFLSGYAAALAYGR
RFARGGFLAATARILRRAWQLYVAHIALFVLALALIALLALLFGNPDYLEELNLGPLLADPLGALLGLLL
LTYQPGYFDILPLYIVLLLLAPLLLWLARRRPWLVLALSVALWLAAQLFGLNLPAYPDGGGWFFNPFAWQ
LLFVLGLVLGLGRARGRRLVPRSRWLVWLALAYLLFSLVLVLFPFWWLVPALLWLPALLPLFDKTNLSPL
RLLHFLALAYLVAWLLPAGWRALRSRLLRPLILLGRHSLPVFCAGVVLSLAGQIVLDVTGGGPLLQTAVN
LAGIALLLAVAYLLEWFKRRPR
>gnl|CDD|443684 COG4646, COG4646, Adenine-specific DNA methylase, N12 class [Replication, recombination and repair]
GLRTLDSESDEDRLRLEEEREERDERLEDLDAALVIKADEALEERGSEDDELGALSEDLASSLEDAELED
TELELLAILDGLPLLEEELLAGRDALDDEAEEGEEVEGLSEGLKIAIELSRLGSELEAVLGAEAGDGLAA
AIEAPIEIENSEKLKAASTLLETVTEPEVEAELAEVELLSAEAAAADEEVSSESLASTPAAARAGAAKIL
AVLLAEGALALKLARAAERLALAESGGERRNNAKIEELALELDEELEADELANAAADAELRDATKAAELA
TELDARARESDARAAGFRGGEGAILLEGGGLEGLAGGLIGEGGLGIGAEGAGSAGALTAALLNEQLAGAG
GAIALLADPLAADLAFGLFPFLFVAANVFGGLKKLFLADLHILFLSAAARLVRGRDALATLGSLKDAFPK
ARARRAARIAADLAASVAASLAAAARALATAEILEITEIREADRLEAEADEDLKDLEVVFAELEGEGAII
DVNRYFADHPEVTPPADPSVKDGSYTFEDGVLYVDEAHNFKNLEVPATKMRRVAGLIPLRDAVRELIEAQ
AEDDGSQKALRMRLNCRYDAFVAKYGPINSRPNLRAFRDDPDYPLLLSLEEYDEETGTARKADIFTKRVI
RPPTETSVDTAAEALAVSLNERGRVDLDYMAELTGTPISNSLAELYGMIYLDPDTLEDGWVTFDEYLSGN
VREKLAAARAAAELDPRTFGENVTALELVQPEDLEPSEIDVRLGATWIPKTRFEAFIRELLGTPITVSYS
PETGEWSVKGKNGNAAATSTYGTERANAPELLEDALNVADIRIADPVPDERRVLNTEETEAAKEKQEAIK
EAFAEWVWEDPERAERLVRLYNDKFNSIVPREYDGSHLKFPGDSRKISLRPHQKNAVARILYGGNTLLAH
EVGAGKTFTMVAAAMELRRLGLANKPMIVVPNHLLEQDAPSKLNLYAAANILIATKTDFEKGTRLVFCAD
IATGDYDAVIIGHIQFEKIPASGERQEEILEEQIAEILKAIKELKAVVRKRFTVKQLESTKKLGAGKLKQ
LDLLALKDLDVPWEPLDVDQLFGRGSRQGNNNFLVTKMRNVAGLAFSDAAKLSDYFGKQRYRDELTAGKG
VVVATGTDESNLMYELYTAQAYLQLLLLGKQGLTNFDTWASTLEELVTAAELAPERTAYRANTREAKAVN
LPEEDVMIKEAEDAKTADELLLPTPEKISGGVATKPSEVQKELLEELEERAAIVRKNDGEPDRDNMLVIT
DDGRKAALDQRLDIKTLPDDEGSLVALCVTNIDRIWEDNPESKLTQLVFCDLSTPKGDGTFNDLEDIREK
LIEEEIAELEIAFIHLALDDQEKAELFARDRLGAVEKLRISTAKMGAGTNVRLLLEATHDLDVPWRPRDA
EQRAGRGRRQGNENEEVEEIRYVTENTFDAYLWQAAETKQKFIAQIMTSKSPVRSLEDVDEAALSYAERK
ALAAGRPKEKEKMDLDIEVLKLKLLDAAALEQLYAEEDKLRKSYLDEEEALEERIEAATKDLRLARAASQ
EEADEQESASKEAAAGEKKAAAAELLAALQAAGLIVLDGGRTPRGEKGGGLLARALLEAATLLLPIEEAE
GSEGADATGDRRTGAAAEIELAAEALILNLAERLERALRDGAEEEEIAPRELEAALKEEAALLARAGELA
ELELDKADLEAELEALADDLAEAAEEERKEA
>gnl|CDD|443685 COG4647, AcxC, Acetone carboxylase, gamma subunit [Secondary metabolites biosynthesis, transport and catabolism]
ILLPLTEYLYIVQDLDKERWVKCECGHEFGDARENWKLGALVYVRDPEEIHPEIYPYTFAPDPEWQRIRE
YYCPGCGTLLEVEALPPGYPVTHDFEPDIDTFYREWLGRPLPEEAVI
>gnl|CDD|443686 COG4648, COG4648, Uncharacterized membrane protein [Function unknown]
MRRLLGVLLALLLLAYPLLVYFGLSHGGPRWLALLLAPLLLLRLLLARRSRRRLRALALVLALAGALLLL
LSLLLHSEWLLLLYPVGVNLLLLALFGRSLLPGPPLIERLARLVEPDLPPAGVRYTRRVTQVWCVFFALN
GLISLLLALYASLAVWSLYNGLISYLLMGLLFAGEWLVRRRVLPRHERASILD
>gnl|CDD|443687 COG4649, TPR1, TPR-like repeat domain [Function unknown]
MSNDDDFFREVDEELRRDRLRALWRRYGPWIIGAAVLVVVGVAGWRGWRYWQEAQAEAAGDAYLAALELA
EAGDAAEAAAALAALAADGPGGYAALARLRAAALLAQAGDTAAAVAAYDAVAADASAPPLLRDLARLRAA
LLLVDTGDPADVRARLEPLAAPGNPWRHSARELLALAALKAGDTDAARRLFQAIAADAEAPAGLRQRAQQ
LLALLGADAAAA
>gnl|CDD|443688 COG4650, RtcR, Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms]
MMKKTVVIGFLGTTLDRRGKGPNRWEKWRPTVSLCQQEDLLVDRLELLHDPRDRALAEQVAEDIAQVSPE
TEVRLHEVDLADPWDFEEVYAALLDFARAYPFDPEREDYLVHITTGTHVAQICWFLLTEARYLPGRLLQT
SPPRKRRAGAAGSYTIIDLDLSRYDAIASRFAQEQQEAVSFLKSGIATRNAAFNRLIEQIERVAIRSRAP
ILLTGPTGAGKSQLARRIYELKKARHQVSGRFVEVNCATLRGDGAMSALFGHVKGAFTGAVSDRAGLLRS
ADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLAR
INLWTFRLPGLAERREDIEPNLDYELARFAREQGRRVRFNKEARARYLAFATSPEALWSGNFRDLNASVT
RMATLAEGGRITVALVDEEIARLRRLWQRAEAATGDDLLAELLGAEQAAELDLFDRVQLAAVIRVCRRSR
SLSEAGRTLFAVSRQQKASPNDADRLRKYLARFGLSWDQVKART
>gnl|CDD|443689 COG4651, RosB, Predicted Kef-type K+ transport protein, K+/H+ antiporter domain [Inorganic ion transport and metabolism]
MHETPLITTIALILGLAAVLGLLAQRLRQPPIVGYLLAGVLIGPFTPGLVADVELIEQLAEIGVILLLFG
VGLEFSLKDLLAVRKIALPGALLQIALTTLLGFGIALLLGWSLGESLVFGLALSLSSTVVLLKLLEDRGE
LDTLHGRIAVGWLIVQDLAVVLMLVLLPALAGGGGGLLGTLGLTLLKVALFVALMLVVGRRVIPWLLHRV
ARTRSRELFLLAVLAICLGVAYLAALFGLSFALGAFLAGMVLAESEYSHQAAAELLPLRDAFAVLFFVSV
GMLFDPSFLLENPLPVLALLLIVLIGKPLIAFLIVLALGYPLRTALLVGLSLAQIGEFSFILAALGLSLG
LLSEEAYQLILAVAILTIALSPYLIALADPLYARLERRPPLAARLERDRPEESDLVVHVVVVGGGGGGGG
LALRLLLRGIVVVVVVDNVEEVVRARRRGGIAGGGGAAADLELLAALLAAAAIAVVAIPAAAAALLLIAA
ARRALPLLIIIARAARRAEEEELLLAGAVEVVVEEEEEAAEAALLLLLLLLLLRALAERAILRAARRRLR
AERA
>gnl|CDD|443690 COG4652, COG4652, Uncharacterized conserved protein, DUF1430 domain [Function unknown]
MKKKTGYPTFSRGSYQLLPLSDLENSDPRGSYLIFGGPGSVEEFINELSEKGVTAEYEGQSKISAFSFFF
SGSLLLLILILLLLFMLLIIYYVIYSLKKYAIKKLHGYSKLSIIFRLIKRIIRLAILLALISLLLSILIL
WLFYNGLAGFGLFFLLSLLLLSVLLLLIILLISLIALLLIRRISIVSAIKGKLPTKGLLALSYVVKIIAL
ILVIFTLITSLAAIQQLKTLLATLEAWEKAKDYYTLSLSVNGDDGSKLDDNDKLSDFYKDAEEKGDLFLA
DSNSLSGSEDSINSYYSDEGNSLLVNPNYLKRNPILDENGKRIKEIDDEKNEVILLVPESYKGEEKEIKK
YYKEYLYFQKNEGEEETKLKPQDLKVEIIYIKDGQSLFTYNSNVNGDTDNLITDPIIVVVTPNNLLGESF
YLSALSNGGLKFKDYDAIEPLLKKYGLGDYISSINNAYDEYAESLNETKRELRLLLIGAIISILILLLII
ISLVLTYFELNRKRIFVRRLHGYSFLRRYKRYLLLELGLWLLGLAISLIISHASLLYILLVALLILIIEL
IITILTLSKFEKRSFVKILKGEL
>gnl|CDD|443691 COG4653, gp36, Predicted phage phi-C31 gp36 major capsid-like protein [Mobilome: prophages, transposons]
MAFGAYLRRGDARLREEAKALSTGTDADGGYLVPPEFANEIIEALKEYSPIRQLARVITTSSGSYKIPVS
TTGPTAGWVGEGAARETSTPTFGQVTLPAHELYALPKVSQELLDDSAFDLEAWLAEELAEAFARAEEAAF
VNGDGTGKPKGILTYATVAAGTVAAGAAGAITADDLIDLIYSLKAAYRANAVWVMNDSTLAAIRKLKDGN
GRYLWQPGLAAGQPATLLGYPVVESEDMPDIAAGAKPIAFGDFSRGYLIVDRQGLRVLRDPYSAKGQVGF
YATKRVGGGVVDPEAIKLLKFAAS
>gnl|CDD|443692 COG4654, CytC552, Cytochrome c551/c552 [Energy production and conversion]
AADAAAGKALAKKSGCLACHAVDKKLVGPSYKDVAKKYKGKADAVAKLAKKIKKGGSGVWGDVPMPPHPQ
LSDAEAKALVKWILSLKK
>gnl|CDD|443693 COG4655, TadX, Uncharacterized conserved protein, contains TadX/Tad_C domain [General function prediction only]
MTTRLRLRLRRFLRRQRGAIAVLAALLLPVLLGFLALAVDIGSLYLEKRDLQRAADLAALAAAQNLAGCA
AAAAQASAAANGYPGVADTSVTVELGRYTADPSLAPGLRFFVAGGATPANAVRVTLTKTVPLFFASVLGG
SPTLSATATAARTPLAAFSVGSRLASLNSGLLNALLGGLLGTNLSLSVMDYNGLADADIDLLDFLDALAT
RLDLTAGTYNDLLAANVSLGQLLNALASALGDQGVLGAAVAALSTLEASTGGSNLKVPLGDLLDLGAPDV
LGADAALDAQVNALDLLSAAAQVANGNNAVALPLGLNLPGLAGVKVRLAIGEPPQIAVGGPGTIVRTAQV
RLFLDVQVDGLLGALALARVDLPLYVEVASAEATLTSIDCPAPGPPTSVTIGVTPGVAELCIGNVVPLGN
AAPQTLTFTPADIPAGTTKTVSTGNLLASLLSSLLGLVLGLDLGGVLTGALAPLLSPLTAPLDPLLDPVL
SLLGVQLGEADVRVTGVRCGRPVLVQ
>gnl|CDD|443694 COG4656, RnfC, Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and conversion]. Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
MKLWTFKGGIHPPENKELSADKPIERLPLPEKLVIPLQQHIGAPAEPLVKVGDKVLKGQLIAEADGFVSA
PVHAPVSGTVVAIEPAPHPSGLKVLCIVIEPDGEDEWIELEPLADYEDLSPEEIIERIREAGIVGLGGAG
FPTHVKLSPPPDKKIDTLIINGAECEPYLTCDDRLMRERAEEIIEGIRILMKALGAKKVIIGIEDNKPEA
IAALRKALAGDDDIEVVVLPTKYPQGGEKQLIKALTGREVPSGGLPADVGVVVQNVGTAYAIYRAVRDGK
PLIERVVTVTGDAVKEPGNLLVRIGTPVSDLLEQAGGFKEEPGKLIMGGPMMGFALPSLDVPVTKGTNGI
LALTKEEVPPPEEQPCIRCGRCVDACPMGLLPQQLYWYARAGDFDKAEEYNLMDCIECGCCSYVCPSKIP
LVQYIRLAKAEIRARRREKQKAEEARERFEA
>gnl|CDD|443695 COG4657, RnfA, Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfA subunit [Energy production and conversion]. Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfA subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
MMELFLIFISAILVNNFVLVQFLGLCPFLGVSKKLETAIGMGLAVTFVMTLASAISWLIYNYILVPLGLE
YLRTIVFILVIAALVQFVEMVLKKVSPALYRALGIYLPLITTNCAVLGVALLNVQQGYNFLESLVFGFGA
GLGFTLALVLFAGIRERLELADVPKAFKGLPIALITAGLLSLAFMGFSGLIKF
>gnl|CDD|443696 COG4658, RnfD, Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfD subunit [Energy production and conversion]. Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfD subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
MPKLKVSSSPHIHSGDSTSRIMLDVLLALLPALAAGVYFFGWGALIVILLAVLTAVLTEALILKLRKRPP
TLGDGSAVVTGLLLALSLPPTAPWWMVVIGSFFAIVVAKQLFGGLGQNPFNPAMVGRAFLLISFPVQMTT
WLPPAPLAAGFLDSLALIFTGGGVDAVTGATPLDALKTGLSALTVSEILQDLFFGNIGGSGGETSALALL
LGGLYLLYRRIISWHIPVAYLGTVAVLAGLFGLIDPDRYASPLFHLLSGGLMLGAFFMATDPVTSPTTPK
GRLIFGAGIGLLTYLIRTFGGYPEGVAFAILLMNAAVPLIDRYTRPRVFGHV
>gnl|CDD|443697 COG4659, RnfG, Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfG subunit [Energy production and conversion]. Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfG subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
MKSILKMALILGLIALVAGGLLALVYELTKPPIAANEAEALLAALKQVLPEASFDNDLLADTLTVTDPEG
SGGPLTVYRARKGGEPVGYAFEAAPDGYGGPIKLLVGIDPDGTILGVRVLSHKETPGLGDKIEERSDWIL
QFKGKSLDNPDARWAVKKDGGEFDAITGATITSRAVVKAVNRALEFFKEHRA
>gnl|CDD|443698 COG4660, RnfE, Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfE subunit [Energy production and conversion]. Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfE subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
MSYKKIFTNGLWKNNPVFVQLLGLCPLLAVTTSATNGLGMGLATTFVLVCSNILVSLLRNLIPDEVRIPV
FIVIIATFVTIVDLLMNAYFPELYKALGIFIPLIVVNCIILGRAEAFASKNPVLPSALDGLGMGLGFTLA
LVLLGAVRELLGAGTLFGITLFPESYQPFLLMILPPGAFIVLGLLLALKNWIDKRKKARAKAAAAAAAA
>gnl|CDD|443699 COG4662, TupA, ABC-type tungstate transport system, periplasmic component [Inorganic ion transport and metabolism]
MDYILEGFAEALRLLLSGDPELWEIVLLSLRVSLTATLIAALIGLPLGALLALKRFPGRRLVISLLNTLM
GLPPVVVGLLVYLLLSRSGPLGFLGLLFTPTAMIIAQTVLALPIVAALTRAAVEDLDRRLRETLRSLGAS
RLQALLTLLWEARFGLLAAVLAGFGRAISEVGAVMMVGGNIKGYTRVMTTAIALETSKGEFALAIALGIV
LLAIALLVNALLSLLQGRGRRR
>gnl|CDD|443700 COG4663, FcbT1, TRAP-type mannitol/chloroaromatic compound transport system, periplasmic component [Secondary metabolites biosynthesis, transport and catabolism]
MKRRSFLKGAALGAAAAAAALAAPAIAQAQPTIRWRMVTSWPKSLPGLGGAAERFAKRVEEMSGGRLKIK
VFAAGELVPAFEVFDAVSNGTVEMGHTASYYWKGKDPAFAFFTAVPFGMNAREMNAWLYYGGGLELWREL
YAKFNVVPFPAGNTGAQMGGWFRKEINSLDDLKGLKMRIPGLGGEVLAKLGAVPQQLPGGEIYPALERGT
IDAAEWVGPYDDEKLGFHKVAKYYYYPGWHEPGTQLELLVNKKAWDALPKDLQAIVEAAAAAANADMLAE
YDARNPAALKRLVAEGVKLRRFPDEVLDALRKAADEVLAELAAKDPLFKKVYDSQKAFRKDVRLWFRVAE
LAYLNF
>gnl|CDD|443701 COG4664, FcbT3, TRAP-type mannitol/chloroaromatic compound transport system, large permease component [Secondary metabolites biosynthesis, transport and catabolism]
IELLALLMFGGLLVLLLLGFPVAFALGGVALVFGLIGFGPAGLGLLPNRIFGVMTNYTLLAIPLFVFMGV
MLERSGIAEDLLDAMGQLFGRLRGGLAIAVVLVGALLAASTGIVGATVVTMGLIALPAMLRRGYDKRLAT
GVICASGTLGQLIPPSIVLILLGDQAGVSVGDLFAGALIPGLLLAGLYILYILIRAWLNPELAPALPAEE
RALWALLLRLLKALIPPLLLIFAVLGSIFAGIATPTEAAAVGALGALLLAALRRRLTWKVLREALRSTLK
ITAMVFWILIGATAFSLVFRGLGGDELVEELLTGLPGGPWGFLILMMLIIFLLGFFLDWIEIILIVVPIF
APIVQALGFDPIWFGVLFAVNLQTSFLTPPFGFALFYLKGVAPPEVTTGDIYRGVIPFILLQLLGLALVI
LFPQLATWLPSLLYG
>gnl|CDD|443702 COG4665, FcbT2, TRAP-type mannitol/chloroaromatic compound transport system, small permease component [Secondary metabolites biosynthesis, transport and catabolism]
ALLRLSRAIDRLNRWIGRLAAWLILALVLLIVYEVVLRYLFNAPSIWALELQWYLFAAIFLLGAAYTLRR
GGHVRVDILYGRLSPRTRAWLDLLGTLLFLLPFCLLLLWASWPFALRSWAIGERSSSAGGLPLWPIKALI
PLGFALLALQGLAELIRAIAALRGREPPPE
>gnl|CDD|443703 COG4666, COG4666, TRAP-type uncharacterized transport system, fused permease components [General function prediction only]
MSETSSEDAEELLEEESGFRRLTGWLGKLIFALAVALSLFQLYTAGFGPLPALQQRAIHLGFALALAFLL
YPARKKSPRDRIPWLDWILALLALAAALYIVLNYDDLVLRAGFPTTLDLVVGIILILLVLEATRRTVGWA
LPIIALLFLLYALFGPYLPGILAHRGYSLERIVSHLYLTTEGIFGTPLGVSATYIFLFILFGAFLEKTGA
GKFFIDLALALAGRSRGGPAKVAVVSSALMGSISGSAVANVVTTGSFTIPLMKRVGYPPEFAGAVEAAAS
TGGQIMPPIMGAAAFIMAEFLGVPYLEIVLAAIIPALLYYLGVFLMVHLEAKKLGLKGLPKEELPSLKEV
LKEGWHLLLPLAVLVYLLVSGYSPMRAAFWAILALIVVSLLRKETRMTLKDILDALEEGARNALPVAAAC
AAAGIIVGVVTLTGLGLKFSSLIVSLAGGNLFLALLLTMVASLILGMGLPTTAAYIILATLAAPALIQLG
VPPLAAHMFVFYFGILSDITPPVALAAFAAAGIAGADPMKTGFQAFKLALAAFIVPFMFVYNPALLLIGS
WLEILLAVVTALLGVFALAAALQGYLFRRLNLWERLLLLAAALLLIYPGLLTDLIGLALLALLLLLQLLR
RRKER
>gnl|CDD|443704 COG4667, YjjU, Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism]
SNMMKTALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALNGASYLSRQPGRARRVITDYATDPR
FFSLRNFLRGGNLFDLDFLYDEIPNELLPFDFETFKASPREFYVVATNADTGEAEYFSKKDDDYDLLDAL
RASSALPLLYPPVEIDGKRYLDGGVADSIPVREAIRDGADKIVVILTRPRGYRKKPSKFKRLLRRLYRKY
PKLVEALLNRHERYNETLEFIEQLEKEGKIFVIRPPKPLTVSRLERDPEKLRALYELGYEDARKFLAELK
A
>gnl|CDD|443705 COG4668, MtlA2, Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and metabolism]
MLILTKENIRLNASAANKEEAIRLAGQLLVEAGYVEPEYIDAMLEREAQVSTYLGNGIAIPHGTNEAKDL
VLKTGISVLQFPDGVDWGDGNTVYLVIGIAAKSDEHLEILRQLARVLSDEENVEKLAKATDAEEILALLT
GEN
>gnl|CDD|443706 COG4669, EscJ, Type III secretory pathway, lipoprotein EscJ [Intracellular trafficking, secretion, and vesicular transport]
MSRRLLRLLLLLLLLLLLTGCKVELYSGLSERQANEMLAVLLEHGIDAEKVPEKKGGWTITVDESDFARA
VEILREYGLPRPSFVSLGDVFPKDGLVSSPTEERARLIYALSQELEQTLSQIDGVLVARVHVVLPENDPL
GEKPKPASASVFIKYRPGIDLDLLEPQIKRLVANSVEGLSYDNVSVVLVPAEPRQAPPPAEARSPVASRS
AAWLLLLGGLLLLLLALAGALGLLLW
>gnl|CDD|443707 COG4670, YdiF, Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism]
SKIISAEEAAALIKDGDTVATSGFVGAGVPEELLKALEERFLETGHPRDLTLIHAAGQGDGKGRGLDHLA
HEGLVKRVIGGHWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGTFVDPRLEGGK
LNERTTEDLVELVEIDGEEYLFYKAFPIDVALIRGTTADEDGNLSMEHEALTLEVLAIAQAAKNSGGIVI
AQVERIVKRGSLHPKDVKVPGILVDYVVVAPPEDHMQTFSTQYNPAYSGEIRVPLSSLPPLPLDERKVIA
RRAAMELRPGAVVNLGIGIPEGVAAVAAEEGISDLITLTVESGPIGGVPAGGLDFGAAVNAEAIIDQPDQ
FDFYDGGGLDIAFLGFAQVDRHGNVNVSKFGGRIAGCGGFINITQNAKKVVFCGTFTAGGLKVEVEDGKL
RILQEGKIKKFVKKVEQITFSGKYARERGQEVLYVTERAVFELTPEGLELTEIAPGIDLERDILAQMEFR
PIIADDLKLMDARIFRDEPMG
>gnl|CDD|443708 COG4671, COG4671, Predicted glycosyl transferase [General function prediction only]
MSMRILFYSHDLLGLGHLRRSLAIARALVADGFSVLLISGGPPAPGFDLPPGVDVVRLPGLRKDSFGEYL
SRDLGPDLEAVLALRSQLLLAAFEAFQPDLLIVDKFPFGLRFELLPLLEALRARGPRTRVVLSLRDILDE
PSVLRREWREEEVLDLIERYYDAVLVHGDPDVYDLEESFPLPAEIADKVRYTGYVARPAPEPPPEERDAL
GLLPEEPLILVSAGGGGDGAELLEAALAAAELLPPPDHRWLLVTGPFMPAADRAALRARAAALPNVTVER
FTPDFEALLAAADLSVSMGGYNTVCEILSTGKPALIVPRTAPRTEQLIRAERLAELGLVDVLHPEDLTPE
ALARAIAAALARPPRRSPLDLDGLARTARILAELLGARSAA
>gnl|CDD|443709 COG4672, gp18, Phage tail protein [Mobilome: prophages, transposons]
MMITADLQKLEPGALVRLFEVDGTAFGGDVLRFHAGTNEKAKSIWWQGNEYDAWPIQAEGFELSGDGSSA
RPTLTVANLDGLITALCLDFDDLVGAKVTRHDTLAKYLDAVNFPEGNPTADPTQEAVSVWYIEQKSSETA
ETVTFELSSPADLQGAQIPTRQITNLCTWCIRGGYRGDGCGYTGPAYFDEKDNPTDDPALDKCSGRLTGC
KLRFGENNPLPFGGFPSASLIRR
>gnl|CDD|443710 COG4674, COG4674, ABC-type uncharacterized transport system, ATPase component [General function prediction only]
MSLDTMHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFG
GTDLTGLDEHEIARLGIGRKFQKPTVFEELTVFENLELALKGDRGVFASLFARLTAEERDRIEEVLETIG
LTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDM
EFVRQIARKVTVLHQGSVLAEGSLDEVQADPRVIEVYLGR
>gnl|CDD|443711 COG4675, MdpB, Phage tail collar domain [Mobilome: prophages, transposons]
MDPFIGEIRLFAGNFAPRGWALCDGQLLPISQNQALFSLLGTTYGGDGRTTFALPDLRGRVPVGQGQGPG
LSPRVLGQTGGTETVTLTTAQLPAHTHTLNASSAAGTTTTPAGNVLAAGTGGGVNIYASGTPNVTLAPGT
VGPTGGSQPHNNMQPYLALNFIIALQGIFPSRN
>gnl|CDD|443712 COG4676, YfaP, Uncharacterized conserved protein YfaP, DUF2135 family [Function unknown]
LGNEPGDLRVVLTWDTDPADLDLHVVEPDGEHVYYGNKLTPNGGRLDVDDTDGYGPEEFTIRKAPPGTYL
VNVNYYGNGGQAPTTAKVTVYTNYGTPDEKRETVVVPLNKKGELWTVGSFTVGNG
>gnl|CDD|443713 COG4677, PemB, Pectin methylesterase and related acyl-CoA thioesterases [Carbohydrate transport and metabolism, Lipid transport and metabolism]
LLLLALASAPAAAAADYDLVVAQDGSGDFTTIQAAIDAAPAFSTERTTIYIKNGVYREKLVIPSNKPNIT
LIGEDRDKTIITYDDYAGKPNPDGEKWGTFGSATVFVDGDDFTAENLTIENTAGPVGQAVALYVEGDRAV
FRNCRFLGNQDTLYANGEGGRQYFKNCYIEGTVDFIFGGATAVFENCEIHSKGNGYITAASTPEGQPYGF
VFRNCRLTADAPAGSVYLGRPWRPYAKTVFINCEMGAHIRPEGWHNWGGPENEKTARYAEYGSTGPGANP
SKRVSWSKQLTDAEAAAYTLENVLGGW
>gnl|CDD|443714 COG4678, COG4678, Muramidase (phage lambda lysozyme) [Cell wall/membrane/envelope biogenesis, Mobilome: prophages, transposons]
SPPSMPRIPPLVMSGGDPNVRAFLRTIAASEGTDGSDDGYRVLYGGGLFSDLSDHPRICVTIVIPNKGNC
STAAGRYQFLNTTWDEYAKKLGLPDFSPESQDRVALQLLRDRGALELIRAGRIEEALKKLSGTWASLPGA
GYGQEENSTDKLPAIYQKALGEELAG
>gnl|CDD|443715 COG4679, COG4679, Phage-related protein [Mobilome: prophages, transposons]
KMKPVEFYGTKEPVLDFLLALPAKVRAKIGRALDLLQEGGPDLGKPLTKGLGDGLFELRIKGGSGIYRVL
YFAKFGDAVVVLHGFQKKTQKTPKKEIELARKRLKEYLEEKKE
>gnl|CDD|443716 COG4680, HigB, mRNA-degrading endonuclease (mRNA interferase) HigB, toxic component of the HigAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis, Defense mechanisms]
RIISRKTLREFWEKHPDAEQALDAWYREAKKADWKNPADLKKTFPSADIVGNNRVVFNIKGNKYRLIVAI
NYERQIVYIKFIGTHAEYD
>gnl|CDD|443717 COG4681, YaeQ, Uncharacterized conserved protein YaeQ, suppresses RfaH defect [Function unknown]
ALKATIYKAELQLADMDRGYYADHSLTLARHPSETDERMMVRLLAFALNADERLAFTKGLSDDDEPDLWQ
KDLTGRIELWIEVGQPDEKRLRKACGRAERVVVYAYGGRAADVWWQQNQGKLARLDNLSVYQLDAEQLQA
LAALAERTMQLQVTIQDGQLWLSDGGGSVEITPERLKGPA
>gnl|CDD|443718 COG4682, YiaA, Uncharacterized membrane protein YiaA [Function unknown]
MTQKPSAAFIGASWAALLIGFVAYLIGLWNAEMQLNEKGYYFTVLLFGLFSAVSLQKSVRDRLEGIPVTD
IYYGLSWFSTIASILLLVIGLWNATLLLSEKGFYAMAFLLSLFAAIAVQKNTRDLQSFKSLEGEINGE
>gnl|CDD|443719 COG4683, COG4683, Uncharacterized conserved protein [Function unknown]
MMWEVEFTDEFEEWFDALDEDVQEEVLAALLLLEEFGPQLGRPYVDTLKGSRHANMKELRVQSAGGPIRV
FFAFDPRRQAILLVAGDKSGNEKRFYRQLIPIADRRFDEHLAELKKEEG
>gnl|CDD|443720 COG4684, COG4684, Uncharacterized membrane protein [Function unknown]
MAKSKKKTRRLVILALLIAIIIVLGFTPLGFIPLGPIKATIIHIPVIIGAILLGPKVGAILGLVFGLFSF
IRATTAPTPLSFVFSPFPFTNPLISVVPRILIGILAYYVYKLLKKRKKNQALALGIAAVLGSLTNTILVL
GMIYLFFADAYAQALGISATALLGVLLGIVGTNGIPEAIVAAIITPAVVKALKKIL
>gnl|CDD|443721 COG4685, YfaA, Uncharacterized conserved protein YfaA, DUF2138 family [Function unknown]
MALSRKKYAGLALGVVAVLLAAGAWVFGRLAPRAVRHNALQIDLRQPDALLDSRSLSQLPKDLLAVPLLR
DVLTEDFVFYYENNEDRLSLEGSLRRIAYEHDLTLKDRLLAALLDEPAEIALWRSGDGRLGHFVLRLERN
GLARLLEPLAKVALSDRQLSKVGKIKLGGAKVPVYALRYGGRRALLFASHGDRLLVLSDPGMLLDKDGTL
LGDAAKVLGALLSGDVNPWAAAFGLPARGPSAHRIVVSANYLSFGYQRFFPAFAALRFDFGDEGWQSSAL
LNDASLQAQWDFAPLWRALPAGAALCVALPVDWKRAEGLLERLSGEAAAAAALLAALDGAAGVCWYPDSR
LYAPLFVARLAEAAEADLDQTLGKLFGQVIGAHEAKAAGDEYSRLPVQTRKQAGAQLWQRAVSSRYGAYP
KSGADFADQLSGARYFRVSLARSGSTLLFSPDDRLVDDALAVLDKRYPALADVLPPDGPVPLYAAPEQLA
KLLRREVLASLPADAEPVFRNAARTLLLPKLDALAQQPPYALALPAAVQPGGSTGWVPLEWQPLAAR
>gnl|CDD|443722 COG4687, COG4687, Uncharacterized conserved protein [Function unknown]
MVQSLNTKVDLVTKATSYLGLTDYGKIMIGDKAFEFYNDRNVEDYIQIPWEEVDYVAASVMFKGKWIPRF
AIFTKKNGTFTFSSKDPKKVLRAIREYIGPDKMVRSLSFFDVIKRGFKSLFKKKK
>gnl|CDD|443723 COG4688, COG4688, Uncharacterized conserved protein [Function unknown]
MNNVILFIPKAELDAKKNLEAFIKFCRDLLTVYGDQLDWEGNKWDTTTGHKGRVAARFSTLAEKNKPYKY
DPLSEPFLSFAKAYIRYQQGVKPVKNIGNIMRALRVLEDALLEIGGSADILQLTAVVLDRAVELARKRFE
GAAAYRLGGQLEKLADFLREKHLAPSLPSWKNPLKRPRDKRERLDKEAKAWREEKLPSDEALLALADIFQ
DAPSPRDILTSSVLALLMCAPSRIGEILSLPADCEVEEIDGKGDGRYGLRWYGEKGYGDTIKWVPEVMAD
VAKEAIARLRELTRPARRIAKWYEENPDQFYLHEDCPDLREKAPLTVLEFAAALGFEDRSRLHDLQSSQK
WIKRNGLSLMRNDGSYTFSELEEAVLSKLPRSFPYLDKGKGLKVSEALFLVRKNEFHEDRGTKRFSFVAP
TVNQINSALGRRRHNGKSIFDRFGYSDEDGSPIRLTSHQLRHWLNTLAERGGMSELEIAKWSGRADVAQN
RAYDHRTEEEKLAQIRDILENHKNAPGPLVAIRLNIPVSREDFGKLRAGTAHVTEYGFCVHDFAMSPCSK
HGDCITCKEHVCVKGLPDKLERLKSLEAKVEAQLEIAKEALADGTFGADRWVAHHGWTLDRIRKLLTILE
DPSVPDGALIRLPVEL
>gnl|CDD|443724 COG4689, Adc, Acetoacetate decarboxylase [Secondary metabolites biosynthesis, transport and catabolism]
MKRDDVKLKGFSMPLTAPSYPPGPYRFYNREYLTIEYRTDPEALRALLPEPLEPAEPLVAYEFIKMPDSS
GFGQYTEAGQVIPVRYEGEPGSYCPYMYLDNDAAIAAGREIWGFPKKLGNPKLTRDGDTLVGTLDYGGVR
LATATMGYKHRALDLEETLASLPGTPNFNLKIIPHIDGGPAICELVRYYLTDVTVKGAWTGPARLELFPH
ALAPLADLPVLEVVSGYHFIADLTLPGGEVVHDYLA
>gnl|CDD|443725 COG4690, PepD, Dipeptidase [Amino acid transport and metabolism]
ACTTILVGKKASADGSTIIARNEDSGAFYPKRFVVVPAPDHQPGTYKSVLSGFEGPLPQVPLRYTYVPDA
YDKDGIWGEAGINEAGVAMSATETITTNERVLGADPLVEDGIGEEDLVTLVLPRIKTAREGVELLGELIE
KYGTGEGNGIAFADKDEVWYLETIGGHHWVAQRVPDDAYAVAPNQFRIDEVDFDDPENFMASKDLKEFAE
ENGLYDPEDGPFNFRKAYGSDSESDHYYNTPRVWRGQKLLNPSLELDPDSDDYPFSVKPDKKISVEDVKY
ILRSHYEGTPYDPYGGLGTLAEKEWFRPIGINRTQESHILQIRPDLPDEIGGVQWLAFGSPAFSVYVPFY
AGITDTPESYKNGTDEFDTDSAYWAFRLIANLADLHYQEYAPDVEAYQEPLEAKLIAEQAEIDKEALELY
KKDPEKAREYLTEANQEMAEEALKKTKKLLDELLTKYSNGMKNTFSRSD
>gnl|CDD|443726 COG4691, StbC1, Plasmid stability protein StbC1, contains ribbon-helix-helix domain [Defense mechanisms]
TLTIRNLDDEVKRRLKVRAAQHGRSMEAEVRAILRAALSPPPRSPGLGEALRARFAEAGGTDLELPPGRD
EAPREPPSF
>gnl|CDD|443727 COG4692, COG4692, Predicted neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]
MKLKLALLFLLLFLALLSAPAAAEPGILRSEFIFEPAPFPQCHASTLVELPNGDLLAAWFGGTREGAPDV
SIWVSRLDKGSGKWSAPVRVATGEQDDPRRPLWNPVLFLAPDGRLWLFYKVPSPGGWWGSLIRVRTSTDG
GKTWSPPERLPEGPFLIGGPVRNKPVVLSDGRILLPSYTESGGKWRSHVEISDDGGKTWTKSPIPKGFGA
IQPSILELKDGRLQALMRSRGAGRIYRSESTDGGKTWSPPEATDLPNPNSGIDAVTLKDGRLLLVYNPTS
AGGGGRTPLSLALSDDEGKTWKDVRVLEDGPGGEYSYPAIIQTSDGLLHITYTWNRKAIKHVVFDPAWLK
AGK
>gnl|CDD|443728 COG4693, PchG, Oxidoreductase (NAD-binding), involved in siderophore biosynthesis [Inorganic ion transport and metabolism]
MSKPLRVVVCGSTFGEVYLNAFKQPPPGFELAGLLARGSERSRALAERFGVPLYTSPEQLPDDIDIACVV
VRSTVVGGEGTQLAEALLSRGIHVLQEHPVHPDEIARLLRLARRHGVHYWVNTFYPHLPAVRRFIEAARQ
LRRRQRPLYIDATTSRQLLYSLLDILGRALGGLRPWSFADVGQDPGPFRTLRGVLAGVPLTLRVQNELDP
ADPDNHSLLMHRITLGTPAGYLTLTDTHGPVIWSPRLHVPRHQDGLLSLYRRAAGPDAEHLDLPSSETLG
PAAPPSWRDIFEEDWPEAIARALSELRAALAGGQVPARRAQYQLALARLWQQLLRALGPPELVSGAPPRP
LSLDDLLAAAEE
>gnl|CDD|443729 COG4694, RloC, Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]
MITKIKKLKNVGAFKDFGWLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFEIEAGGSAPN
PSVRVFNRDFVEENLRSGEEIKGIFTLGEENIELEEEIEELEKEIEDLKKELDKLEKELKEAKKALEKLL
EDLAKSIKDDLKKLFASSGRNYRKANLEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALL
SEAETLLEKSAVSSAIEELAALIQNPGNSDWVEQGLAYHKEEEDDTCPFCQQELAAERIEALEAYFDDEY
EKLLAALKDLLEELESAINALSALLLEILRTLLPSAKEDLKAALEALNALLETLLAALEEKIANPSTSID
LDDQELLDELNDLIAALNALIEEHNAKIANLKAEKEEARKKLEAHELAELKEDLSRYKAEVEELIEELKT
IKALKKALEDLKTEISELEAELSSVDEAADEINEELKALGFDEFSLEAVEDGRSSYRLKRNGENDAKPAK
TLSEGEKTAIALAYFLAELEGDENDLKKKIVVIDDPVSSLDSNHRFAVASLLKELSKKAKQVIVLTHNLY
FLKELRDLADEDNKKKNCAFYEIRKDNRGSKIIKLDLLNPYESEYHYLFKEVYDFAEGGDSLYLIPNAMR
RILEAYLRFKYPDKLDELLEDDEEEKKSLYRYINRFSHGDNSTDSLLEEYKSVFRRIFEFIK
>gnl|CDD|443730 COG4695, BeeE, Phage portal protein BeeE [Mobilome: prophages, transposons]
MGFFRRLKERRSLSDALGLGGPTASGRSVTPETALRNPAVFACVRLIAEAIASLPLKLYRRTADGGERAD
DHPLYRLLNDRPNPWMTGFEFREALVAHLLLRGNAYAEIVRDGRGRPVELYPLRPDRVTVVPDDDGRLAY
RYTDLGGRTVTLPADDVLHLRPLSLDGLYGLSPIEAAAEAIGLALAAERYAAALFKNGARPSGVLKYPGK
LSDEQAERLREEWEAAYSGAENAGKPAVLEGGLDYKPLSLSPEDAQFLESRKFAAEEIARAFGVPPHLLG
DLGDATYSNIEQQNRAFVRDTLLPLLTRIEQELNRKLLTPFERGLYLEFDVDALLRADSKTRAEAYAKAV
QAGFLTPNEARALEGLPPIPGGDELLVPLNMTPLEDLGGKEPD
>gnl|CDD|443731 COG4696, MazG2, NTP pyrophosphatase, MazG superfamily [Nucleotide transport and metabolism]
MSMKDPFNLVKEFHRTFDLPILETPTAPSEERAKLRASLLAEELVELLEAAEEGDLVEVADALGDLLYVL
YGTILEHGIDLEAVFDEVHRSNMSKLGPDGKPIYREDGKVLKGPNYFPPDIKAELERQKQ
>gnl|CDD|443732 COG4697, COG4697, Uncharacterized conserved protein, DUF2139 domain [Function unknown]
MLYRFPPRYGPEWGSGGIFGLKYHRGVLYYTLAFEAEAHFIHDDSEKIYRFELVGPPPTSGGDTYNAVEA
VDDFIYFGGWVHAPAIYRGKREGRGATIDFTNKYSHVHEYDIEERSVRLLWKESIHHETEWAGEVSEIIY
DPYTDRLLLARADGHINLGVYEIDRRRGKARKLSSKPSLKGAIFHDYACFDIGHNWTKGVEGIQCLDLIE
GKWVYFKLGDPSKYSVDGGGVERPLLGAVASAYNRVFAFVRGGIFVGNPVNGEEFRFVRLFDFPYTFYAP
FRSNALPIGGGVLIAFNAYHDAYYRPTNEEEEVVARATNTIVGPSVLVYIAPPMAKIVGAFGARITSMEK
VGDKILLATNTTPNTGRYDATPFDTGVRGILVLDEDILLENPPPPSFSVPLGLIVDDVFFGGPPLGGYRP
LLLIVAGKKNNLIIYEYYLSLPPPDARETDTYILSEGNNRLDLSNVVSISSFKLEEPDERKRIIIILL
>gnl|CDD|443733 COG4698, YpmS, Uncharacterized conserved protein YpmS, DUF2140 family [Function unknown]
MTKKKKNKWKWAFFILLALNIILVAVIFVLLTQPVEEDSPSEPTEVKESDAEFTVSTTKEQLNALANSYL
EDYLKDSKLPYSVELDDDIELTGEIKLLGQDVPFYMYFEPEVLENGNVLLKQKSLSVGKLPLPISTVLKY
IKKSYDLPDWVTINPKKEQIYVDLTEIPLDKGLRVKAKKIDLKKDEISFDIYIPKK
>gnl|CDD|443734 COG4699, COG4699, Uncharacterized conserved protein, DUF1033 domain [Function unknown]
MYQVIYMKGDYEPWWFFDGWEEDIVEEEEFDTFEEALQYYKELWAELSKKYPNYKTKKYYLTAFWNEEEK
EYCEDCDEDLQIYHGLILLKDGKVIPSEKEREGF
>gnl|CDD|443735 COG4700, COG4700, Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown]
MPFLGYYLHLLLQLFCAVHAVRTGRERYWIFIIFFLPLLGCLIYFFAEVLPELRNSRDARRVQRAARNAL
DPGRELRELEKALEFADTVQNRVRLADALLELGRYDEAIELYEEALTGIFADDPHILLGLAQALFELGRY
AEALETLEKLIAKNPDFKSSDAHLLYARALEALGDLEAAEAELEALARRYSGPEARYRYAKFLARQGRTA
EAKELLEEILDEAKHMPKHYRRLNREWIREAKKLLKSLR
>gnl|CDD|443736 COG4701, COG4701, Uncharacterized conserved protein [Function unknown]
MRDSRPQSLDSLLQQASSLAQIQQRAKALLKLNRAVRALLPAELAPHCRVANYRQGILVLEVDSAAWATR
LRYEQPRLLSALRQQILPSLSSIEIKINPSLARKAPPKQQRPTKLSEQAAELLRELAENSPPKLKEALER
LAALA
>gnl|CDD|443737 COG4702, COG4702, Uncharacterized conserved protein, UPF0303 family [Function unknown]
MDLEDDLAELAEQEARLQFPSFDNDDAWELGSRLVELARARGLPIAIDIRLGGQTLFHAALPGTTPDNDD
WIRRKRNVVLRFGRSSYAVGLRLEAKGTTLEERYGLDPADYAAHGGAFPIRVRGVGVVGAVTVSGLPQRE
DHALVVEALAAFLGRDLAAL
>gnl|CDD|443738 COG4703, YkuJ, Uncharacterized conserved protein YkuJ, DUF1797 family [Function unknown]
SQLLAIIQRLEAMQEDDDNEVQVRRFEKNGEEVCSVKYDPKTETFELEEYRKGQTYQFDDIDLVAIEIYE
LLQ
>gnl|CDD|443739 COG4704, COG4704, Uncharacterized conserved protein, DUF2141 family [Function unknown]
MKRILLLLALLLAALAAAAQAATLTVTVTGLRSDKGQVRVALYNSEEGFPKGGKAVKSQKVKIKGGTVTV
TFENLPPGTYAVAVFHDENGNGKLDTNFLGIPKEGYGFSNNAKGSFGPPSFEDAAFEVDGDNTTITIKLK
>gnl|CDD|443740 COG4705, COG4705, Uncharacterized membrane-anchored protein [Function unknown]
MSTSKSSARQALSKVPEVTLLFWIIKILATTLGETAGDFLSMTLGLGLAVTTAIFGALFAVALFAQLRAK
RYVPWLYWLTVVATSTFGTLIADFLDRSLGVPYAGSTLLFAVLLLAVFALWYRSEGTLSIHSITTRRREL
FYWLAILFTFALGTALGDWLADTLGLGYLGSALLFGALIAVVALAYYFTRINRVLLFWIAYILTRPLGAS
FGDLLSKPVANGGLGLGTGGASLVLLALIVALVVYLTLRRRRVAHASTV
>gnl|CDD|443741 COG4706, COG4706, Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism]
MNPTLDRPPIAALIPHRGPMCLLDRVLAWDEESAVAEVTIRPDNPFRDDGGLPAWVGIEYMAQAVAAHGG
LLARAAGEPPRLGFLLGVRKVELHVPRFPVGETLRIEAERLLQDEGLGLFECRIRAGGELLASGRLNVFQ
PADAEAFLL
>gnl|CDD|443742 COG4707, COG4707, Prophage pi2 protein 07 [Mobilome: prophages, transposons]
MLQTLEVSIPIPEDKVLISKVEYEELKEESLDGRWWSMKDLEERTNKSRDWLKDNILYSPRFRKELDVEN
GGFVYYPKGKGSRWSFLAKKMAKFLDKHFEEI
>gnl|CDD|443743 COG4708, QueT, ECF-type transporter of queuosine precursor, membrane (S) component [Nucleotide transport and metabolism, Translation, ribosomal structure and biogenesis]
MKKMKTKRLALAAIIAALYVVLTLLLAPISFGPIQFRISEALNLLPFFNPKYIPGLTLGCFIANLFSPLG
LIDVIFGSLATLIAALLTYKLRKKYLAPLPPVIVNALIVAAELNILLGLPFWLTMLTVALGELIVMYVLG
APLLYALNKRIDFKKRIA
>gnl|CDD|443744 COG4709, COG4709, Uncharacterized membrane protein [Function unknown]
MNKEEFLNELRKYLKGLPAEEREDILEDYEEHFDDGLEEGKSEEEIIAELGDPKEIAREILAEYGIKKAE
AKPSPSNISRAILALIGLGILNFPIVLPLLLGLLALLFALFIVALSLIIAPLALLIALILGGIGSSLAAI
FFGIGLLLIGLGLLLLIGLIYLSKLLVRLIVRYLKWNIR
>gnl|CDD|443745 COG4710, COG4710, Predicted DNA-binding protein with an HTH domain [General function prediction only]
MKMLSIRLPEELEARLDALAKRTGRSKSFYVREAIEEYLDDLEDYYLAEERLERVRAGREKTYSLEEVER
DLGLED
>gnl|CDD|443746 COG4711, COG4711, Uncharacterized membrane protein [Function unknown]
MERFTLADLAQQIVGALLLAFPFAPTEEVWLLAASMSPWHLLALVALSLLIGYGILYQADFRGQKRREPQ
VGGVPRRTVSVYLVSLLVSALLLWFFGRLDTGDPWTVALKAVIVLGLPAVIGAAAGDLLL
>gnl|CDD|443747 COG4712, DdrA, Predicted ssDNA annealing protein, contains HHH motif, Rad42/Rad22/RecT/erf family [Replication, recombination and repair]
MEKAEILERLAAPFPPEEVEWRVQALSKDKTRALVLPYVDARAVMDRLDAVFGPEGWQNEYRPLGEGGVL
CRLTVRIPDEWVTKEDGAERTDVEPVKGGISDAFKRAAVQFGIGRYLYDLPKVWVDYDDEGRLWNPPQLP
EWALPEGESLAEPDSATLPDRAEASAAPAPPREDAARVPEAAREKPAGKEAIERLIDRLRAEGKGRAVGE
LVV
>gnl|CDD|443748 COG4713, COG4713, Uncharacterized membrane protein [Function unknown]
GDFDSLWSKREEFNGFPGTVIYSPIVYLPQAIGIALGRLLGLSILLTYYLGRLANLLVYAALLFLAIKLA
PRGKWLLALLALLPMTLFLAASLSQDGLTIALAFLLIALVLRLAFRRDPLSRRQLILLLLLFGLLALSKP
PYFPLLLLPLLIPIRKFGSRRQRWLLLLLALLLAAILLLIWLKVYSPITVPFRLGRGVSTSAQLHFVLSH
PLEFIAILFRTLLLYLLFYIRQFIGVLGWLDTPLPAWFYLAYLVLLLAAALLDNKRAIRLTLLERLGLLL
VALASVLLVFLALYLTWTPVGATVIDGVQGRYFIPIAPLVFLLLPNSPPVRPQIRKKAALLLLTVFLLLS
LAVLVSTLLARY
>gnl|CDD|443749 COG4714, COG4714, Uncharacterized membrane-anchored protein [Function unknown]
MTMMRIILAALLLLALLLAAAQAQEAAEQEELEAAVEAALASLQPGPGKISLGDQATLDLPEGFAFLPAA
DAQRVLELWGNPPDEDLLGMIFPAGEDDSWGVVIEYEDDGYVKDDDAKDIDADELLKSMQEGTEEANKER
VERGYEALELVGWAEPPHYDAATHKLYWAKELKFGGADENTVNYNTRALGREGYLSLNLVADMDQLAAIK
PEAQQLLAMAEFNDGKRYADFNPSTDKVAEYGLAALVAGGAAAKLGLLAVIGAFLKKFWKFIVLGVAALG
ALLKKLFGRKKS
>gnl|CDD|443750 COG4715, SWIM, Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown]
MARLELTEDDIRRLAGPRIFERGREYAREGRVLDLDVEDGRLEATVQGSEDYRVRVDLDDGGDLDSSCTC
PYGGGGFCKHVVAVLLALLDQPEEGAPRQSEREALEELLERLSKEELVELLLELAAEDPELRELRRALDD
SGGDYLREELLELSRLAALSLTATLAALAPRSTLALRLALLRLLLLLLAPSSLDGAPPGLSLALVRELLP
ALAERALALLLLVPAPAGLLKLRLLLARPGALLLSLLDLLLRLDLLLGLLLLALLLLLLLLLQLLALLLL
ALRTLAALLLLLRLRLRLGLAAGLALAVLLLLLLLLLPLPLALLALSLLLRLLLALLRLALLVLLYLLLI
LLLLALLLLALLLLLELLLLLALLLLLAEVELARLLEEALLIRRRLLLLLLLLLRLLDLLALLALRLLLL
LLLAVLSEAEDLLLELLETLGLHRLLLLEAREELLPELAADLALLLLLEALDLLALEALALLLLLELLLL
LAVTLLLLAIDELLLLAL
>gnl|CDD|443751 COG4716, COG4716, Myosin-crossreactive antigen (function unknown) [Function unknown]
MYYSNGNYEAFARPRKPEGVDDKSAYLVGSGLASLAAAAFLIRDGQMPGENIHILEELDLPGGSLDGAGD
PEKGYVIRGGREMENHFECLWDLFRSIPSLEDPGASVLDEFYWLNKDDPNYSKARLIHNQGEILDDGKFG
LSKKARLEILKLFLTPEEDLDDKTIEDVFSEEFFESNFWLYWRTMFAFENWHSALEMKRYLHRFIHHIGG
LPDLSALKFTKYNQYDSLVLPLVRWLKDHGVDFQYGTKVTDVDFDISGGKKTATAIHLERDGKEETIDLT
ENDLVFVTNGSMTESSTYGDMDTPAPLNTDGPGGSWELWKNIAAKDPEFGRPEKFCGNIEESNWESATVT
TLDDKILPYIEKITGRDPYSGKVVTGGIVTFKDSNWLLSWTVNRQPHFKNQPDDVLVVWGYGLFSDKPGN
YVKKPMRECTGEEILTELLYHLGVPDQIEELAANSANTIPCMMPYITAQFMPRAAGDRPLVVPEGSVNLA
FIGQFAETPRDTVFTTEYSVRTAMEAVYTLLGVDRGVPEVFPSQYDIRVLLKATYALNDGKKLPGEGLLL
KKLKGTYIEELLKEYKLI
>gnl|CDD|443752 COG4717, YhaN, Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]
MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLERLEKEADELFKPQGRKPELNL
KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE
LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE
LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF
LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ
ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEE
LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAE
EWAALKLALELLEEAREEYREERLPPVLERASEYFSRLTDGRYRLIRIDEDLSLKVDTEDGRTRPVEELS
RGTREQLYLALRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVELFQ
EEGAHVIELES
>gnl|CDD|443753 COG4718, COG4718, Phage tail protein [Mobilome: prophages, transposons]
AMETFTWPPQPGPTVEVTPRVRVVQFGDGYEQRAGDGINPLLRSWPLTFTGTEAEILAIDAFLRRHGGVK
SFLWTPPTGEQGLYRCDSWSVTPLGGGVYTLSATFEQVFAP
>gnl|CDD|443754 COG4719, COG4719, Uncharacterized conserved protein, UCP014979 family [Function unknown]
MKRASIAGLLAAALALASGSALAQAKQGPVQLNLTAEKEVITTDADGKEVEVLVPAATVVPGDVLRYTLT
YRNTGDRPATGLVITNPIPEGTIYVLASATGLGATITFSIDGGKTFGALPTLKVKLPDGKVETRPAPAED
YTHIRWVLSEPLAPGATGKVRYRVKVK
>gnl|CDD|443755 COG4720, ECF-S, ECF-type riboflavin transporter, membrane (S) component [Coenzyme transport and metabolism]
KNLSTKKLVLIALFAALVFVLTMFIKIPIPITNGYIHLGDAFIYLAALLFGPKAGALAGGIGSALADLLS
GYPIWAPWTFIIKGLEGLIVGLIAKKLKKKSFKKIILANILGGLVMVIGYYLAAPILYGGFAAALQSIPG
NLLQAVVGAIIALILLKALKKIRKKKGSLK
>gnl|CDD|443756 COG4721, YkoE, ABC-type thiamine/hydroxymethylpyrimidine transport system, permease component [Coenzyme transport and metabolism]
MSASARRARKRWRLVDIVVAAVLGVAFGVIFWAWGLLYNALSAALALGPGLQGLLYGVWLLAGVLAGLII
RKPGAALLAELLAALVEALLGSQWGPTVLISGLVQGLGAELVFALFRYRRFNLPVAMLAGALAALASFIY
DYFLGGYAALSPGYLLLYLVLRLISGAVLAGLLAWLLVRALAKTGVLDRFASGRERR
>gnl|CDD|443757 COG4722, YomH, Phage-related protein YomH [Mobilome: prophages, transposons]
MTDGFTFNGKNSSDLGIRLLKRPEIPSPERRVETVEIPGRNGVLTFDKGYEPRTITVECNVKPKNLEELR
SKIRAIAAWLDGEGYKDLIFSDEPDKYYRAKVTESIDIERELRSMGSFELTFICDPFKYAVTGEIFTILT
GSGTITNPGTIESEPIITIYGTGNITLTINGQEIKLNGVSGTVTIDSEKLEVYKDGGNALNNLLMTGDFP
VLDPGENTISWTGNVTKIEIEPRWRWL
>gnl|CDD|443758 COG4723, COG4723, Phage-related protein, tail assembly protein I [Mobilome: prophages, transposons]
SMRTIRLYGVLGKRFGRRHRLAVASPAEAIRALCVTIPGFEQFMRTSHKRGLTYAVFRGKRNIGEDELEL
PVGGADIRIVPVIIGAKRGGLFQTILGAALIVAAFFFGGGSLAAFGGGAAGALAMLGASMALGGVVQMLS
PQPKGLSSRQSPDNKPSYAFGGPVNTTAQGNPVPLLYGERRIGGAVISAGIYAEDQQ
>gnl|CDD|443759 COG4724, COG4724, Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism]
MKKNTRKLIAFSLLATSILFPSANEEYSQKIANQPYSSYWFPEDLLNWSPETDPDARYNRSRVPLAPRFT
GSATQINPTLSPDAKVMSLAIDNPNTSGNPSQGGSDFNVYTFTYWQYIDYLVYWGGSAGEGIIVPPSPDV
IDAAHKNGVKVLGTVFFPPGAYGGKIEWVDAFLEKDEDGSFPVADKLIEIAQYYGFDGWFINQETNGTDP
ELAKKMKEFLEYLKEKSPENMEIMWYDSMLENGSVSWQNALNEKNDAFLQDGNKKVSDSMFLNFWWTGGS
LLEKSRDTAKSLGRSPYDLYAGIDVQQNGYNTRINWDALLDDNKKPPTSLGLYCPNWTFNSSKNPDDFYD
NEQKFWVGPDGDPANTTDSNGWKGISTYVVEKSPVTSLPFVTNFNTGHGYKFYINGQQVSDGEWNNRSLQ
DVLPTWQWIVDSEGNSLTPSFDYTDAYNGGSSLKLEGKLKAGGETTIKLYKTDLPITDDTKLSVVYKTDA
KVKLSLGLTFKDGPTEFITFDLGTTSNNGWTTVTVDLSAYAGKTIAAISLKFSSTTDVDNYKINLGQLAI
FNGTTPPSAPPNNTTVSGQTLVDASASAFRLNWWSDASAYGEYHVLQVTNPNAKWLGTNTNNAATVAKTS
DRTVNAILFTITPIGAESISTPNKTATTTTIR
>gnl|CDD|443760 COG4725, IME4, N6-adenosine-specific RNA methylase IME4 [Translation, ribosomal structure and biogenesis]
MTASPSLPLPDGKYDTIYADPPWRFENRSGKGAPHSALNHYPTMSLDEIKALPVADIAADDAVLFLWVTN
PLLPEALQVMEAWGFTYKTAFVWVKRNKDGGPDGRGVGFYTRNNTELCLIGVRGNPRRLAPGRSQVQLIE
SPKREHSRKPDEFYELIERLSPGLPRLELFARQPRPGWDVWGNEADESIEPTG
>gnl|CDD|443761 COG4726, PilX, Type IV pilus assembly protein PilX [Cell motility, Extracellular structures]
MKRRRLRPLPRRQRGAALIVALILLLVLTLLGVAAMRSSLLEERMAGNLRDRQLAFQAAEAALRDAEAWL
RNASAASLTGLSDCTAASNGLYTSWSDPVTWTDATATAVGVAYALGTDGVAATPRYIIEYLGDVTPPTSG
GSSSSGSNYYRITARGFGGNANTVVVLQSTYRRPL
>gnl|CDD|443762 COG4727, COG4727, Uncharacterized conserved protein, DUF2145 domain [Function unknown]
MRLRMRRLAAALLALALAAAAAPAHAGQFCERKPPTAAQQARGLRLAARVAQALDASGARVALLARAGQD
LSRYGLRYSHAGIAYRDPDGPWRVRHLLNACGTARSRLYRQGLGEFFLDDLWRYEASIVVPPPALQARLL
AALLDNPRALRLHQPRYSMNAYPFSTRYQNSNQWVLETLAAAWAPQPVDSRARAQAWLRLKGYQPTVLHI
GSLKRLGARLFVANVAFDDHPNEDRFAGRIEVVTVDSVEAFLQRRGPGAARVEVRRGWAPLAA
>gnl|CDD|443763 COG4728, COG4728, Uncharacterized conserved protein, DUF1653 family [Function unknown]
EIKPGIYRHYKGNLYEVLGVARHSETEEPLVVYRALYGDGGLWVRPLAMFLETVEVDGEQVPRFELIG
>gnl|CDD|443764 COG4729, COG4729, Uncharacterized conserved protein, DUF1850 family [Function unknown]
MKRRLGVALLLALLAALALLPPVTVLCVRDAATGEVLAELPVLPGDEFTLSWTHSVEKTPWEEDYRVTDG
GLVLTETRFQSFGAGMPSPPGELARLEDGWWVIRPIDRPFPELRLRVSTIADHTLCVDGRCYPLSDLLPP
GTPVTISVCRRS
>gnl|CDD|443765 COG4731, COG4731, Uncharacterized conserved protein, DUF2147 family [Function unknown]
MKRLLALLALALLLALAAAAAAADDIVGTWKTIDDDAVVEIYKCGGKLCGKIVWLLEPGKPKKDAKNPDG
ALRNRPLLGLQILWGLKPDGDGEWEGGKIYDPENGKTYSCKITLDSGNKLKVRGYVGIGLLGRTQTWTRV
K
>gnl|CDD|443766 COG4732, ThiW, ECF-type thiazole transporter, membrane (S) component ThiW [Coenzyme transport and metabolism]
MMKTRKLTLAALLVALGVVLSPLISIPVGPAKAFPVQHAINVLAAVLLGPWYAVGVAFIISLLRNLLGTG
SLLAFPGSMIGALLAGLLYRKTKKIWLAALGEVIGTGIIGGLLAYPIAAPLMGKEVALFFFVPPFLISSI
GGAIIGYLLLKALRRTGLLKRLKKD
>gnl|CDD|443767 COG4733, COG4733, Phage-related protein, tail protein J [Mobilome: prophages, transposons]
TNGYGIGGATAAAADRGAAVLVGGVVAGAVVAGALASIRPTNATELVVGVAASGVPATGGAAAIVGAVKV
SGGAAVAAGAIGAAEVAVAVGGIAASISAGYNRSTTAYVVPLGLGQPSAAAALAALVGEYATGDAQLSGV
LAAYGYALVGLRFDAEQFNGSIPNVNALVRGRKIRVPSNYDPSGVWDGTFKWAWTNNPAWVFYDLLTGDR
YGLGRRLTAADIDKWSLYAIAQYCDQKVPDGGGGTEPRFTCNVYIQSQASAWDVLRDIAAAFRGMPYWDG
GKLGVVADRPRDPPVATFTPANVVDGSFTYSYSSRKERPNAALVSFSDPDNGYQQAEEPVEDPDLIARYG
VNQTELTAPGCTSRGQAQREGRWALLTNRYRTRTVTFSVGLDGLVATPGDVIAVADDVLAGRRIGGRVSS
VDGRVVTLDRPVTMEAGDRYLRVRLPDGTSVARTVQSVAGRTLTVSTAYSETPEAGAVWAFGPDELETQL
FRVVSIEENEDGTYTITAVQHAPEKYAAIDAGAFDDVPPQWPPVNVTTSESLSVVAQGTAVTTLTVSWDA
PAGAVAYEVEWRRDDGNWVSVPRTSGTSFEVPGIYAGDYEVRVRAINALGVSSAWAASSETTVTGKTAPP
PAPTGLTATGGLGGITLSWSFPVDADTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRA
RAVDRSGNVSAWWVSGQASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAV
LFAGVATAAAIGAEARVAATVAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVV
LAGVVVYGDAIIESGNTGDIVATGDIASAAAGAVATTVSGTTAADVSAVADSTAASLTAIVIAATTIIDA
IGDGTTREPAGDIGASGGAQGFAVTIVGSFDGAGAVATVDAGQSVVDGVGTAVEAANGTETAAGGGSQ
>gnl|CDD|443768 COG4734, ArdA, Antirestriction protein ArdA [Defense mechanisms]
MTTTETTPRIYVACLAAYNNGSLHGKWIDATQDVEEIQEAIREMLADSPVEDAEEWAIHDYEGFPGATIS
EYESLEKVFELAEFIEEHGEAFAAWLDHFGGLEDAEEAFEDAYQGEYDSEADFAEELIEETGLLLEIPES
LARYIDYEAYARDLFLSDYVTVEGGFEVHVFWN
>gnl|CDD|443769 COG4735, YaaW, Uncharacterized conserved protein YaaW, UPF0174 family [Function unknown]
ATVLRGGEGVSYREVLIDVCDKLKVPYSKNLSTTDLEAEIFLKLLEKAWEKLPEEEKKELTDKVGLSLAI
AVSSVLKPALLAQLARQFALHFASYQLAAQIANYVALQLAGRGMAVSAARYGATRGVFALLGPVGWGITG
LWTAADLGAPAYRRTIPAVFQLAQIRLTRAEC
>gnl|CDD|443770 COG4736, CcoQ, Cbb3-type cytochrome oxidase, subunit 3 [Energy production and conversion]
MDINTLRHFADSWGTVFLFVFFIGIVLWAYSPGNKKRFDEAANLPFDDDD
>gnl|CDD|443771 COG4737, COG4737, Uncharacterized conserved protein [Function unknown]
MRIFKTKWFARWAKKEGLTDEDLCEAVEEMERGLIDADLGGGVIKKRIARPGRGKSGGYRTIIAYRKGDR
AFFLYGFAKNDRANISDDELEALKELAKELLALSEEQLEALIEEGELIEVECD
>gnl|CDD|443772 COG4738, COG4738, Predicted transcriptional regulator [Transcription]
MREETVRKLDEKDEEFVELLQNLGLKRNVAKVLVYLANGDEATSREIERGTGLRQPEVSIAMRYLRERGW
VEEREEKTEGKGRPVKIYRLKVPLDEIIDSIEEEIRKEIEAVLELIEKLKELS
>gnl|CDD|443773 COG4739, COG4739, Uncharacterized conserved protein, contains ferredoxin domain [Function unknown]
MDEENPEKEAVETVAKLMAVAARTAPKGKGVDDIVTAIVTGEDKEKLADEMEEIAEEKGFKFFKRDAENV
RDSDAVVLIGTKESKPGGLNCGACGFETCAEMLEAKVEVDFAGPNCAFRAIDLGIAIGSAVKVAADLGVD
NRIMYSAGVAALSLGLLEDVDVAYGIPLSVSGKNIFFDRKPK
>gnl|CDD|443774 COG4740, COG4740, Predicted metalloprotease [General function prediction only]
MDVSDIRKIFRFSAREKRVIESFGIPGDAFLPLLFSLKFGGSWSYSTESLSSISVKKVTTVYDEEEKTGY
TLEKIYLFLNPEIISKEGTVYRLEKCGNKEERVLVERPYRITVRAKRIILAEVNPLKRKIRIRELEKKPI
TFTGSPAYGAAHEMEHLEGGEIKGEPLWEFEYEKEQ
>gnl|CDD|443775 COG4741, COG4741, Predicted secreted endonuclease distantly related to archaeal Holliday junction resolvase [Nucleotide transport and metabolism]
MSLLLLLIIALAIVIVLLLLLYLLKREIERRARELFEEWRLKELEAEAKREAEAKLREWKQEKEERIRKD
AVKRSRAVLLGKVTEQLAPFLPGFPYNPKDARFIGSPVDLIVFDGLSDGNLEEIVFVEVKTGSSKLTERE
KAIRDAIEDGRVRWEIIRI
>gnl|CDD|443776 COG4742, COG4742, Predicted transcriptional regulator, contains HTH domain [Transcription]
MGSMKLDLLDFLFLSEKRKNILLLLAEGPKTRSELAESLDVSRSTILRQLKELEERGLIERDDGEYELTT
LGRLVVEEMEPLLDTLEVLEENRDYWETHDLSAIPPELLLRIGELGDATVIEPDLTDPFEPVERFLELLR
ESKRVRGVSPVFHPDYPELFSELVEKGVEVELILTEDVFERLKSDYPEELEELLESGNVELYVYDDDIPF
LGLVVTDDFVGLSLYDKDGTYDRALLISDDPSALEWGEDLFEYYREDAEPLTEEILS
>gnl|CDD|443777 COG4743, COG4743, Uncharacterized membrane protein, DUF1616 domain [Function unknown]
MSDSTSRRTPRPVRRLPADLAAVIALAVLALLAVLVPVLNETPLRILLGLPLVLFLPGYALVAALFPARS
RAAAETAGLGQPRGLDGIERLALSFGLSIAVVPLIGLALNYTPWGIRLVPILVSLSGFTLVLAALAAVRR
LRLPPEERFTVPLRRWLAALRAELFSPDSRTDRALNVLLVVSIVLAVGSLGYAVATPKQGEGFTEFYLLG
EDGDGELVAGDYPTELTPGESVPVIVGIENHEGETVNYTVVVQLQRVEDDGNDGTVTERTELDRFSVTLA
DGETWEQPHEVTPTATGERLRLEFLLYKGDVPAEPTIENAYRSLHLWVNVTEE
>gnl|CDD|443778 COG4744, COG4744, Uncharacterized conserved protein, DUF2149 domain [Function unknown]
MRRRRRRRLDEEEDDDPMSGVANLFDVALVFIVALLVALVSSPNMLNLLSPEEDVTIVKNPGQPNMEIIV
KEGKEIKRYKVTGEIGGGGGERLGTAYRLKDGRLIYVPENG
>gnl|CDD|443779 COG4745, PMT, Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General function prediction only]
MSSSPLSSRTRRDRTLLAVLAITALALLLRLVGLGARPFHWDEARVAYWSLRLLETGAYEYRPIYHGPFL
YHVTAALFGLFGASDFTARLPVALVGGLLPLLALLLRERLGDAEVLALALLLAFSPVLVYYSRFMRNDVL
LAAFTLLALGAAVRAIDTRRRRYLYLAAVALALAFATKENAVLYLLCWLGALLLLLDHRLFRARRRGTSV
LLVLRRLRRLVRRLRLLLRWWRHLVGALAVFLAVAVFFYAPRGGPGLWHPGGLPAVLEAATVGAVEKALD
YWVAGGTHEHPYLYYLGDLLGTLLLYELPVLVLAVVGFLADRYGGGRPRPLVAFAAYWGLASLLGYPLIT
EIKAPWLVVHVVVPLAIPAAVGLAALVRRGRRALAAGDAVRAALAALLLLAVVGQVGVQAASASYVNPSD
DNELVQYAQPSDDLRPTLDDIEAAAAANDGTDVLFYGDRFYVADESADRPPAGEYWHNRLPLPWYLERAD
AEVWSTPDPAALTEDPPPVVIAHASDRDELAAQLDGYEARTYGLRLWGREVVVFVDEDAL
>gnl|CDD|443780 COG4746, COG4746, Uncharacterized conserved protein [Function unknown]
VREELREQIVEAFEGADFPVESPMELLPALPDGPDTTCEAGDVSMTAGELAGKLLKDSDFPYKSAEDLAD
DIVERAGL
>gnl|CDD|443781 COG4747, ACTx2, ACT domain-containing protein [General function prediction only]
KQISVFLENKPGRLAEVTRLLGDAGINIRALSIADTSDFGILRLIVDDPEKAREVLKEAGFTVSETDVLA
VELPDRPGGLAEILKALAEAGINIEYMYAFVGRPGGKAVLILRVDDLEKAIEVLKENGI
>gnl|CDD|443782 COG4748, COG4748, Uncharacterized conserved protein, contains restriction enzyme R protein N terminal (HSDR_N) domain [Function unknown]
MDFKEQLKALAERVQKLKESIQTEEATKNALIMPFIQILGYDVFNPTEVVPEYTADVGTKKGEKVDYAIL
KDGQPVILIECKGVGEDLDINHASQLFRYFHVTEARFGILTNGIEYRFYTDLDEPNKMDEKPFFEFDLLD
LKESDIPELKKFTKSAFDLESILSTAEELKYTKAIKKVLAEQLEEPSDEFVRFLASRVYEGRLTAKVIEQ
FTPLVKKAIKQFINDIVNDRLKSALAGSEAPAPEEEPVEEPPESEEPKIVTTEEELEGFYIVKAILREVI
DPDRIVYRDTKSYFGILLDDNNRKPICRLHFNSKKKYIGLFDEAKKETRIPIESLDDIYNLAELLLATVE
RYLKE
>gnl|CDD|443783 COG4749, COG4749, Uncharacterized conserved protein, DUF2150 domain [Function unknown]
MEPSKPFYEFYTQERWQNWLDRLKEEDFDPDESSDEMEDSARLLLNLQDDVAIAVLKIIAAYENGRISKE
EALDELEEVREIVLEEVDFDDEDLDMLIDSVQTSLVVVFAAAEEYIAGGYAEEADIKELVKAAADAEAEE
DLDAALGYAAQIGARVIDGASLDGKVVEDLEYGLVAEWLNGIDSLQAAMSDPEVVEEDDGEDD
>gnl|CDD|443784 COG4750, LicC, CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism]
MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFEYLEDKYGVK
LIYNPDYAEYNNISSLYLVRDKLGNTYICSSDNYLTENPFEKYEYKSYYSAVYKEGETDEWCVKTNRDGR
ITKIEIGGKDGWIMLGHSYWDKEDSKKFKEILEEEYEDPETRDLYWEDIYMDHIDELDMYARKYPAGDIY
EFDSLDELREFDPSYLEN
>gnl|CDD|443785 COG4752, COG4752, Uncharacterized conserved protein [Function unknown]
MGANLYLALVHYPVYNKNGEIITTSVTNLDLHDIARSARTYGVKKYYIVTPLEAQQELAERILGHWQEGY
GAEYNPDRKEALSLVKLVSSLEDVIEDIEEEEGKKPLLVATSARKYPNTISYEELRELLEEEDRPVLLLF
GTGWGLTEEVMESCDYILEPIRGAGDYNHLSVRSAAAIILDRLLG
>gnl|CDD|443786 COG4753, YesN, Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription]
KVLIVDDEPLIREGLKRILEWEAGFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIREL
DPDTKIIILSGYSDFEYAQEAIKLGADDYLLKP
>gnl|CDD|443787 COG4754, COG4754, Extracellular substrate-binding protein [General function prediction only]
TMTTLLLLVLLLVVKSKKGSTGGSLLLLLDVNLLLLEEEEGGLLGGGGSGSSSLLLLIIGLLGPSSGGGG
VLGGPGPPGGPPAVVVFFFFFLLLLLLVVLVVEELLLLAAARAEEARRRRAAAAIIIGLGGGEEAYPPEL
SGGGGRRRRVAAAAAVLPLLLLLLEPDSALALLLLTELLLLLLLLLLGEGRPIIIIIIVVVNIEEEEVVV
DRIIRVGSSSGRRIAVEIVLPPPPRRRRDRAFFARVDIVYYILATTTPPEAAAAGAAPPASGIGYRLPDV
SVGRLAGLLELLADAPGGRADLPDLADELQLEIDDLLPIVEALELLGFAEVEEGDIRLTPLGRRFAEADI
DERKKIFAEQLLRHVPLAAHIRRVLDERPNHRLPAERFLDELEDHLSEEEAERTLKTAIDWGRYAELFAY
DEETGRLSLEEEEEE
>gnl|CDD|443788 COG4755, COG4755, Uncharacterized conserved protein, DUF2153 domain [Function unknown]
MSSRADIESFLRNLDEWVKMQKRLLETFKKAEKKVEEADRLDLILSARAAFQHMMRTLKAFDQWLQDPMI
TSHMPREMLVEVWSTLREILEQLIELDIEHTSEFRDLLKKLAKEGKLNPLLALYKEERGQQEGGRRRGTE
TIR
>gnl|CDD|443789 COG4756, COG4756, Predicted cation transporter [General function prediction only]
MDMTVDAGLSIILLLVLILPFFVKKVEHNLEAFLFVMGIAAVTVSGIWSIELVEEAFKNPILYGITQAVL
IAGLLFYLFHKKIKKAIRKLLDKIPLKVFVFLVIVVLGLVSSIITAIIAALILVEIVNALPLDRKTKVKL
VVIACFSIGLGAALTPIGEPLSTIAISKLNADFFYLFRLLGIYIIPGVLALGLLGAFFVGKASSKKEEEE
EIEDTESLKDVFIRAGKVYLFVAALELLGAGFKPLIDKYIIKLPSYLLYWVNMISAVLDNATLAAAEISP
AMSTEQIKAILMGLLISGGMLIPGNIPNIISAGKLGITSKEWARIGVPLGLVLMVIYFIILFVVGI
>gnl|CDD|443790 COG4757, COG4757, Predicted alpha/beta hydrolase [General function prediction only]
MSTAASPESVTITAADGYPLAARLFPPAGPPRAVVLINPATGVPQRFYRPFARYLAERGFAVLTYDYRGI
GLSRPGSLRGFDAGYRDWGELDLPAVLDALRARFPGLPLLLVGHSLGGQLLGLAPNAERVDRLVTVASGS
GYWRDYPPRRRLKVLLFWHLLGPLLTRLLGYFPGRRLGFGEDLPAGVARQWRRWCRRPRYFFDDDGEDLE
AALAAVTAPVLAISFTDDELAPPAAVDRLLAYYPNAPVTRRRLAPADLGLKRIGHFGFFRRRFAAALWPR
VLDWLRAGA
>gnl|CDD|443791 COG4758, LiaF, Membrane protein LiaF, inhibitor of the LiaRS two-component envelope stress sensory system [Signal transduction mechanisms]
TDLLAFFLIIFGLLLLLENLFFTGGPLFLLLLGILLIYLGLRKRRRLSGLFLFWIGLLLLVLALLSMWAF
RLLLPALLIYFGLSLIQGKKKPEYIEPQFEEADVKKEEITKEPLSKNKLFGDQRTPSEPYEWEDINIQGG
IGDTTIDLTKAILPKGETVIVIRGLIGDVRILVPYDVEVSVHHSVIIGDVKIFDQEEDGGINESLHYETE
GYEEAERKVKIIVSVLIGDVEVRRV
>gnl|CDD|443792 COG4759, COG4759, Uncharacterized conserved protein, contains thioredoxin-like domain [General function prediction only]
MSTPLANCFFCSDVSRQAGEDPIGTAANADTWLLIEQPGPWGRDALESSPLDPALGALLEELAKRAGVRP
LLIRRPGRHSDPGPRRVLLYRRPRGWKQEFLVPDPEELADLDEALLAGPGALGLPYRQETVHTRDILVCT
HGKRDKCCARFGRPVYAALAAAYPEENVRVWECSHFGGHRFAPTLVDLPDGRYYGRLDPESADAILTAAG
DGQVLLPHYRGWSGLPPPAQAAEREVRQRLGWDWLDYLKAGRILEQDLDEDWAEVEVTFESPDGRYYAVR
VEDEGSVPTLPGSCKGKAPKPVRQYAVSSLVKVA
>gnl|CDD|443793 COG4760, COG4760, Uncharacterized membrane protein, YccA/Bax inhibitor family [Function unknown]
SSNPVFSRSPAFSRQLQQMYGAPAAAPADTGRMTVDDVVNKTGLLLGILVVTAAVTWFLLPSPALAMPLM
IGGAIGGLVLALVISFKKEPSPALALLYAALEGLFLGAISAFFEAMYPGIVLQAVLGTFGVFGVMLALYK
TGIIRVTPKFRKIVIAATIGIALFYLVNLVLSLFGVGLGLRSGGPLGIGFSLVVVGLAAFSLVLDFDFIE
QGVRNGAPKKMEWYAAFGLMVTLVWLYLEILRLLSKLRSR
>gnl|CDD|443794 COG4762, COG4762, Uncharacterized conserved protein, UPF0548 family [Function unknown]
MRRSTQRDQPLTYPEVGATRAGYPPAGYRHLERRVRLGSGEERFERAAAALLTWGMQRGAGLRVRADAPP
AAPGATVVLRLGVGPLRLLAPCRVVYVVDEPDRFGFAYGTLPGHPESGEERFLVERDDDGSVWFTVRAFS
RPASWLYRLGGPVLRRVQRRFARRYLRALRRAAGS
>gnl|CDD|443795 COG4763, YcfT, Uncharacterized membrane protein YcfT [Function unknown]
MTKPEKQRVDWIDTAKGICIILVVMMHSVLGVYAAGGLAGFWHYVNAFLKPFRMPLFFLISGLFASRVID
RPWREYLDRRVVHFLYFYVLWGVIQWLFKAPINAAANAAYAGSLSEFLMGLILPFGTLWYLYALAVYFVV
TKLLRRVPPPLVLAAAAALEIAPVLPTGWWGVDSFARYFVYFYLGYFFAPQIFALADWARARRALALAGL
ALWAVANALLVFGLALLPGVSLLLGLLGAVAIVALASLLARRRLMAPLRYIGRNTLVIYLAHFIPMAALR
LALLKAWTGLLTLADLGLYPLLVTLIAVLGSLLVWKLLRRTPGDFLFERPAWARLAAPRRAA
>gnl|CDD|443796 COG4764, SLT, Predicted transglycosylase, contains SLT domain [General function prediction only]
MMRLLLLLLLLLLLLAGCATAPPRNPDNACAIFREKPDWYRAAKAAERKWGVPVHVQMAIIYQESSFRHD
ARPPRTYLLGFIPWGRPSSAYGYAQALDGTWDDYQRETGNRGASRDDFADAIDFIGWYMNKSQRRNGISK
WDAYNQYLAYHEGHGGYRRGTYRSKPWLLRVARKVAARAKRYAAQLRQCRRRLDSGWWW
>gnl|CDD|443797 COG4765, COG4765, Uncharacterized conserved protein, DUF2155 domain [Function unknown]
MRRAALALALLAALLAAPAPAQAEAIENPVAVLRGLDKITGRITDLEVPVGETVQFGALQITVRACRYRP
PTEAPDAAAFLEVDEITLDGEGRRIFSGWMFASSPALNALEHPVYDVWVLRCKGS
>gnl|CDD|443798 COG4766, EutQ, Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid transport and metabolism]
KKLDAPPFEKEVDPSGIKVSVKDERFDTGGPGDKVYLKDVVTLEESSRMGAGFMRLEKTTFPWTLTYDEV
DYVLEGTLTIEIDGETVTAGPGDVIYIPKGSSITFSTPEKARFFYVTYPANWA
>gnl|CDD|443799 COG4767, VanZ, Glycopeptide antibiotics resistance protein [Defense mechanisms]
NLVPFKSILEDLALGGSIAVIQILGNILLFVPLGFLLPLLFKRLRSFKRVLLLGFLLSLLIEVLQLILPG
RVFDIDDLILNTLGALLGYLL
>gnl|CDD|443800 COG4768, COG4768, Uncharacterized conserved protein YoxC, contains an MCP-like domain [Function unknown]
IILYIAALIIAIAFLVLVIYLVKTLKKVKKTLNEVNKTLEGLEKQLDGITTETTDLLHKTNRLAEDVNGK
VEKLDPLFDAVKDVGESVSDLNSSLRDVTSSVSSKVEKNSEKVAQVVKWGKVALGLFKKKKK
>gnl|CDD|443801 COG4769, COG4769, Uncharacterized membrane protein [Function unknown]
MMKTRKLVLIALLAALALVLSLVESLIPLPLPIPGAKLGLANIVTLIALYLLGFKDALLVALLRVLLGSL
LSGTLPGFLLSLAGGLLSLLVMALLKKLPRRKFSLVGISVAGAFAHNIGQLLVASLLIKNPGIFYYLPVL
LLAGLITGIFTGLIANYLLRR
>gnl|CDD|443802 COG4770, PccA, Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]
MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA
KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQD
AEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIE
VQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDA
DGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPFTQEDIKLRGHAIECRINAEDPARGFLP
SPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEGVKTNIP
FLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEELALAAAMKME
>gnl|CDD|443803 COG4771, FepA, Outer membrane receptor for ferrienterochelin and colicins [Inorganic ion transport and metabolism]
LLLASLLLLLALAAQAADALAEDATELEEVVVTATRTEQSLSDAPASVSVITAEEIEKLGATDLADALRL
LPGVSVTRSGGRGGSSGISIRGLGGDRVLVLIDGVPVNNPALGGGGDLSYIPPDDIERIEVIRGPASALY
GSDAIGGVINIITKKPTDELEGSVSLGYGSNGNGTYSGSLSLGGPGDKLSFLLSGSYRDRDGYLDYRNGG
FVGNSGYERYNLNAKLGYRLSDNHRLSLSGGYSRQDRDGGPPTLGDTEISSDNAGDRDTTTDRGNYSLRY
NGDLGDNLDLSLYYSRTDRDSTNGSLGGSTGSFSDSDDTTYGLELDLTYPLGGNHTLTLGAEYRYDDLDS
SSFLGGADASRDTYGLFAQDEWKLTDKLTLTAGLRYDYYSTFGASNYTAFSPRLGLRYDLSDNLTLRASY
GRGFRAPSLAELYGSGTGTPGRYVLGNPDLKPETSDNYELGLEYRLGNGGLSLSLTGFYTDIKDLIVLVP
VGPGPGDVLQYENVGKARTYGLELELKYRLGKGLTLTASYTYLDSKIDDGDTGEPLPNVPPHKANLGLDY
RLPKWWLLLLLTRYYGGRYVTPPSGRLEGYTPGYTLLDLRASYKLTKNLTLS
>gnl|CDD|443804 COG4772, FecA, Outer membrane receptor for Fe3+-dicitrate [Inorganic ion transport and metabolism]
MRRALAAALLLAAAAAAEAATTLETVVVTGSRAAEARLKDVPGSVSVVDREELENQAATSLREVLRRVPG
VNVQEEDGFGLRPNIGIRGLGPRRSRGITLLEDGIPIAPAPYGDPAAYYFPDLERMERIEVLRGAAALRY
GPQTVGGAINFVTRTIPTAFGGELRVTGGSFGYRRTHASVGGTVGNFGYLVEYSRKRGDGFRDNSGFDIN
DFNAKLGYRLSDRQELTLKFQYYDEDANTPGGLTDAQFDADPRQSYRPADQFDTRRTQLSLRYEHQLSDN
TTLTTTAYYNDFSRNWYIRQNTADPNTPGLGLRGNPRGYRSYGIEPRLTHRFELGGVPHTLEVGLRYHRE
EEDRKQYVNTYGQGRSGAGLRRDRRFSADALAAYAQNRFELTGRLTLTPGLRYEHIRRDRTDRYSTRTGG
DDSGSNSYSEFLPGLGLLYQLTDNLQLYANVSRGFEPPTFGDLAYGNGGNPDLKPEKSWNYELGTRGRIG
NGLSAEVALFYIDYDNELGSCSAAGGDRSTFTNAGETRHQGLELALDYDLLKGGGLGLPLFAAYTYTDAE
FTSDFGPVFAGNRLPYVPRHQLTAGLGYEHGGWTANLNGRYVSEQFTDAANTVADGSFGKIPSYTVLDLS
ASYDFGKNLSLFAGVNNLFDKRYIASRAPNYAAGIRPGPPRTVYAGLRLKF
>gnl|CDD|443805 COG4773, FhuE, Outer membrane receptor for ferric coprogen and ferric-rhodotorulic acid [Inorganic ion transport and metabolism]
AAALLAGSGLAAAAAGALAQAAAAAAAEATTLPEVTVTGTAEGTGGYTAKSSSTATKLDTPLRETPQSVS
VVTRQLIEDQGATTLDDALRNVPGVTVSSYDGGGRDSFSIRGFSIDNYLRDGLPLGGFGGGQPDTANLER
VEVLKGPAGLLYGAGSPGGLVNLVTKRPTAEPQGEVSLSAGSWDTYRATADVGGPLNEDGTLRYRLNAAY
EDGDSFRDGVDNRRTLIAPSLDWDLTDDTTLTLGAEYQDDDSTGDRGFLPLDGTLLDLPRSTNLGEPWDY
YDTETTTLFAELEHRFNDDWSLRANARYSDSDRDGRSAYAYGAPDAATGTLTRYASARDGDSRSDSLDAN
LNGKFETGGLEHTLLVGADYSRYDSDSDSATAGTINIYNPVYGNLPEPDFDASDTDTTTRQTGLYAQDQI
SLTDRLSLLLGGRYDWYETDSTNRLGGSTTSYDDSAFTPRAGLVYDLTPGLSLYASYSESFEPQSGADNN
GNPLDPETGKQYEAGVKGELFDGRLNATLAVFDITQKNVATTDPDNPNFYVQVGEVRSRGVELELSGELT
PGLNLIAGYTYTDAKITKDADALEGKRLTNVPRHTASLWTTYRFPSGALKGLGLGGGVRYVGERYGDAAN
TFTLPSYTLVDAGARYDLGKNWTLQLNVNNLFDKKYYASSGSRGYVYYGAPRNVRLSLSYKF
>gnl|CDD|443806 COG4774, Fiu, Outer membrane receptor for monomeric catechols [Inorganic ion transport and metabolism]
KTDTPLLDTPQSVTVVTRELIEDQGATSLADALRNVPGVTFGAGEGGNGDSFSIRGFSASGDIYVDGLRD
PGQYRRDTFNLERVEVLKGPASVLYGRGSPGGVINLVTKRPTDEPFTEVTLTYGSDGQRRATLDVNGPLG
DDLAYRLNGMYRDSDSYRDGVDNDRWGIAPSLTWRLGDRTRLTLDYEYQDDDRTPDYGVPAVANGRPVDV
DRSTFYGQPDDYSDSETDSATLRLEHDFNDNWTLRNALRYSDYDRDYRNTYPTGGNATGTVTRSAYRRDQ
DNDTLSNQTDLTGKFDTGGVKHTLLAGVEYSREDSDNARYSGGGTAPTVNLYNPVYGAPVTGPTLGGADN
DSRTDTTGLYLQDTISLTDRWSLLAGLRYDRFDTDYTDRTTGATTSSYDDSAFSPRAGLVYKPTPNLSLY
ASYSTSFNPGGGAPSLSNAGQALDPEKSRQYEVGVKWDLLDGRLSLTAALFRIEKTNVRTTDPANPGVYV
QTGEQRSRGVELEATGELTPGWSVLAGYTYLDAEITKSANAANVGNRLPNVPRHSASLWTTYDLPLPGLT
LGGGVRYVGSRYADAANTVKLPSYTRFDAGASYRLNKNLTLRLNVNNLTDKRYYASAYGSGYVTPGAPRT
VLLSASYRF
>gnl|CDD|443807 COG4775, BamA, Outer membrane protein assembly factor BamA [Cell wall/membrane/envelope biogenesis]
IKDIRVEGLQRVEAGTVLSYLPLRVGDTFDDEKLDEAIKALYATGLFSDVRIEREGVVLVVKVKERPTIN
SIEFEGNKKIKDEDLKKELGLKEGRVFDRALLERAEQELKEQYRSKGYYNAKVTITPERNRVDLTFEIDE
GEKAKIKKINFVGNKAFSDKELRKVLKTKESGWLTKSDKYSKEKLEADLERLRSFYLNRGYLDARVDSTQ
VELSPDKKDIYITINIEEGEQYKVGDIKFEGNLVDEEELRKLLKIKPGDVYNREKLEKDIEAITDLYGDN
GYAFARVEPVPEIDPENDTVDLTFRIDEGPRVYVDRIEIEGNTRTRDEVIRRELRLKEGDPFSREKLERS
RRRLYRLGYFESVDVETEPGPSTPDQVDLVVDVKEKPTGSLSLGAGYSSDDGFIGGASLSQRNLLGTGQE
LSLSLQLGSYSQSYSLSFTEPYFFGSPLSLGVSLFYRRRDASDYSSYDLKRTGGGLGLGYPLSEDLRLSL
GYGYERTDISDVDSSPDYLPDQNGSSNTSSLGLGLTYDTRDNPLFPTRGSYLSLSLEFAGPYLGGDLEYY
KLSADARYYFPLGKKLVLALRAEAGYLGGYGKDLPFFERFYLGGFGSLRGYEENSLGPRLGGNAYLLGSA
ELRFPLPLPPSAGLRGALFVDAGNVWDSGDDFDLSDLRYSAGVGLRWDTPLGPLRLDYAYPLDKEPGDSG
QRFHFSIGTRF
>gnl|CDD|443808 COG4776, Rnb, Exoribonuclease II [Transcription]
MFQNNPLLAQLKQQLHEQTPRVEGVVKATDKGFGFLEVDDQKSYFIPPPQMKKVMHGDRIKAVIRTEKDK
ESAEPETLIEPFLTRFVGRVQKKDGRLFVVPDHPLIKDAIKARPKKGLEEGLKEGDWVVAELKRHPLKGD
RGFFAEITEFIADADDPFAPWWVTLARHNLEREAPEGDDEWELLDEGLEREDLTALPFVTIDSESTEDMD
DALYIEKLENGGWKLTVAIADPTAYIPEGSELDKEARQRAFTNYLPGFNIPMLPRELSDDLCSLKENEKR
PALVCRVTIDADGSIGDDIEFFAAWIRSKAKLAYDNVSDWLEGKGEWQPENEEIAEQIRLLHQFALARSQ
WRQQHALVFKDRPDYRFELDEKGNVLDIHAEPRRIANRIVEEAMIAANICAARVLREHLGFGIFNVHSGF
DPEKLEQAVELLAEHGIEFDPEQLLTLEGFCALRRELDAQPTSYLDSRLRRFQTFAEISTEPGPHFGLGL
DAYATWTSPIRKYGDMVNHRLIKAVILGQPAEKPDEELTERLAERRRLNRMAERDVADWLYARYLKPKVG
SGQVFTAEIIDINRGGLRVRLLENGAVAFIPASFIHSVRDELVCSQEEGTVYIKGEVRYKLGDTIQVTLA
EVREETRSIIAKPA
>gnl|CDD|443809 COG4778, PhnL, Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism]
MTTLLEVENLSKTFTLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV
RHDGGWVDLAQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLN
LPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFH
DEEVREAVADRVVDVTPFS
>gnl|CDD|443810 COG4779, FepG, ABC-type enterobactin transport system, permease component [Inorganic ion transport and metabolism]
MSATSTRVLRVGRVSLRLRRRALLVTLVLLLLLLALAVLALTLGDYPLSPGDVLRALLGEGDPGASFVVL
ELRLPRALAALLVGAALGLSGAIFQSLTRNPLASPDIIGITAGASAGAVAAIVVLGGSGLAVALGALAGG
LATALLVYLLAWRGGVSGYRLILVGIGVSAMLTAVNSYLLTRADLEDAQSAAVWLTGSLNGRTWEDVLPL
AVALAVLLPLALALARRLRLLELGDDTAAALGVRVERTRLLLLLVAVALAAVATAAAGPIAFVALAAPQI
ARRLTRSPGPPLLPSALVGALLLLAADLVAQHLLAPVQLPVGVVTGALGGPYLLWLLIRENRRG
>gnl|CDD|443811 COG4781, UgpQ1, Membrane-anchored glycerophosphoryl diester phosphodiesterase (GDPDase), membrane domain [Lipid transport and metabolism]
MMKIKKLLKNTLKLFKKNWFRYLLFELIYKLLIAFVFIPLLSFIFNFLLKASGIPYLTNDNLLEILTSPL
GLIFLLLLLLLLLLFIFFEFTFLIIGAYFILRGQPISLKELFKRTFKKLKKLFGPQLLLFLFYFLLIIPF
ANIGLSSSLLSKIKIPEFITDEIFKTPLGIILYILFYLILFYLAIRLIFTLPLFILERKSFKEAIKESWQ
LTKKNFFRLLLLLILINLLIILIVVLIIFLIYLLQLLVDSFPPGNALITASINLTLLQLLTFLFTVIFSV
LIIQVLVALYYQQSKRKKKALVIVLLVIFLIFSGINNSPSTIILIILGRAVGGGNNTASLALAAALTIAL
LADAIILDADQTVVVVVVVLDLLLLLAKDKNIKRLTLLELLELILVSGGSKKISSLFEDLIAAKKLKILL
LLEVIKKTGKTDEDADLVTVAKKKKKLEARLAVEVSDDSAEDIKVEKSLPKEGVIIILLINNFTKTEADV
FVSEYESTSLLDVLLVTEEAKAVYVAIVNIEKTDEREKMKNKNVIIIIDIKDVLAEIEILKDDKEYIPSL
IDLDLVFLTFDIIID
>gnl|CDD|443812 COG4782, COG4782, Esterase/lipase superfamily enzyme [General function prediction only]
MRRRLLLLLLLLLLAGCAGRPAVLVPVAEAAPGATVVTVFVATTRAPSDDPGGLFGGERSDELSFGRADV
SIPPDHKIGEIEWPKSLPPDPAKDFVVLSVEPLDDEAAFLAALAAALAASGKREVLVFVHGFNTSFEDAV
YRAAQIVHDLGFPGVPVLFSWPSRGSLLGYVYDRESATYSRDALEELLRDLARDPGAERIHIVAHSMGNW
LTMEALRQLAIRGRGRVLRKIGQVVLAAPDIDVDVFRSQAARIGKLPRPFTLYVSSDDRALALSRRLAGG
RPRLGAIDPRAELAALGVDVIDVSAVDTGGLGHSYFADSPEVLSDLGALLRGGQAPTDRRVLRTVGNAAG
AVVTAPV
>gnl|CDD|443813 COG4783, BepA, Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones]
AACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPD
EPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD
>gnl|CDD|443814 COG4784, COG4784, Putative Zn-dependent protease [General function prediction only]
MRRRRRRALRLLLALALALLLAGCATNPVTGKRDLVLMSEEQEIAIGAEEHPRILAQYGGAYDDPKLQAY
VARVGQRLAAASHRPDLPYTFTVLDSPVVNAFALPGGYVYVTRGLLALANDEAELAAVLGHEIGHVTARH
AVQRQSRATAAQIGLGRVLSPVLGSAQAGQLAGAGAQLLLASFSRDQELEADRLGVRYLARAGYDPYAMA
RFLGSLKRQSAFRARLAGREGRRSYPDFLSTHPDTPDRVQRAVAAARQLGAPGQGERDRDAYLAAIDGLV
YGDDPEQGFVRGRRFYHPELGFAFTVPEGWQLENSPQAVLAVGPDGDAALRFDGARLPSGQSLADYLRSG
WIQGLQLGSVESLTVNGLPAATAVARAETQGEWDFRVAVIRFGGQVYRFIGAAPAGALAAYDPAFRATAE
SFRRLTDAEAAALKPLRIRVVTVKPGDTVASLAARMPVPDRPEERFRLLNGLYPGGELKPGQLVKIVV
>gnl|CDD|443815 COG4785, NlpI, Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]
LYALALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAERIDRALALP
DLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDY
AYAYLNRGIALYYLGRYELAIADLEKALELDPNDPERALWLYLAERKLDPEKALALLLEDWATAYLLQGD
TEEARELFKLALA
>gnl|CDD|443816 COG4786, FlgG, Flagellar basal body rod protein FlgG [Cell motility]
LYTAASGMLAQQTRLDVISNNLANVNTTGFKRDRAVFEDLLYQLIRRPGAPSSQGTQTPVGLQLGTGVRV
AATQTDFTQGSLQQTGNPLDLAIEGDGFFQVQTPDGETAYTRDGSFQLDADGQLVTSDGYPVLPENGPIT
IPEDATSITISEDGTVSVTLADGDGQQVGQLGLVDFANPAGLEKVGDNLFRETAASGAPIVGTPGEDGLG
TLRQGYLEGSNVDVVEEMVDMIEAQRAYEANSKVIQTADEMLGKANNLRG
>gnl|CDD|443817 COG4787, FlgF, Flagellar basal body rod protein FlgF [Cell motility]
MDRLIYTAMSGAKQTLEAQAVTANNLANASTTGFRADLEAARAVPVQGEGLPTRAFAVTETPGTDFSPGP
LQQTGRPLDVAIQGDGWLAVQAPDGSEAYTRAGDLQVDANGQLVTGNGLPVLGDGGPITIPPGAKVTIGA
DGTISIVPAGGPPNALAEVGRLKLVNPDPAQLVKGDDGLFRLKDGGPLPADPNVRVVSGALEGSNVNAVE
EMVSMISLARQFEMQMKMMKTADENDQAANQLLRLS
>gnl|CDD|443818 COG4789, EscV, Type III secretory pathway, component EscV [Intracellular trafficking, secretion, and vesicular transport]
FLNAASGRSDLVLAALLVAIIFMMILPLPTYLVDILIALNITISVLLLMVAMYIPSPLAFSTFPSVLLIT
TLFRLALSISTTRLILLQADAGHIIETFGNFVVGGNLVVGLVIFLIITVVQFIVITKGSERVAEVAARFS
LDAMPGKQMSIDADLRAGVIDADEARRRRALLEKESQLYGAMDGAMKFVKGDAIAGIIIILVNIIGGIAI
GVLQHGMSASEALHTYSILTIGDGLVAQIPALLISITAGIIVTRVSGDEDSNLGREIVSQLLAQPKALLI
AAVLLLLFALIPGFPTLVFLLLAALLGGLGFKLLRRKRRAAAAAESEPLPALQAAGAKGSEAGLIDGDDF
PPTVPLILRLSPSLAPALEAEALNQEIRRLRNRLFEDLGVPLPGIHIRFNPGLPDDEYSILLNEVPVARG
TLPPGHLLVRDDVDELEALGIPAEEGELPLGEGPSLWVPAEHAELLEKAGIKVRDAEDVLALHLSLVLRR
HAAEFIGIQETRYLLDQMEKKYPELVKEVQRVLPLQRIAEVLQRLVEEGISIRNLRLILEALIEWGPKEK
DVVMLTEYVRIALKRYICHRYSGGQGTLPALLLDPEIEEMIRGAIRQTSAGSFLALDPEQSQAILEQLRQ
ALGPLPPGGQDPVLLTSMDIRRFVRKLIEREFPDLPVLSYQELTPEIRVQPLGRIDLP
>gnl|CDD|443819 COG4790, EscR, Type III secretory pathway, EscR/YscR component [Intracellular trafficking, secretion, and vesicular transport]
MSQLPNPLSLILLLALLSLLPFLVVMGTSFLKISVVLSLLRNALGVQQVPPNMVLNGIALILTLFVMAPV
GQEIYDRLQAAPVDFSSSASVLEAVDAGLEPLRDFLKKNTDPEERAFFLDAAQRLWPEEYAAKLKPDDLL
VLLPAFVLSELTSAFKIGFLLYLPFVVIDLVVSNILLALGMMMVSPMTISLPFKLLLFVLVDGWTLLLHG
LVLSYR
>gnl|CDD|443820 COG4791, EscT, Type III secretory pathway, EscT/YscT component [Intracellular trafficking, secretion, and vesicular transport]
LSLEEYLQDLLLALALAMARLLPVFLLLPFLSGQVLPGLVRNGVALALALPLAPGLPAALLLPPLSPLAL
LGLLLKELLIGLLLGFLAAIPFWAAEAAGELIDNQRGATMASSINPASGSQSSPLGILLSQFLIALFFAG
GGFLLLLGALYDSYRLWPLGSFLPALSAQGAAFFLALLDQLMTLALLLAAPVLLALLLVDLALGLLSRFA
PQLNVFFLSMPIKSLVALLLLLLYLPVLLEQVLAELLSLEDLLPR
>gnl|CDD|443821 COG4792, EscU, Type III secretory pathway, EscU/YscU component [Intracellular trafficking, secretion, and vesicular transport]
MSSEKTEQPTPKKLRDARKKGQVAKSKDIVSAVQLLALLGYLLLEGDALVEHLQALILLPAQLLNLPFDE
ALNQLLGALLELLLRLVLPLLAVLILATILSNVAQVGFLFATEAIKPKLEKINPVENLKRIFSLRSLVEL
LKSLLKVVLLGLIFYYLLRGYLPTLVYLPYCGLACAGPVVGALLKWLWGVLLGAYLVFGLADYLFQRYQF
RKQLRMSKDEVKREYKDMEGDPEIKQKRRRLHREIQSGSLALNVKRSSVVVRNPTHIAVGLRYVPGETPL
PVVLEKGEDARAQQIVKLAEEEGVPVVENIPLARALYADAGLGEYIPEDLFEPVAEVLRLALLL
>gnl|CDD|443822 COG4794, EscS, Type III secretory pathway, EscS/YscS component [Intracellular trafficking, secretion, and vesicular transport]
MNEADIIQLTSQALLLVLLLSLPPVLVAAVVGLLVSLLQAVTQLQDQTLPFGIKLIAVVLTLALTAPWLG
AELLNFAEQIFDMFPAMG
>gnl|CDD|443823 COG4795, PulJ, Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and vesicular transport]
MKRARRRQRGFTLLELLVALAIFALLLLAAYRGLDSVLRSRERLEQQAERLQELQRALALLERDLRQAGP
RPDEGGDPEPALSGGGSCLIDLNRNGWWNPLRSELQRVGYRLRDGALE
>gnl|CDD|443824 COG4796, HofQ, Type II secretory pathway, component HofQ [Intracellular trafficking, secretion, and vesicular transport]
PVPYETRVEGNALLVTLGPAAAAAAAAAAAFAEAAAAAANAIRDIDFRRGEDGEGRVVVDLSDPGVGVDI
RQQGGKLVVDFLNTSLPEELRRRLDVTDFATPVQSIDAFQQGDNVRLVIEPRGDWEYSAYQTDNQFVVEV
KPLTEDENKLAQGGKKGYTGEKLSLNFQDIPVRSVLQLIADFTGLNLVISDSVTGNITLRLKNVPWDQAL
DIILKAKGLDKRKNGNVLLVAPAEELAAREKLELEAKQQIEELEPLRTEYIQLNYAKASDLAKLLKGQRG
SLLSERGSVTVDERTNTLIVRDTPSKLEEIRRLIAKLDIPVRQVLIEARIVEASDSFSRELGVRWGGSGA
NGTGNNRGGIGGSLNGTTAGTPLLPDGLNVNLPAANPAGSLGLTLAKLGGGRLLDLELSALEAEGKGEII
SSPRVITADQQEASIEQGTEIPYQESSSSGATSVEFKEAVLSLEVTPQITPDGRIILDLDVSKDSPGETV
AGGVPAIDTKEIKTQVLVENGETVVLGGIYEQTESNSVDKVPFLGDIPLLGWLFKNTTKTDEKRELLIFI
TPRIVKDALA
>gnl|CDD|443825 COG4797, COG4797, Predicted regulatory domain of a methyltransferase [General function prediction only]
MAAAYPPASFVGGDLSSRQIEAGGDAIIALGLLNNVLLQASILDIDDSFGGFDYIIAHGVVSWVPPAVQE
KILRVCARNLLANGIAYVSYNTLPGWGMRRMIRDMMLYHHRRFRDPLERLAQARALLLFLAEAVASENSA
YAELLKEELELLKQKDDSYLLHEYLEEENEPFYFHEFAARAAAHGLQYLSDAELSTMLPGNLPPEVAEAL
KALGNDLIAQEQYMDFLRNRTFRQTLLCHQEVPLNREIDPERLKSLYFASDLTPASPDILTDDGEQRFRN
ADGGTVSTSDPLLKAALQVLAEAWPNALSFDELVAAAKARLGSAQGAEDRDELAKALLSLYASGLVELHS
EPPRFATEVSEKPKASPLARLQAKRGPGRVTNLRHETVNLDDFDRFLLPLLDGTRDRAALVEFLLEAVEQ
GELTLSDEGQPLTDPEALRAELAELVERLLERLARLALLV
>gnl|CDD|443826 COG4798, COG4798, Predicted methyltransferase [General function prediction only]
MRRKLLAALAAAALLAAAAAPAAEAAAAAAAALQAALAGPHRSAADRARDAYRHPAETLAFFGVKPGMTV
VEIWPGGGWYTEILAPYLGPKGKVYAANFDPDSEPPEYAKRSREAFSAKLAADPALYGNVRVTAFAPPDD
PIAPPGSADLVLTFRNYHNWYRAGDAAAMFAAFFKALKPGGVLGVVDHRAPPGTGLEAVATLGYIDEAYV
IALAEAAGFELVGESEINANPKDTADHPVGVWTLPPTLRLGDEDRAKYLAIGESDRMTLKFRKP
>gnl|CDD|443827 COG4799, MmdA, Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]
AMRALLAELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGSFLELGALAGHRMYDDDDRVPGD
GVVTGIGTVDGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAG
YGRIFYRNARSSGGIPQISVIMGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELG
GADVHARVSGVADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPPARDPEELYGIVPEDPRKPYDM
REVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVANQPMVLAGVLDIDAADKAARFIRLCDAFNI
PLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAYGAGYYAMCGKALGPDFLFAWP
TAEIAVMGGEGAANVLYRRELAAAEDPEALRAELIAEYEEQANPYYAAARGWIDDVIDPRDTRRVLARAL
EAAANKPEERPPKKHGVI
>gnl|CDD|443828 COG4800, COG4800, Predicted transcriptional regulator with an HTH domain [Transcription]
MSTVERLILSALRSDEEFQKALKKVLDEELGLSLKEFSEISGIPQSTLYKILSGRREPNLSTLRQIVKTI
RRIEGSEDEDFIAVIAARPVLDKIPERKIKIGGRLVTIREYPASSMEEAIIAAVRAEREGALAIVCAPIV
SPTVEKIVRIPVATIIPRDSVMEAIEIAARKIE
>gnl|CDD|443829 COG4801, COG4801, Predicted acyltransferase, contains DUF342 domain [General function prediction only]
MSLGSDPLDELVIPDGTTVEEHDLVTDGDVIVGGQSTIEYGVRGRNVIAGERVTFGGDIEAEGDCRLDMW
CEVGGNVLVGEDAYLGERVHIGGKLVVSGDLDIGDDVDIEEGFEANGWIVIRNPMPVIVFLFVYLSELLR
LGEEEEAEELLEELFDDDEEEEDPLVIPRGAKVSDDAWRVSTPATIGDDCRLHGNIRAESITVGEDTTVF
GSLRARGDIVVGSGTTIHGDVTTRNGTVTIEAGAHVLGDVSAEDLVLHEGARVDGTIRARGGMRIERDDE
EDE
>gnl|CDD|443830 COG4802, FtrB, Ferredoxin-thioredoxin reductase, catalytic subunit [Energy production and conversion]
MTSEESEKELEKLREFLEKYAEKKGYYFNPDEEVTEVLIEGLAKNKERYGYPLCPCRLASGKREEDKDII
CPCVYREPDIREYGACHCGLFVTKEVADGGDEQISVPERRPPRKRGGT
>gnl|CDD|443831 COG4803, COG4803, Uncharacterized membrane protein [Function unknown]
MSTLIVIGFDDEDKAEEALEALKELQKEGLIELEDAAVVVKDEDGKVKLKQSVNLTGAGALGGAFWGLLI
GLLFLGPLLGAAVGAAAGALSGALTDVGIDDDFIKEVGETLTPGTSALFVLVRKATPDKVLEALAGFGGK
VLRTSLSDEDEEKLREALAAA
>gnl|CDD|443832 COG4804, YhcG, Predicted nuclease of restriction endonuclease-like (RecB) superfamily, DUF1016 family [General function prediction only]
KGATSSMALLLPEGYELLLDELKLIIRAAQRAAAAAVNEELLLLYWIIGRIISEEQEQGGWGRGVVGLLA
LDLLLAFPTGKGFSGRNLRRMRQFAEAYPDEEIVQALVAQLSWSHNLLLLSKVKDPEEREFYAQEAIEEG
WSVRVLERQIESQLYERLGLSKTNFAATLPEAQSDLAQQILKDPYVFDFLGLPEEYSERDLEQALIDHLQ
KFLLELGKGFAFVGRQYRLEVGGEDFYIDLLFYHRKLKCLVVIELKIGKFKPEDLGQMNFYLNALDDLLK
KPGDNPTIGIILCKSKDDEVVEYALLDSSKPIGVSEYQLYLPLPEELQKELPEIEELEEEL
>gnl|CDD|443833 COG4805, COG4805, Uncharacterized conserved protein, DUF885 family [Function unknown]
MKRRALLALALLLAACAAAAAPAAAAAAADARLNALFDEYWEERLALSPELATSLGDKRYNDRLDDLSAA
ARAARLAALKAFLARLKAIDRAALSPQDRLSYDLLRYQLENALEGYRFRLHEYPINQMSGPHSQLPSLIN
QHPFETVADAEAYLARLAAFPRYFDQAIANMREGAAAGVVPPKFVLEKVIAQLRALIAGAPEDSPLYAPF
KKLPLDISAAEKARLRAEARAAIADKVIPAYQRLIAFLEDEYLPAARTDDGVWALPDGEAYYAALLRYYT
TTDLTPDEIHQIGLSEVARIRAEMEAIMKQVGFKGDLAEFFAFLRTDPQFYYPTREELLDDARAIIKRID
AKLPELFGTLPKAPLEVRPVPAFREPSATSAYYQPPAPDGSRPGIYYVNLYDLKSRPLYELEALAYHEAV
PGHHLQIALAQELEDLPKFRRFGGYTAYGEGWALYAERLGKEMGLYTDPYSRFGRLSYELWRAVRLVVDT
GIHAKGWTREQAIDYMLENTALSEADITAEVDRYIAWPGQALAYKIGQLKILELRAKAEAALGDKFDIRA
FHDAVLGNGAVPLDVLEEKVDRWIAAQ
>gnl|CDD|443834 COG4806, RhaA, L-rhamnose isomerase [Carbohydrate transport and metabolism]
KEENIEKAYELAKERYAALGVDTEAALEKLAQIPISLHCWQGDDVGGFENPDGELSGGIQVTGNYPGKAR
TPDELRADLEKALSLIPGKHRLNLHAIYAETDGEKVDRDEIEPKHFQSWVDWAKENGLGLDFNPTFFSHP
KADDGFTLSHPDEEIRDFWIEHGKACRRIAAYFGKELGTPCVTNIWIPDGSKDIPVDRLAPRERLKESLD
EIFAEKIDKKYNLDAVESKLFGIGSESYTVGSHEFYLGYAAKRNKLLCLDAGHFHPTESISDKISSVLLF
VDELLLHVSRPVRWDSDHVVILDDELQAIAQEIVRNDALDRVHIGLDFFDASINRIAAWVIGTRNMQKAL
LRALLEPTERLKELEEEGDFTERLALLEELKSLPFGAVWDYYCLRNGVPVGEDWLAEVKQYEKEVLSKRS
>gnl|CDD|443835 COG4807, YehS, Uncharacterized conserved protein YehS, DUF1456 family [Function unknown]
MTNNDILRRLRYALDLSDAKMVEIFALGGLEVTREQVSAWLKKEDEPGFVECPDEMLAAFLNGLIIFKRG
KKEGAPPPPPEKRLTNNIILKKLRIALNLKDEDMLAILKLAGFRISKPELSALFRKPGHKNYRECGDQLL
RNFLKGLTLRYRG
>gnl|CDD|443836 COG4808, YehR, Uncharacterized lipoprotein YehR, DUF1307 family [Function unknown]
MKMMKKLLLLLAALVLVFILTGCGSKEETKTYEANENGVEVTLTYTYKGDKVLKQTAENKIPYASLGAKN
KEEAKKLLDPISEKYQGIKGVKESIDYKDEYAIETVDVDYTKADIKKLKKLPGSMFSGDSKKGISMKKSE
KLLEEQGFKEVK
>gnl|CDD|443837 COG4809, Pfk2, Archaeal ADP-dependent glucokinase/phosphofructokinase [Carbohydrate transport and metabolism]. Archaeal ADP-dependent glucokinase/phosphofructokinase is part of the Pathway/BioSystem: Glycolysis
MGVFLAYNANVDAIKRLDGEDLEKLLASFGEEEVLERIEEPPREIDSPSDLVARLLHSMKRGKAAEVPVY
TDDLHEWLKARLGYDELRMGGQAGIMANLLASLGAKPVIAYVPLLSKRQASLFVDKDNLLYPVVEDGKLV
LKPPAEAYDPDEETKINWIFEFSKGDEFFLGGEEIRVPRENRFIAASRPENLRLEIKPELEEHLPEIGEE
VDGAILSGYQMLKEEYPDGSTYEEYLEKAVEVIRRLKRANPDLKVHVEFASIQDEEIRKKILERILPEVD
SVGLDEVELANLLNVLGYDELAARILEKMEIEALYEGAVILLEELGLERIQVHTLGYYLAVTRSDNPLSE
EEVRDALLFAALAAAAKAALGNITSPDDLEAGLKVPVSEKGREALERLEEALGARGAGRKGIGRLTGYTV
VAIPTRVVEKPVSTVGLGDTISASAFVAELALLKKR
>gnl|CDD|443838 COG4810, EutS, Ethanolamine utilization protein EutS, microcompartment shell protein [Amino acid transport and metabolism]
MMDEEEKQRIIQEYVPGKQVTLAHIIANPDPDLYEKLGLDDEEAGAIGILTITPSEAAIIAADIATKAAD
VEIGFLDRFSGSLVITGDVSSVESALREVVEYLGNVLGFTVCEITRT
>gnl|CDD|443839 COG4811, YobD, Uncharacterized membrane protein YobD, UPF0266 family [Function unknown]
LTDIILILFIALLLLYAIYDEFIMDRRKGKTLLKVPLRRRNRIDALIFIGLIAILIYNNITNGGSPLTTY
LLAALILLAIYLFFIRSPKLLFKEQGFFFANVFIPYSRIKAMNLSEDGILVIDLENRRLLIRVKNLDDLE
KIYKFFVGNQ
>gnl|CDD|443840 COG4812, EutT, Ethanolamine utilization protein EutT, cobalamin adenosyltransferase [Amino acid transport and metabolism]
MKVITEDWLRDELKNKEGTEIRLPAGSILTPSAREYLAERKIELKFEDEQGRVFVKEEEQDKPVHGLTEE
GEKPKYVCYLCGAPVDEKPEHMTHLNGNLLVFKNHPRIAFRGKLDSLEALIVLVQTEFAEEGYPKLAEDL
AEILSFLRNIMRAEVLDEPLEEISLLGLSEDELRELSHNPKKYFGHDHILPDYTMGEDVALLNLLRTLVR
ETELAAYEAFKDEDGKVSREDIIQALNRLSSAVYVMMIKVLAGKYKKK
>gnl|CDD|443841 COG4813, ThuA, Trehalose utilization protein [Carbohydrate transport and metabolism]
MIRVTVWNENRHEKENEAVAEIYPDGIHGAIADGLREDAGFEVRTATLDEPEHGLTEEVLAETDVLIWWG
HAAHDEVSDEVVERVQQRVLEGMGLIVLHSGHFSKIFKRLMGTTCSLKWREAGERERLWVVDPSHPIAAG
IPEYIELPEEEMYGEPFDIPAPDELVFISWFEGGEVFRSGCTYRRGRGKIFYFRPGHETYPTYHDPDVQR
VIANAVRWAAPTRGPRPVYGNAEPLEPIEEKGPY
>gnl|CDD|443842 COG4814, COG4814, Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown]
MKKRKFSLILILLIILLIGLLIPKYDWTKSTVKSLKSKYNSKQTPTIFIHGSGGTANSFNTMINRLNEKY
GVGHKVLTVTVSKDGKITYSGKIRKNAKNPIIQVGFEDNRDSIKKQAKWLKKVLKYLKKKYGFKKFNAVG
HSMGGLALTYYLEKYGNDKSLPKLNKLVTIGGPFNGIENEDNNNLTDLLADGKPKPKTQAYKDLIKNRDK
FPKNLQVLNIAGDLNDGTDSDGIVPLASVLSGKYIFQNNVKSYTEIIVTGKDAQHSDLHENPQVDKLIIQ
FLWKKK
>gnl|CDD|443843 COG4815, COG4815, Uncharacterized conserved protein [Function unknown]
ELIQKLIYDPCGLTVSDIQLEKESAEYEACTFKLNGKTIRFRLAKITPKKVGQFVTFWKRDENGPIEPFD
ESDAFDFLIINVRDGNRFGQFIFPKEILIEKGILSTEGKEGKRAFRVYPPWDTPLNKQAKKTQKWQLPYF
LELSKKND
>gnl|CDD|443844 COG4816, EutL, Ethanolamine utilization protein EutL, microcompartment shell protein [Amino acid transport and metabolism]
MLDPLKAKVLAEVVIANVDPDLAEKLGLDPKYRSIGIITADTDDVPYIAADEATKAANVEVVYARSFYGG
AGHASGPLAGEVIGILAGPDPAEVRSGLEAALDFLENTAGFVSANDDGHIEFYAHYISRTGSYLSKAAGI
PEGEAFAYLIAPPLEAVYGLDAALKAADVEVVVFYGPPSETNFSGELLTGSQSACRAACDAFREAVLKVA
ENPKSY
>gnl|CDD|443845 COG4817, GINS, DNA-binding ferritin-like protein (Dps family) [Replication, recombination and repair]
MNWIEKITGSLQKKEYKAYKARAKALPEDYRTAYKAIQRYLWYFGGTDGDDLVRILEDLLDLFEEAAADG
TPVREVVGDDVAEFADELARDYGGGTWIDKERERLNKAIDRKLGKLG
>gnl|CDD|443846 COG4818, COG4818, Uncharacterized membrane protein MJ1443, UPF0132 family [Function unknown]
LDENIAAALAYLLGWITGIIFLLLEKKNRFVRFHAMQSLLLFLGLFVLSILLTLSFIPVLGWLISLLLGL
ASLVLWIVLMVKAYRGERYKLPVIGDIAEKLVKKL
>gnl|CDD|443847 COG4819, EutA, Ethanolamine utilization protein EutA, possible chaperonin [Amino acid transport and metabolism]
MATEELLSVGIDIGTSTTQLIFSRLTIENRASGFSVPRIEIVDKEVIYRSPIYFTPLLSPTEIDAEAVKE
IIEEEYKKAGITPEDIDTGAVIITGETARKENARAVLHALSGLAGDFVVATAGPDLESIIAGKGSGAAAY
SKETGTTVVNIDIGGGTTNIAVFERGEVIDTACLDVGGRLIKVDPSGRVTYISPKIQRLADALGLPLEVG
DRADPEQLRKIADRMAELLVESLGLGPLSPLTKALLTTPPLKLDYPIDAVTFSGGVADCIYGPEEADVFR
YGDIGPLLAQAIRESPALRALPVIQPEETIRATVIGAGSHTTELSGSTITYTADLLPLKNIPVLKPSLEE
EELSPEELAEAIKRALAWFDLEGEQQPVALALKGLKNPSFAEVQELAEGIAEGLEEYIAKGLPLIVVLEN
DMAKVLGQTLRALLPKKRPLICIDQVKVENGDYIDIGEPLAGGRVVPVVVKTLVFNS
>gnl|CDD|443848 COG4820, EutJ, Ethanolamine utilization protein EutJ, possible chaperonin [Amino acid transport and metabolism]
NERLKEFAELINKPRPVPPGGPLKVGVDLGTANIVLVVLDENGRPVAGALRWASVVRDGLVVDYIGAVRI
VRELKAELEERLGRELTHAATAIPPGTSGGDVRAIANVVEAAGFEVTNVVDEPTAAAAVLGIKDGAVVDI
GGGTTGISILKDGEVVYTADEPTGGTHMSLVLAGAYGISFEEAEQLKRDPANHREVFPVVRPVIEKMASI
VKRHIAGYDVDPIYLVGGTCCFPGFEDVFEKELGIPVVKPPHPLLVTPLGIAMSCPREAE
>gnl|CDD|443849 COG4821, COG4821, Uncharacterized conserved protein, contains SIS (Sugar ISomerase) phosphosugar binding domain [General function prediction only]
MTDLASQYLDEVRELLDRIEETQAEAIEKAADLIADSIAAGGLVHLFGTGHSHLLAEEVFYRAGGLVGFN
PILDPSLMLHNGAPGVLQSSFLERVEGYAEIILENYPIRPGDVLIVISNSGRNAVPIEMALEAKERGLKV
IAITSLEHSKAVPSRHSSGKRLFELADVVIDNCVPYGDAVLPLEGLDTKVGPVSTVAGAFILNSLVAEVA
ELLAERGIEPPVFRSANVPGGDEHNEALLEKYRGRIRRLA
>gnl|CDD|443850 COG4822, CbiK, Cobalamin biosynthesis protein CbiK, Co2+ chelatase [Coenzyme transport and metabolism]. Cobalamin biosynthesis protein CbiK, Co2+ chelatase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
MMMKKAILVVSFGTSYPETREKTIDAIEKKVKAAFPDYEVRRAFTSRIIRKKLKKRDGIHVDNPLEALAK
LKDEGYTEVVVQPLHIIPGEEYHKLVREVRALKDGFKRIVLGRPLLYSPEDYEEVAEALKAQIPALKKDE
AVVLMGHGTEHPANAAYAALQYVLRRLGDPNVFVGTVEGYPELEDVIERLKAAGIKKVTLMPFMLVAGDH
ANNDMAGDEEDSWKSILEKAGFEVEVVLKGLGENPAIQDIFVEHLKDALEELGLD
>gnl|CDD|443851 COG4823, AbiF, Abortive infection bacteriophage resistance protein [Defense mechanisms]
MKYTKPALTYEEQIELLKERGLIIDDEEKAERYLKRIGYYRLSGYWLPFRKSDAGDDRFKPGTTFEDILA
LYLFDRELRLLLLDAIERIEVALRTKLAYHLAEKYGPFAYLDPSLFKDRSKHAKFLKKLEREISRSKEDF
IKHYKQKYGGLPPIWVAVEVLSFGTLSKLYSNLKNRDKKAIAKEFGLDSKKVLESWLHSLNYVRNICAHH
SRLWNRKLTIKPKLPKKKKVPLLTNSAANNRLYAVLVILKYLLDTISPGSSWKNRLKALIEEYPEIDLAA
MGFPENWESLPLWKV
>gnl|CDD|443852 COG4824, COG4824, Phage-related holin (Lysis protein) [Mobilome: prophages, transposons]
MKKIIIKAIVATIGGVLGYLLGGWDGLLYALVILMVIDYITGVLAAIKEKKLSSKKGFKGIAKKVLIFLL
VAVAHLLDQVLGTGGFIRTAVIFFYIANEGISILENAGRLGLPIPEKLKKALEQLKDKKDEKKDK
>gnl|CDD|443853 COG4825, MT1736, Uncharacterized conserved protein, contains thiamine pyrophosphokinase N- and C- domains [General function prediction only]
MKLPLLSRRKEALPGVTGTARVDRRTKNLLKRLKPGDIAVIDHPDLDRVAAEALVAAKVAAVVNAAPSIS
GRYPNLGPEILVDAGIPLVDDVGPDVFDRLKDGDKVRIDDGSVYLGERLVAEGVELTAETVEDKMEEARA
GLSDQLEAFAANTLEYLRRERDLLLDGVGVPDLRTDFEGRHVLVVVRGYDYKEDLKALRPYIREYRPVLI
GVDGGADALLEAGYKPDLIVGDMDSVSDEALRSGAEVVVHAYPDGRAPGLERVQDLGVGAVTFPAPGTSE
DLAMLLADEKGAELIVAVGTHATLIEFLDKGRAGMASTFLTRLKVGSKLVDAKGVSRLYRSRISAKYLLL
LVLAALLAVAVALAVSPAGQALLDLLGLRWRDLLGW
>gnl|CDD|443854 COG4826, SERPIN, Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones]
MKRRRLLLLLALLALLLAGCSSSPSSTVSRTATPSVDAADLAALVAANNAFAFDLFKELAKEEADGNLFF
SPLSISSALAMTYNGARGETAEEMAKVLGFGLDLEELNAAFAALLAALNNDDPKVELSIANSLWAREGFT
FKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPPAIDPDTRLVLTNAIYFKGAW
ATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDGFQAVELPYGGGELSMVVILPKEGGSLEDFE
ASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGMTDGENLYISDVIH
KAFIEVDEEGTEAAAATAVGMELTSAPPEPVEFIADRPFLFFIRDNETGTILFMGRVVDPS
>gnl|CDD|443855 COG4827, COG4827, Predicted transporter [General function prediction only]
ILWQLGILFAILIFGIKTGLGLGFSGISKKNILLIALLYGVGIFLLGALLSYVDQSILEFIDRYGMLIHV
LMALLLIGAGIYTIKKWKCNGKDVSKLTFLAISLPCPVCLTALAFSIILLAPIVGLSGWLLGLLVGVLFF
ISIIATYLGFRKILRVLKKPYPIILGNFMLFLGLYFLLGALIIPNYIQAKQMPMTPLSLPSPDIIPLVVL
ALLGLILAGFFLNRKKSVKEE
>gnl|CDD|443856 COG4828, COG4828, Uncharacterized membrane protein [Function unknown]
ELLEEIVEIIALILEAIGVLVIVIGALVALIRFLRRELRRRKADAYRRIRLTLGRSLLLGLEFLLAADIL
RTVVAPTLEELGVLGAIVLIRTFLSYFLEKEIEGRWPWQRAEED
>gnl|CDD|443857 COG4829, CatC1, Muconolactone delta-isomerase [Secondary metabolites biosynthesis, transport and catabolism]
MLFLVRMTVRIPPDMPAEEVDELKAREKAYAQELQRQGKWVHLWRVVGRYANISIFDVESNEELHAILSS
LPLFPYMEIEVTPLAPHPSDIADDDR
>gnl|CDD|443858 COG4830, RPS26B, Ribosomal protein S26e [Translation, ribosomal structure and biogenesis]. Ribosomal protein S26e is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MPKKRKNRGRHKGGKGKEGTVQCDNCGRLVPRDKAVCVTRRYSPVDPQLAKELEKKGAIIPRYPVTKCYC
ISCAIHLGIVKVRAEEERKPKLPL
>gnl|CDD|443859 COG4831, COG4831, Roadblock/LC7 domain [Signal transduction mechanisms]
MSKLDELMKLPGVVAAGEFSDDGDLVEYKGELTEEEAEMLAKMCAANTMMVQMQADMLSAFSGMKGWTPV
RGWAVRGPEYSVCVVGNVGCFVENAEADFNEIFKALAE
>gnl|CDD|443860 COG4832, MA1133, Cyclopropanoid cyclopropyl hydrolase, GyrI-like domain [Defense mechanisms, Signal transduction mechanisms]
MKIDLKKELKELYLPKGKPEIVDVPPMNFLMIDGKGDPNTSPAYAEAVEALYSVAYTIKFASKKELGRDY
VVPPLEGLWWADDMAAFTARDKSEWRWTLMIRQPDFVTEELFEEAVEEVARKKPLPALDKVRLETLEEGL
CVQILHVGPYDDEPPTLAKMHEFIPENGLVRNGKHHEIYLSDPRRTAPEKLKTILRQPVKRA
>gnl|CDD|443861 COG4833, COG4833, Predicted alpha-1,6-mannanase, GH76 family [Carbohydrate transport and metabolism]
MKKLLLPASASNWAARADAAEQALNSRFLNRLGYWGLRDERGFGTWHYWWQAHALDALVDAYRRTGDPRY
RTLIEDLYRGIRVRNGGTWTNDYYDDMAWLALALLRAYDLTGDRRYLDAARELFDDVWSGWDDECGGGIW
WRKGRDYKNAPANGPAAILAARLYNRTGDPAYLDRAKKIYDWLKATLVDPGTGLVNDGINLSNNGEIDDW
VYTYNQGVFIGAAVELYRATGDARYLDDARRTADAVTRSLLTPNGVLRDEGGGDGGLFKGIFARYLAELA
RDLPLRKTYAAFLLRNAESAWANRRVDSGPLFGPDWTGPADLPDEVDLSVQLSGWMLLEAAARLAREG
>gnl|CDD|443862 COG4834, COG4834, Uncharacterized conserved protein, DUF2184 domain [Function unknown]
MRKHMTYDAATQDAGAFLARQLERIDPTIYEALYPELTARRLIPVKTDVPEWAETVTYTVMDRVGAAKII
AGYADDIPLVDVDIERHTAPVYLAGIGYGYTLQELRAAQLLGRNLDTRKAEAARRAIEEKINQIALVGDA
AKGIEGLLNHPGVPVTTAAATGAGSTKWKDKTAEQILADVNAALNSVWAASGYVETPDTLLLPPTQFELL
SSTRVSDNGNKTILKFLQENNIFAENGRPLTIRGVPELEGAGTSGTDRMVAYTRDPDVVEMHLPMPLTFL
PAQYRGLRFKVPGEFRTGGVEVRYPKAIRYADGI
>gnl|CDD|443863 COG4835, COG4835, Uncharacterized conserved protein [Function unknown]
EIKREQEFVEQYHYDARNKEWEKPETEVNVGFQLLEPDEEEDLPEKGTILVAVLPFDIVLDEFVISGAIS
QINQIVDRYFGEPSDLSQEEVEELSRPLLDYIKRLTYEVTEIALDRPGVNLNF
>gnl|CDD|443864 COG4836, YwzB, Uncharacterized membrane protein YwzB [Function unknown]
SIGQQALISIVSHLLFIALAWWALQALRFDKFFKKGRVFQARLLYIFLSIAIGYTVSNFFLDYLGWSQQL
PYLFS
>gnl|CDD|443865 COG4837, YuzD, Disulfide oxidoreductase YuzD [Posttranslational modification, protein turnover, chaperones]
ITVYGAEVICASCVNAPSSKDTYEWLQAALGRKYPDQPFNYTYIDIEEPPENEEDQQFAERILEDELFYP
LVVINDEIVGEGYPQLKPIYRFLEKHGYT
>gnl|CDD|443866 COG4838, YlaN, Uncharacterized conserved protein YlaN, UPF0358 family [Function unknown]
EDDSKEKALELLQEDADKIKKLIKVQMDNLTMPQCPLYEEVLDTQMYGLSREIDFAVRLGLITEEEGKQL
LSDLERELSDLHEAVTEKKK
>gnl|CDD|443867 COG4839, FtsL2, Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning]
MAVNAAREQQAQQPQQQPRTEPQPRKVKKKKRKKITKGEKLLYLLFVVVLLVLAIVLLSLQASIYELNRE
IQSLESKISEQQKENEDLEQEVSELSSPERIYKIAKKLGLKLNNSNVKVVQKQ
>gnl|CDD|443868 COG4840, YfkK, Uncharacterized conserved protein YfkK, UPF0435 family [Function unknown]
MNLSEPSTENLAYMIEEIKDKLRMVNASAMDPEDFDLEKYEDLKDLYDMVMKKNQFSPSEMQAIAEELGS
LRKS
>gnl|CDD|443869 COG4841, YneR, Uncharacterized conserved protein YneR, related to HesB/YadR/YfhF family [Function unknown]
MKITITDQALKWFKEELDLESGDGIRFFVRYGGSSPVQEGFSLGVTVEEPDEPAVETEVDGITFFVEEDD
LWFFDGHDLTVDYDEKTDEPVFEYK
>gnl|CDD|443870 COG4842, EsxA, Secreted virulence factor YukE/EsxA, WXG100 family [Defense mechanisms]
IRVDPEALRAAAGRFGAAAGELQALLDDLRSQLAALQSSWEGDAATAFQAAQAQWDQAATKLNQALEDIA
QALRQAADAYEEAEQANAALFGG
>gnl|CDD|443871 COG4843, YebE, Uncharacterized conserved protein YebE, UPF0316/DUF2179 family [Function unknown]
MEMLFSPLLLPLLIFLARIVDVSLGTLRTILVVKGKRYLAAILGFFEVLIWLLALGQVLQNLDNPLNLIA
YALGFATGNYVGIKIEEKLALGYVLVRVITREDGDELAEKLREAGFGVTSVDGEGRDGPVLILFIVVKRK
DLKELLAIIKEIDPKAFYTVEDVRSVSGGFFPKRVRRRRLR
>gnl|CDD|443872 COG4844, YuzB, Uncharacterized conserved protein YuzB, UPF0349 family [Function unknown]
MNPIVEFCDSNLASGTDEVLEKLEEEDPDVDVLEYGCLSYCGLCAKKPFALVNGEIVEAETPEELLEKIY
EAIEENPALK
>gnl|CDD|443873 COG4845, CatA, Chloramphenicol O-acetyltransferase [Defense mechanisms]
MMYKPIDLETWPRKEHFEFFRNFDPPTFSITVELDVTALYKYAKKNGLSFFPAYLYAILKAVNEIPEFRY
RIEDGEVVEYDVIHPSFTIFHKEDETFSFVWIPYDEDFETFYANYLEDIERYKNSTGLFPKEGNPDNLFY
ISCLPWLSFTSFSHAIPGNPDDSIPIITFGKYYEENGRLLMPVSIQVHHALVDGYHVGRFLEELQELLDE
>gnl|CDD|443874 COG4846, CcdC, Cytochrome c biogenesis protein CcdC [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
MLLIASTIVALLMALLVIFIRMKAAKKPASAKKIILPPLFMSTGALMFLFPEFRVPWLEALEAFLVGLLF
SIPLIKTSKFEVRGDDIYLKRSKAFIFILIGLLVIRIVLKLYLSGTIDPGELGGMFFLLAFGMIVPWRIA
MYIKYRKLEKELNAVAI
>gnl|CDD|443875 COG4847, COG4847, Uncharacterized conserved protein, DUF2175 family [Function unknown]
MMTKWKCYICGKEIVEGEKFTFTKKGPVHYTCLVEKARKKIKGDPEDLRALLDLLEYELTGIVRYKELLR
LASDEEAKEVLDQRRKDAEKNAAKLTRLIEKLSGVL
>gnl|CDD|443876 COG4848, YtpQ, YtpQ protein involved in methylglyoxal resistance, DUF1444/UPF0354 family [General function prediction only]
LRAMEEESTLAGARSRIFPVIRSTSFPEETKEGHPFVYEPHTAELRIYYALDLGESYRLIDEEMLEEWGV
TEEELRELALFNLRRLPTEPKVDEVAGNGFYFLNTNDGYDASRILNEEFLEEMRAKVEGELVVAVPHRDV
LIIADIRNEEGYDVLAQMAMQFFAEGPVPITSLLFVYENGELEPFF
>gnl|CDD|443877 COG4849, COG4849, Predicted nucleotidyltransferase [General function prediction only]
MSNLITISQLLDPEIKEVLTDLKEVADSLNIPFFVIGATARDLLLEHVHGIPPGRATRDIDIAVAVDDWE
QFEALKDALIEGGKFTKDPDQAHRLHYKDGIELDLVPFGGIENEDGEISWPPDGEIIMSVLGFEEAYENA
LTVEIDDGIEIKVASLPGLALLKLIAWDDRPERRNKDAKDILFILENYFDIEEDRIYEEYNDLLEAEDFD
LELAGARLLGRDIAQIASEETKERIKNILEKEISDIKQSKLVRQMVEAGDEDYEEIVQLLEALLYGLEET
LKK
>gnl|CDD|443878 COG4850, App1, Phosphatidate phosphatase APP1 [Lipid transport and metabolism]
MSLRPHLAARLEDALHRLARRLRRRGWPPRIIPYRGYGTPERVRVLGRVLLDRPIDRDLEQDSLWRNLVR
GWRRFETDPVPGARVTVTLGGQEVETVTDRDGYFDVEVPLVGLEPGWHTVELSLLDGEGVPVEAPVLIPP
PDARFGVISDIDDTVLVTGLPRPLKAAWNTFVKNAHARKPFPGMAALYRALHAGHPGNEGNPFFYVSSSP
WNLYPTLERFLRRNGFPKGPLLLRDWGPTNTGWFRSGHEHKREEIRRLLEEFPDLRFVLIGDDGQHDPEI
YAEIAREHPDRIAAIYIRQVSPKEGRPEAVEALLKEIEAAGVPVVLAPDGAEAAEHARALGLIAPEAV
>gnl|CDD|443879 COG4851, CamS, Uncharacterized conserved protein involved in sex pheromone biosynthesis [General function prediction only]
MKKILWILLLASLLLLSGCGPSFDKEEEVVQETGKKEETAIIPKYQISDSYYRTVLPYKTSAARGLTVSN
MNNRYDIDEFETGLMRLSKEVFSTDDYFFQEGQYLDKDTVTSWLKRKYTDEESKSNPLGLNPALNGETDP
EEKAKRNPIYLSHILEQDYLVKTDDDKVKLGGISIGLAMNSVYYYQKEQYGATYEEEISDAEMLEQGKKM
AQEVVKRLRQMEGLKDVPIVIALYKQAPRDSLVPGNFFAYATVKSGSSSIGDWKSINEKYVLFPSDEATK
KYRDDNTNFSNFKQDIEDYFPNYTGVIGTGFYQDDELQKLTIDIPIQFYGKAEIIGFTQYVTGLVMKYFP
SYVPVEVTITSVNGPEALIVREAGDKEPFVHIYE
>gnl|CDD|443880 COG4852, COG4852, Uncharacterized membrane protein [Function unknown]
RYLIAYLATLVVFLVLDALWLGVIAKPLYRPHLGHLLADSPNLAPAALFYLLYVAGIVFFAVRPALAAGS
LLTALLYGALFGLFAYGTYDLTNLATLKDWPLTVTLVDIAWGTFLTAVSAWAGYLVARRLTGR
>gnl|CDD|443881 COG4853, YycI, YycI protein, regulator of the WalKR two-component signal transduction system [Signal transduction mechanisms]
MDWSKIKTIFIIVFLILNIFLLFQLIEKQQENQVLSSLSETTIEERLKADNITLKTDLPKETPPGSYLSA
KFKDFTEAELEQLKGQKVKISDNTKLYSTLKEPIKISDKDDLEDLEDFVKSNVLFGKEYQYWKYDSDGNT
IVFFQTYDGRPIYYNQNAQLTFYLNDDNEITSYTQTYLDDIEELGEKKDLISAIKAIETLYENNELPSNS
TITDIKLGYYSLVQLSDTQVLAPTWRITVENEDGTEIYFVNAITGEIIE
>gnl|CDD|443882 COG4854, COG4854, Uncharacterized membrane protein AF1626, predicted component of bacteriocin or quorum sensing system, DUF2178 family [Function unknown]
MKKNTYRLILIVIAIFEGAILGYAVEIGNPLLAVGVFIAGIALSYLVKRRVDGVIEDERTYRIAEKASRR
TLQVFGIVFALGGAGLIVISLTIPGYTELGYLLAYLLCFLIFLYLLFRMYYSRKYGG
>gnl|CDD|443883 COG4855, COG4855, Uncharacterized conserved protein [Nucleotide transport and metabolism]
MKCYDCAEEGKDTDAVAICIVCGMGLCMEHLVREELPVWEGGYPFPLKKLKKPLPRILCPECHDALKEDG
>gnl|CDD|443884 COG4856, YbbR, Cyclic di-AMP synthase regulator CdaR, YbbR domain [Signal transduction mechanisms]
MKKLLKNNWFLKILSLLLAILLWLYVMNEQNPIVTRTITNVPVEVVNLLDPEGLVVSGELPETVTVRVRG
PRSVLLSLSASDIKAYVDLSGLKPGTHTVPVKVEGNLPSGVEVVEVSPSTITVTLEKKVTKEVPVEVEVK
GKPAEGYEVGEVSVSPSTVTVSGPESVVNQIDSVKATVDVSGATEDFTKSVPVKAYDANGNELDVTISPS
TVEVTVPVLPSKTVPVKVNTTGEPAEGYSVTSITVSPSTVTIYGPEEVLDSISSIETEPIDLSGLTESTT
VEVKLKLPEGVTLVDPPSTVTVTVEVEKKTTKTFENIPITVENLPDGLTASISPGTVDVTVSGPKSVLDS
LTASDIKAYVDLSGLGPGEYTVPVQVELPEGVEVPAKVTVTI
>gnl|CDD|443885 COG4857, MthN, 5-Methylthioribose/5-deoxyribose kinase, methionine salvage pathway [Amino acid transport and metabolism]
MSEYFPLTEEDVIAYLKEKAGLFGPDALLTVREIGDGNLNLVFRVSDEGTGKSVIVKQALPYVRVVGESW
PLTLDRARIEAEALRLQAELAPGLVPKVYHFDEELALIVMEDLSDHKILRKELIAGKKFPGFAEHIGTFL
ARTLFYTSDLYLDPKEKKALVAKFINPELCKITEDLVFTDPYFDHERNNWTPELDPVVEALRSDEALKLE
VAKLKYRFMTKAEALLHGDLHTGSIFVNEDSTKVIDPEFAFYGPIGFDIGNLIANLLLNYASQPGHDSDE
EERADYRAWLLDTIEEIWETFEAEFRELWREEAKDPYAAAEGYLEAYLDRILQDALGFAGCELIRRIIGL
AHVADLDSIEDPEKRAAAERLALELGRALILNREEIKSIDDLTALIREIAKEFQ
>gnl|CDD|443886 COG4858, COG4858, Uncharacterized membrane-anchored protein [Function unknown]
MSEEKLEEMVEQNNELREQLTKKNQEYIFDLRKYLRASGKSEEEIEEILEEMLPELLEAQKTGKTARQLF
GTPTEYAEEILEEPKKASENSPPWLLWLDGSLLLLGIFSLLSGIMGFFSKNAQNLTYGILTLILNSLVGG
LAMYLVYKYLYRSGAKKGKRPGFWKYILILVLAMLVWILLFTATALLPPSINPVLPPIVYLIIGVVAFGL
RYYLKKKYNIQGSLFAIRRM
>gnl|CDD|443887 COG4859, COG4859, Uncharacterized protein, contains DUF2185 domain [Function unknown]
MEEIRELWEGAGGCIVSDRITVEGEPVGFMYREEPDNEQDSGWRFFSGDETDEYMDDPDNFGIYSLNTIL
NIDPAIIPLLDAPYGTAFERDEDGNKFVPVEDWEPQ
>gnl|CDD|443888 COG4860, COG4860, Predicted DNA-binding transcriptional regulator, ArsR family [Transcription]
MVKRIKIINDPSELVPLLQAFDSEVKKKVYDELSTEWMTEEELEEKYGEDVTEALKILKKGGLVESQWRM
PEPGQKPEKEYHTSYSKVQANFQCSMEDLSDIIYLAFMSDEELREYVEEIEEEVENGNVSLGDLARKLGI
SPTFIRGLAKRSSKLDVKGQRLELVKEEE
>gnl|CDD|443889 COG4861, COG4861, Uncharacterized conserved protein [Function unknown]
IDIRNEAIKNLEKEIPIALNLKLPLKKEDGGDTGPLPLLGGDVVVTLVVERKRTVINLQLDLLELLLNKT
KNPLLLVADYLSPALAERLRERGINFIDTAGNAYINQPGLYIFIEGRKPTKSRKKKSNRAFTPTGLKVLF
ALLSDPDLLNAPYREIAEAAGVSLGTVGKVLKELRELGYLRKTNKNGRRLENYEELLERWAEAYPERLRP
KLLLGRFRAPDPRWWKDIDLAQPKTVWGGEPAAAILTGYLRPEEATLYTEEPLRDLIKQLRLRPDPEGNV
ELLEAFWNKDLKENRNPLAPPLLVYADLLASGDPRNKETAQRIYEEYLQLKQL
>gnl|CDD|443890 COG4862, MecA, Negative regulator MecA of genetic competence, sporulation and motility [Transcription, Signal transduction mechanisms, Cell motility]
MEIERINENTIKIFITYDDLEERGITLEDLWYNREKVEELFWDMMDEADEEEGFELDGPLWIQVQPLPAQ
GLEVIVTKAKDDKDGSDDDDEELLDEDFEELLVQDKEKEDDEKEKTLDESLEFIFSFDDFEDVIQLAKRL
PRLYSGESSLYKYEGKYYLVLEFEELDDEEFEDLIAILSEYGEPSTITIARLEEYGKVIIKENALEQLRK
YF
>gnl|CDD|443891 COG4863, YycH, YycH protein, regulator of the WalKR two-component signal transduction system [Signal transduction mechanisms]
KYKETIKSILLTLLVLLSLVLTFAIWTYQPNYENIESTETSVSTEPISKEKSLEDVVRPYQIVYHFGGNH
YGTADENLIEELYNELKNWSFSNIELSSNISREEYESLRSNNSIELIFPDEIPLSLLLSIFNIEDSGNLP
ESSFDRIVIDLNENENNKIYFISDDEKKVYEAKISNADLSNLRKLINKEKEDYIPYTELETLLDNNVYLP
SEPVKLKKYSYLVEEISIEPFKNALFSDPSIVRSIVENNGSTIYTDGSRLLTIDSDNGRLEYVNPSASES
SESLSPYELLNDSFDFINDHGGWTDDYRLFGIDASGYTVTFRLYVNGLPVFSDDGMSDISVTWGNGDVYE
YKRPLYSLDVPIPSEKEEVTLPSGEEVIEALEKNAGYDLNKIDDIEIGYELTKDEENDQVVDLEPTWYVK
YNGEWYSLDSLELYGGEIVGLE
>gnl|CDD|443892 COG4864, YqfA, Uncharacterized conserved protein YqfA, UPF0365 family [Function unknown]
MMMSLIGIIVLVILILIFLFIFFSFVPVGLWISALASGVRVGIFTLVGMRLRRVPPSVIVNPLIKATKAG
LDLSTNQLEAHYLAGGNVDRVVDALIAAQRANIDLSFERAAAIDLAGRDVLEAVQMSVNPKVIETPTIAA
VAKDGIQLKAKARVTVRANIDRLVGGAGEETIIARVGEGIVTTIGSSESHKEVLENPDSISKTVLEKGLD
AGTAFEILSIDIADVDVGENIGAKLQTDQAEADKRIAQAKAEERRAMAVAREQEMKAKVQEMRAKVVEAE
AEVPLAMAEAFRSGNLGVMDYYRMKNIQADTEMRESIAKPGEPKKSGEPS
>gnl|CDD|443893 COG4865, GlmE, Glutamate mutase epsilon subunit [Amino acid transport and metabolism]
MELRNKKIDDEEFLEIRKEVLSQWPTGKDVDLEEAVAYHKSLPESKNFAKKLEKADAEGRTLVQPRAGVA
LLDEHIELLRYLQEEGGADLLPTTIDSYTRQNRYEEAEQGLEESRKTGRSLLNGFPAVNHGVKGCRKLVE
AVDVPLQVRHGTPDARLLAEITLAGGFTSFEGGGISYNIPYAKDVSLEKSIEDWQYVDRLVGYYEENGVI
INREPFGPLTGTLVPPSISIAVAIIEALLAAEQGVKSITLGYGQCGNLVQDVAALRALRELAEEYLPKFG
YKDVEITTVFHQWMGGFPQDEAKAFGVISWGAATAALAKATKVIVKTPHEALGVPTKEANAAGLRTTKQV
LNMLKDQRFPDSEELEEEKELIKREVRAILDKVLELGDGDLAVGIVRAFEAGVLDVPFAPSRYNAGKVLP
ARDNEGAVRYLEFGNLPFSEEIKDFHRQKLEERAKAEGREVSFQMVIDDIYAISKGRLIGRPR
>gnl|CDD|443894 COG4866, COG4866, Uncharacterized protein, contains DUF2156 domain [Function unknown]
MMDFKPITLEDKELLDEYLKAYPYRLSDYSFANLYIWRHYYNYEYAIIDDCLVIRGTTEGGLPFYLPPLG
PGDLAEALEELLEYAKEEGEPLRLRGVPEEFLEFLEELYPGRFEVEEDRDNFDYIYLTEDLATLKGKKYH
KKRNHINRFKKNYDYEYEPLTPENIEECLEFLDEWCEQRGCEEDESLENERRAIKEALEHFDELGLKGGV
IRVDGKIVAFTIGERLNDDTAVVHFEKADPDIKGLYQAINQEFAKHLFEDYEYINREEDLGIEGLRKAKL
SYHPVKLLEKYTVKLK
>gnl|CDD|443895 COG4867, COG4867, Uncharacterized conserved protein, contains von Willebrand factor type A (vWFA) domain [Function unknown]
MMRGFRYGRYEPLGLGDATGAMQDLAELDALLEQLSQLLPGARLDDIDLDALDRQLGDTAAVDARTLRDL
ERELREQGYLRREADGGLELTPKAERRLGKSALRDIFGKLKKGRRGNHDTRRAGAGGELTGETRPWEFGD
TLPLDVTRTLRNAVLRHGPGGPVRLDEEDLEVEETEYRTQAATVLMVDTSHSMILYGRWTPAKKVALALA
HLIRTRFPGDTLDIIVFGNDAWEVEIKELPYLQWVGPYGTNTHHGLLLARRLLRRHPNANKQILMITDGE
PTAHLEPDGEYYKFSYPPDPETLAKTLAEVDRCRRLGIPITTFMLARDPYLARFVDEFTRRNGGRAYFPD
LDGLGAYVVEDYLRNRRKRVR
>gnl|CDD|443896 COG4868, COG4868, Uncharacterized conserved protein, UPF0371 family [Function unknown]
MKIGFDNEKYIEEQSEHILERINQFGGKLYLEFGGKLFDDYHASRVLPGFDPDSKIRMLQKLKDQVEIII
CINAGDIERNKIRGDLGITYDEDVLRLIDDFRSYGLLVNSVVITRYEGQPAADAFKNKLERRGIKVYRHY
PIKGYPTDVDLIVSDEGYGKNEYIETTRPLVVVTAPGPGSGKLATCLSQLYHEHKRGIKAGYAKFETFPI
WNLPLKHPVNIAYEAATADLDDVNMIDPFHLEAYGETAVNYNRDVEIFPVLKRILEKITGESPYKSPTDM
GVNMVGFCIVDDEVVREASKQEIIRRYFKALCDYKKGLVDKETVERIELLMEEAGLSPEDRPVVAPAREK
AEETGGPAAAIELPDGTIVTGKTSPLLGASSAMLLNALKHLAGIDDDIHLISPEIIEPIQTLKTKHLGSR
NPRLHTDEVLIALSISAATNPTAQLALEQLKELRGCDAHSTVILSPVDEQILRKLGINVTSEPVYQSKNL
YHK
>gnl|CDD|443897 COG4869, PduL, Propanediol utilization protein [Secondary metabolites biosynthesis, transport and catabolism]
MDEELIEQIVREVLERLASKPLTIPVGVSNRHVHLSQEDLEILFGPGYELTPKKDLSQPGQFAAEETVTL
VGPKGVIENVRVLGPVRKETQVEISRTDAFKLGIKAPVRESGDLEGTPGITLVGPKGSVELEEGVIVAKR
HIHMSPEDAEKLGVKDGDRVSVKVEGERGLIFDDVLVRVSPDFALEMHIDTDEANAAGLKNGDKVEIIKK
>gnl|CDD|443898 COG4870, COG4870, Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]
AAALPSSVDLRGYVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPGTSLDLSELFLYNQARNGDGTEGT
DDGGSSLRDALKLLRWSGVVPESDWPYDDSDFTSQPSAAAYADARNYKIQDYYRLPGGGGATDLDAIKQA
LAEGGPVVFGFYVYESFYNYTGGVYYPTPGDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFW
ISYDDLLIGAGAAYDPWSIGTTAYTIYVYVDLVAGPPPSSGTAAASAGTTSSTGYGTLVLDITVLLGGGG
KFSVVAKLVTPASEGPISVEYSIGSYDSTTAASSNGSSDAVSLYNGADVSSEAANSNAAATANTTITLET
TAALSAEGTTGVKTGSTSTPDASSSAPKSGESVDLNGVLGKEGSNTVTSAAASTGGLALGEEVTEEGNGT
SDEVLA
>gnl|CDD|443899 COG4871, COG4871, Metal-binding trascriptional regulator, contains Fe-S cluster and ArsR family DNA binding domain [Transcription]
MLLEIYSLEQVKPCIADASKVRAIAHLDQDISEALPYLNAVLGGANYSPRPPSLTFKKGGRLITLYPRKI
TVNKLKDEEEAYEILEWLKDLINDAWEKKDEITPLYEERERPGVIEIYKLLPKTNCGKCGEPTCMAFAAK
LLAGEKGLDDCPPLKEEEYAENREHLETLLEYLGYDT
>gnl|CDD|443900 COG4872, COG4872, Uncharacterized membrane protein [Function unknown]
MISKKFRQRLRQELKRWVEEGLISAEQAEAILARYEFRRARSRFVRILLILGALLLGLGILLFVAANWQE
IPRLAKLALLLALLVGAYGAGFYLEERGSPRLGEALLLLGALLFGAGIALIGQMFHLSGDFPGLFLLWAL
GALPMAYLLRSRPLGILAILLAGIWSGLELFDLLSVVPWMPLLLLLLFLPLAYWCRSRWAFHLAALALIG
SLALLLLSSLIALWVFAIALALAARNLGLLFFGLVGYLLSFPPFWSGAYILLLLLVGFSIGAIGELGSII
FNVLLLALAIGLIRLGLLRGNRGIFWLGLLLFALQILSRYFDTAGDLLPKSLFFLLGGLLLIALGYWFER
KRRRLSAASEK
>gnl|CDD|443901 COG4873, YkvS, Uncharacterized conserved protein YkvS, DUF2187 family [Function unknown]
MAKPEMKKAEVGDIIEFKDGLKGKVEKVNENSVIVDLTIMENFDERDLEYEKTVVNHKNYKIIERADQ
>gnl|CDD|443902 COG4874, COG4874, Uncharacterized conserved protein [Function unknown]
MMMQTTNTVLMVRPVAFRFNEQTAVDNAFQKDLALSNEEIQAKALAEFDAFVEKLRSAGVNVIVFDDTPE
PDTPDSIFPNNWFSTHEDGTVALYPMFAENRRLERREDILEMLEEEFRVQEVIDYSGLEEDGLFLEGTGS
MVLDRVNRIAYAALSPRADEELLEEFCEDFGYEPVVFDAVDGKGKPIYHTNVMMCVGEDFAVICLDSIDD
KKERKEVLERLEESGKEIIEISEEQMNNFAGNMLQVKGKDGKRYLVMSQRAYDSLTPEQIAAIEKHCEIL
PSDLPTIETLGGGSARCMMAEVFLPKRE
>gnl|CDD|443903 COG4875, CaMKIID, Protein kinase association domain CaMKII_AD, NTF2-like superfamily [Posttranslational modification, protein turnover, chaperones]
MKRLLTLLLALLAVLAAASPAAAPAAAPDCAAATEAQIAALFDRWNAALQTGDADKVLALYAPDAVLLPT
VSNKVRTTRAEIRDYFEHFLAKKPQGVIDERTIKIGCNTAVDSGTYTFTFTKDGSTLTVPARYTFTYEKQ
GGQWLITSHHSSAMPE
>gnl|CDD|443904 COG4876, YdaT, Uncharacterized conserved protein YdaT [Function unknown]
MPWTMNDYPASMKNLDPLVRKKAIEIANALLDEGYDEGRAIPIATEQAKEWYRNASKEEEKELKKEDNPQ
KRDDHDSPELLDEDVEVYYEDDGWKVKTEGAKRASEVFDTKKEAVKRAKEIA
>gnl|CDD|443905 COG4877, COG4877, Uncharacterized conserved protein [Function unknown]
MAKKKQFLLRIDPALYEALERWAADELRSVNAQIEYLLREALRKAGRLPKKKRTEPRRGRPP
>gnl|CDD|443906 COG4878, COG4878, Uncharacterized conserved protein, DUF2194 domain [Function unknown]
LGLVVLLLMLLFLQLLRANIRVHSFKLKEEIKFRNEESTATAKKALEPEKGLVLSDENSSGSSEIKKELE
QMLLKMKVKNHVEKVNSNEDDLIDYLSVVIVVLDLMGMLDKLGLLIKKFVNGGGLLIALLRSFPSPRNSN
LGIIGIDGSIESAGYNYTTLEGPGGEKDFMLGYKIVYSSIDLFLSSLAVVLEADATVEPLTWEYGTGLGK
VMYGNSGVTVVNTTRGLGKGSRGLLASAFSLLSFNAKYPVIDDAPFPIPDPPPPSPSGEYEYDIRDFDFS
VKVWWPDMLKLARKYGIRYTGVIIETYNDDTKPPFEDLIENDREPFLYFGRELLKNGGELGLHGYNHQSL
VLPDEDYDEEYGYKPWKDEEQMVESLEELIRFVKYLFPNYQISSYVPPSNVLSKEGRKALGKAFPELKTI
SSLYFGDYSKGEYIQEFEVAYDGIYELPRITSGYMESDEDQFSAYNALANHGVVSHFIHPDDVLDEDRSA
GKGWEQLKKELDDMLSWIYETYPWLRALTASEAAKKVKSYSELEVSVKYSKDRITIYGSNFLDPSYLIVR
VNKGETGSVEGGEVTKLTEGLYLVEATKAKVTIILKEGGL
>gnl|CDD|443907 COG4879, COG4879, Uncharacterized protein, contains DUF2192 domain [Function unknown]
MEKVKELYRKRISVAVDLWSKILREEVLTREELVELLKEVYEKKGIEPIRGKAPEDIYDKELATLYVVGK
YGLGLDEEYPEVFDKLFYIEEKYEEAIEIILEGNPEEAREKLSGEIGGSIDENTVARVLRLVFTKVVLGF
MDEEELIKLLRKLSSAFPELEHTVKSYARFYIAFKIAEGIAEGEIRNRIEKEAFKQALAIRIGIEKPLPS
DEYIALIAKEVFNVPKKRLNRILSLEEEKKKSSVIPKA
>gnl|CDD|443908 COG4880, COG4880, Secreted protein containing C-terminal beta-propeller domain distantly related to WD-40 repeats [General function prediction only]
MKKKLALLAALLVAALLPVASEAELPTFDSYEELRSYLKAAAEASRSFAATAAPATASAAAAAAAASGAA
GRDYSTTNVQVEGVDEPDIVKTDGKYIYVVSGGKLRIVDAYPAEELKVVSTIKLDEGYPQELYLDGDRLV
VIGSSYSVAYPEPGGEASTTKILVYDVSDPANPKLLRELELDGSYVDARLIGDTLYLVTNSYPNYPFPQE
ATIDDWLPSYRDTAGGEGRVIPCDDIYYPPGPSGPNYTTVASIDLEKSGEAADTVSLLGSGSTVYMSEEN
LYLAYTRYPDEPELLLEEREAQPEEEKTEIYKFDIDGGRLEYVASGEVPGRLLNQFSMDEYDGYLRVATT
SGNWRDEPESENNLYVLDENLKIVGSLEGLAPGERIYSVRFMGDRAYVVTFRQTDPLFVIDLSDPAKPKV
LGELKIPGYSDYLHPYDENHLIGIGKETDENGGRTQGVKLSLFDVSDPANPKELDKYVIGDRGTWSEALY
DHKAFLFDPEKGLLAFPVTVYEIKPDNSGEFVFQGAYVFRVDGESGLTLVGKVTHLTSEYYDGNVQRSLY
IGDVLYTVSDSGIKVYDLNTLEELATLPLG
>gnl|CDD|443909 COG4881, COG4881, Predicted membrane anchor for polysulfide/nitrite-type reductase, PsrC/NrfD syperfamily [Inorganic ion transport and metabolism]
MVHGEAWTVVEGFIYPNELEIYWSVLIVVYPYMTGLVAGAFILSSLYYVFGVKRLKPTARLSLLFALAFL
LCAPLPLMLHLGQPERAFEIMLTPHFTSAMAAFGIVYAWYLVVLLLELWFVYRADIVEKAKALKGLRKLI
YRILTLGAWDISEEALKRDEKVVKILAIIGIPVAALLHGYVGFIFGSVKANALWSTPLMPIIFLFSAVVS
GIALVILAYIASMEIRGRSIDKGCVDTLAKYLLYFLILALTLELLDLIHRGYTAEESWDILRGLIYGKLF
VSFFVIQYGIGALVPLVLLLIPRLTVRRHMAAVASLLTLIGVFAMRWNVVIGGQLFSKTFAGFMHYHMPL
FGKEGLSGALAVMALPFIVFTVLSKIFPPWEEEEAH
>gnl|CDD|443910 COG4882, COG4882, Predicted aminopeptidase, Iap family [General function prediction only]
MSILNLYEVLKRLSGYGEIIAGSREERKIVEEIRSFLEEPLDWVRLIPVPVLTWRDEESSIECGDEILEA
LALPYSLGGDVEGKLVDIEGLPDHINKDVEGNIVVARFPEDPDDIKYVYIKAAERGALAVIFYDKDGRRR
RIVVTDDPDYSLSPGSPPPIPVASIPKEDGRKIVKRLGGRVRLVVDADIKVSTGYNVIAIINGSGEREVI
ITAHHDHWLSGATDNLLGVALLLELARKLRGERNKYNLRLISFTAEEGGSPGLPSWYWAWGSRSYLENLR
NRGLLDEVELNINFDVIGRRSLKLYASPSLREVLRKLLKNSWVVEPPEPYFDSYSFTKLGIPSLTIHTLD
DYLEIYHTDLDTPINVDSNTISTAVELANRLVNTVNNLWLYVSLDNYDLEFKTIVAKARIAESLEIIRER
LRIYTKTFYDCLLRRINAHATEEAGLLLPYVLAEEMNLRIGREEIFYKLMLNGKRSMKTP
>gnl|CDD|443911 COG4883, COG4883, Uncharacterized conserved protein, DUF2193 domain [Function unknown]
MSELYEKMVDEAMAAQRADVEVIKKKRGGKFKIDDAKPYVDAVNKMKAIGGQSKAVIDLHVDSVNAHYEI
LKGLTKTIRPEDDPFVEHYQTPPILEILYEEDPAFRKSVEKFIEAIGKSEALIGKESARRYGGFYGPTCV
VDFALIPGSTSNVVNRILKTTDIPVAHKQAILAAKSWGMNTSYGIGDVFAHAIEAGATLAEAVKKEIEML
QFIYDEPVEAQAKLMDDAGHSSFDVRKYMEEYKKRMEPAVKAAMDDGVHYGNIVTVPAYCVGDIAHHISQ
STFNMCKDDVVMAVIEAVTEVMESTLRKALPKFKSEYDVLSLATGSTAAAVEYILELDGFNAPMVVDLLT
KRFHNYVQLYPTRGAAAELHNCDFMDMIYRGWKILDKARRGKNGSGGPLVPKVGGFPVDLSPIHKNEVLM
NPQRYAYPACAITVRFSALMRLADYPCLLTSEPVTATMMTNIIALHKETPAAPARVCKDCASAALIDFRH
QYCQWKEAV
>gnl|CDD|443912 COG4884, YfeS, Uncharacterized conserved protein YfeS, contains WGR domain [Function unknown]
MTLYFDDEEYGLNRETSHPRFVELFTEDFYYDCGDEFSPFGSDEGADALYELEDWRDEKPDASTFEFLKW
LLEEWELGYLPDDGWIKDDLADLDQLGEEDEYYLLTSDNAIIATAFGQLKITGKIDPKLKKVALLALKRQ
ILLAELARNEYGDEDSARLDKMKRDLESFEND
>gnl|CDD|443913 COG4885, COG4885, Uncharacterized conserved protein [Function unknown]
MDRETLLAGGAVGVVVVALVAAAVVPGALADPEDDPVRPGHVDITETTISADEVTGETVDLNVTTRLEHR
GGPTENVTVLVRAVDAESGLLETTTTTDVGTVEGGGEVSVTTNLTVPREGGYRIETVVYEDGQRVDSGRK
TVRGLEALTPDYADSGVEFTESAALPPIDFSVKSVDDNRATLDVDAYLTNEGDAPSEDLRVLVKARQADS
NLVADRTTVPVGSIRPGRTVTVSATLTVPDNYNYYVDAVLWRDGVIVDTARSAANLDPTEVIDVNETVEE
VEIDTSDFEREDGEEADEETPEEEETTEEETPGFGPLVALVALLAAALLARRRSR
>gnl|CDD|443914 COG4886, LRR, Leucine-rich repeat (LRR) protein [Transcription]
LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLS
LLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKE
LDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEEL
DLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLS
NNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALL
TLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAVNTE
>gnl|CDD|443915 COG4887, COG4887, Uncharacterized metal-binding protein MJ0455, DUF1847 family [Function unknown]
KMEMSCADCGVKNCYKGGGKFPKFCPTTSDEEELEESLELYKDEENRKIARAAAEVEGEYYGKLTRVEEI
IEFAKRMGYKKIGIAFCIGLAEEARILAKILEKNGFEVYSVCCKVGGIDKDELGIPEEKIKPGTFEAMCN
PILQAKLLNEAGTDLNIIVGLCVGHDSLFIKYSEAPVTTLVVKDRVLAHNPLAALYSSDSYYRRLLGPKK
K
>gnl|CDD|443916 COG4888, Elf1, Transcription elongation factor Elf1, contains Zn-ribbon domain [Transcription]
MGRRRKKRKKLVRPKRKIPKVFQCPRCGAVTLSVKFKKKDSEGEKKAIIKCGNCGLYAEFEVPPIFDPVD
VYNKFIDLYLEGKIEVEERKEEEEEGESEEEDEGEEEEE
>gnl|CDD|443917 COG4889, COG4889, Predicted helicase [General function prediction only]
MMTTLDDLLDQLRNAARSEREKGTYFERLMRAYLRNDPTYADLYSDVWLWSDWPELYGRSKKDTGIDLVA
RDRDTGELWAIQCKFYDPDYTIQKADIDSFFTASGKKYFSRRLIVSTTDWWSNNAEAALAQQQIPVNRIG
LSDLEESPIDWSQFQWEPPEEVVLKAKKTLRPHQQEAIEAVLAGFKTHDRGKLIMACGTGKTFTSLRIAE
ELAGKGGRVLFLVPSISLLSQTLREWTAESEVPLRSFAVCSDSKVGKRRKKDDEDTSAHDLAYPATTDAE
KLAAAAQKRHDADRMTVVFSTYQSIDVVADAQKLGLPEFDLIICDEAHRTTGATLAGEDESAFVRVHDND
YIKAKKRLYMTATPRIYGDDAKKKAKEASAVLASMDDEALFGPEFHRLGFGEAVERGLLTDYKVIVLAVD
ESHVSRRLQQLLADNGNELKLDDAAKIVGCWNGLAKRGGEEDGTDDPAPMKRAVAFCQTIKESKRIAEHF
VSVVNIYLMFQDDEAEEDAPSLRCEAEHVDGTMNALERNEKLDWLKAETPENTCRILSNARCLSEGVDVP
ALDAVLFLTPRKSQVDVVQSVGRVMRKAPGKKYGYIILPVVIPAGVEPEEALDDNETYKVVWQVLNALRS
HDDRFDAMINKIELNGPDPDKIEVIGITDDIERDPSKTTGEQKKADPEQQELEFELGEIERAIYAKIVKK
VGNRRYWEDWAKDVAKIAQRHITRIKAILENPDQPAREAFDRFLKGLRDNLNDSITEDEAIEMLAQHLIT
KPVFDALFAGYSFAAHNPVSQAMQRMLDVLDEHGLEKETETLEKFYESVRMRAEGIDNAEGRQKIIVELY
DKFFKTAFPKTTERLGIVYTPVEVVDFILHSVDDVLRKEFGQSLADEGVHILDPFTGTGTFIVRLLQSGL
IPPEDLPRKYANELHANEIVLLAYYIAAINIEATYHELMGGDYVPFEGIVLTDTFQMYEDEDDLDDEVFP
DNSERRKRQKKLPIRVIVGNPPYSVGQKSANDNNANLKYPTLDARIRSTYAARSTATNKNSLYDSYIRAI
RWASDRIGDRGVIAFVTNAGWIDGNAADGMRKCLAEEFSSIYVFNLRGNQRTSGELSRKEGGKIFGSGSR
APIAITILVKNPDHSGPGRIHYHDIGDYLSREEKLAKIAEFGSIAGITWQRIIPNEHGDWLNQRDDDFDS
FIPLGDKKKKSPPSLFENYSRGVKTNRDAWVYNFSKEKLAENMQRMIEFYNSELDRYQAAVKQIDVDDFI
DNDPTKISWSRSLKQDLERGKKLEFDPDAIVTSLYRPFTKQWLYFDRRLNDMVYQMPKIFPTPTHENLVI
CVTGPGSGKGFSALITDVLPDLHLLIGGGQCFPLYLYEKVESDGGLLSAEDGSADRDDAITDEVLDAFAA
AYGDYFISKGDIFYYTYYYLDLLLYSEEYRYYAAKELPKKPLRRFAPAFDAAARAPAELAILRFAAETLA
LEELIDLDLAEVPGEIGDNEEEVRVKKMKKGKETKKKDKKDIIYNTIITITKIPLDAYGYVVNAKEALDW
PYERYEVKVDGISGIANDAIDDVNDPNDDPL
>gnl|CDD|443918 COG4890, COG4890, Predicted outer membrane lipoprotein [Function unknown]
MWYFAWILGLLLACAFAIINAMWLEHKEDRAEEDDAEP
>gnl|CDD|443919 COG4891, COG4891, Uncharacterized conserved protein [Function unknown]
TEIEIDAPPERVWQVLTDFPSYPEWNPFIRSIEGELRVGARLTLRLRPPGGRPMTFRPRVTEVEPNRELR
WRGKLLLPGLFDGEHYFELEPLGDGRTRFIHRETFSGLLVPLFLKSLREDTRRGFEAMNQALKERAEA
>gnl|CDD|443920 COG4892, COG4892, Predicted heme/steroid binding protein [General function prediction only]
MKEFTLEELAKYNGKDGNPAYVAVNGKVYDVTNSRLWKNGTHYGHWAGQDLTDELKDAPHGESVLEKFPV
VGKLV
>gnl|CDD|443921 COG4893, COG4893, Uncharacterized conserved protein, DUF2195 domain [Function unknown]
MSSLKYPLLLMSLVAGSAAAADAGRINIENKLSACVDITPGARSTADNMVILNTDVQLRKSIGECGCMSA
LANYTSSVEFDGSELVLQEGLIGLNKSKYKTLPLATEPKLVGDRKVVLRLGCAPPD
>gnl|CDD|443922 COG4894, YxjI, Putative phospholipid scramblase YxjI, Tubby2 superfamily [Lipid transport and metabolism]
MRTLYIKQKIFSLGDDFTIYDENGQPVYLVKGKFFSLGDTLSIYDADGNELATIKQKLFSLLPTFEIYDD
GEPVATIKKKFTFFKDRFTIEADGLDLEIEGDFWDHDFEITRGGKVVASVSKKWFSWRDTYELDIDDEED
RPLVIALAIAIDAVLHKERRAAS
>gnl|CDD|443923 COG4895, YwbE, Uncharacterized conserved protein YwbE, DUF2196 family [Function unknown]
MDGTNRKNIKPGLTVEIVLKKDQRTGKLTEGIVKDILTNSPTHPHGIKVRLEDGQVGRVKEIVE
>gnl|CDD|443924 COG4896, YlaI, Uncharacterized conserved protein YlaI, DUF2197 family [Function unknown]
MRVKCVLCDKIEEIDDDSLLAKRLRNRPIHTYMCPECHERIAEKTKERLATGKFRFYRSKKKKDDE
>gnl|CDD|443925 COG4897, CsbA, General stress protein CsbA (function unknown) [Function unknown]
MITWYVLALFLPALLVILFTRVTYNHYVGLLLTVALIGASVYKGYTHSEWIIILDAASLTAGFLYATRMN
KDKKEDE
>gnl|CDD|443926 COG4898, COG4898, Uncharacterized conserved protein [Function unknown]
NHRIFTMSFASVYPHYVAKAEKKGRTKEEVDQVIEWLTGYDQAGLQAQIDKKTTFETFFAQAPALNPNAS
LITGVICGVRVEEIEDPLMQKIRYLDKLVDELAKGKKMEKILRSS
>gnl|CDD|443927 COG4899, COG4899, Uncharacterized conserved protein, DUF2199 domain [Function unknown]
MMLDSSYQCSCCGETHEGLPALGFDAPDYYYELPEDERESRAELTSDLCVIDGEHFFIRGVLEIPIIGSD
EPFIWGVWVSLSEENFDRYLDLFDDPEENEGPYFGWLSNTLPGYPDTLSLKTMVHTRPVGQRPEIELEPT
DHPLAVEQRNGITLERALEIAAALLHDIR
>gnl|CDD|443928 COG4900, COG4900, Predicted metallopeptidase [General function prediction only]
MMKYERAEDVEELAKKIIESLGLDYIDLERVYVVRSRGSKSRAIARIWGLPKIWQYALGLEPLYVIEVIS
EKFDRLSCEEKIKVLIHELLHIPKTFSGGLRPHGKYVNFREVRKLYKLFKEEKC
>gnl|CDD|443929 COG4901, RPS25, Ribosomal protein S25e [Translation, ribosomal structure and biogenesis]. Ribosomal protein S25e is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MGGKKKPPLSQLEKRQKKEAEQQQKKPKKKEKKKEEEAKAKTITVTEELLKRVEKEIKKEKYVTPYTLAQ
KYNVKISVAKKILRELEKRGLLKLVSKNRRTPVYVPAS
>gnl|CDD|443930 COG4902, MJ0754, Ferritin-like protein MJ0754, DUF2202 family [General function prediction only]
MKKLSLLLSLLLLSLFALVGCAGASSAAEAAGAASPLASLSATEEADLLYMREEEKLARDVYLALYEKWG
LPVFSNIAKSEQTHMDAVKTLLDKYGLPDPVSDEVGVFTNPELQELYNQLLAQGSASLQEALKVGALIEE
LDIADLEKALAQTDNEDIITVYENLLRGSENHLRAFVRQLERIGVTYTPQYLSQEEFNAIIN
>gnl|CDD|443931 COG4903, ComK, Competence transcription factor ComK [Transcription]
MNLEYLESYIINESTMALLPYFEDGKYGTRVIEKDGEYYVPQKPLKIIDRSCKYYGSSYEGRKEAAKHIL
GITHKPPIVIDPLLGIYFFPTHSPRSPECIWISLSHIDRIEEAKDGKTIITFKNGKSIELPISYSSFENQ
YQRTAQLRYRLNKRIRQLQKKLESSLELPKR
>gnl|CDD|443932 COG4904, COG4904, Uncharacterized conserved protein [Function unknown]
MDIGRAKVRATFYLIFYHLFLLEAIPPSAREIIEKLGEIDFNLRSVDVRELRGSVIRKDLDQATREVYEK
VVKDFYENYGFQAEELHPDHLAVMLAFMSKLLREEISAALQGDLEELYKIRAAQHRFLNAHLIPTLKNLP
SAPSLNFVRDFIAEDAKYTNLLLRSSLVGEKNEAADNN
>gnl|CDD|443933 COG4905, COG4905, Uncharacterized membrane protein [Function unknown]
FLYFFIYSFLGWIWETIYCSIKEGKFVNRGFLNGPFCPIYGFGAVLVILLLSPFKDNLLLLFLVGAILTT
VLEYITGWLLEKLFHAKWWDYSNMPFNINGRICLPFSLFWGILGVLLVKVIHPLVLKLISRIPPKLGIIL
ALILLVIFIVDLILTVLALLRLNKRLAGLEKIEELREKI
>gnl|CDD|443934 COG4906, COG4906, Uncharacterized membrane protein [Function unknown]
MKFLNPFKINDWKIRKFILYILLLQVALWLSVILDVLGVNIPILRQVLGFIFLTFVPGYLILRILRLHKL
GFIETLLYAIGLSLVFIMFTGFLINMLYPLIGIDKPISEIPLLLTLNAVILVLMIIAYFRDRDFNNSVTL
DTKDILSPMLLFLLLLPFFAIFGTYLMNYYHNNILLIILLLLIALVPLLVAFKKFIPKRLYPLAIFSIAL
ALLLHNSLISNYIWGWDIHQEYYFSNLVLEAGAWNPSIPNNYNAMLSVVILPPIYSVISGLDPVWVFKII
YPFIFSLVPLGLYYIFKKQTNKKIAFLAVFLFIFQFSFYTEMLGLARQEIAELFLVLIIMVMLTNDLRLT
QKKILLVVFMFGLIVSHYGTAYIFIFLLAVAYLLMRLRNLLKKEIDTPFRLTFDYILLFFVLAVGWYLFI
SGGSAFESITGVGNHIISSIFYDFFNPEATSGLAVLTIESVSILHSISKLIHLLLQGFIGIGLLALILKR
EYRKEEISTEYLSFSIIALVLLIASIVLPFFSSALNTDRLYQITLIFLAPFFIIGYIALIGLIYRILRIR
WTTNSDKKSWRILSVFLAVFLLFNTGVIYEIAYDSPSSIALNPNGDEPFFTDSEVAGAEWLSDNRNGNLP
IYGDTYRSSLLFGFIPENYSDANTSQISVNTTVQGSYIYLGSYNVVKGLVYIPDVVAGDTKWYNYTSANR
YLKSKNKIYDNGGSQVYLY
>gnl|CDD|443935 COG4907, COG4907, Uncharacterized membrane protein [Function unknown]
MKKKRKSLIILLIALVLLFGSLLPPAAAAGDYSIESYDVDAQVQEDGSAHVVETITYDFDGSFRGVYRDI
PLPGGGSIENVQVEDVNGKISQNNSGAPGTYQITDTGGRYEVKVYLPPAEDETVTFVYSYTVKNAVKVYN
DTAELNWKLVGDDWDVPLKNVTITITLPPVNGDEVRAWGHPPLLGQIAFESGNTVVLTVGNVPAGEFVEV
RVLFPPEVLPGNTGFAHIDQNVLEEILKEEQAYADKANARARVLFGLLAVLVILVLLLPLLIYFKYGREP
KPTYPAIYLRELPTDDSPAVVNALFNGDIGKPDADGFTATILDLARRGYITIEEVKEKKKEKKDYLITIL
KDDGSELDDYEKDVLDFLFDYSGDDGIVDLSEIKKYLKKAARRFYKAFERWQKEVKNEVNKRGYFDDKGN
KKLKLFGLLAVILGIIIFVLLILLGANPALLLSLVLLVISGIVLALPSTLFGRWTPEGYEEYLKWKAFKK
FLSDFSLLKEYPPESIILWEEYLVYATALGVADKVLKQLKMLFPEELLDPSYLSYGYYYYGYGGISGFNS
SFSSASSSATASSPSSSSSGGGGGFSGGGGGGFGGGGGGGR
>gnl|CDD|443936 COG4908, COG4908, Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only]
LSPAQKRFLFLEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADL
PLEVVDLSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGIL
LRELAALYAALLEGEPPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPA
VQTFRGATLSFTLPAELTEALKALAKAHGATVN
>gnl|CDD|443937 COG4909, PduC, Propanediol dehydratase, large subunit [Secondary metabolites biosynthesis, transport and catabolism]
MRSKRFEVLDARPVNQDGFVKEWPEVGLIAMDSPNDPKPSIKIENGKVVEMDGKKREDFDMIDQFIADYA
IDLEVAEEAMAMDSLELARMLVDINVPREEIVRLTTGLTPAKLAEVVSHLNVVEMMMAMQKMRARRTPSN
QAHVTNVKDNPVQIAADAAEAALRGFDEQETTVGVARYAPFNALALLVGSQVGRPGVLTQCSVEEATELE
LGMRGFTSYAETVSVYGTEQVFVDGDDTPWSKAFLASAYASRGLKMRFTSGTGSEVQMGYAEGKSMLYLE
ARCIYITKGAGVQGLQNGSISCIGVPGAVPGGIRAVLAENLIAMMLDLECASGNDQTFSHSDIRRTARTL
PQLLPGTDFICSGYSAVPNYDNMFAGSNFDAEDFDDYLVLQRDLKVDGGLRPVDEEEVIAVRNKAARALQ
AVFEELGLPPITDEEVEAATYAHGSKDMPDRNVVEDLKAAEEIMERGITGLDIVKALAKGGFTDVAENIL
NMLKQRVSGDYLQTSAIFDEDFNVISAVNDPNDYAGPGTGYRLSEERWEEIKNIRQAIDPEDIL
>gnl|CDD|443938 COG4910, PduE, Propanediol dehydratase, small subunit [Secondary metabolites biosynthesis, transport and catabolism]
MQEELIEQIVREVLASMNSGSSSTAASASSGKRLTAADYPLAEKRPELVKTPTGKSLDDITLDNVLSGEV
TPEDLRITPETLELQAQIAESVGRPALARNLRRAAELTAVPDDRILEIYNALRPYRSTKQELLAIADELE
TKYGAKINAAFVREAAEVYEKRGRLKK
>gnl|CDD|443939 COG4911, COG4911, Uncharacterized conserved protein, DUF2203 domain [Function unknown]
MMMRYFTLEEANALLPLLRPLLAELRALRRELAELYEELEELEASLAASEEVAGLEAELKALEARLRELI
EELEELGVELKDLDPGLVDFPSLLDGREVLLCWKEGEPEIEFWHELDEGFAGRKPLPEA
>gnl|CDD|443940 COG4912, AlkD, 3-methyladenine DNA glycosylase AlkD [Replication, recombination and repair]
ESTLEEIRAELEALADPERAAFMARYGKEGDPFLGVRVPDLRKLAKRIKKELDHELAEELWASGYHEARL
LALLILDPKKKRDEETLELLEAWVPTIDNWDLVDSLAPKVVGKLLLDPEALELLLEWAKSDNEWVRRAAI
VLLLAFARKGDDTDFELLLEIIERLLHDEEDFVQKAIGWALREIGKRDPELVEAFLEKHDARLPRLTLRY
AIEKLP
>gnl|CDD|443941 COG4913, COG4913, Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]
FRLQRLQLINWGTFDGVHTIDFDGRGTLLTGDNGSGKSTLLDAIQTLLVPAKRPRFNKAANDAGKSDRTL
LSYVRGKYGSERDEAGTRPVYLRPGDTWSAIAATFANDGSGQTVTLAQVFWLKGDASSLGDVKRFFVIAD
GPLDLEDFEEFAHGFDIRALKARLKKQGVEFFDSFSAYLARLRRRLGIGSEKALRLLHKTQSFKPIGDLD
DFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAA
LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERL
ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE
LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGELIEVRPEEERWRGAIERVLGGFALT
LLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGRRFD
YVCVDSPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAE
ERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAE
LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN
LEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYEERFKELL
NENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPFGPGRYLRLEARPRPDPEVREFRQELRAVTSGA
SLFDEELSEARFAALKRLIERLRSEEEESDRRWRARVLDVRNHLEFDAEEIDREDGEEVETYSSSGGKSG
GEKQKLAYFILAAALAYQLGLEGRGRPSFRTVVLDEAFSKMDEEFARRALRLFKELGLQLLIATPLDKIQ
AIEPYVGSVLVVHKDDGRRSRVRELTIEELREERAQARA
>gnl|CDD|443942 COG4914, COG4914, Predicted nucleotidyltransferase [General function prediction only]
MMVSLKALAEVLRKLQERGVDFVIIGSTVVDLALGRKGLESDVDLFVTNPSTLVEEEFYREIAEENGWDY
GQTPLGTPRIIVLVNGEEVQVDLYENILDFYVPPEILESAKRVKIGGVEFKSIRLEDYIVLKARAAREED
EEELKEIAELIKEGKLRIDKRYIKEHIELFPEEAESIKRRLRELGIYI
>gnl|CDD|443943 COG4915, XpaC, 5-bromo-4-chloroindolyl phosphatase XpaC [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]
MKKIISFILRSLLSIPLAVITGLVLFFGFGISFLASILLGAGGGILSYLPSKGLQKRKFLKKIGLTKSEY
KYIRKQLEEARKKIRRLEKALKRIRSLELFKQLNDIQKIARRIFRIVEKDPRRFYQAERFFYYYLDSAVE
LTEKYAELSNQPIKTKEIRQALEETRETLDELEEAFEEDLKKLLEDDLLDLDVEIEVLKQSLKREGLT
>gnl|CDD|443944 COG4916, COG4916, Uncharacterized conserved protein [Function unknown]
YDVALSFAGEDREFVERVAEALKARGIKVFYDENEEAELWGKDLDEYLQDIYRSESRFVVVFLSKDYVEK
KWTGLERRAALARAMQRKKEYILPIRLDDTEIPGILATIGYIDLRNRTPEEIADLILEKLAKGRPKPSRA
LSLAPTETVGSPARPNDAPGVFSTASAKTCVSGNLTGLLAVLDLEEVQGFLIGVRGDTEISRGTGQSAVD
SVVAEVGRAGGGLEQLLAAPEAVGSV
>gnl|CDD|443945 COG4917, EutP, Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism]
MKRIMLIGRSGAGKTTLTQALNGEELEYRKTQAVEYYDNIIDTPGEYIENPRFYKALIATAQDADVIVLV
QDATEPRSVFPPGFAKAFNKPVIGVITKIDLPEADVERARKWLKSAGVEPIFIVSSVTGEGIEELKEYLE
ELGDE
>gnl|CDD|443946 COG4918, YqkB, Predicted Fe-S cluster biosynthesis protein YqkB [General function prediction only]
MKITFTEAAKEKLQAILGSDKKYLKLFYDTEGCGCAVNGVPTLRLVDEPDEYDTAIESNLGPVYIDRSQE
VFFDDEMTIDFNPKGNTFRLKSPGGILNPNLSVVDVRKKNLV
>gnl|CDD|443947 COG4919, RPS30, Ribosomal protein S30 [Translation, ribosomal structure and biogenesis]. Ribosomal protein S30 is part of the Pathway/BioSystem: Archaeal ribosomal proteins
MPTHGSLTKAGKVRSQTPKIPAKPRKNPPPRVRNRREYRKRFVKARQNKAGQ
>gnl|CDD|443948 COG4920, COG4920, Uncharacterized membrane protein [Function unknown]
MSSYNPYNWKMLLISQAYIIIFAIVLAFFPQYYFLVFILYFIIIFGIMSILGYRSNPRDRKEAEEILKGR
TLYEEKDANELIMKDEELVKELQEQAKATMKTFLIMLIYLIIFFLLYRYVPDLIKFVSSALGLNEFLARF
IVYLIYFEALFLISMFVRRRTLRPQMPKNMPMAPTSYKVTEKGIVIKGLMGIKAIPFPLEGYEIVLNEER
KFVEIVSSKQKTPYRIRLYTKDPRKLYEIIERYGKIELKRQQ
>gnl|CDD|443949 COG4921, COG4921, Uncharacterized conserved protein, DUF2209 domain [Function unknown]
MDIVAVDISGRHAEKGGYLMVCAAVSAEVSADHIEKVHQVNVKPFRSREAPDLRDVVKIIEETVSGLKFE
GTIVAEKGDFYNEPEWRVSSMFGREFKYPESLSERRAIEIAHHISLSARKLLLKELDIS
>gnl|CDD|443950 COG4922, COG4922, Predicted SnoaL-like aldol condensation-catalyzing enzyme [General function prediction only]
ATDLDKTEANKALVLDFYDTVFNGGDAEAAERYVADDYIQHNPGVADGREGLIAALEALAKEYPDKYVEI
HRVIAEGDFVVVHSHGTFDPGGKGTAVVDIFRVENGKIVEHWDVIQPIPEKSANGNGMF
>gnl|CDD|443951 COG4923, COG4923, Predicted nuclease (RNAse H fold) [General function prediction only]
MSDDSRVVGVDGCRGGWVAVLLDGDGRPRALVFPDIADLWAAYEDAAVIAVDIPIGLPEVGDGGRACDRL
ARKLLGPRASSVFPVPVRAAVYAADYAEACRINRETTGRGLSKQAFNLFPKIREVDALLRENPEARERVF
ESHPEVAFAALNGGAPLSHPKKTAAGLAERLALLAAVGRDAEPLVQRALEATPPRGVARDDVLDALALAL
TARRIAGGEARSLPDPPERDARGLPMAIWY
>gnl|CDD|443952 COG4924, COG4924, Uncharacterized conserved protein [Function unknown]
MKTPADLRAQLRRRWDRGSLLRAWLLGEAAWPLRLPLKPPTAKEALEDFDAVRAWIAAWRAWSGGRVEWR
ERRWRVLGRQRLPVRLWLDSPDDAAALIGVAREWRRFRARVAQLRARWPALLPWLRRPLRALEELSDDDW
ERLLAVLDWLRAHPRSGLYLRQLPIPGVDTKFIERHRGLLAALLDALLGGAAGAQGFARRLGLRDKPSRV
RVRPLDPALRPLGGLRDLTLPLEELAALALPPSRVLIVENEQTFLALPDLPGTIAVFGAGYAVDWLARAP
WLADKRIHYWGDIDTHGFAILSRLRSYFPHVRSVLMDRETLLAHRDLWVEEPRPARGPLPLLTPEEAALY
DDLRANRWGGNLRLEQERIPWDYVEAALRAWLAG
>gnl|CDD|443953 COG4925, COG4925, Uncharacterized conserved protein [Function unknown]
MKASEQSTSMKIRITIGGQVFTATLADNPTARDFAALLPLTLTMEDYNGNEKIAYLPRKLPTNGAPRGGT
PQAGDLMYYAPWGNLVIFYKDFGYSYGLTRLGKIDDGLEALLGPGNVTVTIERAE
>gnl|CDD|443954 COG4926, PblB, Phage-related protein [Mobilome: prophages, transposons]
MIPVLYDKNETEFDTNGLGVLDNAYDAVVTEELNGEYTLEFEYPYDGEKAEHLENENIIKVDTPRGNQLF
RIYRVTKTMDGTITVYAEHIFYDLLDNFIEDTRVTNVTAQTALNDILDGTQYPHPFTGSSDITTTRSAYV
VKKNALEALLGDENSFASRWGGELRFDNYTVDLLKRRGRDRGVVIRYRKNLTGLERTVDTTEVVTRIYPY
GKDGITLPEYIDSPYIEDYPYPKIKVIDYVSKFDDEDFTTPEQLREAAKEELKNGVDKPRVSYKVDFADL
SQTEEYKHFKQLEAVRLGDTVTVYDEKLGIDLKARVVAYQYDVLAPEYTEIELGSFVPSLTDSLTSIDKL
LDQVEESSKNINQASDNATGLINSGNGKLVPEYPAEILIMDTENGETAKEVFRWNLNGLGISATYIITSD
GAIVADLIGKLSTDDIKN
>gnl|CDD|443955 COG4927, COG4927, Predicted choloylglycine hydrolase [General function prediction only]
MKKMRFLRLRGSHYEIGLQLGKLLKELIIAYLPRGKEKRPFLAEARAALRRYMPELWEELEGLADGLDVP
LEELLLLNGGYYLPLSGCSQFAVAPEGEPLLARNYDFHPDLYEGRLLLTVQPDGGYAFIGVTDGLIGRLD
GMNEKGLAVGLNFVGRKVAGPGFPIPLLIRYILETCSTVDEAIALLKEIPHASSYNLTLADASGNAAVVE
VSPRGVEVREPNGFLVCTNHFQSLEMAEENRN
>gnl|CDD|443956 COG4928, COG4928, Predicted P-loop ATPase, KAP-like [General function prediction only]
NETEEDLLGRKKYAESLANLIKSSDADEPLVIGLDGEWGSGKTSFLNLIEKELESNEKVIVVYFNAWLYD
GEEDLLAALLSEIAAELEKKKKKDKKAAKKLKKYAKRLSKLALKAGLLGGPAEAVAEALKALLKKEYKSK
KKSIEAFREELEELLKELKGKRLVVFIDDLDRCEPDEAIEVLELIKLFFDFPNVVFVLAFDREILEHALK
ERYGEDIDAREYLEKIIQVPFRLPPLSNELLILELDRLLELLLSALLEALLALLLLRALAESISSLRAEF
LLLLLLLKLELLLALLVLLLKLELLLENLLLAALLLLLDELELKKLLREDVASRASLYFINAELANLSLK
LLKISSELLTLELKLEEERELSAKYRLEKRLLIGLL
>gnl|CDD|443957 COG4929, COG4929, Uncharacterized membrane-anchored protein [Function unknown]
MKKKSPLWLLLLALLLQLALLNAMVAQKEYTLATGKTVLLETAPVDPRDLLRGDYVTLNYAISRLDLARL
PGWPDDAKLRRGDRVYVVLELDEDGVARPVRVSSDKPPLAANEVYLKGKVRYGWRVDYGLERYFFPEGQG
ERIEQARYQGPLVAEVRVDPDGNAVLVGLLDDDRKYLF
>gnl|CDD|443958 COG4930, COG4930, Predicted ATP-dependent Lon-type protease [Posttranslational modification, protein turnover, chaperones]
MDALDQKLNEHFPGKVVRKDLVKKIKGGANVPTYVLEYLLGQYCASDDEETIEEGLEKVKRILADNYVRP
DEAEKIKSKIREKGSYKIIDKVTVRLNEKKDRYEAELSNLGLKDVRIDDEYVKKNERLLTGGIWAIVTLE
YDPEEEKKGSPFIIESLKPIQLSNVDLDEYREGRKEFTTDEWIDLLLRSIGLEPEALSERQKLLLLLRLI
PFVERNYNLVELGPRGTGKSHVYKEISPYSILISGGQTTVAKLFVNMSSGQVGLVGLWDVVAFDEVAGIK
FKDKDGVQIMKDYMASGSFSRGKESINADASMVFVGNIDQSVETLLKTSHLFSPLPPEMDDTAFLDRIHA
YLPGWEIPKMRPEFFTNHYGFIVDYLAEILRELRKTSYSDAIDKYFRLGNNLSQRDTKAVRKTVSGLLKL
LFPDGEITKEDVEEYLEYALEGRRRVKEQLKRIGGMEFYDVNFSYIDKETGEEKFVSVPEQGGGKLIPEG
PLPPGQVYTVSPGQDGMPGLYRIETQVGPGSGKLILTGGSSPAAKESVKTAFNYLKANAKRLSGSRDPRE
HDFSIQLRDLNGSGMGSELGLAAFIALCSAALGKPVKGQLVVLGEMSIGGSIEPVDNLADKLQVALDSGA
KRVLIPISSARDLGTVPDDLFTKFQIIFYADPVDAVFKALGV
>gnl|CDD|443959 COG4932, ClfA, Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis]
SVGAKGAGTGVGTVIVEGAGSGSLVAVTTGAVLGLALGSTGGTAGSAAAINSAPATGTATGTSAGATAVI
VIAAGLTATPTETASGLGGDATVTTTANVAKVTNGAAANLTVNADGTASNAGTLAKGAETATGNLDGDAG
DVTVTAAATDGVNDVDGNGASVTDSVTLKKVDDGDTGKPLPGATFTLYDSDGTLVKTVTTDADGKYTFTD
LPPGTYTLTETKAPEGYVLDTKDPTGATITVTVNAGGTVTVTLKNTPKYTKGSVTVTKTDADTGEPLAGA
TFTLTDADGNTVVTTTVTVTDADGSYTFTDLPPGTYTVTETKAPAGYDLDGEAVKVTITAGQTTTVTVTN
GNNEVKTGSVTLTKVDADDGEAPLAGAEFTLTDADGTVVATITTDADGTASFKGLAPGTYTLTETKAPEG
YTLDSTPITVTVTDGGTGAIDTITNERKKGSVQVTKVDAPLAGATFTLTDADGTVVTLTTDADLAGATFE
ADGKVVTTTDASGKYTFKNLPPGTYTDAGGSATVITDDTDGTVGDEATGTDPEVTVTGKSTTTTPDVALL
TNLGTTEDALTSLAKTGDEVGKGLTLTTTTTVDTLDTNATEKTETVTVTAQLIGVKTTKLTDTTDPKGGT
VEEATTTGGTANTGKTGTDLTDDTTVTSTTNTATSVEDTTDVDNKDAFTGGTEPGGTIV
>gnl|CDD|443960 COG4933, COG4933, Predicted transcriptional regulator, contains an HTH and PUA-like domains [Transcription]
RKVLLSIKPEYAEKILSGEKKFELRKSIPKLDPGDTVVIYATSPVGAIVGEFEIGEVIKDSPETLWERTK
EESGISKEDFDEYFAGKEKAYAIEIGNPKLYKKPINLEELRENPGFTPPQSFRYLKEDEPLKLIRKL
>gnl|CDD|443961 COG4934, COG4934, Serine protease, subtilase family [Posttranslational modification, protein turnover, chaperones]
KRAGATDLGPLPPSQPVTVTVSLPLRNQAALEALLAAVSNPGSPNYHHFLTPAQFAARFGPTPADVAAVV
SYLKSQGLTVTAVSPNRLLIVASGTAAQVEKAFGTSLHRYTVGGRTFYANTGAPSLPAALAGVVSGVLGL
DNRPNATPRAAPSATSTAAAGGPSGYTPTDLASAYNLTPLSAGTTGTGQTIAIVDAGGDPYIPSDLATYD
SQFGLPPPTLTVVNVDGGYDPSGDPSGWAGETALDVEMAHAIAPGAKIVVYEAPNTDAGLLDAYAYAVND
NLADVISNSWGGPESSASPSSLAAYDQLFAQAAAQGITVFAASGDSGAYDGTGTGGLSVDFPASSPYVTA
VGGTTLSVDSNGRYSSETAWNDGSSYGGYGGSGGGVSTVFPKPSWQTGTGVPAGGGRGVPDVSADADPNT
GYLVYVTGSGWGVVGGTSAAAPLWAGLLALINQALGHRLGFINPLLYALANSAAYPSAFHDVTSGNNGSC
GGYGYTAGPGYDLVTGLGSPNGAALAAAL
>gnl|CDD|443962 COG4935, COG4935, Regulatory P domain of the subtilisin-like proprotein convertases and other proteases [Posttranslational modification, protein turnover, chaperones]
GAAGGAGSTTGLAAAVLAAAAGTGSAATAEGGAASTATSAAVAGASAAAAAATAVGAGASSLAASAAAAA
AAASGAAAGAVDAAPAAATVVGAALGVVAVAGAGLAATASGAAAGAVAAAANGNTGAGPGSGGTGGGSGG
AGAAAAAAALSAAGAAVGVAAVAGAAGGGGGVGVAAAVGVVLGAGLVADGGNGGGGAVAGGAAGGGGGGG
GGGGLGGAAGGGGAGLAAAGGGGGGAAAAAAAGVGGLGAAATAAAADGGGGGGAGAAGAGGSAGAAAGGA
GAGVVGAAAGGGDAALGGAVGAAGTGNAAAAAAASAGSGGGGGSAAAAGAAAAAAAAAAGAAAGVSGAAS
VVAGASGGGAGTAAAAGGGAAAAAAGGAAAAGAAAGAAAGAAAGAAAAGGVASAAGAVGAGTAAGASATA
AVSTGAASGSSTTSSTGTTATATGLGGGADAGSTSTGTGSAAGAAGGTTTATSGLASSTTAAAAAAAAGL
ATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATFSNTTDVAIPDNGPAGVTSTITVSGGGAVEDV
TVTVDITHTYRGDLVITLISPDGTTVVLKNRSGGSADNINATFDVANFSGESANGTWTLRVVDTAGGDTG
TLNSWSLTFTG
>gnl|CDD|443963 COG4936, PocR, Ligand-binding sensor domain [Signal transduction mechanisms]
LSDLIDLEELQKLLDSFSKATGLAAVIVDPEGNPLTKPSNFQDFCRLIRSTPEGRKRCRESDARGGLEAA
KTGKPYIYRCHAGLVDFAVPIIVEGEHLGNILGGQVLLEEPDEEEFRKIARELGFDEEELLEALEEVPVV
SEEKVQAAAELLFVIANYISELGYSNLEEELELLLQQSEKEEEEEERKELEALSSELSLLLLELLLVLVS
LLLILLALKILLLLLLLLLLIEFLLVVEEKELLALLLLLELLALEAAGIGEKLYFSLVLILKRKLIVVVI
RERDELLEIKVELLIKEFEELLALLARLAIKEEIELAAIEIKILNELSLEELLLALAGLLSDSSLSALEL
LRIKELGLVRRLLERVELSLKLELELGLLLIIVGSLGGSGSSKGFKIVKIEEGSVLVEVLKEEII
>gnl|CDD|443964 COG4937, FDXACB, Ferredoxin-fold anticodon binding domain [Translation, ribosomal structure and biogenesis]
EIIIMKIGIIGGTGEMGQWFAKFFKDFGFEVTIWGRGGKVEIAEKLGVGFANDNDAAIADADIIIVSVPI
VITETTIVEVAPKMPKGSLLMDLTSTKVKPVEAMEKYAPVDVEILGTHPMFGPTPPTLSGQIVILTPIEG
RCDKWFPKIRNLLEEEGARIIIITPEEHDRMMSVVQGLTHFAYISIGATIKRLDFDVKESRKFASPVYEL
MLDIIGRIIGQNPYLYASIQMENPEVKKVHETFIEECNELSNIVRKDDEEGFVEIMKEAAKHFGDTESAL
GRSDKAINALTQEFEKLKKSVGKEVGLKHIYSGKVHVGILKKVTPDFVILKENNKEIKLKISNIRLLSEK
ELREWKIKNLKLYSRDISVLFPKSADPEIILKLLKNIENVIDVEIIDTYEGEQIPEGFLSITFRISVFDK
EELKKLEEEVEKLLEGIGCKLRV
>gnl|CDD|443965 COG4938, COG4938, Predicted ATPase [General function prediction only]
IKSISIKNFGPFKEAELELKPLTLLIGPNGSGKSTLIQALLLLLQSNFIYLPAERSGPARLYPSLVRELS
DLGSRGEYTADFLAELENLEILDDKSKELLEQVEEWLEKIFPGKVEVDASSDLVRLVFRPSGNGKRIPLS
NVGSGVSELLPILLALLSAAKPGSLLIIEEPEAHLHPKAQSALAELLAELANSGVQVIIETHSDYILNGL
RNLIKEGKLLDPDDVAVYFFERDGGGSELRRIEIDENGIISDWPDGFFDEVSEDLAELFEALLEKED
>gnl|CDD|443966 COG4939, Tpp15, Membrane-anchored lipoprotein Tpp15, major membrane immunogen [Function unknown]
IAATAKLKDGTYKAEEDNFDEHGWKGTVTITVKDGKITEVNYDEINKDGKDKSEDEDYGKTMKGKAGQGP
KEAAPALAKYLVEKQDPEKVDVVSGATVSSKQFKELAEKALNAAK
>gnl|CDD|443967 COG4940, ComGF, Competence protein ComGF [Mobilome: prophages, transposons]
MQLNKLIFSAASINRKGFTLLEKLAALMIIAYILAVLELLLKLLLKLNQSLDAGEQIEWELFIEQLIFEL
LEAKLIEVRSNRLVLTDIKPPIVFHKYNSELRRQVNGKGHEPYLTGLKAAHYLATNWEFRIIVTFNNGLE
YERSIPIEDEYDL
>gnl|CDD|443968 COG4941, COG4941, Predicted RNA polymerase sigma factor, contains C-terminal TPR domain [Transcription]
MSDARRAIEALFREESGRLVAALARRFGDLDLAEDAVQDAFLAALEQWPRDGVPDNPAAWLYTVARRRAI
DRLRREARRRRKEAELAADLEAEAPAEDADDDDIPDDRLRLLFTCCHPALSPEAQVALTLRLVGGLTTAE
IARAFLVPEATMAQRIVRAKRKIREAGIPFEVPDAAELPERLDAVLAVIYLIFNEGYAASSGDDLVRADL
CDEAIRLARLLAELLPDEPEVHGLLALMLLHAARRPARTDADGELVLLEDQDRSRWDRALIAEGLALLER
ALAGGRPGPYQLQAAIAAVHARAPSAEDTDWPQILALYDALLRLAPSPVVALNRAVAVAMADGPEAGLAL
LDALAAEPRLAGYHLLHAVRADLLRRLGRRAEARAAYRRALALTRNEAERAFLRRRLAALAA
>gnl|CDD|443969 COG4942, EnvC, Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning]
MRKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR
IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY
LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE
LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPWPVSGRVVRRFGERDGGGGRNKGI
DIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSG
GQGGPTLYFELRKNGKPVDPLPWLAKR
>gnl|CDD|443970 COG4943, YjcC, Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms]
MRMRRRRLLSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNA
LPGDPCSPAHLAALRRLVFSSRYVRDIGYVRDGRLLCSSLGKLSKPVPLPPPDYVTADGYRLWLNVDNPL
DPGRPMLIVGRGNYVVVIDPAAFIDVLSPQPGISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWFIQ
GDRLYASACSPQYPICVVAAAPLAGLLALWRQLLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAI
KRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDL
LAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKARAVIAALREAGHRI
AIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADY
LRARGVQYGQGWLFAKPLPAEEFIAWLAAQRAPASAPA
>gnl|CDD|443971 COG4944, COG4944, Uncharacterized conserved protein [Function unknown]
MKTDDLIDALAADLRPVRRLRPPRRLALALLLGLALALALVLLWLGLRPDLAQAMATPRFWLKFAFTLLL
AVAAAAAALRLARPGRSPRRGLLLLALPALLLWALAAIELAVAPPAAWPALLLGETWLVCLFAIPLLSLP
PLAALLWALRRGAPTRPALAGAAAGLAAGALGAAAYALHCPEDSPPFVAVWYTLGIALVALLGALLGPRL
LRW
>gnl|CDD|443972 COG4945, DOMON, Carbohydrate-binding DOMON domain [Carbohydrate transport and metabolism, Signal transduction mechanisms]
MDGNVIGDKGLDGFSGLSADASALVAIVDDTSLRDRLGIDFGVSVAGLLALDGIQDTEASVLEGGEGDYI
AEEELIRDIASDAYVNGDNARRYLDIAAPGDPFALGLQLPRLGNLFLNSLLALREEPLAGGLLDSLEFWI
DEKAYLEAWGVLTLAWEGLRLVAAYINSELLALKYYAAEEEEFDDWDSGNAVDLDLLTAEGAFQVLGEAA
GSDLLALAADDDADGFADYLIVLKAGYAATEFYFLLALDDGDVDAPILAIEAVVASGLTEDDVIALYLGL
NPGIGVGLPAAHLAVAAELDGDYALSIKTRTGLGSYLYGAGASIGYQLGYAADSTVGSLESGATPSGEVV
GALSTPLPLGGLAFGEDDVAGGEDVGPLLGTVATSLSVFGALLVGIALIVRGEELGEVGPLYAAVVVVGS
IALLPTGAPLVIRFGLLLLLLATILLSVIPAAVAGTVILEITDPTGDDYGPGTYVYPTDPVFKPGLFDLT
RFKVEEDGDKYVFRFKFRDLTNPWGGPNGFSLQLIQIYIDTDGDGGSTRTFKPGANVAFAPDHPWDYAIK
IAGWGSSALVYADGEKVEELIVFEVKADPDGNTITVTVPKKLLGDPDIKGWKYYVLVGSQDGFGPDRIRP
VTAEAGEWRFGGGTDDAAGVAPRVIDLLAPEGEDQEEMLSSYDPSRGKPATLPPVPVPT
>gnl|CDD|443973 COG4946, COG4946, Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown]
MKKLLALLLALLAAAASAQQETGYLRYPAISGDTIVFVYAGDLWTVPADGGRARRLTSHPGYESFPRFSP
DGKWIAFTSDYDGNTDVYVMPAEGGEPKRLTYHPANDRVVGWTPDGKSVLFASNRGSPPSRSNQLYTVPV
DGGLPERLPLPPAGDGSFSPDGKKLAYTRIGREFRTWKRYRGGTAGDIWIYDLGTGEFTRLTDFGGNDRN
PMWIGDRIYFLSDRDGTFNLYSYDPDGKDLRQLTHFKDFDVRFPSTDGGRIVYEQGGDLYLLDLASGEPR
KLNITLAGDFPQRRPRWVDVSGYLTSFALSPDGKRVAFEARGEVFTVPAEKGPTRNLTNTPGVRERLPAW
SPDGKSIAYFSDASGEYELYIAPADGSGEPKQLTLGDLGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASG
KVRKVDTDGYGDGISDLAWSPDSKWLAYSKPGPNQLSQIFLYDVETGKTVQLTDGRYDDGSPAFSPDGKY
LYFLSSRDFNPTYGDLDFDLAFPRTTRIYAVPLRKDAPSPFAPESDEEAAKKEEDEKKKKKKKDDKKKKP
KPVKIDFDGIEDRIVALPVPAGNYSDLAAGKGGVLYLLEPVEGAPGGTLYRYDLEKRKTETLADGVSSYE
LSADGKKLLVRSGGRLRVVDADAKPKDGSGKVDDKRRVVVPPEEEEQQFEEEWRRRRRRFYYDNDHGGDD
DWAGVYYYYLLLLARRRRDLLDLLLDLLGELLLGHLGVLGGGGGGGDRPPGGGLGLGAALLGDGGGVRKI
IIIGEIEDPPAPPPLPPPGVVVGGGGIIIVIVGVGVGDDNDALLLLLLLAGKVTLLVLVLLTEGRGKVVV
VVVVVVEELLRLLRWVRRRRRRVRRRSGGGGGGVGVYGMGGGGGGGFRRRFFFYYDYKGVIVDDIRGGGG
GGGGLIIDLLLLLLLLRLRRRRGRRPPPPPPPPGPGPPPVLVLVASGGGGGSDGFFFFKGGLGGGLGTGG
GGGGGGGGGGGLDGGGGGGGGGPTGVFGGGGGGGGEEVGVPVPDDVVDVEEDVVDDDDDQQDEAAAAALL
LLELKPKKPPPPPPPPPPPPPP
>gnl|CDD|443974 COG4947, COG4947, Esterase/lipase superfamily enzyme [General function prediction only]
MHREYHRWYSPRLGRDMELLVYGHAGAPVLVFPTSGGRFYEYEDFGMIDALAPLIEAGRIQLYCVDSVDS
ESWYNKWAHPHDRARRHNQYERYIIEEVVPFIRADNGGNPPIIATGCSLGAYHAVNFALRHPDLFDGVIA
LSGVYDLRDFFDGYYDDDVYFNSPVDYLPNLSDPWYLDQLRQRDIILAVGQGAWEDPFLESNRRLSDILW
EKGIPHWLDVWGDDVAHDWPWWRKMLPYYLGRLF
>gnl|CDD|443975 COG4948, RspA, L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]. L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
MKITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGGTGAEAVAAALEEALAPLL
IGRDPLDIEALWQRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEE
MAEEAREAVARGFRALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGL
EWIEQPLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALA
EAHGVPVMPHCMLESGIGLAAALHLAAALPNFDIVELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVE
LDEDALARY
>gnl|CDD|443976 COG4949, COG4949, Uncharacterized membrane-anchored protein [Function unknown]
MTLALPLADHPLRAALLNELHARPFPPLEAPARVSHLAFLTDGDAAEADRAHLAALCRRFGVPPPAPGAR
HYSVDLGGFRLRWERHTEFSTYTFFRPGPADEPFDPPALELLPADWLAALPGELLVAVHLEVEPAEEDAP
EPEELSRWFEGNSLVGSRVADGAAVVATDFRIDPDGFSRFLVFDRGLSPRQAGRLVQRLLEIETYRMMAL
LGLPVARELSPELARIERELAELTARMADSSDLEDERELLDELTALAAELEALAARTSYRFGASRAYYEL
VRQRLEELREERIEGLQTLGEFMERRLAPAMRTCEAVERRQEDLSERVARASELLRTRVDVELEAQNQAL
LESMDRRARLQLRLQQTVEGLSVAAISYYAVGLVGYLLKGLKAAGLPISPELATALAVPVVVLAVWLGVR
RIRRRLHK
>gnl|CDD|443977 COG4950, YciW1, N-terminal domain of uncharacterized protein YciW (function unknown) [Function unknown]
MTTATSPDVIDTLAGIAPGSALAALRAQRAKAREATQASYDALFSPALPGGLSLAERLAVALFVARLHGA
QALAAHYAARLAPLPAPALAAAADPDAAAELDPRLAAALAHARLLTLRPREATPAALQALLDAGLSTPDI
VTLSQLIAFVSYQARVVAGLRALAGLPAAAAGAPPAA
>gnl|CDD|443978 COG4951, COG4951, Uncharacterized conserved protein [Function unknown]
MTDAKLQQLLARLAELEAENARLRNLLEAHGIPPDPPPATQPELVTSSSSPEEKIALFRSLFKGRTDVYA
KRWESKKTGKSGYSPACANEWRKGICNKPRIKCKDCKNRSYLPLTDSVIYDHLRGKDVIGIYPLLEDNTC
WFLAADFDKAGWQEDARAFVEVCREFGIPAALERSRSGNGAHVWIFFEEPVSARLARKLGTALLTEAMER
RPELSFSSYDRLFPNQDTLPKGGFGNLIALPLQKKARENGNSVFVDEDFEPYPDQWAFLSSIKKLSEQDL
ESLILKLEGGAELLDVRDDEDDSKPWERPRRTKLLKGDFPKTLTITLANMIYIPKSGLPQALLNRLKRLA
AFQNPEFYKAQAMRLSTFGKPRIISCAEETPGYLALPRGCDDDLILLLKHGKIEILDDDRRGGGKNIEVF
FFGLLRDQQQAAAAALLKHDGGVLAAATAFGKTVVAAIIIARKKVNTLILVHRRLLLQQWKRRLLFFLLI
NEEGPIGGGGGKKKGKKDIIITQQLSRSRSGLDIDDIIAYGQVIVDEDHHHSAAAFEAVEVRAKAAVVYG
LTATATRKRKNHDVILMFVGPGRHHARHKAQAQFEGPVRRVRIRSTKPPEPPIPEDDPRRTTVPRRRRLQ
AEAKLRIIAERDEVVNLLERRIILLEREEVALLLLRLLLVLLRIVLKLEKASGLLKRKLASLELAAGGVL
TTTGKVIGEGGDPLILLFLLLILATGFKGGLIQYRGRLHRLALAKVRVAYRDYVVHGLVLLRDKVLKRRY
GYKRYAYRKRGRLESMEMKKKLG
>gnl|CDD|443979 COG4952, COG4952, L-rhamnose isomerase [Cell wall/membrane/envelope biogenesis]
LLAAHQRDYEALGEQLARRGIDIEAIKAKLAAFQIEIPSWAYGNGGTRFGRFPGPGEPRNLFEKLEDAAQ
VHQLTGAAPSVSLHIPWDKVDDYAALKALAAELGLGFGAVNSNTFQDQSYKFGSLTHPDAAVRQQAVDHN
LECIEIGKALGSKDLTVWLADGSNYPGQDNFRRRFDRLLESLAEIYAALPDDWRLLLEYKPFEPAFYSTD
IPDWGTSYLLAQALGPKAQVLVDLGHHAPNTNIEQIVARLLREGKLGGFHFNDRKYGDDDLTVGSIDPYQ
LFLIFNELVDAEALDPTAFGVAYMIDQSHNVEDKIEALIQSVLNVQEAYAKALLVDRAALAAAQEANDVL
GAQEILMDAFRTDVRPLLAEAREEAGGAIDPIAAYRASGYREKIAAERGGGTQAGGGA
>gnl|CDD|443980 COG4953, PbpC, Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis]
MKRARLRRRRLLALLLALLLLALALWALDRLFPLPLLFAVPYSTVVLDRDGTLLRAFLAADGQWRLPVPL
DEVSPRYLQALLAYEDRRFYYHPGVNPLALLRAAWQNLRSGRIVSGGSTLTMQVARLLEPRPRTLSGKLR
QILRALQLERRYSKDEILELYLNLAPYGGNIEGVEAASLAYFGKPPSRLSLAEAALLAVLPQAPSRRRPD
RNPERARAARDRVLARLAEAGVIDAEEAALALLEPVPARRRPLPQLAPHLARRLLRQLPGGTRIRTTLDA
GLQRRLERLVRRYVRRLKQNGIHNAAVLVVDNRTGEVLAYVGSADFFDASRQGQVDMVRALRSPGSTLKP
FLYGLALDQGLIHPETLLADVPTSFGGYRPENFDGTFQGPVSAREALARSLNIPAVRLLEALGPARFYAR
LRRAGLRLLLPPAEHYGLSLILGGAEVTLEELVGLYAALARGGEARPLRLLAGEPASPGRRLLSPGAAWL
VRDILSDVPRPDGAFGWRALDSPPPIAWKTGTSYGFRDAWAVGFTGRYTVGVWVGNPDGTPVPGLTGAEA
AAPLLFDIFDLLPASRWPLPFPPPAGLLRVEVCAPSGLLAGPNCPQRVTEWFIPGTSPPTLCPYHQLVWV
DAATGLRVNSDCPPSGARSKVYFVLPPPLERWLARAGRPYRRLPPFRPDCPPLASAAGAAPRIISPPDGA
RYLLPPGFPGQQPLPLKLAARGGVGPVYWFLDGEPLGTTAPGHELAWQPGPGFHTLTVVDAAGRSDSVRF
RVE
>gnl|CDD|443981 COG4954, COG4954, Uncharacterized conserved protein, DUF2000 domain [Function unknown]
FDTKIAIVLRDDLAVWQKLNVTAFLASGIGAAAPELIGEPYRDADGNLYLPMSGQPVLVLAADAEQLRAA
HQRALERGLTIADYTEEMFSTGHDAANRAAVAAVPADDLDLVGIALRGPKKAVDKLTKGLKLHP
>gnl|CDD|443982 COG4955, YpbB, Uncharacterized conserved protein YpbB, contains C-terminal HTH domain [Function unknown]
MYLDYIILSCFSKLNGERTASSIYHLLKGKRSSQTLQDAHLYQLLPLFGLFPKLSREDFDQALKKLIKQG
LITEVEEGRYTLTAKGQELLEEFFSKLPHFNGWKYRRNEEVFWQRLSLLVQTLSNLSYGNKRYIPIVRDP
EIQQWVKQWLRQQKEKDELAKQLYDELLRLLEKLSEKEAEILVYRLTGYDQIGLTWEQLAEKLGLDTLDV
YLLFLNALHQLLHEIEKNPNQFPLLSQLLEDLLKESLLTQSAQKTYQLLQQGLSLEEIAQIRRLKLSTIE
DHLVEIAIKDPDFPIEPFVNKEDQQEIIQAIEKLGTWKLKEIKEQLPDLSYFQIRLVLAKREREEL
>gnl|CDD|443983 COG4956, COG4956, Uncharacterized conserved protein YacL, contains PIN and TRAM domains [General function prediction only]
LKKIIRLLFLLLGAALGYLLGPLLPELLGLSSGPLNNIVLPIVGALIGALIGFLLSPLLIKYVVRLIRRL
EKRLRKLPLSDLLAGTIGLILGLLIANLLSAPLSLLPIPIIGPLLPILLSILLGYLGISLGLKKREELLR
LFNPISREGKEAKGSLRKASPKILDTSVIIDGRIADIAKTGFLEGTLIVPRFVLEELQHIADSSDDLKRN
RGRRGLDILNRLQKEPPIPVEIYEGDFEDIKEVDSKLVKLAKELNGKIVTNDYNLNKVAELQGVPVLNIN
ELANALKPVVLPGEEMTVKIIKEGKEPGQGVGYLDDGTMVVVEGGRKYIGETVEVVVTSVLQTSAGRMIF
AKPKE
>gnl|CDD|443984 COG4957, COG4957, Predicted transcriptional regulator [Transcription]
MSDEDEADDLLELTADIVSAYVSNNSVPAEELPGLIRSVHAALSGLGAPAAPEEEKPKPAVPIKKSVTPD
YIICLEDGKKFKMLKRHLRTTHGLTPEEYREKWGLPADYPMVAPNYAAARSELAKKIGLGRKRRKAAAAR
A
>gnl|CDD|443985 COG4959, TraF, Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, chaperones, Intracellular trafficking, secretion, and vesicular transport]
RGDLVAFRPPEPLAAERGYLPRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEALERDRAGRPLPVWQG
CGVVPEGEYFLLGDNRPNSFDSRYFGPVPRSQIIGRAVPLWTPE
>gnl|CDD|443986 COG4960, CpaA, Flp pilus assembly protein, peptidase CpaA [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms]
MSLLLLLLLLLLLALLAFAAYTDLRTRRIPNRLVLALLLLGLLLALLSGLLAGLGLSLLGALIGLAVGFP
LFALGGMGGGDVKLLAALGLWLGPAALLLFLLLTALAGGVLALILLLLRRLPAAAGRPPWLARLRDRKRG
VPYGVAIAAGALLALPASLLL
>gnl|CDD|443987 COG4961, TadG, Flp pilus assembly protein TadG, includes N-terminal TadE domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
MRRRRLRRLLRRFRRDERGAAAVEFALVLPVLLLLLGGIIEFGRAFYARSKLQNAADAAARAAARGQATD
ADTAAAIVAVGGSSQVVAGGAAASGAVVVDLGAASLDLEDSSGDAADTSGLSSASGLNSLGTSLAGSSAV
ALTSGGGGSTAS
>gnl|CDD|443988 COG4962, CpaF, Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
MSQELVERVRRRLDREELREEVRAAVAEALRAEGLVLSDAEREALARAVLDELFGLGPLEPLLDDPDVTD
IMVNGPDEVFVERGGRLERTDVRFDSEEELRRLIERIAARVGRRLDESSPIVDARLPDGSRVNAVIPPVA
RDGPSLSIRKFRKRPLTLEDLVALGSLTPEMAEFLRAAVRARLNILVSGGTGSGKTTLLNALSGFIPPDE
RIVTIEDAAELQLQHPHVVRLETRPPNVEGAGEVTLRDLVRNALRMRPDRIIVGEVRGAEALDMLQAMNT
GHDGSMSTLHANSARDALARLETLALMAGENLPREAVRRQIASAIDLVVHLERLRDGRRRVTEIAEVTGM
EGGRVVLQPIFRFDPGGLDAAGGVRPRFLERLEAAG
>gnl|CDD|443989 COG4963, CpaE, Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
DLVALRPLPRISIQAFCESAALAALIEAAAEDRRLALAAVAVASGGAAAAAAAYLSAPTPNLILLEALSE
SAALLADVLPLSPDELRAALARLLDPGAARRGRVIAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDL
DLQFGDVALYLDLEPRRGLADALRNPDRLDETLLDRALTRHSSGLSVLAAPADLERAEEVSPEAVERLLD
LLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLLRELGLPDDKVRLVLNRVP
KRGEISAKDIEEALGLPVAAVLPNDPKAVAEAANQGRPLAEVAPKSPLAKAIRKLAARLTGRPAAAAAKA
GGKLLKRL
>gnl|CDD|443990 COG4964, CpaC, Flp pilus assembly protein, secretin CpaC [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
MKRRLRRLLAAALLALALLALAAPAPAQAAVRVSDAAAARTLSLGVGKSRVLELPRPIKRVAVGNPEIAD
VVVLSPRELYVFGKKPGTTTLTVWDADGRQIASLDVRVGRDLAGLRERLRRLLPGEGIRVRAVGDRVVLS
GTVSSAADADRAVDLAEAYAGGGKVINLLTVGGPQQVMLKVRVAEVSRSVLKQLGINWSGLGSSGGFSFG
LLTGGLLSGLLGGATAGAFSGFGFGNASISATLDALEQNGLARVLAEPNLTALSGETASFLAGGEFPIPV
AQGDGTITVEYKEFGVSLNFTPTVLSNGRISLKVAPEVSELDPSNAVTLNGITIPGLTTRRAETTVELRS
GQSFAIAGLLSSNTRQNVSKVPGLGDIPILGALFRSRSFQRNETELVIIVTPYLVKPVSPEALALPTDRF
RPPSDLELFLLGRLERPYPTPAAETAAQGSYGFILD
>gnl|CDD|443991 COG4965, TadB, Flp pilus assembly protein TadB [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
MAAGLLALLLTGLLLALLGALLGLLLPRLLLRRRAKRRRKKFEEQLPDALDLLARALRAGLSLPQALEAV
AREAPEPLREEFRRIVRELRLGVDLEEALRRLAERLPSPELDLFAAALRIQRRTGGNLAEVLENLAETIR
ERLRLRREIRALTAEGRLSARILAALPVLVLLLLYLLNPDYLAPLFTTPLGQILLAVALALLVIGLLWMR
RIVR
>gnl|CDD|443992 COG4966, PilW, Type IV pilus assembly protein PilW [Cell motility, Extracellular structures]
RRRQRGFTLVELMVALAIGLIVLAAVLQLFLSSRRSYRTQEALARLQENGRFALDLLSRDLRQAGYFGCA
SGNGNPNGGASVDIADDVSVLDVLLDTLGGSGDSTLGASSVTGLGDATDALSLDGVRLLVTLTTSATLNA
GLVVSTVLALTLDTAVRV
>gnl|CDD|443993 COG4967, PilV, Type IV pilus assembly protein PilV [Cell motility, Extracellular structures]
MSRRRRRRRQRGFTLIEVLVALVILSIGLLGLAGLQAASLRSSQDARQRTQAALLAQDLLERLRANPAAA
GSYPGIKSITVTVRWQ
>gnl|CDD|443994 COG4968, PilE, Type IV pilus assembly protein PilE [Cell motility, Extracellular structures]
MKKRMRRRQRGFTLIELMIVVAIIGILAAIAIPSYQDYVERARRAEAKAALLELAQAQERYYADNGSYPS
ALADLGLPASTSGYYTISIAAAATTYTLTATPQADGTLTLDQTGVKTATGADCW
>gnl|CDD|443995 COG4969, PilA, Type IV pilus assembly protein, major pilin PilA [Cell motility, Extracellular structures]
MKKKQKGFTLIELMIVVAIIGILAAIAIPAYQDYVARARVSEALALASPLKTAVEECALENGSLPNCNAG
DNGLPATIATKYVSSVSVDNGVITVTGTAALAGLTLTLTPTLNNGAITWTCSCSLPAKYPAGCR
>gnl|CDD|443996 COG4970, FimT, Type IV pilus assembly protein FimT [Cell motility, Extracellular structures]
MKRLRRRQRGFTLIELLVVLAILAILAAIAVPSFSSLIARQRLRAAANELAAALRLARSEAIRRGQPVTL
SPS
>gnl|CDD|443997 COG4972, PilM, Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures]
KKPLVGIDIGSSSIKLVELSKSGGGYRLERYAEEPLPEGAVVDGNIVDPEAVAEALKELLKRLKIKTKRV
AIAVPGSSVITRKITLPALSEKELEEAIEFEAEQYIPFPLEEVVLDFQVLGPSEEGPEKVEVLLVAARKE
VVEDYVELLEAAGLKPVVVDVEPFALLRALELLPPSGPDETVALVDIGASSTTLSVLSNGKPIFTREIPF
GLAQEIRRSLQFYRSQSGGNEVDRILLAGGGAKLPGLAEYLEERLGIPVEVLNPFAGMALSVDEEALAED
APSFAVALGLALRG
>gnl|CDD|443998 COG4973, XerC, Site-specific recombinase XerC [Replication, recombination and repair]
KLTLAEALEAYLEHLRERRLSPKTLEAYRRDLRRLIPLLGDADLPLEELTPADVRRFLARLHRRGLSPRT
LNRRLSALRSFFNWAVREGLLEANPAAGVKAPKAPRKLPRALTVDELAQLLDALADDPLAVRDRAIVELL
YSTGLRLGELVGLDWEDVDLDAGEVRVRGKTGKSRTVPLGPKALAALREWLAVRPELAAPDEGALFPSRR
GTRLSPRNVQKRLRRLAKKAGLPKHVHPHDLRHSFATHLLESGGDLRAVQELLGHASISTTQIYTHLDFQ
HLAEVYR
>gnl|CDD|443999 COG4974, XerD, Site-specific recombinase XerD [Replication, recombination and repair]
LTLADLLEAFLEELKREKGLSPNTIKAYRRDLRRFLRFLEELGKIPLAEITPEDIRAYLNYLRERGLSPS
TINRYLAALRSFFRYAVREGLLEDNPAAKVKLPKKPRKLPRVLTEEEIEALLEALDTETPEGLRDRALLL
LLYATGLRVSELLGLKWSDIDLDRGTIRVRRGKGGKERTVPLSPEALEALREYLEERRPRDSDYLFPTRR
GRPLSRRAIRKILKRLAKRAGIPKRVTPHSLRHTFATHLLEAGVDLRTVQELLGHSSISTTQIYTHVSDE
ELREAVEKLHP
>gnl|CDD|444000 COG4975, GlcU, Glucose uptake protein GlcU [Carbohydrate transport and metabolism]
MMGILIALIPALGWGSIPLIASKIGGSPVQQILGMTIGALIFAIIVFLFVQPELTGTIFIIGFLSGLFWA
VGQINQFKSFKLLGVSKAMPISTGMQLVGTSLFGVILFGEWTTTTAKVLGFLALILIIIGAVLTSYQDKK
SSQESKKNLKKGLIALLISTIGYVLYVVIPRLFGVDGWSAFLPQAIGMLIGALILSLKSKGSKFFEKKTY
KNIITGLIWAIGNLFMLISAQANGVATGFSLSQMGVVISTLGGILILGEKKTKKEMIYTIIGLVLIVAGG
ILIGILKS
>gnl|CDD|444001 COG4976, COG4976, Predicted methyltransferase, contains TPR repeat [General function prediction only]
MALDAYVEALFDQYADSYDAALVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR
LTGVDLSEEMLAKAREKGVYDRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLF
IFSVEDADGSGRYAHSLDYVRDLLAAAGFEVPGLLVVARKP
>gnl|CDD|444002 COG4977, GlxA, Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription]
LRVAFLLLPGFSLLDLAGPLEVFRLANRLAGRPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTL
IVPGGLDPAAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRV
DPDRLYVDDGDILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDP
RLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEE
IAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRARAAA
>gnl|CDD|444003 COG4978, BltR2, GyrI-like small molecule binding domain [Signal transduction mechanisms]
VEVKELPAQPVASIRATVPMDELGELIGEAFGELFAYLAENGIEPAGPPFAIYHDTDEDDVDVEVGVPVA
GPLPGTGDIKVGTLPAGKAATATHRGPYDTLDEAYEALLAWIEENGLEVAGPPREVYLTDPGNEPDPEEW
VTEI
>gnl|CDD|444004 COG4980, GvpP, Gas vesicle protein YhaH [General function prediction only]
MKSKNFLLGLLVGAAVGAAAGLLFAPKSGKETRKKLKDKADDLKDKAEDLKDELKEKASELSEEAKEKLD
ELIEEIKEKIEELKEEVEPKIEELKEEAEKLQKEVE
>gnl|CDD|444005 COG4981, COG4981, Enoyl reductase domain of yeast-type fatty acid synthase [Lipid transport and metabolism]
AGNLHPPLSARLANGESSALQFGAQGAQGLDALTALSVLADLEAYAPALAALAAAAAELLAPLLAVARPL
LAVPSDGFLPLDLEAAEAAAAAAAAAALLTLAAASSLPGVLAALGAALAALAAGGLDAAVAPVAAVGGHS
GVLLAEAADAAGAADDALLAAAALLGGAATAVARRRGGLAAGGEAPAMLSVSAVDPELLRALVAEVADLR
TPIHGPVLAIRNSRRRVVLSGAPAQLAAERARCARIAAKEAAEREAKLRGGAPFAPVFEVLPVEVAFHHP
ALADAVALVGEWAGRCGLDADLATSLAAAILVDPVDWVEAVDDAVAAGARWILDLGPGDLLTRLTGAVVR
GTGVGVVPAATRGGRRNLFTPGAAPEVPAAWSRFAPRLVRLPDGRTVVETAFTRLTGRSPILLAGMTPTT
VDPKIVAAAANAGHWAELAGGGQVTEEIFAENVAGLKALLEPGRTVQFNAMFLDPYLWNLQVGGKRIVQK
ARAAGAPIDGVVVSAGIPELDEAVALIEELHEAGFSYVAFKPGTVAQIRQVLRIAKEVPDTPIIVHVEGG
RAGGHHSWEDLDDLLLATYAELRARPNVVLCVGGGIGTPERAADYLTGQWSLAYGFPAMPVDGVLVGTAA
MATLEATTSPEVKQLLVETPGTPDWVGAGGASGGMASGRSQLGADIHEIDNAAARCGRLLDEVAGDADAV
AARRDEIIEALNKTAKPYFGDVAEMTYAQWLQRYAELSVGDAASAADTDATRSPWLDITWRDRFHELLQR
AEARLHPADRGEIPTLFPDDAAVEDPHAALDALAEAYPDAATTVLHPADVAFFVALCRTPGKPVNFVPVI
DKDVRRWWRSDSLWQAHDPRYSADQVCIIPGPVAVAGITRVDEPVGELLDRFEAAAVDRLQAAGVAPDAV
AARRYSVADGAAGALEFVLAAPDVSWAGRLTDNPVHRLGDGDQWLVVDPQGADPGDDRVDLDIPLDGTRE
LVIPLTLPESVADGGVPVVDAERASAAMYALLAVAAGVGNTTALPEVDDGVAHATFTWSPDLGADHAGVT
GGALPSDLSPSAIVPDALVGPCWPAVFAALGSAKTGDGPPIEEGLLAVVHLDHIALLVGELPLLSYTLTV
IATASWAEDTAEGRVVEVVVIVVEHGAEDGTTLARETERFRRRGRVYSRAPPAAAPAAGGAAAGTRRRSR
RLTRRAAVTATDRAAAVGVAHPSHTSDRAAALAAGDAPAVAGMWGSAAAAATASAAAQAVATSAAAPWTT
RWLYTVTPADQLDVTVERDREDVGVGRGGVVVGEVVCRVVVEVARAAVARCTPVVAAPGPPGQGPGQGGM
TRSKRARARAARRAARRIDKLTRSHLAASLLAVVRDLPRDNTTNGVARGVPLGLPTLVQVLTVATATAAA
ALMAAQREEGAEAGAAVFGGHSAGASAALSAALAAIALEVVLELVLSRGSTRGSLMHRLAPRDSNGRMRA
RRPALDDVDDDHVDAEIEARSGESGEFLQVVLYNVAVNLAAIAGAIAGAAAEAERLARAAGRARGAKPFK
GVPGLDVGFHSRVARFVLRPGREVLRGRLPELDPEDLDVGPLVPLLVARLDLLPRIFARDILEVVPSEVL
DADEEEATADADAAAKLPVLLALLLLVLLLPWQWASPLRIEETELLLLSQEEEGLGGVGVVVAIELGGLA
TATLLAATVLVLEFVAVQVNVVHVLRRETDVDLTPEDEAAEAPDDEDAAAPAAAPAAAAAPAPAPAPAAA
APAAPAAPAPAAPAAAAPAALLSFAAPPALDADDAQTTLAASASVRLLLLLSSLTALLSDAGGGLADGAS
LADLSASVDAASSEGMAALAVTSLKQAGKYKALGGVKGGAVSERGPRLTGVSGLGAGAVADRVAAARLLG
LAGASGGGAAGAGGTLALLSTAAGDLAAAASAAAGGAAAVIAAGAATAGGGGAAAVASALAVPAAGLAGG
ASVLSAALGASAASVAASGEVAAKAAAAAAELVELADDALVAAAPADGAPVLVAVDAVVSAARADLDRWS
LARAEATARWVLAILPEADAARAAARDAAAAGAAAAAARTSAAEAASAAAAFAAAKATVAEAGAASADAA
AAAASSAVAGAAAAGAAVAAVASAAAGGQAVAVATAAGVLVRASASARALLRLAAALAAYASVVAADAAI
STADETLAEAVGVAVGKLAGAALLVFSDALAVARAKAEAAPRVPEAASELAKATTVAIGLLLAPDGRLLG
SLSVHGARADSGARLHVLGAGGEVGGVGALAALTATGTAADAVVVASTSALLGTGRVAGLGGGGGGDGLA
TLVQGIVARVVAASETSGVTTALCAAGARLLAGEAPGEADLAGLEGESRAVLAGALAEADLDLALLAAAA
AQAAAAATAAADAAATAGAAAAPPAPLPAPSREPAASAPGASAPPATAVSAVGSEPAGEASAAGLAEAEW
VAGLAAWTDTAVAGWLTGDEVSEDPIEIGALGTDETVAGAEVELNDDAGVDVDGVDERRVESVIALDPTD
SVDSVVLADEYAAFDDTVDESAEAAEEVVWEDEVTAIADSPPRADGRTVGARGPEVDRAPRRTGSVVVTV
GIGDEAVADLVTTADDADDSEIETAVDLSVAVSAVVGASAAVSTFGGMSFTVGALLDRSGEGAVGSGSLS
MIDLVRNALVTNAVGGQGYSSSYPIIAAAVAASVGAEGGVSIGVGAAAVAVVLGAVDGGAVIIELGVASG
AAGAQDTALAGGGGMGRFAAAADDRAMAATRIGQGALDSRGADGRVLGQGGGDVGGVVLVGGVGDVAATL
GVVAGGAALAAGAFGVAAALPVRGGGLGAGGGGDGALASSRASEGGALDAALDDLAANLAAAGALEAGPA
HTLLATSALGSSKAGGAAAEARALGLLAAGGGATAANAPFLGALDALEVGGRNDLHRALLLGDALPLAVG
VVSLLRGSTLALGAASGLLALTQVHRGGLLAALALAVAAQAAALGRPRAAARIAQRNALAELRRVRRQRS
SRRGGAGEPALQRLDREGALAKPSAIRLGAPLLYTPTARGDGDAVYAAILAGGA
>gnl|CDD|444006 COG4982, FabG2, 3-oxoacyl-ACP reductase domain of yeast-type fatty acid synthase FAS1 [Lipid transport and metabolism]
KTATEVDVASADRLLAGAAALDQPATGLLVSLGGRLAAGLAAGLATGSRDSLSGGALEALLAPAVAEALL
AAEALLVPVAAALVVARVAAVAAAALAEAGAVLALAAEAALAAAASAVPAAVIATGAALVAALALKLLGA
AGLLLLAVSVSAQAGAPSAVVALEAASGAGAQLAELLAALALLAAALLAVAARRAGAVSLGVPALRSLLN
ALGLSVLAESAERAGAVRTGLLAALGARRVVRSAPILGTAQQLAEGLLAAGARAEALAKEEKRKLAGGVV
GGAVVDPVQEEVGAALPDGVPEVDAAADLAAAEALDVGLAAELRTAILLAAVVVVVDAVAAVAAVTAAGL
LLLLGPGLTATRTPVSRVGAVGVAPAAVGLAARELFTTPATPVSARRPSDVAPTTVPLAPGAAAAATGRT
ALLARLPILGLVMTPTTTAAAAAAKAAAAAAGAGEVGEGGELEELFAGRLAELLGALAEGVDVFAVALAL
LPALLPLQVGLQRLASEAFQKGVAADGGVVIVGAVAQEAALPLAEVLVDVGIGLVVGGPAGVATIVSIVR
IATAAEVIEVPIIVEEGGGAGGHGSAADLDDLLLTAQALLSRTPPVVIVVGGGIGTAPAAATWAPGGKGV
LGDPSGTPVLAADGVAAAAAAAAGTSLLVAKMVLPETGESPGDLGAGGAGGAAASGGSDLLAITHEESSQ
RRLASRLDDAEAADAAAAEAARARIAAAAEATAKPEFTSDAAAADLEALARADALSALDDDDAAQEAIGV
IEASARWDDTLEDELQRMTARLEARDAAELAAPAATLAADDADLALVHAARPALAAAILPAASAPVLHPA
DVPFAVVLFKPIGPPPPVVPVIFDDVRRWRRIDSLQAAHAARDDADAVVAIGTVAAAAGETLDDEQADEL
LDREVARITAAALAAGAPRALVAARGLEGADVAAGVVLAADDIVWASRLDTNPVRRLEIVASTSAGVDPR
AVREEVIPELVDGADAGVEDAVVLVIPVLLTRVVTDGTLATDGTATGTPADALVAAATAGTAVAAGAAGG
ELAESTPSGAAGIADVGADWAAVPVALVTSATVPDGVPGGPLSTVVPAPLSVLGAATAALGAALAAVHLG
VIVVLDLLLLVLGDAALIHLALSSTLAALVATDLGRVVTADVDVRVVDGVVVTEETRRGAARGTSDEEAA
PGRRAGGRGRDTEAVPGARRTLARTTVRARRRTTAFAAVAGDYSPIHVSVGAAPRAGLDAAAAAGGWLSA
PAAHAAQAAAAAQGSAAAARWTGGPAPLLIGWTTRELTVVRAGDEVVVVVVRVGVERGGEVVVVVACVVA
AVAVSATAAAAAPPGVAGFPPGSRQAAGGGGDDARRRKAAARRWDKAARATRDRLGASVLLVVGRDPTHV
LALLGHTQHPVGGLLLTQQTQQAAATVAAAAVAEAGEAGGFAGAAAALAGSVAGEAALAAVEGVVLLLEL
LGEVVHRGSARHRIVRPGDLRRSDDRAAAAHPSVQVAEDVDDVADVAAIVERTLEFAQEYVNNLLAGQAA
AAAGVVALLAALEAERRRREAGGGGRSFFLRVGIVDVPFSSVLLRGGLPEFRSLLRLLLPDDIDLILRGG
KLPPNLPRSFFELEPEFVESILLVVPDEPVEALLDDWTLAAKLLILLLRTLLIELLAWQFASPVRWIETQ
DLLFIEGLGGGLGVERFVEGGGKSAPTLALTLALTLKLGSAAGTRVVVLNRERDDSLVFATDEDPEPVED
EADAEEAAASAAAAAPAPPAAAAPAAAPAAAGGPRPDDLPFTASDATKALIALSTKIRPDQIGAADTIET
LTDGVSSRRNQLLMDLGSELGLGAIDGAAEADVPTLSATVDKLARTYKPFGPVLSDAIRDRLRKLFGPAG
KRQSYIADRVTGVWQLGEGWAAHVTAELALGTREGASVRGGDLATLPTAAPSNAAAVDALIDAAVAAVAA
RHGVSVALPSAGGGGGATVDSAALGEFTEQITGRDGVLASAARTLLDKLGLAAPAPVAESADEDAELVEL
VEAELGSDWPRLVAPAFDARKAVLLDDRWASAREDLARLWLGDEAAIEAGSFTGAGEAVADQAAWWAGKA
LAAGRAVLARRYGQIAADAEDPSAGEYADDVAVVTGASPGSIAAAVVAGLLAGGATVIATTSSLDSDRLA
FYKELYRENARGGAALWVVPANMASYRDVDALVEWIGTEQTETVGATTTVTKPALTPTLLFPFAAPRVSG
DLADAGPRAESQMRLLLWSVERLIAGLAAIGADTDVDHRLHVVLPGSPNRGMFGGDGAYGEAKAALDAIV
NRWRAEKSWSSRVTLAHARIGWVRGTGLMGGNDPLVAAVEAAGVRTYSTEEMAAELLDLCTAEAREQAAS
APLDADLTGGLGEVDLDMAALAAEAEADAAEEAAAADSAAAGTIAALPSPPRPAQPVALPDWGEVTARPE
DLVVIVGAGELGPWGSARTRFEAEVSVELSAAGVLELAWNTGLITWEDDPKPGWYDTETGELVPESDIAE
RYHDEVVARCGIRPFVDDGAMVDGTSPLLASVFLDKDLTFSVSSEAEARAYVDADPEHTVIAPDEESGEW
QVTRKAGTEIRVPRRATMTRTVGGQFPTGFDPTRWGIPASMVDSVDRIALWNLVTTVDAFLSAGFTPAEL
LQSVHPSDVASTQGTGMGGMTSMRKLYVDRFLGEPRPNDILQEALPNVVAAHVMQSYVGGYGNMIHPVAA
CATAAVSVEEGVDKIRLGKADFVVAGGIDDIGVESITGFGDMNATADSEEMLAKGIDDRFFSRANDRRRG
GFVEAQGGGTILLARGDVAAKLGLPVLGVVAFAQSFADGAHTSIPAPGLGALAAARGGKDSKLARDLAKL
GVTADDIAVVSKHDTSTNANDPNESELHERLAHAIGRTDGNPLFVVSQKSLTGHAKGGAAAFQLIGLCQV
LRSGVIPPNRSLDCVDDKLAGDDHLVWLREPLRLGAKGPLKAGLLTSLGFGHVSGLLAVVHHAAFFAALE
AEEADAYAAAARARRARGRRRRAAAMAGGGMGYRRPPRRRRDGRRDHEAAAALDLLELLRADDGDAGAVA
GLDGDAAA
>gnl|CDD|444007 COG4983, COG4983, Primase-polymerase (Primpol) domain protein [Mobilome: prophages, transposons]
PEELKERAQWVLWRYEQRDGKPTKVPYNPATGGPASSTDPETWATFDTALEAAERGGYDGVGFVLTEDDP
LVGIDLDDCRDPETGEIDEWARDIVERLDSYTEVSPSGTGLHIFVRGELPGGGNRKGGIEIYDTGRFFTV
TGDHLPGTPTEIAERQDALDAIYDEYFGATDPSKAEDEPVDLDDEELLERARKAKNGEKFRRLWSGDTSG
YGSQSEADLALCSLLAFWTGGDREQMDRLFEKWDRVHGGETYGERTIEKAILPTGGAIAEVDEDVALDAE
EVDDELGGDDARDDKDATSLAPEGDTAAERREALENDEGSLSDAGGENEEGDDGVTDEEVKLGGGGTAPG
AAIEERIAFQDAAGFGERLAASEATSLVRGAELGKLGAELVEAGKTALEKGLVAGEGEDTGTDKLEMLGL
SLVAGDDAREVDLVTPTAKVPFLALAAVDESVLGKDRKLERLTVVAPLIAAELLDGMARELMRDRQDLPS
AADSKEAYTSGTEQGSTVEGL
>gnl|CDD|444008 COG4984, COG4984, Uncharacterized membrane protein [Function unknown]
MTQLSALTAPDLDPAALERALQLAGVTPSRAAWRRFLARLLLLLGALLLLSGVIFFFAANWASLHRFAKF
ALLQALLVASALAAWRLGLERLAGQAALLLAAVLVGALLALFGQTYQTGADPWQLFALWALLILPWVLLA
AFLGLLLLYLLLLNLLLILYFLQVRSDFELNWLTLVLALLAALLLALLLVLALDKLSLLSAAYLGILLLL
ARLILVLAIAALAAFVVALLGRSSLLLAAGLLLTLGAVYLGQLYRLVILFLLLLLLVALLLLFLLLFSQG
RLFALLALLFLAALALALAVILLLALLLLSLLALALVGA
>gnl|CDD|444009 COG4985, PstA, ABC-type phosphate transport system, auxiliary component PstA [Inorganic ion transport and metabolism]
MKKWFKSGSPWIWLTAGAVSISLIAVLGLLLLIAVRGLGHFWPAPVYEFTYTQPDGEPVRLIGEIYDREE
VPRARLRDAGVPLPGEDAEFVTRYLIKTGNRDLYGLDFRWVLEPDIVERSYPKDLAVLERREWGNFYGYL
VAVKEDGQVVAEGDAAWEELQQRLERALELRDQIDDIEKGDIGAINYQLERLRLKERRLELDGQLDDEAQ
ADIEAERAELEAEYAVLEQQLDALRQQINRDSLVVRDMDGEEVEIPLVVVVVAVPNNNMMLAKKKKGFFL
FGKFFFDSEEEAEEEGGGGIFFIIFVTVVMVLMVVVVVVVVVVAAALYYYYYAGGGLTIRIIRVVNNNLG
VVVVVVVGGFGGFFFFLGGGGDDDFFFFAAAPPPTPGGGGLLLLLLLLLLLLVVVVVVVEEEELRRRSSR
RSGSLLLAAAATTATTLWVVVLPAAAMAMMLLLAAAAAAAAAAALLLLVVVVVALPPPLPLDPPFFLLLL
KHKFMHFFFYIVDVFSQPPVAAAALLLVAALLLLLVVVILLLLAIAIIRRRRRRR
>gnl|CDD|444010 COG4986, COG4986, ABC-type anion transport system, duplicated permease component [Inorganic ion transport and metabolism]
MTRRLFPANSTRRRPNRWDLAALLLVLALLVLLAYGAKQMTAPLAPGETPPISLDPANLPYYALRTTLRM
FAALAASLLFTFVYATLAAKSRRAEKILIPLLDILQSVPVLGFLSFTVTFFIALFPGSLLGVELAAIFAI
FTSQAWNMAFSFYQSLRTVPRDLDEAARIFRLSGWQRFWRLELPFAMPGLVWNSMMSMSGGWFFLVASEA
ISVGNQDIRLPGIGSYLALAIAQGDLGAIGWAILAMLVVILLYDQLLFRPLVAWADKFRFEQTASEEAPR
SWVLDLLRRSRLLRALGRPLGPLGRALLRLRLRLLPRAPRPPAVSRALSRWLDRLWLALLALLVLYGLWR
LLLFLLTEVGLSEVLHVFLLGLLTLLRVVVLIALASLIWVPVGVWIGLRPRLARRLQPVAQFLASFPANL
LFPVAVLLIVRFGLNPNIWLSPLMILGTQWYILFNVIAGASAIPNDLREAARNFGLRGWLWWRRLILPGI
FPYYVTGAITASGGAWNASIVAEYVSWGDTTLQATGLGAYIAQATAAGDFPRILLGIAVMSLFVVLFNRL
VWRPLYRLAERRYRLD
>gnl|CDD|444011 COG4987, CydC, ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
RDLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPPILNLFVPIVGVRAFAIGRTV
FRYLERLVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVAL
LVILAAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAA
YGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVL
AALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPV
LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHL
FDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDA
PILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN
GRYRQLYQR
>gnl|CDD|444012 COG4988, CydD, ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
QKPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLL
RALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLF
LAALVPLLILVAVFPLDWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTL
KLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLSSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFV
LLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR
PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNP
YLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLR
DAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLA
KNG
>gnl|CDD|444013 COG4989, YdhF, Predicted oxidoreductase YdhF [General function prediction only]
MKRIKLGASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLS
PSLREKIELQTKCGIRLPSEARDNRVKHYDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVA
EAFDELKASGKVRHFGVSNFTPSQFELLQSALDQPLVTNQIELSLLHTDAFDDGTLDYCQLNGITPMAWS
PLAGGRLFGGFDEQFPRLRAALDELAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDIE
LTREEWYELYEAARGHEVP
>gnl|CDD|444014 COG4990, YvpB, Predicted cysteine peptidase, C39 family [General function prediction only]
KGHFGVTLLSFILGGGTAGSTYFKKVETKKTGDKIARVLLALTLTKVLKTVLKKVAVDSLALKEKTKAAL
GLARVYGVSSYGLARSAVRVSLTGELPAPGMKKIIYPKPNPDSVLLNVPYISQLPELPTGCEVTSLAMLL
NYYGIDVTKDELAEYLPKVPLPYNGYGGNPNKGFVGDPYGSDPGYGVYAPPIAQLAKKYLPGKAVDLTGA
SFEDILDELASGNPVIVWTTLDFSPPSAFRSWTTPDGKTFDFTANEHAVVVTGYDDEGVYVNDPLGGNKY
VKYSRSLFERSWEQMGKQAIVIR
>gnl|CDD|444015 COG4991, YraI, Uncharacterized conserved protein YraI [Function unknown]
MRRALLAAALALLLLAPAAAAAATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGCTSGGGWCKVSYG
GQRGWVSARYLQVSYDGQPVPL
>gnl|CDD|444016 COG4992, ArgD, Acetylornithine/succinyldiaminopimelate/putrescine aminotransferase [Amino acid transport and metabolism]. Acetylornithine/succinyldiaminopimelate/putrescine aminotransferase is part of the Pathway/BioSystem: Arginine biosynthesis
TSEEIIELFDQYLMPTYGRLPVVLVRGEGSYLWDVDGKRYLDFLSGIAVNSLGHAHPRLVEALKEQADKL
IHTSNLFYNPPQGELAEKLAELSGLDRVFFCNSGAEANEAAIKLARKYGYDKGTGRPKIIAFENSFHGRT
LGALSATGQPKYRKGFGPLLPGFVFVPFNDLEALEAAIDDDTAAVIVEPIQGEGGVIPPPPGYLKGLREL
CDEHGALLILDEVQTGMGRTGKLFAYEHYGVEPDILTLAKGLGGGFPIGAVLAREEVADVFTPGDHGSTF
GGNPLACAAALAVLDVLEEEGLLENVAEKGAYLREGLEALAAKYPLVKEVRGRGLMIGIELDDPAAEVVK
ALLEEGLLVNAAGPNVIRLLPPLIITEEEIDEALAALEEALAELAA
>gnl|CDD|444017 COG4993, Gcd, Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism]
DPGDWLAYGGDYAGQRYSPLDQINPDNVKKLKVAWTFSTGDLPERGHEATPLVVDGVLYVCTPHNRVFAL
DAATGKELWRYDPKLPDDAACCDVVNRGVAYYDGRIFLGTLDGRLVALDAKTGKVCWDVKVGDPKKGYTI
TSAPLVVKDKVIVGGSGGEFGPRGVVRAYDARTGKLVWRFDTIPDPGEPGAETWPPGDTWKRGGGNVWGT
MSYDPELGLVYLPTGNPAPDWNGGQRPGDNLYSSSIVALDADTGELKWHYQTVPHDLWDYDGPNEPILVD
LPVDGKTRKALVQATKNGFIYVLDRETGEPLVTQPFVKPPNWATEIDMWGATPIQTPPSLDGKTTLICPG
ALGGKNWGPAAYDPETGLLYVPANELCMDYELVPREYQAGAPYLGATLTMYPCPAPPWGTLTAIDLNTGK
IVWQVPLGFPNWGGPLATAGGLVFIGTLDGYLRAFDAKTGKELWKFRLPSGGQATPMTYEVDGKQYVAVA
AGGGGWLGLGLYTPQGDYLIAFALP
>gnl|CDD|444018 COG4994, COG4994, Uncharacterized protein CV0675, UCP033623 family [Function unknown]
MADAEDDLLEELRELERALLDPEVRADRARLEALLHPDFVEIGRSGRRYDRAEVLAALADEASMGPIELS
DFELRRLSPDVVLLTYRAEDEGSGRASLRSSLWRREDGGWRLRFHQGTPVA
>gnl|CDD|444019 COG4995, COG4995, Uncharacterized conserved protein, contains CHAT domain [Function unknown]
LLALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAA
AALALLLLALALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAA
LAAAAAAALAAALAAAAAAAAAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAAL
AAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAA
ALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALLLLLAAAALLAAALA
AALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLRLLLAALALLL
ALAAYAAARLALLALIEYIILPDRLYAFVQLYQLLIAPIEAELPGIKRLVIVPDGALRLLPFAALPDGKG
QYLIERYAISYAPSLSLLRARPRPPLPAGLRVLAVGNPDFSRGLPPLPGAEAEVEAIAALLPGGTVLLGE
EATEAALLAALPGYRILHLATHGLFDPDNPLRSGLLLADGLLTAYELAQLDLSPAELVVLSACETGLGDV
RGGEGVLGLARAFLYAGARSVVASLWSVDDEATAALMTEFYRNLAQGKSKAEALRQAQLALLKGSPYSHP
YYWAAFVLIGN
>gnl|CDD|444020 COG4996, COG4996, Predicted phosphatase [General function prediction only]
MMIKLLVLDLDGTLWDHHNISELKPPFKRISENSIVDSYGREVRLFPDVREFLEWAKERGAILSTASWNV
PDKALEALEALGLDEYFDYPVIEPHPYKFLMLEEILRRLKERGIKIKPDEIVYVDDRRIHFGNIWLYVGD
VKFIEMWKDVKSFEELKELLKKLIS
>gnl|CDD|444021 COG4997, COG4997, Predicted house-cleaning noncanonical NTP pyrophosphatase, all-alpha NTP-PPase (MazG) superfamily [General function prediction only]
MKREYNKLVRDRIPEIIESSGKTCVTRILSDEEYLQALRKKLIEEAQEYAEASDEDALEELADLLEVIDA
IAEAHGISLEELEEIRKEKREERGGFEERIFLIEVEDE
>gnl|CDD|444022 COG4998, RecB2, Predicted endonuclease, RecB family [Replication, recombination and repair]
MALSGKRRWRSSERIAARILEEMGFRVLETHKKVKVEGVEVGEVDIVAEDKDGEKYAVEVKAGKVDVSGV
RQAYVNAKLLGAKPLIVARGFADESARALAEKLGVEVIELSDVFLVDSEELEDIVEEAVYDALEELLEVL
SACSNLSPEELEVLRAIAQSEDIEEAAKKLGVSAEELARLIERLRRKGVLPRSSYRALRLAAKLLLLRAR
LRALLEKLETLER
>gnl|CDD|444023 COG4999, BarA5, Uncharacterized domain of signal transduction histidine kinase BarA [Signal transduction mechanisms]
MTMTLRRRRRIILLLLLLLLILLLLLLFFFFFVYRYQLLQQQLSASIIIIIAAAAASSEYLMNKRRREQL
LLLLLRRHHRHSIIISAIDDNNNLNNLSNNNNNNLNLLLLQLPPPSPPLLLLTRSDLILLLIPPISIIYE
DESSEPSDNTAANPLGYIAIELDLSSDRLQQYQEQFVATLLLLLLLLLALLFAYRLMRDVTVPITNMVNV
VDRIRRRRLDSRVEGGMLGELLLLKNGINNMAMSLAAYHEEMQQNIDQATSDLRETLEQLEIQNVELDLA
KKRAQEAARAKSEFLANMSHELRTPLNGVIGFTRQTLKTTLTPTQTDYLQTIERSANNLLNIINDILDFS
KLEAGKLLLELIPFPFRDTLDEVVVLLALLAHEKGLELTLLLDNDVPEDVIGDPLRIQQILQNLLGNAIK
FTETGNIDIIVELRTQRQNSVELQVQVRDTGIGISERQQAQLFQAFFQADASISRRRGGTGGGLVITQKL
VKEMGGEIGFISRLSQGSTFWFTFFLLLNLAPALSDPLPLDRLQGKRLLYVEPNPAAAQATLDLLSQTPL
EVTYSPTLEQLPEAHYDILLIGLPVTYRNTLADLTDKLAQALRMADCVILALPSTAQVLAEQLKAAGARA
CLSKPLSATRLLPLLLDECLFELPLPAATPEAPLPPLVVAVVDDNANNLLLIALLLELVVQVVVCCSSGE
AAAAAAAQQLDDILIMDIQMPMMDGIAAEEIIRQLPHNNTTPIVAVAAAAAAGREELLLAGGMDDYLAKP
IEEELLLLLLLRYQPGPHTVPSPPPVPPSLAPLVLLQASQLSLDAAAALQQALDALLLLLELLLLLLLEL
LEVLILRQEIDLLGALDLLHGLHSSLLCSGLLRLKGLLSLQLQLEPEELLLLEEEEELLEELDEELLLES
EELQRLEANAL
>gnl|CDD|444024 COG5000, NtrY, Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms]
SGLQILFLLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARA
FNRMTDQLKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLP
ELDLAELLREALERGWQEEIELTRDGRRTLLVRASPLRDDGYVIVFDDITELLRAERLAAWGELARRIAH
EIKNPLTPIQLSAERLRRKLADKLEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLPEPQLEPVDLNE
LLREVLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVSTRREDGRV
RIEVSDNGPGIPEEVLERIFEPFFTTKPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLAEE
AE
>gnl|CDD|444025 COG5001, COG5001, Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms]
LLALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAA
ALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAA
LGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLAL
RLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSG
RRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAV
AERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERA
RERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLG
EWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPE
EALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLG
LEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA
>gnl|CDD|444026 COG5002, WalK, Sensor histidine kinase WalK [Signal transduction mechanisms]
LLLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLL
LLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSA
LLLGLLLLAAVERDITELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGAADDPEERREYLEIILE
EAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPLLVLGDPD
RLEQVLTNLLDNAIKYTPEGGTITVSLREEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGG
TGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLARE
>gnl|CDD|444027 COG5003, gp37, Mu-like prophage protein gp37 [Mobilome: prophages, transposons]
MIAQIEDALIARLRAGLGRLVRTVESYPGEWDDDVRRVVRRLPAVWVAFGGSRKEPVGTGRRRYKVTARW
VVFVAARSLRGEAAGRRGDKREVGAYQLLEAVRRLLNGQDLGLLGTPLVPGRVRNLFNDTQQGQGVAVYA
LEF
>gnl|CDD|444028 COG5004, gpX, P2-like prophage tail protein X [Mobilome: prophages, transposons]
MAMTYRTRQGDTLDALCWRYYGRTAGVVEAVLAANPGLAALGPVLPAGTVVTLPDIPAAPTVETVRLWD
>gnl|CDD|444029 COG5005, gpG, Mu-like prophage protein gpG [Mobilome: prophages, transposons]
MMIEITLDDAELQRALARLAARLGDLTPLMRDIGEVLESSTEDRFETEKDPDGTPWAPLSPSTLARRRGG
KILQDTGDLRDSITYQAGDDSVEVGSNLIYAAIHQFGGTKGAGGPVTIPARPFLGLSADDEAEILDILED
YLAEAL
>gnl|CDD|444030 COG5006, RhtA, Threonine/homoserine efflux transporter RhtA [Amino acid transport and metabolism]
MSASSSRLPGVLLVLLSALSVQLGAALAKLLFPGVGPLGVTALRLAFAALILLLIFRPWRRRLTRRDWLA
LLLYGVALAGMNLLFYLAIARIPLGIAVALEFLGPLAVALLGSRRRRDLLWVALALAGVVLLLPVGLSGG
SLDPVGVLFALGAAACWALYILLGRRVGARLPGLTGLALGMLVAALVLLPFGLPTAGPALLDPPVLLLGL
GVAVLSSVLPYSLEMVALRRLPARTFGILMSLEPAVAALAGWLVLGEVLTPLQWLGIALVVAASAGATLT
ARRRPPPAAA
>gnl|CDD|444031 COG5007, IbaG, Acid stress protein IbaG/YrbA, BolA-like family [Signal transduction mechanisms]
MTPEEIKQLIEAGLPCAEVEVEGDGSHFEAIVVSDAFEGLSRVKRQQLVYAPLGDYIASGEIHALSIKTY
TPEEWAAQRKL
>gnl|CDD|444032 COG5008, PilU, Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures]
MDLEDLLKLMVEKKASDLFITAGAPPSIKIDGKLTPLSQQPLTPEQVRELAYSIMNEEQREEFERTKECN
FAISLPGVGRFRVNAFRQRGSVGMVLRRIETEIPTLDELGLPPVLKDLIMEKRGLVLFVGATGSGKSTTL
AAMIDHRNENSSGHILTIEDPIEFVHKHKKSIVTQREVGVDTESYEVALKNALRQAPDVILIGEIRDRET
MEHAIAFAETGHLCLATLHANNANQALDRIINFFPEERRPQLLMDLSLNLRAIVSQRLVPTKDGGRVAAV
EVLLNTPLIADLIRKGEIHEIKEAMEKSRELGMQTFDQALFRLYEAGKISYEEALRNADSANNLRLRIKL
GSEGAAKADLDAGFDGLTLD
>gnl|CDD|444033 COG5009, MrcA, Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis]
MRLLKILLILLLLLLLLGALAVAGLYLYLSPDLPDVETLKDYQPPTPSRVYSADGKLIAEFGEERRIPVP
IEEIPPLLINAFLAAEDKRFYEHPGVDPIGIARAAVVNLRTGRRVQGGSTITQQVAKNFLLSPERTLTRK
IKEAILALRIEQELSKDEILELYLNKIYLGHRAYGVAAAAQTYFGKSLDELTLAEAAMLAGLPKAPSRYN
PIRNPERALERRNYVLGRMLELGYITQAEYEAAKAEPLTARYHGASAEVDAPYFAEMVRRELVERYGEDA
LYTGGLKVYTTLDPRLQEAAEKALRDGLLAYDRRHGYRGPEAHLDLAEEDWDEALAEVPDVGDLRPAVVL
EVDDKSARVGLRDGETGTLPLEGLKWARPYINDNRRGPAPKSASDVLKPGDVIRVRPVADGGWRLRQIPE
VQGALVALDPHTGAVLALVGGFDFEQSKFNRATQAKRQPGSSFKPFVYAAALDNGYTPATIINDAPIVFD
DGGGGGVWRPKNYSGKFYGPTTLREALEKSRNLVTVRLLQDVGIDYVIDYAERFGIYSKLPPNLSLALGS
GEVTPLEMARAYAVFANGGYRVEPYLIDRIEDRNGKVIYRADPARACEDCDAAEWDGAEPRLPDPAEQVI
DPRTAYQMTSMLRGVVQRGTGRRARALGRDIAGKTGTTNDSKDAWFVGFTPDLVAGVWVGFDDPRSLGRG
ETGGRAALPIWIDFMKAALKDKPEKPFPVPEGIVTVRIDPKTGLLASPGDPDAIFEAFKPGTEPTESASE
DLGPDASEGTGEGLF
>gnl|CDD|444034 COG5010, TadD, Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDF
EESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDE
AKAALQRALGTSPLK
>gnl|CDD|444035 COG5011, COG5011, Uncharacterized conserved protein, DUF2344 family [Function unknown]
QRLRVRFAKGGRLRFLSHLDLMRLFERALRRAGLPVAYSQGFNPHPKISFAPALPVGVESEAEYVDLELT
EPVDPEEFLERLNAALPEGIRILEVEEVPLKAPSLMALLNAAEYRIELPLADELPEELEEAIEAFLAADE
ILVERKTKKGRKEVDLRPLILELEVEEGEVLRLVLSCGSGGNLRPEELLEALEEVTGLELELLRIHRLEL
YLR
>gnl|CDD|444036 COG5012, MtbC1, Methanogenic corrinoid protein MtbC1 [Energy production and conversion]
SLTRPYGEELLESLADAVLEGDEDEALELVAEALAAGMDPEEIILDGLAPGMREVGELWEEGEIFVPEEH
LAAAAMKAGLEILKPLLAEEGGRKGKVVIGTVEGDLHDIGKNIVADMLRAAGFEVIDLGADVPPEEFVEA
AKEEKPDIVGLSALLTTTMPAMKELIEALREAGLRDKVKVIVGGAPVTEELAEEIGADAYAEDAADAVEL
AKELLAERR
>gnl|CDD|444037 COG5013, NarG, Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism]
MGPASSHLLDRLRFFRRGEVFSDGHGVTTEGGREWEDFYRDRWQHDKVVRSTHGVNCTGSCSWKVYVKDG
IITWETQQTDYPRTGPDLPNYEPRGCPRGASFSWYTYSPTRVKYPYVRGVLLELWREARARHGDPVEAWA
SIVEDPEKRRRYKSARGKGGFVRATWDEANEIIAAANVYTIKKYGPDRVAGFSPIPAMSMVSYAAGARFL
SLIGGVMLSFYDWYADLPPASPQVWGEQTDVPESADWYNSGYLIMWGSNVPQTRTPDAHFMTEARYKGTK
VVVVSPDYAENTKFADEWLPPKQGTDAALAMAMGHVILKEFHVDRQVPYFTDYARRYTDLPFLVTLEERD
GGYVPGRFLRASDLGGALGESNNPEWKTVVLDEATGEPVVPNGSIGFRWGESEGKWNLELKDATGADVDP
ALSLLDDHDEVVEVAFPYFGGETGGGGVLRRGVPVRRVTLADGEVLVTTVFDLMLANYGVDRGLPGNWPT
GYDDDVPYTPAWQEKITGVPREQVIRVAREFAQNAEKTRGRSMIIMGAGTNHWYHSDMIYRAILNLLMLC
GCQGVNGGGWAHYVGQEKLRPQTGWQPLAFALDWSRPPRQMNGTSFFYAHTDQWRYETLSADELLSPLAD
GKFWGGHLADYNVRAARLGWLPSYPQFNRNPLDLADEAEAAGMEPADYVVDQLKSGELKFACEDPDNPEN
FPRNLFVWRSNLLGSSGKGHEYFLKHLLGTDNGVQGEELGPGLRPREVVWRDEAPEGKLDLLVTLDFRMT
STCLYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPPWEARSDWDIFKGIAKKFSELAAGHLGVRKD
VVATPLQHDTPGELAQPFGDVKDWKKGECEPIPGKTMPKLVVVERDYPAIYEKFTSLGPLLEKLGNGGKG
ITWDTEEEVEELGKLNGVVREEGVAKGRPRLDTDIDAAEAILALSPETNGHVAVKAWKALEKRTGRDLAH
LAAGREEEKIRFRDIQAQPRKVITSPTWSGSESGGRRYSAFTTNVEELIPWRTLTGRQHFYLDHDWMREF
GEGLPVYRPPLDMKTLFGEPGIGPNGNPEIVLRYLTPHQKWGIHSTYQDNLLMLTLSRGGPTVWMSEEDA
AKIGIKDNDWIEAFNRNGVVVARAVVSHRIPEGTVFMYHAQERIVNVPGSEITGKRGGIHNSVTRIVLKP
THMIGGYAQLSYGFNYYGPTGNQRDEVVVVRKRSQVDWLED
>gnl|CDD|444038 COG5014, TM0948, Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General function prediction only]
MIRGYDPIKLGELVEKRVARGEGGVEYRKYYRFRGGRWYGGIATADVVGCNLRCGFCWSWRFRDFPLTIG
KFYSPEEVAERLIEIARERGYRQVRLSGGEPTIGFEHLLKVLELFSERGLTFILETNGILIGYDRELARE
LASFRNIVVRVSIKGCTPEEFSMLTGADPEFFELQLRALKNLVDAGLEPGREVYPAVMLSFSTEESIRKL
IERLAEIHPALVENIDPEYVILYPHVVERLRRLGLKPRKAYTPDGIPEFMI
>gnl|CDD|444039 COG5015, COG5015, Pyridoxamine 5'-phosphate oxidase (PNPOx-like) family protein [General function prediction only]
EEILKFLKENPVFYLATVDGGQPRVRPFGFVFEDEGKLYFCTSNQKDVYKQLKANPKVEICAMKKDGEWI
RLSGKAVFVDDRELKEKILEENPFLKEIYPSADDPIFEVFYLEDGEAEFYDMSGNPKKIE
>gnl|CDD|444040 COG5016, OadA1, Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]. Pyruvate/oxaloacetate carboxyltransferase is part of the Pathway/BioSystem: Urea cycle
MKKVKITDTTLRDGHQSLFATRMRTEDMLPIAEKLDEAGFWSLEVWGGATFDSCIRYLNEDPWERLRLLR
KAMPNTPLQMLLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQ
GAISYTISPVHTVEYYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEALDIPIELHTHATSGL
APATYLKAIEAGVDIIDTAISPLAGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKF
EPEATGVDPRVLVHQVPGGMLSNLVSQLKEQGALDRLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVL
NVLTGERYKMITKEVKDYVLGYYGKTPAPIDPEVRKKALGDEEPITCRPADLLEPELEKLRKEGLAKSDE
DVLTYALFPQVAIKFLKGRAAGEARPDAPLAELAAVEEVVVVAEGVVVVVVVGGGAEGVVVVVVGVPGAG
AVAVVAAAAAVAAAAAAAAAAAAAAAGAAVKKVVAVGGAVVVGVEVVVVV
>gnl|CDD|444041 COG5017, COG5017, UDP-N-acetylglucosamine transferase subunit ALG13 [Carbohydrate transport and metabolism]
MIFVTVGTHQLPFDRLVRWVDELAAEGIIDEEVFVQTGHTTYVPRNAEAVPFLPPDEFQKLIAQARLVIS
HAGMGSILTALKLGKPFILVPRLARYGEHVDDHQLETARALEKLGGIIVVEDPADLEAALDEALALKSPE
PFSVPSPARGALVDFLRAFITELL
>gnl|CDD|444042 COG5018, KapD, 3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction mechanisms]
MMKYLVIDLEATCWDGKPPPGFPMEIIEIGAVKVDENGEIIDEFSSFVKPVRRPKLSPFCTELTGITQED
VDSAPSFAEAIEDFKKWIGSEDYILCSWGDYDRKQLERNCRFHGVPYPFGDRHINLKKLFALYFGLKKRI
GLKKALELLGLEFEGTHHRALDDARNTAKLFKKILGDKRLP
>gnl|CDD|227352 COG5019, CDC3, Septin family protein [Cell division and chromosome partitioning / Cytoskeleton]
NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIDDIRAEGTSPTLEIKI
TKAELEEDGFHLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYF
IRPTGHGLKPLDIEAMKRLSKRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDE
SLEENQDLRSLIPFAIIGSNTEIENGGEQVRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTE
NLLYENYRTEKLSGLKNSGEPSLKEIHEARLNEEERELKKKFTEKIREKEKRLEELEQNLIEERKELNSK
LEEIQKKLEDLEKRLEKLKSNKS
>gnl|CDD|227353 COG5020, KTR1, Mannosyltransferase [Carbohydrate transport and metabolism]
KKIRRFLLLIPRSVLYVLFLVSLFAIYVFYVGEPSSIQSQDEPNELPSSEGDAIRNRDSKFSINCYNDEL
LYLEAPSYPRENATFVMLARNSDLEDVLSSIRSVEDRFNKNFHYPWVFLNDEPFTEEFKEATSDITSGLT
EFGLIPKDEWNFPEWIDEDKAAESLDDMADEGILYGGSESYRHMCRFFSGFFYRHPLLDEYDYYWRVEPD
VKLYCDIDYDPFRYMKDNNKVYGFVISLYEYEETIPTLWRTTKKFIKKNPGYLSENNLWKFISNDDGIDY
NLCHFWSNFEIANLDFFRSEAYRKYFDYLDKSGGFFYERWGDAPVHSIAASLFLDKDQIHYFRDIGYHHS
PFHHCPLNAGTRLGCRCNCDPGKDITDSSGSCLGKWFNLLNGDKPEGWE
>gnl|CDD|227354 COG5021, HUL4, Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]
DLRVGGLLLEDLSCRLFSELFRSNSSVRAEFDLSKDESGVRNSLDYGAAGNKNMSLSDEKGLVRSSIAAL
DGLQNRDCLRSLDPLSVLSVDGLQTSETSFRSSALNPYVNEFLCENDVRLSSSITIQVSDESKQNVIEDV
FSGLENLGSVDVLSTEATKGIDFLEILITRDFLFSSCSLNSDFLKIISGSSVKSRKLAVSNVEKSEPDNV
LFGLPYRSALTMRTNFLKLDTGNLSGEVQALLARYISIKLVIKKLYLGPGPDASSRISTLIIRLSNTNLN
RRLSYILSHSSFEDSLLRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSS
IKDLPHQVGSNPFLEAHPEFSELLKNQSRGTTRDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRRE
QLGRESDESFYVASNVQQQRASREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIR
RIKEDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLT
REWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAF
YKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNEN
KKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTAYHGY
TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTC
FNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL
>gnl|CDD|227355 COG5022, COG5022, Myosin heavy chain [Cytoskeleton]
MSTTNAEVGSGCWIPDEEKGWIWAEIIKEAFNKGKVTEEGKKEDGESVSVKKKVLGNDRIKLPKFDGVDD
LTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAE
EAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSIEKQILATNPILEAFGNAKTV
RNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNP
KDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNGAAIFSD
NSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSL
DHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQ
PCIDLIEKKNPLGILSLLDEECVMPHATDESFTSKLAQRLNKNSNPKFKKSRFRDNKFVVKHYAGDVEYD
VEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIESKGRFPTLGSRFKESLNSLMSTLNSTQPHYI
RCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTWKED
TKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKR
IKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEF
SLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIE
LKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKS
TILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQK
LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVA
QMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDE
KSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEK
LLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFNALRTKASSLRWKSATEVNYNSEELDDWCREF
EISDVDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNLKSRYDPADKENNLPKEILKKIEA
LLIKQELQLSLEGKDETEVHLSEIFSEEKSLISLDRNSIYKEEVLSSLSALLTKEKIALLDRK
>gnl|CDD|444043 COG5023, COG5023, Tubulin [Cytoskeleton]
MSTICKICMKRADEWDGDSLVEHVRNAHGDEPASVEQVYPDLEAEVFAEPEPDEPDAEDGLGSGAGPGSV
DAGGSRGPAETPSDDLMDDPYGKKWYLVGVGGAGNNILDAILLRRDTLEANNERRARIWNGGLAGYGPLN
TNVSELEQTYYAQEEKEYSRNDLLPNCIIGFGKHDYAGAGRRWDEGKKRFEADFADDGDPFRERWDMRKQ
LIQDSQAVMFVHSVTKGTGCGSTPVLAEKIREEVLEHDLVVPKALISSIVIPSEGGWDPVIGGAAAVNGV
VGLARQSKYVDAIIPFDNKRLEEVAADIEPRIDKLHEYNPPDYRGMNLPLVAFLEAFTMSRARETEWDRS
NLEILVRNALYQNWLATFDPTTAWGGTFLVYGPEEKMEEVTEFVSDGTLANIIGKENFLDAINVSGNESV
DIHVFQLVTPDLDDVGLWGTLWNPLVPSLEEMYDHARRIKKEGIKQRFNIEDDRMIFIKIPISCLEQANM
T
>gnl|CDD|227357 COG5024, COG5024, Cyclin [Cell division and chromosome partitioning]
HSESLQEYHQEISRNVAVQSSKNKPNVKLILQQPEMNILETRSAIVDFLNQLSTVTRLSNGINFHSSKST
KLVVGTCLWLAKKTWGIISSGESNERARIPRLSECNLDSILFIQMTLNEDSYEPMIDYILKKDENSLSPY
ELDENQLALDEKQAESKRESQSWQDLDATDQEDPLMVPEYASDIFEYLLKLELIDLPNPNYLIKQSLYEW
SMRSILVDWLVEVHGKFGLLPETLFLAINIIDRFLSSRVVSLEKYQLVGISALFIASKYEEVNCPSIKDL
VYATDGAFTRDDIIRAERYMLEVLDFNISWPSPMSFLRRISKASDYDIFSRTPAKFSSEISPVDYKFIQI
SPSWCAAAAMYLSRKILSQNQWDRTLIHYSGNYTNPDLKPLNESNKENLQNPSVHHDAIFPKYPSPTFGK
ASSPTGEWIRSNSSNDSSLL
>gnl|CDD|227358 COG5025, COG5025, Transcription factor of the Forkhead/HNF3 family [Transcription]
SSSLSEQAMNDLEREKQMIPKKSITVSKLKEVVINGKSHNVSSVLSSPKAPTRVSLDYSNSLNRSVGSEE
IQAYAKLAGSNWTYYVPPYSYATGRGLAILNSPDKPLTLSKIYTWIHNTFFYYAKVVSRWQNSIRHNLSL
NDAFIKIEGRNGAKVKGHFWSIGPGHETQFLKSGLRLDGGGKQMMFTLPSSTEIKITYSSTHSMPLLESN
DSLNSNNERELLDIIKSSALIRIPADSSSNLDVSLGHHISQPSTHTPVLDNHSSGEENISRINNSSQIDS
PTPNYRMSSIDSSVNPSRLANNKDEGRKGSKSSPVPKDAAPPSTLSDLSADVNRTSKPAFSYANSITQAI
LSSPSGKMTLSEIYSWISSNLPYYRHKPTAWQNSIRHNLSLNKSFEKVPRSASQPGKGCFWKIDYSYIYE
KESKRNPRSPKKSPSAHSVHQKLSLHVNDLYQSPATSDIASSSSQVNSQPEFISTQIHSSKGVSNVDLTE
QDSQKEASKGNFLDDSGSLSPNTNEINSFSLNTTDSQQKQSPSHNAPTNNSLNEMASKNSNSQTQASNSN
ENVAAVKAILDASAQMEKPYDLSQAATPTKATESASVRQAPNPPPHQNLV
>gnl|CDD|444044 COG5026, COG5026, Hexokinase [Carbohydrate transport and metabolism]. Hexokinase is part of the Pathway/BioSystem: Glycolysis
MKKLLVDAFLKRHGFDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYLGLPTGVKETGPVIALDAGG
TNFRVALVRFDGEGTFEIENFKSFPLPGTSSEITAEEFFDFIADYIEPLLDESYKLGFCFSFPAEQLPDK
DGRLIQWTKEIKTPGVEGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDGYSGYIGSIL
GTGHNTCYLEPNAPIGKLPAYEGPMIINMESGNFNKLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGEL
CRLTLREAAAEGLFSPGFSEVFETPYSLTTVDMSRFLADPSDEKEILSQCLEAGSEEDREILREIADAIV
ERAARLVAATLAGILLHLGPGKTPLKPHCIAIDGSTYEKMPGLAEKIEYALQEYLLGEKGRYVEFVLVEN
ASLLGAAIAAALNE
>gnl|CDD|227360 COG5027, SAS2, Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]
NKIKDIIIKSKVASEKDGEARKAEILEINTRKSRIKFYVHYVELNRRLDEWITADLINLGAAISIPKRKK
QTEKGKKEKKPKVSDRMDLDNENVQLEMLYSISNEREIRQLRFGGSKVQNPHEGARVKNINEIKLGNYEI
EPWYFSPYPEEFSDLDIVYICEFCLKYYGSQTSLVRHRKKCSLQHPPGNEIYRDKYISFFEIDGRKQRLY
CRNLCLLSKLFLDHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEQDYNLACILTLPPYQRRGYG
KLLIDFSYLLSQKEGKVGSPEKPLSDLGLLSYRAYWSEIVAKLLLKMDKEITDINEISKETGMSTDDVIH
TLEALNILREYKGQYIISLNSDKLHNYLRLWSKKRRRINPDLLLW
>gnl|CDD|227361 COG5028, COG5028, Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion]
MSQHKKGVYPQAQSQVHTGAASSKKSARPHRAYANFSAGQMGMPPYTTPPLQQQSRRQIDQAATAMHNTG
ANNPAPSVMSPAFQSQQKFSSPYGGSMADGTAPKPTNPLVPVDLFEDQPPPISDLFLPPPPIVPPLTTNF
VGSEQSNCSPKYVRSTMYAIPETNDLLKKSKIPFGLVIRPFLELYPEEDPVPLVEDGSIVRCRRCRSYIN
PFVQFIEQGRKWRCNICRSKNDVPEGFDNPSGPNDPRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYV
FLIDVSFEAIKNGLVKAAIRAILENLDQIPNFDPRTKIAIICFDSSLHFFKLSPDLDEQMLIVSDLDEPF
LPFPSGLFVLPLKSCKQIIETLLDRVPRIFQDNKSPKNALGPALKAAKSLIGGTGGKIIVFLSTLPNMGI
GKLQLREDKESSLLSCKDSFYKEFAIECSKVGISVDLFLTSEDYIDVATLSHLCRYTGGQTYFYPNFSAT
RPNDATKLANDLVSHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFNRSSDLCAFSTMPRDTSLLVEFSIDE
KLMTSDVYFQVALLYTLNDGERRIRVVNLSLPTSSSIREVYASADQLAIACILAKKASTKALNSSLKEAR
VLINKSMVDILKAYKKELVKSNTSTQLPLPANLKLLPLLMLALLKSSAFRSGSTPSDIRISALNRLTSLP
LKQLMRNIYPTLYALHDMPIEAGLPDEGLLVLPSPINATSSLLESGGLYLIDTGQKIFLWFGKDAVPSLL
QDLFGVDSLSDIPSGKFTLPPTGNEFNERVRNIIGELRSVNDDSTLPLVLVRGGGDPSLRLWFFSTLVED
KTLNIPSYLDYLQILHEKIKS
>gnl|CDD|444045 COG5029, CAL1, Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism]
MSLGVLSRLEGGSSKSTADFTDSHLDYLRASQNPDGGFAGRSGPSDLYSTYYAVRTLALLGESPKWRDRV
ADLLSSLRVEDGGFAKAPEGGAGSTYHTYLATLLAELLGRPPPDPDRLVRFLISQQNDDGGFEISPGRRS
DTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSPEGGFAYNTRIGEADLLSTFTAILTLYDLGAAPKL
VDDLQAYILSLQLPDGGFEGAPWDGVEDVEYTFYGVGALALLGALAERG
>gnl|CDD|227363 COG5030, APS2, Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion]
MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIEGKNEKIVYRRYATLYFVFG
VDNDDNELIILELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDA
ESTDDKIGRSLS
>gnl|CDD|444046 COG5031, COQ4, Ubiquinone biosynthesis protein Coq4 [Coenzyme transport and metabolism]. Ubiquinone biosynthesis protein Coq4 is part of the Pathway/BioSystem: Ubiquinone biosynthesis
MQATPSLLTRLLRPLRALRAFRALLRDPEDTGQVFDLIDALLDSRAYALLVERLRRSPEGARLLRERPSL
PEIDLEALRKLPEGTLGRAYADFMEAEGLDPDGLVAESEADDDASYIGARLRETHDIWHVLTGYGTDVLG
ELGLQAFTLAQLGSPGALLILAAGLLKTLLGAPEDLAPLLRAIARGWRLGRAAKPLFAQRWEELWERPLD
EVRARLGIPPPTVYRSVHDILR
>gnl|CDD|227365 COG5032, TEL1, Phosphatidylinositol kinase and protein kinases of the PI-3 kinase family [Signal transduction mechanisms / Cell division and chromosome partitioning / Chromatin structure and dynamics / DNA replication, recombination, and repair / Intracellular trafficking and secretion]
DRLAQIIYALPSLLKDCFTEILLRKSDVRSSLFDLLHVSFLDYKEKDERLSNVNDLVRNSTQSLLNTISN
LIKIVKFVLPLKSFFLSPIFAKLRALPMTKILCISADTYCLSLSIKALADDESLTTILKTIRELLSKFLL
RLRLLFLFIGLLAQKFSEAQSKLFFKLLLSILKEILSDAYEALLNDLLENLKSLKETLQNRLLPLLFNIS
DGNYFKVEIGRKLLDHLNALGQILDCQKIAKITKSFRSLPVIIKKFLNLLLIKVSYYLPSFFRLSLLSYL
DHFETDLFKTFLVTSCFLFFVDEICKPESEHLAEEVSEKLSKFLTIEIIDSFPEIRISALSSLLVIFDYH
LALPDAVRLLFGESNDKVFLISELALDSTGRLLRVLPARVLPSLFEFLLSLLTVLKISGLILEFEISAQL
LCNLIRSSNQLLTSLISPYFLFILPKCIDSSNSEISYRVENLGELKDILGLDRITDYQALSLRLIIVSIQ
LRSFVFKREAINQIFKQLASIVIKPFLDYPKRLDLPIKIVTVVYVALLRRPTEKLSGVLGSIDKYSHIES
EEMSSSDFPWTKNPVGLQLLAVYGFIRSIDDLYFTVSDPTLIEILKLPVLSIVHSAIIEAIMLIKLSLGS
ESSQFEDLNPSFLYIFSNNSISDILFYFQNFLELIVIAFFPLIRSEIIGIVLISSLFSKTWILLKLLLIA
FISKLISALQGELKMLAPTLFTLFLVLVERYLDVEYSSVSFKLLLVILVYFGGNLESLVLLILDLIVMLV
EYTELGLQESIFIERLSQFFKFKNLSENASRLLPPLMDNLSKSHELRCVSEDDVSALLIQLLTDRVICFI
PVINSSLGDSRRIFLSLLAQLLDDSLKEESLPYNLNVDRGTDLREFFQTVKSKAEVLSMLPFVQSILFEA
WNRVDFLLKDFWQEELDNLLVALLKELPFMALRDCSILSDLYFMLGRELWNSVSFECWLELMNSYKRLLI
KSLKSKLHLPTIPILILQMLLDSKNLTEFTEHQLKNLPLPSLSIGFYESLCSFLAKLLHDEELYFFPLLF
VSSLETLLSVNYHINQLDLRPNILKHFGSFVRFQLKPHLVKYLQRWYEALNRYFELLSKGDRLFAISFTK
LRNVDALGKLELYSSLAEIDMFLSLHRRRKLLETLVATAYEQVGEWYKAQQLYEVAQRKARSKEFPFSLQ
YLYWHINDIDCADKLQSVLAELSLVTGISELLLEESWRRALFSNIKDSLESELEEIIDGMYKSNEDFGAL
MLLSLSAELWDKILEGRSSCSKSIKLSLNIWLDLSIVVSPKDEPELFIKFVELCEASSIRSKLLEKNIQE
LLEKLEEIKSPLGTLRDRLPPPWALLDLKRLLATWRQNAFLRINPELLPLLSSLLNLQSSSLSKQLVSRG
SSESAISINSFASVARKHFLPDNQLKKIYQLSNILISEAFLLLRYLLLCRLGRRELKAGLNVWNLTNLEL
FSDIQESEFFEWGKNLKLLSIIPPIEEIFLSNALSCYLQVKDLLKKLNLFELLGSLLSAKDAAGSYYKNF
HIFDLEISVIPFIPQLLSSLSLLDLNSAQSLLSKIGKEHPQALVFTLRSAIESTALSKESVALSLENKSR
THDPSLVKEALELSDENIRIAYPLLHLLFEPILAQLLSRLSSENNKISVALLIDKPLHEERENFPSGLSL
SSFQSSFLKELIKKSPRKIRKKFKIDISLLNLSRKLYISVLRSIRKRLKRLLELRLKKVSPKLLLFHAFL
EIKLPGQYLLDKPFVLIERFEPEVSVVKSHLQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLM
NKILKKDKETRRRDLWIRPYKVIPLSPGSGIIEWVPNSDTLHSILREYHKRKNISIDQEKKLAARLDNLK
LLLKDEFFTKATLKSPPVLYDWFSESFPNPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSS
GHVIHIDFGFILFNAPGRFPFPEKVPFRLTRNIVEAMGVSGVEGSFRELCETAFRALRKNADSLMNVLEL
FVRDPLIEWRRLPCFREIQNNEIVNVLERFRLKLSEKDAEKFVDLLINKSVESLITQATDPFQLATMYIG
WMPFW
>gnl|CDD|227366 COG5033, TFG3, Transcription initiation factor IIF, auxiliary subunit [Transcription]
MAPVKRTERLKTQRVIIPGEAKPLGNEERFPVRHTHIWLVFVRAPGKEDIATIVKKVIFKLHPTFSNPTR
TIESPPFEIKETGWGEFDIQIKIFFAEKAGEKTIHFYLHFGDEPYAVDEPVDIPVNRPDLTSELSKSGEV
ESVYKREKRFNEPNIQALKLLNGAKMKLAIGLHKLREDDLVFVVQLVQDPIMAVLNLIEKGEFKIDLYKL
PSDLLHKLESVKAKN
>gnl|CDD|227367 COG5034, TNG2, Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics]
ADLFPGLNDITDHLANVPSETDIRFTELSEIDAKVCDIIKNLRQMISILKKIIDLDSQTYEEVEDGLLKE
IRELLLKAIYIQKEKSDLADRAEKLLRRHRKLLDDRIAKRPHEKVAARIENCHDAVSRLERNSYSSAARR
SSGEHRSAASSQGSRHTKLKKRKNIHNLKRRSPELSSKREVSFTLESPSVPDTATRVKEGNNGGSTKSRG
VSSEDNSEGEELYCFCQQVSYGQMVACDNANCKREWFHLECVGLKEPPKGKWYCPECKKAA
>gnl|CDD|227368 COG5035, CDC50, Cell cycle control protein [Cell division and chromosome partitioning / Transcription / Signal transduction mechanisms]
EVFRRKDKKAIVSKPSLLKSRRPPNTAFRQQRLKAWQPILSPRTVLPLLFLIGIVFAPLGGGLLVASSSV
QELTIDYTDCMTLASDEFSDIPSEYIQFHFKKKVNVLPQWRFSTDEEDDFQKCQIRFTVPSDMKKPVFIY
YRLTNFYQNHRRYVKSFDEDQLRGEALKSDDLKSNCKPLSYNEDKIIYPCGLIANSMFNDTFSSLLTGIE
DTSNYNLTTKGIAWESDRHRYKKTKYNASDIVPPPNWAKMYPDGYTDDNIPDLSTWEEFQNWMRTAAFPK
FSKLAMRNVNDVLPPGTYQLNITLNFPVLEFNGTKSIVLTTNSVIGGKNYFLGIVYLIVGGICALLGLIF
LIKWLFKPRKMADHSYLNWNME
>gnl|CDD|444047 COG5036, COG5036, SPX domain-containing protein involved in vacuolar polyphosphate accumulation [Inorganic ion transport and metabolism, Intracellular trafficking, secretion, and vesicular transport]
MANPEVFNRYELKYLIPEEQADALREALKTYMEPDKYSDESGFYTIRSLYFDTPDLELYRESIEGPKYRE
KLRLRSYGDPTPESPVFLEIKKKVDGVVYKRRAPVPLEEARAFLKGGSLPAHDNPSNKQLLREIDYFLAR
YNLRPKVLVAYDREAFAGKDDGDLRITFDTNIRFRDDDLRLDKGEHGEPLVPPGYVLLEIKYDGRMPLWL
SDLLSRLNLFRTSFSKYGNGYKALLLVARSI
>gnl|CDD|227370 COG5037, TOS9, Gluconate transport-inducing protein [Signal transduction mechanisms / Carbohydrate transport and metabolism]
MDIMPTFYGYIETEEDALLLFQAVRLGYLPRIERRLTPEERELIRSGSIFVFDEEESGIKRWTDGKSWSP
SRISGKFLVYRELPKKNSFEPSHSKLSKNPLLKSTFSARTAGDRSFIINWDTKSSLNKKTIAYLLDEKSV
HVSAYRPSMFPPFSLIKIKFSNQDDVAKKAYPNSLSTPFPSERTVTPSKEDIYSRSRLPFPSYQDLSPEI
KNHPLNIIPSSVVAEKMTQSMNINDVNKKQQCLYNNNY
>gnl|CDD|227371 COG5038, COG5038, Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only]
ASTKQQHYRSSDNYSGNRPIPTIPKFFRSRGQRAEKKEEEQEMQPEDEKLFAPIAQRTVQIADVNFQGAK
GIDDLSFTVPKQSIESSSPEKSDVDTSNTRPSVSRELHKDDYVGPDQDGGWQRKVELSSEQELSDFTDMS
ILLNYILKKFYGDWYQSVAIVLIGSVASWIFGYLGFSFASLFFIILVTMYVYRTCIKRVRRNIRDLVQQE
LSEEKLENDYESVEWLNTFLQKFWPIIEPSISQQVVDQVNQQLAEAIPSFIDALALDEFTLGSKPPRIDG
IRSYPSTESDTVVMDVDFSFTPHDISDVTATSARASVNPKISLVVKKGKSFGSFTLPILVEDLFFKGRVR
VRVELMSKYPFIKTVSFQLLEVPEFDFILVPLGGDFFGVDIFAIPGLSRFIQEIINSTLGPMLLPPNSLT
IDISQIMAGDSGTAIGVVEVKIKSAEGLKKSDSTINGTVDPYITVTFSDRVIGKTRVKKNTLNPVWNETF
YILLNSFTDPLNLSLYDFNSFKSDKVVGSTQLDLALLHQNPVKKNELYEFLRNTKNVGRLTYDLRFFPVI
EDKKELKGSVEPLEDSNTGILKVTLREVKALDELSSKKDNKSAELYTNAKEVYSTGKLKFTNHPSWNLQY
NVLVTDRKNSSIKVVTFDVQSGKVIATEGSTLPDLIDRTLDTFLVFPLRNPKGRIFITNYWKPIYNAGGS
SSKTVYDTPIGAIRVSVRKANDLRNEIPGGKSDPYATVLVNNLVKYRTIYGSSTLNPIWNEILYVPVTSK
NQRLTLECMDYEESGDDRNLGEVNINVSNVSKKDEDSALMETIDGAEETGKLSLTGKKVKGTITYKCRFY
PAVIVLSLEEVRYVDKVSSEKRKSEKRKSALDEKTISLVDKEDSVEESIEVEELTDMYSLKPKLDLNEAL
QYKSGVLGIQILSGELPDPGQYLQIFFDDASHPQIVSSKAPTRGERNGESGDTFIRELEYSETTFRVTKN
AKKSDKVVCEVTLPTLDLVSNAYEKPSSLNFPGSAKVLVQVSYTPVPVKLPPVEMVENSGYLTIMLRSGE
NLPSSDENGYSDPFVKLFLNEKSVYKTKVVKKTLNPVWNEEFTIEVLNRVKDVLTINVNDWDSGEKNDLL
GTAEIDLSKLEPGGTTNSNIPLDGKTFIVLDGTLHPGFNFRSKYALNVSRKEGILGDIAKKVGTGLKAGS
TTVGSVGVKAVGGVADGVKGGKGIISGGKKISEEKMF
>gnl|CDD|444048 COG5039, EpsI, Exopolysaccharide biosynthesis protein EpsI, predicted pyruvyl transferase [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]
DASLIESLKSKLHDILELLPDKSDVALLDYPNHGNIGDHLIWLGTLAFLKDLGPRIRYVASLTDFSIDAL
KRKIPPDDIILLHGGGNFGDLYPEHQNLRERIISTFPDNRIIQLPQSIYFSDPEELKKSARIFNAHPNLT
LFVRDRRSYDLAKEYFPKCKVFLCPDMAFQLDPSDPRRAPRSGILYLLRTDKESVLDADPRILPGNVTVT
DWPDIERAKDRAIRLLGKLERLTLLLRPLNRLVDRIWHRLRESLLKRGLRLFSQHELVVTDRLHGHILSI
LLGIPHVVLDNSYGKNSSYYETWTKDIPFVKFVESLDEVEAAARELLRSS
>gnl|CDD|227373 COG5040, BMH1, 14-3-3 family protein [Signal transduction mechanisms]
MSTSREDSVYLAKLAEQAERYEEMVENMKLVASSGQELSVEERNLLSVAYKNVIGARRASWRIVSSIEQK
EESKGNTHQVELIKEYRKKIETELTKICDDILSVLEKHLIPAATTGESKVFYYKMKGDYYRYLAEFSVGE
AREEAADSSLEAYKAASEIATTELPPTHPIRLGLALNFSVFYYEILNSPDKACHLAKQAFDEAISELDTL
SEESYKDSTLIMQLLRDNLTLWTSDAEYSAQEDEGQQQQAQENQQPEPKESTEGEAKA
>gnl|CDD|227374 COG5041, SKB2, Casein kinase II, beta subunit [Signal transduction mechanisms / Cell division and chromosome partitioning / Transcription]
TMENSLEDDSDNLSDDDSDSSEYDEWIDWFCSRKGNEYFCEVPEEFIEDRFNLTGLSREVPHYSEVLDLI
LDKLAPSNLENDEVDIIEESARQLYGLIHARYIITKSGLQAMLEKYKSREFGACPRVYCNGQQVLPVGLS
DIPGKSSVKLYCPSCEDLYLPKSSRHQSIDGAFFGTSFPHMFLQTFPELFPKRSCERYIPRIFGFRIHSH
ADTGPRMEWLRQYLSTELDGEDFESESETPAT
>gnl|CDD|444049 COG5042, NUP, Purine nucleoside permease [Nucleotide transport and metabolism]
MRKTLRLLLLALLLALALAAVAAAAAAAPIPVKVVVVTMFEIGEDTGDKPGEFQLWVEREKLTQTIPFPG
GYHDVRYNPDTGVLGIVTGMGTARAAAAIMALGLDPRFDLSHAYWLVAGIAGVDPQDASIGSAAWARYVV
DGDLAHEIDAREIPKDWPTGYFPLGTKRPYELPRPPAPGGEVYTLNPGLVDWAYELTKDVKLPDTPALQA
LRARYVGYPNAQKPPFVLKGDTLAASTFWHGKLMNQWANDWVKYWTDGQGNFVTTAMEDTGTLQALTYLA
KAGRVDKNRVMVLRTGSNYTMPPPGLTAAESLAAEYSEGYSGMLPALEAAYRVGSVVVRELLTHWDRYED
TLPGAA
>gnl|CDD|227376 COG5043, MRS6, Vacuolar protein sorting-associated protein [Intracellular trafficking and secretion]
MLEGLLANLLNRLLGSYVENFDTKQLNVGVWGGDVSLHNLRIKPSALDKLGLPIEVTSGLIGTLTLEIPW
SSLKNKPVEIYIEDIYLLISPQAKNSLTREELPQSQQALKQRQLDSWEILRETLEESSSSPNISRKQSFI
ESLITKLIDNIQIYIEDIHLRFEDNLSADLEGPYSFGLTLYSLRATSTDASWTEYFVSTDSSCIHKLITL
DYFSIYWCEISPCITTEDIDSYLENFQPMIAEKSPAYNEYILKPVRGTAKVSINKLPTDEIPRLRGQLSV
EEFSISLSDHMYYSLLGVLDYLQVVMKQQKFLKYRPKSTPKEKPLEWFKYIILVVLDSIHEKRYHWTWKY
FKERCEDRRAYMKIIRKKYLNEQLSADLSKELEKRELTYDLIKYRSRLFRSLAKRRNSIYLKPQTHKLQG
WFSGLWNGKPQAQDEDTLASTDKTAAELTDQEQKDFFSEIEPVGQLYSDTVNLDVEVSIAKGSFVIQKHI
RKINLISQRFENFKSKFSLNKLDLFDGATNPELKPYRSIRNKPKVRESESLQEIEEESRTHLFASFEDSK
PDGKASSTLIIHLRTLVIFYNRVCILSVLKFFVPSRTKIEHVSEWVYSAAATVMTLTRQTRASLDSALEM
HKTSNVTIDLQAPLIVFPEDCTDPKSPTLFLDAGRISIHSQLVEDAIIKKFRELQTLENLMYDRFTISLF
NVRCLIGPDYEGKRELPKGKCDYHILKELKLEINVEISILPKATNLPKIKVSGHMPHASLMFSDVQYKVI
INLMSNILPTISVDEINGDYQQFSSASLPPPFFDIKDNFQIENHANEQTAAKFHAQQIFAFYFKVDYFIC
SGLDSRSENYLVPVLRARLEFYFDLVARKFNLRVTSNSNDIVDKEFTYPSSLCDNLLSRSSPKPKNNFDD
TVFIEYKSIDYDVLDSVYEEVDTTIAVVLSDLILNLEPTSFLTLIDFIRSTFTSPNDEYMIGEDPELTRK
ISDVENIKIEDANVRLDNNDIFLYDCIQLFATVLSYGAFMHMEEREKFFLQLRLMDLELKNHEKSNNPDS
TIVKIDDNKLFIFKYESYDIPDPITDCDCVLDISTGSLHFYFIESYFNFLSKFKRFKVSFSSIRYAAYYK
AYGNKVSNNYKFELRIKHPIVQFPDVLGERNCRMQLIIKPGSFYAFSKCPVVEKNSKLSIFSCELRKGEF
STAVPSSGHHDVLLEELNIHLDLTIDANPTTGENAYVFKATGDLDPVILNLCQSQHLILLDLIDVVTTFF
RIDSSFSTSENLPRELDSEFDRSGTPVKLKHSKKTVVETLDILFTFKLPKIRLNLYTGTFGIHGGDLTGL
HNILFFEIGLDYGFYSSGTVYAEFSIASFRIEDVNPIKDVVFLDVIEYSTNTHNLLVNGCLEYDSQGRLL
NLVLDIDKMFLNLDYLYSIWSIFVHWLRAYYSHLDYLVEQEYFNMGNPNQVACGEESYKLYRITIVDTTL
VFVRDASDMNSYAIPFFFGQFLVTQQSIFTVTANNMGIFACKMSETANINQLLDDFGIRFTISQHCSEKI
QIITTLDFDSLLLRISVNDFLLLQTILRRIYNFIYALYDKETTDEELEKRTKDGQLALNPDFLAASVPTA
QPSSVFGIRLCSEEFLINVDGIRLILISDLHDLPLLDINIKPFQVDLKDWSTELNANASLELFMNFFNFS
RSHWEPVLEPWKVGVHISRNDSKTAVHVFSREIADIVLTPRLIATLHFIFTKLISTPFPIERKCDAPYRI
VNYTQTAVSVWAQFENAADSVECVRHLPNNTSTPWKFEEWRQMQDVVSQDQDRVYIGVHVSNSKYESLRH
VRVNRVGEHLLLISYPRDELKHYMVVDVRLGEDNIKHITLRSPLLIINETQTEIEVVFCDSDGIQRSQIY
HISPEESCSLPIETAYLYSIRIRPVSEDKFNWSSQAISWKSLVDNQQSIVTCLRQHSRDNTWSTPSCKFV
GLHVVANDELYSLVIVNEHDLPLMKLDSGADLEVKGVLLLKGVGISLIDRKDQELAYMTNVGIGLRFIDS
KAYQTFSWECAWVQIDNQLVLGIYPVILYPTEISQEEKEIENHLLPSRKFAVVKDSDSAVTYDKYVTILL
QELSIELDEDLALAYLEKLKFPGSKYMDDKKFDDEIELPDIIINKSGSNIYFEFLHLQPTRLHISFSRSS
ESSGEDGKVVPSSNSYSDFYGMLAMTLGNINDAPVRLNSLLMDNARVSLPELFDLIASHYLQQVEYQIYK
ILGSADFLGNPVGLFETVSSGVSDLFYEPYQGRFLVDNSQEWGIGIAKGGNSFIKKTIYGVSDSVSKFTG
SISKGLSLVTSDPELQSSRRLVRRRNRPKGSVYGVTAGATSLYDSTSSGEKGLALEPIIGAATNGASGFV
KGLGKGILGLETKPLVGFLDLTSNDSEGIKNTTTVLDYHDIPRLRLPRYVWDDGCVAPYDLRESQGQYWL
KTLDAGKYPLDEYKFHDIINNVAVIISRDIHAIVTSKILILKDYIPSKAVQGPKIYSKESNEKLLFNLEQ
FDSGIDPSFVRSVKSNVEGAVPEKIKYCEAIL
>gnl|CDD|227377 COG5044, MRS6, RAB proteins geranylgeranyltransferase component A (RAB escort protein) [Posttranslational modification, protein turnover, chaperones]
MDEETLYDVIILGTGLRESILSAALSWDGKNVLHIDKNDYYGSTSASLTLTQLEKYFDECEKRPSKGGGD
RDLNIDLIPKFLFANSELLKILIETGVTEYLEFKQISGSFLYRPGKIYKVPYNEAEIFTSPLLSLFEKRR
VMRFLKWVSNYAEQKSTLQELYESKDTMEFLFEKFGLSGATEEFIGHGIALSLDLDIPAREALERILRYM
RSFGDYGKSPYLYPRYGLGELSQGFARSSAVYGGTYMLNQAIDEINETKDVETVDKGSLTQKAGKIISSP
TYFREDSKSVGQFYRIIRAICILLVHPVPFTTGLDSLQIIFPPFSLKRKNDIQVAGLGSGSEVCPEGYYL
AYISTIDETPTPEDEILAALELLGPSVEKFVDVEEIYQPDEDTNQVYLSDSVDESSHFESLTYEIKGIYK
RFTGTPLVFDQRQE
>gnl|CDD|227378 COG5045, COG5045, Ribosomal protein S10E [Translation, ribosomal structure and biogenesis]
MLVPKENRYKIHQRLFQKGVAVAKKDFNLGKHRELEIPNLHVIKAMQSLISYGYVKTIHVWRHSYYTLTP
EGVEYLREYLVLPDEGVPSTEAPAVSPTQRPQRRY
>gnl|CDD|227379 COG5046, MAF1, Protein involved in Mod5 protein sorting [Posttranslational modification, protein turnover, chaperones]
SPFYSNRRDSNSFWEQKRRISFSEYNSNNNTNNSNGNSSNNNNYSGPNGSSPATFPKSAKLNDQNLKELM
ITIVVYQMEYRSTNSDKKLFKAIENRCQEDLFALSSSKSSEYAFSLTQQSPFGPYLELSSRSKFNYLFAK
LNASYPDHDFSSEAPTDFSKRRSLGRFVEKPLGTLLSAGRLRFPYDFCWESIGSHRRLSDCEVLNYMPYS
ISTTHKNSDDVWEFVGFLENILHKRVSYLGLEIFSYENRMGPFEDCLWYFSFLFDDKKQRDFVMDNAFMS
DS
>gnl|CDD|227380 COG5047, SEC23, Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]
MNFEIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAPCKAVLNPYCHI
DERNQSWICPFCNQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTA
LKDSLIVSLSLLPPEALVGLITYGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPTKSGGFE
SKISGIGQFASSRFLLPTQQCEFKLLNILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCH
IVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQI
GIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANMEVKTSKNLKIKGLIGHAVS
VKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPAEAYIQFITTYQHSSGTYRI
RVTTVARMFTDGGLPKINRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKDDPS
SFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVL
LDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFI
VTEQGGSQARFLLSKINPSDITNKMSGGGSETILTDDVNLQKFMNHLRKLAVSKS
>gnl|CDD|227381 COG5048, COG5048, FOG: Zn-finger [General function prediction only]
ATLTSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCD
KSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDL
LSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYS
IPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDS
SSEKGFSLPIKSKQCNISFSRSSPLTRHLRSVNHSGESLKPFSCPYSLCGKLFSRNDALKRHILLHTSIS
PAKEKLLNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCK
NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGKD
>gnl|CDD|227382 COG5049, XRN1, 5'-3' exonuclease [DNA replication, recombination, and repair / Cell division and chromosome partitioning / Translation]
MGVPSFFRWLSERYPKIIQLIEEKQIPEFDNLYLDMNGILHNCTHPNDGSPPETEEEMYKAVFEYIDHIL
LKIRPRKLLYMAVDGVAPRAKMNQQRARRFRSAKDASAAALKAEPNGEEIPEEKDEIGNEIDTIDVEKKK
FDSNCITPGTPFMERLAKVLRYYIHCKLSSDPEWRNLRIIFSGHLVPGEGEHKIMNFIRSQKAQPSYNPN
TRHCIYGLDADLIMLGLSTHEPHFLILREDVFFGSKSRRKRKCTKCGRTGHSDEECKVLTHQPFYLLHIS
LLREYLEREFREPTLPFTFDLERILDDWIFLCFFVGNDFLPHLPCLDIREGAIETLTEIWKKSLPHMKGY
ITCDGVINLARLEVILAILGSFEDDIFKKDHIQEERKNESLERFSLRKERKEGLKGMPRVVYEQKKLIGS
IKPTLMDQLQEKKSPDLPDEEFIDTLALPKDLDMKNHELFLKRFANDLGLSISKAIKSKGNYSLEMDIAS
DSPDEDEEEFESEVDSIRKIPDKYVNIIVEEEEENETEKTVNLRFPGWKERYYTSKLHFTTDSEEKIRDM
AKEYVEGLQWVLSYYYRGCPSWDWYYPYHYAPLAADLSKLSDNDIKFELGTPFRPFEQLMAVLPARSKNL
VPEGFRPLMDDEKSPIIDFYPEEFKLDMNGKTASWQAVVLLPFIDERRLLSAVAVKYPTLSEEERKRNLR
GLDLLFSSNKKSDLSELFKDLYSKCKQKEYITMCSKESPYGLFGTVKLGAEGLAPNLLSLCPISFLSYPG
LMVFLEYSKNQSARLVIEDPKSTVTNKSIVLRGFIKPINVLWPYLRESKLVSLTDGSYSYRYNNSNDKKK
FGFITGSKKSSQLRMYSKRKAVKFIATVFPVTGLQPDSDGAYNKTFSPSYNSYPGQLVVESRVNGDERYY
ERNPPPIENEYPLNRKVGFLGDYNYGGENNIDGYYDNRRLKIT
>gnl|CDD|444050 COG5050, EPT1, sn-1,2-diacylglycerol ethanolamine- and cholinephosphotranferases [Lipid transport and metabolism]
MKLAAYSYSVRDRSLLLAFLERYFLRWLAARLPAWVTPNLLTASGALGALAIFVGYLASNGDTGAYLWLA
PVGLIVYWFGDSLDGSLARRTGISRPYGEFLDHSLDALATLLIVIGLGLSPYVRLDVALLALLGYLLLSI
HTFWETRVTGEFRLGYLIGPTELRLILIALTAAMFS
>gnl|CDD|227384 COG5051, RPL36A, Ribosomal protein L36E [Translation, ribosomal structure and biogenesis]
RIMAPGLVVGLNKGKKVTKRQPPERPSRKKGQLSKRTEFVRSIVREIAGLSPYERRVIELIRNSQDKRAR
KLAKKRLGSLKRAKAKVEELTSVIQSS
>gnl|CDD|227385 COG5052, YOP1, Protein involved in membrane traffic [Intracellular trafficking and secretion]
MSGQLVNISVAMLVLDNTLQAFPILREIENLYNRYKKYFMAGASFLYLLNLFSTVLGFGLILTNVAGFSL
PAQLSLVAFYTLNFMDDTQLLTYWMVFGFLSAIEKYSGAILSKVPFYWTLKNVFLLWLLLPRTEGARIIY
DDIIAPDVSDHGFRTIEKTVKNGTKASAAVASSLEKKTAADVQESG
>gnl|CDD|227386 COG5053, CDC33, Translation initiation factor 4E (eIF-4E) [Translation, ribosomal structure and biogenesis]
MSTEEVSKKFEENVSVDPTTKTPRTVLSDSAHFMNKHPLAFHWTLWFLKPPEDGLESWSDLLKSIITFET
VEEFWYILHNISDASRLPRKSDYNVFREGIRPEWEDEANMNGGKWSFQLKGKGCDRLDELWLRTLLAAIG
ETLDPTGSEIGGVVGNMRKGFYKLAIWTRNCNNKDVLGAIGNEFKQVLELSDVETLEYKAHESSKLGSYH
AKTRMSL
>gnl|CDD|227387 COG5054, ERV1, Mitochondrial sulfhydryl oxidase involved in the biogenesis of cytosolic Fe/S proteins [Posttranslational modification, protein turnover, chaperones]
MKRNRDKEGRVIIYDAAGLPCIICNFFSSFRDVDGKPFSPEIKSLPDNVQLAAAEKNDGEGKERKPITMM
STKHDNPDVEELGRSSWTLLHTVAANYPARPTPQQRDDLRSFLFLFSITYPCGECSKHFQKLLDVYPPQV
SSREAATTWACEVHNKVNEKLGKPKFDCDTWNERYDCGCDT
>gnl|CDD|444051 COG5055, RAD52, Recombinational DNA repair protein (RAD52 pathway) [Replication, recombination and repair]
MTFSNPQRRILEQPLKPEQIKTREGNGEELSYIEGWNVIQEANRIFGFADWNRGTLENVCHETLQNNDEV
ICLYETKVRVTVRSDDGDSIIIREGFGTGEANSSSDAHEAAIKTAETDALKRAATTFGNQFGLALYDDNR
QNDFLRGAVNGGLVVRGDLLEYTIYFLSIVEGDASKLKICDVIPTYTTFIPTAFNGSTPLDGGLSTANLG
IAIAADSTNYPKNPTAYITNVKDSDRGETFSALETPPIACSRSNNNGAVVVNIVNLDNVNQDIDPTHLVF
QTQTKPTNSYGFIRFKVKVR
>gnl|CDD|227389 COG5056, ARE1, Acyl-CoA cholesterol acyltransferase [Lipid metabolism]
SKPRIRIRSPLSDISSMIADTSFKPRPSLLDALPNCPLETTFKGPSLEKKIKNLQLRKSKVRAAYTVKTL
SPTPSIVARPYQRNASNFSGFYVLFWMAVARNAPSASPRNYSSHGLSVHGLEIIKYMTSNLFTLASLDLA
MALLSFFVFGIQNLREKGFLRWLPLGTLSLSICELFFLTIFMVLVVSLLDFYWVARIFFTLHSCVLLMKF
HSYAFYNGYLSIIKIELNGSSSILDKVKDSLNIPEKDEQLEKSCHLCVFELSRQKKSNTYPNNISVRNFL
DFLLVPTLCYQLEYPRTARIRWRYVLEKACATFGTIFLMVIVADQYMVPVAMRAIDFENVTDASGTYIAI
ENWINLLFDMIPFIVLYLLFFYLIFDCILNAVAEITRFADRYFYGDWWNCVSWDEFSRIWNKPVHKFLLR
HVYHSSISGFKLSKSQATLFTFFISSVVHELVMSIITKKARGYLLFFQLLQIPLIALTNTKFKRRRPILG
NVFFWFGICVGPSVMCTLYITF
>gnl|CDD|227390 COG5057, LAG1, Phosphotyrosyl phosphatase activator [Cell division and chromosome partitioning / Signal transduction mechanisms]
LSLEEHATFSTPVKRILDMKDMKDFVESEAYARIYNFILDLDESIKGCSDSDYHSEQSSSVNHMMNVLDR
IKEITQETPPIPGPQRFGNPAFRTWHDKLYDTYPQILQEMLPSEYHEAVPELQYYLRNSFGNSIRIDYGT
GHELNFMCYLYALYCLGIFGIADYGALVFTIFVKYLEIMRLLITKYTLEPAGSHGVWGLDDYFFLPFLFG
SSQLCNHKPLKPREIRDKELVEEYADSNLYFGAINFINEVKLGPFREHSPILYDISAVKTWSKVNEGMIK
MYDVEVLSKLPVVQHFIFGEFLPKDPGQAPKDLFDGKDEEREHVHTRFPDCCGIKPPSAIPASHQNQSHI
PFD
>gnl|CDD|227391 COG5058, LAG1, Protein transporter of the TRAM (translocating chain-associating membrane) superfamily, longevity assurance factor [Intracellular trafficking and secretion]
SMNNLKVRSKHRRSSSIGKIDLGTVPSLSTMPESISSKVPAKRRMKDLSGFVAKDSWFSVREPSYRHVWI
KPLCLLIMVYSAYFLSSNSTRNYLHRFIFLSYQIPDTNQYGKGILDLCFVLFYMIFFTFLREFLMDVVIR
PFGLELNVRSEKKIKRFCEQMYAIFYYGVSGPFGLYVMRSSPLWFFNTKALYETYPVFYNPFLFKAFYLI
QAAFWAQQACILVLQLEKPRKDFKELVFHHIVTLLLIWLSYVFHFTRMGLAIYITMDVSDFFLSLSKTLN
YLNSVLATFIFGIFVFIWIYSRHYLNLKILWSVLTAFRTIGNFVLDVATQQYKCWISLPIVFILLQALQL
VNIYWLFLIVRVAYRVIWEGELKDERSDDESEEESDLESSEDKND
>gnl|CDD|227392 COG5059, KIP1, Kinesin-like protein [Cytoskeleton]
QSSDNNSPLKSRLSSRNEKSVSDIKSTIRIIPGELGERLINTSKKSHVSLEKSKEGTYAFDKVFGPSATQ
EDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVS
ISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDES
SRSHSIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDK
KKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSR
EIEEIKFDLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSIISGTFERKKL
LKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSDRVESEKASKL
RSSASTKLNLRSSRSHSKFRDHLNGSNSSTKELSLNQVDLAGSERKVSQSVGELLRETQSLNKSLSSLGD
VIHALGSK
>gnl|CDD|227393 COG5061, ERO1, Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond formation [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion]
AIGITKLISIWNAIWNFKLDPEIIISQTDNSSTGIYQMNSKVRSLLPVLTESDYMFYYRLNLYAKACTLW
PDDNDMCVSKACNVTVRSEEDLVPKVWKDKLSLFKPHSKKLDQFCSESKCPDLSYCYVDNKSIFNDVYIS
LLENPERFTGYKGNHSAEIWRKIYEQNCFDTLLPPTLLEKRMFYRLVSGFHASISTHLSSFYLNVFFGTW
LPNLDLFRARVGNFPDRIENFYFNYALVRSALGKIDVDLSSFTFCPTDKDELSGKLSSLISAIRAQGKTF
NEIQPFALEKSIQLKDRFREHFRDVSRLMDCVGCEKCRLWGKIQTTGYGTALKILFESETQLFDLRSLER
VALVNTFDRLSVSVREATFENILLRSYKAPLLVIASLYWLEMLSPAASILMIFLVKRAWSFRYKFKSYLA
LPRCI
>gnl|CDD|227394 COG5062, COG5062, Uncharacterized membrane protein [Function unknown]
LKPCKEGFVTNLTLSEIELFAVTSITHLSIVVYHLMLPKSTLLEFMFCLVPLYSIIVFLKYSGLTYALFL
CLLGFLFLFWRRLRKPVNPGNPSSKPKQSTDAPQDDEPYTSMAITRYRFLIIGCTVIAILAVDFPFFPRR
LGKSETWGTSLMDIGVGSFVYNSGIVSTRAKSKRKLKNALILLFLGFLRYFSVKLLNYQVHVREYGVHWN
FFFTLGLLNLASLFIRTRANFLLGFFICLTHELLLKFFGLEKFIYSAARSSILTSNREGITSLLPYISIF
LMGADTGKVVFKKKPTRKKAWKIIILYNAFFLCVYLVFNFYSTSSRRLANLPFVMWIMLLHTFHLTVYEL
FDRTSKIYNLVMHRFESKNLNFLLVFSNANVLTGKVNSSSKTMSSCSSHAKCLTYLVAVFSIPCAINSKL
AGKLIVSGL
>gnl|CDD|227395 COG5063, CTH1, CCCH-type Zn-finger protein [General function prediction only]
MGQFPGKVDGSPWSIYTISPDTNSTEEDPLGRCNCLLSRRTSYLRNICECSEYYKKPSLNETISHLSASL
DNKEQSSSEKRQKAEDSSASSNSPQNYPWSPRGSNANKPYGLYKTEMLRSSTEIPYCRYPDKNPFAHSKA
ISSLAQTHPKYKTESLEVFINPGYVPYSKRCCFISLPLTDINLQPLSQRKPKSGKNCTSYTLGKESDAHP
HDELIYQKQEQNKPLYKTNPELCESFTRKGTCPYWISGVKCQFACRGHGLNELKSKKKKQNFRTEPCINW
EKSGYCPYGLRCCFKHGDDSDIEMYEEASLGYLDGPCRTRAKGGAFPSGGAVCKSFDKKNLDFSVKALQR
M
>gnl|CDD|227396 COG5064, SRP1, Karyopherin (importin) alpha [Intracellular trafficking and secretion]
STSRFVPEARRYNFKGKGRFSADELRRRREEQQVELRKQKREELLNKRRNLADVSEEAESSFIPMEQQFY
SELPQLTQQLFSDDIEQQLQAVYKFRKLLSKETSPPIQPVIDAGVVPRFVEFMDEIQRDMLQFEAAWALT
NIASGTTQQTKVVVDAGAVPLFIQLLSSTEDDVREQAVWALGNIAGDSEGCRDYVLQCGALEPLLGLLLS
SAIHISMLRNATWTLSNLCRGKNPPPDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQA
VLDVGIPGRLVELLSHESAKIQTPALRSVGNIVTGSDDQTQVIINCGALKAFRSLLSSPKENIRKEACWT
ISNITAGNTEQIQAVIDANLIPPLIHLLSSAEYKIKKEACWAISNATSGGLNRPDIIRYLVSQGFIKPLC
DLLDVVDNKIIEVALDAIENILKVGEQDRLRYGKNINIYAVYVEKAGGMDAIHGLQDSVNRTIYDKAYSI
IEKFFGEEDAVDELAPETAGNTFTFGSNVNQQGNFN
>gnl|CDD|227397 COG5065, PHO88, Protein involved in inorganic phosphate transport [Inorganic ion transport and metabolism]
MNPQVVNIAISIASMQISRRIDFQDPKIIWYLRILYLCSNLIQLMFSIYIMRRIKATNDCTKLKYVEPAS
PFSGGSEEKLVETTVRDYDLSELTKASRSAVIGFAIMSFMHLYMKYAQPLFVQSISPLRSLFLNNLVTIY
VFNKPALGELRRPFKAPGLFGGIGQAPKTDKKSIKEAELTKLKPT
>gnl|CDD|227398 COG5066, SCS2, VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and secretion]
MAVEISPQTTFYVPLTNKSKEMFSVQNNSPEPVGFKVKTTAPKDYCVRPNMGLIEPMSTVEVEVILQGLT
EEPAPDFKCRDKFLIQSYRFDWRLSGSDFADHWTSSSKKPIWTRKIRCVYSEEEISKNVHECSEDRGAAV
LLVEMPTLLNILYLEVRFFVNQKEVPAEPETQPPVQVKKEEVPPVTQKTVPHENEKQTSVSTPKPQNQIK
EAATVPAENEPSSMPIFVPVALSILNEGWFYR
>gnl|CDD|227399 COG5067, DBF4, Protein kinase essential for the initiation of DNA replication [DNA replication, recombination, and repair / Cell division and chromosome partitioning]
MVSPIIRSPLKDTDNLKHNNGEEASTTAQGHVFSKDNNCDNNNTTTSFPKKRSLERLPLQQTQHLHEKKR
ASIKRSMKNALVPKKPYILIEDESNKYQKFLKEYASSEKPKLHLDSRTYCCAFPAFKFYKDNKSGKRKHR
VKEGFCELGAVVFTFFEEHVTHFITRRFAKDNSNYKKLDVLISAKAFNMKIWSEEKLPNRPLLTLTPVDS
LRNTVGVHCLSNLLYSEKLYGTLDRDEGVPRQDVVYFRHPILYVFDLWQTYKPIITREWKKQLLTDELPW
PILKITSFGRCPFIALQRRALNTSSVNDQTKNIIFIPHSCNNETTENKKTDNSAVQDVRNIHADQTILLN
ETDTKEQPLTSIAEESNKYPQRKEAAATPLCTLKTRLIVDRKLGVKQTNGAPSKETGKDSAVHQKVKKET
KKGYCENCREKYESLEQHIVSEKHRRFAENDLNFEALDSLFELLRRPI
>gnl|CDD|227400 COG5068, ARG80, Regulator of arginine metabolism and related MADS box-containing transcription factors [Transcription]
MDENPDDSSAPSSPRRHIQGDSDANIPSNTINRLSPGELSQQNDGKFDVMIFDSKHSVRVYSNEEPIEQT
KAQLQKFLISVTGRKIGISYITNKTKRSVTFSKRKHGINKKAFELSVLTGTEVLLLVISENGLVHTFTTP
KLESVVKSLEGKSLIQSPCSNAPSDSSEEPSSSASFSVDPNDNNPMGSFQHNGSPQTNFIPLQNPQTQQY
QQHSSRKDHPTVPHSNTNNGRPPAKFMIPELHSSHSTLDLPSDFISDSGFPNQSSTSIFPLDSAIIQITP
PHLPNNPPQENRHELYSNDSSMVSETPPPKNLPNGSPNQSPLNNLSRGNPASPNSIIRENNQVEDESFNG
RQGSAIWNALISTTQPNSGLHTEASTAPSSTIPADPLKNAAQTNSGTRNNNFSDNLYGQLNI
>gnl|CDD|227401 COG5069, SAC6, Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]
MEAKKWQKVQKKTFTKWTNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVME
NVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGELTKHINLLLWCDEDTGG
YKPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDI
VNVSIPDERSIMTYVSWYIIRFGLLEKIDIALHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANW
KVVNFSKDVSDGENYTDLLNQLNALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPPAGNPKLDLAFVA
HLFNTHPGQEPLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLMP
MTVTHKLVKKQPASGIEENRFKAFENENYAVDLGITEGFSLVGIKGLEILDGIRLKLTLVWQVLRSNTAL
FNHVLKKDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVFYLDVLKGIHSELVDYDLVTRGF
TEFDDIADARSLAISSKILRSLGAIIKFLPEDINGVRPRLDVLTFIESLMAD
>gnl|CDD|227402 COG5070, VRG4, Nucleotide-sugar transporter [Carbohydrate transport and metabolism / Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion]
MKKAVSELTASLSYCFSSILMTLTNKYVLSNLGFNMNFLLLAVQSLVCVVGLLILKFLRLVEFRLTKAKK
WFPISFLLVVMIYTSSKSLQYLAVPIYTIFKNLTIILIAYGEVLFFGGRVTSLELLSFILMVLSSVVATW
GDQQASAFKAQILNPGYLWMFTNCLSSAAFVLIMRKRIKLTNFKDFDTMFYNNLLSLPILLSFSFLFEDW
SPGNLANNLSVDSLMAMFISGLCSVGISYCSAWCVRVTSSTTYSMVGALNKLPIALAGLVFFDAPVNFLS
IFSILLGFLSGAIYAVAKSKKQQNQKDPA
>gnl|CDD|227403 COG5071, RPN5, 26S proteasome regulatory complex component [Posttranslational modification, protein turnover, chaperones]
MEQKPEVDYSEKFAELQKSLNNLNTIDIDANLEKLLIFEKKVRQASDTSTNTKVLIYIADLLFSAGDFQG
LNEQLVSLFKKHGQLKQSITSMIQHVMEYLKGIDDLKTKINLIETLRTVTEGKIFVEVERARLTQLLSQI
KEEQGDIKSAQDILCNEPVETYGSFDLSEKVAFILEQVRLFLLRSDYYMASTYTKKINKKFFEKEDVQSL
KLKYYELKVRIGLHDRAYLDVCKYYRAVYDTAVVQEDPAKWKEVLSNVVCFALLTPYDNEQADLLHKINA
DHKLNSLPLLQQLVKCFIVNELMRWPKVAEIYGSALRSNVFAFNDEKGEKRWSDLRKRVIEHNIRVIANY
YSRIHCSRLGVLLDMSPSETEQFISDLVNKGHFYAKINRPAQIISFEKSQNVQEQLNEWGSNVTELLGKL
EKVRHLIIKEEMMNSIQAK
>gnl|CDD|227404 COG5072, ALK1, Serine/threonine kinase of the haspin family [Cell division and chromosome partitioning]
MSSRSKTKTYGKNRTPINPDINISARLDERPCALKPRNIENSGSQLSSSLESIHSKPSKTSSSKWNFWKK
KGSYPENELLAKSSFSSVHTVIFPAGPRDEASKTIVSKKEVTNLLNHKALSSSLSNSLKHKPSHRSLQKV
KQRRKGPFSQFVNSQTKKICPVPDQVSSDKIQAKLADSTSLVSLVSPFGLPGNAQDADVLNLVQILQWCD
VKGFANLHQVVVVLGLYPSLNLEESDQLSSNNWQENICKKVSLGSTQDYTVDCLFLSLTELEHLELRQWR
ECGSVFLETLKVVSLDETLYLYLHFKDHGTPISIIKADRSEEELSFFWSCISILDILEKKFPFEHRNLTL
DNILIDEGNVTLIDFKLSRLSYSQGIISYNRLDHPDLFNGVDDYQFEIYRLMRRLLKGRWAQFEPITNVL
WLYYLSHQLLKKKNLSSPKTETNRLMRRLKQITHLIDPVRKHQFQQAEFKIREKSTIKSAGDLLNLVR
>gnl|CDD|227405 COG5073, VID24, Vacuolar import and degradation protein [Intracellular trafficking and secretion]
QNILNSLDNPFVLDLNGRPNQESSSYASAYGSRTSSPNARSCSLNIVFHKHKKVETYYMIRHKNKRRLFS
SYTRRSGFLRNGAQFGGVQISGYPPLTVEVNIDTVDLPKKDDYSLPHLCGTLNIQNLTDPSSTLTTYFEG
EIIGFNKLPFATEKWSMAPASEEIDVCHWKRFPPFRMDNGTFIERIFNQKSKDYKINQRYIYMKWKELFL
LPDPLQLDTISGASIDGFYYCCLDQETGYIQGYYYHPKHAEKSQQLELVPEQPRKSPSYSFS
>gnl|CDD|227406 COG5074, COG5074, t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]
MSDANPYSLRIYEMIETLNGVTFMNKILSINKNLSVYEKEINQIDNLHKDLLTEVFEEQSRKLRRSLDNF
SSQTTDLQRNLKKDIKSAERDGIHLANKQAQAENVRQKFLKLIQDYRIIDSNYREEEKEQARRQYIIAQP
EATEDEVEAAINDVNGQQVFSQALLNANRRGEAKTALAEVQARHQEIKKIEKTMAELTQLFNDMEELVIE
QQENVDVIDKNVEDAQENVEQGVGHTDKAVKSARAARKKKIRCYGICFIIIIVIVVVVFKVVPFVVFTRI
>gnl|CDD|227407 COG5075, COG5075, Uncharacterized conserved protein [Function unknown]
MEELSADMASLIKEFKFEEVLDSNTCTKVISLLGRIRGKDALLTAEKTHFLFDTVRSQSQRSTGLQDLKE
QTSNDIYYWFLSVVKQDIDFNPTAKSNLIWPATEEHVRKYCSQKRHYVRETPEMYLDIVKPFIQEMRGSR
WKWVNNILYEGAENERIVYEDESVINGFIIIPDMKWDGQTVDSLYLVAIVYRTDIKTIRDLRYYHILWLI
RLNNKILTEVPYQFGVDPNELRMFVHYQPSYYHLHVHIVNIKHPHGGNVACGRAILLEDVIENLRIGPEG
YMKKTITYMIGENHDLWKPGTNEEA
>gnl|CDD|227408 COG5076, COG5076, Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription]
LEFDEVSYSQLGRPSVLKEEFGNELLRLVDNDSSPFPNAPEEEGSKNLFQKQLKRMPKEYITSIVDDREP
GSMANVNDDLENVGGITYSPFEKNRPESLRFDEIVFLAIESVTPESGLGSLLMAHLKTSVKKRKTPKIED
ELLYADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFV
SDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIPEEMLELSIKPGREEREERESVLITNSQAHVG
AWPFLRPVSDEEVPDYYKDIRDPMDLSTKELKLRNNYYRPEETFVRDAKLFFDNCVMYNGEVTDYYKNAN
VLEDFVIKKTRLIREYPKLID
>gnl|CDD|227409 COG5077, COG5077, Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]
MSSEDELGSIGEVFPGSPDKSIGSILPQFDPDVEELLEMSFTWKVKRWSELAKKVESPPFSVGGHTWKII
LFPQGNNQCNVSVYLEYEPQELEETGGKYYDCCAQFAFDISNPKYPTIEYINKSHHRFSMESTDWGFTNF
IDLNKLIEPSPGRPPFLEEGTLVITVYVRVLKDPTGVLWHSFLNYNSKKETGYVGLRNQGATCYMNSLLQ
SLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTELTRSFGWDSDDSFMQHDIQEFN
RVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQV
ETLDGDNRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRD
ADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGDHPYKDK
IRDHSGIKRFMSAYMLVYLRKSMLDDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLY
TIDSFIHYHGFDYPDFSSELNDSGLAQFVIKRGAKISDLRNNIAEHLNTPQSLYLREWTMIKRHNKTVRV
DRPCNRVNITTRELVGMNTRTGEELRSYLERIIEHNQLDSQRKVALTKDGVINIFVKYFDYTTQPISGFG
GLHVNKFLKISSISPWIEDSISSNLPLTLYEEIKPGMVDTIGDNITFIGSEIGTGDIICFEVPGAVEFDT
SSAYDSALKLYDFLQGRVLVAFRRFSDEYRENVFEFLLFIGDFYDDLCRNVSCKLHVTPFYLRGTKSTEL
EDRIRRVVGSKSIFLLKEALSSSSEFRQAPVDFYEVLDVPLSELERKRLIRLCFLSNGYQHVYLAEFYVE
KDYTAVDHLHIVVTKVGCTDELKKSVLVYEVVNLRPVRGHSLKTLIIDDNVRSTLYGEVFPLEQEQLTTN
EMCVVVQHFFKDLIRTHGIPFMFVIVPFETFLDTKVRLVARFGYKYKLFSKIKLFVGKSYTDGELDWPMS
YFNDEDILYDLIERLDYILLDHPDRLRSHSSYDRAIIMK
>gnl|CDD|444052 COG5078, COG5078, Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]
MTPLNIRSRRLANDYEELENILARGSWIHFKATRGNPPKYEVTFNIRGIIRGGPTYGDTHRIEITLPESY
PQAPPQVRWLTPIFHPNIYEAGGSVCIGRADHWTPSLTLDDLIISLARLLQYENYAPHSPVNLEAARWYR
SNKDLF
>gnl|CDD|227411 COG5079, SAC3, Nuclear protein export factor [Intracellular trafficking and secretion / Cell division and chromosome partitioning]
PDNLGKQKRSHKARMQAPVSKDRFDLGMRVFMVLLFSSTLDTNPFELLKKLRAKERELLEAKSANALPSA
IVFVGTCMDMCPEFEREERVLQNDVSPYEANPNVKKASRTLAVKAYHRPAAGKHPELPSDVRPPEVLVKT
IDYLVKLCAGDQLIEMHRFVRDRTRAVRQDFTIQNEKGKDAVECHERIARFHILFLHLLHDHPHFSKQQE
LEQLKKSLASLIELYDDGRAGKKECPNEAEFRAYAILASLGDPRYVAGIQGWPGGIFCDLPVQIALKLMQ
LAQSNNFRLLGRRNTEACFNLYTRFFKLIQSPSVQYLMGCLLEKHNISIRGGALKAMEKEIESAHKNIPF
VDLSGILDFEEKGEGEEFCKYYGLEIRIEDSVKLPIVFMLSACIDYKKPTAILCTLLESRLQARRFADGI
NGGQDEDRDRIAGNTDFSKKMCIALYNKEPVRKIAVKKFSRSMVRNNLRRFLTGWKDEAAKRNKNAPVTN
PYLLLVVLDREISSVNFTGCINSSVLNSLTSNITYIDKTTVDEMLMYNLCVFSVSKSKREEIYSRYRMII
LIQITPQLLSERVEEIYERAVNALFVRKSTRFAFIDGMDKEQYIEALVRLIDNGRNGDRAEGNLALLYEK
KPLEECDIYYEEEGVD
>gnl|CDD|227412 COG5080, YIP1, Rab GTPase interacting factor, Golgi membrane protein [Intracellular trafficking and secretion]
MYNGRENTTIEPDFYEPDAPFAASGGSADFEGDQNLGPDPLLDETLLATSTRGVYPGDPPLLEELGINFG
HIKSKSDDVLGPFDNKAFDILADCDLWGPLIFILLYSLFLSLAGKSHFGYIYGISLFGTLSLHLLLRLLG
HKNISFFSTISILGYSLLPLVFNSLVSIILGRILILGYVVVALFLIWSTYAASGVLKSKLQLSNKRLLVV
YPLLLFYNVFAIIIKFN
>gnl|CDD|227413 COG5081, COG5081, Predicted membrane protein [Function unknown]
PVSDHRRRRSSSLISHVEKETFEDENDQQVLPNMNATWVDQRGAWIIHVVVILLLKLFYSLFGVTDELGW
TLTNMTYNIGSFIMFHLIKGTPFDFNGGAYDNLTMWEQLDEETLYTPDRKFLLLVPIILFLASNHYVHYN
IFLFLINITSLFLVVIPKLGFTHRLRISIIPGITGRAQIS
>gnl|CDD|227414 COG5082, AIR1, Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion]
TSMDDRPRVVDATPTLPIDKLSANSIEESSSNPNELRSLRSSGRYEDRSVEDVSAIREENPVCFNCGQNG
HLRRDCPHSICYNCSWDGHRSNHCPKPKKCYNCGETGHLSRDCNPSKDQQKSCFDCNSTRHSSEDCPSIW
KHYVLNNGDGHPIKKFCYSCGSAGHFGDDCKEPRSSRVPYVCGKKGYVSF
>gnl|CDD|444053 COG5083, SMP2, Phosphatidate phosphatase PAH1, contains Lipin and LNS2 domains. can be involved in plasmid maintenance [Lipid transport and metabolism]
PEDGPSSPRGRDAGAEASGGPTADPQPAYGFVPADVPQPSDDDPSAPVPEGARCFTNLLSEALPRLPGAQ
RSFKHLGSRLLAGLYSPYHMGHDEIVAAGDTQTIVGKFDYGAVFHKDLEDEDVHVYIYGTGMPDWEYLGS
YRTDSDGKIYVPVPAAQEGRYRVRMVVAGDLSSADLFVSVVPPGRKTVVFDIDGTLTLNDFEGVGDYLGG
ETADAHPYAAEVVQAYADKGYRPIYVTGRPYWLAKDTREWLDTQGLPPGILHTTPSATGPIGPDTARYKT
AEIQLLIDDGLNIVRAYGNAATDAEAYANAGIPKSETYIIGEDAGLRGTQRIDGDYSEHFATVVANTPAA
GCQ
>gnl|CDD|227416 COG5084, YTH1, Cleavage and polyadenylation specificity factor (CPSF) Clipper subunit and related makorin family Zn-finger proteins [General function prediction only]
EKNVCSFAIDGKCNLGSGCTYNHSNYTSLNDGLQSVSSKYMGAKQISPSLSSPTFKNKANLMQNTNDNFV
PGNTVACISRNFNSIRGSRLSTPNNHVNPVLSSSVVCKFFLRGLCKSGFSCEFLHEYDLRSSQGPPCRSF
SLKGSCSSGPSCGYSHIDPDSFAGNCDQYSGATYGFCPLGASCKFSHTLKRVSYGSSPCGNYTPPFSPPG
TPSESVSSWGYGKGTSCSLSHPSLNIDIQQPQTAPSRKDSGGTNPIGASSEIGSEADGNMQNSISGSGDS
EEIEE
>gnl|CDD|227417 COG5085, COG5085, Predicted membrane protein [Function unknown]
MEDMRESMPMDVEGEDGIRNSPKQRQVECLHGSPKKKRDMEPSDEELGHTQKVKYPSDALGLATKKAWRP
SVVNIARVPVVLIGYLQLFLNAIVIGIILYFVVKFIVGLQNDVGYKMESRKAEIQHQIAECKTSYLINKC
DPATRVPAIEELCSKWKQCMKNNGYRSVGYTKLIAEVFGDVIDAFIRKFSVRSSLFILIFVIGFLFFSNA
AFGFYRAYYGNGIKTYPLPA
>gnl|CDD|227418 COG5086, COG5086, Uncharacterized conserved protein [Function unknown]
MDINIDDILAELTTAVDSMSFPDLNDLILAWQNERSTPRLLPYALHLIDRFLDRISEQTEHVKIALGKSI
AKNNESILMETELERVKFVVRSYIRTRLKKIDKNLYYDLSDENSLILLSGGELAYYEKHSLIYIDLLKDS
DLYVTPQKFHKVHDFVGFYCMTDEPDWNKFVFGAVNEDLQENDTVGEKELLELFKGDFFVARYDVIMDFL
RRNEVILI
>gnl|CDD|227419 COG5087, RTT109, Uncharacterized conserved protein [Function unknown]
MPDSLSMAIYMEGLHALPMLLSIRRHMESLCGRSKLGKQAFVSNGRHLFLLFNQETLLFGMELQVYEADA
ENRVFVSKADTTGYGNRGVSRGTKIILEFILSIDKIRKQLAPGVCICLFSVPRSQYLFPGSSRNREKHIL
NPGELLEWWIFILEVFLIESLYNDVQAKLRIPGEDHVWVNHYENGISYPLWQVGDIFTSFKAVDEVPYFP
DDPKERKLRRLFEEGLKVSLEEFWAALLCRQEFASGVTSSLVYGQSRGDDTCSVVETSIGVVDPMERAML
RTLDKYIFGSISDARRSAIEAKKNICDFELAREYFQGQGLVRPKKNEEANAVMPATNKNMLKPRKKAKA
>gnl|CDD|227420 COG5088, SOH1, Rad5p-binding protein [General function prediction only]
SSTNGNAPATPSSDSRFEVELEFVQSLANPQYLTLLTQQQIFESENFKNYLKYLEYWRNPEYSQFIVYPN
CLFILKLLNGFMESAIVSEDGLLEGLDELQYPQWLNKMVERWAN
>gnl|CDD|227421 COG5090, TFG2, Transcription initiation factor IIF, small subunit (RAP30) [Transcription]
MSEEKPTVRTEEDDRYEDDADLDLNNRHTKVWLVKVPLFLAEKWLSREAEIGELLGTKRTSTDPAVISLL
LSNEFCNGGFPSSYDLKIKPKDVNNYYVFRESETSTHEKNTAVVGTVNHECYVTPEVNDEYLRYKQDRGF
KSDSKKSDVQVIDYLKGGKRGEKFGSLRSSTLEFLARKRKKMLMDKKRERLPKNEVLDMLFKAFEKYPYW
TLKGLAEFCGQPEAFLKEILDDIAVLNKKGPYANKYELRPEYKQTMDELRQASQSESSSDHTGTSPDNPG
TNAEEDEDDDVEMIDVV
>gnl|CDD|227422 COG5091, SGT1, Suppressor of G2 allele of skp1 and related proteins [General function prediction only]
AYKALYDEKEPLKALHLYDEILKGSPTNLTALIFKAACLEKLYFGFSDWHSDATMENAKELLDKALMTAE
GRGDRSKIGLVNFRYFVHFFNIKDYELAQSYFKKAKNLYVDDTLPLWEDRLETKLNKKNKKQKDSTNKHT
IKPVESIENRGDNNSSHSPISPLKIETAPQESPKMEIAYDFSETSDTAIIFIYRPPVGDEQVSPVLEGNT
LSISYQPRRLRLWNDITISLYKEVYPDIRSIKSFSKRVEVHLRKVEMVRWGGLNGRPADESSRLSDEGKN
SDSATPKSSKKQDDWKELMVEDSGDEENPSVMDSLFQKLYQRADDDTRRAMMKSFYESNGTALSTDWDDV
KSKTITTEPPEGMEPKHW
>gnl|CDD|227423 COG5092, NMT1, N-myristoyl transferase [Lipid metabolism]
MSEEDKAKKLENLLKLLQLNNDDTSKFTQEQKKMGKDHKFWSTQPVDRFDEEAMPEGPIDKHTISIEQPK
LPDGLLFEFEWCVIDVANKKQLEDVFVLLEENYVEDIYAGHRFRYSVEFLQWALDGPGGKKRWHIGVRVK
GTQKLVAFISAKPHLVSVRGKRSSVLEVNFLCIHKELRSKRLTPVLIKEITRRANVDGIWRAVYTAGTEL
PSPVSQGRYYHRPLNWKKLYMCGFSGLPDGRTEKVKEARNALPAKTKTEGLRLAEEKDMEDVARLYLEYS
RRFELYEEFRFEEIVHTFRPVKNVVDKQVTYSYVVEEPNGKITDFFSFYSLPFTTIENKKYKDIQGGYLY
YYAGDDQFKDFDPKATKALKTRVAEMVGDAMILAKVEGCDVFNALTMMDNSLFLADLKFGCGDGFLNYYL
YNYKSEEIPGGLNPDNSNDIKRRSKVGFVMP
>gnl|CDD|227424 COG5093, COG5093, Uncharacterized conserved protein [Function unknown]
MALPRELEMAFSPEEILFIAYNELIEIEPMTTIPQLRLLERATYPPMMPLDIARVPLWAALLLKKQNMCK
IVLPSWLQLESLKMSIDVEIEKADEFSELPPYWLPLATELLNENCDDVEDIEESRMIVEDIREIRQAKTL
KGLKCLNEKALNLDNLTLFEINEIRPLILESMDVGRRIEDLSKEE
>gnl|CDD|227425 COG5094, TAF9, Transcription initiation factor TFIID, subunit TAF9 (also component of histone acetyltransferase SAGA) [Transcription]
MASGGLNLASVSGPRDVRLIHLILRSLGIEEYEPKVPLQLLEFAHRYTQDVLEDALVYAKHTGRGHIATL
GVEDVRLALATKVGRHFVPPPPKEYLLELATERNSKPLPQPDGENGIRLPPEKYCLTNLDWEVLRKDPKK
KRRIY
>gnl|CDD|227426 COG5095, TAF6, Transcription initiation factor TFIID, subunit TAF6 (also component of histone acetyltransferase SAGA) [Transcription]
MSLTLWSKETLKDVAESLGISNIDDDALRALAMDLEYRIKEVCQEASKFMVHSKRTVLTIDDISYALRSL
NVEPLYGYDPSRPLQFSLVFRGLGQSVYYLDDEEVDFEEYINRPLPKVPRRVSIQSHWLAIEGVQPAIPQ
NPILLDKPVAKWASKDTLGVMPGASTAAYQARNGVTSMENAELKPLVKHVLSKELQMYFDKVISALLDES
DEQTRDAALESLRNDSGLHQLVPYFIHFFNEQITKNLKNLEKLTTVVMMYSSLLKNKYIFVDPYLHQLMP
SILTCLIAKKLGNVPDDHEHYALRDVAADLLKYVFSNFSSSYKTLKPRVTRTLLKAFLDREKTESTQYGA
LKGLSILSKEVIRTVIKPNADYYVRLVNKTLEKGNEEEIYENNRVVDLLKDALLILQSDGLPNQRTLPPN
ASGLLEKVGSLMAEKIMKENDTSLLLGLLE
>gnl|CDD|227427 COG5096, COG5096, Vesicle coat complex, various subunits [Intracellular trafficking and secretion]
MRIMSAFKDSIRKARNADSVAALSSGRLESSNDYKKIDAMKKIIAQMSLGEDMSSLFPDVIKNVATRDVE
LKRLLYLYLERYAKLKPELALLAVNTIQKDLQDPNEEIRGFALRTLSLLRVKELLGNIIDPIKKLLTDPH
AYVRKTAALAVAKLYRLDKDLYHELGLIDILKELVADSDPIVIANALASLAEIDPELAHGYSLEVILRIP
QLDLLSLSVSTEWLLLIILEVLTERVPTTPDSAEDFEERLSPPLQHNNAEVLLIAVKVILRLLVFLPSNN
LFLISSPPLVTLLAKPESLIQYVLRRNIQIDLEVCSKLLDKVKKLFLIEYNDDIYIKLEKLDQLTRLADD
QNLSQILLELIYYIAENHIDAEMVSEAIKALGDLASKAESSVNDCISELLELLEGVWIRGSYIVQEVRIV
DCISVIRISVLVLRILPNEYPKILLRGLYALEETLELQSREPRAKSVTDKYLGAWLLGEFSDIIPRLEPE
LLRIAISNFVDETLEVQYTILMSSVKLIANSIRKAKQCNSELDQDVLRRCFDYVLVPDLRDRARMYSRLL
STPLPEFSDPILCEAKKSNSQFEIILSALLTNQTPELLENLRLDFTLGTLSTIPLKPIFNLRKGAVVLQQ
VTVKKPNAELGFITGNINPSGAANEDLRDINLNDSINSISGFVNPRTVDEDYFRELWKMDEFENKIDESS
NNPKKLDDYSEEKSREDNMEILTPSDDLEFSSSSLGSKSDALMSLCLEKPEPVLGLS
>gnl|CDD|227428 COG5097, MED6, RNA polymerase II transcriptional regulation mediator [Transcription]
MEERPLTSIQWVDPEWLQSKGLRTENVLEYFSGSPFYDKSSNNEILKMQTQFRGLDLGQLSKLLSMLGGF
YEVESSNREPTLWVIRKQYRHNDTEETPLMYYIIHGHNIYAAPTNYSIYRCRMGDSMYQLNSFLDRMMEK
RRFNPFSGPKYPKLSNDNLAKSLSNTSKPLDFNKNMEIFNDFKKEQAEDFSVVRAFMQSLHSSKEAPDVK
>gnl|CDD|227429 COG5098, COG5098, Chromosome condensation complex Condensin, subunit D2 [Chromatin structure and dynamics / Cell division and chromosome partitioning]
MSGFSLSEYLTKFQTTDRESYPRLQDPSRELNVIIDQLAVSEQIDASPDSLEALIDLCHDFPHLQKELEI
LISKLKTSTVSDNSEDYNYLVSHNVNFTIPQCNLENKGRIFQLLKSKLNSPLEVAPSLSTNVSKLEKKND
SANVEKRDCNQMEDLLPKIVDLIRGCLSNSRETSEEMDKFLFLFLEPTKVLLERERDSKVRSRLLECIRI
YGKDVRLHNHVIDLMCTKNSNLTYFAHLSGLIAELIPSISDELNRCALKEDIPVLLKNLSFNLPDLSGPK
DISLFLNKLSELSPGIMLRQYEHFDELLDSESFTLRCCFLEICANLVEHFKKDGQMVEHYKQKLNDLVGL
LVERLSDTYPYTRTKALQVLEKIFDLNSKTVGRRHEVIRLVGRRLQDRSSVVRRNAIKLCSKLLMRHPFA
SEHGSQLRLTLWEKNLGSAENQLNSLKSGLQETLCDGEKEVEQDEGQCRTELEGSFNKSAESRIENEVEN
INATNTSVLMKLKLMIVYYEDANQFIDIMKEIQDNISTLLFGKNKTEVNESMDFIVLCFYFRIDGSREAI
KKMFHLVWTKGTDDEGTSIELHVLSCYKLLFQMKPNNSSLFEFAKEIARNLINLSFEASLAELSSLEQLL
GMMYARRYIDKTVISELWSMYSLQKFDFSLLQASGSIIHIGMLLLVDMFHSLVGLSTLLLIGLGVEGLLD
LMLSRYKCIAQIRVRQRVKFDDEINEVLAKNLAKKLEHQVVDVTVSTEYSISTEQAKSAIMLLEKLPDML
RTSLIAISTVGCFGKPHEEDSMQYLEELERLVKLNRLKFKVGKVAIKPLVYEERCEAEFKRRKISAELEE
NVDNDDSILNNSAQDRGESSRIGGTSEDDFVDAFFFIKEKELLYGEKSVLSNFKPVVEEGCSNSSRFSDE
ELQVAAYLSLYKLMCLSFEFCSEHLPLLITSMEKHPIPRIRANAVVGLGDFLVCFNTTADEHTHYLYRRL
GDEDADVRRTCLMTIHFLILAGQLKVKGQLGKMALLLTDEDAEISDMARHFFTQIAKKDNTMYNGFIDIF
STLSSDAENGQEPFKLIIGFLTDFISKERHQKQLKESLFLRLLRCNTQSQWDKLLCSLFNLPDKIAGSGG
LLNRGKKV
>gnl|CDD|227430 COG5099, COG5099, RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal structure and biogenesis]
PNSDTMNNLLPSIKSQLHHSKKSPPSSTTSQELMNGNSTPNSFSPIPSKASSSATFTLNLPINNSVNHKI
TSSSSSRRKPSGSWSVAISSSTSGSQSLLMELPSSSFNPSTSSRNKSNSALSSTQQGNANSSVTLSSSTA
SSMFNSNKLPLPNPNHSNSATTNQSGSSFINTPASSSSQPLTNLVVSSIKRFPYLTSLSPFFNYLIDPSS
DSATASADTSPSFNPPPNLSPNNLFSTSDLSPLPDTQSVENNIILNSSSSINELTSIYGSVPSIRNLRGL
NSALVSFLNVSSSSLAFSALNGKEVSPTGSPSTRSFARVLPKSSPNNLLTEILTTGVNPPQSLPSLLNPV
FLSTSTGFSLTNLSGYLNPNKNLKKNTLSSLSNLGYSSNVPSPSSSESTRNILGNISPNFKTSSNLTNLN
SLLKEKLSNSSSVSATDILGPSIIVSCKDQHGSRFLQKLLDSNSSPEIEVIFNEILDQLVELSSDYFGNY
LIQKLFEYGSEIQKSIMLSKSSKHLVSLSVHKYGTRVLQKAIDIVSTDIQISLLVEELRPYCLQLIKDQN
GNHVIQKCIEKFNKEKNQFIFDSINENLYDLSTHRYGSRVVQRCLENCNSEDKENLVEEIISNSKYLSQD
QYGNYVVQHILDNGAEPNKERIIIKLLSKRVVELSTHKFASNVVEKCIKYASDSFKRSRILNELTNRGIE
KPGFLMLILDDQYANYVIQYLLDVSPEIQRSLLARAIKKVIPSLKKSMYGQHILALLEKVGSSSQSSISN
KECMNTS
>gnl|CDD|227431 COG5100, NPL4, Nuclear pore protein [Nuclear structure]
MIFRFRSKEGQRRVEVQESDVLGMLSPKLLAFFEVNYSPEQISVCSAPDGQGEIFSLLKDQTPDDLGLRH
GQMLYLEYSDIASNNEKKRDVPGKPKQDCSKGIKREKDSMPVIQDPIDDSLEKEDGLIRRSMTMLCQHGS
NGMCSYCSPLDPWDEKYYKDNKIKHLSFHSYLEKMNSNKNKLGSVESYIVPLEEPSFTVKETCEDGHGPW
PHGICNKCQPSNIILAPQVFRMVDHVEFDGKHIVENFIRNWRESGRQRFGYLYGRYMDYENIPLGIKAVV
EAIYEPPQEDEPDGFTIEEWADEGLMDAPASGTGLERIGMIFTDLLDEGSNRGSVTCKRHADSYFLSSLE
VEFIAKMQTMHPNTVKDSREGEFGSKFVTIVISGNLDGEIGLQSYQVSNQCMALVKADYILPSEDPRRFL
ATKEDQTRYVPDIFYRYTDTYGEEVMENAKPAFPVEFLLVTLTHGFPEKPNPLFRSIDFIPKKFGDRKMA
EYFGGDLSKELFSNFTLLTRIQGVFSNFKDLLKIIVLRILDKFDFKSFISSMERYRWECKMCTFINEKNS
CTCEMCNSTRD
>gnl|CDD|227432 COG5101, CRM1, Importin beta-related nuclear transport receptor [Nuclear structure / Intracellular trafficking and secretion]
MEGILEFDKDLDIALLDKVVTTFYQGDGRKQEQAQRILTKFQELPDAWTKADYILNNSKLPQSKYIALSL
LDKLITTKWKLLPEGMRQGIRNYVVQLVIEKSQDDKVRDKQKYVLNKLDLTLVQILKQEWPRNWPTFIPE
LINVSQISMEVCENNMIVLKLLSEEVFDFSAEQMTQVKKRLLKNQMKIEFPQIFGLCKQILEYSRDESLI
EATLESLLRFLEWIPLDYIFETNIIELVLEHFNSMPDTRVATLSCLTEIVDLGRHPQENAEKERILVIHF
QCIEFLKMYSNKPQEEDIYEVYGGMDKNEQIFVQKLAQFLSSLYEVYISLLEAREMAENLLNAHGYLIQI
SRINEREIFKTALEYWNKLVADLYSEFQRLPATEMSPLIQLSVGSQAISTNPNQDSTKPLRKHIYIGILS
QLRLVLIENMVRPEEVLIVENDEGEIVREFVKETDTIELYKSMREVLVYLTHLIVDDTEKYMIGKLARQL
DGKEWSWNNLNTLCWAIGSISGAMSEVNEKRFFVNVIKDLLALCEMKRGKDNKAVVASNIMYVVGQYPRF
LKAHWSFLKTVVKKLFEFMHEDHEGVQDMACDTFIKIVQKCPVHFVTQQEGESEPFIVYIIRNLPKTTGD
LEPQQKHTFYEACGMVISEVPKTRDYKRLVLDLMDLPNSAWLNIVIQADENINRLSDTMTVKIDANKMKT
NVAKCTSLGYRFYPQTCSSYCIMLFLYFAVSFDISNSVAAEGLIATKTPAVRGLRTIKKEILKLVATYIS
KARDLKFVQNDLVNMLCEAVLFDYKNNVPDARDAEVLNLGTTIVRNVESVIYLQRELFLISVFICTLIMI
VKDFDEYPEHRKNFLLLLENINLFSFSAFLSFPQPSFKLVYNTILWSFKHINRDVSDLGLNILLILFKNC
HEMGVPFINQFYAQYYMSTLENILGVLTDSDHKSGFDQQCLLLAFLIRLVKDNKISVPLYDGINPNITIL
SEYIVGLFVKSFPNITQESVKIFSVGLFELCGDDEIFKEHVEDFRVKVYEFGTDEDLQEEIDLKNERIRR
CKN
>gnl|CDD|227433 COG5102, SFT2, Membrane protein involved in ER to Golgi transport [Intracellular trafficking and secretion]
MEGSFQSRLMDPLMRAFKTREESSKTFCSPIPTRYEWSNDYQMFPTRKYDLEHYFQSSEFGLSRFERAVL
FSACLLGAGACSAFLYFMFPVLRLKPRKFILLWTMGSLLFVLMFGFLLGFRAYLEGLTSKERLPHSSWFF
GTTLLTIYVVLKYKRTLLNIAFCFLQVVSFIMYSITFFPFGTSGVSSIISMFFKSLSNWLP
>gnl|CDD|227434 COG5103, CDC39, Cell division control protein, negative regulator of transcription [Cell division and chromosome partitioning / Transcription]
MKSQEQQTPETREKSSSTSESKIESIVKAQILFLLSTLREDQYDTKLEQIRQLINKNAPRVYHHFLRRLI
QGNSYRIFGTGKSSDGLATYKLLLDELKSLTKKRFSDAISGSDSEVFEDFHFQFSIGLTTSLLKNTFQSL
LNQLSDPTQQQSIDKNDLDLLREGTTDYDRKIFRQEIKDVLEKSDPLTALFGPREVDRSFLDDALQRILR
PRREVVPEDVARAILFMADFPDRGEWNLVAIVGAMKSNLEEINWRDVYSCFLDVNFSIWTLEPLYVIIDC
WFYISGIITVPYEFFFKRWKNERAQILFIRLHIESDEKRTFDYSNVFFTRIVSIEDSRGHRFKNYMGYES
NLNCVELFQCIMLGSLPLIEYIARLFLNKSPEWCAAGLGFVQPKFSPLAWNPVQESRIFEELLMGFANGA
PNSFVFVVLFRTHPEMMLQKSRLVLAKDGIPVSRLLDIFLEHKMLPLVSNLLPPEFCFDIIVLSSARDHL
NLGIWLSNNLTTRKDADGLNVFVVSLVQYLDSKVSKHKEPEKQKEESVMFPLNTVIEILGTFTKAVEQYI
RILKPETVVVLNEFPRLIPHGLRRDSIVAATNTTRSKEIDIEEEASSYIQQIYNSQRGIESSINQLKEFL
RSENPRDKELFSCIFHALLEEYGFFYDYPLSALALTAVLFGSLIKFRLLPKPYLRVAIRYIKGSLKHPEN
SKMFSFGFQALEVFQEKLPSYPSYCSEVLEIPTLNNRILIYKSIVEMDSNENTEVEKANPTHPMLPLEDF
VRLIVKCDANNEGRATEVVKSILFAINNLLDLNRNDKIHRLKEALTPGYVGWFSIYMVTQRSTAEENCRR
LYGKVVERLGSKDLYLRFSRKTLEFLKMLLDYRCESPSEKKVLKNLGSWLGRITLAKNKPITSEQFDFKK
FLVESVECRRILFVVPFVSKFLRQASCSIIFKPPNPWVMGILKLLSELHSCAPRVLRLKFEIEGLLRHLN
VELVPIKPSKSLGNHLVLKSRLEKELPEDVLNAKFPDGTDYLAQYIIEDSSQITVTDLVARHVGSPKPAI
KNLTQLALDLSVREICGAVVEKSCGIAIQTTMALFKKDFAMEVEKSMLYVAARNMVVNLAKFLALVTAQE
PLKACISGNVRSYAMKLCSVLDFSAEKVDKIAMENQDVACRLIERAGVSKVSESISAEIEHMIVERVRHR
KTTPNLPFVDPAAANLSLNLPSSLELSIGKATPQQFSLYEDFDRLSLSTIMGHIEKIAINAIDTDSADST
DALNNNLNNTVENEANQTALEYQENLLIIKAQLVQLSKKIPYSSKKNVIADEEHGLLKEGKNQFETVFRR
ILESIASSDDKDLECIQLCRYILGHLSKSPSKEEVLSRCLEKICKISFKTQKEVLGWLIYSNDPRKFNIP
LIGSLIEHNLINVVEYDQALSRKIPLADGNVTDFAIALLASLVTAEVPICTVYDFICTLEMLAGSSDPKV
KDFFQKISNTMMHIVAKGNKQQLNDQIIIVFSEWVELLRNCRFNDTVPEMFLPQLMERGDYSASLDIRSF
FKVSLEHFIRAFHERIPTAYCYLKIDALPSLIKNRLYEEGSTEGTVSVLFRKIIKDILFVFAEAHRKRAE
FVHNYLFFRLFSRILIETLDVIDEDTSCFVNNRSVVYSIFEALQPSRFPGFTFAWLELLSHKFLLPKVLL
VNNDKINDLFSEGLMSFLKFLDLSEEGVVLVMEALYCGFLRTILVYLHDFPGFLITQIYQLFRRNPLECV
QLRNMMLSAYPSDLTYPCPFAQGLKVQEYPHIKNFPNQFRDRIVPLEGQNSFFDLEACLRSALQNRTSVK
VTDLYIGKNTPLWVYLIDNLNEMDAVSHTVVESIKFMIERFMHKSEILTMLWIRMRAGGPPKRYFLLTAI
LAQLRYPEIHTYDFSRVFLKSFKSHGYNPQKLLIKEQMTTVLLERIICNRPHPWGLLITFTELLKNEDYN
FWKHPYIKRNDEICRLFDSLHEHVMAPSSANNVSTEEATELMGQV
>gnl|CDD|227435 COG5104, PRP40, Splicing factor [RNA processing and modification]
MQAALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYY
YNSITRESRWKIPPERKKVEPIAEQKHDERSMIGGNGNDMAITDHETSEPKYLLGRLMSQYGITSTKDAV
YRLTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEEN
KQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMG
GTALGRLEEVLRSLGSETFIIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEE
RKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDL
ENMYGFARRSYERETRTGQISPTDRRAVDEIFEAIAEKKEEGEIKFDKVDKEDISLIVDGLIKQRNEKIQ
QKLQNERRILEQKKHYFWLLLQRTYTKTGKPKPSTWDLASKELGESLEYKALGDEDNIRRQIFEDFKPES
SAPTAESATANLTLTASKKRHLTPAVELDY
>gnl|CDD|227436 COG5105, MIH1, Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning]
MKNIFHGLEDECANEDVFFFQKASKKSIFGDKKNIFRNIATFFKPKAKHALADDDLINKENFAFDKRPLL
SNHRSKEIAGPFLNIKQLGHRDELDEKENEGDDATLHLHFALQRMTSSSANASSDNEQCPADVDQMYIKK
FYEIPWSSSENIEFEDPGHDPFVDNSDNSKMNHLRGSGKQPKCREKIAFAVWTSLQGMRGFSRAGPAPAA
ENSHLIDFFKSFSNGEVFPLPTLGPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHI
INAVNISSTKKLGLLFRHKPLTHPRALIFHCEFSSHRAPRLAQHLRNMDRMKNPDHYPLLTYPEVYILEG
GYKKFYSNYPDLCDPKGYVTMNNAELDYRCLYKMDKFRRNKKFFATKNNSFGKLALASPDSHDSPTAMAS
LALLFRF
>gnl|CDD|227437 COG5106, RPF2, Uncharacterized conserved protein [Function unknown]
MFRAVKPKNARVKRALHKREPKLVEAHKDAIFYPGMSERKTLLDVICDTEALKKPKEIGFIRKNTIHPFE
DTSPLEFFSEKNDKKLSVLFTSVKKRRHNLTIGRAFNYELIDMIELKINRYKSVSDFECAGPELGMKPMV
VFQGINFDAHPTYRRIKSLFLDFFRGESSKVLDSAGLSWVIARTEEGYVLDTYPLPLVVFRVYKTKLLKT
KTNLPRLELEECGPRLDFEIVRSYHCSDDLYKEALKKPKTQEPKPKKNVAKDIFGDKIGRIHIDKQDLGD
LQTRKMKGLKRGVEEWSDSENEEVEIEEDVISDASE
>gnl|CDD|227438 COG5107, RNA14, Pre-mRNA 3'-end processing (cleavage and polyadenylation) factor [RNA processing and modification]
MSSSTTPDLLYPSADKVAEPSDNIHGDELRLRERIKDNPTNILSYFQLIQYLETQESMDAEREMYEQLSS
PFPIMEHAWRLYMSGELARKDFRSVESLFGRCLKKSLNLDLWMLYLEYIRRVNNLITGQKRFKIYEAYEF
VLGCAIFEPQSENYWDEYGLFLEYIEELGKWEEQQRIDKIRNGYMRALQTPMGNLEKLWKDYENFELELN
KITARKFVGETSPIYMSARQRYQEIQNLTRGLSVKNPINLRTANKAARTSDSNWLNWIKWEMENGLKLGG
RPHEQRIHYIHNQILDYFYYAEEVWFDYSEYLIGISDKQKALKTVERGIEMSPSLTMFLSEYYELVNDEE
AVYGCFDKCTQDLKRKYSMGESESASKVDNNFEYSKELLLKRINKLTFVFCVHLNYVLRKRGLEAARKLF
IKLRKEGIVGHHVYIYCAFIEYYATGDRATAYNIFELGLLKFPDSTLYKEKYLLFLIRINDEENARALFE
TSVERLEKTQLKRIYDKMIEYESMVGSLNNVYSLEERFRELVPQENLIEVFTSRYAIKADAILPPLEPTY
MYNEREHSVQMEGGNGDRYHCFLNMSSSFNFLDMEITGNNGNFSNSRLKRDSELPTELDEFLENLPKIQQ
QNTNLLDNQKLVNFLRVEKVISLLKSVQSG
>gnl|CDD|444054 COG5108, RPO41, Mitochondrial DNA-directed RNA polymerase [Transcription]
MRARLDLTKPTARQIALEEEMAEAGRSRFVERIEKARKRGEESGTQYGRRIISDAVELLAEAIEATIDES
SSGGAGNWHTAYAYLRELDAEVLAYLALRQCLDAVTQRHTLQAVAIRIASMVEDEVRGEAIREAFKDFYP
RGKKKIESRTSRAVRYKDDFERRVKNAVAKEEDWPVSDKIHVGFKLIELVVESTGLVEIARDTEGINDTP
VFVRPTETTLEWIAEANLRMAMLSPAYLPMVVPPRNWTTPFRGGYLSGEVRRLPLVKTRNRKYLEELKNG
DMPEVYAAVNALQQTPWTINRYVLAVMKWLWERDLDLGLPQREPITPPIKPENREDITTNQVARKRWKKA
ARKIYIANAKLCSKRVQFRRDLNEAERFSDYREFYFPYQLDFRGRVYAVPAFLNPQGQDHAKGLLMFADG
KPIGDGGAKWLAIHGANVWGYDKASLEERVKWVEDNYEAILAAAADYVAEFWSKADKPWQFLAFCREWYG
YDQHGEGYVSGLPIAMDGSCSGLQHYSAMLRDEVGGAAVNLVPSDKPQDIYAFVAEVDINLAQRIGCPDE
LTTNEILNGIMDMAHNWLAFGITRKVTKRNVMTLPYGSTEYGFRDQVREDMITRKKEEEGEPFPFGGDGF
SAAMWLAKLIWDAIGEVVVAARRGMDWLQDLAGIAAKEGLPVIWTTPLGFPVMQDYRSSKARRINTTTRK
VRVRLTLREEQDTIDKRKQKQGIAPNFVHSMDATHLMMTVNRSNEYGASSFALVHDSFGTDAGSAELMLD
CLRKAFIELYEESDVLEDFKSEIADMLSDDAYALPEVPKKGSLDVSAVLESDFFFA
>gnl|CDD|227440 COG5109, COG5109, Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]
AKFYTDSNLEETNLQKCLDHTHEVDSKLKIDKRRLRKETMRSIDEIRSALSLKNGQEFDTLSHAEADLVG
SWKSLLKEDCRPANFDVQVGNQIYPFSTQTVTYLVVYYLLENNCADVVERHISETKDGKDEIIKIRDGFV
KLKKVISGISEKSTFLLIEFLQIEGYLSKGDTESELELYLVSHESLLLIHKRYDEALRLCFTKLASFVPK
HIQDVKPLLRFLVNAPTDCFRHREKELMQNIQEALKKSLIGQPIEDIDKVNKSRKKLIELFKSEYCAANG
MPNRSPLRELVETGTIAFLQLSKSGSILFDKHVDWTDDSELPMEIKLPKGRHFHSLFICPVLKELCTDEN
PPVMLECGHVISKEALSVLSQNGVLSFKCPYCPEMSKYENILRVRF
>gnl|CDD|227441 COG5110, RPN1, 26S proteasome regulatory complex component [Posttranslational modification, protein turnover, chaperones]
MVDESDKKQQTIDEQSQISPEKQTPNKKDKKKEEEEQLSEEDAMLKGDLELLVERIQDPDIDLQNNSLNM
LKEVIKSSTSSMTAVPKPLKFLRPNYLDLLEIYDKWLEGNKKRWLADILSALCMVYSENGKHKSLAYRLE
GNIIDLKEWGHEYVRHLAGEIAEVKNDQNEMDAPSFADTRDLGLEIVPFFLKHNAEFDAIDLLVEVGGIE
KVLDFVDTHNYNRVCLYLEDCVPLLPPPEDVALLETALKIYLKMGDLTRAVVGAIRLQKSKEIIEYVRAI
EDPDYKKQCLYILARQNLYYEASDEEEKDILSNGYLSDHFRYLGKELNLDKPKVPEDILKGHLKYDKDTR
QLAGIGSANQNLAMGFVNDPINLGYENDSLIPLDDEWIYKCKVPGLISAFASIGVIESWNSDKGLETLDK
YLYADESYRKAGALLGIGLSGLRVFEERPPALALLSNYLQSSSSKHVIAAILGLGAAFSGTQAEEVLELL
QPIMFSTDSPIEVVFFASLTLGSVFVGTCNGDLTSLILQTFVERGKIESETQWFRFLALGLASLFYGRKD
QVDDVEETIMAIEGALSKHEEILVKGCQYVGTGDVLVIQSLLHVKDEFTGDTLKNEEALIESLALLGCAL
IAMGEDIGSEMVLRHFSHSMHYGSSHIRSVLPLAYGILSPSNPQMNVFDTLERSSHDGDLNVIINTIFAM
GLIGAGTLNARLAQLLRQLASYYYKESKALFVLRIAQGLLSLGKGTMTISPLYFDKTTLMPKNTAGLFTT
VFMLLDSSIFPLVSSHALMYFLLCQIRPQKYVTLSEKGEPIKVNVRVGQAVNTVGQAGRPKKITGWQTHT
TPVLLSHKERAELDTDEYNVCTSYIEGVVILKKNPDYREEE
>gnl|CDD|227442 COG5111, RPC34, DNA-directed RNA polymerase III, subunit C34 [Transcription]
MIEMIRGLLDNAKSRPEGVVEKEISSEFPQQELQMQMGKASLTDLASELNALLKRQLISLFRQKGVLYYK
GVLESEASPINTMDDYELTVYSLISQSGGEGIWLKTIKDRTNLHHNVVGKCLKSLESKRIVKSVKSVKNP
TRKIYMLYDLVPSEEITGGPWFTDNELDVEFIARLLEIIERFLEKNLFPRKNFEEGPNVFYAPKYEDYPT
LEDIMNYVRNVNILSVPLRLDNLESLADVLVYDGKVEKLHSGPIYRYRAFKPYAKNQGEGEPAGNKALED
EEEFSFKMFPASVVYFDEWTI
>gnl|CDD|227443 COG5112, UFD2, U1-like Zn-finger-containing protein [General function prediction only]
MGRSDTKRKKRRSNRLRIKRTRLFGRDLDQIKNDLSTKESQKKLPYDPELPGLGQHYCIECARYFITEKA
LMEHKKGKVHKRRAKELREVPYTQEDAEAAVGLTVGPEKESNEALLKEHLDSTLAN
>gnl|CDD|227444 COG5113, UFD2, Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, chaperones]
MEYPGMNRIELYELFITGMPADMDPYELFKEAECIRGSYLTNNSSDNILLTLLPRYKNNTFSYLQESAKF
LIQTIKRIVKNPEMAGSAHSPVALIPLLTNTYGGSVFDVMECFNSEKISEIEGMARKMLLPMIFLSSFKQ
RQLDEASNLDNLFTSALEALTGLHGVLEEDTVLKNVMEIYWGLVNTKPIADVILKFPIYSGTNFPCGFEY
KTLLGFIESLSYKKCDVAARALDYLGIRSRQVVEKSRRSLRLTLSDHSDKLFQIIHSLVRSSKELRANFM
KYFAKVINVNHERSKTIFSWRENISDGFMYNMSMVLSRFSRPFLDIGCSKIDMVDKIYFNNPRVDIKEET
KLNVDEKSLDSFYTKPAEGSNNFISDIFFLYLTKIHYGVNATFTSCEKFGEYIRKLKESLEYECRLLDGS
FQATRLTAQLSRMEAYLKGIDSKMSALNGFLFMTSLFADEFPFTDFMTEYLARVEDPWPTYPFYYKTLPW
MENAPMTFKLIPEATIENALNYVLESIKDWRSPIFKKELEPLCEFVKIVLHRSSAIKNPMLNRKLDYYLS
LGRDEMRMESRSIIHDIFKEGKVFSRWLLPALMAFYIEIESTGQSTQFYDKFNIRFIICMMKDFEYKQPS
YSEGLSSIKDTNLPFFVKFDAKMLNDLTRLLDEALKELVEEHNIQSLLADAISNSNISERIGELQKSLAF
AKRQARNSCLLVDGCFDLFTHILDEIPDAFLVDEIVSRLARMLNYNLKILTGPKCTDLKVKDPEQYGFNA
KNLLRRMVMVYINLRSESKFVEAVASDKRSFDIDFFRRALRICENKYLISESQIEELRSFINRLEKVRVI
EAVEEEDMGDVPDEFLDPLMFTIMKDPVKLPTSRITIDRSTIKAHLLSDGTDPFNRMPLTLDDVTPNAEL
REKINRFYKCKGQKHGGSE
>gnl|CDD|227445 COG5114, COG5114, Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics]
MGGVKIHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNSYPIGEEGWGADE
ELLLIECLDTLGLGNWEDIADYIGSRAKEEIKSHYLKMYDESKYYPLPDITQNIHVPQDEFLEQRRHRIE
TFELPPINPRKPKASNPYCHEIQGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNS
RLTFRARRKHAIFGKNLMDYRNLQAKDKKRSKEECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRI
HELQEWRNNGLTTLEAGLKYERDKFEKFGASTAASLSEGNSRYRSNSAHRSNAEYSQMDVKNILPSKNMT
ISDIQHAPDYALLSDDEQRLCETLNISPKPYLELKKEVISCFLRTRGEFTKEDFNRLFGIDLGKADGLYD
FFLERGWIHEEK
>gnl|CDD|227446 COG5116, RPN2, 26S proteasome regulatory complex component [Posttranslational modification, protein turnover, chaperones]
MSMTTARILPALLAELRDGRESEALDVINAHVDQLWPEISDDLRYIEALYDDDSFDPREMAALCLSKVYY
VLGEYQQAIEYALRAGDRFLVDDGSFYYETIVYKSIEMYVHMMDSAYIGGDKDIIDRILDFVLEVIGAKC
VDDSEIGYLLGIAAEGLRLDIIEKYLSDGNDCDIINYLLDLAITLVEEEGFRKEILRMLAEIGPGKPKPD
YFYVIKAVVYLNDAEKAKALIEKLVKENDLLLYAQVAFDLEDSASQEILEILVTELVAQGYDQAVMSILS
GEFTKKYLGAFLLEKNNTDFKFLNSSKSSLARKFSRFHYAVSLANSFMNLGTSNDSFYRNNLDWLGKASN
WAKFTATASLGVIHLGNSNPGYEILKPYLPSEVASSRQKEGGALYALGLIKAGFGREDTEYLLEYFLDTE
DELTPELAYGVCLGIGLINMGSANREIYEKLKELLKNDRALLGEAAVYGMGLLMLGTWSVEAIEDMRTYA
GETQHERIKRGLGIGFALILYGRQEMADDYINELLYDKDSILRYNGVFSLALAYVGTGNLGVVSTLLHYA
VSDGNDDVRRAAVIALGFVCCDDRDLLVGTVELLSESHNFHVRAGVAVALGIACAGTGDKVATDILEALM
YDTNDFVRQSAMIAVGMILMQCNPELNPNVKRIIKKFNRVIVDKHESGLAKLGAVLAQGISEAGGRNVTI
SLRNATGILSADRIVGLVLFLQYWYWFPLIHFVSLSFLPTTVIGIRGSQAIPKFCFNEDLEEEEFEYPRM
YEEASGKSVRKVNTAVLSTTIKAAARAKQKPKEKGPNDKEIKIESPSVETEGERCTIKQREEKGIDAPAI
LNVKKKKPYKVDNMTRILPQQSRYISFIKDDRFVPVRKFKGGVVVLRDREPKEPVALIETVRQMKDVNAP
LPTPFKVDDNVDFPSA
>gnl|CDD|227447 COG5117, NOC3, Protein involved in the nuclear export of pre-ribosomes [Translation, ribosomal structure and biogenesis / Intracellular trafficking and secretion]
SSKRNNSQSSTEPRTTKKAERELTQEDIEFFNENPEDLGKKVIYDLKKSSSDEEEQDYELRPRVSSSWNN
ESYNRLPIKTKDNVVADVNNGEEFLSESESEASLEIDSDIKDEKQKSLEEQKIAPEIPVKQQIDSEKERI
ASICTKIIEEPEENLGMMEEVFSMITSMAEKAKKVSYLSLLKVFKAIIPGYKIRPLKEEEQMVKDSKEVL
HLKDYEQSLLRWYTSYIKTLVDDVKDESTLDETQSSLYQVAYISLCELIQHASHFNCTDKVFSLVLRGIL
GTTKRPVSMLIIDTIKSKLEEDCTGKTSLVATVIDQMLDKERNPLVLEYVLDIPLSDNSLRDEEKARKYW
EANKPVSKREKKDIFHLSKKLRKIEKERLRIQSEMRDAEDIEEAIEEEKNQSEILKIIFRLYFMVLKGDR
KDLIGYVLEGLVKYRKIINPEFLGDLLEVLYELLNDNPLDKISSDARRQALLCILTAFEIASATLYGKEN
YDLGGFVDLLYSMVHPMNLEPDADLNLKIKRLKDPDAPSKPFVVNATTDNEELLKIVRLLFFKSKQPVHR
RHVIFKKRLLYCCSRSPEEFKGAILDISAKLDIRYSDCSNLKCSEFDIGAGNVDSIPSNPDLSNSSTAVL
FEYFLLKQHYSPAVSQSAKELLKSTSL
>gnl|CDD|227448 COG5118, BDP1, Transcription initiation factor TFIIIB, Bdp1 subunit [Transcription]
PQLFIPESKEIEEDNSDNDKGVDENETAIVEKLVGERSLEGFTLTGTNGHDNEIGDEGPIDASTQNPKAD
VIEDNVTLKPAPLQTHRDQKVPRSSRLASLSKDNSRPSFKPSFLDSSSNSNGTARRLSTISNKLPKKIRL
GSITENDMNLKTFKRHRVLGKPSSAKKPAKISPPTAMTDSLDRNFSSETSTSREADENENYVISKVKDIP
KKVRDGESAKYFIDEENFTMAELCKPNFPIQISENFEKSKMAKKAKLEKRRHVKFLEGSNTHEMDQLLKH
FLDNSNFRQDRRSRKKKASASRDISDQNAEEILMIKNGHIVVDEANMYVDRHKNASIEVEEMEVVEENPF
ARIVTSSTFGKKKGALRWSKKEIEKFYKALSIWGTDFSLISSLFPNRERKQIKAKFIKEEKVNPERINEA
LNEKKPFDQVEYNKLRSYLLEKLIELQNEHKHHMKEIEEAKNTAKEEDQTAQRLNDANLNKKGSGGIMTN
DLKVYRKTEVVLGTIDD
>gnl|CDD|444055 COG5119, COG5119, Uncharacterized conserved protein, contains ParB-like nuclease domain [General function prediction only]
MMRIKEIPLNQIRRPLPRQTDPQKVAALMESIAEEGLQEPIDVLEVDGQYYGFSGCHRYEACQRLGKETI
RCRVRRAPRSVLQKHLA
>gnl|CDD|227450 COG5120, GOT1, Membrane protein involved in Golgi transport [Intracellular trafficking and secretion]
MWLMNLQKSGVVVTSIGFLFFLVGIFLFFDRALLILGNLLMIIGIFLIAGSRKSMFFFLRPEKIQGSVIF
AMGVLLLLYRFPMFGFLLETLGLFLLFRDFIPTIRTFLRTLPLIGPYIDRLLGRLMRPV
>gnl|CDD|227451 COG5122, TRS23, Transport protein particle (TRAPP) complex subunit [Intracellular trafficking and secretion]
MAVEQFFIINKSGGLIFQREFGEGETELNSNEYLILASTLHGVSAILTQTIPLPGSSGRLVLYFRNFVMT
IFQTTTGTKFVFVAEKRTVNALFQLQKIYSLYSDYVTKNPFYSPEMPIQCSLFDEHLKRMFEGH
>gnl|CDD|227452 COG5123, TOA2, Transcription initiation factor IIA, gamma subunit [Transcription]
VPGYYELYRRSMIGKVLEDALDELISAGVISPNLAMHVLETFDKSVPEVLNKSVTSSLTFKGKLDTYNFC
DGVWTFITKNFVMSLNNEYFNAGEVNIVACKARIVACAGRRSR
>gnl|CDD|227453 COG5124, COG5124, Protein predicted to be involved in meiotic recombination [Cell division and chromosome partitioning / General function prediction only]
MPPKGLSLAEKRRRLEAIFHDSKDFFQLKEVEKLGSKKQIVLMTVKDLLQQLVDDGVVSVEKCGTSNIYW
SFKSQTLQKLYDSSELLKKKIQEVKQDIATYKEEIDKEKATRRKKFTEGQKNYNREALLEKRKKEQDEIK
KKLNSLQKIEPIRWDAAKIQEKKKKVHLNKTTDNIEILIDYLCKKFFLKPEQIRKEFGIPEDLDEFQEV
>gnl|CDD|227454 COG5125, COG5125, Uncharacterized conserved protein [Function unknown]
MKLFSGVARVMDEDEVHDRYLNLLQEMRLLKEDLLEDKCRLDKLVSTSNMLFKRIKTSSELKLDAKITAL
STKLACTRMEKDINLEDITPGTLVELARKDLLHDFYRYAMDCSVGMRGPLSFSKKHREAPSRRRAQSQRS
RQTLPETEVPTNITRQEDSVEEPKILAQISRLLAEKGRTNYFKFIIDPRSFSKTIENLFYLSFLLKEGKA
FLEFDEDGTLYVVSEGSEGASTGHLVVEMTYDEYLRIVERMGISKAMIG
>gnl|CDD|444056 COG5126, FRQ1, Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]
DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPF
ARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDYYTPDA
>gnl|CDD|227456 COG5127, COG5127, Vacuolar H+-ATPase V1 sector, subunit C [Energy production and conversion]
MSKSDFILVSLPVEEDGSRPDEDQIWDLYGGRSTVSRFLLPSFKGVSLDGLINQSERLGKLDKQCEGAIS
KILKIFMGYCRSSNGDRVGKGIVYGSTPEYGDFFEWDRQSFVTNKSIEKAILLIDGEYRRISKDYREKAE
EFDGAKRECEKLQRKTRGSLSDISLGIIVEREDVVEGSEFLTVVYVAVPKALVPEFNRSYETLSPHVSPD
SAEKVNSDEEYVLFKVYVFKKGEEDFRTMAREEKFMVREFDKNMVLSEEMIAERDRAAEKESAMEKILMR
FAHVALTEVFRIWIHIKLLRVYVESVLRYGLPPEFMFFITRGEKKSESKVKAQLIAIAKNLPSNRIVYEK
EGDNNDEGEILFAFAELSTDGEYEPFVLFVFNY
>gnl|CDD|227457 COG5128, COG5128, Transport protein particle (TRAPP) complex subunit [Intracellular trafficking and secretion]
MQSTNKELFRSSVSESLKSTAPLMGKSVYEQNLKIMKREVPLSTMAFLFCEMIEYLMEQRSGIQDFEAKL
KSIGYEVGIKLLELCNFRRRNPKREVRILTILQRIHFDLWSYLFGDSDDRLEKSREVDREYMIVDNDPLL
SRFISVPDEWNGLSCDSIVCGIIQGFLMAAGFPCEVTAHPEPSENLPNRTVFLIRIDDLVIAREEVLG
>gnl|CDD|227458 COG5129, MAK16, Nuclear protein with HMG-like acidic region [General function prediction only]
MSDESLWQVSGENFCSFRIKTEEQNFCRNEYNVTGLCDRQSCPLANSRYATVRADNGKLYLYMKTPERAH
VPRKLWERIKLSKNYEKALKQIDESLLFWDEKVIHKCKQRLTKLTQYLLKARRLALFKEHGEYMVRKPKM
NRREKLRERKALNAAKFEKNIEKELMLRLKSGIYGDTPLNVREHLWNKAATEREKRQDEKERYVEEEEES
DTELEAVTDDSEKEKTKKKDLEKWLGSDQSMETSESEEEESSESESDEDEDEDNKGKIRKRKTDDAKKSR
KPHIHIEYEQERENEKIPAVQHS
>gnl|CDD|227459 COG5130, YIP3, Prenylated rab acceptor 1 and related proteins [Intracellular trafficking and secretion / Signal transduction mechanisms]
MMQLGLSIIQEEKTFSEIYRSIKQALGDKDVTREFFNIGRISVPQNFNEAQSRVFANLDRFSSNYLAIIA
ILTIYYLLYNLLLLIVIGIVVAGVYGIRKLRGRPLVCNIELEPRSVLYAGLVCVLIPFGFFASPIVTLLW
LSGASGVVVFGHAALLEEPLEKDFEEQQV
>gnl|CDD|444057 COG5131, URM1, Ubiquitin-like protein [Posttranslational modification, protein turnover, chaperones]
MVKVILKGPLVSLFGAREIEVKGSELRDVLKKLDSEKRLLSEDGKIRPGYLILINGVDWRLLDTQLNDND
IVEIIPINHGG
>gnl|CDD|227461 COG5132, BUD31, Cell cycle control protein, G10 family [Transcription / Cell division and chromosome partitioning]
MPRIPTNRSKPAPDGFEKIRPTLEKFEAEMRQAENAPLAPSKPENLWPIFQLHHQRSRYIYNLYYKRGAI
STKLYGWLSKNRYADHELIAKWDKVGYEKLCCLRCIQPIESKHGSTCICRVPQRNLDVSQRLKCDHCGCR
GCASYD
>gnl|CDD|227462 COG5133, COG5133, Uncharacterized conserved protein [Function unknown]
MAEFLNENPDIKEMNQLPFRAESEEDLLLGSSLEERHPIESENGVLQNEEPDLIDQQEIYDLIADIRDPE
HPLTLEQLSVVSLEDISVPDGIAPNVIRCVKVVITPTIPHCSMATLIGLCIRVRLERHLPPRFHVQVHIK
KGTHISERQVNKQLNDKERVAAACENEQLLDVMEKMLPTCK
>gnl|CDD|227463 COG5134, COG5134, Uncharacterized conserved protein [Function unknown]
MGKYIPPEGNRVLAQPLAKRKFDKLKNARPRGLSIRLETPFPVRCLNCENYIQKGTRFNAVKEEIGDKSY
YTTKIYRFSIKCHLCSNPIDVRTDPKNTEYVVESGGRRKIEPQDINEDPAKAENVEKVPESDAIEALEKQ
LTQQKSEKHNSSAINFIDELNKRLWSDPFVSSQRLRKQFRERKKIEKKQEAKDLSLKNRAALDIDILPSS
SDKDKALLLLDNELGKNKFIRKLDYRRTPSSRTFSTFAKFAETSFAKKDPFARKFVPSEKLR
>gnl|CDD|444058 COG5135, COG5135, Uncharacterized conserved protein [Function unknown]
SLAPWRSPLARALHRNRSPPYSRYLQLATVTGDGRPANRTVVFRGFLEDSNQLKFITDARSEKVDQIQQQ
PWAEICWYFPKTREQFRLSGKLTLVTADDPDPDLQKARQQTWQELSDAARLQFAWPAPGAPREEPEAAFS
PPPPDPDQPLPNFCLLLLEPDQVDHLELRGEPQNRALYHLDDDGEWSGQWVNP
>gnl|CDD|227465 COG5136, COG5136, U1 snRNP-specific protein C [RNA processing and modification]
MPRYFCEYCNKMLTHDRLSVRKMHCGGAKHGLMRKDYYMEMAEDIAAEMASILRDIKTAGEKVECEGNKS
TSYPPFPAFPPGDFYLNLALPEPPKGFVLANGFDFRDKKNAPENITEAIERYAVNLTNQVAFSAPQTTAS
SNTQLTQQQQSLPQTNEHQRARTHSNANNHFTKTHHQGQRSHQRFVRA
>gnl|CDD|227466 COG5137, COG5137, Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics]
MSIVKLLSIEVLNNPAKFGDPYKFEITFECLEELKCDLEWKLTYVGSVHSDENDQVLDEILVGPIPKGKN
KFVFDADPPDVNLIPLSEMFGVTVILLSCRYKGQEFVRVGYYVNNEYPGITKLEKSDVEEPSEKVDEEDV
EREILAEKPRVTRFNIVWDNDEDNDEAPPAQPDVDNEEEERLEESDGREEEEDEEVGSDSYGEGNRELNE
EEEEEAEGSDDGEDVVDYEGERIDKKQGEEEEMEEEVINLFEIEWEEESPSEEVPRNNEESPAKKQKVE
>gnl|CDD|227467 COG5138, COG5138, Uncharacterized conserved protein [Function unknown]
MEYYDIDDILLGESRIPCTFKHKIPGLGFLGPRGRILPENRKVELPYWLASFLAINSFVCELGPGFFSES
VLNAIKAKPSTVDLRSICPHFFYLAEKYAMLLSEGSLVAGLPEFLYERAGDYSSASLNLKGTFSENSQFV
WRLDMVEKSIVVGSHRRFQRFCAWLVAR
>gnl|CDD|227468 COG5139, COG5139, Uncharacterized conserved protein [Function unknown]
MSTADQEQPKVVEATPEDGTASSQKSTINAENENTKQNQSMEPQETSKGTSNDTKDPDNGEKNEEAAIDE
NSNVEAAERKRKHISTDFSDMSLLRKRKNDQSLQPTREPMDSRDSGQDFTEAQSGELGDTGDRQLKAPAA
SRARRKEDLLEQTVDEISLRLKKRMQDAAKKDNANNLEGRPATGKIKNLPEVSDVLMKKALQDTILDNNI
LDSVRGWLEPLPDKSLPNIKIQKSLLDVLKTLPIHTEHLVESGVGRIVYFYTISKKEEKEVRRSAKALVQ
EWTRPIIKPSGNYRDKRIMQLEFDSEKLRKKSVMDSAKNRKKKSSGEDPTSRGSSVQTLYEQAAARRNRA
AAPAQTTTDYKYAPVSNLSAVPTNARAVGVGSTLNNSEMYKRLTSRL
>gnl|CDD|227469 COG5140, UFD1, Ubiquitin fusion-degradation protein [Posttranslational modification, protein turnover, chaperones]
MFSGFSSFGGGNGFLNDLFQLFGEKPRCYPRAMKFDGCRQNANFGGKVILPPSALVKLSSLNIQYPMLFE
ISHSDGIYRTHGGVLEFIAEEGRVYLPSWMMQTLSMEPGDLVVLRYTDFPLGKFVKLIPQSVDFLDIEDP
KAVLENCLRNFSTLTEGDEIEIQYNDEVGSIKFTVVHPEPSANAIYVVETDLVVDFLPPIGYKEKAQQDK
ERNSFGVQGTMATYIEYIDSSHDVKPILMKGLGLYLYGKVDKAEPKQDIKDMKIDGEPAKLDLPEGQLFF
GFPMVLPKEDEESAAKSSEQNFQGQGISLRKSRKTKSDHDSSKSKAPIEID
>gnl|CDD|227470 COG5141, COG5141, PHD zinc finger-containing protein [General function prediction only]
MQTFRLTSTGRNILRPDELAFQPREEIPYKSFHPDLQIDEPLEILEGDHTMYRKKKFSIPCGKSWNPSMS
TSGWLGGKPRNEKSYKAQYRNLELPRMHKFVSKHAPMSEESHDEGKKFIDIEPPRGLFFSVIYDLDEYDT
MWLRYLNESAIDENVSEEAFEIIVTRLEKEWFFFEHGLPDKHVEPIEPSDEFDDICTKCTSTHNENSNAI
VFCDGCEICVHQSCYGIQFLPEGFWLCRKCIYGEYQIRCCSFCPSSDGAFKQTSDGRWGHVICAMFNPEL
SFGHLLSKDPIDNIASVSSSRWKLGCLICKEFGGTCIQCSYFNCTRAYHVTCARRAGYFDLNIYSHNGIS
YCIDHEPLCRKHYPLGYGRMNGLRYFGYEKLRYKNPPTAIPRKVRAARPRATLFMKLCWKQPPATPSVLS
RVEACDLKEKDRQDLPVNIFDICKYWEMKRKSEIGGPLVILPDIVYSLKTLEDWMSKRRMREVAKALQDQ
YQLLTLVESTAKRQLLKCQLSNLRKKFLNLNYFPAQRLLQVKIIDLDVDGLFNMPLDNELKRQVFSYQIG
SISSLEKKLEPIWDVDVIQCIDDMEQLTAMVQFAQKTEGEVKKLFIKAKIYFESLSLDELKVPSLGINGL
EYDNWPGLNELEMSQLDIPSQGNLKSLHDFIEGLDLNEK
>gnl|CDD|227471 COG5142, OXR1, Oxidation resistance protein [DNA replication, recombination, and repair]
MGIGNCKDYLFDSSLPDLPELQFDLMHDGKSYKASLLTEEIVTRIRESLPDRYKYSTSWRLLYSLFENGF
SLRTFYESFGENEWPFRRVGFVLACRDKDGDLFGAFFEDRIRPARHYYGRDEMFLWKAARRPADRLADKE
VAVYPISGGKGFGIYCTPDFLAFGCGGGRYGLLIDKSLLDGESHPVETFGNCLLSSKGHFFRIVYLELWL
VQ
>gnl|CDD|227472 COG5143, SNC1, Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion]
IASISLFRVKGEPLRTLSDAESLSSFSFFHRSKVKEVLRFLSKTSASRASIESGDYFFHYLKMSSGIVYV
PISDKEYPNKLAYGYLNSIATEFLKSSALEQLIDDTVGIMRVNIDKVIEKGYRDPSIQDKLDQLQQELEE
TKRVLNKNIEKVLYRDEKLDLLVDLSSILLLSSKMFPKSAKKSNLCCLIN
>gnl|CDD|227473 COG5144, TFB2, RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit TFB2 [Transcription / DNA replication, recombination, and repair]
SQAWPYKISIIEYLEMLPRHSKTRLYGAPAFCLAFLRVLPELATKFVMDMLFNSHSVSLLDEDEWIKETL
KILLRIQVIGKKGNHIYLDEGLMIRLNPEFKISLMDALTGGTMENSFGVCIGEKLVSVDMLDSYSSRKWE
TILHFMVGTPEAKIPAEGVLELLKFGGLMGRDRNEFKITNRGFQFLLQTINEQLWTLLLLYLKYFEGSVM
DEVAVLHFLFMLGALAVGTAYKIDALSDTQQIMLMDRRLYGLVEQLGILRKIFYPTGLAIGLTFDQLFEA
SEQNRREDDKGFIIVETNNKIYAYTNSPLQIAVIHLFCNLTARFPNLVKGIITRESIRRALDNGITAKQI
IHYLETHAHPQMRKKLELLPPTIVDQIVLWELERNRIFMVPGYLYSDFLTLSDYQKVLEYAIRGGVLVWS
DVDKRMFFIKLEGHSLVKEFVKRILKK
>gnl|CDD|227474 COG5145, RAD14, DNA excision repair protein [DNA replication, recombination, and repair]
MENSSIVKSPNPTIEEQRNEIEKLKNLTGIEEVHVDGAKVNKRKRTFDEQSEITKDYIEYDFSKIEDTKG
GYLLEEKKVEDLMENAPQEGEFFAEEQDERKEVREDAPILLPIALAPKCKECLQIELDDELEDTFGISVC
RSCRHSMPDKYKLLTKTECKSDYLLTDPELKDQELFRRLQKPNPHKGTWSKMHLYLREEVEQFAIKKWGS
LEELDREKQRREKMKDDRKEKKLEKKIKELRRKTRTSNYSRMDVREKEKHVHVFDEFVDGPNEPGVIIQR
CSCGLEVEQEEI
>gnl|CDD|444059 COG5146, PanK, Pantothenate kinase [Coenzyme transport and metabolism]. Pantothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
GMKIGIDAGGTLTKIAYLEDGERRYKKFPSDEIESVADWLNKFINIEKIGLTGGRAEVLAEKLNGDPKQY
IVEFDATGKGVRYLLKEEGHDIDKFIITNVGTGTSIHYMDGDTQERVGGTGVGGGTLMGLSYLLTGISDF
EEIVELAKKGDRDGIDLKVKDIYEGMEPPIPGDLTASNFGKVLITLDESATKEDILAAIIGLVGETITTL
SIQAAEEYDTETIVYIGSTLTNNPLLQEVIESYTILRGKKPIFLENGEFSGAIGALLLLT
>gnl|CDD|227476 COG5147, REB1, Myb superfamily proteins, including transcription factors and mRNA splicing factors [Transcription / RNA processing and modification / Cell division and chromosome partitioning]
DTSLHNKELQIKLMQTKRKGGSWKRTEDEDLKALVKKLGPNNWSKVASLLISSTGKQSSNRWNNHLNPQL
KKKNWSEEEDEQLIDLDKELGTQWSTIADYKDRRTAQQCVERYVNTLEDLSSTHDSKLQRRNEFDKIDPF
NENSARRPDIYEDELLEREVNREASYRLRVPRVSKADVKPREKGEENNPDIEDLQEMKELKSASITRHLI
LPSKSEINKAFKKGETLALEQEINEYKEKKGLSRKQFCERIWSTDRDEDKFWPNIYKKLPYRDKKSIYKH
LRRKYNIFEQRGKWTKEEEQELAKLVVEHGGSWTEIGKLLGRMPNDCRDRWRDYVKCGDTLKRNRWSIEE
EELLDKVVNEMRLEAQQSSRILWLLIAQNIRNRLQHHCRDKYGVLISNSSPFDAGAAIWLIERYSNRKIQ
NGDLIKWRNSVLDSARRRMRDLKDLPEYALLLRTPDYNKSSLERIKKSAIDDGKKVLSLTLRELNKESSP
ERNYISDFKDSATAFIIIQRLC
>gnl|CDD|444060 COG5148, COG5148, vWFA (von Willebrand factor type A) domain-containing protein [Function unknown]
MPWWLLSVYPVLILMGGYEWLQFRRRWYAIKFFNVDLLYTLAKKGEGWRRALFAIAAVLILFTLAHPMAR
PSYDTIEPKERATVMLMLDHSLSMAADDIKPYRFEVAREAVKKLVKKLPPDYNLGLVLFAKSADVLVSPT
KDKNAVLSAIRDLKPLKGATNLGEAVFSALDAITGKRRIVILVSDGGDEDISKIVQLVKGSQLTVVYYGS
VPVDGAGGPGPARISLLSDGYRTSARSVEGGMVAASAADVPVSTIAFGTDTGSVKIKGELQKVPVDRELL
PQIAELTLGLFYEAASVSRLKAVY
>gnl|CDD|227478 COG5149, TOA1, Transcription initiation factor IIA, large chain [Transcription]
MSNSIVGEVYHHVILDVIANSRSDFEENGVDDATLRELQNLWQSKLVATDVATFPWAQAFPIGQLFGLRT
DSLDVTAPAVANSPILNQSATNISFDSSAIPNVQSNNTAPFPSYSSTNQTADSPIINDHSTANLKIYGDI
IAEVISLPNRLEQVEDELSIGKSAITTLRNTDWRERLIDDTQSEWDGERMRRRDGKQGIHQYERLSEGPA
HAFKGKPTTAKDEGMFSDLDDSDVDSGDSEIEGTKGSTNCMLCLYDKVNMSKGKWKCTFKDGVVSINNID
YVFNKAQGELEWI
>gnl|CDD|227479 COG5150, COG5150, Class 2 transcription repressor NC2, beta subunit (Dr1) [Transcription]
MNMEKNDDENSLPKATVQKMVSSILPKDLVFTKEAREIFINACIEFINMLSSEANEACEEEAKKTIAYEH
VIKALENLEFEEYIESCMEEHENYKSYQKQKESKISKFKDSGLSMEELLRQQEELFQNARLRFEHSFEDD
PVKGDNDG
>gnl|CDD|227480 COG5151, SSL1, RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit SSL1 [Transcription / DNA replication, recombination, and repair]
MNENQKSFDSDKSESEDEQKNGRVKVRSRKTDDMNKGYSWEQEYKRSWDDVNDDKEGSLVGVVAEFNLET
KAPYSNNRTTPLQRGIIRHLHLILDVSEAMDESDFLPTRRANVIKYAEGFVPEFFSQNPISQLSIISIRD
GCAKYTSSMDGNPQAHIGQLKSKRDCSGNFSLQNALEMARIELMKNTMHGTREVLIIFGSTSTRDPGDIA
ETIDKLVAYNIRVHFIGLCAEVAICKEICKATNSSTEGRYYVPVDEGHLSELMRELSHPTDFNGTKTDLS
LVKMGFPSPMMEQLPSVCACHSEVKGGGYECPVCKTKVCSLPISCPICSLQLILSTHLARSYHHLYPLKP
FVEKPEGTNPKSTHCFVCQGPFPKPPVSPFDESTSSGRYQCELCKSTFCSDCDVFIHETLHFCIGCELPH
N
>gnl|CDD|227481 COG5152, COG5152, Uncharacterized conserved protein, contains RING and CCCH-type Zn-fingers [General function prediction only]
MFRKRLVNKSSSDEKNQKKRQKINFSEEKLVASDEEKGSSDLMSLAKSGNSRTLQLSHENEGKLQKKGED
LDKYTLTVNDDSTKEDLLNFERKELAEKAKKRRPSDDNELVLNMSGKNKRLTKQINQPTMFRDGEVIDTQ
PDVCKDYKETGYCGYGDSCKFLHDRSDFKTGWKLNQEWNAEYEEAPVISGPGEKIPFLCGICKKDYESPV
VTECGHSFCSLCAIRKYQKGDECGVCGKATYGRFWVVSDLQKMLNKRKS
>gnl|CDD|444061 COG5153, CVT17, Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) [Intracellular trafficking, secretion, and vesicular transport]
MQSISEIVYEKLADAATALDIDPFRAANDDIDGHFAVALDEKAIYDTIIAFRGTQGKPDWKTDINASLHD
YDEKNKEADEKLPLQVHEGFEQYAAQVMDLDYDGAEELAAEVKKQYPDAELSLTGHSLGGALASLVAVAT
GLSKVTFAAPGSGNHALADDLGKRIDAGEFVKSLDAVAGPGDSFFGGAFKQFGHVGEFNHIGNDSGTAHP
AKFTIPLAIPLERDSEDGALFLGLKQKPILAQPIGKKMMQADAFTKFEDSFDGGEKPDGGEFFLDDENGM
LPRPLVLDDGHEKEDNFRIEAGELMKAAQAAGAQVLGDLTEDIGGLGGAFGFFAALALGVNLLEAGGLDR
ANGGATFVGFDNGLTIALLPEEEDHAANIMNLLLFGFSEDRLANIQLFDAHIENH
>gnl|CDD|227483 COG5154, BRX1, RNA-binding protein required for 60S ribosomal subunit biogenesis [Translation, ribosomal structure and biogenesis]
MSTVYKLRAPKNEDEDEEYVQGNSAGFVPKQTSLILSSRGVSYRIRHLMKDLSRLVPHSKKEQKLDMKKN
LGQLNELAELYNCNNMLFFESRKRSDLYLMGARIPNGPTVKFRMHNLHTMDELNFTGNSLKGSRPVLSFD
KEFEDIPHLKYAKELLEHIFGIPKGARRSKPFIDKVLCFFILDGKIWVRCYEIGRENEDKSKDVKLEEIG
PRFVMTVIKILEGSFGGPAIYKNETFVSSTMVRAAIRNQAAENLFARKESNLERQVRAQQNVIPEDPLDN
VFA
>gnl|CDD|227484 COG5155, ESP1, Separase, a protease involved in sister chromatid separation [Cell division and chromosome partitioning / Posttranslational modification, protein turnover, chaperones]
MMVKQEEPLNEISPNTPMTSKSYLLNDTLSKVHHSGQTRPLTSVLSGDASSNSIGILAMHNNIIRDFTKI
ASNNIDLAIEDITTVDHSLNSIYSLLKSHHMWGHINSTVKQHLMIIVKLINNNALGLASSEIIFLFNETN
LFQAHSLKNILLADFSTWNDYYLSNLKILALQIILKRKLVDEYLPHILELFSHDKRYLLKDPNLKAHALT
KIVLSFFSVTTSCKVLFGLKFLQYIKQFKLPFKKFISNITVECFSKNLLHKNYLEMGPNKIYLNSFYLSY
SMLYDGLDKIMLLDILSYEETTEVQRAIKSKKEFNEYCNMSENRLLWSCISVDDLNVILENATNFLQNKG
KHISATLKCLVCLWSTIRLEGLPKNKDILRQFDCTVIYINSNIKSINDESAAALLSELLGVLSEICIDYK
EPKRLSNIISVLFNASVLFKSHSFLLKTANLEISNVLISNDSKTSHRTILKFEKFISSAQSAQKKIEIFS
CLFNVYCMLRNDTLSFVFDFCQNAFIHCFTRLKITKFIEFSNSSEIMLSVLYGNSSIENIPSENWSQLSR
MIFCSLRGIFDLDPLELNNTFDKLHLLNKYELLIRIVYLLNLDMSKHLTTNLSKITKLYINKWLQKSDEK
AERISSFEMDFVKMLLCYLNFNNFDKLSIELSLCIKSKEKYYSSIVPYADNYLLEAYLSLYMIDDALMMK
NQLQKTMNLSTAKIEQALLHASSLINVHLWDSDLTAFQIYFGKTLPAMKPELFDINNDHNLPMSLYIKVI
LLNIKMFTESQKEFLEKGRFIGKPCRATSTRRNTEAIRMVNSILKAPTRSLGLFGLESVSCLYIYEPMLG
IPRYRLCKALVSLCSKVIVRDLYEEIERRIKLHLLRMLYRDVESICESMGFLDYADSSLDEIIVGYLIIR
YKEYLEYNKEAWKIVERVGPRLKAKAKRTFASLLNGWVGSCLLEEKIERLLSSRRRKAAVSVEKKNITHV
LTRDEVEYFFENYPLVSSFLNIPEDLPVIGTVPYLDLRRPFNHEYFDEVCCWNGFTENTSMRGGASREKL
LRDLGLLKLICFRMCREREYDLELMRHELSKIKSSSSFERAFLEGITKVVCQESSAAKEFTLRPMVLEII
RGMGMASIHNIQLCEYDLSSLSHMFNGEYFESVFRLNRGVEDSCKSRLNFVAITILNCTGKLVVSKIGGV
HGPTHLRLPLIRSNSRDLDEMILPFHVAVNELKVIINRSNQNLALKDEMSNLREIRKTWWLERFALDRPS
QQLLDNIEISWRLGRYGVFSPYCIDGSLFIKFFKGFIRIDKDNFRGAKTRMNPILARWVIELFLKLNPQE
IDSRDILEDLIYFGLDIARFWGQRNAYDEIDLDALLGKLLSDIGSYFNGLSVGSIKHTILVLDESTHEFP
WESLPVLRNKSVYRVPSLEYLENALSSFHYQLPLQGASGRSFSYILNPENDLPKTQERFAGQKFLESSGI
TNLVTGRPPSDLECKMLDGCDVFLYFGHGGGEQYLKSSEIKKCGEGATMLLFGCSSVALLCMGNYEPNGT
ILKYLRRGCPMVVGNLWDVTDKDIDSFSARIIESLGSGCNSLGELNSLSVSYAVSRSRDGCHLRYLNGAA
PVIYGLPIKFVS
>gnl|CDD|227485 COG5156, DOC1, Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / Posttranslational modification, protein turnover, chaperones]
NPTPENLQHMFHQGIEILDSARMINVTHLAEWRLSSFKRGHPLRELLDDNMDTYWQSDGVQPHSIQISFD
KRRYIQSVQLFLSFTQDESYTPSKIGVRAGLTREDVREISSVEVVEPEGWVTLSVADKREDDLLKCIYIL
VVINSNHQEGKDSHVRHIKIYEPSTEEIYYKIEWAQTLPETNNVFQDAI
>gnl|CDD|227486 COG5157, CDC73, RNA polymerase II assessory factor [Transcription]
MANSLDLLKKALRDPDACQLSPEEIVSGGKKVPPKQMVKFKGTESKEYTFEQNEETEIEIDSLVQLRIVL
FYWLNRDKSYAVYMTLCRESGIGNIYFLDRTDLIEWLEGNTESSQYLKAPGQKKETSSTTSISARIDSEV
SDPVVVETMKHERILVGHNSRLIGLKPISFLGLLKDKEDKLVQSEGGSLGHKGAHGRPTKYYAKDPIILV
PQSASSPLTLSNIKEFLEEGKYVNPRNLPSCSDGIRISEVEKVELDLDGPFRFIIVDDTGGFKPEYWDRV
VCIFTTGSKWQFGRYNWRDPGELFNTIKGFYFARRGDQSNLYMRNWNVEEIGVHDGKRFVDREVVSSIWE
RLEGCILGRGYR
>gnl|CDD|227487 COG5158, SEC1, Proteins involved in synaptic transmission and general secretion, Sec1 family [Intracellular trafficking and secretion]
NMDLLELQKNKILDEIFLVQPANIWKVLLLDKDTTSILSSLITTSELLEHGITLVDLIENKREPISDLPA
IYFVRPTKENIDLILEDLEQWDPFYLNYHISFLNTVTESLLELLAESGVFEKILSVYEIYLDFFVLESDL
FSLNLPESFLESSLPSTTEALIKIVNGLFSLCVSLGRIPIIRYSGGKNAEHMAKKLSDEIRNELSINFDG
VVSKNPLRPILIILDRSLDPITPLLHQWTYQAMLHDLLGINNNIVTIPSSSVNGPEKKFSLSDKDDPFWN
DNKFLNFGEVGEKLKKLAKELKTKAQLRHKENAKSVNDIKEFVDKLPELQKRSRSLNKHLTLASELLKVV
EERYLDDFSEIEQNLSTGNDVKSDISDLIELLESGVEEDDKLRLLILYSLTKDGLIKDIDELRLLRIQGY
GIEALNFFQRLKELGFLTLKDSKTISLKRGDKDSLFQWFNTYSLSREHQGVPDLENVYSGLIPLKKDIPI
DLLVRRLFEPLKSSQQQSLRLSRPKGRSRSNKKIPQQRILVFVIGGVTYEELRVLYELNESQNSVRIIYG
STEILTPAEFLDEVKRLGGSRS
>gnl|CDD|227488 COG5159, RPN6, 26S proteasome regulatory complex component [Posttranslational modification, protein turnover, chaperones]
MSSKSSLELANNAVKSNDIEKAIGEYKRILGKGVSKDEKTLNEQEATVLELFKLYVSKGDYCSLGDTITS
SREAMEDFTKPKITKIIRTLIEKFPYSSDSLEDQIKVLTALIEWADREKRKFLRLELECKLIYLLYKTGK
YSDALALINPLLHELKKYDDKINLITVHLLESKVYHEIRNVSKSKASLTAARTLANSAYCPPQLQAQLDL
LSGILHCDDRDYKTASSYFIEALEGFTLLKMDVKACVSLKYMLLSKIMLNRREEVKAVLRNKNTLKHYDD
RMIRAMLAVAEAFGNRSLKDFSDALAQYSDELHQDSFIRSHLQYLYDVLLEKNLVKIIEPFSVVEISHIA
DVIGLDTNQVEGKLSQMILDKIFYGTLDQGDGCLIVYGEPAQDNTYDEALEQVEALDCVVDSLYEKASAL
L
>gnl|CDD|444062 COG5160, ULP1, Protease, Ulp1 family [Posttranslational modification, protein turnover, chaperones]
IIFKCLCYFHTLYQGLINLEGEPPATIFNFKQKIISILEDLSSVLRGEPIKGSLPLCCSSENYRRHLHGT
TLLPVFMWYHPTPKTSSDTSQQMKQLAIAGSVGASETNWLNDQHLGAYSLFLAERLQPNAFLLFFAWTYV
VPGLTDRFQKEDAYHILDVRAKPIIFLPLNIPNNHWSLLVVDRRNRDAVYYDSLYNYVSPEDMEQDLQDF
AQYLLQVDPAYDSQKFYTKIAAKPVAQQPDGYSCGDWVLQFLEWYLRDPFTDLNDLPVDSVESFVQACEA
AVQDLPELWPEAKALF
>gnl|CDD|227490 COG5161, SFT1, Pre-mRNA cleavage and polyadenylation specificity factor [RNA processing and modification]
MNYLYSDESDWTVTEGCSAGLFTPSRTCSLLVYNGNILAVRLWKYDSGLVLVDEHMLLEKVTQIEKYPQI
SSEQDGLLLLTHRAKISLLRFDSQANEFRTISLHYYEGKFKGKSLVELAKFSTLEFDIRSSCALLFNEDI
GNFLPFHVNKNDDDEVRIDVDLGMFQMSKRHFSIFPSQGTNTFNKRKRTLFPGKFSAPSKVLKFSELDGK
IKNIIDFVFLENYSIPTVALLYDPKLSLPRKYTILKNPYNAIVFTLDLGAGRSAVIDEFLVLPRDFRVTV
AGPVGALLFGSNELILIDSTGSSYTIPLNSMSEKYGGNKIVEDISLSDVNCFSRGTTSIWIPSSKCLIET
LFLGDLNGDRYYLRISMDGKRIIGFDIASLEFEGDLLKKGSAVSCVGHVNNLLFFGGVGDSNSRVLRIKS
LLPTIETRASEGVGPLEGGNDEEMDDEYSAPENKLFGNKEQEVRRQDEPYDAELFNALSNAGPITDFAVG
KVDVEKGLPIPNIGLLNLVVTKGSDSEAALAVEGTSLEPCICTVSSFIPLEIVWSQKIRGYLRCSRALDF
YILSRVSDSRIFRWSEEFLLEVSGEYTRDVNTLLFVEFGEENRVVQVTPSYLLRYDQDLRMLGRVEFASR
AVEARSVRDPLILVVRDSGKILTFYDREKNMRLFKIDLVTCLADAKNKSFVLSDSNSLGIFDIGKRISQL
EPCLVKGLPYAIQFSPEASPAMDLAGEEDGDDQLTEISMSLTYNLIDMLFRLPSIGNYMVAYLGLDLKEE
YLFDNSLSSEIVFYKTHLPRHVSFNLNVTRNDLAITGAPDNADIKAFSSVGRIDMVFIKAVGHSFMFVTG
KGPFLCRSRYTSSSKAFHRGNIPLVSVIPLSKRGYLMVDNVLGVRASQYVFDNGYVGNKNPVKRTPKHKT
LQKLVYHCAGRYMVVGSCEEAGFSPKGEDGESGIPVDTNVPHAEGYRFYVDLYSPKSWEVIDTYEFDENE
YVFHIKYLILDDMQGTKGKSPYILVGTTFIEGEDRPARGRLHVLEIISVVPSPGSPFTDCKLKVLGIEET
KGTVVRVCEVRGKIALCQGQKVMVRKIDRSSGIIPVGFYDLHIFTSSIKVVKNLLLAGDIYQGLSFFGFQ
SEPYRMHLISSSEPLRNATSTEFLVTGNELYFLCCDAKGNIHGLTYSPNNPISMSGARLVKRSSFTLHSA
EIKMNLLPRNSEFGAGFKKNFIMVYSRSDGMLIHVVPISDAHYRRLLGIQTAIMARLKSVGGLNPRDYRL
NSDIHLHSLSLRSPLDLHIINLFSYFDMSTRESVASKAGRIDRKEISDMIASLNLLRSL
>gnl|CDD|227491 COG5162, COG5162, Transcription initiation factor TFIID, subunit TAF10 (also component of histone acetyltransferase SAGA) [Transcription]
SDINNNEPAENIEQQEGNDEQPETSSTNLPTGDNLAPMSVESPMRLGICSHTLCDDIEENIKQHPHNPRM
KDKTLEELLQNMDSYTPLIPDSVTDYYLEKAGFVTSDQRVKKLLSLLAQKFVSDIAVDAYQYSRIRQGSS
NAKATAQKAKRFAKGGASGIGSSGRRGDRKKPVLTVVDLSKALEEYGINISRPDFYR
>gnl|CDD|227492 COG5163, NOP7, Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure and biogenesis]
MRIKGKNYIGPARKYITRGQAMKKLQLRLADFRRLCILKGVYPREPKNKKKANKGSTAPGTFYYIKDIQY
LAHEPVYRKFRENKRFARKLKRALGTGEFEYAKRLEICDEEYGLDHIIKERYPGFGDAVDDIDDALSMLF
LFSMLPLTDRISSKIANDAQEVCEMFEDYVRRRSLLRKSFMSIKGVYYQATIGGEKVVWFVPYKFPENIP
GDVDFRIMLTFLEFYSTLLHFVSLKLYVEEGLDYPPKFDWSKPNFLDGLSSYELEESSSLPTEIEEDVKV
ESLDSSTLKSAVCNDPGNIDVSKEELSEKIPELMVECRLVEEKLDTFEDNNKNKDIMEMVSKPCSSLKSL
FSGFKFYISREVPGDSLEFIILSCGGSVVGSPCEADIHVSEKVDEKVTHQIVDRPVMKNKVEGRTYIQPQ
WLFDSINKGKLACVENYCVGKRLPPHLSPFASVDSYDPRASLMTMEETQRHSEEDLVNRFEDVRYEHVAG
EEDDDDDEELQAQKELELEAQGIKYSETSEADKDVNKSKNKKRKVDEEEEEKKLKMIMMSNKQKKLYKKM
KYSNAKKEEQAENLKKKKKQIAKQKKLDSKK
>gnl|CDD|444063 COG5164, SPT5, Transcription elongation factor SPT5 [Transcription]
TGLYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQG
ATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDG
GSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVK
KDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEAENRAANPEPATKTIPETT
TVKDLATVLGKKGSDLVTNLMKKGKGTNINAALDFETAATIALEGNVITEKEIEADIMETVTTEEQETDS
LLEETPPVPVVMGHVDHGKTSLLDAIRHSDVTDGEVGTISQHIGAYTVQIAGTPITFLDTPGFESFTAMA
MRVAQITDIAILVVAADDGDMPQTVEGINHAPTAGGEIIVAINIMDKPSANPDRVKQELTEFQLLKEDAG
GETIR
>gnl|CDD|227494 COG5165, POB3, Nucleosome-binding factor SPN, POB3 subunit [Transcription / DNA replication, recombination, and repair / Chromatin structure and dynamics]
VLTLNDCIYLNDSDKKGTVRIARSGLGWKASDSERKPFTLPRNEVKDAEWSRGVRGYKLKIRVKGNAVYE
LDGFSQNDIDELKNIFSEYFRITLEQKELSIAGWNWGELGINGQEAVFFRNTKPIFEIPVDDIENTNLDI
KNEVSVEFRIQDEEYQPAGDELVEMRFYSPGVKTKEDIAGGESVEKSMAEAFYEELKEKADIGESAGDAI
VSFEGLSLATPRGRYDIDFYRDYLRLRGKTYDYKIYYKSIKMLYVLPKIDDGHRYVVIGAEPPLRQGQTR
YPFLVVQFQKDEDVEVELNVEDEDYEENYKDKLKGEYDGLLSEVFSEVMEGLTVRKVVRPSEFESRDGMR
AVRCSMKANEGQLYPLDDCFLFLPKPTLRLDLSDISLVEFSRIGLSSMQARTFDLTLFLRSPGSYTFNNI
SKDEQGALEQFLHSKGIKARNEEVQERLQTDLGSISDSEDINMGSAGEEDESEDEDFQMVSDSDVAEEYD
LQAALSDAEGGSDEERPS
>gnl|CDD|227495 COG5166, COG5166, Uncharacterized conserved protein [Function unknown]
MDSHVLAFPIPDPSTPPPEEASLYASKCPYYESDIYEQIRRLTEEKCLETEKELPVNIKLHVIHKGMSIS
SSRNELVVTVSGSYPNVYTAKIKLLQAIPKILRSKLVLEEPLENLLFDEDGYVYPDTMKHLDKITEITGA
KIYIMHRSMCHDIDFQLTDSGFSNGLNEQQSFYQRHLESTRHEFSCQKNAEMSFFIVIYGAFCSVEHARS
RVLALMDEIRGLSVIFIATSVSSQPILVGKAFSSTAGMKATESINIYTLPFCSDKIPRLQTYPALNSSKI
IITGQSEILQRLEISFYYAEMHLKLFTHVTEISFVKLFIFLAYNMDIMEENSSFIRFPEYFKEGVETTPE
NSKVKIYGSSIANSEKTALRIAKLASKYVQGKTQFGVEDNEDFLRGKKNGKATRIMKGVSCSELSSIVSS
TGSIVETNGIGEKMSFSKKLSIPPTEFPAEIAFIIMESGHEMIIGTGGIEIQENMVKHAVDIAFKNFYKF
GQSQWHDNVLIEAPRKNQDNISGKKNDKLDKVKQQCRFNLKGDIRFCPQSTSIFTVDIYSDEIERVIKNE
TVLLEFPAEMHFYVPSEIHKKGIGENAFRGENIQRVTKLYNSYIEFSTTPFDCYGHNVLIVTPSLFSENL
WAVFESLFEKTAEGLGYDIPKYLLANY
>gnl|CDD|227496 COG5167, VID27, Protein involved in vacuole import and degradation [Intracellular trafficking and secretion]
MNILKKFMESGNKPELITIPSGQFNLLRSKNSPKAALECIYNNATLSVRKIGKFDYELAVYRVEDDSEGG
TGDEAENFEDDTISVLSTQSKKKEEEWSVEISDKIMFHKTWDKQGNVALVWEMVLGDERIEKMLSGVKMK
SLVGDLEQFGEVLMRGCSEVASEDETASALDLVSKKGKMAFKLHQIDDAEHDNKALWFQHAQKKYLFTSN
EKELDELTKSMIPKIREGETLYSKNGVLSRYDTATERFILQKPHVKVVIVDDGKEVFWIRIETRDDVILF
EEVRTETNPYFDQKNTTFVWNYMEDNVFHSFSLRFLDNLDFLQFLSKYIGCLWRNLNNEKWGNEEAERKD
YILDSSSVPLEKQFDDILYFEKMEIENRNPEESEHEEEVEDYEDENDHSKRICDDDELENHFRAADEKNS
HLVVGFRNERSYVTRGNSIGVFKNTDEGSLEFKAAIKNVSDDGGKSIDPEKIMLHDNDSSLIYLDGGERD
KLYKMDIERGKVVEEWDLKDDVVVQYNPYFKFQQMTDEQTLVGLSDYSVFRIDPRARGNKIKVVESKDYK
TKNKFSSGMTTESGYIAAASRKGDIRLYDRIGKRAKTALPGLGDAIKHIDVTANGKHILATCKNYLLLTD
VPIKYGQPAGRDGFLKSFPASEKPKPKRLQLKPEHLAHINTYTKEEIDFTPAKFNTGIDASENTIVTSTG
PYVISWNLDDVLNGKLYSYQIRRYSALVVADNFEFGEDSNVIVALPDDVRKVNVRSLKRPGKGVLMPSAS
LRKMWG
>gnl|CDD|227497 COG5169, HSF1, Heat shock transcription factor [Transcription]
MSMSSRWSQPKEFVHKLYQILEEPEYYKLIQWSPDGRSFVILDPEEFTKVILPRYFKHGNFASFVRQLNK
YGFHKVSHKSGQRSYYNENVWEFGNKNFQLGMIELLKKIKRKKAPSNRVDSNNESKDAMMNIEVENIILP
QSELYNSLSSLSNVNQTLLLYLNELKEYNYRNLRTIDDINAMLADLSMSPFADEHLKSFLQELFGAYKEV
AEPQSPTQHQRGEPGQRFHNSVVPLADSKNEVDQKGDGKVANLQNNLSLDTATNSDSHLTIDALSAAFST
VS
>gnl|CDD|227498 COG5170, CDC55, Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms]
IMGKNEILKFKQCFGDKLDLNSSTEADKITAVEFDETGLYLATGDKGGRVVLFEREKSYGCEYKFFTEFQ
SHELEFDYLKSLEIEEKINAIEWFDDTGRNHFLLSTNDKTIKLWKIYEKNLKVVAENNLSDSFHSPMGGP
LTSTKELLLPRLSEHDEIIAAKPCRVYANAHPYHINSISFNSDKETLLSADDLRINLWNLEIIDGSFNIV
DIKPHNMEELTEVITSAEFHPEMCNVFMYSSSKGEIKLNDLRQSALCDNSKKLFELTIDGVDVDFFEEIV
SSISDFKFSDNGRYILSRDYLTVKIWDVNMAKNPIKTIPMHCDLMDELNDVYENDAIFDKFEISFSGDDK
HVLSGSYSNNFGIYPTDSSGFKDVGHVVNLADGSAEDFKVKCETNNVEKKDKLKNNDWRSVSSSADGFVV
ACEDPDNLDLLKKILHRSWHPFEDSVAIAATNNLFVFSKL
>gnl|CDD|227499 COG5171, YRB1, Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]
MSVERKKKQAKIEKEENEQKERSLDVVSKGDAFGDGKAGGEEKKVQQSPFLENAVPEGDEGKGPESPNIH
FEPVVELQRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKL
CANHFINPEFKLQPNVGSDRSWVWMSTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQEHNEKALKT
K
>gnl|CDD|227500 COG5173, SEC6, Exocyst complex subunit SEC6 [Intracellular trafficking and secretion]
MDKALTQLSETLRHDSDLQTVLDIIEQSTKFEALEHHDGNLSAEISKCLNNILNISKRIYGLEEELKSLV
EGKRRNVRVLKGFFRLVKDYRSVKMTCLAHSNLCNVVEFSDRIEDILGTVLTEDIDMPNLLAYHTKLYDA
RDFGEQLDMYATEISHDDYVTVNKAFSTLEKNSLDFDALVLEISEEIIENVKSGHIEAMDKIFKIVEKEE
ARDELTRKIRDAKSELPKSQDNPVLKEFYGMYRMYATRKTRKLKDFVIKSIEVSVKEKFDRLRNEYIFDN
SGELNMDFIFKDLSFIRENISLSFPPFDNILTLYHNNYQECLLKLFTDEVTERLDAGEILAIIEFVGNYY
NTIESKFNFIADEVGGRLLDNETGELLEKYTKLAQEKLKEWVMNLTRIEVDKFYARNEEPSRDSDGKLVL
PGTVSLFQMITQQLEPIAFTNRSDVVGIVFAHITRTITKYQEIWKSNLVEEMDKQFKSNPESSSPAGLEE
YLIAVGNDGLKIAQYITSLPSNTFELITSEYENDEVKELGKTVDGFIDILKASNTFLAEFIIYDCQPAID
KIFTDEWYGGSVTKVIVDTLQDYLSDYQNTMSEYLFVTFIHELSMSIVIAYLKQLGRKRASIAEENASRT
LKSDHTKLYEMFSGYGDPEDVKTTLSPILKIIPLMDTRNDDLFIVEVKSLKEIYWDIKKSLIKTILKKRQ
DLTESIIQKKTLADRLKECFTDVATSREPTIFSRLLNLSGSS
>gnl|CDD|227501 COG5174, TFA2, Transcription initiation factor IIE, beta subunit [Transcription]
MSKNRDNLNAFKSKVKSAPVIAPAQKKRMASPCHFEVGLNSNDGHSSTAWSKGSSPTKKARIPRMDRDRI
QSIDRGVQRHTNSYLHAAIEYLKQHDRPLSFEEIKDYLSIDLHNNYVLLLKKKRRIRIDATHSTFMFKPL
YSIRSVEDLLKVLRSQGTEEGLSMKKLMDGWPNVVPFVEELEKSNEILILRTDKDGSPVVVWNNTQNLEC
PVDPEFKSLWNQVRIPTYHDLIRELNTAGLKPTSVDPNTKKRPTIKIKKKKRSRRKGKITNTHVKGILLD
YSQDE
>gnl|CDD|227502 COG5175, MOT2, Transcriptional repressor [Transcription]
MMNVQEIHNSEDEEDYCPLCIEPMDITDKNFFPCPCGYQICQFCYNNIRQNLNGRCPACRRKYDDENVRY
VTLSPEELKMELARKEERKMREKERKEAEGQNRKHLSNIRVVQKNLVYVIGIPPKVADEEVAPVLKRHEY
FGQYGKIKKIVVNKKTSSLNSTASHAGVYITYSTKEDAARCIAEVDGSLLDGRVLKATYGTTKYCTSYLR
NAVCPNPDCMYLHEPGPEKDSLTKDELCNSQHKLHGSEVRNKNKKRIHRSTSTARYDTDLLNFTGTPSPA
AMEAQFKHKTSRVFKAPDKILFPPLDFTNTQSATPVTLSNSSSINLPTLNDSLGHHTETTTTTNTNATSH
SHGSKKKQSLAAEEYKDPYDALGNAARLHSLSNYQKRPISIKSDEETYKKWDKKSDNTLANKLVEILAIK
PIDYTASVVQFLQSVNVGVNDNITITDNTKTPTQPISQQIQPPLNVSTPPPIFGPPIQQQ
>gnl|CDD|227503 COG5176, MSL5, Splicing factor (branch point binding protein) [RNA processing and modification]
MSFRRINSRYFENRKGSSMEEKKAKVPPNVNLSLWRKNTVESDVHRFNSLPSKISGALTREQIYSYQVMM
RPFEITEKLRTPDGVPSKRELRSPSPPPRYDEIGRRLNTREARYNKKLEDERLWLKERAQKILPRFVLPN
DYIRPSKYQNKIYIPVQEYPESNFVGLLIGPRGSTLKQLERISRAKIAIRGSGSVKEGKISSDTPESLKN
AEAVLHCLIEADSEDKICRLIKSQLNAIREARRNPEGQNDLKRFQLRWLAHLNGTLRAD
>gnl|CDD|227504 COG5177, COG5177, Uncharacterized conserved protein [Function unknown]
MAHSHRSSLKGHKSYKSKHASKGALKRLYKGKVEKEPVGTGKPDKQMKKRDRRNRAKQKSIGSIARIKEN
KLPFSGKNGAYKVITIVPLGNECDGYDILDKLLHGNDDEGIMVQEVDGGLFYSVHIEEFKMNLLFKRPDE
LSFFQLGDVCKVSDIVVFGLSDVQEVDEFGEQIGRKLKLQGIKSFIPSCLFLSSVQSEKRDAAVKQSLES
FVRRFFPSKERVVEIGGLMDALNVVRILCTSVPRSINWRDNRPYIVPSEASYSDGELFYEGTVRGIGFNA
NRLKHIPDFGDFLSNKIIVNGQYEQTIREIFADRATKLELDLQTVFESNMNRDTLDEYAPEGEDLRSDYD
EDFEYDGLTTVRIDDHGFLPGREQTSKKAAVPKGTSFYQAKWAEDEEEEDGQCNDEESTMSAIDDDDPKE
NDNEEVAGDEESAIDDNEGFEELSPEEEERQLREFRDMEKEDREFPDEAELQPSESAIERYKEYRGLRNL
YTCSWRSDEKDPSFPEEWKSLVFFDNYRNAKNLVVKKDNESVAPDGQMVRIKLRFPKFLYEGLIEPQILL
VVYGLLEYEDKKTVHNFSLQRHFEYEVPLKSEESMVVQLGHRRVDICPLISKGSNSPNNNQKYFRRLKPL
ESGVASFIGPISFGLSPVIIFKKSALDELSATLLASGGMNNFDGDRVIAKRAVLTGHPFKNHKRYVTVRY
MFFSPEDVMWFKNIQLFTKRGRTGFIKEPLGTHGYFKATFSGKIKSQDKVAMSLYKRMFPEPQLPWNGM
>gnl|CDD|227505 COG5178, PRP8, U5 snRNP spliceosome subunit [RNA processing and modification]
MASLPPGNPPPPPPPPGFEPPSQPPPPPPPGVNVKKRSRKQLSIVGDILGHSGNPIYSLRVSDKPVKLGN
KAKTLHVLTLKAPIPPEHLRKIQSPCSDMPSVLTKVDKRSYLGALKYLPHAVLKLLENMPSPWEDVSEVK
VLYHCHGAITFVNEVPRVIEPQLFAQWGLCWSPMRREKRDRYSFKRKRFPPFDDLEPPLSKSQWVLGVEP
LMPINIRLDRMDDEHVRDWVYTSRDLEDHPSVNGAMYRRWKYMLPAMHNLLRLMPMLWESIRDVNYVYLF
SGLSFFVAKALNVAIPGGPKFEPLYSRESAEFEDENEFNGIVRIIRRPPIDDEYPVAFPGLYNSRPRSVA
VECYGSPECRDVFLDEDEDYPANFKDPLINPILGVQLDNHPYDGKGSNEESCVMERKLFSEPIFYPYLYN
ESTEVRTTERAHLLLKNPFPFNKGKGRAERAQDVPLDKPWLLGHCLQERPVKVPVSYQKLLKNYVRNMLH
KTRPRPHTNTHLLKELKNTKYFQRTEIDWVEAGLQLCRQGHNMLSLLIHRKGLTYLHLDYNFNLKPTKTL
TTKERKKSRVGNSFHLMREMLKFIKLIVDIHVQFRLGNIDAYQLADGVHYILNHVGQLTGIYRYKYKLMK
QIRACKDWKHLIYYAFNEGVGKGPGCGFWGPQWRVWLFFLRGHIPLLERYIGNLVTRQFEGRSDYNPKPL
TKQRSDSGYDLELRRQVMADILSMLPEGIRQTKVRTILQHLSEAWRCWKANIPWHVPGEPAPILEVIRRY
IKSKADLWTSSAHFNRERISRGAGVGKTKEKKNLGRLTRLWVKLEQERQVDSAKVGPKSTKEEAKRIGKI
TVLWLESRMFEPIPFPPLRYKEDTKILVLALEYLKSKYTGKIRLNESTREELALLEKAYDNPHDTLFRIK
KSLLTQRSFKEVGITLMRHYDGAIPVYSVDPVEKIVDAYLDQYLWYEADRRNLFPEWIKPSDSEMPPLLV
YKWCQGINNLKAAWDTSNGERLVLYETKLEGIMEKVDNTLLNRLLKLVLDPNLADYIIAKNNVVVVYKDM
SHTNHYGLIRGLQFSSFIYQFYGLVVDLLVLGLQRATEIAGPADAPNVFMDFKSRATETSHPIRLYTRYM
DDIYIVFRFQRKEEDSLLEDYLRENPDPEEANNERYRNYFKGCWPDDCRMRLGPLDVNLGRAVFWEILRR
CPHSLTATRWEPSFGSVYSKINPNLLFSMVGFEVRILPKIRKIEERSLSSGVWRLGDGRTKQRTAHANLA
VSEGGIEMFESRIRHILMTSGSTTFTKVATKWNTQLIALVTYYREAICDTKGLLDKLVKAERLIQNRVKK
GLNSKMPVRFPPAVFYAPKELGGLGMLSVGHILIPHSDLEWSKQTDTGITHFRSGMTTNGERLIPAAMRY
ISRWEYEFEDSQRVWAEYARKRQEAGQQNRRLTLEDLEMSWDRGIPRISTLFQRDRHTLAYDRGFRMRSE
FKQYSLKPNNPFWWTDAKHDGKLWSLNRYRLDVIQALGGVEGILEHTLFKATGFRSWEGLFWEKASGFEE
SMKFKKLTNAQRMGLSQIPNRRFTLWWSPTINRANVYVGFQVQLDLTGILMHGKIPTLKISLIQIFRNHL
WQKIHESVVGDLCQVLDKELDVLQIETVQKETVHPRKSYKMNSSCADILLSGAYDWCVSSPSLLLEERDG
GSNVRTNKLWIDVQLRWGDYDSHDIHRYARAKFLDYTTDPQSMYPSPTGVVIGIDLCYNMWSAYGNWNEG
LKPLIQSSMERIMKANPALYVLRERIRKGLQLYTSEPQEQYLSSSNYAELFSNSIDLFVDDTNVYRVTLH
KTFEGNLTTKPINGAIFVLNPATGNLFLKVIHTSVWAGQKRLIQLAKWKTAEEVFALGRSLPVEEQPKQI
IVTRKSMLDPLEVHILDFPNISIRTCELALPFSAVMGIDKIRDLILRATEPQMVLFNLYDDWLQETSSYT
AFSRLLLVLRALDVNEERVKEILRPDKSIITKINHLWPGFSDSQWIKKEIQLRDLILDRYCSKHNINPSG
LTQSEVRDIILGFRISAPSGARQETAETEKQNSEKALSRPTNVSTKTINGWGREYVVLDGMIYEGEKFSS
KEEWRSEAIRTGPLELRTKNIYVTADENEESIQQMYRLPLNLLEKFMRISDPHVQVAGLVYGKSGSDNPQ
IKEILSFGLVPQLGSLSGVQSSSFVPHDLPGDEDLEILGWIHTQDDELPYLEVAGVLTHRKKIVDPEWDA
VTLTVSYLPGSISLRAYVVKKEGCNWGSKNMDINSDEAIGVEPVLGKDCQLLLSDRIQGVFYVPEEEVWN
YNFAGPFFDDRLEYTWKIGMPLGFYDGFHRPGHFSRFYELRAGGRLEEWQEDAFA
>gnl|CDD|227506 COG5179, TAF1, Transcription initiation factor TFIID, subunit TAF1 [Transcription]
AIFGGEFGSLEISYIGGDEGANSKDYTEHDAVDFEDEDELADDDDDPDANLHPAMMTMAYDDVNENGAVL
IDSNSLNMQLMEAELEICCGKAAEDDGGTPAEEKAVSEAGDGPPGSRMVRIGFLDANEIGLLVIGKVYEG
KLRSIKGGKVPNESMSKYEVDTQAKLRNSMTYARDSNKTLFPLFESGRSLGLRQLLKRRPLEKEISKRRV
KKLDDPLRLVEEVKYDFDLVFNSNYVAPIKNNIIYDFSRAGGRMKRDTVTTEFVDSIDLLIATDDWERYV
IVDEADDMKTPRKSFYKLKSLTDVDWLYDEDIIDAKLKESKAPLNLNDEKLLLKRQAKPKKKQQEVFSDD
KPLNELKGKFNISNDKYYGILKKTHQSKVRNTLSTLGIQHSLPALRLDPPFYKNNHTKEELRNFHRPRFM
VRPGSNIVFSTLEARKRNKDKGKDVQEIIKTAGELTVGDTSPFSLFEYSEEEPFFLSNPGMASLLNNYYR
KSNEQDEYRPKLDVGEYHVLDVQDPSPFWNFGDVEPGTIIPTLYNNMIRAPVFKHSSGGTDFLLIVESSN
SGEMSLYLRNINHLFCVGQTFPVEEVPGPHSRKVTVFCKNRLKMAAFRLFNSKEGGSLRISQLDKHFPDQ
SEGQKRQWLKEFMDYVKDGPDGVWVLKPSEALLDEEDLRSLVTPENICQYESMLAGERKLEDSGYKTVNE
DDDEENEEEMLLPPWCLTRNFINATQGRAMLELSGPGDPTGIGEGFSFRKTSMKGGFEKSGSPVENRKSS
NKKNTHIYNVAQQQSAYKEEIDRIWSKQLASLSIVNFEEPFDESFINRRHREEVKNADLLRETTMLSEKT
LLIVRRTRDENGTSYREVERISDPRVIKAYLKARKQDKEDVNKLDTSKINNKEISEKQKKLLQLELANLE
KSQQRRAARQNSKNGSDLAGKGRKNTTRTCGNCGQVGHMKTNKACPKFSSKDNPASPK
>gnl|CDD|444064 COG5180, PBP1, PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]
VRKATILEIRLLATVPIPPNAARPVLSPELWAAANNDAVSQGDRSALASSPTRPYARKIFEPLDIKLALG
KPQLPSVAEPEAYLDPAPPKSSPDTPEEQLGAPAGDLLVLPAAKTPELAAGALPAPAAAAALPKAKVTRE
ATSASAGVALAAALLQRSDPILAKDPDGDSASTLPPPAEKLDKVLTEPRDALKDSPEKLDRPKVEVKDEA
QEEPPDLTGGADHPRPEAASSPKVDPPSTSEARSRPATVDAQPEMRPPADAKERRRAAIGDTPAAEPPGL
PVLEAGSEPQSDAPEAETARPIDVKGVASAPPATRPVRPPGGARDPGTPRPGQPTERPAGVPEAASDAGQ
PPSAYPPAEEAVPGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGGGR
ETASLGGAAGGAGQGPKADFVPGDAESVSGPAGLADQAGAAASTAMADFVAPVTDATPVDVADVLGVRPD
AILGGNVAPASGLDAETRIIEAEGAPATEDFVAAELSELREAAEEKTGDAINAEVQAI
>gnl|CDD|227508 COG5181, HSH155, U2 snRNP spliceosome subunit [RNA processing and modification]
SSNPEMEDKAEDSRRSTKQASVWYEDRNDSRGNVSQWEATPRTANESKDLKQEQTPLGYIQVREDLYSKT
RMDPGFQPDSDKKRELELNNTWDMEYPDSKRSSRWDEMGYEPPQEINMCLPARGYKALTDFHGYADLGFF
KVEDLKYFADDEKDFFMPLLEDREGDERDVYRLLLKVKNGGKRMRMEGLRILTDKAVNFGAAAVFNKVLP
MLMSRELEDQERHLVVKLIDRLLYGLDDLKVPYVHKILVVVGPLLIDEDLKRRCMGREIILNLVYRCGLG
FSVSSMRPDITSKDEYVRNVTGRAVGVVADALGVEELLPFLEALCGSRKSWEARHTGIRIAQQICELLGR
SRLSHLGPLLKCISKLLKDRSRFVRIDTANALSYLAELVGPYGIEQFDEVLCPLWEGASQHRGKELVSFL
KAMGFIIPLMSPEYACHDTREHMEIVFREFKSPDEEMKKDLLVVERICDKVGTDTPWKLRDQVSPEFFSP
FWRRRSAGDRRSYKQVVLTTVILAKMGGDPRVSRKILEYYSDEPEPYRKMNAGLVSRIFSRLGRLGFDER
LEERLYDSILNAFQEQDTTVGLILPCFSTVLVSLEFRGKPHLSMIVSTILKLLRSKPPDVRIRAADLMGS
LAKVLKACGETKELAKLGNILYENLGEDYPEVLGSILKAICSIYSVHRFRSMQPPISGILPSLTPILRNK
HQKVVANTIALVGTICMNSPEYIGVREWMRICFELVDSLKSWNKEIRRNATETFGCISRAIGPQDVLDIL
LNNLKVQERQQRVCTSVAISIVAEYCGPFSVLPTLMSDYETPEANVQNGVLKAMCFMFEYIGQASLDYVY
SITPLLEDALTDRDPVHRQTAMNVIRHLVLNCPGTGDEDAAIHLLNLLWPNILEPSPHVIQSFDEGMESF
ATVLGSGAMMKYVQQGLFHPSSTVRKRYWTVYNIMYVFDSDAMVPCYPVEEDLNPELARTLHICI
>gnl|CDD|227509 COG5182, CUS1, Splicing factor 3b, subunit 2 [RNA processing and modification]
MARTKSRKRSGNNQNKNASVVNNKAEIAAMIDARRLEQKKKGGVTNSKGKTNKVVDAKLEKEFKDVLQRF
QVQENDTPKEITKDEKNMSRMKSRKAPTIHMEAEIDDEYGFEDRMKPYREESLSRQKKRKALQHRYEQLK
LVVPYPEIFEWEDATCPDPMSLNRMKGCSNGVPVPRHWRSKSRYLSGHGYHKPRPFELPRHIIGTGIPQM
RRMMREREAGMSLRERIRERVQPKMGGLDVDYRKLHDAFFSLGPKPYLSKFGEFYEEVDNDYRFVKKKRP
GAISAELREALGIDSGTPPPWLFNMQKHGMPPSYPDLKIPGLNWAPIPLEGDVYGYQPPGWHEPLFEVGP
ETAEGELLQFEAEEIYNDEEQYTRPVYENEDFEERVDDVSNGGLAEFAPAAVEVAPKEDAKVTKRGKAKR
EKLLYSVLF
>gnl|CDD|227510 COG5183, SSM4, Protein involved in mRNA turnover and stability [RNA processing and modification]
MEKENTPMNEDKRSCRICRTEDIRDDPLFHPCKCSGSIKYIHRECLMEWMECSGTKKCDICHYEYKFKDI
YKEDMPQIIPFSILIRKVADTGWKATRVLLTIGLWCVLQMVKWMGVWNMFGKLYTMMLDGSSFNGDGYLF
AVSTGLQDTDPELTTRAGFYQLLQNSGFRNSFIWIGVGIPLTWLAQDMVNREDCLLNQIFEKFGERLSDK
DLMRRLRRRMLMNPRAILESISRESAQLERNTARQQGEHARENGRDLSSDSNNNVINPVSDNVPSRDMND
SRNVENVRPVRSNDHMNSFLFRPIVDSISGMTLPDSFSSIIYGSSSCNPTDRIHGSFGAFLSSMGLGDLY
SRIVANGVAFWANTSCTEEARKRLGIGRNRIICIFMKVYLIILLNAFFRALTFGLVDHYDFGNIMNKGMY
ALHLDNEYQSPLVIGISFIFHMSIAYTIISIVIRNIFLRFKRCFPTFILHFIPDDIDFGMDELIEASLIG
LSRLSLRLVGYLAFFTLFYGVGLMMISWICDHMGHDIRYSVRGFLKLSLSYSIFTRLLYSNKIFLDTVVK
GLCKVVRLEARMLGRENFLYNAPMERLIFDKLMLMWCANKNKIFFRIELKAFPIRRGTELEICLYFNTHP
SSDFALFYVPKLFPLRSSFIIWSIGLCFMGLFAGYIVMARKIIERPGVLAFIRDPGDPNIKILHDVLLYP
MLAQLFRLSWSVIHYAMFIIRGEGSFPFMLKSAGELCPHGIVNVYINFNTVYPLLGSLMVIVLSNDGTKP
LEMRYWKTPLRLFLRFLRLSSIVEGILSSSEEGYYRNLFRALIRELFTKPKTLEQAELGCKINAFISFVF
DGWYMYNPSTDLVGLSNGEMAVPVTVVGYEIFVEKKKGDEQNDIYSIKYVPPGFYKRLLDLLYLVWRRVV
NIDEEVTFISQALINFVCSFGFLPVVKLLLYSYLNIYYVLHFTTLDEHAVVEEVEHDIERDINNAINQGI
FMAIFSMLVKYNLMVFIAIMIAVIRTMVSWVVLTDGILACYNYLTIRVFGNSSYTIGWFKYDESLLFVVS
SMVNFGTKSLKLFFRNRFLKTMALELFKQGFLHMVIYVLPIIILSLVFLDVSTKQIIDISHSRSFTLSLN
ESFPIYFGLLIALESFTFFFQATVLFIQWFKSTVQNVKDEVYTKGRALENLPDES
>gnl|CDD|444065 COG5184, ATS1, Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]
TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVW
CWGNNSYGQLGDGTTTDRTTPVKVPGLTGVVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLT
PVQVDAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSGVVAVAAGGDH
SCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQ
LGDGTTTDRSTPVKVPGLSGVVAVAAGSSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTPV
>gnl|CDD|444066 COG5185, HEC1, Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning]
AVQRSKFLQVKNPLAKEGNANKELIEILLESSKSEGKTLVFITILFFPLGISRDSLRVTLRSVINVLDGL
NYQNDVKKSESSVKARKFLKEKKLDTKILQEYVNSLIKLPNYEWSADILISLLYLYKSEIVALKDELIKV
EKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKES
ETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRL
NENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQE
SLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADR
QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQI
ESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDG
QAANLRTAVIDELTQYLSTIESQQAREDPIPDQA
>gnl|CDD|444067 COG5186, PAP1, Poly(A) polymerase Pap1 [RNA processing and modification]
DKSTRDIKEQPATFSTKPMRTFEESYERMRWGARDAPARISLTVAEIPVHCKEYPRDKFVPGVRLPSLRE
LTVEDDADPIEPRPARPDFLDELPAGLAGRPRYLRASRFAENTPTFADPALSTLARRLPAEFTVASKPVL
PDLLLTNLSLNDRYDLHRASTARRNALLPVALQELTAVDADQIALEEYLLELLFAALGVGWVYVVSTSSF
GDVADDAGVLSLSLLSRAEVLVLGEGSLKAGTAAVADLALPPAVAAATVLTSADLEDAELRDRTELAALE
IGLAGVRAVVVLLVDLFDAEGGGFARAGKNDAWPLALPRRRPETFDPAFNPTAASLSRRGSRALLDRRLL
RRRRQEVALRAPTPDSGPPGPAPPALLDRRGFGGSTVGVRCGGVVGEPATAATTVPPRPPTVAIPPIQQV
ILAIDPPVDPPIPAQNGRLGFVPEFEFEEAAPLLLAAAAPEAEFLEALELIALRKRSTHWTTVSLFPADA
LTPWKALWARLRRRFPRRLRRSEAAAEPYTLGGQFDEPELAFAKLPVWHLRRGSRAAIALILRRLRRWFE
VRRIIDAEVSLSDRRPKEAVEPAEVGTPKLPKGARIDVLREILSAGAWASQEQRDAVVARVKQALEECLG
FGGVLHVTGSRRLGCALPGSDLDLVAVLPGYLSLEDFETRVRAALPEECSSLRRVLDARVPLLRLSLGGL
DVDLLYVDVGVCPPEEAVARRGERLDEAAARALSGVWDADALLEAVGQEGARRERFRTLLRAVKAWAKAR
GLYSAPFGGLGGLSWAVLAARTCRDASDKSDGDLLANFFGTWAAWDWRQPIALTPSGPQYGVPGPRDPVP
IITPIAPCRNTARNVTRSTLEILRDELYRAWEAVERARAERDAWAALFAPPPLHRRHAAWAVVTVEAPDP
EGREKALGWVRGRIIALLIALEGDRRAFPRPFPTAPRLARHAIGLGLRPPAAAALKELARPWAAGLHEVH
VEF
>gnl|CDD|227514 COG5187, RPN7, 26S proteasome regulatory complex component, contains PCI domain [Posttranslational modification, protein turnover, chaperones]
MRVWIKIMAVWTPMDFDFQVPTLLVSDAIFLLHGTKLGNPESKALEHLERLIIDKCMAPLYKYLAEKGNP
KTSASVIKFDRGRMNTLLKKNEEKIEELDERIREKEEDNGETEGSEADRNIAEYYCQIMDIQNGFEWMRR
LMRDAMSTGLKIDVFLCKIRLGLIYGDRKVVEESLEVADDIIEKGGDWERRNRYKVYKGIFKMMRRNFKE
AAILLSDILPTFESSELISYSRAVRYAIFCGLLRLERRDIKTKILDSPEVLDVIGSSEKLGSLVQLATSL
YECDYGGDFMNLLYLFCNSLQDDVFLGRHVDLFVREMRRRVYAQLLESYRLLSLESMAQTFGVSVEYVDR
DLGEFIPEGRLNCVIDRVNGVVETNRPDEKNQQYSSVVKQGDDLLRKLQKYVATVMRGAFKV
>gnl|CDD|227515 COG5188, PRP9, Splicing factor 3a, subunit 3 [RNA processing and modification]
MNLLETRRSLLEEMEIIENAIAERIQRNPKLPRDELRLERQIRIFENMERISNQIWLVEHERPTGLKDQM
MKRINRSIDRDLYGFYKKLGALNVEGKLDGEIEVKGLRDLGYYESSAPKARDLDVEAAFKGSELYGDGME
LERIFRKYANVHLCSDCSYLEFLKKLERFDLTTEPSKNFRYLEYLSELNEYLGRFIKVKYPLKMFRKVVA
SAPKIFSRAEARGFGKKNGMEGAEWFPKVYCVKCGREFSRSKVFEYHLEGKRHCKEGQGKEEFVYSEYVL
HRYLKYLGDPVSETRSLVLRSLAITAKERKAEISLLSRRKKQPATKSSEKEGAEQVDGEQRDEHVSGKSF
DMPLGPDGLPMPRWLCKLHGLDIEFECEICGNYVYYGRDRFDRHFEEDRHIYGLECLGIKPSRVFKGITR
IGEAMKLWNRMEESSSSLKVPTEYSEEFEDEEGNVMSKKVYEDLKRQGLI
>gnl|CDD|227516 COG5189, SFP1, Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning]
TPSILINNNSDSGKNTDFNGNNTNNVHLYSQGMGGVSWGSISVGSWLRDEIISRRNIVPARPSPQIAYTA
YLPNLEKQYCKDYSCCGLSLPGLHDLLRHYEEAHIVRMTNNTSSANYNLQINNMHQSQHPHHQQNIIQQQ
LQVHTSGAVPTPSVMGSATASSTTANPSITGAPGLLVDAVDVPHNKQINSNNNSTSHNSNMGSKNAKMND
SSKLKKLSLIEEKKFPERVRSRYIDIGHMMDTHQFYLEDVDLMDDDILGPSNEEMLYKYISPSQGSAELF
EESSLGFDYEFIHKSVGNKEIRGGISTGEMIDVRKLPCTNSSSNGKLAHGGERNIDTPSRMLKVKDGKPY
KCPVEGCNKKYKNQNGLKYHMLHGHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYHRKH
SHD
>gnl|CDD|444068 COG5190, FCP1, TFIIF-interacting CTD phosphatase, includes NLI-interacting factor [Transcription]
KLLILDLDETLIHASETPLARAPDFQVFGYHVYKRPHLDDFLSECAARFDVAVWSSSSDDYVAAVVAAIF
PDSIDLRFVWGRSRCTPRRDYATDEYYYIKRLKKVKRKGYRLERILIVDDTPEKVARNYGNAVYVAPFEG
DPTDDELLALAAYLDTLKDVENVRSIEKRGWRNLSI
>gnl|CDD|227518 COG5191, COG5191, Uncharacterized conserved protein, contains HAT (Half-A-TPR) repeat [General function prediction only]
MVEKIQYYMEQMIPELEDLKEKGIFSPDELRRIVKTRRKFELRLQRREKKLNDFMRYIKYECNLEKLRAK
RVKRKKVGKKASFSDMSIPQKKIFELYRSTNKFFNDPKIWSQYAAYVIKKKMYGEMKNIFAECLTKHPLN
VDLWIYCCAFELFEIANIESSRAMFLKGLRMNSRSPRIWIEYFRMELMYITKLINRREKTEILSNEIGLD
SDDKDEIERGQVPFAVFADCFNSSCFTAKKIDEVLEISKDIKELRKREEDYTRGKGPYLTIFDVCMKTLY
INKHKGYYAISDSKMNIELNKETLNYLFSESLRYIKLFDEFLDLERDYLINHVLQFWKNDMYDLSLRKDL
PELYLKTVMIDITLNIRYMPVEKLDIDQLQLSVKKYFAYISKLDSASVKSLKNEYRSYLQDNYLKKMNAE
DDPRYKILDLIISKL
>gnl|CDD|227519 COG5192, BMS1, GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis]
MDEKKAKHSKAEKKKLKKVMDGKVGNNAKAFAVAAIGQMARQAMRTADIEEKKLHVPMVDRTPKDLPPPF
IVAVVGPPGTGKSTLIRSLVRRFTKQTIDEIRGPITVVSGKTRRITFLECPSDLHQMIDVAKIADLVLLL
IDGNFGFEMETMEFLNILISHGMPRVLGVVTHLDLFKNPSTLRSIKKRLKHRFWTEIYQGAKLFYLSGVE
NGRYPDREILNLSRFISVMKFRPLEWRNMHPYVLADRVDDLTLPVDIEQNPKVGRKITVYGYLHGTGLPR
KDMEVHIPGVGDFRMADVEVLIDPCPPPDADHGRRRRLSLKSKLIYSPMSDIGGILKDKDRVYIEVPTSN
FSKDENSEAGEGEKMKMQLQEIEQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGKAIAE
ETSREDELSFDDSDVSTSDENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFDESEGNLRWKEGLASKLA
YSQSGKRGRNIQKIFYDESLSPEECIEEYKGESAKSSESDLVVQDEPEDFFDVSKVANESISSNHEKLME
SEFEELKKKWSSLAQLKSRFQKDATLDSIEGEEELIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAEN
EESADEVDYETEREENARKKEELRGNFELEERGDPEKKDVDWYTEEKRKIEEQLKINRSEFETMVPESRV
VIEGYRAGRYVRIVLSHVPLEFVDEFNSRYPIVLGGLLPAEKEMGIVQGRIKRHRWHKKILKTNDPLIFS
VGWRRFQSIPVYSMKDSRTRNRMLKYTPEHMHCNVSFYGPVVPPNTGFCAVQSEKGDFRVLALGTITDVN
GDAKLVKKLKLVGYPKQIVQNTVFVRDMFTSDLEVLKFEGASLKAVSGLRGQVKGPHGKNGEYRAVFEGK
MLMSDIITLRCFVPVEVHRIFIPVDNLLGKWRGLRRLHEIRESLGLTHSYAPQNDSSSEEMGYGAEEDYS
LPREIESKLPLDKRSIAVVSRRIELPVPPECREKHEIKDRIVKERIKDQEEKERMESLQRAKEEEIGKKE
KEREQRIRKTIHDNYKEMAKKRLKKKR
>gnl|CDD|227520 COG5193, LHP1, La protein, small RNA-binding pol III transcript stabilizing protein and related La-motif-containing proteins involved in translation [Posttranslational modification, protein turnover, chaperones / Translation, ribosomal structure and biogenesis]
SQNLNDNPSNTEHQAEDKKKQTSSLKLASEPTTSEEKSKSQDSNTVIPVEELTESSKSKKEDKNPSKLTS
NTKWTLKQVEFYFSGSKDTDSNFPKDKFLKTTAPKNKKRDKWVPIKTIATFNRMKNSGSPVSAVSGALRK
SLDARVLEVSSSGSNKNRTEKLISNNNKSTSQMQRDVYQNGFGKEDVNNASRPEQQEDLEIQFPPHYHAP
PSQIRNRRDWLNKNFRGSVFVEFKYFREAQRFNNGFYRNKKYPNDPETVYYYSVEPILLSIMAKKEQIEY
YFSEENLKSDEFLRKKFKKAGFIPLSFIGKFYRNLSFGGDKNLILAAMKEVVQNKATNHLEIALGSIEDA
QKNEAKDFSPGKKYFIRKKEWSEWLMESNFSEIADEKEKAKIEKLLGPNSLDPYSYMGYPNFFPSNENGK
KSQSYDQGEISREFEQNL
>gnl|CDD|227521 COG5194, APC11, Component of SCF ubiquitin ligase and anaphase-promoting complex [Posttranslational modification, protein turnover, chaperones / Cell division and chromosome partitioning]
MKVKIKKWHAVALWSWDIPIDVCAICRNHIMGTCPECQFGMTPGDECPVVWGVCNHAFHDHCIYRWLDTK
GVCPLDRQTWVLADGGAI
>gnl|CDD|227522 COG5195, COG5195, Uncharacterized conserved protein [Function unknown]
SNNNNNNDGGDMKLLKRPWFKKSTYKGKNRRFKTLRQLIPRLTIENESSKHRYLSIEAPPSVKPRMKYCD
VTGLPAPYTCPNTGLRYHNSEIYKLICELPSGRDQEYLKLREFGKVLK
>gnl|CDD|227523 COG5196, ERD2, ER lumen protein retaining receptor [Intracellular trafficking and secretion]
MDTFRFLGDFLHLASIAVLIHKIKRTRSCSGLSLKTQFLYSLVFITRYLDLFDFYARSLYNSLMKILFIG
SQVYILFLMRFKYRSTYDKKLDTFNILTLLVGSAVFSLFFTRGGTISNVLWTFSLWLESVAILPQLVMLQ
EAGETESLTSHYVFAMGLYRALYIPYWILRKVYDIKKTGNIAIAAGIVQTLLYLDFFAIYYRYVFRGKSF
SLPS
>gnl|CDD|227524 COG5197, COG5197, Predicted membrane protein [Function unknown]
HTPQQQRPMQIPRNTPVNGQGNANMNANVNGSGGGFPFQDPRGSMAFQLGQSAMSNFIGKDAFNQFQEYV
NKATGNAASSQQISTYFQVSNRYVINKLKLILFPFLNKNWQRIGDSEGFLPPRDDVNSPDMYMPIMGFVT
YILLWNTQQGLKGSFNPEDLGYKLSSTLAFVCVDLLITRLGLYLLIDSKIPSFLDLLAYSGYKFVPLILA
QLLKNVTMPFVLNILIFYLYIAFGVFLLRSLKFNVLSRSGAEIHASISKSTRKRRNYFLFVIFIWQNVLM
WLLS
>gnl|CDD|227525 COG5198, Ptpl, Protein tyrosine phosphatase-like protein (contains Pro instead of catalytic Arg) [General function prediction only]
MSKALPISYLRLYNTASCFIWCIVLLLASLVFYKTMDPAVFHETLRVAGLVQTFAIMEAANSSAGKVNSR
YLTTVMQVISRLFIVWGVFYPYCGIINSWTYPSITTAWSITEIVRYAFYTFRLNGIPNTLRVLRYNLFLI
LYPIGFVSEMYCLRALYNAAGKIFSLLKVVLPIVMLLYIPGFIFLFSHMLAQRKKSRKVKRYKSNRKDL
>gnl|CDD|227526 COG5199, SCP1, Calponin [Cytoskeleton]
MVNTKNRCPGMDKQQKEVTLWIETVLGEKFEPPGDLLSLLKDGVRLCRILNEASPLDIKYKESKMPFVQM
ENISSFINGLKKLRVPEYELFQTNDLFEAKDLRQVVICLYSLSRYAQKERMFSGPFLGPHLATKKPRVFS
SQEVLDRSKGAIHLQYGYSDLSEQSTEKGASNVRRDLR
>gnl|CDD|227527 COG5200, LUC7, U1 snRNP component, mediates U1 snRNP association with cap-binding complex [RNA processing and modification]
MAAEQRKVLEQLMGPERSTFDPCRPTHFTDKKVCISMLVGFCPFDLFRNTKRSLGKCPTSHEEKYKAEYE
RNGRERAEEYEWEYLRLLVRIVLSCNDGIRAAGLEDRTTPEEFGKIKEKEELFNRVDESIGELGMEGDAL
AKRKLVERACSAFNELERLREERKEIKEAVYSMVENNGQGTHQKLQVCGICGAYLSRLDTDRRLADHFNG
KLHLGYLLVRSDLADLLKKFGISRVAEIFKEGFSLKCLRVHPSRDFVL
>gnl|CDD|227528 COG5201, SKP1, SCF ubiquitin ligase, SKP1 component [Posttranslational modification, protein turnover, chaperones]
MSMIELESIDGEIFRVDENIAERSILIKNMLCDSTACNYPIPAPNVRSSVLMKVQEWMEHHTSSLSEDEN
DLEIRKSKPSDFWDRFFMEVDQEMLLEICLAANYLEIKPLLDLGCKIVAEMIRGKSPEEIRETFNIENDF
TPEEERRIRKENEWAEDR
>gnl|CDD|227529 COG5202, COG5202, Predicted membrane protein [Function unknown]
MYNPVDAVLTMIKKLSGVNYLELRFLACLLLTLPFVSILKRNPTRIRTHNLFSISLILFYLFGVRHLVSG
AYILASISLFTYLLRYFYRSAYMPTVLFIVILGHYKIFHAAQLFEERISTSFDITGSQMVLTMKLTSFAW
SYYDGKEYSSDLTEHQKSRARRGTPTVLDFLSYIFFIPGLLLGPAFDYADFDSWLTCEMFRSLMENPYER
PKRPPNGKLALATFLKGLGWLILFQVGRISIPRKHLLEEDFPVRLLPMRWAYLYLFTFGNRIKYYFAWHF
SHGSCILFGLGYNGPDSTQKIRWDRVRNIDFMKVELATNVKDLLEAWNMNTNKWLKNSVYLRVVKKGKKP
GFWSTLGTFAISALWHGINPGYYLTFLSLAASQTIVKENRRLLRPFFLREDGVTPLPSKSLYDVLGRIAM
LLLTTYFSASFFLLSLKDSMYVWRSVYFAVHIFLAFSLAVFIAPIRKKLLPQIGKKNTDLGLKAIEHEKG
KTAEEEEMNLGIPDWEDFCKDY
>gnl|CDD|227530 COG5204, SPT4, Transcription elongation factor SPT4 [Transcription]
EEKFKGTLSRACLGCGIVKTLNGFRKDGCPNCPMLNMKGGVTNVEECTSPKFEGVVAMLQPTNSWVAKWQ
RIDEFRKGLYAMVVEGALSEDVVEDLEQHGRIYYPRTGSFTL
>gnl|CDD|444069 COG5206, GPI8, Glycosylphosphatidylinositol transamidase (GPIT), subunit GPI8 [Posttranslational modification, protein turnover, chaperones]
MKDNGPSMHNKSVIISSFWDIQLFFLFILGSSLACLDTELAYMGVLLPLSGPEGSLLYDAKTLARDQINA
GLGIGGRPLELILRDTGLGDTMTYADYFVRSLRIRVVSGPYTMDEVFQVSEIRIKNHRVFISPTASGDEM
YRAAAGTAEVWRTGTTDGETTAVMMQHYKAHDTKYVSILTINDSYGETFYLWIPYWAIEQEIAVTGAETY
GTTEEIPDAVGRLLTDNPDELIGIYSGEYSEIREVISSLMFVPSPPVLYLVYPDIDSDSRIWDRADSELL
QALLPSGLWMIDTVSTVSTKVPDDTLFLMQKPWDAQFSEEYQAIAHRDTSNAVPTAYDAVLAGAQGMARS
MAFPDISPKELALAVLTKGTGASIPRTVGSIQFELDEILAGDIPILWGAHVRLTFGYERTDRLISWNELT
AIQEGMQNEDGIAYERTTKTSVGLNLPPNENYPPPTGFWAVLVQGSNGWENYRHQADVLNIYQMLRAGGY
DDDHIILVVADDIATAPENPDRGAVRTTPSGENVREGAVIDYRGADLTPGDILNILTGNKTDKTPVVLES
DEGQNVFVFWSGHGQPGGEMVWGDEGNGMTPDLLADVLTEMARSRRFRQMLVCLEPCFSGNIAKALEGIP
GVLAITAAAPDETSKADVYDSELKVWMSDRFTSNLIGHIRENPDGTYRDLYLYCYQNTLGSHVTIYNYGN
FGNLYTTGPKDFFVKR
>gnl|CDD|444070 COG5207, UBP14, Uncharacterized Zn-finger protein, UBP-type [General function prediction only]
TTCTHLDRLPDIVPPDTKGCEECLEEGDRWVHLRMCLTCGHVGCCDSSPGRHATKHFEQTGHPVMRSFEP
GEHWRWCYVDEELV
>gnl|CDD|227533 COG5208, HAP5, CCAAT-binding factor, subunit C [Transcription]
MNSIPDSYSLKQGFPEGLGEYVDPSGNPNSQVRIGYGQDSVSRFQQPVPDVDPTAVNHYNASAPIEVASP
FINVMQGLVGLLDERISRYWQQTIKAAEEERQILLKDHNLPLARIKKVMKTDEDVKMISAEAPVLFAKIT
EIFIEELTMRAWINAEENKRRTLQKSDIAAAVKKSEMFDFLIDIVPRNPFNHLVPSKMHHGGEDFAPRMG
DAYAKQHVLDERQMMEDMVEKMGGSHSQNFYSQEHRVVGGEAPEPLSNPHMSDYRRGFDISFNRDMSADM
TPGSFR
>gnl|CDD|227534 COG5209, RCD1, Uncharacterized protein involved in cell differentiation/sexual development [General function prediction only]
MAYHQVPRGKAEEEEMMEWKLEFLFYPHPGMANAVENDECDPNQRQALVYSWICQLVVGNPKEQALDELF
RKREQSPDLALELWRSDGVMTFLLQEIISVYPILSPSKLDERESNRVCNALNLLQCLASHPETKKVFLDA
HIPLFLYPFLNTSSSNSKFEYLRLTSLGVIGALVKNDSQYVIKFLLTTEIVPLCLRIMELGSELSKTVAI
FIFQKILGDDVGLQYICQTFERFYAVNLVLNSMVSQLVSLGSTRLLKHAIRCYLRLSDKPHARALLSSKL
PDGLRDDTFSLVLADDGGSKECLAQLLTFLNLICS
>gnl|CDD|227535 COG5210, COG5210, GTPase-activating protein [General function prediction only]
PLRSSSDSLISSYSDKAQSLRLSKKLMEFSSPTSSGSAADISISVNESSEEKSVSLLSSPNEEPGSFLNN
DLDKSSFNEELPTLLETADRSSSPGNESLSAVVSNFGLNNKSLKSQSTSPELPKRLKDSLPTHLPEASST
EKDFSSFKGSSSLNSNPELNKEINELSLKEEPQKLRYYELAADKLWISYLDPNPLSFLPVQLSKLRELIR
KGIPNELRGDVWEFLLGIGFDLDKNPGLYERLLNLHREAKIPTQEIISQIEKDLSRTFPDNSLFQTEISI
RAENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEQAFWCLVKLLKNYGLPGYFLKNLSGLHRDL
KVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILK
LLRDKLLKLDSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDILLFIEDLLKKDITPTRYRSELREIQ
RKRNER
>gnl|CDD|227536 COG5211, SSU72, RNA polymerase II-interacting protein involved in transcription start site selection [Transcription]
MAPMPNLKLAVTCASNQNRSMETHDVLAKAGYPVKSFGTGSAVRLPGESIDKPNVYNFGVPYQQIYDDLC
MQNEDHYRENGLLYMLDRNRRVKEAPENWQQRSEDFDLVITCEERCFDAICEDLYARGPSLNQCVFMINV
DIKDTPEDAIAGAKAILELVDVLAKEEERLEYAVDSILRRYQSNHKGLPLLYTVVNL
>gnl|CDD|444071 COG5212, PDE1, cAMP phosphodiesterase [Signal transduction mechanisms]
LLFTAAAAAPSMEVRVLGCSGGISDGNLTTYLLRPLGSDDYVLLDAGTVVSGLELAEQKGAFKGRQGYVL
EHIKGYLISHAHLDHIAGLPILSPDDSPKTIYALPETIDALRNHYFNWVIWPDFTDIGSAPHLPKYRYVP
LKPGQTFPLGGTGLRVTAFPLSHSVPSSAFLIESGGGAFLYSGDTGPDEVEKSTNLDALWEALAPLVRSK
KLKAIIIEVSFPNEQPDALLFGHLTPALLLEELAKLAKYAGGALKGLPVVITHIKPSLKAEEEILKELRA
LNDALGVNFIILEQGDRLEF
>gnl|CDD|227538 COG5213, FIP1, Polyadenylation factor I complex, subunit FIP1 [RNA processing and modification]
MSSDDKFLYGSDSELALPSSKRSRDDEADAGASSNPDIVSDDDSDSDLEVIISLGPSSSKDVISVAMDVF
GAITKQNDEEFFTEAQDVKATESDGELIKEKTPEIDEDKEETEDGQNILDIDIESFKDKPWRKPGADISD
YFNYGFNEFTWKEYCHMQEKLQQDYNPREFAMGLLQQQGELNSGNDRDFNEGKIDDDGDGPNGANGSNDN
GNMGNGMGGRPNGPAGPKEPSFGGLGMFGDFEPFPYEEMGPGMNQGPNDGGKQNSK
>gnl|CDD|227539 COG5214, POL12, DNA polymerase alpha-primase complex, polymerase-associated subunit B [DNA replication, recombination, and repair]
MEFPIDDEELLDERNKLLQICNMDEQTMFYKWESWCLQRGNTKLDLDTFKAFAKDMKFQMERQVKATLKQ
NPERKSIKQIPGMNIDSILGLPVKTTASGDSLMQESKPSTETFELNSSDAGRVLMDLNREVFKILSRRPY
VPSSDVRVAPFDLKPRVSRFMYQKLRKKSKVLDDRIELFSMKPYFLYLLSIEDFAPPNNVSQSSFYTVGR
IVNPSTNFGHKLNSESVFLESSRDGGNGVRVRLNLAHLQRYSVFPGQIVAVKGKNTDGGKFTVEAILPIP
VVPINPASDGQEKKYFQANTNNQPTSIVAFSGPYGPRDDLSGSPLFDAIDRVNANDVDVLILIGPFIDIN
HILIQYGATQSTPDSMLKELFIPRITPILDRNAGPKAVLIPSTNDATSCHNAFPQGPIGRNALRLPSNFK
CTGNPCEFFINEILFGISSLDTPLEISSEECFHDSLLSGGDRLGRISYHLLFQRTFYPVFPGGSLEKCNP
SSLDVVSLSLPEFMSMTAPDIYIVPSKLKHFCRDVGNVVVVNPGLQAKETNEGIAAHITLPPLEAGEKKK
GTVEFYGHPVWARNRKEILKL
>gnl|CDD|227540 COG5215, KAP95, Karyopherin (importin) beta [Intracellular trafficking and secretion]
MKKSEFRCLGKNHVLSPDPNARLRAEAQLLELQSGDFEQFISLLVQVLCDLNSNDQLRMVAGLILKNSLH
ANDPELQKGCSQRWLGMRHESKEQVKGMALRALKSPEPRFCTMAAQLLAAIARMELPNSLWPGLMEEMVR
NVGDEQPVSGKCESLGICGYHCESEAPEDLIQMSNVILFAIVMGALKNETTSAVRLAALKALMDSLMFVQ
GNFCYEEERNYFMQVVCEATQGNDEELQHAAFGCLNKIMMLYYKFMQSYMENALAALTGRFMKSQNDEVA
IQAVEFWSTICEEEIDGEMEDKYLPEVPAQNHGFARAAVADVLPELLSLLEKQGEDYYGDDWNPSMAASS
CLQLFAQLKGDKIMRPVLGFVEQNIRSESWANREAAVMAFGSVMHGPCEDCLTKIVPQALPGIENEMSDS
CLWVKSTTAWCFGAIADHVAMIISPCGHLVLEVSASLIGLMDCPFRSINCSWRKENLVDHIAKAVREVES
FLAKFYLAILNALVKGTELALNESNLRVSLFSALGTLILICPDAVSDILAGFYDYTSKKLDECISVLGQI
LATEDQLLVEELQSNYIGVLEAIIRTRRRDIEDVEDQLMELFIRILESTKPTTAFGDVYTAISALSTSLE
ERFEQYASKFIPYLTRALNCTDRFVLNSAVGLVGDLANTLGTDFNIYADVLMSSLVQCLSSEATHRDLKP
AILSVFGDIALAIGANFESYLDMIMMLFQQASELDPHSDEVYVDDYRKNAVQLVNCAYVGIGDSSKNRVR
SVLPYVISIFHKIGMIAEDPNGSEAHTRAALGLIGDLAGMFPKGELKFGLDEDWVKDFLYGMMKKISSQQ
TKDSARWAAEQVKRQLRA
>gnl|CDD|227541 COG5216, COG5216, Uncharacterized conserved protein [Function unknown]
MSFYDEIEIEDFTFSREEKTFTYPCPCGDRFEISLEDLRNGEVVARCPSCSLIVCVVYDAEDLEEYL
>gnl|CDD|227542 COG5217, BIM1, Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton]
CDKALVESREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIYVDLPDSLVRFPWIAEYKHPGNGKILQ
LLFSDYGIDKAVLVLVLVRCKLQDNLEFLQWLKDHWVRNLGHISYDRNARRLGRTPKSTRELIEWIRSLG
IPISAIRELSKGVASCKSLSTIHSSFPQNFVKNTAGTHDYLRAMQACQEFIGSLNIKLYFPVDTLVKLEM
ERAFYFNKLRSIEILVETLKREGPRASILPGTSLQCPHCKNTREIMDAKDNRIKEILYMTASGFERIMDM
EADLSRAVLKVHATKSNAGGFADDEVKSLLMAFEKRDVYFRKDFIEKYFLEREGLDEELDTF
>gnl|CDD|227543 COG5218, YCG1, Chromosome condensation complex Condensin, subunit G [Chromatin structure and dynamics / Cell division and chromosome partitioning]
MTVSETVSSLESMQLIFNKIQQSSAGHRKSLAELMEMLTAHEFSEEFLRVVNTILACKKNPSIPDRILSF
LKRFFEYDMPDDPEGEELVAGTFYHLLRGTESKDKKVRKRSLQILALLSDVVREIDEVLANGLLEKLSER
LFDREKAVRREAVKVLCYYQEMELNEENRIVNLLKDIVQNDPSDEVRRLALLNISVDNSTYPCILERARD
VSGANRRMVYERCLPRIGDLKSLSIDKRILLMEWGLLDREFSVKGALVDAIASAWRIPEDLRLVELLEFL
DVSRRSVLVAAIKGVFEKRPDVLSEKEFPEYLWSDPTEENTFLSRTELLYCLDNNITELLGRFPESLALP
DLESHYVSLRYRSSYNTLCFIIEQLSIAAERYDYSDESGRRAQLEAMKNLLRIARLYDFLIKIGIEASRK
LILSETDFKLLAKEIIEEVVEEAIEKMEQEEQIASLVCEDDLNNFIGSEIKKNAKSAVENLVQGNGNVSE
SDIINNLPSSASPRMCLMVCKHVMEHIRTPLSENILHEAIVETLILPAVRNSAPNIRETGVEILELGCLL
DVALARPNHAIIQSCVHKGNMELKSMAFQMCVDLVLSHGDEGEGKLDSLLGDILRHILQGLETKERQDII
AEGLSKLALSHRMPDDLRSRFLAFAYFRPYCTQNDALKQYCSILFPVYLFSEDSHQQRMSRTATDLLLIL
CSVLEDLPEVDAMLSHKVIIQQSLYWTDNSKLANQTGSTGSDLLFLNQIMICVRLNSIFESLDNVSQDKT
RKTLVSLLERIEVRSELRCWDPRMTKKILFCCSSVAFKHDTSRLSIGEVIRRLMEQDDGDPRSQEELCDV
KKDLENMSIQDTSTVAKNVSFVLPDEKSDAMSIDEEDKDSESFSE
>gnl|CDD|227544 COG5219, COG5219, Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]
MKKKSTDLYGRKNQSMSGSFSSLQIALDNFSTIYEPPDLSGLDAEMIVIVKNLQKRDIVTKCRALQDLIQ
WNDPSQFDNEQFLNALAVLFPRLSIEVEMNPRLEGLQFDSRLYEILSKKIGKRLKKTILRGLLGLKDVDD
TVSVEANIDTLLEIVEDKWPTIWKSFNLQIKNLVIDVLYHELLSSVEDRRKFSKEESEWLYGRVENSEYL
VLRKLFAEFVDIGLETDKKIEKQTLEDSFVRMLDFKEDPVLGLVCSPQDGVTVSLSDLLLIILKYDLQLL
VKKGRKDYSRMASESIEYLCPMLRLLSNMLSNSPRELREVYKLCKRPLSKLFSNLALGRISPNSGFYEKV
IALKKSIGPKLANPSILKWRLLLDAFLETANQEQRFISDEVPECIRNFLSFVYDSSKYLDKDIVSRTIFE
RLNVGDDIPSTVRSPDSLRVVFSKVKWNEVLFGFFNDEEYLKEYLKFGSLEGLLILTFLGVLYLKNRDFQ
FLNENVDFDPCLSFLMKLSTHEVVNRLVKSQLIINIHFQGDTLIEDISKLVQKMDVKDSSRILKLGPQSP
AFTLLRDILLLLKDYADLSEPWENVANQFTNSMGELDNGQEDNHFHSCSSIGPLGIEDILKALLSSDDGV
FVQGKNKIIRGDIINVELNSQEFTRPEEEVEEVLQHSVEVFPKEYMLNTSFTLCALLPLVLKYPEDVFEE
KIRLYKTLPVILFEDDGHVAAHFESIFSLLKEKALEDSGFSLKLCKDSQELKLNKVLNGFMDACKALDLL
RSLVFSYDSLMEIYLTSDTPIALDLSNKLFIDQDFYYRLLDRVDEPINRPRVDVGTQFVHIIDYYSRILE
EYLDGDSGFIRTFVEKNVINRDMLYIAVVLQLPSDAGIFVESFEVPISTSVTNFFYDLVLNECLYKNIDG
KMPVLFKKNLSSAENTTSFSIREQSQTDLDLRHVDLYLKIYKLSSSKGEIFLLLLLDDSMCIDIREDESL
DRELKSLGILNDGRNQQMLGKNVLPIKRCSTIDRNITNWRGSGIKSLELLPVCIYLGENHHFVEKVFSLS
GDLGLPSFRCSDRKLEQSVLLERIGPRAILYVLRKHNVPPQFVASVSDIKDCIVESNDSMNYLLLKFLFT
HFSYLRNEALSRAVSQLLLKCRKGFPIKFVESQYFEGFPEFPNADDEQMESVCMKFLREKLSADDNELLL
MLLAKSNYRNDRSLDMKGVVRMIERPGDHLLSVKKEEYRERHTIVYLPLWRLIYGHFADTVYNMYSSIIS
QLDMNSLDSEVYVLLRGCFLLSTVLFWDLVDNSLLIVYNISINYSSATDRIRCLAIHIYYQFFEKMVGEK
EEWWVFLKDRGLQRSLEAFVFPNISPSLIKMEVDDLDSFILKEASRTIADVTVKANKLTNEIGITYTADG
TKLEALIKIPSGYPLKNVQVEGIKRVGTSEIGWKSWINLRQNEMIKKNGSFMDLLGLWKKNIDEKFSGHE
ECAICYSVLDMVDRSLPSKRCATCKNKFHTRCLYKWFASSARSNCPLCRSEITFV
>gnl|CDD|227545 COG5220, TFB3, Cdk activating kinase (CAK)/RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit TFB3 [Cell division and chromosome partitioning / Transcription / DNA replication, recombination, and repair]
LMDEYEEMEDRRCPVCKSDRYLNPDIKILINPECYHRMCESCVDRIFSRGPAQCPYKGCGKILRKIKFIK
QTFEDITVEKEVDVRKRLLRAFNKEEEEFGGDLAKYNDYLEEVEELVFELLELIDVSLTEEKVKKYEEMN
QDSILNNLERPTPEVMPGKQKNVLQKRMKLKKRQLERQIEEEERMNKEWTKKEIGNRLGTASEDGNKTIK
IGIISDKFDPEELPRIVVEPTRNNKIYLSNVQGFLKDLQPFAPGGGSYNAHTIFSLAISSYGDPNIKDLE
HKEFIASGFNTNYAYERVLTEAFMGLGCVISEEL
>gnl|CDD|227546 COG5221, DOP1, Dopey and related predicted leucine zipper transcription factors [Transcription]
KPLTIDSNNMDEKREKYEAEMTKKLDAFKTVKEWSDYISLLSSLDKTLQKFSKFPNIPKKKLVSRRLNQC
LSPVLPAGVHNKTLEVYSYIFERIGRETLLKEFNFWTLGLFPFSAHCSILVVSSFIDLIERYIVPLGKDV
RSYCTSILISLLPGMEFESGEYYSLRAHLIITLFKSLIDPDVFWSSMWGILLNDERLRTGVLNSLMREEN
NDSHMDWSERLILPHAGLMVRALCAGLGDNDILVVRNCLDLLLFVFPDKSHVDVSADMLDDKLLIMSVIK
LFLKRDLSLNRRIYGWLCGAMDSFDEVNVSLLSRALKRNLDRGSAEIQLFFEGMMDLLSKGKLCESIMEA
FRIDIAECDRRHERDYIEEYAPPDAFESERSSENIDVEKIARAFLTTDLDSVWKILYLQLKDVLLHSKEF
MLLNMDLTNDEEFNDSMVREEMYSLHSMSLIFNEITSSECFALGASLLEVYKGAYPMSESSLLEEMELKC
KGLLGRVVENRENVSNWIKDANNPNQVLGFIRFAVDNLTFVIDSEVYKYHLPSLVHLVLSDFLLFEPQVL
FSFLDFSEKLMRFRERQLEDGKNLQFLIGKFYLEEDTSVLDEISSTILISISDKIGKVIESNVALSLPMM
STFIKIGVDVFPSGFIQSYKCLVRKISSKFMKEHLEVYKIIDCTQLDPLGMFELLWGRFQHTERSLYLER
PLELDLGGLHDDRSPRAGTREMIWISSLNKLSGIGRVPNRKVLTENLWRVNMLERGSFEKLLLKDMGEVE
EISYFYLLKLENFRGNFDFLELYYVLKSKLDWPDDPVLDIKSLSLGYFDDFLKNIKKKTEDSNIQANDSL
LAESIDGTEQNLNDIVIFLIAGVFKCIKELLKYPRGFRSMLLDSVEKLHSLALPLDEAVDPREMLHRMLV
HFLVNRKENDGRSPDMEIIKILELLVRGGILSGSSIFRVMNSVDLSRIVDVAKENLDDPAIVLGYAPVIK
HSGNLAALQELCSILLSQCFYYHSFLESNLSLTRLIRKVMSNVFSSLSSNEESKIQNRDFGLMIVSEAIT
SMLLKRGWHGILPAFIDKSSKFIFNNSYFFKNQSVDLLEEERGREPLEIAEMLQGIEHHNALTLSSSTCL
QEEAPRTSVRILALKLSTRKELSASLFRKVPIKFVETILEGSPCIPFLMSRDFGEQIYISIMNLVSNNGT
SVFKFLSTLLQVMREVAENMNVYNDSKGLLLKIVSYRAGKDSAPLFTLNFLLGLDLGESDFALVQSVILN
SVYLLQKKLDLKTRNGFKDYEVEVIVLERLTEDKFQRTVLSIVNSLITPIIKLVNSSLGLKNYGLNLLAV
LSERGLEVKSWRKEFVEIFNDLDLFIYGSDQLHKKSSLMRKVVVEDPSILNDLIVRLDSGLITFFVSQDS
DANNKTLNLKRISYLIFSSPYDYFLGFSLKLIEKIATLMNSPSSKLKKEVFLLSRMLILRISHDHLGNLW
PILLYDLGIVVESYESPDFDVDMMTLLEVCKLLDILFLLNTEQFSTEEWTVFLGPRYRVYGEKASGGELV
KSVLESLGGLLRAKDDKEIPSKVRRPIKKIPFLMPGKVDVQLRLFFTSNSLLYYEWLYECLEIDYEYLFN
LILEELLE
>gnl|CDD|227547 COG5222, COG5222, Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]
MSSVINYRFKSQKNFSRISFDGTGLPVFDLKREIINQRKLGSGKDFDLLFYNGETNEEYDDDYFVIPRST
SVIVSRIPAWKSKGTAARYKGGAPKTTGARGYNVKRPRMLQKKAPITSGELNSQSSSEDAAIQQMFQVSS
DQWRETQDKMSSATPIYKPNQHRIGAQKHNKPPPPGYVCYRCGQKGHWIQNCPTNQDPNFDGKRIRRTTG
IPKDFLKPVEGPNEPSNAAIMITPEGGYVVAQPDVQSWEKYQQRTKAVAEIPDQVYKMQPPNISLKCPLC
HCLLRNPMKTPCCGHTFCDECIGTALLDSDFKCPNCSRKDVLLDGLTPDIDKKLEVEKALKKQRKKVGTS
DDNNTPMSEKRKREDPNSSAVFSKATAEPAFKSAMAIPMPSMPHVQGFPPFPMMPLPQMPPMMMIANPPR
TNSRPSN
>gnl|CDD|227548 COG5223, COG5223, Uncharacterized conserved protein [Function unknown]
MSLGFTKVPQRKVHRERTQPKDRRKYGKLEKKKDYVKRAQDINKKQDELKKLREKARERNPDEYYHGMHS
VKTDGGVSSIYREDEPTIMDLAKMLKTQDNEIQRCRRKLERYKPMPCGTQIKFEESSLHTIFVDMRFGQK
EFIPEEFFRTTEELVVRRENRLEKDQIENNELEDSVFSGKLHSKLKEKAATELLLRQKRDKKLAAAEERV
ELDRLLQGKGGKKKVVNGKPVYKWRNERKR
>gnl|CDD|227549 COG5224, HAP2, CCAAT-binding factor, subunit B [Transcription]
AQEAAEAAANGGSTGDDVNATNANDATVPATVSSEVTHTSEGYADSNDSRPSSISNSSESPAPINSATAS
MSPANNTSGNNITSPNVRGELDMSSGPTNTASTSGPVPHDMTVLPQTDSNTSNLMSSGSQLGSFATQSTN
GNNSTTTTTSSAAHPGSFQPDYVNAKQGNEISKRPGLRVYLDDSVSAGRAFYLHESRHKHAMLRVRDPTG
RFLTASEIDPLNLTGNTQDSMIIGQQTYPSHGSSGTMK
>gnl|CDD|227550 COG5225, RRS1, Uncharacterized protein involved in ribosome biogenesis [Translation, ribosomal structure and biogenesis]
LPVMNELKIPTVVDLGNVAAFDLNVLDKNDLDSSQEESNIKSLKRDNVQELKNQLCSLPARRTSDLVLLQ
LPESTTALPREKPLPKEKIETKWERFARTKGIEPKKRSGPLVYDEASGEWVPKWGYKGKNKRLLKQWLVE
GEVKLKTLLRRQRKNNIKKNEANRRGNISRRR
>gnl|CDD|227551 COG5226, CEG1, mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification]
MVLAMESRMELFRPGNKVPPDIAEALKTKIYKLLCITEPRETFPGSQPVSFTLDNIGLLLNNDYLVCEKS
DGVRALLLVTEEPVTGAFRGYFYDRRNNFYEVHTSFPPCSTVLKDGEVLLEDTLLDGELVFDCLPYEKVP
QLRYLLFDCLAYAGMFVERMEKSERLKTLQKEDEKPRERKRVSIEIDSGSFPFHFSVKQMLKSYGFWKIY
KKIPELKHGNDGLIFTPADEPYSVGKDGALLKWKPASLNTIDFRLVLHKKWSEVDDYNYVCSPKFGLDVW
FGRKTYRFFASGEVIDGEWCELKYDCDPLYWRIVECVLKKEGAWKLLRFRDDKDTPNHISVVCNVLESIR
DNVSIEDLSTFYSVIRENSKRREKAMRRGRPLPSQSNATLSTSKPVHSQNDKEP
>gnl|CDD|227552 COG5227, SMT3, Ubiquitin-like protein (sentrin) [Posttranslational modification, protein turnover, chaperones]
MSSSDSGSEFKTNENPLVKPITKHINLKVVDQDGTELFFKIKKTTTFKKLMDAFSRRQGKNMSSLRFLFD
GKRIDLDQTPGDLDMEDNDEIEAVTEQVGGATY
>gnl|CDD|227553 COG5228, POP2, mRNA deadenylase subunit [RNA processing and modification]
HLTNQSMPPIFLDGPNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHY
QTLRANVDFLKIIQLGLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGID
VFEFSELLMDSGLVMDESVTWITFHSAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSV
LNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADEFFLPRFSIFTTSIGQSLLMLLSGCQLSKLSLHKFP
NGTDFAKYQGVIYGIDGDQ
>gnl|CDD|227554 COG5229, LOC7, Chromosome condensation complex Condensin, subunit H [Chromatin structure and dynamics / Cell division and chromosome partitioning]
MSNDNFEEWIKAATDNKINSKNTWNFALIDYFTDIDELRDGEGINFQKASCTLDGCAKIYSSRVDSVSTE
TGKLLSGLANDSNGGNGEGLGGDIEIDDPDRNNTEERRKKQRVGKTTLVKFEKITIKKNICELNIDPLFK
KRCVDFDEGGAKSLLLNTLNIDNTKRLYFDSSPIKDTENVGQGKLQRKEEELIERDSLVDDLMIDSQSLG
ISSNDSTVNDSVISAPSMEDEILGLGMDFIKVLRMSVCRIEGTVIVDDFKMSMDFPAGLLISPSISEDKE
IRDIVEEPAVDNDNEVSDSDGFDMGEHAGLFSGDNFELNEILPPSSNQNPSTTGSIFEKDVYKYFDFSYF
KNWAGPEHWKVQAKKKRVNKESDLLEETRTTITTDKTDDKSMDTSGKQKQKEASFIDFTETVDYEGMLEP
GNTLFDPPFIVEKRESRHLLPDDFRLEVERLYRLFVKPKMSLFSHSSGLFYKKDQAAAEEENDIDHIPAS
CFIEDPEDEFVEDIPSQGVGALDNPFEDDMDGVDFSQKFPDNEEASVKLDLQDKIPYRKTPKKVDVRKLK
DSVWDSVKGGSTSHDSRKNREQSSSETHTELSSTKELKFSDIFEGIPKVYNGEELKDISTSFCFICLLHL
ANEHNLQLTAVENDIDVQMLQYEDLATTQAAS
>gnl|CDD|227555 COG5230, COG5230, Uncharacterized conserved protein [Function unknown]
MFGELGNKLLLEDKRTDVLDPLPPYRRDEIKAIEGENEHLDRRMEEILQEASQAGSGIDEELSVNYVMMK
YFKERNKRCLRAYKFLRSAALFDSFWSKGKRMKSVGDTMLSHEEEEYLEKYSNLLREYKGPFKHIDLTGS
LVPPVQFFIDVRVLKDCGVIMTEYGLINLKKDSQYFVRKNDVERLIDQGFLRKI
>gnl|CDD|227556 COG5231, VMA13, Vacuolar H+-ATPase V1 sector, subunit H [Energy production and conversion]
ASPPPVELDNSQVDEIINNVRMFLKMWEAKARSNELQEIPLETGKELVERFVKMKYRDGRRESNLFLKFL
RKENVPTTILLDSPELLDEEDLIDKFLSLLFGPDIYSFYRSDEMLTKMYEDKKHKKEFLSVFKQMLKDNT
SYVESNYLLFLEYLGKLSQLIDFLTRLFAVSCLSNLEFDVEKRKIEWAENTCSRRFMEILQNYVGVKQLQ
YNSLIIIWILTFSKECAQDIDKMDDLINDLIAIVKERAKEKVLRLCCGIVANVLDKSPKGYIFSPLLLND
ISKCVQVLLERKYSDEELVIDIERIRSRLVQNTKKLCIFDNYLNELDSGRLEWSPYHHKKDFWSTNLDML
IKDNYEIVKVLKKYLQSNNPNTWICVACSDIFQLVRASPEINAVLSKYGVKEIIMNLINHDDDDVKFEAL
QALQTCISSEWS
>gnl|CDD|227557 COG5232, SEC62, Preprotein translocase subunit Sec62 [Intracellular trafficking and secretion]
RFVKQHCKPESALLPITQDQPKNVWAVYLRPKSSLRSRPELKQMHGARQKKTVELFRCKRILRWLNSEEY
TLRHRRRPKVYRGVPAVAILTKEGLDELQARLIMQEMLNEVIKLKVHINKRNTKELDVVLDQKFQEDQHY
VWAYEPTSNISLVLCGVFVLVTLALVLFPLWPRNMRQGLFYMSYGLGGFITFFFVLAILRLILFSITYLL
YPSGIWLFPNLFEDVGFFESFKPLWEYHEKDTYSYKKKLKGTKKEKAAK
>gnl|CDD|227558 COG5233, GRH1, Peripheral Golgi membrane protein [Intracellular trafficking and secretion]
MFIVSKNGKAIESKDDALTMNKSWESKALQLELIDMRTMETSALEESRKDKTRLGIFHTSVNCLLEVLRV
NPESPAEKAGMVVGDYILGINEDPLRFLEMNRRRSVPLLVYNSDLEYVRAVSLQVGVDSLKGCQIGMGEL
YKIPFSQRRCKVEFNSDEIRNDVRRLRRKLRGKDIQWSRLKDVVCSDSHILNVSIQDKPPAYALLSPDED
YIDGSSDGQPLEIGELDLEDVNESPVNLPLSLYYYNPIDDQERAKTERDGVHKGIVGILGCQVGHGFLHR
LPLAGVGQKPQLQKLGTTKRTEDPESHQVEQRGVEENFLPIPKPDTHRSEFAAKNFLSSLPLSFYGKKSE
HKSGTQRAVTTSYHEENGECPLCFKHEEKDRSSESSGEYTPLAPPPSLSSISSSDAGISDEEEAGEI
>gnl|CDD|227559 COG5234, CIN1, Beta-tubulin folding cofactor D [Posttranslational modification, protein turnover, chaperones / Cytoskeleton]
IDESLITSRSSQILDDTLDPRSHSVEAVKYLQFCQFQPTLLDKLLPKYVPNLASYLFKVKGKCNSITAIL
YQFCKIRGHKAVRVLLPVGIQYIKELYTLLNDRSNSPWSFHYIVLLYLSQALNTPFPLNSLADKLDVKKT
IYAIKYLENSPIDIEASNLVLSRLFFRDDALDLLLKRSIFYCLFSLSQFLKICLQSVEVAQFYLVGQENS
ALRKLLCKCLSRLGIVLLPVNLPIDSNEESHIYLEVIVDFLLSSVSSIDSFVRFSAAKGLAKIISRLPWN
LAESFIDIIELMTENMFLSPLENTCDIIITNELVWHGAILFFALAGAGLIDYSDCLILPIIEKGLSYEVR
YGTRVTGQSIRDSSCFFVWSFYRCYSKSAIEGLQTNLIHLLLQTALFDPELNVRRAATAALFEVIGRHAS
IADGLSLISLINYVSVTRISNCSGDLCRKVAHFPKFRSCEDVFQDILLTNLQHWDVKVKQLSAYSLRQLI
KYPKELPIYLPPILDKLSSDFIFGYTILASIIKGFLFPFDINRIHEILSHIQQTKIKLGILKGIQRIFAD
DIRVFRAFFSEAFSVIIGAIDLQEETIIDIVSDAYSVLLKFDDMPETLEVLLDYIVKCSTSKEARIVYSI
LQNTPSLIISFRYQEKICKLLLDIYPQLHSIDYSAPIANALHNIVPFTYEKSESIEEFRKEILNVLSNYL
TDTRGDVGSWIRKPAMKLMSSFLVKDSSGKKLYIIRQTFDKIDSLRGLAYQALEQIRVHYLSRRCEALTN
IGNRISFRNGPNVDGGVLNELNISLLEIPNSFLQAFYGLTVFTADGLGSDLAVKCFSFYIAYSYQLEDSF
KKSNSRGMRYITILSSEDECARFYFPIMESFAYGCFPDFQVKGMSKAIYIVQALTCKSPGGLILELYRTL
FLSRHHALKYNANLLLNPIIKVRYLALDTLEYAKSIGLLTFLPNVLLQKLLQLDWFVPVSQATFVKQLRN
IIQKQIDKLIADR
>gnl|CDD|227560 COG5235, RFA2, Single-stranded DNA-binding replication protein A (RPA), medium (30 kD) subunit [DNA replication, recombination, and repair]
LATLYLLKSLFFITRGQIFGTGSPPPMDRSEGGYIVNTLRPVTIKQILSCDQDETDSTFLVDSAEVTNVQ
FVGVVRNIKTSTTNSMFVIEDGTGSIEVRFWPGNSYEEEQCKDLEEQNYVKVNGSLKTFNGKRSISASHI
SAIEDSNEVTYHFLECIYQHLFYTRQLQRPLEEEVKNDGQSLFAKLDNDTSSGSSRLQEDILECYRRNQD
ENGLHINVVIKMLSQSYSEDETRVNIDVLLRDGHIYPTVDGNEFKTTI
>gnl|CDD|227561 COG5236, COG5236, Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]
MSESVKENVTPTRNFRRTQGPQNNTKPHNDRKNFRRKQKKNNLSAEPNLTTSSADDTDEENMNCQICAGS
TTYSARYPCGHQICHACAVRLRALYMQKGCPLCRTETEAVVFTASSPADITDRRQWKGREEKVGIFYEGE
DVRDEMEDLLSFKCPKSKCHRRCGSLKELKKHYKAQHGFVLCSECIGNKKDFWNEIRLFRSSTLRDHKNG
GLEEEGFKGHPLCIFCKIYFYDDDELRRHCRLRHEACHICDMVGPIRYQYFKSYEDLEAHFRNAHYCCTF
QTCRVGKCYVFPYHTELLEHLTRFHKVNARLSEIPRPGRCSIPVMDPFKRKKAPARVSVIDPSGGNARAP
MAHRGGSRQDTASPSTEAELPKYLNRNILEEERRKLQKRRLVIDRICKAEGNEIEEIINEFLGDSIDVTE
AFNRISKVTGDAAALKLFESAPFGPKQSVVEGSIKALRKRVMFPKFVPSEPVRYREPERKGPGFTVIDLH
KRK
>gnl|CDD|227562 COG5237, PER1, Predicted membrane protein [Function unknown]
MRLAVVVTLLVHCFLVTCSPGDNLDEMKYCFGKCFENSRCNLNKTDTNMFPLVDKLFGWDCDSKCGYMCH
LLCLKFTNSGNIKIYQRHGKWGFQRVLGMQEFFSALFSFMNFITHYIGFHRMLRKILRETRLGRLYYLQW
VYIGMLAWISSSVFHIRDNTITEKLDYFLAGLTVLFGFYMALVRMILIVSPPIEKATRGPLQAIFIAFFA
YHIHRLSNIEFDYVYNMISNCAIGVTQTILSHLVSFLNYRKLGHTFKRIPLFFVFFFFLAGSLELFDFPP
YAYLIDAHALWHLITCISTPFLYLFWSGDVYYHGNRQLY
>gnl|CDD|444072 COG5238, RNA1, Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis]
EAIGTFDRHRNIEELLSANPATTEQSELTKRATIVNLRSYHLHGGAILLARYLQSRSSITQYLRFEGQGD
PGLNPVALEKAAEAFPTQLLVVDWEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRR
INLIQVLKDPLGGNAVHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTV
TTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEG
AIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTL
HSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNRLHTLILDGNLIGAEAQ
QRLEQLLERIKSVY
>gnl|CDD|227564 COG5239, CCR4, mRNA deadenylase, exonuclease subunit and related nucleases [RNA processing and modification]
GPDPDFPRRELDFIQRPFLSIGHYAEKDTDFTIMTYNVLAQTYATRKMYPYSGWALKWSYRSRLLLQELL
YYNADILCLQEVDAEDFEDFWKDQLGKLGYDGIFIPKERKVKWMIDYDTTKVDGCAIFLKRFIDSSKLGL
ILAVTHLFWHPYGYYERFRQTYILLNRIGEKDNIAWVCLFVGLFNKEPGDTPYVANTHLPWDPKYRDVKL
IQCSLLYRELKKVLKEELNDDKEEGDIKSYPEVDILITGDFNSLRASLVYKFLVTSQIQLHESLNGRDFS
LYSVGYKFVHPENLKSDNSKGELGFTNWTPGFKGVIDYIFYHGGLLTRQTGLLGVVEGEYASKVIGLPNM
PFPSDHIPLLAEFASDHKNLMCNAFLFN
>gnl|CDD|227565 COG5240, SEC21, Vesicle coat complex COPI, gamma subunit [Intracellular trafficking and secretion]
MSAHTYKKFMKTKVFTTLTERTLLQDMNESFNKSPVSTRSARKLLSNLFYLLSTGELFPEATATNLFFAI
LKLFQHKDLYLRQCVYSAIKELSKLTEDVLMGTSSIMKDLNGGVPDDVKPMAIRSLFSVIDGETVYDFER
YLNQAFVSTSMARRSAALVVAYHLLPNNFNQTKRWLNETQEAVLDLKQFPNQHGNEGYEPNGNPISQYHA
LGLLYQSKRTDKMAQLKLVEHFRGNASMKNQLAGVLLVRATVELLKENSQALLQLRPFLNSWLSDKFEMV
FLEAARAVCALSEENVGSQFVDQTVSSLRTFLKSTRVVLRFSAMRILNQLAMKYPQKVSVCNKEVESLIS
DENRTISTYAITTLLKTGTEETIDRLVNLIPSFVHDMSDGFKIIAIDALRSLSLLFPSKKLSYLDFLGSS
LLQEGGLEFKKYMVDAISDAMENDPDSKERALEVLCTFIEDCEYHQITVRILGILGREGPRAKTPGKYVR
HIYNRLILENNIVRSAAVQALSKFALNISDVVSPQSVENALKRCLNDQDDEVRDRASFLLRNMRLSDACE
PLFSSDELGDIPSLELELIGYISEDSFATAFDVNQVRKFTEDEMKAINLKRKKSETTLDTTESVPKEDAN
SKADPNIKTKYADELLSIEQIKPFGQLVNSSREIILTEPEAEFVVKVVKHVFKDRLVLQFLLENTLEGIQ
LSNGIVVLTPTGGDKKEESIKVDQIDSSEGTLSIVRFKKLDWDIEEGYVVNGLFFTTKEIEGDTSEPEDE
GFQDEYSIDPFQITAGDFVRPVRIKNFPATFDRLKREITFVLQGDIYASGKKILDKILLNSMKIPTEETE
TPNDSNTHVMKLNGKAYHGTKVSIRVKMVYSMACGCTVKVYCDGESLYVTQLVVGLFD
>gnl|CDD|227566 COG5241, RAD10, Nucleotide excision repair endonuclease NEF1, RAD10 subunit [DNA replication, recombination, and repair]
MNNTDPTSFESILAGVAKLRKEKSGADTTGSQSLEIDVSPLQKGNPQLSRRINSNWVYNAFIKPDEWTDS
KATDLFLSLRFHSTRPEYIVLRISKLKSYKERPLLNHVDSTNWRASIQELVSTTGINTIYLDYSVEERSR
YFLTLTYHKLYSDYIIRRMQSLDRSNEFLILIFIVNKSDSEDTLNDIGKLCRFNGASRDEFELLLGFGFE
KAAKYIEYLNLPFM
>gnl|CDD|227567 COG5242, TFB4, RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit TFB4 [Transcription / DNA replication, recombination, and repair]
MDAISTFKHARSKQVTEESPSLLFVIIDLEPENWELTTEKGSRDKVLNDIVVFLNAHLAFSRNNRVAVVA
GYSQGKTYLYPSSESALKASESENTRNSDMYRRFRNVDETDITEIYRLIEHPHKNSQRYDVGGAMSLGLA
YCNHRDEETSLKSRILIFTLSGRDRKDQYIPYMNCIFAAQKFGIPISVFSIFGNSKFLLQCCDATGGDYL
TVEDTEGLLQYLLSLLFTDGELRPLGVKPNHGSVDFRATCYCHNRVVLLGFVCSVCLSVFCRPVPVCKKC
KSKFSFRKPVVTKLES
>gnl|CDD|227568 COG5243, HRD1, HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones]
MRFILYVLASLVLFGLSVLLSLYSSATVYSALVMTSQLSPVHITIGLNVILLLFFLIANALKTLLFGSLR
TFELELLYEQLWITLTEILLAISVFREAISFSFFMLLSTLLFAKVFHWILSFRTERLQIQSTDQRFHIFS
RFSCAYFLLSILDASLIYLCISSEHLIDKSTLFLFVCEFSVLLLNLTSEANKLCVYNYEARDDDDERSTY
LFRLEVCYDGLTLLAYSLLFMYQFPYVRVPIYLIRQMYTCFYALFRRIREHARFRRATKDLNAMYPTATE
EQLTNSDRTCTICMDEMFHPDHEPLPRGLDMTPKRLPCGHILHLHCLKNWLERQQTCPICRRPVIFDQSS
PTPASPNVRNTQIATQVPNPDNTPTTTAVPGITNSSNQGDPQASTFNGVPNANSSGFAAHTQDLSSVIPG
WTMLPIPGTRRISQSTSTTNPSATPTTGDPSNSTYGGPQTFPNSGNNPNFNRGIAGIVPPWRLVSSNTQS
L
>gnl|CDD|227569 COG5244, NIP100, Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell division and chromosome partitioning]
MSLLSVNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDS
LLNGNAAYEKIKGGLVCESKGMDKDGEIKQENHEDRIHFEESKIRRLEETIEALKSTEKEEIVELRRENE
ELDKINLSLRERISSEEPELNKDGSKLSYDELKEFVEESRVQVYDMVELVSDISETLNRNGSIQRSSVRE
CERSNIHDVLFLVNGILDGVIDELNGELERLRRQLVSLMSSHGIEVEENSRLKATLEKFQSLELKVNTLQ
EELYQNKLLKKFYQIYEPFAQAALSSQLQYLAEVIESENFGKLENIEIHIILKVLSSISYALHIYTIKNT
PDHLETTLQCFVNIAPISMWLSEFLQRKFSSKQETAFSICQFLEDNKDVTLILKILHPILETTVPKLLAF
LRTNSNFNDNDTLCLIGSLYEIARIDKLIGKEEISKQDNRLFLYPSCDITLSSILTILFSDKLEVFFQGI
ESLLENITIFPEQPSQQTSDSENIKENSLLSDRLNEENIRLKEVLVQKENMLTEETKIKIIIGRDLERKT
LEENIKTLKVELNNKNNKLKEENFNLVNRLKNMELKLYQIKDNNTLNKIYLDLVSEIMELRETIRRQIKE
QKRVSIDFSWLDELKQPFKEHIIEMFNFVSTSRILDLKL
>gnl|CDD|227570 COG5245, DYN1, Dynein, heavy chain [Cytoskeleton]
MDINNALCSEIDRVADKLKSLGDIHEWIVDHNGHAYPYRGEMPDEFGYIVKHGKDGLLILKGGHEFIVDA
ISRFMIPAAASKLRKVAATKMLRSLELHIKQMEKIVGGKTCSDSKGMAMETQDVARLYEKYSEEFHSGLD
LGKTLLSHELELIFRSGEQWVGCMRKLYESVCSERDGFYEEKSFWSRFHMEMCHIREFCRSKAFRFACDV
LRKSGKYVTVATLDSLLSSSKYSELGRRLHFYANMDFSGIYFPKSFSEFKDSVISATQAVSRDIGRQSRM
ARRLILVQMDSLARLIVDRICEYVSIEWLGCCEELLTCSMESMSSLVNSFDGEESEAMSLESSLFYEFRG
GEHLAGFYSAFGDIKRILLFTWSFKKLGTLLPSLPGYSSGGMDYGEEYRSLLWELGSEVGDPDSGPVRKW
MRKDLFDAKVRSGVSFGKQEEFVSDIFNITFERIHGMDPTTLEDDEEDTPALAILLGQEEAGRFVKLCKI
MRMFSFFNSLEMFSRRTLANRMAIVKYLSSVVRTGPLFLQRDFFGRMSELLMARDMFMEVDGVLRLFFGG
EWSGIVQLSGIRRAKRCVERQIDDEIREWCSSVLSDDFLEERAVRVERGADGARRLRASSGSPVLRRLDE
YLMMMSLEDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILEDVGDDLDLFYKEMDQVFMSIEKV
LGLRWREVERASEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTVFSSRIQKKEPFSLDSEAYVGFFRL
YEKSIVIRGINRSMGRVLSQYLESVQEALEIEDGSFFVSRHRVRDGGLEKGRGCDAWENCFDPPLSEYFR
ILEKIFPSEEGYFFDEVLKRLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKRFIKVRS
SYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFEAVCDEVCRFVDTENSRVYGMLVAGKGRIYDGTEPRSRI
EAGPICEEERGTEESALLDEISRTILVDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINERNIVLE
IGRRALDMFLSNIPFGAIKSRRESLDREIGAFNNEVDGIAREEDELMFYPMFKSLKAKHRMLEEKTEYLN
KILSITGLPLISDTLRERIDTLDAEWDSFCRISESLKKYESQQVSGLDVAQFVSFLRSVDTGAFHAEYFR
VFLCKIKHYTDACDYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSKMEYEVERYVEKTKAE
VSSLKLELSSVGEGQVVVSNLGSIGDKVGRCLVEYDSISRLSTKGVFLDELGDTKRYLDECLDFFSCFEE
VQKEIDELSMVFCADALRFSADLYHIVKERRFSGVLAGSDASESLGGKSIELAAILEHKDLIVEMKRGIN
DVLKLRIFGDKCRESTPRFYLISDGDLIKDLNERSDYEEMLIMMFNISAVITNNGSIAGFELRGERVMLR
KEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSV
LERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSSIAVSWVTIC
GIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASV
ELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQKESS
TSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKD
ALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRN
IHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEKDTEATLTRVF
LVYMEENLPVVFSACCSQDTSVLAGIRSPALKNRCFIDFKKLWDTEEMSQYANSVETLSRDGGRVFFING
ELGVGKGALISEVFGDDAVVIEGRGFEISMIEGSLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEG
VRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKR
KGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKIWFGEQQSLRR
DDFIRIIGKYPDEIEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLR
EEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILI
NEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGMSFIRISKEFRDKEIRRRQFITE
GVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLS
QARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWK
QLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTD
EIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSS
EFEKWRRMKSKYLCAIRYMLMSSEWILDHEDRSGFIHRLDVSFLLRTKRFVSTLLEDKNYRQVLSSCSLY
GNDVISHSCDRFDRDVYRALKHQMDNRTHSTILTSNSKTNPYKEYTYNDSWAEAFEVEDSGDLYKFEEGL
LELIVGHAPLIYAHKKSLENERNVDRLGSKENEVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYVEDVV
YPIKASRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLVEIDRYPFDYTLVIACDDA
FYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILFLNHLNARKWGNNRDLIFTIVYGKKHS
LMEDSKVVDKYCRGYGAHETSSQILASVPGGDPELVKFHMEEMCRSSAFGVIGQLPDLALCAWLMGPCDS
EYLKAIVYSSRIDM
>gnl|CDD|227571 COG5246, PRP11, Splicing factor 3a, subunit 2 [RNA processing and modification]
MNYGGRGGSKTGGGGTASEIKKNKKRRSRQLLLEAYGQDLMDDPYLSKNHTGKYVCLLCKTKHLTEMSYV
KHREGKKHKENSSRRSEEKSSLGRENQTTHDFRQQQKIIEAKQSLKRSGIPSYKVRSLVEPKGGRRGLGI
QVNYEDDLAEEMPQYRIVSSLEQNVEEYDESFRYLVFACEPYENIAFKFENKEIDFLSIYEDWDAETGTY
TLQFFFLEAGPE
>gnl|CDD|227572 COG5247, BUR6, Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription]
GGSPVGNMGTMPKQNSQKKKKTRFPIARLKKIMQLDEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEAR
KKSSKRMTSEFLKRATESDEKFDFLKNMEQFKNRETQPEEESA
>gnl|CDD|227573 COG5248, TAF19, Transcription initiation factor TFIID, subunit TAF13 [Transcription]
MEREARRVNLFMKDIKSLMYAYGDVVAPRYDTAEALHEYVLDYMSILCTNAHNMAQVRNKTKTEDFKFAL
RRDPKKLGRVEELLITNEEIKLAKKAFEPKDSRYRKELRINTKMHSFITLNKFILT
>gnl|CDD|227574 COG5249, RER1, Golgi protein involved in Golgi-to-ER retrieval [Intracellular trafficking and secretion]
MDYDSSDTMNLITKMNDLKTLYQHYLDRLAPRPDVRWGITGGLFLLFCIRIWSTGGWYLICYCLGIYLLN
AFLAFLTPKFDMSFEQIEDDDEIEEGEKDNEFRPFIRRLPEFKFWYFSTRATGMALIGSYFGIFDVPVFW
PILVVYFIFLVFYTARRQIQHMKKYRYNPFDIGKKKYKSH
>gnl|CDD|227575 COG5250, RPB4, RNA polymerase II, fourth largest subunit [Transcription]
MPRAIFEEDAAQLKLGPEFENEDMLMLSEARYLIEGQLERRRRETNGAEFRSNDVKVFKSTLGYLDDFCR
FKDKEVAEALRTTLSGLGFHEFEIAQLGSLFCQSAEEAKTLIPSLGNKIDDAILQAILKELSLLRKFQ
>gnl|CDD|227576 COG5251, TAF40, Transcription initiation factor TFIID, subunit TAF11 [Transcription]
MIDQVISEDQDYVTWKLQNLRTGGTSINNQLNKYPKYKYQKTRINQQEKESINKVPENDIEPDDILQQQT
QNSNYEDTNPGEDENELAQDERFKLLVTNLDEEQTNRYEVFRRTSLNKTQVKKLASTVANQTVSPNIRIF
LQGVGKVFVGEIIELAMIVQNKWLTSGPLIPFHKREAYRYKLKKYLKKLTFSIIENQQY
>gnl|CDD|227577 COG5252, COG5252, Uncharacterized conserved protein, contains CCCH-type Zn-finger protein [General function prediction only]
MPPKKMAKKQQESGKKATRDMRKELEDKTFGLKNKNRSTKVQAIIKQIETLNLKEQLEKKEKMRMEEKRR
EPEKQVIRAGVDPKTVVCALFLNKTCAKGDACKFAHGKEEARKTEKPDLYSDVRDKEEDVPLGKRPWINT
DRVCKFFIEAMESGKYGWGWTCPNGNMRCSYIHKLPDGYVLSRDKIKDSTQVEISLEEFIELERQSLPEK
LTPLTEENFKEWKDGRRLRILKQKEEKESARKVKGRATGTKGVELFETRRDLFKDDVEAGEEWDYTERCY
SESEDEEGHDKATAPIVSV
>gnl|CDD|227578 COG5253, MSS4, Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms]
TEERPPISRSGTGISMTHDKSTRPNDRSMSNDSSLCGLNQASDANGNEYSPNNKVSKKDTFSDQLHDALS
KEFTLERERDRLQLNKRKYQAIRLQTSTPIVEIFKNNKDAVDPPNHTRSSGNNLSNANVKTLSAPVGEHS
RSNNPPNLDQNLDTEPESSISQWGELQLNPSGKTLSSQPSRKPTSENPKSESDNSKLPTSVNSPLPDKSL
LKRTLSNFWAERNSYNWKPLVYPSCPSEHIFSDSDVIIREDEPSSLIAFCLSTSDYRNKMMRLRDSETMD
ERLLNGMPLEGGHRNPQESYNMLTGIRVTLSRIEEIMIKKTDTHLNEQFEEGLYEFSCKDYFPEVFRELR
ALCGCDEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMIFEYYVHVLFNPLTLL
CKIFGFYRVKSRSSISSSKSRKIYFIVMENLFYPHGIHRIFDLKGSMRNRHVERTGKSMSVLLDMNDVEW
IRESPKIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDEREEASVGLIIDFIRTRMTGDKKLESG
IKDKLTVGSFTKRKEPTAVTPRQYKNRFRKAMEAYIDPFPDKKTQEGFKTNP
>gnl|CDD|227579 COG5254, ARV1, Predicted membrane protein [Function unknown]
MVCIECGSRVDSLYTRYSTSAIQLSRCPSCNRKMDKYFELDGVLKLIDLLLLKRRIYRHLLFNSLRARTF
TNDVLCMLAVRMFCEPILQLHEAFGLLLSWGPGEGVSIAEMATICRDVPESLMETSLILRLVFSMQYLHA
GFVCLSSALLLSSFYYLFMFIMTMWKYQCEESLLVIELSCVACNSPVIMEIWLYDNEIALGCIYWVKFAA
GLVCLRILTTIRLNFFLSGCSTIPKYSPA
>gnl|CDD|444073 COG5255, COG5255, Uncharacterized conserved protein [Function unknown]
EAYPAQLQGPKFDPDGEFLPFPGNTVICHLAENSEFYAALLEAQQRLLEMPFADLFAFLPPSSLHMTVFD
GVWDSARRDPYWPSDLALDAPLQECTAEFFDRLQGFPLPPPLPIRWRVLGLMVLPRPVGVCLVPADEADY
KALRALRRALYQLLGLRIPDHDTYTFHITLGYFGRWLTDEERAALQALLSELLERLLEKAPVITLGRPEF
CKFEDMTAFERLLVLPVL
>gnl|CDD|444074 COG5256, TEF1, Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]. Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERG
VTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQ
LIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEA
LDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQ
AEPGDNIGFNVRGVEKNDIKRGDVAGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTF
VELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVK
PKK
>gnl|CDD|444075 COG5257, GCD11, Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]. Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
KKQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATFYKCPNCEPPEAYTTEPKC
PNCGSETELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVI
VQNKIDLVSKERALENYEQIKEFVKGTVAENAPIIPVSAQHKVNIDALIEAIEEEIPTPERDLSKPPRML
VARSFDVNKPGTPPKDLKGGVIGGSLIQGVLKVGDEIEIRPGIKVEKGGKTKYEPITTTVVSLRAGGEEV
EEAKPGGLVAVGTKLDPSLTKSDSLVGSVAGKPGTLPPVLDSLTMEVHLLERVVGTKEEVKVEPIKTGEP
LMLNVGTATTVGVVTSARKDEIEVKLKRPVCAEKGSRVAISRRIGGRWRLIGWGIIKE
>gnl|CDD|444076 COG5258, GTPBP1, GTPase [General function prediction only]
MSADRAALEKAPKRGERGNIEFKERLSREYHLAEGRLESLAAQMKYRLESGDGEATYVIGVTDDGEIAGI
SPDEFSESMDVLSLLAEEIGAKIEDVETWEVGDGGLVGVVTIREGKEKDPEHIVVGVAGHVDHGKSTLVG
TLVTGKLDDGNGGTRSFLDVQPHEVERGLSADLSYAVYGFDDDGPVRMKNPLRKTDRARVVEESDKLVSF
VDTVGHEPWLRTTIRGLVGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVAITKIDKVDDERVEE
VEREIENLLRIVGRTPLEVESRHDVDAAIEEINGRVVPILKTSAVTGEGLDLLDELFERLPKRATDEDEP
FLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIA
LKGVEEEELERGMVLLPRDADPKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRFEPIDKGYLLP
GDSGRVRLRFKYRPYYVEEGQRFVFREGRSKGVGTVTDILD
>gnl|CDD|227584 COG5259, RSC8, RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / Transcription]
KTNSVDKKHDSGEERNEQSAEIMDHSKSANEKKTTILRVEAETFLMEQTHPIIIPSYAEWFDGSKIHEIE
KRSNPEFFNGRSPSKTPEVYKDYRNFMINSYRLNPNEYLTVTACRRNVAGDVAAIVRVHRFLEKWGLINY
QVDPGTRPSTIGPPLTSHFQDLHDTPRGLSPFLPWGPINQRVLGAKEIEYETHKEENYSPSLKSPKKESQ
GKVDELKDHSEKHPSSCSCCGNKSFNTRYHNLRAEKYNSCSECYDQGRFPSEFTSSDFKPVTISLLIRDK
NWSRQELLLLLEGIEMYGDDWDKVARHVGTKTKEQCILHFLQLPIEDNYLSKGDGKGDNSKGRLPFDGSE
NPVLSTISFLAGIVNPRVQSEKQRAIIKSGKISHINRESQEHIEEVIEYALDSGKEKAKLQATNEERKME
RLRNVLIQAQLEKLKMKLGHLKELEKSTSLERQELDANLLLRRLNAEEKLFAIDEVLSKCLNLISDDQGK
NPDNKPSTETGENHLGQEISNETDVKPISKEAPQFYRYWSL
>gnl|CDD|227585 COG5260, TRF4, DNA polymerase sigma [DNA replication, recombination, and repair]
MNRSSKLFISLNSSSEEEFETIMEQKERRPLDAKKVSIQELLELSIDSVFNEESDELTSELLEFYDYIAP
SDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTETGLALPKSDIDLCIISDPRGYKETRNAGSLASHLF
KKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRR
ALNDVATGTLSSYTISCMVLSFLQMHPPFLFFDNGLLSPLKYNKNIDNLGVLFDDFFELYGKSFNYSLVV
LSINSGDFYLPKYEKGWLKPSKPNSLSIQDPGTDRNNDISAVSFNIKDIKAAFIRAFELLSNKLFTLTSA
IKHDAYGLLIEFNEASYSNTSRSLKEEYDSIYEKAPIPPERYNKVDPYIIRKCLILPDSDMSLQYFTYYC
DSYEKLILKAVLDKLEEIIEISSQYSRPPTLQGSNFIENPSCLISLESDDQSDQNDINPDTV
>gnl|CDD|227586 COG5261, IQG1, Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms]
MTAYSGSLNRYVENLGRPIGTPSHLKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALPELCFEDSL
RNGVFLAKLTQRFNPDLTTVIFPADKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYC
IHALISMLSWPGKTPLINSSGQISFTKEDIAACKKAWPRIPDFKSLGTNINTAASPEEPKEKRSGLIKKF
AKFQRPNIPVESILITPRKSITDANCSTPSDYLKATLKRFPYKRHSGTLEDSVLPQTSLSLFSTRRSTSV
FYTISLEMISNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKRGNKIRLLIQNRMPQEEDTK
FAERLQSNINGRKKYFPLDRRLSLFGPLFFLLQSSIPLFSIAICVGRVKRFSIDALLNIVKLQILGNGYE
IRKLYSLGKSNCEEHLSVSLFQMLLRTEVEATSLVQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQII
NDVAIHEDLEVDINPLLVYRALLNKGQLSPDKDLELLTSNEEVSEFLAVMNAVQESSAKLLELSTERILD
AVYNSLDEIGYGIRFVCELIRVVFELTPNRLFPSISDSRCLRTICFAEIDSLGLIGGFFFLRFVNEALVS
PQTSMLKDSCPSDNVRKLATLSKILQSVFEITSSDKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFE
FDQYIDLVKKSRALEYLVNEIYLTHEIIIEYLDNLYDPDSLVDLLLQELGELCSFPQDQRDTLNCLVTLP
LFNRSDDPIRDLKQQLKRTRVYIIYVDAGTNLFEQLLRLLPSDEPATRNPLDLNPNIRDDPSVSSLKSMS
LMKLKIRAIELLDELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLD
SQLQIYGSYLNNARSQLQPKKSKLKGFSRGVGVVRDKPKSISSGTFKYSAQQLYKRGVLVNITIPEPNVS
NIYFTFSSDSTDNFVIEVYQPGHSVSLPEVSFCFDDLLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFY
RKNA
>gnl|CDD|227587 COG5262, HTA1, Histone H2A [Chromatin structure and dynamics]
VVSGGKGGKAADARVSQSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGN
AARDNKKKRIIPRHLQLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKRSQEL
>gnl|CDD|444077 COG5263, COG5263, Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism]
ELLTTLYVNAGNNTYVASSTSVDATYVNGGYGVFAASDVDLVTENVTVENEKTSGVNGKSKDGGAGEVSE
KGDLSSDVGYVTDSAQGGSGNSSAGNNNDVYDVYVVYEGGSVKDYGGGVSDDGDDVVDKTNVAAGGGGKT
KKGDTNSANTGYLGDDLGGGTADKGGSAGYGAGKDGATAAAKELVGSAADTYYGGASTYLTGDAGAYGAL
GLAAGSGAGAKKTGSTAGASGTAYGDSGGTAGSGLSSLGGSSNALESGGENNQSLAGNGTSYDDAGAAGV
DGTGTTGTVGWVDGKWYYFDAGKMVTGWQTINGKWYYFDSDGAMATGWQKINGKWYYFDEDGAMATGWVT
DDGKWYYLGSDGAMATGWQKIDGKWYYFDSNGAMATGWVKVDGKWYYFDSSGAMATGWLKIDGKWYYFDS
DGAMATGWQKIGGKWYYFDSNGAMATGWVKVDGKWYYFDSDGAMATGWQTIDGKTYYFDSNGAWVG
>gnl|CDD|227589 COG5264, VTC1, Vacuolar transporter chaperone [Posttranslational modification, protein turnover, chaperones]
MSVLPPLVKKPVPGKRIAGPVRVEPKVWFANERTFLSWLSVTVLLGGLGFALYNSGDRLGMISAYVFTIV
AIFCGFYALMLYLKRAVNIRQRSAGPYDDRLGPTLVCVVLLVALIVNFFLAFKAAA
>gnl|CDD|444078 COG5265, ATM1, ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones]
APSARAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGA
AALLVVPVGLLLAYGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRD
IERGTKGIEFLLRFLLFNILPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREM
NEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAM
MLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPP
LVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ
DIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGE
RGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDAD
EILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEALAA
>gnl|CDD|444079 COG5266, COG5266, Uncharacterized protein, contains GH25 family domain [General function prediction only]
MKKLLLLAALALALLLAASAQAHDLWLEPSSTVVSGGGWVTLDLAFGHPFEGDHMPLKPERPKRLEVVAP
DGKKTDLENGAEGKYRATADVKLEQPGTYVVAVEPDPGFWSKTADGKRYWRGPKREVPEGALKSEQYQKY
AKTLVTVGGPSDGWDKPVGLGLEIVPLTNPYDLKAGETLTFQVLYDGKPLAGAEVEVEYGGDRYPDDAGA
QVLKTDADGKFTFTLPEAGLWLLAALHKDPAPDKKGADGRSLWATLTFEVK
>gnl|CDD|444080 COG5267, COG5267, Uncharacterized conserved protein, DUF1800 family [Function unknown]
MAAAYAAAWTRAEAAHLLRRAGFGATPGEIAALAADGPEAWLDAQLAAPALPAPARLAALRTLTPAERRK
ALRREARRLFRELAAAWLRRALTSPDQLRERMVLFWHNHFVVSADKGDVRSALAMAYYNDALRPHALGNF
RDLLEAVALHPAMLVYLDNAQNRKPDGPNENYARELMELFTLGVDGGYTEADVKEAARALTGWSIDRPGD
GDTGPFVFRPNRHDPGEKTFLGRTIGGTGEADGEDALDILAAHPATARFIARKLARRFVSDNPPPALVAR
LAAAFRDNDGDLRAVLRALLLSPEFWDPEAIGGKIKSPVELVVGALRALGATPPDPRPLLGPLRQLGQPL
FRPPSVAGWPDAGRAWINSSTLLARLNFADALANGAGGGVTADAADPRALADLLLGGALSPATRAALARA
ESPAEALALLLASPEFQRR
>gnl|CDD|444081 COG5268, TrbD, Type IV secretory pathway, TrbD component [Intracellular trafficking, secretion, and vesicular transport]
MAEEAVEGFRVPVHRALTRPILLGGAPRELAILNGTLAAALGLGLQLWIVGLALWLVGHALAVWMAKRDP
QFFKVYLRHLRYKAYYRP
>gnl|CDD|227594 COG5269, ZUO1, Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones]
MPNWIIKFEKPVGELARIHSEYFKGRNVLNLYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKK
VYKYHPDKTAAGGNKGCDEFFKLIQKAREVLGDRKLRLQYDSNDFDADVPPPRIYTPDEFFEVWEPVFER
EARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKL
KNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAALKGKAEAKNKAEIEAEALA
SATAVKKKAKEVMKKALKMEKKAIKNAAKDADYFGDADKAEHIDEDVDLIMDKLGDEELGQLAADIKAEA
AGAAAVFDEFAKMFIDRGKLPSADLSFFA
>gnl|CDD|444082 COG5270, PUA, PUA domain (predicted RNA-binding domain) [Translation, ribosomal structure and biogenesis]
RPVYLGKIHLYWCDKCNVPLLGKKCSICGSETREVPLTPPGDVRPAFPYDIELINRLLLEQFGADLIPEG
RLVLLNKIPGEDRMDEVIVDGEVIGTLRFDPEERRWRFDLRPEGARLLVEHATKKIVVLDKGAVKFHKGK
NVLAPGVLSADPDIKKGDEVIILTRDGEVVGVGRARMDGAEMVESERGVVVKVRKIKPPEPSVPPGEATD
EDDVVAANNELLEEEANAAAHIKRRTVNKPKLPAPVSSSGGGDSLALLLLLLAAGALFFLFFFDTGLETP
ETVEEVVEEAGEFLLKVIRADAPAKAAFDFGPPGPPPPDKRKCCCKCCKLLKTLIILPEGGKCGVLGGGG
QRRERRRRSSVSRRRWWPPVVNNSPIAAPIQLSSALLWWLIILKYLYLYPLYYERGGDIGCCCCPCSLSL
EDELEEREHELKWPEELEYLWRRAKRRGLPPKWGEWGWWRWWRWPPKKAKEAAKKKGLDEPEPITRLL
>gnl|CDD|444083 COG5271, MDN1, Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis]
SINDDRTVILDLDNSLAGRDLEDDDADLAGLDTQSETASEREDKLPDTDKDLLILTDADAASDEGKLLDL
KSADGAALSAESDAGASLITAANLEEGDIAGNAADDSADEESDANAKEDATDDADSSGDAQGDPLATDTL
GGGDLDLATKDGDELLPSLADNDEAAADEGDELAADGDDTLAVADAIEATPGGTDAVELTATLGATVTTD
PGDSVAADDDLAAEEGASAVVEEEDASEDAVAAADETLLADDDDTESAGATAEVGGTPDTDDEATDDADG
LEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEA
ATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEA
DEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDD
GDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPE
ATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEE
EAAEDEAAEPETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEE
ADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLE
EALEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEA
GIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAA
EDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEESDDAAADDAGDDSLADDDEAL
ADAADDAEADDSELDASESTGEAEGDEDDDELEDGEAAAGEATADLAA
>gnl|CDD|444084 COG5272, UBI4, Ubiquitin [Posttranslational modification, protein turnover, chaperones]
MQIFVKTLTGKTITLEVEPNDTIEAVKAKIQDKEGIPPDQQRLIFAGKQLEDDRTLADYNIQKESTLHLV
TRTLGISEIELSNLKLDLDPNPSHLFIFILGLIGSYSYTIGSINGTVQKSGQIRDQLKINIQNLRTGLYI
LKLDKGNQLGFIKEAQIYGVAGQGAINSPVATGLNGQVRHYRNTTAIITGRDKHIVHYGGVIIYYDGLKS
ITL
>gnl|CDD|227598 COG5273, COG5273, Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]
GRRKSWLPSTLGFIVFLVRLLRTGLYAYKMFIGLFLLSRIVVYTLLVIVKSLSLVVLFIILFIVILVLAS
FSYLLLLVSDPGYLGENITLSGYRETISRLLDDGKFGTENFCSTCNIYKPPRSHHCSICNRCVLKFDHHC
PWINNCVGFRNYRFFYQFLLYTILVALVVLLSTAYYIAGIFSIRHDTSLAICFLIFGCSLLGVVFFIITT
LLLLFLIYLILNNLTTIEFIQISRGGSTLEFFPLCRESNLPFTNIFDSSEGALPLDLGIGQNLSTIKGSN
ALYWLTPLHTNYCNSYDFSLRSDTLAELL
>gnl|CDD|444085 COG5274, CYB5, Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism]
MKKNTTPATDAAAPEKTYTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFN
TKHPHSPKAERLLESYRIGRLAQ
>gnl|CDD|444086 COG5275, COG5275, BRCT domain type II [General function prediction only]
DTLHEKIMARFVDRRTSALMRGLAVREEMLAGVAADGPQTVEGHPVIRLSGAQFEAAQGQSVLETKELRA
ALDHAVGVEIAKELGRLAAAPDEAFGLSPDGTVLWQGEAAGVKTGGAPFSLRKRLLADLGHDAARQRAQR
ALEAFEAFEAARRLSLLRALEVAVAEGKIRGSAEGLAYRLPESRKRAGRVLDRAEVRQDVELYQVEKRAL
RGLRVVITGALSLMMRDLLQDLARALGAHVAQSIASKTTCLVTGPQDSASSKALKAYQLGVPVVDEEAFD
ELLAEEGP
>gnl|CDD|444087 COG5276, COG5276, Uncharacterized secreted protein, contains LVIVD repeats, choice-of-anchor domain [Function unknown]
LLATGTASNVELLGNVDLGGRANDVWVSGEYAYVAGGSNGLAIVDVSDPANPVLVGSLPTPGGTWRDVKV
SGDYLYVASEGSEGLQIFDISDPANPKLVGRYDTGGSGAHNIAVDGNYAYVAGGSDNGLVIVDISDPTNP
VLVGRYSLPGQAYLHDVQVVGDYAYVADWEDGLVIVDVSDPSNPKLIGSYDYSPPGYTHTAVPVEDGNYA
YVGDELGGPNGLRILDVSDPANPVLIGTYPTPGADGAHNLYVSGNYLYVADYNAGLRVLDISDPSNPVEI
GYFDTYDAGFGGAWDVYVDPGGYIYVSDINRGLLILRVTG
>gnl|CDD|444088 COG5277, COG5277, Actin-related protein [Cytoskeleton]
MSDAYKLKYVIGIDFGTSYVKYGPIALEEKPRVIQTRGLFLRIVGESKLLGPMEGLSRGLVVGDEVSKYL
SSVRDAIRNLKYPLRDGIVRRDDEDAWRVLKELLRYTFAQFLVVDPEFHGFLVVVALSALAPDYMRERLF
DIHFEVFSEEGAPAVTIIPQPLAVAIAEKAVTCVVVEAGHGNSQVAPISRGPIREGLVALNRGGAEANAI
TREILKDRGYSDTAREEYVVRVVKEALGLVPRDLAKAIQKAASNPDSFEAKVRLPNPTVEIELGNYAWER
FLIGEILFNPNHEGFESYIQQGRLRIEDAVIGDVVLYGEMGLAEAIINSIMKCDVEIQDELYSNIILSGG
AFNWSVPPGLEDVAVDSVTRVQIELSELAPELKVNVRLVSDPQYSVWKGAIIYGYALPFSVKWSWITKEG
WYFL
>gnl|CDD|444089 COG5278, CHASE3, Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]
MKNLSIRRKLLLGFALALLLLLVLGVLSYLSLNRLREASEWVEHTYEVLRALEELLSALLDAETGQRGYL
LTGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALA
LVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLE
AELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAA
AALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL
LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAE
ALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAA
AALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL
>gnl|CDD|444090 COG5279, CYK3, Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle control, cell division, chromosome partitioning]
GVSKVYIKAIYAEALSDLFLLAGNAAVTKDTTLTGLGSLYELAVLLFALLEGNSLAAFLKDAISSSTIYA
LKDEEGLLTEKATIADESKDDDYIITPGMSDYEKVRAIHDWIVDNIEYDYEAYNSGKSDSHSAYGALKNG
KGVCEGYAKLFKLLCNKAGIECYIVTGYARGSGGESGNHAWNAVKIDGKWYLVDATWDDGVPDNGGGDVN
YDYFLLSDEEFAKDHLPEDPKWQLLDYPISKDEFANLYYV
>gnl|CDD|444091 COG5280, YqbO, Phage-related minor tail protein [Mobilome: prophages, transposons]
MADRIKGLTIEIGGDTSGLTKEIKGFGKKFERAGEKMDRAGKKMKSIGAALTAGVTAALVAAGAAAVKAA
ADFEKAMSTVQAVTGATGEELEALEQLAKELGATTGESAAEVAEALGSVAQAGLSGDELIAVTEGALVLA
AATGVDLNEAAEIVASAMNAFGLSADEASRVADLLAAGAQAGNTTSDELADALKEYAPLAAALGFSLEET
LAALALLANAGIKGSDAGTALKEFLIRLADPSKTAAEALEELGINVFDASGKLKGLSEILGELAKKFAGL
GEAARAAVLAAIFGDDAGRAAIALLLFGTDWYAKLTAALKNSAGAADEAAATMQDNLAGALESLKSALEG
LAITIGETLLPALRDAVEALTGLADWFNELSPAVQELIIAIAGLVAALGPLLLILGALITGIGALAGAFG
ILSTALAKAKGALLAGPIGIVIAAIAALAAALVLLYKNWDTIKEFLTGLWNSIKEAIGGVWDGIKTSVEG
LKGAAGAALSAAAGKAIEALAGISVDALKQGVILSGTISMLWGAAGTEVSLKGGAAQDNVSDAASSAGDG
ALAIINSAEQAIIGLAAALKTASTSSALQASTKAAAATKAEKTILAIAMATVKGVTSATAALANAAGVIL
QGAIKNGISGALDSAGATTVAKLAEEEAINEKIVELLKAAANGANKEAVANALLLDAAAKQNINGQEAIL
EGITAKGVQTDELQDSDAIQAKFQFEELSEGAKATINAINGNGVLGGIIADGIKTNSAELKAAANELKGD
INRVAAAINSLAEAGAEEIKSEAKEAGSDKAITGEAGQAALELAVARVNALISRVTKNITGTLSGSTVSI
LKGNTTEIENASKKITESGDKIMTGKDIELLAEGEFAVLIKNVKANGGNIAGGGGGGVKSIGASGNNNVR
SLTVGTTGVSGGFGGEVSDEAIIIKATLGISINNTRYDRPGIGFSGSTLQLP
>gnl|CDD|444092 COG5281, COG5281, Phage-related minor tail protein [Mobilome: prophages, transposons]
AAALAAAAALAAAAAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAA
AAAAAAADALAAALAEDAAAAAAAAEAALAALAAAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAA
AAAAEAAKAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAA
AAAAAAEAAAAEAQALAAAALAEQAALAAASAAAQALAALAAAAAAAALALAAAAELALTAQAEAAAAAA
AAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAAAQALRAAAQALAALAQRALAAAALAAAAQE
AALAAAAAALQAALEAAAAAAAAELAAAGDWAAGAKAALAEYADSATNVAAQVAQAATSAFSGLTDALAG
AVTTGKLLFDALASSIASIADALANAALASAADALGGALAGALGGLFGGGGGAAAGAAVYAGALGPFASG
GVVSGPTFFAMAGGAGLMGEAGPEAIMPLARGADGRLGVAAAGGGGGAAVVVNITTPDAAGFRRSQAQIA
AQVARAVARGGRGLAAAAAAAGAADGGAGGGAAAAKKALAGSG
>gnl|CDD|444093 COG5282, Zincin, Zn-dependent metallopeptidase, zincin/DUF2342 superfamily [Posttranslational modification, protein turnover, chaperones]
MSDNPADLGQMFAQLQQMLSGGGDGPVNWDLAADTARRLARAGDPSVTRAERAALRDAARLAELWLDEVT
GLPAGVGPALAVDRAEWVEATLPSWRRLTEPVAESLADALGEALPEEMAAMLGPLGGMMRQMGGAVFGMQ
LGQALGFLATEVLGQYDIGLPLGPPGRLALVPPNIAAFERGLDVPPDDFRLWLALREAAHRRLFAAVPWL
RDHLLGAVEEYARGITIDTSALEERLRGLDPSDPEALQEALSGGLFEPEQTPEQRAALARLETLLALLEG
WVDVVMDAAGPERLPSVAAIRERFRRRRATGGPAERTFRRLVGLELRPRQYRDAAAFWRAVVDAVGMEGR
DAVWAHPDLLPTAAELDDPAAWVARVHG
>gnl|CDD|444094 COG5283, COG5283, Phage-related tail protein [Mobilome: prophages, transposons]
LQVILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQ
ALDQAGIDTRQLSAAQRRLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQRLAGAGAAAAAIGAA
LAASVKPAIDFEDAMADVAATVDLDKSSEQFKALGKQARELSAQTPQSADDIAAGQAALAQAGVSAEDIL
AFTPTAAKLATAFDTDAEEAAEIAAKILNAFKLPADDVERLGDALNYAGNNGATSLADLADALPYVGPVA
KALGVSGKEAAALGAALADAGIEGEEAGTALRNMLTRLTSPTKAAAKALKKLGIDTQDSKGNLRGLAKIL
AKQMQKDAQGALAELLKALKKLDAAKRAAALKQLFGEEAVSALAPLLQNGDELRKQLAVAEAAAAQGSMD
KEAAKRTDTLAGQLKLLKNALENLGISIGEALLPALRELAQALTPVVGKLADWAKANPGLIKTIVKVAAA
LAGLKAALGALRLALALLLSPLAALKAAAALLGGGGLGGAGRGAGALAALGGAKGLKLAGGAVLWLGRAL
LANPIGLVIAAIAAAAYLIYKYWEPIKAFFKGVWEGIKAAFSPAWEAIKALISNWLGPVWDGLAIAGAGA
GEAAAAAAVAGAQAAAGGAVTAAQLGAGAKNGAGATGGGGALLGLAGTGRALFAAGGGAAAVGGDGGGAI
AGSALSRSAGIAAFGAQAAGLAEKLGGLLGVQEAILEGTQGASQVLM
>gnl|CDD|444095 COG5285, PhyH, Ectoine hydroxylase-related dioxygenase, phytanoyl-CoA dioxygenase (PhyH) family [Secondary metabolites biosynthesis, transport and catabolism]
LLTDEQIAFFERDGYLVLRGVLSPEEVAALRAALDRLLAEAPDEGDLEYSEADGGRLRRIYNLHRRDPAF
RDLARHPRILAVAEQLLGPDVRLHHSQLFFKPPGGGGATPWHQDFPYWPLEPPRAVTVWIALDDVTEENG
CLRVVPGSHRWGLLPHRDDDGSLDDALDEEEAVPVELKAGDVLIFHGLTLHGSGPNRSDRPRRALVLRYN
AADNRPQERQWLAVPRGLPELARGRDL
>gnl|CDD|227610 COG5290, COG5290, IkappaB kinase complex, IKAP component [Transcription]
MENLFTRYMSTFPTASGDEDELGFDSVGDWIYITCVLGSTDKGIEVAKESSIYDESGLKRFEIPFFPDKL
LSFKHFHVLTFEYFLIDEGDIIHLVNDPTPAELEMEIVGKVSNGIVAASWSADEKTWCVVTSTREILLFD
KYFDPISEYHLKKSDLVEFGKHIRVGWGKKETQFRGKGARAQLRDPTMPYMVDYGDLFAVDTNKKIIFWR
GDTEYNLVGRSEERPRRAFRVYSREGQLDSASEPVTGMEHQLSWKPQGSKYATIGTDGCSTSESVIFFER
NGLRHGEFDLRVGCDEKAFLENWNLLSTVLAVAEGNLLKLWTTKNYHWYLKVERQIPGISYVKWHPEEKN
TLLFRDGERILRVFFSEKKTHHGSEYPFDNGTSYVIDGSYMLYTPLSLKNLPPPMFSVRVGFDTNVVDVF
PSFAEKKGAALLRDRLIMFRWDSEEFINKRTEFLESEFDSIVLFDGFLVLKSGHVFLLKDTNNESDTYIT
RNGDVDERKKRGTVETRRTSTLVHQLCQTLLRYGTCVGVVKHYNFEEKLYELLKFPNGVIDFSVDPVHST
LVAIGITDIGQLFALQVLLKKSVFSHNGTKLFVLFTTTENILSFVHLESTFKPLITVEEGTVRFFDERKR
SVERGSHKVELLPSKDFVVLQVTRGNLETIYPRIMVLAFVRKLIAAKKYKDAFDVCRTHRVPLGILLDYD
PELFIENLEVFVTECRRVDYLSLFSEALQRDDVTKTDYSFISKSEQARRFRKVFDLKVNLECKDTREHLE
SLIYNDESIQTIITAYLIGNPGNGKAALMRISPLSRCSESLDEDVKNLCFLRDVNFFNEFALSLYDKSLA
LLIAQLSQKDPREYLPFLVERQDLEALRRKFSIDNYLSIYESALGHLNEDLNVIREVMKYICRHDLYDFL
LLLYRYDGELQKFKINIFAGNLVDNLYHISAAKAYEVEGKYIEAHGAYDSALMWRECGSISTQEKGYEFN
LCAELLPSDLLVEFRKAGDAEKILLTYLENLYEAVAMDCKGSEYREAFCEAMVSRLVESEKHYEAGQLGE
EFGGKPELAADEYVQIKSQGDRLRVLRDKKCEMPEAREILREELLTLDDVSEAFVKYSTRLSALTEYTKD
ECMSKTSRSTTKNMRRGERKRARGKKGTRYEEEYLVSSIRRLILRLVGWRPETERLVEILKRFNMEEQAR
AHQTNFDEVGRAIKTEVDSIFSVERRLLERVNGEDPNRPVPEKPDFSKWLIVD
>gnl|CDD|227611 COG5291, COG5291, Predicted membrane protein [Function unknown]
MPSIPQGNNTFLLGQMLRIPPITRYMTLLISAVTILVYVDLVSPWYSLYYSPLFLKRLQIWRLFTSFLYF
GKPTLDMFMHVYFLYRYSRMLEEGCFNTSLVEYFWYLLVISLVIFAISNIYGGISALGTSFSATITYIWS
KRNPRAIIQFFGFISVPGKYLPFILLGFSFLSRRGISIDDVLGFVVGHLFHYFGDIYPMIGRDILSTPCW
VKKLFNEHPSSFCSARKGITIRHERNMGYSNASTTTEESQCCAETFKGSGVVLGTKSMAVSTVVGSSTEA
KNNYLDFTEALCDKEVVAEQNPESQSNEEWDEK
>gnl|CDD|444096 COG5293, YydB, Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown]
MMLKKLYSNLPRFKPIEFNPGLNVILGEISSPENDKDSTNGVGKSTLLELIDFCLGADKDKKRFLKHEDE
LGDHTFFLEFELDGKDLTIRRSVSDPKKISLCGDGYEWDHEKVSLEEAKALLEELLFGLPALKGPSFRSL
LGYFLRRQGDDFKDPLQLFSTAQKDADWKLYLAYLLGLDWDLAAEKYELKEEIKELKKLRKALKDELIGS
VVKSISELRAEILELEEEIEKLEKDLEKFDVAENYEELEKELDELKREINELRNERYSLERRLKKIERSL
EEEIDIDPDELEKLYEEAGVFFPDQVKKRFEEVEAFHKSIVENRREYLEEEIAELEAELEELEAELAELG
KERAELLSLLDSKGALDKYKELQEELAELEAELEELESRLEKLQELEDEIRELKEERAELKEEIESDIEE
RKELLDEINKLFSEIVEELYGNRKASLSIEVNKQGHLDFDAEIPTDGSTGINYMKIFCFDLALLLAHLNG
RFPGFLVHDSHLFDGVDDRQKANLLNLIAEVAREGGFQYIVTLNSDDLPKADDEGFDFLDKEIVLRLTDE
GESGRLFGFRFW
>gnl|CDD|444097 COG5294, YxeA, Uncharacterized conserved protein YxeA, DUF1093 family [Function unknown]
MKKFIKIGIIVLIVLIFGGLFLLKGPNLDRFNPFVGKETYYVKITNDGKKLKTKDSGNGYGIYEYTLTAY
DEDGKEKEVTFTASKELRKGAYLKLYNKGKGVKSWEEVQKEDIPKKAKEKL
>gnl|CDD|444098 COG5295, Hia, Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]
SASNAGAVAAGTALTTVASGASTTASGSSATVTSAAQSTGSAATSSGSSSAAGGSGSTSSLTAAAATAGA
GSGGTSATAASSVASGGASAATAASTGTGNTAGTAATVAGAASSGSATNAGASAGASAAAAAGSTAAAGG
AAASTGGSSAAGGSNTATATGSSTANAATAAAGATSTSASGSSSGASGAAAASAATGASAGGTASAAASA
SSSATGTSASVGVNAGAATGSAASAGGSASAGAASGNATTASASSVSGSAVAAGTASTATTASTTAASGA
AGTATAAAGGDAAAAGSASSTGAANATAGGGNAGSGGGGAAALGSAGGSSGVGTASGASAAAATNDGTAN
GAGTSAAADATSGGGAGGGGAAATSSSGGSATAAGNAAGAAGAGSAGSGGSSTGASAGGGASAAGGAAAG
SAAAGTSSNTSAVGASNGASGTSSSASSAGAAGGGTAGAGGAANVGAATTAASAAATAAAATSSAAIAGA
TATGAGAAAGGAGAGAAGGAGSAAAGGAANAAAASGATATAGSAGGGAAAAAGGGSTTAATGTNSVAVGN
NTATGANSVALGAGSVASGANSVSVGAAGAENVAAGATDTDAVNGGGAVATGDNSVAVGNNAQASGANSV
ALGAGATATANNSVALGAGSVADRANTVSVGSAGAERQITNVAAGTADTDAVNVSQLKAVNSSTDQRFNQ
LSNRINRVDKRARAGIASAMAMASLPQAYAPGKSAVAAGVGTYRGQSAVAVGYSAVSDNGKWTVKLGGSA
NSQGNVGAGAGVGYQ
>gnl|CDD|227615 COG5296, COG5296, Transcription factor involved in TATA site selection and in elongation by RNA polymerase II [Transcription]
MADFQDELLALAGIDDSDVASNRKRAHDDLDDVLSSSSDEDNNENVDYAEESGGEGNEKSEEEKFKNPYR
LEGKFKDEADRAKIMAMTEIERESILFEREEEISKLMERRELAIRMEQQHRSSGCTDTRRSTRYEPLTSA
AEEKKKKLLELKKTREREERLYSERHIELQRFKDYKELEESEQGLQEEYTPSYAEEAVEDISRTDDFAEL
YDFNQCRVGRDMVARNVFKPIFEDEVIGCFTRVRIGERGGYLVYRIVGVGKGSTYSKPYGRKEVKTNRYL
DVSTGRTYKVFRINNISNSPFLREEYQRVWRSFKVGKLSMPSIAKVKEKYDKLVDTMGRRLSDKEISKMV
ACKDEVHPKRSNVIHEKTELRQKRQRAIELKNKKAAMEYQRQLEEIEDNEGARVHNVNSGRPLLAKVNER
NRRRNHTEIRLAEQRMNEEAATATPMSAPTSVLTQPSPSLSTSIMPKLNPSESVVVASEKASSPDLSPKL
LPSEIAVTQTPAVHGIDDIIATVDFGIDINI
>gnl|CDD|444099 COG5297, CelA1, Cellulase/cellobiase CelA1 [Carbohydrate transport and metabolism]
GAGAGAASAGAAGAGALAGSDGTGAAGSGSGGDVASGAASASGSASGSSASGAGAGAGAAASGADTGSGG
GAGAGAGVGVGAGGAAGGAGGSAGVAGAASAAGAAGAAATSSGATSSSSSGTSSGGGGGSSSSTSDTTTS
SATSGSSTSTSSPTTGSTSTTTGGGIANQPTAVWDRIAAITATVRAHLDAALAAPLPGRDCGVTYSVYSD
WGSGYTAAVTVTNPGSLPLNGWTLAWDLPGGAGVTNAWGFTLNQSGYTVTATNVSWNGTLAPGGSVSFGF
DTSRNGWNPSGRGLDGACTGG
>gnl|CDD|444100 COG5298, YdaL, Predicted metal-dependent carbohydrate esterase YdaL, contains NodB-like catalytic (CE4) domain [General function prediction only]
ILLLLSLATLSANAAEAPTSAKAQEGKPKVLVLYDTTNNLKLGENYVIMLDNLLGHFNSDVTLIPVADYK
AGDLSRYDAVFYVGSTYDEPLPKAFLSDVLSYKKPVLWIGYNIEQLAQFNSRYGFLPTGFEPDNVDTVTY
KGKELTRDILDSEGILNVVITDSTKAKVLATAKDGEGTTYPYIVRSGNLWYVAEIPLSPRDRYLIFADLL
HDFLGPNTPERHRAYVRLEDVHPLVDPEALREIADYLYEKNIPFMVAVIPVYVDPKGGYVVTLSDAPELV
KALKYMQDRGGTIIMHGYTHQYGNVGVSGEDFEFWDAKNDRPAYVQYDGPLPEDSKAWAKDRITKGIREL
TDNGLYPLAFEAPHYAMSAEGYKALSKYFSTYYGQLQLSDKTFKVGQFFPYIVTDSYGMRVIPENLGYIE
PEEPRTPQDILENARQNLVVRDGFASFFFHPYLGLEYLKELVEGLEALGYTFVDLRELK
>gnl|CDD|444101 COG5301, COG5301, Phage-related tail fiber protein [Mobilome: prophages, transposons]
MTQKYYTLLTDIGAAKLANATALGTKLNLTQMAVGDGGGSLPTPDPSQTALVNEVRRAPLNSLSVDPKNP
NQIIAEQVIPEEVGGFWIREIGLFDDDGTLIAVGNCPESYKPLLTEGSGRTQTVRMVLIVSNTEAVTLKI
DPSVVLATRQYVDDKLAKHEKSRNHPDATLTEKGFVQLSSATDSNSETLAATPKAVKTAYDLADTAFVAA
SGNAAGTAATAAAAGGLTLNAAALSVSTYSATAGAVLGTGGLST
>gnl|CDD|444102 COG5302, COG5302, Post-segregation antitoxin (ccd killing mechanism protein) encoded by the F plasmid [Mobilome: prophages, transposons]
MPTTQSQAPKKATNVSLDADLLAEARALGINLSAALEEALAEAVREAKAERWLEENAEAIEAYNRFVEEH
GLPLDEYRSF
>gnl|CDD|444103 COG5304, COG5304, Predicted DNA binding protein, CopG/RHH family [Transcription]
MKKKIPKFKLDKEEEEFLDSHDSGEYVDVPDSKFKPAAFELKPKDKRINIRLSESDLEAIKARANEEGIP
YQTLIKSLLHKYVTGRLVEK
>gnl|CDD|444104 COG5305, COG5305, Uncharacterized membrane protein PF0508, contains N-terminal glycosyltransferase domain of PMT family [General function prediction only]
MSFSLLKSRRPRWLRLLLLLILLLGIALRFANLDRKSLWYDEAATLLRSLGYTFAEVPLDQIISLEELLN
AERSLGDLIRALAEEDAHPPLYYLLLHLWMQLFGNSEWALRSLSALFGLLAIPLIYWLGRELFRSRRVAL
LAAALMAVSPFHIYYAQEARMYSLLTLLVLLSLLALLRALRRPTRRLWLLYALANALGLYTHYFFALVLI
AHGLYLLLLAWFRRDRKTWLRYLLAAAAAVLLFLPWLLVLLTQLSRGNSQTGWISPPLPLLQLLAAWLLM
FSLLFVDLNPLTGLLALIFLILLILGLYFLLRRTPRRLSTWLFLLLILVPLLLLLLLSLLLGPDFSLVPR
YLIPYFPAVLLLVAYLLATLWRKPWKIALALLLLLGLLSCLVSQKSSDPLLI
>gnl|CDD|444105 COG5306, MJ1470, Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type IV pili-like system [General function prediction only]
MKRKLLIALLFLLLLLPASAHAWWNPDWSYRKPITIDTTAIGGDLTDYPVLVRLHTGNFDFSSAKEDGSD
IRFVAGDDKTPLKYWIEKFDPLNEMALVWVKVPSIPAGAGTTIWLYYGNPKAPSASDGKGTFDFFDALVW
HFAEAGGPPQDSTAYGNHAVGAGASVDGGLIGSGAQFDGTSPLVVPASPSLALDAGGGFTFSAWIKPAQL
DGNAVLYSRRDGANGLDNGAPFVEVGGAGGTRSAAGAPLAAGTWHHLAVVADAGKVTLYVNGVAAGSLDA
SLPTVTGGATIGAVGLAAIASLSGQAVEAGGALIGLLVAEIQAGVSEAAASVNGAAKRTLSAYRKDLASA
FSAGSQDRAALLQIAELDSESYVSSLVELVLWSAQEVGGLRPSYRSEAAGLVEQASLTAQFADAASASAT
SAIGAAGQSSNNVTTLNAIVVGSAAGLLLVTLTVGGAYGAATLATAGEITVAAPAVAASAAAAYTALAAA
AAALALDATDYLVRFTVAAATGLDRGENVTLTSEVTSDF
>gnl|CDD|444106 COG5307, COG5307, Guanine-nucleotide exchange factor YEL1, contains Sec7 domain [General function prediction only]
MGDEIDKLAKNEIIEAFNAKPKNGIAKIKEICEDNKIDFIAEIAEFFHEEKKNLDLEAVGDYLGSDEADN
QKVLEAFTKQFDFKEKDFLEGLRRFLKSFKLPGEAQKIDRLVESFGGAYFEQNLDIDINNADAAYILAFQ
TIMLNTDLHNPSIAEKKKMTFDGLKNNLKGGNEGGDFDAKFLEEIYDEIEAKPFELNFVDSSPGYEINNI
SLNKDKTFKKLDQFLEEKDVNINNIFPGIQGDNLKIEFDNPKSFLSFFTGYKGSIIIKDEKSGAQAEIQV
YKPNIFSKWFFGEKPKIIIQP
>gnl|CDD|227624 COG5308, NUP170, Nuclear pore complex subunit [Intracellular trafficking and secretion]
MRQEGPHVGVSGMGYYELLLLALHWIGMLLKRDTKTPSLDEAKYYEEGLDYIFSIETGFTPFYAQQVMNI
PDRILSQISRTEYKTDMGIFPELNRCWITNDNKLILWNYNNSNEYQEIDDFSHTILKVKLVRPKANTFVS
RISHLLFVATEKEVMILGVSKDTKTGELSLFNTGLVVSVQGINVRCIVSEEDGRIFFGGENDPNVYELVY
KSSDSWFNSKCSKICLTKSILSSLLPSFFSFGIPGETIKQLAVDQSRGLLYVLRKKSAVRAYSITKNGLV
GPVFISFASIDRNAAILNATSPLLEPRMYKIVKIVSIPAYENNQLFLVAITSTGCRLYFDGSRGRVSIVA
LKLDSVKFPPPSTLMQLEQNKGSRDFYENLFLDRLVMLKRQPNSSDMTETTEMSTIISPGIYFSAVNKRY
DSSNTNKGSTVTAISLNVDQHKLWVSIPDYGILKSSKYVENVVFLDDIELIQNIDPRTELFNQTNTPQAT
FALLYGNEKLFVAVLTSVEKEIYSYRTPDEIFSGLIGNPLPFYKSYGEAEACSTALLYYCKLNKSEDVGS
LALLFLKLGIPDVVDIKPKYYRYSGSVPILSQSRFNKPSSLDFVRLSPRFYGLALLITRLERNIWLERVF
SKMQNKMINIRGASIKIKIEYYLSGIDFLDEFLENNKSSIEGLNSPLISNDEIAVQAESIANNALLLEYQ
SIKEGLSLLNVLYEDGVSDFHEIVSSTSIDIQKSCSNLTFSELFTPNKTKKLIKEILKSLVNRNIQSGGS
IEYLIKTLSERCGSFCSAEDVLYFRALEHLNKAKSREVDLESLNNHLKNAVQLNESLVAKYNEEGLRYAV
TTMISLNYYPKAVNFLLEYAVEIDKGNQACAYVLNGLAENDPRKDFYDKRIKVYSLIFEILISVDKENSL
RNSELKCCVYPSAMGSNDRLFHYCFYDWLVFKGRTDRLIKIDSPFILPYLKEKAMSSLKISNLLWKYYVK
REDFVEAAQVLYELATSNFDVSLEERIELLRRANGFCSSHVPNSQKHVNVQLFNEVKERLEVASIQDDIL
RLVRVDPRIDNNKREELSKQLDGEILSLSELFNDYADPLKYPEIALKIFKISDYRDKAVIRELWEELMSS
HENAIISPVGSSDFESFVSFLSNLLIKISKSENVFPIMDLNDIVGDIFCDKEMAAGGSVGSAFLSAGVSH
LKVYYILEELIEQSKDRLFFLIKEMTWLIKEWYHSDMSFRARILLEDIKKLKNYNEFYDPVEKYCKRKYG
ILD
>gnl|CDD|444107 COG5309, Scw11, Exo-beta-1,3-glucanase, GH17 family [Carbohydrate transport and metabolism]
MKRRLLALLLLLLVALLHFGLWAWLNRPVPLPALGGKIQGVSYSPYREGQSPLKGDYPSEEQIKEDLKLL
APYTKCIRTYSVTEGLEEVPELAAKHGLKVMLGAWLSGDPERNEREIEALIELANEYPDIVKRVIVGNEV
LLRGDLTPEELIAYIRRVKAAVKVPVTYADVWHFWLKHPELADAVDFITIHILPYWEGVPIERALDYAKD
RYDEVRAAFPGKPIIIGETGWPSAGRQRGGAVPSEVNQARYLREFLAWANEEGIDYFYFEAFDQPWKRAL
EGTVGAYWGLFDADRQPKFPLTGPVVENPDWPLLAAAAVLLALLLLFLLARRRRRLRLLGRLFLAALAQA
AATALVWLAYLPADYYLTPLDLLVGGGLLLALLLLLAVLLIEALEFAEVLWARRWRRRFLPLPPAPAERL
PFVSIHLACNNEPPLMVIATLASLAALDYPNFEVLVVDNNTKDEVVWKPLEARCARLGPRFRFFHLPLWP
GFKAGALNFGLTATAPAAEVVG
>gnl|CDD|444108 COG5310, COG5310, Homospermidine synthase [Secondary metabolites biosynthesis, transport and catabolism]
VHARFDGPIVMIGFGSIGQGTLPLILRHFDVDPSRITVIDPDDTGRKLADERGVRFVQEALTPDNYREVL
SPLLTEGDFLVNLSVDVSSLDLMELCRELGALYIDTVIEPWAGFYFDPSLSPAERSNYALRETVLALKRK
WPGGPTAVSCHGANPGLVSHFVKQALLNIAADTGLDATEPTTREGWARLAQKLGVKVIHIAERDTQRADR
PKPPGEFVNTWSVEGFVSEGLQPAELGWGTHEKWLPADARRHDFGCKAAIYLARPGANTRVRSWTPTEGP
QHGFLITHNEAISIADYLTVRDGGKVVYRPTVHYAYHPCDDAVLSLHELAGKNGKLQPRQRILEDEIVDG
IDELGVLLMGHAKNAYWYGSQLSIEEARRLAPYQNATGLQVTSAVLAGMVWALENPQAGIVEPDEMDHRR
CLEIARPYLGPVVGVYTDWTPLQGRPGLFPEDLDESDPWQFKNFLVR
>gnl|CDD|444109 COG5314, COG5314, Conjugal transfer/entry exclusion protein [Mobilome: prophages, transposons]
MKRRSRRRRLAAALLAAALALSPLAPQPAHAQIIVFDPSNYAQNVLTAARALEQINNQITQLQNQAQMLI
NQARNLASLPFSSLGQLQQNLQRTQQLLGQAQGIAFDVQNIDDQFQQLYPSYYDSSLSDAQLFADAYQRW
QNTVDAFQDALKVQAGVVGNIDSDRATLSALVSQSQSAEGALQALQAGNQLLALQAQQLQDLRALVAAQG
RAQALEAARQAAAEEQARAQRRRFLGSGTGYTPGNVRMF
>gnl|CDD|444110 COG5316, COG5316, Uncharacterized protein, contains DUF4139 domain [Function unknown]
MKRRLLLLLLLAIAEAASTAAAQSALAVTIYNNGLALVRETRSLDLPAGENTLRFSDVAAQIDPESVLLR
GQLGLRVLEQNYDYDLLSPAKLLEKYVGKEVTVIRTNPAAEETEEGTLLSAEGGLVLETDDGIELLRPGR
LVFPSLPDGLRTKPTLVWTLDSAKAGKRELELSYLTGGLSWQADYVAELDDDGDTLDLSGWATITNQSGT
DFKDARLKLVAGDVNRVRPRPPLPAAALMAAAMAEAAAPAAEEESLGEYHLYTLPRPTTLADNQTKQVAL
LSAAGVPARKEYVYRGGPNDEPLKVAVLLEFKNSKANGLGMPLPAGTVRVYKEDSDGSLQFVGEDRIDHT
PKGETVRLKLGRAFDVTAERKQTDFKRLSKGRTEEETFEITLRNAKDEPVTVRVEEPIPGDWRILSESHP
HEKKDAGTAEWKVTVPAGGEKTLTYTVRVRY
>gnl|CDD|444111 COG5317, COG5317, Uncharacterized conserved protein, DUF1465 domain [Function unknown]
MSESEAGGAAPVSFAERFASSELFEALYREGMVLVEETAAYLDGPGREEAKALDRLAALAYATESMRLTT
RLMQLASWLLLQRAVNEGEMSPEQAASEKRKVRLDAPDPRDPDGWDELPERLRELIARSLRLQERVRRLD
RAIYAPAAAPAPAANPVAAQLDRLRAAFGR
>gnl|CDD|444112 COG5319, COG5319, Uncharacterized conserved protein, DUF1178 domain [Function unknown]
MIVYDLKCDNGHRFEGWFRSSADFDDQQARGLVSCPVCGSTKVEKALMAPRVATSRKAAAAAAPAAAAAP
AAAALSAPAAELQAALRELRRHVEANSEDVGDRFAEEARKIHYGEAEERGIYGEATPEEAKALIEEGIEV
APLPVLPKEK
>gnl|CDD|444113 COG5321, COG5321, Uncharacterized conserved protein [Function unknown]
MSIAPPPVDGRQSETALAVARGVCRLLRALGFACLPELPLANGRRADLMALGPKGEIWIVEIKSSRADFR
ADRKWPDYLDWCDRFFFAVDPDFPRELLPEDTGLIVADGYGAEILREAPEHPLAPARRKALTLRFARAAA
RRLHALEDPGLAAGGRL
>gnl|CDD|444114 COG5322, COG5322, Predicted amino acid dehydrogenase [General function prediction only]
MMEKFAFIIHPLSLEDIARKFPFLKYLPDELVERALAYLPPFVVSHITGVRSPTGAEAEGWLIACPLTPE
QMLSLPPEFVYRKIIAAGKLAEKLGAQIVGLGAFTSVVGDAGITVAKRLNIPVTTGNSYTVATALEATKQ
AAERMGIDLKKATVAVVGATGSIGSVCARLLAREVKRLTLVARNLERLEELAEEILRNPGGKVTITTDID
EALREADIVVTVTSAVGAIIDPEDLKPGAVVCDVARPRDVSRRVAEKRPDVLVIEGGVVEVPGDVDFGFN
FGFPPGTAYACMAETMLLALEGRYENFSLGRNITVEKVEEIGRLAKKHGFKLAGLRSFERAVTDEEIERI
RELALEKRKAAG
>gnl|CDD|444115 COG5323, COG5323, Phage large terminase packaging protein [Mobilome: prophages, transposons]
MLKSGASATPETLEAFLAALSPAELAALPYDWEFWARPHQLPPEGDWRTWLILGGRGAGKTRAGAEWVRA
LAEGAGPARRIALVGETLDDVREVMVEGESGLLAVHPPDRRPVWEPSRRRLVWPNGAVAQLFSAEDPEAL
RGPQFDAAWADELAKWRKAEETWDMLQFGLRLGDRPRQVVTTTPRPVPLLKRLLADPSTVVTRAPTEANA
ANLAPSFLEEVRARYAGTRLGRQELDGELLEDVEGALWTRALIEAARVAEAPPLDRIVVAVDPPASSGKG
SDACGIVVAGLREDGRAYVLADASVRGASPAGWARAAVAAYRRHEADRVVAEVNQGGDMVESVLRQVDPS
VPVRLVRATRGKAARAEPVAALYEQGRVRHAGGFPALEDQMCDFTPGGLGGGGSPDRLDALVWALTELML
GPARRPRVRRL
>gnl|CDD|444116 COG5324, Trl1, tRNA splicing ligase [Translation, ribosomal structure and biogenesis]. tRNA splicing ligase is part of the Pathway/BioSystem: tRNA modification
TLISLLLREAYTLEADYFRRLTCIPELTQGGDDELLFQLGEETTEDGLREIEETSITATMLLDGTRGDFR
KINQKYDCVDAVNIFDVYVEELHQEEVIRKRNVPSVVFKKQIREHQKASRYRILTSDPEEGCIDRNSISI
EINLFKVGDINGITDEDDIILDAGGYQNVEEKIMHIEDKQMRVLFLGDRLVRGYELLDYLRRNDILNSGN
HIMLLGNVNLNLLTNLQEEKKPTSKETDKVLFAIITENEKKVIFISTTFLKRLKPFYLHQHTYFSAHDIK
YLDAGLTFKFNLKGGFSTIDQPGDTKQAYLTSAEYINGSVQEVRGEIDPVYKSYNLIGSEVSASHAGEVE
GGGLGIVTYEGDLAVLDTSAYNYSTIHASLEGEKEKIIKNLDEHYTKNELINEMIASKYVNVKKTEPNLY
SLNFTRKVFYKRLWNESTIKARGLFVDRETGEIVGRSYNKFFNYGERKETKLAYLRNTLTYPVTAYEKYN
GFLGIISVIDEELVFTSKSSTSGTHVDWFESLFHKLTEEHKASLKEYLKKNNVSLVFEVVSPERDPHIIP
YEKDHLYLLDIIENTLDYRKLHYDLCFSEKELAELKFKHRIITFEEEIPKKEDADEILKLLNEVRNSFSE
AEGYVIRDSNGFMVKVKLPYYSTWKFRRGILEPY
>gnl|CDD|227635 COG5325, COG5325, t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]
MEFFGIDAQSKGNSVRFTDEYKNQHRKEDDALTPTFILSAASVDQELTAVRRSISRLGKVYAKHTEPSFS
DKSEKEDEIDELSKKVNQDLQRCEKILKTKYKNLQSSFLQSKLLRDLNTECMEGQRIQQKSAQFRKYQVL
QAKFLRNKNNDQHPLEEEEDEESLSSLGSQQTLQQQGLSNEELEYQQILITERDEEIKNLARGIYELNEI
FRDLGSLVGEQGELVDRIDFNIENTSDNLKNANKELEKAPAHQRRTKKCRFYLLLILLVVLLFVSLIKKL
RSK
>gnl|CDD|444117 COG5328, COG5328, Uncharacterized conserved protein, UPF0262 family [Function unknown]
MSPPAAERDRLVAVTLDEASIGRRSPDVEHERAVAIFDLLEENSFAPPGGPEGPYRLHLSIQDNRLVFDI
RTEDGEPLATHHLSLTPFRRVVKDYFMICESYYDAIRTATPSQIEAIDMGRRGLHNEGAELLRERLEGKI
EVDFDTARRLFTLICVLHWRG
>gnl|CDD|227637 COG5329, COG5329, Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms]
MQCFLGEKPRSIAIVSNNYALSFRRLGVKNSERILCATELVGVRFEPDEGFSSLSSAHKIYGVIGLIKLK
GDIYLIVITGASLVGVIPGHSIYKILDVDFISLNNNKWDDELEEDEANYDKLSELKKLLSNGTFYFSYDF
DITNSLQKNLSEGLEASVDRADLIFMWNSFLLEEFINHRSKLSSLEKQFDNFLTTVIRGFAETVDIKVGG
NTISLTLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQYIFSFTQVRGSIPLFWEQSNLLYGP
KIKVTRSSEAAQSAFDKHFDKLREKYGDVYVVNLLKTKGYEAPLLELYEKHLDLSKKPKIHYTEFDFHKE
TSQDGFDDVKKLLYLIEQDLLEFGYFAYDINEGKSISEQDGVFRTNCLDCLDRTNVIQSLISRVLLEQFR
SEGVISDGYSPFLQIHRELWADNGDAISRLYTGTGALKSSFTRRGRRSFAGALNDFIKSFSRYYINNFTD
GQRQDAIDLLLGKFRPQEAFSYRPLRITFLLLMITACTISWFSTIIFISSLLCSNPSLLLVLAVILIVLS
KLYQFPHGRQ
>gnl|CDD|444118 COG5330, COG5330, Uncharacterized conserved protein, DUF2336 family [Function unknown]
MAAAALIVQDLLRLARDASAEARAELARALARLFLLAADLSDEERALADDVLTRLLDDAEPRVRAALAER
LAPSPNAPRDLIRALARDEIEVAGPVLERSPVLTDEDLVEIARSGSQEHLLAIARRPDLSEAVTDALVER
GDEEVVRALLANPGARLSEASLERLVERAGDDPALREALLARPDLPADVAERLVAKVSEALRARLLARAA
LDPERAARLAREARERATLALADGARDFEDARALVRHLRRAGRLTESLLLRALCSGRLAFFEAALAELAG
VPLERVRRLLADGGGEGLAALCKAAGLPRATFPAFLAALAAAREERVLTALAPADLEELLALLERLAVEA
A
>gnl|CDD|444119 COG5331, COG5331, Uncharacterized conserved protein [Function unknown]
MSQTAILLPVLALVALTFVVLLWMYARRIPAVKKGKVDPDDFALGESAAWPERVRQAANNYNNLFELPVL
FYALCLLLAVTGAVDGLALALAWLFVALRIVHSLIHVTSNRVMHRFALFALGSLVLLAMWIRLALALLLA
>gnl|CDD|227640 COG5333, CCL1, Cdk activating kinase (CAK)/RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH/TFIIK, cyclin H subunit [Cell division and chromosome partitioning / Transcription / DNA replication, recombination, and repair]
MANALESNLVSSRPLLSFDSSQNAIELDLLVLEPELTLEKELNLVIYYLKLIMDLCTRLNLPQTVLATAI
LFFSRFYLKNSVEEISLYSVVTTCVYLACKVEDTPRDISIESFEARDLWSEEPKSSRERILEYEFELLEA
LDFDLHVHHPYKYLEGFLKDLQEKDKYKLLQIAWKIINDALRTDLCLLYPPHIIALAALLIACEVLGMPI
IKLLDFVSYETKEEVIALNYKSIVKNKIKTFKAEHLSRDLPFTLQNIAEPQFALDKKPKSEEEADKIPDH
NKYLQPSSTITDKNNVQ
>gnl|CDD|444120 COG5336, AtpZ, FoF1-type ATP synthase AtpZ/Atp1/AtpQ subunit, putative Ca2+/Mg2+ transporter [Energy production and conversion]. FoF1-type ATP synthase AtpZ/Atp1/AtpQ subunit, putative Ca2+/Mg2+ transporter is part of the Pathway/BioSystem: FoF1-type ATP synthase
MSDEDEAAKNPKKKESLSALGLASRLGIELVAGILVGVGIGYLLDKWLGTSPWFLIIFLLLGFAAGFYNV
YRLAKKLQ
>gnl|CDD|444121 COG5337, CotH, Spore coat protein CotH [Cell wall/membrane/envelope biogenesis]
PGAADLFDQDVVPTVDITIDPEDWEALLADPTDDEYVPATLTIDGKTLYNVGIRLKGNSSLRFVWPKKSF
KIKFDKFVKGQRFYGLKKLNLNNNYSDPSLLREKLAYDLFRAMGVPAPRTAFVRLYINGEYEGLYLLVEQ
VDKSFLERRFGDDDGNLYKADGGADFSYLGDDPASYQDGFEKKTNEDEEDWADLIELLKALNQTPDAEFA
AELEKYLDVDSFLRYLAVNTLIGNWDGYGGMGHNYYLYRDPETGKFTFIPWDLDLAFGRFWDGLSLDPDG
NGLGGGLLEVGLLRPLLLLDVLGRLYLALLLLELEVALASALADLAVTLLALATEALAAALAEEALAALT
LLAFAAELIPAPSALQLSAQEGLAADKGGLAALGEDARTALLSA
>gnl|CDD|444122 COG5338, COG5338, Uncharacterized conserved protein [Function unknown]
RRRPVPERDPYEPLGIRLGSFTLRPSLELGLGYDDNIFATSTNEVSDAITTVSPGLRLRSDWSRHALTLD
ARGDYGRYFSSSDENYTDHNLGARGRLDLTRRTRLDLSAGYRLGHEDRGSPDAPGGASEPVEYDTLGASL
GVTRDFGRLRLTLGAGYDRTDYDDAELADGTTLDQSDRDRTEYTGGLRLGYELSPGTALFVEVRGNRRDY
DEAPDTGGYDRDSDGYRARVGVEFDLTGKLSGEVSVGYLERDFDDPRLEDISGPSWEASLTWSPTRLTTV
TLTASRSIEETTTAGASGILVTSVSLSVDHELRRNLILSAGAGYGRDDYQGTDRDDDTYSAGLGLTYLLN
RWLSLTGSYRYEDRDSSLAGRDYDRNRVGLGLRLQL
>gnl|CDD|444123 COG5339, YdgA, Uncharacterized conserved protein YdgA, DUF945 family [Function unknown]
MKKSLVAVGVVVALGAAWTGASWYTGKQIEQRLQEQVAQANAQLKAPLPGLKVSYQDYQRGWFSSTATYV
LQLDPGALANAPLGPGQSIVFNETIDHGPFPLAQLKKFNLIPAMASVHTELVNTEATKELFELTGGKSPL
TATTRIGYSGDTSSTLSLPPFDYTEDEVKVAFSGLTLTVDYDGDGKELSLTGSAPSLSVTLGQKESLTLK
GLTLDSDTKKGKFGLYLGDQKLTLKKLSISVAGKPAVSLKGLSLDSDSSEDGKLLNGQVDYSLGSLKVGG
QDLGSGKLALSLSNLDGKALQALSQAYNQLSQALLQQEALQQALLAALLANLPLLLKGNPELSIAPLSWK
NPKGESTFNLSLDLKDPASADLENPAALLKKLVKSLDAKLSLPKPMLTELAAQQAQLEGYSAEEAQKLAK
QQVDGLLAMGQMQGLLTVEGNNISSSLQYANGQVTLNGQKMPLPE
>gnl|CDD|444124 COG5340, AbiEi, Abortive phage infection protein AbiEi, antitoxin conponent of an AbiEi-AbiEii TA system [Defense mechanisms]
MRTQGRGVFTTADARAAGLSAGISRRLLSRLVKKGELERVRRGLYVLPPAEADKEHDELLIAARLVPPGY
ISLLSALALHGLTDQIPFTVYVAVPRRSRPIKIGGPPIRFVRFSKELFFEGVEEVKIDGGKVRVTSPERT
IVDCLRYRNKIGGIDEVLEALREYLRRKKLDLDKLLEYAERLRNSAVEKRLGYLLEALLIEGE
>gnl|CDD|444125 COG5341, COG5341, Uncharacterized conserved protein [Function unknown]
LMKKGDIILILLLLALSVLSFLVFWLAGNGGGGKVAVIRVDGKVVKEIPLDDVKEDRTIEVPGPLGTNII
EIKDGRVRVKEADCPDQICVKTGWISRPGETIVCLPNKVVIEIEGEDEDEIDAISY
>gnl|CDD|444126 COG5342, IalB, Invasion protein IalB, involved in pathogenesis [General function prediction only]
MSRLVALALAALLALAAAAAAAQEAAAPAAGPGAVKETFGDWTVRCDKPPGAAKEVCELVQNLVADDTGQ
PVLSVSLRRTPDGAKALLTVLVPLGVLLPPGLTLQVDGGKPVRLPFQTCLPDGCVAEVPLDDELLAALKK
GKTATVTIVNAAGQPVTIPVSLKGFTAALDALPKLPK
>gnl|CDD|444127 COG5343, RskA, Anti-sigma-K factor RskA [Signal transduction mechanisms]
MNTPEYDLDALAGEYVLGTLSGEERREFERRLASDPELAAEVAEWEERLAPLADAVEPVAPPPSLWARIE
ARLDAARAAAAAPAARLWRRLRFWRGLAAAAAAAALLLAVVLVWLLQPQLNPAPQQVPQLVAVLAADDGG
PAAVVVVDPSSGELVLTPLGLPAPPAGKSYQLWAIPDDGAPVSLGLLPPGGSTTLPLPAALAPLLAAGAA
LAVTLEPAGGSPTGLPTGPVLAVGRLVRL
>gnl|CDD|444128 COG5345, COG5345, Uncharacterized conserved protein, DUF2333 domain [Function unknown]
MLDPIVEFQAIKRGIGLLAAWLWPFDASRRGGIWRGLGLLVGLYLLIFWVLGWYWSFEPDYFDVYQVAEE
RAKAGEELVTGYTTTSTLIDVAETLLDKPGGYLSNDILPPGVFLDNMPNWEFGVLVQVRDLSRALRDDFS
RSQSQSTEDPDLQKAEPQFNFDNDSWYLPSTESEYRKGIKALRSYLARLADPNDCDAQFYARADNLRQWL
DRVEKRLGSLSQRLSASVGQYRLNTDLAGDPNAQSTPTPSEVVVKTPWFEIDDVFYEARGQLWALLHILK
AIEVDFADVLEKKNALVSLDQIIRELEATQEPIWSPMILNGSGFGLFANHSLVMANYISRANAALIDLRD
LLEQ
>gnl|CDD|444129 COG5346, COG5346, Uncharacterized membrane protein [Function unknown]
MNDNNIEEKQEAIVNDPLEDEEARIYQSRESFSGPLPPPEILEQYESILPGGAERILAMAEKEQNHRHEM
EKKALRGQISESKRGQWFGFLIGLLILGAGAFLAYLGHPTAAAAIGGTTVVGLVSAFVIGKKKSKDENEK
SE
>gnl|CDD|227651 COG5347, COG5347, GTPase-activating protein that regulates ARFs (ADP-ribosylation factors), involved in ARF-mediated vesicular transport [Intracellular trafficking and secretion]
MSTKSEDRKLLKLLKSDSSNKKCADCGAPNPTWASVNLGVFLCIDCAGVHRSLGVHISKVKSLTLDNWTE
EELRRMEVGGNSNANRFYEKNLLDQLLLPIKAKYDSSVAKKYIRKKYELKKFIDDSSSPSDFSSFSASST
RTVDSVDDRLDSESQSRSSSASLGNSNRPDDELNVESFQSTGSKPRSLTSTKSNKDNLLNSELLTLNSLL
SSNSEVGSGTKSRSDAQEKSSTKATESVKPGPVNTSSTSSLPPAIKRSPVQQLESFTTTPVYFPVNTPAT
FDATLKSYYSSLTANIAQNGFSPTNADLNDKAQQKKAWD
>gnl|CDD|444130 COG5349, COG5349, Uncharacterized conserved protein, DUF983 family [Function unknown]
MTPAPPERPLLSALLRGLRGRCPRCGEGKLFRGYLKVADRCPACGLDLSHARADDGPAYFVILIVGHLVV
PLALWVEVAYRPPLWVHLAIWLPLTLALSLALLRPLKGALVALQWANRAHGFRLDDDD
>gnl|CDD|444131 COG5350, COG5350, Predicted protein tyrosine phosphatase [General function prediction only]
MPMIHVCSLSELPETVARTGASHVLSLLDPGTPVPRPASIAAHRHLFLRFNDIIEPMPGLILPTEEHVEA
LLAFGRDWDREAPLLVHCHAGISRSTAAALIAAAALNPDRDEAELAQRLRAASPSATPNLRLVALADELL
GRDGRMVAAIRAIGRGAEAFEGEPF
>gnl|CDD|444132 COG5351, COG5351, Uncharacterized conserved protein, DUF2169 domain [Function unknown]
MELVNLTPFAAGLLVWRDRDGREVLVVVVKATFDLVPDGELRLAEEQEPLLLADEYWGEPGSSSLRYESD
LAPFKPRTDVLLVGHAYAPGGKPVTSLDVRLRVGDLDKTLRVFGDRVWRRGGGGWALSEPEPFTRMPLRY
ERAFGGPDRSDPGEPRNPVGVGFAARPDALGGRPLPNLEDPGAPITSPGDRPEPAGFGPIAPHWPPRRRL
AGTYDEAWLEERAPLLPDDFDWRFFNAAPPDQQLPGYLRGDERVVLENLHPEHGRLRFRLPGLRPRAFVR
RRGGRPEELPLRLDTLWIDPDRGRVTLVWRGSLPLPRDALEVRRVVVGVELPAPRAWARYAG
>gnl|CDD|444133 COG5352, COG5352, Uncharacterized conserved protein [Function unknown]
MSWTDERVELLKKLWSEGLSASQIAAELGGVTRNAVIGKVHRLGLSGRASPARPAAAPRAAKPRAPPAAP
AAPAAPAPTRSAGATAVAPAPAPAAAPAGAPAPVAEVVVPIAERLTLLELTERTCRWPIGDPGTPDFHFC
GAPVVPGKPYCAAHARIAYQPARDRRRRRAV
>gnl|CDD|444134 COG5353, YpmB, Uncharacterized conserved protein YpmB, contains C-terminal PepSY domain [Function unknown]
MKKWILFILIIILLLLLIISILVYQVANSPKRQAEEEAVEIAKEKTGLTSVDSVYWYNGKETYYVVTGKN
KKGKEIYVWVPKKKKKVTVLKASDGISEQQAIKIVQKECPPKEILHIKLGLEKGGPVWEVTYLDQNGRLN
YVYVDFEDGEWLKRISNL
>gnl|CDD|227657 COG5354, COG5354, Uncharacterized protein, contains Trp-Asp (WD) repeat [General function prediction only]
MKSQFPLDYSAVISVFWNSQSEVIHTRFESENWPVAYVSESPLGTYLFSEHAAGVECWGGPSKAKLVRFR
HPDVKYLDFSPNEKYLVTWSREPIIEPEIEISPFTSKNNVFVWDIASGMIVFSFNGISQPYLGWPVLKFS
IDDKYVARVVGSSLYIHEITDNIEEHPFKNLRPVGILDFSISPEGNHDELAYWTPEKLNKPAMVRILSIP
KNSVLVTKNLFKVSGVQLKWQVLGKYLLVLVMTHTKSNKSYFGESNLYLLRITERSIPVEKDLKDPVHDF
TWEPLSSRFAVISGYMPASVSVFDLRGNLRFYFPEQKRNTIFFSPHERYILFAGFDNLQGNIEIFDPAGR
FKVAGAFNGLNTSYCDWSPDGQFYDTDTTSEKLRVDNSIKLWDVYGAKVFELTNITWDPSGQYVTTSSSC
PKHKVEHGYKIFKIAGALYPEEARGGFKNFAWRPEPPSKLTIESAKKYVKPSRHRFVPFEKAVIMEADSA
NRSSAPRKKELVEQWPEYSDEDKIRSLLKKLRAIEALKERMRSGEELEVIQVNKIETEEEVLSELKELVE
D
>gnl|CDD|444135 COG5360, COG5360, Uncharacterized conserved protein, heparinase superfamily [General function prediction only]
MSRLAGLLAARLLRRARRRLVRGPLYRWRLRGRAPDRLLIAPEDLRPGDPARGREIYAGRFLFAGKLVEA
PGRSPFDLPPPSPAWAAELHGFGWLRDLRAAGTDLARANARALVLDWIARFGRGDGPAWEPEVTARRLIN
WLSHAPLLLAGADEAFRRRFLRSLARQARFLRRRLEGAPDGNPRLEAAIALVYAGLSLPGGERWLRRALR
ALARELDRQILPDGGHVSRSPEALLELLLDLLPLRQALAARGREPPPALLAAIDRMAPALRFLRHGDGGL
ALFNGGGAGPADRLAALLAYDDARGRPLRSAPHSGYQRLAAGRTVLIVDAGPPPPGALSGHAHAGTLSFE
LSSGRQRLIVNCGVGPYAGGEWRQAARATAAHSTLTLDDTSSSRFLGGGRLGRRLGLLGGPSPVEVERRE
EDGGTRLEASHDGYARRFGLTHERRLTLSADGRELRGEDRLEAAGGRRRGGIPFAIRFHLHPDVEASLDR
DGAAVLLRLPSGEIWRFRADGGELSLEESVYLAAGGGPRRTQQIVLSGRAGEGGTRVRWSLSRAGAA
>gnl|CDD|444136 COG5361, COG5361, Uncharacterized conserved protein [Mobilome: prophages, transposons]
KKRLLLLALLALLAIAAPDTVETPTAATAEKLYDELAFAIAVEAYLYGYPLVSMYATRRGYTNVGGPPGK
APFNQFVHARRLPDPDDRLVVTPNSDTLYSSAWLDLSAGPVVLEVPDTGGRYYLGQLLDAWTNVFADVGS
RTTGGKGGKYLIVGPGWKGELPAGYFVIRSPTNFVWLIGRTQLNGPGDLAAVHAIQDGYKLYPLSAYGGP
PAPPAAKFKSIDTIPPDDLAFFEYLNALLQDNPPHAADPELLGRLAAIGIGPGKPFDPDALSPEMKAALE
EAAADALAMIRAAFASLGRPDNGWSNPLFGGRGRYGTDYLYRATVASPGLGANPGEEAVYPLAYVDADGN
PLDGAKTYKLHFPAGQLPPVKAFWSVTLYDDQTRFLVDNPINRYSIGSRTDGLKKNADGSLDLYIQPEAP
GGDKESNWLPAPGGPFFLILRLYGPKEEALDGTWKPPDVEKVK
>gnl|CDD|444137 COG5362, COG5362, Phage terminase large subunit [Mobilome: prophages, transposons]
SRRMDAVAALRLAALAARFRASALAVGRFALFPLPNALEALLAARLGLKLRLLLLIVIGRLPRVAIAVLS
SSISVPAALVAWLLLRLGRRIIASALAKSLAADLASGKALRLRRSISRQKLSKGTKELRRDTTTDGRAEG
SAGGGGGAGGGGGGGGDDIDIIDDDDDDDKRAAASRAESADLWLLRRESIISRILAALVPTRIVVDLLVI
RLLDDLLLLLLLLILLELRLDLIAEAEGRRRLRRLGGIPLRDKEGEELLPLLLRELELRRATQAQYQQAA
QQQGQPAGGGLFKREWFRRYDELPADFDRIVQSWDTAAKTGETNDYSVGTTWGGRDGRYYLLDVVRGRLE
YPELKRAIKALAKRWGPIAILIEDKASGKALIQELRRELAGLPVIAVKPKGDKLTRASAVSAQIEAGNVL
LPKDAPWLDDFLDELLAFPNGAHDDQVDALSQALNELLGSRGRVLSDRGTGL
>gnl|CDD|227661 COG5366, COG5366, Protein involved in propagation of M2 dsRNA satellite of L-A virus [General function prediction only]
MPIRGLEEVRAHPGQNFFTLVPQKAFKKMRILIDGNWFYLDYVDVSSICRGLVFGMELVIFEPLLKLPEF
KDENGVTMIWLWDGIGFNKLQGTSSGGLGTLLTSGFKEYTQENYRKAGKLWRNFIMQKSEMDVASKILEE
KGVAVIIAPYSATFQCAYLMSAETCSYAFGPSDILLLDGVDRIILDMSFGSDKPPLDVFHVPRFLEMFLL
SSRLFYALGLLLGCDFCSTIPRCATDADFSLNQVIGDMKGQELFSKAIRGTCEYEGSRKKYTLEFLRSLG
LVTYLLVMGVSGSYHAYSEESVPGNLNKILGLKLAPGFDPYLFNNKRSGDVYQANGPTPGNDRDSKPIKL
VEAARSRNDGGARKKKFSKDTKNEPGSVPPFVNLISPAMVLTKDIDPSLGVLLFMTIELRWGETPLKMKE
LCLHRQTGTPERLKISDATLKYYVGISRLFNLIKEVKELYEVTMNKSLDGLFCEAPTLFSANLHELFGFS
LSSGESNRRFLKSARDFLRANEKLSPIIPYIVEEIEVTLKK
>gnl|CDD|444138 COG5368, COG5368, Endo-beta-1,2-glucanase, glucoamylase superfamily [Carbohydrate transport and metabolism]
MKLLALALLLAACPAAPAKAPTLSDDALLDLVQRQTFRYFWEGANPVSGLARDRSPSDDGDVASIAGTGF
GLMAIIVGVERGWITREEAVERTLKTLRFLENKADRFHGFFYHFLDGETGKRAWDDEGSLVDTAFLLQGL
LTAREYFDGGNAAEKEIRELADALYERVDWDWYTNGQNVLYWGWSPEYGFMNHPWDGYNEALILYVLAAG
SPTHPIPAEVYEGWARTGAINGGTYYGIPLILGYGGPLFFHQYSHLWLDPRGLRDRYADYFENSRNATLI
NRAYCIDNPKGFKGYGEDCWGLTASDGPGGYAAHGPPYGNDDGTIAPTAALSSLPFTPEESMPALRHFYE
RYGDKLWGRYGFYDAFNPTENWVAPDYLGIDQGPIVLMIENYRSGLLWKLFMSNPEIQRGLKKLGFTGGW
LD
>gnl|CDD|227663 COG5369, COG5369, Uncharacterized conserved protein [Function unknown]
MLIGRSIRLKEGVRNSTMNDQHGASAFHDDPIFQGVIDCSQRDEQALFNKSLRLLITLNELEKRDITGTY
YFLLVETGFTSERDFNGFAEENCMSLELLALLSGTSRCQNTPEGVRNCIIQLKEFIKSQSLDPSSIHISM
LRSFRIIISESDTDQASFYEKYVTSHLAFFLSVIEIEHQSLCLNSKKNDVIELLYRMLETDTRPVKARLR
SRRVFKNDCNPDIQIINLLNELLDEYLGKHVKIGRIRKRRDDSNGVKNKLDVLSCCVKLYFMSHSEDKVR
IFERWIFYPLLDELIQYRKESTPMNNPVLVLLGIFCVQDDVQACLSLPQLFEKDIELTSKIIDRFHESKE
SERLLLLTPELLFNMYELTAGLEENQRFIAARSKMIESVTGTFKTKVNRKQDDLDFVAIVLFLKSMSRSV
TFLRTGLLDYPIVELLIDALSNPEIMIEFPDTIDICNKVVPFSNLGAGFLEKSIIDVLVNLVMSKDDALQ
ANSEWVLRHLMYNCQKNEKFKFLAKIGVEKVLSYTNDPCFKVQHQVLQILRNFTCDTSKNEKSKDVFIKA
TPRRYLFKRLIDKYEENNPMEILEGCYILVRNAACDDTLDYIVQSQEDMLDSIFEILDEFAGRTPLSPGS
KEEHVLLPISYTIVNLSENSDKFKRLVLTTPHLDNMKKDSTTRNDELSIAGIWIIINLSWKEDGSEVTRA
TVERIQILCANGIREWLVKIQAKDSLIVREKIGTALENLRLAL
>gnl|CDD|444139 COG5371, GDA1, Nucleoside diphosphatase, GDA1/CD39 family [Nucleotide transport and metabolism]
MFRKLVFLCILCFLALSAASTTCAKHQCIAVIDAGSSGSRLHIYQYDLDKSNTPIAIEEGWNKKAKPGLP
TIEANKATIDAYLTKLLSDAPDGNVPVYFYATAGMRLLPQDQQKAIYQLLRTWFRQQSQWQLVGARTISG
REEGLFAWLAVNYKLATLNLEAHTLVGVMDMGGASVQIAFPVTTCSNIDDNNITQINLYGKLLPFYSHSF
LGLGQDCFAKVYALP
>gnl|CDD|444140 COG5373, COG5373, Uncharacterized membrane protein [Function unknown]
MELLLILIGLLVLALLVGLLGRVARLRRRVEELEAELAEAAEAASAPAEPEPEAAAAATAAAPEAAPAPV
PEAPAAPPAAAEAPAPAAAAPPAEAEPAAAPAAASSFEEWLGGNWLVWIGGLSLALGGAFLVKYSIEQGL
LGPELRLALGALFGLALLALGERLRRRADGRALYPLALQGGGIGTLYATVFAAYRLYGLIGPGTAFVLLA
LVSLATVALALLQGPLLAALGLLGGYAAPLLVSTGSGNHVALFSYYLLLNAGILALARFRRWRWLNLLGF
AGTFGWGLLWGVLLYRPELFLSTELFLIAFFLLFLAIALLFALRHPGPLRGPVDGTLLFGTPLVAFALQL
ALVADSGYGLALSALALALLYLALALLLRRRRPALLALAFLALGVAFATLAIPLALSARWTAALWALEGL
GLLWLGLRQWRLLLRWWALLLQLAPLAALLAAYWPVANLAGSYLWALLALALAALFAALALRLARRRSAG
LRLWGAAWWALAALAAIALALTLLLEEAALTLALALLVLSLAWLARRLDWPLLRWLAALLLPLVLLRLLW
DPGLVGGPLAGFNWLLWGYGGPLLALAAAAWLLRRRRLRRWLEAAALWLLVLLLALELRYLLWGGDLFAS
EWSLAEAGLLALLWLALALALLRRWLRRAGRVYRLAALALGPLAALSYLLLLLLLLNPLWSGAPVGYLPL
LNPLLLAYLLPALLLALWARLLLLAPRLRRAAAGLAGLLGFLWLNLEIRRLWHGGDLALWLGVSDLEQYS
YSIVWLLLALALLLLGIRRGSRALRLAGAALLGLVVAKLFLVDMAGLGGLLRILSFIGLGLLLLGIGYLY
PRPPRRAEAEAAES
>gnl|CDD|227666 COG5374, COG5374, Uncharacterized conserved protein [Function unknown]
MGIYYTLVFSLLVVEMVMFFILVLPLPKRLRRSLMKLYSTSKVYRGFKHILKITFIFILLLFIDSWKRVY
RVSKEANLYSASINNYAVTRIAVLASRFYAQRNMYLSGSALFLSIVVMRVMSIVEEMLEENAKKGGKIDK
MEADSTDLKARLRKAQILLEGLQKNQEELFKLLDKYNELREQVQKESSKKKE
>gnl|CDD|444141 COG5375, COG5375, Uncharacterized conserved protein [Function unknown]
MTATAAARRAAAARARRRRAFRAARRHSRRVRWLKIALPLAALALLATLFLWPLIRPLRPEVSLPLSLGN
VEIEGERLRMENPRYSGVDKDGRPYSLTADSAVQDITNPDLVELEDIRARITLPDGGWATLTAATGVYDS
KTQTLDLTGDVRITTSDGYEARTESADVDLKTGTVTSDGPVEGTGPGGTITADGMEVDDNGRVIVFTGGV
RLVLDPGALGAPPA
>gnl|CDD|444142 COG5377, COG5377, Phage-related protein, predicted endonuclease [Mobilome: prophages, transposons]
MKLVNTKDLSQSREEWLALRRKGIGASDAAAILGLSPYKSPLDLWLEKTGGLPPDLEENEAMYWGNLLEP
VVAREFEKRTGLKVRRVNAILQHPEYPFMLANLDRLVVGENGVLEIKTASAYLADEWGEDEVPDYYLCQV
QHQLAVTGASWAYVAVLIGGNEFRWFRIERDEELIEELIEAEKDFWEHVEKGVPPPPDGSDDAEEALKAL
YPEDDGSSIDLLDEELAELIEELEELKAEIKELEERKKALENQLKAAMGDAETALFGGGRVTWKTKRRGR
VDSKKLKKEQPEIYEKYTKTSSSRRFRIKEPKK
>gnl|CDD|444143 COG5378, COG5378, Predicted nucleic acid-binding protein, contains PIN domain [General function prediction only]
MMKLVVDANILFSALLGGKSRIRRLLLNLELELYTPEYALDELEKHLEKIAKKSGLSEDELAQALDLLLS
RINIVPEEIYNDYLEEAYELIPDRDPDDTPFVALALALDAPIWTGDKDLFGGLGFVKTWTTDELLRLLDG
L
>gnl|CDD|444144 COG5379, BtaA, S-adenosylmethionine:diacylglycerol 3-amino-3-carboxypropyl transferase [Lipid transport and metabolism]
MVHQNSALSKDGLSERLFKALFSGLVYNQIWEDPDVDLAALQLTPGDRVLSIASAGCNALAYLTADPARI
TAVDLNPAQNALLELKLAAIRHLDHEEFLRFFGRGDSPRNLELYRRKLRPHLDPDARAYWDGRDSLFRRG
FYRHGLLGRFIGLFHLYAPLRLLGKDIRELLAARSLEEQRRFFDERLAPLFWRRLVRWLFSRPASLFGLG
IPPAQYDYLEGEYDGGVAGVLRERLERLACDFPLSENYFAWQALTGRYTPGALPPYLRPENFETIRARAD
RVEIHTASLTEFLAESPAASIDRYVLLDAQDWMSDEQLNALWQEILRTARPGARVIFRTAAEPRLLPGRV
PPALLDRWTYLEELSEELHARDRSFIYGGFHLYEVKA
>gnl|CDD|444145 COG5380, LimK, Lipase chaperone LimK [Posttranslational modification, protein turnover, chaperones]
MMLAVLLIAAAAALWLAAAAPVQAASTGPSLPPSLAGTDVDGALKVDANGNLILDREVRDLFDYFLSALG
EESLAAIRARIQAYIRRQLPEPAAAQALALLDRYLAYKEALAELEAQAGPASADLEDLRQRLEELQALRR
QYLGPDEADAFFGDEEAYDDYTLARLEILQDPALSAEEKAAQLAALEAQLPEEVREARQAALRLAELAAQ
EAELRAQGASAAELRQLRAALVGPEAADRLAALDQQRAQWQQRLDAYLAERAQILDSGLSPADRQAALEQ
LRQQHFSPQERLRVEALERIARAA
>gnl|CDD|444146 COG5381, COG5381, Uncharacterized conserved protein [Function unknown]
MTQIFGDFIEDLPPSQEYLELTFSPSSLPLKQRWRNNGLSADFIADYFATFFPGDEDDPSTEDRRAEIKG
AVSYIANELLENAMKFNDEGSDYPITIELHLESDRFIFFVTNSIDPQTAEKFQAFIKELLSSDPEELYIQ
QLEKNAEDENSSGSGLGLLTMINDYGAKLGWKFEPVEEDPDVVTVTTMVQLAV
>gnl|CDD|444147 COG5383, YdcJ, Uncharacterized metalloenzyme YdcJ, glyoxalase superfamily [General function prediction only]
PDELRTSFKALEEVPAFGEADGELLAGSHTARFGEIEQRGHAATRKGRALYDALLARVFAVMGMAPVGYY
DAAAYVAGLPVHFTAFPDDWAELRRNPLRYFTYLLRLKGELIEDAALRLIAAGILRARPIFYEDFLPVSA
AGIFQSNLGDDEARHSAATVDQATFEAHLGPRVLDIDALYARMEERSIEAKAAILR
>gnl|CDD|227674 COG5384, Mpp10, U3 small nucleolar ribonucleoprotein component [Translation, ribosomal structure and biogenesis]
MSELFGVLKSILKDPTSKDVKAYIDSVINTCKNGSITKKAELDEITVDGLDANQVWWQVKLVLDSIDGDL
IQGIQELKDPSLDGSTLNSSSGEESELEEAESVFKEKQMLSADVSEIEEQSNDSLSENDEEPSMDDEKTS
AEAAREEFAEEKRIPDPYGINDKFFDLEKFNRDTLAAEDSNEASEGSEDEDIDYFQDMPSDDEEEEAIYY
EDFFDKPTKEPVKKHSDVKDPKEDEELDEEEHDSAMDKVKLDLFADEEDEPNAEGVGEASDKNLSSFEKQ
QIEMDEQIEELEKELVAPKEWKYAGEVSAKKRPKNSLLAEELEFKQGAKPVPVSTKEDTESLEDIILQRI
REGTFDDHAYRIREEVTIADEIPEFELLESKSILSLAEEYEGDLMQIVDESALSEELDKGHNEIFVLDSE
IRMVLDTLKSLHSVPKPGAKSLEIIKNVPTLKMEDAQPLYMSNASSLAPQEIYNVGKAEKDGEIRLKNGV
AMSKEELTREDKNRLRRALKRKRSKANLPNVNKRSKRNDVVDTLSKANITVINQKGEKKDVSGKTKKSRS
GPDSTNIKL
>gnl|CDD|444148 COG5385, HPt, Histidine phosphotransfer protein ChpT, HPt domain [Signal transduction mechanisms]
ALDLAALLCSRLCHDLISPVGAINNGLELLEDEGDAMREPALDLIRESARNASARLQFFRLAFGAAGSGQ
QIDLGEAEKVLEGLFAGGKIKLDWQVPRDLLPKNEVKLLLNLLLIAETALPRGGTITVTAEGGGDAGGLR
ITATGPRARLPPELWAALAGEAPEDELDPRNVQAYYTGLLAREAGRTLSLEAEEDEVVLTAT
>gnl|CDD|444149 COG5386, NEAT, Heme-binding NEAT domain [Inorganic ion transport and metabolism]
MKKVFDGMLSVLLAALLSVTFASVDVTEPTTAAATLADGTYSINFKVLKDGTDEASMMNQYFEKPAKLTV
KNGKYYVTMTLNDSSWVTSFKVEVNGSFVDATVVSEDKAANTRVVEFEVPDLSKPLNAKVHVVIPAINYD
HKYDVRLVFDTNSIKPVGPVKEEPAPPPENTTDPEKLEDGTYTIDFKVLKDGTKEISMMDQTRTVEFKNP
KPSDNVTSTAANSGSLQAKEGIKSQPTKSDSTSKPATTTKPKKKVVPIAVNSLKLGLKFSNTVNKKQILN
KLTEGGVVAEATQELAVSIEVK
>gnl|CDD|444150 COG5387, Atp12, Mitochondrial FoF1-type ATP synthase assembly chaperone ATP12 [Posttranslational modification, protein turnover, chaperones]
SEWLPKRFYKEATVAEAEGGFAVLLDGRPVRTPAKAPLVVPTRALAEAIAAEWAAQGEEIDPATMPLTRL
ANTAIDRVAPQRAAVADELAAYAGSDLLCYRADSPEELVARQAAAWDPLLDWAAERLGARLVLTEGVMHV
PQPPEALAALRAALEALDPFRLAALHDLTTLTGSLVLALALAEGRLDAEEAWAAAHLDEDWQIEQWGEDE
EAAARRAARRAEFLAAARFLDLLRA
>gnl|CDD|444151 COG5388, COG5388, Uncharacterized conserved protein [Function unknown]
MSSLTDFRAAMRHPALRALFAYWNRLRGGRSAPDRSDIDPAAIRRLLPDLFILERDAPGDYRFRLAGTRL
CELFGRELTGRPLSELWAPEDRARLADALEAVFEDPAPVVLTLEAETGDGEELEFELLLLPLRSDGGEVD
RILGALAPLGARPIRRLRLSSLRLIAPDRA
>gnl|CDD|444152 COG5389, COG5389, Uncharacterized conserved protein, DUF721 domain [Function unknown]
MARRRRRRRGFRPLSDLVPGVIRPALRKRGFASSRLLTHWPEIVGEDLARITRPEKISWPRGRGEGATLT
LRVEGAAALELQHQSPQIIERVNAFFGYRAVARIRIVQGPVTGAEGRPKRPPPPLDPAEEAELAASLAGI
EDPELRAALERLGRAVLSRRKRR
>gnl|CDD|227680 COG5391, COG5391, Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only]
NSPDASSSPKNESSASDSGPSGSSSESQESSTVKNNDGSPVNSSIKSTPLDIQKRYSGFESSAKLPRISD
APSFVPPPGGHTISYTIAIHDSKIHSRASEFRSLRDMLSLLLPTSLQPPLSTSHTILDYFISSTVSNPQS
LTLLVDSRDKHTSYEIITVTNLPSFQLRESRPLVVRRRYSDFESLHSILIKLLPLCAIPPLPSKKSNSEY
YGDRFSDEFIEERRQSLQNFLRRVSTHPLLSNYKNSKSWESHSTLLSSFIENRKSVPTPLSLDLTSTTQE
LDMERKELNESTSKAIHNILSIFSLFEKILIQLESEEESLTRLLESLNNLLLLVLNFSGVFAKRLEQNQN
SILNEGVVQAETLRSSLKELLTQLQDEIKSRESLILTDSNLEKLTDQNLEDVEELSRSLRKNSSQRAVVS
QQPEGLTSFSKLSYKLRDFVQEKSRSKSIESLQQDKEKLEEQLAIAEKDAQEINEELKNELKFFFSVRNS
DLEKILKSVADSHIEWAEENLEIWKSVKEQLDRL
>gnl|CDD|444153 COG5393, YqjE, Uncharacterized membrane protein YqjE [Function unknown]
MADGTQGPSPGLLASLRRLAATLLGLLETRLELAAVELEEEKARLIQLLLLAGLALLFLLFGLVFLSVLL
VVLFWDTYRLLALGILTALFLLLALILALWARRKLRRRPTLFSATLAELAKDREALKPRH
>gnl|CDD|444154 COG5394, COG5394, Polyhydroxyalkanoate (PHA) synthesis regulator protein, binds DNA and PHA [Secondary metabolites biosynthesis, transport and catabolism, Signal transduction mechanisms]
MAAMDEPRVIKKYPNRRLYDTETSSYVTLEDVAQLVKDGEEFQVVDAKTGEDLTRSILLQIILEEESKGQ
PLLSIDFLRQLIRFYGDSMQGFVPSYLEKSLQAFADQQEKMREQMQGLMGQSPAMQGMEEYAEQNMALFE
QMQEQFSPFAGPEAASADDLDELKKQLAELQKKLSKLGKKP
>gnl|CDD|444155 COG5395, COG5395, Uncharacterized membrane protein [Function unknown]
MSLAPLAAAPPAIQIHLAAALPALLLGPVQLLRRKGTRLHRLLGRIWVALMLVTALSSFFIRTIRLPGGF
SPIHLLSVLTLVGLPLAVWAARRGNIAAHRRAMIGLYIGALLIAGFFTFLPGRLLGQLLFGDA
>gnl|CDD|444156 COG5397, COG5397, Uncharacterized conserved protein [Function unknown]
MMMKELSLAAQTAYADLLQALRDAALFNLRGSFVWKTVKGRVYWYRRYRIRGGERRRRYLGPDSPETRAR
IERFKALKADAEARRKERARLVRLLRAAGLGRTDRQTGSVLEALAAAGLFRLGGTLVGTHAFRAYEGELG
VRLPADAAATGDIDIAQFERLSLALGDVVEPPLLDVLRSVDPGFEPVPHLSDGRVWRWAQNRSGYLVEFL
TPNRGSDDEEPVPLPALGVSAQALRFLDYLLADPIRAVALYRSGVLVQVPDPERFAVHKLIVADRRGRDP
AKARKDRAQAAFLIEALAERRPDDLAEAYEEALSRGPKWRERIRASLSRLPETV
>gnl|CDD|444157 COG5398, COG5398, Heme oxygenase [Coenzyme transport and metabolism]
SPLSTALREGTAKAHTAAENSGFMKALLKGRLDRDAYVALLAQLYFVYSALEEALERHRDHPVVGPFYFP
ELNRLPALEADLAFLYGPDWRDQITPLPATRAYVARIREVAAEWPELLVAHHYTRYLGDLSGGQIIKRIL
QRAYGLPDGEGTAFYEFDEIPDPKAFKDRYRAALDALPLDEAERERIVDEANLAFRLNTAVFAELERDLP
A
>gnl|CDD|444158 COG5399, COG5399, Uncharacterized conserved protein, DUF2286 domain [Function unknown]
MKILVIKSEEGKVTSKEIVEGDLTEVVKNVAKKALNEWNPEKSDFIILRDSQELRLKLPLKPELYDKIKN
YNLRREGDEAIAEIPVYIISFDNRWIEEDYKDKKVYVVSPYIDDEIKKELEEYAIETTSEEKEEEGEEEE
LEEELE
>gnl|CDD|444159 COG5400, COG5400, Uncharacterized conserved protein [Function unknown]
MSMMRRLLAALALAAAALLAAAAPAAAQDAEPGPPAAAGAPSDTYSQDEIVDAGHGFFGSTSEGLAKVVE
KAFKDYGRPNGYILGEEASGAFVVGLRYGEGTLYTKNAGDHKVYWQGPSLGFDFGGNGSRVMMLVYNLPD
VEDLYQRFPGVEGSAYLVGGVGMTYLRAGDVVLVPIRTGVGLRLGANVGYLKFTRKPTWNPF
>gnl|CDD|444160 COG5401, GerM, Spore germination protein GerM [Cell cycle control, cell division, chromosome partitioning]
MRRLLLAGCGVAWEATPSVSPPSSPETAQPQTSATETVTVTLYFLDEDGGYLVPETREVPKSDEEVAKAA
LEELLAGPTEENGLSSTIPEGTKLLSVKVKDGTAYVDLSKEFTEGGGSTGEQLRLYQIVNTLTEFPGVKK
VQILVEGKPLEVLGGGLDLSQPL
>gnl|CDD|444161 COG5402, COG5402, Uncharacterized protein, contains DUF1214 domain [Function unknown]
MFRLLLLLLLALALALGLGLGSAWYALDRGLGFGSVRIGPWTAWPRAGTADADPYARARVARSGLLPLGR
AEGLYFTARTDSAGRPLDGRCTYRISGGTPPARFWTLTAYDADGRLIPNPAGRYSFTSAEVLRNSDGSFV
ITVSPRARPGNWLPTGGGGRFVLVLRLYDTPVATSSGLDDLPLPTITREGCR
>gnl|CDD|444162 COG5403, COG5403, Uncharacterized conserved protein, DUF937 domain [Function unknown]
MMNLLDLLNSALGGQAISNLAQQLGLSPEQTQSAVSAALPALLGGLQRNASSPEGAASLLGALSSGHDGS
ILDDLGGLAGGSPEAVADGNGILGHIFGSKQRAVANQLAQATGLDPGSVKQLLPVLAPLVMGGLGKQKQQ
QGLDAGGLGDLLGSLLGGASQAGGLDGDGSLDDMFGGGGLLGGL
>gnl|CDD|444163 COG5404, SulA, Cell division inhibitor SulA, prevents FtsZ ring assembly [Cell cycle control, cell division, chromosome partitioning]
MRTASSRAQLSLFTASPSLDAQLPSGGWPNGLVSELVYSEDGPLQLQLLLPLLQQLSQQSRWLLWLAPPQ
KLSRSWLQSAGLPLSKVLQLHPKSPENTLEAMEKALRSGNSSAVVAWLPELSEEDRQRLQQAAQRGNALG
FIMRPRRAQKPA
>gnl|CDD|444164 COG5405, HslV, ATP-dependent protease HslVU (ClpYQ), peptidase subunit [Posttranslational modification, protein turnover, chaperones]
FHGTTILAVRKGGKVAIAGDGQVTLGNTVMKHNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEY
SGNLTRAAVELAKDWRTDRYLRRLEAMLIVADKEHILLISGNGDVIEPDDGIAAIGSGGNYALAAARALL
DHTDLDAEEIAREALEIAADICIYTNHNITVEEL
>gnl|CDD|227693 COG5406, COG5406, Nucleosome binding factor SPN, SPT16 subunit [Transcription / DNA replication, recombination, and repair / Chromatin structure and dynamics]
MPEIRIDEERFEKRSRDLRKHLNEEDGGPDSLLVMLGKSQDVNPYQKNTALHIWLLGYEFPETLIILDDV
CTAITTSKKKAILLQKGLAETSLNIVVRNKDNRTKNMEENKKLFKGSIYVIGSENKIVGDFCKDVLQGKF
INEWDSIFEPVKSEFNASDVSLGLSKMFLTKDAEEIANCRASSAASSVLMRYFVKEMEMLWDGAFKITHG
KLSDLMESLIDDVEFFQTKSLKLGDIDLDQLEWCYTPIIQSGGSIDLTPSAFSFPMELTGDVVLLSIGIR
YNGYCSNMSRTILTDPDSEQQKNYEFLYMLQKYILGLVRPGTDSGIIYSEAEKYISSNGPELGPNFIYNV
GLMIGIEFRSSQKPFNVKNGRVLQAGCIFNISLGFGNLINPHPKNNYALLLIDTEQISLSNPIVFTDSPK
AQGDISFLFGEDDETPEYLTLQDKAPDFLDKTISSHRSKFRDETREHELNARKKRVEHQKELLDKIIEEG
LERFRNASDAGPDSIEEKSEKRIESYSRDSQLPRQIGELRIIVDFARQSIILPIGGRPVPFHISSIKNAS
KNDEGNFVYLRLNFKSPGKGGGKTEELPCEQRGEQFLRSITSRSIRGNRMSDLFKEINDLKKGATKRETE
RKEDADVLEQDKLIERKLSRTDVYMKTDVRPGSDGKRKPGNLEIHENGIRFQSPLRSDSHIDILFSNIKH
LFFQECNGELIVIIHFHLKSPILTGKRKVQDVQFYREASDTMVDETGKRGRKEHYGDEDELEQEQEERRR
RAALDQEFKSFASSIAEASEGRIEFKVQFRKLGFYGVPFRSSVMIKPTTDCLVQLDEAPFFVITLEEVEI
VNLERVQFGLKNFDVVFILRDFYRPLVHINTVPVESLDKLKEWLDSNDILFMETSANLNWNTIMKSIMKD
PISFFEDGGWSFLMVGSDDESDESEEEVSEYEASSDDESDETDEDEESDESSEDLSEDESENDSSDEEDG
EDWDELESKAAYDSRPGKRRK
>gnl|CDD|444165 COG5407, SEC63, Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport]
DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRAR
>gnl|CDD|227695 COG5408, COG5408, SPX domain-containing protein [Signal transduction mechanisms]
MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSLQKDQLSSYHGVSDNDETRDEAGEPSNWRDRFNHALKKE
LSPLQANYVAKFFENYISEEAIKLDEFYSQGQYIAYKKREFRKISSKFFYSERKALVQKEENTASSNYDT
FLNLQTDEGAYVADARKRAEAKSYDPFDSLRIDTSKEGLTKRNLNLPDYEKIVSGTDEEVPSNDQDDEDQ
DFDYLAKKNDNTALLDLSQFNFKIVKYQKRSLLKKRIIELYIQLHQLKSFIELNYTGFSKITKKYDKTLH
QNLRHEYMSRSVNEYY
>gnl|CDD|227696 COG5409, COG5409, EXS domain-containing protein [Signal transduction mechanisms]
DLEVVGLEKGVSLSLGLYIQNLLNVGEPQSFIVLILLALWGGWILVFFLAFLFDVSCYILTRTPINYRFI
FLFEQLSSTARNFNLDFHRIIIPFHFFTTSLFIFLNAVEGLKFILLFVYFLPLLQVGTVFWFLLKPFQII
YYWSRRYLIESLIRVFLFGYSLVRFTDFFFGDILISLTYALGDIYIFFCVYSLLFREPLCKSSHSDLSGL
AALLPVIVRFLQCLRRYRDSLHEFPHLLNALKYSLNIPVLFCLWLYRVYEGEERLFHLQIWFALLNSIYT
SFWDVFMDWSLDSLTSLRSWSKRAVTLLKYHIAMIINFLLRFSWIVYYLPPNHIQHSADIFIFIMQLLEI
LRRFVWVFFRVEAEHSINFASFRAAGELKVTPHD
>gnl|CDD|444166 COG5410, COG5410, Uncharacterized conserved protein [Function unknown]
MSKASNLEAIARAARRALARRDFLSFARLTFPLRPGQKFVDNWHHRLICDALERVIDGEIKRLIINMPPR
HGKSTLASVAFPAWLLGRNPDKRIIVASYSQDLATKFSRDVRNIIQSPWYQDLFPGTRLSSDKDAKNEWS
TTAGGGRLATSVGGTITGFGADLIIIDDPIKAEEANSETVRDKVWDWFTNTLLSRLNPGKGPIIVIMQRL
HEDDLAGRLLAGGQGGKWEHLSLPAIAEEDDIYLGRKDGEALWPERESLEDLEALKREMGSRVFAAQYQQ
RPIPLGGRGPVELSGIDAYLDLPDYVDSRVDDADSADAAADDVSGTKDVVDTTGVVDDGKLVLLFVLLRL
IRPLKLKADLRRAKAIKTIAAKLIELIAILKKAGAAGVAALLIIIKRIKRVVLRRPKAEDRARAVAARLA
ALVLALPLLLAAAALDAAAGEDDLADDLSDDDDLDDDAAVLLDMALALLALDSRALGRL
>gnl|CDD|227698 COG5411, COG5411, Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms]
SPVPIYDPRHPYIVAVLRQRRSKYVIEKDVSIFVSTFNPPGKPPKASTKRWLFPEIEATELADLYVVGLQ
EVVELTPGSILSADPYDRLRIWESKVLDCLNGAQSDEKYSLLRSPQLGGILLRVFSLATNLPVVKPVSGT
VKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAGVNNIEERIFDYRSIASNICFSRGLRIYDHDTIF
WLGDLNYRVTSTNEEVRPEIASDDGRLDKLFEYDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEYD
TSDKGRIPSWTDRILYKSEQLTPHSYSSIPHLMISDHRPVYATFRAKIKVVDPSKKEGLIEKLYAEYKTE
LGEAGDISCDNFTILVLYGHVDGKIAIFSLGQPRLLELIGSDVIVGPTLWMIYVPDVSLKSPPGHKASHN
GATPILKRLQVVSSVSPAMGATEMRSPFPEYSTDPSSLIR
>gnl|CDD|444167 COG5412, COG5412, Phage-related protein [Mobilome: prophages, transposons]
AAAADASAKEAASAALLLAQAKAADSELTAASGGVVSAAAKAQGSIAQLGKIGAAAGAEAALADSSLAFA
TLAAALGATVAGASLLLAAGGARAKGSAAAAAALGAVAAAAKVLNGALAAAGAALAATQALAAAATGAKG
EANAAAKAGGAAALASAGLAAAGAAAAASALAAAGAIAKAILSASKLSGQALAGQSAAAGGALEAAAAAA
AGAAAAGAAAAAATAASALLALAALQGLAAGAATGAAAGAAGAAGLGAAGAGAGQAAALLGLVAGAEASG
GTAGGAVAGLAAGLAAAAGASANLGAAAAASFGASLAASAGVDTAAAALAAAEAIADGSLVAGLGSAGTV
LSTLSGAVGGLEGAIGQLGAAGGLGSALGGLTGPIGIVIAAIAALIAAFVALWKNSETFRNLVQGVWELN
AIKTAIEGVVSAIVTFISALWEAIKALLTAIGGALPQLIAAVWNGIVQFISAIITNLPLILQAALQLIKA
LIKGLWTAIKGVIQGAIEIITGIIQFITALLTGDWSGIIWEGIKQLVSGIVEIIPNIVAAVPQGGIAALW
DAIKGFFPGLIEAIVQLVSNIINAIISIISSILNAAGSIISSIWNAIKSAVSSIISAKSIGKNIVNGLWN
GIKSAAGAVTDKVKDIVGGIVDGIKGALGIHSPSRKFLEIGKMIVAGLAKGIEDAFSVNSAVSKLADGLN
NAID
>gnl|CDD|444168 COG5413, COG5413, Uncharacterized integral membrane protein [Function unknown]
TMADPHAPEVYQGQFGEFTIDFWDRLTVIIYRLGLVLAALSFALGSALVLQSPVPQLLTPLYAGFLIALG
VSLSTIHIYLKNLHRLLQFFWWIGLLAAVAFALSSSEPLALTVYNQPLTLLGLGFTFAALTGIYFKEAFC
FNRLETKLLTPLVPLLLLGHLLGILPLLLEQILLLVWAILFLIFAIRKWRMPLHFDIGDKSVFQYLKQQR
>gnl|CDD|227701 COG5414, COG5414, TATA-binding protein-associated factor [Transcription]
MAVIRIKKPRGPPLEGRIKTKVTDEDIPKPKLKINLKKKKGPKAPKLRLKPIRIPGEAYDSEASDIEDDP
LIEQQFILRLHPSIQIEHVVDLGESGDYSGITIKIKDDRSAVVTHNNKKYPAILVDLPCIIESNKSMDSK
QHYKVADISQMLVALEAVYHENSFLNKHLKKEREYYYLHGLSPPLKYVRARRFRKKSSKIEIEEVEKKVD
DLLEKDMKAESVSVVLKDEKELARQERVSSWENFKEEPGEPLSRPALKKEKQGAEEEGEEGMSEEDLDVG
AAEIENKEVSEGDKEQQQEEVENAEAHKEEVQSDRPDEIGEEKEEDDENEENERHTELLADELNELEKGI
EEKRRQMESATNPILQKRFESQLNVLLKELELKRKQLEMEED
>gnl|CDD|227702 COG5415, COG5415, Predicted integral membrane metal-binding protein [General function prediction only]
MGSRFDKDFVTKYTADLSRLESQIHQLDVALKKSQSILSQWQSRLTVYSLALTVLALSYIYWEYHGYRPY
LVITALLLGSGSLYMFRWALTKLYEFRNNRRLRKLAKLRAIHRKKLEKLKEETHYNATSSIIQKYSEELN
AKYQELNNLKTEKEKFKKESHVKKKEDSDAWFDKVISVLAGGNELDLSPFKALICPQCHHHNGLYRLAEK
PIIEFICPHCNHKNDEVKEREDSNEAKQPAQPSQSEKEKTK
>gnl|CDD|444169 COG5416, YrvD, Uncharacterized integral membrane protein YrvD [Function unknown]
MKQLYLILGLLVLLLLLIFAVQNTQPVTVNFLFGQFELPLILVILGAFVLGALLGALAGLVRILRLRREI
KRLRKELKELEKELAELRALPLEEEN
>gnl|CDD|444170 COG5417, YukD, ESX protein secretion system component YukD [Intracellular trafficking, secretion, and vesicular transport]
HINVTVDLKHYGGGVYDLRISDHQTVKQLIDILWQTLSISIPPREGYWIKVVNKGIVLSGNDKLADYGIT
TGDRLEIL
>gnl|CDD|444171 COG5418, COG5418, Predicted secreted protein [Function unknown]
MKRSKKIVVVAHCLLNPNSKVKGLAEYEGVLEELVKLLLEKGVGIIQLPCPELLYLGLKRWGHTREQYDT
PFYRKHCRELLEPIVDQIEEYAKNGYEIVGIIGVDGSPSCGVNTTCSGNWGGEISAAEHLFYKIDNIEMV
PGPGIFMEELEKELEERGIEIPFVGIDE
>gnl|CDD|444172 COG5419, COG5419, Uncharacterized conserved protein, DUF2285 domain [Function unknown]
DAATWLRPLPDGRRAILPAPLPTALAQSRGRRLLEDPILDARDAHGRVLPVDDRVVQLSPDIPLDADGLD
RLEALLRLWRALHGRPLPPDLRLTPQQRRRLRRMLRALDGRLAGASYREIAEVLFGAARVAAEEWKTSAL
RDRVRRLVRDGRAMIAGGYRKLLRHRRRR
>gnl|CDD|444173 COG5420, COG5420, Uncharacterized protein, UPF0437 family [Function unknown]
MSDIEELKAEVKKLSARATQAKMDLHDLAEELPTNWEEIPEVAQKTYDAYAELDEARAELKAAEKA
>gnl|CDD|444174 COG5421, COG5421, Transposase [Mobilome: prophages, transposons]
EISSRSLGHLGLLAGLWKELGLDEILDKLLPKDRREGLSVGELILALVLNRLGDPSSKLYVEEWFKDTAL
EELLGLDPEDLNDDRLYRALDRLGEHKIEEIESELALRTLKLFGLEVDVVFYDTTSFYFEGEYEDGLAKY
GYSKDHRPDLKQVVLGLLVDRDGIPLAYEVFPGNTADVKTLKPVLEKLKKRFGLKKVILVADRGLYSEDN
LALLEEAGLKFITRLPLKEAKELLKDAILDPSNFEEGEGYRVYEKEVEYGGGEQRLVVVYSPARAKKDRK
TREKKLEKLEEELEKLRKKLKKKRFACEADAEKAIKRLLKKLGYSKYLKVEVEEKRPYQIAKVEIDEEAI
EQAEKLDGKFVLITNVETDLSPEEILRAYKDLWKVERAFRFLKSDLELRPIFHWTEERIRAHLFICFLAL
LLYRLLERRLREALLKDTLRWLLEELSTIHLVTVEGKGKTFVIITELTEKQREILKALGIKPPKYYLLVL
>gnl|CDD|227709 COG5422, ROM1, RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms]
PNALGLNERNRAYEEIFGAPRKSDAFVSKQLLPPRRLQRKLNPISIRNGADNDIINSESKESFGKYALGH
QIFSSFSSSPKLFQRRNSAGPITHSPSATSSTSSLNSNDGDQFSPASDSLSFNPSSTQSRKDSGPGDGSP
VQKRKNPLLPSSSTHGTHPPIVFTDNNGSHAGAPNARSRKEIPSLGSQSMQLPSPHFRQKFSSSDTSNGF
SYPSIRKNSRHSSNSMPSFPHSSTAVLLKRHSGSSGASLISSNITPSSSNSEAMSTSSKRPYIYPALLSR
VAVEFKMRLQLGDHKKDGLLYRDAFTGSEAVDVLMLIIRTSDRNLALLNGRSLDAQKLFHDVTYDHRLRD
SRIEIYQLRGYSDMRIAHNFPTSSTSFENMGKATLTNSSSSTNEPATPKAEYNPNGVFTLLTECYSSTCS
RDELCYSISCPRRLEQQARLHLKLMGGLKRNSSLALDKFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIY
EVIYTERDFVKDLEYLRDTWIKPLEESNIIPENARRNFIKHVFANINEIYAVNSKLLKALTNRQCLSPIV
NGIADIFLDYVPKFEPFIKYGASQPYAKYEFEREKSVNPNFARFDHEVERLDESRKLELDGYLTKPTTRL
ARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLFHLNQQLLFKPEYVNLGLN
DEYRKIIFKGVLKRKAKSKTDGSLRGDIQFFLLDNMLLFCKAKAVNKWRQHKVFQRPIPLELLFISPDED
SPDRAEYLKPAPSADVLDPAYNTKPPKNAYGFELYGNGQRYQITLYAETHAGRDTWLEHIKNQQDILRTR
TLWFTSFPICDQFFSTTNKVNPVPLYDSGRKLLTGTNKGLYISNRKDNVNRFNKPIDLLQEPNISQIIVI
EEYKLMLLLSDKKLYSCPLDVIDASTEENVKKSRIVNGHVSFFKQGFCNGKRLVCAVKSSSLSATLAVIE
APLALKKNKSGNLKKALTIELSTELYVPSEPLSVHFLKNKLCIGCKKGFEIVSLENLRTESLLNPADTSP
LFFEKKENTKPIAIFRVSGEFLLCYSEFAFFVNDQGWRKRTSWIFHWEGEPQEFALSYPYILAFEPNFIE
IRHIETGELIRCILGHNIRLLTDGRGPLLHGGEILYKCYEDDVGEENERSLSLHL
>gnl|CDD|444175 COG5423, COG5423, Predicted metal-binding protein [Function unknown]
MEDNLEELIEKALELGFSDAKVIDPDDIVVAEWVRLKCRFGCGNYGKNWSCPPNVPTPEEFRKILSEYKK
ALLLQTESPLEDSFDDKEMMELSRDHQKILLELEKLAFRAGYYKAFALGAGPCRLCEECAYPDEPCRFPD
KARPSMEAYGIDVFKTAKKAGLPLEFLPDKNDTVTYYGLVLLE
>gnl|CDD|444176 COG5424, PqqC, Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism]
LLSPEEFEARLRAEIARRYLLKHPFLQRLREGKLTREQLRAFALQRYHYVKHFPRYLAAILSRCPDEELR
RALLENLYEEDGEGPEEGHIELWLRFAEALGLDREEVDARPPLPETRAAVDAYVNFCRRRSLLEAVAASL
TAEGFAPEISRERLEGLLEHYGLPDEEALEYFRLHAELDPRHAEEALELVLRLADTPEDQEAALEAARFK
LDLLWAFLDALYRAYVAP
>gnl|CDD|444177 COG5425, Usg, Usg protein (tryptophan operon, function unknown) [Function unknown]
MVSSDFELQLEGYGLTTAEILYRMPDHPSLLQSFVWQDYDLAPDFPELFRFLDFWQREIEGPLHSVRVAH
RRLIGPAEWRAVDGEFRLH
>gnl|CDD|444178 COG5426, COG5426, Uncharacterized protein STM3548, contains class I glutamine amidotransferase domain [General function prediction only]
LLVAAALALARLALLALLLLALAGALAALLVLAARLRLLLALVVVLVLLVLLLAALASLLLALRAALAAL
RLRLALAALALLLLLLAELALLLAAAGTLGLLAALAAAAAVAVAARAAAAAVSLDGAGAAAAAALAAADA
ARVALALARERSLEDRARRAALAALAAAAEAALADAARDVDGGGAAGGVVAVTVRRNGAAGALLVVGPGP
VGALVVVTVGAGRAGAELAVAAVVGEVTELNNREVARIDAVRVVLDVLLVLGESGAGERGGRNLLKLDAV
DDLVDLTILRPLEKQDGTPINELSLLALITFPLFELKEVEFDLIDLVRYQRREVLPRLYLDYMKLRVLRF
LRNALERPGIEVDHIPAHEALIGFPSTEEELFAYDVVILSDIGANTLLPNQLELLADYVERGGGLLMAGG
PLSFGPGSYARTPLADVLPVELLPGRGEVPEGPFRPELTEEGRRHPVTRGLPGSAANPPAWGELPPLLGY
NRVGAKPGAEVLATGPDGDPLLVVGRYGKGRVAALASDQAWLWARGFFGGGPYARLWRQLLRWLMKEPEL
EEEALRALADGRTLEIERQTLIERAAPVTVTTPSGGTRVVTLVEGEPGLREAEPEAPELGLYRGEFGALE
ALAAVGPAAPREFEEVTSTTEVLAPLAEATGGEVLRLAPAAALLLLEARATAGGGRGLDGLDLLRALLPA
DPRLVPLVVRLLLLLLALLLLLLLLLLLALLLRRRRRR
>gnl|CDD|444179 COG5427, COG5427, Predicted membrane glycosyltransferase AF0583, Arch_YYY/DUF2298 family [Function unknown]
LAGLPLAARLFPRLPDRGAGLARPLGLLVVALVVWWVGSLGWPFGRVTILAGLLVLVALSALALWLRRGE
LRRGLRPRRRAILEAEAVFLAAFLFLVLIRAFNPDLWHPGGEKPMDFGLLNALLRSGTLPPYDPWFAGEP
VNYYYGGHLLAALLAKLTGTAPRVAYNLALAGFFALLATAAFGLAGNLAAARGGPRRRARLAGVLAAFFV
GLAGNLVTAIRLLVGLVLLPAGLRRRLAGERLAAGPGDFDYWDASRVIPGETINEFPFFAFLNGDLHAHM
MALPFLLLALALALAYYRTPARQRRRRLLLLFALLGLVAGALAVTNTWDFPTYLGLAGLALALAPWRSQS
RLLAELRRLLVALGVAALLAVLSALLALPFLLGFASGYRGIGLLPGERSPLGELLLVHGLFLAIFLSYLV
RRLRSRLSRRWLRVAGLALLLLAAVGVLLLLGVPALALLLPLLVLAWVLLRRPRSARGVGFELLLIVAGA
GLVLLVEFVYLRDDAGPGRMNTVFKFYMQVWVLWALAAGVALAWLLASARSVSSLLRPRVRAVWAVVLVL
LVLSALLYPLLATPAHLADRMPPAPPTLDGMAFMETDHPDDAAAIRWLRENAEGSPVILEAPGTDYRWGN
RVSSLTGLPTVAGWVGHERQYRGGEALPEYDERVRDVDTIYSTGDPATAAELLERYDVRYVYVGPLERAR
YGPVGLAKFEQGPGLEVVFRDGAVTIYRVDQDALP
>gnl|CDD|444180 COG5428, YuzE, Predicted antitoxin component YuzE of a toxin-antitoxin system, DUF2283 family [Defense mechanisms]
MKVTYDPEADALYIRLRDGPVVESEEVSPGIILDYDEDGKIVGIEILNASKRLDPEILKELEA
>gnl|CDD|444181 COG5429, COG5429, Uncharacterized conserved protein, DUF1223 domain [Function unknown]
MKRLLALLLAAAAGTLAAAAAAAAAAAAKPPVVVELFTSQGCSSCPPADALLGELAARPDVIALALHVDY
WDYLGWKDTFASPAFTERQRAYARALGRRSVYTPQMVVNGRDHVVGSDRAAVEAAIAAALAQPAGAPVTL
SLSRDGDTLTITVGAAPGAAGPADVWLVLYEPEATVEIRRGENAGRTLTYVNVVRSLQRLGMWDGKGPAS
LTLPPELTPGDDGLAVLVQEGGPGPILGAARLPL
>gnl|CDD|444182 COG5430, SCPU, Fimbrial subunit ScuA/B, ScuA/B/SCPU domain [Extracellular structures]
LLLALALALLLLLSACSSAAAGTATGTFTVTATVTAGCTINSAGTLNFGSYSPLLTASLDATGTITVTCT
NGTPYTIGLDGGLNASGVGTRRMKNASGGNTLPYQLYQDAARTTVWGNTTGDTVSGTGTGSAQTLTVYGR
IPAQQTPPAGTYTDTVTVTVTY
>gnl|CDD|444183 COG5431, COG5431, Predicted nucleic acid-binding protein, contains SWIM-type Zn-finger domain [General function prediction only]
MSDEDTRSYERLIRLHGDRGKKAIEAVLEGRVKKYSSGDRDFWVVVGHEDDYVVEGGFCSCKDFTYNLDS
RKPKEPCWHLLAVKIARRTGKYDEIDMWYSDVRKILNEILTLGLSPTLK
>gnl|CDD|227719 COG5432, RAD18, RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms]
NELDATDPSDWNQTKIPSLKGLDSMLRCRICDCRISIPCETTCGHTFCSLCIRRHLGTQPFCPVCREDPC
ESRLRGSSGSREINESHARNRDLLRKVLESLCRLPRPIKEERPCRWETVIAQDSASGDEEWEDDLASNSS
PASIAKKTSRDSKKRKREDLVHCPACSNLVPHNQINQHLDSCLNSPSSPSSSSSPYKNKDNSKSNSLLSF
KTDDDSITKRRLRSFNSADELPLKDRVRLPKLTYALLSESKIRSKLSEMGLPTDGHKQLLQRRHAKWVTL
YNSNLDQKQPVSKRNLIRQLIDWERVQSKSIGVEKEKLGGGDWEKAYAEDFADLINRAKQSTTNKNDSLR
NTAVESSTEPSTSNGFPATSVSPPLTIDLTNSQTGSDGPQS
>gnl|CDD|444184 COG5433, YhhI, Predicted transposase YbfD/YdcC associated with H repeats [Mobilome: prophages, transposons]
LLDALRVLLLAGLLSVLFARAGLALIGDAAELRAAGLLKLLLLLLGIALKAAIPDVITLRRARDAQRARI
NHVASLAASAGGASLGGGAVIAADGEIAAASLRLKLLLIALLLVTIAALAQAALLAQIIVIKKAEEILAI
KGLLLLALAGKAITTLAALTLARIIALLDADLGAEILLVREASRASLAADVAEIAGDGKRSRLARAIIEG
RLETVRAGKTERELRYGRKRGKKSNEVRYYISSLSADAELLAKAIRGHWGIENKLHWVLDVVFREDASRI
RSGNAPENFACLRRIALNLLRQDGDYKLSIKGKRKRAAWDDDYLLKLLFGK
>gnl|CDD|444185 COG5434, Pgu1, Polygalacturonase [Carbohydrate transport and metabolism]
AEPSFPAKTFNITDFGAKGDGKTLNTAAIQKAIDACAAAGGGTVLVPAGTYLTGPIFLKSNVTLHLEKGA
TLLGSTDPADYPLVETRWEGGELKGYSALIYAENAENIAITGEGTIDGNGDAWWPWKKEARQSGWVPVGA
YDYLRPRLIQLKNCKNVLLEGVTLRNSPFWTIHPLGCENVTVDGVTIDNPADAPNTDGIDPDSCRNVLIE
NCYIDTGDDAIAIKSGRDADGRRNRPTENIVIRNCTFRSGHGGIVIGSETSGGVRNVTVENCTFDGTDRG
LRIKSRRGRGGVVENITIRNITMRNVKGTPIFINLFYEGDRGGPTPTFRNITISNVTATGAKSAILIAGL
PEAPIENITLENVTIGAAYGFYI
>gnl|CDD|444186 COG5435, COG5435, Uncharacterized conserved protein [Function unknown]
TYQFNEGSFDLPDGWQDRSVNILVLPDPGGSGPSLVISRDPLPPGETLEAYVDRQLAELRKQLKGFQLLE
RREVTLGGRPAVELEYRFRSGGQRVYQRQVVVLLPDGTLLTFTATSPGPFTEEQDAHWEAILASFRP
>gnl|CDD|444187 COG5436, COG5436, Uncharacterized membrane protein [Function unknown]
MRRLLLALLAGLVLAGIVHIVVVLALPYLAMRDAYSRLAALGPPNKFTLLPRPTPGSQPLPRLDPALAYA
VCRFDLSDGPVRLTAPVPDPYWSLSFYDRNGDNFYSINDRAAGRGTLDLVLMTPAQLEALREDEPEEAAR
SLIVESPTDEGFALLRALAPDPSARPEARAALAAASCTPLAA
>gnl|CDD|444188 COG5437, LmaA, Phage tail protein, TP901-1 family [Mobilome: prophages, transposons]
MAAQKGKDLLLKIGDGTGPGTFETVAGLRTRTLSFNAETVDVTSKDSAGGWRELLAGAGVKSASVSGEGI
FKDDASDAALRAAFFDGEVRDFQVVIPDFGTIEGPFQVTALEYAGPHDGEATYSLTLESAGALTFTAA
>gnl|CDD|444189 COG5438, COG5438, Uncharacterized membrane protein [Function unknown]
MKKKLAILILLLILLLIFLLLYPTSYVKAKVTSVDNEDLSTGGERTGSQTVTVEILSGPHKGKTVEITNP
LSLPYDIKLKVGDKVVVVISDTEDGGILSYSIYDYDRDNPLILLAGLFALLLLLVGGWKGLRALLGLAFT
LLVIWKFLLPALLKGYNPLLVALVGSALITFVTLYLVHGFSRKTLAALLGTLLGLLIAGVLAALFGKLAH
LTGLSSEEAETLLYISGYPGLDLRGLLLAGIIIGSLGALMDVAMSIASAVWELKEANPDISRKELFKSGM
NIGRDHIGTMVNTLILAYAGGSLPLLLLFSAYGRPLLQILNSEFVAAEIVRTLVGSIGLVLAVPLTTAIA
ALLYKRKKRKK
>gnl|CDD|444190 COG5439, STAS, STAS domain [General function prediction only]
MEIKTEDYRVWYDPATSTVTFQGSLRLNGMDEYAPILSLLNEVAESEPPTLTLDLRELEFLNSSGINMLS
KFVIEVRKKKDVQLVVLGSKNIPWQGKSLKNLKRLMPSLQLELE
>gnl|CDD|444191 COG5440, YbjN, Global stress regulator YbjN, DUF2299 family [Signal transduction mechanisms]
LKEEIRKWLKEEGLIVEEPPDANAEFHIVVETPPPGRVVLDIIRPKDKSDRVVIAMGIGVSPEHKRALSS
LKEEERREFLWSLLFDLLFMCVDFQILPPNENLPQSIQVSKEIYFDGLTKNRLLDAVYRVRNAKLYVIWK
FNERFGETPEQPDS
>gnl|CDD|444192 COG5441, Tm-1N, ATP-binding helicase-inhibiting domain, Tm-1/UPF0261 family [Defense mechanisms]
MMKTVLVVGTLDTKGEELAYLRDLIEAAGVDVLTVDVGVLGDPAFPADISAEEVAEAAGSGIEALRASGD
RGAAMAAMAEGAAALVAELYAEGRIDGVIGLGGSGGTALATPAMRALPVGVPKLMVSTVASGDVSPYVGA
SDITMMYSVVDVAGLNRISRKVLSNAAGAIAGMAKAEEPEPTEDKPLIGLTMFGVTTPCVTAAREALEER
GYEVLVFHATGTGGRAMEKLIDSGLFAGVLDLTTTEVADELFGGVLSAGPDRLEAAGRTGIPQVVSPGAL
DMVNFGPRDTVPERFRDRNLYVHNPQVTLMRTTPEENRELGRWIAEKLNAATGPVAFLLPLGGVSALDAP
GGPFHDPEADAALFDALRETLDPNVELIEVDAHINDPEFADAAAEAFLELMAKGGVK
>gnl|CDD|444193 COG5442, FlaF, Flagellar biosynthesis regulator FlaF [Cell motility]
MAASAYAEAADSTASPREREAEALARATARLQAARDAGADSPELAEALHFNRRLWTILAADLADPDNPLP
DELRANLISLGLFVLRETSKVLRGESEDLDPLIDINRAIAAGLSGRAAAA
>gnl|CDD|444194 COG5443, FlbT, Flagellar biosynthesis regulator FlbT [Cell motility]
MGLKLSLKPGERIIINGAVIRNGDRRVRLEILNDAPILREKDILQPEEATTPARRLYFAVQLMYIDPEDA
EDARELFLELLEELLQAFTDPDARALLDEASELVLAGRYYKALKALRKLIPYEAELLAAAEA
>gnl|CDD|444195 COG5444, YeeF, Predicted ribonuclease, toxin component of the YeeF-YezG toxin-antitoxin module [Defense mechanisms]
MKVLDVSSLHTAIDQTIKQLKQLREQFVALKKAVEGIAELDDAFKGKGADAIKAFYQECHLPFLDFWLTF
IDSYIAFLKKIKSALESLEPSENGFISESFLEHELENGLKKAKEITSELTDEINQILASVSDIVSLPKLS
DSDFQEQIDKAKKKRDDTVEKLYELDQNQTTELAQLENDLQTMKTYISKLEEATTGGKISPTNFNAKAYH
NFAEYSELHKKAGEIKKQTEDTMMYLALKKQQEEAREINKLAEEDEILINRPWYYKAWSTVITFTGEVTG
YYDVKRAATGMAAAGAAPEVGWAGRMVKLATKGAAKGSKVLKAGKYGGYGLDSANKFKTVKTALAKAGLA
LAGGVPYNIKNSKGLK
>gnl|CDD|444196 COG5445, YfaQ, Uncharacterized conserved protein YfaQ, DUF2300 domain [Function unknown]
GELACALLDAAGVALAVTAAGDQLELVLRQEDLLPTSGVSLSGVWKLVSYARTAEGALRWLEYLYQGSRP
DRVPCPEPGQQGRRGEALYRCCGGYTIGRDLALARGRGLGFLPARLPLAAAAWRGRQARQQARAPAWLAL
LWLGQPATPVRVASLLDVLAAALGEAARTLLGVLVVRDRAKTVTMFGSRLRVRTWVWAWASDDGAEGRGG
GFAGWGTDGTPLWGWGSRVSQLLDGAAALALPLVGPVPTDDDDAVCVEVFYFYRYPEARLADGKPAAEGV
LAGRYRVRFANGNRLSIASRGELRLSREDGRPRLTGRLGLEDYVARVVEREARAEPPAAARALAVAARTY
LVQHANHDGGCLAIDDSSATQRVSPRPPSAAARRAAAWTDGLVLTGAPVRYHSSRAAPGQMSWADAVAAA
QQGLRFDQILARAYPQATLTSRWGAPAGDCQALPGAEAWLAKRRPQWRRRLAGEPGYETPPLPAVCRLAE
GRPYADRQRGRLYVRGFQSLEERLTLTHEYLHLAFAGHPRGLDENFIERLARRLLGTD
>gnl|CDD|444197 COG5446, CbtA, Putative cobalt transporter membrane subunit CbtA [Inorganic ion transport and metabolism]
MFRRILFAALLAGLLAGLVLTGLQFFQVTPLILQAETYEEAAAAAAHSHAAAHAHAHAEGAAAAHSHDEE
AWAPADGLERTAYTVLANVLTGVGFALLLAAAMAAAGRRITWRNGLLWGLAGFLAFFLAPALGLPPELPG
MPAADLGARQLWWLATVLATAAGLALLAFRRAPWAKALGLVLIAAPHLVGAPHPEDHESGVPAELAAQFA
VASLATNAVFWAVLGLLAGWLWQRFTRRA
>gnl|CDD|444198 COG5447, COG5447, Uncharacterized conserved protein, DUF1491 domain [Function unknown]
MRLKSDIWVSALLRRLRAAGGFAAVLRRGDEEAGAILVKLNRLDGTARLYGPAPQLMDGERAWERLLGAD
PVDEAEVDAYLARQRRFDPDLWVVEVEDRDGRHFL
>gnl|CDD|444199 COG5448, COG5448, Uncharacterized conserved protein, DUF2460 domain [Function unknown]
MMAFHEVRFPLDLSFGSSGGPERRTEIVTLASGREERNTRWAHSRRRYDAGYGVRSLDDLAALIAFFEAR
RGRLYGFRWRDWSDFKSCAPGAAPSPLDQVIGTGDGATTAFQLVKTYGSGGAPYVRPITKPVAGSVRVAV
DGVELAEGVDFTVDATTGLVTFAAPPAAGAAVTAGFEFDVPVRFDTDRLEVSLASFQAGEIPSIPLVEIR
V
>gnl|CDD|444200 COG5449, COG5449, Uncharacterized conserved protein, DUF2163 domain [Function unknown]
MRTISAALAAHLAGEVTTLATCWRITRRDGVVLGFTDHDRDLTFDGVTYRAASGLEPSAIESGDGLAVDN
LEIEGALSSDAISEADLAAGRYDGARVEIFLVNWEDPEGRVLLRRGTLGEVTREGGRFRAELRGLAHALQ
QPIGRLYSPTCRARLGDARCGVDLAPFTAEGTVTAVDDRRITVSGLPAAGWFAYGRLTFLSGANAGLAAE
VKAAGGGSLELWEPLPEAIAPGDAFTLTAGCDKRFATCRARFANAVNFRGFPHIPGNDFVLR
>gnl|CDD|444201 COG5450, VapB6, Transcription regulator of the Arc/MetJ class [Transcription]
MRTNIDLDDDLFAEAVRWTGLKTKKDAVHLALRALLRQRKQKHARVLRGKIGWEGDLDAMRS
>gnl|CDD|444202 COG5451, COG5451, Predicted secreted protein [Function unknown]
MRRRALAVLLLLALAAAPAAAAPAEAAPAPYEGDLLRLAEILGALHYLRNLCGAEEGQEWRDRMQALLDA
EAPSEARRARLIAAFNRGYRSFAQTYRTCTPAARAAIQRYLAEGAKLSREIASRYGN
>gnl|CDD|444203 COG5452, COG5452, Uncharacterized conserved protein [Function unknown]
MLFSLFRRRRRRAAVEALYGAIVAQARQPAFYADLGVPDTVEGRFDMLSLHLFLVLRRLRAEGEAAAELA
QALFDAFFDDMDASLREMGVGDLSVPKRMKKLAEAFYGRAGAYDAALDAGDDAALAAALARNVYGGAEEA
PAAAAALAAYVRAAAAALAAQPLDDLLAGRLAFPDPAA
>gnl|CDD|444204 COG5453, COG5453, Uncharacterized conserved protein [Function unknown]
MMSFLKKLFGGGGAAEAPPPVAEPVEYKGFLIYPEPMAEGGQYRVAGRIEKEIDGETKEHRFIRADLFPS
RDDAAELTLRKAKQIIDQQGDRLFD
>gnl|CDD|444205 COG5454, COG5454, Predicted secreted protein [Function unknown]
MGITSAIAIYFVIWWLVLFAVLPFGVRTQGEAGEVVPGTDPGAPARPRLGRKALITTLIAAVVWALIYAV
ILSGWITLDDIPFFPRMP
>gnl|CDD|444206 COG5455, RcnB, Periplasmic regulator RcnB of Ni and Co efflux [Inorganic ion transport and metabolism]
MKKKLIILALLAASLLAAASAAFAQPPGPDRRGHDRRRDDRHDDPGHRDKHRGAGPGEDYKRWRRGDRLP
PEYRGRRYVVNDWRRYGLPAPPRGYHWVRVGGDYVLVAIATGIIVSIVLGR
>gnl|CDD|444207 COG5456, FixH, Nitrogen fixation protein FixH [Inorganic ion transport and metabolism]
STASQAPRELTGWHVLAIFVGFFGVVIAVNLTMAYLAVSTFPGLVVENSYVAGQAYNRTLAAARAQAALG
WTVSADLEPDAGGGGRLTVRLTDADGQPVDGAQVTARLGRPTDARDDFTLDLTEVGPGVYVAPVALPLPG
NWDLRIEATRGDGTVFRQRRRLFVRG
>gnl|CDD|444208 COG5457, YjiS, Uncharacterized conserved protein YjiS, DUF1127 family [Function unknown]
MATITTTRAALLARLARRLARWRERRRTRRELARLSDRELADIGLTRSDIRREARKPFWRA
>gnl|CDD|444209 COG5458, COG5458, Uncharacterized conserved protein, DUF1489 domain [Function unknown]
PLHLIKLCVGAESVEDLAAWQAERRAAGPDGEPRHTTRMWPKRADELLDGGSLYWVIKGVIQCRQRILGL
EEVTDEDGIRRCAIVLDPELIRVEPRPKRPFQGWRYLKPEDAPPDLGEGGGGGDALPPELRRELAELGLL
>gnl|CDD|444210 COG5459, Rsm22, Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]. Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins
ELPAALRRALEDLLEGRSGARLRAAIRRLSERYRAERGSRRPYLADEADALAYAAYRLPATYAAVRAALA
ELAEAGPDFAPLTVLDVGAGPGTAAWAAADAWPSLLDATLLERSAAALALGRRLARAAANPALETAEWRL
ADLAAALPAPPADLVVASYVLNELADAARAALVDRLWLAPDGALLIVEPGTPAGSRRLLAARDRLIAAGA
HVAAPCPHAGACPLAEPDWCHFSRRLARPRLHRRLKGAALPNEDEKFSYLALRRDPARRPAARVLRHPLS
RKGGVELKLCTPDGGVRERLVSKRDG
>gnl|CDD|444211 COG5460, COG5460, Uncharacterized conserved protein, DUF2164 family [Function unknown]
MMKIELSKEEKEQLIAKIQRYFEEELDEEIGQFDAEFLLDFFLEEIGPYIYNQGLADAQAVLQERLEDLD
EELYELEKP
>gnl|CDD|444212 COG5461, CpaD, Type IV pilus biogenesis protein CpaD/CtpE [Extracellular structures]
MTRPTRAARAALLLALALLLAGCASDRPNTTGSIPDDYRTRHPIVVEEAAETLDIPVGPGDGGLTPAQRA
RLAGFAAAYRRRGGGRVVIDVPSGSANERAASAAAAEIRAVLARAGVPPSNIAVVTYGAGDPEAAAPIRL
SYTRYVASVPPCGDWPEDLASTFENRPYWNFGCATQSNLAAMVANPRDLVGPRAETPADAARRTKAIEKY
RKGESTATEYEDQESGSVSG
>gnl|CDD|444213 COG5462, COG5462, Predicted secreted (periplasmic) protein [Function unknown]
MIRLLNILLILAVIGLAFWLYRIKYETQALAEEVAKLERQIAAEREAIAVLRAEWAYLNRPDRLQKLAER
HLGLQPLEPEQFVRLDDLPERPPAPDPIGALIEVLADPAASATPSV
>gnl|CDD|444214 COG5463, YgiB, Uncharacterized conserved protein YgiB, UPF0441/DUF1190 family, involved in bioifilm formation [Function unknown]
MKRSKNINLDKSRKSFTVAPLALAVAVLALAGCGDEDEEASLYTSVDDCIAANPSDAEQCQTAYAEALQE
AERTAPKYASREDCEAEFGEGQCTQVPASSSGSFFMPLMAGFMMGNMLSGGGGYASQPVFRSRSGNSPAY
GKWVTADGKSYGSATTGRSVTVPKTALKPKPAVTRTISRGGFGSTVAAKSSWGGSSSSRSFGG
>gnl|CDD|444215 COG5464, RpnC, Recombination-promoting DNA endonuclease RpnC/YadD [Replication, recombination and repair]
MKTPHDALFKQLFSNFPRDFFELLLPEELELIDLSTLELLSTEFVDDKLRAFRSDGLFSPKTKDGPGYIY
LLIEHQSQPDKLMPFRLLRYIVLYLRQYLKKGPVIPVVIYHGRSSPWPVPTRYLDLFADPELAEELLFSY
RLIDLYLIEDEEILQHPLGALLPLVKILDRTDALEELLRLLARLLQEIEDEAQREQLEALIEYIAVKFQP
DLEREEIEAMLRLIDELKETIMTIYQELLQEGREEGRQEGREGRQEGRQEGKLELALRLLKRRFGLPLEL
IARITGLSLEQLEALGEALLD
>gnl|CDD|444216 COG5465, YbjN, Uncharacterized conserved protein YbjN, helps stabilize unstable proteins [General function prediction only]
MSLLESESERDAHPLDVVEQLATANDWPFERVGEDEIAMAVEGQWGDYSLFFAWREEDEALHLACAFDLK
VPEARRAEVYELLALINEQLWIGHFDLWSEDGVIMYRHGLLLAGGQEASPEQIEALIDAAVEACERFYPA
FQFVVWGGKSAEEALAAALFETVGEA
>gnl|CDD|444217 COG5466, COG5466, Predicted small metal-binding protein [Function unknown]
MKEFKCGDVGPDCDFVARAESEEEVLRQVAEHARAAHGEEEITPELVEKIKSRIKEVA
>gnl|CDD|444218 COG5467, COG5467, Uncharacterized conserved protein, DUF1476 domain [Function unknown]
MTTFDDRERAFEAKFAHDEELRFKAEARRNKLLGLWAAELLGLTGDEAEAYAKEVVAADFEEAGDEDVFR
KVRADLAAAGVDASEAEIRAKMAELLAEARAQVKAE
>gnl|CDD|444219 COG5468, COG5468, Predicted lipoprotein involved in lipopolysaccharide assembly [Function unknown]
MSSRRRLLLLALALLAALLLAGCGFRPLYGPGGAGGGVAAALASVEVAPIDDRLGQLLRNALIFRLGGGG
GPAPPRYRLDVTLSESRESLGITSDGTATRYRLTGTATYTLTDAATGKVVASGTATAFASYDRSSQRFAT
LRAERDAEERAARELADQIRTRLAAYFARKPA
>gnl|CDD|444220 COG5469, COG5469, Predicted metal-binding protein [Function unknown]
MMAKHTLFVCTTCRRSGDDREGMGPRPGAQLLEALRAAAAAWGLPEGVEIQPVECLSACSRPCTVALSAP
GKWTYLFGDLDPDEDAEDLLEFAALYAASEDGLVPWRERPEGLRKGILARIPPLPIVT
>gnl|CDD|444221 COG5470, COG5470, Uncharacterized conserved protein, DUF1330 family [Function unknown]
PAYWIARVDVTDPEAYAEYAAAAAPALAKHGGRFLVRGGAPEVLEGEWPPDRVVVIEFPSMEAARAWYNS
PEYQAAKALRQAAAEGDLIIVEGVD
>gnl|CDD|444222 COG5471, COG5471, Predicted phage recombinase, RecA/RadA family [Mobilome: prophages, transposons]
MKNYVQPGDTITLTAPAAVASGDVVLVGDLFGVAATDIAAGETGELVTEGVFELPKASGDAIAVGAKVYW
DATAKVVTTTATGNTLIGVAVAAAAAGSTTVRVRLNG
>gnl|CDD|444223 COG5472, COG5472, Predicted small integral membrane protein [Function unknown]
MMTIRLSKILLVLAIALFALLVAFNNITDYGTNFQFVQHVLSMDTTFPGNALMYRAITSPALHHAAYILI
IALETLAGLLCLIGAIKLLRARKASAAAFNRAKAWAIAGLTLGFLVWFFGFMVIGGEWFLMWQSKTWNGQ
EGAFRFFVTILLVLIYLNQPDEELA
>gnl|CDD|444224 COG5473, COG5473, Uncharacterized membrane protein [Function unknown]
MTDTHASAAASPAPLPEVRRVTLADPLDWLAAGWRDFRAAPGISLFYGLIFALIGLLLLLVLLAAGLPPL
LFPLAAGFLLVGPFLAVGLYEVSRRLERGEPPSLGDALAVWRRNLGQLALLGLVLLLLFLAWLRAAALLF
ALFFGGGPPSLSGFLAAVFLTPEGLTFLAVGTLVGAVFAALVFAISVVSIPLLLDRDVDAVTAMITSVRA
VLANPVPMLLWAALIAALTLLGMLPLFLGLIVVLPVLGHATWHAYRDLVAPEA
>gnl|CDD|444225 COG5474, CRR6, NAD(P)H dehydrogenase cyanobacteria/chloroplast-specific assembly factor CRR6 [Energy production and conversion]
MTITIALNADQINSLDLSPAQTVIEPLLAEGAIASYEQQLRFEIDYPREPDDPRELSEIPEVRLWFIRLD
ALYPWLPFLLDWKAGELARYTAMLVPHQFSRTEGIQYNPEALEIFVMHKIFVLSDWLKQQGIPSQSRLKS
MAQMLGYELDDEFFELL
>gnl|CDD|444226 COG5475, YodC, Uncharacterized conserved protein YodC, DUF2158 family [Function unknown]
KMKFKVGDVVQLKSGGPAMTVTGVLDSGMVECVWFDGGELQREAFPEDTLEKV
>gnl|CDD|444227 COG5476, COG5476, Microcystin degradation protein MlrC, contains DUF1485 domain [General function prediction only]
IAVAGFQHETNTFSPVPTTLEDFEAGGLLRGDAILEALRGTNTEIGGFIDAAEAAGWELVPTLWARATPS
GPVTRDAFERLKAEILEALRAALPLDGVLLDLHGAMVTEGLDDGEGELLARVRAVVGPDVPIAASLDLHA
NVTPRMVDAADALVAYRTYPHVDMAETGRRAARLLARALRGGIRPAMAWRRLPMLIPIERQSTDDEPMAS
LYALARALEAEPGVLSVSVFAGFPYADVPEAGPSVVVVTDGDQAAAEAAADELAAAIWAAREDFVFDLPP
PDEAVARALAAAAGGPVVLADTGDNPGGGGPGDTTGLLRALLAAGAEGAAFGLICDPEAVAAAHAAGVGA
TVTLSLGGKTDDLGGAPLEVTGTVEALSDGRFVATGPMYGGQRFDLGPTAVLRIGGVDVVVTSRRAQPFD
LAQFRSVGIDPERYRILVVKSSVHFRAAFEPIAAAIIVVDSPGPTTADPARLPFRRLRRPIYPLD
>gnl|CDD|444228 COG5477, COG5477, Predicted small integral membrane protein [Function unknown]
MSWMAWTLPTALFFIGIALLLAGMTVWEIKSPGVERKGFLPIETTRGDRLFISLLGSAYIHLAWLGLTGP
PLWIALGLSLVWAAAVFRWG
>gnl|CDD|444229 COG5478, Fet4, Low affinity Fe/Cu permease [Inorganic ion transport and metabolism]
MRAPSDSSTMRDLFDRFATAVARAAGSPWAFLLAVAVVVVWAVSGPFFGFSDTWQLVINTGTTIVTFLMV
FLIQNTQNRDTAALQLKLDELIRALKGARNRLIDIEDLTEEELEELRAEYEALAELAREERAARASHSEA
>gnl|CDD|444230 COG5479, Psp3, LGFP repeat-containing protein, may be involved in cell wall binding [Cell wall/membrane/envelope biogenesis]
LLGVPWTDEADVPGRAQDFGWSPATGAHAVRGAILAKYLALGGPRGLLGYPTTDELATPDGGGRYQRFQN
GSIYWSPATGAHAVVGAIRAKWGALGWESGPLGYPTTDEVPTPGGGRYQTFQGGSVYWTAGTGAHAVHGA
IRGKYAYHGWEDGPLGYPTSDEKATPDGGGRYQIFEGGGIYWSPATGAHAVRGFIRGAWAALGWELGRLG
YPTSDEYLVSGGRRQDFQGGTITWAAATGAVRARAA
>gnl|CDD|444231 COG5480, COG5480, Uncharacterized membrane protein [Function unknown]
MKGFDRRLGAAAALLALLAALLLLAAPAPAAADFRVCNRTSSVVGVAIGYKDGEGWTSEGWWRIEPGSCE
TVLRGPLSARYYYLYAEDYDGGGEWGGDTFMCVREKEFTIRGAEDCLARGYERTGFFEVDTGEQKSWTVQ
LT
>gnl|CDD|444232 COG5481, COG5481, Uncharacterized conserved protein, DUF465 domain [Function unknown]
MNDDDEEELRARLAELRQEHRDLDAAIDALAATGPADQLQLQRLKKRKLALKDRIARLEDQLIPDIIA
>gnl|CDD|444233 COG5482, COG5482, Uncharacterized conserved protein, DUF2161 domain [Function unknown]
MKMRETDLYAPVKAFLEAQGYEVKGEVGGCDLVAVRGDEPPVIVELKLSFNLELLLQAVDRQALTDEVYI
AVPRPKGGKGRRALKDNRHLCRRLGLGLITVRLADGRVEVLCDPGPYAPRKSKKRRSRLLREFRRRRGDP
NVGGSTRTKIMTAYRQDALRCAAALAEHGPSRPADLKAATGVPKATRILRDNHYGWFERVERGIYALTEA
GRAALERWPEVLEYYAE
>gnl|CDD|444234 COG5483, COG5483, Uncharacterized conserved protein, DUF488 family [Function unknown]
MTLFTIGHSTRSLEEFLALLKAAGVTVLVDVRSNPGSRKNPGFNKEALAAALAEAGIEYVHLPELGGRRE
GRKAYKKSPNGCWRNESFRDYADYMLTPEFRRGLEELLELAAGRRIALMCSEADPWRCHRRLVADYLVAR
GVEVVHI
>gnl|CDD|444235 COG5484, YjcR, Uncharacterized conserved protein YjcR, contains N-terminal HTH domain [Function unknown]
MTTTTSKYSDEPRRQAKLLYWKGWRVAEIAEELGLKARTVYSWKERDNWDDLLPVERVEEAIERRLILLI
AKENKTDADYKEIDLLIRQLERLARIKKYENGGNEADLNPNVANRNKGKRKKPVKNDISEETIEDLEEAF
LDGLFDYQKHWYEAGLKHRIRNILKSRQIGATYYFAREALEDAILTGRNQIFLSASKAQAHVFRSYIIAF
AREAFGVELKGDPIVLSNGAELYFLGTNSRTAQSYHGNLYIDEYFWIPNFQELRKVASGMATHKKWRKTY
FSTPSSKTHEAYPFWSGELFNKGRAKRDRVDFDVSHEALKGGRLCPDGQWRQIVTIEDAIAGGCDLFDID
ELRLEYSPDEFFNLLMCEFVDDDASVFFFSELQRCMVDSWEVWDDDPPPAARPPGGEPVWGGYDPASRDD
DSAVVVVAPPPAPGGKFRLLLELWRGGNDFEQAAAIIKKFKQRYNVVYIIIDTGGGGGVVVLLVQQFFPP
APAIIYYVEEKNRLVLKKADVIIKGRLEEDEGDKDIAAAFMAIIRTTTTSGGSGTTYAARATETGHAADA
AAAAHALINEPLEPGTKANSSSMEIK
>gnl|CDD|444236 COG5485, COG5485, Predicted ester cyclase [General function prediction only]
LVRRFFEEAWNEGDLDALDELVAPDFVYHGPLPGEPRGPEGFRAFLRGLRAAFPDLRFEIEDLIAEGDRV
AVRWTFTGTHTGEFLGIPPTGKRVEFRGIDIYRFEDGKIVEEWVVEDLLGLLQQLGALPP
>gnl|CDD|444237 COG5486, COG5486, Predicted metal-binding membrane protein [Function unknown]
MTRLRLLVVAALLALALLAWAYLLAMAAMMLAGGPWSLAAAALFLLMWAVMMAAMMLPSAAPMLLLYARL
LRARRRRGGAATALFLAGYLLVWLLFGLLATLLQWALAAAALLSPMMASASPLLAGLVLLAAGLYQFTPL
KRRCLSRCRSPLGFLLSHWRRGARGALRMGLRHGLYCVGCCWALMLLLFVVGVMNLLWMALLALLVLAEK
LLPWGRRLARALGVVLIVAGLALL
>gnl|CDD|444238 COG5487, YtjA, Uncharacterized membrane protein YtjA, UPF0391 family [Function unknown]
MLRWALIFLVIALIAGVLGFGGIAGAAAGIAKILFFIFLVLFVVSLVAGLLRGR
>gnl|CDD|444239 COG5488, COG5488, Uncharacterized membrane protein [Function unknown]
MPYRWTVSPGEEPPLFEAVLRPNRSLSPRGFVILMAALAAVSLLIALAFLLLGAWPVLPFAGLELLLLWL
AFRRNYRHARDREVITLTPDRLRVERVDPRGRRQEWEFNPYWVRVELEEHDGPGPSRLTLSSRGREVEIG
RFLSPDERRALADELRRALRRARRGR
>gnl|CDD|444240 COG5489, COG5489, Uncharacterized conserved protein, DUF736 family [Function unknown]
MAQIGTFTRTENGFTGRIRTLTLDAKITLVPNESKDNENAPDYRVLAGGDGVEIGAAWKRTSEEGGEYLS
VKLDDPSFPAPIRANLFRAPDDGGSWVLIWSRPRKRD
>gnl|CDD|444241 COG5490, Phasin, Predicted polyhydroxyalkanoate (PHA)-binding protein, phasin family [Function unknown]
MATATAAFPFFEFPEAMRDFAEKGVEQARKAYEEFKAAAKKNLEALEASAKTAAKGAQAIARKAAEYAKK
NFEAAFAAAQKLAGAKSPQEAVELQSEFARSQFEAAVAQAKELGELAAKLAKEAFKPLKARVSKAVEEAK
AAA
>gnl|CDD|444242 COG5491, Did4, Archaeal cell division protein CdvB, Snf7/Vps24/ESCRT-III family [Cell cycle control, cell division, chromosome partitioning]
MFSKKWNKQSKPSIGDKIKGAVKPKGPLKPRIEEAIYKLQTQINRLDEMIRKLKERDRELFEKVVEAQQE
GDTARAKIYANELAEIRKMSKMLSTAKLALEQVQLRLETVSDLGDVVVTLGPVMGVLKELKSSLKGIMPE
LALELGEISESLGSIMVESGIGTGSTIDPATADEEARKILEEASAVAEQRMKEKFPELPSS
>gnl|CDD|444243 COG5492, YjdB, Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only]
TVSADTLTGLGKGVLTVTAVNTGDNDSTAGVTSSSVTANLSVLASNDTSTTSSVASVVSTAGSGGTANTS
STVAVSGAALAAGAVSTVGVDATTVAQTVATASLEAGGVSSTGTGTATTETVGTAATADAQIVKAASTGS
GSVTAAVAVGSVGVASAGTSVTTTVATATSASLVSTLVVTSVGLTTASGSLNTVVVTSVVGNGATDASTA
SAVVAAVTAVTSAGSLTSAASVTTAGDDGTGVVATTVTTTISTSSSTTLTVTGATSSASTLGSGSTTSTN
TVTAGVGDTGVSVAVASSSAATTSAVVGTLSSSGGGGGVVTAAATTGVTVVTASSVATTVDVVPVTGVTL
NPTSVTLAVGQTLTLTATVTPANATNKNVTWSSSDPSVATVDSNGLVTAVAAGTATITATTKDGGKTATC
TVTVTAAGSTGTVVVVSLAATSAVSASVVLTPAGTVNAGASTASLNVNATDGVSTTVGVANVVSAVTVTA
SVAEVATSVGGGATVTVTVSTAATVTVTVGVKSTGIAVAGSTGILAGIVLSGSAKGDVAGGATLVDAGTA
DVGGTTSTTTSVTDASVVSLTGSTSSTGVGVGGTTATGTAVAALVTGTGATVV
>gnl|CDD|444244 COG5493, COG5493, Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only]
MSLLKEELKRELLELLREDPEFRYAVLGLLATKDGLEELLERLEKLEEQMRKWEEQLRKLEEEIKKLREQ
VRKLEEDVKRLEEQERKLEEAMAEHSELREELMKLIKRLERSIGALGARWGIDSEEAFREALKGILEEGL
GGVKVEKWIYYDDEGYVYGRPSIVELDVVVKDGKLILVEIKSSVSRGDVYIFERKAELYEKVHGRKADRL
IVVTPMIDDRALELAKELGIEVITGSVIE
>gnl|CDD|444245 COG5494, COG5494, Predicted thioredoxin/glutaredoxin [Posttranslational modification, protein turnover, chaperones]
MMEVEIFVHPTCATSHELIRGLREKGLLDRVKIVDTELPPFLALERGVWSVPWIFVDGELVAADPVDPEE
VEAILRGEVGGKIDKSEPVEAFMEGVLHSFAASAWLYLNGSLDPVLADKDFVMAATRLPLSGDDEYNELR
NEIVKRGRELFEEWEDKMLRALAINFVRELYWLYGGKLSKEELLSLYPLEVVAHWLLAKGSVGRVGLPIH
PLGEDMERIEEVYSFVSKTADGLLRKVEKEQEEILGDEEYWEIVRELSG
>gnl|CDD|444246 COG5495, COG5495, Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only]
MARMKIGIIGAGRVGTALAAALRAAGHEVVGVYSRSPASAERAAALLGAVPALDLEELAAEADLVLLAVP
DDAIAEVAAGLAAAGALRPGQLVVHTSGALGSDVLAPAARAGALTGSFHPLQTFSGPREDLERLAGIPFA
IEGDEEALPVLEALAEALGGEPFVIDSEQRPLYHAAAVFASNFLVTLVALAAELLEAAGLEDAFDALLPL
IRETLDNILELGPAAALTGPAARGDAGTVAKHLAALAELDPELAELYRALSRSTLELAGKKGLLAAEELL
ELLEEE
>gnl|CDD|444247 COG5496, COG5496, Predicted thioesterase [General function prediction only]
ELKPGLTATFEFTVTEEDTAAALGSGDVPVLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAP
TPVGMTVTVTAELTEVDGRRLTFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAAEKAAK
>gnl|CDD|444248 COG5497, COG5497, Predicted secreted protein [Function unknown]
MTMLSLRSLLVALALAAAASPAAAGDAAELRILGFSADGRYFAFEEYGVQDGSGFPYANIFVIDLATDKW
VPGSPFRVRLDDEAATLAAARAEARARAAPLLSDLELTDNPGVLLAFNPVTELGADPHTITFNIRPPGPP
IDEPLTLRLEEIPLPATEECEGFGEEAKGFRLTLVEEEGGETTRLHEDQRIPASRGCPLGYRIAGVVTFF
PSDGDPVAVVLISVRSPGFEGPDRRFIAVPGRL
>gnl|CDD|444249 COG5498, Acf2, Endoglucanase Acf2 [Carbohydrate transport and metabolism]
MKRTALTLLALALAAGLLSAAAPAAATVAVGAGSYTLPAGIKNGAPLTPQRLADATGLPPPTNRWWSSLV
FGREPYSEPVFPHPLSFKATADGLAVGYPTTPDITGDGTTIEYMGGHSPDLTVGVSGLNAPDARVDDYSD
WSVTAYWSDGGRVLRATIGHGSPFVYFTASGGDATINTAAAPTVFSNSGNVLGVTVNGHHYGLFAPSGTS
WSGVGTTLTVTLAGGGYFSVAVLPDGSAATLAAFATYAYAFVTGTRVSYSYDEATATVTTTYTYTTTAKE
GTAGGTLVALYPHQWKNTDAALTGYTYRSPRGTMKVVAGTSFTTTMPFVGVLPALPDVGSYDRARLATYL
DADVAQADNWNGATDTYWGGKALGRLAQLAPIADQLGDTAARDELLGRLKAELEDWFTADGGRTSRCFYY
DDNWGTLIGYPASFGSDTELNDHHFHYGYFVYAAAVLARYDPSWASDSQWGPMVNLLIRDIANPDRNDPR
FPFLRNFDPYAGHSWASGHAPFADGNNQESSSEAMNAWAALILWGEATGNTELRDLGIYLYTTEAAAIEE
YWFDVDGDNFPAGFDHPTVGMVWGGGGDYATWFSAEPEAILGINLLPITPGSLYLGYDPDYIAANYAELV
GENGGPDTQWRDILWMYQALADPDAALAAFNAVAGLYEPEDGESRAHTYHWIHNLASLGRVDVTADTPTA
AVFVKNGARTYTANNITTYAATVTFSSGTTLTVPAGTTATSTGGGTGGGTSGGGPTGDTNDGTGTSGSDS
TSTTGVSATVGDLDGGDTVTAASVADGGNSTYTPTLSLTVTITSATGTNDPAAGGVTATGGAVDLGGTAT
AGATTTYLTPSSTDGSGDTVSGVATSTTSGA
>gnl|CDD|444250 COG5499, HigA, Antitoxin component HigA of the HigAB toxin-antitoxin module, contains an N-terminal HTH domain [Defense mechanisms]
MTATFNAAPPLKPIRTEADYEAALALIEELLDADELGTPEGDLLDLLATLIEAYEAKHYPIPPPDPIEAL
KFLMEQHGLTQKDLAPEIGSKSRVSEILNGKRSLTLEMIRKLAERFGIPAELFIQPY
>gnl|CDD|444251 COG5500, COG5500, Uncharacterized membrane protein [Function unknown]
MLLTALLLLAALGTGLVAGVFFAFSTFVMPGLARLPDAQGIAAMQAINRAILNPVFMLAFFGTALLSLVL
AVLALLGWGGPGAWWLLAGALLYLVGVFGVTIAGNVPLNDALAAVDPSSAEAAALWARFESRWTRWNHVR
TVASLAAAALLAIALLLA
>gnl|CDD|444252 COG5501, SoxY, Sulfur oxidation protein SoxY [Function unknown]
MTRRTFLKGGAAAAALALLAPAPALAAKDAFEAKSWDDAIKALFGGAAIAESGRVKLTAPEIAENGAVVP
VTVDVDLPGVESIAILADKNPTPLVATFHFGPLAGLAYVSTRIRLAQTSDVRAVAKTADGKLYVASKEVK
VTIGGCGG
>gnl|CDD|444253 COG5502, COG5502, Uncharacterized conserved protein, DUF2267 family [Function unknown]
VFDHAAQKYDEFLDEVADRAGLPDREQAYRATRAVLHTLRDRLTVEEAADLAAQLPPELRGILVEGWRPS
EPPERFDRDEFLARVAERLGVDPEDAERAIRAVFAALREAVSEGEIEDVLAQLPEELRALWEP
>gnl|CDD|444254 COG5503, RpoEps, DNA-dependent RNA polymerase auxiliary subunit epsilon [Transcription, Defense mechanisms]. DNA-dependent RNA polymerase auxiliary subunit epsilon is part of the Pathway/BioSystem: RNA polymerase
MIFKVFYQENKDEVPVRENTKSLYVEAESEREVRKKLEDNTYNIEFIQPLSGAHLEYEKQSEDFKLEEF
>gnl|CDD|444255 COG5504, YjaZ, Predicted Zn-dependent protease YjaZ, DUF2268 family [General function prediction only]
MTVIDTYKWLLEYLEAPVEDREDLLRERLLEPFKKPGKEDIQAHLLQHGLFRPIERLEEALEKLKEDDIW
QRIEEALEKLKEVLPGPDVPIFVLPGDPENRFLMEELKGKSGLAGIPGKIFLFLDPDYTEERLKALLAHE
YHHVVRLEGPDWDPEGVTLLEALISEGLAEAFARELYGEESLGPWTTSLSDETLEEVWERIKENLDSTGY
DEHAAYLYGDKPVGLPRWAGYAVGYRIVESYLEKTPLSIAELTLLPAEEILEGSGYFEG
>gnl|CDD|444256 COG5505, COG5505, Uncharacterized membrane protein YjcL [Function unknown]
MTPLITNDAVVLALLMLILALVFYLEQKKKKKFYKKVPGLLLCYFLPALLSNLGIIPAESSPLYDVVSRY
LLPAALVLLLLSIDLKKILKLGGKALIMFLAGTLGIVIGGPVAFLLLKSFIPEDLWKGAAMLAGSWIGGG
ANFAAMAEAFGVPGELFSAAVVVDNVVAALWMAVLLALPGKAKKFDKWLKADTSAIDELKEKVEAYWAED
RKIPSLKDLALLLALAFGVVAVSHFLADLLPPFIPSNFSSLTSKFFWTILIATTIGLLLAFTPVRKLAGA
SELGTVLIYIFVATIGMKADITALLDNPPLFLFGLIWMAIHALLLLIVAKLFKAPLFFLAVASQANIGGA
ASAPAVAAAFHPSLAPVGVLLGVLGYAIGTYGGLLVGQLLRLLA
>gnl|CDD|444257 COG5506, YueI, Uncharacterized conserved protein YueI, DUF2278 family [Function unknown]
MAKKDLEDYLLEGIYGAPELKPDEQRRYLGTFRERVVLALTKEQVEEPKGYKELEEALKDHPALKLLING
NLDLDFQKPYIKLANKYGISFTIVDNPDAKSDIGLVVVSDHAVNKEDIDVEERYPKLKEKGKSEKIIYKK
LSFWKKLFGTK
>gnl|CDD|444258 COG5507, YbaA, Uncharacterized conserved protein YbaA, DUF1428 family [Function unknown]
MSYVDGFVLPVPKANKEAYRAMARKAAAVFKEHGALRVVECWGDDVPDGKVTSFPRAVKAKDDETVVFSW
IEWPSKATRDAGNAKVMADPRMQPLPEEMPFDGKRMIYGGFEPLVDL
>gnl|CDD|444259 COG5508, COG5508, Uncharacterized conserved protein, DUF1674 domain [Function unknown]
DNTPAPAKPLPPAAQRALAEAEARRAAAEADAELPKEIGGRDGPEPTRYGDWEKKGRAIDF
>gnl|CDD|444260 COG5509, COG5509, Uncharacterized small protein, DUF1192 family [Function unknown]
MDDDDEPRPKPAAHLIGEDLSLLSVDELEERIALLEAEIARLEAEIAAKQASRAAAEALFKK
>gnl|CDD|444261 COG5510, COG5510, Predicted small secreted protein [Function unknown]
MKKLILLLLLLLLALLLAGCNTVKGAGEDIESGGEAIEDAAEKVQ
>gnl|CDD|444262 COG5511, COG5511, Phage portal protein [Mobilome: prophages, transposons]. May form a hole, or portal, that enables DNA passage during packaging and ejection, and also form the junction between the phage head (capsid) and the tail proteins
MSRLLDRAIGYFSPAAAARRVAARAALPNSRRAYDAASTGRRLAGWRPPNRSADADILPALDTLRARARD
LVRNNPIAAGAVDTLVDNVVGTGIRLQARPDARDGEEAEELRRAVEALWREWAESPECDATGRLDFYGLQ
RLALRTWLEDGEVLARLRWRPRDGLPVPLQLQLLEPDRLDNPKNLADGNRIRQGVEFDADGRPVAYWVYR
RHPGDGFLGSASSLEWVRVPAEEVLHLFEPERPGQVRGVPWLAPVLERLRDLDDYEDAELVAAKIAACFA
AFIKSPDPTEEAPDALGGGVDEADGDRPVELEPGMIPVLPPGEDIKFSDPARPGGNYEAFVKAQLRAIAA
GLGVPYEQLTGDYSGVNYSSARAALLEFWRTFERRQEWLVAQFCQPIYEAWLEEAVLSGLIPLPAGFYDN
RAAYLRAEWIGPGRGWIDPLKEAQAALLAIRAGLSTLSEEIAERGYDPEEVDRQRARERARARELGLPFD
SDPAAAAASGDTSDEPEDEGDE
>gnl|CDD|444263 COG5512, COG5512, Predicted nucleic acid-binding protein, contains Zn-ribbon domain (includes truncated derivatives) [General function prediction only]
DPQSLGSLLGRLVKQRGWEEQLAVGRVLGRWPEIVGPEVAAHTRPVSIEDGVLTVAASSTAWATQLRLLR
PQLLAKLNEELGEGVVTDIRFSGPAAPSWRKGPRSVRGRGPRDTYG
>gnl|CDD|444264 COG5513, ICP, Chagasin-like inhibitor of cysteine peptidase, I42 family [Posttranslational modification, protein turnover, chaperones]
MKKSLLLAGCASQGAADNGTTVELKVGDTFVIRLPENPTTGYSWELTSSDGSVLRLVGDEYVPPDPSGAV
GAGGTHVWTFKAVKAGETTISLVYRRPWEKETGPEKTFTLTVTVE
>gnl|CDD|444265 COG5514, COG5514, Uncharacterized conserved protein, DUF1794 domain [Function unknown]
EDIYTEPEPVDPDTLANLGPLTPLAGIWEGDRGVDVNPKADGPERQAYIERIELQPIDPQTNGPQLLYGL
RYHTHITKPGEVETFHDQVGYWLWEPATGLVIQTLAIPRGQVAMAGGKAAPDDRTFTLTATRGDPTYGIC
SNPFLEEAFRTESYTITVTFHDDGTWSYEQDTVLRIAGTDEPFHHTDRNTLRRVAEPTPN
>gnl|CDD|444266 COG5515, COG5515, Uncharacterized conserved protein, DUF1737 domain [Function unknown]
MKLYRLLTGPDDSAFCHRVTEALNKGWELYGSPTYTFDAARGVMICGQAVVKEVDGLTYSPDMKLGEY
>gnl|CDD|444267 COG5516, COG5516, Uncharacterized conserved protein containing a Zn-ribbon-like motif, possibly RNA-binding [General function prediction only]
MLFAPPAFDFDGGRLALDLVNTVDARGGRPVDRLATPADLAAWLRAAGLLGRPAATAADLAAARALREAL
RALFAAAARGDPPPAEAVAALNALLARAPARPRLTRHPDGRLRWHLHARRPAPLAERLLAELAAAAADLL
TGGDLDRLRVCAAPDCRLVFVDTSRNGSRRWCSMAVCGNRAKVAAHRARRRAA
>gnl|CDD|444268 COG5517, HcaF, 3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites biosynthesis, transport and catabolism]
AAVDLELRAEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPARENRDTDPGLPLSLIYDDRAMLEDRV
ARLRTGNAWAEDPPSRTRHLVSNVRVEETDGGEIEVRSNFLVYRTRRDGQTDLFVGRYEDRLRRTGGGLR
IARRRVVLDNSVIPTKNLSYPL
>gnl|CDD|444269 COG5518, COG5518, Phage capsid portal protein XkdE [Mobilome: prophages, transposons]
MSKKKGQPKAQTEAFSFGDPEPVLDRRDLLDYLECANNGRWYEPPVSLDGLAKLFRANVHHSSALYFKRN
ILASTFIPHPLLSRQDFSRLALDYLVFGNAYLEKRRNRLGQVLKLRHLPAKYMRRGKDLGTYWFVQNWGE
PHEFPPGSVIHLKEPDINQEIYGLPEYLSALQSALLNESATLFRRRYYKNGSHAGFILYTTDANLNEEDV
DALREALRSSKGPGNFRNLFVYAPNGKKDGIQIIPVSEVAAKDEFENIKNVTRDDVLAAHRVPPQLMGII
PQNTGGFGDVEKAARVFARNELEPLQERFLEINDWLGEEVIRFKPYALLPPAP
>gnl|CDD|444270 COG5519, COG5519, Predicted ATPase domain of Cch-like helicases, DUF927 family [General function prediction only]
IALAMAARPSAAFADLAAEAGKDPEESAPAALLAAAALAVADVKKDKSDVLAKDGDDQDNQLTTKLAAEA
EATTTDTGAQASDLEDQSAQEIPLPERERPVGAGGELRRELLAKGLTITTNRKARALLADYLQRSGPKRR
ARCVTRTGWHGGAFVLPDEVIGTPEEPVIFQGRSAAAAGYAVAGTLEDWREEVAALAVGNSRLMLALSAA
FAGPLLELLGAEGGGFHLYGDSSTGKTTALNVAASVWGGPDGFRRTWRATANGLEGEAAAHNDGLLALDE
IGQADPKEAGQIAYMLANGQGKARATKDGGARAVARWRTLFLSTGEVSLETHMAEAGKRTKAGQEVRLLD
IPADAGKHGAFENLHGFTDGAALADALKRAAAQHYGHAGRAFLEYLTKDRQDLAELLRELKDRFLALLLP
ADASGQVRRVAERFALVAAAGELATEAGITGWPEGEALDAAQECFNAWLAARGGGNKEDRQALEQVRAFI
ERHGDSRFADWDDDDQDPRVRDRAGYRRVEDEDGGREYLVLPEGFKKEICKGFDPKRAARVLAEAGWLKP
GKDGKRTRKRRLPGRGGVRVYVVRPDVLGGEE
>gnl|CDD|444271 COG5520, XynC, O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis]
LPACAAATVEVWLTTADGSLLLAKQAPAFFAQPASAEPTITVDPDKTYQTIDGFGASFTESSAELLGKLS
AAKRNELLKELFSPEKGIGLSLLRTPIGASDFSLGSYSYDDVPDGDPDLGHFSIARDKKYLIPFLKEALA
INPDLKIMASPWSPPAWMKTNGSMNGGSLKPEYYDAYADYFVKYIQAYKKEGIPIDALTPQNEPLAPQNW
PSCLMTAEEQADFIKNYLGPALEKAGLDTKILAYDHNRDYKPDYPITILSDPEAAKYVDGIAFHWYGGDI
SALSRVHEAFPDKNLYFTEGCGGGWDGDWDGALHYANLIIGDLRNWAKGWLDWNLALDENGGPNHGGYCN
GLVTIDTKTGEVTYNPEYYAIGHFSKFVRPGAVRIGSTSSDGGLENVAFKNPDGSIVLVVLNTSDEAQTF
NLKLGGKSFTYTLPARSVATFVWKG
>gnl|CDD|444272 COG5521, YvdJ, Maltodextrin utilization protein YvdJ (function unknown) [Carbohydrate transport and metabolism]
MKKKPFPIRYFKSIFSPRRMFAGRKQFSWWQLIFLFIFLNALLMFPIALHFSSMTTFNLSLIMPSVIQLL
TDKFAQALQGGTIKNGTLTDTDTVVIEKTQNVVAVDLTDEKQEGYKNAIIFQKNELVITDQNGYGFSVSY
PKDQTLSDLTDRDSLKEFINAQWYQQNKPYIILFLLLLAGLALVVSNLILTLVAAFFIWLTKRSKLSSIR
SFKESLNIVVNALGLPSLAALIIGLIHFDFTLMMTVQSLGLVLMVSWVFYKTHFRDPNLKSKSASK
>gnl|CDD|444273 COG5522, YwaF, Uncharacterized membrane protein YwaF [Function unknown]
MEYFFSLYEAEEPFTLFSPSHLIALAIFALGAILLVLLRRRLRDTRARRKLRRLLALLLLISEVGLQIWY
ILNGNWSLEDSLPLHLCDIALILAAIALITRSRWLFEITYFWGITGAIQALLTPDLSYGFPHFRFIQFFI
GHGLIVLAALYLTFVLGYRPTWRSLRKSVIVLLIYALLIFIVNNLLGTNYMFLNGKPSTASLLDLLGPWP
WYLIVLELLALLVFLLLYLPFRLRDRRKKKLREI
>gnl|CDD|444274 COG5523, COG5523, Uncharacterized membrane protein [Function unknown]
MKSRSELKAEAKEALKGNWGLAVLATLLYSIISGLLSIPYIGPILVLLILGPLTVGLAFFFLKLVRGEKA
SVKDLFSGFKKNFGKAFLAYLLMGIFVFLWSLLLIIPGIIKSYSYSQTYYILADNPELGAMEAIKESKKM
MKGNKWKLFLLDLSFIGWYILSILTFGIGLLWLIPYIETTFANFYRDLKKEKGDV
>gnl|CDD|444275 COG5524, COG5524, Bacteriorhodopsin [Energy production and conversion, Signal transduction mechanisms]
LVTTWFWLGAAGMLLGTLFFLALGRRVDPRYRLYYLVTALITLIAAVAYLGMALGWGAVEVPDGRFVYWA
RYIDWLLTTPLLLLELGLLAGASRRLLVTLVGADVLMIVTGLAGALSTGPARWLWGLLSTAAFLVILYLL
LGPLRRSAARQGGEVRSLFGKLRNLLVVLWLIYPIVWLLGPEGLGLLDVTIETVGYTYLDLLAKVGFGLL
LLRSARALSSADTEAASATAAPAD
>gnl|CDD|444276 COG5525, gpA1, Phage terminase, large subunit GpA [Mobilome: prophages, transposons]
ATYAAARAVLRAALEALRPPPRLTVSEWAERYRRLPAESSAEPGPWRTDRTPYQREIMDALSDPPIERVV
FVKSAQVGKTTLLLNWIGYFIHHDPGPMLVVQPTEEDARRFSKTRLEPMIRDSPELRERLAPPRSRDGDN
TLLSKRFPGGSLLLIGANSPAGLRSKSARYVLLDEVDRFPEDIGGEGDPVTLAEKRTTTFSRRKILLGST
PTIKGTSRIERAYERSDQRRFYVPCPHCGEEQELTWENLKWDKDPEAPETAHYVCPHCGCVIEEHHKRAM
VRAGRWVAEAPDGRSGHAGFHLNGLYSPFQTWEDLVREFLDAKGDPEKLKTFVNTDLGEPYEEKGEAPDW
ERLRARAEDYPLGTVPAGVLFLTAGVDVQGDRLEVQVVGWGRGGESWLIDRGVIDGDPDDEEVWAELDAV
LKRTWRHADGGELGIDAVAIDSGGYVTDAVYAFVRRRGGRRVFAIKGDSGRGAPLIGKPKPVDTTRGGRR
GVRLYIVGVDTAKDELYARLRREEPGPGYVHFPDDLDDEYFDQLTAERRVTKYRRGKPVREWEKLPGRRN
EALDCRVYARAAARILGLDRITEWDALEARAPPALAATKPAEVAPAAAPEAATSAPEAPKLARRRRARAR
RSGWL
>gnl|CDD|444277 COG5526, COG5526, Lysozyme family protein [General function prediction only]
MSSMLLLEALKPEYEKLWASCQIRPERLGEVGRVADRILAGRDRYEAVERATGVPWYFIAVIHYRESSLD
FDTHLHNGDPLSARTVHVPAGRPTAGGPFFTWEESAIDALRLKGLHGAHDWSIAATLYRLERYNGFGYRA
PGVNSPYLWSGSNHYRKGKYVRDGVWDPNAVSKQCGAAAILKALMEEGD
>gnl|CDD|444278 COG5527, COG5527, Protein involved in initiation of plasmid replication [Mobilome: prophages, transposons]
SKKNLIVVKSNESGNAYERLKEALERLMKKMIEIEEEDGKKWEQFPLFSSAEYNKGEGTIELRFSPELKP
YLLDLKKNFTKYELENVLSLKSKYSIRLYELLKQYKDLGKREISIDELRELLGLEDKKYKRYGDFKRRVL
EPAIKEINEKTDLSVEYEEIKKGRKVVGIEFTIKKKKKSKLEKEPAENLLELKEEELEEYNEEEEVKKLD
LLLKEIEDLKKLLLEKELELELVKEKLAIEAKKKAKQLAKLAGEEILEE
>gnl|CDD|444279 COG5528, COG5528, Uncharacterized membrane protein [Function unknown]
MLYLLLKWLHILSATVLFGTGAGTAFFMLMADRTRDPAAIAVVARLVVLADWLFTAPAVILQPLTGLWLA
HLAGYPLTSPWLLWSLVLYVLAGACWLPVVWLQIRMRDLARAAAAAGAPLPPAYWRLFRIWFALGIPAFV
ALLAIFWLMVAKPVL
>gnl|CDD|444280 COG5529, ECs1768, Phage-encoded DNA-binding protein ECs1768, contains HTH and DnaT DNA-binding domains [Mobilome: prophages, transposons]
FSRQAALWGIALPELAAFRAHWQKHGKEFGSQQKLARYVQQARAFVNRPPRRDRGTLTKTRPNGDTLVYD
PDTNEFAVKSKDGVPRTMFKPDGFRGGLGYWNKQ
>gnl|CDD|444281 COG5530, COG5530, Uncharacterized membrane protein [Function unknown]
MADPEEPEDRVGAELPETSSEEISALAHLYRGEVYRSTTWRTRLDRTTNWAVTTTAAVLSFSFSSPDAPH
YVLLLGMLLVLLFLFIEARRYRYYDVWRARVRLLEENFFAPALDPEPGVEDPDWREELAEDYRRPTFKIS
LLEALGRRLRRNYLWLFLILLLAWLLKITAHPPPATSLAEWVERAAVGPIPGWVVLAVVALFYAALLALA
LWPSWRDRRAKGELRV
>gnl|CDD|444282 COG5531, Rsc6, DNA-binding SWIB/MDM2 domain [Chromatin structure and dynamics]
AKRKKNAAFMKPLTPSAELAAVVGAKPLPRTEVTKKVWDYIKKNNLQDPANKRNINADAKLKKVFGGKDQ
VSMFEMTKLVSKHLK
>gnl|CDD|444283 COG5532, yfdQ, Uncharacterized conserved protein YfdQ, DUF2303 family [Function unknown]
MSQTLLKSAISDIQDLAAALANEAIEETAVPAVPAAIVPDGFKLESLENLREGPRRFRGTFTTADLESFI
AYVNKHADEGTAIFIDADNMTAVAVFDYHTQDAPGWADHRASLKLPKTAEFQAWLAIDGKAMSQKEFAEF
LEDWIADLVAPTGAELLEIAQALQANRKVTIKSATRLDSGDTQFSYKESVMASAEAKGKLEMPEEFTFTL
RPFEGGEEYEIEARLRYRTDGGALVLWYRLVRPEAVEEDAANEFVDLLRAEFTGVPVFIGSFNA
>gnl|CDD|444284 COG5533, COG5533, Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]
GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLKNVIRKPEPDLNQEEALKLFTALWSSKEHKV
GWIPPMGSQEDAHELLGKLLDELKLDLVNSFTIRIFKTTKDKKKTSTGDWFDIIIELPDQTWVNNLKTLQ
EFIDNMEELVDDETGVKAKENEELEVQAKQEYEVSFVKLPKILTIQLKRFANLGGNQKIDTEVDEKFELP
VKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKKGGKWEKANDSDVTPVSEEEAINEKAKNAYLYF
YERI
>gnl|CDD|444285 COG5534, RepA, Plasmid replication initiator protein [Mobilome: prophages, transposons]
MSRRRLLPSRDPQLDLFVPDIGDAPPKDDRDLMEHPFFSLSKKPRTRPIRYEHGDVWIEVEASPEHGMAT
IWDADILIYAASQLVEAMNRGRPTSRTLRFTPYDLLKFTGRGTGGRDYERLKAALDRLQGTTIKTNIRTG
GERRRHGFSWINEWKEVSRTRDGRVLGVEITLPDWFYRAVLDDALVLTIDRDYFRLTGGLERRLYRLARK
HAGRQEAGWRFSLEHLHKKSGSLSPLKRFAFELRDIVARDPLPGYRLSLERGAGGDLLVFRPRDALSPVS
PPLDPLVLE
>gnl|CDD|227822 COG5535, RAD4, DNA repair protein RAD4 [DNA replication, recombination, and repair]
MKRDLENSYNDQARRKNSKIEKKNVSFKEEEEVDSSFDSFYQDEEKDIDEEPVELDGDLTVTVNNIRRDR
SKVSKYSDDHNEKLQSSQLHLIMIPFMLLKSRNKWIDDERLNRRLKRSVPKLGGKSFKDWSVRKSAHIMD
STCLLLLGFIRNLWFRSKMLSNGLRFNRLEKQIKYLDNQNESSISESTYKKLLEGLRFYGNKPFKNIGVE
DNRKLAKRTMKQMESSDFWEEIFENYSLEVVPLKSADGRRDADVRGFEAEHRILNVFARLIASLIQPVFS
NNSDLDVLSEGLLEYIDSLEYPGFWGEVVDKFEKKWVFVDPVRLYIVYSELKCKFEPAASIHLNIMEYVG
AYDACVYVKDVTLRYRDQSYSFLKRITKHLFSVQYFVRQFPGLGKCKEASDEEAIEDFDDLDERRSEGIP
KSVQDLKRHPKFVLESHLKWNQAIKPGAKPGFTLTKGKNSVEAVYLRRDVVRLKSAEQWYRMGRVIKPGA
QPLKIVKRMRERVRNLDDKVIRELYSPEQTELYGPPLVVAGIIPKNMYGNIDYYVPSMIPRGCVLIPNRN
ARDIARLLGIDYADAVTGFDFGRSTVKPVLRGIVVPKKNLEAISNFLAEYERIQEEKERSEVRLGGLKRW
KILLRKLRIRLRINEEYGLK
>gnl|CDD|227823 COG5536, BET4, Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, chaperones]
PEDLDLRRVKPLPIQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWN
YRFSILKHVQMVSEDKEHLLDNELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSD
SRNYHVWSYRRWVLRTIEDLFNFSDLKHELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGDVISQKYLE
KELEYIFDKIFTDPDNQSVWGYLRGVSSEFATDIVMIGEKVEDLGKYIVIINGKELDLGPKENLPCLHSL
LELEFLCHAEKALLTERDIEQKALVELAIKVDPARRNLYSTLHERFNC
>gnl|CDD|227824 COG5537, IRR1, Cohesin [Cell division and chromosome partitioning]
TGESEESSSEDDYEDQDDDDYVDTATAKRKSRSRKPMSKENSPDGVLAKDMSSDQKSVTPNLPGISGHGS
CPFDVFEPDALFSRLFFYELLDEDVIREILSVHWFEDYMKNLSKFLNSLINFDLSCCGCLTRVGNFDVQD
YDSTYETLGQIQLSILRGKGFEVVLYLYDENFKVRFRDVYQDFNIRALLVEFVSEWVVSVGIFNSSCYLD
YIGWALSMSNSTVRCFRHTATSCCRLIQKKLCVQAFSLSEKKSRMNELALYDLNPSLIRDEIKDICDSVF
VSRYIDVDDVIRVLCSMSLRDWIGLVPDYFRKILGLRYNGWSLSDNHEGVRLLVSKILLFLCSRIPHTDA
IRRFVERFKDRILEFLRTDSDCVRICSIKSLCYLRILGVLSSSEILIVSSCMLDIIPDSRENIVESVESI
CKIDAEVIKEKIPLATKTNRLLEAMKQGSERYFVVCEEIFSRFVHLLKKVELSFEASVYRITEIRRFFSN
GEFTCPIIKSFLISEGIGSIHPTEVKEDIAKLRLMDNSDYEDVNGYELKDTANPAVLCSFILFFREKCIE
FAVLNRPVERASDQVECFKVMYDRLSALIHSEAERCFVDPKFIISLFKLVDEGLYTDESNKIFKKCGKEL
IDIFNSRSKSRMNIVSGYFRHLMDVEEKNVQEGVLRLIGSKCGMLKKGLGEEKTVFRGRKALINKKQLFL
NDSVLIYFVSSLTFNECIIIEQGLEKSKLKASLLRRIRES
>gnl|CDD|227825 COG5538, SEC66, Endoplasmic reticulum translocation complex, subunit SEC66 [Cell motility and secretion]
MVSIYVPLIYLLILILSTVILMFTFRKRKNRKKAPGDEEWFSENLELEVYFLQKSENPGASSSTLKAALV
KRAAEFKRRVMKLKKDMEVLNTLYEDGMIGEEHWERFNEESKNCELERIDIESEANILQPGWGQEIFKDC
SEISENETIGPRKGKIPKDGTLYQKKWEVLELELDRKLGV
>gnl|CDD|227826 COG5539, COG5539, Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, chaperones]
RMKKKTQAAAETAMESLTEKQRFELKDLQTKITRIMKQLTFGRPPQRLNGKCLDLSYALSQKDEVEIEKA
PKLRAETNEADQEDSLTPLQNIPELGISSFEKSVSQQSINVLEDMPGQDDNSRLFQAERYSLRDASVAKL
REVVSLEVLSNPDLYNPAILEIDVIAYATWIVKPDSQGDGCIEIAIISDQLPVRIHVVDVDKDSEDRYNS
HPYVQRISILFTGIHFDEETLAMVLWDTYVNEVLFDASDGITIEIQQLASLLKNPHYYTNTASPSIKCNI
CGTGFVGEKDYYAHALATGHYNFGED
>gnl|CDD|227827 COG5540, COG5540, RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, chaperones]
MSYYQIIVCILASISYIILLEVIALDLGVLDNIFMPPRKAQSTDMARRLGNNNVLLWNIMRSMLKHLDTR
IASSDIDAYLTPSGVFMNRLRCRNLVDLISGYFGDGDDGREYDETRIPPPSRDLRGSGRKVRGSARQEVP
SVEERNLVDRCNRRGNETEEDPTRERRRTRFKGVIRGSERNGETFRLHYMVAPDKVDPRSEGVEDPVTLT
TSINVTWDGLGNTYQAPSQSAEAQDETGDMFWPRLSRFVGSRGFRVVFPRIPSQELRFLFLTQSKGSRFN
IILEIQINFDVGFYSSSEAIPTTTTKGSLKPLSIERAVEADKGVECAICMSNFIKNDRLRVLPCDHRFHV
GCVDKWLLGYSNKCPVCRTAIPPP
>gnl|CDD|227828 COG5541, RET3, Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, chaperones]
MNLSLYDVEALLILDSQGERIYRKYYQPPHRSEGHQLVFNSVKKEKEFEKKLAEKTAKDRESILMFYDRL
VMCKRLDDVLLYIVSPMEENEPFLGQVFDEIRAALILIVKTPTDKRNVWENYDQIVLLVDETIDEGVILE
TKSDEIADRVPKPPNFEGQDGMKVPRGFASFLHKATKKLSERSNKGL
>gnl|CDD|444286 COG5542, COG5542, Mannosyltransferase related to Gpi18 [Carbohydrate transport and metabolism]
FTAFLSPWYRAIATSGYFAALGKQFGDYFPLYPYLLRLVMYLGLPFLLAGKLVSILADLVAAYLLYRWVK
KYYGGNAALLAAAVLAFLPTVLLNSAIWGQTDSLYTLFSLAALYALLRGRYGWAALFFALATAFKPQAVF
LLPALLILLLKERIRLAYLLLAPVVYALALLPALLAGRPLLLLFSLYCNQAGEYPYLGFNAPNWYALL
>gnl|CDD|227830 COG5543, COG5543, Uncharacterized conserved protein [Function unknown]
MTTDVQFSSQEIELFRVKEFLIANNPAKINNENKDVLTQIEHDFRYLIYIKDGLPNLLRSPMDSCWDTKS
LFLLRLEIGNLHKIDYKEIMSMVLESGMEISCTNESGEEVRDFGHLGRYKEEEAKTDFFSKLLELQLGRC
PKEAVKDVLFNWMNHLLLLLSGADVASQLIIFLMFYKLAVKYKVYDPRFLHKSKTLLHLIHLARAVLKTI
IAYLLNRVDLVFNEFEGEEVMWMNLWCPKDLKYIHDKQPADPDSIRAVKRLFSSMPKASFRYSLRILKNK
DERFFVYLPDLKISTGYSILRELLGKLSPDRVRSIIKIVGDEYKLQSFARLFLPLKMSDPQRFFTFRSVE
VRIESLFHIDGVGLRRRFLESMQHFFIRSRSMLKSLARYFRKFPDEQLWLKEKVEEAHKFLTMYLEVIKP
MLRPTNAYQRVLGSLYLMDSLIAEGIDKSTPQKFLIQNKREFPFSAQLLFDSDHERLMIDLLVSNYADIR
KLSTKILLGLESMSESRGLFLDTLDANALKVKIESHQSHDVHGDAGATVYCVEFIKSCQSRSFVGHTKSI
LDSHMKNFVSGKKSMEEISIGPHFAALSLILGLFNSEENHQDTSKILSELIEHDIITWVDIVYVCCFDSL
SGVLPGQEDDCGVPDQVILSVYWRNMKECSSLLCGMLLKYPLTRGNLALSGRLVQVLLSHIRHLGAFLQV
SPYLNMVCKRCNMEFEEDELLELVKVSFNRIEKCKAITRRSGGIPLLFTSILRAEVTKYPSLLERTLKRL
LELAETPESSHQDEFDLPQVHALNILSRIFEEGCLSSKLPLQIEEAFGLAFKCFRSNLWAIRNCSIMLFT
NLVNRAFGRGPEGIVGMAHAGSRKLFFKKLSLLRDKLLDVLALSIAHLSGRMRESNGEESIFLVTEALWR
LSPRGGVTGLKSFNICTKKCWKMPNWKARPRASMVLNPLLSEGEVLLRVLILLDSEAVEQNGMHGSLLEN
VYGLSSYSSEYLKHYTVQRICEIGYQEAAAQRLRFYSLKIERSLSCFFLESPSNEDSDLKHAISLMRMYR
GQENNIYVVDGSKQLYLAQILDMLLKYEDSIYLDDICLLGLYSPFYEAQLSTLQYMNTNFHWETTRNSEF
LEQLQLLLRVPDLLPMAKALVVKILSRKKNTLSLTTCTDLLKTNNSEDTKLAAVSSLSAKLSSQTFHQVW
NLLQGFFADSCSKDFLASLECLTAYPESCKNSRILLQLYNFLWDDDSEIREKASFYLNKNFIQTADWEYN
RNTSVTALIFTKKFVDVFTSSEVVEELCLQLFQYLNEYAKNCLFTIEKDNQFINELQKAMHILNMIKLTS
KCYKDQIHHLKSALLEHFEDFKDSPLGWCSNAEIFSRITLLKELIQHYSPSYENFINVLTKHSVHPSYSQ
>gnl|CDD|444287 COG5544, yfiM, Uncharacterized conserved protein YfiM, DUF2279 family [Function unknown]
MRAALLLSLLLLLSGCSHAANDPWTGKDKAQHFLASAALAAAGNAYGDHQGWSRRRSAAFGLGFSISLGA
AKELYDSRPAGTGWSWKDLAWDVAGAATGYLLAQLADL
>gnl|CDD|444288 COG5545, COG5545, Predicted P-loop ATPase and inactivated derivatives [Mobilome: prophages, transposons]
GLTKSLSEGLIRILDRVLDGSKPTLLEELPLADSSDYALEGALLARALGLKDAKALLRPDEAEKSDDLED
NSVLDLAPADELNEELLEGKAELPLAGADEVEVQAGQPDTDKYSLELLVPELSLIPKGDDADLAAGEFAD
PLLAQALELARLELLKAADSASSEADSGLALAAASEAGLGLVLGADATLDEGSESARLALLLAEKLASAT
AALLLKTLSDLALELSEADLDAKAKLGDRVKRLLEALKAVRLELTAEEKYLELADDNRLRYLEREYGIDI
SKDKIRDAISSVAKENSYHPVREYLESLPEWDGVPRIDTLLIDYLGAEDPEYTRAVLKKWLVAAVARVYE
PGCKFDTVLVLVGPQGIGKSTFLRILAGPEWFSDSLSDLDDKDAAEKLQGNWIIELDELDALSKADVEAL
KAFLSRTVDKYRPPYGRKVEDHPRQCVFVGTTNEDEFLRDPTGNRRFWPVEVEKIDIEALRADRDQLWAE
AVHLYKSGERWWLTDEEEEEAEEEQEEFTEEDPWEELILEYLEKPEPVTAAEILERIGAIGDSTTLLESR
ENTTDILLLLLTKAKKRLVLVRKKKEGKELKRRKRRRRYKKNSSPVTRKKVRRPE
>gnl|CDD|444289 COG5546, COG5546, Uncharacterized membrane protein [Function unknown]
KINWKVRLKNKAFWVALIGAILLLAQQVLGLFGIDLDIASLLEQLTDIVNAVFAILVLLGVIVDPTTKGI
SDSEQALTYNKPRKDDK
>gnl|CDD|444290 COG5547, COG5547, Uncharacterized membrane protein [Function unknown]
MKQEKLLEFLKKHRGKIIGGLIGLIIAILILTIGFWKTLFIIICILLGYYIGKYLDGTGDLKDFLDRLLP
PRR
>gnl|CDD|444291 COG5548, COG5548, Uncharacterized membrane protein, UPF0136 family [Function unknown]
MNLGIIAALIYGILVIIGGIIGYVKAKSKVSLISGVISGILLLVAGYLQLQGQVWGLTLATAITALLVIF
FAYRFVKTRKFMPAGLMVILGLVALVLMVLQLVGGS
>gnl|CDD|444292 COG5549, COG5549, Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]
MKKSTKLRRLLILLGLVILTGILVILTSLPSVSNLNNASSLPPLKVHPLPPTLAQWQDPTNSGDYFSQIK
PTPVGYLVWSQFPVKVYIDRPPSAAQQRAQQWVAAVLQAIAEWNAYLPLEVVENPENADIIIVRSNPPLT
ASPNPETGARSAETTYEFYDTGNILSHRFTILLSPNQTGKYLLATARHELGHALGIWGHSPSPTDAMYFS
QVRNPPPISPRDINTLKRIYQQPT
>gnl|CDD|444293 COG5550, COG5550, Predicted aspartyl protease [Posttranslational modification, protein turnover, chaperones]
MIIMGEAFVEVEVIRLPDGESLEVDALVDTGFTGFLVLPSQLIEELGLPELGRRRARLADGSEVEFDVYE
ATIEWDGQEAEVPVLAGDGITEPLLGVALLEGLGLVVDPIEGGLVLI
>gnl|CDD|444294 COG5551, Cas6a, CRISPR/Cas system endoribonuclease Cas6, RAMP superfamily [Defense mechanisms]. CRISPR/Cas system endoribonuclease Cas6, RAMP superfamily is part of the Pathway/BioSystem: CRISPR-Cas system
SLVLELTPLSDIPLPPFTGSALHGLFLSLLRRVDPDLADLLHDAETPKPFTISPLQGLQGGGQKVLRPGE
RYWFRISLLDDELLPYLVQALLNAGELGLGRAPLEITSVEITEQATTYEELLEQASSAPPSRRIRLEFLT
PTSFKQKGRYVLLPTPRLVFNSLLRRWNALSPLELPLAQADFLRLVEENVDISRYSLRTVTVALGKRKLR
GFVGWVTYRLPGDPELLKLFNALLRFAEYSGVGKKTTMGLGQVRLEV
>gnl|CDD|444295 COG5552, COG5552, Uncharacterized conserved protein, DUF2277 domain [Function unknown]
MCRNIRTLFNFEPPATDDEIRAAALQYVRKVSGTTKPSKANEEAFDRAVAEIAAATRRLLDSLVTRAPPR
DREEEAAKARARAAKRFARA
>gnl|CDD|444296 COG5553, COG5553, Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General function prediction only]
MTTQRRPPRLRRFIAALRALVDRGPDEREILAAVRPLLRRLVASDDWLPAEFAEPDPDRYARYLLYADPD
GRFSVVAFVWGPGQKTPIHDHGTWGVIGVLRGAEKNTRYRRTDDGARLEPGGEVVLGPGDVIALSPPGDI
HQVENAGDEPAISLHVYGGNIGRLVRFVFDPETGTAKPF
>gnl|CDD|444297 COG5554, NifT, Nitrogen fixation protein NifT [Secondary metabolites biosynthesis, transport and catabolism]
MKVMIRKNGDGGLSVYVPKKDLEEPIVSMETPGLWGGEVTLANGWRLYLPPLPADPRLPITVEAKRL
>gnl|CDD|444298 COG5555, COG5555, Cytolysin, a secreted calcineurin-like phosphatase [Intracellular trafficking, secretion, and vesicular transport]
MKYVSRRCFLAGAAGFGLAEPFGTSAFRAASQPAIDVTFLVVADTHAGRVASGLAPGCPEEGKTDKALER
HVAALNGIAGQAWPPAIGGVVGRPRGLLVGGDLTEDGQGRQLDQFKARYGLGGGPGLLHMPVYEGLGNHD
LDQNGPPWYRREVRDYVEQRHRESVFYKPPVPVTEYHGSDCYSWDWGDLHLVQLHRAPGDEVKGDVSSLD
WLKKDLAAAAADGRPVILFFHYGLEGFSTEYWFASGPDRQALLDILKGYNVLGIFHGHYHTTGIYRWHGI
DVYKPGAAKNGGFAVVRVTDGRMTVASYNAARGHFTDAFSKPIGH
>gnl|CDD|444299 COG5556, COG5556, Uncharacterized conserved protein [Function unknown]
MAALKPEVKAFIVQALACFDTPSQVAEAVKEEFGIDVTRQQVESYDPTKRAGKGLSKKWRDLFEATRKRF
LEDISSIPIANRAYRLRALQRMATKAEKMGNMALAAQLLEQAAKEVGDAYTNRQKVELTGKDGGPITSVT
VVTDENGDA
>gnl|CDD|444300 COG5557, HybB, Ni/Fe-hydrogenase 2 integral membrane subunit HybB [Energy production and conversion]
STKITADILRPVLKGSKGYWIWLAVLLALLLIGLYAWAYQLTEGLGVTGMNNPVSWGLYIVNFVFWVGIA
AGGTLISAILYLFGQKWRKPIARLAEALAIFAVICAGLFIVLDLGRPWRLYWLFPYPNFRSPLFWDVFVI
STYLTVSLLFLYLGLIPDLATLRDRAPGFRRKRYEKWYLILAGLATPLALSVHTVTGFLFAGLSARPGWH
TTIFPPYFVAGAFASGFAMVILLLIILRKVTKLEDYITDEHLDKLGKLLGAFGLIVLYFYLTEFFTALYS
GNPYEAEAFIYLFFGPYAPLFWGEIILGVVLPLQLLWFPKLRRNPKLLFVASILVNIGMWFERYVIVVTG
LARPFLPSSWIGEYSPTLVEWGLTLGTIALGLLLFLLFLRVLPVVPIAEVKELLHEAA
>gnl|CDD|444301 COG5558, COG5558, Transposase [Mobilome: prophages, transposons]
MGLVRSEDILEEINNILGKKYVQEHPEKGRNWRTYESEFSRRIKEAMKELPEYIEKAVSIMHIQKRPGRP
HKLPLAQRVFLILIKVLSGLSNRRFVNLLDIFSMLGGIDVSYKTIERLYSDNEVVMALHNLHILLLPNKN
IESDFAGDGTGYSLTVTKNYESYKQRRKKDFRYWFKIADLDTRMYIASGTSDKSENDAYDNALRIVTAEG
FNIDSISLDKYYSSRSNLELLDGDTAVYIIPKKNLTGKGSHKWKSIIREFVNNTMEFLKHYHKRSNSESG
FAADKRKFGWNLKQRREDRIGNALLCKNVWHNLFVVIHE
>gnl|CDD|444302 COG5559, COG5559, Uncharacterized conserved protein, DUF2281 domain [Function unknown]
TIMEEIYELIKKLPPDLQQEVLDFIEFLLEKYAKKKKRRLKLDWAGALSDLRDQYT
>gnl|CDD|227847 COG5560, UBP12, Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]
IESTESQASSVSASQNEIIAPASLPLMMQEELIDEKPAESSKQCEYAVIFAYAWYEGMFDRASCDGGSPG
PIVQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYGLAGLITPRITVLLPSESAPEVESYPVVFK
LHWLFSINGSLINLGHDPVPHSASSHGTLRDLSERVMNAFVDPSDDFRLWDVVPEIMGLRLGLDSFFRRY
RVLASDGRVLHPLTRLELFEDRSVLLLSKITRNPDWLVDSIVDDHNRSINKEAGTCGLRNLGNTCYMNSA
LQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEF
SGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQG
MYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQPLKIELDASSTIRGLKKLVDAE
YGKLGCFEIKVMCIYYGGNYNMLEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVHLRIEKGYKSKRLFG
DPFLQLNVLIKASIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRLLREESSPSSWLKLETEIDTKREEQV
EEEGQMNFNDAVVISCEWEEKRYLSLFSYDPLWTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPG
CKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVD
NHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS
>gnl|CDD|444303 COG5561, CGGC, Predicted metal-binding protein, contains CGGC domain [Function unknown]
MKKIGIIRCGKYEDRCPGTGCFKAFNERKGAFEDYKEDVELVGFFTCGGCPGRKVVRRAKELKKKGADVI
HLASCMVKGGPPCPHIEEIKKAIEKKTGIKVVEGTHHYPK
>gnl|CDD|444304 COG5562, YbcV, Prophage-encoded protein YbcV, DUF1398 family [Mobilome: prophages, transposons]
MFTLEQIQAAFEKVKSGADFPQFVQELKAAGVEHYIYDVADGNTTYYGEDGYSVVLPTNYVALPVAPTFD
AEAVKAALRAHQAGETDYPTFCKQAAAAGVFKWVVDLTGRTVTYYGRDGELLVIEPIPGVEP
>gnl|CDD|444305 COG5563, COG5563, Uncharacterized conserved protein CPn0794, contains PKD-like HAF repeats [Function unknown]
MKSSATGISNDGGVVVGSSDTAGGTYHAFRWSNGTMTDLGTLPGGGSSSANGINDDGQIVGTSYTASGSN
RAFRWTANGTMTDLGTLGGGTSSEANAINDDGSVIVGSSDTAGGNRHAFRWTPNGGMTDLGTLPGGDSSE
ATAINDDGQVIVGSSTTASGETHAFRWTDNGGMTDLGTLPGGTGSQATGINADGQVVVGTSSTANGERRA
FLWTENGGMTDLGTLLAAPSGGQLSSATAISDGGQIVGTGETADGQIRAFLLTLD
>gnl|CDD|444306 COG5564, COG5564, Predicted TIM-barrel enzyme [Function unknown]
MRFTRQEILERLRAQIAAGKPIIGAGAGTGLSAKCAEAGGADLIIIYNSGRYRMAGRGSLAGLLPYGNAN
EIVMEMAREVLPVVKHTPVLAGVCGTDPFRLMDAFLDQLKEAGFSGVQNFPTVGLIDGRFRANLEETGMG
YDLEVEMIRLAHELDLLTTPYVFNPEEARAMAEAGADVIVAHMGLTTGGSIGAKTALTLDDAAARVQEIF
DAAREVRPDVIVLCHGGPIAEPEDAQYVLDNTPGAHGFYGASSMERLPTEKAITEQTRAFKALKL
>gnl|CDD|444307 COG5565, COG5565, Phage terminase large (ATPase) subunit and inactivated derivatives [Mobilome: prophages, transposons]
SLSSPLKIESALEQKALLAELLERELRRRQVRRRLYYYRPYFPQQEFHGAGYRFRERLAMAGNQRGKTTA
GAAEIAMHLTGWYPPWWKGPRFFWPAGVIWETGSSELTRDLVQRLLIGGPKGTGGWPTGAIPGTAIGATV
PRSGDANAVRSATIRHVSGGASTLLFKSYEQGRAKWQGDTVDGVWFDEEPPEDIYSEGLTRTNATGGFVI
LTFTPLKGMSDVVRRFLDEPSPDRAVMNVTIDDAEHYTPKERQKIIASYPVHERDARTKGIPILGSGRIF
PVTEEFITVDPFPIPCHWHQIGGMDFGWDHPFAAVQLAWDRDNDVFYVTRAYRAREATPIEHAAALKSWG
PWLPWAWPHDGLQHDKGSGLQLAEQYRAQGLKMLPEHAQFEDGSNGVEAGLFEMLDRMRTGRFKVFSTLT
DWFEEFRLYHRKDGGVVKEVDDLLSASRYALMMMRFARVRYGDIKWKKTKRKVIPAPIRPV
>gnl|CDD|444308 COG5566, Mor, Transcriptional regulator, middle operon regulator (Mor) family [Transcription, Mobilome: prophages, transposons]
MEDAEEDLRSRWPELLAELADVLAATLEELPGLDEELAELIGLEVALALASYYGGQNIYFPKGDSLRRAL
RDLEIWREFNGNNHRELARKYGLSERWIYEIVKRVRKEERARRQPSLFDE
>gnl|CDD|444309 COG5567, YifL, Small periplasmic lipoprotein YifL (function unknown) [Function unknown]
MKKLLRLLLLLLLLFTLAGCGLKGPLYLPPAEKEKQPSQKQVE
>gnl|CDD|444310 COG5568, COG5568, Uncharacterized conserved protein, DUF1150 family [Function unknown]
MNTEPLRPLTPEDFAALGGGEIVYVRPVRSEDLPRLFPQAPEIPPGLTLYALHSADGTPLALVDDREAAF
ANARENDLAPVSVH
>gnl|CDD|444311 COG5569, CusF, Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism]
MKKLLAAALALAASDGAAAAAAAAAATAEAEGTVKAVDAAAGKVTIAHGPIPALGWPAMTMDFKVADPAL
LKGLKVGDKVRFEFERVGDGGYVITSIEPAK
>gnl|CDD|444312 COG5570, COG5570, Uncharacterized conserved protein, DUF465 domain [Function unknown]
MSLQSHLEELRRKHAALEREIEDEQRRPSPDDLEIAELKRRKLRLKDEIERLRAAAT
>gnl|CDD|444313 COG5571, YhjY, Uncharacterized conserved protein YhjY, contains autotransporter beta-barrel domain [General function prediction only]
SLGASAAGSLGYLASASSNAATAPGLAAATASAAGAAGLGAASTASSLSGASLALLAAQALGAGLSGTNG
FSGGAGSSSGTGPTANGGLAGAGGVDLAGAGGGGGASGLAGGAGGAGGTAAAGGAAAAGGGAAGNAATAA
AAAAAGTALQLSGLTTAGAVGGVAGTAALNGATANTGLGAAAALAAAAAAAAAAAAAAAAAAAAATAAAA
AAAAAAAAAVLASPAPAAGGAAAAAAGAAAAAASAAANAATQANLLLLALALGSNGNAVGLNAVGLANEA
AAPGAVGGDAGSTGATPSTLSSASCVASSLTAANANTLYAAADTAGPAGATAALAAAAAAVLASAAAVAQ
AALALAAAGGQARSLAVAAGQGRGARGGQTRGGGGAGGTTGGGVGAGGGDGDGPNLTLGVDYRLSDNLLL
GAALSYGRQDLDFGDGGSYDARSTSLSLYAGYRAGGLWVDADLSYGDLDYDIRRHIRLGPATRTETGDTD
GSQWGARLTAGYDFTAGRLRTGPFAGLDYQKVKVDGYTETGAGSTALSFGDQDRDSLVGSLGWRADYQLL
GRFNPYAEVAYEHEFGDDDRDVTAGLASLPAGSFSLPAAAPDKNWGRATLGASAALTNGVSLFAGYSGTF
GRDDGRQTSVNLGLSARF
>gnl|CDD|444314 COG5572, COG5572, Uncharacterized membrane protein [Function unknown]
MNTLKALALAAALAAALALGAAAAAAAAAAAGKEKCYGVAKAGKNDCAAGAGTHSCAGTSTVDYQGNAWK
YVPKGTCEKIGGSLTPAKR
>gnl|CDD|444315 COG5573, COG5573, Predicted nucleic acid-binding protein, contains PIN domain [General function prediction only]
MSARVFVDTNVLLYALDKDDPAKQARARALLAALWRERGGVISTQVLNEFYNVATRKLKMPLEEAREALR
DLLELWPVVPLTAETVLAALDLAERYGLSFWDALIVAAALEAGCRTLLSEDLQHGQVIEGLTIVNPFLSA
>gnl|CDD|227861 COG5574, PEX10, RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones]
MALRPEAHIREENLRNKRADLESVRQFAESIEGSNAISRRRSRFFSNVPGYPMDVREKILERPSGSTSEE
EAVDLIAAIRSKGLREDSLSRFNREETLSIEYSRETNIDKEGEVLYPCGIFFCIGCDYIWSIDLKQTANT
HEASPSQLLKFLPTIRLAMNIPEVISDLTAVALSLDESRLQPILQPSNNLHTLFQVITKENLSKKNGLPF
IPLADYKCFLCLEEPEVPSCTPCGHLFCLSCLLISWTKKKYEFCPLCRAKVYPKKVIILRK
>gnl|CDD|227862 COG5575, ORC2, Origin recognition complex, subunit 2 [DNA replication, recombination, and repair]
MLINEHVRERYHFLRVSLTRVAHLVFANSHESNDLKMVENVSSTPKKGVLEDPSTLTPEVVTPRTPGHRI
IKAKGAYTKDRSAKRRRGRIEIERHLLGEFDDNVGSNSLLDVPLYSLEAEPLSPSVMLEDESMEGINQSP
QGISVEKLGKEDNRSRSSTPASPSLESHEFSESEAGLSQSNGFEARSHGTGFDEYFDKFSQRKTSSNTLS
QLPVLDNQVYLDTVKEICTETMGSDQVLFHLQCKNFHQELFELARSFNLLFYGYGSKTAFLRKFFPSALP
CFPIFYLNGYCPIMSRREVLAEIMEALRHRSKLEAQDEVSKAPTIREIDSFSLGEKIGSRVHNEDGKSVM
ANRFQFGLLEFSSLRNFAILASVDHIGIRLLWDDVERSSFNFVFHDLTTFEPYEEEATYENSLGMGIHLR
STRAEASKRVLRSLPRNSRLVLKELLSHQLERMMCNADFDARQGEKVGVELGEFFEKCKAKFFLSNETSV
RSMLNEFIDHGLLKIKRNGSEIEICWVPYERNELEGLLDQMDEDV
>gnl|CDD|227863 COG5576, COG5576, Homeodomain-containing transcription factor [Transcription]
SPVQPMQPLSALESQRMPQIRTIKTTKNKREVEAADSEMKLERKQDGSSPPKSKRRRTTDEQLMVLEREF
EINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKKRSGKVEQRPGEEEADLAKIGSLSTGQISIIE
TLEFSRTSYEEGGLQY
>gnl|CDD|444316 COG5577, CotF, Spore coat protein CotF [Cell wall/membrane/envelope biogenesis]
TELNDQDIATDMLGSAKAGARNYANAALEAANPELRRVLADQLNQCIEMHYEIFQYMNQKGWYQPPQLPQ
QDIQQAKNAYQPAQ
>gnl|CDD|444317 COG5578, YesL, Uncharacterized membrane protein YesL [Function unknown]
MEMGGFFNGLYRILEWIWRLAYLNLLWLLFTLLGLPVFGIGPATAALFAVVRKWLRGEEDIPIWKTFWRA
FKENFKQANILGLILLLIGLILYVDLYFFRQLSGLLGLVLSFVLLVLLLLLLIVLLYVFPLLVHYDLKLK
QLLKNAFILGLASPLTTLLLLLGLALLLYLTYFLPGLIPFFGGSLIAYLIMWLFYRVFRKIEAKLEEEEE
>gnl|CDD|444318 COG5579, Mll0975, Uncharacterized conserved protein, DUF1810 family [Function unknown]
MSDPFDLQRFVDAQAPVYDQALAELRAGRKRSHWMWFVFPQLAGLGRSATAQRYAISSLDEARAYLAHPV
LGPRLRECTEALLALEGKSAEEIFGSPDDLKLRSSMTLFAAAAPDEPVFQEVLDKYFDGERDERTLALLG
>gnl|CDD|444319 COG5580, COG5580, Activator of HSP90 ATPase [Posttranslational modification, protein turnover, chaperones]
MMKTIKKYYTIPASPEEVYKALTDSQTHSAWTGGPAEMSPEVGGEFSAWDGYIVGRNLELEPGKKIVQSW
RSSDFGDQEEDSIVTIKLHPHGGGTSLELIHTNIPDGDGEDIVEGWDEYYFGPMKKYFE
>gnl|CDD|444320 COG5581, YcgR, Cyclic di-GMP-binding flagellar brake protein FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell motility]
LEVSFGGGEERYKSRLLDVDPDRGLLIDAPIGPEGRNLPLLEGEKVVVVFFSDGVKYQFSTEVLGRVKYD
PIPALVLSLPEEIERIQRREYFRVPVPLDVPVRCLRPDGEGEPLEGRLLDISGGGLALVLPEPPPLEVGD
ILELRLDLPDEGEIVVDAEVRRVVEVELGKGKYRLGCEFVDLSEADRRKIQRYIFELQRERRRKG
>gnl|CDD|444321 COG5582, YpiB, Uncharacterized conserved protein YpiB, UPF0302 family [Function unknown]
MTTSVSVAEKKDFLRWFLQNYQLKRREAVWILNYLLSHDQLLENVHFVEEARYCPRGIIISTVCSDEVPF
RFYKDNVVTTDAEKAFHDIRLNPNEDLYIQLNFPNAYQSPEYLAVLEENPYLPEDLQISEKDKLLAEQLL
DESLREFQREKLLKQIDEALDTGDKERFYELTEELNKLKE
>gnl|CDD|444322 COG5583, COG5583, Uncharacterized conserved protein YezD [Function unknown]
MSEGPAKSQISAEVLEKILEALKGLRFGSVTIVVHDGRVVQIERTEKVRLKKAKKNK
>gnl|CDD|444323 COG5584, COG5584, Uncharacterized conserved protein YtzB [Function unknown]
MNWKNFLIGVGAGIAAGYVVKEYVKKKKKISAEKVLEKVKEAFKKEGPIEGSWIYMKPEPFNKFGLTTKV
YRGGISRLEDGELVQYEFIADAYTGTILDLYRV
>gnl|CDD|444324 COG5585, COG5585, Putative phage head morphogenesis protein, F of phage Mu or gp7 of SPP1 [Mobilome: prophages, transposons]
MDNALLSIYNLRMQVNRLLLGAELDLELKALANGEQDAIEAFLSEAYLREVLRAPGDLGLAAEFAAKAES
LLDKVINVSWNGKNWSDRIWRNKDNLGSKLADDLTTSLLRGKNPKTIIKELRREFDVSKYAAARLVITES
ARVQSEVQLLSYKDLGVKKYKILATLDKKTSDICRSLDGKIFDVKEAKIGVNAPPFHPNCRTTTVPYTFE
DTEDERVAREADD
>gnl|CDD|444325 COG5586, COG5586, Uncharacterized protein, contains DUF2293 domain [Function unknown]
RGRRAGEDTTRQAAIAKALRRLFPGCPSSDAEAIAAHALSRALRRLPPETAVWLAVVAHVRHTHTDYDAL
LDDGYDRDEARFFVRDEINAVLASWGA
>gnl|CDD|444326 COG5587, COG5587, Uncharacterized protein, contains DUF2461 domain [Function unknown]
FTMFSKETLDFLKELAKNNNREWFDEHKKRYEAVRAPFLALVEALIPELAKIDPEIAGPKPKKSIFRIYR
DTRFSKDKTPYKTHFGASFSRGGKKSGRPGYYLHIEPGESFLGGGFWMPEPETLKRIRQEIDYNPEEFRK
ILEDKKFKKTFGELEGEKLKRAPKGFDKDHPAIELLKRKSFIVMHELTDEEVLSPDLVDELVEGFKALKP
LNDFLNEALTTDL
>gnl|CDD|444327 COG5588, COG5588, Uncharacterized conserved protein, DUF1326 domain [Function unknown]
MATVDWRLKGDYFENCNCDVGCPCQFNEPPTHGYCEAVLAWHIDEGHYGDVDLDGLNVALLVHWPGNIHE
GNWRVALFIDERADDAQREALLKIFSGQAGGPMATLATLVGEVLGVEFAPIEFEVDGRTRSLRIPGVIEA
EIEPIRGPVTGEEHRVRISNPPFSVGPGGPAEVGKATKSRVRDGGIDWDFSGRNAHFAPFHWSGP
>gnl|CDD|444328 COG5589, COG5589, Uncharacterized conserved protein, DUF2390 domain [Function unknown]
MSEAALSNLTAEALWDFSLALYARPGVAEACLALQDRYGADVNLLLWALWLAQRGRALSAAELAALLAAA
RQWREQVVLPLRALRRALKAPAADDAALEALRQQLKAAELEAERLQQERLAALLNPLPAAEPPAPEALAN
LAAYLRSLPAADAEALLAALAALAE
>gnl|CDD|444329 COG5590, COG5590, Ubiquinone biosynthesis protein COQ9 [Coenzyme transport and metabolism]
DMTLDELRDALLDAALPHVAFDGWSEAALRAAAADAGVSPDEARLLFPRGAVDLLDAWHRRADRAMLAEL
AAADLSALRVRERIAAAVMARLEALAPDREAVRRALALLALPQNAALGAKLLWRTADAIWRAAGDTSTDF
NWYTKRATLAGVYSSTLLYWLGDDSEDHADTWAFLDRRIDNVMRFEKLKARVRKNPGALLADPARLLGRL
RAPA
>gnl|CDD|444330 COG5591, COG5591, Uncharacterized conserved protein [Function unknown]
MKKLLLTALALAALLAAGAALADDDCTNVPKAEWQPREALKQKLEAQGYTVKKFKVDDGCYEIYGTDKDG
KKVEAYFDPATLEVVKSE
>gnl|CDD|444331 COG5592, COG5592, Hemerythrin domain-containing protein [General function prediction only]
MMNIQDLIRMDHQKVNTLFEEILQTNDPQKIQEYFGQLYKDLRAHAEAEEEVVYPAVRPFYGEEPTQELY
DEQAEMKQLLDEIKALDPSSPEFKDRIRQLKDLVGDHVRQEESTLFPAIRNNLSPEQQEQLATEFKAAKS
KLQDQMAQAVS
>gnl|CDD|227880 COG5593, COG5593, Nucleic-acid-binding protein possibly involved in ribosomal biogenesis [Translation, ribosomal structure and biogenesis]
EANLSSEPEMGKSKSGNEEKRGSKGTRPSGKGGDPDKPWYEIPLPQVNDDASRKKKEQIEKLEKRGIVLL
RRDCPIQGEEFPDATSQAKIEKDLLSHGTVKDRISALTLLVQRSPSHNAKNLETLLSFCEKKSRNVAYQV
LKNLKDLFISGLLPNRKLRYFKNQPGLSKEVQNKYLKQRIFESFLKNLRFRVLEVLEVLSHDPIQYVKKQ
VVRLVYDLLEARPEQEVNLLHLFINKLGDKRDKVSSKASYVILKLELLHPGMKEVVLDGIEDFYFKPNDL
FRSRYYALITLNQTELENREKAVANKLVKVYFSIFRKFLENIPKEHRVNSNILEEKLVIGLGKNKGSEKI
CKTEIIRKEVHTEKNSFYGSAVLTGCNRAGPFALLFRNAVKSHMMTLFKITHEFLFNTSEQALMLIDQEF
YRFLLDSDRYYTPLYESLIDPRLSESSKQGIYLNLLYKSLRVDTNVHRVDAFRKRALQVISGWMVLPFDT
GDFMSLLQLEMACGDLKNLLTNTPVDYEYESDAEEEQGDKDIKRKEYDGRKRDPKFANAEKSSLWEINNF
INHFHPTVKTYANAYVTGEEQIAKPDLGLFTLSHFLDRFVYRSAKQTNTARGTSIMQPLFSGVNDSLVKA
SMHDQGPVNTEDWLTKKVEDIKPEDKFFYQYFTKKTADGKGKKSNKASFDSDDEMDENEIWSALVKSRPD
VEDDSDDSELDFAEDDFSDSTSDDEPKLDAIDDEDAKSEGSQESDQEEGLDEIFYSFDGEQDNSDSFAES
SEEDESSEEEKEEEENKEVSAKRAKKKQRKNMLKSLPVFASADDYAQYLDQ
>gnl|CDD|227881 COG5594, COG5594, Uncharacterized integral membrane protein [Function unknown]
MVDSKSDLFVNGAKPPLNRSTSAVITQLVFAGLIFLVFLILFLILRKRWKRLYAPRTNFDGQNECLPEPN
PSSYWGWLEPLVKIPDEFLLQYAGLDGYFFLRFLKMLIKLLFILSLILIPILLPVNYHFQKATNGNSDSE
SGLDKLSISNVSPSNRLYAHVFLSWFFFGYVLFIIFRELRFYVVLRQAYLRSPLYQQSLLTLQNNLSSRT
VLISGLPSELRSDEELKELFDKLKVGEIDSDVLCRDLGTLQELYKERDKILKKLEKALNELLNKLLKKSH
LKTNKKSGKLTPSRKKEFEILPEYVPDKKRPKHRIKKLNKGIFGKKVDAIDYYSAKLTKLDAEIENARKS
LYENTPTKSGFITFKSQASAQIAAQSQIYSRVLGKLKVEIAPAPNDIIWDNLRLSRKERLFKRISANILF
ILLIILWAFPVAFVGTISNLNTLSSLWPFLKFILKDPPFLAGILTGLLPTVALSLLMSIVPYFIRWLSYM
QGLVSYSEEEIYVQNKYFAFLFVNLFLVVTLASSFSSIVWSLLKEPTSIMTLLANNLPKASNFFISYIIL
QGLSGFPGTLLQIVPLLLSLVLGKFKDSTPRQKWNRLETPPSFQFGTVLPQPILLFTITICYSIISPLIL
LFGAVYFILNYLAYKYNLIYVSNHSPESGGGYWPRALFQIIVGLYLFQVCLLGLFSLAKGWGLSVLLFPL
IVFTVIFHYYFKKMFDPLSKYIKLSSYKLLIPELEYLSTFSESTKVDEDDKFEEVWSYFPDGFDLSIERS
YPALRAKDPEEWLPEDPLGLSETAISDSSGSLPENFDDNTTFDENGNVEDLYNPPDY
>gnl|CDD|444332 COG5595, COG5595, Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only]
MYLVEVSFECYADTTISAAEDAINQLLDALRYNGQILGREFPTYVAEGIFQVRVVCPEQDSLHPRYNSEQ
VNSALQKLEEAGLLFPKFEILGRDLNSDETAECESPSWQILYTTYLHSCSPLRCGDHLAPIPLYRLPATD
NGLHKALIKWQENWQACDQLQMNGAVLEQAALAEISDFNSALSKRGRDLCRRIEELTGIPTYYYLYRVGG
DSLAAELARKCPSCGGDWRLTEPLHDIFDFKCDPCRLVSNLSWDFQ
>gnl|CDD|227883 COG5596, TIM22, Mitochondrial import inner membrane translocase, subunit TIM22 [Posttranslational modification, protein turnover, chaperones]
MVYSGFGLEQLSPPSPNAYNILSPEERDPCPLEKLADFMKAFSYSCIGKSALSGLKGFRLGGPSGGFSSS
LAYGTGLVHLLGLNFGGVWGGLFSTIDCTPFRLQLKEQLNNAGKRGFFTGKNLGVLGLIYAGINSIITAL
RAKHDIANAIAAGAFTGAALASSAGPQAMPMGGAGFAAFSAGITLAMKSED
>gnl|CDD|444333 COG5597, Gnt1, N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis]
MTGLHPDGPAGSRRAYVTLVTNADYALGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAALGARLVR
VDLLPTSDAFNARHARGRLHGAAPFTKGRKPAFHTPLDNFCKLRLWQLVEYDRVVFIDADALVLRNIDRL
FDYPEFSAAPNVYESLADFHRLNSGVFTARPSQATFEAMLARLDAPGAFWRRTDQTFLQTFFPDWHGLPV
FMNMLQYVWFNLPELWDWPSIRVLHYQYEKPWQKDHAKADRLRPLIDLWHAYAGGGPIPDLASLPNPTG
>gnl|CDD|444334 COG5598, MttB2, Trimethylamine:corrinoid methyltransferase [Coenzyme transport and metabolism]
PRYEPLSEEQIERIHEAALRILEEIGVEFEHEEALEIFKKAGARVEGGRVRIPRALVEEALATAPSSFTL
YARNPERDVELGGGNVVFGPGGGAPFVLDLETGERRPATLEDLANFAKLADALPNIDFSGGNPVEPSDVP
VEVRHLDMLYAMLKYTDKPIMGSATGRERVEDSIEMARIVAGGEEELREKPVVITLINPNSPLRFDEEML
EALIAYARAGQPVIITPFGLAGATAPVTLAGALAQQNAEALAGLVLAQLIRPGAPVIYGTFSSSMDMRTG
APAFGTPEAALLSAAAAQLARYYGLPSRSGGGLTDSKLPDAQAGYESAMSLLAAALAGANLILHAAGWLE
SGLTASYEKFVLDNEIIGMVRRLLRGIEVDEETLALDAIKEVGPGGHFLGHPHTLKHYRTEFYYPKLSDR
ENYEQWEEAGSKDLLERANEKVKEILAEYEPPPLDPEIDEELDAYIARR
>gnl|CDD|444335 COG5599, COG5599, Protein tyrosine phosphatase [Signal transduction mechanisms]
VSPKNPIAIKSEEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETALRANLGYLNANY
IQVIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKVKMPVYFRQDGEYGKYEVSSEL
TESIQLRDGIEARTYVLTIKGTGQKKIEIPVLHVKNWPDHGAISAEALKNLADLIDKKEKIKDPDKLLPV
VHCRAGVGRTGTLIACLALSKSINALVQITLSVEEIVIDMRTSRNGGMVQTSEQLDVLVKLAEQQIRPLL
RS
>gnl|CDD|227887 COG5600, COG5600, Transcription-associated recombination protein [DNA replication, recombination, and repair]
NDMANTLLDAVAHGNSSHLTKCLSQNGREIAILGKVLTGDSKIDAKLKETIQRPFGRNDTAVTLVLQKFL
NLGRDKDPWSKRSSELLQELYKNLTAELSYSSAPHLEVLVKNAVRMLGREIWNLTVVKKQLYGLLELKSE
LNQDNLSKISRLLTRMFNSILNDRSPALNPSKKVGLYYIANLLFQIYLRLGRFKLCENFLKASKEVSMPD
ISEYQKSQVVVFHYYLGIYYLLNENFHEAFLHLNEAFLQCPWLITRNRKRILPYYIPTSLLVNKFPPTKD
LLERFKRCSVYSPLVKAVRSGNIEDFDLALSRNERKFAKRGLYLTLLAHYPLVCFRNLFRKIWRLHGKQS
RLPLSILLIVLQLSAIDNFHSFKEVECILVTLIGLGLLRGYISHSRRTVVFSKKDPFPVSVKP
>gnl|CDD|227888 COG5601, CDC36, General negative regulator of transcription subunit [Transcription]
MLNILKPLEQIEDEEQSIHDLGKDLLSEILSLVRPKKYQDRPSTTLYSPWAESTKKPVQPMFMLPNCYPN
APNPPIFKVNIEDMKMDNFHDETLFYIFYSFPNDVLQEKAYDELLKRNWRFHKMLKCWLTFNPGMSPATA
DHVKERGSYVFFDPFSWSKVSLDFLLDYKAVR
>gnl|CDD|227889 COG5602, SIN3, Histone deacetylase complex, SIN3 component [Chromatin structure and dynamics]
MDAMNVPVDPPHDNPGDKVMTGSLKQISPKYHPSMSRDHDVNTSLQNSEPWPDNGSARKPSYSPESMSSY
GGPMDERSGTRRYYEDVEQILSSLAGDNPDPSTDHGSASNQNMERSPPPRIPYRPLDVSDALSYLEKVKE
QFSNRPEIYNNFLDIMKDFKSQAIDTPGVIERVSVLFRGYPHLIEGFNTFLPSGYKIEGSLPQPNGSRLH
VTTPQGPLSSPPVQSSYYVAPCNHDQRTSHPTLPSDSQPEPSAPSHMPSDARGKHQVDFNQAIIFVNKVK
VRFQNNPEMYYDFLDSLRTYQMKQRSIQEVYARVTKLFAEAPDLLEEFKEFLPDSSVSAEQSTANAQKPS
KRLPPIGSFSLPTAAPEQNRPSLLWESPRSISNISRYRADLLTSFSRNFVPIRIHMPISHLSNESEDFFE
RIKQYLKDKNLYHEFLKLLNLYSQKIIDKNDLVERLFAFLGSNEELIRWFKAFINYSEPEKEPLRETRKD
LEKFEKCGPSYRLLPKSEEEIKCSGRDDLAWEVLNDDWVSHPTWASEDSGFIAHRKNQYEEALFKIEEER
YEYDRHIEATQRTIKALEQIIDKIKDMEESEKANKTLPGGLGLPSKSIYKKVIKKVYDKEHAPEILEALL
KKPHVTIPIVLKRLKMKDEEWRSCKREWNKIWREIEEKNYHKSLDHQGVSFKSRDKKILSTKNILEEIDD
RSQAKIHVSIDDKKVFQFVFVLCDTYIFVNILDLKDTLITNMSSYLESDKERLKANLKTIVSLFFLLCIF
RIIIIVYERLLNVKGLNIDGLKADRSSRSDESAQRYSKVKSGNLEQVSKQIDEYAIEDEIKEPTHPDGLK
EHNISKGISENEKQVIALTEFGNSLMYVFFRLRFDSYERLYEIKKIKEAVTIGMMEPGHYENELWDSYRL
IFGALTPCEFEKYLRPFYNNTCYKIYTIDRLRQSLKKQLHPITYDIKYIAKSELFEMNSAASSKRKQDQT
KYRLEVESLLNPDEILFRFCWINKFKSFGIQIMKRADLTVDQSLDTQRVWKYYVQSYAIQHLTEGISYKN
YKCPFLCRNIEKERTVEQLVSRLQTKLLRSHELVSGLQAFLCLDTFKLLYLPNTEDSYIDASYLRLRDSD
FLDCQKRKQRWRNWESLLKSVRKTSANTAEVNFDADINALFIP
>gnl|CDD|227890 COG5603, TRS20, Subunit of TRAPP, an ER-Golgi tethering complex [Cell motility and secretion]
MGEYLAIIGEKDNPVYEREYDPINKTSDGEYCRLLNQFIIHASLDIVVWLQWSVNTSYFDCLDSFGDLRI
SAYIMPSGMKFLFIHQNQSRKNARSFLQEVHELYAKTLMSPFYEPDEPIRSQAFDDGVREAARVCL
>gnl|CDD|227891 COG5604, COG5604, Uncharacterized conserved protein [Function unknown]
MGKASKATKKFTKNHLKNTIDRRKQLARSKKVYGTKNRNSHTENKMESGTNDNNKNKEKLSKLYSDVDSS
SSEEEEDGSESISKLNVNSKKISLNQVSTQKWRKELDLLASLAYLQKLSGAFKAAALLNNEEEDLKYTID
DVKFFARLKILQDLRVPYAEILLTPFFEKKGYQNLSSALDVIHIKKFSKSPNGSVLQLLNIFTNHSKARL
DLQKAVNHICKIDSTLSVAVFQVLYSPLLDFFKSSPTEVNDFDTINFLQNSAKNLFELDESYLYKIGFSY
IRQLAIHLKNTVLNPRKVDRKMVYNWQYVHSLDFWLRVISFAVWNGIESKLLRLHYPLVQYTLGVIRLIP
TYQDYPLRFHLLRSLIRLSRGSGVYIPLSPYLVEILKSAISVKNPKASVLRKFDFDSMLKPDTEYLRSKE
YQMGVIEEASSLLLEYFALFSKNIAFPELVGPVISELKRLRKGSKLNKVVLTMVNKLEQQSKFVLEKRNK
VKFSPIDGSTVSSFESDIDWRSTPLGQYVSDQR
>gnl|CDD|444336 COG5605, COX4, Cytochrome c oxidase subunit IV [Energy production and conversion]
MAHTAHAAAHHEGQQHPIKLYLKVWGLLFVLSAFSYLVDYFQVQGMLRWTLIIIFMLLKAGLIVAVFMHL
KWERLALIYAILLPPLAVLVLIALMLIEGDYTFLTRLLFFGA
>gnl|CDD|444337 COG5606, COG5606, Predicted DNA-binding protein, XRE-type HTH domain [General function prediction only]
KEEIEIEESSGNVFADLGFPDEEAEELKLKAQLMAAIRKLIKERGLTQAEAAELLGITQPRVSDLLRGKI
SKFSLDKLVNMLARLGQDVEIVVRPARAAAGHVTV
>gnl|CDD|444338 COG5607, CHAD, CHAD domain, binds inorganic polyphosphates [Function unknown]
RDETAGDAVRRILAEQLDKLLAALAGVRADDDPEALHQMRVALRRLRSLLRLFRPVLPRPKLAALRRELR
DLARALGPLRDLDVLLETLEALAAALPEEERPALARLLARLEARREAARAKLLAALDSARYQRLLAALEE
WLARPPWRDRADKPLRDLLAKRLARRYRRLRKAGAALDLDADDEELHELRKAAKRLRYALELFAPLYPEK
LKALLKALKALQDLLGDHHDLAVLRELLRDLAAEAGLAPELPALGALLALLRARRERLRAELLELWRRLL
AEEP
>gnl|CDD|444339 COG5608, LEA, Dessication stress tolerance protein, LEA/WHy domain [Defense mechanisms]
TLLLSGCASLTPVFEKPEVSLTDAEWGEVSLEEQTFALTLRVYNPNPFPLPLKGLSYDLSLNGVKLAEGV
SDEGITIPANGETTVEVPVTLDLSDLLRWLTHLLNGETLPYRLDGKLKVGGGTVRVPFDYEGTIELPE
>gnl|CDD|444340 COG5609, MpsC, Na+-translocating membrane potential-generating system subunit MpsC, DUF2294 family [Energy production and conversion]
MNPTKGQLEAEISQAIRKLEKEYLGRGPESIKTYILDDMIIVRLEGVLTPAEKFLAETEEGKDLVKQVRT
ELIESIRPQLKELIEEITGVKVVSLLSDISTETGETVIVFVLDEPLEVRLSE
>gnl|CDD|444341 COG5610, COG5610, Predicted sugar hydrolase, contains GT1 and HAD domains [General function prediction only]
MNSLEDLKRAIESGAKVVSFDVFDTLLVRPVAHPEDVFDILARRLRAELLLPGDIEEFARIRVEAEREAR
ERKSGGEEVTLDEIYARLPRLFGLSDALAEALAAAELAAELELCFPNPEVVALLRYLLAAGKRVVLISDM
YLPKEVIEKLLDRNGLGLLFDPLYVSSDYGLSKASGELFDYVLEEEGVDPKQILHIGDNPRSDVQRPRKL
GIQALHYPRASLSRIESLEREGLSLDASLLAGLLRLRRLQSPEGAPGPSVAYRLGYSVGGPLLLGFVDWL
AEQAKKDGIDRLYFLARDGYLLKRLFDRLGPDRGDDIETHYLYGSRRAATLLLPLFLAEEFDLEDFILDG
FLELLRAPFLRLSNLLLAILALLTLLLLGDLGLLLRILSGLRLPALLEERLLIDGARLIAIAAELLLLAL
LYLGQVELLLLRLGFLLSLGGGALRLLLLLLLTDAELRKLLLSVLLAASRSLRRRLPRVGLHSLALYLSL
ELSLIRKLSSG
>gnl|CDD|444342 COG5611, COG5611, Predicted nucleic-acid-binding protein, contains PIN domain [General function prediction only]
MIAIDTNVLVRYLTQDDPEQAAKARRLLEQLTGEEPLFVPLVVLAETVWVLRSVYKLPREEIAEALEALL
GLPNVVVEDREAVEAALALYAEGGADFADALIAARARAAGCEPVVTFDRKAAKLAGVR
>gnl|CDD|444343 COG5612, CnrX, Ni/Co/Cd-binding protein CnrX (heavy-metal resistance) [Inorganic ion transport and metabolism]
MTTQSRRRRWLRILLIASLALNLFLVGLLAGGLLRGPRPPPPRDRALRPAARALPPEDREALRRALRAAR
RELRALRREARAARREALALLRAPPFDRDALEAALARARAAEAALRARVEQALLEFAAQLSPEERRALAE
GLARRHGPDGPPAKR
>gnl|CDD|444344 COG5613, SseC, Type III secretion system effector SseC (host membrane pore formation) [Intracellular trafficking, secretion, and vesicular transport]
TPVAGAPLPSDRVEAEEHHVSGSASKVGQVQLNAPLAVVQPVSLQQARAALTQLLGAVPAGAGADGLIKV
TLPTLSDILLTSPDALEMELTKLTSKLEGNQAKLKIQQIKVAAALRLKQVEENQEQIKKAEEQADEAQKA
GIFSKIFDWISAIVEAVVGAIKVATGVGAAAGALMVAAGVMGMVKAAAETAAADGADLISQEVMDVLGKV
QMAIEIAVAVVDVVVIFGGSAARGIAKAAAKVLEKGAEMVATAATKAAEFAAKVAAIAIGESNMVGQAVE
KMVKKAVEKATKKALKEGGEEKLRKQVVSQALDATRAVAQGANQIAQSVIQAERAELQADIQLLIADQTF
LQFVIDFTEDRLKEEQKRLEELFQGVMEAIFDMLQAQADIAGNLA
>gnl|CDD|444345 COG5614, COG5614, Phage head-tail adaptor [Mobilome: prophages, transposons]
MSAGRLRHRITLQRPTETPDGAGGPIETWEDLATVWAEVEPLSGREYFAAGAEQAEVTHRITIRYRPGIT
PDMRIVYGGRIFNIRAVIDPDGRGRYLEILCEEEVSG
>gnl|CDD|444346 COG5615, COG5615, Uncharacterized membrane protein [Function unknown]
MSLMALLLWLHLLAAVIWVGGMFFAYMVLRPAAAALLEPPERLRLWAAVFRRFFPWVWVAVALLLATGLY
MIYLRFGGFAALPTYVHIMLGLGLVMVLIFLHIFFAPYRRLRRAVAAQDWPAAGAALARIRRLVGINLVL
GLVTIALAVAGRAGG
>gnl|CDD|444347 COG5616, TolBN, TolB amino-terminal domain (function unknown) [Signal transduction mechanisms]
ASPAPAAPDRPSIAVLPFENLSGDPEQEYFADGLTEELITALSRLRGLRVIARTSSFAFKGRAVDLREIA
RELGVRYVLEGSVRRSGDRVRVTAQLIDAATGRHLWSERYDRDLDDLFALQDEIARAIAAALAPR
>gnl|CDD|444348 COG5617, PTPS, Predicted membrane glycosyltransferase TK1552, contains 6-pyruvoyl-tetrahydropterin synthase (PTPS)-related domain [General function prediction only]
MRFKNSLKVTLALLLLLLLALIAFHPLINSGLPSGYDALFHLFKADHLAESWKEGIFYPPWNPYWYNGFP
VFRFYPPLPYYLIALLSLLGLDFITAYKLFAILAIFLGGVGVYLFARLMTGSRKAAGIAAVLYLLSPYFL
EDLYIRGALPEVLALAFLPLILLFLYRWLKTGKKRWLILLALLLALLVLSHHLTAIFGTIFFIFFLLALA
VMDRLRSLKELLALIKAVLLGLGLTSFWLLPALEESKFNPITQVPITGSFDPLKPGSRDNFLEPFSSGLV
FFLLFLLGLIFSKRRAIKLYLFFLLAFILLLLLTTGGFTPIWKLLPTLNNIQFPWRFLLVASLLIALLAG
IVLERVLGWFAALSIIGILFGGLTSRILLGLGLLLFLNSFDVVSFLIALLTLSLLFEEVGFTTQITLFNP
QVQFKLGISGYNVFLEVVEISLPRLLIELNSVYLFYIPQAAQIAQLVIANIETGPALVEVLPLAVRLGEV
ELWAQAESLTSLVITLSLSKRVLLILTSKSIRRLLYSGYRLVLGNGSLLLLLPVPGILELFYKKSKIKIV
>gnl|CDD|444349 COG5618, COG5618, Predicted periplasmic lipoprotein [Function unknown]
MSLKIWAAKALLAALVLLLSGCKVVKLDELAKPIIASSAGFDPAAYADEIWDSKVVPAAEEKAVDLAELL
AALAEDPDAAGEKYGYRAGGGNPWSFFVKGTGTVVAVDTSSREGKLTVDVDGDGKKDVRVQIGPVIRGTA
LRDATGFISFDDFTNQIEFAQLSRALNKRAKKEVLPPLDDASLVGKTVTVTGAFTLWDGPKLILITPVEL
EVQGG
>gnl|CDD|444350 COG5619, COG5619, Uncharacterized conserved protein, DUF2290 domain [Function unknown]
MMNPQTILKDINKLTSKLNEVGLSLDSNFSNIRLLGDNISEISYSSSHLSIALKDLGYLEVYSELLENKH
YNIKLIDGALIQFSYTFERNELLSHRLAFYPSPYLEPFQNEPELYMEDEEYLTILDTHTKNIVPSPIRFD
FDPDQYQEIAHPKSHLHLGSFSECRIPVSSPLTPRWFIKFILRNFYNTAWHKYVEGLPINSVEFEEHITE
IEENKMHFAIS
>gnl|CDD|444351 COG5620, COG5620, Uncharacterized conserved protein, DUF1851 domain [Function unknown]
FENFLERFGPFEDVEPVSEETIERYKGKLPEELLEFWREYGFGGYGDGLFWIVNPDEYEPVLEEWLGGDP
DFSDDRYHPIARTAFGDLILWGEDYGVSLNIRKGTVTVVPSGFELDPEVQFFSLLLDEGLDLEDELGQPL
FDRALEKLGPLAPDEIYGFVPALALGGAEKVENLRKVKAVEHLALLAQLVGPVLYD
>gnl|CDD|444352 COG5621, CrtC, Predicted lipocalin, contains AttH/CrtC domain [General function prediction only]
MRRRRRRLLLLLLLALAAAAQGFAGLGAAAAEGFAPVLPGRPLVFPRDHGAHPDFRTEWWYLTGNLEDAD
GRPFGFQWTFFRSALAPGAPANPSGWASRQLYMAHAALTDITGGRHLHAERFARGGIGLAGASADPFRVW
IDDWQLRSSGDGLFPYRLRASADDFALDLTLTATKPPVLQGDNGYSRKGPDPGQASYYYSQPRLAVSGTL
TLDGRTVAVTGQAWLDHEWSSSLLAPDQVGWDWFSLQLDDGSALMAFRLRRADGSDPWSSGTLIDADGTT
TPLSPDDVRLTPLRTWTSPRTGARYPVEWRLRIPSRGLDLTVEPLLDDQELSTGVPYWEGAVRVSGSHAG
RGYLELTGY
>gnl|CDD|444353 COG5622, COG5622, Protein required for attachment to host cells [Cell wall/membrane/envelope biogenesis]
MMKKTWVLVADGSRARIFRNEGDAKGLNLVEELVHPESRLKTRELGTDRPGRSFDSGGGGRHAYEPETDP
HEEEEERFAREVADRLEKGRAAGAFDRLVLVAPPRFLGLLRKALSKEVRALVVAEIDKDLTKLPPDELEK
HLADALAP
>gnl|CDD|227910 COG5623, CLP1, Predicted GTPase subunit of the pre-mRNA cleavage complex [Translation, ribosomal structure and biogenesis]
VMEIRIPKNQEWRIEVNETQKLKVMVVSGLAEIFGTELANERWYAFRNTKTFIYTFSGCKLKVEGACDLQ
YVSDTTPMPLIFNLHFFLEKRRMFNYEKGPTVMVVGGSQNGKTSFCFTLISYALKLGKKPLFTNLDPSQP
GNIFPGAISAIHVDAILDCQEGLWGQSLTSGATLLRLKNPLVFNFGLTEITENMELYDLQTSKLQEAVKA
RNHLVEDLRLSGCPVDTPSISQLDENLAAFYHTIIKRFEVNIVVVLGSERLYHSLKVIAEKLMINRIFFI
SKLDGFVEVEKEVGRSLQRRSISRYFYGSVNNELSPFTFNVDYKWLVVRIGEMYVANVSALPLGSTEKVG
CVETSDVEVLQNSILAISEAREIEDQATVAGSPILGYVVVINVGAFKRKLRILCPVPRLLPSTALIQGDL
KHVE
>gnl|CDD|227911 COG5624, TAF61, Transcription initiation factor TFIID, subunit TAF12 (also component of histone acetyltransferase SAGA) [Transcription]
MNFFEEDDGVKQHKKSKRGIVDNKNVSQQMLGAYEEQLMKLMHFFEMHSRFARNVGNSTPIGSVDDFQAA
KIRESAMFREGQGLAQEGRAPNLGPQQRPQQWGGNSDVGCGAVYGVNTREFPQLHMQGRVSGIVRHGRFM
PSSMYLPSMGMQLSVGWNWRPVNFRGQSRNANGLFGAWPYLEVKSKDFGEGCGNGIHMNQGLRARQEMMG
LGIMAGGVYGVHDGRSKRRLVDRYPQFQQGQKQVLSPQQRFLHGMERYEASGMPPPAEWAGSNGLHVLPG
RREEVPRGIFRCPSPESSRGEPTHLDYRNGMANNAQRSRFPGTCSIYPENPGKRWCSTKYPQPLVHKGDR
DTETGGCAAPDGGLATPGRDKGPLYERDDLWRLDSKRKLEELQHGGVDEEEKIENEVEELLLSRADGFVE
PVTEFSCRLAKHRKSDTLEVRDGQLHLERNWNIRCPGFVDDIIHMSYRKQKPTVEYCQKKLAIKTEKGIE
LPSDDVDPKDTPSEE
>gnl|CDD|444354 COG5625, COG5625, Predicted DNA-binding transcriptional regulator, contains HTH domain [Transcription]
HRDKVIGRLLMALKVIGIRIYGLLLFLSERSVREHLLKLTGFGAVARELGILGWIGYTLATTPPPKPIEE
IEKEIEEELEEIEKELKEQS
>gnl|CDD|444355 COG5626, Ssr3000, Uncharacterized protein Ssr3000, DUF2288 family [Function unknown]
MSDLRAKLNEETARIEWRELQRHFARGAVIVVAPELDLVEVAVAIAEDNKAAVQAWISEGLLAKPSDEQA
LDWNERDARFWAVV
>gnl|CDD|227914 COG5627, MMS21, DNA repair protein MMS21 [DNA replication, recombination, and repair]
MQLFSVYEGPSDGLDPPAQNTLFPSINLNDGYAFVLVCVYMSSEYTLNALFDVTAERPIGIQESITDVDH
VLVRKQPTEAQQNVPKESIGDLYISLHLGSSVCSFVVLLHGDAVFHELRIVSQQIHLLAVEVHETRQGDN
INKRCGVLSMDEYIWRAEALKAADNIVMKSPNPEEGLVDKILIHQELLSNRCPITLNPDFYPILSSKCNH
KPEMDLINKKLQVECTRVCPRLICSQKEVVDPYVCDHILEKREAMKYIRNSQEQIGCNKRLTKKR
>gnl|CDD|444356 COG5628, COG5628, Predicted acetyltransferase [General function prediction only]
MKVSIERVTAEDKPILENLYQLYLHDLSEFTGILPDADGLFEYEYLDTYWTDDDRHPYLIYVDGEPAGFA
LVRRLPFLESDYEIAEFFVLRKYRRKGIGKRAAHELFKRFPGRWEVKQLEANVPAVAFWRKVIGEYTGGA
YTEEERYIDGRPGLVQRFEVAGP
>gnl|CDD|227916 COG5629, COG5629, Predicted metal-binding protein [Function unknown]
MLMEELPSNSRKGVLYLPMDKDIPKCVGDGLGPFKDHVGLDSLYTPEDRGRTIQLVVRIVTVNVYEDKIL
VPWSDGELARDDTLPDGFRCKQGNEILHSIRSMNDLPSEGWEELIDCWSCHNDYCEFKSMLGGPLTPRPR
EGGLLLGDSYLLINDADLEGKVAYGPNFKLHCSFCNARLGLPNDSSIRKLFRYNKEVIPNGCTKIHPHED
LAYSYLNAYFRDKNVLLLEANQARSYEIWHFYRAILITVEPNRSLSRAEAMKVTIKNTDVPPKITKSTES
SEDIPVSSFNEFYSKLIYDNVMSPTSDIKAGGWKISFVTEI
>gnl|CDD|444357 COG5630, ARG2, N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism]
TNAKQTRQTIVRLLSNMGSAKEIEQYLKRFSQVDAERFAVVKVGGAVLRDDLDALASSLSFLQQVGLTPI
VVHGAGPQLDAALAAAGIETQRVDGLRVTSPEALEIVRRVFQQENLKLVEALEAMGTRARPIPSGVFEAE
YLDRDTLGLVGEVTGVHLAPIEASLRAGSIPIIASLGETPSGQILNINADVAARELVHALQPYKIVFLTG
TGGLLDEDGKIISSINLATDFDHLMAQPWVNGGMRLKLEEIKDLLDDLPLTSSVSITRPSELAKELFTHK
GSGTLVRRGERVLRHDSWDGLDLPRLRDLIESSFGRKLVEGYFDKTKFYRAYVSESYRAAAILTLEDGVP
YLDKFAVLDDAQGEGLGRAVWQRMREENPQLFWRSRHDNPVNGFYFAEADGCYKQEKWTVFWYGLDGFDE
IQACVEHALARPPTLKD
>gnl|CDD|444358 COG5631, COG5631, Predicted transcription regulator, contains HTH domain, MarR family [Transcription]
MTPDAPSPSTADGPIVSSAHLASGRSPELSEFEFALIRANNAFSRWMVRCMAAAGVPDLSPLDVLVLHNV
NHRDRPKRLADICFVLNIEDTHNVQYSLKKLEKAGLVESEKRGKEVTYSATEKGRALCERYREVREECLV
DALEDLGGDEEELSELARLLRLLSGLYDQAARAAASL
>gnl|CDD|444359 COG5632, CwlA, N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis]
MGVNIKKKLIPKNNSYRPGYKMKPKGIVIHNTANPGATAENHANYFNNNNRSASWHYFVDDKEIIQHIPL
NENAWHAGDGTGPGNRRSIGIEICENKDGDFAKAYENAAELIAYLMKKYGIPIDNVVRHYDWSGKNCPHG
LLANGGYRWDQFKADVKSALNGLSTVKPYTKVVKASG
>gnl|CDD|444360 COG5633, YcfL, Uncharacterized conserved protein YcfL [Function unknown]
MKKLLIALLAVLLLAGCSSSPTSGIPVNSQQPLVMESSVLAAGISAEKPTLSQVGGLLRAQATLSNKSNK
PVTLQYRFYWYDKNGLEIHPEESPWRTLTLPGNQTVTIQSVAPNPEAKNYRLYLRLKR
>gnl|CDD|444361 COG5634, YukJ, Uncharacterized conserved protein YukJ, DUF2278 family [Function unknown]
MPLKNYGVLKGKAVDRKRADGSSPHYQIHVVDDGTPYRIAINVKSSEAPSELLYLVDDDFTHPITDKLAA
LPYGFTPLPSKPGGLALDYIRGNLFDRTEMRPLPYDVPGPDNDLNDLIDLYVQRAIADEDAVVYAFGERW
GPENGKPDKYFGFLPGNGIHDIHMNQGNVGRFKGDNGVWQDGGLLIHFPDRNQWAAIFLAFQSQSWHTDD
KTGNPLPGAPPIPPSGAGARVTAPVPLVSPAGIEVLVIILNGADTTLDTVVLTKADDTSKTKSLGALLLK
AGGATPILAPLVPAQGLLGGGGGILAPLGGIGGLLDGGGITNAQGAVVGFTA
>gnl|CDD|444362 COG5635, NACHT, Predicted NTPase, NACHT family domain [Signal transduction mechanisms]
LLLLLALILALLALVLLLDLLVTRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAA
ALLARALSALLLVLLLLESLLLLLLLLLLLAEALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLAL
LILLLDADGLLVSLDDLYVPLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLD
AEDPIPILIELRDLAEEASLEDLLAEALEKRGGEPEDALERLLRNGRLLLLLDGLDEVPDEADRDEVLNQ
LRRFLERYPKARVIITSRPEGYDSSELEGFEVLELAPLSDEQIEEFLKKWFEATERKAERLLEALEENPE
LRELARNPLLLTLLALLLRERGELPDTRAELYEQFVELLLERWDEQRGLTIYRELSREELRELLSELALA
MQENGRTEFAREELEEILREYLGRRKDAEALLDELLLRTGLLVERGEGRYSFAHRSFQEYLAARALVEEL
DEELLELLAEHLEDPRWREVLLLLAGLLDDVKQIKELIDALLARDDAAALALAAALLLALLLALALLALL
ALLLLLRLLLALLALLLLALLLLLLLALLLALLALDLGLAALLLLLLLLLLLLLLLALALLLALLLLLLL
LLLAELLLLALLALVLLSLLLASRLLLITLLLLAAASAALLLLLLLLLAELLLALLALASLLLLLLLALA
LALALLLLAVLLAAALDLLLLLVLLLALLLVLALALSLLLLALALLLAGALLLESSALLAVLLASLLLAL
LLLSLLLLLVLLLALALLASLLLALLLLILLLVLLGSLLLLRLLDDLALLLLLALAAARLLLSSLALVAL
ELARASLGASLVLLALLLATLLLLLLLLLALALALLSLLSLSSLALLSLLGLLLALSLLALLLLSLSLAL
AALLLAAREALTLDRLLSLASLLLA
>gnl|CDD|227923 COG5636, COG5636, Uncharacterized conserved protein, contains Zn-ribbon-like motif [Function unknown]
KYETVHYLTPEAQTDIKFPKKLISVLADNGSLIGLSDIYKVDALINEIINEPDYCWIKMDSSKLNQTVSI
PLKKKKTNLQSGSKLPTFKKASSSTSNLPKKADHSRQPIVKETDSFKPPSFKMTTEPKVYRVVDDLMEDK
EELRKLLRSKAQYMMRKDTDPRTIMEDELLDEDSEDKAIQRSECPPSKTKKKRACKDCTCGLKEEEENEI
VRTRQDKVVKFTEDELTEIDFTIDGKKVSACGNCYLGDAFRCSGCPYLGLPAFEPGDVVSFSMNLDNEFQ
GDDA
>gnl|CDD|444363 COG5637, COG5637, Uncharacterized protein, contains SRPBCC domain [Function unknown]
MTTVEKSITINAPVEEVYAYWRDFENLPRFMKGVESVTVLDDTRSHWVAKGPLGVTVEWDAEITEQVPGE
RIAWRSVEGDIPNAGVVRFEPAGGRGTRVTVTIEYDPPGGLLGKALAKLFGGVPERQLREDLERFKQLIE
TGEIPTGAGRPAGR
>gnl|CDD|227925 COG5638, COG5638, Uncharacterized conserved protein [Function unknown]
MGKKNAKSESADPRFQSVHSDPRFSRLKRGNFKVKVDERFKKEDKDFKTTASVDRYGRPLNQDKATKEID
RLYELENESSESSEITDNEEVASASSELTDEYDPARGEGIISTSESSDESREESEEEKANEISEKAGAVP
EEGNPTKRLAVVNMDWDRVDAKDLFKIFSSFLPYGGKLSKVKIYPSEFGKERMAAEHVQGPPRDIFTPAD
NQPSSQKFGDDNVFSDRDAGEDALIEGDRGNEFDMVKLRQYQLERLRYYYAVVECEDIETSKNIYSACDG
VEYENSANVLDLRFVPDSLTFDDDSREVCTKAPEKYEPRDFVTDALQHSKVKLSWDAEDPHRKDLCKEAF
TDDGIRDKDFSAYTASKLSDEDDDSVMESKMQKLFSEKEIDFGLNSELVDMSDDGENGEMEDTFTSHLPA
SNESESDDKLETTIEKLDRKLRERQENRKERQLKKTKDDSDVDLKDKKESINKKNKKGKHAIERTAASKE
ELELIKADDEDDEQLDHFDMKSILKAEKFKKNRKLKKKASNLEEGFVFDPKDPRFVAIFEDHNFAIDPTH
PEFKKTGGMKKIMDEKRKRLKNNIEQTQDGKPELKIKKRKAEKGDQRQELDRIVKSIKRSGK
>gnl|CDD|444364 COG5639, COG5639, Uncharacterized conserved protein, DUF2274 domain [Function unknown]
MTKLKLGPLPDDKPVKLTIELPADLHRDLDAYAALLAREYGEAVDPAKLIPPMLERFLATDRGFAKARRA
GRSAPAQG
>gnl|CDD|444365 COG5640, COG5640, Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones]
MRRRRLLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVL
TAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLAT
SADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGD
SGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGLG
>gnl|CDD|227928 COG5641, GAT1, GATA Zn-finger-containing transcription factor [Transcription]
QFSEFDSLFRSPPDLFLSCDINSIDLHKHNLPNAAPNIEDNTNRSASIDQSLKDNPEHGDLTENMTPSLP
SGNASISGSPRFVNRIQEHRASSRQSSISSLSDFPISSSSSTSNAASPSTNYTDESNQQFSSYNTTLNPG
GTSSLNPNNNQSDNSNQPHVCSNCKTTSTPLWRRASSESSLPGNNLCNACGLYLKLHGSPRAPISLKSDS
IKSRSSRSSHNNNDSNGENANTESIGNSSASKLTKSWEERPQGRQLLSDAGSLSPRSNNPKSPLLEGLMG
STSLQPVSTPKLVLPSDKKRSTLTTSTATPLWRRTSDKSSFSCNASGSALKPPGSKRPLLPKPDPNSKRS
NATCMNCSSTPTNKILSPPTTSNSPGAQVKLPNQTRSTGATKKKITRRRMNSGKIPALSSSMKNPVPKEF
SPLIPQSTESETPSQSKSSLTSKLEEFESLSLLKSVSSMMNLENDLSSSHDSALFDKLDDSAGVKNSEIH
NMNSDSCD
>gnl|CDD|444366 COG5642, COG5642, Uncharacterized conserved protein, DUF2384 family [Function unknown]
MSTASALGLLLSLSPRSPLDLIELIREGLPASALDRLAELLGLSDDELAKILGISRRTLSRRKKEKKRLS
PEESERLLRLARVLARAEEVFGDEEKARRWLRRPNRALGGRTPLDLLDTEAGAELVEDLLGRIEYGVFA
>gnl|CDD|444367 COG5643, COG5643, Uncharacterized conserved protein containing a metal-binding domain [General function prediction only]
MVGKGRGNLLKMRKTITDFLLLVFLVFSLDITPGKATEENALELKALGFKAAEKAMQGINFEKGDSNVLV
LTDAGYARVNGQTTEKAIDGITDVSGSRTGRSNLLPVHRALWKPLWFTFFDKDTGDAVYIEYDPGTGLLS
ADDTKLPDGQAFSDIGPENINLDTLLNSTNAGNKTVNSKVFGGNEFSILTIANAWAYGAPYDFLQAALFH
NHICPGVSSGYLIAKYIEENYPLKKGESYIVISCPNWCKDDAFQVRWDATPGKGGMFVSALTDEDKESLS
IYGGNPAGILIIWDKKAKTGKAVVLGFDFDKVDALVGVAKWTGPSWASKILYDGAMMDYLNQPEVLVTEL
EEFITDSELLIEMGAAGSNPYEVLG
>gnl|CDD|227931 COG5644, COG5644, Uncharacterized conserved protein [Function unknown]
LPQPQGKHQRKGKKQLENKILHSYEEESAGFDSEELEDNDEQGYSFGVNSEDDEEIDSDEAFDEEDEKRF
ADWSFNASKSGKSNKDHKNLNNTKEISLNDSDDSVNSDKLENEGSVSSIDENELVDLDTLLDNDQPEKNE
SGNNDHATDKENLLESDASSSNDSESEESDSESEIESSDSDHDDENSDSKLDNLRNYIVSLKKDEADAES
VLSSDDNDSIEEIKYDPHETNKESGSSETIDITDLLDSIPMEQLKVSLKPLVSESSKLDAPLAKSIQDRL
ERQAAYEQTKNDLEKWKPIVADNRKSDQLIFPMNETARPVPSNNGLASSFEPRTESERKMHQALLDAGLE
NESALKKQEELALNKLSVEEVAERTRQLRFMRELMFREERKAKRVAKIKSKTYRKIRKNRKEKEMALIPK
SEDLENEKSEEARALERMTQRHKNTSSWTRKMLERASHGEGTREAVNEQIRKGDELMQRIHGKEIMDGED
VSEFSDSDYDTNEQVSTAFEKIRNEEELKGVLGMKFMRDASNRQMAASKISVADLVKVENGDDIDVGELD
EVGGDAIYANAGRREVFPVVEQRRKLAPRKRKEDFVTPSTSLEKSMDRILHGQKKRAEGAVVFEKPLEAT
ENFNPWLDRKMRRIKRIKKKAYRRIRRDKRLKKKMPEEENTQENHLGSEKKRHGGVPDILLKEIEVEDDE
KTPILSPGGDEEVEEGLSIKTQEELVALAFAGDDVVAEFEEEKREIVNREAPKEEDVVLPGWGEWAGPGL
KVIKKKSNTVKKVVGGIKYSKRKDFNLSHVIINEKVNKKDKKFLADEVPFPFETREQYERSLNAPIGREW
TTRASHKRLVRPRTRTKNGEVIEPFKAPP
>gnl|CDD|444368 COG5645, YceK, Uncharacterized conserved protein YceK [Function unknown]
MMKRMLKALLLLLGLLLLSGCSSVMTHTGPKEGYYPGTRADVEMLKDDDTGWGMKPLLALDLPFSAVLDT
LLLPYDYYRSDSDSEKQNQATNAVIPPAPM
>gnl|CDD|444369 COG5646, Fra, Iron-binding protein Fra/YdhG, frataxin family (Fe-S cluster biosynthesis) [Posttranslational modification, protein turnover, chaperones, Inorganic ion transport and metabolism]
MKTVDEYIASLPEEDRERLERLRALIREAAPEAEEKISYGMPAFKLDGKFLVGFAAAKKHISLYPTSGAI
EAFADELAGYKTGKGTIRFPLDKPLPEDLIRKIVKFRVAENA
>gnl|CDD|227934 COG5647, COG5647, Cullin, a subunit of E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones]
MITNAIKIDVPRKTLSEEDFESTWEFIERAIGQIFERLYDSMAILSLMEVYTKIYNYCTNKTRSLESDLR
WKIDFIYLGSRLIQKLVDYAKNYIEEYNRGRSQENMEEFLDELVKFWNRFTKGATMINHLFLYMDRVYLK
KARYDKTLVFEVYSLCLVKEKIESFRLIVDSLINPLLYYVERYRALQSIDRKYIEDAKDMLESLERPSDY
KKENLSYYKSVFEPIFLEETWEFYEMESSEVIELLSVTEYLEKAHKILEREEELVEIYLKVSTKKPLLEV
LEDVLITRHLDDLEEQGSGFREALDASNLEKLQVLYRLLSETKYGVQPLQEVFERYVKDEGVLINIETNY
IFHCKVDVGFLGSRECLPKLYVQKLLSCHDLFPSLVNESFEGDGSIVKALGNAFKTFINGNESADSGPSE
YLAKYIDGLLKKDGKQSFIGKIKDLLQDIITLFRYVEEKDVFEKYYKKLLAKRLLNGRSASAQAELKMIS
MLKKVCGQEFTSKLEGMFRDISLSSEFTEAFQHSPQSYNKYLDLFVWVLTQAYWPLSPEEVSIRLPKELV
PILEGFKKFYSSKHNGRKLKWYWHLGSGEVKARFNEGQKYLEISTFSVYQLLVFLLFNDHEELTFEEILE
LTKLSTDDLKRVLQSLSCAKLVVLLKDDKLVSPNTKFYVNENFSSKLERIKINYIAESECMQDNLDTHET
VEEDRQAELQACIVRIMKARKKLKHGDLVKEVIAQHKSRFEPKVSMVKRAIETLIEKEYLERQADDEIYV
YLA
>gnl|CDD|227935 COG5648, NHP6B, Chromatin-associated proteins containing the HMG domain [Chromatin structure and dynamics]
MQLFDAMPPYLTLQAPLSLIIFHKMVFMSGIRQLHTTLVELEKPLQQLLTKPRKKTKSKRLVRKKKDPNG
PKRPLSAYFLYSAENRDEIRKENPKLTFGEVGKLLSEKWKELTDEEKEPYYKEANSDRERYQREKEEYNK
KLPNKAPIGPFIENEPKIRPKVEGPSPDKALVEETKIISKAWSELDESKKKKYIDKYKKLKEEYDSFYPE
A
>gnl|CDD|444370 COG5649, COG5649, Uncharacterized conserved protein, DUF1801 domain [Function unknown]
MIAKGSGDAPVDAYIAALPGWRGEIARRLRALILEAVPDVEEEVKWGSPVYSVDGWFCGGEAYKKHVKLT
FFRGASLPDPAGLLNGSGKTRRAIDLREGDEIDEAALAALIRAAVALNGE
>gnl|CDD|444371 COG5650, COG5650, Uncharacterized membrane protein [Function unknown]
LLLLAVVTLALGWLQKAPCLQLDWSGGRQYTAACYSDIVPLYGARGLDEGAFPYLDSWGQGRYMEYPVLT
GLFMWLAALLAHGLGGLAPVIAQVAVFFDVNALLLAALWLVTVWALARLAGRRPWDAALVALSPLVILTA
FTNWDLLAVALAAAALLAWARRRPVLAGVLLGLGAAAKLYPLLLLGPLLVLCLRAGRLRAWLRTAGAAAA
TWLAVNLPVALLYPEGWLEFFRLNSERGADPGSIWYVLSLLTGFDGPGEPPEVLNTLSLVLFVLACAAIA
ALALTAPRRPRLAQLAFLVVAAFLLTNKVWSPQYSLWLVPLAVLARPRWRDLLAWQAAEALYWVAIWLYL
LGTSNKGPGLPEGWFVLAVLLRDAAVVALCALVVRDIYRPERDPVRRGGDDDPLGGVLDGA
>gnl|CDD|444372 COG5651, PPE, PPE-repeat protein [Function unknown]
MDFMALPPEVNSARMYAGPGSGPLLAAAAAWDGLAAELASAAASLESVLSGLTGGSWQGPAAAAMAAAAA
PYVAWLTAAAAQAEQAAAQAEAAAAAYEAALAAMVPPAEVAANRAQLAVLVATNFFGQNTPAIAANEADY
AEMWAQDAAAMYGYAAASAAAVALTPFTQPPPTITNPGGLLGAQNAGSGNTSSNPGFANLGLTGLNQVGI
GGLNSGSGPIGLNSGPGNTGFAGTGAAAGAAAAAAAAAAAAGAGASAALASLAATLLNASSLGLAATAAS
SAATNLGLAGSPLGLAGGGAGAAAATGLGLGAGGAAGAAGATGAGAALGAGAAAAAAGAAAGAGAAAAAA
AGGAGGGGGGALGAGGGGGSAGAAAGAASGGGAAA
>gnl|CDD|444373 COG5652, VanZ, VanZ-like family protein (function unknown) [Function unknown]
MKKLQRRRLRWLLVLLWAGLIFYLSLQPGEESPSLSGLVFFGFDKLAHFLAYFILGFLLALALRRSRLRR
RRALLLAVLIAVLYAILDEIHQSFVPGRSASLADVLADTLGALLGVLLVLLLLRLRRI
>gnl|CDD|444374 COG5653, BcsL, Acetyltransferase involved in cellulose biosynthesis, CelD/BcsL family [Cell motility]
ASGLRVEVITDLDDLAALEAEWRALEARAAAASPFQSPEWLLAWWRHLGPGEARLRVLVVRDGGRLVGLL
PLARRRRGGRRVLRFLGGGLSDYNGPLAAPGAEAAALAALLRALAAARPWDVLDLEGLAWDGALANALAD
ALARRGLAVRVRRRSPAPVLDLPGGFEAYLARALSSKTRKNLRRKRRRLEELGELRFEVATTPDELDAAL
DALFALKAARWKARGGTDVFADPRFRAFLRALARRLAARGRLRLSALRLGGRPVAALLGLRSGGRLYFYK
TGYDPEFARYSPGLLLLLELIEAAIERGVRRFDFGRGDEPYKRRWATRERPLYDLVLARPSLRGRLAALA
RAARRALKRLLRRNPWRLLRRLRA
>gnl|CDD|444375 COG5654, RES, Uncharacterized protein, contains RES domain [Function unknown]
MTLYRITKPRYADDPLSGEGAALFGGRWNSKGVPVLYTAESPALALLEVLVHLDAEDLPDPYVLVSIEIP
DDLSIELLDPADLPPDWRAPPAPPATQAIGDAWLAEGRSLGLLVPSAIVPGERNYLLNPAHPDFAKIKIV
EVEPFDFDPRLF
>gnl|CDD|444376 COG5655, REP, Replication initiaton protein REP (rolling circle plasmid replication) [Mobilome: prophages, transposons]
MKFNNDEINKDDEVLSDLSGKKRPWDEKKSNNVKIAELYAKAIESKKKAERIKDCGEVLEFDLTREGDKL
KLAKANFCKVRLCPVCNWRRSLKWSAQLYKILEEILKQKPKARWLFLTLTVKNVKGEELRKTLKEMNKAF
KRLTKYKKFKKNVKGYLRSTEITYNKERGSYHPHFHVLLFVEPSYFKKKENYITQEEWTELWQKALKLDY
EPVVDVRAIKKNKKKTKAIQAAIKETAKYSVKSSDLLTDDEWFNE
>gnl|CDD|227943 COG5656, SXM1, Importin, protein involved in nuclear import [Posttranslational modification, protein turnover, chaperones]
MREELLQCFLQTLDADAGKRTIAEAMLKDLEKQPGFVMALLHICSKDEGDLNVKLSAAIYFKNKIIRSWS
SKRDDGIKADEKSEAKKYLIENILDVFLYSPEVTRTALNAILVNIFSEDKPSDLWGLFPKAANLLRSSEA
NHVYTGLLCLEELFKAYRWKYNDEQVDILMLITALFPILEKVGGNLESQGNYGSVETLMLILKSFKSVCY
YSLPDFLSAIETFSSWFQLSLRILQKPLPNEVLSLDPEVRSLSKWVKCKKWAAYNLYRSFQRYIKKSYKK
SYLSFYITFMTRVPMILATFFKQIEEWGQGQLWLSDIELYFIDFFVELCVDADQTWRLMEPHLQYIISGV
IFPLLCLSEEEEELFENDPDEYIRRYYDFFDNGLSPDLAALFFLIISKSKRKEETFQGILSFLLSILGQS
AATPSNIDNARQAEGALRLLASIKSFITKMSPAANVMEYFIVNHVIPAFRSNYGFLKSRACEFISTIEED
FKDNGILLEAYENTHNCLKNNHLPVMIEAALALQFFIFNEQSHEKFSAHVPETMEKLLSLSNTFEIDPLS
MVMESFVEYFSEELSPFAPELAGSLVRQFLKIAQSLLENSSDTSSVVDDKQMAASGILRTIESMILSLEN
RPLVLKYLEVSLYPVISFILKNEISDFYQEALDILDGYTFMSKEIEPIMWGIFELLLNLLIDEITAVYSE
EVADALDNFITYGKTEFMDAGIYGSICSEISKLCLCSEENFLEDFIGVCRIIESLILNIRDELLSQYLPL
FISVAGSGLKMIDELGPASVYALELIINNLILRPKETLQILEEQGYLQSFFEKWFSQIPKFKRVHDKKLS
VLAILTIIRLQEVGALPELLVHNLGEVLVALVTSLPEAIRLRAKEKDDEDFPEPDLTTEYDECVDASDIS
ETFILEEDPLFETELDQVDPFGYFSEFLSNLQPASGTYYEKIISTLTDSQQDSLQTILNG
>gnl|CDD|227944 COG5657, CSE1, CAS/CSE protein involved in chromosome segregation [Cell division and chromosome partitioning]
MEDLPVVKQLDLAQSPDPPSVKCAEERLRQWEKQHGFALKLLSINLSAFNSMSLRWAALIQFKNYIDKHW
REENGNSILPDENVLIRDELFSLIISSSNQLQIQNALAVSRIARLDFPDEWPTLVPDLLSLLSEKDMVTN
ENSLRVLHHIFKRLRRLFRSDALFLEIAPVLLSILCPFLFSSAYFWSMSENLDESLLSLFQVCLKLIRRY
YDLGFQDIPEFFEDNLDKFMEHFCKLLSYSNPVLQKDCLEDCVYFKLKGSICEIFNLYTTKYPEVITYLI
YDFVEIVWNLLTTITRPYIRDYLVSKSLTVLINVIKYPIRKTAEVLSNVSENLINNLVDLLILPNLILRE
EDLEEWEDDPLEYIREQSKTDYEVNVRPCIENELKDLFDVFGRIAVGHELTVIESEATTPNILDEARQLF
AAYASFGLGVEAVNRMVDFVKFLGSIIYPDLLSPNEIIHLRILRSRIAYILTFRNQLDSSELSESKFLAS
QFFVNYTTACIDAVVLLTTREAYSTIFDDWNFSVCSKIGLLENLILLVLSLMASPSSLEEREFLLQLISR
IIIIDPELIAPLGSEILQLLDNLVEINAKNPSNPQFAHYTFEDIGALVFLKSGMCEITIPTLVLALVPEF
PVLLSEDATELWSYVLQLLSILPEHFSGDVLPSVVKILRQPSLATELLPTKLEILKSYRLLDNPILTTGY
IFKSSGFQPVLGILQYLLGSEPHDALCFLNLTVVETLYLENIYEPYVNLIFVLLLSRLKNSKTERFVIKI
IHVFSLVSFKDSLTVGCDNLISKINQTKNILIVQLYGNWILGFDEIHDSKDRKIHLIGLSNLLRTLHPEV
LSYVSVTNLIISLLSEIFETASGDAIIYELNDDYADDWFDGEISAEEFSRLAQLEFKVDPVHDIDNTKYF
ISFFMEAMNSNLGNENEIVFRLPTENQSLLEQLQEKL
>gnl|CDD|444377 COG5658, SdpI, Bacterial immunity/signal transduction membrane protein SdpI, SdpI/YbgB/DUF1648 family [Defense mechanisms]
MKKKWSLILSLLLILLSLILGLLAYPQLPDQVPTHWNAAGEVDGYGSKLEGAFLLPLLMLGLYLLFLVLP
RIDPKKENYEKFRKVYRLIRVLIVLFMLVIHLVTLLAALGYEINVGRVVPLGIGLLFIVIGNYMPKVRPN
YFVGIRTPWTLASEEVWRKTHRLGGKLFVLGGLLILLAAFLPGPWAFILLLGVILVAALVPVVYSYLLYR
KEEKRG
>gnl|CDD|444378 COG5659, Srso17, SRSO17 transposase [Mobilome: prophages, transposons]
MSAADLEAWAAELDEYCARFADLFPRSDQRERARAYVRGLLSPGGRKSVWPIAEAAGDAGPQSLQHFLSE
SPWDADAVRDRLRDYVVEALGPRDGALIIDETGFLKKGKHSVGVARQYSGTLGKVENCQVGVFLALASDK
GSAPVDWRLYLPESWTDDPERRAAAGVPDEVQFRTKPELALEMIDRALAAGVPFGWVLADAGYGDSTTFR
RALEERGLPYVLAVRSNTKVWPPDPLPGGRGRPPDTPPVSARDLAAALPAKAWRRVTWRDGTKGPRTYDF
AAVRVRPADGDEERARPGGELWLLIERPKGDPGETAYWLSNLPADTPLKELVRVAGLRWRIERDFQEAKQ
ELGLDHYEGRSWRGWHRHVTLVMAAYAFLALERLAANDSKPKSNTWRDANWLPVFPRPKRRKGFEQL
>gnl|CDD|444379 COG5660, YlaD, Anti-sigma-YlaC factor YlaD, contains Zn-finger domain [Signal transduction mechanisms]
MDCETCREALSARLDGELEPVPAAEVDAHLAGCPACRAWLERAAALTRRLRTRPAPEVPDLTDAILAAAP
PAFPRRRAYLRLALALVALAQLALGLAQLLGSDVSAHIHGMATSGHLLNESTAWNLALGVGLLWAALRPT
VAAGLLPVLGAFVAVLLGFSVGDLEAGQVAAERVLSHGLLLVGLALLLLVARQHRGGGDPGNKLRASSSQ
RGRRHLRPA
>gnl|CDD|444380 COG5661, COG5661, Predicted secreted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]
AASPALAEVIVKKKTEYYPVRGRTAAELREQLNRRGPILKTGKRHPGATQWRFRWRFTYQERNGRCRITS
VTVTLDATITLPRWKSRRRADPELRLIWDTLSAALKRHEEGHADIAREAAREIEKALLALPPAPDCAALE
ARANALARRILERHDRRQARYDRQTNHGRTEGANFPDRL
>gnl|CDD|444381 COG5662, RsiW, Transmembrane transcriptional regulator RsiW (anti-sigma-W factor) [Transcription]
MTCDDVEELLHAYLDGELSPEERAEVEAHLATCPACAARLAELRRLRAALRAALAPDEPVPARLRARVMA
RLPRRRRRRWRAVAAADLSAAGFRLVGGRLLPIDGGPDAGHRITLYVRPASAFRQEGGVNVFYWRDGGLG
YALVGDLDRAELAEL
>gnl|CDD|444382 COG5663, YqfW, Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only]
MRIGIDIDGTITDPYPYFIPLLNKYFGKNITLEDITTYDLHEVLGLTEEEFDKFFEENEEEIYTEAPPVP
GAKEVLNKLKDQHELYYITARPKHLEEVTENWLEKHGIPYDELILLGSHDKVEAAKELGIDLFIEDKPDN
ALQLAEEGIPVLLFDTPYNRGPLPEGVIRVNNWQEIKQIIEKLFKKL
>gnl|CDD|444383 COG5664, COG5664, Predicted secreted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]
MRRTALLALLAALVAFPPAASAGWQAVEQVKTYAITGSTGPELYASIGERGPKAGGVGRAIAHTDFKLTW
DRDYERRGDACVLVSAKPKLIITYTLPKPARPLPPATKRRWDTFIAGVRAHEEVHGDIIKDMVKEIEAAS
VGLSVANDPKCQKIRRELQKRLGELSQAQRQRSRDFDRVEMSDGGNVHQLILALVNGP
>gnl|CDD|444384 COG5665, Not5, CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription]
MAAFRSSVAGRILVLLLAVVLALVLALLIAADAQSSPPPVTVRDGVLGLDVVRPGKTVQASSSVTNNGAT
PISNPVLEMHVSSSRVTTRAMLAEASRRSPGEPLGRLVASTGLNASGVSANSAATIAPGANATLTSSAGA
DSLQASSEMALWGPRRVALVVRDGASNPVAVVVTTMIAVPSAPAAPPNAVDYSVLVPIAAQDPAASVSTP
QAFNASATSGRSQHIVQAAKRVGVEWWGDPSLLATPPATPATEEKSSQQPKSQPTSPSGGTTPPSTNQLT
TSNTPTSTAKAQPQPPTKKQPAKEPPSDTASGNPSAPSVLINSDSPTSEDPATASVPTTEETTAFTTPSS
VPSTPAEKDTPATDLATPVSPTPPETSVDKKVSPDSATSSTKSEKEGGTASSPMPPNIAIGAKDDVDATD
PSQEAKEYTKNAPMTPEADSAPESSVRTEASPSAGSDLEPENTTLRDPAPNAIPPPEDPSTIGRLSSGDK
LANETGPPVIRRDSTPSSTADQSIVGVLAFGLDQRTQAEISVEAASRSNPLLNSQVKSFPLGKRSEGAKG
KTQTDRGISNALVNASALITNLKSAARRSDTKQQENDKTEVGGLSEQWKSGISSATEEVEQDANADGEKK
KKEVALLKDAKEGEVKKTLTDLEKDADKECKTAKKDADREKKKQEEKPKSLAGKIWGGIKKVAKASVDGI
TKAVSFIFAKLRQAVKTIFEGAKQLAVGIIESGVRLIVSLIKGRGLVLIGLVKPLLAKFPGIANKICNLI
DKAVNKAVAAVTKLAALLSKIVTAALGFLRSAVDGLFAGLQKIVVTVMGLIKKFNTMDFKKIFGDILEAA
EIGAEIALAFATGGGAVLIQIVKWRATTLPQLLR
>gnl|CDD|444385 COG5671, NdhL, NAD(P)H dehydrogenase cyanobacteria/chloroplast subunit L [Energy production and conversion]
LLVALLYLALAGAYLLVVPAALYFYLKKRWYVASSIERLFMYFLVFFFFPGLLLLSPFLNFRPQRRQIES
>gnl|CDD|444386 COG5672, NdhM, NAD(P)H dehydrogenase cyanobacteria/chloroplast subunit M [Energy production and conversion]
MLLKSTTRHIRIYTAEVQNNELVPSDNVLTLDVDPDNEFNWNEDALQKVYRKFDELVESYSGEDLTEYNL
RRIGSDLEHFIRSLLQKGEISYNLNSRVLNYSMGLPQVESPETE
>gnl|CDD|444387 COG5673, NdhN, NAD(P)H dehydrogenase cyanobacteria/chloroplast subunit N [Energy production and conversion]
MALITTGKKFIRDLEKSGALGVYAPLEGGFEGRYQRRLRAAGYTTLNITARGLGDVAAYLTGVHGVRPPH
LGKKTIGQEAAVGDVYYVPPIATYQLENLPPKSKGLVLWIIEGHILSRQEIEYLTNLPKQEPRVKVVLEM
GGDRYFRWQPLKDTLA
>gnl|CDD|444388 COG5674, NdhO, NAD(P)H dehydrogenase cyanobacteria/chloroplast subunit O [Energy production and conversion]
MAIKKGALVRVVREKLENSLEAKASDSRFPSYLFETKGEILDIKGDYALVKFYVPTPNVWLRLDQLEVA
>gnl|CDD|444389 COG5675, PetH, Ferredoxin-NADP+ oxidoreductase PetH, often fused with N-terminal CpcD domain [Energy production and conversion]
MYNPSAVGSAANTESGNRLFVYEVVGLRQNEETDQLNYPIRRSGSVFITVPYSRMNQEMRRITRLGGKIV
SIKPLNGDSPANGTTPVAEAQSQKADTKSKPMTQAKAKKKKADVPVNIYRPKNPFIGKCISNYELVAEGG
IGTVRHLTFDISGGDLRYLEGQSIGIIPPGTDKKGKPHKLRLYSIASTRHGDNVDDKTVSLCVRQLEYKH
PETGETVYGVCSTYLCNLEPGADVKITGPVGKEMLLPDDEDANIIMMATGTGIAPFRAYLWRMFKEQEEN
PDYQFKGLAWLIFGIPTTPNILYKEELEELQAEYPDNFRLTYAISREQKNPEGGRMYIQDRVAEHADELW
KLIQKPKTHTYICGLKGMEDGIDEALTAAAAKNGVNWSDYQKQLKKAGRWHVETY
>gnl|CDD|444390 COG5676, CytM, Cytochrome cM [Energy production and conversion]
MDNQLAKPEVLIQRIALVILAVLLAILLSILGVHLAQVSDPYVKEVLSLTGDPTRGHAIFQINCAGCHGL
QADGNVGPSLQGVSKRKSDVSLIEQVISGKTPPMPKFQPSPQEMADLLSYLETL
>gnl|CDD|444391 COG5677, PetJ, Cytochrome c6 [Energy production and conversion]
MKKLLSILLLAIALLLLAFTSPALAADLANGAKIFSANCAGCHIGGGNIIRRGKTLKKEALEKYGMDSLE
AIATQVTNGKNAMPAFKDRLSEEQIEDVAAYVLDQAEKGWKK
>gnl|CDD|444392 COG5678, PetA, Cytochrome b6f complex cytochrome f subunit, PetA [Energy production and conversion]
MRTPDISARWQRGKRAITKTLLVAIATVALFLASDLALPQSAAAYPFWAQQTAPETPREATGRIVCANCH
LAAKPTEVEVPQSVLPDTVFEAVVKIPYDTSVQQVLGDGSKGGLNVGAVLMLPEGFKIAPEDRIPEELKE
KVGGLYFQPYSEDQENVVIVGPLPGEQYQEIVFPVLSPDPATDKNIHFGKYQVHVGANRGRGQVYPTGEK
SNNNVYNASAAGTITAIAKQEAGGYEVTIQTADGEAVVDTIPAGPELIVSEGQAVAAGEALTNNPNVGGF
GQKDTEIVLQSPARIKGLLAFLAAIMLAQILLVLKKKQVEKVQAAEMNF
>gnl|CDD|444393 COG5679, PetD, Cytochrome b6f complex subunit IV, PetD, 17 kd cytochrome b [Energy production and conversion]
MSQLLKKPDLTDPKLRAKLEKGMGHNYYGEPAWPNDLLYIFPVVILGTIALCIGLAVLDPAMMGEPADPF
ATPLEILPEWYLYPVFQILRVVPNKLLGIVMMAAIPLGLMLVPFIENVNKFQNPFRRPVATAVFLFGTLV
TLWLGIGAALPIDKSLTLGLF
>gnl|CDD|444394 COG5680, PetG, Cytochrome b6f complex subunit V, PetG [Energy production and conversion]
MVEPLLLGIVLGLIPVTLAGLFVAAYQQYKRGNQLGLD
>gnl|CDD|444395 COG5681, PetL, Cytochrome b6f complex subunit VI, PetL/Ycf7 [Energy production and conversion]
MSGIIAYFGFLAGFTGIALGLYFGLRAVKLI
>gnl|CDD|444396 COG5682, PetM, Cytochrome b6f complex subunit VII, PetM/Ycf31 [Energy production and conversion]
MTGEIFNAAILSFVLVLVGLAWGFLLLKIQGGEE
>gnl|CDD|444397 COG5683, PetN, Cytochrome b6f complex subunit VIII, PetN/Ycf6 [Energy production and conversion]
MDILTLGWVALLALFTFSIAMVVWGRNGF
>gnl|CDD|444398 COG5684, ApcA, Allophycocyanin alpha chain [Energy production and conversion]
MSEVIQVIQNADDELRYLTDGELEQIKAFLPSGEQRLRIAKTLRDNAKKIVDQARKQLLQKRPDITAPGG
NAYGQERAAACLRDFWHYLRLITYGIAAGDKDPIEEIGLIGVREMYQSLGVPLPAMVEGIRCLKEASLSL
LSGEDAAEAAPYFDYLIQAMS
>gnl|CDD|444399 COG5685, ApcB, Allophycocyanin beta chain [Energy production and conversion]
MRDAVTSLIKNYDVQGRYLDRNALDKLKAYFASGTARVQAAALINSNAASIVKDAAAKLFAEYPELIRPG
GNAYTTRRYAACLRDMDYYLRYATYALVAGDASVLDERVLNGLRETYNSLGVPIGPTVRGIQIMKEVVKS
MVADAGGAEVDEYFDHLIRGLS
>gnl|CDD|444400 COG5686, ApcC, Phycobilisome linker polypeptide [Energy production and conversion]
MRMFKITACVPSQTRIRTQRELQNTFFTKLVPYDNWFREQQRIQKMGGKILKVELATGKQGTNTGL
>gnl|CDD|444401 COG5687, CpcA, Phycocyanin alpha chain, CpcA/CpeB [Energy production and conversion]
MKTPLTEAIAAADSQGRFLSSTELQSVFGRFQRAAARLEAAKALAANADSLAKGAADAVYKKFPYTTQMG
GPNYASTARGKAKCVRDIGYYLRLITYCLVVGGTGPLDEYLIAGLREINRTFELSPSWYVEALKYIKANH
GLSGQAAVEANAYIDYAINALS
>gnl|CDD|444402 COG5688, CpcB, Phycocyanin/phycoerythrin beta chain, CpcB/CpeB [Energy production and conversion]
MLDAFSRVVSQADARGEFLSGAQLDALKAFVADGNKRLDAVNRITSNASCIVADAARGLFAEQPGLIQPG
GNAYTNRRMAACLRDMEIILRYVTYALLAGDASVLDDRCLNGLRETYQALGVPGASVARGVQKMKAAAVA
IANDTNGITQGDCSSLASEVASYFDRAAAAVS
>gnl|CDD|444403 COG5689, CpcD, Phycobilisome linker protein CpcD [Energy production and conversion]
MLGQTALGSNSSSPSASRVFRYEVVGLRQSDETDKNSYPIRRSGSVFITVPYNRMNEEMQRITRMGGKIV
SIQPLTAEANSS
>gnl|CDD|444404 COG5690, Ycf58, Phycocyanobilin lyase CpeS/CpcS (= Ycf58) [Energy production and conversion]
IMEFFELSAGKWFSQRTTHHLAFREAESGKSNITVEPLSADDPKVIELCQQHGIDPSLALGGFKVSWDGS
SDWDEEEKQKGSTVLVPIPDPDNPREGKLLRDRGYAEAIPVVGRYHFDEDGALTLTTEYETMSSEERIWF
ASPNLRLRTSTVKRFGGVSLASFCSEIRVV
>gnl|CDD|444405 COG5691, CpeT, Phycocyanobilin lyase CpeT/CpcT [Energy production and conversion]
MTHSTDLITLARWMAGDFSNQEQAFANPPWYAHIRVCMRPLPLEFFDGIGLYSEQAYDYDLDQPYRQRVL
RLVDVGDHIEIENYMLKDEELFYGAGRNPEILKTLTPDQLEKLPGCTMIVEWTGNSFKGSVEPGKGCLVT
RNGKTTYLDSEFEITENTFISLDRGRDPETDEQVWGSLAGPFHFVKRQSFADEVP
>gnl|CDD|444406 COG5692, PcyA, Phycocyanobilin:ferredoxin oxidoreductase [Energy production and conversion]
LETSQPSLREQQHPLIQPLADRIEAVWQEYLDLSPYPLPEDLGYVEGRLEGEKLVIENRCYQTPQFRKLH
LELAKVGNSLDILHCVMFPRPEYDLPMFGADLVAGPGGISAAIVDLSPLNRDRTLPEAYQEPLAPLPIPI
FSQPRELPPWGDIFSPFCLFIRPENEEEETRFLDAVKDYLTIHCQQAIAAEPVSPEQLAEILEGQRRYCT
QQQQNDKTRRVLEKAFGEEWAERYITTVLFDL
>gnl|CDD|444407 COG5693, ApcE, Phycobilisome linker protein ApcE [Energy production and conversion]
MSVKASGGSSVARPQLYQTVPVSTISQAEQQDRFLGRGELNELASYFRSGAKRLEIAQTLTQNSDLIVSR
AANRIFTGGSPMAFLEKPREEEMAMVGAGGGSGDVQEGMKLGTVTYVESGGGFLEGLRSLFSASGSGPIP
AGFRPINVSRYGPSNMQKSLRDLSWFLRYVTYAIVAGDPNIIVVNVRGLREIIENACSGDATIVALQEMR
AASLGYFRNDAEAQEIVSQYFDVLITEFKAPTPSNKLRQRPSSDQQGLQLPQIYFNAAERRPKFVMKPGL
SASEKNEVVKAAYRQVFERDITRAYSLSISDLESKVKNGDISMKEFIRRLGKSPLYRKQFYEPFINSRAL
ELAFRHFLGRGPSSREEVQKYFSIVSKGGLPALVDALVDSQEYSDYFGEETVPYLRGLGQEAQECRNWGM
QQDLFNYSAPFRKVPQFITTFAAYDQPLPDQHVYGSGNDPLEIQFGAIFPKETRNPSTSPAPFGKDTRRI
LIHRGPGINNQNSNPGARGVAPGSLGPKVFKLDQLPGTSGKGSSNGASVKFSESSTQAVIRAAYLQVFGR
DVYEGQRLKVAEIKLENGDITVREFVRILAKSDLFRKLYWTSLYVCKAIEYIHRRLLGRPTYGRQEMNKY
FDICSKKGFYALVDAIIDSKEYSEAFGEDTVPYERYLTPGGLSLRSLRVGTIREDGGTKVQKEETPRFVE
LGTVSELRTEPDIQFRINQGVTKQREQTKVFKLTNTSDKVALKTVIRAAYRQIFERDIEPYIVKNEFTAL
ESKLGNGEITVKEFIEGLGCSDLYIKEFYTPYPNTKVIELGTKHFLGRAPLDQKEIRKYNQILATQGIKA
FIGAMVNSMEYAQVFGEDTVPYRRFPTLPAANFPNTEKLYNQLTKQNKDLVVPSFEPVKARGRS
>gnl|CDD|444408 COG5694, ApcE-CpcD, Phycobilisome linker ApcECpcD fusion protein [Energy production and conversion]
AITTAASRLGTSAFDDTPPVELRPNWSEDDAEAVIRAVYRQVLGNDYVMESERLTSAESLLRNGSLTVRE
FVRAVAKSELYKSKFFYNNFQTRFIELNFKHLLGRAPYDESEVIYHLDLYQNKGYDAEIDSYIDSPEYQE
NFGENIVPYYRGFKTQAGQKTVGFTRMFQLYRGYANSDRGQLAGKSPRLARELAQNTASAVVPPSGGSDG
WSFRPSPLGVTPRTRLGGSAGESGRVYRIEVTGIRSPGYPKVRRSNQAYLVPYEQLSQELQRIHRQGGKI
ASITPA
>gnl|CDD|444409 COG5695, NdhP, NAD(P)H dehydrogenase cyanobacteria/chloroplast subunit P [Energy production and conversion]
MDVKLILLILTAVFTLACLFFGTKNGFYDSDKYHGNGSAH
>gnl|CDD|444410 COG5696, NdhQ, NAD(P)H dehydrogenase cyanobacteria/chloroplast subunitQ [Energy production and conversion]
MATDFNRGIMKFDGADSPAMIAISAVLILGFIAGLIWWALHTAYA
>gnl|CDD|444411 COG5701, PsaA, Photosystem I reaction center subunit A1, PsaA [Energy production and conversion]. Photosystem I reaction center subunit A1, PsaA is part of the Pathway/BioSystem: Photosystem I
MTISPPEREEKVRVPVDNDPVPTSFEKWGKPGHFDRTLAKGPKTTTWIWNLHALAHDFDTHTSDLEEISR
KIFSAHFGHLAVVFIWLSGMFFHGARFSNYTAWLADPTGVKPSAQVVWPIVGQEILNADVGGGFHGIQIT
SGLFQMWRAWGITNEFQLYCTAIGALVMAALMLFAGWFHYHKRAPKLEWFQNVESMLNHHLAGLLGLGSL
AWTGHLIHVSLPVNALLDAGVAAADIPLPHEFLNPSLMAQLYPGFASGVGPFFTLNWGAFSDFLTFKGGL
NPVTGGLWLTDIAHHHLAIAVLFIIAGHMYRTNWGIGHSMKEILEAHKGPPLLFTGPEGHKGLYEVLTTS
WHAQLAINLAMMGSLSIIVAHHMYAMPPYPYLATDYPTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYD
PAVNQNNVLDRVLRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMRALGRPQDMFSDTAIQLQPVFAQWIQ
NLHASAPGTATAPNAGGTVSEAFGGDVVAVGGKVAMMPIPLGTADFMIHHIHAFTIHVTVLILLKGVLFA
RSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSLSVVIFHFSWKMQSDVWGTVNADGS
VNHITGGNFAQSSITINGWLRDFLWAQSSQVINSYGSALSAYGLMFLGAHFVWAFSLMFLFSGRGYWQEL
IESIVWAHNKLKVAPAIQPRALSITQGRAVGVAHYLLGGIATTWAFFLARLIALG
>gnl|CDD|444412 COG5702, PsaB, Photosystem I reaction center subunit A2, PsaB [Energy production and conversion]. Photosystem I reaction center subunit A2, PsaB is part of the Pathway/BioSystem: Photosystem I
MATKFPKFSQDLAQDPTTRRIWYGIATAHDFESHDGMTEENLYQKIFATHFGHLAIIFLWSSGNLFHVAW
QGNFEQWIQDPLNVRPIAHAIWDPHFGKPAIEAFTQAGASNPVNICYSGLYHWWYTIGMRTNTDLYQGSI
FLLLLAAVMLFAGWLHLQPKFRPSLAWFKNAESRLNHHLAGLFGVSSLAWTGHLVHVAIPESRGQHVGWD
NFLSTLPHPAGLAPFFTGNWGVYAQNPDTAGHAFGTSQGAGTAILTFLGGFHPQTESLWLTDIAHHHLAI
AVIFIIAGHMYRTNFGIGHSIKEILEAHQGPGRSGFFKTGLGHKGLYDTINNSLHFQLGLALACLGVITS
LVAQHMYALPPYAFIAQDYTTQAALYTHHQYIAGFLMIGAFAHGAIFFVRDYDPEANKDNVLARMLEHKE
AIISHLSWVSLFLGFHTLGLYVHNDVVVAFGTPEKQILIEPVFAQFIQAAHGKVLYGIDTLLSNPDSVAS
TAWPNYGNVWLPGWLEAVNNGANSLFLTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDF
GYAFPCDGPGRGGTCDISAWDSFYLATFWMLNTIGWVTFYWHWKHLSIWSGNVAQFNESSTYLMGWFRDY
LWANSAQLINGYSPFGTNSLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLVWAHERTPLANLVRW
KDKPVALSIVQARLVGLTHFTVGYIVTYAAFLIASTASLFP
>gnl|CDD|444413 COG5703, PsaC, Photosystem I reaction center iron-sulfur center subunit VII, PsaC [Energy production and conversion]. Photosystem I reaction center iron-sulfur center subunit VII, PsaC is part of the Pathway/BioSystem: Photosystem I
MSHSVKIYDTCIGCTQCVRACPTDVLEMVPWDGCKAGQIAASPRTEDCVGCKRCETACPTDFLSIRVYLS
NAETTRSMGLAY
>gnl|CDD|444414 COG5704, PsaD, Photosystem I reaction center subunit II, PsaD [Energy production and conversion]. Photosystem I reaction center subunit II, PsaD is part of the Pathway/BioSystem: Photosystem I
MAEELTGKTPKFGGSTGGLLTKAETEEKYAITWTSPKEQVFEMPTGGAAIMNEGENLLYLARKEQCLALG
TQLRTKFKPKIEDYKIYRVFPNGETQYLHPKDGVFPEKVNEGREYVGKVDRNIGANPNPATLKFSGKAPY
DV
>gnl|CDD|444415 COG5705, PsaE, Photosystem I reaction center subunit IV, PsaE [Energy production and conversion]. Photosystem I reaction center subunit IV, PsaE is part of the Pathway/BioSystem: Photosystem I
MVQRGSKVRILRKESYWYQDVGTVASVDKSGIKYPVIVRFDKVNYAGVNTNNFAEHELEEVEAPKKKK
>gnl|CDD|444416 COG5706, PsaF, Photosystem I reaction center subunit III, PsaF [Energy production and conversion]. Photosystem I reaction center subunit III, PsaF is part of the Pathway/BioSystem: Photosystem I
MRRLFALILAITLWFGFAPPASADLAGLVPCSESPAFQERAKNARNTTADPNSGQKRFERYSQALCGPDG
LPHLIVDGRLDHAGDFLIPSILFLYIAGWIGWVGRSYLQAIKKSKNPEEKEIIIDVPLAISSMLSGFAWP
LAAFKELTSGELTAKDSEIPVSPR
>gnl|CDD|444417 COG5707, PsaI, Photosystem I reaction center subunit VIII, PsaI [Energy production and conversion]. Photosystem I reaction center subunit VIII, PsaI is part of the Pathway/BioSystem: Photosystem I
MTGSYAASFLPWIFVPLVGWVLPAVVMGLLFIYIESEA
>gnl|CDD|444418 COG5708, PsaJ, Photosystem I reaction center subunit IX, PsaJ [Energy production and conversion]. Photosystem I reaction center subunit IX, PsaJ is part of the Pathway/BioSystem: Photosystem I
MSYFLKYLSTAPVLATVWLSITAGILIEFNRFFPDLLFHPLP
>gnl|CDD|444419 COG5709, PsaK, Photosystem I reaction center subunit X, PsaK [Energy production and conversion]. Photosystem I reaction center subunit X, PsaK is part of the Pathway/BioSystem: Photosystem I
MNSLLAALLATVPTTVEWSPTVAIVMILCNILAIAIGRFTIQYPGVGPKLPLPSPALFGGFGLPALLATT
SFGHILGAGVILGLANAGVL
>gnl|CDD|444420 COG5710, PsaL, Photosystem I reaction center subunit XI, PsaL [Energy production and conversion]. Photosystem I reaction center subunit XI, PsaL is part of the Pathway/BioSystem: Photosystem I
AETRDNDVVKPYNGDPFVGNLSTPINDSGFTKAFINNLPAYRKGLSPNRRGLEVGMAHGYFLVGPFVVLG
PLRDSEYANLAGLISAIGLVLIATACLSIYGLVGFQPPVATSTSPNPPDPLKTREGWSQFAGGFFLGGMG
GAFFAYFLLENFDVLDAILRGLVNV
>gnl|CDD|444421 COG5711, PsaM, Photosystem I reaction center subunit XII, PsaM [Energy production and conversion]. Photosystem I reaction center subunit XII, PsaM is part of the Pathway/BioSystem: Photosystem I
ISDAQVLIALVVALHPGILALRLGTELYK
>gnl|CDD|444422 COG5712, Ycf4, Photosystem I assembly protein Ycf4 [Energy production and conversion]. Photosystem I assembly protein Ycf4 is part of the Pathway/BioSystem: Photosystem I
MTAQTTTTDSQVLRQEVLGSRRFSNYFWATVVSIGGVGFLLAGLSSYLKVNLLPFSDPTQLQFIPQGIAM
GFYGVAGLLLALYLWLVILWDVGGGYNEFNKETGKVRIFRWGFPGKNRRIEINCPLEDVQAVRVEIKEGL
NPRRALYLRVKGRRDIPLTRVGQPLSLSELENQGAELARFLGVPLEGL
>gnl|CDD|444423 COG5713, Ycf3, Photosystem I assembly protein Ycf3, contains TPR repeats [Energy production and conversion]. Photosystem I assembly protein Ycf3, contains TPR repeats is part of the Pathway/BioSystem: Photosystem I
MPRTQRNDNFIDKSFTVMADLILKMLPTNKKAKEAFVYYRDGMSAQADGEYAEALENYEEALKLEEDPYD
RSYILYNMGLIHASNGEHEKALEYYHQALELNPRMPQALNNIAVIYHYQGEKAKEAGDQDEAEALFDKAA
EYWKRAIRLAPNNYIEAQNWLKTTGRSKIDVYF
>gnl|CDD|444424 COG5714, Ycf37, Photosystem I assembly protein Ycf37, contains TPR repeats [Energy production and conversion]. Photosystem I assembly protein Ycf37, contains TPR repeats is part of the Pathway/BioSystem: Photosystem I
MDNSLPIIYLSILLGLLGIAAIFVFRQILKTRRIESTLSRLQKKLKKEKGTAQEYYELGSIYLDKKLYVQ
AIALFQKALKAAEEEEPENLALIYNALGFAYFAQEQYDLAIRQYKEALKLKPDYVTALNNLGHAYEKKKL
TAQALETYEEALKLDPNNKTAKRRAESLRKRLVTSS
>gnl|CDD|444425 COG5715, Ycf33, Photosystem I auxiliary component Ycf33, involved in cyclic electron transport [Energy production and conversion]. Photosystem I auxiliary component Ycf33, involved in cyclic electron transport is part of the Pathway/BioSystem: Photosystem I
MQDFFKNVSRYPRYFITILLGIFFSAFEPLKPLFKNPVTAIALIGFLVGGFAFLYFTLRAMLGLTPL
>gnl|CDD|444426 COG5716, PsbA, Photosystem II reaction center D1, PsbA [Energy production and conversion]. Photosystem II reaction center D1, PsbA is part of the Pathway/BioSystem: Photosystem II
MTTTLQRRTELPFFSSWERFCAWITSTENRIYLGWFGVLMIPTLLTAFIIFGIAFLAAPPVDMDGIREPV
IGSLLFGNNLITAAVEPPSPAIGLHFYPIWEAASMDEWLYNGGPYQLIVFHFLIGIWAYWGRTWELSYRL
GMRPWIAWAFAAPVAAATSVGLVYPIGQGSFSEGVPLGIFGTFDFMLAFQADHNILMNPFHMLGVAGVYG
GALLFAMHGSLVTSVLRRETTESESINAGYFGGQRELTYIVDRGTAGERARLFWRWTMGFNARSIHFWLA
AFPVLGIWTAGLGILLTAFNLNGFNVDNSIWDSQGRFIPTYADLINRANLGIEAMHERNAHNFPLDLAAG
EAVPVA
>gnl|CDD|444427 COG5717, PsbB, Photosystem II reaction center chlorophyll a-binding protein CP47, PsbB [Energy production and conversion]. Photosystem II reaction center chlorophyll a-binding protein CP47, PsbB is part of the Pathway/BioSystem: Photosystem II
MGLPWYRVHTVVLNDPGRLIAVHLMHTALVAGWAGSMALYELAIFDPSDPVLNPMWRQGMFVMPFMARLG
VTNSWGGWSVTGESVADPGFWSFEGVAAAHIVLSGLLFLAACWHWVYWDLEIFRDPRNGEPALDLPKIFG
IHLLLAGLLCFGFGAFHLTGIFGPGMWVSDPYGLTGHVQPVAPAWGAEGFNPYNPGGVVAHHIAAGIVGI
IGGIFHIVVRPPERLYKALRMGNIETVLASALAAVFFAAFVVAGTMWYGTATTPIELFGPTRYQWDQGYF
KKEINRRVQANLAEGKSLSEAWSAIPEKLAFYDYVGNSPAKGGLFRVGPMNNGDGVATAWLGHPVFKDKE
GRELFVRRMPNFFETFPVVLTDKDGIVRADIPFRRAESKYSFEQTGVTVSFVGGTLNGQTFTDPADVKKY
ARKAQLGEPFEFDRETYNSDGVFRTSTRGWFAFAHACFALLFFFGHIWHGARTIFRDVFAGIDPDLQEEQ
VEFGVFQKLGDPTTRKKETV
>gnl|CDD|444428 COG5718, PsbC, Photosystem II reaction center chlorophyll a-binding protein CP43, PsbC [Energy production and conversion]. Photosystem II reaction center chlorophyll a-binding protein CP43, PsbC is part of the Pathway/BioSystem: Photosystem II
METPFNSGLISAEGRDEASTGYAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMLLFEVSHFTPEKPM
YEQGLILMPHVAALGFGVGPGGEVVDTYPFFVIGVIHLIASAVLGFGGLYHSLRGPEKLEDYSPFFGYDW
SDKDKMTSILGYHLIFLGIGALLLVAKAMFFGGLYDTWAPGGGDVRLITNPTLDPGVIFGYLFKSPWGGG
GWIVSVNNLEDIVGGHIWIGLILIFGGIWHILTKPFGWVRRAFIWSGEAYLSYSLGALSMCGFIATMFIW
FNNTAYPSEFYGPTNAEASQAQAFTFLVRDQRLGANIGSAQGPTGLGKYLMRSPTGEIIFGGETMRFWDF
RGPWLEPLRGPNGLDLDKLQNDIQPWQVRRAAEYMTHAPLGSLNSVGGIATEPNSVNFVSPRQWLASSHF
VLAFFFLVGHLWHAGRARAAAAGFEKGIDRETEPALSMPDLD
>gnl|CDD|444429 COG5719, PsbD, Photosystem II reaction center D2, PsbD [Energy production and conversion]. Photosystem II reaction center D2, PsbD is part of the Pathway/BioSystem: Photosystem II
MALYQSIETKYQVRGGTLPGVPLPDGDEPRIGKPFFSYWLGDLGDFQVGPIYVGFFGVTSIFFGFLAIAI
IGLNAAASVTWNPIQFVRQFFWLALEPPDPEYGLGLAPLAEGGWWQIATFFLTGSFLSWWLREYERARKL
GMGTHVPWAFAAAIFLYLVLGVIRPLLMGSWGEAVPYGIFPHLDWTSNFSYRYGNFHYNPFHMLSITFLF
GSTLLLAMHGATILAVSNPGGGREVKQITDRGTAAEREALFWRWTMGFNAGTESIHRWGWWFAVLAGFTG
AIGILLTGTVVDNWYLWWLKHPIAPPYPAIWPPVPD
>gnl|CDD|444430 COG5720, PsbE, Photosystem II cytochrome b559 alpha subunit, PsbE [Energy production and conversion]. Photosystem II cytochrome b559 alpha subunit, PsbE is part of the Pathway/BioSystem: Photosystem II
MAGTTGERPFGDIITSIRYWVIHSITIPALFIAGWLFVSTGLAYDVFGTPRPDEYYTQQRQELPIVSDRF
EAKQQIDEFTQKL
>gnl|CDD|444431 COG5721, PsbF, Photosystem II cytochrome b559 beta chain, PsbF [Energy production and conversion]. Photosystem II cytochrome b559 beta chain, PsbF is part of the Pathway/BioSystem: Photosystem II
MMTSSNPNQPRTYPIFTVRWLAVHALGVPTVFFLGAIAAMQFIQR
>gnl|CDD|444432 COG5722, PsbH, Photosystem II reaction center 10 kDa phosphoprotein, PsbH [Energy production and conversion]. Photosystem II reaction center 10 kDa phosphoprotein, PsbH is part of the Pathway/BioSystem: Photosystem II
MAQRTWLGDLLKPLNSEYGKVAPGWGTTPVMGVFMVLFFVFLLIILQIYNSSLLLEGVDVDWTGLGG
>gnl|CDD|444433 COG5723, PsbI, Photosystem II reaction center protein I, PsbI, oxygen-evolving center [Energy production and conversion]. Photosystem II reaction center protein I, PsbI, oxygen-evolving center is part of the Pathway/BioSystem: Photosystem II
MLTLKIVVYIVVLFFVGLFIFGFLSNDPARNPGRKDLE
>gnl|CDD|444434 COG5724, PsbJ, Photosystem II reaction center protein J, PsbJ [Energy production and conversion]. Photosystem II reaction center protein J, PsbJ is part of the Pathway/BioSystem: Photosystem II
MSGDGRIPLWLVATVAGTGVIVVVGLFFYGAYAGLGSS
>gnl|CDD|444435 COG5725, PsbK, Photosystem II reaction center protein K, PsbK [Energy production and conversion]. Photosystem II reaction center protein K, PsbK is part of the Pathway/BioSystem: Photosystem II
MAALLLLAKLPEAYQIFDPLVDVLPVIPLFFLALAFVWQAAVGFK
>gnl|CDD|444436 COG5726, PsbL, Photosystem II reaction center protein L, PsbL [Energy production and conversion]. Photosystem II reaction center protein L, PsbL is part of the Pathway/BioSystem: Photosystem II
MRTPNPNNQPVELNRTSLYLGLLLVFVLALLFSSYFFN
>gnl|CDD|444437 COG5727, PsbM, Photosystem II reaction center protein M, PsbM [Energy production and conversion]. Photosystem II reaction center protein M, PsbM is part of the Pathway/BioSystem: Photosystem II
MEVNDLGFIATILFVLVPTVFLLILYIQTASRQSSS
>gnl|CDD|444438 COG5728, PsbN, Photosystem II reaction center protein N, PsbN [Energy production and conversion]. Photosystem II reaction center protein N, PsbN is part of the Pathway/BioSystem: Photosystem II
MEPATVLSISIAAVLVAITGFSIYTAFGPPSKELADPFEDHED
>gnl|CDD|444439 COG5729, PsbO, Photosystem II reaction center Mn-stabilizing protein, PsbO [Energy production and conversion]. Photosystem II reaction center Mn-stabilizing protein, PsbO is part of the Pathway/BioSystem: Photosystem II
MRYRALIAAFLALCLGVLTACSEGPAAADRDLLTYDQILGTGLANKCPQLSETTRGSIPIDPGQSYRITD
LCLEPTEFFVKEEPANKRQEAEFVPGKLLTRYTSSLDQIQGTLKVNEDGSLTFTEEDGIDFQPITVQLPG
GEQVPFLFTIKGLVASTQPGLTSINTSTDFEGEFKVPSYRGANFLDPKGRGVASGYDNAVALPAQADSEE
LRRANVKRFDTGKGKISLQVAKVDSETGEIAGTFESEQPSDTDLGAKEPLEVKIRGIFYARVEPA
>gnl|CDD|444440 COG5730, PsbP, Photosystem II reaction center protein P, PsbP [Energy production and conversion]. Photosystem II reaction center protein P, PsbP is part of the Pathway/BioSystem: Photosystem II
MLKRIAALLLLVLSLSLSGCSSATAGLQSYVDSNDGYEFLYPNGWVPVKVPGGPDVVFHDLIESTENVSV
VISPVPEGKTLTDLGTPTEVGYRLAKNVIAPPGSGREAELVNAEQRESDGKTYYLLEYAVKLPNQQERHN
LASVAVSRGKLFTFNASTPEKRWNKVKDLFEQVVNSFTVY
>gnl|CDD|444441 COG5731, PsbT, Photosystem II reaction center protein T, PsbT/Ycf8 [Energy production and conversion]. Photosystem II reaction center protein T, PsbT/Ycf8 is part of the Pathway/BioSystem: Photosystem II
MESIAYILILALAIGTLFFAIAFREPPRIGKKK
>gnl|CDD|444442 COG5732, PsbW, Photosystem II reaction center protein W, PsbW/Psb28/Ycf79 [Energy production and conversion]. Photosystem II reaction center protein W, PsbW/Psb28/Ycf79 is part of the Pathway/BioSystem: Photosystem II
MATIQFFRGIDEEVLPDVRLTRSRDGGTGTATFYFENPKALEKFSTQEITGMYLIDEEGEIVTRPVKAKF
INGGPEAVEATYEMKSEDEWERFMRFMERYAEANGLGFSKS
>gnl|CDD|444443 COG5733, PsbX, Photosystem II reaction center protein X, PsbX [Energy production and conversion]. Photosystem II reaction center protein X, PsbX is part of the Pathway/BioSystem: Photosystem II
MTPSLANFLWSLLAGAVIVVIPATVALIFISQKDKIQRS
>gnl|CDD|444444 COG5734, PsbY, Photosystem II reaction center protein Y, PsbY [Energy production and conversion]. Photosystem II reaction center protein Y, PsbY is part of the Pathway/BioSystem: Photosystem II
MDLRVLIVLLPILLAAGWALFNIGAAALRQVQKFLNKEA
>gnl|CDD|444445 COG5735, PsbZ, Photosystem II reaction center protein Z, PsbZ/Ycf9 [Energy production and conversion]. Photosystem II reaction center protein Z, PsbZ/Ycf9 is part of the Pathway/BioSystem: Photosystem II
MTILFQLALAALVFLSFVMVVGVPVAYASPQNWDQSKKLIWIGSGAWVALVLVVGVLNFLV
>gnl|CDD|444446 COG5736, Psb27, Photosystem II reaction center 11 kD protein, Psb27 [Energy production and conversion]. Photosystem II reaction center 11 kD protein, Psb27 is part of the Pathway/BioSystem: Photosystem II
MKRYLSRLLALVLVVVIGLTGCSSAPTGLTGNYRQDTLAVIESLRTAIELPEDAPNKAEAQAEARQLIND
YAARYRRDSSVSGLSSFTTMQTALNSLAGHYSSYPNRPLPEKLKDRLEQEFKQVEAALKRGA
>gnl|CDD|444447 COG5737, PsbU, Photosystem II 12 kDa extrinsic protein PsbU [Energy production and conversion]. Photosystem II 12 kDa extrinsic protein PsbU is part of the Pathway/BioSystem: Photosystem II
MKRLVRLLALLSLLVGCLGWLGPQPAQALNLNSVTLQSAPVLAVEAPRRNRADAKLATEFGQKIDLNNSN
VRAFRQYRGLYPTLASKIIKNAPYESVEDVLNIPGLSERQKERLQANLDNFTVTPPEPAFNEGDDRYNNG
VYR
>gnl|CDD|444448 COG5738, PsbV, Photosystem II cytochrome c550, PsbV [Energy production and conversion]. Photosystem II cytochrome c550, PsbV is part of the Pathway/BioSystem: Photosystem II
MLKRFILLALATVLFVFQLFVGSAAAAELDEEPRTVPLNEQGETVTLSLKEVSEGKRLFNSNCANCHVGG
ATKTNPNVSLSLEDLAGATPPRDNIEALVDYLKNPTTYDGEEEISECHPSTESWDIFPEMRNLTDDDLEA
IAGFILRAPKVKGPGWGGGKIYY
>gnl|CDD|444449 COG5739, PsbQ, Photosystem II oxygen-evolving enhancer PsbQ/CyanoQ [Energy production and conversion]. Photosystem II oxygen-evolving enhancer PsbQ/CyanoQ is part of the Pathway/BioSystem: Photosystem II
MLRYRSILSLILVLVATFLVSCGSPSATAPPTYTPAQIEQIQRYVPPIQAARDRMPELETLIQKRNWVDV
RNFIHGPLGELRREMTYLSRNLLPKDQPKARELARELFNHLEKIDAAAKERNYQQALSNYQEALADFDAF
LQLIPKAS
>gnl|CDD|444450 COG5740, THF1, Photosystem II biogenesis protein Psb29 (thylakoid formation protein THF1) [Energy production and conversion]. Photosystem II biogenesis protein Psb29 (thylakoid formation protein THF1) is part of the Pathway/BioSystem: Photosystem II
MNNVRTVSDTKRAFYTAHTRPINSIYRRVVEELLVEMHLLSVNVDFRYDPIYALGVVTSFDRFMQGYRPE
ADKESIFNALCQAVGGDPQQYRQDAQRLLALAKRLSAQELLSWLSSPTALGGDEDLQDTLRAIANNPKFK
YSRLFAIGLYTLLEQADPELVKDEEKRNEALKQIAEALHLPEEKLQKDLDLYRSNLEKMAQALIVMEDAL
EAERKKREQRAQEKTT
>gnl|CDD|444451 COG5741, Ycf12, Photosystem II subunit Psb30 (=Ycf12) [Energy production and conversion]. Photosystem II subunit Psb30 (=Ycf12) is part of the Pathway/BioSystem: Photosystem II
DIFDFLSNINWEVIFQLTMVALIVIAGPVVIFLLAARGGDL
>gnl|CDD|444452 COG5742, IsiA, Chlorophyll-binding protein PcbABC/IsiA [Energy production and conversion]
MQTYGNPNVTYPWWAGNARFTNLSGKFLAAHVAHAALIVFWAGAFTLFELSRFDPDLPMGEQGLILLPHL
ATLGIGVGEGGVVTDTYPYFVIGIIHLISSAVLGAGGLFHALKGPEDLEDSEVGQARKFHFEWDDPKKLG
FILGHHLLFLGLGALLFVAWAMFHGLYDPAIGEVRVVTNPTLNPTVIFGYQFHFAFVDNLEDVVGGHIFV
AFLLIAGGIWHILVKPFGWYKKLFLLSGEAILSYSLGGLALMGFVAAYFCAVNTLVYPVEFYGPALELKF
GIAPYFADTVDLPDGGHTSRAWLANAHFYLGFFFLQGHLWHALRAMGFDFKRVPKALSNLGSAEIT
>gnl|CDD|444453 COG5743, LHCA5, Photosystem I light harvesting complex protein, LHCA5/LHCA6/HLI5/Ycf17 family [Energy production and conversion]. Photosystem I light harvesting complex protein, LHCA5/LHCA6/HLI5/Ycf17 family is part of the Pathway/BioSystem: Photosystem I
TSSTYRGRLNNFAVEPKDEEPRFGFTPYAERLNGRLAMIGFVALLLIELLTGQGFLHWLGLL
>gnl|CDD|444454 COG5744, PsbC2, PsbC-PsaL fusion protein [Energy production and conversion]
MTAVISDSPYKGQIPEVGWWAGNFRFVNLSGKLLGAHIAHAGLIVLWAGAMTLFELSRYNPSLPMYEQGL
ILLPHLATLGFGVGAGGEIISTYPYFVIGVLHLISSAILGAGGIYHALLGPEVLEDKGTFAGFFGYDWKD
GDKMTTILGIHLVLLGIGALLLVAKAMFWGGLFDPWAAGGGNVRVITDPTLNPLRIFGYLVGAWGLEGMA
AVNNLEDVVGGHIWIGLICILGGLWHILTKPFAWARRVLVYSGEAYLAYSLGAIAYMGFFAAYFVSVNDT
VYPEVFYGPVGTLETSDGIVSARGWLALFHFVLAVLFLLGHIWHALRSRAIAAGFDFKKGDLVQPPQNNP
QLGNLATPINSSDLTLTFLKNLPIYRPGLSPLARGLEIGMAHGYFLLGPFLKLGPLRDSDQANLAGLISA
IALIVILTIGLSIYGTVSFEKRLETVRPNFSATVPNVPENLQTYDGWSQFTGGFLVGGVGGAIFAYLLLD
NLVRAGAV
>gnl|CDD|444455 COG5745, PsaX, Photosystem I protein PsaX [Energy production and conversion]. Photosystem I protein PsaX is part of the Pathway/BioSystem: Photosystem I
SDVAKKTAKPPYPFRTIWALILLAGNFLVAAIYFHIIN
>gnl|CDD|444456 COG5746, BchB, Light-independent protochlorophyllide reductase subunit B, BchB (= ChlB) [Coenzyme transport and metabolism]
MRLAYWTYEGPAHIGAMRVATSMKGVHYVLHAPQGDDYADLLFTMLERRPDFPPVTYSTVQARDLGRGTA
ELVKDTIRQADERFKPDLIVVGPSCTAELLQEDLGGLARRAGLPIPVLLLDLNAYRVKENWGADETFYQL
VRFLAKPAGRLPQEKTERPSVNILGPTSLGFHHRDDLTELTRLLATLGIEVNVVAPLGASPADLARLPAA
WFNVVPYREIGLGAARYLERTFGQPYTKTVPIGVGATARFIREVQQLLNVQGADPPLEAFSPDGTSAPSR
VPWFSRSVDSTYLTGKRAFVFGDATHAVAAARILRDELGFEVVGAGTYSREFARWVRAEAAGYGDEALIT
DDYLEVEAAIAELEPELVLGTQMERHSAKRLGIPCAVISAPVHVQDFPARYSPFMGFEGANVIFDTVYHP
LTLGLEEHLLDMFGGDFEFHDTAGPSHLGAAAPEPAAASAAEGAPAAEPATEAITAPAASAPGDPVWTAD
AEAELKKIPFFVRGKVRRNTEKYARERGLTEITAEVLYAAKEHLGR
>gnl|CDD|444457 COG5747, BchN, Light-independent protochlorophyllide reductase subunit N, BchN (=ChlN) [Coenzyme transport and metabolism]
TPTGCSDLPILRERGQREVFCGLTGIAWLHRKIQDAFFLVVGSRTCAHLLQSAAGVMIFAEPRFGTAILE
ERDLAGLADANDELDRVVERLLKRRPDIRVLFLVGSCPSEVIKLDLERAAERLSQRHAPRVRVLNYSGSG
LETTFTQGEDACLAALVPRLPAEDPREARSLLLVGALADVVEDQFRRLLAALGIGVVGFLPARRSTELPA
VGPGTVVLLAQPFLSDTARALERRGAKRLAAPFPFGPEGTTAWLEAIARAFGVDPARLDAVTAPRRARAW
RALEDYRELLRGKRIFFFPDSQLEIPLARFLTRECGMELVEVGTPYLHRQYLAAELALLPEGVRISEGQD
VENQLDRCRAARPDLVVCGLGLANPLEAEGLTTKWSIELVFTPIHGFDQAGDLAELFARPLRRRALLKLG
WTE
>gnl|CDD|444458 COG5748, LPOR, Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism]
MSQDQKSTVIITGASSGVGLYAAKALADRGWHVIMACRDLEKAEAAAQELGIPPDSYTIIHIDLASLESV
RRFVADFRALGRPLDALVCNAAVYYPLLKEPLRSPDGYELSVATNHLGHFLLCNLLLEDLKKSPASDPRL
VILGTVTANPKELGGKIPIPAPPDLGDLEGFEAGFKAPISMIDGKKFKPGKAYKDSKLCNVLTMRELHRR
YHESTGIVFSSLYPGCVADTPLFRNHYPLFQKLFPLFQKNITGGYVSQELAGERVAQVVADPEYAQSGVY
WSWGNRQKKGRKSFVQEVSPEASDDDKAKRLWELSAKLVGLATE
>gnl|CDD|444459 COG5749, PobA, Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism]
MSSTRQGPGFNQPFIFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSE
GRVEGGNLRCPYHGWQFDGDGKCVHIPQLPENQPIPKNAKVKSYPVQERYGLIWVWLGDPPQADETPIPD
IPELDDPEWVATSSVRDLECHYSRLIENLIDPSHVPFVHHGTQGNRKQAQPLEMEIESTPNGITASYTAQ
SYYQLFFPFLGNLDETLTITFIYPNTVSVDIGSGLGGRFGIVLYATPIDEGKTRAYAIFFRNFAKKPRWL
RHFLKLLRNGILEQDVIILESQQPALLQLGSYELPTPADRAIIEFRRWLDKQAAGEGPWQEVSPDPQLL
>gnl|CDD|444460 COG5750, Ycf53, Chlorophyll biosynthesis regulator GUN4/Ycf53 domain [Signal transduction mechanisms]
EDAAETQEELLLLQSKEQLLSNELLKDQLIDLISSVYLLQAQEQQANQADQEAEELATIQLDLEENQTEA
LSLLESKLSPQEEDDGIDYTRLRDLLAAGKWKEADEETSKLMLKIAGREEQGWLDPEDIENFPCTDLRTI
DQLWVKYSNGRFGFSVQKQIWQELGGTLDYDYEIYEKFGDRVGWRVNGSWLNYSDLTFSLNAPEGHLPAI
WWLSGGGLKMLVALFSRLETCNL
>gnl|CDD|444461 COG5751, A-ycf53, Photosynthetic regulator, contains GUN4/Ycf53 domain and N-terminal all-alpha domain [Signal transduction mechanisms]
MTDPTTSSPQDTSNDISELREQLQSGSEKNQLQLIPQLANLGEAGLEVLMEFLLSRRDNPPTLVDGKAYQ
VLYQSNSPKAQEFLQTHFPTGVVPLKSERGIDYQPLQQLLAQQDFQEADRLTLQKLCELAGPAAVQRKWL
YFTEVENFPITDLQTIDTLWLVYSEGKFGFSVQRELWLSLGKNWDKLWPKIGWKSGNNWTRYPNEFTWDL
SAPRGHLPLSNQLRGVRVIASLLSHPAWSK
>gnl|CDD|444462 COG5752, K-ycf53, Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms]
MSYCLNPDCLNPQNSDTAKFCQKCGFKLLLKERYRAIKPLGQGGFGRTFLAVDEDIPSHPHCVIKQFYFP
EQGPSSFQKAVELFRQEAVRLDELGKHPQIPELLAYFEQDQRLYLVQEFIEGQTLAQELEKKGVFSESQI
WQLLKDLLPVLQFIHSRNVIHRDIKPANIIRRRSDGKLVLIDFGVAKLLTITALLQTGTIIGTPEYMAPE
QLRGKVFPASDLYSLGVTCIYLLTGVSPFDLFDVSEDRWVWRDFLPPGTKVSDRLGQILDKLLQNALKQR
YQSATEVLQALKRQPPVSYSPIPVAPTKLPIQAQPPDITLKSAKGVDYTQLQDLLAAGKWKEADQETWKL
MCQALGKPKGGYLFKSDIEKLPCEDLRTIDQLWVKYSNGRFGFSVQKQIYEQVGGDYGKFCDRVGWRVYN
SWNDYADLTFSLSAPTGHLPSRRWVGGSQWWRHLETLASRLESCGL
>gnl|CDD|444463 COG5753, BchX, Bacteriochlorophyllide reductase subunit BchX [Coenzyme transport and metabolism]
MATRIIAIYGKGGIGKSFTTSNLSYMMAQQGKRVLQIGCDPKHDSTTLLFGGRSLPTILETSAEKKLAGE
EVSISDVCFKRDGVFAMELGGPEVGRGCGGRGIIHGFEVLEKLGFHEWDFDYVLLDFLGDVVCGGFGTPI
ARSLCQKVILVGSNDLQSLYVANNICSAVNYFRRLGGNVGVLGLVINKDDGSGEAEAFARAAGIPVLAKI
PANEEIRRKSASFQIAGRPPEWGELFEDLAQNIAEAPPVLPKPLDFEEFLRLFGAVSEVRPDLFGAKANL
LPPHEEDLQALRESASVKSEEDLR
>gnl|CDD|444464 COG5754, BchY, Bacteriochlorophyllide reductase subunit BchY [Coenzyme transport and metabolism]
MSDTHRDTSAASDEAPTSGDGMGCHAGAETMRAAARAAGKSEILDRYAADYPAGPHDQPQSMCPAFGSLR
VGLRMRRTATILSGSACCVYGLTFTSHFYGARRSVGYVPFNSETLVTGKLFEDIREAVHELADPERYDAI
VVINLCVPTASGVPLRLLPKEINGVRIIGIDVPGFGVPTHAEAKDVLAGAMLRYARQEAEAGPVQAPRGG
RSDRPTVTLLGEMFPADPVGIGAMLEPLGLAAGPVVPTREWRELYAALDCAVVAAIHPFYTASVREFEAA
GRPVVGSAPVGYDGTAAWLDAIGEACGVAQAKIDAAKNRFLPAIKGALAAAPIKGRITLSGYEGSELLVA
RLLIESGADVPYVGTACPRTPWSAPDREWLEAKGVRVQYRASLEQDLAAVEEFRPDLAIGTTPVVQKAKE
RGIPALYFTNLISARPLMGPAGAGSLAQVINAAIANKARFDAMRAFFEGVGTGDTAGVWEGAPVLRPEFR
AAYAKKLEKLAKAAKAEEM
>gnl|CDD|444465 COG5755, BchZ, Bacteriochlorophyllide reductase subunit BchZ [Coenzyme transport and metabolism]
MLILDHDRAGGYWGAVYVFTAIKGLQVIIDGPVGCENLPVTSVLHYTDALPPHELPIVVTGLGEEELGRD
GTEGAMRRAHGTLDPDLPAVVVTGSIAEMIGGGVTPEGTNIQRFLPRTIDEDQWQSADRAMLWLWTEYGP
KKVPRRKPRKAGAKPRVNIIGPTYGTFNMPSDLAEIRRLVEGIGAEVNLVFPLGSHLADVPRLADADVNI
CLYREFGRLLCEALEKPYLQAPIGLHSTTAFLRKLGELLGLDPEPFIEREKHTTLKPLWDLWRSVTQDFF
GTASFGVVANETYARGLRHFLEDELGLPCTFAVSRKAGVKTDNAAVRAAVLEKPPLVLFGSYNERMYLAE
LGGRAMYIPASFPGAIIRRHTGTPFMGYAGATYLVQEVCNALFDALFHILPLGTDLDRVEATPARLHREL
PWDDEAVAALDKVVEAQPVLVRISAAKRLRDAAERAARAAGEERVTADRVDQAARRLAR
>gnl|CDD|444466 COG5756, Atp1, FoF1-type ATP synthase subunit Atp1, cyanobacterial family [Energy production and conversion]. FoF1-type ATP synthase subunit Atp1, cyanobacterial family is part of the Pathway/BioSystem: FoF1-type ATP synthase
MKLATKEESPDGESSTEPVDDSMQEYYQLQQELLLTTLVLTGIIFISVWIFYSLNIALNYLLGACVGLVY
LRMLAKDVERLGREKRRLGKNRLALFVGLIIVATQWQQLQILPVFLGFLTYKAAIIVYVLRTAFLPDSK
>gnl|CDD|444467 COG5757, AtpR, Na+-translocating membrane ATPase (N-ATPase) assembly subunit AtpR [Energy production and conversion]. Na+-translocating membrane ATPase (N-ATPase) assembly subunit AtpR is part of the Pathway/BioSystem: FoF1-type ATP synthase
MNEILLLLLALLAGLLLGALFFGGLWWTVRRLLRSRRPALWFLGSLLLRTAVVLAGFYLLARGGWQRLLA
ALLGFLLARLLVTRLTRPPPGKLVARKEAP
>gnl|CDD|444468 COG5758, Tab2, RNA-binding protein Tab2, reqiured for psaB translation [Energy production and conversion, Translation, ribosomal structure and biogenesis]
MMTIWELDFYSRPILDENGKKLWELLICDSIDTSPTRLFRYSQFCPSSEVNSIWLAEALQEAIAAAGKPP
DKIRFFRRQMLNMITKACEDLGIPVEPSRRTYALKQWLQERMQEVYPQEPGYQGEAYPPVQLDPPPPQPL
PDALWGDKWAFVSLPAGDFAEMPEWPIPFGEAFPLNLGLASTTPIPGLIIFSGRALPLARWLSGLEPASL
NYEAGPPPGLILETGLSDRWILATLTDPEVLAEAQGFEQAKQQAKGLHFLAVQPDPSSETFAGFWLLQEL
PL
>gnl|CDD|444469 COG5759, Ycf59, Mg-protoporphyrin IX monomethyl ester cyclase BchE, aerobic (=Ycf59) [Coenzyme transport and metabolism]
MVATLPKPRPGTKAAAKETLLTPRFYTTDFDAMARMDVSPVRAEWDAMLAEMRADYNRHHFVRDEEFDQS
WDHIDPELRREFIDFLERSCTSEFSGFLLYKELSRRLKNRNPLLAELFNLMARDEARHAGFLNKAMKDFG
LSLDLGFLTKTKKYTFFKPKFIFYATYLSEKIGYWRYITIYRHLEKHPEHRFYPIFKWFENWCQDENRHG
DFFAALMRSQPKLLNGWKNRLWIRFFLLAVFATMYLRDHERPDFYEALGLDATEYDQEVIRKTNETSARV
FPVILDVDHPRFFARLERCVEANLKLAAIKASGGKVVKFLQKLPLAAAAAWAFLRLYLIKPIDAEALPGT
VR
>gnl|CDD|444470 COG5760, PetP, Cyanobacterial/red algae cytochrome b6f complex subunit PetP (= Ycf86), DUF2862 (PF11061) family [Energy production and conversion]
MEIGQKVKVCRLRDRVSPDIVNKLGKVGTIKGFKMTDGSGVGVVVEFDDGTSTWFFEDELKPV
>gnl|CDD|444471 COG5761, Cp12, Cyanobacterial/chloroplast protein CP12, regulates Calvin cycle by forming a complex with GAPDH and phosphoribulokinase [Energy production and conversion]
MSNIEERIEQAREEARAACDTEGANSPECAAAWDAVEELQAEASHQRQAKPRKTSLEQYCDENPDAPECR
IYDD
>gnl|CDD|444472 COG5762, PM23, Uncharacterized cyanobacterial/plant protein PM23 (seed maturation protein), contains DUF760 (PF05542) domain [Energy production and conversion]
MNFNPNRGSDFFSSEEEQANSLWQYLQSQSPETLAQLSKPASPEVKQIIERNIQGLLGMLPSEHFNVQIT
TSRENLGRLLASAMMTGYFLRNAEQRMELEKSLQGSESLSSDS
>gnl|CDD|444473 COG5763, Ycf20, Cyanobacterial/chloroplast protein Ycf20, involved in dissipation of absorbed light energy, DUF565 (PF04483) domain [Energy production and conversion]
MQNTRLNTLVDVLGARLEQWFSNPWRRLSLLIISLLFGFFLGSAISTIAGQLALWDIIVAAVLVIFTEVV
SRIVYRRSGKKRRSLWLELLNAFKIGLTYGLFLEAFKLGS
>gnl|CDD|444474 COG5764, Ycf34, Cyanobacterial/chloroplast FeS cluster protein Ycf34, regulator of photosynthetic electron transport, PF10718 domain [Energy production and conversion, Signal transduction mechanisms]
MCICVNCYYVDRCQTYHAVETQHQQPHLTETPDFEPVEPTINVNIRTKEDYIEMEWDVVGCESFLRDTGK
WARLRPGELVPT
>gnl|CDD|444475 COG5765, Ycf35, Uncharacterized cyanobacterial/chloroplast stress-induced protein Ycf35, DUF1257 domain [Energy production and conversion]
MSHFSTIKTQIRNLESLKAALRDLGYDVKEGAQPVRGYQGQTRTAEVVIRQDNGYDIGFRWNGGEYELVA
DFWGQPLSVERFLNKVTQRYAYHTVLAETAEQGFQVAEEEVGEDGSIRLVVQR
>gnl|CDD|444476 COG5766, Ycf36, Uncharacterized cyanobacterial/chloroplast membrane protein Ycf36, DUF1230 (PF06799) domain [Energy production and conversion]
MESSVSNCPVPPEQQPINEYEQLKESWFFRWATLEWRSYLRKLAWVWLWSWLIAGPIAAASFPPQKYPVQ
FILCGAAGASLLVILVLLRLYLGWSYVRDRLLSETIFYEESGWYDGQTWTKPPEVLTRDRLIVSYQVQPI
LQRLQQTFALLALLLLIGGLIWQLL
>gnl|CDD|444477 COG5767, Ycf51, Uncharacterized cyanobacterial/chloroplast membrane protein Ycf51, DUF2518 (PF10726) domain [Energy production and conversion]
MLTTADFLQYTQWSGIATLAFAVLTILAFIFKWGIRFRLVGVTGFMGVLTGGLFALSLGPFTRTVIPGAV
RYSLVYDNGANQAVIAVPPTITESELEATLRQAASDLFSYGRLGGGDNQLTIRARTIIHPEPGVSEPLYL
GQVKRSLASREDDQMEIEIFPDNFAKLPQSAN
>gnl|CDD|444478 COG5768, Ycf55, Cyanobacterial response regulator with REC-Ycf55 domain architecture [Energy production and conversion, Signal transduction mechanisms]
MSDRPLKLLLIDDDPIFRLGLRTALEQFPDLQVVAEADTLTAALQILAELAQENAPDLVILELGLTRSIN
QQSGLQLCQQLKQQYPNLPILLLTSVQDPELLLAAKALGVEGYCPKGTPISELVAAIRQVAAGETYWQSA
SLLNSPPLATLSSSPFARWRSRLRQSGLQQIEAALAQVTAQLQNPGLSLLDRLFLAGRRRELLAARWLVS
QLLPQPVPRQQEPANPPPSPEDPLSSPASPANPSLTPLPTSPPLLSPRALQSTLFDSTLAKLQSGLQNLT
GIPLEIDILREDKKRELLYLILQQLEDLLDELRFSQITPEQLPEKRSLILRDLWQAATTDFFGKYYTLKI
GNSDVEIVEVLLQEAEIVQTEILNKIPLVTELFSYLLFQTPLTIDNTSYAAGSPEAKERAEALLENLLIQ
VANGVVQPLLNRFADVEEIKQNFYDRRLISTREIERFRNNLSWKYRWNRYWQEPKAIFESRYELFVLAPR
GIAKTSIYAPRQQELEQLSGIPLAVTLALELRDAIAPRLRALVSFVGSGVVYLLTQVIGRGIGLIGRGIL
QGIGNSWQEKRFKKNSSRG
>gnl|CDD|444479 COG5769, Tic20, Cyanobacterial/chloroplast membrane protein Tic20/Ycf60, involved in chloroplast protein import [Energy production and conversion]
MTWRGSTTVKDRIFAALPYLLPLIDALPFGIFLFRQFPLLQILYLPLLPLIQIYYGIPFAGLIIFFVLFL
AVVRNEKISHFIRFNTMQAILLDILLILCGLVLQILGQGIPGGGLLIETLSNTIFLGTLAAVVYSIVQSL
RGRYAEIPTISEAVYMQVR
>gnl|CDD|444480 COG5770, Ycf66, Uncharacterized cyanobacterial protein with Ycf66_N domain [Energy production and conversion]
MVNFGLNSASLLGIVLAVAGAGLYFLRSFRPELARDHDIFFAAVGLLCGFILLFQGWRLDPILQFGQFLL
TGSAIFFAVESIRLRGVATEQA
>gnl|CDD|444481 COG5771, Pro0776, Uncharacterized cyanobacterial/chloroplast protein Pro0776, algal eyespot protein with methylated Arg, DUF1350 (PF07082) domain [Energy production and conversion]
MEWQEISGNWVLIPPRPKGIIHFLGGAFVATAPQLTYRWLLEQLAKQGYAIIATPFVNTFDHQAIAREVL
NRFENALERLQARQGLGKRYLPIYGLGHSMGCKLHLLIGSLFGVERAGNILISFNNYPARRAIPFLEQLN
LLPAFDVEFTPSPEETNRLIQKSYQVRRNLLIKFNNDTIDQSASLVPILQQRFPDMVTLQTLPGNHLTPL
GQDIKWQTGNYFTPLDALGQWFKQEVYRDLNQLKREILRWLN
>gnl|CDD|444482 COG5772, Tic21, Cyanobacterial/chloroplast membrane protein Tic21, involved in chloroplast protein import, DUF3611 (PF12263) domain [Energy production and conversion]
MSNESESSSLPPAIQRIANTFRRTGWIGFWLQLVLGVVSGLLLLFAIFSRNGSQQNNPGIGFGLFLAVCG
LLVLGFSIYWAFRYTRLGRRLQSPDPALRPKKADTIQLLRIGLIVNLVGMLLTILGAEAIVGVLLAKSLS
QPQGVAIYNPSRIIRPLDIFVVQANTNTIAAHFIGIVVSLWLLNRITQH
>gnl|CDD|444483 COG5773, Pro0765, Uncharacterized cyanobacterial/plant membrane protein Pro0765, DUF3082 (PF11282) domain [Energy production and conversion]
MTDSNPTPKTSESETPKPTPLRCLTGAVISGGLAFALYSLTSSIATTFAAKPIHSDNQLAINIASAVRTL
VVGVAALATGIFAIVALGLILLAIQLLIQRLTKRKSP
>gnl|CDD|444484 COG5774, Ccb1, Cytochrome b6 maturation protein CCB1 [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
MDTPILPSTFLLTLLLAVGLFFFIRASVKDRTEQVQLISEQPEASLLPQLQQYFESRAYRVAAVDAEQNQ
VTFEGFVRPSWFLAIFLTLLAALGLLCLGLVLSLLFPSLGWLFLGLVLLAPLAGIFYWQKAGRPEQVSLK
LESADSDHPGQSLLTVTAHRDELIALQQALPLKPAE
>gnl|CDD|444485 COG5775, Ccr2, Thylakoid membrane protein DAC/CCR2, involved in assembly of b6/f complex and response to cold stress, DUF3007 (PF11460) family [Energy production and conversion]
MRRIDVIGIGLGVFLAGGLAYLGLQLAGLDSLSAGIWSQALLVGGLVGWLLTYLFRVVTKNMTYNQQRKD
YEDAVLQKRLDEMTPEELAKLQAEIEQEKQAQS
>gnl|CDD|444486 COG5776, PH, Bacterial PH (pleckstrin homology) domain [Energy production and conversion]
MGIREEVFYEGGPHIGDLIINLLLGLTVIGLPLTVGAIVRALWLRYRITNRRISVTGGWMGRDRTDIVYS
EIVKVVKVPRGLGLWGDMVLTLKDGSRLEMRAVPRFREIYDYINEKLAAKTGKPSTAI
>gnl|CDD|444487 COG5777, Pro0498, Uncharacterized cyanobacterial/plant membrane protein Pro0498, contains N-terminal TPR repeats [Energy production and conversion]
MSSESLEIFKQEYQAGKAAFERGRYRQSVENLEKASALVARNSRLGGEVQIWLVTAYEAAGQTEDAIALC
QQLKRHPHPETRKQAKRLLYILEAPKLKRPKEWMTEIPDLGALSENDSKTRRAASPSKKSPKKKPPEPEP
VDLSQVNTKDNRFIWVALIAIGLTLGGLVWLS
>gnl|CDD|444488 COG5778, Pam68, Photosystem II assembly factor PAM68, DUF3464 (PF11947) domain [Energy production and conversion]
MASESSRDRLPFEPRKKRKKPAKAPPAPPAPSKSEKKKKAAKKPKREKESMAIPEVVSQRMVRRMALFSG
IPTALGILTFVVSYLIVSNDWFELPNTAVLLVSMGFFGLGVLGLSYGVLSASWDEERSGSLLGWQEFKTN
FGRMTAAWREARQKSKEK
>gnl|CDD|444489 COG5779, TAP/TPM, Thylakoid acid phosphatase, contains TAP/TPM domain [Energy production and conversion]
MQNRFPRRLLVSLAAFLLALSTWAIAPPAQAYNNPELLPDEQTPVVDLANFLTDIQEEALVKDLEEFEAE
TGWKLRVLTQYDRTPGRAVKNFWGLDDKSVLLVADSRGGNLLNFSVGDAVYELLPRTFWVELQTRFGNQY
FVRDNGEDQAILQALETVKTCLRQGGCNVVPGLPREQWILTLITSILGGVICGFAAQPRKEGQVFAWQWA
LIFSPLWGILFIAFGIGPVVTRTSDWLPLFRNVSGFLLGALVAYLTPILNQSSPSETE
>gnl|CDD|444490 COG5780, Ape1, Acclimation of photosynthesis to environment protein APE1, affects chlorophyll fluorescence, DUF2854 (PF11016) domain [Energy production and conversion, Signal transduction mechanisms]
MLRQISLGTLGLVVGGILTVVGFVAYATDNATLNLAGFFYGIPLLLGGLALKAAELKPVPFSQPTSPEVL
ALREQQATPTQNQIRKDVTRYRYGQEAHLDESLERLGLSPTDEERPVLVGLRETEIDGAYTLILEFDSPL
VPLETWQEKQEKIERFFGPGIRAEITQPEEDRIELALITTA
>gnl|CDD|444491 COG5781, Ccb2, Cytochrome b6 maturation protein CCB2 [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]
MAKSDPNRVLRLLPLFAGGLGGTLLLINRLLTPELTDSQARSDALGVILSAVLILTGLLWQQVQPRSPDA
VTLIGEEGFELAPDLPEAVKTELAWASHLLLTNTVTRSLVVYYQGKVLLRRGILGENSEVKPGAIVQRVL
ETQKPVYLVNLKLYPGRIEFDYLPENTQGVICQPLGDRGVLILGANAPRSYTKQDENWIEGIADKLANTL
SRSLNASAAE
>gnl|CDD|444492 COG5782, NdhV, NAD(P)H dehydrogenase cyanobacteria/chloroplast-specific subunit NdhV, DUF2996 (PF11210) domain [Energy production and conversion]
MAEETKSTPEATKPAAAKAAKAKKEKPPAVEDKPFEEFIQQHYLPALQKALTDQGIEDLELSFKKQKLPV
VGLESEECWQVIGSWQNGQRQFNLYFPDEDISGKKAFSCAEGGSKPSTLESFLIDERKVTLDLLVSYTVQ
RLNGQKWLGRN
>gnl|CDD|444493 COG5783, CSAP, Chloroplast senescence-associated protein CSAP, DUF1997 (PF09366) domain [Energy production and conversion]
MELQFTASQSVELPVPEQPIPIQHYLRQPQRLVNALADPSRIEQLGEDRFRLKMRPLNFMDLHIQPTVDL
KVWADAQGTVHLRSVDCEIRGIDYINDRFSLDLKGKLAPYEKNGQTYLQGQADLEVSVDLPPPLWLTPKP
ILEATGNGLLKSVLLTIKQRLSHQLLSDYRRWANSQQQIEA
>gnl|CDD|444494 COG5784, Pro1025, Uncharacterized cyanobacterial/plant protein Pro1025, DUF3531 (PF12049) domain [Energy production and conversion]
MEVQFREFNPFDLWIWLEFSTVPSEMEKQYVEEVFDSWFYLGKLGGFNAENLQVQETGLDLSYMDYDNDG
ADNSLMALMHNMGEFEYQGTWGRCWFDLGTSDAIALDVLINALRQLSKEYVEIEELIIGGENEDWPVEDS
RDSFFYDN
>gnl|CDD|444495 COG5785, Cr066, Uncharacterized cyanobacterial/chloroplast protein CR066, DUF3172 (PF11371) domain [Energy production and conversion]
MKRKPRYSRPPRRSRPPPSGGKKSPFNYTTIAILGGVFILGIGIGIAFSSTTTFNPENVASREFIDRSAP
NPELCVQYGASAIVTDMRVFVTLNPFNVYVTQPSMQPGCVLRRNNWAILEQRKLVTSEQVRDCKNRMNTF
GFTGDLESKPEIDCVYQNDAAGNLFLNQPGAVGPPPETDNF
>gnl|CDD|444496 COG5786, LPA3, Cyanobacterial/plant protein LPA3, possible role in PSII assembly, DUF1995 (PF09353) domain [Energy production and conversion]
MTELPKTLEEAIAQAKEATQAALADGYTRIQVELVFPEIALQAQSLALQFLPLFEEYGSGLKVFFPDTGA
AALARRDWGEVPFKITDLGTSRSPIESKIQPEDQIFLVVAPSAVEVAQVEKLCNLAGDRPVILLIPQLED
VSIVGIGYAARQLRERFLSTLESCYYLRPLDGAAVFRCYPSLWQVWLEKEGEYQLIAELPQKPVGDELDL
ILLKATPQTDEDSTTNASPAKKPGLFASLQRFLKALSQ
>gnl|CDD|444497 COG5787, Alr2454, Uncharacterized cyanobacterial/plant protein Alr2454, DUF3067 (PF11267) family [Energy production and conversion]
MTGQELRQLLLSKWGRSYDIQLRRTKGKIFLQVMWKYLEQASFPLSEAEYLAHLDAIANYLNAWGGVEQV
QQYIETTRERPRLGKAVSIPLDLGERASEWLL
>gnl|CDD|444498 COG5788, SipA, Cyanobacterial/chloroplast protein SipA, regulator of sensor kinase NblS (Hik33), DUF3148 (PF11347) family [Energy production and conversion, Signal transduction mechanisms]
MSKEFAIGDKVRLIALPPYLKTADPMPMLRPPDLIAIGEEGIILDRRPGGYWGVRFTRGAFLLESQYLEA
VES
>gnl|CDD|444499 COG5789, Pro1627, Uncharacterized cyanobacterial/plant protein Pro1627, DUF3143 (PF11341) family [Energy production and conversion]
MTLPSADTPLYNHPLPQIEQWLRSLGCQQDEEELHCWHVERPDWKAEICLDIEELTVRYLNAGEDGQDIQ
RSFKYSLSRQDIEQAVFSGP
>gnl|CDD|444500 COG5790, NdhS, NAD(P)H dehydrogenase cyanobacteria/chloroplast-specific subunit S (CRR31) [Energy production and conversion]
ILPGSTVKVINPDDTYYGFEGLVQRVSDGKVAVLFEGGNWDKLVTFRLSELEVVEPTAK
>gnl|CDD|444501 COG5791, CRR7, NAD(P)H dehydrogenase cyanobacteria/chloroplast-specific auxiliary subunit CRR7 [Energy production and conversion]
MPDPLMYQEDAYVVLETNQPEQFLTPAELLEKLKEILAQRQDDLPRDLQKFPSLEAQAQYLLDTACELDL
GPGGYLQWYAVRLEK
>gnl|CDD|444502 COG5792, CBS-CP12, Fusion of CP12 with N-terminal CBS domain pair [Energy production and conversion, Signal transduction mechanisms]
MKAADIMTTDVVTIRGSATVAEAVKLMKEKGLRALIVERRHEQDAYGIVTETDIVYKVTAYGKDPKKVRV
YEIMTKPCIVVNPDLGVEYVARLFANTGIRRAPVIQGKLLGIISVSDILTKGDFVEQPKSLLLEQEIQQA
IEDARAICAQKGATSPECAAAWDIVEELQAEAAHQRAEKLEKTAFEEYCEENPEALEARIYDT
>gnl|CDD|444503 COG5801, Spo0A, Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
MMEKIKVLIADDNREFCELLEEYLSSQPDMEVVGVAYNGLEALELIEEKKPDVVILDIIMPHLDGLGVLE
KLREMNLEKRPKVIMLTAFGQEDITQRAVELGADYYILKPFDLDVLAERIRQLAGGKAESETSKKKSSPE
TASVDKARDLEAEVTNIIHEIGVPAHIKGYQYLREAILMVVEDVELLGAITKELYPSIAKKYNTTPSRVE
RAIRHAIEVAWDRGNVETLNKLFGYTVSNGKGKPTNSEFIAMIADKLRLEHKVS
>gnl|CDD|444504 COG5802, Spo0B, Stage 0 sporulation initiation phosphotransferase Spo0B [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
IELLRHARHDWMNHLQLIKGYLSLGKLDRVQEIIEEIIEEAEEESKLSNLGLPSLSEWLLTFNWRYDPLR
LEYEVEGEVKDLSAYDERLAELLEEIFSLLNEHLDPYSENHLTITLQQTEESLRLFLDFEGKFTDLEELE
KALEKILQGRVEIESFTVTEEECTVRLQAE
>gnl|CDD|444505 COG5803, Spo0F, Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
MMKKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKE
IDPDIPVIMMTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLLK
>gnl|CDD|444506 COG5804, Spo0E, Stage 0 sporulation regulatory phosphatase Spo0E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
MSMELEELLKKIEELREELNELAEEKGLTDPEVLELSQELDKLLNEYQRLKKKKK
>gnl|CDD|444507 COG5805, KinA, Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
MSTKLYDFIHEVKKDGTPIWINNEVLRMAIEITEELETILENLPDAIIAVNREGKVIYINPAMEKLLGYT
SEEIIGKTIFDFLEKEYHYRVKTRIERLQKGYDVVMIEQIYCKDGELIYVEVKLFPIYNQNGQAAILALR
DITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCD
KEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELMAR
SEKLSIAGQLAAGIAHEIRNPLTSIKGFLQLLQPGIEDKEEYFDIMLSELDRIESIISEFLALAKPQAVN
KEKENINELIQDVVTLLETEAILHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTITIH
TEEEDNSVIIRVIDEGIGIPEERLKKLGEPFFTTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFT
ITLPLS
>gnl|CDD|444508 COG5806, KinB, Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
IKDLLLNLLFILLPIFIYQIFWEDRRRNKPVKNRMLIGVLSSIAIILCMTFPIHITDGFIFDLRQVPIIL
GTLYGGWRVGLFLFLILLLYRFYLGGEGVFVTLLVYTVILILPLLLRRKFHRLSRKGKIVLAILLSFLSA
LLLLLLAIIFIADISELLDFILYFIIIQLLAMLIAVYLIENLIENILLRKELQRAEKLEVVSELAASIAH
EVRNPLTVVRGFIQLLQEPELSDEKRKQYIRIALEELDRAEAIITDYLTFAKPQPEKLEKIDVSEELEHV
IDVLSPYANMNNVEIQTELEPGLYIEGDRQKLQQCLINIIKNGIEAMPNGGTLTIDVSIDKNKVIISIKD
TGVGMTKEQLERLGEPYFSTKEKGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITLPLA
>gnl|CDD|444509 COG5807, KinC, Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
MIKQRATDFYHIEEKNQEFKLTEDSEFKFKQLFDSILEFVFFIDSKGEILECNDFAEDLYGLSQNEYIGK
TFVEEKCILKDEQLYNKEAFDRIEISYLTKNGEFDEIIYPIYYKDGVILGLITVYRDITKRKEAEDKLLR
SEKLSVAGELAAGIAHEIRNPLTSIKGFLQLLQESREDSEREEYFNIIISEIDRINTIITELLVLSKPKK
FNFKKLNLNDVLEDVIALLSTEAILKNISIKYDLADDEPVINGDKNQLKQVFINLIKNAIEAMETGGNIT
IKTYVEGDFVVISVKDEGIGIPEEVLEKIGEPFFTTKEEGTGLGLSICKKIIEEHNGTIEVESKPGKGTT
FTIYLPLY
>gnl|CDD|444510 COG5808, KinD, Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
MKGIQKRVGLYIILVIIPTIIISAFFYEDERDKMIEENLQELNLYRNKLDYFIETLARLDSLATADIKVI
KGILDETYDKDPRFSGLYILDESLMGAKATKKTVISSDITSTISAPIMDKELTNFLLASIRMDYIRALIN
ILDPDKYIEIVDQNGQSVFTSGHREESKSVSNKLDKVPWEVEVYPNPVTNDELGQALAIRKLIILVLISI
IFLLLQYNLLKRKTLLERVIQEINTQKLELIGTFAASTAHEIRNPLTSIKGFIQLLQEKYPELEDQKYFD
IIQEEIQRINQIVSEFLVLGKPTAKKLELDDLNELIEEILSIIDSEANLKNIRVEKQSLDEPLHIKCDKD
RIKQVLLNLIKNAIEAMKEGGKLTISIENDDEKAVIEVIDNGEGIPEDIIDEIFEPFVTTKEGGTGLGLS
VCKRIVEMHGGEIDIESEEGKGTTFTIRLPLKKE
>gnl|CDD|444511 COG5809, KinE, Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
MKSSKMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEK
ELREILKLLKEGESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESE
EKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGG
IAQGEVRFWTKDGRWRLLEASGAPIKKNGEVDGIVIIFRDITERKKLEELLRKSEKLSVVGELAAGIAHE
IRNPLTSLKGFIQLLKDTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYEPKDLNTLIEEVIPL
LQPQALLKNVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPEGGNITIETKAEDDDKVVISVTDE
GCGIPEERLKKLGEPFYTTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQVSMN
>gnl|CDD|444512 COG5810, KbaA, Sporulation protein KbaA, activator of histidine kinase KinB [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
MTSRKWVRFFFTTLLIGGVVTLIVGLIVRWDEYSKYLLSGELGEFLAGLFWFIGVGFTFSVISQMGFFAY
LTIHRFGLGIFRSLSLWNWVQLLLIAFVLFDLVYFRYLPFAQEGGSIVTYILLPLLLLAVGIIVAYIKVK
ETNKKAFIPALFFMVVVTTLEWIPALRVNDTDWLWLMLFPLLACNAYQLLALHKLNAKSEKDRKKREERK
K
>gnl|CDD|444513 COG5811, SigE, Sporulation sigma factor SigE (mother cell-specific, SpoIIGB) [Cell cycle control, cell division, chromosome partitioning, Transcription]
LRLWLIKLLLKLGLKKKEVYYIGGSEALPPPLTREEEAELLEKLEEGDESVRSTLIERNLRLVVYIARKF
ENTGIGIEDLISIGTIGLIKAVNTFNPDKKIKLATYASRCIENEILMYLRRNNKTKSEVSFDEPLNVDWD
GNELLLSDILGTENDIIYKNIEEEVDRELLKKALKKLSERERKIMELRFGLNGGEEKTQKEVADMLGISQ
SYISRLEKRIIKRLKKEINKME
>gnl|CDD|444514 COG5812, SigF, Sporulation sigma factor SigF (forespore-specific, SpoIIAC) [Cell cycle control, cell division, chromosome partitioning, Transcription]
KPLLSDEEVKELIKKAQAGDKEARERLVECNLRLVWSVVQRFLNRGYELEDLFQIGCIGLIKAIDKFDLS
YDVKFSTYAVPMIIGEIKRFLRDDGPIKVSRSLKELANKIRRAKEELSKELGREPTINEIAEELGVSPEE
IVMALEAAQSPTSIYETVYEDDGDPIYLIDQIADEEDEESDWFDKIALKEVLSKLDERERQIIYLRYFKD
KTQSEVAKRLGISQVQVSRLEKKILKKIKEQLEES
>gnl|CDD|444515 COG5813, SigG, Sporulation sigma factor SigG (forespore-specific, SpoIIIG) [Cell cycle control, cell division, chromosome partitioning, Transcription]
MRNKVEICGVNTSKLPVLKNEEMRELFERMKQGDKEAREELIKGNLRLVLSVIQRFNNRGENVDDLFQVG
CIGLIKAIDNFDLSQNVRFSTYAVPMIIGEIRRYLRDNNPIRVSRSLRDTAYKALQAKEQLISENSREPT
IEEIAKELGIPREDVVFALDAIQDPVSLFEPVYHDGGDPIYVMDQISDEKNSDENWLENISLKEAMKRLN
EREKLILTLRFFEGKTQMEVAEEIGISQAQVSRLEKAALKHMRKYVS
>gnl|CDD|444516 COG5814, SigK, Sporulation sigma factor SigK (mother cell-specific, SpoIIIC/SpoIVCB) [Cell cycle control, cell division, chromosome partitioning, Transcription]
MMGFLLALLLSLIKGILLLVSYINNNAFPQPLSEEEEAKYLERMAEGDEEARNILIEHNLRLVAHIVKKF
ENTGEDTEDLISIGTIGLIKAINTFDPDKGTKLATYAARCIENEILMHLRSTKKTRKEVSLQDPIGTDKE
GNEITLIDILGTDEDDVVDQVELKLEKEKLYEKLKKLSEREREVIELRYGLLNGEEKTQREIAKKLGISR
SYVSRIEKRALMKLFKEFYKEGCK
>gnl|CDD|444517 COG5815, SpoIIAA, Stage II sporulation protein SpoIIAA (antagonist of anti-sigma F factor) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
MEVDFEKKGDTLIVRLEGELDHHTAEELREKIDRAIEKGGVKHLILNLEGVSFMDSSGLGVILGRYKKIK
ALGGKVAVINVSPQVKRIFELSGLFKIIKIYDSEEEALEA
>gnl|CDD|444518 COG5816, SpoIIB, Stage II sporulation protein SpoIIB (spatial and temporal regulation of the dissolution of septal peptidoglycan during engulfment) [Cell cycle control, cell division, chromosome partitioning]
MDKPSRKSVKINGKKQNYSEDAQTSVSSREKKDDVEDEMAAEQERAEEVTDLPVLLPLKKKKKGPTRKKN
RSALARKKWPTKLIAAVLSAVLIGTVLGFLLLQVFSQQSDLPVSSDLFEPSSVQAVEVTDADASATGGTS
LIPLNAFVVQAGVFSSKEGAEAVQESFKEKGFPAVIWESDGQYFVFVGIAPDKEIAEQLAEQYQEEGVDV
YVKDWDTTSVSLKLSKEEAQWLTQVQSLLQDSLALSDSLKSGEGIDSDLWQEWVESIPKEAEQLSEETTL
NDFLSQAVEALADDKSDEEQLWSLQQDLLDLWESYQKLAAQL
>gnl|CDD|444519 COG5817, SpoIIE, Stage II sporulation protein SpoIIE/SpoIIH (serine phosphatase - sigma-F activation) [Cell cycle control, cell division, chromosome partitioning]
MMEKTEIYPYKRVKKRKKATLKKLKKKLKLASLLILEGLLLFLLGFLLGRAVILGGLAPFGLAFFAAVLL
LKRDRALLVLLGALLGYLTLGGGSALFKYLAALLLFLLLSKFLKRKKKKKILVLPLLVFLSVLVVGLVYL
AFGGGSPYDLLMALFEAILAFVLTYIFLQALPLLTEKRKRKSLTNEEIICLLILLASVLTGLGGLTIGGL
SLKNILSRLLVLLAAYIGGAGLGAAVGVVIGLILSLSNGSSPYMIGLYAFAGLLAGLFREFGKLGVALGF
LLGNLLLTLYVSGSGELLLSLYEIAIASLLFLLLPKKLLDKLSRYLPGTSEHSEEQQQYLERIRDITAER
LEEFSEVFQELSKTFEEVSEKEKVEDDKDLDSLLERVAEKVCQSCFLRRRCWEREFYQTYQAMNELLEIL
EEKGKISEKDLPREFKKRCVRSKELLEAINREYELYKVNRKWKKRLYESRELVAEQLKGVSEIIEDLAKE
IEKEIKFDEELEEQIREALAKLGIDVEDVDVYSLEKGRLEIEIELPPCRGKGECEKLIAPLLSDILGEPF
VVKKEECGIKPNGHCTLTFVSAKKYRVETGVAQAAKGGELVSGDSYSFFELGDGKYALALSDGMGSGKRA
AEESSATIRLLEKLLEAGFDEELAIKTVNSILSLRSTEEMFATLDLALIDLYTGEAEFIKIGAAPSFIKR
GNEVEVIESSSLPIGILEDIEVDSVERQLKPGDLLIMVSDGILDAPRHVENKEEWLKRFLKEIDTDDPQE
LADLILEEAIRLSGGKIEDDMTVLVAKVEKNTP
>gnl|CDD|444520 COG5818, SpoIIGA, Stage II sporulation protein SpoIIGA (protease, processing of pro-sigma-E to active sigma-E) [Cell cycle control, cell division, chromosome partitioning, Transcription, Posttranslational modification, protein turnover, chaperones]
MVVYLDVVFLLNFVMDYLILWLTARLAKRRTSKWRLLLGALLGALYVLLLFFPPASFLYTILGKLLVSVL
MVLIAFGPKSWRRFLKLLLYFYLVSFALGGGVFALHYFLQSSGLVANGLFLTFSPISWLFLLLGFPLAWL
LGKLGWEILRKRKLREDLLVPVEITLDGKVVEVTGLLDTGNQLRDPLTKKPVIIVEYEALKELLPEELRE
ALQEGDDLADILDALEPSEWASRFRLIPFRSVGKENGLLLGFRPDEVEIVTEGEIIETKKVLIGIYPGRL
SSDGEYQALLHPELLEGAAGA
>gnl|CDD|444521 COG5819, SpoIIP, Stage II sporulation protein SpoIIP, required for dissolution of the septal cell wall [Cell cycle control, cell division, chromosome partitioning]
SLLGSEIPGLAAYDSKILVAGEGTEETNEPIESPPPAEVVLEEIDASELLDEPPKIATTGGKPLVLIYHT
HSTESYLPSLGGAYRSTDGKGNVVKVGDALAEELEKKGIGVVHDKTLHDYPSYNQSYARSRKTVKELLKE
NPSIKVVIDLHRDAVPRREKTTTTINGKKVAKVMFVVGTPNPNWEKNLAFAKQLKAKLEEKYPGLSRGIY
LKKGRYNQDLSPRALLIEVGGVDNTLEEAKRSAELLADVLAEVLKE
>gnl|CDD|444522 COG5820, SpoIIQ, Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell division, chromosome partitioning]
MREENKKQTKKKSKWKRLFRKRWFFPAIYLGAAALILTGVLWYQALNNDDVEPQDAEQSDDTATDNDEPA
VPVNAQVEVLKWPVADAEEVEVVMKFYDVDASEEEQEAALVVYNNTYYPSTGIDIAAKDGESFDVLAALS
GTVTEVEEDPLLGYVVEIKHDNGVSTVYQSLSDVKVKAGDEVKQGQVIGTAGRNLFNKDAGVHLHFEVRK
DGKAVNPESYLPKP
>gnl|CDD|444523 COG5821, SpoIIQ2, Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning]
MKKKKKLKKFLDKKGFYIVLFLCICIVAATAVWVTNNNLNKLEEETVKNKSESNEKSKSKVTASTSNKFL
KPVSGKITREFGEDLVYSKTLNEWRTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHGNGIK
TVYANLDSKIKVKVGQKVKKGQVIGKVGSTALFESSEGPHLHFEVLKNGKPVDPMKYLKK
>gnl|CDD|444524 COG5822, SpoIIR, Stage II sporulation protein SpoIIR, required for processing of pro-sigma-E [Cell cycle control, cell division, chromosome partitioning]
MLKKIIILLLLGLILLLLVLSAEGAAASGTASADEQAYIPDNLIRLHVLANSDSPEDQALKLKVRDAVLA
YLTPWLKDAKSIEEAREIIRENLPEIEEIAEEVLKAEGYDYPVKVELGKFYFPTKTYGNLTLPAGEYEAL
RITIGEGEGANWWCVLFPPLCFVDSSNGTAVEEAEEELKEVLTEEEYKLEEEEEEVEVKFKIVELLKELF
K
>gnl|CDD|444525 COG5823, SpoIIIAB, Stage III sporulation protein SpoIIIAB, component of the engulfment complex [Cell cycle control, cell division, chromosome partitioning]
MMKLIGALLIIGASTLIGFLIARRYKKRPKQLRQLQSALQLLETEISYGATPLPEALERIAEQSEGPVSK
FFAEAAEELEEGRGKTAGEAWEEALEELWKNTALKEEDIEILLQFGKTLGQSDREDQQKHIQLALEQLER
EEEEAEEEQEKNEKMYRYLGVLAGLLIVILLL
>gnl|CDD|444526 COG5824, SpoIIIAC, Stage III sporulation protein SpoIIIAC, component of the engulfment complex [Cell cycle control, cell division, chromosome partitioning]
MMDIDLIFKIAGIGILVAVLHTVLKQAGKEEQAQLVTLAGVVVVLFMVIQLISDLFQEVKSVFQL
>gnl|CDD|444527 COG5825, SpoIIIAD, Stage III sporulation protein SpoIIIAD, component of the engulfment complex [Cell cycle control, cell division, chromosome partitioning]
MEIIQIVGLGLVATVLAVVLKQQKPEIALLLSLAAGIIIFLFILGKIGAVIDLLRDLAEKANIDSVYLST
LLKIIGIAYIAEFGAQICRDAGEGAIASKIELAGKILILVLAIPILTAILETILSLL
>gnl|CDD|444528 COG5826, SpoIIIAE, Stage III sporulation protein SpoIIIAE, component of the engulfment complex [Cell cycle control, cell division, chromosome partitioning]
MKKLRLLIILLLLLLLFALPAAAEAASEESIMDEIIEEQLEELDLSEIEKYWEELDQEYGGYLPELDLKE
LIEDLIKGELSLSIKDILKGLLKYLFKEVLANGKLLGKLLVLAVISAVLQNLQSAFENGTVSKLAYAVVY
LVLIILALNSFRLALNIGKEAIDNMVSFMQALLPLLLTLLASMGGVTSAALFHPLIIFLVNFSGTLIKNV
VLPLIFLSAVLSIVSNISDKFKVSKLAGLLRQISLGLLGIFLTIFLGVLSIQGAAGAVADGVTLRTAKFA
TGNFIPVVGKMFSDAADTVVGASLLLKNAVGIAGLIIILLICAFPAIKILALALIYKLAAALIQPLGDGR
IVDCLNDIGKSLILVFAAVASVGLMFFIAITIIVGAGNLTVMLR
>gnl|CDD|444529 COG5827, SpoIIIAF, Stage III sporulation protein SpoIIIAF, component of the engulfment complex [Cell cycle control, cell division, chromosome partitioning]
MEFLKEWIRNIVIIVLLATFLEMLLPNSSMKKYVKLVMGLLLILAILNPILKLFNKDVDLLLPALSQASS
LEDKNEIEEKGKELKAKQRAYILEQYKKQLKKQIKEELEEKYGVEVADVDVEIDEDESENFGDIKSITVT
LKEAEEGEGEKKVEPVEPVIIDIGESGEEEEKGESELAEEIKNFLSEFYEIDKENIKVSIEGGE
>gnl|CDD|444530 COG5828, SpoIIIAG, Stage III sporulation protein SpoIIIAG, component of the engulfment complex [Cell cycle control, cell division, chromosome partitioning]
MNKWLKKLKEKLGKKKKKKKLKNLIILGLIGVLLLLLGSFFSSPKSTPPNAGSNAETEEASAKSGASSEI
EDYEEELEKKLEEILSQIEGVGKVEVMVTLESGEEKVYAKNTTTSQQTTEEKDKNGGTRTTTETTEEEQV
VLVRQGGGEEPVVVKEIKPEVRGVLVVAEGAEDPQVKAEIVEAVQTLLDVPAHKISVLPKKK
>gnl|CDD|444531 COG5829, SpoIIIAH, Stage III sporulation protein SpoIIIAH, component of the engulfment complex [Cell cycle control, cell division, chromosome partitioning]
MMLKKQTVWLLTLLSLLVVLSVYYISLPSKSEQLPETDSDETNDTAAVGDEESAASEETGAEVATVSNSS
GSDYFAEYRLEREQERSQQKEELKEIIANPNASAEEKEEAQKKLLELTEKSEKEAEIENLIKAKGFEDAV
VRIDDDKVNVVVKADELSKKEAAEIIDIVSRETGVPADNISVKYKPS
>gnl|CDD|444532 COG5830, SpoIIID, Stage III sporulation protein SpoIIID, transcriptional regulator of sigma-E- and sigma-K-dependent genes [Cell cycle control, cell division, chromosome partitioning, Transcription]
MKDYIEERVLEIAKYIIETKATVRQAAKVFGVSKSTVHKDLTERLPKINPELAKEVKKILEYNKAERHIR
GGEATKKKYKKQKK
>gnl|CDD|444533 COG5831, SpoIVA, Stage IV sporulation protein SpoIVA, required for spore cortex formation and coat assembly [Cell cycle control, cell division, chromosome partitioning]
MEKFDIYKDIAERTGGDIYIGVVGPVRTGKSTFIKRFMELLVLPNIENEYDRERARDELPQSGAGRTIMT
TEPKFVPNEAVEITLEDGLKFKVRLVDCVGYMVEGALGYEEEEGPRMVHTPWFDEEIPFEEAAEIGTRKV
ITDHSTIGIVVTTDGSITDIPRENYVEAEERVIEELKEIGKPFVILLNSTHPYSEETLELAEELEEKYDV
PVIPVNCLQMTEEDILKILEEVLYEFPVREVNINLPKWVEELESDHWLKQSFIEAIKEAVKDVRRLRDVD
RAVEALGEYEFVEEVELEEMDLGTGVAEIEVTAKEGLFYQVLSEITGFEIEGEHDLLRLMKELSKAKREY
DKVADALEEVKETGYGVVTPSLEEMTLEEPEIIKQGNRFGVRLKASAPSIHMIRADIETEISPIIGTEKQ
SEELVKYLLEEFEEDPEKIWESNIFGKSLHELVREGIQNKLYRMPENAQVKLQETLQRIVNEGSGGLICI
IL
>gnl|CDD|444534 COG5832, SpoIVB, Stage IV sporulation protein SpoIVB, serine protease, degrades SpoIIQ, SpoIVFA [Cell cycle control, cell division, chromosome partitioning, Posttranslational modification, protein turnover, chaperones]
MKRKKKRKLLGLLLAILLLALSFTPPFRSYLSLPSELRLFEGEELSLNFGLPVSVTINVDNPGVLKINGL
KNSGIKVDLKNPLSLKALKPGQAKLELKLFGLIPLKTVKVDVVPDVKVIPGGQSIGVKLHTEGVLVVGYS
DVETEDGKKYSPAKDAGIQVGDIILKINGQKIKSAEEVAELINKAGKAGKPLKLTVKRGGKIFTVKLKPV
KCKEDGRYRIGLYVRDSTAGVGTLTFYDPKSKVYGALGHVITDIDTGKPIDVGEGEIVKASITSIKKGKK
GQPGEKIGVFIEESNVLGNIEKNTPFGIFGKLNEPPKNPYYNKPIPVALAQQVKEGPAKILTVVDGQKVE
EFDIEIEKVVPQKRPAGKGMVIKVTDPRLLKKTGGIVQGMSGSPIIQNGKLVGAVTHVFVNDPTRGYGVF
IEWMLQEAGILPKKKAEK
>gnl|CDD|444535 COG5833, SpoIVFA, Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning]
MSRRVDEVRKGYPPVVTYSHPLKRSSKFLVKVLISACLFLLVAILFQSDSPPLEKAKAWVATVLTEEFQF
AAVNQWYEETFGGPLAFLPPFGKEEETVEQGEAFALPVSGKVVESFQENGKGVDIETPGGANVKAVKEGY
VIFAGKDEETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQKIGTVPATEGEEGTFYFAIKKGGKFI
DPIQVISFD
>gnl|CDD|444536 COG5834, SpoVAA, Stage V sporulation protein SpoVAA, subunit of dipicolinate uptake complex [Cell cycle control, cell division, chromosome partitioning, Amino acid transport and metabolism]
AMKETVYIRLKKRVTVKPGSVVTLGDIAQIVADDAIKEQLEGIPIYRIQKKDGNRVVIDVLDIIEAIREK
YPNVDVQLIGEPQTIVEIEKRKKKPSLLKVVLVWLLLFIGSALAIMNFHTDVSMQEVHQRIYELITGEKN
EHPLLLQIPYSIGLGLGMILFFNHFFKKKINEEPSPLEVEMFLYQQDIDQYVIENENKKKRRDKDG
>gnl|CDD|444537 COG5835, SpoVAB, Stage V sporulation protein SpoVAB, subunit of dipicolinate uptake complex [Cell cycle control, cell division, chromosome partitioning, Amino acid transport and metabolism]
IRELLLIFIGLAGGIAVGSGFVAFLTVLGIIPRLAQLTKTYKHIILYEWAVILGAVFGTLFSFYDIRLPL
PKILLIVYGLFAGIFVGMLAAALTEVLNVFPILAKRLRLDKGILWLLMAIVLGKVAGSLFYWLYFV
>gnl|CDD|444538 COG5836, SpoVAC, Stage V sporulation protein SpoVAC, subunit of dipicolinate uptake complex [Cell cycle control, cell division, chromosome partitioning, Amino acid transport and metabolism]
MAKKLTKTQKEYQQLVKQVEPKPPVLKNCLKAFLVGGLICTIGQLIQNFYMRFGLSEKDAGNPTSATLIF
LSALLTGLGVYDKIAQFAGAGSIVPITGFANSVVSPAIEFKSEGYVLGVGAKMFKIAGPVIVYGVVSAFV
VGLIYYLLK
>gnl|CDD|444539 COG5837, SpoVAD, Stage V sporulation protein SpoVAD, subunit of dipicolinate uptake complex [Cell cycle control, cell division, chromosome partitioning, Amino acid transport and metabolism]
MMKKVGKQTWVFENPPVIISTASVVGPKEGEGPLGDYFDKIHEDLYFGEKSWEKAERKLLEEAIQLALKK
AGLKKEDIDFLLAGDLLNQIISSNFAARTLGIPFLGLYGACSTMMESLALAAMLVDGGFADYVLAATSSH
NATAERQFRYPTEYGGQRPPTAQWTVTGAGAALLSREGSGPRITHATIGKVVDMGIKDPNNMGAAMAPAA
ADTIVQHFRDTGRTPDDYDLIVTGDLGKVGKEILKELLKEKGYDISENYNDCGLMIYDEDQDVHAGGSGC
GCSAVVTYGYLLKRMKKGELKRVLVVATGALLSPTSFQQGESIPGIAHAVVIEAGG
>gnl|CDD|444540 COG5838, SpoVAEA, Stage V sporulation protein SpoVAEA, mutants lead to the production of immature spores [Cell cycle control, cell division, chromosome partitioning]
MMEKRKVILVTDGDRVARRAVEIAAKNIGGRCISQSAGNPTPLSGEELVELIKQAPHDPVVVMFDDKGDP
GEGAGEQALRYVANHPDIEVLGALAVASNTHGVEGTRVDFSIDRDGELVEGGVDKEGIPEPEGGRINGDT
VDILDQLDVPLIVGIGDIGKMDGADDIEKGAPITTKAIEEILERSGYHGGRTH
>gnl|CDD|444541 COG5839, SpoVAEB, Stage V sporulation protein SpoVAEB, subunit of dipicolinate uptake complex [Cell cycle control, cell division, chromosome partitioning, Amino acid transport and metabolism]
MDYLWAFLVGGLICVIGQLLMDLTKLTPAHILVTFVVAGAILGGLGLYDPLVDFAGAGATVPLTGFGYSL
AKGAIEEVEKHGLLGVFTGGFEATAAGISAAIVFGFLAALIFKPKG
>gnl|CDD|444542 COG5840, SpoVAF, Stage V sporulation protein SpoVAF, subunit of dipicolinate uptake complex, GerA superfamily [Cell cycle control, cell division, chromosome partitioning, Amino acid transport and metabolism]
MEQSKEMKQPISKDLDENLEYLKEELGVGESFDVGVREFEIGGRKAALYYVNGFVDDEVLTEILKELLRL
EREDLSVDALKKLLENHLPHVQVEEVDTLDEVVDQVLSGPVALFVDGEDEAIIIDVRSYPGRSPEEPDLE
KVVRGSRDGFTETLVFNTALIRRRLRDPRLRFEILQVGKRSKTDVCIAYIEDIANPELVDEIKERIQQIK
IDGLPMAEKSLEEFITKGKWNPYPLVRYTERPDVAAAHLLEGHVLIIVDTSPSVIILPTTFFHHLQHAEE
YRQNPLVGTYLRWVRFIGVLASLFLLPLWLLLALNPELLPESLSFIGPKKEGNIPLFLQFILAEIGIDLL
RMAAIHTPTPLATALGLIAAILIGDIAIKVGLFSPEVILYMAVAAIGTFATPSYELSLANRLVRLFLLIL
VALFGLPGFVIGITLIFLLLARTKSFGVPYLWPLIPFNPKALKDVLVRTPVPLKNLRPSILKPKDRDR
>gnl|CDD|444543 COG5841, SpoVB, Stage V sporulation protein SpoVB/SpoIIIF, required for spore cortex synthesis [Cell cycle control, cell division, chromosome partitioning]
MKKQSFLKGALILTAAGLISKILGAIYRIPLQNIIGDEGFGLYQMAYPIYGLFLTLATAGIPVAISKLVA
EYNALGDYKGARRIFRVSLLLLLILGLVFFLLLFFGAPFIARLLLGDPRAYYSLRALAPALLIVPVMSVL
RGYFQGLQNMTPTAVSQVIEQIVRVIFILLLAYLLLPYGLEYAAAGATFGAVIGALAGLLVLLYYYRKRK
KKLKRLLEKSKTKSKESSKDILKELLRIAIPITLSSLVLPLFQLIDSFTVPRRLQAAGLSASEATSLYGI
LSGMAQPLVNLPTVLATALATSLVPAISEAFAKKDRKLVRRRINQALRLTLLIGLPAAVGLAVLAEPINT
LLFGNPEGGGILAILAPSAIFLSLQQVTTGILQGLGKQKIPVINLLIGLLVKIILNYLLVPLFGIYGAAL
ATVIGYLVAAILNLAALKKYTGFKLDLRRRLLKPLLASLIMGIVVLLLYRLLSLFLPESRLGALLATLIA
VLVGAIVYLLLLLKLGLITKEELRRLPKGGKKLARLLRKLKL
>gnl|CDD|444544 COG5842, DpaA, Dipicolinate synthase subunit A (sporulation protein SpoVFA) [Cell cycle control, cell division, chromosome partitioning, Amino acid transport and metabolism]
LTGKKIAVIGGDARQLELIRELAELGATVKLYGFDQDEGFTGVEKADSLEEALKDADVIILPVPGTDDEG
RVEAPFSNEKIVLTEELLAKLPPGCLVFAGIANPYLKELAERKGIKLVELMERDDVAILNSIPTAEGAIQ
MAIEETPITIHGSNVLVLGFGRCGKTLARKLKALGAKVTVGARKPADLARAYEMGYEPVHLSELAEYLGE
ADIIFNTIPALVLDAEVLAKLPPDALIIDLASKPGGTDFEAAKKLGIKAILAPGLPGKVAPKTAGRILAD
VIPRLLLE
>gnl|CDD|444545 COG5843, DpaB, Dipicolinate synthase subunit B (sporulation protein SpoVFB) [Cell cycle control, cell division, chromosome partitioning, Amino acid transport and metabolism]
RLKGKRIGFALTGSHCTFDEVFPQIERLVEEGAEVVPIVSYTVQTTDTRFGKAEDWKKKIEEITGKKPID
TIVEAEPIGPKKLLDCMVIAPCTGNTLAKLANGITDTPVLMAAKAHLRNGRPVVLAISTNDGLGLNAKNI
GRLLNTKNIYFVPFGQDDPVKKPNSLVADMDLIPDTIEAALEGKQIQPVLIEYFR
>gnl|CDD|444546 COG5844, SpoVM, Stage V sporulation protein SpoVM, required for spore cortex and coat synthesis [Cell cycle control, cell division, chromosome partitioning]
MRFYTIKLPRFLGGIVRAILGAFKKD
>gnl|CDD|444547 COG5845, SpoVT, Stage V sporulation protein SpoVT, regulator of stationary/sporulation gene expression [Cell cycle control, cell division, chromosome partitioning, Transcription]
MKATGIVRRIDDLGRVVIPKEIRRTLRIREGDPLEIFVDRDGEVILKKYSPIGELGDFAKEYAESLAEST
GHIVLITDRDEIIAVAGASKKEYLNKPISSELEKIMEERKTVLENDGGELELVEDDEEKFTSQVIAPIIA
EGDPIGAVILLSKEEGAKMGELEVKLAETAAGFLAKQMEQ
>gnl|CDD|444548 COG5846, SpoVID, Stage VI sporulation protein SpoVID (LysM domain), required for assembly of the spore coat [Cell cycle control, cell division, chromosome partitioning]
MSNEQSVLRFSLEESIWFKKGQEVEELLSISLEPDISIEENDDYVSIRGALELTGEYVPEQEEAEGEAED
LQDFASFRFVEEVEPREDGTNEFSHRFPVDITIPKDRISNLEDVYVTIESFDYELPESRQLKLTADLSIY
GIQQEPPRQQEEDEPAEEEEEEEEIAAEFEVEAKQESYEEEESPSEKEEPEQPAEDEPTLQLEEVDEEEA
QEDEPELESKSESDKVEEEPALVEEQSEQQTEEEPKSQQYAEFFPEEELEEAAQYEVFGEREPEVEEEPE
SESVEAEAEESSVEESSEIEEVQAVIEEQEEESEAEEEEEKERRDENALYLTKLFTKNEEEEFTKLKMCI
VQEGDTLETIAERYDISVQQLIRVNQLESDEVSEGQILYIPVSRKKHK
>gnl|CDD|444549 COG5847, SpoVIF, Stage VI sporulation protein SpoVIF, required for heat resistance [Cell cycle control, cell division, chromosome partitioning]
MSNMQKNFFDKIEKKTGVNMDDIFKLANSVQNADFSDEKTVRQLVRQVSKLANKPVSKEKEDKIVKAIVN
NGIPLDMSTLSKMLK
>gnl|CDD|444550 COG5848, BofA, SigmaK-processing regulatory protein BofA (Bypass-of-forespore protein A) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
MEELNVILAILVGLLLLLLVGGALLKPLKWLGKLILNLLIGALLLFLVNLFGGFFGFHIPINPVTALIAG
FLGLPGVALLVVLKLFLL
>gnl|CDD|444551 COG5849, BofC, SigmaK checkpoint regulator BofC (Bypass-of-forespore protein C) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
MKRKKKLLIFILLAVLLLASLVFLGSLEESEEDVTAAETLLTAEHNEPVSVEVVLERQYLDGEVSEETKT
ESITSMEDLWAKYKGWQLVSQEKGRIVFRKQVDDISPLLKENGYFGISEDGTLSIFEGLPKEQEVIQSFF
QIDIKKLESHLPEQLKKGIRIESKDEYESVIETYRSYADEKQK
>gnl|CDD|444552 COG5850, RsfA, Prespore-specific transcriptional regulator RsfA [Cell cycle control, cell division, chromosome partitioning, Transcription]
MTKVRQDAWTEEDDLLLAETVLRHIREGSTQLAAFEEVGDKLNRTAAACGFRWNAVVRKQYEEAIQLAKK
QRKERKRALGKAQSRRKDSLYQPPSVALAKSSLTLDDVIAFLQQLKKLQVQSAQLEKENERLREELEELQ
EENEQLEKELEKLEKELETVQEDYETLVQIMDRARKLVLLEEEEEEIAPRFKMDRNGNLEKVAK
>gnl|CDD|444553 COG5851, Sda, Stage 0 sporulation inhibitor Sda, checkpoint for initiation of sporulation and replication [Cell cycle control, cell division, chromosome partitioning, Replication, recombination, and repair]
MKKLSDELLIESYHKAKELKLSPDFIELLEEEIQRRSLSHKLSASS
>gnl|CDD|444554 COG5852, SspA/SspB/SspC/SspD, Small acid-soluble spore protein SspA/SspB/SspC/SspD (alpha/beta-type) [Cell cycle control, cell division, chromosome partitioning]
MANNRNSNKLLVPEARQALDQFKYEIAQELGVQLGQDGYWGDLTSRQNGSVGGEMVKRMVQMAEQQLAGG
>gnl|CDD|444555 COG5853, SspE, Small acid-soluble spore protein SspE (gamma-type) [Cell cycle control, cell division, chromosome partitioning]
MAKYAKEFASETNVQQVRQQNQQSAQASGAGQFGTEFASETDVQQVRQQNQQSEAKKQQNSGSQQNNQQ
>gnl|CDD|444556 COG5854, SspF, Small acid-soluble spore protein SspF (alpha/beta-type) [Cell cycle control, cell division, chromosome partitioning]
MARRRGIMSDQLKYELAKELGFYDTVQREGWGGVTSRDCGNMVKRAIERAEQALAQRNNP
>gnl|CDD|444557 COG5855, SspH, Small acid-soluble spore protein SspH/YfjU [Cell cycle control, cell division, chromosome partitioning]
MDVQRAKEIVESPEMINVTYNGVPVWIEHVDEENETARVHPLDNPEEEQEVPVSELEEE
>gnl|CDD|444558 COG5856, SspI, Small acid-soluble spore protein SspI [Cell cycle control, cell division, chromosome partitioning]
LDIRQAILANVHGNSKEELEDTIVDAIQSGEEKLLPGLGVLFEVIWKNSSEQEKQEMLDTLEQGLK
>gnl|CDD|444559 COG5857, SspK, Small acid-soluble spore protein SspK [Cell cycle control, cell division, chromosome partitioning]
MRNKEKGFPNNNKFDGEPRAKAEFASKRADGTINTHPQERMRASNQR
>gnl|CDD|444560 COG5858, SspL, Small acid-soluble spore protein SspL [Cell cycle control, cell division, chromosome partitioning]
MSKKKSKDKGKKASGVNPQGLGEDAADQEPKSQLEQRAKKKNTK
>gnl|CDD|444561 COG5859, SspN, Small acid-soluble spore protein SspN [Cell cycle control, cell division, chromosome partitioning]
MSNPKDNSSQFAPNHLGTQPRKAGGNKGKQMQDKSNEHPQVIQTKGE
>gnl|CDD|444562 COG5860, SspO, Small acid-soluble spore protein SspO/CotK [Cell cycle control, cell division, chromosome partitioning]
MVKRKANHSIPGMNAAKAQGKGAGYNEELPNEPLTEAQRQNNKKRKKNQ
>gnl|CDD|444563 COG5861, SspP, Small acid-soluble spore protein SspP/CotL [Cell cycle control, cell division, chromosome partitioning]
MGKRNKGPKQQKNPKLPKGPNQGQPEPLSGSKKVKNRNHSRQKHNEGH
>gnl|CDD|444564 COG5862, CsgA, Small acid-soluble spore protein CsgA [Cell cycle control, cell division, chromosome partitioning]
MDQTLAYLRESLSNYLENEVCQRIYKKLISKPYANEEEFVKDLDEEEMAFLNRVLEHEIKYAKNEQDDKR
VYELNEVYELLI
>gnl|CDD|444565 COG5863, Tlp, Small acid-soluble spore protein Tlp (thioredoxin-like protein) [Cell cycle control, cell division, chromosome partitioning]
MPKPDDRSDNVEKLQEMIQNTIENIEEAEEYLEEEASEEEKENIEEKNERRRESIEGMREEIKDEAAAK
>gnl|CDD|444566 COG5864, SASP, Small acid-soluble spore protein SAS2, clostridial type [Cell cycle control, cell division, chromosome partitioning]
MSKKKKKKPETPLEKLKYEIAEELGLLDKVEKEGWGSLTARETGRIGGLMTKRKKRLAEKELAERGK
>gnl|CDD|444567 COG5865, CsfB, Forespore-specific anti-sigma-G factor CsfB/Gin [Cell cycle control, cell division, chromosome partitioning, Transcription]
MEEVQKKEKCIICEQEKEEGIHILGKFICESCEKEIVKTDTDDPKYPFYVKKLKKIWLSKLYS
>gnl|CDD|444568 COG5866, YabG, Sporulation-specific protease YabG [Cell cycle control, cell division, chromosome partitioning, Posttranslational modification, protein turnover, chaperones]
MDIKIGDIVARKSYGKDILFRIVDIKEDNGRKIAILKGLDVRLIADAPLDDLEKVDERELKEYKKKEKEK
ENESLRLIRQDRELEREKREYRATSGYKDKAEYFEMPGRVLHLDGDPEYLKKCLDLYKQLGIPAVGIHVP
EKEQPEKVLELLEKHRPDILVLTGHDAYLKNKGDFSDLNNYRNSKYFVEAVKEARRYEPSLDDLVIFAGA
CQSHYEALIRAGANFASSPSRVLIHALDPVFVAEKIAYTSIMETVSIWDVIRNTITGEKGIGGIETRGKL
RLGLPKSPY
>gnl|CDD|444569 COG5867, YabK, Anti-sigma-F factor Fin [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]
MAIHYRCRHCGTKIGELDQDQVDEERLGFHQLTPEERQDMITYDENGDITVKTICEDCEEALERNPEYHE
LENFIQ
>gnl|CDD|444570 COG5868, YabP, Sporulation protein YabP [Cell cycle control, cell division, chromosome partitioning]
MEEKEKSKRHNLTLENRKRLTITGVKDVESFDEEEILLETELGLLTIKGENLHIKKLNLEKGEVSIEGEI
DSLEYSDEKSQGEKGKGLLSRLFK
>gnl|CDD|444571 COG5869, YabQ, Spore cortex formation membrane protein YabQ [Cell cycle control, cell division, chromosome partitioning]
MTLTTQFYTFLAMVLGGILLGALFDTYRVFRGRFKLKRWLTFIEDLLFWLIQTLLVFYVLLLVNWGELRF
YVFLGLLLGFALYFLLLSKLVIRLLERIIRLVRRLYRKVLRLLYKLIIYPFRFLFRLLKKPLRFIKRILL
KILRFLLRILFKPIRWILPKRIRKFLGAGFKKKLKKKLKKWLKKKRK
>gnl|CDD|444572 COG5870, YbaK, Uncharacterized sporulation protein YbaK, contains DUF2521 domain (not related to E. coli deacylase YbaK, COG2606) [Cell cycle control, cell division, chromosome partitioning, Transcription]
MGVITSFTEKKREKQLTYERKMLRELSLRKIKQSIQEHFQPLFPFYRLHHDAIEEGCIDFAIEAYLLGAR
YSRFGYYGESAEDVKKRCAQEEKQLIDELFDFLLFWGNINDQFDLESLYDACEAFIDHWWKEGFEKGEKR
YRLKLH
>gnl|CDD|444573 COG5871, YqfC, Spore cortex protein YqfC, YabP family [Cell cycle control, cell division, chromosome partitioning]
MKKRKKKLKKWLAELLDLPKDVVLDLPRITMIGNLQLYIENHRGIVEYSPEEVRINTTEGELIITGKDLV
IKTILPEEILIEGRITSIEFLEG
>gnl|CDD|444574 COG5872, YqfD, Stage IV sporulation protein YqfD [Cell cycle control, cell division, chromosome partitioning]
MLLRLWNYLRGYVIIKVEGESPERFLNLCARRGIYLWDIKRKNEGTLEAKISLSDFRKLRPLARKTGCRV
RIVEKKGLPFLLRRLKRRKGLLAGALLFILLLYLLSSFIWFIEIEGNEKVSEEQILKALAEAGLKPGALK
FSLDPEEIERKLLLDLPELSWVGVEIKGTRAIIEVVEKVLPPEEEEDGPCHIVAKKDGVITEIIVLKGQP
LVKEGDTVKKGQVLISGIIGPEEEEEEDEPRLVHAKGIVKARVWYESYVEVPLEETVKVYTGESKTRYYL
KLGGKEIPLWGFGKIPFAQYEKETEVKTLPLWRNWKLPVELIKETYREVETVKEKLTEEEAKELAKEKAR
EELLKKLPKDAKILSEKVLHLTVENGKVRVKVLVEVEEDIGVEQPIEIE
>gnl|CDD|444575 COG5873, YqzE, Uncharacterized sporulation protein YqzE [Cell cycle control, cell division, chromosome partitioning]
MSGNDYVKFVTEQFVKYMDTPKEERKKRRKERKQERPPLSYRWFGVLPVALRLWFKKR
>gnl|CDD|444576 COG5874, YtxC, Uncharacterized sporulation protein YtxC [Cell cycle control, cell division, chromosome partitioning]
MMQLLSIGTSDYIDELRERLKEELKNLEEEGIKISLEEEQEGGYTFLECNIEEEERDEETKNIFRHYIAN
ALADIIIDHWEKKLIKKIIRKNYYYFSSEEKEEILEKALKILNGEEEGEADSFKISRKNKILRKILDYLD
ENNEINIDGFIRFRLKDYLEELEEAVDKAVDEYLMEKEYNEFIKLLRYFVDIQEPKVELVHVVVTKDGSF
RLYDENGNPITNEYLEEFLLELLDGEINYEDLLISALITIAPRKIVLHGVDEAPNKEILETIKNVFEGRV
EICNGCELCREDTSKKKK
>gnl|CDD|444577 COG5875, YunB, Uncharacterized sporulation protein YunB [Cell cycle control, cell division, chromosome partitioning]
MMRRRRRRRRRRPLPRRRVFLLLLVIFILLLILSFWLINRRLRPTLLAIAETKAKQIATEAINKAVNEKI
AEDIDYEDLIEVHKDNEGRVTLIQANTVEINRLASETTLRVQEALKELEEIVIEIPLGQATGSSLLANLG
PKIPVRFEPIGSVNVDIETEFEEAGINQTRHEIYLHVEVNVRIIVPFASKTTTVTTEVPIAETVIVGDVP
QFYVNGGGGKSPSIPVP
>gnl|CDD|444578 COG5876, COG5876, Uncharacterized sporulation protein YozQ [Function unknown]
MNMAKQEQSNNVAGKQYEPSDYKSNDQLDKGLATTHEQVSDTYTEGTIDGKID
>gnl|CDD|444579 COG5877, YjcM1, Stand-alone amidase domain [Cell cycle control, cell division, chromosome partitioning]
MNPPKRLHPYNREAAVAYAHTWALSRNPAYPDFDDLGGDCTNFISQCLYAGGGPMNFTPVRGWYYRKGDD
NNRSPSWTVAHSLYWYLTNNKGPGPFAKEVTTASELEPGDIIQYDFDGDGVFDHSPIVVGFGNDPGLGDP
LVAAHTYDADNRPLSYYDYTKYRFLHIIGYRR
>gnl|CDD|444580 COG5878, YyaC, Uncharacterized sporulation protein YyaC,contains DUF1256 domain [Cell cycle control, cell division, chromosome partitioning]
MNLFQKKEKLRIHYDDPNAVEKLSEALLSLLPKLSSNREIVILCIGTDRSTGDSLGPLVGTLLKEKNIPP
LHVYGTLEEPVHALNLKETLEKIKKKHPNPFIIAIDACLGRLENVGYITIGNGPLKPGAGVNKDLPPVGD
ISITGIVNVGGFMEYFVLQNTRLSLVMKMADIIARGLVLALHRLSKKKKPESNLF
>gnl|CDD|444581 COG5879, CotD, Spore coat protein CotD [Cell cycle control, cell division, chromosome partitioning]
PMHCPPHVTPPIVHPTKCNVQHNFSETVVPHIHPSHTTTVNHHVYKHQHYFPHTTSVVNEVSHQHTYCGG
PGPHPGPGGPGVMPRPG
>gnl|CDD|444582 COG5880, CotE, Spore coat protein CotE [Cell cycle control, cell division, chromosome partitioning]
MSFDREYREIITKAVCGKGRKFTQTTHTITPPHKPSSILGCWVINHKYEAKKKGDAVEVEGSYDINVWYS
YNDNTKTEVVTETVSYTDLIPLSYRDENCLHDDVEVIARVIQQPNCLEATISPGGNKIVVEVEREFLVEV
IGETKVCVSVHPLGFEDEDDEDWEFEDEDDEFEDLDP
>gnl|CDD|444583 COG5881, CotI, Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, chromosome partitioning]
MEELIEEILENYDLKIESIKPVRGVYKIETDQGPKCLKKIKYSPERLLFIYEAQEHLKKNGFNNIPRIVP
TKDGKPYVKYGGKLYYLTEWIEGRECDYKNPEDLKKAAETLAEFHKASKGFEPPPGSKGRSHLGKWPERF
EKRLEELEKFKKIAEKKKNKNEFDRLFLKNIDYFLEQAEKALELLEKSAYYKLVKEAKKEGGFCHHDYAY
HNILIDEDGKIYIIDFDYCIYDLPVHDLAKLLRRVMKRGNWDIEKAKEILEAYNKINPLSKEEIEVLLAF
LLFPQKFWRLVNKYYYEKKNWSEEKFIKKLQKLIEEEEEKEEFLEEFEKIL
>gnl|CDD|444584 COG5882, CotJA, Spore coat protein CotJA, required for the assembly of CotJC [Cell cycle control, cell division, chromosome partitioning]
MFTQRKSYRPYVSPFDPCPPIRVKTYVTPPNLYMGFQPPNLPQFSPREALRKGTLWPALYDPYENPYEGG
RRG
>gnl|CDD|444585 COG5883, CotJB, Spore coat protein CotJB [Cell cycle control, cell division, chromosome partitioning]
MDKERYELLKEIQALDFALVELNLYLDTHPNDQEALEDFNQYAQKLKKLKKEYEEKYGPLTNFGASPSDY
PWQWIEEPWPWEIEY
>gnl|CDD|444586 COG5884, CotN, Spore coat protein CotN/TasA [Cell cycle control, cell division, chromosome partitioning]
MGIKKKLGMGVATAALGLSLIGGGTYAYFSDSETTNNTFAAGTLDLSVDPTAIINVDNLKPGDTMTREFE
LQNNGSLDIKKVLLETDYSVTDAKGDNTGEDFGEHIKVQFLYNVDKKNEVVYETTLAELKNMTPDAVAKD
IFIPLLEEKGLPAGTTDKLKVKFEFVDNGEDQNQFQGDSLNLTWTFEATQTAGEAK
>gnl|CDD|444587 COG5885, CotO, Spore coat protein CotO/YjbX [Cell cycle control, cell division, chromosome partitioning]
MSMKKKKAAKKPLLYIVQPDFKKAEASMQTIYITPKKNNDPKAEEPARNENVQTSAVEEVIRQEKQNKAA
EAVSQPQKDEATEEEEDKAEEQEPQSRPRKKPFKEMTIEEKIDFLLNLPHHIPKMKCEIKTEGRTYRGII
VDYENDIVQIRTFKRPAPTELPIEDITSIRLLGF
>gnl|CDD|444588 COG5886, CotV, Spore coat protein CotV/CotX (outer spore coat) [Cell cycle control, cell division, chromosome partitioning]
MEGRYDRPKKWSALDPCSDHSDDDNADVDQEADQVSLNEQISDELIIIKDSCDVEVTTTDTQAAVSLQAA
LQAAIAVVISISIADSDRAELVAQELLQKVATKQVNRQKTVIENSRNVTVTTTDTDIAVNIQLLLQILVA
LVAKLDIL
>gnl|CDD|444589 COG5887, CotW, Spore coat protein CotW (outer spore coat) [Cell cycle control, cell division, chromosome partitioning]
MSDNDKKEFKADLPDPMLELLVDDIFKKHGVTEDKVKNLSDEEKQMIRNLVKDLQSQVDTFLDNQKKRIN
KANANDQNNEK
>gnl|CDD|444590 COG5888, CotY, Spore coat protein CotY/CotZ (outer spore coat) [Cell cycle control, cell division, chromosome partitioning]
MGCGKNHTHSGNCVCDILRAILDAQDAVVDDEDCCPTSCILDLLGGPARSGADTRPFILYCKDGKPFKGF
GVTPSDTFKCFESPFFRVEDVDDDCCATLELLRPVDDEGNSDFNSPCDPVDDVTDLEATGICITVDLNCF
CAIQCLPDVLLLL
>gnl|CDD|444591 COG5889, GerQ, Spore coat protein GerQ/YwdL (inner spore coat) [Cell cycle control, cell division, chromosome partitioning]
MSENENQRQQPQQNPYYYYPQYQPAYYPSMQGQQPQQPMQQQQQGPQPGFGQQIPQMPTGQQPTGPSVPG
MLPLEQSYIENILRLNRGKVATVYMTFENNSQWNAKIFRGVIEAAGRDHIILSDPQTGKRYLLLMVYLDY
VTFDEEINYEYPYALATYSPR
>gnl|CDD|444592 COG5890, YhbB, Uncharacterized sporulation proteins YjcM and YhbB, contain C-terminal amidase domain [Cell cycle control, cell division, chromosome partitioning]
DNLKGKEQVVELKKSKAELVKRRIKAIVEETKKNYLIEEEVKELEKLVYELKFTSILNKSRVKSDEEEED
LRRDELDGDKTAEDATLDALEEPKREQPPLEEEDDKDLSTSGEYDRLKAVRYAEKYWNKYNPAYKNFNVG
DCTNFVSQCLYAGGAPMRGYPNRDSGWWYNGGSWSYSWVVAHAFRNYLSYSGRGLYAEEVSSAYELLPGD
VICYDFKGDGRIDHTTIVTGKDSKGYPLVNAHTTDRYNVPWRRLRYWDYDDSTAYTPHY
>gnl|CDD|444593 COG5891, YheC, Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, chromosome partitioning]
MSKIVKVTLRFGSRRLGLPAGIPYRLRYDGRTLRLGPLIGILTSRFSPGKPFGGETSYFRELAKAARKLG
GLVYVFTPEDIDWDEGTVRGYVYNPTGGKWKRGTFPLPDVIYNRIPSRKAERSEKVKELREKLKKRPGIP
FFNPRFFNKWEVYQLLSKDPRLRPYLPETELLTSPEDLLEFLKRYKSVYLKPVNGSLGRGIIRIEKKGDG
YLLRYRRKKRNVRRRFSSLDELLAFLRRLLRRKRYIIQQGIPLATIDGRPFDFRVLVQKNGRGEWVVTGI
VARIAGPGSITTNLSGGGTALPLEELLRRAFGDSKAEEILQKLERIALEIARALEESYGGLGELGIDLGI
DRDGKIWLLEVNSKPGRSIFDEPGDKELRRRSLRRPLEYAKYLAGFKKAK
>gnl|CDD|444594 COG5892, YlbD, Spore coat protein YlbD, FlgN family [Cell cycle control, cell division, chromosome partitioning]
MSKSNLHPSVEEFKQFVQKHPKLIKEVRKGKKTWQEVYEDWVLLGEEDPIWEQYREEAEASESKKEKEKK
KEWVGQLLKMLDKIDVDKVQEHLAQLSSAITTIQSLIGQFQGSKQQQNQPNSNQHPFSFRKD
>gnl|CDD|444595 COG5893, YmaG, Spore coat protein YmaG [Cell cycle control, cell division, chromosome partitioning]
MNPTRLYYGFGRPGFGGYFGRRPFFGFFGAPFFGGFLGGLLGSALFGYPRPYPYPYPPYPYYPYGGYPYY
Y
>gnl|CDD|444596 COG5894, YppG, Spore coat protein YppG [Cell cycle control, cell division, chromosome partitioning]
MHWYQRNMNMYHYARPALRPEQPYGPYQNQHQQPYYQQTNTQQPFPPPSPTPYPSPKPLQTQPSQFQSLL
SQFKKADGQYDFNKMMNTVGQMANTMNQVSGILKGFGGFFKK
>gnl|CDD|444597 COG5895, YpzA, Uncharacterized sporulation protein YpzA, contains DUF2564 domain [Cell cycle control, cell division, chromosome partitioning]
AHSGFNDLKQVEMAVETAQKMVGQATRSLDSTTLDHATQAVEDAREQLSRAKSLATGLDEPFLLQQEQLL
ADAEHQLDEARH
>gnl|CDD|444598 COG5896, YraG, Spore coat protein YraE/YraG [Cell cycle control, cell division, chromosome partitioning]
QNLGAHETLELHELLNFKTLCLTKSKTMQGLVSDQELKDLMQQDVQQTTQQLQELQDLLSKASLQ
>gnl|CDD|444599 COG5897, YsxE, Spore coat protein YsxE, aminoglycoside phosphotransferase family [Cell cycle control, cell division, chromosome partitioning]
MDRMEWIEPILRQYGLYPESVEKVGNRVWKVYTNRGTFALKRSRLSRERLSFWQSVYQLLHEFGISGVVP
VYLTKQGELYVTDGGTSYYLMPWLEGEEADERNEKYEPLFQTLARLHQKTKQEITISEEEAEPSYQELKR
RWEQRKEKLEEFAEHAEQRWYMSPFELQVCTHFHELMHAAQFADERLERWYEDEKEKKKWRIVLCHGRLS
PSHVLFDESGQGYLINFERAGFDTPVRDLALFFRRAFRTAPTNEEELVEWFSAYEKELPLSEEERSLLAS
YLLYPERYIKVLDRYQEKPNEKSELEYVRRLERAYRQLKNMEQFVMKLQEKKEEK
>gnl|CDD|444600 COG5898, YuzC, Spore coat protein YuzC (inner spore coat) [Cell cycle control, cell division, chromosome partitioning]
MYYPYYYYYPNWQMPTFTTRPYPPIDPNLFKQSAKAMQTLMKEAGTVLDKLANSPEFAAELMSAAQQSNQ
DEVQRLIRSIGITSKIDISYNPDGLRLTLSPQVGDLPCCHLTIALRW
>gnl|CDD|444601 COG5899, YwqH, Spore coat protein YwqH [Cell cycle control, cell division, chromosome partitioning]
MGYISTLNLILSSLSSKLAEKEEQIERLKRAKKELEQEQKEFSDEIRSILKPELNSTWTGSLADDFDKIR
EEAKTAYYKIVNDQYSEYIQSIEEKIFSLENEIESLQNEASSLLHKGEKAADELGDKIRKLKGR
>gnl|CDD|444602 COG5900, YybI, Spore coat protein YybI (inner spore coat) [Cell cycle control, cell division, chromosome partitioning]
MYNPYQLNLQKNTYILDSKKGDVNGDGILDRVYLTGNKEDPDSPFVENITLVVQDGKTGRVTAITLKNNG
GYNPTLFLGDFTGDGVKDILVSIDSGGSGGIYYYYIYSFKNNKPREIFDFEDFNEGYKYTVNYLDNYKVE
VISKNLNQTYILDLSYKGDEYLNEIYDKNGKLKKPIEGWVDPLSGLYPVDFDGDGVYELLAYQRIIGRYN
ADTLGYVESTLKWDGGKFKLKSQEVSIFGDEK
>gnl|CDD|444603 COG5901, GerAA, Spore germination receptor GerABC, GerA subunit (L-alanine receptor) [Cell cycle control, cell division, chromosome partitioning]
KPISKSLEENLEYLKELLGNSSDLVFREFKLAGNIKAALVYIDGLVDKDILNENILKPLMELEETLDDDL
LEKLKERILPVSEVKEVDDLEEAVDALLSGDTVLLIDGSDEALIIDTKGWEKRSVEEPETESVVRGPREG
FTETLRTNTALIRRRIKDPNLKVESLTIGRRSKTDVAILYIEGIANPELVEEVKRRLKSIDIDGILDSGY
IEELIEDNPFSPFPQVLYTERPDRVAAALLEGRVAILVDGSPFALIVPATFFEFFQSPEDYYERWIIASF
LRLLRFIAFFISLLLPALYIALTTFHQEMIPTDLLLSIAASREGVPFPAFVEALLMELTFELLREAGIRL
PRPIGQTIGIVGALVIGQAAVEAGLVSPIMVIVVALTAIASFTIPSYSLSIAIRLLRFPLIILAAFFGLF
GIILGLLLLLIHLCSLRSFGVPYLSPFAPFRLKDLKDTLIRAPLWKMKKRPKFLRPKDPTRQG
>gnl|CDD|444604 COG5902, GerAB, Spore germination receptor GerABC, GerB subunit (amino acid transporter) [Cell cycle control, cell division, chromosome partitioning]
MEKGKISARQLFFLIILTIIGVGILTLPRLLAKIAGQDAWISVLLAGLIGLLLALIIVKLLKRFPGKTLV
EISEKILGKWLGKLLGLLYILYFLLIAALVLREFGEFIKTTLLPETPIWVIILLFLLVAVYAVRGGIEVI
ARVAEILFPLILILLLLLLLLSLPEIDFSNLLPVLENGLKPILKGALPTSFPFGGFEILLMLYPYVKKKK
KAKKAALIGILISGLLLTLVVLVSIGVFGPEETSRLTFPTLELARLIEIGDFLERLESIFIIIWIIGIFI
KISLFLYAAVLGLAQLFGLKDYRPLVLPLGLLIYILSLIPFPNIAELLDFLDKVLPYYGLIFQIIIPLLL
LIIAKIRKKKKKKKK
>gnl|CDD|444605 COG5903, GerAC, Spore germination receptor GerABC, GerC subunit [Cell cycle control, cell division, chromosome partitioning]
MKKLLLLLLLLLLLLLLTGCWDRRELEELAIVLAIGIDKGEEGKYKVTVQIANPSALAGGGGGGEEPVWV
ISATGKTIFEAIRNLNTKSSRRLFFGHLKVIVIGEELAKEGIGEVLDFLLRDPEIRRTVYVAVTKGKAED
ILKVKPPLEKIPAEYLEDLLENSEKTSKIPPVTLHDFLQDLLSPGIDPVLPYIEIVENKEKKELKISGAA
VFKGDKLVGWLDEEETRGLLWLRGKVKGGVITVPCPKDEGGKISLEIIRSKTKIKPKIKGGKPKFTIKIK
LEGNIAEYTSDIDLSDPETIKKLEKALEKEIKKEIEKAIKKLQEYKSDIFGFGEALRRKYPKEWKKIKKD
WDEIFPDAEVEVKVVKKIT
>gnl|CDD|444606 COG5904, GerD, Spore germination receptor GerD [Cell cycle control, cell division, chromosome partitioning]
MRKLLRLLLLIFLLLLLAGCSGSSGGSQQPDYDETKKMVVDILKTEEGKKAIREVLADEEFKQLLILDQD
EVKKAIEDTLTSEKGKEFWEKTFKDPKFAETFAKSMKKEQKDLLKDLMKDPEYQKMMLELLKNPEMEKQL
LDLMKSQEYRKQLEKVMQETLESPLFQAKIQELLLKAAEEELKKGGGGGSGGGEGGSGGGESGGGGGDSG
>gnl|CDD|444607 COG5905, GerE, Spore transcriptional regulator GerE (stand-alone HTH domain) [Cell cycle control, cell division, chromosome partitioning, Transcription]
MMPSSSTSHPSLLTKREREVLELLAEGLTNKEIARQLFISEKTVKNHVSNILRKLGVRNRVQAVVWALRL
GLLSLD
>gnl|CDD|444608 COG5906, GerPA, Spore germination protein GerPA/GerPF (inner spore coat) [Cell cycle control, cell division, chromosome partitioning]
MPAIVGPIKINSVSSSGVVNFGDVLNISPKSVAKTFAGSGSFNTGDFLNTNNGISATNTFDPDVADQNVV
GNA
>gnl|CDD|444609 COG5907, GerPB, Spore germination protein GerPB, DUF2539 family (inner spore coat) [Cell cycle control, cell division, chromosome partitioning]
MNFYVNQSICINSLKIGSITNSSVLQIGSAGSIQALSQLYNTGGFTEPAPQATPDAGEEPPLVPLQPPSR
>gnl|CDD|444610 COG5908, GerPC, Spore germination protein GerPC (inner spore coat) [Cell cycle control, cell division, chromosome partitioning]
MMDQSWYTYLQQLHQYLQWQQKKIQHLEQRLLQLESQLNELKQRPRTTIEKIEYKFDQLKIERLEGTLNI
GLNPSDFDTIEDFSVPQSPTKIPQQEPSPQLFQQIQQEVHAYLQEEAPEILEQLEQEYNYRLDDTYRQFI
LEDIRKQLDERIRYYLQQAKKHENIPTPDQLEQYIAQKVKRDIDQSIDHFLKHLPNEGNNE
>gnl|CDD|444611 COG5909, GerPD, Spore germination protein GerPD (inner spore coat) [Cell cycle control, cell division, chromosome partitioning]
MNFTVINRKLHVGDIRIEGVSSSSVFLIGDTDTISLSSIFDTPPESLIIGPFVPL
>gnl|CDD|444612 COG5910, GerPE, Spore germination protein GerPE (inner spore coat) [Cell cycle control, cell division, chromosome partitioning]
MMKRTSVVDLVKINSLGISSVLQIGDTQRINLKSRALAVQRESELFFGNEGSFSDFPIFSQPIPTPLPPT
PVCSQTLHECPYIRVRSIRILGVSSSSVVHIGSTESIDAESRVKHIRQLFGNESSS
>gnl|CDD|444613 COG5911, Gpr, Spore germination protease Gpr [Cell cycle control, cell division, chromosome partitioning]
KMEDLKMFSIRTDLAVEAHELAREETGGEIPGVEVEEEEEEGIKVTRVKILNEEGAKAMGKPKGNYITIE
APGLRENDTDLQEEVSKVLAKELKSLLNLPEDATVLVVGLGNWNVTPDALGPKVVEKLLVTRHLFELAPE
EVDEGYRPVSAIAPGVLGITGIETAEIIKGIVEKVKPDLVIAIDALAARSLERVNTTIQISDTGIHPGSG
VGNKRKGLNQETLGVPVIAIGVPTVVDAATIANDTIDLLLEHFGREAKEGSAFYGMLKNLDEEEKRQLIK
EVLSPYGGNLMVTPKEIDELIEDIAKIIANGINIALHPGITLENVNRYLH
>gnl|CDD|444614 COG5912, CoxA, Spore cortex protein CoxA (YrbB), YhcN/YlaJ family [Cell cycle control, cell division, chromosome partitioning]
MKKRRLLAIALLAALALAGCGTNNKPAPNTETNNVEPNNRPTRVKNTANNGDANTNNHLNGNRDRTGDYN
NENQELADRIANRAARVPGVKDATVVVTGNNAYVGIDLKGNLDGKRTDTIKYKVAEAVKSADPRIKNVYV
SADPDFVDRIRNIANDIRNGRPVSGFFDELAEIVRRIFPEA
>gnl|CDD|444615 COG5914, YpeB, Spore germination protein YpeB, HAD superfamily, activates cortex-lytic enzyme SleB [Cell cycle control, cell division, chromosome partitioning]
MRLRRWILILVLALALVGTGYWGYQQYQEKNALLIYLENQYQRAFHDLVYHVDNLEVLLGKSLAANSPRQ
LSPLLAEIWRQASAAQEDLGQLPLSLLPLNKTEKFLSQVGDFSYSLARRDLDGEPLTDEERKTLEELYEQ
AGELNQELRDLQSKVLAGNLRWMDVEKALASKLAKQADNTIIDGFKTVEKSLQEYPTLIYDGPFSDHLEK
RTPKGLTGKEISEEEAKEIAKDFLGKKGAENVTVTGEGGGKIPTYSFEVTPKGNGGTIYMDVSKKGGHVI
WMLDNRPVGEPKLSLDEALEKAEKFLKKRGYKNMEPTYSEQYDNIAVINFVYKQDGVRIYPDLIKVKVAL
DNGEIVGFDATGYLMNHHKRNLPKPKLTEEEARKKLNPNLKVEETRLALIPTDGGKEVLCYEFKGTLGGE
TYLIYINAQTGKEEKILKLIETENGTLTM
>gnl|CDD|444616 COG5915, Tgl, Transglutaminase [Cell cycle control, cell division, chromosome partitioning]
MIQIAGRPVTPDDIAAYWSLDSVERKILEAMASSPEVYRYSSLDELLFELKLRANIVAAARELDKSGASF
ATFRKSRCNPRYWTRTEEGGFRLKPDVPPSDAIRDIFINGRLYAFECATAIVIVFYKALLDVIGEETFNR
LFPRLLLYDWHYDEDLGLYTKGGGDFLPGDCLYFKNPDFDPETPQWQGENAIDLGNGLYYGHGIGIKTAE
QIIASLNRNRKPGATESAYLLDQITRPDFKYLSQYARGFSTVTSSFIRASIGSTTYLH
>gnl|CDD|444617 COG5916, YfkD, Uncharacterized sporulation protein YfkD [Cell cycle control, cell division, chromosome partitioning]
MKKLRILFLSLLLLLLFFPFSAEGEAKAKAKKDTKIPSSVLNISKENTYPNPTQDLPVLEPSELAKELLK
SANVKIENPELIKMLNESSISPSPLAIGYRATIYLGRWPLNYESKETSVNWEYQKINTNELDNRGGKSVK
KLSYKQEEQKKVKGGLTAKIPNPDDVKKMMLLKAMKKTKLPLSFETVIGAGTKKDNTYNVPPKKIGYLYA
YAPAVNEKGKVTYGEVYLVLKGSKKKIVVKNVTKQGIGAWIPVQDHLSFSFVASSQ
>gnl|CDD|444618 COG5917, YjbA, Uncharacterized sporulation protein YjbA, contains UPF0736/DUF3603 domain [Cell cycle control, cell division, chromosome partitioning]
MLYLHDVWVNWFEGEENGYNVCHFHEWRKEDGIELLDQVPLLYVEKELFNYIENDLSDLPKPLLDDVHQK
AYLRKNQERIQLEYAFVVTDGEGILAFDTMGYTIPIRKSRLIPRQEQLVYEMIENTKPESYSFQEKEVKK
EYHILSLAPELMVGLTRKERQLKQLLMMALDQLRTTKNLEEIRYWLTEWDPEQYPYIQGMDFEEAWDALY
EGVKHGWSSKHEDLCEKLIKGQPFFEKLWELENGEKVN
>gnl|CDD|444619 COG5918, YmfJ, Uncharacterized sporulation protein YmfJ, contains DUF3243 domain [Cell cycle control, cell division, chromosome partitioning]
MSILENFDQWKDFLGDRVEQAEKLGMSEETIAKLAYQIGDYLAKNVDPKNPEERLLKELWDVADEEEQHA
LASLMVKLVQNKGKH
>gnl|CDD|444620 COG5919, YodI, Uncharacterized sporulation protein YodI [Cell cycle control, cell division, chromosome partitioning]
MSMSHYYNLCCRYHGKVVRITDRDGRVHVGRITRVDRTRVYIEPVGSRGPGGFGYGFWGWGWGWGFGYGI
ALGAIAGIALAPLFFW
>gnl|CDD|444621 COG5920, YqfT, Uncharacterized sporulation protein YqfT, contains DUF2624 domain [Cell cycle control, cell division, chromosome partitioning]
NPFIKQLVNQKLNQLTPDELLSYAKQYGIPITQKQAKQIVNLLRGKNINPFNESERKRLLKQLAKITSPE
TAQKANQLFLQFIK
>gnl|CDD|444622 COG5921, YqfX, Uncharacterized sporulation protein YqfX, contains DUF308 domain [Cell cycle control, cell division, chromosome partitioning]
MRYDDEARGDEGEPQRSNAGRGLGIIALVLSILSLFFLPILLGPAGIILGFIARRRGAKTLGNWAIGLGA
VSILLGLFILPFF
>gnl|CDD|444623 COG5922, YqhG, Uncharacterized sporulation protein YqhG [Cell cycle control, cell division, chromosome partitioning]
MNQEQIHDFLERYFEANGCTILEKSPGYLTVQLTVEMDKELMNRPFYWHYVEKTGGEPEPMQLTLITDPE
AAPEDVKGEFIHFGSPRLHQIFESAKKRGRFVRLYEQVDAAGSSTPLTPWLGVNYKVSYICDRKKDELLS
LGINLINGTIVENFYERLQTLQLSPTIPDYCYTLSPLIKPESAYQRLENYLENYIQAEDHSWAEEAKERL
QEELALLEHFYEDLEEEEKPEEYEIEKEALKWQYEPRIEVEIINGGLFYLS
>gnl|CDD|444624 COG5923, YrzE, Uncharacterized sporulation membrane protein YrzE, contains DUF3792 domain [Cell cycle control, cell division, chromosome partitioning]
MSKSGRKNGSAILKGLLVAFIITLILSLILALLLTFTSLSESSLSWLTLIITLLSLFIGGFIAGRKAKEK
GWLNGGLTGLLYMLIILLLSFLGYDFTFSLSQLLKLLIALLAGAIGGIIGVNLKG
>gnl|CDD|444625 COG5924, YtfI, Uncharacterized sporulation protein YtfI, contains DUF2953 domain [Cell cycle control, cell division, chromosome partitioning]
MPWILILLLILVILLLLILLLPIKVDIRYKRKGEDDRLEITIRALRGLIRYRLEIPYIKLKGEKPGVKLK
AEKEAGLGKKEKKKKKITFEEIKRLIKQIKNLLRLVKKLKEILKYFLKKIRLTKLEWKTEIGTGDAAETG
ILTGLAWGLKGTLVALLSRYVRLVTKPEISVVPNFQRKGFETRFECIFSFRIGHIIIAGLKILKRIRKRR
GKWRNIKSKA
>gnl|CDD|444626 COG5925, YtrH, Uncharacterized sporulation membrane protein YtrH/SpoVIGA [Cell cycle control, cell division, chromosome partitioning]
MMDRFFAKLILDFFIALGVVLGGSLIGGLGAVLTGEPPLTTMLRLAKRLKIWAIVAAIGGTFDTIRNLER
GILGGELRDLVKQILYILSAFLGAHTGYLLIQWLTGEGIS
>gnl|CDD|444627 COG5926, YtrI, Uncharacterized sporulation protein YtrI [Cell cycle control, cell division, chromosome partitioning]
MRIPPYYKKPGWQRFFAGAAIGALISWFVFLYMYGQLQEKQVEENRELQEEIAELENKIEILLEDQEELN
EENKEKLTVQSIEIKITNAESYKLDNLTLHELEELIKEELSHLIGKDIETVAKSRDLLISTIENKTYTID
DFTYQLKVKKLYIFTTLSIEIELKPAR
>gnl|CDD|444628 COG5930, Cas10d, CRISPR-Cas system type I-D effector complex large subunit Cas10d/Csc3, contains HD superfamily nuclease domain [Defense mechanisms]. CRISPR-Cas system type I-D effector complex large subunit Cas10d/Csc3, contains HD superfamily nuclease domain is part of the Pathway/BioSystem: CRISPR-Cas system
NDDDEDDDEFSGESDRTEETLSLLLTLKLLTSAIDAEPILDSVEEDFLEYVEPNLAKIAAGVGEYGGHFF
DLLDEGRWAAEKKKSREDNKADQSLLSHLLNGLFPAHRLARYLEKAGLPPLSDLELRLLIALYILHDYHK
FPYGGAEREEDENKASRFDIHRKECEELIEKLGLDEFLDPDWELYIDDFLSLAVNHQDKWDTNLTLSTRG
LDPRLDDRTRLVLRPLVRLADLLASIKTPEDAENGRLQELLHALSPGQLKLTYHRLDENRGVLTNLLNNA
VIEYLEELGYTPLLYLPDGVVYLAPRDAPAPDTDDLPERVVADIKSLCAGQLSASQPGFGRDGKGLKYAD
YYPDFFSSAKLMQVVVRKTLRILADGKPSSAPKRSENLVKFQQMGELPADLDLKFEDDIRIDGLAEFGDT
IQRKFWDPLLDRIATDLELIQKTAEAFGLSEELPDILTIQPENKSLKLTGGVPYDWYYLAAQYLLHNPGI
DEDDIRELLEQLIAGLASLIEPWTIVAQAQAGDGWDDLRAYVSRVLSLPGGALTPEPPSFLDELDEYTAA
KTGRGRQKICSLSSSAYTVTEQMESAVLFLPQVYSNRQMLGGKRAKRGICSICSIEMMLRQILMSAVGKD
FEDQGYRFLYLYPTYFFTPETNKFLSRAYNRIARTRFGRLRKHFIDDDLQANSYQEFDSFIDEELQPEKG
RTFKQSYPEDLNLTFGAQTLPPGRDDTDTESWVFPAFLALALPLYLGVKVVVSESPVPPYTSGAEFEETV
LLDGGFTAVRSLYKGDSVRLDDLLGPLNALTAAYSLHLDVNGKKRNDPLWGKFLRLARDLETEPLPVFHL
LKRWLRKDDGETASIAKIRLYMRFAVCLDPYTGITQGNSTMETPLNRIRKLTELYRRFYRPNSGYGPKPH
AILRPIDEAAKVILKTGLQLSRQDLIDVVAGRLQKLLDRVARSTAYGRPLEDSDAGEEEREAVEEFAEYF
VDEIFEGSFKGDRARLARQLNLLKDGCEFAYRRLDDEERQEQSEEEPDENED
>gnl|CDD|444629 COG5931, Cas12a, CRISPR-Cas system type-V protein Cas12a [Defense mechanisms]. CRISPR-Cas system type-V protein Cas12a is part of the Pathway/BioSystem: CRISPR-Cas system
MLNYDEFTKQYPLSKTLRFELKPQGRTLDNIEELNLLEEDKARAENYERLKPVIDEGHKDFLNDALKNCD
LDWEKLAEHFLKGDKSAYAKDSKIYLEKIKKLKKEIVKTLLKADGFKGLFSKKELDQLLKDFIRKEHGNE
EEKNILSDILETFNGFLGYFSGFHESRENTYSTDTSTSVAKRIIEENFPIFLANIPKFQKALEKKIDWEE
VEVNFAVEIDEFFSVNNFNQILSQEGIDSYNRVIGGITTEDGEKEKGLNELINLANQKIKSKHLLPIFKQ
LYKQILSERDKSFIDDHFDSDEEVVQVIKEFFSQIIEQEFIERALENFKKISGFNLEGIYVNKKKLNELS
NLIFGEWDAIRLLLEEYKKNSLNDKKLEKKEKKYRFDKFVNAVKKKVFKLSDIFDGLTKMTGNDILDFEF
ENICKRREAAENYMRIIEAYRNIDKSRLNIKGNEEVVSKIKEFLDSLNELRHFLKIFNVGDDIPKDAEFY
NEFDGVFEKAFEIYKLYNKVRNYVTKKPASTNKIKINFKNSTLLSGWDKNKERNSAAIFRKGNNYYLGIL
NPKKKPKEIKTKDLSGDEEFFKRMIYKFQKGLNKNLPKCFIRSKNDKNAPAVEKPLLPTRRILEIYDNGK
FKTENKGEAFFKDSCRKLIDYFKEFIARYKSYSHFNFKLKESDSYEDIAEFYSDVEKRCYTMEFENISFE
EIKKLVDEKELYLFQIYNKDFSKKGTGNKNLHTMYFEALFSDENLEDPVFKLNGGAEIFYRKASLKKKIV
HKKGEILVNKTYSNGTRIPDSIYEEITEKKNNGDISSLDEAKAYLDKVAIKKANHDIIKNRRYTEDKFFF
HLPITLNFKASGKDNINKKVIEFIADNRDINIIGIDRGEKNLIYVSVIDQKGEILEQKSLNIIDGVDYRE
KLEEREKKRDDARRSWSEIEKIKDLKEGYLSLAVHKIAKLAIEYNAIVVLEDLNHGFKRGRSKIEKQIYQ
KFEKALIDKLSYLVFKDIKEEEAGGILNAYQLTNPVKSLNKVGKQTGVIFYTNAAYTSKIDPTTGFVDNF
YKSNLINVQSKREFFQKFKSIRYDKKENRFEFTFDLKSFNTKKTLAKTEWTVYTNGERSYYNKDKGEYVL
FNVTQEIKDALSKAGIDYDGNLIPDLLAISNGKLHKSIYYLFALALQMRVTNKDGENDYILSPVGPFFDS
RNFGKSLPIDGDANGAYNIALKGILKLERIGENKKKPDLLIFNKDWLNFMQAR
>gnl|CDD|444630 COG5932, Cas3f, CRISPR-Cas type I-F system-associated endonuclease/helicase Cas3f, fused to Cas2 domain [Defense mechanisms]. CRISPR-Cas type I-F system-associated endonuclease/helicase Cas3f, fused to Cas2 domain is part of the Pathway/BioSystem: CRISPR-Cas system
MNVLLVSQCEKNALKETRRILDQFAERIGDRTWQTAITQEGLDTLRKLLRKTARKNTAVACHWIRSRNRS
ELLWIVGNARRFNAQGAVPTNTTERDILRAEDENDWHTLEDIKLLAALAALLHDLGKANALFQAKLKGNG
KSKGDPYRHEWVSLRLFQAFVGGDTDEEWLERLADIDPDDEASWLARLQKDGLDANAANPFADLPPLAQA
VAWLIVSHHRLPLLPSDDDDGDKLRNLNAPQLQQLLAQIDADWNSINREDAWAAKRIQAYWQFPHGLPVD
SAKWRKQAAKLAKRLLKHPSLLAGAWLDNRFTMHLARLCLMLADHHYSSLPATPKWRDPDYPLYANTDRK
TGQLKQKLDEHLIGVAQNALLIARALPSLERSLPALTRHKGLKQRSADPRFRWQDKAFDLAASLRERSEQ
QGFFGVNMASTGCGKTLANARIMYALADPKQGLRFSVALGLRTLTLQTGDALRDRLGLGDDDLAVLVGGS
AVRELHELNKEKAEEEQTGSESAEALLDEDQYVSYEGSLDDHPLLQWLLHDPKLRKLLSAPVLVCTIDHL
IPATESLRGGRQIAPMLRLLSSDLVLDEPDDFDLADLPALTRLVHWAGMLGSRVLLSSATLPPALVEGLF
NAYRAGRAAYQRNRGQPPAPVNICCAWFDEFGTQAADCADLEAFRQAHQAFVSKRVEKLAKQPVRRKAEI
VPLPSPKKKEAEVYRALAETLLQAALRLHQQHHQTDPKSGKRVSFGLVRMANINPLVAVAKALLALGAPE
DTRIHLCVYHSQQPLLLRSAIEQRLDAVLKRKDPDALFQHPEIRQALDKHPEKHHIFIVLASPVAEVGRD
HDYDWAIVEPSSMRSIIQLAGRVRRHRPGEPAQPNILILDKNLKALKNGGKPAFCRPGFESKSFKLSSHD
LTELLDPEQLRVIDAIPRIQEPEKLEPKKNLVDLEHARLADTLLGPKDLPLPLNAAALWWRPHAHLTAEL
QQRQPFRKSTPPEVDLVLLPDEDDEPVFYRFNDGGEPGYVPVEASLNIRPDPELELGPGISPWLQRDYLA
ALAELAEELDMSLEEVARRFGEVSLPERDEGWRYHPQLGFYKEK
>gnl|CDD|444631 COG5933, Cas5f, CRISPR-Cas system type I-F effector complex subunit Cas5f/Csy2, RAMP superfamily [Defense mechanisms]. CRISPR-Cas system type I-F effector complex subunit Cas5f/Csy2, RAMP superfamily is part of the Pathway/BioSystem: CRISPR-Cas system
MSQPSGLLVLPRLRVQNANAISGPLTYGFPAITAFLGFMHALSRKLQEDHGLALEGVGVICHHFQVQAYQ
SGYDRTFNLTRNPLTKDGKTAAIVEEGRMHLDVSLVIEVSGSLDEGDEDREALAQQIAELLLTQRLAGGS
VLPIGPVQLIDLPDDAEPRAKEFRRLRRRLLPGFALVDRSDLLAEHLKELQQTNPEATLLDAWLDFSRLN
HRPVPDDEKGKVKWEYVRKPGSGWLVPIPVGYQAISPLYPAGEVANARDPSTPFRFVESVYSLGEWISPH
RLNDLEQLLWRYHSDPENGLYLCRNGYQADVQEEDTNDE
>gnl|CDD|444632 COG5934, Cas6e, CRISPR-Cas system endoribonuclease Cas6e, RAMP superfamily [Defense mechanisms]. CRISPR-Cas system endoribonuclease Cas6e, RAMP superfamily is part of the Pathway/BioSystem: CRISPR-Cas system
MTTFVDIHVLQTYPPSNLNRDDTGSPKTAVFGGVRRARVSSQSWKRAWRTSFEEALAGHLGVRTKRLGEE
VAERLVEQGVDEEEAREAAEAVAAAFGLKLKKPKKKPKDDLETEQLLFLSPEEIDALAELAAELAAELKK
PDKKELKLLLRGGHAVDIALFGRMLADDPDLNVDAAVQVAHAISTHAVEVEFDYFTAVDDLNPDEEDTGA
GHIGTVEFNSGTFYRYACIDVDLLVENLGGDKELARRALRAFVEAFATVMPTGKQNSFAARTLPSYVLVE
VRDDQPRSLANAFEKPVRARGGGLLEPSIEALADYAAKLDRAYGDCADAAFVLNVGDAALAALGERVGSL
DELVDFVAAAVRE
>gnl|CDD|444633 COG5935, Cas6f, CRISPR-Cas system endoribonuclease Cas6f/Csy4, RAMP superfamily [Defense mechanisms]. CRISPR-Cas system endoribonuclease Cas6f/Csy4, RAMP superfamily is part of the Pathway/BioSystem: CRISPR-Cas system
MDHYIDITLLPDPEFSESFLLSALFAKLHRALVELGAGDIGVSFPEYGDKGKTLGSKLRLHGSEAALEKL
MATKWLQGLRDYTHITEIAPVPEKVKYRTVRRVQAKSSPERLRRRLMKRHGLTEEEALQRIPDSVEQRLD
LPFVQLKSLSTGQRFRLFIEHGPLQAKPVEGVFNSYGLSATATVPWF
>gnl|CDD|444634 COG5936, Cas7f, CRISPR-Cas system type I-F effector complex subunit Cas7f/Csy3, RAMP superfamily [Defense mechanisms]. CRISPR-Cas system type I-F effector complex subunit Cas7f/Csy3, RAMP superfamily is part of the Pathway/BioSystem: CRISPR-Cas system
KKNLKTASVLAFERKLDPSDALFYAGNWDNRDSQWTPLAIREKSVRGTISNRLKNKITNDPAKLDAEIEK
PNLQTVDVAALPADADTLKVSFTLRVLGGLGTPSACNSADYQAKLQATVKGYIAEHGFAELAKRYAHNIA
NGRFLWRNRVGAEQIEVRVSHLNDGASGQSWTFDALDYSLRDFDQPDEDLAALAAVIAQGLAGERFVLLE
ITAFVRLGAGQEVFPSQELVLDKGKGKKSKTLYQVNGVAAMHSQKIGNALRTIDTWYPDAENGAGPIAVE
PYGSVTTLGKAFRQPKEKQDFYTLFDNWVLKDKLPEVEQQHYVMAVLIRGGVFGESG
>gnl|CDD|444635 COG5937, Cas8a4, CRISPR-Cas system type I-A effector complex large subunit Cas8a4 [Defense mechanisms]. CRISPR-Cas system type I-A effector complex large subunit Cas8a4 is part of the Pathway/BioSystem: CRISPR-Cas system
MYQDKYYIPKDTGTYADMLEAYGLALLLSRLLGDERVTIKDRGDYYEISLNRPITLEMLGNCRYDPGYPY
IKTKKDDAIPDGIDYEFEKEKANLYNEFYKEQKKTSKKKRAKIDKKAYKAYSNSPNEPRPDWDLLKALNP
LRAANGYNKLLFQNLYNNRENIKEAVKHVLRLYASPFQNQDEVEKSAKRKISSGDLRKIVDVTASQALNP
ISGKGVNRTKPDGVGPGGLPSFVVDWFAEWMKYRGMFSIMLPYRNGDDFKIYVLVPGEINPSALSSVYKD
LLKLVLGWGAVRLDITAVLRLAEILIEHSEVYQDEEGSKRRQRRPAQVISGLYTAYFKSMGTAAALMNVS
FLGLPGWFTIENKDDAGAWIDIIDEHRDCIGNLNEEHSSDLPLLQQYRDFISSGNLEDFLDFTAEYSTFL
MSKREKNEYGVRQFSISNLRRLFMMEKNYSEILKNEGFLNIAKAIRRSTVTAQYRKSQGDRKYEIRYGLA
QDLKRKSKYKDEFVIALSDFVQDYNAENARVAEKRPEKRRASVSTQDLEDVLELIDKYGSELVAMLLLAY
GYAREEKTLDDNMTSVSKEGDVE
>gnl|CDD|444636 COG5938, Cas8b1, CRISPR-Cas system type I-B effector complex large subunit Cas8b1 [Defense mechanisms]. CRISPR-Cas system type I-B effector complex large subunit Cas8b1 is part of the Pathway/BioSystem: CRISPR-Cas system
MIEAIKEIGEYLLEETKDLLDELIEDPLKPKKYLYLVIIIFDLEEGDVEFIGVDLEEFDKDKVSKYLYVG
NSSGGSPQAKLTTKNLKYLLGNRIPNLFKKLSKYGLEDNELKKKIKNIEEILDKNKEKILKALEKKLEDL
IELKKKDGVLLTIKLDGKYLGEIPEYREALLRYLIEKLFNTKEESSEEGVCSVCGKKEEVYGTSDKFKFY
TTDKPGFASGFNKKKFWKNYPVCEECALKLLKGEKYIERNLKFRFGGLNYYIIPKFIGESELILEEILEI
LKDKKDIALNLESLKELEEDEEEILDILEDEDDLYNLNFLFYKKDQNAFKILLLIEDVPPSRLSKIFEAK
EKVDELFKNLNGLKFSLGTIYKLFPVRKNNKKDKDLDKYFLEIYDAIFKGRPIDRSFLIDIFLELIRKDF
RNDRHTEDKNIKRKILQAFMLLEFLEKLGLLKEEETMMSKLNELREEIKEFFEKIKDMFYDNEKKALFLL
GVLIGYLLNIQYKKRDKSKPFLKKLNGLGMDKKDVKRLLNEILNKLRQYKHNEGKFAELFELISEYFLLA
NDNWNLSIDENVFYFLSGYAYATKLAISKKEKEEEEDEEN
>gnl|CDD|444637 COG5939, Cas8b2, CRISPR-Cas system type I-B effector complex large subunit Cas8b2 [Defense mechanisms]. CRISPR-Cas system type I-B effector complex large subunit Cas8b2 is part of the Pathway/BioSystem: CRISPR-Cas system
CILCGERAADTDFSTGIRSNFPGLNSDNVINFFWNFNPGLPICPICLLIYQCLPLGLTRVGGRFLFVNSD
TSILELYFANNLLKDNLKKISSSQAENLLFEFLSEIVLEVEEEKAEWELQNITFYEFTNDGQGPKLYIYN
IPKPLAEFLRAAKDHYKKNWKKLVKKYYKIKKKEKPRYNEVLEKLLNNRSIYAALYFLLRYFLSSDNGST
YLSPYVVNILWLLLERYLKEVMNMDEKRLWKIKKLGDELAEYLRKEAENKINSLAYKLLNALKAGNRYQF
MDTLLRIYMDYQKEIPSGLKELNDKDREFLTLGYSFIRGLLLIEEEEENPEEEEDE
>gnl|CDD|444638 COG5940, Cas8b3, CRISPR-Cas system type I-B effector complex large subunit Cas8b3 [Defense mechanisms]. CRISPR-Cas system type I-B effector complex large subunit Cas8b3 is part of the Pathway/BioSystem: CRISPR-Cas system
LNAPLVFQSGLLYATSLTIRLRAGGLGLELTLLKFEKKTLLPHQAGIAGSIGATSWTNELDDIQLDLVGL
DATNLKWFLKDGEARAKLIQIDRDGIDNALMGTFLQHLRAQFSTASKGTTTIFLKSTKLRSKQLIVEEYK
IRIDKYAPQIYASFLLGGDWQYERLVLLKGPISPVAGAYPGAAERHIGTKVECFLLYAAELSCVFLLAPY
CLQYKCSLCLVEKDVSNLVIFIRDLIDFELRRRERWPLSALDRKRSSVSLAGLAGLLLLNLKEEDNEVKR
ARACEVLVAMKMNAWSRQQKLRVIEVRVRLIYLELDLLKAAFLFFKKAQRKPDKKGTAKAVSISPIRPLI
AENLAAGRPWYADFAELLVEEDDKIKLFSQLRFERKGLIAMIENSWEDEAEQAFIQSFHEALRRRFAKIY
ERTQEGGRTFNARIERENERIRNALARAKTADDFRKALADFWARAGSNASLQEHWGELLPLITKDSNWKR
ARDLALLALASYQ
>gnl|CDD|444639 COG5941, Cas8c, CRISPR-Cas system type I-C effector complex large subunit Cas8c [Defense mechanisms]. CRISPR-Cas system type I-C effector complex large subunit Cas8c is part of the Pathway/BioSystem: CRISPR-Cas system
ILQALYEYYERLLGDGEPDLPPIGFSTEKIHFEIVLDADGNFVDAEDLRDGSGKKKKPRLTLVPATAKRT
SGIAPNFLWDKTQYVLGVTAGGGKRTAEEFAAFKELHLEWLASSDDPGLQAVLRFLEKWTPEDLDLLPKW
KPEIQGDANVVFRLDGDPSYLHERPAVRAAWARFLAATDAKQGLCLVTGEKAPIARLHPAIKGVRGAQSS
GAKLVSFNDDAFTSYGKEQGENAPVSEEAAFAYTTALNWLLARQSQRLQIGDATVVFWAEAGDEAEDLFA
DLFDPPDKPDDDEETQKIAALLKKIRQGYPLDLDPDTRFYVLGLAPNAARLSVRFWREDTFGDFAERLAQ
HHEDLAIEPPPKQFKGAPSLWRLLLATAGQGKSENLPPNLAGELMRAILTGGPYPRDLLNAALMRIRADG
DVNWERAALIKAALNRGYRLNKTKKEEYPVSLDPENTNRGYLLGRLFAVLEKIQEAALGEKNATIRDRYY
GAASATPASVFPTLLRLLQHHLAKLRKKKPGLAVNLEKLIGEIMDGFPEDFPRHLSLELQGRFALGYYHQ
RQAFFTKKETKEAAEA
>gnl|CDD|444640 COG5942, Cas8e, CRISPR-Cas system type I-E effector complex large subunit Cas8e [Defense mechanisms]. CRISPR-Cas system type I-E effector complex large subunit Cas8e is part of the Pathway/BioSystem: CRISPR-Cas system
FNLIDEPWIPVRRKDGRREEISLRELLDRAHPIVDLAGPRPDFEGALLRLLLALLQRAFGPEDDDEWRAL
WETPLPPEELDAYLARWADRFDLFHPGPPFMQDPGLLAGEVKPIAKLLIEAPSGNNKDLFDHRGRVEALS
PAEAARALFTLQTNAPSGGHRTGLRGGGPLTTLVLVLPEGRTLWETLWLNVLPYPPLDRESSEDDVPPWE
RAPTRTSEVKGGERTPSDVGPLQLYTWQPRRIRLDPEEDGGALVVGYVTINYGVNYKEGAWPHPLTPYRR
SKKDEGELLPVHPQPGRALWRDWLGLLPTSEDDGRRPALVVRWARDLRRDGSLAPLRLWVFGYDMDNAKA
RCWYEERLPLPLALLDDEPELRERVRDLVEAAEEAAQALRSALKDAAFAAGSDDKKGDRSAADEAFWART
EAPFRRLLADLAAGPDPDEALAEWLRALRRAALDLFDAALAGAPDDARDLRAIAEARRRLRRRL
>gnl|CDD|444641 COG5943, Cas8f, CRISPR-Cas system type I-F effector complex large subunit Cas8f [Defense mechanisms]. CRISPR-Cas system type I-F effector complex large subunit Cas8f is part of the Pathway/BioSystem: CRISPR-Cas system
MSIQGLRSAIEAFIEERKEAKLEKLKKDDEKAEQELAEKRQELEEKYELDNWLEDAARRAGQISLVTHAL
KFIHPDAKGSNIYAQPDSLPPDGYLGSHNLAQLAIDAVGNAAALDVYKFLKLEVDGRSLLALLQADDPLA
LAALSDDPEQAEEWKDGFKQLLESKGKPASHKLAKQLYFPVGADDDEYHLLSPLYPSSLAHELHQRINDI
RFSEEAKAARDARKKNKWHETGYVDYPNLAVQKLGGTKPQNISQLNSERGGRNYLLASLPPVWKSRDLRP
PLNTESFFDRSERRYQVRSTVRELHRFLKSVPKNNLDIRDKRDAYLDEIIDELLDFAAEIQNLPAGWSKD
EECRLPRYQKLWLDPYRADDDAEFAEEREKGDWPEEIAKDFARWLNRQLRKRKEALDLGDAEYREWRKEV
KQDLREFKEALR
>gnl|CDD|444642 COG5944, Cas8g1, CRISPR-Cas system type I-G effector complex large subunit Cas8g1 [Defense mechanisms]. CRISPR-Cas system type I-G effector complex large subunit Cas8g1 is part of the Pathway/BioSystem: CRISPR-Cas system
MTEVIRLTGLDPTNPLAFLAALGLLRLLAEQADPGARLAWEQEVFGWRPVLHLPTELSREELVEFLAEYL
PTPIVAPWFGGSGFFKADNLKPPEAFRALLSSATERLAAKPGDRRKADLLAALRNDVPDDAAVGVLTTDK
GKTKPTPLLGTGGNQGRLDFTNNFLQRLRQLLDGKTPEPAEETRAFLREALFGPWTYKDEQASSGRWDPA
DDRRYALRAGDPSSSKGKEGGQLTNPGANILAIEGLPLFPGAARGRLGSVELATTGFATSERRRGEFWWP
LWRQPVTLAVLRSLLTEPRLQRDRPARNTLDFAVARGVVAVFRSGFRRIGVRSGPYANFSPADPRPVVWT
GRSRDSQPRA
>gnl|CDD|444643 COG5945, Csb1gr7, CRISPR-Cas system type I-G effector complex subunit Csb1, RAMP superfamily Cas7 group [Defense mechanisms]. CRISPR-Cas system type I-G effector complex subunit Csb1, RAMP superfamily Cas7 group is part of the Pathway/BioSystem: CRISPR-Cas system
MSTLDLDTLQEAVAGAAALRIRAELQPAGGPGDKIFPPTYPDLGAATYATEERRPDGESVRCVLVDSVQS
QANRMEEALLDAIRELRGLPLIEVDFPGEGEGTLLITSLQAPHRIADAILRDSLLDGTPFRKSELGRALR
DASPKNATALFEYDPTALLFGAWDSTGPLGGLGAKFARALVSEIVGIGADVGERGGSRIDPLGIQGDAGP
GFGAVPFGRTEKVAEAKTAYFNPDLAGKRGGGLGKSAETLLIILALGKLSALLAGGLRLRTACDLRVASL
LLLLAARALLRLRAERAAAALASLLAALAAAAALALTPRGLVAAETGSAPEETLRLERETLTAGLPKAAG
LDLLEAALLILEAAALEALVALSGAEGSQELLAP
>gnl|CDD|444644 COG5946, Csb5gr5, CRISPR-Cas system type I-G effector complex subunit Csb5, RAMP superfamily Cas5 group [Defense mechanisms]. CRISPR-Cas system type I-G effector complex subunit Csb5, RAMP superfamily Cas5 group is part of the Pathway/BioSystem: CRISPR-Cas system
MLGLEIRYLTGRAHATDGADRGRPEWPPSPWRIFSALVAAYFETGEDAERAERAALEWLENLPPPVIALP
AAVAARVTTHYVPVNDLGAGRGANLESLPPARTRQPRTFPAAVPPDAPLFLVWPDAEPTEAHLAALDRLC
GRVTYLGHSASLVRMWVLEELPAEVDSPAVPGSGGAGERLRCPLPGSLESLAALFETLRASGGRRPLPAL
WVTYRREPLAPPDPRATTRFDSNLLRLRLVSGPRLPVTAALAVTEALRDALMSRCPDRAPIPEIVSGHRP
DGEPDGAPHLAFLPLPFVGHPHADGHLLGVALYLPRGFPLLEREGVLAALPRLRTLRLGRLGRWRLELEP
LSRPRYSLLPSTWTGPARRWASVTPVVLDRHPKKGGLAAEAEAAKQIRKACRRAGLPEPVAVVTDRHSLF
AGVPRAAHKFPRYRARGSIPARPGVHAELEFAEPVAGPVLLGAGRFFGLGLFRPVREG
>gnl|CDD|444645 COG5947, Csc1gr5, CRISPR-Cas system type I-D effector complex subunit Csc1, RAMP superfamily Cas5 group [Defense mechanisms]. CRISPR-Cas system type I-D effector complex subunit Csc1, RAMP superfamily Cas5 group is part of the Pathway/BioSystem: CRISPR-Cas system
MQIYECTLELHDNVFFASREIGRLYETEPYIHNYALAYALGLASSRYVDATQRPTYEEDLAPLNQQGIYV
TPARPVSVSFVTNTFNAASDNYWVPNYEMEKFPNKGAQKNFPSFGRAKELAPGSTFRFYVISQDELELPK
YIRLGKWMSKARVEYKELPVSKQKSGTFTCNHPLNPLDLPFTIQLLSYDVINMPPVSLIKNAQFRGEYYQ
IDESKDIKLPADMKFLAGKRN
>gnl|CDD|444646 COG5948, Csc2gr7, CRISPR-Cas system type I-D effector complex subunit Csc2, RAMP superfamily Cas7 group [Defense mechanisms]. CRISPR-Cas system type I-D effector complex subunit Csc2, RAMP superfamily Cas7 group is part of the Pathway/BioSystem: CRISPR-Cas system
MTFLEKLQSSEFHYEIPKKPMGKYIHFVTLRETQSYPVFRTDGELNVARVRAGLEDTDQISRLVMFKRKQ
KTPERLTGRELLRAYGLIGRKPKNETECEYNGKPSCKFCPDCIVYGFAIGDSGSEKSKVYYDDAFSLLPK
DESHGEFTFNAPFEDGTMRDSEDGENSSSLNEQDHIKPGVFFPSVVTLRDPTLEEFRYVLGNILRTRRYG
AQTSRTGNMRNHLIGIAFADGEIFSNLELTQALYDLLKEDNEDPLNTSDVLTAAKEVLHNLLAKEGVRST
VINGDELDELLNEVDAILSDEEQLKALLKRLAQETANYADTWK
>gnl|CDD|444647 COG5949, Cse2gr11, CRISPR-Cas system type I-E effector complex small subunit Cse2 [Defense mechanisms]. CRISPR-Cas system type I-E effector complex small subunit Cse2 is part of the Pathway/BioSystem: CRISPR-Cas system
MSETEERDSRVGEFVARWWRRLQRDRALDRGDRARLRRALGPEPGALPPAWPRLARFLPGDEPPREERAL
ALVAALLALHKQSDPGRSLGRALARLRGGDRPGVSELRFRRLLAADTPDELLRHLRRLVRLLRSKEIPVD
YARLADDLLYWQDEPADRVRRRWARDYYRAAAPEEDDTA
>gnl|CDD|444648 COG5950, Csx10gr5, CRISPR-Cas system type II-D effector complex subunit Csx10, RAMP superfamily Cas5 group [Defense mechanisms]. CRISPR-Cas system type II-D effector complex subunit Csx10, RAMP superfamily Cas5 group is part of the Pathway/BioSystem: CRISPR-Cas system
MKRIELTITLLSPLLIASRKGDGNVVETLDYIPGSVIRGALAARLLKRLGLENATEDRDFRRLFLDGKAR
FLNAYPAVKGQKGYPTLPVPLSLRSCKTNPGFGPHGVFDTLLDRFCAPECPECRERLEPREGFYTLNDLE
EYRKHSVKKRILTHVGIDRRRGRSEDGILYSYEALNPGQTFRGEILGDDEALAEALQKLLNDGDGEIRLG
GSRSRGYGKVKITLSEIEDPSLLELPSDLDDRTYFTLTLLSDAILRDEWGRTTVSPDAEMLEQLLGVKKE
ALELHSAYSRYRYVGGFNAAWGLPRPQELALAAGSVFVFSLPEGPDDDWLEKLEELEAEGIGERRAEGFG
RVAINHPFHEQFREKAP
>gnl|CDD|177099 MTH00001, ND4L, NADH dehydrogenase subunit 4L; Provisional
MYYKYLILVVILFLLGIWGIILNRGHFIIMLVSIELVLLSTFFLFLINSIEIDLLIEQIFTIMGLTIAAA
ESAIGLAIMVAYYRIRGTISLKSLNSLRG
>gnl|CDD|214398 MTH00004, ND5, NADH dehydrogenase subunit 5; Validated
MTLLLNTTTLLTLLILLTPILLPLLSKNLKNSPTTIKTTVKLAFLISLIPLTLFLNSGTESITTNWPWIF
TTTFNIPISFKLDQYSLMFLPIALFVTWSILEFSTWYMASDPHITKFFKYLLIFLIAMLILITANNMFQL
FIGWEGVGIMSFLLIGWWSGRAEANTAALQAIIYNRIGDIGLILSMAWLAMTLNTWEIQQLFSPTQTPTL
PLLGLILAATGKSAQFGLHPWLPAAMEGPTPVSALLHSSTMVVAGIFLLIRTHPLLQNNQTALTICLCLG
ALTTLFAATCALTQNDIKKIIAFSTSSQLGLMMVTIGLNQPQLAFLHISTHAFFKAMLFLCSGSIIHNLN
NEQDIRKMGGLQKTLPITSSCLTIGNLALMGTPFLSGFYSKDTIIETLNTSYLNAWALLLTLLATSFTAA
YSLRMILLVQTGFPRTPPTTPINENTPTIINPITRLALGSILAGLLISSTILPTKTPPMTMPTTTKLAAL
IVTILGILLALELSNMTTTLTPPKQNTLHNFSNQLAFFNPLTHRLLPMTLLKSSQKIATHLIDLSWLEKM
GPKGLANLQLTASKTLTTLQKGLIKNYLTSFALTILLLLLLT
>gnl|CDD|164583 MTH00005, ATP6, ATP synthase F0 subunit 6; Provisional
MLTDIFSSFDPATNSLFNNLSSTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHL
KGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPD
WLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVG
ICLIQAYIFCLLLSLYSDDHP
>gnl|CDD|133649 MTH00007, COX1, cytochrome c oxidase subunit I; Validated
MRWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPV
FIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSV
DLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDR
NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVL
GFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGL
TGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNL
TFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLE
WQDTLPLDFHNLPETGIITTP
>gnl|CDD|164584 MTH00008, COX2, cytochrome c oxidase subunit II; Validated
MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPA
LILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDN
RAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIV
LEAVDTKSFMKWVSSFAE
>gnl|CDD|177101 MTH00009, COX3, cytochrome c oxidase subunit III; Validated
MIRQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHT
SYVTKGLRWGMILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGV
TVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGS
SFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFVDVVWIFLYLCIYWWGS
>gnl|CDD|164586 MTH00010, ND1, NADH dehydrogenase subunit 1; Validated
MNISFFISILLSYVMALLAMAFYTLLERKALGYFQLRKGPNKVGLAGIPQPFADAIKLFTKEQTKPSPAN
ITPFLGAPMMSLILALLLWSLYPHKHPSFFLKFSILLFLCVSSMNVYTTLGAGWTSNSKYALLGALRSVA
QTISYEVSMSLILLSALLILQTFSFSKIIMSQYSWILLMIIPLTVSWFITNLAETNRTPFDFAEGESELV
SGFNVEYSSGLFALIFMAEYANILIMSLFTSVFFTSFIPSIFISDLMLILKTVFLAFLFIWIRATFPRMR
YDRLMNLTWKSFLPMSLTSLMISIPIMFLLL
>gnl|CDD|164587 MTH00011, ND2, NADH dehydrogenase subunit 2; Validated
MMSTFPTMFLFSSTMTLGTLMALSSNNWLFLWMGMELNLLSFVPLMTSSKMNQESEAAVKYFLAQALGSG
LLLLGMTMMWSFPSLLKNITALMLLVSLMLKLGMAPCHFWFPSVMSSISWTLCLILSTWQKIAPLSILFF
FTSHNILPMMTSMAAMSALAGGLGGMNQTQLRPLLAYSSIGHMGWMTMISVFSPSMAILYFMTYIIITTP
LMLLFAYLNAFSTKFNSKISSMSQTTSMSLFIMLLSLGGLPPFTGFMPKLMAIETLTSNSMILILLVLIV
GSLMNLFYYLNLIFNFMYLSPTFSSLKSAPYEPKTKILISMCTLSLGLIP
>gnl|CDD|164588 MTH00012, ND3, NADH dehydrogenase subunit 3; Validated
MSLMMIPMMISLILPPLVLGAAWVLAARSTADREKTSPFECGFDPHKTARIPFSLRFFLLAIIFIVFDIE
IVLLMPVPTILMTSTSKTVVYTSILFLLILVIGLIHEWREGSLDWSS
>gnl|CDD|133655 MTH00013, ND4L, NADH dehydrogenase subunit 4L; Validated
MMSPLFILSISPFISMFNLSLQRKHLLMSLLSLEAMILSLALFIPLSLMFANQVNGMLAIVLLTFGACEA
SLGLSLLVLMTRSYGNDMLKSLTSNKC
>gnl|CDD|214399 MTH00014, ND4, NADH dehydrogenase subunit 4; Validated
MLKLIMPLISLLLLPLIKYPWSWALTFSTLLLLSLFTLLNLYPMSAPYSMFTESLSSDMLSAPLITLTLW
ITALMILASFKIFQNNKAPKTFMTNILILNLILLLTFSASNLLMFYIFFEASLIPTLFLILGWGYQPERL
QASFYLMIYTVTASLPLLMSILLIFYTNNSLSMLMSSMEPPSIYLMNLWWLITILAFMVKMPLYTVHLWL
PKAHVEAPVAGSMILAGILLKLGGYGLLRMSSLFMHINKSLSAPFSSISLVGAVITSLICIRQPDLKSLI
AYSSVGHMGLMTAGIMSNTSWGWQGALAMMIAHGLCSSALFALANMTYETTHTRSLFLTKGLLSLFPTMT
MWWFLLSAANMAAPPSINLLSEIMLLTSILSSSLSTAILLAITSFLAAAYSLFLYTSTQHGSPPSFMNPL
NLFTPRNHTLMTLHLVPLFILILKPDLITNWL
>gnl|CDD|164590 MTH00015, ND6, NADH dehydrogenase subunit 6; Validated
MSLSFFLILMISLTCSLFLATTPITLGINILMMALLLATTMASALSSWFAFLTFLIYVGGMLVMFAYFLA
LTPNQQLNLGPMAKYTLITLLTLSTTLKLTNPPSPSFFSSTQGNTFLYQPENAPLLIFLALILLLTMVIV
VKLTRRSSGPLRPFK
>gnl|CDD|177102 MTH00016, CYTB, cytochrome b; Validated
MFSPMRKTHPLIKIMNGSLVDLPAPSNLSIWWNFGSLLGLCLVIQILTGLFLSMHYTPHIDLAFSSVAHI
SRDVNYGWLLRNLHANGASFFFICLYLHIGRGIYYGSYFLMETWNIGVILLLLTMATAFLGYVLPWGQMS
FWGATVITNLLSAIPYIGKMLVQWLWGGFSVDNATLTRFFALHFLLPFVIAALSMIHLLFLHQTGSNNPL
GVNSNSDKVPFHPYYTSKDIVGFIVMLFLLLSVVLLWPNILGDPENFIPANPLVTPTHIKPEWYFLWAYA
ILRSIPNKLGGVVAMFASILILFFLPFIFKQKFRGLSFYPLNQILFWLLVSNFLLLTWIGGRPVEPPYEF
LGQIFTVFYFFYFMINPLLMKLWDKLLK
>gnl|CDD|164592 MTH00018, ND3, NADH dehydrogenase subunit 3; Validated
YGLFILLIFSVVLSALFSGASYFLGVKQPDREKVSAYECGFDPFGFPGRPFSIRFFLIGILFLIFDLEIS
FLFPWCVLYNQIAPFGFWTMVGFLFILTLGLIYEWIKGGLEWE
>gnl|CDD|214400 MTH00020, ND5, NADH dehydrogenase subunit 5; Reviewed
MYLLVLFLPLLGALLSGLFGRKIGEKGAGILTSSCLIISLSWSFLIFYEILFNSSTTYIKLWRWLDSDLL
TVYFGLQFDGLVAIMLLVVTTVSTLVHIFSTAYMRGDPHIPRFMSYLSLFTFLMVVLVTSDNYLQLFIGW
EGVGLCSYLLINFWLTRIEANKAAIKAMLVNRVGDIGLLLAMFLLWDRFGSLDFSSVFNMVVSAPSSDIT
LICLFLFIGAVGKSAQLGLHTWLPDAMEGPTPVSALIHAATMVTAGVFLLIRSSPLFEQAPLALIIVTIV
GSLTVFFAATVGLVQNDLKKVIAYSTCSQLGYMVVACGLSHYSISLFHLMNHAFFKALLFLSAGSVIHAL
SDEQDMRKMGGLISFLPLTYIFFLIGSLSLMGFPYLTGFYSKDLILELAFGQYYLIFAYWLGCFSALLTA
FYSIRLIYLTFLSNTNLKKAVFFHLHEGDWNLLLPLGILALGSIFVGYLAKEMIWSFQITLPPIVPLSIK
LLPVFLSLGGIGLVIILYFYSSKTFRVPFSFIGRNSYTFLGSAWQFNYILNYFLIKKIWKGGHLISYRTI
DKGVLELVGPKGISNFLIILTQGLSSLQSGLVFNYALVILIGVAIFIWGL
>gnl|CDD|214401 MTH00021, ND6, NADH dehydrogenase subunit 6; Validated
FFSLGIIGSGIMVISALNPVHSIFWLVVVFVNSAVFFILLGLDFLALMFLIIYVGAIAILFLFVIMLLNL
TDFPPAFGGEADMTNYIPIGLIIGTLFFSEIASSWLIIGGPYVERWDLAFPWFLISYHNIEALGRILYIT
CYYLFLLASFILLVAMIGAIVLTQEPGSEVGPLSKKQDIFFQISRANS
>gnl|CDD|164595 MTH00022, CYTB, cytochrome b; Validated
MPLRKENPLLSIVNGFLVDLPSPSNISYLWNFGSLLGLCLVIQIITGCFLSMHYCSDVSLAFASVGHIMR
DVNYGFLLRYLHANGASLFFLCLYIHIGRGLYYGGYLKFHVWNVGVVIFLLTMATAFMGYVLPWGQMSFW
GATVITNLLSAIPYVGTDIVQWVWGGFSVSNATLNRFFSLHFLFPFILAFLVIVHLIYLHVDGSNNPIGL
NSSVDKVSFHVYYTSKDWYGIVVLFFLLSFIVYFAPNLLGDPENFIQANSLVTPVHIQPEWYFLFAYAIL
RSIPNKLGGVVAMFFSILILFFLPLLHTSWLRGLTFRPLGRMAFWFLIVDFILLTWIGSQVVEEPFILIG
QLLSFFYFFYFLVLIPLLGELENQLLFKN
>gnl|CDD|214402 MTH00023, COX2, cytochrome c oxidase subunit II; Validated
MFNNFFYRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFL
EIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLN
SGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEI
CGANHSFMPIVIEAVSLDKYINWLLSLSND
>gnl|CDD|214403 MTH00024, COX3, cytochrome c oxidase subunit III; Validated
MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGH
HSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSS
GATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVII
GTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVDVVWLFLYLCIYWWGS
>gnl|CDD|214404 MTH00025, ATP8, ATP synthase F0 subunit 8; Validated
MPQLDTTTYLTQYRWTLIVLFLLLFFLVFFVLPTIKRNWLIRKSLMKKGAAFSKGLGLNKEVVFIWDWLL
>gnl|CDD|164599 MTH00026, COX1, cytochrome c oxidase subunit I; Provisional
MTSFVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFL
VMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHS
GGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITML
LTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLA
IGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNLIFTTPMAWALGFIFL
FTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLM
FIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREEPFDINIM
AKGPLIPFSCQPAHFDTLEWSLTSPPEHHTYNELPYIVGGPKSS
>gnl|CDD|214405 MTH00027, COX2, cytochrome c oxidase subunit II; Provisional
MKNVYCLTIVNWEGGALYPMNVASMIKDANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLI
IRILLGNNYYSYYWNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGFSANITIKVTGHQWYWSY
SYEDYGEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVP
GRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGREDV
>gnl|CDD|214406 MTH00028, COX3, cytochrome c oxidase subunit III; Provisional
MSLVYHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGH
HTQIVVRGLKLGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSS
GATVTWAHHAIIGTGNPASLEKGTQGIEGPNPSNGAPPDPQKGPTFLLSDFRTNAVIGLLMTILLGIIFT
GLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHF
VDVVWLFLYVFVYWWGS
>gnl|CDD|177108 MTH00029, ND1, NADH dehydrogenase subunit 1; Provisional
MTIYSYITVTIKLLIIFVPLLLSVAYLTLAERKVLGLMQNRKGPAIVGPWGLVQPIADGVKLLTKELIIP
SQANKFLYYIAPIISFTLAILAWAIVTMDQGVFLSDLDVGVLYFLAISSLSVYAILLSGWASNSRYPFLG
AIRCAAQMISYEVAIGLIIISVILCVGSLNISEIVISQRSVWLIIPLFPAAIMFMVASLAETARAPFDLT
EGESELVSGFNVEYSSLSFALFFLAEYSNIILMSCMMTIFFLGGWLSPLDGIPTPPEAFSIFEQIASSKS
SFWFFTKSSIFILFFIWSRASFPRIRYDQLMKLLWKTYLPLSLGLVILTAGILIGFNGVPPPF
>gnl|CDD|164603 MTH00030, ND3, NADH dehydrogenase subunit 3; Provisional
MNPEFKTIFFSTLLGVGIILLLVSISFTLGNSRIGLTKPDSEKSSIYECGFDPFGKIRTPFTIKFVLVGI
LFMIFDIEISFLFPWSIVFNQLNLFSFWIVYTFLIVLAIGLAYEWIKGGLEWD
>gnl|CDD|214407 MTH00032, ND5, NADH dehydrogenase subunit 5; Provisional
MYLLVLLLPFINAFLLGFFGRLIGTIGSGILSTICMGSSTLIALFLAYEVLINDAVVHIELYKWIESEIF
ITHIGLLYDTLSVTMLLVISSISTLVHIYSTSYMSDDPHVPRFLCYLSLFTFLMMVLVTSDNYLQLFIGW
EGVGVCSYLLVAFWTTRIQANKAAIKAIVVNRVGDVGVILGMVLIYKTIGSLDFLTFNGGSVGSGIMDRG
YYGGGAYESPLAPFAIIGILLLIGCIGKSAQLGLHTWLPDAMEGPTPVSALIHAATMVTAGVFLMIRSFP
LFEKAPLTLLIITIFGALTAFFAATVGLVQNDLKKVIAYSTCSQLGYMVLIIGIEGSHNVGLFHLVNHAF
FKALLFLSAGSVIHSTTVDEQDMRKMGGLIHSIPFTYTMMLIGSFSIMGLPYLTGFYSKDLILELTYSGR
NMGIPFGSSLLKIQGDIGIKKDDRGSIGGPEGYPSRGSAFAFWLGTVAALLTAFYSIRLVYITFIISPNS
PKESLISSHINIVDKRVLTVLSLLCFGAIFVGYLIQDILIGDIEHPIVPPLIKVMPTLMGLFGMGLCLWA
QKGTREGELYWGFDPIGPSFLLSIYSFLGGAWQGDHLINKLVAIPLFSFGHWGIYKTLDRGWLELFGPQG
ISTIALRVSQFISNLQSGVISRYALVLLSFTIIFLALWG
>gnl|CDD|133672 MTH00033, CYTB, cytochrome b; Provisional
MRLRKTGLLEPVNDIIDLPTPSNISYWWNFGSLLCLCLGIQILTGVLLAMHYRSDVSLAFSSVAHIVRDV
NYGWILRYVHANGASLFFICVYCHIGRGLYYGGYSRVLTWIVGVLIFFIMMLTAFIGYVLPWGQMSFWAA
TVITNLVSAIPSVGGSIVEWIWGGFSVSNCTLNRFFSLHYLLPFVLVGLVLAHLLTLHEKGSNEPLGLVG
LSDRTAFHVYFTIKDILGFLILFGVFVIIGIEPRIETLLQDPENFIQANPLVTPVHIQPEWYFLFAYAIL
RSIPNKLGGVLALFASILVLLLMPILDRSKIRSLTFNPTGKFFFWFIVGDFIILTWIGSAPAGADPYVLI
GRIATIFYFGYFLVLVPLLGYLSNLFYEYNGTT
>gnl|CDD|177109 MTH00034, CYTB, cytochrome b; Validated
TGPLRKSHPLFKILNSSLIDLPSPSNLSIWWNFGSLLGLCLIIQIITGIFLAMHYTADISLAFSSVSHIC
RDVNYGWLLRNIHANGASLFFICLYFHIGRGLYYGSYVNIETWNIGVILFLLTMLTAFVGYVLPWGQMSF
WAATVITNLVSAVPYIGTDIVQWIWGGFSVDNATLTRFFAFHFLFPFIIAALSIIHLLFLHQTGSNNPTG
LNSNYDKVPFHTYFTTKDLVGFLILFAALSSLALLFPTALNDPENFIPANPLVTPPHIQPEWYFLFAYAI
LRSIPNKLGGVIALVAAILVLFLVPILHTSNNQSSTFRPLSQIAFWLLIATFFILTWIGSQPVEYPFILL
GQVASVLYFSLFLFFFPLISYLENKLIFS
>gnl|CDD|177110 MTH00035, ATP6, ATP synthase F0 subunit 6; Validated
MIINNSIFGQFSPDTILFIPLTLLSSVIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTA
PWAGLLTTVFILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSF
LIPLMVWIETLSLFAQPIALGLRLAANLTAGHLLIFLLSTAIWELSNSPLISIITLIIFFLLFILEIGVA
CIQAYVFTALVHFYLEQNI
>gnl|CDD|214408 MTH00036, ATP8, ATP synthase F0 subunit 8; Validated
MPQLDFTWWLFNFLLAWSLVFIVFTYLLLNNWPSTNASNSSSNTSSSNNNNWLW
>gnl|CDD|177112 MTH00037, COX1, cytochrome c oxidase subunit I; Provisional
MQLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMV
MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAG
GSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLL
TDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAI
GILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTI
GGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIG
VNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSS
SLEWQYSSFPPSHHTFDETPSTVILIK
>gnl|CDD|177113 MTH00038, COX2, cytochrome c oxidase subunit II; Provisional
MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPA
FILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDN
RLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIV
IESVPFNTFENWVSNFLEE
>gnl|CDD|177114 MTH00039, COX3, cytochrome c oxidase subunit III; Validated
MTHQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMH
TLIVINGLRYGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSG
VTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIG
TTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVDVVWLFLYVCIYWWGS
>gnl|CDD|214409 MTH00040, ND1, NADH dehydrogenase subunit 1; Validated
MSVILFLINLLSFIVPVLLAVAFLTLVERKVLGYMQFRKGPNVVGPYGLLQPFADGLKLFIKETLKPSNA
SPYLFFFSPVLFLFLALLLWSLIPVPTPTLNVNLSLLLVLGLSSLSVYALLGSGWASNSKYSLLGAIRAV
AQTISYEISLGLILLSLVIFSGSFSLSSISNSQNGSWLLFPCLPLFYIWFISTLAETNRAPFDLTEGESE
LVSGYNVEYAGGPFALFFIAEYANIIFMNLLSVILFLGGGSPFNEIFPINIIIVGIKTTFLVFLFLWVRA
SYPRFRYDQLMFLTWKNYLPLSIGLLIFYLLLLSLLNILPPNY
>gnl|CDD|177116 MTH00041, ND2, NADH dehydrogenase subunit 2; Validated
MNRNVLIFLITSIILGTIIVISSNHWFLIWLGLELNTLSIIPILSSNFSPRSVEATIKYFLVQAFSAAIL
LNGALIQAWLSGSWSINGPLNTLSSIIITLALALKLGLAPCHFWFPDVLQGLPFLQGLIIATWQKIAPLI
LLISISNLLNSNILILCGILSVLVGGWGGLNQTQTRKILAFSSIAHLGWIIITSAYSPNASIIMFLIYII
INTSIFLIGNNFSLSTLSHLNKLSQLNPISAFLFILSILSLGGLPPLTGFLNKFISLYCLIQNNSILISI
ILIIGSLLSLFFYLRISFNTSLTLFPQHSISLFSWRNSGNITVYGVILSILSSISILGLLLIPLFLSFL
>gnl|CDD|177117 MTH00042, ND3, NADH dehydrogenase subunit 3; Validated
MTNLIFFLLIILILTSLLLLAGHFLPSRSPDLEKSSPYECGFDPLNSARLPFSFRFFLVAILFLLFDLEI
ALLFPLPPATLITNPSTLLPISLIFLIILTIGLVYEWVNGGLEWAE
>gnl|CDD|214410 MTH00043, ND4L, NADH dehydrogenase subunit 4L; Validated
MNIILIIILSSFFLGLLGILINRLHLLSILLCLELLLISLFLNISIWSLNYGNFSNLSFSLLLLTLSACE
ASIGLSLMVLLSRNHNSDLVASLNLLQN
>gnl|CDD|214411 MTH00044, ND4, NADH dehydrogenase subunit 4; Validated
MITLILLSLGIAITSWIVPKNKLWPISISQSSLISLLSLFLLNNHWSSSWHNLSLSLATDSLSSPLIILS
CWLAPLSLLASINHLSNNSPNNQRTFISLIIIILTALIITFSSLELILFYIAFETTLIPTLILITRWGAQ
KERIQAGLYFLFYTLFGSLPLLISLIAIYSSSSSLSIPLSELNWLTSLSSNSSSIWWIFCILAFLVKMPI
YGFHLWLPKAHVEAPVAGSMILAAILLKLGGYGLIRLINLFSLPSANNISFILIVFCCWGALITSIICLR
QTDLKALIAYSSVGHMSLVAAGIFSGTNWGINGALILMIAHGLVSSALFCLANILYERSGTRTLSITRGF
KLITPLLPLWWLIFCAANLGLPPLPNLIGELLIISSIISWSILSFPIIGLATVFGAIYSLLIYQLTNSGS
FPSWISNVSPISSREHLLIFLHLLPLILIIINPNIILI
>gnl|CDD|177120 MTH00045, ND6, NADH dehydrogenase subunit 6; Validated
MVFYLFLILMLFGSTLVFYSLSPYYSALGLVLVSLSGCLLLSLLGLSFLALLLLLIYMGGMLVVFVYSSA
LSAERYPSVSNLGEVLVLSLLLSLWVFISFDNFLELSNNNWSLVSLSDLVGSSELYNSGGLYLLLGGFIL
LVALVVALVISFGHEYSSLRAL
>gnl|CDD|177121 MTH00046, CYTB, cytochrome b; Validated
MISLIRRNLIDLPTNYSLNYYWCSGFVLSVFMVIQVLTGVLLSLLYVADSLCSFFCVMSLSNDSFFTWCV
RYWHIWGVNVLFILLFIHMGRALYYSSYSKKGVWNVGFILYLLVMVEAFLGYILPWHQMSYWAATVLTSI
VDSVPIVGSLVYKYIVGGFSVTGVTLVRVFSVHICLGFVILGLMVVHLFYLHKSGSSNPLFSSNGYSDVV
YFHSYFTVKDLFLFMVVCSLLVFWLFVSPDLVLDIEAYLEADPLVTPVSIKPEWYFLAFYAMLRSINSKI
GGLVLVLSFLFFLWVPTFNGSSVYSVWRQVNFWLIVSLFFSLSYLGGCHPEYPYLLISQLFSVLMVLLLF
IFKLF
>gnl|CDD|214412 MTH00047, COX2, cytochrome c oxidase subunit II; Provisional
MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSGNGSVNFGSENQVLELLWTVVPTLLVLVLCFLNLN
FITSDLDCFSSETIKVIGHQWYWSYEYSFGGSYDSFMTDDIFGVDKPLRLVYGVPYHLLVTSSDVIHSFS
VPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS
>gnl|CDD|177123 MTH00048, COX1, cytochrome c oxidase subunit I; Provisional
MNSLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFF
LMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAGVGWTFYPPLSSSLFSSSW
GVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFD
RNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVC
LGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVWWVVSFIVLFTIG
GVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGF
NLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLGLWGSSSC
VVNVLMSPVPYHNDYFYVFAV
>gnl|CDD|177124 MTH00049, COX3, cytochrome c oxidase subunit III; Validated
MSWFPLFNASFVGFGLVGLFLWKPFILLVFLILWVLLIVIFVSDGLVQVKHHYESAFWLFILSEVIIFGS
LLVCCLWFDDWSYISLSSSLEIPFVGCFLLLGSSITVTAYHHLLGWKYCDLFLYLTILLGLLFVVLQVFE
FEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLSTLLLVGSSSFGVYRSTVLTWYWHFVDYIWLLVYL
IVYVC
>gnl|CDD|177125 MTH00050, ATP6, ATP synthase F0 subunit 6; Validated
MFVNDFSSLFSLIYKLILGGSVSYYYSVVLFIVLFLFLLYRLPYIYSPFLFVVFLFVVVFPLFISLFLSR
VFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALGNLCFISYWWFL
VLFFLFFYEVFVALVHWFIVSSILSFSVDH
>gnl|CDD|177126 MTH00051, COX2, cytochrome c oxidase subunit II; Provisional
KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLI
PAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLL
EVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSF
MPIVIEGVSLDKYINWVATQSEEI
>gnl|CDD|164623 MTH00052, COX3, cytochrome c oxidase subunit III; Provisional
MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQG
HHTLIVKQGLKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLS
SGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVL
IGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFVDVVWLFLFIFMYWWGS
>gnl|CDD|164624 MTH00053, CYTB, cytochrome b; Provisional
MTKTIRKENPVISLVNSMFIDLPSPSNISYLWNFGSLLGFCLIIQIITGIFLAMHYCADVNLAFSSVAHI
TRDVNYGFILRYLHANGASMFFLCVYFHIGRGIYYGSYTKIIVWNVGVLIFLLMILTAFIGYVLPWGQMS
FWAATVITNLLSAIPYVGDDIVRWVWGGFSVSNATLNRFYSLHYLLPFILAGLALVHLIALHEDGSNNPI
GVRSDIDKIPFHYYYVLKDLYGAVILLIILSIIVFLFPYSLGDAENFKQANPLVTPVHIKPEWYFLFAYA
ILRSIPNKLGGVVALVFSILVLFFLPYLHKSRFRGLSFRPLSKILFWFLVGDFFLLTWIGGQPVEEPYIL
IGQIASIFYFAYFLILMPLAGYLENKLLKLV
>gnl|CDD|177127 MTH00054, ND1, NADH dehydrogenase subunit 1; Provisional
MGIIIIKILAILVPLLISIAYLTLAERKVLGYIQCRKGPNVVGVYGLLQPLADGLKLFTKEIIIPNHANI
FIYIMAPILSLTLAFIAWGVIPYGEGVVLSDLGIGILYLFAVSSISVYAVLMSGWSSNSKYAFLGAIRAA
AQMISYEVSIGLIIISVVLCVGSLNLTEIVLAQKNIWFIFPLFPAAIMFFVSALAETNRVPFDLTEGESE
LVSGFNVEYSSMSFALFFLAEYCHIILMSTFGVILFLGGWLVISGPTSYFSNFVWFGIKIALIIFLFIWI
RASYPRIRYDQLMALLWKSYLPLSLAFVVLVSGILIGFNALPPF
>gnl|CDD|177128 MTH00055, ND3, NADH dehydrogenase subunit 3; Provisional
MSMEFLGIFILLLFSIGLSTVISGASYIVGVKQPDSEKVSVYECGFDPFESSRIPFSVRFFLVGILFLIF
DLEISFLFPWCVVYNQIGLFGFWVMYLFLIILTIGLIYEWVKGGLEWE
>gnl|CDD|177129 MTH00057, ND6, NADH dehydrogenase subunit 6; Provisional
MEGLFYLFALGVIISGIMVISALNPVHSVLWLIVAFTSASALFILLEVEFIALIFLIVYVGAIAILFLFV
IMMLNLTDLEGGGDMSNYLPAGFIIGVVFLFEVSSGISLLSSGTKIGQWDFPNWIEKESNIEVLGRVLYT
DYYYLFILASFILLVAMIGAIVLTHDLIIEIKRQDIFIQTSRQLWQ
>gnl|CDD|177130 MTH00058, ND1, NADH dehydrogenase subunit 1; Provisional
IFGLVSGLEGLLIILLLVAFFILGERKILGYIQLRKGPNKVGIVGLLQSFADLLKLVVKFKVYGFQSRSW
FSLFGVFLLVLLVVFYCFIYGSYYSGSYSSLSLLWFLVVTSFSSYSLLCVGWGSYNKYSLLSSIRSAFGS
VSFEACFMCIVIFCGLCYGSYSLVDFYYSGWLSVLLFPLIYILWLVCILCETNRTPFDYGESESELVSGF
NTEYSGIYFTCLFACEYLIIFIFSWLGSVLFFGGGFVSIMLLFHLLFFMWARATLPRVRYDYFVNFFWEY
CLVLLILSLFVIV
>gnl|CDD|177131 MTH00059, ND2, NADH dehydrogenase subunit 2; Provisional
RFRYIDVVIFSLILSLFFCLLCLVSDSLLGFWVFLELCGLSLIPCFFLSSNSNVLNFYSSLLSYIVMSGL
SSSLLVSGLLFSDLYFFIFFGFVVKFGLFPFMFWVYRVFSNSSWVVIWLISVVMKFPVLFFCFFLQGGGL
SLVFVDCFLTILFCGFLFWFYSLNWEYVWCHISLSSSATLVVACFCLSIDLCFFLYLYYFFWSSGVIIYF
SSLSDSNDLKGYYFFGFCFLLLSTPVSFPLFYKLSVSIGIIYSSIYVLLVWVIYSFSEQFYLFKLLVSYF
VSNVFNVWV
>gnl|CDD|177132 MTH00060, ND3, NADH dehydrogenase subunit 3; Provisional
MLVLLFVFFVFFLLFLVIYFFHSGLWNNKIYSGGFSWVSSFECGFFSSGLSENCFSFTYFFLLVFFVIFD
LEISLLLNMPFQGLLFYNFWYYYFFLLLLFLGFVVELFSGYVRWVY
>gnl|CDD|177133 MTH00061, ND4L, NADH dehydrogenase subunit 4L; Provisional
MVSLFLLGFGVILISLFLSGSRLLNYLIVLENFNVLLLLFCLLLSSGDSHMIFIALMVIFTVEVILGLVV
LTRVWECSSLLELVGF
>gnl|CDD|214413 MTH00062, ND4, NADH dehydrogenase subunit 4; Provisional
FYFFSVGFFLGFLLLLLFCLLYSSGVGCCILVVNNVFNGLFIFDSLSFYLILLVLFLGLYSQVMFYNLLS
GVSRFFLFLSLIFSILCFCVNNSLLFWFFYELSIIPLLYLLFSESPYSERYLASWYFLGYLLLTSLPLLL
CLLYLSLVNGSFNFSDWGSDDSVSLIVYYVLSFMFITKVPLFPFHTWLPIVHAEASSPVSIFLSGYIMKL
GLLGVYRFCGFIFSGSFLGYLFLCCLFSVFFLITACSELDGKRWLAFLSLSHILVPVLGLFVGDWSSINL
SFFYCLGHGLSAGLVFLLLWCFYEVSGSRNWVLLKSGINGSLVLRVIVVFSFLSLCSFPPTIQFFCEVFL
VSSSFGVLVYLLFWCFYLFFGGLVPLILLGHLLIRSESYESINVSNYSYLFFLIFLVFWCYLGFLVL
>gnl|CDD|214414 MTH00063, ND5, NADH dehydrogenase subunit 5; Provisional
SVLLVSLLLCLLIFFLFLVGVSSSVSLNFLSFGGYSWLINFDFDYVTFGVLLMLLICFYYSLLYTFHYFG
GSYASFLLNKLIVLFVLVMGILVLTGDFLSTLIFWEYLGVVSFFLILFYDNFLSLRASVVTLVSSRFGDV
CLFLLIGLSCWGGSGSFLCCLFFFLIVFTKSASFPFISWLLEAMRAPTPVSSLVHSSTLVAAGVWFVMRY
DYLLGFSWLSIFFSVLLLLTIFITGVSSLFFSDLKKIVALSTCNNISWCVLYLIYGDVILSLFQLVSHGV
SKCLLFMLVGDVMSGSGGSQSSNCVYSSILYGSWNLFYLFLLVLGLSGVPFIGVFFSKHFLLSSFSSVVF
NVSLLLVVILCVFLSYLYSFRLCLILFGVKSSLSSGVRFLFFNSGLMVFLWLFINYYVFLLLDEVVYLGV
FISLVLLLVQLLGLLVGVLFYDSNLFSNWSSSLFGCDNLVELFYELFYSILDLVSLFFFRWEIYLIELLC
GVGSSSSLLYSWFSLNLLLLSLFFLLIYLLII
>gnl|CDD|177136 MTH00064, ND6, NADH dehydrogenase subunit 6; Provisional
MLLEVLFSLYFIVLVLFSFSSHPVYYCVLLVVNSLISSLICYLVYGFSWYSLLFCLVYVGGVYILFIFVS
VFSPNSSFVSYSNLGELGVFFFFFFGLLLCVLVFYSLVNVEFSFYLCTSSEGVFYLFLCLVLMFGFIVLS
FIVSSKTSYYR
>gnl|CDD|214415 MTH00065, ND6, NADH dehydrogenase subunit 6; Provisional
MMYLGFLGMLGLVVGLVAVASNPSPYFAALGLVLGAVCGCLVLVELGVSFLSLVLFLIYLGGMLVVFAYS
AALAAEPYPEAWGSWSVLVYVLFYLLLLIVGYILFGCNFSLEFLFTNYDTEFSVVGYDWGGVGLMYSSGG
WFLMISGWVLLLTLFVVLEVTRGLSRGSLRAV
>gnl|CDD|214416 MTH00066, ND5, NADH dehydrogenase subunit 5; Provisional
MNLMLIFNSSMILSLLLLILPLLLPKSNNFHTNVKTSVKTAFFISLIPLMIFINQGLESITTSFHWMNIF
NFNINSSFKFDQYSIIFLPIALFVTWSILEFAIWYMHSDPKINRFFKYLLIFLIAMMILVTANNLFQLFI
GWEGVGIMSFLLIGWWHARADANTAALQAVLYNRVGDIGLILSMAWLAMNTNSWELQQIFLLNDNSTLPL
LGLILAAAGKSAQFGLHPWLPAAMEGPTPVSALLHSSTMVVAGIFLLIRFHPLLENNQTALTICLCLGAL
TTLFTAACALTQNDIKKIVAFSTSSQLGLMMVTIGLNQPQLAFFHICTHAFFKAMLFLCSGSIIHSLNDE
QDIRKMGGLQKALPITTSCLTIGSLALTGTPFLAGFFSKDAIIEAMNTSNLNSWALILTLIATSFTAVYS
FRIIYFSSMKFPRSLPLSPINENNPLIINPIKRLAWGSIIAGLLIIFNILPMKPQILTMPTFMKLAALLV
TLLGLLIALDLAKITSKTTPKTKMHSFSNLLAFFPTIIHRLSPKTNLNSGQNIATHLTDMTWYEKSGPKG
LTNQQLPPIKTITNIQTGLIKTYLTLFLITLLLMLILL
>gnl|CDD|177139 MTH00067, ND4L, NADH dehydrogenase subunit 4L; Provisional
MSPTYFTFYSAFLLGLMGLAFHRTHLLSALLCLEGMMLSLFIALSLWSTQFESLSYFSLPMFMLTFSACE
ASTGLALMVATTRTHGTDHLKNLNLLQC
>gnl|CDD|214417 MTH00068, ND4, NADH dehydrogenase subunit 4; Provisional
MLKIIIPTLMLLPTTWLSPKKWLWTLTTTNSLIIAFLSLMWFNLPSETMNFTNKYFGIDQISSPLLILTC
WLLPLMILASQNHLKNEPINRQRTYISMLIILQLTLILAFSATELILFYIFFEATLIPTLIIITRWGNQE
ERLNAGTYFLFYTLAGSLPLLIALLILQNSLGSLSLILLELMSPMQLMTYTNKIWWLACLLAFMVKMPLY
GLHLWLPKAHVEAPIAGSMILAAVLLKLGGYGILRISILLTPLSKELSYPFIILALWGVLMTSLICLRQT
DLKSLIAYSSVSHMGLVIAAALIQTPWSFSGAIILMISHGLTSSALFCLANTNYERTHSRTLLLLRGAQT
ILPLMATWWLLSNLSNMALPPSPNLWGELTIMVSLFNWSNWTILITGLGTLITAAYTLYMFLMTQRGPLP
NHLKTLFPTYTREHLLLALHILPMLLLILKPELISGMF
>gnl|CDD|177141 MTH00069, ND3, NADH dehydrogenase subunit 3; Provisional
LIMLMLLISTILSLILITISFWLPLNNPDSEKLSPYECGFDPLGSARLPFSIRFFLVAILFLLFDLEIAL
LLPTPWASQLNTPTNTLFWSTLILILLTLGLIYEWIQGGLEWAE
>gnl|CDD|177142 MTH00070, ND2, NADH dehydrogenase subunit 2; Provisional
MSPYALSILLSSLALGTMITLSSNHWFLAWMGLEINTLAIIPLMTKTHHPRATEAATKYFLTQASASALI
LFSSTINAWFTGEWTIMNMQTPLPTIMLTIALMMKLGIAPFHFWLPEVLQGLDLTTGLILSTWQKLAPMA
LLIQISHLLNSNLLIIMGLLSTLIGGWGGLNQTQLRKIMAYSSIAHLGWMIIILTFSPHLTLLNLLIYLI
MTSSMFLMLMNLNSTNINKLSSSWSKNPTLTSMMMLTLLSLGGLPPTTGFIPKWLILQELTKQNLTTLAT
LMALSALLSLFFYLRLSYAMSLTTSPNTSNSKLYWRFKNKTNNLLSLTIILSLMLLPITPTILNLF
>gnl|CDD|214418 MTH00071, ND1, NADH dehydrogenase subunit 1; Provisional
MMTLISLIINPLLYIIPVLLAVAFLTLVERKVLGYMQLRKGPNIVGPMGLLQPIADGLKLFIKEPIRPST
SSQILFILMPTMALTLALIIWTPLPMPNNLSNLNLGILFILALSSLAVYSILGSGWASNSKYALIGALRA
VAQTISYEVTLGLILLCLILLTGGFSLMNFNTTQEFMWLIIPAWPMAAMWFISTLAETNRAPFDLTEGES
ELVSGFNVEYAGGPFALFFLAEYANILMMNTLSTILFLGSTYNHLQPELSTMNLMIKASILSMLFLWVRA
SYPRFRYDQLMHLVWKNFLPITLAMTIFHISLPISTLGIPPM
>gnl|CDD|164642 MTH00072, ATP8, ATP synthase F0 subunit 8; Provisional
MPQLNPGPWFAIFLMSWLIFLLILPFKISNHKNLNEPTSQNKKNKPESWNWPWT
>gnl|CDD|177144 MTH00073, ATP6, ATP synthase F0 subunit 6; Provisional
MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWA
LILTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIP
ILIIIETISLFIRPLALGVRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMI
QAYVFVLLLSLYLQENV
>gnl|CDD|177145 MTH00074, CYTB, cytochrome b; Provisional
MAHPIRKTHPLLKIINNSFIDLPTPSNLSSLWNFGSLLGVCLIAQIITGLFLAMHYTADTSSAFSSVAHI
CRDVNYGWLMRNIHANGASFFFICIYLHIGRGLYYGSYMYKETWNIGVILLFLVMATAFVGYVLPWGQMS
FWGATVITNLLSAIPYMGDTLVQWIWGGFSVDKATLTRFFAFHFLLPFLIAGASIIHLLFLHETGSNNPT
GLNSNPDKVPFHPYFSYKDLLGFLIMLTALALLSLFSPNLLGDPDNFTPANPLVTPPHIQPEWYFLFAYA
ILRSIPNKLGGVLALLASILILMLIPMLHTSKQRSLMFRPLTQILFWLLVANTLILTWIGGQPVEDPFIE
IGQAASILYFLLFIIIIPLTGWLENKLLKW
>gnl|CDD|177146 MTH00075, COX3, cytochrome c oxidase subunit III; Provisional
MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGH
HTPPVQKGLRYGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLAS
GVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVII
GSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS
>gnl|CDD|164646 MTH00076, COX2, cytochrome c oxidase subunit II; Provisional
MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPA
IILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDN
RMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIV
VEATPLNNFLNWSSSMLE
>gnl|CDD|214419 MTH00077, COX1, cytochrome c oxidase subunit I; Provisional
MMITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMV
MPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAG
ASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLL
TDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSI
GLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTV
GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIG
VNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTST
NIEWLHGCPPPYHTFEEPSFVQTR
>gnl|CDD|177148 MTH00079, COX1, cytochrome c oxidase subunit I; Provisional
QGGLSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFM
VMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPG
SSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLL
TDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSI
GLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTI
GGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVG
VNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINS
SPEYSLSSYVFGHSYQSE
>gnl|CDD|177149 MTH00080, COX2, cytochrome c oxidase subunit II; Provisional
NYFQGYNLNFSNSLFSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVF
PVLILLMQMVPSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLE
VDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFM
PIAVEVTLLDNFKEWCKLLLD
>gnl|CDD|177150 MTH00083, COX3, cytochrome c oxidase subunit III; Provisional
MFHNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEGLSGYHNFF
VMDGFKFGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSV
TWSHHSLCLSNKSCTNSLLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFL
LFNLLRLLKSHFNYNHHLGLEFAILYWHFVDVVWLFLFVFVYWWSY
>gnl|CDD|177151 MTH00086, CYTB, cytochrome b; Provisional
NFVNSLVVTLPSSKSLSYWWNFGSMLGMVLVFQILTGTFLAFYYTADSSMAFSSVQYIMYEVNFGWLFRI
FHFNGASLFFIFLYLHIFKGLFMMSYRLKKVWISGLTIYLLVMMEAFMGYVLVWAQMSFWAAVVITSLLS
VIPIWGPSIVMWIWGGFGVSSATLKFFFVLHFLLPWGLLVLVLFHLIFLHSTGSTSSLYCHGDYDKICFG
PEYWNKDAYNIIFWLVFIIFSLFYPFNLGDPEMFIEADPMMSPVHIVPEWYFLFAYAILRAIPNKVLGVI
ALLMSIVVFYFFIFVNNYTSCLNKLNKFLVFSFIVVNVILSWLGQCLVEYPFLFLSQIFSFIYFFLILLM
LFLFY
>gnl|CDD|177152 MTH00087, ATP6, ATP synthase F0 subunit 6; Provisional
MNQVFFLDVFMFVFLLQYLLYFKESMLNVLVKKFFGLLIIVFSYSNKLPLSSVISFFTFIVLLLFCFGGL
FPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFSVYLSKGSDSFLKTFSMLFVEIVSELSRPLALTL
RLTVNLMVGHLISSLLNFLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE
>gnl|CDD|177153 MTH00090, ND1, NADH dehydrogenase subunit 1; Provisional
MLLLMMIFILQAIAFITLYERHLLGSSQNRLGPNKVSFMGVLQALLDGVKLLKKEQMLPLNSSDLSFLLV
PGVSFVVMYLEWFVLPYFFDFLSFEYSLLFFLCLIGFSVYTTLISGIVSKSKYGFLGALRASSQSISYEI
AFSLYLLSIMLHNNSFSFVSSFSLSLFVIYLPFLIMIIAELNRAPFDFSEGESELVSGYNVEYSSVAFVL
LFLSEYGSLIFFSVLTSVLFFKFSFLMLFLIFSLLIFIRSSYPRFRYDMMMSMFWFKFLPLSLIFLGFFV
VLFI
>gnl|CDD|177154 MTH00091, ND2, NADH dehydrogenase subunit 2; Provisional
LFLSLLNFMSLNIFVWWSVFLLMTLLFVFLNKGMGSYSSLFNYFVLQESLGLLFLLFSFGYFQFLILMMK
IGVAPFHFWIFSVTNGLFGWNLMWFLTFQKLPFLLVLLQFFSKNFFFLLLFGLLICFFQMFLLKSYKNLL
ILSSTESFNWLILSFFFSFFNVFFLFFYYFLLMLFLIPKFNNVNKLNFVSWETLLVFMNLPFSVTFFVKI
FSLSEILKVLGFFLLFLLFLMFLSVLSLSFWLVNLSTKLFLMLFKYNKGFFFFFLPLMLLSLI
>gnl|CDD|177155 MTH00092, ND3, NADH dehydrogenase subunit 3; Provisional
MLVLIFVFLFTLLLLMLLYLLNFFLSVKKFDLLKVSSFECGFESVGKIQNSFSIHFFKIMLMFVIFDLEI
VMFLGLLVSDFSSLISFFMLMIFIFFGFYMEWWYGKLIWVI
>gnl|CDD|177156 MTH00093, ND4L, NADH dehydrogenase subunit 4L; Provisional
MIFLFISLLMLFFKYKRLIFILISLEFLMMSLFIYFMYFLNEMMFFYFMCFSVISSVLGMVVMVGNLKFY
GSDKCLF
>gnl|CDD|177157 MTH00094, ND4, NADH dehydrogenase subunit 4; Provisional
LSLLFFFSPFLFFLFLMFFSFLMFNNYSWSGLFFFFDSFVFVLLIFMMVFILGLVLLSEKNFNLLILSNL
LILICLLFFVSSNMLMLYMFFELSMFPILIMILGYGSQIEKINSSYYLLFYAAFFSFPFLFVYLKNFFFF
SLCYFDFFLSWEMFFILSLSFMMKFPVYFLHLWLPKAHVEAPTTASMLLAGLLLKLGTAGFLRILGSLNF
VYNNFWIIFSLLGMILSSFCCVFQSDSKSLAAYSSVTHMSFLLLSLVYMSMSGKLSGLMMMLAHGYTSTL
MFYLIGEFYHISKSRLIYFMNSFFSSSMFFGLIFSLVFLSNSGVPPSLSFFSEFLIISNSFMKNKFSFFF
IFFYFLVSFYYSLFLIVSSFMGKKFSNFNNFNVGLSLPLVFMMFNMFWLSLFY
>gnl|CDD|177158 MTH00095, ND5, NADH dehydrogenase subunit 5; Provisional
MNILIFLILFFFFFLLLFILFLPFMKLNLFFLEWDFLSLKFNFYFNSLLFSLILLLVTLSVLVFSSYYMN
GELNFNYFYFVLLIFVGSMFMLNFSNSVFTMLLSWDLLGISSFFLVLFYNNWDSNSGAMNTALTNRIGDF
FIFLFFSGFIFSSYYFFSFSFFSSSMILMLLLTSFTKSAQFPFSSWLPKAMSAPTPVSSLVHSSTLVTAG
LILLMNFSYLILNMNVMKIMLLIGLFTMFFSSLSALVEEDMKKVVALSTLSQMGFSMLTFGSGLSFVSFI
HLLSHALFKSCLFMQVGYLIHSNFGQQDGRNYSNNGNLPMFIQLQLLVTLFCLCGLMFTSGMVSKELILE
LFFFNNYMIFFSLMFFFSVFLTFGYSYRLWKSFFLSFSKVVNVYSSSVLMNFLSLMLVFFSVFFLWWLNF
NLLNLPSLFLYLDFYVPLFYLFMIMLFSFFFFKLLFKELKYKFFVDYFAKNVIYKLKNLKFFDLFLNKFG
YKGFNFFSSFSFFFFSYMKSFKYNSLLILLFLIFLFL
>gnl|CDD|177159 MTH00097, ND6, NADH dehydrogenase subunit 6; Provisional
LILSMLFWMPLLSFSGHVWFSYFICLLFLSGIFVILVYFSSLSSFKLKKPYLVFFSLFLSMFFFFFFYFF
KVYFFSNLSLNVFELYYNIFWLIVFFILFVLLFFMNFISYFLNFSGALRKV
>gnl|CDD|177160 MTH00098, COX2, cytochrome c oxidase subunit II; Validated
MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPA
IILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDN
RVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIV
LELVPLKYFEKWSASML
>gnl|CDD|177161 MTH00099, COX3, cytochrome c oxidase subunit III; Validated
MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGH
HTPIVQKGLRYGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLAS
GVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVII
GSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS
>gnl|CDD|177162 MTH00100, CYTB, cytochrome b; Provisional
MTNIRKTHPLMKIINHSFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTTTAFSSVAHIC
RDVNYGWIIRYLHANGASMFFICLFLHVGRGLYYGSYLFLETWNIGIILLFTVMATAFMGYVLPWGQMSF
WGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALAMVHLLFLHETGSNNPSG
IPSDSDKIPFHPYYTIKDILGLLLLILTLMLLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAI
LRSIPNKLGGVLALLLSILILAIIPLLHTSKQRSMMFRPLSQCLFWLLVADLLTLTWIGGQPVEHPFIII
GQLASILYFLIILILMPIASLIENNLLKW
>gnl|CDD|177163 MTH00101, ATP6, ATP synthase F0 subunit 6; Validated
MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSL
MLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPM
LVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQ
AYVFTLLVSLYLHDNT
>gnl|CDD|214420 MTH00102, ATP8, ATP synthase F0 subunit 8; Validated
MPQLDTSTWFITILSMLLTLFIIFQLKISKHNYPLNPEPKSLKTKKQNTPWEKKWTKIYLPLSLPLQ
>gnl|CDD|177165 MTH00103, COX1, cytochrome c oxidase subunit I; Validated
MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMV
MPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAG
ASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLL
TDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSI
GFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTV
GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVG
VNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTT
NLEWLHGCPPPYHTFEEPTYVKL
>gnl|CDD|177166 MTH00104, ND1, NADH dehydrogenase subunit 1; Provisional
MFMINILLLIIPILLAVAFLTLVERKVLGYMQLRKGPNIVGPYGLLQPFADAMKLFTKEPLRPLTSSTTM
FIIAPILALTLALTMWIPLPMPYPLINMNLGVLFILAMSSLAVYSILWSGWASNSKYALIGALRAVAQTI
SYEVTLAIILLSVLLMNGSFTLSTLITTQEHLWLIFPSWPLAMMWFISTLAETNRAPFDLTEGESELVSG
FNVEYAAGPFALFFMAEYANIIMMNALTTILFLGAFHNPYMPELYTTNFTIKTLLLTILFLWIRASYPRF
RYDQLMHLLWKNFLPLTLALCMWHISLPIMTASIPPQT
>gnl|CDD|177167 MTH00105, ND2, NADH dehydrogenase subunit 2; Provisional
MNPLILIIIYLTLFLGTMITMISSHWLLAWIGLEMNMLAIIPILMKKHNPRSTEAATKYFLTQATASMLL
MMAIIINLMYSGQWTITKLTNPTASTLMTIALAMKLGLAPFHFWVPEVTQGIPLSSGMILLTWQKLAPLS
ILYQISPSINPNLLLTLAILSILIGGWGGLNQTQLRKILAYSSIAHMGWMTAILPYNPTLTLLNLLIYII
MTLTMFMLLMLNSSTTTLSLSHTWNKTPLMTSLILLTLLSLGGLPPLTGFMPKWMIIQELTKNNNIILPT
LMAITALLNLYFYMRLIYSTSLTMFPSTNNMKMKWQFENTKPMTLLPTLIILSTMLLPLTPMLSILE
>gnl|CDD|177168 MTH00106, ND3, NADH dehydrogenase subunit 3; Provisional
MNLMLTLLTNTLLASLLVLIAFWLPQLNIYSEKASPYECGFDPMGSARLPFSMKFFLVAITFLLFDLEIA
LLLPLPWASQTNNLNTMLTMALLLISLLALSLAYEWTQKGLEWTE
>gnl|CDD|177169 MTH00107, ND4L, NADH dehydrogenase subunit 4L; Provisional
MSLIYMNIMLAFTISLLGLLMYRSHLMSSLLCLEGMMLSLFIMATLTILNTHFTLASMMPIILLVFAACE
AAVGLALLVMVSNTYGTDYVQNLNLLQC
>gnl|CDD|177170 MTH00108, ND5, NADH dehydrogenase subunit 5; Provisional
MNLFTSSTLLTLLILTLPIIMTLTNPYKTNNYPLYVKTTISYAFIISLIPTMMFIHSGQEMIISNWHWMT
IQTLKLSLSFKLDYFSMIFIPVALFVTWSIMEFSMWYMHSDPNINRFFKYLLLFLITMLILVTANNLFQL
FIGWEGVGIMSFLLIGWWYGRTDANTAALQAILYNRIGDIGFILAMAWFLLNLNSWDLQQIFMLNPNNSN
LPLMGLLLAATGKSAQFGLHPWLPSAMEGPTPVSALLHSSTMVVAGVFLLIRFHPLMENNKTIQTLTLCL
GAITTLFTAICALTQNDIKKIVAFSTSSQLGLMMVTIGINQPHLAFLHICTHAFFKAMLFMCSGSIIHNL
NDEQDIRKMGGLFKTLPFTSTALIIGSLALTGMPFLTGFYSKDLIIEAANTSYTNAWALLITLIATSLTA
AYSTRIIFFALLGQPRFPPLITINENNPLLINPIKRLLLGSIFAGFLISNNIPPTTIPQMTMPLYLKLTA
LAVTILGFILALELNLLTNNLKFKYPSNTFKFSNMLGYFPTIMHRLPPYMNLTMSQKLASMLLDLIWLEK
ILPKTISLIQMKASTTISNQKGLIKLYFLSFLITLTLSLLLF
>gnl|CDD|214421 MTH00109, ND6, NADH dehydrogenase subunit 6; Provisional
MMMYIVFILSVLFVLGFVGFSSKPSPIYGGLGLIVSGGVGCGIVLSFGGSFLGLMVFLIYLGGMLVVFGY
TTAMATEEYPETWVSNKVVLGALLLGLLMELLLVLYVLKDDEVEVVFNFNGLGDWVIYDTGGSGFFSEDA
MGVAALYSYGTWLVVVTGWSLFIGVFVIIEITRGN
>gnl|CDD|177172 MTH00110, ND4, NADH dehydrogenase subunit 4; Provisional
MLKIIIPTIMLIPLTWLSKNNMIWINTTTYSLLISLISLLLLNQPNDNSLNFSLLFFSDSLSTPLLILTT
WLLPLMLMASQHHLSKEPLTRKKLYITMLILLQLFLIMTFTATELIMFYILFEATLIPTLIIITRWGNQT
ERLNAGLYFLFYTLVGSLPLLVALLYIQNNLGSLNFLLLQLWAQPLPNSWSNNLLWLACMMAFMVKMPLY
GLHLWLPKAHVEAPIAGSMVLAAILLKLGGYGMMRITIILNPLTEFMAYPFLMLSLWGMIMTSSICLRQT
DLKSLIAYSSVSHMALVIVAILIQTPWSFMGATALMIAHGLTSSMLFCLANSNYERIHSRTMILARGLQT
LLPLMATWWLLASLTNLALPPTINLIGELFVIMSSFSWSNITIILMGLNMLITALYSLYMLITTQRGKLT
HHINNIKPSFTRENTLMALHLLPLLLLSLNPKIILGPTY
>gnl|CDD|214422 MTH00111, ND1, NADH dehydrogenase subunit 1; Provisional
MPTLLLNLINPLLYIIPILIAVAFLTLLERKILGYMQLRKGPNIVGPFGLLQPIADGVKLFIKEPIRPST
SSPILFTLTPILALLLALTIWTPLPMPFPLADLNLGLLFLLAMSSMAVYSILWSGWASNSKYALMGALRA
VAQTISYEVTLGIILLSLILLSGGYTLQTLATTQEPLWLIFSSWPLAMMWYISTLAETNRAPFDLTEGES
ELVSGFNVEYAAGPFALFFLAEYANILLMNTLTTILFLNPSTLNLPPELFTINLMTKTLLLTSGFLWIRA
SYPRFRYDQLMHLLWKQFLPLTLALCLWHTSMPISLAGLPPQL
>gnl|CDD|214423 MTH00112, ND2, NADH dehydrogenase subunit 2; Provisional
MNPHAKLIITTSLILGTIITISSNHWLMAWTGLEINTLAIIPLISKPHHPRATEAATKYFLTQAAASALI
LFSSTTNAWNTGQWDITQLTNPTSCTLLTLALAMKLGLAPFHFWLPEVLQGSTTTTALILSTWQKLAPLT
LLLMTSNSLNPTLLLTLAILSTLIGGWGGLNQTQLRKIMAFSSIAHLGWMIAIITYSPKLTLLTFYIYIL
MTTPMFLTLNTTSTKTLKDMMTSWTKSPTLNTTLMLTLLSLAGLPPLTGFMPKWLILQELTKQNMTPTAT
IMAMLSLLSLFFYLRLTYISTITLPPNTTNMMMKWRTKPKKNTLTATLTTLSTLLLPLSPMILTII
>gnl|CDD|177175 MTH00113, ND3, NADH dehydrogenase subunit 3; Provisional
MNLISMLTISLALSTILTTLNFWLTQTKPDNEKLSPYECGFDPLGSARLPFSIRFFLVAILFLLFDLEIA
LLLPLPWAINLTTPTTTLTWATIILTLLTLGLIYEWLQGGLEWA
>gnl|CDD|214424 MTH00115, ND6, NADH dehydrogenase subunit 6; Provisional
MMYFVFLLGVCFVLGVVGVASNPSPYYGVVSLVLASVFGCGVLVSLGGSFVSLVLFLVYLGGMLVVFAYS
VSLAADPYPEAWGDWGVVGYVVGFVLVVVVVGVVVGGLWGMEGVGVVTVDSGGLFVVRLDFSGVSLFYSS
GGGGLLVCGWGLLLTLFVVLELVRGLSRGALRAF
>gnl|CDD|177177 MTH00116, COX1, cytochrome c oxidase subunit I; Provisional
MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMV
MPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAG
ASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLL
TDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSI
GFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTI
GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTG
VNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTT
NIEWIHGCPPPYHTFEEPAFVQVQE
>gnl|CDD|177178 MTH00117, COX2, cytochrome c oxidase subunit II; Provisional
MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPA
IVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDH
RMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIV
VESVPLKHFENWSSLLS
>gnl|CDD|177179 MTH00118, COX3, cytochrome c oxidase subunit III; Provisional
MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGH
HTPTVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLAS
GVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVII
GSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS
>gnl|CDD|214425 MTH00119, CYTB, cytochrome b; Provisional
MAPNLRKSHPLLKIINNSLIDLPTPSNISAWWNFGSLLGLCLITQILTGLFLAMHYTADISLAFSSVAHI
CRDVQYGWLIRNLHANGASMFFICIYLHIGRGLYYGSYLYKETWNTGVILLLLLMATAFVGYVLPWGQMS
FWGATVITNLLSAIPYIGQTLVEWIWGGFSVDNPTLTRFFALHFLLPFLIAGLTLIHLLFLHETGSNNPL
GLNSNTDKIPFHPYFSYKDLLGLTLMLTLLLTLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYA
ILRSIPNKLGGVLALAASILILFLMPFLHTSKQRSMTFRPLSQLLFWTLVANLLILTWIGSQPVEHPFII
IGQLASILYFTILLILFPLLGALENKMLNY
>gnl|CDD|177181 MTH00120, ATP6, ATP synthase F0 subunit 6; Provisional
MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWA
LILTSLMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIP
ALILIETISLLIRPLALGVRLTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMI
QAYVFVLLLSLYLQENT
>gnl|CDD|214426 MTH00123, ATP8, ATP synthase F0 subunit 8; Provisional
MPQLNPAPWFLIMLLTWLTLILIIQPKILSFTPTNNPTKTNTTTNTTPWTWPWT
>gnl|CDD|214427 MTH00124, ND4, NADH dehydrogenase subunit 4; Provisional
MLKIILPTIMLIPTTLLSKPKFLWTNTTTYSLLIALLSLQWLKPPYYPTKNLTQWLGIDQISAPLLVLSC
WLLPLMILASQNHLQHEPLQRKRTFLTTLILLQTFLILAFSATELTLFYIMFEATLIPTLILITRWGNQP
ERLSAGTYFLFYTLISSLPLLIAILYLHNQTGTLSLPMLQLTHPTLTNSWTNLLLWLACLMAFMVKMPLY
GLHLWLPKAHVEAPIAGSMVLAAILLKLGGYGIIRITLLLPPLSNTLHYPFLTLALWGALMTSLICLRQT
DLKSLIAYSSVSHMGLVIAATMIQTPWSLSGAMILMIAHGLTSSMLFCLANTNYERTHSRTLLLTRGLQL
LLPLMTTWWLLANLTNMALPPTINLMGELTIMTSLFNWSPTTIILTGLATLITASYTLYMFLSTQRGTLP
THITTIQPTHTREHLLMTLHIIPLLLLILKPELISGT
>gnl|CDD|177184 MTH00125, ND4L, NADH dehydrogenase subunit 4L; Provisional
MTPTHFSLYTAFMLSLLGLSFHRTHLMSALLCLESMMLSLFIMLSLWPITTQTPSFTPMPIILLTFSACE
AGTGLALLVATTRTHGSDHLKNLNLLQC
>gnl|CDD|177185 MTH00126, ND4L, NADH dehydrogenase subunit 4L; Provisional
MTPVHFSFSSAFILGLMGLAFHRTHLLSALLCLEGMMLSLFIALSLWALQLESTSFSAAPMLLLAFSACE
ASAGLALLVATARTHGTDRLQNLNLLQC
>gnl|CDD|177186 MTH00127, ND4, NADH dehydrogenase subunit 4; Provisional
MLKILIPTLMLIPTTWLTPAKWLWTTTLAHSLLIALASLTWLKNLSETGWSSLNLYMATDPLSTPLLVLT
CWLLPLMILASQNHTAPEPINRQRMYITLLTSLQIFLILAFGATEIIMFYVMFEATLIPTLIIITRWGNQ
TERLNAGTYFLFYTLAGSLPLLVALLLLQNSTGTLSMLTLQYSQPLQLSSWADKLWWAGCLLAFLVKMPL
YGVHLWLPKAHVEAPIAGSMVLAAVLLKLGGYGMMRMMVMLDPLTKELSYPFIILALWGIIMTGSICLRQ
TDLKSLIAYSSVSHMGLVAGGILIQTPWGFTGALILMIAHGLTSSALFCLANTNYERTHSRTMLLARGLQ
MILPLMATWWFIASLANLALPPLPNLMGELMIITSLFNWSPWTLALTGLGTLITAGYSLYMFLMTQRGPL
PDHIIALNPSHTREHLLMALHLLPLLLLILKPELIWGWT
>gnl|CDD|177187 MTH00129, COX2, cytochrome c oxidase subunit II; Provisional
MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPA
VILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADH
RMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIV
VEAVPLEHFENWSSLMLEDA
>gnl|CDD|177188 MTH00130, COX3, cytochrome c oxidase subunit III; Provisional
MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGH
HTPPVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLAS
GVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVII
GSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS
>gnl|CDD|177189 MTH00131, CYTB, cytochrome b; Provisional
MASLRKTHPLLKIANDALVDLPAPSNISVWWNFGSLLGLCLITQILTGLFLAMHYTSDISTAFSSVAHIC
RDVNYGWLIRNLHANGASFFFICIYLHIGRGLYYGSYLYKETWNIGVVLLLLVMMTAFVGYVLPWGQMSF
WGATVITNLLSAVPYVGNTLVQWIWGGFSVDNATLTRFFAFHFLFPFVIAAATILHLLFLHETGSNNPLG
LNSDADKISFHPYFSYKDLLGFAILLLALTSLALFSPNLLGDPDNFTPANPLVTPPHIKPEWYFLFAYAI
LRSIPNKLGGVLALLFSILVLMVVPILHTSKQRGLTFRPLTQFLFWTLVADVLILTWIGGMPVEHPFIII
GQVASVLYFSLFLVLMPLAGWLENKALEWA
>gnl|CDD|177190 MTH00132, ATP6, ATP synthase F0 subunit 6; Provisional
MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWA
LLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIP
VLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMI
QAYVFVLLLSLYLQENV
>gnl|CDD|177191 MTH00133, ATP8, ATP synthase F0 subunit 8; Provisional
MPQLNPAPWFAILVFSWLVFLTIIPPKVLAHTFPNEPTPQSTEKPKTEPWNWPWH
>gnl|CDD|177192 MTH00134, ND1, NADH dehydrogenase subunit 1; Provisional
MLSTLITHIINPLAYIVPVLLAVAFLTLLERKVLGYMQLRKGPNIVGPYGLLQPIADGVKLFIKEPVRPS
TSSPFLFLATPMLALTLALTLWAPMPMPYPVTDLNLGILFILALSSLAVYSILGSGWASNSKYALIGALR
AVAQTISYEVSLGLILLSVIIFTGGFTLQTFNTAQESIWLLLPAWPLAAMWYISTLAETNRAPFDLTEGE
SELVSGFNVEYAGGPFALFFLAEYANILLMNTLSAILFLGASHIPTLPELTTINLMTKAALLSVVFLWVR
ASYPRFRYDQLMHLVWKNFLPLTLALVIWHLALPIAFAGLPPQL
>gnl|CDD|177193 MTH00135, ND2, NADH dehydrogenase subunit 2; Provisional
MNPYVLTILLFSLGLGTTLTFASSHWLLAWMGLEINTLAIIPLMAQHHHPRAVEATTKYFLTQATAAAMI
LFASTTNAWLTGQWDIQQMSHPLPTTMITLALALKIGLAPLHFWLPEVLQGLDLTTGLILSTWQKLAPFA
LILQIAPTNPTLLITLGLTSTLVGGWGGLNQTQLRKILAYSSIAHLGWMILVLQFSPSLTLLALLTYIIM
TSSAFLTFKLNSSTKINTLATSWTKAPALTALTPLILLSLGGLPPLTGFMPKWLILQELTKQDLPLTATL
AALSALLSLYFYLRLSYAMTLTISPNTLNGTTPWRLPSTQLTLPLAISTTATLMLLPLTPAILALLT
>gnl|CDD|177194 MTH00136, ND3, NADH dehydrogenase subunit 3; Provisional
MNLITTILTITIALSLILAIVSFWLPQMTPDHEKLSPYECGFDPLGSARLPFSLRFFLVAILFLLFDLEI
ALLLPLPWGDQLPSPLLTFFWATAVLILLTLGLIYEWLQGGLEWAE
>gnl|CDD|214428 MTH00137, ND5, NADH dehydrogenase subunit 5; Provisional
HPTTLIMTSSLILIFALLIYPLLTTLSPNPQKPNWALTHVKTAVKTAFFVSLLPLFLFLNQGAETIITNW
NWMNTLTFDINISFKFDHYSIIFTPIALYVTWSILEFASWYMHADPNMNRFFKYLLIFLIAMIILVTANN
MFQLFIGWEGVGIMSFLLIGWWYGRADANTAALQAVIYNRVGDIGLILAMAWMATNLNSWEIQQIFALSK
DFDLTLPLLGLILAATGKSAQFGLHPWLPSAMEGPTPVSALLHSSTMVVAGIFLLIRLSPLMENNQTALT
TCLCLGALTTLFTATCALTQNDIKKIVAFSTSSQLGLMMVTIGLNQPQLAFLHICTHAFFKAMLFLCSGS
IIHSLNDEQDIRKMGGLHHLTPFTSSCLTIGSLALTGTPFLAGFFSKDAIIEALNTSHLNAWALTLTLIA
TSFTAVYSLRVVFFVSMGHPRFNPLSPINENNPAVINPIKRLAWGSIIAGLLITSNILPLKTPVMTMPPL
LKLAALIVTILGLLIALELASLTNKQFKPTPTLPPHHFSNMLGFFPAIIHRLTPKLNLTLGQTIATQMVD
QTWLEKTGPKGIASLQLPLITTTSNIQQGMIKTYLTLFLLTLALATLLLLL
>gnl|CDD|177196 MTH00138, ND6, NADH dehydrogenase subunit 6; Provisional
MTYLMSLFLLGLVLGLVAVASNPSPYFAALGLVVVAGVGCGVLVGHGGSFLSLVLFLIYLGGMLVVFAYS
AALAAEPYPESWGSWSVLGYVVGYLVGVVLAAGLFWGGWYEGSWVVVDELKEFSVLRGDVGGVALMYSSG
GGMLVICAWVLLLTLFVVLELTRGLSRGALRAV
>gnl|CDD|214429 MTH00139, COX2, cytochrome c oxidase subunit II; Provisional
MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPA
FILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDN
RLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIV
VEAISPKFFLEWILEK
>gnl|CDD|214430 MTH00140, COX2, cytochrome c oxidase subunit II; Provisional
MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPA
LILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDN
RLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIV
VEAVPLEDFVKWLELMSE
>gnl|CDD|177199 MTH00141, COX3, cytochrome c oxidase subunit III; Provisional
MTRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHT
SKVQRGLRWGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGV
TVTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGT
TFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLSIYWWGS
>gnl|CDD|214431 MTH00142, COX1, cytochrome c oxidase subunit I; Provisional
MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMP
VMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGS
VDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTD
RNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGL
LGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGG
LTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVN
LTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSL
EWSHRLPPDFHTYDELPILVV
>gnl|CDD|177201 MTH00143, ND1, NADH dehydrogenase subunit 1; Provisional
LVSLLSSVFTYLCVLLAVAFFTLLERKGLGYFQIRKGPNKVGLMGLPQPLADAVKLFTKEFVKPTMSNKF
PFFLAPCLSLILALLLWQLYPSYFSSSYFGWGLLFFLCVSSLNVYGVLLAGWSSNSKYALLGAVRAVAQT
ISYEVSMSLILLFPLFLSGSFSFIEISESQFSVWLGFLMFPVFLMWFVSCLAETNRAPFDFAEGESELVS
GFNVEYGGGGFALLFLAEYANILFMSLLTVVLFFGGSSVLFLLGGVVFMFKVLFFAFLFIWVRASYPRFR
YDLLMMLCWKSFLPFSLSILVLFVVLV
>gnl|CDD|214432 MTH00144, ND2, NADH dehydrogenase subunit 2; Provisional
MSSPSNLLFLFLMVMGTLLSLSSSHWLGVWVGLEINLIGFLPLLVYKKKSSESESVVKYFIIQSLGSSLL
IFGSLIMYNLSFSWFSMSLLLLGLCLKLGLFPFHFWVPSVMAGLSWLSCFLLLTWQKVAPLFLLSNFLDL
YWLAYLLCVISVLSALVGSIGGLNQTQVRALLAYSSISHTGWMLVAILHGSWLMWMYFLIYIVSSGFLFF
SLWSGDSGSMKDLGSLKPSYKTGLSIISLLLSLGGLPPFLGFCSKLLVLISSMESSPLLLILLLLLGSLI
SLFFYLSVFFSSFLSSSKSKKSNSSKVLNSSIISLNLLGGLLFLLLYL
>gnl|CDD|177203 MTH00145, CYTB, cytochrome b; Provisional
MLSPLRKSHPVLKVVNGSLYDLPAPVNLSIWWNFGSLLGLCLGIQILTGLFLSMHYTAHVDLAFSSVIHI
MRDVNYGWLLRSLHANGASFFFICIYLHIGRGLYYGSYLMQHTWNIGVTLLLLSMGTAFLGYVLPWGQMS
FWGATVITNLLSAIPYVGKMLVEWVWGGFSVGNATLKRFFSLHFLLPFVILGLSVLHLLFLHETGSNNPL
GLDSDGDKVPFHPYYTIKDLVGFVVLLFLLVFLVLFFPNLLGDPENFIPANPMVTPVHIQPEWYFLFAYA
ILRSIPNKLGGVIALVMSIVILFFLPLLHVGKFRSLSFYPLNQVLFWIFVGNFFILTWIGACPVEEPYET
IGQVFTVLYFLFFLILPLVQKLWDNILDY
>gnl|CDD|177204 MTH00147, ATP8, ATP synthase F0 subunit 8; Provisional
MPQLSPLNWIFLFILFWSAVIIVSVIIWWSTKNLYTINKSPKTNKENKWNW
>gnl|CDD|214433 MTH00148, ND3, NADH dehydrogenase subunit 3; Provisional
MLSILLSLLFALILSPVLLLLGLVLSKRSYSDREKSSPFECGFDPISSARSPFSLRFFLLAILFLVFDVE
IVLLFPVLQSLGSSFSVWSLTSLFIFLLILILGLFHEWNEGSLDWVS
>gnl|CDD|214434 MTH00149, ND4L, NADH dehydrogenase subunit 4L; Provisional
SMFMLLLLSLFGFLMGVFALLFQYKHLLSILLSLEALMLSLLVMMFSSSGLISFSSYLFLIILTFGACEA
SLGLSLLVSLIRLHGNDYVSSLSSLKF
>gnl|CDD|214435 MTH00150, ND4, NADH dehydrogenase subunit 4; Provisional
LSLLLLYSSFSSYESLSELFSVDSMSSLLISLSLWISGLMMLASQKSVKLRNKSSSFSLLVLLLCLILVL
AFSVSSLLMFYFFFEASLIPTLLLILGWGYQPERLQAGMYMMLYTVGASLPLLLVILWMSSSYGSSFMLL
ISSLRKLLSSMGLWGLLVFLAFLVKLPMYPFHLWLPKAHVEAPVAGSMILAGILLKLGGYGILRMMMVFS
LSSSSFSIFLISLSLWGGVLTSLICLRQSDVKSLIAYSSVGHMSLVLAGVLSNTSWGWVGALIMMVSHGF
CSSGLFCLANYTYEKVHSRSLFLSKGMLMLYPSLSLWWFLFCIINMAAPPSLNLLSEIMIFPSLISYSPW
FFVPLGLMVFLSGLYSLYLYTSIQHGGSSSFLKPFNELKSSEMLLLLLHWVPLLLLILKSDLLFMWI
>gnl|CDD|214436 MTH00151, ND5, NADH dehydrogenase subunit 5; Provisional
LKMSSLSSFLLFSYSVFLFPLLGYFGLNGISLIFEWELLSVSSCSFSFELVLDWVSLSFSGVVCLISGCV
FLFSSSYMSEDPFLKRFMWLVMLFVLSMNLLIFIPSLPSLLLGWDGLGIVSFALVIYYQNKKSLSAGMLT
ALTNRIGDVLILLSIALLVLLGHWSILSMWDFKLSGWLGLLLVLAAMTKSAQIPFSSWLPAAMAAPTPVS
ALVHSSTLVTAGVFLLIRFFPFLSSSSGFSSFLLFISLLTLLMAGISACYENDLKKIIALSTLSQLGVMM
FSLGLGMPSLALFHLYTHALFKALLFLCAGSIIHSSSGTQDIRLLGSLFLSLPLTSGCLNISSLSLCGAP
FLSGFYSKDLILESSLMSPTSLLMVLLMFVGVGLTALYSARLSFCLVWGSMKSSSLSSKSDEDFYVSLPM
LLLSLGALIGGKLLQSLFEGFSEEFFLPSYLKLLIGFVILLGLFLSFGFWDSGFSSSKMVKLSFFFSSMW
FLSPLSSQPLKSLSLKLSNSSMKSLDMGWLEILGGQGVFKANKSFSVLNESWPVKWFNFFIGLILLLVLF
LVVIS
>gnl|CDD|214437 MTH00152, ND6, NADH dehydrogenase subunit 6; Provisional
MSLMILLSVCFSLFLLLPLSKQPLSLGLVLLLLSLFVCVEIGLTLSSWYGYLLFLVYVGGLLVMFAYVVS
LSPNPLFGSNFKFVFFSLTLFGFLGLFFFFLYLYSSGGLSLSSLFDGSSGSLSFGGGLYSSSGWSIFVFL
AVLLLIVMVSVVKICYYEEGSLR
>gnl|CDD|177210 MTH00153, COX1, cytochrome c oxidase subunit I; Provisional
MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMP
IMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGAS
VDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTD
RNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGL
LGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGG
LTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVN
LTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSI
EWLQNLPPAEHSYSELPLLTN
>gnl|CDD|214438 MTH00154, COX2, cytochrome c oxidase subunit II; Provisional
MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPA
IILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDN
RLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIV
IESVSVNNFINWIKNMS
>gnl|CDD|214439 MTH00155, COX3, cytochrome c oxidase subunit III; Provisional
KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHT
KKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGV
TVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGT
TFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY
>gnl|CDD|214440 MTH00156, CYTB, cytochrome b; Provisional
LKIINNSLIDLPTPSNISYWWNFGSLLGLCLMIQIITGLFLAMHYTADIELAFSSVIHICRDVNYGWLLR
TLHANGASFFFICIYLHIGRGIYYGSYKLKHTWMSGVIILFLVMATAFLGYVLPWGQMSFWGATVITNLL
SAIPYLGTDLVQWIWGGFSVDNATLTRFFTFHFLLPFIILAMVMIHLLFLHQTGSNNPLGLNSNIDKIPF
HPYFTFKDLVGFIIMLMLLILLTLINPYLLGDPENFIPANPLVTPVHIQPEWYFLFAYAILRSIPNKLGG
VIALVMSILILMILPFTNKSKFRGNQFYPINKILFWIFVNIVILLTWIGARPVEEPYILTGQILTILYFL
YFIINP
>gnl|CDD|214441 MTH00157, ATP6, ATP synthase F0 subunit 6; Provisional
MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTL
IFISLFSFILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPF
MVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYV
FSVLSTLYSSEVN
>gnl|CDD|177215 MTH00158, ATP8, ATP synthase F0 subunit 8; Provisional
MPQMSPMNWLILFILFLITFILFNILNYFIFI
>gnl|CDD|214442 MTH00160, ND2, NADH dehydrogenase subunit 2; Provisional
MMMNSSKLLFLSTLIMGTLISISSNSWFGAWMGLEINLLSFIPLISNKKNLMSSESSLKYFLIQALASII
LLFSIILNMLNLMLFNNISSMLINSSLLLKLGAAPFHFWFPEVMEGLSWINCFILMTWQKIAPLILLSYL
INNNFIIIIIILSAIIGAIGGLNQTSLRKILAYSSINHLGWMLSSMMISENLWLIYFLIYSIISLSIILL
FNKFNIFFLNQLFNSNNKSKKIKFLLFLNLLSLGGLPPFLGFLPKWIIIQLLISNNMFFLLFILIMSSLI
TLYFYLRISYSSLMLNYNKNKWNLKKKKNKFSLILNFLSFISLFGLILSSLLFLL
>gnl|CDD|177217 MTH00161, ND3, NADH dehydrogenase subunit 3; Provisional
MILIILLIILLISIILMILASLLSKKSIMDREKSSPFECGFDPKSSARLPFSLRFFLIAIIFLIFDVEIA
LLLPMIFIFKTSNMMSWLITSSFFILILLLGLYYEWNQGALEW
>gnl|CDD|177218 MTH00162, ND4L, NADH dehydrogenase subunit 4L; Provisional
MMMLLIFLFMFFSGLLVFLSKRKHLLLMLLSLEFMVLSLFFLLFLYLSFFNYELYFLLFFLTFSVCEGAL
GLSILVSMIRSHGNDYFSS
>gnl|CDD|214443 MTH00163, ND4, NADH dehydrogenase subunit 4; Provisional
MLKFLFMLLFLIPLCFLKNSWWLVQSLLFLLSFLFMLLFSLSFYFSNISYFFGLDLLSFGLILLSFWICM
LMILSSESVYKKNNYSNLFLFLILFLLIFLLLTFSSMNLLLFYIFFESSLIPTLFLILGWGYQPERLQAG
IYLLFYTLFASLPLLVGIFYLYNNSGSLSFFLLNFFGSLNFLWYLSMILAFLVKMPMFFVHLWLPKAHVE
APVSGSMILAGVLLKLGGYGLLRVMSFFSKLGLKFNYIWISISLVGGVIVSLICLRQVDLKSLIAYSSVA
HMGLVLGGLMTFSYWGLMGSLLMMIGHGLCSSGLFCLANIIYERLGSRSLLINKGLLNFMPSMSLWWFLL
SSSNMAAPPSLNLLGEISLINSLISWSKLSMIFLMLLSFFSAAYSLYLYSYSQHGKYYSGLYSCSSGKVR
EYLLLFLHWLPLNLLILKSDLFMLW
>gnl|CDD|214444 MTH00165, ND5, NADH dehydrogenase subunit 5; Provisional
MSMCLISFFFLFFLSLILFFLGLYFLLNDYSLFIEWELFSLNSSSIVMTFLFDWMSLLFMSFVLFISSMV
IYYSKSYMSGDKNINRFIYLVLLFVLSMMLLIISPNLISILLGWDGLGLVSYCLVIYYQNKKSYNAGMLT
ALSNRIGDVAILLSIAWMMNFGSWNFIFYLDFMKNSFEMLLIGLLIMLAAMTKSAQIPFSSWLPAAMAAP
TPVSALVHSSTLVTAGVYLLIRFNNLLFSSFFSKFLLLISLLTMFMAGLGANFEFDLKKIIALSTLSQLG
LMMSILSLGFPKLAFFHLLTHALFKALLFLCAGSIIHNMSNSQDIRFMGGLSNFMPLTSSCFNISNLSLC
GFPFLSGFYSKDLILEMVSMSNLNFFIFFLFFFSTGLTVSYSFRLIYYSMSGDFNLKSLNNLSDESKFML
KSMILLLFMSIFGGSMLSWLIFPEPYMICLPFYLKLLTLFVILLGGWLGYELSLMSLSYNLKSLKNYKLS
SFLGSMWFMPFLSTYGISYYPLNLGSLSLKSFDQGWSEYFGGQGLYNFLKKLSKLIQWLQNNNLKIYLLS
FLLWMIILLLLFL
>gnl|CDD|214445 MTH00166, ND6, NADH dehydrogenase subunit 6; Provisional
KMMLMMLLLILSIIFLFLNHPLSMGLILIIQTILISLLLGLMMKSFWFSYILFLIFLGGMLVLFIYITSL
ASNEKFKFSLKLLILFLLMLLLMLNNFIKNSEMSNFNNNFNFFENSFSLSKLYNFPTMLITLFMIIYLLL
TLIVVVKITNIFKGPLRSKN
>gnl|CDD|177222 MTH00167, COX1, cytochrome c oxidase subunit I; Provisional
MWINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMV
MPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAG
ASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLL
TDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAI
GLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTV
GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIG
VNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTST
NVEWLHGCPPPHHTWEEPPFVQ
>gnl|CDD|177223 MTH00168, COX2, cytochrome c oxidase subunit II; Provisional
MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPA
FILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDN
RLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIV
VEFVPWETFENWVDS
>gnl|CDD|214446 MTH00169, ATP8, ATP synthase F0 subunit 8; Provisional
MPQLDSVTYLTQYIWTLIILFFLFSLLVNYILPKIQQQLVIRTKGVNSVEGKKERPKIEIFKKLFDL
>gnl|CDD|177225 MTH00171, ATP8, ATP synthase F0 subunit 8; Provisional
MPQLNPIPWFFIFLFSWLIFLTLLPNKITKHIFTNKPSPNQTEKPKPNEWNWPW
>gnl|CDD|214447 MTH00172, ATP6, ATP synthase F0 subunit 6; Provisional
MSSSYFDQFNIVWLIGLTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLK
YFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGL
APLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVA
VIQAYVFCLLTTIYLADTIVLH
>gnl|CDD|214448 MTH00173, ATP6, ATP synthase F0 subunit 6; Provisional
MMVDLFSSFDDHNSSFSSLSFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGG
FSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGL
NPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVGYFIFEVAV
MLIQAYIFTLLIKLYSDEHPV
>gnl|CDD|133799 MTH00174, ATP6, ATP synthase F0 subunit 6; Provisional
MVAAYFDQFNIIPIFSIWVYFLSFWINGEFFCFTNTFFMMSFAVFLFYTIGAKGNNNTLVPNRILVGLEL
IYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLI
TFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILI
GSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYLRDTVELH
>gnl|CDD|177228 MTH00175, ATP6, ATP synthase F0 subunit 6; Provisional
MLAAYFDQFNIIRLITIQAFLGDWLVTFTNSSMMMVLAVIIFWLLLKGDKLIPNRWQSIMELIYLNIRSV
VHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLS
ILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNGLIILSLFPMLI
MIFITLLEMAVAVIQAYVFCLLTTIYLGDTIALH
>gnl|CDD|214449 MTH00176, ATP6, ATP synthase F0 subunit 6; Provisional
MLVDLFSSFDPPNKNIFSMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILG
SASIIISLFILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLL
NPFLVLIELVSLLIRPLTLAVRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVC
MIQAYVFTLLLSLYLDEHP
>gnl|CDD|177230 MTH00179, ATP6, ATP synthase F0 subunit 6; Provisional
MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWA
VLFLSLMLFLLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIP
MLVWIETISLLIRPLALGVRLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMI
QAYVFVLLLSLYLQENL
>gnl|CDD|177231 MTH00180, ND4L, NADH dehydrogenase subunit 4L; Provisional
MYYEYLTVGIILFILGVLGIVLNRSNLIIMLMSIELMLLAISLLFLINSVAIDNLIGQIFTIMILTVAAA
ESAIGLAILVAYYRIRGTIAVKSLNLLRG
>gnl|CDD|214450 MTH00181, ND4L, NADH dehydrogenase subunit 4L; Provisional
MMFVFISAFILLLLGLSLYKTHLLSLLLCLEGMMLFLFLLLALFSLLSSSSSMLMFGLILLTFSACEAVL
GLSLLVATNRTHGSDHLLKFNLL
>gnl|CDD|214451 MTH00182, COX1, cytochrome c oxidase subunit I; Provisional
KNLYLTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFF
LVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAH
SGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITM
LLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAML
SIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLF
TLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMF
IGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEG
TGESWASLEWVHSSPPLFHTYNELPFVYKSKLSEG
>gnl|CDD|177234 MTH00183, COX1, cytochrome c oxidase subunit I; Provisional
MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMV
MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAG
ASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLL
TDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAI
GLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTV
GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVG
VNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTST
NVEWLHGCPPPYHTFEEPAFVQVQSN
>gnl|CDD|177235 MTH00184, COX1, cytochrome c oxidase subunit I; Provisional
MSLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFF
LVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAH
SGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITM
LLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMV
SIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLF
TMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMF
IGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVGWVED
SGHYPSLEWAQTSPPAHHTYNELPYVYKG
>gnl|CDD|164736 MTH00185, COX2, cytochrome c oxidase subunit II; Provisional
MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPA
IILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDH
RMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIV
VEAVPLEHFENWSSLMLEEA
>gnl|CDD|177236 MTH00186, ATP8, ATP synthase F0 subunit 8; Provisional
MPQLSPLFWALLFIMIWLLIFLAMSMTWWLQNPKLPSSSKVKMTLKSPKWKW
>gnl|CDD|177237 MTH00188, ND4L, NADH dehydrogenase subunit 4L; Provisional
MFFSMILVILLFVVLGLFTFLLNRKHLLMLLLSLEAIMLSLFWFLLVGLSYMEKELYLSLVLLTFAACEA
SVGLALLVSLIRSHGSDYVSSLNLIKC
>gnl|CDD|177238 MTH00189, COX3, cytochrome c oxidase subunit III; Provisional
MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFH
TPPVQKGLRYGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSG
VTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIG
STFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS
>gnl|CDD|177239 MTH00191, CYTB, cytochrome b; Provisional
MRKTHPLLKIVNGSLIDLPSPSNISYWWNFGSLLGLCLIIQILTGLFLAMHYTADISLAFSSVVHICRDV
NYGWLLRNIHANGASFFFICIYLHIGRGLYYGSYLNKETWNVGVILLILSMATAFLGYVLPWGQMSFWGA
TVITNLLSAIPYIGDDLVQWLWGGFSVDNATLTRFFTFHFLLPFLIAALSLIHLLFLHETGSNNPLGLNS
DSDKIPFHPYFSYKDILGFFILLFLLLFLVLFSPNLLGDPENFIPANPLVTPVHIKPEWYFLFAYAILRS
IPNKLGGVLALVMSILVLFLLPLLHTSKQRSNTFRPLTQVVFWLWVANFILLTWLGGQPVEDPFILLGQI
SSFLYFFLFLLLFPL
>gnl|CDD|177240 MTH00192, ND4L, NADH dehydrogenase subunit 4L; Provisional
MTTGYLLVSIILFTTGVSGIIINKNNIILILMSIELILLAISYLLIVYSVTLDNLLGIIFSLMVLTVAAA
ESAIGLAILVAYFRLTGTITIKALNLLRG
>gnl|CDD|177241 MTH00193, ND1, NADH dehydrogenase subunit 1; Provisional
LMMMLINFLLLIICVLVSVAFLTLLERKVLGYIQIRKGPNKVGFMGILQPFSDAIKLFTKEQTYPLMSNY
LLYYFSPVFSLFLSLLIWLIYPYLFNLISFNLGILFFLCCSSLGVYTVMIAGWSSNSKYSLLGSLRSVAQ
TISYEVSLALILLSFIFLIGSFNLLDFMNYQKYIWFIFFSFPLFLIWFVSCLAETNRTPFDFAEGESELV
SGFNVEYSSGGFALIFLAEYSSILFMSMLFVLMFLGGDLLSLLFYLKLLFISFLFIWVRGTLPRFRYDKL
MYLAWKSFLPLSLNYLLFFFGLKIFL
>gnl|CDD|214452 MTH00195, ND1, NADH dehydrogenase subunit 1; Provisional
WMISVIHFLIQIVPVLLAVAFFTLLERKILGYIQLRKGPNKVGPYGLLQPIADAVKLFIKEPVKPSTSSL
WLFFFAPVLALALALILWVPIPSPFGFSSINLSVLFFLCVSSLSVYSILGSGWASNSKYALLGAIRAVAQ
TISYEVSMGLIILCPICLAGSFDFTIMVISQGFSWVILLCPPISFMWYVSTLAETNRAPFDFAEGESELV
SGFNVEYAGGPFALIFMAEYSNIIFMSVLTTILFLGGGGTIIVALKSLFLSFCFLWVRGSLPRFRYDQLM
HLTWKCYLPLILSLLIPLAAIPFALNS
>gnl|CDD|214453 MTH00196, ND2, NADH dehydrogenase subunit 2; Provisional
MVALGILCLISSSNWLSVYLAIELQTLSLFILIAQNRGSGYSAEAGLKYFVLGALSSGLFLFGCALLCGT
TGGLHLSYINLVLNSGQSFSSVSVPIGYLLIIVALLFKLSVAPFHMWAPDVYEGAPTKTTALLAIVPKLG
IFSILVSIGLNVNILLIGGLFSLFVGAIGALNQTKIKRLLAYSGIGHMGFVLWGIEIGSFESIQASLVYL
FIYIIMSICVFSIILALNVYKNLIIEFSGLSRRLPILAITLALTFLSIAGIPPLVGFLGKWLILLSGVVY
QYYLIFLLAVFCSVIAGVYYVRIVKILFFQANSFLLISTKILKKENKINLRKALLIGFSLYLILFTILSP
NFFFQLAHWAIGGLF
>gnl|CDD|177244 MTH00197, ND2, NADH dehydrogenase subunit 2; Provisional
FLFLFIIFGGVLFSLSSSNWFLVWIGMELNLIGFIPLLSQNKSITENEGAMKYFLFQEFGSALLLMGGSL
SFSNLYLSLLSVVLVILGLLLKLGAFPFHFWVPSVMESLSWFNCFLLATWQKLAPLLILAFNSSSFMGLL
ICSVLSSLIGGIGGMNQSNIRQLLAYSSIGHTGWMLMSLVYSPSIFMLYYLIYFVIMFMLFLFLSKNNLS
SLNQQYSNPESMSSNLVFLGLSFLSLGGLPPLSGFFLKWLILTSLLSSNISLITFMLILSTCFSLYYYLS
LAYKSLILSNWMINFLMKINLLYSGLFILLMMMLPLLMIFTMI
>gnl|CDD|214454 MTH00198, ND2, NADH dehydrogenase subunit 2; Provisional
MNSPRDLLDPIISMITQFGSILVITFAIFIILLRPVSRRSHLYIAFFATFIAFFFTIQGSFGYSGGSPLG
SPSTLKDLWENDVKSLSPAFENSEPMTPFPWILMDPTLGRGEPVPLNLFDILSNYFGGAFGAFAMGPNGA
EILGLRGLGNLSVSAFGMVKENSHWASECVILLSLMGLLFLTNERGPRSGFALVLIVGLGGLLLIESANW
LTIYLALEFQTLALFILAGEGSQPGSHFPSPGNTPPESGLKYWILGAMSSGFYLFGCALYFGFTGNEGML
GTILSATLETTNIELRQGSLGYLFITVAILFKLAAAPFHMWTPDVYEGAPTPTTALIAIIPKFTVYILLT
SLVITSKLLLSVAIISLVVGAFGALNQTRIKRLLAYSGIGHIGFILIGVSAGTYESLQASWTYAVTYLVS
ALASFTVICTLEEFGTRTPTSRQRDGSFGNYNLVRRLVDLTILSRGQPYIAFSLAIVFLSLAGIPPLLGF
LGKWFILVGSIKIAFSSSLSIYYLVALFAIICTCISAFYYIRIVATIYFNFTRPLIKTKTPLSFILTWES
ILKGGTSEAAPGGGKSILISIYMYFILFLIICPQPLLLISYEAMPGT
>gnl|CDD|177245 MTH00199, ND2, NADH dehydrogenase subunit 2; Provisional
MIIINPEVLLSLVVLSLVLYGVNLSTLKLSIGVLLLIGLIVELNSLNLFQSDKVLDGTNGLLLTNSWIII
SKIIIIIGSISILLMGSGETILSEGGQSSPILILIVALGSLLLVSSINWLSIYLAIELQTLTLFILVALK
RDSAYSTEAGLKYFVLGAVSSGLFLFGCALLYGLTGETSIQGINSILTGDVGKILITISLLFKLSAAPFH
MWAPDVYEGAPTITTALLATVPKIGVFSILVQIGPVTNVVLICAVLSIIYGAIGALNQTKIKRLLAYSGI
GHMGFILFGVAIGSFESIQASLIYMIIYVIMSICSFSIILSLKLTKGLIVEVSGLSRKNPVIALTLALTF
LSIAGIPPLAGFLSKWLILLSGVSSGYYLICIIAVLSSVIAGVYYVRVVQIIYFQADYSILIWQKVLKKE
ERLDLSKSILIGVTFFIILFLMISPNFLLQITHDATISLY
>gnl|CDD|177246 MTH00200, ND2, NADH dehydrogenase subunit 2; Provisional
MSPLILPLFILSLGLGTLLTFSSSHWFLIWLGLEINTLAIIPLLIKQHHPRKVEATTKYFIIQATASALL
LFGGLLNAWTSGQWGISEMLGPLSETLILLALALKLGLAPGHFWVPDVLQGLSLQTGLILSTWQKLAPFA
LLIQLAPALNSNILLLLGLLSVLVGGWGGLNQTQLRKILAYSSIAHLGWLLSGLVYSPNLALLYLLLYVI
ITLTVFLLLNLLNSTKINSLSSSKTKNPILSMLLGLTLLSLGGLPPLTGFFPKWLILQELSKQGLFIYAT
ILLLGSLLSLFFYLRLSYLTLLTLSPNQINMMSSWRTKSNSNLLVGLLLLLSILGLPLTPQLLFLFF
>gnl|CDD|214455 MTH00202, ND3, NADH dehydrogenase subunit 3; Provisional
MLLILFMSILSILISSLLFLVSWMLSFRSLMDREKSSPFECGFDPKESARLPFSMRFFLLAVIFLVFDIE
IALLLPLPLVLKSSWSKGGLLGGTIFLLILIGGLIHEWKEGSLDWVK
>gnl|CDD|214456 MTH00203, ND3, NADH dehydrogenase subunit 3; Provisional
MNLIMLFFLIALLLSLILLFIAFWLPKVNPDGEKLSPYECGFDPLGSARLPFSLQFFLVALSFLLFDLEI
ALLLPLPWSNQLSSLSLLLAFLFLILLTLGLIYEWLQGGLEW
>gnl|CDD|164750 MTH00204, ND4, NADH dehydrogenase subunit 4; Provisional
NGLSLIFLILFMGIINVMGVPRENSVKLKKRALEWSLAILFSTLVLWGAFDGEGQFQFINLIEWIISPTL
NFQWGPLVFAVDGVSLFFILLTTLLIPICILISWKSIKFLFKEFLLCLLFLEVLLIGVFSVLDLLLFYIL
FEGILIPMFLLIGIWGSREEKVRASYYFFFYTFAGSVFMLLGIFQLYSITGTTDYQILLNIKLPLSIQKW
LLVGFFLSLAVKIPQIPFHIWLPQAHVEAPVAGSVILAGILLKLGGYGFLRFSWPLFPAASEYFAPLIVM
LSVIAVIYGSLTTCRQVDFKRLIAYSSVAHMGLVPLGLFTHTIEGLVAAVFLMLAHGFVSSALFIAVTFL
YERHHTRLIKYYRGLTLTMPLFVIIMLVLSLANMGFPLSCNFVGEFFSLLAAFEYSLGLGVLVTSGMVWS
AAYSLYLYNRISFGGGSNYLLFSRDLNRRELLAILPLIIAIFLLGIVPFIIIDLVKNSLVFSPGG
>gnl|CDD|214457 MTH00205, ND4, NADH dehydrogenase subunit 4; Provisional
MSIFGVFSLLIILFVLKFKDWSFFSNLLLIGLFFSSFFFSNSFLMTSFISSSFSFDSLSLPLIMLSFWIS
LLMVLASYKVFKSNKNSKLFTVSVIMLLLILILSFSVDNLLLFYITFEASLIPTLILILGWGYQPERLQA
SMYMMMYTLCASLPLLIGLFFLNSLNFSLSMFFNFPLNFSDFYLFLYWIFLMLAFLVKLPMYFVHLWLPK
AHVEAPVSGSMILAGVLLKLGGYGLIRITSMLYKLNSNFSELFFSISLWGGVMTGMICLRQVDLKSLIAY
SSVGHMGLMVVGVFSNTSWGMNGAIIMMVAHGLCSSGMFALANVNYERTNSRSMLMNKGVLNTFPFLVLM
WFLLISCNMAAPPSLNLASEILLIMSLLSSSKISGIPLSLISFLSGAYSLYLYSQSQHGKVSSQISSFLA
ISEREYYILILHWFPLNILILKLKIFIC
>gnl|CDD|214458 MTH00206, ND4, NADH dehydrogenase subunit 4; Provisional
KILIPLIMLLLMTILSKKKWLWRSTTFFSFLIALLFLLWFKWSSEVGWSFSNLYLSYDPLSSPLVILSCW
LLPLMFLASQNHMKNEPINRQRIYITLLIVLQLFLILFFSSSNLLLFYILFEASLIPTLLLITRWGNQKE
RLNAGYYFLFYTLIGSLPLLIALLFLQNSLGSLSLYILYFSKLTTWNNNLWWLACILAFLVKLPLYGVHL
WLPKAHVEAPVAGSMVLAGVLLKLGGYGMMRIILILGPSTKLSSYFFIILGLWGSIMTSSICLRQTDLKS
LIAYSSVSHMSLVTAGILSGSPWGFKGALLLMIAHGLVSSALFCLANLLYERSHTRTILGNRGLQMILPL
LSFWWLLFFLANLGLPPFPNLFGELLIITSLFSWSNFTLPLLGLGFLFTAIYSLYMFVMTQHGKTPNHLL
SLSPSSTREHLLLFLHLFPVILLILNPNLI
>gnl|CDD|164753 MTH00207, ND5, NADH dehydrogenase subunit 5; Provisional
LRMFKPSSIASYLLWFMSILMFPLSLYLMMCNKTILIEWEIFTISSSPINFTIILDPTGTLFSSTVLFIS
ANVLLFAKTYMQEDKFLSRFISLVLLFVLSMNMLIFFPHLMILLLGWDGLGLVSFILVIYYQNPKSLGAG
MITALTNRIGDVMLLLSIGWTLNQGHWSITNMWQTDMNNYIALSIMIAAMTKSAQMPFSSWLPAAMAAPT
PVSALVHSSTLVTAGVFLLIRFYPFLSSTYWFNPALLLTASLTMLMAGLSAMTECDMKKIIALSTLSQLG
VMMASLGLGMPKLALFHLITHALFKALLFVCAGSLIHSHHHSQDLRTMGNLTNQMPLTTSCLLIANLALC
GSPFLSGFYSKDLILESSLFYPHNSLMILMIFLATALTAAYSTRFTLAVLWSPNSSSPYHHLEDEDKSLT
TPMLLLTLGAITSGSALNWWLPTPQEEPILPLQYKLLPLLVVTLGALLAWLFTTPNITKTPLLINNPLSH
FASCLMWFLVPLSSQFIMSTPMNLSHNYLKLLDQGWLEMLGAQGTFKMFSRSSNNVMKLQKNIPNNYLMM
SFVLLTIIIIMT
>gnl|CDD|177251 MTH00208, ND5, NADH dehydrogenase subunit 5; Provisional
MVINPSMIISSINLSIFIILLISIFFSSNLPNISTSNASLGGNNNNNSIINYNNSNFSISLLKTLAFLSL
INLLIWILLGCPNINISLSNWLSNTLFNFSLSFIFDFYFILFFSVALFVTWSIIEFSHYYMSNDPNKNAF
FRLLIIFLLNMLILTSSNNLFLLFIGWEGVGFLSFLLISWWTTRNDANSSALQAVIYNRIGDIGIILFLS
LSLINFNSWNLNEILSLNNSNSFLINILLFGILLAAAGKSAQFGLHPWLPAAMEGPTPVSALLHSSTMVV
AGVFLLIRTSPLISNSPWFLSLCLILGSLTALFAASTAISQHDIKKIIAYSTTSQLGLMVVAIGLNQPNL
ALFHICTHAFFKAMLFLCSGSIIHSLNNEQDLRKMGGLSFLLPVTSSCIILGSLALMGTPFLAGFYSKDL
ILEAGLASISNLLSIILALIATLLTAVYSFRIIFFCFLNNPSFSPLSPISEENPNLTNPLLRLAIGTIIS
GWFFSNFVFNLPPLTLPLILKSLPLIVTIIGAAFSFSFLLSLSSNPINSNFFSFLSNQWFFVNISHSIII
SFSFFTSLFGSTRTLDRGWSENIGPQGIGNTSSTLSKSYQLTQTGYIKQYLLSSTLLFLLILTLSLII
>gnl|CDD|177252 MTH00209, ND5, NADH dehydrogenase subunit 5; Provisional
FKKMQMFSLMLLFLFSFLMFVIFMWFQKIVILEWELLSLNSMSISFPLIIDKMSLLFSSVVLLISGSVMW
FSTSYMAGEKFKKRFILLVLLFILSMNFLIFVPNLITLLLGWDGLGLVSYLLVIYYQNSKSLSAGMLTAL
TNRVGDALLILSIAWMLMHGNWNIFYLNFNSNLGSVISVLIVLAAMTKSAQIPFSAWLPAAMAAPTPVSA
LVHSSTLVTAGVYLLIRFFPSLFSSPFFSMSLLLLGSLTTLMASMSANVESDLKKIIALSTLSQLGLMMC
SLGLNQPELAFFHLITHALFKALLFICAGNIIHSHGHSQDIRMVGNLWYQMPITSICLNIANLSLCGIPF
LAGFYSKDLILESMLESNMPIMTLILMFLSTSLTAAYSMRLSYFSLWGPNSSKSLNSSFDQNKLNLKPML
VLTLGSITGGSVMSWVMVPSVNSVVLPWFLKLLPIMLILFGVLLMYMVLKKNFFLIKGYKVNYFLSQMWF
LPDLSSQPVNKFTMKLSKTMLKLLDQGWVEKMSGQGSFKVLKKSSKLSQIIQNNSLKLFVTFMMLILLGV
ILFM
>gnl|CDD|177253 MTH00210, ND5, NADH dehydrogenase subunit 5; Provisional
MYILVLFLPLLSAIISGLFGRKIGTKGAGILTSSCIVISAIVSCCIFYETTLNGSATYIKLWRWFDSELL
TTYFGLQFDSLTSTMLIVITSVSALVHIYSTGYMSGDPHIPRFMSYLSLFTFLMIVLVTSDNYVQLFIGW
EGVGLCSYLLINFWLTRIKANKAAIKAMLINRVGDIGLVLAMIMILKEFGTLEFSTISSLLVTNINKESL
TIICLLLFIGAVGKSAQLGLHTWLPDAMEGPTPVSALIHAATMVTAGVFLIIRSGPLFEGSPLALTIVTI
LGALTAFFAATVGVVQNDLKKVIAYSTCSQLGYMVMVCGISNYSTSLFHLMNHAFFKALLFLSAGSVIHA
VSDEQDMRKMGGLIKSIPFTYVMILIGSLSLMGFPYLTGFYSKDLILELTYDKYYIAFAYWLGSFSALLT
AFYSIRLIYLTFITNTNSKKEVFIGVHESSWNITFPLLLLAFGSIFVGYLGKEVVLSNVIPPIVPNSIKM
IPLLFSLLGALLAFVIYNSMVFLIKISRRGVSIRLYHVIYTFLNSAWQFNYVINHFIVKNIWKFGHLITY
RIIDRGLLEIIGPRGISKVLIKLTQKISNLQSGMVFNYALIMIIFTTLFISGAGIE
>gnl|CDD|214459 MTH00211, ND5, NADH dehydrogenase subunit 5; Provisional
MNTIFNSGFLLILILLLLPLLLPLNNSKLHIKKAVKLSFFISLIPLLIFLDQGLETILTNWSWINLGLFS
LNLSFKFDFYSIFFTSVALYVTWSILEFSLWYMSSEPNINRFFKYLLLFLIFMLILVSANNLFQLFIGWE
GVGIMSFLLISWWYGRSDANTAALQAVIYNRIGDIGLLLSMVWLLLNLNSWEISQLFILNLDLTLFLLGL
LLAAMGKSAQFGFHPWLPSAMEGPTPVSALLHSSTMVVAGVFLLIRLSPLFQNNQLILGAVLLLGALTML
FGALCALTQNDIKKIVAFSTTSQLGLMMVTLGLNQPQLAFLHICTHAFFKAMLFMCSGSIIHGLNNEQDI
RKMGGLSKNLPFTSSCLFLGSLALMGFPFLSGFFSKDLILESMNGSYLNAWALLLTLLATSLTAAYSFRL
IFLSLGGYPRFLSLSPINENYKLLKNPLKRLALGSILAGFIITSNLPPEKPEILSLPFLLKLMPLLVTIV
GLLLGLELVNLTHKQLKTSTLSFSNMLGYYPPIIHRLLPKLSLKWGQTLSTHLMDLGWYEKLGPKGLGVN
QKKLIKLVTSPQQGLIKSYLALLLLSLLLILLLFLLF
>gnl|CDD|214460 MTH00212, ND6, NADH dehydrogenase subunit 6; Provisional
MLLSLLLSLLLLLMLLFPLSAHPLTLGVSLLLSSLLSCLIITMESNSWYGYILFLIYIGGLLVLFGYMVA
LSPNEHLFFKKYFKGFGMILISLNLYLLLMTLGSSNFSPMLNLKLELNVSKILSNNNIPILLFLGLILLI
ALLMVVKICQYYKGPLRPFL
>gnl|CDD|177256 MTH00213, ND6, NADH dehydrogenase subunit 6; Provisional
MTIRGGAGPPTSSAVTPTYSHNFLASVFWLILTFIGSSGLFIVLGMEFLGLIFLIVYVGAICIIFLFVIM
MIPGGAKGFKPTKGNKKEKERKKGEETGRIGAPPAIGILIGAILAAELASAVPDSFLNNPSGRGGAERYE
LTNILSDRNRGVSSLLGSDKESITTGIQNNIYMRVGATGAPYLYNDSFFTLNGSGGTNLEAIGSVLYINY
YYAFILVSFILLVAMIGAIVLGLQSSDRN
>gnl|CDD|214461 MTH00214, ND6, NADH dehydrogenase subunit 6; Provisional
MLYFVFLLMFGFLLGLMMVASSPSPYFGALGLVLLALLGCFLLLSHGNSFLGLILFLIYLGGMLVVFSYS
AALAADPYPESWGGWSVLLFFLFYLLGLGFVGFYFYGGWEMLSWMGVDEANNLDLSGVSDLYSRGFFLLL
LGGVVLFLVLFVVLELVRGLSRGALRVV
>gnl|CDD|164761 MTH00216, ND1, NADH dehydrogenase subunit 1; Provisional
MMVFIIFYLIKILIIIVPLLIAVAYLTLAERKVLGYMQARKGPNVVGVYGLLQPFADGVKLFTKEMVIPH
HANLFVYIVAPVLSFTLALIVWGVIPYERGVLISDFKIGILYILAISSISVYAILMSGWGSNSKYAFLGA
IRAAAQMISYEVSIGLIIISVLLCVGSLSITEIVLAQNNGIWFFFPLFPVAIMFFASALAETNRAPFDLT
EGESELVSGYNVEYASMSFALFFLAEYAHIILMSCLTTILFLGGWLSPIKYFKGGAGWFGLKVVFIIFLF
IWVRASFPRIRYDQLMALLWKSYLPLSLGVVIFVASVLFGFNGPPPI
>gnl|CDD|214462 MTH00217, ND4, NADH dehydrogenase subunit 4; Provisional
MLELVFILPLIGILHLLIIPRDNIVRLKKIALEWSLLTLTATILLWASFDGEGQFQAIKKFEWIPGIEPV
FGPVVFAVDGISIFFLILTALLTPICILISWNSIKFLIKEFLLCLLVIEILLMGVFTILDLVGFYILFEG
ILIPMFLIIGIWGSREEKVQASYYFFFYTFIGSVFMLLGIFTLYSYAGTTDYQALCCLKIEKELQYFIFL
GFFLSLAIKIPKIPFHIWLPQAHVEAPVAGSVILAGVLLKLGGYGFIRFSWPLLPEASEYFSPLIQTLSL
LAIIYGSLTTCRQVDLKRIIAYSSVAHMGLVTLGIFSHTIQGLVAAIFLMLAHGLVSSALFIAVTFLYER
HHTRLIKYYRGMVITMPLFGILMLLLVLANASIPLSCNFVGEFLSLLAAFEYSYIVGVLASLGMVLSAGY
SIYLYNRVCFGAPSKYLYFSRDLNRREFYVLLPLVFLIYLMGIFPFIIIDVIKSSVIFQEWY
>gnl|CDD|214463 MTH00218, ND1, NADH dehydrogenase subunit 1; Provisional
MLLSLINLLLYILPVLLAVAFLTLLERKVLGYMQLRKGPNVVGPYGLLQPIADGVKLFIKEPIRPSTSSP
FLFLLAPILALTLALLLWMPLPLPFSLINLNLGVLFILAISSLGVYSILWSGWASNSKYALMGALRAVAQ
TISYEVSLGLIILSLIILTGGFSLEGFNLTQETIWLLIPEWPLALMWFISTLAETNRAPFDLTEGESELV
SGFNVEYSGGPFALFFLAEYMNILFMNTLSVILFLGTSLTTINLMLKATLLVFLFLWVRASLPRFRYDQL
MHLAWKNFLPLSLALLLLHTSLPLSFASLPP
>gnl|CDD|214464 MTH00219, COX3, cytochrome c oxidase subunit III; Provisional
MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMG
LHTSKVSTGLRIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLA
SGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVI
IGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS
>gnl|CDD|164765 MTH00222, ATP9, ATP synthase F0 subunit 9; Provisional
ATEILTAAKFVGAGAATIGAAGSGAGIGTVFGNLIIGYARNPSLKQQLFTYAILGFAISEAMGLFCLMMA
FLILFAL
>gnl|CDD|177260 MTH00223, COX1, cytochrome c oxidase subunit I; Provisional
MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPM
MIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSV
DLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDR
NFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVL
GFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGL
TGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNL
TFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLE
WDNLLPADFHNNSETGALVINP
>gnl|CDD|164767 MTH00224, CYTB, cytochrome b; Provisional
MFKPFRTTHPAIKILNGSLIDLPAPNNISIWWNYGSLLGLCLVIQVLTGLFLSMHYAPNIEMAFSSVAHI
SRDVNYGWLLRSIHANGASMFFLFIYLHVGRGLYYGSFNLSETWNIGVILFILTMATAFLGYVLPWGQMS
FWGATVITNLFSAIPYIGKDLVEWIWGGFAVDNATLNRFFSFHFLLPFAIMGATILHIMFLHQTGSNNPI
GINADSARIPFHPYYSIKDALGYLIAILLLSLMVLFEPNLFTDPENFLMANPLVTPIHIKPEWYFLWMYA
ILRSIPNKLGGVVALFAAILILFILPLTSVMNKRSLPFYPLNQLLFWLLVTSWAILTWIGGRPVEDPFEG
IGQVFTILYFSYFIISPAISKLWDDLLNA
>gnl|CDD|214465 MTH00225, ND1, NADH dehydrogenase subunit 1; Provisional
MSFLLKFLIMLICLLLSVAFYTLLERKVLGYIQLRKGPNKVGLMGLPQPFADALKLFTKEQTKPQLSNKL
PYYIAPILSLILSLILWSLYPSMFSIYSFKFGILFFLCISSLNVYTILLAGWSSNSKYALLGALRAVAQT
ISYEVSMALILLSIVFLVLTYNLFDFSYNQKYFWFMFVLFPLFFCWMISMLAETNRAPFDFAEGESELVS
GFNIEYSSGGFALIFMAEYGSILFMSMLTSILFFGGFFVTIDLFLILKIMLLAFWFIWVRGVLPRMRYDK
LMSLTWKSFLPLSLAYLFMVLIILM
>gnl|CDD|214466 MTH00226, ND4, NADH dehydrogenase subunit 4; Provisional
MNWVLSSLLFLPPLMGVFHLLTAGNIRGSIRGPTARIPSGTSSLKRIALFWSFISLISTIILWLSLDQEG
GFTPLMDIDWIEGPEKIIPIIMGGPLVFAVDGISIYFIILTGFIVPCSILISWHSVKYLTKSFLICMLIL
EFLLYAVFSVLDIFMFYILFEGVLIPMYLILGIWGSREEKMQAAYYFFFYTLIGSVLMLLCLFSLYNIHG
TTDYLTLASCSHVVSEQTQKWIFLGIFLAMAVKIPIFPFHIWLPKAHVEAPVAGSVLLAGILLKLGGYGL
VRLSWPILPLGAQNLAPAVIAMGIVGIVYGSFATCRQIDVKRLVAYSSVAHMGLVSITLVTHDIIGLTGS
IFIMLAHGIVSSLLFILVTILYDRHHTRLIKYYRGLSITMPIWGTIMIVTSLANVAVPPSGNFIGEYLSI
LSSFNWNPIIGVFVCSGVILSAVYSFYFANRVTFGAPGNLITFARDVNRREFYITASMVFFAFLIGIYPI
FILEVIQNSLFFLAL
>gnl|CDD|164770 MTH00260, ATP8, ATP synthase F0 subunit 8; Provisional
MPHLSPMSWLTAMIIFWFILLIFASSMWWSQSPKFPASSTKSALPSLSQWNWS
>gnl|CDD|177263 MTH00261, ATP8, ATP synthase F0 subunit 8; Provisional
MSQLDLSLYFNHYFVLLLLFFILIILISIKFYNFFLVLNIRNNFICNSLELIIINFKQFSILQNILKL
>gnl|CDD|411074 NF000031, MFS_efflux_LmrA, lincomycin efflux MFS transporter Lmr(A)
MSVFARATSLFSRAARTRAADEAARSRSRWVTLVFLAVLQLLIAVDVTVVNIALPAIRDSFHVDTRQLTW
VVTGYTVVGGGLLMVGGRIADLFGRRRTLLFGAFLFGASSLAAGLAPNLELLVLARFGQGAGEALSLPAA
MSLIALLFPETAARSKALSVWASVASVGLVLGFLLSGVITQLFSWRWIFLINIPLVSLVLVAVLLLVKKD
ETTARNPVDLPGALLFTAAPLLLIFGVIELGEDEPRLPLAVGSLLAAAVCAAAFVAVERRTAHPLVPLTF
FGNRVRLVANGATVLLSAALSTSFFLLTMHLQEERDLSPIEAGLSFLPLALSLILASLLVPRLIERIGTT
GAAVLGMALAALGIGCFALLPSDNSLLTSVFPGMILLACGMATGLVALQNAALHAVTEADAGVASGVQRC
ADQLGGASGIAVYVSIGFSPHLGGDWDPFTVAYSLAGIGLIAAVLAVLALSPDRRLAAPREQED
>gnl|CDD|439388 NF000040, Tn10_TetC, tetracyline resistance-associated transcriptional repressor TetC. TetC, as found in composite transposon Tn10, is a transcriptional repressor of itself and of TetD, which is a transcriptional activator for some stress response proteins in the SoxS/MarA/Rob regulon in E. coli and which therefore contributes to antibiotic resistance
MELKLHQPEHFDSINILLVCSAKIIFEEKGHQAENFDEISGKALNSAGAFFHEFGNKAQLIDACSGKALI
MIDAFIHHFKDKKNGLSACEKIFEHMIDAIIDNKKDLINGQEALEIIFEHELDKIIDENINGIPIAEVMK
IIGENELEAIDDDVIKGKLNAIFMHIAIEAKLKAEDADKKGNFIAGWFGFIAIHADK
>gnl|CDD|411076 NF000058, Erm41, 23S rRNA (adenine(2058)-N(6))-methyltransferase Erm(41)
MSGQRSRRQWGWYPLTDDWAARIVAESGVRSGEFVVDLGAGHGALTAHLVAAGARVLAVELHPGRARHLR
SRFAEEDVRVAEADLLAFRWPRRPFRVVASPPYQVTSALIRSLLTPESRLLAADLVLQRGAVHKHAKRAL
VRHWTLRAGITLPRSAFHHPPQVDSSVLVIRRR
>gnl|CDD|411077 NF000060, MFS_efflux_LmrB, lincomycin efflux MFS transporter Lmr(B). The lin-2 mutant, described in PMID:12499232, alters Lmr(B) expression in Bacillus subtilis and allows Lmr(B) to confer resistance to lincomycin
MILETTAKASQQYKVMPIMISLLLAGFIGMFSETALNIALTDLMKELNITAATVQWLTTGYLLVLGILVP
VSGLLLQWFTTRQLFTVSLIFSILGTFIAALAPSFSFLLAARIVQALGTGLLLPLMFNTILVIFPPHKRG
AAMGTIGLVIMFAPAIGPTFSGLVLEHLNWHWIFWISLPFLVLALVFGIAYMQNVSETTKPKIDVLSIIL
STIGFGGIVFGFSNAGEGSGGWSSPTVIVSLIVGVVGLILFSIRQLTMKQPMMNLRAFKYPMFILGVIMV
FICMMVILSSMLLLPMYLQGGLVLTAFASGLVLLPGGILNGFMSPVTGRLFDKYGPKWLVIPGFVIVTVV
LWFFSNVTTTSTAVLIIILHTCLMIGISMIMMPAQTNGLNQLPREFYPDGTAIMNTLQQMAGAIGTAVAV
SIMAAGQHDYMSTVKNPADPAVIPQALTAGVQHAFVFAMIVAIIGLIGAFFMKRVKVDH
>gnl|CDD|411078 NF000106, 40850658_otr, oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit
MTRKTISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGPXGAAXXRGALPAHVXGPDAGRRP
WRFXTWCANRRALRRTIGXHRPVRXGRRESFSGRENLYMIGRXLDLSRKDARARADELLERFSLTEAAGR
AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQL
AHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHAAELDRMVGAIAQAGLDGIAGATADHEDGVVNVP
IVSDEQLSAVVGMLGERGFTISGHQHPSAQLXEVFLAITGQKTSEAADGGPQDGPQDQQGVQDKQYEEVP
A
>gnl|CDD|439389 NF000124, fos-Vibrio, FosG/FosC2-related fosfomycin resistance glutathione transferase
MILGLNHITIAVSDLERSLKFYRETLGFTAHAKWDNGAYLSVGELWFCLSHDEPCPKTDYTHVAFDIEPK
EFEAFAKRVVSLGVEVWKQNKSEGQSLYILDPDGHKLEIHSGSLKSRLESLRTKLYSGLVWL
>gnl|CDD|411079 NF000140, AAC_6p_Salmo, AAC(6')-Iy/Iaa family aminoglycoside 6'-N-acetyltransferase. Members of this family are chromosomal acetyltransferases from the genus Salmonella. Analysis has demonstrated a case in which a member designated AAC(6')-Iy, identical in two different strains isolated from a single patient, conferred resistance to tobramycin only in the isolate where a deletion event upstream of the gene resulted in high expression. Members of this family are therefore considered cryptic aminoglycoside N-acetyltransferases. which may or may not confer resistance, depending on expression levels
MDIRQMNKTHLEHWRGLRKQLWPGHPDDAHLADGEEILQADHLASFIAMADGVAIGFADASIRHDYVNGC
DSSPVAFLEGIFVLPSFRQRGVAKQLIAAVQRWGTNKGCREMASDTSPENTISQKVHQALGFEETERVIF
YRKRC
>gnl|CDD|411080 NF000217, MATE_multi_FepA, multidrug efflux MATE transporter FepA
MAKNMEILETDSVKKIYFRYLIPSLVGMLLMSLNIVIDGIFVGHKLGGVALAGINIAVPVFTIFTAISIW
IGIGAATQFSFAIGEKNVAKAQTIFTNAILAVVSITVIIGIIAFIFKVPLAYFLGANDDTIGYVLEYMNI
LLVFGFALTLENILSIFVRNDGDPNLSMIALIVTAISNVILNYLFLFVFEWGVTGSALATMIAIIIGVLI
LITHFFKKSSRLKFVKVDWNKAFFKKTLAIGLPSFLAEVGVSVFTLGYNISIAAIAGTAGVAAFSVLNYT
HSVILMLFLGMGSAIQPLISYYRGAKARQKEIETLKIAIMVAFSTGVGFLLVGLFGSNLLVSMFGNFSPE
IKDLASNGIKLFYTAYLFMGFNFVMMTYFQTSDKVKMATWITISREIIFMVIFLLVLPPIIGIPGVWLAI
PISEMIVAASIIFYMKKKHILFK
>gnl|CDD|439391 NF000342, glpA_Cterm, aminoglycoside O-phosphotransferase APH(4)-Ib. The C-terminal half of CAA52372.1 shows homology to hygromycin-modifying enzyme APH(4)-Ia. The N-terminal region shows no homology to any other protein. The gene glpA was identified as one of two in a 3.0-kb DNA segment capable of conferring on E. coli the ability to degrade and use the phosphonate herbicide glyphosate as a sole carbon source. The expressed protein conferred minor (3-fold) increase in tolerance to hygromycin, but this protein probably should not be considered an aminoglycoside modifying enzyme associated with the spread of resistance in bacteria toward clinically important antimicrobials
LIEAFDGKMGHDEAPANADAHKPRGEDALDNIKDSLGGSEAGLFFAECNFALIPAALPCGELLDIGEFNG
KQPLFAACFAARELDFPALEKMAQHQKCCGLAHAIAAADLAHSSGFAPFCPCAAGQETMRNDGRDCIEDL
QCWSDLSHKGDSLLASTAPGFEKFLLGAEDCAEAEHGGIHRKGDNAALLEPALIEAADDGMQASGAGRLG
PTPDPRGPDALGFITDPR
>gnl|CDD|411082 NF000349, mfpA_AE000516.2, pentapeptide repeat protein MfpA
MQQWVDCEFTGRDFRDEDLSRLHTERAMFSECDFSGVNLAESQHRGSAFRNCTFERTTLWHSTFAQCSML
GSVFVACRLRPLTLDDVDFTLAVLGGNDLRGLNLTGCRLRETSLVDTDLRKCVLRGADLSGARTTGARLD
DADLRGATVDPVLWRTASLVGARVDVDQAVAFAAAHGLCLAGG
>gnl|CDD|411083 NF000391, EmrB, multidrug efflux MFS transporter permease subunit EmrB
RKPLEGAQLAWMTIALSLATFMQVLDSTIANVAIPTIAGNLGASNSQGTWVITSFGVANAISIPITGWLA
KRIGEVKLFLWSTALFALASWLCGISNSLGMLIFFRVIQGLVAGPLIPLSQSLLLNNYPPAKRSMALALW
SMTVIVAPICGPILGGYISDNYHWGWIFFINVPIGIAVVLLTLQTLRGRETKTEIRPIDTVGLVLLVVGI
GSLQIMLDQGKELDWFNSTEIIVLTVVAVVALSFLIVWELTDDHPIVDLSLFKSRNFTIGCLCISLAYML
YFGAIVLLPQLLQEVYGYTATWAGLASAPVGLIPVLLSPIIGRFGHKLDMRRLVTFSFIMYAVCFYWRAY
TFEPGMDFGASAWPQFIQGFAVACFFMPLTTITLSGLPPERMAAASSLSNFTRTLAGSIGTSITTTLWTQ
RESMHHSQLTESINPYNPNAQQMYQQLEQLGMSQQQASAYIAQQITNQGLIISANEIFWLSAGVFLILLV
LVWFAKPPFSA
>gnl|CDD|467948 NF000535, MSCRAMM_SdrC, MSCRAMM family adhesin SdrC. Features of this protein family include a YSIRK-type signal peptide at the N-terminus and a variable-length C-terminal region of Ser-Asp (SD) repeats followed by an LPXTG motif for surface immobilization by sortase
MNNKKTATNRKGMIPNRLNKFSIRKYSVGTASILVGTTLIFGLSGHEAKAAEHTNGELNQSKNETTAPSE
NKTTEKVDSRQLNNNTQTTTSDQPKVTMSDSASVKETSSNMQSPQNATATQSTTQTSNVTTNDKSSTTYS
NETDKSNLTQAKDVSTTPKTTTIKPRTLNRMAVNTVAAPQQGTNVNDKVHFSNIDIAIDKGHVNKTTGKT
EFWATSSDVLKLKANYTIDDSVKEGDTFTFKYGQYFRPGSVRLPSQTQNLYNAQGNIIAKGIYDSTTNTT
TYTFTNYVDQYTNVSGSFEQVAFAKRENATTDKTAYKMEVTLGNDTYSEEVIVDYGNKKAQPLISSTNYI
NNEDLSRNMTAYVNQPKNTYTKQTFVTNLTGYKFNPNAKNFKIYEVTDQNQFVDSFTPDTSKLKDVTDQF
DITYSNDNKTATVDLMKGQTSSNKQYIIQQVAYPDNSSTDNGKIDYTLDTDKTKYSWSNSYSNVNGSSTA
NGDQKKYNLGDYVWEDTNKDGKQDANEKGIKGVYVILKDSNGKELDRTTTDENGKYQFTGLSNGTYSVEF
STPAGYTPTTANAGTDDAVDSDGLTTTGVIKDADNMTLDSGFYKTPKYSLGDYVWYDSNKDGKQDSTEKG
IKGVKVTLQNEKGEVIGTTETDENGKYRFDNLDSGKYKVIFEKPAGLTQTGTNTTEDDKDADGGEVDVTI
TDHDDFTLDNGYYEEETSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS
DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS
DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDAGKHTPA
KPMSTVKDHHNKAKALPETGSENNGSNNATLFGGLFAALGSLLLFGRRKKQNK
>gnl|CDD|333720 NF000536, YmiA, YmiA family putative membrane protein
MPSGSDKPQRDPALKRKAWLAVFLGSALFWVVVALLIWKIWG
>gnl|CDD|333721 NF000537, YncL, stress response membrane protein YncL
MDVSSKTVVLINVLAAVGLLSLLSVRFGWF
>gnl|CDD|333722 NF000539, plantaricin, plantaricin C family lantibiotic. This family describes plantaricin C-like lantibiotic precursors. The seed alignment straddles the cleavage motif (typically GG), and includes both an extended leader peptide region and a Cys-rich core peptide region. Because of the mosaic structure of lantibiotic precursors, this family can be expected to overlap other lantibiotic precursor families in the same clan
WKNPVLRNKESVNEPAGDILEEISEQDLQNIAGGGTATWYVAALSASLGNKGRVCTLTKECQPCC
>gnl|CDD|467949 NF000540, alt_ValS, valine--tRNA ligase
PEKPSLDGLEAKWAARWEEDGTYAFDRPAAREEVFSIDTPPPTVSGSLHVGHVFSYTHTDVVARYQRMRG
KEVFYPMGWDDNGLPTERRVQNYYGVRCDPSLPYDPDFTPPEKPGPKDQVPISRRNFIELCERLTAEDEK
AFEDLWRRLGLSVDWSLTYRTIGDRARRVSQRAFLRNLARGEAYQAEAPTLWDVTFQTAVAQAELEDREY
PGAYHRLAFHGADGGPVHIETTRPELLPACVALVAHPDDERYQPLFGTTVTSPLFGVEVPVLAHPLAEPD
KGSGIAMCCTFGDLTDVTWWRELQLPTRAIIGRDGRLLAETPEWITSEAGRAAYAELAGKTVFSAREAVV
ELLRESGDLDGEPRPIQHPVKFYEKGDKPLEIVSTRQWYIRNGGRDADLREALLARGRELAWHPEHMRVR
YENWVEGLNGDWLISRQRFFGVPFPVWYPLDADGEPDYDAPIVPAEDQLPVDPSSDVPPGYTEDQRGVPG
GFIGDPDVMDTWATSSLTPQIAGGWERDPDLFARVFPMDLRPQGHDIIRTWLFSTVVRAHLEHGSLPWRH
AAISGWILDPDRKKMSKSKGNVVTPTGLLEQHGSDAVRYWAASARPGTDTAFDETQMKVGRRLAIKLLNA
SKFVLGFGAPAGDPAAVTEPLDRAMLAALAEVVEQATAAFEAYDYTRALEVTESFFWTFCDDYLELVKER
AYGADGEAAAASARAALATALSVLLRLFAPFLPFATEEVWSWWQEGSVHRAAWPTADELELPADGDPALL
ALASAALAGIRKAKSEAKVSMRTPVARATVTGPAAQLALLEAAEDDLRAAGRITELV
>gnl|CDD|411084 NF012135, ANT_3pp_9_crypt, aminoglycoside nucleotidyltransferase ANT(3'')/ANT(9). Known members of this family are restricted to Salmonella enterica. Activities as both a streptomycin 3''-O-adenylyltransferase and a spectinomycin 9-O-adenylyltransferase are cryptic because of a lack of expression, but detected if cells are grown on miminal rather than rich media (see PMID:21507083)
MTLSIPPSIQCQTDAACRLITRVTGDTLRAIHLYGSAVAGGLKPNSDIDLLVTICQPLTEAQRATLMQEL
LALSSPPGASAEKRALEVTVVLYSQLVPWCFPPSREMQFGEWLREDICQGIYEPAQQDWDIVLLITQILE
TSIPLKGERAERLFTPAPAAQLLKALRYPLDLWQSTADVQGDEYHIVLTLARIWYTLSTGRFTSKDAAAD
WLLPQLPEDYAATLRAAQREYLGLEQQDWHILLPAVVRFVDFAKAHIPTQFT
>gnl|CDD|333724 NF012136, SecA2_Lm, accessory Sec system translocase SecA2. Members of this family are SecA2, part of a Sec-like preprotein translocase called accessory Sec. This SecA2 family is characteristic of Listeria species
MAQSYDDRKIVKAYREIARQIVKKEGLYRNMDQAELCEQTQIWREKFKTKEMTERDKINIFALVREAARR
IIGLEAVMVQLIGALVLGDGKIAEMKTGEGKTLVSLFVMYIEVLRGNRVHLVTANEYLAKRDREEIGQVL
EYLGVSVALNESGLDKEQKKAIYTADVIYGTASEFGFDYLRDNMVRQTEDKVQTGLDFVLIDEADSILID
EARTPLLISDRKEEDLSLYQVANKLVKTMLKDDYEVEEHKRFVWLNDAGIEKAQRFWGVDSLYSEEAQPL
LRITMLLLRAHFLMHKDKDYVVLDDEVLIIDPHTGRALPGRRFNDGLHQAIEAKEGVEVREESRTLATIT
IQNYFRMYKKISGMTGTAKTEEEEFRQIYNMDVVVIPTNLRVNREDMPDDVFYTKKEKGRAIVYEVSWRY
EKGQPTLIGTSSIKSNEWISELLTKAGIPHQVLNAKNHAQEAEIIARAGKRGMVTLATNMAGRGTDIKLD
KDVHKLGGLAVIGTERHESRRIDLQLMGRSGRRGDPGFSKFMISLEDDLLEQFDSKRWEKYRRKLKRKAP
RDGKPVNSRKIHQLVVEAQKRLEGANYDIRKDLLSYDEVIDLQRKMVYKERDRLLGRDKLGVSSEKILRE
VAEDVFSEREDDQDERMEKYYKRQKELLGGTKFPYSFDQVTLMDPREVVEKLIFWHKKQRAKFPAETINA
IEKEVYLNLMDQMWVMHLDQMVQLREGIHLRAYGQQDPLVMYQKEGAELFEKFQDDYHFYFAHALLELDP
EGLVMG
>gnl|CDD|333725 NF012138, exosort_XrtR, exosortase R
LIALLLAAIGVLLMLNEHTARQLEAEVAAWIANHTFAEDAVPARSAGNPAVAFGVGGEWLALRITIECAI
ALYLGPIAFLAAALTLVPRFRLLRVLLAAAIGVILMILLNQVRLLGLAFALSEGGHDAFSWAHSPGGSFL
MLVGLAGILALFFVIVIRRR
>gnl|CDD|333726 NF012139, exosort_XrtP, exosortase P
MTVAALLAAAVALVLAERAYRTAEITLAGAILRVITSSGVYVAPERQTVYFGLGSDTPLGLRMTPECTSA
FLLLPLLVVTAVMIALRPRIARRVLFALGVAALAVVLVNQLRILTLVGLVNWLGTDEGYYWGHTLLGSMV
SVIGGAAALVLFVWLATRK
>gnl|CDD|411085 NF012144, ramA_TF, RamA family antibiotic efflux transcriptional regulator
TISAQVIDTIVEWIDDNLHQPLRIDDIARHAGYSKWHLQRLFLQYKGESLGRYIRERKLLLAARDLRDTD
QKVYDICLKYGFDSQQTFTRIFTRTFNQPPGAYRKENH
>gnl|CDD|467950 NF012162, surf_Nterm_1, surface-anchored protein thioester-forming domain. This model describes a conserved region, fairly rich in insertions and deletions, located just past the signal peptide region in long, variable, and typically highly repetitive and sortase-dependent surface proteins. Members are found in a broad range of taxa, including many strains of Streptococcus pneumoniae. A conserved Cys forms a thioester bond, often to a host protein for covalent attachment
ILTLVVVFLMLLALAGSIIFGSLAYAADEKGFPNDAKGVSPEGKYYGYDKYGKLYTTYHRLRVVENLEGS
DDYQAFCFNLKKKFPSYDDSSVKKWYKKLLGSDKETFKKYARDPRRDGTISNPNELWDKLRKVIYNGYPK
DPTDIMGRSGLTPLNFINVTQNAIWYYTDGSKVSKDDNSYEYEAQNSQSQEQLELMREALKKLIDPNSDF
ELRIYKPQDVGGQKGYQALLSGRL
>gnl|CDD|411086 NF012163, BaeS_SmeS, sensor histidine kinase efflux regulator BaeS
LRPGITGKLFLAIFATCLLLLIVMHWAVRVSFQRGFIDYIKDGNEQRLQRLSDALGEQYAQHGNWRFLRN
NGDRWVRQLLRTLEHDNDSDKPGPGLPDHLGWRSRLWLVDANHRFVVGPPDPVSDDGTRRPILVNGQEVG
ALGASPVERLTRNTDINFDSQQKRASWLIVALALLLAALAAFLLARGLLAPVKRLVEATHRLAAGDYTTR
VTPTSNDELGKLAQDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAIQDGIRKFTPESLDSL
QAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSSLVFGDR
DRLMQLFNNLLENSLRYTDSGGSLHISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASG
GSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP
>gnl|CDD|333728 NF012164, AlbA, subtilosin maturase AlbA. AlbA is a radical SAM/SPASM domain-containing protein responsible for introducing thioether crosslinks during that maturation of bacteriocins such subtilosin A
FPFINESVRVHQLPEGGVLEIDYLRDNVSISDFEYLDLNKTAYELCMRMDGQKTAEQILAEQCAVYDESP
EDHKDWYYDMLNMLLNKQVIQLENQASRHTITTSGSNEFPMPLHATFELTHRCNLKCAHCYLESSPEALG
TVSIEQFKKTADMLFDNGVLTCEITGGEIFVHPNANEILDYVCKKFKKVAVLTNGTLMRKESLELLKAYK
QKIIVGISLDSVNSEVHDSFRGRKGSFAQTCKTIKLLSDHGIFVRVAMSVFEKNMWEIHDMAQKVRDLGA
KAFSYNWVDDFGRGRDIVHPTKDAEQHRKFMEYEQNVIDEFKDLIPIIPYERKRAANCGAGWKSIVISPF
GEVRPCALFPKEFSLGNIFHDSYESIFNSPLVHKLWQAQAPRFSEHCMKDKCPFSGYCGGCYLKGLNSNK
YHRKNICSWAKNEQLEDVVQLI
>gnl|CDD|411087 NF012168, BlaI_of_BCL, penicillinase repressor BlaI
KKIPSISESEWEVMKVLWEKAPQTANEVISSLQEQTDWKPKTIRTLLDRLVKKEVVGVNKDQRVYTFFPL
YSQDECQRAETQSFIKRIYGGTLKSMLVQFIEEESLSEEEIKELRSILDEK
>gnl|CDD|333729 NF012179, CptA, phosphoethanolamine transferase CptA
DWAGLGWLLLFFWYFSGLTQALILLSGTSGFAGFRDALLLSSLWLIPVLLFPRRTRLLAAVIGVVLWAAS
LAALSYFVIYGQEFSQSVIFVMFESNTNEAGEYLSQYFSWWIVLALLAYTAVAILLWTRLRPVYLPRPWR
WPVSVLLLVALIGYPLYKQTVIQHRPFADALEKVESRMEPAVPWQFVVGYRQYRQQLDNMQGLLNSNSAL
PPLANLKDSSGNAPRTLVLVIGESTQRGRMSLYGYPRETTPELDALKASDPNLTVFNNVVTPRPYTIEAL
QQVLTFADEENPDLYLTTPSLMNMMKQAGYKTFWITNQQTMTKRNTMLTTFSQQTDEQVYLNNQRNQNAR
QYDGNVLAPFKKALADPAPKKFIVVHLLGTHMKYQYRYPEDYDKFTGRTQGVPAGLSDDQLETYNSYDNA
VLYNDFVVSSLIKDYAATDPNGFLLYLSDHGEDVYDSPPHDTLGRNEGKPTRPMYTIPFLLWTSPKWQAA
HPRDFSADVNRPYSSSHLIHTWSDLAGLSYDGYDPTKSLVSPQFKARPRWIGNPYKKNGLIDFDLL
>gnl|CDD|467951 NF012181, MSCRAMM_SdrD, MSCRAMM family adhesin SdrD. Features of this protein family include a YSIRK-type signal peptide at the N-terminus and a variable-length C-terminal region of Ser-Asp (SD) repeats followed by an LPXTG motif for surface immobilization by sortase
MLNRENKTAITRKGMVSNRLNKFSIRKYTVGTASILVGTTLIFGLGNQEAKAAESTNKELNEATTSASDN
QSSSKVDNQQLNQEDNTKNDNQKEMVSSQGNETTSNGNKSIEKESVQSTTGNKVEVSTAKSDEQASPKST
NEDLNTKQTISNQEALQPDLQENKSVVNVQPTNEENKKVDAKTESTTLNVKSDAIKSNAETLVDNNSNSN
NENNADIILPKSTAPKRLNTRMRMAAVQPSSTDSKNVNDLITSNTTLTVVDADKNNKIVPAQDYLSLKSQ
ITVDDKVKSGDYFTIKYSDTVQVYGLNPEDIKNIGDIKDPNNGETIATAKHDTANNLITYTFTDYVDRFN
SVQMGINYSIYMDADTIPVSKNDVEFNVTIGNTTTKTTANIQYPDYVSRDNNSIGSAFTETVSHAGNAED
PGYYKQTVYVNPSEKSLTNAKLKVEAYHKDYPDNVGQINKDVTKIKIYQAPKDYVLNKGYDVNTNQLIDV
TEQFKDKITYGANDSVNVDFGSINNSYVVMVDTKFEYTTSESPTLVQMATLSSDGNKSVSTGNALGFTNN
QSGGAGQEVYKIGNYVWEDTNKNGVQELGEVGVKGVTVVVYDNKTNKEVGRTITDEKGGYLIPNLPNGDY
RVEFSNLPQGYEVTPSKQGNNEELDSNGVSSVITVNGKDNLSADLGIYKPKYNLGDYVWEDTNKNGIQDQ
DEKGISGVTVTLKDENGNVLKTVTTDADGKYKFTDLDNGNYKVEFTTPEGYTPTTVTSGSDIEKDSNGLT
TTGVINGADNMTLDSGFYKTPKYNLGNYVWEDTNKDGKQDSTEKGISGVTVTLKNENGEVLQTTKTDKDG
KYQFTGLENGTYKVEFETPSGYTPTQVGSGTDEGIDSNGTSTTGVIKDKDNDTIDSGFYKPTYNLGDYVW
EDTNKNGVQDKDEKGISGVTVTLKDENDKVLKTVTTDENGKYQFTDLNNGTYKVEFETPSGYTPTSVTSG
NDTEKDSNGLTTTGVIKDADNMTLDSGFYKTPKYSLGDYVWYDSNKDGKQDSTEKGIKDVKVTLLNEKGE
VIGTTKTDENGKYRFDNLDSGKYKVIFEKPAGLTQTGTNTTEDDKDADGGEVDVTITDHDDFTLDNGYFE
EETSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS
DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS
DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDAGKHTPVKPMS
TTKDHHNKAKALPETGSENNGSNNATLFGGLFAALGSLLLFGRRKKQNK
>gnl|CDD|333731 NF012182, exosortase_XrtQ, exosortase Q
LDALPAWAWLALQAAALWPTWRWMAARMADGSDDPLGLLALAALALLLWRDRRRLRAAPRLGWLALALVG
TLAATLLRAGLPPLAAALLAVLALAAGLLAFLPPGQAALPVLGLAVLALPLLSSLQFYAGYPLRVVTAEA
SRWLLRALGFAVEREGSALVVDGQLVIVDAPCSGVQMVWLGYFTACAVALWLGLRDRQFLRRLPWVGLLV
LAGNVLRNTLLVALEAAGNPLPAWAHEAIGLAVLAAVCGGVARLMA
>gnl|CDD|467952 NF012196, Ig_like_ice, Ig-like domain. This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein
VTSHDAAGNTATATAHHTVTIDTHADATITIDTVTGDNVLNAAESQQPTTTITGTVGGDVKVGDPVTLTV
NGHTYTGTVVDLGNGQLGYSVDVDTSDLLNNPNDVTAT
>gnl|CDD|467953 NF012197, lonely_Cys, lonely Cys domain. This model describes an unusual domain, over 700 amino acids long, that is largely restricted to the Streptomyces (prodigious producers of natural products) and that may occur ten or more times in giant proteins. The most striking feature is an extremely low cysteine composition, one residue per domain, and that in an essentially invariant position
LARLDALRRADPALRGGPLDLDALARRVLHLDPDAPVTAAERAELYRLVGDAAAAGRATSLAALAAFHLV
RRGVLAPDRFRTTGAGGRVPGLNWTGTPVPADLDTTTVGLLVRDPDGTPGPGGPRPAPWRGGPTPYVVAA
DGGHDHVTVRGPDGTTRDVPIEVFVELLALDPELAGLPPDVPVVLAVPFAGDRGLDLPRALADRTGRTVW
AHSGEVRLGLPPDPGRSVIGVLHREGRPRGDWIPSDPGLVPDPLDDGADWERDVVSRPIVSADTRRQIGR
ALFHDADLARRREETYRRLDRMTEYVHYNPATGTYSAPRPLPWPAGGPRAYFLAGHGGPGSTSWALRDGS
TRRADGRETGRWLARRPSLASLPKDHWIVLLVCWSGAPPGRGGVPGLGRAGPPPFVPDPLADVSVGQHVA
NETRRTVRASTSVQGARDHDGEPVRVLYTDARGRRGRWVEFRPEPEGAELDRRARAAGLHTGPGPVPEEV
RERTLRLVRALRLTFGPDVDDDPDYPELLRGAGALERMRRADPRLRGAGPFTLDLFERVVAAHLPEGAAG
PDRAAYRAVLAAAAAAWAAGPGTPLSDFVTLPALDRAAAWLAATPDVDAEAADALGLPGPAPVGEAERSR
MFWARVKAEELLRAVGPDLDALAARVLHLPAPDPARRDEALDLVTRAFAAGRDPADPDELAAYHLERRGA
LSDATL
>gnl|CDD|411088 NF012198, MarA_TF, MDR efflux pump AcrAB transcriptional activator MarA
MSRRNTDAITIHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKL
KESNEPILYLAERYGFESQQTLTRTFKNYFDVPPHKYRITNMPGESRYLHPLNH
>gnl|CDD|467954 NF012200, choice_anch_D, choice-of-anchor D domain. This HMM describes a repeat domain just over 100 amino acids long and usually found in tandem copies. Members appear to be extracellular proteins that have some C-terminal anchoring domain, such as type IX secrection (T9SS) or PEP-CTERM
QTVALTGNGVAAADPSITPSPASIDFGNVRVGDTASQTVTITNTGTAALTIEGLTISGTNAGDFTVSGNS
PTTLAAGGSCTLTVTFDPTAAGARSGTLTIASNDAGE
>gnl|CDD|333735 NF012201, WIAG-tail, WIAG-tail domain. This 80-amino acid domain occurs in proteins in a single copy at the C-terminus. In most proteins, the domain immediately follows a long, variable run of tandem 10-amino acid repeats. The domain is named for its C-terminal motif, WIAxGx, hence the name WIAG-tail
LQQFGLTPFRFPAQEESVEVTIRFDEPFADTNYVLVAMTNHPGCYASLKSKTRESAVITVVRTRGGPEPY
GVLNWIAIGE
>gnl|CDD|467955 NF012204, adhes_FxxPxG, leukotoxin LktA family filamentous adhesin N-terminal domain. This model, related to TIGR01901, describes a conserved single-copy N-terminal domain found in repeat-rich, extremely long proteins such as the leukotoxin LktA of Fusobacterium necrophorum
TDITTDTVSGDVGFNSFDNFNLGAGNTANLHFPAGTSNLVNLVDDKVVINGILNAYRNGKIGGNLYFASP
HGFVVGASGVINVGSLTVITPTQDFYDKLLGDDGVPNAGAVAKLLAGDVPLSPDGTITIDGKINAVDGVT
LAGANISVGGGA
>gnl|CDD|333737 NF012206, LktA_tand_53, leukotoxin LktA-type filamentous protein tandem repeat. This repeat, about 53 amino acids in length, may comprise most of the length of proteins over 3000 amino acids long. The best characterized protein with this repeat is the leukotoxin LktA of Fusobacterium necrophorum, where it is the major virulence factor
GGVGVGGSVAVNTIDNTTEASIDGSTVTAAGDVTVSAEDDSTIDALAGAAAAA
>gnl|CDD|411089 NF012208, SDR_dihy_bifunc, bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR. Members of this family are SDR family oxidoreductases, unrelated to previously known families of dihydrofolate reductase (DHFR), one of which was demonstrated to be a bifunctional dihydropteridine reductase/dihydrofolate reductase. The DHFR activity can give a heterologously expressed protein the ability to confer resistance to trimethoprim, an inhibitor of most forms of DHFR
ALVTGSARGIGRAIALALAREGFDVAVHYRRSAEAAEQTAQEAEALGVKAITLQADLTDPEQARSLVEEA
AEALGGLSVLVNNVGNYLHKPLLETTDEEWHEMLDSNLNATFYVTQAALPLMRAAGWGRIVNLGYAGAQN
LLARPGITPYVIAKTGVIIYSKALAKELAGDGITVNVVSPGVAENSVSQPLPEIPAGRPATLEELADAVL
FFVRPSSDYITGQVLEVAGGWNL
>gnl|CDD|333738 NF012209, LEPR-8K, LEPR-XLL family repeat protein signature domain. This model, just 24 amino acids long, describes an N-terminal single-copy region that contains the most highly conserved motif in a collection of repeat-filled giant proteins. Member proteins average over 8000 amino acids and include at least one longer than 35,000 in length. The signature motif is LEPRxLL
LLFEALEPRLLLSADPLVAAADLA
>gnl|CDD|467956 NF012210, PDxFFG, PDxFFG domain. This model represents the conserved N-terminal domain of family of large proteins with signal peptides, found in Mycoplasma and Ureaplasma. A short conserved N-terminal domain and a large conserved C-terminal domain are separated by poorly conserved regions of variable length. This domain is named for its best conserved motif, PDxFFG
KKLSLWAKYLISLGSIAAASGITLGSMKLYSKNSDEVLGRKNPTDKSDLKNDFSDIRDEPKLNFLDPDKG
KKVASYDPKGTKFTFVKDPNKKYSYDEFFDKYYEKYNELPILEVKYGSFSFYNEYVEAVSPKEFIEFTKW
FIKNVSWGPDILTLKSFSIVKGVEQNGNSITLGSHSTLNKEETEIKFFPDAFFGSLPIYSELAGRGNAPD
SLTYKLNKKLLTKEELDEFLKNIPLYNALANSSSDTLNKYSFRNILDPRLLKNKKVYVY
>gnl|CDD|333740 NF012211, tand_rpt_95, tandem-95 repeat. This 95-amino acid repeat occurs in tandem in proteins that may be several thousand amino acids long
STDEDGSITITQEQLLANASDVDGDDLTVSNVSYSGPTNGTVTDNGDGTYTYTPNENFNGDDSFTYTVSD
GTGATATATVFVTVNPVNDAPVAGNDAF
>gnl|CDD|467957 NF012221, MARTX_Nterm, MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region. This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains
MGKSFWRSTEYFFTGNYSADDGNNDIVAIGFGGIIHAYGGDDTITVGSIGATVYTGSGNDTVVGGAGYLK
VVDTSGNLTVKGAAGYADINKSGDGNVSFTGAAGGVKIDHTGDHGDINYSGAAAYNGITRKGLSGNVSFE
GAGGYNKLWHETNQGNLSFAGAGAGNKLDRTWFNQYQGSHGDVTFDGAGAANIISSRVESGNITFTGAGA
DNHLIRKGKEGDITLQGAGASNRIERIRNAQDVYSETRGNIRFEGVGGYNSLYSDVAHGDIHFSGAGAYN
EITRKGSGNDSNSEGLEYAKADEIVLTTAYMGGSWIDQSVQVTAIKSTREPNTYLFAFADGMYTKINKVQ
LRNDPETGKLKYYSTSWYKEGNHLSNLAGQDISSGNGFESTPTDGDVNAVKSNRKPNTYIYAKLLGTYTK
IVVVELANDAETGALKYQARAWYKEGDHTANLANEDISESNGYTAMGKGGYSLSDLHYSVNTVRIVSERV
ADIREYSDQELFKSSADSGESSGDINFNGAGGGNVIKSNVTRGNVYFNGAGIANVILHSSQFGNTEFNGA
GAANVIVKKGEEGDLTFRGAGLANVLVHQSKQGKMDVYAGGAANVLVRIGDGQYLAHLLAYGNISVHKGN
GDSRVVMLGGYNTHTQIGNGNGLWLAAGGFNVMTQVGKGDVTSVLAGGANVLTKMGEGDLTSGMLGGANI
ITHISNDEETSNTTAVALGGANILTKKGKGNVLAVMGGGANVLTHIGDGSTTGVMLGGANILTKVGNGDT
TGIMLGLGNVLTHVGNGQTLGVMGAAGNIFTKVGDGTTIAAMIGAGNIFTHVGEGDAWALMGGLGNVFTK
VGNGNALALMVAKANVFTHIGDGMSVALMLAKGNIATKVGNGMTLAAMVGNANIFTHIGHGSTFAAMIGQ
ANILTKVGNDLTAALMVGKANIYTHVGDGTSIGLFAGEANVMTKVGNGTTLAAMFGKANIMTHVGDGLTG
VLALGEANIVTKVGDDFMGVVAAAKANVVTHVGDGTTAAVLAGKGNILTKVGDGTTVGLLISDVGNIMTH
VGDGTTIGFAKGKANIITKVGDGLGVNAAWGKANILTHVGDGDRYNFAKGEANIITKVGDGQEVSVVQGD
ANIITHVGNGDDYTGAWGKANVITKVGDGRNVVLAKGEANIVTQVGDGDSFNALWSKGNIVTKVGDGMQV
TAAKGEANITTTVGDGLSVTATYGDANINTKVGDGVSVNVAWGKYNVNTKVGDGLNVAVMKGKANANIHV
GDGLGINASYARNNVAIKIGNGDFYSLAVASSNTSSNKLSALFDNIKQTVLGVAGSQAINYLVQGDEAST
SGTHKGRGAIALPEVSKLDGFQMNEIDEVGSDLGDSLTGSVTQVETPDLNAMQNALNIDESVLSTQAPNL
IVNGDFEQGAEGWNSTYGVEASHSASVYGLRAEGHGARVSELDTYTNTSLYQDLSNLTAGEVIALSFDFA
RRAGLSTNNGIEVLWNGEVVFASSGDASAWQQKTLKLTAKAGSNRLEFKGTGHNDGLGYILDNVVATSES
SQQADAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDA
ILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGLLDRVQEQLDDAKKISGKQLADAKQRH
VDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSR
GEQDASAAENKANQAQADAKGAKQDESDKPNRQGAAGSGLSGKAYSVEGVAEPGSHINPDSPAAADGRFS
EGLTEQEQEALEGATNAVNRLQINAGSR
>gnl|CDD|411090 NF012226, AdeS_HK, two-component sensor histidine kinase AdeS. Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline
KNKSGISKQLFIALSIVNLSVTLFSVFLGYFIYNYAIEVGWITLSSLQEDWTEFHFVDWIWLFTVILCGS
VISLIIGMKLAQRFIVPINFLADAAKKISQGDLSARAEDSQIHSAEISELMHNFNDMAQKLESSVKNAQV
WNAAIAHELRTPITILQGRLQGILDGVFEPDPALFKSLLNQVEGLSHLVEDLRTLSLVENQQLRLNYESV
DLKDSIEKVLKMFEDRLEQAQLTIVLNLTATPVFCDRRRIEQVLIALIDNAIRYANAGKLKISSSVIQDD
WILQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEYSNSQGNSVFTIK
LPA
>gnl|CDD|411091 NF012227, AdeR_RR, efflux system response regulator transcription factor AdeR. This protein, the DNA-binding regulator AdeR, works with its two-component system partner AdeS, to modulate expression of the AdeABC efflux pump
FEASFSFDCRDKQILVVEDEYDIGDIIEHYLKREGMRVIRAMNGKQAIEIHASQPIDLILLDIKLPELNG
WEVLSKIRQKAQTPVIMLTALDQDIDKVMALRIGADDFVVKPFNPNEVVARVQAVLRRTQQNQQASNKNL
IYKNIEINTEIHSVYIHQQDKKQLLNLTLTEYKILLLMIDHPHKVFTRSELMNHCLPDSDALERTVDSHV
SKLRKKLEEHGLQNMLINVRGVGYRLDHP
>gnl|CDD|467958 NF012228, RobA_TF, MDR efflux pump AcrAB transcriptional activator RobA. The original characterization of RobA as a Right side Origin of replication Binding protein A (robA) may be misleading. Characterizations in large numbers of papers since then treat RobA as a transcriptional activator of the AcrAB antibiotic efflux pump
QAGIIRDLLVWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGQAIGAYIRARRLSKAAVALRLTSRP
ILDIALQYRFDSQQTFTRAFKKQFNQTPALYRRSEDWNAFGICPPIRLGKFTLPEPEFVTLPEQHLVGIT
QSYSCTLEQISDFRTEMRVQFWRQYLGNTPTIPPVLYGLHHSRPSKEKDDEQEVLYTTALEPEHAPEGVQ
EGQPVVLEGGEYVQFTYEGPPEGLQDFILTVYGTCMPTLNLTRRKGQDIERFYPHGDKKRDEPPTHIRCE
YLIPIR
>gnl|CDD|333742 NF012230, LWXIA_domain, LWXIA domain. This domain occurs exclusively at the C-terminus of a set of long proteins (average length 4000 residues), and is separated form the rest of the protein sequence by a Pro and Ser-rich spacer region of poorly conserved, low-complexity sequence. This domain is named for its most conserved motif, LWxIA. Some but not all sequences in the seed alignment score well locally to the LysM domain model of PF01476, which may have a general peptidoglycan binding function
TPQPYIVVAGDSLWVIADRHRDSLLDAAHVSDADRQAMSDDQQVAAALREILQLNPNLAANPGHLDPGQP
LIVG
>gnl|CDD|333743 NF028536, PAP2_near_MCR1, PAP2 family protein. Members of this family belong to the PAP2 superfamily (see PF01569). The founding members of this family are notable for being encoded next to mcr-1, a phosphoethanolamine--lipid A transferase that confers resistance to colistin
MPYLSNKRLLAEMSIALVMAIVATLTLEHSQIDLMVADWFYLGIGHWMVAKQAFLPDLLLYSGLKKLLMA
MLIYLLVATICRAYHEKKGNAITAKWLVPVTKFRVRELAYLVLTLILVPTVVASLKAYTHVVCPVHLTIF
DGTLPYLPMLDSMRNTIPDKCFPAAHASSGFALFAFAFAPSLRRRRGAIIIVVMALGWAMGCYKMIIGDH
FLSHTVVSMMLAWAMSAGLAWVFFKKG
>gnl|CDD|467959 NF028538, PAP2_lipid_A, PAP2 family lipid A phosphatase. All members of the seed alignment for this family belong to the PAP2 superfamily and therefore share homology with the lipid A 1-phosphatase LpxE of Helicobacter pylori. LpxE removes one of two KDO sugar phosphates from lipid A, making it possible for a phosphoethanolamine--lipid A transferase to add the modifying group that increases resistance to colistin. All members of the seed alignment for this model are encoded close to the gene for a phosphoethanolamine--lipid A transferase, such as MCR-1
LLLLGLTIVSTLTFEHSQLDVRISQLFYSNGQWLLEKGAQPYRFIFYDLPKALLILLGVYLLIALIIRYW
QRSKSLTIQAPAKFNRPLLPLSKRELGYLLLTLILVPAVIATLKAVTHVSCPNHLTIFGGDLPYLSLWQN
ILAQTPAKCFPAAHASAGFALYAFAFLPRLQRHRWKIIIAVTALGWTMGLYKMLIGDHFFSHTLVSMLLA
WTIAAGLAAVFFRK
>gnl|CDD|467960 NF032891, tail_200_repeat, tandem large repeat. This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species
LPTLTSVTFNPTHQAIGQSVTVTLTFDKAVQEATATLGGVAVTSLTDTADKKVWTGEVVVPASSELTVGL
VVSGYQDLSGNVGEEDTSHSLPITPTITITPIGDVDESEAATVVISGTSTRFEDGQTLTVEVKAQGSETV
EVTGTATVQSDGSWTTNELDLSSWPDGTITVTVTGTNNLGVAAEEASTTFTL
>gnl|CDD|467961 NF032893, tail-700, PLxRFG domain. This domain, nearly 700 residues long, begins with a nearly invariant motif YxPLxRFGx[YF]. It occurs as the extreme C-terminal domain of large size, some over 5000 amino acids long with an average of nearly 3000. The function is unknown
GGYFPLSRFGDYFVDVVDADGERVSFSMFETMAEADRAAEQLRAAFPGAEVTSGTKSQEAFKLRDAISPE
FVADFGEMLGGSGMSQGDAAQDQIFQLYLQSLPDRSARKRFIHRKGVAGFSQDAGRALASFMFHGARQLA
RLRYADELQEALDDIQKEAGELKNQVRAQRVVDELRKRHDWVMNPQESALAQALTSLGFVWYLGGSPAAA
MVNLTQTAQVALPVLSAKGGFAKAAKALLRASGDFVRGKGSIDISTLLNGDEKAALKRAEDDGVIDPTQA
HDLAGQAEGGPGDYRPAWAKVMRKISWGFHHAEVFNREVTFIAAYRLARDAGMDHPTAFEQARKATWDTH
FDYSNANRPRFMQGDVAKVALTFKQYSQNMLYLLFRNAHQALKGETPEERKEARKQLAGALAMLALMGGA
GGLPFVEDIEDLIDGAGMLFGDDDDPWDAETALKEFLADVFGKELAGFILNGVSGLPAPIDISGRIGMGD
LWFRPGTRLLDGKDAYESDLAQALGPVGGLGKNAATGAQKILDGDYARGIETMSPKAVRDLLKAARYATE
GVRDKKGDKVVDDLSLFEAAAQAIGFQPARVAEQYEANSAIKNYERFLNDRRQSLMNAWAMALREKDGEA
VKKVREAIADFNRSNPERPITVETLQQSLRVRQRNSAKAEDGIYLSPKALR
>gnl|CDD|333747 NF033069, acnA_upstr_60, acnA regulatory region 60-length spurious protein. This HMM describes an apparently spurious protein translation from the region upstream of the aconitase A gene acnA in Escherichia coli str. K-12 substr. MG1655, positions 1335595-1335774, and in related strains. Evidence against its expression as a real protein include a putative TTG start codon, the lack of good RBS, non-conservative substitutions where found, the absence of credible homologs in any species besides E. coli, and a DNA region in Salmonella enterica LT2 in which one third of the translation is present, but the other two thirds are missing
MVLDGRVFSVDALLGRTPLDHYSLIPDPAAAGFSFALPQGFSSFINLGCYQIVTRCLCYL
>gnl|CDD|333748 NF033070, rSAM_AprD4, AprD4 family radical SAM diol-dehydratase. AprD4, as described originally in Streptoalloteichus hindustanus, is a radical SAM enzyme involved in C3-deoxygenation of the intermediate paromamine during biosynthesis of the aminoglycoside apramycin. It acts as a diol-dehydratase, and works with the partner protein, AprD3, a reductase
RRMRLGRVLLVSPKTSFGRDLQRTYAGGLGTVCKDEDFLLPPLDLMRLAGVLREAADDIRIVDEEVTGPV
PSLAPGDMVICQVSLPSLREDAERLAEFRAQGARCYAYSSIRSPAQWRELFETGGCEGVLLPESISFARA
ALTGDLTVPGLVTPGTLLDPRHHQPVFGDLAAEPLPARDLVDHTPYMFPPIAGTGITSINGSFGCPYPCR
FYCPYPLSEGRKIRTYPVERIVAEFRQCAELGITAAVFRDPVFSFHRRRTLELCEAVKAAGTGVPWWCET
RIDRLDEEVVAALVDAGCVGVEVGVESGDPRMQATAVRKRLGLDTVRAFHATARQTGLNLVFLFLFGLPG
ETRMSIRRTFDFILELGLADTEFNLSVITPYPGTELHAIALDRGWIDGDQNAFTSHNAVMHTDELSEDDL
EEALAFVDELHAVCGGCAPPEARAEFQSRVHAWSGT
>gnl|CDD|467962 NF033071, SusD, starch-binding outer membrane lipoprotein SusD. SusD (Starch Uptake System D) is an outer membrane lipoprotein that binds starch and participates in a TonB-dependent nutrient uptake complex. Related proteins from similar TonB-dependent complexes that import other, usually multimeric nutrient substrates include RagB and NanU
MKHIYLKTIFAAALITLGMTSCINDLDISSIDPQSSSSFDQMELFAKQYATLGLTGQKGPAGSPDISGQD
EGESGFYRTTFNLQELPTDECIWAWQTDADIPQLTNISWNSSSQRTEWVYQRLGYDITLCNFFLDQTEGK
TDEESLKQRAEVRFLRALHYWYFLDLFGKAPFKEHFNNELPVEKSGKDLYDWIDQELTEIEPDMYEPGQF
NNSAPFGRADKGAAYLLHARLALNAEVYTDGGVADYQKAIDYCDKVINSGAYELCKTAKNGSGYAQLFMA
DNDENPQAMKEIILPIRQDGVKTRSYGGSTYLVCSTRIAGMPYMGTTNGWSCIFARKALVGKFFPNLDDV
PMATEDAPVPATEAEIIALDAQYGVRTKDIIAAAGDDRALFYSGAGGGRRKLTTDKITGFTDGLSIVKWQ
NIRSDGAPTSDTEYPDTDIPLFRLAEAYLTRAEAKFRLGGKQDAWEDINELRNRAGATTILATITEDYIL
DEWAREFYLEGRRRSDLVRFDMFTGNKYLWDWKGGVAEGTSVSSHYNVYPIPADDINNNPNMTQNPGY
>gnl|CDD|333750 NF033072, NanU, SusD family outer membrane lipoprotein NanU. NanU, related to SusD and RagB, is an outer membrane lipoprotein from a TonB-dependent nutrient uptake complex
MKKIFIYLLAGLSLLLFTRCDSLDMEPVSSITDANYWKSEAQFSAFNVGLHALLRERSYNFFLLGEPRAD
IYGDNPFGGEATQGMERLPYNTINKENVGISNFADMYKVINQINLMIAKTNETTLLTEATKNYYLGEAYG
MRAYLYFHLLRSWGDVILYLDYTSGSSLDLSNLSKAASPATEVMEQIKKDIEASEKAFGDDYSFKYGKHY
WSKAATQMLKGEVYLWSGRQMGGGNADYTTAKTALQDVKKADVALQDNFTDVFAYNNKKNKEIIFTIHNG
KDEYSMWGDSYRMNMVPQQAYMTSNYCDENGVSFVETPDAQLNGLIRLQIKKDFYNKLFREGDTRKAGSL
KAVYQKEEDGNLTYVAPIAYKFQGTLLEGSSTRSWLDDYPIYRYADCLLLLAEAKALLGEDPSAEINAVR
ERAYGSEYFEANKAEVAYPNDKGPDFYTDNPFVAGDENAIEAILKERLREFMFEGKRWYDIRLLGWDYVT
KYSTANESRLLWPIDENTLTNNPALKQTPGY
>gnl|CDD|467963 NF033073, LPXTG_double, doubled motif LPXTG anchor domain. This unusual LPXTG-type C-terminal protein sorting domain occurs largely in the genus Clostridium and typically is separated from the main body of the protein by a glycine-rich linker sequence. In this domain, the classical sortase cleavage motif, LPXTG, has the consensus sequence VPLAxLPKTG. Much of this motif, the sequence VPLAxLP, is repeated an average 20 amino acids upstream within this domain. This unusual structure of a sortase recognition site-containing domain suggest a specialized form of interaction with its cognate sortase
VTIEPEDVPLAPLPGSPDDLITIDDGEVPLAPLPKTGDRSPAATLTMLLSGILLALYAALSKKKKE
>gnl|CDD|467964 NF033092, HK_WalK, cell wall metabolism sensor histidine kinase WalK. This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR
FFRSIHFKIVLIYVLLILIAMQIIGVYFVRQLETQLLNNFKESINLRANLLSYNLEQELSKEDEDDETLE
EDIRTILNDFNNNDISEIQVIDAKGTILGTSDPSNQSIVGQKTTDSDVKRALLGGKDNEKILIDPEDNNR
VYVLATPIKSSNGEVVGAIYIEASMESVYDQMNNINLIFATGTLIALVITAVLGILLARTITRPIKEMRK
QALAMAKGDFSRKVKVYGNDEIGQLAEAFNNLTKRLQEAQATTESERRKLDSVLSHMTDGVIATDRRGRV
ILINDPALEMLNVSRETVLGQSILDVLGLEEEYTLRDLLEEQDSLLLDFSTEEEPLILRANFSVIQRESG
FINGLIAVLHDVTEQEKIEQERREFVANVSHELRTPLTTMRSYLEALADGAWKDPELAPRFLGVTQNETE
RMIRLVNDLLQLSRMDSKDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFKREFPKRDLWVEIDTDKIT
QVLDNIISNAIKYSPEGGTITFRLLETHNRIIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGL
GLAIAKEVVEAHGGRIWAESEEGKGTTIYFTLPY
>gnl|CDD|467965 NF033093, HK_VicK, cell wall metabolism sensor histidine kinase VicK. This model describes the protein VicK (or WalK) as found in Streptococcus pneumoniae, This protein is shorter than the WalK of Staphylococcus aureus, although apparently is functionally similar. Compare to model NF033092 (HK_WalK). VicK is a sensor histidine kinase involved in regulating cell wall metabolism. Its two component system partner is the response regulatory VicR
MIDNIKQNIFSFEFAFLLLLLGFILYFILLALRNRRDNKQLRQLNQKVKDLIAGDYSEVLDMQGDPELTE
LTNSLNDLSEVFRLTHENLEQEKNRLASILSYMTDGVLATNRRGQIIMINDTAQKQLNVKREEALNMNIL
DLLDIDDEYDLRDLITKTPELTLDSRDENGEFLSLRVRFALIRRESGFISGLVAVLHDTTEQEKEERERR
LFVSNVSHELRTPLTSVKSYLEALDEGALSEPVAPSFIKVSLDETNRMMRMISDLLSLSRIDNQTSHLDV
ELTNFTAFITFILNRFDQIKSQDTETGKKYEIVRDYPITSIWVEIDTDKMTQVIDNILNNAIKYSPDGGK
ITVSMKTTDTQLIISISDEGLGIPKKDLPLIFDRFYRVDKARSRAQGGTGLGLAIAKEIIKQHKGFIWAK
SEYGKGSTFTIVLPYDKDAVKDDEWEDE
>gnl|CDD|380163 NF033113, halo_ClmS, chloramphenicol-biosynthetic FADH2-dependent halogenase CmlS
KRSKVAIIGGGPAGSVAALTLHKLGHDVTVYERETFPRYRVGESFLPGTMSILNRLGLQEKIDAAGFVKK
PSATFLWGQDQAPWTFSFSTPKVAPWVFDHAIQVKREEFDQLLLDEARARGITVHEGTPVTDVDLSDPDR
VTLTVRRGDETSTVEGDFVIDAGGSGSPLARKLGVRRYDEFYKNFAVWSYFRCPDPFKGDLKGTTYSITF
EDGWVWMIPLKGDLYSVGLVVDRSKAAEVRELGPDAFYRRTLAKCGRAMEILGDAEQVDEVRIVHDWSYD
TEVFSAGRFFLCGDAACFTDPLFSQGVHLASQSAVSAAAAIDRITQNPDEADAVHAWYNRSYRETYEQYH
EFLASFYTFASFTEPESEFWRKRRISESDDERLERRKWFERLVGEAREDSDWSVADFRDRASTMIAIGRH
QRQELSDEFSDAELNPARVRWISQLTKQLNSITRLEWNGSKVRLKPYYKVDPLSFRLEPKQVLANEDGLD
MTKYPVDEAVRQIFQDLAEEEFGYKTLIKRLGDVGRQELSSQIVIRLMEAGLLTGYDAHGERVVIQDRLR
FDGVGVEYEV
>gnl|CDD|411094 NF033138, RND-peri-MexC, MexC family multidrug efflux RND transporter periplasmic adaptor subunit
MGNLRAIGMAGALAAAIALAGCGPAEEQQAAAEVARPVEVVAVATEPLALTSELPGRVEPMRVAEVRARV
AGIVLQKRFEEGADVKAGDLLFQIDPAPLKAALSRAEGELARAQAVLLEAQARVKRYEPLVKIEAVSQQD
FDTATADLRSAQAATRSAQADLETARLNLGYASVTAPISGRIGRALVTEGALVGQGDATLMARIQQLDPI
YVDFTQSAADALRLREALKDGALAAGDSQALSIRVEGTDYERQGALMFTDVAVDRGTGQVSLRGKFDNAD
GVLLPGMYVRVRTPQGTDNQAILVPQRAVQRGSDGSAQVMVVGADGRAEARSVRTGAMQGSRWQISEGLK
AGDQVIVGGLAGLQPGAKVVPKQAQ
>gnl|CDD|467966 NF033143, efflux_OM_AdeK, multidrug efflux RND transporter AdeIJK outer membrane channel subunit AdeK
QKVWSISGRSIAVSALALALTACQSMRGPEPVAQADIPESYAGNASGTSIAEQGYKDFFADQRLLQVIDL
ALANNRDLRTAALNIQRAQQQYQITENNQLPTIGASGSVLRQDTPSRDPNNPYSTYNVGLGVTAYELDFW
GRVRSLKDNALDSYLATQSARDATQISLIGQVAQAWLNYSFANANLKLADQTLKAQLDSYNLNKKRFDVG
IDSEVPVRQAQISVETARNDVANYKTQIAQAQNLLNLLVGQPVPQNLLPQQRVTRITQQSALSAGLPSDL
LNNRPDVKAAEYQLSAAGANIGAAKARLFPTISLTGSAGYASTDLSDLFKSGSFVWSIGPSLDIPIFDWG
TRKANIKISETDQKIALSDYEKSIQSAFREVNDALATRQNIGDRLTAQRRLVDATNTTYKLSNARFRAGI
DSYLTVLDAQRSSYSAEQGLLLLEQANLNNQVELYKTLGGGLKANTSDTVQYQPSSAERK
>gnl|CDD|411096 NF033147, GXX_rpt_CTERM, Gly-Xaa-Xaa repeat protein C-terminal domain. This model often occurs at the C-terminus, and companion model N_to_GlyXaaXaa (NF033172) at the N-terminus, of proteins that in between consist largely of variable numbers of Gly-Xaa-Xaa repeats, reminiscent of collagen repeats. Member proteins observed have been found so far only in Gram-positive bacteria. This domain contains a motif IPxTG near its C-terminus, suggesting it is processed by some form of sortase
PNFPVATAVLGNSNPQTVSPGNNFQFNTTFNLNNIIFNGTDTLTVLETGVYVISFSASTTFPGSAPFGFG
ISINGQVPTDNFSTNVIGSSLSFSTIETLAAGTTISVQPTANTISIPNTGNTTARLTVFRIA
>gnl|CDD|467967 NF033153, phage_ICD_like, host cell division inhibitor Icd domain. Icd from temperate phage P1 inhibits cell division in its host. Homologous sequence is found in many other proteins, often as the C-terminal region of what appears to be a much larger protein. Putative phage proteins that contain this domain may be designated "host cell division inhibitor Icd-like protein". See PMID: 8491703 for a description of Icd. Many proteins with this domain also have the Ash domain described by PF10554, which also occurs in phage
FTWRFAAVRRTDRTARPCVIRITADTEREARRQLARDYVLVFAARIPV
>gnl|CDD|467968 NF033154, endonuc_SmrA, DNA endonuclease SmrA. YdaL is a small endonuclease with homology to the C-terminal domain found in the endonuclease MutS2, but not found in the related mismatch repair protein MutS. The biological role of this endonuclease is not yet known. As one of two Small MutS2-Related proteins in E. coli, This protein was designated SmrA by Gui, et al. (PMID:21276852). The term SMR is much better known for describing a large family of Small Multidrug Resistance (SMR) efflux transporters, but in that context is used with three capital letters
DDFDLFLQEMGDVKPLKQDTVALLTKKHQPTLAQLARREAAEAELEEDDNFLSTDFVELLDPDDPLEFKR
DGVQEGVFKKLRLGKYPIQARLDLHRQTVEQARQELFSFIRDCHKRGLRTVLIVHGKGRRSKPHPAILKS
YVAKWLPQFDEVQAFHSAQPHHGGSGAVYVLLRKSEEKKLENRERHAKR
>gnl|CDD|380165 NF033155, CatA_like_1, CatA-like O-acetyltransferase, family 1. Members of this family are homologs to members of the CatA family of chloramphenicol acetyltransferases, although less than 30% identical. There is no evidence that members of this family act on or confer resistance to chloramphenicol
MAHYKIIDKESWPRKDHFDFYRKFANPSFNLCVPVEAQRLYECAKDRGVSFFQLALYALLRAANAVPQLK
QRLLGDEIIEYDSIAVMTPVMTAQEGFRQVWCDNAADFTAFSAAATPKIEAAKNTAPAPLIVQGENFFCA
SCLPWLHFSAITHAEYYVGAAVPALTWGKLKNGVIPVAGKFNHAFVDGLHASRFFALIEEGFANPDALW
>gnl|CDD|380166 NF033157, SWFGD_domain, SWFGD domain. This small domain (29 amino acids long) is named for its most conspicuous (although not invariant) motif, SWFGD. The motif occurs primarily, although not exclusively, in protein sequences with a BON domain (PF04972), suspected of involvement in attachment to phospholipid membranes, or with a DUF2171 domain (PF09939). Two copies of the motif may be found in a single protein
EDRGFFDRAGDEVASWFGDDDAERRREMD
>gnl|CDD|380167 NF033158, Myrrcad, MyrrCad domain. This domain appears at or near the C-terminus in expanded paralogous families of proteins in Mycoplasma and Candidatus Mycoplasma genomes. Proteins with this domain typically show an N-terminal sequence regions followed by a repeat region, highly variable in length and similar to the leucine-rich repeat. The center region of this domain resembles alpha-helical hydrophobic transmembrane segments. The domain ends with a cluster of basic residues, suggesting an orientation in which the C-terminal residues of the domain face the cytosol. The coinage "MyrrCad", rendered without full capitalization because it is an acronym rather than an amino acid sequence motif, signifies "MYcoplasma Repeat-Rich protein C-terminal Anchor Domain"
SSSNLGLILGLVLGSITLLGIGSGLGYYYRKNLKNL
>gnl|CDD|467969 NF033160, lipo_LipL36, lipoprotein LipL36. Members of this family are lipoprotein LipL36, as described in Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130 but found broadly in the genus Leptospira. Close homologs that are not lipoproteins by sequence are likely defective in their reported coding region
MRRNIMKIAAVAALTVALTACKSDDDDDDVVMLALLYLADQTSGNCVTITKDDAAHSGAAGAGDGKPTYT
ATGTTKPKAACGGTFNVVFIVNNAEAVVTSVKASYQAAKDKADAAGSNCAAVSTSLQAAIDAVTTLKVQQ
TLAADPGNGSCLGSGTGWNLNPLALGGSSVSVDPNPEYFGKTVYACSSEQAKEKLLAQLNTNTFSTIAGS
VATDMATNLAFKQKTAAVTASNFKWTADAAAKGRLINVTELTTAGKSGAALVAFGTALQANVALVGNGNG
AGATTARACAKDILSKESEEVQKIAFALHDADPGIGFNGAMTGGVLDSIITTAQAASVKEVLFTSLTCKY
GDFDEEAAGNKTTVGTETNVKNIGTCPATYPKI
>gnl|CDD|467970 NF033161, lipo_LipL41, lipoprotein LipL41. Members of this family are lipoprotein LipL41, as described in Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130 but found broadly in the genus Leptospira. Close homologs that are not lipoproteins by sequence are likely defective in their reported coding region
MRLSLLSLLCLLMFLGNCQSVTVEYPVFPKTKEGRDLQKFLGGVRNVGLAVEPPKKSLWEHDFGAGRSFI
LQVPSKVFEAFSKDSYFKLIDLSKRADIINEATLSLAGITKNRVKLGNLLGAEAILYISVQKPYSECSVE
MKMDYLAAGMKVLGAAAAMASGKRVLTRAPISPGNDPVMKPTGVRKMLIPIEATLIRVDTGEVKKAVISK
PSKIYNGVGDLSCPSILDSLSQALDEAIPEIKRRLSPKVKTERISIFTEDEDPEVAALLLEGYEEITGET
PSFKRAKEAWEKADQKAKGKSWAAKANLATYYFSQGDFEKAIKLYEEAMKLGGPEKDYLKELRKRVEAPP
AVDEATEE
>gnl|CDD|380170 NF033162, lipo_LipL21, lipoprotein LipL21. Members of this family are lipoprotein LipL21, as described in Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130 but found broadly in the genus Leptospira. Close homologs that are not lipoproteins by sequence are likely defective in their reported coding region
IKKLIVCALLAAFLTSCGSADGAQKDATSVGDGGWIFEGWACAPDAAAAKRGKSPADTCKGKEKEFDYLY
MKFAARASAKAIAAKSLAMKQSTCREAARLQGAGDGLKKILGETLEQASGVSDGEATASVIVGESAGIIK
GVGVYDCCALGNESDICANVGEPDNWEECQCVGYAKFAGGQDALEAKAQAI
>gnl|CDD|467971 NF033163, lipo_LipL71, lipoprotein LipL71. Members of this family are lipoprotein LipL71, also known as LruA, as described in Leptospira interrogans but found broadly in the genus Leptospira. Close homologs that are not lipoproteins by sequence are likely defective in their reported coding region
MKKKKKTSLFSALVLFSGFFVNCGQELPLKELALAKSQITRAKRAGAEEYAPEEFEEARKNLLTAHEKAS
EEKLSETKKSADYAISKAYDALEKSLPKLADKSRKEAVAAIDAADEAYASQLAPEPYNKAVALRKEGDTL
RAQADRTLESYPKESKDDAKLLKRLAAFQQYEDSHNKYQDSKKIASEAKKLALSQKQQLIDSAADIDKNL
DDADSYAKGGDPEVDETRARLASAKSKIQAGKIKEGYSEIDDIRKKSAELVAKNIKDYAKKRKAQAKEVV
EDANLRLAELDADKYLSSNDAQESYQRAQENLKAANESLQAAENLYESEKYEDSITRSEEAIRLSRISVD
QIETLAERINVAKKDRKTVGTDTEETTADSKEPSTTEGKNKSSSSQVEELPEGWKRYVVRKKVPADCLWR
IADRKDHYGTSKLWRRIYEANRKKIRNPNLIYPKQVLLIPPKKGKTGKDPKE
>gnl|CDD|380172 NF033164, lipo_LipL46, lipoprotein LipL46. Members of this family are lipoprotein LipL46, as described in Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130 but found broadly in the genus Leptospira. Close homologs that are not lipoproteins by sequence are likely defective in their reported coding region
KLPILRITALTLVLGFAFACATGSSTRRKKKEEYEKEGNTITVIGEAPIYNGDKANAKQRALKDAKINAV
RKVVGEEISNKSQASDGESLGSSLLSKTDAFVKSYDIVDEAEGKIDTQPILKLTVRCTVEESKLSTAVDS
LLADVGNPRIAVLVPSVVGGAPVPPLSAGNIAEAEIIKALKKAGNKVVDPSTAAKTVKKSQVDADNVTSL
DAGSPILIQAQASGAEVLIVGNVETEDQKPVTSIGGKKLDRPIYNTAATGPYKVILLWGDGKIVDSGTGD
GRGADITQKVSREKAVADWAESVSKKVNKQLKEEWFNLTENNTIILKFTGLNADEATKFKDDLTEFTAAK
DINVRTSDVNGSEWEVTYPGKDALFMDELVYKKDRGFSFLATKKLNVKSATRGVVTLEFKPNK
>gnl|CDD|467972 NF033165, lipo_LipL45, lipoprotein LipL45. Members of this family are lipoprotein LipL45, as described in Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130 but found broadly in the genus Leptospira. Close homologs that are not lipoproteins by sequence are likely defective in their reported coding region
KKIIIVASAVLFTGLLVSGACKKPAENATAANAKQSDPSAVVVFSVGESKIQHADLTEEKAQLGASLKTG
DKVVTKDKAKVDIQFADGSAIRISEKSAIDFAALSLDSAGNTDTRLALVSGKVFAKVNKASKEDQFSVVT
PTAIAGVRGTSFIVDRTKSDRAVVKVLEGAVAVAPRVPALEGLSDEEISKNADLKKIQDSLAKAEVILEK
DQASTVKAKDKELGKKDDSKIADLEKAIPKAVKKLSNAGISKNEEQEIRTIVTVDKDTAEKIVKLNEESQ
SGKLDEQKAAVNEAERKKIEKDVAKRQEEEKKKFKEVLVSAPKELKSKKDIVNYYERIEKIVLADGKTSI
IGAIVDQQGSTMIVHTEQGIKKINQDDVQEVIYDFQTKSKF
>gnl|CDD|380174 NF033166, lipo_LipL31, lipoprotein LipL31. Members of this family are lipoprotein LipL31, as described in Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130 but found broadly in the genus Leptospira. Close homologs that are not lipoproteins by sequence are likely defective in their reported coding region
LSLFVLLSLLFFAGCGDGSPVIESIDGNKITVGGFEAAYDTALDTLSRTQNIEKKNLIEFITKDISEVPQ
QFRPLRYEFQKKNFFDRYRQMMMTKLAADKSGFTKRPDIKEILKFQEMQLISQMYIAEQVESKIKISEEE
AKAECQELRAKYKQIESLTIDRCLLFARAQIKGRKSREVYPKVLERIKEGVTIKHNDKFDLEAYLDKKFK
>gnl|CDD|467973 NF033167, lipo_LIC11695, LIC_11695/LIC_11696 family lipoprotein. Members of this family are lipoproteins found broadly in the genus Leptospira. Two paralogs, LIC_11695 and LIC_11696 are found in Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130 (a well-studied reference strain), where they are encoded by tandem genes, and are among the 25 proteins whose expression is up-regulated the most by the increase in osmolarity that signals entry into a host species
KKKIKLLLIILTIFTLLSFCKNEEKVNVNEILGILLLKQNSESEGESLGLTIAFSHRFSKPNGEILSCRE
YSTAYLDKKAEWEQGLEQFVATIKNGIGLDLVVDRIDGPCVVPNKVSACIYEGVDGINDPIPYAYSYEGE
REYLVPAMIYYNGFTDVKTAKEACENLKNRGIAGTYKCYAPGQCWE
>gnl|CDD|467974 NF033168, lipo_LIC10766, LIC_10766 family lipoprotein. Members of this family are lipoproteins found broadly in the genus Leptospira
KSITIFILSFLILFFVQCKSKETKEPKEEKPKKTTTVMEESNESEADEFTKATEGFLNSSTFQVVVSSLE
GNEDEAQDLARKRALNLLIAEKGDNFRPSDRKELKELVESKGKIVKKSVSIQGKTYFLFQISSPDLKRSL
KK
>gnl|CDD|467975 NF033169, lipo_LIC10494, LIC_10494 family lipoprotein. Members of this family are lipoproteins found broadly in the genus Leptospira
KYSIFLIFLILLSGQCSYINKFGSARVAVKKDKEKFPYLIGRIENRDSRFDPFVAENFSDMLKFELLKEG
YEILEIEEEKKTSEPNPKTSVTTKKKNETTFPPEPSNVKTMNSENLRQVLDKGTVLLSENEIKNLSAKTK
FDYFIQGAVGMNDNGNLLDEDFSSLIFLRVYDKNGKLVGSINYTVDGRTLTEADLLKEVCRSIINKIVKL
EEK
>gnl|CDD|467976 NF033170, lipo_LIC13355, LIC_13355 family lipoprotein. Members of this family are lipoproteins found broadly in the genus Leptospira
FLVLLISLISCKPSSSSDDESLAALLLLQLTQGSSPNASPCPPSPLPSGIFLANTVVSAPANVSGTGFSD
STKAINGVCGGGEFNGSLDVYTLDTSGAGATLILSWGGKTVKNVSGIDFIVYENPFRISGSSNTYFLEPM
VVEVSNDGTNYCGFNPSYTGGGAFSNDPSSWLRFAGLRPVLYNMTTNPLSVEDLFTNTGSVFLLGGGDGF
DLDDLNFGNSGTGCDAALRTDIQTNGFKYIKLTSASAVLNPFPIPPGSYNGPDIDGVIAKSVS
>gnl|CDD|467977 NF033171, lipo_LIC11139, LIC_11139 family putative lipoprotein. Members of this family are restricted to the genus Leptospira. They are putative lipoproteins with only a single Cys residue, invariant at the proposed lipoprotein signal cleavage site. Residues in the -1 position are unusual for lipoproteins in general, but consistent with observations in Leptospira, as described in PMID:26890609
KRIQKLLGALALGLTILSLQNCFISDSVSSVSDSLSKSSDSLESLSKSIKSLVSSIFSSSSDDDEKKKKA
YLRDVETLTAMHLENGFQSIEFENDLATLALKNGITNWKSSEVTYVGIGRGLKKAGVEEDKFQSFAQEFG
TSRPEIVKALRKGYHSL
>gnl|CDD|467978 NF033172, N_to_GlyXaaXaa, collagen-like repeat preface domain. All protein sequence used in the seed alignment for this model comes from the N-terminal region of proteins with extended collagen-like Gly-rich repeat regions, and occur in Firmicutes
ISKSQLTRLISLLQELTTLIPAVFTNPTPSNISALQNLLRQLLKFLNSLNLSSAEKAALLSIIENLITIL
ESPPFSPGALAILLQQLLNALLSIVLLFKIDPCIKDSLIGLIRELQTILSNA
>gnl|CDD|380181 NF033173, anticapsin_BacC, dihydroanticapsin 7-dehydrogenase. Members of this family are dihydroanticapsin 7-dehydrogenase (EC 1.1.1.385), one of seven key molecular markers for biosynthesis of the non-cognate amino acid anticapsin, a building block for the dipeptide antibiotic natural product bacilysin
NLTDKTVLITGGASGIGYAAVQAFLNQQANVVVADIDEAQGEAMVRKENNDRLHFVQTDITDEAACQNAV
QSAVDTFGGLDVLINNAGIEIVAPIHEMELSDWNKVLQVNLTGMFLMSKHALKHMLAAGKGNIINTCSVG
GVVAWPDIPAYNASKGGVLQLTRSMAVDYAKHQIRVNCVCPGIIDTPLNEKSFLENNEGTLEEIKKEKAK
VNPLLRLGKPEEIANVMLFLASDLSSYMTGSAITADGGYTAQ
>gnl|CDD|467979 NF033175, fuso_auto_Nterm, autotransporter-associated N-terminal domain. This domain typically is found in the genus Fusobacterium, in N-terminal regions of large proteins that are recognized as autotransporter proteins by C-terminal regions matching Pfam model PF03797. In paralogous families of such proteins, the N-terminal and C-terminal regions are fairly well-conserved, but the repetitive central region is poorly conserved in both length and sequence
KVEKNLRSFAKRYKNVKYSLGLLILFLMTGTSAFSEEVVSTEEEIEESKKELLTSIKNLKSKIKEARKEN
EKLLKGLNLELIQLMEQGDQVVKSPWSSWQFGANYFYSNWNGTYKGRGDKK
>gnl|CDD|380183 NF033176, auto_AIDA-I, autotransporter adhesin AIDA-I
MNKAYSIVWNHSRQAWVVASELARGHGFVLAKNTLLVLAVASTIGNAFAQNISSGVVSGGVVSSGETQVV
YSNGQTSNATVNSGGIQNVNNGGKTTSTTVNSSGAQNVGNSGTAISTIVNSGGVQRVSSGGVTSATSLSG
GAQNIYNLGHASNTVIFNGGNQTIFSGGISDDTNISSGGQQRVSSGGVASNTTINSSGTQNILSGGSTVS
THISSGGNQYISAGGNASATVVSSGGFQRVSSGGTATGTVLSGGTQNVSSGGSAISTSVYSSGVQTVYAG
ATVTDTTVNSGGKQNISSGGIVSGTIVNSSGTQNIYSGGSALSANIKGSQIVNSDGTAINTLVNDGGYQH
IRNGGVASGTIINQSGRVNISSGGYAESTIINSGGTQSVLSGGYASGTLINNSGRENVSNGGSAYNTIIN
AGGNQYIYSNGEASGTTVNTSGFQRVNSGGTATGTKLSGGNQNVSSGGKAIAAEVYSGGKQTVYAGGEAS
GTQIFDGGVVNVSGGSVSGASVNLNGRLNVFAGNVTGTILNQEGRQYIYSGASATSTVANNEGREYVLSG
GVADGTVLNSGGLQAVSSGGSASATVINEGGSQFVYEGGNVTGTVIKNGGAIRVDSGASALNIALSSGGN
LFTSTGATVTGTNHYGSFSVSQNHASNVVLENGGLLAVTSGSTATDTTVNSAGRLRIDEGGALDGTTTIN
ADGIVAGAKIKNDGDFILNLAGDYDFNTELSGNGALVKDNSGVMSYEGTLTQARGVNVKNGGIILGSAVV
NADMAVSQNAYINISDQATINGSVNNKGSVVINNSIINGNITNDADLSFGTAKLLSATVNGSLVNNKNII
LNPTKESAGNTLTVSNYTGTPGSVISLGGVLEGDNSLTDRLVVKGNTSGQSDIVYVNEGGSGGQTIEGIN
IISVEGNSDAEFSLKNRVVAGAYDYTLQKGNVSGTDKKGWYLTSHLPTSDTRQYRPENGSYATNMALANS
LFLMDLNERKQFSAVNDNTQPESASVWMKITGGRTSGKLSDGQNKTTTNQFINQLGGDIYKYHAEKLGDF
TLGIMGGYANAKGKTINHTSKKGARNTLDGYSAGLYGTWYQNGANATGLFAETWMQYNWFNASVKGDGLE
EEKYNLNGLTASVGGGYNLNVHTWTSPEGIKGEFWLQPHLQAVWMGVTPDTHQEDNGTVVQGTGKNNLQT
KAGIRASWKVKSSLDKDTGREFRPYIEANWIHNTHEFGVKMSGDNQLLSGSRNQGEIKTGIEGVITQNLS
VNGGVAYQAGGHGSNAISGALGIKYSF
>gnl|CDD|467980 NF033177, auto_Ag43, Ag43/Cah family autotransporter adhesin. Members of this family, restricted to Escherichia coli (including E. coli K-12) are the autotransporter adhesin Ag43 (antigen 43), also known as flu, or its calcium-binding homolog Cah, differing mostly in the central region. The C-terminal region forms an outer membrane beta-barrel autotransporter domain, which enables type V secretion (autotransport)
MKRHLNTSYRLVWNHITGTLVVASELARSRGKRAGVAVALSLAAVTSVPALAADTVVQAGETVNGGTLTN
HDNQIVFGTANGMTISTGLEYGPDNEANTGGQWIQNGGIANNTTVTGGGLQRVNAGGTASDTVIRDGGGQ
SLNGLAVNTTLNGGEQWVHEGGIATGTVINEKGWQAVKSGALATDTVVNTGAEGGPDAENGDTGQTVYGT
AERTTINKNGRQIVAASGTANTTVVYAGGDQTVHGHALDTTLNGGYQYVHNGGTASDTVVNSDGWQVVKE
GGLAGNTTVNQKGKLQVNAGGTATNVTLKQGGALVTSTAATVTGTNRLGNFSVENGKADNVVLENGGRLD
VLEGHSAQNTLVDDGGTLAVSAGGKATTVTMTSGGALIADSGATVEGTNASGKFSIDGISGQASGLLLEN
GGSFTVNAGGQASNTTVGYRGTLTLAAGGSLSGRTQLSKGASMVLNGDVVSTGDIVNAGEIRFDNQTTPD
AALSRAVAKSNSPVTFHKLTTSNLTGQGGTINMRVTLDGSNVSDQLVINGGQATGKTWLAFTNVGNSNLG
VATTGQGIRVVDAQNGATTEEGAFALSRPLQAGAFNYTLNRDSDEDWYLRSENAYRAEVPLYASMLTQAM
DYDRILAGSRSHQTGVNGENNSVRLSIQGGHLGHDNNGGIARGATPESSGSYGFVRLEGDLLRTEVAGMS
LTTGVYGAAGHSSVDVKDDDGSRAGTVRDDAGSLGGYLNLTHTSSGLWADIVAQGTRHSMKASSDNNDFR
ARGWGWLGSLETGLPFSITDNLMLEPQLQYTWQGLSLDDGQDNAGYVKFGHGSAQHVRAGFRLGSHNDMT
FGEGTSSRDTLRDSAKHSVSELPVNWWVQPSVIRTFSSRGDMSMGTAAAGSNMTFSPSQNGTSLDLQAGL
EARVRENITLGVQAGYAHSVSGSSAEGYNGQATLNMTF
>gnl|CDD|467981 NF033178, auto_BigA, autotransporter adhesin BigA. Members of this family are the adhesin BigA, found in Salmonella. BigA is an autotranporter, meaning is has a C-terminal outer membrane beta-barrel, through which passenger regions of the proteins are transported
MQKKKLISIAIALTLQSYYIPAIAAENNDDEKECPSNISSLPKEKRAKLSPTCLATPENDNHWGWVAGGV
AALVAGVAIGVENNGGGDSNHSYTPPTPDNGGDVTPPDDGGNVTPPDDGGDDDVTPPDDSGDDDVTPPDD
SGDDDVTPPDDSGDDDVTPPDDSGDDDDTPPDDSVITFSNGVTIDKGKDTLTFDSFKLDNGSVLEGAVWN
YSEQDNQWQLTTADGKTLNVTGWDVTDANAAVIEGTQENGLYWKYDSRGYLIIADDNTTVISGDDQAHNS
DRGMDISGQDRTGVIISGDRTVNTLTGDSSVTDGATGMVISGDGTTNTISGHSTVDNATGALISGNGTTT
NFAGDIAVSGGGTAIIIDGDNATIKNTGTSNISGAGSTGTVIDGNNARVNNDGDMTITDGGTGGHITGDN
VVIDNAGSTTVSGADATALYIEGDNALVINEGNQTISGGAVGTRIDGDDAHTTNTGDIAVDGAGSAAVII
NGDNGSLTQAGDLLVTDGAMGIITYGTGNEAKNTGNATVRDADSVGFVVAGEKNTFKNKGDIDVSLNGTG
ALVSGDMSQVTLDGDINVVSVQDSEGVFSSATGVSVSGDSNAVDITGNVNISADYGQDDLAAGAPPLTGV
VVGGNGNTVTLNGALNIDDNDLSATSGQYLDVVGLSVTGDDNDVEIGGGINITHSEDPLDGTSADITGIS
VSGNSTVTLNGHSTIDTNTVVGGHVVLARVNNGGSLILGDDSVVDVNVSYIPTGYYTYNALLMADGEGTS
IENKGDITSHGVYSVIRADNGSEVSNSGDILVYATSSNSSEDRAAITRASGEGSAVHNKAGGDITLISDQ
TPQGSGGIEVYPLKWYTHTFYAMMASDYGDVVNDEGATIHLQGAGVYGVTASRGKALNEGDIYLDGLVPT
LDDENNITSTSYWQPSSLYLTSSGMVAGSTDADGDATAINTGNITVNNAGFGMMALNGGTAINQGVITLT
ADDGVTGQADELVGMAALNGGVVINDTSGVINIDADYGQAFLSDSSSYIINNGSINLNGSPMDDTDSHMG
GTPTDKIWIQSLPGSGDSDTRTSDTGFFTAGTLANYGTETLNGDVDVNGGWLYNEAGASLTVNGTVTING
GANALANYGTLDADAISTWHSLFNEADGSITTDLLTLNGDVTFYNNGDFTGSIAGTSYQQEIVNTGDMTV
AEDGKSLVSGSFYFYNEEDATLTNSGSAVEGGENTIINLTRANDSLTQVNSGTITATNGYSAITTVNGSN
DPKWIWNTATGVINGINPDAPLINLGRGYNFGNQGTINVQGDNAVAISGGTSSYVINLVNSGTINVGTEQ
GKEDGTNGTGLIGIKGNGNATTINNTADGVINVYADDSYAFGGKTKAIINNGEINLLCDSGCDIYAPGTT
GTQNDHNGTADIVIPDATTAPTEGSIPTPPADPNAPQQLSNYIVGTNADGSSGTLKANNLVIGDNVKVDT
GFTSGTADTTVVVDNAFTGSNIQGADNITSTSVVWNAQGSQDADGNVDVTMTKNAYADVATDSSVSDVAS
ALDAGYTNNELYTSLNVGTTAELNSALKQVSGAQATTVFREARVLSNRFTMLADAAPQIKDGLAFNVVAK
GDPRAELGNDTQYDMLALRQTLDLTASQNLTLEYGIARLDGDGSKTAGDNGLTGGYSQFFGLKHSMAFDE
GLAWNNSLRYDVHNLDSSRSVAYGDVNKIADSDMRQQYLEFRSEGAKTFTMMSDTLKVTPYAGVKFRHTM
EDGYKERSAGDFNLSMNSGNETAVDSIVGLKLDYAGKDGWSATATLEGGPNLSYSKSQRTASLQGAAGQS
FGVDDGQKGGGINGLATIGVKYSSNDTALHLDAYQWKEDSISDKGFMLNVKKTFR
>gnl|CDD|380186 NF033179, TnsA_like_Actin, TnsA-like heteromeric transposase endonuclease subunit. The transposase of transposon Tn7 contains multiple subunit. Members of this family are largely restricted to the Actinobacteria, resemble the endonuclease subunit TsnA of the multimeric transposase of Tn7 and its relatives, and occur in genomic neighborhoods that suggest a similar role in transposition
LADAAAVRFEDAAPVRTFPSYRGQRHYPGWYWSATTGRHVGYESWLERDRLMLLDFDPDVVGIASQPFWL
LWRDGGRVRRHVPDYFARLADGTAVVVDVRPADRIGPRDAEAFAWTRAACEAVGWRYRVVGPPDPVLLAN
VRWLAGYRHPRCAGPGLAAALREAFAEPRPLMEGARAVGDPLAVLPVLFHLLWRGELTADLSRPLSERTL
VR
>gnl|CDD|467982 NF033181, NiFeSe_hydrog, nickel-dependent hydrogenase large subunit. Members of this family are the large subunit of the periplasmic nickel-dependent hydrogenase. Some members contain a selenocysteine residue
AQKIVIDPVTRIEGHLKIEVEVENGKVTDAWSSGTMFRGFEIILRGRDPRDATYITQRICGVCPTSHGTA
SSLALDDAFGAKVPANGRIIRNLILGANYLQSHILHFYHLSALDYVDGPAVAQYKGNDPGLLAVKDKIVK
LVAAGDTAPFTPRYEPDDYRLNDPEVVTTAVAHYLKALEMRAKAHEMSAIFGGKMPHQSSIVVGGVTELP
TKEKIEAFRSRLAEVIDFIENVYLPDVLAFGTGYLLDLFQAGVGGGNYLSYGGFPLDDSGKDKNLLFKPG
VYTDGDGKVMPLDPSKITEDVKYSWYKDSTNGLHPYEGVTVPDPDKKGAYSFVKAPRYDGKPMEVGPLAR
MWVMQPKGLPDIVKLYGIKPFSVVARHAARALETKLVAKAMLKWLDELEPGMPTGTPREIPASAQGMGLT
EAPRGALGHWIKIKNHKIENYQMVVPTTWNASPRDDKGVRGPVEQALIGVPVPDPDNPINVVRVVRSFDP
CLACAVHLIDPETNEIKKF
>gnl|CDD|467983 NF033183, colliding_TM, low-complexity tail membrane protein. Members of this family appear typically as an unusual gene pair with members of PF11998 (DUF3493). Strangely, members tend to have tail-to-tail overlapping regions, where the tail region from this protein is long, low-complexity, and typically rich in Asp, Glu, Asn, Gln, Ser, and Thr. These gene pairs occur broadly in Cyanobacteria. The function of this pair of convergently-transcribed overlapping proteins is unknown. The low-complexity region was trimmed from the seed alignment to build this HMM
SEPFLWIHLAGLAAVPLELLLCLLGLAVGDPGPPPWLERLLIAAIGILPPLWMQWQRPFDIFSLLLVALP
PEQLTEEQRRILALFKTLRNRLLAALGAVLLLPLLWQLYRLAPLAAAISPLPPQWRLLGLLLAAIAFLLS
NLFLQVPVSVLRVLLTSESELAATEPLPVEQIAQDFTILGLPVLQILP
>gnl|CDD|439394 NF033184, B3_Acin_new1, putative subclass B3 metallo-beta-lactamase. This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017
KKKMLFIGSILLTSLSTSAAPLKLPDDWTQNTQPFQITENIYYVGTHGLAAYLLASGHQALLIDTGLPEN
TEQIEQNIKQLGFKLSDVKIMVTSHAHWDHVGALARIKQDTGAKLIAMQQDVKALEIGKPIGENTFQTIP
FTPVKVDKVIHDGEVVKLGKFKLKATLTPGHTPGCTTWSTEVKSNGKNLNVVFPCSLSVAGNVLQNNHQY
PNIVADYRKSFERLKNMKADIVLTSHPEVADVLGNKARKDAGQTNAFIQPEKLSSIVKDAEMAFEKSLVS
SHP
>gnl|CDD|380189 NF033185, B3_Acin_new2, putative subclass B3 metallo-beta-lactamase. This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017
IRNTFLFIFGLATVSTGNILAEPLKLPAEWTQSIEPFRIAGSIYYVGTRGLGSYLLVSGSKAILIDTGLT
ENAALIEQNILKLGLNLSDVKIILVSHAHWDHVGALAQIQKNTGAKVFAMDKEVTALTTGKPKGDNILQS
FSYTPVKVDHILRDKEVIKMGKIHLKATLTPGHTPGCTTWSTSLKEHGKTLNVVFPCSLSVAGNVLSNNQ
TYPGIVQDYQLSFHRLSKMPADIVLTSHPEAADLMNRKAKSEAGQLDAFTDRKLLEKIIKDAEFSFNQSL
DNQKK
>gnl|CDD|467984 NF033186, internalin_K, class 1 internalin InlK. Internalins, as found in the intracellular human pathogen Listeria monocytogenes, are paralogous surface-anchored proteins with an N-terminal signal peptide, leucine-rich repeats, and a C-terminal LPXTG processing and cell surface anchoring site. Members of this family are internalin K (InlK), a virulence factor. See articles PMID:17764999. for a general discussion of internalins, and PMID:21829365, PMID:22082958, and PMID:23958637 for more information about internalin K
MSVKSNIVKIGVCFAVLAVPVSQTTLPVFAAEQTGLKASQDNVNIPDSTFKAYLNGLLGQASTANITEAQ
MNSLTYITLANINVTDLTGIEYAHNIKDLTINNIHATNYNPISGLSNLERLRIMGADVTSDKIPNLSGLT
SLTLLDLSHSAHDDSILTKINTLPKVTSIDLSYNGAITDIMPLKTLPELKSLNIQYDGVHDYRGIEDFPK
LNQLYAYGQTIGGKKLINSDIKSSALTYNAENQTLYVPFSLMTERTVNYDGYVPDFVKSTASSDTYFTMN
EKQVNGNRLTITSDGLTVSDVSKTDFDNLEKMEYNARIDLSYQSYNIPEQFQNGGSYTISMPIYDHYFTV
DHSLNISADSEKTYIENQPVTEAEFLADIHAKTDDGSTVTSDFADKVDFKTPGTYTVTLQSENNSGLKAA
PVQVNVTIKEKTAITADEKITYKVDTSKTEAEFLADIKAKTNDGTAITSDFATVVDLSKPGKYVVTLNAE
NDLQKALPVQVTVIVEKETPIPDPTPDPTPDPTPTPDPTPTPDPEPTPNPVINPNVNKPEVPSYKIPSIT
VNENNVKAETSKNALPKTGDSLPVGGISVGFLLIGLSFIVSRKK
>gnl|CDD|380191 NF033187, internalin_J, class 1 internalin InlJ. Internalins, as found in the intracellular human pathogen Listeria monocytogenes, are paralogous surface-anchored proteins with an N-terminal signal peptide, leucine-rich repeats, and a C-terminal LPXTG processing and cell surface anchoring site. See PMID:17764999 for a general discussion of internalins. Members of this family are internalin J (InlJ)
MKTSKIIIASLVSLTLVSNPILTFAATNDVIDSTTEITTDKETSSTQPTIKTTLKAGQTQSFNDWFPDDN
FASEVAAAFEMQATDTISEEQLATLTSLDCHNSSIADMTGIEKLTGLTKLICTYNNITTLDLSQNTNLTY
LACDSNKLTNLDVTPLTKLTYLNCDTNKLTKIDVSQNPLLTYLNCARNTLTEIDVSHNTQLTELDCHLNK
KITKLDVTPQTQLTTLDCSFNKITALDVSQNKLLNRLNCDTNNITKLDLNQNIQLTFLDCSSNKLTEIDV
TPLTQLTYFDCSVNPLTELDVSTLSKLTTLHCIQTDLLEIDLTHNTQLIYFQAEGCRKIKELDVTHNTQL
YLLDCQAAGITELDLSQNPKLVYLYLNNTELTKLDVSHNTKLKSLSCVNAHIQDFSSVGKIPVLNNNLDA
EGQTITMPKETLTNNSLTIAVSPDLLDQFGNPMNIEPGDGGVYDQATNTITWENLSTDNPAVTYTFTSEN
GAIVGTVTTPFEAPQPIKGEDVTVHYLDDKGEKLAADEVLSGNLDDPYTSSAKDIPDYTLTTTPDNATGT
FTTTSQSVTYVYTKNIVAAEPVTVNYVDDTGKTLAPSETLNGNVGDTYNATAKQIDGYTLSAEPTNATGQ
FTSSAQTVNYIYTKNPAPEKGVVEIHYVDENNKQLSSATKISGTVGDNYTTEPKNIDGYTLTTTPDNATG
TFNTSSQTVTYVYTKNIVAAEPVTVNYVDANGKTLAPSETLNGTIGDTYKATAKQIDGYTLSAEPTNATG
QFTNSAQTVNYIYTKNTNIDQPLPDKKTTKPSNLKTTEVKKASDTLPKTGDSAPWKSALLGVFLSSTALV
IWKKKK
>gnl|CDD|467985 NF033188, internalin_H, InlH/InlC2 family class 1 internalin. Internalins, as found in the intracellular human pathogen Listeria monocytogenes, are paralogous surface or secreted proteins with an N-terminal signal peptide, leucine-rich repeats, and usually a C-terminal LPXTG processing and cell surface anchoring site. See PMID:17764999 for a general discussion of internalins. Members of this family are internalin H (InlH), or internalin C2, two class 1 (LPXTG-type) internalins that are closely related, one apparently derived from the other through a recombination event
MKKRWNSVFKIVLMVTAILGISLYVTTSQGVEVRAESITQPTAINVIFPDPALANAIKIAAGKSNVTDTV
TQADLDGITTLSAFGTGVTTIEGVQYLNNLIGLELKDNQITDLTPLKNLTKITELELSGNPLKNVSAIAG
LQSIKTLDLTSTQITDVTPLAGLSNLQVLYLDLNQITNISPLAGLTNLQYLSIGNAQVSDLTPLANLSKL
TTLKADDNKISDISPLASLPNLIEVHLKNNQISDVSPLANTSNLFIVTLTNQTITNQPVFYQNNLVVPNV
VKGPSGAPIAPATISDNGTYASPNLTWNLTSFINNVSYTFNQSVTFKNTTVPFSGTVTQPLTEAYTAVFD
VDGKQTSVTVGANELIKEPTAPTKEGYTFTGWYDAKTGGNKWDFATDKMPAEDITLYAQFTINSYTASFD
IDGKLTTQKVTYQSLLEEPVAPTKDGYTFTGWYDAKTGGNKWDFATGKMPAGNITLYAQFTKNDNPNPDD
PTPNTPTGNGDGTSNPSNSGGNTTLPTAGDENTMLPIFIGVFLLGTATLILRKTIKVK
>gnl|CDD|380193 NF033189, internalin_A, class 1 internalin InlA. Internalins, as found in the intracellular human pathogen Listeria monocytogenes, are paralogous surface or secreted proteins with an N-terminal signal peptide, leucine-rich repeats, and usually a C-terminal LPXTG processing and cell surface anchoring site. See PMID:17764999 for a general discussion of internalins. Members of this family are internalin A (InlA), a class 1 (LPXTG-type) internalin
RKKRYVWLKSILVAILVFGSGLWINTSNGTNAQAATITQDTPINQIFTDTALAEKMKTVLGKTNVTDTVS
QTDLDQVTTLQADRLGIKSIDGLEYLNNLTQINFSNNQLTDITPLKDLTKLVDILMNNNQIADITPLANL
SNLTGLTLFNNQITDIDPLKNLTNLNRLELSSNTISDISALSGLTSLQQLSFGNQVTDLKPLANLTTLER
LDISSNKVSDISVLAKLTNLESLIATNNQISDITPLGILTNLDELSLNGNQLKDIGTLASLTNLTDLDLA
NNQISNLAPLSGLTKLTELKLGANQISNISPLAGLTALTNLELNENQLEDISPISNLKNLTYLTLYFNNI
SDISPVSSLTKLQRLFFYNNKVSDVSSLANLTNINWLSAGHNQISDLTPLANLTRITQLGLNDQAWTNPP
VNYKVNVSIPNTVKNVTGALIAPATISDGGSYAEPDITWNLPSYTNEVSYTFNQSVTIGKGTTTFSGTVK
QPLKAIFNAKFHVDGKETTKEVEAGNLLTEPAKPVKEGHTFIGWFDAQTGGTKWNFSTDKMPTNDIDLYA
QFSINSYTATFDNDGVTTSQTVDYQGLLQEPMAPTKEGYTFKGWYDAKTGGDKWDFATSKMPAKNITLYA
QYSANSYTATFDVDGKTTTQAVDYQGLLKEPKTPTKAGYAFKGWYDEKTDGKKWDFATDKMPANDITLYA
QFTKNPVAPPTTGGNTPPTTNNGGNTTPPSANIPGSDTSNTSTGNSASTTSTMNAYDPYNSKDASLPTTG
DSDNALYLLIGLLAVGTAVALTKKARANK
>gnl|CDD|467986 NF033190, inl_like_NEAT_1, NEAT domain-containing leucine-rich repeat protein. Members of this family have an N-terminal NEAT (near transporter) domain often associated with iron transport, followed by a leucine-rich repeat region with significant sequence similarity to the internalins of Listeria monocytogenes. However, since Bacillus cereus (from which this protein was described, in PMID:16978259) is not considered an intracellular pathogen, and the function may be iron transport rather than internalization, applying the name "internalin" to this family probably would be misleading
KKNYIKALVVATTLAIPFATYSTPALAALKIEANQSVAAASDRTYDTEIKIYKDQKDEPSMVSQYIKDPK
VAIEDGKKIVTVTMQDSDYFQYLRIEDKNQPGVFHDVKVLSEDKRKNGTKVVQFEIGEFEKKHNMQMHIL
IPAIGYDHKYQVQFEIKDPTVGDKETEKPDDNSNSGNTETDNPVDNQNMITDNKLRELVNKKVFNRKDLN
TPITKEELLQVKDLFLNTNEILDYSALKYMPNLKSLTVANAKIKDPSFFTNLKQLNHLALRGNEFSDVTP
LVKMDNLESLDLSNNKITNVAPLTEMKNVKSLYLSGNQIEDVTALAKMEQLDYLNLANNKITNVAPLSAL
KNVTYLTLAGNQIEDIKPLYSLPLKDLVLTRNKVKDLSGIDQMNQLEELWIGKNEIKDVTPLSKMTQLKE
LDLPNNELKDITPLSSLVNLQKLDLEANYISDLTPVSNLKKLVFLSFVANEIRDVRPVIELSKTAYINVQ
NQKVFLEETEVNKEVKVPIYEKDGKISTKIRLKSEGGTYSNDVVKWSTPGEKVYEFGVKDPFADTGIFFT
GSVIQNVVESKGEDEKEEVVEFKDVPKGHWSEEAINYLAKEKLFIGYGNGQFGFGDNITRGQVALLIQRY
LKLENKLEQKTMFTDTKGNMYEQAIDAVVQAGIMTGDGNGKFRPDGVLTRYEMSVVLQKVFQLKENENSV
ENFKDVPTGHWAEGYVKALVDNNISKGDGKGNFLGDDFVTREQYAQFLYNAITK
>gnl|CDD|467987 NF033191, JDVT-CTERM, JDVT-CTERM protein-sorting domain. This bacterial C-terminal protein-sorting domain, superficially similar to MYXO-CTERM (TIGR03901), occurs in a variety of Proteobacteria, including Janthinobacterium, Duganella, Vibrio breoganii, and Thioalkalivibrio, hence the name JDVT. Its local genomic context in species examined so far includes a homolog of eukaryotic type II CAAX prenylation site proteases (see PF02517). The architecture of the domain consists of a run of Gly residues and an invariant Cys residue (a probably modification site), followed by a hydrophobic predicted transmembrane alpha helix and then a cluster of basic residues, mostly Arg
GGGGGCSIGPDGAFDPTLPLLLLLALGVLGWRRRR
>gnl|CDD|467988 NF033192, JDVT-CAAX, JDVT-CTERM system glutamic-type intramembrane protease. See NF033191
LLSLVLLQPLLEEWVFRGGLQEWLLRRTWGRARLGGISLANLLTSAAFALAHLVAHPWLWALAVFVPSLL
FGLFYERSRSLGPCIALHAFYNAGFLAV
>gnl|CDD|467989 NF033193, lipo_NDxxF, NDxxF motif lipoprotein. Members of this family are lipoproteins, about 200 amino acids long in precursor form, found in Staphylococcus aureus, Bacillus cereus, and various other Firmicutes. The protein family is named for one of its several highly conserved motifs
KKFIILSLLLLLSLILSACSNGDDDDEDHDVNAPKNVKKLIPKDIFSSSKKNEKISEKEMKKSIKKYLDV
NSDLLDNKYPLQHKLDDSDTKLTKKQAKKLSKLSNLAKKNDMNFKNFIKNNTLPKGYKKNTERISKYFTA
LNSTIANLDKKIEELNYQPQNTINVVDVPTKYAGDVNGKQQKKIEKFLKKKNIKTKAFD
>gnl|CDD|380197 NF033194, lipo_EMYY, EMYY motif lipoprotein. Members of this family are lipoproteins, about 300 amino acids long in precursor form, found broadly in the genus Staphylococcus and in some related species
KKILLIILLLLLVLILSACGNKLESDLKQFESQMKDVEQKEKEVNKTLDEIDLKQLDDLSKTDTTDKNKK
EFNQLQKDIDKELVPKFKAYEKAAKQLPAENEEVKELKSTYLESVEKKEDFINQLKEFVDLYNQSIKSNE
DILDYTQLFEKNRSEVEKNIKKAKSSGETEEIDQLIDKLEENNKELKETAEKLLEDEDVKEKQQAIDEEI
MPLIEKQIKDLNQTNISDDHVNRARKNAIEMYYSLQNYYEERKKTIEISEKLQKIDIQNLPKTGEDLEKY
DETYNEELDELK
>gnl|CDD|467990 NF033195, F430_CfbB, Ni-sirohydrochlorin a,c-diamide synthase. Members of this family are Ni-sirohydrochlorin a,c-diamide synthase, involving in synthesizing coenzyme F430, used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) the enzyme cobyrinic acid a,c-diamide synthase, involved in cobalamin biosynthesis
RVLIAGDRSGSGKTTITTGIMAALSKGYNVQPFKVGPDYIDPSYHTGATGRPSRNLDSFFMSEEQIREVF
AHGCKGADIAIIEGVRGLYEGIESLGDVGSTASIAKALNAPVILVINARSITRSAAAIVKGFKAFDPDVN
IAGVILNNVGGERHAKKAKEAIEHYTGVPVIGAIPRDEEMKLSMRHLGLVPAVEGRERGEFLERIEKIGE
IIEENLDLDALLEIAKEAFPLPEPEEDLFLWEENKNDVKIGVALDEAFNFYYADNFDALEANGAEIVYFS
PLHDEELPDVDGLYIGGGYPELFAAELEANKSMRESIREFSGDGTPIYAECGGLMYLTESIDLQGKGEES
SYEMVGVFPGHTVMKAVRVLSYVIGEFSKDCPIGKKGETFRGHEFHYSKVTLDPETKFAYKLSRGTGIID
GLDGLVVNNTLGSYTHLHAVSYPGFASSFVE
>gnl|CDD|467991 NF033196, c_type_nonphoto, c-type cytochrome. Members of this family are apparent c-type cytochromes that resemble the photosynthetic reaction center c-type cytochrome (PF02276) but are smaller and found in non-photosynthetic organisms
KNLKVLPKDISKDQLDSIMKGFSAALGVKCNFCHAPNKENKKLDFASDEKPEKEIAREMMRMTNDINKKY
FKKDKEDDEGLPVVTCYTCHRGKTHPE
>gnl|CDD|467992 NF033197, F430_CfbE, coenzyme F430 synthase. Members of this family are coenzyme F430 synthase, involving in synthesizing coenzyme F430, which is used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) MurD, an enzyme of bacterial cell wall biosynthesis
LVLDTNHGGLILARELRGLGYDVDAVDVYGKLEKDDLFLLEEKGIISKKEAPFSDYDLVIAPVHCPPDGK
PFITHHEAVGEILKKKYGRIPKKFIEITGVKGKTTTAELLAHILSDEYVLLHTSRGTERYPEGELSNKGS
ITPASILNALELAEEIGIDDYGFLIFEVSLGGTGAGDVGIITNILEDYPIAGGKRSASAAKLQSLKNAKV
GSINVADLGIYINGKNKLVITVAGVEILSKYPLRFKYGNTEFEFNPLLFGPHYRENSLFAIEAALNLGVD
PEDIISALKGFKGLPGRMAVKKEGGVVIVDNINPGLNVKAIEYALDDALELLGDGTLVIGGDFGVVCEEI
DIDKLSEVLKKYRPKIDILVGVGTELGKRLKKYLDKLEGYEAGTLEEGLDDARELTGEGNTLVIYRKTW
>gnl|CDD|467993 NF033198, F430_CfbA, sirohydrochlorin nickelochelatase. Members of this family are sirohydrochlorin nickelochelatase, involving in synthesizing coenzyme F430, used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) sirohydrochlorin cobaltochelatase, involved in cobalamin biosynthesis. Some members of this family are double in length because of a duplication
GILLVGHGSRLPYNKEVIESIAEMIKEKGDYYIVEVGFMELNEPTIPEALDKLAGEGVDKIIVVPVFLAH
GVHTTEDIPEILGLDEGTDEGTIEFDGKEVEIVYAEPIGADPRIADIILDRAKE
>gnl|CDD|380202 NF033200, F430_CfbC, Ni-sirohydrochlorin a,c-diamide reductive cyclase ATP-dependent reductase subunit. This family, very closely related to the nitrogenase iron protein, was identified as a subunit involved in biosynthesis of coenzyme F430 in archaeal methanogens and archaeal anaerobic methanotrophs
KQIAIYGKGGIGKSTTVSNLAAALSEEGKKVMVIGCDPKADSTRTLMGGRRIPTILDLLRENKNIKEEDV
VFEGYGGVRCVESGGPEPGVGCAGRGIIVAMQLLEKLGAFMEDLDVIIYDVLGDVVCGGFAVPLREGYAD
EVYIVTSGEYMSLYAANNICKGIKKLKGRLGGIICNSRNIENEEEIVEEFAERIGSRLIGFIPRSELVQK
SELEAKTVIEKAPDSEQAAVYRKLAKKIMENTDFVIPEPLEDEELEELFR
>gnl|CDD|467994 NF033201, Vip_LPXTG_Lm, cell invasion LPXTG protein Vip. Vip (Virulence protein), like the LPXTG-type internalins, is an LPXTG-anchored surface protein of the mammalian cell-invading pathogen Listeria monocytogenes, but absent from the related species Listeria innocua. For certain cell types, Vip is required for Listeria's ability to invade. It appears to bind the endoplasmic reticulum (ER) resident chaperone Gp96 as its receptor
MNKYFKNLATVLFTVSLLTTSITALPAMASAYEETHNASTIYISPLDAPHVGDTKITGKTTALSSFAIAI
YTPEGRLTGTFFGTTNAAGTYAVDLSDFTYYDPLGYEASGNVILEKGAMVRSMTETNSDLIKTVTINYNY
IQTAINELFLNNDPTGTILAATDQNAINAVQEQINTVTSSEKETFQEQLNNAQQQLDARIAQEQAAIQAV
NQLFLEDNPANSIKAETTQDLIDQAQTLVDVLPASELKDTLQANIVKAQTELDERSKPVTPPKNDPETDN
PEEPVTPVDPATPTPDEPSTPTDPATPTPDEPSTPTDPATPEKPEITTPENPESTVVESDSSENEPEKSA
DSKIVNNPIQITSQATKQATKQAKSSVTKTTTLPIPKTGDTETTSSILFGTLMLASLALFRRKK
>gnl|CDD|380204 NF033202, GW_glycos_SH3, GW domain. The GW domain of Listeria belongs to the clan of SH3-like domains. A similar but broader model (PF13457) occurs in Pfam. The GW domain occurs as repeats on surface proteins of the cell-invading pathogenic bacterium Listeria monocytogenes, and is involved in binding to glycosaminoglycans. Members of this family include the GW-type internalin InlB and several paralogs
DKIEYEKAVNLTAYVKNAKGNGIWSKPYNTDGAKKVGTLSSYKNKKLKIDREAKTEGGTWYQFKDNGKVI
GWIDAKALTIF
>gnl|CDD|380205 NF033203, entero_EhxA, enterohemolysin EhxA. Members of this family are the RTX toxin called enterohemolysin or EhxA, because it is found in enterohemorrhagic Escherichia coli (EHEC) strains such as O157:H7
TVNKIKNIFNNATLTTKSAFNTASSSVRSAGKKLILLIPDNYEAQGVGINELVKAADELGIEIHRTERDD
TAIANQFFGTAEKVVGLTERGVAIFAPQLDKLLQKYQKVGSKIGGTAENVGNNLGKAGTVLSALQNFTGI
ALSGMALDELLRKQREGEDISQNDIAKSSIELINQLVDTVSSINSTVDSFSEQLNQLGSFLSSKPRLSSV
GGKLQNLPDLGPLGDGLDVVSGILSAVSASFILGNSDAHTGTKAAAGIELTTQVLGNVGKAVSQYILAQR
MAQGLSTTAASAGLITSAVMLAISPLSFLAIADKFERAKQLESYSERFKKLNYEGDALLAAFHKETGAID
AALTTINTVLSSVSAGVSAASSASLIGAPISMLVSALTGTISGILEASKQAMFEHVADKFAARINEWEKE
HGKNYFENGYDARHAAFLEDSLSLLADFSRQHAVERAVAITQQHWDEKIGELAGITRNADRSQSGKAYIN
YLENGGLLEAQPKEFTQQVFDPQKGTIDLSTGNVSSVLTFVTPTFTPGEEVRERKQSGKYEYMTSLIVNG
KDTWSVKGIKNHKGVYDYSNLIQFVEKDNKHYQARIISELGDKDDIVYSGAGSSEVFAGEGHDTVSYNKT
DVGKLTIDATGASKPGEYIVSKNMYGDVKVLQEVVKEQEVSVGKRTEKIQYRDFEFRTGGIPYDVIDNLH
SVEELIGGKHDDEFKGGKFNDIFHGADGNDYIEGNYGNDRLYGDDGDDYISGGQGDDQLFGGSGNDKLSG
GDGNNYLTGGSGNDELQAHGAYNILSGGTGDDKLYGGGGIDLLDGGEGNDYLNGGFGNDIYVYRQNYGHH
TIADEGGKGDRLHLSDISFDDIAFKRVGNDLIMNKAINGVLSFNESNDVNGITFKNWFAKDASGADNHLV
EVITDKDGREIKSDKIPHNNNERSGYIKASNIASEKNMVNITSVANDINKIISSVSGFDSGDERLASLYN
LSLHQNNTHSTTLTTTV
>gnl|CDD|467995 NF033205, IPExxxVDY, IPExxxVDY family protein. This protein family is uncharacterized. Member proteins average about 160 amino acids in size, and feature two widely separated invariant Asn residues, as well as the larger (though less invariant) motif for which it is named. Members are found primarily in the Flavobacteriia branch of the Bacteroidetes
HKLDLDDFYEDDFKLIAIHSSLEDYKLAYLLNKLLGINLSRSKDLDLDFNYNQASFSIFEYEDEEEHVTW
YLIANKSKGEEQKVLSSLFEESETTQYLIPELKKVDYFLKIEDTEDQFDLFSLILKLNKIPFIQTAYEID
PEKLKSKENLIF
>gnl|CDD|467996 NF033206, ScyE_fam, ScyD/ScyE family protein. This family includes ScyE, a protein involved in scytomenin biosynthesis and export, and its paralog ScyD. Some members of the family contain a C-terminal PEP-CTERM domain that predictions anchoring to the outer membrane
TVVADGLNNPRGLAFGPDGRLYVAEAGTGGCPSPSPLCYGNTGAVSRITPDGKKTRVVTGLPSLALGEGA
AGPADVAFDGDGTYYVLTGLGGDPATRDGGPLLGTLLKVDLGTGSLTTLADLAAYEAANNPDGGDVDSNP
YGLAIGGGTLYVADAGANALLRVDADGKVSTVAVLPPRPVTIPAGPPPGLPLPDCPVGYPAQAVPTGVAV
GPDGALYVSELTGFPFPPGRARVYRVDPGGAPTVYATGFTGLTDLAFDPDGNLYVLELAGGGLLKGDPTG
SLIRIAPDGTRTTLLDGLELPTGLAVGPDGTLYVTNNGLLPGDGQVVRID
>gnl|CDD|467997 NF033207, midcut_by_XrtH, midcut-by-XrtH protein. Members of this protein family occur in bacterial genomes that encode the exosortase/archaeosortase family member XrtH (exosortase H). While many targets of XrtH are C-terminal protein-processing signals described by TIGR04174, the IPTL-CTERM domain, members of this family have a version of that signal in the N-terminal half of the protein. This architecture suggests that XrtH may performs a cleavage that releases the C-terminal domain of midcut-by-XrtH proteins from the membrane, perhaps as part of some regulatory pathway
RRRGALALVAGLLLAAGAAAQSGGVTITYAPVAAASVPTLSEWGLLLLALLLAVLAYRALRRRGQGRPLA
ALLLAGGALLAAGWGGPALAAPVGDLSLTNPAGGTVNIPAHPDFFGDGFERYTVTNTSGVTQRITGITVT
PGYTCPNPGPTPTCTVGLTLAPGATCYVRVS
>gnl|CDD|467998 NF033208, choice_anch_E, choice-of-anchor E domain-containing protein. This HMM describes a domain just over 100 amino acids long and usually found in tandem copies. Members appear to be extracellular proteins that have some C-terminal anchoring domain, usually PEP-CTERM but occasionally a type IX secrection (T9SS) recognition domain
TYSTTFALTTTDWINETLTFPKFDSSLGTLTSVTLTLTGDLTGSGGVENTGASAASTVTVTLGSTLTLTS
PDGSSLLTDLPTTSGSFNLAAFDGTTDFAGTSGVTFGNLSASGSGSVTFTDASDLSAFIGTGTVDFLFTA
LATTSSVSGSGNITSGINTTASAGVTVTYTY
>gnl|CDD|467999 NF033210, RBP7, reticulate body protein Rbp-7. Members of this family are the 7-kDa reticulate body protein found in several species of Chlamydia. The protein is often overlooked during genome structural annotation; members observed so far are 65 to 67 amino acids long. The protein has been demonstrated by mass spectroscopy, and shown to be present only in reticulate or intermediate bodies
MQHTIMLSLENNTEELASALQRITTASSCVLSASKESESDKQPYEVSQAESTLSVEASKISSVAEGTLLE
CCCK
>gnl|CDD|439396 NF033212, SapB_AmfS_lanti, SapB/AmfS family lanthipeptide. Members of this family are class III lanthipeptide precursors. These typically are short peptides, encoded next to the gene for the lanthipeptide synthetase that creates the characteristic lanthionine (or beta-methyl lanthionine) bridges for which these natural products are named. Members of this family include SapB and AmfS, which are considered morphogens rather than antibiotics. Members also include labionin-containing peptides such labyrinthopeptins A1 and A2
MALLDLQTLETPEAEAGGGGGGSTASLLLCGDSSLSLLLC
>gnl|CDD|411104 NF033213, matur_PanM, aspartate 1-decarboxylase autocleavage activator PanM. Members of this family, called PanM (or PanZ), although related to the GNAT family N-acetyltransferases, have a different function. Then enzyme PanD, aspartate 1-decarboxylase, has an active site modified Ser residue, created by cleavage of a precursor form. PanM promotes the maturation of the CoA biosynthesis enzyme PanD, but also inhibits its activity in the presence of CoA. Figure 6 in PMID:26276430 identifies residues considered critical to interaction with PanD; seed alignment sequences and cutoff scores were chosen to separate proposed PanM from functionally distinct relatives
MKLTIIRLTTLSEQDRIDLAKIWPEQDPDQLQAWLDEGHRLYAARFNDRLLGAVKVTIDGTQGELSDLCV
REVTRRRGVGLYLLEETLRQNPEIKHWWLALADVGVEDRAVMAAFMQACGFSAQSDGWEK
>gnl|CDD|468000 NF033214, ComC_Streptocco, competence-stimulating peptide ComC. Members of this family are ComC, a secreted peptide that stimulates competence for natural transformation in Streptococcus. ComC peptides fall within the broader family of PF03047, a homology family of pheromone/bacteriocin precursors that is also restricted to Streptococcus. The PF03047 HMM runs only a few residues past the GlyGly precursor peptide cleavage site, and thus does not distinguish ComC from other pheromone precursors, such as BlpC
MKNTVKLEQFVALKEKDLQKIQGGEMRLSDFIRDFIFFRRK
>gnl|CDD|380214 NF033215, BlpC_Streptocco, quorum-sensing system pheromone BlpC. Members of this family are BlpC, a peptide pheromone that stimulates production of BLP (bacteriocin-like peptides) family class II bacteriocins. BlpC peptides fall within the broader family of PF03047, a homology family of pheromone/bacteriocin precursors that is also restricted to Streptococcus. The PF03047 HMM runs only a few residues past the GlyGly precursor peptide cleavage site, and thus does not distinguish BlpC from other pheromone precursors, such as ComC
MDKNQNLTSFQELTTTELNQITGGGWWEDLLYSINISKHNITKGLHQPIQL
>gnl|CDD|468001 NF033216, lipo_YgdI_YgdR, YgdI/YgdR family lipoprotein. Members of this family are exclusively lipoproteins of small size, including YgdI and YgdR from E. coli K-12
KKLLAALLAALALLALAGCSSPYVITTNDGRTIVTDGKPEYDKDTGLYEYEDADGKTQQINKDDVKTIKE
L
>gnl|CDD|380216 NF033217, Fur_reg_FbpC, Fur-regulated basic protein FbpC. Members of this family are FbpC, Fur-regulated basic protein C. This protein has also been described as MrgC (metal-regulated gene C). Members of this family are found so far only in the genus Bacillus, although the small size may have interferred in gene-finding
MTMFFLLAAVCTYSLLIGFVLKGISNKSA
>gnl|CDD|468002 NF033218, anchor_AmaP, alkaline shock response membrane anchor protein AmaP. The founding member of this family, AmaP (Asp23 membrane anchoring protein), is related to Asp23 through part of its length, but includes a highly hydrophobic N-terminal region that should make it an integral membrane protein. Asp23 (alkaline shock protein of 23 kDa), described in PMID:7864904, is a cytosolic protein in Staphylococcus aureus, strongly induced by a pH shift from 7 to 10, and also recruited to the membrane. AmaP appears to be the partner protein with an integral membrane segment and the ability to anchor Asp23 to the membrane. This model was built to identify full-length homologs of AmaP, while excluding Asp23. Some but not all members of this family score above the cutoffs of Pfam model version PF03780.11, but full-length homologs of Asp23 score considerably higher. Asp23 family members previously were known as DUF322
MKKFKKFLLSLLGLLLLLLLGFVILLYLPPWLLTFFQLYPLINPWLQPYLFWVAAVLLLLALILLLVALF
YPKTRKELVLKTDDGKLTISKSAIEGFVREALSKVDGVRNPKVKVKLKKRKIKVDVKGDLDPRSNLPELT
EEIQEEIKEGLEELLGIPVKKVKVKV
>gnl|CDD|468003 NF033221, ANT_6_Ig, aminoglycoside nucleotidyltransferase ANT(6)-Ig. Article PMID:27154456 describes a streptomycin resistance protein, "Campylobacter ANT-like protein A", highly similar to WP_002785795.1, and reports internal primers that match exactly to genes encoding WP_002785795.1. Campylobacter ANT-like protein A was shown to confer resistance to streptomycin. This model identifies proteins from this family, including WP_002785795.1. The most closely related sequence found by database search was the family of "Campylobacter ANT-like protein B", such as WP_038855261.1, which also is found in Campylobacter coli but which could not be shown to confer resistance to streptomycin
MQNQDKFLKQFKKLALCDENIRLVTLEGSRVNKKAKKDKYQDYDVSFFVPLDKMKDFLGLNEKQNFNECK
NLPKCILELEKSSYFKKILMLQMPECMEFYPPDLPQNWISFLVLFESGVRLDLTIIPLEDLKNYYEFEPL
SQALLDKNGLFTHTIPKAPFSITHLSQRSFDDVCNEFYFLYSCLKKALLRKQFILSNHLLNSLRKALFDL
LSFKIGLNFGFEIWLGKEYTNILEFLEEKEVKIILKSFNTATLEHIKKARKKLEILFHKNAKFVAKKSDF
KLFPYRKNVKRYCKILGKL
>gnl|CDD|380218 NF033222, listolys_S, listeriolysin S family TOMM bacteriocin. Members of this family include listeriolysin S from some strains of Listeria monocytogenes, and staphylolysin S. Members are encoded in biosynthetic clusters similar to those for streptolysin S (found by model TIGR03602), a precursor similar in length, architecture, and composition, but different enough to require a different HMM
MNINSQSLNGYSETGTGSEAMNYAAGCCSCSC
>gnl|CDD|380219 NF033223, YHYH_alt, YHYH domain. Proteins with this form of YHYH motif-containing domain have it located near the N-terminus of a protein just after a signal peptide region. The domain has two characteristic motifs, GxC and YH[YC]H, separated by a short spacer region of variable length. A different family of YHYH domain-domaining proteins, in which the YHYH domain is more C-terminal and is repeated, is described by Pfam model PF14240
AYAHPGGTDSNGCHTNRKTGEYHCH
>gnl|CDD|380220 NF033224, PmrR, LpxT activity modulator PmrR. Members of this family are PrmR, and extremely small protein at 29 amino acids in length
MKKRIYESLTTVFSVLIVSSFLYIWVTTY
>gnl|CDD|380221 NF033225, spore_CmpA, cortex morphogenetic protein CmpA. Members of this family are CmpA (cortex morphogenetic protein A), a small protein (37 amino acids) involved in endospore formation and frequently missed during genome annotation
MPQWLKNQLRRAFLEKDRRQIKLLNQCWFFYRKKNK
>gnl|CDD|468004 NF033226, small_MntS, manganase accumulation protein MntS. Members of this family are MntS, a small protein of about 42 amino acids that seems to play assist bacteria in accumulating manganese when iron is limiting. It may function as a manganese chaperone, or may inhibit manganese efflux transporters
MNEFKRCLRVFSHSPFKVRLMLLNMLCDMFNGKPQQDDKPS
>gnl|CDD|380223 NF033227, Fur_reg_FbpB, Fur-regulated basic protein FbpB. This model describes FbpB (Fur-regulated basic protein B), one of three paralogous small proteins recognized by Pfam model PF13040 in Bacillus subtilis
MSKRKIKTYHQLVEEYKKEIMRSPKEMDMIYDRIDRKHQKRLL
>gnl|CDD|380224 NF033228, div_inhib_SidA, cell division inhibitor SidA. This protein, SidA (SOS-induced inhibitor of cell division A), is found so far in Caulobacter and Phenylobacterium. It interacts with FtsW
MIRLARESLALVSVASFVWMMCTVAQLVA
>gnl|CDD|380225 NF033229, small_MgtR, protein MgtR
MNRSPDKIIALIFLLMSLLVLLLALWQIVL
>gnl|CDD|411106 NF033230, phage_region_01, phage region protein. Members of this family are found broadly in the Gammaproteobacteria and may be a marker of temperate phage or prophage. A member (YP_008766900.1) occurs in Shigella phage SfIV
SKYSNLFQAIKKRVAENRGISYSGNVDSPDDSKARNRAAQIFLLEILLHEHRKKYATPFNPLSGKKALHH
LIFTKTKWSPSEIRSLSLNDALFVLQDELKPENLPEEAQEFLRSLNLSSYSYGFDDFSEEEWDPELNDKF
LK
>gnl|CDD|380226 NF033231, small_Blr, division septum protein Blr. Members of this family are Blr, named beta-lactam resistance protein because mutants have heightened sensitivity to beta-lactam antibiotics, but actually involved in cell division. The protein is very small
NRIVELIGWIVLGVSVILLGVAHHIDNYQPPEPVAAVQKK
>gnl|CDD|380227 NF033232, small_YtzI, YtzI protein. Members of this family include YtzI from Bacillus subtilis, and homologs widely distributed in the Firmicutes. The pattern of sequence conservation suggests the protein begins with a hydrophobic stretch without any basic residue near the initiator Met residue. Members of this family average about 53 residues in length. At the time this model was constructed, members were included in Pfam model PF12606.6 (Tumour necrosis factor receptor superfamily member 19), seemingly in error. This model was constructed to separate the two families
MTIVIIISIIIVLIVLALSVLTTSKGYAYKHTVDPLPDEPH
>gnl|CDD|380228 NF033233, twin_helix, twin transmembrane helix small protein. Members of the seed alignment for this family are small (average length 68 residues), strictly bacterial, and extremely hydrophobic. Pfam model PF04588 (HIG_1_N) includes both eukaryotic proteins, including a protein from the fish Gillichthys mirabilis, and the members of this family. Similarity between those eukaryotic proteins and the members o this model may represent convergent evolution related to the similar composition of their transmembrane alpha-helical regions, rather than a common origin or common function
KILIVIALLAVLASLGSGLFFLMRGGDSNRSNKLMRWRVGLQAVAILLILLALYLGGI
>gnl|CDD|380229 NF033376, lat_flg_LafA_1, lateral flagellin LafA. This HMM describes rare second type of flagellin from E. coli and some closely related species, called LafA, where the familiar and common flagellin, FliC, is nearly universal and carries the H-antigen used for serotyping strains. In contrast to FliC, whose center region is highly variable, LafA shows little variability in sequence. In many E. coli strains, the Flag-2 locus either is absent or is cryptic, appearing degraded and non-functional
MLSINTNNASMAAVNAISKSSSSLSTSMERLATGDRINSSADDAAGKQIANRLTAQSSGMDVALSNINDA
TAMLQTADSMFDEMSDVLGRMKDLSTQAANGTYSDDDLQAMQDEYDELGQQMSDMLQNTTYGGTNLFGVS
GTSNTGTDGLFQSAVTFQVGAESSDTMTVNISSQLNQLVTDLSAISNSFSADQADTTGTAGVSGGTELTA
SGSANQMINSISTAMDDVSQIQSKLGASINRLNDTANNLTSMQDNTEVAIGNIMDTDYATEASNMTKQQV
LMQTGITMLKQSNSMSSMVSSLLQ
>gnl|CDD|468005 NF033377, OMA_tautomer, 4-oxalomesaconate tautomerase
MRGGTSKGPFFLASDLPADPAERDAVLLAAMGSPDPRQIDGIGGADPLTSKVAIVSPSTRPDADVDYLFA
QVSVDEARVDTAPNCGNMLAGVGPFAIERGLVPAQGGETTVRIFNVNTGQIAEATVQTPGGRVEYEGDAR
IDGVPGTAAPVPLNFLDAAGSKTGALLPTGNARDVIDGVEVEVTCIDNGMPVVLIRAADLGLTGYESPAE
LDADTALKARLEAIRLQAGPLMGLGDVSDKVVPKMVLVAPPRAGGAISTRYFIPHRCHASIGVTGAVSVA
TACLLPGSVAHGLAGLPGGGRKRVSVEHPSGEFDVELELDGEVAGEVTRAGLLRTARKLFDGEVFVP
>gnl|CDD|380231 NF033379, FrucBisAld_I, fructose-bisphosphate aldolase class I. This family consists of fructose-bisphosphate aldolase class I. All members of the seed alignment are from prokaryotes, although class I is the common form in plants and animals. The common form in prokaryotes is class II
ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPGLGDYISGVILFDETIR
QKTADGTPFPKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIG
DGIPSRACIEANAHALARYAALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLE
GMILKPNMVLPGKDCPDQASPEEVAEATVRCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLGPLPW
PLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARMNSLAAL
>gnl|CDD|380232 NF033380, Rlm_2499C5, 23S rRNA (cytosine(2499)-C(5))-methyltransferase. This model describes a 23S rRNA modification related to RlmI of E. coli, but that modifies site C2499 rather than C1962
RLRLRVTAAAESHLRAGHPWVYESSVREQNREGEAGELAVVYDRRDRFLAIGLYDPHSPLRLRVLHAGSP
VTLDDAWWAARLDAALARRAPLFGPDTDGYRLLNGESDGWPGLVLDRYADTLVLKLYTAAWFPHLPRVLG
LLAERFPGFRVVLRLSRNIQDRAAEAGLHDGQTLVGDLPDGPVVFRESGLAFEADVVRGQKTGFFLDQRE
NRRRVEGLARGRRVLNAFSFSGGFSLYAARGGAREVVSLDISAHALASAERNFALNPGLAAPHETVQADV
FEWLTDTRREFDLVILDPPSLARREAEREGAIRAYGKLAADGIRRLAPGGILVSASCSAHVSAEEFFEAV
RGAARRSGRRWRELRTSRHAPDHHASFPEAEYLKAIYLQFD
>gnl|CDD|468006 NF033381, MonaBetaBRL_TX, monalysin family beta-barrel pore-forming toxin. Members of this family are secreted in a water-soluble pro-toxin form, but undergo cleavage and oligomerization to form beta-barrel pore. The founding member of the family is monalysin from Pseudomonas entomophila. This family is built narrowly, and therefore excludes a set of pore-forming proteins (not necessarily toxins) from a eukaryote, Dictyostelium. Analogous (but perhaps not homologous) beta-type pore-forming toxins include aerolysin and leukocidin
GFPVKRGSYEIERYLLGGDELHPGCWVDGETVYGDVRIGGQNWATYTRPVFAYLEYVDTVRVPSAGEQTR
EVSVAQGHSKSFTKSVEASYSVSAAIDLVNVGSELTTGFSSTEAWSPSTSRKHTLEVKGPGTFYIYQVHL
VYAHCATSAGDQLADLFKYSKTSLVGDNDGREDLYFLSSVATDQLVAVASENSVAPLSWDQLQQAVLIEG
YEAAGNAGRWSFDYSAYNNP
>gnl|CDD|468007 NF033382, OMP_33_36, porin Omp33-36. Members of this family are outer membrane beta-barrel proteins that facilitate passive transport from the extracellular milieu into the periplasm. Known members are limited to the genus Acinetobacter, and the name, Omp33-36, reflects variability of this protein across the lineage. Note that this HMM previously was named CarO in error. Both this protein and CarO affect carbapenem transport across the outer member and thus carbapenem susceptibility or resistance
MKKLGLATALLLAMTGAQAYQFEVQGQSEYIDTTANDKNFTGAVQGTYYFKNVDASKGPLAEAAFLNQAS
NVSLAYNYAEYDQKNTVDVKSHTYGVKGEAYVPTPYVPVYASASYSHTITDGKNNGSRDDNGDRYALEVG
AMLAPNFLVAVGYTSVADQFALDAFNILNNGVAKAVGESATIGEDQDAVTARTKYVGAIDGTNMAVGFEA
GLVYGEDTAYGLKTDLYLTPKLSVGASYAESSFSGSPDSAWGANVNYFITPAVAVGASYVNANAKNGVAL
DTQTVGLNAKFRF
>gnl|CDD|439397 NF033383, induct_EntF, EntF family bacteriocin induction factor. Members of this family have leader sequences like bacteriocins (see TIGR01847), but characterized examples function as signaling peptides that induce production of a nearby encoded bacteriocin, rather than as bacteriocins themselves. The founding member of this family is enterocin induction factor EntF
VKKLSEKQLKQIKGGSGGTQLGKPASNIAQCVFSFFKKC
>gnl|CDD|380236 NF033384, enterocin_MR10, enterocin L50 family leaderless bacteriocin. Members of this family are leaderless peptide components of bacteriocins in which the two subunits share about 74% identity with each other and are each about 43 amino acids long. Members include enterocin subunits L50A and L50B, MR10A and MR10B, etc
MGAIAKLVAKFGWPLVKKYYKQIMQFIGEGWSIDQIADWLKRH
>gnl|CDD|380237 NF033385, enterocin_LsbB, LsbB family leaderless bacteriocin. Members of this family are leaderless peptide components of bacteriocins with a conserved motif KXXXGXXPWE
KKFPNPYTLVAKLTTYEIAWFKNKHGYYPWEIPRC
>gnl|CDD|468008 NF033388, ubiq_like_UBact, ubiquitin-like protein UBact. This HMM describes a protein family that includes most, but not all, of the proteins designated UBact (a ubiquitin-like protein) in the article first describing a biosystem related to bacterial pupylation. Protein modification by ubiquitin in eukaryotes, pupylation in many bacteria, and this system is a few other bacteria, is considered a signal that can trigger altered protein handling such as rapid degradation. Proteins that the authors consider members of the same family, but that show very little sequence similarity other than protein size and the final two residues, include WP_008669967.1 in the genus Rhodopirellula and OHA48658.1 in Candidatus Terrybacteria
ERKTRPQPPGRKPGGDGPGPKRPDVEKPDTDELLKRMKKVDPDQAERYRQRTGE
>gnl|CDD|439398 NF033389, scrub_typh_TSA22, major outer membrane protein TSA22. Members of this family are TSA22, one of three major outer membrane proteins, the so-called type-specific antigens, in two species of Orientia, including O. tsutsugamushi, causative agent of scrub typhus. The other type-specific antigens are TSA47 (a serine proteins in the DegP/HtrA family) and the much better known TSA56, which is quite variable in size and may be used for strain typing
MSKEATELKESMDRAMESASQNSSISAEQKVQLENEKKELQGQISDISGKDEQEQQTTLQKLKEWMLKIK
DFIMSDDFSKLVDSMVQFVQTAVKVSTEMVQAFTGMKDKGIMGVAAGIQTVTHGVKDITQSVKDMVEAGE
AAQKHFSSPEDKMKEILGAEGLAKLQAASAGLQSNASIASSSASVSTPTAARSSQKDSSIAR
>gnl|CDD|468009 NF033390, Orientia_TSA56, type-specific antigen TSA56. This protein is the immunodominant major cell surface protein of Orienta tsutsugamushi, known as "56-kDa type-specific antigen" or TSA56. It should not be confused with unrelated proteins TSA47 (a serine protease) or TSA22. An ortholog is found in Orientia chuto, and included in the seed alignment
MKKIMLIASAMSALSLPFSASAIELGDEGGLECGPYAKVGVVGGMITGVESTRLDPADASGKKKLSLTTS
MPFGGTLAAGMTIAPGFRAELGVMYLMNVTAEVEAGKSKGDSDGADSNVGADAPIRKRKKLTPPQPTIMP
ISIADRDRGIDIPNQPQAQAPQPQLGAEQRAAERIAWLKNYAGIDYMVPDPNNPQGPRIINPVLLNIPQG
NPNANPRQAAQPFDILDHEQWRHLVVGIAALSNANKPSVSPIKVLSDKITKIYSDIRPFAKIAGIEVPDN
PLPNSASVEQIQNKMQELNDLLEEIRESFDGYLGNAFANQIQLNFVMPQAQQQQQGQQQQQAQATAQEAV
AAAAVRALNGNDQIIQLYKDLVKLQRHAGIKKAMEQLAAQEEDQSGDGKKQGVAPCSKAGGASEKGKKDK
KKETEFDLSMIVGQVKLYADLFTTESFSIYAGLGAGLAHTSGKIDGKDIKAHTGMVASGALGVAINAAEG
VYVDIEGSYMHSFSKIEEKYSINPLMASVGVRYNF
>gnl|CDD|468010 NF033391, lipid_A_LpxO, lipid A hydroxylase LpxO. Members of this family are LpxO, an enzyme that modifies one of the lipid chains in lipid A by hydroxylation, with resulting changes in resistance to the host immune response and to the antibiotic colistin. This family, as built, includes LpxO1 from Pseudomonas aeruginosa, but not its paralog LpxO2
KWIILAIFIASVLYVHFRGRVRHKFSRQLSDHSTFMAPINCFMYLFSRVPNTPYLPTEEFPELQPLQDNW
EVIRDEALALQEAGHIKAAEKYNDAGFNSFFKTGWKRFYLKWYDDAHPSAEALCPRTTALLRSIPSVKAA
MFAELPPGSRLVRHRDPYAGSLRYHLGLATPNDDRCFIEVDGQRYSWRDGEAVVFDETYIHYAENKTDQN
RIILFCDIERPMKYRWAQAVNRWFGRNLMSAAASPNDEGDRTGGINRLFKYVYAIRLKGKRLKKRNRTLY
YLLKWALFGGIAALIIW
>gnl|CDD|380242 NF033392, PSM_delta, PSM-delta family phenol-soluble modulin. Members of this family are phenol-soluble modulins (short peptides, usually cytolysins) with an intact N-formyl-methionine at the N-terminus
MGIVSTIIEIVKTIVDIVKKFKK
>gnl|CDD|380243 NF033393, TRP47_fam_Nterm, TRP47 family tandem repeat effector N-terminal domain. This HMM describes a conserved N-terminal domain of a family of proteins found, so far, only in the genus Ehrlichia. The repeat region is followed by a long repeat region with a large content of acidic and serine residues, but other than in composition, the repeats themselves may be unrelated from one lineage to another. Characterized examples, such as TRP47 from Ehrlichia chaffeensis, are glycoproteins and are immunodominant antigens
LHLTTEITNIDFSNDLHIHSGDRFVVTSGDLQLDVGNHPGHGYHILFKNNGHVISDFHGVKAEDFNFDVK
NHSLNASFLVDPMAPFHELDVNNHPNFSINMHAAS
>gnl|CDD|468011 NF033394, capsid_maj_Podo, phage major capsid protein. A founding member of this family, AKO59007.1, was identified as the major head protein in Brucella phage 02_19 during a comparison of Brucella phage genomes. The N-terminal half appears to the better conserved region with fewer insertions and deletions
ELAEILATTLENYSKKVADQVSNNNPLLAALKKKGKVFPGGGEEIRVPLRYGGNSGAQWYTGYDTLPTAP
PDTLTAAEFPWKQAAGGISITGTELKANGGKEQLINLLESKIEDAEESLANSLERALYGDGTSSGKEITG
LGAIVPDTPTTTVGGIDRATNTWWRNQVADATGTATAATTALPAMERLWRQLSRGGKPDLIVAGSDFYDA
YEASLQANQRYTDAMLADGGFDALKFKGIPIVWDPGLDDAPAKRMYFLNTDYLKLRYHKDRNFVPLDPAR
PPNQDAYYAGITWYGNLVCSNRNAQGVLSIAT
>gnl|CDD|468012 NF033395, fibronec_SfbI, fibronectin-binding protein PrtF1/SfbI. PrtF1/SfbI is a fibronectin-binding protein a C-terminal region LPXTG region that mediates processing by sortase and covalent attachment to the cell wall. Near the N-terminus is a TED domain, which includes a Cys residue that forms a covalent thioester bond
MNNKMFLNKEAGFLAHTKRKRRFAVTLVGVFFMLLACAGAIGFGQVAYAADEKTVPNFKSPNPEFPWYGY
DAYRGAFLRYHDLKVNLNGSKEYQVYCFNLKKFEPRKETSSDKNWYKKLEGTAETFKKYAMNPRVGGEEL
EKNILSVMYNGYPNDGNGIMKGLEPLNAILVTQNAVWYYSDSSPYDIETLWESEAKEGKISESQVTLMRE
ALKKLIDPDLEETLVKKVPSNYKLNIFESSDKSYQNLLSAEYVPDDPPKPGDTSEHNPKTPELDGTPIPE
DPKRPDENLEPTLPPVMLDGEEVPEVPSESLEPALPPLMPELDGEEVPEVPSESLEPALPPLMPELDGEE
VPEKPSVDLPIEVPRYEFNNKDQSPLAGESGETEYITEVYGNQQNPVDIDKKLPNETGFSGNMVETEDTK
EPEVLMGGQSESVEFTKDTQTGMSGQTTPQVETEDTKEPGVLMGGQSESVEFTKDTQTGMSGFSETVTIV
EDTRPKLVFHFDNNEPKVEENREKPTKNITPILPATGDIENVLAFLGILILSVLSIFSLLKNKQN
>gnl|CDD|380246 NF033396, pilus_ancill_1, pilus ancillary protein 1
NRKPKQLTVTLVGVFLMFLTLVSSMRGAQSIFGEEKRIEEVSVPKIKSPDDDYPWYGYDSYDSSHPYYEP
FKVAHDLKVNLNGSKSYQVYCFNITSHYPSKKNSVSKQWFKRVDGTGDVFTSYAKTPRIEGEELNQKLLS
VMYNAYPNNANGIMKGIEPLNAILVTQNAVWYYSDSSQINPDELFKSEAKSNKINDQQLGLMREALSELI
DPNLGEKYSNKTPSGYRLNIFESHDKSFQNLLSAEYVPDTPPKPGEEPPAKTEKTSVIIRKYAEGDYSKL
LEGATLKLTQIEGSGFQEKIFQSNSSGETVELPNGTYTLTETKSPDGYKIAEPIKFRVKNGKVFIVQKDG
SQVENPNKEVAEPYSVEAYNDFSEDGYLSSGFRPYGKFYYAKNKDGSSQVVYCFNADLHSPPDSYDGGGT
IDPDISTMKEVKYTHVAGSDLFKYALRPRDTNPEDFLKHIKKVIEKGYKKKGDSYNGLTETQFRAATQLA
IYYFTDSADLETLKTYNNNKGYHGFEDMDEATLAVTKELIAYAQNDEAPQLTNLDFFVPNNSKYQSLIGT
EYHPDDLVDVIRMEDKKQEVIPVTHSLTVKKTVVGELGDKTKGFQFELELKDKTGQPIVNTLKTNNQDLV
AKDGKYSFNLKHGDTIRIEGLPTGYSYTLKETEAKDYIVTVDNKVSQEAQSTKASVTEDKTVTFENRKDL
VPPTGLTTDGAIYLWLLLLVPLGLWVWLIGRKGLKND
>gnl|CDD|380247 NF033399, thiazolyl_GetA, GE37468 family thiazolyl peptide
DLDDLPMDVFELADSGLTVESLTAGHGMPEVGASCSCFCGCCCSCSS
>gnl|CDD|468013 NF033400, thiazolyl_B, thiazolylpeptide-type bacteriocin
LELDLEELDLEIEVLEVDDTVALPETAASSGSSSCSSCSSCGSSS
>gnl|CDD|468014 NF033401, thiazolyl_BerA, thiocillin/thiostrepton family thiazolyl peptide. Members of this family include the precursor peptides for the antibiotics thiostrepton, nosiheptide, thiocillin, and berninamycin
ELDLDALEISDLIDESELDDETLSQVMAASCTTCICTCSCSS
>gnl|CDD|380250 NF033402, linaridin_RiPP, linaridin family RiPP. Linaridins are ribosomally translated, post-translationally modified peptide natural products, or RiPPs. Examples include cypemycin, SGR-1832, and legonaridin
MSILADFANTELVDVEPGRIGSDATPTMVTPLATLATPEATPVGFAATSATAAALNMVTHDVQ
>gnl|CDD|380251 NF033403, linaridin_rel, linaridin-like RiPP. Members of this family share N-terminal (leader peptide) sequence with the linaridin family of ribosomally translated, post-translationally modified natural product precursors
MSLVAEFANETLTDVTPGMLSETDSAMRLDAPADPVMSTPFLTVTVCLDGLTRGALAANIANYV
>gnl|CDD|468015 NF033404, YneK, putative protein YneK. Members of this family, YneK, are found so far only in Escherichia coli and Escherichia albertii, with 68% sequence identity but in identical gene neighborhoods. In E. coli O157:H7 strain Sakai, yneK has a nonsense mutation and is therefore truncated. The function is unknown
MVTPVSISNYISLPDDFPVRNIAPQVKEVLKDFIDALSIIICDEEWRTSLNINSATKKIFNNLDNLSYIQ
RTSFRDNDTLYNEKVQFKLTYPVKNGRHKENIEFQVVINLSPIYLDNFRHDGEINIFCAPDPKPVTMGRV
FQTGVERVLFLFLNDFIEQFPMISPGVPIKRAHTPHIEPLPPDHHTAADYLRQFDLLVLNFISRGNFVIL
PRLWNKSEVHRWFANKPPNLITAILDITDSELKEDLLQSLMDSLGSNKHVLPEVCICFLSLLAEQESPHF
QELFLFFANMLLHYQQFMNPNENDLNDVLIPASLSEDKIIKHMARKTLKLFVKNEIPPKVTHEDLVKNRP
RSPVRPPIPSTTKTPDLPERH
>gnl|CDD|439401 NF033405, FosLL, fosfomycin resistance glutathione transferase. This putative fosfomycin resistance glutathione transferase was detected in a mobile island in Acinetobacter baumannii D1279779 and is found in many other isolates as well
MKLSGLNHLTISVENVDRSFSFYKDVLGFTPRAKWNKGAYLSLGELWLCLSLDEVSISSDYTHYCFSISE
DDIDEFRQKIKLLNIREWKNNQSEGESIYFLDPDGHKLEVHVGNLSSRLESCKKNPYEGMVFFDE
>gnl|CDD|468016 NF033407, SnoaL_meth_ester, SnoaL/DnrD family polyketide biosynthesis methyl ester cyclase. This HMM represents mutually closely related methyl ester cyclases from a number of polyketide biosynthesis pathways. Examples include proteins designated SnoaL (nogalamycin biosynthesis), DnrD (doxorubicin biosynthesis), RdmA (rhodomycin biosynthesis), etc
MSEQIDVVRRMVEAYNTGKTDDVAEYIHPDYLNPATLEHGDLRGPESFAMAVKWVKMTFSEEAHLEEIGY
EENGDWVRAYLVLYGRHVGNLVGMPPTGRRFSGEQIHLIRIVDGKIRDHRDWPDYQGTYRQLGEPWPEDE
GWRP
>gnl|CDD|380254 NF033411, small_mem_YnhF, YnhF family membrane protein. Members of this protein family, are small membrane proteins, about 29 amino acids in length. YnhF from E. coli was shown to have an intact fMet residue at the N-terminus and to be chloroform-soluble. The previously generated narrow cluster PRK14756 includes some members of this family
MDTDLKFALLTTVGALAVILGFGLTAILH
>gnl|CDD|380255 NF033412, primase_PriX, eukaryotic-type DNA primase noncatalytic subunit PriX. In most archaea, the eukaryotic-type DNA primase has catalytic subunit PriS and a regulatory subunit PriL. The proteins in this family are PriX, an essential second noncatalytic subunit found in a subset of the archaea
RDYSWIEKVLEKGLPDGRKRFILYVASRYLVNVKGLSEDEAVKVIKDFYYKNGCGKIYDSWIRSVIRGVK
SKGLKPWSLKKIKEKDKELYEEIVKVLS
>gnl|CDD|380256 NF033413, RiPP_TM1316, Cys-rich RiPP peptide. Member of this family include the small, Cys-rich peptide TM1316 of Thermotoga maritima, encoded near the peptide-modifying radical SAM/SPASM protein TM1317 (AE000512.1). TM1316 is expressed at very high levels in stationary phase
MQKMPKPIIPNDYLKPGKGCGGAGLVCGWCG
>gnl|CDD|380257 NF033414, bottro_RiPP, bottromycin family RiPP peptide. Bottromycins are one of the rarer known classes of ribosomally translated, post-translationally modified peptide (RiPP) antibiotics
MGPAVVFDCMTADFLNDDPNNAELSALEMEELESWGAWDDDADQ
>gnl|CDD|468017 NF033415, thiovirid_RiPP, thioviridamide family RiPP peptide. Thioviridamide represents one of the rarer known classes of ribosomally translated, post-translationally modified peptide (RiPP) antibiotics
QAIEELVSQIKEAEAEMTALQRAIIDEKALSELAGVSPEELQAFLEEKAGISPDEEAQGSVMAAAATVAT
HC
>gnl|CDD|380259 NF033416, YM-216391_RiPP, YM-216391 family RiPP peptide. YM-216391 represents one of the rarer known classes of ribosomally translated, post-translationally modified peptide (RiPP) antibiotics
TAEIEEVDIEVGFIIGSSCCSLELEEDDLDVAADE
>gnl|CDD|468018 NF033417, glycocin_F_RiPP, glycocin F family RiPP peptide. Glycocin F, from Lactobacillus plantarum strain KW30, represents one of the rarer known classes of ribosomally translated, post-translationally modified peptide (RiPP) antibiotics. Members of the family are glycosylated, which is uncommon among RiPP natural products
MSKLLKTLSDEEINSYTEEGKGPFDVGCTYYALLCSTGYDSGTCSWIFEQCGRKGGGGGGNCGTCTCQ
>gnl|CDD|380261 NF033418, T6SS_TagK, type VI secretion system-associated protein TagK. Members of this family have full-length homology to SciF, a type VI secretion system (T6SS) protein from Salmonella typhimurium island SPI-6. Homologs occur in some but not all T6SS loci, and the broader family is now called TagK
MKSNITWGLQKIQAHGIKDNTIYATAGTQIIFTVAIPWLPVFEVNENVKIALSLTRHEEAWWIINQSDEY
CCTVNDQIVEPHHRMRLNEGDLIEWGLSSWCLVRNNPESPDTRPEKTTTQIAPSSETITEYLDLDWFRQQ
QLASQNPFDIIPVHGTDSSQEESEAENILHELYQEYRQALLSPEQDDHRWADPFPQNEEASTQDLISLRD
LSGETDTLQDMVTGGLSIDAILDVLDTTGEGETFWPAEKTIPDILHLLSPEYAQETAHSHILPDLTRKEH
RIIGIDSHYRITPFQHGDISHDKN
>gnl|CDD|468019 NF033419, T6SS_TagK_dom, TagK family protein C-terminal domain
EDDLLDSLHAEYRRALLDPEQSLAADWAAPLAEAEEPAAAPPSPDDPLADARTDSADSIEDLLSGGRLID
DVFGELDALDEPELFAPEPVPDILRLFAPEEYHAAAARRPPALTRREHHLLSIDSPL
>gnl|CDD|411112 NF033420, T6SS_PAAR_dom, type VI secretion system PAAR domain. The PAAR domain is widespread, but this model represents a narrow clade that may occur in type VI secretion systems (T6SS), either free-standing or fused to a long extension. Effector domains of T6SS may be separate proteins, or may be fused to on of the tube or spike proteins: VgrG (spike), Hcp (tube), or this PAAR family (spike tip). Members of this family that have long extensions are likely to be T6SS effectors
MGNAALLGDIGTDHDGFPPTPVIAGSPTVKIDGKPAARQGDPLAPHDKPKHPPHPRSIAGGSSTVFIDGK
PAARTGDAVSCGGVVIGSGTVNIG
>gnl|CDD|468020 NF033422, onco_T4SS_CagA, type IV secretion system oncogenic effector CagA. CagA, an effector injected into host cells by the type IV secretion system (T4SS) apparatus of Helicobacter pylori, is an oncogenic toxin. Tyrosine phosphorylation at multiple Glu-Pro-Ile-Tyr-Ala (EPIYA) motifs creates a scaffold that interacts with multiple host signaling systems and sometimes allows neoplasias to begin in gastric epithelial cells
MTNETINQQPQTQTAFNPQQFINNLQVAFLKVDNAVASFDPDQKPIVDKNDRDNRQAFEGISQLREEYAN
KAIKNPTKKNQYFSDFILSFVFDKKQSSDLKETLNQEPVPHVQPDIATTTTDIQGLPPEARDLLDERGNF
SKFTLGDMEMLDVEGVADIDPNYKFNQLLIHNNALSSVLMGSHNGIEPEKVSLLYGGNGGPEARHDWNAT
VGYKNQQGNNVATLINVHMKNGSGLVIAGGEKGINNPSFYLYKEDQLTGSQRALSQEEIQNKVDFMEFLA
QNNAKLDNLSEKEKEKFQTEIKDFQKDSKAYLDALGNDRIAFVSKKDPKHLALVTEFGNGDLSYTLKDYG
KKADKALDREKKTTLQGNLKHDGVMFVNYSNFKYTNASKSPNKGVGATNGVSHLEANFSKVAVFNLPNLN
NLAITSFVRRNLEDKLIAKGLSPQEANKLIKDFLSSNKELVGKALNFNKAVAEAKNTGNYDEVKKAQKDL
EKSLRKREHLEKEVAKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANREARAIAYAQNLKGIRRELS
DKLENINKNLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGINPEWISKVENLNAALNEFKNGKN
KDFSKVTQAKSDLENSIKDVIINQKITDKVDNLNQAVSVAKATGDFSGVEQALADLKNFSKEQLAQQAQK
NESFNVGKNSELYQSVKNGVNGTLVGNGLSKTEATTLSKNFSDIKKELNEKFGNFNNNNNGLKNSTEPIY
AQVNKKKTGQVASPEEPIYAQVAKKVNAKIDRLNQIASGLGGVGQAAFPLKRHDKVDDLSKVGRSASPEP
IYATIDDLGGPFPLKRHDKVDDLSKVGLSREQELTQKIDNLNQAVSEAKAGFFGNLEQTIDKLKDSTKKN
VVNLWVESAKKVPASLSAKLDNYATNSHTRINSNVKNGAINEKATGMLTQKNPEWLKLVNDKIVAHNVGS
VPLSEYDKIGFNQKNMKDYSDSFKFSTKLNNAVKDIKSGFTQFLTNAFSTGYYSLARENAEHGIKNVNTK
GGFQKS
>gnl|CDD|468021 NF033424, chlamy_CPAF, protease-like activity factor CPAF. CPAF (chlamydial protease/proteasome-like activity factor) is a serine protease secreted various species of the intracellular pathogen Chlamydia. Early attribution of contributions of CPAF to virulence by cleavage of specific host cell substrates contains a number of errors, and the true role of CPAF, and its contributions to virulence, remain under study
LKKLLALLFSLLISSSSSGSSKSLVKENALADLDFIKHLFEVKYAPAEWKKKLFGWDLDEETEKAKAKIL
SEEKPSTKDYQRILRDFFNSLKDYHVGVTFYSTEMAYLPFDVKGAEGRYFIVWIDKVKVPTSSLDIQVGD
EILEFDGMPIEEVIEELRLAEFGRGSTETDQALAERTLTSRSAALGHQVPQGPVTLKVRRPSGLIRTYKL
EWRYTPEKIIDLSLILPLIKSPKSPLTSKKSILRLFKKEMVPPFWKELRDLYKRSGESPYNLGSKKSFLP
PLGPIVWEADSGPFHAYIFETPDGKKIGYLRIPTYVGGEAEWEEFGEIIDIFEAKTDALVIDQTNNPGGS
VFYLYGLLSMLTDKPLETPKHRMKLTQDEVMSALEILDLLEGVQTDEEAKEALGETMEGYPIDYQAVGYL
KSFSKFILDEWNSGKILTDPIHLLGFDTINPHPKHRYTKPILVLINELDFSCADFFPAILQDNGRAKLFG
TRTAGAGGFVLQVSFPNRFGIAGFSYTGSIAERKDGKPIENLGVTPDIPYELTVEDLQNGYSGYIEAVLE
AVLAL
>gnl|CDD|380267 NF033425, PSM_alpha_1_2, alpha-1/alpha-2 family phenol-soluble modulin. Members of this family are extremely short proteins, about 21 amino acids long, that are known to retain an N-formyl-methionine (fMet) at the N-terminus. These proteins, phenol-soluble modulins of the alpha class, including alpha-1 and alpha-2 from Staphylococcus aureus, are exported by an ABC transporter, and affect the state of the host immune system in a number of ways
MDIIAGIVKVIKGLIEKFTGK
>gnl|CDD|380268 NF033426, PSM_alpha_3, alpha-3 family phenol-soluble modulin
MEFVAKLFKFFKDLLGKFLGNN
>gnl|CDD|380269 NF033427, PSM_alpha_Shaem, alpha family phenol-soluble modulin. This family is based on an alpha family Staphylococcus haemolyticus phenol-soluble modulin, somewhat similar to delta-lysin
MGIISGIIELVKFIIDLTKK
>gnl|CDD|380270 NF033428, PSM_epsilo, epsilon family phenol-soluble modulin. Members of this family epsilon-family phenol-soluble modulins. Species with members include Staphylococcus epidermidis, Staphylococcus capitis, Staphylococcus lugdunensis, Staphylococcus pseudintermedius, and Staphylococcus schleiferi
MFIINLIKKVIEFIKGLFGNK
>gnl|CDD|468022 NF033429, ImuA_translesion, translesion DNA synthesis-associated protein ImuA. A three-gene cassette encoding ImuA, ImuB, and ImuC ("inducible mutagenesis") is induced by DNA damage, is capable of DNA synthesis across DNA damage lesions, and consequently is associated with mutagenesis. This family, ImuA (previously misnamed SulA in Pseudomonas putida) shows some homology to SulA itself and to RecA. ImuB resembles Y-family polymerases but may be catalytically inactive. ImuC is a C-family polymerase, and catalytically active
SLWRGSQLARAAARVVPTGFAALDAELPGGGWPLGALTELLSPQPGIGELRLLLPALARLTQRGRRIVLV
APPHLPYAPALAAAGIDLEQLLVVRADSPADALWAAEQCLRSGACGAVLLWLPQARPAALRRLQLAAEAG
DTLLFLFRPLAAARQSSPAPLRLALSPAPGGLQVRILKRRG
>gnl|CDD|380272 NF033430, TfxA_RiPP, trifolitoxin family RiPP peptide. Trifolitoxin is ribosomally synthesized and post-translationally modified peptide natural product (RiPP) antibiotic produced by some strains of Rhizobium and active against others. At the time of building this model, only two variants sequences from this family are detected, both 42 amino acid-long TfxA peptides that differ at only two positions
MDNKVAKNVEVKKGSIKATFKAAVLKSKTKVDIGGARQGCVA
>gnl|CDD|380273 NF033431, cinnamycin_RiPP, cinnamycin family lantibiotic. Members of this family are RiPP precursor peptides from which the lantibiotic cinnamycin is the most heavily studied. Mature cinnamycin is 19 amino acids long with nine post-translational modifications, including lanthionine, methyllanthionine, and lysinoalanine bridge modifications
LETLLQQAAVDAEFRAELLADPEAFGISADTLPAAVEQQDQESLELWTEGIAAVDIYACRSTCSFGPFTI
VCDGTTK
>gnl|CDD|468023 NF033432, ThioGly_TfuA_rel, TfuA-related McrA-glycine thioamidation protein
KIVVFTGPSLSHEEAKKILDAEYRPPVKRGDILKALKEGPDIIGIIDGVFFQDPAVAHREILEALKKGVT
VVGGSSMGALRASELDTLGMIGVGKIYEWYRDGVIESDDEVAVVFDPETFEPLSEPLVNIRYTLKAAVEE
GIITEEEKEELLKIAKSLYYPERTYERILKEAVKKILSEEKKEKLLEFLRENEVDIKREDAIEVLEYIKE
I
>gnl|CDD|468024 NF033433, NisI_immun_dup, NisI/SpaI lantibiotic immunity lipoprotein domain. This HMM describes a domain that occurs twice in the nisin lantibiotic self-immunity lipoprotein NisI, and once in the subtilin lantibiotic self-immunity lipoprotein SpaI, and once or twice in numerous other known or putative lantibiotic resistance lipoproteins
EFELNKENARQFSYKGKDYTITDDEVSEDSLGEWIGKIAELVVVDEEGKVLLSKELNKIDWLGENLNEKR
ETLNYGNVYSIKGTDSDEEVAVEINDEYYKAVLE
>gnl|CDD|380276 NF033434, AzmA_fam_RiPP, azolemycin family RiPP peptide. The azolemycin precursor peptide, AzmA, contains a mature (core) peptide region derived from the sequence VVSTCTI. Examining genomic context from that RiPP precursor peptides related to AzmA are much more similar in the leader peptide region than in the core region, and that the proper length for the percursor peptide is probably about 36 amino acids
MPENDDLFEEMAIPEPEAAFAGHSCLSAVEDIEETE
>gnl|CDD|468025 NF033435, S-layer_Clost, S-layer protein SlpA. In Clostridiodes difficile, the S-layer protein precursor, SlpA, is one member of a large paralogous family of protein that share several cell wall-binding repeats. SlpA is cleaved into a larger and smaller protein. The S-layer protein itself is important to adhesion, and portions of it are highly variable, and then N-terminal and C-terminal are well-conserved
NKKNIAIAMSGLTVLASAAPVFAATTTNDKGYTVVQKKYKKAVKELQKGIKDGTITEVDVYFDGSSIKTV
DVGSTETDAREEAADKLYNLVDDKLDNLGDGDYVDFNVTYNTAAKIYTKAELDALKTKLGKDNKIVIKKA
TEATKGIVKQDSDNATKAVAADTPLTLSDVFTITVVTDTNGGYTLTITPKTTAATYKYGTDGDGAGTTTY
TTAIAFTADTTTTVLLGGGKKLDLSKSLKFDSTTKTISGLSVKATTPTADAQTANVRVINAKEETIDIDA
SSYDSAEDLAKKYVFDDDELETIYKELNALNKDLDGSLVEKVDGKYQVVLYPEGKRLSTKSATSTSGLAD
EDSPAKIVLKADKLKDLKDYVDDLKTYNNSYSNVVTVAGDDRIETAIELSKKYYNSDDDNALTEDAVNNV
VLVGSQAIVDGLVASPLAAEKHAPLLLTSKDKLDSSVKSEIKRVMNLKSTTGINTSKKVYLAGGVNSISK
DVENELKDMGLKVTRLSGDDRYETSLEIADEIGLDNDKAFVVGGTGLADAMSIAPVASQLKDGDATPIVV
VDGKAKDLSSDAEDFLDDAQVDIIGGENSVSKDVEDAIDDATGKSPERISGDDRQATNAEVIKESDYFEK
GGVKNYFVAKDGSTKEDQLVDALAAAAVAGNFGATYDNDGSTGTVSPAPIVLATDSLSSDQNVAISKVVN
DDGGKNLVQVGKGIADSVINKLKDLLDM
>gnl|CDD|380278 NF033436, SpoVM_broad, stage V sporulation protein SpoVM. Members of this family are SpoVM (stage V sporulation protein M)
MKFYTIKLPKFLSGIVRAILGIKKKE
>gnl|CDD|380279 NF033437, YpdK, membrane protein YpdK
MKYFLMGISFMLLLWVGTFMLMV
>gnl|CDD|468026 NF033438, BREX_BrxD, BREX system ATP-binding protein BrxD. BrxD is an ATP-binding protein found in types 2 and 6 of BREX (bacteriophage exclusion) phage resistance systems
SPRRRREIIDALRRGTVPQRGLDAFAVGLDRFEAALDEELDRVAGGGGVFKAVRGEYGSGKTFFSRWLGE
RAQARGFATAEVQISETETPLHRLETVYRRLVERLATASCPPGALRDILDSWLFTLEEDVLAAGEGDEED
APGFDAAVDELLEQRLASVARTAPAFAAALRAYRRAVAEGDTATADALLAWLGGQPNVAAAAKRAAGIKG
DLDHFGALGFLRGLLAILRDAGHKGLLLVLDEVETLQRMRSDSRDKSLNALRQLIDEIDAGRFPGLYLVI
TGTPAFFDGPQGVQRLAPLAQRLHVDFLTDPRFDNPRAVQLRLPGFDLARLVEVGRRVRDLYAEGAEDPE
RVAARVDDGYIARLARAVTGELGGKVGVAPRIFLRKLVDVLDRVDQFPEFDPRQHYALTVDDAELTDTER
AAL
>gnl|CDD|380281 NF033439, small_mem_YoeI, membrane protein YoeI. YoeI, a hydrophobic protein of only 20 amino acids, is found in at least these genera: Escherichia, Salmonella, Citrobacter, Enterobacter, and Klebsiella. It is known to be expressed in E. coli
MGQFFAYALAFTVKGNNHVA
>gnl|CDD|380282 NF033440, small_YrbN, protein YrbN. YrbN, a small protein of only 26 amino acids, is found in at least these genera: Escherichia, Salmonella, Enterobacter, Klebsiella, and Yersinia. It is known to be expressed in E. coli
MKITENFHDELCRLAAINFEAHVLHG
>gnl|CDD|468027 NF033441, BREX_BrxC, BREX system P-loop protein BrxC. BrxC is a P-loop-containing protein, and probable ATPase, from BREX (bacteriophage exclusion) systems of type 1
KIKDLFAKPIDRPINGVIKVDQDDEEVLRQELEEYVVTGELEKHLEKFLDAYLNALDGPTDKPGVWISGF
FGSGKSHFLKMLSYLLENREVDGKTARDFFLDKIDDPMLLADLKKAAKRPTDVILFNIDSKADAKSDKDA
ILLVFLKVFNESLGYSGDQPHVAQFERWLDEEGKYEEFKAAFEEIGGKDWEEERDNFLFEEDEILLALAP
ALGMSEEAAESWLDQYREDYDISIEDFAKAVKEYLDRKGPDHRLLFLVDEVGQYIGDDSQLMLNLQTIVE
SLGTKCKGKAWVIVTSQEDLDEVGDMTKVKGNDFSKIQGRFPTRVSLSSADVDEVIRKRLLEKKEEAKAE
LEALYDQNGGILKNLLSFTDGSGTLKGYRDEEDFVDDYPFLPYQFDLLQKVFEALRKHGASGKHLSSGER
SMLSVFQEAAKKLADQELGTLVPFDFFYDAIESFLDSSIQRVIIEAEKNADGNGDDELAVRVLKTLFLIK
YVDEIKATLDNIATLLVDDIDADKLALRKKVEEALERLERQTLIQRNGDEYRFLTDEEQDIEREIKNQEV
DPSEIARELSELIFDDILKDKKYRYENKGDFKFNRKLDDRPLPGGRNNELTVWVLTPWSDDYNSVEDEAR
AASSSSDELLVVLPKDSRLREELREYLKIEKYLRQKPSTSLGEEAKRILEAKRDEAEEREKRLKELLEEA
LLEARVYVNGGELEIKGGDLKERINEALEYLVERVYPKLKYADAPAESEADISKVLTAKGDPDGLALGDG
GETVNHPALKEVLDYIQLQARRGGGVTGKDLRDRFEKAPYGWSEDAIDGLVAALLRAGKIKLRYNGNPLD
PKDLEAIDALTKRNKFGKASFEPRVTISAEQLRKARELLKELFDGTAVPDDEDALAKEIREKFPELLEEL
KALAGRYQAGGYPGPDPLEPALALLEEILSIKDNEEFLKALNKKEDDLLDLIEDWEDVKSFFEGDQLPIW
DRALRLLKEYEDNLDYELDEEAEEAIEELRSILADPDPYSRIPDLPPLLEALREALREALEELREAALEA
IEEAKAELEADLEWQELSDEQQNRLLAPFDELKERIEPEVSIASLRALLDQLADALLDRLLDRIEALIQR
FQEEKAEPEVKEAAAEPPEPKVKTVSLPRLFPGTLETEADVDAYLAELREELL
>gnl|CDD|468028 NF033442, BREX_PglW, BREX system serine/threonine kinase PglW. Members of this family are PglW, a predicted serine/threonine kinase of the Pgl (phage growth limitation) system (now called BREX type 2) and the BREX type 3 system
GRWKTITPSEFPHEREALDFVRELLPDAEPYRAWSNFEFTANDGSINEVDLLVLTPAGLFLVEIKSWPGR
LSGDGGTWTWTRPGGRRRTEDNPLLLTNRKAKELASLLEWQARKVGRKERIPFVQPAVFLSAPGLRCELP
GPARAGVYGRDGREDQTGLPGIWDRLLEPPSDHRRVDEEFSRAIARALEEAGIRPSRRQRRVGDYTLERK
PLDEGPGWQDWLAKHTVLTGEERRVRIYLVRRGASEEARASVERAARREYQLLEGIRHPGIVRALDFQDH
ELGPALVFEHDPDAQRLDHYLAEHGDRLDLDQRLDLVRQLAEAVRYAHRRRLYHRALSPRSVLVRDRGSG
APRLQIADWQTAGRIFGSSSTSSTTLGPSHLAAHVEDAARVYLAPEARAPDADPVALDVFSLGALAYLLF
TGQPPAASRLELLERLREGGGLRLSAVVDGVSEELDELVQDATRPDPGERLASVDDFLERLDEVEEELTA
PDPEVVTDPLEARPGDELAGGFEVRRRLGTGSTSRALLVRDRDADGEERVLKVALDDEHAARLRAEAEVL
GRLRHPRIVALVEGPLEIGGRTALLLEYAGEQTLAERLRKEGRLSLDLLERFGDDLLSAVVHLEGQGVWH
RDIKPDNIGIRPRPSRTLHLVLFDFSLAGAPADNIEAGTPGYLDPFLGTGTRPRYDDAAERYAAAVTLYE
MATGTLPVWGDGQVDPATLDDEVTLDAEAFDPAVRDGLVAFFRRALARDARDRFDTAEDMRRAWRAVFTA
ADTPPPPTTPAEEARDAPAEEATADTPLGAAGLSPRALSALERLGITTVGELLALPRRRLRRLRGVGAKT
RREIRDRIREWRARLGKPEAAPLTPAGRPEAAAEGALSLDALAALLLPAAGRRGRTRRRAVRLLLGLPED
AGGLLDPWPTQAEVARALGLTQGRVSQLLKEARTRWSKNPALTALRDELVELLAASGGVMTAEELADALL
ARRGSLEDEPPQRRRLALAVVRAAVETELARGEPRFVLRRHGGRVLVDDPTVATAPALADYAEALGRRAD
ELAAADPLPSPARVLQELRAVPAPEGMAPLPDTRLLRLAAAASRGAALSSRLELYPRDLSAERALRLAQG
ALLGSPGLTVAEVRDRVRARFPELEPLPGRPELDALLREAGPGLTWDPARGRYRPPDAEATSTTSSTTTP
RRYTATGSGPGATPDLADAAQAEERLARSLREGGFLALTVRPRRLERAAEELARRFGLERVDVTALFLDA
LRELADEAGVPWELVLAADAAEPGSRDWQGLQRLVRRAWPRLEARLAAADGPVLLTDAGLLARYDQMDLL
GRLADQARRRPGPHGLWLLCPQDRPQRGPRLDGVAVPLIAGPGEFVRLPDSWLDNLH
>gnl|CDD|468029 NF033443, BREX_PglZ_6, BREX-6 system phosphatase PglZ
VSLALEQELRGEVRRHGLVVWLDAHGHYTPLVDGLSALAKQGELPYPVVAFRGSFLEIVLELEPYGSGVD
NARLLIHLPGFNEDSIRATPLLELYKAGFRYRKDLKTLVREAAAGRVAPDALEQYLARGTLSLAAADAWL
ASQLSHGREGLAALLENLSLDALVDDLLRRESLAQRVGSDGDREALEAWLARQTGMDAAWLRFFDVSLQN
SFSYGADPKAVPLESVAGALVSWALSVEYVHDLNRPPFSPLLVRVRDLPAPVRKACLELVDHLRGKHTDF
YRSLADETELRLHDEVPAIRAEDLGRIDTFRFEEQRILQAAVDALRAREWDKARGWAEARNEERSYWLRR
DAARRRAWQLVAEAAALGSAITAAGRPLEAVDSLDAAVERYAATGAKVDRAHRRLEQRRAKLLDSQLPHF
GDVREILDVLRSAWRGWADRWARDFAAACRAAGFLPDATLQQRALFDQVVQPLATDGRTALFLVDALRYE
MATELLAELGKTAGTVVDLDARLAELPTVTEVGMNALAPVSQGGRLQPEIVNGTFGGFSTGEFTVRDPDT
RRRAIGLRTGGKTCPLLQLGEVLELEAEKLKRKIASARLVVVHSTEIDDAGEAGLGPATFEIFLRQLRTA
WALLRKAGVKSFVFTADHGFLLLDETTQKAQPYGRKIDPARRYVIDEHAAAHSGEVRVSLSALGYDGLAL
HLMFPEDTAVFDTGNAGATFVHGGNSPQERVIPVLTVRHRRPLGGTLMAYRVDAERLPDAMGLHRLRVRV
RVAHDAGQLDFVAAPEVSLALRAPGHPDVRAELKGVSGGARVEDGTLRAAVGEDFELFFRLEGPTSERVR
VELYHPDRVAKVEPKPLDGRFDVVRDWRRASVEPTAPQPERVLDWLAALPAGGVRAVFEHLAVHGAITET
EVTRMLGSPRAFRRFSLDFEEHAAKAPFRIRIDPVSGGKRYVKEGERL
>gnl|CDD|380286 NF033444, BREX_PglZ_5, BREX-5 system phosphatase PglZ
TTLPDQAKDTIEDEFDDAYATDPRVLWWDDGGYLRDIVRAAADRLGVGFSEAEQTPLELRADAIDEPHVW
YVPQASKEDRDWFRDVRHTGGEVELTIEQLTAELFEVNPLQAWDIYDAERGATESDRETAANVLKTQLAG
GGLPRLGDLITEIVTKGEGDPVEFVLEGGWPEIDDDDETIARVQDLLKDRGVAAVDNESTPETIEDVTRR
WAVAEWLVAEGKDVDAFPEGYGNEGSTLGDIPELKSILDSTRQSKRLAERYLSESYWGDVIESSDDPWEL
AACPVDAALEARLWDEWLESFEEGRYEECIERANERQEALDGVYGDDIPWTQLWEQAEQVAELALRLATW
EERSQSFDVVDLYADQEDGTWQIDNAVLNLEISGEPEQELPNSHPATETLDELRAELLESRYMNYLEDLG
DLVVSSIEAGSPFVGEDHAYQFFTDEEQDLASGQTVALFLIDALRLDLARELADRLRRELPDYSVAESTW
VGTLPSETEFGKAALTPGRAHRFRIKLRDGKLSPERGGRRLDNKRRVKLLERDGWDVPDERDSGWQHTRV
AYYDNDIDDIGEKELDDPEEHFTSRIDELYDLITEKLENGEWDRAYVLTDHGFVLLPKGVTMESISSPDG
DGEVKRRWVAGDDIDDDGPGVLLDGQTPLGYLDASVSLLAKPRQRFSKQGLTDARFYHGGILPQEFVLNF
LRIT
>gnl|CDD|468030 NF033445, BREX_PglZ_4, BREX-4 system phosphatase PglZ
RYPVRFILFENFEDFKFVIKLLELGGIEVEVVDLSDFCQGDDKFPTIDELLNKIKTLIESKPGNDFVIVP
FSELLRFYDNEFDSLLKTIKLIEASLSAENNHRRIYIPLLGLESKFSKKFKNDFRRIDESRPVWVLDSPD
DKVKIYFLIPTLGNSTNNYTVVNGIKEWLKLWENGVKENIICTSKVILANAKNAQPDNAFTFTVCSNYYE
FLTKGLGIDFGIPYSEGEDEYWRELLKEIDKSNFFESFIKKKFNVFDLLDDDLIEFVKSLFDNSDDFERW
LLKNYLKLINKGEGSYLCRVLKNSNSYSDFEELIENAILEIFDEDNNTLSLYRERERKSLLKKLGEKLSE
IAEFKLKEKLNKIADPYKEAIYYLTDLTSAEKELIIKWVGQGDIIIEDLKEVYPELYYYLSPYSFNSDEL
PDWLNDYFEEYKKSKLSNKITDELLELIEEKNANESSFYSWYTRFKTVKKLLEKRKDDVLYWIDGLGVEW
LPLIKNLLEKEYGLLNEIEIARANLPTITEINKEFLDELPVGGLEKIGDLDDIAHKGKGYYPYENLIKEL
EIIEKIIKKILSLEYNGKKIAIVSDHGASRLAVIQFKEGKKLKGETSDHGGRSARCCKGSEEPDNPYIVL
EDDNGYICLLTHNRFSGKRPAGVEVHGGATPEEVLVPIIIISKLKKKSKNYSVKLITLEISGGNPILVFK
IKPKPSDDVPVVVYNGKYYALKKIDGNHYESELL
>gnl|CDD|468031 NF033446, BREX_PglZ_2, BREX-2 system phosphatase PglZ
AQVDAVLRHQPGARRRAVLLRAAPQWPGEPTLTVRGRPVRVAPCPSPLAVREALQDLADRDPADPWLVLL
TDLGDHELGADVLARLAGGRVRSVDPWRAVRQRFGATAIDPRLRAERWLAEALLDLAPPGGWPPAPGGVL
TRDHALSALAARRLGLTRTADRLDAASLLRWSASPAATARLGDLPAAERDGLLGWLGDAAGPAARAVLRL
VEAGRGGDAVALGLVAGVLWGRAAADPEAARARGRLEERFGGGRLPATEALRAWGRAAEAVVRRLLDDPA
ARETLDRVLRRAEELLAQLGATEAAARSPLLPSGFEARLRALADALALAALAPGDTGAAEDALRRLRAHR
LARVQRERVRRAEMAVRLVRWLASAPTPPTTLADALHRQLDEGAWVDRALARLWGGDDAPALAQAYRALL
TAVRARRDRHDRRFARSLAAWTQAGSGEPGRLLLVEQVLDRVVAPLARQGPVLLLVLDGMSAAVAVELLE
DLARDGWAEVVPEGLGRRRAALAALPTVTEVSRTSLLCGTLTTGGQADEKAGFAGHALWRAHSLGRPPPR
LFHKGDLRAGTAGEALSDDVRAAIADPDHKVVAVVLNAVDDALDKSDPGRTEWSLDDITGLRALLRAART
AGRAVVLTSDHGHVVDRGGTAVDASGGESARWRPATGADAEGEVVLSGPRVLLGGGSIVLPWDEDLRYGS
RKAGYHGGASLAEVVVPVLVFLPSARLLPPGWRPLPDQRPAWWSLPTRTVAAATAPASTKTPAARPAAPA
RAGSQPLFDVEPAAVAPAPTEDLVARLLDSEVYAAQRALLARGAPPDEQVAAVLDALAAGGGRLTQSALA
ARLGVPAARAGGFLSALRRLLNVDGYPVLSVDPDGRTVRLDLELLREQFG
>gnl|CDD|468032 NF033447, BrxE_fam, BrxE family protein. This family is uncharacterized, but a subgroup within this family is BrxE, a protein of unknown function found in type 6 BREX phage resistance systems
LDDLLKLRLLVARLGEKDQAGWWPSSFLSEGGRAFLERLFPRTHFLAQYRGVREAARRVHDEHIGVGGVY
HLFRLPEELEEELHERLADWKDSAEDWEELLPELLGDKESALAALRDLAGSSGDASEGPVRIGRISDGDI
DDSLREVAALYAAAFLRGNLVFPYFR
>gnl|CDD|468033 NF033448, BREX_6_BrxE, BREX-6 system BrxE protein. Members of this family are BrxE, a protein of unknown function that is found in type 6 BREX systems of phage defense
SKSDLDKILTAQLVVAWAGEGGEPKRLGWWRTDLIDETGGGDLFRRLLPRTWQWAALEAAREAARRTDAK
LRSRMADPDAVLTLFHLGFELDERLEDRLAHLKRSGRPPAEALPILNVLIAPHWDRDAFEEWLSSEGNVE
FTVVPAGRELKGKPPDSLDELVRRLAAALLPLAGSYPLPFYR
>gnl|CDD|468034 NF033449, BREX_PglZ_3, BREX-3 system phosphatase PglZ. BREX is a phage defense system (BacteRiophage EXclusion), with a number of described subtypes. The first described, PGL (phage growth limitation), is not called BREX-2. This model describes one of the two core proteins universal across the first six defined BREX subtypes, the phosphatase-like PglZ domain protein, as found in BREX-3 systems
RDAILDKFKPSVSRLILVADPDGLLLEEGLLEELRERGFELIPFKDPIAFRYAYESKYRSRWDRGEETDL
VVVLRSGSELNDLPYDLLQAGRKLSFSLGDLFPKLSYPVLKALDSELLDKLYEAYQKYDGRQLGENETKD
FILKHVFGIAPELINNPVDLLKTLLRLHYKGQELPQILSEHLIQKLRGKSLFKDWPLEEIIPDRDAFFAF
LQERWPVFLNDLAEGNHVEEEIPFDHPDIRVYIDNLFLEGYLQPVAVSNIDILPETWVRSGILEDELEDR
LRRLKGLLEKLEKLLPTAKSRYRDWGDFAKIWAELLALVYELNQVEDEERFESLSKLIDERFAEWLLKHY
ASLINLPYTNGPVMVHHIPRYLARLLKKEGNSKVALLVVDGLALDQWVIIREYLNENDPSLRFEEKAVFA
WIPTLTSVSRQAIFSGEPPLYFKDSIFTTNKEEKLWKQFWMNEGISRDEVAYQRGLGDFDECELDDIINN
PKLKVVGLVVDKVDKIMHGMQLGSAGMHNQIRLWLEQGFLAKLLDKLLKNGFEVYLTSDHGNIESVGKGR
PSEGVIAETRGERVRIYESEGLRAEVALEFPKAIKWPGIGLPDDYNVLIAGGRNAFVPKGETIVTHGGIS
IEEVIVPFVRIS
>gnl|CDD|468035 NF033450, BREX_PglZ_1_B, BREX-1 system phosphatase PglZ type B. BREX (bacteriophage exclusion) is a phage resistance resistance, in which two protein families are core but other proteins are variable. BREX subtypes are based on PglZ domain protein, a putative phosphatase. This family is one of two major subtypes of PglZ as seen in type 1 BREX systems. Most members of this family contain an additional C-terminal domain that is not included in the seed alignment. Family TIGR02687 describes the alternative type A for PglZ of BREX-1
TLLDALVEALRAAARYNPGVQVAPAAILWTDPERQWEPVIPRLRERLPELLVLGDYDPEERTGPAIWLRC
VVAGTLPEVALPDGRVPIIYLPGVSRQDLRAIEDCPEELKPLAELQYRGTWWSQRNGKDWTVLAFLTSPQ
GGLGLDVAQDAATREALLRALPRLLDEPVEDLRGRRLDADDFNALLTPDPVRDLLRWLNDPDAFRARWDG
ARWAAFRSVCKSEFGFDPEKDGVLTAAEKLAAREGAWAAVWERFAEAPKRYPGIPELLRRAKPPDLGAAD
PERWPQVNEQEEDALRKALLALADLPPAEARARILALEKEHGERREWVWAELGEAPLARALEHLARLAEL
TRTPLGGGTPEALAEAYAEEGWQADDAALRALAAARTAADQEAVSAALRALYLPWLEESARAFQKLVEAA
GYGIAEAKPAYAEPGTCVLFVDGLRFDLAKRLAERLEAAGLEVSLTWRWAALPSVTATAKPAVSPVADKL
TGGEDGEDFEPSLADTGKPLSSYRLRKLLAEAGWQVLEGSETGDPTGRAWTETGDIDHLGHDLGWKLARR
IDEELDEIAERIQELLDAGWKRVRIVTDHGWLLLPGGLPKVELPKSLTETRWGRCAVLKDGAQTDLPTVP
WYWNPSVRIALAPGISCFRAGEEYAHGGLSLQECLTPVLTVT
>gnl|CDD|468036 NF033451, BREX_2_MTaseX, BREX-2 system adenine-specific DNA-methyltransferase PglX. This protein, PglX, is a site-specific DNA methyltransferase associated with PGL (phage growth limitation), a type 2 BREX (bacteriophage exclusion) system. The phage resistance appears not be restriction, but does manage to inhibit phage replication
ALLKDLKRQVTLLEDDLRARVEAVAEVGARLRAEYDAAREAGRTAATWESWLDERVTQAAVAWVLGTVFV
RFCEDNGLVEEPWIAGPPGERLALAEDRHEAYFREHPDLTDRDWLEAAFEELAALPATAGLFDRRHNPLW
QIPPSGDAARALLEFWRRRDPDGGVLVHDFTDPEWDTRFLGDLYQDLSEHARKTYALLQTPEFVEEFILD
RTLEPAIREFGLEGLRLIDPTCGSGHFLLGAFRRLVARWREAAPGRDRRERVQRALDSVHGVDINPFAVA
IARFRLLVAALKAAGARRLDDAPDFPINLAVGDSLLHGRGAGGGQQFDLADEADDVLAAFAYATEDVDRL
QDILGRGQYHVVVGNPPYITVKDKALNALYRELYDACHGKYALSVPFAERFFELAKRGDGDDGGAGFVGQ
ITANSFMKREFGKKLIEEFFARRVELTHVIDTSGAYIPGHGTPTVILVGRNRRPSRSDTVRAVLGVRGEP
SQPENPAKGLVWSAIVDQIDRPGSESEWVSVADLPRDSFSRHPWSLSGGGAVELLQLIESAAVRLLGSIV
ESIGFTAFTGEDDAFMLPEGTLRRRGIPPAVRRPLVLGDDVRDWTISPGVDAVFPYDSDLRPLSPELSSP
VARFLWPYRTILRSRVDFGRTQEERGLPWYEYSMFFPERYRTPLSIAFAFVATHNHFVLDRGGKVFNQTA
PVIKLPEGATEDDHLRLLGVLNSSTACFWLKQVSHDKGGGGGGGGGGGSDEAWERRYEFTGTKLQEFPLP
ESLPLELARELDSLAQQLAATEPAAVAAAGVPTREALAEARAEYESIRARMIALQEELDWQVYRLYGLLD
EDLTARLDPDGAEVPEIALGERAFEIVLARRVAAGEVETEWFERHGSTPITEIPAHWPDEYRELVQRRID
VIESNRDIGLIERPEYKRRWATEPWEKKEQAALRDWLLDRLEDRDLWFDEQGQPRPLSVAQLADALRRDA
DFVAVAELYAGRPDADLAQVLAKLVADEHVPFLAALRYKESGLRKRAQWERVWALQRREDAGEDVAADIP
VPPKYTSADFLKTSYWRARGKLDVPKERFISYPGAGRDTDPTLLLGWAGWDHAQQAQALATLYADRKDQE
GWPAERLTPLLAGLAELLPWLRQWHNEYDPEFGGSPADYFTAFLAEKQGEHGLTDDDLTAWRPAATTR
>gnl|CDD|468037 NF033452, BREX_1_MTaseX, BREX-1 system adenine-specific DNA-methyltransferase PglX. This protein, PglX, is a site-specific DNA methyltransferase associated BREX (bacteriophage exclusion) type 1 systems. The phage resistance appears not to be through restriction-modification, as phage DNA appears not to get degraded, but it does manage to inhibit phage replication
LKKFAPQARRELIEEVTQQLQTLGITEDKIGDVEALEALVLGDLSLARREEPEQRKKLVKRIKEKGFDQV
IEEVAYTWFNRLIALRFMEVNGYLPHGVRVLSSGTGKPEPDILAKAGEIALDLLLDKKREVELLLSGNKD
EELYRLLLLAQCNALHRAMPFLFERIDDYTELLLPDNLLSTDSVLRKLVDDIPEEDWQEVVEIIGWLYQF
YISEKKDQVFAKLKKNKITSEDIPAATQLFTPDWIVRYLVENSLGRLWLENHPDSKLKEKMEYYIEPAEQ
EPEVETQLLKITPESLSPEDIKVLDPACGSGHILVYAFDLLYAIYEEEGYSERDIPRLILENNLYGLDID
DRAAQLAAFALMMKAREYDRRFFRKEVRPNICVLNVVLNILSIQESNGLDLEKLEELDEGAADLGKDLLT
LLLRTLLEQFEDAKEFGSLIQVPEEDPEELLEVLEALEESELGDDLLLKEAAERLLPLLKQAEILSQKYD
VVVANPPYMGSKGMNDELKKYAKKNYPDSKSDLFAAFIERCLELLKENGYVGMITMQSWMFLSSYEKLRK
KLLDNKTIVSLAHLGYRAFEEIIGGEVVQTTAFVLRNLKNTSFKGYYVRLRLGEGEANSEEEKELLFLNK
NNNRFYEVSQDDFEKIPGSPIAYWASEKLIELFENGPPLGDVAEAKQGLATGDNDRFLRLWWEVSSNKIG
FNAKSREDAKASGKKWFPYNKGGEFRKWYGNNEYVVNWENDGKEIKEFSDSNGGKRRSRIRNEDYYFKEG
ITWSKISSGGFSFRYSPEGFIFDVKGSSIFPDDESDLYLLGLLNSKVASYLLLFLNPTLNFQVGDIKKLP
IIKSESKKEIEELVEELIEISKEDWDSFETSWDFKTLPLLSGKHRAATLEDAYANWREHWESRFNELKRL
EEELNRIFIDAYGLQDELTPEVPDEEITLRCNPAKADLVRDIKELISYAVGCMFGRYSLDKEGLIYANGG
NDLSDYLARVPEPTFPPDEDNIIPITDGEWFEDDIVSRFREFLRVVFGEETLEENLDFIAESLGKKANEA
RETIRRYFLKDFYKDHLKTYKKRPIYWLFSSGKKGAFKALVYLHRYNPDTLARVRTDYLHPLQAKLEAEI
ERLEEQLIDDSSSAAEKTRAKKELEKLRKQLNELREYDEKLLHPADQRIEIDLDDGVKVNYAKFGDL
>gnl|CDD|468038 NF033453, BREX_3_BrxF, BREX-3 system P-loop-containing protein BrxF. This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins
LEKLKRSVDEAESLYYKLILLVGPPGSGKTALLRELAAKRGAPVINVNLELSRRLLELPEKQRALRAPRL
LDEIAEKSSGDVVLLDNIEILFDKHLKLDPLRLLKRISRNRTVVAAWNGSITGGRLTYAEPGHPEYRRYD
LDDLLIVEI
>gnl|CDD|468039 NF033454, BREX_5_MTaseX, BREX-5 system adenine-specific DNA-methyltransferase PglX
GDSLSQRKAQLDKEEREHLEDVVAEMRERVEDNVRFQLTQKGLDDEPEDRDSLDEETEQLVEAIELEAVD
GETWSEAFEQYVTGVGYTIVNRLAALRCMEVRDFIDEEVTVFKDNGLTPAAETLVHEEFLLEDEAILEAY
HNACDDLAEEIEILFDRSSAYSLIDPDDDTFEDLCGMLDSVPDEVWRADDVLGWVYEYYNRPVVEALDAK
NGLEPEDVGPANQFYTPHWVVRMLTDNSLGKLYLEATGQLQAVPEPEALSPEERKDRLVTPDDSPSVAEL
CTYLIPDEEEGEAPEFDHPRELRVIDPACGSGHFLLYAFDVLERIWWAETDLDRAEIPAKILEHNLYGVD
IDLRACQLSAFNLYLKARTRAEAEGAGGFEMPNVGIVCADARVAEVEEATAVLDEITGEGSDVREALDDI
IDTFQHTEALGSLLDVSGTLEELFDDDKTQTELTDYDPGAHQTLNSFLKALRRAVEEHTSDSFGEQNLRS
FLRLLVVLTQEYDVALMNPPYGSGGRMPDDVQDYVEEHYEYYPEYYINFFEVCDRLTKDDGRIGMLVPRS
FMFKKSFEDFREDFVGGRGAFDFLAEFGYGILDNATVRTVGTVVRSGAQSNATGTFIRLHDVEKGEKEGA
FLNTSFSSEDDDVQRLFERPLSEFSKIPGTPISYWVPPDIRELYDSETVLDADNAGLDDRESVGDVKQGL
ATGNNDRFVRKFWESSSDDWVPFAKGGKDAWLLPRIKETVLWGNDGKEIKRYSGSRPQNTQYYFKEGLTW
TYIKESGRRFGYLPEGSVFSHTGFMLFPPDRSSLWELLSYTNSDLFTYLMLSQTTERMWEVGEVSRLPWR
DELEELDELEELAKEQVGHLISKRQYDFASPYYIGPELLPVLGVDDPLFFYDHPHRTLREDLELDQPEET
ASPSASLRELGTAAAKHLEEIEKELEDCADEIDEAVFDCFGISEEQRETVLQEIALRTIEDPRDREVPDP
ESVTEPPDDFPEQVKDLLLHFALEAVREEDDGIIPLSGIDGEPDLLDRIEDEFERVWGEHAEDRLAEVDE
VLGSESAAEEAYPNLRAWLEEDLFDYHVSKFDRTPIVWRFTTERLVSDPEGEGFACLVDYHQLDAGLFDR
LQNRYLEPRKAELRERRSAANRRRNDDSLSASEQAEAAEEYERCESGLEQIEVFEDRLQELAQPSPRDWD
DEDRELAAAAAERVAEFRERTAERLETLDELAEMEDVDFGDLFSPNFYEKVEEWRDEWIDALDDLETAFE
AYAAPADEPVEAHLYDLFDYFNDDLLGSSHYASNGILFMTYYFDRFGAADQDRLGDAGLSERERLLSSLA
SDLDEYKALAEEIDDDCQAISSRISSDWADRALSEITTAGYQPNHKHGVEINITPLADAEIVPKTVDDEV
L
>gnl|CDD|468040 NF033455, BREX_6_MTaseX, BREX-6 system adenine-specific DNA-methyltransferase PglX
TPDAKAKLSKTIRALRARLLDDLHEAAESTYRLSIPPAKAAGLSEAARERRRRLEAWLAEQVRAQGGKKN
KKAKARSRERFLRDAEKEAAATLLNRLVLLRHLEALGLSKPAVVTGGWQSPGYREFREFAPDLCKDETEG
YGFLLQLVFDELALELPGLFGDVGLTELFPVPAATLRAVVEALDAPALESAWTDDTTLGWVYQYWNDPER
EALDAKLNGGGKIEPHEIASKTQMFTERYMVEWLLQNSLGPMWLAICQKHGWTPEAEADGTLARLEARRA
EWRAKREAGEVALDALMPIETELEERWKYYVPQPIPDDAVEHAPESVRDLKLLDPACGSGHFLVIAFDLL
FALYREEARHRGESWSDREIVESILENNLHGIDLDPRAVQIAAAALWLKARAVAPDARPKRLNLVASNLR
LASLPDDDPALVELRREVEAETGIPEALTDRIVEALAGADHLGSLLKVDAAVDEAIADYEKELGRSPAQG
DLFQGFSEQPIEKISGGEEARATLLDKLEQFLARHTGGDDLGLRLRGEQLAAGVRFVRMVREGRYDLVVG
NPPYQGTSKMADASYVAKHYPRGKADLYAAFLERGLQLVRPGGVSAMLTMRNWMFIKQYSALREHLLDTY
DLRLLGDFDRGAFEEVPDEVVAVAVSVFRRAAPAAEESVAIQPTPLDDPSRDRGRTARKRAALLCQVGRF
EFDSDRFEVIKEKPLVYWWDKEFLKRYAEAPKLGDVAPVRKGMCTSDNTRFLRRPWEVKTSSVARRRSSA
DSEPEQLQRTWVPYIKGAKGRAWFEPLSEVVLWEDSGLEIKVLEEYLYGSYSRTIKNEAFYFRRGVAFTT
IGSNFSARLHRYRSVFGDKGSSVFPEDIAQVVCLMNSSVARDVLSSLNPGLSFTVGDVNRLPLFPIESAD
AIFSQLEGAFTEHEAAREPSVEFRRPGPSPWRYAQDWAQQAVDRPEGAPLPDYDPEYDPPPPTDHLSFAL
GVALGRFGANGEGILDPTPADLSHALPHGILFLSAYSDDEDRRPDSLGHPACAPLHAAWAEHGSAIGKRA
SLRDWLRLDFFKDVHKGMYENRPIYFPLSSANKTFVAWISIHRWTDQTLRTLLADHLLPELRRLEGELAD
LRAARNSGDKKTAAKAEKRYAEVQKLLEELAEFIALVRQCAERGPPPTDPKCPPREVDARYDMDLDDGVM
INSAALWPLLEPQWKDPKKWWKELATAQGKKDYDWSHLAARYFPTRVDEKCQQDPSLAVAHGCFWKYHPA
KAYAWELRLQDEIGPDFTIDEPGSDEHRQAFLREHPKEALAIIEKEAKRRERKAKKADA
>gnl|CDD|380298 NF033456, RiPP_CCRG-2, CCRG-2 family RiPP leader. This model consists of the conserved leader peptide domain of CCRG-2 family ribosomal peptide natural products (RiPPs), up to the Gly-Gly presumptive cleavage site, plus one additional residue (hydrophobic, or another Gly). Members are found almost exclusively in the genus Prochlorococcus, in multiple instances per genome
MTNNELTIDQLQSIAGGG
>gnl|CDD|380299 NF033457, elgicin_lanti, elgicin/penisin family lantibiotic. The HMM describes the elgicin family of lanthipeptides active as bacteriocins. The leader domain occurs in additional proteins that lack homology in the core region, although sharing richness in Cys residues there
MANNNFDLDVQVKSVNPANSNLGLYTSTCYSSQCYSSKCYTDSCYSSDCYTGRHQCGYTHGLSC
>gnl|CDD|380300 NF033458, lipid_A_LpxG, UDP-2,3-diacylglucosamine diphosphatase LpxG. Members of this family are LpxG, the lipid A biosynthesis enzyme UDP-2,3-diacylglucosamine diphosphatase ()EC 3.6.1.54). This family is unrelated to the more common LpxH, or to LpxI, which share the same activity
SESLSDAWAIPLVIGIWARFIEPNLLRVSKLTWKLPKKPAHLHGLRIVQISDLHFNKSVPQKFLKKVSRK
IKSLSPDILVFTGDFLCRAKLEDKERLKAFLNSLHAPLGCFAILGNHDYDSYVSRNIKGDIDVIPPSSSR
PLKRAFISLLQGLFPSGHYKYAENLKPQEPHPELLTLLKNTPFRLLHNETHQIPDTLNIVGLGDLFAKQF
DPEKAFKNYNPTLPGIILSHNPDTIPLLEDYPGDLILSGHTHGPQINLPWPKFANKIWNKFSGLENPHLA
RGLFLFSEGKKQLYVNRGLGGLKRFRFFSPPEICLMTCKYE
>gnl|CDD|380301 NF033459, DksA_like, RNA polymerase-binding protein DksA
NELKEFKNILLERKEQILKNINSSSNEIEELRNSELNDEGDYASISTDSMIEYAISNQQKKELNEIEEAL
KKIKNGTYGICEMCEEPIGIERLKVKPHAKYCITCREIVEKEN
>gnl|CDD|380302 NF033460, glycerol3P_ox_II, type 2 glycerol-3-phosphate oxidase. This FAD-dependent enzyme (EC 1.1.3.21), glycerol-3-phosphate oxidase, also called L-alpha-glycerophosphate oxidase, converts sn-glycerol 3-phosphate plus oxygen to glycerone phosphate plus hydrogen peroxide, which contributes to virulence. This form, called type 2, is shorter than type 1 and is found exclusively in Mycoplasmas and other members of the Mollicutes
KYDVCIIGGGIIGASIAYELSKYNLKIVLLEKNPVVAMETSTGNSGVIHGGFDPTPGKLNAKLNVLGKKL
WQEDIFKELDFPRAKIDSLVLAFNDEEMKHLHMLYERGLTNGLNPEELKILDKEELLKREPNINKEVVGA
LLCNSSWAIDPVEATKALLKNAIKNGVELKLNSKVTSIKKENDLFEITTNNGEIIKAKIIINAAGHYADE
IAKLAGYPDFKLTTRRGEYRILEKSENGIVNSVLFMVPTIHGKGVIVAPMLDGNILVGPTAEDNVPKEET
RLVTREKYDEIGKIGKKIIPSLDMEKTCMTFAGSRPIDIETNDFVIKPAKNNKNFINVAGMKSPGLSSAP
AIADEVVKLVK
>gnl|CDD|411122 NF033461, glycerol3P_ox_1, type 1 glycerol-3-phosphate oxidase. Glycerol-3-phosphate oxidase, also called alpha-glycerophosphate oxidase (GlpO), is an FAD-dependent enzyme related to the glycerol-3-phosphate dehydrogenase GlpD. Notably, GlpO releases hydrogen peroxide, which can contribute to virulence
TFSIKTRQESIQKLQDETLDLLIIGGGITGAGVALQAAASGMKTGLIEMQDFAEGTSSRSTKLVHGGIRY
LKTFDVEVVADTVKERAVVQGIAPHIPKPDPMLLPIYDEPGATFNMFSVKVAMDLYDQLAGVTGTKYANY
TLTKEEVLEREPQLKKEGLQGGGVYLDFRNNDARLVIENIKRAHEDGALMASRVKAVGFLHDENGKINGV
KAEDLLTGETFDIHAKLVINTTGPWSDKVRNLDKKEALVPQMRPTKGVHLVVDRSRLPVPQPTYFDTGKN
DGRMVFVIPRENKTYFGTTDTDYTGDYKHPTVTQEDVDYLLEIVNNRYPEANITIDDIEASWAGLRPLIS
GNGGSDYNGGNNGKLSDESFDEVIDVVKDYLNDEASRDDVEKVLNNLESSLSEKELNPSAVSRGSSLERA
EDGLITLAGGKITDYRKMAEGALKLIQKILKEEFNRSFELIDSKTYPVSGGEIDPTNVDEELEFLAKQGV
EKGLSEEDALYLANLYGSNAPKVFALIDKVEPAEGLSLAETLSLHYALDEEMVLTPVDYLLRRTNHMLFM
RDTLDEIKQPVVDEMADYLGWSDEEKAAQTEELEEVIAESDLKYLKK
>gnl|CDD|380304 NF033464, cyanoexo_CrtC, cyanoexosortase C. Cyanosortase C (CrtC) belongs to the exosortase/archaeosortase family of multiple membrane proteins that act as cysteine proteases, and probably as transpeptidases, analogous to (but unrelated to) the sortases. CrtC is known so far only in Cyanobacteria, and appears so far primarily in the lesser-studied genera: Leptolyngbya, Oscillatoriales, Scytonema, Alkalinema, Phormidesmis, etc
KTHHGRIVLLGLLVGLFYLPTWLGFLVDRTLKGSSSLLLNLGFLYLGLRQLWKQRQQLAQLKASEEDRWL
GHLLILGGVALFPFCRFSLWPQALLWLLILAGIALSTWGLGFFRRYPLPILLILLSLYPNPGFIARTLWR
FFTPPQFLERLMAWVGSWALRAIGQPATAQGQFISLPTGAVEVAWGCNGFDMAFTMAGASLLLGLLFKQS
WPQTLLLIGLGIVLALIFNVPRIMLLTIAAVYWGKESFEFWHGPWGGQIFSGILFTVYYYAVMAILNR
>gnl|CDD|380305 NF033465, PTPA-CTERM, PTPA-CTERM protein sorting domain. This C-terminal sorting and processing signal, called PTPA-CTERM, is a variant of the widespread PEP-CTERM domain. It is restricted a subset of Cyanobacteria that encode the sorting enzyme named cyanoexosortase C
VPTPALLPGLVGLGLAALRKRKE
>gnl|CDD|380306 NF033471, J25_fam_lasso, acinetodin/klebsidin/J25 family lasso peptide. Members of this family include precursors of at least three lasso peptides, namely microcin J25, acinetodin and klebsidin. All members of the family are encoded as neighboring genes to homologs of the processing protein genes mcjB, mcjC, and mcjD
VKKVSVISIKKSASKMTRGGDGPIPEYFNPPGLPVNFYG
>gnl|CDD|439404 NF033473, trim_sens_DfrEf, trimethoprim-sensitive dihydrofolate reductase. This dihydrofolate reductase was originally described as the intrinsic dihydrofolate reductase of Enterococcus faecalis, sensitive to trimethoprim and incapable of conferring resistance to that antibiotic. Although the protein was referred to as DfrE by Coque, et al. (1999, PMID:9869579), to contrast it with the much rarer, resistance-conferring enzyme DfrF, we do not use the term DfrE, as a name in that series suggests a TMP-resistant form. Instead, we reserve the name DfrE for the trimethoprim-resistant enzyme WP_012655890.1 and close homologs, as described in PMID:34374564
MLAAIWAQDEQGVIGKEGKLPWHLPNDLKFFKEKTIHNTLVLGRATFEGMGCRPLPNRTTIVLTSNPDYQ
AEGVLVMHSVEEILAYADKYEGVTVIGGGSVVFKELIPACDVLYRTMIHETFEGDTFFPEIDWFVWEKVA
TVPGVVDEKNLYAHDYETYHRNDK
>gnl|CDD|468041 NF033474, DivGenRetAVD, diversity-generating retroelement protein Avd. Avd (accessory variability determinant) is part of diversity-generating retroelement (GDR) system through which a portion of a protein-coding gene can be rewritten, creating diversity that can affect host range. The founding member of this family, bAvd, from a Bordetella bacteriophage, belongs to a retrohoming element called BPP-1. Members of this family are four-helix bundle proteins, related to those of family TIGR02436, some of whose members are found in long intervening sequence (IVS) regions in 23S rRNA
LPIIQKTYDLIKYLYPILQRFPKSHKFVLADRILNALYDLLELLIEANKRSNKKSKLYALDAELDVLRYL
LRLAADLKLLSPKRYEYASRLLNEIGRMLGGWIK
>gnl|CDD|380308 NF033477, EmaA_autotrans, collagen-binding adhesin autotransporter EmaA. EmaA (extracellular matrix protein adhesin) is an outer membrane protein first described in Aggregatibacter (Actinobacillus) actinomycetemcomitans, a member of the Gammaproteobacteria. It is a glycoprotein, and has a C-terminal beta-barrel domain that marks it as an autotransporter. It serves as an adhesin that binds collagen, the most abundant material in the host extracellular matrix. It shares homology with the collagen-binding protein YadA of Yersinia enterocolitica
MNKVFKVIWCKTSQTWVAVSELSKAFSLSTTTDTPKKSSHTSQLTKIFIASAPLLFLFNVNAYIAIGSVE
NNSVKSEGANASPRTSRTGNSPFNYFNPGSKSYDNKDQPNTPNRLYDSRYAYGIAIGKNTDARDADQDSN
GIALGDYSKATGGLAMALGSFSRAEKNGGVAIGTASRSSGINSLAMMRQSAATGDYSTAIGSVAWAAGES
SFALGASATAKGNQSIAIGSLEQKVSPTGSGVPITKYNGLDNTQTNGDRSMALGTAAKTNGDDSFAIGYK
SQTGEFDIVHDSYLNENVTSANTSKKANKAIAVGTNALAQKESSIAFGYEANSLGVNAISIGANANAAYD
NVVAIGQSATATKSGSMAIGQGAQSNFKNSLALGTGTVVNSVDGGQSKFTSQNYDVENGVISIANVGKER
RIINLAAGRNDTDAVNVAQLQYVNKNLAKSIGGDNYTGYSDADGHTYQAPVFNIKNAQYNNVKAAVEAAQ
TNYVSVNSSNKANNSNYDNKGAKAAGSIALGDTAVQKAAQDAIKVSGTSPITVNKTTVNGVDDYAVSFNG
TEAAKSIPLTYKANGNNDKTVMLNKGLNFTNGTMTTASVANDGVVKYDVNLSTIKVENGKAAVAGTPVNG
ANGTDGKDGVATVKNVVDALNKAAWTITASKSEGEVAGNASKEVKNGDTVTYDAGKNIKITQNDKKFSFA
TKDDVEFTSVTTGNTKLTTNGVEITNGPKLTQAGIDAGNKKITDVADGVIAANSKEAVNGGQLFTETAKA
KTTVEKGDENIQITSETATDGHTNYKVALKPSLTVGPRTNGHPITINGNDGHITGLTNKSWTGTPTSGRA
ATEDQLSVVDKKFDNKVSLGGDNGRTTEKALSHTGGIKFNIKGGDSQKYVTTTASGDDVTVDLAQTTKDK
IDNAADKNLSNITNDGKKAITGLGAIVEAADNTITVTNETDNVTGQKTYKIKANIPTPEKTAMASGKNTV
IDGDGSAANPFKVDLKDDLELGQKDAGGINGKDSSVKVNGKDGSSVAINGKDGSITLNGKDGANPVSLKT
TQGPAGLNGTAPKDRLTVNNEAVATLEDGLQFAGDNGTDEVINKKLNQKLEIVGGADKTKLSDNNIGVNA
NNGKLEVKLAKELNGLTSAQFKNGDNTTVINGNGMTITPKDPAKAVSVTDKGLNNGGNQIVNIDSGLKQA
DGSAVALKDASGDTLKNAVNVGDLQKSINDITDATKNGGFGLSDDNGTTAKANLGETVKVKGDGSVITKV
VTDNGKPTLQVGLAKDITVGDNTNPGTITVKGENGKDGVSINGKEASVTFAKDGKDGMSLAGSRDAEGKD
AITIKGKDGKDGVSFKEDGRITNVADGVDDKDAVNKSQLDKSIAQAKSGVNAGKNITVTPQKNADGSTTY
TVETKDDVEFTSVKSGDTTMDNNGISITGGPSVTKDGINASDKKITGVKDGDISATSKDAVNGSQLHQTN
QNVNNLTTTVNKGLNFQGDNQEVTVNRKLGDQLNIRGGANPKKLTQNNIGVVADKNGTMTVQMAKDVNLG
PDGSLTVGNTTVNNDGIAIKGGPSMTQSGINAGGKRISNVARGKAPNDAVNMSQLQEVGNAINNRIDNID
NRVNKMDKRRKAGTASALATAGLMQPHRDGQSALVAAVGQYQSETAVAVGYSRISDNGKYGVKVSFSTNS
QGEVGGTAGAGYFW
>gnl|CDD|468042 NF033479, Efa1_rel_toxin, LifA/Efa1-related large cytotoxin. Members of this family are large and almost certainly multifunctional proteins found in various pathogens from genus Chlamydia, about 3000 amino acids in size and related to lymphostatin (Efa1/LifA) from enteropathogenic Escherichia coli. Roles have been suggested for Efa1 (EHEC factor for adherence) in adhesion, so some members have been annotated as adherence proteins rather than cytotoxins
DSRLVLYDELVNQNHSTEDVVKIGAQLQQQFYNLTTSKNVSFSASPSHHTGNWKTSLLYNLAQLVAHLFP
TTIQPARITKVTISPPQENSTKTNTTSSSKKLSTKQSSVSSFSRKSPRLGGGVNVPKHTPKPKSRVESSS
KISRKPRSVSRRKRALEKDPQQAASQKYDLTAKNIAEKLKLTPEQQKKCQKSLNNLKKAINRYNALREKN
SRKGQSLLVKQSKFLEEIQKKAKLTEEHESIQVMTTIKTEFKSHRVQVDKHIHGIWIAGAPPDGTDEYIK
TFLQTYPDFDFLFWVDEKAYGAAKFSSILKKIAFDAAIKELRESTPESVQAFIKKYDELKKKYDSTKNPE
EKNQYLEDLQKLYEKYNKLSKEIRSNFDALFLKNMVTSQDSFFNYCLLKGVGTISDETRIEYLEKELKLP
EEEIEQYKKLIEANKKKIKDIVKKVNKDLGSERVFIKDIKELKSMQDKTNLYNYEMEMFLRWNYAAATDQ
VRMYMLKEYGGIYTDLDMMPQYSQEVLQIIMDVGGSRFFEDLPIRRAISDAVLKLANGESTTVSIEEISK
DIDISKLTREDKTKLSELFKDLETFSKASNSSKKSSKKKSFFQRMSPDVVRDFMPILQRYHKWSTGWNVR
GLNGLMMAHKGSAVVDAVIKGQRQAYDELKALRENVLSGEFFNSLEDLKHLDHKSLIGGHLVKDYLGKSL
FFDFRQDSIIPGAVSTLGITGPDLIMKEMVEYFRDLGPIGEDFLEPRGKKLGKAAFLGAYKKIKDDGGKT
TFDWLNPLSVGANDVTPADESTWCGSKQRCAAELLFSDSSKLSDEKPKGITRTRVDKEDFTKLWSEESKK
KLPPDLLDRFNLLIESSNLDILKLSELDRDIYVLMTAIQDDPAAKASVFSLQLQLAELIRSVPFPISNQV
NFFPNAQKNFESDLEKAIKLYLKSHSQTKIVLWHSSTSDRVLFLKDMLAIAERRLAIKNLISSKDQSPLS
SEEIELLTSYEELKAKDSLDLLSEAELEKFLEVTTQIAENPELFSKISQIEEQISSGYLYRDLEETLSKW
LSLSEQDRKKKILDFLKELEKDDEKGKSDQKEHKKWYEELYDKAYKKRVTEPKKKIQELIKKFQENERVI
LLNIDEYLSKNPLFQRMHKDGYAFADFTEITRFMLADAGISGIFSSDSIFPAPSKQLVDIMKTTLGEDYD
DMQDALPTVYDWLAEDPNSEEAKQAFDKIPEGLREKLEGYTPHDLLTPPIDSSVSALGMRYGTEEGRESE
HVMTSIAPGFFNPASYSMARYLEALYEIHREIHSGSLTSEKAKKILQSKGAACFINETGIDLLLQYSKEK
YYLSLTEIHKILTGQVNLAEASSALLTGALPGIGRIILRDGDFGRPLATTMTDSVALNSYDYRGVGLSKD
LFSTPHDVPTIQSIVEQAKYTLLSWPEFYERHAGIWSDLANRLGAESLSVHPQTFLYDTEGRCMGLSMLY
MSAEDVVSYRLLQENLMTVSSLFQEKEREHLPLTPADQKFLDRSLSLIDWLQYQGNKELQTGGIFSPLSW
DIPTLTKKFEKSTVKSVLITTPTHSLTLHFLGSFFRVTDPNFGHVDFPSLEAALYFLEEMVQVSPEIKAR
YGISDDKSVSEQLKVYSPDTQEAENALFSSTDAGLLSQHQMTTLEKMIVRGEVTISQIRTTWATLYKIGG
TIDHKRIDETTRESDLDKLKINGDVLSDFLSKNVLDSDLVSLIQTLLETHGLEPGTKLVSPSAIVETPND
VASLLQTSKNKTSRMKSMLQVLLSEISKKIKSIGLKDSDKVSVKSVEVDDSDKITVEFKKGSSQLKTISF
KGKGLADSFRKFGAMLNELAGTGVMDLELGMSIVSLVQYARLVEAGKGKDALAIFNLVLDVKELAEMTLG
SVIQALGKKFITQEGIDGFRLETALASQLQKVGTRVGGTVGKALSRAARVLELPVLETVAGVWNLYNSVE
ELLHADSHSDRVAARVQVAFDVITLALTLSSVVAPALMLAAGPIAAIGMGAASIARNVAYKEERHEQWLK
YKKFLEDGSKHVVFAFPERGLLDLSGNQVLGNIYLDLRQNPPILKGDRSYNANRWIGHKPGWTDWQVRDR
LGYAYRISPTYALAKGHANSFWPREIPSIPKGVYRTVILGYGITYKAVTEVVYLSNQVVWREAVMEPDSR
YYQPPLTAESKSSTIIAGDTPLTVIPVRLLDEDSKERIDQAASYKDYKIIIVGGKGGLTVQIGGAGYYNL
TGDPGAKNTISFRAIPPPLSVTFNLSHLEQDVPLIRPNGTKINILKIKQTGFNTIIGSSGGYDTLTGNND
TKFYLSPGGGTIYSGLGKNWYHIPKLTGRLDIILASNSTEHLLLLEMKSYEWKPVGENLNLIPRYLNGNN
TSGIFISNEDKSTSFSRWVGKFTVKLADGITLQALKKIHPGNTTNRVTLGVKSCDQTKWQKKHPEEPGYP
ENILKWLKKLSWWFAPEVTILQKEGTAVFFTTDKSLVYRPDPYSELSIRAQDGYNTVVQGSVGCTYILSS
SPNVNTKTIEITLAEDDDYPQILDLSSLVPTSIRGKMTNGTNNSIDLEISSPRYTIPLSLSWKGHELPRQ
TRIEINPNHRPRLGEWYDILQKNPGKWHTLYHNSMLIPERIEGVLSLNNTVTLMLSENRRNNEHILGVEN
RGDVNLKVLGQLQSGHIKGAMEENLRWKTFFNLKKFDITVPAHSIKYLAFKGEEKSGDNILFYSVLEPKT
LEAKQKPLTQISRHKWSSYDEIQVFATSLNLEDFQRYRISEETPALSRQLMYAQNLVSIQNRDFILKFFY
VREGSGIGAIRLVFKNFFVESMEGITEKTLEREAKPILAENPISLINPSYREHLELILGEETLNLAILVQ
EFSSTSHILPLQEDKATHELLEPPRYRAKNLAVLTYTIDPKKIYTSEGRTLWKFIDPAMKEYRLPLPTIL
EASYYLDPVSGDLYLTRIILFNPQVEQAFVIKFKGYKRHWLEFQNIFISGSHTRTISSSGTILTGLMFVG
PELRHLEIDFAKNTIGGTSLKERISSRSGIVFPTNDQVVHYDPRIAKQFYSYIDYMLWDLRDRAKGSKRA
KAYDSYLLEAAMHLDDKNPQWKIPPSVLEYAIGYYRAVVSTWVKNRIRVGTLIKLPAGSITISLITTQNE
IFAKKRDSGFAIYYSILGLNKHVKPVHQVPGDMLLDIKKDVVLTVKKVDESDYDKKRIYVVLELATEEER
KLR
>gnl|CDD|468043 NF033480, bifunc_MprF, bifunctional lysylphosphatidylglycerol flippase/synthetase MprF. The C-terminal region of MprF tranfers lysine from a charged tRNA onto phosphatidylglycerol to make lysylphosphatidylglycerol (EC 2.3.2.3). The N-terminal region of MprF acts as a flippase. MprF helps confer resistance to antimicrobial cationic peptides
RRLLKILFVLAVLILVLFELHRLLKEISLADVLAALSALSPWQLLLALLLGLLSVLPLLGYDFIALRYLG
LKLPLRYIALTSWIANTFNNLLGFGGLTGGALRYRFYGKAGLDKKDIARVISFVALFFLLGLSILSGLAL
LLIFFALSLLLGLPWYWIWLLGGGLYLPLLLLITLLLKRRGLFDLTLRIGGWKLRLPLIGVSLLQWLAAA
LDFLAAGAVLGVLLPAFPAFLPIFIIASVAGVISMVPGGLGVFDLVMLLGLSQLGVPDEQVLAALLLYRL
FYYLLPFLIGLILFAKEEGRRANREPLARLDGLPRRLLQKLAPLLLAILVFFSGIMLLLSGATPALSERL
KLLRPFLPPFIEASHLLSSLLGFLLLLLARGLARRLKRAYWLTLVLLLLGIVFSLLKGLDYEEAIVLLLL
LLLLLLSRKEFYRESSLYSWELSLGWLLAIALVLILYIWLGFFAYRHVPYSNDLWWQFALFPSEKDAPRG
LRALLIVALVLLLFALYLLLRPPPKPLGPDFDELRRAAILVAYGGNTDSHLAFLGDKRLYFSQDDTAFLM
YRIKGNSWIVLGDPVGNPEAFAELIWEFRELADRLGYRPVFYQVSEEYLPLYHDLGLDFFKLGEEAVVDL
EDFTLEGKKRKGLRAALNKFEREGYTFEVLEPPFSPELLPELKAISDEWLAGKKEKGFSLGFFDEDYLQR
APIAVVRDEEGKIVAFANLMPTYDKEEASIDLMRHLPDAPNGTMDFLFINLFLWAKEQGYRYFNLGMAPL
SGVGQSRLSFLWERIAALVYEHGERFYNFQGLRAYKEKFAPEWEPRYLAYPKGSSLLFALLDLTRLISG
>gnl|CDD|411124 NF033481, auto_Ata, trimeric autotransporter adhesin Ata. Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane
MNKVYKVIWNASIGAWVATSEIAKSKTKTKSKTLNVSAAVLSGVICFAPNAFAGTNTEGGIGQGTSISGT
TSCREGSANTANQKDIAIGCGAQTQDRTGSNIANRNNPYNNSTGAYAGAMKQGGAISVGTGAVVEKGLGT
AIGSYATTQGISGVAIGTGALSSGNTALAVGRQSAATADFSQAIGNVAAATGKGSLAIGHSATAEGYRSI
AIGSPDIENADPVAGQAGAAYQPKMATKATGKDSIAFGGGAVATEENALAIGAFSESKGKKSVAIGTGAK
AQKDNAVVIGDQAEASFEGGVAIGKGARSEAENSIALGKDSKASQATGESFLTKQSAPTGVLSIGDIGTE
RRIQNVADGAADSDAATVRQLKAARTHYVSINDNGQQGGNFENDGATGRNAIAVGVNASAAGREAMAIGG
SAQAIGSGAIAMGSSSQTVGRGDVAIGRNASTQGAEGVNSNQSVAIGDQTKAIGDQSVAIGADVIAKGNS
SVAIGGDDVDKIARDTELSNTYTEITGGTLQAGKYPTTEANHGSTAVGVQAVGTGAFSSAFGMTSKATGD
ASSAFGVMSNASGKGAAAFGAVAQATGDGASAMGINSLASGTNSTAIGSGNKPGEGAKATGNSSAAIGSG
AQATGDNSAAIGKGAEATNENAAAVGGGAKATGKNAAAIGGGAIADQENAVAVGQGAQSLVEGGVALGAR
SKVEAKNSVALGQDAVATEATGTSFLTNRDASQSNGVISVGSAGKERRITNVEDGSADSDAVTVRQLKNV
DSRVNQNTSNIGKNTQNITNLNQKLDDTKTNLGNQITDTNKNLNDAKKDLGNQITDTNTKLNTTKDQLTT
QINDTKTELNNTIGNTKTELNTKIDNTKTELENKGLNFAGNSGADVHRKLGDKLNIVGGAAASTPAAKTS
GENVITRTTQDGIQIELLKDSKFDSVTTGNTTLNTNGLTIKEGPSITKQGINAGSKQITNVADGINAKDA
VNVDQLTKVKENLNGRITDTNNQLNDAKKDLGNQIADTNKNLNDAKKDLGDQITDTNTKLNNTKDQLTTQ
INDTKTELNNTIGNTKTELENKGLNFAGNSGADVHRKLGDKLNIVGGAAASTPAAKTSGENVITRTTKDG
IQIELLKDSKFDSVTTGNTTLNTNGLTIKEGPSITKDGINAGGKQITNVADGINAKDAVNKGQLDNLAAK
QNATDDAAVKYDDAKTKDKVTLKGKDGTVLDNVKAGHISSTSKEAVNGSQIHNISNSIKNSIGGNTVVNP
DGSLTTNNIGGTGKNNINDAISEVKNTATKAKTTVTEGDNIVVKETVNKDGSTNYEVSTKKDLTLNSVTT
GDSVLNNNGLTIKDGPSITKDGINAGGKKITDVANGVIAQNSKDAVNGGQVHHISNSIKNSIGGNTVVNP
DGSLTTNNIGGTGKNNINDAIKSVDEKVTNGVNDLTQKGLNFGANDQKTTQGKAVHRKLGDTINIVGGAN
PETAEDKTSGENIITRTTEDGVKIEMLKDVKFDSVNVGGHVLNQQGLTIKGGPSITVNGINAGGKQITNV
ADGINAKDAVNKGQLDKQINEVKDQIGKDIGKLSDHAVQYDKDKNGNVDKNSVTLGGGEKGTNLKNVADG
KIAEGSKDAVNGGQLWNVQNQVDKNSNDIKNIQNNIDNISNGKAGLVQQQKPNGEITVGKDSGGTSINMA
GKEGDRVVQGVKDGEIKAGSNQAVNGGQIHKISESIKNSIGGNTTIDPKDGSITTNNIGGTGKNNINDAI
GTLNQSNQELGNKITNLGDQLQQVFYDTNKRIDDVEKKANAGIAAAMALENAPFVAGKYTYAVGAAYHGG
ENAVGVTLRKTSDNGRWSITGGVAAASQGEPSVRVGISGVIN
>gnl|CDD|468044 NF033482, RiPP_thiocil, thiocillin family RiPP. Members of this family are ribosomally synthesized and post-translationally modified peptide natural product (RiPP) precursors. Nearly all contain at least one Cys residues expected to be involved in thiazolyl peptide modifications, and are expected to behave at least in part as antibiotics. Genomes of some species (Bacillus atrophaeus, Streptomyces coelicoflavus, etc.) may contain multiple paralogs
DLYAEEDFELEELPEGNALGSFSTASSAGSASCPGSSASTASTASSAG
>gnl|CDD|468045 NF033483, PknB_PASTA_kin, Stk1 family PASTA domain-containing Ser/Thr kinase
IGKLLGGRYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVLRPDLARDPEFVARFRREAQSAASLSHPNIV
SVYDVGEDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILI
TKDGRVKVTDFGIARALSSTTMTQTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDG
DSPVSVAYKHVQEDPPPPSELNPGIPQSLDAVVLKATAKDPDDRYQSAAEMRADLETALSGQRLNAPKFA
PDSDDDRTKVLPPIPPAPAPTAAEPPEDPDDDGEGGEPADDPEKKKKKKRKKKLWLLVIILALLLVLGVG
LGFWAFGGFGSGKEVTVPDVVGKTEAEAKEALEKAGLKVGKVEEEYSDDVEEGKVISTDPEAGTRVKEGS
TVTLVVSKGPEKVKVPDLTGKSLDEAKKALEDAGLKVGTIEEEYSDDVPKGTVISQDPAAGTEVDKGTTV
TLTVSKGPEPVTVPDVTGMSEEEAKSALESAGLKVGVEEEEVSSDVPAGTVISQSPAAGTEVAKGSTVTL
TVS
>gnl|CDD|468046 NF033484, Stp1_PP2C_phos, Stp1/IreP family PP2C-type Ser/Thr phosphatase. Many Gram-positive bacteria have a protein kinase/protein phosphatase gene pair that responds to peptidoglycan metabolites and can be instrumental in resistance to beta-lactam antibiotics. Characterized examples of the phosphatase component are Stp1 of Staphylococcus aureus and IreP of Enterococcus faecalis
LTDIGKVRKNNEDYYGVFSNKNGINLFIVADGMGGHNAGEVASRMAVETLGEYFEENEEEEIEEWLKEAI
EEANEEIYEKAKENEELKGMGTTLVAALITDNKLYIAHVGDSRAYLIRDGELKQITEDHSLVNELVKSGE
ITEEEARNHPQKNIITRALGTEEDVEVDFFEVELEEGDYLLLCSDGLTNMVSDEEIEEILKSDNDLEEKA
EKLIELANENGGKDNITVILIE
>gnl|CDD|468047 NF033485, small_SCO1431, SCO1431 family membrane protein. Members of this family, including SCO1431 from Streptomyces coelicolor A3(2), are small and extremely hydrophobic proteins that lack an N-terminal signal peptide. Known members are restricted to the genus Streptomyces, where the protein family is widespread
TATSATAARARARTGGPKDDGPKLLEHVLGWTLVVVLAMLVTQLGLL
>gnl|CDD|411129 NF033486, harvest_ssl1498, ssl1498 family light-harvesting-like protein. Members of this family appear restricted to the Cyanobacteria, and include ssl1498 from Synechocystis sp. PCC 6803. These proteins are small, usually about 56 amino acids, with an N-terminal half related to a number of light-harvesting proteins, and a highly hydrophobic C-terminal half likely to be embedded in membrane
TTEEGGRLNNFAVEPKMYYAEYPTPEQQRNYLLQGALAALLVTGLILVAFAVS
>gnl|CDD|411130 NF033487, Lacal_2735_fam, Lacal_2735 family protein. This small protein is widespread but uncharacterized. Most members are shorter than 60 amino acids in length
MFGLFKKKSEVEKLQKKYKKLMEEAYKLSRTDRIKSDKLTAEAEKILKKIERLK
>gnl|CDD|411131 NF033488, lmo0937_fam_TM, lmo0937 family membrane protein. Members of this family are very small (about 45 amino acids) and highly hydrophobic, suggesting a presence in the membrane, and have a broad phylogenetic distribution. The member protein lmo0937, from the pathogen Listeria monocytogenes, is described as up-regulated when the bacterium is in the mouse spleen, suggesting a role in stress response
LWTIAVILLILWLLGFVGFTAGGLIHILLVIALIVILLRLITG
>gnl|CDD|411132 NF033490, small_SPW0924, SPW_0924 family protein. Members of this family average less than 44 amino acids in length, and are found exclusively in the Actinobacteria (mostly Streptomyces). The N-terminal half is organized like a signal peptide, beginning Met-Arg and then continuing with a hydrophobic stretch that is unusually rich in alanine. The C-terminal region has a nearly invariant motif TSPxPLLTTVP. The function is unknown
MRALVAAAIGLAAALALVLTVTAVGSPPGETSPKPLLTTVPAHP
>gnl|CDD|411133 NF033491, BA3454_fam, BA3454 family stress response protein. BA3454, a protein less than 45 amino acids long, is up-regulated strongly by SpxA2 during stress conditions. Related proteins are found widely in the genus Bacillus, although not in Bacillus subtilis
MIEVTVTVNYKGKNYQTNVIANKDTSEEEILRLAEEQVKKQWK
>gnl|CDD|411134 NF033492, podovir_small, putative phage replication protein. Members of this family of very small, highly hydrophobic proteins are restricted to the genus Acinetobacter, and appear to be entirely of phage origin. One member is encoded in the Podoviral Bacteriophage YMC/09/02/B1251 ABA BP (although the coding region is not predicted in GenBank record JX403940.1). Evidence suggesting the reading frame really does encode protein includes the overlap of a TGA stop codon with an ATG start codon at both ends of this protein, suggesting translational coupling with the much larger adjacent genes immediately upstream and downstream
MNKFEILAWGLLISFFTAAICGAVVLWWLARKEADE
>gnl|CDD|411135 NF033493, MetS_like_NSS, MetS family NSS transporter small subunit. MetS, as described in the Gram-positive bacterium Corynebacterium glutamicum, is the small subunit of MetPS, an NSS (Neurotransmitter:Sodium Symporter) transporter involved in methionine and alanine import. While MetS itself is small, only 60 amino acids, homologs in gamma proteobacteria such as Vibrio sp., similarly found next to an NSS transporter large subunit, may be barely half that length and consist almost entirely of a predicted hydrophobic region that would localize to within the plasma membrane
MTTSAIIMMVIGLVIIWGGLAASILIAMKK
>gnl|CDD|411136 NF033494, NSS_import_MetS, methionine/alanine import NSS transporter subunit MetS
MSGIAIIMMVLFIVVIWGGLVASVVHLRRHPDETSGELGTAPGTTDEVLIAQE
>gnl|CDD|411137 NF033495, phage_BC1881, BC1881 family protein. Members of this family of very small proteins (average length is about 50 residues) include BC1881 from the phBC6A51 prophage region of the Bacillus cereus ATCC 14579 genome
VSTKELSEELKKREGVETINVEPYEKIEVGGIKVEGPAIILINQD
>gnl|CDD|411138 NF033496, DUF2080_fam_acc, DUF2080 family transposase-associated protein. Members of this family appear restricted to the archaea. They tend to be encoded upstream of predicted transposase genes within insertion sequences such as ISNagr11, ISHca1, ISH36, etc. The widespread distribution suggests this protein may be more than a mere passenger gene and may participate in some transposase-associated function. See PF09853, COG3466, and arCOG03884 for alternative (currently narrow) treatments of this family
EEVIEKEVKPSGNSGRVYLPKEWIGKKVKIVRLD
>gnl|CDD|411139 NF033497, rubre_like_arch, rubrerythrin-like domain. This rubrerythrin-like domain is found primarily in the archaea, occasionally as part of a larger redox-active protein. It features two CxxC motifs with a spacer of 12 to 13 amino acids
YECFDCGTRVTAATHPGTCPDCGGELRNRAVPRE
>gnl|CDD|411140 NF033498, YlcG_phage_expr, YlcG family protein. Members of this family include YlcG from the DLP12 prophage region of Eschichia coli K-12, and homologs from the Gifsy-1 and Gifsy-2 prophage regions of Salmonella enterica subsp. enterica serovar Typhimurium str. LT2. Members of this protein family are small, about 46 amino acids long. YlcG is known to be expressed. It is encoded immediately downstream of the Holliday junction resolvase RusA
MKPELIEILRMRWQRLRLYRHRGSVLVDYRILRNFVRIYQK
>gnl|CDD|411141 NF033499, Xis_Gifsy_1, excisionase Xis. Members of this family are excisionases such as Xis from the Gifsy-1 prophage of Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
MSKKTFELMSTRDICSQLGISSRTLERYRKRPPDVNPFPEPDCSYMGGSNKWLKTKVAEWQLREMSRKTR
RPMSHLNLPRDSRGRLIRRDAA
>gnl|CDD|411142 NF033500, phi80_GamL, host nuclease inhibitor GamL. Members of this family, including GamL from phage phi80, are phage inhibitors of host nucleases such as RecBCD and SbcCD. This family has a distant relationship to Gam (see PF06064), which inhibits RecBCD
MNAYLTYDRIEERRWAEQQLTDEKEKWIDDRAQELIDMFPKEPLLFRSLFLPPDASEALRSEKAEEAYND
FISALAYAQAEEEWDRQTG
>gnl|CDD|411143 NF033501, ArfB_arch_rifla, 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase. MJ0116 from Methanocaldococcus jannaschii, the founding member of this family, was shown be 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase, catalyzing the second step in archaeal riboflavin and Fo biosynthesis
ELRLNSGNILNEKVHKIGIIALGSHLENHGPALPIDTDIKIASYIALNASIKTGAKFLGVVYPATEYDYV
KHGIHNSLDDLVEYIKFLLNSAKKIGIEKFLIVNCHGGNILIEKEIKDLEEKTGLKIIMNNKIITHAGTG
ELSMGYVIGIADETKLKEHTPEKYPEIGMVGLKEARENNKNIDEEAKIVEKNGVKVDEVLGQKLLKNAIN
SVVNDVKKL
>gnl|CDD|468048 NF033503, LarB, nickel pincer cofactor biosynthesis protein LarB. This protein, related to AIR carboxylase, is part of a three protein system involved in producing a specialized nicotinic acid-derived, nickel-containing cofactor, as used in the nickel-dependent lactate racemase of lactic acid bacteria
LDHHRELRTGFPEVIYGEGKTPEQIAEILEALLERGGRVLATRVDEEKAEAVRAALPDADYDELARTLVL
GREPPPPGKGKVAVVTAGTSDLPVAEEAALTAEFMGNEVERIYDVGVAGIHRLLARLDEIRQADVIIVVA
GMEGALPSVVGGLVDKPVIAVPTSVGYGASFGGLAALLSMLNSCAPGVSVVNIDNGFGAAYAAARINRL
>gnl|CDD|468049 NF033504, Ni_dep_LarA, nickel-dependent lactate racemase. LarA from Lactobacillus plantarum is a nickel-dependent lactate racemase and the founding member of a family of isomerases that depend on a nicotinic acid-derived nickel pincer cofactor. While it is not yet clear which homologs of LarA act preferentially on lactate, this model identifies one clade of architecurally similar proteins from among a broader set of LarA homologs. Note that the crystal structure 4NAR, on deposit at PDB but not associated with any publication, represents a protein from Thermotoga maritima that falls outside the scope of this family and that is annotated in PDB as a putative uronate isomerase
IKLPYGKGKLEVDIPDENLLGVLEPNAVEYLKDEEELIRRALANPIGSPPLKELVKGKKKVVIIVSDITR
PTPSKIILPPLLEELRSAGVPDEDITILVATGTHRPQTEEELIQIFGEEIVERIKIVDHDARDKEDLVYL
GTTSSGTPVYINKLVVEADLLIVTGFIEPHFFAGFSGGRKSILPGIASYETIMANHSLALIGSPNARTGN
LEGNPVHEDMEEAARMVGPDFILNVVLDSDKKIIAAFAGDLVEAHRKGCEFVKEIFGVPIPEKADIVITS
AGGYPLDINLYQAVKGLDNAEAAVKEGGVIILVAECRDGIGGEEFEEWLANADTPEEVLEKIRKEFELGQ
WKAQKLARIALKAEVILVSDLPDELVKKMGMKPAKTLDEALDKALEKKGKDAKVTVIPDGVSTIPKL
>gnl|CDD|411146 NF033505, paceosortase, pacearchaeosortase. Members of this family, pacearchaeosortase, are archaeosortases from the uncultured (so far) Candidatus Pacearchaeota archaeon lineage and its close relatives. In most assemblies where pacearchaeosortase is found, only one protein can be found likely to make it the target for sorting and cleavage, and it is encoded by the adjacent gene. This dedicated arrangement suggests the adjacent gene encodes a critical surface protein, most likely one that helps form an S-layer
FSNLIIRYIVLLLLGLFSLAIFYFIFTPLTIYPVYYLLKLFFDASLLGNLIFFNGYTIEIIGACIAGSAY
YLLLILNLTTPNIKLKKRIKSLFFSFILFLILNIIRIVILSILLVNGSSYFDITHKLFWYFGSTIFVVAI
WFLTVKIFKIKEIPFYSDIKFLYKNSK
>gnl|CDD|468050 NF033506, PACE-CTERM-PROT, putative S-layer protein. Assembled genomes from the Candidatus Pacearchaeota archaeon group and its close relatives, so far all uncultured, have a single archaeosortase, called pacearchaseosortase. A search protein archaeosortase targets, with a C-terminal domain resembling other archaeosortase and exosortase sorting signal regions, found this family as the best candidate. It is nearly always encoded by a gene found adjacent to the pacearchaseosortase gene. This dedicated arrangement, a sorting enzyme encoded next to its only predicted sorting substrate, suggests that members of this family, called PACE-CTERM, may be an important and abundant surface protein, most likely the major S-layer protein
AKKFALIFLSLFALVVLASFVSSASLTTTPADLPEDVSTSQSFTFNLTNTGNLETATLSIPSLKNDGNVA
LNISLSISNGNFEVTFTVDPSTFTLNAGQSKVITITPYNLPSGFKFGLGTSTITAKAINGSGTANDTTTI
TFKKSFCSNGPIGGNLDIRSVNIDNNGDGNDDDDWYLLDEIEVEVKVKNNGDDDIRDVQVEWALYDSNGE
NVADDLDSDGDEEDFDLDIDDGDDETITFTFKVPADFIDDTDYRLYVKAYGDDDGEEELCIDTSESLKSE
FYGIDIRTEDDKEKFVIVDNITIDPNELICGETVSITGDVYNIGDEDQDRVYVTLYNSELGLDIEFEILG
DIDKGDSETVDFSFTVPKDAEEKTYSLEFLYDYDYNNDIYDNSSDDEAIVLTVFSVSGNCGITGSALISA
SLESDAKAGEELIVKATITNTGSESATFTVSASGYSSWATLGSISPRTLTLNAGESQDVTITLNVNKDAS
GDQTFNIETISGGQLANQPVSVNIEGSSAGGFFTGFSIGGNWYLWGIVLLNVILIVAIIIVAVRVARR
>gnl|CDD|411148 NF033507, Loki-CTERM, Loki-CTERM protein-sorting domain
IPGFPIVILLAFAGLATIILARRKRR
>gnl|CDD|411149 NF033510, Ca_tandemer, Ca2+-stabilized adhesin repeat. This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica
THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTV
PAADLAALADGTYTVTVTVTDAAGNTS
>gnl|CDD|411150 NF033511, metallo_CpaA, metalloendopeptidase CpaA
SAVYAATDLSPNQNGGSGDIPGGYADLDFYLSNGNWAKNLTLPNSAKDQDKITIQSSAGYKSYLDTSNTD
IPIESLTINSGDSFSFVYDASKKKWVIQAPTLSPNSNNGSGEIISLTNGKIQRVDLADGDWAQTITLPSN
VPDGSLLQVVSTAAYTSSISKQNLLFPSTFNLRKGDEYWFKYNAELQKWVPEKIPPTTLNVKNIGTQLNA
PVAPLTEVNFADGNWVPNFTLPATANDRDRIIVKSTATWSATISNTNINTTATLKLKTGDRYEFMYVKDK
AHWVLQSSPTKVITANSLITSQLPDMKQPVLRVKISNGNWQPQLNLPVKAQVGDKVIVSSTADWDFTVTA
ANGLSGTIKTGENRRFVYTAQGWVLDSRTIDMLLVNSPEVAAILGESAAKLRLIEGLRLTNEALENSNAK
FYLKSVGYLKYKIPASTLGDALNVGRSDTTVQAERKRVGADAVYYEGNEDGCGLAWVNASAYNMIGTGSL
GCGTTVMRHEFGHNMGLYHGDSTNIGSPYGFGHPLGSTIMGGNNIPYYSSPYLYNPKYGVRLGEEGKTDA
VRAINENSKTVSQFN
>gnl|CDD|468051 NF033512, T2SS_chap_CpaB, metalloprotease secretion chaperone CpaB. The cpaA and cpaB gene pair, as described in the genus Acinetobacter, consists of a metalloendopeptidase virulence factor, CpaA, and a tightly binding membrane-bound chaperone, CpaB, important for its secretion by a type II secretion system (T2SS). CpaA, in at least some Acinetobacter, is the most heavily secreted T2SS effector, and behaves as a virulence factor that cleaves factor V in blood and alters coagulation
KNIYLILGLALTGLVTAGLVLFLKGEPDASSASLQDQQVDQENVPSLASPESEVPRRNLSLDETDLEAAK
HEQPLLHEVGPDEVASHAPLPLSRQKSDGRMFIAYDPNVIESKKVGDTVKFQLPEYGINRHGVIDEIEKV
DGDIIRWSGSFEDGNPTQNFFTITQTMKDQYTIGQIYTDMGTYSAEIKNGQGWVMDQGVEDHLLH
>gnl|CDD|411152 NF033515, lipo_6_6_Borrel, Lp6.6 family lipoprotein. In Borrelia burgdorferi, the tiny lipoprotein Lp6.6 is plasmid-borne and was originally described as a major low-molecular-weight lipoprotein that could constitute 2% of the dry weight of defatted cells. Lp6.6 was later found to facilitate transmission from ticks to mice, and to be down-regulated after infection
MTKLMYAIFLSAILFVACETTRISDEMENTSDEDSKVTAPMPEDKSMKSTKKPMMKSMKK
>gnl|CDD|468052 NF033516, transpos_IS3, IS3 family transposase
EFKLEAVREVLEGGKSVAEVARELGISPSTLYRWRKKYRGGGEAADAGRLKELLTPEEEENRRLKRELAE
LRLENEILKKARKLLRPAVKYALIDALRGEYSVRRACRVLGVSRSTYYYWRKRPPSRRAPDDAELRARIR
EIFEESRGRYGYRRITALLRREGIRVNHKRVYRLMRELGLLARRRRKRRPYTTDSGHVHPVAPNLLNRQF
TATRPNQVWVTDITYIRTAEGWLYLAVVLDLFSREIVGWSVSTSMSAELVLDALEMAIEWRGKPEGLILH
SDNGSQYTSKAYREWLKEHGITQSMSRPGNCWDNAVAESFFGTLKRECLYRRRFRTLEEARQAIEEYIEF
YNHERPHSSLGYLTPAEFE
>gnl|CDD|468053 NF033517, transpos_IS66, IS66 family transposase. Members of this protein family are DDE transposases from the IS66 family insertion sequences, which typically consist of two accessary genes (TnpA and TnpB) and the third gene encoding the transposase
QPGHKGKTRKPLPDHLPREEVVHEPESCPCCGGALLHRIGEEVSEQLEIIPAKFEVTEYVRPKYACRHCG
TVVQAPAPARVIPKGQAGPRLLAHVAVLKYADHLPLYRQQQILARLFGIELSRGTLANWVGRAAELLEPL
YDALKEELLAAPVLHADETGVPVLEPGRGKTGWLWVYASAPPAVLFDYAPSRGGEVPEALLEGFNGVLQS
DGYAGYNKLAAVTHAGCWAHLRRKFQEAAERKGKSIAEEALKRIGELYAIERRIRGLSPEERRALRQERS
RPLLDELKAWLEAGLAGVLPKSPLGKAIRYLLNRWDALLRFLDDGRVPIDNNAAERAIRPVVLGRKNSLF
AGSDRGAEAAARIYSLIETAKLNGLNPYAYLRDVLTRL
>gnl|CDD|468054 NF033518, transpos_IS607, IS607 family transposase
GEAAERLGVSRQTLRRWDREGLIKVPRTPGGRRRYPEEEVGRLLGVKVPAGDERKTVIYARVSSADQKDD
LERQVARLTQYATAKGWQVDEVVTDIGSGLNEKRKGLLKLLDDILNGEVSRVVVEHKDRLTRFGFEYLEA
LFKANGVEIVVVNEDEKSPEEELVEDLIEILTSFSARLYGKRSAKNR
>gnl|CDD|468055 NF033519, transpos_ISAzo13, ISAzo13 family transposase
LLPHLDERQRRLYAAAEAKALGRGGISLVARATGVSRRTIRRGIKELESGGEETLAPGRIRRPGGGRKRL
EEKDPGLLEALESLVEPHTRGDPMSPLRWTCKSLRKLAEELKRQGHSVSANTVGELLRELGYSLQANRKT
LEGKSHPDRDAQFEHINAQVKAFQAAGQPVISVDTKKKELIGNFKNGGREWRPKGEPVEVLDHDFPSPAL
GKAIPYGIYDLGRNEGWVNVGTDHDTAAFAVESIRRWWQTMGKARYPHATRLLITADGGGSNGSRSRLWK
KELQKLADETGLTITVCHFPPGTSKWNKIEHRLFSHITRNWRGRPLTSHEVVVNLIAATTTKTGLKVVAE
LDENVYPTGIKVSDEELAALNITRDEFHGEWNYTIKP
>gnl|CDD|468056 NF033520, transpos_IS982, IS982 family transposase. Currently, there are 46 seed sequences in this family
SDSEIITILILGHLLGIDSFKAFYRFYIKHFPSSFFPLPSYSRFNRRCRRLLPLIEAIRQELAKKTKSEE
TGIAIIDSTPIPVCHNKRIKRHKVFKGIADRGYCASKKGWFYGFKLHLLVNLSGEIVSYVITPANVHDRK
VLEDLLLTKPLPGKLFGDKGYISKELQEKLKEQGITLITPLRKNMKEKLEKPNDKLLLRKRKRIETVFSQ
LKNQFGIEHSRARSLWGFLTRLLGKLLAYNLVQ
>gnl|CDD|468057 NF033521, lasso_leader_L3, lasso RiPP family leader peptide
YEAPTLVEVGDFRELTLGSS
>gnl|CDD|468058 NF033522, lasso_benenodin, benenodin family lasso peptide. This family consists of both the leader (removed) and core (mature) portions of precursor peptides from the benenodin family of lasso peptides
MERIEEHEDDLIDLGAASVETQGGLLDGDEDGGGRQPTGISDD
>gnl|CDD|468059 NF033523, lasso_peptidase, Atxe2 family lasso peptide isopeptidase
VTARDLVELRDIGGPDDSDPPSPFALSPDGRRVAFQVRRADPETNSYCLGLVVVPLDGGAPPRRVDDGGE
LIRATFLRGGAGFPTGLPAPITPRWSPDGRWIAYLKRVDGRTQVWRARADGSGARQVTHSPADVEDFAWS
ADGRSLIYSTRPGRAEAEAAIDREGLSGFLYDDRFDPLAGQRPLPRGPIPPGRLATDRLSGGWPATPLEA
DAPDRWRAIDLATGPVGALAAARAPAGAAAAWAPPDPDGVLSPLRLVAADAGGRRIRCAAPACCGDRITG
LWWRPDGDELLFLRREGWAGSRTALYRWRPGTGAVRRLLRTDDLLIGCAPAGDALICARESATRPRRLVR
IDLRTGRTRLLFDPNPEFAALRLGRVERLRWRNAFGIESFGDLVLPPGYRPGERLPLVVVQYRSRGFLRG
GTGDEYPIQPLAARGFAVLSFNRPPFVGSAQPAATSAEAARANQDDWADRRSVLSALEAGIDLLIARGIV
DPARIGITGLSDGASTVQFALINSDLFAAASVSSCCEDPSSYLLNAGPGRARSRYLRGGYPLGAPDDPAF
WRPLSLALNADRIDAPILMQLADQEYLLALETYTALRRAGKPVELYVFPDEYHIKWQPAHRLAVYERNLD
WFRFWLQ
>gnl|CDD|411161 NF033524, lasso_PadeA_fam, paeninodin family lasso peptide. Members of this family are lasso peptides in the paeninodin family, mostly from the genera Bacillus, Paenibacillus, and Thermobacillus. The HMM covers the leader peptide region but only about half of the core peptide region, since it is quite diverse
KKEWQKPELEVLDVNMTMAGPGGKIPDAVQ
>gnl|CDD|468060 NF033525, lasso_albusnod, albusnodin family lasso peptide. Members of this family are lasso peptides in the family of albusnodin, and appear limited so far to the Actinobacteria. Members are more strongly conserved in the core peptide region than in the leader peptide region, which is unusual for ribosomally produced, post-translationally modified natural products. The founding member of this family is not only circularized by the formation of an isopeptide bond, but also acetylated
DLLSTEATDEPVLLVDLGDAAALTLGQGGGSSEDKRRAYN
>gnl|CDD|468061 NF033527, transpos_Tn3, Tn3 family transposase
LSEADLRRYFTLSDDDLALINSRRRDHNRLGFALQLGYLRYPGRFLGPGEEIPPGVLRFVAEQLGIGPDL
LAEYATRGRTRYEHRAEIRELLGYRLFDESDRRDLLRWLLEQAAWTDKPRQLADAAIEWLRRRKIIIPGY
TTLERLIAEALSAAERRLAAALASALSPEQRQALDALLTSDRGDRLSRLAWLRQGPGRPSGREMLEELER
LEPLRSLGLPLGILLGVPDKRLRHLAREGASYTPQDLRRLKPPRRYATLVAFLTEREATLTDDLIDMFDR
LIGKLFRRAKRKAQKEVQASRKKLADKVRLLARLGKALLDAKEDGEDPFAAVRQVALWDRLAELVAEVCK
LARPSREDFLAQMLESYGTLRRFLPPLLAALEFEAAPAAQPLLAALALLRELYASGRRKLPADAPTGFLR
KRWRRLVLTPDGGIDRRAYELCVLFELRDRLRSGDVWVEGSRRYRDLEDYLIPPEEFQADRLAYYLPLAL
PADAETFLQELLARLDARLAAVARRLPEGDLENRIITDKRLHITPLWALDEPPSADRLRDQIYARLPPVD
ITDLLLEVDAWTGFSRCFTHLSPREPRAKDELLSLLAALLADGTNLGLTRMARACPGVTYDQLSWVQAWY
IRDETLRAANARIVNAQAALPLAAHWGDGTTASSDGQKFETGRRTEKAGYVNKYFGSGPGVTAYTHVSDQ
YAPFHSQVIPANEREAAYVLDGLLRHESDLKIDEHYTDTHGYSDHVFALAHLLGFRFAPRIRDLGDRRLY
LPDGDADYGELNPLLGGRIDLKLIEAHWDDILRLAASLKLGTVTASLLLRKLGSYPRQNPLAQALRELGR
IERTLFLLDYIDDEELRRRVQAGLNRGEARNALARAIFFGRLGEIRDRRFEEQELRASALNLVANAIVLW
NTLYLQRALTHLRARGQTIPDELLRRLSPLGWEHINLTGDYLFT
>gnl|CDD|411164 NF033528, lasso_cyano, lasso peptide. Members of this family are lasso peptide precursors of a type common in the Cyanobacteria and so far restricted to them. Some members have a pair of Cys residues in the core peptide region, C-terminal the region modeled in the HMM, and therefore would form bicyclic compounds
MKKTYSTPKLTVHGDVAEITQILGSSSRTDFLFFT
>gnl|CDD|468062 NF033529, transpos_ISLre2, ISLre2 family transposase
GDVTFKRRYYRDKETGKYVYLLDEALGLEKRKRVSPLVKEKIVELATEMSYRKAAEELNLLTGPVISHQT
VRNLVKEAGEELLKREEALREEVFEKKKVPVLFIEADGDHIKLQRGKKVEVKLAVVHEGWEEVGKRNELK
NPHYFAGLSEDEEFWEEVSDYLEEHYDLSKITLIIINGDGAGWIKKGLEYFPGAEYVLDRFHLNRKIKEA
LGRDPELQRKIRKALRKGDLDELEAILDTAESQLIDEKRRKRIRRLRRYLLRNWDGIRDYREERDEKGVS
AEGAESVSHVYAYRMKSRGRSWSEKGAEAMARLLAAKANGELLREQWLKRDFEGEETVSLPKKIIKAARQ
RLKRREPEVGLQGNIPALNGKSSPLGRA
>gnl|CDD|468063 NF033530, lasso_PqqD_Strm, lasso peptide biosynthesis PqqD family chaperone. Members of this family are homologs of PqqD, a chaperone that binds RiPP peptide precursors for their modification into bioactive natural products. By context, this set is involved in the biosynthesis of threaded-lasso peptides. This model focuses on lasso peptide systems from Actinobacteria. Similar systems, with different subfamilies of PqqD-related peptides, occur in lasso peptide systems in other lineages. A characterized example is LarB1 from the lariatin system of Rhodococcus jostii
RPHVSTTETEYGTVLLDERTGRYWQLNPTGALVLRTLLDGGTPDQAAAALTARYDVDAARARADVRALVA
SLRAAGLV
>gnl|CDD|468064 NF033532, lone7para_assoc, type VII secretion system-associated protein. Members of this family occur almost exclusively in the genus Streptomyces, in the context of type VII secretion systems (T7SS). Several paralogs may accompany a single T7SS. A few members of this family are large proteins with additional domains that add or remove, ADP-ribosylations, suggesting that all family members may have effector activity as well, and that the longer members of the family are multifunctional effector proteins
DHWLYLVDPAWDPDGPPPPWAVVGAWRSDADGEIGEFRPNPEYRPSPEALGWPEPTDPVDAALQLAATGY
GPAEDLAAALADAEVAVAVTPDGRPLIAASPDGTPVVPVYTSPAHLPRDGAPHHRRVPLRELVELLPDGH
DLLLNPGGPASARVPADFLREA
>gnl|CDD|468065 NF033533, lone7_assoc_B, type VII secretion system-associated protein. Members of this family are found almost entirely in the genus Streptomyces, and are associated with a type VII secretion system (T7SS)
DLTHLDKAALQNFIDNDVADFLTDLKKIREDGDPGGIPALKSLVDGDSLGDLSGQPQPLAIGPMAGDDST
GGKTLVEAVKTAATAIDKILKDQVTLFKDIEDALEETIETLLKTQGDNLDAIDAQKFLDIFEDVD
>gnl|CDD|411169 NF033534, rhodolasso, lasso peptide. Members of this family are lasso peptides as found in the genus Rhodothermus. The leader peptide region shows sequence relatedness to several other groups of lasso peptide precursors. Known members of this family have a pair of Cys residues in the core peptide region, suggesting a bicyclic product, with one cross-link from the signature lasso peptide isopeptide bond and the other from the cysteine disulfide bond. This subfamily of lasso peptide appears not to have been discussed in the literature yet
KAKRTWSAPTLVIHGKVEEVTHQRGPCWLGKQGGKYDADLGPGSLSDCR
>gnl|CDD|468066 NF033535, lass_lactam_cya, lasso peptide isopeptide bond-forming cyclase. Members of this family are the isopeptide bond-forming cyclase of lasso peptide biosynthesis systems, from a subgroup that contains primarily cyanobacterial examples. These proteins resemble the glutamine-hydrolyzing asparagine synthase AsnB (EC 6.3.5.4)
MSGIVGIYYLDGRPVDREDLQQMVDILAHRGPDGADIWCEGSVGLGHRMLWTTPESLLEKLPLVNQTGDL
VITADARIDNRDELISALQLNNCPPEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARD
HFGVKPFYYYQSDKRFAFASEIKALLCLPEVPRRLNEVRIADYLALMLEDKVITFYQDIFRLPPAHSMTV
SQSGLQIRSYWSLDPSRELRLDSDEEYAEAFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCVARQLL
AEEKKAPLHTFSNIFDKVTECDERPFINAVLEQGGLIPHYVHADQFGPLSDLEQIFEYEDEPFLGPNHFL
PWGLNRAAQKEGVRILLDGFDGDSTVSHGHGYLTELANQGKWLTFAQEIRALSKNYGTSPWGLLRQYGLP
YLEKLARQFKWLTFLKPANQIHKHFGISRRQLFLQHGIKPLVPRALLKLWRKLRGQAQPGNSWRPIINPD
FAERIGLKERIQRLDPPPSSSPLTVREEHWQSLTSGILPFVLEVLDKYAAAFSLEARHPFMDKRLVEFCL
ALPPEQKLRQGWSRMVMRRAMEGILPPQVQWRGGKADMSANFVHGLLNFNRQLLDQVMSNDLESIEPYVN
LEFLRQAYQRLISKEEQASDLDVMAVWQAVILTLWLQQ
>gnl|CDD|468067 NF033536, lasso_PqqD_Bac, lasso peptide biosynthesis PqqD family chaperone. Members of this family are homologs of PqqD, a chaperone that binds RiPP peptide precursors for their modification into bioactive natural products. By context, this set is involved in the biosynthesis of threaded-lasso peptides. This model focuses on lasso peptide systems from Firmicutes. Similar systems, with different subfamilies of PqqD-related peptides, occur in lasso peptide systems in other lineages
SLNDIVVQSEGNIVSDMDGEKVMLSIENGKYYNLGEIGGEIWELIKEPITIEELVTTLLSEYEVEREECE
EQVLSFLEQLLEEGLIEV
>gnl|CDD|468068 NF033537, lasso_biosyn_B2, lasso peptide biosynthesis B2 protein
LRLLLLEAALLLVAARLALALLPFRRLRRVLGLLRRGAALTRPASAEEALIRRARRAVRAASRYCPGRSK
CLPRSLAAALLLRRRGIWPTLCIGVRKDGPFAAHAWVEADGGVLVGEPEPTDRFTPILTV
>gnl|CDD|468069 NF033538, transpos_IS91, IS91 family transposase
LKDIFEANQHWDAFLAQHGGRLRPVQLEAVTKMLACRTSALGGHHYRCDNCGHVKYVYNSCKSRHCPSCG
AKATEQWIAKQQAELLPCPYRHVVFTLPDELWPLARHNRAWLLGALFRSAADTLLTFAKNRRHLLEIGAF
AVLHTWGRRLNWHPHLHLLVTAGGLDEDGRWKKCKGGILFPAKALSKVWRAKFLTLLRQAYDAGELFPAE
LAHIKLPSAWNKFLLGLYPRGWVVHAKKKTGNGRQVLEYLGRYLKRPAISNSRLRHYDGGEVTFRYKDHR
TKGTKTLTLSPDEFIRRFLQHVPPKGFRRIRYYGFLANRSRGRALPTVYAALPEPPPKKAAPLVFAQMLK
RLLKVDPPECPLCGGRMVFIAFIRGP
>gnl|CDD|468070 NF033539, transpos_IS1380, IS1380 family transposase. Proteins of this family are DDE type transposases, which are encoded by IS1380 family elements. It was first identified and characterized in an Acetobacter pasteurianus mutant with ethanol oxidation deficiency caused by disruption of the cytochrome c gene by the IS1380 element
KAEFDGGNLTSDAGLLLLGELLDKLGLSKRLDAALGDPRDPNAGHSLSDILRQLIGGLAAGYEDLNDIDA
LRHDPAFKLALGRKPVASQPTLSRLLRRLTEGAIALNALDALNRRLLKLLLASAPLLAPKEVVLDIDATV
IDVHGHQEGGAFNTYKGEDGYHPLVAFLGGTGELLGAELRPGNVHSAKGAVEFLKRALARLRRAWPRTRI
LVRGDSGFASPELMDWCEERGVDYVIGLNLNSALRKAIDLIDKRAWRPVGRKPDADPDAWYAEFSYKAKS
WSKPRRVVVRRERRHPGGQQLLFDEIRFIVTNLPTDTPPEDVVELYRARGTSENRIKELKNGLGLDRLPS
GKFAANQLRLLLAALAYNLLRWLRQLALPGTELARARIKTIRLKLIKVAARLVRHARRIVLKLPSSC
>gnl|CDD|468071 NF033540, transpos_IS701, IS701 family transposase. Members of this family are transposases in the family of that of insertion element IS701, narrowly defined. Note that a molecular phylogenetic tree of the broader sets of transposases from IS elements classified as IS701 family or IS4 family by ISFINDER shows the two groups interleaved. This model represents an unambiguous clade that includes IS701 itself and the majority of proteins called IS701 family. The poorly conserved C-terminal region of members of this family is not included in the seed alignment
FGSKRQRAHARAYLTGLLSPGERKSVWPIAEAAGPPNPQSLQHFLTRAPWDADALRDRVLDYVLEHLGTR
RDGVLIIDDTGFPKKGKHSVGVARQYSGTLGKIDNCQVGVTLAYASDGGSLPLDFRLYLPESWTDDPDRC
KAAGVPDEVGFAKTKPELALEMIDRALAAGVPFGWVLADAGYGSDTAFREALEERGLGYVLAIKSNRKVW
PPGGRPLGSVKELAQSIPAKAWQRVTVGDGTKGPRLYDWAAVRVRDARGLPEEWLLIRWPKTDPGELKYY
LSTLPAGSTTLAELVRVYGERWRIETFFRQAKQELGLDHYEVRSWRGIHRHWTLVMLAYAFLTLL
>gnl|CDD|468072 NF033541, transpos_ISH3, ISH3 family transposase. This family contains transposases from the insertion element ISH3, and related transposases from other mobile elements with similar transposases. This model reproduces the classification from ISFinder except for ISC1439B-like transposases, since those are extremely different
PEEILEVLLGASTDGTSIESLSNDYEDSPCADTVRNYLHTLNREQLEKVLNSLLRKMSLEILDPDRSRDV
AIDFHDNPYYGDEDDTGGLRRIKAKKGTSWGHAYATLYVIGNGKRFTLAVTPVVNGETKSDVVERVLERV
DKYGLKIDLVYLDRGFYNSEVIRFLRELKYAFVIPVVKKGERIKQELKTYESRMTDYDTTFKKERETEQV
TFPLAVDVSYQNGDRGKHGKIVAGYAAAGPIDRTPRQVAELYRKRWGIETSYRLIRQFRARTSTRDPVVR
LLFFVVSFLLYNVWRVLR
>gnl|CDD|468073 NF033542, transpos_IS110, IS110 family transposase. Proteins of this family are DEDD (Asp, Glu, Asp, Asp) type transposases, which are encoded by the IS110 family elements
FVGIDVAKEVFDVAVVDASGGEVLRKKFKNTKAGREALLAWLAKLAPPCVVVMEATGGYHAWLRELLALG
GFPVVLVNPRHVKPFRKGARAKTDRIDAEAIAEAARRGRMRFVPVKTEEQQALRALHRRREQLVKERTAL
KNRLRGLLAEFGIALPKAGLAALRRQLRAILEDLDNELPPLARELLRRLLERLLALEEQIKEIEKEIEAL
AREHPDAACQRLMSIPGIGPITAAALLAEVGDIRRFKSARQFAAYAGLVPRQYSSGGKVRLGRISKRGNR
RLRRTLLVAAARAVRRRNPASRAFYDRLRAWGRRLAKRKGKKVAIVALARKLARILWALLRDGTP
>gnl|CDD|468074 NF033543, transpos_IS256, IS256 family transposase. Members of this family belong to the branch of the IS256-like family of transposases that includes the founding member. It excludes the IS1249 group
KETTAVDELLDEALLGLKALEDLTDDELLRELLKALLEQLLEAELTAHLGAEKYERTGRGNVRNGYYPRT
VLTRGGPVELRVPRDRDGSFEPQLILKRYRRSEKALEAVIIELYLKGVSTRDIQEALEELYGIDVSSKSV
SRLTDAVDEEVEAWQNRPLEERYPYVFLDATYLKVRDGGRVVNKAVLVALGVDADGKKEVLGLWIGPSES
AAFWLEVLRDLKNRGLKGVLLVVSDGLKGLPEAIREVFPGATWQRCIVHKIRNVLAKVPKKDRKEVAAAL
KAIYQAPDAEEAEAALDAFAEELWKKYPKAAASLEEAWEDLLAFFDFPPEHRRSIYTTNAIESLNAEIRR
RTKVVGIFPNDESALRLLYALLLEAEKKWRRRRGYKQLLSLLAILKFKDGRLETAL
>gnl|CDD|468075 NF033544, transpos_IS1249, IS1249 family transposase. Members of this family belong to the IS1249 group branch of the broader IS256 family of transposases. This group differs sharply from the main branch, which includes founding member IS256 itself, by having an N-terminal region with two pairs of closely spaced Cys residues
RPRCPVCGGKMKKNGTTSAGTQRWRCKACGASFTKKRRDDTRAADLKAFLDWLTSKQSQAAMRAGGSGRT
LRRRTAWFWNIWPPPPKVGEVYDVVFVDGTYLARGWCLLIACTETHVIGWYWCRRENTRAYQALLSRIAA
PLVVVTDGGRGARKAIKKVWPNTRIQRCLVHAQRNVRRYTTSRPRTDAGKELYRLALKLTRITTLDQAAE
WVAALNAWHTTWKDFLNEKTYADEDGATRANWVWTHERLRKAYNSLNRLIREGTLFTYLDPPLTLLDPGP
VPSTTNRLEGGINAQLKDLLRNHRGLSLERRRKAVEWWCYMHTELPLDPAEILRQMPTDQDILALYRALT
ERSENQADHETGRPALYGTAIDWNEFHNSGI
>gnl|CDD|468076 NF033545, transpos_IS630, IS630 family transposase
RRARILLLAAEGLSITEIAERLGVSRSTVYRWLKRFNEGGLEGLLDKPRPGRPRKLLSEQQAELLALLLE
EPPEGAGHWTLRELAALLEEEFGVEYSRSTVRRLLKRLGLSPKKPRPRAPKQDPEFVEKFKEVLGLYRAP
PDPAEVVFIDESGIQLLDTRGRGWAPKGQRRPRVHVYGRRGTLNLFGALDPLTGKVFVLFTGRINSEDFI
EFLEELLAAYPGKKIHLILDNASTHKSKKVREWLEEHGRIELHYLPPYSPWLNPIERVWAVLKRRLLRNR
AFRSVDELREAIDAFLNR
>gnl|CDD|468077 NF033546, transpos_IS21, IS21 family transposase
IRLLFRQGLSIREIARELGISRNTVRKYLRRAGLDEPPKYERRPPRPSKLDPFEPYIPDWLEAHLRKPGV
TATLLWEELRAEGYPGSYSTVRRYVRRWRAEQGPAKVFVRLEHAPGEQAQVDFGEATVVVTGGTGKILHV
FVAVLGYSRYTYVEATPSESQEDLLDGHQRAFEFFGGVPREIVYDNLKTAVDKRDRYEEPRLNPRFAAFA
AHYGFEPRPCRPYRPQEKGKVERAVGYVRRWFLRLRGRRFESLAELNAALAEWLAELANQRPHGTTGGSP
AERFEEERPALQPLPA
>gnl|CDD|468078 NF033547, transpos_IS1595, IS1595 family transposase. Most transposases of this family of transposases, IS1595, have an additional short N-terminal domain with a pair of CxxC motifs
ASKLPLRKWFKAIYLMTQGKKGLSARQLARQLGVVSYKTAWRWRHKIREAMGERDDAYKLGGIVEVDETY
FGKGQRKGRRRGGKRGRGSKGKVPVVVAVERNGKGRVYVVVVGDASAATLEPIIKGHISPDSILCTDGWR
SYRGLAKDGGVHHRRVNHSKGEYVKGGGYHINWVNSFISNLKRWLRGTFHGVSTKYLQNYLDEFEFRFNR
R
>gnl|CDD|468079 NF033550, transpos_ISL3, ISL3 family transposase
VVEAELTRGDATCPECGKPSRRVHDTGKRRIRHLPIFGRPVYLELRVRRFKCPECGKTFTEELPWARKRS
RITLRLEAAVLALLLELMSVAAVARQLGVSWSTVWRILLRAVRRLLAKRDPRLPRVLGVDEFALRKGHKY
VTVIVDLETGRVLDILPGRSKATLKAWLRRLPDKGRDQVKVVAMDMSAAYKSAARELLPNAKIVADRFHV
VKLANEALDKVRRREQKELRKRRRERKTLKRYRWLLLKNPENLTEKQRERLEALLEASPELAKAYELKEL
LRDIWREKDPDEARELLEAWIASAKPSGLPELKKLARTLKKHLAGILAAFEHPLSNGPTEGINNKIKLIK
RRAYGFRNFENFRARILLA
>gnl|CDD|468080 NF033551, transpos_IS1182, IS1182 family transposase. Members of this family are transposases of the IS1182 family. About two-thirds of the members of this family have an extra domain between the middle and the C-terminal domain, about 50 amino acids in size and containing four invariant Cys residues
PPDRNQLELFPVSLDDLVPEDHLLRFIDAVVDFLDLSELFADLYCSDNGRPAYHPALMLKLLLYGYLEGI
RSDRQLERELRENLAYRWLLGLGLTDPVPDHSTLSRFRRRLKDTDLLERLFDQVVELAREAGLVGGKRVA
IDGTHIKANANKKKERIAAAKKRLDELELAKEELEASAEAAKQRAEKALLAGKDRRVSTTDPDARFMKKS
NGGFWFGYNVQIAVDTESGLIVAVEVTPGNGHDGGQLIPLLEQVEERLGLLPEEVLADAGYGSEENLEAL
EERGIEPVIPYRRKGAFKPGRFRKDDFRYDEEDDTYICPAGQRLTFKTTSREGYREYRFDPEDCRGCPLR
EQCTKSKEGRVVTRHIHEDLLEEARARLKTEEGKELYRKRKATVERVFAELKQWHGLRRFRLRGLEKVRA
ELLLTALAHNLKRLAAL
>gnl|CDD|468081 NF033553, MerP_Gpos, mercury resistance system substrate-binding protein MerP. Members of this family are MerP, a substrate-binding protein for a system in which toxic Hg(II) is transported into the cytosol, where it can be reduced to the much less toxic form Hg(0). Members of this family are found, so far, in Gram-positive bacteria. A related MerP family, as found in plasmid-borne systems in Gram-negative bacteria, is described by TIGR02052
MKVQIIRIMMLLSLLLVVSACSNEKEAQNTIDAKKEVKTTVEANKTGTFTVLGMDCCPPSVVEDVISQVE
GVGKTDIKVSGSTGKVTVSFDDKKTDLKAIKTAVSDFGLGVE
>gnl|CDD|468082 NF033554, floc_PepA, flocculation-associated PEP-CTERM protein PepA. PepA was described in Zoogloea resiniphila as a PEP-CTERM protein regulated by the PrsK/PrsR two-component system. Knocking out that system blocks flocculation, after which expression of recombinant PepA can restore flocculation
KLLALLAAALLLAAASAAAAALPDFTVDPDGVGGTGAVFTADKIDGGSSERLTFTGGSGGTFTATGYATF
GSFVLNSGGTSTGTSGLNLDGYELYAVFTFTGTCSSGGAGGTTFTFTSGSFTLYLDPNPDTTFTTGTGAT
DGVAILTGDDILLGSGSLNGGTGTLDAGGAGGGFLGGANVFNNFTLTAAGSAYFTSPDPFYLIAFVDGNN
TSFGLDAGGTAIVQGDGSADFTAVPEPATLALLGLGLLGLGARRRRRS
>gnl|CDD|468083 NF033556, MerTP_fusion, mercuric transport protein MerTP. MerTP is a transport protein for the mercuric ion, Hg(II). Once imported to the cytosol, the highly toxic ion can be converted by MerA, mercury(II) reductase, to the less toxic Hg atom
AGLLTAIAASLCCITPVLALLAGTSGIASTFSWLEPFRPYLIGLTVLVLGFAWYQKLKPTKKEIDCACET
DEKPSFWQSKKFLGIVTVFAILMLAFPYYSHIFYPKTEKEVIVVNQSNIQTVEFKIKGMTCAGCEEHVNH
EVNKLPGIVSVKTSYEKGNAIVKFDKSKTSIEEIEKAINSTGYKVT
>gnl|CDD|468084 NF033557, LLB_putidacin, putidacin L1 family lectin-like bacteriocin. Putidacin L1 is a well-described member of a family of lectin-like bacteriocins found almost exclusively in Pseudomonas. This subfamily is narrowly defined, and does not include the homolog pyocin L1
FTGNGSSVLPPRQTMSPGQYLQSPNGRFKLILQPDGNLVLYDGGAAVWVADANQPYSSTLPLRKKVPTSF
YVQYGAFLDDPLRGRTWLTNNSTPGGSSEDAWNRTHLQLQDDGNIVIVDSQALWNSNPSIPLTPGAPAAV
IIPPGTELEVGQRYVAGDTTLVFQGDGNLVVYGPNGSVVWASYTQNKGAVRAVMQADGNFVIYAANGVPL
WNTGTGGNPGAYARLQANGSFSIVKEKPVWARFGFTPTIKPRRVFYPDHTTGPWPTYDHVGWTF
>gnl|CDD|468085 NF033558, transpos_IS1, IS1 family transposase. Proteins of this family are DDE transposases encoded by the IS1 family elements usually through a translational frameshift mechanism
CPRCQSDNVVKNGKSVRGKQRYRCKDCGRQFQLDYEYRGYSEGTKEKILQLYLNGMGFRAIARVLGVSHN
TVLRWLKKLGPRQVTPEPLKPADIVLICELDELWTFVGNKKNKRWLWYAYDRKTKRILAYVFGDRSAETF
RKLWALLKPFKIGFYCTDHWKVYAEFLPDEKHLVSKGETQRIERENLTLRHRLARLVRK
>gnl|CDD|468086 NF033559, transpos_IS1634, IS1634 family transposase. Members of this protein family are DDE type transposases encoded by the IS1634 family elements, which were firstly identified and characterized in Mycoplasma mycoides
LGFLSRRLYLKFPEFFRTLVIERLLGPTSKLGVTVALPGIEAEHLNDDRLGRTLDALYAAGPTALFTELA
LALRELFGLDLQVLHYDTTSISVEGEYESEDEIRQITFGYSKDHRPDLKQFVLGLVVDQEGIPLFHEVFD
GNTADKKTLVPTLKRFLEQLPLDRVVLVADSGLYSEDNLEALQSQPLSFISRVPATIKEAKELLLSDLHE
EECDSAGYKIYEGESTYGGVKQRWVLVHSEERAKEEAKTLEKRIEKELAKADKALKKLSAQDFACEADAR
AALERWAKELPLHELSEAELEKKGYAKIGRPKKGEDLFEYYRISAELVLDQEAVARAKARDGRFILATND
TDLDPEEVLAYYKSQQKVERGFRFLKSDLFEISPVFLKKPERIEAHLMIMFLALLVYRVLRQRLKETGTG
LSNQPTLRWIFEQFRGIRELELEIGGKIISGISNLTDEQREIL
>gnl|CDD|468087 NF033561, macrolact_Ik_Al, albusnodin/ikarugamycin family macrolactam cyclase. Members of this family show homology enzymes known to form the lactam bond of the isopeptide linkage of lasso peptides. This family includes the peptide cyclase involved in biosynthesis of the lasso peptide albusnodin. However, another member of this family belongs to the biosynthesis cassette for ikarugamycin, a macrolactam whose biosynthesis relies on a hybrid PKS/NRPS system, not a ribosomally produced peptide
WFGGFSGGAPPPPRPLGAAPVPPGARVLWWVGGWPPRELRRTRGGRRRVAVLGPCGATDAELARLAAADL
PDDVAWRWPGSYTVVEETGDGVVVWTDPAGACPVYTTRTDGGWVWSSSARALAGLTGAPVDAWRLAAALL
APSVPALAAGRSAFAGVEQVPPGHRLTLPADGGAPRTPWWWRPDPRPGPDAVARLRAALAAAVALRVDGA
PPLSSDLSGGLDSTTLALLAARCLPVGRRLTGVTVHPEGRTEGGDLDYARLAARAPRIRHRLLPLGAEHP
PYTALTAVPATDEPAPSTVTWARFSAQLRWMREELGTRCHLTGDGGDSLLFPPPAHLADLARHGRWRRAV
REALGWARLRRTSPWPLLRAAVRRARTSRPLLPVPPWATAAARWLAAAAAERAAALPGLDAAVRALVDEI
REVARTARADAQLAAALGVELHNPFLDSRVVDAVLSVPLDDRPSPHRYKPLLADAMADLLPAALAARTTK
GSFTADHHQGLRANLPALLDLADGHLAALGLIDPARLRRALRRAAAGVPMPLATLEPALAAEAWLRAHHR
A
>gnl|CDD|411192 NF033562, BH0509_fam, BH0509 family protein. This family of unknown function appears restricted to the Firmicutes. Proteomics evidence for expression was provided for the member from Bacillus cereus by Dr. Samuel Payne, Pacific Northwest National Labs. The family is named, for now, after BH0509 from Bacillus halodurans
MSRQERKNMIEFISLVRGFERESLMYMTDEEIEHIYNLTYKQH
>gnl|CDD|468088 NF033563, transpos_IS30, IS30 family transposase
STISREIKRNSGLQGYKADQAQRVYEKRRKRCGRKLKLSPELIEYIEHLLRLGWSPEQIAGRLKREEKEV
SVSHETIYRYIYAGKLGGGKLYRHLRRGGKRRRPRGGKDRRGKIPDGRSIEERPEEVEDRSRFGHWEGDT
ILGKKHKSALLTLVERKSRFVILVKLPDKTAESVNKALIKLLKPLPKHLRKSITADNGKEFARHSEIEEA
LGIDVYFADPYSPWQRGTNENTNGLLRQYLPKGTDLSEVSQEELDRIENWLNNRPRK
>gnl|CDD|411194 NF033564, transpos_ISAs1, ISAs1 family transposase
ILFLALCAVLSGAEGWEEIEDFGEAKLDWLRRFLPLPNGIPSHDTFARVFSRIDPEAFQACFLAWVNSLR
ELTGGEVIAIDGKTLRGSYDRGKGQSALHMVSAFATENGLVLGQVKVDEKSNEITAIPELLELLDLKGCL
VTIDAMGCQKEIAQKIVEKGADYLLAVKGNQPKLYEAVEAYFTDARDNDLQGIPHDSHETTEKGHGRIET
RRYWVLPAVDWLDLEEKWPGLKSIIMVESERTVKGKTSTETRYYISSLPLDAERFAKAVRGHWGIENSLH
WVLDVVFREDASRIRKGNAAENLALLRHIALNLL
>gnl|CDD|411195 NF033566, adhes_LIC20035, LIC20035 family adhesin. LIC20035 of Leptospira interrogans was characterized as a surface exposed adhesin that binds host extracellular matrix components. Orthologs appear restricted to the genus Leptospira. Member proteins average about 430 residues in length, much of which consists of repeats. All members are predicted lipoproteins
MKKILSLALITSLLIGCSSTSIVENKGKDQEFQILEPNIRVEKFKETFNLKAEGPVKLDCSGKPCTPDQV
SALTPDQIKKLKRNGAWKEYVEKEDAQKKKFSVLVRVGEYKDDKREGIWKTLYETGETLRETPYVAGLKE
GEEKKLAKDGTQTESTTYKADKKNGPYWSKNDKGELSEEGSYKDDKKDGTWKEYYDEDGAKKKVSEYKNG
LKSGQEINYHKDGSTVSSEGNYTDDLKTGYWKNYYDNGSIQAEGTYAPKGTGAEKKSLRTGAWKEYYKNG
KVFAEGQRDHTRKGEWKFYWSNGNPAYKGAMMNEFMMSSAEVYDKEGQIIGKGKLFFSLLLIDEKTDELK
AKYKPDIPFTYYKNGKKSFEIRSEEKAIEYDESGSKIGEGPIMPGTNAKNGCWTTPQGKKYYINGKENPK
MGEMQGCK
>gnl|CDD|468089 NF033567, act_recrut_TARP, type III secretion system actin-recruiting effector Tarp. The founding member of the Tarp (translocated actin-recruiting phosphoprotein) is CT456 from Chlamydia trachomatis. Tarp is a type III secretion system effector. Orthologs are found other Chlamydia, but are highly variable in length because many lack much of the repeat region
MTNPINNPSTTNVTTTTSTTPVVTTSGSLGGHSVSTTGTGAVEQTAQTVNTAADQAVQQAESDEGAVNFT
TERSVSTTTPSTGSSGTTATAASLKGSQILGGGRTRPDSTSSSDSSSTSSSSHTSSDYDSGDTSNNENAS
SDADLGDLNSLRGSERAEGAEGPEGPGGLPSMALPKYDPTNKASILTFLSNPSVQAKMQTKAGHFVFMDE
ARSSFIFVRNGDWSTAESIKVTNGKTKEPITDIKDLEMCIAKFCVGYETMHADWTNNVQPRVAGQTGETG
NYNHLLMSMKFKTTVLYGPWNSKESSSGYTPSAWRRGTKVDSGPIWGDVGGLKGINWNTQAGPDDGTSFS
NETPGAGTAAQPQPTPYSIPVINVNLGGISVNVGVTNVGGTTTTTTTQSTDASTDTSDDDISTDDQTDDT
NTDDVDTDSAGTQEEDTISFTDSGSGEDSLAPSSSESPKPPGPPPPQGSVNITGMPNASLKQILQNVRQH
LDTVYDQNGGSHEGPIQANQNLGDVIQDVETKPTQPEGVFSAWKVDTDSTGSAGGGGSRTGTGSRTTSLM
MATGGGGRGTLEHLLPRIRAHLDISFDAQGNLVTPQEPNVGSIVKAFRERTGSGGIVAPVPQQATVITSS
PRTQQSATTSILPQAQTAETTSAPGKPDLAQAATGVGGSLSNLLQAATAATVTSPAPSQQTATSTPVAGT
RQTAVTQALGNVAGKVNLFEQGQRLSEALNSAGTGSQQGRQLFQAAAQTTQVLSKLIDTAT
>gnl|CDD|411197 NF033570, FIB_Spiroplas, cytoskeletal motor fibril protein Fib. Fib, a 59K protein also called fibrillin, is the repeating subunit of the linear fibril that runs through the shortest path along the length of Spiroplasma cells, members of the Mollicutes that lack cells walls but have a spiral shape. The fibril is a linear contractile ribbon, and Fib is its only component
MIGIISTAYFTVKDRPGIKTVKKYWWRNMVIQHVKYRGKFFIIATIGYGKANAAMAITYLMEEYPGLETV
LNVDLALSTNDKFDTTDTVMSTKFIYRDADLTVFKDIKYGQIVHEPEAFSFNTEFASQVKNFKLGVSDGI
VGTADMLIYNSKQFKEMVDKYGQTIDVIDTEAGAIAQVAKKSSVNFIAMKIMYNNALSPWDNDPLHKFKI
YETTNTLKYLLARLFNLLSSNYIIDFTKNSNDELEIINELFELEHDAWVKRFKKNTVSLLSGLGPSLMLV
DKKGKTPEALDIVEVMKSKIEDEGPSKVILGEDEWKNAPKKWLRKLMFLENIHVNDDELLWNKSAKYDLK
NEKIYSIEDVAKAISKAIADRSQDKSSYTYDGATVPKKHLLVAVDAAISFYITHNQTHEFVESPKHGSQL
VANEFVKFLNEQLAEVESPFEKIIIYIKIPAIGASKLPVFITTKSKANQPIVFSGYSQKDQKTYTVVDIT
RNDYDPLKVGSFKVTIRLKNE
>gnl|CDD|468090 NF033571, motil_scm1_spiro, motility-associated protein Scm1. Scm1 (Spiroplasma citri motility gene 1) was shown by loss-of-function mutation to be involved in motility. The Scm1 family is widespread in the genus Spiroplasma, members of the Mollicutes (bacteria with no cell wall) that have a spiral shape organized around a contractile ribbon fibril made of repeating subunits of the Fib (fibril) protein
KHKSWLKFSIIFAILFITILIVTLVLPSLIDVVKELKNIIINSLESGITENLPLLNLNINNPFSLAYFLF
GYEGFSGIIALHSFNLFKFTLFWVFILPILFIIFGFFLSIFIILLLIERIRREYKYNTIKKVGKWGMYIS
FISFYLFALIGLILFSILENSLKKNDQLKAWYNTFNYDNSFSYITGLKYLPNGTLFSILGNGINQILGND
FFNFNTGLLQASLVFLVILLPIALIILIIFLSIWIATFISNRSSSHSKFSNWLGNIRIDSKREFRSLLLK
NIWFWILVIGFIVTIIFPGFVHPYKNTTQIIITVISIVIIPLVFIPLIIGWIRIVKIRRFNYNLLMFIQI
LILLIIGLIWQLNIWILFKEEFQYPAWVSIIIPFITITISLISFFGFIKGK
>gnl|CDD|468091 NF033572, transpos_ISKra4, ISKra4 family transposase
PEGELELVEELKLIAAILYDEAEDEGLSLEEGKELLRTLQQQLLQAQAPYDAQIRCCFDCGRRRTSKGGR
TRKIKTLFGEVTVTRPRYYCCRCGGAGPQDSPLGLLPGDRLSPELEKLCALLGALVSFREAAELLEELTG
VKVSKTTRQRLVQRAARLEPAFEEVCPPDWPELPPPEPVLVVSLDGGKYRLRTPEKGERKRMRDFEVVYG
KSPAIRRPDRRFASVQGSAAEFGRRLFLEAWRRGQQLAQPVTVLGDGADGIWNLLFELFPGPVQAEEILD
WFHLAEYLWKVAQALKGLERAKWKLWHGKVLEALKLLKGLAVDLSELRELAPRELAAKKRKALDEFITYL
ENNRERIVNYGEYQAEGLPIGSGVVESAVKQIVKQRMKKSGMRWSLEGAHAVLQLRAAYLNGRL
>gnl|CDD|468092 NF033573, transpos_IS200, IS200/IS605 family transposase. Most IS200/IS605 family insertion sequences encode both this transposase, TnpA, about 130 amino acids long, and larger accessory protein, TnpB, that may act as a methyltransferase
YRSGSHTVYLLKYHLVWVPKYRRKVLTGEVEERLKEILREICEEKGVEILELEVDPDHVHLLVSYPPKLS
PSKLVNALKGKSSRRLFKEFPELKKKLWGGHFWSRGYFVSTVGGVSEEVIKQYIEN
>gnl|CDD|468093 NF033576, mCpol, mCpol domain. The mCpol domain (minimal CRISPR polymerase) is named for its homology relationship to catalytic domain of the CRISPR polymerases (often called Cmr2 or Cas10). It is predicted to generate cyclic nucleotides, potentially sensed by CARF domains which in turn activate various effector domain including HEPN RNases, CARF sensor and effectors are found in conserved genome contexts. It is part of a broader class of conflict systems reliant on the production of second messenger nucleotide or nucleotide derivatives. The putative function of the mCpol domain implies that CRISPR polymerases of the type III CRISPR/Cas systems have a nucleotide synthetase functional role
LYITIDGDDIGRKITSAYLSNDEAELRKISNLVQEATSKISKFLRSNGFAIIFCAADGVAAKTEDEIDMQ
FIFSQIESIADSELTFSAGVGSSLREAYVALLSAKSNGKNKICDFELI
>gnl|CDD|468094 NF033577, transpos_IS481, IS481 family transposase. null
GRLELVRLVLEDGWSVREAARRFGISRKTVYKWLKRYRAGGEEGLIDRSRRPHRSPRRTSPETEARILAL
RRELRLGPRRIAYELERQGPGVSRSTVHRILRRHGLSRLRALDRKTGKVKRYERAHPGELWHIDIKKLGR
IPDVGRLYLHTAIDDHSRFAYAELYPDETAETAADFLRRAFAEHGIPIRRVLTDNGSEFRSRAHGFELAL
AELGIEHRRTRPYHPQTNGKVERFHRTLKDEFAYARPYESLAELQAALDEWLHHYNHHRPHSALGGKTPA
ERF
>gnl|CDD|468095 NF033578, transpos_IS5_1, IS5 family transposase
QPDLFRSRLDDILNPRHPLVKLADLIPWEEFEEAYAPLFSSHTGRPAKPTRLMVGLLILKHRYDLSDEEV
VERWVENPYWQYFCGEEFFQHELPFDPSSLTRFRKRIGEEGLEELLAETIEAARKSGAIKPEDLGRVIVD
TTVQPKNIAYPTDARLLNKAREKLVKLAKKLGIKLRQSYNRVGPRLYRRIGRYAHAKQFKRARRALKKLR
TYLGRVLRDIRRKLESIAELLRERLAKLLEVAKRLYEQKTHSKNKIYSLHEPEVRCISKGKAHKPYEFGA
KVSVATTSKDGLVVGARSSPGNPYDGHTLAEALEQYEELTGQYPERALVDKGYRGRENRGLCKGIRISGP
KRGRTPKLKRWLKRDENRRSAIEPVIGHLKSDHRLGRNRLKGAEGDAVNAVLAAAGHNLRKLLRL
>gnl|CDD|468096 NF033579, transpos_IS5_2, IS5 family transposase
RNWSSYNVALAKRGSLTIWLDPDALAQWYAPPKGKRGRPQTYSDAAIQTLLLLKVLFGLPLRQTQGLLNS
LFKLIGLDLAVPDYSTLCRRFKRLKVAIPLSAKLLGGPLHLAIDSTGFKVYGEGEWYRRKHGKEKRRQWR
KVHLAVDVKTGEILAVEVTTNKVHDAKVLPDLLRQIPEDIDSVLADGAYDTKKCHEAIRERGARPLIPPR
KNARLWKEGKARNAAIREIRRLGRELWKKWSGYHRRSLVETAFSRLKRLLGERLRARNFDRQVREVKLKV
AVLNKFT
>gnl|CDD|468097 NF033580, transpos_IS5_3, IS5 family transposase
YRSDLTDEQWERIEPLLPPARRGGGRRRVDDREVLNAILYVLRTGCPWRDLPERFGPWSTVYRRFRRWSE
AGVWERLFEALLAELRIDWERLAIDSTIVRAHQSAAGAKKTGPNGYQAIGRSKGGLKTKIHIAVDALGLP
LAFVLTGANVHDSKGALPLLDGLPVLRPPRPKHLLADKGYDSDALRAALRERGAVPVIPRRRNRLRPAYD
FRLYKKRWVVERTFAWLKRFRRLATRYEKLARNFLAFVHLACIRIWL
>gnl|CDD|468098 NF033581, transpos_IS5_4, IS5 family transposase
RLFRRLSGVPWETFEALIEPLYPKRAGRGRPPYPPELMLRILLLQTLYYLRDERLEEQLYDYLSFRAFVG
LSEDDVPDASTIWRFRELLEEHLLAEALFAEVNRQLLAKGLLSKEGVIVDATLIPAPRSPKKRDKKRDPD
MRQTKKGKKSRHGYKAHIGVDPKSGLVHSLVTTPANVHDSRAAKELLHGDEKTVYADKGYDGDEGYQGLR
EAGVKPHIPRKKSRNRPLTEAQKRRNRLKSKIRARVEHVFGVLKRFFGLSKVRYRGLKRVGARFNLIAAL
YNLE
>gnl|CDD|411207 NF033583, staphy_B_SbnC, staphyloferrin B biosynthesis protein SbnC. SbnC, related to siderophore biosynthesis protein IucA and IucC, is encoded in Staphylococcus aureus in the sbnABCDEFGHI locus responsible for the biosynthesis of staphyloferrin B, a carboxylate-type siderophore. SbnC is found in many species of Staphylococcus
TANHQVNRAQTTILRDLVDALLFEDIFGLASKSEVLQIAQQTILRYENEDQVLLIPVYFSGLNVYRFAGS
AVVTIESKTEKHPLTAVELWQTLVEMNADLATEWNVARFREGLETAVQQLTAQLSGLDLSEHPFIQSEQF
ASLKDRPFHPLAKEKRGLSAEDYQVYQAEYNQPFALKTVAIHKDHVLHGDTANEAELEEFLGITLEQCTQ
TLEAKGLDAEDYMIFPVHPWQYEHVLPVMFEAEIAEGIVVLLDYKFGRYLSSSSMRSLIDIERPFNHLKV
PFSMQSLGALRLTPTRYMKNGEQAEQLLRQIIAQDETLAGHVALCDETQWWSFMNADKDIFQDQLGHLTM
QLRSYPESVKANAQQLVSMAALAAHDRTLYEMILGKDHPSMTSEQIEALFEDISDQFLKMTLSFMKYGVL
PELHGQNVLISFREGHVQQFVLRDHDTVRIYPPWLTANGIELPQYAVRKDTPNTLINEDLETFFAYFQTL
AVSVNLYAIVDALVDVFGVSEHELMTLLKQTMKNHVDTIDWLPGDKEEVRHILFEKQTWPFKRILLPLLH
QRGSGGGSMPSSIGTVPNPMMRYD
>gnl|CDD|411208 NF033586, staphy_B_SbnF, staphyloferrin B biosynthesis protein SbnF
NIEQQVKQRIMNQLVTSLIYEDVVQYQVSQQDAVETFTIEGEDATYRVTVQESDSFQRLTLTSPVWRIVG
DGETETLDYAQLLREVEFTFEKDEEKLEQFIIELLQTELKDTQALRYREQHPPSKLLTFDDYESYAMEGH
MYHPSYKSRLGFTLEDNLRYGPDFRPTFQLQWLAIDKDHVETTVSQNIEVNQLLQQQLGDETYAHFVETI
QAHGKSLEDVVWIPVHPWQFEHIIQVELAEEWLNGEILWLGESDEMYTPQQSIRTLSPTDTTKYYLKVPI
SITNTSTKRVLAPHTIENAAQITDWLKHIQAQDTYLQDDLKTVFLGEVLGQSYLNTQLSEAKQQAIYGAL
GVIWRENIHHYLASEEDAIPFNALYSLDKDQRPLIDAWIAQYGAEAWMKQFLKVAVQPMIHMLYYHGIAF
ESHAQNMMLIHEDGWPTRIALKDFHDGVRFKRELLSEIAQNPQLKDTPEAHKKVNSNSFIETEDVALVRD
FLHDAFFFINIAEIIMFIERQYGLDERLQWEYVYAVIEQYQQTFPNLPNYAHFDLFEPTIQVEKLTTRRL
LEDSELRIHHVSNPLGV
>gnl|CDD|411209 NF033587, transpos_IS6, IS6 family transposase
FKRERFPPEIILLAVRLYLRGPLSLRDVEEILAERGVSVSHSTIYRWVHKYAPQLAKRLRRRKPRPPDSW
AVDETVIKINGKWYYLYRAVDKEGETLDFLLSPRRDTDAAKRFLRKLLKKHDGSPRVILTDKAPSYPAAL
RRLGLEGRLPRRIEHRQRKYLNNLIEQDHRRTKRFINSMLGFKSFRTARRTLAGFEAMYNLRK
>gnl|CDD|411210 NF033588, transpos_ISC774, IS6 family transposase. ISC774 is an example of an outlier clade of IS6 family insertion sequences. Members so are appear restricted to the archaeal genus Sulfolobus
VILSLMEYINLKPRFHSSEEVALALASYLLGLSLRRFHVPHSTVLYYWRRLANYRYPVSLSGFYAVDETK
IRVVKGLLYYLWVVRDVNTGAIPFFMVTSTRSGLDVIILLKGLRVRTEENRVVYLHDGLPVYNALSWLGV
GHEHVTFGKRNYVEQGFRSLKHRLSSMDFHFPWNASKNSLMRWFSAFFTLYNLLY
>gnl|CDD|411211 NF033589, staphy_B_SbnI, bifunctional transcriptional regulator/O-phospho-L-serine synthase SbnI. SbnI is a bifunctional protein involved in staphyloferrin B (staphylobactin) biosynthesis in Staphylococcus aureus and other members of the genus. It is a bifunctional protein. The N-terminal region is heme-binding, and loses the ability to bind DNA when heme is bound. Under low iron conditions, the biosynthesis operon for staphyloferrin B, a carboxylate-type siderophore, is derepressed. The C-terminal domain is a kinase that acts on free serine, producing O-phospho-L-serine, which is used as one of the precursors of staphyloferrin B
MKQMYETLKLIPVDKIDLHETFEPSRLEKTKASIEAEQFIRHPVLVVKTQSGRYMVIDGVHRFTSLKALG
CQVIPVQVIHETQYSIGTWHHKVPFGQWWEILQQEPLLPWTTEIRQETPFITMCKGHTEQYLYVEDLGEA
KLEAWKKVVASYSSTCKVERIAQSACTCLSSQDILMKYQPLQISEIEAVVNRGETVPAGVTRFNISGRCL
NLQVPLHLLKEQDELSQHRKWHQFLQKKIESMRCYTEKVYLVEQ
>gnl|CDD|468099 NF033590, transpos_IS4_3, IS4 family transposase
AAYRFIRNENVSAEDILEAHFQATVQRAKAHPLLLAIQDTTELNFTHHSVREGLGHLGNQGKQSRGLLLH
STLLVAPETQQPLGLIEQQRWSRDIKTRGKKRRRKRRPYEEKESYKWLEASEAAAERLGSPMTQVISVCD
READIYEYLEYKTTNQQRFLVRAMQNRRLEEEDGKLYDYSSQLQSAGEYTVEIPQKGGRKARQARLEVRF
APVTLKPPANKRAKAKELPSIPLNYVGCVEINPPEGEEPLEWHLLTSEPVTSLEQALEIIDWYELRWLIE
DYHKVLKSGCKVEELRLQTKERLERMLVIYSFVAWRVLQLRELGRSDPELDCTSTLLSPKEWKLLYWLKK
EKKPPPEKPPSLKWAYRWIAKLGGWLDRKRDGRPGWKTLWEGWFRLQDIAEGY
>gnl|CDD|468100 NF033591, transpos_IS4_2, IS4 family transposase
LTLTELGRALPGPAQVKSRIKRIDRFLGNPHLQRERLAIYIIHTPLLTGFLTEPVILIDWTNWKEGKRDI
NLRASIAVWGRSATPLEWTLLPKKQGNSNPKEHKAFLERLLALLPDDCIPIIVTDRGFIGRSWWFWLVEQ
LGWDFVGRVRGNVKVEPQGWQSVKRLYLKASGRALYLGEVRLGKKRPLVCGLVLYKAALKGRKKKRAKGA
KEPWLLLTSLPDSAKQAVKLYARRMQIEELFRDLKSRYGFGLEDTRSRDPERLDILLLLAALAFIWAWLL
GLAAEALGLHKHFQANTVKGRRVLSLFRLGLDVLRRPPLYLIRSLWLLEALKLLQFLSRT
>gnl|CDD|468101 NF033592, transpos_IS4_1, IS4 family transposase
LLRLLPPELLEELARETGFVQRRRKLPPDDLLWLLLFAQLSADESLRDLVRRLNALTLGGRTSVSKSALS
KARKRLPVEFLKELFERLLAQLQLGQLLPRKLWRGLRVLAVDGTTIRLPDSLENWAPGRGGKNSFPGVKL
HLLYDLLSGLPLDAAITPGKTHERTLLRQLLETLPPGDLLLFDRGYFSYELFAEIQEAGAYFVSRLKSNT
NYEVVEELGETDELQDVYVDTEESLQARKKKPQLPEKKKLRLVSVRDEEGEKEYVLLTNLPDPRLPAEEI
AELYRLRWQIELLFKELKSHLQLDHLRSKSPEAVEQELWGALIAYLLLRLLM
>gnl|CDD|468102 NF033593, transpos_ISNCY_1, ISNCY family transposase. The ISNCY insertion sequence family, as defined by ISFinder, encodes several apparently unrelated families of transposases. Members of this family resemble the transposases of ISNCY family elements such as ISRm17 from Sinorhizobium meliloti, ISMav9 from Mycobacterium avium, and ISNfl1 from Nostoc commune
LDPLLRDEIPELLRELQHIDQLLDDRDELFALLERDLPKRVSKKTGRPGMPAETVLRLAVLKLLYNLDYE
ELAEEVNDSITLRQFCRIGWGKVPSKSTLIDNISLLTPETLEQINQALVRAAHQEKLEKGRKLRVDSTVV
ETNIHFPTDSSLLWDGVRVIIRLLAKIKELAGLTGTRWRDRRRSAKKRKRSIRRTLRRKGGEAKEKRKRA
YRELLKIARKVLKQARQVLEKLKQAASTGALQRLLEKLEEFIDLAERVIDQTERRVIKGEKIPHSEKVVS
LFEPHTDIIKKGKAGRPVEFGHKVCLTEDQSGFILDHVVMEGNPADSELLVPMVERHIKRFGRAPRAVSA
DRGFASKANEAALKELGVKDVVLPKKGKRSKARREMESSRWFKRLRRWRAGVESRISALKRHYGLDRCRD
RGLEGFKRYVGLGVLAYNLQRIGR
>gnl|CDD|468103 NF033594, transpos_ISNCY_2, ISNCY family transposase. The ISNCY insertion sequence family, as defined by ISFinder, encodes several apparently unrelated families of transposases. Members of this family resemble the transposases of ISNCY family elements such as IS1202, ISTde1, ISKpn21, and ISCARN1
KVIQKVVDGRLTVKEAAELLGLSERQVRRLLKRYREEGAAGLVHGNRGRPPNNRLPDELRERVLALYRER
YYDFGPTLALEKLRERHGISLSRETVRRWMIEAGLWSPRKQRRPKVHQPRERRACFGELIQIDGSPHDWF
EGRGPKCTLLVAIDDATGRLMGLRFVESESTFGYFEVTRQYLEKHGKPVAFYSDKHSVFRVNEEELAGKG
DGLTQFGRALKELGIEIICANSPQAKGRVERANQTLQDRLVKELRLAGISTIEAANEALLPEFIPDFNRR
FAKPPASPEDAHRPLPPDEDLDLILCWREERKVSNGLTFSYDNKLYQLEDTPGNRRLIGKKVEVVEYPDG
RIELRADGRLLPYLEFD
>gnl|CDD|468104 NF033595, denti_PrtP, dentilisin complex serine proteinase subunit PrtP. PrtP, a chymotrypsin-like protease known as dentilisin, forms a complex with PrcB and PrcA. It is found in Treponema denticola and in numerous other Treponema species. Dentilisin from T. denticola plays a significant role in pathogen-host interactions in periodontal disease
ILFLSAAFALLFASCSMGINNTVIGNNGAVVAGTTAGNGVFSSEWIINQQEYKPDDNDIVEGYVIVKTAD
GFDKTLFTKLGGDVAGELSLTDTGFTYWYLHKEGDNKKLLLAVRSIEGVLYADPDYKVVAPDGVKADNQN
DSPRDTEPNASTFGLGDGNLLDDPEADLADYGLTITGALEAYKDIGYGDKTVVAGIIDTGINMLHEDFKD
ANGESIVLYAKSALTSGVGTYIGDGNPFTEIPIGENWDNDGHGTHCSGTIAARGNNNKGIAGVAWKNTKL
ISYQSLGASGGGDTWAVYGALADLTNIVEILRKEPATRTPAEFAGLPSYLQNTNFQITQKTVPVNMSLGG
SAGSEFAFEMLTNALAAGVLPVIAMGNEGRYTAAYPAAFPGVLAVGATNGKDKKAHFSNGGAWISVSAPG
ESIYSCGNGGTPDVKDSYEWMSGTSMATPFVTGTIAYLLSFDNAHDLTPYQIKTLLEKTADKIDGASSFT
DYYGYGRVNVLKAAKAVKDGNIPAENSVYSEKAVKVTVKNNGAAQTKPVVWKYELVDGITAAPLAYAGPV
GLTDDANAVSFKGLRKGREYSIGINDAGTYKTQTFTAANTDDTIYIFF
>gnl|CDD|468105 NF033596, denti_PrcB, dentilisin complex subunit PrcB
VLFLLFVSLSGCKTLPKNPAGTSVPDDKVLTVPAKSAAGEKNEHFKASKILSSQSDRIQISYEILESGNY
SKNGLPSVIRNQKDLDKLYSVLYGRSLKAPKIDFSKKAVVAVRAGPFNTGGYSIKLVSAIKTKDILELVF
LVKAPEPNEMVTQAFTRPYLIVSVDAEPSTKIFV
>gnl|CDD|468106 NF033597, denti_PrcA, dentilisin complex subunit PrcA. PrcA is a lipoprotein that, together with PrcB and the serine proteinase subunit PrtP, form a chymotrypsin-like surface complex that is also known as dentilisin, after its discovery and characterization in Treponema denticola. Dentilisin is an important virulence factor in periodontal disease
AAALCCICALACLFTSCPQSGSAQEPEIPADFVSVEVNVLDSVGGTPVDGTTLTVYKSGTTKQLYSQVTV
TNGKVTLYLSKNQRYDFELSGKKGKWAGSVIENYWVPSADEQTLTMIQREHGQITRGITPPKITSVKLNG
ASFTDISVWTGISGQPMKLYIVFTSPVGAVEEVAWNGFGAKLGIGKSPSSYNGIAGVSPVCKRNGDGSFT
STYVFDFEKISFPDGKNELIIVGYDVANNRVERHIPVEFKERRPAAKDLSNASFKNFRVEMERVPHSLNL
FSTPPQSGLRPFALNPVNGESSSYEALLWFQIKDKASTDLPIRGFDLYRREQGQAGWFKFVSRTYYDDYK
GETNPGWGFHQGYDTDSSLEENVEYEYKIRAFNDSHELDSPVATAKLLEAFTYELTSPANNGFVKKSEAA
NLSYSCKISNPDLWTKEQADWFSLGLLILDKTGQPVFGGKLRYVLKKSGGEPDILIDAISGTPGELSFRE
LYKRGLIAALQSYGINSLTDLDKVDYSTGIITITPKFLKTPFFNVPAFGPMEYQTGVTYQWDIQDWGKDA
VSLYDDEALAFVKMYQSKDADGNEIPCPSEPLGNNSSFGANAVNGRFTFTV
>gnl|CDD|468107 NF033598, elast_bind_EbpS, elastin-binding protein EbpS. The elastin-binding protein EbpS is an adhesin described in Staphylococcus aureus, with orthologs found in many additional staphylococcal species. EbpS is a membrane protein that lacks an N-terminal signal peptide region, has extensive regions low-complexity sequence rich in Asn and Gln, and has a C-terminal LysM domain
KNNFKDDFEKNRQSIDPEDHQETTDSENEQDDNEQESVEDKTNQQFPPRNAQRRQRRRDTATNNNQQQDD
KQTNNNEVQNEDGSLDDRHDESSLHKKENNNYDNHTKSADTAHSEPNESDKKDSKGKKAAAVGGAATGAS
AAAAHKHQKPKHSSDNKHNDQEDHHDDKSADADNDEHGAHDSSKGKGAAAAGAGAAAAAKHKHKKDNGMS
NNEQQDQDEKDDKKSGKKKKKAAVGAGAAGAAGAAASAAHSHAKKEHHNNDHDDKDKNKKKGGPLKKLLP
LIAALLILGALAIFGGMYLNNHNNSKNDDDKVAEVVKKDSDEAKASDKDKDKDKDDDKDKDKSKDDDKDK
AAEDNDASESDEANSSANNASAKAANENRTNNQAQNAQQQAAAQNNNQQQKQQAEQQNSQSQNAGQQTHT
VNGNENLYRIAIQYYGEGSPENVEKIRAANGLSSNNIHNGQVLVIP
>gnl|CDD|411221 NF033599, His_racem_CntK, histidine racemase CntK. CntK (cobalt and nickel transport system protein K) is a histidine racemase that performs the first step in the biosynthesis of staphylopine, a metallophore involved in the import of multiple divalent cations. It was first characterized in Staphylococcus aureus
RQVVEFSKYNPSGNMTVLVHSKHDPSEYASIANQLMATSHVCCEQVGFIESTQSDDGDLYHLVMSGNEFC
GNATMSYLHYLKEHQLLQSHQLQLQVSGCSDLVPCKIHDDGYYEVTMPQPQQVEPRQLHLGNQSFDALEI
TYESYVHYVVPIEEISEELKQQVEQFVRSQQWSNHFKTIGIMLFDVQKQFLYPLIYIPEVQSLIWENSCG
SGTASIGVFENYQTNQACEDFIVHQPGGSILVSSTKCEKNGYHTSIKGQVSTVATGQAYIE
>gnl|CDD|411222 NF033600, staphylopine_DH, staphylopine biosynthesis dehydrogenase
VLIAGTGPVAIQLAVICNQYTDHNIDMVGRASTSEKSKRFYQAYQRDGQFEVTTQNDAHQQLAGEFTLRH
FYKDYQDVEQTYDTLVLACTADAYRSVLQQLSLKTLQRLKHIILVSPTFGSHMIVEQQMSDLNPDIEVIS
FSTYLGDTRVIDTEQPHRVLTTGVKSKLYIGSTHESSKTINELKTLFEQLNIQLTVMDTPLHAESRNSSL
YVHPALFMNDFALKAIFEGTDVPVYVYKLFPEGPITMTLIREMRLMWQEMMTILKKLNVPSVNLLKFMVK
ENYPVRPETMDEADIEHFETLPAIHQEYLLYVRYTAILIDPFSEPDENGRYFDFSAVPFKQLYQNEQGVW
HIPRMPSEDYYRTQIIQAIGRALGIKTPMIDTFLHRYEAYCEAYQATHPHQQLSSQFNIQDFEEDIALVT
KYLK
>gnl|CDD|411223 NF033601, Sta_opine_CntL, staphylopine biosynthesis enzyme CntL. CntL (cobalt and nickel transporter L) is an enzyme involved in biosynthesis of staphylopine, a metallophore involved in the import of zinc, cobalt, nickel, and other divalent cations. CntL transfers aminobutyrate from S-adenoyslmethionine, and is sometimes misannotated as a SAM-dependent methyltransferase. The staphylopine biosynthesis pathway was first characterized in Staphylococcus aureus
TEIETQLQTYLEQFEQLYEKVLQDEEYIDALETLIDEYSQFILNPQYQQQYQAWRDTEEKQSLTKQLADI
TAQCVKQVEVIRARRLLDGKASTSGYFDNIEHCINEEFGQFEITKNDKLLLVGSGAYPMTLIQVAKETGA
SVIGIDIDEEAVDLGQRVVNVLAPNEDIEITNQTVDQLEDISEVTHIIFSSTVPIKYDILDQLYDLTNDN
VVVAMRYGNGLKSIFNYPSQETDPQKWQCVEKQTRPNQIFDIALY
>gnl|CDD|411224 NF033602, campy_sm_acidic, highly acidic protein. This highly acidic protein, usually between 50 and 55 amino acids long, is found so far in Campylobacter jejuni and Campylobacter coli. A reanalysis of proteomics data, performed by Dr. Samuel Payne of Pacific Northwest National Labs, shows strong evidence for expression of AIW09513.1, founding member of the family
MAYDDEDLEFDDYEGEEDEYAHNHHKSYNYDDDDYDFDDEANDDDFYEMD
>gnl|CDD|468108 NF033603, mini-MOMP_1, mini-MOMP protein. Mini-MOMP proteins, found in several species of Campylobacter, are small proteins (about 63 amino acids long before removal of the signal peptide) with strong homology to the N-terminal region of MOMP, the major outer membrane protein that is Campylobacter's major porin
MKKIFLIGMILNLGFHFVFAAPLDEVFKDIEVSGTVRYRYEIKKEKKYDKKNHKYQNKTQTEI
>gnl|CDD|411226 NF033604, epsi_CJH_07325, CJH_07325 family protein. Members of the CJH_07325 family are small proteins, shorter than 70 amino acids, expressed in members of the genera Campylobacter and Helicobacter. The function is unknown
EKLVRDSYGKVGYINIPYFNTGSVSDLTYGKTNPKELDEALQKLSDLLDKLYKKYE
>gnl|CDD|468109 NF033605, Zn_bnd_ABC_AdcA, zinc ABC transporter substrate-binding lipoprotein AdcA
MKKSLYILSLVIALAIVLAACGKGDSKNKDNDKIKINTTVFPLKSFAEQIGGKHVEVESIYPAGTDLHSY
EPTQKDILNASKADLFVYTGDDLDPVAKKVASTIKKDDKKLSLEDKLDKSTLLTDQHEHGEEHEHEEEGH
EHEHHHHHGGYDPHVWLDPKFDQTFAKEIKDELVKKDPKHKDEYEKNYKKLNKDLKGIDKDMKDITKDKQ
GNAVFISHESLGYLADRYGFVQKGVQNMNAEDPSQKELTEIVKEINDSGAKYILYEDNVSNKVTDTIRKE
TDAKPLKFYNMESLNKEQQKDKDLTYQSLMKENIKNIDKALNDKIKVKDDKAESKHDKAISDGYFKDSQV
KDRELSDYEGDWQSVYPYLKDGTLDEVMKHKAEDDGDMSAKEYKAYYDKGYKTDISNIKITGDTITFTKN
GKKVTGKYEYDGKDILKYEKGNRGVRYTFKLVGDANKDLPKYVQFSDHNIAPKKAEHFHIFMGNDKDKVL
KELDNWPTYYPAKLSKDEIKEEMLAH
>gnl|CDD|411229 NF033607, disagg_AAA_ClpG, AAA family protein disaggregase ClpG. ClpG, as characterized in Pseudomonas aeruginosa, is a Clp family member of the AAA+ family of ATPases. ClpG has stand-alone ability to disaggregate proteins from aggregates that result from heat stess. Both ClpG and its mobilized homolog ClpK provide increased survival of exposure to heat
MAQELCAICHERPAVARVSLVQNGQRRELALCELHYRQLMRQQRMRSPLESLFGGGSPFDEIFSGFGEQS
PVSPVRAREPEAVDIAEYFSKQTTEYLQRAAQVAAEFGKREVDTEHLLYALADADVVQAVLKQFGLSPAD
LKQYIEANAVRGAGKGEASEDMTISPRVKSALQHAFALSRELGHSYVGPEHLLLGLAAVPDSFAGTLLKK
YGLTEQALRQKAVKVVGKGAEDGRVDGPSNTPQLDKFSRDLTRLAREGKLDPVIGRSKEVETTIEVLARR
KKNNPVLIGEPGVGKTAIVEGLAQRMVQGEVPEVLRDKRLVELNINAMVAGAKYRGEFEERLKQVMDELQ
AAQSEIILFIDEVHTIVGAGQGGGEGGLDVANVLKPAMARGEMNLIGATTLNEYQKYIEKDAALERRFQP
VFVPEPTVEQTISILRGLRDKLEGHHKVTIRDEAFVAAAELSDRYIGNRFLPDKAIDLIDQAAARVRIAS
TSRPAEIQELEAELAQLKREQDYAASRKWYDEAKVFEKRIQERKEHLEQITERWQQTQGSKTEEVRVEDI
AEIISRLTGIPVTELTAEEREKLLQMEERLHQRVIGQQEAITAVSDAVRLARAGLRQGSRPIATFLFLGP
TGVGKTELAKALAEVVFGDEDAMIRIDMSEYMERHAVSRLIGAPPGYVGYDEGGQLTERVRRRPYSVILL
DEIEKAHADVNNILLQVFDDGRLTDGKGRVVDFTNTIIIATSNLGSDLIMKNAQAGEFAQPPEKLKRELM
NTLRGHFRPEFLNRLDEVIVFESLSKAQIEDIVRLQLERVKRAAHAQDIHLHIDDSLVGHLAEEAYQPEF
GARELKRQIRQQLETRLATAMLKGDVKEGETITFFHDAKDGVGYRKGAAPKPAARKKAGAGETPKGRASA
ARKPAAKKGAAAKGKADKPKAK
>gnl|CDD|411230 NF033608, type_I_tox_Fst, type I toxin-antitoxin system Fst family toxin
DILVTIIAPIIVGCIVALFDHWLRNRDK
>gnl|CDD|468110 NF033609, MSCRAMM_ClfA, MSCRAMM family adhesin clumping factor ClfA. Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif
MNMKKKEKHAIRKKSIGVASVLVGTLIGFGLLSSKEADASENSVTQSDSASNESKSNDSSSVSAAPKTDD
TNVSDTKTSSNTNNGETSVAQNPAQQETTQSASTNATTEETPVTGEATTTATNQANTPATTQSSNTNAEE
LVNQTSNETTSNDTNTVSSVNSPQNSTNAENVSTTQDTSTEATPSNNESAPQSTDASNKDVVNQAVNTSA
PRMRAFSLAAVAADAPAAGTDITNQLTNVTVGIDSGTTVYPHQAGYVKLNYGFSVPNSAVKGDTFKITVP
KELNLNGVTSTAKVPPIMAGDQVLANGVIDSDGNVIYTFTDYVDTKEDVKATLTMPAYIDPENVTKTGNV
TLTTGIGSTTANKTVLVDYEKYGKFYNLSIKGTIDQIDKTNNTYRQTIYVNPSGDNVIAPVLTGNLKPNT
DSNALIDQQNTSIKVYKVDNAADLSESYFVNPENFEDVTNSVNITFPNPNQYKVEFNTPDDQITTPYIVV
VNGHIDPNSKGDLALRSTLYGYNSNIIWRSMSWDNEVAFNNGSGSGDGIDKPVVPEQPDEPGEIEPIPED
SDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDS
ASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS
DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS
DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS
DSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASNKNEAKDSKEPLPDTGSEDEANTSL
IWGLLASLGSLLLFRRKKENKDKK
>gnl|CDD|468111 NF033610, SLATT_3, SLATT domain. The SLATT domain contains two transmembrane helices. SLATT domains are generally predicted to function as pore-forming effectors in a class of conflict systems which are reliant on the production of second messenger nucleotide or nucleotide derivatives. SLATT domains are predicted to initiate cell suicide responses upon their activation. This SLATT family is always N-terminally fused to the SLATT_1 family, and is typically operonically linked to either inactive TIR domains or SLOG domains which could act as regulators of the SLATT channels. The SLATT domain defined here (170 residues long) is similar to the DUF4231 domain (105 residues long) described in Pfam model PF14015
LFRAADAASLKGQRRYLRLTRLQLLLLLVAAALGSLSWDVGSGGLDLAALLAALAFLGALALEVYLSRRR
PERHWYEGRAAAESVKTLAWRYAVRAEPFDGSDADADALFRERLEEILRENRDLGWLDPRSDLGPQITDA
MRELRALPLEERRDTYLRERIEDQ
>gnl|CDD|468112 NF033611, SAVED, SAVED domain. The SAVED (SMODS-Associated and fused to Various Effector Domains) domain is predicted to function as a sensor domain, sensing nucleotides or nucleotide derivatives generated by SMODS and other nucleotide synthetase domains. The sensing of ligands by SAVED is predicted to activate effectors deployed by a class of conflict systems which are reliant on the on the production and sensing of the nucleotide second messengers
DASKRELLIAEIGGLRSPLTESEALAALPPDRLEDRPDLVLDLTQAFSDRKIPSPEDWDEELLELLEKLA
KFLRQALRAGDGVRLALFGLAPVPLAFALGAILGDKSGVTVYQYQRDSSWAWSTRDPDPEGPPFEVEELE
VLQGGDEVALAVSLSYDINDEDLIEELGPNVGRIISLSLPGPGNDSIRSPEDAAALAKEIREAIRALRAK
PGVKRIHLFLAAPASLAFLLGQRLNARGPPIVVYEYDRDNGTYPPALTLPS
>gnl|CDD|411234 NF033615, CDF_MamM, magnetosome biogenesis CDF transporter MamM
YEKCVKCSKKIGWVGLVVNLVLAVMKAFVGIISGSQAMLADALYSAKDVVTSLLVIVGLKVSGKPLDEEH
PYGHGKIEFVLSLVISVVFIIGTGFLLVHAVKVLLDGSSHRAPHLIALWAALISVVVNVKMYSYSRCVAI
ETNSPMVRTLAKHHHADAISSAAVALGIIGAHYLGMPWIDPLVAVIETIHLLYLGGVVFWDSVKGLMDSS
VDKETRDRIEELARLVPGVEEVTSLRARKVGQEIWAEMIIGVDPDLTIEEAYKIGERVEETIAKRIPHIG
GINVSAEPYE
>gnl|CDD|411235 NF033616, CDF_MamB, magnetosome biogenesis CDF transporter MamB
CKECRDEVVWWAIFVNIAQTVFKGVLGVLSGSAALVADSLHSGADVVASIVTMASVKISSRPADEKYPYG
YGKIQFISSSIVGLILIFGAIFLLYESVSKIISGDIEAPSVIAVLGAAVSIITNELMYRYQSCVGTENNS
PAIIANAWDNRSDALSSIAVLVGIVFAVIGFPIADVLAAIGVSILVIRIGIELNIDAIDGLMDTSVEMDE
LTDIYQIAKDTPGVHGVYYLRGRNVGEDLHVDINIEVDGKLKVYESDLIAEALKQRIFREIPHARDIQVF
VTPV
>gnl|CDD|411236 NF033617, RND_permease_2, multidrug efflux RND transporter permease subunit
SDVFIKRPVATLLLSLLILLLGLLAFRKLPVREYPEVDFPTITVSTSYPGASPELMQSSITQPLEQQLAQ
IEGIDEMTSQSSLGYSTITLQFRLGTDLDVALSEVQAAINAAQSLLPSEAPDPPVYRKANSADTPIMYIG
LTSEEMPRGQLTDYAERVLAPKLSQINGVGSVDVSGGQRPAMRVWLDPEKMAARGLTADDVRSALNSNNV
NSPKGAVRGDSVVSTVRANDQLKTAEDYEDLVIKYADNGAPVRLGDVATVELGAENVRNRAWANGVPAVV
LGINRQPGANPIEVADEIRALLPELQETLPKNIKVNVLYDRTRFIRASIDEVESTLLEAVALVILVVFLF
LRNLRATLIPAVTVPLSLIGTFAVMYLFGFSINLLTLMALVLAIGLVVDDAIVVVENIHRHIEEGESPLE
AALKGAREIGFTVIAMTLTLVAVYLPILFMGGLTGRLFREFAVTLAGAVIISGIVALTLTPMMCSRLLKA
NEKPGRFARAVDRFFDGLTARYGRGLKWVLKHRPLTLVVALATLALLPLLYVFIPKELAPSEDRGVIFGM
IQAPQSISLDYMSAKMRDVEKILSSDPEVQSLTSFNGVGGNPGDNTGFGIINLKPWDERDVSAQEIIDRL
RPKLAKVPGMDLFLFPLQDLPGGAGSSLPQYQVTLTPSDYDSLFTWAEKLKEKLRKSPQFADVDSDLQDK
GPELNVDIDRDKAARLGISMQDIGSTLEVAFGQRQVNTIYTDGNQYKVVLEVDRRYRLNPEALNQIYVRS
NDGKLVPLSTLAKIEERAAPLSLNHFNQFNSATLSFNLAPGVSLGEAIEALDQAAKELLPSGISGSFQGA
ARAFQEEGSSLLFLFLLALAAIYLVLAIQYESFVDPLTILSTVPLAGCGALLALALGGQSMNIYAQIGLI
TLIGLVKKNGILMVEFANELQRHQGLSRREAIYQAAALRLRPILMTTLAMLLGAIPLMLSTGAGAESRFP
LGIVIVGGLGVGTLFTLFVLPVVYLLLAR
>gnl|CDD|411237 NF033618, mlaB_1, lipid asymmetry maintenance protein MlaB. MlaB belongs to a system that maintains asymmetry in the outer membrane of Gram-negative bacteria, with LPS in the outer leaflet and phospholipids in the inner leaflet. Several components of the system share homology with typical ABC transporters
EALSWEREGDTLALSGELDRDTLLPLWQQREELLAGVTCIDVSGLERVDSAGLALLVHLRAEARQQGREL
KISGVSDRLRTLITLYNLPEIILP
>gnl|CDD|411238 NF033619, perm_MlaE_1, lipid asymmetry maintenance ABC transporter permease subunit MlaE
ARLGRRTLDALARLGRATRFLLRALFGSPQSLKRPRLLIRQLYFVGVLSLLIIVVSGLFVGMVLGLQGYY
TLVRFGAEEALGQLVALSLLRELGPVVTALLFAGRAGSALTAEIGLMKATEQLSAMEMMAVDPLRRVIAP
RFWAGVISMPLLAAIFSAVGILGGYLVGVDWLGVDEGSFWSQMQASVDFRDDVLNGVIKSLVFGVVVTWI
ALFQGYDAVPTSEGVSRATTRTVVYSSLAVLGLDFILTALMFG
>gnl|CDD|468113 NF033620, pqiC, membrane integrity-associated transporter subunit PqiC. PqiC (YmbA), a lipoprotein, has been identified as part of the PqiABC system, a transporter that bridges the inner and outer membranes in species such as Escherichia coli and is important to membrane integrity
KWLPLALALLLSACSSSTPQKTYYQLPAVAATASAVSTSSQSGQRQLWVEQVSVPDYLAGNGVVYQTSDV
QYVIASNNLWASPLDQQLQQTLVANLSAALPGWLVSSQPLGSDQDTLNVNVTGFHGRYDGKVIVSGEWLL
THQGQLIKRPFNIELPQQEDGYDALVRTLAQGWQQEAQSIAQQIA
>gnl|CDD|468114 NF033621, de_GSH_amidase, deaminated glutathione amidase
KVALGQFAVTPDWQENAQTCVDLMAQAAEAGADLLVLPEAVLARDDTDPDLSVKSAQPLDGPFLTQLLAE
SRGNDLTTVLTVHVPSGDGRAWNTLVALRDGEIIAQYRKLHLYDAFSMQESRRVDAGNEIPPLVEVAGMK
VGLMTCYDLRFPELARRLALDGADVLVLPAAWVRGPLKEHHWETLLAARALENTCYMVAVGECGNRNIGQ
SMVVDPLGVTIAAAAEAPALIFAELDPERIAHAREQLPVLENRRFAPPQL
>gnl|CDD|411241 NF033622, repair_DdrC, DNA damage response protein DdrC. DdrC is a DNA-binding protein that seems restricted to the genus Deinococcus, and that plays a role in the ability of members of that genus to recover from fragmentation of their DNA. Note that the region where DdrC is found in Deinococcus radiodurans R1 originally had incorrect structural annotation, with a feature designated DR_0003 shown on the opposite strand
MKSAPLTLEFGSVRLPVSADGLLHAPTALRQLGLDEADWETLAATHDLPSPPRDFGAGPEATLSVDDFTR
LAFALDTPEARRWRKRAQELLARAMQGDVRLAAQIAERNPDPEARRWLAARLESTEARRELMSTVARHGG
EGQVYGQLGSISNRSVLGTDSATIRRERGVKNTRDGLTSAELLRLAYLDTATARAIQEHGAHGNAAILRL
HERVARRERLLWD
>gnl|CDD|468115 NF033623, urate_HpxO, FAD-dependent urate hydroxylase HpxO. HpxO is an FAD-dependent urate hydroxylase (EC 1.14.13.113). Like the factor independent urate hydroxylase (EC 1.7.3.3), it consumes O2 and converts urate to 5-hydroxyisourate, which decomposes spontaneously to allantoin and CO2. However, HpxO oxidizes NADH to NAD(+), and produces H20, while EC 1.7.3.3 produces H202 as a byproduct
KVIIIGAGIGGLTAAIALRQAGHEVEIYERVRELRPVGAAISLWSNGVKVLNRLGLGEEIAALGGDMDRM
AYRDGHTGETLTRFSLAPLVEEVGQRPYPVARADLQQMLLDAFGRDDVQLGKRCVGVEQDADGVTAIFED
GSRATGDLLIAADGTHSVLREYVLGEPVERRYAGYVNWNGLVPADEDLAPADQWTTYVGEGKRVSLMPVG
GDRFYFFFDVPLPKGLPNDRETYRAELREHFAGWAEPVQKLIDRLDPETTNRVEIHDIDPFDTLVKGRVA
LLGDAAHSTTPDIGQGGCQAMEDAVVLARALQTTNLSVEDALKRYEAARKERVGDLVLKARKRCDVTHGK
DPEVTQAWYEELRQEDGERIIRGIAKTILGGP
>gnl|CDD|411243 NF033624, HpxX, oxalurate catabolism protein HpxX. HpxX is a small protein of unknown function, about 60 residues in length, encoded in the set of four genes, hpxWXYZ, that belong to the oxalurate metabolism portion of a complete pathway for hypoxanthine (hpx) utilization, as in Klebsiella pneumoniae
WAAYIAQMEQLLALELDDARRAELLVQFSRIAAMAQPLMAFPLDDRLEIAGVYKA
>gnl|CDD|411244 NF033625, HpxZ, oxalurate catabolism protein HpxZ. HpxZ is not characterized, but it is encoded in the cluster hpxWXYZ, associated with oxalurate catabolism, within the larger hpx (hypoxanthine utilization) locus of species such as Klebsiella pneumoniae, where KPN_01771 is HpxZ
EINLPDVLAEVTAAFARYEQALVSNDVAVLDELFWNDPRTVRYGAGENLYGYDAIRAFRAARPPAGLDRT
LRNTVITTYGRDFAVASTEFRREGSPRIGRQSQTWVRFPEGWRVVAAHVSLM
>gnl|CDD|411245 NF033628, snapalysin, snapalysin. Snapalysin (SnpA, or Small Neutral Protease A) belongs to the metzincin family of zinc-dependent metalloendopeptidases
ALSAALGLGLAAALLGAAVPAAAAPAPAAPAAATSYAAYAGSAEEAAANKAFFEAVMKSVAEKRAANPGA
AAVTVTYNASQAPSFRSQIARSTQIWNSSVSNVKLQEGSNADFSYREGNDSRGSYASTDGHGRGYIFLDY
AQNQQYDSTRVTAHETGHVLGLPDHYSGPCSELMSGGGPGPSCTNAYPNAAERSRVNQLWANGLAAA
>gnl|CDD|411246 NF033629, RiPP_CPAC, RiPP peptide. null
NAFDMEIEEAFADDIAIEELGDMAGAGGTTNTGGTFGSTTCPACIGTAFSWS
>gnl|CDD|468116 NF033630, SLATT_6, SLATT domain. The SLATT domain contains two transmembrane helices. SLATT domains are generally predicted to function as pore-forming effectors in a class of conflict systems which are reliant on the production of second messenger nucleotide or nucleotide derivatives. SLATT domains are predicted to initiate cell suicide responses upon their activation. This SLATT family associates with a SMODS nucleotide synthetase domain fused to the predicted AGS-C sensor domain. It is sometimes further coupled to R-M systems
MNKEDLLKQIAETGYNVGFGAKKHFATYDIVEKLPGWISFISLAIGILALAFDELSTKELSAALIILGII
GLYISFYDSDKEKYEKAGIKLTQLFNELRDLYYEVKSSSDSDDLTEAQERLKEIENEFYSISISKQILFS
DWYAHYKFFWQSQIDWIDEQLKFTFWRDKIPLSLRITII
>gnl|CDD|468117 NF033631, SLATT_5, SLATT domain. The SLATT domain contains two transmembrane helices. SLATT domains are generally predicted to function as pore-forming effectors in a class of conflict systems which are reliant on the production of second messenger nucleotide or nucleotide derivatives. SLATT domains are predicted to initiate cell suicide responses upon their activation. This SLATT family contains an additional C-terminal alpha-helix, and strictly associates with a reverse transcriptase domain, part of a predicted retroelement with diversity-generating potential
LLDKIWITRKARFNASRRLLRKNFLSTFSLSFYSIYLIALSLLQLIFPNNFSNNLLSIISIILSVLVLVI
SLLISSANYKERAEKLHECALELNELYRKLKLLLSNEKDSNEEKKELYKELAKEYEEILDKYENHSDIDY
KLAKLEKSKEYGNRKPTKWLYIKYYLLSIFRYLILILLILLP
>gnl|CDD|468118 NF033632, SLATT_4, SLATT domain. The SLATT domain contains two transmembrane helices. SLATT domains are generally predicted to function as pore-forming effectors in a class of conflict systems which are reliant on the production of second messenger nucleotide or nucleotide derivatives. SLATT domains are predicted to initiate cell suicide responses upon their activation. This SLATT family is often coupled to the SMODS nucleotide synthetase and is sometimes further embedded in other conflict systems like CRISPR/Cas or R-M systems
ELREWYERVLYTHKAHEKAADRLRKYHLWLGIPSIILSALTGTGVFASLGDEIWAKKLITGVLSLLAAIL
TALQTFLNPSERAEKHRSAANRYLALREKYLSLLLDIKDGAISDEELRERRDELREELDELYSDAPPTPS
KAYKKAQKALKIGE
>gnl|CDD|468119 NF033633, SLATT_2, SLATT domain. The SLATT domain contains two transmembrane helices. SLATT domains are generally predicted to function as pore-forming effectors in a class of conflict systems which are reliant on the production of second messenger nucleotide or nucleotide derivatives. SLATT domains are predicted to initiate cell suicide responses upon their activation. This SLATT family is the only prokaryotic SLATT family to exist as a standalone domain, with no as-yet discernable genome associations
LAGRPFPLGDWGEPAERLDELYRWAEAEALETIDWYLADRRVKRRASRVLRALAALGAVAGALLPLLALT
GVPGLTQWGYVALALAAGCVAADRYFGLSSGWMRDIATAQALQRRLEAFQFDWASESVREVLGPTEGTAS
EAAERCLGVLRRFSEDVSELVRAETADWMSEFRAGLEPLPT
>gnl|CDD|468120 NF033634, SLATT_1, SLATT domain. The SLATT domain contains two transmembrane helices. SLATT domains are generally predicted to function as pore-forming effectors in a class of conflict systems which are reliant on the production of second messenger nucleotide or nucleotide derivatives. SLATT domains are predicted to initiate cell suicide responses upon their activation. This SLATT family is often C-terminally fused to the SLATT_3 family, and is typically operonically linked to either inactive TIR domains or SLOG domains which could act as regulators of the SLATT channels. In relatively rare instances, it is genomically linked as a standalone domain to the RelA/SpoT nucleotide synthetase and the predicted NA37/YejK sensor domain
YLRERIEDQIDWYRKKARRNRRRYRRLRVLTIVLSAAIPVLLALLRAGGPSAALLWDIALVLSALVAALA
AWLQLFRYQELWIAYRLTAEELKREKDLYELLSGPYRADEEAFALFVERVESIISREHTQWLARR
>gnl|CDD|468121 NF033635, SLATT_fungal, SLATT domain. The SLATT domain contains two transmembrane helices. SLATT domains are generally predicted to function in bacteria as pore-forming effectors in a class of conflict systems which are reliant on the production of second messenger nucleotide or nucleotide derivatives. SLATT domains are predicted to initiate cell suicide responses upon their activation. The role of this fungal family is not yet understood, although the expansion of the family in many fungal lineages points to a potential role in conflict
LGLYARAVRERRKAARQYRLTSYLLNILLGLQIILGALLTALGATSGRHGIAITVLGALNTVIAGLLALL
KGSGLPERLRDLENELRKVEDFIEDTERETGVPLDEEVDEEVEELRRRYEEAKAN
>gnl|CDD|468122 NF033638, RNase_AS, polyadenylate-specific 3'-exoribonuclease AS. RNase AS is a 3'-exoribonuclease, found in Mycobacterium tuberculosis and other Actinobacteria, that acts specifically to degrade polyadenylate sequences from the 3'-end of RNA
YFYDTEFIEDGRTIDLVSIGVVAEDGREFYAVSTEFDPSRAGPWVRRNVLPKLPSPSSPAWRSRAQIRDE
LLEFLTADGGRDPPELWAWVGAYDHVALAQLWGDMTALPRELPRFTRELRQLWEDAGRPRLPAAPADAHD
ALVDARHNLAKFRAI
>gnl|CDD|468123 NF033640, N_Twi_rSAM, twitch domain-containing radical SAM protein. Members of this family are unusual among radical SAM proteins in several ways. First, the N-terminal region consists of an iron-sulfur cluster-binding twitch domain (half of a SPASM domain), something usually found C-terminal to the radical SAM domain. Second, the radical SAM domains in many of the members of this family score poorly vs. the Pfam HMM, PF04055 (version 19), used to identify radical SAM. Lastly, the majority of members sequenced to date come from uncultured bacteria from marine or aquifer sources rather than from conventionally cultured bacterial isolates. The function is unknown
SKTFCPLPWTHLYIHPDGNVRPCCHARDDKGPLGNLKETSLEEIWNSDYMKKIRKKMLNGERPPGCEKCY
KEEDSGGRSLRQESNERWAKHIEDAIKSTDEDGSDDVNPRYLDLRFGNLCNLKCRMCGPHSSSSWAKEAK
KLGGPKLGDKKKISWFEDEEFWKWLEELLPSLKEIYFAGGEPLLIKEHYKLLEKLVEKGRAKNIELRYNT
NLTVLPDKLKDLLDLWKKFKSVSISASIDGVGERNEYIRYGSKWDEIEKNLKKLKEECPNVELRINPTVS
ALNVLHLPELLDWLLELGLGPIDIYLNILRDPEYLSIKNLPKEIKQKVIEKLENFLEKNDNGFDKYLIKK
LKRLINYMNSEDNSELLKEFKKFTKKLDKIRGENFLDVFPELKELL
>gnl|CDD|468124 NF033641, antiterm_LoaP, antiterminator LoaP. LoaP is a paralog of NusG with an extensive presence in Firmicutes. The founding member, from Bacillus amyloliquefaciens, was shown to serve as an antiterminator for the transcription of genes involved in antibiotic biosynthesis
WYVLFVRTGKEEKVKKLLNKLFDKELLRCFVPKRKLPERKQGKWYKVIKPLFPGYVFIETDMNEELYYKL
KKIPGIIRLLGNEGDEFSPIPEEEMEFLLKLLNDDDIIEYSKGYIEGDKVIVISGPLKGLEGIIKKIDKR
KRRAKIELNFMGEERLVDVGIEIVSK
>gnl|CDD|411256 NF033642, stress_AzuC, stress response protein AzuC. AzuC is a basic, extremely small protein (28 amino acids in Escherichia coli K-12) whose expression is repressed by cyclic AMP response protein (CRP) and stimulated by acidic pH
KLRKILKSMFANYCKTFKDVPPGAMF
>gnl|CDD|439409 NF033643, EspJ_gen, EspJ family T3SS effector ADP-ribosyltransferase
MNIIKNCLSSLNNILGMSCRSYAVSKGHQASKFLNRIISPKNTPVELLTYRNADLSKERFITQNVLSIFN
IKRDFVAVRIQEDKFTDLKNKTIQGHKNTVAKVRDWYNPYQNAFGISMGTPRRSSDIAKKECRNALNVML
MEKNDFNEKILNSDNLQKQYGGTENKSWVVASLGELLDKGAKVYPDESCSLRLGEPFIITLPETVKVNVD
IYPVKK
>gnl|CDD|468125 NF033644, antiterm_UpxY, UpxY family transcription antiterminator. The UpxY family of NusG-related transcription antiterminators was described originally from a paralogous family of eight members from Bacteriodes fragilis, UpaY to UphY, each of which was associated with a distinct capsular polysaccharide biosynthesis locus. There is no UpxY protein per se
WYALYTRPRREKKVAELLEKKGIESFLPMQKEIRQWSDRKKRVEVPLIPNLVFVHITEKELDEVLEQTPG
VVRYIRDDRGKSKPAIIPDKQMERFRLMLDPSDEVVVYLEAPLKKGDKVRVIGGPLKGLEGELVRVKGKK
RVVVRIPGLGAVATVEVPPSYL
>gnl|CDD|468126 NF033645, pilus_FilE, putative pilus assembly protein FilE. FilE is found almost exclusively in the genus Acinetobacter, and is assigned as a putative pilus system protein from local genomic contexts that include several additional putative pilus system proteins. Note that some members of this protein family have proline-rich repeat regions for which spurious translation in another reading frame can give a false-positive match to Pfam's collagen repeat region HMM, PF01391
QRPKLAISLLLLALASVSTVYADGEFYTIIGPDGRPMIVPRKAVKKKVKPKKQVQETEPEKKPQKKSVST
SKKLVKSKSVAEKSPVNVENPSLTKSQAPTAPTAPTAPTSPVAPTAPPAPQEKVNKVVSETVPQVQVKTT
KPQQTESQKSLVIEKPEAKKKSVSVTIQKKASQASSSSTSTKDKSPFTEIDGEEYVNNEYLEDQEFNLEG
KKRFYTMPDGSGRMETIERKKGVSRSVLDKLFNRSQQSELKPIVLAPTYYRLSQQDLASAFENDRCFLEK
YLKSIKTLSLNKEVGLWPRKPLKEKFEYEVVKLDSSIQYMQIDSYASSNEKPTYYWPLVVFLDEKGCVLE
GVSGFKNQETPATVLQHAAIQGVLKVPENTRYILLTPLASAVDVEEKELSNQGQIKLSVIR
>gnl|CDD|468127 NF033647, adhesin_LEA, LEA family epithelial adhesin N-terminal domain. LEA (Lactobacillus epithelium adhesin), as characterized in an adhesive commensal strain of Lactobacillus crispatus (ST1), is a large, repetitive protein with an N-terminal YSIRK-type signal peptide and a C-terminal LPXTG site for processing by sortase and attachment to the cell surface. Family members contain variable numbers of an 82 amino acid long repeats similar to Lactobacillus Rib/alpha-like repeats. This HMM describes the N-terminal region upstream of the repeat region, just over 600 amino acids long
MKKNRFIEFKEKRRYAIKKVSGKTASVFIGATIFGIILSSHSVKAATKETVSTTATTISNDQTSETSNVV
TLANNQKNESSTSENATGKVQQSSASNNATANNSTEAATTSQSTPNTQGSADTDIKDIRSSTAISAAKLA
TMNLMQTSGSTGTDTGATGATGTTTGSDRNAAGTVDQNNINTQPAKENQKLANKTNLTSSDNYSSNIYKG
TDGKYYKIVTIYGNDYVYRAADIQANGTAFGQWATTAEDTKNNINISKEDLGNGKTRWTVVFFPNKGLQN
VGSTLSGLSSAKFGIALTNDYQIVGNVDMDVISDPNQTFVSHTFKDGSNSATDIPVQNPPAEVKFSFNPN
TDVDPNTGLINSKTMPAYNNKYLQGPYYFTTATSTGAKNLWQTYFKDGVEYNNAYDGTTPYLGGNHDFHF
NNFEIKNKTGVDGAKYGDKIIYDKLGYRLNSKNANSNGVFNSDNFNQAMEFKSQGVTSQSQFSSYVISFT
TQHTDSHEVELATGPKNQQFSGISANIYSYQNGYYNMFSRLYGEQRALNPAGAAYPEVNPKDIIPNWVPA
EDAMAKINKDYLNNAQINVLRNKILNNITDPDAVNNIIKEGNSLNDAMKKLGNSIGQYDDDGSFADHKVD
TTKASDRYKYASPDKKAAYDDATEA
>gnl|CDD|468128 NF033649, LipDrop_Rv1109c, lipid droplet-associated protein. RHA1_ro05869 from Rhodococcus jostii RHA1, an ortholog of Rv1109c from Mycobacterium tuberculosis, has been shown specifically with lipid droplets that consist of a neutral lipid core enveloped by a phospholipid monolayer and surface proteins. Lipid droplets of triacylglycerol can be especially prominent in members of the genus Rhodococcus, but occur also in Mycobacterium tuberculosis and can support dormancy of that pathogen
MKRAPFPARVAAGLAVTAVEETRKLPTTLLTLPMTAVSQALQLSMRVQQNVTELAIKGDEALESLFRPPE
EQPEWATFDEDLDPAPDDAPADPDGAGAEERATEGRFALYSEDPWAEEERARAALYSSGPADVAAATASG
PAPEIVELLDYDSLTLAQLRARLRSLSVDDLEALLAYERATRARAPFVTMLANRITNAR
>gnl|CDD|411261 NF033650, ANR_neg_reg, ANR family transcriptional regulator. ANR family transcriptional regulators include the AggR-activated regulator Aar. The name ANR (AraC Negative Regulators) refers to an effect on, rather than homology to, certain AraC family transcriptional regulators
LYKRYAEEAAEAERAGDYARAAELWRKASLLAKNEENREWCENRADFCEKAAAR
>gnl|CDD|468129 NF033651, cyto_nec_fctrs, CNF1 family cytotoxic necrotizing factor. CNF1 family of cytotoxic necrotizing factors, glutamine amidases that find their way to their eukaryotic host cells' cytosol and permanently activate certain GTPases, includes full-length homologs of CNF1, CNF2, CNF3, and CNFY, but it excludes smaller proteins such as the type 3 secretion system effector VopC
MNNQWQQKYLLEYNELVSKFPSPEKVISDYIKNKFNTDLPWFSWVDPDNLYFIQFSQSRSNSKSYTGWDH
LGKYKTEVLTLTQAAIINIGYRFDVFDDANAVAGIYKTSNADLFDEKNEAKMLPSEYLYFLKNCDFAGLY
NKALSDYWSKNYEKFKLLLKNYYISSILYLYKNNLISKDEYDFAMNALNRKNNISLFFFDIYGYYSSDIF
VAKNDERVMLFIPGATNPFLFSKNINDLRGRLKELIKESDNKELLSQHFSLYDRQDGTTYYGVNSVLNKI
VNDNFNESYFMYSNKKITERDVFDAIAISVKKRSFSDGDVIIKSNSEAQRDYALTILQTILSMTPIFDVI
LPEVSVPLSLGIIASSMGISFDQLINGDTYEERRSAIPGVATNAVLLGLSFAIPFLISKASANKEILSKL
VSNEDNILNETNIDDFLKEYGINKDDIPSTGVLEIELKNTEQPVNIVKLSDEDNKIVAVKGSSLSGIYYE
VDIETGYEILSRRVYRTEYNNKIFWTRGGGLKGGQPFDFENLEIPVFFKDKPYSELASSSELSFINDDSP
LLYPDVDSRLPKPTPEMDIRNYSTDRSSFKEQTVTLMRGTTEEEAWNIANYKTAGGSNEELEEIFIGGGP
QSNLSFTEYTSNINSADAASRRHFLVVIKVKVKYINNDNVSYANHWAIPDEAPVEVLAVVDRRFLFPEPP
SPPKLSIIQKILRRFFKENIAETSSINFQRLNSGNINVLKGRGSISSTRQRAIYLRFDAANADELRPGGF
YIKKNRFDDLGYDRYFYNNTVGLNGSPTLNTYTGEILTDSSSLGSTYWKKYNLTNETSIIRVSNSARGAN
GIKIALEEVQENKPVIITSGNLSGCTTIVARKGGYLYAVHTGTSEPLAGFTSTTGVKKAVEVLSLLSGQE
IPKVEGIMNNDFLVNYLAENFDESLITYSSSELKPNSIITISRDNVSTFPYYTDDIPLPGFGTSVTILVR
VDGNTVVKSLSESYSLNADGSKISVFKVLSKDF
>gnl|CDD|468130 NF033652, LbtU_sider_porin, LbtU family siderophore porin. LbtU, from Legionella pneumophila, a novel TonB-independent siderophore uptake outer membrane protein from a species that lacks TonB, is the founding member of a class of porins that may be involved generally in siderophore-mediated iron acquisition
PRISISGLLEVEAAYGSPYDGKSSSDITLATAELGIEAQINDWVEAYISLLYEELDNDDLNVDEAYITIG
NLDKSPFYFTAGKFYVPFGNYSSNMISDPLTLELGETRATAAQLGYEQGGFYASVYLFKGDTTIDGKDNR
INSWGANLGYAFELDNVSYEIGASYISNLADSDGLQDTAANPGTGFGTLDPTDRVPGWSVYANAGFGPFS
FIAEYVAATDSFAAGDLSFNGRGAKPSAWNLEAGYTFPVFNKPSSLAVGYQGTDEALALNLPKQRYGVGL
SVSIFKDTTLSLEYRHDIDYDNPTGGTGNKSDTVTLQLAVEF
>gnl|CDD|468131 NF033656, DMQ_monoox_COQ7, 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone monooxygenase
DRLISEFDKALRTLFAPARASRPSPAAALEAAGALSDAERRHAAGLMRVNHVGEVCAQALYQGQALTARD
AAVREALEEAAREETDHLAWCEERLRELGSRPSLLNPLWYAGSFALGALAGRLGDKWSLGFVAETERQVE
AHLDSHLERLPEQDARSRAIVEQMRDDEARHAAAALAAGGAELPAPVRALMRAMSKVMTTTAYRI
>gnl|CDD|468132 NF033657, choice_anch_F, choice-of-anchor F family protein. Choice-of-anchor F is a domain found in prokaryotic proteins with a variety of C-terminal sorting and transit domains. These include the autotransporter outer membrane beta-barrel domain, the JDVT-CTERM domain, and variant forms of PEP-CTERM domains
GAIYWDEPEGQAPGLKVVTGDDFTGSPGGVTNCIMASGPNPQCSDPFQSGKRFKLQLTGDGPVDLVFDVA
ADGGETIYRVFQKLSNLTGARLTGFTIELGFGVGGDFVPSTPGDGLGFSLTGTFDADANDIELSAQFPFG
LFGDADKNHEGDGFFDTERAGFGLDATEDLLTSGGLSGADYSALFGDWLSNSMVPDGLFWDDDGDPTTDN
ALMAWCDGAAGGWVTGRLGVDLDDNGAPSLGVDVADLAVPAAVLAAWAANGLYEVDPIEDLANLNLNYFI
TVGDIAGGGSFTLRVT
>gnl|CDD|411265 NF033662, acid_disulf_rpt, acidic double-disulfide repeat. The acidic double-disulfide repeat is an Asp-rich repeat with four nearly invariant Cys residues in a repeat length of about 35 amino acids
EATDTTCSDGIDNDGDGLTDCADPDCAGNPVC
>gnl|CDD|411266 NF033663, AceI_fam_PACE, AceI family chlorhexidine efflux PACE transporter. The AceI family of proton-coupled multidrug/biocide efflux transporters includes several shown to respond to the presence of the biocide chlorhexidine and improve resistance to it, among other biocides and antibiotics. Members of the family seen so far, including founding member AceI, have been chromosomal and restricted to the genus Acinetobacter
MLISKRRLIHALSYEVILLVIIAIALSFIFEMPMEVTGTLGIAMAVTSVIWNMLFNHYFEKFEAKHQLKR
TIKVRILHAIGFEGGLMLATIPMVAYAMQMSLWQAILLDFGLTLCILVYTFIFQWCYDHIEARLGY
>gnl|CDD|411267 NF033664, PACE_transport, PACE efflux transporter. PACE transporters, including the chlorhexidine efflux transporter AceI, average about 140 amino acids in length and consist of two tandem homologous domains described by Pfam model PF05232. PACE transporters are single component efflux transporters that sit in the plasma membrane and couple proton import to substrate export
GLKERIVHAVLFEVIAILISAPLLAWLMGRSLSHSGALAVMISTIAMLWNMIYNALFERWERRQRVRRRT
VRRVLHAIGFEGGLVLILVPLAAWWLGISLLEAFLLDIGLLLFFLPYTFVFNWAFDKLRG
>gnl|CDD|411268 NF033665, PACE_efflu_PCE, multidrug/biocide efflux PACE transporter. PACE (proteobacterial antimicrobial compound efflux) transporters are single component proton-coupled efflux pumps that help confer resistance to a number of biocides and antibiotics. The family has also been named PCE (proteobacterial chlorhexidine efflux). Members of this subfamily of the PACE transporters, distinct from the AceI-like branch, include several whose expression is increased by exposure to chlorhexidine and/or help confer increased resistance to it
SLTERIFHAVGFEGIAVLICAPLLAWLMDRSLLEMGALTIMLSTVAMLWNMIYNALFDRLWPRLGVARTL
KVRVLHALGFEGGLILIGVPLAAWWLGISLLQAFLLEIGFFLFFLPYTMVYNWAYDKLRA
>gnl|CDD|468133 NF033668, rSAM_PA0069, PA0069 family radical SAM protein. PA0069 from Pseudomonas aeruginosa is the founding member a family of radical SAM enzymes of unknown function. Note that inclusion of some members of this family in COG1533, along with some spore photoproduct lyase (SPL) proteins, has led to some family members being annotated as SPL
RGRGAQSNPSGRFEKEEREAFDDGWESLEELPPFKTEVIVERAKTIITRNDSPDIGFDRSINPYRGCEHG
CIYCYARPTHAYLGLSAGLDFETKIFVKPDAAELLERELARPGYQPKTIALGGNTDPYQPIEREFRITRQ
ILEVLLEARHPVGIVTKSALVLRDIDILAEMAKRGLVKVALSVTTLDRKLARKMEPRAATPEKRLEAVRA
LSEAGIPVGVMVAPIIPGLNDHEIERILDAAAEAGAREAGYVLLRLPLEVAPLFRDWLLRHYPDRARHVL
SLIRSMRGGKDYDSRFGTRMRGEGPYAWQIGRRFELACRRLGLNRRRPALRTDLFRPPRKGGGQLSLF
>gnl|CDD|411270 NF033672, mbn_chaper_assoc, copper uptake system-associated domain. Proteins from this family that may contain just an N-terminal signal peptide followed by this domain, or have a copper chaperone domain in addition, just past the signal peptide. A majority of bacteria that encode a peptide-derived methanobactin precursor encode a member of this family as well, strongly suggesting a role for this domain in copper acquisition
AIRALLKATFDKPDAPLTVAPVVVSGDHAIAGWTQGERGGRALLRRGGGGWQIVLCGGDGLKDAAALEKA
GVPAADAAALAAALAQAEAKLPPERVALFSSFEG
>gnl|CDD|468134 NF033674, stress_OB_fold, NirD/YgiW/YdeI family stress tolerance protein. Members of this family possess an N-terminal signal peptide, and are associated with tolerance to various toxic stresses. These include antimicrobial peptides (YdeI), hydrogen peroxide (YgiW and YdeI), and nickel (NcrY and NirD)
KLLLAALLALLSAPAFAADGGFTGPAANVTTVAQALKAKDDTPVTLTGNIVKQLGDDKYEFRDATGTITV
EIDDDLWRGQTVTPKDKVRITGEVDKDWKPTEIDVDRIEK
>gnl|CDD|468135 NF033675, NTTRR-F1, NTTRR-F1 domain. NTTRR-F1 (N-terminal To Repetitive Region - Firmicutes 1) is a homology domain found strictly as the N-terminal non-repetitive region of otherwise highly repetitive proteins of various Firmicutes. The repetitive region that follows typically is collagen-like, with every third residue a glycine
SINNLIVNGGFETGSLTPWSGVNASITSQFSHSGFYSARLLGGTVNSFISQTVPVTPGESFEFLVSLAKT
GNLPSPQVNIQIAYYDAAFNFLGTGLIITIPSGRLPNANNGTWLEIYQTTSPAPAGATQALVLINKLPQA
GSADVLVDDVSLLTV
>gnl|CDD|411273 NF033676, Lacb_SerRich_Nt, serine-rich glycoprotein adhesin prefix domain. Lacb_SerRich_Nt describes a Lactobacillus-restricted N-terminal non-repetitive sequence region shared by proteins with extensive serine-rich repeat regions, all likely to function as adhesins. This region contains a variant form of the KxYKxGKxW motif (see TIGR03715) followed by a region related to serine-rich glycoprotein adhesins of the Streptococci
NRKIDEQEDKSKVKLYKTHRGWFSALTRFFKLFSFGSKKEVKAEQFNDLDSLKDDDDSTSTDAYKKGLAT
VATLLGAGAI
>gnl|CDD|411274 NF033677, biofilm_BapA_N, BapA prefix-like domain. Two largely unrelated repetitive proteins, both named biofilm-associated protein BapA (from Salmonella enterica and from Paracoccus denitrificans) share homology domains at the two ends. Both lack a typical signal peptide for translocation by Sec, and instead depend on type I secretion for export and for contribution to biofilm formation. The conserved prefix (i.e. N-terminal) domain is shared by a number of other large, repetitive proteins of Proteobacteria thought to be associated with adhesion or biofilm formation
ISVISKETGVVLTQTQGEVVLLNEPSVVKIKVSREDVASYTRQGNDLVITLKDGETIVIENFFV
>gnl|CDD|468136 NF033678, C69_fam_dipept, C69 family dipeptidase. Members of the MEROPS C69 family (subfamily 001) are dipeptidases (EC 3.4.13.-)
ACTTILVGKKASIDGSTIIARNEDSGAGAFPPKLFVVVAPEDQPRHYKSVLNGFTIDLPDNPLRYTATPN
ADDKDGIWGEAGINEANVAMSATETIYTNERVLGADPLVEDEGGIGEEDMVTLVLPYIKSAREGVERLGK
LIEKYGTYEGNGIAFSDKDEIWYLETGGGHHWVAQRIPDDAYAVAPNQLAIQEFDFDDPDNFMCSPDLQE
FVEEHHLNPDADGGFNFRHIFGTHDEKDRHYNTPRVWYGQRYFNPEKDQDPESQDLPFIRKPERKISIED
VKYVLSSHYQGTPYDPYGTGTEEDKHRYRPIGINRTQESHILQIRPDVPAEIAGIHWLAFGVNAFNPYVP
FYANVTDTPAYYRNTTDEYDTDSAYWLNRLLAVLVDAHYHKYAPLVEDYQEATLAKGRALVAETDKAAAG
DGAEATALLTEANDKMAAEALDLTQKLLGKLLTQGTNLMKLKF
>gnl|CDD|468137 NF033679, DNRLRE_dom, DNRLRE domain. The DNRLRE domain, with a length of about 160 amino acids, appears typically in large, repetitive surface proteins of bacteria and archaea, sometimes repeated several times. It occurs, notably, three times in the C-terminal region of the enzyme disaggregatase from the archaeal species Methanosarcina mazei, each time with the motif DNRLRE, for which the domain is named. Archaeal proteins within this family are described particularly well by the currently more narrowly defined Pfam model, PF06848. Note that the catalytic region of disaggregatase, in the N-terminal portion of the protein, is modeled by a different HMM, PF08480
ADTYVSSAYPNTNYGGSSYLKVGNDGGGGNRRSYLKFDLSSLPAGATITSATLRLYVYYSYSTDSGTSPT
TVEVYRVTSDWSESTVTWNNAPAAAYASITITVSSVPDGGWVEIDVTDLVQAWVSGTYPNYGFLLKASDE
SNGWKSFYSSEAGNASNRPYLVVT
>gnl|CDD|468138 NF033680, exonuc_ExeM-GG, extracellular exonuclease ExeM. ExeM, as described in Shewanella oneidensis, is a biofilm formation-associated exonuclease that cleaves extracellular DNA (eDNA), a biofilm component. Members of the ExeM family contain two or three pairs of Cys residues, presumed to form disulfide bonds, and a C-terminal GlyGly-CTERM membrane-anchoring segment. Strangely, engineered removal of the GlyGly-CTERM region did not result in net export from the cell and appearance of the enzyme in culture supernatants
MDNVKKLSVLALSIAAALPMMASADVMISEYVEGSSNNKAIELYNSGDAAVDLTGYKLVRYKDGATTASD
MVALDGTIAAKSTKVITHNSAAITLDAGVDSMTGNLYFNGGDAVALMKDGVVVDVVGAIPTPDDWGKDVT
LQRKDDALAASTVYVESEWTTLAKDTFSGLGARSGDFVGGAGTEPEVPAFSCVGATITPIYDVQGAGFSS
PLVAEGKYESDEEVTIRGVVTARGDSLFKGFYLQEVQGDNSPYTSDGIFVYLGEAAPEAIQPGVEVCVQG
KVKEYYGLTQIDIKADKKFEVGADGEVPAAEAFYVADGETLADALERYEGMKVVLDAGSDMKVTRTFSYD
YAGRRNNMVLSHKAPLMKPTQVYAPLSDEAIALAKANRANQLFIESDFKAANGVVPYFPDFNAETGYIRI
GDQLTNLEGMVGYSYGAYRLVATNEITAGDFIRDNDRTDAPEVATKGDIRVASFNVLNLFTSDDDVGGKD
DANADGASRGCGRGAHTLEEYLLQRTKIVNAITEMNADIVGLMEIENNGFGETSSIQYLVNALNAELPAD
DAYSFIEIADADKYKGKFIGSDAITVGMLYRPAKVKPAGDAFVIATPEQHAAEGVATRGEGDKVETSPSY
DKYQRHSLAQTFSINDEKLTVVVNHLKSKGSGCLEDWLEFSESKDPADLQGKCNEFRVSAAKVIGESLKD
VEGDLLVIGDLNAYGMEDPVRVLTDYDAATSDRDIVTASWTTLNGKVYEREGSKIDKGYGLINLNTQAHG
AATYSYSYNGELGNLDHALGNASLAARLVDIEDWHINSVESNLFEYSSKYTGDLEKSENAFSASDHDPVI
VALSYPAPVEPPEPEPPPKKDDGGSLGYLGLALLSLLGLRRRK
>gnl|CDD|468139 NF033681, ExeM_NucH_DNase, ExeM/NucH family extracellular endonuclease
VEGVVTAVPTGGLNGFYLQTPGTDGDGNPATSDGLFVYTGAAVTDVAVGDRVRVTGTVSEYYGLTQLSAV
SAVEVCGTGAAVTPTPLTLPVDEALRLERYEGMLVRLPQDLTVTDNYNLGRYGELVLSAGGRLLQPTQVA
APGSAEAAALAAANAARRIVLDDGSTAQNPGPVPYYPGLSADNTLRVGDTVTGLTGVLDYRFGAYRLQPT
NGATAPDFVPANPRPAAPALVGGDLRVASFNVLNYFNGDGFGGPADFPTNRGADTAAEFERQQAKIVAAI
NALDADVVGLMEIENNGYGRDSAIADLVDALNAAAGGGTYAYVPSPGTDPLGTDAIRVALIYRPAKVTPV
GDAAILDDPAFDGSNRPPLAQTFRPKGGGETFTVVVNHFKSKGSGCASGDDDQGDGQGCWNATRVAAAQA
LADWLATLPTGVGDGDVLLLGDLNAYAKEDPIRVLTDAGYTNLVARFHGDDAYSYVFGGESGSLDHALAS
PSLAAKVVGATDWHINADEPTALDYNTEYKGAADLYAPDPYRSSDHDPVIVGLDL
>gnl|CDD|468140 NF033682, retention_LapA, retention module-containing protein. The retention module, as described for the giant adhesin LapA of Pseudomonas fluorescens and for an ice-binding giant adhesin of an Antarctic bacterium, appears at the N-terminus of a number of very large repetitive proteins, many of which have C-terminal regions that make them substrates for type I secretion systems
TQVAVVKAVSGTVFAVNADGSVRVLKVGDTLQAGEIVITGNGAAVELQLADGSTLTLGENCVACVTEDNG
LIEFDAEEAAAASFDDPDIAAIQAAILAGADPTELLEATAAGLAGGAGGAGGGFVTIDRNGDEVLPSTGF
PTAGF
>gnl|CDD|468141 NF033683, di_4Fe-4S_YfhL, YfhL family 4Fe-4S dicluster ferredoxin
MALLITDECINCDVCEPECPNEAISMGDEIYEIDPDRCTECVGHYDEPQCVQVCPVDCIIPDPDHVETQE
QLMEKYERL
>gnl|CDD|411281 NF033684, suffix_2_RND, transporter suffix domain. Members of this protein family contain a highly hydrophobic region about 70 amino acids long that usually occurs as essentially the full length of a small membrane protein, but in some cases occurs as a C-terminal suffix domain for RND efflux transporter permease subunit proteins
RKKLGIGLLILSFLYWIAVPILPFLDIPTSNKAALISVLLIVGEVLFLIGIALLGKEYWQKIKRYLNPK
>gnl|CDD|411282 NF033685, Tet_leader_L, tetracycline resistance efflux system leader peptide. Stalling of the ribosomal translation of a tetracycline resistance system mRNA from inability to properly translate a short leader peptide can affect mRNA secondary structure, preventing early transcriptional termination and therefore inducing expression of the resistance protein. This leader peptide is found upstream of efflux transporters such as tet(L) and tet(45) (which occur in Gram-positive organisms), but on occasion may occur as a fused additional N-terminal domain of such efflux proteins
MKCNKMNRVQLKEGSVSMAL
>gnl|CDD|411283 NF033686, leader_PheM_1, pheST operon leader peptide PheM
MNAAIFRFFFYFSA
>gnl|CDD|411284 NF033688, MG406_fam, MG406 family protein. Homologs to MG406 from Mycoplasma genitalium and MPN605 from Mycoplasma pneumoniae are about 150 amino acids long on average, highly hydrophobic, widespread in but restricted to the Mollicutes, and highly divergent there. MG406 itself appears to be an essential gene
IFKNKFKKKILIILLILSLLVLIVLLILVLTKIINWNWLTGWLLGLIFSLIGFFILKFSVKLLIKNENPF
LFYFFFILRIGIYAIPFLISFYLPNIFSIIGVLIGLSPIILLPFFNN
>gnl|CDD|411285 NF033689, N2Fix_CO_CowN, N(2)-fixation sustaining protein CowN. Carbon monoxide inhibits the ability of Mo-nitrogenase to fix nitrogen, but expression of CowN is protective, and allows nitrogen fixation to continue
PDRYVSFKGIDCDGNARRLMARLRRHIADPAKDSPFWDYFRQKLDEAAGRGLDDLFLLHSQINTLRELFE
EHDDEEALALLERLEEECC
>gnl|CDD|411286 NF033690, ErmCL_fam_lead, ErmCL family antibiotic resistance leader peptide
MGMFSIFVINKVHYQPNEK
>gnl|CDD|411287 NF033691, immunity_MafI, MafI family immunity protein. MafI proteins, as described in Neisseria species, are small proteins encoded in modules with MafB (multiple adhesin family B) secreted toxins. Homologs are found broadly, primarily in Proteobacterial genera such as Neisseria, Cronobacter, Enterobacter, Pseudomonas, etc
INERIKELGESLKGRLPEELLREALEYIDHGEYGLAFETLCDHICEYDVVITPEEYELIEELANEMN
>gnl|CDD|468142 NF033694, perox_inhi_SPIN, SPIN family peroxidase inhibitor. SPIN (staphylococcal peroxidase inhibitor) binds to and inhibits human myeloperoxidase to resist killing after phagocytosis by neutrophils
KKLIVATVAVGVLSTGAFAVTPHNQADAKVTSQNGIILHDDSRLLEHELSYVDVLLDKNTDKKTKAQLKA
YFKLQGLKSVSDIVKKAKKDGLDTSKYDH
>gnl|CDD|439412 NF033695, trnsprt_adja_30, KPN_01571 family protein. Members of this family are very small, highly hydrophobic proteins regularly encoded adjacent to transporters and likely to be previously overlooked small subunits of transporters
MNPFIWVFIALLALDAVRELMGASSVLGLW
>gnl|CDD|411289 NF033696, CrpP_fam, CrpP family protein. CrpP, described originally as a protein encoded by Pseudomonas aeruginosa plasmid pUM505, confers elevated resistance to ciprofloxacin, but not to four other fluoroquinoline-type antibiotics tested. The apparent mechanism is phosphorylation. However, CrpP appears more closely related to the ribosome modulation factor Rmf than to any known aminoglycoside phosphotransferase
HKTSDRRRFNNPHAAVMRAGAEAARKGLPVHACPYRHPAMRASWLKGFAQAQQQSLDF
>gnl|CDD|439413 NF033697, leader_RseD, rpoE leader peptide RseD. RseD, as described originally in Escherichia coli, is a leader peptide translationally coupled to the extracytoplasmic stress response sigma factor RpoE. It participates in the CrsA-mediated fine-tuning of the stress response. It is found also in Salmonella enterica, Cedecea neteri, etc. The corresponding locus in Klebsiella pneumoniae appears to be split into an upstream and a downstream peptide
DTLTLCLLKNALMEWRFDSAWKFGLGRHYLG
>gnl|CDD|411291 NF033701, yciY_fam, YciY family protein. Members of the YciY family are named after the gene symbol given in E. coli K-12, but members of the family are found also in Salmonella, Klebsiella, Yersinia, Erwinia, etc
MKRSRNEVGRWRMLRQVQRRRARWLEGQSRRNMRIHSIRKLLVNQQRRSLLFAVYY
>gnl|CDD|468143 NF033703, transcr_KstR, cholesterol catabolism transcriptional regulator KstR. KstR, a protein characterized in Mycobacterium tuberculosis (MTB) and M. smegmatis is a TetR family transcriptional regulator that is essential for pathogenesis in MTB. In controls the expression of about 80 proteins involved in the earlier stages of cholesterol catabolism. KstR binds not to cholesterol itself, but to catabolites found early in the degradation pathway
GSAAQRERRKRILDATLALASKGGYDAVQMRAVAERADVAVGTLYRYFPSKVHLLVSALAREFERVEEKL
DRSALPGDTPYERLRFVLDRITRAMQRDPLLTEAMTRAFMFADASAAAEVDQVGRLMDRMFARAMGDGEP
TEEDLAIARVISDVWMSNLVAWLTRRASATDVANRLELTVRLLLG
>gnl|CDD|468144 NF033704, helico_Hpn_like, nickel-binding protein HpnL. The Hpn-like protein HpnL, or Hpn-2, including founding member HP1432, is a histidine and glutamine-rich metal-binding polypeptide that binds nickel, among other metals, any may help deliver sequestered nickel for the biosynthesis of urease, which is critical to the survival of Helicobacter pylori during exposures to strongly acidic conditions. This protein is a paralog to the histidine-rich nickel storage protein Hpn (e.g. HP1427). Both nickel-binding proteins are expressed in response to nickel, under control of the regulator NikR
MAHHEQQHQAQQQQQQQANSQHHHHHHAHHHHYYGGEHHHHNAQQHAEQQAEQHAQQQQQQQKAQQQNQQ
Y
>gnl|CDD|411294 NF033705, helico_Hpn, nickel storage protein Hpn. Hpn (Helicobacter pylori nickel) is a histidine-rich polypeptide, 60 amino acids in length, capable of binding nickel and several other metals. It can store a reserve of nickel for biosynthesis of active urease, critical to the ability of the bacterium to survive acid exposure during colonization, and hydrogenase. Hpn is closely related in its N-terminal region to a somewhat longer His and Gln-rich protein, called the Hpn-like protein. Both are expressed, under control of NikR, in response to nickel
MAHHEEQHGGHHHHHHHTHHHHYHGGEHHHHHHSSHHEEGCCSASDSHHQEEGCCHGHHE
>gnl|CDD|411295 NF033706, Ni_bind_SCO4226, SCO4226 family nickel-binding protein. Members of the SCO4226 family belong to the larger family of DUF4242 domain-containing proteins, described by Pfam model PF14026. SCO4226 itself was shown to dimerize and bind four nickel atoms per homodimer
MAKFMDVHHGMKGITADQLKAAHRADLAIEGEEGVHFERAWADPESGTVYCLSEAPSAEAVQRVHERAGH
PADEIHPVPLTV
>gnl|CDD|468145 NF033707, T9SS_sortase, type IX secretion system sortase PorU. PorU, part of type IX secretion systems (T9SS), is the protease responsible for both removing the C-terminal sorting signal found in substrates and for its replacement by anionic LPS, through which most T9SS substrates become attached to the cell surface after secretion
VLASGNWYKIRVTESGVYKITKAFLRQLGFSVNSIDPRKVKIYGNGGNMLPELNSDPRPDDLPENAIQVV
GEEDGRFDAGDYILFYAEGPVSWNSNEEFRHTRNPYSDYGYYFITEGSGPGKRIDSQVSPAATATTTITT
FDDYQFHEVDLYNLLKSGRNWFGEPFSIGNSQTFTFTIPNLVTSEPVKLTVRVAAGSSSSSSFTVSINGQ
SLGTITISSISSGSYDKGREATFTYSLTNNSNNVTVTLTYNNNGNPGGPGYLDYISLQAKRPLRGYGAQF
FKAPAGTLKEYVAFDPSDFPAPEYVGRVTNQNLHGDQDPDYLIITPPKLLSQAERLAQFHRTHDGLNVKV
VTLDQIYNEFSSGTPDITAIRNFLKMLYDRASSPADRLKYLLLFGDGSYDYRNRTSDNNTNYVPTYQSEN
SFNPVSSYVSDDYFGFLDDGEGGNLSSSDKLDIGVGRFPVRTPEEAKTMVDKTIAYESNKSFGDWRNNLT
FVADDGDNNLHMVDADELADTIEQNKPEYNVKKIYLDAYPQESSAGGQRYPEVTQAIKQAIEEGALIMNY
FGHGGEDGLAHERVLTLSDIQNFTNKNRLPLFITATCEFTRFDNPNRTSAGELAFLNPKGGAIALLTTTR
TVYASYNFALNRAFLEHLFEYNENGKPPTLGEALRLTKNNSISTSNKLNFFLLGDPALKLAYPKPKVVLT
SINGVPVAGSTDTLKALSKVKLKGEVTDANGNLLTDFNGTLTVTVFDKKITRTTLGNDGSALPPFTYTDR
GNVLFRGQASVTNGRFEFSFVVPKDINYSVGNGRISLYAVNADSTEDATGANSDIVIGGINENAPNDNIG
PEIKLYLNDESFVSGGIVNTSPYLLAKLEDESGINTAGSGIGHDITLIIDGDESNTYVLNDYYTADLDDY
TKGTVLYPLPNLEPGLHTLTFKAWDVYNNSSTAELQFVVVGGLELTIRNVLNYPNPFVNYTEFWFEHNRP
GEPLDVQVQVFTVSGKLVWTHNQTVTSTGFLSYTITWDGRDDFGDRLGKGVYIYRLTVKSSDGNKKAEKA
EKLVIL
>gnl|CDD|468146 NF033708, T9SS_Cterm_ChiA, T9SS sorting signal type C. The sorting signals of type IX secretion systems (T9SS) in the CFB bacteria are long, compared to other prokaryotic C-terminal sorting motif-containing signals, including LPXTG, PEP-CTERM, and GlyGly-TERM, and they seem to contain multiple motifs. A few T9SS substrates, including ChiA, have a variant form of T9SS sorting signal that may score poorly to both TIGR04183 (type A) and TIGR04131 (type B), depend on T9SS for secretion, but are released from the cell rather than left anchored to the cell surface
IKSVTVYDILGRLLYSKKNINNNELTILNLLLSQQVLIVKVTLTNGKKVSKKIIF
>gnl|CDD|468147 NF033709, PorV_fam, PorV/PorQ family protein. Proteins closely related to PorV, and its paralog PorQ, are found regularly in species with type IX secretion systems (T9SS), the system associated with a type of gliding motility in many of the Bacteroidetes
TTAVPFLLIAPDARAAAMGDAGVATSPDANSQYWNPAKLAFAESKSGVSLSYTPWLRKLVADINLGYLSG
YYKLDERGAIGASLRYFSLGEIELTDENGNPTGTFSPYELAIDLGYSRKLSDNFSMGVTGRYIRSDLGSG
GEDAKPASAFAVDVGAYYQSPFFLGNKEGRLSFGFNISNIGPKIKYDDGGQKDFLPTNLRLGGAYDLILD
EYNKLTLALDANKLLVPTPYPNKSFISGIFKSFGDAPGGFSEELKEITLSLGAEYTYNNLFALRAGYFYE
SELKGNRKYFTLGAGFKYNVFKLDFSYLFATNNPLANTLRFSLGFNF
>gnl|CDD|468148 NF033710, T9SS_OM_PorV, type IX secretion system outer membrane channel protein PorV. PorV, as characterized in oral pathogen Porphyromonas gingivalis, is a component of the type IX secretion system (T9SS) needed to process a subset of T9SS substrates. PorV is a paralog of PorQ
LLLLLLLSASALAQQQDPEFNPITTAVPFLLIAPDARAGGMGDVGVATSPDANSQQWNPAKYAFAESKAG
VSLSYTPWLRKLVNDIFLGYLTGYYKLDDRSAIGASLRYFSLGEIELTDANGNSLGTFNPNEFAIDVSYS
RKLSENFSMAVAGRYIRSDLAGGTSNNDAKPGNAFAADISGYYQSEEILGNFEGRWRLGFNISNIGPKIS
YDDGGQENFLPTNLRLGTGFDFPLDEYNKLTFALDFNKLLVPTPPDGDGDGDIDPGDDYEDVSVISGIFK
SFGDAPGGFSEELKEITWSLGAEYWYNDQFALRAGYFYESPNKGNRKYFTLGAGFKYNVFGIDFSYLFST
SQNNPLDNTLRFSLTFNF
>gnl|CDD|468149 NF033711, T9SS_PorQ, type IX secretion system protein PorQ
KKLIFLLLFLLLLSLSAFAQGGQTVYNFLNLPVSARAAALGGDNITLIDDDPSLAFSNPALLNSVMDKTL
SLNYMNYLAGINYGTAAYAYTVGERGTWAVGAQYLNYGKMKGTDENGNETGTFSANDIALSGGYSYNLSD
RFTGGANAKFITSSIESYNSFGVAVDLGLNYYDPDKDLSVSLVARNLGGQLKAYNETREKLPFDVQLGVS
KKLEHAPLRLSLTLHDLQHWNISYSNPNNGEYDLDEKVSFGDKLLRHLVLGAELLPSKNFNIRLGYNFRR
ANELKIQDSRHFAGFSAGFGLKLNRFKFNYAYAKYHVSASSSMFGLSINL
>gnl|CDD|468150 NF033712, B12_rSAM_KedN5, KedN5 family methylcobalamin-dependent radical SAM C-methyltransferase. KedN5, the founding member of a family of radical SAM enzymes with an N-terminal B12-binding domain, is a C-methyltransferase that relies on a methylcobalamin cofactor during natural product biosynthesis
VALVQQGVWDMPLESMPLAAGYLKAVALADPRLAGEVDIRIRNFRGGVTLLEMANDLFADGVPDVLAFSV
LGWNYRQFGALAETFKQLNPDGWVVFGGNHVANQAERVFREFPAVDVVVNGEGELTFRELLRAYLDGRSP
RDLHDIAGISFRDPDGEVVTTPDRDRIDDLDIIPSPFLTGAIPLTDEDGRFRYDVALMETNRGCPYKCSF
CYWGGAVGQKVRAFSRERLRAELELFAKHKVHTIVLCDANFGMLPADEEFVEDLIEIRERYGYPRALETS
WAKNKSKVFYRIVRKMKEAGLRSSFTLALQTLDDDALTLMNRRNMKVNDWEDLAEWLNEEGLDCYAELIW
GAPGETVESFLEGYDRLARHVSRIAVYPLLLLPNTDYSENRELHGFVTVRGEDDDFEYVLAHRTMTLAEN
LRMQRFLFWARVLAENQVLRHIWVPLRELAGITQSQVILSLDDWIEASDDPAAEPLREAAPVALADSPAL
APALRYLYTTPEAKRLLRRWWREAVVPRLPAEWREFLDELFRYDLLTRPVYVPPGREPPDGLPLVSVDGE
DYYVSDDVRFPYDVPALLAALRAGEPPDPEPEPTTVDLYYRVGFEDFLGSTNHEEIAHYMGTPE
>gnl|CDD|411302 NF033713, DbpA, DbpA
MIKYNKNLLKLTLLVSLLIACGLTGETKARLESSAKDITDEIDKIIKEAAKKGVNFDAFTDTKTGGKVAE
GPFIREAKIRAIAVAEKFLKAIEEEAIKLKETGSSGEFSAMYDLMFEVSKPLEKIGIQEMTKTVSEAAEK
NPPTTAEGILEIAKTMEEKLQNVKEK
>gnl|CDD|468151 NF033715, glycyl_HPDL_Lrg, 4-hydroxyphenylacetate decarboxylase large subunit. 4-hydroxyphenylacetate decarboxylase, an enzyme with a glycyl radical active site, depends on a radical SAM enzyme for activation, and is found in strict anaerobes such as Clostridium difficile. It has a large and a small subunit
ATKLEEILAERGIPLEFQVGGEAPEEISEREIKKEPSPRAKKLMDIYYDTLSTADMEFPYWYNREWWEND
GELPVVRRAKALKAAFSHLTPTIWPGEKLVMNKTKFYRGSFPMPWLSESFFNAKEEALYKEALAPGSASA
DEVSVFGAGGGNVTKSFGNVVSIAGKFGMRKEEVPVLVKLAKEWEGKSVEDLGNKYEKMVPDYDIKENIM
KSVICMFDSGFTIPQGREVINYYYPLEYGFDGLIEMCDEKIAEVAGEADGDGIIGMDRLYYYEAMKLVIE
GLQKWILNYAKHAKRLASIETDPEQKKEYEEIAEVLENIAHKQPRTFREALQMTYLLHIAVVNEDAISGL
SPGRIGQVLYPWFEQDIENGRITEEEVIELLELYRVKITCIDCFASAGVVGGVLSGNTFNNLSLGGLNRD
GKSAANRLEYLILEAGIRCQTPQPTLSVLYDEKTPEDFLMKAAECTKLGSGYPAWMNNQTGMEFMLRQYG
DEGMTVEEARAWALGGCLETSPGCWKPLHLNGKVYWIPGGAGQPTSVGVHFIANPKVLELVLTNGVDKRT
GLQVFPPHNKKLETYEELVEQFKAYYEKTCDVLNRCNNIQHDIWRKFNMSIVNSLLKPDCLDKGQHIGNM
GYRYNATFNVESCGTITFINSLAALKKLVYDDKKYTLEEMTDAMLNNFGFKTAYEVGSFSLADQEKTDDS
GKYDKIHADCLNAPKYGNDDPYVDNILKDYEDWFCDVCPTYESLYGKPLYACQISVSTHGPQGAVTLATA
DGRLAGTTYADGSMSAYPGTDKNGIYALFESATVWDHSMSQNSQMNLKLHPSAVKGIEGTRKLLDLTRAY
MRKGGFHIQYNIVDSKVLKDAQAKPENYRDLMVRVAGFTQYWCEIGKPIQDEVIARTEYEG
>gnl|CDD|411304 NF033716, glycyl_HPDL_Sma, 4-hydroxyphenylacetate decarboxylase small subunit. 4-hydroxyphenylacetate decarboxylase, an enzyme with a glycyl radical active site, depends on a radical SAM enzyme for activation, and is found in strict anaerobes such as Clostridium difficile. It has a large and a small subunit
HSDCKNYIPLDVEKGICRLTGQIVLIDSEACPEFEPAPKCKFCKNFCDPDKYGIGTCKGLEKEYWAYATM
GASTCEGFE
>gnl|CDD|468152 NF033717, HPDL_rSAM_activ, 4-hydroxyphenylacetate decarboxylase activase. 4-hydroxyphenylacetate decarboxylase activase is a radical SAM enzyme, found in anaerobic bacteria where 4-hydroxyphenylacetate decarboxylase occurs and required to prepare the glycyl radical active site of the enzyme
QLKGLIFDIQSFSVHDGPGCRTLVFLSGCPLRCEWCANPESWEKKKHIMFAEGKCKWDKGCRRCRDACPH
GAIRFNDDGKPKIDWEICEDCTTFECVNVCPNDALKQCVKEYTVDELMKILKRDRNNWGSDGGVTFSGGE
PLMQHEFLLEVLKKCKELNIHTAIETSAFASEEVFLKVMKYIDFAFIDIKHMDREKHKEGTGVGNELILS
NIEALANSNWQGRLVLRVPTIAGFNDSVENASKTADFMNENGLYEINLLPFHRLGESKWEQLGKEYEYTN
DGDTSPEKLEELQDIYLDNGIACYVGSDTPF
>gnl|CDD|468153 NF033718, indole_decarb, indoleacetate decarboxylase. Indoleacetate decarboxylase is a single subunit glycyl radical enzyme that depends on a cognate radical SAM enzyme for its activation. It performs the final step in the anaerobic fermentation of tryptophan to skatole, a malodorous volatile compound
LETGKTATWPPTSEEQEESGFVQKEVKGQPSTDRTKRIKQRFLNAKCMLDPEFPILYTKAWREYEGKPLY
IRRGLSYKYMLENLTPVILEDELITMSKTRYTRGATVYPQFSTKFMISFLSQAEDKEEAKLYSVGGGDEA
HHVEEEGWIQVGQLFSIREEEVAPMLDCLEYWKTRCIEDVSEKFMKESFPYYEDLNNAKKVGLFPGSGLH
SGCDGRWVPAYDIAVERGLEDVIEECKEHIANTLPTTKEVAEKVFFWQACIYACEGVINWAKNYAKKARR
LAETATEPRKKELLEMAERLEWVPAKPARNFMEALQAAWTGHIAVGSDSLALGLSPGRWGKLLYPYYKKD
LEEGKITKGQALELMELIRIKFSSEEYITPSAWAAMASSNSFQHMVVGGLDPKTGKCTDNELEELILEAG
INMPTPQPTLGILVSSKTSNKLLMKAAECTKAGNGYPAWFNYDMMVQHLLWCHREEGITLEDARDVAIAG
CVEIGMQGTGHGIAHPAFYNEGKTLELALNDGVDPRTGIRCFDGLGPIKTYQDLWDNFCKIREHYMKVYM
RYWNYVVACQREIHPKIMGSVLMHDCIKTGRPVDNNGCRYNKSVTLLDSGTVNVANGLAAIKKLVFEDKK
YTMDEFKEALDNNFGFELGAEKGNFSMLNQEIDPRIHMKYAKIHRDILNAPKFGNDDDYVDDIFVDLWQD
YDRVCASETTYLGYRWITAALSISAHGPHGRVTGATPDGRLAGVTLCDGILSASPGTDVNGPIALLNSGV
KLDSTEMRSVQLNMKFHPNAIRGDEGSKNFVDFIRSYFSMGGYHVQFNIVDSKMLRDAQKHPENYRDLMV
RVAGFSAYWVELGKPIQDEVIARTEYNS
>gnl|CDD|411307 NF033719, ind_deCO2_activ, indoleacetate decarboxylase activase
GTVFDIQSFSTHDGPGIRTNVFLKGCPLKCPWCANPEGQKGTPELLYTKMKCVGCMFCVKVCPHKAITAV
TDPEENAKYIKIDRSKCDKCTTHECVNACFNEALSVAGELMTVDDVMKKIERDSVYYRAKGGVTLSGGDP
LLQPDFALELLKACKEEAINTAIETELCVPPENIERFIPYIDLFLTDIKIMDPEKHKRITGVSNDVILKN
IRLIGERCKRILLRIPIIPGYNDDDENIDGTAKFAAENHISTINILPYHKLGVSKYERLGSTYLLPDVQP
PSADKMRELKDIIESHGVKCII
>gnl|CDD|411308 NF033720, DbpB, decorin-binding protein DbpB
MKKLNLIIVALFFALLVACNFGLTEETKAALESSSKDVKNKILQIKKDATDKGVNFAAFTDSKTGSKVTN
GGLALREAKVQAINETEKFLKIIEEEALKLKENGNSSQFLAMFDLMLEVLESLEAIGIKGVKTSISEEAK
SNPINTAERLLEVKVQIENKLEVVKKKQNLENEEKKINKSKK
>gnl|CDD|468154 NF033721, P12_lipo, P12 family lipoprotein
LFLYMLLLIGLLSCNLDSKLSNNKREQKNNNNVKEFLESVQEDGLNNLYGNQEKQKDFIKNFEELKYEDL
VVPVGPVVSSKSSNNKINIPNISYNHQEKKEIKEEDLIPSTDEEKRADKAIKDIENILGDSGFDKLIEDV
RKLKDEYALIESSFYDVILKIQNKKTSLMKNNRNNRIKIRELIQLLQNLLKIRGEIDELMNKIDSAENEI
RSAAYFFEKAQKTLKEAIIKRLESKNKRSYASNLARQALSEAESALNQLESSSSKIGEAMGRKEEIKELI
EHAKSVL
>gnl|CDD|411310 NF033723, S2_P23, S2/P23 family protein
VTWIKSKALMEIKDENGNLIKELKGLKYSYIVSPIKNDNNYSNYIMPIILFETTKEGDKKYEITSFKLIS
EGSNLDFNQNKGNFLNKLPLKEKSKEEGYINAYPFGILNANSLIKAFKSLYKNGNWSYMLAEITVKNKQT
KKTKTYEISLDSKLFNDFIKLILKKYPNLKTAKLKFFID
>gnl|CDD|411311 NF033724, P13_porin, P13 family porin
MNKFLIFVLVTFCVFSSFAQAKDSKSAFGLGAGEKLLKYETKKKDPLVPFLLNLFLGFGIGSFVQGDILG
GSLILGFDAVGIGLILTGAYLDIKALGFNTKKAAFKWTWGKGMMLAGVVTMAVTRLTEIILPFTFANSYN
RKLKNSLNIALGGFEPSFDINMGQASALGFELSFKKSY
>gnl|CDD|411312 NF033725, borfam_49, chromosome replication/partitioning protein
YNSLKEQLKINLKDEIYNKIETMKILKEIKDKKLYKLDGYKSFEDFIKDYKIAKTQAYLYLKIANAILEG
IISEEYIKENGIRETLRFLKNKESITIKKSKQNPIKPLRFQLKDQESYDFYKSNAKFTSFILDELFENKK
DLLNKLMKEY
>gnl|CDD|411313 NF033726, borfam52, P52 family lipoprotein
MRILVGVCIITLALLGCYLPDKQEQAVQTFFENLESESYDMGSDEIVTEGIFSNLKLYASEHRLLVDIKK
TLISLKDPNYRDVPPVPDYNEEYFNKFFLDLGSERSKELIKLFGRVKNEQNNKFKHEVYWLYSCIRELYS
PDIKYSGEGGHEYYVNFMPRPTIDQQYLKVK
>gnl|CDD|468155 NF033728, borfam54_1, complement regulator-acquiring protein
KLLIFIKLGILFLFSCTLDANLNEDYKNKVASFLNTTKDEQETISINTKSNATKNIPNADAAELKKQSQA
APQKGLQNQEQAASTKDLKILSFKANLKNLTSLIDKLQELKNRLIRIIKEEKLQTQNNGFRETYDQFGMK
DSMFELIDVISNDSVYDRSLAPKLNSNTPEAENERRQFYASLSFDTTKIFNFGEIMNKLYKEPQNHDLIK
SLISSGLGIQISFEVALEEIAIKIEIFKQNYLNTKINSFDFKNKLEELYSKLNDILEEKKEWLNTIETLI
KSSNANLELQNSEKLAEYIQNRYKDKMQNARQKSLQTYI
>gnl|CDD|411315 NF033729, borfam54_2, complement regulator-acquiring protein
MKKTKLNIIKLNIITTILTLICISCAPVNKIDPKTKSNTNSKENTQNLENKSQDLKSSNQKSQQETIISK
LKAIGKKLEAQKKEEDIQIAKIDAEQFDFLGTFKADPYDLFDENEKMKIKRIIYSSLNYEKEKILTLKEI
LEKLKKNSEHRNIVKRFLYNISLSIQLQLEEHLKLIQDKLHTLSKENLEELLMDVESDLKLKEKFKKTLN
KTIEAYNQN
>gnl|CDD|411316 NF033730, borfam54_3, complement regulator-acquiring protein
MKKNTIYKILKLFKITLLFSCSFYSKSNNTEATSELQPNPIEIKKTGIKKEENLKKIQNLQQNQLLNNEK
ENIIKKITQEFNENEKLIQKIGPNIEIFAQKINTDIQKIEPIDQFGINKNTFPEKQDMNIDAMLKDNQFR
RLFYSSLNYDENKIKKLITILAQTSSSNGYHYRVIGLIFWTGFKIQESFEKAVNLLTKNEQRRLMFNFRT
KTVKDIQENFEKLIQERNSWIKTVENIISEYDNNIAGVKADGIILGEIIRVGYEHKLNPNESMQILNDIE
TLLKACCDHIHY
>gnl|CDD|411317 NF033731, borfam63, fibronectin-binding protein RevA
MKNKNIFKLFFVSMLFVMACKAYVEEKKEIDSLMTDVLALNNDSSGEKFKDYKDKINELKESLKDVGNAE
LKEKLLNLQSLFQDKLAAKLAALKAAKQTIEGITDKDQSTAKTKIWAEAKLVGVTVPFSGSNTSGKGQEM
SKNAVEQIDKIIKFLEEGTN
>gnl|CDD|411318 NF033732, borfam95, exported protein A EppA
MKKISLLLFLFLFILSADLDAFLSANIEKNYAKAKKAFSKEDFNLIKKRLDNYDFKSEYEKSVFFAFAPE
IRGSLRKIGIKEKSVFLDALDVIGYLIKNKIDTDYLKFESYDIISLINGYPDQIFDYLIQLDSDKIDYAE
KYGDKARENFEESYSKDKINTVKQILKQILADLPKD
>gnl|CDD|468156 NF033733, MFS_ArsK, arsenite efflux MFS transporter ArsK. ArsK, a major facilitator superfamily (MFS) transporter, was shown in Agrobacterium tumefaciens to be induced by arsenite and antimonite, to reduce their accumulation, and to confer resistance when expressed heterologously
PIAAIAALGLTQIIGYGTLYYSFSILAPDMARDLGWSTEWVFGALSAALLIGGLSAPWLGRWIDRFGAGR
VMTIGSALAAAALAACALAPGKAVFVLALIALEIASNLVQYGAAFALLVQIRPRVAQRSITYLTLIAGFA
STIFWPITTALHAHLSWREVYLVFAALNLLVCLPLHAWLSRLGRRHSRRAPATRPAEPVEGSLPPHARRR
GFLLMVTAFALQSFVLAAILVHMVPLLGALGLGAAAVVVGTLFGPSQVLSRLINMVFGKNLSPLHLAVIS
AALIPAGLVILLLTAPSLPGAMAFAVLFGLGNGLNSIVQGTLPLALFGSEGYGALQGKMMAARLIVSATA
PFAFALAMENLGVSWSLGITAALGALAVAAFVAIALLR
>gnl|CDD|468157 NF033734, MFS_ArsJ, organoarsenical effux MFS transporter ArsJ. ArkJ regularly is encoded next to a glyceraldehyde-3-phosphate dehydrogenase that can synthesize 1-arseno-3-phosphoglycerate in the presence of arsenate, and appears to provide arsenate resistance by exporting that organoarsenical compound before it spontaneously dissociates into arsenate and 3-phosphoglycerate
RQYLLVTANYWAFTLTDGALRMLVVLHFHQLGYSPLQIAMLFLFYEFFGVVTNLVGGWLGARFGLNRTLN
IGLALQIVALLMLTVPDPAWLSVAYVMAAQALSGIAKDLNKMSAKSAIKLLVPEDAQGQLFKWVAILTGS
KNALKGVGFFLGGLLLALLGFQGALLAMAALLALVLLLSLLLLPKDLGKAKKKPKFSELFSKSRAINILS
AARLFLFGARDVWFVVALPVFLYSVLGWDFWQVGGFLALWVIGYGIVQALAPKLTRRSSGSKAPDGRAAR
LWALLLALVPALIALALQLGGWPPTIAVLVGGLLLFGAVFAINSSLHSYLILAYADSDGVSLDVGFYYMA
NAAGRLIGTLLSGLLYQVGGLEACLWVSAAFLLLAALISLKL
>gnl|CDD|468158 NF033735, G3PDH_Arsen, ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase
IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRIS
FSSNKDIEDTPWGDGVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDPAR
HRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSA
TAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSV
DYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANRMVDLA
>gnl|CDD|411322 NF033737, Amm_Lyn_leader, ammosamide/lymphostin biosynthesis leader domain. Precursors of the ammosamide (Amm6) and lymphostin family of natural products share both a strongly conserved leader peptide region that interacts with natural product biosynthesis enzymes, and a critical Trp residue at or near the C-terminus that is incorporated into the small molecule natural product eventually produced - a pyrroloquinoline alkaloid whose core is derived from tryptophan. An additional, shorter homolog, Xan, encoded in a less well understood natural production biosynthesis locus, lacks the critical Trp. It is thought to be a trans-acting leader peptide that does not need to be linked covalently to a core peptide, if that is the substrate of the natural product biosynthesis enzymes, in order to enable them to perform their modifications
VEDLDDLDDIDFDLEEVENKIAPLALA
>gnl|CDD|468159 NF033738, microvirid_RiPP, microviridin/marinostatin family tricyclic proteinase inhibitor. Members of the microviridin/marinostatin are ribosomally translated peptides whose post-translational processing converts them into tricyclic depsipeptides that serve as serine proteinase inhibitors. A single precursor usually has one core peptide region near the C-terminus, with a nearly invariant TxKYPSD motif, but may instead have two or three repeats of the core region
PFFARFLEKQIKDPEKVKGGDTVTSPSDDTVTPPVVTMKYPSDGDED
>gnl|CDD|468160 NF033739, intramemb_PrsW, glutamic-type intramembrane protease PrsW. PrsW, an intramembrane protease, cleaves the anti-sigma factor RsiW, which regulates the activity of the ECF-type sigma factor SigW
LALLSAAIAPGLALLSYFYLKDRYETEPISMVIRTFIFGALLVFPIMFIQYVLQEEGLGDSPFLQAFLIS
ALLEEFFKWFVLYFTIYNHVEFDEPYDGIVYGVAVSLGFATLENILYLLANGIEFAFLRALLPVSSHALF
GVIMGYYLGKAKFSTSKKKRKYLLLSLLLPFLLHGIYDYILLTQQYWLYFIVPFMIFLWWFGLRKVKRA
>gnl|CDD|468161 NF033740, MarP_fam_protase, MarP family serine protease. The founding member of this family of membrane-spanning serine proteases, which is restricted to Actinobacteria, is the acid resistance periplasmic serine protease MarP of Mycobacterium tuberculosis. Recent work shows that MarP is required to cleave and activate the peptidoglycan hydrolase RipA, and loss of RipA activity creates a defect in progeny separation during cell division. Therefore, the requirement for MarP in order to survive acidic conditions may be a consequence of peptidoglycan hydrolysis requirements, explaining why MarP family members are distributed more broadly in the Actinobacteria than the subset of species capable of surviving intracellularly as pathogens
LDLLLVVLALLAAISGWRQGFVASVLSFAGVVLGAVAGVWLAPLVVDLVDDGAWRLLAALGVVVLLVVLG
QALGSVLGRALRRRIRWRPLRAVDSVLGAVLQVVAVLLVAWLVASPLASSGLPGLAQAVRGSRVLGTVDR
VMPDPALRALPSLRALLDDSGFPQVFGPFGRTPIPEVEPPDPALATSPAVRRARPSVVKVRGTAPSCGRA
LEGSGFVVAPDRVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIAVLAVPGLGLPPLPFADEPAE
TGDDAIVLGYPEGGPFTATPARVRERIALSGPDIYGSGTVTREVYTLRGTVRPGNSGGPLLDPDGRVLGV
VFAAAVDDSDTGYALTADEVRPDLAAAAALTTPVSTGACV
>gnl|CDD|468162 NF033741, NlpC_p60_RipA, NlpC/P60 family peptidoglycan endopeptidase RipA
AVPLSAALLLSTPGVAGGLATAQPAPPDTIAALVADVAEANQRLQDLGAAIQAEQESVNKAIVDVQTARD
AAAAAQREVEASQQAVKDANTAIAAAQKRFDTFAAATYVNGPSSSYLTASDPEDILATASAGQTLALSSQ
QVMADLQRARTEQVNKESAARLAKQKADQAAADAEASQDAAVAALTEAQQTFGEQQAELDRLAAERDAAQ
ARLDAARPVSATSAPAPAAAAGAAPPPGDRWDRGPGSPGPAGGNWDGLWDPTLPMIPSANVSGDPIAIIN
AVLGISATSAQVTADMGRKFLQKLGILPPPDTGITNGRIPRVYGRQASEYVIRRAMSQLGVPYSWGGGNA
AGPSRGIDSGANTVGFDCSGLMLYAFAGVGIKLDHYSGSQYNAGRKIPSSQMRRGDVIFYGPNASQHVAM
YLGDGQMLEAPYTGSVVKISPVRTSGMTPYVTRLIEY
>gnl|CDD|468163 NF033742, NlpC_p60_RipB, NlpC/P60 family peptidoglycan endopeptidase RipB
PDDGQWDPTLPKVLSAGAPGDPLAIANASLQATAQATQTTMDLGRKFLSSLGLGGPPASAAPVAPGRGPR
VRGPQAIEYVIRRGGSQMGVPYSWGGGSLTGPSRGVDSGANTVGFDCSGLTRYAFAGVGVLIPRYSGDQY
NAGRKVPPSQAKRGDLLFWGPGGSQHVALYLGNGQMLEASGTAGKVTVSPVRTAGMTPYVTRIIES
>gnl|CDD|468164 NF033743, NlpC_inact_RipD, NlpC/P60 family peptidoglycan-binding protein RipD. RipD proteins, such as founding member Rv1566c from Mycobacterium tuberculosis, is a catalytically inactive paralog of the peptidoglycan endopeptidases RipA and RipB. A catalytically important Cys and His pair is replaced by Ala-83 and Ser-132
RRIYALVIGLALLGLATPGLASADPVPRPADNQQAIDVVIARALSQRGVPFSYGGGNANGPTRGTGAGPA
ALNLPGAAPGAPGPNVVGFDASGLMVYAFAGAGVKLPRSSGEQYKVGQKVLPAQALPGDLIFYGPEGTQS
VALFLGNGQMLEATDPGVTVSPVRTNGMAPYLVRIIG
>gnl|CDD|468165 NF033745, class_C_sortase, class C sortase
LILLFLVGLGILLYPFVSNYYNNYQQSQAIAEYDKKVAKLSKEEIEKLLEKAKAYNEELAGDGPVVDPFT
SKDEEYAEYESQLNVNETGVMGYIEIPKINVKLPIYHGTSEEVLQKGAGHLEGTSLPVGGKGTHSVITGH
RGLPSATLFTDLDKLKKGDKFYIHVLGETLAYKVDQIKVVLPDDTDKLKIVPGKDLVTLLTCTPYGINTH
RLLVRGHR
>gnl|CDD|411330 NF033746, class_D_sortase, class D sortase
SFQPETGEAIGILEIPKLDAELPIVEGTDEDELEKGVGHYAGTALPGQNDQIVLSGHRDTVFRRLGELEI
GDQLIVETPYGTFTYEITKTKIVDADDRTVIVPKPEETLTLTTCYPFRYIGDAPDRYIIYAKLVS
>gnl|CDD|468166 NF033747, class_E_sortase, class E sortase
VRVLGELLITAGVVLLLFVVYQLWWTNVEADREQDEAADALREQWPPPAPAAPPAADPPPAPGAPAPGEA
FAVLYIPRFGADWAVPVVEGTSLDVLLRGPGHYPGTAMPGEVGNFAVAGHRVTHGAPFRDLDRLRPGDAI
VVETADTWYVYRVVRGLEIVSPTDVEVIAPVPGQPGVTPTGRYLTLTTCHPEFSSTERLIVWGELVSWQP
K
>gnl|CDD|411332 NF033748, class_F_sortase, class F sortase
PAAAPLPRSRPVRLRIPAIGVDAPVVPLGLDADGTLEVPPADDPNLAGWYAGGPTPGERGPAVIVGHVDT
RTGPAVFYRLGALRPGDRVEVTRADGRTAVFTVDRVEVYPKDDFPTERVYGDTGRPELRLITCGGGFDRA
AGGYTDNVVVFAHLT
>gnl|CDD|468167 NF033749, bact_hemeryth, bacteriohemerythrin. Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is named based on its homology to eukaryotic proteins such as myohemerythrin
LITWSDELSVGIKEIDEQHKKLVDLINELHDAMKTGGKGREVLGKILDELIDYTVYHFATEEKLMEKYGY
PDYEAHKAEHDKLVAKVLDLQKKFEAGEATLSIELLNFLKDWLVNHILGTDKKYGPFLN
>gnl|CDD|468168 NF033750, vWF_bind_Staph, von Willebrand factor binding protein Vwb. The von Willebrand factor binding protein Vwb, like its paralog staphylocoagulase, is a coagulase and a virulence factor. It induces clotting, not by being an enzyme, but by activating prothrombin to generate fibrin
MKNKLLVLSLGALCVSQIWESNHASAVVSGEKNPYVSESLKLKGKKSKSWTLEQYKESLDDLISSLSIND
NEGYDEPEYKEAVKKYQQKFMAEDDALKKFFDEEKKIKNYNKNNNTVNNDILGLTHERYEAIYNSLKENK
EEFLKEIEKIEEKNPDLKDFNEEEQYKADVELNELENKVLMLGYTFYNTNRDAVEDLYNKLDMIVGYSDD
ERENKKPTNERMLKEKKEDLETIIDEFFNDIGENRPLNIPALTNEKEKNKEMATKLKADTEAAKTDESKR
SKRSKRSLNTQNHKSASQEVTAEQKAEYEKRAEERKARFLDKQKIKKTPVVSLEYDFEHKQRIDNENDKQ
LVVSAPTKKPTTPTTYTETTTQVPMPTVERQTQQQIIYNAPKQLAGLNGESHDFTTTHQSPTTSNHTHNN
VVEFEETSALPGRKSGSLVGISQIDSSHLTEREKRVIKREHVREAQKLVDNYKDTHSYKDRLNAQQKVNT
LSEGHQKRFNKQINKVYNGK
>gnl|CDD|468169 NF033751, pallilysin_like, pallilysin-related adhesin. In contrast to pallilysin itself (a bifunctional adhesin and protease), members of the pallilysin-related adhesin family average twice the length, lack the HEXXH motif essential to pallilysin's metalloprotease activity, and are likely to function in virulence only as an adhesin. Typical members of this family include TDE0840 from Treponema denticola and BB0038 from Borrelia burgdorferi, which share less than 20% pairwise amino acid sequence identity
PLIPLPSDETLIAVLDVNLDLDGYDEQQIVAVRKSDDPFSIYLIVADYDPIRNKYERSWEIPTEATQPRT
FSLYLMDLTGDHNNEIIYSGMNENGEQTLDIFRKSSSKDGGLSFRSIFDLSADGTIFIQESERSQAYELG
QSNGESFPIWVYESDPESENNLDQIQTTYYWNSEQGKYVLSSEEKIPGERIEEQRLRKLQDGTVETFEEF
LSGLWYRESTNNGGEGRYLFFDPESREIIFYSDDIQEVYEWENSSRTIRNGLYISTQNESIPNIRRRIDI
SLESLDEIRVRVQDDVRRLKIGELWDGTYKKLSPGLQLNLTAKSSPAEASEKLLTLSGGWYKSDDGEELF
FDDPRFTLKTEGKIESGGYSIFTINGNTILQLR
>gnl|CDD|411336 NF033752, linaridin_CypA, cypemycin family RiPP. The cypemycin precursor CypA belongs to the linaridin class (linear "arid" peptide, following dehydration modifications) of RiPP natural product precursors. The signature terminal motif CL[VI]C is modified by decarboxylation of the C-terminal Cys residue, followed by cyclization
PESLAVQAFANSVLADAEPGFHSDSETPAMTTPATVTAAQFVIQGSTICLVC
>gnl|CDD|411337 NF033753, RiPP_decarbCypD, CypD family RiPP peptide-cysteine decarboxylase. CypD, a Cys decarboxylase flavoprotein, oxidatively removes the carboxyl moiety from the C-terminal Cys residue of CypA, the precursor of the RiPP natural product cypemycin
EVGTFEGAELHLHVTGSISAALVPWWIHWLRFINPDVVVNVSVSRNATRFVTVDALRHLANGQVWLDEWD
DPSLPHEWRSGRSGASECFIVFPATLDTVMRLAQGRADSPALMMLQVTDLPIVIADVFPAENEVIEHWRE
ILLLRPNVSFAPRVEGTRATDRSTAESGFNLPGALAVANEAI
>gnl|CDD|468170 NF033754, gliding_CglC, adventurous gliding motility lipoprotein CglC. CglC (cell contact-dependent gliding (or conditional gliding) motility protein C, also called adventurous gliding motility protein AgmO, is found in delta-proteobacterial species that exhibit a taxonomically restricted form of gliding motility
ARLALLLAAALLLAGCEVTTDLGKPCTLVKKAPDEEQEAAGVKFVPILERDIAAGQDFISFGSVECEDLI
CVRDAGSPRSKNPEAEALGYCSKACVQGSSDCEVTDDDVEEGLKTGLSCRPLLLDQATLAALRAADEDFY
RRTFGENNSPYFCARA
>gnl|CDD|468171 NF033755, gliding_CglE, adventurous gliding motility protein CglE
EVERGFYVEADLGGFFTLGPPGEPGPSNAGPYLGLGVGYDLGERLSLGLHFGLGGSAGNCYDYSGGSDGC
LPSGDFSLVFFGAGARYALLGLTKRLYLYAKAGGGYTRLDPSPVLPGDPGRGLSDVNAGAGLGVEYYTRL
RHFSVGLDVDGRYLIGPGIPGLAVYPRVKYTF
>gnl|CDD|468172 NF033756, gliding_GltC, adventurous gliding motility protein GltC. GltC is a soluble periplasmic protein required for a type of gliding motility found in certain social delta-proteobacteria, including the model species Myxococcus xanthus
LAWATPAPAQSFEGLDLSGKSKKKKKKKKPSKKADKGKPAPPDDDESSSSAPATSEAPSPAPTAPPAPPV
APAPSPPAQDEETSSGGMGLDLGESPKPPAPTMSFEAVDVSGKTADRQRLDAAVALFKNDEYEAAALAFY
ELLQDPKLAGLHVEARYLLAKSLYRMGLYHSALGEFSKILSRGPQTKFFKTSLEWLFFISRKTVNETVVL
DEIARYANYEFPEKYRDEFRYLLARYHFVRGRALDQAGQADEADKSFEEARRLALTIPRGDPFYPKAKYL
EGLALFRNGKRQGALEAMKEVVRLTRPRRGRTPEEAKLDQSLRELAFMQLARIHYGHRQNRYAIFYYNKI
ERGSEQWLESLFESSWANYRVGQYEQALGNLITLSSPFFRDEYFPEALILKAVIYYENCRYPESRLILED
FERTYGPVHDELDKLTAKNMEAAEYYDVLADVQKKNKEGLEKGETDEILERILKLALTDQDLKKTNDSIL
ELEGEMDSFAERRDTFRYSELAKHLLEGLKEQRTELIQKAGLMAKGKLETELVALKQLLANGLRIKFETT
TKEKEFLEEQLKAGGRVAIVKKYRYSVAVSDDQLYWPYEGEYWRDELGTYQYTLTKGCIER
>gnl|CDD|468173 NF033757, gliding_CglB, adventurous gliding motility lipoprotein CglB. CglB is an outer membrane lipoprotein required for A-motility in Myxococcus xanthus and other delta-proteobacteria. It is transferable between cells that have a compatible TraAB system, and was therefore named conditional (or cell contact-dependent) gliding motility protein B, or CglB
AVASGCQTYDFEPVEPLAIAQTTVETVITARASKPNVMLLVDTSGSMTLPVNPSLPACRVADLQGTGVIC
GEGNPCDTTKCPTRWSELQGAMDSFLTESGTIARFGLTTYPEPQATGGDQCGPATSVRVALPAGDDDDDA
TLQAHANEINAKLQAIPNGGPGGPTGGTPTSGSLRFVGSLPELQDDDRDDFVILLTDGLPNCNEANPNSG
PSAACRCTLANSQCPSSGPYERRGCLDKDASVAAVRALKAKGIQTIVIGFGAETAAGDGPAVLNAMARAG
GFARTCKTDADCGAGDTCDVATGLCGRRFYQAANQDELAAALREISERIVPGEPCLIRLDPSQLPSDPKL
IVVYVNGERTSPGPDTWSLTGPGVRFTGSTCDRIEASTPENPVKVEVRAVRQL
>gnl|CDD|468174 NF033758, gliding_GltE, adventurous gliding motility TPR repeat lipoprotein GltE. GltE (also called AglT) is a tetratricopeptide repeat protein with a lipoprotein signal peptide and a role in A-motility (adventurous gliding motility) in Myxococcus xanthus and other delta-proteobacteria
LLLAAAALLAAGCTSTKAAGPTGPSKTDVGKTGTKPAEPPSISNRAKLLFEDALKAFDAQKKAKAFDYPS
LERKFKAALEADPNLAEAEYNLGVLAERQGKTDEAVARYKAALKKKPTLRQASENLAVMAQNAGDVAGAV
ALYQDVLKRYPDDASSRARLAEIYRQTGDHDKAMELSRAALMRDPQSTTALKVMMRSYLDRKQLAMAKLV
ALRAVKIDQNDPELHHTVGLILLQEGDKDGARLQFKRALEVRADYVPSHVELAQLALDAEDYPGAEEHLR
RILQADGKNAAAHLNLGVAYKGQGQYDKAMQEYDEAEKLDPELAAIYLNRAIILHRVKDAPERAVELYKK
YIAMAGGEVALNAEAPVFGLLREAESVVQAKREAKAAEAQAKQMEELQKQQQAAMKAEEAK
>gnl|CDD|411343 NF033759, exchanger_TraA, outer membrane exchange protein TraA. TraA, together with its partner TraB, mediates a large scale exchange of outer membrane lipoproteins, and lipids, between closely related strains or clonally identical cells, certain delta-proteobacterial species such as Myxococcus xanthus. The exchange mechanism is likely to involve fusion of outer membrane, probably done to coordinate the social behaviors these bacteria display
VVVTGDPVAPSPAQPGTGLCVASNVSTNPAADFPQSRSTYIGGLNTFMEENRNSRVTSVLRTPFDLSNNN
NDGRTLSYGDFVNVVTGCPSGGCDFFINDPSTSFVSRFRGYLNVTPDMVGRPLHFGFYADDAVSLVIYDR
SQRRYQVINRPPQLGAATWRTTNSVTFTQPGLYPVEILYAQITEHAALEMSVLVGTFTDFERPANQPPIV
NLNDSGFTLVQPAQFFQTESGRPSFPDDPNQCEQCNRQFANTPGNGGCGPSYYCNGAALCAPCDSALFCG
PSCSPCGPSTPHCANRNGTFTCVQCTEDSQCPNGRCDLTTNQCRGCNEDSDCVCDEPTFTCVECNTDEQC
PNGQVCATDLNECRECNQDSHCPRGESCSNNTCQPCSTNDSCAGNSCNCCPNGTQCAAPTPGASPSCVEC
TTDSQCADGQRCDTANGRCVDQVPECNTSDRCGPGCVKCPGDRPYCLDGQVCVQCRNDLECGDGQFCLSG
ECASCTTDKRCGPRCEACPGETPFCLTDGTVQGSSCVGCRNDADCGSGTCDPTTRTCSNTGACAVTCAEG
TVCDGAACVECFADAHCPCGGTCDTATNTCTTSCADSGDCLGVEHCSAKTQQCERGRRKPGTEPQGGAFC
CGTTADATPAGSTAFLLLLAAGFLLLRSRRRA
>gnl|CDD|468175 NF033760, gliding_GltG, adventurous gliding motility protein GltG. GltG proteins, including the founding member MXAN_4867 from Myxococcus xanthus, occur in certain delta-proteobacteria and are involved in adventurous gliding (A-)motility. GltG has an N-terminal forkhead-associated (FHA) domain domain, often associated with signal transduction
MAVPLTLKVFKGDELVASKDFERDIIKIGRLASAHLCLDDEKVSRIHSVIEVAADGSLSIIDMGSVEGTY
VNGKRVNKGALSFGDEIRVGGTTIRLENPAAVAAANLAAAVASAAVAAAPAPVVAAPEAPAAGLAQAAAA
PAPAPAARAAPAPQAADASPAPAQAAPVAAPVAAAPAPVHAAPAEPAPRARPVRRSKGSGPLGLSLRFLW
GDQRVGEFFLAPGKKKSFSVGSAEGVDFVMGDSRLGGPPFEVLRTDGQSFTVRFTGKMKGELIRKGETLD
LKAVIESGKASHEGEAYALTLEEDDFAWVDLGGVRLEVCFQPVPKRVFVPLAESVDYTVLNIFLVLFFLA
AMFVIGAANRAADGDAFADELFGNNARLAKLIIKPPETQKNPFLEKLNQQKKESGEKAAKAKGEEGQMGK
KDAPKTNARAAPKADPNKKEEAKNLALKIFGGGKGGLSTLFGSAGLGGDLKGAMGNMFGAAVGDAGGFGG
LGLRGSGGGGGGSGDTIGIGAIGTKGRGGGTGGYGSGVGGLGGKGSVDVGIASSEPVVMGSLDKELIRRV
IQRNRGQIRYCYESQLNRNPKLAGKVAVKFVINPEGSVASSSVAQSTTGNAELEQCVAGRVRTWQFPKPK
GGGVVVVTYPFIFKQAG
>gnl|CDD|468176 NF033761, gliding_GltJ, adventurous gliding motility protein GltJ. Adventurous gliding motility protein GltJ, also known as AgmX, occurs in delta-proteobacteria such as Myxococcus xanthus
MRFVCDSCRAQYMISDDKVGPKGVKVRCKKCGHVILVRPAGAARPKEDGAEAAAAGGAASAANQTANAEF
ALPASLGTPPEGGLFTGVEDDEIGAVFDQVLSSGSHKIPAGEAADEAAAKGAAAEAVRKLAEAEATAAPA
EEAPAAAHEWYVAIDEKQVGPLTLEKVKDHWDRGEVGPDSLCWRAGFSDWIPLSEVAELASVLAPRPAKP
VIVAPAPVSSSPPSVASGPVESAFSAGGASKGARAEAPAPEEDVGWKPSAASVLASLVKEENEALSKPPP
APAPVPEREPPSASRLLDLPPPPPEPVSSPSPGAPATGAAPAPMPAAPQPAPAYAQPAPQPYQPAPYPPP
GYPGAYPPAAVAPGAGGKRGLIVGIVAGVLLLVGGAGAGFWAGGRSQPPPTPAPVVAPAPPPAPAPPPPP
PPAAAQPPPPPAATPPAAATAAATPAAPPAAAPAAAAPAAAGTPPAAPAAAPTPPPAPKAAEPPAAAPAA
PARVARPERRTTRRRTSSSRRVPAPTAPVDAEPAPAPKPAPSSSSFGSGDDDFDELFGTKKPKPEKKASS
AKRTAYIPPAPGGGGAVPDRLGQSDIMEVVLANKPAIVKCVNEQKKKDPGLSGKLVMRWTIQTSGKTSNV
SCQTDEFRSTYMATCISGLIKGWNFPKHKKQGDPIDFPFTF
>gnl|CDD|411346 NF033762, social_mot_Tgl, social motility TPR repeat lipoprotein Tgl. Social motility in delta-proteobacterial species such as Myxococcus xanthus depends on a type VI pilus, which in turn depends on assembly of the PilQ secretin complex. Tgl, a tetratricopeptide repeat (TPR) outer membrane lipoprotein, is required for PilQ assembly
MPRILSACSLALALALAGCAHVPTEKERRSSEIHYDLGVQAQQAGHVQDALREFQKALELDPDNPEAHNA
MGILLHLSFRRHAEAIAHYEKALELRPTFSEARTNLANVYLDQGRYDEAIKLYEQVLNDMLYPTPFIAQG
NLGWALYKKGDTARALQNIKAAVTTNPGFCLGYKNLGIIYDETGKTEEACRQFGRYREKCPDVADAYMRE
GVCQAKLGQADAAKQAFATCEAKAKAPEQVLKDDCRRLLEHL
>gnl|CDD|411347 NF033763, exchanger_TraB, outer membrane exchange protein TraB. TraB, as described originally in the delta-proteobacterium, is a protein with a C-terminal OmpA-like domain, and is encoded in an operon with TraA. Together TraAB make it possible for bacterial cells with close enough kinship to exchange outer membrane lipoproteins, such that certain motility defects in mutant cells can be corrected through the exchange. This exchange most likely involves membrane fusion events, as large amounts of lipid are also exchanged, and it is restricted by a bi-directional kin recognition requirement. Among wild-type cells, these exchanges likely help coordinate various social behaviors
ALALALGLATAAAAAQDARFDVQLFRPSGAPQDLVVVGQSRPLSHLSVSGGPYFSYSLNPLVLVPEGGDS
KKISLVGNRLQLDVMASVGLFDWAEVGVDMPLVLAQGGDNLEAIGTEGSVESFVLGDLRLTGKVAIPGLR
RPAEGSGWGAALTLNVSFPTGLQEAFAGDGELTWAPGLVVDYRFESGILLALNGGFWKRPDRVFAGVQWG
DMAPFGLGAEVPILRGSGITAVGMVHGAVGLKKLPGQPRQIPAELLVGLRWYSSTGLTFTVGGGGGCGCS
LTSPTLSFFTSIIWVPAKTREWEAIERFKEPPEPPPPPPPPVDPDGDSVIGEGDRCPDVAGPVENGGCPD
TDQDGDGVVDRLDRCPDVPAGPRGRDGCPLARIDGNKIVILEQVNFATDQDVILSESFPILEEVARVLLE
HPEIDRVLVEGHTDSRASDAYNLDLSRRRAASVMRFLLESGVAVERLCSQGFGRSRPLADNDSEEGMALN
RRVEFTIQPPSDGPRPPCPEDPAAKKKKPPTK
>gnl|CDD|468177 NF033764, gliding_CglF, adventurous gliding motility protein CglF. CglF, as originally described in Myxococcus xanthus, is a gliding motility protein. It has the property that motility in a cglF loss mutant can be restored by close contact with compatible kin strains where cglF is wild type. The restoration of motility depends on bidirectional kinship recognition, which is mediated by TraAB and leads to exchange of outer membrane proteins and lipids. This cell contact requirement leads to the gene symbol, cglF, meaning conditional (or, cell contact-dependent) gliding F. This protein has also been called GltF
RKLLLLAAALALAAALAQDESAAAQAGEGGVEYKKKTVINFEDDTIEGDLTRPDGEYVEARKRVKHSNLI
RIREDFRDKVLQSVGEL
>gnl|CDD|468178 NF033765, gliding_CglD, adventurous gliding motility lipoprotein CglD
MRNPLKRLFACALLAASLLAGCGGGPDPDPDPQPTGDGGTSDGGPDAGDEEDAGVDPDPDPDPGEVPTDP
RDPDNKTKDSDCDGLTDAEEFANIYAGGLKTNPGLRDTDGDGIRDGVEVGRTSSVNPLCSFIADQDPTSR
TSPVKADTDGDGIPDGLEDRNRNGRRDPGETDPNAIDSDGDGLSDGEEDTNKNGIVSPGETDPRKRDTDG
DGLSDGLELKTGTDPLKPDTDGDTCSDGDEDRNRNGLVDPGETDPKVADCAASIPDADFDGIPDSVEVAT
GTNPNNADTDGDGLPDGVEDRNRNGRVDLGETDPRLTDTDCDGLQDGPGRNGFLGEDLNANGGVDPGETD
PTNPDTDGDGLLDGLERGVTTAAAPRKTCGYVGDADPGTKTSPTNADSDGDGIPDGAEDSNQNGRVDPGE
LNPSNPADGASTTPAGQACSVQNLRTVTFKEDNGADIRLALPPTFKDANLKTISAGGATVGVIGYDDTKQ
VTFIAYKRGQVGNSTTPTGDEAGIRGASLNPATRDFYQTFTTWDGYPALQARYEMSGTSDLKAFTNTLAR
SLVPASTGTLTGTAGVSGPFKIQAQYVHRSNQSVLVVLAITPTARYNEAGSLFTMSDTAGGSALAQFGDA
DAVQCETFTSATAVVDFLFVVDDSGSMASSQAALANAATAVANKLGNSTLDWRLAMVTTSYTGGNSSNRG
LFRGFTRNINQFKAWLTQNAPCGAGQCSGVTIPPGTAPTTCSANTGCWVGTGGNGSERPLEAARKAINYL
ASAGTTVATRIRPGAKVVVVILTDVRDQSTDTIDTYSQYFKGTGTTATTKNPTGQAIQVHGIICPPEGAT
DTSTWCSSQEDPRNPRHLDIIQATGGVVGSIRDSASITTTINAIVDSVIASVGYKTLKPPIGASLKVAVA
AVADASKCPTPSDLPRSRTNGFDVDGISRTLSFYGACRPQEAGTTQAALSYRYWSDRTTNANGNPPPCYS
DTPYYDPTQADFCKGKLVCNRTTDKCECPADCGGGGAPGQVCNTDRAVCAFTCAPDCGGTCGTFETCNTS
TCACSCVQSATCAPGFKFDATACGCVCDTGALNCGSNYQADANACACACKDDCGGCGAGTKCNVSTCACE
GIIG
>gnl|CDD|468179 NF033766, choice_anch_G, choice-of-anchor G family protein. Choice-of-anchor proteins belong to homology families in which various branches carry C-terminal sorting signals known, or suspected, to be processed by transpeptidases as sortase, exosortase, archaeosortase, rhombosortase, or the type 9 secretion system sorting enzyme. Members of this family, called choice-of-anchor G, included sortase and exosortase targets, and are likely to be found on the cell surface
DVSEAEGRFLSGSLLGTDLDDVAALAGAYAANDGTPSAPVTDTNPLDVSALGALNVDLGGGLQLLGPNGL
LQLGAVNQYASAPDDGSSAAASGAVSDDGAIGVGTPGPGSPPGPATLDLTPLLGGPGLTDALDDLSLELG
AVAASAEQTADGAPTGDYGIAGAGLTLTSPLVGGLVGTLNTAVGTLDTTVNGLGGPDGLLAGALDGLLLL
LLGLLLLGGSGGTVTVTGTLDLQAAVAPLLAEPLTDGGVTIDLATGTITVDLAALLGGGGGALNGLPPNT
EL
>gnl|CDD|411351 NF033767, exosort_XrtS, exosortase S. Members of the exosortase S family occur in the high GC Gram-positive order Micrococcales (a branch of the Actinobacteria), in genera such as Arthrobacter, Microbacterium, Curtobacterium, and Paenarthrobacter
RVALALLLLAAAALLVVFQAAFRAAEAALTAAVLDLFTPGRAAAAGSIVYFGIGTGEPYGLDITTLCSTV
VLVVPLLLLAGALLLIGRFRVGRVLIGLIVALGIVVACNLLRFLMIALALQRWGQQGFDLVHHYLGSIFV
ILGFAAAIIVLLRIA
>gnl|CDD|468180 NF033768, myxo_SS_tail, AgmX/PglI C-terminal domain. The AgmX/PglI C-terminal domain described by this HMM (myxo_SS_tail) occurs as the C-terminal domain in multiple proteins per genome for a number of species capable of surface gliding motility, e.g. 12 in Myxococcus xanthus. Member proteins include the adventurous gliding motility proteins AgmX (GltJ) and PglI in M. xanthus. The domain is about 92 amino acids long, and features a pair of Cys residues about 45 amino acids apart in almost all cases
LDKEAIRRVVRAHLGEIRYCYERELKRNPSLAGKVVVEFTIGPSGRVSSVKVVSSTLKDPKVESCILRRI
KRWRFPKPKGGEVTVTYPFIFS
>gnl|CDD|411353 NF033769, after_VWA_1, after-VIT domain. The after-VIT domain is a bacterial surface protein C-terminal domain found on some proteins that have both the Vault protein Inter-alpha-Trypsin (VIT) domain and a von Willebrand factor type A domain. Note that some of after-VIT domain-containing proteins, such as members of TIGR03788, may have a known C-terminal sorting signal, such as LPXTG or PEP-CTERM, instead of the after-VIT domain. The after-VIT domain appears to be homologous to the myxo_SS_tail domain, some of whose member proteins are involved in adventurous gliding motility in Myxococcus xanthus, and it is similarly located
IQVVSVTGLDEAAIADLTQHLQSLNLPAGFSGELVFELQVSKGRVRRVVLDEEASTLKDKAVIDLIRRSL
LTWRVPQSLTGTVRLTLRIQ
>gnl|CDD|411354 NF033770, exosort_XrtT, exosortase T. Exosortase T is a variant form of exosortase, typically found in Alphaproteobacteria in genera such as Pseudovibrio, Labrenzia, and Ruegeria. Members of this family may be dedicated enzymes, processing a single substrate encoded by a nearby gene, rather than processing multiple proteins like exosortases A and B
WLGLALASAILAIEPIRWLVRTWRDPSYQSNGALYLLLVAGLLLWSLASPVAPVAPGHRQVAFLLLLLAA
LIRLLGQVLAINVLGALALAVDVFALALLLRLGERKRALSPFWLAVLFLFALPLERILQRTLGFPLQMIS
ADLACGLLSLFFPDVSCEGVRIQLAGRDVLVDLPCSGASGLLLLLALFVALNALYRPRLLQALLGLLATL
ALAVLGNSLRISLLAIGLAYPEAVGGIDVMAEPLHDLIGLLTLALSALPVLLFYRPRPAPSVSSPAPAPA
PSLPKPLRAPVALAFLALALAIVSLPRQPVDVSRPVTPPPLPAQLAGFRGQPVALTPVEQAYFTAYGGTA
QKAQYGPMGLNLVRTSSPLRHLHAPDECLRGLGYSVRFLGTRFEPLPTAVYRATGPDGQQWRVAVSFVSD
RGEVTPSVGEAVWLWLNGPGRTWTSVQRITPWSLPESQRADFEAAALAALDL
>gnl|CDD|439417 NF033771, colonize_BriC, biofilm-regulating peptide BriC. BriC (Biofilm-Regulating peptide Induced by Competence), as characterized in Streptococcus pneumoniae, is a cell-cell communication peptide, or peptide pheromone, that is induced by expression of ComE (a master regulator of competence). BriC contributes to biofilm formation, and to colonization in a mouse mole
MTGTETFTVLSTEDLEQTSGGLAVWEDGYGRWLYYREFAPYMGQGALNSYRDAWKYGFRA
>gnl|CDD|468181 NF033772, pheromone_VP1, peptide pheromone VP1. VP1 (virulence peptide 1), as characterized in Streptococcus pneumoniae (a.k.a. pneumococcus), is part of a large panel of secreted regulatory peptides with paralogous leader domains, typically ending with the cleavage site GlyGly, but with highly variable core regions. VP1, along with other pneumococcal peptide pheromones such as BriC, participate to cell-cell communication to regulate pathogenic processes such as biofilm formation
MLNLQFAETMELTEAELEKVYGGDLVYNANIPGGGNWGGLGTPWSITNFWKKYFNHDSSTVNRRR
>gnl|CDD|411357 NF033773, tellur_TrgA, TrgA family protein. TrgA, a protein associated with tellurium resistance (but less critical to the phenotype than TrgB, encoded by the adjacent gene), is the founding member of a family of hydrophobic proteins, about 150 amino acids in length, probably embedded in the membrane, and possibly involved in transport
PTAAKLVAALLFAALAWLASELVKPLLPEGTDFGYFSPVNAAIGLLCGWRVMGRRAGRGYSAAIGNGLTG
AAALVFWALFVQSFYEMLRRSLRRRYDGPMEALVAVFEIMVEYGLLLLTPPVIGTLLVGGVVAGLLTEWA
ARRWR
>gnl|CDD|468182 NF033774, phos_trans_PitA, inorganic phosphate transporter PitA. PitA is a low-affinity transporter for inorganic phosphate. It imports phosphate complexed to divalent cations such as Mg(2+) or Ca(2+). Loss of PitA function can confer reduced sensitivity to high levels of Zn(2+). The PitA of Escherichia coli has a closely related paralog, PitB, that is functional but only minimally expressed. Note that the term PitA is used broadly. This exception-level HMM identifies a rather narrow clade of PitA transporters which, however, includes both PitA and PitB of E. coli K-12
MLHLFAGLDFHTGLLLVLALLFVLFYEAINGFHDTANAVATVIYTRAMRSQLAVVMAGVFNFLGVLLGGL
SVAYAIVHLLPTDLLLNVGSAHGLAMVFSMLLAAIIWNLGTWYFGLPASSSHTLIGAIIGIGLTNALMTG
TSVVDALNIPKMISIFLSLIISPIVGLVLAGGMVFLLRRYWSGTKKRRRIHLTPAEREKKDGKRKPPFWT
RIALILSAIGVSFSHGANDGQKGIGLIMLVLIGVAPAGFVVNMNASGYDITRTRDAVNHLQQYYQQHQDA
LTHVIDLTPPVPTPPETVGGQPKEFHCDPSRAMDAINRAKGLLNNLQSYDDLSVDQRSQMRRLLMCISDT
ADKVAKLPETSADDKRFLKKLRKDLLSTVEYAPIWIIVAVALALSLGTMIGWRRVATTIGEKIGKKGMTY
AQGMSAQMTAAVSIGVASYTGMPVSTTHVLSSAVAGTMIVDGGGVQSKTVKNILLAWVLTLPVSILLSGG
LYWLALKLI
>gnl|CDD|468183 NF033775, P_type_ZntA, Zn(II)/Cd(II)/Pb(II) translocating P-type ATPase ZntA
MSTPETKGKKVPQFSAFKLSPAPQKADDCCCDGACESQPTAAEPESGTRYSWVVNGMDCAACARKVENAV
RQVPGVNQVQVLFATEKLLVDADNDVRAQVESAVRKAGYTLRDENAPAEEKTSRLRENLPLITLIIMMAL
SWGLEQFNHPFGQLAFIATTLVGLFPIARQALRLMKSGSWFAIETLMSVAAIGALFIGATAEAAMVLLLF
LIGERLEGWAASRARQGVSALMALKPETATRLRNGERETVAINDLRPGDVIEVAAGGRLPADGKLLSPFA
SFDESALTGESIPVERAAGEKVPAGATSVDRLVQLEVLSEPGDSAIDRILKLIEEAEERRAPIERFIDRF
SRIYTPAIMAVALLVALVPPLLFAAPWLPWIYKGLTLLLIGCPCALVISTPAAITSGLAAAARRGALIKG
GAALEQLGRVRQVAFDKTGTLTVGKPQVTAVYPAAGISENELLALAAAVEQGSTHPLAQAIVREAQSRGL
AIPAATAQRALAGSGIEAQVNGERVLICAAGKFPAAALAAQIQQLESAGQTVVLVVRDGTLLGVLALRDT
LRDDAREAVAALHQLGVQGVILTGDNPRAAAAIAGELGLEFRAGLLPADKVRAVTALNAHAPLAMVGDGI
NDAPAMKAATIGIAMGSGTDVALETADAALTHNRLTGLAQMISLARATHANIRQNIAIALGLKGIFLVTT
LLGITGLWLAVLADTGATVLVTANALRLLRKK
>gnl|CDD|411360 NF033776, stress_YhcN, peroxide/acid stress response protein YhcN
MKIKTTIAALSLLSVLSFGAFAAQSVNAEQAQNLQSMGTISVSGVGGSPMDIRQALSQKADEQGASAYRV
IEARNGGNWHATAELYK
>gnl|CDD|411361 NF033777, M_group_A_cterm, M protein C-terminal domain. M protein (emm) is an important virulence protein and serology-defining surface antigen of Streptococcus pyogenes (group A Streptococcus). M protein has an amino-terminal YSIRK-type signal sequence (associated with cross-wall targeting in dividing cells), and a C-terminal LPXTG domain for processing by sortase and covalent attachment to the Gram-positive cell wall. Past the signal peptide, M protein has a hypervariable region, but this HMM describes only the well-conserved region C-terminal to the hypervariable region. It discriminates M protein from two related proteins, Enn and Mrp
EAELQKLEEQNKISEASRKGLRRDLDASREAKKQVEKDLANLTAELDKVKEEKQISDASRQGLRRDLDAS
REAKKQVEKALEEANSKLAALEKLNKELEESKKLTEKEKAELQAKLEAEAKALKEQLAKQAEELAKLRAG
KASDSQTPDAKPGNKAVPGKGQAPQAGTKPNQNKAPMKETKRQLPSTGETANPFFTAAALTVMATAGVAA
VVKRKEEN
>gnl|CDD|411362 NF033778, trans_TimA, TIM44-related membrane protein TimA. TimA was first described in Caulobacter crescentus, a member of the alpha-proteobacterial lineage that gave rise to the mitochondrion. It is notable because of homology to Tim44, a protein involved in protein translocation in both human and yeast mitochondria, although TimA itself is not considered involved in protein translocation. TimA is found localized to the plasma membrane, on the cytosolic face. The mitochondrial homolog, Tim44, is found as a peripheral protein of the inner face of the mitochondrial inner membrane, and serves as an adaptor to recruit other subunits into the translocation complex, rather than in transport channel itself
ELIIFAALAAVVLYQLYAVLGRRVGRQPEDAPAAEPAPAAARPAERAADPAAEGLTGLAALKARDPSFDP
GRFLSGARGAYEMIVKAFAEGDRETLKNLLSPDVMANFEAAIAAREAEGRTEKVEFLHPPRADLEKAEVV
GDLARATVRFLAEVRSRSKGPEGEAVDDRRTAELWTFERSLKSRDPNWTLVHVDAAEA
>gnl|CDD|468184 NF033779, Tim44_TimA_adap, Tim44/TimA family putative adaptor protein. Members of this family resemble both the eukaryotic protein Tim44, important to the assembly of a protein translocase in mitochondria, and the TimA protein of alpha-proteobacteria such as Caulobacter crescentus. TimA may assist in protein recruitment to the membrane, as Tim44, but appears not to be part of any complex associated with protein translocation
IELIILAMIAVFLFLRLRSVLGRRTGFEKPPFDPAAPRPAPARPPDEVIEGPGRAPDPDIIDGVAEPGTA
VAAGLAAIKAADPSFDPKEFLEGARAAYEMIVMAFAKGDRDTLKPLLSKDVYESFEAAIAAREAAGETVE
AEFVGIDKAEIVDAELEGRVAEITVRFVSELISVTRDKDGEVVDGSPDAVKEVKDVWTFARDLGSRDPNW
KLVAT
>gnl|CDD|468185 NF033780, exosort_XrtU_C, exosortase U C-terminal region. The XrtU family of exosortases is marked by a distinctive C-terminal region, modeled by the exosort_XrtU_C hidden Markov model. Because members of the archaeosortase and exosortase family perform cleavage of target proteins, in pathways thought to lead to new covalent attachment at the C-terminus and surface anchoring, the XrtU C-terminal domain may indicate the presence of a novel anchoring chemistry
SQLGGWTLTGFETERREENPILGVNSDVWTYSRGGLQAQVSLDQPFPGWHDLTVCYEGLGWKLLDRVVRD
LPGGDDTWPFVEAEMQKPTGQRGFLLFSLFDQDGDPVQPPETLGRLGGRLLNRLKSPPGPVAPTYQLQLW
VTSPEPLSEEEREALRELFAAARAKLRQQIRAE
>gnl|CDD|411365 NF033782, lipoprot_Omp28, Omp28 family outer membrane lipoprotein. The Omp28 family of lipoproteins is named for a founding member described in Porphyromonas gingivalis, where it has been shown across many strains to be an expressed surface antigen. All members of the family are predicted lipoproteins
MKKILYLLLLLAAALLTSCDNVDEDDRLIEVPAATVGRNVLIEDFTGQRCINCPAAHETIAQLQAQYGAD
KLIAVAIHAGPLALKPPSGVVGLRTDAGDAYYKHWAVPNLPKAIVNRRGGVLSYDAWAGRIYEELAQTTT
VNIDLKAQYDATKRQVTIKTDLLTLNEGVKGKLQLWLVEDGIVAPQLFPNNKLDKNYVHNHVFRAAVNGI
WGEEISLQKDYTQTEEFEYTLPEGWVPDNASIVAFVYNDSGVLQVVRQKISLQ
>gnl|CDD|411366 NF033785, sulfur_OscA, sulfur starvation response protein OscA. OscA (organosulfur compound A) is a small protein, about 60 amino acids in length, in the DUF2292 family. As characterized in Pseudomonas corrugata, OscA is required during sulfur starvation for obtaining it from organosulfur compounds. The pathway is required to remediate oxidative stress from chromate, so oscA was discovered by the loss of high resistance to chromate in Pseudomonas corrugata 28 when the gene is insertionally inactivated. The oscA gene tends to be found near sulfate transporter genes
MSASLRSLDGQDEATILREIQSALRGLRFGAVEITVHNGQVVQIERKEKFRLQQPGNKNS
>gnl|CDD|411367 NF033787, HTH_BldC, BldC family transcriptional regulator. BldC, a helix-turn-helix transcription factor with homology to the mercury resistance transcriptional regulator MerR, is a DNA-binding protein. It is considered the founding member of a subfamily of regulators with an asymmetric head-to-tail oligomerization for cooperative DNA binding, rather than classic dimerization
ELLTPAEVAALFRVDPKTVTRWAKAGKLTSIRTLGGHRRYRESEVRALL
>gnl|CDD|411368 NF033788, HTH_metalloreg, metalloregulator ArsR/SmtB family transcription factor. Transcriptional repressors that sense toxic heavy metals such as arsenic or cadmium, and are released from DNA so that resistance factors will be expressed, include ArsR, SmtB, ZiaR, CadC, CadX, KmtR, etc. However, some members of this family, including the sporulation delaying system autorepressor SdpR and its family (see NF033789), may lack metal-binding cites and instead regulate other cellular processes
LAELFKALADPTRLRILELLAEGELCVCELAEALGLSQSAVSQHLKVLRDAGLVTSRREGRWVYYRLADE
HVAELL
>gnl|CDD|411369 NF033789, repress_SdpR, autorepressor SdpR family transcription factor. Transcription factors in the family of the sporulation delaying system autorepressor SdpR (of Bacillus subtilis) resemble metalloregulatory transcriptional repressors such as ArsR, SmtB, CadX, ZiaR, etc., but may lack the key metal-binding residues
TFKALSDPTRREILELLKEGDMTAGEIAEHFDMSKPSISHHLNILKQADLVTDERKGQFIYYSLNTTVFE
EVLGWLLDL
>gnl|CDD|411370 NF033790, CnrY_NccY_antiS, CnrY/NccY family anti-sigma factor
MADIDKWLADAAKVTLEASAGADAAALQQRLAAEPAPAALAARRDARRAMLCAALAALVAFAAIGRLAMI
LQPKPAPTWVAAPSAASPFGLLIGK
>gnl|CDD|411371 NF033791, ActR_PrrA_rreg, ActR/PrrA/RegA family redox response regulator transcription factor. ActR, PrrA, and RegA are examples of lineage-specific names given to a response regulator transcription factor that acts as a global regulator and belongs to a sensor-regulator pair that is highly conserved in the alpha-proteobacteria. Examples of this regulator include ActR (acid tolerance regulator) in Sinorhizobium meliloti, stationary phase response regulator SpdR in Caulobacter crescentus
DRSLLIVDDDKPFLQRLARAMEKRGFEVTTAESVAEGLAAAKAAPPAFAVVDLRLGDGNGLDVVEALRER
RPDARIVVLTGYGNIATAVAAVKLGAVDYLAKPADADDVEAALLARPGEKPEPPENPMSADRVRWEHIQR
VYELCDRNVSETARRLNMHRRTLQRILAKRAPR
>gnl|CDD|468186 NF033792, ActS_PrrB_HisK, ActS/PrrB/RegB family redox-sensitive histidine kinase. This redox-responsive histidine kinase, found in alpha-proteobacteria, shows strong sequence conservation, including the notable motif [VA]AAAAHELGTPxTI. It always acts as a partner to an ActR/PrrA/RegA family global response regulator transcription factor in a two-component sensory transduction system. Lineage-specific names and gene symbols given to this histidine kinase reflect downstream regulator changes such as entry into stationary phase, anaerobic expression of photosynthesis genes, and survival of exposure to low pH
LGRRSRRLRLRTLVRLRWLAVAGQTAAVLVVAFGLGFPLPLGPCLALIAASAWLNLLLTLRFPPNRRLSD
REAALLLAFDILQLAALLFLTGGLQNPFALLLLAPVTISATALPLRHTLLLGALAIACATLLAFFHLPLP
WYDGEPLVLPPLYLFGVWLALVIGIAFTAVYAWRVAEEARRLSDALAATELVLAREQHLSALDGLAAAAA
HELGTPLATIALVAKELERELPDDPPLREDAELLRSQAERCRDILRRLTSLGEEGDAHLDRLPLSALIEE
AAAPHRGFGKEIEVVVAGDPGEEPVIRRNPEILYGLGNLIENAVDFARSTVTVTASWDAESVTITIEDDG
PGFPPDVLSRIGEPYVTTRRGEERRPGGGGLGLGLFIAKTLLERSGATVTFANRPPPEGGAVVTVRWPRA
ALE
>gnl|CDD|411373 NF033793, peri_CopK, periplasmic Cu(I)/Cu(II)-binding protein CopK
MLKKLLIAAALSAVALSAFAVDASNVEKSYELKDGSTVYVFKDGKMGMEDKFGRAVRMKEGHVMETKDGQ
KIMMKGNEVWRLDSLLHK
>gnl|CDD|411374 NF033794, chaper_CopZ_Eh, copper chaperone CopZ. Copper chaperone CopZ, as the name is used in Enterococcus hirae and related species, is a small copper-binding protein with close homology to domains found, sometimes in multiple copies, in various copper-translocating copper-translocating P-type ATPases, and to distinct families of other small copper chaperones that also named CopZ
KQTFSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKFDETQVTAEKIAQAVNELGYQAEVV
>gnl|CDD|411375 NF033795, chaper_CopZ_Bs, copper chaperone CopZ. This model describes CopZ, a small copper chaperone, as found in Bacillus subtilis and related species. A number of longer protein, such as copper-translocating P-type ATPases, contain multiple CopZ-like domains, with its signature invariant CxxC motif. CopZ from other species may be more different in sequence from this family than some of those domains of longer proteins
KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIEDQGYDVV
>gnl|CDD|468187 NF033796, selen_YedE_FdhT, selenium metabolism membrane protein YedE/FdhT. Members of this family are predicted multiple membrane-spanning proteins, and therefore thought likely to be transporters. It appears that all species whose genomes encode a member of this family produce selenocysteine-containing enzymes, typically formate dehydrogenase. The family member from Campylobacter jejuni was show to be essential for formate dehydrogenase (a selenocysteine-containing enzyme) expression and activity, and so it was named a formate dehydrogenase accessory protein, FdhT. Note that this family is related to (but distinct from) that of TIGR04112, which is similarly restricted to species with pathways for selenium incorporation
KYLVRFWNPYPAVIALGVLSAYYFGITGTVWAVTGEFTRWGGHILQLFGVDTSEWSYFKLIGLKGTPLTR
IDGVMIIGMFAGALIAALLANNVKLRLPQSKRRIFQALIGGIIAGFGARLAMGCNLAAFFTGIPQFSLHA
WFFTLATAIGTYFGVKVTLLPFFRGKPKLQKGSAGKPLGQAAPKARAKIQFRLGILIFVAFLGWAVYLFA
SGSTMLGLAALFGLAFGFLIERGQICFTSAFRDLWITGRTTMAKAIIIGMAVSTIGTFAFIQLGVPPKIF
WAGPNAIIGGLLFGFGIVLAGGCETGWMYRAMEGQVHFWIVGIGNIIGATLLAYSWDHIAPALATSYPKI
NLLESFGPYGGLLLTYALLALLFLLVLWWEKRFFKKR
>gnl|CDD|411377 NF033797, phero_SHP2_SHP3, SHP2/SHP3 family peptide pheromone
MKKISKFLPILTLVMDIIIIVGG
>gnl|CDD|411378 NF033798, biofilm_StcA, StcA family protein. StcA (streptococcal charged A protein), as described in Streptococcus pyogenes, is a small, positively charged, secreted protein that participates in a quorum-sensing system, and promotes biofilm formation. Related proteins are found in several other Streptococcus spp
MTKKQFYLILAISILCFILAVSPKPPTPKHTIERTSTAMTTTHKKQHPLKKEALDQKKPKNKAPFLPSKD
GVIKPVITMTVEHVEIPLD
>gnl|CDD|411379 NF033799, inhib_PhrA, PhrA family phosphatase inhibitor
MKSKWMSGLLLVAVGFSFTQVMVHAGETADTEGKTFHIAARNQT
>gnl|CDD|411380 NF033800, quorum_NprX, quorum-signaling peptide NprX. NprX, also called NprRB, belongs to the NprR-NprX quorum-sensing system in Bacillus. The mature form of the peptide pheromone is the SKPDIVG heptapeptide
MKKMVFGVLAFIVTLTVAGGIHQYSSKPDIVGQQAKTVEQINS
>gnl|CDD|411381 NF033801, NprX_fam, NprX family peptide pheromone
MKKMIAGILAVVVVLTVVGGVQYASKPDTYGQGAKVVETVNS
>gnl|CDD|411382 NF033802, AimP_fam, lysogeny pheromone AimP family peptide. AimP is the quorum signaling-like peptide pheromone of a phage system, called the arbitrium system, that detects environmental evidence of predecessor phage activity, in order to direct a lysis/lysogeny decision
MKKVFIGLTIVAALAVSFVAGQQSVETASGDDDIEVASASRGA
>gnl|CDD|411383 NF033803, TOMM_BorA, TOMM family putative cytolysin BorA. The BorA family of thiazole/oxazole-modified microcin (TOMM) peptides that are putative cytolysins and virulence factors have been found, so far, encoded by plasmids in members of the genus Borreliella
MFIRNKHFLTSIGINANYAVIPGSCCCSCTCSCSFSL
>gnl|CDD|468188 NF033804, Streccoc_I_II, antigen I/II family LPXTG-anchored adhesin. Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc
KKKEVYGFRKSKVAKTLCGAVLGAALIAVADQQVFADEVTETTSTTNVEVTTTGNPATNLPEAQGEASQA
AKESQAQAGSKDGALPVEVSSADLDKAVKDAKSAGVNVVQDETVDKGTATTATENAQKQTEIKSDYAKQA
EEIKKTTEAYKKEVAAHQAETDKINAENKAAKDKYQKDLKAHQAEVEKINTANATAKAEYEAKLAQYQKD
LAAVQKANEDSQADYQNKLSAYQTELARVQKANAEAKEAYDKAVKENTAKNAALQAENEAIKQRNETAKA
NYEAAMKQYEADLAAIKKAKEDNDADYQAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNTAIQAEN
EAIKQRNAAAKATYEAALKQYEADLAAVKKANAANEADYQAKLAAYQTELARVQKANADAKAAYEKAVED
NKAKNAALQAENEAIKQRNAAAKADYEAKLAKYQADLAKYKKDLAEYPAKLKAYEDEQAKIKAALAELEK
KKNEDGYLSEPSAQSLVYDSEPNAQLSLTTDGKLLKASAVDEAFKKDTAQYGKKNLQLDNLNVTNLEQAD
ATTSSVELYGNIGDKSDWTTNVGNKTEVKWGSVLLERGQSVTATYTNLQNSYYNGKKISKIVYKYTVDPS
SKFKNPGKVWLGIFTDPTLGVFASAYTGQVEKDTSIFIKNEFTFYDENGQPINFDNALLSVASLNREHNS
IEMAKDYTGTFVKISGSSIGEKNGMIYATETLNFKKGQGGSRWTMYKNSQPGSGWDSSDAPNSWYGAGAI
SMSGPNNSVTVGAISATNVMPSDEMPAVPGRDNTEGKKPNIWYSLNGKIRAVNVPKITKEKPTPPVAPTA
PQAPTYEVEKPLEPAPVAPTYENEPTPPVKTPDQPEPSKPEEPTYETEKPLEPAPVAPTYENEPTPPVKT
PDQPEPSKPEEPTYETEKPLEPAPVAPSYENEPTPPVKTPDQPEPSKPVEPTYDPLPTPPVAPTPKQLPT
PPAVPTVHFHYNKLAAQPQINKEIKNEDGVDIDRTLVAKQSVVKFELKTEALTAGRPKTTSFVLVDPLPT
GYQFDLEATKAASPGFDTSYDKASHTVTFKATAETLATFNADLTKSVETLYPTVVGRVLNDGATYTNNFT
LTVNDAYGIKSNVVRVTTPGKPNDPDNPNNNYIKPTKVNKNKNGVNIDGKEVLAGSTNYYELTWDLDQYK
GDKSSKETIQNGFYYVDDYPEEALDLRPDLVKITDANGNQVSGVSVQQYDSLEAAPKKVQDLLKKANITV
KGAFQLFSADNPQEFYKQYVATGTSLTITDPMTVKSEFGQTGGKYENKAYQIDFGNGYATEVVVNNVPKI
TPKKDVTLSLDPADSENVDGQTIPLNQVFNYRLIGGLIPANHSEELFDYSFVDDYDQTGDQYTGNYKVFA
KVDITLKDGSVIKAGTDLTQYTTAEVDAAKGMITIRFKEDFLQSISLDSAFQAETYIQMKRIAVGTFENT
YVNTVNKVAYASNTVRTTTPEPKRVPSPKVEKPEAPTPQPNSVGKPNTTLPQTGTNDSSYMPYLGLAALV
GVLGLGQLKRKE
>gnl|CDD|468189 NF033805, invasion_CiaB, invasion protein CiaB. CiaB (Campylobacter invasion antigen B) is important for host cell invasion by Campylobacter. It is found as well in a number of other species capable of invasion, including Campylobacter coli, Campylobacter rectus, and Helicobacter pullorum
DFKKLYELLEERKEKLNALYKILDSKENELIEAFLKLLGLPGNKETRLALLRRIVDLKEDALVNELKKLG
FSEEEILEIKEKAYEFVRDFYEKRHEELIAEIKEKKLLTPFYRALLQGVHNIGLVLNKWQSSWTKHIIDG
INKELSAKFNGDEAKAMEFLEKNKLYQKDPNGEICDRSYSVLVKIGGKYKFVPYAEAFEEEVKEVKDAFE
KLIENLEGLEDNEQKEAYIAYFEALKNAFCEKDNDELIKAWAEVDRAWMDIKTPLQVGHPLEYYEDHYRK
AVALEWDIRLANPSLFDAKKFKNNIKEFFEEIYKKIGKNDEEIHNCVLSNIDKTQLYIGRPMIYYGAELN
GLFSAQVVPNDEFVSSECGKKIFAFVDFVYESAKAKPFMKLSSEIFGKEFLDFGREILFNKPEIWKKVYE
ISTIGHEFGHILWIDEDTEKVMNKSGQFKNIEEFKATTGGLVNFFLHEDEELKEPVFHELIKRAVGLIAW
MEVDEVLPYYCEGLIHLSLLFESGVLKFDGKFLSIDIDEAAYEKFKEWYLQNYHKLAKHYLSKKDAKEFL
SKFCKKEEGVYLPKDEEVREFVKYYYARYEEIGNEIDESG
>gnl|CDD|411386 NF033806, laterosporulin, laterosporulin family class IId bacteriocin
MACVNQCPDAIDDWAYGDWKCHGVEGKYYRHVYAVCMNGANLYCRTEWGKGC
>gnl|CDD|468190 NF033807, CopL_fam, CopL family metal-binding regulatory protein. The founding member of this family was shown to be involved in the copper-responsive expression of a multicopper oxidase copA encoded downstream. The regulatory function likely involves copper-binding, but activity as a DNA-binding transcriptional regulator was not demonstrated directly
LLLRLLLILALVLNGAGGAWASVRMAMPHMAAAAAAAAAAAAAAAAAPCHGDAPAAAAAAPPAADHDPHA
DDCCKSGSCDCACAQHCSAALPTLPALPAHLPGSLAVAAPLLSGHPSPALPHLFRPPIG
>gnl|CDD|468191 NF033808, copper_CopD, copper homeostasis membrane protein CopD. CopD is an inner membrane protein encoded in Gram-negative bacterial systems that provide resistance to excess copper. It is typically chromosomal, although the PcoD protein of the plasmid-borne pco copper resistance system is a exceptional member of the CopD family
DALLIALRFAHYLALMLLFGLALFGLYLLPGSLRALLRRRLLRLLRLAAVLGLLSSLLWLALQAAAMGGG
WLDALDHTLWMVVLGTRFGQAWLWRLVALVLALLALLLLPRRPRRLLLALLGAVALATLAWTGHAAMDEG
LLGVLHLLNDILHLLAAGAWLGALLPLLLLLRRARLGRDAWRRLAIRALMRFSRVGHLAVALLIVTGVVN
YLLIVGPWPLDWLSSSTYGRLLLLKLALVALMLGLALANRYRLVPRLERALRGALRALRRSTALELALGV
LVLALVAWLGTLSPV
>gnl|CDD|468192 NF033814, copper_CopC, copper homeostasis periplasmic binding protein CopC
SLLAAGAALAHAHLKSSTPAANATVAAPAKITLTFSEGLEPAFSGVKLTMTGMPGPMVVTGAAVLGGEDG
KTLVVPLAQPLAAGTYTVDWHVVSVDGHKTTGSYSFTVK
>gnl|CDD|468193 NF033816, Cj0069_fam, Cj0069 family protein. Cj0069 from Campylobacter jejuni, described as a serological marker that can show a patient was previously infected with that organism, is the founding member of an uncommon broadly distributed family of proteins. Members of that family are found also in various Helicobacter spp., Bradyrhizobium spp., and Corynebacterium spp
KVAIFEVGDGSDKGEAGPRKDTMPIVFAALARGWDAEPVVYDDEFADEIRAQLKANDDVYVSRVNPGNLP
GGERGYFDALLRLVAAGVVGSAHPDVILAYGAKDVLVKLRDTGLVPSDTHAYYDAEEFRAEFPTRLAYGE
RVLKQNRGSTGEGIWRVELLDGSLLDTKIKVTEAQDNHTEERQLGAFMDFCEQYFEGDNGMLVDMPFQPR
IKEGEIRCLLVGDRPVGVGHKKPAALADNFSATLFSGRLYRYDDPERWQELRDLFEDEWPPILEKLGGLD
DLPLIWDADFMLDPDEAGEDTYVLGEINCSCVGFTSELAPGIKVADEIIRRLE
>gnl|CDD|468194 NF033817, Mplas_variab_LP, variable surface lipoprotein signal domain. This HMM describes a homology domain of lipoprotein signal peptides restricted to the genus Mycoplasma, and found in paralogous families that typically are associated with antigenic phase variation, as expression of some members of the family is turned on, others turned off, by the means promoter region modifications by site-specific DNA invertases. The avg family of Mycoplasma agalactiae represents one such family of lipoproteins
KKNKFLLSLGSLSSLAAIPLVAASCGDTK
>gnl|CDD|411392 NF033819, IS66_TnpB, IS66 family insertion sequence element accessory protein TnpB. The IS66 family insertion sequence element encodes a DDE transposase TnpC, and two accessory proteins, TnpA and TnpB. It has been assumed that the TnpA, TnpB, and TnpC proteins are produced independently in appropriate amounts and form a complex, which acts as a transposase to promote the transposition of an IS66 family element
IYLATGPTDMRKGIDGLAALVQEVLGLDPFSGHLFVFRNRRRDRLKILYWDGSGFCLYYKRLEKGRFRWP
RAADGVVALTPAQLAWLLEG
>gnl|CDD|411393 NF033820, STM0539_fam, STM0539 family protein. STM0539, from Salmonella enterica strain LT2, is the founding member of family of proteins of unknown function, about 145 amino acids in length
KKSIFLALVLSLALSSLPGAAEISSSAPYALSSAISSVGSSALVSGIILSPVLLPAALIAISVEKNKKQK
TATITGKTPKGETVKLLVPLEVVEKAPLKPGDKLTLEPAPEGTGAYLKKEGKVISHMVNQDDAELSHQEP
L
>gnl|CDD|411394 NF033821, YoaK, YoaK family small membrane protein. YoaK is a small protein (about 32 amino acids) found in E. coli (from which it is named), Salmonella, Klebsiella, Pantoea, and related taxa. It associates with the inner membrane
MKIGILFPVAIIIAAVVFLAWFIIGGYAAPGG
>gnl|CDD|468195 NF033823, archmetzin, archaemetzincin family Zn-dependent metalloprotease
RILIVPIGEVPAELLDEVARKIKEVYGVEVVLSSPLPVPERAYDPSRNQYRADAILDYLLRIRVGGADKV
LGVTDVDLYEPGLNFVFGLAYPGGKVAVVSTARLRNEFYGREPDEDLFLERLAKEAVHELGHLLGLGHCP
NPRCVMHFSNSLDDTDRKSKYFCPSCRRKL
>gnl|CDD|411396 NF033824, Myxo_non_zincin, non-proteolytic archaemetzincin-like protein. Members of this family resemble the archaemetzincins, a mostly archaeal family of Zn-dependent metalloproteases, but it lacks the critical catalytic glutamate (E) in the signature motif HEXXH, within the longer pattern HEXXHXXGX3CX4CXMX17CXXC that defines the archaemetzincins. Members of this family are found in Myxococcus xanthus and related members of the Delta-proteobacteria
PQKVLLLVPVGSPPPSLLRDLEEPLATHLGLSAVVSKTALSRPAYAFNKDRSQYHCNAIMRRLVTLLEPG
QALVLGVTDVDLFVPDSPFVFGEADRESRSAVVSLARLRQGAEGEQLRRRVQVEAVHQAGHLLGLSYCED
ARCVMFFAQTPQDVDRKQLSLCNNCRNELNKLNR
>gnl|CDD|411397 NF033826, immun_CdiI, ribonuclease toxin immunity protein CdiI. CdiI proteins, including the founding member from Escherichia coli strain STEC_O31, serve as immunity proteins for the toxic tRNA-cleaving ribonuclease toxin CdiA. The system confers contact-dependent inhibition (cdi) between different strains of bacteria
KELFGQPYDNSDPHWIIKSYFDRMYGDGYFLKAIGYISKKISFHVDGAYCNFPDMNSYDESEHFEGVEFA
YGYPPSEADTIIVSEEICYKYVRLACEKYLKLHPEDTEKVNALLAKLP
>gnl|CDD|468196 NF033827, CDF_efflux_DmeF, CDF family Co(II)/Ni(II) efflux transporter DmeF. DmeF, a metal efflux transporter belongs to the cation diffusion facilitator (CDF) family. Examples from different species have been described as primarily being induced by, or performing efflux of, different panels of metals, including Co(II) and Ni(II) for Rhizobium leguminosarum and Agrobacterium tumefaciens, and a broader spectrum Wautersia metallidurans CH34
GHDHVFLGADHDRNERRTWWVVALTAVMMVAEIVAGTLFGSMALLADGWHMSTHAGALGIAALAYAYARR
HARNPRFSFGTGKVGDLAGFASAIILALIALLIGWESVVRLLSPVPIAFGEAIAVAVLGLAVNLVSAWLL
GGDHHHHGHGHGHGHGHHHHDHGHHHHHHHGHRDNNLRAAYLHVLADALTSVLAIAALLAGRYLGWVWLD
PLMGIVGALVIARWSWGLMRDTGAVLLDATPDEHLAAEIREAIETDGDRITDLHVWRVGPGHHAAIVSVV
THAPRDPAFYRARLAPVHELSHVTVEVR
>gnl|CDD|411399 NF033828, entry_exc2_fam, Exc2 family lipoprotein. Exc2, a plasmid-encoded predicted lipoprotein of small size, was once described as a plasmid entry exclusion protein (1985). However, a more recent article (1995), says entry exclusion activity should instead be ascribed to MbeD
RALLLAITALALSGCASSKSSPERHARHFVYQSSDFFDPNFRTNKADSYRLNVPFFRQFYQQGKKDRAAG
ISRAEAQQRADYFRSQEFLSSLKTTSIFAGNDYWDSDMEPKDAQLLGDELAATYLDGYNGR
>gnl|CDD|411400 NF033829, plas_excl_MbeD, MbeD family mobilization/exclusion protein. MbeD, as found in the ColE1 plasmid, was originally described as a plasmid mobilization protein. Later, it was shown that MbeD additionally was responsible for a plasmid entry exclusion phenotype that had previously been ascribed to products of the exc1 and exc2 genes
MTELEKQLLSALEQLQQDYEQRLQEWESAFAELQKMFEVTQQENAALDERVQQLSQQVQSLSEQVERLS
>gnl|CDD|468197 NF033830, NleE_fam_methyl, NleE/OspZ family T3SS effector cysteine methyltransferase. NleE from Escherichia coli O157:H7 strain Sakai, and its homolog OspZ from Shigella, are the founding members of a family of SAM-dependent protein--cysteine methyltransferases. Both are type III secretion system (T3SS) effectors involved in virulence, and have the host protein NF-kappa-B as substrates
SPNTNNAEDVIRNIYPEINADFFNEKPNIYDQKYISGITRGLAAFKLEEFINKKARIRQYIKRMYSPCPE
NFTPISRSEANTPEGSWLTVISGKRPMGQFSVDSLYSPVLHALLELPNIGCKIFPKENNDFLYIIVVYRR
DSEQGEQRANRFIELYNEKREIMQSLTGESHELKAIKSELVIAREMGEILSYLPEEIDNYMKMMNTLLEQ
IQ
>gnl|CDD|468198 NF033831, sce7725_fam, sce7725 family protein. This family of uncharacterized proteins is named for founding member sce7725 from Sorangium cellulosum, from the Deltaproteobacteria. It belongs a gene pair found sporadically in genera as diverse as Enterococcus, Lactobacillus, Staphylococcus, Streptococcus, Acinetobacter, and Klebsiella. The partner in each gene pair is a member of the sce7726 famly
YYPYLRGKQFELLALRELAEKGLLSKKVIPIIEPVKESSNTLKKTLEAFNKANHPAIVIVNPQVGDFKED
GNNLDSLLNAELLHLPNISIGKALISDTNIETIDNLLDSYAIHNALLIHAGDFSDDLDLYEQLFSDLKNT
RYVLIPDESRLRRRVFNGSKKVLLRDGFTKQPRNADYPEKPDEFFSDLHLYYQEDGYIGFSDYSIVGDEY
SEGGGPAYAVAIHLTYIDPDDNLRIHHFVSDSNDTPTDPAGKFFEALEKLIAWLNSNPSQLLETTGLKEL
LEYLHQGHFPGLGVVKKLSIMHHIELMSRYL
>gnl|CDD|468199 NF033832, sce7726_fam, sce7726 family protein. This family of uncharacterized proteins is named for founding member sce7726 from Sorangium cellulosum, from the Deltaproteobacteria. It belongs a gene pair found sporadically in genera as diverse as Enterococcus, Lactobacillus, Staphylococcus, Streptococcus, Acinetobacter, and Klebsiella, or in phage from those lineages. The partner in each gene pair is a member of the sce7725 family
RNEYDIKNALLNKLLLGRHSLNTTTILEELRIGKSRADLVVINGKLTGYEIKSELDSLKRLESQLEDYSK
VFDKVYVVTGEKHLDKVLKIVPEWVGIIELTERNKISLKTIRKAKENPSRDKETLFSLLWKSELLNILKK
FYGYLPTVPNKSRYELCEKLFEKIPLDELRALFRKELKKRRY
>gnl|CDD|411404 NF033833, rhodan_ChrE, rhodanese family chromate resistance protein ChrE
MPNAISSSELAAAIQGLVAPQLIDVRRKAAFDASAQMIAGASWRNPDDIGNWITTLDANRPVVVYCVHGH
QVSQDCAARLEAAGFDATYLEGGIEQWAAGNHPTISKP
>gnl|CDD|468200 NF033835, VraH_fam, VraH family protein
IKEIIKQWEDLLNKKWGSKNILILIVYVIILSIFTTPLLGIPAGLLAGAYLLKN
>gnl|CDD|411406 NF033837, GarQ_core, garvicin Q family class II bacteriocin core domain. This HMM describes the core (mature) peptide region of GarQ, the class II bacteriocin garvicin (garvieacin) Q, and homologous peptide with similar core regions. Some members, such as GarQ itself, have a classical GlyGly-containing ComC/BlpC-like leader peptide, but others have N-terminal regions (probable leader peptides) of a different type
MNGANGYAYRDKNGHWHYKVTKGPVEAVTGVIANGWGSAAAG
>gnl|CDD|468201 NF033838, PspC_subgroup_1, pneumococcal surface protein PspC, choline-binding form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site
MFASKSERKVHYSIRKFSIGVASVVVASLFLGGVVHAEEVRGGNNPTVTSSGNESQKEHAKEVESHLEKI
LSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKK
VAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAK
AKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKE
NDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKTLELEIAESDVKV
KEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQP
QPAPAPQPEKPAPKPEKPAEQPKAEKPADQQAEEDYARRSEEEYNRLTQQQPPKTEKPAQPSTPKTGWKQ
ENGMWYFYNTDGSMATGWLQNNGSWYYLNANGAMATGWLQNNGSWYYLNANGSMATGWLQNNGSWYYLNA
NGAMATGWLQYNGSWYYLNANGDMATGWLQYNGSWYYLNANGDMATGWLQYNGSWYYLNANGSMATGWVK
DGDTWYYLEASGAMKASQWFKVSDKWYYVNGSGALAVNTTVDGYGVNANGEWVN
>gnl|CDD|468202 NF033839, PspC_subgroup_2, pneumococcal surface protein PspC, LPXTG-anchored form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A
MFKSNHERKMRYSIRKFSIGVASVAVASLFMGSVVHATEKEGSTQAATSSNRGNESQAEQRKELDLERDK
AKKAVSEYKEKKVKEIYKKSTKERHKNTVDLVNKLQNIKNEYLNKIVESTSKSQLQKLMMESQSKVDEAV
SKFEKDSSSSSSSGSSTKPETPQPENPEHQKPTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLAVATYM
SKILDDIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNVNTKVEIENTVHKIFADMDAVVTKFKKGLT
QDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETP
KPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEV
KPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQ
ADDKKPSTPNNLSKDKQPSNQASTNEKATNKPKKSLPSTGSISNLALEIAGLLTLAGATILAKKRMK
>gnl|CDD|411409 NF033840, PspC_relate_1, PspC-related protein choline-binding protein 1. Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC
MEKFNTNKRYALRKLGKIFGSVIVGLTLFLGGILNTSFVHAASTIRYIKDDTRPVGSNVLTESDGEDGIK
KITTTYDLNEKTGEVTVKENTTTIEKKAQDIIYKVAAQDKIQEKTINHKTRFEKDENKERSENPVTIDGE
DGKVVTTTTYDVSPETGTVTENVTIEKKEPTDTVIKVPAKSKVEREVLPTSVIRFEKDETKDRSENPETI
DGEDGYVTTTRTYDVDTETGEVTEKVTTDRTEPTDTVIKVPAKSKVERRVLPTSVIRFEKDETKDRSENP
VTIDGEDGYVTTTRTYDVNPETGKVTEKVTVDRKEPTDTVIKVPAKSKVEEVLVPFATKYEADNDLSAGQ
EQEITLGKNGKTVTTITYDVDGKSGQVTESTLSQKEDSQTRVVKKGTKPQVLVQVIPIETEYLDDPTLDK
GQEVEEAGEIGEITLTTIYTVDERDGTIEETTSRQITKEMVKRRIRRGTREPEKVVVPKKSSIPSYPVSV
TSNQGTDAAVEPAKPVAPTTGWKQENGMWYFYNTDGSMATGWVQVNGSWYYLNSNGSMATGWVQVNGSWY
YLNSNGSMATGWVQVDGSWYYLNDNGSMETGWLQNNGSWYYLNSNGSMKANQWFQVGSKWYYVNASGELA
VNTSIDGYRVNDNGEWVR
>gnl|CDD|411410 NF033841, small_YshB, YshB family small membrane protein. YshB, a membrane-associated protein typically 36 to 40 amino acids in length, is found conserved in genera of the gamma-proteobacteria including Cronobacter, Enterobacter, Escherichia, Klebiella, Salmonella, and Serratia. The gene symbol derives from E. coli K-12
MLESLISMISHGAEIGAAASHTPQTAIAAVLCAALVNLFS
>gnl|CDD|411411 NF033842, small_MgtS, protein MgtS. MgtS, previously called YneM, is a small inner membrane protein that modulates Mg(2+) concentrations through its effects on the P-type transporter MgtA
LGNMTVFIAVLGVILFSGFLAAYLSHKWDD
>gnl|CDD|411412 NF033843, small_YpfM, protein YpfM
MIERELGNWKDFIEVMLRK
>gnl|CDD|411413 NF033844, small_YqgB, acid stress response protein YqgB
MNKKPVAQSQRQHYLLGNRAVYGLLSRLRIAIVVNCFTLS
>gnl|CDD|468203 NF033845, MSCRAMM_ClfB, MSCRAMM family adhesin clumping factor ClfB. Clumping factor B is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif
MKKRIDYLSNKQNKYSIRRFTVGTTSVIVGATILFGIGNHQAQASEQSNDTTQSSKNNASADSEKNNTIE
TPQLNTTANDTSDISANTNSANVDSTAKPMSTQTSNTTTTEPASTNETPQPTAIKDQATAAKMQDQTVPQ
EANSQVDNKTTNDANSIATNSELKNPQTLDLPQSSPQTISNAQGTSKPSVRTRAVRSLAVAEPVVNAADA
KGTNVNDKVTASDFKLEKTTFDPNQSGNTFMAANFTVTGQVKSGDYFTAKLPDSVTGNGDVDYSNSNNTM
PIADIKSTNGDVVAKATYDILTKTYTFVFTDYVNDKENINGQFSLPLFTDRAKAPKSGTYDANINIADEM
FNNKITYNYSSPIAGIDKPNGANISSQIIGVDTASGQNTYKQTVFVNPKQRVLGNTWVYIKGYQDKIEES
SGKVSATDTKLRIFEVNDTSKLSDSYYADPNDSNLKEVTDEFKDKITYKYQNVASINFGDINKTYVVLVE
GHYDNTGKNLKTQVIQENIDPATGKDYSIFGWNNENVVRYGGGSADGDSAVNPKDPTPGPPVDPEPSPEP
EPEPTPDPEPSPDPDPEPSPDPDPDSDSDSDSGSDSDSGSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS
DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD
SSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS
DSDSDSDSDSDSDSDSDSDSDSDSDSDSRVTPPNNEQKAPSNPKGEVNHSNKASKQHKTDALPETGDKSE
NTNATLFGAMMALLGSLLLFRKRKQDHKEKA
>gnl|CDD|411415 NF033846, Rumino_NPXTG, NPXTG family C-terminal sorting domain. Rumino_NPXTG represents a flavor of C-terminal protein sorting signal in species related to Ruminococcus albus. In that lineage, multiple sortases per genome may be found, including multiple B-type sortases. Proteins found by this HMM (more than 12 encoded in a representative complete genome) may represent substrates of a panel of related sortases, while additional proteins found in Ruminococcus genomes with below-cutoff hits to this model may be processed by other sortases
NPNTGAAAGLALAMLALAGAAAVVSKKKK
>gnl|CDD|468204 NF033847, MCP_Sipho, major capsid protein, Siphoviridae type. This protein is a phage major capsid protein, as reported in primary sequence submissions of a large number of Siphoviridae, many of which have hosts in the Mycobacterium and Gordonia genera of bacteria
TDDELAALLAEAVAAFDELRARDELTDEDLARLRALADAVDAIRAEQAERAAAAAAAAAELDALAARVAA
ADEAAEGDDEADDAEAAEEGDPAAEAAAEAEAEAEAAAAAAAAPAAAAAAARPRVSLAAARRRAPRVLPE
APAPGPGITAAADVPGFAPGQPLDGFADLAAAIDSRAKGLPTGGRRPGGGVRARQGVASLRRPFPEELDL
SSDPEGDTAAIEAAADESRLPGGSLVAAGGWCAPSETLYDFCDVPAADGLLDLPEIQITRGGIRYPVEPD
LAALYGALGFVFTEAQDIAGTPTKPCYEIPCPDFVEVRLEAVGVCLEAGILQQRAWPELVEWFLRLALVA
HAHRVNARTIAKMVAGSTAVTIPATLGATSSVLNALALQATDLRYRHRLSRTATLEVVAPSWLREVLRAD
LARRNGVDTLDVTDAQIDAWFAARGIRVQWVYDWQDAVPGAGFGGATAATAWPTTVDVLLYPAGTFVRGR
GNVINLGVVYDSTLLQTNDYTALFTEEAIAVGKRCGESRLVTVPLCVNGATGARVTLTC
>gnl|CDD|468205 NF033848, VgrG_rel, VgrG-related protein. Members of this family resemble Vgr proteins of type VI secretion systems (T6SS) as found in various proteobacteria. However, members of this family occur instead in genera such as Streptomyces and Roseiflexus. The biological roles and molecular functions of proteins in this family appear not to have been characterized
FAAVLVVEIGGAPLPADVAPLLVSGYVDESVGLPDAFVLTFRDPGHTVLGKTGITIGTPVVLSVVTDGPG
APEPLLTGEVTALEADYDGTGTFTVVRGYDKAHRLFRGRRVAAYRNMTASDIVRKVAARAGLAVGRVDAT
GTVYEHISQPNVSDWDFLSRLADENGAVVRVDDKGKLQFVKPKPASGAPSPSTPADKSPLVLEAGRNLLR
LRAAVTAADQVPEVEVRGWDVTTKKPLVATAPATTSPTVLPGLTPAKAAGKFGSAKLVVTDTPYRTQAEV
DAAAKALADDVASSFAELEAVARGNPKLRAGVPVALGNVGAPFEGKYTATSVRHVFEPGRGYTTWVTVSG
RQERSLYGLASGGGGAPARGPRLPGVAIAIVTDVKDPLKLGRVKLKFPWLDDTYVSDWARTVQWGGKGGG
GVFLPEVGDEVLVGFEQGDLDHPYVLGGLYNGVDKPPPHDVVPLVDGTSGKVNRRSLVSRSGNRVELLDQ
TGGGPQGVRLATGDGKLTVNLDRTKTEITVTSDGSVTIKGLRSVSVDAGTGLTLDAG
>gnl|CDD|468206 NF033849, ser_rich_anae_1, serine-rich protein. This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments
LDYLWFRLEVEPEGGREYRGYKAVRLLRLIRLPKEARRDTGLLDMQRQVLRGLYGAQVNFVYLAAGIFKP
EPLGLVQLYGVQGVSETIEEAKARADRDLAALEAALAGTYRQIRLRPLDAQEAEWLLEKLYQMPYVLVVR
GIPDPREAGGRGGDGGFGGQNANPYSEEQNEELFRGMSDLEEYLFQVLASPVSLDTLTRWLEAAAEETSN
WASRQQGQKSISFGVSLPMMYAANLGQSAGTGYGESVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHG
STRGWSHTQSTSESESTGQSSSVGTSESQSHGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSSHSDGTSQS
TSISHSESSSESTGTSVGHSTSSSVSSSESSSRSSSSGVSGGFSGGIAGGGVTSEGLGASQGGSEGWGSG
DSVQSVSQSYGSSSSTGTSSGHSDSSSHSTSSGQADSVSQGTSWSEGTGTSQGQSVGTSESWSTSQSETD
SVGDSTGTSESVSQGDGRSTGRSESQGTSLGTSGGRTSGAGGSMGLGPSISLGKSYQWEDDPAILLTEIL
RYQEERLNLASREGAFYTDVYILTESEDAAAAAMGLAPSAFHGTEAVTTPVQTRELTDEEQEYLLLHARA
FSPSTRKEGIPGVFEGYKYSTLLLSLELAAYTAPPRIEEGGILTTVADTPKFAFPPMMPGEIVLGHQYSP
ETGYLTPFPYRLDEDRLFHTAFTGDTGSGKTVAAMRLAYELSHVRRTTRGWHLRTVVLDFKQDWRALLNW
VEPGLEGRVDFYQLGPGAFRPLRWNPLKIPKGVNPERYRDAVAEIFARAGGLGERGLQILRDALTELYSE
AGVLTDDPEPNWGDVQTLQYLAVERSKKVTLSDLYERLEEKKEALERRDTDSRTALEGILDRLEQFARGY
SIAAQYFGGSDGIGIEDLLGDDDVTVLEGAGLDEFFKAFLLGLITSGLYQDAVARRGEVLAEDQYETQIV
FEEANKVLTGVDGGSDGGSGSLGGVSEEFETMLRDSRKYGLFLHLITQKISDLPSSIISSCANVFVGRLK
DPKDIDLVLAHIGRSEKFVDRDYKRWLPRIPIGWFICKSSYSRDFKMAEPVLVRPLMLDVPEPSDEEIDE
IL
>gnl|CDD|411419 NF033850, LCxxNW, mobility-associated LCxxNW protein. This protein belongs to a family of small proteins, about 65 amino acids long, with three invariant Cys residues, including one in the motif LCxxNW, for which the family is named. Member proteins are found in contexts that suggests they are accessory proteins of mobile elements. The context includes members of families PF01695, PF01610, and PF00665, all associated with transposition and/or integration
NYCAFSKDHKCIKWTDYELTRHELEEADELCHGNWIEIQRLYDYIEELQALLDENGIPYPE
>gnl|CDD|468207 NF033852, fulvocin_rel, bacteriocin fulvocin C-related protein. Fulvocin C was described in 1981 as a bacteriocin from Myxococcus fulvus, 45 amino acids long with 8 cysteines. The precursor form was not described. However, the most closely related precursor-like proteins represent the founding members of a family of proteins that average over 225 amino acids in length, the majority of which have a C-terminal tail region in which the 8 Cys residues are essentially invariant. The long N-terminal region, and the sharp change in amino acid composition at the start of what appears to be the bacteriocin core peptide region, suggests that the N-terminal region may contribute directly in peptide maturation or transport, rather than merely providing for recognition by maturation proteins
RRAIFRALSPEQKAKLWLEKLDQYRALHPDLSAEQRAVLDEAEAFLSDELFFFEEPEDEFDDFLYELREA
AVAAFGWDEARALLATLGPSEAKALQAASAAESLLGDCNCSTSSDWCGGGGYCVSGGNCTETSSGCGFLW
LYPCDGLCG
>gnl|CDD|411421 NF033853, KPN_two_small, small membrane protein. Members of this family, including paralogs KPN_01023 and KPN_01923 from Klebsiella pneumoniae subsp. pneumoniae MGH 78578, are small proteins, typically 40 amino acids in length. A highly hydrophobic region, about 25 amino acids in length with a composition typical of transmembrane segments, is followed by a highly basic region of about 15 amino acids. Analogous proteins of similar size, with apparently similar hydrophobic regions, have been described as membrane-associated proteins expressed in response to various types of cell envelope stress
SNLFLLIVAIFLLGVSVYSLISYIKDRRKTKLPFNKR
>gnl|CDD|468208 NF033854, esterase_BioV, pimelyl-ACP methyl ester esterase BioV. BioV, found in Helicobacter pylori and a number of related Epsilonproteobacteria replaces BioH as a pimelyl-ACP methyl ester esterase required for biotin biosynthesis
RYFSGFCLRNEKELFDEYLLKSDYTVAGFSYGAIKAFEYALNSSKRVDKLQLFSPAFFQTKPEKFKRLQL
LAFKKDPELYMENFLKNAGYPSPLDLSNYKHEGSLEELEELLTYKWDKEKLQFLLEKGVKIEVFLGLEDK
IIDAKKALEFFKPYATVYQIKGANHFL
>gnl|CDD|468209 NF033855, tRNA_MNMC2, tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD. This HMM describes either the N-terminal region, called MNMC2, of the tRNA modification bifunctional enzyme MnmC, or a free-standing protein that performs the same methyltransferase function, in partnership with an FAD-dependent protein, or C-terminal region, called MNMC1 (see TIGR03197)
PVSPRFDDHYFSKHGGLAETRHVFLEGNGLPERFAPGFTILELGFGTGLNFLATLAAWEESGAPLHYTSF
EAFPLSAEDLARALYAFPELAPLAEALLAAWPEEPLKLTGDFTLTVIFGDARETLPQLDGRADAWYLDGF
SPAKNPEMWSPELFAELARLTAPGGTLATYTAAGFVRRALQAAGFTVERLPGFGGKREMLRGVKP
>gnl|CDD|411424 NF033856, T4SS_effec_BID, T4SS effector BID domain. The BID domain (Bartonella intracellular delivery domain) is recognized by the type IV secretion system (T4SS) virB (not trw) of Bartonella and related taxa (e.g. Ochrobactrum), and is found in T4SS effector proteins such as BepA, BepB, BepC, etc. Multiple copies of the domain may be found in a single protein
TEEEIIEKIAKDPSVQESRKEIEHLSKIVYGNSKILNEQMEEINKNPELGEQLAWQIANNPESISKLAGF
KILGIKSPARKNAEENISPLCQAIENYADAVKQVKEEIL
>gnl|CDD|411425 NF033857, BPSL0067_fam, BPSL0067 family protein. null
KPLVGSGQCVALVQHYAGAPHTSTWREGEAVLGNKSIRKGTAIATFVNGKYPNRSHGNHAAFYLGQDADG
IYVMDQWKGDKKKKISKRFIRFKGKDKNGTYIDPSNNADAFSVIE
>gnl|CDD|468210 NF033858, ABC2_perm_RbbA, ribosome-associated ATPase/putative transporter RbbA
VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARH
RRAVCPRIAYMPQGLGKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGG
MKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATAYMEEAERFDWLVAM
DAGRVLATGTPAELLARTGADTLEAAFIALLPEEKRRGHQPVVIPPRPADDDDEPAIEARGLTMRFGDFT
AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSL
YGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI
LDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAARGA
ATLEEAFIAYLEEAAGAAAAPAAAAAPAAAAAAPAAPAPAPRRRFSLRRLLAYARREALELLRDPIRLTF
ALLGSVILMFVMGYGISLDVENLTFAVLDRDQTPESRAYLLNFAGSRYFIEQPPIADYAELDRRMRSGEL
SLAIEIPPGFGRDLLRGRPPEVGAWIDGAMPFRAETIRGYVQGMHQQWLADLARERGGAAAASPATIETR
YRYNPDFKSLPAMVPAVIPLLLMLIPAMLTALSVVREKELGSITNLYVTPVTRLEFLLGKQLPYVALAML
NFLLLVLLAVFVFGVPLKGSFLALALGALLYVTATTGLGLLISTFTRSQIAAIFGTAILTLIPAVQFSGL
LDPVSSLEGAGRLIGRIFPATYFLTISRGTFTKGLGFADLWPSFLALAAFIPVLLGLSVLLLKKQER
>gnl|CDD|411427 NF033859, SMEK_N, SMEK domain. The SMEK domain is named for four genera in which multiple, diverse members of this uncommon family of bacterial proteins are found: Staphylococcus, Mycoplasma, Escherichia, and Klebsiella. Members of the family are highly variable in length. This domain occurs as the N-terminal region. The four scattered invariant residues in the seed alignment, which may provide a clue to function, are Glu, Asp, Gln, and Lys
KEYINNIEEKLAVLATEIELRTKLNLLDINIHSENFFIPLLNILYGYNLVNLNQIKQNFPGIDLIDEKNK
IAIQVTSTATKEKIKKTLDKFIKKKYN
>gnl|CDD|468211 NF033860, Wzy_O6_O28, oligosaccharide repeat unit polymerase. Members of this family are oligosaccharide repeat unit polymerases in a subfamily that includes the Wzy proteins for polymerization of the O-antigens O6, O28, O39, O59, and several others
KPRKLILLLYIIANIISFIYFIITGELGGDFSGVEINLSNILLLIILLLILLFFLFLYLLYKLFKKIKVK
NKSIIKNSKRLGIFIFILQILFIIFNIYTGVGKAGVSNSSVSSPLSYLFIILNPDLLFLIYYFYLRKNKL
FKLNVILYLISSLLRGWTGFLLILFLLELRYRKRKKKIKLKKLLILLLLFILLYPFIYELKWYIRGSGFD
VSSISSDGYLDSYFDSLGKLIGRFQHVSNVAYIIENSDYLSSLYQNGNFLPFYFEGLLQPIIPKLFGIKD
FRSLNNYVAESFIPDSGDNWSSNIGLLGWLFILPEKSIFYIIYIFILLFISFFLSKKISGNYSFNLLLWL
FLLFLLFHGWFGAYFNYIQALFIFLIIILFLNGI
>gnl|CDD|411429 NF033861, sm_mem_Ecr, Ecr family regulatory small membrane protein. Ecr, as described in the genus Enterobacter, is a small membrane protein predicted to span the inner membrane. It was found to modulate expression of PhoP, part of the PhoP-PhoQ two component system, which in turn induces the arnBCADTEF operon, leading to modification of LPS and conferring elevated resistance to colistin. The form described in PMID:31169899 (WP_048029797.1), at 72 amino acids in length, is aberrant compared with the typical length for the majority of family members, about 46 residues
MSKTEIILLIIILLILIFGLWFIFSGEIWLLVSYLENSLYPTFDAP
>gnl|CDD|468212 NF033863, immun_TipC_fam, TipC family immunity protein. This family is named for founding member TipC1 (previously TipC), an immunity protein for the toxin TelC, which is a type VII secretion system (T7SS) effector lipid II phosphatase
KKILGLVILVVLLLSGGFYYYYISQPKNIFDEIYQETKKTYRSNNIFRQIIGSDIKNRKYTPFITYDYKK
LPNDYSEISLGFNFSEETKGISIRYEKQLASGVYLWINYKYDYKKKTLTKEVAISDEDDNSNNYIDDESQ
VKEYLEKYGITAKDLDKKSDEILNQKVLKDWCSIYSSRYSPDNYGDVTIETQ
>gnl|CDD|411431 NF033864, cytochrome579, cytochrome 579. Cytochrome 579, as described originally in Leptospirillum from acid mine drainage, is an abundant red cytochrome that acts as an electron transfer protein involved in Fe(II) oxidation
AVMGAAVLGFASATAFAAELDILKPRVPADQLAAAKAMKPPFPVTADAIAKGKEVFNGAGTCYTCHGVAG
DGNGPGAAGMDPSPRNFTNHQFEQVRTSGEMFWVVANGSPLQPAMVGFVSAGQITEKQAWEAVIYERSLG
CGGDMDCVAGSADWVGKQPVHEEAAGNLKPEYLNASAK
>gnl|CDD|468213 NF033865, fusolisin, autotransporter serine protease fusolisin
MRKEILKSKMMLIALASILFVSCGGGGGGGGGSSNLPLNPGTPSVPSTPSTPSNPEDSYPTVTNPLDSQK
GNMSALKTSLYNAQNNSGASIPKDTRELNGSGVKVAILDSDFVDAARRKRYLTNRYPGIEILPRTKNGPT
GSEHGEEVLEVLRDTDYARTKGKNKIGAIAGSIGMEGGVNKEKIGAVLPTKETYEAALARFGPNQKVKVF
NQSFGSDKTIEDARYNNYRFANIASGDDSKPMLPYFKDAVNNKGGLFVWAAGNTLNKTEFNNASLEAGLP
YLDNELEKGWISVVGVKKKEGGKLNIHYGTDHLAYAGDEAKYWSISADAESIDSKGRVGRGSSYAAPRVT
RAAALVAEKYDWMTADQVRQTLFTTTDKTELDADPANENETKLRNVTTSPDSKYGWGMLNQERALKGPGA
FMNISKYGNTNIFKANIPAGKTSYFENDIYGDGGLEKLGKGTLHLTGNNSFAGGSIVTEGTLEIHKIHSS
PITVGSGGTLVLNPKAIVGYNVSSFTLIGTVDPQKITDSGIKVKNYGTVKFNGTTAIIGGDYVAYNGSTT
EVGFKNSVKVLGKIRIQNGNVSILSNDYVTQNETATVMEGKSFEGNIANVETNGMRKANVEVKDGKVVAT
LSRQNPVEYVGENAEASSKNVAENVEKVFQDLDQKVLSGTATKEELAMGATLQTMSTSGFTSATEMMSGE
IYASAQALTFSQAQNINRDLSNRLSGLDNFKNSNKDSEVWFSALGSGGKLRRDGYASADTRVTGGQFGID
TKFTPTTTLGVAMNYSYAKANFNRYAGESKSDMVGVSLYGKQDLPYGFYTAGRLGLSNISSKVERELLTS
TGDTVTGKINHHDKMLSAYVEIGKKFGWFTPFIGYSQDYLRRGSFNESEASWGVKADKKNYRATNFLVGA
RAEYVGDKYKLQAYVTQAINTDKRDLSYEGRFTGSSVKQKFYGVKQAKNTTWIGFGAFREISPVFGVYGN
VDFRVEDKKWADSVISTGLQYRF
>gnl|CDD|411433 NF033869, viru_reg_Rsp, AraC family transcriptional regulator Rsp. Rsp (repressor of surface proteins), as described in Staphylococcus aureus, is a large protein with an AraC-like helix-turn-helix DNA-binding domain. Regulatory targets include the accessory gene regulator (agr) operon, which in turn regulates a large number of virulence factors
MTCTLNIHEQLSTAPSRNINQIIILFSLTNELRITINGETKDLDNHIAIINHGDIYNINQGSNLVELSIP
VFYFYIEDNDFFNCYFDRHLLQSSHYIKSLILQLIHHDSNNEEQDDQVISKIIQTLYKEAVVRHPHLYIP
NIAVNNPVFINCLTFIHDHISSNLSLRDVAQHCNISESYCSNLFVRYLNMNFKDYFTSLKLCHAIQLLLS
TNHSINAISELSGFSSHTNFTNQFKNYLNFSPKQFRTLLSKIDPLPQIHFSSDIVAQFLELISQFEFTDQ
LATETTEIDIDHFNPKDHTQRSKAFIRFNNFNELFQFVFNEYYDIDLSYLPKPVILINDISDIEMSQINY
NLLNRCFEKLFEKNIGLAMTIKSTQQFETIYQLILTFLQNNQDYKKNKKLVKFMLVFDSESMTIHDIHLC
HLKIKNKNRNIKYGVTVDGLLHQYSTLQETYDIMKRLNFDYYFIDIENIETKNLLITKSKGFTHTSTHFE
NYKQFILDSGIPSTKFVYNNLSLKCFKYTNNGTNPLQLSDLVCHLIALLRYGGGISYQLIEDDSMYISLF
NKYGSPLPLMHLYKMVAAFVNEPIEITNNYLMSRKDGNYHFLLFNKINDRYLSDSKQHFIFKNNLKENSL
IIVKTLNHEHGSIQNLLPQDKQLVYIEKEILDQLDRSNYPKTELAIQEEDNKTFEITLKHDEVKYICIKP
S
>gnl|CDD|411434 NF033870, VOMP_auto_Cterm, Vomp family autotransporter C-terminal domain. The Vomp (variably expressed outer-membrane proteins) family, as described in Bartonella, consists of autotransporter surface proteins including collagen-binding autotransporter adhesins VompA and VompC
GSTEAITGNQLYSMSNQLAAYFGGGAGYENGKWTAPTFKVSQFNADGSTVEKKSYNNVADAFGGVNKSMS
NINNRINDVINKVDSDGLKWNEDKGAYDASHNGKPSKIKNVADGKIEKGSKDAVNGGQLWETNERVSGVE
NDVNHIDKRVTVTNIGETVNNIKNIVNDLADGAVKYDKDEDGKKTNKITLVGGDESEPVVIDNVADGKIE
KGSKEAVNGGQLHDYTEEQMKIVLDDAKKYTDERIKNIVVDAIDDAVAEAKSYTDMKFEALNYSIEGVRK
EARQAAAIGLAVSNLRYNDTPGKLSVAFGSGLWRSQSAFAFGAGYTSEDGKIRSNLSATSSGGHWGIGAG
LSLTLN
>gnl|CDD|468214 NF033871, deAMP_SidD, deAMPylase SidD family protein. The founding member of this protein family, SidD from Legionella pneumophila, is a type IV secretion system effector that acts as a deAMPylase of the host protein. Homologs are found in several other Gammaproteobacteria, including several different Legionella and Coxiella species
IITQQCNGVVAGKTYHSSRNLLDKGNSEIFASSLFAHFDKGKRIAKKKNSDDKIVIGYTHDGLPFQIVVD
GFYGGETQHTFDFIDTYIVPLIENYSLKLSIEADPKDVTENLIKTIYTLRAQHLSGAEFTMSLAITYQKD
GELYCAGFGIGDTGIAIKRTDGEIEQLVYHQEVDGFKDAF
>gnl|CDD|468215 NF033872, SidA_fam, T4SS effector SidA family protein. The founding member of this protein family, SidD from Legionella pneumophila, is a minimally characterized type IV secretion system substrate. Homologs are found in a wide range of Legionella species
LSEKMQKLKKRINDLLLEQKSFIEIIHKGSKLSSTILEGIQKIFNLIASIFSSSKEIPIIGFVFQMLSVI
PNAITTLTDKKKSIAEKILAGILLLVITALSITAFVLGGIVAAIIGLVFSSLTTLFEGISFIGSIINKYQ
TSKAYKEKKEFMDLLEKRNYPLENDKYREQLEIRALELEHLLEKSDLKKEEKEKLKEELEFINDILKKKG
ISLGPNDESSASKLSKLYKDRKEQLSYLAEKLELIDETKKLEEKSELIDEISELQKEIAKTDKDIENITK
PLHELKRENLLANEKIALSYSTFALGGAGVILSTIGLLILVGVVAAPPILGPILLGFGIGLAVFGLIKWG
AEKYAEREDEKIMEEREEEQEEIILEEAL
>gnl|CDD|411437 NF033873, SidJ_poly_Glu, SidJ family T4SS effector polyglutamylation protein. SidJ, called a pseudokinase because its polyglutamylation activity differs from what might be expected from its kinase-like fold, is the founding member of a family of such pseudokinases. SidJ itself, as described in Legionella pneumophila, is exported by a type IV secretion system (T4SS), and modifies and modulates the activity of T4SS effector SidE
PVKQFRFAKIGETDTHDKSLLPAVKFVSGRSIPLKEIPFETTRSELIQIYLLSLDQCIKANKLKEIPPQA
LAGHYLLIKSLAAVAQNKTEKSQLLNLEKPFANYLKSKESSIWSMVNEYTRDSEFPIVQWLKNQSSNSNF
MVSFIIDNNKGTLTRNQNAFIQQFKDSPAFFFPNPIYMSWLTHSYEKDSSLNPMYNISKKTHYYHATITD
NLLLRTQPKQVTFAPKHYYQKGKGIVDTDFRYTMNQSNLLRIQGRTLLFTDESNELIAVKVQKKGEPKSN
LTEEFQMADYLLKHQNRLDLQSQLPTPLGQYSVKRTEILEKCRKSPHYEQFLDLISDTKDLEVYVYKAPV
SYFTYLHDEHQSFRDFTASVKKNVHDLFVLLREGIVFSQLADIFHTHSDEEERVDKGRYQALVQLLSVFQ
SQLGRLDKWQKAVEFVNLRASGIADLGDSLPITSLLTSSEFTKKYFSELLTGGYHQTFFDSSSGTASSLY
TGKRKLFGNYLYLNTIAEYLLVIQLVLGSYGDKVTRKIDDKSKKQKMWQQLAELMFDSCAEAVTLMTGIP
HSRALALLNQRAKIDNHLQQTQFWMTPDYADLDESEMRMQQYVLYPGEAGYEINSELVPGIGLSVDGVNQ
DLGGYNQELPLRELEKLLYATVTLIEGTMQLDKEFFKQIEQTEKLIASACSAEDCYQAVAKLLDMARPGC
HFQKRLALSYYEEIKLKYPSSSQTDIDKRFEKVEKHFAVKTIQSFWREYLAHKKLVSE
>gnl|CDD|468216 NF033874, SidJ_rel_pseudo, SidJ-related pseudokinase. Members of this family are uncharacterized but exhibit strong local sequence similarity to SidJ, a protein that exhibits a protein kinase fold, but that surprisingly exhibit a different activity. In the case of SidJ itself, the activity is polyglutamation activity. For this family, the activity is unknown
LDFSAAYLAVRNLRRLIERNPDSIDPETVSALESLLESPRHSSQRQAFFLYREAAEALAALLRSGDPPLS
ASALSALLDLLLTSTGKAHRAAAEALGSLPLLLIGPPEPPEPPAEAIPSISWDELLRALGKPIADLAAPR
WQGRSLVAPLAGGRLLVVKFARSGENPEGLAREAAWMERLARSEGDSFPVRFDIPRPLRIGGRYLFRLTG
IPDTIPPPPGLHPEGYAIAFIAHKDYFVYPNDPRPGRRLSKEEFKEVMGRNAWLLGRLASRGIVHTAPIP
LFHNRVQQGRREDGGLYEWERGGRLDRWLDSCRYPNFGLSGLRDFEHLEALKGSGRRLYRYIGTHLLSLL
LVAGSYFRNKDPELRGLDPDGNPVDARHLFDKDLLEELITGIFENYYEGFTGKEFTGELPFDLEELARRM
IEEMGVDRHMEEILRVADQEEMTDEEFRDFLLSRGMSPEKAAGLKKGEEDITLVTGPHLGGFNQRISLPE
LIEFVATASALCIAGRYL
>gnl|CDD|411439 NF033875, Agg_substance, LPXTG-anchored aggregation substance. Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain
MKQQTEVKKRFKMYKAKKHWVVAPILFLGVLGVVGLATDNVQAAELDTQPGTTTVQPDNPDPQSGSETPK
TAVSEEATVQKDTTSQPTKVEEVASEKNGAEQSSATPNDTTNAQQPTVGAEKSAQEQPVVSPETTNEPLG
QPTEVAPAENEANKSTSIPKEFETPDVDKAVDEAKKDPNITVVEKPAEDLGNVSSKDLAAKEKEVDQLQK
EQAKKIAQQAAELKAKNEKIAKENAEIAAKNKAEKERYEKEVAEYNKHKNENGYVNEAISKNLVFDQSVV
TKDTKISSIKGGKFIKATDFNKVNAGDSKDIFTKLSKDMGGKATGNFQNSFVKEANLGSNGGYAVLLEKN
KPVTVTYTGLNASYLGRKITKAEFVYELQSSPSQSGTLNAVFSNDPIITAFVGTNNVNGKDVKTRLTIKF
FDASGKEVLPDKDSPFAYALSSLNSSLTNKGGHAEFVSDFGANNAFKYINGSYVKKQADGKFYSPEDIDY
GTGPSGLKNSDWDAVGHKNAYFGSGVGLANTPGRISFSFGMTTKGKNVPVSSAQWFAFSTNLNAKSIKPY
QNKGNPKEPEKATIEFNRYKANVVPVLVPNKEVTDGQKNINDLNVKRGDSLQYIVTGDTTELAKVDPKTV
TKQGIRDTFDAEKVTIDLSKVKVYQADASLNEKDLKAVAAAINSGKAKDVTASYDLHLDQNTVTAMMKTN
ADGSVVLAMGYKYLLVLPFVVKNVEGDFENTAVQLTNDGETVTNTVINHVPGSNPSKDVKADKNGTVGSV
SLHDKDIPLQTKIYYEVKSSERPANYGGITEEWGMNDVLDTTHDRFTGKWHAITNYDLKVGDKTLKAGTD
ISAYILLENKDNKDLTFTMNQALLAALNEGSNKVGKQAWSVYLEVERIKTGDVENTQTENYNKELVRSNT
VVTHTPDDPKPTKAVHNKKGEDINHGKVARGDVLSYEMTWDLKGYDKDFAFDTVDLATGVSFFDDYDETK
VTPIKDLLRVKDSKGVDITNQFTISWDDAKGTVTISAKDPQAFILAHGGQELRVTLPTKVKANVSGDVYN
SAEQNTFGQRIKTNTVVNHIPKVNPKKDVVIKVGDKQSQNGATIKLGEKFFYEFTSSDIPAEYAGVVEEW
SISDKLDVKHDKFSGQWSVFANSNFVLADGTKVNKGDDISKLFTMTFEQGVVKITASQAFLDAMNLKENK
NVAHSWKAFIGVERIAAGDVYNTIEESFNNEKIKTNTVVTHTPEKPQTPPEKTVIVPPTPKTPQAPVEPL
VVEKASVVPELPQTGEKQNVLLTVAGSLAAMLGLAGLGFKRRKETK
>gnl|CDD|468217 NF033876, flagella_HExxH, flagellinolysin. Flagellinolysin is a variant form of bacterial flagellin in with the normally hypervariable central region contains an M9 (MEROPS classification) family metalloprotease domain, with its signature HExxH motif. The founding member of the family, from the pathogen Clostridium haemolyticum, shows EDTA-sensitive metalloprotease activity. The large count of flagellin subunits in a complete flagellum means the capacity of flagellinolysin to perform as a protease may have implications for host-pathogen relationships
LQKEINQLKQEIDRIAETTEFNGKKLFDQGASVGSADPDKQAILDGLKSGWLENAEDLIKEYYGLTADGA
DLTVNLEYTDGAGGTLAYVSSGSGGGGKGGNLTLTIDMADFSPANLPNGGTAPQYLDRTIAHEMVHAVMG
RTMNFSSLPTWFIEGTAEFIHGADERLAADLAGGTSDAAGVAALFNGGAWTSTSADYSAGYAAVRYLHDQ
IKAAGGGGIKDIMQYLKANAGSTLDQALAAATGGAFATEADFLADFNANGAAFIKNYMDLTNADTGAIGG
LDADGGPVLTAESVVPDTGSYPGEDPLSGFNVIWPTFSGAGTTVQLQVGANAGQTIEISFGDMSAEALGL
DDVDVSTDATSAIDIFDKALDYVSNQRAYL
>gnl|CDD|468218 NF033878, thiovarsolin, thiovarsolin family RiPP. The thiovarsolins, named for a founding member from Streptomyces varsoviensis, are RiPPs (ribosomally synthesized and post-translationally modified peptide). As with the thioviridamides, thiovarsolin precursors are encoded in loci that encode YcaO and TfuA family proteins, suggesting post-translational modification by thioamidation
LDDLAELNPEQLQSFLEERSGAAVHGATDAYFSGPRAQTVRGAGDSFFAAPRAQTVRGAGDSFFAAPRAQ
TVRGAGDSFFAAPRAQTVR
>gnl|CDD|411442 NF033879, smalltalk, smalltalk protein. Smalltalk is a membrane-associated protein of very small size (less than 35 amino acids), found broadly in Bacteroides and Prevotella, both of which are prevalent in human gut microbiomes. Genomic context suggests a role in crosstalk in the gut microbiome, whether that involve toxins and immunity, signaling, or some other form of interaction. The family was identified and discussed by Sberro, et al., in a screen for overlooked small proteins encoded within human microbiomes, and named smalltalk here for its small size and cross-talk role
KKSTWKKILKVIIAVATAIAGALGVQSCM
>gnl|CDD|411443 NF033880, Prli42, stressosome-associated protein Prli42. Prli42, as characterized in Listeria monocytogenes and found broadly in the Firmicutes, is a membrane protein of very small size, essential to the function of the stressosome. It appears to be related to DUF4044 (PF13253)
MSNKKFQKIIVYLMLIAMLLSTLLAGLSMFL
>gnl|CDD|411444 NF033881, aureocin_A53, aureocin A53 family class IId bacteriocin. Members of this family include leaderless, unmodified class IId bacteriocins such as lacticin Q, BacSp222, and the founding member aureocin A53
MAAFLRLVAKLGAKAAKWAWANKGKVLEWIKDGMAIDWIIDKIKKILG
>gnl|CDD|468219 NF033882, T4SS_lipo_DotD, type IVB secretion system lipoprotein DotD. Members of this family are the lipoprotein DotD from type IVB secretion systems, which are also called Dot/Icm secretion systems. DotD is is related to conjugal transfer protein TraH as that term is used in IncI1 plasmid transfer regions
LTGCKTVTYKKPPPNPPSDDAQIQLAEAATSVSDSLQELAAVEKAAHPPKKLNTPPIPAAYGMQGLASVD
WSGPIEPLLKRIAKAAHYRLRVLGKEPAIPVLVSISAKNTPLADILRDIDYQAGKKANIVVYPNSRVIEL
RYA
>gnl|CDD|468220 NF033883, conj_TraQ_IncI1, conjugal transfer protein TraQ
DAVQMLVNFANGLFSSGINLLWSLGALVGIIGAIGYLARARRAARKPGGRPVSGGKTVAVLLLCAGLISL
SQMINAGGAQFGFGDVSFDAISYVSASTFGAAAEAVNAVLTLARLAGVGFFLRGLLILRRSLLDGHTGLS
AGEDVSRGLVKFICGVLLVCNPYVLDALQATLGLH
>gnl|CDD|468221 NF033884, conj_TraO_IncI1, conjugal transfer protein TraO. TraO, involved in the conjugal transfer of plasmids such as IncI1 plasmids, shares homology with IcmE of type IVB secretion systems
ALIGLAAVVLAGGGYLLWTWLSTPSPTQSSVNLNRVAGGTGRTTQESPQYRELLREYNERGAAQAERNGQ
SFIASLSAGQDVPDPPTAKAPQQQPQAPDPVPYYQQPSQPQQEGEAAKRKKRVEALLKLLAAQWAPVPHG
LALPTGGAAGGNGAYAGSISPATVSGGGGASQTAALQGAASSTSVADTDVVVVPALTRVPAVIDTAVDSD
NPNSQVLASIPAGPYAGAVLFAPGVKLAGDGVDIHFTRMEWNGMTYKVDAYALDDDTLRSSVASDVNNRY
FSRIILPALAGGIGKTGQLYEDANTQIITNNGGTITGRPGMPDGKAVAGTIAGGMAQQAGQVLTNDAARL
PVKQVTVDRGQVVAIQFMGPVYSSDALAPGA
>gnl|CDD|468222 NF033885, conj_TraP_IncI1, conjugal transfer protein TraP. Members of this family are the conjugal transfer protein TraP, as the term is used for the member protein from IncI1 plasmids and for their homologs. Note that the same terminology may be applied to unrelated proteins from other forms of conjugal transfer system
LPFWKRPLFWGLSLPWWGGIALILLAAVVYLFLPSPSEQTGASFNAAPPAVQEAQQPSPQEEVVQSPPAS
AVPPSPGEDLSQLARDLKEELDDRLEALRSTITKLSEGITALSEALKKDEQQIQELKQQLDRLRARLNSL
QTQPPAPATTGTPASRRKKTRSPLSGMRINSLSNGMAWIRWQGSTWAVREGDQLGGITITGIDPAKRTVT
TSAGVIR
>gnl|CDD|468223 NF033886, T4SS_DotA, type IVB secretion system protein DotA. This HMM distinguishes DotA of type IVB secretion systems from TraY as the term is used in the conjugal transfer systems of IncI1 family plasmids
SDYSVVFLGQIFGVVDGVLHGTGSQILGTMFGVFNSAVLALGGIIIMYTLVVSTMNTAHEGEFLGQKWSS
IWIPLRSVLGLALLIPKASGYSLIQIFVMWVVVQGVGAADKVWNAALDYLNRGGVIIQPAASLTSDSSGA
SGIATGAGTILQGQVCMLGLQKQLENQRQSYLNAKSNGPCSPSSQMQSFCNTAVPDFLSSVNAVAVQNNN
SYSVDMPNFDSGSPYAFLNGICGSLTWNSISNASVGNSSTTLTSAELLTAQMSRAIAIQQMYLDLSAVAQ
VMVNNDPQLPPTSSTNATNYSPVATQQFGVPYTASGTPCNSSSNCVTWGPDPGSSTPLFNGTEFQNAIND
YNGIMLPALNLLNQANSSSSASASRDFIQQAKNQGWIMAGSYYFNLAQLNNQTDSNTGLDGSTFPTQLTS
PFGGDKTSLNQVQTLINGSPLSSNLPAVGGALSSTVYGFINNSLMVQLPGQPGLSPPTFANNINFSLYSL
PSQSFSCGKLGGILGNIFYNIIFVNVYNFFLNLFGQIINSVVMAFQGMATIFQQGVQIIAQPGVNPIVAL
ANMGNGLINFAENLWIALLGIAIASALIPLFGIFIFALLSLLMPLLMAWLGVLFSIGFVLAYYVPLIPYM
IFTFGAIGWLIAVIEAMVAAPLVALGVTHPEGHDALGKAEQAIMLLLNVFLRPSLMIIGLIAAILLSYVA
VWILNAGFGTAIAFIQASTTWANSGSSSGYSGWAGIYAFFFSILIYTTLYLTVVNKSFSLIHVLPDKVLR
WIGGQAE
>gnl|CDD|468224 NF033887, conj_TraX, conjugal transfer protein TraX
GWVALNIFLPLSETRRIARTAGRPLSKNLQRLRRLLPERQAEDYRSQEILSWEEAVAASGQTPEQLERRY
RRRKRLWWVLMWLPGLLALLLLLMLLLAASSLPGGTLLRALSTLLVLLALAALGFVKALICTYRLWQLRE
RRVSEAEKGTFRDFLAETRWIRQ
>gnl|CDD|468225 NF033888, conj_TraW, conjugal transfer protein TraW. Members of this family are the TraW protein of conjugal plasmid transfer systems, as the term is used for certain transfer systems, including that of IncI1 family plasmids. Note that an unrelated protein, also designated TraW, participates in the assembly of F-pilin subunits, involved in transfer of F-plasmids
SALAYPVNVNSSVPITTQVMPALATINGTLAEILTTQTQIGTAINQNGDKIAAVIEQAAQAQREQDIFAR
QTRRLEEARRSYSVPDSICSESASGGAAQVSAAARATQSSLSSGGGISNKAIKQALTSPAPAPEQDAYRS
AAIHAQYCTSEDYAAYGGTALCPSVSDLPGGDKQLRSLLDGAGKEGKAPDLTFSQEQTDAAMAYMKNSAR
RSAGRQLGKGEVKTASGRQYQGLMTQYNAIISAAAQPQLAMIAASQPNPATRDALAEALQAPSAAAYFDQ
TASSEAKRTGMMSAREFEAFEVGRRYANTDYQTDLQAMDGDNLLREQIRVQSLNNWLLLGIKNQLQKNNI
LAGQQLALLARQEYRPRLAAKLEQVSAGVA
>gnl|CDD|468226 NF033889, termin_lrg_T7, phage terminase large subunit. The phage terminase large subunit (TerL) is also called DNA maturase B. It oligomerizes into an ATPase that forces DNA into a pre-existing phage prohead to package the DNA. This TerL family includes members from phage T7 and phage T3, among others
DFRNFLYLVWNHLGLPTTPIQYDIADWLQHGPRRLMLQAFRGVGKSTITAAFAVWRLIRDPNLRILVVSA
SKDRADKMSRFVKRIIERHPLLEHLRPSAGDRWSAEAFDVGRALPDKSPSVKAVGITGNLTGSRADLIIA
DDVEVPKNSDTQTKREKLRELLKEFDAILKPGGRILYLGTPQTEDSIYNELPERGYTVRIWPGRYPTDEE
LENYGDRLAPPILDTGGGDDGLRGQPTDPERFDEEDLAERELSYGPAGFALQFMLDTSLSDAERYPLKLS
DLIVMDLDLDRAPEELVWGSAPGLRKDLPNVGLKGDRLYAPAWWDPAFGPYTGKVMYIDPAGRGGDETAY
AVVKDLNGNIYLHDVGGLKGGYDDETLRKLAKLAKEFKVPVIRVESNFGDGMFPALLRPVLARIYLPCGV
EEVRSSGQKERRIIDTLEPVLAQHRLVVHESVIETDFESEMRYPEWRPDYSLFYQLTRITRDRGALAHDD
RLDALAGAV
>gnl|CDD|411453 NF033890, DotM_IcmP_IVB, type IVB secretion system coupling complex protein DotM/IcmP
APLWIIALIFVAGLVIWYFFHTYIVSFVFYLRLYEIKLISFFLGDDLLDLLIYLMQTIDPATVDWNQLVD
ISREVGDYLRYPVILILLVLAALLYFSNVTLKFRKTYSMKTLRAQEQENWPQITPVVKLDLVKEDIDKGP
WAMALTPMEFAKKYNLLKKEDVVLDKPVPGKEMTATLRRGDAKRVFTLQLGPLWQGVERLPPHVKALFAV
FAARANRDRKAARKLLEQIAASAASGKLDFSGVDELLKKYENSKIVQWIVKRHAYVLTVMASLLEAARED
GVLASAEFLWLKPVDRRLWYMLNSVGRQTPFVEVAGPFAHWLAEKKLGRPLLVPMVDEAVKALEEAIKEI
LYVP
>gnl|CDD|468227 NF033891, surf_exc_IncI1, plasmid IncI1-type surface exclusion protein ExcA. The surface exclusion protein ExcA, as found in R64 and other IncI1 family plasmids, is not required for plasmid transfer. Instead, it is required for blocking transfer of closely related plasmids into the host cell
QRTKTRKEAWWYLIRLAYFLFGIPFLLFFGLVSLIMALSSRYSERRPEDYLYTTGSWLALIIPLGWFYSG
YKSRRRKLKKIVQVIKSDKFFDPDPEYEIYSEGSGKYFGIDTKNGTMLYVRRYPKNQMDVIGLTIDNWTN
REVEGKNKLRIYTKYPDLPMIEIQTPCAWARLLYDTLHAMAHRQYSYPVPFPRYVQEKRKELERDAGVPV
>gnl|CDD|468228 NF033892, XcbB_CpsF_sero, XcbB/CpsF family capsular polysaccharide biosynthesis protein. Two partially characterized members of this family are XcbB, as described in Neisseria meningitidis serotype X, and CpsF as described in Enterococcus faecalis serotype C. In the latter case, loss of CpsF converts capsular polysaccharide to serotype D
LLALARKNDEAKKLYKELLANDYILYGHKGGISRFVKRKRIYSLWPKDLIKYKDVFYTLIYPSGRKPNNG
LAPKKLLVIFSSMPASDFYDSLNRADRYFPKNFPSIEKSLVKNTYILRIADLNLVHGSFYLNTVNYPDYE
DDIQELIEKVAKELGIEKDNVVLYGASKGGTGALYHGLLGDYKTVAVDPILDDEYYLEEKNDRHFLKGLR
FPDLKPDINALLENSNLSPENKIVIGSSNVSPQYPYIKRLNLLLSKITLINLNDSNIKSHPDVSRNTVPE
QLTLLNQLLLG
>gnl|CDD|411456 NF033893, pheromone_ipd, peptide pheromone inhibitor Ipd. The pheromone inhibitor iPD1, in mature form, is the last 8 amino acids of the product of the ipd gene. It was described in conjugative plasmids of Enterococcus faecalis
MKQQKKHIAALLFALILTLVS
>gnl|CDD|468229 NF033894, Eex_IncN, EexN family lipoprotein. Members of this family are lipoproteins, typically associated with mobile elements such as phage, and related to the entry exclusion protein Eex of IncN-type plasmids. Members of this family tend to be small (shorter than 90 amino acids) with three invariant Cys residues, one of which belongs to the lipoprotein signal peptide. This family shares some similarities with TIGR04359, which includes the entry exclusion lipoprotein TrbK of IncPalpha-type plasmids
KIILTLLLLCTGLLLAGCSEKTYSVDWYKAHPDELKEVLAKCKKNPGELADSPNCRNAREADFKL
>gnl|CDD|411458 NF033896, MFS_LfrA, efflux MFS transporter LfrA. This efflux transporter, as characterized in Mycolicibacterium (Mycobacterium) smegmatis, provides low-level fluoroquinolone resistance (lfr) when overexpressed
MSTCLDATPSTTRTPRRAWLALAVLMLPVLLIAIDNTVLAFALPAIAEDFRPSAATQLWIVDVYSLVLAA
LLVAMGSLGDRIGRRRLLLIGAAGFAVVSAAAAFAPSAEYLVAARAALGVFGAMLMPSTLSLIRNIFTEA
SARRLAIAIWASCFTAGSTLGPIVGGALLQHFHWGAVFLVAVPILLPLLVLGPRLVPESRDPNPGPLDPL
SVVLSFTAMLPFVWAIKTAAHDGLSAVVAAAFALGIASGVLFVRRQNRSATPMLDMGLFRYGPFTSSILA
NFLSIVGLIGFIFFVSQHLQLVLGLSPLTAGLVTLPGAVVSMIAGIAVVKAAKRFAPQTLMVTGLVFVAA
GFLMILLFRHDLTVVAVIVSFVVLELGVGVSQTVSNDTIVASVPAAKAGAASAVSETAYELGAVVGTATL
GTIFTAFYRANVELPAGLTPAQTGDAGESIGGATSVARDLPAETAAQLLDSARTAFDSGIAPTAAIAAVL
VLAAAAIVGAAFRR
>gnl|CDD|468230 NF033897, GUMAP_C, GUMAP protein C-terminal domain. GUMAP (Giant Ureaplasma Membrane-Anchored Protein) is a very large protein found in several species of the genus Ureaplasma, a lineage that resembles Gram-positive bacteria by ancestry but that lacks a peptidoglycan cell wall. GUMAP proteins average about 5000 amino acids in length. Near the C-terminus, these proteins have a strongly hydrophobic segment followed immediately by a cluster of basic residues, as is characteristic of proteins with a C-terminal membrane anchor. Because of the potentially large computation cost of performing database searches with a protein profile HMM that is thousands of residues long, this HMM models only about 750 amino acids of the C-terminal region of GUMAP proteins
TTSEYTIIDDNYYNFSRLDGNEIFKKVKNLKKLFDQLKKKNQNLNFEDEILSKEEEDNLELLEIKKNDAN
LFDLNDLKLMLSAPENLVLNLEKNQPKYVYLINNVPYVLSEKDINIHFPSVDEVIANNGNIEDAVLKKIK
NLPRNEGGNVNLGGKLINPNYVEVIAREDGTIKIFTKDPLKPNLKTLIVAIGPPDNNFKNPVFLNDAVSA
KDHRKLIKIYEIFKQAIPKEKNLNQTLISNLWINQNIISLYSKKKDPDGLVDSFKDDWTVQYNPNLDKII
FKGGNKDVSKRAVVIVINNVKKVINASELYNNNDVLDNNNTPISISDLIALNRQNINNKLINKNQIGEYL
VNNPTLVRTFIYNNNHAYLDKKQNAKYLIIKQKNDNDSVIIDDNNYLPYVIDKSIYKTALDQTIEQFNNE
LALNNGVAKLNEQPNQFINADLLNYPELTENLTDLNLKPAKISKIDDFLQIIGVDDDGKHIVLKIPTIPN
VVSKNSIPYISIDDVIKANGDLGAAIKNILNNENKYPRDKNGKIRVGNGNIDPDNVVVEIDKNGNVLLFY
RDPNNLKITKPLAKILVNKKDNEIVVDNYTGYYLQDLNESALADLLRDLNKNGQPKGKLKTSSEIFKDSI
IKNLLPKKFLDLSKATIEFDADSKKIIIRDNNPQNPNVFVIYTLPLPNSDVEENERVEYRAKDDYWRIWA
PVVSSIAAIIIAIVGIIIGIKKKKKRKKN
>gnl|CDD|468231 NF033898, QWxxN_dom, QWxxN domain-containing protein. The QWxxN domain is about 125 amino acids long, and appears typically as the conserved core region in up to 9 tandem repeats, each about 200 amino acids long. Proteins with this domain are known so far only in the genus Enterococcus, and may reach over 3000 amino acids in length
NKIVTAYINGRPSPIPTSEPLPPFWYDLELFQKRNKTEKVNEAVKKFLCKQGVSCKDLSGSELVLALQEW
IEKGGTYTEILERRKQLAYIILKAYGLEGEELSDTEARAIFLQWRNNNAFKGYTFKE
>gnl|CDD|468232 NF033899, T4SS_pilin_TrwL, VirB2 family type IV secretion system major pilin TrwL. TrwL is the major pilin of Trw type IV secretion system (T4SS) of Bartonella species. It is related to VirB2 of related T4SS and to the conjugal transfer protein TrbC. The Trw system is unusual for having duplications of certain subunits, and TrwL has divergent, tandem-duplicated copies, named in series TrwL1, TrwL2, etc
MKQLNILQSKINNKIIAISAAITVFFMTHPVYAQATLTNAKTALETLKTDLKKIIPIAAAVILLCLAIGY
AGRYIEKDTFVRWAIGVVIAGSATQLANMLFKP
>gnl|CDD|468233 NF033900, T4SS_IcmE_DotG, type IVB secretion system protein DotG/IcmE
FTNTRSRVIIIFTAVLLIIAVVVGLIKFHRSQEGSSAGSAVVRAPPGIQSIPGAGDPTAQYAKLQEQQNV
QQAQQALKTGGSAIPTIIRTQAVGSGVQFIGSQQGEGGVGFSTLAREDEAGTQKSLWLQKLNPANCSKCN
LQLARSQGVTALELLKQGCSCPQLKDAGYTAGELKQVGCSAKELKAAGFSARQLKDAGYSAKRLRAAGFS
ACELRNAGFSAQELKDAGFSDGELKGAGFSDSEIAAAGGLPEGITAADVRKAGCDAAALKKLRAAGVSAA
AIRRISGCSAAQLKAAGYTAKELKNAGFSAADLKNAGFTPAELKAAGFSARDLLNAGFSPSDLKDAGFSP
AELKAAGFELPPGITAGDVKKAGCDVDALLKERLAGGSAALILKYAGCSAAALKAAGFTAKDLANAGFTP
EQIIAALSDEAIRAAGCDPEKLKELRAQGVSAKRIRDLNGCSAAALKAAGFSAKDLLDAGFTPQELKAAG
FTPKQLKQAGLNPAAIIAAGRTADCSVASLAAARKAGVSAATIKQTLGCSAAALKDAGFTAAQLKAAGFT
AAELKNAGFSAAELKAAGFSAKELKDAGFSAADLKDAGFSAGQLKAAGFSAADLKAAGFTAAQLKAAGFS
AKFSAKDLKAAGFSAAELKAAGFSAKELKAAGFSAGDLKRAGFSADELGAAGFSAAELLNAGFSPGASVA
GLQQAALVPSGITSASAAIPSIGGAASATAAAAPAQRLQAILKRQQQQMADQQYQQAIQQRQSQMLSAAN
QLLQTWKKVSAQTYTAGPPEEANAGGAPGNAGNAPGGASGNAPATATGAGGMAQKAIIKTGTIMFAVLDT
SVNSDEPGPILATIVSGKLKGAKLIGSFNLPSNADKMVISFNTMSVPGASKTISINAVAIDPNTARTALS
GRVNHHYLLRYGSLFASSFLSGFGNAFQSANTTVTIGGTGGGDNITNQNGIGRSTLENAVIGLGTVGKSW
GQVAQQQFNTPPTVEVYSGTGIGILFTQDVTL
>gnl|CDD|411463 NF033901, L_lactate_LldD, FMN-dependent L-lactate dehydrogenase LldD. LldD is an FMN-dependent L-lactate dehydrogenase. It occurs in E. coli, Salmonella, and as one of two L-lactate dehydrogenases in Pseudomonas aeruginosa. It is unrelated to the NAD-dependent enzyme
MIISASTDYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETKLFGETLA
MPVALAPVGLTGMYARRGEVQAARAAAAKGIPFTLSTVSVCPIEEVAPAIDRPMWFQLYVLKDRGFMRNA
LERAKAAGVTTLVFTVDMPTPGARYRDAHSGMSGPNAALRRMLQAVTHPQWAWDVGLLGRPHDLGNISAY
RGKPTGLEDYIGWLGNNFDPSISWKDLEWIREFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQL
DGVLSSARALPAIADAVKGDIKILADSGIRNGLDVVRMIALGADSVLLGRAFVYALAAAGEAGVANLLDL
IEKEMRVAMTLTGAKSIAEISRDSLVQ
>gnl|CDD|468234 NF033902, iso_D2_wall_anc, SpaH/EbpB family LPXTG-anchored major pilin. Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis
MNKFTKTCVAAVAAAAMALTLCVAGAVGAAAAAWAAAAAAPAGNIDLDKTGTSSITIHKYLGPPATGTGG
GTKGTGDSAAGGKPLKGVTFTITKVTKIDLTTNAGWAKIAKLTTAAAGTAAAFATTLGDTTKTTTTTGTT
DADGTAKFSNLPLGLYLVEETDAPYSVVVKAAPFLVTVPLTNPTGNATKWNYDVHVYPKNQKLSDKVTKT
KDVTDAVGNGVGDTITYTITAPVPKIDANTLDDFKGFTVTDTLDTRLDEVAGVVKSVKVGGTGLTATLTV
TTDYTVTTDGLTADQKVTVTFTEAGLAKLAAAKNVKVTVTFKTKVTKTAKGGTNGEITNKAGLIPNNPGP
NTPEPTTPGTPDPTPTVKTYFGKLKIKKVDADDTSKKLKGAEFKVYACEADAAAACVNAIGINGKTTFTT
GADGTVSIDGLHVTDLEDGASVKAAAGKDYCLVETKAPAGYVLPPKPVEVTVVKVTVTAATTADVKNTVV
NNKKTVPNWFFNLPLTGGAGVIILAAAGAALLGAGAFVALRNR
>gnl|CDD|468235 NF033903, VaFE_rpt, VaFE repeat. The VaFE domain, about 121 amino acids long, typically occurs as a tandem repeat in sortase-anchored surface proteins of Gram-positive bacteria. A single protein may from one to over fifteen VaFE domains. The domain is named for a particularly strong motif with a nearly invariant Phe-Glu residue pair. The function is for the VaFE domain is unknown
VAVHADINDEGQTVYFPEIGTTATDKADGDKEVVADKKVTIVDTVTYKNLIPGKEYTVTGTLMDKETGKP
LLVDGKPVTAETTFTAEKADGSVEVTFTFDASALAGKTVVVFEKLYYEGKE
>gnl|CDD|468236 NF033904, LlsX_fam, LlsX family protein. LlsX, as found in Listeria monocytogenes, is a small protein of unknown function, encoded in the island responsible for listeriolysin S biosynthesis and processing. Related proteins are found in additional Gram-positive lineages, such as Streptococcus sobrinus and Lactobacillus sp
KQVLRIIIEIIIGILLSMLLLSILISFGYAHAYATGLAEYNVNLLGLPIYRITKVGGEYSGTPNNQNMGL
IGVICSLLLVILVELRHRLK
>gnl|CDD|411467 NF033906, ExsE_fam, T3SS regulon translocated regulator ExsE family protein. ExsE, through protein-protein interaction, serves in a regulatory cascade that modulates the role of ExsA, a transcriptional activator of Pseudomonas aeruginosa's type III secretion system (T3SS) regulon. ExsE itself is a substrate for translocation (i.e. removal) by the T3SS system, providing feedback that modulates expression of secretion system genes. Homologs found in multiple species of Aeromonas and Photorhabdus may be functionally equivalent. Note that VP1702 from Vibrio parahaemolyticus, given the same gene symbol and ascribed an equivalent function, appears unrelated in sequence
MKIQESQPSPALQVAEENKVGCFAGRTMSAVPPRASQAPLSALLRRSIALDQVQELALQRLQDGEHTPLS
ERRIRVL
>gnl|CDD|468237 NF033907, ExsE2_fam, T3SS regulon translocated regulator ExsE2. ExsE2, as described in two Vibrio species, is called functionally equivalent to ExsE from Pseudomonas aeruginosa, but appears to lack detectable sequence homology. In each model organism, a type III secretion system (T3SS) contains a DNA-binding transcriptional activator ExsA, an anti-activator ExsD that binds ExsA and inhibits its activity, and a secretion chaperone ExsC that can bind to and counteract ExsD. ExsE2 (in V. alginolyticus) or ExsE (in P. aeruginosa) can bind its chaperone ExsC until it exits the cell by successful T3SS translocation, providing fine tuning of T3SS gene expression through these interactions. We renamed the Vibrio family from ExsE to ExsE2 to help minimize confusion between these two very dissimilar families
MSNDIQPTRNNSSIHTLESSTQTNSVPQGTFLGRTVVLISPSEREQNRANSKLELSEQLSQLANLELCNS
VLSFEKKDQNAIQSLLNRKVQVI
>gnl|CDD|468238 NF033908, AcfA_fam_omp, AcfA family outer membrane beta-barrel protein. AcfA (accessory colonization factor A), as discussed in Vibrio cholerae, is a porin-like outer membrane beta-barrel protein. It encoded in a locus with other proteins also termed accessory colonization factor, near the toxin-coregulated pilus genes, and its presence aids in intestinal colonization, but its molecular function is unknown. Members of the broader family, described by this HMM, are found in many species of Vibrio, Photobacterium, Aliivibrio, and related genera. The name AcfA is used also for a member of this family from Vibrio alginolyticus, that is no more than 40 percent identical in amino acid sequence, but it is unclear that all members of this family should be considered AcfA
KKILLLLLLSCSFSAAASPYVGLEYGFGSTNHDYKVNFSADNVTLTPDSSDGIFGGFVGYSFNNNWALEL
GYSQFELDDSRSQFLGIISVDGNVYEHEREWDASLKAKQFTLAPVYFYSLNDKWTLKLKAGLTYTQYKYS
SSKYDEYELVLNDDIESSTPLSSGSKSSNELGGIASVGVEYNVYPNLTLGANAKYQFDSFANTSSFNLST
TYYF
>gnl|CDD|468239 NF033909, opacity_OapA, opacity-associated protein OapA. This family consists of full-length homologs to OapA, opacity-associated protein A as described in Haemophilus influenzae. OapA shares a C-terminal homology domain, called the OapA domain, with the Escherichia coli protein YtfB, which is now known to bind peptidoglycan through its OapA domain and to act as a cell division protein
NPSQNELDLGFNQMEPITPKKVIQPEPSIFDKAKGLFAKKEQKAETQFAVRKEPTFGESSAQGEAPSTSE
ENTETVQEPAVQEVSTEEEESPVEELVSVETTQSETVEAKEAPKAGLKNPEKWKVLQILPQKHRRLFVAI
FGLVLLLIIFFALKPSSDTVQSFEQQNSNEVPIQFQSLDQSQPVETTVLDNPPAQNDNAAAQTNQAENAP
KAAEPNNATAVEPQAENAGSTQQATEQTTTTAAENKPEPVKPAQTEPVKAVEVSKVQETVKPKVAQEDVK
KEEPKVAEKAKPPTKKTEQTVAKTAKKAPQEAKPVQAKTEKKVQDIVDAKSATKTASTTSSKTLTVPQGV
SLMQVFRDNNLNISDVNAMTKANGAGNALSSFKPGDKVQVSVNSQGRVSELRLSNGARFVRQADGSYQYK
K
>gnl|CDD|468240 NF033910, LWR_salt, LWR-salt protein. This family of uncharacterized proteins was assigned the name LWR-salt (pronounced "lower-salt") to mark a well-conserved motif LWR (part of the longer motif WxFFRDxLWRG) and its restriction to the Halobacteria, a branch of the Archaea
YVFRVRFRLEPDEPGVSVDPDTFETTLRRPAPEPGEDGWLFFRDNLWRGEVNDEAHARELAEDWLGVPVP
VESVSFRELRTDEAYLDALKAAIAADLDAFNADSVDEVLHKYLGSSIR
>gnl|CDD|468241 NF033911, botu_NTNH, non-toxic nonhemagglutinin NTNH. The botulinum neurotoxin (BoNT) is always encoded together with associated non-toxic proteins (ANTPs) that are co-produced with it and form a complex that protects the toxin. Often, NtnH (non-toxic nonhemagglutinin) is one of these ANTPs, with the ntnh gene lying immediately upstream of the bont gene
MKINDNLNINSPVDNKNVVIVRARKTDTFFKAFQVAPNIWVAPERYYGESLNINEDQKSDGGIYDSNFLS
QDSEKDEFLQAIITLLKRINNNIAGEKLLSLISTAIPFPYEYIGGDYRQTNYLSSKDNKHFYAANIVIFG
PGSNIVENNVVYYKKEDAENGMGTMAEIWFQPFLTYKYDQFYVDPALELIKCLIKSLYFLYGIKPSDDLV
IPYRLRSELNNLEYSQLDIVDFLISGGIDYKFINTNPYWFTDNYFSNAKKNFEKYKNIYETEIKNNNAIG
NSIKLYLEQKFKINVQDIWELNLSYFSKEFQIMMPERFNNALKHYYRKEYYKIDYFKNYNINGFVNGQIN
TQLPLSDKNQDIINKPELIVNLINENNTSLMKSNIYGDGLKSTVDNFYSNYKIPYNRAYEYHFNNSNSYL
DNVNIEEIDNIPPIIDADIYPYRKNCDTFIPVYNITSTKEINTTTPLPINYLQAQITNNEDITLSSDFLE
VVSSKDKSLVYSFLDNVMDYLDSIKYDKPIDTDKKYYLWLKEIFRNYSFDITATQEINTSCGINKVVPWF
GKALNILNTSNSFVEEFQNLGPISLINKKENLSMPKIEIDEIPNSMLNLSFKDLSENLFNIYSKNNSYFK
KIYYNFLDQWWTQYYSQYFDLICMAKKSILAQEKLIKKIIQKKLSYLIGNSNISSDNLALMNLTTTNTLR
DISNESQIAMNNVDNFLNNAAICVFQSNIYPKFISFMEQCINNINKNTKEFIQKCTNITENEKLQLINQN
TFSSLDFDFLDIQNIKNLFNSETELLIKEETSPYELVLYAFQEPGNNVIGDASGKNTLVEYSKDIGLVYG
INSDALYLNGSNQSISFSNDFFENGLTNSFSIYFWLRNLGKDTIKSKLIGSKEDNCGWEIYFEDNGLVFN
MIDSNGNEKNIYLSDVSNNSWHYITISVDRLKEQLLIFIDDNLVANESIKEILNIYSSNIISLVSENNPI
YIEGLSILNKPTTSEEVLNNYFKNLNNSYIRDSSEERLEYNKTYQLYNYVFPENPIYEVKQNNNIYLSIN
NTNNLNIQPAKFKLLSINPNKQYVQKWDEVIISVLDDTEKYLDISNENNRIQLVDNKNNAKKIIINNDIF
ISNCLTLSYNNKYICLSMKDENYNWMICNNNSNIPKKAYLWILK
>gnl|CDD|468242 NF033912, msc, mechanosensitive ion channel. Proteins of this subfamily are mechanosensitive channels, involved in numerous biological functions. Representative proteins of this subfamily are WP_092311603 and WP_068170239 (TCDB accession: 1.A.23.8.3 and 1.A.23.8.5, respectively)
ILAALVILVIAWFLAKAVKWAIAKLVDRIPFLKRHNGANPGQTVGEQLGDIAYWLVWLFGLLAALQPLGL
GQVVGPLNTLLNNVFAFIPNIVGAGLIFFIGLVVATIVRRVVEAALQAANFDRWLNRAGLDNVTGNTGLS
RTIGTIVFVLIIIPVAIAALEALGIESISDPATAMLRTILDAIPRVIAAAILLAIAYVIGRWVAQLLEQV
LPSLGFDRSLSSLGNFSGVPPAGTTPSKVVGRIVLVAIMLFAAIEAARLLGFAELAAMLAQVLELGGRVL
FGAVIIAAGVLIANLLARLIARSGGGSDGFAATIVRWATIALATAMGLRFMGLADEIVNLAFGLILGSAA
VACALAFGLGGRDAA
>gnl|CDD|468243 NF033913, fibronec_FbpA, LPXTG-anchored fibronectin-binding protein FbpA. FbpA, a fibronectin-binding protein described in Streptococcus pyogenes, has a YSIRK-type (crosswall-targeting) signal peptide and a C-terminal LPXTG motif for covalent attachment to the cell wall. It is unrelated to the PavA-like protein from Streptococcus gordonii (see BlastRule NBR009716) that was given the identical name, so the phase LPXTG-anchored is added to the protein name for clarity
MRRAENNKHSRYSIRKLSVGVTSIAIASLFLGKVAYAVDSMQPISSTQENTANTSQKWHHINDDGIIPLG
ISLEAAKKDFKKEVEESRLSEEQKETYNQKIDAETDKDELLLTYHSEYSTDIKNLPASTEPTTQPVEASV
QETQASASDSMVTDDSTSVTTDSPEETPSSETPAPSIPALPEAPAQSAESEEPSVAASSEETPSPETPAA
PETPEEPAAPAPSPESEPSVAASSEETPSPSTPAAPETPAESEAPAQPAESEESSVAATTSPSPSTPAES
ETQTPPAVTKDSDKPSSAAEKPAASSLVSEQTVQQPTSKRSSDKKEEQEQSYSPNRSLSRQVRAHESGKY
LPSTGEKAQPLFIATMTLMSLFGSLLVTKRQKETKK
>gnl|CDD|411475 NF033914, antiphage_ZorA_1, anti-phage ZorAB system protein ZorA. Proteins of this subfamily are putative H+ channel proteins, but it has been reported that they are also involved in anti-phage defense
LAGGIFAVAAGLAVAFFVLHVLPIALSLWRARRVIARAKGREAFARNYESIRQRLERHPLIGHAWREFDE
TLVKPDVDEGGVIRNTVRPQSFFNLGLARERLFGLKMMGAIPGYFVGVGLLLTFIGLVLALYKAGAAASA
GDAEAMQDAMTELLQIATFKFATSIAGLGASIVLSIVFRIYTIWIEGSFDKFCEALERKLLYAAPQSIAA
EMNETLKEQRDQLKEINSDDFFARMGEELAPRINSAFASAMAPVTTSISSAVGKLTASSQSGVSDMLQRF
SDSVQGGAGTELRELAETLKQMQGSLVEMQGGLRGSGEDFARRMSEAAENLNRLVSDAGSSLGDSAEQSR
DALAEVVAALRQTFEKANAEVDEALGAAAGGASGKLEEAMGRVLEKLEAQIGGLGEGLGAFQGTLAEQLD
ETREQIAAAQQSAAAAVASASAEAAEALRDGLADALATIRAEIDRFEAAMRASEGALASQANAIGDATSQ
TRKVADAFSKTAQDVRAAAAPLAQSGERIAGATESMAESVGRTVEALEAAQTASGELAAALTGQNEQLGA
FWSSYAARFDRVDEALGKAVEALSRATEAQGERLAGYVQDVDKGLAQAVDKLSPLLTDI
>gnl|CDD|411476 NF033915, antiphage_ZorA_2, anti-phage ZorAB system protein ZorA. Proteins of this subfamily are putative H+ channel proteins, but it has been reported that they are also involved in anti-phage defense
AWFWLALALVFGFSLIFLFVHFRRFRTRVRALRKLLDGQSKETLADSRRETLQKAQALKAKNVGHLWREF
DESLVESSDQKRLFNTLDAEHFFNARTLAGGLTASRLLAAVPSFLVAIGVLGTFVGLTVGLSGLNVGTSA
EIEELKGGINKLISGAAVAFMTSVWGVFFSLLLNFIEKMFERSALGKIQKLQHRIDFLYPRIPAEQSLVH
IAEYSKESKEALQELHERIGDRLQESLNGMSEAMQTALTDALNNIMAPAIQTLVSTTSQQSTQVLESLVG
NFMDGMTSAGREQGLQMQQAAADVNAAVSGMSERLNQLFNSLSEQQGRQMERAQQQSSTFETQLQRLSGS
ANERQAQLEQRFEELMSGLTEQLQTQLGAAQQR
>gnl|CDD|411477 NF033916, antiphage_ZorA_3, anti-phage ZorAB system protein ZorA. Proteins of this subfamily are putative H+ channel proteins, but it has been reported that they are also involved in anti-phage defense
ATAPAAHFFSEQAIVDTPLKTEFFKHLPGILTGLGIIGTFFGLMLGLQHFDPSTPEQVQASVAGLLRDVL
YAFIGSAFAIFASILVTWLEKWRLGRCYKRLEKLTESIDGLFDGGVGEEYLAQLVKSSQESATQARQLKD
SLVSDLREMLTNLVDTQVRENLKLAETLSASYRESGQQMATQVSGAIENSLKSPLEKIAGAVQTASGDQS
GQVQNLLTDVLTAFMSKLESTFGQQFTGMSEMLGQSVEAMQSMQLGFSALLQDMRSASEASTQGSAQQIA
QLLSDMQAGQNAMQAGMNEMLASLQASVARIGSEGEGAGERIAGQLEKLFADSEARQQAMAEQMQAFVEQ
IQSSVGQGQSETMEKMAASVDALGTQLGGLFSQLEQQQQQMDESQQEAQQRLHEQTERLIGSLDDQIKQL
LALVAEQQQAMQETIQLLAGQTERHLQSMQAGADKMRLAAERFDTAGSSVSEANESTADVLGSVQSASAE
LSSASRELTSIVADYRNNR
>gnl|CDD|411478 NF033917, antiphage_ZorA_4, anti-phage ZorAB system protein ZorA. Proteins of this subfamily are putative H+ channel proteins, but it has been reported that they are also involved in anti-phage defense
MFLMFLKGFFNLIIHPTFTKIYILIEFLFFAYFIFKKGSLINKFKNEDDELQEEEIINFANFWPNFFITL
GILGTFAGIIIGIINLDFENDNSLKNSINSLLSSMGTAFFSSIIGIIFSIAAQIINKKLINDLLEIPKNN
KEKILDEIIGIRNDIKELNEIFAKPFETISEKAGQTVEKYSQKFNEINESFNNNFEKNINIFSNIVHKIS
EEISKQFDSIKQQSELIEKKEELIQKEKELLKDFSEIIEKSKELFNEIFEKQKNIVDKLEELEDLINSII
ENKADFEKLNENVLELIEKFEEFTDEFNSNFNEFINSINEINNKIPNQMILKYKKAFEEIELFTIDFFSK
FKDISVYLDDSIDDFDKSLEEFNESLLKIKNDIEFAIEDFKNSLIQLLDDFYKISNNINDEEDKKNE
>gnl|CDD|411479 NF033918, LGIC_1, ligand-gated ion channel. Prokaryotic ligand-gated ion channels (LGICs) are a large group of transmembrane transporters, which might contribute to adaptation to pH change
TVVKTSAFITDIISLDEVNEQLQIDVIFKFEWNDPRLKFDANEEKSPYKLYQGDFQYDEVFEGWKPQISI
INEIGSPQIKARQIKVYPDGRVIYKEQRTLTLETPMKLEKFPFDKQVLKAYMIPFGYDSREVQLEVEPNM
KITVKEYVKTNPNVNIAEWHLTNFNLTNTIPTKYYYGKDEEVSMLELSISLKRKPTNIIWKVLIPLTLLV
LAMWAVFWMDTKALSDRLNISFIGILSVIAYQFLIEGEMPRIDYFTFTDGFLLLSFVILFSTILESLIVY
WLSRADKQSLARRVDIFSRWLFPLT
>gnl|CDD|468244 NF033919, PA2779_fam, PA2779 family protein. Homologs of PA2779, an uncharacterized protein, average about 130 amino acids in length. The most distinctive feature is an extremely hydrophobic region at or near the C-terminus, consisting almost entirely of the bulkier hydrophobic residues Val, Ile, Leu, and Phe. The function is unknown
RLAALLAALLLLLGLPPSPAQAAMMIGTDQVIQQQQAQADRAQLLAFLERKDVQQQLAALGVSPEEAEAR
VAALTDAELAQLAQQIDELPAGGGGVIGVLVIVLLVLLITDLLGATDVFPFVR
>gnl|CDD|468245 NF033920, C39_PA2778_fam, PA2778 family cysteine peptidase. Members of this family are MEROPS classification C39 family cysteine peptidases, a group that includes many processing enzyme for peptide natural products such as lantibiotics and other bacteriocins. This family, more specifically, includes PA2778 as found in Pseudomonas aeruginosa. All members of the defining seed alignment are encoded in the vicinity of a homolog of PA2779 (see HMM NF033919). Note that the C-terminal region consists largely of tetratricopeptide repeats (TPR), so classification using this HMM must be based on comparing the top domain score to the second gathering threshold (GA2)
ELTDVPFFPQEEYQCGPAALATVLNAQGIDVTPEQLAPQVYIPERQGSLQIEMVAAARRHGLLAYPLPPG
LDALLAEVAAGHPVLVLQNLGLSWWPQWHYAVVIGYDLDRQEVILRSGTTERHRLSFSTFERTWARADYW
ALVVLPPGQLPATADPLAYLRAAQDLEQTGQPEAALAAYQTATKRWPDSWLAYFGLGNAAYAAGDYAAAA
AAFRQAVERHPDSAAAWNNLAYALAAQGCTAQARAAAECALALAP
>gnl|CDD|468246 NF033921, por_somb, iron uptake porin. Proteins of this family have typical porin structures. It has been reported that Synechococcus outer membrane (Som) porins (SomA and SomB) are involved in iron uptake in cyanobacterium Synechococcus
VTSVSQLSDVQPTDWAFQALQSLVERYGCIAGYPDRTYRGNRALTRYEFAAGLNACLDRVNELIAEATAD
LVTKEDLATLQRLQEEFAAELATLRGRVDNLEARTAELEDNQFSTTTKLNGEVIFAVADTFGDRVAGDSD
DSQTIFAYRVRLNLETSFTGKDLLRTRLQAGNFTNFAEVTGTNMTRLNFDDNSNNDVEVPHLWYRFPLGD
NLTVTVGATGIGYTDITDTLTPTIADDGNGIPSRFGRYNPLYRRGPGGGAGVNWQISDNLSLTLGYLAGD
PNDPDEGNGLFNGSYNALAQLAFYPEQGIALGLTYSHSYFPGGNVDLTGSTGSALANRPFGNNIATSADI
FGLQGYYRITPNFQLHGWGGYIWANAESGTDSLFVNNGDSADIWNGAVGLSFPDLGGKGNLPGILFGMPP
RVTNSDVRDDRDTSYHIEAFYRFQLNDNISITPGFWVILNPENNSNNDTQYVGVIRTTFKF
>gnl|CDD|468247 NF033922, opr_porin_1, Opr family porin. Proteins hit by this HMM model are members of the Opr family porins, which are mainly found in Pseudomonas and other Gram-negative bacteria with different substrates
YGQSNDNKGGTKDDGFSNGYASLGYETASLYGFSAGVGAWGNLKLGEKNDGDYDAPIENNALMSEAYIKY
EHEGMGSIVAGRQAVDLEWLTDYIEGAVAEITAIPNTTLVLGWAKRQAVVDIDELSEDFEKMNGNKGIYV
LDAKYTPIEGLELNPYYYYAPDLLDAYGLKTTATLEPFEALAHYAKSNSDSASGLEDGSIAHVEQGVEFN
GFTAAAGYIKTDKDGGGGIASFGDQISPFEDGNYVYDPDAKTVYGSAGYEIAGVSLGALYGQTKYDDATK
KLKEKELNLSVGYEITENLEASLIYVNVDNDNSDDDYNKVLAHVEYTF
>gnl|CDD|411484 NF033923, opr_proin_2, Opr family porin. Proteins hit by this HMM model are members of the Opr family porins, which are mainly found in Pseudomonas and other Gram-negative bacteria with different substrates
MKKLKLSLIAMLAISSCSIASANSLQEALKNGKVSGEVSVTYESRHQDKETSTYYQDTAYSVGSFALKYE
TAVWNNFSLTSKFRAYKTLFEDDKNFKTGHGKGDATERFYEDGKNRNVDLEELYLKYNANDFSVKAGRQF
ISTDWINKTHDAVRIDANIENTTIEAIWTRRKGRVYARDYRPMEKINENKGLYKLGLTYKFNDNISAKAY
GLYAPDLKDIYGGKINYDYDDFGGRAHYAQSDEDDDNVKDSSIFELKLSTSILGFTPTLGYVKVDKDAGF
GGMTAAGETIVPFEEGDYMYLKDAKTYYAMLSKSFGDLSVTALYGITDYDKDSDNKKYKQDEFTLWLGYP
ITKNLKANLGYTNVNEDSKDAPTDLDQLNATLTYSF
>gnl|CDD|411485 NF033924, T3SS_LcrQ_reg, type III secretion system exported negative regulator LcrQ/YscM1. The type III secretion system (T3SS) protein called LcrQ in Yersinia pseudotuberculosis and YscM1 in Yersinia enterocolitica is a post-transcriptional regulator of T3SS effector gene expression. Successful chaperone-dependent export by the T3SS allows the translation of T3SS effector proteins to proceed
MEINDLQSLINMQIAEFGGGEKAGRLKETLPLTENSHAISSAEKAFANAVLEHAKNTALNRHDIACLLPR
ASNFELKQGKAGEVILKGLRTEQLSLEDAKLLLDAAMRKC
>gnl|CDD|468248 NF033925, pora_1, PorA family porin. This HMM hits Corynebacterial Porin A (PorA) family porins, which are short membrane proteins
MENVLEFLGDLSVLSSNGLIGYVFDFLKASADWAGAVADLIG
>gnl|CDD|468249 NF033926, msp_porin, MSP porin. Members of this HMM are MSP porins (major outer sheath proteins) in Treponema. They may play a role in immune evasion and persistence
KKILLILMILVLVGGVAFAQVAAEPDIEGSATLSWGIDLGGGKTGTIKHGFKNEASWKVVFPLFKKGDFS
SKGEGDVYAEVSLKDVELALESDSDAKFALTGKVDSVEATLHFYGAYLTVYGKPDFKTNYAQIWEPIDAD
DKDKDDPKFNPGFTGYGTKIGYANDDLMDLDVGLKFGSNGSWKPKGASYYQTMKYVDGNTALGNGEYIGW
LTGKVVFTSDGWAPEAGQYYFVTTAYTDPTDSKYGLGFDFSMGPVDKYLGVEFTINATFSSDYDYDPATP
PADNGNLNFGAKVTSEPVDGLKLKLGFDGGVKFTDAQKTFAWDAVFTAGYKWVGAGVYVGSAGTPYAGNN
KSNKAGTDMAAFAAFETKGDGDDTNLVEGLDAGVDVRMYHLLSKISDEDRVKYAKFPLGLKVWGSYKYNL
TDSMWVKPYANFWGETNHDHVDPDKSKDKLYFGLAYEVGVTFSPVEKVEIDASWEHGKLNKNKYEGGTSM
IKTPVNDKTHNGTFVLSLKVTY
>gnl|CDD|411488 NF033927, alph_xenorhab_B, alpha-xenorhabdolysin family binary toxin subunit B
DLSNVIAALRKSAAKIANKLDDLSQINLREATLDLLAQLQEQIAELEAQIAALESKLNELAEDRKVIIEA
IDLIEKYNIADLFKDLLPTAEEIDSLGLPPPEKDLVKAAIERLKKLLGKISEGLTYIDLVEARDKLRDRI
NALLAESRTLDKDIKALAGKLEELTAIAAIDEERATWVAEARKVEQAWESFLDQLTELTSDSANLAQLIT
QLNGFIKFLNDVS
>gnl|CDD|468250 NF033928, alph_xenorhab_A, alpha-xenorhabdolysin family binary toxin subunit A. Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family
FILTKEDWISIQKYVQAALALPTTLEEVESYLGYPKDGIPGLEPKDLLDLFQNIRNHARSWSNLEPKIKQ
LANDLANYARNIVVTGNPIIDLINEMPIIKRGDLTEEELSELPPIPLSSDDKEIVKELKEILEDLKNDIK
DYQQKADDVKKELDDFENDLREELLPQLKLKKKLYDDNLGSDSIEELREKIDQLEKEIEQLNKEYDDYVK
LSFTGLAGGPIGLAITGGIFGSKAEKIRKEKNALIQEIDELQEQLKKKNALLGSLERLQTSLDDILTRME
DALPALKKLKGVWQSLLTDIDSSINALKEIDDADSLRLFKLEFEQVIAPWKEIQDYAKQL
>gnl|CDD|468251 NF033930, pneumo_PspA, pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus
MNKKKMILTSLASVAILGAGFVTSQPTFVRAEEAPVASQSKAEKDYDAAVKKSEAAKKAYEEAKKKAEDA
QKKYDEDQKKTEEKAKKEKKASEEEQKANLAVQKAYVKYRKAQRRKKSDYKKKLAEADKKIDEAKKKQKE
AKAEFNKVRAKVVPEAEELAETKKKAEEAKAEEPVAKKKVDEAKKKVEEAKKKVEAEEAEIEKLQNEEVA
LEAKIAELENQVDNLEKELAEIDESDSEDYIKEGLRAPLESELDAKQAKLAKKQTELEKLLDSLDPEGKT
QDELDKEAAEEELSKKIDELDNEVAKLEKEVSDLENSDNNVADYYKEALEKDLATKKAELEKTQKDLDKA
LNELGPDGDEEETPAPAPQPEQPAPAPAPAPKPEQPAPAPKPEKPADQQAEEDYARRSEEEYNRLTQQQP
PKAEKPAPAPAPKPEQPAPAPKTGWKQENGMWYFYNTDGSMATGWLQNNGSWYYLNSNGAMATGWLQYNG
SWYYLNANGAMATGWAKVNGSWYYLNANGAMATGWLQYNGSWYYLNANGAMATGWLKYNGSWYYLNANGA
MATGWLQYNGSWYYLNANGAMATGWAKVNGSWYYLNANGSMATGWVKDGDTWYYLEASGAMKASQWFKVS
DKWYYVNGLGALAVNTTVDGYTVNANGEWV
>gnl|CDD|468252 NF033932, LapB_rpt_80, LapB C-terminal region repeat. This model describes a tandem repeat about 80 amino acids in length per repeat, found in at least 12 different surface-exposed proteins of the pathogen Listeria monocytogenes, and in particular found 10 times in tandem in the surface protein LapB, for which the repeat is named
GDYTVTLNATNEDGNKATPVKVTVTIVDTSAPVITADKEVSYPKGTTITEAEFLQDIHAKTTDSLSGVKI
TSDFATAVDLNKA
>gnl|CDD|411492 NF033934, KCU-star, KCU-star family selenoprotein. This family is named KCU-star because nearly all member proteins end with tripeptide lysine-cysteine-selenocysteine, followed immediately by a stop codon (represented by an asterisk, or star). Members occur in primarily in species of Helicobacter (although not Helicobacter pylori, in which selenocysteine incorporation capability has been lost) and Campylobacter. This small family belongs to the larger YbdD/YjiX (DUF466) family described by Pfam model PF04328, which regularly occur in the company of CstA family pyruvate transport proteins, and may be part of the transporter
LYEKSDRFFHPLVGLPSYDKYLEHMRKNHPDKIPKSRKEFFKEALEAKYGAGRNKCU
>gnl|CDD|411493 NF033935, inclusion_IncB, inclusion membrane protein IncB. When Chlamydia invades a cell, the host-derived membrane of the vacuole in which it resides becomes known as the inclusion membrane. The chlamydial type III secretion system (T3SS) delivers a number of effector proteins into the inclusion membrane, including this protein, IncB (inclusion membrane protein B). IncB proteins from different chlamydial species share a conserved hydrophobic C-terminal region, represented by this HMM, but their N-terminal regions vary considerably in length and sequence
TCKKVLAVVLTIIALIAIAVLIACIVAVCGGFPLLLSLLNMYTIGACISLPIISCASVALLILCLLSIES
LLKPQPAI
>gnl|CDD|468253 NF033936, CuZnOut_SO0444, SO_0444 family Cu/Zn efflux transporter. Members of this family are apparent metal cation efflux transporters. Architectural features include an average length of about 400 residues, with well conserved and highly hydrophobic N-terminal and C-terminal domains. The central region is highly variable in length and sequence, and rich in both Cys and His residues, as often seen in proteins produced in response to toxic concentrations of certain metals. The founding member, SO_0444, was shown to confer resistance to high levels of Cu and Zn ions. The best conserved region of the protein is a CSCG motif in the N-terminal region, found at least twice as in a selenocysteine-containing form, USCG
FWDLFLEAAPWLLLGLLVAGLLKAFVPDDFLQRHLGGGGFGSVIKAALIGAPLPLCSCGVIPAALGLRRQ
GASKGATTSFLISTPETGVDSIAVTYALLGPLMAVVRPIAAFVTAIVAGLLVNLFDKEEEKDKAAPVSES
AASSCCSSSSCCSSSCGAGHVAQKLKAGLRYAFGDLLGDIGKWLLIGLLLAALITTLVPPDFLAQYLGSG
ILAMLVMLLIGIPMYICATASTPIAAALLLKGVSPGAALVFLLAGPATNIATLGVVRKELGKRALAIYLA
GIIVCALLFGLLLDYLYARLGLDVTAQVGSAAHELLPGWLEWASALLLLLLMLRPL
>gnl|CDD|411495 NF033937, porH_1, PorH family porin. Proteins of this HMM family form major outer membrane hetero-oligomeric pores on the cell wall of Corynebacterium with PorA family porins
MDIFVMLLRHVLKLIQYLLVTPTVASDNHSIRWCIPAHLKEKNMDIQFIASQLKNFDTFVTNIATLFQGF
PKLIQTLANLFKNNAAGWGDAWEATKK
>gnl|CDD|468254 NF033938, porH_2, PorH family porin. Proteins of this HMM family form major outer membrane hetero-oligomeric pores on the cell wall of Corynebacterium with PorA family porins
MDLSFIQEQLGNFATFAGAIGDFLQGPAKIFDTIFGWFAGAGTDGDSFDVKPDLDWTSSALSS
>gnl|CDD|468255 NF033939, DESULF_POR1, outer membrane homotrimeric porin. Proteins of this HMM family are primarily identified in sulfate-reducing Desulfovibrio, but this HMM may also hit proteins from other Gram-negative bacteria. Porins of this family form transmembrane pores for the passive transport of small molecules across the outer membranes of Gram-negative bacteria
MKRLVTLALAAALVLGAAGAASAVDIKAKGQWQFNFNWLDNPDFQSDDGNSEDDFNARQRLRTQFDFIAN
ENLKGVLYFEIGDTTWGQGSGGALGTDGKNVEVKRAYIDFNIPGTDVNVRMGLQGLALPGAVGGSPILDD
DVAAITVSYPFTDMVGLTAGWARAYDNNAGDGTDTNSNDEMDVFGLALPVTFDGFSLTPYFAYAAIGKDT
NASSGGAAAAGLLPLGATANGGDDDDANAWWAGLAFEMTMFDPFVLKADFNYGSVDADTDQNDRSGWFAD
LAVEYKMDFVTPGLFFWYASGEDDDASDGSERMPVIAGDWALTSFGFDGSAFTGDDNLLGNAGTGTWAVG
LSLKDISFIEDLTHDLRVAYAQGTNDKDLAKNGAAATTNSDGLYLTTEDSAWEVNFDTTYQIYENLAAIL
ELGYINLDLDEDTWGRGDDDDDDAWKAAFGLVYKF
>gnl|CDD|411498 NF033940, ErpA_rel, ErpA-related iron-sulfur cluster insertion protein. null
MFTVTITDAILAKLRAMLEEEDEDACVRLREYKVGGGCKSKIELGLGLDEPDDEEDEQIDVDGVPFIAEK
DFLDKYGKSFTLSLDEDKGMPLVAA
>gnl|CDD|468256 NF033942, GjpA, outer membrane porin GjpA. GjpA was first identified in Gordonia jacobaea strain MV-1 as an outer membrane channel-forming protein. It has been reported that GjpA could be of relevance in the import and export of negatively charged molecules across the cell wall
AGIAIVGAGLIAVTPVAAPLPDVPVSRDVALTAGGDPLAPWTDVFNTASANATTLLNNFFLAPGVGLQQF
IANQVGYWQQVLDDPSSIPDVLQQMQANLQAVLTGYTLQGASDDTLDTVLVHTLDDGLHDLLLGLLPQFL
PAGVDPETVTPIVNFLASPLSGVLIGSLGPSISPWVALLNSIQDGDSLLNIPANMVGAFLNGATLNLDAL
LPLINDAGLLPEGTTIDHLDIAFGGLLTPGSVAVGPYEVTDPGGEVVSVPAVGGSIFNSLGLDLGTTPLL
GFPLDIDGHAVGPIGAWEAWSQTVGALLGSGWDGKGNPVVVTPPLAGIDFP
>gnl|CDD|468257 NF033943, RTX_toxin, RTX family hemolysin. RTX family toxin are secreted from the bacteria and inserted into the membranes of infected cells, causing host cell rupture
LILLIPKDYDGQKGNGLNDLVKAADELGIEVQREERNNTAIAKKSFGTAEKLLGLTERGVVIFAPQLDKL
LQKYSKIGNGLGSSAENIGNNLGKAQTVLSTIQSFLGTALAGMELDELIKKGEDVSQLELAKASIELINE
LVDNIASSNQTIDAFSEQLNKLGSLLSNAKGLGGLGNKLQNLPNLSKAGLGLDVISGLLSGISAGFILAD
KNASTGTKVAAGFELTNQVLGNVTKAVSSYILAQRVAAGLSTTGAVAALIASAVSLAISPLAFLSIADKF
NRAKQLEEYSERFKKLGYDGDSLLAEFQRETGTIDASLTTINTALSAISAGVSAAAAGSLVGAPIALLVS
GITGLISGILEASKQAMFEHVANKLANKIAEWEKKNGKNYFENGYDARHAAFLEDNFKLLSSLNKEYQVE
RAVAITQQRWDENIGELAGITKNGDKISSGKAYVDYFEEGKRLEKKPDEFSKVVFDPLKGIIDISNSKKS
TLLKFVTPLLTPGEESRERKQSGKYEYITKLVVNGVDKWTVKGVGNAGSVYDYSNLIQHAAIESGKYREI
RIISNLGAGNDKVFVGAGSSNIDAGEGHDRVYYSKTDTGYLTIDGTKATEAGSYTVTRELGGDVKILHEV
VKEQETSVGKRTEKIQYRDYELRSGGYGYTATDTLKSVEEIIGSNRNDKFKGSKFNDIFHGADGDDTIEG
NDGDDRLYGGKGDDKLYGGEGDDLLDGGEGNDYLNGGYGNDIYIYRKGYGNHTIYDSGGKNDKLSLSDIS
LSDLTFKRVGNDLIINKNDNGVKNGITIKNWFKKESGNKKNHKIEQIIDKDGRVITSDQIDKLLKKKNGK
ISYILLSKLADNYNESNLSSLANSLSKIISSAGSF
>gnl|CDD|411501 NF033945, AcrIIA2_fam, AcrIIA2 family anti-CRISPR protein. Anti-CRISPR proteins are phage proteins that defeat CRISPR-Cas systems for immunity based on phage-derived spacers found in arrays between CRISPR repeats. The founding member of this family, AcrIIA2, works against a CRISPR-Cas class II system
TTAQRKYYEAMNEFEEMTDKEVESTPDFAQEVLNDSDYVVITKNEKYAVALCTLNTDGFDTRLYLDEKLV
DSTFLDVNGETYYINIVQTNEFDDLELATDEDIEKYDKQEVILKSELN
>gnl|CDD|468258 NF033946, AcrIIA4_fam, AcrIIA4 family anti-CRISPR protein. AcrIIA4 is an anti-CRISPR protein that affects Cas9, a class II CRISPR system protein used in biotechnology applications for targeted genome editing
EIRELKREIKAKDYTVRLEGTDSNSITQLIINVDGDGNEYPISESQNESIKEKFIETFKNGWNGTYEDEE
EFYNDMQEIAQELILE
>gnl|CDD|468259 NF033947, PEP-cistern, cistern family PEP-CTERM protein. Members of this family are PEP-CTERM proteins, that is, surface proteins of Gram-negative organisms that carry a short C-terminal region used to help target proteins to their proper cellular location, hold them in position for post-translational modifications that might need to occur (such as glycosylation), and which is eventually removed by exosortase as the protein is ligated to something else. In this family the most conspicuous feature other than the PEP-CTERM sorting signal (with variants that include PEP, PAP, PTP, and SEP) is a pair of Cys residues about 6 amino acids apart from each other. The second Cys occurs in the middle of run of amino acids that are all either small (Gly, Ser, Ala) or else Asn. The local context suggests the Cys occurs at a turn at the end of a structural feature such as alpha-helix or beta-strand, rather than in the middle of one. The word "cistern" was assigned to suggest the proposed Cys-turn feature
AVTITSADVGDSFTVDFDGFVGGTTVDGLSATATFTLTSFTGTTATFDYSLTNTSSGPVTSRISSFGFDV
DPDITGASSTGAFSYASLNGNFPNGFGTVDVCFKAGNNCSGGGNGGLAAGNSGTFTLTLTFGSAVTSITL
SDFFVRYQSIDGAGGSTSGSGVGTVTGGSGSGGTPVPEPGTLALLGLGLLGLGLARRR
>gnl|CDD|468260 NF033948, AcrIIA3_fam, anti-CRISPR protein AcrIIA3. AcrIIA3, as found in siphophages infecting Listeria and Streptococcus, is an anti-CRISPR protein that prevents Cas9-containing CRISPR systems from protecting against phage infection
YNKSEIMKQAWNWFNDSNIWLSDFEWVSFTDKEKTFSVCLKEAWAKEKEEVERVAKESANAPKSEEAKAW
DWACRKLGVHFNIDADEKVTNVKDMAKEMWGLNVWACAMKAVKLHIELF
>gnl|CDD|468261 NF033949, Cas12b, type V CRISPR-associated protein Cas12b
LWKTHELVNDGVRYYTEWLLLLRQELLYTLDDKQDREPTGERKKRRVLLALSWLSVEDEEGAPNNLILDG
GPRVKKTKEALQAELLERLRAKQEINGWPRDCGDDDEVLVALRQLYELLVPSSLGKEEAWGDAQGIARKF
LSPLKDPDSEGGKEAKDLVQKAGQWLSGRSGSGRKPDWKRMKEAGDPKWEEEKEEKGKKAEAKKAEDPTA
EVLNRLDELGLIPLFPLFTDKVDLAKWKPKAKSQGVRTWDRDMFQQAIERLLSWESWNKRVEEERRKLEE
KAKKLEGKPEEGDEGLFELLRRLEEERSEESGAFAGKAGAYRIRRRALRGWDEVVEEWSKLDPGATEEDL
IEALRALQRDNRRKFGDIQLFEALAKPENWCLWDAEGRADPDFLTRYAAYNELQRKLERAKVPATFTLPD
PRLHPRWYRFEASSGSNLHKYKLLTDEKRGYVTFPRLLVPDENGLWEERKVRRVPLAPSRQLRDDLALAL
PWLQPGKKALGYADRAASQPFKGTLGGAKIQFDRKELNRRLQALRVYLNLTVDVEPQAPRAEKLRKPIGW
LVQFSPKLDGQGPVLRYAAQHGKELPPWWNNKRKGHAKLILPGLRVLSVDLGQRTAAACAVFEVLHEKPV
DRTKLFRPIGDDGTEHLWAVHERSFLIKLPGEDESVRRALVRELEGKLGREARLIELRTLRLQLRRLGNL
LRIAKLDNPDERKEFPGGWDELLEAEGRALARLDALHLWRDLFSSPLWSDDEAKKLWKEHVAELNEYERP
DLAVQAHRELLRSLAKRLANSWRKRWRKGDKRWLSDAGARGETRRVVGGLSLWRIEQLEELRKLLKSWSM
RPRPPGEVKRIERGEDFAPALLEHINRLKEDRVKQLAHRILMAALGYGRVYDPKKKDRHGEWERVYPPCQ
LIVIEDLSRYRFSEDRPRRENSRLMKWSHRKIRKYLKEQAELYGLPVGEVPAAYSSRFDARTGAPGIRCR
EVTEADLLDQPWWRKLVKTLNENGKVWLERFLKDLKRNWKARDKGERLKPGDLVPTGGGELFVSLSDSES
KELRVIHADINAAQNIGLRAWTDPPEWWRVPCRLRTEDGDELYVPKPQKKKGKGSFGFPVFGPEPVYSWV
KGEKGKIKDDEDEEEKEILEEADELKGESVNLFRDPSGIFFPKGEWVEGKAFWSTVKRRVWRRLAER
>gnl|CDD|439422 NF033950, Cas12c, type V CRISPR-associated protein Cas12c
ARKWRKAIAASLARRTKETVFTYKFPLDTKVSNIDFDLAVQAYNILEGVGPGSLLGYLCAFHLLGFRLFS
KAGEANAFRNSSKYPNEEFADKLRRELGIVLPSLEPLTLDLLFQSPPRSRNGVAPEWSTDAIINRLYTNL
TGKGPGAKPSGHLLELAEQIAKEIVEDFDTWKDLTANPDKGLKAFDKYFQAQGDFPSLNVLPPSKVLKPI
NSGIDYDTDADFDIDGPADETLIYQAVARCAARIRREAPKPDANKGDFIKQVQDAITTQNNNALSWLFGV
GLKYFKESTVDELAEDYGIPSVIRDCHALIKLAADAIALNPLFDKPHYSDFRASVGGKIDSWVTNYVKRL
LELESSLSSISKEPPALNRFIGGSPDVTKHISFLEEDAQQLLDQLSSHISTLTEAVKSLNILLGPAQAMP
TLEDLRLAERGSLVDELEAAISLILQRIGQLAERLKPLEAAAIREKSWVGNKWKRLLKLKELNGLSSGTV
PVDDDELQAALLFNGLLTDSKEHYLKITADKLPSRLKDAEDEFDRLMGLKEGGLSHASIEQVEKVALEIR
AFLGKVERFANRLQNDLCKELEEDLLKCKVFHSKREFNLFFHNRLGSIYRSPYSTSRSQPFYLAKGTDWV
LGLTDLLEDILKDYQQAGQADELELRDLISLEYFRKSQLLRGLPDVVPSSLILPRVLDQQSLDPRLKLLL
QEDQVDRSTCIKAFNLYKSAISGCLYRLNREGFIVRTKFSRIEGSTLVYVPKTKDWKYPKRLLHGRGPIE
AALSSDWIEKDDAGVIDPVDTAKNLSNTPKTGFQSAGVKEYLVQLPHDWYVPIDLRGEADYVPGLAVSKE
ITSLKRLSKRVAFRLVGPSSFKSKLLSGLLSGKVSPGDMTLERDQYYKQSLKNGQVKISYEPTDRQVEAA
IPVTDKRERSSKEPDWLFDHIIAIDLGEYGLGYAVFNIKNGLRLESGSIAIPSIRRLAKKVSSHRRKRQP
RQKYNQTYSNALENARENAIGDVCSIIDTLMAKYNAFPVLESEVANSEGGSRQLSKVYGSVLSRYTYSDV
DAHKAKRKSHWYGANHWDIPGLMVRKWNEKTSKSSKVFKPLKLFPGVQVSAYGTSQICSQCGRNPIEALR
EHFNKTKKVKIENQGELDLDDGTIKLFEGSDSSWTEKKRSQSRRKRRRLNERKPLNYFVKDGSHSAKQLI
TVIRRNLRRPPKSVMSKDTTQSRYFCAYKNCGFEGHADENAAINIGRKYLTEIIDF
>gnl|CDD|468262 NF033951, Cas12d, type V CRISPR-associated protein Cas12d
GKKGYRLHDERLAYTGKIGAMRSIKYPLKDSNKTVRNEIVDAIISDYKWLYGLLNLNDYYEWYSRKDEEY
SLLDFWLDSLRAGVVFSKKSTELKNLISKIRGDKSALQKLFETIDDDLKHLLDRKQIKDFIKFLSDTRKT
NDQGRLKKQIKNCFKGEKREFRKKDNKAVDEIKKKIIRIGDSFAKNKSKKYTIFKLDKPHTFFPHINDNQ
DLFFCTPDFEEITERDRTKTLDLILNRLKKRYESKEDDKTSNRMLGYSNNQGAFSNYLNELFLFVLDRGD
DFSLVLADLENSFSWSNEEKELEKRLQILKYAEKKLGEPKLADKWDDYRSDFGGKLESWYSNYIEKLKKI
PEQLSKLRENLKKHKKVLKKNKQNLSKKILESDQKEIEAIRDYLVSLEKPELKKFSWINDMADREFIELY
RLWLSDLRSQLNEYNTYDEKISFEKKGKKKNKETKDENKWYPKLSKSIKLIPNFFGESKRERYKKFINLK
DLTFSEGKNVENIIMSAEAEDLKNIFKEYKEDIEFTEKQLEKLLRKYYARFNSDRFKTVLENIAREAGTF
KKYGNNNNRNAEVFYLNPRERDVFRIIKVEKSNTVKKILELVDLPSLLDEAWRDLVKKNKNGELIDLIEL
SKTILALLLSHSKFKIDKSLLDLDLFASAYQYLKLEDEELSGDKLKQFGQNYIHSELKGYIALISRREFI
SRYSVQTMNGTQCKLLLIKGEGKATWHSSKKGNLIEKKGYDGGVAKNQDKSKIFKKKIKNSHKTVDFNQN
KIKIQVRSSKYQIQFLDWFFEKHKGKKTDLEVSGSFLIAEKKVKVDWDGDNLRVGLKREDSEEERVFVSQ
PFTLIPDDERRKMIETRNRYLGIDIGEYGLAWTLIEIDNDNRGIKILEQGFITDPQLQKLRENVKSWKQN
QVRGTFTSPDTKIARLRESLIHSLRNQIHSLALAYKAKIVYEYEVSNFETGGNRVAKIYDSIKRADVYRE
TKADNSQNDQVWGKGIKQWGSEISAYATSQFCTHCKRWPLLIVDIEEYDEKGYNDNLFKVKKGWRLGEKI
KGKELFKPIKDFMRPPIDGLLMKIGDDLRDWKKRRGNSAIFICPFCRHISDADIQAAFNIALRGYVKD
>gnl|CDD|411508 NF033952, AcrID1_fam, AcrID1 family anti-CRISPR protein. The AcrID1 family of anti-CRISPR proteins occurs in virus infecting the Archaea, primarily Sulfolobus. It targets and inactivates type I-D CRISPR-Cas systems
EFKELKSILDKFFEDSTIKELNLKFKEPLEITEEEFEELIGNGDLLNRYENNGIIIDEYEYWENDNIYVK
LEIVYYKKDNKIYIYEIDFWREK
>gnl|CDD|411509 NF033953, AcrF10_fam, AcrF10 family anti-CRISPR protein. Members of the AcrF10 family of anti-CRISPR proteins have been found in phage from various Vibrio, Shewanella, and their relatives. AcrF10 is considered a DNA mimic protein
FQIENARIETITDEFDMVKFDLVTDLGRVELSEHVNYDSEGDFKSVEYTDSNIRCNMSDELCSVFDMSDK
PSLMPIIDYVPFAEIIEAVEEMIE
>gnl|CDD|468263 NF035921, staph_coagu, staphylocoagulase. Past residue 485, the protein consists of a variable number of 27-amino acid tandem repeats (see PF04022). This HMM omits coverage of a portion of the repetitive C-terminal region
MKKQIISLGALAVASSLFTWDNKADAIVTKDYSKESRVNEESKNGTPISDWYYWGIIKSLESQFYNALDL
LEDYQYGEKEYKDAKDKLMTRVLGEDQYLLEKKKDEYEKYKKWYKKYKSENPNSKLKMKTFHKYNLYDLT
MKEYNDISKSLKDAVDEFNKEVKDIQSKNKDLKPYDEETEKKATDEVYDLVCEIDTLYAAYYGDKQYGEN
AKELRAKLDLILGDEKNPHRITNERIKKEMMDDLNSIIDDFFMETNQNRPSNITKYDPNIHDYKKKPENK
ENFDALVKETREAVAKADESWKTKTVKKYGETETKSPVVKEEKKVEEPQAPKVGNQQEVKTTVGKAEETT
QPVAQPLVKIPQGTIQGEIVKGPEYPTMENKTLQGEIVQGPDFPTMEQSRPSLSDNYTQPTVTTLTNPIL
EGLEGSSSKLEIKPQGTESTLKGTQGESSDIEVKPQATETTEASQYGPRPQFNKTPKYVKYRDAGTGIRE
YNDGTFGYEARPRFNKPSETNAYNVTTNQD
>gnl|CDD|411511 NF035922, Trp_DH_ScyB, tryptophan dehydrogenase ScyB. The tryptophan dehydrogenase (EC 1.4.1.19) ScyB performs a reversible NAD(+)-dependent deamination of L-Trp to 3-indolepyruvate. ScyB occurs in Cyanobacteria that biosynthesize scytonemin, a natural sunscreen, from tryptophan
KLFETVKEMGHEQVLFCHGKNPNIKAIIAIHDTSLGPAMGATRLWPYVSEEAALKDALRLSRGMTYKAAC
ANIPVGGGKAVIIANPEQKTDELLRAYGRFVESLNGRFITGQDVNITPEDVRTISQETKYVVGVSEKSGG
PAPVTALGVFLGIKAAVEFRLQTQDLKGLKVAVQGLGNVGKNLCQHLHEHGVKLFVTDINPEKAEEIKRL
YGATVVEPDEIYSLDVDIFAPCALGGILNSQTIPQIKASIIAGAANNQLENEQLHSQMLTSKGILYCPDY
VINAGGLINVYNEMIGYDEEKAFQQVNNIYDTLLEIFDIAEEQEITTNDASKRLAEERIMKAKNLK
>gnl|CDD|468264 NF035923, TPP_ScyA, scytonemin biosynthesis protein ScyA. This HMM distinguishes ScyA itself, found within the ScyABCDEF operon, from closely related paralogous TPP-binding ScyA-related proteins encoded outside the operon
MSQNYTRSSSQITTEPYKVYQPSGYVESSLNGSHQEQSEKDSDNSAAKPGVNKKSLTVADAIAQMLEDLG
VKCAFGVAGGAMATLWGALSNSSIQVLNCRHESGAAFAAVEAYFATGRPTVVFTTAGPGITNALTGLFAA
RGEGAKVILLSACTSAPQRGRWAIQETSAYTLPQDGIFTSGALFNYATTIESAAQLPQIFRRLALGLSQP
GGFVAHLSIPTAVQTSPLDESLPQLDVVHSLITPSEEAIAHCVELLSEGPFAIWVGFGARNAAEEILQLA
ERTGAAVMCSPRGKGIFPEDHPQFVGVTGLGGHGSVLTYMQEQTPLRTLVLGTRLGEPTSFWSPAMVPPG
GFIHVDIDPEVPGVAYPDAETFPVQADIKTFLRALLQHMPNIASSRANISLPRPERETIAPATDSPVRPE
VLMAAIQKVIVEGSDAVVLAECGNSFTWSTHLLRFAQPNRYRVSTGVGAMGHAVTGVLGAAQARNGKAVA
IVGDGAMLMNNEISTAVKYQIPAIWIVLNDARYNMCHQGMKMLGLTGADALIPQTDFVMIARGMGAEGIR
VDKESDLEAALEKAIASPGPFVIDVIIDPDRRAPSKGRNKSLAAQGVKSTPAKQTAKVSFPNV
>gnl|CDD|411513 NF035924, scytonem_ScyC, scytonemin biosynthesis cyclase/decarboxylase ScyC. Of the various markers of scytonemin biosynthesis, ScyC appears to be the clearest, as there are few or no close homologs from outside of the set of confidently predicted scytonemin producer bacteria
EKNTFATSAYIATSPETAFDYLCSLENLDEWTLFSRMIEQIDENTWLGTASGYQRNLYYHVKKIENPLFY
GIEWHCGFEYQKYFQVYPVLLFPPDYIEPGTDEKGVYFHWLSFVDPKRRTPMIMQGIHTVHTSECRSLKA
ILERKAGLTEAAKGRYRIDTDTIYVDAPIELGVEYLSDLRNMDEWAHLLRPDGEISPQSGEFLDEYDQKV
KVTFRTHALSKYYLIEQDYFYPDYGFYQRCPVLLIPCSYAFGDPSASGFIQHRITFWKVDEPLRHGKLQI
EDFGAESMNIKRLLEAKAGNLETFARGMSYIP
>gnl|CDD|468265 NF035925, Geo26A_fam, geobacillin-26 family protein
ITIKILEDNESERVVEVTDGNKITIATYDKKTNELTIEEKGLKTNSKEEISLNEIKKESSENSQSAAIAT
ASSKLIDSASDLWYGYYYYIYTYRNIWVIQIPKGSKKNPTETSSNKSDLNNFRNSVDNLRSAELAAVAAV
GTAVAAAIAAVLTAPAPTGWGAVIAGLTAAGAGATAAANAYDAYQAAKDADYYFDRV
>gnl|CDD|411515 NF035926, scyF_NHL_VPEP, scytonemin biosynthesis PEP-CTERM protein ScyF. ScyF has multiple tandem copies of the NHL repeat, making it a beta-propellar protein. It has an N-terminal signal peptide, and a C-terminal PEP-CTERM domain for recognition and cleavage by exosortase, suggesting that ScyF is sorted to an extracellular location, perhaps the outer leaflet of the outer membrane, and attached there covalently
NLSLAIASAGFMVLATAAQAKAVTLTYDSSIGSPGFGPGQLFVPQGIGVQDSTGNIFVSNGRGLNPDGSF
NPNLGNRVEVFDPQGNYLRAIGSGGQGPGQFDEPADLKFDPVTGNLYVGDVFNSRIDVYDPQGNYIRSFG
SFGGPVEGRLFFGPGGMSFDKDGNLYVTDFSGDVIKKYGKDGELIGTIGSSGTEPGQFQGPAGIRISPNT
GNIYVADQYNNRVQVLDPEGNPLLAFGSQGSEPGQFNQPIGIEVDEYENIYVADSINSRVQVFDKNGNFL
TAFGEPARNASGEVVPPPALGGPPFGNPLDLTPGKFNWTAGLHYDDGKLYVGDFFQGRVQVLNVEGSTKV
PEPSSLLGLGLLGLGAAAIKLRKRRQ
>gnl|CDD|411516 NF035927, TPP_ScyA_rel, ScyA-related TPP-binding enzyme. Members of this family are not ScyA itself, which is described in TPP_ScyA (NF035923), but instead are closely related paralogs that are likewise restricted to the Cyanobacteria. Nostoc punctiforme, for example, has ScyA itself, but also has three members of this family, all more closely related to each other than to ScyA. By homology, members of this family are expected to be thiamine pyrophosphate-binding enzymes
SVAEAVVKMLEDMGVKYAFGVSGGGIAPLWAALEHSSIQVLHFRHEAGAAFAATEAYFASGRPVVVFTTT
GPGITNALTGLFAARWEGAKVILLSASTSAPQRGRWACQETSAYTMPSSGIFTSGPLFHYATTLESSDEL
PEIARRLALGLAQPGGFVAHLSIPTNIQTSLLKTSLPQVNFSRAPPTASEEAIAECVQLLSEGPFAIWVG
FGARGAAAEIRQLAERTGAAVMCSPRGKGIFPEDHPQFVGVTGFSGHESVLKYMQEQRPLRILVLGTRLG
EFTSFWNPAMVPSRGFIHVDIDPEVPGTAYPSAETFAIQSDVKVFVKALLKYFPERQDQSKVLSLPRPER
NVINPRTEGLVRPEVLMDAIQRVIVEGSDAIVMAEAGNSFAWATHLLRFTQPGRYRISTGFGAMGHAVTG
VVGAALARNGKAVAIVGDGAMLMNNEVSTAVKYQIPAVWIVLNDARYNMCEQGMALQGFKGVDTEIPQTD
FVKIAQGMGADGIRVERESDLQAALEKAMASTVPFVVDVVIDPTRPAPIGGRIQSLISQGA
>gnl|CDD|411517 NF035928, holin_1, bacteriophage holin. Holins form transmembrane pores for releasing endolysins that hydrolyze the cell wall and induce cell death
YVFQDWEFVKWLLVLIVVDTVLGVWKHWKHKDVSSKGFGRIFKKILVYISLLILSHVLTNFTVSGSVVGA
FQWFGTYIYVAMMVREAISILENIAAIYPILVPKSILKRLKDFNESG
>gnl|CDD|468266 NF035929, lectin_1, lectin. Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor
AALVTSPATLVNPFIGTSNDANDFPGADVPFGMVQWSPDTPSRPPGGGYEYNDSSITGFSLTHIAGPGCG
AAGDVPVLPTVGAVDNSATDSFSHANESASAGSYKVALDNKVTTELTATTRSGMARFTFPSTTQANLVFK
LTGSQNGATSTQFTVVSATEVSGQVTSGRFCGAGNTYTVYFDMVFDRPFTSQGTSAAKSTLPPPSPHRAS
KNAPEKPNKPVLHGDMPKAPGGAAAPDAAANAHVTFDTTAHPVVQAKVGISYVSVANAVANRTAENPGWD
FDATRAAAQNAWNSALGKIQIGGGTADQQRIFYTALYHSLLHPNVISDTNGQYYGFDGRTHTVDPGHHAA
YANYSGWDIYRSQAQLEALVSPYYAFGARDFDTSAALSGLVKQASTANNDRPGLNYLDAPGYMPHDGSYG
CCNFYGPVATTLEYDTADFALSAFAGALGDTANQKTYADRAQDWRNVLNPASGFVQPRNADGTWTGGFDP
TSGTDMVEADSWIYTGMVPFDVAGLATAKGGNTAMNHYLDTVLRSYTGANGYAWVGNEPSIELPWEYDYT
GEPYKTQGTVRAIQDQIWSDTPSGLADGNDDLGAMSAWYVWSALGMFPMTPGTSDLALGSPLFTQAVITL
PSGGTLTVNGNGAADDAPYVQSATWNGAAWNNAYAPTTAITSGGTLTYTLGTSANTSWATAASAAPPSYG
GDVAAPPSPRVGPVTSGVSAGLCVDDAGSGTGDGTHVQIWGCNGTYAQDWTVAGDGTLRTLGKCLDVANS
GTTNGTLVQLWTCNGTGAQQWKPGAAGSLVNPESGLCLDDPNSSTTEGTQLQIYTCNGTAAQNWTLP
>gnl|CDD|468267 NF035930, lectin_2, lectin. Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor
QTVELRSSGGYQSYRLPDDVTQVELVEQLAGACRFNRTWGYDLGNRELWVNGGCGGRFKITTTAAQGNRE
GSSSNTGAAVAAVAAIAGIALLANKNDKDKDRDRDYPDYPGQGGGGWGGREIRGKGGLCLDVSGGLRPGN
GLIVYNCNGGENQRFTWGRGGELRVGDLCLDVADGNTRDGARVIAWSCSGGPNQRWRWRGGQIRSRLSGK
CLDIEGGRARPGQPVIVWSCNGGPNQRW
>gnl|CDD|411520 NF035931, lectin_3, lectin. Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor
PPRSTQVDVQRMSRSLGNIGLTCELNSPQACRGYVADVLATFPREGTPHNITGARAGASKEYEYQIVSRD
PQAWMDQVNVIMANAEWVRANHIFAVDYDRVLDTREETTLHLIQNIFISVALVLGRLSGGHIDPDQLLKY
LGDWISDTTSNQHYVSQREFWFVESLHVAHIDGTGTTTRVGGITYDYKLEVSDIRNKKSTTHRSSLEMER
WSMTFSSGTILNSIFE
>gnl|CDD|468268 NF035932, lectin_4, lectin. Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor
LKEATPTKVTVESLKKQLHNIGLTCEQTSDEKLQEYIDEVRSQLPSGEVQTFAIGAPVEGLAGAAPAGAQ
EFVDSVSAADPATRSFASRLASTDPGTRNFVEHLLKDNPGGGEFVSQVREVDSEAPDFAERLAADNPSGL
LFLATLALLGLTPAATGNWEPDQSGNGYSPELEYIQYPDHFDKLKDKRGKPDKRFGGVEYRPPSYTGNYT
SADAIKKLFVEVGTNASATLVKGLDKDDIEAVLSNAIAPLNDENASDYDKTDSRVIFLVDNYDPETGEAD
GIGVLTIEWHLQIKDYKRKKKDDRHDTTLKITARSVLY
>gnl|CDD|468269 NF035933, ESAT6_1, pore-forming ESAT-6 family protein
AQEAAAPADMAAAYEAARNQLGVLKYCQEKGHIDGDAVEIQTKLLGMIPAGDTAKGDAAEAKGKKGTVSA
MGVEQSLEDAAKAQNTTEEALCKQMEAAVKQAGAQLP
>gnl|CDD|411523 NF035934, ESAT6_2, pore-forming ESAT-6 family protein
EGIKISLAEVSKTAGTIRTLNQQLYDRLEEIKKEMNSLASTWQSDASETIRTRFNALAPRFEEYRQIIDS
YAKFLDTTVSSYDSAETTINNNASAF
>gnl|CDD|411524 NF035935, ESAT6_3, pore-forming ESAT-6 family protein
DRISYDTGASAQVQGDIQGIIGRLESLIGERDQQVKAAMADFQADGVSDEYHGVEQRWNNAANEVRSIIA
LVKTTLEKNDETAQTTLSRARAAVQNIG
>gnl|CDD|468270 NF035936, agg_sub_LPXTH, serine-rich aggregation substance UasX. Members of this protein family are repetitive, serine-rich surface proteins of the Firmicutes, found primarily in the genus Leuconostoc. The variant form of sortase signal, LPXTH, is replaced by LPXTG in members from some lineages, such as Weissella oryzae, and therefore recognizable. Some members of this family have the KxYKxGKxW type signal peptide as seen in the glycoprotein adhesin GspB, a substrate of the accessory Sec system for secretion. WOSG25_050600 from Weissella oryzae SG25 is identified in a publication as an unnamed aggregation substance, a conclusion supported by the sorting signals and composition reported here. We assign the gene symbol uasX (unnamed aggregation substance X) based on our evaluation of the family
DTSTAQSVQATTTTLPQVKAVVLSATTDPVSDASSTVDDGTTGKSLDDGTPVDDGGSSSSSDNGTSSSSD
DNTGSGTPDPTPGDNNDNGSTSPDDNGGSNSDNGGSSSSTDNGGSSSDNGGSSSSDNGSSSSSSDNGGSS
SNGGGTDSSNTGGNGSSTDNNTVPLTPTTPDVNDQGELNHVKPVPVTPDNSGNVVVVPTQVASVPSVARA
VEAYNQALTANDKDANNAKVVEAKQKLDDAVAKALPETHATEKSSMGSIGILALAMSGLVALGALIFKRK
K
>gnl|CDD|411526 NF035937, EboA_family, EboA family metabolite traffic protein. This HMM describes a narrow, cyanobacterial-only clade of members of the EboA (eustigmatophyte/bacterial operon A) family. Members of this family appear required for transport of certain secondary metabolite precursors to the periplasm, including (but not limited) to precursors of scytonemin. More than half the members of this clade belong to scytonemin producers
IINLLYSWLSQQVSTEALAWLEEKQEQISQGAAQRVFFTAFSAVPRYTGKQDLQLTLEDLQAASALRSGW
CPGHWSVDQAARTLLVLSLPHDDAEKYLQTLEQVFTAADVGELVALYQALPLLPYPEKFRARAAEGVRSN
MTAVFNAVALRNPYPAEYFDDLAWNQMVLKALFVGSPLHLIQGLDSRANPELAKMLIDYAHERWAAKRSV
SPELWRLVG
>gnl|CDD|468271 NF035938, EboA_domain, EboA domain-containing protein. EboA (eustigmatophyte/bacterial operon A) belongs to a broadly distributed system of six proteins. The ebo system in general appears to involved in trafficking certain of certain natural product precursors whose biosynthesis requires export at least as far as the periplasm. Scytonemin is an example of one natural product whose biosynthesis requires an Ebo system
DDAARVLLLLALPEADAEAYAAELEQLFRTGDAAERRALLRALPLLPYPEAWLPLAADALRTNDTRVFAA
AAGPNPYPARHLDEHAWNQMVLKALFTGVPLARIAGLDERANAELARMLADYAAERWAAGRPVPADLWRL
V
>gnl|CDD|468272 NF035939, TIM_EboE, metabolite traffic protein EboE. EboE (eustigmatophyte/bacterial operon E) belongs to the TIM barrel fold superfamily by homology, as shown by Pfam model PF01261. Although its exact function is unknown, EboE is encoded as part of a widely distributed system that appears to allow export of precursor metabolites of various secondary metabolites so that biosynthesis can be completed outside of the cytosol
LTYCTNVHPGEDWAEVFAQLETYAPPVKARLSPDAPLGIGLRLSAPAARELAEPDALARFRAWLAARGLY
VFTLNGFPYGGFHGTVVKEQVYLPDWTTPERLEYTLRLARILAALLPEGAEGSISTLPLSYRPWWSAEEA
DARATRNLDELAAHLARLEERTGRLIHLALEPEPDCVLETTAEAIAFFEDLLLPAEKLEEAETLLREHIG
VCYDTCHLAVEFEDPAAALARLQAAGIPVGKIQISAALKVDDPADREARLAALAPFAEPRYLHQVRARGA
DGGTLVRYDDLPEALAALPGAGEEWRVHFHVPLFLEPYGPLSSTQDDLLEVLALLKGGPLTDHLEVETYT
WEVLPEELRPDDLAEGIARELAWVR
>gnl|CDD|468273 NF035940, prenyl_rel_EboC, UbiA-like protein EboC
AYLQLMRPANIVTAWADILAGFAISGFLTLTWSSAPNDISLIWLLLATIGLYGGGVVFNDVFDAELDAVE
RPERPIPSGRVSKQAALLLGSLLLLIGILAAFQVSLLSGVIALAIALAALLYDRFGKHHAIFGPLNMGLC
RGGNLLLGMSVVPEALSEYWFLALIPIVYIAAITMISRGEVHGGKKSTLIIALLLYALVIASLLGLAFLQ
NGNLLIALPFVLLFAILIFPPLIKAIQNPIPPNIGKAVKAGVLSLIVLNAALAAGFGGWPYGLLVLLLLP
LSLLLAKIFAVT
>gnl|CDD|411530 NF035941, GBS_alph_likeN, alpha-like surface protein N-terminal domain. Most Group B Streptococcus (GBS) have a member of a mosaic family of repetitive surface protein. The founding member is the alpha C protein (bca), but other named members with complete sequences include Alp2, Alp3, and Rib. This HMM describes the shared, non-repetitive N-terminal region, including a YSIRK-like signal peptide region
MFRRSKNNSYDTSQTKQRFSIKKFKFGAASVLIGISFLGGFTQGQFNISTDTVFAAEVIPGSAATLNTSI
TKNVQNGNAYIDLYDVKNGKIDPLQLIVLNPSDYSANYVIKQGGKYYTDVSQLQTTGAASITYNILDENG
NPHTKPDGQIDIVSVSLTIYDSTALRDKIDEVKKNANDPKWSEGSRDEVLTGLDTIKTDIDNNPKTQSDI
DNKITEVNELEKLLV
>gnl|CDD|411531 NF035942, T3SS_eff_HopBF1, T3SS effector protein kinase HopBF1. HopBF1, found in plant pathogens such as Pseudomonas syringae and in the human pathogen Ewingella americana, it a type III secretion system effector that acts as a protein kinase. It phosphorylates the eukaryotic chaperone HSP90 on a serine residue, inhibiting its ATPase activity. The inhibition interferes with the proper folding of client proteins of HSP90 that are important to resistance to bacterial infection
PNVSNAASIQRHLGISNVAAPTEFTSIPSLGEKLGSGSQKDVYHSRQDPRQCVCLIRPGTTGTISAEEYA
AKELAMTKRLKNLGFPVVDAHALVKYDGKVGLSKDYIHHALDSEDIIHNRKSLPTDKAFNKNVLKDCDEI
ISRLKTHSLHIEDLQFLIDEHGRVRINDPRDVIRSSPEKSIAKVRELRAIALNNLLDDSD
>gnl|CDD|411532 NF035943, exosort_XrtV, exosortase V
PLLLGLLALAIPTLVSLARQSWSTEQGAHGPIVLATGLWLLWREWPELRALARPGSAWLVALLLAVALPL
YVFGRITDIIEIEGAALYGALLAVLYALVGGRALRRLWFPLFYLAFLFPPPGTLVAALTQPLKLFISQAA
VGLLSLLGYPIARSGVTIQIGQYQLLVAAACSGLNSLISLSAIGLFYIYLRHNANWRYALLLVLLIVPVA
ILANFVRVLILILLTYYFGDAAAQGFLHDFAGITMFAVALLLIFALDAVLSP
>gnl|CDD|411533 NF035944, PEPxxWA-CTERM, PEPxxWA-CTERM sorting domain. This variant form of PEP-CTERM sorting signal shows unusually strong conservation across much of the hydrophobic transmembrane segment, including an unusual Trp (W) residue at position 6 of the seed alignment. The Trp is replaced by Tyr (Y) in a number of proteins hit by the HMM. The top-scoring members of this family tend to occur in Sphingomonas and related genera, encoded by genomes that also encode the sorting enzyme XrtV (exosortase V)
VPEPATWAMMIGGFGLVGGAMRRR
>gnl|CDD|468274 NF035945, Zn_serralysin, serralysin family metalloprotease
SGYDDVNDLLHYHDRGNGLTINGKPSYTVDQAGDQITRGDATWNGKNVFGKPANLTYSFLTSAPSSNPNG
DTGFSAFNAEQKAQAKLSLQSWSDVANITFTEVSAGQKANITFGNYSDSGQAYAYLPGTSDVSGQSWYNY
NSDYIRNLTPDLGNYGRQTLTHEIGHTLGLSHPGDYNAGEGNPTYKDATYAEDTRQYSVMSYWSESNTGQ
DFKGHYASAPLLDDIAAIQKLYGANMTTRTGDTVYGFNSNTDRDFYTATDSSDKLIFSVWDAGGNDTFDF
SGYSQNQRINLNEGSFSDVGGLKGNVSIAAGVTIENAIGGSGNDVLVGNDADNILKGGAGNDVIYGGGGA
DQLWGGAGKDIFVYGAVSDSTPSAPDWIMDFVSGIDKIDLSAFNQGDGGGGFLHFVDAFSGKAGEALLSY
DAQSNLSDLALNLGGHANPDFLVKIVGQANQATDFIV
>gnl|CDD|468275 NF035950, RumC_sactiRiPP, RumC family sactipeptide. The founding member of this family of radical SAM/SPASM-modified sactipeptide bacteriocins is ruminococcin C1, AEC03333.1 from Ruminococcus gnavus. This bacteriocin, from a human gut bacterium, is interesting because of its anti-clostridial activity. Known homologs to RumC1 average about 65 amino acids in length and have four invariant Cys residues
KLVNPKGETLETGANFEGSRSGCVCSGTVAVANSHNAGPAYCVGYCGNNGTVTRNANMNLAKT
>gnl|CDD|411536 NF035951, rSAM_RumMC, RumMC family radical SAM sactipeptide maturase. The RumMC family of radical SAM/SPASM domain peptide modification enzymes creates sulfur-to-alpha-carbon (sactipeptide) linages in RiPP peptide natural products in the family of ruminococcin C
MKKFYELVPDENYGRLGTVFETTNNKYFYDTGTGKVFECGEVEYKILKYLFEYNDLNPKNIYDKYSAEEV
CDSYEEILEMIEKEHILQAPPYKEFVRETDEELEALLDYDLQQVILELTEKCNLRCKYCIYNEYNPAYRN
FELQDMDWDTAKRAIDYARRHSGEKVAVTFYGGEPLVKFELMKKCIEYSRMIMKDKELTFSFSTNLTLMT
PEIAKYIASVKGCSVLCSLDGPKVIHDAYRVKIDGKGTFEKAIQGLRYLVEAMGERAKERIIINTVVCPP
YSKKKLDMIQEFFDKLDWLPKELDKKCDYVEGGSLRDEDIDVTFLDGEDIIEEYQGFELDSIRSWALDNV
LEQSDDKGYSFGLAKDNLVRIHNRFLTDKPCKRLKRNGCCIPGNRRIYVKVDGNFLLCEKVGDSPSIGNV
FEGIDLEKVKKYYLEEYDKKSIEQCSNCWAVNLCGICYAACYRENGLDIEAKNNACDYQKEQAKGELIAY
YQLLEEKPEVIEKIKDIPII
>gnl|CDD|468276 NF035952, WxPxxD_TM, WxPxxD family membrane protein. This uncommon, extremely hydrophobic protein of about 240 amino acids occurs sporadically in members of the Firmicutes, including the Listeria, Bacillus, Anoxybacillus, and Terribacillus genera. The protein is named for its most distinctive motif. The function is unknown, but the size and hydrophobicity suggests a transport-related function
KKKRLLLILILFLFFSVVWYFQNSPYLDADPEYELLLYMNGSAFGYSSIKAYTLFYTIPFLLFLNFFFKK
EHPYAIVRYKSRTKLYNKRIKNIIISSLLFSFIHLIVNLLFTFIFFDNSLLKESNFYLITLLNFLLLFLF
YFSIGLLYRIIYDLSNSIGIALIGTFLIIFLLYFLDKLLLNGVWTPLKDLNIFDPLLENGWTLSSILFIY
LRQLLIVLILYLIGSFIFERKDFI
>gnl|CDD|468277 NF035953, integrity_Cei, envelope integrity protein Cei. Cei (cell envelope integrity), as described for the founding member Rv2700 from Mycobacterium tuberculosis, is a transmembrane protein with an extracellular LytR_C domain. It lacks any DNA-binding domain and is not a transcriptional regulator. It shares homology to C-terminal regions present in some members of the LytR-CpsA-Psr family, a family in which some characterized members transfer teichoic acids to from carriers to mature peptidoglycan
DRHGRPFRRRRPLPALILVAVLAVVAVVVWVVALTSPDDVAEAVACNPPPPAAPEAPPPPLGTQVSRDAM
LDVAPAPLSDTKVRVLNASGQRGQAGEVADDLRDLGFAPAPDAANDPVYANQDLECQGQIRFGPAGRAAA
AAVWLVAPCAELVRDGRTDDSVDLALGTYFTDLSPSQDAQAVLAALRSADPGDATTGVDPALLKAAHTAS
C
>gnl|CDD|411539 NF035954, ocin_CA_C0660, CA_C0660 family putative sactipeptide bacteriocin. Members of this family are Cys-rich peptides about 65 amino acids in length, regularly found in the vicinity of the radical SAM/SPASM domain enzymes. The most closely related such radical SAM enzyme is the RiPP modification enzyme that introduces sulfur-to-alpha-carbon peptide (sactipeptide) modification in ruminococcin C, whose precursor is very similar in length and in Cys content and arrangement
MKLVNPVGRDLTTFETEVNSCHCVCSSGSWNAKMAGWDDGTCGCECCWGNHANNNANYNVAYNA
>gnl|CDD|411540 NF037932, ocin_sys_WGxF, bacteriocin-like WGxF protein. Members of this protein family of hydrophobic proteins about 60 amino acids long are found various members of the Firmicutes in three-gene contexts that suggest a role as a bacteriocin or an immunity protein. The protein is named for its most striking sequence feature, a nearly invariant WGxF motif. The two conserved neighboring families are TIGR01654-like (e.g. WP_149116529.1) and TIGR03608-like (e.g. WP_149116530.1)
MKIIGLTLLNCILILITVLIHKIIFRVFLLPYDSLLFYWGLFVAIFFILNLLTNLIFLK
>gnl|CDD|468278 NF037933, EpaQ_fam, EpaQ family protein. EpaQ, as described in the Gram-positive bacterium Enterococcus faecalis, is encoded with the enterococcal polysaccharide antigen (epa) operon. It is distantly related to some O-antigen ligases of Gram-negative bacteria, and may have a similar molecular function. EpaQ contributes to biofilm formation and resistance to certain antibiotics
EKLLNKISALILLLTISASYFLWTAGIGTPTTLFLYANSAQLLTIGVIILLLLNVYKLKKADFLYIGLAV
VIFIFFSLFSELRHSSFFIDLLIPLIILFVLCFKWTEFDKIDRGILLLVFLVFLGITLYRIFTEIPKPVP
GNSIWAPSNKLSDIWINTNTIGSSLMTLALLISGLAKSFERWYIRLLVIPVYIAGLLGIWVCQSKTALVA
LIVFILLDILPKKLFLKIRAPFLIGYSLVLILAPPISYFAANSDTINLFTGREEIWKEFYETLFEKKQQV
LVGMKPFTFQRGWQILGNHNSYNSILNNYGLIGYIILFLLLLYFVGRITLKADLSNGQISFLIAFLAVMI
QSFMEDTLTAYHWIPIVYSLLGLASHK
>gnl|CDD|468279 NF037934, holdfast_HfaA, holdfast anchoring protein HfaA
ALAQSMGTGGSASFQAGYGRSRGQESTAVDGSTRDANGNRVIVDGVIQTGADQSVYSYSQSSGAGDSYSG
AGAGSGGGGIGGSTAIGNNLNVVVQGNNNTVIVNSTQTNNGNVTA
>gnl|CDD|411543 NF037935, holdfast_HfaB, holdfast anchoring protein HfaB. HfaB, part of the holdfast anchoring complex of Caulobacter and related bacteria, is a homolog of the outer membrane protein CsgG of curli biogenesis
LALALSACASAPAAGGAGNYAKPIGNAPVTANPTPYSAALVCLASYARQNGLASPRIAVGRISDYTGKVD
FDGGAKVTQGASLMAISALAKAGAPLVERFDTSVSELELKYANNKLISDAPEQAGQDPDNYRKIYAGQIA
GSDYYLVGGITELNYNIRSSGIDAYAGDVGDDGPKGNFSARTYVMNVALDLRLVDTRTLEVVDVVSYQKQ
IIGREISAGVFDFLNGNVFDISGGGSALEPIQLAVRTLVERAVLEFAANLYGVT
>gnl|CDD|468280 NF037936, holdfast_HfaD, holdfast anchor protein HfaD
NQINLGDVFADQTLNVVTVDDGVTVSTAAQANNVAGGVDDADASLTSNQTMSGAVTAHTTLTVNGTGGGS
SAVATTARGNYLSTTASQGTIDADAVQVNTGDVTARTQVEAPTARALDGGASSAAAIGNTVALGLPNGSL
TARADQSSQADVLAEVGADVQYSPAPANFNATAVANAYQASSTNSSAQDLIVRQTNAAATVTARTFVYYG
NGWNIAANATAMGNNLVLANQGGSLDVDGDQTNSSYVRAQAEVTSYDFGQAQITAYGVGNSAMAGNNGIY
LNLDNTQLNTGGVEALASFEGGNGYDAYVTATAIGNAVTGYACSTCGGAMNVNNTQTNNSDVTATSTATV
GSSGRNVVGGATAVGNSATFYVN
>gnl|CDD|468281 NF037937, septum_RefZ, forespore capture DNA-binding protein RefZ. RefZ (regulator of FtsZ), a DNA-binding protein in the family of TetR/AcrR family transcriptional regulators, participates in septum placement and in chromosome capture during the asymmetrical cell division in endospore formation. The five nearly palindromic DNA motifs (RBMs) to which RefZ binds affect chromosomal localization, not transcription, so RefZ is not considered a transcription factor
KEKILDAAISLFNTKGFDGTSVRDIAKKAKVNVALISYYFKGKQGLLEYLVTSFFEGYLEILEEGFEELK
NLSAKECLKQLVRNILHYQQEHHQLTRFVHRELSLDSQLVREIMSTYLAKEKYYLKKIIEKGIKEGEFRK
QVSVSFLIIQLKGMLTMPFLNPQYLREVLHLEPSEPYFVEKYLKEIERWIDGTLC
>gnl|CDD|411546 NF037938, Myr_Ysa_major, MyfA/PsaA family fimbrial adhesin. The related adhesins MyfA and PsaA are fimbrial major subunits of Myf fimbriae from Yersinia enterocolitica, and Psa (also known as pH6 antigen) fimbriae from Y. pestis
MKKFAKKPLAIAVLMLAFGGMANMAHASDVIHSQDVSADKEVKQGGAFKVEFAASPNEIVSGKQAKDVPA
FVLKVSDSAEHSGWRLIPTGSSKGGYMYSDSGDKVELHSANWTWDGGDNNWYINDSGSAEVEATLYVAKG
TVVKAGTYHFTGRVEEYL
>gnl|CDD|468282 NF037940, PKS_MbtD, mycobactin polyketide synthase MbtD
LPDGRVPVLLSAHAEELIGADAAAILDYLERHPAPGVAAVAATLLRTRRVRRHRAVVRAADRAELAAGLR
ALAAGEEHPLVTRSAETSAPRIAFVFPGQGNQWPSMGAQAYRELPAYRAAADRCAAAFVAAGHPSPLPYL
TAPAEGDWSQVEIQGAQFTHAVALAAVWRSCGVLPDLTVGHSLGEVAAAYVAGAITLADAVAVVIARATV
VDRLPGDYGMAVLGVGPDEAQALIAETPGWLELSVVNAASSVVVSGERDAVAALVATARSRGVFAREIDV
DFPAHTSALEPLRDDLVELLPTAQFADSPVQFIGSATGDVVPAGTDFADYWYANLRNTVRFDRAVAAARR
CGAGTFVEMSAHPALLFALGDLVGDESALVVGSGRRDEPLTETLSANIAAVAVADPGYRWADLVGPDNQP
PLRGFPNAPMRAVHLWAAPEPLPPVSGLTVAAETWEPVTPRTPPAGRRRRIAVLDLAGPRGALADRLRAA
VDAHPGTELVDPADADLLVVVAPALDHPDAAAAVTALAALVDAGLLDYPDAIGPRCRDVWLVTVGGEQVR
AGEPVALPAQAALAAMHRSIGFEHPDQAFRHLDLPSWDLDAATAVAAVDALLGGAGELALRGGGGPTLFV
RTLRECAPSAPAWALDSGALDEVVITGGSGAVGLHYARHLAERGARRIVLLSRRGVDPAALAELAAGGTE
VVAPQCDITDPEQLAAVAAEHGGDGASLLIHAAGAATFADHDDLTGAAFADTAAAKVTGLARMAELWPLR
PDARILLCSSVSGLWGGRGHAAYAAANRMLDVLAGQLRADGRDCTAVRWGLWRGSGIVDAAEIARIERSG
LRPMAPDAAIEASLRDYPGDPLVFSADADRLQVFLGSQPMEAPSPAAPDVAAEAVPAGADAAAVVRAELA
AVLKLPDAATIDLDASLLDLGVDSLLALDLRKRLRRATGRSVPLATLLGGITGAELIAGLDDR
>gnl|CDD|468283 NF037941, PKS_NbtC, nocobactin polyketide synthase NbtC
SEYRLPDGTIPVLLSSDTPDGLRREAAALLDYLRAHPEVTPERVADMLFRTRVARRYRALAMVTERAELL
EALRAVAAGEPHPAVVRGDTAASARRIAFVFPGQGSQRPGMGRVFYELSPAYRAEVDECAAIFQELFGHS
PLHYLLGDEGPYEDTVWEVQPALFMQMVGLAAMWRAAGVDPAATVGHSQGELAAAYVSGVMTLADAVLVV
TLRARLVERISPRGYSMAVVGMDREECEALLARNSGWAELSVVNSPHILAISGDRDTVVEMVDALTARGR
FAREIRVAYPAHTSIVAEFRDEFEAFLGDELSNPEFLDTEIDCIGATLGEPITPDLPVGDYWYWNLRNRV
RFDRAVAAAVEDGVDTFIEVAEHPTLQLALQENLSLVPPARDFQVVGTSLRTAEDLGEFTRNLAQVAVHD
LGYRWDALRTDSDGRPRLPLRDFPNTQMNPKRLWAPYAACTPAAEAETEAAAPPPQRLVEQWVRLERRSL
VPPRTLGVVDHTGRCGDLADALCAAADRHGATARIVDPAAAAASAGDDFDTAVVLLPELPDLDTAAAAAE
VAAFFADRTWLPDLDGVRPDCWLVTVGGEAVVAADPPPHLFHAAASAGFRCLGAEHPGIAFRHLDLAAGL
AAPDSAAAIVGALHTAGEPELALRGGGLYAKRLVADDASAAASDAADLRHVVIVGGTGNLGLEFCEHFAR
AGAGRITLVSRSGETADIARRLRRLRRLGATEIVVRACDVTDAAAVRRLAAEIGDRPVDLIIHAAVDYVD
AELADLTAEKVRAAARAKVVGLDHVLDTVPLTADARVLLCSSTAATIGGRGQILYAAVNRMLDAAAARLR
AQGIDCVSVQWGLWRVVGPLDAAGLAQVAEAGVVPMAPADAIAAGLTGLAGNAIVAAADWDRLRAVLSAF
GYGPLLSQLKELAPPAETPTPEPVAASPAAAASPAPAAAPVPETDLAERMRTLLAEVMGMDGAETIDGSV
PLVALGLDSLQALDLRKRVKAELDRDLPVAAILGGASLDDVVTLLG
>gnl|CDD|411549 NF037942, ac_ACP_DH_MbtN, mycobactin biosynthesis acyl-ACP dehydrogenase MbtN. MbtN belongs to a family of dehydrogenases that in most cases act on acyl groups carried on CoA. However, MbtN appears to act on an acyl group carried instead on the mycobactin biosynthesis acyl carrier protein MbtL
TLDEYRELLDEVFDERVRAWTAEAEATERFPRELIEHLGRSGVFSAKWGDGQHPDVAKLVELAFALGRLG
SAGIGVGVSLHDSAIAILRRFGRSDYLKDICEQAIRGEAVLCIGASEESGGSDLQIVETEVRSARDGFEV
RGIKKFVSLSPIADHIMVVARSVDHDPTSRHGNVVVIAVPTAQVEVQTPYRKVGAGPLDTAAVHIDTWVP
ADALVARAGTGLAAISWGLAHERMSIAGQIAASCQRVIGITLARMMSRRQFGHTLYEHQALRMRMADLQA
RVDLLRHALNGIAAQGRLDLRTAAAIKVTAARLGEEVVSECMHIFGGAGYLVDETPLGRWWRDMKLARVG
GGTDEVLWELVAAGMKPDYDGYAEVV
>gnl|CDD|411550 NF037944, holin_2, bacteriophage holin. Proteins of this family are homologs of the mycobacterial phage holin Gp29. They can cause host cell lysis to release progeny phage particles
MPYLPSLALVALGLLVLVVLLVRVVRVLRRFRRTASMVAARTQDRAGLLRARSAALRVAFAQRR
>gnl|CDD|411551 NF037945, holin_3, bacteriophage holin. Bacteriophage holin can cause host cell lysis to release progeny phage particles. Proteins of this family have about 60 amino acids, and a transmembrane domain is usually found on the C-terminal
NCPLLTGALFLCYNIVGMFVRFHPISRVKLLFGVAFF
>gnl|CDD|468284 NF037946, terminal_TopJ, terminal organelle assembly protein TopJ
MEEKRDYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYG
HDGVDGEGGFGFDAFDVFSSFFETINKSGAFLDDSVDESVSADDDLDRLFDDSKEPSFTSGLDEIVQFWE
AFIGNPDYGYYDENNEWNLILDKNLFTPESVIPTKNTDLVTKKDDIVVENFDNLNETTYKSIVDLLNNET
SGTLALKDGNKETINISNPTVLSKNLEFDEQTEKLDFSKLFLRKQLPRISETEVVEQPITNLQEPNLNII
YEVKIPQILLFNNATKRIKYTRNDCKGKSYTKEQITLDIQLPITDKLKLSVNYPGFGHIVGSKTKGDLTI
VFKVIKSKFFKLKKNDIHTAALVDPLVAYNGGEILVPTPNQLIKVKIDPGTKNNDQIIIKGLGLPARYDV
VTKTKYDQGDLIIHVYYASV
>gnl|CDD|411553 NF037947, holin_4, bacteriophage holin. Bacteriophage holin can cause host cell lysis to release progeny phage particles. Proteins of this family usually have two transmembrane domains
LDPRALGLALGILWGLSVLLLGLLARYYGYGERWVELLGDLYPGYEPTIGGSVIGAVWAFIDGFIGGYLF
AWLYN
>gnl|CDD|468285 NF037948, signal_int_SinM, signal integration modulator SinM. SinM (signal integration modulator) is a regulatory partner of the hybrid histidine kinase/response regulator SinK (signal integrating kinase)
MRLALLSVLLLGVACSSDKPPEPGEPDASGPEDSGTDAGSDPDGGTADDGGSTDDGGTGKVDAGPGEEDA
GSCEPPASVRETLLVPGLNTPRRLAVDATDLYISESHSLRPTQPDGEGQVLRLPRAGGDATSVAKGFIAP
DAIAVDAKNLYVLDQMGLWRVDKATGARGTVPIEASLNNVITGGTDILLTRLQGRDVLVVATGARRLVRV
DTTGATRSSLVLFEGTAGTQVRGARVDGTDVWFLVTGGTEPGLYRVPLDGSTPAQRVDASITAGTSLELT
PTHFLITEGGGGTGRVLRWPRAGGEARVLASGLQGPLFPVELNGAVYFKESVAGGSDFLRRVRGCPPGTS
DPVGPEGTGPGGLIVDGDTLLFTSQESGTGGAVGRVP
>gnl|CDD|411555 NF037949, holin_5, bacteriophage holin. Proteins of this family can cause host cell lysis to release progeny phage particles
MMLDTASEAGKGTAAIAGAGAAVLCPNEIASLAAAVLTALFVAAQLITLLPKMLDSIAELRKRF
>gnl|CDD|411556 NF037950, spanin2_1, bacteriophage spanin2 family protein. A number of bacteriophage proteins cause lysis of host cells. Holins and endolysins induce the disruption of inner membrane by degrading peptidoglycans. Then, spanin2 family proteins are involved in the final step in host cell lysis by disrupting the outer membrane
MRSRRRVATALLAAGLVGALSGCGAVQEASDTANQVGNAADKAQVCAEALKLAGFTPDTTDPEQAVEEAH
DAADELTDLAAKAADTTVNQAITGLAATLREVTLDDLDPASPAAWLQQKADQVAALTQAC
>gnl|CDD|411557 NF037951, spanin2_2, bacteriophage spanin2 family protein. A number of bacteriophage proteins cause lysis of host cells. Holins and endolysins induce the disruption of inner membrane by degrading peptidoglycans. Then, spanin2 family proteins are involved in the final step in host cell lysis by disrupting the outer membrane
MKNYFKILILLIIISLTSCQTRVVSPGKPLQDNSLELYQKYTIQTNDAKIHKMKVLKVDAEKIYGKSKKG
ETVEIEKSDIREVKKVDVLSSVIIGLAAIAAVIFVPI
>gnl|CDD|468286 NF037952, spanin2_3, bacteriophage spanin2 family protein. A number of bacteriophage proteins cause lysis of host cells. Holins and endolysins induce the disruption of inner membrane by degrading peptidoglycans. Then, spanin2 family proteins are involved in the final step in host cell lysis by disrupting the outer membrane
LLLCLALAGCGSLPGLLKGAIGGGPNVAANVQAGRTNAQTVGQSTVTDQRIVRPQARSIEQSAGDTGVRA
ERVQTVVVREDPPWLWLVALIGWLLPTP
>gnl|CDD|468287 NF037953, frad, septal junction protein FraD. Proteins of this family are components of cyanobacterial septal junctions (microplasmodesmata) in heterocyst-forming cyanobacteria
IKKLLIPPKAYSWQTLIYLSVFSWLMSYFATGYIKDIIAFCGWLFLIAGTAWYTTDDPLRVPGTNMPVGA
VITGFLVSVFAFGNQEDVITPRTIVLWPTISALITAIPEFFEGSGTDVKAQIPKPEDRQKIIVLVASCML
ISCWLQFYFVVDKWLKEYPSLLADNFQRSTFVIRTEPPEKIPENGVLILNKLQPLVEEQINGRPWSEVER
WLLEANQRVGNLGRQVIEKNLGEYEEKELWRVEPRVSNTKSDGYKLDLLSIWTGPSSNPRGYYLKKSCQI
EPIASTSTVTTKKPEEKNTVAEIEC
>gnl|CDD|468288 NF037954, het_cyst_PatD, heterocyst frequency control protein PatD
LSLNYRQKYQELLTLLEQLQSDVTTNQLDAPTLRQRLEQLQQFFQQQILPLTDDELSPELSREQSYQTEI
SKQLRLLETDVMFLQGARQAATAQTRLKTISDRLTTLIGYCQAILQ
>gnl|CDD|411561 NF037955, mfs, MFS transporter
RLSLLYAVVFVEIGIAMPFMPVWLEALGLDAGVIGLLLALPIAVRIVATAPLMSLIDRGVGARRLLLAGS
LGLALTYALMPAAAALGWPLLALLVALNAVAQAPLVPSIDYLTLAAVRRDPRLDYARIRMSGSVAFLAAN
LAGGALLGALGERVAVPLLLTGLALVAALVALASRVRAAAAPPRPREAGRPRLPRVLWLAIAAGAAIQAS
HAAIYAFGSIHWRAHGISTAWIGALWAIGVVAEIVLFALLGRLPARWRTPFRLLGLGAAAALVRAIGMAL
LGGTLAAVVPLQALHGLTFGATQLGAMAAVSAFAPEGARGRAQGTYSAANALASASATLASGLAYRAGGP
LAFALMAPLALIGLCL
>gnl|CDD|411562 NF037957, freyrasin_like, freyrasin family ranthipeptide. A ranthipeptide is a ribosomally synthesized and post-translationally modified peptide (RiPP) whose linkages from cysteine sulfur atoms are to something besides the alpha carbons of other amino acids. Thus, ranthipeptides differ from sactipeptides (sulfur-to-alpha carbon RiPP peptides). The founding member of this family is freyrasin itself, the PapA protein from Paenibacillus polymyxa (see SUA72395.1). All members so far are encoded next to radical SAM peptide maturases
MLKQINVIAGVKEPLSRYGCHPNDICILCDTRDLCKSCDALDFCIKSDT
>gnl|CDD|468289 NF037958, QH_gamma, quinohemoprotein amine dehydrogenase subunit gamma
MKHLKPLNRKAKLIEEAVEEGRAEEVVAMQSVVGCTTTFDPGWEVDAFGGVASLCQPMEADLYGCSDPCW
WPAQVPDTMNTYPDWNKDCPAAARDWRKLQ
>gnl|CDD|468290 NF037959, MFS_SpdSyn, fused MFS/spermidine synthase. Proteins of this family are fusion of a N-terminal MFS (Major Facilitator Superfamily) transporter domain and a C-terminal spermidine synthase (SpdSyn)-like domain. The encoding genes usually near the genes encoding S-adenosylmethionine decarboxylase (AdoMetDC) on many bacterial genomes. It has been shown in Shewanella oneidensis that the fused protein aminopropylates a substrate other than putrescine, and has a role outside of polyamine biosynthesis
SAASLVVEIVAGRMLAPYVGMSLYTWTAIIAVVLAGFSAGHWWGGRLAERPAGRALRRTGWALLAAALTT
AAALLLLRLVAGPVLAAVLHPVAAIVALTLLLFFLPSLFAGVPAPVLTQLAVRGAERSGRALGAMFAAGA
IGAIAGTLLAGFLFISWLGSAGTLLVVAAVYALLALLFLWLAGGRRRGLAAAALALLAALALAGLALAAP
SPCDVESRYFCIRVVDVSADPGGPARLMVLDHLAHGINARDDPTVLFTPYAAMLDELARLRMGRADFSAF
FIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVAAEDFWFDPASATVLHEDARRALRRRPEERFDVIVG
DAFTDIAVPAHLVTREFFELVRARLTPDGVYLMNVIDHADRLRALAALVATLREVFPVVEVWTEARPPAP
GERRTFVLLAGDAPTPVSTIRARAPEPRRFARLPPAFVDALAARRSPPVLTDDYAPIDRL
>gnl|CDD|468291 NF037960, MFS_trans, MFS transporter
MLAGLIASFLGSSVVEGGVPGLVALGVLPVAWLALYKTLTEVIDFAAPLYARLLGKFSPGRVLVACELAE
VVLSLVALALILLGPGWAAPVLIAYLLLASVLPLVTDIAEEFYGADLAQVDEKAALRFNASLYSALAFVG
LVVGRPLGSLLASVSIAAVLAVNLVLSLAAAALRLRSRRTVAPEHAGPANESDAEDFLAAGSREPLRAFP
RDLFRSGPASPLLSLLITLAGALTGEYVLLWVAGAASGLGAFVALALVLAVFGVGAAVGPLLGRALRRRG
GARRVLRLAAALSGALTLAVALYLLLVGADVSLVVALGLVVLNAALWRARNVALETLRQVLFRGKRFARV
MGWSFSFGALGGLAGSWLGYLLRAAQNPLWAL
>gnl|CDD|411566 NF037961, RodA_shape, rod shape-determining protein RodA. Proteins of this family are members of the FtsW/RodA/SpoVE superfamily. It has been reported that RodA proteins play important roles in maintaining cell shape and antibiotic resistance in bacteria
DWITILLYLLLVGFGWLNIYSASHTGESTSIFDFSQIYGKQLIFIGLSFVLIILILAIEAKFYERFSSII
YIISLLSLLGLFIFGKTINGATSWYAIGGFTLQPSEFAKAATALALAKYLSDIQTDIKRFKDQLKAFAII
LIPAILILLQPDAGSALVYFAFFFVLYREGLPLIYLIIGFILILLFVLTLKFGPIWVLIIAALLIFLYYF
LKKKKKPPILKIIIILLICILFSFSVNFVYDNVLEQHHRDRFSLWLGLEKDPEKLEQMKKTIGYNTNQSE
KAISSGGFTGKGFLEGTRTKGNFVPEQHTDYIFSTVGEEWGFLGSSLVVLLFVLLLLRIIYLAERQKSQF
SRVYGYSVASILFIHFFINIGMVIGLIPTIGIPLPFFSYGGSGLWGFTILLFIFLKLDANRINEW
>gnl|CDD|468292 NF037962, arsenic_eff, arsenic efflux protein. Most proteins of this family have 8 transmembrane domains with two 4 transmembrane halves separated by a hydrophilic loop of variable sizes. It has been reported that some proteins of this family are involved in arsenate/arsenite resistance
DTFKLVPFLFVTYLLMEYLEHKTGGKLSRIIQKAGKLGPLFGALLGALPQCGFSIVASTLYSGRVITFGT
LVAVLLSTSDEAAPLLLANQVPAGAILPILGLKFVVGVISGYAVDLIFREERRIKHKSKNIYAREHEELF
IHELCEREHCHCEDEEESEHDHESHKEILRSALMHTLFITVWIFAVTLVLNIVIEIVGEDALASLFSGHP
VLSPFLAALVGLIPNCGPSVVITELYLEGVIPFGAMIAGLLSNAGVGLLVLFRLNPNRKAAIVITLYLYV
PAVIVG
>gnl|CDD|468293 NF037963, heterocyst_HetZ, heterocyst differentiation protein HetZ. The HMM distinguishes HetZ itself, a heterocyst differentiation protein, from a closely related paralog
IFQLLFQELRQSTRASEQNCREVAERIAEEVNRICTESKRIQASGEVESWAMTLARHRLQQCLRYYQLGS
RRGRVELHSTLSAIVYRYITPPQVQSSYQARLTLIEDFLQGFYLEALNAFRREAQLPATYRPRTLLELAE
YMAFTERYGKRRIPLPGGRSQQLIILRAQTFSQQQPPETSVDIEQAAEGSSGESDQTWNDASVQQVREAM
VAQDPEPPAEDSLRETVIEELMAYLEERQQSDCADYFALRLQDLPTSEIEAILGLTPRQRDYLQQRFKYH
LIRFALSHRWELVHQWLEADLERNLGLTPQQWQLFQEKLSSEQRKLLQLKQQGLSDSEIAQALGCTVTQV
QKRWFKLLEQAWEIRN
>gnl|CDD|411569 NF037964, HetZ_related, HetZ-related protein. Members of this cyanobacterial protein family are paralogs of the heterocyst differentiation protein HetZ and occur in largely the same set of genomes
QALVQLLLQELQAQLKSSPRSAQAVAMRIAKEVERICDKSDRIQNSGEVRSWQLTLARHRLQKCLSYYKL
GSKQGRVELHSNLSAMVYRHIAPSRAQLGFQARYNLIEDFLQGFYIESLKAFRRENELPEDYTPRTQLEL
AEYMAFTEQYAKRRITLPGGNNQQLIVLRAQGFARRQPQETSVDIEMAVESPKGEEAEAYSRSSAVQQVR
EQMVSETVDPAEAVLRDRVISELVQYLESQGQSDCIDYLVLKLQDLSAPEIDEILGLTSRQRDYLQQRFK
YHVEKFARSHNWKLVHQWLGADLDQKLGMSSQQWEAFLSQLSPQQQQLLQLKQAQLSDQEIAKALKCTPK
QLQKRWTQLLELAWKIRNSS
>gnl|CDD|411570 NF037965, HetZ_rel_2, HetZ-related protein 2. Members of this family are cyanobacterial proteins distantly related to heterocyst differentiation protein HetZ, which also has a much more closely related set of paralogs in heterocyst-forming species
AQQWRSRLAEDCPEQSPATRESIVRWLLGEDPERFETLTPKELEIAKQAMEYRYRILRQRYLGVSPERAY
RNLITRLGSLVLLRNKIRTWVALSRDRQRAVVDVLQEVIQEMLQSDRYLQQQIAWIAECTKDSRLRNALL
LASIEEYCLRPIRNQPLLVYRFVNYLRRSQRGGLTQVPGGELVRLVSEEILTDDSDNPVSLLDNQAVAQY
QEQQAWEEQQALRQLVQQEFEAYLAENLGPTAAEWLRLYLQGKSQEAIAKQLNLPIKQVYRLREKISYHA
VRVFALKGQPELVANWLETSLQEHNLGLTPSQWQQFWESLTPQQRQILELLKAGQSIEAIAKELKLKTHQ
VMGEWTKLYLAAQALRN
>gnl|CDD|468294 NF037966, HetP_family, HetP family heterocyst commitment protein. HetP and its paralogs occur in heterocyst-forming members of the Cyanobacteria, and play a role in commitment to development into heterocysts, which specialize in nitrogen fixation rather than photosynthesis
NQQISESNSNFDKIITPEQFEQIIEAILAGKYSWACVLILRFAGYNPLHYIPYRTYNRLLKEN
>gnl|CDD|411572 NF037967, SemiSWEET_1, SemiSWEET transporter. The SWEET (Sugars Will Eventually be Exported Transporter) is a superfamily of sugar transporters found in both eukaryotes and prokaryotes. Eukaryotic SWEETs usually have seven transmembrane helices (TMHs), but most prokaryotic SWEETs (SemiSWEETs) have only three TMHs. Proteins of this family have 7 TMHs
GLLAAALSIALVWPQVWRSCRHRRTRGLSPTACWLAVALPLGWLTYGLLTGDPAQIVTNAVVGAAGTAVL
VALLLTQPELRSRRALLRTAAGAAGLLAAAAGSAAAVALPGADAAAVAAMLGAVLAVVGAAAALPQPLSL
LRDRTQDLSGLSPARWRLAAGSCASWTAYGLGTGQPAVWLSAGVGLVCALVVCAVL
>gnl|CDD|411573 NF037968, SemiSWEET_2, SemiSWEET transporter. The SWEET (Sugars Will Eventually be Exported Transporter) is a superfamily of sugar transporters found in both eukaryotes and prokaryotes. Eukaryotic SWEETs usually have seven transmembrane helices (TMHs), but most prokaryotic SWEETs (SemiSWEETs) have only three TMHs. Proteins of this family have 3 TMHs
GYVAATLTTVAFLPQVIKTWKTKDTKDISLGMYLVFTTGVALWLIYGILIGDLPIILANAVTLLLAGIIL
VLKLRY
>gnl|CDD|411574 NF037969, SemiSWEET_3, SemiSWEET transporter. The SWEET (Sugars Will Eventually be Exported Transporter) is a superfamily of sugar transporters found in both eukaryotes and prokaryotes. Eukaryotic SWEETs usually have seven transmembrane helices (TMHs), but most prokaryotic SWEETs (SemiSWEETs) have only three TMHs. Proteins of this family have 3 TMHs
MSLIERIGKALEPFMLFMGLVSPLATLPQLYKLYFSHSEHASGLSLTTWSLYAFIALLWTIYGLYHKNPT
IWVGNGLGFLMYLAMVVGILIHAGVTF
>gnl|CDD|468295 NF037970, vanZ_1, VanZ family protein. VanZ was originally identified in Enterococcus faecium. VanZ increases teicoplanin resistance in Enterococcus faecium, but has no impact on vancomycin resistance. Proteins of this family are homologs of the VanZ protein. They may be involved in teicoplanin resistance
WMAVIFYLSSQPGDESSSLSPFVQKLKELPKLEFLEFFIRKWAHFFAYFILAILLFLALGKFRKKGKSKL
LALLLCVLYAVSDEFHQSFVPGRSPDVRDVLIDSIGA
>gnl|CDD|411576 NF037971, lipo_BcpO, CDI system lipoprotein BcpO. BcpO is a small lipoprotein, about 74 amino acids long on average, encoded in Burkholderia bcpAIOB locus systems for two-partner secretion and contact dependent growth inhibition
VVVSLAVFALLAACETVPPDAPPRPPPKPEMEPVLPSWSSTTWVMGYWKWSGTEWVWIPGHLAPKP
>gnl|CDD|411577 NF037972, HuaA_fam_RiPP, huazacin family RiPP peptide
LVCGLGCAAPCLGICALDGPSPIADAVGVTSGAKAGHASA
>gnl|CDD|468296 NF037974, SslE_AcfD_Zn_LP, SslE/AcfD family lipoprotein zinc metalloprotease. Members of this family are surface lipoprotein zinc metalloproteases, from the family that includes accessory colonization factor AcfD from Vibrio cholerae, SslE (YghJ) from E. coli (Secreted and Surface-associated Lipoprotein from E. coli), and VPA1376 from Vibrio parahaemolyticus. Each is about 1500 amino acids long, and SslE is a known substrate of a type II secretion system (T2SS). SslE is known to have mucinase activity
VTCNGQPANNGTFTVKQGDSVSCTLGLATFGDFFDAIPKRTSSRAVNRKVLALFDADEFAEPDAGSNAQA
LLKSIGTCPGEDQICLDEIDSFDILDFYNNLDLAAVDFFLLPKEEEANDNVGDKPPSHHDPDVVPEVTPG
TSNDLNAGFVSANAESSYAYKPSAEEKILTKGRLTDSQGRPVAGVSYFSASSRGVTDENGEFEFLWGETI
SFGIDTFELGSVRGNQVSYKLTDLGDNAVVGANIEALIERYATTQDNNTLEISDKVTQVFALYPNVINEI
INLSLPNGAKLLDIGGGTTQTVPNEFEAQFSQGLAAEIDQALCQPPCWFRSFFSKPKTASDDSGGYVTAS
LQKLWGGVEQFHVFHDNTNFYGSTGYARGQRAVNISNRAFPVMMPRNDNNYWIPFGEEKAWDRDGLAYIT
EAPSMVRPEKVSKDTATFNLPFVSAGEIGKGKVMFMGNARYNSILSCPNNYWWNGGVNIDGQCQQCTYDS
GSMKNFFSNLFRWLTPDKSEGINVGTNIPKVYFKRHGQVMGNKYDFFIDPRFGFVNTVQLLSFGGLDPET
TPLLILQGYEYKGGGDGYTLPVVADLDQPKLSQDDVTALIDYVNRGGNILFMEAIENTTNPEPIARLLDA
AGIAFGGGNSVVTNNQPSCGYSDRCRSQRQPNLHVLERYAAVVGERFQDPDLPYFIVNQDGSVEWPYPDD
KPKLEIARYTETDEDGGKMVTRYAFIDVKDEEELAAAIQEILAAFPGYPECKDSNYHYEVNCIEYRPGNG
IPVRGGMHRPDYTRYELSPDVVKAMVKAANLGTNIEALYQHELYYRTKGKQGERLSSVDLNRTYDNLSVW
LWNDLDYRYESSVQDELGFKRFTEFLNCYTNDKHQGGTTCPEDLKQSLIKNGMIYGEGELAGQMNPSYPL
NYMEKPLTRLMLGRSFWDLDIKVDTRQYPGETSGSGGGATVTIDTNNNTVAYFAGNRQSTGLWAPALQEV
TVSGGGEATITVALADDLTGREKHELSLKRPPRMQKSFVYDGGSSLTFTVPYGGLIYIQPGNSESVESTF
SFSGVVKAPLWKNGQWVNPLNSPAPIAEIDSGSFIYTTPKANLNASDIAQFAKDLNRFAEDASDFYGRDE
GTSDGKHRRFTYSALPNNRHRFVNDVQISIGAAHSGYPVMNSSFNADSTSIPTTPLNDWLLWHEVGHNLA
EAPFNVEGATEVTNNLLALYMQELRLGNPKMDRVEQDIQKAPDFVSAENGHAWSAGGAGERLVMFAQLKE
WAETEFDIDDWYSEGELPSYYIYGEDQGWNLFKLMHRLARGDGQGDLGGNNCCSSSTGLSKGDLLMLCAS
YAAQYDLSDFFKAWNPGETAFILPDGSKQYEGGITSAGLSKVAALKLPKPKRSPLSINS
>gnl|CDD|411579 NF037975, pilot_rel_YacC, YacC family pilotin-like protein. Members of this, including YacC from Escherichia coli K-12, resemble the lipoprotein GspS of type II secretion systems (T2SS), but in general are not lipoproteins. In E. coli K-12, where the T2SS is cryptic (not expressed, but able to function after manipulation to force its express), YacC is encoded far from the locus where the main set of T2SS genes are found, and it is not clear that YacC is a true GspS
MKKFILALLLLSLLGFSSASKALTESEAEDLADLTAVFVYLKNDCGYQDLPNRQIRRAIVFFAQQNRWDL
SNYNSFDMKKLGEDSYRDLSGIALPNDKKCKSLARDSLSLLAYVK
>gnl|CDD|411580 NF037976, gtrA_1, GtrA family protein. The GtrA family proteins have 3-4 transmembrane domains. They are involved in translocation of lipid-linked glucose across the cytoplasmic membrane
LALRYAAFAAIATAANIGAQDLVLRLYSGPYALLLSVLAGTAAGLVVKYLLDKRWIFRDKARNAGHDARK
FALYTVMGVVTTLIFWGFEFGFWAIFGTDAMRYLGGVIGLAIGYIVKYHLDKRFVF
>gnl|CDD|411581 NF037977, Lpg0189_fam, Lpg0189 family type II secretion system effector
LVGSLVLLPLLAFSNPQDNKTELIFSPLPENKNTIVKTYSNESEGLNQLKSAQRTIDYPTQIVRMEGNLE
GQQLSCEQVHEEIDEIFVKKISPDKFTYNIYISCSYDPETNYATNFTINSYFDPLTDEAIDYLKSYLSEY
NGSDLLGTPLNIESAKGLIVSLNIAAGMKKNPNKPPFTEYRQDRSNFYFKSNYEMRNKLFADIYQNFYSN
DPDKILPFLDKWIFSHASSVYKAILKDSNYLELQPERIFLMENEEDIFVSDLKYYFAHLCMKNPNHRCL
>gnl|CDD|468297 NF037978, T2SS_GspB, type II secretion system assembly factor GspB. GspB (general secretory pathway B) occurs in type II secretion systems (T2SS) and is viewed as an accessory protein, a factor involved in the assembly process rather than integral to the completed T2SS apparatus
AEGRMYRIPGYLLVVYALLLIALGWFGHQQWRSPSEPIAPPAARPAPQPAAAPVAHAALVPLQQTSAATP
DAPVQAAPLKSALAAPTVDRGELPPLAYSAHVYTSDPEKRSIVLNGERYREGDSPLPGLVIEQIQQDMTI
FSFNGETFTLAALQDWPG
>gnl|CDD|468298 NF037979, Na_transp, sodium-dependent transporter
RKWTLYLIFLVAGYAVGIGTFWLFPQFWLQYGLTGLVVYLIFLAVLTYLAILEAESTKKSRYYIVELYTK
VARTPAMILVLLMFLVIFLGVISYYTANGGLLLSPILGTGTLGILIAKLLMILLAFLILTRAKEKTLDIM
AIGSVLFVIFVVVSAILFRSQVLSVAPQAAQYLSMAKSMIFSFHPITLKLVVDMALQAIYSLGLGFGFYL
VLGSFLPERFNAKKIIGIGILLQTLLSFLATFTVVYSLGPAHPGYLTAFVYGGEEEAISLFYSLPLILRD
VPGGPTLLYLLMLSLFLAGLTSILPLGEVGGQIISEVFQLGRNKALIYVLGISLVLGGIDSLPSIATMLL
KAVSVFIFFTAIVEAYPLISSEELSAINRGWVYVGIALLILLGLYALYYTLRAGGQYVKLGILLGLV
>gnl|CDD|468299 NF037980, T2SS_GspK, type II secretion system minor pseudopilin GspK
QRGVALITVLLIVALVAVLAAGMLERQQLQVRRTENQQAQQQARWYALGAEALARLLLRDDLRDDSDVDH
LGQPWAQPLPEFYPEGGQVSGRIEDLQGCFNLNALVGGGGPDAAAQAPYALRVFQRLLELLGLDAYEALA
DALADWLDADDQPRGPGGAAEDYGYESLSPPYLAANQLLADVSELRLVPGVTPALYARLRPYVCALPTTT
LAINVNTAPAEVLAALAALLSLSQARALLAARPAAGFRSVGDFLAQLALAGLALDASDKEQLGVRSRYFL
LRGEVRLGEARLRLRSLLYRDGVGKVTVVRR
>gnl|CDD|468300 NF037981, NCS2_1, purine/pyrimidine permease. Proteins of this family usually have 14 transmembrane domains. They belong to the NSC2 superfamily transporters. They are specific purine and/or pyrimidine permeases
MKLFLGGLQWMAFMIAASIAAPIAIADLFHLNPAETAGLVQRTIFVLGIAGLLQALFGHRLPINEGPAGL
WWGVFTIYAGLVGTLYSTNIETLQALQGAMLVSGVFFFLLSVTGLIDKLAVLFTPVVTFIYLLLLVLQLS
GSFIKGMMGIGYEGNEVDPLVFLLSLVVIILTFYFSRHKIKWIRQYSILLSLAGGWLLFALFGKAPAIAH
TGGSIISLPELFVFGPPVFDSGLIVTSFFITLLLIANMLASIRVMEEVLKKFGKIEVSERYRQAGFASGI
NQLLGGLFSAIGSVPISGAAGFVATTGIPSLKPFIIGSLLVVIISLFPPLMNIFASLPAPVGYAVTFVVF
SKMVGLAFGELDKEENKERARFVIGIALLAGVGAMFVPASALSGLPPVVASLLNNGLILGTLIAIAVEQ
>gnl|CDD|468301 NF037982, Nramp_1, Nramp family divalent metal transporter. Nramp (natural resistance-associated macrophage protein) family divalent metal transporters are widely conserved divalent metal transporters, which enables manganese import in bacteria and dietary iron uptake in mammals
GPGVIAAAAGVGSGEFILWPYIGSQFGYTLLWAALVGVLMQMFLNMEIERYTLATGETLFTGFRRLWKPW
GWFFWVQAELVNIWPGWATFSAAALTYLLGFGIPILWIAIATLVLIGLILTLAPVVYRALEKVIGVKVGL
LVVFVAVAVVAVIAAPDWGALGAGVLFPQLPDGDLFAVLLGAIAFAGAGGAQNMVQSNWLRDKGFGMGSH
VPRLTSRVTGETEAEPSTGYMFPTDEENLARWRGWWRVANFDQLIAFWLIGFINISMLSVLAAATFFGSG
SLANDVAFLDVEGQTLAALVGPWFGTLFWLGGAASGLSSALGIVDYVSRLAADVVKQGFLGGASRWSESR
IYLYLVWGLTMFGIVILLAGGDQPLVLLVISAVLLGFGMFAYSILLLLLNRRRL
>gnl|CDD|468302 NF037993, cyano_chori_ly, cyanobacterial-type chorismate lyase. This variant form of chorismate lyase is widespread in the cyanobacteria, including founding example sll1797 from Synechocystis sp. PCC6803. Previously, members of this family were named DUF98 domain-containing protein, as found by Pfam model PF01947. The product, 4-hydroxybenzoate, is next prenylated by slr0926, during plastoquinone biosynthesis
LWQGDETDVQQGLPHSQLSPAWQLLLLGDGSPTRHLQLLTGEPTEVDVIAMSPIGDDDDGAPSEIEELPG
PRLRRQVWLRTASGQRLAYATSWWNASHVDEYLQNRSLPIWASLTQLRTELYRDVDGIYLGDSPWLEEAF
GEPGPFWGRHYLFWHGGQPLTLIYEVFSPYLEKYLG
>gnl|CDD|468303 NF037994, DcuC_1, C4-dicarboxylate transporter DcuC. Proteins of this family usually have 11-12 transmembrane regions. They transport C4-dicarboxylates under anaerobic conditions, which plays an important role in anaerobic energy metabolism
LIKKYETQTVLLGAGLLLCLIALIPGYLLDAKKSTGFSWFDIFEAFKKSMSSRLAGLGLAIMASMGFAYY
MKHTGADRALVHLLTKPLKLIGSPYFLLPIAYLITQFINIAIPSAAGLAALLGATLIPVLVAAGVSPASA
AAVIAGTFGSDLSPGSSHNAFAAKMAGMDVADYFIHYQLPIAIAAIIVVAIVAFFVQRYFDKKDNFSVEA
QEIESEENTEKVPLLYAILPIVPLILVLVFSGLVLPKIKMGVPTAMLIGTIIAMIIERIRPRDITKEFSS
IQVFFDGMGKAYANVVGLIIAAEVFAAGLKAIGAIDALIEGLKNSGFGFIGVRIGGTIIPFLMAIITGSG
DAAFFAFNELVPPIAASLGVEPVNLGMPMQIAGALGRTMSPIAGAIIVCAGIAGVSPFELVKRT
>gnl|CDD|468304 NF037995, TRAP_S1, TRAP transporter substrate-binding protein DctP. Proteins of this family are members of the superfamily of Tripartite ATP-independent Periplasmic Transporter (TRAP-T). They transport hydrophobic substrates, usually lipoprotein
KIATLAPEGSPWMKELKKMAAEVEEITGGRVSFKFYPGGVLGGERDVIRKMRLGQLDGAALTSGGLAEVV
PDAGVLSLPFLFRNYAELDAVLDALGPELEKGFEKKGFVALGWSEVGFRYFFSKKPIRSPADLKGIKIWR
TMGDPIHIAAFKALGANPVPLPIGEVLTALQTGVVDGAENPPLGAVALQWYEVAKYMTDLPHAPVPGGLV
ISKKAWNKLPPEYQAILRKAAAEAGEELRALVREDNAEALAKMKKAGVTVIELTPEEKAEW
>gnl|CDD|468305 NF037996, B-4DMT, B-4DMT family transporter
MSAWLLRGLVMAAVHVVVRVLLGAAIVAWPTQGSLIRWLALAVVVLAALVWGGLDGRRDARANPDPDRRE
DLTMTWLKAGLVAGVVSGLVAWIIGLFYVDGLGVNGLFFELTTGAAFTALLVFVPAGIGVALGRFLVDR
>gnl|CDD|411591 NF037997, Na_Pi_symport, Na/Pi symporter. Proteins of this family belong to the Phosphate:Na+ Symporter (PNaS) superfamily
FALYIAIFLLGMTVLRSGLFNLSGHKLKTWLLKFTDTPLKGFLTGTVITAILQSSSAVMVLTVGLVSAGI
LTFRQSIGIILGTNIGTTFTTEFITFDIDRLIIPLLIIGALLLFLPRPALKSLGMSLFGLGAIFTAMRGF
ESLAGPLTSLPFVHSLLESTNESLLLALLIGTVLTAIIQSSSATTGITMSFLNEGILTLPAGIAIMLGAN
IGTCITALLASIGSGKEAKLTAYAHIWLNVLGVLLFLPFIHLLGEFVALLASSPDVQLAHASVLFNVISS
LLVLPFAGLFARFI
>gnl|CDD|468306 NF037998, RND_1, protein translocase SecDF, variant type. Members of this family are identified by TCDB as belonging to 2.A.6.4.4, a variant 12-TM type SecDF, as found in Spiroplasma, Mesoplasma, and Acholeplasma
KKIVRIFCLFIIICSLIIGIVFSSQSFSNNYKLGSRYSGGYQALVEVYDLNEENTDNGSPNGDAKKGAES
LENKLSPFSDNTIDIKTVGKNRLKVRAPKDAYQSNTLFKNAIQQNGGLYLLNSNYKDLLFDDTTMTKERT
GISDIFGGVKYTPSGVGQANSPFINFEIGNGSKYLSKLTSLSTSEGGAPATPLLTIITDIETFINNLREY
YNLAPDDDNIDAIETYFNGIIEPLRSVYNSSNDKVKAVLDDFFDGSYKSKGTGGTAVYISGSLLDTSAPD
VSIEQLKEVLETNDSFRFTNNTSKYVIDPNSKTEDFNGTKGKYIDPLKLYLSQNATPQLMKIDEVFKVLN
GLILSFNDKTTTSNFNQYLDEKIKNYILNNDTINGTKTGAGAGSNTNSNQLIVATSTETIARTIEALINQ
TTSGFTFKVNGISEFNPVVTLLMLIASIIFLLILAIAIMIYLLFAYRLLGLFAIIIALTSISLTLYSPTW
FGLAIGPESITAIFIAIGLVLESCSLLFEAFKKHLYKNKRSIEESFKIANKETIGIIVDALVVLLIPNLS
LFWIGSNSIKSFATILLVGVIISLVLVIIVARLMIWLTIKLQWFKKYPWLLPLDTDFANQGVAILNYKIS
RLENKIEKLTNKEKLSSKLLLKIKKINDKIDLLKKKEENKEAKKNAKLIEKVKAKIKKLEQKITKLKLNK
KKSNKIIKIRWKKKDWIFFLKDNTDVILAIESEIEIQVIEKIKVKRNENNIFNITKIIIIIGLILSIIGG
IVGFTFGPNYDSTFGKGTTYTVYGDNLEELSNNNFVVTDIIDFGSKDKANEIQELKDKIINEVSDPQAES
SLNDSKKLEETAGYVFSFFFNNDLVDAFYNGSVSKSNNYVISYGTDYNYESSSNASNVPWVSINVSNSTN
FGKFKALMKRIFSSIAGFTKEGNIGNTPSGGILGLRQTPFTAYGQILQIAISFAIILLALIVYILIRFKW
TYYVALALAIVFAPAITVSIVIIFRVPITFEILIAFVSIIGFAIASAIIILGKAKSLISSKNKKELENYF
KKEIEHRAQIKRLRRELNNELFALKVEYKEEIKKLKIKNPKPEKKELKKEFKEFKKQKKLDFKDLKKKIK
KEKKANKKEINRVSKENNFLKEVFNNTFKFGLKRCLLIGGIYAIFAIILAATLPSIVGFGITLLIGVVVA
MFVTLFLAVPLWVWLEKRRIRNKYGRKRFINSLKVSHEEQIVKGIND
>gnl|CDD|411593 NF037999, mutacin, lantibiotic mutacin. Mutacins are lantibiotics in the epidermin/gallidermin/nisin family, found in the biofilm-forming dental caries pathogen Streptococcus mutans. Named members of the family include mutacin I and mutacin 1140. This HMM separates the mutacins (MutA) from paralog MutA' encoded nearby, which lacks mutacin activity
MSNTQLLEVLGTETFDVQEDLFAFDTTDTTIVASNDDPDTRFKSWSLCTPGCAGTGSFNSYCC
>gnl|CDD|411594 NF038000, mutacin_prime, mutacin-like lanthipeptide. MutA', a paralog of the nisin-like lantibiotic mutacin precursor MutA, is a lanthipeptide of unknown function, encoded in Streptococcus mutans within the same region. It is not required for mutacin function
MLNTQLLELFGSDTFDVQEDLFDFNITDTAVIQSNDSPDTHSKVGSFSICPPRKTSASFNSYCC
>gnl|CDD|468307 NF038001, HYExAFE, HYExAFE family protein. This uncharacterized protein is named for its best conserved region, the motif HY[ED]xAFE, found near the N-terminus. It appears to limited in taxonomic range to members of the Planctomycetes
IRRNHYEAAFEAYLRERRIPYVAVDEARRALLADGSLKSFDFLVYPPGGPNLLVDVKGRRFPGGRAGRRR
WENWVTRDDLESLARWEELFGPGFRALFVFAYELAGPDVPDDFEDVFEFRGRRYAFRAVRLDDYRAHMRP
RSPRWQTVSLPAADFRRLARPLAE
>gnl|CDD|468308 NF038002, bifunc_CbiS, bifunctional adenosylcobinamide hydrolase/alpha-ribazole phosphatase CbiS
GLVVLEFGNPVRALSSAPLNGGPPKVRAVAFMQVPKDFDGDYMEDARSARVGYGLPEDSVVFLTAAEVPK
AFSVAEEGEVFAAATAGMTNASCVGNTLDRWGEGTINVAVVVDRPLDDWGLVDLLRTAVEAKCLAAVDLG
LRCNGRRAGGTVTDAVAVLAPEGDGESHFAGPATELGRRVSKLVYEAVRKGGSPDGYDLLRRLLGAGRGE
FLWLVKAALGKAPEPVAQGFEEELERLLKDPNVWALIYAALELDVMAARGTIPGLSPEEHEADSPRIVAD
ELLGAALADYIGGFKAVLNTYWLDRVKPGILPELPMFLDDVLSGLVAGVYLRL
>gnl|CDD|411597 NF038004, darobactin_RiPP, darobactin family peptide antibiotic. Darobactin, discovered in the genus Photorhabdus, is a peptide antibiotic, made from a ribosomally translated precursor, and modified by the radical SAM/SPASM peptide maturase DarE. Darobactin A is the founding member of a new class of antibiotic that appears to target BamA, a component of the outer membrane beta-barrel assembly machine. It is seven amino acids long, Trp1-Asn2-Trp3-Ser4-Lys5-Ser6-Phe7, with two crosslinks, one from Trp1 to Trp3, the other from Trp3 to Lys5. Homologs of the darobactin A precursor are encoded in various strains of Photorhabdus, Yersinia, and Vibrio
KEKLESLEESFKNNELSINDNEIENLKNSNSNPKITAWNWSKSFT
>gnl|CDD|411598 NF038005, rSAM_mat_DarE, darobactin maturation radical SAM/SPASM protein DarE. The radical SAM/SPASM protein DarE is a maturase for the ribosomally translated, post-translationally modified peptide natural product (RiPP) darobactin, including forms A, B, C, D, and E. The mature form is just seven amino acids long, with two cross-links, a Trp1-Trp3 linkage and a Trp3-Lys5 (or Arg5) linkage
MDGIIPVKNIDCIEISDINIQELKKLSKCEYKQLSAYLIGKIPAEKILDDDELEIYNEEITKSISAKPIK
ANKLVVVLKATRLCNLRCTYCHSWAEGPNQTVSFSTLVHIVRRILAIPNVNRFEFVWHGGEVTLLKPAFF
KKLIWLQQQFKRPEQYITNTMQSNAVNISDEWLTFIKGIGMNVGISLDGVPAINDKRRVDYRGRGTSERV
AKGIKKLRQYNIPYGALIVVDRDVYQTDMREMLDYFISIELTDIEFLNIVPDNRLVPGEDIGNSYISYAE
FIKFLSELFTIWWKGYREKIHIRVFEDFIRVLKNPSKKLSACYWSGNCSQEIITLEPNGDVSPCDKYVGD
KGSIYGSLLDTDLATLLANSSHNQQAINEEIEATEKMHHCEWFSICHGGCPHDRVINRRHTEGYNDTCCG
TGKLLATIQQYL
>gnl|CDD|439423 NF038006, NhaD_1, sodium:proton antiporter NhaD. Proteins of this family usually have 10-13 transmembrane regions. They extrudes Na+ or Li+ in exchange for H+. They have been identified and characterized in a number of bacterial species
MRKSKPVLVAAGLIWAMIGWVYVQAGLPDVAEAAFEHNLLEYAELLLFLLVAMTYINAMEERRLFDALRA
WMVEKGFSYRSLFWITGFLAFFISPIADNLTTALLMCAVVMKVAEGDKRFINLCCINIVIAANAGGAFSP
FGDITTLMVWQAGLVRFQEFMELFGPALVNYLVPAIVMSLFVPNRKPSAIEEHVELKRGARRIVLLFLLT
IATAVLCHAMLHLPPVLGMMMGLGYLQFFGYFLRKTLPRSLARKRAMASARGDWRKLKRLGSVVPFDVFT
RISRAEWDTLLFFYGVVMCVGGLGFLGYLGLVSETLYTGWNPVWANILLGLLSSVVDNIPVMFAVLSMQP
EMSMGNWLLITLTAGVGGSLLSIGSAAGVALMGQARGIYTFFSHLKWAPVIALGY
>gnl|CDD|411600 NF038007, ABC_ATP_DarD, darobactin export ABC transporter ATP-binding protein
MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVT
NLSYSQKIILRRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPM
QLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRI
INMKDGKL
>gnl|CDD|468309 NF038008, ABC_perm_DarB, darobactin export ABC transporter permease subunit
FLNDLKLSPLSSILAIIITAIGLVSLFLVLLLYLTDSRIEKHHSDYSDIYRIETQFNLPNGDKVKSAQVP
LPLISVLQNDKNIKRVGYAFRLFTNLQVNDKTISKVDIYAVSPEFFNTLNPYQQKIPALAQNEIYITPEF
NRQYLHLDNPKGKVITLGNKGQFIIKDVVELNKSSSFNTDAIIAFSPELIDGYHDKRHDWYDTHAYVFIT
MKSGIKPTSEQLNQIVTQYAPQLPGAPFTPEEFIQLSARNITDIHYDNALPDEISTVISKSYLYTLYGAG
IFVFLTTTMNFFNINNVINANKRNSFQIKKSIGASYYQLITESLFIATLQLLFVLLLSLFILISLIQFSD
GIKELILTQGSLIFLTAFSITLASTYIAILLSHFLFLLTFVFPNQSGHSISRSEQPLSRYITKLTLCIQI
LIAGIIIYLWAGVMTQLFFMQDADFGYDKENTITFKLNDELKSDVSINNLQDELNNEIGTSNIALSSWRP
FDMSRSNISVFHANQQEKDKLVTVNYLNANKNFINVWGLKTLAGNENPLLPSDNDNIVHAIVTKSFMTLM
GNISYDEVLNNLFYINLGDGQQEIRILRVVDDFYLGDRKEDFDPLLIFIKDDIQKYGALKLNNIQDIDAV
KKILERYGVNPEQIKLVSELHKEYFSNLSLIQKTINFVTLLSIVLILISTIIISLSETKRLSKTLKIMES
IGGSIYTNIIFFIQQNIIPILIASIIALPIGFLLLHRWLNQYDLVQFLSYVYATSALLIFILSIVIIMTL
TLIFSKK
>gnl|CDD|468310 NF038009, TatB_1, twin-arginine translocation system-associated protein. This family is suggested by TCDB to be part of the twin-arginine translocation (TAT) system, but lacks detectable sequence similarity to subunits such as TatB
AMKKELNTLLTKKMDRKDFLKHVGLGVVAVLGLSSLLKALTGKSAKAASNSTNNSPSGYGSSTYGGTKDS
>gnl|CDD|411603 NF038010, ABC_adapt_DarC, darobactin export ABC transporter periplasmic adaptor subunit
KIEKKSNINNRAKLIIFCVLLLFISCLYYIYYLSTTQRTLLISREDVTFHTVQPEVYQDVLITRAIAVPN
ESVIISSERGGKVTEIVKQAFDTVKKGDVIARLSNYDFMLEATSRIADITEQINNLRNMRMQLEQDNRDT
KLNLQEAQHQILIISKDLARHQVLDKKSMIAKSELENQVDMLKNWKIKSEILKEHNNKNKKSLPSQFKEI
DESILLLEKMMKMIENGMEQLVITAPIDGTLSVLDIELGQQIKPGEKIAVIDNLNSYYFNVYFSEYYLDK
IKPQSHITSQINGQDIPLLIESVSTIVENGKFKAKLIPLQESIIPLKRGQSIEIRIPLQEENNNVLLVPT
ESIFSDKNGNSFVYIYQPEKDHAIKTKVEIKRRNAMKTEITSGLKAGQQIVIPPDNNNNEYDIIEFK
>gnl|CDD|411604 NF038011, PelF, GT4 family glycosyltransferase PelF. Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter
DICLLLEGTFPYVRGGVSSWVNQMIRGFPELTFAVVFIGSRREDYGKRAYALPDNVVHLEEHYLYDAWAP
PQPRASRGDAAAFARVADLHDALRHPDAPAEAGALGRELLPMLADGGRLSEEDFLHSRASWDYITEQYRR
YCTDPSFVDYFWTVRIMHKPLWQLARIARNLPPARVYHTISTGYAGFLGALLHRRTGRPLLLSEHGIYTK
ERKIDLAQSQWIRDNRGLFERDDSEVSYFRELWIRFFEALGRLCYDAADPIVALYEGNRLRQIADGAPPE
RTRVIPNGIDLPRLAPLRAQRPAGIPPVVGLIGRVVPIKDIKTFIRAMRTVVRAMPEAEGWIVGPEEEDP
AYAAECRSLVASLGLQDKVKFLGFQKIDDLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQ
LIEGLDEEDRALGAAGEVVAIADPQALARAALDLLRDPQRWQAAQAAGLARVERYYTEELMFDRYRELY
>gnl|CDD|411605 NF038012, DMT_1, DMT family transporter. Proteins of this family belong to the drug/metabolite transporter (DMT) superfamily
AALLALCAALASAIGDVIRQRSAQEVTDEPVGHLELFRRLLRDRRWWLGSLAAVAGFGLQAAALGLGSVL
LVQALQVTALLFALPIYARLTHRRVTRREWMWAVLLAAAVAVVVTVGDPTAGHSRASLQTWIVVAVVLGP
ALVLCVIGARIWSGRPVAAVLLAVVSGSLWALFAVLTKGVVDVLGHGFAALLRAPELYAWVLVALAGMIF
QQSAFRAGALTASLPTMTVAEPVVASVLGVVVLGETLHAGGAGLVVLVAAVAVVVVATVALARGEA
>gnl|CDD|411606 NF038013, AceTr_1, acetate uptake transporter. Proteins of this family are acetate transporters, which usually have 6 transmembrane regions. The homologue in E. coli is YaaH
NPAPLGLLGFGMTTVLLNLHNAGFFPLSSMILAMGIFYGGLAQIIAGIMEFKKGNTFGATAFTSYGFFWL
SLVGIWLLPKMGLAEAADETSMGAYLLLWGIFTLFMFIGTLKHNRALQFVFGSLTILFFLLAIGDFTGNA
LITTIAGYEGIFCGASAIYLAMAQVLNEEYGRTVLP
>gnl|CDD|468311 NF038014, Chlamy_inclu_1, inclusion-associated protein. Proteins of this family are inclusion-associated proteins in Chlamydia. It has been shown that protein CPj0783, which is identical to the HMM seed protein WP_010892266, was localized on Chlamydial inclusion. CPj0783 interacted with host Huntingtin-protein14, which may play an important role in disturbing the vesicle transport system to escape host lysosomal or autophagosomal degradation
PYILFAIFIHGACIGLLFYSPPQKKQPKLKPFKEKLVTLPPEPKVTTTPTPSSKTITKPKTIQPSPQKKA
KKPPSEKKKPKKPPKPKEKPSPKPQKEKKPTTKKTEISQAQLKTLADLAKTLSDHLEKSESHLADISLPT
QRQLTINSSLEATQEEELCQLFREYVVLPFSGEVRLKLVLTPQGRIQECVFLSEISEADKQLLLMRIQKI
PFQKFLDKYKISKNISFHIKLLSNES
>gnl|CDD|468312 NF038015, AztD, zinc metallochaperone AztD. Proteins of this family are components of the AztABCD zinc-uptake system. AztC, AztB, and AztA are the extracellular solute-binding protein (SBP), permease, and ATP-binding protein, respectively. AztD is a zinc chaperone to AztC, and it may store zinc in the periplasm for transfer through the AztABCD transporter system
VADTYDGGVYVLDGETLEVLETFPLEGFNRLNPAGDGRHVFVVTSDGFRVLDHGDHAAADPALTDVEFTG
AKPGHVVRHAGKTVLFFDGTGEVTIFDPADLADGKPEVRTVTTAAPHHGVAVELGDGTLVTTLGDEDART
RPVGARVLDADGKEIARSEDCPGVHGEATAQGEAVAFGCEDGVLIYKDGAITKLDYPDPYGRIGNLAGSE
GSQVFLGDYKVDPDAELERPDRVVLIDTATGTLRLVDLPTRYTFRSLDRGPAGEAYVLGTDGALHVIDPV
TGEITKSIPVTEPWSEPGHWQDPRPRIAVAGDTAYVTDPAKSKVHAVDLETGEKTATITLEGKPNEIVGV
GG
>gnl|CDD|411609 NF038016, sporang_Gsm, sporangiospore maturation cell wall hydrolase GsmA. The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain
LNVRSGPATDSAVVGTLANGAKVTVVCKVRGEQIRGTVRTTSQWDRLGSGRYVSHAYVRWSPSLPTCPWC
APKAATVATVTTGGGALNVRAAAGTGAARVGTVANGATVTVECQVWGQEVDGTGVWYRLGDGRYVSAAYV
RRPWLPWCGQDPPTVPRGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGI
KCFGSPGPIAVGCRSYATFECSPTGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYAPAFAYTDDPDQF
AREIHKAGYATDPTYADKLIGLMKQYNLYQYD
>gnl|CDD|411610 NF038017, ABC_perm1, ABC transporter permease. Proteins of this family are the permease subunit of an ABC transporter complex, which may be involved in tungstate uptake
SLRVSGTATLIAALIGIPLGALLALRRFPGRRLVISLLNTLMGLPPVVVGLIVYLLLSRSGPLGFLGLLY
TPTAMIIAQAVLALPIVAGLTLAAVQGLDPELRLQILSLGATRWQALWTLLKEARFALLAAVLAGFGRAI
SEVGAVMMVGGNIRGYTRVLTTAIVLETSKGNFDLALALGIILL
>gnl|CDD|411611 NF038018, qmoC, quinone-interacting membrane-bound oxidoreductase complex subunit QmoC. Proteins of this family are the transmembrane subunit of the quinone-interacting membrane-bound oxidoreductase complex, which consists of the QmoA, QmoB, and QmoC proteins. It has been reported that the QmoABC complex is essential for efficiently delivering electron to adenosine 5'-phosphosulfate reductase AprAB, which is important in sulfate reduction in sulfate reducing prokaryotes (SRPs)
PDLQFIKELQAAGGDSLKKCYQCATCSVVCPLSPADAPFPRKEMVWAQWGLKDKLVGDPDIWLCHNCGDC
SDYCPRGAKPGDVLAALRNMAIQEYAPPKFLGKWVSSPKYLPILFAIPAVLFLIIWFITGGGGLFFPEAG
EIVFGKLFPGDYTIDPIFMPTFLFAVVIFWLGVSRFWKDLEPEGRTLVIKKKSFLGSLWDVIIEILTHRK
FKECGDDNKDRATGHLLVFYGFVGLAIVTAIVAVYHWGGVLPWISPYPLLNPVKILANISAIALIVGLAL
LTANRLNLDDQKGKSSYYDWYLLGVIWAVGATGMLAELFRLAGVATLAYLTYYLHLVFVFMLFAYLPWSK
LAHLVYRTVAMVY
>gnl|CDD|468313 NF038019, PE_process_PecA, PecA family PE domain-processing aspartic protease. PecA from Mycobacterium marinum, and by homology, three related paralogs from Mycobacterium tuberculosis (PE26, PE_PGRS35, and PE_PGRS16) are all PE domain-containing proteins secreted by a type VII secretion system (T7SS, also called ESX in Mycobacterium), and all share a C-terminal aspartic protease-like domain. PecA itself is now known to be a functional aspartic protease that cleaves within the PE domain of T7SS secretion substrates that have the domain, including itself. Members of this family typically contain a long, variable, low-complexity region. This HMM represents the aspartic protease region C-terminal to the low-complexity region
NVTVPLEVVNTTEPVVNVSVNGGPTVPVLVDTGSAGLVVPFWDVGLQNLGLPTGFGIVQYGGGLYYFYAT
YPTTVDFGNGIVTAPTSVDVVLLAFPTTLNSLGTWAFGDYLGPSGVVGVLGIGPNAGGPGPSIPTTALPG
DLNQGVLIDQPGGELQFGPNPLTPGTSVTGAPITTLNVQINGGPLQPVPSIIDSGGVYGTIPSSVLGVGP
TGGTLPAGTTISVYTSDGQTLLYQYTTTATNSPTVTSSGSMNTGNLPFAQQPIYISYSPSGVGTTIFN
>gnl|CDD|411613 NF038020, HeR, heliorhodopsin HeR. This HMM represents heliorhodopsins, a group of phylogenetically distinct microbial rhodopsins, which play an important role in absorbing and transferring light energy for numerous biological processes in bacteria. Heliorhodopsin was initially identified and characterized in a Gram-positive actinobacterium based on functional metagenomics and photochemical approaches. Heliorhodopsin have seven transmembrane domains, and exhibit similar biological function as microbial rhodopsins. However, heliorhodopsin form a distinct cluster based on phylogenetic analyses. Most microbial rhodopsins are hit by the Pfam HMM PF01036, which does not hit heliorhodopsins
LRRFNLVAGVLHLVQGVAMLVLSNDFTLPITTTYLTFGPPGTTLPPEPVTLFEVPLGLLVAAFLLLSALA
HFLIATPLFKRYVANLKKGMNPYRWYEYSLSSSVMIVLIAMLVGIWDIGALVAIFGLNASMILFGLLMEK
HNQPTEKTNWLPFIFGCIAGIVPWIVIFIYFIASGSSSDTEPPGFVYGIVISLFVFFNTFAINMVLQYKK
VGKWKDYLFGERVYIILSLVAKSALAWQVFAGTL
>gnl|CDD|411614 NF038021, mannan_LmeA, mannan chain length control protein LmeA
RKVLIGLVATVVALAVGAVGVDFGAAIYAEYRLSRSVRTAAHLDSDPFVAILGFPFIPQAMRHRYDEVEI
KASGVDHPVVGKASLEATLHSIDLSEASWLIRPDAPLPVGKLESRIIIDSTHLGRYMGIKDLLVEAPPRE
TNDATGGTTESGISSNHGLVFTGTPKAAGFDKRVSVAVDLSIAGPDQTTLVFTATGVLTGPGTADQAVPE
DKTAAVLAAFSGRLPGQKLPFGVAPTTEGARGSDVIIEGIAEGVTIDLDGFRQS
>gnl|CDD|468314 NF038022, PorACj_fam, PorACj family cell wall channel-forming small protein. Members of this unusual protein family are small (often 40 amino acids or shorter), variable, and detected so far only in the genus Corynebacterium. Despite its small size, the founding member reported to form into homooligomeric channels in the cell wall (not the plasma membrane). This family, as built, may also include PorA subunits of PorA/PorH heterooligomeric cell wall channels
TEILGQLADFFGGFKDIFKGLKDVFEVISGWA
>gnl|CDD|468315 NF038023, S_layer_PS2, S-layer protein PS2
MFNNRIRTAALAGAIAISTAASGVAIPAFAQETNPTFNITNGFNDADGSTIQPVPAVNHTEAELRDATDA
TGAYLADFQNGDVEAIVGAYIAASENGFDPSEEAAYEAFEAARQEATQQLAFSAETITKTRESVAYALKV
DQEATEAFLAYRNALRGAATSINPLIDAANAANRTDKSEIEDYDNLYLASDVFTDAPLLLPAYQELVALQ
AEVNEDLEWLGEFAIDNDDDNYVQRYHIPAVEALKAEIDARVEAIEPLRADSIAKNLLAQKSDVLVRQLF
LERATAQRDTLRVVEAIFSTAARYVELYESDENVNVEGDTLRNHYVALLPTLFGAAVFNISELNAADAAA
EDYYLVWDTDLATNDEDAAYAEEKRQFAILTYAKILINGIWQEEVKYVQNLDAGARAEAARREAERAADE
AYRAEQLRIAQEAADAQKAIAEALAKEAENGNNNGGDNSSDDKETGSSDIGSWGPFAAIAAIIAAIAAIF
PFLSGIVKF
>gnl|CDD|468316 NF038024, CRR6_slr1097, CRR6 family NdhI maturation factor. The protein Slr1097 and its functionally equivalent cyanobacterial homologs are required for proper maturation of NdhI, a subunit of NADPH dehydrogenase complexes, so that NDH-1 complexes can assemble properly. The related protein in the model plant species Arabidopsis thaliana is known as CRR6 (chlororespiratory reduction 6)
TLNADAINNLDLSPVQTVIEKLLKGAILSHEQQLQFEIDYPREPDDPRELSEIPEVRLWFIRLDARYPWL
PFLLDWKSGELARYAAMLVPHQFSRTEGIQYNPEALEIFVMHKIFVLDDWLKQQGIPSRSRLKSMAQMLG
YELDDEFFELL
>gnl|CDD|468317 NF038025, dapto_LiaX, daptomycin-sensing surface protein LiaX. LiaX (lipid-II-interacting antibiotics X), as described in Enterococcus faecalis, is expressed under control of the the LiaR response regulator, and is involved in the process of resistance to daptomycin and to antimicrobial peptides of the innate immune response
MNERERILDLVKKGVLSTEEALDLLENMAKEKDEKQIKKAADEVTAEKDDLLDELENEQEEEPETFTEQK
EEEDKEDLEAILDELATEANKASAELDEVNAEIQGVKEEIKEKQEQLMVLDTKEELDELSEEELAERQEL
EAEIKQLEAQLDELEEEKEELEEELKTIRKDQWSQTKEKISEKFDIPDDWKEQATETLNQVGEKVGEAGS
QLGKFLKKTFQTVSETVNDNVEWKDVNVKVPGVATTKFEHEFVYPASEATILDVKVANGNVVFKTWDEPD
VKVEAKIKLYGKMDAATPLEAFEERSQIEVDDEHISFQVPNKRVRADLVFYLPKRTYDHVAIKLLNGNVT
VEELDAKDVYTKSTNGNITFKSIDATMLEIEGVNGNITVRDGEILDSIIETVNGNVTITATPQNAGVSLV
NGDVKLTFKEDDLKKLEASSVNGNVKVALPTTLGLEGEAKTSLGSINSRLSNYEVIREKKERTNQLLQFR
RVADEQMAQIDLSTTTGNIYLKD
>gnl|CDD|411619 NF038026, RsaX20_sORF, putative metal homeostasis protein. Members of this family average just 38 amino acids in length, but are widely conserved among species of the Gram-positive genera that include Staphylococcus, Enterococcus, Leuconostoc, and Lactobacillus. Expression of an RNA designated RsaX20, which encodes a member of this family, was studied in a Staphylococcus aureus of possible structural RNAs, and shown to be controlled by Fur-like transcription factor Zur. The broad conservation of the coding region across multiple species and protein-like pattern of amino acid substitutions in multiple sequence alignments strongly suggests that that members of this family are indeed translated into functional proteins
KTDLASAYRRLKSPNIKTRKRALKIIKEHKRN
>gnl|CDD|468318 NF038027, TssQ_fam, TssQ family T6SS-associated lipoprotein. The founding member of this protein family, TssQ (BB0812) from Bordetella bronchiseptica, is a lipoprotein, and possibly all other family members are as well. TssQ is encoded within a T6SS locus but its function remains unknown
PASPAAEQALAEGRQAYDAGDYGAAIRRLGRSSELQTAPPATRVEALKLLAFSYCVSGRTKQCRDSFRRA
LALDPDFDLAPAEAGHPIWGPVFEKAKAAA
>gnl|CDD|468319 NF038028, spiralin_repeat, spiralin repeat. The spiralin repeat is a domain that appears once in spiralin (the major lipoprotein of Spiroplasma species) and up to six times in related proteins
DISDVTVPDIKVIADPDVTYDELNANNTIIKAVITAINKKLNITVTTKDFTITNDNDKEGNQSAGTVVEF
TVTAKDTSKLIKGSFTFT
>gnl|CDD|411622 NF038029, LP_plasma, lipoprotein signal peptide. This HMM describes one of several homology families that can be found of mutually closely related lipoprotein signal peptides in the Mycoplasmas and closely related genera (Mesoplasma, Spiroplasma), but absent outside that taxonomic group. Member proteins include spiralin, the most abundant lipoprotein in Spiroplasma
MKKLLSILGSITLIATTSTSVVAC
>gnl|CDD|468320 NF038030, spiralin_LP, spiralin lipoprotein. Spiralin is the major lipoprotein in multiple species of Spiroplasma, a relative of the Mycoplasmas
MKRLLAILGAFGLTATGATSVVACNNGKTESNDLSKVKTITAPATVAATKVIAVTKGEVKTALKANVLKA
VQKVVKTATATDFTYDVYKDNKGTALKTVNLEAGTVDVYVQITAAKDKTVVIGSSGYIKVTLPKEDQVAK
VDISGVTVPEQTVGITVTDPTDVTKNELSALNKDATLAGAVLTAIKAKAGVAQVATDFTITNNGAAGDYS
AAKTVEFTVKAKGDSTKISGEFKFTAKVK
>gnl|CDD|411624 NF038031, PavB_Nterm, PavB family adhesin N-terminal domain. This HMM describes the portion of PavB from Streptococcus pneumoniae, and closely related proteins from Streptococcus mitis and Streptococcus pseudopneumoniae, N-terminal to the repetitive region with variable numbers of SSURE (Streptococcal Surface REpeats) regions (see PF11966), which bind fibronectin. The PavB region is notable, in part, for its rare variant, WSIRR, of the YSIRK motif signal peptide. Full-length versions of proteins from this family have a C-terminal LPXTG-containing region for sortase-mediated anchoring to the cell wall
MKFNPNQRYTRWSIRRLSVGVASVVVASGFFVLVGQPSSVRADGVNPTPGQVLPEETSGTKEGDLSEKPG
DTVLTQAKPEGVTGNTNSLPTPTERTEVSEETSPSSLDTLFEKDEEAQENPELTDVLK
>gnl|CDD|468321 NF038032, CehA_McbA_metalo, CehA/McbA family metallohydrolase domain. This domain, a branch of the PHP superfamily, is found in several partially characterized metallohydrolases, including McbA and CehA. Both were studied as hydrolases of carbaryl, a xenobiotic compound that does not contain a phosphate group, suggesting that presuming members of this family to be phosphoesterases (like many PHP domain-containing proteins) may be incorrect
GWYSGDLHIHTNHSDGPTTPEELARAALAEGLDVIALTDHNTISGRAYFAELLASERGLLVIPGMEVTTF
WGHMNLLGLDLDPYIDWRNTDPGSPDIDEVIDEAHRQGGLVGIAHPFSPGGPLCTGCGWEALIDDLGKVD
AIEVWNTPDPAPTNERALALWYHLLNEGFRITATGGSDAHDDFDERPGLPRTYVYVDGELSYEAILAALK
AGRTYVTTGPLLELTVNGTAMPGDTLEAAAGGSVTVTAEVRAVAGLDRLELIVNGGVVATLEIAADGGAT
TVSFELPLDGSGWVRARVYGGAGGLLAHTNPIYVE
>gnl|CDD|411626 NF038033, FEA1_rel_lipo, FEA1-related lipoprotein
LIGMLLSLALLAAACGDDDGGTVRELGSSSSSSGSGSGSGSGSGSGSGSGSASSSGSASASASASASASA
SGSASASGSAPAGTAGPTSDATAADGGYAYASNVDSHRLVVADVCDINELLGADPIDFDAIAEIYNDGVN
SVKSDGSVRTIGGFASAEGKKHGVDAYYGTATPLDDFVTAALEGTGMFAGESDGVRKQGVQKGIQNQIMV
AWVVHELNAALDKAADGNFDAASGAPHNWDEAWAFYHGAEPGCGPYATADKRAGNFGTLGADGETALANE
AILAAMIAGRDALLAGDAAAAVAAAAEIVKNLVVTYSQATIRYAVKVESDLADGDMEAARVHQAEGLAFF
RVIEPLLAGAGADIAAINAIYDLSNEPGSGSGDEVRAALQPAWASLGITAADIGTL
>gnl|CDD|411627 NF038034, lactGbeta_entB, lactococcin G-beta/enterocin 1071B family bacteriocin. This HMM was built to improve on Pfam model PF11632, which in version PF11632.8 had a two-member seed. It includes 12 residues of leader peptide and GlyGly cleavage motif (see TIGR01847), and has a shorter but more broadly conserved core peptide region. Characterized member proteins include lactococcin G and enterocin 1071B
LTEEELSDISGGGKGGKWIGLIDPAYDFVKGVAKGFKK
>gnl|CDD|411628 NF038035, lactGalph_entA, lactococcin G-alpha/enterocin 1071A family bacteriocin
LTEKELKTINGGGVFSKIGNVVGKALYWLCKGLG
>gnl|CDD|411629 NF038036, TCP11_Legionella, TCP11-related protein
ENSGRNRQEEILQAARVIQFWWKQVHLKQTAKESSRYINHIVSLQKAQDKSFSKLEEFILDPNTQTITHK
LLMHLEQAKDLIIPDREHLPDVQRPERIFLSAYLIATKSDHIFESPTEIDERLLTQAGEMLVSFEKLCKF
MSETYMPDPPARVDSPLARETPSSDQVFASMEHYQLSQSQERMRKDHRFMAEGRPYLEAFHKAQMAYYET
FVEWESHNRTRLAKICIAQYLRIEIKRFATLNNPDPRQLELYEGFGQQQETLRKKINELLGEEGIEMLEE
ELQALREALEANKWTSAPNEVLVHEMALNPHFTLPEEDFLIHPQNDIDAAIGALESENLEPILAVLEEIR
DRIAFLTPHNQQRIRNLWEEFSREGITAQIESLGLEVGLYKVINALIEKIKELESPAHAPETTAFQNELD
FKLSLGEDRNLLLKESIDFIYKKFSEINRELGNFYINQARTLVAHNIVEFEQQKFYERLQKGQFNLANVL
AWIDQIVVSPTNFRLNTAALCSQYIASHVAHAICLGLLQKPGNFELAALPETFYLDRKRLINWHEQYQQI
FYTAAAMGYLDVFCQQYGVKLSPEELIEQKNALIMTLKEEQLTDPKAIAAHVLTTLMALLAKHGKILSPR
EERLLTKIMENICTGNHRIAEIIHKRLGDQLSMYFSKGRLPEQSQGQGKLYGLREELAELGKEILPLLRL
HLKVHEKFYRRSIETRLWEPLFATLREPTPPSEIPSLLSIQQESIEATHAYIHKMAFLLSGLALIQQTVA
FADMWNLNIGIKNSTLKSLAESFGLIEMVSDPSISKDHMENKLLELMKHVAAEHEISYEEDDERKMARML
RLAKNAQSPGCKVFLDELTTVYRQFIAKGELPKINPNLLTAEFPEEIKKMCQQVKKIMDDVKEAHLPEDV
DPVAQTIPTLRSGKTLG
>gnl|CDD|411630 NF038037, cytob_DsrM, sulfate reduction electron transfer complex DsrMKJOP subunit DsrM. Proteins of this family are the DsrM subunit of the DsrMKJOP complex, which is a membrane-bound redox complex involved in sulfate reduction in Sulfate-reducing organisms (SROs). The dsrM gene encodes a cytochrome b reductase, which usually has six transmembrane helices and five conserved histidines
VIALVLIAYLGVGAAGLQYLFGVVIPYAAVAVFLVGFVYRVVDWARSPVPFRIPTTCGQQKSLPWIKQNK
IDNPSTTAGVVGRMALEVLLFRSLFRNTKAELKEGPKLVYGSEKWLWLGALAFHYSFLVILLRHLRFFTE
PVPFFVQLLESLDGFLQIGLPALYLTDIVLLAAVTYLFLRRVVIPQVRYISLPADYFPLFLILGIAITGI
LMRYFTKVDIVAVKELTMGLVTFHPVIPEGIGALFYIHLFLVSVLLAYFPFSKLMHMGGVFLSPTRNLAN
NSRAVRHVNPWNYPVKVHTYEEYEDEFREKMIEAGLPVEK
>gnl|CDD|468322 NF038038, cytoc_DsrJ, sulfate reduction electron transfer complex DsrMKJOP subunit DsrJ. Proteins of this family are the DsrJ subunit of the DsrMKJOP complex, which is a membrane-bound redox complex involved in sulfate reduction in Sulfate-reducing organisms (SROs). The dsrJ gene encodes a triheme periplasmic cytochrome c subunit, which contains three conserved heme c-binding sites (CXXCH) at the C terminal
MYDGGKIIAGLVIFVALVTFPFWYNLGKAAYAPEPELQPKDEKQCVEPTEYMRANHMQLLNEWRDEVVRD
GKRVYVNSDGKEYEMSLQNTCMKCHSNKEKFCDKCHNYASVSPYCWDCH
>gnl|CDD|411632 NF038039, WGxxGxxG-CTERM, WGxxGxxG-CTERM domain. This domain, a possible protein-sorting signal, begins with the motif that usually takes the form DWGW, followed by a hydrophobic (and probably membrane-spanning) stretch xGxxGxxGxxG (where x is hydrophobic), and then a short patch of mostly basic residues at the C-terminus. This domain has a broad taxonomic range that includes Firmicutes, Cyanobacteria, and Deinococcus. Members from the Firmicutes tend to occur together with a DUF3231 (PF11553) family protein
DWGWLGLLGLLGLAGLRRR
>gnl|CDD|411633 NF038040, phero_PhrK_fam, PhrK family phosphatase-inhibitory pheromone
MKKLVLCVSLLAVVLGGAALSQSSTDSPSSIQVAELPVGG
>gnl|CDD|468323 NF038041, fim_Mfa1_fam, Mfa1 family fimbria major subunit
KLKKFLLAGLAALALGLASCSNDDDPPGGQENPEGGDAYMSLSISLPGSTAGTRAANDGEDDYGTVGGES
KIKTVDVYLFDADGVLETVTFGTFTETTSGGGTTGTVLTPKTAIKTTPGTKKVYVVVNPPTDILLALTAA
TAFNAAYSAIALAATTIADLATDNGFVMTNAGKATTITVAPGVTEEEAKEATANRVTVTVERVVAKVLVT
TKGATFVVKDTDNPGGGTITDVKYALANGNKKFYLFRKVATIKTPNYDYVPSTSAIDDGNDYKTDPDYAT
TAFNYYDYTDLLNDGGDAVPADGNAATTATATLKGKYCLENTMKAGTSNQKKGNTTYVLVRAKFTPKKIY
TAIAENGLTAGGTFYVGDGKYYTSKAAAEAYYDPTDGGLAGQKVRTYTNGKCYYYAWINHDDNTKMGVGN
YGVVRNNIYHLTITSIKGLGTPWNPLPKPDPIDPEDPIDPEETYLSVDITVLPWTVHSYDVDL
>gnl|CDD|468324 NF038042, actinodefensin, actinodefensin. The actinodefensin family is named (here) as an Actinomyces-specific branch of the (otherwise eukaryotic) arthropod defensin family described by Pfam model PF01097
MDKFIRRTTSLADADFTQALRSETHAPLEGAEGFGCPPNEEYKCNRHCRSIGGYRGGYCGGTFNLTCKCY
>gnl|CDD|411636 NF038043, act_def_assoc_A, actinodefensin-associated protein A. Actinodefensin (see family NF038042) is a bacterial branch of the arthropod defensin family. Members of that family occur in the Actinomyes lineage, have a distinctive N-terminal region that may reflect how processing and transport occur, and are found in a conserved gene neighborhood. Actinodefensin-associated protein A is found exclusively in these conserved gene neighborhoods
SLHDSPWAEAAQLLINSEGSWEQVDEKTLADKHASASLRFVLARIADVRPPFGQSVFTGVLHRTPGTRLV
GDSIQPYAQEQYDLGPRSLESAEEVLAQALRRHGASDASSSSTPVDDIILRYLSELTAPTTDPVSPPSET
EAADIDARGIRDLIGAIPSEAKKQQAGRGFLQRLLGRKDKSDSHEHEHASEASEGPIIVEPAPQWLSIDA
IQMIDVARIVSLTSWEEALRGLPPRVSQLLWTASNDPATSSDAPYRPAHDPQVIAAFAQVPYEQRSTEVR
NGIRTHDAALCRRYGRDPVDDHAAARLRAVREAAEMWPSWQEELADGSLAARGCIDVDGMTLIGQDPFLR
QKYALDVKKTVETERWVTSWLSAGGSLTE
>gnl|CDD|411637 NF038044, act_def_assoc_B, actinodefensin-associated protein B. Members of this family are small proteins, averaging about 70 amino acids in length, restricted to the Actinomycetes. Member proteins typically occur in the vicinity of actinodefensin, which represents and Actinomycetes-restricted branch of the arthropod defensin family. The function of this protein is unknown
WRLAPGVTLTRLPFGGAVLVDLRTLAVAELDEEAAALLDRLLAGGAPPPLREFAADLLASGWL
>gnl|CDD|468325 NF038045, GEF_RalF, T4SS guanine nucleotide exchange effector RalF
EIEKAQREIIELFNSKPKNGIQKIKDICGEHNIDVAEQIAEFFHEQKQNLDLEAVGDYLSGPDAENQKVL
QAFTSQINFRGQSFTEGLRTFLKSFKLPGEAQKIDRLVQSFGEAYYQQNYPGVIADKDAAYILAFQTIML
NTDLHNPSIAPKDKMTLEQLKNNLKGTNNGKDFDDAFLKKIYDEIKAKPFEFNFVKTSPGYELNSSTLDN
DPTFKKLDSLLQSSNSNIQNVFPGISDNVKATVDKPKSWLSIFTGYEGTITLTDEKTKALATIQVYKPSI
FSKWLFGEQPKVIIQPLGQDGEQPKASIDLAAKIAASFETPVTSFKATYDYEKDDLIKAYD
>gnl|CDD|468326 NF038047, not_Tcp10, AAWKG family protein. Members of this family are found primarily in Streptomyces. The family is notable in part because a region outside of the N-terminal region modeled here contains 9-residue repeats that resemble the 18-residue repeats found by PF07202 in the C-terminal region of eukaryotic T-complex protein 10. The family is uncharacterized. This model was constructed, and named for family's most prominent motif, AAWKG, to head off any possible confusion with Tcp10
NWEHIIKQLTGFTGGTREDVGKVGGTDDAKGDSGIPWLRAKIKKKIKAKLTEDDTPLSGGPDPDGMGRVI
KFYDGGGEGSDVVKGYEVTLYVPWSSSGGNDFGDNGKAGAWDWGYGEALHLLMTDYSTAGFDSPYPSGGS
VDEKDAVDLATFTTTAKSFDRVGDFFTDHSETLEQWVKSLGGDDAAWKGSAADVFRDLIDGLHTGYKDFA
SELTPPGFSPSHTSVSDGYTSSSLHGDSIIRAENALHDAATKLYEAWNTWYAKNATPVAATKPDGQQTSD
WDPTAHLDKMLDKVATWLNENNIQKVRLTIDGQGTPGKGKSHKGEGFSIYYPVTSGYGDLTDASTWKALA
NEAVKRWTANIETNLDTPARTAVSTLNNAFADVLNPGWNFTFAFGDSD
>gnl|CDD|411640 NF038048, DIP1984_fam, DIP1984 family protein. Members of this family, including the Corynebacterium diphtheriae protein DIP1984, which has a solved crystal structure, are uncharacterized with respect to function. Some members of this family previously have been annotated, incorrectly, as septolysin. This model was constructed to overrule and correct such errors. Note that septolysin O, and other members of the family of cholesterol-dependent cytolysins such as listeriolysin O (WP_003722731.1), are unrelated
KLAEALILRADLQKRIEQLKSRLLNNAKVQEGEEPAEDPNELLKELEELLDELEELIIRINRTNSATKLG
DGRTLTEALAERDALKLRHSILRDIADAASEKQDRYSRSEIKFVSTVDVKELQKQADELAKELRELDTKI
QEANWQTDL
>gnl|CDD|411641 NF038049, SelD_rel_HyperS, SelD-related putative sulfur metabolism protein
ERFRERLEKYRSLGLNPLSLATGCAVKVDLIDVVYPALEKLRDELEKLNIEIAPREDADIFPGREEAELK
RLILGLGPELDPNLGEFDPDRAVVLIQVYQETAGSPEKFAKFVLRLYTSLGKTRRRLTIGKGHSIVTTKP
KAEFAVLDLIKLDGGKNSYTLANNDTIQIIDPTEDPGSYRQVAVAISNSLNDLFTKGAYRDLKIAPVYDA
PTEELKEKLEKNYESFASRYGAELVDDPQPKTGYLLMGATVIGKSDREPPTFYDKVDEGMEIIVTRPFGE
LAPINTYLWSLADEELLDELESRGISLEDLEEAKEKALEIMSKPNIEVAKVIYKYLPELGEDFDPEEHIA
ATTDVTGPGIFVIKELAEKANVDIELYDVPLIDPEISEFATENFIIPNATAGTNGAIVIFASKKVIDDIV
DELSKPGLEPMVIGEVIGKGEGRVIVPKEVTKYIHRKNLLKKFKL
>gnl|CDD|411642 NF038050, NrtS, nitrate/nitrite transporter NrtS. NrtS family proteins were first identified and characterized in Synechococcus sp. PCC 7002. The homologous proteins NrtS1 and NrtS2 are encoded by two neighboring genes on Synechococcus sp. PCC 7002 genome. The heteromeric transporter was shown to transport nitrite as well as nitrate. This HMM hits both NrtS1 and NrtS2 proteins, which have extremely high sequence identity and conserved motifs
TALRVALVVGTILFTINHGSALLQGKMTRTRWISALLTYLVPYCVNIHGQYISRRR
>gnl|CDD|411643 NF038051, MamC, magnetosome protein MamC. Magnetosomes are membrane-enclosed organelles containing crystals of magnetite (Fe3O4) that cause magnetotactic bacteria to orient in magnetic fields. MamC interacts with the magnetite surface and affect the size and shape of the growing crystal
LAPYLAQSAPGVGVLGAIVGGAAAAAKNIKLLKDGLVSTKEAVIDTGKEAAGAGVATAVSAVAVGAVGGG
LVVSLGTALVAAVAGKYAWDRGMDYVE
>gnl|CDD|468327 NF038052, histone_lik_HC2, histone H1-like DNA-binding protein Hc2. This model describes highly repetitive, Lys and Arg-rich histone H1-like protein Hc2, as found in the genus Chlamydia
MLGVQKKRSTRKTAARKTVVRKPAAKKTAAKKAPVRKVAAKKTVARKTVAKKTVAARKPVAKKATAKKAP
VRKVAAKKTVARKTVAKKTVAARKPVAKKATAKKAPVRKVAAKKTVARKTVAKKTVAALKPAAKRVASTK
KSSVAVKAGVCMKKHKHTAACGRVAASGVKVCASAAKRKTNPNRSRTAHSWRQQLMKLVAR
>gnl|CDD|468328 NF038053, hist_H1_lk_Burk, histone H1-like DNA-binding protein. This model describes histone H1-like repetitive basic proteins as found in Burkholderia and related species. It excludes the Hc2 family found in Chlamydia and involved in DNA condensation for the formation of elementary bodies
MATAKKKPAAKKAAAKKAAKKAAAPAKKAAAKKVAVKKVAAKKAAAAKKAAAKKVAAKKVAAKKAAAKKV
AAKKAPAKKKAAKKVAAKKAAAAKKAAAKKAAAKKAAAKKAAAKKAPAKKAAAKKAAAKKKAAAKKAAAK
PAAKAAAKKAAAKKAAAAPAAAPAAAVAPAAPAAKTALNPAAAWPFPTGSRP
>gnl|CDD|411646 NF038054, T3SS_SctI, type III secretion system inner rod subunit SctI. This model describes protein SctI (Secretion and Cellular Translocation I), an inner rod protein in the basal body of the type III secretion system (T3SS) as found in many pathogenic bacteria. SctI has some sequence similarity to the needle filament protein SctF. Lineage-specific names for SctI in various bacteria include BsaK, PrgJ, and MxiI
DVSLEDRLISAFANYAVTSSQEKAAINEKLNSPDLVSNPEKLLQLQNRLGNYSLYVSLISTLARKGVSAI
ETLLKS
>gnl|CDD|411647 NF038055, T3SS_SctB_pilot, type III secretion system translocon subunit SctB. One SctB and four SctE subunits, located at the tip of the type III secretion system (T3SS) injectosome, combine to form the translocon (translocator pore) in the membrane of targeted cells. Species-specific names for this highly variable component of T3SS include YopD, EspB, IpaC, SipC, etc
LDSDNGIGGAALLGLGELGATSQVEKSAETKIEAASLQGVSESSVSDPGLPQLDGPPAPSLGLQASRVEK
LLGALDSSDAISDSLALMSLLYQVAKLSREQQLQQRDIEVKANISSQKSQADEMRNAAKAMIAMAVVSGV
MAGATAIIGGFGSFKAGKKIKQEMSLNAAIAGQNAGFDQKSQLLKKTGLSPEDQAQVGKVWESGEADLAA
DQNALTSGGRKFDKMTSVNQAANAVLQSLGQMANAAVQVEQGESQARSKEDEVNATIAQAEKQKADENMS
FNENLIKELLQLMRSIAQSQNQAWRAAAGVV
>gnl|CDD|468329 NF038058, adhes_P110_Nter, P110/LppT family adhesin N-terminal domain. Members of this family include the multifunctional adhesin P110 (as the name is used in Mycoplasma hyopneumoniae, not Mycoplasma genitalium) and homologs presumed also to be adhesins. Homologs include LppT (lipoprotein T), which despite its name seems to lack the signal peptide region Cys residue required for conversion into a lipoprotein, and paralogs MHP683 and MHP684 from Mycoplasma hyopneumoniae
KLKKKKWIIIIGLSLTAIISAIVGVPVGLSSYNKSYYSKLNGNVEKPKALSLSSNSNFSNEEFDKLVDNL
KLKDNFKKLSAKTALNLAKDKLYSFDLLDAFDFSPLSKKYPNLSFDLTPSDKENAKVEGNSIKNVVVFAH
DKKTNITYSKKTDLKGFSTKSTSDGNLVNFSIDQSKSSISLSLESKKNLLASEFAIKLQDSF
>gnl|CDD|411649 NF038065, Pr6Pr, Pr6Pr family membrane protein. This family is defined by TCDB as prokaryotic 6 TMS (Pr6Pr) family membrane protein(http://www.tcdb.org/search/result.php?tc=9.b.302). The function of this family proteins is not understood
FFSYFTIQSNMLGAVVLTAAGVAPLRRRGRWFLRAAVRAAVLSYVVVVGVVYHFLLAPTWNPQGYYLEGP
WLLHYVIPALALLDWTLFAPRGRLTWRAVGWWLLFPVAYCAWTLVRGALVGWYPYPFLDVGQVGLGFVLI
NWAALLVGVLAVSAIIVALDRV
>gnl|CDD|468330 NF038066, MptB, polyprenol phosphomannose-dependent alpha 1,6 mannosyltransferase MptB. Proteins of this family are Involved in the initiation of core alpha-(1,6) mannan biosynthesis of lipomannan (LM-A) and multi-mannosylated polymer (LM-B), extending triacylatedphosphatidyl-myo-inositol dimannoside (Ac1PIM2) and mannosylated glycolipid, 1,2-di-O-C16/C18:1-(alpha-D-mannopyranosyl)-(1-_4)-(alpha-D-glucopyranosyluronic acid)-(1-_3)-glycerol (Man1GlcAGroAc2), respectively
LPRLGTAGSRSALLHEDLLAPAGDTRFDVSPVRPAGTSARRLSYAELRRFAVLRWLGTVGALLIGFGALG
AGALPVVGNPYDSFPGGSLMSRMLQTSSALVLIGVGLLVLAWVLMAPFVGASLRRSGTPRALVSTSMLRR
TFAAWVLPILLTAPLFTQDIYSYLAQGSIVAQGLDPYSAGPVDLLGAENHLARSVPFIWAHSPSPYGPVA
LGIAAAISRITNDSIVLGVLAHRLLSLLGVAAAGWAITRLARRCRVSPQAALWLGILNPLTILHLIGGIH
NESILLGLMLVGLELGLRGVDRLRAGRRGPAWGLLALSGALISCAGMVKVTGFIGLGFVGMALARHLHLR
RGRSPWRAIAVAAAVQVAVLVATIAAVTLLTGIGLGWITGQGGAATIRSWMSITTDIGVISGFLGMLLGL
GDHTEAILTVTRAAGVLVAAAFMVRMLFATYRGTIHPVGGLGVATFVLVILFPVVHPWYMLWAILPLAAW
ANRLFFRIAVVAYSAAMSFFVLPRGLALPPGTVLSIYLGAALSFAVLLGLGWWLLRRRGIRGLH
>gnl|CDD|411651 NF038067, OMP_CarO, ornithine uptake porin CarO. The outer membrane porin CarO (carbapenem resistance-associated outer membrane protein), found in Acinetobacter, is of clinical interest because of its role in allowing entry of carbapenem antibiotics and its variability from strain to strain. CarO should not be confused with Omp33-36, an essentially unrelated outer membrane protein that is similar in size and that also affects carbapenem susceptibility
MKVLRVILAASALTAIAGSAMADEAVVTDSYAFDFSQLIPVGVRAEVGTTGYGGAILWTANPYVGLALGY
NGGDISWSDDLSVNGTKYDLDMDNNLTYLNAEIRPWGASQNNWAQGLYVAAGVAYLDNDYDLDKRVGAGR
TFSVNGNDYNAGAGGGRINGKMSYKNDIAPYVGFGFAPKINKNWGVFGEVGAYYTGNPTVNLTSVGLAAV
VNGGGASLQDAVAAEERKIRNDDKYEWLPVAKVGVSFRW
>gnl|CDD|411652 NF038068, LaoB_over_CadC, L-arginine responsive protein LaoB. LaoB (L-arginine responsive overlapping gene) is a small, rare protein, encoded in an antisense frame to the gene for CadC in some strains of Escherichia coli. CadC, in response to acid stress and the presence of sufficient lysine, activates expression of a lysine decarboxlation and lysine/cadaverine antiport system, which provides resistance to the acidity
MLRLWEGEAVAGIASGIEGGEDNIISSPSSALYQITGTINL
>gnl|CDD|411653 NF038070, LmbU_fam_TF, LmbU family transcriptional regulator. LmbU is a well-described member of a family of DNA-binding transcriptional activators for natural product biosynthesis in Streptomyces and related species. Besides LmbU (lincomycin), some other members include CouE (coumermycin A1), CloE (clorobiocin), and HrmB (hormaomycin)
RVGLRLPPGLSLDEWERLGRQLFRISDSSAWWLGDWLIYGQERYPDRYRRAIKATGLDYQTLRNYAWVAR
RFPLSRRREALSFQHHAEVASLSPEEQDYWLRRAEREGWSRNELRRAVRASRRGDEAARRRAQEVLLQLE
LPAERLERWRKAAEASGLPLEEWVTAVLDRA
>gnl|CDD|468331 NF038071, lat_flg_LafA_2, lateral flagellin LafA
MGLSIHTNYASLVTQNQLNSTNKMLGTAMQRLGTGLRINSAADDAAGLQMATRLQAQSNGQKVGMRNAQD
AISMMQTAEGAMDEMTNITQRMKDLATQSANGTASAADRAAMDAEFKELSAELDNIMDNTTFGGQKLLKD
GGKFEAAVTFQIGGSSAEKLDVDASANVQKVNAEVVGTEKDVTAGIGTQAKAASAAITKLDTLLGDIGAV
RSQFGANINRLEHTVNNLSNMKENTDMAKGRIMDADFAAESTNMTKNQMLMQAGMSVLSNSNQMTGMVTS
LLR
>gnl|CDD|411655 NF038072, IcmL_DotI_only, type IVB secretion system apparatus protein IcmL/DotI
ALTLVLLRNQFYRDNYRRVSIILLAALVINVVLLAALVYLLTTRPEPKYFATTTNGRIIPLHPLDMPVMN
DSAVLQWAADAVRAAFTLDFENYRTQLQEASKYFTPDGWESFLNALQSSGALDSVKDNKLVSSAVVTGAP
IVLQKEVVHGVYSWRVQMPLLVTYQSASEVTGQNNIVTVLITRMPTYDAPKGIAINQFIA
>gnl|CDD|468332 NF038073, rSAM_STM4011, STM4011 family radical SAM protein. Members of this family are putative radical SAM proteins that (at the time of HMM construction) fall outside the scope of Pfam model PF04055 available at the time (version 21), as many radical SAM proteins do. The function is unknown. Members are somewhat variable in architecture, and found mostly in Streptomyces and related species. However, the family is named for a member in Salmonella enterica, in the model strain LT2, protein STM4011, whose function is unknown
LTILYRGPLSSCNYDCPYCPFAKRKDSAETLAKDRAALERFVDWVAAQTGDRLSILFTPWGEALIRRWYR
EALVRLSHLPHVERVAIQTNLSCRLDWLEDADPDKLALWATYHPGQTTVERFLAQCLELDAAGIRFSVGV
VGLPEHLDAIRRLRAALPPDVYLWVNAYKDEGHYYTDEEIAFFTEIDPLFEYNRRPHPSLGLPCRTGESV
LSVDGDGTVRRCHFVRVPIGNLYDGSFEAALRPRPCPRKVCDCHIGYVHLEDLPLYDVFGGGLLERIP
>gnl|CDD|468333 NF038074, fam_STM4014, STM4014 family protein. Members of this family are proteins of unknown function, regularly found in a conserved gene neighborhood that also includes two uncharacterized radical SAM proteins. The protein family is named for a founding member from the Salmonella enterica model strain LT2, although the system is rare in the Proteobacteria and relativly common in Streptomyces and related taxa
FVVVGNPGNRRVTLFQQAARAAGLPPARVVPWADLLRGGGLPFDPGALVRIDSPGEDFEVDRLLRGLPED
PGRIEGPAQWYRGFLRALARLRRIAAALGARLLNDPADIAVLFDKRRCHARLAAAGVPVPPSLTSGPPVR
GYDELRALMREAGMRRVFVKPAHGSSASGVLAYRTNPRGRERAYTSVELVEGGGRLYNSLRVRRYTDEAE
IAAIVDALAPDGLHVERWLPKASLGGRAYDLRVVVVAGEATHAVVRTSRSPITNLHLGNARGDLDALRLA
VGAAGWIWALETCERAAACFPGTLCAGVDLLLEPGWRRPYVIEVNAFGDLLPGLTGEGLDTYEAQIRAML
>gnl|CDD|468334 NF038075, fam_STM4013, STM4013/SEN3800 family hydrolase. Members of this family are sulfatase-like metal-dependent hydrolases, of unknown function, regularly found in a conserved gene neighborhood that also includes two uncharacterized radical SAM proteins. See PF00884 for information on related proteins
MNEIVGSHDILFITLDTLRYDVAQEELAAGRTPNLARYLPGGGWEKRHTPGSFTYAAHHAFFAGFLPTPA
TPGPHPRLFAAKFPGSETTGPKTFVFDAPDIVSGLAAAGYRTVCIGGVGFFNKRTPLGSVLPGLFQESYW
SPEFGVTDPDSTENQVDLALKILAALPPDQRLFLFLNVSAIHQPNYFYLPGAKGDSVESHAAALRYVDGH
LGRLFDALRKRRPTFVIVCSDHGTAYGEDGYTGHRLGHPVVWTVPYAHFFL
>gnl|CDD|468335 NF038076, fam_STM4015, STM4015 family protein. Members of this family are proteins of unknown function, regularly found in a conserved gene neighborhood that also includes two uncharacterized radical SAM proteins. The protein family is named for a founding member from the Salmonella enterica model strain LT2, although the system is rare in the Proteobacteria and relativly common in Streptomyces and related taxa
VAWRLRVDYDDGEEGFAELFERFLATVDTARVRALVIGDWGEAYESSSDPIVDLLVEAADRFPALRALFI
GDMTYEECEISWIEQGDLTPLLAAFPRLEELTVRGGTGLRLGPVRHESLRSLTIESGGLPAEVVREVAAS
DLPALEHLELWLGVEDYGGDATVADLAPLLSGERFPALRHLGLRNSEIQDEIAAAVAEAPVVARLEVLDL
SLGTLTDEGAEALLAGQPLTHLKRLDLHHHYLSEEMMERLRAALPPVGVEVDLSEDDEEDEDDEDDEVYR
YVAVSE
>gnl|CDD|411660 NF038077, MFS_export_MxcK, myxochelin export MFS transporter MxcK
SASFPPRQERLLLWLLAAVQFTHLLDFMIVMPLGPELMRRFSLSAAQFGALVSAYTLASAAMGVLGVFWL
DRFDRKRTLLALYAGFITATLACGAAQSHTALLVARTLAGGCAGLMGAVVMAIIADTVPGERRGQAIGTV
MTALGLSAVAGVPLGLGLANLGGWRAPFWAIGALAAFVWLGLLRVLPRVDGHLSTDSEASPATSLTALFT
PSLALGWLLTFSVVFASFLLIPYLSAFMVGNLGLASTDLPWVYLAGGAATLLAARWIGRMTDRLGPARAL
ALLLVGTMVPHLLFTHLPPSPLPVVAVVFVLFMSLTSTRAIPTIALVASRVPPSLRGRYLAVNMAASDGA
SGLAAWMSGLLLTTAPDGALIGFGQAGWLAVGVSALSLCLLWTFGRSAVRLDAAP
>gnl|CDD|468336 NF038078, NRPS_MxcG, myxochelin non-ribosomal peptide synthetase MxcG
QEARWPLSAAQHGIWLGQQLDLASPVYNAGECIEIRGPVDPAVFEAALRQAVGEAEALHMRFVPGEEGPR
QLLDPSADWPLHRVDVSGTPDPWAAAQAWMREDLARTVDLSRGPLFAEALFKAAPDRFFWYQRAHHIALD
GFGFSLLARRVAELYTARVTGRPATGGFGSLRAVLDEDAAYRAGPQCELDRAFWMERFADRPTPVSLAEP
APMSRSFVRQTRHLSPSEMERLQAVARQAGLSWPDLVLAATAAWLHRRTGAPEVVLGLPVMGRLGSAALR
VPCMAMNIVPLRVPVRPGAGLLALARGVAAELRAIRPHLRYRYEQLRRDLKLVGGQRRLFGPVVNIMPFD
YALRFAGMPAIAHNISAGPVEDLSIGVYARSDGRGPRVDFDANPACYSADELDAHQREFLQLLEALLAAP
EQAVARALIPGAAAPAPAASRPGSLLDGGPLPAPARPVLELIAERAREQPDAIAVEHGPRRMTYRELLLA
ARALAARLVAAGARPDTLVAVMLPRSIDAIVASLGVLFSGAGYLPLDPFGPSSRTAAILADAAPALIVTS
SEHAPTAKAGPQAPGALVVRRLEEAVPSPAPEAPPRPADERLAYVIYTSGSTGQPNGVQISRGALAHFVA
GATQRYGVRRDDRVLQFAPLHFDASVEEIFLTLCAGARLVLRTDEMLQSVPRLLDACAEHGITVLDLPTA
FWHELAYSVSTGAARLPSSLRTVIIGGEAALPERVARWRAAVGPRVRLLNTYGPTEATVVATVATLSGGG
AAGDEGDEVPIGRPLPGVRAALLDAQGRLVAPGAEGELYLLGGGLARGYLGRPELDAARFTTLEALPGRP
RAYRTGDLVRLREDGQLVFVGRVDDEFKISGHRIDPAEVETVLLGHPGVREAAVVGQVLPGGTRRLCAHV
VADAPAPSAAELRRHLLSALPAPMVPGAFVFAERLPRTSTGKIDRAALRRAGPAEESATSAAAATALERV
VLRVWEQVLGVSGLSAQDDFFELGGQSLQSIQVANRLGVALGREVPVATVFRHPTAAGLAQALEHGASVA
AESGGLTPAMLADAELPEDIVPPLATPSASPAPPRQVLLTGATGFVGAHLLDQLLRQTDARVVCLVRARD
EAHAMERLRAALTGQRLPTEGLAERVLALPADLTQPWLGLGSARFHGLAAECDAIYHNAAVVSVVREYGS
LQAVNVRGTRELLRLAAAVRPKPLHYVSTLAVAPQANLSPEVPEAFVPAHPGLRDGYQQSKWIAERLVQQ
AGERGLPVAVYRLGRVVGAPDTGIVNPQDLVWRILLAGIPAGALPQLDVGETWTPVDYVARAIVRLSLVP
RPGTVFNLAPAPEVRLSELFRWVRDYGYPVELCPVPEWRARVAERAAGAANSATLAFFDLRSGSAEPAFG
LGRIRCERVTRALAGSGITCPPTDRALLHRYLDYCVEQGLLPRP
>gnl|CDD|468337 NF038079, TonB_sider_MxcH, TonB-dependent siderophore myxochelin receptor MxcH
PPKLLEFVEAPYPAEALAARLEATVVLRLTLDAQGRVTEAEVVEPAGHGFDEAAREAALRFRFEPARRDG
VPVASRILYTYEFRLPPPPPPSPAPAPPPAEPAAPPPAPAPAPPEAKAPIEVTVRGESEAERRRQSAEAV
QVVETERAQREAADLGEVLARTEGVGVRRSGGLGSRARFSLNGLTDDQIRFFLDGVPLELAGYGFGLANV
PVNLVQRVEVYRGVVPVRFGADALGGAVNLVTDQDVRGTGASASYQLGSFGTHRLTLSGRHLHEPSGFFV
RASGFFDTARNDYPIDVEVPDDLGRLSPARVPRFHDAYRAGGGGVEVGFVDRPWARRLLLRAFLSGYDKE
LQHNLVMTVPYGEVTYGETSAGATLRYEQTFGRGLRVDAVAGYTFRRTRFLDLSTCVYDWYGRCVRTRPQ
PGEIESRAVDQTVWQHTGFARLNLGWTLAPEHTLRLSVAPTFVARTGEDRRLRAPGQRDPLTADRDLFSL
VTGLEYELDAFDGRLENIAFVKDYLQRARAEELLASGTFRPLDRDTHRLGVGDSLRFRLTPWLYAKASYE
WATRLPRPDELFGDGVLIVENLDLEPETSHNVNLGLTLDPLRTPAGSFRANVNGFARLADQLIVLLGRDS
YFTYQNVYAARSLGVEGAAGWTSPGQYLSLDGNVTWQDFRNTSSEGTFGAFEGDRIPNRPWLFANGSARF
QLSGLASPRDELSLTWTTRYVHEFFRGWESLGAAGSKQVIPSQLLHSLALTYVVRDGRATLSWTAEVQNL
TDARAFDFFGVQRPGRALFAKLTLEL
>gnl|CDD|411663 NF038080, PG_bind_siph, peptidoglycan-binding domain. This domain occurs shows apparent homology to known or putative peptidoglycan-binding domains in families such as PF01471. The domain occurs once, or twice, at the C-terminus of proteins such as cell wall amidases. In particular, member proteins can be found among putative lysins of phage of Streptomyces from the Siphoviridae family, such as phiBT1
FPGAAFFGPGASNPIVTALGRRLVARGCGRFYRVGPGPRWTEADRRSYAAFQRAQGWRGADADGYPGPET
WRLLFV
>gnl|CDD|468338 NF038081, BN159_2729_fam, BN159_2729 family protein. This uncharacterized protein family occurs in Streptomyces and related species. Some members have insertions of long stretches of low-complexity sequences
MNKNLPHAARVIREALAGERLDPARAFAHALDAAGLLVDPERSYGAVLPRTTPGGGWVRPPTEPAPREAT
ELEQQALAWDAACARARAVAAALETEHAGHPDVTSIRADGDRVVVALRATSLADWEYWRAYFGITLDQET
PLGYAQTGEGHRDGVRVSVVAYDVPQLLDEAAAAAKRPYRLGGRVYDLALPQRDAHGDTWYFQGQRQEDG
MPLLSLDGRPERCSLANIVTQVGPLTP
>gnl|CDD|468339 NF038082, phiSA1p31, phiSA1p31 domain. This domain occurs in Streptomyces and related lineages, in proteins with highly variable architectures, typically at or near the C-terminus. Member proteins include at least two from known temperate phage of Streptomyces, including phiSA1p31, for which it is named, from Streptomyces phage phiSASD1
DGVTYDLAAPYRDRDGDVWRFTGRRTERGGMPLMSSDGRGGGEPCPLADVVALYGPLTPV
>gnl|CDD|468340 NF038083, CU044_5270_fam, CU044_5270 family protein. Members of this family occur largely in Streptomyces and related species, often with several members per genome. Lengths average about 340 amino acids. The function is unknown
PPGRLARHRERLLAAIRAAPGRRRPRLWRRALLLAAAAAALAAAVAAALLLTGPDPAPAAAPPAPLAVSG
SAVSAAEVLLRAAAAAARQPAPPPRDGQYVYVKSRSAGTEGSDGGGPTVLEELHEREVWTSADGTGRELR
TGWLPEPPGRPDEPGGWVPDGKTYPPGGAGPPRPTYRFLASLPTDPDALLARLYALGGAGDGGGEDRDQA
LFSAIGDLLEESPLPPAVRAALYRALAKIPGVRVVGDVTDAAGREGVAVARDDPGSGERRELIFDPDTGA
LLGE
>gnl|CDD|411667 NF038084, DHCW_cupin, DHCW motif cupin fold protein. Members of this uncharacterized protein family resemble other cupin superfamily small barrel proteins. This family has a signature motif, DHCW, for which the family is named
PNIPFGTTDWSQIEPTEHPGETGTAYWRTQQFGDIRVRMVEYSPGYLADHWCSKGHILLCLEGELVTELE
DGRKFTLTPGMSYQVADNAEAHRSSTETGAKLFIVD
>gnl|CDD|468341 NF038085, MSMEG_6728_fam, MSMEG_6728 family protein
MQTFLPYPDFAASAAVLDPRRLGKQRVETLQVLRALTVPGYGWRHHPAVRMWAGYEEALVRYGLAMCAVW
TARGRADTCAATLAADLPAATGLAARTQAELAAAGELPPWLGDEAFHRSHRSALLRKDPAHYRPLFPDVP
DDLPYVWPA
>gnl|CDD|468342 NF038086, anchor_synt_A, protein sorting system archaetidylserine synthase. Members of this family are homologs of CDP-diacylglycerol--serine O-phosphatidyltransferase PssA of subclass II, as found in Gram-positive bacteria, but occur in a branch of the archaea. In Haloferax volcanii, the member of this family HVO_1143, together with the PssD-related decarboxylase HVO_0146, were both shown to be required for the archaeosortase ArtA to cause removal of the PGF-CTERM sorting signal and replacement with a prenyl-derived C-terminal lipid anchor. Based on these observations, members of this family are suggested to be CDP-2,3-di-O-geranylgeranyl-sn-glycerol:l-serine O-archaetidyltransferase, generating archaetidylserine en route to archaetidylethanolamine biosynthesis
PRFVGRLGVADAVTVANAALGFLAAVAAFVDPALAARLILLAAIADGLDGVVARRYGGTPAGPYLDSLAD
VASFGVAPALLVVAVVRDAWGAAADPPVAVGAVVVAALFVAAAVVRLGLYTAYDTAHEETEGVQTTLAAT
ILAAAVLAGVTDPAVLVAATVVLAYLMVSPITYPDLLARDALVMGVVQALAILAPGAFGRAFPRALLTLA
LAYLVLGPRFYW
>gnl|CDD|468343 NF038087, arch_ser_synth, archaetidylserine synthase. Members of this family, including founding member MTH_1027 from Methanothermobacter thermautotrophicus, resemble subclass II bacterial CDP-diacylglycerol--serine O-phosphatidyltransferase, but act as instead as CDP-2,3-Di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase (archaetidylserine synthase)
KSFIAIPDIISLLNASSGFLSIIMAINGNLILAAILMLLAVIFDSVDGWVARKINRVDELGFGKNIDSLS
DIISFGVAPAIFLYSATATISFRYINILVSLLIVICGILRLTRFNVIADKGPTKGFIGLPIPGTALILSS
FYLSGLFNEYIALILMIIVSLLMISNIEYPKFNNKKLIAIGAILIILTILPIPITIYIINIPALILFILT
LIYLLI
>gnl|CDD|468344 NF038088, anchor_synt_D, protein sorting system archaetidylserine decarboxylase. Members of this family, including founding member HVO_0146 from Haloferax volcanii, are archaeal homologs of bacterial phosphatidylserine decarboxylases (PssD). HVO_0146, and the PssA homolog HVO_1143, were shown be required for archaeosortase A (ArtA)-mediated removal of the PGF-CTERM protein-sorting signal and replacement with a large, prenyl-derived, C-terminal anchoring lipid moiety that is proposed to be archaetidylethanolamine
FAPGAWRYALPPLLAAPVALVFSPPAGAVALALGAGVLWFFRDPERTPPPTGVVAPADGTVSVIREEGER
VRVGVFMNVTDVHVNRAPFAGTVTDVEHRPGANRPAFSKESDRNERVHIDFETDSGDAEVTLIAGAFARR
IHPYVEPGDELERGDRLGHIAFGSRVDVLLPPEVDREDLAVEKGDSVRAGETVVAE
>gnl|CDD|411672 NF038090, IscA_HesB_Se, IscA/HesB family protein. Members of this family, a large fraction of which are selenoproteins, are homologous to proteins of iron-sulfur cluster biosynthesis such as IscA, and belong to the broader set of HesB-related proteins
MLEVTDLASRKLKEYFADKKIDSPIRVFLNQGGUAGPSLGLALDEPKENDEVFEQDGLTFVIDKELLEQC
GPIKVDFIDCRSGFSITSSMPLGGGGCGS
>gnl|CDD|468345 NF038091, T4SS_VirB10, type IV secretion system protein VirB10. Members of this family are VirB10, an outer membrane-associated protein from the apparatus of protein type IV secretion systems (T4SS). The model attempts to exclude related TraI proteins of conjugal transfer systems as well as the ComB10 protein of a DNA-translocating competence protein of Helicobacter pylori. Because the N-terminal regions of VirB10 proteins are highly variable, the model
ATRLGDRDLLLTQGTMIPCVLETAIDSDLPGMVRCVVTRDVYSANGRVVLIERGSRVIGEYQSGLSQGQA
RVFVLWTRIETPDGVIVNLDSPGTDELGRSGLPGYVDNHFWERFGGAILLSLIGDAGQYAANKGQNGNGS
GNGNSVNFENTSQAASDMASEALENTINIPPTLYKNQGDRINIFVARDLDFSGVYEL
>gnl|CDD|468346 NF038092, T4SS_ComB10, DNA type IV secretion system protein ComB10. ComB10, a VirB10 homolog, is an outer membrane-associated component of a DNA-translocating type IV secretion system (T4SS) involved in competence. Most T4SS translocate proteins, but both ComB10 as found in Helicobacter, and the T4SS of Agrobacterium, translocate DNA
GVDGFSNQKSKDIATNEHKLLRTITADRMIPAFLITPISSQIAGKVTAQVESDIYASMGRAVLIPKGSKV
IGFYNNNNKIGEYRLEIVWRRIITPQGVNIMLTNAKGADVKGYNGLVGELNNRYWQRYGIPLLLSTLSNG
LLIGITSALANRMNKNNFFGDYYLMQLTRQSGMDINQIVQQILQQQSQIKPIIIIREGSRIFISPNLDIF
FPIPKNGEVLAEFFN
>gnl|CDD|468347 NF038093, GrdX, GrdX family protein. GrdX is a small protein, of unknown function, encoded in grd operons for selenocysteine-dependent glycine reductase systems. A small number of GrdX proteins appear to be encoded with a UGA-encoded selenocysteine residue appearing close to the N-terminus, at sites that do not align with Cys residues in other members of the family. This arrangement suggests that the ability to complete translation of GrdX selenoproteins may have regulatory value, in addition to whatever may be the molecular function of GrdX itself
IIVTNNPLVKEKYKNIVYLVEGSYLDVLIKVRDLIHKGYRLLTHPLSGSIKPNETPYRSVILSKGKSASL
DMDSLELIENAIETYEKFMKNRKPPNWSEKILEDFQTIDLELIESALE
>gnl|CDD|468348 NF038094, CueP_fam, CueP family metal-binding protein. Members of this family including CueP itself, a copper-binding periplasmic metallochaperone, as found in Salmonella enterica serovar Typhimurium. Many family members, although not CueP itself, are lipoproteins. Several other members of the family are selenoproteins, including members from Bacillus selenitireducens, Bacillus beveridgei, and others
DAEEIIDLLDQLSVAERPTDLSASVTSDELVLSDGDDGETTLPLPEDEFYVSIAPYVEQTHPCFFHSLTG
CQGELANEEFDVTITDADGGEVLDDETVTTYDNGFIGLWLPRDITGTITISHDGKTAESPISTFEDDPTC
ITTLQL
>gnl|CDD|468349 NF038095, met_chaper_CueP, copper-binding periplasmic metallochaperone CueP. This narrowly built model for CueP includes periplasmic proteins from Salmonella enterica, in which it contributes to an increased tolerance to copper, and from various other Gram-negative bacteria. It does not include CueP lipoproteins from species such as Corynebacterium diphtheriae
KRLTLLALLALALSGSALAATQETAFLAQHGLAGKTVEQMVDAIDQSPQARPLPYSASVTSTELKLSDGQ
QAYSYPLGDKFYLSFAPYENQTHPCFNHSLSGCQGEMPNTPFDVKVTDKKGKVILQKTMKSYQNGFIGVW
LPRNIEGTIEVSYQGKTASSPFATHDDSQTCLTTLQL
>gnl|CDD|411678 NF038096, thylak_slr1796, thylakoid membrane photosystem I accumulation factor. Members of this family, restricted to the Cyanobacteria and chloroplasts, show homology to thioredoxins. However, the core region of family protein alignment shows either one Cys residue or zero, suggesting family members may share the thioredoxin-like fold but lack redox capability. The founding member of the family, slr1796, was shown by proteomics to localize to the thylakoid membrane, consistent with taxonomic restriction to the Cyanobacteria. Targeted mutation of slr1796 shows a role in successful translation and insertion of photosystem I proteins into the thylakoid membrane
ALAGLDDDRYDGNIFALYAGNGSLVPPRVTLAQSLARHRPALLVFYLDDSSDCKQFAPVVSQLQAFYGRA
ADIIPVTVDSLPLKDSYDPTEPGYYYKGVVPQTVVLDQDGKVVLDEKGQVPFEEIDDALREVFDLLPRSE
SVELKRRSFNEFNSELV
>gnl|CDD|411679 NF038097, KCGN_DNA_rpt, KCGN motif-containing spurious repeat. This AntiFam-type HMM recognizes spurious protein translations, often with the motif KCGN, of a DNA repeat widespread in the genus Leptospira
GNSHKLRFFTKLLKCGNSYKL
>gnl|CDD|411680 NF038098, GyrA_w_intein, intein-containing DNA gyrase subunit A
RIEPVDIQQEMQRSYIDYAMSVIVGRALPEVRDGLKPVHRRVLYAMFDSGFRPDRSYVKCARVVAETMGN
YHPHGDSSIYDTLVRMAQPWSLRYPLVDGQGNFGSPGNDPAAAMRYCVTGDALVRLPDGQSVRIGDIVPG
ARPNSDNVIDLKVLDRHGDPVRADRLFHSGEHPTLTLRTREGYELTGTHNHPVLCLVDVAGVPTLLWKLL
EEIRPGDRVVLQRTPPDEFGPADWRETAEALLAGAFVSEGFVSENRAGFNNLDRDFFAMVVAAYDAVVGG
PRYVSSRTIASGSTLHELDVQDLTALRKSRLGELVGQRSADKRVPEFVWQSPAAVKRAFLQALFEGDGSC
SALPRNTIQVSYSTRSERLARDVQQLLLEFGVVSRRYRHATGEIKVVITNRRDARLFATRVGFGGAKQDK
LEAILAAVPADSRAMSSDHVPGLAEFIRAHGASRWTERDWLRRHNVDRIERWERDRDEILSRITDPDVLA
VVEPLTDGRFYYAEVASVTDAGVQPVYSLRVDTDDHAFITNGFVSHNTEARLTPLAMEMLREIDEETVDF
IPNYDGRVQEPTVLPSRFPNLLANGSGGIAVGMATNIPPHNLRELADAVFWCLDNPEADEEETLAAVMER
VKGPDFPTHGLIVGTQGIEDAYRTGRGSIRMRGVVEVEEDARGRTSLVITELPYQVNPDNLIESIAEQVR
DGKLAGISNIEDESSDRVGMRIVVELKRDAVAKVVLNNLYKHTQLQTSFGANMLSIVDGVPRTLRLDQMI
RHYVDHQLDVIVRRTRYRLRKAEERAHILRGLVKALDALDEVIALIRASPTVDVARTGLIELLDVDEIQA
QAILDMQLRRLAALERQRIIDDLAKIEAEIADLEDILAKPERQRAIVRDELKEIVDKYGDDRRTRIIPAD
GDVSDEDLIAREDVVVTITETGYAKRTKTDLYRSQKRGGKGVQGAGLKQDDIVAHFFVCSTHDWILFFTN
KGRVYRAKAYELPEASRTARGQHVANLLAFQPDERIAQVIQIKDYEDAPYLVLATRNGLVKKSKLTDFDS
NRSGGIVAINLRDGDELVGAVLCSAEDDLLLVSAKGQSIRFSATDEALRPMGRATSGVQGMRFNEDDELL
SLNVVREGTYLLVATSGGYAKRTPIEEYPVQGRGGKGVLTIQYDRRRGRLVGALIVDDDDELYAITSGGG
VIRTAARQVRKAGRQTKGVRLMNLGEGDTLLAIARNADEPDD
>gnl|CDD|468350 NF038099, AsSugarArsM, arsenosugar biosynthesis arsenite methyltransferase ArsM. This form of arsenite methyltransferase works together with the radical SAM enzyme ArsS in a pathway of arsenosugar biosynthesis. Examples of ArsM such as slr0303 from Synechocystis sp. PCC 6803 and alr3095 from Nostoc sp. PCC 7120 are encoded next to ArsS
SYLETTADFYKEAAETPDVGLCCVQTTPLQLPGLKIPKIMQEMNYGCGSTVHPRELVNNPTVLYVGVGGG
LEALQFAYFSRRPGGVIAVDPVDEMREAARRNLKIAAEENDWFDPDFVDIRKGDALDLPVPDNSVDVAAQ
NCLFNIFEPDDLKKALQEMYRVLKPGGRLVMSDPIATQPIPEHLRQDERLRAMCLSGALTYEEYLQVITD
AGFGQVEIRARRPYRLLDPNHYGLDENLLLESLESVAFKVPMPEDGACIFTGKTAIYFGNEEYFDDGAGH
ILQKGQPLAVCDKTAAALASLGRDDIVITDSTWHYDGGGCC
>gnl|CDD|411682 NF038101, Trm112_arch, methytransferase partner Trm112. This HMM describes an archaeal branch of a small protein, Trm112, that is conserved in the three domains of life and that serves as general activator of methyltransferases for RNA or protein
MKESLMDILCCPVCKGDLELEVDEEDDEEIIEGTLTCTACGEDYPIEDGIPNLLPPDMR
>gnl|CDD|468351 NF038104, lipo_NF038104, NF038104 family lipoprotein. This family of small lipoproteins of unknown function, about 68 amino acids long, occurs in genera that include Acinetobacter, Moraxella, Neisseria, and Psychrobacter. The N-terminal half, including the lipoprotein signal peptide, shows significant sequence similarity to the divisome-associated lipoprotein YraP, a three-fold longer protein, as found in Eschericia coli
MKKIIRLLALLACVLSLQGCIHVKVVTVAVKVAYKTTKGVVKGTGAVVDAVIPDGDDDDDKD
>gnl|CDD|411684 NF038105, acin_NF038105, NF038105 family protein. This family of small proteins, about 66 amino acids long, appears universal in the first 20 species of Acinetobacter examined, but absent outside the genus
MTTKKFDATPTPSEPISLDEISKENVKEAWKDYEAKPEYKEFNKHDLIESMQSAKEEDQKSQ
>gnl|CDD|411685 NF038106, gamma_NF038106, PA4642 family protein. Member of this family are small (about 95 amino acids), uncharacterized, and apparently restricted to the Gammaproteobacteria. Members include PA4642 from Pseudomonas aeruginosa PAO1
KKDKQKVIGEEWSDERVKSFLDVEPPDGTNADFHVLIKAYRGMRAEDFERFVGFFVEAGRDLNATDPDGQ
TFLDIIAEHRQSAEYAEALKAAG
>gnl|CDD|468352 NF038107, rSAM_NF038107, Cys-every-fifth radical SAM/SPASM peptide maturase CefB. Members of this family are radical SAM/SPASM domain proteins, most of which perform post-translational modification on RiPP peptide precursors or enzyme subunits. Target residues for modification often are Cys residues. Members of family NF038108, with a Cys Every Fifth position (CefA) over most of the short length of that family, are the putative target RiPP proteins
MKYSRYNLIIPVSDNKNILFNTLTGEAFIIEDDVKNAIESGNIDKLDDDEIKKFSNKKIIIDDNFDELKY
FEYYHNKVKFQNNHLTYTILLTWACNLKCVYCYEGAGENRNDFMTKETADKVIKFIKKQAEKRKVKSISI
FLFGGEPLVNFKEGKYILEELNDFCEERGIILNSGIITNGTLLTDEIIDDLKHFNCKYIQITLDGTKEIH
DMRRIRKGGSGSFDEIISNLHKLKKYEKKLNVVIRINIDKTNIDEVPKLLKYLKKEGLTSCSIDFGIVRG
STEACSSYEGNCFSESELGQILDELWKEAEEVGFNILTKPMRKWTYCGLYSDSNFTIDPTGNVYKCWEHV
GEEEHKMGAIDENGEITNLNFKYYKWMTRNPLDSDECRNCVYLPACGGGCGAISYNETVSYDSKGCFKVK
GVIEKQIKLYFKDKLEHKCAECSA
>gnl|CDD|411687 NF038108, RiPP_NF038108, Cys-every-fifth RiPP peptide CefA. Members typically are shorter than 100 residues, with from nine to eleven Cys residues spaced strictly as every fifth residue and usually with at least one adjacent Gly. Most family members occur in the vicinity of a peptide-modifying radical SAM/SPASM domain protein, marking those family members as putative RiPP (ribosomally translated, post-translationally modified peptide) precursors. Because of the small size, richness in Cys and Gly residues, and strictly repetitive nature, it may be expected that some predicted proteins, scoring above the thresholds for the model, are related by convergent evolution rather than by homology, and are not themselves RiPP precursors
YVGNSYGGGAETVCGADVCPAKACGANACGADGCGINACGGNGCAIEGCPVDACPVDGCWIDLFP
>gnl|CDD|439425 NF038109, tapY2_fam, TapY2 family type IVa secretion system protein. Members of this family average about 100 amino acids in length and include two invariant Cys residues. The family is named for TapY2 (Type IV Aeromonas Pilus Y2), which in PMID:18212071 is called the counterpart to PilY2 from the type IVa pilus system Pil in Pseudomonas aeruginosa. However, sequence similarity between TapY2 and PilY2 is very low, and is not certain to represent true homology
LLLSSMALLAAAEAVSRQDYKCYLTLEKGAQVVFYRWKESTVNLNIASLPGKKLFSNDGKKYYIKEVIEC
VPLNADFTNEKAKQLDEITPR
>gnl|CDD|468353 NF038110, Lys_methyl_FliB, flagellin lysine-N-methylase
PDYYKKFKCIGSKCEDTCCKGWWIDIDKKTYKKYKKKSGDFGIRLRAKKNIKKIKKSEDGWAGIILLDED
GRCPFLDEDGLCDIHKELGEEALSDTCKTYPRVINEFEDVREKSLSLSCPEAARLILLNPEAIEFEESEE
DEEEYKEEIEDIDPSLFQYLLEIRDFLINILQNRELSLEERLYLLGQFLLKLQELYKDGDEFEEIEELIE
ELLEFLIDGELKEYLKPINYLLQLQLLLELIDARDWLGELNSLRYKLLGNEFLELLKAFEDALEEEEIDR
LLQAWNEYYEPFLEEYEYILENYLVNYIFKNLFPFSLSESLDSYQLLVLDYLLIRELLVARALKNGGLTE
EEDVIEIIQSYSKEIEHNDENLELL
>gnl|CDD|468354 NF038111, rhom_dep_M36, rhombosortase-dependent M36 family metallopeptidase. Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal GlyGly-CTERM domain, recognized and cleaved by rhombosortase
TAIATAVSAALATAALSAAANDANQANASYQSQAQAQAQQAQRALAQQPTVSGMRNQYDAQLGKATFQWA
PKGQAAPNLGALAAEHQLAFAADFYLNQLTGLSSTKSSQLKAVLASMHDLGRGAKIAKYKQEVAGVEVFN
REYNIMMDREFNLVASSGYFADKTASAAASIKAALAAFGDAETAINAAFKAMGGDSNSLSLTAKKSEGKY
QSFSVTNSSTDKKILGEPRAKKVFFELKGKLVAAHYVEVETADSDSVDSDYYSYVIAADTGKVLFKNNLT
SHAADFNYRVYADEDGYPWDGPHGNVIPAPSADQVDATEYLDAPLVTLSHGPISTMDPWLADDATTTSGN
NVFAYVDAIAPDGFTNGDYTAETTSANTFDYKYDTDEAEYSVNNRKAAIVNLFYMNNYLHDDFYDHGFDE
ASGNAQLSNYGRGGVEGDPLNAEVQDNSGFNNANMSTPADGRSPRMQMYLWDSKDAVVGEDYGVTVTSHD
DIGLLDSTQRSSFGPGQFDISGDLVRLDDGTGPVNDGCEAATNAAELAGKIAIIDRGACAFTVKVKNAQD
AGAIAVIIVNNVDDGTPAPMGGDDDTVTIPNMGLSFADGAAIYAALDAGETVTVSMFNNRPFKDSSWDNG
IVAHEWGHYISNRLVGNGSGLINNQGRSMGEGWGDFHALLLLSEADDALIAGNEKFQKAYAATTYVASFY
TGIRRYPYSTDMEINPLTFKHIELGAGTPTDVAEVHAAGEVWAAMLWDSYVALINDERHTFAEAQSRMKD
YLVAGYKMTPVAPTYTEARDAILAAAYANDPEDYKLILAAFARRGMGLGAVSPERFSTDHAGVVESYKTE
LSAFAVASHTLNTNYEGLTVGYCSNDGILDKGETGTVSFTIKNRGSETLTNLKAKVEVVSDHDVTFANDG
KITFDDLAPFASATSSPIEFTLNEAGTADELELKLSFPELAEGVVPEEYSLSTTVNYDFKDKALVGNSST
DDMETYSLLNDFKENVLVGGDLAKGTQSLDNTFNIAFFSGFDLGEQYMFLNNNGFESDVAYETKAFTVGY
GGDFTISFWHYYALEEGWDGGVVEISVNGGDWVDVTEVGGGFFGVGYNGTLIENLEQALPGRPVFTGNSF
NGGNTETINFGTALNGNQVKFRFRIVSDSNANDFGWWIDNVTFSNITTSVFSDVVAGDSNACDNRLPNVS
IVASSQSVNEGDSVTLTATATDANGDTLTYSWKQTSGTAATLTGADTATASFTAPSISSGETLEFEVTVS
DGTGSVVSTVSVTVNDVPVPPPPPPPKKSSSGGSTGWLALLLLPLALLRRRK
>gnl|CDD|468355 NF038112, myxo_dep_M36, myxosortase-dependent M36 family metallopeptidase. Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes
MRLRVKLLSSLLLVPLAGTSAWAKELPNYDAFLEQRPSRPLAVDPATAVARGLRVEHTEARLGVPTFVWA
TRQSGAQSKSAALAGMTPEQAARAHLQEVADLYRLSSEDVAGASLRSVHRTGRGAVVVTFAQEVDGIEVF
RNELKVLMDQNNELVAVSGYLSPHESTLTARAKARLAFRLGAAEAIAAAFKDLTGSSLDASSLVNTGVTK
GDYTHYELAPYARPALPQGLAIPARAKQVFFPLPDGLVPAWYVELNTGPAGSTDSDYYAYVVSAADGRVL
FRNNLTAHAAFSYRVWADTTSPYIPHDGPQGNDATPHPTGTPDGYQAPLFVPPNLVTLQNSPFSRNDPWL
PAGATQTTGNNVDAYADLVAPDGFQPGSDLRATVTAPGVFDYVYDFTQAPGASAEQIKAAVTNLFYVNNF
LHDWFYDAGFDEASGNAQADNFGRGGVEGDPIRAEAQDYSGRNNANMSTPADGASPRMQMYVFDGTPEQT
LTVTAPASLAGVYEAGSASFGPQAFDVTGDVVLAPDGTGSDTDGCTPFTNAAEVAGKIALIDRGTCDFTV
KALNAQNAGAIGVIIANNAAGAAPGLGGTDPAVTIPALSITQADGNAWKAALANGPVTVRLRREPALDRD
GTLDNGIVAHEWGHYISNRLIGNAAGLTNNQGRSMGEGWGDFHALLMQVREEDINVPGNANWQGAYAVAG
YASSGGSNDGYYFGIRRVPYSTDMSKNALTFRHIANGVPLPTTAPINPLTGLSNAEVHNSGEVWATMLWE
CYASLLNAHPFQEAQDRMKRYLVAAYKLTPNAPTFLEARDALLAAAYANDPADYQRFVAAFAKRGAGFGA
KAPDRDSTDHAGVVESFATGNNLEVVSIELDDSVGGCDQDGVLDNGETGLLRVTVRNVGAGPLSAFTATV
SSSTAGVTFPNGGTVSFPALARGATATVTVPVSLTGAGTVARAGFTVAFRDEPQLPPGDKTATFDVRVNY
DEVPASSTTETVESGLSPWTVSTDELLASGDWSVVEEPDGNRYFHGPNPSVAADIRLTSPWLQVSATGDF
VFSFKHRHSFESDYGGAPPYYDGAVIELSEDGGQTWVDIGDLDADPGYTGTLYEGGGNPLEGRPAFVGTS
AGFPAFISATLNLGTAFAGKTVRFRFRIGSDVAVGAYGWDLDDLKFTGITNTPFTSLVAEPGVCNRRPVA
NAGPDQTVLERTTVTLNGSGSFDPDGDPLTYAWTQVSGPAVTLTGADTATPSFTAPEVTADTVLTFQLVV
SDGTKTSAPDTVTVLVRNVNRAPVAVAGAPATVDERSTVTLDGSGTDADGDALTYAWTQTSGPAVTLTGA
TTATATFTAPEVTADTQLTFTLTVSDGTASATDTVTVTVRNVNRAPVANAGADQTVDERSTVTLSGSATD
PDGDALTYAWTQTAGPTVTLTGADTATASFTAPEVAADTELTFQLTVSADGQASADVTVTVTVRNVNRAP
VAHAGESITVDEGSTVTLDASATDPDGDTLTYAWTQVAGPSVTLTGADSAKLTFTAPEVSADTTLTFSLT
VTDGSGSSGPVVVTVTVKNVNRAPDGGGCSSTGGSPGGMLPLLLLLAALALSRRRRA
>gnl|CDD|468356 NF038113, T9SSA_dep_M36, T9SS-dependent M36 family metallopeptidase. Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131)
LLLFLLFFFSFNLGFAQDYEELIKDYLNKNKSKLSLNNQDISDLIILNEDFSKSTGANVVYVQQTYNGIP
VYNAISNVVIKNGKVVSAKNNFIENLSSKVNSTQPSLSPNQALQKAASHLGLGNISNLTLLETKSNKDVL
SNGGISLENIPVKLVYFFSENGTLKLAWELSIYELDSSHWWNVRVDALNGEILDKNNLVVSCNFEHNTHS
HTVEKSNSFNLVSNNLAENSNSLLADGAASYNVFPLPVEAPNHGSRTLVTNPWDLTASPFGWHDTDGTNG
YTITRGNNVYAYEDVNNTNTPGYSPDGGATLNFDFPLDFNQEPLTYRDAAITNLFYWNNIMHDVWYKYGF
DESSGNFQTNNFGRGGNGNDAVNAEAQDGSGLNNANFATPPDGSAPRMQMYLWSGAPDGNLLQVNAPGSL
AGRYPGVRAGFGPRLPDAPITGDLALATDSSPDPNDGCDPILNAAALAGKIAVIRRGSCEFAVKVLNAQN
AGAIAVIIVNNVPGEPIVMGGGDTGPPITIPSIMISQADGEAIITALNNGETVNVTLKDDGSGPVMIDGD
FDNGIIAHEYGHGISNRLTGGPQGSSCLSSLVNEEQMGEGWSDWFALMMTMKPGDTATDARGIGTYALGQ
PTTGRGIRPAKYSTDFAVNDYTYGDTNNASLAVPHGIGFVWATMLWDLTWAYIDKYGFDSDLYNGTGGNN
KVLQLVIDGLKLQPCSPGFVDGRDAILEADQLTTGGANKCLIWKAFARRGLGVSASQGSSNSRSDQVEDF
TVPPPLANCTSLATNEFGANKFIIYPNPAKGEIFISFSNKDSGEVKVKVYDINGRLVLSDKVELTNTKTI
NTSGLQSGIYIVKIEGGSKSYTEKLIVK
>gnl|CDD|468357 NF038114, rightmost, PxKF domain. The PxKF domain is found in a number of extracellular proteins, always as the most C-terminal domain (710 of 710 at the time of HMM construction). Upstream regions of proteins with the PxKF domain often mark them as members of largely surface-associated proteins, processed and anchored by the type IX secretion system, exosortases, rhombosortases, etc. The species distribution of PxKF domain-containing proteins is broad - mostly Actinobacteria, but also some Firmicutes, Deinococcus, etc. That broad taxonomic distribution, plus its large size (over 100 amino acids long) compared to most known N-terminal or C-terminal sorting signals that are recognized but then removed, suggests that the domain is retained in the mature protein, and has some function involved in surface-binding
GGFLQPVDNPPVLNTVKAGSTVPVKFSLGGDRGLDVLAAGSPTSQPVACDTGAPVDEIEETVTAGGSSLR
YDATGGQYIYNWKTPKSWAGTCRRLTLTLDDGSSHTALFKFK
>gnl|CDD|468358 NF038115, SVAGG, SVAGG family GlyGly-CTERM protein. The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane
KLLIAIGLLLALLSAMATTTIDVNFVVDQAIVESQGREALDKQIEAAISLSNETYLSAGTDLHFNVRQVV
VESDNSVDATCTSGLGGALDGLLASGQIACRDAYDEAFNHMDNVVWDCPSPGDNDRVGNAGYSYGADFWV
TIVSGSDGNANGVAQVGMDLQVKGYNVTLDLYVATQTLAHELGHLFGLYNGHAESAECSEGGYRLMCGSL
AENFENLFGSSELQRFYNNADSTLDDWTYNNRSYSGWPKASGAGVMPAPAVGLRTVSLQVSGTTLDNTAP
SIEVSVTLSGADQLDHDVSVELYTEGGTAKAGDNYFDDVYQRVTFDPGETDKRVDVRLTHKDLRFTDKSF
TVGLRYGNAVAVDSNVVTVTVAGTGVENGKDSGSGGGSTGPLSLLGLLLLALWRRQK
>gnl|CDD|468359 NF038116, Sden1266_dom, choice-of-anchor H domain. The choice-of-anchor H domain is observed, in from one to four copies, in over 500 proteobacterial proteins with a C-terminal protein sorting signal, GlyGly-CTERM, that directs processing by rhombosortase, transport by a type II secretion system (T2SS), and (most likely) covalent attachment to the outer membrane. The domain is also observed occasionally, in up to 13 tandem copies, in proteins sorted and processed instead by a type IX secretion system (T9SS), which also implies transpeptidation and covalent attachment on the cell surface. One member of this family, Sden_1266, is toxic if expressed as a transgene in Escherichia coli, as might be expected given the lack of the required processing machinery in that species
DFWIYDADTELFSDLDGDGYYSQFSVTFDADTDYSSADVYAVLYLSRDGGPWELYYTTDVFTIYGDSSSD
SYEIETELLSGYPSGYYDVLIELYDADTGELLATYSPYDDSDLSDLPLESADYD
>gnl|CDD|468360 NF038117, choice_anch_I, choice-of-anchor I domain. This domain is found in the N-terminal third of the alkaline phosphatase PhoA of Synechocystis sp. PCC 6803 (see AGF50645.1), upstream of the region presumed to have phosphatase activity. It is found in a number of other cyanobacterial proteins called PhoA, although those annotations may be incorrect. Proteins with this domain include a number with the PEP-CTERM protein-sorting domain, but also a number with the LPXTG protein-sorting domain, making this a choice-of-anchor domain, that is, a new homology domain of what was previously "dark matter" (that is, lacking any HMM), whose members include proteins targeted for covalent attachment at the cell surface by at least two different protein-sorting systems
AEIVAYDPATQRLFVVNASANGVDVLDISDPAAPGLLIQHIDTGLANAGGSVNSVAVHNDGLAAVAVEAP
TKTDPGTVVFFDTNGRLLNGGSVTVGALPDMLTFTPDGSKLLVANEGEPADDYTVDPEGSVSIIDLSTGV
AVVATAGFTAFNGGDELLPEGVRIFGPNADTVSQDLEPEYIAVSADGTKAYVTLQENNAIAVLDLATGTF
TDIVGLGFKDHSLPGNGLDASDRDGAINILTWPNVLGMYQPDGIASYTAGGQTYLVTANEGDAREDDGYS
EEARVLDPSAFGNAGAELQADENLGRLNVTTTDGDTDGDGDYDELYAFGGRSFSIWDEDGNLVFDSGDDF
EQITAALGPEFFNSDNDENYFDGRSDDKGPEPEGVTLGEVGGRTYAFIGLERIGGVMVYDITDPANPSFV
DYVNNRDFSLGAAGDLGPEGLLFISAADSPTGQPLLAVANE
>gnl|CDD|468361 NF038118, PEP_CTERM_CCXG, CCXG family PEP-CTERM protein. This exosortase-dependent PEP-CTERM protein has an unusual CCXG motif, with two adjacent Cys residues
AGNASASVITIQTGYSTAGAQATADAYRSAVSAAAATSAAGYGSTVLSTYDNVSNFSLFGSGNSNIAFKS
TINFGVTAALAGTWSFRAGVDFGYGGAVFLDGVLLDNRTDDLWWGGNWSNTSDVLSGSAANLSAGNHTLD
IYGLEGCCDGGQQAQFKVDGGAWQTFSVADLLAAAVPEPASLALLGLGLGGLAARRRRR
>gnl|CDD|468362 NF038119, PEP_CTERM_MHFG, MHFG family PEP-CTERM protein. This PEP-CTERM protein, dependent on exosortase for processing and export, is named for a distinctive MHFG motif
QPNCSWDRPGVNPYMGDVAAAVDRYTDIPAAVRATLKARMEARQYDDIVTITRDAIAGKYQYDPAIRDMH
FGAGSVCRTVTRAKWSAQRQEPGLVYCVDGHCILVPTICGNVSRITRLPASGAAAAGAPAGAGFPPPAAG
LAAAPPAADLPLPDAPPAAGAPGAALPPAPPDGVPPLPPAAAAAPPGSGPLGLTEGGLPEPPPPPGPPPP
FGPRPPPPPGIDGGGGPPPLPPAPPVPEPDTWAMLLAGLALLAWAARRRR
>gnl|CDD|468363 NF038120, PEP_CTERM_QFxxD, NF038120 family PEP-CTERM protein. This family of PEP-CTERM proteins has a notable motif, QFxxD, near the PEP-CTERM region, for which it is named
PAQAAVIDFESLAPSGLYGGGDTFQEGGYTLTVLSNPPDAQGGGLVGAIIDGSDPGSCAGLACPVGNASN
YYAGLNDGSLDFTRADGAAFSLSSLDASFIGPGGGLYPASAGQLRLQGFRADGGSVSATFDLPGPDANGN
FNFGTFDLSAAFGNTVFTSVTFFACLCDASGSCSAFATNQAQFALDNISVAAVPEPASAALLGLGLGALG
LAARRRR
>gnl|CDD|468364 NF038121, PEP_CTERM_LEVG, LEVG family PEP-CTERM protein. This well-conserved family of PEP-CTERM proteins occurs in Cyanobacteria
MKKFNLLAKTLAATTLGLGIAGAMSAAQAASLVPQQEGEIKLTNLCLDLNCCIATTSTLPLGYTVTSLDY
DTTYGKSRLFVDDRTTANTYGGGGISFGTTDAGTNPGAGEYWFRPVAIDANGKLPENGQLEVGRFKFDFT
KILSELTLDFFDVEDIGFTGILSVNGQSVNLSALLLAAGPNNGNIQSLTLKNVKSFVLQLGNPGGDKFPK
TTGDGVRLQGEGKSVPEPGTTLGLGALAVAGMFGLRKRKKAS
>gnl|CDD|468365 NF038122, metallo_LGF, NF038122 family metalloprotease. Members of this family are marked as probable metalloproteases by striking local similarity of its HExxH motif-containing region that of PF00413. This family is notable in part for the large fraction, nearly half, with a PEP-CTERM domain or similar C-terminal signal for protein sorting and covalent attachment at the cell surface
AEAAFEAAAAYWESLFTDPVTVNINVGFTPLGSGVLGGTSSTLLSVSYSDYRAALAADATSALDATAVAN
LPTGPTSGPSNNSTLGLTTANAKALGLLAASGGGGGLDGSITFNSSFFNFDFDPSDGISAGTYDFVGVAA
HEIGHALGFVSGVDGLDYNNGNTLTNYFTPLDLFRYSAPGVRSGTSGNGVGAAYFSIDGGVTNLAGFSTG
SGNGDGRQASHWKDDALGLGIMDPTLGPGERGAITALDLAAFDVIGWD
>gnl|CDD|468366 NF038123, NF038123_dom, spondin domain
ATYTVTITNLTPPNGQPFSPLVVAAHNGNFDLFEVGEPASEGLERLAEGGDPSGLLSALADQAGVVVVAV
PGGGPLAPGASESVSFTFEAADGDYLSLATMLVPSNDWFVGLDSLDLFDLAGGGTVTLSLNAYDAGTEAN
DEPEVNIPGPAGGGEGFNGAGPDTDENGVVAIHPGVPGDDDADGGISDVLNPNHRFDNPVAKVVITRT
>gnl|CDD|468367 NF038124, PEP_CTERM_TLD_A, PEP_CTERM-anchored TLD domain-containing protein. Members of this family represent one branch of the TLD domain family, predicted to be a family of enzymes (see PF07534). All members furthermore have a C-terminal region, PEP-CTERM (TIGR02595 or one of its variants) for recognition and processing by an exosortase, and presumably attachment on the cell surface
KFAAAAVALLAVAAAAACASAGVAAGGSTLLDAADQAQLESWLGEGPLDLTNIYTKTAGDTSADFHAAVD
GKGRTFSLMEASNAAGQTWLVGGYNPQSWSSSGGYNVTPDDSDRTAFLFNLTSGVVHRQTPKDFVLDSYG
AYQTYNDADYGPTFGGGHDLYVPDDLTTGGYSLLYSYGDPSNTGRSIIDGSPYGGPNFTVGALEVFSIAA
VPEPGTLALLLAGLGLLGLAARRRR
>gnl|CDD|468368 NF038125, PEP_CTERM_THxN, THxN family PEP-CTERM protein. This family of PEP-CTERM proteins is named for one of several well-conserved motifs. The function is unknown, but DVUA0032 is mentioned as a member protein whose expression depends on a 54-dependent promoter. PEP-CTERMs are expected to be expressed covalently attached to outer membrane
KTLLAALALALALGAGSASAAPITEWDYSVDSAFTNFTSGGGTGSGDGTTTLSWGNGGGDQSGLGISNSP
GTLITNGAAVDGGTFTHFNNPITGSSATLTSADLSSTLTLTPFDPAGGALPTPTTTFDFLFNETPNSGPC
APGSNSPCDDIFVLDFGFLSQSFTIDGYTYTVSFLELDGLGTLSDAACAAAGAAAGCIGFTTPEGQSNTF
QFRFRITARPVSVPEPGTLALLGLGLAGLGLSRRRK
>gnl|CDD|468369 NF038126, PEP_CTERM_FxDxF, FxDxF family PEP-CTERM protein. This family of PEP-CTERM protein is named for a well-conserved motif near its N-terminus, FxDxFxF. A few members of this family have two full copies, suggesting two sites, rather than just one at the C-terminus, for cleavage by exosortase and covalent attachment to the outer membrane
LLLAAALAAAAAAAAASNTTTTLDLTGGAALWTTASFGATHTAGGTFTDTFTFTPSGGSGSVSASLVSIG
FSALSGLDFTSFTLNGGNGVSSGTQLSTGATDVWTLAPTGPLAAGPYTLTVSGTVLGSAGGSYSGTLNVS
PVPEPETYAMLLGGLGLLGFLARRR
>gnl|CDD|468370 NF038127, FDP_fam, DVUA0089 family protein. This family is named after oldest member mentioned in a publication, the plasmid-encoded PEP-CTERM protein DVUA0089 from Desulfovibrio vulgaris Hildenborough. Nearly every member has the PEP-CTERM sequence at its C-terminus (or a related variant), a single for recognition and processing by exosortases, and probably for covalent attachment to components of the outer membrane after cleavage and transpeptidation. This HMM appears to be related to PF04151.15, which describes a domain often found in the C-terminal regions of peptidases
QAADFSFTGNFAYDNDVVLFSFTLTAASTVVTLWTDSYAGGTNAAGAGGFDPILALFDATGTLIAENDDG
GSIGSQDDGDGGALDDSLLLTNLAAGTYTLAITQYDNFANGALLSDGFAFDGQTPIAFADWDGPQRGGAW
ALDITGV
>gnl|CDD|468371 NF038128, choice_anch_J, choice-of-anchor J domain. The choice-of-anchor J domain, about 160 amino acids long, occurs as many as times in a protein, although most often only once. Proteins with the domain include proteins with serine hydrolase, metallohydrolase, or adhesin-associated domains. Notably, many members are also found with either the PEP-CTERM term domain, or the type IX secretion system type A domain, both associated with protein-sorting system expected to leave target proteins covalently attached to the bacterial outer membrane
LLNEGFEDVGTLPAGWTIINNSGPGGTTWFQGNPGVFGAQSGAANSYIAANYNNAAAGGTIDNWLITPEL
SLGGATTLSFWVRAASSSGFSDHLEVLFSTTGGTDVADFTTLLLTTTGYPTGWTQYTVDLSAYAGGTGYF
AFRYVGDADTAGYIGIDDVSV
>gnl|CDD|468372 NF038129, PEP_NF038129, NF038129 family PEP-CTERM protein
RRALLALALAAGAGAAAAGTYHVSIDTSTLGGATGYLDLQFNGLGGAPPATATLSNFSGAFGGAADLTGD
VSGSLAGGVTLGNGTGFNDLFQAVNFGGVFSFDVTFSGDFDTSPGGSGSTFSVALYDADGNTYLGNDGAL
VQFNLTPGGAGGVGSVAADAAVSAAVSAVPEPSTWLLLGTGLALLGLVRRRR
>gnl|CDD|468373 NF038130, PEP_NF038130, NF038130 family PEP-CTERM protein. This family of PEP-CTERM proteins occurs in Cyanobacteria such as Nostoc, but also in floc-forming bacteria such as Zoogloea ramigera and Candidatus Accumulibacter phosphatis
KLLIGASVAAGVSAIAAAPAFAGSLTGATIGGPSDYLTYDSDGTNTFLVGNTNANNLAAVLDGNAASPGG
NVELFASSETADFTSNTTLTGTIGGKAITLSSLTATDWFSSYGGNTLASQWFNGALAANGLGGSLLTNNQ
LGAAVNAFLNTGGFQRFSDPNISYVNQDDTTGQISIGLAGHLDATPLLSALLAYVLDGLPGNFLNLVPPG
IQASEVVKVTYNGVTDYLYSFSATASGLVASDDGVSHTGNYEVSLPGVPPAAVPEPSVMLGLLGVGGLFA
TRR
>gnl|CDD|468374 NF038131, choice_anch_K, choice-of-anchor K domain. The choice-of-anchor K is a rather uncommon extracellular domain about 170 amino acids long. A substantial fraction of member proteins have C-terminal regions that target them for sorting to the cell surface, including PEP-CTERM, its variant VPLPA-CTERM, and LPXTG. The domain is found occasionally in RTX toxin-like proteins
SGSSSGTWSNPTPGSGNANPVVTGVGTNTFTWGVPVPGGPPSSLTFDGNSFSTVTVGTLFVLGTLTYFNG
TIYAGTSVSSVPLTLTVSFTSPANFDESFTFNFNLDNTPNTGDPPPDADTVSLGNSFSNLSFTFGGNTYT
LELLGFSQGGTFVSEFIVPEGGTNTAGLY
>gnl|CDD|468375 NF038132, PEP_NF038132, NF038132 family protein. Most members of this family, but not all, are exosortase-dependent proteins with a PEP-CTERM protein-sorting signal at the C-terminus. This HMM excludes a set of related proteins with an additional insert region that features a near-invariant LFTART motif
GWTCVGNCGTSGADGDVTLSPGGGSQYGYVSTAGGVTGVGLPGVGLGSETNGSRLTSSLFSANAGDTLSF
YFNYVTSDGAGFADYAWARLLDADGNQVALLFTARTTPGGDTVPGFGMPAPEATLTPASVPIIGGAPTWS
PLGGSSGTCYDAGCGYTGWIQSSYTIAAAGNYRLEFGVVNWSDTAFDSGLAFDGITIG
>gnl|CDD|468376 NF038133, choice_anch_L, choice-of-anchor L domain. The choice-of-anchor L domain, about 220 amino acids long, is an extracellular domain found often with a C-terminal cell surface, such as PEP-CTERM or the type IX secretion system (T9SS) type B sorting signal. It tends to be found only once per protein, but the family contains some members proteins over 4000 residues long
QLLANALVGSGVTISNVTYTGANSTAAGTFTGGGFSAGIGIDSGIILSTGNASNAVPNNSGGGGTNNGGT
PGDADLDALIGGTTYDAAVLEFDFIPTGDTLFFNYVFASEEYNEYVGSSFNDVFGFFISGPGIVNIALIP
GTGTPVSINNVNNGSNSAYYVDNDPGDNGNPGGYNIEYDGFTTVLTATASAVVPGQTYHIKLAIADAGDG
ILDSGVFIEAGSF
>gnl|CDD|468377 NF038134, choice_anch_M, choice-of-anchor M domain. This model represents a domain about 180 amino acids long, often repeated and sometimes cyclically permuted, containing a signature region described by TIGR03769 (which is just 41 residues long). Many members of this family have either LPXTG or PEP-CTERM domains at the C-terminus, for covalent anchoring at the cell surface by sortases or exosortases, respectively. Other member proteins that lack such C-terminal regions may instead have lipoprotein signal peptides at the N-terminus. The domain is duplicated in members of TIGR03773, such as CmrA2. The related protein TroA (see TIGR03772), with regions homologous to most of the length of this model, appears to have a function related to zinc uptake
VITKGHVDAIGPRLDDGKLSLGLKDDSGTTPVWRDPDDVVLRVGDAAKTTVPDDPAYAFLGKPGDPVWVL
PQTQDPGVLWPGWNTQDLPVGAFLDGGVTLDLVGVSGPGGVELFFQSGSFGGPQRLLDSGDGLPQSIWVE
AGTHTHANWVFTKPGTYTLTVRATATLKDGKTVSSEPQTLTFAV
>gnl|CDD|468378 NF038135, rSAM_Rv2578c, Rv2578c family radical SAM protein. This radical SAM family, which includes Rv2578c from Mycobacterium tuberculosis, is uncharacterized, but is notable in part because inteins are found in many members of this family. Although inteins are viewed mostly as selfish genetic elements, they occur often in important housekeeping proteins, such as RecA, in a way that suggests domestication of the element into a regulatory system in which triggering intein excision results in an irreverisible change to the host protein. Intein-containing members of this family are found by HMM NF038136. Rv2578c itself appears to be part of the SOS regulon
MRWDGQRLDADDGAALPGLERAGLVRSVRTPEFAGITFHEVLAKSALNRVPGASRMPFRWTVNPYRGCSH
ACVYCCFARPTHEYLDLDAGRDFDSQIVVKVNAAEVLRRELARPSWRREHVALGTNTDPYQRAEGRYRLM
PGIIAALADSGTPFSILTKGTLLRRDLPLLAEAARVVPVGLAVSLAFVDDELWRSVEPGTPSPRARLDLV
RALRDAGLPCGVLVAPVLPGLTDSPEQLDALVAAIAAAGATSVTPLPLHLRPGAREWFLAWLAREHPELV
PRYRRLYGRGAYAPKEYRRWLTARVRPLAARHGLG
>gnl|CDD|468379 NF038136, rSAM_Rv_intein, intein-containing Rv2578c family radical SAM protein. This radical SAM family consists of intein-containing radical SAM proteins related to (but not including) Rv2578c from Mycobacterium tuberculosisis. Rv2578c and its homologs are uncharacterized, but presence of inteins in multiple members of the family is notable. Although inteins are viewed mostly as selfish genetic elements, they occur often in important housekeeping proteins, such as RecA, in a way that suggests domestication of the element into a regulatory system in which triggering intein excision results in an irreverisible and situationally beneficial change to the host protein
MRWDGQSADADDDGALPGLPGGLVRTVRTPEFAGMTFHEVRAKSVLNKVPGGSRVPFGWTVNPYRGCSHA
CTYCLAGDTPILMADGRTRPLADLRVGDRIYGTERRGAYRRYVPTTVLAHWSTVKPAYRVTLADGTSLVA
SGDHRFLTERGWRHVTGAPPGEGARPPLTTGNRLLGFGEGPAPGPAYSPGYLGGLLGGDRTSGGSRRRFA
AGLRERTASARALASLFTSGAVTPLDEVTDALTRGWLAGFLAGRFDAAGFGRVLLGGDLERLLFFRHLTP
AVIARRDISGVAVRSDRRLAVSVIEDLGLELPLFDITTGTGDFIANGVVSHNCFARNTHTYLDLDAGHDF
DTQVVVKVNAPEVLRRELARPSWTREHVAMGTNTDPYQRAEGRYRLMPGIIRALADSGTPFSILTKGTLL
LRDLPLLTEAAEDVPVGLAVSLAFLDDDLQRSVEPGTPSPRARLDLVRRLTDAGLPCGVLVAPVLPGLTD
SAEHLDALVAAIAAAGATGVTVLPLHLRPGAREWFASWLAREHPHLVPRYRELYGRGAYAPKAYRRELTA
RVRPLLRRHGLD
>gnl|CDD|439452 NF038137, leader_TrpLE_al, trpE operon leader peptide TrpLE. This HMM describes a variant of the trp operon leader peptide, as found in Sinohizobium meliloti and other alphaproteobacteria. In Sinohizobium meliloti, tryptophan biosynthesis genes are divided into three different operons, and only the trpE-encoding operon is proceeded by a leader peptide, designated TrpLE. This family differs substantially from that of Pfam model PF08255. Melior, et al. (2020) describe an usual activity in trans, something not previously known for leader peptides, affecting expression of antibiotic efflux proteins
MANARNISIWWWAR
>gnl|CDD|468380 NF038138, phena_PhzG, phenazine biosynthesis FMN-dependent oxidase PhzG
SLTGDIDLDFPEFDAPPAEPLGLLRRWLEAAVALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVF
TTHAGSRKGRELAANPWASGVLYWRETSQQISLSGPVERLPDAESDALWAARPVATHAMTAASRQSEPLD
DEAALRAEARELAEAGGPLPRPARFVGYRLVPEEVEFWAAGPDRLHRRLRYDRDGDGWTHVRLQP
>gnl|CDD|468381 NF038139, Reg_Aceta_RamB, acetate metabolism transcriptional regulator RamB. RamB (Regulator of Acetate Metabolism B), as described in Mycobacterium tuberculosis and Corynebacterium glutamicum, is a transcription factor with multiple targets connected to acetate metabolism. It features an N-terminal XRE (Xenobiotic Response Element) family DNA-binding domain and a DUF2083 (PF09856) domain-containing C-terminal region
TYVGSRLRQLRRERGLSQAALAATLGISASYLNQIEHDVRPLTVPVLLRITEVFGVDATFFSRDDDSRLL
AELREVVLDRELDPSPVDLQELSELVYAHPTIARAMVDMHRRYRNVRDQLAAATDERFSDSGSGAISMPH
EEVRDFFYQRQNYLHELDTAAEDLTARMRFHIRDVERELADRLTDVHGVRIVRRVDLGGNVLHRFDPETR
VLELSARLSPGQRAFRMAAELAYLEAGDLIDALVDEGPFTSEESRKLARRGLANYFAAATVLPYTQFHGE
AEDFRYDIERLSAFFGVSYETICHRLSTLQRPNLRGVPFTFVRVDRAGNMSKRQSATGFHFSSSGGTCPL
WNVYETFAYPGKIMRQIAQMPDGRNYLWVARTVERRAARYGQPGKTFAIGLGCELRHADRTVYADGLDLD
DLAAATPIGAGCRVCERENCPQRAFPALGKALDIDEHRSTVSPY
>gnl|CDD|439455 NF038140, amidase_Rv3717, Rv3717 family N-acetylmuramoyl-L-alanine amidase. This zinc-dependent amidase functions as a peptidoglycan hydrolase, and affects septum formation, cell division, and cell morphology. Model proteins for this family include Rv3717 from Mycobacterium tuberculosis (MTB) and MSMEG_6281 from Mycolicibacterium smegmatis, a fast-growing laboratory surrogate for MTB
ALLVAASVLAAPAAPAAAANIAGKIVFLDPGHNGANDASIGRQVPTGRGGTKDCQTSGTSTDDGYPEHTF
TWDVTLRVRQALTALGVRTALSRGDDNSVGPCVDERAAMANALRPDAIVSIHADGGPATGRGFHVNYSSP
PLNDAQAGPSVQFAQVMRDQLVAAGLPPATYIGSDGLYGRSDLAGLNLAQYPSILVELGNMKNPADAALM
ESPEGRQRYADAVVRGIAAFLSA
>gnl|CDD|468382 NF038141, choice_anch_N, choice-of-anchor N domain. The choice-of-anchor N family occurs in both bacteria, with a PEP-CTERM sorting signal at the C-terminus, and in archaea with a PEF-CTERM sorting signal. Well-conserved motifs in the multiple sequence alignment include AxPxLQ near the N-terminus, and HFD and PxSHD near the C-terminus, the latter just upstream of the sorting signal region
AVPTLQLYIPGGTYDGTYDPTTETWVTTSDTFDLWVIGANGGNNTYYISGALLPGSFDFSGTGPSTGTTS
VAILDMSVGTPPLGSVTVGVYGDGGDLPPHGIFPTYYYEYDFGFFDLTDSPIGDFAPGSGGDAIGPGGGY
IKVFTVDVSGLYWVHFDAYGLNVKGNGKKTIIDFAPFSHDAT
>gnl|CDD|468383 NF038142, exosort_XrtW, exosortase W. Exosortase W is an EpsI domain-containing subtype of exosortase, a bacterial protein-sorting enzyme that is probably a transpeptidase rather than a simple hydrolase. It is most closely related to exosortase D, which is VPLPA-CTERM-specific. However, it is the sole exosortase in Candidatus Manganitrophus noduliformans, the nodule-forming Nitrospiraceae bacterium identified as the first manganese-oxidizing chemolithoautotroph. In that species, target proteins have the more classical PEP-CTERM sorting signal at the C-terminus
VLLQAALLIAAFLFLYADTLIWLVRTWWTYDGYSHGFLIPFISLYLVWTKRDRLRNLPVEPNYVWGTLLL
LAGLALLLAGRAGGIILLEELSLIVTIAGLVLLLLGTAYLKALAFPIGYLIFMIPVFDELLEPLHWPFQL
FTAWIASALLQLIGIPVLRDGQFIELPNITLEVARACSGVNYLISVLAIGIPLAYLTLRSWWRRIALVLS
AVVIGILANGLRVALIGIWAYYGKGEDLHGPYHIFQGSFVFFIGLVVLFLGAWLLSRGPAASVAGPLPER
SELSWPLVRAGKSINIAWLLALALLALAGLYLHFLKPQPVPLKSPLATFPTVIGGWTGQDADNSEGPFKV
PGADEELVRTYRDSSGREVKLYIGYFESQSQGKELVDYRSAPLHEGAEEIEIPLGGGTVEVNRTILSDGG
RRRTVLFWYDINGRIVTDRYLAKLATLLDAFVHRRTNGAIVIVSSELRSDDGEEAERNLEEFIKEILPVL
QGYL
>gnl|CDD|468384 NF038143, HYxxLL, NF038143 family protein. This family is uncharacterized
EKKELILEHEEQFARRLALAVIEKPKPSVWMILIPILFVFYFLRLKRYKEGLKDFAENFLFTRKLALDAA
LEAVETGEPREEELSQIEPDTKALLEKLGLYSEEIREKQMEEIELLIDHYLRLLNAEGDDYEALVRSAYR
SRGNYLLFLNRLNKAEKEVNQALLPTLGGDDEDAREVIEKMEEASERLRREEAERIF
>gnl|CDD|439459 NF038144, PxxKW, PxxKW family cysteine-rich protein. Members of this uncharacterized protein family are shorter than 100 residues, with four invariant Cys residues, including a CxGC motif. One branch of the family has three additional conserved Cys. Other notable motifs include PxxKW (for which the family is currently named), CNxATH, and NP[LI]KASKR near the C-terminus
ECAFMTKEGCSYNGGVCQPIVEKCEGCERIVEFEGGKYCTSYPDPAAKWRLGICNFATHVKAEIKKAKKA
KINPLKASKRA
>gnl|CDD|468385 NF038145, Hvo_1808_fam, Hvo_1808 family surface protein. Members of this family are secreted proteins from halophilic archaea. Essentially every member has lipoprotein signal peptide at the N-terminus, or else a PGF-CTERM sorting signal at the C-terminus, but not both. Both types of sorting signals are processed in such a way that, following removal, a lipid moiety left at the new terminus of the amino acid chain anchors the protein in the plasma membrane
DRLGWENGYWYNESLDVDQSDGLNESELEAVVARSMARVERIRGLEFEETVPVEVISRERFRNEERGGGN
VSEADRLFDNVKFEALFLVGEDTDAIEVQESNYGGSVLGYYSPSDDRIVVVSDSEEPPLVDELTLAHELV
HALQDQQFDLSGSYETTDDQLNARNGLIEGDANYVEYRYEERCGSEWDCLCPPDSGGGGGGGGDANLGLY
LLIYQPYSDGPAFVESLRERGGWEAVNAAYDDPPASTEQVIHPERYPDDEPTDVSVEDRSSDGWERLDVD
GRPDYATVGEAGLFAMFWYPSYDSGGESVVVPPEEFLNRALTGGEVDDYDPYNYDHPATAGWAGDRLVPY
VNDDGGENETGYVWKTVWDSEADAREFADAYRELLLYHGAEAVDGRENTYRIPDDGPFADAFRVTRDGDT
VTIVNAPTVDDLDEVH
>gnl|CDD|439461 NF038146, LxmA_leader, LxmA family RiPP leader domain. LxmA is the founding member of a family of ribosomally translated and post-translationally modified lanthipeptides whose lanthionine moiety is created by a novel class of enzyme. This HMM represents the leader domain, and the first four residues of the core peptide, of LxmA, its full-length homologs, and a number of other RiPPs that much lower sequence similarity outside the leader peptide region
EDLIAGYDAYTDAEELAAEAAADAPATTPT
>gnl|CDD|439462 NF038147, lanti_IV_venA, VenA family class IV lanthipeptide. Members of this family include VenA, precursor of the class IV lanthipeptide venezuelin, and all detectable homologs
ENFDLDLLAELQALPETDPVEVDGAQFGGTCACLGLLTLLNTVCVGITC
>gnl|CDD|439463 NF038148, lanti_IV_SflA, SflA family class IV lanthipeptide. SflA is the precursor peptide of a RiPP biosynthetic gene cluster (BGC) designated "sfl", for the Second-most abundant class Four (IV) Lanthipeptide
MPVAVLDIRDAGPLDIDDEAIAFEDDDDADREPTACLADPWVTATTRFACDL
>gnl|CDD|439464 NF038149, leader_PheL, pheA operon leader peptide PheL
MKHTPFFFAFFFTFP
>gnl|CDD|468386 NF038150, lanthi_synth_IV, class IV lanthionine synthetase LanL. Several classes of lanthionine bridge-producing peptide-modifying enzymes (lanthionine synthases) have been defined. LanC enzymes are class I, LanM are class II, LanKC are class III, and LanL are class IV. Members of this family are the class IV enzyme, active in the maturation of class IV lanthipeptides, a large fraction of which act as lantibiotics
WTVRPDDFWCRVTPPGGTRRAQGWKLHVSATPASAPEVLARALPVLLRHGCAFKFARSLEQLRALNSRRT
DRGSVGKFITVYPRDDEQARRLAEELHRATAGLPGPRILSDRPYRPGSLVHYRYGAFTGRRRLGNDGLYE
WMLTDPDGNPVEDRRTGWYSPPPWAVDPFPAPPAPAPPPAAGPAPVLLGGRFAVREAIRHSNKGGVYRAV
DRRTGAPVVIKQARPHVGADASGRDARDRLRHEARVLEALAGLGLAPRPVDLFEQGGHLFLAQEEVPGVT
LRRWVAERLRYRGDGGPPRADALALARRLVDLVAAVHARGLVLRDLTPNNVMVTPDGELRLIDLELAARP
GDLVTRVGTPGYSAPEQLAGAPPAAPPTADLYSLGATLFFLATGLDPVLLDDEPAARPVNERLALWLLAA
ALPGPAPRALAPLILGLMADDPARRWDLARARAALAGPAPPAAARLPPAAPDRLLVDGLDHLVATMTPDD
DDRLWPVSAPFGGETDPCNVQHGAAGVLAVLTRAAELTGDPRLREAVAAAARWIARRLRTEPRLLPGLYF
GRAGTAWALYDAGRALGDPALADRALALALALPVRWPNPDVTHGTAGAGLAQLHLWRRTGDPRFAERAVA
AADALLAAAAPPEPGGVSWPVPEFDSALAGARHLGFAHGVAGIGYFLLAAAAATGRTDYLELAVAAGETL
LALAVVTGGAAQWPAGAPGATPRAPHWCSGSAGIGTFLVRLWQATGDPRYLDLARRAARAVRRLAWRAGL
SQCHGLAGNGEFLLDLAEATGDPRYRDWAEELARLILARRAGRDGRLVFPDETGADVSAGWNTGLAGVLA
FLLRLRHGGPRLW
>gnl|CDD|468387 NF038151, lanthi_synth_III, class III lanthionine synthetase LanKC
YEAYCLADPLFYDTPDRYSAAAPDFAAALRPVPEGWRRHRSGDWTYLRPPGAELPEQGWKIHVSATLDNA
EEVLDAVWDYCVERGIAFKFLRSPRLLLLRNSKYADRGSSGKFITIYPADEEQLERLLEELDALLAGEPG
PYILSDLRWGDGPLYVRYGAFAERYCVDEDGELVPAIRDPDGRLVPDRRGPYFQVPDWVTLPDFLEPHLA
ARNADTLSGLPYRIESALHFSNGGGVYLATDKRTGRKVVLKEARPHAGLDADGRDAVARLRREREALERL
AGLGGVPEVIDYFTVWEHHFLVEEFVEGRPLNSWLARRYPLTRADPDPEALAAYTEWALRILRQVERAVA
AVHARGVVFGDLHPFNIMVDPDGSVRLIDFEAASPADEDRRPALATPGFAAPRDRTGFEVDRYALACLRL
ALFLPLTPLLDLDPGKAAHLADWIAERFPVPRAFLDEAVRELLGPDPPEAPAPEALPALPPEPPDWPALR
DSLARAILASATPERDDRLFPGDIAQFETGGGLGLAYGAAGVLYALHRTGAGRPPEHEEWLLRRALRPPP
GTPLGLYDGLAGIAWVLDELGHREEALDLLDRALDEPWERLDPDLFSGLAGIGLALLHLARRTGDPALLD
RALRIADRLADRLGEDAPGSGGDAPRAGLLHGWSGVALFLLRLYERTGDPALLELAERALRRDLARCVTD
EDGTLQVDEGWRTLPYLGGGSAGIGLVLDEYLAHRPDERFAEALPGILRAATSRFYVQPGLFRGRAGLLL
FLARLTAPGDPTAREELARQLRGLALHALPYPGGLAFPGEQLLRLSMDLATGSAGVLLALG
>gnl|CDD|439467 NF038152, TrpL_Coryne, trp operon leader peptide. Member of this family are tryptophan biosynthesis operon leader peptide TrpL, as found in the genus Corynebacterium. It differs substantially from Trp-rich leader peptides documented in other lineages, such as in the gammaproteobacteria
MNNPCLSQSTQWWWRAS
>gnl|CDD|468388 NF038153, lant_leader_L1a, class I lanthipeptide leader domain. This HMM describes a homology domain found regularly as a leader peptide, ending with a GlyGly dipeptide (a leader peptide cleavage site), of putative lanthipeptides (probably lantibiotics in most cases) encoded in the vicinity of a class I lanthionine synthase, or LanC. The designation L1a reflects model construction for class I lantibiotics (L1), first in a possible series (L1a), from the lanthipeptide RiPP collection found in PMID:32493223. Because the leader peptide may reflect constraints on cleavage and export, it may be expected that some members of the family undergo modifications other than lanthionine bridge formation, or no special modifications at all
MKKKKKLNKKLSLNKETIAKLNEEQLKQVKGG
>gnl|CDD|468389 NF038154, lanthi_III_a, class III lanthipeptide. This family of putative class III lanthipeptides, here designated family lanthi_III_a, averages about 44 amino acids in length, has a strongly conserved N-terminal ten amino acids including an invariant motif LxLQ, and usually has Cys as its final residue. The designation III_a indicates that it is the first family defined here from the collection of putative class III lanthipeptides reported by Walker, et al. (PMID:32493223)
MNEVLELQKLEEDTEVKGQAITWTTTVGLSTISNHC
>gnl|CDD|439470 NF038155, lanthi_I_FDLD, FDLD family class I lanthipeptide. This HMM finds a broad collection of putative class I lanthipeptides with a well-conserved motif FDLD near the N-terminus, and poorly conserved but typically Cys-rich core peptide regions. Some members belong to the more narrowly defined family of gallidermin/nisin-like lanthipeptides
DDFDLDVQVSAEESSPGATSAITTTTICTTVTC
>gnl|CDD|468390 NF038156, lant_syn_V_LxmK, class V lanthionine synthetase subunit LxmK
VPEVDALLERLGLGPFDPDTLTAFPGRNDNWAGTTTSGRRVFVKRLVGPPEDVAARFRRLLAFERLAAPG
GPLRTPRLLGADEEAGLLVFELLEDARSGAELAADGEFDDELARRAGRALGALHALPPPPAGELDTSPPP
LPPVGLLEALPLEVFLEASAAELEAWRLLQNDAELVAALRRLREREAAAPRVPVHGDLRLDQFLVADGRL
YLTDWEEFRLGDPARDVGAFAGEWLYRAVLDIVTTRGDAPGPDAELTHEEILARGAEELERLRPLIEAFW
RGYREARPAADPGLAVRATAFAGWHLLDRLLAAAESRARLSAIERAAAGIGRTALLAPARFAATLGL
>gnl|CDD|439472 NF038157, lanti_ALQxL, ALQxL family lanthipeptide leader peptide. This 17-residue leader peptide region HMM identifies a family of lanthipeptides that average 40 residues in length, with typically 3 or 4 Cys residues C-terminal to this region. Most members of the family are classified as class IV lanthipeptides by proximity to class IV lanthionine synthases
MELDVDALQLLPAEEEQ
>gnl|CDD|439473 NF038158, lant_leader_L1b, class I lanthipeptide leader domain. This HMM describes a homology domain found regularly as a leader peptide, ending with a GlyGly dipeptide (a leader peptide cleavage site), of putative lanthipeptides (probably lantibiotics in most cases) encoded in the vicinity of a class I lanthionine synthase, or LanC. The designation L1b reflects model construction for class I lantibiotics (L1), second in a possible series (L1b), from the lanthipeptide RiPP collection found in PMID:32493223. Because the leader peptide may reflect constraints on cleavage and export, it may be expected that some members of the family undergo modifications other than lanthionine bridge formation, or no special modifications at all, but amino acid composition of member proteins C-terminal to the leader domain suggests that all are lanthipeptides, and probably act as lantibiotics
KKQIKKLEIKKDDILNLSKNNAQNVIGG
>gnl|CDD|439474 NF038159, lanthi_III_b, class III lanthipeptide. Members of this family are class III lanthipeptides, most likely active as lantibiotics. They average about 43 amino acids in length, with two conserved Cys residues, the second of them often appearing as the final residue. The family lacks the GlyGly motif that many other RiPP precursors have as the cleavage site between leader peptide and core region. The designation III_b indicates that it is the second family defined here with no characterized member but with members in the collection of putative class III lanthipeptides reported by Walker, et al. (PMID:32493223). The family has some overlap with the SapB/AmfS family of class III lanthipeptides (NF033212) and with the lanthi_III_a family (NF038154)
NKVLSLQKLEAKEEVELHAGSSLSVNCKKSSTISLFFC
>gnl|CDD|439475 NF038160, lanthi_III_c, class III lanthipeptide. Members of this family are class III lanthipeptide precursors of unusually small size, 36 amino acids long on average. Most have a Cys-Cys dipeptide pair not far from the C-terminus. Members lack the Gly-Gly cleavage site that many RiPP precursor polypeptides have between leader and core peptide regions. The designation III_c indicates that it is the third family defined here with no characterized member but with members in the collection of putative class III lanthipeptides reported by Walker, et al. (PMID:32493223)
MSVLKLQSLEPTTTESAVALSSLTSSSSDCCNT
>gnl|CDD|468391 NF038161, lant_II_LchA2, class II lanthipeptide, LchA2/BrtA2 family. Members of this family are class II lanthipeptide precursors. Most members have three Cys residues in conserved positions among their last 15 amino acids. Named members include lichenicidin A2 (LchA2) and the birimositide beta chain, BrtA2
DPLGKVDENELKELAGAGDVNGGTTPATTVAIGVAVSAALCPTTACTSKC
>gnl|CDD|468392 NF038162, RctB_rel_intein, intein-containing RctB family protein
RLKKISDYVWELPKDYKDGMRVPGRIYASEKLLDELEPDALEQAANVACLPGIYKYSIAMPDVHYGYGFP
IGGVAAFDLDEGVISPGGVGYDINCLTPNARVLTEHGYYIKIEELPEKGDEPLKIYNTEEGHNESSRIAF
VFERTPDEKAIRIWTEGGRVLEGSEDHPVLTPQGYVPLKELKEGDRVAVYPFEGVEYEEPSDEIILDEDD
FPDYDKQIIRYLKERGLLPLRYDDKKIGTLARLLGFAFGDGSIVRERGGRLRLAFYGRRETLEEIRKDLE
SLGVKASRLYSRRRRHRIRTVYGEYASECEDVSLRVTSRSFALLLHKLGMPIGKKTEQDYRIPEWIKKAP
LWVKRNFLAGLFGADGSKPVFKGYTPLPINLTQSKSAELEENLREFLEDIARLLAEFGVETTIYEVNSLL
GSVRYRLAIVGEENLRNFLGKIGYEYNREKKELGLLALAYLKYKEQVKEQRKKAVELAKEIYEEGVSEIE
RARRLAKEDINRRFVERTIYENLGDTPRVPDNFPSFEEFIKERGNGGGFVWDEIVKIEEVEPPYDRVYDI
GVDHKDHNFIANGIVVHNCGVRLIRTNLTKEEVRPKIKELIDTLFKNVPSGVGSKGILRVSKQELDDVLV
EGARWAVKEGYGWEEDLEFIEENGRMEGADPSAVSDRAKERGAPQLGSLGSGNHFLEVQYVEKIFDEEAA
KAYGLEEGQVVVMVHTGSRGLGHQICSDYLRIMERAARKYGIKLPDRQLACAPFESEEGQSYFKAMCCGA
NYAWANRQMITHWVRESFQEVFRMHEEDLGMEIVYDVAHNIAKKEEHTIDGKKVKVIVHRKGATRAFPPG
HPQIPKEYRSVGQPVLIPGDMGTASYVLVGTEIAMKETFGSTCHGAGRVLSRAKAKKLWRGDEIQERLLE
RGIIVRAASKAVMAEEAPEAYKSVDLVVEVCHRAGISKKVARMRPLGVIKG
>gnl|CDD|439478 NF038163, bactofencin_A, bactofencin A family cationic bacteriocin. Bactofencin A (BnfA), a class IId bacteriocin from Lactobacillus salivarius, is a disulfide bond-containing 22-amino-acid defensin-like peptide with a broad spectrum of activity. Precursor forms for BnfA and other members of the family average about 49 amino acids in length, with the core peptide starting immediately after the GlyGly motif of the leader peptide
KKNIKKAFKHNRISDKDLAKVMGGRKKHRCRVYNNGMPTGMYRWC
>gnl|CDD|439479 NF038164, garvicinKS_A, GatA family leaderless bacteriocin. GatA is one component of the multipeptide leaderless bacteriocin designated garvicin KS, as found in Lactococcus garvieae KS1546
GKKIIGGTAAWLGWEAGERIWK
>gnl|CDD|439480 NF038165, garvicinKS_B, GatB family leaderless bacteriocin. GatB is one component of the multipeptide leaderless bacteriocin designated garvicin KS, as found in Lactococcus garvieae KS1546
MGAVIKGGAKIIGGGAAGGGGTYGLEKIFG
>gnl|CDD|468393 NF038167, cyan_ocin_like, CTB family bacteriocin. Members of this family, which average about 85 amino acids in length, resemble class II bacteriocins. They show N-terminal sequence similarity to bacteriocin leader peptide domain TIGR01847 and lack Cys residues (enriched in lanthipeptides as well as disulfide-forming bacteriocins) almost entirely. They are undoubtedly cleaved at a GlyGly motif while being exported in the manner of bacteriocins, as they are regularly encoded next to homologs of families TIGR01193 and TIGR01000, involved in bacteriocin cleavage and export. Because multiple family members can be encoded in tandem in a single genome, such as the set of six in Cylindrospermum stagnale PCC 7417, we name the family CTB (Cyanobacterial Tandem Bacteriocin)
MSNEINLFVELSEEQLEVVAGGADFELNATNFAQKNLVLQGATSSGPNGSTATSNGASTEINTAALKFLG
LG
>gnl|CDD|439482 NF038168, phazolicin_TOMM, phazolicin family TOMM bacteriocin. Phazolicin is a ribosome-targeting thiazole/oxazole-modified microcin (TOMM), also called a linear azol(in)e-containing peptides (LAP)
TQNLNPPQFGTEIEFVDGGDAAGVQTAAACARCDSSSRCGASGKSSGSSSCVST
>gnl|CDD|439483 NF038169, lachnocin, lachnocin family radical SAM-modified peptide
KKVNLKKINKANNSTVRTLDCHCGCEGKPVSAVGDGYVGQFL
>gnl|CDD|439484 NF038170, lachnocin_rSAM, lachnocin radical SAM maturase
MYLSKIIKTKNNVYIYDALNNNFATINSEDDILDDNKYKDFLRDNDFRDIKKPCEFKIKYPYSKEELNNM
YKSKVKSMTLALTEQCNLRCKYCGYMPKYMDDNYKLKEMSKEVAFKAIDILMKNSHESEVCHIGFYGGEP
LLRLDLIKECIDYIKEKYPFRKPTYNITTNAVLLDDKVADFLIENDIKIIISLDGPTEEQNKYRVFGNGE
SSYERVFKNIQALYRKDPKYFRENVTYNVVMYNGASNELFESIDNLWKSNVNMIDLFPTEYFAKVRDKSD
EECKNEKIDVKKYDFAYKNMLKGMKKYYNSFNGSAGGNTILPGGFCIPGVRKNFVTTDGKIIVCEKVDES
KEVFEIGDVYNGIDINKVNRLVDETLKSLEKCKHCWAAKFCKICFKDILNINEEFCEKSRKDVERELGYY
LEQVSNDRDLINYVANISLI
>gnl|CDD|439485 NF038171, maturase_LodB, lysine-epsilon-oxidase maturase LodB. L-lysine-epsilon-oxidase (LodA), which acts on free lysine and produces hydrogen peroxide, contains a cysteine tryptophylquinone cofactor. LodB, usually encoded next to LodA, is the maturase required for formation of the quinone moiety. Note that a related system consists of cysteine tryptophylquinone-dependent glycine oxidase, GoxA, and its maturase, GoxB
DVLIVGGGPAGASAALSLLNYSNLKVTIIEQSDLNTTRVGEHVSASIFDLLDYLKIDKSDFEEGSFIPGY
GSTAYWGSDKPSSRHSIFTTEGATYQLDREKFDLTLLEQVAERGGTIFPRTKCLEFEQLEDGGWLVQLSH
PTKGKFTIKARYLVDATGRQSSVCRKLGAKSKKYDQLVGVGAFLEFDEDTTLEQEQLIESVEEGWWYSAA
LPNQKMVVTFFTDADIISEQKLNKAENWNRLLSQTKHIKKRVKGATSLGDKLWVRNAFSQISDFSTIKNF
IAVGDAAASFDPISSMGIGFAMSSACHAAKAIINYLTSEGDNTLDLYQQDIERIFDQYLQLKQQFYQKEQ
RWPDSPFWQRRH
>gnl|CDD|468394 NF038172, Lys_ox_CTQ_LodA, CTQ-dependent lysine 6-oxidase LodA. LodA converts free L-lysine into 6-semialdehyde 2-aminoadipic acid, ammonia and hydrogen peroxide. It has antibacterial activity because of the hydrogen peroxide produced, and was originally named marinocine. The enzyme depends on a cysteine tryptophylquinone (CTQ) cofactor, formed by post-translational modification by an accessory protein, the maturase LodB
TLSIHPSVGVARLGNSPTQFCLSPDQIGGLPFEADANGNKLGPIINFKDAAGQVKRQGQPFKIYDEDGEE
LTLDSPNVASIEWTVHLANKKAAWYQYSELKGNLLYGEENSYTNQGVPFRNPNVTGESDRQTLIIDPGPR
TISGARQSIGFDRANVPAGYPVSYPPEKVTYGTPITTLGDLKTDDQGRLIVLGGYGHAGGNEPLTSYGGS
DTWHDDISDGPVYCTVTFNDGTPPITLQAWVIVGSPDFAPEIVNISTLSDTMFDVGVRHFNLVPEMYSNG
TWNTSYVANYQRDILPIIQRISRYQWVANVQSMMAFTSNIFDFSDPSEANKANRENYFSYFRQPDDKPPV
SPDQPQQQLFKENGEDIFPMMPLNSGSNSVSNINIEKFLALDETQYFLLGQWAEGKFVNDPNYEPYPVNP
MDQASVGNCVGLPMCPGIEVTWSLQNPVIYAAPYVIKDQKGENGYNQTGLTPSRDECEGGGCEPGDLTKR
MACPWQADFFQCTIQYVNFTDPTVNKETGTTTTEPVPLPPTYYSYWWPPQSPWDVLTGELTAEGQAASHL
PAGQQVNYARGINSFVQMVEHWSALAFIRDQNAGDPGFPYFVETERNNELFSYKEVPVGQISGNPEDNET
TIPVFYIEDNKQKVKEKSERAKLLVEFLEERAFKPIAVAPEGLGLPRSGTRNRR
>gnl|CDD|468395 NF038173, Gly_ox_CTQ_GoxA, CTQ-dependent glycine oxidase GoxA
KRRDFLAGAGAGAALAGLPLLAKAAIAQTPAAEAAPAGAKIARLGIYPAIGICRVGGSPEWFLAPEVPGL
PPQPEGGFKDGTQKIKKQVQRFRVYAFDDQDRVIGEITAGDATIEWSVHVANTKAAWYGFNNPLDNGELA
PGLPGQKRNQYFVSDEQRERMLVIDGGPKTISGRDTNLDGGDPAYAMVGRFWGSEDVGLGHLRTDDAGRL
LVFPPDGVSNSPTGAPITSFADNDGWHDDWCDGPVTATVTLADGRVLEADPAWVACVGPNFAPEIPPITT
LYDVIADMNVEEGWTPPPALPLSFRKYIYPTFRRLALMEWVTAAANLRQGWLDVGDFSDPAYIARLADPS
PANAAFRQSVFAKFRNPYNDSPTAYKEERLKIPYMLGDGINYDGSPLQWFQFPKLQYEFLKAWAAGDFVD
DLDDDAADAVETLDDIPLELQPAALTEAALEPCSGGAFHPGVELTYYLRLAPMYARNYDPTAEPFRIAHG
DRPSLVQNLGRLLTPEKAFEGYGGTPPPIGPQMPGDLTRWMGLPWQCDAFSCQQVLMQEDFPTAVWWPAL
LPIDVLPEEYYEQLMREDLSAEERVKFFENRVAWARGVAGIGYHANASYWDGITNMITLWERMGFVVKRP
GPTDPGRPEGIPRELYVEVGRGNMEFRFDWTPADGQLP
>gnl|CDD|468396 NF038174, maturase_GoxB, glycine oxidase maturase GoxB. GoxB, a flavoprotein, is responsible for the post-translational modification that forms the cysteine tryptophylquinone (CTQ) cofactor of the quinone glycine oxidase GoxA
ADVAVIGGGIAGAAACLALAQAGLSPLWIAPEPATGDKPGESLSPAANPLLAALGLADLLDAPVHRPANT
TFSAWGSDQLVERNAIVHLEGPGTVLDRAAFEADLRALAAAAGAERVEADLADLAARGDGGWRLTLEDGE
QLSARFVIDASGRKAVVARRLARRFRADRLVAAYAFLAQQDSDVEPTPATLIEAVEDGWWYASLLADGRL
VVNFYSDPDLLPRGLTRDLAAWRALLAETRYISRWIDDAGFGLSAPPRLASAGTTWLAPAAGAEGAGWAA
VGDAAAAFDPLSSHGMTTALWTGIRAADAAAAALDGDRAPLAAYADAVARGVQDFLTQRARIYAREKRFA
DSPFWQRR
>gnl|CDD|439489 NF038175, IniB_NTERM, IniB N-terminal domain. This domain is found as the N-terminal fifty amino acids of a number low-complexity proteins that often bear little or no similarity to each other elsewhere in the protein. The domain occurs twice in Mycobacterium tuberculosis strain H37Rv, in two adjacent proteins, Rv0340 and the isoniazid inducible protein IniB (Rv0341)
SLIDFILSLFRDPDAAAAFVADPEAALAAAGLGDVTAADVQAVAPLVAD
>gnl|CDD|468397 NF038176, Rv0340_fam, Rv0340 family protein. Homologs of Rv0340 from Mycobacterium tuberculosis H37Rv are regularly found encoded upstream of the genes for IniB, IniA, and IniC. As with those families, mutation in this family can contribute to resistance to isoniazid, a front-line treatment for Mycobacterium tuberculosis that works by inhibiting cell wall biosynthesis. Rv0340 and glycine-rich repetive protein IniB are homologous across the N-terminal 50 amino acids of each, but otherwise dissimilar
MANSLLDFVMSLVRDPDAAARYAADPAQAIADAHLTDVTSADVNNLIPVVSESLSMAAPAGGADAGAPAA
DHGNVWASGAATAAFDAFDDHVPAAVVDQHGPVGGVIDQPAAPAPDDAPADPQPLGVDLHDPSVQLTGPE
IDDPAVDHGAFPADDPADWDHPVIDDHDLDPDHHGFDIF
>gnl|CDD|468398 NF038177, epimerase_AlgG, mannuronan 5-epimerase AlgG
LLSALLLGALLLASGAAQAAVPAQPEAPRQLAKELQQAKTYTVTSAPIEPLEMDPPKLPDLSGYTAAAVE
KKIVRKPGGKISVARMMQETALKEFTGGDNKLAEWVVRQHGIPQAIFIEDGYVNLGQLAKKVPKQYLSEV
EPGVYVARLPIVVGQGGILEIDKKVKELRLSQERGAFLVNDGKLFVTDTKVTGWSEKNNGPAAYRTPKEF
RPFLLSWGGTETYISNTKMASFGYNTSKSYGVSISQYTPNMAKRLKRPEPTGWIIDSEFSDMWYGFYCYE
TDDFVVKGNTYRDNIVYGIDPHDRSHRLIIAENTVYGTKKKHGIIVSREVNDSFIFNNRSYDNKLSGIVL
DRNSVGNLVAYNEVYRNHTDGITLYESGDNLLWGNRVIANRRHGIRVRNSVNIRLYENLAMANGLTGVYG
HIKDLSDTDRDIALDPFDTKVSLIVVGGELSGNGSGPLSIDSPLSVELYRVSMLAPTKSSGISLNGVLGE
RQDEILDLLVRQQKAVLIDPVESQTELQD
>gnl|CDD|439492 NF038178, AlgP_Nterm, AlgP family protein N-terminal domain. This HMM describes the conserved N-terminal domain of a protein that has extensive lysine-rich repeats in the C-terminal half, typically PAAK, and is called histone-like for that reason. Some reports have called AlgP (also called AlgR3) a regulator of alginate biosynthesis, responsible for a mucoid phenotype in Pseudomonas aeruginosa, but recent work casts doubt on the specificity of the connection to alginate
SAKKKPVTTPLHLLQQLSGSLLEHLEKACSQALADAEKLLAKLEKQRGKAQEKLHKARTKLQDAASAGKA
KAQAKARAAIGELEELLDLLKARQSETRTYIAQLKRDAQESLKLAQGVGKVREAAAKALASR
>gnl|CDD|439493 NF038179, stress_YobI, stress response small protein YobI. YobI, as found in strains of Escherichia coli and Shigella sonnei, is a hydrophobic protein of very small size, 21 amino acids, whose expression increases after heat shock
MYIFITHFFTEYVIFKYLLPI
>gnl|CDD|439494 NF038180, leader_pinensin, pinensin family lanthipeptide leader domain. This family of class I lanthipeptide leader peptide occurs in Gram-negative lineages such as Chitinophaga pinensis (for which pinensins, antifungal lantibiotics, are named), Fulvivirga, Longimicrobium, and Pedobacter. Most member sequences contain the motif SFVT, and the leader peptide ends with a typical GlyGly motif
KKLKLDDLKVESFVTSLDEEESNTVKGG
>gnl|CDD|468399 NF038181, reg_ATPase_IniR, isoniazid response ATPase/transcriptional regulator IniR. Two unrelated first-line drugs for the treatment of tuberculosis, isoniazid and ethambutol, block different steps in the biosynthesis of the Mycobacterial cell envelope, and induce expression of the iniBAC operon, mutations in which often lead to adaptive resistance to those drugs. IniR (iniBAC Regulator), an ATPase but also a transcriptional regulator, with an N-terminal P-loop motif GGxGxGK[ST] and a C-terminal LuxR-like helix-turn-helix DNA-binding domain, responds to the envelope stress signal and induces IniB, IniA, and IniC
LPPAAREAVAALEADPTAPVKLLVTGGIGTGKSTVLAAVRAALRAAGRPVLTRPPRPGDPPEAAVVVDDA
HLLDDDELDRLTELVADPAATVVVAAEPLAHRPALRALATALERENPAVSLGPLPPAEVSRAAAAALGAP
PPPELVRALLSATAGLPFLLRPALAAAGDPATAIRQAARFALIERLRRLDEPTLDTLLVTSLSPDLGPDD
VAAALRISADDALALVDRARASGLIEPSHPPAFLRSVHDAVAQIVGAARHHDIEISLLVSQLELSTLSAD
LALRLAEHGLRDDRLATALTDLAARTRGQPARAARLYRAAADAGATALSARLADALALTGDCATAGRLAD
DLLTSPDPAERAAAVRIAASVALHDGSAAQAADLFRWLGPYPDAVVGAAGTIVALAAGDAAAARATLQTE
SAGPPTSTARAARSLAEGLLLTLDQPYPVAVARLGQAIAADQPATRVLPDTPAALVTLAALHGGDPVRAR
SVIGRAVRAGARDGPADAAFVTRRHRLLLGWVRMQDGQLPAAAADVAAAAAGGLHRRDALWAAALQTAIA
RRSGDSGAMQKHWYAAMEVLAEYSVDLFSLLPLGELWVAAARMRQVDRLRHTLDEAFALLDSLGDPVLWS
VPLHWAGVHAGILANSPEAVAPHGQALTAAAAHSPFAKALATAGRTWLRVLANHVDVDEVTAAARGLAQF
GLTWDATRLAGQAALQTSDARVSGAMLQLARDLKQSVAADEAPAPEAAAAPVAAPAAAPARPPAARLSDR
EREVAELLLLGMPYRDIGAQLFISAKTVEHHVARIRRRLGAESRSEMLSMLRAMLAP
>gnl|CDD|439496 NF038182, penta_rpt_SmQnr, SmQnr family pentapeptide repeat protein. The pentapeptide repeat protein SmQnr is a chromosomal homolog of quinolone resistance proteins QnrA and QnrB, found in Stenotrophomonas maltophilia and related species. Most alleles appear to contribute little or no resistance to quinolones, but some exceptional alleles to reduce susceptibility
MSPTVHRKLRIGADQYTGQKVVDQQFHECDFSGADLTATEFINCSFYDADSRTGCRFNGATLKEASFRSC
DISMCHFNFIKALGLEISECRAQGADFSNASFMNQITTRSWFCSAFIKKSNLRYANFSRVTLEKCELWEN
RWDGANVSGASFAGSDLSGGQFEGIDWNSANFTDCDLTNSELGELDLRSTNLRGATLDVQQVALLMQRIG
ITVVP
>gnl|CDD|468400 NF038185, KdpD_non_kinase, KdpD-like non-kinase potassium sensor. Members of this family contain the N-terminal sensor region, but lack the C-terminal histidine kinase region, of the sensor histidine kinase KdpD found broadly in species such as Escherichia coli, Mycobacterium tuberculosis, Clostridium acetobutylicum, and Staphylococcus aureus. Members are found in Bacillus anthracis and related species
FRRRSPEELLREIEKQKRGKLKIYIGAAPGVGKTYKMLQDAHELKKEGIDVVIGLVETHGRKETEEQIGD
LEIIPLKEIPYKGKEFQELDVEAIIKRNPQVVIIDELAHTNAPGSKNKKRYQDVQELLDAGISVMSAVNI
QHLESVRDIVNQITGVKVRERIPDFILQKADEIQLVDVTPETLRKRLREGKIYSPEKIEQSLNNFFTLGN
LSALRELTLREVADDVDDRLEKYRNKGVVGPIGINEKILVCVQYRPNAEKLIRRGWRMADRLKADLYILH
VYNEEELLSEKNKKKIKEWQMLANQFNASFIVEEAKSRKPAQVIIEVAKQNNITQILLGQSARTRWEEIR
KGSIVNAIMRQTKNIDIHIVADS
>gnl|CDD|439498 NF038186, YPDG_rpt, YPDG domain. The YPDG domain may occur once in a protein, or up to 22 times in tandem repeats. It is common in proteins of Gram-positive bacteria with C-terminal LPXTG sites for anchoring on the cell surface
ESYEPSYEDGTVKPGETVKVPAPTFKDKDGKAVDVPEGTKFAPGDAAPEGWTVTVDEDTGEITVTAPEDA
KPGDEVTVPVTVTYPDGSTDEVPATVTV
>gnl|CDD|439499 NF038187, FadE_coli, acyl-CoA dehydrogenase FadE. This HMM describes a narrow clade of medium-chain and long-chain acyl-CoA dehydrogenases that includes YafH from Escherichia coli K-12 and Salmonella enterica LT2 (also called FadF), now called FadE
LLSILAMLVLLGALAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPFLIIALPLNVPSIRQSLISAPA
LKAFRKVMPEMSSTEKEAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDF
QITHELADLPPEVWQYLKDHRFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGEL
LQHYGTEEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDFGVVCKGEWQGEEVLGMRLTWNKRYITL
APVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDIFVPLDFI
IGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQFKLPIGKMEGIEEPLARIAG
NAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNFLARGYQGAPI
AITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDSEQALNDFDKALFGHIGFVGSNLVRSFWLGL
TNGRFSSAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRY
EDEGRQKEDLPLVHWAVQDSLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKIL
QTPSATRSRLGRGQYLTPSEHNPVGLLEQALKDILAAEPIHDRVCKAAGKRLPFMRLDKLAEEGLALGVI
TEEEAALLERAEASRLRSINVDDFDPDELAAKPAKRPAKQKQDEAA
>gnl|CDD|468401 NF038188, cas13A_C2c2, type VI-A CRISPR-associated RNA-guided ribonuclease Cas13a
MKITKVKGRSVAVKKGKRYKDPGKLVLNLEDKSDGEKNIDLPDFLFSKDKLVIAQWKSILDKIIKKPKKY
GKKKKNKEIKKLRKKLIGKAIWELLTKEIKLKKLIDDAIIKLLKKKWRRKLKPYKIGKKKFELPDVLKGR
LYKVFGDAKSWDIDEAELKEIAEAIKKHLNEKKKRIVKSIENNKIVLQPEEDGGFLIKESISKRKEALAE
FLLDYANEEGRKELLWKLRDLAVYYFYGDLAKEIKEKFDVTIAKELKIDKEIKKKLKELAGRILKEHIRK
IFIEHYRRAEKSIEDEKKNLLFFYHKEVKKYYKHYFPIKKKKILKKKELERLLPLNKGYLSEKVWKQLKN
RLLNKLIRLGKLVHYFADDDDIWPGKIDEANSRGWTSFDQEEIKANEAFVREWRTAVAFAANTLRNWVDP
ENNIDEDILLKKKFKEALKKNTIKNEFKEKILLFFGGRLDEFDDKDKDDIEELLWAIRKSIYSLRNESFH
FKTKARFLKALENGGFEVDKYNDELLKKLFEKDIEKIKDREKEKLYSNNVPLYYSEEDLEKILEKLYSEF
NKRAPQVPSFKRVLKRGDNLQKSDDYLKLLKYFNRLDEEKEKEALSAQYYLLKLIYYNPFLPWLQKNKEL
FKDYIDRALERNKKANKKKNARKAKKNFKKAIRELQKEESLSDYLQYLQAEYAQENRVQRGYKSDREQAR
EQAKHYEDFLCDVFAKAFDDYLKENGFDFILEPKPSKTEEKKEEFLPFLKSVELESLIEEIKNEDWLIAL
YLLLHLLPVKELSELRHQLRKYRQLVEKIERRAKETEKIELLEKLLEVLELYLLMHDAVFNEGKDYFEDE
EEYAEYLKLFVDFELFDNLEPSSFYVQEDGKNPILNRNIRELKRYGTLGLLSKIFKKHKVTKKEIEEYYE
LENKIEEIQKRQEELHEKWEKKKKKGLEEDDKEYQKALRKIARYNWLKNKVELNDLVRLHRLLMDLLGRL
VGFSGLWERDLYFLLLGLLYLKNNSPEDVEGYKKLRNNKKTKIDGFFNAILYQIVAMYNNKLPSVGAKIK
DFEKVYINYFEKEHDNIVDIRNYIAHFNYLRNPNDDSSLTEYINRLRRLLSYDRKLKNAVTKSIIEILLR
HGLILKFKMKDGGNHKLKIASLKSKKITHLGKKDLKKIEEPAVSEEYLEMVAALL
>gnl|CDD|468402 NF038189, VI_Cas13d, type VI-D CRISPR-associated RNA-guided ribonuclease Cas13d
KKSKAKAAGVKSVFVIGDEVYMTSFGRGNDAVLEKKIDGDVVSNLNIDSPAYDLPEVTKKNYGISKKNGH
ERGPVKVTTANPRYRAVPRKPVGEDMLGLKPKLEKLFFGKTFDDNIHIQLIYNILDIEKILAVYVTNIVY
ALNNLSLDGSEDNKDLIGYLSTRNTYDEDPEKSNESDDNKKKLEAQFDNFDKFIENKRLGYFGNEKNKEE
KDKREEEEEKKLYHILALLGMLRQWTFHGKEGDRETWLYNLDKNLDYEFRKTLDKLYNEKVEEINKDFIK
NSKVNIQILCEIMDAESIEKKKLVRDYYDFIILKEYKNLGFSIKKLRETMLDRYGYAFKEYIKDAKYDSV
RQKLYKLMDFVIYDYYINNDKERAEEIVDKLRSSKNDDEKENIYKKEAEKLWEKLRNVINSIKDFMNGEK
IKKLSKKNIDIKSSYIEDISIDSIEDNADYFCKLIYLLTRFLDGKEINDLLTTLINKFDNIRSFIKVMKE
LGLECKFTEEYKMFEDSKKIAKELRIINSFARMSKPIDANAKRTMFRDALTILGISDKTKDLENLLDTIL
DLKENGLDKKRHGFRNFIANNVIKSNRFKYLIRYSNPAKVRKLAKNEKVVKFVLSKIPDEQIDRYYESCS
GKSSEGCSVEEKRKKLTEKITGINFDDFENVKQYSKATPEENEDKEKKKAIIRLYLTVLYILVKNLVNVN
ARYVIAFHCVERDAGLYGETIDECKKKDKKKDYNGIDKLEFPKLFAEEKYREETYLPNEKVGDYIKKNLE
NSDDKTVREYRNNVAHLNVIRKVPEYIKDIKDINSYFALYHYIMQRIIFNECKEREEKSEKNGKLINYLE
NVRKHHTYCKDFVKALNVPFAYNLPRYKNLSIEDLFDRN
>gnl|CDD|468403 NF038190, VI_Cas13b, type VI-B CRISPR-associated RNA-guided ribonuclease Cas13b
LEEDKHYFGAYLNLARHNIFIVLNHINKKLGIKEKANDEDLKKIITLLFKDNKSPDDYEKLIKLLKKYFP
FLKYFDKESKNKKEKKEKKNKEKDLEELKEILKLLLEALNDLRNYYTHYYHKPITIEEELFEFLDDIFDA
AIRLVKKRFVKEDKDFEHLKRKLKEELDKLIKLKAFNYYLYKDKNKNTLTESGLLFFLSLFLEKKEAEQF
LSKIKGFKGKVELKFKATHEVFTYLCIKLPKDRLESDFTKETLLLDMLNELSKCPKELYQTLSEEDQEKF
IEDINEYDKDNEEDNSDEESEVEHPVIRKRYEDRFPYFALRYLDEFELFPNLRFQVDLGNYVHDRYKKTI
GGETEDRVIKKKIKGFGRLSEFEKLKPDYFKKIIDLDDKEDSYIEEFPPHYHFENNKIGIYINNDKDKIW
PSLKKERTKNKKKKYKLIKQPKPDAFLSINELPALLFYELLKKKKPEGKKIEEIIKDKINNQKKFIKAFA
EGKKISKEQLSKKLRKKKILNVSHLPKKLIDYLLNIEKDEIEKAEEKLKEMKEDTKKRLEKLRKKKKKRK
KKFKNPKIGEIATWLARDIKRFQPKDKKKKWTGYQYSELQRALAYYGERKKELIALLRELNLIDGSNPHP
FLKKINFEKCNNILDFYKAYLEEKKKYLEKLLKELKNKNIYFLKLKIKKKEPFKLFKKRLYQLKNLETLK
NNLLKKPINLPRGLFDEKITEILKKKLKENKEEFKKEAAADWIKLYFKEELKDDYQPFYNWPRNYELFDK
LKEFLNSEEREKLWKELKELEKVYRFKKKKREKIKKTKRKLLPEEEKEKEKKSILKNEKKIRLIKIQDRL
LFLMAKDLLKKLFNNLELSLSELYKLREERPENEADKSNNILNENFIWSKTITLYLGNGKITIEKVKLKD
YGKFRRLLKDRRLKNLLSYFKDDEWAESLSKEEIERELEEYERIRRELFKEIQELEKKILDKFPDELEKE
DLKKNGNPNFKKYLVDWLKKKGLINEFNEDKEELELLILIRNKFSHNQYPMKEIYELFQKYPKIIEEKNG
ETIAEQLLELFKEIINE
>gnl|CDD|468404 NF038191, V_Cas12k, type V CRISPR-associated protein Cas12k. Cas12k is the large effector protein of type V-K CRISPR systems, which belong to the class 2 systems. Cas12k has also been known as C2c5, and type V-K as type V-U5
QITIQCRLVASEDTRQHLWQLMAEKNTPLINELLKQVAQHPDFETWRQKGKIPKGVVKQLCKPLKTDPRF
AGQPGRFYTSAISLVDYIYKSWLALQKRLQRQLEGKQRWLEMLKSDTELVEESGCSLETIRAKAQEILSQ
LESESEQSTQPDKKKKKTSKKKKKSSSSKSLFDILFDAYDETEDILTRCAIAYLLKNGCKVPEKEEDPEK
FAKRRRKKEIQIERLEEQLESRLPKGRDLTGEKWLETLEIATQQVPEDEEEAKSWQAQLLTKSSSLPYPI
LYETNEDLTWSKNEKGRLCVRFNGLSEHTFEIYCDQRQLHWFQRFLEDQQIKKASKNQHSSSLFTLRSAR
LLWQEGEGKGEPWNVHRLYLHCTVDTRLWTAEGTEEVRQEKAAEIAKTITKMKEKGDLNDNQQAFIKRKE
STLARLNNPFPRPSKPLYQGQPNILVGVSFGLEKPATVAVVDVSTGKVLAYRSIKQLLGDNYKLLNRQRQ
QQQKLSHQRHKAQKKGAPNQFGESELGQYVDRLLAKAIVAIAQQYQAGSIVLPKLGDIREIIQSEIQAKA
EQKIPGYKEAQKKYAKQYRISVHQWSYGRLIENIKSQAAKLGISIEEGKQPIRGSPQEKAKDLAISAY
>gnl|CDD|468405 NF038192, V_cas_c2c8, type V CRISPR-associated protein C2c8
KTLEFKLYLNKEQQAKIDRWLDSLRWVWNLGLGLLEEFDQFTYWDKLSKTLVPCCPLPWDYRKDETEDRG
ELAPFERLARTKPYRKSCPIPKVYRNPELETPNKFGLIYYFANSEKIDKPWFCYVPAKFVAGTLKSYIKK
AILDVPPKFRTGTLSSLATAWQEYKKGKRGKPKFKRYRDKIKSLVNNNPNAIKIKPANNNQLVLPKLGKV
KVKGLDKRWDKSPRVRTLKIVKEPSGYYLQLTGEVPREPFKPSNKAVGIDPGLKYLLTTDDGKVVEPPRY
YRKSEKKLARLQRKLSRQQKQRPISWYNHPLREHFLIKPIFPGGGANQAKTQKKIAKLHEKIRRQRRAYN
HKLSTKLVREYGAIAIEDLKIKNMTKRPKPKKREDGKGYEQNGAKRKSGLNKSLLDAGLGQLITLIEQKA
KANGREFIRVKPKYTSQECPQCGHRDKKN
>gnl|CDD|468406 NF038193, VI_Cas13c, type VI-C CRISPR-associated RNA-guided ribonuclease Cas13c
KKSNRNSIPKIIISNYDSKGIKEIKVKYEKQARLDTFEIKTMEKDEKINIEFIECKIKAREKYRYSFEID
GKIKFSKTNNTILILKKDGKIKKTFKEIRKYVITLKVKEKKKRLVEAKIKDLLESNDLRDGERNKRRRKS
STERKLLSETVIKNYSQISGCPVEEIDSKKIYKIKRFLSYRSNMLFYFAFINNFFCKGVKNKKNEIWKIN
DKDSEKEKLVEYIKYTLNDSIKNYRQSLNNYIEKKEKLKKEEKSDESIKEDFEKIIKIFSDLRHALMHYD
YKFFENLFENKKNEEFDLKDLLDLNLFKSLPLIRKLKYENKTNYLEDDETITVLGKNINAKKLYTFYNKI
CEKKNGFNKFINSFFVKDGEENEEFKEYINEKFEKEMEKLEKYIEKIKLLKKELDEMKKHRLWLNCAYFI
DIHSSKEYKKLYNERKKLVEEQNEQINEKKDKQKIKQINDKLLELKKEMNEITKQNSLYRLEYKLRLAFG
FLMNEYNGNIKKFKDEFDSDNNEKIKSYLDKGEKYLNYKYEKKKKKNFEKIDKDIFKIIETETLLELVEE
NNLFKFYLLTYILLPKELKGDFLGFVKKHYYDIKNVDFDDKDKEEKLEEMKNDSFFLKLRLFEKNLKKLE
IFKYSISTNELYKKYFELFYEDGNYFGKEYKGLEISHNQGEFNKNLILPIFKYYQILFKLLNDFEIYALL
TLANKKNINFEKLLVLVKDKNSFRGYYNFSTLLKQIFNRLTKNQKKNEEIAQLRNKIAHLNYKNLLKELL
NNEININEQRRKIIKFIEENGLMKIELGYNFINDFYMKKEQLLFNQKQKKSLNVSSEKQQKNDKIEELLK
KYDLTPNDFYNIYK
>gnl|CDD|439506 NF038194, AlgK_TPR_lipo, alginate biosynthesis TPR repeat lipoprotein AlgK
APPLLLLALAIALAGCAGLPDQRLANEALKRGDTATAEQNYRQLADLGYSDAQVGLADIQVASGDPAQLK
QAEATYRAAADTSPRAQARLGRLLAAKPGATEAERREAETLLKQAFAAGEDSTLIPLAMLYLQYPQSFPE
VNAQQQIDQWRAAGYPQAGLAQILLYRTQGTYDQHLGEVERICKAALASTDICYVELATVYQKQGNAEQQ
AALLEQLKAAYKAGRVPAQRVDSVARVLADAELGQPDEKTAQALLEEIAPTYPAAWVSLAKLLYDYPELG
DTEQMMEYLDKGRAAAQPRAELLLGRLYYEGKWVPQDPKKAEEHLLKAAASEPSAHYYLGQIYRRGYLGK
VYPQKALDHLLSAARNGQNSADFALAQLFSQGKGIRPNPVNAYVFSQLALAQNTPQATELAQQLEQQLPP
AQRAQAQRLLRQERAARGALWQNTLALQ
>gnl|CDD|468407 NF038196, ferrodoxin_EFR1, EFR1 family ferrodoxin. Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1)
IFYFSGTGNSLYVAKRIAEELGDELISISKAIKEGDFKLKEDEPIGFVFPVYAWGLPRIVEDFIKKLKLK
GNKYIFAVATCGGSIGNALAQLKKLLKKKGLKLSGGFSIKMPNNYIPLFDVPSKEKAKKILKKAEEKIKE
IAEKIKNRKKGPEKKKGFIPRLLSKLVNPLFYKFKVKDKKFHVTDKCIGCGICAKVCPVNNIEMEDGKPV
WGHNCTHCLACIHRCPKEAIEYGKKTKKKGRYH
>gnl|CDD|468408 NF038197, prim_adj_arch, primase-associated protein. Members of this family are found exclusively in Archaea, always adjacent to a DNA primase-like protein
PVDDERAAYRVAALPDEYGESEINQLFTRGYDRYIVDGEDQPEDLLADIERFGTAAFDPSVRTKAAEEPF
VDDPATLAVLATLSAICIKAHPKFENAPPRKIQLLYDIRELYVNNLLSLLREYGDQTLQQEIAEVLYAKE
PGEDGPHPGRVCTGITEMPEFGEGLYLEIPMAAASRKCLARFHNGPDTNEVGGEILTHVKDNHLYVPVSH
FDAKYREYAKEAFKRLLRVQEDSLSEDQQQWLTNNESAITERIDRFIETGHHERIWTDWDPGERLLRLLR
NAIKDADDLQIGEFHTAEELYEAVDAYDPEGFWERQVCRRISSPRSLANSLADHREHRSVTIRRDRRTNT
YRIGRSSGGYKQITVDELEDLFELPCFANMDERLHEKKPVRKDLFNFVRMVMWLPQYQDSSLDAIVDDLK
DLFSRWPWYDEETTDYQIRYELSNTIGGNTPLPMNCDNDDMQRYCIGKDQCPYSIYGSLPFPDEMYDQLD
ESDSV
>gnl|CDD|468409 NF038205, Campy_LoFi_RPT, LOFI repeat. This weakly conserved (low-fidelity, or LOFI) repeat appears primarily in Campylobacteria, but not exclusively, in proteins such as Cj0967, Cj0736, and Cj0735. The HMM models a core region about 23 residues in length of repeats whose lengths vary typically between 35 and 50 residues in length
APFLVGGYALKGNANNNKLILKK
>gnl|CDD|468410 NF038206, RGCVC_fam, RGCVC family protein. This family of small proteins, averaging just over 60 amino acids in length, has conspicuous motifs CxxCxH, HD, and RGCVC. The last motif, for which the family is named, is distinctive. The family appears in GC-rich bacteria. The function is unknown
MTSPTPTTPDAPTEGAAEDTCPVCPHPWAAHDPIAARFCTATAAGGLDRGCVCR
>gnl|CDD|439510 NF038207, glyco_res_GraF, glycopeptide resistance-associated protein GraF. GraF was discovered as a small stress protein expressed at higher levels in glycopeptide (vancomycin, teicoplanin)-intermediate strains of Staphylococcus aureus. Overexperssion leads to a thicker cell wall, and reduced sensitivities to glycopeptides and oxacillin
MSKEDLNKKAAEKAKEVEEKLKDQKEEATDDIEQTKKDIQDTLD
>gnl|CDD|468411 NF038209, mft_etfA, mycofactocin-associated electron transfer flavoprotein alpha subunit. Members of this small protein family are putative electron transfer flavoproteins, related to FixA from E. coli and EtfB from Methylophilus methylotrophus but clearly forming a distinctive clade. All members occur in species with a mycofactocin system. Mycofactocin is a small molecule redox carrier, synthesized from a pair of amino acids in the ribosomally translated peptide MftA, with aid from the radical SAM enzyme MftC, in a pathway analogous to the biosynthesis of PQQ
MLAVVVVRDGVLPLGADEAVAEAGGAALVVGSGAREAAGELTAARRVWTAETGPGFAPGALAAALAPLLA
GVPLVVLPASPDGRDLAPRLAAALDRPLLAGAVRVGADGAELSRWDGRVLVTVTADGPFVATLLPGVRGA
EPVADPPETELPLPVVPAPDVPDAEVLEVLEPDPETADLAEARRILGAGAGLVRGGELDGPAAFALLGEV
AAALGASVGATRVVTDAGWAGYERQIGTTGVVVDPDLYVAFGVSGAAQHTGGLGAPRHVVSVNTDPSCPM
TAMADLGIVADAPALLRELARRLG
>gnl|CDD|439512 NF038210, GMC_mycofac_3, mycofactocin system GMC family oxidoreductase MftG. This model describes a set of dehydrogenases belonging to the glucose-methanol-choline oxidoreductase (GMC oxidoreductase) family. Members of the present family appear to be restricted to the genus Dietzia, and occur in the context of mycofactocin biosynthesis genes and mycofactocin dependent oxidoreductase genes
VVVVGAGPAGCVMARRLAEAGADVLLLEAGTERATTRAGLLDIGPGSRVVTRHRATLGDTALELPRGRTL
GGSGAVNGGYCTPARPSDLAAWGPDWPRRYAVGLARAAERLRPRLAPMGPVAARVAAAFPGRVSAIAQAR
RDGRRVTAFDAWDPAGAGVRVRTGAAVRELRWAGGRVGGRCDGVVLDDDEEIAARQVVLCAGTIGTAALL
LGSGIGPATGHPVGHSVQEHPELLLDLPADPARGADPGPRGDPDAHGGLPPLLSHVVRLTLPGPRGVVEI
EVRPYAVPMHRVIPGLEPQPHRIGVALMNPVGRGRVRGDGTVDLADDPHDAAALAEAAGFVADRLGIDGD
PTRSTSQHLSGSARIGEVLDDSGRVLGVEGLRVADASVLPSLPRCGPYYTVLAVAEDLAARVVAERAW
>gnl|CDD|439513 NF038211, MFT_alt_reg, mycofactocin system transcriptional regulator MftR2. Member of this family bear almost no resemblance to the mycofactocin transcriptional regulator MftR (TIGR03968), but occur in the equivalent position, next to the start of the mycofactocin biosynthetic gene cluster and transcribed divergently from it. It is found primarily in the genus Nocardia, but also in a few species of Rhodococcus
LSESEIVEAALRVVREDGVEKLSMRRLSRELGVSPMAPYYYVADKRELLDLVASAALAGVRTPPPDSGPW
QQRLRDLIDQIDEKLRKHPGLGDILIEQMLGKQLDLIAAVMEILFDAGFSDRNVLAAYATIHTYLFGRSR
VNPRDRTAPPDVVLPEAVARATEYLPDLRGKYSYDFGMEVLIAGLEAQLVRQQ
>gnl|CDD|439514 NF038212, argG_rel, argininosuccinate synthase-related protein. Members of this family are related to, yet distinct from, the argininosuccinate synthase ArgG
IRSIEDLEFIADRTKHVLTLFSGGLDSSYLLYLLSKSGFAKVTALAVDLGEGIDEEELQQITDHFGAELI
IIDAREAFVEDAVLPAIQAQAKYLGLYPISSSLSRPIIARLAVELAAELGCDAILHTANQSQNSLRRLNG
AIEQLGFSGFYGSPYEYSAITREEKAAELSAAGLDGFKSRGVSGDSNLWCREFESGVLDDPEDFTVPESL
FTWTRWPPAPQVPDQISITFRGGIPVALDGQPLPLIELIAFLNHRVGAYGIGRYVGLEHLDGGEKVLEVR
EAPAAALLMDAYRHLETATLDAELIREKIHLEQLWVREAVEGRWFSTLKAASEAFIAHTAEKVSGSVTYR
LSRGSALARSIVADAPLYLRDRDLWEKQAAR
>gnl|CDD|439515 NF038213, SDR_TniO_fam, SDR family oxidoreductase
NGRIAIVTGATSGIGRATARALAEAGARVVGNGRRADRLAALAAEIAEPGGAFLGVAGDAGDEEVIDKLL
DAALRAFGGPPDIVVVNAGRGLGGSVLDSDLSQWEELLRINVLGAARLMRAAAQYMVESQKADFPRQAAD
IVVIGSVVGRNISPFSPVYGATKFAVHSLAEGLRREVCPKGVRVTLVEPGIVVSGFQEVAGYDMELFAKF
EEEFGPLLEGEDVAEAIHFVVTQPPHVHINDIMIRPTRQ
>gnl|CDD|439516 NF038214, IS21_help_AAA, IS21-like element helper ATPase IstB. This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements
LRQLKLPGMARALEELAEQAAREELSFEEFLALLLEAELAERENRRIERRLKRARFPAAKTLEDFDFTAA
PGLDKAQIRELATLDFIERAENVLLLGPPGTGKTHLAIALGYAACRQGYRVRFTTAADLVEQLAQARADG
RLGRLLRRLARYDLLIIDELGYLPFSREGANLLFELIADRYERGSTIITSNLPFSEWGEVFGDPTLAAAI
LDRLVHHAHILELKGESYRLKE
>gnl|CDD|439517 NF038215, acineto_lipo_PV, NF038215 family lipoprotein. This small lipoprotein, about 60 amino acids long on average in precursor form, is widespread in the genus Acinetobacter. The motif PVxxxDY is conserved in most members. The function is unknown
KKLSIVLSVLLLLLLTGCDAKDDLNKPKTEVRTMIIGGMPVYDQDYKLSDLQAAA
>gnl|CDD|468412 NF038216, ABZJ_00895_fam, ABZJ_00895 family protein. This family of proteins resembles transporters in their extensive hydrophobicity. The actual function is unknown, but family member ABZJ_00895 was one of a number of proteins whose expression was reduced signficantly in a lab-generated, colistin-resistant lpxC disruption mutant of Acinetobacter baumannii (see PMID:28275586)
LRYYLVFFAVYIALTLVLGVLAALLGIDLGSSALTIIPLMAAAMIAGQKFVKREGRAPTSGEKWRLALGA
TLIALLLSLVLVLALLLLLPGAAALLLAPLGLGILLIVLAVLLLIYLLLNRLFYGFGAKNALKA
>gnl|CDD|468413 NF038218, IcmG_DotF_IVB, type IVB secretion system protein IcmG/DotF
MADNDQYNDEYQFADLDSLSPDPMGEEEPASESAPSKAGKRFGGKNIRRNALIAVGLIVLAMLGYKFLGS
FFSGKSTSVDAPPTVPPVTQTATPQPVPTTPTVTPPQPVQPPPVTEDNPQLNQKLSALEQSQQSLRSEVS
SLNNQLGGINSNVNNLNAQIAQLNQTITTLSAQVEQQSEEIAVLTVRTKPKPVKRVVRKVPPRPIYYIQA
VIPGRAWLIATNGSTLTVREGTKIAGYGVVKLIDPNQGRVLTSSGQVIRFSQQDS
>gnl|CDD|439520 NF038219, IcmV_IVB, type IVB secretion system protein IcmV
MKKKSGSRIVKIFKSIFNVRAWFDWDRMKSFTLYLGNGFKRLFVPQKKVQGESFEEAMARLNLTEADLLA
KQKALFRLSILMLAAAFLIFGYAIYHLFYGSYRAFIVSLVVMLIALVLAFRYHFWYFQIKERKLGCTFKE
WYRQGLLGE
>gnl|CDD|468414 NF038220, IcmT_TraK, IcmT/TraK family protein
WRDTARPPRFFIIDARACFPILLFLFHWRWWTLILAIVGIVFFGVLSRFGLTLPVALRLLRRWLAGPRRP
ARPWWKRRRF
>gnl|CDD|468415 NF038221, IcmJ_DotN_IVB, type IVB secretion system protein IcmJDotN
MAANQELKLMASPGSWRLFSARKADERFKAFEQKVFQRDRYTCQFCGFQARLYQEVINLDGNYTNNRLSN
LVTACCFCSQCFFLESVGVGGYGGGTLIYLPELTQAELNSLCHVLFCAITNDTGYKSSAQNIYRSFKFRS
QIVEEKFGEGTSDPAILGQLIIDSGANSPELKDKIFKNIRLLPSRAKFRVQIEAWAASALEEL
>gnl|CDD|439523 NF038222, IcmW_IVB, type IVB secretion system protein IcmW
MPDLSHEASAQYWKEYGDPNIYRVLTFMESVEDWTIDGDPELEDALVELGEALDDIDAVDLLELGDEDEF
IRLVNYLKSSRMLRLLQALDTVHPGSASRLLIHAEELSKSSNDSAGLFLKRNILFERLRLLSRVFSSER
>gnl|CDD|468416 NF038223, IcmN_DotK_IVB, type IVB secretion system protein IcmN/DotK
CKRDGYVPLDNEDPKLPCKVAGASDAAIIKMQKKLNKRGVKVITIGQDYLISIPAAALFADQSPRLTWAS
YGLLNEVACFLKQFRKVAVNVTSYSSKYVSPKREHALTLARARAVADYLWSQGIDSRFIFTEGLGSDKPI
VAFTQGGDKSPNSRIEITFRDAVA
>gnl|CDD|468417 NF038224, OmpA_like_CmpA, C-OmpA-like family protein CmpA. Proteins of this family are one of the six L. pneumophila proteins containing an OmpA-like domain. It has been reported that CmpA was important for efficient intracellular replication of Legionella pneumophila
MSLKSSKGRLAFVGLLALLLSGCFHPPYNNFKPYNRAYRTTAPGAGVGTAAGAAAGGTVGGALAGTAIGG
AVGAAVGLYKDSKPAIIKELQKQDIQYVQYGDTMTLIVPTDKYFMFNSPRLNELCYPGLNNIIRLLKFYP
CSPIYVAGFTDNVGSRYHKKKLSQARAETMLTFLWANGIPAQRLKAEGYGDKNPVSDNKLIHGSAQNRRI
EIQWFNSCATPAAAPQPYIGYTK
>gnl|CDD|468418 NF038225, IcmX_IVB, type IVB secretion system protein IcmX
MKLLSKLVLPNLLLLASFPASADDSTPYYYQQQTSTNMQKLVQYLQNLGQYLGYDLTQSPTSNNPQGFSQ
TLLNLNTAQLAQLYLFNTFLGAIPVNTASSQALSQFVPSNIPGASTLNALANTTFKSNYSSPSSSSGNVS
VSPLIDQQPYQQDPVSQAVLNILGTPDYSYCMNNDGTTWIPNCSYLYQNLVMQNVIGTLPGTTTFFTYSY
NQPFLSQLNSNSLIAPLLYSTQSSGSNGTSSSSGNGQNQGLTAQNQAQQAANFIRYASGAVVPISLPKRS
DYDNLYSQATNTSGSTTDLQQQQAQATLSNYLASLRTYAAQTSVGISNLYYILSKRLPQNQSGQGGSSTP
TSQALSEFNMATWRLYNPDQSGGSGQGNTQWINQINTASPATVQKEIAILLAEINYQLYLDRQQQERILL
TNSILLLQNARAGQPS
>gnl|CDD|439527 NF038226, IcmF_IVB, type IVB secretion system protein IcmF
MDKSLQALCDALKKILSQLKPQNNALSFLLLTGKNSQGKSALLRQSNLEHYPVDSEQHAKIYYNQQGIIV
ELGESWLNQSKNLLQNTLKQLNRCHRNLKISGLILCVDINELLLAEPVQLAEQCKSHAQLLERFGSALGY
QVDLALLFTKLDTLAGFCEFFQSEHASDLSKPLGFSLDCSNQRKKKIEAYRQQFDQLIEVLGQQVINKMH
PARSSVKRTLIREFPLQLASLRAPIQSLIQNISPQLFRLQAIYFTSAEQGGLSVDRLNKKIQHEYALTVQ
DTFPQATNYRAYFIEGAIKAFQEQTKRHPPQRSFSQKPLIGLAAGLAGLSLLWLSYQHFKTSHLLDEASK
ELLAYETLLSQKNNKAQALYHLSRAANKLDHIPSNSLSLPTVHQLKTQLHNNTKHRLHGNFLPSLLAELE
QVITDPSQTPIARYQALKIYLMLGEPEHFSEAEVTDWFKQYWQAQPPENLQKQLALLKQALKQPMQPIAI
NQQLVSDARNYLNALPASYLYYSLAKEYFPQEKQKIAIEGFDLATKELPVYFTKAGFKEVIAQLPKISAQ
LQAENWVLARQDLSNLQAQLEQAYCFEYVTWWQNFIRRSQPLHYQDYQQARQLTQTLQQTNAISKLITLI
QQQTSPDLTENSSLFNQKIASQFTDLNLMSLSATKELSQNINELEKFLTTLSVVNDQGKTAFTLTRARFQ
GESLSDPLSTLYNRARQLPEPVSSWAKQIADDTWFILINDSRQYINQQWQQTVYNEYQNTIANRYPFDSS
QTEEVALADFDRFFATHGTLNTFVENYLKPFLDTSSAQWQPKEVNGYVLPISSDTINELIRANVITNMFF
PDQGEESKIEFSLQKINLDPVVANLQLEIGNTKLTDNQNSESFTRFSWPQSNAKLALNSIEGNHYELEEQ
GPWAFFKMLQKVNVLVDEQDSSSLQILFEVNGNSGRYLLKTQNQINPFTPGILNGFTLNEEIA
>gnl|CDD|439528 NF038227, IcmM_DotJ_IVB, type IVB secretion system protein IcmM/DotJ
MSRETWNLIKNSKSFYVNTYRRGLTFLIISLVLNLILGLLIYYLYFNQPERDFYATSGITPPVKLTPLDT
PNYSSTALLPPDPPNDDENKVIPQ
>gnl|CDD|439529 NF038228, IcmH_DotU_IVB, type IVB secretion system protein IcmH/DotU
MAAEHQSASLVNRLSLPGPHKMPQGYYRSKLFIAPFTTNPLVAAAGPLLSLLERLRVSPSLPNVPGIREN
IEHELKAFHSKLRSLGYPEELIAIARYLLCATIDELLGKSYLRLYGEESEFKAFTPLSHDETGPGERFFD
ILNRIKERPNQYLDLLELAYYCLILGFEGEYHEKADGRQVLDNLIEDLYQLIRQYRVNKSHRLFKEQPNP
KNTKKNYKPLWAVTIVAVGLLILTYLVSHVLLENKAKTVQQGHTVIAK
>gnl|CDD|439530 NF038229, Glyco4_Geo_Pelo, GPMC system family 4 glycosyltransferase. Members of this family are family 4 glycosyltransferases of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family
RILIITPYYQPPVTGNAVTVRRIARHLEQLGHEVRVLELDALDAAEILAALRQFRPDIIHAFHAYRSGRV
WLELARALGIPYLVTLTGTDVNEALDPDRRPETLRVLRGAAAIVAFNPLVRERLGQHLPPLAAKLVVIPQ
GVELGGEPFPLRELGLFDSDEFVFLLPAGLRPVKGVLFLLEMLAPLHAEDPRLRLAFAGPVLDEEYAAAF
FAALARRPWARYLGEIPHDAMGALYRRADVVLNNSLFEGMANALLEAMALGRPVLARDIPGNRSVVRPGV
TGLLYRDEAEFLRQARQLLQDPALRRRLGRPGRQLVRERYSPEREAEAYLRLYRAVLA
>gnl|CDD|468419 NF038230, Regu_Geo_Pelo, GPMC system transcriptional regulator. Members of this family are family are sigma 54-interacting transcriptional regulators of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family
DSQLKQLIEKINAYGKENLEEILHVLAEGVRLLTGQSRCRIYLEDLTSGALSCAAATGPNAAELRERSFP
INSSEFLVSRVYVSQEPLQFEDMDTSSSPLDRELAERFGIRASYLLPLVHQGRSIGVLCVDSSRPGQLPS
GKQRQQLRQFLTQVAPRLDQARKYHQQLLLARRVDEAKKREAALFMVKSAVRLIDKLALASVLVPSPAGE
DGEEGLQILASYSEEPELKKLYEDEGLISLGPGTSLLSRYIDDDGVIVDDRLLEPLYIPDLASETLQKRY
LTEELGLKSLYVVPRYEPRTRRVICLVNYYTRELYRFSEFEKGLLEAHAEMAERVIQEIGGEHLEIQVLS
EINDLLQERFEGLQPFLTRVLSKATELIGADTGSIALVREREGERWLVVEDEDGTLVGAKNKEWLKKNIP
PIRVGGEELPPEERSLTGYVAHTGQPKIIGDTDEEKQNGGFYRSMTELIKSEIAVPVICDDEVIAVICLD
SLRPHYFTEEHKRILQIIERMIARHISDLQRIEKLTGEVNRLRSDVGYKDPKVSSYRLGNIIGNSRKAQE
IVEFIQTVTPPLFNRIALWSQNVLQEATLGLPSILITGETGSGKEFLFNNLYSRLNEMYREQLNPRGELP
VKKTNIAAYSGELTYSELFGHKRGAFTGAHADRKGILEEAHGGVVFLDEIGDADPKTQVQLLRFLDNGGF
VRLGENQTRFSRVLLVAATNKDLRQLIAEGLFREDLYHRLSELTIEVPSLNERREDIPDLAVHFLGKLYR
VYRGPEETEEDPPILSEDAKQLLVQHHYTGNIRELRSILLRALFFRRGRVITGEDIRRALAGGGAGSESA
AGSAEELAGQLADEILERIERGEDDFWSAVYEPYSRNRISRDVVRLVIERARSRGARSMPRVARYLKACD
PASDDDEERKRFFKFKNFLYKTIRI
>gnl|CDD|439532 NF038231, MBL_Geo_Pelo, GPMC system MBL fold metallohydrolase. Members of this family, distantly related to metallo-beta-lactamases, are MBL fold hydrolases of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family
KITILGSGTSTGVPMIGCHCPVCRSTDPRNKRTRCSALLSWGGKNILIDTSTDLRQQALREGIPHIDAVL
YTHAHADHVHGIDDLRGFNFLHRRVIPCYGSAATMAQLRRNFSYIFRGEEGAGYRPLLEPHPISGPFDLF
GLRVVPVPLRHGAMEATGYRIGPLAYLTDCSAIPEASLELLQGLELLVIDGLRFRPHPTHFNIEQAIEVA
QRLGARRTILTHLSHEVDHARDGAELPAGVEFAYDGMQLS
>gnl|CDD|468420 NF038232, STM3845_fam, retron St85 family effector protein. Members of this family, such as STM3845 from a retron in Salmonella enterica called St-85, are found in the vicinity of reverse transcriptases (RNA-directed DNA polymerase) and retron structural RNA genes. The protein is not required for msDNA (Multicopy Single-Stranded DNA) biosynthesis, but instead is assigned an effector function
NKIRVKNNPKIIFLCGGPVDVSSSKPSSLRDAFRRYLEKHNPEYEIILPEDFFDWLLDGIKYKDLLDFEE
DLADISDLIVIFLESPGSLAELGAFSNNESLRKKLLVVVDEKYKKEDSFINLGPLKLLKNKNGSSVIVYP
WDDINDLGSDLEEELLEDILDDIKKKLSSLPKSEKFDPNNSGHLLLLILDLIYLFGPLKLSEILDLLKFI
FGIEINRKKLKRLLSLLEKFGLIEKKEYGSETYYYPLKKGFPYIRFGLDKKGKFDRLRLKAEILEYY
>gnl|CDD|468421 NF038233, retron_St85_RT, retron St85 family RNA-directed DNA polymerase. All members of the seed alignment are reverse transcriptases St85-like systems. However, members of this family may include reverse transcriptases from other types of retron system
EDLSEELGLSPKELFSLIKTAPYRYKTYKIPKRNGGKRLIAQPSKELKAIQRWILDNILSKLPVHESATA
YRKGKSIKDNAEPHKGNKYLLKMDFKDFFPSIKPSDVFRFFKKLGGIEYSDEDANLLANLCFYKGRGRLP
IGAPSSPAISNLIMYDFDERISGYCKKRGIVYTRYADDLTFSTNNKGILDKVEKFIKKILEDEGFPILKK
NREKTVFSSKKGSRRVTGLVITNDGKVSIGRKRKREIRALVHKYSHGKLDYEELSKLKGYLAFIKSVEPD
FYNKLKKKYG
>gnl|CDD|468422 NF038234, retron_eff_Eco8, retron Eco8 family effector endonuclease. This ATPase, found as the effector protein partner next to a reverse transcriptase in Eco8 type retron systems, is a predicted OLD family endonuclease
MPIKSIKIKNLLSFDDLEIDDLKDINCIIGKNNVGKSNLLKALKFFYKNLTGEKVIPPILDSNYSSKGEI
SITYDTSRLKRIARSNTNKNEYFKHIYNPFFKKIIFSFKKYLDKNTLFTLTLKIYKNGSISWSIKDYETR
KLLSYLFPFFFIESRHINLYDWDELWDLIGRLKKFNLSGLSNEEIIDFFDEKISSNYSNSYKDIIEEIKK
SIETKPYSYKEKILSYIKLGLGGYKFNIDGEELKTQSDGTNSFNFIKLFLNLLITLSRREYITPFIFIDE
PELGLHPKLNEQLINEIYESYSFKKKDNKTPYPKIILATHSPRIIKNIIKLFRDNHLIYHFSNENKYTKI
SRMNSTYDDERFLNIFSDNEARLYFSKFILFVEGETELELFGNKNLSELFPHLNKIDVYKSGSNEVILKR
INPSYSNSSIPYLVLFDADKILNYDGKKKKFTLSKSKKSLKPLKLENIIKKYKLGYSKKRRETLYNRKRI
IGIINKKLSFNDDKWGFCSDANYANLVNLIKNYLLKYNIFINSTTIEGCLINEENLEIFYKWLEYKKNLN
ISEIIKKEKIDNYLNQEEKTTFLRLIFNGKTDTLLSYKEFNNKQAIKKGRKLIKKLKKTILKKKPYFLGK
TDGWVTSFLNYFIEEIENGSKLEYKSFKSIFKLYFPELYDIIEKLESDS
>gnl|CDD|468423 NF038235, retron_Ec48_2TM, retron Ec48 family effector membrane protein
IKILAYAFIIIAFIGLLLSIISLAITIINDKNFSRPFCFSNECIKNFVKIFSGSISLLKATLTLLASFAT
VGGVYIALKTYILSVRNNALNNHLSHLNIFSDYLKSEVEKRDRLSIKSIDVFKWYNLIFPNSRSGKFDVS
DEYLLKINDLNDLIEESNEYITKASNGSFKYKNHQKRMISVLKKFGIEIEEEPRNDFYEIENQVLDLIDS
VNKSFCNSS
>gnl|CDD|439537 NF038236, retron_eff_Se72, retron Se72 family effector protein. Members of this family are cold shock domain-containing proteins encoded adjacent to reverse transcriptases found in Se72-type retron systems, and considered effector proteins contributing to phage resistance
GTVNAYDPFKGFGFIRREKGKDVFFFYDDINDEGDDIIEGDKVSFEVRKTPKGPRAYNIKKV
>gnl|CDD|468424 NF038237, retron_Ec67_fus, retron Ec67 family RNA-directed DNA polymerase/endonuclease
LKKLKAAKTLSDLARLLGVKPKALTYILYKKPPENKYTTFTIPKKSGGERTINAPNPELKLLQKRLANLL
QDCLDEINKKKGPKKNLKKPSLSHGFERGRSIITNARIHRNKRYVLNIDLEDFFGSINFGRVRGFFIKNK
NFKLDPKVATVIAQIACYENKLPQGSPCSPVISNLIGHILDIRLAKLAKKYGCTYTRYADDLTFSTNKKK
FPSEIARDEDGKWVAGKELEKEIERSGFKINEKKTRMQYRDSRQEVTGLVVNKKVNVKREYYRTTRAMCH
SLFKTGEFTIKKNGEKVPGTINQLEGRLSFIDQVDRYNNKRQKEPLPGKKKNKEKLNGRERLYRKFLFYK
YFYANEKPTILCEGKTDNIYLKAAIKSLAAKYPNLAEKKSGGKYELKVSFFKYSKRTRFLLELGGGTGGL
KNFISNYKKFLKKFKAPPPKHPVIIVVDNDSGAKGIKPLIKFINKKKKAIIKPDGKKDIGKAPFYHVTHN
LYLVLTPLLGKGKKETDIEDLFDDKTLKTKINGKTFNPGKKFDDDTKYYGKKAFASKVVKKNKKTIDFSG
FKPLLDRIEEVIDHY
>gnl|CDD|468425 NF038239, T6SS_TssL_short, type VI secretion system protein TssL, short form. TssL is a type VI secretion system (T6SS) protein, related to IcmH/DotU of type IVb secretion systems (T4bSS). Some forms have a OmpA-related C-terminal extension domain, likely to mediated interaction with peptidoglycan, but this form, also called SciP, lacks that extension
DIDALLQDTWLLVVQLRQGAEIQDGEALYQRCCAQVEQVRQALKEAGYSEESIEHILYAQCALLDETVLN
RGVQDDGYVQWRKSPLQARFFNTLNAGEALYERIREVLREPAPDPAVLTCFHRVLMLGFQGRYRSLDDPE
REQLLSALNARVPPFALSQDAPLVVRASGRRSGRWLRSWWFWIGLAVLLLAALWWGLSHWLQQLLAQ
>gnl|CDD|468426 NF038240, fibro_bind_EfbA, fibronectin-binding protein EfbA. The virulence factor EfbA (enterococcal fibronectin-binding protein A), like its close homolog PavA from Streptococcus pneumoniae, is an anchorless adhesin, meaning it has no site for processing by sortase and covalent attachment to the cell surface, but still contributes to adhesion that contributes to pathogenesis
MSFDGVFTHLMVKELSETLVSGRISKIHQPYENEIVLVIRSQGKNHKLLLSAHPSYARIQLTQIAYQNPD
TPPNFVMMLRKYLDGAILESIEQIENDRVIHFTFSKRDELGDLQNIVLIVELMGRHSTIVLVNKETGKIL
DAIKHIGSSQNTYRSLLPGAEYIAPPKQDQLNPFTASKEKVFELLSQLPELTGKYLQQQFQGLGRDTADE
LAYRLNQRPNEKMAVWQEFFTALTTQLQPTLYQTGKKEFFTPIAYQSLANQADSVTTYPTLSELLDAFYH
EKAEKDRVKQQGGELIKKIENELKRNQTKLKKREQTLADSENAEEFRQKGELLTTFMAQVPRGANEVTLP
NYYEENQPLTIKLNPALTPNQNAQKYFQRYQKLKNAVKLIGQQIAEAKDEIAYLESVLAQLEIAGPMDIE
VIREELVAQGYLKKKTTKKQKKQKPSQPERFLSSDGTEILVGKNNLQNDQLTLKTARKTDYWLHAKNIPG
SHVIIKSDDPSEETILEAAELAAYFSKYRHSAQVPVDYVQVKHIRKPNGAKPGFVIYENQKTLYVTPEEE
IIEKLKK
>gnl|CDD|439541 NF038241, RipB_Ich, (R)-specific enoyl-CoA hydratase RipB/Ich
MDTLLSAYKTIGERRYRETSGLYFEDFEPGDVFEHRPGRTVLDVDNVWFTLLTLNVQQVHFDAAYAAKTE
WKKLLVDSTFTLALLTGMSVRTVSAKVVANLGWDKVKATHPVFAGDTLYAESTVLSKRESKSRPTQGIVT
VSTRGVNQDGVEVMSFERTMLVYRRGHSPEEAANY
>gnl|CDD|439542 NF038242, RipC_Ccl, itaconate degradation C-C-lyase RipC
TRSWLFTPATRPDRFAKAAEVGADALIIDLEDAVAPSDKAEARAAALAYLAARPEDRLPCALRINGLDTR
AGLDDLHALLESPAEPDYLILPKTESAAHVQIVDRLLSEAGKSTRLIALIESVRGLNAVEDIASATPRLA
ALMFGAADMAADLGAGPAWEPLLLVRSRLVQACAMAGIAAIDSPFFDIRDEAGLKQETKAAVDLGFHAKA
AIHPAQIATINAALTPTAAEIAAARAILAENRQGVGSVDGQMVDEAVARKARRVLARA
>gnl|CDD|468427 NF038243, TRP75_fam_Nterm, TRP75-like N-terminal domain. This N-terminal domain is found in TRP75 (tandem repeat protein, 75 kDa) of Ehrlichia chaffeensis and TRP95 of Ehrlichia canis, preceding the region of 24 amino acid long direct repeats. It appears also in non-repetitive proteins from Anaplasma and Wolbachia, which likewise are members of the alphaproteobacteria
FSRVLNILLFLIFSFVTSCSNKAKYQFSRKYSPPYNPGGENFHEDEEFARSYSLYKERRELLKKDKGQGS
KNVVSKEKLIKKLKVKKIDSLDNLNEYGACIVDEGEDLMINQNGINLARVEGARFI
>gnl|CDD|439544 NF038244, pheromon_TrpTrp, quorum-sensing system DWW-type pheromone. Members of this family are pheromone precursor peptides about 31 amino acids in length, including a signal peptide. The active pheromone is derived from the C-terminal few residues, containing a nearly invariant DWW motif. Member proteins are found encoded near Rgg-type quorum-sensing transcriptional regulators
MFKKYKYYLLLAAMLLFKAAQVLSEVDWWRIG
>gnl|CDD|468428 NF038245, bile_salt_hydro, choloylglycine hydrolase. Bile salt hydrolase, also known as choloylglycine hydrolase, enables commensal or pathogenic bacteria in the digestive tract to escape the antimicrobial activity of bile acids, which are cholesterol derivatives conjugated to glycine or taurine
MCTALTYTTKDDHYFGRNLDLEFSYGEKVVITPRNYPFKFRKEADLKTHYAIIGMATVVDNYPLYFDAMN
EKGLGMAGLNFPGNAYYAEEVEGGKDNVAPFEFIPWILGQCETVDEVKEALKNINLVNIPFSEQLPLSPL
HWIIADKTGSSIVVESTKDGLHVYDNPVGVLTNNPTFDWQLFNLNNYMNLSPKQPENTFWGDLELTPYSR
GMGGIGLPGDLSSPSRFVRAAFTKANSPSGDSEEENVSQFFHILGSVEQQKGCCEVGNGKYEYTIYSSCM
NLDKGIYYYKTYENSQINAVDMHKEDLDGSELIS
>gnl|CDD|468429 NF038246, bile_salt_MFS, conjugated bile salt MFS transporter. Members of this family are MFS transporters found regularly in the vicinity of bile acid hydrolases in Gram-positive bacteria such as Lactobacillus acidophilus and Enterococcus cecorum, and presumed to be bile salt MFS transporters, or transporter subunits
GYKYFIVFACMLIQAIPYGIAQNIQPLFIHYVVNGFGFSLASFSLIFTIGAVASSIASPFIGKILSKVNV
KLLYLIGIILSAGGFMLFGLATKLWQFYVASAIVQVGTTIYSGIGVPWLINAWFPKEGRGKALGIAFCGG
SIGNIFLQPITQNLLKSPMHLGYMAPYFIFGIAALVVGLLIILFFVRLPKKTEEVLSANEIKKKEKTAAD
KTASEFWGYGAKETTKMKWFWIFSIGFLFIGLYVSALSEQYANYLDSLLKLSLTLVGTIGSVFALFCLIG
NISGGILFDKFGVAKSMTIAGVLQIIAILMLIFIGKIPALGYLFAILYGLSVFSYMSGPAFMTKDLFGAK
EFGVILGIVSLFFAIGFAVGSPLFGMIVDKFGFTAAWISMIIFVVIGYTLLLIAIIKIK
>gnl|CDD|439547 NF038247, memb_stab_MspA, membrane stabilizing protein MspA
LYLILLPLLYLIVSYISIFKMRSIFTRILRIIMGILLLFVVAVTTLQFPPENWWVFAVLLLLVGNVEITA
FKESKGDKKGVFILNLMTIMLFVIYIILTFVL
>gnl|CDD|468430 NF038248, FakA_VfrB, fatty acid kinase catalytic subunit FakA. Fatty acid kinase A (FakA, also called VfrB), works with a fatty acid binding-protein partner (either FakB1 or FakB2 in Staphylococcus aureus, depending on the substrate) to assimilate host fatty acids for membrane biosynthesis
SKINGKLFADMIIQGAQNLSNNADLVDSLNVYPVPDGDTGTNMNLTMTSGREEVENNLSQHIGELGKTFS
KGLLMGARGNSGVILSQLFRGFCKNIEDEEEIDAQQFAESFQAGVETAYKAVMKPVEGTILTVAKDAAEA
AVDKAEETEDCIELMEYIIEAAEESLENTPNLLPVLKEVGVVDSGGKGLLCVYEGFLKALKGETIEAQAP
KLDTESFVNDEHDFHGVINTEDIVYGYCTEMMVRFGKDKKPFDEQEFREDMSQFGDSLLVINDDEIVKVH
VHTETPGDVFNYGQQYGELIKLKVENMREQHREVVRKEQSNQQKQQEETETVETAIITISMGEGISELFK
SMGATHIISGGQTMNPSTEDIVKVIEQSGCKRAIILPNNKNIQMASEQAAEIVDAETVVIPTKSIPQGIA
ALFQYDESASLEDNKAHMTEALETVKSGSVTYAVRDTKIDGVEIKKDAFMGLAEDKIVTSDADQFEAVKG
LLSEMLTEDSEILTIITGEDANSETTDALEEWIEETYPDVEVEVHDGQQPIYQYLFSVE
>gnl|CDD|468431 NF038249, fatty_FakB1, fatty acid kinase binding subunit FakB1. FakB1 binds saturated fatty acids. Its paralog, FakB2 preferentially binds unsaturated fatty acids
MKIAVMTDSTSYLPQDLIDKYNIPVAPLSVTFDNGENFTENDDISAEEFYKKMKSSKTIPTTSQPAIGEW
IENYEKLRDEGYTDVIVIFLSSGISGSYQTATQAGEMVEGINVHTFDSKLAAMIEGSYVLRAIELIEQGY
EPDAIIKELEEMREHTGAYLVVDDLKNLQKSGRITGAQAWIGTLLKMKPVLKFEDGKIVPEEKVRTKKRA
LKTIEQKVLEIVKDYDEVTLFVINGDKKEDGKWLYEELKEKYPDYNIAYSEFGPVIASHLGSGGIGLGYT
GRKIRL
>gnl|CDD|439550 NF038250, nitrate_NreA, nitrate respiration regulation accessory nitrate sensor NreA. NreA is a nitrate-binding, GAF domain-containing accessory protein to the two-component system NreBC. It is involved in the regulation of the the nitrate reductase operon narGHJI
FENFNYQENLDEIREEEGFDFAGIALYEDDSTSSPIKWQYVSGNLNDRYKLIVLRKGRGLAGNVMKTGKR
MIIEDVDQSLSPNEKFKYPILLSENLTAVVAIPLWYENRVYGVLLLGQRNGKPLPENLEQIDISKKLGIF
TE
>gnl|CDD|439551 NF038251, AdcR_fam_Zn_TF, zinc-dependent MarR family transcriptional regulator. This HMM represents one of several unusual clades within the MarR family transcription factors that bind Zn(2+) and regulate the response to zinc abundance or scarcity. Members include AdcR (adhesin competence regulator), which regulates expression of the high affinity zinc uptake transporter AdcABC and various other proteins
ELAQQIDQFLNQILLKAENQHELLIGKCQSDVKLTNTQEHILMLLSEERLTNSDLAKKLNVSQAAVTKAV
KSLVKQGMLESVKDKKDARVTYYSLTELAKPIAEEHEHHHQHTLSVYDELLDQFSDEEQEVISRFLDALS
EEL
>gnl|CDD|439552 NF038252, cable_major, cable pilus major pilin CblA
MLKYVPIAAAALMSMSAHAVQKDITVTANVDTTLEMLSADGSALPTTMQMQYLPGSGLQAAEVNTKIFTN
DKAKDLQIRLATDPSLKNQTSPGAAEIPLAVKLGGTELSTTATTLKAAELFTGELAQGSNVLPLSIGQKT
VAAVTASGSYQGLVSVIVTQSAASGS
>gnl|CDD|439553 NF038253, GBS_IgA_bnd_BAC, IgA Fc-binding protein BAC. The IgA Fc-region binding protein of Streptococcus agalactiae (group B streptococcus) is a surface-anchored virulence factor with a YSIRK-type signal sequence at the N-terminus and an LPXTG sorting signal near the C-terminus. It is also called beta-antigen
MFKSNYERKMRYSIRKFSVGVASVAVASLFMGSVAHASELVKDDSVKTTEVAAKPYPSMAQTDQGNNSSS
SELETTKMEIPTTDIKKAVEPVEKTAGETSATDTGKREKQLQQWKNNLKNDVDNTILSHEQKNEFKTKID
ETNDSDALLELENQFNETNRLLHIKQHEEVEKDKKAKQQKTLKQSDTKVDLSNIDKELNHQKSQVEKMAE
QKGITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKVREELGKLFSSTKAGLDQEIQEHVKKETSSEENTQ
KVDEHYANSLQNLAQKSLEELDKATTNEQATQVKNQFLENAQKLKEIQPLIKETNVKLYKAMSESLEQVE
KELKHNSEANLEDLVAKSKEIVREYEGKLNQSKNLPELKQLEEEAHSKLKQVVEDFRKKFKTSEQVTPKK
RVKRDLAANENNQQKIELTVSPENITVYEGEDVKFTVTAKSDSKTKLDFSDLLTKYNPSVSDRISTNYKT
NTDNHKIAEITIKNLKLNESQTVTLKAKDDSGNVVEKTFTITVQKKEEKQVPKTPEQKDSKTEEKVPQEP
KSNDKNQLQELIKSAQQELEKLEKAIKELMEQPEIPSNPEYGIQKSIWESQKEPIQEAITSFKKIIGDSS
SKYYTEHYFNKYKSDFMNYQLHAQMEMLTRKVVQYMNKYPDNAEIKKIFESDMKRTKEDNYGSLENDALK
GYFEKYFLTPFNKIKQIVDDLDKKVEQDQPAPIPENSEMDQAKEKAKIAVSKYMSKVLDGVHQHLQKKNH
SKIVDLFKELEAIKQQTIFDIDNAKTEVEIDNLVHDAFSKMNATVAKFQKGLETNTPETPDTPKIPELPQ
APDTPQAPDTPHVPESPKAPEAPRVPESPKTPEAPKVPESPKTPEAPKVPETPKTPDVPKVPDVPKLPDG
LNKVGQAVFTSTDGNTKVTVVFDKPTDADKLHLKEVTTKELADKIAHKTGGGTVRVFDLSLSKGGKETHV
NGERTVRLALGQTGSDVHVYHVKENGDLERIPSKVENGQVVFKTNHFSLFAIKTLSKDQNVTPPKQTKPS
TQGSQVEIAESQTGKFQSKAANHKALATGNETVAKGNPTSTTEKKLPYTGVASNLVLEIMGLLGLIGTSF
IAMKRRK
>gnl|CDD|468432 NF038254, T4SS_assoc_EirA, T4SS-associated protein EirA. EirA (essential for intracellular replication A) was charactized in Coxiella burnetii as critical for replication in host vacuoles. Its absence appears to block secretion by the Dot/Icm type IV secretion system (T4SS), and family members occur strictly in species with T4SS
RFLIIFLLFFLLIAGAVSSDATSDTTSATPTKYCPPINQLVKDPDKGTWSAPTGGWKSYSTSFATTLTQF
LGAQWQGANVGQITCVYSSEQNFTFPVVLFYNTLVFQPTGGKWKKKKGGLYNCYSTNVSDCPFKPRVKPS
VKDIYKEAESLK
>gnl|CDD|468433 NF038255, exopoly_VpsD, VpsD family glycosyltransferase. Member of this family include VpsD (VC0920), involved in the biosynthesis of Vibrio polysaccharide, an exopolysaccharide component of biofilm matrix
KKVLLIMPLSTLNWGEKNAGGVDSVCQMLVRELANQSRPNYRYRVLAFDPLSQHQYTGEVIQLSENVEVI
FCPANEKRFGLPLPGIISQNLRVREQLKLFQPDLVHSHLNSWMIGPGGKAKNVLTLHSYRKIGRKSVSKL
NDFLYEKIIPWVSDFSVDFYTCVGEELLQALKNDTNKPIQVIGNPIDQEYFSQNKNKQKSRNEIKLVTCA
LITRRKRVDLAIVLLAELKKRGVDSTLNIIGPVVDPVYYEELKQLVESLGLENNVSFLGKLNQEEIVQQY
QNADVGVFTSEEETFGLAPLEMLAAGLPLIATPVGILGERKAEFAKLGVVFFSDGEEDEIANRILSINVN
DSQAIQKYLRDKFSVENVIEQYQNLYREVLS
>gnl|CDD|468434 NF038256, exopoly_VpsF, VpsF family polysaccharide biosynthesis protein. Vps genes contribute to biofilm formation by directing biosynthesis of the exopolysaccharide VPS (Vibrio polysaccharide), a major component of the biofilm matrix. Members of this family show some distant similarity to O-antigen ligases
SRLIYLLMVLAILSLFTLSGYLLENLGIDYVSEGGSPLEKIHVYTYLIFLLFALVLLRRGNPGFLKPLGL
LKRLWLISLLCIAIVILYGIVRFGTSGMAYLIDTFLLPLLLVPLLLQLSASQKRRLLTLVHYLILLNAVL
AIIEFLLGQRIVPVEFGSFSEFRSTALLAHPLNNALITASLALALLNKTRRLRIPRLIYILVQLLALFAF
GGRAALGIFLLGIFILLLPKLWRFLTGVRVSKLKFAVLLLLVYFAAIAVAVLLALGPIDERILSKLYDDG
SAQARFDVFILLEQLSWSEWLFGASHDLLESIVFYIGINWVIENYIIGWVLTFGLLGTILLTIGVFLFIF
ELARRSRMPAWLAILTFLLISLTNNSLTSKTPVLALFVVVLYLL
>gnl|CDD|468435 NF038257, exopoly_VpsP, VpsP family polysaccharide biosynthesis protein. Vps genes contribute to biofilm formation by directing biosynthesis of the exopolysaccharide VPS (Vibrio polysaccharide), a major component of the biofilm matrix. The specific function of VpsP is not known
LVLRAVLALIALVILYFSFQSGIASNYYYSAENTLEAWSKSPESATLEEVEEALTAIELAISLEPSHPHY
YQLQGQVYEWKAYLSDEVSTTQSTDKKQALKQAKQAYLKSLELRPTWPDTWIGLAKVKSQQEGPSERVYQ
YIQQAKKVGPYKPIVHLGIIQIGLANWQQLSPKQKALYVNHLALALKHPNSRHFVLDYLKQHNALKLVCR
WLQ
>gnl|CDD|468436 NF038258, PBP4_Staph, penicillin-binding protein PBP4. Members of this family penicillin-binding protein 4 (PBP4), as the name is used in Staphylococcus aureus and related species from the same genus. PBP4 is not essential. It has transpeptidase activity, provides low level beta-lactam resistance, and in mutant strains can contribute to high level beta-lactam resistance
IVSLLLLSTIITPPASAAAETPVEIANQEGYQNLSEQYNPEGAIVTTQTGQILYDYHGNKKWDPASMTKL
MTMYLTLEAIKKGKLSLNDKVKITSDYEKMSTLPNLSTFPLKPGQTYTIKELLKQTALASSNAAALILAE
KVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGADNNLLKPYAPKKYKDETKSKSTAKDMAILSQHLIKKH
PKILKYTKLTADTQHGVTLYTTNLSLPGQPMSLKGTDGLKTGTSDEGYNLALTTKRDGLRINQVIMNVGP
YPSEGAKHARNKIANALMERAFKQYEYKKVLSKGEHKIDGKTYYVKKDLYDVVPKDKSKYDLKINKDGKV
YVDYPRQFIKGSHPP
>gnl|CDD|439559 NF038259, ectoine_DoeA_2, ectoine hydrolase. This HMM describes a second family of ectoine hydrolase, related to TIGR02993. Members of both families carry the gene symbol DoeA. Ectoine is a compatible solute commonly used in halotolerant bacteria. This family was reported in halotolerant methylotrophs
MRERDDMTFPFEEYERRINELRERMAERLLDAVVISDPENLMYLTDYQTTGYSFFQALVVPLEDEPFMIT
RALEESNVIARTWVERTRPYPDTGDAIQMLVDALREFGLSGKRIGYERNSYFFPAYQQDRIHTTLTDGRL
LDCFGIVEEGRICKSPVEIEVMRKAAVATEAGMKAGIEACVAGVTENEIGAAISAAMFRAGGEPPAVMPY
VTSGPRTMIGHATWEGRTVQPGEHVFLEVGGCYRRYHTAMMRTVVLGELSDSMYKAQETMKLALAELRSL
VRPGMTVSDVDNLVRNIITDNDVGARLITRSGYSIGIAFPPSWDEGYILSLKQGDSTVLEEGMTFHIIPW
MWGVDGDKTCGISDTIYITEDGCESFFTLDEDFVVK
>gnl|CDD|439560 NF038260, ectoine_DoeB_2, N(2)-acetyl-L-2,4-diaminobutanoate deacetylase DoeB2. This HMM describes a second family of N-alpha-acetyl-L-2,4-diaminobutyrate deacetylase, unrelated to the previously recognized DoeB described in TIGR02994. Because of the lack of homology, we reassign the gene symbol for this family from doeB to doeB2 in the interest of clarity. Ectoine is a compatible solute commonly used in halotolerant bacteria. This family was reported in halotolerant methylotrophs
WQETIAFATAFRHQLHQHPELTWQETNTAATIRQQLDALGIPWRACAGTGTVATLAPNASGPHIALRADI
DALPITEQTGVAWSSQQPGCMHACGHDGHTATLLAAARWLKQHEAELPGPVTLLFQPAEEGGHGAREMIE
DGALDGVDEIYGWHNWPAIPFGQAVCPDGIVMAGNGTFEITLHGKGGHASQPELCRDPVLAASAITLALQ
QIVSRRLAPQSAAVVSVTSIDAPSAPTVIPETAKLEGSIRVADEATRDQINQLITEIAEQTAAAYGVEAE
VEVFPRYQATINHADQAARYREALQQELGEDWLDSDIALPIMASEDFSYYLQEIPGAFALIGSDDGEGHQ
APCHSPHYDFNDRLIPPVTRLFARLAGA
>gnl|CDD|468437 NF038261, rhodoquin_RquA, rhodoquinone biosynthesis methyltransferase RquA
IPDYLQETYWWAYVHPRAVRLLDRQWVVNLILWGNYRRLRDAALAELGPGQRVLQVACVYGDLTPRLAER
VGPEGRLDVIDVAPIQLENLRRKLAGDPQARVRRADAAALQFGDGSYDAVLCFFLLHEVPEDVKRRIVAE
ALRVVKPGGKVVFVDYHRPAWWHPLRPIMKPVFRWLEPFALDLWRHEISDYAPDADGFEWRKETYFGGLY
QKVVATR
>gnl|CDD|468438 NF038262, SiaB_fam_kinase, SiaB family protein kinase
LYSLYEELRQNGILLSYNGPFSQEIIEELGEALRNKLEAEGADPSVRRKVFSVFVEMAQNIRHYSAEKLT
LGEQEAEARSGIVVIGREDGRYFVICGNLVENEDAEALRERLEELNSLDKDELKAAYKEQLRPESPEGSK
GAGLGLIDIARKSSEPLEYSFEPIDDEYSFFSLKATI
>gnl|CDD|439563 NF038263, prot_phos_SiaA, biofilm regulation protein phosphatase SiaA
GLRGKSILALLLACLLALVPAVLLGWQALDGVRDHFGEAYARNFTLLNRQKILAPVSRELALSQRLAESV
LTRQWLRDEDDPAKRTLFFREAEGFRRDFADHSYFLISADSGHYYFNDGDQPFSAAPRYTLDRDDPKDAW
FFATLRSGEPYNINVNVDDKLGVTKVWFNVLVRDGGRVLGLAGTGLDLTRFLDDFISTREPGVTPMILDR
DGAIQAHPDPKLIALGSAAGAASPERTLFGLLDDGEDRAALRRAMAQARAAPGSVATLWVTLDGRPRLLA
LAYIPELDWYVLTAVDLGAAQVLDERWLWPAALALVLLLALLLLGFAYAVERLVLRPLRRLRRSAQAIAA
GDYDVPLPTARNDEIGELSRAFGSMADQVRAHTEELEDKVQERTRALEQANREMAAAHKKIQDSIDYASL
IQRAILPDRQLTRALGEHHFVLWKPRDVVGGDFYLFREDEGGYLIGVVDCAGHGVPGALMTMLARAAIDH
AIQELGLDDPAAILRRTDQALRAMLRDAELPRALATNMDAGLVYVDLRRGRLRFAGAKISLYASDGEEVE
ELKGGRRALGDRRRGEYENIELPLEPGWTYYLTTDGFLDQAGGEHGFGFGNRRFAELLRRHARLPLAEQA
EAFEQALAEYQGEHPQRDDITVLSFRFD
>gnl|CDD|439564 NF038264, kinase_SiaB, biofilm regulation protein kinase SiaB
DLLSLREAFNQQRILLCFNGPISRSLIEEIGNALRNYLEAEQAQPSAAMDVFSVYIEMTQNIRHYAARHG
YGEAEASATVVVARDEDGHYVVSAGNLVEPADGEALVARIRELAALDKAELKAAYKTQLRQPRDPGGASG
AGLGLIDIARRASAPLAASLKPLGDGRAFFSLRAVI
>gnl|CDD|439565 NF038265, phos_prot_SiaC, biofilm regulation phosphoprotein SiaC. The founding member of the SiaC family, PA0170 from Pseudomonas aeruginosa (NP_248860.1), is phosphorylated on Thr-68, as part of a regulatory system that affects aggregate and biofilm formation. The broader family, originally named DUF1987, if described by Pfam model PF09345
NDLEIPGTQSTPAIRADWEAGVLVMQGDSYPENSFELFQPVIDWVERFLAEEDRPLRLELELLYLNTSSI
KAMMDIFDLLEEAHQEGREVSVTWYYDPRNERVAELAEEFKEDCTFPFEILA
>gnl|CDD|468439 NF038266, diguan_SiaD, biofilm regulation diguanylate cyclase SiaD
LDERIEALLADPAHQGHPLREALAELWEQYREQLRRLERLTRISDGYQSAARERELSLAERYDRQLRRLE
KIVRISDRYQRMMRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRIN
DRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDD
VLSVTASAGLAEHRPPEEGLSATLSRADQALYQAKRAGRDRV
>gnl|CDD|468440 NF038267, amidase_AmiC, N-acetylmuramoyl-L-alanine amidase AmiC
MSDSNHNLSRRRLLQGAAATWLLSVSRVGFAASSQVIAVRIWPSSTYTRVTLESNVPLKYKQFALSNPER
IVVDIEGVHLNSVLKGMGEQVRSDDPYIKSARVGQFDPNTVRLVLELKQNVSPHLFTLAPVAEFKHRLVL
DLYPANGADDEDDPLLALLEDYNKGDLERSLPAEAPKPGKAGRDRPIVIMLDPGHGGEDPGAIGKYKTRE
KDVVLQIARRLKALIDKEPNMKAYMTRNEDVFIPLKVRVAKARKQRADLFVSIHADAFTSRAARGSSVFA
LSTKGATSTAARFLAQTQNESDLIGGVSKSGDRYLDHTMFDLVQTATINDSLKFGKEVLKRMGKVNKLHK
NRVDQAGFAVLKAPDIPSILVETAFISNLEEERKLRTARFQQQVAESILAGIKAYFA
>gnl|CDD|439568 NF038268, TF_SarA, global transcriptional regulator SarA. SarA (staphylococcal accessory regulator) is a transcription factor affecting multiple virulence-associated processes, such as biofilm formation and protease secretion
MAISKINDCFELLAMVTYADKLKSIIKKEFSISFEEFAVLTYISENKEEEYYLKDIINHLNYKQPQVVKA
VKNLSQEDYFDKRRNEHDERTVLILVNKKQRKKINELLERVNKRIKEANIE
>gnl|CDD|439569 NF038269, lipase_LipE, lipase LipE
GRIRVPADLDAVTDIGAEDHSEIDPAAVERIWQAARHWYAAGMHPAIQLCLRHNGRVVLNRAIGHGWGNG
PDDPPDAEKIPVTTDTPFCVYSAAKAITTTVVHMLVERGHFSLDDRVCDYLPSYTSHGKDRTTIRHVMTH
SAGVPFATGPRPDLKRMDDSEYAREMLGELRPLYRPGLVHMYHALTWGPLVREIVSAATGRNIRDILATE
ILDPLGFRWTNYGVAEEDVPLVAPSHATGKPLPAPIAAAFRKAVGGTPHEIIPFSNTPLFLTSVIPSSNT
VSTANELSRFAEILRRGGELDGVRVMSPETLRAATAPCRRLRPDVATGLMPMRWGTGYMLGSKRFGPFGR
NAPAAFGHTGLVNIAVWADPARALSAGLVSSGKPGRHPEAKRYPALLDRIAAEIPRA
>gnl|CDD|468441 NF038270, membran_MsaC, Msa family membrane protein. Msa (SA1233) was first described in Staphylococcus aureus as Modulator of SarA, but later reports suggested the locus was actually a non-coding gene, msaC, in the 3'-untranslated region of cold shock protein CspA (msaB). To construct the seed alignment for this HMM, we found full-length homologs across a broad taxonomic range within the Firmicutes, with the appearance of well-organized transmembrane alpha-helices. We further note amino acid substitution patterns suggesting translation into functional protein, and generally (in our opinion) the look of real protein rather than spurious translation, such as richness in Lys and Arg residues at the C-terminus just after the last transmembrane segment
KLILLALILNLLLFFIGSLFLLSLSVLLFLLLIYLLPLILNGILIKLQKNNKKKLYSLILPTISTLFYII
FSYLLMSSGGWDEFIERNTVSNGDMSIEIAPNLLDLSQIIFVFLLYFGISFLLYFISRKK
>gnl|CDD|468442 NF038271, strep_PBP2X, penicillin-binding protein PBP2X
KKRFLDYVLKDRRTPAKNRERVGQNLMILTVFLFFVFLINFAIIIGTDSKFGVDLSEGAKKVYQTTVTVQ
AKRGTIYDRNGNPIAEDSTTYSIYAIIDKSYVSATGEKLYVQPSQFDKVAEILNKHLGMEKDYVLKQLKQ
KKLKQVSFGTKGSGISYSTMTAIKEAMEKAGIKGIAFTTSPGRMYPNGTFASQFIGLAQLVENKDGSKSL
VGKTGLEASLNDILSGQDGKVTYEKDKNGNILLGTETVVKKAVDGKDVYTTLSAPLQTYLETQMDVFQEK
AKGKYASATLVNAKTGEILATTQRPTYNADTKEGLDKKDLNWNNLLYQTNYEPGSTMKVMTLASAIDNGT
FNPNETYSNSNGLTIADATINDWDVNEGLSTGQYMTYAQGFAYSSNVGMTLLEQKMGDDKWLNYLSKFKF
GLPTRFGMGDESSGILPSDNIVTIAMSSFGQGISVTQVQMLRAFSAISNDGVMLEPKFISAIYDPNTGTA
RKSKKEVVGKPVSKDAASQTRNYMVTVGTDPYYGTLYSKTTGGPIIQVGNYSVAVKSGTAQIAKEDGSGY
LEGENNYIYSVVAMVPAEDPDFIMYVTVQQPEHFSPLFWQDVVNPVLEEAMLMKDTLNLTAPALDDVTKE
TEYKLPDIIGKSPGDTADELRRNLVQPIVLGTGSKIKKVSVKAGSNLKANQQILLLTDKFEELPDMYGWT
KENVEKFAKWTGIEVTFKGSGSGKVVKQSVDVGTSLKKIKKITITLGD
>gnl|CDD|439572 NF038272, strep_PBP1A, streptococcal penicillin-binding protein PBP1A. PBP1a is a bifunctional enzyme of cell wall biosynthesis, performing both polymerization of GlcNAc-MurNAc chains (glycosyltransfer, GT) and peptide cross-linking (transpeptidation, TP)
KQTILKILKYLAIALLSLFILAIVIGGLLFAYYVSSAPKLSESKLVATTSSKIYDSNNNLIADLGSEKRE
NVTADEIPTDLVNAITSIEDHRFFNHRGVDVYRILGAALNNLTSSSTQGGSTLDQQLIKLAYFSTSTSDQ
TLKRKAQEAWLALQLERKYTKQEILTFYINKVYMGNGNYGMQTAAKSYYGKDLKDLSLAQLALLAGMPQA
PNQYDPYTNPEAAQERRNLVLSEMYEEKYITKEQYDQAVATPVTDGLQPLKSTSSYPAYMDNYLKEVIEQ
VEEETGYDILTTGMKVYTNVDPDAQKRLWDIYNTDEYVYYPDDELQVASTVVDVTNGKVIAQLGSRHQDS
NVSFGTNQAVETDRDWGSTMKPITDYAPAIENGVYTSTAASINDSPYNWPGTSTPVYNWDRRYYGNMTIQ
TAIQQSRNVPAVKALEAVGLDKAKSFLNGLGINYPEMHYSNAISSNTSSSDKKYGASSEKMAAAYAAFAN
GGTYYKPQYVNKIVFSDGTTKEFSNKGTRAMKETTAYMMTDMMKTVLTYGTGTNAAISGVYQAGKTGTSN
YTDDELAKIEKETGLYNSSVGTMAPDENFVGYTPKYSMAVWTGYKNRLTPIYGDGLKVATDVYRSMMSYL
TEGSGSEDWTMPSGLYRSGSYLYLNGS
>gnl|CDD|468443 NF038273, strep_PBP3, streptococcal D-alanyl-D-alanine carboxypeptidase PBP3. PBP3 (penicillin-binding protein 3) is the lone D-alanyl-D-alanine carboxypeptidase in Streptococcus pneumoniae. The gene is known as pbp3 or dacA
KKLILLLLLLLAFFLATTVSADDFDVAAKHAIAVEANTGKILYEKDATTPVPIASLTKLLTAYLVYKEIK
SGKLSWDTPVKISDYPYELTTNYEISNVPLDARKYTVKELLEASLVASANSAAIALAEKIAGSEPKFVDK
MKAQLKEWGITDAKLVNASGLNNSYLGDHIYPGSKKDDENKLSAKDVAIIARHLIKDFPEVLKITSKTSA
DFAGTTIYSYNYMLKGMPYYREGVDGLKTGTTEKAGASFVATSVENGMRVITVVLNADNADEDEYARFTA
TNQLLDYIYQNFEKVTLVKKGQAYKDSKLPVIDGKKKTVSAVAKKDLTVIQKIGTDSKPSVKFTPKKKEL
TAPIKKGQVVGKATFKDKDLIGKGYLGEPPSVELVAKKDVKKSFFLKVWWNHFVRYV
>gnl|CDD|468444 NF038274, strep_PBP1B, streptococcal penicillin-binding protein PBP1B
LDIGAVFLRTLKLLSNFFYVIILLFGMLGAGIAFGYLASQFDSVKVPSKESLVKQVSSISRISKLTYSDG
SLISEIDTDLLRTPVASDAISDNVKKAIIATEDENFKSHKGVVPKAVFRATLGSVLGLGSSSGGSTLTQQ
LIKQQVVGDAPTFKRKAKEIIYALALERYMSKDEILTTYLNVSPFGRNNKGQNIAGVEEAAQGIFGVSAK
DLTIPQAAFLAGLPQSPIVYSPYTSDGQLKSDEDMAYGLKRQKDVLYNMYRTGALTKEEYESYKAYDIKK
DFLPPETVTTNSHDYLYYTVLEEAQDVMYDYLIKRDNVSEQDLKNDATKASYEELALQELQQGGYTVTTT
INKKVYNAMQNAVANYGGLLDDGTGTVEVGNVLMDNKTGAILGFVGGRDYASNQNNHAFDTKRSPGSSIK
PILAYGIAIDQGLMGSASILSNYPTTFSSGQPIMHVDSEGTAMMTLQEALNTSWNIPAYWTYKLLREKGV
DVEGYMEKMGYHIPDYSIESLPLGGGIEVSVAQQTNAYQTIANNGVYQKQYMVEKITASDGTVIYQHKSK
PVQVYSKATATIMQDLLRGPISSGATTTFKSRLSALNPGLAGADWIGKTGTTNNYSDVWLMLSTPKVTLG
GWAGHDDNTSLAPLTGYNNNANYMAHLVNAINQADPSIFGTGERFNLDSSVIKSSVLKSTGLKPGTVTVN
GRTITVGGETTTSYWAKNGAGTTTYKFAIGGTDSDYQKAWSSILG
>gnl|CDD|439575 NF038275, Myrrnad, MyrrNad domain. This HMM, the N-terminal domain counterpart to MyrrCad (NF033158), represents the N-terminal regions of a family of LRR-like repeat proteins. The coinage "MyrrCad", rendered without full capitalization because it is an acronym rather than an amino acid sequence motif, signifies "MYcoplasma Repeat-Rich protein C-terminal Anchor Domain."
MKLRNFNKFLIGLAAISAGPAGTVLSNSNIHSSLVVENKATNDISWSIDDNGNISPTDKSKISGEITIPS
TVNGKPVTGIA
>gnl|CDD|439576 NF038276, strep_PBP2A, streptococcal penicillin-binding protein PBP2A
SYQRSKGYEEKAKKRPAWLSRIKPSPQNPIRRFWRRYHLGKILLILGGTFVLLVGSYLFYLAKTTNVSDL
QNALKATTVIYDKDGKEAGSLSGQKGTYVELDAISDDLENAVIATEDRSFYKNSGINYKRFFLAILTAGR
FGGGSTITQQLAKNAYLSQDQTIKRKAKEFFLALELTKKYSKKEILTMYLNNAYFGNGVWGVEDASQKYF
GTSAANLTLDEAATLAGMLKGPEIYNPLYSIENATNRRDTVLQNMVDAGKIDQAQADEAAAVDMGSRLAD
TYEGKSDDYRYPSYFDAVINEAISKYGLSEKDIVNNGYKIYTELDQNYQAGMQVTFDNTSLFPVSEYDGT
SAQSASVALDPKTGGVRGLVGRVNSTENATFRSFNYATQSKRSPGSTIKPLVVYSPAVASGWSIDKELPN
TTQDYDGYKPHNYGGIESEDVPMYQALANSYNIPAVYTLNELGIDKAFSYGKKFGLNMDKVDKELGVALG
GGVTTNPLEMAQAYATFANGGVMPDAHLITRIENASGKVIKTHKDKSKRVISQSVADKMTSMMLGTFSNG
TGVNANVYGYTMAGKTGTTETDFNPDLSSDQWVIGYTPDVVISQWLGFPKTDENHYLTDSSSGTASTIFS
TVASYILPYTKGTEFTVENAYAQNGIAPVYTANETSTETSSESQDIIDDIRESAQNAVDSASKAVDDAGI
KEKAKSLWDSIVDWFR
>gnl|CDD|468445 NF038277, accessory_MacP, cell wall synthase accessory phosphoprotein MacP. MacP was characterized in Streptococcus pneumoniae as a partner protein to the cell wall synthase PBP2a, required for its activity
MGKPLLTDEEIERANRGEDIEEERLQDEDQETKIYEKEDSEKEISNFYRKELKKNEKPITKSRRIENAKR
REFQSKLNKILIIVILLLILLILAVFFL
>gnl|CDD|468446 NF038278, strep_PBP2B, streptococcal penicillin-binding protein PBP2B
RKKKNASIPRRLNLLFFIIVLLFTVLILRLAQMQILNKDFYTKKLAAATTYTVKTSSPRGQIYDAKGKPL
VENEIKQVVSFTRSNKMTAEEIKELAQKLSQYVTVSEVKVTTRAKKDYYLADPEVYAKVVEKLPKKKKYD
SDGNRLTESKIYANAVDSVTDSQLNYSDEELKVIYLFSQMNAVANFNTVNLKTDDLTAEQIAYIAANKSK
LPGISVTTDWDRKVLDTSLASIIGTVSSEEAGLPAEEADDYLKKGYSLNDRVGTSYLEKQYESVLQGKRE
VKEIKLDKNGKIESDKITSEGQKGKNLKLTIDLDFQDGVEDILKKYFQSELASGNATYSEGVYAVALNPK
TGAILAMAGLSHDLGTGNLTEDALGTITNVFTPGSVVKGATLTAGWENGVISGNQVLTDQPIQFAGSAPI
TSWFTQYGSRPITAVQALEYSSNTYMVQVALKMMGQDYHPGMTLTTDGLKEAMEKLRSTFAEYGLGVSTG
IDLPGESTGYLPKDYTVSNVLTEAFGQFDNYTPMQLAQYAATVANGGKRIAPHLVEGIYDNNDNGGLGDL
VKTIETKVLNKVNISDEEMAIIQQGFYQVVNSSSGYATGRTLQGAAVTISAKTGTAETYVKDKNGQTVTT
VNLNVVAYAPSDNPQIAVAVVYPHATDLLSKVSQSIARDIINLYHSMY
>gnl|CDD|439579 NF038279, TF_CBS_SpxR, CBS-HotDog domain-containing transcription factor SpxR. SpxR from Streptococcus pneumoniae, like its full-length homolog YtoI from Listeria monocytogenes, is a transcriptional regulator with an N-terminal DNA-binding domain, and with CBS and HotDog domains. SpxR regulates the pyruvate oxidase SpxB
MSKHQEILDYLEKLPIGKRVSVRSISNHLKVSDGTAYRAIKEAENRGIVETRPRSGTVRVEKKTKVRLEK
LTYAEIARISDSEVLAGQEGLSHEFSKFSIGAMTEKNILRYLVKGGLLIVGDRENIQLLALENHNAILVT
GGFPVSDKVLKLANKLGIPVMVTHYDTFTVATMINHALSNVRIKTDIKTVEQVYQPKHEYGFLRDTDTVE
DYNDLVKKTRHVRFPVINQHNMVVGVVSMRDVVGKDPQTTLDKVMSKNPITTKPNTSLANISQKMIFEDL
NMLPVVDDNQTLLGVITRRQVMENLSNSQHSNLPTYSEQILSNLEEENDGFQFVVEPAMIDNSGNLAQGV
LTEILKEITLRVLTKKHQKNIIIEQMMIYFLQAVQIDDVLRIQPRIITETRRSATLDFEIYLEDQLVAKA
IITTKIN
>gnl|CDD|468447 NF038280, IS607_TnpB, IS607 family element RNA-guided endonuclease TnpB
WVVQAYRFALDPTPAQARALRSHFGARRKAFNWGLARVKADLDARAAEPLTESVKWSLRSLRKAWNTAKD
EVAPWWAENSKEAYSDGLAGLARALWNWQASRAGTRAGRRVGFPRFKSKRRDADRVRFTTGAMRVEPDRR
HVTLPVIGTVRTHENTRRLARHIEAGRARILAATVRRNGGRLFVSVRVEVQRPQQRAPARPDSRVGVDLG
VRRLATVATATGEVIERVPNPRPLEAALRALRRLSRALSRRTPGSRRWRKATAELSRLHRRVADLRRDHL
HKLTTRLARTHGTIVVEDLDVAGMLRNPGARALRRGVSDAAMGEIRRQLSYKTGWYGSRLVVADRWFPSS
KTCHGCGHVKDKILWDRHWQCDACGLVHDRDDNAARNLAARYETTPSVVGPVGAAVGRGADRKTGPSGAG
GAEARKPRGAG
>gnl|CDD|468448 NF038281, IS200_TnpB, IS200/IS605 family element RNA-guided endonuclease TnpB
HKAYKFRIYPNKEQEILINKTIGCSRFVYNHFLAKWNEAYEETGKGLSYNACSKQLTQLKKEEEWLKEVD
SIALQNSLKNLDDAFKRFFKKQNGFPRFKSKKNPVQSYTTKNTNGNIAIVGNKIKLPKLGWVKFAKSREV
EGRILSATVRRNPSGKYFVSILVETEVQLLPKTNSAVGIDLGLKDFAILSDGGKIENPKYLRKLEKKLAK
LQRILSRRKKGSSNWQKQRIKVARLHEKIANQRKDFLHKLSTRLIKENQVICIEDLQVKNMLKNHKLAKS
ISDVSWSEFRTMLEYKAKWYGRTVVKVGKFFPSSQLCSCCGYKNKEVKNLALREWTCPSCGTHHDRDINA
SKNILNEGL
>gnl|CDD|468449 NF038282, LapC_YejM_PbgA, LPS biosynthesis-modulating metalloenzyme YejM. YejM (LapC, PbgA) belongs to a regulatory system that controls the activity of LpxC, the enzyme that catalyzes the first committed step in the LPS synthesis. The earlier report (2015) by Dalebroux, et al (PMID: 25856753), which assigned a role in cardiolipin transport and introduced the name PbgA (phoPQ-barrier gene A), is no longer considered accurate
MVTNRQRYREKVSQMISWGHWFALFNILLSLGLGSRYLFVSDWPSSLAGRIYALVSWLGHFSFIVFAAYL
LILFPLTFVVMSQRLLRFLSAILATAGLTLLLVDSEVFTRFHLHLNPVVWELVINPDQGEMARDWQLMFI
SVPVIFLVEMLFATWSWQKLRSLNRRRFGKPLAALFISAFFASHLMYIWADANFYRPITMQRANLPLSYP
MTARRFLEKHGLLDAQEYQRRLVQQGNPEALSVEYPLSDLSFRDKGSGYNLLLIVVDGLNNSDIAKAMPA
LARFAEQNVQFTQHYSSGNQNDTGLFGLFYGISPSYLDGILSSRKPSALITALNQQGYQFGLFSSDGFKS
PLYRQALLSDFSLPPPQSQSDAQTTSQWQQWLNGQKNTNPWFSYLNLNGTSTASDDGKQKQRRYQRGAAD
VDQQINTVLDTLKERGLLDNTVVVITASHGVALDDNDDNFKFNRAQLQVPLVIHWPGTPAQTINKLTDHQ
DVMTTLMQRLLHVSTAAADYSQGEDLFAAQRRHNWVATGDDGTLVITTPTQTLVLDNNGSYRAYDLNGRE
IKDQKPQLALLLQVLTEEKRFIAN
>gnl|CDD|468450 NF038283, viperin_w_prok, viperin family antiviral radical SAM protein. Homologs of a viral defense radical SAM enzyme found in Homo sapiens, viperin (RSAD2), occur in prokaryotes with a strong bias toward placement in phage defense islands, encoded next to CRISPR system and restriction enzyme genes. Further investigation shows members indeed perform the anti-viral function of synthesizing modified ribonucleotides such as ddhCTP, ddh-guanosine triphosphate (ddhGTP) and ddh-uridine triphosphate (ddhUTP). Those non-standard ribonucleotides can interfere with viral replication machinery
ELVINWHLTEACNYRCKYCFAKWNDVKSPRHHDKGHLEKLLEELAEFFKLLSYGFVRINFAGGEPLLYPD
RLLDLIKLAKELGFKTSIITNGSLLTEEFLEELAPYLDWIGISIDSANEETNRKIGRVDRKGRVLSLEEL
LELIALIRQINPNIKLKINTVVNRLNWDEDLSELIRELNPDRWKVLQVLPVVGQNDDLLISDEQFDAFVE
RHKALGSIIVAEDNDDMTGSYLMIDPEGRFFQNSGGGKGYRYSEPILEVGVEEALSQINFDPEKFLSRYG
>gnl|CDD|439584 NF038284, bifunc_DapF, bifunctional diaminopimelate epimerase/glutamate racemase
MASFSPSTIYKYFLYSGAGNRFILGETCPELEDISFLCQEEQVDGFLYVLPSSCADAKLIIFNSDGSRPS
MCGNGLRCAIAHVAQVLGKEDISVETDSGVYSGKFYSWDRVLVDMTLPDWKYTCHRLTHTLPGLPKEVFF
IHTGVPHLVVFVPDVSKVPVQEWGSFLRYHEDFSPEGVNVNFVQILSHRELRVRTYERGLERETLACGTG
ALASALVVAKRYGLQDFSIAIRTWSGVLMKISLNRGRVYLEGPV
>gnl|CDD|468451 NF038285, deiodinase_rel, deiodinase family protein. Members of this protein family are related to iodothyronine deiodinase, a human selenoprotein. Some members of this family (although not of the seed alignment) likewise are selenoproteins, with the selenium-containing motif GSYTUPPF
KAYPGRPPEAVRMLLAILRGSQLGPTDGWFGPAQSRYGWDWLAERFDRDGDGAIARDEFPGPDADFARLD
RDGDGRLTADDFDWSDRSPWVQPGYMLNRLFRRADRDGDGKVTREEWDAFFDRAAGGKGFLSLDDLRDAL
LPRGPSGGFSPGDAPSKETLIRGLFRQEIGSLQEGPKLGEAAPDFTLKTLDGKETVTLSKLIGPKPVVLI
FGNFTCGPFRSQYGNVEKLYRRYKDRATFLMVYVREAHPTDGWRMESNDRVGVAVAQPTTFEERVAVAQQ
CRAKLKLGMPMLVDDIDDPVGNAYSGMPARLYVIDRAGKVAFKSGRGPFGFKPGELEQALIMLLLEE
>gnl|CDD|439586 NF038286, peptide_16_IlvX, peptide IlvX. The very short peptide IlvX, 16 amino acids long, is found in Escherchia coli and related species as the apparent first encoded peptide from the ilvXGEDA operon, for which ilvL, further upstream, is the classical attentuator system leader peptide controlling expression. IlvX is preceded by a ribosome binding site, terminates just two nucleotides from ilvG, and has evidence of increased protein expression during isoleucine expression. Its biological role is unknown, and skepticism that IlvX has any molecular function after its biosynthesis may be appropriate
MNNSTKFCFSRFRTGN
>gnl|CDD|468452 NF038287, Amuc_1100_fam, Amuc_1100 family pilus-like protein
KKNKFLAALLAVALVLLGAAGYLLYSASSAYSEAKQELEEAAAELKRLESLDPFPSEENVKALKKQLEEY
EAALDKLREALKAGVPPLLSPQEFQSRLRQAVEELRKAAEKAGVKLPENFAFGFEEYAGSLPSPEAVPRL
AQQLSAIKALVNILFDAKVDSLTSVRREPLPEEAGAAPGAAASGGAFAAKPAGSAAPPGLYERLPFELTF
TGSESALRKVLNGLASSPYFFVVRSLRVENEEEELRVTLRVDVVRFL
>gnl|CDD|468453 NF038288, chaper_GTP_ZigA, zinc metallochaperone GTPase ZigA. The GTPase ZigA (Zur-induced GTPase A) is a zinc metallochaperone thought to be important for histidine utilization (HUT), supplying Zn to the histidine ammonia-lyase HutH when required under low-Zn conditions
LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGASLSRTEEKLVEMSNGCIC
CTLREDLLVEVRRLAREGRFDYLVIESTGISEPLPVAETFTFADEDGVSLSDVARLDTMVTVVDAVNFLR
DYDSADSLQERGESLGEEDERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPIS
FGQVPLDKVLNTGLFDFERAAQAPGWLKELRGEHTPETEEYGISSFVYRARRPFHPQRFYDFLHSEWPGK
VLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMWWAAVPRERWPQDEESLAAIRENWDEPFGDRRQELV
FIGQDMDEAALRAALDACLLTDEEMAAGPEAWATLPDPFP
>gnl|CDD|468454 NF038289, Zn_piracy_ZnuD, zinc piracy TonB-dependent receptor ZnuD. ZnuD, as described in Acinetobacter baumannii, works with the zinc uptake transporter ZnuABC to overcome sequestration of zinc by the host. ZnuD, TonB-dependent receptor, pirates zinc from the host protein calprotectin. A similar ZnuD family protein, outside the current scope of this model, has been characterized in Neisseria
SFHKNLLTLSILAVISPSVFAQENEPVQQLETIQIQAHPLVQTAADFAVADHVVDQKQLSQGATTIGDAL
ADELGVYSNQFGAGSSRPVIRGQDGARVKVLQNASETMDVSTLSPDHAVTVDPILAKQVEVIRGPSTLLY
GAGTVGGLVNVTDSKIPTQMPEKGYEGQVGLRYNTGSDEKLASAGVTVGLGDQVALRVEGLKRDANDYIA
PDYLHEGEFTKERRVDNTFAESQTVNVGLSWIYDRGFTGISYSNRQDQYGLPGHSHEYESCHPHGPHLHC
GSHDHGDDEGHHHHDHEHDHAGPWIDLKSERYDFRTELNDPFAGFKKLRAQASYTDYQHDEIEEDEIATT
FKSKGYDGRLELVHNPIAGWEGVIGTQYSQQKLNLTGEEAFMAPNTTKKWSLFALEHKQWNDVHVELAAR
VDQQKIDIDSTQKDYDGTAFSYSGAANWEFAPNYKLSLVASHQERLPLAQELYADGKHFATNTYELGNDN
LDKEKSNNLELGLHYDNDKLDYHVHVYHNWFDDYIYAQTLDRYEDFRLVQYTQDKARFYGAEAEAGYQIS
PRYKLSVFGDYVRGKIDNENAPRVPAGRLGTKVNADFGDGWSGSAEYYHVFNQDKIAAYETETQGYNMLN
LGLAYAGQYSNKTDYRVYFKANNLLDDQVYQHASFLSNIPQVGRNFTVGVDFSF
>gnl|CDD|468455 NF038290, repM_Acin, replication initiation protein RepM
DLVVKDNALINASYNLDLVEQRLILLAIVEARETGKGITANTPLEIHASSYANQFNVHRNTAYKALKEAC
KNLFERQFSYQIDRDKGKEEVVKSRWVSKIAYVDNEGIVELTFAPDVVPLITRLEEHFTSYELKQVSQLT
SKYAIRLYELLIAWRSTGKTPIIELNDFRSKLGVEENEYKRMSNFKKRVLDPAIKQINEHTDITVKYEQH
KKGRTITGFSFKFKQKKKEKKIESKRDPNTPDLFIKMTDKQRHLFANKLSELPEMSKYSQGTESYEQFAV
RIAEMLLDPEKFKELYPYLKKVGF
>gnl|CDD|468456 NF038291, rep_pAB02_ORF2, plasmid replication DNA-binding protein. This uncharacterized protein, with an N-terminal DNA-binding helix-turn-helix domain, occurs in replication regions of a large number of Acinetobacter plasmids. The founding members of this family, AAR00518.1 and WP_000839337.1 from plasmids pAB02 and pMAC, are referred to as ORF2 there, sitting adjacent to RepM, which in turn is adjacent to the DNA repeat region at each plasmid's origin of replication
AKLSVSEASKLFNISRSTIYKAIKKGDLSKDSDGLIDLSEAIRVFGEPSKKSTDVNTSQSINSQKSTEVE
LLKQQVDMLKKQLEQAKERESFYQKQIDDLQLLLEYKAPKPNMTTFTDQPEANDTATDPQPETEQKHDGL
TTPEETENKRIPVPEHVEPEPKKRGLFGRFFG
>gnl|CDD|439592 NF038292, SagF_ScfC, SagF family protein. This protein of unknown function SagF is encoded by the extended locus that includes the key proteins of streptolysin S biosynthesis. Because it is encoded just upstream of genes for ABC transporter permease and ATPase components of an ABC transporter, one group calls the protein a probable ABC transporter substrate-binding protein, designated ScfC (subcutaneous fitness C). However, the protein lacks any readily detected homology to any other ABC transporter substrate-binding protein. Additional members of the family are found in other loci producing RiPP class peptide natural products related to streptolysin S, such clostridiolysin S
ILLALLSFLLLLTLWLTSKRRRRLKRWHLNLVSALSYQQWLDWLLSLYQLLLILVILFAYSAYESLVKFL
SFLGQANWIWQIFCYIILYLLALIEITLLVLILLVDVLLKKDSRLLFKKMTWLAFRKEKPFYSLLLLSLV
VLEDALFYLGLLYLLGKYSLVSLMLLILGYAIVKACRYSGWLEQLLAFCLFAFIGIWCVTATLLYGWLVG
LLLLTLTYLMISFKE
>gnl|CDD|439593 NF038293, permease_SagG, SagG family ABC transporter permease subunit. Members of this family are ABC transporter permease subunits, typically found in extended loci for the production of bacterial cytotoxins such as streptolysin S and clostridiolysin S
LLNIIKKEILQNFRDKKAMFMMVLFPILMILILGFAFSSSFNSSTSVPKTKVVYQIEGKKEYQKNFKEFL
KDLEKELGIEFKEIKDEKNAKEKVKEGKYDCYIKIEDDKTIKVYKNNIRQFNADLVNMLLNTFVDKYNTI
SEIAKLNPQALSKIKKRSSPDYVKVKSIDKSKSPTSIDYYAITMFTMIILYSIMSGAMLILGERQRKTYN
RIRCSPVSKSNILFGKLIGAFLATSFQLLIVYLFSRYVLKVNWGNNPWPIILIIASLVFMSVSIGIGLAI
MIKNEAVLSVASNIIIPIFVFLGGGYIPLETFNSNILNQISNISPIKWTNDSIFKLIYGNNFSPVPIAIA
VNLIIALVFLIIPLLIFRRQ
>gnl|CDD|439594 NF038294, lipo_LIC11966, ErpY-like lipoprotein. Members of this family are surface-exposed lipoproteins from the genus Leptospira. Members include the founding member LIC11966, reported to be a fibrinogen-binding protein
MKKQNIFTLIATICCIFLLSSGCKQDPVDYNNKIMEVLNASINDMDALNAAMEKDDLTNAENVRKAWETK
LTSSLDKLKGIGDFKGDSSFKNASIQALETYLNVVSKDYKRLIELRGLGDKADQNEINQILNRINQDFEK
AANTLNAASDKFAKEYAA
>gnl|CDD|468457 NF038295, EPS_HpsP, hormogonium polysaccharide biosynthesis glycosyltransferase HpsP
KILQIVPSISLVYGGPSQMVLGLSAALAKEGVEVTILTTDSNGDTGQKPLDVPLNQPVKQDGYEIIYFRC
SPFRRYKFSLDLLKWLNNHAKEYDLAHIHALFSPVSSAAATIARQQKLPYILRPLGTLDPADLRKKKQLK
QIYAALLERPNLAGAAAIHFTSEQEAKISERFGVSTRDLVIPLGVIPPENLPEDGKIRQQFGIPDNVPLI
LFMSRIDPKKGLDLLIPALEKLLAEGLDFHFVLAGTNPQDPDYEQKIKSQIQNSPLASHTTITGFVTGEL
KLALLQAADLFVLPSYYENFGIAVAEAMVAGTPVVISDQVHIWQDVEESEAGWVGTCEVEALTQLLREAL
QNPQERQRRGLNAREYALQNYSWDAIAQQTIQAYQQIL
>gnl|CDD|468458 NF038296, HisXaaSer_A2, His-Xaa-Ser repeat protein HxsA2. This model represents a short form of the His-Xaa-Ser repeat protein HxsA, while TIGR03979 represents a long form. In the short form, sequences average about 97 amino acids in length and end with the HXS repeat region
MKKRKFLVPLAVLAAALAAAQASAAIVPTASNEDTTTSATALHIAALGEQLLVYVKGGEAFKFVLKRNEA
GQMMAYHSSHSSHSSHSSHSSHYSSS
>gnl|CDD|468459 NF038297, hybrid_HK_HrmK, hybrid histidine kinase/response regulator HrmK. HrmK (hormogonium hybrid histidine kinase) is a regulator found in heterocyst-forming Cyanobacteria. It affects the formation of hormogonia, motility-conferring filaments produced only by heterocyst-forming cyanobacteria
MQQYSSLPEQNSQVDATPTLLTTIQQLRAELWLERSLNQLQSRLNDCLLSAACTTVNQQGVATEAEIFQT
VVNELNSALNSSRVACAVAIALFQPQETVGKICYVSSSSSTDSQSPLLEVILKKGKKLRLKLQEVIDIED
LQQLETQQPPSAWRLADDSGGVIGWLIIATASPNSDAESLKASQLAQLISQLMTRAAEQCATALAQLRQI
QSLQQQSQQLENFNQELERTNQLKNQFLANTSHEIRTPLSSIIGFTHLLLAQGYDPTRERHQEYLNIIQS
SGKHLLALINDILDLSKIEANQLEVQWETVDVPELCRNVLALVKEKAANKGLKLRLEIDPDVTTLVADSL
RLKQMLLNLLFNALKFTNTGTVGLQVKSQGSFVHFTVWDTGTGISKENQAELFQPYFQIANSVVSREEGT
GLGLAVTRKLAEIHGGWVEVESEVNQGSRFTIVLPLKPEGEVLEAEREVEEEKETSSSPLPITPSTSSSP
DILLVEDDLPNAELMQIYLEKLGYQVTWVKNAAEMWEALSQQEPAVILMDIYLPDGNGLNLVQQLRENPQ
YQNIPIIAQTAMAMKGDRETCLAAGVNDYISKPIDLPLLASLVAKY
>gnl|CDD|439598 NF038298, EPS_HpsO, hormogonium polysaccharide biosynthesis glycosyltransferase HpsO
MKILVASHTYIVDLNCEKLRALAQLEPGIEVTVVVPKRWKPGGVQNKIIETQPRDEGSFRVVPISNFSQN
NQGLLTFGADLISLLRQFRPQIIQVEQGSKSLAYAQLITLNKLLGLKAKNVFFTWWNLPYQLKFPVSLLE
KYNLRNTDGIIAGNQDGADILRQRGYQGPIKVMPQLGVDETLFRPQPQPELAAKLGIKPDDFVVGFVGRF
VEEKGLLTLLKALAGLKDKPWKLLLLGRGELKEELLQKATEAGIKDRLIWVESVPHDEVPRYINLMNTLV
LPSETTYKFKTLTAVGWKEQFGHVLIEAMACKVPVIGSDSGEIPHVIGDAGLVFPEGNAEALADCLRQLM
ENPELAQDLGQKGYQRAMAKYTNKALAKQQLEFYQELL
>gnl|CDD|468460 NF038299, EPS_HpsN, hormogonium polysaccharide biosynthesis glycosyltransferase HpsN
PLISVIIPTYGREEPLRDTLADVLKQDYPNFEVLVVDQTPTHEPETQAYLEELAESGKIQWFRLDWASLP
GARNYGVRRATGEIILFIDDDVQLPPGFLAAHARNYLERPEIGAVAGRVFDRMKLADSGGELTIEYLPPE
AMDPGIAWYYIDLVHTVKPQQVISARGCNMSFRREIFTKHGLWFDERFRGSAVREESDFCLRLRKTGYKI
WYDPEAHLVHLGEETGGCHDISTRSLKYQITFYHNHFLMALKNLTLSQQLRLFARLFDCHVLGNPPCNKS
GSPIKILTRGVFYTLGFLDALKTLIQSLWDDGQIYSR
>gnl|CDD|468461 NF038300, EPS_HpsL, hormogonium polysaccharide biosynthesis protein HpsL
KSKSKKSKKSKKQSKTETPTLSLKERLAQKRKAAQARKELISLLSTSIFVGIFVGIPLFFVGGIKLAIAG
VLGIIVLSLSYKYPRQALWAFLIYMPFSGTITYWIGGNPILQLAKDAFYIPALIALWQECRKKRLPIIIP
KAIKTPLLILLGCCLLTLLFVNGGQQFNPPCSGLFEPCPGEIPILMGILGLKVFLGYVPLIFCAYYLIRD
KKDLLFLSRLQVVLAIICCLLGLIQYLMLKTGRCAGTRGATGADLFKASLEARCFVGGSLLYSPSQGQIR
LPGTFVAPWQWAWFLISSAFFTFATAFSDPSIIWRLIGLGSMALVFINAVISGQRIALALVPVCFVILLV
LTGQIANLKRFIPIGVGLALILGIAMASNPDVVQERIDSFVSRWNASPPQEFIVQQFEESWKNQDGPLGS
GLGRATNSARAFGKTKLVETYYPKLLYEVGILGLLAFLAFVTHLTILTFKAYRSVKDKNLRSYGASFWVF
ILFISYNTYYYPLDVDPVAVYYWFFAGVLLKLPEIDKQEREEL
>gnl|CDD|468462 NF038301, EPS_HpsA, hormogonium polysaccharide biosynthesis protein HpsA
KRQLVKAIKKLFKKLSKHSLSAIKRQIIWLLRTLFITKRRRRTANAGFVLPTVAMVSLVVVLLTTAILFR
SFERAKNASNVRVNEAVLNAATPAIDRAKAKIEKLFKDPRLPRSTPSDIALYNALKNNIDEYTFGDETQL
KLNFDINGTSGIQNDETLDTAWKFPVDTDNNGKFDSYTLYGIYFRSPPRNSSNQFNRARNPLEARTPPMD
TGQSGGGCPDAVGTSASLVGDSGWYKSGGKLKKSFFVYTANVPITNTGTLDTNYETYKGNKGFSALEYQQ
DRERIPLNNNAVWYEDDLEITPGEAFRLNGRIHTNSNLLTGSTNSNTITLYQVSSPNSCFYEEENSKITV
GGNLGTGRVSDTDNGGGTTVDLFKGNNGNPATPGSISTNKKSTVSNGGNDIAYNDLAYVQRINRLVEAQM
ANCTTCTTDPEEVKDGIADKKDDTGLTTSSRVRVRRDELELYFRKRTRRVPFAEVSNPFGGNNSVALGTY
AIGNPLQDGSGDTLRPPDAWIYPTNPNDGKTGTGYTGLTLNTDGKLYLPATEPTKQKQGGKEQYLGDRVL
VGNNLPAYWYDSDKGKFVGPGTEDTQIISGITWDDPGTYPRTRRTQIQPLADLGITDRDGFWEFAAAQVP
DNPLDPVGGLRVVTGAGIYLPDPGGGYTGSTTSFLPPPTDDYIVVWPDTMPMRRTTPTYDQSTPDSAKPD
LRMRATAVYHYKDNYYDQTSPTPIACVSSYYDPTNSTTAKNKSGLPWNNATGLGTTSTDGLSNNGIVYGP
PTRTTAFTAYLAVLSYQANLKYPNGRWVNEPLRNALAKATANRTLAEQSAIDAALCALQILDGETGFTPT
DTAIPHGAIKEAAFLDAREVKAIDDVTGFFSNSATTYDLDLEDRQPLEIRVTVLDLGKLRTTTIGGSEPY
LLPNSGIIYATRDDALPDDSAGTSRRADWDNFISLSPVDFKLDPTRRPNGIMLINGSNLARSNTYDDKEK
GLILVSNLPVYIKGDFNLHQTTGGTTQEEFTTTLTDDWSNFYTRSTLNPNFACRPGDPGCTGGDLWRPAT
ILADAVTLLSGNFRDGFRNEGDYDLRNNAGISPDGGSSSAPTFDEDNNFVTSANWYETDGAPPKDLDGAN
SQGSSYLNNFVTPIQRRIAFNEYLMEICPKPPVSACQPDDWVVNYDGDGGAKNYSIREDLAANNGDSDVT
RLKAGTTAQPPEPSAYQRYPRRVAFLRNLATGKLVLDGDGAPVPLGIDNNGKVQAFPYTETTTLPRTNTN
ALWFRTTFNGTNAPHFIYNAQPLLVPVLQINSPFGTPSNPTNTGSDTNGRQNNWLQRATNTTFNAIFASG
DSPSRPTEDNGGLHNFVRFLENWNGKTLTKARISGSFIQFKRSSYATAPFATVLVARANDLSIFGYGITT
YDTNNGNGRTPFYLAPTRQWGYDVGLLSQSPDLFAQRFTTPPTGPPDEFFREVGRDDPWVKTLLCAKKDS
DGNYALPADQRPVSCP
>gnl|CDD|439602 NF038302, EPS_HpsE, hormogonium polysaccharide biosynthesis glycosyltransferase HpsE
LDFTVAIPTYNGANRLPEVLERLRSQIGTESLSWEIIVVDNNSTDNTAQVVQEYQKNWPSPYPLRYCFEP
QQGAAFARQRAIQEAKGELIGFLDDDNLPAPNWVAAAYAFGQEHPQAGAYGSQIHGDFEVEPPENFERIA
PFLAITERGNEPLLYEPKKKLLPPGAGLVVRKQAWLESVPERLILTGRVGGSMLTGEDLEALLYIQKAGW
EIWYNPAMHIYHKIPAWRLEKDYLLPLFRGIGLSRYHLRMLNLKPWQRPLAFLAYMLNDLRKIILHLLKY
RGQLKTDLVAACEMELLLSSLISPFYL
>gnl|CDD|468463 NF038303, EPS_HpsB, hormogonium polysaccharide secretion pseudopilin HpsB
SESGFTIIESLVAIVVVAILLAAIAPVIVLSVATRVQARRVELATQAAKTYIDGVRTGSIAAPNHTVTLT
TTTFNSSRNIFANAAPPATGLLTCTANTAPYCTNPTSSLYCVDLDGSGGCTSTSNKDFIIQAFRSNTATT
DADKGYLLGVRVYRADAFKDSGTLLKSDGDNKTQATFTGGLGDRQAPLVEMTTEISSGETSFQDLCDRLG
>gnl|CDD|468464 NF038304, EPS_HpsC, hormogonium polysaccharide secretion pseudopilin HpsC
SLLKFLLKTQLKRSKQAQTISGFTLIELLVAMILAVLVITPLLGFMINILNTDRKEQAKANSEQEIQAAL
DYIARDLQQAIYIYDADGITAIRNQLPPPTCTTRVPILVFWKREFIPNAVPVTSTTGCNTDDTFVYSLVA
YYLIKDNNSTWSKAARIARWQIRDGVRDTTGNGETTNGYIYGLAPDPGFKPFDLSDAGTLKEKMNQWTKA
SGNYYNTNPVLTLVDYIDQTTVTPPPTAATCPTALGLTQVPNYTGSNTNKTGGFYACVDSSKTIAQVYLR
GNALARIQQNNANYNSNNSAYFPTASIQVQGRGFL
>gnl|CDD|468465 NF038305, HpsJ_fam, HpsJ family protein. HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria
FSALLLRLVGYILLLLALLDYLILLIPPQFTNPAWQIQTIGQLVDRGIVPLVGLALLFIGYWIDSGARSR
KEGLDLRFLSWILSLLLGLLFLLLIPLHLNNTRRLSTQALQQINQQAGQQETQLQQQLNQLQAQTSPQQL
NQLLKSEQKQGQALASGQLPEEQKEQLQQFKSNPQALDKFLAQQLTQIRTQAEEAEKQARLEALKSSLRI
GLGSLLLAIGFITIGWTGLR
>gnl|CDD|439606 NF038307, EPS_acetyl_HpsU, hormogonium polysaccharide biosynthesis acetyltransferase HpsU. HpsU is related to the colanic acid biosynthesis acetyltransferase WcaF, which acts on a fucose residue in a disaccharide attached to a lipid carrier
LVDLRKYDQSWFDRGRPGWYILLWWLVQAIAFPLTPHNFNGFRCWLLRLFGAKIGKGVLIRPTARFTYPW
KVEIGDYSWIGDDVVLYSLDRIRIGSHCVISQKSYLCTGSHDIQDPAFGLKTAPITIGNGVWVATDCFVA
PGVKIGANAVIGARSSVFKDMPAGQVCWGSPCRPRYPR
>gnl|CDD|468466 NF038308, RNA_repair_RtcR, RNA repair transcriptional activator RtcR
MKKTVVIGFLGTTLDQGKGAKRWQKWRPTVALCQQPDLPVDRLELLHDRRDRALAERVAADIEEVSPETE
VRLVPVVLRDPWDFEEVYGALLDFARAYPFDTENEDYLVHITTGTHVAQICWFLLVEARYLPARLLQTSP
PRDKEEGTYEIIDLDLSRYDALAQRFAREQAEAVSFLKSGIATRNAAFNRLIEQIERVALRSRAPILLTG
PTGAGKSFLARRIYELKKRRHQVSGPFVEVNCATLRGDLAMSELFGHVKGAFTGAQADRAGLLRAADGGT
LFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLYARINLWT
FRLPGLRERREDIEPNLDYELDRFARELGRQVRFNKEARFRYLAFATSPEALWPGNFRELSASVTRMATL
ADGGRITEELVEEEIARLRAAWQSAPAAADDDALADLLGGEQLAELDLFDRVQLAAVLRVCRQSRSLSAA
GRRLFGVSRQQKASPNDADRLRKYLARFGLSWEDIKA
>gnl|CDD|439608 NF038309, HisXaaSer_A3, His-Xaa-Ser repeat protein HxsA3. This model represents an alternate form of the His-Xaa-Ser repeat protein HxsA, while TIGR03979 represents a more common form. The model covers a conserved N-terminal region, followed by the His-Xaa-Ser repeat region, but does not cover the C-terminal region, which is highly variable in this branch of His-Xaa-Ser repeat family protein
KFPKIKKSIEDFIYDEEGNIPRNKVLMIGSMIVILGMLLSDDVFAAHRSHSSHSSHSSHSSGSSGGHSSH
SSHSSHSSHSS
>gnl|CDD|468467 NF038310, lysogeny_AimR, AimR family lysis-lysogeny pheromone receptor. The founding member of this family, AimR (arbitrium receptor), is a DNA-binding phage regulatory protein that acts as a receptor for a 6-amino acid signaling peptide cleaved from the C-terminus of AimP. AimR controls expression of AimX, the third member of the quorum sensing-like arbitrium system and an inhibitor of phage lysogeny
IKNDLESKGITNRKLAKKIGVSKSTLSKFFNGKGEISFDSLLKILRVLYPNDEERRELIREYCLTLKPKL
NIRQALEYASLNGEYELLKKLIEKEKNSKNATNKEYAKVYELLYKRNKGEISGQELLDELEKKKKSKDPE
MKILSDILLMYAYYDLGNYNLMLEYADEIEKNIEEIKNGFIKDSYEYRIKELLAYAYLRRNELEEAREYC
NEIINSANNFPLLKATAYYCLGESYIFEDYEKALKYLEKSLELLKKIKNKKIERKYKAFLNTLAFLKIYW
NKDLDKIDILDPAEKAFLEIKKGNKEKAIKILEELEKENGFLSPFQYYYLGLATNDKELLKKSLEMFEKS
GNYFYAQLPKKEL
>gnl|CDD|468468 NF038312, SCO5918_fam, SCO5918 family protein
MRCVIARFPFDLTKSGVLESMKGVKPEPVTGESVIIGRRHYPVKQVGEVITRQDRRDFSAGEVTRAMTRL
GFTCRTLPEAAPAPALTPLQTASALLGT
>gnl|CDD|439611 NF038313, HisXaaSer_A4, His-Xaa-Ser repeat protein HxsA4
KLPSFKRSPGGMLSPEEREISDKALDAADQAGRLGPDPGGDGPLLAQHCSHGSHGSHGSHGSHGSHGSHG
SHGSHGSHGSHGSHGSHGSW
>gnl|CDD|439612 NF038314, epimerase_MslH, lasso peptide C-terminal Trp epimerase
MTRLTVALSGDCMATRGALITSDPAAGRLGELLHAADFAVTNLEVVPGDGRGHPVHNAAGGGCLIADPGV
LDEITAAGFTVLGCANNHALDLGTEGLLGTVDLLRAKGIPFAGIGADLTAARRPVYVDRPAGSLALISCS
ATFLPGQEAADPSPDLPGRPGLNPLRHGATLRVTAAQMDVLRQIDAETGLRARRAEARTLLGVDPALPGP
DRLELFGTRFRTADEPGFTTECDPRDLDGIARWVAEARRRADLVVVSVHSHEPGPTPETPGEFLRAFAHR
MIDEGADAVVGHGPHFLRGVELHRGRPIFYSLGNIVSQIELADRVPAEDYAKVTTDEPLTPGRYFDRLGG
HGRRLFAPHRRYWQSLVPVLTFDDGVLVGARLHPVDLGFGQPVHRRGRPRLADPVEAKEILTDVARLAEP
YGTTVTVGDDGTGELLLDG
>gnl|CDD|468469 NF038315, HxsD_rel, HxsD-like protein. Members of this family resemble HxsD, although usually shorter. HxsD is a possible chaperone of a radical SAM-catalyzed peptide modification system. Members of this family often are found in the context of other Hxs system proteins, suggesting it may be one of a pair of chaperones in those systems
LRFNKELYSKKAIDEAIKAFSDLAEIEVEEDGDYWVVRFTDCDEDEERLADEFANYVLGLTI
>gnl|CDD|468470 NF038316, DrmE_fam, DrmE family protein. Members of this extremely diverse family include DrmE, a protein of unknown function sometimes found as part of a DISARM antiphage defense systems
IYYNDKEISKEEILKDILDFLSNIFTSSEKKNLLILHPGSNCFDSLLLVAAALKSIINNKSDDDDDILDL
KIGDKVLYGNKRVEFKGIEDEEYIKLKYKDGGKTYIPLKDAYLLQPYNGSSKVLDGRGIRKKKKVRKDFL
SELLGIKTTEIPSVIDYSVVIVAGRKKFDEILKNLKIKGNNKKYKLLELFPAYYTSEDNEYKYGGNDNKQ
EPVLKFTSNLSVARELIKNDNKIDGIIVDGSSIISRDGTELSDLLNRKNIKLIFITSPLDSESILLLENE
NFNVFAWTKEYLLKNTLEIVEKNSLFLSLNRQIKNLINNEINIEVVKSGDFEDEIEKIKKKLYKLKKDDF
DDEDKNLFIILAYSLLNLLETAPFPISEYEYDIINGKLNTIEELLEELKESLGDSENDLFEEIIELLEDI
YEKLYSENPKFEALKELLNNAYDKGKKILIIVPKKYYAKILKEYLSLRLRISISNIDVITPNKFNDSTEI
YDKVIVVGWLNGKKLNILLCFNASKIIVLLYEFEKKWFNSLQKKLKKFLNNLIEKLSKKNEFEDLYKRLN
LEKEEVEEEEVEEEFELEEYIENLDENDYSSYIASGNASYTGTEAVKAKLVGFEDGEKAFFTKYYKAYVL
DEDKKEVKEKKVDELKVGDSLVFINNDDRTKDIIEELLESIKLNDKYKELYELSKYWKELLKEYMEKNGL
SYNDLAKKLKKLGCKKHEATIRNWLDDSHIVGPRDEEDIEAIAKITGDPELLENAEEYYEACREIRSIRR
KILKLLGKIIIDSLSGIEDEEISILENIYLNIEELSEVVEIEKIIEIEEEYNVPPNLVNRPI
>gnl|CDD|468471 NF038317, DISARM_DrmD, DISARM system SNF2-like helicase DrmD, long form. DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase
VPEPGQLVEVRGRQWVVSDVQLPRSPADQQHLVTLQSLDDDALGEELDVIWELEPGARVLERAGLPEVTE
GGFDDPERLAAFLDAVRWGAVTSADRRLLQAPFRSGISIEDYQLEPLVRALDMPRVNLLIADDVGLGKTI
EAGLVIQELLLRHRARRVLIVCPASLQEKWRDEMREKFGLDFRIVDSEYVAQLRRERGLHANPWTSFPRL
IVSMDWLRGERAQRLLRDVLPAHADTPRAFDLLIVDEAHNVAPASPSKYAVDSQRTRLIRDLAPHFEHRL
FLSATPHNGYSESFTALLELLDPQRFARGVPPDEKQLDEVMVRRLKSDLVDRDGSPRFPERELEALPVDY
SADEREIHELLDEYTELRRKRLAGKRGRRAADFVTLLLKKRLFSSPAAFARTLEVHRATLERGAARGGPL
SDDERLLRDDVLDDEEDYADDELLEEAEDEALEEASELSPPLTAEERALLERLRAWAERAEARPDSKARA
LIDWLRANLRPGGRWTNERVIVFTEYRDTLRWLVELLAAEGYGGDRLALLHGGMDDDERERIKAAFQADP
SEHPVRILLATDAASEGIDLQNHCHRLIHYDIPWNPNRLEQRNGRIDRHGQRADPVLIWHFVGKGTEGAA
EGDLEFLDRLARKVATIREDLGSVNPVIADQVERLLLGRRRDLDTEAAEIEAAKRRELAAERELREQLER
LHEQLEESREELHLTPANIRRVVDTALELAGQPPLVPVGDPGPDGRVFEVPALSGSWARALDGLRHPLHT
GQIRPITFDPEVAKGRDDVVLVHLNHPLVQMSLRLLRAAVWSDDKPLHRVTAVVVPDDGLEEPAVAALSR
LVLVGGDGARLHEELLLAGGWLRDGRFRRLEGVTDVEALLDAALPSGRPAPPAVRDRLAERWPRLRERLE
EALEARARDRLDALERTLADRGEAEAQRIRAVLDELRATLREALAEDEEPEQLALFSEDERRQLRRDRRA
LERRLARLPEERERELAAIEARYADPKPRTFPVAVVFLVPESE
>gnl|CDD|468472 NF038318, DISARM_DrmD_b, DISARM system SNF2-like helicase DrmD, short form. DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase. This HMM describes a distinct form that is somewhat shorter than the majority of DrmD proteins
NLLLEQYARYKRQELEKSPYHCLLMADIDPNPHQINAFCAAIAALKTGGIILADEVGLGKTIEAGLVLKY
VLESGAKKILIILPANLRKQWEIELEEKFDLESLILDSLTVEKDAKKWNKRLTDNKKVRIVITSYDYASK
LMKRFPKVKWDFIIIDEAHNLRNVHKGGKRAKNLYELTKGIPKILLTATPLQNSLLDLYGLVSFIDPRIF
GSEKVFSKRYIKDEDYSDLKRELSPVLYRTLRKDVADYMQFKKRKCITVDFELSPDEIELYVRVNNFLKR
DILYSIPTSNRTLIILVIRKLLASSSFALAETFEVLKKRLEKLKEGTRSANAQEGFDLFWSFVEDEIDES
GFEEKQDELYTRQKEFIQHEIDEVDAIIDVAKRIKTNAKVTALKTALEIAFEYQREEGIAQKVVVFTESK
RTQKYIAEELRKSGYEGEDILLFNGDFDDAMTKEIYRAWQVKNYGKANYGRSVEYKHAIVDYFKNNAKIL
IVTDAGSEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLNTQNVADKRVYEILSEKF
ELFEGVFGASDIALGLLESGTDFEKRVLQIYQSCDTTAEFKKEFDKLEKKLDAKRNKKARELRSLLITES
SEAKKQALEGTKLEIDEYLQEVEYWSSVAEPEVDYPKYWKVDGWGEQNIGGIEHGYLFIGAFCNNADLLF
PVLLLCDENGKYIDFSEEDIVPALEKIDDSDVRYFTPTKIEIALYQKVYDNLTSEMLQKYDRQNKPIIEY
NRRKIENWLRIQKEQLVLQYQDMSAEIEELKEQERASKNFYEKIDIKKEEKEKQLEKFQASFHERGTAFK
AEGEREIEEFNKQFDINPVLLIKIVLKF
>gnl|CDD|468473 NF038319, DISARM_DrmC_I, DISARM system phospholipase D-like protein DrmC. DrmC, a phospholipase D (PLD) domain-containing protein, is a component of DISARM (Defence Island System Associated with Restriction Modification). This HMM represents most but not all DrmC of class I DISARM systems, which contain a DNA adenine N6 methyltransferase. DrmC appears to be an auxiliary rather than core component of DISARM, required for resistance to some phage but not others
LGALLPPTELRALAEALASGRSLASALSAVLPAPAAREAVARLLRAWRASGLSPEELAAALRGAAAARAR
QSEEQSVELVWTGPTTPGVPVRRTEQVLLELIRAARQSLLLVTFAAYKVSPLVEALAAAAARGVAVRVLL
ETSEGAGGALSGDEPARAFAGVPGARVWHWPVDPRALRGGSLHAKVAVADRRVLLVTSANLTESALERNI
EAGVLIRGGALPERLAEHLRALVR
>gnl|CDD|468474 NF038322, ImpA_fam_HExGH, ImpA family metalloprotease. Members of this family are metalloproteases related to the ImpA from Pseudomonas aeruginosa (PA0572 in strain PAO1), a virulence factor that cleaves CD44 on the surface of human macrophages, inhibiting phagocytosis. Members of this family are distinguished by a strong motif, CGxGCSGNPxD, just a few residues upstream of the familiar metalloprotease motif HExxH (typically HELGH here) and completely lacking in more distant homologs of ImpA
ALASGDASLLSDSAELLAAALALIEARRQQQAALLAALYGGLTAISWDPTHDSQLITPTYGENATPLLTN
NVGDSGYDTLAALAIAGEQGGRYAAYGSNPFRVMAGGSNEQQMEPLLKNLLGWLLGGNADLALPATLKVA
VAGYDDSYYFPTRNWLTAHYPNATVINCDGAALANCLQDADLLVLGQHGSAGDDAGLAAAVRQALAAGIP
VLYLHTDWNDSPLGRALLAAMGLSLGYGGNYWAKDGLADWRTAADMLAAPDQLGALQTLLQRLKDGDFAF
DLSACDDTSCDDVAGFDSEFYTGADQLRNALRALDSAGINLFADPGYRLLKLLVLLADKYRQDIDYPMDK
ATTPTADFLRAYFADHWVYYARSINPAQPDLGNFSRSDAQSLPPSTTPETKTVTLPSKSGFTAIGRYALP
GQTVTVTRTDNSGATLAVFINTLRSGSTREFDKNGYNRPRFLQSPRIPLAPGETVTFTSPYGGPLQLNFS
GATAGLTVTLRFKGVAKHPHWRDFTDNAQIAAFVAALAAGDFDWAELKTPGFEVHSRLDKMRKSIGRWNG
DPADYADAIRTYVFNSNHILAGFKGPGISLPAEVQDFCTALGWDCTDTIHRAPIVQHFNADQATCGYGCS
GNPYDAYWGFSPLGWGDSHELGHNLQQGRLRIYGGRSGECSNNIFPYYSKWRYYAETGNDPSCQRLDHKD
LFALLQASRAQADPEAYRADMYQRLWSDGNNGPRMAFYIQLAMLAQKLGLGDTLDNGWHLFTLLYLHERL
FGKAAASEADWDANKAKLGFGSYALAEANSISNNDFLLVALSKITGRDMRPYFDMWGLPYSDKAAAQVAA
LGLPAAPLVFYALPPGKGYCLSEGLWVLPLDVDGGTPAW
>gnl|CDD|439619 NF038323, DISARM_DrmE, DISARM system-associated protein DrmE. DrmE appears as an fifth component in a subset of class II DISARM phage defense systems. Its role in DISARM is unknown
KKIKISKAEKSIIDELEDCIKNKENIVVCYPNSNFFFFLILEAVLKDEIENFKNRKDPSKRASVLIITNN
KEMLDFLKNLNVNASYLFQTCKRKHKFLRENGVFCNMNDPYFARVYWRHILYKYYEGKIPEEIPLHYIFP
IAIGYHTFNAISRGNRNKLGRKDNKQQPVFYITDNLNILKDNEQEFDYIFVDCTYIKKFISVIPKGTLYF
FDSPLDDRLLYLVQKWNIKNYILDGVPLKNIIEKEIGRPFQISIQDMIKSSDINSLNIEYVKSPFENELE
KAIELLQKLSKKKFSSYDLNIIRKLLYNIIRMPVSAVEYDLIAEFEPYYETINDLLNELKESDNRYENID
FERIIELLEDIFYKYNLDNVSPKFEELKKYIEKEVKQGKKVLIVVPNKIVSLALKEKLSLSLGISISDLE
EKGLYFLSKKDIINGLQSEDCDTVLIYSAINLSDLSILLKINYRKAILLLYKIEINLLKSKLKKLSDIKN
YALELFDSNDKELMKTNIYRYLYNRLKRFNIQKEINLDFILDKLLEEITSSKIHYSIRENKDYKGKNAVK
AKLVRFEDGSKMFFRKESKVKVLNKKQKRIIIKKFSELKVGDEILFIDNDVRKDLYTVFIKNIDNKNESK
KNYLLIEKWRELYEDKFLELRMDDEKLFKKMKELGWDKTTKSILRNWRSGYSYGPRDLEDIILLGKVLNI
PEFIENAHFYYDAMSHIRVERRNAARILNKIIYFSKKALEKSDLSFLEKYNLSIEQLKEAVKIKKVKNIS
EKVYYVKPSEIGILF
>gnl|CDD|468475 NF038324, DrmB_fam, DrmB family protein. Members of the seed alignment for this HMM are the DISARM anti-phage system protein DrmB from both class I and class II
GEIRPSQLITTYGPGAIVDLPNFSVIILGLDDWDYDRCEPFEIEEPRLLAAVRRRLGPQVERLRPPPWNA
ELDDDPFARVGVPVRPFPRWLRCTKCDLLAPLDSGLFELRNTPYRPDLARFVHEGCPGKKKGKRPPAVPA
RFVLACPNGHLDDFPWRYFVHRGNSTCKGTLRLRERGAGGSLADITVKCPSCGARRNMSEAFGERGRENL
PRCRGRHPHLGTFEPDGCDEEARLLQRGASNLWFPETLSALSIPPADNPLAQLVEEHWEDLEDLESAEEL
KGIRKLLPKRKALPLEKYSDDEVWAAIERRRAGIEEEDTDPVDLKVPEWEALASDPHPSDTPDFEAERVP
VPPGLQKYFSRVVLVERLREVRALLGFTRLDAPDPGEDDELVRRAPLSRGGPKWVPASEVRGEGIFLRFD
EEALAAWEQRPAVSSRWEALREAHRRWREARGSDPPDAGFPGPRYVLLHTLSHLLIRELALECGYSAASI
RERIYAGDDDGDPMAGILIYTAAPDSEGTLGGLVELGEPDRLERLLRRALERARLCSSDPLCAEHLPDDD
EFLHGAACHACLFISETSCERGNRFLDRRLLVPT
>gnl|CDD|468476 NF038325, DISARM_DrmAS, DISARM system helicase DrmA, short form. Members of the seed alignment for this family are DrmA helicases from representative DISARM anti-phage gene clusters, mostly from class I systems, but a few from class II systems. This HMM excludes those members of class II systems that both are divergent in sequence from this set and have a characteristic long insert
VRDELVDALRRDLLGPAGGPEEELDEMPVRPRDRYLVGMLAPRDSEIEGDEDEEDDTDDDDDGDAEEDES
AEDDVDAEEDGEEIDAPKNGSLFPSSMGLSFCVPADTDSLEVTASWGRYERVKSEEEEKEGGKKRRVWKR
EPVEGTLVVVPLDEGPITPIPLPDDPGVVLQVSVRPLKGGDRLVSLFLVNDREEPEDENRDEAWLFQPEL
EVRAEDGAAVFLPRDDPLRDGDDDDDEERRLELLYRDRLEFAVGHGVAVHAEVAEGPRRATEVRTTWIPT
YEVPQTSAPGREELAGGELDMKALAAAALKRAELIAALRPLVDGYRAWIDEQQAEAIGLPEGLRETAEEA
LDRCREALDRIRAGIDLLEDDDKALEAFRFANRAMALQRRHSQYARKRRRGEELLSYDEADDEVKNRGRA
ASWRPFQLAFILLNLPGLADPEHPDRSADRAIVDLLFFPTGGGKTEAYLGLAAFTLAIRRLQGVVGGGYD
GDAGVAVLMRYTLRLLTLQQFQRATALICAAEVIRREDPATDPRWGEEPFRIGLWVGGKVTPNRFEEAKE
QIEDARESGSGGRGSPLQLTSCPWCGTEIDAGRDLEVDNTDGDRRRVLIYCGDKLGRCPFSKGKSPGEGL
PVLVVDEEIYRRLPSFLIATVDKFARLPWRGETGALFGRVDRYCPRHGYVHPGLDCGTCGHHPAKKGLPA
AKVKPVVRPLRPPDLIIQDELHLISGPLGTMVGLYETAVDELCSWEINGKKTVRPKIVASTATVRRAAEQ
VRGLFGRKVAVFPPQGLDVGDSFFSRQRPVSEKNPGRRYVGICAPGRSLKTALIRVYEALLAAAQALFDR
YGNPADPYMTLVGYFNSLRELGGMRRLLEDDVQTRLRRVGKRYGDGLARRYVNFGMNVEELTSRVSSADI
PKTLDRLEVPFDPEFDTTAGKPWRPVDVVLATNMISVGVDVDRLGLMVVVGQPKNTAEYIQATSRVGRDR
PGLVVTLYNWARPRDLSHYERFEHYHATFYRHVEALSVTPFSPRALDRGLAGVLVALARLGNAEMAPNEG
AARIVDLDDPEAEEVIDRLLERAEIVAGDERARDDVRERLDRRLDEWEKRASQQGRGSLRLGYEKTGDGG
DKTLGLLNSPGEGRWDEFTVPNSMREVEPEVNLLL
>gnl|CDD|468477 NF038326, DISARM_DrmAL, DISARM system helicase DrmA, long form. This HMM identifies some DrmA helicases from class II DISARM anti-phage systems, and none from class I systems. Members distinguished from the shorter, more common form (see NF038325) both by sequence divergence in regions that align and by an insert that makes members of this set longer
MREELIEELIKEVLGPRNGPEEKIIGANPRTEYITGVLEPPNCKSERDPDSPDSEDELIEEGETDEEDDE
DGEEASSPVLSPELDPRSLPKSFGISFLVEGKNENPEIEICVTWGRYFKIEESGWKDEPKEYNSRRKSWK
RKPYSKINEDIILEKVEEEGTIYDGEDGKILLIVRRLKSVATSYHISIYLVNELEVPEGKNPITERSIFQ
PSIRVVLGEGTLSIPYSRAVETDIDEEDEELDFLYRNRPVLARGHMCSAIWKEIDPQDEFPGKSLWPDGP
FYWEDGEIVAEDLCKKFFDPDVRTEFVPLYPLSAPDFTWPGSYGPEPELDPEKLSEMWDPEEIEKYLSPL
VNGYRNWIEEQEEESLTLKPEEQELAKRLINEQEIVLKRIKKGIELLKTDEEARLAFCFANKVIWLQAKW
KSGGKNGVWRPFQLAFILMNLESLVNPDSPDRDYCDLLWVPTGGGKTEAYLALMAFTLALRRRRAKRNGA
GDRTGAGTAVISRYTLRLLTIQQFRRALKMITACEYLRVFRLGGGGGIGWRPEKCEVSDDFIWGTTRFSA
GLWVGGAVTPNHLRGTTFRGENFNKKIPGAIKILKGESKGEGEPAQVTKCPVCGTILAVPEGGLPEGSHT
LYLVIRSEKTLEELKPIVSTLEPPKGLIAEARIPLHGSNKYNTLILYIELESILKVNEEEIDAIWRKLLL
QLNGEGLGLVSARPSRPGYFIKKYYSERGKTSSSPYDFEIFCPNPDCPLNNAWGEGVPAGIVNAAETVPR
NELGDSKDFLPDPEPFKENEHPFLRASRIPIPAYTVDEQIYHRCPSIIISTVDKFARLAFEPRAASIFGN
VEFYHARYGYYREDAPPLSSLPKHPAGYASSEKLSVAVEPFAPPELIIQDELHLIEGPLGSLVGLYETAV
DELCKESGGKPKYIASTATVRRAGPQVKALFNRRLAQFPPPGLDIEDRFFVRIPETHPGLDANRPGRLYM
GICAPGKGPLTPIIRIWARLLQTVYELRRDGAIDPFWTLVGYFNAIRELAGGRALYRQDIPERLKQISGD
SKLRRRNLDEEQVVELSSRIDSTELPQLLERLESGKSRDIPENPDAIFTTSMFGTGVDIPHLSLMVVNGQ
PKTTSQYIQATGRVGRRRGALVITFYRAGRPRDLSHYEFFTGYHRALYREVEPVSVSPFSPGALERAAGP
VMVAILRNAPNTGVDWFREDSGAHMIRNSRSNRDVKKLVSLCECRAQRQPADRRPDIESVEREFRSGLDR
WKRIARKNGDTLVYSEYALYRKPEKPVVLGDPQHERYGLDVVFENAPQSLRDIEETTNFEV
>gnl|CDD|439622 NF038327, c-di-AMP_CdaM, diadenylate cyclase CdaM. CdaM is one of several classes of diadenylate cyclase (the cyclic di-AMP synthesizing enzyme), characterized originally in Mycoplasma pneumoniae
LVNLILLAFSVILLLLLFLYVSKEKFWFKKYTWKLFRRKSISASEFENFYFNLSSSLLKLSKKKIGALIV
IEKYDNLQKYINLGYEVKSKFFPEFLYNVFLNKESSMHDGGVIIRGLEIVSVSSYFPITSQKNIPNSYGS
RHRAALGITEKTDAIAFLVSETSGKISVSQGGKIKELNKDNLDRLIKKLIKLLSFY
>gnl|CDD|439623 NF038328, c-di-AMP_CdaS, sporulation-specific diadenylate cyclase CdaS
MKQKLKEYLEQIIGDLQHILQTLDEEDCCLLGEFEEIRKLFLQIESLAASFYLQCYLSPYTDKYAELSLA
IQHLSEKRHGALIVIEREDPLDSLIQPGIPIGAELSASLLESIFYPGNPLHDGAVLIRENQIVSAANVLP
LSNRTTGDKKLGTRHRAAIGLSERSDALVLVVSEETGRISFALNGKLYPIS
>gnl|CDD|468478 NF038329, gly_rich_SclB, LPXTG-anchored collagen-like adhesin Scl2/SclB. SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats
MNKTKQNKTKQNKTKQNKTKHSLLCRYGLTSAAALLLTFGGASAVKADQEAATIETQQRKLQELREAFPR
LEEIYKSTPLDDTTVNKIYKYLEERDKKLNSYLEELDEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDR
GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG
PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER
GPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQK
PDTAPHTPKTPQIPGQSKDVTPAPQNPSNRGLNKPQTQGGNQLAKTPAAHDTHRQLPATGETTNPFFTAA
AVAIMTTAGVVAVAKRQENN
>gnl|CDD|468479 NF038330, adhesin_SclA, LPXTG-anchored collagen-like adhesin Scl1/SclA. Scl1 (streptococcal collagen-like protein 1), also called SclA, is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats
MLTSKHHNLNKLVWRYGLTSAAAVLLAFGGGASSVKAEGSAAPMTSEQRQQEIKKIKEEIKKKYPKASEE
KFWSSGWYGRTYLDEEKYQKGLEEFTEEALKEIVDLIEKGATKGDKGDAGPKGPRGPAGPPGEAGAKGDT
GPKGDRGEQGIQGKPGKAGEKGEKGDKGETGERGEKGETGATGAQGPQGEAGKDGAPGEKGEKGDRGETG
AQGPVGPQGEKGETGAQGPVGPQGEAGEPGEQGPAGPQGEAGKPGEKAPPETPEQPGEKAPEKSPEVTPT
PETPEQPGEKAPEKSPEVTPTPEMPEQPGEKAPEKSKEVTPAPEKPADKEANQTPERRNGNMAKTPVANN
HRRLPATGEQANPFFTAAAVAVMTTAGVLAVTKRKENN
>gnl|CDD|439626 NF038331, Tsi3_fam, Tsi3 family protein. Members of this family are related Tsi3, the immunity protein for the type VI secretion system effector muramidase Tse3
LVLELPEGFEAEQTADGFRVRPPGSEARRSPLEITVTLHPGPEPPPGDPSRRSLGGRRARYRVDREEGGS
GGDEYTLTAWEPLGGGYVRYRQTTQSEGGEPDFELAWAVLESARCQ
>gnl|CDD|468480 NF038332, rSAM_rare_HxsC4, radical SAM protein HxsC4. This rare radical SAM protein, closer to HxsC among previously defined families, shows up regularly in the context of putative RiPP target HxsA4 and additional members of the His-Xaa-Ser repeats system
AEPSIEERIAGQRERVHILTGAVCNNNCIFCMEEDRDGRYVTNSATTDERVRWILEQHRGAEEVCFTSGE
PTTNPRLPRWVKWAKEAGYRRISVMTNGRALSYEPYARGLVAAGMNRFYVSIHGHTKKLHEGLTRTPDSF
EQTVAGIDSIARLKRFGVELHTSTVVTKRNLPHLGDIYRFLRAHGVDQVVFNVMQANGRANTYFEQIFPR
YTEIAAAFRAFLAEQAVREPRVMAFLVDIPLCTTEGIPDFNRGYVESYVHYEPALAERLVLLPAEDLAER
RAGGDGGLVQIRRADLDDAERQKRAECASCRYDAVCEGVWGNYLRRYGWDEFVPV
>gnl|CDD|439628 NF038334, malate_HK_MalK, malate sensor histidine kinase MalK
MKKTLKLQTRLTIFVCIVVLISLCITFFTIGSETAKNIREQERDIALQTAKMVAEAPITAKSLESGKSYK
ELRQYTTRVQKITGTEFVVVMDMNGIRKTHPDPNKIGKKFAGGDEEPALKGHEHISTASGTLGKSMRAFV
PVYDKDGKQVGAVAVGITLNEIDLIISQSLRPLYFVICLSIFVGIIGAVIVARKVKNIMFGLEPYEIATL
LEERSAMLESTKEGILAVDQHGKIKLANAEAKRLFHKMGIMTNPIDQDVQDILPKSRLKQVIETKKPLQD
RDVRINGLELVFNEVPIHLKGQIVGAIATFRDKTEVKHLAEQLSGVKMYANALRAQSHEFMNKLHVILGL
VQLKNYDDLGTYIKDIAIYQQTETSEIINHVKNSVLAGFLLGKQSYIREQGATLEVICSTQIPNAADPAV
IHDLITVIGNLLNNALDAVSQTEKKNISISFRFHDEQLDIEITDTGVGMSKEEQAKMFDQGFSTKGQNRG
FGLYFVQQSIENLNGHMIVTSEKNEGTTFSLRIPYEPKEDNHD
>gnl|CDD|468481 NF038335, YPO0640_fam, YrhA family protein. Members of this family include YrhA from Escherichia coli, which is found as a pseudogene in the K-12 model strain, and YPO0640 from Yersinia pestis. Only full-length forms are used in the seed alignment for this HMM. The function of this protein family is unknown
WKELLNEIKKIEKKYGYELNPPASEDEIEKLKEAVKKKFGGIWLPPDYLEFLKISNGLEFNGLVLYGIDQ
SLLDGEPNDFINGLIEANEIWRENEWQDKYLFIGESDISWYVYDLKSNKYEELDKPSGDVIESFDSFDEL
LEAALKTVL
>gnl|CDD|468482 NF038336, YjiT_fam, STY4851/ECs_5259 family protein. Full length members of this family, about 1100 amino acids long, include STY4851 from Salmonella enterica subsp. enterica serovar Typhi str. Ty2 and ECs_5259. The family also includes the half-length pseudogene translation YjiT from Escherichia coli str. K-12 substr. MG1655, for which the corresponding complete protein is WP_048814575. The function is unknown
WLAEFLSRRGLTKPDGRPLYSYRVTDEEYSELKTLLRASLPRQDPSVFSRYWAALFVLFAAEWFRREYTG
GHWSWDPILKSLGIDLPANQRSELVEKGLRFWKRPILSYSNGRNYLGSLAVEGGLPSRLLAEEGSRLQSY
FRRVISDYGLAKGLGSSAASLAEAHLERLPVSFREEAFYELIAELAETLYELVDEYGLDAQSDPVQFLDK
VSPDWRDSLPLPLDDETARELLNGLLRQASEERRRRPKKQKSLRCERYLSEDDDEWQLAARISLPGELSF
PLNKLELLPTRFELAIYEGGELLARLGSAFAPPENDQWRVRVLTKLLRLVRFNFDAELSLVLRDDGRLVG
AFVLPGSELDIGELPWVFEAESDEWLLVGQGSVSVKSSAVFILLPAGASLPSESGSECLGRTIEALGRSL
YKVTGQADVLIGDGDRYRIRTGQDDDESEELTLRGKRVLYTTSPSPVFLGKPKLVADSNGQSRDIPEDEL
RWRGGDSLEWLSVSSVPYGLQEISVRNENGETLLRRKIAILPADFDIEILPGESANEGQIVLSSLHPCNV
ELLNVTGELTVKRSGDLTEDISLKANGKPPARVELALSWNLGAKPISLTLPFPARGACLLDGDGEPLRGK
EITVDDLLGSRLFLYKNGEPTTFELELELKASNGPGALHRWRYSVNEFPVEISLYELREDIEELLALSSD
LDAVVRMSVSGPGRLLSTNIRRYDYSLEPDREIGIISLDAFPHDESSSIKLVAMPLADPEREPLPLPERT
SEGVAVGEFELPELENSNGPWLVYPRDGSEVQFRPLLIPGELELLSSPSNSLQKALRLFNPQFRKNAIDQ
VLGQMANDPLHSGWQYLKSLVENLDHLPLTTFEVWKALARNPRALAALLFKAELDEAEFLWRLQNELPFL
WESIPLSAWKKAIELFYKSLEEQLGEPEELARNILENRLQELGTYFPGLEDSLADLLSLKQSPSVVPPAV
MQQVFDGWYQDLLRNHDDDRWPTHFGKELSRWIIQSELKQLLPLELTPDSDFRFAVMYLPVLLAAVASGK
ASLTDVFENEPELVFALRQLRDFDRQWFEQAFALTL
>gnl|CDD|439631 NF038337, FAAL_FadD21, fatty-acid--AMP ligase FAAL21/FadD21
MQNSSVVSLLRERAGLQPDDVAFRYTDYEQDWAGVTETLTWAQLYRRTLNVAHEVRRHGTTGDRAVILAP
QGLPYIVAFLGAMQAGLIAVPLSVPQPGSHDERVSAVLADTSPSVVLTTSAAAAAVAEYLHRPDTGAVPA
VIEIDSLDLDGPNSPSIRISDAPSIAYLQYTSGSTRLPAGVMVSHRNLQVNFQQLMAAYFPDTNGVAPRD
TTIVSWLPFYHDMGLVLGVIAPILGGYRSELTSPVAFLQRPARWIHAMANGSPVFSAAPNFAFELAVRKT
TDADLAGLDLGNVIGIVSGAERIHPATLDRFCKRFAPYNFREDMMQPSYGLAEATVYVASRAEGGAPEVV
HFEPEKLSEGSAQRCEARTGSPLLSYGTPTSPTVRIVDPDTCIECPAGTVGEIWVHGDNVAEGYWQKPEE
TRRTFGGVLANPSPGTPEGPWLRTGDLGFISEDEMFIVGRMKDLLIVYGRNHYPEDIESTVQEITGGRVA
AISVPVDETEKLVTIIELKKRGDSDEEAMRKLDAVKNNVTAAISRSHGLNVADLVLVPPGSIPTTTSGKI
RRAACVEQYRRQQFTRLDG
>gnl|CDD|439632 NF038338, FAAL_FadD28, fatty-acid--AMP ligase FAAL28/FadD28
MSVRSLPAALRACARLQPNDPAFTFMDYEQDWDGVAITLTWSQLYRRTLNVAQELSRCGSTGDRVVISAP
QGLEYVVAFLGALQAGRIAVPLSVPQGGVTDERATSVLRDSSPVAILTTSPAVDDVVQHVSARPAESAPS
IIEVDLLDLDAPNGSGAGTENYPSTAYLQYTSGSTRTPAGVMLSHQNLRTNFEQLMSGYFADTDGIAPPD
STLVSWLPFYHDMGLVLGVCAPILGGYPAVLTSPVSFLQRPARWMHMLASSFHAFSAAPNFAFELAAKKV
SDDDMAGLDLGNILTILSGSERVQPATIKRFADRFARFNLQEKVLRPSYGLAEATVYVATSRPGQPPELV
DFDAESLSTGQAKQCESGAGTSLISYVLPRSPIVRIVDSDTCIECPDGTVGEIWVHGDNVAIGYWQKPDE
SERTFGGKIASPSEGTPEGPWLRTGDSGFVTDGKMFIIGRIKDLLIVYGRNHSPDDIEATIQEITRGRCA
AISVPGDRSTEKLVAIIELKKRGDSDQEAMDRLGAIKREVTSALSNSHGLSVADLVLVAPGSIPITTSGK
VRRAACVEQYRQDQFARLDA
>gnl|CDD|468483 NF038339, FAAL_FadD32, long-chain-fatty-acid--AMP ligase FAAL32/FadD32. FadD32, also called FAAL32, is a marker enzyme for the biosynthesis of the type of mycolic acids, the very large "eumycolic acids", found in Mycobacterium
EFEPFLDENGNIRFPDGATLVDHVERNARERADTLAYRFIDYSRERDGEARDLTWAQFGARLRAVAARLQ
QVTKPGDRVAILAPQGLDYVVSFFAAIYAGNIAVPLFDPDEPGHTDRLHAVLGDCKPSAILTATSSAEGV
RKFFRSLPAKERPRVIAVDAVPDSVGSTWVRPDADLDDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMV
DAIELDENSRGVTWLPLFHDMGLLTVILPALGGKYITIMSPAAFVRRPGRWIRELAAVSDGAGTFAAAPN
FAFEHAAARGLPKEGEPLDLSNVIGLINGSEPVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSS
TPREDEAKVIYVDREELNAGRIVEVDPDAPNAVAQVSCGYVARSQWAVIVDPETGTELPDGQVGEIWLHG
NNIGTGYWGRPEETEETFHNKLKSRLEEGSHAEGAPEDANWMRTGDYGVYYDGELYITGRVKDLVIVDGR
NHYPQDLEYSAQEASKALRPGFVAAFSVPANQLPAEVFENSHSGLKYDADDSSEQLVIVAERAPGAGKAD
PQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACKAAYIDGTLRGGYQQTAFPDA
>gnl|CDD|468484 NF038340, SAR2788_fam, SAR2788 family putative toxin
KKYLISLIVATLLFSYIPPNFASAAEDEVNEEEENIDEEEIEEELNEEISEELDIEIIEENSEVIVVETT
LETEDLEVESELELDLETGEITVSGELEDENGNEINKEFDVEVLEIEGEDFKATFIDQETGEEYEVDTEE
VQASALPLVVIVAFIARYGIKYAIKKYGKSAVTKAIK
>gnl|CDD|468485 NF038341, ligase_FadD4, fatty-acid--CoA ligase FadD4
MQIREHAGADKPAVILHPSGTVVTFAELEARANRLAHHFRRAGLVEGDTVAILMENNEHIHAVMWAARRS
GLYYVPINTHLTAAEAAYIVDNSGAKAIVGSAALRDTCAGLAEHLPGGLPELLLIADGDLDGWQRYPECV
ADQPDTPIDDEIEGDLLQYSSGTTGRPKGIKRELPHVPPAEAPGLMTALVGFWMVPDSVYLSPAPLYHTA
PSVWSMSAQAAGITTVVMEKFDAEGALDAIQRYRVTHGQFVPAMFVRMLKLPEAVRNSYDVSSLQRVVHA
AAPCPVEIKKQMIDWWGPIVDEYYASSEAAGSTLITAEEWLTHPGSVGKPMLGVVHILDEDGNELPPGQA
GEIYFEGGYDFEYLNDPAKTAASRDKHGWVTVGDVGYLDEDGYLYLTDRRHHMIISGGVNIYPQEAENML
VTHPKVMDAAVFGIPDDEMGQSVKAVVQTVDPADATDEFAAELLAWLRDRLAHYKCPRSISFEAQLPRTD
TGKLYKQELIEKYS
>gnl|CDD|439636 NF038342, FACL_FadD6, long-chain-acyl-CoA synthetase FadD6
TRTSVGLLDIAARLPGLLADAPVMLRGVLTGFGARPSAKTSIGKVFQERAARYGDRVFLRFEDQQITYRE
ANETANRYAAVLAARGVGRGDVVGIMLRNSPETVLLMLATVKCGAIAGMLNYHQRGDVLAHSIGLLDAKV
LVAESDLVEPITESGADTADLLTIEELDRLATTAPTTNPASTSAVLAKDKAFYIFTSGTTGLPKASVMTH
YRWLRALAGFGGLGLRLRSSDTLYCCLPLYHNNALTVAVSSVLNAGATLALGKSFSASRFWDEVIRYDAT
AFVYIGEICRYLLNQPPKPTDRAHKVRVIAGNGLRPAIWDEFTERFGIERVCEFYAASEGNTAFVNAFNI
DKTTGICPSPIAFVEYDPETGEPLRDENGRVRKVKPGEPGLLLSKVSSLQPFDGYTDPAASEKKLVRNAF
KDGDVWFNTGDLMRPQGFGHAAFVDRLGDTFRWKGENVATTEVEAALSADPTVEECTVFGVEVPGTGGRA
GMAAIKLRDGAEFDGKALAKTVYDRLPGYAVPLFVRVVGELEHTSTFKSRKVDLRKQGYGDSIEDPLYVL
AGRDEGYVPFYPEYPEEVAAGKRP
>gnl|CDD|439637 NF038343, ligase_FadD11, fatty acid--CoA ligase FadD11. The fatty-acid-coA ligase FadD11 is disrupted in multiple strains of Mycobacterium tuberculosis, including the type strain H37Rv. This HMM represents full-length versions
TTLCEAFQRTAAIDPDAVALRTPGDAQTLTWREYAAQVRQVAAGLAGLGVRRGDTVALMMANRIEFYPLE
VGAQHVGATSFSVYNTLPAEQLTYVFGNAGTKVVICEAQYVERIRASGAPIEHIVCIDGAPPGTLSLEDL
YAAAAPDFDFESTWRAVQPDDVATLIYTSGTTGNPKGVEMTHANLLFEAYAFDAVLGIEFGDRITSFLPS
AHIADRMTALYLQEVFGTQVTVVADARQIAAALPDVRPTIWGAVPRVWEKLKAAIEFAVANEPDEARRQA
LQWALSVAAKRAAALLAGEPMPAELAAEWARADELVLSKLRAKLGFDELRWAVSGAAPIPKETLGFFAGL
GIPIAEIWGMSELSCVASVSHPRDAKLGTVGKLLPGMEGRIADDGEFLVRGPLVMKGYRKEPAKTAEAID
ADGWLHTGDIVTIDADGYLRVVDRKKELIINAAGKNMSPANIENAIKAACPMIGAMATIGDGRPYNTALI
VLDADSAGPYAAQHGLSDASPAALAADPDVIAQIAAGVAAGNAKLSRVEQIKRFRVLPTFWEPGGDEVTL
TMKLKRKPIAAKYAAEIEELYAESP
>gnl|CDD|439638 NF038344, bile_CoA_BaiB, bile acid--CoA ligase BaiB
KTDFFNKFNTGTSSFVTPGKQLAYIAKVKPDATAIIYIDKENKESVITWKQLHTLSNRLAWYLLEQGIGP
GSVVMVAFPNIIEHIIAAFAIWKTGACYMPVSSKTADKELSEICECISPSLAFTNREKPDGYFCLSSEEL
YEVMEDYSEEMPPDVLADPNMISLSGGTSGKTKFIRQNMPSGESDEGLKTWFAMSGMRFEQRQLLVGPLF
HGAPHSAAFNGLFCGNTLVIPRNLCAENIVRLIKKYKIEYIQMVPTLMNRIIKLPGFRKEDFASLKALCH
TGGVCSPDLKRKWIDILGPEKIYEMYSMTECIGMTCIRGDEWLKHPGSIGRPVCGGKISIRDEEGKELPP
GEIGEIYMTWPGNCPRTEYINHEPLETDEGGFRSVGDIGYVDEDGYLYFSDRRSDMLVTGGENVFAAEVE
TVLKRHKKVVDAVVVGIPDEEWGRRIHAVVETTEEISAEELITFLLNYLPPYKIPKSFEFVDHIPRGDNG
KVDRSRILEECLAR
>gnl|CDD|468486 NF038345, wall_hydro_RipC, peptidoglycan hydrolase RipC. RipC is a peptidoglycan hydrolase, found in species such as Mycobacterium tuberculosis, that is activated by conformation change sent as a signal by the cell division-regulating transporter-like complex FtsEX. Members of this family are distinguished from more distant homologs by a Pro/Gly-rich region
LTRVLKRRLVGALAGLALLSGVLAATVQADPADDALAKLNELSRQAEQTTEAMHSAQLDLDEKLAAQRAA
EKKHAADAAAADAAKAQLATYQTAVDKVAAAQYMGGRTDGLSAILTAESPQQLIDQLSVQRVMATEMSAQ
MKSFRAAGEQAAKAEQASAKSAADARTAAEQAAAVRADLQSKQSQLQVQIAVVKSQYEALTPDQRAALAA
PGPVPAPAPAPPAADPAILAAPPGGIPPGDAAPPAGGGDGATVVQAALTRIGSPYSWGGSGPNAFDCSGL
VMWAFQQAGISLPHSSQALARGGQPVSLDDLQPGDVVTFYSDASHAGIYIGDGMMVHASTYGTPVRVAPI
SSAPIYNVRRY
>gnl|CDD|468487 NF038346, FtsX_actino, permease-like cell division protein FtsX
ARFVLSEVGTGLRRNLTMTIAVILTTAVSLTFLGAGLLLQRQVDKMKGYWYDKVEVSVFLCTDVSSTDPN
CAGGAATQEQRDAIRADLESDPLVPLVESVYYESKEEAYERFFKEQFKDSPLADSVTPDDMPASFRVKLK
DPETKYQVVAEAFSGRPGVESVVDQRELLDPLFSVLNGATWAALGLAAVMLVAAVLLIANTIRLSAFSRR
RETGIMRLVGASNWYIQLPFILEGVIAALIGALLAVGGLVAGKYFLVDGWLALSLTFIIAFIGWGDVVLL
VAPWLLLVGVLLAAIASWVTLRRYLRV
>gnl|CDD|468488 NF038347, FtsX_Gpos, permease-like cell division protein FtsX. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
IRTFFRHLREAFKSLKRNGWMTFASVSAVTVTLLLLGVFLLLILNVNKLASDVESDVEIRVYLDDDATDE
QIEELEDKIEKIPGVKSVTFSSKEEELEKLKESLGEEGKLLELLEGDNNPLPDAFIVKVKDPEDVKSVAK
IIEKLDGVEKVNYGQGVVEKLFKITKTVRNVGLVLIVLLAFTAMFLISNTIRITIFARRREIEIMKLVGA
TNWFIRWPFFLEGALLGLLGAIIPILILYFGYQYLYNKLNGSLLFSFLISLLPPNPFLLQISGLLLLIGI
LIGALGSVISVRKFLK
>gnl|CDD|439642 NF038348, T2SS_HK, histidine kinase
MQGTYDLSLVLLSLVIATLASYTALDLSALISLLDKPRLRRAWLAGGAAAMGTGIWAMHFVGMLAFSLPI
PLGYDLRETGLSLAIAMVVSYFALNAVTRAKLTRERLAAGGVLMGLGIAGMHYTGMAALQMQPGIRYDSA
LFVASIGIAILASTAALWLAHRLRTENAGRVIVKRIGAATVMGVAITGMHYTGMAAAHFAPNARCGAANG
ISGPWLGTTIALFTATILIVTLVISRFDARTMFLRGITDALEDLVQLRTAELEGALRQYELTTETLQRTR
VHMEREIEERKAAQARLEQEKDEQRRLIHELEETHVQLLQSEKLASIGQLAAGVAHEINNPIGFVSANLN
TLKGWVHSLLDVIAAQEAATPAHAAQTRAPLAAAGRDADLDYVRGDIMTLIDESIDGAMRVRRIVQDLRD
FSRPSGDEWSFADLHAGLESTLNVVHNELKYKADVVREYGDLPLVECNAAQLNQVFMNLLVNAAQAIPGR
GTITIRTTCDGDHASIAISDTGKGIPPDVMGRIFDPFFTTKPVGQGTGLGLSISHGIVEHHRGRIDVASE
PGRGSTFTITLPVR
>gnl|CDD|439643 NF038349, dPGM_arch, 2,3-diphosphoglycerate-dependent phosphoglycerate mutase
VILIRHGESDSNVKGILSDDINNYPLTEEGIEQAKFAADELKKLKFDKIYTSPILRAYQTASIIANELGL
EPVIDDRLRERGLGELNNKRIDENDHWKLKIPRKQREELGMEPWESLQKRMIEFIESYEGIVVAVSHSDP
IRALIGYILDLDEISSFGISIPNASMTAIDVEIGRILSIGSPLLSDEILKKLS
>gnl|CDD|439644 NF038350, taxis_HmpF, pilus motility taxis protein HmpF
MLYLAEVQKQKGGFIGGGKTELKLLACQRNDQSWSAVPGEEVIAAEEASKLNDGALVLVELSPNRQVQRI
QEAGRPLVNILQNFSRLLEKFKLQEEEIEQWKQSLTFQSQELNRREMEMEARLEQLEQMEEELERLEAQR
QEVETSREEIERLREELERNRQELEGAWEHLRGEQRRLEEQQAELQQGAVLDEEQARQLQELLDRLSSAV
APTETVREQLNLAFELVEQQQATLNPHWQQLEQQRQQAEQQQQEVERLSQELQQRQQEWQQAQASLEQAK
AQLKVQQATLESKQELLQILKLQLQAQEELYQQLSRLAAGSGDVGLSQKVDVEALENMPLEELEEIVQDL
QEDLEKDSRFVNDQEEELTLQQQTIEELQAKIAQASEFERLNLEEELADEQERYQMLNETLVGQRRNLQE
RQEILLQHQRVLRRRQGITVPESEEPKIDLEPILLQIESQRQQQSQELQKLESEIEQLRASIEQLQEMIA
QQTQELEQKRQELQQLEENLQQLQTATAELWGRVNLYQEALQPIQDSLDGLRQKLEAIAESLA
>gnl|CDD|439645 NF038351, cyt_ox_assem_30, cytochrome oxidase small assembly protein. Members of this family are small proteins, averaging about 40 amino acids in length as predicted, with a conserved core region just 30 amino acids long. The conserved region contains a highly hydrophobic probable transmembrane alpha helix. Members regularly are found encoded in the context of much larger cytochrome oxidase complex subunits, in members of the Burkholderiales such as Bordetella pertussis and Burkholderia sp
RAGNRRLGLILASIAAVFFVGFVVKQVLLS
>gnl|CDD|468489 NF038353, FxLYD_dom, FxLYD domain. The uncharacterized FxLYD domain, named for the strongest (but not invariant) motif, spans about 75 amino acids usually in the C-terminal region of a protein
YGSVTVTGTVENTSDRPIGYVEVTFNLYDADGNQIGRALANTSDLAPGETWKFEAPLLTDPSDVADYDVT
A
>gnl|CDD|439647 NF038354, trnsprt_adja_43, putative transporter small subunit. Members of this family are very small, highly hydrophobic proteins regularly encoded adjacent to transporters and likely to be previously overlooked small subunits of transporters
LLTLYVLIWPVIVAGVLFVLCRGFFKDWREARKEGRDLI
>gnl|CDD|439648 NF038355, FDH3_beta, formate dehydrogenase FDH3 subunit beta. Members of this family are the beta subunit of the FDH3 type of formate dehydrogenase as found in Methylorubrum (Methylobacterium) extorquens
ARMKFLCDTERCIECNGCVVACKNAHELPWGINRRRVVTLNDGVPGEKSISVACMHCTDAPCAAVCPVDC
FYIRADGIVLHDKDKCIGCGYCLYACPFGAPQFPKDGAFGARGKMDKCTFCAGGPEETNSEAEREKYGQN
RIAEGKLPLCAEMCSTKALLAGDAEVVADIYRERVVARGA
>gnl|CDD|439649 NF038356, actino_DLW39, DLW-39 family protein. DLW-39 is a small protein, restricted to the Actinobacteria. Its sequence features a highly hydrophobic stretch of about 15 amino acids, flanked by pairs of basic residues, and C-terminal region in which most members share the motif DLW. Members typically are about 39 amino acids in length when a start site supported by sequence conservation is chosen. The family is uncharacterized
KKLLLVAAAAAAGLLVRRKVQASKAERDLWSEATDPVD
>gnl|CDD|468490 NF038357, BN6_48550_fam, BN6_48550 family protein. This uncharacterized domain, named for its occurrence in the arbitrarily chosen protein BN6_48550, seems restricted to the Actinobacteria. This domain tends to be N-terminal in longer proteins that contain additional domains, such TIR-like (PF10137) or glycosyltransferase domains. The function is unknown
QELVVHLFAPLDGPGAAAAYAALRALWARCRDLLGMTEPIPGLGLPADLPADLPALPGEGVLAAAQRPGG
GYQAVLRREHDVLNLSVLLAPPPAAAPGWAELDRRWARLAGDLPDGLLGEARVYLALVPGGAAAPAALAA
ALRAALPAPAADGDWWRRGVTTPGGFAVWELGPGDDDRADRRLVVLAPPDADAELSAWTWSRGGPELPPL
ARYLLHAAKLRYQLRVWRAGRPLRELRRRLDEAVDRLLRLLPALARLLAAAAALARLQAGEAGLAATLAR
LRDMRRTVEIAAANMRAALGSDAGPGGPFADDRALAEWLLAQLDDDLAYLEAARERAR
>gnl|CDD|468491 NF038358, phophono_PhpG, CMP-5'-phosphonoformate--3-phosphoglycerate phosphonoformyl transferase. Members of this family, including founding member PhpG, are inferred to be the enzyme CMP-5'-phosphonoformate--3-phosphoglycerate phosphonoformyl transferase, conserved in a number of phosphonate natural product biosynthesis pathways
KVYLVALCGGADRPIAELGGRTPLEAAATPHLDALAARGQSGLLTVIDPGIPPESDSGAMALLGYDPLVY
YTGRGPLEGLGMGFWDPEGSSVAFRINFASLDPDSGRLDRRTSRDLTDEELQALAAEIRAGVRLDDDVRF
DLTAFGRHRGILALTSRTTPLSGNVSNTDPGFVREGPFGVPVAEPAPAPLPCRPLDDTPAAELTAELVNA
FVAQSAAVLEASPVNRARRAAGRRPANLLLVRDGGDTLPKLPPFSERYGLTLSMFGQVPAERGLARLIGA
RFTETRPAPGQPDPDYYRELAPRLLADPADVVFVHLKGPDEPGHDGRPHDKVRAIEAIDRHFVGPLLKAL
GPSDTLVVTCDHATPCELGIHSDDPVPVAVAGPGVPADEVTRFGERAAARGALPVERADELLPWLLG
>gnl|CDD|439653 NF038360, rad_fix_GrcA3, autonomous glycyl radical cofactor GrcA3. This small protein, like GrcA and GrcA2, is a lineage-specific small protein related to the glycyl radical active site-containing C-terminal region of pyruvate formate-lyase (PFL, also called formate C-acetyltransferase) from similar species. Because PFL is prone to damage and inactivation, this protein is made as a spare part that fills in for the portion of the protein that was damaged and lost. The distinct families we now call GrcA, GrcA2, and GrcA3 all have the surprising property of being much more closely related to some full length PFL than to members of the other GrcA-series families
VSEAQIDNLVSLLDGYAEKGGHHLNVNVFNRETLLDAQAHPEKYPQLTVRVSGYAVNFNKLTKEQQDEVI
SRTFHEAM
>gnl|CDD|439654 NF038361, rSAM_Sden_1168, Sden_1168 family B12-binding radical SAM P-methyltransferase
MTEQTNDTIPIDLRVKQTKLDIHLPQESPLRLYLAEKDETARVRKPRPGPQLVVVREPLGRIPRTLLVLP
PMCMYEGAVKRVVPPLGLCYIAGALEKEGIDVDILDCIVEGIDEETPVAPGVWNLGMTEERFRAYIAEND
FDVIGFTMIYSSDLQNLYRYAQIVKEVRPETTVIAGGLHASIYAERFLQDAVQDDVPFIDFVLRGEGEIR
LGDFLRNLADGRIDIHADGLAGWHDGKVFANPQFARITDLDDLPFPAYHKLPLEKYFAHNVPFSPYPRGK
RVMQLYTSRGCPIGCTFCASTNFSKQYRARSVENVIAEIRHYKDEYGVDEVQFADDNLTFDRKRAIELFE
KMVPLGLPWCTPNGIMVNTLSEPLVDRMVRSGLYQITLSLDSGSAETLKEKHRKPVDLTRVPDLMAYLDK
RGVLMHGTLVVGMPGETEEQIEDGFAYVEQLPFHSINVFIAQAIPGSELFEVSVSNGAITYEGALHIDTA
RSTLRLTDIDGERLEELVEGFLSRYNRAIYQRDPEAWERKYRDHKERMARICVGSASAITSTIIEASAES
>gnl|CDD|468492 NF038362, Sden_1164_fam, Sden_1164 family protein. Sden_1164, homologous to nucleotidyltransferases, is the founding member of a family that co-occurs with the Sden_1168 family of B12-binding radical SAM P-methyltransferases. The system to which these two protein families belong is uncharacterized
DECAIVLAAGENRRMGGHSLPKSLLPLRINDAEGPSFLSRHLELLRKAGVERVFLVVNSANRAYFEPFAS
DDVELVVVQTGVERTGSSVSMLAGLRALLAWRPEGPRTLITDADIVYEQALLDRVVDFNASSALFVIPRV
SGDEEEVRVYGRSQDQPVLIGKGLTSEMTKGLYLLGESLGLIKLDADEAPLAAELTTWIVGDPPNPRPYG
YGGRLSEHEEVWQYLFTLGRLIVVSVAGDLLFSECDFPEDRAHIREELFPAILRRD
>gnl|CDD|439656 NF038363, SecM_small, secA translation cis-regulator SecM, small type. Members of this family are a short form of SecM, found in members of the Pasteurellale, only three-fifths as long as the SecM of Escherichia coli. It is likewise encoded immediately upstream of the gene for SecA. The speed of translation of SecM and processing of its signal peptide provides a control mechanism that fine-tunes the translation of SecA
LFSHFHKTPFWSQLLLGMIAIFALPEIQELPNQPSTENYQTVINQSLQQILYAVSALQQEQQQQFLEQKP
AIVEVPPQAVQFQPFFAKSYFFDGAPIRAGPQF
>gnl|CDD|439657 NF038364, AglZ_HisF2_fam, AglZ/HisF2 family acetamidino modification protein
LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLAS
ECFMPLCYGGGIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDVKKNLFGGYEV
YTHNGTKKTKLDPVEFAKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDL
KEAIKQAGASAVAAGSLFVFKGKHRAVLINYPTPEELE
>gnl|CDD|468493 NF038365, Sca4_fam, Sca4 family spreading effector. Sca4 (surface cell antigen 4) is a surface protein of Rickettsia (intracellular pathogens) that mediates protrusion from an infected cell and engulfment by the adjacent cell, in order to mediate spreading
SKDGNPDISEFDPLNREFTEAEKQQQTKQEQELFSQPTLDIADDGFSVASSTQSTPSISVLSGSISPDGQ
TSDPITEAIRKEILEKQRDLIREQILKEYAANTNPDLAEQIAKEEKDKKFRAFLSNPDNRELIDKALENP
ELKKKLESIEIAGYKNVLSTYSAANGYQGGFKPVQWENQISASDLRATVVKNDAGDELCTLNETTVKTKP
FTVAKQDGTQVQINSYREIDFPIKLDKADGSMHLSMVALKADGTKPSKDKAVYFTAHYEEGPNGKPQLKE
ISSPQPLKFAGTGDDAVAYIEHGGEIYTLAVTRGKYKEMMKEVALNKGQSVDLSQTIAEDLTKVQGRSQE
TPQPIITPNQELKSSIETPTTTQVPPITPANQPLQPETSQMPQPQQAQPSPNGVLNAATALSGSMQDLLN
YVNASLTKEKDGNKQIDLIKEAATAILNNEKSDIAEKQANIIALAENTLNNKDLTPDAKVAGVNAILETI
KNDQNTPDLEKSKMLEATVAIALNSENLEPKQKQQMLEKAVDVGLSLKDDASRAAAIDGITDAVIKSNLS
TEDKGTILIAVDDKVNASELSNAEKQKLLGSVLKKGVEAQVLSPEQQQLMQQNLDKITAEQTKKDTIKKV
NGILFDPLSNTVLKTTNIQAITTNVLDSPAKVEIKSEIIEGITKTVAESPLEAKDKAEIVKGVGEAIATH
SDTSLSLPDKALIMESAEKGIAESKTDLPDRELMTKGLVEGIYEGKGNPEITKAVSSGIDKSNANPEEKE
ALKDIASEAALDRETQNLTKGLKGQNIEESKPRDDIYNKAQDVTDALKNVITPVLDAHPEKRVVSEEEVV
KKTSSILNDISQYVIEKVNNLRAMLSEDRNLKTAEEKKAESEKKVDELVKKFNEKSSTEEQQSFIKANLI
DNKTLSKEVRLQIIDNLLQEQAQKRAEAVENPSVKTEDVRVVSGKSELKPISKDEPDIEKAKMVVGRDRV
NIKDNIKIMGALMNARDSIQSENLNKSTPIKRESSFP
>gnl|CDD|439660 NF038367, OM_lipo_TUL4, TUL4 family lipoprotein. TUL4 family lipoproteins, including paralogs designated LpnA and LpnB, are highly expressed on the outer membrane in the genus Francisella
MKKIIKLSLLSLSIAGLASCSTFGYGSDDSIKANPDDNLANPDQADQQSTAEDKPTAKLKLKKTNQDEIK
ATIYTTYNNNPQGSVRLQWQAPEGSKCHDTSFPITKYAEKNDKTWATVSVKQGNKVCSGKWTANVVNDKS
VIASDSIEI
>gnl|CDD|439661 NF038368, P2_Rz1, Rz1-like lysis system protein LysC. LysC is an Rz1-like component of a phage lytic system, substantially overlapping although not fully embedded in the gene for the Rz-like LysB component. The phage lysis defect in the absence of a functional LysB/LysC system is appears in the presence of high concentrations of divalent cations
KRYAAGLTLLCLMLLSGCTSAPPSPAPTITYNGCPKVTPCPLPASAPRTNGDLSADLRQLEAALAACALQ
VDMIKACQERHDEKT
>gnl|CDD|468494 NF038369, GroEL3_Chlamy, variant chaperonin GroEL3. GroEL3, as found in Chlamydia trachomatis, is an atypical paralog of the normal GroEL, divergent in function and not encoded next to a GroES
MSDKENLLNYNTDKKLFLGIDKVFQIVKGFYGPAYSLSSKSFFEERGYSILSRIELSDPYENIGVDFAKA
MANKIHKKHLDGVTTGVILLYAFLKESYPFIDQGLSPYKLSSALKKMKEKLLEALQKHSWPLKDASKVKG
IIFSALPDPTIAEEFAEAFAYVGSEGFISLSQREGSSLQVTQGIKIPCGYASPYFISQDASRTTTLSAPR
IFVTDQKISSILSFLPLLQELSENQEHLLIFCKDIDPDVLATLIVNKLEGLLQVVVVTIPQLSTLDQTLA
EDIALFTGTTVFSQPPSSNKPPPERPSLGSCASAEISEDHTLLICGNHVPEVLKLKIRQLDEEIRTTSCQ
ESKKALIKRKHRLQSSVAIIPVKEDTEPLYSLALKTLNSAKESGYVPGGGAALFYASLNLGSEKELSEEE
QAAIHILQTACRAPLEQLINNAQLDGKAVIDKLCSLGTPSLGFNVLSQQIEDLIASGILDPLATISDIFS
CALETAITILSSKVII
>gnl|CDD|439663 NF038370, GroEL2_Chlamy, variant chaperonin GroEL2. GroEL2, as found in Chlamydia trachomatis, is an atypical paralog of the normal GroEL, divergent in function and not encoded next to a GroES
MANSFRNQEQGLQAVLRAARVISQMFSQTIGPYGFGTIVHNVQDPRITQDSQRMLKDILFPDVFENIGMK
LIRDAALQTRNRFGDGAKTTALLIEALLEEGMAGIQRGLDPQEFRRGMLLAEKKIQEIFYRETFSITDLE
HLVCVSSIARRFNSDIASVLSSAVRYGGKNGYYILEEHEGKSTHWFAEEHAVWDFGYASPYFITHAETGT
VEYSQVYILVSESPLHSSDPSFLTFLEAVVQAGKTPLVILAEAFDRELLAMLEINQIEGGFPVCAVRVGG
KHARESLEDIAVLTGASLLSEMSFEDSEEERITNRLGFVEGICISSTSLCIPREVDNKKRWAEHCSLLQD
KLEHLHGEEARARLRKRLARLSSGEVRICIAEDSIPQEELAYITSSVRAMTESLRSGCLPGGGCSFIRAA
REISVPLSLSPGERFGFLAVLSAVERPFRAIVARSGRVVEEVFSQVFSQADWRVGFNGLSGFVEDIVAQG
ICDGASCIQHALSHAVGTVGLLLTSALFFASQEPMFREENSEE
>gnl|CDD|439664 NF038371, phegan_RiPP_fam, pheganomycin family RiPP precursor
MEREIVWTEIEESDLAEIVSDSNVKDIGIVSSSNVKD
>gnl|CDD|439665 NF038372, tryptorubin_fam, tryptorubin family RiPP precursor. Tryptorubin A is the founding member of the atropitides, a class of polycyclic RiPP natural product featuring crosslinks through aromatic amino acids
MKLLFSLKNKLTAEKSLKAYAWYIWY
>gnl|CDD|468495 NF038373, cittilin_RiPP, cittilin family RiPP precursor. Cittilins, such as cittilin A from Myxococcus xanthus, are RiPP natural products. Known examples of the peptide precursor end with sequence YXYY. The precursor may be only 27 amino acids long. The mature form contains bicyclic tetrapeptide scaffold with biaryl and aryl-oxygen-aryl ether bonds. The biosynthetic gene cluster includes a cytochrome P450 enzyme and a methyltransferase
MKKAAYSLAVFLRIARKDRLTAPYIYY
>gnl|CDD|439667 NF038374, omphalotin_tail, omphalotin family RiPP precursor domain. This HMM describes a RiPP cyclopeptide precursor peptide region that appears as the tail region of certain self-sacrificing fungal methyltransferases . The founding member of the family is omphalotin A precursor region
MPSSLLDAARQSGEEASQNGFPWVIVVGVVGVIGSVVSSA
>gnl|CDD|439668 NF038375, crocagin_RiPP, crocagin A family RiPP precursor
MKKTIKQISAGDRSKKGNIYW
>gnl|CDD|439669 NF038376, microvionin, microvionin family RiPP. The antibacterial RiPP peptide microvionin, from Microbacterium arborescens, is the founding member of lipolanthine-type natural products
MSLEQLEALDASSEAAEMAASLGSQSC
>gnl|CDD|439670 NF038377, TglA_fam_RiPP, TglA family RiPP precursor
MTQPTVTPVIANEHTTEVKTEPAPQATEEALFEEFDLDDIEVIESKVFA
>gnl|CDD|439671 NF038378, DNZ54_00345_fm, DNZ54_00345 family phage region protein. Members of this uncharacterized protein family appear to be membrane proteins, and are found in bacteria encoded within prophage regions
MKKLKTSWFFDLLLALLLLVSLVYPQSHAVNLVAAWAWFECLLCWVVGFAGLYACTLTGGDRKEVRAFLL
RFCRLPDKVPLRWYHRLFIAVFLAGAGWKLTALFYLLTVVTFLMIRSELRQAIA
>gnl|CDD|468496 NF038379, amino_Aden_PurZ, succino-amino-deoxyadenylate synthase PurZ
VDVVVDGQFGSTGKGLIAGYLAERAAPDVVVRAAGPNAGHTYIDDEGRKFVHRMLPNGIVSPPLKQVLIG
PGSEIDLEVLREEIEELEDAGHDVGKRLLIHEQATVIELHKHVEEEAGPMTKIGSTKKGIGAARAAKIRR
NPSTLGDAEGDFGEGAVRDQPWEIAERVVDNALYDFALQAAERIQIEGTQGYSLGLHAGFYPYCTSRDCT
PADFLADAGIPLPNVDAFKVVGTARTYPIRVAGWSGNSYPDQGETTWEELGLPEELTTVTKKVRRVGTFS
AEQVREAVQANG
>gnl|CDD|468497 NF038380, phage_DpoZ_1, aminoadenine-incorporating DNA polymerase DpoZ
NYEIIALDTETTGLEYWLDKAFGFSVALSLPDGRSWYWDIRDQPNALQWLRDILLRSYRLVVNHHASFDY
QMLRAAGINIPLDNWDCTMIRACLINEHLLSYDLDSLAKKYLGASKDNEIYEELAAIFGGKPTRKAQMPN
LARAPPEIVAPYAKSDARLALELWLWQQEEIERQGLQRVVELERRLFPVLIDMEWRGIRVDLEAAEAAIP
ELDKVIDQLQKELNEIAGFEFNVNSSPQIRKLFKPKKISKGQWVAIDGTPLETTDAGKPSLGADALREIK
HPAAAKILELRKLIKTRDTFLRGHVLGHAVGGGVHPNINQTKGEDGGGTGTGRLSYTDPALQQIPSRDKA
IAAIVRPIFLPDEGQVWLCSDLAQFEFRIFAHLVNNPSIIAAYAEDPELDFHQIVADMTGLPRNATYSGQ
ANAKQINLGMIFNMGNGKLADKMGMPYEWEEFTFGKEVRRYKKAGPEAMAVIENYHRKLPGVKELADRAK
AVAKERGYVRTAMGRRLRFPGGMKTYKASGLLIQATAADLNKENLLEIDEVLGSLDGRLLLNTHDEYSMS
LPEDDVRKPIKERVKLFIEDSSPWLRVPIILELSGFGRNWWEAS
>gnl|CDD|468498 NF038381, phage_DpoZ_2, aminoadenine-incorporating DNA polymerase DpoZ
ILPSDLLHLMDTRGLFPGSPVAVDTETSGLWVDAGARVSTVSVAWAVDDDQLAEWDFVLGGGEQYLWDTG
IWTLRKEPTAGARSNEWAKGDWLQDHWVLSFAWPFDQGVSGTGKPEDNTDETLWPGQGGLLEWTPDLPEA
DAENLPLSEWTALLEWLRLVGEDVGLTMHNAKFDIHMMRAGVRYRWPGIGDDLMDLVDWDTQGGNDLWVG
WRTATSGKPTTSLKPATEWLWGESEGDEKHVISAYLKKKKLPKGRWDLMPWDVIAKYADQDARLTCRLRI
WQEDEQKRIKGCQGKVDWMEGGWGRGWAPEAFERRMETMRMLYRVERRGLPFDIEEAQQASAELKFRIAE
VEKVLPFKLGTVTLPMAKHYWFGSGDKSGEKGKGVRGLGLPPYATTDGGAPSVDAADLGKMIRDGLPLVE
EWRAYKKLTDAKSRWYEGWGTRAGADGRLRTGFRQNGTASGRFSVEEIQLQAIPADYKVKGYGLDGIPSP
RDLIGSGVPKGYELWEMDLAQAELRVAALFAKCQRMLDMIDAGMDLHGETAKELFDASPDDENWGQRRQV
AKRGNFSLIFGVGWATFQATLWKEAGIDLSDREAQVLIKAWNALYPEYKRAINVHEARVMRRYDKYGVGW
ILDMATGERRWFTKWDVEFFDQRRQELREGAHKAFNQRVQPALAQYGIDRWLLEDRYLSSQLTGEELEHG
GAGLVLMVHDSSVLLLPNERAEEVTADLIRMGVELWAERFPGLPGGLDASAWN
>gnl|CDD|439675 NF038382, RaxX_RiPP, RaxX family RiPP. RaxX (Required for Activation of XA21-mediated immunity X), produced by many strains of Xanthomonas, is a RiPP microbial peptide family. Characterized members have a sulfated tyrosine and interact with the rice immune receptor XA21
MNLLNKSPANGARSLQREAGAKGRLEPLDERLWKHVGGGDYPPPGPNTRHDPPPPGNG
>gnl|CDD|468499 NF038383, lipo_LIC12048, LIC12048 family lipoprotein
IFRIVVRFLILFLLIPFVATCLSDKGFGTMGNVDLAKATWLVAEKVPLVVDKEGVPVKPGGGGSVPVTPV
NGLFNLPPGTKVSAQALGGTIDPTGTTIVNDFDGDGILNQNETTTNVWVADYPQIETVIAPPVTLKIQIL
KSSTNQSDEIVSEINSDDFESSKNEGSEKIHQNELNLRTVQFQDSFSNETEFGTSNESSTSVGVTTGYIG
VVSLGLNYSNSSSNSWNKKNATSATTTKWADKPFKNNIDRDAWNLKSDSSSNKARKYRSEKSTKINSTSK
VEPNAGYVRAALYIKNLSVNMPVKLSNILCSLMFETGTGELVPVQSFRLRNDDYSLFEVEVYGGSEFGPY
VVELPNLNTAEVEKAIASGYTPKIMIVDYTMTHVADSNYKSSLLNFTGDNLKIIEENAKGRTSLIKVFGP
NIREMYRVAAFDTPNVSNPCNTKTATVFSPGISLKKALERISCSGLNITFKDYVIDLSESAPTLGESRIH
VKGIKSFGGISTNLPCEDETSTGSDGVSRTACVQKPYSQWTDSEKANSGVWAIYSKGKYYSPTEYWTDGG
NIRKFDPWRGAVAAPMVKGVDSIIWAGDYYDLVYISFKDLIKVEQKFGTNPLETGEGFPLNTAWDLKQLG
EHPYYPDTNSLYLGEVGFGEKVELKIKLDKTKYLNPNFGTPEDTGTYQYFTNFSYNPQVSTDRYNIDQAA
DFEISLGFGGTRTDWFHIIKDLSSSDPYKLKNCGTTLDFITQTYTLCVQLPTLSTTVDPAISLVKLYIRP
SLNSAYRKTIWPLHYTDVRKMRGELGVPIVIGTTTIYLANSYGNIEVGDTLYIQGDENNYYVVQSVLPPA
PDGSFDVQLDSGVQIDAPKTTSVYVPGTLTAPDVRLSVDTGFVTDWNAQVNSSFPTNYDQPQYLPFLNSG
SVSCSTLPFHPSSCLGFTPDYNALNWMGIYNEGVALWNSWADGGDFSSFLYSGLFRLTANTGKSYRLESS
NTDFTLSADVNAVPLGEPVSVSNGDVAMVVWRQDTTILGRYYQISTGTALGNPFDINTTTAASTGKYIVK
AKNGKAVIIWENGNDIYISVRNLATAATIVSETKVVTRNTPGSFYSRIDVAVGNDRALVVWNDVYPLWYP
CSLFWFCSGHTVYNYSVAGRIYNLDTGAATAGSFNIDTVTSTNAWRYYEVAADGNGGNQILVGWHYSDIS
SNSHTIDSRVYNLTTGTIVGSDKTLSSESVRPGDGLFVGASGGKGLVIWRRPDGTILGRGIDLSTGTLLG
TSNLAIDTGPVDSLKLSLFGDTGLITYSKNGKDIYLKVVNLQDGQLLYPNALSLGSSKTADQRKPGVTVL
SGNKILTTWEHTEGTKRTIRGRTATLSPFTLKGSGEFFLSTTNEGTQTGPSVVVYSGSGLPAWLSQDKTQ
QRIRGAKLDLNNPGALQYGLNNFFVAPLIERDYTIRAKIKY
>gnl|CDD|439677 NF038384, zinc_YnfU_fam, YnfU family zinc-binding protein. The founding member of this family of putative zinc-binding proteins is YnfU, from the Qin prophage region of E. coli K-12
MSFFDALKRFRNRLVKVTCPKCAKVSEQSASKVQKNATLICPKCGALFLPKE
>gnl|CDD|439678 NF038385, IS66_access_TnpA, IS66-like element accessory protein TnpA
YRTLLLDALRLRFDESLSYRAIGRQLGVSKSTIHSLFQRFLRAGLSWPLPDSMSADQLDAALYPNRKKPP
SAPTVTRPVVWKKIRRPNFSREFKIRLVEQTLQPGACVAQIARENGINDNLLFNWRHLYRNGLLQPDNEQ
ETALLPVTLTPEPDPTIPVPAQDPEQQNTTADSLCCELVLPAGTLRLFGP
>gnl|CDD|439679 NF038387, CBS_CbpA, cyclic di-AMP binding protein CbpA. The founding member of this family, Lmo0553 from Listeria monocytogenes, now called CbpA, binds cyclic di-AMP, a signaling molecule, through its CBS (cystathionine-beta-synthase) domain
MLLKSLVKPKEDLTTVKEDATLEEALKILEDSGYRCVPILDETGKIFRGNIYKMHIYRHKSRGGDMSLPV
THLLKNATKFISVNSSFFKVFFTIKDLPYIAVLDENNHFYGILTHSSLLNMLSQSWNVNTGSYVLTVASS
GERGDLAKMAKIITKYTSIASCITLDEQSDELVRRTLFTLPAGVDEETLDKIVSRLERKGFRVVEIEDL
>gnl|CDD|439680 NF038388, sigmaX_act_ComW, sigma(X)-activator ComW. The pneumococcal DNA-binding protein ComW, critical for natural transformation, interacts with the sigma factor that is a master regulator for competence, sigma(X)
LQKIYEQMLDFYDSIEEEYAILFADDLEWEHLHLKFLIYYLVRYKIGCMKDFIVYHYRAAYRLYLEKLLM
SRT
>gnl|CDD|468500 NF038389, ArsS_fam_HK, ArsS family sensor histidine kinase. ArsS in Helicobacter pylori is a sensor histidine kinase participating in a two-component system that controls the response to acid conditiions encountered during the process of gastric colonization. This HMM identified ArsS itself but also a broader collection of apparent orthologs from closely related non-gastric colonizers such as Helicobacter hepaticus, Campylobacter jejuni and Wolinella succinogenes. See BlastRule NBR014349 for specific identification of ArsS itself, distinguished by a signature His residue that becomes protonated at low pH
HSIFFKITILFAIALVSVSALFLILLKYQKENYNEELNKKYSLIANTLLQLYQKNINEEELEKYLKNFGF
MPITDKKLEKEILEIGKNKFILKENGSFRILKYNDKIYLLIKNDGFSLLLEDNEKKSYRYYYIIVFFIFL
ILLLLILYISVLKSLKPLKKLKKQIKKFANGDFDFIKSESNGDEIGEVANEFDKAVKKIKALNESRQLFL
RNIMHELKTPITKGRIVAEMLEDEKQKERLISIFERLESLINEFAKIEQLTSKNYKLNKKEYRLSDIIDE
AIDMLMIDDSSVIIKVSLEDFKLNVDFELFSLAIKNLIDNAIKYSPDKKVTIEIKGDKIEFKNKGEPLEE
PLEYYFEPFFKGNEKSKSGFGLGLYIVKNILKAHGFKLEYEYENGYNIFIIK
>gnl|CDD|468501 NF038390, Nsidase_PpnN, nucleotide 5'-monophosphate nucleosidase PpnN. PpnN (pyrimidine/purine nucleotide 5'-monophosphate nucleosidase), widely conserved in gamma proteobacteria, plays a role in purine homeostasis. It can bind the the stringent response alarmones ppGpp and pppGpp and then, because of allosteric changes, have a much higher rate of cleavage of preferred substrate GMP. PpnN was previously known in E. coli as YgdH
IARISPEGSLDLLSQLEVDRLKDSSSGGLYELFRNCALAVLNSGSQTDDSKELLEKYKDFDINVIQRERG
IKLELINAPASAFVDGEIIRGIREHLFAVLRDILYVSNEIEELPRLFDLNSSEGITNAVFHILRNAGVLK
PGEDPNLVVCWGGHSISREEYDYTKEVGYELGLRGLDICTGCGPGAMKGPMKGATIGHAKQRIKNGRYIG
ITEPGIIAAEPPNPIVNELVIMPDIEKRLEAFVRLGHGIIVFPGGVGTAEEILYLLGILLHPENRDQPLP
LILTGPAESAAYFEQIDRFIGATLGDEAQSKYQIIIDDPEKVAREMKEGMEKVREYRKATGDAYYFNWSL
KIPPEFQQPFEPTHENMAALNLHRDQPPHELAANLRRAFSGIVAGNVKEEGIRAIEKHGPFELHGDPELM
AAMDKLLKAFVAQGRMKLPGSEYEPCYRIV
>gnl|CDD|468502 NF038391, streptophobe, streptophobe family protein. Members of this family of uncharacterized probably membrane proteins are restricted almost entirely to the genus Streptomyces, and are highly hydrophobic through the aligned region, hence our coinage of the name streptophobe. Member SCO7274 from Streptomyces coelicolor A3(2) was shown to be expressed as protein
AGHGWLQALAAVLAALAAMAVVAALGLWAAGAADLPDGAFGPVVAAVVVLAVGGSVELSGDAGALALAHA
ALTVMPLSVTLVGALVLGAGFLRPLRHRAVAGAGELAARAARVAVLWLLALLGLAWAARHTFTISLGDLG
LGDLGDLGGLLGDAPTVGFTVDVPPTLLGGLLWLAGVLALALLVSRRAPLPRRLLRFHRSVRPAASAMVT
LLLAAVAAGLVAALVAAATRGHPARTAAVALLGLPNLVWLALTLGLGAPWEGRVQGPFGLPLPHVLDEVL
RGPDDSTLDLGTLAELDGRVWWLLVAAAVLLLAAGFLTAVRSPARTRAWRHALRLGVALALTLLLVCLLT
RVSAHYGLSVLGIGDLGGLGGGLELRPRLWLALGLGALWGLVAGFLGALLARA
>gnl|CDD|439684 NF038392, div_DrpB_YedR, cell division protein DrpB. DrpB (division ring protein B) is a non-essential cell division protein with a limited taxonomic range, found in enteric bacteria such as Escherichia coli
EEKATRSPGGKLALWVFYAFCGYFVWAMVRYVWVVSRIQSVPGAGIEGDLGSTSGKWLGALLGFLVLGVV
GAILGGIAWYTRPRQS
>gnl|CDD|439685 NF038393, lipo_LIC_10705, LIC_10705 family lipoprotein. The LIC_10705 family of lipoproteins, found in the genus Leptospira, includes tandem-encoded paralogs such as LIC_10705 and LIC_10706 in L. interrogans serovar Copenhageni str. Fiocruz L1-130
MLKQILLLILISYLNLNCDDSQGTSTGDYHNEFMLEYSFFFILPNLDLNQYCPPTDQIPILEPGTYTRYM
SEGDTYIFDNRARLNQSATSGSSEYFTFTIQENPGQEIKLTSPECGTSSNEYKADDDSGLSGQLETVYIG
LKVPPLPPKRSGFFTKLKAISGSGTITFTTPSAPDPPQ
>gnl|CDD|439686 NF038394, lipo_LipL32, major surface lipoprotein LipL32. LipL32, a surface lipoprotein, is found in the genus Leptospira only in pathogenic species, where it is the most abundant surface protein. LipL32 belongs to a broader family of surface lipoproteins (see PF12103) found also in other host-colonizing bacteria such as Pseudoalteromonas tunicata
MKKLSILAISVAILASFTACFGGLPSLKSSFVLSEDTVPGVKTVKTLLPYSETVNYWGYIKPGQAPDGLV
DGNKKAYYLYVWVPAAIAEMGVRMISPTGEIGEPSSGDLVSDAFKAATPEEKSMPNWFDTWIRVERMAAI
MPDQIEKAAKAKAVQKLNDDDDGDDTYKEERHAKYNSLTRITIPNPPKSLDELKNIDTKKLLVRGLYRIS
FTTYKPGEVKGSFVATVGVLGPPGIPGLSPIIHSNPEELQKQAIAAEEALKKAASGAKK
>gnl|CDD|439687 NF038395, nocathioamide, nocathioamide family RiPP precursor
MGAANAEMAEPGYDDFDLEIIDASLFDDEQSRPAAPACHTLSSLPCCAN
>gnl|CDD|439688 NF038396, NF038396, NF038396 family protein. This small, highly hydrophobic, uncharacterized, strictly actinobacterial protein shows hints of sequence similarity to the envelope stress response protein PspG found in some proteobacteria. It sometimes occurs as a tail domain attached to dihydrofolate reductases
PEALFFLGYMLFPLLALVTAVLGLWLVLTGRKIAGLIFLLVVTQVFVFGGLWAINRRKR
>gnl|CDD|439689 NF038397, AB5_pltB_like, subtilase family AB5 toxin binding subunit. Members of this family are the B subunit of AB5 toxins such as the ADP-ribosylating cytotoxin subtilase, which is related to pertussis toxin. These B subunits, in general, form homopentamers. This family does not include any related pertussis toxin subunits (such as PtxB, PtxC, or PtxE), although some members of this family may have carried legacy annotations saying they are pertussis toxin proteins
KKILSVLALLLLFLSSNAYAEWTGDNTEYYSNVVINNLHTGQYDSGPYFCIKAVRSGGTPISACSVSNYS
IWAASFDTLYEQAMYYYTTGQKVRVYYKPNVWTDPDFVKAFSSNALVGFSTCSSNDYCFGPT
>gnl|CDD|439690 NF038399, NH_RiPP_Os17, Os1348 family NHLP clan protein. This HMM describes a region about 63 amino acids in length, including RiPP precursors Os1348 and Franean1_4349, showing some sequence similarity to both NHLP family RiPP precursors and to the nitrile hydratase alpha subunit itself. Some members of the family are long proteins, with this domain at or near the N-terminus
EAVERLLGRALTDEEFRAALLEDPEAALKEAGFDLTPEELAALKGLDAEALEAFAESLDERIS
>gnl|CDD|439691 NF038402, TroA_like, helical backbone metal receptor
RVVSLVPSLTEAIAATAPELLVGATDWCTHPADLDVARVRGTKNPDRAAIAALRPDLVVANQEENRELDV
DRLRAAGVPVWVTRIETVDEALASLRRLFTEALGVPVPGWLDEAEREWAAPAPAPRRRAVVPIWRDPWMV
VGRDTFTGDLLARLGLRNVFADHPERYPHVDLDELDAAGPDLVLLPDEPYVFTADDGPEAFPGLPVRLVS
GRLLTWYGP
>gnl|CDD|468503 NF038403, perm_prefix_1, permease prefix domain 1. The permease prefix domain 1 is found as the N-terminal domain of putative permeases resembling ABC transporter permeases, and also of hypothetical proteins of unknown function. In at least some permease families, this prefix domain is only variably present, and may be replaced by a different, seemingly unrelated prefix domain
LFRNLFRRRRARRELKEELRSHLEDKVEELIAAGLSEEEARRAAIREFGDPDELREELR
>gnl|CDD|439693 NF038404, perm_prefix_2, permease prefix domain 2. The permease prefix domain 2 is found as the N-terminal domain of putative permeases resembling ABC transporter permeases. In at least some permease families, this prefix domain is only variably present, and may be replaced by a different, seemingly unrelated prefix domain. This domain is considerably less common than permease prefix domain 1 (NF038404)
PPRWADRLLEWFCAPHLLEEVQGDLHERFAQRVARVGERRARWRYWLDVLGFLRPFFIKRKP
>gnl|CDD|468504 NF039170, SdrH_fam_CTERM, SdrH family protein C-terminal domain. The founding member of this family of staphylococcal proteins, SdrH from Staphylococcus epidermidis, is one of three MSCRAMM family proteins, but is atypical in lacking a recognizable LPXTG-like C-terminal recognition sequence for cell wall anchoring. This HMM represents the entire region C-terminal to the repetitive, low-complexity region that is a feature of all members of this family. That repetitive region consists mostly of Ser-Asp dipeptides in S. epidermidis but has radically different compositions in other species
NRFNQLATGSFKYNPFVINQVNRLSEDDGNVSDQDIYNLLRKQNFSDNSYLNSLQQSTNYFRFQYFNPLN
ADQYYKNLDKQVLALITGEIGSMPDLKKPKDKDKKSKGQYEKHKKDEQEGTKTEKKNMKTDTKLKFSRTL
ITLIGAIIVIFIGVIILYLYKRR
>gnl|CDD|439695 NF040463, all3515_fam, all3515 family Zur-repressed PEP-CTERM protein. Full-length members of this family have an N-terminal signal peptide and a C-terminal PEP-CTERM (or related) recognition site for sorting and cleavage by exosortase, a probable transpeptidase for attachment to the outer membrane. The founding member of this family, all3515 from Anabaena sp. strain PCC 7120, showed the greatest upregulation of any protein to challenge by zinc deficiency, over 250 fold
YYVGVDGLATLTSGTYAGLANPNYNRLTLLFAHGFEDPTSNHFHGIGAYSYSGPADSPTVNPTNTNNRLP
EPYTGQPPLTLLPGSGVFAGKLVSGLTPEDEYSDLTIAPVQSLSGAAAGSEEQYLFNSSGGRWNGSLDGA
TIGLELVSISPGLNVGDSSGPDLFASVGDIYTLGSGDSFSFTPVFWTDASAPPGTYSATFRLVDLSGNSA
FGDSGTFSFDFQVVPEP
>gnl|CDD|468505 NF040464, SCO3374_fam, SCO3374 family protein. This HMM describes a family restricted to the genus Streptomyces. The HMM produces scores that are significant, although below the cutoffs set for this model, to about 10 percent of the proteins in the seed alignment of Pfam model PF09250.11, designated "bifunctional DNA primase/polymerase, N-terminal"
WYENELGWATVPGPPVRLVTGLRFDVLDVPAEAGAAALRRLGPGSPVALRGDRMRLLVAAGSAEELPGLL
DWLEWGGLALDLTALGAGGRMEAPLPPGPGPAGAGPPGPRQGAAVWLRPPEPGCEVEASLPALSALGGGG
GAPDLVRLVDTAATECHRVRLRR
>gnl|CDD|439697 NF040465, T7_gp19.5, gp19.5 family protein. Members of this family are phage proteins in the family of gp19.5 of phage T7
AVLLTLLKHRVTYRFLAVLLAALGVASGTQHLGQLETLVCSVLTCSD
>gnl|CDD|468506 NF040466, ydjY_domain, YdjY domain. The founding member of this family is the poorly characterized protein YdjY, an apparent lipoprotein, of Escherichia coli K-12. Many members are lipoproteins. YdjY and other members of its branch of the broader family have an invariant GCxxCxxxC motif
VVVDKKKKEVTVPAEVNGYEGEPLEHLAVFPDGTKEHESVLATDAKPSDFHAALLLLGAKPGNPLTFDNP
EGKPPEGDPVDVSVTWKDDGKEKEVPANEWIRDSNGKPMDAADWVFGGSGFWGGAAYAANTGCIICLDSC
PVAIISNAAYSSGADGELLFEGNTEVLPPDGTPVTVVLRPA
>gnl|CDD|439699 NF040471, ydgH_STM1478, DUF1471 family protein YdgH. YdgH is the rare paralog in the DUF1471 family (PF07338) with three tandem copies of the DUF1471 domain instead of just one. Note that STM1478 from the Salmonella enterica model strain LT2 is also called SssB
MKLKNTILASALLLSLTALSSAQAAQELTPEKAAALKPFDRITVTGRFNAIYEAADAVSRRADKMGAASF
YIQDTNDVNNSGNWRVTADLYHKDAPKADKDPKYRVFNGVKELPKDEAYLLEPFDTVTVSGFFRSQPDVN
DAIAKAAKEKGAASFFIVRQVDANSGGNQSITAYIYKADAPKRVVQSPDVIPADSDAGRAALAAGGAAAK
KVEIPGVASSESPSSKVGRFFETQSSTGGRYTVTLPDGTKIEEVNNITAAQMVPFDSITFTGHFSSMTDV
SYQVAKRAAKKGAKYYHITRQWQSNGGNLTISADLFK
>gnl|CDD|439700 NF040473, peri_YbiM_McbA, DUF1471 family periplasmic protein McbA. McbA (YbiM) is a member of the DUF1471 family found in Escherichia coli K-12, where it is one of many paralogs, but not found in Salmonella enterica LT2. Many members of the DUF1471 family of small enterobacterial periplasmic proteins participate in response to various forms of stress, such as low pH
MKKCLTFLAATVLTGMSFAAFAAQPMSSPDTGQLRPAGTVSATGASNLSDLEDKLAEKAREQGAKGFVVN
SAGGKNQMYGTATIYK
>gnl|CDD|439701 NF040474, peri_RclB, reactive chlorine resistance periplasmic protein RclB
MFKKTVLFATLLSAPMAFSANAQDKTEVKHVSVSSVSATPSVLEDAIAKLAQKKKASSWKITSMRIDNNS
TATAILYK
>gnl|CDD|439702 NF040475, chlor_reg_RclR, reactive chlorine-specific transcriptional regulator RclR
MDALSRLLMLNAPQGSIDKNCLLSSDWQLPHAAGELSVIRWHTVTQGAAWLEMPTGEALTLRPGQVVILP
QNSAHRLRQSGEEETHIVCGSLRLQTSSRYFLTALPEVLLLAPEQNSPESHWLLAAIALLQQEAESPQPG
MDALCSQQCATMFTLAVREWLRQNTQAKSVLNLLLHPRLGAVIQSMLESPAHPWTVESLAQRVHMSRASF
AQLFREVSGTTPLAVLTRLRLQIAAQMLSREALPVIVIAESVGYASESSFHKAFVREFGCTPGEYRRRVK
ALAM
>gnl|CDD|439703 NF040476, chlor_memb_RclC, reactive chlorine resistance membrane protein RclC
MKQLLGLLSRGDRLGLTLMRLAIAIVFLWIGLLKFVPYEADSITPFVANSPFMSFFYEHPEDYKQHLTHE
GELVPANRAWQTANNTYGFSNGLGTVEVLIGLLVLANPVSRRLGLLGGVLAFLTPFVTLSFLITTPEAWV
PALGDAHHGFPYLSGAGRLVLKDVLMLAGALLVMADSARRLLAE
>gnl|CDD|439704 NF040477, chlor_oxi_RclA, reactive chlorine resistance oxidoreductase RclA
MNHYQAIIIGFGKAGKTLAATLAKAGWRVAIIEQSAQMYGGTCINIGCIPTKTLVHDAEQHQDFSTAMQR
KSSVVGFLRDKNYHNLADLDNVDVINGRAEFIDNHTLRVFQADGEQELRGEKIFINTGAQSVLPPIPGLT
TTPGVYDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQ
DQGVELILNAQVQRVSSHEGEVQLETAEGVLTVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYL
RTTADNIWAMGDVTGGLQFTYISLDDFRIVRDSLLGEGKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARA
SGADIQVVTLPVAAIPRARVMNDTRGVLKAVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLR
DQIFTHPTMSESLNDLFALIK
>gnl|CDD|468507 NF040479, porin_porB_Neis, trimeric porin PorB. This HMM describes PorB, a trimeric porin found broadly within the genus Neisseria, including in N. gonorrhoeae and N. meningitidis
MKKSLIALTLAALPVAAMADVTLYGQIKAGVEVSRVKAHSNGQKTKSKTATEIADFGSRIGFKGHEHLGN
GLNAIWQVEQKTSVAGTDSGWGNRQSFIGLEGGFGKVRAGKLNTQLKDTGDNVDPWESNNDALGLGKITR
VEERKVSVRYDSPVFAGFSASVQYTPRDNANPSDKRDHAVKSRESYHAGLNYENSGFFAQYAGGYKKHAV
VTTDGLVKDGQVHRLVAGYDANNLFVSVAGQYQDAKLDVANDANKKNETTEVAATAAYRFGNVTPRVSYA
HGFKAKVDGAKDNGTQYDQVVVGADYDFSKRTSALVSAGWLKEGKGDDKTETTAGLVGLRHKF
>gnl|CDD|439706 NF040480, CGLAU_01105_fam, CGLAU_01105 family protein. Members of this family are found, so far, almost entirely in the genus Corynebacterium. The function is unknown. The model was built, in part, to prevent misannotations that might result from a now-corrected improper inclusion of a family member in the seed alignment of Pfam model PF05407, which represents an endopeptidase of Rubella virus, MEROPS family C27
DNLREAGDALLSAGSALGDVVGDFAGRFREDRDEEDGLLDRLKAAAAEARERLNSASTDGDVRAAAASFA
GEAESIFRDLAGSVRRAADETRDSEAADDAKAAFGSAVAEVRESFDDAVDKVRARRDESAEGAVDDLRSR
LDDLVARVQDQFSGEDAAPDIIDGEVIS
>gnl|CDD|439707 NF040481, YdcK_fam, YdcK family protein
MNKYRLSEETRAFSYQEDGTKKSVLLRQIIALRDFADVKAGTAGGWVDDESALSQQGDCWIYDQNSVVFA
GARIRGNARLTGPCVISHGARIGDNAWIDAAEISHGARISDNVTVQDSVVRGECRIFGDARVLHHSLIIA
AQGLTADRDQILQIYDRATVSASRVVHQAQIYGDAIVNHAFIEHRAEVFDFAIIEGNEENNVWVCDCAKV
YGHARVIAGREEDAIPTLRYSSQVAENAVVEGNCVLKHHVLVGGHAVLRGGPILLDDHVLIQGHARITGD
VLIEHHVEITDDAVIEAFDGDAIHLRGPKVINGEQHITRTPLLGSL
>gnl|CDD|468508 NF040482, auto_BafA_Cterm, BafA family autotransporter C-terminal domain. BafA from both Bartonella henselae and Bartonella quintana, and possibly all Bartonella BafA, are mitogenic autotransporter virulence factors that help induce vasoproliferative lesions during infection. This HMM represents the more conserved C-terminal portion only, as the passenger region is more highly variable in length and sequence
GGQIKGSSAYDTVIYGQGETLGQQNVYDGGIAWNTKVMQGGVQNVAKKSQSAKNGGFAFNTEVFGGGKQR
VLAGGKAIGVTLNETAVQEIYAGGFVKNLTINDEAKSWVYAGATLEGKTLVNHSGQLYLYAGDDKHHTTV
EDIILNGRDTKLYSIVDEFDGKSSLIQKLSGEGSVIFASTGSDPYYSQLHVNNLSGSLHFKFNTSIAGNR
GDYLFIENGKGNHTISVADSGVEITDPFSNKRDLITDQSGGANFTLTNLSGEKINAVDGGTYMYGLKQRK
DENGKIWYLSADRISGQESSSPDPSEPLSVSDFLTTPSTDAVLSMAVAPGLIFNNELQTVRTGRGILDRN
KKNTALWTYAIKSKERIATGHTHFKLEQTGIVLGADGLSELTHGDLYIGGFGSYDQARIAHARGGVSDIN
TYSIGAYATYFDHRGWYLDGILKYNYYQNNLKAVSTNGLAIQGDYNQWAIGTSFEAGYRFETAQNTWMQP
YGQLTWLQVEGKKIKLSNGMTGDISPSTSLRSEVGLSAGHEFIVGAETSLTAYITAAWLRENIDNNHTTI
NKQHKFITDLSGNAGKLGIGLNSFVSDKLTLYAEAHYLKGHKIKQSLQGILGLRYSF
>gnl|CDD|468509 NF040483, serum_opaci_fac, serum opacification domain. Serum opacity factors are virulence proteins from Streptococcus pyogenes and related bacterial pathogens. The opacification domain binds to apoA-I and apoA-II of HDL, and apparently in non-enzymatic fashion causes HDL to release the lipid it was carrying. That lipid then coalesces in serum, forming droplets that opacify mammalian serum. This HMM represents a region within the described opacification domain from which poorly conserved regions and sequences recognized as von Willebrand factor type A domain have been removed
KTIIEEKVTHTNPLLPWPFYFDHTNRKANMIKDAKSLIKLLEKLGISRFDALKSVLSLAGTGSGLGGSLI
GIKSPLDYITLKELDSDNLEESNFDYSKKVGEGYHYHSFSERELDELPFKDIIIAALKSNLKKELDKENW
FGKILDKFGLGNTTQKAAKLVINKALDYIFYKREYIFYNHNLSAQAEAKMAQEEGITFYSVDVTDPNKAN
KRVRRQSAVPKGEEERNNKFDKYLKKMSEGKKFLKTDVDDADKFKDTLTELTIKDEFEDKVTVEKNWKKS
LDKTDLKSSKGKVKHTSSSSGWSFSSTKESLTWTISKEQLKKAFETGKPLTLTYKLKVKKDK
>gnl|CDD|468510 NF040485, ZirU_fam, ZirU family protein. ZirU, as found in Salmonella, shares with ZirS the property of requiring ZirT for its type Vb-like secretion. This HMM describes a broader family of ZirU homologs. The N-terminal half of this HMM shows detectable homology (although scoring below the cutoffs set for the model) to ZirT (zinc regulated transporter), but no similarity to ZirS (zinc regulated secreted protein)
VVTSPPTATVKGRAPVVADSTIEVTDTNVNGVLTAGDTLSISDFAFTDSDGDPIDASTYQWYVDGADIPG
ATGDTYTITADDLGKVITVLVTPHTDPGTTDPADGAASGVGGGTDADGSGNGIFVANGPVVLSVAVNGTV
LTGNPVVGTTLTAVVTCAGTLCDGVLNYQWQIETAVGSGVYTDIPGATSSTYTPTGTDQKRKIRVVVT
>gnl|CDD|468511 NF040486, SrfA_fam, SrfA family protein. The virulence factor SrfA (SsrAB regulated factor A) from Salmonella enterica is a secreted effector. The mechanism of secretion is not known. SrfA belongs to a set of three SsrAB regulated factors, along with SrfB and SrfC. Operons related to srfABC are widely distributed in proteobacteria, suggesting coordinated action, and the three proteins appear able to form a complex
KTFLRSGNLDDFLALGENGQPVYDSALQLRETLRLRKQQAIADCLAIPQHNEEGDRIDWYAPFEGKVTSW
SAASEEERAAARRQLEACQASVAALSERALQSEKPAQQLFGALLEKALQFPDENHVYLVDGKPVITFWGF
VNLNEGARDDPLDCLRAVEPPPPPPAPTPPPPPPAAPPVPVLLPLPDAPLPEPPPPPPELPVPVAEPEPP
PAPVAAARRERRRLLWLLPVAALLAAAVAALLGWKPVSAAPAAPAAPAPVPAPAPPAVTPAPVLPALPPA
LPLAPATVVPPAKPKPKPAPAPAAAPPIAPAPKDALVMPADAVKIGSTRFLNGNWRVGVGIKDPPTGKPP
SLRYQFKNGKGTVRVRQGDGVVCRADVFAGLHQSGNLVINSRGQARCSDGSRYPMPEIVCKQGATGAADC
TGRYDADTVFPMTMKRE
>gnl|CDD|468512 NF040487, T3SS_CigR_fam, anti-virulence regulator CigR family protein. Members of this family are full-length homologs of CigR, an inner membrane protein that appears to act as an anti-virulence factor. It was previously thought to be exported as a type III secretion system (T3SS) effector. A low-complexity, variable length repetitive region, rich in Gly, Pro, His, Lys, and Asn, separates a short, hydrophobic N-terminal domain from a longer, well-conserved C-terminal domain. A short stretch of that C-terminal domain, about 25 amino acids long, shows similarity to the C-terminal half of the domain described by Pfam model PF11776.10 (RcnB), but similarity between CigR and RcnB is not extensive
LAALAAVLSLALGSAPALADPGNGKGNGNGNGGHGNHGNKGNGGNGGKKKNGGDPDLVGPSISYGRARGL
AVNYGLTGYSSLPPGIAKNLARGKPLPPGIAKKAVPGRMLGQLPHYPGYEWRQAGTDLVLVALATGIVYE
VLNGVFD
>gnl|CDD|439713 NF040488, SCO5389_fam, SCO5389 family protein. The function of this protein is unknown. A member of this family was shown to have two-fold increased protein expression in a strain of Streptomyces tsukubaensis under redox stress from knockout of the hydrogen peroxide-scavenging enzyme AhpC. A one-time classification of this protein family as a recurring spurious translation of shadow ORFs overlapping a different and real gene family appears to have been in error
MSLTVSPELLEQAERGEVDDAAFVACVRDSLPYAWELVERLAAELEASGADFADNQVPPPSEQARGQLLR
ALASDAIRGALERHFGVKLAFQNCHRVAAFRPDAVGSEAYREFVSPRAQILNQSPELRDC
>gnl|CDD|439714 NF040489, variant_MftA, variant-type mycofactocin precursor. Mycofactocin is a enzyme cofactor derived from the C-terminal amino acid pair, usually Val-Tyr, of the RiPP precursor peptide MftA. A rare variant form of MftA, with differences from the consensus for several key amino acids in the last ten, occurs in Deltaproteobacteria. The most notable amino acid replacement, true for all members of the seed alignment, although not necessarily for all members of this branch of the MftA family, is Ile replacing Val in the terminal dipeptide destined to become part of the mature cofactor. The variant form tends to co-occur with a variant, somewhat shorter form of the radical SAM maturase enzyme MftC
EQPCILEEIVIEELAVDGICGIY
>gnl|CDD|439715 NF040490, SDR_subfam_3, mycofactocin-coupled SDR family oxidoreductase
KLEGKVAIVTGGARGNGLAAAKCLAEEGADIAIADICADMETIPYPMSTPETMAEAVEEIEALGRKALGI
KCDVRKAADVEAMVEQVLETFGKIDILVNNAGNSSMVAIAEMDEETWDEVLDTHLKGTFLCCRYVLPHMI
AQHSGKVVSISSVGGQRGFGMGGHYCAAKHGIIGLNKSLAMEVADHNINVNVVCPGTVWTDMMQGIAAYF
GMEGDEAKEQFFAGHLIKDPEVTPEDIGRAVLWLVTEDSRCITGNMITVDAGWTAQAP
>gnl|CDD|468513 NF040491, SDR_subfam_4, mycofactocin-coupled SDR family oxidoreductase. Members of this family are uncharacterized SDR family oxidoreductase regularly found encoded next to genes for mycofactocin biosynthesis proteins, and never found in genomes lacking mycofactocin. Members of this family are likely to represent a family of proteins that share a specific function
RVALVTGAARGIGAATVRRLAARGYAVVAVDACAGDPAPYPLGTEADLDALVASSPGRVETVVADVRDRA
ALAAAVALALDRWGRLDAAVAAAAVIAGGRPLWETPPEELDALWDVDVRGVWNLAAAAVPALLAGPDPRG
CRFVAVASAAGHRGLFHLAAYCAAKHAVVGLVRGLAADLAGTGVTACAVSPGSTDTPMLAATAALYGLDD
VTELAAHQLVRRLLDPDEVAAVVAFACSPGGAAVNGSVVHADGGFG
>gnl|CDD|439717 NF040492, not_ScfB, ScfB-related radical SAM/SPASM orphan maturase. Members of this rare protein family are SPASM domain-containing radical SAM enzymes that closely resembly ScfB, the thioether bridge-forming peptide modification enzyme of the SCIFF (Six Cysteines in Forty-Five residues) RiPP precursor. However, they form their own, distinctive clade within is ScfB-like family, are noticeably different toward the N-terminus, and are found in genomic contexts in which no ScfA-like encoded protein can be found. The protein is designated an orphan maturase because no substrate has been identified
MTLIHKFKQGDEYFILDVNTGAIHVVDKIVYDILDEDKLESKNNIINKFKEKYDEKIINECYDEIEELIK
EEQLYSEDQYEEIAKKSEEDRDYIKAVCLNIAHDCNLRCKYCFADEGEYDGQKKLMSFEVAKKAIDFVIK
NSGPRKNIEIDLFGGEPLLNMGVVKEIIKYARSNEKQYNKNIRFTMTTNATLLTPEIMDYLEKNMGNIVL
SIDGRKEVQDSVRVKIDGSGSYDDILPKIKEMVKRREKSKQYYVRGTFTRENLDFSKDIMHLINEGFKEI
SIEPVVLPDGNPLSIREEDLDTIFEEYDKLYEEMLKRKIEADDFIFYHFNIDIQGGPCVYKRISGCGAGF
EYVAITPDGDIYPCHQFVGNEDFKMGNIYDGIKNKKISKKFRKAHIYNKPKCRECWARFYCSGGCQANNY
NFNGDTKIPYEIGCKMQKKRIECAIALKAY
>gnl|CDD|439718 NF040493, TA_anti_VapB, type II toxin-antitoxin system VapB family antitoxin. The term VapB has been used for the antitoxin component of various type II toxin-antitoxin systems called VapBC but showing little or no sequence identity. The family described here includes member proteins such as STM3034 from Salmonella enterica LT2 and VapB2 from Haemophilus influenzae, and is seeming unrelated to proteins called VapB in Mycobacterium tuberculosis
AKVFKNNRSQAVRLPKEVRFPGDVKEVEIRRVGDERILRPVRPSWDSFFDGPSVSDDFMAEREQPEQQER
EAL
>gnl|CDD|468514 NF040494, nitrored_ArsF, nitrophenyl compound nitroreductase subunit ArsF family protein. The founding member of this family, ArsF, acts together with ArsE as a nitroreductase for trivalent forms (having As(III) instead of As(V)) of two synthetic aromatic organoarsenical biocides, nitarsone and roxarsone, reducing the nitro group to an amine, after which efflux confers resistance to the arsenical. Because the nitro group is rather far from the As(III) moiety of the known substrates, it is likely that conversed properties of members of this family include nitroreductase activity but not arsenical resistance activity
VEVYYFHGTQRCPTCKAIEAYTKEALEEYFADELKSGKVVFRSINLDDPENAALAEKYEVTGSSLVIVVV
KGKKEDWKNLTEFAFWYAVNNPEKFKAYLKEEIDKL
>gnl|CDD|439720 NF040495, tranport_ArsG, aromatic aminobenezylarsenical efflux permease ArsG family transporter. ArsG belongs to a broadly conserved ArsEFG cassette that was found in Shewanella putrefaciens as part of an organoarsenical resistance locus. ArsG performs efflux after the nitroreductase pair, ArsEF, converts a nitro group into an amine on the aromatic ring that elsewhere carries the arsenical group. TCDB names the system the Aminobenzyl Carbon-arsenic Defining Exporter (ABCDE) Family, 2.A.131
DNSSIPLLSAFWLGLLTAISPCPLATNIAAIGYISKDIESKRRVLLNGLLYTLGRALSYTLLGLLLVFGG
ASVFGVSKFLQKYGEKLLGPLLILIGLFMLGLIKLNFPGGGGLSEKLSEKLSKKGLWGAFLLGVLFALAF
CPYSAALFFGMLIPLALSSASGLLLPAVFAIGTGLPVIIFAWLLAFSVSKVGKFYNRVQKFEKWARRIVG
VVFILVGLYYIVIYL
>gnl|CDD|439721 NF040499, Bdr_N_group1, Bdr protein N-terminal domain. Bdr (Borrelia direct repeat) proteins have an N-terminal domain, a variable length region of repeats, typically 11 amino acids long with a KID repeat, and a non-repetitive C-terminal domain. This HMM describes the conserved N-terminal domain of families designated BdrA, BdrB, and BdrC. A related but non-overlapping model, NF040500, describes the N-terminal domain of additional Bdr families
ITEQMVYNELVKAGMNKDIADDLSYRYYHNELTYKDLEYLEMNFNLKLEDLE
>gnl|CDD|439722 NF040500, Bdr_N_group2, Bdr protein N-terminal domain. Bdr (Borrelia direct repeat) proteins have an N-terminal domain, a variable length region of repeats, typically 11 amino acids long with a KID repeat, and a non-repetitive C-terminal domain. This HMM describes the conserved N-terminal domain of families other than BdrA, BdrB, and BdrC, which are described by sister model NF040499
MNNLAYRTYKYEYVKQEFLEKGFSEEAIDFVLLHNDNYNYENLKEKM
>gnl|CDD|439723 NF040502, PPT_acetyltrans, phosphinothricin N-acetyltransferase. Phosphinothricin N-acetyltransferase (PAT) provides resistance to producers of the natural product phosphinothricin, non-proteinogenic amino acid antibiotic
MSPERRPEGIRLATAADMPAVCEIVNHYIETSTVNFRTEPQLPQEWEDDLARLRERYPWLVAEVGGEVAG
IAYAGPWKARNAYDWTTESTVYVSDRHQRRGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRLHEAL
GYESRGRLRAAGHKHGGWHDVGFWQRDFVLPEPPRPVTPVTDI
>gnl|CDD|439724 NF040505, ArsO_flavin_mono, ArsO family NAD(P)H-dependent flavin-containing monooxygenase. All members of the seed alignment for this HMM, including founding member ArsO (ABB70173.1), are encoded in arsenic resistance islands. However, protein functions in this family maybe both variable and promiscuous. ArsO is related to the flavoprotein CzcO (see PMID:12100555), which was found to modestly enhance the activity of cation diffusion facilitator CzcD
VDVVVIGGGQAGLAAAYFLRRTGLSFVILDAQPAPGGAWQHGWDSLRLFSPAAWSSLPGWPMPAQPGEGY
PTRDHVVDYLTAYEQRYALPVQRPVRVDRVERDGGGLRVETDAGDWRARAVISATGTWSRPFIPAYPGRE
LFTGRQLHSAHYRSPEPFAGKRVLVVGGGNSGAQILAEVSKVAETTWVTLRPPRFLPDDVDGRVLFERAT
ARLKAQQEGRTDDGPVGGLGDIVMVPPVREARDRGVLHAVPPFTRLTATGVVWADGTEAAVDAVIWCTGF
RPALDHLRPLGLVGPDGRVAVEGTRAVKEPRLWLVGYGDWTGPASATLIGVGRTARAAVREIAAYL
>gnl|CDD|468515 NF040506, PG0870_Nterm, PG0870 family Cys-rich N-terminal domain. This protein N-terminal domain, about 60 amino acids long, has four nearly invariant Cys residues, two in the unusual motif VGRCxxxxxCGYH. The family is named for a member protein, PG0870
FHLEKYKGSSKHTCPSCGKKRCFVRYIDTEGGIYFPDYVGRCDHESSCGYHYTPKD
>gnl|CDD|439726 NF040507, LBP_cg2779_fam, LBP_cg2779 family protein
DELSELAEEIIDFQKKNHLTDNDLAFGSHLSVERIHAIKSMEGTPTDEEVRLIKDFMQ
>gnl|CDD|439727 NF040508, LVIS_2131_fam, LVIS_2131 family protein. This uncharacterized protein, found in members of the Lactobacillales, is named after LVIS_2131 from Levilactobacillus (Lactobacillus) brevis
SWNWLGILLWIILIAYLVFIIHNIRVRRLKMIVKTKKRFTWKNFLIDVVEVVVFLLALGGMSYLTFFRNV
DLTDKSRVTSSYKYEPLILQTGAGDSYYVTVNSGNGKHPVQSYTYWTNGSKYTVSSRYATVSDGKSPLNV
AASAYPWNKKKLKKEDQKYQHAYVATYTATYKNNWLNGLGLHAGRLADRYTLIRVPDSSFIK
>gnl|CDD|468516 NF040509, Lacto_palin_RPT, translation of Lactobacillus palindromic repeat. This model was built for AntiFam to prevent false prediction of DNA repeat translations as proteins related to WP_020751851.1
ITRSPAQKPACKDLGRNGQSPAITPKATYTPVSNRAGSRS
>gnl|CDD|468517 NF040510, avirulen_svx, Svx/AvrXca family virulence/avirulence protein. This family is named for Xanthomonas proteins such as AvrXca, called avirulence proteins, and the virulence factor Svx from Erwinia carotovora. Svx is described as secreted, regulated by a quorum-sensing system, and post-translationally modified. These proteins belong to the DUF6055 (PF19527) domain family
LVSCLLLLAGLAAANGAAAAAACIAGNWQADSGTTDMPAVQYETEHFAFRWKDGDVNQNDVVAAGKTLEL
IWDKYINQIKFPEPYCNTTVKYKANIHLDPSFGLSGGIAGSGSMGMWIGPASLKDNWGLAHELTHALQGQ
TGGFRDSNYVGWIWESHANWMTHQLDEFRHTSVHCSEMLVNYPHLYLGSTRDRYCNWQFMEYLKNRFGYA
AVNDLWAKAPKPGDAGQETADPFSVLRSNMGWSQSQLNDVFGDWALHNVNWDYTDPDGSDQGQVYRRTYG
SYGAFDPNQRNRDRLLRVTQLDPVDAQARRFAVPFEWAPQRWGYNIVRLIPDNGATTVTVKFRGIVQTAP
AVNRLPGLKNDPATLTAPDSDWRWGLVAIDADGKSRYSALQRGASATVSFAVKSGDKALYLVVMGTPSQM
QKIKWDQAYYSIYRYPWMVDLTNAWPEGSQPGAPTPTANGHRHPNGGGWVANGAQVASTAYVGPYARVLG
GKVLGNARIEDHATVLGGTVSGNAVVGGLTVVQGGVVVKDNAQVHTVFMGPGAFEPGIVVSGTAQLRGDV
EIRGASASQGVFYGFVDAAEVTSPQAGANLTDAVPEVTERP
>gnl|CDD|439729 NF040511, membrane_GPGG, GPGG-motif small membrane protein. Members of this family are small membrane proteins, nearly all between 47 and 49 residues in length and very well conserved
MATILWIIAVILVIAGIVALVRGQLLWGIVLIVVGLLVGPGGVSIFT
>gnl|CDD|468518 NF040512, histam_anti_2, histidine-histamine antiporter. Members of this histidine-histamine antiporter found in Firmicutes such as Lentilactobacillus parabuchneri and Clostridium thermobutyricum are more closely related to antiporters of different substrates than they are to TIGR04298 family histidine-histamine antiporters such as found in Haemophilus influenzae. Members of the seed alignment were selected with help from proximity to the hdcB gene
KAGKLGLVGLIALCVSAMVGSGVFDLPKNMSMVAGLTAQILAWITTGIGIWFIAEMFVILSDVKPDLTAG
LYKYAEVGFGPFTGFFTAWGYFVCECAANAAYAVLVMSTLNYFFPGTFTGGNNWPSVIGASIITWAITAL
VLRGVEVSSGVQKVATAIMLAVVVVFIVTVIVHFNWHTFTTNANATHSLPSVSDKPLGSVMHQVMNTMMV
TLWLFGGIEGAVVMSGKAKNVKQVRKATIIGFIICLVMYALVGMLSLGVYSYGQLANLTSPSTAYILTNL
WHNNLGRDIITVALLVAVFSSWISWIQMLAELPQHAAAEDGTFPRAFAKTSKRNVPVFSILIATVVIQII
ILIAHFDGSAYQMLLTIVGTMTVPPYLISAMYLIKISAKESNEFPGNTKHHRRAGLIIGILAFVYTLFMG
YSAGIKYTAISFIFYAIGIPLYIWARKQHGKKIFTKGELIFAIVIVLVAIYGIYVLI
>gnl|CDD|468519 NF040513, antiport_TyrP, tyrosine-tyramine antiporter
QSKKLSLFQLIGITMAFFGTVRSVPTLAATGWTQIFYMIGAVILFAIPIALISAELATGWPEEGGPQVWV
KEALGEKWGFVTAWLLWVQMFFGMVMVASTVGVLLGYVIGNPDLGQNNIFVFIVILISYWIITLLNLKFD
MVKVAGNIGAVIGVYIPFIALVVLGIAYAIKFGINPGGYLGTFTASKLLPNLHSLSTLSYFSGIIFIFAG
VEISSVHANNIDNPKKNYPIAVFFSLILLVVFNLLAGLTVANAVPAGKIQLSNITQPFVLYCNILGIPTI
FTNIISFMIAIGVLAQLSAWVLGPSKAMIKVAEEGNLPPFFQKRNKKGVPITFVLIQAIVISLVALLYVV
VPDVNSAFLMITITTTILYCIVYLLIAISAIVLRYKKPDVKRPFRLGGKGNGLMWFVAILALFGVILTII
VSLIPPSILPASEHTGYLIFQIIITIVMFVIPLIIFKFKKPEWKK
>gnl|CDD|439732 NF040514, CAL67264_fam, CAL67264 family membrane protein. Members of this family are small, well-conserved, hydrophobic, lineage-restricted bacterial proteins, about 60 amino acids in length, with an essentially invariant C-terminal motif LKGRV
NKNTVLGWATLIMILMGLVLIALGAFRYDDVAGWGFAAVGIGFFAIAWVFNALKGRV
>gnl|CDD|439733 NF040516, CapE_47_fam, CapE family protein. Known members of this family are full-length homologs of CapE, a 47-amino acid linked to polyglutamate synthesis in Bacillus, or longer proteins sharing N-terminal homology with CapE
AKRTFGWVVPILIVAGLLITLGSFKRSETLTTDEQEKID
>gnl|CDD|468520 NF040517, Lacto_Palin_RP2, translation of Lactobacillus palindromic repeat. This model was built for AntiFam to prevent false prediction of DNA repeat translations as proteins related to WP_015765070.1. Additional models represent translations from other reading frames from the same class of repeat
MAKARPSRPRPLTLRFLTGPAHAH
>gnl|CDD|468521 NF040518, Lacto_Palin_RP3, translation of Lactobacillus palindromic repeat. This model was built for AntiFam to prevent false prediction of DNA repeat translations as proteins related to XXXX. Additional models represent translations from other reading frames from the same class of repeat
MAGLWPLRLRSLHAGFWAGERVM
>gnl|CDD|439734 NF040519, Sbal_3080_fam, Sbal_3080 family lipoprotein
LALLLVLLLSGCSIPQYVQPVILPANQSKEIVCIEDNPTRVGFLDSMENWLRRHGIKTKVYPDGSSPSSC
EYTLTYTARWSWDMATYLSYADIKLYQNGQRVGEAEYDAPRNGGGLLDKFGSAEEKINELVDQLFG
>gnl|CDD|468522 NF040520, Ig_like_BLP2, Ig-like repeat protein Blp2. Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats
MTRIVVASKKNLDVLQDGQLKKVVLNQPSIIQIGVNQKDIKSIEKQGNDLVITLKNGEKIVLENFFNEAN
TTEHSLAFPTEDGKFVEAQFDDSGKFIRYTGLTHLTQLAYTETPTQAATMAAVDDDPGISKSQLLKAGLA
ALAAEGLYLWAVKDDDKDDSNGPVDITPPATPTATLADDTQTITGKAEANAKIYIKDATGKVIATGQADA
SGNYTIKLDQPLVNGNKVNVTAIDAAGNASKATVVTGTKDTIAPDAPQAQLNADGTIVTGKTEANAKVSV
YDADGKLLGTVTANKEGLYSIKVSPPLTSDKGGTVIAEDAAGNKSEPSKIIAGKDTIAPDQPLVEVNKEG
TSIEGRAEANAKVQIKDADGKVIGTGTADAQGKFQITLSPALKTSQKGTIIVEDAAGNQSKPLEITAGKD
TIAPDKPTAQINAAGTSVTGTAEANAKIEIKDSAGKVIGTGTADADGKFTITISPALTDKNIGKVYAIDA
AGNRSDATDVTGTKDTIAPNKPVLQKVTDDVGAVKGAIAAGGETDDAKPKLSGSGEAKATLTIYDNGQAI
GTVTVGDNGKWSFTLDKDLALGKHKITLTQTDAAGNTSEVSDPFTFTVVAPKTASASEQSEVDTSNTETA
SLADSVGLNTLKLAQETTNETNSQQQESVSLDDLLKSSSSSESNQIDDVLSSQLKPTQTNEQSDVNNSSS
DVTTNLEDLLPDTKSDPLDQLLDQQHPIV
>gnl|CDD|468523 NF040521, C45_proenzyme, C45 family autoproteolytic acyltransferase/hydolase. Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis
SGSPYEIGRQLGELLKELIRDLYLALLRAWGLVSWRELRDFAKEFLAALEAFAPELWEELEGIADGLGLP
FEDVLALNARTEILAAPDGCSTFAVLGEDGEPILARNYDWHPELYDGCLLLTIRPDGGPRYASIGYAGLL
PGRTDGMNEAGLAVTLNFLDGRKLPGVGVPVHLLARAILENCKTVDEAIALLKEIPRASSFNLTLADASG
RAASVEASPDRVVVVRPEDGLLVHTNHFLSPELEEENRIATPSSRERYERLEELLKGKLDAEDAKALLSD
GYPLPICRHPYPDGDRFGTLATVVFDPAAGTL
>gnl|CDD|439737 NF040522, VC1465_fam, VC1465 family Xer recombination activation factor
IKETREKAGLTRQQAAEMLRVSLRTVQNWETGKVPMPYCAFKLERRLIPGSGLHGKEWDGWMFRGGKLIT
PEGHTFTPADIEWLNLQVDQARAVDKERRRVRGAARAGLAP
>gnl|CDD|468524 NF040523, adhesin_AbpA, amylase-binding adhesin AbpA. AbpA, an adhesin of oral streptococci, binds the host salivary protein alpha-amylase, contributing to colonization. Its C-terminal motif for cell wall attachment, LPKTxAVK-COOH, is recognized and processed by a dedicated B-type sortase
KKVLLSSVAALAVFAAAAPVFAQGENPGASNQLIQKAYVSQTDFADEANEYVAAHEAEIAAEAAQDPAVV
AAKAALDAVEGGSHLYGEKKAAYEAALNDARNAVRNKYIQKLQQTYNTAAKAEGNYYNDIGVETNEQKNA
RYEEDHGAQTGADQAAKDQAATKPEGGKPVVVDEAKKVEKAAKKAGAGAKAGQKALPKTSAVK
>gnl|CDD|439739 NF040524, LPKTxAVK, LPKTxAVK class sortase B sorting signal
AKAGAKALPKTSAVK
>gnl|CDD|439740 NF040525, SrtB_LPKTxSAVK, class B sortase, LPKTxAVK-specific. This branch of the class B sortase family is found in multiple species of Streptococcus and Gemella. It processes target proteins that end with the motif LPKTxAVK-COOH, which differ from most sortase recognition sites in lacking an additional C-terminal transmembrane helix. Substrates of this sortase include the amylase-binding adhesin AbpA, as well of other proteins with similar N-terminal and C-terminal domains but unrelated central regions
LLLLVFLVLAAGFFFLKGCSKKSSTTTSTSSTTSSSPESTYTVSQEEKAYLKNRFAPLKAVNPETIAYVY
APGTKLDEPVVQTTDNATYLDKTFEGGYEPYMGTVFMDTDNKKDFSDRLTWLFGHARGSKVPDHRMFNDV
NFYDDQDYFDQHPYVVIETPERKYYYEAAFLIIVPETTAFYRTSFDSDEDFEEQLTEVYEEAHTKNPNIK
INASDKYLVLSTCREEDETIRSNLYLRQIPDSELPDFLAKHGDKLAYVPTR
>gnl|CDD|468525 NF040526, SCO0930_lipo, SCO0930 family lipoprotein. Members of this family are full-length homologs to the lipoprotein SCO0930, Streptomyces coelicolor A3(2). SCO0930 contains four copies of the repeat described by Pfam model PF03640. By comparison, PA5359 from Pseudomonas aeruginosa PAO1 has only two copies of the repeat, differs substantially in several regions, and is excluded from this family
WRSASLAASAAAVLALTTACGQETSPPAASQNVGAAAAAAGQGGAGAGGGSTGGGGGAQPAAGSKPAGQL
AVSTVAKLGKVLTDSAGLTLYRFDKDTAEPPKSNCDGDCATTWPPVPADDAVAAAGVDKALLGEVTRADG
TKQLTVGGWPAYRYAKDTKAGDAKGQGVGGTWYALAPDGKKAGAAEAAAADDLPGLSTRKDPKLGEIVVD
KNGMTVYRFTKDSAWPMKTACTGACLEKWPPVAPVDKNDTKGIDKKGLMTFTRPDGTKQQTVDCWPVYTF
AGDKKPGDTNGQGVGGTWYAVEPDGKKVGA
>gnl|CDD|468526 NF040528, SP_0198_lipo, SP_0198 family lipoprotein. Members of this family, found only in Streptococcus, are lipoproteins with a lipoprotein signal peptide, a Ser-rich low-complexity region, and a C-terminal DUF3642 (PF12182) domain
KKFTLSLASLASLSLLVACSQQTQQSAQSQSQSSSSSTSSSSSSESSSTSSSNATVAQTTNLDGTYKGQD
EGDQITLVITGNTGTWTEVEADGEQEIKQVTIDPANQRMIIGDDVKRYRINGNQLTIEDLDQEPDDDDTI
VLTK
>gnl|CDD|439743 NF040533, endo_SpGH101, SpGH101 family endo-alpha-N-acetylgalactosaminidase. Members of this family are streptococcal surface proteins with a complex (and somewhat variable) architecture that includes a crosswall-targeting N-terminal YSIRK domain, a C-terminal cell wall-anchoring LPXTG domain, and a central endo-alpha-N-acetylgalactosaminidase that removes an O-linked disaccharide from host glycoproteins
MDKGLFEKRCKYSIRKFSLGVASVMIGASFFGTSPVLADTAQVGSTANLPADLADALAKAKDDNGRDFEA
PKAGENQGSPEVTDGPKTEEELLALEKEKSATEKPKENKPAEAKPETAKTVTPEWQTVARKEQQGTVEIR
EENGVRYNQLSSTAQNDNGAKPALFEKKGLTVDANGNATVDLTFKEESETGKSRFGVFLKFKDTDNNVFV
GYDKGGWFWEYKSPGVSTWYQGGRVAAPVNGSTNHLSISLKSDGQLNATNNDVKLFDTVTLPAAVNDALK
NEKKILLKAGTYGTERTVVSVKTDNQEGVKTEEETAEKETGPVVDDSKVTYDTIQSKVLKAVIDQAFPRV
KEYSLNGHTLPGQVQQLNKVFINKHEVTPEVTYKKINDTTAEYLMKLRDDANLINAEMTVRLQVVDNQLH
FDVTKIVNHNQVTPGQKIDDERKLLSSISFLGNALVSVSSDQAGAKFDGATMSNNTHVSGDDHIDVTNPM
KDLAKGYMYGFVSTDKLAAGVWSNSQNSYGGGSNDWTRLTAYKETVGNANYVGIHSSEWQWEKAYKGIVF
PEYTKELPSAKVVITEDANADKKVDWQDGAIAYRSIMNNPQGWEKVKDITAYRIAMNFGSQAQNPFLMTL
DGIKKINLHTDGLGQGVLLKGYGSEGHDSGHLNYADIGKRIGGVEDFKTLIAKAKKYGAHLGIHVNASET
YPESKYFNEKILRKNPDGSYSYGWNWLDQGINIDAAYDLAHGRLARWEELKKKLGEGLDFIYVDVWGNGQ
SGDNGAWATHVLAKEINKQGWRFAIEWGHGGEYDSTFQHWAADLTYGGYTNKGINSAITRFIRNHQKDSW
VGDYRSYGGAANYPLLGGYSMKDFEGWQGRSDYNGYVTNLFAHDVMTKYFQHFTVSKWENGTPVTMSDNG
STYKWTPEMKVELVDADNNKVVVTRKSNDVNSPQYRERTVTLNGRVIQDGSAYLTPWNWDANGKKLPTDK
EKMYYFNTQAGATTWTLPSDWANSKVYLYKLTDQGKTEEQELTVKDGKITLDLLANQPYVLYRSKQTNPE
MSWSEGMHIYDQGFNSGTLKHWTISGDASKAEIVKSQGANEMLRIQGNKEKVSLTQKLTGLKPNTKYAVY
VGVDNRSNAKASITVNTGEKEVTNYTNKSLALNYVKAYAHNTRRDNATVDDTSYFQNMYAFFTTGSDVSN
VTLTLSREAGDEATYFDEIRTFENNSSMYGDKHDTGKGTFKQDFENVAQGIFPFVVGGVEGVEDNRTHLS
EKHDPYTQRGWNGKKVDDVIEGNWSLKTNGLVSRRNLVYQTIPQNFRFEAGKTYRVTFEYEAGSDNTYAF
VVGKGEFQSGRRGTQASNLEMHELPNTWTDSKKAKKVTFLVTGAETGDTWVGIYSTGNASNTRGDSGGNA
NFRGYNDFMMDNLQIEEITLTGKMLTENALKNYLPTVAMTNYTKESMDALKEAVFNLSQADDDISVEEAR
AEIAKIEALKNALVQKKTALVADDFESLDAPAQAGEGLANAFDGNLSSLWHTSWNGGDVGKPATMVLKEP
TEITGFRYVPRGSGSNGNLRDVKLVVTDESGKEHTFTATDWPDNNKPKDINFGKTIKAKKIVLTGTKTYG
DGGDKYQSAAELIFVRPQVAETPLDLSAYEAALAKAQKLTDKDNQEEVASVQASMKYATDNHLLTERMVA
YFADYLNQLKDQAE
>gnl|CDD|439744 NF040534, resp_reg_YycF, response regulator YycF
KKILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKKY
DMPIIMLTAKDSEIDKVLGLELGADDYVTKPFSTRELIARVKANLRRHQQQNTEEEEEENNEIVIGSLTI
HPDAYTVKKRGETIELTHREFELLHYLAKHIGQVMTREHLLQTVWGYDYFGDVRTVDVTVRRLREKIEDN
PSHPEWIVTRRGVGYYLRNPE
>gnl|CDD|468527 NF040535, LiaF_C_term, cell wall-active antibiotics response protein LiaF, C-terminal domain. This HMM represents the conserved C-terminal domain of LiaF (called VraT in Staphylococcus), an additional key component of the histidine kinase LiaS and response regulator LiaR system. The system responds to cell envelop stress in the Firmicutes, and plays a role in resistance to cell wall-targeting antibiotics
WDDINIQHVIGDTTIDLSKAILPKGENVIVIRGLIGDVKILVPYDVGVSLEASVLYGEVTFFGEEEYDLR
NESLKYESPNYEEAERKVKIVVSLIVGDVEVKRV
>gnl|CDD|439746 NF040536, export_ArsQ, arsinothricin export permease ArsQ
MLTQVLRIKTRPWLRRLWKSASWPFPVAMILITLLIGLLGGFGSSEIISTLNKGFGYNLGYFALILLSSF
FIAAAISRGKIEIHGKIGVGLSPLVGAGMVCPDTAYAALSPIAGRHKKSIAVGSYAGFKLLIPAGPLIIG
TGLGANVADPRLLALGLLLMIPVWVAGLVWLWVITHEGALTANPAEAKLQPAPSSLKMLFPLALLATLLI
LGYAFDLRFNPWIDFFTNPAGALLITAALAYLLVKPRDRKDCLDSAVRRTASLLFIIGCASALGAMLATV
LPVNLLEETFAPQDSGAIALIGLFSMTALFKLLNGSSLATFAAAPPVLAPVVAASGVDPMAAVYAICLGS
FVAILPNDSFYWLVRKDAFANGTTFNYITTITGGSIIQAFVGLAILLGIY
>gnl|CDD|439747 NF040537, radical_ArsL, arsinothricin biosynthesis radical SAM protein ArsL
AKYIVASTFEGGYQPLNALSAATALRNAGFDTQLLDAYVEGLDIEKFSDADTIIISVPLFDSLQAGIQLA
KQLDEANPTAIKVFFGQYATINAERLSGRYGDYAVVGEWEVPLVSLAKRLSGGQEDPLAGVVDHGATTSE
KIVVPLLLRNTFRLPLRDIAPPLSKYPQPQLEKLLGEKKIVGGVEGTRGCHHKCTYCSVYAAYDGKVLLV
SDDLVEEDTDALVGQGMQHLTFTDAEFFNAKRHGLDIMRRLHERHPDLTYDFTTRVDHILENKDAIKEMR
DLGLRFITSALEFPKQEVLDQVRKEMDVDDIEESIRFLKGSGIKLNPTFIMFNPWVSLEDIARFHDFIER
NNLENIVDPIQFETRLHLYKGSPLLQNDTVKSLRLEEHEFHFDWFHSDSRVDELFRASVTPPEEGVFKRC
CLKC
>gnl|CDD|439748 NF040538, methyl_ArsM, arsinothricin biosynthesis methyltransferase ArsM. The ArsM found in the arsinothricin (AST) biosynthesis can act as a typical arsenite methyltransferase, acting on inorganic arsenite, methylarsenicals, and aromatic arsenicals. In arsinothricin biosynthesis, the radical SAM enzyme ArsL acts first, synthesizing hydroxyarsinothricin (AST-OH) by adding 3-amino-3-carboxypropyl derived from S-adenosylmethionine (SAM) to As(III). This ArsM then methylates AST-OH, producing the naturally occurring arsenical antibiotic arsinothricin. Other forms of ArsM would not be expected to have this specific activity
IENIIIADYTEALRSGNVVLESELAESCCSDAYDAQLLKNIPKRIIDADFGCGNPTKYVREGDVVLDLGS
GSGKICYILAQIVGPQGAVIGVDINPSMLQLARSEQKAFQEATGSANLRFFRASISDLKTDLELAEERLS
GESCENLASWKNFEQFLSDSRQSNPLIADNSIDLVVSNCVINLVGTTEKQNVFAEIFRVLRPGGRIAISD
NVSNIAVPEELKNDTELWSACYSGVLQEQEFYRQLQDVGFTGLTIEARNDAPTKRIGSVEFYSVTVTATK
PLEAVVGSGDMTTVIYRGPWTEVTDDSGNQYKRGKITLVPTELAAQDRYLSFQEHLFVLDGQPGSNGKSC
CG
>gnl|CDD|439749 NF040539, AST_met_ArsM_2, putative arsinothricin biosynthesis methyltransferase ArsM. Galvan, et al. (PMID:34378964) identified a 3-gene cluster for biosynthesis and export of arsinothricin, an arsenic-containing antibiotic., with key enzyme ArsL, a radical SAM enzyme, catalyzing the first step. The cassette contains a methyltransferase, designated ArsM, capable both of completing arsinothricin biosynthesis and of methylating inorganic arsenite (see NF040538). Examination of additional genomic neighborhoods of ArsL showed that in species such as Paenibacillus sambharensis and Vogesella fluminis, this arsenite methyltransferase appears to replace NF040538
ANCCSPEPEELEPAFQAIKDFYDSVAEGDGPYNAGTDKFSPSGPTERIKEYVLASDKQRILDIGCGMGTT
LLSLVKEHTSGQQFIGVDFSEKMIARARERSKSLDDKLRKKIGFFVADAQSLPYMDGQFDFVYSECVLNL
VPDREKAISEVYRVLAPGGLFVYTDFVSYAPVPDSIKNDLSLVSGCRAGSIPLSENIAQLENAGFVDIEI
INFTEDKNKRYQELMEESEEYRKEYEKFRKEHPEAAAFLEEKVGYYLIKAKK
>gnl|CDD|439750 NF040542, rSAM_RCCLKC, RCCLKC-tail radical SAM protein. Members of this family radical SAM enzymes of unknown function with an intriguing, nearly invariant C-terminal motif RCCLKC-COOH
ILLVSTFEGGYQPITAATAATALRDAGVDEVTLLDTYVEGVDEDKFKDADLVAISVPLFDSLEPGIELAK
RVREANPTAHITFFGQYATINAERLVGKYGDFCIVGEWELPLVSLADHLSGSKHLDLAGIVSAADATLGK
TPRPLISRKHFRVPDRSLLPPLSKYPQPQIEKLLGSEQVVGGTEATRGCHHKCTYCSVYAAYDGKVILVP
EDVVIEDVRNLVDQGMTHLTFIDADFFNAKRHGIKILRKLHEEFPFLTYDFTTRVDHILENEDTIPEMAE
LGVRFITSALEFPSQEVLDIVAKEITVDDIEEAIRFLRKSGIKLNPTFIMFNPWIDLEDLSTFHDFIERN
GLEDIIDPIQYETRLHLYKGSPLLNNPSIQALELEEHEFHYEWKHPDPRVDELYQASVTPAEEGVFKRCC
LKC
>gnl|CDD|468528 NF040546, rSAM_CUAEP, CUAEP/CCAEP-tail radical SAM protein. Members of this family are radical SAM enzymes with an N-terminal apparent B12-binding domain. Some members of the family have Cys-Cys motif about 10 amino acids before the C-terminus, but the majority of the family are selenoproteins with the second Cys replaced by selenocysteine, in a strongly conserved motif W[YF]C[CU]AEP. The proximity of the selenocysteine-encoding TGA codon to the C-terminus may have impeded recognition of this novel family of selenoproteins
ILLLSCYELGHQPFSLASPAAWLRRAGYAPRAVDTAVEPLPDAAVAAARFVAISVPMHTALRLGVPVARR
VRAANPAAHICFYGLYAPLNADYLLRTGADSVIGGEYEEPLLALVQALEAGEDGPVPGVSTREGPSGPAL
ARLDFPVPDRSSLPPLSRYARLQAGGRLRLAGYTEATRGCKHTCRHCPIVPVYRGRFFAVPVETVLADIR
QQVAAGARHITFGDPDFLNGPTHALRIVRALHAEFPDVTFDATIKVEHLLKHRDLLPELRALGCAFVVSA
VESLSDEVLARLDKGHTRADVREALALLREAGIALRPSLLPFTPWTTLEDYLDLLEFIEEHGLIEHVDPV
QLSIRLLIPPGSALLERPDVREWLGPLDAAAFTYRWRHPDPRMDELQERVAALVEQGERRGADPYETFAR
VKALAYAAAGRPFPPADARVAYGPRPAVPRLTESWFCUAEPTADQLAL
>gnl|CDD|468529 NF040549, Nt5e_LPXTG, cell surface ecto-5'-nucleotidase Nt5e. Members of this family, found in Streptococcus sanguinis and related species, are LPXTG-anchored cell surface proteins. By hydrolyzing pro-inflammatory extracellular ATP in the host, it may blunt immune responses and contribute to virulence. Nt5e has also been called adenosine synthase AdsA
KKKLLLPTLSTLLLSTAILANQVYADEAETTTSAEPSTVVATVSTTATTPTSAVQTSAAPAATTEPSPAS
EESQSTVASSEAPAETAAVPSTSQDEDEVTILHTNDVHGRIVEEKGVIGMAKLATVVEEERAKGTTLVLD
AGDAFQGLPISNSSKGEDMAKIMNAIGYDAMAVGNHEFDFGLDQAKKYKEILNFPLLSSNTYVNGARLFE
ASTIIDKDKTVVGDEFVVIGVTTPETATKTHPKNVQGVTFTDPISEVNKVIAEIEARARAEGKTYKNYII
LAHLGVDTTTPVEWRGSTLAEALSKNPLLKGKRVIVIDGHSHTVESATYGDNVTYNQTGSYLNNIGKITL
NSNQVLGNASLISAADAKNVTPNPKVAAMVDKIKAKYDAENAKVVIDNSPVELNGDRENVRVRETNLGNV
VADALYDYGQTGFSHKSNLAVTNGGGLRETIAKDKPITKGDIIAVLPFGNTISQIKVTGQQIKDMFAKSL
GSILQVDKDGKPVLDENGQPLLEPSGGFLQVSGAKVYYDTNLPAEKRILYIEILNPETGTYEPLDLTKTY
YLATNDFLAAGGDGYTMLGGAREEGPSMDVVFADYLAKADLTQYAVINPNSRTISISSTLDTDGDGFPDY
IELIAGTDPTDPKSYPGQAPNPQKSATPVETGQVPPKASKVTSKSPETIPVSYPKSVAVAKKATSSQATL
PNTGSQESIALLLLGLSLAGLGLYGLRRRK
>gnl|CDD|439753 NF040552, mini_lipo_xxCxC, CGxCxC motif mini-lipoprotein. Members of this family, found so far only in the genus Akkermansia, are apparent lipoproteins of very small size, typically 45 amino acids. The mature form of the predicted lipoprotein begins CGxCxC and is only 26 amino acids long
CGECACNSYNPDYLRDVPVSSSRSFE
>gnl|CDD|468530 NF040553, SGO_0316_fam, SGO_0316/SGO_0317 family LPXTG-anchored serine peptidase. Members of this family are cell wall-anchored streptococcal serine peptidases from MEROPS family S8, which contains subtilisin and its homologs. In several species, such as Streptococcus gordonii, two members of this family are encoded by a tandem gene pair
MENDRKQRFSFRKYAVGLVSVLVGCLFVGPMVLAQEVGGEEQVEPPAIVDTANEALAEEVTKLETPSLST
SLSDTTSQETQPSDKGNEPVKEEGENAPDKVADEKEAGSKASKESSKPEATPTKEKTLEKKKEEKNHKEV
ESAVINSLDEAARVEALVRLKEEKSGTPTSATDIARRIEENNPEKEAVLKELEEKGIQYKKLADFDLLFN
GFVLETTYKDAKKIRGLARVENVDITPLSTRVEEQQLPKKQPTLSPTKVSEENSLINLQPLWDKGIKGQG
RVVAVLDTGLDYAHNFFSLTDKSKAKYKNEAQMEAAKKKAGITYGKWYNDKVIYAYNYSDMNDEIKEDDP
RSHGTHVAGSAVGNATKPAPTGEILKGVAPEAQLIFMRVFSDKKGGTEQGFIVAKAVEDAVKLGADTINM
SFGGASGSIADTGPLTRQAFEFARKAGVTINAAAGNYATSGYWHAKPKADAPDYGTTDTPAVEPNVLAIG
AFNNSIKHETKISLEVPALKDKKEFQNGLIDLPVYRLIFPVEGPQSYVYVPKGGEENYRGASVNGKIVLV
ESGGDVSDEDKVNQLRQAGAKGVLVYQNKEQGDTPTKLDLGYWGSFFPVGVIGHSLGKELAAHAGEYQLT
IHQEVKKVPYSEANKMLYFSGWGLSAEGDLKPDVTLPGGMIYSSVNNGSYYMDRGTSMATPHAAGATALV
KQALEERFPHYSPEQLHTLLRQLVMSTAKPHVDEESNTYSSVRQQGAGLMDVTAAAFGDLYVTGKGAKSS
LTLGNVKDSFEFEVTVHNLSNQAKELTYHTVVNTDQVEDGRITLKMRQLLDQKGEKTITVPANGSVTIPV
SVDTSKYTSELSKQMKNGYFLEGFVFFKDAKTKKDLVSLPYIGFKGTYQDLPGIEKPIYEFTGSEKPFYY
YKDEKADTPEKDPGNHFTSLVSYVYENGESVQVVLGEDGDKYDGNQLYFSPNGDGSFDSVKLKAVVLRNV
DNIHLTVYKKDDTKREHPIFEKGNESQRKSDYGWRINNRSEELYASSWEGKDKDGQVVPDGEYQYVITYR
PSAPGAKPQELNFKVKIDNTAPQLETTSDLYDPKTRVFRPGKIIETGSGLAGTYLSYTKDGETVELTPNE
DGSYLIPEGVDLSTVRFSIWDKVYNTNTLDLEGKKIEASTTKENNKAEEPTSSETEKETATKGRLEVVFT
DESGEVISQYPEMMRYQVFDSQGNRVDKEFNTYYESSLPTLPFGTYTVKIVLQDQNYSWVSPTVKTVTLS
KEHPEGVVTFVYHYLDKNRLDVVFDKPLPEGTRVFAIDKTGEQRELEQTIYEPKTFEKILLNGDYRIHIE
LPEGYRAVENDFFYEVTNKINRYLTSFVKVNEDPSEDPTVTSNPIPNPSPSPNTPPQTPDPGTKSNNTNN
THPNKITKKADLRPMYVKPDEKKYKTALSTSEVSSKTSKVLPNTGQEGDTSTALSGFGVTLLGVALIVQK
KREG
>gnl|CDD|468531 NF040554, mini_HHHH, HHHH-motif protein. Proteins in this family are small in size, averaging just 46 amino acids in length, half of which belongs to an apparent signal peptide. The C-terminal region contains two invariant Cys residues, and between them, an HHHH motif, unusual in such a small protein. The function is unknown
MKTLLKSLTAAAVALAVLAPAIAEAHPHRVCHFDHHHHRVCHWVR
>gnl|CDD|468532 NF040555, Pro-rich_NTERM, AAA family ATPase Pro-rich N-terminal domain. This HMM describes an extremely rich N-terminal domain that is well-conserved for a family of AAA family ATPases seen in Streptomyces. The HMM was built to support correct structural annotation of this unusual, low-complexity domain
MQHAVGAPLPPPHQPGHGPAAGWSPAAHHPGPPHPQGPAPVPPPAPGFPAPPGPQPGWHPPAPQHAPAPP
APDTTGHVQLPPGGPVPMPSPPP
>gnl|CDD|468533 NF040556, CAS_Csx28, CRISPR-associated protein Csx28
ITELLKTLISLIAIIIAAYLTYRYAIKKLRKESIENIERAKYEAILKAHKSIYKLLRFTTDTENDDCILV
WEQPKGGGEKTYYFRQANIRKFIKELTEEIYNEGNGIFLSKEVISLIFEYRSIVYGLLLAEQNNPDETIR
IKNEELAKRMIEIHQSLSIQIRQDINLKQRDL
>gnl|CDD|468534 NF040557, CAS_Csx27, CRISPR-associated protein Csx27
MEKLSLYEFLSFVLPGVIFLVLFRWIFSFVHLSLPLFNPLGLSNSLLTLVYALFIGAVLHVLTFSLVKKY
KGYYRHVYKLYQKMKALHPYINDALPFLAEEYGANKKYLSEENFNNSEAQSNFFDYAYYYLEFNGKLAQA
KNFQSYYFFFRNSFTGLLFFLVILLIYLLLSYFMNVDCEDIREISFIFIPILIISGIFVFLAQWFRIKMV
EKMYWTYYASLIH
>gnl|CDD|439759 NF040558, CAS_Csx18, CRISPR-associated protein Csx18
YLSKRAALVRNIAVAIANGAITLIILLIAPLGLAAVIINTVLVTLATFIVGTVADRVVLWLQRS
>gnl|CDD|468535 NF040559, CAS_Csx20, CRISPR-associated protein Csx20
LFLLFSHTLTEEQIEEAKNSLGVEEIIYLPPELQNIWSNIPPDLESISEYLEPIKDWLKENAKKGDYVLI
QGDFGATYLLVNFAKKNGLIPVYATTKREAKEERLEDGKVKKTHIFKHVRFREY
>gnl|CDD|468536 NF040560, CAS_Csx15, CRISPR-associated protein Csx15
IILNFSHPLTPEQREQIEALTGQPIEEVITVPVQFDPDQPFAPQAQALLDRVGLTSEEWQTAPIVVNPPG
LAPLAAALLAELHGRMGYFPPVVRLRPVPGSVPPRFEVAEIINLQAVREAARERR
>gnl|CDD|468537 NF040561, PrimPol_Msp, CRISPR-associated primase-polymerase type A1
ALDNSQFEKALELFERAELWLSLEDEQLLRWAELAQEFGLYDQAKEVFEKIVEKEPDSKEALLALARLLE
ELGDLRAQQLAPANSVRRDQAAEIYEPLGAGAGIEKEEELLKEPFFTFRLREEDLSRFMELFSGREDCFA
RQWNDREEKQGYSPVRRPMTEEDVLEHLNGKRTYGIYLLRKDNRVRFAVLDIDIKKSLRARQLTPKNKQS
VRREAVYVALRIPELLKDEGLKCLVEFSGGKGYHFWFFFDEPVPAYKVREFLKTILNKIEPDLSCINLEV
FPKQDRLGGKGLGNLVKLPLGIHRLTGKRSLFVDENGEPVENQLEFLLKIRPNSKEAIEALFSGGESEEV
VVHPSLKAWKEQYPELAKLIEKCTVLKQIITKAQAGRYLSVREEKILLGTLGFLPRGKRLLHHLLKNLPN
YNPHRVDYQLSRVRGTPIGCKKIRRLLLSATLSLSCDCCFFKFGERYPHPLLHVPQWEEITLEQISVAEI
AEKVVNLQDEKDELETAIRNLERFL
>gnl|CDD|439763 NF040562, PrimPol_Db, CRISPR-associated primase-polymerase type B
LRFGTHITSAGDQLQDVSLAKLHQALTNPKPAVASLIRRLRAVRAMDPAQYRKLKTRLPYIVCAQFHPAV
RRKENFLYTEYFILDIDHLSEHGLSLPELRDQLVADERVELLFVSPSGDGLKVLFRLQEPCTDAGLFSAF
YKAFAREFAMRHGLTQVLDLKTSDVTRACFVSFDPKAYYNPEAEPVDMSDYLDEEPEVEPFATKAELAAK
EERKEKSSAEPATPGKDLDEEVLARIREKLNPKTRPPRRKKQYYVPEELEAIIAELKDFLEETGLQLLEV
IPISYGRKIRIRSGGKWAEINVFYGKRGFSVVKSPKTGTDPELADLLADVLKAFL
>gnl|CDD|468538 NF040563, guided_IscB, RNA-guided endonuclease IscB
VFVLDKNGKPLMPCHPAKARLLLKQGKAKVVRRYPFTIQLKYRVETGYTQQPLRLGIDPGSKTTGIALVT
ENNKVLFAAELEHRGDQIKKALTQRRAYRRSRRNRKTRYRKPRFLNRKRPEGWLAPSLQHRVDTTLTWVK
RLRKLLPITAISVELVKFDTQKLQNPEIISGVEYQQGELYGYEVREYLLERDGRTCQYCGAKDVPLEVHH
IVPRSKGGSDRVSNLILACEPCNQKKGNQPVEEFLKGPELLKRILKQAKAPLKDAAAVNATRWALFNRLK
ETGLPVETTSGGRTKYNRIRLGLPKTHWNDAAIVG
>gnl|CDD|439765 NF040564, SCO2523_fam, SCO2523 family variant P-loop protein. The family of proteins related to SCO2523 of Streptomyces coelicolor is limited to the Acintobacteria, and part of a conserved gene neighborhood encoding proteins SCO2521-SCO2524. The N-terminal half shows homology to P-loop-containing regions of multiple protein families, but the key motif differs substantially from the P-loop consensus, DKGGTGRS when GxxGxGK[ST] is typical
MLVFATSDKGGTGRSVTSANLAYRRALQGDDVCYLDFDFGSPTAGAIFEIGDAERGTRRGGLHSYLRGEV
GEPARIDVWSETDRPELRRRPPGSGRLVLLPGDEGGGEFAADEEMVRRCVELFLRLEEEFDLCLVDLSAG
RSYATDIVLAATATPQLRGVTARWLVFHRWTRQHIIAAAGLVYGERGILDTGAERGHDPEELRRRIRFVR
TAVPDPDSPELSGLRPAQAAWLRECDGELRRLAGRNRVGRTVLLGSVPLDPVLQWREQLITDEDVLARQI
ANAETVEAFDELAKRLTDDSAWEGL
>gnl|CDD|468539 NF040565, SCO2521_fam, SCO2521 family protein. The family of proteins related to SCO2521 of Streptomyces coelicolor is limited to the Acintobacteria, and part of a conserved gene neighborhood encoding proteins SCO2521-SCO2524
GEVRTGLLPNSTALDRSAARQLLALRPGERVRWSERPIAYAVSPDVLTGVDCRLPTASGARVRAVGTVAS
RAVLTGGRVLQGSAYARVVAAGARRRLPWSHYLARPGVVEVIGKLPAADLATGFLRGGPPADLLDLGAIA
ARLLDRLQRSPLLDRRAPLRARRTRLRWAAEPGDGEGPRGAFTLEDDTLRTVRLTVREAADLPAAVALCE
DLALHDWLLTTLLDLLDRDRLGAASSREVVDRLAPALDHLLHLWMPGARVPAALRPLWEELERRPGFTRQ
WQTLVQRVRDQLALATLAALR
>gnl|CDD|468540 NF040566, SCO2522_fam, SCO2522 family protein. The family of proteins related to SCO2522 of Streptomyces coelicolor is limited to the Acintobacteria, and part of a conserved gene neighborhood encoding proteins SCO2521-SCO2524
VFRETSAVPRVESVPLSHLSVELGHLYMEDFEAGPDDLRRHFRRIAPWVDAARAAAAAGRAGRRPRVSTC
FLIDDYFTRFSSPAEVVPRLLAAAAEAGLRIDYLARESGCARAGGVSLAELVEDRLVAEPPPGTNGSRPP
VSESGWLTNGQRSPGAQAMPAMGARAGWQPPRENAARRHSIFLDVELWSEEPGGRLWSCPFLAAVWQLLR
LGLLRHEGRPVVTPVPLDPADLPDRWDELPAVLRLNPRAAPFCAYRTLSVLDSRFLPVEHAVRTILGQVA
VDPEVLQQVARRAAGEGITLPDEVVDRLSYVFL
>gnl|CDD|468541 NF040567, SCO2524_fam, SCO2524 family protein. The family of proteins related to SCO2524 of Streptomyces coelicolor is limited to the Acintobacteria, and part of a conserved gene neighborhood encoding proteins SCO2521-SCO2524
MRIQPRQQLLEIWRAAARHSFQDGKWVWGGRGGSNSISDAEQLLCLLYPATEIPAFRLDQPDTTEDDVLR
ALRPLGDRLEIPRNLVEVLTEYLRRYTDPDGRPTFSGGTYFRPADPGAEVTPEQLQLDVVDSFSMSVTLC
LATLGFLKVFRQSVTRPELLREIRELEEAASARLTAAMVGLLRSFTVNVFDADSEQGRALLRTVNQSRLS
DRRVVDRLRRRLRPLRAGLRDLTIGSQVVDDLDNENLLFECGWSWGVVRDAPEVETPEPVGPQPPGVADD
APYLYFTVVALDGIQDLFSERTRVLGLLDEEQQRLAEALQLRWELTQQYWSTVARFGEGRWPLEDIPWRT
TDGEESDYFSLLVTSIVVHDLVRRRATDDDLTRVVAVLEELANRGRITRRPTADDPAVALHSPGVRLPLL
GSERLGPPLLQWVVTDFAALLLKRTIQLAGLSRNLRTRDRLLRLADQIWDHLWRRRIRDGEGAGLWDQPA
AVFPDLPAIRRDEPSWYYTERVVECLVAAANLYREPPLRSPELAELARELLSEAEHLFDKEQLEGSAEAG
PKVRRALRRIEARLRRARAIVDERPGTAVALALDVLRELDTLAAARRAAAE
>gnl|CDD|468542 NF040568, SCO2525_fam, SCO2525 family SAM-dependent methyltransferase. The founding member of this strictly actinobacterial family of class I SAM-dependent methyltransferases, SCO2525, appears to affect development, as inferred by mutant phenotype in Streptomyces coelicolor. SCO2525 belongs to a conserved gene neighborhood that also includes SCO2521-SCO2524
NADADWDRFDPDAYVEHNYATLRDDDRQILELVRDFFADHFRRTSPGPGLRGVDVGAGANLYPALAMLPF
CDRITLLERSASNVAWLRRQVDGYDPNWDPFWDVLRERPAYARVTDPRERLAERARVEQGNLFDLPPRRW
DMGTMFFVAESISTSHDEFRRAVRRFLGALKPGAPFAAAFMENSEGYEVGGTSFPAVAVDEADVRAALAP
VATDVEIHRVESPGEPLRDGYTGMILATGRR
>gnl|CDD|468543 NF040569, DUF2007_rel, DUF2007-related protein. This family of small proteins, 74 amino acids in length on average, includes some proteins included in the seed alignment for Pfam model PF09413 (DUF2007), but most members of this HMM, apparently a distinctive branch within the family of DUF2007-related proteins, fall below the detection limits of PF09413
MKEEDKSSLVEVFRGSPWEAELVKGLLESAGIEAMLKDGGILSILLSYIAPDVAVLVNEEEYEAAMEVIR
EREK
>gnl|CDD|468544 NF040570, guided_TnpB, RNA-guided endonuclease TnpB family protein. This family includes RNA-guided endonuclease TnpB from IS200/IS605 family elements (NF038281) and IS607 family elements (NF038280), but also many additional proteins. It exhibits homolog to or actually includes some CRISPR-associated (Cas) proteins such as the type V CRISPR-associated protein C2c8. For a long time, TnpB proteins were described as accessory proteins in IS (insertion sequence) elements, present as one of just one or two proteins encoded in the element but not necessary for transposition. The programmable RNA-guided endonuclease TnpB proteins may provide a CRISPR-like, widespread form of phage defense by RNA-guided DNA degradation
YKYRLYPTKEQKRELAELFGAARFLYNAALAERKEAYEKNGKFLSYKALLKKLLTELKKEKELEWLKELS
SQALQQALKRLAKAFKNFFKKLKKAGFPRFKSKKKKVPSYTPQSVNKRLRKKRNRKKKNGRLKLPKLGGV
KLRLSRILPILLDGKGGKIKSVTISKPKKGKYYVSISVEVEVPEPPPKEVTGKVVGIDLGLKNFATLSDG
GEKIENPRFLRKKEKRLRRLQRKLSRKLQRKGKGSSNRKKARKKVARLHRKIANQRKDFLHKLSKRLVKE
ADANNVVVEDLEVKGMVKNKKKKKLAKSIHDWAFGQLRRMLEYKAEWYGIKVVKVDPAYTSSQCCSCGGH
RKEKLLLSCREWTCPECGYTVHRDINAAINILRR
>gnl|CDD|468545 NF040571, peroxidase_FMP, peroxidase, FMP-type. This novel form of the heme-binding enzyme peroxidase was originally described as occurring in Flavobacterium meningosepticum (now called Elizabethkingia meningoseptica), hence FMP (F. meningosepticum peroxidase), although the species attribution may have been incorrect
DPVPPYTEEVLQQIVNPADYGVLKQLEGTWVNYNPDNNKTGWGLHTTCMPSPGTNSETIPGKFHFLCEEY
TEELTFTLVPGGVRNRGGANEQFCGAVKYEQSIQDVNGNLIHEENGMYLWLSDMYNHPATEESIKTDIGI
PELKPGAGSNGPYFVPPYSISRSGVIPHGSTITLLGDITESSGGAPQFPSGTAAWDPPHLSISPTMGGAG
ASPKDPINLDEPAPAWVHDTSLPQNDPGSNKTYTQRILAHDLYPYSVRPDLRLRDALKGQNIKNYVLIEM
SSKHDTGPQGGILNTPFVNRFVPVVEMNMRMWIETVIEDGKEILQLQYEQIIFFEFMFGSDGGTTRWPHI
QVNTLRKKE
>gnl|CDD|468546 NF040572, heme_bind_FMP, heme-binding protein, FMP family
LGPLAQLIGTWKNVNGKGWNVIPLPFGGTPGGGGPGFRLLVNPYYETLTFSPIGGPVPNRGGQGDQFLVA
LFYEQRVFDKADDDGIHDEPGYWLYLPDTTQPQPGYTIARSATIPHGDSVLALGSASVVDGAPTIPPVSA
LPIGVGGAPYLAPYKHFHDNPPQFDPVNPNLLLRDALKGQNITSTTVLTVDTTNDGGIANIPFIQKNANA
TSMDATFWIETVDEDGTEFLQLQYSQTVLLDFYPRDGGGISWPHISVNTLVKV
>gnl|CDD|468547 NF040573, holin_dep_muram, holin-associated N-acetylmuramidase. Members of this family are N-acetylmuramidases (lysozymes) associated with the family of large, 3-transmembrane segment-type holins that is described by Pfam model PF11351. All members of the seed alignment for this HMM are encoded adjacent to a holin from that family, and may depend on the action of the holin to access the peptidoglycan layer. Systems including the holin/N-acetylmuramidase may include both gene transfer agents (which package DNA into particles that escape without lysing the host cell) and typical phage
VRQIAEEIVAREGGYVNDPDDPGGATKYGVTIHTMRRLGLDLDGDGRVDAADVRALTRDQAVDIFIEHYF
RRPRIDRLPEALQASVFDMYVNAGANAVKILQRLLRDMGQAVAVDGVIGPQTIAAAAAAAAAAPDHLADA
YGIARRNYYYRLADRRPASRKYARRRDGGKGGWITRAEEFISPRYHLTEAEHRARVAAWG
>gnl|CDD|468548 NF040574, T3SS_ATP_VscN2, type III secretion system ATPase VscN2
MLQHFFKVKESYQDTVVCYVDIDTFVGQECFIHTVGDERIRGEIMKIEGHRVEIKLLQPGTIQRGAKVEI
TPRRFCFPLNEEALIGKVINCYGESLYGEPYLIDEGEYKDLPICIEPIPLKERAPIETVFPTKLKIIDGL
FTIGEGQRLGLFAPAGAGKTTTVSIMANNMDADVVIFAMIGERAREVVEFLEGEIGPEVIQKSITIVSTS
EANPLEKVRSGLVAVSIARYFMEQGKKVVLYFDSLTRFARAQAMLDGTPIQGGIPIGVSLALSRLVESCG
NSIRGSVTGIFTVLIEKEIDSDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKSRLQNKIQDKRYV
QLSERIKDMVYRYFDVELLIRVGEYEKGNDLLTDEAIELYPQIMEFLKQGFDGVEYEETLENMERIWSNY
>gnl|CDD|468549 NF040575, syringactin, syringactin. Syringactin are close homologs of the normally eukaryotic protein actin, found in the plant pathogen Pseudomonas syringae and related species. This model was created, in part, to clarify that the family is real and distinct, rather than an artifact of eukaryotic contamination of bacterial genomic sequence data. As of the creation of this HMM, the family is uncharacterized
LSFDDDKYRLEGVFLKSAASAILFSLDRTKTTLEGETVPEVTGVAIRTDKKTAIITVDPVRVNESGFYEK
LKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC
>gnl|CDD|468550 NF040576, T2SS_GspM_XpsM, type II secretion system protein GspM, XpsM type. This form of the type II secretion system (T2SS) protein GspM (general secretion pathway M - the old name for T2SS) is more closely related to the type IV pilus protein PilO than to other GspM. Note that PF04612 refers to this type of GspM as type b
RLLALGLLVLVLLLLLLLLVHPLLGRLADRAARIAELRDRLARYQRLLAQLPALQARLAELRQAAAARAP
FLPGPTPALAAAALQQRVQAAVAAAGGRLSSSQVLPARRDGPYGRIAVRVSLTGTTEALVALLYDLETGR
PFLFVDDLSIRASRRARDAGARAPSGALDVRLTVSGYRRG
>gnl|CDD|468551 NF040577, cas_Cas7fv, type I-Fv CRISPR-associated protein Cas7fv. Cas7fv is one of the CRISPR associated (Cas) proteins of type I-F variant (I-Fv) CRISPR-Cas system. CRISPR (clustered regularly interspaced short palindromic repeats)-Cas modules are adaptive immune systems found in archaea and bacteria against foreign nucleic acids such as phages and plasmids via RNA-guided endonucleases. CRISPR-Cas systems are classified based on Cas protein content and arrangement in CRISPR-Cas loci into two main classes (1 and 2) and at least six types (I, II, III, IV, V, VI). Class 1 systems utilize multiple Cas proteins and CRISPR RNA (crRNA) to form an effector complex while class 2 systems employ a large, single effector with crRNA to mediate interference. Type I CRISPR-Cas systems are most widespread in nature and the Cas protein composition of the employed Cascade interference complexes differ between seven subtypes (A-F, U). Type I-F variant (I-Fv) is a subtype that rely on a minimal set of five Cas proteins and has structural differences with I-F and I-E Cascades. Double strand DNA recruitment and recognition in the type I-Fv Cascade is facilitated from the major groove side by Cas5fv instead of the large subunit Cas8 and the finger domain of Cas7fv
GIKSVDFKIKALGHGVVNWNGPTTLKQGGDGGVKTVSNHTMPKLRGYTNINGKIKEGGKKFKEATDVDFD
KTPLYISQNCIRHHLFRDEAFGLHLSKDGSNLLKVLSSYTGLIRGYVIPSNGNKRTSPLLITDFVDQLGN
GNFEQLGRSGSKEKEENKSGKESSNSFFSKTTFGDTEYIAYGSISIEQLQFISLDNKFGREAMRIKQGQE
GEEVAEKIEDYIKSLDRCLNPKATYHGNYVRKGTIFSEGEEGILLNDDAIDALVQQTLNRIENLSIRQAK
GYMYVDSVEVDYNDSPKMMRIKRDESTINPEKNSDYAQYYEAK
>gnl|CDD|468552 NF040578, S1_dom_Ygs, S1 domain-containing post-transcriptional regulator Ygs. Ygs, as first described in Staphylococcus epidermidis, is a full-length homolog of GSP13 (YugI) from Bacillus subtilis. Each has a single copy of the S1 domain, an RNA-binding domain repeated several times in ribosomal small subunit protein S1, and each has been shown to be induced by stress and improve survival. Ygs was shown in Staphylococcus epidermidis to affect polysaccharide intercellular adhesin biosynthesis, and through it, biofilm formation. More recently, the full-length homolog CvfD was shown to be a post-transcriptional regulator, suggesting all members of this family are
MNKHYKVGQHIKVKVTGIQPYGAFVETPDNTEGLIHISEVMNDYVHNLKKFLSEGQIVKAKILSIDEEGK
LNLSLKDNDYFKNYERKKEKRSVLDEIRETEKYGFQTLKERLPVWIKQSKKA
>gnl|CDD|468553 NF040579, S1_dom_CvfD, CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator. CvfD, Ygs, and GSP13 form a family of full-length homologs of RNA-binding proteins from the Firmicutes with a single copy of the S1 domain. Several members of the family have been characterized as general stress proteins, and the most recently characterized, CvfD, was shown to act as a post-transcriptional regulator
YKIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKHGYVKDINDFLKVGQEVKVKVLDIDEYTGKISL
SLRALEEAPEKHRKRRKHRWTNKRLKIGFNPLKEKLPEWIEEA
>gnl|CDD|468554 NF040580, MBL_fold_Vmh, Vmh family MBL fold metallo-hydrolase. Members of this family are zinc-binding enzymes with a metallo-beta-lactamase fold. The founding member, Vmh from Vibrio vulnificus (AAO08273.1), was described as having actual beta-lactamase activity. Because the search for beta-lactamases in known and potential pathogens has been so intense for so long, the potential zinc-binding motifs differ so greatly from those of the well-characterized metallo-beta-lactamases, and reports of beta-lactamase activity have not been widespread throughout this family, the question of whether the beta-lactamase activity seen for Vmh is essential or incidental is not yet answered
MKLSRLALLTALLFSAAASAAPLTLTTYNPQEKGIFPVSSTLVSGPKEAILFDAQFSVKDGEKLVEMIKA
SGKKLTTIYITSGDPDFYFGLEPLVKAFPNVKVVATPAVVKHIEATKDAKLAYWGPILKDGAPTKLIVPQ
VLNATTFTLDGEKIEIKEPNTYAAYLWIPSNKTILGGVGVYSGIHVWTADTQTKEARQQWRQTLDRMKAL
KPERVIPGHYLGEIPKGTEAVTFTRDYLQDFEQALKKHKDSAGVIEAMKAAYPNLAEESSLELSAKVNTG
EMKW
>gnl|CDD|468555 NF040581, cas_Crn1, CRISPR-associated ring nuclease Crn1. Ring nucleases cleave second messengers such as cyclic oligoadenylate produced by type III CRISPR system effectors, in order to provide an off-switch for the regulation of CRISPR activity. This family of ring nuclease, which includes Sso2081 from Sulfolobus solfataricus, is designated Crn1
KLVATLGTSPGGIAETFENLRKGNYEAEFPKPVKIDEIYVIRTKDKEVEKAWKLLKAIFLCCVKPFVEIA
EIPLPIDDITSPEDFITFREEVRKVLSPGDYVDFTGGRKAMSVAAALAAREAGAHLVTTIIPQEEYNRIN
EKIRELKDREEEVERKGCCEDCKEYFCSLISKNARTIVF
>gnl|CDD|468556 NF040582, STY4528_fam, STY4528 family pathogenicity island replication protein. The founding member of this family, STY4528 from Salmonella pathogenicity island 7 (SPI-7) of Salmonella typhi, belongs to the core set of proteins of SPI-7-related conjugative elements, and is assigned to the replication region. Members include a protein designated Api5 from the Yersinia pseudotuberculosis adhesion pathogenicity island (YAPI)
SGLLFSGNVHDTVPRRLLLDTRLTPLEKNAWQVIRLLAQENGGAAFPTYDELQPYLSASPCGGKASRETV
ARALTMLRLTRWLSLCRRVRDEKGRVRGNIYALHDEPLTPADAEQLDPDYLDLVAQALEHANKAVREVAQ
HVLQEIAQDPDTMRHLPSRLDVIEERLGAPQTPQQMAARRASRTQSSLSQSELSSDSEGSSLSLLRNSNS
PSSDSELSLKSLSYGSVRNPNSDRTRRSTTQSVNKVTYVPGAGEEELRLPEALPLLLAEQQRGALAALLQ
VLPELRQAVLDELQARCRSGTVRNPVGYLLALIKRAREGEFNA
>gnl|CDD|468557 NF040583, dnaB_SPI-7_type, SPI-7-type island replicative DNA helicase. Members of this family are DnaB-PI, a pathogenicity island (PI) variant of the replicative DNA helicase DnaB. Members are found with other conjugative element replication proteins such as ParA, ParB in genetic islands whose core proteins (but not cargo proteins) are shared with the Salmonella typhi SPI-7 island
GPYSVEAEQSVLGGLMLDNDRWDDVALLLAADDFYSRAHRIIFRAMARLVSAGQPIDLITLSESLEQQGQ
LEQVGGFAYLAELSKNTPSAANIVAYAEIVAEYSRARQLLALGHDLSADASAPRADIADLLEQAEQRLFD
IAEQAEPQQEVTLIEGLETLVSELELRCQSGNGITGTPTGFAELDEMTCGLQPGDLILLAARPSMGKTAL
ALAFCLGALRGKPDKVVQIYSLEMPTEQLLMRLVSMLGRVPLQRLRSGLLDDEDWARISQAMALLTDWKD
RLIIDDTSYLTPALLRARARRNARKYGKPSLIMVDYLQLMRCPGQENRTQEIAEISRSLKALAKEMGCPV
LALSQLNRQLESRADKRPNNGDLRDSGALEQDADLIMFIYRDEVYNPNTPDKGIAEIIIGKQRQGPTGTV
KVQFDGRYTRFSDL
>gnl|CDD|468558 NF040584, STY4534_fam, STY4534 family ICE replication protein. Members of this family regularly are found near a TopB family topoisomerase, in mobile elements such as certain pathogenicity islands, in regions of those islands thought to be involved in replication. The founding member of the family is STY4534 in Salmonella pathogenicity island 7 (SPI-7), a core protein shared by members of SPI-7's subclass of integrative and conjugative element (ICE)
NYFNLHITGIGYLNNIREVEPKKGGPFLACVIAALSGPTDNPEYTRFDCTVAGKEAEKLIKRCQKAVDEE
KKVLIGFVLSDLWTDTFTYSKGDKAGETGVSLKARLIRIDWIKVDGEMVYKAEKR
>gnl|CDD|468559 NF040585, SjiA_fam_FXSXX, FXSXX-COOH family cyclophane-modified RiPP peptide SjiA
DTKSRATEADSAAAEAQSTRPVPVRLAKRGDAAHSLMLSRVLPDNGVSRLDVAAFNSSI
>gnl|CDD|468560 NF040586, FxSxx_TPR, FxSxx-COOH system tetratricopeptide repeat protein. Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids
VPPRNPNFTGREELLERLRDQLRSGGAAVVPQALHGLGGVGKTQLALEYAHRFRADYDLVWWIPADQPEL
VRASLAELARRLGLPLGPDDVDEAARAVLDALRRGEPYRRWLLVFDNADDPEDLRDLLPTGGPGHVLITS
RNRAWSEVAAATLEVDVFSREESVALLRRRVPGLTSEEDADRLAEALGDLPLALEQAAAWLAETGMPVDE
YLRLLDEQATAALLLELKPPGYPTSVAATWRLSLDRLRERSPAAARLLELCAFFGPEPIPLDLLRSSDEM
ARLLLPYDLRLRELLLDGILLSRALRELGRYALARVDSGRRTLQVHRLVQAVLRDRLSEEERARARHEVH
RILAAAAPGDEPDDPRNWPRYAELWPHLEPSGALESDDPEVRRLLLDQVRYLYLRGDYESARDLAERALE
RWRERLGPDDRQTLRLRFHLANALRSLGRYEEARELDEDTLERQRRVLGLGEDHPHTLMTAGGLGADLRA
LGRFREALELDEETLERHRRVFGEDHPRTLRAANNLAVSLRLLGDYREALELDREVLRRRRRVLGPDHPR
TLLSANNLARDLRELGRYAEALDLLEEALERYREVLGGPDHPDTLRAAKSLAVALRRAGRLEEALELAED
TYERYRRRFGPDHPDTLAAALSLANDLRALGDADEARELAREVLDRYRRVLGEDHPFTLACRNNLAVLLR
ALGDPEEARELAEAALEGLRERLGPDHPYTLAAAVNLANDLAALGDLDAALGEEALERLRRLLGEDLRAG
PDHPDTLACAANLALDLRATGRTEEAEELRADTLARLRRVLGPDHPDTVAAREGRRLDRDIEPPPI
>gnl|CDD|468561 NF040587, rSAM_lost_HExxH, FxsB C-terminal extension domain without HExxH motif. This HMM describes a branch of the TIGR04267 domain family in which the presumptive metal-binding motif, shared by many metallo-proteases, has been been lost. The domain appears as a C-terminal extension for some of the radical SAM enzyme family FxsB proteins, involved in post-translational modification of the 60-amino acid long RiPP precursor proteins, collectively named FxsA
ALSPAVTDPDELRLAQLDLTRTLLARLHDRLAGRGGADWDEAWRLALALDADEATAAHLDTVLAHPYTRT
WLLRALDGLRAGRPDAVPAALRLAAVVAAAAVRAGLDLPVPVAYRDGVLHLPTLGTLRLGGPGERGRAEV
RATGGGFLVRRPDGGERRIVPPAEPGPGWRPVRTVGLAGAPALLLDDLDPYRDCFDAPVADRLGPSDAAA
WAERLRAAWELLDRAVPGQAAEAALSLTTLTPLAPGTGVRLGRHGPGALGVALDADPEELALALLRGGRR
ARLRALREVTDLYALDGAWEHPAPWQEEPVPASRLLAEAYERVGLGAYDPRFAEGALEALDALEAAAELT
VSGKRLVAELRKEL
>gnl|CDD|468562 NF040588, FxsC_Nterm, FxsC protein N-terminal TIR-like domain. Members of this protein family, FxsC, occur in the context of FxSxx-COOH class RiPP precursors (FxsA) and their radical SAM/SPASM domain maturases (FxsB). Most but not all members have an additional C-termimal domain (see TIGR04276)
PYFFLSYARTPRSGAGSPDPDEWVERFYDDLCAHVAQLTGLPAGSTAGFLDRGMRPGADWSEELGEALAH
CRVFVPLYSPRYFSSEYCGREWTAFRRRLRSHRARTGGRAPAIVPVLWTPVPPRTHLPEAARRLQYDHAE
LGEEYAQNGLYGLLRLGRNGRDEYERVVWALAQRIVAVAEQ
>gnl|CDD|468563 NF040589, Synergist-CPBP, SYNERG-CTERM system CAAX-type protease
IGLAVAAFMLYFPYLWCRLRKESPEDYGLKWFLTRRAWRDVLLALALTLIPLTFIALHWPGEWLPRGPGL
PVALDLLGSGLAAAVIEETFFRGWLQTLLSRRLGPLAAIVLASLLFALSHLIVLPGPLRLATFFPGLVMG
LLRHRHGSVLPAILYHALGNIWAIWFFPLP
>gnl|CDD|468564 NF040590, Pyro_CPBP_1, CPBP family archaeomyxosortase MrtA. Members of this family are CPBP family (CAAX-like) intramembane metalloproteases that are found only in the branch of the Archaea that includes the genera Pyrococcus, Thermococcus, and Palaeococcus, and appear both universal and highly conserved in sequence within that lineage. Comparative genomics suggests this enzyme, distantly related to Rce1, processes the C-terminal sorting signal CGP-CTERM. Because CGP-CTERM resembles MYXO-CTERM, processed by bacterial myxosortases, we designate this protein archaeomyxosortase
NPYLLYLILLPLSFVPRLFGGNFFEWALYLLLFYLLVPLILALLLGFKPKELGLKLPKREGYKLALILFL
LAIPLSFYGLTIPSMRSYYPIFPYSSWLDFLLKELAIGVIMFAHEAFFRGFLLFPLAKKNEWLAILAQDI
PYTLVHIGKPGIEIPYSFIAGIVFAKIDLKGESFLPSFLLHWLGSAFFDVLCAL
>gnl|CDD|468565 NF040591, choice_anch_O, choice-of-anchor O protein. Members of this rare protein family have been observed with the JDVT-CTERM sorting signal at the C-terminus, or with a low-scoring variant of the GlyGly-CTERM domain (see WP_188923155.1), or with alternative sequence regions not currently recognizable as sorting signals or homology domains. The function is unknown
ARDIFVRVSLDDGSTWKPTNLSNTADLSSIDVDWNGDGSTAYPGDSDKPNIAAAGNNVLVAWNDKYCPGG
NPPTDLYLPDLFGVNGSQGSVDYEGRDGREPVGEVPFSCVWTARGVSEEGDDGITWSKAEQLTSGRRDAN
QDENAASEGGGFALTWQEDPEGLRPGEGEGPGDGWSGASANHGTDIWYSYISTADFDTVDDTGDTGKPKS
AIPFSMPVRITDNAVCNVTNPGPYCTGADYDGNLCATTGTDPTGNDDKCVTEDGLILSGDTAATRPNLGL
VGATVVVAYEETKGEDLEGDPNSEGLDEGKNVRYHSFPMNTPDTVETYPPVSAGCIINFDDYDPTENARR
VRLVPQSDAGAGESGLRAGILWKQGIMTQGGPSDIMARRATGGYSPANMNPAVDMNCATSDYADASGLCN
DPAINLSSRTPDTCATTDAGEDTTLTWHGSNLDDQTWENPLENAKGHRGFLRGDDVYVGYAYTPNWALNT
YGNDRYNFYIRRSFDGGSTWTAPRNVSQLTDNQITTLDPRFVPTPESITGADPLGEDCRNPNRFFVAWGT
GDNVTEALGEPEELDLFYTRSTDKGETYEPVVRISEFDNLAIGKSGAEEFESQLQASPDGETLYAVWNQ
>gnl|CDD|468566 NF040592, tRNA_mod_ArcS, archaeosine synthase subunit alpha
EVHKRDGAARIGELRLSEPVTTPALIDDDLVDAGSLWAAEREVPEGDGIKNLTILPHRAFPEGTPEEVQE
AFAKDHPDVDYPSAGVVSSTAEDEGGDAYVLSNAGGLVGHARAFVEAIIELREKIPPDTALYAPGVATPS
NVALLVYLGVDLFDNTRAKLAAAQGIYLTPEGEFFLEDLEELPCSCPACRGPDLEFTREDLADHNRNALE
AELALVRERIREGRLREYVEGQARHEPWLTALLRLLDRQYDYLEERTPVFRSSELLATTSDSLRRPEVQR
FAERVTERYRPPFDTVLVLLPCSARKPYSLSQSHRQFIDAIGKRRKRVHEVILTSPLGVVPRELELTYPA
QHYDTPVTGYWSEEEIEFVAEVLERYLEKNDYPRVIAHVPGGGYREICERVEDALGIEIEFTVEGHPTSD
ESLSNLKAALEGERKYRKREREHNTIRAIADYQFGAGAGDALFPDTKGRYPKLQVFDGKEQLATLVPQYG
LLSLTLEGARRWVESDAPTYRVEIDDFVPKGSVLAPGVVDADERIRPGDEVVVEGPKAFGVGRALMSGPE
MVESTRGVAVDVRHV
>gnl|CDD|468567 NF040593, CAAX_MXAN_2755, MXAN_2755 family glutamic-type intramembrane protease. Members of the family are restricted to the taxonomic order Myxococcales, within the Deltaproteobacteria. The N-terminal region is a domain unique to this family. The C-terminal domain is an CPBP family (Rce1-like) intramembrane protease domain (see PF02517), related to eukaryotic CAAX endopeptidases, which cleave at the site of a prenylated Cys residue in a C-terminal motif involved in protein sorting
SRADRTPWRPSAVQEAVGLWALGFLGIIAAFLLFGGTSVPKLVATVGFLYLPLIPMRWRDEDYRDYGLTL
RAWRQDVRLFLGMSAIVGPLFFAGFALFVEVLPHLPEELARLLTPFRGEGHFQPRLPPRFGEWVVDQLFV
VALPEEFFYRGYLQTRLRDAWPQGRRVLGVRLGPAFWLTALLFALGHLAIFQAWRLSVFFPALLFGWMRE
RTGTVVGAALFHAACNLYVRFLEVSFFG
>gnl|CDD|468568 NF040594, CPBP_fam_mrtC, MrtC family glutamic-type intramembrane protease. Members of the family are restricted to the taxonomic order Myxococcales, within the Deltaproteobacteria. The N-terminal region is a domain unique to this family. The C-terminal domain is a CPBP family intramembrane metalloprotease domain (see PF02517), related to eukaryotic CAAX endopeptidases, which cleave at the site of a prenylated Cys residue in a C-terminal motif involved in protein sorting. The founding member of this family is from Chondromyces crocatus
VLLAALVVTALVTALSRGLPDRYAATGVGVAFLFATWALVLRRDDPAGVRRYGLSLGGLLEPAPLDPRRL
ARALGRALGWALGLAAVVFPPFAFGFRLWWHPSRAFALSAPPDLADEALGQLLVVALPEEAFFRGYLQTR
LDDAWPPRRRRVLGAELGPGLLLTSALFALGHVLTEPHPARLAVFFPSLLFGWLRARTGGIGAAVVFHAL
CNLFSELLGRG
>gnl|CDD|468569 NF040595, HTH_Cbp1, CRISPR DNA repeat-binding protein Cbp1
EEELIEKIKKMYEEGKSIREIAKELGLSYSKVRRILIKAGVKFRGKVPDELVEKIIELAKQGYSANRISK
ELNLNENTVLRILKKHNLGKRKRKLSKEEIEKIKEMYKKGESIYKIAKELNISTNLVVYHLKKLG
>gnl|CDD|468570 NF040596, MXAN_2562_fam, MXAN_2562 family outer membrane beta-barrel protein. This homology domain, found in Deltaproteobacteria such as Myxococcus xanthus, comprises the near full-length of proteins about 240 amino acids in size, or the C-terminal domain of longer proteins. A distant relationship to PF13505 suggests these proteins may form outer membrane beta-barrels
HFAVELRFGGYLPDIDDEFGLGGGPYADTFGDKSRFLFGAELDWFFLPGIGTLGVGVGAGYTEASGKAQL
AGSGSESADRTSLEVIPLHLSAVYRFDYLARRWGIPLVPYGKGGLGYGFWWVTKGDGTEVVDGVKGRGGS
WGWHAALGLMFLLDFLEPRAARSLDRDTGINHTYLFAEYTYADVDNFGGDGSLNLGDSTWMFGLAFEF
>gnl|CDD|468571 NF040597, carb_anhyd, carbonic anhydrase
MKFNQIFTILILSLSLTLAGSGCVSEGEGAEDNVAQEITESEFSNIRANPVTPWNPEPTEPVIDPTAYIH
PQASVIGDVTIGASVMVSPMASVRSDEGMPIFVGDRSNVQDGVVLHALETIDEEGEPVEENLVEVDGKKY
AVYIGERVSLAHQSQVHGPAYVGDDTFIGMQAFVFKAKIGNNCVLEPKSAAIGVTIPDGRYIPAGTVVTS
QDEADKLPEITDDYAYKHTNEAVVYVNVNLAEGYNAAS
>gnl|CDD|468572 NF040598, Ala_zip_lipo, Lpp/OprI family alanine-zipper lipoprotein. This model derives from PF11839 but is more narrowly focused. All member sequences of the seed alignment are bacterial lipoproteins between 78 and 103 amino acids in length. Members include OprI (major outer membrane lipoprotein I) from Pseudomonas aeruginosa, and Lpp (Braun's lipoprotein), called the most abundant protein in Escherichia coli. Lpp becomes covalently linked to the cell wall, while anchored in the inner leaflet of the outer membrane, providing structural stability to the cell envelope
KKLKLSALALSLALLAGCATTSDLENLQSQVQELDAKVDQASSDAAAAQSRADEAAAKAEQAEAAANAAQ
QEADEANERADRMFKKSMRK
>gnl|CDD|468573 NF040599, LdtF_DpaA_YafK, peptidoglycan meso-diaminopimelic acid protein amidase. DpaA (previously YafK and LdtF) murein L,D-transpeptidases, but actually functions as an amidase. In E. coli, the most abundant protein is the lipoprotein Lpp, anchored to the inner face of the outer membrane, but cross-linked to the peptidoglycan cell wall by the transpeptidases LdtA, LdtB, and LdtC. DpaA (peptidoglycan meso-diaminopimelic acid protein amidase A) is an amidase that hydrolyzes those linkages
MGKIALLLAMLFSLPAVSFASSSASEVVPVAPVSKQQLLGSPVYIQIFKEERTLELYAKIGNEYRLLDSY
RICNFSGGLGPKRREGDFKSPEGFYSVDLRQLKPDSRFYRAINIGFPNEYDRAQGYSGKYLMIHGDCVSI
GCYAMTDAYMDEIYQYVEAALRNGQPRVEVSIYPFRMTDQNMQRHRNSSYINFWRQLQPGYAYFVQNHQP
PAVSVNNGQYVVNQPSLAASQLASNLALTEAK
>gnl|CDD|468574 NF040601, TerS_not_xtmA, phage terminase small subunit. Members of this family are phage terminase small subunit proteins, based on adjacency to terminase large subunit proteins, and on a small N-terminal homology domain, described by PF10668, about 67 amino acids in length, shared with TerS from PBSX (XtmA) and from phage related to PBSX. Terminase small subunits related to XtmA of defective prophage PBSX have a C-terminal PF03592 domain, accounting for most of the length of those proteins. Members of this family differ from XtmA-like TerS over most of the their lengths, C-terminal to the PF10668 domain, and show no trace of homology to PF03592
MARARSPNRDKAFEIYLESGGKITLKEIAEELGVSEKTIRKWKSQDKWDGESTTKKKKENTTNKKGAPPG
NKNAVGNGGGKGGAPKGNKNAVKHGEYEKILPDTLSDEEKEIYEEIPPDPPLDLLWEIILLQYRAIRRAQ
RIMFVEDGDDMTKEEKLQELVPGGKDGKTEEEYKVQFAWDKIAAFLEAQSRAMGTLAKLIKQLDELAFSD
DERELELEQQELRIEKAKA
>gnl|CDD|468575 NF040602, F420_dehyd_FpoD, F420H2 dehydrogenase subunit FpoD
EIKGPSEMIVHMGPQHPMQPGPFRLNLKLKGETVKDAFVELGFIHKGIEKILENKTYLQGIPIVDRMCYL
AALTNEEAYCGCVEKLAGIEPPERAQYIRVILEELSRIQSHLLGTGEFGEFIGFVSMFMYTIKDREDILS
LIESVTGARITHSFLRFGGVRDDLPEGFKEKCKKVFAYLRERIEEYEELFSSDTIYKERTVGIGVLTPDT
AKRLGVSGPPLRATGVPFDIRKDEPYLVYDDLDFKVCTETAGDSYARIQVRLDEIRESMYIIEQCLDQIP
SGPIFPEDLPYGKRTPVMRVPPGEVFYRVEDPRGEMGFYMVSDGSDKPYRVKVRGPVYPTMQALPPLIKG
VYIADVVAIAGSMDGCTSEVDR
>gnl|CDD|468576 NF040603, choice_anch_P, choice-of-anchor P family protein
FSGSAYGTRVNVGGGVTSGPTALVSLPCTGTGGGTATNTVAGVNVPVLTAGAVTTTATGTVTATGATATS
TATVAGVNLLGGLITADAVTATATATATGGGGSSSSGGSTFVGLTIAGVPITVSVAPNTTIDLPGVGTVV
LNEQIRSADGGSAGITVNALHVVLLAPNGLPVGADIVVGSATAGVT
>gnl|CDD|468577 NF040604, HacB_Meth, homoaconitase small subunit. Part of the 2-oxosuberate biosynthesis pathway in methangoens
MIIKGRVHKFGDDVDTDAIIPGPYLRTTDPYELASHCMAGIDEDFPKKVKEGDIIVAGENFGCGSSREQA
PIAIKYCGIKAVIAESFARIFYRNAINIGLIPIVCKGITKEVKDGDIIEIDLENEKIIINDKKTLNCEVP
KGIEKEILDAGGLINYAKK
>gnl|CDD|468578 NF040605, mycolic_FabG1, 3-oxoacyl-ACP reductase FabG1
SRSVLVTGGNRGIGLAVAQRLAADGHKVAVTHRGSGAPEGLFGVKCDVTDSESVDRAFTEVEEHQGPVEV
LVANAGITDDTLLMRMSEEQFEKVIDANLTGAFRVAKRASRAMLRARFGRFIFLGSVVGMMGTPGQVNYA
ASKAGLIGMARSLTRELGSRSITANVVAPGFIDTDMTAALDDKYQEMALQAIPLGRIGKPEEVAAVVSFL
ASDDSSYVSGAVIPVDGGMGMGH
>gnl|CDD|468579 NF040606, CytoC_perox, di-heme-cytochrome C peroxidase
WSDEDRQWFYFTSQGSRLLPYDWFLALEQPDSEELFRSDENLARLGYLPQKPSSLNPDGLPVGFAKDQDP
DGTGEPWVGLTCAACHTGQITYQGTAIRIDGGPALADFQGFLQALVAALAATLNDPAKFDRFAARVLGAD
DADRAALRAALKAFLAWLARAAYNAANRGLYPTEYGPGRLDAFGRIFNRVAALALGIPENYRPADAPVSY
PFLWDTPQFDWVQWNGSAPNADIGPLGRNVGEVLGVFGDVDLKPPPAGLRGYPSSVRVRNLGRLERLLRK
LKSPKWPEDILGAIDAALAARGRALFAQNCASCHAPIDRDDPGRPIKAVTMTPLDEIGTDPTMACNFATR
RADTGKLEGTKAPLLLGGEPLEPVDPAADLLANAVAGVIAEVEDRAYRDAGIPDERLLAALDGYGLPPGD
KEPRAYKARPLNGIWATAPYLHNGSVPTLYDLLLPPEERPKTFYVGSREFDPVKVGFVTDAFPGGFLFDT
RLPGNSNAGHEYGTDLSDEERWALIEYLKT
>gnl|CDD|468580 NF040607, mycolic_Pks13, polyketide synthase Pks13
MTVAELREWLRNWVANATGQPADQITDDRPMEEFGLSSRDAVALSGDIEDLTGVTLTATVAYQHPTIASL
ATRIIEGEPEVAADDDDDADWSRRPRSDAHDIAIVGLATRFPGAGNTPEEMWEALIEGRDGITDLPEGRW
SEFAADPRIAERVAKANTRGGYLDDIKGFDAEFFALSPLEAENVDPQQRLALELTWEALEHARIPASSLR
GEPVGVFIGSSNNDYQMLAVADPAEAHPYALTGTSSSIIANRVSYFFDFRGPSVAVDTACSSSLVAVHQA
VRALRSGEADVAVAGGVNMLLTPAVTLGFDELGGVLAPDGRIKAFSSDADGMVRSEGGGVVVLKRLADAR
RDGDTILAVIAGSAVNSDGRSNGLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTGTILGDPIEADA
LGRVVGRGRDADKPALLGSAKTNFGHLESAAGAAGLAKVVLAMQHDKLPPSLNYAGPNPYIDFDAEHLKV
VDEPTEWPRYSGHAVAGVSGFGFGGTNAHVVVREVLPADLVEPEAQPDEDTEAELAGLTAEAKRLLAEAE
LAAEFAPAAPEGPVVPLPVSGFLPSRRRAAAADLADWLESEEGRATPLADVARALARRNHGRSRAVVLAH
THEEAIKGLRAVAEGKPGPGVFSADAPAANGPVWVLSGFGSQHRKMAKQLYLENPVFAARIDEVDELVQD
ESGYSIVELILDDEQTYDIETAQVGIFAIQIALADLLRHHGAKPAAVVGHSMGEAAAAYAAGGLSLEDAV
RVICHRSRLMGEGEAMLPGDDIRLMALVEYSAEEIETVLADFPDLEVCVYAAPTHTVIGGPREQVDAIVA
RAEAEGKFARKLQTKGASHTSQMDPLLGELAAELAGIEPQPLTVGLYSSVDRGTFYRPGHEPIHDVDYWV
KGLRHSVWFTQAVRKAVDAGHTTFLELAPNPVALMSVAATTFAAGLHDAQLIPTLKRKEDESESVLNALA
QLYVHGHDVDLRSLFGAGDYADIPRTRFKRKPYWLDARPSSGGGSGRMPGAHVALPDGRHAWEVAASAVT
DLAALVKAAAAQVLPDATLTASEEHAELPASGTLTTTLTRHPGGASVQVHARIGESFTLVAEAVVTGGGA
LPAAVGAVAAAVASAAAVAAAAVAAELSDEVVADAGLGADADRWDPDSGETVEDRLAAIVGESMGYDPED
LPREIPLIELGLDSLMAVRIKNRVEYDFDIPPLQLQAVRDASLADVEKLVEYAVEHRDEVAALAAQAQKG
AEEIAAAAAEIEAAAAAEAEAAAEEAAAAAPEAAAAAPDPAADVLTQEAVAEALGVDVPPRDAAERLTFA
TWAVVTGKSAGGIFNELPVLDEETAEKLAARLSERAGGEEITVEDVLDAETIEELADIVREHLEAGDVDG
FVRTLRARPEGSDAVPVFVFHPAGGSTVVYEPLLKRLPADTPVYGFERVEGSIEERAAQYLPKLREIQGG
GPYVLGGWSLGGALAYAVAQQLREEGADVAFVGLIDTVRPGEPIPDTPEETRARWERYAAFAKKTYGLDF
PVPPELEELGEADDEGQFKIILDMVKASGVKIPGGIIEHQRTSFLDNRALDTVDPSPYDGPVVLYRADRM
HDGAIELEPAYAEIDPDGGWGEIVDDLEIVQIGGDHLQIVDEPYIAKVGAHLTERLAEIEA
>gnl|CDD|468581 NF040608, division_SteA, putative cytokinetic ring protein SteA. Members of this family on membrane proteins from Actinobacteria were reported (in 2019) to be SteA (Sensitive To Ethambutol A), a cytokinetic ring protein that partners with SteB and contributes to proper cell division. A short region of sequence similarity to some proteins characterized as thiamine pyrophosphokinases may cause confusion in functional annotation
IKGTARVDRRTKKLVKRLGPGDIAVIDHPDLDRVAAEALVEAGVKAVVNAAPSITGRYPNLGPRILLDAG
IPLIDDVGEDVFDRLKDGDKVEIRGGEIYVGDELIARGEELTSETIEERLAEARENLSDELEAFIGNTLE
YARKEKPLLLDGLGIPDLKTDIEGRHVLVVVRGADYREDLKALRSYIREYRPVLIGVDGGADALLEAGYK
PDLIVGDMDSVSDEALRSGAEIVVHAYPDGRAPGLERIQDLGLGAMTFPAPGTSEDLALLLAYEHGAELI
VAVGTHSNLIDFLEKGRKGMASTFLVRLKVGSKLVDAKGVSKLYRSRISGKGLAWLVLAALVPLAAVLLI
SPPGGDFLDLLWDTWNLLA
>gnl|CDD|468582 NF040610, F420_dehyd_FpoH, F420H2 dehydrogenase subunit FpoH
EIPAIIIPPWIRGLVGLALIGAVFGGAMLAVWLERKLSADIQFRYGPNRVGPWGILQLVADAIKLFTKED
IIPRKADKLLYVSAPIVAMGSVFLMLVAIPFGAVIINGVEYPLVVTNMDISILYIEAVSAISIIGIFMAG
YSSNNKYSLLGAFRNFARMIGYEVPLGICVVSVAIMAGSLNIVEIVEAQSPIWFAFLQPIGFIVFFIALM
ADMGRLPFDQNEAEEELIAGWITEYSGMRFGLGFFAEYIHLILGSFLVVLLFLGGWNLPGFVTDIPVLGI
ILPTLFFLMKVAIVLMFIIMIRWAVPRFRIDQVVDLSWKRLLPLSLLNLGWAIALGLYL
>gnl|CDD|468583 NF040611, F420_dehyd_FpoC, F420H2 dehydrogenase subunit FpoC
MDAKTIIDSLTGKFPEAISDATIESEIRISAYVDAENVVEVCRYLKDELQFDHLCSETGVDYIKRNEIEV
VYHIASYDHPVVLTLKARLPRDNPEIESIVPVYWNANWYERETYELFGVQYKNHPDLRPLVLPEELLGEW
PLRKDYEGFPNKTAKNLV
>gnl|CDD|468584 NF040612, F420_dehyd_FpoI, F420H2 dehydrogenase subunit FpoI
MVLKNIKKALKNIYKPPVTRMYPEEPSELSDRFRGLQKLDKSKCIGCGICANTCPNNAIKIVRARVSPDS
DKQRWFPEIDIGHCLFCGLCIDQCPKEALSSTKVYTTGVIKWKHEDLLFTPDMLAREVDIGEEEE
>gnl|CDD|468585 NF040613, F420_dehyd_FpoJ, F420H2 dehydrogenase subunit FpoJ
IIPRILGMLVALLFLAVVLVSVFGTSWPTVDQLPQNIEDQSNIEGIGVLIFTDFVVPFEILSIVLLSSLM
GAIYMAKGDDN
>gnl|CDD|468586 NF040614, F420_dehyd_FpoK, F420H2 dehydrogenase subunit FpoK
PLELYLGLAAIIFSIGLYGFMTQKNGIRLLMCVELMLNSANINLVAFSSYNDDLTGQVFALFSIALAAAE
AAIGFAILMAIYRMRDTINLDNINILRW
>gnl|CDD|468587 NF040615, HacA_Meth, homoaconitase large subunit. Part of the 2-oxosuberate biosynthesis pathway in methangoens
MTLAEKILSKKLGKEVYAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANTVK
AANMQKITREFVKEQGIKNFYLGGEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMG
YIYATGKTWIKVPKTIRVNIVGKNENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCN
MAIEMGGKTGIIEADEITYEYLRKEGVSEEEIAELKKNRITVNEKEENYYKEIEIDITDMEEQVACPHHP
DNVKPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIF
VKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGNINSYIYLSSPKIAAKSAVKGYITNEE
>gnl|CDD|468588 NF040616, F420_dehyd_FpoF, F420H2 dehydrogenase subunit FpoF
HPKILEVIEHDVCTACGACVSVCPAGAITMNKKAEIRDPDNLELYEKGAAPNVCEGCLTCGRVCPVVDGY
VEDEFANVKSFFGAKSNIEGQDGGVTSAILKSLLEKGEIDCVVGITRNENWETELVLMTKPEDVDRTTGT
KYTYDSVLSALREPFEKYDRIAVVGVPCQAHGARLISENVNDKIVLIIGLLCMESFYHDVMTEKIIPEIM
GLNIEDVVKMDFGKGKFWAYTKDGEEHSVKIPEVAPHARNPCHHCCDYTSVFADISVGSVGAPDGWNSVL
IRTDIGEKYFDMVEDELEIMEDPKPGMDLIKKLAKMKHDNNSEHYLEVCEKFSFDEC
>gnl|CDD|468589 NF040617, F420_dehyd_FpoL, F420H2 dehydrogenase subunit FpoL
AIGDFAFLIPLLPALAFVLTFFLGKKLPSGGAIIPIAAIAASFVISLLITLNLLQNPEEVVSQSYHWFAI
LNLGILIDPLAAVMLTMVTFVSLLIHIYSVGYMSHDPAKPRYFAETALFTASMLGLILSDNILQLFISWE
LVGLCSYLLIGFWYQKPSAASAAKKAFLTTRIGDVMFLAGIILLFSDLFKIFNGNIPEGVYLLRFDEIFN
HIPELAAMNATILGFEVSHLTLITLLFFGGAVGKSGQFPLHVWLPDAMEGPTTVSALIHAATMVTAGVYL
VARTFPMFIAAPDSLIVVAYLGAFTALFAATMGIVMNDLKRVLAYSTISQLGYMMLGLGMGAVIGAEAVG
VSIFHLINHAFFKALLFLCAGSVIHAVGTHDMRQLGGVGKVMPITAATMLIASLALAGFGIPGTSIGTSG
FFSKDPIIEAAYLFGEHTGNWLPYLFAIVAALLTSIYIFRLIFMTFTGKPRTDYGGHESPASMTVPLSIL
AIFALVFGALTRTPFNHFLEETFVNNFVNMDIEALAELGNYHLAHHAGHEPLLILWMPVIVAVAGLVIAY
LIYYLRVIDMSSLVSRNNPVYKLLYNRYYQNEIFTEFFAVKIVYEGIALAGYHIDRGIDWIVNGISDITI
EAGESLRKIQTGVVQNYATAVIAGVSLLIILVKLIMEVL
>gnl|CDD|468590 NF040618, PPA1309_fam, PPA1309 family protein. This family of uncharacterized proteins, restricted to the Actinobacteria but absent from the genus Mycobacterium, is named for founding member PPA1309 from Cutibacterium (Propionibacterium) acnes
LAAAVLEIERHVAAEGWDQPPRLFALVPTAELLAAEPALADQLDDSAPDPLTPVEQEDLPAGDDLEELLA
TIAWPDAVAGCALAQERVVLPPEAEADLPDDDEAARAAAAAHPDRQDVRLVVGVLRDGTSLCLLRLRPHD
DDDELLTGPDLAPGLVAALRATLE
>gnl|CDD|468591 NF040619, AksF_Meth, homoisocitrate dehydrogenase
MPKICVIEGDGIGKEVIPETVRVLKELGDFEFIKGEAGLECFKKYGDAIPEETIEKAKECDAILFGAVTT
PKPTELKNKNYKSPILTLRKELDLYANVRPINNFGDGQDVKNIDFVIIRENTEGLYVGREYYDEENEIAI
AERIISKKGSERIIKFAFEYAKKNNRKKVSCIHKANVLRVTDGLFLEIFNEIKKKYKNFNIEADDYLVDA
TAMYLIKNPEMFDVIVTTNLFGDILSDEASGLIGGLGLAPSANIGDKKGLFEPVHGSAPDIAGKGIANPI
ATILSAAMMLDYLGMKEKGDLIREAVKKCLENGKVTPDLGGNLKTKEVTDKI
>gnl|CDD|468592 NF040620, fused_HadA_HadB, fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB
VGRHYRVDDYYEVGREKIREFARAVQDFHPAHWDEAAAAELGYDGLVAPPTFASIVGMLAQRALFETVLT
GYDLSQILQTDQVFEFHRPILAGDRLTCDVSLESFRQFAGGDLIVVKNVLTDQHGEVVQTGHTTLVARTG
AEVDPGIADAVEGVMMHGVGPDGRPAADPGPLEPLEAPVPPPGPARPRPPHTAIDFDDLAVGDELPPRTV
RLTRGDLVNYAGVSGDPNPIHWSDEVARLAGLPTVVAHGMLTMGLGAGYLTSWLGDPGAVTKYSVRFTSP
VYVPADAPAEIEFTGKVKSLDPETRTATIALTAKSGGRKIFGRATAEVQ
>gnl|CDD|468593 NF040621, Dietz_HadA, (3R)-hydroxyacyl-ACP dehydratase subunit HadA
MSTDNADDIEVVVDGDPVTVTPVVVARFAEVVGAPDGQVPHTLAAALTAPVQRAVMEHPRLRIDLARTLH
TAQRSEHHRPLEVGDVLTATATVTSVRSARGGRLITFVTVLRDPSGTTVQTLRSALLTAEVE
>gnl|CDD|468594 NF040622, MfnE [5-(aminomethyl)furan-3-yl]methyl phosphate kinase
MHLIKIGGSLTYNAKPLLNKLKSYANESEKKIIIIPGGGEFANVVRKLDEKTNLSNSGSHKLATKCMDLI
GEYFSEISGIKTYDNLFDAKKILKKENIVILLPSKIVLSTDELPHSWEVTSDSIALYIAKLLNLKEIIIA
TDVDGIYDKYPEGKLLNTINAKDIKGFTSVDKYLPKLLKKYNMECYVVNGKYPERIINILKGKNDICTKI
T
>gnl|CDD|468595 NF040623, MfnF, (4-{4-[2-(gamma-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine synthase
MILGIDIGGANTKITEIDNGKYKIHHIYFPMWKNNDKLTELLKNYSDNVDKVALVMTAELADCYETKKEG
VEDILNKVENAFDDKIYVFDVDGNFLTPEEAKKNYLKVSASNWTATAEFVSKFIDDNCILVDMGSTTTDI
IPIKDGKILAEKTDLDRLMNNELLYVGTLRTPLSFLTNKIEFRGKLTNVSSEYFAITADISIILGKITEE
DYTCDTPDGKGKDKESCLIRLSRVLCGDLEQISEEELIDIAKQFYNKLLELIRENVDKVAEKYGLKDVVI
TGLGEEILKDALKDYNIISIKERYGKDVSLATPSFAVAKLLKN
>gnl|CDD|468596 NF040624, HadA, (3R)-hydroxyacyl-ACP dehydratase subunit HadA
VGMHYRYPDYYEVGREKVREYARAVQNDHPAHHDEEAARELGYDGLVAPLTFISIIGIIAQRALFEEANV
GYDLSQIVQTDQRLKFHRPIVAGDRLTCDVYVDSFRQMAGTDIIVTKNIITDQDGEPVLTTYTTLVGRTG
EDGE
>gnl|CDD|468597 NF040625, HacB2_Meth, homoaconitase small subunit
MEIIKGKVWKFGDNIDTDVIIPGRYLRTFNPDDLASHVMEGERPDFTKNVQKGDIIVAGWNFGCGSSREQ
APVAIKHAGVSAIIAKSFARIFYRNAINIGLPVIVADIEADDGDILSIDLEKGIIKNKTTGEEFKIQPFK
EFMLEILEDGGLVNHYLKEKE
>gnl|CDD|468598 NF040626, AksF2_Meth, homoisocitrate dehydrogenase
MYKITVIPGDGIGKEVMEAALYVLDALDLNFDFIEAEAGRECFKKNGTTIPEETIKIAKKSDATLFGAVT
STPGQKSPIITLRKELDLYANLRPIKSYEGINCLFKDLDFLIVRENTEGLYSGLEEEYTEEKAIAERVIT
RKASERICKFAFEYAIKLGRKKVTAVHKANVLKKTDGIFKDTFYKVAKDYPQIETEDYYVDATAMYLITK
PQDFDVIVTTNLFGDILSDEAAGLVGGLGLAPSANIGDKNGLFEPVHGSAPDIAGKNIANPIAMILSASM
MLDYLGETYEANKLENALEKVLREGKVVTPDLGGNAKTMEMANEIKKKIEEL
>gnl|CDD|468599 NF040627, GFPS_Meth, geranylfarnesyl diphosphate synthase
MNIEEWEEYRYVESGISDFIAQMEDSSLKKMVEHVCNTGGKRIRPIILLLSSEICSGSYSQSLNAALAVE
MMHSASLIHDDLLDQGLVRRNLPSAPEKFGPSRALLCGDYLIAKSIEFISPYGEKVIRDFGKAGMDMAEG
EVLDLRLDDDNFGESDYFECIYKKTASLFAISASIGAYTGGADEALAERFNFFGNSLGTAYQIVDDILEF
LEVVEGKESKFTSETLPHVYMKNMSKEEAIEKSIDAVKLHVNAAKETLLTFRACPARDKLFQITDYITVD
MLENI
>gnl|CDD|468600 NF040628, GT-D_rel, GT-D fold domain. This HMM describes a domain related to the GT-D fold glycotransferase domain described in Pfam model PF08759. The two families share the strong motif R[VIL]GDGE, and full-length homology, but only about 16 percent identity overall. As characterized sequences included in PF08759 include glycosyltransferase proteins or domains, members of this family are proposed also to be glycosyltransferases and to share the GT-D fold of PF08759
LLNPAEVLDRIEQALDEGRPLSLVRLGDGENLVLAQDTVLSIEEVLQEGWALKANQGYKGVRLPNLAARD
ALAESIRKADIVGIPTIRAPDYRPLTFPVFRAYGIDPLRLTHATVNRELAQQGYFWRMLAGRRVLLVGNE
AAQLAEVLEQDPYGLQIAGALPVDGYEDIPRVLKEIARHDFDIALVSAGVNAVILAQRIAEELGKVAIDF
GHLANILIKGEAN
>gnl|CDD|468601 NF040629, PGI_Meth, glucose-6-phosphate isomerase
MLSYDYENALNVGEISLEDINKVDFTNAYSNLMEKLDNGVVGFRDVIYDENLDKYKSLNGYKNVVVVGMG
GSILGTMAIYYAISPFNNNAYFIDNSDPEKTLSILKKVDLNESIIYIISKSGNTLETLVNYYLIKKRIEK
LNSFKGKIVFITNGGKLKREAEKNNYEIYSIPENVPGRFSVFTAVGLAPLYSLGIDISKILEGAREMDKL
CQNEDILKNPALLNGVIHYLYDKKGKDISVIMSYIESLKYFGEWYKQLIGESLGKNGNGITPLLSIGAKD
QHSLLQLYMDGKKDKIITFITTKKYRLDEEIVFEDINDEEISCMLSDIIKCEQKATEIALTNNGVPNVRI
TLDEINEMTMGALLYMYEMQVGFMGELYNINAYNQPAVEEEKKICW
>gnl|CDD|468602 NF040631, InhA, NADH-dependent enoyl-ACP reductase InhA
GLLEGKTILVTGIITDASIAFHIAKVAQEQGAKVILTGFDRLRLIERIAKRLPQPPPLIELDVQNEEHLA
TLADRVREHAPEGIDGVVHSIGFAPRSCMGPPFLDAPWEDVAKAFEISAYSYAALAKAVLPVMNEGGSIV
GMDFDPRRAMPFYNWMGVAKAALESVNRYVAREVGAKGIRSNLVAAGPIKTLAAKAIAGTATGDGKQMDL
LNEGWDQRAPIGWDVDDPTPVAKTVCALLSDWLPATTGSIIYVDGG
>gnl|CDD|468603 NF040633, FadD32_Coryne, FadD32-like long-chain-fatty-acid--AMP ligase. Members of this family are found in the genus Corynebacterium, are most similar to the key mycolic acid biosynthesis protein FadD32 of any fatty acid--AMP ligase in Mycobacterium tuberculosis, and are likewise encoded next to Pks13. However, as the mycolic acids produced in Corynebacterium and in Mycobacterium differ substantially, it is not clear that assigning the same name in Corynebacterium is appropriate
MDLSAAMGQFFDEKGNITLPPQLTLAGLCEMLYQADLAAGGGDRVCIRFWDYSESREGTAVEYTRAEVNT
RIKAVAARLQQVGKPGDRVAILANNSPEYIFGFLGALYAGMVPVPLYDPNEPGHADHLRAVLADSGPTVV
LTNKTSAPAVRAHFADLPAAERPRILSVDSLPDSLAESWVNPMATIEGQPLLAPAGTDPSDDTAFLQYTS
GSTRTPAGVVLTNRSIVTNVLQIFTAAQLKTPLRLVSWLPLHHDMGIILAAFVTILGLEFELMSPRDFIQ
QPKRWVDQLSRREDDVNVYTVVPNFALELAARYANPEEGEDLDLSAVDGIIIGSEPVTEKAVDAFLDAFG
PYGLRRTALRPSYGLAEASLLVTTPQTEERPLFTYFDREALAEGRAVEVAEDSENAVPFASNGQVVRPQV
LAIVDPETGQELPDGTVGEIWVHGDNMAAGYLDREEETAETFRNTLGERLAENSRAEGAPEDNWMATGDL
GVIVDGELYITGRLKDLIVIAGRNHYPQDIEATVQEASDHIRPDSVAAFAVPGDDVEKLVILAERDDEAD
ESGDAEAIEAIRAAVTSAHGVVPADIRIVAPGEIARSSSGKIARRVNAKAYLE
>gnl|CDD|468604 NF040636, AcpM, meromycolate extension acyl carrier protein AcpM
TTQEEIVAGIAEIIEEVTGIEPSEVTIEKSFVDDLDIDSLSMVEIAVQLEDKYGVKIPDEDLASLRTVGD
AVAYVQKLEAENPELAAEIEAKF
>gnl|CDD|468605 NF040637, CatA_like_2, CatA-like O-acetyltransferase, family 2. Members of this family are homologs to members of the CatA family of chloramphenicol acetyltransferases, although less than 30% identical. There is no evidence that members of this family act on or confer resistance to chloramphenicol
REIDPKETNRAKAFELWMKAPMPMVTFFKTLDVTNLVKLSKKKGYKFNMLMCWCIGKAASDTKEFYLLPV
GDKLIQYDKIAVNTIVKNKNGEISSCDIPFSDDLEQFNRDYLRLTQQVRETCEDYDLEDSMVIGTSALVH
TEIDGAVNMYSGIFNNPFLIWGKYRKRLFKTTLPISFQFHHTQMDGAHAARFLENLQTEINRL
>gnl|CDD|468606 NF040638, CatA_like_3, CatA-like O-acetyltransferase, family 3. Members of this family are homologs to members of the CatA family of chloramphenicol acetyltransferases, although less than 35% identical. There is no evidence that members of this family act on or confer resistance to chloramphenicol
NYKVIDKEKYYRKGVFRHFTEDCKCSVSITARIDVTDLVEYSKKTGTKFYINFLYILSKVLNSREDYRMG
YLWQTDELICYDKINPTQYIFHEDTETCTPVYTEYFEDYEVFYKNALADIERAKETREYGLDSANHPNWF
DASYISWLSYDSLNLELPDGYLYFLPIVNWGKYREENGRLMMPVSVRLNHAIADGYLVANVFRLLEKEIA
YF
>gnl|CDD|468607 NF040639, LETM1_rel_film, LETM1-related biofilm-associated protein. This bacterial protein family is related to the mitochondrial protein LETM1. The founding member, WP_060382447 from the fish pathogen Flavobacterium columnare, called a calcium-binding EF hand protein, was found highly up-regulated in expression during biofilm formation
NPSASGWIKKFFHEVKDKYIFLYLDEEEFYEALRKTGFIYGSNVSVLLPIIIEHKLTEEEIAKINLLNAL
YFIYYLEKKNNDFEDFIESVIEFYKELNPHKSSFFKKLFLGKKTSSSKLEKIIDSRVQTNDNIISKNFSH
ILTNALLFIDVLAFERYLKGGTDPEKYAKNLEEIIINIVYLALNSKEEKTKYDELLIKLFESSLRYNDFS
KINFDGTYEELLLNYFTSLEKYYLLDLACMASWSDEVIEYEESDFLFELGEDLGLSDEFIEKSIEDVNVF
FEKNKDKIPYLKSSNPVKHFYDNSSKSVKKLISRNKKRLLKELSESKELMILLSKSTTRDLNDEEKKKVK
KQLLDIFKSIPSLAIFLLPGGALLLPILIKFIPKLLPSAFNENREE
>gnl|CDD|468608 NF040640, YcgZ_fam, regulatory protein YcgZ. YcgZ, as found in Escherichia coli, is a small protein of unknown function that appears to participate in regulatory cascades involved in processes such as biofilm formation and response to blue light. YcgZ is homologous to YmgB/AriR, a paralog also found in E. coli and described as having a role in regulatory cascades
MRQNGYNPDSASDIARYFSKASLPSQQETLGQIVVEILRAGKNLNRKAICSKLLRRLELASSPEEERHYQ
ELIGLLF
>gnl|CDD|468609 NF040641, bifunc_ST_SDO, bifunctional sulfur transferase/dioxygenase Blh
VRINDRLSVSGQPDAEDFASLAAQGFTAVINNRPDGEEPGQPGNAAERAAARQAGLSYSFIPVTGDTITE
ADVRAFQKALAAAKGPVLAHCKSGTRSLTLYALGEVLDGRMKAEDVRAFGQQHGFDLSAAVAWLARRAAR
RPQVKGFFDPRTGSVQYVVSDPATRRCAIIDPVLDFDEKSGATSTTNADAILAYVAEEGLTVEWILDTHP
HADHFSAAHYLKEKTGAPTAIGEHVVDVQKLWKGIYNWPDLPTDGSQWDRLFADGDTFKVGSIDARVMFS
PGHTLASITYVIGDAAFVHDTLFMPDSGTARADFPGGSARALWRSIQAILALPDETRLFTGHDYQPGGRA
PRWESTVAEQKRSNPHLAGQDEASFVALREARDKTLPMPKLILHALQVNIRGGRLPEPEANGRRYLKIPL
DAL
>gnl|CDD|468610 NF040642, sulf_sens_BigR, sulfite-sensing transcriptional repressor BigR. BigR (biofilm growth-associated repressor) is a winged-helix DNA-binding protein active as a transcriptional regulator for Blh, a bifunctional sulfur transferase/dioxygenase found in a number of plant-associated bacteria. Oxidative conditions that allow disulfide bond formation between the invariant residues Cys42 and Cys108 cause BigR to lose DNA-binding transcriptional repressor activity
AEMEARAGEVADLLKTLAHPARLMLVCTLVEGEYSVGELEEKLDIHQPTLSQQLTVLREAGIVETRREGK
QIFYRLTEEKAAQLVGALYTIFCAK
>gnl|CDD|468611 NF040643, S6_alt_immun, pyocin S6 family toxin immunity protein. All members of the seed alignment for this family are found in the genus Pseudomonas, always adjacent or close to proteins with the killing domain (see PF09000) of 16S rRNA-cleaving colicin E3 and pyocin S6 family toxins. This family is unrelated to that of PF03513, a well-characterized family of immunity protein for ribosome inactivating toxins in the family of colicin E3, pyocin S6, but is called an immunity protein for the same family of toxins by Dingemans, et al., (2016) in pyocin S6-encoding strain P. aeruginosa CF_PA39. In most strains with a toxin from family PF09000, an immunity protein is found either from this family, or from PF03513, but only occasionally from both
YLCITGFLPDDNEDDSLKYELDVPPEFEQAVLEVLGWKSLEEEPDGEWLLTDEQVRQIAELLGEPLPTDL
DLFIGVRA
>gnl|CDD|468612 NF040645, K_channel_Meth, hyperpolarization-activated voltage-gated potassium channel
MNLKSPKFYKIIEILSLIFTLEIIISFILSTYNPPYQDLLIKLDYISISFFTFEFIYNFYYSKDKAKFFK
DIYNIIDAIVIIAFLLYSLEIFYSKAIVGLRIINLVRILVLLRIIKLKKLEENPELINFLTILTICFISS
CFIWVVESEVNPAINNFFDAFYFTVISITTVGYGDITPKTDAGKLIIVFSVLYFISGLITSLQ
>gnl|CDD|468613 NF040646, HPT_Archaea, hypoxanthine/guanine phosphoribosyltransferase
MLEKLKESLKNAPVVKRGEYNYFIHPITDGVPLVEPELLREIADRIIKIADLDVDKIVTVEAMGIPIATA
LSLKTDIPLVIIRKRKYGLPGEVEVHQSTGYSKGELYINGINKGDRVLIVDDVISTGGTLIAVIKALEKA
GAEIKDVVVVIERGEGKKIVEEKTGYKVKTLVKIDVVDGKVVIL
>gnl|CDD|468614 NF040647, IPPK_Arch, isopentenyl phosphate kinase
IILKLGGSVITDKDIYPKIDWDNLERIAKEISNALDEDKLIIVHGGGSFGHPKAKKYGIGEGINGEEFER
KRKGFWETQNAMRRLNNLVCDALIEYGIPAVSIQPSSFIRTGNKRILHFDLDLIKKYLELGFVPVLYGDV
VLDNNIKYGILSGDQIIPYLAKKLKPDRVILGSDVDGVYDKNPKKYPDAKLIDKVNSLDDLESLEGTNNV
DVTGGMYGKVKELLKLAELGIESYIINGNKPENIYKALGGEKVIGTVI
>gnl|CDD|468615 NF040648, lactal_redase_Meth, lactaldehyde dehydrogenase
MFINGKWIDREDIDVINPYNLEVIDKIPSLSREEVKEAIEIANEAKEVMKNLSPRKRYNILMDIAEELKK
NKEELAKLITIDAGKPIKQSIIEVDRSIETFKLAAFYAKEIRGETIPSDAGLIFTKKEPLGVVGAITPFN
YPLNLAAHKIAPAIATGNSVVLHPSSKAPLAAIELAKIIEKVLKKMNIPLGVFNLVTGYGEVVGDEIVKN
EKVNKISFTGSVEVGESISKKAGMKKITLELGGNNPLIVLKDADIEKAVESAVKGSFLNSGQVCISVGRV
IVEEEIADEFIKKLVEETKKLKVGNPLDEKTDIGPLITEEAAIRVENLVNEAIEEGAKLLCGGNREGSLF
YPTVLDVDEDNILVKVETFGPVLPIIRVKDIDEAIEIANNTKYGLQAGVFTNDINKALKFADELEYGGVI
INKSSTFRTDNMPFGGFKKSGLGKEGIKYAVEEMTEIKTIVIN
>gnl|CDD|468616 NF040649, FucA_Meth, L-fuculose phosphate aldolase
MDLKEFIKICHLLYDRKYVVGSGGNVSIREDDLIYITPTGSILGFLKEEDIAIVDLDGNIIKGKPTSELN
MHLKIYRKRKDINAIIHTHSLYSTALSILDKKIELLTPEAKIFLKKIGYVDYLEAGSLELAEEVSKRDED
VIILKNHGIVCLGKDLIEAYIKTEVLEEIAKLNLIVLLL
>gnl|CDD|468617 NF040650, sulfolac_dhydr, L-sulfolactate dehydrogenase
MKITPENEKKLIIDILKKYGVSEEDAEIVADVTVDADLKGFTSHGIGRFPQYIKGIEAGNINPNGDIKIE
KETPATALINGNHGFGQVVAYKAMELAIEKAKNTGIGAVGTHNSNHFGVTGYYSDMAMKEDMIGIVIANT
EPAVAPLGGKEPILGTNPIAIGIPSNKTYISLDMATSASARGKLLEAKRKGEKIPENVALDKDGNPTTDP
EEALEGSILPFGGHKGYALAFMIEILAGPLVGAAFGTGVKGTANPEEKCTKGDLFIAIDPSKFVDKEEFK
EKVDEFVEEIKNSGPNVLIPGDIEVKNIKKNKKEGIEIDEKLYEQLKEICDKLDLDIED
>gnl|CDD|468618 NF040651, MtaB_Meth, methanol--corrinoid protein co-methyltransferase MtaB. MtaABC catalyze the formation of methyl-coenzyme M from methanol and coenzyme M. MtaB methylates the corrinoid protein MtaC
VKRYTKMAYDSADEMVFGEAKFPVKAGLGLEIGAGYVTPEINYAPRPGAEESKEKLVKEYERITTDIMER
AVQIGFPAVVLETEHVQQMTNNPDWGAEVAHAQKEIMEEYHDEYGIKCALRHTPADIREEEDGLRLRGDK
YSKLMESFEACAENGADLLSIESMGGKEVSDYAILRNDIRGILFGIGVLGSIDMEYMWQDIVDIAKKNGV
IAGGDTDCAQANTAMFIAGGLLDKNLAHTLAAIARAISAARSLVAYECGATGPGKDCGYENPIVKAIAGV
PIAQEGKNSTCAHSDLMGNLIAQCCDLWSNESVEYHGEFGGTTVQCWLEALGYDCALMNTALETGNEKIL
RDLYTLSDKYRDPQGYILAYDNAYRIGEAIVKNGDDIYLRAKAAALEACEIINEAVKGKKLQLTRFERDA
LDKAKKDLEALPDDEDKFMDECLKKYKREVKVFKPKNYGL
>gnl|CDD|468619 NF040652, Mbox_reg_Rv1535, Rv1535 family protein. Members of this family include Rv1535 from Mycobacterium tuberculosis, regulated in response to changes in Mg(2+) leves and encoded immediately downstream from an Mbox Mg(2+)-sensing riboswitch
MTAVLYDEVVTVAPAPRLTVVRDTTPAPAPKKAARRRDRPPFGAGDPLVDGAARLLSIPLRHVYAALWRV
GVLEVRA
>gnl|CDD|468620 NF040653, Rv1535_dom, Rv1535 domain. This HMM describes a domain found in the C-terminal region of Rv1535 from Mycobacterium tuberculosis, a protein whose expression is regulated by a Mg(2+)-sensing riboswitch, and as nearly the entire length of proteins of about half the size (about 40 amino acids in length) from other Actinobacterial lineages such as Nocardia
DPLVDGAARLLSIPLRHLYAALWRVGVLEVR
>gnl|CDD|468621 NF040654, MtaA_Meth, methylcobamide:CoM methyltransferase MtaA. MtaABC catalyze the formation of methyl-coenzyme M from methanol and coenzyme M. MtaA transfers the methyl group from methylated MtaC
MNLKERFLNALKGKEVDKVPVCSVTQTGTVELMEATGAFWPEAHSDAEKMATLAIAGHEIAGLEAVRYPF
CLTVLAEALGCEVNEGTKDRQPSVTDHPFKDVDDLEVPDDLLERGRIPTVLEATEILKEKVGDDVPIIAG
MEGPATLASHLLGVKNYLKWSITKPEIVEELLDIATDACIEYANALFEAGADAVCVADPVAGPDLLDPLD
FESLVKPRYEKFAEKIKGPKILHICGDATPILDDMADCGFEGISIEEKVDLKYAKEIIGDRACLIGNVST
SFTLLSGSPEEVKEEAKKCLEDGVDILAPGCGIAPRTPLENIKALVEARDEYYK
>gnl|CDD|468622 NF040655, MtaC_Meth, methanol--corrinoid protein MtaC. MtaABC catalyze the formation of methyl-coenzyme M from methanol and coenzyme M. MtaC is methylated by MtaB and provides the methyl group that is transfered to coenzyme M by MtaA
LDIDPSDILVRYNVKLEKEMTPEEAAEELYPKDELIRPIAEAIFEGDEDDVIEGLQKAIDAGKDPISLID
DALMVGMGIVSKLYDDGVIFLPDVMISADAMLDGIEYCKEKSGETPETKGKVVCHVAEGDVHDIGKNIVT
ALLRANGYEVVDLGRDVPVDEVIAAVKKEKPIMLTGTALMTTTMYAFKEVNDRLLENGIKIPFVCGGGAV
NQDFVSQYELGVYGEEAADAPKIADAILKGAGIEKLREKFHKH
>gnl|CDD|468623 NF040656, GHMP_GYDIA, GYDIA family GHMP kinase. The GHMP kinase family is named for galactokinase (G), homoserine kinase (H), mevalonate kinase (M), and phosphomevalonate kinase (P). This uncharacterized protein family, most closely related to mevalonate kinase (see TIGR00549), has several distinctive nearly invariant motifs, including WGLG[ST]SSTL, GGSGYDIA (for which the family is named), and SLGAWGGF
TFYSNGKLLLTGEYLVLDGAKALALPTKFGQSLEVEEIEDQQITWKSYDEDGSIWFEATFDLDNLEIKET
NDEEIAETLLKILREAQKLNPDFLKSNKGYEVETKLEFPRDWGLGSSSTLINNIAQWAEIDPYELLENSF
GGSGYDIACAQNNSPILYQLKNGKPKVEPVNFNPPFKDQLYFVYLNQKQNSREAIAHYRKNKKSKAKLIE
KISEITEEILLCKSLEEFEKLIEEHEQIISSILGIPTVKEKLFPDFPGAIKSLGAWGGDFVLATGKEDPK
EYFKEKGYETIIPYSEMI
>gnl|CDD|468624 NF040657, immun_SitI3, SitI3 family protein. The founding member of this protein family, SitI3 from Myxococcus xanthus (WP_020478554.1), is an immunity protein encoded immediately downstream of a lipoprotein toxin, SitA3, that can move between cells by means of a transfer system for exchange of outer membrane lipoproteins involved in kin recognition. It is not yet clear what fraction of the members of this family are immunity proteins from other toxin/immunity-type conflict systems
IEYSLYLATDLSPEEVAALLADALGEEPLLELLSADLLDGLGVGVDVVTGRGGYVRVEDDDEEPFEWEGF
DPTVSVTFRLDKDADDEAQAADNMLLVVALLLLVEGEDAVLLFNGETVLLLRRGGELVLNDRDDWWTPER
>gnl|CDD|468625 NF040658, Myxo_OME_TraC, outer membrane exchange accessory lipoprotein TraC. This lipoprotein family, found Myxococcus xanthus and other members of the Myxococcocales branch of the Deltaproteobacteria, is involved in a kinship recognition-dependent system for exchange of outer membrane lipoproteins. TraC is described as an accessory protein to the TraAB pair that was shown to be critical to outer membrane exchange
RARPARPPSPLSLRRPLAALALAALLAASGCTAFSRAVKEGDGATAQRKWAEAEAAYLRALAADPGDSEV
KVKLRAVRKEWSAEVLAEAEAVHAEGDLPGATKLLVRALELDPENAEARALLTQTLDARVAVGQKALKEE
RLQEARAEFDAVLAVAPDHVAARKGVDAVQVAWARRWFGTAQRLEERGKLGNALLAYVRADQERVGATAA
RERAEAVRQKLRDEVAFLVVATPVEDKAEAPDVAQRLSAGRLAAMLPTELPIRVVTEAPEGREGVRLGLA
LERVLPLKTVEQSQRSQRYLAGNRSVPNPRRAQFETKLLQAERTLEEVERKQAAALREYLRKQAELATVR
EAAERCRERERRECREALQECGEAAREAEKPGQVPAECNPARCAPGQCDQEERLLAQRAAAVKQLERRLE
AALEKAEDQRREVQRGRDAVYREPLTVEEPMYSDFVYDVELHRLTVTATVTAVLRDLLKDQAVPAPRTQD
YAVTHEDSAHKGYDRYGVLADPVQLRSELELRVEVGDKAVTDLARRVKERFDAYRQKRVEDARRGMVRPG
AEDVVETAVRALLLTADAPPADILQPLARARGLTRPEALLGR
>gnl|CDD|468626 NF040660, mycolic_MTase, cyclopropane mycolic acid synthase family methyltransferase. Members of this family include tailoring enzymes that make site-specific modifications to mycolic acid precursor molecules. These include Mycobacterium tuberculosis enzymes MmaA1-MmaA4, CmaA1-CmaA2, and PcaA. The family also includes UmaA, reported to be the lone member of this family not involved in mycolic acid biosynthesis. No members of this family are found in species that lack mycolic acids. This model excludes two more distantly related paralogs, Rv0447c (UfaA1) and Rv3720, that are also encoded in the Mycobacterium tuberculosis H37Rv genome
LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCG
WGATMRRAVEKYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGH
ERYDDFFKRAYNILPADGRMLLHTITGLHRKEMHERGLPLTMELARFIKFIVTEIFPGGRLPSIEMVVEH
AEKAGFTVTRVQSLQPHYARTLDLWADALQAHKDEAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFT
LAK
>gnl|CDD|468627 NF040661, Osc7112_2153fam, Osc7112_2153 family protein. This rare, small cyanobacterial protein, about 80 amino acids in length, has a signal peptide and a pair of invariant Cys residues that suggest disulfide bond formation. The protein regularly is found encoded just a few genes away from exosortase O (XrtO), but the significance of that finding is unclear
MKRTVLISSTILAIITVLELSQASKALPTPATVKPTVNNSVETLFNSNQSMRRCRDKDGGKYPCPRFVMP
QESAE
>gnl|CDD|468628 NF040662, attach_TipJ_rel, host specificity factor TipJ family phage tail protein. Members of this family form a family related to that of host specificity protein J of phage lambda, a tail tip protein that mediates attachment to LamB on the surface of E. coli. Binding of the phage tail to the LamB receptor triggers the injection of phage DNA into host cells. Proteins with this domain are likely also to be phage tail proteins
AGEEATQLELDFSFPNGLYYSVSVEVEYRKVDDNGVPGGAWTSLYGVGTAATRDTLGRTRRIKLPPPGRG
EVRVRRRRTRDNNSNSRARDEVKWYGLRAYLPRSPTVYPNVTLLAVRVRATDNLSSQSERKLNCIATRKL
PVYNGGGGWSDPTPTRSIAFALADLARDPVIGRGLPDEIDLDTLYALDDEVWTGRGDEFDYTFDDESVSF
EEALQMIANAGRAEPYRDGGLLSFVRDEPRTVPGALFNPRNIVPDSFKRSYTMPVEDDYDGVEVEYVDPD
TWKKETVRCRLPGSAGRNPKKIELDGIRNRDQAWRRAMREARKLRYQRRSVSFTTELDGLLVNYGDRVAV
ADDIPGWTQSGEVTARDGLTLTTSEPLDWSDGQSYVIVLRRPDGSVDGPLATPGEDDYDVFLARIPLIDL
VIDGDTDVQTEPTYFIFGDSERWAQRFLVTSIKPSGDGTVELTAVNYDDRVYA
>gnl|CDD|468629 NF040663, salivaricin_M, salivaricin M family lantibiotic. Members of this family are type A2 lantibiotic precursors in the family of founding members EGX30806.1, called salivaricin M, from Streptococcus salivarius strain M18 (previously strain Mia), a commensal strain of the oral microbiome, and ALO23661.1, called salivaricin E. Salivaricin M affects the caries-causing oral pathogen Streptococcus mutans
KKENNEIDSLDFEINNQELEGKSGAGWFTAIQLTLAGRCGRWFTGSYECTSNNVSCG
>gnl|CDD|468630 NF040664, HEC_x9_TCC_lant, lacticin 481 family lantibiotic. The lacticin 481 group exert their antimicrobial action by disrupting the cytoplasmic membrane. This model contains a lipid II-binding motif. The docking of the lantibiotic with lipid II is part of the mechanism by which family members form a membrane-disrupting structure. The lacticin 481 group includes lacticin 481, mutacin H-29B, variacin, nukacin ISK-1, butyrivibriocin OR79A, streptococcin A-FF2, ruminococcin A, mutacin II, and salivaricin A
QEVSDEELDQILGAGGNGVIKTISHECHMNSWQFLFTCC
>gnl|CDD|468631 NF040665, relax_SAG1250, SAG1250 family conjugative relaxase
MVITKHFATHGKKYRRRLIKYILNPEKTDNLKLVSDFGMSNYLDFPSYEEMVEMYQANFLNNDTLYDSRN
DRQEKKQQKIHAHHLIQSFSPEDNLTPEEINRIGYETIKELTGGNFRFIVATHTDQDHVHNHILINSVDL
NSDKKLKWDYALERNLRMISDRISKVAGAKIIENRYSHRDYEVYRKSNHKFELKQRLYFLMEHSKDFEDF
LKKAEQLHVEIDFSRKHSRFLMTDRDMKQVIRGRQLNKRQPYDEEYFRTYFAKREIESRLEFLLPRVNSL
EELLEKAKELNLTISLKQKNVTFTLEENGQKISLNHKKVSDKKLYDVQFFQDYFKEREVTDIEETENLQE
DFEIFKEEQEKEKLSVEEIEEAYEEFKEKRDAVHEFEVELADHQIEKLVDDGIFIKVSFGIKQEGLIFIP
NYQLDILEEENKKKYKVFIRETSSYFIYNKEASDKNRYMKGRTLIRQLTNDSQTIPYRRRPTVDSLQEKI
AEINLLIELNVTNKSYQEIKDELVREIAQLDLRLTELQEKIATLNKMAEVLLNLKSDDVESRKLARYDFS
KLNLTENITLEQVEKEIEALQNQLDKYIDEYEKLVRRLEKFVKVLN
>gnl|CDD|468632 NF040666, Tn5252_Orf10, SAG1252 family conjugative relaxosome accessory protein. SAG1252, a member of the Tn5252 ORF10 family, occurs in mobile elements from a class associated with the movement of bacteriocins and antibiotic resistance proteins in Streptococcus. This HMM excludes related MobC proteins, such as the adjacent SAG1251, a homolog over the short length of these small proteins except for a small central region recognized by Pfam model PF05713 (MobC)
YRDIRKEFNLTAEEEEQIQELMKEQGYEQFSPFLRQKLLKLDEQKQSLEEWFSLWQSQKLEQISRDVHEV
LVLAESNHQVTQEHVSILLTCVQELIAEVENTIPLSQDFRDKYM
>gnl|CDD|468633 NF040667, hom_kin_desulfo, homoserine kinase, Desulfovibrio type
PCISLIGMAGAGKSTVGRALARRLGWAHVDTDHLIEAYYGRPLQDITDALGKEAFLDAEEEVVSSLGLRR
TVISTGGSVVYREAAMEHLKSLGPVVYLDVSLETILERVARNPDRGLAIAPGQTLEDLYNERQPLYERYA
DFTVDTDALSPEECAEAILDWLP
>gnl|CDD|468634 NF040668, regulator_TseB, cell wall elongation/penicillin-binding protein regulator TseB
MGKKTLIFTLIFGIIFLTAILAGANIYQTAMAQKEEGHEAAAETAKKKADLKQVDQVETFVGKEKQYIVE
GKNKKGEKMYVWVPADKKQKTISKKAADGITSRQAAKAVQDEGLVSKLKEVHLAREGNVLLWEVTYLNKD
GQYSLSYVDFTNGKIHKNITP
>gnl|CDD|468635 NF040669, MtaC2_Meth, methanol--corrinoid protein MtaC
EELESKMDQDFIAIRYNVKIEGPAIKPEEDPEVQEILPQEEPFRSIALAVLYGDKEECLDNVQKALDSGE
SPIDIINNGLMKGMDAVSALYTKGFYFLPDLMLAGDAMMEGVKLCEKVLGHKSETKGTVVSFAAEGDPHD
IGKNLIVMFLRANGYDAIDLGRDVPTEDVVKAVKEYNPIFMTGTALMTTTMTAFPKVVAALQEEGIDVPA
IGCGGGAVRKDFVESFPMTVYGVEAYHVPKLADAILKDGKTWEDIRKEYSEIVGEFV
>gnl|CDD|468636 NF040670, wall_bind_EntA, cell wall-binding protein EntA. This HMM describes the cell wall-binding protein EntA, as found in Bacillus cereus. EntA is related to EntB, EntC, and EndD, but it lacks the central region of KAXEXX repeats that EntB and EndC have. EntD also lacks those repeats. Ent proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain
MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGHKLDVLNTENGWSQIKLD
GKDAFVSAEFTKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPF
LTGTAPVIEKQETPAPAKAEAPAKAQAPAQAKPAAKPAVKAAETSEPSGGRELTVVATAYTAHPSENGGT
YGGRVLTAMGHDLTANPNMKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSDSAAQKW
GRKTVKVKILK
>gnl|CDD|468637 NF040671, PLuB_AAA, PLuB system helicase-like protein. The PLuB system is found in the genera Persicimonas, Lujinxingia, and Bradymonas, all members of the Deltaproteobacteria. This protein, with an AAA+ domain, shows strong local homology to various helicases. The system also includes a CPBP family intramembrane metalloprotease and a PQQ-binding-like beta-propeller repeat protein
PENLADQPPRYEAPTGPVWLMDGAAIRGDSERDEEGEYLVRRLPASGSMLRVSPALRHAARADHPGLWGP
SYWWLHDNALWLAAPYPGGELLANAALERLSWSAALELWRPLAEALKRLHRRGLVHGALGPWRVWYDPTT
GRLSAVGAGCWIGLDFAALGGPHAEWIAPELRCPRNVRSPSPATDIYGLARLLLRLTLPPRQATAARPNF
TGIPAFAIPALERALSPDPARRPQRVAELLAALRPRTFEGDAPPDAGDSEDTPATTVSILHARVSDIEHL
EHPKQGPGIKFYLDHGDEGSVGAFFYAKQHPEVFNSVKWVWEGCELNLLDARVITNSAGETFLTAQANTL
PVLEPHMPMSVSDVLKAEGCPSRFLVDQRDRGDSSRPLVFGNLVHGLLDDLVEPEPPSFEAALESRVPEL
RLDMLAAGLDDADLASLEVDARQHFDNIRRFTAPRTASSPGADRVGWSGRNVEVTRYSTRYGIEGRVDLV
VEDPREGLQIIELKSGKPWDGHISQVRFYAFLWEGLAEERSLPITGHLLYSRDGTMRAAPMNDTDRERRI
LRARNELIACLRSFVDPAYAYDVPYFMQEPRACRSGTCRFRRDRCKAQTELLGLAHRQQPQPDYGVFAWP
STDPELVRRAWAWHAHFSRLIEMERWAATAALGAVLHPQRLSERKENYLASDNLHLVPVEGEPGRARFRG
ENLQIFSPGDYLLAHRGDFDTSHILRGRVVSVDDDQITLRLRGAHIAEELSGDGWILDLLPARLGFRQAH
HALYRVLREQSRDLLEVLFRPTTPAAQNLMRGQDATPNLHPATAALNPSQRNAVEHALCAPGGALIQGPP
GTGKTTVIAHAVRELVARGKRVLLSAFTNTAVDTILIKLLEAGHDDFVRVGSAAKSPDLARALQESGRNP
DHYFTDDLAHAHTSLDLLAEDLLRATVIASTAHRCARSPLMAFLERQRGDYPFDVAIVDEAGQITEPMTL
APISLGHRFVLVGDHRQLPPIVENEQAHSNFITADHSPFKLNDDLEQAGCAGLDRSLFERLISGLPYVML
DEQYRMHAPIMSFSNEAFYDNKLRAHPSVEDRHLAFDTLAATPRVDLTHPLLAPDEPLAFLDVRGTEDTK
RHNARHNLKEAEAVVETVSALLEDRAPPLSIGVVSPFRAQVHLLRTLLADRTLPEAGSIDVDTVERFQGS
ERDVILVSLVKTERAGDFLADERRLNVTLTRARRKLIVFGSSACLLLNPLYRPLIEQPHTTWVTWT
>gnl|CDD|468638 NF040672, SCO2322_fam, SCO2322 family protein
AQAAGYRYWSFWQRDGGAWAYATQGPATARPADGAVEGFRFAVSEDSADAPRPRGAADFAAICGGTPAKD
GTKRVALVLDFGTPADAPSGETPPKPRTACAQVPEDATAAEALAAVAKPLRYDSSALLCAIAGYPRTGCG
EQVS
>gnl|CDD|468639 NF040673, PLuB_PQQ_rpt, PLuB system PQQ-binding repeat protein. Members of this family contain a region similar to the PQQ-binding repeats domain (see PF13360), and occur in a conserved gene neighborhood together with a helicase-like protein and a CPBP family intramembrane protease. This system, designated PLuB, is found in the genera Persicimonas, Lujinxingia, and Bradymonas, all members of the Deltaproteobacteria
ALLLLAALLLSACDAQKDARDESAPQAPEPAAPLKMLAWSPPEAIDLRRPEPLPQRTLKLGPSQKFPRCH
ELFEPDGRPISAWPLRDDPQRALALAGCEPEAAERLEDGRRYVAYAVPRPPDSPASDLRLVAYNPDGELL
WHRRLDRSRQADNFTANFRGSFIARLLQRLVCAGTLWQGGTQAACVDAESGEVIWSGIMPFWSGIAPQGV
GNSLVGADLNGLTRRYPYSGVEMRHRAFDARGGRSAFYASDSTHLFFVPARAEEPRLSAYDLDTFEPDWR
LPLPARPQPNWGTVFEALNLLVFKIDDTLYALSTETGEQLWALEVGPDNPPVAAFEGGLYLLLRREDRPN
LLYALDPQDGKVNWAAEVPTGTLALGTDEDTLLLRSVRAVQEV
>gnl|CDD|468640 NF040674, PLuB_CAAX, MrtP family glutamic-type intramembrane protease
REVLLVYLLALVLTALLSLLAGAIPFVAQNLLALVAAVFLYLPALVLRRRGLDPADFGLHTRPWLRGLAW
GLLVALLTLPLFLLGYHLWQTQVLGREFRPSLSNLRRWPEELEGRPPSSGPPDGGVVWVWGRDLTLFWAW
WRPAPGELVLTARLGSPGGRPLGRGVATGRPRTEQRTWDIGLLGRGARAGLVALRPGGTRVRVRLTRDGE
PLPASRLRLGGDAAPPADDGPLTVSRSLWWLLLLLLTQLLLVALPEEFFYRGYLQTRLDQLLPRRRRLLG
ALVGWGANLLTSALFALGHVLIGPGPARLAVFFPSLLFGWLRERTGGIAAPVVFHALCNLLVQLLSRHYF
>gnl|CDD|468641 NF040675, wall_bind_EntD, cell wall-binding protein EntD. This HMM describes the cell wall-binding protein EntD, as found in Bacillus cereus. EntD, like its close homolog EntA, is related to EntB and EntC, but lacks the central region of KAXEXX repeats that EntB and EndC share. Ent proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. They may play a role in maintenance of cell wall structure and stress responses that support virulence, and probably lack any direct role as enterotoxins
MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKLD
GKEAFVSAEFTKSTYYVTANVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKAAYVHVPF
LTGTAPVIEKKEVVTQEEAPARVNTSVKNNTAVKSKESVKNVESSKPVAKEKPAAKPVAKSTETSAPAGG
REITVEATAYTANPSENGTYGGRVLTAMGHDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGA
IKGNRIDVLVGSDGSANSWGRKSVKVKVIK
>gnl|CDD|468642 NF040676, wall_bind_EntB, cell wall-binding protein EntB. This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity
MKKVIGAATATVFGLGAFTTTATAETIVTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIELN
GKEVFVSSEFTKDVYHVTANLLNVRTEANTESEILGRLKKDDVIESTHQVKDGWLQFEYKGKTAYANVSF
LSSTAPTEKKADEKTKQVAKVQKSVKAKEEAKTQKVAKAKETTKAQEIVKPKEEVKVQEVVKPKEEPKVQ
EIVKPKEEVKVQEEVKPKEEEKVQEIVKPKEEAKVQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAK
AQEIAKAKEEAKAQEIAKAKEEEKAQEIAKAKEEAKAREIAKAKEEEKAREIAKAKEEAKAREIAKAKEE
AKAREIAKAKEEERAKEASKNNIQSAKRELTVVATAYTADPSENGTYGGRVLTAMGHDLTANPNMRIIAV
DPKVIPLGSKVWVEGYGEAIAGDTGSAIKGNRIDVLMGSKSKAMNWGRQTVKVKIL
>gnl|CDD|468643 NF040677, wall_bind_EntC, cell wall-binding protein EntC. This HMM describes the cell wall-binding protein EntC, as found in Bacillus cereus. EntC is related to EntA, EntB, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity
MKKFMGIATAAVFGLGIFTTSAKAETIVTTDVLNVRENPTTESKVVGKLLDGYKVNVLHTENGWSKVKLN
SGKEAFISADYTKDTYYVTANVLNVRAGANTDSEILGKLKKDDVIETTHQVQNDWIQFEYNGKTAYVHVP
YLTGKAPVKVQPVVKVEKTTKVQDTAKVREAVKAGEVAETQAKAKAQEATKAREAAEAQAEAKAQEAAKA
REAAKAQEEAKAQAAAEAQAEAKAQEAAKAREAAKAQAAAEAQAAAKAQEAAKAREAAKAQAAAEAREAA
KAQEAAEAREAAKAQEAAKAQKPATQQPVAKETETSAPSSSRELRVVATAYTADPLENGYKAGDQVKSAL
GHNLTANPNMKLIAVDPSVIPLGSKVWVEGYGVAIAGDTGGAIKGNKIDVLMPDKGTSSNWGRKTVTVKV
LN
>gnl|CDD|468644 NF040679, halocin_of_epi, halocin C8 precursor-like protein. Members of this family are bacterial (mostly staphylococcal) homologs of the archaeal bacteriocin halocin C8 precursor. Members average about 245 amino acids in length, with the 76 amino acid Cys-rich mature peptide region at the C-terminus. Cutoff scores are set fairly high because this HMM is designed to identify full-length members of the family such as WP_002493350.1 from Staphylococcus epidermidis
KKLFVALLSITVLFSLCVPSIFASVEAALNENTLVEKPTSNVSSKTKQKIINKVKKSDAYKNHAKSTSIN
SIKDDNIIVHLDKGDNTNVYSVNFIFGKELAKQNDNLAMVEFKYNEANKEVFYDHMMFSKFVDDDNINMK
GVLNGKPYYEFNIDPEGVYYDLNFKETSKEEIEDNSQKNIPPKERSWCEWAVGALCGTGGAGGCYAAAGA
LGITTGWGGLGLAAICALILSLGCTGATNYICK
>gnl|CDD|468645 NF040680, chromo_anti, enediyne antibiotic chromoprotein. Members of this family are the apoprotein polypeptides of chromophore-containing antibiotics such as neocarzinostatin and actinoxanthin, interesting in part for the roles as anticancer therapeutics
GAAAAAALGLALAAQPPASAAAPSVTVTPSTGLSDGQTVTVSGTGFTAGATVHVGQCAEVVAGVLACDAA
TAVTVTADASGAASTSLTVRKTFTGVDGADGTPWGTVDCATVQCQVGAGNDAGEGGGVPISFG
>gnl|CDD|468646 NF040681, GPS-CTERM, GPS-CTERM domain. The GPS-CTERM domain, defined by this HMM, is found in Actinobacteria such as Nocardia and Streptomyces, at the C-terminus of at least to otherwise unrelated protein families. It is an apparent novel protein-sorting domain
DGGPSTGLWAGTAAVLVLGAAAVWQARRRR
>gnl|CDD|468647 NF040682, PorA_Arch, pyruvate synthase subunit PorA
CERKVITGNEAVAEAAKLAKPKVIAAYPITPQTTIVEKLAEFVADGELDAEYIKVESEHSAMSACVGASA
AGARTFTATSSQGLALMHEILFIAAGMRLPIVMAVANRALSAPINIWNDHQDSIAQRDTGWIQLYAEDNQ
EALDLILLAYKVAEDEDVLLPVMVCLDGFILTHTVEPVEIPKQELVDEFLGEYEPKHAYLDPERPITQGT
LADPDYYMEARYQVEEAMERAKKVIEEAAKEFEEKFGRKYGLIEEYRLEDAEIVLVAMGSVCGTLKDVID
ELREEGYKVGLLKIRVFRPFPKEEIKELLKNAKNVAVLDKNISIGLNGALYTEVKSALYNKKERPLVVGY
IVGLGGRDITPEHIDKIIEDAEKAEKIEDETNWIGLKE
>gnl|CDD|468648 NF040683, PorC_Meth_Thtga, pyruvate synthase subunit PorC
MIEIRFHGRGGQGAVTAAEILAKAAFEDGKYSQAFPFFGVERRGAPVMAFTRINDEPIRLRSQVYNPDYV
VVQDETLLEVVDVVSGLKEDGIVLVNTVKDKTGFNAKIHTIDATGIALDELGRPIVNTVMLGAFAGVTGI
VSIESIIKAIKETFPGKVGEKNAEAARRAYEEIKKSE
>gnl|CDD|468649 NF040684, PorD_Arch, pyruvate synthase subunit PorD
METIGAIVYKPGSTRKNKTGSWRTFRPILDKEKCIDCDNCYIFCPEGAIIQEENGMFEIDYDYCKGCGIC
ANECPVKAIEMVREE
>gnl|CDD|468650 NF040685, conju_mem_TcpD, conjugal transfer membrane protein TcpD
MKNLKNVKEKVVNKVKQYKARIEVFFVTLLALFGTSTYAYASINGEAIKNNVINNILLPFCFVVICFLLI
KELLKKNVAGIVIVLIVGGFVLVVIAKPDIIKIFGDFVKTILGI
>gnl|CDD|468651 NF040686, TcpD_dom, TcpD family membrane protein
FVKELGVYIIIGIAVFKAIKEWAKGKVGKMIVAIVIGGLVYFFLNNPETVLNAIGGILKKLFG
>gnl|CDD|468652 NF040688, ADPRT_certhrax, ADP-ribosyltransferase certhrax. The two members of the seed alignment include the originally described ADP-ribosyltransferase called certhrax, extended somewhat upstream of the originally predicted start codon, and a full length homolog from Bacillus toyonensis with 72 percent identity, likely to function in the same way and merit the same name
ILSVSCLVSMIAVITPIFMTNTYAMNEHHIEEAKSHEDVDIHVEEKNKEDKIEKEKSPEERMKEIIRNIV
ELDVRADTDENAKKTQELLEKLPHEVLELYDNVGGEIHITDKKLTQHEELNDSSHKDMFIINSEEKGFPL
KEHFVFAKGGKEPSLIIHAEDYASHLASKEVYYELGKAIIRDTFPLNQEELGNPEFIKAINEVNQQKEGK
GLNAKADEDGRDLLFGKELKKNLEHGQLIDLDFIIGHLSEFQHVFAKSFAHYFEPHYKEALKSYAPALFD
YMEELDQMRFKEISDDIKEKNKNVLDFKWYTRKAESWGLQTFKEWKENLTISEKDIIKGYTGSKYDPINE
HLRKYDGEIIPNIGGDLDKKGEKAKEKIENQIKDLDAALKKSKIPENLIVYRRVSELQFGKEYEDYNLRQ
GGIINEEKLAELEGKFKGQTFIQHNYMSTSLVQDPHQSYSNDRYPILLEITIPEGTHGAYIADMSEYPGQ
YEMLINRGYTFKYDKFSIVKPTRAEDKGKEYLKVNISIDLE
>gnl|CDD|468653 NF040689, MtrAB_MtrA, MtrAB system response regulator MtrA
ILVVDDDPALAEMLGIVLRAEGFETVFCADGAEAVEAFREVRPDLVLLDLMLPGMDGIEVCRQIRAESGV
PIIMLTAKSDTVDVVRGLEAGADDYVVKPFKPKELVARIRARLRRSEDEESEVLRIGDLTIDVAGHEVTR
GGEEIPLTPLEFDLLVALARKPGQVFSREELLEQVWGYRHAADTRLVNVHVQRLRAKIERDPENPEIVVT
VRGVGYKAG
>gnl|CDD|468654 NF040690, mycolate_SDR, mycolate reductase. Catalyzes the final step in mycolic acid biosynthesis
SLPAPSPDARAVVTGASQGIGEALARELAARGHNLILVARREEVLEELAAELTAAHGVTVEVRACDLSDP
AARAALIDELATREISILCNSAGIATFGPFADLDWDYERAQFELNATAVHDLTLAVLPGMLARGSGAILN
VGSAAGNMPIPNNATYVFTKAFVNTFTEALHYELKGTGVHCTLLAPGPVREAVPPEEEQSIVDKVVPDFL
WTTYESCARETLDALARNKRRVVPGPLSKAMSVASQYAPRAILAPIVGSFYKKMG
>gnl|CDD|468655 NF040691, MtrAB_MtrB, MtrAB system histidine kinase MtrB
WRRSLQLRVVAITLLLSLVVILVLGVVLALQITNGLLDNRVDAALGDSRRARTQAQSQLNASDASTSDSA
QQLLRTTLLSVLASASGAMQGAFDVVLLVPGDDPSGLGPRASGSVGLVSQIPEELREAVAGGQVAQQYQS
VALPSGDGSSAPALVVGTPVTLPVAGNYELYLLFPLEDEQSTLALVRGTLLLGGLALVVLLGLIAWLVTR
QVVAPVRSAARTAERFAAGDLSERMPVKGEDDLARLARSFNQMADSLQRQIRQLEELSRLQQRFVSDVSH
ELRTPLTTIRMAADVIHDSRDDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDVEPVDLRP
LVRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQDDTAVA
VTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTL
PRVAGDRLTTSPLPLVP
>gnl|CDD|468656 NF040692, recomb_assoc, gamma-mobile-trio protein GmtX. Members of this family are found regularly in the context of a XerC/XerD-related recombinase and with a member of family PF13009, called a putative integrase by Pfam. The family is named GmtX, for Gammaproteobacterial Mobile Trio system protein of unknown (X) function. Members of this family include VPA1268 found in a pathogenicity island of Vibrio parahaemolyticus
EVLLELLKEGASPRKQKSLEAIHEICREQYERGSRDFSIATIGRLSKARGGPSAQSIRNKTGEDYRALIE
AWAEYAGPTTKKPPKKKKKKSVPSDNDWLDRIEDPAVRALVGILIAERKKLKAELNLLKPNAEIVIDRRP
VGGASLLPSLSAKLTDSEREALEYAISEEFLEKWGWTEGERGEVVDENGREVFKPGFVDAIKKILG
>gnl|CDD|468657 NF040693, recomb_GmtY, gamma-mobile-trio recombinase GmtY. GmtY (gamma-mobile-trio system tyrosine recombinase) is a putative integrase regularly found associated with two other proteins of unknown function, in a cassette found sporadically in various Gamma-proteobacteria. Members of this family include VPA1270, found in pathogenicity island 6 of Vibrio parahaemolyticus RIMD2210633
VKVKAKIVRDNTGVTTELPVLLTEKGILLPLLLYYLERNRDKSLSWMRRVAFAVGLLLDYIEANASEFSS
PTELFRAFAQALYSGTIDDDGGDPSGLYWRPRSPEDANRLLSHLTEFSDWLAERYGGTALNNPLRKATSA
EERLNWAAYYHRRQNAFLGHLKDKSIASERAKARRRVRRPRRPKVDGSDAKAFPEEHIEDLLFDGFGNAG
AADGRLDLRDILITLLMHGGGLRESEPFHLWVDDVFIDPDNPDEALVRIYHPEDGKAPNDWKTGRKGKTN
RAEYLAEKYGLLPRNTYAGSHRLHAGWKGPLLDHKDNYFEVYWFPPEAGELFLELWRLYLKYRRPVDLNH
PYAFVNFHGETGQPYTIKAFNQSHKRAVKRIGLTPSKSLGTTPHGHRHAYGRRLRNAGVDPLEIQKAMHH
KSPESQLVYTQPTAAEVRAAL
>gnl|CDD|468658 NF040694, ribK_Meth, CTP-dependent riboflavin kinase
MKIFGRVVSGKGEGRYFMSLPPYKEKFKKILGFEPYEGTLNIKLNEKFNLDKFNPIETDDFEYNGKKYFG
VKVLPVKIFNKDGGEIDGAIVAPKKTYHSSNILEIIAPIKLRKYLSLKDGDVVKIKI
>gnl|CDD|468659 NF040695, FlaK_Arch, preflagellin peptidase FlaK
INYIIGLIGLLIASIQDLKSREIEDYIWISMVIFGFLYHIYLSFTTGNYSYIINSISGFIICFILGYFMF
LLGVGGGDGKLLMGLGALVPKYNMPIYSPLGSLLNINYIPSFPIMVFINGIFFMIFLPIIIFLKNLIRGV
KPKTKKEFILMFFGEKMKVKEAKKKNRLILGKDENIKLFPSSEDDCDFSKYDDDEEIWVTPAIPFIVPIT
LSYILTPIIGDKIIYIILPF
>gnl|CDD|468660 NF040696, isopcys_mtase, protein-S-isoprenylcysteine O-methyltransferase
LALKIIFVIGLVAWFIIRYPYARRARRNKIVRDRRTPREKLLLFLSFVGLGILPLIYVFTGWLDFADYAL
PPWAAWLGVVVFAAALWLFRRSHKDLGRNWSPSLEIREGHTLVTSGVYRYIRHPMYAAFWLWAIAQALLL
PNWIAGLAGLVGFGILYFLRVPREEQMMLETFGDEYRAYMQRTGRLIPKI
>gnl|CDD|468661 NF040697, VPA1267_fam, VPA1267 family protein. Members of this family occur in mobile elements, as for VPA1267 found in pathogenicity island 6 of Vibrio parahaemolyticus RIMD2210633
ANGQQLAEENLEKFEAWKASKTDDDFRQMVHRGQLNRGEIAKECGFGKSALRQNPRIKAALKELEDDLRE
RGVLPPLTEKAKESVDAPPKLYDAEAKRRARDAERLRRLEQENAELKAENAELKAKLERYGELSEVLAET
GRL
>gnl|CDD|468662 NF040698, IdsA_Meth, short chain isoprenyl diphosphate synthase IdsA
MDVTEILKKYSEDIDAEIEESLSTIDPEELQEASIHLTKAGGKKLRPALTLLSCEAVGGNEEDALKTAAA
IELIHTFSLIHDDIMDDDDMRRGKPSVHVVWGEPMAILAGDTLFSKAFELVLETKEDNVSYERVVEALAT
VADACVKICEGQALDMGFEGRFDVTEEEYLEMIYKKTAALIAAATKAGAIMGGATPEQIEALYEYGRLIG
LAFQIQDDYLDLVSDEESLGKPVGSDIVEGKMTLMVVKALEKASEEDKERLIEILKAEDQEDVDEAIEIF
EKYGSIEYAKNVALEYVNRAKELLDILPDSEAKEALLKLADFVLERKH
>gnl|CDD|468663 NF040699, VPA1262_fam, VPA1262 family protein. Members of this family occur in mobile elements, as for example VPA1262 found in pathogenicity island 6 of Vibrio parahaemolyticus RIMD2210633
ALQLWVLQIKSEESIEYRLLYGRVLPYDFSSNLWSFSDIDKKKSFGGYKAQVIRLTLYLNSEELKGFLEK
LIEGRSLSEASENLGLNLSKKLDVLFGDTHLAEKNLAYRPVMYLLNRDLYNRRTLLSPHSSASADSASIT
QLNKLSLFDVDGGNYDLALAEFLVEKLNEETGLDFGGADAWRLGNLEILVFPALDDKEKSLLSVKWVKKS
RTLSVRINPKLTPVPSDLLVNLRISNDGQVVYSLIKTASRDDEYPFEIEFELESQLNEITDSIELEIFDF
SVDSETGELCYEWRVHLIREINFQMHVVGGGSSPVKDDWLKKLVRPSSSKRLEAALKVNRGTHGSNIVVG
GRKADPWVPANRELKSLLAKLFPPKSEGRFFPKGGDSDGEGRLEFVEWFKELLEKYQDKQVVIFDPYFED
VGLSKLLARLGATNAEYIVFTSLPKPDPQEKDESDNKNSNRINNLLAACKHNPPLLGGVKLRIVGLKEQK
LHDRYILIRDKDGLPVDGYHLSNSLQSAAENYPLLITPIPSDVLLKVEEYIDELLQGAKQEKEAPEVELP
SMKLLFKSSKSKEEPKSLYEPLSFLEKPEAGDVLSPWLGEPSLEGLSGDRLKEKLETLGLLDDDSLLLQE
KFGLLLCIFWKDGLDLSDFNKLWDALGEVLAHSPAGDYLLSLELRSEPELLREFLELLLEFLDASRDRAH
QEIKDKELAIDLLKFLQKSLEELLHSSYQPLHLFHPTKYYLLSWGDYYAIKLLWSYAPQALLRILEEQAS
LLPIEPDSSNARRLSLLSQILSEISLSIEFDWISDEQLDALLKSDNPLLRWLGLLALESQLEKPDKLLEA
VLKLLLLLSEDEKVKLLGWLINEARNENNKAKIYEELILLLHQILPESLPKEDLKELLDSMRGHMGQLEW
AEPWLLKDVLLPLLESGRLSLDDACEIWFDELIELLKPKLGKNKRLFFKARSEGQFTNEAAWLFAESSPE
DQEELLKELKKILNKARRILQQPLASTSNYSKWDDAFKVSLWIL
>gnl|CDD|468664 NF040700, VPA1262_N_dom, VPA1262 family N-terminal domain. The founding member VPA1262, of this domain family is a large protein of 1104 amino acids, found in a pathogenicity island of Vibrio parahaemolyticus RIMD 2210633. Many homologs of half that length share homology only to the N-terminal half. Members of the family share well-conserved DP[FY] and HDR motifs. The related model NF040699 describes full-length homologs of VPA1262. The function is unknown
AKLYRLRLVLDAEEAKDWYRGLSRGSSLIPASERLGLDLSSKDGWKFGGTSLSDELPPWPVLFLPNRDAF
LSGSRILSPNGWAGSYSAEIFDEFKDDLFLLGDDADELLQELLEFLKDETGIDFGGYDERLGNLELVAPD
PDDREVTLFLVKAKDGDESRGLFVRFIPRPGASLRGLRVTLENGDQVLLSSFKTLDVPEDGPLEIEFPSE
EPIGSYGLKVWDPEGGLLLYAWPVSFIREINFNMHVVGGTRVVKVPWLEKLKSPDRAYKVERRSRSSSVV
GGRPKDPWVPARLYIAELKRLLLPPKSEGRFFQRGWGDGRLEALEWIRKLINQAGSKGVIIVDPYFEAVD
LLQLLFRLSRSDVDLTILTSLKAFDPDDKDGTNPSRDRIQRLLAALEELKNKQLLHLELRVLNLPRGWAF
HDRFLLIGADDGDPDVWLLGNSLNSAGENYPLLITKLPDDVLLEVIDYLEELLNG
>gnl|CDD|468665 NF040701, RecJ_Meth, single-stranded-DNA-specific exonuclease RecJ
MIRKNEDKNILIYTHIDTDGITSRAILSKLLERLNIDAEFEFLKQINLDTIDDIPFDYDLIIFADLGSGQ
LSLIKEKITSNSKIIILDHHPPERKKIPENIIEVNPHNYGIDGSKEICGAGVCYLLAKTFNPNWDLSKYA
VLGAVGDMQNLEGKLVGLNREILKDAIELGDVVSFPDLQIYGRQTRPLFVSLSYFGDVRTDLTNNDSEII
NFINKLNIKYNKNIEPTRSLCDLTFEEKRILGSELLRKCSRYVPPRWVKYLPKVIFGESYEFLSEEKYSP
LRDLEEFSTCINACSRYGDYETALNVLKGDRGKYLDKMEKMLREHRRNLAEKLDWIKDEVEIIQKDNFQY
FETDKIKSNIIGIVAGMSYSIGEVDWKKPIFAIGELDNGYKVSARCPRLLAFAEDINLGKAIKYASEKVG
GSGGGHKFACGAYIPEGKEDFIKYLEESL
>gnl|CDD|468666 NF040702, ileS_w_GNAT, isoleucine--tRNA ligase, N-acetyltransferase domain-containing. This unusual form of isoleucine--tRNA ligase, found in at least six different species of Moraxella, has a GNAT-type N-acetyltransferase domain, about 170 amino acids long, inserted after position 270 of forms lacking the insert, such as that of Escherichia coli
DYKNTLNLADTPFPMRGDLAKREPKWLEQWEKDDVYQQIRKARQGLEKYILHDGPPYANGQIHLGHVVNK
VLKDIIVKYKTLDGYDAPYVPGWDCHGLPIEQKVEGIIGKVGQPHKDKKNGAIVTATEFRGACREYAKSQ
IALQMADFKRLGVLGDWDNPYLTMNFQQEADTVRALAKIYDNGHIVRGLKPVNWCLDCGSALAEAEVEYE
DKKSDAIYVGFDIVNRENLPATANISGTLQAVIWTTTPWTLPANQAISVHSDFDYAVIKGKKTPAFALPS
QIDSENFTLRTLTKADKQALQACASDPAIWEFMPTKRHLPEVFEPFFEQALKDKAYAIIDKRTGNIIGTT
RFYDDNAKDDSIAIGFTFITPEYWGKGANAEIKQTLLNHAFKYRNTVWFQIHEGNDRSKKAVEKLGATYQ
KDVENDFGKMWVYTIATNPSTINHTAHFIVANDLVADFSKNVALDDVKVITTIKGADLTVLNAQHPLISE
RQVPIITGEHVTADSGTGLVHTAPAHGVDDYNVGRKYNLPTENPVGGNGVYLPEAKVFVGEHIYKAQPKI
IETLQASGHLLKHKKITHSYPHCWRHKTPIIFRATPQWFISMEKNGLREQALDDIPKVVWTPAWGQNRIE
AMMHGRPDWCISRQRTWGVPIAFFIHKDTGELHPRTSELIEQVAQLIEQGGIEAWFDAPAEDFIGDDAKE
YHKSTDTLDVWFDSGSTNFAVLAQRDELTNPADLYLEGSDQHRGWFQSSLLVSEAIYGRPPFKQVLTHGF
TVDAKGYKLSKSKGNTKGFEPQELADKYGIDILRLWVASSDYRYEMAVSKEGFDRTTDMYRRIRNTIRFL
LANTDDFDPATDMVAADELVSLDKYILHRAKQVQAEIRKAYTNMDFHQVCQAVMGFCSQDLGGFYLDIIK
DRTYTTKADGLPRRSAQTALYHIAHALLRWIAPILSFTAQEAWQVLKGTDGYIFTQEWYELPSVAMDDIT
SDDWQAILAVKDTVNKAIEQARTDKIISSNLTAKVTITADGDTADALNKLGDELRFVFITSDASVKPGDT
LSVTITPADGEKCVRCWHIRTDVGTHANHPELCGRCVTNVDGDGEVRHYA
>gnl|CDD|468667 NF040703, cyclopro_CfaB, C17 cyclopropane fatty acid synthase CfaB
MLAQLPPALRNLQLPLRLRLWDGKQLDLGPSPRVTLVVKDPSLLSQLTHPSLDLLGSAYVEGRLDLEGPI
MEVIRVGDELSQALLGDDDEAPPERTAHDKATDAAAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDL
AQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVEVFGITLSKEQLKLARERVAAEGLQDR
VQLELLDYRDLPQDGRFDKVVSVGMFEHVGHANLPLYCQRLFGAVRPGGLVMNHGITARHTDGRPVGRGA
GEFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLHYARTLEHWSARLEARLDEAARLVPERALRI
WRLYLAGCAYGFARGWINLHQILAVKPLADGSHELPWTRADLY
>gnl|CDD|468668 NF040704, IPP_alt_MvaD, archaeal-type phosphomevalonate decarboxylase. The archaeal alternate mevalonate pathway generates isopentenyl diphosphate by decarboxylation of mevalonate monophosphate followed by phosphorylation of isopentyl phosphate. This model represents the enzyme responsible for the decarboxylation of mevalonate monophosphate that is found in halophilic archaea
KATARAHPIQGLVKYHGMRDEELRLPYHDSISVCTAPSHTTTTVEFDPDLDEDTYVIDGEEVDGRGAERI
ERVVDHVRELAGIDHRVRLESENSFPSNVGFGSSSSGFAAAAMALVEAAGLDLSRPEISTIARRGSASAA
RAVTGAFSHLRAGLNDEDCRSERIETDLEDDLRIVAALVPAYKETEEAHREAADSHMFEARMAHVHDQLA
EMRDALREGDFERTFELAEHDSLSLAATTMTGPSGWVYWQPETLEVFNTVRELREEEDVPVYFSTDTGAS
VYVNTTAEHVDRVEEAIADCGVETRVWEVGGPARVLDESEALF
>gnl|CDD|468669 NF040705, sigma_mbnA, methanobactin precursor domain-containing sigma factor. This variant form of sigma factor is found exclusively with a C-terminal methanobactin precursor domain
TIDRLFRSHHRDLITRARRVIGSDDAEDMVQEAYLKMLESDRGELVANARGYVSKMTCTLAIDALRRQRT
HARALAEDGAWFQSAARDAPIASALDAFGLAFDVQAALARLPRCCRQIFLMSRILGFSHSEIAQELGVSL
RTVNRKLGRALEHFDRAFEIARRSAPVSAPPLKADSPRESLAQSPAAPSVVRDATEIKIPSARKNSRRRL
SDFCGLARHTIRVPRSAEPVWTFQTNSKGEAPMTIRIAKRITLNVIGRASARCASTCAATNG
>gnl|CDD|468670 NF040706, photo_cyt_PufC, photosynthetic reaction center cytochrome PufC
EQPPVESVQTGYRGTGMEQIENPRTLAALDAANQVPEPIPAADPGGPKAGDVYENVQVLGDLSVAEFNRL
MAAITEWVSPEQGCNYCHNPENLASDELYTKVVARRMIQMTQNINENWKGHVAATGVTCYTCHRGQPVPA
NVWFTDPGPPHAGGFAANNQGQNTPAASVGYTSLPYDPFTPYLLGDKEEIRVHGTTALPTGNGASIQQTE
WTYGLMMHMSNSLGVNCTFCHNSRAFYDWDQSTPQRVTAWYGIRMVRELNNDYLEPLTDVFPANRLGPLG
DVPKVNCATCHQGAQKPLYGANMLKDYPELA
>gnl|CDD|468671 NF040707, Siroheme_Dcarb_AhbB, siroheme decarboxylase subunit beta
FTKTERAILRIVQDNLPDSHTPYADIASELGTDEQTVLALLRNLKEEGKIRRFGASIKHQAAGITHNAMV
AWNVDDEQVEEVGNIAAEHPEISHVYYRPSTAPDWPYNLYTMIHGRHPEDCEKVIVRLREETGLEEYAVL
FSLRELKKTSMTY
>gnl|CDD|468672 NF040708, Siroheme_Dcarb_AhbA, siroheme decarboxylase subunit alpha
ELDETDKKILDIIQTGFPLEPRPYAVLGEILGLTETEALARVRALNERKAIRRLGANFSSWKLGFRSTLC
AAKVPEDRIDEFVAEVNEHVEVTHNYLRAHQYNLWFTLIAPSWERVCSILDEITEKTGIPILNLPAKHLY
KIRVDFDMD
>gnl|CDD|468673 NF040709, benzoate_BenM, benzoate utilization transcription regulator BenM. The LysR family transcriptional regulator BenM is both a paralog and a neighbor of CatM. Both transcription factors sense the catabolite cis,cis-muconate in order to play a role in benzoate catabolism. This model describes BenM
MELRHLRYFVAVVEEQSFTKAADKLCIAQPPLSRQIQNLEEELGIQLLERGSRPVKTTPEGHFFYQYAIK
LLSNADQMISMTKRIASVEKTIKIGFVGSLLFGLLPRIIHLYRQAHPNLKIELYEMGTKAQIEALKDGRI
DAGFGRLKISDPAIKRTLLRNERLMVAVHASHPLNQMKDKGVHLNDIIDEKILLYPSSAKPNFSTHVLNI
FSDHGLEPTKLNDVREVQLALGLVAAGEGICIVPASTQSIQLFNLSYVPLLDPDAISPIFIAARNMEEST
YIYSLLETIRQIYAYEGFS
>gnl|CDD|468674 NF040710, benzoate_CatM, cis,cis-muconate-binding transcription regulator CatM
MELRHLRYFVTVVEEQSISKAAEKLCIAQPPLSRQIQKLEEELGILLFERGSRPAKTTEAGMFFYQHAVQ
ILTHTAQASSMAKRIASVNKILRIGYVSSLLYALLPEIIYLFRQNNPEIEIELIECGTKDQIEALKQGKI
DLGFGRLKISDPAIKRILLHEEKLKLAIHKHHHLAEFAAQGIHLSQIIDEPIFLYPASQKPNFATFIQSI
FTELGLVPKDLIEIREIHLALGLVAAGEGICIIPASAMDIGMKNLLYIPILDDDAYSPISLAVRNMDHSN
YIPKILACIKEVF
>gnl|CDD|468675 NF040711, partner_SinI, SinI family autotransporter-associated protein. Members of this family, including SinI from Salmonella enterica LT2, are putative passenger proteins of a variant-type type V secretion system (T5SS), in which SinH or a homolog is an inverse autotransporter that transporters a member of this family as well as its own passenger domain
KRRLTKVALALALAGYCAVPAAAAATGSTGTIQGTVPVLSAPTDKAHVTVTIDRGARTSEGDKQLHVGDK
ITLNYAIGDTEGDLDASTATKVTIKWVSYSDQAGVDAKEISGTAGKDSYTIPAADADRYIGVKITETTTT
GDPNVGQTITLNDLSTNAGGGSDSDDIPPGPVVDGTVGVYIYEDTAFTTNLIGTATKLNVGHTYVFKLWD
DKNGNGVYDAGEDDVTNNYDYRWRFTGTSATLGTAGGIANSSTNNKDLVIPATNAEAKGAFATAGADGVQ
GYGLSVDY
>gnl|CDD|468676 NF040712, SepH, septation protein SepH. Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments
MRELRLVGVEPDGTHLVLKDADGERYRLPVDDRLRAAVRGDRARLGQIEIEVESQLRPREIQARIRAGAS
VEEVAEAAGVPVERVERFAHPVLLERARAAELARRAHPVREDGPAVLTLGEVVAERLAARGHDPEEVEWD
AWRNEDGRWVVQLSWTAGGSENTAHWTFDPGAHGGTVTALDDEARWLIDPDFGRPLRPLATVPRLAREPA
DARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEP
PAPGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRASVPSWDDVLLGVRSS
>gnl|CDD|468677 NF040713, ZapE, cell division protein ZapE
RYEAAVAFGGYRPDPAQAAAVERLDRLAEELAAPAKKRGLLGRLFGRKKSPPRGLYLWGGVGRGKTMLMD
LFYEALPIERKRRVHFHEFMREVHQRLALLRGQADPLPPVADEIASEARLLCFDEFHVDDIADAMILGRL
FEALFERGVVLVATSNTPPDDLYKNGLNRERFLPAIALIKAHFDVVNVDGGTDYRLRRLEQAPVYLTPLD
AEADAALDAAFARLTGGAAAEPGTLEVNGRELPVPRAAGGVAWFDFADLCEAPRSPSDYLALARRFHTVL
LSGVPPLGDESRDAARRFIALIDELYDRKVKLIISAEVPLEELYTEGGLAFEFERTLSRLQEMQ
>gnl|CDD|468678 NF040714, streptamidine, streptamidine family RiPP. Streptamidine is a ribosomally translated, post-translationally modified peptide (RiPP) whose modification depends on a YcaO family maturase. The mature product derives from the central hexapeptide HLSATH, or a similar peptide. See related model NF040715 for a similar family in which a related RiPP precursor domain occurs typically in two or more tandem repeats
VFTPVEEERQLAHLSASHSNALVENPFD
>gnl|CDD|468679 NF040715, AmiA_rel_RiPP2x, streptamidine-related RiPP repeat. This HMM represents a family of streptamidine-related RiPP precursor proteins, most of which have two or more repeats of the 35 amino-acid long domain that contains the modification site. Modification is performed by a YcaO family peptide maturase. The related model NF040714 describes the family of RiPP precursor proteins that includes streptamidine (AmiA) itself and close homologs. While in the streptamidine precursor AmiA itself and its homologs, the core peptide is HLSATH or something similar, the six residues from this family that align are typically APQGPG, suggesting a very different mature product
MSEISFEEIAAAAVLAAPQGPGTNALVHNPFAFEE
>gnl|CDD|468680 NF040716, YcaO_for_S12, 30S ribosomal protein S12 methylthiotransferase accessory factor YcaO. YcaO acts as a partner for RimO to achieve the modification of ribosomal protein S12. Homologs of YcaO are involved a wide variety of RiPP (ribosomally translated, post-translationally modified peptide) natural product biosynthesis pathways. Some members of this family have an additional N-terminal OsmC-like domain
TFIPGKDAALEDSIANMQTKLQALGFNIEEASWLNPVPNVWSVHIRDRDCPMLFTNGKGASRKAALASAL
GEYFERLSTNYFFADYYLGEEIANADFVHYPNEKWFPLGDDDSLPEGLLDPELRAFYDPEGELTASDLID
LNSGNAERGICALPYVRQRDGETVYFPVNLIGNLYVSNGMSAGNTLAEARVQGLSEIFERAVKNRIIAEG
ICLPEVPEEVIARYPAIAAGIEALEAQGFPVLVKDASLGGQFPVMCVTLLNPKDGGCFASFGAHPRFEVA
LERTLTELLQGRSLDDLDGFPPPTFDLEEVAEPENLETHFIDSSGVISWDFFSDTPDYEFVDWDFSGTTE
EEFDWLIAILHAEGKDVYIADYEHLGVYACRILVPGMSEIYPVEDLIWDNNNVGLLLREALLNLPELDDE
QYAELLDRLEESGLDDHQPVAELIGLAPDPGTVWGTLRIGELKLLLALALGDLEAALEWVDWILQFNQLT
AERLLFYRCLAALLELTLDEERDPEDYRAALARMYGEETVDAAWGLIDGSVRFFGLTAGGLNLEGSQAHQ
RLLAAYQKLQK
>gnl|CDD|468681 NF040717, BcsR_only, cellulose biosynthesis protein BcsR. BcsR (bacterial cellulose synthesis R, previously YhjR in Escherichia coli) is a small cytosolic protein essential for cellulose. It appears to form part of the Bcs macrocomplex that also includes membrane, periplasmic, and outer membrane components. BcsR shares homology with the N-terminal domain of BcsP, a longer protein with variable and repetitive C-terminal regions, found in beta-proteobacteria. See PF10945 for an HMM that describes the shared region
DDIAALSQAFSLPELRYVDISRQERLAAALARWPLLAELAEE
>gnl|CDD|468682 NF040718, BcsP_of_Ic, cellulose biosynthesis protein BcsP N-terminal domain. BcsP is a protein of bacterial cellulose biosynthesis, encode in the beta-proteobacteria in type Ic cellulose biosynthesis operons. Only the N-terminal region, homologous to the much smaller protein BcsR, is well-conserved. Pfam model PF10945 describes the region shared by BcsP, BcsR, and some other cellulose biosynthesis proteins
SDSDDISNLFRRFGGDAGQYREIGRENEAKQARERWPLLGAVDPGQAAIVPPVVG
>gnl|CDD|468683 NF040719, Lar0958_adhesin, Lar_0958 family LPXTG-anchored mucus adhesin
MLSRKNYKETIRKQTPTKQYYTIKKLTVGVTSVLIGLSFMGELEGDSVHADTMTASSESTSVTSTTAQDG
LKKSPQLYLQVTDTNNPSTPLSASSTGTSKNVTSSAAVQVKSASDEEDSDSTLAKGENKFARSAVKDSVT
DGKTSTAEINPAKLSSPALITQLNQSLAKSSTSDAAKANDELEIKATDPTNYPNCGDVYGPLFELDASGQ
LVNKDEVISLKDMYIFQILKLVNTKDSDFQYVILTMNRKDTADRSVYLFVTGSNYSNAVVVKVKPNDTYE
LSKTGYSVTYTEPTTINGHYVDGTFYVTGSTYDDGFIMPDWQLQHLQIIYSLGNYDPSNTDATSVCEIMP
SYEKVPVIKYSGVPSNISQPKVYITGFTGQEFNVTDIINNYKKVFKGYYLQNPNVASMGTLSQFENGGYY
LKTYYDNDGNVDFKGLYHQIDDQGTMSVSVLNADNKTIVGPENILAGKSHNFNFNGHNWIARNPYVTSSA
HEVILKYAKLGSVIPVDENGNKINDGWQYVNDPDDASKATSPYEKAPVIDGYVAVNPDETIVLPHNLSSD
TKIYYRKRIKVTYSGSDSKTYDGNPANFEPTTVQWSGLKGLNTSTLTSADFTWNTADKKAPTDAGKYTLS
LNTTGEAALRKANPNYDLKTISGSYTYTINPLGIDKVTYSGSDSKTYDGNPANFEPTTVQWSGLKGLNTS
TLTSADFTWNTADKKAPTDAGKYTLSLNTTGEAALRKANPNYDLKTISGSYTYTINPLGIDKVTYSGSDS
KTYDGNPANFEPTTVQWSGLKGLNTSTLTSADFTWNTADKKAPTDAGKYTLSLNTTGEAALRKANPNYDL
KTISGSYTYTINPLGIVTVNYKGYDKKVYDGQPGTINPGKLTWSKLPDGTSLKMPTWSIDDFAWETADGL
APTAVGTYRIILTDAGKAALKKINPNYDLSSITGVFTYEIKPAQTPEILGQTPEQQPGQNTNQSGAENGF
GSSTRPNASTNSNLNQLPQTGNEHSNTALAGLALAFLTAMLGLGKKRKHD
>gnl|CDD|468684 NF040720, MptN_Meth, tetrahydromethanopterin:alpha-L-glutamate ligase
KIGIIVTDRNDWTANALIRACEKKDIDPVLIDLSKIEVSIGSDIKFKYGKINLLDLDAIFVRDIGAGSNE
GVSFRFDVLRYLEELGIPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKFEDAVL
KPVFGYKGKGIVRIKNGESIATKLELLNEFKEERGMLYIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPE
GNWINNLSQGGTPERCELTEEQEELAIKAAEALGLVYAGVDLIESKDGLKVLEVNATPSWAGIYKVWGIN
IAEKIIDYII
>gnl|CDD|468685 NF040721, Trm14_Arch, tRNA (guanine(6)-N2)-methyltransferase
MEFYATLSPGLEKISAEEIEELGGKIKEIREGKGRVFFEGDLELIPKLNYLSRTLERIVILLHREKFEGS
LEDIYKRVYSIDFSFIKPEQSFAIRPLRVGEHDFTSIDIGRVAGEAVIDSYLRDKGVRLKVNLDEPDVIV
RVELIFDELLVGIDTTGDEGLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAA
LIKRNIPPGKFREDFAFKKIFGHELLEKIKKDVELKIYGIEKFRKHLEGAKKNAENAGVDDTIKFIQGDA
TKLDKYFDSVDVIVTNPPYGLRIGKKRIIKKLYNNFLRSAKKILHKRSRIVVITAEKKIFEEAAAKNGFE
IIEEFNVMYGGLLTKVFVLK
>gnl|CDD|468686 NF040722, MfnD_Meth, tyramine--L-glutamate ligase
FFFEYAVGSGIVDKDILEEGKLMFDTLLNQFLKEGYTVITLIDEKYYNDYKNYKNLKILEINNGDNLMEK
IEEILNNEKIDYALIIAPEEDGILYNLTKIIEEYGVLNLGSSSKAVKIAGDKYLTYEAIKDIVKTPKTFP
PKKYVIKKIDGCGGTHQIIDENYIIQEFIEGEPYSVSFIVGKNSIYPLSLNKQYINEKGYCGGEVNIDHP
LKEEIINECEKALKKIDGLNGYVGVDVIVNGDEIYILEINPRITTSICGIKTNPSLAKLLIDNALGKELK
FKVEVGKKFK
>gnl|CDD|468687 NF040723, UDP-GlcNAcDh_Arch, UDP-N-acetylglucosamine 3-dehydrogenase
LRVGVIGVGAMGYNHARIYSEMEGVELVGIADVNKERVKELAKQYNTKAFTDYKELLKEDLDAVSIVVPT
KLHKQVALDAIEAGVNVLVEKPIADTIENAQEIIKAAKKNNVKLMVGHIERFNPAVLKLKEIIDSGLLGK
IVSISAKRVGPYNPRIRDVGVILDLGVHDIDVISYLYGSKVKEVYAIAGSVIHPFEDHASIMLRFEHNIS
GLVETNWLTPHKTRKLTVVGTEGIAYLDYINQTLTIHDEEWVKEAKIEKEEPLKNELEHFIECVENGKEP
LVSGEDGLHALKVALAAIESYK
>gnl|CDD|468688 NF040724, GpgS_Meth, glucosyl-3-phosphoglycerate synthase
MDFYQEDITTIHDFCIDKERLEERIEDLSEKRPAVLIIPILYEEIENPPLQNIVEELNKCTCLKQVVIAL
AADNEEQYRHVVEFFKQLKLPHMVVWCNGPRVQNIIEDMKEKDLDITSFKGKGKDVWLALGVASLNSYAI
ALHDADIVTYSKDIPAKLLYPIVNPELNFFFNKGYYARINLEKKTMHGRVYRLFVRPLLDTLQKELRCQS
DILDYLRSFRYTLSGEFAMTSDLALNIRIPADWGLEVGLLAEVYRNATLKRICQTDLGFYDHKHKELGKD
RSEGLCKMVGDIFTTFLRIVTETTSTEISPSFLHSIRVKYKRLGQDLIRQYHTDALCNGLNYNRHEEETY
VDMFAKVIMKSGEEYLDDPSDVLMPDWTRALSAIPDLREQLREAALEDAKEF
>gnl|CDD|468689 NF040725, panto_kin_Meth, pantoate kinase
MVRTAVAAFCPGHISGYFKRVIGESPATTGSIGAGIVIDEGVTATASPADETSVKVRRTDRDGTVLEESE
GSPPIEYALDRLGVTASVTTECRLPIGAGFGLSAAALLATLTALNALFDLGLSREEIAALAHEAEVVHRT
GLGDVAACQGGGLVCRKGPGIDGEITRRYDDDEPIWAVTFGPLPTPSVLGSPEAMERIAAAFPGRCPESL
EEFFRLSREFAEKSGLITPEVREVLAACDAAGVPASMTMLGNGVFAYGDRAEEVLSKFGEVYPLHVAESG
FRILEV
>gnl|CDD|468690 NF040726, BetaRFA-P_synth, beta-ribofuranosylaminobenzene 5'-phosphate synthase
MIIKSPSRLHMTLIDLNGSIGRVDGGVGITLDKPNLVIEGEESDEIEIEFDNSILNEELLKDYEERIKNA
AKKVLDYIGEDGGIYFKVKEDYPAHSGLGSGTQISLATGKLISELYGLGLDARELAKIVGRGGTSGIGVA
SFEKGGFIVDGGHSFGKEKGDFLPSSASKASPAPIIFRHDFPEWDIVLAIPKGEGVHGKKEVDIFKKYCP
IPLEEVQKLSHLILMKMMPAVIEKDIESFGEAINEIQNLGFKKVEVSLQSPAVKDLIEFLQDAGAYGVGM
SSFGPTVYSFTDSDAKDIVEAAKEFLDDTGGGGEVIITKANNTGAKI
>gnl|CDD|468691 NF040727, SBP_SaoB_CU, ABC transporter substrate-binding (seleno)protein SaoB. Members of this family are apparent substrate-binding proteins of an ABC transporter, found in Clostridium difficile and a number of other anaerobic heterotrophs, as part of the SAO (selenocysteine organometallic-assisted) locus. Six of the nine core proteins of the SAO locus can be selenoproteins, including this protein and the permease subunit, SaoP, encoded next to it
IIFLLLALVAALLAAALFLPYEERRNKKSIKIGAGDDASGLLMHYLINEKGKESAIVESDFESYSFKDCC
SSTAQWALSSGEIDMAVLCPDAAQKLVEKDERFEIVGPVVMNSDVLVYRDDAEPKKIGIMQKREYQKELV
KETFGQDVEIVPMLPTALPYALEKGQVDAAVLDILKALTLPGYKLPALSDDDYVTYVLVVRKDFKKTPRF
QNFLKAYNEAVDELNNEEILQNLLGHYKEIEFTKEEVEQWKKLNIKFLTLE
>gnl|CDD|468692 NF040728, MerB_rel_SaoL, MerB-like organometallic lyase SaoL. Nearly all members of this family, SaoL, are selenoproteins with a CU motif that suggests interaction with a heavy metal such as mercury. While SaoL is homologous to the organomercurial lyase MerB, its context is different. SaoL occurs as part of the SAO (selenocysteine-assisted organomercurial) locus, with nine conserved proteins. Six SAO proteins can be selenoproteins, including multiple subunits of an unusual ABC transporter with one permease subunit but two associated substrate-binding proteins
DSIYSKLTAEENKLRLYIMDYIIDNKRPFNLEELEKELLKKLNMSKEEVKKIIKSLIEKNGMVVDEDGNI
NFIYPVSALPTNHRVTLEDGREFCAMCAIDAIGSAFTFKQDIKINSKCSECGEEIFVEIKNGEIVELSPE
NLHVLHVDLNKNTNWAGSC
>gnl|CDD|468693 NF040729, ABC_ATP_SaoA, ABC transporter ATP-binding protein SaoA. SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs
KLKIQNISKTFINNKKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVT
KPGPDRGFVFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQR
TAVIRALACKPEVLLMDEPLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDK
GKILEDLKIDLPRPRNRESEKYLEYKDHLTNILKKALN
>gnl|CDD|468694 NF040730, CxCC_doxin, thioredoxin-like (seleno)protein SaoT. SaoT is a predicted cytosolic protein, usually a selenoprotein, from the SAO (selenocysteine-assisted organometallic) locus. Other proteins in the system include a putative metal efflux protein, a surface protein, an ABC transporter with multiple selenoprotein subunits, and the selenoprotein SaoL, a homolog of the organomercurial lyase MerB of some mercury resistance systems. The SAO system may use mercury or another heavy metal atom as a cofactor, incorporating it into an organometallic intermediate, associated with import of that metabolite, and then exporting the metal after its release for use in a subsequent cycle
AKVLVEFINTCPCCDEYGEMIKEVAAKYGDEVEVKIYYAGKDFDYLKKYGMVTKGTMIINGKKKYDNLSK
SIIEKAIAEAVRE
>gnl|CDD|468695 NF040731, flavo_sub_EftB, electron transfer flavoprotein subunit beta. Members of this family electron transfer flavoprotein subunit beta (EftB) as found in pathways for leucine reduction to isocaproate as seen in the strict anaerobe Clostridium difficile
KILVCVKQVPDTNEVKIDPVTGTLIRDGVPSILNPDDANALEEALKIKDEYEDVTVTVITMGPPQADDML
RECLAMGADEAYLLSDRAFGGADTWATSNTIAAAIRKIGDYDIIFAGRQAIDGDTAQVGPQIAEKLGIPQ
VTYVQDFKIEDDKVIVQRQLEDGYEVIEVQTPCLLTAVKELNKPRYMSVKGIFDAYEKEITVWNIDDVDV
SPEEVGLKASPTRVFRSFTPPPKGKGVMLEGTVKEMAAKLISRLKKKHII
>gnl|CDD|468696 NF040732, DsrE_rel_SaoD, DsrE-related protein SaoD
MKVAYVFSSDNSRKILDNMIIPQLEAGRHGAEVVGMFFFFDNTYMLLKGTEIGERLQKLHEKTGMLLMAC
DQCAIERGIEDKLIDGAGIGCFPNLYAALGSAGVDQVITL
>gnl|CDD|468697 NF040733, ABC_perm_U, ABC transporter permease subunit SaoP. SaoP, one of the nine proteins of the SAO (selenocysteine-associated organometallic) locus, is nearly always a selenoprotein, and is one of six novel selenoprotein families from that locus. The Sec (U) residue occurs at a position described in other ABC transporter permease homodimers as the channel-gating position. A role in importing (and perhaps even forming) organometallic compounds, in a cycle in which the metal atom is reexported and reused, as a cofactor that aids in utilization of some otherwise refractory substrate, has been suggested. The SAO system occurs in Clostridium difficile (a human gut pathogen), Brachyspira pilosicoli (an intestinal spirochete in chicken), Desulfopila aestuarii (a deltaproteobacterial sulfate reducer from estuary sediment), etc
KKNGIKELIYKIIVFIIIIIIWQFAANYYDSPLLLPSPEDTLKAFIYSITDPEVLTNLLITLRRVLKGFL
YALLIGLPLGFLMGYSKTALKLISPIIDSLRQVPIMAWVPLTIVWFGIGDGPTIFLIAFSGVFPIILNTI
AGVQNISKDYYNAARSMGAGPLSIFKDIIVPASLPDILTGARLAISLGWMSVIUAEFIATSAGFGYSMVE
AQTRMQTDKLIALMIMAALVGFGIDRILQLLNKSLTKWRYV
>gnl|CDD|468698 NF040734, CC-COOH_SaoC, Cys-Cys-COOH (seleno)protein SaoC. Members of this family, now called SaoC, include CD2366 from Clostridium difficile. The most striking conserved motif in this family is a pair of cysteine residues at the C-terminus, which takes the form Cys-Sec (CU) in the occasional members of this family that are selenoproteins. Selenoprotein examples include WP_252346676.1 (Finegoldia magna), WP_252346670.1 (Merdimonas faecis), and WP_252346671.1 (Lachnospiraceae bacterium). The SAO (selenocysteine-assisted organometallic) system contains six selenoproteins overall, including three ABC transporter subunits and a homolog (SaoL) of organomercurial lyases. SaoC is proposed to play a role in chaperoning heavy metal atoms effluxed by SaoE to an ABC transporter with selenoprotein permease and substrate-binding proteins, for reuptake after covalent incorporation into an organometallic intermediate of some unknown class of fermentable nutrient
KILLIVIILLLLGCSGNEKKKKEKGEQVEEDNELLQYFKKNYPDKEVILCAEEDLNNDGIKDLVVIYRES
KEKNRMVVVIDDGGEYKLTNPVPAPIENQKIQFKDIDDKPPIEFIVSGSKGGNVGYAIYRIEDGELIDLF
GEGMEDC
>gnl|CDD|468699 NF040735, SBP_SaoX, ABC transporter substrate-binding subunit SaoX. Members of this family include CD2365 from Clostridium difficile, and are identified as SaoX of the selenocysteine-assisted organometallic (SAO) system. SaoX, an ABC transporter substrate-binding subunit, is an occasional selenoprotein. Partner proteins SaoB (another substrate-binding protein) and SaoP (an ABC transporter permease subunit) are selenoproteins most of the time. The transporter complex likely imports some (currently unknown) organometallic compound, and might actually couple its formation to its transport, employing a heavy metal atom as an inorganic cofactor that lowers activation energies for anaerobic fermentation of refractory substrates
KDYVIQLGYYNCDHMTAAPIAEDAGIYEALGLNVNVTGNGKVPQAMAAGQMDVGYIGFSGLLRAVNKGAP
IFVAANNHLGGSYYLVVSNDIKDPKDLIGKKLGIGTDPEEDNPWWRTYAKELGIPVEGKNYENIDMGDKD
AYLALKTGQIDGFTCCDPWGSMAEYEGTGKIMATSWGLEGDDGWGICCVYSMNKNFAKEHPELAKKMVLA
HTKAIEYIYTHPYKAAKIFAENYNVPEEVGLMTIYKKTVAEGRTLTWKIDEENIKNYIDYYKDYGELEIP
PDYEDFVDLDILEESGADDFDKFIKEKVDPVFPVGMSYEDWKAKAKEIDG
>gnl|CDD|468700 NF040736, efflux_SaoE, efflux transporter SaoE. Members of this family, including CD2367 from Clostridium difficile, are related to efflux proteins associated with resistance to arsenic or organoarsenicals, copper, and zinc
LNFIKKIILSSIDILNGSSGWLVISFILAGLLHNFLSPEKFQKMLGNKKISSIIKSTISGMLLPICSCGV
IPLGISLYYSGAYLGPTLAFMTATPIINPIAVILCYGLLGPKITIIYLITGFVVPIIIGILGNRFGGDEL
CAPGVEEEIEVIELEEDKRSFKEKIKSGLKWSFTDLALTVSKYVVPGMLLAGFILTVVPQSFIQQYLGNP
GMISLGGIAVLAAIMYVCAVGHIPFIAALVASGAAPGVAITFLMAGAATNLPELISIYKLIGKRAVIIYF
GTLVVFSLLVGYITNLLLLPNFKPVMDFDSVQNTISIANKLIFTAPDWLKYICSVIIVLLGVYAIWPKLK
KL
>gnl|CDD|468701 NF040737, peroxi_PrxU, thioredoxin-dependent peroxiredoxin
KVGCARPTGGPVGEQPPEEEPETAASVKKEEVMMMIKVGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVL
CFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKMWNDEELSKMVTGGVPFPMLSDGGGK
IGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQHVRETKGTEATPSGWQP
GKPTLKPGPDLVGKVWKVWKVEM
>gnl|CDD|468702 NF040738, nickel_Mua, nickel-binding protein Mua. Mua (modulator of urease activity), as found in the genus Helicobacter, is described as a nickel-binding protein
AIFQEFIKKLPDIKESWEVVQLFEEERQKFQEELQSYEDEILQAQAVLKDLRAEIMETKNQIKDLESQKQ
KKEEEIQQLQQELISHKIKRDLKKLEKDKKELQESRQEPLPQALKSVEIYLKDGSIAKAKPAKRFFGEDL
YRKYRVLLKENHVLKNKIFELELENSTLKIELRDFYTELFLEGMG
>gnl|CDD|468703 NF040739, ornith_OrtA, 2-amino-4-oxopentanoate thiolase subunit OrtA
AKKGDWVQIHKIVLEPEERAPQVPEDTKKVPLEMWVKGFLLEDAKIGDEVTIETLIGRKVEGTLVAVNPR
YTHDFGEPVPELLTIGKELREIL
>gnl|CDD|468704 NF040740, ornith_Ord, 2,4-diaminopentanoate dehydrogenase. This model does not distinguish between 1.4.1.26 (NAD-only) and 1.4.1.12 (NAD or NADP)
VKVIIWGLGAMGSGMAKMILSKKGLEIVGAIDRRPEKVGKDLGEVLGRGNKIGVIVSDDPEKVIKETKAD
IVLIATDSFTKEVFPKIKFILENGINVITIAEEMAYPWAQEPELAKELDELAKENGVSVLGTGINPGFVL
DLLVLALTGACLEVESIKARRVNDLSPFGPTVMETQGVGTTPEEFEKGVEDGTIVGHVGFPESIRMIADA
LGWELDKIEQTREPIISNVDRETPYVKVEPGMVAGCRHTARGYVDGEVVIELEHPQQILPELEGVETGDY
ITIKGTPNINLSIKPEIPGGIGTIAMAVNMIPHVINARPGLKTMIDLPVPRAIMG
>gnl|CDD|468705 NF040741, ornith_OrtB, 2-amino-4-oxopentanoate thiolase subunit OrtB
NSYEAVMARKNEIMKKALGIDYSKFEIGGIAFDYEGMMNEVGYSLEEIREIQRETGVGNTPLLELKNLTK
LARKISPPGKGARIFVKDEAANPSGSFKARRASVSVYHAKKLGYKGVIAATSGNYGAAVASQAAMRGLKC
IIVQECYDSRGVGQPEILEKGRKCEAYGAEVVQLTVGPELFYTFLRLLEETGYFNASLYTPFGIAGVETL
GYEIVEQCRERIGKDPDAVVVTNAGGGNLTGTARGLRKAGAEDTKIIGASVDLSGLHMASDRDFNRKSFT
TGHTGFGVPFATWPDRSDVPRNAARPLRYMDRYVTVTQGEVFYMTEALAQLEGLERGPAGNTSLAAAFAL
AQEMDEDQIIVVQETEYTGAGKHPQAQLTFAKENGIEVRRGDPKEEVPGKSIIIPEHPEQIKAKDLDLDK
LRQSYIKNAVKNLGVKTLTEVDIDFLAEETRTDKEFVRSLLAEL
>gnl|CDD|468706 NF040742, racem_Orr, ornithine racemase Orr. This type of ornithine racemase occurs in an operon for anaerobic oxidative degradation of L-ornithine as occurs in strict anaerobes such as Clostridium sticklandii. The enzyme from C. sticklandii was shown to act on the basic amino acids ornithine, lysine, and arginine. Additional close homologs, outside the family defined by this HMM, likely have similar activity profiles, but occur in different genomic contexts and would not receive the gene symbol orr
YPRIEIDLNKLRHNTKTIVDLCKKKGIEVAGVTKVFCADPEIVQALVEGGVDYLADSRIENLKKLKDINL
PKMLLRIPMISEVEEVVKYADISLNSELETIKLLSKEAKKQGKIHKIILMIDLGDLREGIFYEDEILDTV
KEILKLKNIKLVGIGTNLTCYGGVIPSEENLGKLVEIAEKIENKFNIKLEIISGGNSSSLYLIENGEMPK
GINNLRLGESILLGRETAYGERIEGTHQDVFKLVAEIIELKEKPSVPIGEIGVDAFGNKPVFEDKGIMKR
AILAIGRQDIDPDSLTPVDSKIEILGASSDHLILDVTDSNKDYKVGDKIEFNLDYGGLLSAMTSEYVKKV
Y
>gnl|CDD|468707 NF040743, ornith_mutase_E, D-ornithine 4,5-aminomutase subunit OraE
LKPNKKLDIEEILKDLEKYRPRRRGWTWRKKVENLKMGPFEYHDVSEPLKNSVPLPAAKYFGNIDPQPDC
VITTEIASGRFEDDIRRMRMAAWHGADHIMVIRTAGQSHFDGLIEGTPEGIGGVPITRKQVRATRKALDL
IEDEVGRPINFHSYVSGVAGPEVAVMFAEEGVNGAHQDPQYNVLYRNINMVRSFVDAAEAKKIMAWADML
QIDGAHNANATAREAWKVMPELMVQHAINSMFSVKVGMKKENIALSTVPPTAPPAPCLRLDLPYAVALRE
LFKDYKMRAQMNTKYMESDTREATVTHVLNLLISRLTSADIQSTITPDEGRNVPWHYNNIEAVDTAKQAL
IGMDGLKEMVELKREGPLREKVRELKERAVLFMEEILEVGGYFKAVEEGFFVDSGYYPERNGDGIARKID
GGVGAGTVVERDEDYMAPVCAHFGYNNLPEGDEGVEKPCDLIGGCTLEKPEKIVYIDELDEEDNVNVRLE
ETKEYREGNLIKPEVEWAGDGIVLLTLFLPTDERVAEFAALEIAKKMGLEDPEVIHKEVMHPAEGTRVEL
KGKVPFTIDPDELVIPEKPETLSDDEIRQDVEENPMKVVAATVGEDEHSVGLREIIDIKHGGIEKYGIKY
HYLGTSVPVEKLVDAAIETNADAILASTIISHDDVHRKNMKKLHELCVEKGIRDKVILIAGGTQVTNEIA
VENGMDAGFGRGTKGIHVASFLVKKRREME
>gnl|CDD|468708 NF040744, ornith_Or-4, GlmL-related ornithine degradation protein. Members of this uncharacterized protein family, given the temporary name Or-4, occur as a part of a conserved gene cluster for anaerobic oxidative degradation of L-ornithine. That cluster includes a B-12-dependent enzyme, D-ornithine 4,5-aminomutase. Or-4 is related to but distinct from GlmL, a protein of unknown function encoded next to subunits of a coenzyme B12-dependent glutamate mutase
IDVLVAEIGSTTTVVNAFDGIDTPCPKFLGQGQAPTTVLEGDVTIGLEGAIEDLKENLGEDNLEYSEMLA
TSSAAGGLKMTVHGLVYDMTVRAAREAALGAGAVIKYVTAGKLRRTDLKKIKEIKPNIILLAGGVDYGER
ETALYNAELLAELGLNIPVIYAGNIANQEEVKEIFEEAGKKLYIVENVYPKIDQLNVEPTRKVIQDVFEK
HIIHAPGMEKIREMVNGPIIPTPGAVMEAAKLLYEEIGDLLVVDVGGATTDVHSVTEGSEEIQRILVSPE
PLAKRTVEGDLGVYVNAHNVIELIGEEKLRKEFEEDLEELLENIKPIPKTEEEKKFVERLTKEAVLTAVR
RHAGRIRYLYGPTGRKTVAEGKDLTAVKYIIGTGGALTRLPNGVEILKSIKTLNKSLELLPKEEAKILID
NDYIMASLGVLSKKYPEAALKLLKKSLE
>gnl|CDD|468709 NF040745, accessory_GlmL, methylaspartate mutase accessory protein GlmL. GlmL (glutamate mutase operon protein L), a protein with unknown activity, occurs invariably as part of a locus that also includes the E (epsilon) and S (sigma) subunits of methylaspartate mutase (also called glutamate mutase. A related protein occurs exclusively in a locus the anaerobic degradation of ornithine, where a different cobalamin-dependent enzyme occurs. It seems likely that GlmL is an accessory protein for the methylaspartate mutase
YLLIDFGSTYTKLTAVDLEKEEILATAKAYTTVETDIMEGFNKALAKLEAKQGGKKIEFVKKLACSSAAG
GLKMVAIGLVPELTAEAAKRAALGAGAKVLKVYSYELTRSEIEEIEALKPDIILLAGGTDGGNKEVILHN
AKMLAESKLDCPIVVAGNKSAADEVEEILKDAGKEVVITENVMPKLNKLNIEPAREAIREIFLKRIVKAK
GLDKAEEFIGGILMPTPAAVLKAAELLAEGTENEEGIGDLMVVDIGGATTDVHSIAKGEPTKPGVVLKGL
PEPYAKRTVEGDLGMRYSALSLLEAAGARRLAKYLGLSEEEIDVEEYLEKVNENPEYLPQDEEEKRFDEA
LAKAAVELAVERHAGTLETVYTPMGTVYVQTGKDLTEVKYVIGTGGVLINSPNPAEILKGALFDEDDPTI
LKPKNPEYLLDKKYILAAMGLLAEVYPDAALRIMKKYLVK
>gnl|CDD|468710 NF040746, reduct_C_beta, glycine/sarcosine/betaine reductase complex component C subunit beta. Protein C is the shared acetyl-phosphate-forming component of three types of selenoprotein-containing complexes, acting on glycine, sarcosine, or betaine. Protein C itself has a large subunit and a small subunit (sometimes fused), and does not contain selenocysteine. This HMM describes the large subunit, called beta
PVIKGASYVLVHTPDMLVHNGTTQTTERVKNPDSEYLKNLPNHLRSFEEVVNYPPNQVYIGNITPEELAE
IPRPWYENLLEGASRFGKFGEIMPEDEFYGLMKIVDVFDLVKLEEEFAAEVKEKLAAHPLIKEDDLAKLK
GGVDLSEIEELVENHHAEPLYLGGKLVGCVKRAHDVDENLSAHVMLENLVVKASGVLALLHLLKKTGIDP
EDIDYVIECSEEACGDMNQRGGGNFAKAIAEIAGCVNATGSDVRGFCAGPVHALIEAAALVQSGVYKNVV
VVAGGSTAKLGMNGKDHVKKGMPVLEDCLGGFAVLVSENDGVSPVIRTDIVGRHTVGTGSSPQAVMSALV
ADPLEKAGLKITDVDKYSVEMQNPEITKPAGAGDVPEANYKMIAALAVMKGELERKELPNFVKEHGMPGF
APTQGHIPSGVPYLGHAREDILAGKINRAMIIGKGSLFLGRMTNLFDGVSFIIEKNS
>gnl|CDD|468711 NF040747, reduct_C_alpha, glycine/sarcosine/betaine reductase complex component C subunit alpha. Protein C is the shared acetyl-phosphate-forming component of three types of selenoprotein-containing complexes, acting on glycine, sarcosine, or betaine. A different subunit, B, determines the substrate. Protein C itself has a large subunit and a small subunit (sometimes fused), and does not contain selenocysteine. This HMM describes the small subunit, called alpha
IKKLIAEVFNEIADALETGQFGKKVRIGLTALGSEHGVEELVKGAELAQKADPGLEVVLIGPKVDTGLEW
VEADCEEEAHKKMEELLDSGEIDGAVTMHYPFPIGVSTVGRVVTPAKGKEMFIATTTGTSSTNRVEAMVK
NAIYGIIVAKALGIENPTVGILNVDGARQVERALKELKENGYPINFAESVRADGGAVMRGNDLLAGTPDV
MVTDTLTGNLLMKVFSSFTTGGSYEALGYGYGPGIGEGYDRVISIISRASGAPVIANALEYAAELVKGNL
PEVVKEEFKAAKKAGLEDILASLKPKAAAAAEEEVKAPPKEVVTEEIHGIDVLELEDAVKALWKEGIYAE
SGMGCTGPVVLVAEENLEKAREILKEAGYL
>gnl|CDD|468712 NF040748, reduct_selen_A, glycine/sarcosine/betaine reductase complex selenoprotein A. Selenoprotein A (GrdA) is the A subunit of a complex whose specificity is determined by a different subunit, B, in a glycine or sarcosine or betaine reductase complex. In some species, only one type of B subunit (also a selenoprotein) occurs. Protein C is usually a heterodimer of two subunits called beta (GrdC) and alpha (GrdD), and is not a selenoprotein
LAGKKVIIIGDRDGIPGPAIEECVKTAGAEVVFSSTECFVUTAAGAMDLENQKRVKELAEKFGAENVVVI
LGAAEAEAAGLAAETVTAGDPTFAGPLAGVQLGLKVYHIVEPEIKEEVDPAVYEEQISMMEMVLDVDAII
EEVKKIREEYC
>gnl|CDD|468713 NF040749, tetrathio_RR, tetrathionate respiration response regulator TtrR
MIHLVDDDVAVTDACRFLLESLGYEVQCWNDSEAFLAQADLYQEGVVLLDMRMPGLDGHQVHQALREQGS
TLAVVFLTGHGDVPMAVEQMKLGAVDFLQKPVSAAPLQAALERALAVSAAAFERHQIRQRYQSLTPKERE
IAGLVVQGLMNREIAEALNIAVRTVEVHRARVMEKMAAGSLAELVSQLQQL
>gnl|CDD|468714 NF040750, tetrathio_HK, tetrathionate respiration histidine kinase TtrS
PAQAAEWTIGVLALRGDASTQSHWQPLVDTLNQQLPGEHFQLQPLDLNQMREAVNQGRVQFVLTNPAQFV
QLNSHYPLRWLASLRSSHEPDATRNVIGSVILVRRDSDITTPQDLIGKTVGAVDPDAFGGYLLGYKALRD
AGLRPEKDFRLRFSGFPADALLYLLRERAIQAAIVPVCLLENMDKEGLIDKADFRPLLAKPTSIPCLTST
ELYPNWSFAALPGVPDNLADAVTRVLLNAPDSAMFRWGAPASTSQVEALLRDVNQHPQQRRLWQDVKSWL
IQHRLLIGGILLVLLLLGANHIWVAFLVRRRGRQLEQAHQQLREQEQALEQARQLSILGEMASGFAHELN
QPLSAIRHYAQGCLIRLQREDPQHPLLPALEQIDQQAQRGADTIRNLRLWAGKAPHSEATAWLSQSVRQT
IEHVWQLLRVEQHYPGLTLHTDIDPALTLMLPPTLLEQVLANLILNALQAGATQLWFSAHRDAGRVLLVL
QDNAGGMTAEQLAQAFQPFRSTKSEGLGLGLVICQRLLRSQGGDIALENQIAPDGKNGLRVTLT
>gnl|CDD|468715 NF040755, AgaR, transcriptional repressor AgaR
MKGTSERREQIIQRLRQQGSVQVEDLSALFGVSTVTIRNDLAFLEKQGIAVRAYGGALINDGFIPGAEPS
VEDKSRLNTAVKRLIAAAAAELIKPGDRVILDSGTTTYEIARHLKQHQDVVVMTNGLNVANELLEAEGVE
VLMTGGHLRRQSLSFYGDQAEQSLQNYHFDKLFLGVDGFDLERGITTHNEDEARLNRRMCEVAERIIAVT
DSSKFGRSSLHKIRDTGRIDTLITDSGIPEEYLQGLRKLGVEVILV
>gnl|CDD|468716 NF040756, corr_regen_AcsV, corrinoid activation/regeneration protein AcsV
KVTFKPENKEVEAEEGENLLEAARKAGVFIDAPCNGNGSCGKCKVKILSGKVDSEKSRHISDEEYAQGYR
LACNTKIIGDIEVEVPDIASAFMNGMKIEDLSSERERKIFDRAKKQLEENGIEFKSGLEKDYIELDLPTL
DDNISDFERLKRYLRNKLGYEQVRCRLPVLRKLPDVLRENDFKITVTYRKRGDRITIIDIEPGNTEDVLY
GLAVDIGTTSVAACLVDLYTGEILAKASSGNAQIKYGADVINRIIYSTKKGGLEKLRHAVIEETINPLIE
KMCQEAGISKDDIYRMVAAGNTTMTHLFLGVYPDFLRLEPYIPAFFKSPFLKASDLGLEVNPEAFVYLAP
SVASYVGGDITAGVLASGIWNSEENVLFIDLGTNGEIVFGNKDFMMTCACSAGPAFEGGEISCGMRASDG
AIEAVTIDKETLEPSLSVIGGEKPVGICGSGIIDLICEMFRTGIIDRKGKIIRDLKNKRIRFDEYGIGEY
VLAFKEEYGLGKDITITEVDIDNFIRAKGAIYSGIRTLLNSLGMDFSMIDKVYIAGGIGNGLNIENSIRI
GMLPDIPLEKFHYIGNSSLMGAYLTLMSEEAREKLEEIASNMTYLELSVYPSYMDEFISACFLPHTDIDL
FP
>gnl|CDD|468717 NF040757, AgaW, PTS N-acetylgalactosamine transporter subunit IIC
IAIWAGIAGIDLFDGLTHIHRPVVTGPVVGLILGDLQTGLIVGGTLELVWMGLVPLAGAQPPNVVIGGIV
GTAFAITTKVDPEVAVGVAVPFAVAVQMLITLLFTVFSPVMHKADKMAENANTKGIERVNYLGLLALFVF
YFICAFLPIYFGAEAAKAIVEYLPKWLIDGLSVAGGMMPAIGFAMLLKIMLKKEYIPYFILGFVAVTYLK
LPILAIALAALAIALIDYMRKSSEPSNPTQKEEFEDGI
>gnl|CDD|468718 NF040758, CODH_ACS_meth, carbon monoxide dehydrogenase/acetyl-CoA synthase methytransferase subunit
MDKFMVIGERIHCISPAIRKALAERDPEPILKRAKEQLDAGAHYLDVNIGPAERDGEELMTWGVKLLQEE
FDNVPLALDTANKKAIEAGIKVYNRTKGKPIINSADAGDRIELIDLAAEYDAMVIALCAKEGIPRDNEER
MAYCTEMLERAMMLGMDPEDLLFDPLFLVIKGMQEKQQEVLEAIRQISEMGLKTTGGLSNVSNGAPKHIR
PILDSAFCAMAMQCGLTSAIVNPCDKRLMETIKTCDIIKNNTLYADSYLEL
>gnl|CDD|468719 NF040759, WLP_AcsD, acetyl-CoA decarbonylase/synthase complex subunit delta. This component of the acetyl-CoA decarbonylase/synthase complex, as found in acetogens with the Wood-Ljungdahl pathway, is the corrinoid iron-sulfur protein small subunit, AcsD
FKKSVQKFSGKINEVEIGTGDKAIKLGGENVLPFYSFDGDIGNAPKVGVEISDVYPEDWIDALKELYKDV
ANDPAEWAKFVEEKYGPDFICLRLEGADPNGANKSVEECAEVAKEVAEAIDLPLVIAGCKNHEKDAKLFE
KVAEALEGKNVLFLSAVEENYKAVGAAAGLAYGQKVGAESSVDINLAKQLNVLLTQLGVKNENIVMNVGC
AAVGYGFEYVVSTMDRIRLAALGQNDKTLQMPIITPVSFETWKVKESVATEEDAPEWGSQEERGIAMEVS
TAAAVLAAGSNAVILRHPKSVETIKKFIKELV
>gnl|CDD|468720 NF040760, AgaE, PTS N-acetylgalactosamine transporter subunit IID
MASNAQTLPQASAADETLVSGVNDNVYEDQSIGAELTKKDINRMAWRSMLLQASFNYERMQASGWLYGLL
PALKKIHTNKRDLARAMKGHMGFFNTHPFLVTFVMGIILAMERSKQDVNSIQSTKIAVGAPLGGIGDAMF
WLTLLPICGGIGASLALQGSILGAVVFLVLFNVVHFGLRFGLAHYAYRMGVAAIPLIKANTKKVGHAASI
VGMTVIGALVATYVRLSTTLEITAGDAVVKLQADVIDKLMPAFLPLVYTLLMYALVRRGWSPLRLIGITV
VLGIVGKFAHFL
>gnl|CDD|468721 NF040761, AgaF, PTS galactosamine/N-acetylgalactosamine transporter subunit IIA
MIGIILTGHGGFASGLESAVEQIIGEQPQFIAIDFPESMSTAQLEAQLEQALAELDSGEGVVFLTDLLGG
SPFRVASTLALQRPNIEVITGTNLQMLLEMLLERDGLSLEEFRDQALECGHRGITSLADELQKKREAEEE
EDGI
>gnl|CDD|468722 NF040762, Hydr_FeFe_Clost, ferredoxin hydrogenase, clostridial type. Members of this family of hydrogenases share full-length homology with many other iron-only hydrogenases, but differ in transferrring electrons only to ferredoxins (EC 1.12.7.2) and not to NAD(P)+
KTIIINGKEIEVEENKTILKVAKDNNIDIPTLCYLKDCSNIGKCGVCLVEIEGKEELVRACSTKVEDGMV
IRTNSERVQEAVKERVSELLDKHEFKCGPCKRRENCEFLKLVIKTKARASKPFLPEDKEEYVDDRSKSIV
IDRSKCVLCGRCVAACKEKTGTESIKFIDKNGERIVGTEDDKCFDDTNCLLCGQCVAACPVDALSEKSHI
DRVKEALEDPNKHVIVAMAPSVRTAMGELFKMGYGVDVTGKLYTALRMLGFDKIFDINFGADMTIMEEAT
ELIERIKNNGPFPMFTSCCPGWVRQVENYFPELLDNLSSAKSPQQIFGAASKTYYPSISGIDPKDVFTVT
IMPCTAKKFEADRPEMENDGLRNIDAVLTTRELAKMIKDAKIDFANLEDSEADPAMGEYTGAGAIFGATG
GVMEAALRTAKDFLENKDLENIEYTQVRGLDGIKEATVEIGGKEYNIAVINGASNVFKFMKSGKMDEKQY
HFIEVMACPGGCINGGGQPHVNSKDREKIDYRKLRASVLYNQDKNLPKRKSHENPALIKMYDNYMGKPGH
GLAHELLHFKYK
>gnl|CDD|468723 NF040763, FeFe_hydrog_A6, NADH-dependent [FeFe] hydrogenase, group A6
VNLTINGKEVEVPEGTTILEAAKKAGIKIPTLCYLKDINEIGACRVCVVEVEGARNLVAACATPVAEGMV
VKTNTPRVREARKTVLELILSNHPQDCLTCVRNGNCELQKLAAELGIREIRYEGGEEKSYYIDDTSSPSI
VRDPNKCILCRRCVTVCNEVQGVGALGAVNRGFKTVVGPAFGKPLADTACTNCGQCIAVCPTGALTEKDN
TDKVWDALADPDKHVVVQTAPAVRVALGEEFGLPPGTIVTGKMVAALRRLGFDKVFDTDFAADLTIMEEG
TELLDRLKNGGVLPMITSCSPGWVKFCEHFYPDLLDNLSTCKSPQQMFGAIAKTYYAEKMGIDPKDIVVV
SIMPCTAKKYEAARPEMSVDGYPDVDIVLTTRELARMIKEAGIDFANLPDEEFDNPLGESTGAGVIFGAT
GGVMEAALRTAYEVLTGKELEKVDFTEVRGLEGIKEATVDINGTEVKVAVAHGLGNARKLLEKIKAGESD
YHFIEIMACPGGCIGGGGQPIHTGNVDVRKKRAKALYEEDKNKPLRKSHENPAIKKLYEEFLGEPLSHKA
HELLHTHYTKR
>gnl|CDD|468724 NF040764, CODH_ACS_al_bet, acetyl-CoA decarbonylase/synthase complex subunit alpha/beta. Members of this family have both alpha and beta regions. Proteins scoring between 400 and 800 have only the C-terminal (beta) region
IRGAIKAVSRAEELLKEAIAKYGPDQPVGFPDTAYYLPVIYALTGKKVETLGDLKEALNRARSLLIVWLP
YLGNALDAGMATLFAAEIIEALKYLEGPDPYEAPYGEIWTGFIDDAILRKLGVPLVDGTIPGFAVIVGAA
PDSEEAAKIIKELQKKGLLVFLVGEIIGQLLEAGVKMGWDTRLVPLGPDITSVIHAVNFAIRAALIFGGV
EPGDYEELLDYTKERVFAFVNALGEVDDEWVAAAAGAINLGFPVITDTDIPEIEPTGYEHVVSQVDYDKI
VQTALEVRGIKITVTEIDIPVAFGPAFEGERIRKDDMYVEFGGGKTPAFELVRMKEMDEVEDGKIEVIGP
DIDDVEEGSRLPLGIVVEVAGRKMQEDFEPVLERRIHHFINYIEGVMHVGQRDIIWIRISKEAVEKGFRL
KHIGEILYAKFKQEFPAIVDKVQVTIYTDEEKVKELLEEAREIYAKRDERLKGLTDESVDTFYSCTLCQS
FAPSHVCVVTPERLGLCGAVSWLDAKAAYEIDPTGPNQPIEKGEVIDEVLGIWEGVNEFVYKASQGAVER
VNLYSIMEDPMTSCGCFECIAAILPECNGVMIVNREFSGMTPCGMTFSTLAGMTGGGVQTPGFMGHGKHY
ITSRKFISADGGIARIVWMPKELKEELRERLNKRAEELGLEDFIDKIADETVGTTEEEILEFLEEKGHPA
LTMDPLM
>gnl|CDD|468725 NF040765, adhesion_FAF, adhesion factor FAF. FAF (Finegoldia adhesion factor) has firstly been identified and characterized in the opportunistic pathogen Finegoldia magna. FAF mediate bacterial adhesion to hosts through interactions with the basement membrane protein BM-40
MKLNKKLLTAALAGALIVTAVPANTFAAENAPEISYTYLLNLSKEQAAAKIAELSAEIKELSARRAEIVA
QPWASELTSEGLIEKLQAEEAAAKKAYEAAKAAYEAATKAWEAAKDAQEKARLAKIKADDAADAKQGEYY
KAVKEAEKERDAAKKAAKEAYETTIANLQRKFESATAAADKALIELNAAKKALESAKKSGSNEEQLTRLR
KEVEEKELAHEQAKNLYDAEAAKASDERADAKNGAKEALAAAENQADENFQAKKQYLNKKYILSDGWNGS
AAELTKLERERLKAIDAYNNAVANTKAAHDAYISARDAYDAASKAYAAANQRTYKVTEELKSIEKQLKEN
YVTINAILKDQNKGINSLADQLNAELIKEIEEFAKLSSSEQAAKIAKLQEELNKLKEEYAKTKDEIKEVK
SVYTYKFAVKDTAGKGVQGLTLRFTNIEDTSKVYTATSDENGDIVVKGIVEGTYKIAVTKVPTGYKVVQK
GKMVSEVKALFRPEAEVKAENNAEETKKEEAKKNKRVDIPEIVTIKGNKEDKKDDKKDEKVIDGGTIVVE
KEKKDNKDNKKPEKEDNKKPEKKEKENNKKPAKPAKQRKKLPKAGAAAEAATIAAAAMATMGGAYLSLKK
RK
>gnl|CDD|468726 NF040766, CODH_aero_grp5, aerobic carbon-monoxide dehydrogenase large subunit, group V
TTRLFGEPVARREDPRLLTGNGRYLDDLGHGALAAAFVRSPHAHARIVDIDVSDALDVDGVVAVYTYEDL
PGPMAEPLPLLIPHPALTHGRTGYALAKDEVNHVGEAIVMVVATDRYVAEDAAARIRVDYEFLPPVVGIE
AARAAEHLVHDDVPGNVAAHLVQEVGDAEAAIAAAPHRLELDLDIERSASMPMEGKGVYARWDADDGSLR
VYSSTQTSTSVRAAVAAKLGLPLAKVEVIAPDVGGGFGVKIVHPWPEEVLVPWAARALGRPVKWTEDRRE
HFISSAHERGQLQHVRVGFDDDGRLLGLDVTFWHDNGAYTPYGIIVPIITSTQLLGPYKPGAYRVEFESL
YTNTVIVTPYRGAGRPQGVFAMERTMDAIAAYLGLDRTEVRAANFIQPDEFPYDHGLTFQDGRPLIYDSG
DYPASLDKLKELVGWDGFEAYRAEAAAEGRRVGIGLACYVEGTGVGPYEGGHVQVETSGKVKVATGLTTQ
GQGHQTVFAQIVADELGVPIEDVEVTTGDTRRFGYAVGTFASRAAVMSGSAVALAARKVREKALRIAADA
LEADPDDLEIVDGVVRVKGTPGASIPLGTVAVLSNPLRYAFDEAAKAATQFAGPGDPDKPPVAEGDEPGL
EGRDYYSPPRSTFASGMHAAIVETDPDTAEIRILRYAVVHDCGTLINPMIVEGQIHGGVAQGVGGALYER
MAYDEHGQLLNASFMDFLMPYATEVPHIETDHLETPSPLNPLGIKGAGEAGVIPVSAVIASAIEDAEGFP
ITRMPISPSELFELR
>gnl|CDD|468727 NF040768, Epx, enterococcus pore-forming toxin Epx
GTTTTEKDENGNIKTIITVKNRQIESYNSTDSGTTKNNSSVTVNANFLNDKYSNELTTILSLNGFIPSGR
KFIFPPNNTWSGSMLWPKKYSTTVVNISLDKPVKIINSTPNNTIRNKEVSDSITYGIGGGVKIEGKTPGA
SLDANAAFTKTISYQQPDYETSKTKGTTKEAVWDTSFTETTDGYTRNSWNPVYGNQMFMYGRYTYSVKNN
FTPDYQLSSLITGGFSPSYGVVLKAPKNVKKSRIKVVLSRRSETYQQEWSGFNWVGRNFLDQSNSDWSSN
VTLTFEIDWENHTVKFI
>gnl|CDD|468728 NF040769, SelL_rel_redox, SelL-related redox protein. Members of this family are related to the C-terminal region of selenoprotein L (SelL), found in many non-mammalian animals. But while SelL itself has a pair of selenocysteine (U) residues (e.g. XP_029705782.1), typically in the motif ULPU, this family is defined more broadly. Most members of the seed alignment for this HMM are bacterial proteins that have one or zero selenocysteine residues, and are shorter than SelU, although SelU members are also included
KTAPEVELLDPDGTLVRLLEFLPQGPLLLVFLRHLGUIPCREHLAQLREHQEEFAARGCRVLVVSFASPE
FAEKYLERTWLSWPLVVSDPDRKLYRAFGLKRATFLELWGPKVLVGYLRALLKGGNFYGKPGGDILQLGG
DFILDRDGRILFAHRSRDPADRPSVADLLAAL
>gnl|CDD|468729 NF040770, hetero_SS_HdrA2, CoB-CoM heterodisulfide reductase HdrA2. HdrA2 represents a distinct subclass of the HdrA family, which is the A subunit of the CoB-CoM heterodisulfide reductase. HdrA2 from Methanosarcina acetivorans. A distinctive feature is a MvhD-like C-terminal domain, where MvhD is the signature delta subunit of the F420-non-reducing type of hydrogenase, Mvh
RIGVYVCHCGLNIAGVVDVEAVAEYAKTLEDVVLARDIQFMCSDSGQEQIKKDIKEHKLDRVVVAACSPR
LHEPTFRRVLEKAGLNPYLLEMANIREQCSWVHMDDPQMATQKAKDLVRMGVARARLLEPLEEKTIPVNR
DVLVIGGGVAGIEAALDLADAGYKVYLVEKEPTIGGKMALLNEVFPTNDCSICVLAPKMTEVGNHPNIEL
LTLSEVTEISGSVGNFTVKVLKKPRYVDEDKCKGCIDDCSSVCPVEIPNEFDYGLGKRKAIYMPFPQAVP
QVAYIDMEYCVGCGLCVLACPADAIDFEQKEEEFEFEVGAIIVATGYDVFDASRKEEYGYGRYPNVITNL
ELERLLNASGPTGGRVVRPSDGKVPKSVAFIQCVGSRDEKVGNPYCSRVCCMNSIKNAQLIKERYPDTEI
TIHYIDIRAFGEMYEEYYTRAQEMGVDFIRGKVAEIIEDEDGNLILRYEDTLEGEVREEEYDLVVLSVGM
EPNKDAEVIQRMLNLSRRPDGFFMVAHPKMRPVDTHTKGVFLAGCASGPKDIQDSIAQASAAAARAMILL
SKGELEVDPITAHVDEEKCIGCGICEDVCPFNAITVDNGKAVVDEAACAGCGTCSAACPADAIDMRHFTD
EQILAQIDAATEVKSEFPLIVAFLCNWCSYAGADLAGTSRIQYPTNVRIIRVMCSGRVDPEFVLEALKRG
ADGVLVAGCRLGECHYIDGNYHAKKRMEALKKVLEEIGIDPERLRLEWISAAEGERFAKTIEEFVEELKK
LGPIGSE
>gnl|CDD|468730 NF040771, AAH_UGLYAH2, bifunctional allantoicase/(S)-ureidoglycine aminohydrolase, UGLYAH2 family. The UGLYAH2 family acts primarily as allantoicase (allantoate amidinohydrolase, EC 3.5.3.4), while unrelated to the AllC family of allantoicase enzymes. It belongs to a broader family of enzymes with (S)-ureidoglycine aminohydrolase activity (EC 3.5.3.26) carried out at the same active site. However, Puggioni, et al. consider that activity secondary, as (S)-ureidoglycine is an unstable compound expected only as a product of allantoate amidohydrolase (AAH) activity, and AAH is nearly always absent when UGLYAH2 is present. UGLYAH2 is an acronym for (S)-ureidoglycine aminohydrolase type 2
YYAPPGGLPPQTDLLTDRAVFTEAYAVIPKGVMRDIVTSFLPFWEGTRAWVLARPLSGFAETFSQYIMEV
APGGGSDRPEPDPGAEGVLFVVEGELTLTIDGEEHELTPGGYAYLPPGADWTLRNGGDAPARFHWIRKAY
EPVEGLDAPEAFVTNERDIEPTPMPDTDGAWATTRFVDPADLRHDMHVNIVTFEPGGVIPFAETHVMEHG
LYVLEGKAVYRLNQDWVEVEAGDFMWLRAFCPQACYAGGPGPFRYLLYKDVNRHMPL
>gnl|CDD|468731 NF040772, double_cubane, double-cubane-cluster-containing anaerobic reductase. This subfamily of double-cubane proteins occurs strictly in anaerobes (facultative or obligate), such as Escherichia coli and Clostridium difficile. The enzyme always co-occurs with an accessory protein, an ATP-dependent activase. The cofactor contains a pair of 4Fe-4S cubane clusters, bridged by a sulfur atom, for an overall 8Fe-9S cofactor structure. However, we observe that that this family essentially always co-occurs in bacteria with SelD, the selenium donor protein required for biosynthesis of selenoproteins, selenouridine-modified tRNAs, selenium-dependent molybdenum hydroxylases, and selenoneine
FDEARKEGFLAEKEEKEEGKKVVGTFCTYVPEELILAAGAIPVGLCGGSQEPIPAAEKVLPRNLCPLIKS
SYGFALTDTCPYFYFSDLVVGETTCDGKKKMYELLAELKPVHVMELPQMKDEEAALALWREEVRRLKERL
EELFGVKITDEKLREAIKLVNRERKALKRLYELRKLDPPPISGLEDLLLLFQIAFYFDPERFTELLEELC
DELEERYEAGGGVAPKGAPRILITGCPMGGPNEKVIRLIEESGGVVVAEENCTGTRYFEDLVDEDLEDPL
DALAERYLKIPCSCMTPNTGRLELLLRLIDEYKVDGVVDVTLQACHTYNVESYKVKKFLKEKGIPYLHIE
TDYSESDVGQLKTRIEAFLEML
>gnl|CDD|468732 NF040775, endonuc_Nei2, endonuclease VIII Nei2
MPEGDTVFRTAAKLRDALAGKTLTRCDIRVPRFATVDLTGQVVDEVLSRGKHLFIRVGPASIHSHLKMDG
SWRVGRRPRRPDHRVRIILEAADVRAVGIDLGVLEVLDRARDMDVVAHLGPDLLGDDWDPEVAAANLIAD
PDRPLAEALLDQRVLAGVGNVYANELCFVSGLLPTTPVGAVADPLRLVSRARDMLWANRSRWNRTTTGDT
RRGRELWVYGRAGLPCRRCGTPIERDTSGERVSYWCPSCQR
>gnl|CDD|468733 NF040776, AlsR, transcriptional repressor AlsR
GLALAPKIRMKLEGMTNTESRIVEWLLSPGNLNAKTAIKEVAEALGVSEAMIVKVSKLLGFSGFRELRSA
LVEYFSELEQVITAELSSDDSPQDVVNKVFNISLQTIMEGQSILDPDVIAEAARCFFKAKQRDLYGVGGS
NTICADIEHKFLRIGIRCNAYSDAHLMMMSASLLQEGDVVLVVSHSGRTSDLLKAVELAKKNGAKIICIT
HSDHSPIAQLADFVICSPAPETPLLGQNASARILQLTLLDAFFVSVAQQDIEQAEENLEKTSTIVAYFR
>gnl|CDD|468734 NF040779, Sec_lyase_SclA, selenocysteine lyase SclA. In bacteria, selenocysteine lyase activity (EC 4.4.1.16) usually is seen as a secondary activity of a cysteine desulfurase (EC 2.8.1.7). However, SclA, as studied in Enterococcus faecalis, acts primary on selenocysteine, binding cysteine just as well but acting on cysteine with much lower catalytic efficiency
VYLNHAATSNHKFEATIQALCAYLQENNNLNTNRGLQGLDELGLAFETRQALADFFHAPDPAHVIFTANA
TTSLNMVLNGLLKPGDHVLTTSVEHNAVARPLHLLETEQNVSVTYLPCEKDGQLDPEQIEAAIRPETKVL
VMTHASNVLGTILPVKECFKIAKKHGIITVLDSAQTAGFLPIDMEEMSIDVLAFTGHKSLMGLAGIGGFA
LAKNIEKKIDPWLTGGTGSASLSLEQPDFLPDKFEPGTPNTLGILSLKSSVKAIQELGLEKIQAHERALT
ARFLTGLKELPVTILGTKDAAQSVPVVSITAPGIDSGELAQQLFDRYGIITRSGLHCAPLAHQTAGTLKT
GAVRFSFGWNTTAEEIDYTLSALKEILS
>gnl|CDD|468735 NF040782, PG_glutam_Chrys, protein-glutamine glutaminase. This HMM describes full-length protein-glutamine glutaminases that share end-to-end homology with the founding member from Chryseobacterium proteolyticum, can hydrolyze amino groups from the glutamine side-chains of proteins. Pfam model PF18626 identifies a central region, about one-third the length of this model, that includes the catalytic triad Cys-His-Asp
MKKNLFVLLVMSVALLFCSCSNGDHNEMEKSIQTTTFELIKKQIGNLVPNGIEVKGDQARISFHLSAQLY
SITLTDENSQFIEYIKKAMRDESPLEISIKNNSKEIGKVSESPDEDINFFKGNITPLVKREAAANRLDGW
IPDISTLNDLFAEIRNQSCTTTASSPCINFDYPVDGCYARAHKMRQMCNRMGYECDKVFVYGSLRATSGK
FDCCVSWRYHVAALVYVKYGDGVLQMMIIDPSLPYTYPITDEEWRNACTNSTCGGYSESSYTATPGNVYY
RSNGGQLLYDDLYVNTDCTLDMFKNASGCSAPVPSTAHCGF
>gnl|CDD|468736 NF040785, CD3324_fam, CD3324 family protein. Members of this family include CD3324 and CD1583A from Clostridium difficile and YraL from Bacillus subtilis. Members show stretches of sequence homology to Mor, which is a transcriptional activator from phage Mu, and to other members of Pfam model PF08765
YINAKDILPEELLEEIQKYIDGEYLYIPRKEENRKKWGENSGSRKELKERNKEIYKKYKNGISIEELAEK
YFLSEKSIRKII
>gnl|CDD|468737 NF040786, LysR_Sec_metab, selenium metabolism-associated LysR family transcriptional regulator. LysR family transcriptional regulators regularly appear encoded adjacent to selenecysteine incorporation proteins such as SelB. This model represents one especially well-conserved subgroup of such transcription factors from species such as Merdimonas faecis, Sellimonas intestinalis, Syntrophotalea acetylenica, and Hydrogenivirga caldilitoris. Seed alignment members were selected by proximity to selB, but not all family members are expected to have similar genomic locations
MNLKQLEAFVNVAEYKSFSKAAKKLFLTQPTISAHISSLEKELGVRLFVRNTKEVSLTEDGKLLYEYAKE
MLDLWEKLEEEFDRYGKESKGVLRIGASTIPGQYLLPELLKKFKEKYPNVRFKLMISDSIKVIELLLEGE
VDIGFTGTKLEKKRLVYTPFYKDRLVLITPNGTEKYRMLKEEISISELQKEPFIMREEGSGTRKEAEKAL
KSLGISLEDLNVVASLGSTEAIKQSVEAGLGISVISELAAEKEVERGRVLIFPIPGLPKNRDFYLVYNKN
RQLSPTAEAFLQFVKERY
>gnl|CDD|468738 NF040787, S-lay_SlaA_Mtsph, S-layer protein SlaA
MNEKAIRYLSILLVFLMGGSFLLGVVPQAQTSSTAGGVTISASSEWVGPGQVVLVAVYNPNVPQSAIGAK
YVLGNITVTNGTVTLPLNSFNLTNLSTVYYLQNGGHYFWFFITMTPTSTTSSNHVTETPGLTINSTLTNV
NLTNPYLTLNSGTLGVFQFTLPSSFPNNLTSNYGQTVSGGGYVNVTNLYYFSSSKTITISYSTGASVTIN
NYLANSSNYSPTLTSSESTVPLNSTWEVFFNDSIMQANPLVGGNGGFSVTVNGETPNPVIQNVSYVAIMN
GVYVNTTVFADNPISNALAMFGYGNVYNGNFTMYTSSVVTNKTYATLTPGNTYSPSYVTGSQYYNLINRD
RLFTTNTPITIYVSDWLGNNASVSVTGTIKETTPQSFSLSVQKGENLTVNAFDNISNFSVTESIHVYVSL
QSSSGSTFSSAQVRLNETYAGSGVFSLPTVLEIGSSPSIGITSSPNVTITLPPYDFSNTTILITATNDIG
ASFYYLGSTTPKNISTPGTIAVGTPSLVPIPNVVSVPNVTPVIELAYYEPNLAFGTATTLTVSGGSISYN
GVPVATDSVTYVLPNGTSITTNLNALGITRLTSANGNGTFFIVVPRTAILTLLGLSYIPSGTQLTFKIYD
EFAAQTLTVTYTFQTIAPVITIETPTSTSFSSSETAYLPPLPYNVLPEKHYINVNVTDQLYAQSVPSSAL
QATLKIIVENPAGKSVKVTSPTTVTITETSPGTGLFTGSIYYTVTYNSGTYYLSINGQNITNLKNVVNGG
LLVFEYTSPSSNQTVNATVTLKPSPFTLTVNQTSANPGQKVNVTVNSPGLVEGSNMKYTGSLKIYAQYVE
WNGYTTPTVVTSPITLKEVSAGSPVFGGTIVLGNSSVVSSGNLTSLITTSGYTVAPGSVVLVNANATIGP
TSTSSSITPYYQQQTISINVPDVNVSILNPSPASPFAKLEIELNSSLFNLLSHPAPGNYTSISSSEASTL
LENQISTITTQQSQQLITGSQLISSPKTSFYYNNSIWIITVPMTLWSGTPGSYGIPLNVNLTDLVTVTHN
VYSIHVVEVPNVTTGTVSIVSAYAVPSVSSQVATLQINGLVPPVISVYFNGNNITQSASGAVPFPNTTAG
ELVNITVYAPDAVLNPNVPGTGTTFNVTIVNTANGETTTLTLTQMTKIVSGVAVPTPYYTGLLKVVEPTV
YTPGVSGEISASPGLVNKVLVNMNVVEGTYFNYQGLLQQLTMKASSYFYVGVIKLSVLVSHFTLTLNGTP
VTSMQVGKSYSILFNITDNGNVNETIYGTLEVLLNGTPVQPEVIAQVTLAPGQSTQVGTLFTPTMPGNYT
IVFIPFQNNLLSIPYNQGLTEVVSAS
>gnl|CDD|468739 NF040788, S-lay_SlaB_Mtsph, S-layer protein SlaB
MKYNFLPLILLVLLVVPLLAFGSATPITVTTQPVYHPGQTVFIEGTTSPNTLVGVTIYNPQGKAVYSNTT
TSNANGAYSLKAFTFPSQPTTTLPYGTYTVQVGTSTGFTNSTTFQFLPLTATVNVLVVNPQGVPVSGATV
TADSVSAVTNSSGQAVLSLPTGTYTLKVVPPAPYAPASENITVVAPQTYSFKVTVQIQELALTVVKAISP
NVNLQDLTSGTGITMVGGTTLTVMSTVTFAGQPVSTATVTAMYNGTTYTATYMNGYYVINITVPNVQYET
DLVITATYSGMTSNTVTLPLTVNLNEQAIISSLNATLSSLETQLSSLSSTVSSLSSTVSSLSSTVSSLST
TLSTLNSTVTSLQSSVSTLNSEYTTLNSRVNALSGLSGTVDIALAVSIIAIIISIVVLILVFRKIS
>gnl|CDD|468740 NF040789, gerfarn_diphsyn, geranylfarnesyl diphosphate synthase
MDVTEILKKYSEDIDAEIEESLSTIDPEELQEASIHLTKAGGKKLRPALTLLSCEAVGGNEEDALKTAAA
IELIHTFSLIHDDIMDDDDMRRGKPSVHVVWGEPMAILAGDTLFSKAFELVLETKEDNVSYERVVEALAT
VADACVKICEGQALDMGFEGRFDVTEEEYLEMIYKKTAALIAAATKAGAIMGGATPEQIEALYEYGRLIG
LAFQIQDDYLDLVSDEESLGKPVGSDIVEGKMTLMVVKALEKASEEDKERLIEILKAEDQEDVDEAIEIF
EKYGSIEYAKNVALEYVNRAKELLDILPDSEAKEALLKLADFVLERKH
>gnl|CDD|468741 NF040790, glucon_galact_dh, bifunctional D-gluconate/D-galactonate dehydratase
MKIKEIEPIVLGSKEEKSAPWASTMILVRVVTSDGRVGYGEAVTTLRVLPVKESIKEVSRVFIGKDVFNI
EKNYREWYKQDFYLSRSFESTTALSAFDIASWDIIGKELGAPIYKLLGGKTRDKVRVYANGWYSDCVTPE
DFAEKAKEVVKRGYKALKFDPFGPYFDWIDEKGLKEAEERVKAVREAVGDDVDILIEHHGRFNANSAIEI
AKALEKYNPLFMEEPVHPEDIEGLRKYRSYTSVPVALGERLINKKEALRYISEGLVDVLQPDLTNIGGIT
EAKKVAAIAEAFGVEVAFHNAFGPVQNAATLQLDATIPNFLIQESFYDWWPQWKRDLVYNGTPVENGYVK
VPGKPGIGVEVNEKLLEELKVEGMEPFVPEEPVWVVKGTW
>gnl|CDD|468742 NF040791, gly_kin_Thpl, glycerate 2-kinase
AVNNINDIATNDRRKFILKIIDDTLQDLEPENAINNAFNVDINKYKRVYVIGFGKASFEMYSGIRPHVLK
KLRYAGIIVPDDEVVHNFPELRILRGTHPYTSSLSVSSSIKLLSKLKNLNENDLVIVLISGGGSSLFEIP
EDGITIDDIKEISKEMMDSGGDIYELNTIRSGLSSVKGGKLAKYLYPASVISYIISDVPYDDLSIIASGP
LVRNDYDPDDVYEISRKYIKNDDFIEKNYRNNSIDDKYFRNVKNRIILKNRDFVDYIYSNLDEPIVSLGS
NINGDVEDVSNYLINILRNIYSIKGKSFWFVCGGETTVNVKGNGIGGRNLELALRFMKLYNNSDFLFLSI
GTDGIDGVSPAAGGIVDNDTKIDNIDEYLKNNDSYTLLSKYHGAIMTGRTGNNVSDIILG
>gnl|CDD|468743 NF040792, glyc_ald_dh, D-glyceraldehyde dehydrogenase
MKIYIDGQWVDSSSGKTLDKYNPVTGEVIDTFPAATKDDVDRAIDAAEDAFWKWNDLGSVERSKILYKAK
ELIEKNRKELENLLMLENGKIKREAKEEVDGVIDQIQYYAEFERKLNGDIVEGTSSKRKIFQYKVPYGIV
VALTPWNFPAAMVARKLAPALLTGNTVVLKPSSDTPLTAEWIVKKFIEAGVPKGVLNFITGKGSEIGDYI
VEHKKVSLVTMTGSTSTGQRIMQKASANMAKLILELGGKAPFIVWKDADIERALKTLVWAKYWNAGQSCI
AAERLYIHEDIYDKFMKKFVEVTKRIKVGDPETADMGPLINKSALKNTEKVVEEAKESGYKILLGGSKPD
LSGKYKNGYFFEPTIIENVPQKSPIFQEEIFGPVIGAEKVSDVDEMYRKANDSKYGLASYLFTEDPELIF
EASEKIRFGELYVNMPGPEASQGYHTGFRMTGQAGEGSKYGINEYLKLKNVYVDYSRKPLKINTVRDD
>gnl|CDD|468744 NF040793, sarcosine_GrdG, sarcosine reductase complex component B subunit alpha
MKLELGKIFIKDVQFGEKTEVKNGVLYVNKQEIEDLVLEDDRLKSCNVELARPGESVRITPVKDVIEPRV
KVEGEGEIFPGVIGKVKTVGSGRTHALDGACVVTVGKIVGFQEGVIDMSGPAAKYCPFSKTNNVCVVIEP
KEGLETHVYEKAARMAGLKVAAYLGKAGRDLEPDEVEVYETKPLLEQAAEYPDLPKVGYVHMLQSQGLLH
DTYYYGVDAKQIVPTFMYPTEIMDGAIVSGNCVAPCDKVTTYHHLHNPVIEDLYKRHGKDLNFMGVILTN
ENVFLADKERHSDMVAKLVEFLGLDGVLITEEGYGNPDTDLMMNCRKCTQAGAKVVLITDEFPGKDGKSQ
SLADACKEADAVVSCGQGNLVIHFPAMDKIIGTLDYIEMQIGGWKGCLNEDGSFDAELQIIIASTIANGF
NKLAARGY
>gnl|CDD|468745 NF040794, sarcosine_GrdF, sarcosine reductase complex component B subunit beta
MAKYKVVHYINNFFAGIGGEEKADIKPELREGAVGPGLALQAALGEDYEIVATVICGDNYFGENLDEATD
EILEMIKKYEPDLFVAGPAFNAGRYGVACGTICKAVEEELGIPVVTGMYVENPGVDMFKKDLIIVETGNS
AAGMRKAVPKMAKLGKKLAKGEEILGPEEEGYIERGIRVNYFHEKRGSERAIDMLVKKMKGEEFETEYPM
PVFDRVPPNPAVKDISKVKIAVVTSGGIVPQGNPDHIESSSATKYGIYDITGMDSMSKDDFTTIHGGYDR
AFVLENPNLVVPLDVLRELEKEGVIGELANYFITTTGTGTSTGNAKGFGEDFSKKLIEDGVGAVILTSTU
GTCTRCGATMVKEIERAGIPVVHIATVVPISLTIGANRIVPAIGIPYPLGDPNLGEEDSKKIRRELVERA
LKALQTPVDEQTVFE
>gnl|CDD|468746 NF040795, betaine_GrdH, betaine reductase selenoprotein B
KAILYINQFFGQIGGEDKADFEPEIREGLVGPAMELNKQLEDAEVTHTIICGDNFMGSNTEEAVERILGF
LEDKEFDIFFAGPAFQAGRYGVACGTICKAVKEKFNVPVITSMNEENPGVEMFKKDMYIFKGGNSAAKMR
KDVKAMAKFANKLLKGEELLSAEEEGYFGRGIRHQVWLEDGKPAADRVIDMLLKKLNGEPFQTELPIPKL
DRVPIAPAIKDLSKAKIALVTTGGIVPVDNPDRIQSASATRWGRYDISGMDRLEGGVYKTIHAGFDPAAA
DADPNVIVPLDALRAYEKEGKIGKLHEYFYSTVGTGTTQAEAARMAKEIVPYLKEDGVDAVILTSTUGTC
TRCGATMVKEIEKAGIPIVQMANLIPVAKTVGANRIVPTISIPYPLGDPSTSKEEQWKLRYHRVGVALDA
LTTDIKEQTVFKVKI
>gnl|CDD|468747 NF040796, toxic_TimP, small toxic inner membrane protein TimP. The gene timP (toxic inner membrane protein) occurs within the small structural RNA ryfA. Proteins of the TimP family can be found encoded in Escherichia coli, Salmonella enterica, Citrobacter, and Klebsiella sp
MKIRCFCIVLIVSGALLLHADNNRSYSGNSVLVTLNAQSK
>gnl|CDD|468748 NF040801, spore_GerD, spore germination lipoprotein GerD. This HMM describes the spore germination GerD, as found in Bacillus subtilis and other endospore-forming bacteria. It appears that every member of this family has a lipoprotein-type signal sequence
LLLILLLLLLLTGCGGEQNQSSSQPDYDETKKMVVDILKTDDGKKAIQEVLSDEEMKQLLVMDQEQVKKA
IEDTLTSEKGKKFWKKAFKDPKFAETFAKSMQKENKKLLKDLMKDPEYQKMMIDILKDPEMEKQLLDLLK
SKEYRKQLQKVIQETLESPLFQAKIQDLLKKAAE
>gnl|CDD|468749 NF040808, CspC_non_triad, bile acid germinant receptor pseudoprotease CspC. Members of this family share homology with MEROPS S8 family serine proteases, but with substitutions that replace key catalytic residues, as seen in CD2246 from Clostridium difficile. The related germination-specific protease CspC of Clostridium perfringens, outside the scope of this model, retains its serine protease catalytic triad residues. Adjacent to CD2246 is the fusion protein CD2247, CspBA, in which the CspB region retains its subtilisin-like catalytic triad while the CspA, like CspC, has lost it
EKSYNIIYQGNIEQSLQENGITNFMVLNNQLAVIYVPADFDENILNNINQVAWWEESEPMSSLINITNNL
LQGETVRTASGIAYIYNNPYNNLSGRGILIAIIDSGIDYLHPDFINEDGTSKIVSIWDQESNKKPPPEGM
IFGSEFTREEINEAIKNNNGDLSRDEIGTGTIAAGILVGQGKINSNYKGIAPNAELIVVKLREYIDTFKK
GRINYQSTDFLAAISYVINVAKKENKPIIINFTIGTTSGSVISTSILDTFEELSQSGIVLVSGAGNQGNT
DIHYSGSFNNNGEYQDIIIQVGDDKNLDIIINGYGPDKIGIAIISPSGEISPTISYAPDNYIYAGKFNLE
NTTYSMRYIYPWISSGKEQLKIKLKDIKPGIWTLRLTPEFIINGEYNIYLPNKNLISDNTRFLDPDSNAT
ITRYGLLDNVITVGTYNTKTNSMWIGSSKGPAGGRQIKPDIVAPGVDIISTYLNNTYNTGTGTGVSSSIV
CGVLALIMEYIIKQTEFPRLSLYTEPLKTYLMLGATKKEIYTYPNISQGYGILNLKNTIQQIANNL
>gnl|CDD|468750 NF040809, germ_prot_CspBA, bifunctional germination protease/germinant receptor pseudoprotease CspBA. CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity
IIEYEVIVKYNGDILRLENELNVSVEILSSNYAIITSTTPEDVDRLLDYPEIEYIEKPFILETQDTQSFS
STGITSFKNRTGLTGKGTILGIIDSGIDYTLPIFKDSDGNSKILYYWDQSIDGNPPEGFREGTLYTNEDI
NEAINGNKYIPISTTSMHGTHVAGIAASIANEASIIVVRVGRRQTDTFSKSTEFMRAIKFILDKALELKM
PVAINISYGSNEGSHRGLSLFEQYIDDMCLFWKNNIVVAAGNNADKGGHKRIQLKNDESQEVEFVVGENE
KILNINIWPNFVDNFSVHLVNPSNNQTQEISQDSGEINNNLGGTRINGVFYEIAPYSLSRRVTIQLSSNT
QITPGIWTIVFTPIDIVDGNIDIYLPTSEGLSKDTRFLEPSKILTVTVPGTASRVITVGSFNSRTDVVSV
FSGEGDIENGIYKPDLLAPGENIVSYLPGGTTGALTGTSMATPHVTGVCSLLMQWGIVEGNDLFLYSQKL
KALLLQNARRSPNRTYPNNSSGYGFLNLSNLNLYSLSDNNQDLGTYRREKNLQIKNNLINENRINGAVLF
HNPEFEEELKNFGLEYNFFKLSENLGVLFITDTDISQIGEILKIPSVIRIESLVRMAPLGQISQGTSGGV
VATEDIGVNFFKNNPNINLTGRGVLIAIADTGIDYLHPDFIYPDGTSKILYLWDQTKEGNPPEGFYIGTE
YTREDINRAIAENDSSLSQDEVGHGTMLSGICAGLGNVNSEYAGVAEDAELIVIKLGKIDGFYNNAMLYA
ATQYAYKKARELNRPLIINISVGSNSLAGFTNRTNAEKAYFTRGLCIVAGAGNEGNTQTHASGKISAVGE
SVDVELEIEEDEENLQIEIWMDRPDRINVIIISPTGEESKDVGLSNYDEVSGIFDLENTEYLIRYSYPTS
YSGQQFTNVNLKNAKKGIWKIRLTGVYINSGIYNMYLPNRVFLKPGTKFRESDPFYTINYPAVQDDIITV
GAYDTINNSIWPTSSRGPTIRNIQKPDIVAPGVNIIAPYPGNTYATITGTSAAAAHVSGVAALYLQYTLV
ERRYPNQAFTQKIKTFMQAGATRSTNIEYPNTTSGYGLLNIRGMFDQLR
>gnl|CDD|468751 NF040810, BenC, benzoate 1,2-dioxygenase electron transfer component BenC
YNIALNFEDGVTRFIECNAGETVLDAAYRQKINIPMDCRDGACGTCKCRCESGSYDLGDDYIEDALTEEE
AAQGYVLTCQMVPQSDCVIRVPASSAACKTGQATFEATVAAVEQLSDSTIELSLDLDDDAALAFLPGQYV
NIQVPGTGQTRSYSFSSLPGAREASFLIRNVPGGLMSSYLTERAKPGDRLSLTGPLGSFYLREVTRPLLM
LAGGTGLAPFLSMLEVLAEQGSEQPVHLIYGVTRDADLVEVERLEAFAARLPNFTFRTCVADAASAHPRK
GYVTQHIEAEWLNDGDVDVYLCGPPPMVDAVRGWFREQGITPASFHYEKFTPS
>gnl|CDD|468752 NF040811, BenD, benzoate diol dehydrogenase BenD
RFAGKVVVVTGAAQGIGRGVAERAAAEGARVVLVDRSDLVHEVAAELRAAGGEAIAVTADLETYEGAEAA
MAAAVERFGRIDVLINNVGGTIWAKPFEEYEPEQIEAEIRRSLFPTLWCCRAVLPHMLEQGGGTIVNVSS
IATRGINRVPYSAAKGGVNALTASLAFEYAERGIRVNATAPGGTEAPPRRVPRNAAPQSEQEKAWYQQIV
DQTIDSSLMKRYGTLDEQVAAILFLASDEASYITGTVLPVAGGDLG
>gnl|CDD|468753 NF040813, pro_dh_Thprot, D-proline dehydrogenase
KVVVVGGGVVGLFTAYYLRREGADVVLVEQGEPGHWSRAAAGILEFTRFEINRINVRGYPKRYLKMIRRG
KARIKTWDWKWLLAYLKVYGREPPQEMWEAIKEMGEFSWREYRRLAEEKNDFEYREEPLYEVVVDVEKEV
EELKRDPLRPRFEVGECCGREAIVYLDAAKLSTDLLAERLLRELSGVRIVRARAQEVAGGEVVLEGGKVV
EADAVVVAAGWWARKLGIPVAPFKGYGFRTKAKKRPGAMFIDFVDGVFVVPLSKWVKVTGRFDLDGTEDH
SPSAKVLEAAREWLGNFEVIDMAVGYRPCTPDGLPILEKRGEVVIATGACRLGWTYGPALGKLAADLALG
RRKDTALTARRF
>gnl|CDD|468754 NF040814, tRNA_cyt_mtase, tRNA (cytosine(49)-C(5))-methyltransferase
YKEEFREINLKFYERYSKLDDSEEFWEYMYKPLRQSIRINTLKAPLDEIVKRLKEKFELEPIPWVKEGFF
INSYNYGTLIEHSLGLIFPQEASSMIPPVVLDPKPGELILDMAAAPGSKTTQIAQYMENEGCIIANDAKR
DRANILIANLNRAGVLIAKVTVKDGAYFARFENTFDRILLDAPCSSVGMIRKSFKFAKTWSIGKVYYYSR
IQKKLILAAYKALKPGGVLVYSTCTVDPLENEEVVDFLLQKTDAKLEKIKLPLKSTEPVLEWEGRKYSEE
VKKTLRIHPQDNDTEAFFIAKIRKP
>gnl|CDD|468755 NF040815, recomb_XerA_Arch, tyrosine recombinase XerA
MSVRNEVIEEFATYLELEGKSPNTIRMYTYYVSKFLEEGGSPTARDALRFLAKLRKKGYSNRSLNLVVQA
LKAYFKFEGLDEEAEKLKPPKVPKSLPKSLTEEEVKKILSVIPPTKKRDRLIVLLLYGAGLRVSELCNLK
KEDVNFERGLIVVRGGKGGKDRVVPIPKYLLDEIKAYLESRSDDSPYLFVEDRRKRKDKLSPKTVWYLLK
KYGRKAGVEVTPHQLRHSFATHMLERGVDIRIIQELLGHSNLSTTQIYTKVTVKHLREAQEKAKLIEKLI
GG
>gnl|CDD|468756 NF040816, Fbpase1_Arch, class I fructose-bisphosphate aldolase
MSYQYVGKRVRLSRILRDGRAVIFAFDHGVEHGPGDFPPEHVNPRVIIRKVVDAGVDAVMMLPGIARMTW
DIWKNRVALIIKVTSKTNLRPKEEQLLQSIIGFVEDAVALGADAVAATVYWGSQYEDLMLERWFQIRSAA
ETLGYPCLQLAYPRGPAIKNRYDVEVVRYGARAAAESGADLIKTYYTGSTETFREVVKAAAGVPVLMSGG
AKTENPIDFLKVVWSVMEAGGQGVVVGRNVFQHENPELMIKAIMAVVHEGEDPEEAAKLLG
>gnl|CDD|468757 NF040817, GdhA_Arch, glutamate dehydrogenase
MVEQDPFEIAVKQLERAAQYMDISEEALEFLKRPQRIVEVTIPVEMDDGSVKVFTGFRVQHNWARGPTKG
GIRWHPEETLSTVKALAAWMTWKTAVMDLPYGGGKGGIIVDPKKLSDREKERLARGYIRAIYDVISPYED
IPAPDVYTNPQIMAWMMDEYETISRRKTPAFGIITGKPLSIGGSLGREEATARGASYTIREAAKVLGIDL
KGKTIAIQGYGNAGYYLAKIMSEELGMKVVAVSDSKGGIYNPDGLNADEVLKWKKEHGSVKDFPGATNIT
NEELLELEVDVLAPAAIEEVITKKNADNIKAKIVAEVANGPVTPEADEILFEKGILQIPDFLCNAGGVTV
SYFEWVQNITGYYWTLEEVREKLDKKMTKAFYDVYNTAKEKNIHMRDAAYVVAVQRVYQAMKDRGWVKH
>gnl|CDD|468758 NF040818, GAPOR_Arch, glyceraldehyde-3-phosphate:ferredoxin oxidoreductase
MKFSVLKLNVEKKEVESEEFEKEGVYGIIDYGLYLHDEVYKTYELDPYDPRNVVVFGKGPFAGSALPGAH
RLMFFFRSPLYGTLFPSAMGGAAYQFQHVGVDFVVIEGKAEKPTVIILKNDGENLSVELHEIELEKVIEI
WRGYKGEEGVYALTQYLIDNLGSKFDGMEFRIAVVGPAALNTNYGAIFSQALRNGKRVVGSEDWAARGGS
GSVLLRAHNVVAIIFGGKKRKKEFPGEDISNFKTAKRIVEGVHKKPYNDVITEKTVKYRYNPKLKTGGTF
GGNYPAEGDFVPILNWQMPYIPKEERIKIHENIMKYYWEPFNKEAIEPKNWTTCGEPCPVVCKKHRRGHH
VEYEPYEANGPLSGSISLRASDISVHAVDAMGFDAIEFGGTAAWVLELVHRGLLKPEEVGISDKPEFTKD
ALLEKPVEASEKNAKLVAELAHRVAFAETEIAKIIGLGKRKASKILDEKFKDRLKYGESFKDYAVFTPLG
EDGEITPTMYWAIGNYIPLPIQGRYWTFYQFGVFLEPEELAQKIVASALWEFWYDNVGWCRFHRGWMKPV
LKALFMEAYGENVDMEEHAKKQIRKLINYAKKAGYEPVFWDSMRVIDLVAKGSEEFGNEKWAEKFKEDKV
GTAKEYLKRVLDAYSQLLGVDWTI
>gnl|CDD|468759 NF040819, helicase_HerA, DNA double-strand break repair helicase HerA
EEPYVGIVRGEATFSSYEFSVNPDADLSFGEFVVTKNRDGEWVIGTVRGVKNINWLLSSGKSTFNSLLLD
IEEYGESIGENEELIATVRILGKVKGGGEAELVPNRVPVPNGEFVYKASDDLLRAIYYPGGGSIEVGTLL
LRENVPIYLDVDELVSRHFAVLAVTGAGKSNTVAVMIKGIVEDLGGTVVVLDPHGDYVKLRLPETGRDLV
NIIEAKIRPEELDSEELADLIEVRSNASIQREFLARAWETVKHENQGLGGRELLEKLRDKLNEWISNKGI
KYWDPKEGRYYKLEELKSERKETIRGVIMRIRRFLRNYGALLTSEDLVAAIEPGMVNVIDLGPLDEGQMK
VVVGKFLERVFEARVDYEKARKSLERSSRAEKIEELEKIMREIERKYPALAEPILVIVEEAHIFAPQGEE
NDAVRILGRIAREGRKFGVGLGVVSQRPSKLNEDVLSQTNTKIILRIVNPKDQEYVLRASEQLSKDLMDD
IAGLGKGEAVIVGQAIKLPALVKIYNFKELGGDYGGEDIGVVDRWRKRAEREEAERMKEELYEEEGIDID
F
>gnl|CDD|468760 NF040820, trans_reg_LrpA, HTH-type transcriptional regulator LrpA
MIDERDRIILEMLTKDARTPFTEIAKVLGISETAVRKRVKALEEKGIIKGYTIKVDPAKLGYNLVSITGV
DTKPEKLFEVASKLKEFDFVKELYLTSGDHMIMAEIWAKDGEDLAEIISNKIGKIDGVTKVCPAIILEKL
K
>gnl|CDD|468761 NF040821, dipep_PepQ_Arch, Xaa-Pro dipeptidase PepQ
ERIEKLRKYIDENEIDAALITRNENLFYFTGSSPVLGGYLVVTPDEATFYVPELEYEEAKEESKVPVEKF
KKLDELYEALKRFKSLGIEGSLSYSFVNSLKEKANIKEFKKIDDVIKELRIIKTEEEIEVIEAACKIADM
AMMAAIEEISEGKREREIAAKMEYLMKMNGAEKPAFDTIIASGWRSALPHGVASDKRIEKGDLVVIDEGA
LYRHYNSDITRTIVVGSPNEKQKEIYEIVLEAQKKAVEAAKPGMTAKELDSIARDIIAEYGYGDYFIHSL
GHGVGLEIHEWPRVSQYDETVLKEGMVITIEPGIYIPKFGGVRIEDTVLITENGAKRLTKTERELI
>gnl|CDD|468762 NF040822, lys_aminopep_Arch, lysyl aminopeptidase
MVDWELMKKVIEAPGVSGYEFLGIRDVVVEALKDYVDEIKVDKLGNVIAHKKGSGPKVMVAAHMDKIGLM
VNHIDKDGYLHVVPVGGVDPRTLVAQRIRFFTEKGERYGVVGHIPPHLRKPEDRKKAADWDTIVVDVGAD
SKEEAEEMGFRIGTVGEFAPAFTRLSENRFATPYLDDRICLYAMIEAARALENHEADIYFVASVQEEVGL
RGARVASYAIDPEIGIAMDVTFAKQPGDKGKIVPELGKGPVMDVGPNINPKLRAFADEVAKKYEIPLQVE
PSPRPTGTDANIMQINREGVATAVLSIPIRYMHSQVELADARDVDNTIKLAKHLLEELKPMDLTP
>gnl|CDD|468763 NF040823, deglyc_PfpI, deglycase PfpI
MKVLFLSADGFEDLELIYPLHRIKEEGHEVYIASFKKGKITGKHGYTVKVDLTFDEVDPDEFDALVLPGG
RAPERVRLNEKAVAIAKKMFEDGKPVASICHGPQILISAGVLKGRKGTSYITIKDDLINAGAEWIDKEVV
VDGNWVSSRHPGDLYAWMREFVKLLK
>gnl|CDD|468764 NF040824, damage_ctl_Phtase, damage-control phosphatase
MKVHYECLACAANQCQKIVEMSTEDLEKRKKAMIFAAKLIAEEFNEDSIPAIAGSRLFLELYKFLGNDDP
FKEYKELSNELARKVVEDLKRKLKIDLKTALKLAIAGNVIDFAVGYSPEKIEEDIEEMLKEELYIDESDE
LFEELKRAKILLYLTDNCGEIYFDKLFLEKIREEFPDLEIYIAGKEGPIINDATVEDLKEAGFEEIGKVI
STGTRIVGVPLEYVSEEFREIFEKADVIIAKGQGNFETLSELKDSRIFFLLKAKCPPIARELGVPQGALL
CI
>gnl|CDD|468765 NF040825, UDPMaNacDH_Arch, UDP-N-acetyl-D-mannosamine dehydrogenase
MKIAVIGLGYIGLPTAIMFASSGHNVIGYEIREDVVKKINSGKAHIVEPEIEERLKKVVEEGRLKATTDP
EDLKGADAFIICVQTPLKEDKPDLSYLENAIRTVAEVMDRGALVIIESTVPPGTTVKMARLLEELTGLKE
GEDFYMAHAPERVMPGRIFKELVYNSRIIGGVSEKSAELAEKLYRSFVKGEIFLTDATTAEMVKLMENTF
RDVNIALANEFALLAHQYGVNVFEAIELANTHPRVKIHVPGIGVGGHCLPKDPYLLLSNAKEDFGLIRLA
REINEDMPLFAKDLLFEALEEANVPPEEAVVTVLGLAYKGDTDDTRNSPALKFVELIEDDVKEVRTYDPY
VGGTHESLEDAVKGADAIVIATDHSEFKSLNWEELGKLMRTKILIDGRHIIKEPPKGFIFKGIGRGDV
>gnl|CDD|468766 NF040826, lxa_BCAM0308, BCAM0308 family protein. Members of this family average about 170 amino acids in length, and have a conserved pair of CxxC motifs, suggesting metal-binding. Many of this proteins register as part-length, borderline-scoring hits to Pfam model PF04981, which hits the N-terminal domain of Nmd3 (nonsense-mediated decay 3) in yeast, involving in export of the 60S ribosomal subunit from the nucleus, as well as archaeal homologs of Nmd3. This HMM was built to provide a clear separation of member proteins from that family. The family is named for BCAM0308 from Burkholderia cenocepacia, one of many proteins in the lxa (low oxygen-activated) locus, whose proteins are induced when oxygen concentrations are low
RRDRLIQEYRHDPYFTKGKLPEPTVCPQCGAVFHDGRWQWKEAPANANQILCPACQRIEDKYPAGIVELK
GEFLKKHRDEILNLIKNEEEREKAEHPLERIMAIEEEDDGIVITTTDIHLARRIGEALHHAYKGELEIHY
NEGEKFLRVYWER
>gnl|CDD|468767 NF040827, CotZ_rel, CotZ-related putative spore coat protein. Members of this appear only in endospore-forming bacteria, and are distantly related to spore coat protein CotZ
INNLTKHEGFVHKCSMSSPFFLIMREGEHFYASGISNGSVFKTCYFSLISINEKRNCVVLELLVPCCMRS
LCCNKALYRSSSRILIDISFFCGMGEVEIPVYDYLILKTIIKDKFCLCFSTNESKPEILWNNETKFLNTA
TVTLHHKDGKDVPIKIILQTKEGLYSLVVQKGESCAITVKDLECLLKSSSKEKVKGRLDIQLNHIQKNII
YF
>gnl|CDD|468768 NF040828, sulfhyd_ShyA, NAD(P)-dependent hydrogenase/sulfhydrogenase 2 subunit alpha
MIIELDEFTRVEGNGKAEIVIENGEVKEVRVKIVEGPRFFELLTLGRHYWDVPDLEARICAICYLSHSVA
SVLAIERAFGVEVPEEIQLLRELGLIGEIIESHALHLYLLVAPDVFGYPDAIRMATKHGELVKEGLAIKA
FGNYIRELIGGREIHGINVKPGGFGRYPSEEELEKIEKHSEALIRFARRAVGIFASQEPFGARAEHFVAT
DGYLWGDKLIANDGERFQYFERIEEKSLPYSFAKQSRYKGKPFFVGALARLLLKGESLTPTAKRLFEEHR
EKLESGYVSYNNLAQAIELVYALERAGEIAKELLDKGIEGENVPVEPKEGEGIGYVEAPRGVLVHHYRID
ENGKIVYSNIITPTAFNHALMELSLLEEARRLYGSLDEEELKQKLEETVRAFDPCISCSVHFVKL
>gnl|CDD|468769 NF040829, sulfhyd_ShyB, NAD(P)-dependent hydrogenase/sulfhydrogenase 2 subunit beta
MRYVKLPSENFPEFFNSLKEWGKVYGPVKKGSTYSFEEVEDLSEVSLDYTRTMLPPKKFFVRPRDTMFKL
KNGEWEEVKGVEPFVLFGVHSCDIHGLKILDKVYLSEPVDPYYKARRENAFIVGISCMPDEYCFCKSLGT
DFAMDGFDLFLHELPDGWLVRVGSVKGHEVVWENEELFEEVTEEDLKHFKEFEEKRAKAFKRELNKEGLA
DMLDLAFNSPVWKKYAEICLGCGNCNMVCPTCRCYEVCDRWINAYEAVRERRYDSCFMETHGLVAGGHNF
RPTRLDRFRHRYYCKSYFDPSAGFNCVGCGRCDEFCPAKIEHVKVLDEVRESLQ
>gnl|CDD|468770 NF040830, sulfhyd_ShyC, NAD(P)-dependent hydrogenase/sulfhydrogenase 2 subunit gamma
MNPYQSYDARILEVKELTPREKLFTLRFLDPEVEENFTFKPGQFVIVDVRGFGEFPISLCSSPTRKPIQL
CIRKVGRMTKFIHKMKEGDVVGIRGPYGNGFPMEKMEGSNLILVAGGLGMAPLRSVLWYAIDTGKYEKIY
LFYGTKSYEDILFRDEIIHLLKHGEALNCHVKLAYEVESPSCIYLEKGFSEKVCKGVVTDLFRGEEFDVE
NTYALICGPPVMYKFVIRELLDRKLSPGRIYMTLERRMRCGIGKCGHCIVGTSVSIKYICKDGPVFTYWD
ALSTRGLI
>gnl|CDD|468771 NF040831, sulfhyd_ShyD, NAD(P)-dependent hydrogenase/sulfhydrogenase 2 subunit delta
LKLGVFELTDCGGCALNILFLYEKLFDLLEFYEIAEFHMATSFKEREHLDVALVTGTVSTQRDLEVLKEA
RNRSEYLIALGTCATHGSVQGSVEGPIREKLRKVYGDRKNPMKALDSKPVVEYVPVDFAIPGCPYDKEEV
FQVLMDIAKGVEPVRKDYPVCLECKLNEYECVLVKKGIPCLGPITLGGCNAKCPRSGLGCIGCRGPLPGE
ANPPGEFEVLKELGYDEEYIARKFKTFARW
>gnl|CDD|468772 NF040832, sulfhyd_HydA, NADPH-dependent hydrogenase/sulfhydrogenase 1 subunit alpha
LYLPITVDHIARVEGKGGVEIVVGDEGVKEVKLNIIEGPRFFEAITIGKKLEEALAIYPRICSFCSAAHK
LTALEAAEKAVGFTPREEIQALREVLYIGDMIESHALHLYLLVLPDYLGYSNPLKMVDEYKKEIEIALKL
KNLGSWIMDVLGSRAIHQENAILGGFGKLPDKATLEEMKRELKEALPLAEYTFELFAKLEQYSEVEGPIT
HMAVKPRGDVYGIYGDYIKVSDGFEFPSEEYKKHIVERVVEHSFAKHSFYKGEKPFMVGAISRIVNNADL
LYGRAKELYESHKDLLRPTNPFANNLAQALELVYFTERAIDLIDETLAKWPIKPRDEVEIKDGFGVSTTE
APRGLLVYALEVKDGRVSYADIITPTAFNLAMMERHVRMMAEKHYNDDPERLKLLAEMVVRAYDPCISCS
VHVVRL
>gnl|CDD|468773 NF040833, sulfhyd_HydB, NADPH-dependent hydrogenase/sulfhydrogenase 1 subunit beta
MRYVKLPKENTYEFLERLKEWGKLYAPVKISEKFYDFREIDDVRKVEFHYNRTIMPPKKFFFLPREKLFE
FSISKAEYREVIENVEPFVVFGVHACDIFGLKILDTIYLDELPDKYYKVRREKGIIIGISCMPDEYCFCN
LRETDFADDGFDLFLHELPDGWLVRVGTPTGHRIVDKNIKLFEEVTTQDICNFREFENKRHQAFKYHEDW
GNLRYLLELEMEHPMWDEQSDKCLACGNCNTTCPTCRCYEVQDIVNLDGDTGYRERRWDSCQLRSHGLVA
GGHNFRPTKKSRFMNRYLCKNAYNEKLGISYCVGCGRCTYFCPAGISFVRNLRTILGLEEKSCPPEVSEE
IPKRGFAYAPNIRGEGL
>gnl|CDD|468774 NF040835, sulfhyd_HydG, NADPH-dependent hydrogenase/sulfhydrogenase 1 subunit gamma
MMLPKEVMMPNDNPYALHRVKVLKVYQLTELEKLFLFRFEDPELAEKWTFKPGQFVQLTIPGVGEVPISI
CSSPMRRGFFELCIRKAGRVTTVVHKLKPGDTVLVRGPYGNGFPVDEWEGMDLLLIAAGLGTAPLRSVFL
YAMDNRWKYGNITFINTARYGKDLLFYKELEAMKDLAEAENVKIIQSVTRDPDWPGLKGRPQQFIVEANT
NPKNTAVAICGPPRMYKAVFESLINYGYRPENIYVTLERKMKCGIGKCGHCNVGTSTSWKYICKDGPVFT
YFDIVSTPGLLD
>gnl|CDD|468775 NF040836, sulfhyd_HydD, NADPH-dependent hydrogenase/sulfhydrogenase 1 subunit delta
MEGKKVRIGFYALTSCYGCQLQFAMMDELLQLLPNAEIVCWFMLERDSYEDEPVDIAFIEGSVSTEEEVE
LVKKIRENAKIVVAVGACAVQGGVQSWEKDKPLEELWKTVYGDAKVKFQPKMAEPVEKYIKVDYKIYGCP
PEKKDFLYALGTFLIGSWPEDIDYPVCLECRLKGNPCILIEKGEPCLGPLTRAGCDARCPAFGIACIGCR
GAIGYDVAWFDSLARTFKEKGLTKEEILERMKIFNAHNPKLEEMVEKVFQG
>gnl|CDD|468776 NF040837, BMC_EutD_Gpos, ethanolamine utilization phosphate acetyltransferase EutD, CD1920-type. Members of this family of bacterial microcompartment (BMC) enzymes for ethanolamine utilization are thought to have the same phosphate acetyltransferase activity (EC 2.3.1.8) as EutD of Salmonella and E. coli, but lacking sequence similarity and instead being related to PduL, phosphate propanoyltransferase (EC 2.3.1.222) of propanediol utilization BMC enzymes. Examples discussed in the literature, such as Lmo1182 from Listeria monocytogenes and CD1920 from Clostridium difficile, are called EutD despite the lack of homology
LEAIVDEVVKRIKERLFEGIEVEASGRHVHLSREDVDALFGEGYQLTKVKDLSQPGQFACKERVTLIGPK
GTIHNVVVLGPERKETQVEVSLTDAVALGIKAPVRESGDIEGTPGITLSNGDKSVQLDKGLIVAKRHIHM
TPEDAKKFGVSDGEIVKVKVNGERPLIFDDVVVRVSPKFRTYMHIDYDEANACGFTKGTRGRIVK
>gnl|CDD|468777 NF040838, T4_PilC_Neiss, neisserial PilC family type IV pilus tip adhesin. PilC, as found in Neisseria meningitidis and Neisseria gonorrhoeae, is the tip adhesin of the type IV pilus. It also occurs in the bacterial outer membrane, and contributes to pilus biogenesis and to competence for transformation. Typically two paralogs are found, PilC1 and PilC2, and this HMM does not distinguish between them. PilC genes are phase-variable because of expression is controlled by frameshift mutations in a run of G residues in DNA encoding the signal peptide region
MNKTLKRQVFRHTALYTAILMFSHTGGGGGAQAQTYKYAIVMNERKQPEVKWGGSYSSPLKDKDRERKFD
HTSGCNGGGSNTDFSFNNTDTLVSQQSGTAVFGTATYLPPYGKVSGFDADNLKERGNAVDWITTTRPGLA
GYSYTGITCFSSGGCPKLVYKTRFTFGNSGLAKTRGGLDIYEDKSRDNSPIYKLKDHPWLGVSFNLGSES
TVKDGKSSNKLVSSFREDNSNNQNLVYTTEGHPISLNDWQREHTAMAFYLNAKLHLLDKKQIKNIAQGKT
VNLGTLKPRIEVTQPTNGGGNLLRTWAKWKIEDKGHISVKLKLPEVKAGRCINANNPNPKTKAPSPALTA
PALWFGPVQNGKVQMYSASVSTYPDSSSSRIFLQNLKRKDDPSKPGRYSLKPLSTSEIKSREPNFTGRQT
IIRLDGGVHLIKLNKNNEVAGFNGNTGKNDTFGIVKEGSVMPDANEWKKVLLPWTVRAFGNDNQFNTFNK
EIDANTRKKKYSQKYRIRDNGKHERDLGDIVNSPIVAVGGYLATSANDGMVHIFKKGNGTDERGYSLKLS
YIPGTMPRKDIDNQDSTLAKELRAFAEKGYVGDRYGVDGGFVLRQVNLNGQDRVFMFGAMGFGGRGAYAL
DLTKAESNNPPTGVSLFDVKNNNGVKLGYTVGTPQIGKTHNGKYAAFLASGYATKDINSGENKTALYVYD
LESNGTLIKKIEVPGGKGGLSSPTLVDKDLDGTVDIAYAGDRGGNMYRFDLSGNDPTKWSVRTIFEGTKP
ITSAPAISQLKDKRVVIFGTGSDLSEEDVDSKDEQYIYGIFDNDTGTGVAQDGQGKGLLEQVLTKDGNTL
FLSDYKRSDGSGDKGWVVKLEAGQRVTVKPTVVLRTAFVTIRKYKDNGCGAETAILGINTADGGKLTKKS
ARPIVPEANTAVAQYSGHKKTAKGKSIPIGCMEKDNETVCPNGYVYDKPVNVRYLDEKKTDGFSTTADGD
AGGSGIDPAGKRSGKNNRCFSQKGVRTLLMNDLDSLDITGPTCGMKRISWREVFF
>gnl|CDD|468778 NF040839, tungstate_WtpB, tungstate ABC transporter permease WtpB
YTTIFFAILGSFLVLFILLPIITMLLNQDPGDLSKALHDPEVIKSLLVSLYAALIATLIALIFGVPLGYI
LARKDFKGKSFVEAIIDIPIVIPHSVVGIMLLVVFYGTGIGGASKIGLKIVDNFWGIVVAMLFVSAPFMI
NSARDGFLSVDEELEHVARTLGASKLRTFFTISLPLAKRSIVSGAIMTWARGISEVGAILIVAYYPKTAP
VLIYERFNNFGLSASKPIAVILILISLALFVILRLLIGRK
>gnl|CDD|468779 NF040840, tungstate_WtpC, tungstate ABC transporter ATP-binding protein WtpC
MIRIENLSKDWKEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPE
KRGIAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVA
LARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLS
QVGDVREVFRRPKNEFVARFVGFENIIEGVAEKGGEGTILDTGNIKIELPEEKKGKVRIGIRPEDITIST
EKVKTSARNEFKGKVEEIEDLGPLVKLTLDVGIILVAFITRSSFLDLEINEGKEVYASFKASAVHVF
>gnl|CDD|468780 NF040841, AMEP412_fam, AMEP412 family response elicitor. AMEP412 (WP_017418614.1) from Bacillus subtilis strain BU412, a 76-amino acid protein that is the founding member of this family, has been shown both to elicit a hypersensitive response in tobacco and have antimicrobial activity against Streptomyces scabiei. Members of this family are found regularly in the context of an apparent ABC transporter ATP-binding protein and a large (about 520 amino acid) protein whose hydrophobic nature suggest transporter permease function
SAILNALKALVSKIPWDKVAAFLKWAADLAAAAAKKTYAQGKKILNFIKNNPGKIVDWFLKGYSVYEIIK
MILG
>gnl|CDD|468781 NF040842, elici_assc_perm, AMEP412-like elicitor-associated permease-like protein. Members of this family are found as part of a conserved bacterial gene neighborhood, along with AMEP412 family proteins and an apparent ABC transporter ATP-binding protein. The hydrophobic nature of this protein suggests the protein is a transporter subunit associated with AMEP412 family protein export. Members of the AMEP412 family (see NF040841) are about 76 amino acids in length, and affect both plant cells (hypersensitive response in tobacco) and other bacterial cells (antimicrobial activity vs. the plant pathogen Streptomyces scabiei)
MNFINYLSFKYKITRNKPKGSKKDVLAEWIAIIILFLLLTAILYFIIKLLPQSIQVNMNKYTLGLFAFLC
LISISTSVKKFYKEYFLSPEREILLVAPIKNSQIILSRFFIVAIEVLFINFIFLFPFVLANYFAGNISLE
IVLITIPQIIALSIFFSSLAHILFAFAFIISKGKGLKTVAYSLMTLASVGVIAIIVYLQNYKSFFLTQNS
WIEKIFYVLFQYPEYLLSNQINGVDVGLFTLFITLNALLFIPIAYFLTKYCYKKGLLTISSRDLEKSFYS
NKISLVINKYINNHFIKKDLLYLIRSPKLFSVYVSPILFTSVIEYKNQFASSGVFLTILINIFALVITTV
TLNILFSDDLNHQDLLFSIPFNIEELYKSRSRLLHILSFLISGIYLVIICLLESVRIEFILFALLQLFIL
TYISSKVLLSRVIKRSIKNSPGYRYNGKIVKTIFYYFFVWNIPLLILFSILQEYLRRLIENHSLSLQAYI
ILILTLLIIIGMLYKSTKTTIN
>gnl|CDD|468782 NF040843, SE2200_fam, SE2200 family small protein. Members of this staphylococcal protein family are small, typically 33 amino acids long, with the first 18 amino acids resembling a signal-anchor domain for membrane insertion. A proteomics study demonstrates significant protein expression in Staphylococcus aureus, and conservation in the genus suggests purifying selection as would be expected for a real protein. This family, broadly distributed in the genus Staphylococcus, was once described as DUF2648 by Pfam model PF10855, but at the time this model was built (April 2022), that Pfam model had been retired under suspicion of not identifying real proteins
MKKLLVVLIIGGAAFVAFKRYQQHVNKAPNIEY
>gnl|CDD|468783 NF040844, Lac_Quin_Ox_NO, L-lactate dehydrogenase (quinone), SACOL2623 family. Members of this family, found primarily in the genus Streptococcus, were shown to be L-lactate dehydrogenase (quinone) (Lqo) although they have generally been misannotated as malate dehydrogenase (quinone). Staphylococcus can survive nitrous oxide exposure from host defense through a response in which L-lactate is excreted in large amounts. Lqo acts in L-lactate consumption after its reuptake
KDIILIGAGVLSTTFGSMLKELEPNWNIKLYERLDRPGIESSNERNNAGTGHAALCELNYTVQQPDGSID
IEKAKEINEQFEISKQFWGHLVKSGDIENPREFINPLPHISFVRGKNNVKFLKKRYEAMKNFPMFDNIEY
TEDIEVMRKWIPLMMEGREDDGIMAASKIDEGTDVNYGELTRKMAKNLEKHPNVEVQYNHEVVDFNRRSD
GKWEVKIRNRATGEVFTQVADYVFIGAGGGAIPLLQKTGIPESKHLGGFPITGQFLACTNPQVIEQHDAK
VYGKEPPGTPPMTVPHLDTRYIDGERTLLFGPFANIGPKFLKNGSNLDLFKSVKPYNITTLLAAAVKNLP
LIKYSIDQIIMTKEGCMNHLRTFYPEARDEDWQLYTAGKRVQVIKDTEEHGKGFIQFGTEVVNSEDHSVI
ALLGESPGASTSVSVALEVLEKNFPEYKEEWKPKIKKMIPSYGESLINDVKLMRKTRKQTSKDLELNYY
>gnl|CDD|468784 NF040845, lmo0850_fam, Lmo0850 family protein. This family of small proteins, averaging about 45 amino acids in length, occurs widely in Gram-positive genera such as Staphylococcus, Listeria, and Bacillus. The function is unknown, but the sRNA LhrA sRNA regulates expression of Lmo0850 in Listeria monocytogenes by negatively regulating the stability of its mRNA. The regulation depends on Hfq and involves an antisense interaction
KDHDKLKKVVSNLSELGVKVSKTKSRLELMKALA
>gnl|CDD|468785 NF040846, SAS049_fam, SAS049 family protein. This family of small proteins, about 59 amino acids in length, includes SAS049 from Staphylococcus aureus, SE1307 from Staphylococcus epidermidis, and closely related proteins from other staphylococcal species. The N-terminal region appears highly similar to Rv0909 from Mycobacterium tuberculosis, which appears to be the antitoxin member of a novel class of type 2 toxin-antitoxin system (see PF14013)
MSFMDKAKDAAEKFKNSDNEQVNKVKDKINEYTGGNNKDKKEDKDDK
>gnl|CDD|468786 NF040847, mev_decarb, mevalonate 3,5-bisphosphate decarboxylase
NDLHVYGEKIKNMLLDLGYYSEPDDYEPDLEDGNISFAYSYPIKAFEKFLGYYDRDNRIANNPSISMRTD
FSFCLAACRYRKNGNSDTVILDGKNNEKYYKKAEFALDYFRKEYRINGSFDFYIKRYRRYRKAKGLSESS
AVAAAVSRALIANVFGEDAAKDDVFVSRYARLVSGSGTRAAHNGISIWLSYPGMDLRDCAAFKIGKDNDK
LNYGIFPKYSDIATDNAHSIAVNSIFYNSWVNEKYFNIKRLIENNFDINDMLKIAENDMLRLNSVLFSGG
LIIQTPESLRILREILKFKNKNEGLYFTADTGPSIMVMSFDKSLISEFRENVDDPYIEGSYNFKGHKERL
>gnl|CDD|468787 NF040848, mev_kinase, mevalonate-3-kinase
MDYKYVEARAYPTIGIILLGGISDPKNRLPLHTTAGIAYTGLDGDIYVETRLYASKAKKGYVNGKEIDTD
SPRSPFRVIDKYKHEILMREEEDGTKNVSFSSENFNVLSGSSDAGAAAIGECIESIFEYNINIFTFENDL
QAISESAGRSLFGGLTINHANGKESLTEKILDPEAFSDYVIVACHFSEDRNPSDVIHSNIIRHELYPERV
KSAEEKAKELEELAKSRDIKGIFELAEEDTDEYHSLLRDVGVHIITDEMQNLIERVKELKNEFWNAYIVT
GGTNVFVAVEKKNVDKLFSALNTFCSKPVMLKVAGPPWVISPN
>gnl|CDD|468788 NF040849, tRNAmod_TiaS, tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS
MLLHIGIDDTDSPNGMCTTYLGALLYREISRLAEPIDLPRLIRLNPNIPYKTRGNGAVAMSFEVDEEDVG
EIKDLVLEMVKELADFDHENTNPGVVFLEGEVPEKLEEFAYKAIREHVTIEEAEKVAKKVGAEIHKFKLG
RGIIGALAAIGYPLEDFTYELLAYRKRENWGTERRVDKESVFEMDREFYPFTYDNVDPYKGTVLITPHGK
DPVLVGIRGIDKGKVLLAFESVKIEEPVEFFQIFKTNQNTDDHLRFKKIGDLKPYDSAVVRGKVAKKYWE
KGRHVFFEIEDETGKIRVAAFEPTKKFRNYVRKLLPGDEVIAAGGVKEFEGVLTLNLEKFYPVKLAEKVE
YKKPKCPKCGGTMKSKGDYLKCKKCGYKMPKVLIPVKVPRELKRKIYEVPPDARKHLSRPLVLPNGEEKI
LE
>gnl|CDD|468789 NF040850, Trm14_Thcoccales, tRNA (guanine(6)-N2)-methyltransferase
MKLLLTTSQGIEDLAKREVEGLLSKLGVPFRVEEKPLGVEGRLLAEVEEAYYTDEKGRKRELSIATYLNE
NSRLLHRVIIEIASERFKGIEEEEPEKALKRIEDFVSSLPVERYVKVSESFAVRSFRKGEHEFTSVDIAR
TVGKAIFERLSRFGTPKVNLDHPAVIFRAELVGDVFFLGIDTTGDSSLHKRPWRVYDHPAHLKASIANAL
IELAEPDGGSFIDPFCGSGTIPIELALRGYEGRIIGLEKYRKHLRGAKMNALAAGVLDRIEFILGDATRL
SEYVESVDFAVSNLPYGLKIGRKSMIPELYMDFFSELSKVLEKRGVFITTEKKAIEKAIEENGFKIIHHR
LIGHGGLMVHTYVIE
>gnl|CDD|468790 NF040851, tran_reg_TrmB, HTH-type sugar-sensing transcriptional regulator TrmB
MEIPPEILQALSEIGFTKYEILTYWTLLVYGPSTAKEISTRSGIPYNRVYDTISSLKLRGFVTEIEGSPK
VYAAYSPRIAFLRFKKELEEIMEKLEKALKRVKREEQRPAIWRSKDFDEAIEMFRESLDSAENEVIVVTP
SEFFEEIRDDLIKTLERGVTVSLYTDKVPDLSDFKGKGNLFVRRFYKLNHLIGMADGKEVITIQNVSFRP
KNPPSFKATYPEIIFSQYSLIIEIFKESSLELEVINNPQDIRFFAMFHAVDFVRRHLKDSDIYAEVIGKN
LKTGEVETLYGRVVGYTLSLREAINNIHLETENGVVKVGGMFAVLEDYESTDIRLTLT
>gnl|CDD|468791 NF040852, nitrile_Arch, nitrilase
MKVAYVQMEPVLLEPEKNYSKAEKLIKEAAKQGAKLVVLPELFDTGYNFESREEVEEVAQPIPDGETTRF
LMELARELEVFIVAGTAEKDEGGRLYNSAVVVGPIGYIGKYRKIHLFYREKLFFEPGNLGFHVFNLGFAK
VGVMICFDWFFPESARTLALKGADIIAHPANLVMPYAPRAMPIRALENRVYTITADRIGEERGLRFIGKS
TIASPKAEVLAMGSEDEEEVGVVEIDLSLARNKRLNELNDIFKDRRPEYYFL
>gnl|CDD|468792 NF040853, KEOPS_Pcc1, KEOPS complex subunit Pcc1
RIEGRIEIEFPSEEIARVVYESVLYEHESVPYRRSRIEFRLEGRKIVIEFTATDNSALRGTLNSYLRWIK
VAMDSVEL
>gnl|CDD|468793 NF040854, Hol_resolv_Hjc, Holliday junction resolvase Hjc
MYRKGARAERELIKKLWEAGFAAVRSAGSGATKKPKPDIVAGNGKIYLAIEVKSTSKDPLYISSEDIEKL
VEFSRRFGAKPYIAVKFIRKGWRFFPPEDLEKTRGKNYKIDLDLALPKGLDLDEVLGKQKQLKL
>gnl|CDD|468794 NF040855, iso_homocit_dh, isocitrate--homoisocitrate dehydrogenase
MYRVAVIKGDGIGPEVIDAAIRVVNAVTDRIRFYEFEGGFEVFKRYGSPIREEDLEEIRKMDAVLFGATT
TPFDVPGYKSLIITLRKELDLYANLRIIPDLWNGREIVIVRENSEGLYSGLGAVFSDRAVDFRIITREGA
ERIARFAVNLAKERGSFITFVHKANVLTGDKFFRKIVLEIAEREGVEVREAIVDSFTIKLVRNPWNHGVI
LSENLFGDILSDLATIHAGSIGIVPSGNYGDDIALFEPIHGSAPDIAGKGIANPIGAILSAAMMLDYLGL
DGSIIWEAVRRYVRKGNLTPDMGGTATTKEVTRGIISEIYRLDPLEIDEVWRDEIRLGRIPLLIS
>gnl|CDD|468795 NF040857, condensinMksB, Mks condensin complex protein MksB
MIDPKRVLRALAEHWALLEPLCERFDSGTLSLAELRSQLAAQLPDSTPADITALLDQWIRLDILVPVAKS
PNRFELNAQIHDFLAYLRREHRLGLCLEIEAYLRHLERLAGHIQDAFEIRDGNDLARQLRLLDMRVRDVL
KKLANDEQALVGVAERAKTSDRQIPLRQRYAEVLATWDEYVEPMIQLVSADGAFEQGVRRVEQVLLRLLG
EQQRLGHLVDDDLLLRTHARILEMQTTAQLTLRRARELLLPLREEARRHNAVTRGAALALAAIRRKGLDA
VPQAALPLFSRPQSTFLGTASQVEAYVYALARFEPKPARFPKASGKRKGGEPPRAPRTAREMLERCEAAL
PLPDLMAWLLEQEPEGATDELLYWFSRLSRDARFQRERLERRDYLTREHRVSLCSFALAAAP
>gnl|CDD|468796 NF040858, condensinMksE, Mks condensin complex protein MksE
MHIDLSELTQLAPIFRELFKGYHISRRDPELYAQLSNLQDQYRALFKALGFELVCDTRGFYYFVPEQMGA
QVNKTAQRLALFTFILVEHLADQGRDPLAVLDGGSLGRDELPALLEKYRDLFLQAEVQTQDELEEKIMRR
LTQLGFASEDNGVYRFLPPMHRFLDVCLSVQQDRDLAASLHSDLPLPAPVLMDDDEEPIVSLDEELEEES
EEDALARAIAEERAAQEADA
>gnl|CDD|468797 NF040859, condensinMksF, Mks condensin complex protein MksF
MSQERYGIRRFALLNTAGYSLGLFPLEHPLSVYGANNLGKSASINALQFPILARMSDMSFGKYSLEQSRK
FYFATDTSYILVELDLPHGPHVIGVAGRGPGGGFGHQFFAYAGELDLAHYQKNGTCLRQRELFANLERAG
LKAYELKPEELRRLLVGGHTSIPLDLTLIPLRSTSEQSLKTFRALFINLLHMREITAAKLKQLFLDAFEH
SLRSGSVDYIAACEEAFRDVRRMEQDYQALVAAGPLVEALANGVAQRDILRGKLHRLSPLLDSLLGTWQD
YAGARREELLIQAEHYRSEQDGLQNEQRGGTQELMRLEREISEIQRWLGELAVLKNRFALVEDVKVLEQQ
LLAAKDAHDELAGALAQSRQFSSEDLDERVRDLEKRLKSVRQQLDHADNNSYARLREEFSQQDVERLMRL
FNGALFSLPLGEKGIQLDDDGAWVKTLEAILDGFKGERFEAPGLSIDLSHIEPPALQALADRAALRDQKD
RLERELKQLKTQQAVAADRAASKAQAEQLYQAVLDAQKALEDFRRCQTLSAEEPEKLEQLAQLEAAQDEL
KRSSDAFTERVQQLSAKLQLVGRQLADLEAKQRTLDDALRRRQLLPADLPFGTPFMEPVDDSLDNLLPLL
NDYQDSWQALQRIDGQIEALYAQVRLKGVAKFDSEDDPERRLQLLINAYAHRQDEALTLAKARRAAVTDI
ARTLRNIRSDYDNLEHQLALFNREINRRQVSNLESFRIVLAPNKDALRHIDQIIHSAGQYEEGETLSVFD
LTQSAEQDAKNEEAKEYLARLVAANHNQLGLKDLFELAFEITKVGGQPVIHTDIDGAASNGTTMTIKALT
NMYLLLHLMDREQAGRVRLPYYLDEAADIDERNQQALIETSLQLGFVPILASVKPQVSAHVAIDLEGGSG
PNGIYIDEADWKYIRR
>gnl|CDD|468798 NF040861, pufA_517_ASD, light-harvesting antenna LH1, alpha subunit
WKIWLVFDPRRWLVAIFVFLLVLALLIHFILLSTEGFNWLE
>gnl|CDD|468799 NF040862, pufB_517_ASD, light-harvesting antenna LH1, beta subunit
SLTGLTEEEAKEFHKIFVKSFRGFTVIAVVAHILVWAWRPWL
>gnl|CDD|468800 NF040863, HgcA_corrinoid, mercury methylation corrinoid protein HgcA
VPQVSTELTFADRLGAWKARWGIGRMNYKVEPGLYALGNPDAESPVLVTANYKLSFDALRKELAGLDAWI
LVLDTKGINVWCAAGKGTFGTDELVRRIAATGLAEVVSHRTLILPQLGAPGVAAHEVRKRSGFKVVYGPV
RAADLPEFLDNGMKATPEMRRVTFTLRDRLVLTPVELVGALKPSLAAALILFLLAGLGPGTAAALAGLAA
FAAYLGAVLAGTVLTPVLLPWLPGRAFAWKGLLLGLLWALPFALLFGGPLPPWYGLLEALAYLLILPAVS
AYLAMNFTGSTTYTSRSGVKKEMRRAIPAMAVAAVLGILLWLVSSFL
>gnl|CDD|468801 NF040864, HgcB_ferredoxin, mercury methylation ferredoxin HgcB
RYLKNVATLELDPEKCVGCGRCLEVCPHRVFALGEGKAVIVDRDACMECGACARNCPVGAIEVKPGVGCA
SAIINGWLTGKEPSCDCSGGGGCC
>gnl|CDD|468802 NF040865, a_tRNA_ed_AlaXM, alanyl-tRNA editing protein AlaXM
TEKLYLEDSYLKEFDATVVRVKGNGVVLDRTAFYPTGGGQPHDTGTLVRDDKEFRVVDVRKEGGEIAHVV
DRAPGLKPGDKVKGEIDWDRRYRLMRYHTASHILSAVLYREYGALITGGQISPDKARVDFSLENFDRELL
EEIIEEANEIIAEGIEVKIYWLPREEALKIPGLVRLAKRLPPEIEEVRIVEIEGVDIQADGGTHVKNTGE
IGEIKILKRENKGKGNKRLYFTLE
>gnl|CDD|468803 NF040866, AraD_Arch, arabinonate dehydratase
MIKEIKTYKLCYEGINEERDALAVKGLAEHPMEIVVTEIETSDGEIGYGESLAYGCSDVVQVTIEKILKP
LLLKEDEELIEGLWDKMYKATLRFGRRGIVIAGISGVDIALWDIMGKKTKKPIYKLLGGSKRKIRAYITG
GYYSEKKDLEKLREEVAYYVKMGFKGVKIKIGGKSMEEDMERLKAIREVVGEDVKIAVDANNVYTFEEAL
KMGRELEKLGIWFFEEPIQTDLLDLSAELTEALEIPIAGYETAYTRWEFYEIMRKRSVDIVQTDAMWTGG
ISEMMKIGNMAKVMGYPLIPHYSAGGISLVANLHVAAALGSPWIEMHLRKNDLRDKIFKESIEIDNGHLV
VPDRPGLGYTLREGVFEEYRCK
>gnl|CDD|468804 NF040867, prot_deacyl_CobB, NAD-dependent protein deacetylase
EKAAELLASSRHAIAFTGAGISTESGIPTFRGPDGLWRRYDPEELATIEAFERDPKLVWEFYRWRMEKLF
DAKPNPAHYALAELERMGILKAVITQNVDGLHQRAGSRNVIELHGNMRRVRCTSCGRTYDLEEVLRKIDK
GELPPRCPECGGLLRPDVVLFGEPLPDDALEEAFELAERSDVVLVVGSSLTVYPAAYLPYIAKENGGKLI
IINPEETPLDPIADIVLRGRAGEVLPKLVEEV
>gnl|CDD|468805 NF040868, carboxypep_CpsA, carboxypeptidase CpsA
AEKILKEAKEIEDKIIEIRRKIHENPELSYQEYRTAKLVAETLRSLGIEVREGVGLPTAVVGILRGKKKG
KTVALRADMDALPVQEETDLPFKSKVPGVMHACGHDAHVAMLLGAAYILSKHKDELSGEVRLIFQPAEED
GGRGGAKPMIEAGVMEGVDYVFGLHVSSSYPSGVFATRKGPLMAAPDSFKVEVHGKGGHGSAPHETIDPI
FISAQIVNALQGIRSRQIDPLQPFVLSVTSIHSGTKDNIIPDEAVMEGTIRTLDEDVREKALEYMRNIVE
SICEAYGAECKVEFKEDAYPVTVNDPETTKEVMDILSEIPGVKVVETDPVLGAEDFSRFLQKAPGTFIFL
GTRNEKKGIIYPNHSSKFTVDEDVLKLGAAALALLAMKFSR
>gnl|CDD|468806 NF040869, G3PDH_Arch, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
EKSPLFKDIYRIGEDGVPEFKTYVAGEWVFGGEFADVKSPIDGSVIARVSRLSREQVEEAIETIYEKGRW
KIRDTPGEKRLEIFLRAADLLEKHRDDFVNVLVLNAGKTRSAAEGEVNASIERLRKATLDVRKIYGDYIP
GDWSEETLESEAIVRREPYGVVLAITPFNYPLFDTVNKIVYSLLAGNAVILKPASADPLPALLFARVLEL
AGFPKESLALLTIPGREMDKVVADRRISAISFTGSTETGEHVLRTGGIKQYIMELGGGDPAIVLDDADLE
LAAEKIVTGITSYSGQRCDAIKLILAEEKIYDELKKRLVEELSKVKVGDPRDENVVMGPLIDEKTADEIE
EAIKDAVEKGGKILYGGRRLGGNYVEPTLIEVDKEKLKDLRLYNEEVFAPVALLVKVKDLDEAIELANSR
RYGLDAAIFGEDINRIRKVIRLLEVGAVYINDYPRHGIGYYPFGGRKDSGIGREGIGYSIEYVTAYKTIV
YNYRGKGVWEYL
>gnl|CDD|468807 NF040870, AztC, zinc ABC transporter substrate-binding protein AztC
VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLEEGFLRHLIAAS
ATGAPVVEVGDGVDPLPYPEGGHYHFEAGAGPPDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANA
AAYRAELDELDAEMREAFAAIPADRRTLVTNHHVFGYLAERYGFRVLGAVIPSGSTLASPSAADLASLAR
AIREAGVPAIFAESSQPPRLAEVLASEAGLDVGVVELYSESLSEPDGGAATYLDMMRANAEAIVDGL
>gnl|CDD|468808 NF040871, AztB, zinc ABC transporter permease AztB
EWLLAPFEVDFVQRALVGGVLVSLVCAPVGTWVVLRGMAFLGDAMSHGMLPGVALAFLLGGPLTLGAAVS
AAAMALGVGALSRSRRLSEDTSIGLLFVGMLALGVIIVSHSGSFAVDLTGFLFGDVLAVRDADLALLAGA
LAVTLAVAALFHRAFVALAFDPRKASTLGLRPRLAHAALLGLVTLAVVASFQAVGTLLVVGLLIAPAAAA
RLWARRIPTMMALAALLGAAAVVGGLLISWHASTAAGATIAASA
>gnl|CDD|468809 NF040872, MFS_HP1165, HP1165 family MFS efflux transporter. HP1165, the founding member of this family of MFS efflux transporters, was shown to provide mild resistance to tetracycline after long exposure, but does not appear to be dedicated to resistance to specific antibiotics. It seems instead that expression may be raised by various factors including the effects of host response to infection
LRKNILAYYGANFLLIIAQSLPHAILTPLLLSKGLSLSEILLVQTFFSFCVLVAEYPSGVLADLMSRKNL
FLFSNLFLIASFCCVLFFDSFILMLLAWGFYGIASACSSGTIEATLITDIKENKQDLSKFLARNNQITYL
SMIIGSSFGSFLYSKMHASMYMVAIFLVLLCMLTIIFYFKENEVDFKSQKSLKLLKEQVKGSLKELRDNP
KLKILLVGHLIVPLFFMSHFQMWQAYFLAQGIKEQHLFIFYIAFQVISILVHFLKASSYSQKITLSSLVV
LLSVSPLLLTNIPYLFIGVYALMVAFFTYMSYCLGYQFSSFVSKNNISSLSSLMSSCVRVVSVLILSLSS
LELHYFSPLSIITMHFAITLLILFFFLYKAKVFSE
>gnl|CDD|468810 NF040873, AztA, zinc ABC transporter ATP-binding protein AztA
GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSL
PLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADL
LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL
>gnl|CDD|468811 NF040875, SAS053_fam, SAS053 family protein. This small protein of Staphylococcus, Macrococcus, and Mammaliicoccus occurs in a conserved gene neighborhood, downstream of a larger uncharacterized protein distantly related to glucosamine-6-phosphate deaminases. The function is unknown, but its gene is known to be translated into protein. The family is named for founding protein SAS053 from Staphylococcus aureus subsp. aureus N315
EPENEMVDDFDDVVELGKEMEQISEQNDEDKLNQSHDEDVRS
>gnl|CDD|468812 NF040876, RHE_PE00001_fam, RHE_PE00001 family protein. RHE_PE00001, the founding member of this family, was shown to be essential for growth on rich medium, despite being encoded on a plasmid. Members of this family contain an apparent helix-turn-helix domain described by Pfam model PF11972, suggesting DNA-binding activity
RYDIDKLPLQTLLPPIAAAEDALARLDERLARSPVGDGFIERAHFFDACASLWVDGELVHLEDLVLHDAG
MDIRAPTHELTIAHAVLRTRRRIASAPPGWALSPAGLASLRGRGGGGEAAEAGGGAEEADEAPDEEDEEL
DDEEDDPLAAEFAEIDAVLARSDRLLDGAKAPGPPASETVERDPLVYDLDWDEDERLEEWRAVLAQAENL
PPVLAAAVLLDAWEELEPLQRQPWLGRLLAAAYLRQRGKTTSHLPAFNVGLKTIPRERRRARDRETRLLA
FLDAMTAAAEAGLKEHDRLSLAREQMERKLRGRRSSSRLPELVDLVLSRPLVSAGMIAKELKVTPRGALN
LVAELGLREMTGRGRYRAWGII
>gnl|CDD|468813 NF040877, SE1832_fam, SE1832 family small protein. This small protein is known to be expressed, but its function is unknown
EIEQKIAELKSDYVRLQGDLEKLESTGGNVEKLEKQLEEIEEELKELRKQL
>gnl|CDD|468814 NF040878, SE1561_fam, SE1561 family small protein
KEEQLQYLKNRLEMFLEVLDSLDPEEADVEDIDRLIEMLDELEIKV
>gnl|CDD|468815 NF040879, SAR1012_fam, SAR1012 family small protein. This small protein of unknown function is encoded in multiple species of Staphylococcus. It has been demonstrated by mass spectroscopy to be expressed with an unmodified N-terminal fMet residue
MNIIKRVVRTIITGYVVKFIRNKISGKSSG
>gnl|CDD|468816 NF040880, adnlytase_SelO, protein adenylyltransferase SelO
MTLSFTARWRDELPGFYTALNPTPLNNARLIWHNAELAQQLGIPASLFDPEGGAGVWGGETLLPGMSPLA
QVYSGHQFGVWAGQLGDGRGILLGEQQLADGTTLDWHLKGAGLTPYSRMGDGRAVLRSTIRESLASEAMH
YLGIPTTRALSIVTSDTPVYRETTEPGAMLMRIAQSHVRFGHFEHFYYRREPEKVRQLADFVIRHHWPHL
QDEADKYALWFRDVVARTASLIASWQTVGFAHGVMNTDNMSILGLTIDYGPYGFLDDYQPGFICNHSDYQ
GRYSFDNQPAVGLWNLQRLAQTLSPFIAVEALNAALDRYQDALLTEYGKRMRQKLGFFTEQKGDNDLLNE
LFALMAREGSDYTRTFRMLSQTEQHSAASPLRDEFIDRAAFDSWFARYRARLQTEQVDDDARQQLMQSVN
PALVLRNWLAQRAIEAAEQGDMAELHRLHEALRNPFNDRDDDYVSRPPDWGKRLEVSCSS
>gnl|CDD|468817 NF040881, PTS_reg_TmaR, PTS system regulator TmaR
MENTTKPSFQDVLEFVRMFRRKNKLQREIVDNEKKIRDNQKRVLLLDNLSDYIKPGMSIEEIQAIIANMR
SDYEDRVDDYIIKNAELSKERRELSKKLKAMGE
>gnl|CDD|468818 NF040882, cfpA_ASD, cytoplasmic filament protein CfpA
DLPKSPNVFHPEKPSAVGSRNSLAQEYRDQQKEVNQLLEEETNKVLHHLNTKLPKEVLERLDVMGGLKEK
LYNYFNQNYQNMFNRYMVTAEDEMVKKVRNFIDKEEMKVLARYTPKEIATLLDEVGGADKFNTGEIEKSI
VNMYGHLQGHIQRGVNDLENLTNSLLRQKTDVGAFIRGENAYSVVKCAFKDNLYKPKTVTDVKLSVNILD
SELISPIFHYQVTVEYLIKDLISKHIMDLIDKEIEKLKDELIDQGKEELSDSEIIFEKMKRVEDFTDDDV
DNPKSKRYSFVAKSLMERIEGLRAEIDPEEFDQLNIRENLKKIIDIENIRNRGFNTAINSITSILDTSKM
GYQYIENLKNARELIIREYEDTDVANLPDERYQIRLKYYDNAQLIEERKAYDVQLKSFETEVQHLWDVLE
MIYEDSKFMKRVTDFDDLAKKYKKKIKKKIKDKTGDPLYEDIAKVWDEISFVKPAETEVERMNRTYVYEK
DKIRKKLILMREKLKQMYGYQYPVERRVMEDRLAFLEREFNRFDYLINPYHIQPGLLLDVDITSIKRKKA
TLDGMANVLNEFLHGVSKGFQDAAFASFSRRRSTVRADIAQSFSS
>gnl|CDD|468819 NF040883, amid_act_ActS, amidase activator ActS
LALWFRIAVCLTLGLLLAGCSGKKSDYDGSYSGSTYTVKRGDTLYRISRITGTSVSELARLNGISPPYTI
EVGQKLRLNGSSKSKKSAAKSSTKTAKVTPSSAVPKSSWPPVGQRCWRWPTSGKVVLPYSTADGGNKGID
IAGKRGQPVYASGAGKVVYVGNQLRGYGNLIMIKHGEDYITAYAHNDTMLVNNGQSVKAGQKIATMGSTG
ADSVRLHFQIRYRATAIDPLRYLPPQGSKPSC
>gnl|CDD|468820 NF040884, acetylneur_anom, N-acetylneuraminate anomerase
MILGDLSQPESASGLPPVLQDALTLALAADLQELAPGRYEIDGDDIFMNVMEFETQPAESKKAELHRQYI
DIQLLLSGEERIDYGLAGSARECEEYHEEDDYQLCDTIENEQTLTLTPGMFAVFMPGEPHKPGCVVGTPP
GEIKKVVVKVHASLL
>gnl|CDD|468821 NF040885, diguan_DgcJ, diguanylate cyclase DgcJ
KHKLLRFFISAGVVVLTSSFLIYELVASHRDMNGYMRYIIEKGESAFLYDKYQNQSIASQLMRAFSTPEK
PPSAEKRHQICASVESANGVYGLNLTGHTYPALHGTLQTRNADCEQWAQDIPALPAFDSAVAENRSQYDF
SPGLGKSEDKFRYYIDLQNQYIYFYSLVDTKNFAFSNWLFLQDGTLGIDQASLDGLFSGRTVTSSIYRDG
YTHKNIISFLTPVYQDGTLKGIVMVDVNIQDLATIFYTADRPLVWRYLDISVTDSDSGKEIIVHRSENHL
FSYVNYSHDLTGNLHVELSLDVLYFILSSWKLFLFYLLSTALLLHLVRMHFRLYHNVSRENISDSMTGLY
NRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLG
GDEFCIILIDYEEAEAQNLIERIRQHLRTIDPDKRVSFSWGAYQMQPGDTLDDAYKAADERLYLNKKQKH
>gnl|CDD|468822 NF040886, cyt_C_like_Sec, multiheme c-type cytochrome (seleno)protein ExtKL. Most members of this family are selenoproteins. The gene symbol ExtKL predates recognition that a UGA codon separate ExtK from ExtL actually encodes a selenocysteine residue
RFKLLSLALLALALAAAAGVAADATAAASKKKAKTLDELIAMYDSSSCKECHEEIYEQWEKSLHARSLFG
GRTAATITTFIEVGLKKWPYSGVKKPTDVKVEHLMPCAKCHLPQLADATDSVAQEIAEAIVDAKDAYKAG
DEKEEAKEKLEKLNIGCLVCHNRKAIVHKWTDGYPQPGVIYGPKDGDHDDEKFPKMKKSPIMKESIFCGQ
CHGLGPNLELDEPTQCATLYGSYLHAYIPEGGTKTCQECHMRKSGLGHRFPPYRDDKMVKEALDFEVEAL
GYRWRPDGKERLWIPLVVVKVEITNKAGHRIPDGUPTPNRVVLEVTAKDKDGKELFSEEKIYMPQPQLLD
RGNRMGRGPYEKSGIIRDTSLQPFKTKEETFEIPLPTEVKEAEIEVKLWYLPFGGKPDDEFLWHEVTKKV
SLK
>gnl|CDD|468823 NF040887, trans_reg_YciT, DNA-binding transcriptional regulator YciT. Involved in osmolarity control regulation
MNARQQQILQLVNDRGRVSVSELAQLTGVSEVTIRQDLNLLEKQSYLKRVHGSAVALDSDDVDTRMMTNF
PLKQKLAEYAASLVEDGETVFIEGGSTNALLARYLAERKDITIITVSHYIAHLLKDSACEVILLGGLYQK
SSESVVGPLTRLCIQQVHFSKAFIGIDGWHPETGFTGRDMMRADVVNAVLAKGAENIVLTDSSKFGQIHP
YPLGPLHQFSRVITDDGLPADYRQQLEEQGIRVDLV
>gnl|CDD|468824 NF040888, trans_reg_YafC, DNA-binding transcriptional regulator YafC
MKATSEELAVFVTVVESGSFSRAAEQLGQANSVVSRTVKKLENKLGVTLLNRTTRQLSLTEEGERYFRRV
QKILQEMAAAENELLESRQTPQGLLRVDAATPVVLHLLVPLIKPFRERYPEITLSLVSSETFINLIERKV
DVAIRAGELTDSSLRARPLFNSYRRIVASPDYLARHGTPETVEDLAQHCCLGFTEPESLNRWPLLDADGQ
LYEITPGLSANSGETLRQLCLAGNGIACLSDFMVDKDIAEGRLVELLAEKTLPVAMPFNAVYYSDQAVST
RIRAFIDFLSEHL
>gnl|CDD|468825 NF040889, trans_reg_YeiE, DNA-binding transcriptional regulator YeiE
MHITLRQLEVFTEVLKSGSTTQASQVLALSQSAVSAALADLEGQLGVQLFDRVGKRLVVNEHGRLLYPKA
LALLEQAGEIEQLFKQGNGALRIAASSTIGNYMLPEMIARYRQDFPHTPLELNVGNSQDVINAVADFRVD
LGLIEGPCHHPELITQPWLEDELVVFAAPDHPLAGQPVTLEDLAAAPWILRERGSGTREVVDHLLLSHLP
QFHLAMELGNSEAIKHAVRHGLGISCLSRRVVAEQLASGTLVELTIPLPPLSRTLYLIHHRQKHLSNALL
RFLSYCRE
>gnl|CDD|468826 NF040890, trans_reg_YgbI, DNA-binding transcriptional repressor YgbI
MIPVERHQQILALVAERGVVSIAELTERLGVSHMTIRRDLQKLEQQGAVLSVSGGVQSPERLAQEPSHQD
KEAMASRQKAAIGQLAAQQIPPNSCIYLDAGTTTLALARHLAERQDLTVVTNDFVIADYLIENSQCTIIH
TGGAVCRENRSCVGEAAAQALRNLFIDIAFISASSWSMRGLSTPSEDKVAVKRAIVEASRQRVLLCDTSK
YGKIATYLALPMTVFDTIITDDGLPEAAKEALEKAGISLLLAK
>gnl|CDD|468827 NF040891, colicin_tol_CbrC, PF03691 family colicin E2 tolerance protein CbrC
MTQNNRPLPVFKYHPDPLETGAFETDKTVTCDCCQQPTDIYYEGPFYSVDDIDALCPWCIADGSAAEKFD
GSFQDSASIEGIDSEYDEDGEFSGTTNPYPDEMLDELVERTPGYRGWQQEHWLAHCGDFCAFIGYVGWDD
IKDRLDEFASLEDDCAEFGISYEDLPKYLHNGGDCQGYLFRCLHCGKLRLWADFS
>gnl|CDD|468828 NF040893, SAVMC3_10250, SAVMC3_10250 family protein
RELVYLSEAKLDQLLPQLPRRLLRRRGVEASVDLKVAGAEVSLPAAPAEDAEARLERVIRHLEREARVGW
FTEPGLRPGQWVRFEAPLRYGVLGGGAPEDLVLFGGEAGGPSPGDTRLLLHGSARHLLGRRDPAGPDGPP
VSASGLPSLVRALAELAGEDLEAAAVFRAPISAESAPVPLLEEGALELVAELDDRLTPPATAAEFVGHAR
VTAVVPDPSWIRRVVVASPLYVEYAD
>gnl|CDD|468829 NF040894, puhB_PGC, photosynthetic complex putative assembly protein PuhB
HDDFAFEPVRGLPERLPEGERILWQGRPDWWALARRAFHLRWVAGYFALLAAWRVAASLDDGAPLGQALA
AALPFLVLGAVACGLLLLLAWLQARATVYTITNRRVVMRIGAALTMTLNLPFKQIGSADLKLRRDGTGDI
ALELIGDTRLSYLVLWPHVRPWRFRRPQPALRCIPD
>gnl|CDD|468830 NF040895, MFS_effux_SdrM, multidrug efflux MFS transporter SdrM
KLKSIGIVVALVLIMFMAAIETSIISLALPTIKEDLNAGSSISLVFTVYFIALVIANPIVGELLSRFKII
YITILGLLLFIIGSLMSGLSETFTMLIISRIIQGLGAGVMMSLSQIVPKLAFEIPLRYKIMGIVGSVWGI
SSIIGPLLGGGILEFATWHWLFFINIPIAIIAIILVIFTFHFPEEETTSKTKFDVKGLTLFYIFIALLMF
AVLNQGHLWLNIISFILAIVVFFLLFKVEKKVKNPFLPVKEFNKSIILVFFTDFLIAMMLMGYNLYIPIY
LQEHLGLSPLQSGLVIFPLSVAWLILNFNLAKIEAKLTRKGLYIGAFTLLIVCSILILFGLKLPLLIAFA
LILAGLSFGTVYTKDSVIVQEETSPSNMKKMMSFYTLTKNLGSSIGSTIMGYIYALQVGLFGLSIQNILA
LIIIILIILIILWSTLYKEQK
>gnl|CDD|468831 NF040896, SP_0009_fam, SP_0009 family protein
MENLIETIEKFLAYSDEKLEELAEKNQALREE
>gnl|CDD|468832 NF040897, SPJ_0845_Nterm, SPJ_0845 N-terminal domain
MGLKFKRQDDLDKMFDKFAVLPDDK
>gnl|CDD|468833 NF040898, CC_mini_metal, LDCC motif small metal-binding domain. This small and previously undescribed domain, just over 30 amino acids in length, occurs primarily in small proteins of unknown function. It is identified as a probable heavy metal-binding domain by its CysCys pair (seen often in mercury resistance proteins), by the presence of metal-binding or transport domains such PF00403, N-terminal or C-terminal to this domain, in longer members of the family, in some cases by local genomic context
KKFWKKFLEKLAKANKKSFGGGKLDCCDLNK
>gnl|CDD|468834 NF040899, ryptide_rSAM, radical SAM/SPASM ryptide class RiPP maturase
MIYELEDGVLKKIEESNNVQTISLTSIYQQKINDKFTLLINSFKNKVLVVESKKIKNNMMEIDSSLSEWF
ETPSSNLDHFSPETLYDEELLSESKKKIQISLAITYSCNLRCSYCFQQKYDGLARKPITLEELEKTLDKI
SLLIYENPELEVSLGLFGGEPLLPKNEPIIDRIFQYCVENKLKIDITTNGIFLPYFAKKLIIYRSIISVI
AITVNTLPETYKEIVKITKVANNTEKLLAITDLLLDYGLVMDVGTNFDKTNLHELVPIYHYFKDKGYFSK
WNFHWNIGRVDDRLFDTGYDDYIVSETDILLELMKIRKQVPSNLHAGFIQTCKNLTDKLKLSFNESQTKG
TYNYCWNVSPYDRVFYIDNELNLFRCTVTVGRPQYILGNLRTIDLMNYQHETKTFLDYKDCQICHIGGFC
SGGCKLSADVDFYKQCEWEKKEFEKFVNQILIPELREKLEVLYV
>gnl|CDD|468835 NF040900, porin_ExtI, selenite/tellurite reduction operon porin ExtI
KKIGTLAAAALGLVLLAGTAFAGPIWTFGPNDQGALQLDYKGQFQMTVRDTGSGSNGDDDTAEFNFRRNR
LALMGAYGDKFSLYVQTEYTEDRNITPLNVADGSDGDEFQLLDAVMRFKVNDSFNVNVGKFKYNLTRENL
EACEMPLTLDRSLFIRAPFVTTRDKGVAVWGNLFDDMFQYRLDAMEGRKDVSGESAPGSNFRYTARAHVT
LLDPENGYGYKGTYLGKKKVLTIGAAYQYEPDVAYGNTALKTDAKDYKAWTVDGFFEYPVEGVGTFTASA
AYEDYDLDDAYLGANPDPDVTGINGEKNGGYVKAGYMLPNLPLQFFGRYEKWSFANLNGVYDQEIDWYGG
GVNYYLRGQNLKLTAEYSSTDFDKEGGFGGTTQNTEDFMTFTTQLQVIF
>gnl|CDD|468836 NF040901, SeO3_TeO2_ExtH, selenite/tellurite reduction operon rhodanese-like protein ExtH
KKSRSLLVGLLGVLAATALTLWGCGGGGSDTPAEKPVTTKTPTALIEAATLKSWMDAGLVNKAGGYDRVV
ILDVSSTNAYYTVGHIPGAQLISSGFLDNTRLEGLAVTGSMVCTGATMDAIIQRAGIDQNTTIVLTSVNA
AGFVNVARAYFTFRYWGFPKERLKVLNGGNAAWDAAGADLTWTVATYAKSTYGVAQNGTSRVNTDMRVSL
PEMLRYVIGEMIGNVDKVTLGDTVTGATNVSIADISGTTDLLATGGKATPFDGAIKGSYSLKATVMYNPT
NTLYFKDAAAIRADLEAALGTDGTKTTITYCRAGNYASTGFFALDGILGWPVKWYDGSWGQWNLYASSDH
TAVDTTGTVNAGGKLAVGSIWDTTSLTDNLTWNVWRPRTTTFDTAATLIIDYASNVYYVEPSDPRANQIE
NEDRAY
>gnl|CDD|468837 NF040902, NuoF_pre_CCxxC, CCxxC motif-containing NuoF prefix domain. This domain of about 50 residues, containing seven invariant Cys residues, is a rare N-terminal extension to the NADH-quinone oxidoreductase subunit NuoF
MKNLMDKCCEKCTHSPQAPCRDYVACRTEGPLCHDDEACREKRQQLLANIKVP
>gnl|CDD|468838 NF040903, GguC, GguC family protein
MRLIQFEDEDGQRRVGVVEGGQARVLQGVSSVYELALAAIAAGKSLAAVVEALGLGEAVDYAALLAEGRL
LPPLDHPDPAHLLVTGTGLTHLGSASTRDKMHQKAADEEATLTDSMKMFRMGLEGGKPAAGQAGVQPEWF
YKGDGSIVVAPGAPLPSPSFALDGGEEPEIAGLYVIGPDGTPYRIGFALGNEFSDHVTERKNYLYLAHSK
LRACSFGPELLVGDLPDHIEGTSRILRDGEVIWEKPFLSGEANMSHSIANLEHHHFKYSLFRRPGDVHVH
FFGTATLSFADGIKTQPGDVFEISAPEFGLPLRNPLAVAAPEPVSVKAL
>gnl|CDD|468839 NF040904, PhrA_Strep, PhrA family quorum-sensing system peptide
MKKNRGIQKLLTLLLLGVFTFSNTIPYQQFIQKDRQYEIRVQSQKKSNGLDVGKAD
>gnl|CDD|468840 NF040905, GguA, sugar ABC transporter ATP-binding protein
ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILFDGEVCRFK
DIRDSEALGIVIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDI
GVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSIT
VLRDGRTIETLDCRADEVTEDRIIRGMVGRDLEDRYPERTPKIGEVVFEVKNWTVYHPLHPERKVVDDVS
LNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYG
LNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLF
TDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREE
ASQERIMRLI
>gnl|CDD|468841 NF040906, GguB, sugar ABC transporter permease
NLRQYGMLIALVAIVVLFQILTGGILLRPLNVTNLILQNSYILILAIGMLLVIIAGHIDLSVGSVVAFVG
AVAAVLMVNWGMPWWLAVLLCLLVGALIGAWQGFWVAYVGIPAFIVTLAGMLVFRGLTLVVLGGQSIGPF
PDGFQKISSGFLPDLFGGTGLHLLTLLLGVLAAAALVWSQLRGRRRRIKYGLEVEPMALFIAKLVLIAAA
ILFFTYLLASYRGLPNVLIILGVLILVYSFVTNRTVIGRHIYAVGGNEKAAKLSGIKTKRVTFLVFVNMG
VLAALAGLVFAARLNSATPKAGNGFELDAIAACFIGGASASGGVGTVVGAIIGALVMGVLNNGMSILGIG
IDWQQVIKGLVLLAAVAFDVYNKRK
>gnl|CDD|468842 NF040907, ChvE, sugar ABC transporter substrate-binding protein
VGIAMPTKSSERWIADGNNMVKQLEAAGYKTDLQYAEDDVPTQVSQIENMITKGAKVLVIAAIDGTALTD
VLQQAADAGIPVIAYDRLIRGSENVDYYATFDNFKVGVLQGTYIVDGLGLKDGKGPFNIELFAGSPDDNN
AYFFFDGAMSVLQPYIDSGKLVVRSGQTDFDQVATLRWDGATAQARMDNLLSAFYTDKKVDAVLSPYDGI
SIGIISALKGVGYGSGDKPLPVVTGQDAEVASVKSIIAGEQTSTIFKDTRELAKVTVKMVDAVLKGEEPE
VNDTKTYDNGVKVVPSYLLEPVSVDKDNYKEVLVDSGYY
>gnl|CDD|468843 NF040908, CPC_1213_fam, CPC_1213 family protein
DNKMKKTKNNKKEDGKFKKKNIKHDPQAESARAVFGEPKAKT
>gnl|CDD|468844 NF040909, OadG_rel_small, OadG-related small transporter subunit. Members of this family are transporter subunits of small size, related to the N-terminal region of OadG the oxaloacetate decarboxylase gamma subunit. OadG itself is described the longer model PF04277
DLTFGLELLVVGMGGTFLVLGILYLVSKLLKKLFPV
>gnl|CDD|468845 NF040910, CD1375_fam, CD1375 family phage-related protein. Members of this family of usually small proteins are found typically in prophage regions of Gram-positive bacteria
MVKVYAYLVKAGRRTIEQVPEEYREPVAEYLAAE
>gnl|CDD|468846 NF040911, KGW_Acineto, KGW motif small protein. Members of this family of small proteins are found in the genus Acinetobacter. The family is named for KGW motif that is its best-conserved motif, at the midpoint of the 40 amino acid length sequence. C-terminal to that motif, the sequence is extremely hydrophobic. Members are found encoded next to a YqfO/Nif3 family protein. The function is unknown
MKNENYIDTVYLKQKGWFWFGLVVVLQILFIVGNYLVQ
>gnl|CDD|468847 NF040912, SGM_5486_fam, SGM_5486 family transporter-associated protein. Members of this family, found in the genus Streptomyces, regularly are found encoded next to an MFS transporter gene. Proteins average about 40 amino acids in length, with the last 25 extremely hydrophobic
PVLDPNPQNGQKKLLLVFGAMLGIFVVIGVIATIASP
>gnl|CDD|468848 NF040913, DsrE_rel_ELSE, SaoD/DsrE family protein. Members of this family are closely related to SaoD (see NF040732), and both families are distantly related to DsrE
MKVAYVFATPMAASYKLGKMILPQLEAGRHGAEVVGMFFFDDNTYVLRKGDPIGERLAKVAKEQGILLMM
CDQCALERGLAEGEPRCGTGEGRGKGTVEGVQVGCFPDLYAALSGNPPDQVITL
>gnl|CDD|468849 NF040914, Mrt_core, myxosortase core domain
LLLVLTQLLLVALPEEFFYRGYLQTRLDQLWPPRRRRLLGAPLGPAILLTSALFALGHLLTIPHPARLAV
FFPSLLFGWLRERTGGIGAPVVFHALCNLLVELLARHY
>gnl|CDD|468850 NF040915, CPBP_fam_mrtZ, MrtZ family glutamic-type intramembrane protease
SPEQARRLARTAVLATVGLYAGYGLMRQVPGPPLIAESRGAALIAGFYFLPGWMLRDQPELAARWQVGPD
GPIPPWRRSGWRWALGACLLIFPPFALGTWWFYWQVCQGDLRLLAPVLAVEQQTPWAGGLERFLERQCRG
HPGGFWPRGLYVPATWTSYYGLGFVFAVAVGLFAVALPEEVFHRGYLMSALEQRFPPRRRIFGVPFGWAA
VISSLLFALGHLVGMAQTARLATFFPALVFAWLWRRSDSLWAPALFHVASNLLMDLLLASTFRPR
>gnl|CDD|468851 NF040916, MamD, magnetosome protein MamD
MQDLLMAKVEGAMQAAQVSALAGQSATVGKVSAAGNGMGHWAFLTPTAAGQAPVAVKLEGARQVAELSAL
VGKTVTVGKAPTVIGGIGKWLALTPVAGGAAAAAAAGAGQLVMMKVEGAAQAVQLPALAGKSFTVAQPVA
AGTKAAGWLFLQPVGGGDLIALKVQNAATQTGGLVGKTFVVGPSPVMGGTTGKFLVLKPAAGGAGKAAGG
GAVAAKFAPAAVTGTGKAAAVGGGAAAALVAAGAAAVTATAAAGTGSTIWTGKGMSLGLGLGLGAWGPVL
LGAAIAAGGYGIYTYRKRRHGVADLSDDALLDAVSD
>gnl|CDD|468852 NF040917, Mms6, magnetic particle specific iron-binding protein Mms6
MPAQIANGVICPPGVPAGTKAAAALGEMEREGAAAKAGAGKVGAAKTGTAAAKAGAAKAAQAVAAPAAPA
NVAAAQGAGTKVALGAGKAAAGAKVVGGTIWTGKGLGLGLGLGLGAWGPIILGVVGAGAVYAYMKSRDIE
AAQSDEEVELRDALA
>gnl|CDD|468853 NF040918, LPFR_fam, LPFR motif small protein. This HMM describes an uncharacterized small, hydrophobic protein that is widespread in the genus Streptomyces. Multiple sequence alignment shows a well-conserved start site, patterns of conservative substitution of amino acids, and a best-conserved motif VTLPFRxxARLF. Coding regions for this protein have been systematically underreported previously because of small size, often less than 45 amino acids, and the lack of supporting evidence such as this HMM
MRAIADALRAIGGAIATVVTLPFRALARLFGGASG
>gnl|CDD|468854 NF040919, Clostri_philic, clostri-philic family protein. Members of this unusual, uncharacterized protein family are small in size (about 45 amino acids), rich in charged residues and therefore highly hydrophilic, and largely restricted to the genus Clostridium. We propose the name clostri-philic. The function is unknown
NNPMQKGERRQKLHENQNNVGNPKNPPEYENFDGEPIK
>gnl|CDD|468855 NF040920, CD1871A_fam, CD1871A family CXXC motif-containing protein. Members of this family typically are small proteins (often less than 50 amino acids in length) with a highly conserved C-terminal motif CLECxGIG that features an apparent redox-active disulfide bond. The N-terminal portion is hydrophobic and resembles a transmembrane alpha-helix
LLLLALGIAMIVYGVYRGEAAVVLSKAINICLECIGIG
>gnl|CDD|468856 NF040922, flgE_Caulobact, flagellar hook protein FlgE
MSINSAMLAGVSGLTANSAALAAISDNIANVNTVGYKRSQAEFQTLVTAQSAGAGYSAGGVLANTRHFIS
QQGLLQRTTSSTDLSISGQGFFVVTEKAENLTATDTRLFTRAGSFQVDNLGYLKNDAGLYLQGWPVDANG
VITTDPSDLTRLRSINVGSVGGTAEPTTRVQLNANLRSSQPVSAAASAVATVVDSATAVTYSPTGIATAY
DPATNSMAMYDPDTGTGVKPDFEIQIPVSDSKGGQRTLTLSFLKSDTPNQWYAEIRAVPAGDVVNGAALA
NGQLKSGLVAFTQDGRLDVDFMPWTAGGALFDDPANAALTFGASDGAAPAPGAGQVRWADALGIDAQTVT
FDLAASAGGLTQYDSQSVVQSVNTNGTAFGNLTNIEIDEQGYVTAIFDNGVTRRIAQVAIATFPSPDGLT
EVNGNAYRVSQESGTYNLKAPGTGGAGLIAPSQLEASTVDLSTEFTGLITTQRAYSASSKIITTADEMLE
ELINIKR
>gnl|CDD|468857 NF040924, small_MgtU, magnesium transporter protection protein MgtU
MRKGSLDKVFVQVVIIALILILLTVWIR
>gnl|CDD|468858 NF040925, LD_carbox_ElsL, cell wall-recycling L,D-carboxypeptidase ElsL
YTLEQADILIDLAQQTLYLPKHNKFYVISSGKNGIGEQENSGKTPRGWHRIAEKFGADAPKNSVFIARQP
TGEIYSSELAAQFPERDWILSRILWLDGLEEGFNQGEGCDTYQRYIYIHGTPDTEPMGIPMSHGCIRMRN
TDVIELFELVPEQALVYLSEHKLE
>gnl|CDD|468859 NF040926, small_YadW, small protein YadW. Next to a transporter, as common for small proteins. Supported by cross species conservation, proteomics, and ribosome profiling. Has some overlap with next gene, but hydrophobic then amphipathic, next to a transporter, looks good
MAIIIGLEFAQLPMSFGAKYE
>gnl|CDD|468860 NF040927, ABC_perm_SloB, metal ABC transporter permease subunit. Members of this family are metal ABC transporter permease subunits, including SloB from Streptococcus mutans and a number of others, closely related but characterized as acting on different panels of metals, and named in a variety of ways. The SloABC transporter, for example, is characterized as acting on manganese and iron, but its regulator SloR responds only to manganese
NFIEGLQQFHFLQNALITAVVIGIVSGAVGCFIILRGMSLMGDAISHAVLPGVALSYILGINFFIGAIVF
GLLASVIITFIKENSIIKGDTAIGITFSSFLALGVILIGVANSSTDLFHILFGNILAVQDIDKWITIGVS
VLVLLVIVLFFKELLITSFDPLLAKAMGMKVNFYHYLLMILLTLVSVTAMQSVGTILIVAMLITPAATAY
LYANSLKSMIFLSSTLGALSSVLGLFIGYSFNIAAGSSIVLTSALIFLISFFISPKQRFLR
>gnl|CDD|468861 NF040928, ABC_lipo_SloC, metal ABC transporter substrate-binding lipoprotein. Members of this family, such as SloC from Streptococcus mutans, are lipoproteins found in metal ABC transporter cassettes. The panel of metals bound and transported can vary from member to member but typically includes manganese, and names provided in publications differ as well. It appears that some members of this so-called LraI family of lipoproteins moonlight as adhesins
LLLLALLALVGLVACSNSKSSTAKNDKLKVVVTNSIIADITKNIAGDKIDLHSIVPVGKDPHEYEPLPED
VKKTSQADLIFYNGINLETGGNAWFTKLVKNANKKENKDYFAVSDGVDVIYLEGQNEKGKEDPHAWLNLE
NGIIYAKNIAKQLSAKDPKNKEFYEKNLDAYVAKLEKLDKEAKSKFAAIPENKKLIVTSEGCFKYFSKAY
GVPSAYIWEINTEEEGTPDQIKSLVEKLRKTKVPALFVESSVDDRPMKTVSKDTGIPIYAKIFTDSVAKK
GQEGDSYYAMMKWNLDKIAEGLSK
>gnl|CDD|468862 NF040929, quorum_TF_HapR, LuxR/HapR/OpaR family quorum-sensing transcriptional regulator. Members of this family are closely related quorum-sensing master transcriptional regulators in the genus Vibrio, and belong to the broader TetR family, in the genus Vibrio. Members include the virulence gene master regulator HapR in V. cholerae, LuxR in Vibrio harveyi, OpaR in Vibrio parahaemolyticus, and SmcR in Vibrio vulnificus
DSIEKRPRTRLSPQKRKQQLMEIALEVFARRGIGRGGHADIAEIAQVSVATVFNYFPTREDLVDDVLNYV
VRQFSNFLSDNIDLDLHAKDNLANITSAMVELVIQDCHWLKVWFEWSASTRDEVWPLFVSTNRTNQLLVQ
NMFIKAIERGEVCEQHDPEHLATLFHGICYSLFVQANRLQDEAAMKKLVDSYLDMLCIYK
>gnl|CDD|468863 NF040930, ABC_arch_GlcS, glucose ABC transporter substrate-binding protein GlcS
VVFYTWWATEGKVALDHLIPAFEKAYPQYTVQPELVPGAGGTNAKYAILALIEAGKPPAAFQAHYGPEML
SYVEAAPNGIKDFVNMTPIAQQMGLFNNAVPEVLEAGAYNGTMFSLPVNVHRGALLYINPQLLRKYNLPI
PTNLSTLIYDTVQLAEHGVSPWMVPGADGGWDQLNLWEDIFLSLAGPRLYNELMYGTLNLSNPTVQKIIN
ETNNLFLNFTSYDYPGWQSLTWTQGLALLIQGKAAFQANGNWLTNYAYDFLNTTTYPATPPYINWSNVTL
VAEPFPGTQGYYALVIDSVAVPVGPQEQAALTFAKFWSSYQGQEVWTKWKAVTYYKNGTDYYNTPAQWYD
YQQLLNLSSTPPQNFVYQLSDGGLFDDVFAQLISGLLTLQEVGSSYLSTWNSTLASAMHEEESEWLAAAK
LGLGYLGFPGHPFGGYLPPWVNP
>gnl|CDD|468864 NF040931, ABC_arch_GlcT, glucose ABC transporter permease GlcT
MALPTLFFGAILLYLVIWNVYYSFTNWSLLNSSPTFVGLSTYANLFSTYFFRSSLLHSLELSVGLVAIGN
ILGILFAGLLYFLKSNKQRSVYLSIFIYPLAISMAANALIWLWLFNPQIGIDWLLKRIGLPAIPWLSSTS
TAFPSLILVEIWAYTGLAALFYLASFMGVDKSIIEAARLDGAGPFKILFRILLPNSMNGFIVSTALLFLF
SFRIFSLPYVLSGGPTNPFLQTSVEYMYYLFTTEYFAQAAAVSTIIILIAAAVIIPYALLGIKRWVRR
>gnl|CDD|468865 NF040932, ABC_arch_GlcU, glucose ABC transporter permease GlcU
KYALHQLVLVILVIIWLIPLYAMVINGLKSNFEVLSTPVLVPPSKPTLSAYYTVWSGLAPPLINSLIVVI
PVALISTFLGAMGAYFFYRLSERHSILSDFLFSLIALATFIPYQATLVPLTRLEVSLGLFNTYWGLIFAL
LIFYIPTAALLMSIFIPVLPKYLIEAARIDGASDWTIFWKVVLPLTVPGFISTLIFIFIESWNNFFIPLV
LTTTPSMRLIPVAVRSYTGGYGTLYNESFAAAVIASIVPLLIFIFLGRYFIRGLAALGGGGK
>gnl|CDD|468866 NF040933, ABC_arch_GlcV, glucose ABC transporter ATP-binding protein GlcV
VTVRVENVTKIFKKGKKEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLV
ASPGKIIVPPEDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPR
ELSGGQQQRVALARALVKNPQVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLAD
RAGVINNGKFQQVGKPEEIYDNPANIFVARLIGDINLLEGKVEEEGLVDGNDLKIPLPNPKLEAGEVIIG
IRPEDIDISESDMRLPPGFVEVGKGRVKVSSYAGGVFRVVVSPIDDDSIEIIVNSDRPIEEGEEVNLYVR
PDKIKIF
>gnl|CDD|468867 NF040935, helicase_Hel308, ATP-dependent DNA helicase Hel308
MEFIDVDDLPLDEKIKDILKKRGIVKLNPVQTEAIKKGLLEGKRLLVTSPTGSGKTLIAELGMISHLLKK
GGKAIYVTPLRALTSEKYSTFKDWEKLGFKVGMTSGDYDTDDAWLKNYDIIVTTYEKLDSLWRHNPSWLK
EVDYFVLDEFHYLNDGERGPVVESVAVRAKRRNLLALSATISNYKEIAKWLNAEPVTTNWRPVPLKEGVL
YPERKKSFVVIFSDGTTIKLKGDDPILAYTLDVIEKGGQVLVFRNSRKMAETTARKIAELMNFVKLKDKE
LLELASRIKEVEDAGSNEKEDLYELIRRGVAYHHAGLSKGLRDIIESGFRERIIKVIVATPTLAAGVNLP
ARAVIIGDIYRFNRKILGFQEEIPVMEYKQMSGRAGRPGFDSEGEAVIVVRNKREAERVFKKYILSPPEP
IESKLGNESAFYSFLLGILSSEGELTEEELRDYAEETLLDKELVKSYLDKGINWLRENEFIAEDDDKLKL
TKFGRRVADLYINPFTAKTIKDYLTKNEKSCDLAYLHLLAYTPDGPLVSVSRNEEDELLDELDCPLFIEE
PEDEDEFYNYLSALKVALIVHDWIEEVDEDTILSKYGIGSGDLRSIVETMDWLTYSGYHVASVLDLEEHA
EVLRKLNARVKDGVKEELLELVKIPGIGRKRARLLYNNGIKKPEDIVMNPEKVKSLLGQKLGEKIVKEAA
RLIG
>gnl|CDD|468868 NF040936, hexpp_archaea, hexaprenyl pyrophosphate synthase
MDLIEFWLKSKETIDDLVEKFLNDVKDWELLEMSKYIMKDGKRFRGTLMFLFTEALGGEEKDAYKGALAT
EILHSASLALDDIVDYDLTRRGDKSAWAVYTNRRVIFVSNYLIPTALNIISSYGEDALKISIELWKDTAV
GALKDMYGNKEDYFKTIELKTASLFKLSTMLASFSSRREELLDELLDAGKYLGIIYQLIDDYVDCVKYER
EELVGSAKQLFELTGGKVEEFVKQEYAKLKESYLEIINSIPFRSEYRDLIISLPDFLAAGLLSEA
>gnl|CDD|468869 NF040937, HerA_Thermprot, DNA double-strand break repair helicase HerA
MIIGYVIGEATTQEATMLAEKPVRLGRYVVLEYDGVKVLGLITNVTRGSPLLDDSLNDVEIVQRLKKFDN
KIPQYIKAKIKLLCDLNGSGSQPDLPPVAGTPVRLATEEELKKIFSDGDIRIGKLIGTNVEVKIRVNSLA
RHLAILAATGSGKSNTVAVLSQRIAEIGGSVLIFDYHGEYYDSDIKNLNPIEPKLNPLYLTPREFATLLE
IRENAPIQYRILRRAFTEYKEEIREKIKEGEIDLSSLNSNFVEDLERKIDEQGKDEKQKSRKDSKDEVLN
KLEEFADRYSGIIDLTAPDIINRIKLGKVNVVDLSHLDEDAMDAVVSHYLRRILDSRKEFKRKGTGLRFP
VITVIEEAHVFLSKDENTLTKYWASRIAREGRKFGVGLIIVSQRPKGLDENILSQMTNKIILKIVEPTDK
KYVLEASDNLSEDLVEQLSSLDTGEAIIIGNIVKLPAIVKIDKFEGKLGGSDPDLIGEWKKAKEEEE
>gnl|CDD|468870 NF040938, KDG_KDGal_kin, bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase
MVALGEPLIELNALTPGPLRHVNYFEKHVAGSEANYCVAFVRLGNRCSLIARVGDDEFGYNIIEWLRGKG
VDVSHIKVDPESPTGIFFIQRHYPVPGRSESIYYRKGSAGSRLSPEDVDESYVRSADLVHSTGITLAISD
SAREAVFKAFELAKRRSFDTNIRLKLWSPEKARETIMRLLKEGVDFLITDPDDARILLGESDPDEAYRRF
SEYGVEVLVMKLGPKGAYVYYDGKKYFSPGYSVPVEDPTGAGDALGGTFLSLYLSGFPIEKALDYAVAAS
TLVVTVRGDNENLPSLEDAERFLKE
>gnl|CDD|468871 NF040939, trans_reg_lrs14, HTH-type transcriptional regulator Lrs14
KVKVKLPSGKEAGLIDALSFCYDISDTDFQVLKELIKGGEKTEDELAEMLKLSKASINRSLNKLVSIGFV
EREKDQSSKGGRPRYIYKAIDPEELLEKIIKDFKYCAKLFGEILPKEL
>gnl|CDD|468872 NF040941, GGGWT_bact, fibrinogen-like bacterial YCDxxxxGGGW domain. Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV
SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDGGGWTLV
>gnl|CDD|468873 NF040942, hypo_ExtJ, selenite/tellurite reduction operon protein ExtJ
MKKMMTLVAAALMTLALAAGAFAAGPFSGKVTKVDGEKVTVTVEKAVPAWVKKGAVVTAAGGMPTVVAVQ
GNEVTLKFSKAKAAKIKVDSTMSLSECEGDELQGC
>gnl|CDD|468874 NF040943, cytoc3_ExtM, selenite/tellurite reduction operon c-type cytochrome ExtM
LLLLLLLALAGCSPRAGEGSTCVSCHQGIELVSSSHPDCVSCHGGDPLAEDKEAAHRGMYGPKNPSDPEV
WEKTCGSCHPYQLDRVRSNLMYTATGMIKNIQLTWEGEDGRLYSSRGDELYDADGNALELKPVAELDNLS
GELYRKFCSLCHVGQESNQVYGASHASGCAACHFPYNDNATYEGNDPTVKGKWPYSASHAMEALPGNQVC
FRCHNRSGRIALSYQGLNDGNNSLVPTRNGYPGPVLISGLRNVTHIAPDIHHEKGMECIDCHTSRDIMGD
GYAYENMYLQTEITCEDCHGSADEPPRYREIARENDEPVRESASYQMQMRPGDEMVLTAKGRKYSNVFYE
DGKVWVLGKRSGKLFESKVITGTPEHTIVGHGRMECYACHSRTVVQCYGCHTEYDERETGMDFIKGVETP
GQFSETEDYRMLYPFPLALNQRGKISPVTPGCQTFVTVIDPDGTVSKDEYVARFKGKQQLRFAPFYGHNT
GKKAVGCAECHANPAFLGFGQHVVEGDSITGTLICEKSADKPLDGFLTLEDGKVRAFSAITRENSRPLNT
REIRRALAVNLCLVCHTKAKDPIYQKELDYRALDDCLHR
>gnl|CDD|468875 NF040944, MYPE2350_fam, MYPE2350 family membrane protein. Members of this family are membrane proteins as found in a paralogous family in Mycoplasma penetrans. Note that Pfam model PF07666 described this family first (incorrectly calling it family 26 instead of family 6), but that model also pulls in a large number of apparently unrelated hydrophobic bacterial proteins as well. This model is designated equivalog in order to give it higher precedence as an annotation rule than other rules that are less specific
FKKIRKISPLIVIFYIMGVAILIVALLTYVPAIEDRKYLSNNFYEFSPQVNTGWNVGIILIALASIFYIA
MFVLEIFLTIKVSSAKGKHPEFQDITVHKILLIIGIVILPIFSIIDCFILYSKSSKIL
>gnl|CDD|468876 NF040945, CCC_membrane, CCC motif membrane protein. Members of this family average about 150 amino acids in length and are hydrophobic, with several probable transmembrane alpha helices. A notable feature is a Cys-rich cluster, often CCC, starting at about position 22. Members of both this family and NF040944 previously were both included in Pfam model PF07666. But while both families are hydrophobic, they appear not to be truly homologous. NF040944 identifies members of a paralogous family in Mycoplasma penetrans that includes protein MYPE2350, and consequently some members of this family have carried names suggesting (improperly, we think) a relationship to that family
NATLVLVLGILSIVCCCCYGILGLILGIIALVLANKAEKLYQENPELYSNYSNVKTGKILAIIGLVLNVL
YLLYTIYYIATIGWDALQEQLQEMMEEYQ
>gnl|CDD|468877 NF040946, PSII_PsbP, photosystem II reaction center PsbP
LKRIAAILLLVLSLTLSGCCSSGTAGLQSYVDSDDGYEFLYPNGWVEVKVSNGPDVVFHDLIESTENVSV
VISDVPEDKTLEDLGTPTEVGYRLLKNVIAPPGSGREAELINAESREVDGKTYYLLEYAVKLPNQQQRHN
LASVAVSRGKLYTFNASTPERRWDKVKDLFETVVNSFTVY
>gnl|CDD|468878 NF040947, trans_reg_LysM, HTH-type transcriptional regulator LysM
LDEKDEKILEILKRNARASYVDIAKELGLSESAVRKRIKKLIRLGVIKRFTIEYGLENEISAIVLVRTNP
TIPTPEVSKKIAKLPGVEVVYEVTGDYDILAIVRATNISDINKCIDYIRSIEGVSGTNTMIVLRTW
>gnl|CDD|468879 NF040948, alpha_gluc_MalA, alpha-glucosidase MalA
MKILEESNVGIYRILINDPEPPVDFPFGGELSAEKCLKDFGLEIEEGGGGLVVEKPLGLKEHVLGLGEKA
FELDRRRGRFIMYNVDAGAYTKYSDPLYVSIPFFISVKGGKATGYFVNSPSKLIFDIGLERYDKVKITIP
ENSVELYVIEGPTIEEVLETYSELTGKPFLPPKWALGYQISRYSYYPQDAVVEVVDELRKEGFPVSAVYL
DIDYMDSYKLFTWDKEKFPDPRKFIEELHSRGVKVITIVDPSVKADQNYEVFRSGLGKYCETENGELYVG
KLWPGNSVFPDFLNEETREWWAELVEEWVKQYGVDGIWLDMNEPTDFTEDIERAALGPHQLREDRLLYTF
PPGAVHRLDDGKKVKHEKVRNAYPYFEAMATYEGLKRAGKDEPFILSRSGYAGIQRYAAIWTGDNTSSWD
DLKLQLQLVLGLSISGVPYVGCDIGGFAGRSFPIDNSPELLVRYYQAALFFPLFRTHKSKDGNDQEPYFL
PSKYKEKVKRVIKLRYKFLPYLYSLAWEAHETGHPIIRPLFYEFQDDEDAYRIEDEYMVGKYLLYAPQIY
PKEESRDVYLPRGKWLDFWTGEEYEGPSWIESEAELPIYIREGSAVPLDGDLLVYGNGKSIIYYDG
>gnl|CDD|468880 NF040949, minchrom_main_MCM, minichromosome maintenance protein MCM
LGEKFKEFIRTFRDSFGNEKYKERIFEMIAMRKRSLVVDFNDLYMFDPELADLLIEKPDEVLPAASKALK
EIVEEEDPEYAEEVAKFHVRFRNLPRTVPLRDLRSEYIGKLIAVEGIVTRTTPVKPRIVKAVFRCRDCGC
EFEWPEEEEESYEIVEPPTVCPVCGKPGSFRLLQEKSKFIDWQKIVVQERPEELPPGQLPRSIEVVLEDD
LVDTARPGDRVTVTGILRIKPDSSLKKGSRPIFKNYIEANHIEVSQKELEEVEITEEDEEKILELAKDPW
IREKIIASIAPSIYGHWEIKEAIALLLFGGVPKVLPDGTRIRGDIHVLIVGDPGTAKSQLLQYVARLAPR
AVYTSGKGSTAAGLTAAVVRDKLTGEYYLEAGALVLADGGVAVIDEIDKMREEDRSAIHEAMEQQTVSIA
KAGIVATLNARASVLAAGNPKFGRYDPNRSVAENIDLPPTILSRFDLIFVIRDKPNEERDRRLARHILDV
HSGKEKVKPEIDPDLLKKYIAYARKYVRPKLTEEAKKLIEDFYVEMRKSSKSSEDPDSPIPITARQLEAL
IRLSEAHAKMRLKDEVTAEDAERAIRLMLAFLESVGIDVETGKIDIDTIMTGKPKSKREKMSKIVEIIKE
LEEEEECVKIKELIKEAEKKGIDEEKVEELISDLKRSGEIYEPRPGCYKKV
>gnl|CDD|468881 NF040950, archin_ph_syn, archaetidylinositol phosphate synthase
LNKLRPQVKKILEPIAKPLAKIGISPNQLTILGLLVALLYVAYFFYTGNPLLGALFIALSGLLDALDGAV
ARATGKVTRFGAFLDSTLDRFSDAAIIIGLYFGGFVPWLVGLLALIGSLLVSYVRARAESLGIKMEGVGI
AERGERLIIILIAALLYILLALIISAIAVYLLAILSWITVLQRIYHVYKAL
>gnl|CDD|468882 NF040951, CRSPR_nucase, CRISPR system ring nuclease
MAKVHVCAVGTSLLKNSLDDDRVRKEVERLGLKDWDRLKFDDDRQNRIKSNFDRLEPLLLNFLKSKGKVA
SAELDSLFSAFEKLKHDKEEIYVFLYSTNTWNSQLAGEVIKDYLDEEGIRSELVTVKTISSEETFYEGIE
DLFDKVIYKILKFKEQGNEVYINATPGLKPETIFLTLAGLLAGADLIYYKYQEFNDVVILPSPPITISPK
YLEWLIRFANSGYTLSEKRAEELGIPVRVLETKNLVERKGEDAYRLKDWVRKLLGIYLPIGAQNSYYKVI
VEGEGEKVFNNEVEAYEYMEAKRKEGKRVRVEVPDKVYFLGL
>gnl|CDD|468883 NF040952, Arch_mtprotase_TldD, zinc metalloprotease TldD
MKLLKRAEELGATFADIRYERVKELSLTVTEDRKQVTSNGIDEGYSLRVLYNGNWGYKSTTELTEDEVKK
AINSAYGDENVNIVYLPSKHDRVKIKPKKPVNKSPEEKMNDLRKIKDEVFNLDPRIKSVNVRYYEETIHK
EYYSSEDREIEQDYNISGLSIRAVAREGDVVASASESLSTYLGYPLEVFDINEILETLKRRIENQLKGKT
PKAGEYPVVLAPEVVGVFAHEALGHLAEADLAVNGILGKLRGKKIAPEFVNIVDSPLLDYPMAIGITPYD
DEGVEGREVKIIEKGVVKEFMVDRYYSAYLGEKPTGNARAEDFRSPILIRMRNTYMKPGDMSLEELLEEI
KEGYLLVSPLGGQTSPDGTFQFGIQEGYRIENGEIKEPLRNVGISGYTIETLGRIDGVSKDFGVWPGFCG
KGGQSVPVGTGGPYIRVKKVKVG
>gnl|CDD|468884 NF040953, Arch_udg, type-4 uracil-DNA glycosylase
LEDIAEEIRKCRKCPLHKTRTNAVPGEGNPNAKIMFVGEAPGRNEDETGRPFVGAAGKLLTELLESIGLK
REDVYITNVVKCRPPNNRDPTEEEIEACSPYLLRQIEIIKPKVIVTLGRHSTRYILSLAGLEFESISKVR
GKVYEVEIGGGKVKVIPTYHPAAALYNPPLREELEEDFRKIKE
>gnl|CDD|468885 NF040954, Arch_KDGaldase, bifunctional 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase
MEIVVPIITPFRKDGKIDVEKLKTHAKNLLRKGVDAIFVNGTTGLGPALSKEEKRELLEAAYDVTNKVIF
QVGSLNLDDVIELVKYANDFDIIAVASYPPYYFPRLPEKFLVKYFRDICEASSHPVYLYNYPAATGRDVD
AKLAKEIGCIKGVKDTNEDLAHTLRYKRLLPNMKVYNGSDSLAFASLSSGLDGVVASAANYLPEVLVKIR
EAIKAGDVEKALRLQFLIDEIVELARKYGQLSAIYELVEEFQGYDVGYPRPPIYPLEEEERAALKKEVEK
IKKKLELL
>gnl|CDD|468886 NF040955, Arch_DPS, DNA protection during starvation protein
KKVGREVVEKAGVDVDKLVELLVKNAAAEFTTYYYYTILRMHLTGLEGEGIKEIAEDARLEDRNHFEALV
PRIYELGGKLPRDIREFHDIAGCPDAYLPENPTDIKNILKVLLEAERCAIRTWTEICDMTFGKDPRTYDL
ALAILNEEIEHEAWFIELLGERPSGHFRRGEPGESPY
>gnl|CDD|468887 NF040956, Arch_Xpf_endonucase, 3'-flap repair endonuclease Xpf
MLRIYADYREKQSGIPDILKELGAIVIFQQLTVGDYVISDDVAVERKSVEDLVNSVFDKRFFDQLSRLSE
AYRKPFILIEGDLERIRKITSKWKAINSALISAIVDYDVKVLYSSDKRESAEVLYKLAEKFQEDGNKRKP
ISLHDKPKFESLKDMQLYVVESFPNVGEKLAEKLLEKFNTIRNICNASISDLEKVLGSRKKAEELYKILN
TPFSSKNDDKSN
>gnl|CDD|468888 NF040957, Arch_PMK, phosphomevalonate kinase
MISAPGKVLWIGSYSVVFGGISHVIAINKRVRCEITESDKLIFETSYGTFKEKGNELIESVLSVFREHLG
DIPKLHVKLINDEDFQIDGKKTGLGSSSASTVALTACLYYYVKGKIDLDEIHKLSQKANYIRQKGIGSGF
DIAAAVYGSVVYRRFTDLNKVDSYVEPLRLGNGYEILLGFTGRSSDTVNLVRKFIEKSNLERFKELMREI
EIENEMAIKLLKLGKLDEAIPHIKLARKYLNLLAEKVVGVELESEEERKLIKIAEKNGALIALSPGAGGG
DSIFALGEDLSRVREAWEKIGIKVIEVKEDEGLRVE
>gnl|CDD|468889 NF040959, MamA, magnetosome protein MamA. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family typically contain five tetra-trico-peptide repeat (TPR) motifs. Based on structural analyses, MamA forms a large homooligomer through self-recognition to regulate protein-protein interaction in magnetosomes
DSLSLYAHSFLLVSGRILNNMVNGYNRLFSLSDRDRAKMYRNKGISHAKKGRYDKAVRYLEQVARIDPDD
VEALYRLGVAYLKTGQYDRAIKVLEKVLSLAPDHVKAAYRKGVALLKIKDYEKAVEDLEEALEEKPDNFN
LNYRLGLALDGLGQYDKAIEAFQKALELDPNEIKYHQAIGFMYVQKGDHETAAEHFKKAMELEE
>gnl|CDD|468890 NF040960, MamE, magnetosome formation protease MamE. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family are serine proteases involved in the maturation (membrane growth) of magnetosomes through cleaving magnetosome proteins
FIYRQSSGGLRLGAMLEQMGHGAGAVNVPAATAPAMSVPAGARVGPPSAAGAIATLPPVVDFGPAQVGSG
GGFSSVVTLLRNSVVSVTASSSGGQAMPDPLGLANPDGLPRFANPTTRSVENIGTGVIVRDDGFIVTNYH
VVRGANSVFVTVSDDAGSTRYSAEIVKMDEALDLALLKIAPKAPLTAAVLGDSDAVRVADEVIAIGTPFG
LDMTVSRGIISAKRKSMVIEGVTHSNLLQTDAAINQGNSGGPLVIANGTVIGINTAIYTPNGAFAGIGFA
VPSNQARLFVLDEVGWLPTSTAEGPSMGLVAMQRPGGGGVGAAGPAIMAGVPAPHTDGRQNMDCTNCHQI
IPAGAGPQAPMMPVAAPNPPPPIPANAVSPHTDGRQNMNCASCHQIIGAGAGPIGQPGGGGYQFAQPPGS
LAINVQGPRGGQAAGAGPGRHTLLGAALAPMSQQLSLQTGLPAGRGVFVTGVSPNTPAASAGLRPGDVLL
KVDGRPVALPEEVVAIMAEMPNGRSVRLGVLRDGDVRNMTLVAGPAVQAPAAPNQNPMGGVAPVRPGVPA
KPPKPPTEFNWLGMEIETFQAPPPMNGVPGEPPVRGTGAQVAEVLAGSRAAVAGLQANDLILEVNNRPVT
GPARLDAAIKAATKAGQQILLKVNRNGQEFW
>gnl|CDD|468891 NF040961, MamO, magnetosome protein MamO. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family are essential in the formation of bacterial magnetosomes. MamO promotes crystal nucleation and activates the MamE protease
MIEVGETSGDLPTNKIVFCERSWRVPVVILAFLVLVTFAWGIYLLDDYREDDYFPGADDLSVGQFLFRNV
AMPDVQRLYQTVPPAVVGIGGGGINAGPVASGALVGSNGYVITALHLVQNLPEIQVRVATPGGIRDYPAQ
VVKVIPEHDLALLKIQTTDKFLYFRLADTQTVVPGQQVFAFGDNMAGAPIVRQGVVQSADAPLAVGTLQI
THLLRTDAIYHWEQTGGPLVNRQGDLVGINVAVQGPTGRVEGFTVPAHVIVAHFQDVVRFKTGGAAAAAA
PAPAAAPGMPDNQGVAASGVAQPPGTQTVPMGSSDAWWSKARAVVGGQTPLGMNVAVQPQAPPSTPSGMP
FLDTDHSGGARIFGYSVADIFGLMLLALVAGVTGGMMTMGGGVLQVAGMMVFFGYGMYLIRPVAYLTNIF
VYGAAALRNDKAGLVQWDKVKPLIPWAVAGVVAGYFIGNALGDSVIGMLLGLFALLMAIKAVLEILEPNA
GEITLEAIKTAEAEDEMDELFALAEGESRPKPEGLWLPTRSAVLGLPMGLISGILGISGGVVEVPLQRYV
GRVPLQNAIANSAVLVFWASVVGSVVAFWHGVSTGLIDWEAPVTLALIMIPGAYVGGMIGAWLMRVLPVR
VLRGIYAALMAAIAVKML
>gnl|CDD|468892 NF040962, near_HgcAB, HgcAB-associated protein. Nearly have the members of this mostly archaeal protein family occur in species with methylmercury formation proteins HgcA and HgcB, encoded next to HgcA
CCRVEAIVSVDERGQMVLPKEIREKAGIKPGDKLALISWEKDGKICCLSLIKADELSGMVKDVLGPLLKE
>gnl|CDD|468893 NF040963, MamI, magnetosome protein MamI. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. It has been reported that proteins of this family were involved in magnetosome nucleation in MTB and were essential for magnetosome formation
MPSIIFGLLAIALGLWGIYAWWWSVVDLLRGGVPVALVIFGLVALLAGVSTVREPRQEKESDSEEDIDG
>gnl|CDD|468894 NF040964, MamK, MamK family actin-like protein. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family include the magnetosome protein MamK, which is encoded by the mamK gene on the magnetosome island (MAI), and MamK paralogs/homologs. It has been reported that MamK and MamK paralogs are important for magnetosome chain formation in MTB. MamK family proteins can also be found in bacteria without magnetosomes
LLVGIDLGTSRTVIMSDRGVKTMVRSVVGYPKDIIGVKLLGRPYVVGDEALKKRSYLDLRYPLEDGVLKE
YSERDEEVARHLLQHVIKLAEPQAGEEVCGVIGVPARASAANKKLLLKITQEVLDTVMVVSEPFMVAYGL
GKLNNALIIDIGAGTVDICAMKGTIPGPEDQITLTKAGNYVDEVLENLILERYPDVQMTANMARAIKEQH
AFVGAPGERVTAELRVAGKPVTCDVTDELRQACETIVPDIVEGIESLIASFDPEDQAEALKNIVLAGGGS
RIRGLDTYIEEYLREYGDVRVSRVEDPLFAGAAGALKLAQELPPEYWDQLGDV
>gnl|CDD|468895 NF040965, MamP, magnetosome magnetite formation protein MamP. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. The MamP protein is involved in biomineralization through redox-control of magnetite formation in MTB
MNSKVKLIVVGLLLALVLVILAGFFSLSDAIGRQGAVAPQSSGSPSQAPPASPVAAPVAFVQPVTPPVQG
PAVPVQPQPATQGGASPAAEQSPLPNFVPPKLQLFEGHWQGLDARPLTEELARKLNYPLGLEGLLVDEVT
LNAAASGLLAGDVIVAVNDTPVTDLEEFQAATRRVANRKEARIAVYRKGKRPGGPVMRKLTVVLVAEPDL
GFAQLEGAPMILPGDPRPHPYRGPCTQCHAIGQGFELTPDPDLISLPPPPIRRGAVARGVSPHRDRGPCE
ACHIIQ
>gnl|CDD|468896 NF040966, MamQ, magnetosome protein MamQ. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family are essential for magnetosome formation
SVLSVLVFFATLLYRYNEFVTMREDAQSKRSNFEVAIQRRNNLFGNLVNLTLNHAALEHSVFSHTSDKRT
EIIKGGKKKPEGAKAEQLLKQGGLGKGNMGGGKALLGADGGFGAALGRLLAVVEQYPDIKSAKTYKQMMS
SLVEMEDRIANRRVEYNESARIYNTEISKFPWKYLAKITGFKRREYFHQGQEGDAIINAPIVTPEIYQQL
LPLDHAQGGKK
>gnl|CDD|468897 NF040967, cytc_ExtN, selenite/tellurite reduction operon c-type cytochrome ExtN
MRWIVVLIALLLLLLSPAPAAGENCRDCHRKALTGVHAELACADCHGGDRETLADPASLAARAAGCVGCH
QGYDGIFDQAMTTREAEKAFVARSWGRADPDFFQNNCASCHVSGCLDCHGGDGHAIARPTDEDCLSCHRG
YFVGADYYGYAPREDAPRYQRGPQALGEHYLKMRPDVHAEAGMECGDCHSMASLAAGKKAAKGCRDCHEP
DPSVIEHRIAAHLEKLECYACHSAWAAQEYGTFYLRFTKGSPEQEYFRVRTDQTAEDYVKSAYLRRQDAP
PLGLNERGRVSPIRPQFIAYFSDIRGERVVGEENRLLAAQWKAFFPHTVRRGTVMCDGCHDNPRRFLLEN
PEDRIYRPDADGLGLPSFWDQQGQRVVNGSFYSPARFRRMSRKDAAYTKAYVEKWKKLLGHVEASS
>gnl|CDD|468898 NF040968, FeS_ExtO, selenite/tellurite reduction operon b-type cytochrome iron-sulfur cluster-binding subunit ExtO
MRWIVVLIALLLLLLSPAPAAGENCRDCHRKALTGVHAELACADCHGGDRETLADPASLAARAAGCVGCH
QGYDGIFDQAMTTREAEKAFVARSWGRADPDFFQNNCASCHVSGCLDCHGGDGHAIARPTDEDCLSCHRG
YFVGADYYGYAPREDAPRYQRGPQALGEHYLKMRPDVHAEAGMECGDCHSMASLAAGKKAAKGCRDCHEP
DPSVIEHRIAAHLEKLECYACHSAWAAQEYGTFYLRFTSGPVQEYFRVRTDQTAEDYVKSAYLRRQDAPP
LGLNERGRVSPIRPQFIAYFSDIRGERSVGEENRLLAAQWKAFFPHTVRRGTVMCDGCHDNPRRFLLENP
EDRIYRPDADGLGLPSFWDQQGQRVVNGSFYSPARFRRMSRKDAAYTKAYVEKWKKLLGHVEASSPR
>gnl|CDD|468899 NF040969, cytb_ExtP, selenite/tellurite reduction operon b-type cytochrome ExtP
MLNDLALHLVPRHVPRRALKFSYTWCLGGLTFLLFVILTVTGIFLMFYYVPTPEAAYESVQYLQNEVAFG
QLVRNMHHWAANLMVVMVFLHMLRVFYTGSYKPPREFNWVVGVGLLVLTLGLSFTGYLLPWDQLAYWAVT
VGTNIAGSIPVVGTLLQLLQLGGSEVGAATLTRFYALHVFVLPAALIILMAAHFWRIRKQGISGP
>gnl|CDD|468900 NF040970, memb_ExtQ, selenite/tellurite reduction operon b-type cytochrome membrane protein ExtQ
YVKSSPHFFRPIKRAFVLLTLALLLLAALIPAPLQEPADLARVPNPVKSAWFLLWIQELVSYSNYLIYLI
LALGLFFLLLPWLPRGRPAERARWFGREQRLVNLLALASFAAILALTVVAMFFRGENWSFVL
>gnl|CDD|468901 NF040971, cytc_ExtS, selenite/tellurite reduction operon c-type cytochrome lipoprotein ExtS
MVLRLALLILVLLLLVLCCAAAAPGDPCLSCHPPHYAELGSCVDCHRGDPRSSRLEIAHGGLIPARYSWF
TLPGSAPVESGKRLLDEFACRRCHTIGGRGNRLASNLDRLAQTTTPEELAEAIREPVLFMPDFHFSEPQL
IELVNAILAGGRQVGGKGTEQGPLVVHFEGERTKEENVFEKHCGGCHRALTAARGGLGRGTVAPNLSGLF
TEFYPPTFRDDSPWTRENLEKWLKNPRKIRPATQMRPVPLKKEELRRLLDIL
>gnl|CDD|468902 NF040972, T6SS_VF_TecA, type 6 secretion system effector deamidase TecA. TecA (T6SS effector protein affecting cytoskeletal architecture), a type 6 secretion system effector confirmed as a virulence factor of Burkholderia cepacia in a mouse model, is a deamidase that inactivates RhoA and other Rho GTPases in host cells
MQLTQLGGHVAQSGIAERQKHAQALMYGMANIDEYVSRGVCYDAAAYVRYLLRGDGLITPGTLLDTTGQL
WRTRFNFENGGQWDGRASIPAGTAVGFSRGGNVFHAAIAVGGTRIRAVNGGRLGSGWLRPVDLARVLEPD
EGGGFLYDRTNIRVHLSRL
>gnl|CDD|468903 NF040973, restrict_Sau3AI, Sau3AI family type II restriction endonuclease. Members of this family include type II restriction enzymes such as Sau3AI, while excluding proteins more closely related to the DNA repair protein MutH. Both Sau3AI and MutH endonucleases act on GATC sequences
YDTEEIVHYRAKELIGKTFKEIDKKGRLNNKKNKGSLGNLIEESYFGYEPNSDAEPDFKEAGVELKVTPI
KKNKKGGKYSAKERLVLNIINYMEEIKEDFEESSFWKKNKNILLIFYLYEKGVKKKDYKIKKVVLFTFPE
EDLEIIKQDWETIVQKIKEGKAHELSEGDTNYLGACTKGANAGKSLRQQPFSEILAKQRAFSLKQSYMTY
ILNNYILGEKEEYESIIKTPELLKKNTFEEIVIEKFNPYIGKSVEELAKEFDIEVNAKAKNFISNLISKR
ILGIKGDNLDKIEEFEKANIVIKTIRLEPNGKPKEDMSFPAIDFKELVNEEWEESTVYDYFEETKFLFVV
FKENEEGKLILKGAKFWNMPEEDLEGEVKKVWEETKDIIKEGVELTYKPNKKLIIKNNFPKKSFNKICHV
RPHASKSKYEGTGNLSDTDELPDGRRITKQCFWLNKKYIKEIIK
>gnl|CDD|468904 NF040974, RepABC_RepC, plasmid replication protein RepC
MESGLVTTPFGRRPMTLALLASQAAAEEIPPGKTVDKWEVFRALCEARPVLGLTDRALAVLDALLSFYPE
DDLSGEARLVVFPSNAQLSLRAHGMAESTLRRHLARLVEAGLIARRDSPNGKRYARRGRGGEIEEAYGFD
LSPLLARAEEFEALAEEVQAERRALRRLRERLTLCRRDIAKLIEAAIEEGVPGDWDGFQDRFRLLVRRLP
RKASLAELEALLAELEALREEVRNTLEIHPKTENLSANESQNERHIQNSNPDSTNELEPASEKSQGAKPS
PADEPRAEPLKALPLGLVLKACPEIQSYAPGGAIRSWRDLMSAAEVVRPMLGISPSAWEEACEVMGPENA
AIVLACILERAGHISSPGGYLRALTEKAREGEFSLGPMLMALL
>gnl|CDD|468905 NF040975, leader_RepB_LM, IncL/M-type plasmid replication leader peptide RepB
MRTLLQYSPANMCRGW
>gnl|CDD|468906 NF040976, RepC_IncLM, IncL/M type plasmid replication protein RepC
SRVTERQELKSNLEKQRDYRNRIRETHDQLNLYLPKDAKRMLIEITKVKKLTQAEVIEFLVKSYYDGLKF
DDSEE
>gnl|CDD|468907 NF040977, RepA_IncFII_LM, plasmid replication initiator RepA. Members of this family are the plasmid replication initiator protein RepA, as the term is used in IncFII (see TIGR03474) and IncL/M plasmids. Other RepA proteins may have no readily detectable homology
KNPNPVFTRPAHYKKLPGFIGKAMNRAVKKDKARSRLRYSRHPYFVKTRSAAGRKRAFRPERRRAIDALL
QAMLSHVDIATGRVTASVEQLADECGLSTKSKAGNVSITRASRLITELERFGLIKCETEWDRINGCYIPK
HITLTPAFFRLLGVSMDKLLAAQEQRLEWENKGLIKKGLEPISVKEARRRWYEQHRKRALLYRREKAAHG
KKRRRARRLAKLPEDDRRHEILRALVKTYPAGELYALGPEGLRKLVWQRLYQLRL
>gnl|CDD|468908 NF040978, Ve_IatC_Nterm, inverse autotransporter adhesin IatC N-terminal domain. The inverse autotransporter (type Ve secretion protein) IatC contains a central region that is variable in the number of repeats seen, and averages about 3000 amino acids in length. This HMM describes a mostly non-repetitive region N-teminal to the architectural differences from different repeat counts are seen. IatC can contribute to biofilm formation
MAGKAHGNGDRRGDKTICGLGDRLRRLTAGICLITQTIFPVMAAAPTHINPAHSDTAASLILPNVKTIPY
TLGALESPPTVAARFGITVDELRRLNQFRTFARGFDNVRQGDEIDVPLINSNSPEARNLKAMQMERDGKD
PQMQVAEMAQQSGTLLARDMDSEQAASMARGWVASSASAQATDWLSRWGTARVSLGVDEDFSLKSSSFEF
LHPWYETPDNLVFSQHTLHRTDDRTQTNHGIGWRYFTSSWMSGVNMFIDHDLTRYHTRTGMGVEYWRDYL
KLSGNGYLRLSNWRSAPELDNDYEARPANGWDLRAEGWLPAWPQLGGKLVYEQYYGDEVALFGKDERQND
PHAITAGLSYTPVPLISFSAEQRQGKQGENDTRIGMELTLQPGHSLQKQLDPAEVAARRSLAGSRYDLVD
RNNNIVLEYRKKELVRLTLTDPLKGKPGEVKSLVSSLQTKYALKGYDIEAAALQSAGGKVAVSGKDIQVT
IPPYRFTAMPETDNTYPIAVTAEDSKGNFSRREESMVVVEKPTLSLADSTLSVDLQILLADGKSISTLTY
TARDSSGKPIPGMTLKTHAKGLQDFALSEWKDNGNGTYTQIVTAGKTSGALSLMPQFNGDDIAKTPALIA
IVANMASRADSMIETDQDNYVAGKPIGVKVTLKDDNGNGVTGRKELLKQAVKVDNTKADAVSAWTEESEG
IYKANYTAHLIGDKLTAQLTMPGWQTKHSDAFSIAGDKDTAKIAAMQITANNAVARRDHNTVAVTVRDVH
QNLLQGQNVTFTVVNGAAVFADPNGGIVTTDKDGIASVNLASDQAVNSLIKAEINGSSQSVEVSFITGDI
SQLTSTIKTDDVSYTAGGKIKVSVTLMDEQKNLVKGMASLLAGSGVVEVSGTDKNETGNWSEESDGVYTT
TRTAKIAGDRHYATLKLSTWSSAQQSDAYAIRESGAVLAYSSIVTDKTAYTAGGAIKVTVTLKDSYENLV
GGQRDAINLAIQLPNTKAESIAWNEDQKGIYTATYTALLPGTGLKAQLQMSGWANALTSNDYSISGDAAS
AQIVAMQVTTGNLDV
>gnl|CDD|468909 NF040979, Ve_Ilp_Nterm, inverse autotransporter adhesin Ilp N-terminal domain. Ilp (Intimin/invasin-Like Protein), as found in Yersinia, is an inverse autotransporter (type Ve secretion protein) that can have over 40 repeats of the Bacterial Ig-like (BIG) domain (PF02369) and has an average length over 4000 amino acids. This HMM describes the non-repetitive N-terminal domain
MLNYFRAILISWKWKLSHHTSRPHDVKEKGHPRKIKVVAWITLFFQFAFPLSLSFTPAIAAANTTNSAPT
SVITPVNASILPPAARATEPYTLGPGDSIQSIAKKYNITVDELKKLNAYRTFSKPFASLTTGDEIEVPRK
ESSFFSNNPNENNKKDVDDLLARNAMGAGKLLSNDNTSDAASNMARSAVTNEINASSQQWLNQFGTARVQ
LNVDSDFKLDNSALDLLVPLKDSESSLLFTQLGVRNKDSRNTVNIGAGIRQYQGDWMYGANTFFDNDLTG
KNRRVGVGAEVATDYLKFSANTYFGLTGWHQSRDFSSYDERPADGFDIRTEAYLPAYPQLGGKLMYEKYR
GDEVALFGKDDRQKDPHAVTLGVNYTPVPLVTIGAEHREGKGNNNNTSVNVQLNYRMGQPWNDQIDQSAV
AANRTLAGSRYDLVERNNNIVLDYKKQELIHLVLPDRISGSGGGAITLTAQVRAKYGFSRIEWDATPLEN
AGGSTSLLTQSSLSVTLPFYQHILRTSNTHTISAVAYDAQGNASNRAVTSIEVTRPETMV
>gnl|CDD|468910 NF040980, Ve_Inv_Crono_N, inverse autotransporter invasin Inv N-terminal domain. Inv, as the term is used in Cronobacter sakazakii, is an inverse autotransporter virulence factor that mediates invasion of host cells. Member proteins can have variable numbers of the Bacterial Ig-like (BIG) domain (PF02369). This HMM describes the non-repetitive N-terminal domain only
MHEQSIMEKNTLKISLLKKIIIWAQILLQIAFPLLVLPAHASSGPGATETDMSDASTLSASLASSAAQNG
ADAMKNTATHLATTHAASTVEEWLSHFGTAQVTLDVDDNGNWDNSAFDFLAPFYDNKKSVLFTQLGIRAP
DGRTTGNIGLGVRTFYVRDWMFGGNVFFDDDFTGENRRIGFGAEAWTNYLKLSANTYIGTSQWHNSGDFD
NYNEKPADGYDVRAEGYLPSFPQLGAKLMYEQYYGDNVALFDKDHLQSNPSAVTVGLNYTPVPLITAGID
YKRGQDSMDEMKFSLNFHYALDSSWQSQISPEQVATRRSLAGSRYDLVDRNNEIILQYKKKATSKAVADM
>gnl|CDD|468911 NF040981, Ve_YrIlm_NTERM, YrIlm family inverse autotransporter adhesin N-terminal domain
RKLKIIAWGNILFQLLFPLSLCFTPAIAAAPTSLTSNANIPSTEPYILGVGENVDSVAKKYGISVDELKK
INIYRTFSKPFNRLSAGDEIDVPRKASPFSIDNDKNNTDIDIPLDHALAGHAQTGAAALASGDAAKSAAQ
LARSAANNEFNSSAQQWLSQFGTAHVQLNVNDDFHLDGSALDVLVPLYDNQSSILFTQLGARNKDSRNTL
NIGAGVRAFLGDWMYGMNTFFDNDVTGKNRRVGVGAEAWTDYLKLSANSYFGTTDWHQSRDFADYNERPA
NGYDVRAEAYLPAYPQLGGKLMYEKYQGDEVALFGKDDRQKNPHAITAGINYTPIPLFTVGAEHRAGKGS
HNDSRINLQFNYRLGESWQSHIDPSGVAASRTLAGSRYDLVERNNNIVLDYQKQDLIGLTLPEQVTGESS
SSATVNAQVTSKYGLERIEWDSAALMAAGGNLVQVSPQTVSVTLPPYQATRSSNTHT
>gnl|CDD|468912 NF040982, ComGD, competence type IV pilus minor pilin ComGD
IKGFTLLESLLVLLIVSSLLLLTLSLSIPQTYEQVEEKLFFEQFENDLLYAQQYAIASQQSTTITFSPDE
IQYQFQEGGNTSNRPYPLKIPISITVTKPNTITFNKNGGNNSLKGTFYIKGKKQTYTYQFQLGSGRYRKE
>gnl|CDD|468913 NF040983, BimA_second, trimeric autotransporter actin-nucleating factor BimA. This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half
MVLYIRMKYHRFPRSHAQQDTGRAASTVPFQRFAHLLCSSIAPLALGFSTDALAIEQAESTAFNAVIDQI
KKGDFKLKPVGDRTLPNKVPPPPPPPPPPPPPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPPTTTP
PTRTTPSTTTPTPSMHPIQPTQLPSIPNATPTSGSATNVTINFNSTGASAMGTNSIALDFHARAKDSDSL
ASGRLAHASGPRSTAIGAEANASGQNTVALGAGSIADRNNTVSVGRHGDERQIVHVAAGTQATDAVNVGQ
LNLAMSNANAYTNQRIGDLQQSITDTARDAYSGVAAATALTMIPDVDRDKRVSIGVGGAVYKGHRAVALG
GTARINENLKVRAGVAMSAGGNAVGIGMSWQW
>gnl|CDD|468914 NF040984, BimA_first, trimeric autotransporter actin-nucleating factor BimA. BimA (B. pseudomallei intracellular motility protein A) is a trimeric autotransporter, homologous in its C-terminal half to a number of trimeric autotransporter adhesins. It is a virulence factor that nucleates actin, so that actin polymerization can drive escape by B. pseudomallei out of one cell and into a neighboring cell. HMM NF040983 describes a homolog with similar activity but substantial difference in sequence architecture in the N-terminal region
MHAKASSSHAPDAPKPSSIATTLCRALASLSLGLSMDAEANPPEPPGGTNIPVPPPMPGGGANIPVPPPM
PGGGANIPPPPPPPGGIGGATPSPPPLTPVNGNPGASTPTKTGLLKTLNRLSAELQNNPRVTEDVVDNVD
AVIRNAVNLAPDANGDFSGRSAMPIEMAANAALRSLKKNPGDAGHAAPAYLPAERIGQLREKVRRTIEAL
ESNRPPKPQPRSTPPQSTPPKPTQHPTAPNPNAPDASTPDASTPPDASTPDASAPDASAPSRPAPAPRAG
TGAPAASAATRAPAFANRVRKPNPAMPAASSHAIASDFASSNAFAIGDDSTAVGAQAIAFSEQSIAIGSR
AIAAGARSIAVGTDATAAAPDSVALGSGSIAEREGTVSVGRDGHERQITHVASGTEPTDAVNVTQLRAAM
SNANAYTNQRIGDLQQSITDTARDAYSGVAAATALTMIPDVDRDKRVSIGVGGAVYKGHRAVALGGTARI
NENLKVRAGVAMSAGGNAVGIGMSWQW
>gnl|CDD|468915 NF040985, MamG, magnetosome protein MamG. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family regulate magnetite crystal size during biomineralization
MAAQVGGQILAAMAAPAKASAAAGGVGGAALGVGGGITASPVGAAAIGNAMLTGKGVCLGLGLGLGAWGP
VLVGVAGLAGAAYLYGYLKNRKAEVPAAAEAT
>gnl|CDD|468916 NF040986, MamH, magnetosome biogenesis transporter MamH. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. It has been reported that proteins of this family were iron transporters involved in biomineralization of magnetosomes
VERHHHNALYLLVALCMIFMTLVVAVQPLFLRNVLGLSRENAGFVNANIQVITEVLDLFLVGYLGYLSDR
FGRVPIMVYGFLVAGIGALLAPFSLELGAALGIDGLAFYYVARILMSLGTGAVWPQISTLAGDYTDVESR
PRLLANVAFMMAFGATLVYAVLMQIPEHAGVVVVMLLTALIALAGAWLSRRFLVDVAPRLEQSSFPWRRV
WELVKKKSRLRLSFASAFFARSDMVIIGLFLMTWFIYFADLVGVTHAQAAARAGLVIGLIGVVVLVSIPV
WGWFIERYGRVEAILLGLALSGLGFIGMGFIVNPFDWWILLPVALVALGQAGCLVAPQVLTLDLAPPEIR
GSVLGAFNVVGCIGIIFFVQVGGFLFDWIGPTAPFLFTGVANLLIMGYALWVLKGGATERQTSNDPGDD
>gnl|CDD|468917 NF040987, MamJ, magnetosome protein MamJ. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. It has been reported that proteins of this family were involved in the assembly of magnetosome chains
MAKNRRDRAKGAPDDGEGLWKDGGIASEPEIVSVTVHPSPTLAAAVAKPQQGDIWASLLESSPWSSNQGG
NKETVQPPPAPIRPQESAPVGDLVSRWSQPIWRTPSQAEEVESSESGDVAEIEQRPEPTTSDSTVSVSDL
VIEVQPVQSAELEASIEVEPALPPAEPVAEVEDVFVDVVAEAEPEPEAVVIEAEGAEAEPEDALPEPEPV
EEVIEIDAAEIEPEPEAVHDNEMTEAEGDPEMIPVEVEAEIEPEPELIDAVVELVTEFEVSEAEAVVSAE
AIAAPAPATDSPLAELSMAAAAMTLISAPSVAVAAEPVRIPNKVEKAAPAAKKVSPVQEVPVEDLLGGIF
GVANSAVRGVISLGAGVVGGVVKGGRAVGSNVVAGARRLTQSIKESCGICSTSQCDAVGKKK
>gnl|CDD|468918 NF040988, MamL, magnetosome protein MamL. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family are involved in magnetite crystal maturation
MVRLIGLLVFGGLIVLLASSNAHMVETRLGPLAMIAPHFVVLGITFFLGFAIGIVSVLANVMKRRKQKTP
GKSIVIKR
>gnl|CDD|468919 NF040989, MamN, magnetosome biogenesis transporter MamN. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family are probably ion transporters involved in biomineralization
MPAFVTLVVFVATFAVIYRDAVGRHLAVLAGALALVVIGTISGFYSPKMAFSSIYFETLALIFGMSAISA
LLARSGVFAYLAARTAELSQGNGRWILVMMALVTYGLSLASNNLVTMAVVVPVTLTVCFRTGIDPVPVII
AEIIASNLGGASTMIGDFPNMIIAAAGKLHFNDFIGGMMVPCLVLLAAMLVFFQRRLHDWKAREIPVDLT
TIRGEVLRHSPVDRYLLRYGLIVFGVTLVGFFLAGPLKVRPGWIAFVAGLTALVLGRFKDQEFFSACGGG
DILFFGGLFVMVGGLTAVGILDWAVAWIEGIGNGHDRVRALLLMWMAALLTIFLNAGTSTAVFVPVAATL
RLDGDGQAVWWALSLGVLAGSSAALSGATAGPLAASQYSGFLKRHPELASAAAAGLQFDFREYLRWGLPL
MGIFLVLSSVYIAVLAG
>gnl|CDD|468920 NF040990, MamR, magnetosome protein MamR. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family have a predicted DNA-binding domain and play an important role in crystal number and size control
MIWAAIVSGIRLISILAAALSLVDGVFGLSQFYGSNEINPSRIYSSGEAAKFLGVERLEVLKLIRSGKIQ
AKKVGNNYRILGQNLINYLNR
>gnl|CDD|468921 NF040991, MamS, magnetosome protein MamS. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family are involved in magnetite crystal growth
KPEQWILGLGILLFLGLVVGALLPDRFTGGNAKEALPEVGGVALQAAAQALPTPQPNAAQLAAGGAWARP
DAQLPGLSPFTQAPTLQFSGRVQQVASIGNDDGWGQVHIWIDNGTGAEQEISVAPQWFLTHMGCPLSHDA
QVSGVGFKFDKGRPNAELYAKSIRVDGRTCRLRNDEGFALWSNKLR
>gnl|CDD|468922 NF040992, MamT, magnetosome protein MamT. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family have magnetochrome domains and may play a role in magnetite crystal maturation
VLLVVLGLGLLWDKASDTLGEWPSDRSPRYAQGELLGRMPLPTEPSIGAPVEETVEPPLRYRKMTVKHIP
TIKPGAKMPHPYWGPCTQCHLIVGGPPPGSQPKTPVGAVLEKISRVRKLGPPILPNSTRPHPPAGRCIKC
HDIVVKVPVAK
>gnl|CDD|468923 NF040993, MamU, lipid kinase MamU. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family are encoded by the mamU gene on the mamAB operon and predicted to be lipid kinases, but their roles in magnetosome formation have not been determined yet
MRLALVINRSAGTFRRLPPDATVAAISAALGSAGHQVETILVGRRDLARTLSKAARDPDLDAVVVGGGDG
TILTAILAGLGRDKPLGILPLGTLNLFARDLGLPLDPIEAAAALAGASPTPIDLAEVNGLPFAIWASLGM
HPWFVRRRDHLQRKGMRKFRAMALAALRAFRRYPLVDVTLSLPEGRARVTTPMLFISNNPWRDEPLPLSR
ERLDTGTLVIHVAACSGRLSLLWLGLEAVMGHWRSSERLQTFSAHEVRVTSRKRRMMVSLDGEVTVMEAP
LVFRARPKALRVLMPK
>gnl|CDD|468924 NF040994, MamV, CDF transporter MamV. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family are encoded by the mamV gene on the mamAB operon and predicted to be transporters, but their roles in magnetosome formation have not been determined yet
MGNSGCKDCVERAARLDLGGTLAQAVFRSLLGVMSGSMGMAAQGLYSIGDAITKSLTLASIRISKIPPSK
TFPFGAGKILFVTSLIIGISLIGTGVFLASTSFNEPSTVEATPSLFAIVGVIISAAFSELMSRYLSCVAE
ENDNIALRSASRDNRIDAITSIVVLTGIVLSDAGWDAADHIAALLVSVIVMNIGRIIAWDAIKGLLDVSV
PRERLDEIARKSRAHKGVREIKLIRGRSLGEFWEVYMHVSIDEQLTVAESNAITRELRSNILRSFPHVQH
AWIITVPDPSRTVDVDDYWADHLFADAIKQEPPAPRLAS
>gnl|CDD|468925 NF040995, MamW, magnetosome protein MamW. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family are involved in magnetosome alignment
MLTAIIAGILLFLFGVLIKGVFAHAMVILVAWLAKNGLLLAFLRTRFGRRVVRNVRFKTYAQVGPGGGRR
RAYQVFKRMAGAERATVRVLTRVRDGFALMIRRRPSTAVRPIRKQSS
>gnl|CDD|468926 NF040996, MamX, magnetosome protein MamX. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family are involved in biomineralization through redox control
VAEWIMALGIAFSLAFFLLAVFNDNPWEDHAYDLAPPIVAGMPAPHRDGREKMVCSSCHEIIPPDGGQGA
GFGTLPIVQGTPAPHKDGRDKMPCASCHTIVKKNSVAKKGKAVPVPPAIAQGQPAPEAVSIALKKKPPLP
PAPAAAPLGPEAHERFTPFRFQGKVTRVVDKGPRSGRGNLHILVNDGINPPMWIDLAPYWFLQQEGCVVR
PGMFVKGTAYRDMTQASGELDYAMTVSVNGASCALRDNHLNGLWDPPGMDAEEE
>gnl|CDD|468927 NF040997, MamY, liposome tubulation protein MamY. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family are involved in liposome tubulation during the formation of magnetosomes
MLPHEFFIVLLSIALPIGLTVLILMLSRIVKSVDTLKSEVTNLSRNDVVSEGSVAMLADLFREHRTAIAA
QVAAQVEATAQLVRLNQDGRALAAPAQDSGTDDAMTLLAQLFREHREAVAAQLEAQASATAQLVQVTRDS
RDGIVDELRSQRVLSQEITQELSQIAQSRNVAPVPEPGLDPSQRIDRMRALAEVLGLALNDLSMTATQVL
TEHLNAAHGDRDGTRKFISTLTTAYFAGDKNVFFRSLVQEAVNRSEQLRRCAEDTENVRQQISKILREAR
EIRSLVAACDPNDLVRIVFEDGELWALEKALAEHFLIDGSPVWTE
>gnl|CDD|468928 NF040998, MamZ, magnetosome biogenesis transporter MamZ. Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family are predicted to be MFS transporter and involved in redox control of biomineralization
PEALFRSWRWNAIYLLSATSSLIIALAVGVQPLFLDEIFGIPFEKEGTINADIQVVAEMVSLVCVGYLGF
ISDRIGRVQIIFYGFLVAMIGAALAPFSLQLGAALGVGGLGFFYLARVLITLGADTVQPQLITLVGDVSS
FHNRPHLMSNVVFMMVFGGTVLYAIIMQIPHYEGGVYVVMALPVLVGLAGAWLTRYKLHEVADPGLEVKE
HPLDRVWSLVSGDPRMQLAFAAAFYTRADMIVISLFLSLWLISEADSVGVSRGYATAHAALLVGVLGLVV
LVSIPLWRRFIEHHSRITAIGASLSLSAAGFVWLGFFVNPFDWAMALPLILIGVGQGGCLVAPKVLAVDL
APKDILGALLGMFYLVGGIGLVMLVQSGGYYFDAVGPRAPFILMGTGNLLVMLYAVWLRPTGVDEDSGHE
LKKKRKKVNWKPLIFLTALLPLIWLLGRVLLGGYISGSSLGQMPVGFINRYLGDWAFNFLIISLSLRPIY
EITGIKYLAKYRRMIGLYAFFYAVLHVLTYVWLEWDFNWGHMVDDIYKRPFILLGLAAFVILIVLAITST
KSIIKKMGGKRWKRLHKSTYVLNILVALHFILAANHENGEPYIYAALVAVLLGYRVRQFWQKRNRARSPR
RG
>gnl|CDD|468929 NF040999, pilin_ComGC, competence type IV pilus major pilin ComGC. ComGC, encoded in the comG operon, is the major pilin of a type IV pilus involved in natural transformation of monoderm bacteria (those lacking an outer membrane) such as Bacillus subtilis and Streptococcus pneumoniae. In the seed alignment, Bacillus proteins have a pair of Cys residues likely to form a disulfide bond while Streptococcus proteins lack Cys residues
VKGFTLIEMLIVLLIISVLLLLFVPNLSKQKESVQEKGCEAVVKVVESQVELYELDHNKKPSLSELVSEG
YITKKQCPNYKDYY
>gnl|CDD|468930 NF041000, ATPase_ComGA, competence type IV pilus ATPase ComGA
EELIEEAIELRASDIHFLPREDGYQIKFRIGGGLIPYRELSLEEGQRLISYFKFLAGMDIGEKRRPQSGA
FTYELNEQQISLRLSTVGDFLGRESLVIRLLYQLEQIKPQLFFPEQFQLLKQLLQRRSGLILFSGPTGSG
KTTTMYSLARKLALNKQVITIEDPVEIKEPNFLQLQVNEKAGMTYDTLLKAALRHRPDILIIGEIRDAET
AKAAIRAALTGHLVLSTVHAKSAAGVIYRLLELGISKEELEQTLIGISYQRLIPT
>gnl|CDD|468931 NF041002, pilin_ComGF, competence type IV pilus minor pilin ComGF. ComGF is one of several minor pilins in the type IV pilus involved in the competence system of natural transformation by various Gram-positive bacteria. Oddly, while nearly all members have an N-terminal region with a consensus site for cleavage and methylation, ComGF from Bacillus subtilis appears N-terminally truncated, and may be functional despite the truncation
EKGFTLLECLVALLVLSLILLLIPLLIKLLLKVEQYLNNSDQLEWLLFLQQLESELKESTFKVKNNKLYV
KLDLIKSNGKTVAYEKYNSDIRKRVNGKGHQPLLQGVKSVSFSQKNNQVTIKVTFENGLEREAVYPFF
>gnl|CDD|468932 NF041003, GGPP_syn, geranylgeranyl diphosphate synthase
ELDEYFNEIINNVNATIKSYLKGDVKELYEASRYLFSAGGKRLRPLILVSSSDLLGGDRERAYLAGAAVE
VLHNFTLIHDDIMDQDTLRRGLPTVHVKWGVPMAILAGDLLHAKAFEILNDSLKGLDSDTIYKAFSIFSK
SVIIISEGQAMDMEFENRWDVTEEEYIEMIKKKTAQLFACSAALGGLIAGANEEEVKKLFEYGLNLGIAF
QIVDDILGLTADEKELGKPVYSDIREGKKTILVIKALEEASEEERKIILEGLGSKDAEKLKKAAEIIKKL
SLDYAYSLAEKYYEKALSALSSIESKNEIAGKALKYLAEFTVKRRK
>gnl|CDD|468933 NF041004, Beta_gal_BgaS, beta-galactosidase BgaS
IKFPKDFRFGWSQSGFQSEMGLPGSEDPNSDWWVWVHDPENIASGLVSGDLPENGPGYWHLYKQFHDNAE
KMGLNAARIGIEWSRIFPKPTFDVKVDVEEDEDGNVVSVDVNESALEELDKYANKEALEHYREIFSDWKN
RGIHFILNLYHWPLPLWLHDPIRVRRGDDRAPSGWLDERTVVEFAKFAAYVAWKLDDLVDMYSTMNEPNV
VYGNGYINVKSGFPPGYLSFELSEKAKYNLIQAHARAYDAIKSISKKPVGIIYANTSFTPLTEKDEEAVE
LAEYDNRWSFFDAVIKGELGGEVRDDLKNRLDWIGVNYYSRTVVRKVGDGYAPVPGYGHSCERNSVSPDG
RPCSDFGWEFYPEGLYDVLKKYWNRYGLPMYVTENGIADEADYQRPYYLVSHIYQVHRAMNEGADVRGYL
HWSLTDNYEWASGFSMRFGLLYVDYETKRRYWRPSALVYREIATSKGIPDELEHLNRVP
>gnl|CDD|468934 NF041005, cell_div_CdvB1_B2, cell division protein CdvB1/B2
MLGKDFQKYWGGSDQEPSIGEKIKNAFKSKEPLKYRLVMAQYKLRTMISRLDVYISRMQERDRTLFERVV
EAQMSKDTARAAMYANEVAEIRKISKQLLTTQIALEQVQLRLETVTELGDVFVNLIPVVGVINELKNALK
GVMPELSLELAELGEGLQEVVIEAGEFTGGSSYFAASSPEARKILEEASAVAEQRMKEKFPDLPSSVTST
QQ
>gnl|CDD|468935 NF041006, cell_div_CdvC, cell division protein CdvC
MSAQVMLEEMARKYAIAAVKADKEGRYEEAINNYKKAIEILTQIVRLYPDSPLRHAYEQMINEYKKRIEV
LEELVPAEPAGPDVEKESDEELVVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFPLGWPRGILLY
GPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSKEEGKPAIIFIDEIDAL
LGVYSSEVGGEVRVRNQFLKEMDGLQDKSENYHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLE
LLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEKGLGEPRPITMEDFKEVLKIR
KPSVNQEMLKAYEAWHEKFKA
>gnl|CDD|468936 NF041007, cell_div_CdvA, cell division protein CdvA
PISVEVLTKFIGQKVKDVYGRDFGYLIHVYTEIDGTVTGIEIAQGSSFSTIDPSRIKVDGDSLVVLPDWK
AEAIKSLGLMEKIRKRQRALEELYSKQEIPKSMYDDMKRKLDSEMLKIRDDYSKIKSKLKNRLNEIEDQL
AQIDKAMIAVKMSYIAAELPETAYKNSIEILRQAKDSYTLEKDDIRKTLDKLDLLDKEGLDIKPPGSLTT
SSEQSSKNDQNKSEIPLPIPVKVIN
>gnl|CDD|468937 NF041008, cell_div_CdvB, cell division protein CdvB
MFDKLFLFSFFNSDKKRKEQLGKLLTEISLKLKDQQDRLDEAIRRLKERDKDLFEKVVRAQIEGDSARAT
IYAQEISDIRKMIKIIYTAFLAIEKVRLKLDTVQELQGVSLVLFPVAKILGELKDQIKGIAPEVAIALDS
ITSSVNSIAIETGALNDKSIVPAVVDEQAKKILEEAQKMAEAKIKEILPDLPHPPSPSRGQSEQKVVKRK
LTEDELLNYIKSTGGFLDVDYISKIYGVDKDEVMNLLRSLANKGLISLEG
>gnl|CDD|468938 NF041009, cell_div_CdvB3, cell division protein CdvB3
KKKKTLAELLTDVRIARNKIRLWINRIENRIEQYERLSLSNAGRFPYLSKEYAKESEQLENIIDFLNTLD
VLLEMLEIKLETIIYIGYIVNYLPPVVEALKELKKQTGMSPEFSLLIDEIYTGFYASVTVPKPIKIKAKE
EAKKILEEAEKIAKKRLKEEYKIS
>gnl|CDD|468939 NF041010, glycosy_Agl16, glycosylation protein Agl16
MKVWMVTPLFLPVRGGTEVHVYNLSKELVRMSIDVEVHTTRDTYTERRSLERFEYVDGIKVVRHDRTWRY
GDGPDILHFHNLGRKFSLWNLYTFLFLLLGSRDEPVVMTPHDIFIVDRGKVINSIQRLIGRRVDVIIAVS
EWEKEEMVRLGYPKSKIKVIPNGVEDKAFELPKEEGPLDYLLYLARISREKNQLFAIECLQKLGVKLVLA
GQIRDQEYLEEIMNRVKELGLEDRVKYLGVVTDEEKYSLIDGSLAVVLTSEVEAEPIVIKEAMVRGVPVI
VGNKAKVLPTLVKDEENGFVVSDCEELREAVEKLKDEKVREEISENNKEISKEWRWRNVAKRVLELYKEL
L
>gnl|CDD|468940 NF041011, dihydoor_dh_Arch, dihydroorotate dehydrogenase PyrD
IRLAGLELEDPLIIASGILPDVPEYIERVCEKYGPSAITTKTLTLNPLEPHKPPTVVKLHDGCYLNAIGL
GNPGIGLLEEIRVKLCPLIVSIGGSSLEEIVEVAEIAEEKADAIELNLSSPNRKGYGASLASLVREIVKA
VKSVVKKPVFVKLGPWDNVLEIAGKALEAGADGLTLINTVKGMAIDVESFKPVLSYGTGGISGKCIHPLA
VRIIYDVYREYEAEIIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLKL
EDIIGIAVK
>gnl|CDD|468941 NF041012, T4P_ComGB, competence type IV pilus assembly protein ComGB. Members of this family occur in Gram-positive bacteria as part of a type IV pilus system used for DNA binding and uptake when species such as Streptococcus pneumoniae or Bacilus subtilis are in a competent state for natural transformation. Members of this family, typically called ComGB (second protein of the ComG operon), belong more broadly to the family of GspF, part of type 2 secretion systems (T2SS) in Gram-negative bacteria
KQQAKFLQRLGELLESGFSLSEALEFLLRQLPKKSKEYLQKILEGLKEGASLSEILKQLGFSDEIVTQIY
FAEKHGNLAETLKEIAEYLKRKEKQKKKLIKVLQYPLLLLLFLILILLGLRQYLLPQFEQLYSSMNVMLS
SFTNLLTLFIQHLPLIILGFLLLLLLLFLIYIFYFKKLSPLKQIKFLSKIPLIGSLYKLYLTYYFARELG
NLLKQGLSLQQILQLMQEQKSDPFLQELAKRLEERLLKGESLEQILKKYPFFEKELSLIIEHGEKKGKLG
KELLLYSQLLLEKFEQKIEKLLKFIQPIIFLLIALLIVSIYLAILLPMYQMME
>gnl|CDD|468942 NF041013, T4P_ComGE, competence type IV pilus minor pilin ComGE
KKNKGFILLESLVALALLALIVSLLLPSLTQIQKEREEIKQKEEALQVLYEALQTYQLHLELNGVEITVE
RSNTQIKVYWEGK
>gnl|CDD|468943 NF041014, pilin_ComGG_2, competence type IV pilus minor pilin ComGG. ComGG is an especially variable protein of ComG-like DNA binding/uptake type IV pilus formation systems. This HMM identifies ComGG proteins as found in Streptococcus pneumoniae, not Bacillus subtilis
KKVKAGILLYALLMAAIFSLLLQFYLERVQATQRLTQATKEYYQAKLMAEMFLDEAKQDSGEKKQGELSF
NQGTVTYEKKNEQLNVTVTLDKGQSYTYQFP
>gnl|CDD|468944 NF041015, UDPsulfquin_syn, UDP-sulfoquinovose synthase
MKVLILGIDGYLGWPLALRLAKRGHEVIGIDNLSTRRAVEEVGSDSALPIPSMEERVRAAKEILGVDIKF
YEGDVTDYDFLKDVIKKFKPDAIVHFAEQRSAPYSMIDLEHAVYTMINNIIGTLNLIYAVKEIVPDIHIL
KMGTMGEYGTPNFDIPESAFVEAEINGKKDRIPFPRWAGSWYHWSKVHDSYNLMFANKLWGLTITDIMQG
PVYGTRTEEIIDEGLRTRFDFDEVWGTVVNRFCAEAVLGLPLTPYGKGGQTRGFLSLEDSIQALTLLLEN
PPEQGEYRVVNQFDEIYSVNEIAELVKKAGEELGLDVEIKHVDNPRVEKEEHYYNPERKVLPSLGFKPKR
NLKEEVKIMLEDLIPYKDRLERFKEVIMPKTKWK
>gnl|CDD|468945 NF041016, trans_reg_ArnR, HTH-type transcriptional activator ArnR
MNKSVFDVLRELDSIVDFSRAKLQWDILIIIASKGPSSVSEIAETTNNSRKAVIDAIRKLVDKELVTKVK
YDIYDLSEKGKELLNKLNSLTSITVLDGNKIDSSIDLNSILTNPSQYFYLIELLKMALINNDILPIDKAS
RELGISKQTLKYYIELFTEKKIFKKINKKTLFGKNKQCYVLTNEGKKLAYRLPELIKMKNNLFLKLLLKL
TFSYRYESALIKVMLFLALSSPIIIYYRDVPQLGIIGIIWLYVLIFLTLLSVFAYITMR
>gnl|CDD|468946 NF041017, DNA_import_CedB, DNA import protein CedB
KYALILILILLILLGIIYRNPLFLILLILILFLLFKTGKKKFGFIISKIFKRKKQRNLSSIVIEDGYIIK
ENEYIAVLIVDDIPFDYRDLSESSLRSSINSFHKILNVGSQIDIVFRKKYIDKNKYLESLLNKAQNLRII
IESDPSNEKAKRELEIIQSILDKISEGEYPFKYEIYLLIHSKSKEEALSLAEVIRRGLESLGIKARLATK
DEIEDLIFLKEKKLNKIGLPSQIPFLTPFSIEKLPKFEIRSDGIYLGKDIEHNTPVFWNIDKSENPHLLI
IGPTGSGKTEFLISLGTKLNLNYGIPIVFFDVKGDIKSRLRKYGLPFKVLNPLFYSIGLLKEPGIPIQIK
ALQIEKILSNSFRLDKYESSILYKVLNRVLEDSYSGKISDWDVIEKKAKLDNDEQVKYYLSKIINIIKSL
DHGGGSLVDAIEEGINVIDLTLIKSEELRRLIIYSVITDIYNKYSLSVDDGLRIALVLDEAWTILKSEKE
DYPIVADLIKRGRGHGISLLMATQNIEDLGELSDIYLDNIGLLVFMNNGDKKFWNNEVKRFVNISDEEIS
NNLSFLGRGEALVRFLGDPRPLLVKLDVLT
>gnl|CDD|468947 NF041018, glyceraldDH_alpha, glyceraldehyde dehydrogenase subunit alpha
SYVGKPIKRLEDDKFVTGRSTYVDDIEIPALYAGFVRSPYAHAKIKSIDVSDALKVPGVVAVFTGKDINP
LLKEGIGPWATYIDPRPWKFVPRKFAENKVRYVGEPVAIVIAQDRYVVRDAVEKVNVDYEPLPAVVDMEE
AMKDKVLVHEELGTNIAYDEPFNAGNVEKAFKSADKVIEVEISNNRLIPSPMEPRGIVASYEGGTLTVWY
STQVPHFARSEFSRIFGIPSSKIRVIMPDVGGAFGSKAHIYPEELAVIASSIKLGRPVKWTATRSEEMLA
SEARHNVFKGEVAVKRDGTLLAIKGTLLVDLGAYLTYTEGLQPAIIPLMIPGPYKVRDLRIRSVAVYTNT
PPITMYRGASRPEATFIIERIMSTVADELGLDDVEVRERNLVRADEMPYTNPFGLKYDSGDYLGLLEEGL
EKLGYYELKKWAEEERKKGRKVGVGLAFYLEITTFGPWEYAEVRVDEDGDVTVITGGTPHGQGTETAIAQ
LVADELQIDIERVRVIWGDTDTVPAGIGTYGSRTITAAGSAALLASRQLLEKMKKVAARLLKADVEEVEY
SNGEFINKKEGKKVSWNDVAKAAYRGKEPGLSASVTYEADVTFPYGVHVAVVEVDDTGIAKVLEYRAYDD
IGRVVNPALAEGQIHGGAVQAVGQALYEEAIYDENGQLAVTYADYYVPTAVEAPRFESYFAEKPHPSNYP
TGTKGVGEAALIVGPAAIVRAIEDATGKRFNKTPVTPEEIY
>gnl|CDD|468948 NF041019, glyceraldDH_beta, glyceraldehyde dehydrogenase subunit beta
MYPPKFGYVRPDSLDEALDFLEKHEDAKPLAGGQSLIPMLKLRIIRPSYLVDINRLKELSYIKDEGNEVR
IGALTTHYEISKNDIVKSNLPLLSEAASKIGDPQVRNMGTIGGSLSNADPAADYPAVLLALDAKVVIRSK
SGEREVKAKDFFKGPFTTDLNQGEIVTEIVVPALKGYKTSYQKLVRRAGDFAIVGVAVLLKVSGGVVEDV
RIAYTGVNDKPYRAKEAEKALKGKKLSEELIEKAAEKASEGANPPSDIRGSSEYRKKVMKVLTKRALKEA
>gnl|CDD|468949 NF041020, glyceraldDH_gamma, glyceraldehyde dehydrogenase subunit gamma
MVVEPGEKVKIRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVL
AVQADGAEITTIEGLSKDGKLHPIQEAFWENHALQCGYCTPGMIMQAYFLLKENPNPTEEEIRDGIHGNL
CRCTGYQNIVKAVKEASQKMKA
>gnl|CDD|468950 NF041021, SCO5717_Nterm, SCO5717 family growth-regulating ATPase N-terminal domain. Members of this unusual protein family have a short domain described by this HMM at the N-terminus, then (typically) a long, low-complexity, typically Pro-rich region, then a AAA+ family ATPase domain, and then another region of low-complexity sequence
MSSDRDEIRGGGTTPGDDQSDAESAVEMTGEFTIDYTPPAWYTQNASG
>gnl|CDD|468951 NF041022, rodlin_AB, rodlin
IKKALATAAVAASVVGVSAAAAPQAMAIGDDHGTTTVNGNGAAQSYGNSTTGGDMSPQMGLVQGSLNKPC
IGLPLKANVQSLVGLVPIGVQDINVLSSPQNQQCTENSTQAKGDEPLSHILDDIPILSGNGVAN
>gnl|CDD|468952 NF041023, PP0621_fam, PP0621 family protein. Members of this family of small proteins have an N-terminal signal peptide and three invariant Cys resisdues, two in a CXXC motif
MKLLLLIAIIALVYWLFRKKRRPARARKKPKKPKAAEPEPMVRCAHCGVHLPRSEAILSGGKYYCSKEHL
>gnl|CDD|468953 NF041024, acVLRF1_NCBI, acVLRF1 family peptidyl-tRNA hydrolase. Members of this family, found in many Actinobacteria, share a consistent architecture and belong to the larger set of Vms1/Ankzf1 family peptidyl-tRNA hydrolase, which release nascent polypeptide chains from stalled ribosomes. The broader family is quite variable in domain architecture
RWVEVPPERLAGWVDRFAERHGGVTETEVTPGGVRVTAADGATATLQVPFPPLGRPGRGGLAVARLVAHA
SAPRRVGLLLVRRGGYAVGVAEGGRLVASKVGSRYVQGRTAAGGWSQQRFARRRANQARAALEAAAEHAA
RVLLPRVAELDAVVLGGDRRAVDAVLADPRLARLAALAEPRVLDVPDPRRAVLEEAAARARAVRIRVT
>gnl|CDD|468954 NF041025, antiphage_deaminase, anti-phage dCTP deaminase. It has been shown that proteins of this family prevented bacteria from phage infections by depleting deoxycytidine triphosphate (dCTP), which are important for the replication of viruses. The anti-phage dCTP deaminases have an N-terminal kinase and a C-terminal dCTP deaminase domains, however, the housekeeping dCTP deaminases usually do not have the N-terminal kinase
ELVIGLVGPIGSGLTTVANILEEELKEFGYDVESIKVSDLITELLSHGEELKKSDEYERYNSLIDAGNKL
RKKYGNNAILAELAIREIREIRREKGDDDSKPPRRTAYIIDSLKNPEEVELLRDVYGDAFYLISVHAPEE
DRKKRLKKKIGLSEEQAKKLIDRDEDEEGEKHGQRVRDTFHLADFFIDNPGSNNEDLKAQLERFLDLIFG
PPLITPTRDERGMYAAFSAALRSACLSRQVGAAITDKDGEIISTGWNDVPKAGGGLYWPGDEPDHRDYSL
GYDRNDEEKRKIIEDILKRLADAGSESLKKKGRNASECFKLILKKSRIKDLIEFGRAVHAEMNAILSAAR
LGGSTKGGTLYTTTFPCHNCAKHIVAAGIKRVVYIEPYPKSLALELHSDSITEDESSDDKVRFEPFEGVA
PRRYLDLFSKPGRRK
>gnl|CDD|468955 NF041026, antiphage_dGTPase, anti-phage deoxyguanosine triphosphatase. Proteins of this family are distant homologues of human antiviral protein SAMHD1. It has been shown that proteins of this family protected bacteria from phage infection by degrading dGTP into phosphate-free deoxyguanosine. The anti-phage dGTPase may also be involved in other biological processes
WQERRRGEEKKRRNDHRSPFQRDRARIIHSAAFRRLQAKTQVLGLGESDFYRTRLTHSLEVAQIGTGIVA
QLKAKQPEPLRALLPDDSLIEAICLAHDIGHPPFGHGGEVALNYMMRDHGGFEGNGQTLRILTKLEPYTE
HHGMNLTRRTLLGVLKYPALYSQVQAPQLPPKVSNFRQLKASDWKPPKGYYDCDQDVVDWVLAPLSENDR
ALFTSLDEKPGKQHGKTRFKSLDCSIMELADDIAYGVHDLEDAIVLGLVTREQWQEAVAPKLAALGDPWL
SDNLDELSDKLFSGEHYERKDAIGALVNYFITSIEIKEVDAFEEPLLRYNAVLPPEVAALLEVLKQFVYQ
YVIRSPEVQQLEYKGQQIVMELFEALASDPERLLPENTRERWQEAEEDGENGKRVICDYIAGMTDEYALR
LYQRLF
>gnl|CDD|468956 NF041027, GSU2204_Se_pt_1, GSU2204 family CXXCH-containing (seleno)protein, part 1. Most members of this family, including founding member GSU2204, are selenoproteins that average about 730 amino acids in length, with a cytochrome c-like CxxCH motif and also a selenocysteine site, typically GUA, about 145 amino acids from the proper C-terminus. This family was listed in Zhang, et al., in Biomolecules (2022). This HMM describes the family up to the residue immediately N-terminal to what is normally a selenocysteine residue. Cutoffs are set so as to exclude most homologs from related clades in which both the CXXCH and the U/C sites are missing, suggesting a similar architecture but different function
LALLLLLVPLAAAAEEGGATTEGSVEVGGHYTDDDDSPGKVGEYERSDDGATPELKLLEGGRGGGGFFDL
DGDYYDPDDQRGLLLDDFGRIFRAKFSYQSFEHRLDHDPLDNLEAREAVDGAPGGKVVTHEDLDPGADYG
ITRSELESRTELQLPGLPNLTFHAGYRDERREGTEQAITMSHCSSCHVTSQSREVDERTEDFKAGATGKF
GPVTVDYEFLYRDFDEDAAAPTNYYDDALHPVNGGSGDEFDSRLQYDDADGPLPYDQTPDSEKDSHTVKA
RLDLPKNTALGGSVVYSVEENKDTDLETDYDGGALRLTTRLGPKLRLSARGRYYEIDNDDVFVDLPERRA
GAGPQAGAYPGGGQDFDYTRYSALDRDVFEGGADLIYRLAKKTTLRLGYEYESIDRDDYEVAEDGGETTT
NTLKAALRSRPGKKLSLRAKYRYEDIDDPFMNVDGLGESPGLGVLEPPPGGPGPPGGIYYFQRYDARYAD
LTNQPTDVHELKLSATWSPSSKLSLTANYRYRDEKNDDLDDLDDWERTSHSPGVSLWYAPSDKLSLTAGY
TYNDQESETPFCVPLFDG
>gnl|CDD|468957 NF041028, decahem_GSU2203, GSU2203 family decaheme c-type cytochrome. Members of this family are DmsE family decaheme c-type cytochromes (see TIGR03508), but belong to a narrow clade that includes GSU2203, and that co-occurs with a GSU2204 family protein, most of which are selenoproteins (see NF041027)
LLVGLLLLVACATGAIREKAYLTLPVIEGASYVGSEACADCHEDIAENFKHNIHGRLADFEVPGVEKGCE
SCHGPGSLHVEEGDPEKILRFGELSAEEASAICLKCHTSGELMDWAGSEHALNDVACTDCHKIHGNKGKA
LLKKEEPELCYSCHQDVRAKTNFPSHHPVKEGKMSCSDCHNPHGSGNPNRGLKTDERKNDLCLKCHTRYQ
GPFVFEHAPVVEDCTICHDPHGTVANNLLKQNEPFLCLQCHELHFHATRAPDTSALASAAIPIVGISGAH
GFQMSFTTKCTQCHSQVHGSDLPSQSVPGGGKALTR
>gnl|CDD|468958 NF041029, Mre11_Pyroc, DNA double-strand break repair protein Mre11
MKFAHIADVHLGFEQYRLPYRAEEFAEAFREAIEKAVEEKVDFILIAGDLFHSSRPSPETIKTAIEILSI
PKENGIPVFAIEGNHDRTQRRPSAYHLLEDLGLLYLVGLREEKVENEYLTSERLGGKWLVKGVFEKGGKS
VEIHGMKYMSAAWFERNKLKDIFRPEGDAILMLHQGIKELIERMMKLPESQRDYFELKLEDLPKGYLYYA
LGHIHKRFETSYDIGKVVYPGSLQRWDFGDYEVRYRWDGRAFKPEAGTDKGFYIVEDFKPRFVELKVRPF
IDVKIKADEETAKKELKRLSPKIPREAFVRLDIRWERPFDVSWIKEILKVEYLYIRTRFERKLKGEEGGG
VPKPEEYFTPVELKIIELTGEKDFEAVDEVVELFLGGGWEEEPKKEKEEKEEEVKDTKKEKKEKPKKVEK
IKKKKPPKKPGDLLAWLG
>gnl|CDD|468959 NF041030, Mre11_Halo, DNA double-strand break repair protein Mre11
MTRVIHTGDTHLGYRQYHSPERRQDFLDAFRQVVDDAVEDDVDAVVHAGDLFHDRRPGLPDLLGTLSVLR
TLDDADIPFLAVVGNHESTRDGQWLDLFESLGLATRLGDEPVVVGDTAFYGLDFVPRSRRDDLDYEFEPH
DADHAALVSHGLFEPFAHADWDTETVLAESNVDFDAVLLGDNHAPGTAEVDDTWVTYCGSTERASASERD
DRGYNLVTFDDDVDIRRRGLDTREFVFVDVELAEGEGVERVRERVREHDLEDAVVIVTIEGEGEPVTPAA
VEEFALDRGALVARVTDRREIEDEAEVDVSFADPDDAVRERVRELGLSEAARDIDETVRASKVADSNVRD
EVERRVRELL
>gnl|CDD|468960 NF041031, Mre11_Sulfo, DNA double-strand break repair protein Mre11
QILHISDTHLGKRQYNLDSREQDVYDTFSQLIDIAIKEHVKAVIHTGDLFDVYNPPNKALKVAIDELKRL
KDKGIPFISIPGDHDTPKRKGEIYPQRILEELGLIKLLDGDQPELVKDGLKVEIYGIRHIPTVSKEALKE
LLSSLKPEGDRNVLMLHQGIREILPYDGAWQLEIGDLPKGFQYYALGHFHTRRKEKLPDGSILAIAGSPD
IIREEEIEGYKKNGKGAYLVDLSKKEPSIQPINVDIRPQEVVTINTDNLDQEIEKLIQKLSSYKKKPILH
IILEGDSIRKSVLMKKLSKLQDVAEYYRIYKDNTVDGDEKKVKVKSPSTIDELIREYLKKRGYTDEEAKL
ILEIINNYDSDEAVELLKKFAGV
>gnl|CDD|468961 NF041032, NurA_Pyro, DNA double-strand break repair nuclease NurA
YRLISRASVDRIKDMLLRGLKEAEEKLKDLIEWRPLPERKESKVYAVDGSQGKQRLSGTIIYFVSSYAFG
NGPAYRLVYTNAMLYNYGISDQIIRLQMETLENKLGYLAALLGEVDLILMDGTLTGSLTRPPVYPESVRG
INTLRSLLGEDDFEELIEEFLEELDEHYRELEEKLEEEGKSDSPVILADEVVDEFRKKYLAMKIIGYKKK
IRIPSCETRPEKIGIPLELLEKALEEGKSVEDLLEEIKEEYGEEKTLTKDDIRDAIHVVLSYLEYLYSLE
KLLEVLNLVYVAKSFYTRKLASKLGIDIVDVAYLDAYLRKLLGEELPGYLVFEEPKKKPEHEIPDVLRKH
FKNVEKFIERGVPSAYVRTMKGGVIYLLQSNREIEDDLLPEILWHESGGYFRPLQRAHEGVKIEKKEFRA
ELEALINILKAKDPELRVFVKYGRSPLE
>gnl|CDD|468962 NF041033, NurA_Sulf, DNA double-strand break repair nuclease NurA
MIDKVYEELVENRQKIKKKLNFFKNELDKEVKEKVKEIWIEYEPSSEIPKKFLAIDGGEFVKELRTGTVF
VVNAEAVITEGINVEPIDQDVKIGVFRPGNDAKERVSELMALLELKLALKNGDKADYILMDGSLKKKLGK
KKDIEGNSLFDEDEITSLEEKDEEEMLKHLILENQLLLSKLIERYGGKVLWISKNSRSRDLFGQEYSDIT
VLELFTENPGYTKPIIKTIDEEYIVEGDEREILSGLEYSSFYARLEKGERVLRVDIFGRIDEEFIKEIMD
DLSSVSIKGYPYPLLKVHYDVKVSKEDRKRIISLLGLKRRKGVSWWPSQFY
>gnl|CDD|468963 NF041034, Rad50_Sulf, DNA double-strand break repair ATPase Rad50
MKIERIFLENFLSHESSEVNFKGSINAIIGHNGAGKSSIIDGIVFSLFRESSRGNNEDLIKKGKKTATVE
LKLEDNGKTYLIKRNIPNSYSDDDTISNLKTIARGSTEVNQKIQEILNLDKDVLLSTVIVRQGEIESIFK
NLPDVMKKILKIENLEKLTDSNGPIYSVIKEIENKLKYLESEKERYESKEAEKEKLEKEIEESKNKLEDL
EIKKEEKEKELNDLKKEFEELEKKRERYDELTGRLSSLNKRINEIEEDLKDLEKLKKEKEKLEKEIKEKE
KLEEKNEIISELKELIKSIKELKRQLNTLEKEIEEYKENLKKKKELEDKAKKYEELKREKEELEEKENEY
NSLKSRLNSLKKKLEEIENEISKLGIIINIEELKKKLDKLSEEINNKNNEKGEIKGRKEQLLKILKNLNN
VKGNKCPVCGRELDEEHKKKIREEIEEKIKDLNKQISKLEKEVNSLNKEKEELENKINKLQEEKLIKLEK
LLKELQRLKKEIEEIEKELKELEESHEEYEEIKEELKELEPKYKEYLKVSNVTEEELEELERRLSEIKSE
LDELEKKYSELKEKIGDDREELTQIEKKIEKKIKEIKELKNKLEKLKEEIAKIEKEKEEIEKIENEIKEL
EEEISSLNFDEERYQNLKEKIEKLNKELNRIEQEISKLEGKIEALENDIDNLNSELEKIKEKLNKIPKLE
NAIKKLEKLREDLSGSGLQNYIISNVKSKIENNLNDILSKFDLSFSRVEIDFEIGGKTKKGKSEIKAYNT
AGQDLDVNALSGGERISIALALRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIV
VTHDEELKEISDYIISVEKKGDSSKVKVGSYD
>gnl|CDD|468964 NF041035, Rad50_Halo, DNA double-strand break repair ATPase Rad50
MRFDRVRLRNFKCYADADLRLDDGVTVIHGLNGSGKSSLLEACFFALYGAKALDGTLDDVVTTGAEEAEI
ELWFTHDGGDYHIERRLRASGDRATTAKCVLEGPDGTIEGARDVRAFVTELLRMDAEAFVNCAYVRQGEV
NKLINASPSQRQDMIDDLLQLGKLEEYRERASDARLGVEDVLDDKRGALSDLDSQIEEKEDKDLHERLNA
LESELAEVDEEIERYEEQREKAEETLDEAEEVLEEYEEKREELDDLEEEIEELRETIAETEREREELRER
IRELRERREELESERDDLLAETDLDAADEEAVEARRDELDERDEELREELEEARVEATELENQAENLRER
ADDLESRAEEKRERADELEAEAEEAEETLEERREKLEELDDEIEALRARFEDAPVEFGEAEDHLEELREE
LDELRERLAELRAELESARERVEEAERLLEAGKCPECGQPVEGSPHVDSIDEDRERVAELEAELEELREE
REDLEERIERAESLVEAERRVDRLEENRENVEQLVEEKEETVEEKRERAEELREEAEELEEEAEEKREAA
EEKEEEAEEARERVGELNAEREEIKERRERLDRLEDLLEEIADAEDEIERLRERREDLAELNDERRERLA
EKRERRDELEDEVDEDRVETAREDKERAEDYLEQVEEKLDELRERRDELQNAIGGVENEIEELEELRERR
EALAERVEALESLHDEAETLEAMYGDLRAELRQRNVETLERMLNETFDLVYQNDSYARIELDGEYELTVY
QKDGEALDPEQLSGGERALFNLSLRCAIYRLLAEGIEGAAPMPPLILDEPTVFLDSGHVSQLVDLVESMR
ELGVEQIVVVSHDDELVGAADDLVRVEKDPTSNRSTVERGEAP
>gnl|CDD|468965 NF041036, decaheme_TF, multiheme cytochrome-associated LysR family transcriptional regulator. Members of this family, including founding member GSU2202 from Geobacter sulfurreducens PCA, are LysR family transcriptional regulators found regularly in the vicinity of multiheme cytochromes such as GSU2203, a decaheme c-type cytochrome
METRYLKTLVIVAEEGSFSKAAEKLHLTQSAVSQRIKFLEECYGYQLFDRSGPSLEPTAAGEMVLEKARR
ILDIEDSLMDELKSFKGRQRLSICCTPTFGMAHLPGVLNRFMLRNADVVDLKFLFHSPAQALEGIQNKEF
DLAIIEHCADLDLGRFHTYPLPQDELVFVSAPSLGLPTPNVTLERLLELCLITRRDGCSSRDLLRRNLAE
QGRDLDDFRRVVVSDDLRLTIQTVLDGGGISFVSRSLVCEYLKNGQLREHYVEGFPHVRCRTVVARKCRE
NDPLLSAFMACLFKVFDDPSP
>gnl|CDD|468966 NF041037, microcin_B17, microcin B17 family TOMM. Microcin B17 is a thiazole/oxazole modified microcin (TOMM), a type of ribosomally translated and post-translationally modified natural product (RiPP). It is a toxin that corrupts gyrase activity and causes gyrase to to cleave chromosomal DNA, killing the cell
MELKASEFGVVLSVDALKLSRQSPLGVGIGGGGGGGGGGSCGGQGGGCGGCSNGCSGGNGGSGGSGSHI
>gnl|CDD|468967 NF041038, FslA, rhizoferrin biosynthesis protein FslA. FslA and FslC are the two major enzymes involved in rhizoferrin synthesis in Francisella, which has a reduced genome and cannot directly use putrescine to synthesize siderophores. Rhizoferrin biosynthesis in Fransicella starts with ornithine as the substrate. First, FslA mediates the condensation of ornithine with citrates to produce N-citrylornithine, which is then decarboxylated by FslC to generate N-citrylputrescine. Finally, FslA mediates another round of condensation of N-citrylputrescine with citrates to generate rhizoferrin
MQIEQLQKNNTPIDIESLELIGLTITDLSLTLEKIKASTLNKQFKRVALSFYREGLLGKSKKTNDTLFFY
NQENKKILKINKPSLFSLNRILFPRNLTIQNCDSKKETSIESLEELLNWAKDNNPQINHDDWKQFELELN
NSFENELSMNIYRSFWQKQLANNINSSNYSNLWQWLNTSMSKNEQLSFLEQWGAVGHIYHPGSKTKLGLS
KFENILYSPEFQAEVDIIFGAIHKNIAHTEIIDNLITTYQDWMINNYPEQYKIWCHELAKKGLDSNDYLM
IPIHPWQAEHILPEKHKCLIDCQQLIIINNCKYTTKPSMSFRTMLPTSNKDKTLMPHIKLPVAIHATSVM
RTVSPESVKTGPRISKILLEILDKEPQIAKSMNILADIAGIHTTKACRKDDIRQLSAIFRENPEKYLSTD
EIACPLASLFVKTPNNQALICDILDLLDYKSPIEILEYFRKYTKITLTACLDLYLLYGIALEAHQQNTLV
VFKDNLPQKLMIRDLGGMRLHLPSFEASGIHLPKDTFSLTFTNSQTITRRKFIHACLQSNIGELILQLSS
HYKINEEHFWTIVKQEIHQRFEYLKPRISVDKYNQEYSEILEKPWSMKALTRMRLNDKLDCDKDDMQGDI
YVNLKNPLA
>gnl|CDD|468968 NF041039, FslC, rhizoferrin biosystnesis N-citrylornithine decarboxylase FslC. FslA and FslC are the two major enzymes involved in rhizoferrin synthesis in Francisella, which has a reduced genome and cannot directly use putrescine to synthesize siderophores. Rhizoferrin biosynthesis in Fransicella starts with ornithine as the substrate. First, FslA mediates the condensation of ornithine with citrates to produce N-citrylornithine, which is then decarboxylated by FslC to generate N-citrylputrescine. Finally, FslA mediates another round of condensation of N-citrylputrescine with citrates to generate rhizoferrin
MSKLSNSNSIFKKLSKNKIEEITQLYGSPCFIIDENALLERAILFQKAITNQYKNSIAAYSVKTQSLSTI
IQKFYEVGFIPEVVSSDEFELIEKLQLNNKGIIFNGPYKTDASLIKALSLNSIINCDHFDEILRIAKIAK
KLNITAKIGLRVCDNKTPQNWSRFGFALTNQQNSNCDIFRTIDKIKNIPNLQLSGIHCHIGTNIRDLSRF
NAMSKNIAKLAETILTKYKQTLDWIDLGGGLAGISPTLDDKQLAPYSPFDLELYAETIIAPLKEYLNKTN
NKTKLIFELGRSLVDYSTALITTIVGTREQNEDFQSLITDAGIHIAPTTSVYRHPIYHLKQTDSTSKKTL
LLGPSCMQHDFLAENIFLPKLEYGDKLLVDGLGAYNISRNNEFIHLKPSVILIDKNNQYQILRVKQTH
>gnl|CDD|468969 NF041040, FslB, rhizoferrin export MFS transporter FslB
MNNHIKSQILLLCCCQLIVIAAMEMSNPFLPIYLQSLSNFGLLSANTWSVLAYALPLISAIIFSPFWGKY
ADRFGYKTMILRAAGALAVIQLLIYLTDSILIFITLRFIQGAIAGFLLASQSYAVVIVSKEYRSRVLAWL
QSSTAIGIAIGPLVGGILASILSYNQIFLISAIIACCTFILLLFKLKSISPTPSSKKETKNYYYKNKANN
YLIYIYFSVIFLSIFLAQTAKFLPQSFFAIYAKNFFSSNPIIIGAIYAAPAFSLLLISAPLGHLFDKLLK
RNNKQYFFASGYFIILFTLATIAIYIHATTHNIYLIIIARLILGVSFAGTLPCLFSLACRVKDNNFGYLI
GYCNTFSKFGNLTGIFLGGIIFQLSNMQTVFYITSFIYMFLVIMYICLLYLFDPKSSNFQNKELINV
>gnl|CDD|468970 NF041041, FslD, rhizoferrin import MFS transporter FslD
MNLDTKNIKYIPLLVLSTWFLGNMGVHFLLPLLPILSKDLDASVKLTQYVIAFFLAGKALGMIVYGPLSE
VYGRRKFMLIGLLLYITSSLLCMLATDIYWLIFFRFIQGLGVSATILMGRVIINDSYPNDKAANVFGYLF
ALAAVIIACLPTLGGIIAIFKNWQLAFITMLIYSSFIFIIMLKYLPETQSDDLQKKLSLLGILKDYSTIF
RHPVFFGYLMCTGLMVAGESAFNTNAAFLMIKTYGISPKTFGMMMSSLLVAHLLGAVICGRYVVKKGISN
LTGVGALILVLAAVFLLATSILKFDGPYLTISAMFIYFLGTGFIMTTAAVGVVSPFPKMIGTAMAFALSL
EFLLSSLSSFITSHLSISSLFPITVLITLLSLSSFAMWFFYIKRDK
>gnl|CDD|468971 NF041042, FslE, rhizoferrin import outer membrane protein FslE
MSNKINILSIIFLLILFTLGFSISFSNTNKQSNDFNSLSKETILELQSQIQNLQSEINNLQQENSQNSTT
FSTYNSKIEEIDLISDIPADNKNAYEILTNIDTNNSIINLKNKPIGGIFDKNGGINVGNAPAITTRGEVT
FLGAYSGNNSIPIGMISGNLFASTLIGQRNKFDSYSIFFGGKIEVDAQAWSGSNGISNGNTTLPSNGQNI
YLTAANLYFLSNIGHYVTAQFDFSTTELNNFGLGNAFVIFGNLDTSPFFLTAGRNKLSVGAFGGGGPWTG
GITGFLAPGRVTNVSLNYKDDILNANIAVFGSNDNQANFSTGLFYAEKWTEDLAVGFNTGYVYNIAGAGN
ASLSKFLQSQDSPNDTIGSFNINGNLTYTIGGGFLNIGAGWASTTNKKDFNGSNENVLAGGWYAAANYSL
VLGGRNTNFGASYGQSYNATNIPMPLTASPLSFGKSTSGIKNQLILSSQRAYFDNNVLVGPEYSYQELYN
GKHMNTVTLDMSVYI
>gnl|CDD|468972 NF041043, BPSS1780_fam, BPSS1780 family membrane protein
AGTGWQWIKEGFALFRRQPLALWILFFLYLFLILILLSLVPLIGQLLALLLGPVFSAGLMAACREIDEGR
PLEPSDLFAGFRDRLGPLLLLGLLYLLGSLLIGLLLSLLDGGLLLAALLGGGTAEPAEAAAAAAAGLLLA
LLVALLLYIPLAMAFWFAPALVAWHGMPPGKALFFSFVACLRNLLAFLVYGLIWAVLFFLAPLLVGLVLA
LLGAALAALPLLLGLLVLAPVLYCSFYASYRDIFGA
>gnl|CDD|468973 NF041044, GIVxVP, GIVxVP protein. GIVxVP is a rare, small, uncharacterized protein found in Cyanobacteria such as Synechococcus lacustris, Cyanobium gracile, and Microcystis elabens, in a conserved gene neighborhood of unknown function. Member sequences are about 70 amino acids in length with two apparent transmembrane segments
MSRNRTAKGIVLVPCLLLGGAFLSTAVWGDGAAAANRPLALGLGGLLLAAGLLAQLL
>gnl|CDD|468974 NF041045, RsbA_anti_sig, anti-sigma factor RsbA family regulatory protein. Members of this family have MEDS sensory domain in the N-terminal region and a histidine kinase-like ATPase domain in the C-terminal region. RsbA of Streptomyces coelicolor, the founding member of this family, was suggested as an anti-sigma factor by genomic location preceding sigB, by homology to RsbW of Bacillus subtilis, and by binding to SigmaB and effects on its activity. Members of this family include full-length homologs, but it appears members they may perform different regulatory functions in different lineages. Therefore, the symbol RsbA will be inappropriate for some family members, such as PrsR from Streptomyces avermitilis
FVHEALFYRSDEEFLAGTVPFLREGLAAGEPVVVAVPPRNLALLRDALGADADRVRFLDMTEAGRNPGRI
IPAVLLAFADAHAGGGRVRIVGEPVWAGRSAAEYPEWARHEALINAAFAGRPLTILCPYDTRRLPPAVLA
DARRTHPVLVDGGGRRPRNSAYYDPPDAVVARYNEPLPEPPPAAALFDPGDLPAARRFAAARAARLGLPP
DRLDDLVLAVTELATNSLRHGGGPGTLRLWREDGRLVCEVRDAGRLTDPLAGRRPPPPGQLGGGRGLWLV
RQLCDLVRIHTGDPDGTTVRLHFR
>gnl|CDD|468975 NF041046, UGSC_fam, UGSC family (seleno)protein. This family includes selenoprotein members with a UGSC motif, and non-selenoprotein members with a CGSC motif. Selenoprotein members were discussed in Zhang, et al., "Selenium Metabolism and Selenoproteins in Prokaryotes: A Bioinformatics Perspective" (2022)
AGLRVGLLDNTKPNADIFLDELESLLEEDHGAAEVLRVKKPTFAGAAPTELQIEIAAECDLVILALGDCG
SCTSWVILDAIALERAGIPTVVICSDAFAVFAEALAQALGMPGLRIVEIPHPIAGLSDEEVRAKADKAIP
QILDALT
>gnl|CDD|468976 NF041047, GSU3128_fam, GSU3128 family (seleno)protein. This selenoprotein family is described as distantly related to the peroxidase/peroxynitrite reductase system component AhpD
MKIRKKVFADFEYEEVLDAKTRELIRVAVAVATGCPDULKKHFAVAKQAGATEAELREAMAYGIIGPAGR
AKNFVLRMLGELDV
>gnl|CDD|468977 NF041048, TusA_like_YeeD, thiosulfate utilization sulfurtransferase TsuB/YeeD. YeeD (TsuB) is a TusA family putative sulfurtransferase associated with thiosulfate utilization
IKKLDVVTQVCPFPLIEAKAAMAELASGDELVIDFDCTQATEAIPQWAAEEGHSVTDYQQVGDAAWSITV
QK
>gnl|CDD|468978 NF041049, thio_trans_TsuA, thiosulfate utilization transporter TsuA/YeeE. TsuA (YeeE) is one of two paralogous transporters in Escherichia coli described by Pfam model PF04143. TsuA, and adjacent putative sulfurtransferase TsuB, are involved in thiosulfate utilization
LQMILTGLICGALLGFVMQRGRFCLTGGFRDMYIAKNNRIFYALLIAIAIQSVGVFALIQAGQLSYDAGA
FPWLGTVVGGYVFGIGIVMAGGCATGTWYRAGEGLIGSWIALFAYMLMSAVMRSPHAAGFNQQLKSLSTE
HNSIAETLGLSPWPLIALLVVVTLWLVAKELKKPKLKVATLPPRKTGLAHLLFEKRWHPFVTAVLIGLIA
LLAWPLSEATGRVFGLGITSPSANILQYLVIGDDKFLNWGVFLVLGIFLGSFIAAKGSREFRVRAADAAT
SVRSFAGGILMGFGASIAGGCSIGNGLVMTAMLTWQGWIGLVFMILGVWTASWFLFVRPQRKARLQAA
>gnl|CDD|468979 NF041051, SelTWH_Campy, SelT/SelW/SelH family (seleno)protein, Campylobacterial type. Members of this family are primarily (perhaps exclusively) selenoproteins, found in Campylobacter species such as C. lari, but also in members of several other lineages. The protein family is related to SelT, SelW, and SelH, and features a CXXU motif
VSIEYCNSUNYLPRAARLADELLSKYPDAEVELIPGSGGVFEVEVDGKLIFSKKELGRFPEEGEIVTLLK
>gnl|CDD|468980 NF041052, OsmC_like_Se, OsmC-related (seleno)protein. Members of this family are distantly related to the hydroperoxide resistance protein OsmC (osmotically inducible protein) of Escherichia. Proteins found by the HMM include large numbers of selenoproteins, most of which currently are known only from Metagenome-Assembled Genomes (MAGs) of uncultured organisms, a large fraction of which are assigned to the Chloroflexi
TVEVRAEALLGMRKLAEVRVGKFTIACDEPPRLGGTDTAPSPLAYFAAGIAFULLTQLSRYAHMLKVPID
SAKVEVRARFDRGGSVLGGTVEAGCDGVETELEIESDAPPEKVRELVRNAERGCFAEQTLRNPVPVETTL
TLNG
>gnl|CDD|468981 NF041053, CobW_rel_Se, CobW-related selenoprotein
MRVVSVSGTQGSGKTTLIRELVTRLGALGKRSAVIVNEDGEEDYEDEFIRSHQVAVEYLRGGUVGCSLAA
SLVALIKKIKRTDNPDYLFIEPSEMVVTKELRDVLAMGLRDIRYEIGPFITLIDGPGFEFLWEERRQLLI
GQISGADLVALSRADLLDPQKLERIKTTLKPYSKNILLLSTPDGWGIEEVLAKLA
>gnl|CDD|468982 NF041054, WAxxUGC_long, ResA-like WAxxUGC motif-containing protein, long form. Members of this family average about 350 amino acids in length. Many are selenoproteins, with a motif WAxxUGC, located in region homologous to smaller proteins such as the thiol-disulfide oxidoreductase ResA of Bacillus
MILTSLTVDPAEFERGTGWELKPEGACKGERCVPLPAAVDDGTVDVEVVAERLGMPLVHDEAHGLWALGP
ETVGGRALTSAAAPELELPDLDGNPFRLSSLRGQKVLLVAWASWUGCRFDLPVWQELREELHPEGLEIVT
VALDTAGAEAARPWIEAAAPTHPSLIDQEHVLDELFGIVNVPSGVWIDEAGMIVRPAEPAFPPRRPALRD
MKIPDDLPPRLRDMLTEAKKIRTDPEAYLAALRDWVARGAASRYALSPDEVVERSRPRPMDEATAAAHFE
LGQHLHRAGHHDAAIPHFREAHRLQPDNWTYKRQAWSLVDPLQGPTDVYDGDWLSDVRAIGPENYYPALE
L
>gnl|CDD|468983 NF041055, ryptide_RrrA, ryptide family R-Y-crosslinked RiPP peptide
MSIEFTKEELLQMKTIDDLMSSEQDEPGGIIVGQHITRRRY
>gnl|CDD|468984 NF041056, ryptide_ex_MFS, ryptide export MFS transporter. Members of this family are MFS transporters that belong to a system in which ryptide precursor RiPP peptides are produced, modified by a radical SAM/SPASM enzyme that introduces an arginine-tryptophan crosslink, and exported
MSKSIWQLLISQAVANLADVFLRVVVIANVFIISKSVIATSMVPILIGLSSFVASFLVPLVTKKLALNRV
LSLTQCGKTILLAILLLLLWLSEAIALPILYVFVVLISILDGFAAPVSYAIVPRYATDLGKANAALSMSG
EGVQLVGWGLGGLLFASVGLFPSMLIILVLYLISTVLMLTLPLVKNEVLESETNFETLTKGWRLVAKNPK
LRLFVQANLLEILANTIWVSSVILVFVTEVLHQTESYWGYANTAYSIGILLGGFIVFRLSEKLLKYKWQS
ILFSLFAMAIVTVLIILFPNASAFLIFSALIGFLSQLKEVPESVFLQETVDENDLVNVYSVFEVISTLAF
SVFVFLMSSITERFGVISSFWISIICLILEAILIFINRDLIK
>gnl|CDD|468985 NF041057, Rcas_1661_fam_Se, Rcas_1661 family thioredoxin-like (seleno)lipoprotein. Most known members of this lipoprotein family are selenoproteins, but the family is named for Rcas_1661 (WP_157042591.1), with a CXXC rather than UXXC motif. Members are found primarily among the Chloroflexi
LLLLLLLLLVACASAAEPATEPPPAATAPTATPTPPPAVAATSTPTPTPTATPPEPTAQPPTAEPTPTPA
SVPRGRTAEGAFFLGDPDAPVTLIDYSDFLUTSCRAHVLGVEPQIIENYVATGQVKLVFWPVLNHGEPSL
YATEAAECAGQQDPDAFWEMHETLFENQGDLWGADRDYFVDTAVALGLDQAAFEACYDGGAARAQVEALD
AARRQRGIRSQPVFDINGERLVGAQPYETFAQVIDAA
>gnl|CDD|468986 NF041059, DpdA, tRNA-guanine transglycosylase DpdA
MKFYFPDSQDQVDPSYDFITDEYSPGRVRQRDDLYAHEILSPAPYDGILVSKAIVDGSAKGAGKYTEAQR
ERLYREGARRFFRLPKDLPIMGDCGAFTYVKEEEPPYTVDEVLEFYEDCGFDHGVSIDHIIFGYDPDASA
LDAVPPEWVRRQEITLENAEEFLAASRSRGYKFTPVGVAQGWSPESYADSVKRLQKMGYRRIALGGMVPL
KTPEILACLEAIRDVRKPDTQLHLLGIARVDSIPEFAKLGVTSFDSTSPLRQAFKDDRNNYHTADGSGYT
AIRVPQVDGNPKLKRLILAGIVSQEDAIRLEREALKALRAYDKGEADLDETLEALLAYERLLGGSKKKSR
LAAYRRTLEDRPWKRCPCDICREHGIEVIIFRGSERNKRRGFHNLYVFYKHLRKL
>gnl|CDD|468987 NF041060, DpdB, DGQHR domain-containing protein DpdB
LRVPALRIRQGEGRDVYCFAVDGKDIHRFAAISRVRRDEDGQLQGYQRPEVLSHIRAIRRYLESGDAMLP
NAIVLAFDSRVRFEPSRGPKPDDYSVPGTLVIPVDSEGEKPAWIVDGQQRSAALRDADLREFPVPVVGFI
ADDEEEQREQFILVNSTKPLPKGLIYELLPETSGQLPRDLARRRLPAELCERLNFDPDSPFYGLIKRPTN
PDGVIKDNSILKMIENSLSEGALYQYRNPSDGSGDVEAMLLLLVNFWTAVRDVFPEAWGKPPRESRLMHG
AGIQAMGFLMDRITERVPAEEVTKDEFREELRRLAPHCAWTSGTWDFGEGLGRRWNELQNTPRDIRLLTD
YL
>gnl|CDD|468988 NF041061, DpdD, protein DpdD
LTRFFGAGNDIWPKIVSPPELADRLRPLLDALRRGRADPVVLPRRRSGGRLYWYVIARDAAQLRELRELL
DAFLGPSYTDFDGRPARLDPSDPVEAALLDLFGAGVLRFRLLPGSDTEARDEVRDALLLLLDLLARRPPR
EWRVPRPTGRLLADFDAALAAGDEAAAEAILDELRAQGGLSAENLAFLEIQLLAALGRWDEILALPDLDD
LLRLRPPPPVTEALLEALYRTYLAEPLAAGDLAAALEALRELGLPFPPLLRGVPGIRSAAAVKVLLLWAL
ARGDLARLRRLLAELDARGWLESLLEAAPTPASVPAPATAAEAASALDLLLPLPPSLEAALLLLACALEL
GDAEAAAAALEALEALPEALLSSLAARPRLRADLQSLEDEAAPAAPPTGWLEWLAALAEGDEAGALAIAE
EGWAEWPPPALDDEALAEILDGLSDEAAEVLRDALPAFLEALDYDEPAPRTALPLYLALLELLALDDRFS
PGDLAALQALLEILLRGGPSAAEYRELLEALEEIWERWVSPVTADWALDLLELLALAPCPDPAARERLAN
ALLSPLRSHWSRLSPAQLALARRLAEELGLGLDWPPPEEEEEDEEEAPLADLPGKVIGIYSLTESALRRA
AEALRQLFPGLKVELNSDKVGTPQLRALARNADVFVFATRSAKHAATYFIKAHRKDRPIIYPDGKGSSSI
LRA
>gnl|CDD|468989 NF041062, DpdE, protein DpdE
GDLVRSPGFPGIGKVVAIDGEEARVEFFESPAEPEAERQTVPLSDLRRVSLSPETRVYVRDPSSGRWRAG
RVIGSRPGNDYLVRFPNGQDLDVPESELFVRWDRPVHDPVEVLAAGGNESPFFHDARSPFLESLIAQRAA
CRGITALLSSAVELEPHQVAVVRRVLQDPVQRYLLADEVGLGKTIEAGLVIRQHLLDNPDARVLVLVPDA
LVRQWRRELRDKFFLDDFPGARVRVLSHEEPERWEPLLDAPDLLVVDEAHQLARLAWSGDPPERARYREL
AALAHAAPRLLLLSATPVLGNEETFLALLHLLDPDLYPLDDLEAFRERLEEREELGRLVLGLDPDNPNFL
LRQALDELRALFPEDEELQELAEELLPLLDEFDDEEPEERARAVSALRAHISETYRLHRRMIRNRRSSVL
GADYLVPGRAGPRVLVWESPAREAADEALEDWREEAALLDAESDPAARAAYARALAWLVARLGGPDDLAA
LLRWRLRGDAASADLAGERELLEALIAALEDEAKDADLLAALADWLLPLLRGSGKAVVFCGDGSLADHLA
AALARLGAGSVERHLSGQGADQAERAVRAFRQDPSARVLVCDRSGEEGLNLQGADRLVHLDLPWSPNRLE
QRIGRLDRYASLRGGRPVESYVLAPSDDDSLYSAWADLLREGFGVFDRSVASLQDALDEGLDEAWRALLE
EGPEALLEAIARLRGELARERRRIDEQDALDSIEADAEEARSFAEALAEAEEDADELRDALLGWITKGLR
FRKRRDEVDDVFRFDFASRRTLLPPRLLIRRFLPGLDREGTFSRSVALRRPGVRLFRYGNPFVDALARLL
RWDDRGQAFAMWRLDPSWRGEPRLYFRFDFLVEADLLPALALLDGAARRALRRRADRLFPPFTLRVWVDA
DGEEVTDPELLAWLNAPYSKPGGVGGRDYNLNGSRWEALLELFGADEWRELCRAAEEAARALLRSRADLA
EACARAQARARADLAVRLAQLRARAAAGSLVEDAEELAREVALAQALADGIRNPSVRLDAVGCVVLSG
>gnl|CDD|468990 NF041063, DpdF, protein DpdF
LQELLANWPTADSSFPEDPFLRRLRDALADLSEAGPLDLAALLRQVLRREQARGGGAPSLRVPRRPPWPS
REQWEAAGLDVDPLGEGHLLLTARPWRPEWLDAAADDPPFEDVFAERLRRTLEPVPGDPFLAEALGFTHY
RSPGQREAVRAALLAPPGSTLIVNLPTGSGKSLVAQAPALLASRQGGLTLVVVPTVALAIDQERRARELL
RRAGPDLGGPLAWHGGLSAEERAAIRQRIRDGTQRILFTSPESLTGSLRPALFDAAEAGLLRYLVVDEAH
LVDQWGDGFRPEFQLLAGLRRSLLRLAPSGRPFRTLLLSATLTESTLDTLETLFGPPGPFIVVSAVQLRP
EPAYWVAKCDSEEERRERVLEALRHLPRPLILYVTKVEDAEAWLQRLRAAGFRRVALFHGDTPDAERERL
IEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIA
KSLNRPKLISVEKGLERWRAMFDSKQPLGDGRYRVDLDTVPPHLDRQSDQNRAWNLRTLLLMARAGLIEL
DSPPPPQPADDEDESEERLEEFWDEYFNSVVVRILDDGHLDEETWETRVEPVRQRELRAARKNLELLREL
LRGKRCLSELLAELYTLRSPGRGVPPSRACGGCPACRREGRPPFSGLAPEPRPVWQSPFPRLGGLLLRLL
ESLLLVYYDDPDERALLLRRRRLLVRLVRRGVREIVAPGAVLDELRQLLKRASSRFVFLDDDYEPLRLPY
GPTLVVVPPDGTPLPPRLLRLASRPPRIILAPEDLPDPDRPGR
>gnl|CDD|468991 NF041064, DpdG, protein DpdG
MSILNNASPGSLPNLLVLIDRVLARAGKPLSREELLALCRPESLPKDDNAEGRARKNLNFWTELGLFSED
EEGEEPFRGRLGASPDTAEARLPRRVRRLLLDAENNADLWESEGNRAADLLRALAWLLAQDIYTLPPLSS
GNLEELVNRQLPSRRILNNDTRWNGLLAWARFLGFAEPDKSGYVIDPTRAIREVLPEIFGGGEQLPIKEF
LERLAEVLPVLDGGAYRQEVEEALSGDGWQPPEPGQLSTSLSRALLRLELSGIIQLETRSDASGSLTLTG
PNGRTRSVSHV
>gnl|CDD|468992 NF041065, DpdH, protein DpdH
YVCWSPEEVAACINTEAESPSDAVFLATHEPLRLRRRRRELSGTGEEVTEEDLLDDFLERRRPSGALLMP
IVGESGVGKSHLVRWLRAQLKRHPDSDRRHVIYIPKSTSLRRVVELLLEGLEGEEFDQLRKDVDRVTEQL
DEETLARRLLNELAEALGAAGPHGARKLDGPELARVLVGPRGLPALLQDPHFREHLLEPGGFIPRLAARL
LGGRGDGEIERPYQFTADDLPLDILDINKAAAPARRYLQLLLSDPELQEAAVDLLNEHLDAAVRQAFSLG
GGRLQDLMLEIRRQLARQGKELVLLVEDFAAIQGIQRDLLDALIEEGVREGKKVLAPIRTAMAVTTGYFL
RLPDTVLTRARAEWVYDLDSEFDSEDEGLERIVDFVGRYLNAARVGREELERWAGVALGDWVPNACDECE
FRAECHAAFGKSSDGYGLYPFNRSALRRLVHSTAPKDKPLVFNPRTVLNEVLRPVLVEHRDAIEDGQFPP
PGFRERKGDPRLSAEVASEIELLDPSDAERRETLLEFWGDAPSELANLPPGVHEAFGLPPLADLLVSIPP
PPPRPPPGPKPTPDAPPPAATPSDELPPSLQRKLEALEEWAQGGRRLPQALARELRKILSEALNDRIDWS
DPLMKEPGKAVLKKAAWPNAAGSVSIEGAAAEVLFGDEDAPIRLKRTPLAALFFQSLLRANADYPGGAED
YRRLARLAERWVPQVLARVLRELREEDEDLVAAVRALLLGAALLGLAWPGMTDADLLAALFDDGQSWERS
DAASRVPRWTALRERHLSAREELVDRLRSLLGIFQGTGGAVRAIDAARLLPLLREAAKEWTWQPELPVEL
PEWVKLAVLGFARLDKAVEEQLAALQELLERIRDRLPEGTDGVELVDAVKEALEAARELGLWPLGVRGRE
TLPALLAALEELDWSAVKSLERDLARLDDAEDNSDDRALLAALSRDRGASLEAIREFLEAADRWLDAALQ
AAEAQSGGSELEAAAEEIQDLLAEW
>gnl|CDD|468993 NF041066, DpdI, protein DpdI
MTLKEQLQQLRKQLVRKQSAAALEEEYNVLKTISDRLANVASRLKKAARKLEVLKLLEIIDLWQEEGVAA
LKTARTALIAFAERFKESPDEATLVEKSGLYELTDALKAVAKSVDEKQDATWRAFTEALFSQVMVEEVKL
EQQKTLHGNKELYNDYRKAKDEFNEQKNSGPFDVSVVRRLQQYAKQLVELKGKMNFNAPDDVKKFFDALS
NNGGAPLDLLTPEVIEWLEENGMLSNFVV
>gnl|CDD|468994 NF041067, DpdJ, protein DpdJ
LDRLEERELRLLSWGVTDGSFSEDELLEIIDDVLDDHDEDLDAEDVLEELLERALLFEVPSPSGSRYRTR
MAETVRLLARLRQLFPGQPWQSAPTLVADFRFLRRPRRYPRRDIPASTALAELAQLPGLTPLQRQALRAL
LGRPGGLLLAGFQVRATRRILRALESHRSRGTIVCAGTGSGKTLAFYLPALAALAELLRADSRWVKALAI
YPRNELLKDQFAEAYREARRLDGVLAAEGRRKIRIGALFGDTPTSASDADASYAGWKRRGGGFVCPYLRC
PTDGCGGELIWRDADREAGRERLTCSKCGAVIDEDEIALTRESMQKTPPDILFTTTEMLNRRLSDSRLRH
LFGVGAGARKPRLVLLDEVHTYTGTHGAQVALLLRRWRHLLGAPVHFVGLSATLRDAARFFADLTGLKPG
DVEEIEPAEDEMEEEGAEYQLALRGDPVSGTSLLSTTIQTAMLLRRVLDPPDSRPSDGLFGSRAFVFTDD
LDVTNRLYDDLLDAEGRTSFGRPDGGKPPLAALRSPGAPDDSARYLAGQSWRLCEDIGHDLDSDRLRVGR
TSSQDAGVDADADVVVATASLEVGFNDPRVGAVIQHKAPRDMASFLQRKGRAGRSRGMRPWTVVVLSDYG
RDRLAYQAYETLFDPELPARSLPIGNRYVLRMQAAFALLDWLARQLRRRNGWGSVWRDLSGPKDGRSADR
ARQQKLAELLEALLEGPALQRELARYLQRALQLSADEVQALLWEPPRSLLLAVLPTLLRRLRSNWAVAVD
PGEEWKDLQVDNHPLPEFVPRNLFSDLNLPEVTIVLPPQTRNDEPEREAMPILQALREFAPGRVSRRFAV
RRGEHRHWLPPPPDPGEQTLPIEEFAEEHEEEGEFQIDDGEPQSIPVYRPWRVRLQQPPREVSDSSNARL
LWRSQIVPPGDGLSIDVPRGSPWSRIITDVRFFTHAQRSPVEVRRFATGADAEIRFRDGEEARVTFRFTL
DGEPAALGFRLEVDGLRFRFRLPDELLAALVLPPLLLRALRTAYFRHRVLEDPALPEVANPFQREWLAQI
YLAALLLEALADGRSLEEAAAALLNGSALQRLAEVLDVLFQSLDVEETEDEDEEERLQQRLRELLADPEV
LARLDALAELLWAPDDAAWEPWARRRYADTLGAALLQACLQLCPDADDGDLIVDIDPGPDPGGTAEIWLT
ETTIGGGGVIEALARRYAEDPRRFFRLVEAALAPSDYELVDSDLTRLLELLTTDGELADAVAALRSAESH
AERVQALDRLRAALSARGFLPSHSFVSALNNRLLRPGSGPETDALLLDLLREWRALEARLGIEIDARVFA
YALARRDDLDAALVLLGGVGAQDFWRFDVIQGLLWPRGNQIRQRALQSYNPFADNPPTDRLLVRALLDET
LPRVDLTDPDWRERLQEALAEHGSVELVAPPDQRGALAAALVRLPVEPVDVGFLQVYPRVEGVRREGGRI
VVRLELREAV
>gnl|CDD|468995 NF041068, DpdK, phospholipase D-like domain-containing protein DpdK
RRIFKSGPTSSREIRDLLQSLFVAELLSPSPRLWLVSPWISDIDVLDNRAGQFDALNPDWGRREIRLSEV
LAALAARGTRLRVVTRPDPHNDPFLRRLQALAADGGDRLRVVEDEDLHEKGLLGDDYLLSGSMNFTYNGI
TVNDEHVTLRTDPEAIAEARLEFEDRW
>gnl|CDD|468996 NF041069, IPMS_Sufob, isopropylmalate synthase
VRIFDTTLRDGEQAPGIDLTVEQKLRIARQLAELGVDVIEAGFPASSEGEFEATKKILEEVGDQVEVTGL
SRANKNDIDKTIDAGVSSIHVFIATSDIHLKYKLKMTREEVLDRIYESVRYAKDHGVTVEFSPEDATRTD
EEFLLTAVRTAIDAGADRINIPDTVGVMHPFKMYDLIKKIVPATKGRIVSVHCHNDFGLATANSIAGVEA
GARQVHVTVNGIGERAGNASLEEVVMALKKLLNYEVGVKTWLLYETSRLVSEMTGIPVPYFKAIVGENAF
GHEAGIHVHGVIENPFTYEPISPEEVGNFRRIALGKHSGIHGLKKLLEEQGIPLDDDKLRRVLDEVKRLA
DMGKKVTEEDAKEIAEKVLNE
>gnl|CDD|468997 NF041070, carrier_LysW_Arch, alpha-aminoadipate/glutamate carrier protein LysW/ArgW. involved in lysine biosynthesis via the alpha-aminoadipate pathway and also in arginine biosynthesis
MKKKCPECGADIEVPDDALDGEIVECPDCGASYEVVKSGGGVELKPAEEVGEDWGE
>gnl|CDD|468998 NF041071, Trm10_mtase_Thprot, tRNA (adenine(9)-N1)-methyltransferase Trm10
LGKILAKALRELGIDSLYIPRLKKCFGDLLQCIAVNLLLGNYGLCRGEFYGKLIGEEEGIKLLSGKGGEK
TTYVLAKGGEKIVIDIPPEFPLFIIDLSLWDRHTEEEKNKLVEQILASISTIRRYLWDGNLSLNNAPSEF
LEHARGLGHANIIRRDVPPIENAVVLDPYGDCEATEEIIRSTDTFIIGGIVDKERRWKYATAELAELAGY
DFPRVRIELRGSRVGVPDRINKIIEIILRVREGESLEEAIIETQSKADKVSRLLREIAGNGVLEENANWL
KANDKVLELALKK
>gnl|CDD|468999 NF041072, FtrB_double_U, FtrB family double-selenoprotein
KELTFEEALARAIRMSERYVEKGPYKFFPDPEVVEEVQEGLAKNEVEHGYRYCPUMPLSGDPVEDRKKIC
PCERHHEDIARDGFCIUMFFVSEEFLRKYEAGEEFSSTLGEAVPPGESLFP
>gnl|CDD|469000 NF041073, S-lay_SlaA_Sulfolob, S-layer protein SlaA
MNKLLGLILSILFIASIFIFGIPLTTTAALPSIPPSAGHIIAIYLTQVNGLQIQSVAFVVNVSNINVSAN
NNLTNLITYVGTNIQPVIVFKNATTGQTIQSLTIPSTTFTYYIYYDEGAKVVFFLVGVVYNSYVNKSEQI
PITYLEQFLPNLGVAVNEYDTAQTTVTQVSSANPYSLLVYGTTGTQSVGTNAILSSLLTPSNLAPNQFYE
YVYGQTLQSFTVGGLTIPASTTNQVIVFAPFSFSPSPEQTGFFNPLQINGNLGPALQSVASTKPVIWGRA
LINTTLVDPFLSAGGPDNFTFQLNYSTPGPLTINLAQLAQIASIPNFPSKFTYLSYKFSNGYWSFLGFIS
DNLSITINGVVIKPSGTFTINGKELYYAYLLAILPLSTATTKLEYVSNLTIYYPYNNNITHTMLVNPNAP
PTSYTLPVYVYSAPAGSTITLTGYFNGTKYTVNIVVGSSPTLSPYVATISLVATAYEGIKVSGVSSPYYT
SAILSTPPSQIAISGSSQIQAQGQFTSTQASATVTLLTNATLTYNNVPLPGYSFNGIIVTPEYPIINGTI
AMQYMITAQYFMTNGEYELAILGSQEPMAVSMYNGLQNLVISEPLPPFSLTLTAPTVPATETGTSPLFLE
FSTVPQYTYITLVDFGLWSNETSVVVTAYSTQNGTTSANHGYFYAIIIPPQISTTPITPQSFECYNNAVD
VTIYDPDAILDPGYPSGSFTYAIATLNYSNRVVPGAVIFYGSTVYNVSGTFGKYSYNKLTVVSSFTYTEQ
TIPFSPTAYQLTLNGNTISVIGPNGETSAIYLAYYADNNPTVNYYFEQSLTVNNNMDVELAGIAIIGLNV
SYNNVLPSPQNQVGYMELLPTAAPAGTPYPGAAEPNYVINNYITYKIDGSASGSNAPNGLYVVNSNTFLT
VVPNASFVGSSDKYKYITTDYAVFHYFASSGQYKVETTVTVPNVTATLYFSSNVTPLYSSSALLYLNEPY
YGSNLPTYLALGTGGTQQWNSPNYQLLGVSATQQLLGKMMSINVTLPNGVTVTIALTTSNLTTLFVSLNG
QELQYCNGTFEFQISIPGLESILHLTVQQLNNSILSVSYHDYVTGETLVATTKLVALKELQLVAAQPGQV
EFFLTAYPSGVSLTFAPPWFIAEKVYIQPFLNFSDYQFAHTNPSSLLSLMVTNITVVHNVGQVAMIYYNA
TSGQTVAKNVYGQVVLTASGNVIPTIAETAAGSGIFTGTLSFAIVPNNTLVTLTTAFNKTSVYTNGSLAI
TLSGKNYPLGPAGLFLLPFVTYNGTTIGYNANVSVTVSDSVSTVTVSTYITAANFTPIRLAPFNVPTIPP
IPHAPKSTYYYNGSVVITPTSQVIKIYVTSVLPYPYEFFILAVVYEASNFNVTTGKIITPVVYYSYSAVV
AKPALGTSSAVPYLLVYVQLQGISSLPAGKYVITLYAVPFAGGPAISEYPVNLVFTNVTVTK
>gnl|CDD|469001 NF041074, quin_ox_SoxA, proton pump complex quinol oxidase subunit SoxA
MLILVAIFVGWNIYGVTNGSSTSYRYGLPLFSGLPKQAQNAVKYFESHPPAGQTSEVINGILVVNMTVTQ
YKGFTPDVIVANPSEPVVIILNSPQVITGFFLRLPDGVVNVNAVPGYTSYVYFVAPSQPGNYTWRDPEYA
GYNFSYMTGTLEVV
>gnl|CDD|469002 NF041075, quin_ox_SoxB, proton pump complex quinol oxidase subunit SoxB
TAGALAWLAVLGIAAMWFRTILLYPHNSPKPGYAIGPLYYFLVTLHGQSAMFILVPDLALAIIAYSLYKS
GMSIIHTKLMTILFWLINLPLIFAFAGGPDTGWYMYPPLALQQNSWLFYHGALIGLAYFMLFLNSLGAII
ASLTLFFDAYKTRPKEGKIPIFAAYGMAFSGMFIPLTLPALTAAELWYTLYFWANVPVNPLTWVVLFWFY
GHPVVYYVPFPVFGGLYYLIPKFAGRSLYSEKWARWNIFLLFTFSMLAWVHHLQTWPLPVVLRAFITPTT
LILAAGSGLTVLNLGLTIFTGKGYNWKDPVGMAALIALIGFILAGLQALILPINPLNVIVHNTYYVVGHF
HLMIWTIIIVGFTAILLDMLRSKMGPGADFSSLSRGMLRAGLIMWTVPFLALGYTMSYAGYLGLIRRWIA
YPVKFLPYMDAMTFLAEIMGASFVMFAIPALFTLLPVKTSSFWSGSSS
>gnl|CDD|469003 NF041076, cyt_b_SoxC, proton pump complex cytochrome B SoxC
ISDWILERLGLDELPFFRTPDYMYNVSYWLGALVAAAFIYTVISGLILLLYYNPAAGYQSTQFIINSVPY
GSVVLFSHLYGAYAMIILAYIHMFRNYFKGAYKKPRELLWITGVLLLALTLGASFFGYSLVGDVLGVSAV
DVGAGILSGIPGATTIVPWLFGNGYDSGLFDRVLAWHIILVALIGLLFVFHFFLAERYGMMPSRKVKPKA
PAVYTKEEWQKFNPWWPRNFVYMLSLVLMTWGFILIVPNALANLNGLPQYLPPFLNPKPAPPPNSPAAAH
VTPYPPWFFLFLYKIADFLLPNGQPVLPFLVIAVIIPLVYLILVPFLDRSDELHPLKRKFWTWVGIVMIT
YLIQLSIWGYLAPGVPAPFSQQVEVLLPPAVIVAIGVYFLPPRKKGKKVKTKSSTTVKKPGISPLSILGF
SVLSLLFAGTFGDFLNSPSLIGLGILIPLGILFYLFTKRMVPAALKPENAVGSTSSSSLETKKKIAEIAI
PVLFIVSVILAALMWTIPSTGPQSNLAGIDLGLIFIMWGEAISLYHYVVYVK
>gnl|CDD|469004 NF041077, tRNAmeth_TrmJ_Sulfolob, tRNA (cytidine-2'-O-)-methyltransferase TrmJ
MIRVVLVEPEGEYNVGFIARLCKNFEVDELYIVNPKCDLNEALKFSAKGSEILEKAKIVNNFDDAIKDLD
LKIATSSIADNKGDMLRKSIKPWEISDLIGGKKVALIFGRESVGLTREEISKADFLLHIPANPEYPVLNL
SHAVGIVLYEIWKSRGNKSTKYNVSSESLKLIDKYVKTLYDLIKRSEGDESMYIALKRALIKGIRDEEEA
RAVVRFLRKLYMRLIHSEE
>gnl|CDD|469005 NF041078, cGAS, CBASS cGAMP synthase
MANLSKLFYSTTDDDGFLKRLDLSDEQRDFLKEARNKVRDHLRDGFKEALDKYGGTKVTPRFFTQGSWAY
GTLNRPAQPPQEMDVDDGVYLPMSFFEDERPSVAAKTFFEWVEEALKELCEEEGWKLDTDKPTCIRIIIA
ADAHIDVPLYAIPDDEFDTLQEAVAKYAYDSLDEAVDFAEWEALPIDVVLLAHRDGGWIESDPRAVKEWF
LDEVDRKGEQLRRIVRYLKAWRDWQWEDGGPSSILLMILAANAFEKRPDRDDLALLDVLKALPERLRGGV
YNPTVDDGEDLFRRLSEEEREEFLDALEELIESLRQALEAESKSDALKWLQEHFGDRFP
>gnl|CDD|469006 NF041079, CBASS_lipase, CBASS cGAMP-activated phospholipase
FQILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKD
IFPKRKWPRRLLGLLKKPKYSSEPLREVLEEIFGDKTIGDLKHRVLIPAVNYTTGKPQVFKTPHHPDFTR
DHKLKLVDVALATSAAPTYFPLHEFDNEQFVDGGLVANNPGLLGLHEALHFLGVPYDDVRILSIGTLSSK
FTVRPSLKRKRGFLDWGGGKRLFELTMSAQEQLVDFMLQHILGDRYLRIDDVPTNEQAKDLGLDNASEAA
LETLLGRAKQAAQRALGNPKIKAFFTHPATAPTFYHG
>gnl|CDD|469007 NF041080, DGGGPL_reductase, digeranylgeranylglycerophospholipid reductase
RYDVLIVGGGPAGSTAAYHLAKKGLKVLLIDSKPWNRIGDKPCGDAIGKHHFDELGLPYPEGEVLEQKIE
GIKIYSPDEKTVWTVKGEGFEIDRPAYGQWLLKEAQKRGAEIFDKTTALKPIVEDGKVVGVKAFNRRGGE
QVEVRAKVVVDATGYSGVIRRKLPKEWPVTEPLDPKDADIAYREIRETKDEIEEPQYIRIYLNQEISPGG
YWWYFPKGKNKVNVGLGIQGGMGYPSPRTYYEKYLDPYAPDKDKNRVIVAGGALVPTRRPLNTLVWNGIV
VIGDAAYTVNPVHGGGIGSAMISAYLAAKAIEKAFEKGDFSEETLWSYNLCYMEAYGAKQASLDVFRRFL
QRLSNDDINYGMRKKIIKEEDLLEASTKGDLKLSVAEKAMRVLRGLGRPSLLMKLKTVAEYMKKIKELYL
NYPESPSGLDRWVARVNSLYNEFRKKL
>gnl|CDD|469008 NF041081, prot_lys_mtase_Arch, protein-lysine N-methyltransferase
MLELAKVGEDDVVYDLGCGDGRILITAVKEFNAKKAVGVEIDPERIKEAQQNIEKNGVTDRVVLINDDFF
NVDISEATVVTMFLLTNVNEMLKPKLEKELRPGTRVVSHEFEIRGWKPKEVVKVEDGNMTHTVYLYVIGE
HK
>gnl|CDD|469009 NF041082, thermosome_alpha, thermosome subunit alpha
QPILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEH
PAAKMIVEVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKV
DPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVAEKDGGYNVDLDNIKVEKKVGGSIEDSELVE
GVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSG
ANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGG
DKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELALRLREYAA
SVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEP
LRVKTQAIKSATEAAVMILRIDDVIAAA
>gnl|CDD|469010 NF041083, thermosome_beta, thermosome subunit beta
QPVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQH
PAAKMLVEVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKV
DPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVAEKRDGKYYVDLDNIQIEKKHGGSIEDTQLI
YGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKAT
GANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVG
DDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVELAKRLREYA
ATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELGVIE
PLRVKTQAIKSATEAATMILRIDDVIAAK
>gnl|CDD|469011 NF041084, trehalase_H1_Arch, alpha,alpha-trehalase TreH1
PLGFISNGITSALIDGGSIVWFPVPRFDSPSVFSKLLDEEKGGEFSISPEEEVEKVSQEYVVPNVLKTTF
KTKDGKAEVTDLLPLGEPAIIRKVESEIPLEVVIKPVFNYGLYRPIVEILKDGIKFINPKSRECLELLIL
GNGKISEGKNVWWFSPGKGYLYLLYSSDLRYGLFSKKGFVYSDPERAFEKTINYWRSELKRGRKGEELED
LYYTSLGVLLGLIYSPSGAVIAAPTTSLPEVVGGSRNWDYRFAWVRDSSIIAEALISAGYIVEARRIINF
LLSLVNFSSKPFDHPLYTVDGTIPPPEEELPWLSGYKNSRPVRVGNAASLQVQLDVEGFFMDALYKYYKA
TGDKVYIRDHWWKIEYIADWVSENWKLKDAGIWEERGVPRHYTHSKVMMWVALDRAGKLAKELGKEDRWK
ESREEIREWIMENCVKDGYFVRYPGSEEVDAALLTLPLYGFVDVKDPTFLNTLKRIERELVVDGLVKRYR
KDFMGEAKHPFTLASLWLARVYIRLGRIDEAKEILENLLECSGGLYLLGEHIDVETCEFTGNFPQAFVHA
QLILALKEL
>gnl|CDD|469012 NF041085, trehalase_H2_Arch, alpha,alpha-trehalase TreH2
KYYAFLSNGITSALEKEGSIEWFPVPRFDSPSIFTKILDEEKGGYFSITPDEEYYVIQQEYVEYSLILRT
EFKTKKGKLELIDFLPLSLPAIIRIYDSEIPFKVDIKPVFNYGLINPGIEVVEDGIIFKNPLSKEGVELL
IYGNYEIEDPYKITIKPGKGYLYLLYSKDLRYGLFSQKGFVYSRPYEALNKALSYWRKELSRAKKVSIFE
DAYYRSLSVILGLTYLPSGGIIASPTTSLPEIVGGSRNWDYRYVWVRDASYAAEALIKAGLLTKARRVLD
FLTSVVDPSSKSFDHPFYTIDGTPPPAEEELDWLSGFKNSKPVRIGNAAYLQIQMDIEGAYMHSLYEYYK
ETKDKEYINDIWWAVEAIAEWVKKSWRDKSTDIWEQRGVLEHFVHTKVMNWVALDRASKLAEELGYNKEA
EEWKSVAEEIKEDVLNNGYSEKGSFVRYYGSDEVDAALLTLPLYDFIDANDPRFLNTLKRIEKELKVSDG
LLLRYKKDFMGSVVHPFTLVSTWLARVYIRLGKIDDAKRLLEKLISCSTDLGLIGEHIDQKTCEPRGNFP
HLFPHAGVVLAIIELEEK
>gnl|CDD|469013 NF041086, STAUR_1299_fam, STAUR_1299 family protein. Members of this family, including STAUR_1299 from Stigmatella aurantiaca, are found so far in genomes of cultured bacteria only if the bacterium belongs to the Deltaproteobacteria. The restriction to the Deltaproteobacteria is less absolute in MAGs (metagenome-assembled genomes)
LLARAFERAPGAEANQAISEVREELEGGGGAPALSYEVVLPPEAPWEFLLDRVLPRLVRYLKSKGARPPG
CPGVFVSLFVGDRLYFVEAGDFLAALAEAEGLDLDELVRRVG
>gnl|CDD|469014 NF041088, ala_glut_racmase_Arch, bifunctional L-alanine/L-glutamate racemase
KNITEILHHLGEEDFPFGAVSPPIFQTSIFSFKSFDEFSEALSNETNHFLYTRGNNPTVNILEKKLAALE
HAEDAKLFASGVAAISASILAFLKSGDHVVCVKDAYSWTKTLFEQYLKRFGVEVTYVEGTDVEEIIAAIK
PNTKLIYLESPTTFTFKLQDLRAVAELAKERGIKTVIDNTWATPIFQNPIDLGIDLVVHSASKYIGGHSD
VVAGVVAGSEEDIRHIFETEFLNIGAVPDPFEAWLILRGLRTLHVRMQKHYENALKVIDFLQTHPKVEEI
NYPFYEKHPQYELAKKQMRGGSGLFSIKLKTDSIEKVKKFTNSLRIFRRAVSWGGYESLVVPYAVSHRDG
PDENVSLVRIHIGLEDPELLIEDLDQALKAI
>gnl|CDD|469015 NF041089, alpha_gluc_AglA, alpha-glucosidase AglA
VKISIIGAGSAVFSLRLVSDLCKTKELSGSEVSLMDIDEERLNAVYILAKKYTEELGANLKFEKTTNLEE
AIKGADFVINTALVGGHVYLEKVRAIGEKHGYYRGIDSQEFNMVSDYYTLTNYNQLKLFLDIAKLIEKLC
PNAWLLQAANPVFEGTTLISRLTKIKMVGFCHGHYGVHEVAETLGLEEEKVDWQVAGVNHGIWLNRFRYD
GKDGYELLDKWIEEKSEKWKPKNPFDDQLSPAAIDMYRFYGMMPIGDTVRNSSWKYHYNLETKKKWYGKP
WGGADSEIGWKWYQEQLRQITEAIIELAKAVEKNPNLKLLKVWPYLKFLPEKDFKEEIFTLLDPEKLSGE
QHIPFIDALVNNKKARFVLNVLNKGTIKGIPDDVVVEVPALVDKEGIHPEKIEPDLPERIKKWYLKPRIM
RMEWALEAFLTGDRKLLEEILIRDPRTKSYEQVKKVIDEILNLP
>gnl|CDD|469016 NF041090, Cyc-maltodext_AglB, cyclomaltodextrinase
IPSWVYDSVVYQIFPDRFAIGKGKTVEDKEKLYEKRGGRIVEWGVPPKRTGDGSHVKVFYGGDLWGIAEK
IDYLKDLGVNVIYLTPIFLAPSNHKYDTIDYFKVDPQFGGLEAFKKLIKKAHKNGMKLILDGVFNHVGKE
HKWFKKALKGDSEYRDFFYFYEDHYRGWWGVKSLPELNLEEVEVREYLFTVVKHYLKLGIDGWRLDCGQD
LGPEINRLITSKVKEVSSEKYVVSELWTYPSGWDMVDGIMNYHFREVVISYLNGELKNAGKILEKAYKET
DNIYGCWNMLDSHDTPRLATVLPDKKLRKLAIVLQFTYPGVPVIYYGTEIGMEGGEDPECRATMEWDELK
WDNELREFYKKLIKLRKSEPALRYGSFELLNNSPLVFLRKTPMVLDLVIVAVNKSDEEVELVVSIPDGRL
LSGTPFVDLFTNEEFWIKGGVLKINIPGRSFRILKPENKRVNGYDQYKRI
>gnl|CDD|469017 NF041091, asp_aminotase_Arch, aspartate aminotransferase
SKIIDSIPPSKTLEINAKAKELKKKGEDVVNLTAGEPDFPTPEPIVEAAIEALKKGKTKYTDSSGIPELR
EKIAKYLKKKKGLEYSPDEIVVSNGGKQALFNALAAILNPGDEVIIISPAWVSYEPQIKLCGGKPVHVKT
KFENNFVPKIEEIEKAITPKTKAIIINSPNNPTGAVYPEETLKEIAELAKKRDIYVISDEVYEKLVYDGE
HISIASFVGMKERTIYINAFSKSHSMTGWRVGYLAANKEIAKAIAKIQSHLTSNINTIAQYAALKAFEVD
NSYMVEEFKKRRDFVVERLKEIGLKFVEPKGAFYLFIDVREFLGNDEEFCKKLLEEKKVALVPGSAFNAP
GFVRLSFATSIENLKKGLDRLEEFLK
>gnl|CDD|469018 NF041092, beta-fruc_BfrA, beta-fructosidase
MFKPNYHFFPITGWMNDPNGLIFWKGKYHMFYQYNPKKPKWGNICWGHAVSDDLVHWRHLPVALYPKDET
HGVFSGSAVEKDGKMVLVYTYYRDPGHNIGEKEVQCIAMSEDGINFVEYTRNPVISKPPEEGTHAFRDPK
VNRNGDRWRMVLGSGKDEKIGKVLLYTSEDLIHWYYEGVLFEDESTKEIECPDLVKIGGKDVLIYSTTST
NSVLFALGELKEGKLFVEKRGLLDHGTDFYAAQTFFGTDRVVVIGWLQNWKRTALYPTVEEGWNGVMSLP
RELYVEDGELKVKPVEELKSLRRRKILEIETSGTYKIDVKENSYEVVCSFQGRLELVFKNESNEEIAIST
NEDDLVVDTTRSGISEGDRKKVRVKFKETNHIRIFIDSCSVEVFFNDSMALSFRIHPEYPYNILDVKSEP
LKLEVYKLKNIWL
>gnl|CDD|469019 NF041093, CheC_Thtogales, CheY-P phosphatase CheC
DKLNDRQLDALKEIGNIGAGNAATALSTMLNKKVEITVPSVKVVPISKLWFIFEDPEEIVAGVKMGVKGD
LEGAILLLLGTDSTKKILELLMGPRPEDLTQLDEMTSSALKEIGNIMCGSYITALSNFTGLNIDPLPPEL
VVDMLSAIVSEASLMSTEGEDYVILIETDISIEEIEKEITGYLILIPDEGSLEKILKKLGL
>gnl|CDD|469020 NF041094, CheX_Thtogales, CheY-P phosphatase CheX
MDARIINALLAAVVNTFKALLKIKPKVGKPQVLKEIEPKYDVVTVIGFTGVLEGNLIYSFSEETALKIVS
KMMGGMEYDELDELALSAIGELGNMISGAIAMNLEKIGYKIDITPPTVVRGKDLKVSVEGLILKLPVSIF
EEEEMELYLVIK
>gnl|CDD|469021 NF041095, dival_cat_tol_CutA, divalent-cation tolerance protein CutA
MILVYTTFPDEESAKEIARKLLEERLIACVNLREIRSMYWWKGKIEEDKEVGAILKTTKERWEELKEELK
ELHPYEVPAILVIEVEDVNKEYLSWLDEST
>gnl|CDD|469022 NF041096, esterase_EstD, esterase EstD
MKKFILILLLLSSTLTFSSKYQQEAFSYIQHLISENFEKAYEMSSDIMKKQLPVSKLKEIWETIEQQYGK
FENIEKIKIIQKGEYEVYIFTSKFEKGNLNISITVDKEGKIAGLFFNPAQKVEYKIPEYVDKDKFEEKDI
KVGKWKLPGKLTIPKGKGPFPAVILIHGSGPNDMDETIGPNKIFKDIAYGLSSNGIAVLRYDKRTKVYAK
EKDPETITVKEEVIDDVLAAIKLLKNFNYVKKIYLLGHSLGAYLAPYIATKNDKISGIILLAPPARNLED
VMLDQLEYLKSLDGKSNSKEILEKLEKLKNNKLKDSEIVLGAPAKYWYDLRNYNPLKYLKSLKIPVLILF
GERDYQVTKKDFEIFKKELSEKKNVKIKVYEDLNHLFIPGEGPKTPYEYYKEGHVSKKVIKDIVKWIKER
K
>gnl|CDD|469023 NF041097, keto_inos_dh_IolM, scyllo-inosose 3-dehydrogenase
MKALVLDAEWDPRPGYKLSPREIEGRRARNGSQVWRNPRLEVTERPDPVPGKDDEVLIRVRACGICGSDV
HMYETDEDGYVLYPGHTKLPVIIGHEFSGEVVEVGKAVTRFRPGDLVAAEEMLWCGRCRACRRGFPNQCE
NLEELGFTLDGAFAEYVVVPEKYCWSLEPLRERYGSEDKALEAGALIEPTSVAYNGLFVRGGGFRPGDYV
VVFGAGPIGLAAVALARAAGAAKVIAFEPSAERRELARELGADYVFDPTELDPAEAVLELTDGEGADMHV
EAAGAPAATYPEIEEALAVGGKVVVIGRAAAPVPVDLEVLQVRAASIYGSQGHSGGGIFPRVIALMASGR
IDMTKIITARFPLEEAPEAIERAATRRDGKKLVHP
>gnl|CDD|469024 NF041098, diketo_inos_hlase_IolN, 3-dehydro-scyllo-inosose hydrolase
MDKPDGIYFQNMTGKQVEERLKKNDIIIIPVGSTENHGPHAPYGEDTFLVTRMAEQVAKKTGCTVAQPIW
YGSHPYHHMGMPGTIVIPEEVFADYLRAVIAGFWNTGFRKQILLNGHGQEYVIPNAIHEFGKKYQVPAII
LNVNWPHAIPEYLKDKEHGGPYETPFIHADEVETSWSLALFPEMIHMEDAVDTEPKGFLPPGHIDKGGDI
YGRPIPWYCHVGAGGIEVIAYPEGVVGKATLADAEKAEPGIEALLDYLVKLHNDILEKFPAGKLPPIEKV
TQRDREEIEALLKGPLKGGRHIYTLAY
>gnl|CDD|469025 NF041099, keto_glucon_epim_IolO, 5-keto-L-gluconate epimerase
MKLSLVVSTSDAAFDALAFKGDLEKGIEKAKKLGYDAVEIAIRDPKLVDVNELKGLLYELNLPVVAIGTG
QAYLAEGLSLTDPDENIRKKAIERLKKHIDFASIFGAKVIIGLIRGKKEGRAEEEAEKLFVESMKELADY
AEKKGVELVIEPLNRYETDFINTIHEALEVIRKLNRPNVGILADTFHMNIEEPNIEESLRKCGDKLYHFH
VADSNRWAPGYGHIDFDSIVKTLKEIGYNGAVSVECLPLPGGPEEAARLAFETLKKLLL
>gnl|CDD|469026 NF041100, betagal_LacZ_Ttogales, beta-galactosidase LacZ
YEWENPELVSEGLEKPHATFIPYFDPFSGQWEYPKDFISLNGKWKFKFSNNPFELPKEFFSEDFDDSSWD
EIEVPSNWEFTGYDKPIYTNVVYPFDINPPYVPKDYNPTGIYRKKFFIPDDWFDKEIFLHFEGVRSFFYL
WINGKEVGFSKDSCTPAEFRITDYVKPGENTITVEVLKWCDGSYLEDQDMWWFAGIYRDVYLYALPKLHI
RDIFVRTDLDENYRNGKLFVDVEIRNLSNLKDKDTLKITLVDPDGDEKILIKETIILSYGERTLSFTFDI
SKPLKWSHETPNLYVLKVKLGEDEKKVNFGFRKIEIKDGTLLLNGKLLYIKGVNRHEFDPKRGHAVTVER
MIQDIKLMKQHNINTVRTSHYPNQTKWYDLCDYFGLYVIDEANIESHGIGWDPEVTLANKEEWEKAHLDR
VRRMVERDKNHPSVIFWSLGNEAGDGENFEKAALWIKSRDNTRLVHYCPLGADRPGDGYYLDVVSVMYPK
IEKLLEYSSKKRERPLIMCEYAHAMGNSVGNLKDYWDVIENKPYLHGGCIWDWVDQGIEKKDENGRLFWA
YGGDFGDEPNDGNFCCNGLVLPDRTPEPELYEVKKVYQYVKIRFIGNNRFEIENNYMFTNLENFDGIWKL
RKDGEVIEEGKFKISLPPGEKKTLKINLPELDDGREYFLEISFVLEKDTRWAEKGHIVAWEQFKLKDPEF
ERKSIKGKVNLREDGNKYTVLAKDVEYVFSKLTGLLEQIIFNGKEILKEPLVPNFWRAPTDNDIGNKMPE
RLAIWKKASYERRLHRMIIQKEKNKVSVLSTFQLPGDSWLYLTYTVFPNGDILVDYYLIPSEDLPEIPRI
GLQFKMPKDFKHVEWYGRGPHETYEDRKESGIFGIYLKEVDEMYHKYVRPQETGNRSDVRWFSLSDERTN
LFVSGYPTINFSVWPFSMEDLEKAQHINELPERDFVTVNIDYKQMGVGGDDSWGALPHKEYILWPKPYSY
RFRIKPSQNSKKEWRNLPAFEEDFEFSMSLPKVKLKRNEPLKVSLFLKNNSPVTYEKDILLYLDEKLVYV
KRVVVPPYEKVDETFELKIEKKGDHLISTNLGNKKTVYVR
>gnl|CDD|469027 NF041101, manno_glu_gly_synth, mannosylglucosylglycerate synthase
MKIALIHYRAGLMDGVSLEMEKWKKVLTRMGHEVDIVAGNNKEGVDVVIPEIGFENPKYRIINKNAFEKL
EDFSIDELLNEIFEESEEILHDFEEVLSKYDLIIPNNIWSLGAFLPAAIALTRYAEKHKEKPFIGHHHDF
WWEREYFLNPTDEKIKELLEKYCPPDLPNIKHVVINSIAKEALYRRKGIEATVVPNVMDFEEPPFISEEL
NLKIREEYNISENSIVFLQATRITERKAIELAIDLVALFNKLSKNYKGKKLYNGEIFSGEIVLAFSGMCE
DENYKYKLLDKAFKLGVRTVDLYPNVEKGVWSFWDLYSIADIITYPSILEGWGNQLLEAIIAKKPVVLFE
YEVFKSDIKNSGLEYISLGNRYILKEGLVKVDEEILEKAAKELFEILFDKEKYEETVEKNFEIGKKFFSL
ETLEKIIKRLL
>gnl|CDD|469028 NF041102, endonuc_V_Ttgales, endonuclease V
LHSWDLSPEEAIKIQKQLRSLLKLKPLEKEPRLVAGVDLSFPKKEYGLAVIVVLDFKNFKVIEVVYHVQK
VTFPYIPGLLAFREGPVFLKAWEKLKIKPDVVFFDGQGIAHPRKLGIASHMGLFIEKPTIGIAKSKLYGN
YEEPGNKKGSYSYLYDKGEIIGIVLRTRENVKPVFVSPGHLIDLDSSLKITLKFTTKYRLPEPTRLAHIY
TQKLK
>gnl|CDD|469029 NF041103, PFKA_PPi_Ttgales, diphosphate--fructose-6-phosphate 1-phosphotransferase
LAILVGGGPAPGINSVISAVTIEAINHGWEVLGIYDGFKHLAKGDTSKVIPLTIDDVSRIHFRGGSILGT
SRANPTKSEEDLENVVDTLKELGVTHLVTIGGDDTAFSASKVAKYAGGRIRVVHVPKTIDNDLPLPEGIP
TFGFETARHVGVELVKNLMEDARTTNRWYFVVAMGRKAGHLALGIGKAAGATLTIIPEEFREEKITLQTV
VDILVGSIIKRLAMGRNYGVAVLAEGLIEKIDPEDLEALGGVERDEHGHIRLAEINFGEILKKAVKKRLK
ELGIKITIVDKNIGYELRCADPIPFDIEYTRDLGYGAVRFLLEGGTGAMISIQNGRFVPIPFEDMLDPKT
GRTRVRMVDVESESYRIARRYMIRLEKEDFEDPERLEKLAAAAKMTPEEFKKRFGY
>gnl|CDD|469030 NF041106, ArsC_rel_Se_1, ArsC family (seleno)protein. Weak hits to Pfam model PF03960 and to COG1393 suggest a relationship to glutaredoxin-like arsenate reductase protein ArsC. This family contains significant numbers of selenoproteins
IDWYYHRKGCTTCKKAQAFLEEHGIEVKETVDARKERLDPEEALALLKGVDKIYAAKGKKVVEFDLKKDK
PDDEELLALLIGPTGNLRAPTLRIGKTLLVGFNEEMY
>gnl|CDD|469031 NF041107, RQC_minor_1, RQC-minor-1 family DNA-binding protein. The DNA-binding RQC domain (PF09382) appears primarily in RecQ, a DNA helicase involved in recombination, replication, and repair. However, it appears also in this uncharacterized protein family, to which we give the name "RQC-minor-1 family DNA-binding protein." A majority of members contain an additional C-terminal predicted zinc-ribbon domain. Members appear not to show any conserved gene neighborhood
PLPEEEIRAILRAADEIIATGGRTMLAKILKGSKDKKVLELGLDQCPAYGYYKSLTLEEITAKIDWMIKH
DYLEIEYDGRLPLLVFTERGWEIEREQYADELLQEWEEWLEQGKQPPDMIYLKDRNRGMILLLLEKIKES
GDKRYIPLLEAWEKIDYKKVRAEIREVIDHLES
>gnl|CDD|469032 NF041108, RQC_minor_2, RQC-minor-2 family DNA-binding protein. The DNA-binding RQC domain (PF09382) appears primarily in RecQ, a DNA helicase involved in recombination, replication, and repair. However, it appears also in this long, uncharacterized protein family, to which we give the name "RQC-minor-2 family DNA-binding protein."
YPSLTFLPIGKKNKEIRSIGHKEERGLLSRLNEAVSEALSALSQEEQQLLQTFLGLEGEAGLPVPIDKEE
ELYPHLIKPELFLWKKFSPQHGLPIHSEYFYPEDYTTLSKEQLERHLKQVIKDYLFCARIHQKSREEWLE
KINKAYHRHPFIQLAREKRDVIEAVERMNRSSLLSVLKYPEDVAYWRHRVEIVMRPYRSLPPEWFWDACE
HEKELTFHSSEESIECTCETCGYSVYYHVEEDRVTLEEEVNMEQAVKRIATIERQFNEIAEQNPKVIEKL
RKLQQLKQKLEPYEPLLEEILQLQEQLERRSIPAPPLLFLYKSLRSSTLPEERVESSLLWLSQVHLPDIA
LLKEVEEWLKLLKEELEKELQELLQELKEELEENQPKPDDVIFTIKGYPLTYGQVERILDLIHESDENVP
AHLLVQVLKGEATNKIRRLGLHETPIFGLLSDWPEKHIVKAFKQL
>gnl|CDD|469033 NF041109, VF_TspB_C_term, virulence factor TspB C-terminus-like domain. Members of this family share a C-terminal domain, perhaps a surface-anchoring domain, with T and B Cell Stimulating Protein B (TspB) of Neisseria meningitidis, an IgG-binding protein that helps confer serum resistance. This short domain (51 residues long) contains two invariant Cys residues and an apparent C-terminal transmembrane segment, suggesting a role in anchoring to the surface of the outer membrane. Member proteins often are found in prophage regions
CPAPITFSITLFGGQSFSFSYEPLCDFAELIRPLVIALAYLLAAFIVFGSL
>gnl|CDD|469034 NF041110, HPE1_fam_CxxC, plant virulence effector HPE1-like domain. This HMM describes the N-terminal 90 to 100 amino acids of a family bacterial proteins from plant-associated species. Most members of this family have some form of additional C-terminal domain of similar length. However, the best-studied members of this family are shorter proteins, virulence effectors from two plant pathogens, HPE1 ("hypothetical protein effector 1") from Candidatus Liberibacter solanacearum, and CLIBASIA_00460 from Candidatus Liberibacter asiaticus. Members of this family begin with an N-terminal signal peptide, for apparent Sec-mediated secretion, and nearly all share a CxxC motif
MRRLLLTAALLLAAGSAMASSIEVIHGGRAGNGSIITISCASCPPLKPKKKKKSYAVPSLAPGTQKVEIR
EIDGEKKLVRTEAWMGGSPVTFVS
>gnl|CDD|469035 NF041111, effector_HPE1, HPE1 family effector. The founding members of this family of virulence factors from bacterial pathogens of plants are HPE1 ("hypothetical protein effector 1") from Candidatus Liberibacter solanacearum, and CLIBASIA_00460 from Candidatus Liberibacter asiaticus
MRHLILAMLLSAFSTNIGKAQSVYHIHSPRITQKSSIHVKCHSCTLNKHHINKTPDSSSSVIYTQKEEII
DGKKAIVTTDNLMGGEPETFIKYFFEEEK
>gnl|CDD|469036 NF041112, chap_CsgH_alph, curli-like amyloid fiber formation chaperone CsgH. The designation CsgH was given to the broad set of homologs, found outside the Enterobacteriales, of the curli amyloid fiber formation periplasmic chaperone CsgC from species such as Escherichia coli and Salmonella. Members of the seed alignment belong to the Alphaproteobacteria. Because CsgC and CsgH proteins are related, and CsgH is defined broadly, this model does not exclude CsgC proteins, although they are covered also by a more specific HMM NF007507 (PRK10102.1)
RCEIRVEPSGGGVTLEAVVHADEAVSGSYRLSVTKRGGGGSSSIRQGGAFSLAAGETATLGTVSLSGAGA
RYDARLTVTAGGGTVSCAAR
>gnl|CDD|469037 NF041114, UPxT_UxV_star, UXX-star (seleno)protein family 1
VIIYGKDTCPYTRAAREAYAEKAEYIDVLKDPEKLEEMLELSGGVRRVPVIVEDGKVSIGFG
>gnl|CDD|469038 NF041115, UxxU_metal_bind, metal-binding (seleno)protein. Known members of this family are selenoproteins with an exceptional UXXU motif, with two selenocysteines. Known members so far derive primarily from MAGs, and have an N-terminal signal peptide N-terminal to the region represented in the seed alignment. Note that this model represents a specific clade of a more widely distributed domain that frequently appears 3 or 4 times in a single protein, so the domain-specific cutoff is critical to identification. Homologous domains, outside the scope of this model, are found in CopZ family copper chaperones and heavy metal-translocating P-type ATPases
ALAETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGFRAS
VIEE
>gnl|CDD|469039 NF041116, CBASS_cyclase_a, CBASS oligonucleotide cyclase
HRDLAYFADDKVNLPKEKAKEYRAQVNRLREKLEKKIAEDPDLKLVKMLLAGSFAKGTALRRTEDEPNDV
DVAFYVSGEDDAPNDLAKLLDWLAERLREAYPNKDPDDFEPQTKSVTISFRGSGLDVDIVPVLYDGDPDD
YGWLVSRSDGSRLLTSVPLHLEFIRKRKDASPVHFAQLVRLAKWWRNHQKLEDPEFRFKSFMIELIVAHL
LDNGGVFSDYPEALQRFFLYIAQTGLKERIAFTDYYGASDVPAFSDPVQIIDPVNPENNVAKRYTELERD
EIVDAAEEALDAINAAIAADTKGEAVEYWKEVFGPSF
>gnl|CDD|469040 NF041117, CBASS_cyclase_b, CBASS oligonucleotide cyclase
FEKFKSRLELNDREQELASERLDEIRDALEEEIEIEDDFLFGSYRRHTKTKGLSDVDILVVLNDTSLRDK
SPSEVLDAFARRLREKLPNTEVSVGRLAVTVDFGDGMSIQVLPAFKTGDGYKIPDTRDGKSWSKTNPKKF
AEKLTAANQACSGKVVPLVKMIKAWNRNLPKPVQPSYHIEVMAIDAFKGPYGGPKTYKRMLRHFFATAAD
RVLSPWPDPAGQSPHVDDYLGAARRARASRKRKAASQALERAIKLMRNGRTGESLEAWRELFG
>gnl|CDD|469041 NF041118, A_G_epim_Thtga, L-Ala-D/L-Glu epimerase
SKIKDVKFKLKKYEYEKPFHITGSISSEATNIEVELELEDGTKGYGEASPSFRVNGEKVEALLALESFVK
EMLVGMDVRNYRKIFEITDKLFATPSLKAAVQFAVLDAFSEEIGTPVYQILGGAKDEIETDKTVGIDTLE
NRVKDAKEIFDEGFRVIKIKVGENLKEDIEAMLEIAEVTKGAKYIVDANMGYTPKEAVEFAKALYRNGID
IAVFEQPVKAYDIEGLKFVRFNSPFPVAADESAKTKYDVLRLIKEEAVDFINIKLMKSGISDALAIVELA
KAANIQLMIGCMGESSLGINQSVHFALGTGAFDFHDLDSHLMLKEEKFRGKFKQEGPKIIL
>gnl|CDD|469042 NF041119, CheD_Thtga, chemoreceptor glutamine deamidase/glutamate methylesterase CheD
KKKIIGIGEYAVEKNPAILVTLGLGSCVGVCIRDKVAKIGGMVHVMLPDSRGGKTPKPGKYADTGIKLLV
EELKKMGANLSRLEAKIAGGASMFESKTMDIGKRNVEAVKKWLKYLGIRLVAEDTGGNRARSIEYNIETG
KLLVRKVGGGEKVEIIEI
>gnl|CDD|469043 NF041120, RqcH_arch, ribosome rescue protein RqcH, archaeal type. This HMM (built with support from arCOG01695) describes archaeal homologs of the RqcH (Ribosome-associated Quality Control H), involved in release of defective mRNAs that lack a stop codons and so are stuck on ribosomes. Conservation of a role in ribosome rescue for this archaeal family is supported by presence in a conserved gene neighborhood with homologs of Pelota/Dom34 and ABCE1/Rli1 homologs, proteins involved in splitting the ribosome into large and small subunits
SSVDLAALVRELKELLEGARVDKIYQYGPDELRLRLFKFGRGRGDLLIEAGPGKRIHLTKYPPEAPKTPP
SFAMLLRKHLSGARITSIEQHGFDRIVEIEFERGDEEYTLIIELFGRGNLILLDEEGKIIFALKQKEFRD
RTIKPGEEYVPPPSRGDPPEEDEEELLEELRESDRDIVRTLATGLGLGGEYAEEVCLRAGIDKNKPAKEL
TDEELEAIYEALRELFEEILNGKLYKVGEPVDVLPIPLKEYEYEKKEFDSFNEALDEYFSELELEEEKEE
EESEEEKEEIEKLERRIEQQEEAIEEFEKEAEELREKAELIYANYQEVEEILNTLRKAREKIKKILKEAE
EGIPAAKRVIEVDPAKGTVTLDLDGEEVELDIRKSVEENASRYYEKAKKLKRKIEGALEAIEETKKELEK
LEKKREEKKEEARRVRRKKEWYERFRWFITSDGFLVIGGRDADQNEELVKKYLEDNDIFFHADIHGAPAV
VIKTGGESVPEEDLREAAQFAASYSKAWKAGLGSGDVYWVYPDQVSKTPPSGEYLAKGSFMIRGKRNYIR
NVPLELAVGIIEYEGETRVIGGPPEAVKKRSEYYVVIEPGDFEKNDVAKKIYREFKEKLEVKKIASPDEI
VRFLPPGGSDIV
>gnl|CDD|469044 NF041121, SAV_2336_NTERM, SAV_2336 family N-terminal domain. This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems
DWEELADALWLAAQMGRAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSL
APPPPPPPGPAGAAPGAALPVRVPAPPALPNPLELARALRPLKRRVPSPRRVELDEEATAERIAETGLWL
PVFRPARERWLDLVLVVDASPSMVVWRPTVAELRQLLERLGAFRDVRVWRLDTDPDGGPQLVLRPGAPAQ
PLRSPRELIDPTGRRLVLVVSDCVGPAWRSGAAHRLLARWARRGPVAVLQPLPQRLWPRTGLPPERGRLL
RPEPGAPNARLRFTPPLLWDPEPAPDGALPVPVLELEPEALGAWARLVAGAGGARTPGALLLPDARQPAA
PEPRADRGPAELSAEERVRRFRATASPAARRLAVLLAAAPLSLPVMRLVQRAMLPESGPAHLAEVLLGGL
LTRLPGGDWTDGGGPWYEFAPGVRELLLASLGRTETAEVLRAVSEYIAQRFGR
>gnl|CDD|469045 NF041122, panto_kin_Thplsm, pantoate kinase
LIRAFVPAHITAFFVPIFNENPLLAGSLGAGINLSKGTNVFLSIEEGLERHIHVAFNGEPVKREEAVITY
SVAEKILPEDFIGEVEIWQYFDFPNGYGFGNSAGGALGTALALAYKFGGTLLQAAQIAHEAEVLHKGGLG
DVVAQLAGGIEIRIKEGGPGIGVVDNIFFEGYKVLVIPLGRLSTREVLDSDVVKAIEVEGKKALEKLLKN
PTPETLMREARRFAERTGLLSGELLEIAREIDKVLSLPSSMIMLGKGLFALVREEEVEKVKEVLKDLDLP
YDICEIYWGKPKVGRWIG
>gnl|CDD|469046 NF041123, phpantohe_syn_Arch, 4-phosphopantoate--beta-alanine ligase
MIPKDHPRYESLLTREKIVEGVKKGIVAKQGLIAHGRGEAFDYLIGEKTTESALEAERAAAALLLLAKHP
VISVNGNTAALAPDEIVELAKASGAKIEVNLFHRTEERVEKIAELLEEHGAIEVLGGTDERIPPLSHDRG
KVSEEGIYSADVVLVPLEDGDRCEALVRMGKKVIAIDLNPLSRTARTATITIVDNITRALPNMTKAAKEL
KDK
>gnl|CDD|469047 NF041124, CoaD_Thcocales, phosphopantetheine adenylyltransferase
RKKYRKVVVGGTFDRLHLGHKALLRKAFEVGEYVYIGLTSDEMIRDKPYAEKILPYELRLRDLIKFFEVN
GYSNYRIIKIHTAIGFADEMKSLEAIVVSEETYKGALVVNRAREENGLKPLEIVTIGLVKSSLGPKISSS
LIRAGLIDPFGRPLSR
>gnl|CDD|469048 NF041125, deph_CoA_kin_Thcocales, GTP-dependent dephospho-CoA kinase
FYFKLPPELREELKKPLGELIRGEIPEPYLKIKEELEKPFLVTVGDVVTENVLKLGIKPNLAIYDHKTKR
REYKPEIESNAVILTVKNPPGTITKALLNAIRKAYELAGRGRRVHIKVNGEEDLAAIPAVLYAPLGSLVL
YGQPDEGIVLIKVTPECKRRCAKILRRMEVVRDGD
>gnl|CDD|469049 NF041126, FBP_aldo_phos, fructose-1,6-bisphosphate aldolase/phosphatase
KITLSVIKADIGGIGGHTRPHPELLEAVEEVLKEAKKDGLLIDFYVTHCGDDIALIMTHTRGVDNEEIHK
LAWDAFKEATEVAKELGLYGAGQDLLKDAFSGNVKGMGPGVAEMEFEERPSEPVLVFAADKTEPGAFNLP
LYKMFADPFNTAGLVIDPKMHDGFKFEVMDVYEGKVIELNTPEELYDLLALIGDPGRYVIKSVYRKKDGE
IAAVVSTERLNLIAGKYVGKDDPVAIVRAQSGFPAVGEVLEPFAFPHLVAGWMRGSHNGPLMPVSLNDAT
PTRFDGPPRVIALGFQLHNGKLTGPVDLFDDPAFDYARRKAAEIADYMRRQGPFEPHRLPPEEMEYTTLP
KVLEKL
>gnl|CDD|469050 NF041127, exo_beta_glucsam, exo-beta-D-glucosaminidase
MKVEHDGKLYVIDGERVVIYGGTLQFFRVPRDAWKDRLEKMKRHGLNTVDTYVAWNWHEPEKGSFDFTGE
THPQRDLVGFLELAQELGLYVIIRPGPYICGEWRNGGIPDWLIDEHPEILAKGPNGPLPRDIYYPPITYL
HPTYLEAVMEWYEAVFPIIRDYLYTNGGPIISVSIDDEPSYWETIFQPFLTDYNEVITKPGGLWEKWLRE
NYSLDDLEERYGGDFSDYSEIKPPTSFSEPLPKILDWHHFKIWMINEYVRRLYEKMRRYVDVPISILDPY
LLLAAWRHFYRYVREHNLDIHLWTEFWYSFYRSFDFKEDKLGHIYYKTGIYRYYVRKLGTPPLSIETQSS
LAHTIEPDEAELLYSLLPALGIHNINYYLYVGGENPRGYESHNGVTWDVYSPIGLDGSERPHVEPIKWLG
EFLKSNKDFADSELKPKVAFGMYEPYEALNLWGYRPEFKESVNLNEYLLGERGLLTLLAMSNVPFDVVDL
EESTLEEMLSYEQLWVYSLDFMSREVQDKLVEFVERGGNLVILPMLPYLDENMKPYSALEDFLGVEVERE
KARDNFRLIPFVSVDAEGIDRMLVRNVVREVKGGEPIAFVGDKPVGALVRKGKGSAVVLGFRLQYYSSYH
DLHRKFVDKLLELQGVRRDFEVTDRDMIVIPRGNYLVLINPRGHRVKGKISYRGLEVPRLLDGIEMKKRG
VLFLPFGVRIGDVEVVYATATLLRGEGDVLTFRNHLSGTSEVALKGVESVKVSGGKIVDESDEGEVLRVV
IEHEGEEFELEL
>gnl|CDD|469051 NF041128, glucosaP_deam_GlmD, glucosamine-6-phosphate deaminase
HATLTEIRKTPEGIIKAQEAFERVKDEIRLPRRILYTGCGSSHFLSQLLAMATNALGGRGVALPCSELLY
SREYYPIGKPELIVAISRSGETTEVLKALEVLNVPKLGLTAYESSLSRKADYALIVPTPEESVVMTHSFT
AFYFAYLQLLRHSYGLETYDAEEVSELTEEALKNEGYIREIVEDFDFRNVIFLGSGILYPVALEAMLKMK
EMALFWSEAYPTFEVRHGFKSIADENTLVVLLVDEPFEWHEKLVKEFQGQGARVLLIGNEELGADYFIEV
PRLDELLTPIVYLPVIQLLSYYKAVKRGLNPDNPRFLEKVVRW
>gnl|CDD|469052 NF041129, maldex_phorlase_Thcocales, maltodextrin phosphorylase
IEKKLPENLEGLLELAYNYWWSWSRRATKLWEKIDPEHWREYKNPVKLLLDVPEERLKELSKDDDFLDLY
ELVIERFESYMNEENTWFSTNYPKWDKPIVYLCMEYGISKSLPIYSGGLGILAGDHLKTASDLGLPLIAI
GLLYKHGYFKQEIDKDGKQIEIFPEYNPEEMPIKPLLDEKGKPLLIEVPIDDRIVYARVFEVKVGRVKLY
LLDTDVPENPEEDRKICDYLYNAEMDKRIKQEILLGIGGMRLLKALNIEPGVIHLNEGHPAFANFERIKW
YMEEGLSFEEALEVVRGTSVFTTHTPVPAGHDKFPVDFVEKKLAKFFEGLPKEKFLSLGKEEENDPEFNM
TLLAIRTSSFVNGVSKLHAEVSKEMWRNLWKGVPLDEIPIEGITNGVHTLTWVHNEIAKLYDRYLGRVWR
EHTNLEGIWYAVERIPDEELWEAHLKAKKEFIELIKRKIRRRNERLGIDEPLPEIDENALIIGFARRFAT
YKRATLILSDLERLKKIVNNPERPVYIVFAGKAHPRDDAGKEFLRRVYEVSQMPEFKGKIIVLENYDMGS
ARLMVAGVDVWLNNPRRPLEASGTSGMKAGLNGVLNLSIYDGWWVEGYNGKNGWVIGDESTEPETEEDDP
RDAESLYDLLENEVIPTYYENREKWIYMMKESIKSIAPRFSTHRMVKEYMDKFYSKAMENGIWLSRDNFE
WAREIAAWKEKILESWDKVSIERILTEDARSVEVTVNLGGLSPEDVKVELYYGVKAEGYIIEKPYIIELR
HPQSLGGGRWIYRYEGNALKNLGNPCWHYAVRVYPYHPKLPHKFLL
>gnl|CDD|469053 NF041130, PenR_Burk_TF, beta-lactamase transcriptional regulator PenR. PenR, as the term is used in Burkholderia, is a LysR-family transcriptional regulator of adjacent chromosomal class A beta-lactamase genes of the blaPEN family, which include blaPEN-A in B. multivorans, blaPEN-B in B. cenocepacia, etc
MTKLRPHLPLNALRAFESSARHLNFTRAGLELSVTQAAVSQQVRSLEERLGCTLFTRLPRGLGLTDEGRA
LLPVLSDAFSRIETVLKQFDGGRFREVLTLGVVGTFAIGWLMPRLKRFGDTHPFVELRLRTNNNVVDLAA
EGLDFAIRFGEGNWPATRNERLLDAPLTALCAPEIARRLAQPADLANETLLRSYRTDEWLGWFDAAQLEP
WTVNGPVFDSSRLMVEAAMQGAGVALAPACMFARELQLGLLARPLDIDVHAGGYWLTSLKSKPLTPAMTL
FRDWIVAEAADA
>gnl|CDD|469054 NF041131, RicT_YaaT_fam, regulatory iron-sulfur-containing complex subunit RicT. RicT in Bacillus subtilis (originally YaaT) was described as stage 0 sporulation protein affecting phosphorelay signals. However, RicT belongs to a iron-sulfur containing regulatory complex that is conserved also in many non-sporulating species, together with homologs of YmcA (RicA) and YlbF (RicF)
DYVIVETERGLELGKVVLGPKEVSEEELKKPLKPIIRKATEEDLERYEENKEKEKEAFKICREKIAEHGL
DMKLIDVEYTFDRSKLIFYFTADGRVDFRELVKDLASIFRTRIELRQIGVRDEAKMIGGIGPCGRPLCCS
TFLGDFEPVSIKMAKEQNLSLNPSKISGVCGRLMCCLKYEDDFYEEAKKKLPKVGSKVETPGGKGKVVSI
NIL
>gnl|CDD|469055 NF041132, DNA_protcyst_Mta_Thcoc, methylated-DNA--protein-cysteine methyltransferase
MLSVEKFKIAGREVWIGVLFEEKIQGITFSLDGEEFLRERIERLAEFLRKRGVKVSLEEEESDYPELVFD
VLIGKIDNEEALEELSFEGLTPFERKVYEWLTKNVKRGEVITYGELAKALGTSPRAIGGAMKRNPYPIVV
PCHRVVAKDGIGYYTPKLEYKKFLLEIEG
>gnl|CDD|469056 NF041133, branch_enz_Thcocales, 1,4-alpha-glucan branching protein
GYLTFVLHTHIPYVRKHGKWPFGEEWLFEAISETYIPLLMEFERLKEKGVKFELVISFTPVLMEQLADEY
IKAEFEKYMERKLKAMREDLEKGKDEKLKKAISYMIGYFEDVYSYWKAINGDIIGKFRELQDEGYVEVIT
SAATHGYLPLLGRDEAIEAQIANGIATYEKHFGRKPRGIWLPECAYRPDGLWKSPSTGEVVWRKGIEKFL
KKFGIEYFFVESHLIDEGPASSKYGEILPAKTKKSTLRPYFLKNGNIAVFARNRETGHQVWSADIGYPGD
FWYREFHKKAEKSGGQYWRVTGKDIDLGEKEPYEPEKAMERVEEHARHFVSLVKSLLEEFEEKEGEKGIV
VAPYDTELFGHWWFEGVKWLGRVLELMAEEGIKTTTISEFLDNYSGERYEIELPEGSWGMFGTHYTWWNP
EVEWTWPHIHLAEDRMVALASKYLGKDRLGDRVLEQLGRELLLLEASDWQFLITTGQAKEYGKRRILEHA
HDFHRLANELERYFETGEFDEMELLEELEERDNPFRPIIVEPYVSEEPPEVPEYVEPPEVPPE
>gnl|CDD|469057 NF041134, R1P_kin_Thcocales, ADP-dependent ribose-1-phosphate kinase
LDVVGIGNLNYDIIMLLDRFPEFHEKVNAKKAYFGLGGAAGNTASWLAHMGLKVGFIGAVGNDEIGEAHI
EYFKKIGVDTSGIKVVDEPSGVAVAMIHGEDKRIVKYPGANRFRELDFEYLARARHIHLSSNPPELIEEA
VNFAKERGITVSLDIGEAELPEEVEEKIDYLLMNEDEFKRKYGSLDKISLVKAKNLIVTLNGGGALVRDE
KGEVFEVRGLSAKVVDSTGAGDSFDAGFIYGVLKGWSLEDSAKLGMLLAYLTVQKVGARSAIVPLEEIKK
IAKELGLELPF
>gnl|CDD|469058 NF041135, IPPtranDIPPsyn_Thcocales, bifunctional L-myo-inositol-1-phosphate cytidylyltransferase/CDP-L-myo-inositol myo-inositolphosphotransferase
MKAVILAAGLGTRMGGKPKGLLKVAGREILYRTMKLLSELGVKEFVIVTNEKYRKKYEEFLKKNGFNAKI
VINPHPERGNGYSLYLAKNHVSGRFVLVMSDHVYEEAFVEEAVKGEGLIADREPRYVDIEEATKVKVENG
RVKDIGKDLKEFDGVDTGFFVLDPSIFEVAEELLKEKEEIELSEVVKRAKLPVTFVDGLFWMDVDTPEDL
KKARKLLVKTAVKGTGDGFISRHLNRKISTRISALLVDHITPNQATVLTFLLGIFSALLNFFSPPLAGIL
YQISSILDGVDGEIARASMRTSKFGGYLDSILDRYVDFAFLLTLAYVTLPEPLLWWAIALLAIFGSVMVS
YSTERYKGAYGRDAYKEIPALRYLPGKRDERIFLTMIFCLLGLIKALFALLAVLTNLRVALTLYLVWRK
>gnl|CDD|469059 NF041136, MrpORP, iron-sulfur cluster carrier protein MrpORP
LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPV
EYSDNLKVMSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDA
GAVIVTTPQELALADVRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLG
RIPIDPEIVEAGDAGRPFVLDYAWSPAAKALEKIVDPILELLENKKSLTEEPGTMKIAIPTANGKLCAHF
GHCEQFALFDVDGGKIVKKETLTPPPHEPGVLPRWLAEQGVNVIIAGGMGQRAQDLFAEKGIEVITGAPS
GSPEELVAQYLSGTL
>gnl|CDD|469060 NF041137, B3_blaSPR, SPR family subclass B3 metallo-beta-lactamase. Members of this exceptional subfamily within the subclass B3 metallo-beta-lactamases, SPR (described originally in Serratia proteamaculans) have an altered zinc ion binding site that binds a single Zn(2+) only in the absence of substrate, but may recruit a second Zn(2+) after substrate binds. Purified enzyme is effective against benzylpenicillin. The assignment as subclass B3 enzyme is based on homology, not Zn-binding residues. Note that additional examples of functional B3 enzymes with altered Zn-binding sites have been described
MKKSMHYLMAMAFSLSFSTQAKLDPAQPLSSAPPYSLFEEWAQPIAPFQIFEQVYYVGTSNLSSVLLSTP
QGLILIDAGLESSAPGIKANIERLGFSIKDLKYILNSHARLDQAGGIAQLKRWSGARLVASAANARQLAL
GGRQDFALGDMLTFPAVQTDIVVADGDSITLGGLTLTAMMTPGHLPGATSWLTTLRHNGKPYRFIYADSL
ATPDYYLIGNKNYPQLIEDIRGSFARLARVQADIFIANKGTRFALADKWRRLQAGDTQAFIDPAGLQRYV
QESQQGFEEQLKRQENVKR
>gnl|CDD|469061 NF041139, TreT_Thcocales, trehalose synthase
MYEVKKFGGKGKKLEDYKSIIGEEAIEKIKEKAEDLKGKSFVHVNSTSFGGGVAEILHNLVPLMRSLGID
ARWFVIEGTDEFFNVTKTFHNALQGNKELKLTEEMKDLYLETNKENAENLDLSEFDYVLIHDPQPAPLIE
FYEKRQPWIWRCHIDLSDPNPEFWSFLRRFVEKYDRYIFHMPEYVQKDLDKNKVVIMPPSIDPLSEKNIE
LSDSEILKILERFDVDPDRPIITQVARFDPWKGVFDVIEVYRKVKEKIPDVQLLLVGVMAHDDPEGWIYF
EKTLRKIGEDYDVKVLTNLIGVHAREVNAFQRASDVILQMSIREGFGLTVTEAMWKGKPVIGRAVGGIKF
QIVDGETGFLVRDVDEAVEKTLYLLKHPEVAKRMGIKAKERVKENFIITKHLERYLDLLNSV
>gnl|CDD|469062 NF041140, Trm10AGmtase_Thcocales, tRNA (guanine(9)-/adenine(9)-N1)-methyltransferase
MKKLGDVFRELLREKGIEKVGTLSKRIPKRGSKDKLQDIALAVLEGKGAIVEVPEPTAIAWDLSGKRVEG
SKYAYIPLCMAEKFEIVLTPEELRAKLPEYPYFIIDLMHWDKHTPKEKGKVALQVSQSYGVLRDYLWGEL
LAVTWANEEFKELAKFPLDRVTAYEGPTAEFLKEKGIDEVVLLDPWAEEVLSEEDFSVKAFIIGGIVDTG
GTKKGTTAKIGEALESEGIKVRRRKIVLRGDVIGVPDRINHILEILLKMLVEGKDMEEAVLEVQSPLHAR
WRLRKELPKRKIRYLIDGKKYLVVEKELFDEYSKWLNIRWEDFVKVLRELGFVALERKRIHHLNKISNPR
IINGKLYRVILLKKAAMLCYNC
>gnl|CDD|469063 NF041141, tran_reg_TrmBL2, HTH-type transcriptional regulator TrmBL2
MVKDRMVELLQEHFELNLYEARAYVALVAFGVLTPAELASVSEVPAPRTYDVLRSLEKKGFAISQPGKVN
KYRPVHPKNILEKFIEEWQERVKEELEAKKKAKEELLELMTPLIETEIPKYGVERVWVVRGIRNSTLKTK
EMLEEVEKEILLADDGYIAINLENDIIKAVDKGVKAKIVVTKQLLPRLETSKIMDYYKEGKLELKALDKI
ELPMLICDEEVFFALEDLAARYFNYETQVWIKDFRVVELFKGKFNEYWEKAEKV
>gnl|CDD|469064 NF041142, PCNA_Inhib, PCNA-inhibitor
MDRKLDEFINNSIPKKKEEPSAKPRRKKKRLKSTSLDSFLPEEHINYFKALRIGSKKIRNAKIEE
>gnl|CDD|469065 NF041144, expansin_EXLX1, expansin EXLX1-like domain. This HMM represents nearly the full length of EXLX1 (YoaJ) of Bacillus subtilis, a cellulose-binding bacterial expansin, and similar domains in related bacteirial proteins. Expansins, which are small and non-catalytic, have the ability to loosen plant cell wall material and improve enzyme access, but an expansin domain can occur as an auxiliary domain in cellulases such as CelA of Clavibacter michiganensis, a bacterial pathogen of tomato plants. Pfam model PF01357 (expansin C-terminal domain), somewhat less than half the size, is related but is oriented toward plant expansin and hits relatively few members of this family above cutoffs (as of version PF01357.23)
GEATFYGAGYGGGACSLDPIPADMMIAALNPADYNGAAACGAYLEVTGPKGTVTVRVTDRCPECAPGHLD
LSPQAFAKIADPVAGIVPITWRLVSAPSGPGPVSYRIKEGSSQYWAAIQVRNHRNPVAKLEYRKGGTWVA
LPRTDYNYFVSESGMGTGPLTIRVTDIYGQVLTDTGIPLPPGVVQPGNVQFP
>gnl|CDD|469066 NF041153, organophos_OPH, organophosphate hydrolase OPH. The organophosphate hydrolase OPH, also called aryldialkylphosphatase (EC 3.1.8.1), Phosphotriesterase, and paraoxon hydrolase, is the product of opd (organophosphate degrading) gene clusters found in mobile elements. It is a zinc ion-binding lipoprotein
MQTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITVSEAGFTLTHEHICGSSAGFLRAWP
EFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFDPPLSMRL
RSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVLKAAARASLATGVPVTTHTAASQRDGE
QQAAIFESEGLSPSRVCIGHSDDTDDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTR
ALLIKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGIT
VTNPARFLSPTLRAS
>gnl|CDD|469067 NF041155, encap_f1, family 1 encapsulin nanocompartment shell protein. Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide
LHRELAPISDAAWAEIDEEAVRTAKRHLAGRRFVDVYGPLGWGLSAVGTGRLDPLEEPGEGVEAGQRKVL
PLVELRVPFTLSRRDLDDVERGAKDLDLSPVKDAARKIALAEDRAIFNGYAEAGIEGLLNASGNPTVKLP
SDVENAPAAVAEALNKLREAGVDGPYALVLSPDLYTALQRTQDGGYPEIEHIRRLVDGGVIWAPAIEGAV
LVSTRGGDFDLVIGQDLSIGYLSHDAMNVELYLQETFTFRIKTPEAIVVL
>gnl|CDD|469068 NF041156, FolD_Thplmales, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MILDGEEIAEKKMERLKNEIEKIKNKYGIEPKLKLIQIGNDYASTIYANAKIRRGKKLGIDVDLEKYDNI
TMDDLVKLIKDYSADPDINGIMVESPLPKPINYYDIVKNIPYYKDVDGLSPYNQGNLYLKNEFIAPATAR
AVVDILDYYGIKSGNVCIINRSPVVGRPLSMMLLNRDYTVSVCHSKTVDIKEIARSSDIVVVAVGKPGFL
DRSYVTDKSIVIDVGINYVNNKICGDANFDNVSEKVKAITPVPGGVGPVTATDIFENFINGAKYQIK
>gnl|CDD|469069 NF041157, Cit_synThplmales, citrate synthase
MEISKGLENVFIKYTSLTYIDGEKGILRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINE
SYEVPDHVISIIRSLPRDSDALAMMETAFSALASIENYKWNKENDREKALKIIGKASTIVANVYRHKEGL
KPRIPEPSESYAESFLRATFGRKPSEEEIKAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALA
ALKGPLHGGAAEAAFKQFLEIGSPDNVEKWFNENIINGKKRLMGFGHRVYKTYDPRAKIFKEYAEKLAST
NEAKKYLEIAEKLEELGIKHFGSKGIYPNTDFYSGIVFYSLGFPVYMFTSLFALSRVLGWLAHIIEYVEE
QHRLIRPRALYVGPEKRDFVPIDERK
>gnl|CDD|469070 NF041158, Spm_actase_Thplmales, spermidine N(1)-acetyltransferase
MITIRKLSAEDVDALIEVARESWKWTYRDIYSNEFIESWISEKYSKEKLLNEIIRSQSNLDIIFLGAFVN
SALIGFIELKIIADKAELLRLYLKPEYTHRGIGKLLLSEAEKIMK
>gnl|CDD|469071 NF041159, Rham_dhyd_Thplmales, L-rhamnose 1-dehydrogenase
MDFKNKNAVVTGGSRGIGNAIAKGLADNGANVIITYASNDSAADEVVNYIKSKGVKAYKYKIDQSDINEI
PRFIDFVKSTFKTVDILVNNAGICPFKDFFDIDVDLFEKVWKVNVESHFFITQRISKIMIENNINGRILF
ISSISAIVGGEFQAHYTTTKSALNGLMHSLAIILGEHGIMVNSLEPGTILTDINKEDLSNQEKRRYMEKR
IPLGRLGLPEDIAGPALFLVSDENTYVNGAELLVDGGMLVNLQ
>gnl|CDD|469072 NF041160, DGGPL_Thplmales, digeranylgeranylglycerophospholipid reductase
MLNYDVLVVGAGPAGSSAARYAARYGLKTLLIEKRPDIGSPVRCGEGVSKAWMPEVDIKPEDHWISDEVK
GARIYGPSEKKPIMLTAEKAGNEVGYVVERDKFDKHIAALAASEGADVWVKSPALSVIKEGNKVVGAKIR
HNGEIVDVRAKMVIAADGFESEFGRWAGLKSLILAKNDIISALEYRMINVDSDEDYTDFYLGSIAPAGYI
WVFPKGPHEANVGIGVTISKMKDRFDVKNYLDRFIKSHPGYSKGKIIQLITGGVSVSKVKDKMTMPGLLT
VGDAARLIDPITGGGIANGMISGKYAAQVSKKAIDSNDYSEEMMKNYEKMVKDKFERKHLRNWFAKEKLA
TLSDDTLDKLVDVVSDVKITTISVEEILKAVQLKYPELVEELEDLI
>gnl|CDD|469073 NF041162, encap_f2a, family 2A encapsulin nanocompartment shell protein. Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide
LGDVAARQLANATKTVPQMETITPRWLVHLLPWVPVEAGIYRLNKVKEPDTVEVLCSQRDESELPETFVD
YEENPREYVLSAISTVLDVHTRVSDLYSSPHDQIAEQLRLTIEAVKERQESELINNPDYGLLANVAPSQR
ISTRTGAPTPDDLDELITKVWKEPAFFLAHPRAIAAFGRECTRRGVPPPTVSLFGSQFLTWRGIPLIPSD
KLPVEDGKTNILLLRTGESRQGVVGLYQPGLPGEQSPGLSVRFMGIDRNAIASYLVSLYCSLAVLTDDAL
AVLENVEVGNYHDY
>gnl|CDD|469074 NF041163, encap_f2b, family 2B encapsulin nanocompartment shell protein. Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide
SLSTAAARNLATTTKTVPQMQGITSRWLLRMLPWVQVSGGTYRVNRRLTYTVGDGRVTFTNTGADVRVIP
AELRELPLLRGFDDEEVLAALADRFVQREYAPGEVIVEAGQPADRVYLIAHGKVEKLGTGEYGDETVLGV
LADGDHFGDQALLDSDGTWDYTVKAVTACTVLTLPRQAFAELLDRSPALRAHLDRFRAAPRPPQNKYGEA
AIALASGHSGEPELPGTFVDYELAPREYELSVAQTVLRVHTRVADLYNEPMNQTEQQLRLTIEALRERQE
HELVNNREFGLLHNADLKQRIQTRSGPPTPDDLDELLSRRRKPAFFLAHPRAIAAFGRECTRRGVYPDTV
DVFGHPVPAWRGVPILPCDKIPVSPTGTTSILLMRTGEEDQGVVGLHQTGIPDEYEPGLSVRFMGIDEKA
IISYLVSAYYSAAVLVPDALGVLENVEIGR
>gnl|CDD|469075 NF041164, NucKinThplmales, nucleoside kinase
MKFLAFFGHLNIDVKISVPSLPMPGESVGVKNLREKFAGTAGNFAIVAKKLGLDFDLYSAVGSKTHSGYL
AFLKKRGINTDHVKIFKDENGPICYIASDGKEQVAYMYQGPMNNWKPSLHFEYEYTYIHFGTGPVKEYMK
IAERNKKSKIVFDPGQEIWYKYNKEEAKYMVNHSYISIFNRNEFYVLLEMTGLSSADVYNTVDYIIVTEG
ERGSSLYEDGEKKHFPAIKSDRIGDTIGAGDSFRAGFYFALYNNYSIEDSVSIGNIVASHAIEDGIIEFS
LNFNDIEKEFKNYKS
>gnl|CDD|469076 NF041165, ZFX_Thplmales, zinc-containing ferredoxin
MVKLEDLDFKPKPIDENFLEDEKNYPVTGEHNGHKVRAEGKQRMDADGKPYPTKLGIHGTIVAVDWDCCI
ADGACMDVCPVNLFEWELNPGKSGTGNDKKIEKGDKELWEKYRTDKCDPVRESECIFCMACESVCPVSAI
KINP
>gnl|CDD|469077 NF041166, f2_encap_cargo1, family 2A encapsulin nanocompartment cargo protein cysteine desulfurase. Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization
MTTPTPTSNGALSAPAGLPDPATLARLANELFSALPGEAPAPGLPAAPPAAPAPPGSNPAPAAGPGGLGA
GVPGAALPQGLVPGANLLPSAPSPVGALGASAPALAPHAAAGNVGLPDAVVAVAPAEPRAGGAALPVGLP
QAPVPAAPSAAAAPPDLVAPQAFGLPGEDAALRALLPAASPAPPSAPSAAAAESSYYFLDERAAPSPAAA
PPGSPPALASAHPPFDVNAVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAA
HELAARATDAYEGAREKVRRFIGAPSVDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIV
PWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVL
VDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDLLEAMPPWQGGGNMIADVTFEKTVYQP
APNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGLAEVPGLRLIGTAADKASVLSFV
LDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAVLRRL
>gnl|CDD|469078 NF041167, f2_encap_cargo2, family 2 encapsulin nanocompartment cargo protein terpene cyclase
GGPTGLGTSAARLPSRLAAPPAAGAVSEPAPTPAAPEPPWGDGAIPGLYCPPAVRDDPALAAEVNRRLVA
WAEEVGLYPGELDKLRKADFGRLMMLAHPDTDDPDRLLAAAKCAVAEWAVDDYYCDDESLGASPELLGPR
LALAHAAMDPAHLPGEYAPQLEEALRADPVLRALRSAFEHLARYATPAQVQRLRHELAIMFVAYGAEAAW
RATGRVPPVWEYLAHRQHNSFRPCMTLIDAVGGYELPADLYADPRVRRAFTLAGTAAVLVNDLYSMAKEL
ASDGRHFNLPLVIAAEEGCSLREAVLRTVEIHNELMHAFEAEAAALSATGSPELRRFLAGLWAWMGGNRE
WHATSTRY
>gnl|CDD|469079 NF041168, f2_encap_cargo3, family 2 encapsulin nanocompartment cargo protein terpene cyclase
QPFELPDFYVPYPARLNPHLEGARAHSKAWAREMGMLDSPGDGDGEPVWDEADFDAHDYALLCAYTHPDA
PAPELDLITDWYVWVFFFDDHFLEAFKRTRDLAGARAYLDRLPAFMPVDPGTAPPEPTNPVERGLADLWP
RTVPTMSADWRRRFAESTRNLLEESLWELANISEGRVANPIEYIEMRRKVGGAPWSANLVEHAVGAEVPA
RVAASRPMRVLRDTFADAVHLRNDLFSYQREVEEEGELSNGVLVVERFLGCDTQRAADLVNDLLTSRLQQ
FEHTALTELPALFDEHGLDPAERADVLAYVKGLQDWQSGGHEWHMRSSRYMNAGAGAPTGPVPGGPTGLG
TSAARLGLSPGAPGPGRLRSHTHVPFQRVGPVPLPDFYMPYPLRLNPHLDAARRNSKEWARRMGMLDVVP
GVGVWDERKFDGADFALCAAGIHPDAPAAELDLSADWLTWGTYGDDYFPVVFGRTRDLAGAKAFNARLSA
FMPLDAGPLPVPTNPLERGLADLWSRTAGPMSPEARRAFRRAVEDMLESWLWELANQIQNRVPDPVDYIE
MRRKTFGSDLTMSLSRLAHGDSLPPEVFRTRPMRALENAAADYACLTNDIFSYQKEIEFEGELHNGVLVV
QRFLDCDRQQAVAVVNDLMTARMRQFEHIVATELPALFEEFGLDAEAREALRGYVEELQDWMAGILHWHR
GTSRYKEAELRREPAPWPVPPGGPTGLGTSAAR
>gnl|CDD|469080 NF041169, f2_encap_cargo4, family 2 encapsulin nanocompartment cargo protein polyprenyl transferase
AAEVLAWSRALVDPALRAAVDTLPGSMRRVAGYHFGWWDADGTPAAADGGKAIRPALVLLAAEAVGGDPA
AAVPAAVAVELVHNFSLLHDDVMDGDDTRRHRPTAWTVFGVSDAILAGDALLALALEVLAGSPHPAAAAA
ARRLAAAVQELCEGQYADLAFERRDDVTLAECLRMAEAKTGALLGCACALGALLAGADPEQVDALDAFGR
ELGLAFQLVDDLLGIWGDPAVTGKPVGSDLRARKKSLPVVAALTSGTPAARELAELYRRGGPLDEAELAR
AAELVEAAGGRAWAQAQADDRLARALAALRAAVPDPAAAAELLALARLVTRRDH
>gnl|CDD|469081 NF041170, Oxoac_fdxalpha_Archa, 2-oxoacid:ferredoxin oxidoreductase subunit alpha
MDISWMIGGPQGGGVDTSANIFGRAFARAGYYVFGNREYYSNIKGRHSYFHVRVSDKRPRSLSYPVDILA
AFDAETVFTHFDEVKEGGYLIYDKGVENTKLDEIQSMEPELKERIKKELKSKGVPPTVKSVVKYLESKGV
KLIPLDYDEILKKLAEKLKVPLSVVVRYKNTIAVAASAALLGLDEDYLLDAIKRTFKGREKIVELNKMAA
ELVYDYVKPNFGLLEKPLPPVEKRRIQVDGNDAVAMGKIVGGLRFQSYYPITPASDESVYLEAHQEVLLD
DPEGDKRKGSIVVVQTEDELAAINMAIGAALTGARAATATSGPGFSLMAEGLGWAGMNEVPVVITYYQRG
GPSTGLPTRGGQSDLLFAIFAGHGEFPRIVIASGDHEEAFYDAIWAFNLAEKYQTPVIHLVDKFLANSYS
TIPRPDPDKVKIDRGKLVDKNPGGDYKRFELTEDGISPRAFLGLAAIFWYTGDEHDEYGHITEDPENRIK
MYEKRMKKLETADKEIPEEERAKLYGDEDADILLVTWGSPKGPILDAMEELKKEGIRAAYLQLKMFSPFP
SELVKKLLSGKEKIIDVEHNYLAQAAKLVKMNTGIEITKYILKYTGRPMTRDEVYEAVKKILEGKEKRVV
LSYGA
>gnl|CDD|469082 NF041171, Oxoac_fdxbeta_Archa, 2-oxoacid:ferredoxin oxidoreductase subunit beta
EWVDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLA
NPELEVIVNGGDGDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQD
AVNPIALALASGYTFVARGYAYDVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKRVYKLDD
EPGWDPVVRSPEEADEKMAKAIEKALEWGDRIPIGIFYQNELVPTFEERIAERLPNYLDNPPAKQPIEKD
GKPVTIIEDIFKEKIV
>gnl|CDD|469083 NF041172, AcrlCoa_red_Thmprot, acryloyl-coenzyme A reductase
MKAVVVPGKKQGYEIREVPDPKPGKGEVLIKVKRAALCYRDLLQLQGYYPRMKYPVILGHEVVGVVEEVG
ENVPGFKPGDRVVSLLYAPDGTCDYCKRGEEAYCKNRLGYSEELDGFFAEYAKVKANSLVKVPSGVSDEG
AVLVPCVTAMVYRGLRRAGLRKGETVLVTGASGGVGIHAIQVAKALGARVIGVTSSEDKAKIVGKFADHV
IVGSKFSEEVKKLIGDVDVVIDTVGTPTLEESLRSLRMGGRIVQIGNVDPSQSYSLRLGYLILKDIAIIG
HASANKKDIEETLKLTREGKIKPVVAGTVSLEEFDKALEMLKDKSRVGKVLLKP
>gnl|CDD|469084 NF041173, Sug_nt_acttase_Thmprot, bifunctional sugar-1-phosphate nucleotidylyltransferase/acetyltransferase
MKAVILAAGKGERLEPITHTRPKPFVPILGSTLIERTIEILRKLVNDIDIVVVIPDELPSEYKEFFSRLN
GVKLVEQGERKGTAAALSSVRSLISDEFLLIYGDVFFDEESIEKIINSEGNAILGVEVNNPKEYGVLVID
NEGYLSKIIEKPENPPSNLINGGIYKLSSDIFTYIDKISISSRGEYELTDAVNLMAKENKVKVIKYNGFW
IDIGRPWDIIDANKWALDREKSKILGEVEDNVKIKGKVIIEEGAKVLSGTYIEGPVYIGKNSVIGPNSYI
RPYTVLGSNVKIGASVEIKESVIMENTKIPHLSYVGDSVICEDVNFGAGTLIANLRFDEKEVKVNIKGKR
ESSGRKKLGTIIGGHVRTGINVSILPGVKIGAYARIYPGAVVNRDVNKGEFFKA
>gnl|CDD|469085 NF041174, SDX_Thmprot, sulredoxin
AWKRTISAKALEKAGSAAVKLVDGKVVFIANVNGKLYGIDAVCSHARCILGILDEDKLTVRCPCHHAVFD
LRTGKMLEPPYVAPNAPKEKLGLKTYNVRENGGWIEVDV
>gnl|CDD|469086 NF041175, RNAseHI_Thmprot, ribonuclease HI
MAIGYFDGLCEPKNPGGIATYGYVIYLDNKRKIEGYGLAAEPWSKDSTNNVAEYTGLICLLEKLLELGIS
EVIIRGDSQLVIRQLNGEYKVKSPRIIPLYEKALELLSKFRSIEFEWVPREENKEADRLSRIAYELVLKG
KLKK
>gnl|CDD|469087 NF041176, GlyK_Thmprot, glycerate 2-kinase
VKKILEYSDPYKALSEKVKVSKNEIIVNGFEFQFTKPLVISVGKASYKMANFFLDRLKPVKSLVVTPKGS
NKVLGNAEVIESGHPYPDESSFKAGKRVIELLRKEDYDLVIFLLSGGASALMEDPVIPLEEYREINKKLV
TSGLSIDEINIVRKHLSKIKGGRLAELSKAPVVTLIVSDVPGNDLSSVGSGPTVPDPSTVEDALEILEKI
GLSEYLKYLIETPKELNNSKNFIILDNMEVLKKLSNHLPNPLILSSEVRGEARDFGAFLASIYNSSRSYS
IPFKRPFTLLLGGEPEVTITGKAGKGGRNGEVCLSFLKYVRGNKFKLYAIATDGIDGNSEYAGCIVDSSM
KIPKDEIEEALRNHSSYELLEKYGAVIKTGPTGTNVNNVYVLIAP
>gnl|CDD|469088 NF041177, Cyp119_Thmprot, cytochrome P450 Cyp119
MYDWFAEMRKEDPVYYDGEVWNVFKYEDCKEVLNDFKRFSSDLTGYNEKLEDLRSGKILFDIPTRYTMLT
SDPPLHDELRSMTADFFSPSNLQTLENFIRETARSLLSNLDNEFDVIRSFAVPLPIIVISKLLGLPIEDV
KKVKEWSDLVALRLGKPSEIFTIGKKYLELIQFVKNHLNSRKEGEDLTSKIANSNLSDIEKLGYIILLLI
AGNETTTNLIGNAIVDFTRFNRWDYIRGENGYLKAVEEALRYSPPVMRTVRVTKEKVKLRGQTIEEGELV
RVWIASANRDEEVFHDPDSFIPDRSPNPHLSFGSGIHLCLGAPLARLEARIALEEFSKKFRRVEILEKEK
IPNEILNGYRKLVVRVKT
>gnl|CDD|469089 NF041178, TQO_small_DoxA, thiosulfate:quinone oxidoreductase small subunit
MERTVIIGIIFAVLVVGWILGTGQWAYGNVVGPLVNYSKLPKLEITYINAYPTGNGTLLILNITDVDGPD
AYPASAPLMEIYNSTWHIYLNSSQISNYTVKVIQAPWNENKKDYVNWYSGFVVILGSEAQFQLLLPIHLS
PGTYTVKLYTPAISPKSEATATFTI
>gnl|CDD|469090 NF041179, TQO_large_DoxD, thiosulfate:quinone oxidoreductase large subunit
MSNKEVDLKNMTRTEYLFPLRFAVGWMFLDGGLRKAVLKPAKLDPNSSSFVGGKLVNFLPHAGPFKGFLL
MTLENRSLDVTFLTIFSYVEIIVGLFLIIGLLTRLAAFGALAMAIGFAPAYWLGSTCEDEWQIGALLTAG
SVTLMLTAAGRVWGLDYFLYKKFGDRGLSNNVPILKWIKLW
>gnl|CDD|469091 NF041183, Pks2_ls1_myc, sulfolipid-1 biosynthesis phthioceranic/hydroxyphthioceranic acid synthase
VTPVAVIGMACRLPGGIDSPELLWEALLRGDDLVTEVPLDRWDVDEYYDPEPGVPGRSVCKWGAFLDNVA
DFDPEFFGISEREATAIDPQHRLLLETSWEAMEHAGLTPATLADSRTGVFVGLTHGDYTFVAADAQALEG
PYGNTGTSFSMASGRVAYAMGLHGPAVTVDTACSSGLSAVHLACRSLHEGESDLAFAGGVYVMLEPRKFA
SGSALGMLSPTGRCHAFDVAADGFVSGEGCVVLLLKRLPDAQRDGDRILAVIRGTAANQDGHTVNIATPS
QPAQVAAYRAALAAAGVDPATVGMVEAHGTGTPVGDPIEYASLAEVYGLDGPCALASVKTNFGHTQSAAG
ALGLMKAVLAVQHGVVPRNLHFNRLPDELAEIETNLFVPQETTPWPTNGHGAPRRAAVSSYGMSGTNVHA
IVEQAPETPQEAQDKAAATAPGIDGALIFPLSASSADALRQTAKRLADWVDAQGDDLVLSDLAYTLARRR
GHRPVRTAVLASTVAELIAALREVADGDTPYPAAVGQDDRGPVWVFSGQGSQWAAMGADLLANEPVFAAT
VAEIEPLIAAESGFSVTEAMTAPETVTGIDRVQPTIFAMQVALAATMKSYGVRPGAVIGHSLGESAAAVV
AGALSLEDGVKVICRRSKLMTRIAGAGAMASVELPAQQVLSELMARGINDVVVAVVASPQSTVIGGATQT
VRELVAAWEQRDVMAREVAVDVASHSPQVDPILDELTEALADLTPLTPEVPYYSATLFDPREEPYCDAYY
WVDNLRHTVRFAAAVQAALEDGYRVFTELSPHPLLTHAVDQTARSLDMPVAALAGMRREQPLPHGLRGLL
GDLYAAGAAVDFSVLYPSGRLVDAPLPAWTHRRLLLDRDQQDHRAAGGSTVAVHPLLGSHVRLPEEPERH
VWQADVGTAALPWLADHQIHNAAALPGAAYCEMALTAARTVLGEASEVRDVRFEQMLLLDDETPVSAVAT
VESPGVVDFAVETLQEGGRSRRASAVLHDVSDDEQPPAYDMAALLAAHPNRVDGDELRQLFDEHGVQYGP
AFTGLAAAHTAEEAGSTVLAEVALPGSIRSQQGAYGIHPALLDACFQSVAAHPDVQNAGNGGLLLPLGVR
RIRAYGPARNARYCYTTVTSVGGSGVEADLDVLDEHGTVLLAVRGLQMGTGASENGNRDRVLNERLLTIE
WQQRELPEVDHAEAGSWLLISTSDAADLAATELTDALKLHDAQCTTMSWPLHADHAAAAERLRAQLEAGG
FTGVVVLTGPQTGNPDQESAVRGGEYVQHVVRIARELPELVGQAPRLYVVTRNAQTVLADDCANLEQGGL
RGLLRVIGAEHPHLKTTHIDVDEQTGVEQVARQLLLGSDEDETAWRNDEWYTARLCPTPLRPEERHTTVV
DHQTDGMRLQIRTPGDLQTLEFVAFDRVPPGPGQIEVAVSASSINFADVLVAFGRYPTFDGHLPQLGTDF
AGVVTAVGPDVTDHKVGDHVGGMSPNGCWSTFVTCDARLATTLPEGLTDAQAAAVTTASATAWYGLHDLA
RIRAGDKVLIHSATGGVGQAAIAIARAAGAEIYATAGSPQRRELLRDMGIEHVYDSRSIEFAEQIRRDTD
GYGVDIVLNSVTGAAQLAGLKLLALGGRFVEIGKRDIYGDTKLGLFPFRRNLAFYGVDLGLMSVSHPAQV
RELLNTVYRLTAEGVLPMPQSTHYPLAEAATAIRVMGAAEHTGKLILDVPHTGRSSVVLPPEQAPVFRGD
GSYIITGGLGGLGLFLAEKMAAAGAGRIVLSSRSQPSQKALETIELIRAIGSDVVVECGDIAQPGTAERL
VAAATATGLPLRGVLHAAAVVEDATLANITDELLDRDWAPKVYGAWHLHEATANQPLDWFCSFSSAAALV
GSPGQGAYAAANSWLDAFTHWRRAQGLPATSIAWGAWAEIGRATAFAESTGAAIAPDEGAYAFEALLRHN
RAYTGYAPVIGSPWLTAFAQRSPFAEAFQSLGKGRSGTSKFLAELDELPQDEWPARLRRLVSEQVGLILR
RTVDPDRPLSEYGLDSLGALELRTRIEAETGIRINTTDITTVRGLADHLYDQLAP
>gnl|CDD|469092 NF041186, SenA, selenoneine synthase SenA. Selenoneine is the selenium analog of ergothioneine, a sulfur-containing derivative of a hercynine, which derives from histidine by trimethylation of its amino group. SenA, a homolog of ergothioneine biosynthesis protein EgtB, completes selenoneine biosynthesis in a pathway that also requires a SelD protein to prepare selenophosphate, EgtD to prepare hercynine, and the selenosugar-producing glycosyltransferase SenB (TIGR04348). SenA catalyzes selenium-carbon bond formation between hercynine and selenosugar to produce selenoneine. Other enzymes that create carbon-selenium bonds include SelA, involved in selenocysteine biosynthesis, SelU, involved in selenouridine biosynthesis, and SbtM, a radical SAM enzyme involved in post-translational modification of the RiPP precursor SbtA (see PMID:34730336)
TAGPAELAAALRDARARTLALFADLSDEQLRVPYLPIVNPPLWELGHIAWFQEWWILRNPERSDPFAARH
PSLLPDADALYDSSRVPHDTRWSLPLPSLAATLAYLAEVLERTLALLARAPDDDAALYFFRLALFHEDMH
GEAFTYMRQTLGYPAPPLAAAPAPAPAAGDLAVPGGTFRLGSDPGPGFAFDNEKWAHPVEVAPFEIDAAP
VTNAEFLAFVEAGGYRDPRLWSAAGWAWLAAQGLAAPRYWRRGADGAWQERRFGRWQPLDPDAPVVHVSA
HEAEAYCRWAGRRLPTEAEWEYAAAGAPGFPWGDSVWEWTASPFAPYPGFAPDPYRDYSAPWFGTRRVLR
GGSFATPARLRHPRYRNFFTPERRDIFAGFRTCA
>gnl|CDD|469093 NF041188, encap_f3, family 3 encapsulin nanocompartment shell protein. Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide
PGEEFARAVAADGPDAEVPFDATLTDAFPLFKTRPRYTVRHLLKVADVSGDPVRYWHETPPEEVAAAGTS
YDATPEAAFRFGLAEAGLTPITAWVQVPEGLLRDPEALASFIDYRLLVRLGTAENEALLHGSGDGAIPGL
LNMPGIRRLPARGDLGAGLLAACAEVEQTGGSCDGIVVNPRDYWRLVGSGALLADLAEAGVRISRTRMVA
PGQALVGDFRAAATLLDPGRSTIRLAEPPPGTFARPGDAVCAEIREGLAVHLPQHF
>gnl|CDD|469094 NF041190, encap_f4a, family 4A encapsulin nanocompartment shell protein. Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide
MRGDLIRVLSEIEEKANELKLDGYEPDVVLFGKEAYEFVKEQVNEEFGGEEEVLELSGLKVRILDELGGD
AVVIDSKALGLGPGAAKRIRVV
>gnl|CDD|469095 NF041191, encap_f4b, family 4B encapsulin nanocompartment shell protein. Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide
ELLELLETAINELKEEGLEPDILLVGPGFIEYAGEVLKDLGLKVYRIEELGYDAVIADSKYLGQLKKASR
RISIEPLLEEKEMWEEIKEL
>gnl|CDD|469096 NF041192, encap_f4c, family 4C encapsulin nanocompartment shell protein. Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide
MTILEHTPEDDELLDFIDDSVRQLQEAGHEARFILVGPLAYERLCKALAARFGRGAGRFETYNHLPVVVD
PFRDEEVCVVPAPRETAEGAQGYRI
>gnl|CDD|469097 NF041193, lipo_SP0191, SP0191 family lipoprotein
MKKILILLGALLLLLTGCGQKKESKASSKSTTKSSSASTLPVISNAEKNTVVTKTLVFPKDENGIQQTQT
ITYKGKQFLKLVIEQLTPLPEELKSAIAEVGLEEAQKALRESLEKDEKYQQAKSLAGFSIETKLTNENEL
KTTTTYDFQKLDVDKASKLEYFKNLGLKELLKLTPSQYIENLKANGAKEE
>gnl|CDD|469098 NF041194, LD_carboxy_LdcB, LD-carboxypeptidase LdcB/DacB
VSYNGSYYSVQGKYDEIIIVNKHYPLSKDYNPGENPTAKAALLQLIADMQAAGYPISDQYSGFRSYETQT
ELYQNYVNQDGKEAADRYSARPGYSEHQTGLAFDLIDTSGNLLEEPKASQWLLDHAADYGFIVRYLKGKE
ASTGYMPESWHLRYIGKEAKEIADSGLSLEEYYGFTGGDY
>gnl|CDD|469099 NF041195, ScbA_BarX_GamBu, ScbA/BarX family gamma-butyrolactone biosynthesis protein. Members of this family initiate the biosynthesis of gamma-butyrolactone autoregulators, a class of compound that include A-factor in (2-isocapryloyl-3R-hydroxymethyl-y-butyrolactone) in Streptomyces griseus. Through its receptor, a member of the TetR/AcrR family of transcriptional regulators, gamma-butyrolactones can control various processes such as antibiotic biosynthesis
VPRELVHRAAVAEVLLTDWRRLGEDRFSVTAQWPRDHAFFRPVDGGRHDPLLVAETIRQAGLLLAHAEYG
VPLGHHFLLRDLSYTVDPEALAVGGAPAPLELDLVCSDTRGRRGGRLAGLRLDVTLRRDGRLVATGSARF
TCVSPAVYRRLRGADRAAARGRALPLPPPVPPALVGRARPRDVVLAPTGRPGRWQLRVDTRHPVLFDHPV
DHVPGMVLLEAARQAAHAATGPAGFVVPTAVDTRFHRYVELDSPCWIEAEVLPPASGTRTLRVVVTQDGR
TVFTATLT
>gnl|CDD|469100 NF041196, ScbR_bind_reg, ScbR family autoregulator-binding transcription factor
QERAIRTRRAILEAAAEVFDERGYAAATISDILERAGVTKGALYFHFSSKEALARAVLEEQVARLREAVE
PQRAGGGSKLQELVDLTHVLARRLRTDPVVRAGVRLSIEQAAIGAGLPTPYREWIDLVAELLAEARAAGE
LLPGVDPEEAARLLVGAFTGVQMLSDVLSGRADLPERLAELWRLLLPGIAV
>gnl|CDD|469101 NF041197, CxxC_Se_CxxC, dual CXXC motif small (seleno)protein. Members of this family have a pair of CxxC motifs. An additional Cys in the 16 amino region separating the two motifs occasionally is replaced by selenocysteine. This family was reported as OS_HP3 by Zhang et al. in PMID:17626042
ARAAQTTVACPKCGGELTIERSCHEVYLRCPSCGKEYDLAEYAAEMDDDFEEFMENVYCDRI
>gnl|CDD|469102 NF041198, UshA_like_PCGU, UshA-like (seleno)protein. Members of this family are distantly related to hydrolases such as UshA and CpdB of Escherichia coli. Most members are selenoproteins with a PCGU motif
VLLILLLLLTVSSPASPAAPAAEFTIFYSNDVRGETEPCGUKSNQLGGLSKKAYQIKQIRKEGKKPILFL
DAGALLFKQERLPPGLLAQARITADGIIEAYNLMGYDAVGVGEQDLAAGLDFLKELQKQSKFPWLSANLV
DKKTGKPIFKPYIIKKIGGLKIGIIGLTGPQGPPSLQEDEAGITILPWQEVLPDLLKELRRQCDLIILLS
SLPPSENKEIAEEFPGIHLIIQSGGSSANLNPQLVNNTLITQTGRQGKYLGRLDISWNKSKRWWRESALS
ELLEKKQELDRLNWQILRMESKGDPEEEYKDKPKRLESYRNLVSKRKELRDEIAALEKKKETSKENPSTY
SNQFIALDSSLPDDPEVRKIVEATKQKVNELGRKKAEKLRQQGSAAITSIAIDSHYAGWQACKSCHAEQT
AFWQKTRHAKAYQTLVAKNQQFNLDCLPCHVTGYYKDGDEATLLSLPEDLRGVGCEACHGPGRGHAADPK
GGSNMKRKPDEAVCLRCHTPEHDDNFNYL
>gnl|CDD|469103 NF041199, trx7_PDZ_seleno, Trx7/PDZ domain-containing (seleno)protein. Members of this family, most of which are selenoproteins, have an average length of about 420 amino acids, with an N-terminal signal peptide and then a PF13899-type thioredoxin-like domain (Trx7), followed by a more C-terminal PDZ domain. The selenocysteine residue occurs in a CxxU or UxxU motif
IWWLNDYAAALAEAKKTGKPIFVVFRCEPUEDCRKFDGQVVRLDKSILEKLLDQFVCVRITRMNGVDLNL
FQFDYDLTWMAFFLNADEQIYGRYGGRDAASADSYLSLASLELAMERVLELHKHYQAGKLERAGKRGAPK
FPKDIPPLPAATGRKGKSCIHCHQVGEAQRRELEKEGKLDKEKDLWVYPLPENIGITLDVDKGNVVVVVE
PGSPAAKAGLKPGDVIVSLNGQPVLSFADLQWALHKAPRKGGTLELTVERGGETVELTLELPDGWRRTDI
SWRPSLHWVLPRLPFWGRPLSAAEKKKLGLPADGLALRVTYVWGPAVHQAAKAAGLRKGDIIVAVDGKTD
DPTRQLQFYIYLRLNYKAGDTVTLTVLRDGKRLELPLKL
>gnl|CDD|469104 NF041200, mob_BfmA_Nterm, BfmA/BtgA family mobilization N-terminal domain. BfmA was identified as a mobilization protein for a pathogenicity island that includes fragilysin (Bacteroides fragilis toxin, or BFT) and the fragilysin family metalloproteinase MP-II. BfmA has partner proteins BfmB (a member of the PF18976) and BfmC. The distantly related protein BtgA, also found in Bacteroides fragilis, is a mobilization factor for antibiotic resistance factors
FKTIRIKKSTAKRFDKFSKKVGKSYSETLEAMLDFFEVTGISPTDNLGPPITTAIKKRIDRVIAIIKNIE
KDQLKPTKEML
>gnl|CDD|469105 NF041201, recomb_XisF, fdxN element excision recombinase XisF
IVGYARVSTREQADDGHALEQQIARLKKAGASEIFFDIESGRSDKRKGFNQLLKLVKSGKVTEIIITRID
RLTRSVVTIYKAIEVLQKKGVKLVILDAPLDDLSSPGGWFTINQLAALAEFESRLLSERVRHGLEYFREQ
KKAHPKPPFGYVRIDDKYAPDCLLYDKSELTVWEIAREIIEIFLENGSLRGTCRYLNEKYGLKRKVYKKQ
RSLPWSPTGLRRWLTNPVLRGHTPYNVKTKNKKPEEWEIHWNTHEALISEEEYQQIKRILRENRKNRGSG
RRKKSTREQNPLSGLIKCAECGGKMTRKGSKVKKKGTYRLYCQCAYYYGGGFCSNKKSIRLSELEEAVIK
ALVKKAEELANIANLEETPTQEESPELLELKQQLKALEQLPDSNPDIEDAIAKLRLQIENLEQQTENTDS
ISEERVELLIAFSSNADFWESLSDEDKRKIYRELVERVVVDNG
>gnl|CDD|469106 NF041202, StoA_CxxC, endospore biogenesis thiol-disulfide oxidoreductase StoA. StoA (originally YkvV in Bacillus subtilis) is a paralog of ResA. It is involved in proper formation of the peptidoglycan cortex of the endospore, while ResA is involved in cytochrome c maturation. Both are membrane-bound and outside of the cytoplasm. This HMM separates StoA from the much larger set of ResA proteins
MLRKRLALPACILLLFLILWLPEAQAEAKKAAPAVFLMKTIEGERISIPAKGQKTILHFWTSWCPPCKEE
LPQFQSFYEENQSDVQLVTVNLLNAEKNKQAVKRFIKANKLTFPIVLDSKGEMMKKYNIMTIPTTFLLNE
KGELEKSIVGPMTAEQLKEWAEK
>gnl|CDD|469107 NF041203, rhodanese_LYCAU, rhodanese-related (seleno)protein. Most members of this family of rhodanese-related putative sulfurtransferases are selenoproteins with one or two selenocysteines in a CxU or UxU motif
VLLLLALAAAVATAAAAADVPRMTKEELKAMLGSPDLVILDVRAGRDWSSSEFKIKGAVREDPGDVDSWA
AKYPKDKTLVLYCAUPNEATSARVAQKLMDKGYTKVYALKGGWREWFRAKYPVEPK
>gnl|CDD|469108 NF041204, VdcC, non-oxidative hydroxyarylic acid decarboxylases subunit C
YNDLRSFLDLLEEEGQLLRITDEVDPEPDISAAARAAGNLGDGGPALLFDNIKGYPGARVALNVHGSWAN
HALMLGLPKNTPVKEQFFEFARRWDKFPVPPERVDQAPCQENTITEDINLFDLLPLFRLNEGDGGFYIDK
ACVVSRDPEDPDNFGKQNVGIYRLQVKGKDRLGIQPVPFHDIAVHLRKAEERGEPLPIAIAIGNDPVITI
MASTPLGYDQSEYEMAGALRGAPYPITKAPTTGLDVPAGSEVVIEGEILPRVREIEGPFGEFPGSYSGGR
KMPVIKITRVTHRTNPIFESLYLGMPWTEIDYLIGLNTSVPLYQQLKAAFPEVQAVNAMYTHGLVAIIST
KKRYGGFAKAVAMRALSTPHGLGYLKIVIVVDEDVDPFNLPQVMWALSTRVRPAKDVIVIPNMSVLPLDP
SSEPPGITHKLIIDATTPVAPDPRGHYTQLVDDPPETDKWEKKLRKL
>gnl|CDD|469109 NF041205, VdcD, non-oxidative hydroxyarylic acid decarboxylases subunit D
CPRCASEKIEVLATSPVPGVWEVYQCPRCLYTWRSTEPARRTDPEAYPEAFKLTPEDIANAPEVPAIPPL
>gnl|CDD|469110 NF041206, VdcB, non-oxidative hydroxyarylic acid decarboxylases subunit B
RLIVGVTGATGAILGVRLLQALKEIPDVETHLVLSRWARKTIELETDYTVEEVEALADVVYSPKDQAAPI
SSGSFRTDGMIIAPCSMKTLAGIRNGYADNLIGRAADVMLKERRKLVLVPRETPLSLIHLENMLALSRMG
VVIVPPMPAFYNHPQTIDDIIDHIVGRVLDQFGLDHPDAKRWAG
>gnl|CDD|469111 NF041207, tRNA_bind_PBP11, tRNA-binding protein Pbp11
FLRRLFGRKGKKEEEEEIVSRKPVGKFRVEKVLKVLGRDVLIGEVLEGIIYPGYKVKGKKVAPIMKIERE
RKKVEFAIPGDRVALILEGSIKAEKGDVLEVYQS
>gnl|CDD|469112 NF041208, celldiv_DipM, cell division endopeptidase DipM
MGELNMRFPILQHTSERLLRNAAIVLIAGFGAGCSADTMRFTDGLYTGSTSNQRVVQQPAGNVYASAPVA
AAPPVSSGTVQRNSLPPVSSAPVAAASTQMQNQVDQAQDAAAERVNDTVNAAETQVASAATAAHNAANNA
KENVLGQLPATANGVPLPMDNNAAASPPAPAVDGKPPQTAAAGGAYMVKSGDSLFSIAQKHNVPVDELKA
ANGLTSGAIRVGQSLAIPSAAGAPTQVAAATPQPAKPAKAANVKPASPAPGAAAEVKPYTPPQASNKVIE
DAEKDQAAAPSSTGISQMRWPVRGRILASFGQRDGTSVNDGIDIMVPEGTPVKAAENGVVIYAGDGLKEF
GQTVLIRHDNGLVTVYGHNSQILVQRGQKVRRGEDIAKSGMSGNAKSPKLHFEVRKNSSPVNPAKYLES
>gnl|CDD|469113 NF041209, resp_regPieR, two component system response regulator PieR
MKLLMIEDNESVTQMMELFFLKEQIDATFVHDGKMGYERFLKEDFDLLIIDLMLPSMDGMTICRKVREVS
DVPIIILTAKESESDQVLGLDMGADDYVTKPFSPLALIARIKAVSRRKNSASDDTENNEDTHILETTYFK
ISKRTREIFYQDEPLEALTPKEFDLLYFLMEHPRQVFSREQLLERVWGYQFYGDERTVDVHIKRLRKKIA
TEEHLFLHTIWGVGYKFDETE
>gnl|CDD|469114 NF041210, his_kin_PieS, two component system sensor histidine kinase PieS
MKFKYQYQLFLTQFIILLIACLMIGLLISHFLKDYFFESQVNDLTKYGVTISRDIKYMSDEDQTVPVLNT
YQRILDVKNIHYTILNNNNQIIYPNNNRPLPPDFKISDADMKKLEKGETVSIKVDNRFNQEMSVVYVPIL
NGDEFLGSIILNSPISGTEKVIGTINQYMFYTILLSITIALILSAILSKLQVNRINKLRKATKRVIRGNY
ETRLKENNFDEIGALAHDFNKMTETLAESKEEIERQEKRRRQFIADVSHEMRTPLTTISGLTEGLVNDII
PKSETDRCIALIDTEAKRLTKLVNENLDYERIRSNKIQLYKTRFGVHAFLDLIKEQLEPLASEKGNQIIV
DAPLDLEVYADYDRLTQIVINIVKNSIQFTENGTITLTGRQDYKETILTITDTGIGMDTGELEQIWERFY
KADMSRTSTAFGESGIGLSIVKQLVEYHDGSIEVESEPNKGTTFTIRLPFFSDN
>gnl|CDD|469115 NF041211, CxxS_UxF_star, SbtA. Members of this family have a HPDCxxS motif, instead of xxxCxxC or xxxUxxT as found in some homologs. Members tend to be selenoproteins, with a novel C-terminal UxF-COOH motif
IVIYTHPDCSYSDALKDDLRRQGIDYEEIDLSKNPEAWPELERLTGGERITPVIVEGDRVTIGFHGVGUS
F
>gnl|CDD|469116 NF041212, Uxx_star, Uxx-star family glutaredoxin-like (seleno)protein. A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature
VVIYTKPGCPYCAAAKEDLARRGIPFEEIDVSKDPEALEEMLRLTGGERIVPVIVEGGEVTVGFGGGUGF
>gnl|CDD|469117 NF041213, plasmid_TraA, plasmid transfer protein TraA
KFATNTGAAANGFVGGMGASFAPGFNVNVNNNTTGGGGGGGGGRGGHSESLLPDPEFTSPADVRNYCNAL
RAAAVTLSIEVAMAAEILKAVLAEVPDPEGRPFGSRMRARKVARKLQKAADALRDAAKNAAATYAAFQQE
YEEEINRVRHRARRPQARRFDWAQ
>gnl|CDD|469118 NF041214, plasmid_TraB, plasmid transfer protein TraB
YLLSRAKPYLPPWLGVAGTGPAGAGAHWAWGDSPWAGVGLTLASVALTAATWWAGKATSQQRRLHSAITV
AAGSAWLTAATLAGPLAGPLLDLYLMGGAALALSWNIRQALRRNPDGDGESADKGLLEKVGLAKAQIGAA
KVEPNKVTAPLQLPAGEQTNDDVQKALDRIASALDLPKGAVRYQPDPDSASRGELVIVPEDMLKEPVPWP
GPSNPGGSIADPLVIGRYEDGAPLVLWLPGDPETGRNATHLLIAGMTGSGKSDGALNALTEILTRRDVIV
WVSDPSKGEQTFGPLLPALDWAVEGGAGTEAMVEALPAVIPARTRWLGAHGYRQWVPEAAEQQTDPCPGM
PYLVAWFEEAAKTLRDLGDFTGIAQEARSAGISLVVSLQRPSYDQMSTDTRAQLGSVWCFGVKDPRDAGF
ALPDEVLDAGARPEAWKNRRPGYCYLVAPGIDEDRYATPGRTFRFTDDAELLAAWAVRNGARADPVTAGA
AAALAGPAYTGRTTTAPGADAPSVAAPLEGEEDADMDAGLLVDPEDADIDPDAELPPVPDGDDAPLFGQP
TGRKPSPEEARALLAAALAEFEAEGRMVVGPKDFPDWCDRFGRSRSWVSGELKELADEGRLAETGQTGRY
RIVPALAAA
>gnl|CDD|469119 NF041216, CU044_2847_fam, CU044_2847 family protein
VLVEVEEVGGGDEEERRDVGFGDRAAARTFEEALDTIRPVARAVLDALKELAAKPDEVEVEFGVKLGGEA
GAVIAKGTAEANLEVTLEW
>gnl|CDD|469120 NF041217, BagE_FevW, bagremycin/ferroverdin synthetase BagE/FevW
LPAIGDWKTFDGLRALQRERVGPTLRHALNSPFYAGRLEAGQALSSVGLTGKSDLRDSYPFGMLGVPRER
LATYHESSGSTGNPTPAYFTEAEWTDLADRFVRKTVPIGPADTMLVRIPYGLVLAGHMAHWAAMRSGATV
VPGDCRSLAVPYSRVVRLLRDLEVTLTWSTPSESLLWVAAAKAAGYPADSFAALRALYVAGEPMSSARRR
RIEEIWGAPVIEEYGCTEVGPLASDCPHGRMHFWADRVLPEIYDPQTGAITAEGTGQLVITPLYREAMPL
LRYNLEDLVELRYEDCPCGWKLPTVRVLGRLGQGYTVGGRRLGQVQVEELVYRLPAAYGVLFWRARAEPD
RLVVQIEVPGPGGGEAAALLAASVEAELGVRCEVGAVPEGTLVPAALLAQRLDAMKPRKLFGPDEDWDQA
VVRG
>gnl|CDD|469121 NF041218, BagM_FevK, bagremycin/ferroverdin biosynthesis UbiX family decarboxylase BagM/FevK
MRLIVGMTGATGAVLGVRLLTELRGNPRVETHLVLSRWARATVELETGLSAREVAALADVTYSPDDQGAA
ISSGSFRADGMVIVPCSMKTLAGIRAGYAEGLVGRAADVTLKERRRMVLVPRETPLNEIHLENMLALARM
GVSIVPPMPAFYNRPESVDDIVDHIVTRVLDQFGIEVAGARRWEGFPRPAAGRPGPAADVPAVRHNGTKQ
RSARS
>gnl|CDD|469122 NF041219, BagN_FevL, bagremycin/ferroverdin biosynthesis UbiD family decarboxylase BagN/FevL
VTRFKDLRGYLDALEALGDLRRVRRTVSADLEAAAITRLSCERQSPAPLFENVEGVAPGFRLLGAPAALS
AAPGKPLARVALSVGLPAETTAAELVEHLARARHAAPVPPRLVGREDAPCKQNVLLGDDATLDRFPVPRV
HEFDGGRYPNTWGIIVARTPDGRWTNWSIARIMLIDGKHMTGLVIPAQHIGMIWQEWVERGEPMPYALVQ
GGDPAIPFVGGIPLPPGVDEAGYIGALYGEPVEVVPCETVDLEVPASAEIVIEGHLSVGRDAREGPFGEF
AGYASTETSMQPVYTVEAITHRDDPIWPLVAEGRPVDEFHTVTGVGQAAEVLAELRAAGLPVTTAWSPLR
AAAHWMVVTVPQDWRERLPGVDSAEFTHRIGEVLSESHSGRATAATFVLDDDIDPADDTDLLWALATRIH
PLDRAEAWYGFVHPLLNCYTHEERAAQSGPIVFHDGLLPAPGEGRLPHSSFAQAYPERIRRRVLDHWDD
>gnl|CDD|469123 NF041220, BagH_FevF, bagremycin/ferroverdin biosynthesis o-aminophenol oxidase BagH/FevF
MVHVRKNHLDMTAEEKRRFVRALRRVKELGIYDELVRIHIRINSGDYLDKDGGKRWGHMSPGLFPWHRQY
LLILERALQRVDPTVTIPYWDWTKDQSEDSPLWGDDFMGGNGRPGDRQVMTGPFARCNGWKLNVSVVPVG
DEHPAFNGHYTADDRDYLVRDFGTVNPNLPTVKELADTLALTTYDTPPYNYTSGYGSETQSLRNHLEGYA
KFPWEANLGKLHGAGHTWVGGHMLYIGSPNDPIFFMHHCFIDKLWSVWQQAHPDVPHYLPVEEHPDVPSL
HTKLAPWYTMSPADLLDHTKFYRYA
>gnl|CDD|469124 NF041221, BagZ_FevE, bagremycin/ferroverdin biosynthesis copper chaperon BagZ/FevE
MKRRDVMKGIAGAAAVAAVPAAVIHAGNTWAAAHDDAAVDQAAEEPGDLYTETYKGRTITVSKADGTVHI
DGRELHLMKLGEGAYLSAMCHYRIEPTPLAAGRQAVDELRGANLLPSGTHHA
>gnl|CDD|469125 NF041222, BagA_FevW, bagremycin/ferroverdin biosynthesis tyrosine ammonia-lyase BagA/FevW
LTIGQVMAAASREGSEFSVSEDALKAMDASRNLKLEILRTGKPIYGVTTGFGDSVNRQISPEKTARLQSE
LIRYHLNGTGPLASDEVVRATLLIRANCLARGNSGVSLPVVERLLDFLRHDVLPTIPERGSVGASGDLVP
LCYLAYALTGEGKVRHGGEDRPAADVLAELGLEPVQLEAKDGLALINGTSFSAAFAALNTEAAAELAEVA
DICTALASEGMLGNRGHYAPFIHDEKPHDGQRASAARIHELLDGSALAMTHDQVVDLNDPLDGRHYQKLT
RSIQDRYSLRCAPHVTGVLRDMLDWVRTWLTVEINSSSDNPLFDPSTGAVYSGGNFYGGHVVTAMDALKT
AVAGIADLLDRQLALLVDEKFNNGLTPNLIARVADDDTEAGLQHGFKGMQIACSALTAEALKNAGPVSTF
SRSTEAHNQDKVSMAPIAARDARTIIELTREVAAIHLIAACQAVELRGVAEMSPRTRAVHARVREVVPFA
AKDRQMDGDIAAVVGLITSGALTEAAR
>gnl|CDD|469126 NF041223, BagB_FevI, bagremycin/ferroverdin biosynthesis DhnA-type aldolase BagB/FevI
MISNGAFGRRLRLRRLYRNDSERLLIVPLDHSVSQGPITGGEGLDALVGRLATNRVDAIVLHKGSLRHVD
PAWFSSTSLIVHLSASTVHAPDPDAKYLVAGVEESLRLGADAVSVHVNLGSDGEQRQIADLAAVADACDR
WNVPLLAMMYPRGPRISDPRDPALVAHAVTLAADLGADLVKAPYVGSVAEMKEITSCAPVPVITVGGPRN
DDEGQVLAQVAEALSAGVAGVAMGRNVFEAPDPGVMAAKLADLIHSE
>gnl|CDD|469127 NF041224, BagC_FevH, bagremycin/ferroverdin biosynthesis 3,4-AHBA synthase BagC/FevH
MKLSWLDIRNLDEAKAAIVQEALHHRLDAIVAADPADLAGLPPTVGKVLFPRGKPLPDDFGEATVVIVDP
AFHKITPAELALAHPELEFGRFVEIIDAKTLEDACEAARTEQWSLLLFRDPTKIPLEIVIAASAASPGSL
ITVAADVEEAEIIFGVLEHGSDGVMMAPRKVGDAAALKAVVEAETPDLGLTELEVVSTEHVGMGERACVD
TCTYFRKDEGILVGSHSKGMILCVSETHPLPYMPTRPFRVNAGAIHSYTLAKDGRTNYLSELKAGSKIIA
ADIEGRTRLVTVGRVKIETRPLISVNAVAADGREANLILQDDWHVRVLGPGGAVLNSTELKPGDKVLGFL
PTEDRHVGYPLDEFCLES
>gnl|CDD|469128 NF041225, Cas_III-E_gRAMP, type III-E CRISPR-associated gRAMP effector Cas7-11. The giant RAMP (gRAMP) effector of type III-E CRISPR/Cas systems, named Cas7-11 because of its multiple domains, works together with the caspase-like TPR-CHAT protease (Csx29) in a subset of type III-E systems. The complex of the Cas7-11 and the TPR-CHAT subunits is called craspase (CRISPR-guided caspase)
IHLTFLEPYRMAEWFEPEDRKKNNRDFLRGQSFARWHKSKKGNKGRPYITGTLLRSAVIRAAEELLSLNN
GKWGGVACCPGKFNTEAFRKKKPKFLRRRPTLQWTTEGKKICDKEEGNACPFCLLLGRFGKAGKEEKKNN
DYDVHFSNLNLPGKPKKSWPEDIASERVLNRVDFLTGKAHDFFRIWEVDHEQWGDFTGEITLADDVSSKA
RKLLLASLGFVDKLCGALCRIEVDGLKLAEKTSKDKPQCNSGDSTLEVSEEPFFNELEKLAKVIVEAFPR
NDKLEKLRLLADAIRELRREGPDIIETLPKGHEGKLDHHLWDSKDVNGVTLRNILEEIARQCKSKNQWRT
FCEKLGEALYLEYKKVTGGLAPRRRILGETEYYPKKTIPEKSISRFILGPTKEWIIVGTLKAETPFFFGV
EQELEENEHTSLKILLDKDGRYRIPRSALRGILRRDLRTAFDSGCNVELGGDRPCDCKVCRIMRRITVMD
SRSETKEPPEIRHRIRLNPFTGTVAEGALFDMEVGPEGVVFPFVLRYRGEKTLPGALRSVLRWWQEGKAF
LGGDASTGKGRFALENIKIFRWDLSDETARNDYIKTRGLRGIEKEKLDKEKIPDDKTGPWSKGLSDLSKE
SLRKGLSDYLEYLGPPWTKVAYKISINSPLLTADPISALTEPENDDVIAFKKYKTEDGEVKPVPALKGES
FRGIVRTAVGRRGVPLIKDDHEDCSCTLCRIFGNEHEAGKIRFEDLEFVGEPEPKKIDHVAIDRFTGGAV
DKKKFDDRPLVGSPEKPLKLKGRFWIRRDFSGDEKESIKTALADIRDGLYPIGGKGGIGYGWVADLEIDD
DAPKLSELMKEASDIQDAPLNYKKGSAPLTQRLKKGAIYYPHYFLEPGKKVEREKVPPGHEEFHEGRLLS
GKITCTLETVTPLIIPDTENEQEKDEYHKSYDFFRLNNEIMIPGSEIRGMISSVYEALTNSCFRIFDEKK
RLSWRMSPEHKDYLPDFIPDNGRVIQGGKRIQKESREYRYPFYDRTDTEKLEQEGYERLEAEKIILKNSG
RIKLKDKIKRQELYKLFALKDKIYKGQKPFTFDLKKKAEKIGRWIKRILKFAESRGGELPYLNHATPTDK
KLLSLAANNRNIKQQDFKVQYRIIKLKEGKKPDFRSLVKSFEKSFQELCKGGPRGRELRGGYLKISGPNK
VNKSNHSNGDVSDNFDDTLDFVFLNIGLNALEKRKSRKREYPRPALTFTDDGKEYTMTKRCERVFEDSKA
NKIEPVPRKVREKYKIILRDYEKNAKHIDTPEAFQTRLPKYGELNDGDLVYFKPDDSDKTVTDIIPVRIS
RKVDDRPLGKRLDKDLRPCVGECLEDGDLSKLIADPVEKRLLGRHPDGLCPACRLFGTTSYKGRVRFGFA
SLKNKPKWEDPREPNQGKYVTLPLLERPRPTWSMPDDESEVPGRKFYVHHNGWREVKKGDHPKNGRATVQ
TENNRTVEALDKGNKFSFEVAFENLREWELGLLLYSLELEPGMAHKLGMGKPMGFGSVKIRVESLHTRKV
NGQWRNEKSSTDLPWVTKGKLKLSEWFKIEDLRKLLWLPEEDDIKLVYPKGLKKKEGEGGDSGYEELADY
DPLPELVRQKGLTTPWEPW
>gnl|CDD|469129 NF041226, BagK_FevA1, bagremycin/ferroverdin biosynthesis FAD-dependent oxygenase BagK/FevA1
MYRSATVQRLAGRLSGPVLGPGDDGYAAEVAGFNRVVQHRPAIVVGVRDATEVRKAVAFAAETGLPTAVQ
ATGHGPSRAAEGTGLLINTRRMTGVTIDPVARVARAEAGAQWHQVVDAAAAHGLAPLNGSSPLVGVVGYT
LGGGLALLSRAYGFAADHVTAVDVVTPDGRPRTATAQRNTDLFWALRGGKGNFGVVTAIEFGLVPVTRFY
GGGLFFPGDTAAEVLHAWRSWTESVPEETASSLALLRMPDLEPIPEFLRGRLVVHVRVAHLGPGDEGERL
VKPLRAIAPTLVDTLGEMPYTRFADIHNDPAFPIPYDERSVMLRELGPDAADDLLALAGPGSDCTDLVVE
LRHLGGALGRPPAVPSAVDHRDAAYCLSTLGPPGGRPDHVVDGMAHRGTGRSYLNFLAGPGTAQLAERGY
GPATYARLGEIKARYDPENLFRFNHNIPPRAKS
>gnl|CDD|469130 NF041227, BagG_FevA2, bagremycin/ferroverdin biosynthesis FAD-dependent oxygenase BagG/FevA2
MTTGKSIARPAAAELSERLRGRVLRPGDDDFALELDGFNQITEHDPDLIAVVAGAADVREAVAFAAARGL
PVAVQATGHGPSTAADGGLLISTRRLRGVSIDPAARTARVEGGTQWFEVIQAAAEHGLAPLSGSSPLTGV
IGYTLGGGLGLMARRYGYAADLVTAVEIVTADGQSHRATADRDTDLFWALRGGKGNFGVVTALEFGLVPV
SRLYGGGLFFAGEAAAEVLHAWREWTASVPEELTSSLALLRLPDIEAIPPFLRGRLTVHIRIAYLGSAED
GDRLVAPLRAAGPLVVDTLAEMPYTRCGEIHNDPTEPIPYSERSMMLRELDEAAVDALLALAGPGADCID
LVVELRQLGGAVGRPPEVPNAVDHRDAAFALSTLSLPDDRPPLVVDGMAPWGTGRRYLNFLASPDTAHLA
ESGYEPATFARLADIKARVDPDNLFRFNHNIPPRP
>gnl|CDD|469131 NF041228, BagJ_FevB, bagremycin/ferroverdin transporter BagJ/FevB
MTTNSAVQAPPQTAPGAGLTGLRLGALFGPVIFGVTAAGVALPDVAMAMEVRPAVAGWVLTAHALALGVG
TAFFGRLSEKWGVRNTLLVGSLFLAVGAVLCLVAPNFGTLIAGRFVQAAGSGAITSSALTLASAAAPAQR
TKILAIFGASMALFSSTATLMGGMVTDWLDWRLTLVLPALSLLVVPFCLKLAATRPGYGKAVDLLGGTLL
GTGATSLLLLIQASSLDLDTPLVIALAALLVVSVAGLVVHIGRRPDGFVPRWLATDRTFLVAAVVGLGGY
AGLFAAMYAVPQILTVQYGWGVFKIGAWLLPGAVVGAVCARVASKLTLGKGGSLLLAGAAVSCAVFLGIV
GLVEGGIVVMLIGTSMGMATFAATQVLTTAVLSSRLEPAQRGGAMGVLNLLFFVGGGIGSAAAGALSEHM
DLTSALAVVAALPLLAGLIALLLPPARAQQEA
>gnl|CDD|469132 NF041229, BagF_FevY, phospho-2-dehydro-3-deoxyheptonate aldolase BagF/FevY
MSPQATASDLAAVVARVESAGGEAFVSRGTSRTVVGLVGDLEQFGTLNLGALRGVAEVVRISVPYKLISR
QSHPDRSVVRVGGASIGPGTPTLIAGPCAVETPEQTLRAALMARAAGATVLRGGAFKPRTSPYAFQGLGE
AGLKILADVRAETGLPIVTEVVDAHDVELVASYADMLQIGTRNAQNFALLQAVGDVGKPVMLKRGMSGTI
EEWLMAAEYVAQRGNLDIVLCERGIRTFETATRNTLDIAAVPIVQRLSHLPVIVDPSHSGGRRDLVLPLT
RAALAVGADGVIVDVHPDPRTALCDGPQALVHEDLEELGAVMRGNSVRRHRILDGFVPLS
>gnl|CDD|469133 NF041230, BagL_FevM, MarR family transcriptional regulator BagL/FevM
MTNTSPRPRPQLEEALPHQLRRAGQAWTALWQQRLPDLTSPQFAVLLVLDDHGSLDQSALGALAAVDRST
LTVLLDRLEARGLVTKEMDPANRRRRIVALTEAGRRRLAEAVEEAGRLHARVEELLGERRLRDLVGMLRV
LGDMP
>gnl|CDD|469134 NF041231, BagI_FevR, AfsR/SARP family transcriptional regulator BagI/FevR
VTNGDERIEISGIRRQKLLAALLLQPNQVVSLDRLVDAIWDDEPPASAHGQVRICVSGLRRLLRGRERDS
VIETHPSCYRIRVRDDDALDLFTFEKLVAQGRAMVRDDRLERAEGLLKSALALWRGPVAAGLDSRALASL
VVKLNEDRLTVSEEYFDVALKLGRHQQIIGDLTGFVAENPFRERACAQLMLALYHSGRQADALETFRAVR
RRFSEDLGIEPAQDLHVLHQSILVGRLSSVAPPPRDVPAPPPPRSPGRRGRPAGVALLPRTSPNAVTADP
LEQLRLENDLLRVERDGLRQILSLWLNSNEEDPGA
>gnl|CDD|469135 NF041232, BagY_FevT, LuxR family transcriptional regulator BagY/FevT
PTVIGRDELISRAGRADSPHTLFSTLATQLRRAVPYDAAVWRATDPETGMITSPILAENIEDHSCAVYWQ
YELFTEKINLFRDLALAPVPVASLWESTGGEPERSSLYRGFLAPRGVHDELRAVLRVDGRPHGYVSLFRE
KGRAEFSTGERRFIEDLGTPIARRLRSYAKQRPEPSTGGLTGTGLLLFDADGALISANDDARRYLEEMPE
GPTSLTALGIRVPLWVHGTAMRARAIAEERGGDTARIRMRSRTGRWLVCHASCLREADGRLGVSAVIIER
APVSDVTPLIVQAYELSERELEVTQRVARGLSTGGISEELHLSPHTVRDHIKAIFEKLGVSSRGELVGKL
FTEYYEPLPPGSTGRR
>gnl|CDD|469136 NF041234, CAS_csx30, type III-E CRISPR-associated protein Csx30. Csx30, encoded in type III-E CRISPR systems, was identified as the proteolytic target of craspase (CRISPR-guided caspase), which is a complex of the gRAMP (giant RAMP) protein Cas7-11 and the TPR-CHAT protein Csx29
IDILLEWGKTHLLSPDFPEYLSELEEEWKSLIDDDLGDELESGIEELIKKVESALALLSGPELITLTDDD
ELWHEAEEAFLTLDNLVYLMEALERLLFPQDKELAEDLLEKLDEILQRITDWLEDGEFSPLRLIPLNEWR
REILEQIPEDYRYLFPWYELYSEVDEDILEILAENFHLFLKGDKAAEELPEELLGELLAELKRDKVLFKY
IEKEARLSKSLVKAVSKHWSLRLLRLAREANLDYPLPEDVEEKGLAAVARHLISDPPRSEADRIELLFLA
AFCGPDLDDKQRLSLLSKVEEILKRIDISGIPSDSSVLKTLKLWAEGRLSDEELAQISFDTWEEQLERAA
QQMRTREPDEDPLWRAVENLLKQPIPKKLASEPEPFFFKDIEKSWIEIFPRWIDRFVATFLLWVLAQACL
QPEQAPDDEEVKIYLKLPPNREGEYPIILEDGSVKSLLDDAFEDYKKLWNYLAGKTETLYWGGILIKEDG
QWEEIEPKPIERDILEEITGDVPYRVAIIGISTDKEQLEEFIELLKGSREPEPVREKFLNVKVLIIWLIY
>gnl|CDD|469137 NF041235, CAS_csx31, type III-E CRISPR-associated protein Csx31
PGDIFPEAKVLSVSRRDGNRWILKTVDYRGEQLILRDQYLPKGVDVKRGEIVKNLVVISYEKKFKLAVAL
RNYCETLLGKFYYNDYEVRPKKRNWKVWSRRWKESACKFFKVNFKLEKIGRNIDQPGKSWFIVKGPDWMM
PVHLHKYLDYLNGEPLFYPASLDTNDNRGILRSVYKTDGFENNDFPVCFKGKITNEKGNSKRVRIYLHGF
LEPRKWHYGVWKHMLALPKGREEGEKLWWELYSGLELSESVENKFKDCKENKKQSCDERHCLENSLFKKV
HKAIKDLCKKYLEQAVTFFESNTTNKVVLSNDGHSSQKVEAKFLDVDCFNIIENITEHAKKYPVLILRGV
CYNWDSSEDEPVIHLNIVTMYLK
>gnl|CDD|469138 NF041236, CAS_III-E_sigma, type III-E CRISPR-associated RpoE-like sigma factor
HECLESRGRGPECKDCPIFKRGFCEIFVKILRKKARNLASSYTGIPPEDREDILSETVEAVQRGIGKFEG
RRGAKFSTWVWRIFRNKRVDYFRKKYKKKEYSLPLEGAEDDQEEEPEDDIEEMFAAEDIIECLKKKVDDG
ETGCIRLLLDLYRWFKEGLTQKEMAESYGLKPNTLNQRISRCRKRIKQLLEE
>gnl|CDD|469139 NF041237, CAS_csx29_CRASP, type III-E CRISPR-associated TPR-CHAT protein Csx29. Csx29, the protease subunit of the craspase complex, is a TPR-CHAP family protein of type III-E CRISPR/Cas systems. Craspase is guided by crRNA, but cleaves protein, not nucleotide, and therefore is highly interesting for potential technological applications
RREWLEDAIRILKNLEKEKKKKESPEVLVLLARAYLHRGLLILPKGFTVPAKKKEALKKALRLAEKAIDN
KEKNLEALRLKAQALLELERINKDEDSEKTLKELLEEAVQNGCNDFIAELEDIEIFLRYSERDKLLDKIE
YLLQIIGSWLSNNDELLLKAKLAAILNKANDDVDKYLNKAIEKAPKAIFSDPVWDDLVDFLKKLKKKGSD
DWKELALAAWEVCRKKEKEITSGLHLRWYWSRQRDLYDLAFLAADDLEDKAEIADSLKSRPALRWQALEE
LKAKEIEGIEEYYEMEAQARDGRYLKKSEDLKRKKKPKPKAKPKPVPFKKLPKGWIVVHFYLNELEGKGY
ALIYDSDTDTWKIKEFFYAPLWRAFLTWQENYFSGKEGERFSADQLVELCKEIGKAMPFLFDLAENPKGR
PVLFIPHGFLHRLPLHAAIKEENGEYLLEKHPSRYLPAWSLAPKTDASPKSGKGRILLKRFREYDYDLIA
YEELENSEWDNKKDEKEATSDDDLEEIKANPEILVILCHGKADPTNPFRSRLKLKNGGISVLDILKAKLN
LSGTRVILGACESDLAPPLSFPIDEHLSLATAFLSKGAREVLGGLWEVRPEDVEEIYKEILDADDKSSLL
SAEIKQKQQEGIMKRKKDKKNGEYTRFYRIAPFRIIGFP
>gnl|CDD|469140 NF041238, AhpD_rel_CFYUT, alkylhydroperoxidase-related (seleno)protein. Members of this family are almost entirely selenoproteins, with an average length of 370 amino acids and typically with the motif CFYUT. Cutoffs are set so that most incomplete proteins that run from the N-terminus to the selenocysteine-encoding TGA codon, ending CFY, still score above cutoffs. So far, the vast majority of family members are reported from uncultured organisms assembled out of metagenomic sequence
IREDLAAAHRRAWERLASPGTWWTGAERVAIAAEARNARDCDLCAERKEALSPYAVDGEHDSLGDLPDAA
VDVIHRIVTDPGRLTRSWYDSVIAAGLSEEEYVELVGVVATVVSIDTFARALGLPLPPLPEPPPGEPSRY
RPAGAKVGGAWVPTIPPEDAGGPEADWYPGLYGVPNIIRALSLVPDEVRGFFDLSAAQYLPLADIRDFDY
EDRALSRAQIELVAARVSALNECFYUTTSHAMLLRASGEATGTDVDLSAVTGGGAGDDGGVPHGAELLAF
AEAVVGRDEAALAAARAALRAALGEAALVDAAAVAANFNGIVRIADATGIPLDDGKAELTADLRAELGID
RFAS
>gnl|CDD|469141 NF041239, Moor_selen_rel, CC/Se motif family (seleno)protein. Many members of this family have a double-Cys motif. Others, including several from the genus Moorella such as WP_263870381.1 and WP_263870380.1, have a selenocysteine at a similar location once structural annotation is corrected
MKIRISPEARDYILQKGGAVTVRLSPRGGCCGGTAPVPVVYAGAPKDPSRYERVEVDGIKVYLAKDAIAP
EGLRIDLEGFLGFKRLYVEGL
>gnl|CDD|469142 NF041240, YebF_not_Cmi, protein YebF. This HMM identifies the exported protein YebF from E. coli, Salmonella, Providencia, Xenorhabdus, and other closely related lineages. It excludes the colicin M immunity protein Cmi, a YebF homolog. The related model from Pfam, PF13995, covers both families
KKTGLLAAALLLGASFAASAAEDEQRTAKFPSCEGLDADQIAAQVKRDFLQNRIPRWADDKKLLGTADPV
AWVNPNDITGKDDKWQVPLTVRGKKTDKHYNVTVDCKAGTITYS
>gnl|CDD|469143 NF041241, YhfZ_full, GntR family transcriptional regulator YhfZ. Full-length homologs of the transcriptional regulator YhfZ from Escherichia coli, with an N-terminal GntR-like domain, are quite divergent. See PF14503 (YhfZ_C) for the broader family. This HMM identifies a subset in which the motif MPLPYxxxYEGLA and the C-terminal PxY motifs are both well conserved, suggesting orthology with conserved function
EKFLKKNGLAIIKLARELLSLKEGDRIPTISELAEKFGVSRGTVQNALKYLEESGAIKLESRGHLGTFLV
KIDYKKLLELAGIGTIVGAMPLPYSRLYEGLATGLYAAFEKAGIPLNLAYMRGAKVRIEALLNGRYDFAV
VSKLAAEQYIEEGEDLEIALDFGPGSYVSEHVLLFRDGEKKEIRDGMRVGIDSSSLDQKILTEAEFEGKD
VELVELSYNQLLDALAKGEIDAAVWNLDEIKDKKLGLNYQPLKSEKANKDASEAVIVVRKDNEEIKALLR
KLIDVEKVLAIQKKVLEGEIIPSY
>gnl|CDD|469144 NF041242, T6SS_PdpE_Fran, type VI secretion system protein PdpE. PdpE is encoded within the type VI secretion system (T6SS) locus in Francisella tularensis and several other members of the genus, is secreted by that system, but has not been shown to be essential to virulence and is therefore not currently named as a T6SS effector protein. So far, no homolog is detected outside of the genus Francisella
MSKKIFKLLLISLIFSNIYQQGFSNTITASIFELKNSSKKNATIFLNLNELCPTNIKACKDENDNNCIYI
TELIREPLSRINYYLAVPITGKSVKDLTILYKYDKEESPPEAINICLSLFKNNKYETYYSQVIYNWFVSS
ELYLSHSEGSIFINKDINNCKNYDKGNFLRVNLERIADGWAPPHYEKKITII
>gnl|CDD|469145 NF041243, T6SS_IglJ, type VI secretion system baseplate protein IglJ. IglJ (intracellular growth locus J), a encoded in the type VI secretion system (T6SS) of Francisella tularensis, is characterized component of the baseplate in a lineage-specific form of the T6SS apparatus
IEFLNKIKKKLSINNLLAIIHSYGIDAKDIKFIPVFSDSPSNATILDISYSNNTLYIKINVFKLKPFAKL
ENYYQQYEKNDNENAISVLEYGISSLLYRYFYGTKPLYNLTQGNALYIKADAPSLTIDNLINSLYKKLSE
DYCTIINYEKKKINIKRKPSILGKSYLGNIYLGGYIPSTKYIIKINVYLLNYNQSLIDNIKNQIKKFQKK
ITNLPIKIKIIIS
>gnl|CDD|469146 NF041244, IglI_fam, type VI secretion system protein IglI family protein. IglI (intracellular growth locus I), from Francisella tularensis, occurs within the type VI secretion system (T6SS) locus, and is important to virulence. This model describes a broad family of related proteins, the majority of which likewise encoded in the vicinity of other T6SS proteins such as baseplate subunit TssK
FSEIASLVENGEYEEAAELIEELLEEGIYDIRLICYYLYGLFLENGLAALPEILEALAELLEENWEALGP
AKKKEKHLDKSLNWLFKQLLKKLQYEEKTWQRWLSEDSSDELLEEALEALEELLEALEEALEDLPLLELL
SKLNKWLRKLKQALAKEPEEEPEPEEEEEEEEEDEEEEEEEAEESPAPAPSPSGDNLEGSSYKWQQLLKK
IEAFEQLVEEGDFFKAAIVADDIQEELENFDPREYFPELFAPFYKLLAPHAEEILPHIDNKDSLEWQALE
QLYQVDLDAFLE
>gnl|CDD|469147 NF041245, T6SS_IglE, type VI secretion system lipoprotein IglE. IglE (intracellular growth locus E), as found in Francisella tularensis, is an outer membrane lipoprotein important to the role of the type VI secretion system locus that encodes it in pathgenesis. IglE is a distant homolog of TssJ, as revealed after multiple rounds of PSI-BLAST and seen in its similar crystal structure
KLLLIIAVILLLSGCSTFSASDTFNINIQPSKLSNNGQPFYVVIEQPSDMKNFVSATYDSVSQSILDDNH
QSKLIHPKDGKNSISLKKSDKPGAVYFILKKNKPYNTWKYYINSPSGNSWSFTISKNNVIE
>gnl|CDD|469148 NF041246, T6SS_IglH_TssF, type VI secretion system baseplate subunit TssF/IglH
KVLLDTLEELGSNIEEDFDNYIREERNSRLKKYYPHLFTPLPKHCLVKIKDNLNNDSLYIDLGEQFFIED
KLNNKQFLYSTNSLTIILPFEVTNVYKQSDNLSLEFAAKSPFFLDIDSFDLWINPLLWKPYQLIYLYNLL
LKNKKGKVKIEYSDGSVTEKKVKLEFGIDYTLHPNENIRLNLHSPEFFLGFNINIEDLFYKDQKFKKIDL
LLEVDTDNLIEEDLQKLFHTNLIPLFNLFEDYSSSISYDGTKESYPLKHPEDDDAQPIEVLSVYENNKPL
IPISYKEIYKDGKSEYEFNLISQSSNKLIYAHIYPSLPNDSLSTKIHVNAEWTQLIEHSDLIKISSNSIS
TYKLDFKSIIYKSFKDNYNFNSLENLLKLLKLFNITQLRVKDFKLLLKFLDGDISAYSKISSLLNDIEVD
GITNELIIICSDKLYKAFVRFYARQIEEFINKNTPHFIKLKVGF
>gnl|CDD|469149 NF041247, UsfY, protein UsfY. Proteins of this family are encoded by the usfY gene on Mycobacterium genomes. The usfY gene is tightly linked with the anti-sigma B factor rsbW (usfX). However, the function of UsfY is unknown
DPVDHARTTRPHAGESMKDNLNWPGLILIGVGVVGFVGCLAAFATGHHEWGLTLGVVAVLGFVAGLLWLA
IEHRRVRRIEERWYAEHPEAARQRP
>gnl|CDD|469150 NF041248, T6SS_IglG, type VI secretion system PAAR-like protein IglG
MLDILEDSLKRLKELQQNSSSIANSISDLVSELNNIKTLLSPTKLNLSSSASTLTPSMGAQIKCSFSLAP
GSYLSIRAKTLTGNLPASNITDSKLGVNILPFAGCTNPANPTMNPFVFPWVCIPNLTPFIPTNPTTLLEN
APITTINSKAMCTFAPGGIVNFINSGQINAKTS
>gnl|CDD|469151 NF041249, T6SS_TssI_Fran, type VI secretion system tip protein TssI/VgrG, short form. Members of this family are TssI/VgrG proteins of type VI secretion systems of a variant short form found in Francisella tularensis and related species
MAKHDHAMNSDGVGLQVDGKDDSKGCSTSYESTGKATTQVSDTISSTADKTISLNVGDSKISITKDEILI
ATKNSSIMLNDDKIVLKIGSSSIELDDSSISIESDTINIKGSASISIEATQNASIKGANNAIKAKQAMSV
EGTTLNIKGSATATLKGATTSVG
>gnl|CDD|469152 NF041250, VI_TagQ, type VI secretion system-associated lipoprotein TagQ
STSKRRALLLAAAGFSTVLLGGCASSPVSKVAKTTKVEYYPSCYEPVQHLRSTDSAMTKSVATGAVTGAL
GGALTGALTGDSEDRGRNAAIGAAGGALVGGAAGYYTERQKQISDDRQRIGSYATDIDKSAADIDRSIAY
AKASQSCYQREFTNLLAGRKAKTISDAEGRKRLAEIVAGLKESNDLIAAVNGRAGEDLNNYTQAYEKDLQ
QVGVQRADVATVATAESAPATTKKATTKTKKKPKALPKVPKEAVTTEQTLQKAQAKQAESQQVASAGQTQ
VNSMCKNPDMGDWAPVPCPNV
>gnl|CDD|469153 NF041251, omp10_alpha_prot, outer membrane lipoprotein Omp10
MKRKTILALLAAAAALAACQSSPRPGPNAPAPQPAPAGVEGAWVDPNGIVSTFQGGTFETRTTDTNQLLA
SGNYVNVSPQLVEINMTSLVRGTQSKVNCALVTPSQLNCTSDSGAQFSLTRR
>gnl|CDD|469154 NF041252, outer_memb_MapA, outer membrane lipoprotein MapA
MKKKIFFIALALFLSACAAKQDTFAQVNQISKQTQCYSCESSQGFEAKIKGLLYISDVGIKCCANKRTLD
TGVALKKVYLHRFYDLKEEKKVLYANGQKYFIDENFNAIFYTYLKQELEARGIVVLENNNQNSPYVLKVD
LSFIDFYSKQDSNGLHSRLVGVLSLKDINKNKKFTIRTKQDVQGFENLKELSFYTHLLIKQMANKAASII
SSL
>gnl|CDD|469155 NF041255, mycofact_MftM, mycofactocin oligosaccharide methyltransferase MftM. Mature mycofactocin has an attached oligosaccharide chain of glucose residues with beta-1,4 linkages. In Mycolicibacterium smegmatis but not in Mycobacterium tuberculosis, the second glucose residue is 2-O-methylated by the SAM-dependent methyltransferase MftM
MTATTLLDPLAPAPPGRWDDSPVRVRRVPLVPPGFTRCGLLSWRRFCLRRDGGRLEIAHPLTPEEISDDL
VVLLLDELVEAGALSGQEEFELVAVGIVRSTVDDPLDAWTAFYRNSLRELRSGTAAFAPVHRRARSLVPG
GSVLDVGSCFGFFALRLAEDGHDVTATDISPGAMDLLDAVARRLGLPVDTLVCDAAALPLPDDSVDTVTL
IHLLEHLDPAHGDAALAEALRVARRRVVVAVPFEDEPSAHFGHVRRFDEEDLHALARQVRHTGLPAEVFE
DHGGWLVLD
>gnl|CDD|469156 NF041256, GntI_guanitoxin, guanitoxin biosynthesis pre-guanitoxin N-oxide kinase GntI
VDKIITKLLGWDTEEALVEIQDSGLTNRNYRVENGGEKFVVRISGGNSNLLGINRHAELIALKAVAAMGI
GPEVLAFDPPEGHLVTRFIEGRHFSLEDLTQPENIDRIAQLLKQVHSGPPIPGRFSPYRDIEDYIQTAFA
RGIDLPPPLERIEGLLRNIERKRGAFPDRFEGLCHNDLFANNFIDDGGSIRLLDWEYAGMGDILFDLANF
SMNQSLDREGDKILLESYFGKVSQALLAALNLMKFVVIFWEAMWGVLQAGISHFDFDYAGFANENFQTL
>gnl|CDD|469157 NF041257, GntH_guanitoxin, guanitoxin biosynthesis MBL fold metallo-hydrolase GntH
YFPGTEELGPDEMRITFLGSGPPPPRRGQANTSILVELGNGERDKFFFDIGSGSVANIIALQIPYNLLNK
VFITHLHVDHYGDLPYLYPFGAWSGRWTPLRVWGPSGRTPELGTKHMVEGMKEMLAWDTDAFSGFPIGDG
YEIEVNEFDFRDENGVVYEENGVTVRSWPRSHAKDGAVSYRLDWNGLSFVFTGDGRPNELTVEYAKGADV
FIHECFDTPELLSGKYGVPPELARYTIDTHHTPPYAAGKVFSLVQPRLAMATHFFNDPDTVAEILAEIRA
HYDGPLSFGPDLMVVNVTKDAIWVRMAVLPDYPWPRPPQAPEWFDFPLPQLVPPDPRTPREDQQEQFVRD
MEIDPKEYYPPGYWRELDQEWP
>gnl|CDD|469158 NF041258, motor_HelR_2, RNA polymerase recycling motor ATPase HelR group 2. This HMM describes the second of at least two "HelR" subclasses of the RNA polymerase recycling motor protein HelD for which at least a few members have genes preceded by a Rifamycin Associated Element (RAE) and are known or predicted to be induced by rifampicin, a rifamycin-type antibiotic. HelD proteins, including HelR, are helicase-like motor proteins that play a role in transcription, removing and recycling stalled transcription complexes that could interfere with normal transcription or with DNA replication
YEEELRSEREYVAGLYARLDAERARVKGRYRAALRGNGGTLVERDAEVRALAREVARLDVADNGLCFGRL
DAVSGERSYIGRIGLFDEDNDYEPLLLDWRAPAARAFYVATAANPENMRRRRQFHTRGRRVVDFTDEVLG
RPDGDERGDAALLAAVNAPRGEGMRDIVATIQAEQDEIIRLDHPGVLVIEGGPGTGKTVVALHRVAYLLY
TQRERMERHGVLVVGPNPAFLDHIGRVLPSLGETDVVFMTTGDLVPGLRVTAEDTPEAARLKGSLKILDV
LAAAVADRQRLPEEPLPIELADVTVRIDAETAEWAREEARASGLPHNEARAVFTEIVTYVLTERAIARIG
RGWLTRDDREAWERLRADLLDELADNEAFTAALDELWPILTPETLLAELYSSPERLRAAGADPALWRADG
DAWTVSDVPLLDELVDLLGRDKAADRAAERERRAEAEYAAGVLDLMVDREDLMDDEDHLLATDLLYAEDL
AERFVERDTRDLAERAAADRDWTYRHVVVDEAQELSEMDWRVLMRRCPSRSFTVVGDLAQRRSAAGATSW
GAMLDPYVPGRWVYRSLTVNYRTPAEIMAVAAAVLAEFAPDVQPPESVRACGVRPWSRRVSDDELASAIE
EFVRDEAGREGTSVVIGPPDVPGAVPPSETKGLEFDAVLVVEPERILADGPRGAAELYVALTRATQRLGV
LHRGPLPPALSGL
>gnl|CDD|469159 NF041259, mono_DmmA_fam, dimethylamine monooxygenase subunit DmmA-like domain
LRAALAEARMGTRLYLAGPEGFVWTARAAARAAGLLDDEITAEHTGTLARRVYCVHCRTTTEAVTGDVVT
CPGCGRDLLVRDHFSRRLGAYLGVMADAE
>gnl|CDD|469160 NF041260, actino_IHF, integration host factor, actinobacterial type. Members of this family are nucleoid-associated dsDNA-binding proteins called integration host factor (mIHF in mycobacteria and sIHF in streptomycetes) because of similarities in cellular role, not in sequence, to the integration host factor proteins of Escherichia coli. Actinobacterial-type IHF actually shows more sequence similarity to 30S ribosomal subunit protein S13. Some members are fused to an additional guanylate kinase domain. This HMM assigns the gene symbol mihF broadly across the actinobacteria
ALPPLTPEQRAAALEKAAAARRARAELKAALKAGELSLAEVLDRAETDEAVAKMKVSDLLEALPGVGKVR
AAAIMEELGIAESRRVRGLGVHQRAALLERFG
>gnl|CDD|469161 NF041261, RHS_core, RHS element core protein
MSGKPAARQGDMTQYGGPIVQGSAGVRIGAPTGVACSVCPGGMTSGNPVNPLLGAKVLPGETDIALPGPL
PFILSRTYSSYRTRTPAPVGVFGPGWKAPSDIRLQLRDDGLILNDNGGRSIHFEPLFPGEAVYSRSESLW
LVRGGVAAQPDGHTLAALWQALPEDIRLSPHLYLATNSAQGPWWILGWSERVPGADEVLPAPLPPYRVLT
GMVDRFGRTLTFHREAAGDLAGEITGVTDGAGREFRLVLTTQAQRAEEARKQRTSSLSSPDGPRPLSSSA
FPDTLPGGTEYGPDNGIRLSAVWLTHDPAYPESLPAAPLVRYTYTEAGELLAVYDRSNTQVRAFTYDAQH
PGRMVAHRYAGRPEMCYRYDDTGRVTEQLNPAGLSYRYQYEQDRITITDSLNRREVLHTEGEGGLKRVVK
KEHADGSVTRSGYDAAGRLTAQTDAAGRRTEYSLNVVSGDITDITTPDGRETKFYYNDGNQLTSVTSPDG
LESRREYDEPGRLVSETSRSGETTRYRYDDPHSELPATTTDATGSTKQMTWSRYGQLLAFTDCSGYQTRY
EYDRFGQMTAVHREEGISTYRRYDNRGQLTSVKDAQGRETRYEYNAAGDLTAVITPDGNRSETQYDAWGK
AVSTTQGGLTRSMEYDAAGRITTLTNENGSHSTFLYDALDRLVQQRGFDGRTQRYHYDLTGKLTQSEDEG
LVTLWHYDESDRITHRTVNGEPAEQWQYDEHGWLTDISHLSEGHRVAVHYGYDDKGRLTGERQTVENPET
GELLWQHETGHAYNEQGLANRVTPDSLPPVEWLTYGSGYLAGMKLGGTPLVEYTRDRLHRETVRSFGGAG
SNAAYELTTAYTPAGQLQSQHLNSLVYDRDYTWNDNGDLVRISGPRQTREYGYSATGRLTGVHTTAANLD
IRIPYATDPAGNRLPDPELHPDSTLTAWPDNRIAEDAHYVYRYDEYGRLTEKTDRIPEGVIRTDDERTHH
YHYDSQHRLVFYTRIQHGEPLVESRYLYDPLGRRMAKRVWRRERDLTGWMSLSRKPEVTWYGWDGDRLTT
VQTDTTRIQTVYQPGSFTPLIRVETENGERAKAQRRSLAETLQQEGSENGHGVVFPAELVRMLDRLEEEI
RADRVSEESRAWLAQCGLTVEQMARQVEPEYTPARKLHLYHCDHRGLPLALISEEGNTAWQGEYDEWGNL
LNEENPHHLQQPYRLPGQQYDEESGLYYNRNRYYDPLQGRYITQDPIGLKGGWNLYQYPLNPIRFIDPLG
L
>gnl|CDD|469162 NF041262, colicin_Z_Cterm, colicin Z C-terminal-like domain
AWAPPGFWGPWVDLQGHIGPNTYTVSFDTDSNAPSTFDVEIKYATGNGMKTINTLGPGSYTITGTGAAGT
DRIRFKSHSVGQNIRVT
>gnl|CDD|469163 NF041263, colicin_Z_full, colicin Z family toxin. This HMM represents full-length homologs of the colicin Z activity protein. The C-terminal is found more broadly, and is described by model NF041262
DSVNYDAFNCNSGKPHEPNTHWDPRTKAWEWNDLKLNSGSIPDSLPQEVKEALENNICIVCGKKNCPYIK
NNKDYQELIDALKSGDKGEARKIYMTKFAQFRGQKKGRIMEGLQKARNARERQGPCGYSGPFQSRRVIAT
PGIWSEWIELEGSTGNEQHPHVYTVNFNPSSNLESSFDVEIKYPESNGMKTINTIGPGSYFIKATGAGNS
YIRVKSHSVPITVTIDFPK
>gnl|CDD|469164 NF041264, MobA, plasmid mobilization protein MobA
RRTTVLPTIRCTPEEKEAIREKAADAGLSVSAFLRAAALGRRIRSKTDSRILNELRRLGGLQKHLFNEGK
GVLSKEYSEVLVAIKAAIRRL
>gnl|CDD|469165 NF041265, NadS, NadS family protein
MSFFDELKASLEEAVEIKNGVKAPARVTRYEVADVKAIRAQLNVSQAEMAKALGTSVDTIKSWESKRRNP
TGLAAKVLATIQDNPAFFKELAAH
>gnl|CDD|469166 NF041266, YsgD_CorL, YsgD/CorL family protein
MDTPSRYWLTYLSSRYNS
>gnl|CDD|469167 NF041267, relax_RlxS, relaxase/mobilization nuclease RlxS
DDFEPRLGRIGARRGPKGRRYLSRVLAAANLAGGGTGGAGRGRRFTGGRIGRGAGIGRVLASRDRHAGFR
SRRVVVKARIVKLGGKGLGAARAHLRYLQRDGVTREGERGELYGADADRADGKAFLERCDGDRHQFRFIV
APEDGAQYEDLKPLVRRLMTQMEQDLGTKLDWVAVDHFNTGHPHTHILLRGVDDRGKDLVIAREYISHGL
RERAAELVTLDLGPRSDREIEQRLRREVEQERLTSIDRRLLRDADDEGLVSPTARDPFQQALRAGRLQKL
ERMGLAEELGPGRWRLAPDLETTLRRMGERGDIIRTMHRELTAKGLDRSPADYVIHDPAAAGTRPLVGRV
VARGLADEHNDRHYLIVDGIDGRSHYVDIGKGDATDPLPEGAIVRIRPRPAGPRAVDRTVAEIAAANGGR
YSVDIHLRHDPTASEAFAETHVRRLEAMRRAGGKVEREADGSWIIAPDHLERVAAYERRQARRAPVIVET
LSARPLDRLVGADGATWLDRELVAEAPEPLRDAGFGREVRSALALRRQWLIEQGLAREEGGQVRYRRNML
AILRRRELLRVAGQLSDELGLPFAEAQPGERIEGRLRRRVDLASGRFALIERSREFTLVPWRPVLERHVG
KQVSGLMREDGISWTIGRGRGGPS
>gnl|CDD|469168 NF041271, Phos_CheZ, protein phosphatase CheZ
MTQEELDALMNGGDLESLEALETETKEEAKEEHNDEQKEDSKSSEKMTVKKEDAEKYGKISPNEWPPPPP
TEEHKVVHQLDDVTRDSEVKATQIFDQLDLIGASAEKIAKMVKKIQEPLKKHQEIFENLHTHFPSIESFK
TALNEQQEILNALKTIEEEAENCSDSSMQAMDIMQFQDIHRQKIERVVNVMRALSQYMNSLFEGKIDDSK
RVSSATYITGDDDKDLASADDIEALIASFGAK
>gnl|CDD|469169 NF041272, Chtaxis_ChePep, chemotaxis regulatory protein ChePep
MKMILFNQNPMIKKLLESVSKKLELPIENFEHYQELSARLKENQEWLLIADDECLEKLDQVDWLELKETI
SQNKNSVCMYKKGNEAQPFLEGFEMKIKKPFLPTEMLKILQKKLGFNTDASELEPTENLDPTQEILETNW
DELENLGDLEALAQEEPNNEEQLLPTLNTQEETQEKEEQEEETKKELVKEIQEEVKEQEKEEVAETPQDE
EKPKDDETQDVKEVEENTETQGVKETEKDTETQKELETPQELEDPKEETQNTEQEPVKEETQETKEEKQK
KTQDSPSAQELEAMQELVKEIQENSNTQENKEETQEVKEVEENTETQDVKEVEENTQELEVPKEEEQEVK
EVEEKTQAQELEKQEIAETPQDVEIVEEQDETQQELEIPKETETENVKEVEELTETQDVQEVETPQETQE
LSTEDHYESIEDIPEPVMAKAMGEELPLLNEATTEPPKNENDTETPKESVTETPKENTKTQKSDKTSSSL
ELRLNLQDLLKSLNQESLKSLLENKTLNIKITLEDKNPHA
>gnl|CDD|469170 NF041273, GlcN_kinase, glucosamine kinase
LDLLDLGDGHRLAIVASDGGLSAVPMVRDADGGWRRARPGDGVAEALLRLLARAPGSSTRGRFTVRSWTG
RTARGERPITVDQTNESVIVGDAAVVKWATHLQPGPHPAPRRIAALRAAGFTGMPAPWGLVTWRPPDGAE
TLVASVDEYLPGAVDGWTWAVDLVTAAARDGDPAPVAAAAAAVGTLVADLHAALAATATTATAADARRWR
DAAFDTLETACALADSASAALLRARRDEIAAVLDGLGDLAGTPVIDGHGDLHVGQVLRSDGRFVVTDFDG
NPVLPAAERVLPIPAALDVAGMAQSLAHVAIVARRYTDLDPAALAAVDAAARAAFLDAYTTRLAALGHAD
LYDPRALRAFRLQQVLREIVYAARHLPRWMYVPDAALPALL
>gnl|CDD|469171 NF041274, isoleu_diox_hilA, L-isoleucine 3(1)-dioxygenase
IKLSGKHKDNFGYLESTDGDIDFSIVKNIILNGHHHGNVLYIIRNYANKLVCSDIAKNFDQEVNQSGGNR
ADDGFVLTNQIGATQFSRNGEQYIKEVNRVNQSVAELMSSADGYATESLFLNRTLEKEFLDEGIHFGPAR
FKNSYACFATFRRWLDNGVMSLMPHEDKAQLKFADQDDFEIAAAQTVTAYNVCLEAAQGGGELKIWNLIP
DDECRARLGVTDTGYPYPPELLGDIESLSVRLNAGDIYFMNACHLHGVSSVSQGSRLTAGRFIGKLNDRK
VVYWT
>gnl|CDD|469172 NF041275, MurL_Xanthmoales, UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate epimerase
TFPRDAIRAFRFVRCGFDAATGVARLVYAFDDGPELVERVRFPGAPFALDAARAAAVEAALRLLHLIAGV
SYYKAAVPPEIRIEGYAIDAATAALLDELYLHGLGEFAYRNGLDLRGRIRFPAGAAAAAAAPALGLRRRA
LVAIGGGKDSLVSIEALRAAGVEQTVTWVGGSPLIAACAARTGLPTLNIGRQLAPELFELNRQGAWNGHI
PVTAINSAILVLAALLYGVDQVVFSNERSASYGSLIYGTGEVNHQWSKGWAFEQAFAAYVRRHVAADLHY
YSLLRPLSELAVARQFARLDRYDAHFSSCNRNFHILGERPADRWCGQCPKCHFVFLALAPFMPKPRLVGI
FGRNLLDDPSQAAGFDALLEYRDHKPFECVGEGRESRAAMAALAQRPEWREDALVARFAREILPQLDAAE
LALEPLLQPAGEHRIPAALWERLRAHF
>gnl|CDD|469173 NF041276, treh_trans_TtfA, trehalose monomycolate transport factor TtfA
MVPLWFTLSALCFVGAAVLLYVDIDRRRGLGRRRKSWARSHGFDYEPESTDILKRWKRGVMSTVGDVTAR
NVVLGQIRGEAVYIFDLEDVATVIALHRKVGTNVVVDLRLKGIKEPRENDIWLLGAIGPRMVYSTNLDAA
RRACDRRMVTFAHTAPDCAEIMWNEQNWTLVSMPITSTRAQWDEGLRTVRQFNDLLRVLPPVPQTAAQAA
AAAAARRNAAPSRPLAPAPAEEPPPGRADAPPPRRPAARPRPRRRPAREAGRPEARRPPPPRNGRQAPHY
QR
>gnl|CDD|469174 NF041277, coba_remo_CbiR, cobamide remodeling phosphodiesterase CbiR. Rare cobamides, analogs of B12 with critical differences in the lower ligand, can become available for a salvage-like pathway to B12 biosynthesis through the action of enzymes that cleave the lower ligand. Members of this family are CbiR, a phosphodiesterase, which joins CbiZ, a previously discovered amidohydrolase, in the guild of cobamide remodeling enzymes
FRLGTTSFIIPDTYLPNVRFLAGKVDEIELLLFESDECLENLPSPAEIRELAELAAELGLTYTVHLPLDL
PLGSGDAAERRRSVEVLLRLIELTAPLSPSAYVLHPPGDPSPDDLRRWQEQALESLEALLRGTGLDPSKL
AVENLEGYPFELLWPVVEALGLSVCLDVGHLLLYGQDPLEFLDRWLPRVRVIHLHGVDPGRDHLSLDHLP
PEALREVLDLLKDAGFDGVVTLEVFSEEDLEESLAVLRQ
>gnl|CDD|469175 NF041278, CmcJ_NvfI_EfuI, CmcJ/NvfI family oxidoreductase. Members of this family are typically biosynthetic cluster enzymes, including the Fe(II)/2-oxoglutarate-dependent dioxygenase NvfI, the hydroxylase/desaturase EfuI, and the hydroxylase-like subunit CmcJ of the CmcI/CmcJ methoxylation complex involved in cephamycin biosynthesis
EATLNYLVPTDERPRRYAFDPPGGVPWITGELEPHPVTIRDARPLADAPSLDREGFELVDHPSAVTDFRD
PAAVRRVYYPEVEALLKRLTGADRVVVFDHTLRRRDPGARAAGIRPPARRVHNDYTEASAPQRLRDLLGA
EEADARLYGRFAIVNVWRPISGPVQDSPLALCDARSVAPEDLVAADLVYPDRVGEIYLLRYNPAHRWYYF
PDMTPDEALLFKIYDSDPDGRARFTPHTAFDDPTAPADAPPRESIEVRTLVFF
>gnl|CDD|469176 NF041279, repress_GgpR, glucosylglycerol biosynthesis transcriptional repressor GgpR. Members of this family, called GgpR, found so far exclusively in the genus Synechocystis, are encoded upstream of the glucosylglycerol-phosphate synthase GgpS and are characterized as essential to transcriptional repression of glucosylglycerol biosynthesis
MRSNNRKKSIHPAHTNSFKVNKKNRIYRNQWVNSQVMPPTSEVEILPEKLFLLLYLTSNYFFHSPGAAFQ
KPEIGGLPLLFSTGPRGKGN
>gnl|CDD|469177 NF041280, mem_Micro_34, small membrane protein MtfM. Members of this family are typically 34 amino acids in length, consisting largely of one highly hydrophobic predicted transmembrane segment. Many are from the genera Micromonospora and Actinoplanes. Note that many annotation pipelines are unable to predict a bacterial protein this small without supporting homology evidence as from this HMM. We suggest the symbol MtfM (Membrane protein of length Thirty-Four from Micromonospora)
MVTEIGFVSLLVAGLGALAGGLVYLAVRISRGRW
>gnl|CDD|469178 NF041281, TraA_gammapb, TraA family conjugative transfer protein
AMAGTGGTEFDDVYTTLTGWTQGTLGRVIALAFILVGLVAGVARQSLMAFAVGVGAGLGLYNAPTIIDGI
MSATL
>gnl|CDD|469179 NF041282, TnpC_regulator, Tn3 family transposase post-transcriptional regulator TnpC
TPYGEVDAAALEKLRQSFDTTQLLRLVDRLDACRARLGGPDGLRDDLLRLHGMAHTVINGAGLSVPTEDA
SIWEQAEDVLDELEDLVAWLRSARAVLEPLEALRP
>gnl|CDD|469180 NF041283, PrgP, ParA superfamily DNA segregation protein PrgP
MGYVIVLANQKGGVGKTTDTVMEAVVASSVFNKKVLVIDTDLQGNATQFLSKTFNVPNFPQSFMKCVEDG
DLEKGIVHLTPNLDLIAGDYDTRELGDFLADKFKSEYDRTFYLKKLLDKIKDDYDFIFIDVPPSTDIKVD
NAMVAADYVIVIQETQQFAFEGSKKLILTYLQTLVDDFGDEINVQVAGILPVLLQARRPLQQKIVDETIE
YFGKDNVFNNIIKNHARLEWYGEQGIQFEDYHDRRMFALFADIFCELEERIKSFEKTGDVENFTYTHQYI
NQNKLTPKGKEITINGF
>gnl|CDD|469181 NF041284, PrgO, DNA segregation protein PrgO
MALLKRDNNQQVRIKKTAIDDDSRDEYGEKKYKAKDRKPIQVDPPVLELIKSLSYAKDMPMYELVRLAMN
AYLDTLTDREREIYDRRIKK
>gnl|CDD|469182 NF041285, ABC_SBP_TrpX, tryptophan ABC transporter substrate-binding protein
ATIIILVAFLGGAFFYESKSQQEKKKKTPKVVKVGILQLVSHPALDQIYKGIEDGLKEEGYVNGKNVKID
FQNAQGDQSNLKTMSQQLVNENNDVLVGIATPAAQALANATKDIPIVMGAVTDPVGAGLVKNLKHPGGNI
TGVSDQAPVKQQLDLIKELLPNAKTIGILYTSSEDNSTSQVKEFKKLAKKLGLTVKEYAIPSTNDINQTS
QVMASKVDAIYVPTDNTIASAMSTVVKNANAAKIPVFPSVDTMVKDGGLATVSVNQYQLGVETGKMAAKI
LKGKKPATTPVKVVDKGEPVINLKQAKKLGITIPESLLKEAK
>gnl|CDD|469183 NF041286, lipo_GerS, germination lipoprotein GerS
MKKKWTILLIMIISLVTIVIGCQKRQSTKEEVYKDFQKKISKMKYYTCKADVEVIGNKSSHKYTFIHTYK
KPDNYKLEVISPKHLKGKTIEYKGDKILVKNPEIDDVVELPNVGKNSQYLFIGDFIKNYLQNEEIKIKLS
KGYLVLETDIPGDNKYFNKQILYIDAKTKNPNKMEILDNEGNPRFIVNYKDFEYKK
>gnl|CDD|469184 NF041287, lipo_GerS_rel, germination lipoprotein GerS-related protein. Members of this family are related to the lipoprotein GerS that is found in the spore cortex of bacterial such as Clostridium difficile, and that regulates the activity of other spore cortex proteins. Similar between members of this family and GerS family lipoproteins
KKKLLILLLLLIPIIIIILVIIFRKTKEPTNEDIIDYLKNIKSYSTDVEYTIKNDRQEIEYNTKQYYSKD
KGYRIEFGKDRVKIYKDDKIYVKDNINGKKYTLDKDFDEIYKLAFIEEYLSLLYTNEEIKESFKEWGDTE
YLVINLDIPGNNKNLNKAELYIDKKKKIPKKLIIYDKKGKERVKIIYKNFKKNKEIDKELF
>gnl|CDD|469185 NF041288, YdaE_coli, YdaE family protein. Members of this family include YdaE from the Rac prophage region of Escherichia coli K-12, a homolog from the Gifsy-1 prophage region of Salmonella enterica LT2, and related proteins from other closely related species. The presence of four conserved Cys residues has led to annotations as a zinc-binding protein or metallothionein, but the actual function seems unclear
KKCAYCRKPIEEGKEVKSTLLYMHGTQLARKERKYCSKRCAEYDQMAHEL
>gnl|CDD|469186 NF041289, KorA, KorA family transcriptional regulator
MKLIEQSQVESAFNQGAVREVTIVRVSEREWYPTFDADDPVTGKPNTYSLRTQRGFELRTWADPRYLFKF
LHERVGVKECSLSLSDDEWEE
>gnl|CDD|469187 NF041290, StbA_2, plasmid stabilization protein StbA
MKPKSIRAAIQLMLPEIEEMLSLGVSREEIFKAVSERFGLENVNVRSFDTALYRARQNRKNVLHNTHDRS
SNKGAAESVLHNTQPSEPEKQESNKAESPGIIDKEFFKKINENFDPKKFNKKF
>gnl|CDD|469188 NF041291, StbC, plasmid stabilization protein StbC
MDKQPDKEEVLMEWFLGDAKEINADQKSALAKATALLEGLEEANGSLDSTVEKARRELITAHRELTQAIR
DAEAARAEALQRVAAAQKSAAAAGVRRALPITAVCSGVSALIGAAIAAFILR
>gnl|CDD|469189 NF041292, StbB, StbB family protein
MKVAVINFSGNVGKTTIAAHLLAPRMPGAEIFAVESINETASDLGLDVEQLKGKQFGELFEELMLEDDAI
VDVGASNVEDFLKLMSRYDGSHEEFDYFVVPVVPETKQQRETIKTIEALAALGVPAEKIRVVFNRVESDD
DVEDEFAPIFAYAKKTKSFTLNPEAVIFENELFDRLAAKKLTIAELLADTTDYKALLREATDEKERDHLA
DMIALKRLAKSVNRNLDAVFAAL
>gnl|CDD|469190 NF041293, G6PDh_Azf, NAD-dependent glucose-6-phosphate dehydrogenase Azf
MDDPVLLTGAGGRVGQAILEGLGDDYDWRLLDREPPPEDKLPDGVPDHEYYVADVTDEEAVREAMEGVGA
VIHLAGDPRPEAPWDSVLRNNIDGTQTVFEAAVDAGVEKVAFASSNHAVGAYETDERTPDMYRTDDEFRL
DGTELPRPGNLYGVSKAAGETLGRYYHDEHDLSVVCVRIGNLTEGHPPIDYERGQAMWLSYRDCAHLFDR
CLEADYDYEIVYGISDNDRKYYSIERAREVLGYDPQDNSAEY
>gnl|CDD|469191 NF041294, Scnl_mescCoAtase, succinyl-CoA:mesaconate CoA-transferase
MGALSDLRVLDLTQVLAGPYCTMLLADMGADVVKIERPGGDLIRSNPPFHEDPDEEAYGGYFQSVNRGKR
SLELDLGDEDDREDFLSLVETADVVVENYRAGTMEKFDLGYETLRERNPELIYSSIRGFGDPRTGETHRQ
GQPSFDLIAQALGGVMEITGQEDGPPTKVGPGIGDLFTAVLNAVGILAALHHRERTGEGQFVDTAMYDSM
VSLCERAVYQYSYTGEVPTRRGNSHPTLFPYDAFEAADGYVVIAAFGDNHWRALCEAMDRPDLAAEYPDA
ASRLENRERLREEIADWTAERTTETVLDALEGRVPCAPVQDTADIFADPHVHDREMLVEVEQPGADETVT
IAGSPIKMTETPPEPGGRAPLLDEHREELLG
>gnl|CDD|469192 NF041295, dynobact_RiPP, dynobactin A family peptide antibiotic. Members of this family are RiPP precursor peptides modified by radical SAM/SPASM enzyme maturases. The founding member of this family, from Photorhabdus australis, has the ten amino amino acids WNSNVHSYRF in the mature product called dynobactin A. This antibiotic targets BamA, involved in the insertion of beta-barrel proteins correctly into the outer membrane
IWNKALLDCVGGTARDLKGKDIDEKIVEKLVKEAASPSWNGNVHTYRF
>gnl|CDD|469193 NF041296, RNAactase_tcmA_Halo, tRNA(Met) cytidine acetyltransferase TmcA
AELARALRAEARRTNERRLLVLAGDREAGRDAARDALDAADVPLTETTLVGPRDGLRCERLPPKRADELL
GTTRDAVVLDAHEECRPNALGRVVGAVDGGGLLVLLTPPLDEWPDRRDGFDETLAVPPFDVADVTGRFRR
RLVETLRAHPGIAIVDVDTGTVERDGLTDPAPRAPDPPPPPPDDHAFPRAAYEACLTADQVDAVAALEAL
REPGRAVVVEADRGRGKSSAAGLAAGALAAAGRDVLVTAPAYRNAAEVFARARELLDTLGALADDDDEPR
ELRLETTGGGRVRFARPADAADLPGDPDVVVVDEAAALPVRLLESFLDAPAVAFTTTVHGYEGAGRGFSV
RFRDRLAESDHDVTEVTLDEPIRYAAGDPVEVWAFRALLLDARPPVDQLVADATPETVEYRRLSPADLLA
DEHLLREAFGLLVLAHYRTEPDDLARLLDAPNLSVRALTHDGHVVSVALLAREGGLSAETRAEMYEGGRI
RGNMLPDVLTSQLRDEDAGEPVGQRVMRIATHHAVRSRGLGSRLLDEIRAEFADDVDWLGVGYGATPELL
DFWRRNGYRTVHLSTTRNDTSGEYSALMLDPTSDAGRELHDRHAAWFADRIGGVLSDPLSDLDPDVVRAA
LRAVDATPDLDLSDREWRVVAGAAYGPGLFDTAPGPFRRLALRHLVDGADEDDLSAREERLLVRKVLQGR
PWEAVADELDYHSTRQCMRALGDALEPLVDEYGTDAALEERDRY
>gnl|CDD|469194 NF041297, UDPGDh_AglM, UDP-glucose 6-dehydrogenase AglM
MNVSVIGSGYVGTTVAACFADLGHDVVNVDIDEDIVATINDGEAPIHEPGLDELVAEHAGDRLRATTDYD
AVLETDVTFLALPTPSNDDGSIDLSIMEAGAESLGEALAEKDDDHLVVVKSTVVPGTTEEVIAPALEDAS
GKTAGEDFGVAMNPEFLREGSAVEDFLNPDKVVLGADDDRALDRLREVYEPLVEAADAPVVETGIREAEM
IKYANNAFLASKVSLINDLGNICKEFGVDAYEVADAIGLDDRIGEQFLRSGVGWGGSCFPKDVAAIIAAA
REAGYEPALLEAAVEVNDRQPERLLDLLDEHVDVAGERVAVLGLAFKPGTDDVRNSRAIPVIEGLQERGA
DVVAYDPVATENMRERFPDIEYADSAADALDGADGALVVTDWDEFAALDEEFDAMATPVVVDGRRIVERR
DGITYEGLT
>gnl|CDD|469195 NF041298, rSAM_mat_DynA, dynobactin maturation radical SAM/SPASM protein DynA. Members of this family are the radical SAM/SPASM protein DynA responsible for the maturation of dynobactins. Dynobactin A is a BamA-targeting peptide antibiotic, with amino acid sequence WNSNVHSYRF, made from a RiPP precursor peptide through post-translational modification
FTNVIKPTHICNLACTYCYNDDVRKPVMTLETLERVIEQTFEYARDTGGFTGVEFIWHGGEPMVAGLDFY
ENAVEFQEEYANGIRYSNSIQTNGTLINDEWIDFFKKNDFSVSLSIDGPKEIHDANRVDRNGKGSFDRVM
KAIEKLRKAGIPFGVCLVLSKANIDHVDEIYDFLVSEKLPFNIIPLTKSGSARDHYEDLGLSADEYAEAW
IKLYDRWFDAEDDDYVYVSDFVRKTRAILAGRPADCIGMSQCADTNISVDPVGDVYPCASLSGHPDAKYG
NINEKSLAELMNSPRAREWRTRQVDPQCAKCKWQHVCHGGCMSRAYKFFGDINRRDYYCPSLFKIYEHIE
KRLRER
>gnl|CDD|469196 NF041299, RiPP_near_DynW, DynW-associated RiPP peptide. This rare and poorly characterized RiPP family contains proteins encoded next to the DynW family of radical SAM/SPASM peptide maturases. This family was described by bioinformatic analysis of related families DynA (radical SAM/SPASM) and DynB (RiPP propeptide)
ADRISSFGASLSARQQSLLSAMLVKVRARLDAAETRLSPGDVSEVLAERAKSGTNQSGWTFDIWTYRF
>gnl|CDD|469197 NF041300, rSAM_mat_DarW, radical SAM/SPASM peptide maturase DarW. DarW is a radical SAM/SPASM domain-containing peptide maturase most closely related to the darobactin maturase DarE
SAIEFIGRLPAEDILNAHEQAIFAIEEARGLPPTRSPARWLVVVLKATRLCNLRCTYCRSWAEGPNQTMT
FDVLARAVREALSMPGLHGVEFVWHGGEVTLLKPKVFKKLIWLQQQFRQPGQEVRNSIQTNATHLTDEWI
EFLSELGMGVGVSIDGPPEVHDRRRLDKDGRPTSSRVAGGIARLRQAGIPHGALVVVDRELIDAGAERLL
GYLAEIGLDKISFLNVLPENDPDDPEIVKSTYFTFPEYVRFLTETFDVWWNSYRDRMEIREFRDLIPKMS
VGAKPIGCYWMGNCMGRYVTLEANGDLAPCDKYRGDPGSILGNVMHSPMADIIRTSGYLADAKKEASDAK
TRMAPCKWFHVCQGGCPHDRHLNSRFVPAVDPRCCGLAPLLDHMRRTAGRTMERAGIRAGSSGLD
>gnl|CDD|469198 NF041301, Cit_synth_Halo_CitZ, citrate synthase
MSDELKKGLEGVLVAESELSYIDGDAGRLVYRGYDIEDLAREASYEEVLYLLWHGELPTEEELAEFSDAM
AAEREVDDGVLETVRALAAADEEPMAALRTAVSMLSAYDPDADDADPTDREANLRKGRRITAKIPTILAA
FARLRDGEDPVEPREDLSHAANFLYMLNGEEPDEVLAETFDMALVLHADHGLNASTFSAMVTASTLADLH
SAVTSAIGTLSGSLHGGANQDVMRMLKEVDESDKDPVEWVKDALEEGRRVPGFGHRVYNVKDPRAKILGE
KSEELGEAAGDTKWYEYSVAIEEYMTEEKGLAPNVDFYSASTYYQMGIPIDLYTPIFAMSRVGGWIAHVL
EQYEDNRLIRPRARYVGPKDREFVPLDER
>gnl|CDD|469199 NF041302, HMG_CoAsyn_Halo, hydroxymethylglutaryl-CoA synthase
MTAVGIDAIEIWTGKLKLDLPETFAPAKGEDPEKYTKGLGLHASSFPDVYEDIVTMGANAAKRLMERKGL
EPDDIGRIDVATESAFDNSKPVSTYIAGCLEQVYDGDFHHANKGERKFACIAGTQALDDAYNWIRAGRNR
GRAALVIATDTALYERGDPGEATQGAGAVAMLIDEDPDLVELSTEQGYGSADETDFLKPNQQFPSVDGKR
SMQVYLARMREALEDYESVAGDTHPDDFAYIPFHTPFPGMVRKAALLGYRHMIRDTEIEDELAEEIGRQP
REEAFDDDEAYEEAIREYMDALKETDRYREWYERTIEPTLDISRRVGNWYTGSVHLARASALKHAAEEGR
DLAGERLLVGSYGSGAQAEIHAETVQPGWREEIDALDIDEQLAARYDLSFEEYEQVHDVHNHDKEVDVEP
FTTPEGEFVFDGWGRMGERKYRY
>gnl|CDD|469200 NF041303, Indglycph_syn_Halo_TrpC, indole-3-glycerol phosphate synthase
NAEEELAPAVRSILAAARERPGGDERVSVDARSLPDAFAAAEADGRVPVIAEVKPTSPTTDGTRDDDPVE
LAEAMVAGGAAALSVLTEPEHFGGSPETLRRVREAVDVPVLRKDFLLREAQLDAVEADVVLLIARFVGDD
LEGLVAAARERGFQPLVEVHTRAELERALDAGADIIGVNNRDLAKLEVDLGTFESVAPHVPDDDVTLIAE
SGISTPADVRRMREAGADALLVGSAIMDGDVRENTRRLTT
>gnl|CDD|469201 NF041304, AvrBs2, type III secretion system effector avirulence protein AvrBs2
MRIAPLQPAATHTAAPATPTHTSASTPTQVPHAPGSNPPLRPRPRRRAAGAPPLVPLPDSAMTGKPALVA
LDGEFSEQRLAEVQARQITVQALQSKLATHLAQAGTALKPDSIAARFAAGTLQPVYLDTAAFRAMARSLP
GRARAAAGPVLVDAQQGRIIFDLQRAFAPGDTFSDAALAALGKALDLPGQGLANPDWLQPAQSRPPRRKL
QQAPRYHGHEIPAQDGGAGFFKANDHRLLEGKQALLREHRKELVHENYFQAPSTRALGKDVMVHRGLFDF
HAGIPENSLAAIDRAYAQGYRTLELDVEVSADGVPVLMHDFTIGRTLDDPQNRLVAQVPFAELRDQPLVI
RNPVDGNFVKTDQRIASIEQMLEHVLQTKPGMSVVLDCKENTAEDVALLLMRRPQLRPIAAIKVYSKAYK
GGFDQFFSNLCKHLQINPLHSQDEPRRAKLRRDLSKINVVPVLSQGMIEDPQLRDFFPGKDDGAEGLADT
ATQWMQSWNGMHPVIAEAMVTDPDSDAGKAMQLARARLRQPGSGYEKAAFSAAYRYEDFSLPRSDGDRDY
FTWGNFGEINPVPESGFEPKRGTAGAFRDQGESVLTDQPDEEVLALRENRTLPRGHTGMELDVPPDTPID
TNRDAEIVQLRRQEFMAAKQPLDPVHVAAVREGARLDRGASLQLDPAARRAIDKRAESLGLLTDRYRGAP
VSHYLNEQAKQTEPEE
>gnl|CDD|469202 NF041305, SecF_Halo, protein translocase subunit SecF
MVEFEVPEVDYTRYSNRQLAAVPLAVLAVALLVIAGWYVLTGAPVNLGIDFTGGTELRVQTDASQAQIRA
AFDAEPESIQSVAGEDTYIVTFQSGDNDATDALEQQAEDAGFEVQSVSSTSASFGADTQRLALIGVAVAF
LGMSVLVFALFRTFVPSIAVVLSAFSDIVIPLALMNLLGIELSLGTVAALLMLIGYSVDSDILLNNHVLR
RSGDFYESTYRAMRTGVTMTLTSIAAMAVMAIVATLFGIQLLASIGLILVFGLAADLMNTYMLNLSLLRW
YKFEGVA
>gnl|CDD|469203 NF041306, RnaseHI_Halo, ribonuclease HI
MPVIECDPDAARERLEEAGVEIEPGNTDHERWRAERGGATAVAYDDKVVVQGSDPADLTALLREDGGGRA
HVYFDGASRGNPGPAAIGWVIVTGDGIVAEGGERIGRATNNQAEYEALIRALEAAADYGFDEVEVRGDSE
LIVKQVRGEWDTNDPDLRERRVRVRELLEGFDDWSIEHVPREINERADELANEALDD
>gnl|CDD|469204 NF041307, AvrBs1, AvrBs1/Avra family type III secretion system effector
MKINHSSKALPSKPFEEEVDLQKDSSARSGLVTPSLDSPTLKKAPRKGRIKNNIAPLHTSLLERVHEKKI
QVQNLAQLQEKLAKASNGVELEELIDASSVKELLFKRNSDIEEEYGAGKPLMIRSLRFSSPQEATGKFGA
SGKTPAKREVDTLCNKSTGHDIVMTPASLIAKDVKMNLISEMERPKDKPKYKGLPSVVYGQVSSGSESSY
LARRNGFGDVHSFKSNNAFNSDYEKAAPSLSHAEKLGLIERNLKPFIKPDPDRPSEGFSHSIQELAEHQS
LLQARRPGSILRHNEYCTKLELWDAKAIAVGESRALAVATLIEFNLEMLSIAREIESEGHEGKMLTDFIE
RQLSWLGPQAALDLKSTLERLSALTAQEREFILNGICSQLRRGVSLCTYEKQETGSHIRELSLLDFSAED
IMEGIRIFLSSKLLH
>gnl|CDD|469205 NF041308, AvrBs3, type III secretion system effector avirulence protein AvrBs3
MEPIRSRTPSPAREPQAGSQPDGVQPIAGRLVSTAASSPLDGLPARPAMSRTRQPATPAPSPAFSVGSFS
DLLRQFDPSLFDPSLFDSSPAFGAHHADAAPGEMDEVQSGLRAADDPQSHLSAAVTAPSPTPPRTQAAAR
RRSAQTSDASPAESVDLSTLGYTQQQQEQIKPNARSTVAQHHAALVGHGFTHAHIVELSKHAAALGTVAD
RYQAIIAVLPEATHKDIVEVGKQWSGARALQALLMVAEELRGPPLQLDTGQLIKIAKRGGAPAVEAVHAS
RNALTGAPLHLTPHQVVAIASNNGGKQALETVQRLLPVLCQPPHGLTPEQVVAIASNDGGKQALETVQRL
LPVLCQAEHGLTPDQVVAIASNIGGKPALETVQRLLPVLCQPPHGLTPDQVVAIASNDGGKQALETVQRL
LPVLCQAPHGLTPDQVVAIASNDGGKQALETVQRLLPELCQAHGLTPDQVVAIASNGGGKQALETVQRLL
PVLCQPPHGLTPEQVVAIASNGGGKQALETVQRLLPVLCQPPHGLTPEQVVAIASHDGGKQALETVHRLL
PVLCQAPHGLTPEQVVAIASHNGGKQALETVQRLLPVLCQRPYGLTPNQVVAIASNDGGKQALETVQRLL
PVLCQAPHGLTPDQVVAIASNGGGKQALETVQRLLPVLCQRPHGLTPHQVVAIASNDGGKQALETVQRLL
PVLCQPPYGLTPEQVVAIASNNGGKQALETVQRLLPVLCQRPHGLTPDQVVAIASNDGGKQALETVQRLL
PVLCQPPHGLTPDQVVAIASNDGGKQALETVQRLLPVLCDAPHGLTPHQVVAIASNIGGRQALETVQRLL
PVLCQAHGLTPDQVVAIASNNGGKQALETVQRLLPVLCQPPHGLTPHQVVAIASNIGGKQALESVVAQLS
SPDPALAALTNDRLVALACIGGRPALNAVKKGLPHAVALIRKMNNRVPERTAHLVADLTQVVRVLSFFQC
HSNPAQAFHEAMTQFEMSRQGLLQLFRRVGVTELEARSGTLPPASQRWQRILHALGLKPSSASAQTPGQE
SLHAFADSLERELDAPSPMQDASQAGSSSRKRSRSDDPVHGFPAQQIAEALIPEHRDAPHLLPLSSWGAK
RRRSRIAGGLPDPGMPTDADLAVSSTAFWEQDADPFAGAGEDFPAFDEEETAWLMNLFP
>gnl|CDD|469206 NF041309, XopB, XopB/HopD1 family type III secretion system effector
PLHAGAVRRKNGRLVSDDPVIHALLSYAQADQPLPANIASINGMQLEIRAHPDLEAALEAFKEAFTVETA
NLVPAADSSERVSEDIEADIHIPLLLKAIERGAAAFGTNASIEMGDGDQVPAHAFLAAHAPTVTSNDDVL
QLFINQKLRADTDLQVRLGAQSLLHAATKKEFQLKGLAGSLGVSSGLGSAWELGASELLKNALFGKNFSP
SKYALQAAGIDSVPPILIETLDTMCVLSIIKGMKGEDWSLRDLLPKAMKAGAISSVLSFPNNLLQYAGFK
SRPADLAANTATTEAAIFGAASGIPPEVKENEELMRAGLFQSMKDGVLAHPAREMSPKQTIEQMTRHALD
IAPGESTAVKSMGLASIVGMIPLIAGDKATGLVSESVLRIFRSTVFNPIEAIALNALALGSRVDIPGLFD
SDNAKHARVVQTILARASQQMEAGGREISAEELHRMLAPRSEFLRHVGTAIVNGMNATFDAIPALVRKLG
YGEAPLSERIPYQDLAVPAT
>gnl|CDD|469207 NF041310, Prot_Kin_Rio1_Halo, serine/threonine-protein kinase Rio1
MTDEFGLLEPEEADAPGDEWEEIDVSDTEADRIARKRDREFDEFRKRIKDADQFKVEASVFDDATYAALY
KLVQDGYIDAFGGPISTGKEANVYEALGGDGEVAVKVYRINASDFRQMRDYLEGDPRFEGIGGDKKAVVL
AWTRKEFANLKRARKAGVRVPEPIAVQRNVLVMELLGTEDDRAPRLSEVHIENPETAYEVVREYMRRLYD
AGLVHGDLSEYNIVVHDGELVVIDLGQAVTVHHPNAEEFLERDCENVANFFARQGVDVDGDDL
>gnl|CDD|469208 NF041311, Sig_rec_Srp19_Halo, signal recognition particle subunit SRP19
MVENVIWPAYFDAELSRSEGRRVPEDLAVEEPTVDEIAKAVQQVGYDAVIERDVAYPREHWEERGRVLVK
DADDAGKNDLVQAVAAYVGALRE
>gnl|CDD|469209 NF041312, Superox_dis_Halo, superoxide dismutase
ELPPLPYDYDALEPHISEQVLTWHHDTHHQGYVNGLNSAEETLAENREAGDFSSTAGAMRNVTHNGSGHY
LHTLFWENMSPNGGGEPEGDLADRIEEDFGSYEAWKGEFEAAAGAAGGWALLVYDPVAKQLRNVAVDKHD
QGALWGSHPILALDVWEHSYYYDYGPDRGSFVDAFFEVVDWDEVADEYETVVELFE
>gnl|CDD|469210 NF041313, UDPGP_AglF_Halo, UTP--glucose-1-phosphate uridylyltransferase AglF
MKAVVLAAGKGTRLRPLTDDKPKGLVEVDGKPILTHCFEQLVDLGADELVVVVGYRKEQIIDHYGDEYRG
VPITYAHQREQLGLAHALLTAEPHVDDDFMLMLGDNVFRANLGDVVERQREDRADAAFLVEEVPREEASR
YGVCVTNDYGEITEVVEKPDDPPSNLVMTGFYTFTPAIFHACHLVQPSDRGEYELSDAIDLLIRSGRTID
AVRLDGWRVDVGYPEDRDRAERRL
>gnl|CDD|469211 NF041314, Malate_DH_Halo, malate dehydrogenase
MTKVSVVGAAGTVGAAAGYNIALRDIADEIVFVDIPEKEDETVGQAADVNHGIAYDSNTEVRQGGYEDTA
GSDVVVITAGIPRQPGQTRLDLAEDNAPIMADIGSSLAEHTDDFVSVTTSNPVDLLNRHLYEAGDRPREK
VIGFGGRLDSARFRYVLSDRFDVPVGNVEATILGEHGDAQVPVFSKVRVNGTDPEFTDDEREEILEDLQE
SAMNVIERKGATEWGPATGVGHMVEAILRDTGEVLPGSIPLDGEYGHEGVGLGVPVKLGSDGVEEVVEWE
LSDFEREQLDEAAEKLAEQYEKIA
>gnl|CDD|469212 NF041315, malate_syn_AceB_Halo, malate synthase AceB
QHDREFVRTFFTSPTAVEGEDDSAKMLRRAAQLRGMQAPDVWVPDNEDATAPSMRDEGVENIVEVVAEHG
ADFPGEIHPRVVWHRDDPETRYQGFQQMLEIADPENGAVEHIDGFVIPEVGDIDDWKKADEFLTIVENEH
GLEEGSLSMSVIVESGEAELAMGDLREEMGKPSNNLERLFLLVDGEVDYTKDMRAMTPTGELPPWPELRH
NTSRGASAAGLIAVDGPYDDIRDVEGYHERMTENRAKGMLGIWSLTPGQVVEANTAPLPPETGYWLLDAD
GREVELDDEDGVQVYDGDRLSLEETGDGRYRLTVGGDERELDEDELREELLDLTSYVPSMDDIVDSMEEF
EAAKEAGKGAIAMTQSATLRIDGVEVDISRDRMWDEATYQAAQTPISLFQDVYENRPDQHEELEERYGED
VVERAMEVG
>gnl|CDD|469213 NF041316, NleH, type III secretion system effector kinase NleH
MLSPHNANLGCSWNSLTRNLTSPDNLVLSSVRDAAARSDNGRQVKVGNRTYRVVVTDNKFSVTRESHSGC
FTNVLHRLGWPKGEISRKIEAMLNPSPVNDTSERGSVHSKRPDLPPVDYPQPELPEVDYKTSSKKVKFVN
NLPVPGNVIGKGGNAVVYEDKSDPTKVLKMFTVSQSKEEVTHEVDCFNKYYGEGSAEKIYDDNGDMIGIR
MKKINGESLLNIDSLPAQAEQAIYDMFDRLEQKGILFVDTTETNVLYDRDRNEFNPIDISSYNVDSNGSW
NEKQLLQAYHGGRQDLIGVVLSII
>gnl|CDD|469214 NF041317, HtdO, plasmid transfer protein HtdO
MRKVTFLKLLLFLSFGFAVFLATRCYYQSTYIPKGTVTIIPSEPVVEEIANSAFEKPTIVLNDPTLENKF
VGSDTENEGRKTDIHKENELKGNGHHENSKALVPVESDRVHLSVKDSWVKAGEPYIVPQMSENERQLKIK
RYLAPKSGANNGH
>gnl|CDD|469215 NF041318, phage_rep_C1, phage repressor protein C1
MVNYVYGEQLYREFVKFRDLFLSDAVARAQHVDVTSDGRKVRPVVVLPFKETDRIQAEIDKWTEMANELE
QYPDLNIPKTILYPIPNILRGVRKVTTYQTEAINSVNMTAKRIIHLIDKDIRIQKAAELGERSKKYIANL
ERTKKLMEKYPEDEKFRMRIHGFSETMLRVHYISSSPNYNGGKSVPYHVPLCGVFICDETLRDGLTIGPE
FEKEKFSLYDSIEPIICDRWPQAKIYRLKDIEEVKNKHAIEREEKKAKSAASATRSRKTKKGDPVNDNPE
SAK
>gnl|CDD|469216 NF041319, PTS-HPr_Halo, phosphocarrier protein HPr
MERTVTVVPEAGLHARPASKFVETANEFDAEVTVGRADDDGDLVNAASMLAVTGLGVRHGEDVRLVAEGD
DAEAALDALEAVLSTPE
>gnl|CDD|469217 NF041320, pfkB_Halo, 1-phosphofructokinase
MILTVTLNPAVDHTVELDEPLEPGTVARTDDAQFDAGGKGINVSKYLVALDVETVATGLLGGFLGRFIRD
QLDADGIPTDFVEIDGPTRLNTTILTPDGEYKINQNGPTVDESAVDDLVETVREHDPETVVVAGSLPPGL
GPDAIDRIARAGDWETAVDVGGDLLAELDAEYALCKPNREELAAATGRPVDTVEDCAAAARELRERGFER
VVASLGADGAVLVTPDGVLHAPALDVDVVDTVGAGDALLAGVLAALERGESDEAALRTGVAVASRVVSVP
GTSVPSLDDVRADRDRVSVSSY
>gnl|CDD|469218 NF041321, Alpha-amyl_MalA_Halo, alpha-amylase MalA
MHHPGPPRFVAVGDTVELAPRDPDPDATYRWRVTSAPVASTASLGDDPVEEFVPDAPGTYVVELDAPDGT
HDLTVRAFPGDLAPAGEGGGSSGGSGGSGMSGGSGSGSSGSSGPGRSGGGSGSGSGSDGAGGGSGGRPRI
RLDGAVEGDEVVVRADPQPHPDSSESAADLDVEFLLDDRDDVDRDAVTVDGRELRIPLDALPDRVRVHAV
AVGESYSVPDAVEVERDGEPDGGGDGGGAVVSGGSVAVVRPYDPPEWAEDATLYEIYVRGFAGDDEDAET
TFEAIEDRLDYLDDLGVDCLWLTPVLQNDHAPHGYNITDFFSIADDLGTREDYERFVDAAHDRGMKVLFD
LVLNHSARDHPYFQDAYGNPDSEYYDWYEWQDSGEPGTYFDWEYIANFDFTNLEVRRHLLDAVDEWAELV
DGFRCDMAWAVPNSFWRELRDRVKARDPEFLLLDETIPYIADFHEGMFDMHFDTTLYFTLRQVGNGHEPA
EAILDAVEGRAEVGFPDHAAFMLYAENHDETRYIVECGDPAAEAAAGALFTLPGVPMLYGGQELGQRGRR
DALAWDHADEELREHYDDLIALRDEHPALGADGDLVRVDYEEGDSDRVVAFARETDDEAVVVVLNFGEEP
ATVGVDEAVDATDLVSGESVAAGDGLTVDDVAVLPAD
>gnl|CDD|469219 NF041322, Anth_synII_Halo, anthranilate synthase component II
FVDNFDSFTYNLVEYVSEQREHAETTVLKNTASLAEVRAVDPDAIVISPGPGHPKNDRDVGVTADVLREL
SPEVPTLGVCLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVATEVPDCF
EVTATTDHDGEELVMGIRHREHPIECVQFHPESVLTGVGHDVIENFLAAA
>gnl|CDD|469220 NF041323, Nitr_red_NasA_Halo, assimilatory nitrate reductase NasA
MRCAVGCGHVQRGVDSGYGLDTVRGDAAHPVNRGLACQRGIRETADPDGEWLTRPLVRRDGELVPTTWDT
ALGRAVEGLRAALERDPDGVAVLGSGQQTNEAAYALGKLARGGFGTRYYDANTTLCMASAVTAYYDAFGS
DAPPPTYDDIPEAETHLVWGANPAVAHPVMFRWIRDSADDDDSELIVVDPVESETAEVADHHVAPDPGGD
LALARAVLARLVETDRVDEAFVAEATEGFDELRASLPDAETAAATAGVSLDTVDRLAAALEDPTLLYWGM
GVNQSVQGTATAGALIDLCLATGNLGPGSGPFSLTGQANSMGTRVCSSKGTWPGHRPFDDPDHRRAVADA
WDVPVSRLPDDPGPGPVGIVDAIDDGDVEAVWTVATNPVAGMPDATAVRERLEDAFLVVQDAFRTETVEL
ADVVLPAATWGESEGTTTNMERTVSRVRAATDTPSGVRTDLDIIATIGNRLVPGLFDEPPPDPEAVFDEF
AALTAGTPADCSGISYDRLDAELAVRWPAPDADSEGGYRYYDDGDESWSFPTPSGRARFSTGTHGPLPEP
TDEDYPLTLTTAREADGYNTGVRSRGPDDPGPPVARVHPETAAAHADAGDDGDRRVRVESRRGSVTARVE
PDEAVPEGVVWLPIHHPATNELTLPAVDPRSDEPNFKQCAVRLV
>gnl|CDD|469221 NF041324, Bacteroid_MobA, conjugal transfer protein MobA
GRKPKLDPAVHRYSVRLNDEENARFLALFEQSGMKVKAHFIKACIFGKPFKVVKIDKGTMDYYMRLTSFY
SQFRAIGVNYNQVVKELYSNFSEKKAMALLYKLEKQTIELAALCRQIIQLTEEFEEKWLQK
>gnl|CDD|469222 NF041325, Bacteroid_MobB, conjugal transfer protein MobB
MVAKISRGSSLYGALAYNQEKVDEENGKILFTNKIIETADGNYSIAQLMRSFEPYLPANRRTEKPVLHIS
LNPHPDDKLSDEQFADIAREYMEKMGYGNQPYIVFKHEDIDRHHIHIVSVRVDEDGKKISDKFEKRRSMK
ICRELEKKYGLHPATEKKQRAEDPILKPVDYSAGDVKSQIANVVKHLPKYYRFQSLGEYNALLSLYNITV
EEVKGEVNGRPYNGLVYSALDDKGEKVGNPFKASLFGKSAGYEALQKHFEKSKEKIKDKPLKEMTKRTVA
AALQTTTDEKEFKKQLKEQGIDVVFRRNDEGRIYGVTFIDHNSRTVLNGSRLGKEFSANAFNEWFNNGSK
PEIPIPDQSTPETSSTSNAEEPHHLFDFLNSGEDSLIEGLGGLLPEAQGEDYEEEAFARRMKRKKKRKR
>gnl|CDD|469223 NF041326, Bacteroid_MobC, conjugal transfer protein MobC
GENEQALRKILDFTRLISILLLLLHFYYYCYGAFQEWGLTSEFTDRILGNIARTGLFSSFLKSKLFALLL
LAISLLGTKGKKDEKLTWKKILAYLLTGLLLYFLSWLLLYLPLPATLVAILYIGTTSIGYLLLLSGGTLL
SRLIKNNLMNDIFNKENETFPQEERLLENEYSVNLPARYRLKGKVRKSWINIINPFRALLVLGTPGSGKS
YFVIRHVITQHIEKGFSMFIYDFKFDDLSKIAYNHLLKHKDKYKVKPKFYVINFDDLSRSHRCNPLDPSF
MTDITDAAESARTIMLGLNREWIKKQGDFFVESPINFLTAIIWFLRKYEDGKYCTLPHVIELMQVDYDDL
FTILRTEPEIEVLINPFVSAYLNGAMEQLEGQIASAKIALARLSSPQLYYVLSGNDFTLDINNPEEPKIV
CVGNNPQKQQIYGAVLSLYVSRLVKLVNKKGKLKSSLIFDEFPTIYFNGIDSLIATARSNKVATCLGVQD
FSQLRKDYGREQADVIMNIVGNIISGQVTGDTAKQLSERFGKIMQDRQSLSINSSDTSISKSTQLDSAIP
ASKISSLSSGEFVGMVADNPDEKIELKIFHAEIINDHEAIKKEEKAYKPIPVIRDVDDQMIQENYLQIKQ
DVQEIVESELERILNDPELAHL
>gnl|CDD|469224 NF041327, Bgr08870_fam, Bgr_08870 family protein, N-terminal domain. This HMM describes the N-terminal region of Bgr_08870 from Bartonella grahamii. Homologs appear restricted to other species of the same genus. The C-terminal region includes extensive low-complexity sequence, but also regions of homology with other at least one other family of Bartonella proteins
MTKTKKLDMELPKEGRFISSEFPILRENLTKIDQALMEVEEKVDEKAPSKHTHTISEITDLEAALKGKMA
ADKTFTFADLSDIEGAKDAANNYVLYKSSNNNFTFGSAVSLLGAHQHKTEDIVGLDDFRAKINEDLTSYG
RLKQANEWQNYNKFTSKVTMSGGLELLGNSSFNLIHNGEVVTSLSTSGSLLKGPLKVDGDLVYTKSQVD
>gnl|CDD|469225 NF041328, C_rich_MXAN6577, MXAN_6577-like cysteine-rich domain
LLLALAALLLLAGCPEPGAVCPEGLSVCGGACVDLRSDPSNCGACGVACGAGQTCVAGACGCGPGTVACG
GACVDTASDPAHCGACGAACAPGQVCEGGACREACSEGLTRCGGACVDLATDPLHCGACGVACDPGESCR
GGACT
>gnl|CDD|469226 NF041329, CmeU, CmeU family protein
KEEIKKNLNALFKARAEFFAFLDENVPKKENTDVFDFKNAKDLNLKEVYAKFYAYDYAIRKLLPDVYKAY
EIDFD
>gnl|CDD|469227 NF041330, BimD, protein BimD
MKLPILIQILPALALSVASLGGCTRDAEPMPVAHANAGAPASRGWPAYMEEFNESIRSMSGEHETGVHIN
RGWGVFNTIKAVPSADPAASACAAPTDASGARRAPAHAHRPDPAAADSRMS
>gnl|CDD|469228 NF041331, LigA_Halo, ATP-dependent DNA ligase LigA
MEFAEFADRAAAIEAESADLEIVALVADLFADAGDDLPVVARFVQGRVFPAHDSTTLDIGPSLCYEAIAR
AAGPNVSADDVEDRLAEVGEIGAVAASYDFGGQQGLAAFGGGGGDGLTVAEVDDELRALAAAEGSGSQDT
KVDTLFGLFNRCSPDEARYLARLVLSEMRIGVGEGTVRDAIAEAFDVPVEAVERALQVSNDYGLVAETAR
DEGEAGLDAIHLEVGRPVQAMLAQAGTVTDALEAWGEAAVETKFDGARVQVHYDGGDEVRLFSRNMEDVT
DALPEVVEFVEESLDVPAILDGEVVAVDDDGDPLPFQEVLRRFRRKHDVARAREEVAVELRAFDCLHADG
EDLLDAPLTERHDRLEALLDGTAVSDLLLTDDPDEIADIEADALEAGHEGIMLKNPESTYSPGRRGKNWL
KRKPDVETLDLVVTGAEWGEGRRANFLGTFLLSVRTGDGYETIGKVATGITDEELAELTELLEPHVRSED
GQEVDIEPAVVFEVGYEEIQTSPTYSSGYALRFPRFVGVREDKTPADADSLERVERLAE
>gnl|CDD|469229 NF041332, KDG_KDGal_kin_Halo, bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase
MTDLVTFGETMLRLSPPGGERLETADELDVRAGGAESNVAVAAARLGADATWLSKLPDSPLGRRVVGELR
SHGVDTDVVWDDEGRQGTYYLEHGGEPRGTNVIYDRADAAVTTATPEELPLDRIRDAEVFYTSGITPALS
ETLAETTAALLEAAQEAGTTTAFDLNYRSKLWSPEEARETLESLFPAVDVLVVAERDARTVLGRDGDAEE
IAHGLASEYDFETVVVTRGEEGALALHDGEVHEQPAYEADTVDPIGTGDAFVGGFLARRLAGGDVPTALE
YGAATAALKRTIPGDVAVVTPEEVEAVVEDGGGDGISR
>gnl|CDD|469230 NF041333, CruF_Halo, bisanhydrobacterioruberin hydratase
RREVEARLDRLVRENRFTIAVVFPLVGAVLLLASAEGLLPPPLAFNPLLILFGTLVMRLPLVVGLLPLVD
RRAAAALGALTAYAYAIEYVGVRTGWPYGEFEYGVDLGPMLFGEVPLGLPVFFLPLVLNAYLLCLLLLGD
RARSTLVRLPAVIAAVLAMDLVLDPGAVALGFWAYDAGGAYYGVPLSNYAGWVLSATVAVVLLDLAFDRT
ALLERLRDCEFMLDDLVSFVILWGGINAWFGNWVPVAVAGLFGVGLLRTDRFDFDLL
>gnl|CDD|469231 NF041334, XopJ, YopJ family type III secretion system effector XopJ
LGVSKPSSSRSPEHYGANPAQSAPSSSESSPPASPTPSRSPSSPAFSGLPRRPRKKAEALAEALNSANVN
INPELAHYAEATLDNAANIQPTEEITNLDIENLPTLVRTYNARYPGLNLQCFDSPQAFLDSLMTTDEPAW
RAVVRLDPPSLHHVAIDVRTHEDGKKTLIVLEPALAYKMDDGEPTFLPGYTELRRNLQSQFGENAKMAVI
QVEAQKSLIDCVIFSLNFALNAYQKDSVFDDLHERLRNHGRCFPSGDSASLLNKGIELIEGTKVLPPIFY
KHAHSRGTIDEVLKNQPGIADTNVSTGRSNPRETLSERVEAFRVDRGERSYSMSIEASRARKIRKAIE
>gnl|CDD|469232 NF041335, surf_glcprot_Halo, cell surface glycoprotein
MTRNKQIRAVLLAALMVFSVFAGSIAFTGTAAAAADSVSVGSDTVEAGPSASVSVTVDDDNTGSSGGMHV
WVDVNGDGYYNAGEPNVSATSASANPITFDGSFDLASVSAGDYNVSAAEDASLTDGETQATTNADTLTVT
AAEKPSLLSAVHYDDGTPKVEVAFDETVTVNELNVTDGESNLSQSVSVNTGQVVVTLSQVYTDDLEVEYN
VTDDSGNTATGTEDVTFAPVYVAGTSNNTAYKGSKVAVVASSTNTDVEVEGADDDNNYQFAGSTGKNSQV
FVFDTEGKELDTYEFTIGGAQDAEVDVRDLGLEVSVDDLNITDEDALEGSVSANAGGRTVDVVALDSDGD
EVDGASQTLTLDGQGEADFNLSTLDAGDYTVEVTDAFSGVTVESDTVSVSKAKDSTSDFGSSVVTEQVGD
IAEITVTLEGTDEADVMIGGDSLGYTANVTVEDGNDDGEVVLLFNTYDPKKTSSFDVDDSDDEVTVDDIT
TEIPDGDLLDAGDYDLEVATGGDADNVGTLVLEERSTDSQAVWTAPTGADLTESEDVYDAIENENLTQTD
AVANGDVVVHQVSATGLEGAFDAKDFDALTGTQFNLTVEQTNPGPNRDAKVLGINSSSATVIADGENDTY
FIVYDLDDVSASRTDYYDSGADQFAVEDDDAFNATFTVLEDGDLAEDDESASAEFEVVEPELSLDQDEFA
VSAAAEQTISGTASVAPGTALTVRVKSDGDTQPRFLKTATAYVQADGSFSSAFDFSEQKENDTFEVTVSV
DSGSAEDATADGVVGAVAETTTETTTTEETTETATATEEPTEEPTETATEEATEEPTEEPAEETTESSTP
GFGIVVALVALVAAALLAVRRD
>gnl|CDD|469233 NF041336, CheA_Halo, chemotaxis protein CheA
MDDYLDAFVRESEEAITELNNSLLELESDPENEEAMETIFRTAHTLKGNFGAMGFDDASNLAHAIEDLLD
EIRQGELAVTPERMDLIFEGVDQLEAIVDEIEADGETQTDPEATIEEIRASIEEGADAGASGAVEDGDAG
DSSADDGIVDADVVVDDVVVPELAADGEVYHARVEIGDSDMPGVDAMLVLEAIEDEFDLLGTVPDRDAIE
DGEFEDTFDLYVATDNDVDSDDVEAFYELNGYVDTVDVEDVTDEVAAGDLKDGPTEDDDDAGADTDDSGS
SSSMAHSVQEIESVRVDVDQLDQLYGLVEQLVTSRIKLRRAVEEEDLVSAEDELEELGKITASLQDTVMD
MRLVPLKKIVGKFPRLVRDLARDQGKEIDFTIEGEDIELDRTILTELSDPLMHLLRNAVDHGIEPPEERE
AKGKPREGTIELRAERERDHVSITVEDDGAGLDVEEIREKAIEKGVKTEEELEAMDDSEVYDLVFHPGFS
TTEEVTDVSGRGVGMDVVHQTVRGLDGSVNVESEPGEGTTVTLRLPVTVAIVKVLFVTVGDEEYGIPIKN
VDEISRLEDVETVNGREVITHDDEIYPLVSLGDALDVPGETRNGDGMLVRIRESERQVALHCDDVVGQEE
VVVKPFEGILSGTPGLSGTAVLGDGEVVHILDVVTL
>gnl|CDD|469234 NF041337, XopD, Ulp1 family type III secretion system effector isopeptidase XopD
MHPLLEDLPRRNPAQGHQDESVHRMRAPAPTSKTHTDYSKLLEIIPRYGDGESYRNLKRKFPGFGRYLTD
YGLISRFTGTQMLRELNEDQRDYIKHQIIRRIEDLLDPEYREIALQNLESDCSLTLRALDRIKSAKAKAQ
AIDEAKIKATTKAEAEIDAAFEDDDVTIKGILEYLPRYEAGESMSSLLCDIPNFHSYLTGDGSYTKGARG
LLKYSTPDQKKRLDRALERRKLALASQKPKKLKGITRTLHQNPHLLLEISQKFSNRSLSIEDASSGYLSQ
ASLEKLVDQETGELTSLGEEVISGASEGLQAAIRANFRLRYQQPDLPANSPPQAFQRPEESLPAVSFFSG
QLPPTPSGGWAPQNSSGYWNPDSPAKSSFSSLFPPTPLRGWPQDPPGEWRPATPAASSYEPTLPNSFFSG
WSQELSRGWYPDTPATPQYPPQSSASTFGDLSSLNEGNYGYREFDLNTPQEVEQPWRGYDYGTQTPVGHS
AMSPERIDVDNLPSPQDVEDPELPPLTATSWLGDGHLVAYTNDLARRLQGQPNAHLLNFADSQVVTMLVS
GDRRQRNRALRRLVGRGTPPIVFLPINNPNSHWSLLVVDRRTGDAFHYDSMVQPQPAAQATNTQQYYLAR
MAARAMGLDATPVRGMPIAIQRDGYSCGDHVLTGIEVLAHRVIDGTFDQAGGRDLSDIEPDRGLIRDRLA
QAEQAPAESSARQASERPVEQKKKKSKWWKF
>gnl|CDD|469235 NF041338, XopE, XopE/AvrPphe family type III secretion system effector
MGLCVSKPSVSGSPVAGSPEHYATHATEQTTPSTPSSPEASMSPSLHGLAALGPPRARRGRAGQPTLQPH
EVQQAAYQLGMRLNGRPIEDARDRQRLADATATVHETRLALHRGRGNVDSDLRLSNGRSATYSALSYCLG
EHDENLLAGSALAVGAGNCDHNAAINARRHAVRMEDGGQMMTVRDYEVAHLYALYQPPGSAEAEESAVVL
DSWGDGPAVLLRDSRWAETYGTSTTVIERFDKPDAIDALARTNAFRAEIEDPQTELHAYARDLETAFLAN
PAPGYIFSSMPVIAPDLAESTRQRLQEYSPRTRKALAADAARQAYGLDDAQPISPRTTTAILKDAERLDA
LGRPPLSW
>gnl|CDD|469236 NF041344, XopF, XopF/Hpa4 family type III secretion system effector
KAQLRAALDDLPFAAPSGEQRALEAEYLQWAAARLQERIAAFGPDAGYQIVGDMKAAGAKAALPIAYECL
RQFISSAMRTPFGNAAATAYDPRRGPLSEKLSPAVLGGAVAGLTSYTTDTLLLPAMDRRARVANLPRFKA
VDPKILVPDPPPVQLEVTAEGTKRFWRPLRDSEVGGEDDAPTLAELKAQAYDRRAGLAQRQSTLDGKSDT
LLLKPVLTAGFNAARRTLSPPGTLLTPAGVLGLSALASGGAGAVQKATLETGKALARTGQVSVPDLVGGT
QRLNLFALALPDKTRPPAQWSDAVHFPRYLLETGKEALALAKQAFRTANAFTTAVRDVLGRHVASNVLAS
FASTGAGRLIASPLRGGYGTPLPGEALNSPASVLQQAGQSFFNDTVWNALKAKNGSNTTQLATRLDRERA
QKQARLQRTAARTLRALAEPIDQAIAALSPPTPAEIARAMEEGELAPAPGPLAQALRTALETLRTEIGTQ
SVSIATIDAVLTALRAGTRAALSGVPRNALTQTLDAQLETLKRALHQREALRQWRSGR
>gnl|CDD|469237 NF041345, XopF1, type III secretion system effector XopF1
MKLSSDIGTSSSSRATSHAPAHPTQAEEAAASPQERTPSGPLAGLSSPGAALRGRRASLSRRATTDASEA
GSSLGASHRSESSQSSHSSDATFYSAQASSAPSESDAPATPAAAATYAERSAAAAAELKAQLRARLGALP
FAEPSEEQEALQAAYLEWADARVQERIAAFGPDAGYQIVGDMKAAGAKAALPIAYECLRAFIIGAMRNPF
GLAAGAAYDGARPPGSEPLSTATLAGAAAGLASYTSDTLLIPAMDRRARVANLPRFQAIDPKILVPDPPP
VLLEITAEGKRFTRPGEGDAPTLAELKAQTYDRRAGITQWQSTLDDKSLDTLLLKPTINAGFNAARRTSD
DPGTLTPAGQLGLSALAIGGAGVVQKAMLETGKAVARTGQMSVPDLLGGHQRLNLFALALPDKTRRPAQW
SDAVHFPRYLLETGKEGLALAKQAFSTANAVTTAVRDVLGRHMLSNVLANFASLGAGRLIAAPLRGGSNG
SVAGEAANSTAVVVQQAAQTLFNDTVWNALKAKNGANTSQATRLDQERAVAAARHQRTIARTLQALAEPI
DQAIAMLSPPTPAEIARAMEEGEPLAPAPGPLAQALRTALEQLRTEIGTQSVSIATIDAVRTALRAGWAA
MFSGVPRNDLTQTLDTQLQTLKRALHQSEELRQWESGR
>gnl|CDD|469238 NF041346, XopF2, type III secretion system effector XopF2
LDWMPRAADAQPYREKQRQLEAEYVDWAAERLQARHKAFGPNGGYRFRVDMRPVGEASLPAAYDGLRQFL
SSASRTPSGGAIATALDPRKNENGVNDGELNNKFDPAVAGGAVGGLTAYLTESILLSAMDRRARLANMPR
FKPVDPKILVPDPGPVQLRVVEGTKEFWRPLRDSEVGHAETTGSDDRPTLNALKGQAADRRKSLATRQKL
LDGKAEAALLKPVLTGGANVLRRYLSPAQALLSPLPVFGTSVLASGTAGAVTKATLGTGKALPWTGQVRV
DNLVGGTQRLNLFRLALPDPDQPALSWSDARRLPNYALEVAQEAGALLAGPWRSSGGPQRSWRDFSARVG
DLLRSVGGNVVASVVSTGAGLLLASLVRGGYGSPLPGESLRSPGSVLQQFGQSFTNDFVWQAWKAALGDT
SGDLASSLDRRRDQKQLRLWSEALQEQRALDPLLERLQPARLIEVIGAVEQALQRALNLLQALPQGIIEH
GDVATALATLRRLHAHGETPLALRLAKLQARLEKVVRLLEQREALVAWRSG
>gnl|CDD|469239 NF041347, XopG, XopG/HopH/AvrPtoH family type III secretion system effector
YPGIYIESLSNDQRFKAEVEEALDKIASGPSGNQLLDELSALSTRGRKVTIKEIDANQAPVARPVLTRSQ
IEKYGDPSSFEFNREIAKKAAGLGTKKKGEGTSAIVGWSPHASIELNENGSPTRLGSNPDDAFVSLAHEL
VHAKHMMAGTSKGGSGDRYDPSTPAGKEELRAVGLGKYAYSNTGEPSENSIRAEHGLPLR
>gnl|CDD|469240 NF041348, XopH, type III secretion system effector XopH
MPNSISGSIASSVSPDGERDIDAPEAIKQEVASGSSSQCLPAELIGLPARRRRTASTSPQDAPPPRSDTA
GHSQLIQKFRTPLPLPPPPTSTPVLQYDRSPGSSDNFRSSDEFDLPESCNPTGWKDLHVSGSGSIASIGQ
ITRLRPSRDRPVVVLDVREESHAIVGGYPGTWRAPNNWGNVGKSRDEALADEHERIQELKSQETVQIFHR
KDVKSEVPNPRSVTLSKPLIFSEEELVKAAGAKYVRLTVTDHLGPRAEDIDAFIAMEREMAPHERLHVHC
GVGQGRTTIFIAMHDMLRNAREVSFDDIIARQLAFNPGRALDFNKDVSHEGRSEFRNDRLEFLTLFYEYA
KENPKGQPRLWSEWLDHN
>gnl|CDD|469241 NF041349, XopI, type III secretion system effector F-box protein XopI
MPINRTGLPHAAASTSQTEEASTSQAPASQPPLDPPAVQTGRAEIFDRLSALPRDLRREIVRRLGPRSLA
RLGSVSRQMADDAREGMHAFLTARPRYDPSVEFGAVTSAERMRAALHAVTHFPYPDDEDRSEQILRAYGR
LAARIPSLPEAQRFEAFTAVLNHATRYSGPMAFRVLARLTHDLGSLPEDLRALAFHAILPSLIATRRQAL
QAAAGAAHGGDMGAVAEADAGAVQGDAAPGAQGAVAPAQGGAAGGIGGALPFNLLASAIRQLPEEAVNLA
ITEAAALQTGPRLLAEVTLRLHLVGLEPIHRFQQAYAQLAEQLARSGDGAEALTHLVALLNGLPDPGMRQ
AAFRELTRAVHALASTESRVAVLRRLAGALPHQPAAVRYLCSLDVLAAAESLFPSEQIQVIAAVRAQAAA
IPNHAAELIARCDRAIATASMMLATVSRRYMDM
>gnl|CDD|469242 NF041350, XopK, type III secretion system effector XopK
MRIQQPGSSAHSLDPSTPETPVAPKAAQVAQGWPLGLKALKKRPLQRRSDRDAASRRHHGEDANAEIQEA
EAAYDVFVVAKYLADPLHGTADKTAELLNEIPKRGEPEHAPEAEEPAPPEHPPAEHAPAPAGHHAPHPPP
TAGPHASTPEGAHTPAADAGHGADPHAVEHAAKESIMHALAEEGAPGGTFELAMSLGISGAMLPLSGLAI
YAAYKETREVAEQRSALRQRERQLQSERALLQPALATGPLAVAAGAQIHALGEAIETLAYQQQRNTRDGA
IAATSMASASVIFTKAASELAIQGGLAIGAKSANAAGLVGHSAAAAGAASAAGIAGTFVLAPLASVAATA
LGGTFLHQSRKEKTRVVADVARVERFLQQLEPSELSPGAQRYQHFLSTKLAQRSRFAGSFNQWNKGFVVG
GATYTASTLAKVGLSAAVLAGATVAGPVGTGLIIGAGLLGAATMGVGSHQFLLAHGKQKRYRNYETEDMP
GVDRALLAVADLLPAAAAPAAATQDAPLLADQLQRSALDVALTPVADEAAGSAEDDGVAEARAGLGPKHD
HGRPAIGDAPAATAGPAAADAVADASVAREAEDAVPQHGFELRSALYACTDGQEKALETFLQRCADDLNK
HYRAKPRSTDEHTAAGQAAHKASLGRRAKAALRAGATYGRAVLTGKPREAREKAARSYAKHSDTLTETAL
AQWLQTPGSVKPQIAYMQCCLELQKKYLQAKLSARVDLPPLDAHSDPASVAEPPAAAAQRAPARLAAQLR
EARERDETQLRTVNLMLEELGMAEEELASPDARSNARAANRMPGLQQRLVGVLTSNAITPQPGAAGFARF
CMKQAREHTTDVRGTLLATEMQAARIREKAAAAAPA
>gnl|CDD|469243 NF041351, XopL, type III secretion system leucine-rich repeat domain-containing effector XopL
VLSQWQRHCAADRDRWHSAWRQANRNNPGVETRTRRALKATADMLKDAALPERVSLELHSVPLPRFPEQT
SRLSHLQHITIRAAGLQELPESIQQFANLRTLTLARNPLRSLPASISSLSRLRELSILGCPELTELPENL
ASTNASGEHEGLVNLQTLQLSGTGITSLPASITSLQNLKRLQLRNSPLSALPPAIHHMPKLEELDLQGCT
ALRNYPPIVGGLAPLKKLNLRDCSNLRTLPLDIHRLTQLEELDLRGCNNLSRLPPSIAQLPANCTIRVPP
HLQAQLDRLRPEPGRTARVTPGPSASSSGGAAGASSSVTTTELLHKAALERIEDTAQAMLSLVIDDERNP
FLEGAPSYLPEKRPPGTPTTLGQIPALQKMLEESRDPHFLSRVSDMAGPSPRVTNVSNWKAQKSAHLGIV
DHLGQFVYHEGSPLNAATLAKAVQMWKTRELIVIAHPSDRARFPELTLHIPEQTSDDSDSE
>gnl|CDD|469244 NF041352, XopN, type III secretion system effector XopN
MKTAASANPLSRTASPSSAEIHEIEEEASPHASPSHSDAQPDAALTGLSRRPSKRGKETADATAPASQTA
SHLPSVGLQASQPAVSSDPGRATLVRLKEQLAADNLRPVEPQLAAELINKLRPMKLPDATGAQERAATHA
DLLSRISETDVMDWYKAQGLSESDVSNLRRTALLSGMPNPSGSFLNNAMQYIVSPWINYATRQPWAGAGF
GFATAAIAAPMNAAQQSAVVSLCESIREHGGHVIVPDKKQINDKHWLPDLAKALERHIAEFSGCCDRFRE
LKNAADQSPAAAPTAELTAAAHQLLQAEKRLHQAQHDFVMTQGAHDRQWMGNRWQAIPRILRSPLASTLG
LLSKTGAMRALSPTAQTVGALLMTAAQHVAAGFDEQAKQDYNNKLNLLYADVLTETGKSKLARGEPVAAE
DIDQGKLRKLIQSPTQALVKRVTSGLAAMEKALKAEVAASPSPQGAADADDLDLEAGHGAGPAKALKLLS
QDLQALREGRLDELDPDGVAAKLLLGAEKSVVSDQLINDIAKKYTSREFSAQTAQRIGQMFHLGVLGSAA
SSVIGKASSAAQGGTRNVPTAQTLAISALSGGMAAVGALNQHTAITVKNNRREGDTDIGLKQQVLRGVMG
GANEALSQRRATKASKAINALLQDNDVEALLGQARALTQQSGATSSAAQAAPSLTLPQAVEQLRPGVASA
SQSHEVIVQIGDDQAPRPA
>gnl|CDD|469245 NF041353, XopO, XopO/AvrRps4 family type III secretion system effector
MINTSTKSVNSHFTYSLPAEEAQRHTPQADAGSSPPATTSIHPALEGLPSIRLGMQAPRLRQLTESPSAQ
HRQNARLTKAFKAQRQDINTQPGPSNSPHLTALDKLQQRDFKPAAGGLEIPFTPNSLLGGGKRVSQLGSS
SRDVHVVPRGAAAELREAIQDKQLLIQTLTQDLQEATDEANPALIAQNQRLLRQARADLASLQRQYAVYG
EESRRINQ
>gnl|CDD|469246 NF041354, XopP, type III secretion system effector XopP
MEVLNKALKRGKVWNALATDVRPTPAADILSPEARLRLARSAIESARQGLQALADLKRQGRLPSDDADEH
EGELLTHLAQAAALGYDARHRMLNEKWAQQEELGHVSTEPSAMAAFSPLAARLQQPEPWQAWLAELLQYR
AALDEVCRRIKSPMTPKAPRASLKAMLPAVRADMGRCHEAMQTVRGVLIAIYARRLSRLAEQCGLPDVLA
RLRELLEADSHRRDEVAAAFTALDAVADERWSSTEHRLTPQALAQHKAVLEEYAEGLDRVGLQLCLDAAA
LIEMDDADHLWQTMLDLAQALADYRQALLDLCQSAGQGRQLPGAASATPEPAPASEPPPSPARPATAGGS
SRRKHRKPGKPAASPSAAVPAPRAVPVDTRTAAQKQADELLKRCPLDRATVAELGGDFIAIAKRLGKDTR
DVERLMNDSRRDAATAADFARTSVQGWFGERERLLQAKAKLPAGDERIAQLTDRLRALQRIERRVDTREA
DALKRDPQPRAPHLERLLEMNEIARVTAPNRLPSEGDNGDRGTLFEMRIQHKPLSNGDRPAPWFVHLHTS
KPVTADALRTLAYKDFTAVHLKTAREKNLGARWEEMMRALGYTDAKVHRATIGSALLGQLFAAAAGG
>gnl|CDD|469247 NF041355, XopQ, type III secretion system effector XopQ
GAAVLKRSRSAPPSLTAAQRTLLAQLGAEGGTRLTADEAAVLRELRFHRPAVPQDTILFTDPNKDPDDVV
TYTIGKQLQVEGFVRLTDVVVTLGDADVREQRARMAKGVFNRLGLPDVRVSRGQDYPMNAKQAKDHAKFL
QEGHALRAPPDEIHEDSLQAMRERLAQAPHGLSLVVIAGMTDANALVTAHPDLVRERVERITIMGGVEPD
KDADGYVQPDARAYNNTTDLDAARSFYRRAQELGIPLRIVTKEAAYKTAVPPSFYEGLAQSGHPVGQYLK
DVQKNALKGLWEGIQAGLLPGLDKAWFFRTFTARAGPQADAAQWGARKAISFDAIWPKVTKLNLYDPLTL
LAAVPGAAGMLFTPKAIQTEGFSVVELVGADEVKHPEKAKLLMSALAKAALA
>gnl|CDD|469248 NF041356, XopR, type III secretion system effector protein XopR
MRLNLFFRSYHRVAPEPLSPAATDTTPAAPGASSQHPLSQAPKTDAAQGASKSRRGMLASARKSLASLRK
QLPSMCMGSPTTEAVQTPGKASPAHTAAVAPARTQQMHVPQARVDERWQAPMPQPSPRRRVPTQTQAPQQ
MPPTRAAVRVPPRPSRAGQLHGWQRPAPSPMRRDRGGQPQHGAPASPPLPVTPSVSPTPSPPTQSRRLPS
LRNLNLQLAELNKQCYDIDKRLFMEDRTPTPEEQQLLETRAALIAQRNEVRDIQLDAMLVALAPMEDIAA
PRTTTSGLAMVQMDVMQHNRRALLKVRRKSLDMDLIARNYARAQRRLESLKESDAPYDKIRRLQRMMQGY
QNMLALQQIVKRTDDQLERLGAPRLMDSIPTTAEERRQAEQKERDAHQEAIDNGYY
>gnl|CDD|469249 NF041357, XopU, type III secretion system effector protein XopU
MDALRRALPARATASGAQRRHAGTLPPRAVLPFHLPQPPRISSPVQENPAAPHAEDHEDGSDELDFQVIA
DDGPAALQAAQRTAFIARAVEQARSSRDLRAMVRMADAAASQAAALQRLPGTADVIRALGGYRVPPEFQQ
MHRRLLDAAAAWRAAGEQYGAAQAIFSKLHPEADAGDARIHAAQAACEAAERQLLARHQVFWAARRSRFH
PALNSRLQADIQAHLVQCLRQACDYLDADAAAGPETLPRYELDSVLCRELAGMTRAAALRLECLQNGALS
VPAFPELPAADRALRQKEWTSRFIADAEALEAMARRLRAAWGDVLPDPLPETQAAADALRAAPGSAVRAP
AWREASLRRSFGLLLDSLGPLRSRAESTPVESGLLPGLRQLERLRRLCGLLHTAASLPRVLERSLQQWTA
AEREGSAATVATLRERATAQAQAHEREAQALLDEAFLALWQSGSALLGGAARSGFSHEVPALDLPQLASW
ARAAGALLKALPLPAAAEGIDMAVDRLPTELRLQGFFALANACELLGQPPAGTLSAMQRAERLRTVARSA
RSAARGAMAEPLRTLARQCDAAHVLCLSAAVRTHAAEVSQLFAQSRPTLEAAADRLGAELFQSWHFAFMP
ALVQETEAEQAPAPHASSAGDAPAETTLLESLRSIAREVDALHRPSIPMPQEMPPEAVQEHRCAKATLDA
MAYAARVSSTLLALWQETPSLLLPASASSRTARAAEFAQRAISVDLDAPVPGVENAAGTDAMHALSLARE
VRRRGLQMNVALKTMQQVFQARTNALQRVQDLRRLSPAKLNAKVEAIDAPFDSAIRLVTDREAELQSEIR
GDERDRAGKERQLLADWCSMLDWRMGLESILVVSRIYAAVQNKEIEGFAPGSRLAKALQMNRTTLHELIR
NLTDHNKKALQLQPLRENRPLMVAALGASLAAIRQLQDCDERTQALALPGMQGAGGSRAGAGGPKQAGQR
RRAP
>gnl|CDD|469250 NF041358, GntT_guanitoxin, guanitoxin biosynthesis MATE family efflux transporter GntT
MNLTLPSQYDFLPRFFRLAIANVLSNIMVPLAGLISVAFLGHLSEIHHLAGVALAGNLFDYLYRILAFLR
MGTTGVTAQAVGRDDREAMLLVGLRNGLIALVLGILILLLQYPLRELGFALLSATPEVKASGIAYFNARI
WGAPAVLLNFVLIGWFLGREKNGLVVLLSVIGNAANIALDYLLIIRWGWESTGAGLSYAISQYLTLLVGL
IFVCLEIKWQELRAVAGKIWDRSAIKSTFTLNGNIFVRNLIFISALLIFTNESAAMGTIIYAENALLLQI
IFLSVYFIEGLGFATETLTGNFKGKGASEQLVPLVKVSVGTSLLVGLSFAGVCVLFPQTVFGLLTNHTEI
TEQIDIYVPWLLPVLGFSSIAFMLEGYFLGLAEGHTLRNVSLIALTVGFIPLAIAAWYFHSNHILWLALS
LFMIIRMVALGVQLPRTF
>gnl|CDD|469251 NF041359, GntG_guanitoxin, GntG family PLP-dependent aldolase
MSEPIDLRSDTVTQPTPAMRQAMAEAEVGDDVYGEDPTVNRLEALAAELLGKEAALFVPSGTMGNLIALL
SHCGRGEEYIVGDQAHIYLYEAGGAAVLGGIHPQPVPNQPDGSLDLDQVRAAIRPDDEHFPRTRLICLEN
THNRCGGKVLPLEYLAAVRDLAHEHGLALHLDGARLFNAAVALGVDPADLVRPFDSVSVCLSKGLAAPVG
SVLVGSREFIARARRLRKLLGGGMRQAGVLAAAGIVALEEMVERLADDHANAQRLAEGLAALPGVAIQTE
PVQTNMVFFSLHEPELDAQALLAFLKERGILLSDVGERRLRAVTHYGITRADIDQAIDAIQE
>gnl|CDD|469252 NF041360, GntF_guanitoxin, guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF
MELKFKENDFQSFEAIPYLNEYFNNYPSDKYGGIGFENEKFLQFFAEVAHEHHLNNSLLLDFGCGPTIYS
IISLGQNCREIHMSDYLQQNLEQVKLWQQGKPEAFDWNPYLRRALQIETALNQNQPIDSFLDVTDEEIEE
RARLLQEKITSIRKGNARATNPVGEEGKALYEAVISCFCLEGVAEDLAEWKNLIANLSSIIKPGGLLIFA
TQIEADSYRIGDDYGRVLNLTEQDIVQTLLNCNFELGSIKTKELKGDPNHTEYDKFLMLTARL
>gnl|CDD|469253 NF041362, GntE_guanitoxin, guanitoxin biosynthesis PLP-dependent transaminase GntE
MTHNMSKSQALFKRAQKLIPLGVNSNFRYWGDGITPYIQRAKGSHLWDVDGNEYIDYRLAFGPVILGHAY
PEVDQAVAEAIHNGVMFAMTSELEVEVAERIKKMCPCVEMSRLACSGSEATQHAIRLARAYTGRELVLKF
EGNYHGFYDYMLFSTPYSLAETYGNRRNPTPVPSSSGVPKALSSLVLTCPWNDFEQLEKMLKTYGYQIAA
IITEPCQGNCGGLDPAPGWLEFLRKKCDEYGIVLIFDEVKSGFRIANGGAQEWFGVKPDMSAYAKAMGNG
YPLAMFGGKKEIMSIIGPGKVAHGGTYNNNMPGTAAANATLEILQREPVIKTIIKRGQRLMDGLKKILEE
YGVNPVAFSGHPTMFSYAIGVEKPVTCQRDVAESERDLYEKLVDEAVNKGIMPDHDPREPWFLCYSHTEA
DIDETL
>gnl|CDD|469254 NF041363, GntD_guanitoxin, guanitoxin biosynthesis L-enduracididine beta-hydroxylase GntD
LRLVLSAREAAEIDSLVAELAARYDSVEDPEFLRRAPVLAHELPRRLRRALNEFRLTEPSGACVISGFPV
DDAAIGPTPAHWRRRPDPSPTLREEIFFVLCASLLGDVFGWATQQDGRLVHDVLPIKGHEHEQLGSGSEE
LLTWHTEDAFHPYRADYLGLMCLRNPDGVATTVASVDDLRLDEEDRDILFEPRFRIRPDESHLPKNNATG
TEPPGASGLLRRSYERIEEMNRNPEKVAVLFGDPDSPYLRIDPYFMDPVEDDPEARAALDALIAEIDRNL
RDVVLQPGDILFIDNYRAVHGRKPFRARYDGTDRWLKRLNITRDLRKSRAARLSATSRVI
>gnl|CDD|469255 NF041364, GntC_guanitoxin, guanitoxin biosynthesis PLP-dependent (S)-gamma-hydroxy-L-arginine cyclodehydratase GntC
YNLGEGGPDFPTPEHVLEATKDALELLPGSLHYTPNSGSLELREAIAALYKDGYGIEVSPDQVLVTTGAS
EALFLYFHALLEPGDEVVVPVPAFQSLYEVPELLGGRVRPLPLSPENQGFRPDLEALRSLITPRTRAIVI
NSPNNPTGAVMTEAELEAILEIASRHGLIVLADEHYRFLPYDDGKHVSPSLYPGLSERVIALGSFSKTYG
MTGLRVGWLIGPKELIGAILKFKDYTTHCAPSISQYAALEALEQGPQERVKGWVRENVRRRDALVERLER
LIGWVCEPEGGFYAFPKLKDGLPSAAFAEELLEKAGVVVLPGSAFGRPGEGYFRIGFANSPTRLKEALER
LSRF
>gnl|CDD|469256 NF041365, GntB_guanitoxin, guanitoxin biosynthesis L-arginine gamma (S) hydroxylase
KKYRFSKEIKHQIKSLYRYDNWHGPLAVLEDLFVIGVAIALSEQSPYFYPLTILLIGSRQRALATLLHEA
AHGTLTKNRQLNKLLGTYFSGYLIFQSWESYRRSHVKKHHRKLGNPDTDPDYRFYISSGLYQTSSRKDFF
LRHLVKPLLLLNTPKYIKYLVKNRLLDDVSRRELFKLLLVQLILFIILSILVGGWKFYLLYWLLPYLTAF
QAITWFIELSEHFPMINVAKIDLYMTRNRFSHAIEHFFTGMHGENYHLVHHLFPGIPFWNLSKAHRILMK
DPSYAELNSGFGGIFFSRNNAPSILSQI
>gnl|CDD|469257 NF041366, GntA_guanitoxin, guanitoxin biosynthesis heme-dependent pre-guanitoxin N-hydroxylase GntA
MTVNEATARHSEKERKAPQAKGELEEKFREFILHPDFPCVGAKSAFAMDGVRFHEYDDMGSKETARALLR
DLADFVAAYDFESNDFTSFIAVFEGPRSTDELRFEKLLWKQLQRLHDLDARGHRWAPGVSDDPDDPNFSF
SLAGHAFFIIGLHPGSSRIARRFPYPMLVFNLHRQFEKLREMGRYDKMQDAIRERDIALQGSINPNLADF
GEASEARQYSGRAVEADWQCPF
>gnl|CDD|469258 NF041367, CheY_Halo, chemotaxis protein CheY
VLIVDDSEFMRNLLREILEEDHEIVGEAENGVEAVELYKEHDPDLVMMDIVMPIRDGIEATAEIKESDPG
ANVIMCTSVGQEEKMKEAVKAGADGYITKPFQKPSVLEAIEDVV
>gnl|CDD|469259 NF041368, Fbpase2_Halo, class II fructose-bisphosphate aldolase
MPYYRGDELADVYARAREGGYGFFASNVTEPDILVGLLRGAERADSDLVLQVSRGAAAFAGNGDPAAGLR
AFGAYLEALAERYDVGVFLNVDHVTLPDDEDFLDAAVESGIPSSVMVDASAEPFEENVERTREVVEMVDA
ADEDVLVEAELGRIAGVEDGIETDEAFYTDPEQAVEFVDRTGCDLLAVSVGTQHGVAKGRDLDLRPDLAR
EIRDALRDHGLDTPLVVHGSSGLSPEQVRELLDAGVCKVNKNTRYQYEYARTAADFYREHADAIVPPEGV
ADDRDTFFADSDWSPDKTHFDPRVVGREIRERIADVMADLAELSGSAGRSRYA
>gnl|CDD|469260 NF041369, Dhydh_Halo, D-2-hydroxyacid dehydrogenase
ERLGVHESVSAVFPPEALVEALSDLDVPVEIVGDDDELDDCDAVVTFAPREAFLDADWVHCIRAGYDRFP
FDAYEAAGVALTNSTGIHGTTVGETVAGYMLSFARRLHVYRDNQREREWSRPAWDEPFTLAGERLCVVGL
GTLGRGIAERADALGMDVVGVRRSPEPVPGVEEVYTPDDLHEAIADARFVALAVPLTDETEGLVDAEEFA
AMRDDAYLVNVARGPVVDEDALVDALESGEIAGAALDVFETEPLPEDSPLWDMDEVIVTPHCAAATRDYH
RDIAALVRENVERIRAGEELVNRVV
>gnl|CDD|469261 NF041370, desamp_Halo, desampylase
LVLAAAVRDALLAHAREGAPEDPREVCGVLAGDRDDPDTVTAARRVPNVAADPRTRYELDPAETLEAIER
VEAAGLDVVGFYHSHPESPPVPSATDRAQATWPGYVYLIVSPADGRLRAWRWTGEEFEELDVV
>gnl|CDD|469262 NF041371, Diadnylcyc_Halo, diadenylate cyclase DacZ
MSELRELLGDIVADVDAVLLFSPSGSYYERFADVDDVPVVVVAPENEVDAEQFVELPLEFEDVAERIRFG
IEGALDQGYVEEGDEVACATKLFGDDIDTVTRVRADEFTRSGVYDLFVNSRADPSVIRDVLEVAIELGKK
GQKGKPVGALFVVGDAGKVMNKSRPLSYNPFEKSHVHVGDPIVNVMLKEFSRLDGAFVISDSGKIVSAYR
YLEPSAEGVDIPKGLGARHMAAGAITRDTNAIAIVLSESDGLVRAFKGGELVLELDPEEY
>gnl|CDD|469263 NF041372, DUF166_seleno, DUF166 family (seleno)protein DfsP. DfsP (DUF166 Family Seleno-Protein) is a well-separated clade within the DUF166 family (see PF02593). The motif UC, in selenoprotein members, aligns to a CC motif in non-selenoprotein members. Members of this family appear restricted to the Desulfobacterales
QRIVVFQQNGSGERKIAGIRRYGGDRFDIEVVSIDDPLPPVLDDTSEYLPEEIEADLVLDFLKHPDLSED
LARLCVEQGIPVVASGKKITGGGVFTPPTUCGLPRQVGLGDYGERFGAPEIEVEVDDGRIKSIRVVRGAP
CGATWDAAEKIIGLPVDEAVTRIGLEVQFFCSADPAGWDPIYGKSPVHFAGDVHSAALKKALK
>gnl|CDD|469264 NF041373, HGG_STG, HGGxSTG domain
CGAKTRSGTPCKRPPVPGKGRCRLHGGLSTGPKTPEGR
>gnl|CDD|469265 NF041374, GDCCVxC, GDCCVxC domain
STLTCPHCGHQKEETMPTDACQFFYECESCGALLKPKPGDCCVFCSYGSVPCPPIQQG
>gnl|CDD|469266 NF041375, XopV, XopV/AopV family type III secretion system effector
PSLRRTASARARAPFFPDPSKRLDALFGSCQPARGKLLETEDGLVHRTPIQKQEIEKLPEGGWRVRINPT
RILVSTAPALRKAHRSDTAALAARFILTQADIDRIRLTPTFHEQTEGAAASSRSLAQRLRLDDLREKKVE
YKWNISANGSLIIGEIHPGVPLGEPMTTKQARKKKQPFAQGHVTLVGGQPWQEPWQSNRRIPEARISGTL
YYDEDGELCIDNDSGRFSEYADRTPEHLENVAALFKQYGLPVEVEWKKKPPIPLVN
>gnl|CDD|469267 NF041376, XopW, type III secretion system effector XopW
MKPNSIGNAHSPYSASSDTEVAGTSSRQQQSSGTSSQEQVNPALQGLASASRSRLNRRVRFGSWVGVQGE
SDPVGLDSRERKEKYPDAKYKSSSENREMKIEDNARKSAARLYEMYQGAPLPKETKKLLKEGNPAYTKIR
GSEKERKKEGALALQQYEYFARDARDPKVNYEHKKLRAPKNVRRSRLRELEAAAEKEQGGASSSGS
>gnl|CDD|469268 NF041377, XopX, XopX family type III secretion system effector
RANSALASGVQHASAAVSSAASNLWSLSDLRTMLQIHADDPAFLAILRGTDPEQPAPHTLASCRQQITQL
RELIEAAPGLEPRFRKQLLGDIKAVEDALQPLEHGTPAAGRALKSLANLVNLWPVLVPSPLLANQAKTFA
YTIATATKGVLSLSASALRPTADGLPFPLMGGQLGRDANEMHLYAALLNGLFLTTELPKKFGNPSVRHQA
EAVENNLGFAAGASVACAAIVLTPFLWNSLNALGNRLLDGASRLGAAAAQRAGLNNQAQQLRARLTPGQI
SAELRTQLNEIRAQLENGRDAFQQARRDFTGPGGGRELTRTLNAQCTHLLETLDRCSKRLSSALQLDQDQ
PASIPRQLRNQDFSSKLALALLGTGVTGSTVYLIQPDRIGTVDLLADTAIVTAVMAQSAFNKQATRQDAM
ERFKAMCGGSMVMALALGAEKLSKTFADKSLIEASSNSPYYAGAIMSLMAMTMPGPIARGAELAMNWGGR
QLMRLFTGPDGTPLATRVPSSPEELQERTQSTLAYVESLSPEQLQAYEQMVGESALQAIQDAGAAAQARP
SSSVTITEIEE
>gnl|CDD|469269 NF041378, XopZ, XopZ family type III secretion system effector
MPKFPLRPSTTTAGLPGNSETTAHAGKPSPHKQAHHKLHQLDPAAAEAELLAAQFDPAARVRAYLAKAAQ
ASPATPGPRAAPRKRKSLLRLARKAGTALGLARGAPVPHAELLRYQGTPAERDAPADPGDWRSLAAAQAA
ALAAAQDLNDAARIAVRKAAALEYLVALHLERLEEDLALHARRAGNLSDRANQLRRQQAELAALAALLEK
EIGRGSAQAARTEQQLTQTNAQLDQLTADALQMPAPAASARRPALRDLLSHLQAEREAEIEALRARLLQH
ERMLSLQRTHAERCQRHAQRLQQRLASLDATLEQARQSAHVNARELWQTAAQARTLRALLAALAQLRRAV
EHAAARATADEARAAASQALAAASDELLDALPGFRDEAACAALRQALRAWADGLDTAAFGDEALPPAGAL
AIALQALSIAAGGDAALALQALRALRALTWRELIPPPGVPGAAPTIPALEAAATRCVGLLARVPRGMQVL
GQLLRPRHEEAADPSREEAARIALRADALLRATPEADAALRTWLGDAQRAARHALHAADPAQALQACTDD
ERAAYHALRNGYESNAPGSAYARANAHLQMFAQWLHTAAGSAPAGARAPNPLHALPEGLEVGAATALPTP
RRRANEALEKAAAHLTGYLGARRAARPAGQLPSQAELAWQALAEYVQWAPEGTDRTTMVFDAKALARIEE
RAADLQRHFAASASRTPGGQPVAACHPALQSAWEALRAGRMTLPEALRLLQRGLLDHAEQAALQPSGASP
QDAVLASACRAQFHQAVAKASRLLHDGDPGRVTSPRALFDLLRDMLEHLEWRDRLRITGQRVWGLNAGPL
SAALAVAPSAFGLGLKLIAGGQHNRDASLEIYMGRTGLYLQIGRQSTRQVQAGAGISAGYGLPLGTEAAP
VGVTGAADWRWRGESGVENGVQIRVPRLGKGREPELRAQFLDMYEHLLRLAEQTPGDGGQPARRDWMHEL
LAHHPELSVGLIDGAQRSSSGTETSVSVSAGLRVGEVDGRPRRATLGASLGVKARQDNGRTQTTVAGYMT
TLYRDATAQSRVEVAARATASVQLAQWTDPSEGNAAPTPKASLSVSALDAGYARELHAAGSTTFCTLFMF
GNEIDPVRSDRATDFSDFAAFEREVRREWDLWANYGTGKLGGDVDEQLLYLVAERQLEHFMDQVRRFAQG
NKFAALFADKALRAEAAPLLDVLRALAQLARDAGDEAEAAAEDRAFDALLQQPAMWEPTLLLLREKGKLQ
RERGIDFFVKRQNNRIAEAMRTVGQWIPYEPVP
>gnl|CDD|469270 NF041379, OS_HP4_CYCXC, CYCXC family (seleno)protein. Most members of this family, called OS_HP4 in a review by Zhang, et al., are selenoproteins
TPPTLDPALFTGKVRRAYQAAKEIPEVLDQLPCYCGCDENPGHKSLLSCFVDTHGAGUDICQDEALDAYR
MYKQGKTIAEIRAAIDRKFG
>gnl|CDD|469271 NF041380, XopAA, type III secretion system effector XopAA
MHVRTASLRSYAHPHDPVAGDGSSPADRSIEIEAGPGSGTLSPTDATQARARPRPPSETTVCLADLLSIS
NQRPSRPEVIPAIVQVGDDEGVRDLPPQPARSGAQQPRLPNPGEVRDVESGLLMRDCSSRVAAFLGNLSV
VQELQQFDDVEFVGKLRNELVTEPGCPEPKTLLAAMSEKVDELRSHLDKQAATPEEAAFLAEARRYLEPV
MASFETDIDTLQHDASAAKRMFQGALTLLLYPLPLATLFTQKTGTYAAFNIASYTYTAIQLVSLMRRPTT
DAKLFRKHAINRHSLVFFISLIYAVPTFYAKASPLQRNAGFVAGAAVAQGTMMFGLRLGQDLMDSMRLRF
NSAFNRRHDLPDGFKEAIEGIVGDLRTGLGKVNGFVGEFQQDRRITPHMDRQLTFFKQDLSRIVTGLERL
VATGTRQESPVAAKSHTPGPLDAVRRTLEASFANNPDLKGKLALATVAFAVLGSNIALMRNDGLALPDFI
ADAVVSSTFLLCEALSPHVSLTGMNDSVSDTVGGMTIGLPFSVAALMNGYMDDPRGNPSGFIAGTVGYTA
AYMLFGRVAGDVLSKGLMATGGALGWGQRQAIRLGRSAMALGFDLVAGRSSPAAADVHAVAEVEMAGVPR
EPLFFSPSQRASAERTLVGTLEQIGDEWHDARDEWEGGSEETAGGDDPWVDAPAELPVQP
>gnl|CDD|469272 NF041381, XopAC, XopAC/AvrAC family type III secretion system effector
WKRALQAWCGADPAKAAHAQDGLWARLACRNAGNCRGRPLAADLRILNEQREEAVQRVLRALAHAEAGRR
LDLRGLDLSALPPGLERLRHLEHLDVSDNTGLTRLPESLARCRGLRRIDARNCFVTEVPSGIFALPNLEE
LDLSANFELRALPDSIAQAPALRTLRLSHCSLTRLPAGLANLPALKLLDLSHNPELHELPPGWRLDDVRV
RLAGTPLALMARLLRAPPWSPEQRGELGAHLDVLAKGWSGLQKRLAPGGAARLRVDRLRSGLSLTLRSDD
GGASAAWEDAARAVDGWAEEGQPITTERLLELGWLLGPDPNGDPQGVGRLRTQEIQRVPAGTPTGSRYPP
ARSLPAHLAAFEEWLEQGSAQVAAQDPLGAVERAALLYQALVSLHPFADGNGPTALLAMDWALQRHGLPP
VLVGEESRLPAAVFSGGRRASPEDLVAETVRGM
>gnl|CDD|469273 NF041382, Trx_VPGUxxT_one, VPGUxxT family thioredoxin-like (seleno)protein, type 1. Type 1 members of the VPGUxxT family thioredoxin-like (seleno)protein have a single site where selenocysteine residues appear
IALMGLLAAPMNAAEAETTDPETQPAELGSVHWYRNVDTGIELAKEQGKPIFLQFQEVPGUATCNGYAAQ
VLRNEILVAAIENLFVPVLIYTSKGTAHDAAMLKEFSEPAWNNPVVRIIDSEKKDVIDRINGVYKKRGIA
TRLLQAIDKAGISLADEARAVLKKVADGKEPSDEEAQEFRDAVSGKISRELDKSLDSAVSAYESKKFGKA
AELASKVRDDEKSEETAKADAAYLIKLINGRFASLKAKAEKLKAEREYLELFAALDEAEKHFKGLEGAEE
FFKAYSELKKDKAVKAEVKALEKLAKLEEKLAKAKTDRDREAATKSLKDFAEKNPGTRAAEKAEALLGE
>gnl|CDD|469274 NF041383, Trx_VPGUxxT_two, VPGUxxT family thioredoxin-like (seleno)protein, type 2. Type 2 members of the VPGUxxT family thioredoxin-like (seleno)protein have two sites where selenocysteine residues appear, with motifs EVPGUxxC and UFWxGE
ELGRVAWLRDFDAALAEAARTGKPVLLLFQEVPGUSTCKDFGRGVLSHPLLVEAIETLFVPVAIYNNTKG
ADAEVLKRFGEPAWNNPVVRFLDADGKDLIPRLDKVWSTAALARRMVAALEAAGREVPAWLRLLARELLA
RTRGLERATFAMHCFWEGEAELGLLDGVLATRAGWIGGEEVVEVRFDPEVLSLADLLAKAKAEGCARRVF
TTTDAQLKVARKVLGDRAFRLKEYRPAKDSDQKYYLRRSPLRFLPLTPAQATRVNAALPPYRGDAKRYLS
PRQLALL
>gnl|CDD|469275 NF041384, YHS_seleno_dom, YHS domain-containing (seleno)protein
GVAIKGYDPVAYFTEGKPVKGSAEFTYEWKGATWRFASAENRDLFKANPEKYAPQYGGYCAYAVAKGYKA
PIDPEAWKIVDGKLYLNYNKSVQKRWLKDIPGFIAKADANWPK
>gnl|CDD|469276 NF041385, Dggglyphlred_Halo, digeranylgeranylglycerophospholipid reductase
MTDRFDVVIAGAGPAGAQCARDLAARGYDVLVLETEPEDEFPRQSNKSTAGTFPSMMASFGIPDDVVMNF
TDDVVLESPNDHYVQEQPGAVLEFADFKRFLVEDGREKGAEYRFDARVSKPIMEGGEIVGVRYNGDEEVY
ADIVVDATGPAAPLAKALGVSDLERENQAIGIEYEFEGVDVDHPGYADLTDAMMLRLDHDLAPGGYSWIF
HTGEDTAKVGLCYIQNESHREYAKEGMTIDDYLEYWLDTDPRFANAERIEGKQHRGSAHIQMPGSLSTDN
FMAIGDTVPTIDPLWGEGIHKGMKSGRAAAITADRCLTPGEPDTSAENMSVYDDLWHEDVAPKMRARLLM
TELLYLAPNERYDRLMRDLNRLDDDTLAKANAGNKLAIAKLLHLSDLPLLARFAR
>gnl|CDD|469277 NF041386, dihyfolred_HdrA_Halo, dihydrofolate reductase HdrA
MELVSVAAVAENGVIGRDGELPWPSIPADKRQYRERVADDPVILGRRTFESMRDDLPGSAQIVLSRSERE
FDVETAHHAGGVDEAIEIAESLGAERAYVLGGAAIYELFQPHVDRMVLSRVPGEYEGDAYYPEWDEDEWE
LVEETEYDGFTLEEWVRA
>gnl|CDD|469278 NF041387, DNArepr_NreA_Halo, DNA repair protein NreA
MRLDEYIEGLERDERAERRRLAEEKSYEITDYLEDVEDRFEETVQGDSLFGSTSPSIFVGRSNYPNVSTG
ILSPVGDEADAAEFATSGEWYDEGVSIDDVFQRRTGLLNSTRSANVDVADAWDGFVGVQREVAIADRPVD
VEIGLDGRPDLDLDVSLDDVATPTGPRARARSADLTENPHVPRPVEKTLEDDDWRAEGAMTYLYRRGFDV
YDINTILSAGALGQGENRRLVPTRWSITAVDDTVGQFLRGQIRNAPSVDEVEVWYNEYLGNRFWVILAPG
QWEFELVEMKAPGSVWNPDPEAGYWLASDYEGYEGRTGYVEETAGAYYAARLGVLEHLAERGRQAKVLVL
RHVSDDYWGPVGVWQIRESVRNAFEGEPGEAETFHDAVRGVAPQLPVSLGRLRRKSTMVAGLQSSLSDF
>gnl|CDD|469279 NF041388, DNAstvprot_Halo, DNA starvation/stationary phase protection protein DpsA
SVRQEAGTVEENALRLDAEKAEQIVDALNTDLAATYVLYHQLKKHHWNVEGAEFRDLHLFLGEAAEDAEE
AADELAERAQALGGVPVSGPAALEEHAPVEPEGEDVYDIRTSLENDLEMYGDIIESVRDHIELAENLGDH
ATAELLREQLVELEEDAHHIEHYLEDDTLVL
>gnl|CDD|469280 NF041389, dodecin_Halo, dodecin
MVFKKITLIGTSEESFEAAVDDAIDRAEETLDNVHWAEVEELGVEIASVDGREYQAEVEVAFELE
>gnl|CDD|469281 NF041390, TadE_Rv3655c, TadE family type IV pilus minor pilin. This HMM somewhat overlaps with Pfam model PF07811 but extends coverage to include Rv3655c from Mycobacterium tuberculosis and related species. Rv3655c belongs to a cassette that produces an Flp-like type IV pilus structure, and has been ascribed an ability to suppress macrophage apoptosis
VEAAVALPALVAVLALLLWGLAAVAAQIRCVDAAREAARLAARGDPPAARAAARRAAPDGARVTVSREGD
LVRVVVTARAPGPLLPGVTVSAEAVAAAEP
>gnl|CDD|469282 NF041391, DPhHxTase_Halo, dolichyl-phosphate hexose transferase
MGTYNEEAAIGTVLDDIDRVTDGRAEVVCVDGSSDRTPEIAREHGARVIEQEPQGYGVAVREALLAADRP
VVVTTDCDDTYPMERLPDFLDLINEGYDVVSGDRLYHGAETMPALNRLGNHAFAALASLLLGRRVHDTTT
GMRAYRRDVIESIEWTENTGLSAELLLRPLMRGYRVREEPIDYDERLGETTLDPFSGGAEIAGSILRVCL
EER
>gnl|CDD|469283 NF041392, XylDh_Gfo6_Halo, D-xylose 1-dehydrogenase Gfo6
LDEFTERDWQTTTDGTVRFALIGLGWWTRDVAIPAIESSDLCETTVLVSSSTEKAERVADEADTVEHGIT
YDEFHDGAAADAYDAVYVCTPNALHLEYVETAAELGKAVLCEKPMEATVERAERMVEACEDADVPLMVAY
RMHTEPAVRRARELIRDGFIGDPVQVHGNNSQPLLEMIPDPDQWRLDPDLSGYGTSVMDLGIYPLNTARF
LLDADPVAVQASMRSEHEAFADVPDERASFTLEFEDGVQAVCTASQNAHEDTHLRITGTEGEIELEPAFH
GERELRLSRGDTTVDVEFEQVDQMTEEFDYFADRVLSGEEIYPDGRHGLVDMRAIEAIYEAAETGETVEL
>gnl|CDD|469284 NF041393, Frdxn_Halo, ferredoxin Fer
PTVEYLNYEVVDERGWDIDDDDLFEKAAAADLDDEDYGTFEVEEGEYILEAAEDAGYDWPFSCRAGACAN
CAAIVVEGEIEMDMQQILSDEEVEERNIRLTCVGTPATDEVKIVYNAKHLDYLQERVI
>gnl|CDD|469285 NF041394, GtaseAglG_Halo, glucosyl-dolichyl phosphate glucuronosyltransferase
MKVSVVVCTYTMDRYDHFSEAVESVLAQTYDDVELVLVVDGNEAVYDRVREDYGDRENVVIHCNDENRGL
SYSRTKGAELASGDVVAFIDDDAVADPDWVEELVETYEETDAVAVGGKMTPEWVAGKPDFLPEEFYWLVG
VTHRGFAEGGEEVRNTFGSNISFRRDVFLELGGFDPNIGRKGDKNLQAGETELCARLREEYGRGVVYNPD
AVVAHKVFEYRTDPRWLLDRAFWQGYSKRAMETLVPDSSGEESEFLKDLLTEFVPDRLRKLVRSPSLAQV
KQLVMLFVFTAAVGLGYLYGLLKW
>gnl|CDD|469286 NF041395, TranRegLrpA1_Halo, HTH-type transcriptional regulator LrpA1
MSTESTEDRILSVLEEDAQASYAEIAERADVSKPTVRKYIDQLEDEGVIVGYSADVDPKKLSGQSIALVG
IDVESEQYVDATRALKELDAVEALYTSSGDHMLMAEVRAPDGDALGDVISDEILTIDGVTAAHPSFLQER
LK
>gnl|CDD|469287 NF041396, TranRegLrp_Halo, HTH-type transcriptional regulator Lrp
MTYENLDTELINALLGDGRASLRSLAEELDVSVTTVSNHLNDLEDEGVIEGYTPIVDYDELGYDVTAILQ
LKVEGSALPDVTDRLREHKQMISVYEVTGDYDIIAIGKFRDTDDMNDQIKELLSDADINESNTSVVLNAV
AENEQFELD
>gnl|CDD|469288 NF041397, TranRegGlpR_Halo, HTH-type transcriptional regulator GlpR
MLPEERKRKIVELVTERDGCSVEELADELDVSKATIRRDLRDLEDRGLIERSHGGAVPVTSVGRERSYGQ
REVQNLEAKRAIAERAVEEIHDGQVVFFDAGTTTMEVAKRVPTDGSFLAVTNSPLLALELAERDGEVKLT
GGTLRPRTRALVGPTAESFMERTNFDLLFLGTNGIDPDGGLTTPNEDEARMKELMVENAKRVVLVADGSK
FGERSFVRFADLDDVDLFVTDGALPEELREAFEEAGVEVVDVD
>gnl|CDD|469289 NF041398, GluDhGdhB_Halo, glutamate dehydrogenase GdhB
ESALETARRQLERAAAHLDIDPNVVERLKHPTKVHEVTVPLERDDGSVEVFTGYRAQHDSVRGPYKGGLR
YHPEVTRDECVGLAMWMTWKCAVMDLPFGGAKGGVVVDPKDLSEDEKERLTRRFAEELRDVIGPTKDIPA
PDMGTDAQTMAWFMDAYSMQEGETIPGVVTGKPPVIGGSYGREEAPGRSVAIITREACDYYDRPLDETTV
AVQGFGSVGANAARLLDEWGATVVAVSDVNGAIYDPDGLDTHAIPSHDEEPEAVTTDAPAETLSNEELLE
LDVDVLIPAAIGNVLTEDNADDVQADIVVEGANGPTTTAADEILEERGIPVIPDILANAGGVTVSYFEWL
QDINRRSWSLERVNEELESEMLSAWNDVRAEVEERDVTWRDAAYIVALSRIAEAHEARGLWP
>gnl|CDD|469290 NF041399, XopAD, XopAD/skwp family type III secretion system effector
CVSMARDNVLAERNGAGLALPFLDGSVDAQTNARRLDKYLQKLGSASRAAFLPRDLDRCAELAAQYLVKT
GWFEGAPLWQYAHLANALSKHPGGPACMEAIAWIAGQVSQADDLVGLDGKALSLLANAFSKNPDSGRCRR
AVARIARHLLRDRRALQELNAQSLSLLLNAFSKWPDNPDCRAAAHALAARLARDPRLRSAMDAQGVANLL
NALSKWPDEAVCREAALALAGRLAREADLRLALNPQEVANALNALSKWPDEEVCRAAAVALAGRLADRPG
LRLSDLNPQGLANALNALSKWPDEPVCRQAAVALAERLARADEPRLRQALDAQEVANLLNALSKWPDEAD
CREAAVALAERLADDPDLRRALSPQELANLLNALSKWPDEADCRAAAVALAARLARGLRQALDPQGVANA
LNALSKWPDAPDCRAAALALAARLARDPQLRDALDAQGVANALNALSKWPDAPDCRDAALALAGRLADDP
GLRQALNAQGVANLLNALSKWPDNPVCRAAAVALAERLARDPGLRKALDPQGLANALNALSKWPDEPDCR
AAAVALAARLADDAAAGLLQALDAQGVANALNALSKWPDEEVCRAAASALAERLADDPDLRQAFDAQGVA
NALNALSKWPDEEACRQAALALAGRLAEDADLLSAFTPQGVANLLNALSKWPEEPACQQAAVLLAERLGS
AGLPWRQFTMRGLAQIANALARLLMRAEDEGEIQALARARLQALAGHLDLHPERLESASALDIGVLFKAL
ASARLQRDLRPLARPALERLSALCRADGLRENNLETMGNLCAGLLPLARSPELSLRHRRQALRLLNDLQP
IVARKIDAYLRAGGAEASAGPEAHATRCPALTFYQVLKAYAVVARQWKPRYVEGDRQDLRQRREELKAWV
DETLERTREAIEADLGEMSWNLIAQIEAGDQVLDALDLRMAKDAATITQAHPPTRFDLAQVRRSMRTVPG
RPRPPAPGAGATTHVVVDMQGRELSTNATEPDKPYSLFARLTGLPLVEVQLPGKLSAFMLARTFNYQGEP
WRFDLFGGSRLKRGRSTVSSLILAGAKPSASLLPAIRYADTAPGSALMQLARKLAPQREDWSRMQRALLE
MVPHDHVVEGTLRLGLFPDVPGPEHPFKLTGPDGTPIALCPNDGCGFLKAEVALRIPAVRKHYEAWHAVR
AGQATQEQRVLLAGEGRPSSLPPQALQHYPRDEAVLEEAREAMQRRLETLQPDGLDPLTLYRLLTSGGYQ
GQRVRAVPSADDKLHLPTQKSQAFDRAGGPLLLGKPPYDKENLLPVPAERVATVAQGDATARFLDQCFAI
QYSYTGFDDKSGADAPMLHSKGMLIVVPDEMWPADFADRDLVCSKEDLKTLSSWTTGRDRDALPRDMLST
GSLRVKDIFAPGRLGALPIDELRKRDMDTDGDDAFVYAGYPKLAAHISRVMDDREQRRGRQRSFKPPKTA
TPAIDESGRYQAGRASEILAAQRGQKLLGAASTLARRFLAQPDELREAMARRMMFGTYDGIERELRNGLR
QLLEGEQRDPQVLQDLREQAREAIERAHHPEAREAAELLHAQLEALAAGPAAQSAAPALSAALAEAFPGL
AEAYAAATDPRARIHAILDNYPVCRLSHEQFPDGQPGYVPGEPELTMRNLFTLAIKVGTDALKSDTGTAL
FAKIVEACERSERSFPERVRSVPYTKSTARALRDGRFDPEQTKELLQDNPTLAAGVMEDALEALQQAGLL
DPPPPPAERLRTLTPEDIAQRAQALASRARQAEPRITDMLQRVAARHGGQLAGLEHRLKSEGSLTEKLTQ
LMALKQQTLEEAAALVNDALRYSVVLPPQDFTAGYRRILAALDDQGHARVKLTNWFTKRRPTFKAINVTL
RSPDGARWEIQFHTPETFALKERFHDLYKELQALRLQGASREEQRELLAPAREAFRAVAIPPGCEEIDDW
E
>gnl|CDD|469291 NF041400, XopAE, type III secretion system effector XopAE
LSLIHTGLQSLPDSLGQLRQLRHLQVAGSPGLKRLPPSLTRLPNLKTLQLTMLPLEELPADLGRMQSLRS
LTLGGGHYARLPASVVQLSRLTELSVSHSSHLRELPENIGLMQGLRSLEVSSNSKLEQLPGSLTRLHRLE
KLNLSSNRRLAQLPEDIGQLRGLTELSLKNCAALRHLPDSVGDLSQLQLLDLRGTGLQTLPQSLARLPAT
CEIKVPDHLRGQLLQIRNPEAAQRAAQRLADRRRRPAVPAAEQAGASWNRVPEFTRALRSIDADLGERFD
KWTQGLAQNAMIFGAPITPADMPLLDQVVAEAIRSPEFRSSFGEFLSDHTVKTLNMDGMTQVGGGGPAVR
GDVKTAFSEMLKHKLMHTQDQETALSLLQEAIQNPDLGLSRNRLLRSRNELTGRAQMWPPLRAYISMHDV
EGKAAQEAATTWAMAQFDEAEEGVIGEAEAKQESEQAQANANRFIEQRARVLLREWRI
>gnl|CDD|469292 NF041401, XopAF, XopAF/AvrXv3 family type III secretion system effector
YQAARSHPGNPIKDRSESAFPAVRVYDADAGLDRSFELDRSTTVKVAGFNYLVPNDAETRHLYSTGTSQP
NVLVVTDGMGACIAVACAAERIDPGTGERMPGAKVRVFHVLPFNRQELAPGEVLASIRRYVEKTRRQGLT
VRAAMHGGDSDSDSSVSTADALRALFQGLGVPVEFDETCEGRNGNTPLGAVIEDDHSVRFVTHLV
>gnl|CDD|469293 NF041402, XopAG, XopAG/AvrGf1 family type III secretion system effector
RAMKYALGLAGAAYAYDKTANDFFLSTTSLHDGKGGFTSNERLDKAQEKAEAYYQRYHASSPEEQRLNNR
PLNPIRLCGNNQFVTMTDYRAATKVHLARLVNTEEARQSLALNLACLKGERVKPECVAKYGPPQVPKDFD
LTKSALYDKKNKYSLTGVPNEETGSYGYTSRSITHPFVNKGYKHFKDAISSERGLTPKQCVESLEALLEK
DDTLSEEAQFAAGQAILNFRQVYAADEHWGHAEKVVMKTLAEHGLLSQAETDKIDETLMFEDPSKGVLKR
NTSVAGPLLHKLDTRLQEFRLKKDPEALEDLKHMEVANMKNLPIAHFKLNEQGNGFEDCSGLGDSFTCAN
AVACINHARLMSGEERLSKDDVVVLIGCLNAVYDDASGIRHTLHEIARGCFAGAGYTVEDADDFYADVCK
NAAEEFYGGKNL
>gnl|CDD|469294 NF041403, XopAH, XopAH/AvrB family type III secretion system effector
LPGPQAHSRLSPEQQSLVGVARWPDPRYNQSDTPENMEYGRSFYNASREAGARIASGQIQSFRQLWDFAT
DWRLSRAGADAPQTFGEPRDPGYPRVFTTPLTGQYAYIKDRFRNRKDGELEIYDGQLLPPIEHKVFRQRG
KINGEPIPLTTISLSTDPDAHRLAEPYSRLRHLGDSDAGEPNMISHTDAEYVPKIMQHVESLYNQAIDPR
LSDSEALKTLAEIHWWAAHAMPDKRGSAAKAELCVRAIAQAHGIELPPFKHGIVPDLEAMTTSREDFVKR
YSSFFE
>gnl|CDD|469295 NF041404, XopAI, type III secretion system effector XopAI
PLPELSTSDLEAEKQRLWQRIQSEGANFRSTPEERAQFKTAFLSLWTEQYRPSPEARWNEMAERMASLKR
SHPELRHMATEDLIALRAWTATDDYQIVQDVLEAGAPPTAEGLAYAKCIISALHSLPDSYSHQGTVFTGE
DQSDDWVRERHREGQTTTNRRFFATSETKEAAWQGMPVEWETNSTNGKRISMFSEHPNEQEVLFPPGTRF
QVNRIEESGTPPRLKIYQSEVA
>gnl|CDD|469296 NF041405, XopAJ, XopAJ/AvrRxo1 family type III secretion system effector zeta toxin
TDEIFTLGELPSPGPLRWDYLANPENWHPERRQLHDRLIGEAKTAALTLAERIERHGHPPTLFALRGNTA
AGKTRTATKTIPVLAKALKDSDGEGCINPDPFKASLAKAPGGVKISSAQVHAESCVLADRVEDELRLQKT
GSGAIASLVVDKRLAGAHEIDAYLKLAEETGRKVELCDIDAPLERSLVGVLQRKPEGDDPRPPYVAVAGG
FSGVRGNRLDVIDGFISNPSLGSYKLFGTDEDGKKVMVASVRDGELSIPDTQLYERVTAPPSAVAGDVGD
TVIDTALIDRLVNGIDDPARAAKARAALERYQGMTWSQALDAHS
>gnl|CDD|469297 NF041406, XopAK, XopAK family type III secretion system effector
DRAPYRDLERQYADLFRTREIQAVPEASDVEAKRVLDVDMDECEVINTSRDGFDSIGTKGLGPCIAICAR
GKTERGETILGLYHYSGIEEPEDALSELDDKMREKGAHNIEYYLVGGMISEDEDLGSLETERNLLALRNQ
YNIQGVRLHVSEGERDGEDNSVNLVMTPDKIYY
>gnl|CDD|469298 NF041407, XopAP, XopAP family type III secretion system effector
IDAATVDLASAIAQVDLPSAQSRGQDPQLEMRRREVLECMRACAGEAYTADLAAVADIGGLHFDAPMSTP
RLKLWEGATDDAIAVVLGFSGTRMDDADDLLCDLKSQIARPHVNPLDERLPTLGHVGAGWQERWQSEARA
PRADGAVMADVLARYAARARDSGKALSVSVVGHSLGAAVATLAGFDIAHFLRAAGASGKVSVYAFNPPRL
GQAGIETRYRRALRSEDSALRFTLRQFTRALDPIQSVPLFMHHPHWAHDAGADGERAGSASGDRFAQFVT
YTDRPASRVNLADNHELTLWKPYILSGISPAELQRIF
>gnl|CDD|469299 NF041408, XopAU, XopAU family type III secretion system effector serine/threonine kinase
ADADRPETSTAPAPEQSDPPAPGADHPLNLLEKRRSSSGEGSLADESLRLEVLPPRLQASRALSRSSSSS
SSSPTTPGSARSPRSTPYSGLPTLASLLDPPTPGSLELPSDPSSASQILRNERRLTRDMRTRLQDVVLSP
RLVKSLASNSIRPELIAKLAALKPGALEVENGFLRVRLETAHAGPDQSLPAMQPLGRGASGTAYAVRLAE
DLWRGGENCGRDFVFKAMLRTDPQDPIPPTLYDPDFQQDASALKEAISARKAKIIQEYQMTASLDATSRV
MRVYGLVQIDNVFGILLEKIDGITVGNLIGRARPALEQGAITAPEYLDMARQLIADVLIAIARCEDEGVV
HQDISHNNVMYDRSEKMFRLIDMGLGREEGQPRRPGTPGYIDMSSPVADHKRDVYSAAQLLVHFLKRPDY
HMGMIGISRAKTVETFPFMDALRALPPDRKREIVRFINRMIQPETEERATAEELLRDPFFEETALPPRDR
VHATYEKL
>gnl|CDD|469300 NF041409, XopAV, type III secretion system effector XopAV
TSATRRGARDLQQGLATERDAGPSAQAGDPHANTQLAQDLPRRPVREAPLRAPQEPTGVRIANVVRTVAG
AGAAGAGAVFGIAALQAPAAAAYGYATDDLYYKNLAKVSGIAALAAAAATGGLKAIERLASRYAQAQAQG
VVTKAGRARELGTTEACLDAAVEMVTMPDADRPGPEMNEGERNALAKDLLNLATAERSRLPPELWNAASG
VGDDAHALVDRLLAAARARAAAEASASS
>gnl|CDD|469301 NF041410, XopAW, XopAW family type III secretion system calcium-binding effector
MISSVSSSYSSYTSTSSSSTSSARSQQFQKQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFS
DLDSDGDGSLSSDELAAAAPPPPPPPDQAPSTELADDLLSALDTDGDGSISSDELSAGLTSAGSSADSSQ
LFSALDSDGDGSVSSDELAAALQPPPPPPLFSLSSQGSSSSTQPSDSSTASSSSNTTEALNKLIANLSKQ
YQSLDNSASVGSLLNVA
>gnl|CDD|469302 NF041411, XopAX, XopAX family type III secretion system effector
MRITNDDYTPIELLAELLSRRTSTAEDTARFFEEEKSSHDWLVEAWAERLDVILNSFKRYGTDVHETQSI
RDNGVDVLLRFEDLGGSRRVGFQIKSNREADRDKKKKEPEESMVGTLKRQAFEARKSGKVDEWWIVPCFD
LTKHSKLVQAINSELIPGKPLPWPIRVVDPREAASFLSMSDAEIDAICTLLLCRDDEVLKAARSEVIDLS
PFAQKFVLETIFDALEGEREISQDDIFRITDDDEELDEIADVLEELEDSGFLEYDSEESYVLKPTAFPGL
CALYFEGRVRHELSPDAAAEFVRRL
>gnl|CDD|469303 NF041412, XopC, XopC/Rsp1239 family type III secretion system effector
MKTSGVSKSHDLSQFPEGDLTPEILIPVGRNSDIPKDAALSAELKGLRPLNRTPSKVPTDNLQAVNKMIA
ENRENPVGKGAFRLSTQQLGSAKRMDSQAYHQRDETKAPFFFSEFATEKPSLSMVKSLHQGKQDYYAVRH
VGKRGRDLFTDEPIEGENSKIGRLKTSPLLSTQSSGTRAIRGFAATATIDQSRGEYIARLHQHVVNALGG
EGGVVHLVRPSRDPYVEDSTLNFFTFCEQAELASSLNALEAKAAKQNGRSPIVFTDNKSLVGLSRTSRTE
ASPIGRLVQQPFFVTSELRAGDKVVIADDHIQAGGSMLAMEAAARGAGADVLAFATLSTHPFSPQLTMSP
EVRAFLDQTLAAWDPENLVSDRLAQLGMPRDRLTNSEAMILIAYAIDPADTSAVEKFEAMQANFFERAHL
HNVGIDPDAPDAAEQMQQLRARQEAAGTDSARAFIDNARVLEGEHDSLIPILKEKPKSPQEIVQELDQVS
RSSRSSVQASEVKQVVVLDWDDCLRDEKGLNYQLMHNALAIAAREHASTLPELGEAVSRLRSRMESGQPA
GEGAPLLMKSQEDFTSHLMANPSIFKRHIVEDFVRTMLPGLSPDKAKSIVNAVYTQFTRQYKRLTQPQKK
KYLRDVPFPDVQFSLMPGAKELLEKCRTADSRVILISNRGHGDLEDEVNHLGMMHYFDVVSGAPEVTRPK
PDAQPAQMPEDLQKRLTQALRGDDEEALRQVLAEAAIYAHPDTTVIGRIDKKPDATRLLQSLEHLSVQPD
VPITSYGDQPSDVKQLQTLAEQGRHLEGVIINPQRDDVGQQIDVDGVPTRVVRSMEEL
>gnl|CDD|469304 NF041413, ArsR_Rv2640c_fam, Rv2640c family ArsR-like transcriptional regulator. Mycobacterium tuberculosis has several ArsR-related transcriptional regulators, including Rv2640c, a member of this family, and Rv2642, encoded nearby. Members of the Rv2640c family have two invariant CC motifs, one at (or a single amino acid away from) the C-terminus
MPKALPVIDMSAPVCCAPVAAGPMSDDDALEIALRLKALADPVRVKLMSLLLTADDGEVCTGDLAAAVGL
SESTVSHHLGQLRKAGLVESERRGMNVYHRARPDALQALCGVLDPNCC
>gnl|CDD|469305 NF041414, ArsI_CadI_VOC, ArsI/CadI family heavy metal resistance metalloenzyme. This family belong to the broader VOC (Vicinal Oxygen Chelate) domain family (see PF00903), which includes glyoxalase I, fosfomycin resistance proteins FosA and FosB, and dioxygenases such as 4-hydroxyphenylpyruvate dioxygenase. Members of this specific family include none of those, but instead include CadI from Mycobacterium tuberculosis and ArsI from Bacillus sp. MD1. They have an invariant CC motif at about position 95, and have poorly conserved C-terminal extension regions that nearly always contain at least one addition CC motif, often several. ArsI has been characterized as an organoarsenical lyase
RVQLALNVDDLDASVAFYSKLFGVEPAKRKPGYANFAIAEPPLKLVLLENPGAGGTLNHLGVEVESSEEV
HAAIARLEEAGLFTFEEIDTTCCYATQDKVWVTDPDGERWEVYTVLADSETFGTSPALAAGAACCATAAA
SSCC
>gnl|CDD|469306 NF041415, halo_CC_star, halo-CC-star protein HcsS. Members of this family average about 65 amino acids in length, and nearly every members ends with a double-cysteine (CC) motif at the extreme C-terminus of the protein, suggesting binding to a heavy metal atom. Members are found primarily in the Halobacteria, a branch of the Archaea. The gene symbol HcsS (Halo-CC-Star-Short) shows the similarity the adjacent HcsL (Halo-CC-Star-Long) protein. The greater context contains homologs of arsenic resistance proteins ArsD (a chaperone), ArsA (a transporter), and sometimes ArsM (arsenite methyltransferase), suggesting the HcsS and HcsL act in arsenical metabolism
EDVLAAAEALGEELAAAQSESTEEEFESLLRECNEAISEETGIDYGDVCDAGDCC
>gnl|CDD|469307 NF041416, halo_CC_star_2, halo-CC-star protein HcsL. Members of this family belong to the broader YlbF family described by Pfam model PF06133. Members occur in halophilic archaea, and are the larger (HcsL) of two related small proteins that have the CC-star terminal motif (Cys-Cys-COOH). The rare CC-star motif seems most common in proteins such as HgcB that interact with heavy metals. The gene symbol is represents the descriptive name Halo-CC-Star motif Large protein, while its partner is HcsS (Halo-CC-Star motif Small protein)
AVEAKLQEFIDTLVESETYQEFVEAEEALEADEEAQALLQEYQQKQQQLQRGGFDESLMSELRELQTEMS
ENETIQRHQAAQEEFVELLQETNDVISEQIGEEFAQSTGGGCC
>gnl|CDD|469308 NF041417, ArsA_halo, arsenical pump-driving ATPase, halobacterial type. Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms
AREIVEPRGEDTEFVFFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFGQSIGHRVTSID
DVENLSAIEIDPDAAAEEYRQRTIEPMRQLLDDEQLKTVEEQLDSPCIEEIAAFDKFVEFMDEPEYDVVV
FDTAPTGHTIRLMELPSGWSEELEKGGATCIGPAASLQEQKEDYEKAIDTLQDDAQTSFVFVGKPEDASI
DEIERSSKELADLGIKTSLLVINGYLPESVCEDPFFEMKREDEQEILEEVEREFAMQPIATYPLQPGEIT
GIDLLADVGEVLYEGKEPTVDVAVITEEETEETSPSETDKEAVMELLRPQKDTRYLFFTGKGGVGKSTIA
STTATYLAEEGYETLIVTTDPASHLQDIFGTEVGHEPTKVGVENLYAARIDQERALEEYKTRMLDQVEQS
FDKDQIDVEAAKAQVREELESPCAEEMAALEKFVSYFDVDGYDVVVFDTAPTGHTLRLLELPSDWKGFMD
LGSLTKEASDVTGDKYDRVIETMRDPERSTFVFVMYPEYTPMMEAWRAAEDLRNQVGIETSLVAVNYLLP
EEYGNNAFFESRRKQQQKYLEEIRDRFDVPMLLAPLQRDEPTGIEELRRFGSEIYGA
>gnl|CDD|469309 NF041418, MbpA, mobilization protein MbpA
KTEKITFRCSILEKKLLKERAARCGLSVSEYCRALALGGRPRERLTEEQIELLRELAKYKNNLQRIGNYF
GGRNPKELAEEVVALINEIKKHL
>gnl|CDD|469310 NF041419, CC_star_Cory, cory-CC-star protein. Members of this family have the CC-star motif (Cys-Cys-COOH), that is, a pair of Cys residues as the final two residues. A founding member is WP_085549354.1 from Corynebacterium pollutisoli. Members of this family typical are encoded next to an ArsA family ATPase (e.g. WP_085549353.1), suggesting a role in heavy metal metabolism, and predicted carbon starvation protein A (e.g. WP_085549355.1)
RRFEAGLDEFYAAPYRRTLARAQRDEDDLFMLLVFSEALGVPNPASYYTLELYPYLYEDFHEWHQRMGME
RSPLDGIRCC
>gnl|CDD|469311 NF041420, MbpB, mobilization protein MbpB
MIGKGKSISHGVAALEYDLAKEIAGQAAATEICRHELYGCTGAEMVQEMKPYFADFPNVKNNCLRFEVSP
SIEESATFTDADWAELGNDFMQRMGLMNHQYIIIKHSGTESKKEQAHLHILANRVSLSGELYRDNWIGKR
ATEAANAIARERNLVQSQDIGKANKAEIKEAMDGVLKKMQGFDFAKFKEELGKRGFKVREARASTGKLNG
YYVTARSGTEYKASEIGKGYTLAHIEKTQKKLKYNSMSISYGNTLTPGKG
>gnl|CDD|469312 NF041421, MbpC, mobilization protein MbpC
METPSNPETEDSTYKQGQYSPRKRKDTTPKVNPQLAVELVYQELKRVEVYTKRIEDATAKKVQIDGKSLE
SAENRLKNVLADFERQGNRMKNGGYVDKRVSFYSILCAVISLLFACLMCYLWVDAAKDRDNYKQYYEYYQ
QQMNEQKG
>gnl|CDD|469313 NF041422, VirB10_subf, VirB10/TraB/TrbI family type IV secretion system protein
MTDTPFPEQKEKTAAELEREARARARAELASAAPEEKTPPGQPEVNKLKKRRKGRTLIVLALSLVALIVL
AWGGDWIYRALLSQPEKTADTAPPPSSTAPARRRTGLGMDVNPFGLFGQEKPETADNSPQTTTAAPNSPP
EPPSFNKALALADGGGSAAASSSPGNTRQSESTPRGAASSGTPATASAATGPADNPGVARVTGVRRLPYD
PDLYIPENTYIPCSLDRRFVSDVAGKISCTISEDVYSASGHVKLIPKGTTARGVYKTGTLKHGQGRMFII
WTELRTPEPPYLDIPLVDTQAAGQLGEAGIDGWIDTHFWERFGNALMLSTVQDVAAAASGSAPGKDRNTD
YTENSRQATAEMAKTALENSINIPPTLYKNQGDIIGLITGQDIDFSSIYQLRMK
>gnl|CDD|469314 NF041423, MobC_subf, MobC family replication-relaxation protein
MLIHDYAERQARANEKIRLLLNFLKEETYSDFKTLMLLLGFKSHRPLYRLLNKLVAMGLIQKHEFPVRTG
KISLWGITPDGLAVVVTPDDKVFPARFEPSKLKGWTLEHHLDNQRVRLALERKGWTGWINGDRMAFLSRY
PVKHRPDGLITLPSGAVIAIETERTLKTRARYQSIIASHLLARKAGKWDYVFYVVPDPQTKRALERLFDS
IKTVIVNGQPVPLEAKHRNVFRFYTLDEL
>gnl|CDD|469315 NF041424, Brachy_memb_1, WESB_1763 family membrane protein. Members of this family are highly hydrophobic proteins that appear so far to be restricted to the genus Brachyspira, a spirochete lineage. The function is unknown
NNSFINKYNFWANILIIAVLFNYLFFRTLFIDNESFFYLINYILNYSILISFFLLLFYKFYNYLFNSQIL
LSILGIIFLITGTLKLYISDINIYNIIELLFFISTFVLTIKILIPIILLKNINELERGVYIFILLSLGSS
NLNYIIISANKIIDTDIFHYISLYLSVYMSKVSSISFIILMIAYIIIFMKEIIMKNINKSKYFAFILVIL
ISVAILLFGYSFFLIIISFYNALGIGIYLPFVVYMIIIIMFLITLFSSFTSSIISKKYYPELIIFTLFIL
AGLDMSNFSLRLISIFSIMEMSEIIN
>gnl|CDD|469316 NF041425, OS_HP2_seleno, OS_HP2 family (seleno)domain. Members of this family contain a branch of the DUF1573 (PF07610) domain. A majority are selenoproteins, with a UGC motif
VPEPTYEFEPVVEGTEVTHDFIIQNKGDAPLEIEKVKTGUGCTAVSYPRQIPPGGEGKITIKVDTNGYGG
RKLKKTITVYTNDPKNPRLTLTISGKVE
>gnl|CDD|469317 NF041426, TrsA, conjugative transfer protein TrsA
MDNVAMRKRIEEYRKKYMEQKKYTNKENYQSRFGIKDDELNTFNIKGIATDRKENKLVLAEDKQDKQKLL
LYANKNNDMYYLNSGSSYKEAVQNTFGKSTNYEVVDDELFIYNSKKQSLTNYEQLNNYHNREEQLQYDKP
LEEERKERLTDTNKVSEQAKEDLALSLGLTATAFKGDINITDIERVTDNESMITIENEITGKSEHLISDF
KDNFVEKIKEKLNVSPSVRLGFEEFKNASLQIAMGFTEFYGARYDESTLERDPKVVLTEKGYSVSTFDKD
GNKKDLTSADTFEEAVKLSKELKQDNTLSRDSIELEQELERKKG
>gnl|CDD|469318 NF041427, TrsD, TrsD/TraD family conjugative transfer protein
FDYIPPKINKGKQTIQDMSLIEGIYKDYVVTKTGYLVGILEVSGINLDLLNEYEQNDVFEDYNAFLMSTL
GEGSDDSLQFIDMTIPVDMTNYILGLKKRYLEEKENNPNNEFKIQLIASYIDHYQEIQASKEMSTKQHLV
VVKEKIKDKTFESLDLAVKRLDEKVNQIKRDLENAFEDYDLEARKLNAQEILNILKNLINF
>gnl|CDD|469319 NF041428, TrsH, TrsH/TraH family protein
MKKLLGILVLLTLVLAGCSQNQKNQEKKEKEKSVDSTKERNKMIKGLIEYGYTNDDYKGYKDMKDILSKK
MRKQVDNQNQSYETNDIKKEIEDIKLYKDVDNDKELMYSVKVKITNDKTKNSDYSIRYGKIKLKNEDGKQ
KIDNIQE
>gnl|CDD|469320 NF041429, EexR, EexR/EexS family entry exclusion protein
MTNLLKSLPARCWYISLGLFLATLAAAHFFPSEILTASAKLAALPFLICTVVFFSYLGFKATCNPIGLIA
IITMLVAIAYWQASWTIVGLGLFFLAISTGIRFLSSQVKDTGRELSLEEKKYWYWVNEFFDGRYSIYPKK
PK
>gnl|CDD|469321 NF041430, UrfF, plasmid repression protein F
MKDKRDKKTGDLLASPNAVRQARYAERQRAKGRKQRKFWLTDDEAEALRLYLEELRAAQGGGSDPASA
>gnl|CDD|469322 NF041431, S_layer_MEMAR, MEMAR_RS02690 family S-layer glycoprotein. Members of this family are archaeal S-layer glycoproteins in the family of MEMAR_RS02690. Most members of this family have the PGF-CTERM domain, recognized and processed by the archaeosortase A (ArtA). Surprisingly, while MEMAR_RS02690 itself, from Methanoculleus marisnigri, a methanogen from the Order Methanomicrobiales, has the PGF-CTERM domain, and ArtA is encoded in the species, cleavage and lipidation was not successfully shown. All seed alignment members contain the PGF-CTERM sorting signal at the C-terminus, but additional members of the family differ at the C-terminus, and appear not to be ArtA-dependent surface proteins
TKLMVAAVALLLAAALVVAPAAARVNGISSGDTVFVGEEGLNLSAAVGTASQLAWYASGDTPTTDDPSIV
VTVGNSFDLTFYVSPSGTGNWYWNGTSKGAAAVNVRDPSVTLDVVLWDSNTSDSVTGKSVTRGTYLAFRL
TSNLGGLATRPATVAADAIKIEVTTPGGGVYTQLGNNSGGTTNLTGIALNQSQWYWTANDVWDLAALDAK
AGTYTAWAKWNANGMKDFYTGKTDSNTVTFTIATDTVAIEANKDSVVRGNPFSVTITGESKTDYYLWVKD
TSSLTDDQPPFIVPGQPGVTFDSGANAGLYYTYAGGTIAQDVPNGTDGNGTDTYATVKTNASGTRTVEFN
TTATTKDKTYTIRVEDPVGPTLYYDEVKVKVEKGDVTITASGDGSYYLGEEVTLSGTNTDSDTVYLFITG
PNLPSNGVNLEDPNDAVNNGNAASFVTADVEGDDTWEYKWDTAGLALDAGTYTIYAVSQPRDKNHLSNAK
YATVSIVLKKPFVTATASGATVAKGDKLYITGTAEGDPSQVAIWIFGKNYYVLYATESVEDDGSFEYELK
SGDTSNLAAGQYFVVVQHPMYNGEFDVYPDATLAGQLGTGPTGTSNFFKLVGLGSLQGSDAATALINALN
SPNVDDTYTKLTFLVEEPWIRIDPIGDKAVGSKFTISGTTNLAVGDDLLVEVTSSSFQPTDKTQSGEFSG
ASGTVKVQQGTAGYNTWSFEVDASTFKPDEYIVTVESIEADTTATATFNVLEATPTTTATPTAPPTTTPT
TTPTTPPTTTPTTTPTQSPGFGALVALIGLGAVAFLVLRRN
>gnl|CDD|469323 NF041432, MchS3, MchS3 family protein
LSKVSYFSLGMNGFIGKISEGEKLYRKILQSKNAEEIFLRIAESEKATPESKLYAACGLRKLNKKNFDKI
FDKRLKGEVVSVLKGDILRKESFKDVLFSIKKHGC
>gnl|CDD|469324 NF041433, UmoA, UmoA family protein
MSAKSLFILLSLLGLSCTCFAGNGLVDRTWTASGRDTQSYRQALRQPTASSRYTLFNITPDMPVPGGTSN
DPPQGIRYIAMKYGPYGQPEHYKTYQIMFSHYSPGSTKKIRYLGELYTVVGDIYLIDPFATTNEWQRGRS
QIVEEYYEILDKHGNRTGKGLRFHSWDRPIHITKWSSN
>gnl|CDD|469325 NF041434, UmoC, UmoC family protein
PLTQCYESIGDAPRTALAGCLDDKLKLAEKQLNTIYAKSKKDLEDIDSSATKKAIASLKASQEAFIKFRD
AECQRQSDAAMGGSGAGDILLACKIKLTRWRIKQL
>gnl|CDD|469326 NF041435, UmoD, UmoD family protein
MKLKIKLLLIASLIVCLIILIAIIFLFKSPRPKLATVLSSEPIKSTRLVEQEYCHITGVPGPFTQENLSR
NHPAEYECRIFFLIETLQKKEYPALNYSQLKNCIITQKKEQRIVGYDVVYRIGNTPGKVRTPYKPGDFIP
LDEKGRLILT
>gnl|CDD|469327 NF041436, Wzy_Strepto, oligosaccharide repeat unit polymerase Wzy
MTIKINNLFFVCLSFMGIVLSNSQVIVNLGLDSVIQYLSYFILILCIFLKLIKNFKTIVAKRIVYFILIS
FLFTIGICLQDLPFSTKIYLSFSMLIISSLATLPIKLINNISDFRRISYYLLYAVLISTILGIVFGASMF
TVAVEGIGSSYGFNGGLTHKNFFAITILTSYILLYISRKYGVKHQIDSYVLWFELFLILISNSRTVYLIL
ILFWGIINLKLIKNIKKNQRIVLITTIVIISLIFIIIFFEYIINNSDSYTHRVQGIINFFNYYSSDYFHL
FFGDAELAFGDLTHDYAYNIRSVLGWDGTVEMPLLSVMIKNGYIGLIGYGIVLLKFIKSIKKIKNRNIKT
IGLSILIPLLLSATVENYIVNISFVFMPVCFCILNSLKNLELSLN
>gnl|CDD|469328 NF041437, TfpZ, TfpX/TfpZ family type IV pilin accessory protein
RLKAFLIHLLISALVALLAAALVFFVWYPAPLAKAVGVTHIFLMLLGVDVVLGPLLTLLVYKEGKKTLKF
DLSVIILLQLAALGYGLYSIAQGRPVWIVFNVDRFELVRANDIDPENLAKAKPEYQTLSWFGPKWVAARP
PKDPEERNDLLFEELFGGIDLAQRPELYVPLEQAKEQIQQRAQPLSELKKYNPKAAVDAVLAKYPQADAY
LPLKARAKDMTVLIDKETGEVLKIVDLRPW
>gnl|CDD|469329 NF041438, SepM_fam_S16, SepM family pheromone-processing serine protease. This HMM describes a peptide pheromone-processing S16-type serine protease found broadly in Gram-positive bacteria, and named for the founding member from Streptococcus mutans (see BlastRule NBR014542). The Lon-like catalytic domain is located toward the C-terminus, and has a Ser-Lys active site dyad rather than the more common Ser-His-Asp triad found in large numbers of serine proteases. Members of this family also have a PDZ domain
KFKWWLLGILALLLLLFALFFPLPYYIEMPGGAYDIRSVLTVNGKEDKEKGSYNFVAVSLSRATLAQLLY
AWLTPFTEISSAEETTGGYSDADYMRINQFYMETSQNGAIYQALKLAGKKVSLDYKGVYVLDVSKDSTFK
GVLNIADTVTGVNGKTFKSSKELIKYVSGLKLGSKVTVQYTSNGKKKSAKGKIIKLKNGKNGIGIGLTDH
TEVSSDDKVKFSTEGVGGPSAGLMFTLDIYDQLNKEDLRKGRKIAGTGTIEQDGSVGDIGGAGLKVVAAA
KIGADIFFVPNNPVDKALKKANPDAKTNYQEAKEAAKKLKTKMKIVPVKTVQEAIDYLKK
>gnl|CDD|469330 NF041439, TraE_Enteroc, type IV conjugative transfer system protein TraE
DICYYGKRCTVFEKITKKLSTGKSKTVVQVKNYRIEGLKALEEQEYFEGKKKKVILKEPVPLKEIYPRIK
HVYDKNGVLIARRNSPNGPLRCTGKGMGK
>gnl|CDD|469331 NF041440, hydrolase_YghX, YghX family hydrolase. YghX is a predicted hydrolase, homologous to dienelactone hydrolases, but its function is unknown. YghX is encoded intact in Escherichia coli O157:H7 str. Sakai, but is a frameshifted pseudogene in Escherichia coli K-12 MG1655, and consequently is used occasionally as a site for minimally disruptive genetic engineering
RLTAKDFPPELLELYDYYAHGKITKREFLDRAAKFAVGGLTAAALLAALSPNYALAQQVEFTDPDIVAEY
ITYPSPNGHGEVRGYLVRPAKATGKLPAVVVVHENRGLNPYIEDVARRVAKAGFIALAPDGLSSVGGYPG
NDDKGRELQQQVDPTKLMNDFFAAVEFLMAHEATTGKVGITGFCYGGGVANAAAVAYPELAAAVPFYGRQ
PKAEDVPRIKAPLLLHYAELDERINEGWPAYEAALKAAGKTYEAYIYPGVNHGFHNDSTPRYDEAAAELA
WERTLAWFKKYL
>gnl|CDD|469332 NF041442, YgjJ, protein YgjJ. YgjJ proteins are widespread in the Gammaproteobacteria, and named for the founding member from Escherichia coli K-12
LLAALIFTAPSAAAEEVRPAEHDDTQTPETSETSFRFYGELGVGGHVDLEGEDKGRYSDGTYIEGGLEIK
HGNWFGLIYGEGWTVQADDQGNAWAPGHGWGGFEGGFNRFYGGYRTDDGTEIMLGRQDSSLDDLQWWGDF
TPEYGYVIPNTRDLMYALKVQNLEGKLRYSVSAAPESDFDESDAWLHFGKYDRYADKYTYPAMVNGYVQY
DLADDLTLLGGLEVTDGTGELFLLGAEYKNLAARVWHHTGRGNQDSPGTETGFMTSAMYEAAKGVYLSTA
YSYANHRPDNAEDETTSYINFGVWYEYGGGRFATAFDSRFYMGNDSGDPSDQVFLMQYFYW
>gnl|CDD|469333 NF041443, DDRRRQL_YjdP, DDRRRQL repeat protein YjdP. Members of this family average 108 amino acids in length, with a signal peptide and with a highly charged C-terminal region of typically five tandem 7-mer repeats approximated by DDRRRQL. The family is named for founding member YjdP from Escherichia coli K-12
MKRYSTALLFGLLSLTSQLAHADIIDDAIGNIQQAINDAYNPDDSDDDDDRRYDDDRRRSDDRRRQYDDR
RRQLEDRRRQLDDRQRQLDQERRQLEDEERRL
>gnl|CDD|469334 NF041444, SASP_CD1290, CD1290 family small acid-soluble spore protein. CD1290 (CD630_12900) from Clostridioides difficile 630 is the founding member group of small acid-soluble spore proteins (SASP). Members are related to the alpha/beta family described by Pfam model PF00269, but are shorter on average and typically score below thresholds for that model. Sequences that resemble germination protease GPR cleavage motifs are EIAx[D/E] and [E/D]IIEN
DQNAKKALKQVRMEIAADYGMDYEDAFDIIENAHNNGVLANHFKKLEEKKSLGSSKTRHLE
>gnl|CDD|469335 NF041447, TrbC_conju, F-type conjugative transfer protein TrbC
VDRARVNRQVGGSPLTDALLSPGTLALGMAASLVAGFVWPVTLLLSLPVLLVWSPVFSDQRWRMPMRMPM
DMGRLDPSTEREVPRKLLGFLPVTYERIVMSKAAGILYLGYLRGRDAGRELWLSMDDLTRHILMFATTGA
GKTETLLGWVLNSLCWGRGFIYSDGKAQNDVAFAIWSLARRFGREDDLRVLNFITGGRSRAQELLEGDKS
RPQSNTTNPFGYAQETFIIQLMDSMLPPAGNSGEWQDKAKAMNQALVFALVYKCRREGKVMSQRTIQEHL
PLRKIAGLYCQAVEDQWHEEARLPLENYLSTLAGFDMALVRTPSEWAQEALDQHGYLIQQFTRMLSMFND
TYGHVFARDAGDIDLRDVLHNDRILVVLIPALELSASEASTLGRLYISQIAMILAQDLGEKLEGRPEDTL
VVKKYKDRFPFLWICDEVGAYYTEKLGELATQVRSLGYMLVLAAQDIQRLKTAAGDEVWTLNANMGTKIF
GKIMDPKDTLEILQLMAGTEYRAEMGSMVRQGGIIGGSWEDADRLSIREKDKIDVEELQALQEGEGITVF
KGEVVRGNSLYIPDDDKISKLPVRINRFIEVRPPSLDELLALVPATARRRPPRADRVSRILGVLDAKPGR
SDTENLVIIDPALAALAELAEELDNRWDRSPTAAVRGILLWETALEALPERGRRY
>gnl|CDD|469336 NF041448, stress_YjaA, YjaA family stress response protein
MAVLYIQIRKNRMTVRNLDTKQEVSGSGEFSTQRLLVGDFFPAEKLLYQLIRQVAPRFWNAFLPFCSRHR
ILIHALEMNEGGLSQVEERLLIELTASASPRKYKKLVVSAKSVPLSDQEVIALLS
>gnl|CDD|469337 NF041449, K_carrageenase, kappa-carrageenase
SVAAAADPQPVGLVFPDPSGQWVLVEDFSDEFNSAQIDTKKWNIDTEDWGTWSWEPENVSQKDGSLHLQM
VQEDHQRGNNKLAYTSGIARSYRTITYGYFEARIKGCSRFPGACPAFWLYSKGPENRYLAPDGETVAYSE
IDIVELQQGEYDFETKRHNGVNRIDCNLHTVLIRDGKRQWIRPNTHPETCKNEYDAPWDPRDDYHVYAVE
NTPEFIVWYIDGKEVARKPNLYWHLPMHVTLSLGLRPPFEAYAGGGRVAVLEKTTPEGFPTEMSVDYVRV
WQN
>gnl|CDD|469338 NF041450, MobP1, MobP1 family relaxase
EKEYRAKRVFKRSEKASKSPFAYKINKGKKLYNKGKNGRINKKGASREVMVKITGGAKTAQGIKNHIDYI
SREGELELYDNEGSEYTGKDEILEAKDIMINDGADKPQYYGKELKKHTKNMVFSPPEIAGVSQEDLLEAV
RETLKEKYPNNRFVLAYHDDTKNPHVHVVLKIADNDGKRINIRKKDLRELRTGFAEKLKKLGYDVKATHK
QDFELKISIKREQAEAPKRLRNVYEVVDFGEASYQFDKKNKRSNYITYKTLKGGKEVTIWGKDLEEEIKR
EKVQKGSLIKLKKIGQTDVKVPRYDKNGSQVGWKTAKRNNW
>gnl|CDD|469339 NF041451, DDP1, DNA distortion polypeptide 1
MKKVKFRISDEEHELAEDEAGLTGAKSVKVLAKSKVLKEKAKPVDIPVSNEPEKFIKTYLYPHEIELLKR
NAALHGWSLSREIRFRIQSTLKNELDLYPDELKELRRLRTAIDKVGRNIHYIIKGDRFCTVNDPEFRKDI
ERLTSLINQLDKKLENLIMLCKGRSVVNR
>gnl|CDD|469340 NF041452, DDP3, DNA distortion polypeptide 3
MKYKVKEFLNEKYTKAVNILKENLKENYHVFYGVRLSEILFPASEYGTDEFFKEFESINSITLPLVIFDT
LERKPVAVISFEGIEGKDLLEDAGIKVIVIDALKDLLTNEELEPLY
>gnl|CDD|469341 NF041453, Bac51, bacteriocin 51 precursor BacA
EAASTKYNHNHPGYTCYKMSYYVSPSKCKKLKKQTKKLNTPSAIANFIGLGGLTGGVVSLAFGSAVDANQ
VFVKAANQGKGVQLTYIAHFSNYTTDSYSSNFKYVIK
>gnl|CDD|469342 NF041454, FspA, flagellum-secreted nonflagellar protein FspA
MQINFLLKNLSQYTKLNENQTKKKKEDKSQKALNDNAVEVTISKEAKELSQKNSESQEKIPKNNDQNQVE
QSGGGSNDALEELIEKLAEILAKIAELTAKMANANEQMKASYQKQIAVLNAQASTIQAQIQELQAQQQ
>gnl|CDD|469343 NF041455, DSF_Ax21, diffusible signal factor-reguated Ax21 faimly protein
MKRSLLALALLAALPFAASAADGLSYNYVEGGYVATDTDGGDADGWGLKGSVAFHPNFHVFGDYSNQEID
DTDVDFDQWRVGVGYNHEISPNTDLVARVAYEKFDAGSGLDFDGYSAEVGVRGALTPNFEGYALAGYEDY
DDPDGDFYGRLGAQVKFNQNWGLSGDVKFADGDTQWFVGPRFSW
>gnl|CDD|469344 NF041456, surv_prot_CiaI, intracellular survival protein CiaI
MQIDASKNQNFSMDYTTKSGKHLSFSMFDNQSASYNKNEEGKSLSLKRQYGFSFSYEGSKLTQEDLAEIK
NAMKEVEPMIQEFLQNSKVGELNPKEFIQSAMQMANVLPTPNDENHQNAIMDNFTNKLENLLNQNQSPDP
EQNTSMLEDSKKLLDEVLEQMKKQLEKLQEKAKNNNKFDNNFGFYA
>gnl|CDD|469345 NF041457, reg_protDegQ_Bacil, degradation enzyme regulation protein DegQ. gene synonym sacQ
MEKYKIEELKQLLWRLENEIRETKDSLRNINKSIDQYDKYAYVKIS
>gnl|CDD|469346 NF041458, antiadapt_SpxO, anti-adapter protein SpxO
MKEIDDMISRLRSRGIKVEKVKYPKHTLCEKKWMKQPKKKVKATYRDFNGYSFI
>gnl|CDD|469347 NF041459, antitoxMazE_Staph, type II toxin-antitoxin system antitoxin MazE
MTSFNQNRSHSLEQSLKEGYRQMADLNLSLATEAFPSECEACDCNESHLTSNQK
>gnl|CDD|469348 NF041460, kinGactiv_GlnX, protein kinase G-activating protein GlnX
MTVELAHPSTEPLGSRSPKQPAHPRWWFLWTTPGRILTIGVVLAMLGVLSAFATSTTIDHRQQALTTVLD
HTEPLSFAAGQLYTTLSVADAAAATAFIAQAEPAPVRQRYEQAITDASVAVTRASSGLTDEHLVQLLGRI
NAELAVYTGLVEIARTNNRAGNPVGSSYLSEASSLMQDTILPDAQRLYEETSARVDAETTASTRVPAPVI
LVVAITVVFGAFAHRWLARRTRRRVNPGLVAGGLAILVMVIWVGTALVISTTSSRSAKDTSAESLKTITN
LAITAQQARADETLSLIRRGDEQARKQSFYQRIDAMQRQLNQYLARDNAVDKSDLADADQLLDRWRAAND
RINAYIAVGNYQAATQVALGTGEDDSTPAFDKLDEALTKAIGQSRTQLRADITNARRGLSGATVGGVVLS
LAAAIAVALGLWPRLGEYR
>gnl|CDD|469349 NF041461, C_hydro_YcaC, isochorismate family cysteine hydrolase YcaC. YcaC is a well-conserved cysteine hydrolase of unknown function, found in both Pseudomonas aeruginosa and Escherichia coli K-12, with an isochorismate family crystal structure
PYKRLDKDDAAVLLVDHQTGLLSLVRDFSPDEFKNNVLALADIAKYFNLPTILTTSFEDGPNGPLVPELK
EMFPDAPYIARPGQINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSALEEGYEVFVVTDASGTF
NEVTRDAAWDRMSQAGAQLMNWFAVACELHRDWRNDVEGLGTLFSNHIPDYRNLMTSYAAV
>gnl|CDD|469350 NF041462, GalA, beta-galactosidase GalA
DFGWRFHLGDIADPAKDFHFGTDQYTFAKAGNAWGAAAPDFDDSDWRSVDLPHDWAVELPFVPDANASHG
YKPRGIGWYRRTFDLPASDRGKRIELEFDGVFRNATVWVNGSVVGRNWSGYTSFRIDITDFLRYGDENVI
AVRVDATAGEGWWYEGAGIYRHVWLVKTDPVHIATDGVFVRPRLDGGRATVPVETTLANEGDAAATVRVE
STLLDPDGRVVATAESAPLSVAALETATVTQTLPVANPALWSVETPYLYTLVTTVLVDGKVVDEVVTPFG
FRTIRFDADKGFFLNGKPVKLKGVCNHQDHAGVGVAVPDALQEWRLRRLKEMGCNAYRTSHNPPTPELLD
ACDRLGMLVMDENRLFNSSPEYLAQLEWMVRRDRNHPSIILWSVGNEEPMQGTEQGARIVRRMVALVKRL
DPTRPVTAAMNGGFFGEGVSDVVDVVGFNYRTGNYDKFHAAHPNKPIIGSETASAVSTRGEYATDKAKHV
VSSYDTEAPSWGSTAEEWWKFIAERPFLAGGFVWTGFDYRGEPTPYEWPSVSSQFGIMDLCGFPKDAYYY
YRAWWRDEPVLHLFPHWNWPGKEGQPIKVWVYSNADEVELFLNGKSLGRQKVDRNGHLEWSVPYAPGRLE
ARGYRGGKVVLTEVVETTGAPAALRLTPDRTVLAADGEDVAVVTVEAVDAKGRHVPTADNLVRFSVSGPG
RIIGVGNGDPNSHEPDKAPQRSLFNGLAQVIVQSTKGAGAITLTATAEGLKPATLVI
>gnl|CDD|469351 NF041463, GalB, beta-galactosidase GalB
RERISINDGWRFHKGDPAGAADADFDDSGWEQVTLPHDWAIAGPFYKGGPAEVGGGMGRLPSWGVAWYRK
KLDIPASDAGKSIFLDIDGAMSYAMVWLNGQLVGGWPYGYNSWRLDLTPYLKPGGENQLAIRLDNPPESS
RWYPGGGLYRNVWLTKTNPVHVAQWGTFVTTPEVSADSATVDLAVTVDNDSAADADVEVSTEIYALDADG
KRTGKAVARFAPASLTVAAGESATVSGSLTIANPRLWGPPPTQTPNRYVAVTTVYQGGKVVDRYETPFGI
RSLRFDPDRGVLVNGEHIRLQGVNQHHDLGALGAAFNVRAAERQLEILREMGCNAIRMAHNPPAPELLEL
TDRMGFLVVDEIFDSWERKKTPLDFHLIFPDWHEQDLRAMIRRDRNHPSVIMWSIGNEVGEQYTGEAGAA
IARRLHDIVKEEDPTRPTTASMNYAKPDMPFPAVMDVISLNYQGEGIRDAPAYEGLKGIRTPPLYPAFHA
KFPDKVILSSETASALSSRGEYLFPVTPGISAPVRDGRGGDPVTHQVSAYELYAADFGSSADKVFAAQDQ
HPYVAGEFVWTGWDYLGEPTPYYSSRSSYSGIIDLAGFPKDRFYLYQSRWRPELPMAHILPHWNWPGREG
QVTPVHVFTSGDEAELFLNGKSLGRKKKGPYEYRLRWDDVVYEPGELKVVAYKNGKPWAEDTVKTAGAAA
KLQLTADRATIAADGKDLSFVTVRVTDKDGLLVPRADNRLRFSIEGPGEIVATDNGDPTDLEPFPSPERN
AFNGLALAIVRAKPGQAGKITVTAESDGL
>gnl|CDD|469352 NF041464, HelD_BACSU, RNA polymerase recycling motor HelD (Bacillota-type)
MSKEEQEWQEEQQRVDRVVDEIDKKIDKLEQQVGGLKEDIVDIRKNFWDDVTVNLDDPDEAIETFASIKQ
QAELLSERERSHRHAYKQLKTLKRLKQSPYFGRIDFLEDGEKEAERIYLGIASLMDENDEQFLIYDWRAP
ISSLYYDYSPGPAQYETPGGTIEGEMELKRQFIIRNGRIKSMFDTGVTIGDELLQEVLGNQADTQMKSIV
ATIQKEQNQIIRNERSKLLIVQGAAGSGKTSAALQRVAYLLYRYRETLSAENIVLFSPNPLFNSYVATVL
PELGEENMQQTTFQEYLEHRLGKTFDLEDPFTQMEYVLTAMEDPGYEARMEGIRYKASLDFKQLIDQYVE
YLSKEGLIFKDIKFRGEVLISAEEIKEYFYSLDPSLSIPNRMQLVAEWLLKELKKLEKKERKKDWVEEEI
ELLDKEDYLEAYKKLQKKKRFTEDTFDDFEREQKLLAKMVVKEHFKPLRKAVKRLKFIDVPAIYRQLFAD
PELIASFAPDDLLPENWEEICKQTVERLKRSELAYEDATPYLYLKDRIEGFKTNTSIRHVFIDEAQDYSP
FQFAFLKRLFPRSKMTVLGDLNQAIYAHATGPTGFLLLSELFEEEETETIVLTRSYRSTRQIVEFTKGLI
PGGEEIEPFNREGEKPTVTEVEDKEELHEKIAERIRELQEEGHQTIAVICKTAQESREAYEALKDELPLR
LIDKETVSFEKGVLVIPSYLAKGIEFDAVIIYNASKEQYGRESERKLFYTACTRAMHELHLFSLGEPSPF
LS
>gnl|CDD|469353 NF041465, HelD_MYCSM, RNA polymerase recycling motor HelD (Actinomycetota-type)
VPAQGYEDELRSEQTYVDGLYARLDAERARVRGRYSTALRGTGGSAVERDVEVRALAKEAKRLDVADNGL
CFGRLDTVSGEHSYIGRIGLFDADNEYEPLLLDWRAPAARPFYVATAAHPENMRRRRQFHTRGRRVVDFT
DEVLGRPGGGERGDAALLAAVNAPRGEGMRDIVATIQAEQDEIIRLDHPGVLVIEGGPGTGKTVVALHRV
AYLLYTQRERMERHGVLVVGPNPAFLNHIGRVLPSLGESDVVFMTTGDLVPGLHVTAEDAPEAARIKGSL
KILDVLAAAVADRQRLPDEPILIELADVTVRIDAETAQWAREEARASGLPHNEARAVFREIVTWVLTERA
IARIGKGWLTRSDREAWEQLRADLLAELAENAAFAAALDQLWPILTPETLLAELYSSPERLSAAGADPAL
WRADGAAWTVSDVPLLDELVDLLGRDKPVDDAAERERREEAAYAAGVLDLMVVREDLMDDEDHLLASDML
YAEDLADRFIERDTRELAERAAADRDWTYRHVVVDEAQELSEMDWRVLMRRCPGRSFTVVGDLAQRRSAA
GATSWDAMLEPYVPGRWVYRSLSVNYRTPAEIMSVAAALLAEFAPGVQPPESVRACGVQPWSRQVDADEL
PAAIAEFVRDEAGREGTSVVIGPPGVPGAVAASETKGLEFDAVLVVEPERILADGPRGAAELYVALTRAT
QRLGVLHQGPLPQALAGLA
>gnl|CDD|469354 NF041466, factorH_bind, factor H-binding protein
MTRSKPVNRTAFCCLSLTTALILTACSSGGGGVAADIGAGLADALTAPLDHKDKGLQSLTLDQSVRKNEK
LKLAAQGAEKTYGNGDSLNTGKLKNDKVSRFDFIRQIEVDGQTITLASGEFQIYKQSHSAVVALQTEKIN
NPDKSDSLINQRSFLVSGLGGEHTAFNQLPEGKAEYHGKAFSSDDAGGKLTYTIDFAAKQGNGKIEHLKT
PEQNVELAAAELKADEKSHAVILGDTRYGQEEKGTYHLALFGDRAQEIAGSATVKIVEKVHEIGIAGKQ
>gnl|CDD|469355 NF041467, caps_synth_Cap8I, type 8 capsular polysaccharide synthesis protein Cap8I
NKISNLLLLITSIISFIILLINGEILLSLMPLSYVFSKLITRFSKNGNLKFTKGIYDLFGFIRLVLIPLV
IAISGDKKIDNLPLGFMYFNQAVILISVEYIIGSILLVILSKLFKDTVKSRKEFKLSGSRIFYYIFIIFV
IIIFVSIPSVRETISFLIIKTDASGRGTEATSGINVLLRMLLQLALALLFIISSYRSYKKYKVNPKIIYL
ILPLIFGIINISLIVGERRSIQLYTLVGVLVIISILFKYHSKKINIVILSVGAFILILMTLYKELYVFNY
SSYTDALNSSSVNNVKFVDSLQSYFYGPHNVAASIDYLNYYDGSFKQLLFDNTRSIFGINMLVDKSQLIT
SQLFNQIIYGSKQLTGHLISSAGYGYIYFGPLLFPLVLFTNLFMASTLEYLIRKNNSLELIFIGTYLYMR
VSTTIFGHTTPIITLISMILVVYSAIIIISIIVKKFLKLVGID
>gnl|CDD|469356 NF041468, anti_sig_RseA, anti-sigma E factor RseA
MADRGHVFRRAFSWLPSQFASQSDAPVGAPRQFGSTEHLSTEAIAAFVDGELRMNAHLRAAHHLSLCPQC
AAEVEDQSRARAALRDSHPIRIPSTLLGLLSQIPHCPPDPPPGPTSPLSDRFADGDARDRRKRR
>gnl|CDD|469357 NF041469, spor_prot_SB, stage II sporulation protein SB
MAEVKQQKLSFFKEKKEEPNTDFSLVKGALTENINRLEKLMENSPSKYIKGKKLKENA
>gnl|CDD|469358 NF041470, sec_prot_XpsN, general secretion pathway protein XpsN
MRLEAIGLRTWWLATLALWGLLVWVLGLAGLGKRVAPLPDDPAMVQRLPTLPAAAPERLGDFSKYAEIAA
RPAFAEDRLPHPFFLSADNGQTAAPTVRLTGVLLTDTFKMATLTTEPGESLRLQEGGDAVKGWRLLSLEP
RSATISGPGGTQTLELQVFDGKGGQPPTALGPAARAPVPPQPPPQPSAPNAQPNPPPPTPPQPQPGGQPP
GQTPTPQRSGPQEAPRPSDEQLQAIRERIEARRRQLQQQRQNGSSPGQNP
>gnl|CDD|469359 NF041471, phage_reg_YmfL, YmfL family putative phage regulatory protein. Members of this family are homologs of the e14 prophage region protein YmfL from Escherichia coli K-12. Distant homology to phage regulatory protein CII, as described by Pfam model PF06892, suggests a similar function
LKEAVKAMIKAFPGGREAAAAALGMTLDAFNNRLYEKAGSRFFTLDELMALEDLSGTTHLAEYVARRSGG
VFVPLPEPEELDNVELYDRSLELAAKRGELDQAIREALADGVIDRAERKAILAAHRKHMAARQEEVLATI
RLY
>gnl|CDD|469360 NF041472, toxin_DinQ, damage-inducible type I toxin DinQ. Members of this family include DinQ as seen in Escherichia coli K-12 and a family of closely related DinQ-like type I toxins termed DqlA. See model NF041473 for the more distantly related DqlB type I toxins
IDKAIIVLGALIALLELIRFLL
>gnl|CDD|469361 NF041473, DinQ_rel, DinQ-like type I toxin DqlB
MINLLIIVLRAVVALANALIAVLELIRQFID
>gnl|CDD|469362 NF041474, membrane_YkgR, small membrane protein YkgR. This family of stress response membrane proteins is named for the founding protein YkgR from Escherichia coli K-12. YkgR expression is induced by the cyclic AMP response protein (CRP), and the expressed protein is inserted into the inner membrane
MKENKVEQISHKLINIVIVVAVVEYAYLFLHFY
>gnl|CDD|469363 NF041475, membrane_YoaI, small membrane protein YoaI. YoaI, a small membrane protein found in Escherchia coli, Salmonella enterica, Citrobacter rodentium, and other members of the Enterobacterales, averages about 34 amino acids in length. The founding member of this family, from Escherichia coli K-12, was shown to be regulated as part of the phosphate regulon
MNDPMFVETLIITSSFFAIAMILVASVLLLERGG
>gnl|CDD|469364 NF041476, membrane_YldA, small membrane protein YldA. This family of small membrane proteins, averaging about 29 amino acids in length, is named for YldA of Escherichia coli K-12 but is found in multiple members of the Enterobacterales. The family appears homologous to YoaI, also found in Escherichia coli K-12
MSEILVITLIFLIIAAIIVMAVLYLERHW
>gnl|CDD|469365 NF041477, YnaM_YnfT_fam, YnaM/YnfT family protein. This uncharacterized protein family is named for two identical proteins found in prophage regions of Escherichia coli K-12, YnaM (Rac prophage) and YnfT (Qin prophage)
TSILIITSLLIILSALMLFALIKVGIGISNNPDN
>gnl|CDD|469366 NF041478, spor_prot_SspM, acid-soluble spore protein SspM
MKTRPKKAGQKPKTESKSTDQLDKKLGGPNRPST
>gnl|CDD|469367 NF041479, spor_membprot_YtrI, sporulation membrane protein YtrI
MRIPPYYKKPGWQRFFAGMMFGAIISWFFFLFTYGTFQEKQVTLIREQKEHIKDLNEQITLYQEDLHKLN
EDNKRKLLIQSVDVKLINGEQYKISQPDRLKFEEHIKDDISEVITKDIESVYQTKELLKRTIENKVYMIN
EKDYQAKVEELIIYTRLSVELRISFAE
>gnl|CDD|469368 NF041480, flag_mot_ctl_ZomB, flagellar motor control protein ZomB
SVRISLWLSVLVVAALFGWGAWQRRWIADDGLIVLRTVRNLLAGNGPVFNAGERVEANTSTLWTYLVYLG
AWVGGPVRLEYVALALALTLSVAGVVLAMLGTGRLYAPGLQGRRALLLPAGALVYIAIPPARDFATSGLE
NGLVLAYLGLLWWMMVCWSQALRRPPGPANARGRVFTAALAFVAGLSVLVRPELALIGGLALVMMLIAAR
GWRRRLLIVVAGGLLPVAYQIFRMGYYGLLVPGTALAKDASGAKWSQGFTYLANFNAPYLLWIPAVLLVG
LGLVLLATRSRPWWIRHDVPRGYGRLARTVQSPPAVVAFFVVSGLLQALYWIRQGGDFMHGRVLLTPLFC
LLAPVAVIPVVLPDGTRFSREAGYLLAGATTVLWLAVAGWSLWAANSPGMGADATRVTYSGIVDERRFYA
QATGHAHPLTAADYLDYPRMRAVLVAINNTPDGALLLPSGNYDQWDVVPAIPPPPPPPDAPPGYPGPHTV
FFTNLGMLGMNVGLDVRVIDQIGLANPLAAHTARLEDGRIGHDKNLFPDWAVAEGPFLKEPPYIPPYLDE
DWIAQAEAALKCPATDAMLNSIRAPMGPRRFLSNLLHAYEFTRYRIDRVPLYELARCGLPVPPPKGPPYT
>gnl|CDD|469369 NF041481, beta_arabfuran_tase, terminal beta-(1-_2)-arabinofuranosyltransferase
SVRISLWLSVLVVAALFGWGAWQRRWIADDGLIVLRTVRNLLAGNGPVFNAGERVEANTSTLWTYLVYLG
AWVGGPVRLEYVALALALTLSVAGVVLAMLGTGRLYAPSLRGRRALLLPAGALVYIAIPPARDFATSGLE
NGLVLAYLGLLWWMMVCWSQALRAPPGPAARPAAGRRFTAALAFVAGLSVLVRPELALIGGLALVMMLIA
ARGWRRRLLIVVAGGLLPVAYQIFRMGYYGLLVPGTALAKDASGAKWSQGFTYLANFNAPYLLWIPAVLL
VGLGLVLLATRSRPWWIRHDVPRGYGRLARTVQSPPAVVAFFVVSGLLQALYWIRQGGDFMHGRVLLTPL
FCLLAPVAVIPVVLPDGTRFSREAGYLLAGATSVLWLAVAGWSLWAANSPGMGADATRVTYSGIVDERRF
YAQATGHAHPLTAADYLDYPRMRAVLVAINNTPDGALLLPSGNYDQWDVVPAIPPPPDGAPPPPPGEKGP
HTVFFTNLGMLGMNVGLDVRVIDQIGLANPLAAHTARLEDGRIGHDKNLFPDWAVAEGPFLKEPPYIPPY
LDEDWIAQAEAALKCPATDAMLNSIRAPMGPRRFLSNLLHAYEFTRYRIDRVPLYELARCGLPVPPPK
>gnl|CDD|469370 NF041482, ADPrt_Strmyces, ADP-ribosyltransferase
MITTRLRRRAAAAVLSLSAVLATTAATPPAAPASAPAAAAAAAAAAPACPQFDDPVKAAADRRVDVDRIT
PEPVWRTTCGTLYRSDSRGPEVVFEEGFHPKDVVNGQYDVEKYVLVNQPSPYVSTTYDHDLYKTWYKSGY
NYYIDAPGGIDVNKTIGDTHKWADQVEVAFPGGIARQYIIGVCPVDKATKTEIMSDCESNPHYEPWH
>gnl|CDD|469371 NF041483, growth_prot_Scy, polarized growth protein Scy
MRGYERQESHRADDDHLSRFEAEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRSLASRPAYDGADI
GYQAEQLLRNAQIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAELHTEAVQRRQQLDQELAERR
QTVESHVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESARAEAE
AILRRARKDAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAE
AEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEA
AEKARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQL
KGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKAK
ADADELRSTATAESERVRTEAIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELRE
ETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLRTEAAERIRTLQAQ
AEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEA
LAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELV
SAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRR
EAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSD
AAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAET
VGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEA
DQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTDADELLVGARRDATAIR
ERAEELRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRI
AAVKKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAEISRVQDVLEAL
ESFEAPSGGGKGNGVKAGAAAGATRSGGKSSEG
>gnl|CDD|469372 NF041484, membrane_YmiC, small membrane protein YmiC. YmiC is an uncharacterized predicted protein about 32 amino acids long, hypothesized to be real and a membrane protein based on conservation across multiple gammaproteobacteria with constant length and constant hydrophobic character suggesting insertion into membrane. Expression was verified for a construct with an added C-terminal epitope. Homologs tend to show a pattern of conservative amino acid substitutions. Thus, comparative genomics also suggests YmiC is a real protein. An usual feature is three perfectly invariant Trp residues, and a highly conserved fourth, in a stretch of 19 residues
NHSNMKYWSWMGAFSVSILFWAQLIWLLLN
>gnl|CDD|469373 NF041485, spor_mat_CgeC, spore maturation protein CgeC
MESEQLVNREENQDELHVVLLLLILLLRQTSSEGNPSDLRRQLVFAKELGIPVSRVNLINGDTLQNVIVK
EVLSDLAVFQNPLNNTRSNVALSSIVSWGAF
>gnl|CDD|469374 NF041486, rep_init_RepSA, replication initiator protein RepSA
LDPITLGDLLRVAGAPGFDRWQDQIRRTGGCADPIHLTGWTLTKDKTTGQVLHSYSTDAEPGGRLRVACG
NRRASRCPSCAWTYAGDTYHLIRAGLAGDDRKGIPATVRDHPRVFATLTAPSFGPVHNRPDTGRCRCGTR
HAEDDPALGTPLDPETYDYAGAVLFNNHAGDLWRRFTIRLRREIAARAGLTQRELREVARVSFGKVAEFQ
KRGAIHFHAVIRLDGPDGPDTAPPAWATVDLLTDAIRAAAAHPYTTVTVPAAGDQPARTLRWGTQLDVRP
IGAFGDGGELTEQAVASYVAKYATKAAETTGTLDRRIGELAELDRHDVPDHTRRLIRACWDLDPLYPDRR
LWAWAHMLGFRGHFSTKSRRYSTTLGALRQVRADYRAAQERRALGLPDPDPDTTLVLAHWQYAGHGHTPG
ESWLAATIARDIQLNRETAREAL
>gnl|CDD|469375 NF041487, copper_ox_MnxG, manganese-oxidizing multicopper oxidase MnxG
CQRNLVANVVALDQPLMFNRLGAQNVNGMMFALRRDVVDDNQVPLSQGGAAVPGKVTLRPDKRPRPLVLR
VAAGDCLTVNLQNLLAYQANPNSHEGEGEEGEEEEAEVEPEFKIDDQVADRHVGFQVNGMQAVNSIADIA
TNVGRNGNFLLAPGASRSYTLYAEREGAFAATSYGATFGGEGTAGNVGNGLFGQVVVVPKGGRTYRNTVT
EEEMRLASTGRTPAGQPIIDYEARYPQREPWISEGKAGLPILNMVDGNEIIASDTDAIVMGPNPDGSFPP
STYPLESIGKRNPALPNRLEPFRDFASAFHDEAAVTQAFPGYWADPVFGHVLEPTRDSFMINYGSGGIGA
EVIANRLGVGPMHDCLSCAYEEFFLSAHTVGDVAMLVDVPANVGLENIRPGQVPPPDATGIKASMALYPA
EPSNVNHSYIGDFVKFRNTHQGHEQHIFHLHGHQWLFNPNDDNSDYVDAQGIGPGSGYTYEIANGGSGNR
NRVAGDAIYHCHFYPHFAQGMWAMWRVHDVFEEGTRLAVSEQGEDGFHSEPFALRSGLPAAGARALPDGE
IVAGTPIPAIVPLPGKAMPPMPGKVAVVPKLGERLVAADDDDDDGEGDDGGGGSRAIGSVALVDRSEANR
NADGSLKNPGFPFWIGGMESTVGQRPPTPPLDMLDPAKAQALRDSGNALWANLDPAQVGGWDGGLPRHAL
DGWAAGGEAEVVTSALDFSKVITRAKAVFFPEEGTDVEQAAMAFHAKAEHPSYAVLPGGQVVPAAFRTNG
ALPVAGAPFYEPCMDDRQKRLTSAAGAGEFNSGERLDGMSFTGSSPFTADRPRIYKAANIQFDAVFNKVG
YHFPQTRILALWEDAWPVINKQRPPEPLVMRMNTFDCTMYQQTNLIPAFYELDDYQVRTPTDVIGQHIHL
PKWDLTAADGSANGWNYEDGVLSPATVVERIHAIREFNGCQAGDPRDGTADCPKAKAHPYFGQYGRADWL
GARTAMQRWFADPVVNTHGVDRGLGNIFTHDHLGPSTHQQLGLYATVLAEPAGSTWFHAETGEPLYTGRQ
DGGPTSWQAVIATGDLDGDGKNDSFREFFLEYSDFQHAYEAGVYVGAGPDGVPDPGAYPATADSFRYAIN
PPVRKSASTLLESVVEAAGGEVPGCPSRPCPQAISVDDPGIFVVNYRNEPLGLRVYDPNRIAPDGKPGMQ
ADGLAGDLAYALQSRTDRAIPALNLAPSAITSAVGPTGGTTLFPPHINKAGDEPGDPFTPMLRTYSGDNV
RLRVHAGGHEEEHNVTLHGVKWLHSGTGFGNSSNSGWRASQMVGISEQMGFVAPVAMLSSSAADTGDYLY
SMDASLEGYWNGIWGVMRNYTASRNDLFALPNNPKPVAARNTTAFDGICPRFSPNPNGIGTRPTPQRNYE
VVAALANDILDNPLGLTIGDPAGAGQHVGGPLNPAGGTLVYNPRAVSIPQVTVVDPEDGEVFTIGGQSGP
LHDPTAILYVRKADLDPVTGKLKPGVPVEPLVLRAAAGDCINVTLENRLPTVMPDLPNYAVMQGVVKRDR
FGAQGSTTFNNNLMRPSSHVGLHAQLLAYDITKSDGFNVGINPVQTVPPRAGSSGAYPTRTYQYYAGHLE
REGKPVSQLGRNVDNINATPIEFGGLNLLPADPIKQPQKGLAGAMSILPLGATWTEDASSRAAATVQPPG
QPAYRDFSLVWQKGLNMRWANGRPVENIASEGFGVPADPQDNSGMAINYRTEPLWYRFGLAPDAPFGRAG
GHGWGDIPNAHMAYSNALVGGDPVTPILRVKPGQPFRTHVLMPSGGSRGSTFQLDGHVWPLNPFQAEKSD
SYGYPMKYPGVGSVRFGYNPMALYIGAQESVLPAAHFSFMFPSAGGANAVPGDYLYRDYAGFGNASGLWG
LLRVT
>gnl|CDD|469376 NF041488, caps_synth_Cps4B, capsular polysaccharide biosynthesis protein Cps4B
MIDIHSHIVFDVDDGPKTLEESLALIEESYRQGVRTIVSTSHRRKGMFETPEEKIAENFQQVKEEAEERL
PDLTILYGGELYYTSDILEKLENKQIPTLNGTRFALIEFSMNTPWKEIHTALSNVLMLGITPVVAHIERY
NALEFNAKRVQELINMGCYTQINSSHVLKPKLFGDKYKFFKKRARYFLEEDLVHCVASDMHNLDKRPPYM
KEAYQIIEKDYGRERARELFKENPQTLLENQYI
>gnl|CDD|469377 NF041489, sigO_reg_RsoA, sigma-O factor regulator RsoA
MNGPFEFNKEKTDTDEIELLIARFSPMIKKKLSNTSYQEREDLEQELKIKIFEKADMLLCQEVPGFWEFI
LHLINEN
>gnl|CDD|469378 NF041490, trans_reg_SutA, transcriptional regulator SutA
MSDEELEQDDLEGGDEDDGEELAAADDGDDGDDDGDDDESPAPAAKGKAKAAVEPEELPSVEAKQKERDA
LARAMEEFLARGGKVQEVEPNVVADPPKKPDSKYGSRPI
>gnl|CDD|469379 NF041491, membrane_YniD, small membrane protein YniD. YniD, an uncharacterized protein, is named for the founding member of the protein family in Escherichia coli K-12. Length and hydrophobic character are well-conserved and most amino acid substitutions appear conservative, suggesting YniD is expressed and functional in some way
PTKRFAKKHWKMVLVLLCICGALLLLRWAAMIWG
>gnl|CDD|469380 NF041492, MobF, MobF family relaxase
MLSIARIGSAGGAARYYTEKDLDNYYSEDGGTPAGRWFGKGAEALGLSGGAVDGERFKALLDGRLPDGER
LRRRRKGAGRHRPGYDLTFSAPKSVSLLALVGGDKRLIEAHDEAVKEALEYLEERLAQTRVTVDGKGRTS
LEKTGNLVAALFRHDTSRAGDPQLHTHAVVMNMTQRPDGKWRSLDNEELYKNQKALGAIYQAELAEELQA
LGYEIRETKNGQFEIAGVPREQIEAFSKRSQQIEEWLGENPATLASAALRQIAALDTRKAKEADVDPEEL
EAEWREEA
>gnl|CDD|469381 NF041493, MobT, MobT family relaxase
LKEKRLAYGVSQNKLAVAAGITRQYLSDIETGKVTPSEELKETLLEALERFNPDAPLEMLFDYVRIRFPT
TDVQHVIEDILKLKMDYMLHEDYGFYSYTEHYVFGDIFVMVSPDEEKGVLLELKGKGCRQFESFLLAQHR
SWYDFFMDALVEGGVMKRLDLAINDKTGILDIPELTEKCRNEECISVFRSFKSYRSGELVRREEKPDMGN
TLYIGSLKSEVYFCIYEKDYEQYVKNGIPIEEAEVKNRFEIRLKNERAYHAVRDLLTYYDAERTAFSIIN
RYIRFVDKDETKRRSDWKTNERWAWFIGENREKLKLTTKPEPYTFERTLNWLARQVAPTLKVAKKLDEIN
QTDIIKDMIRHAKLTERHEKILEQQTASTEEVI
>gnl|CDD|469382 NF041494, MobH, MobH family relaxase
GLPVLPADELLATQQELIARIRQLLGLSDEEFERLYLPVIERYAAFVHLLPASEAHHHAGAGGLLRHGLE
VAFYALRARDGHLLPPGATPEERRALEPRWRYAAFLAGLLHDIGKPLTDLRVTDRDGSLQWNPYLGPLHD
WALRNGVDRYFVRWRAGRDYRLHEALSLLLLPRILPPEALDWLAEDPELVSALLAALSGQDDAGVLAELV
RRADQASVARDLGGDRSRYGATALGVPLERYLIDAMRRLLKEGSWKLNRPGARVWLTGDGLFLVWKTAAD
DIRALLEQDGIPGIPRDPDRLFDILQEHGLAEPNPEDGKAYWRVQIPEILGEVWLTLLKL
>gnl|CDD|469383 NF041495, MobB_relaxase, MobB family relaxase
MYITITPQKLGGNNKGSSADFVNYLEKENEGKEPEEPEHFFNQYGDEISAEEVIKEIDGNTAKLKKKEPK
FYSITISPSQKELKHLQNDSEKLKQYTREVMKEYAASFNREIRPVTVDDLKYFAKIEHQRTYKGTDKEVK
ENQPYATKILELKNEIRKIERGELQGNIKKLQKKIKRLEREAPHQQNGKRIVQGMAKPGNQSHIHIIVSR
KDATNSYSLSPGSKYRASEVELNGKSVKRGFDRDAFFQSAEKTFDKLFGYKRNYVET
>gnl|CDD|469384 NF041496, MobQ, MobQ family relaxase
MAIYHLSVKIISRSAGRSAVAAAAYRSGEKLTDERTGETHDYTRKGGVEHTEILAPPNAPPWAADRETLW
NAVEAAEKRKNSQLAREFEVALPHELSAEQRIELVREFVQENFVDKGMIADVAIHDPDRDGDQRNPHAHI
LLTTRPITPEGFGAKSRDWNDKENLEEWREAWAELCNRALERAGSPERIDHRSLERQ
>gnl|CDD|469385 NF041497, MobV, MobV family relaxase
MSYAVLRVEKLKGGNLAGSQEHNERETENRTNPNADPSRTHLNFELVNGPDGPIDYLEAIKERIAENAGI
KRKIRKDAVRAVEFILTGSPEFFKELADPGELKEWFEDNYDFLADRYGEENIVSAVVHLDETTPHIHATV
VPITEDGRLSAKDVFGRKKLSQLQDDYAEAMKKYGLERGISGSEAKH
>gnl|CDD|469386 NF041498, MobP2, MobP2 family relaxase
VVLKSKFVTASAKKFSNYIDYIDRDEAKRKKNNNSSNDETDDLKDFSGYNDYMGNPEKSSGLFTSDSDHL
TDEEKKELKELFDKAQKNGSVMWQDVISFDNDWLEENGLYDPKTHTLDEKKLKEAVRKAMKTMLKKEGLE
DSAIWTAAIHYNTDNIHIHVATVEPEPTRPLMLFKETGEVYGEPRGKRKLKTLDAMKSKFANELLDRTKE
LKRINELIRNTLVQSKKKDESLSEDRELKELFKEIYEQLPEDKRQWQYGNNTMNPARPLIDELTDKYLEK
YHKEEYKEFHQLLDKEVEFYKEAYGEGKKRYKDYKENKLDDLYKRMGNAILKE
>gnl|CDD|469387 NF041499, MobP3, MobP3 family relaxase
YIATREGVDTKKQEQLIEGLLGKFPEAKELFEYEDYLENPTRENASNYVKYIAERPRVEKLGSHGLFTDE
GEPVDLSQVAEEVSNHKGNVWRHIISLRREDAARLGYDDAEAWQALLRSHIPEIAEAMKIPPENLRWYAA
FHNETHHPHVHVVFWSKNPKEGYLTKQGIEKIRSALAKEIFRQELLSLYEEKTESRDELKEEAKDILEEL
IKEIKSGLLEPPLIEELLEELAERLKELSDKGRKAYGYLPPEVKAKVDEIVDELLKDERVAQLYELWLEL
KEELASTYTDDPEERLPLSRQKEFKSIKNRV
>gnl|CDD|469388 NF041501, cola_mem, FGLLP motif-containing membrane domain. Members of this family average about 700 amino acids in length, with variable N-terminal regions but a shared hydrophobic C-domain, modeled by this HMM, about 300 amino acids in length
AIPTPSEVSWDLRSLAVSAALAALLLLLVGFPAEAFNKTLEEHRDRIRRWRRRLRRRLRRRRARPRLPPW
LRLLAFALLGAALTVLADPGFGPDGTTLLLFAGLLVAVLLVTLAYEGPKEAYLRRVRGIRGALRVLPAAL
AVAAVCALLSRVLGFPPGYVYGLVAGFAALGERGRDAPTRADEGRAVLVGAVCLLVLSVAAWVAWAPVHE
AARAADAGFWLRVADAALATVFVAGVQAVVFGLLPLRFLDGYALKRWSKAAWAALYAVALFLFVHVLLHP
PSEVDAGPRGASLLRALALFVAFGVLSLAFW
>gnl|CDD|469389 NF041502, integrase_1, site-specific integrase
GYEFDPNDDRWVLDKNVSINFSLLPELLSDELLEGFKKTLAWYAENRSASHTKNMFERFKHFLRFTGASK
ITSEDLINYRASLDKKTEWYLGALRGFLKKWHDLGYPGISDDVVDLLDSWRLKGNEKGVAVLTMDPEEGP
LTDIELQAINEALNNAYAEGEISLEEYALALLFSATGRRPIQIAALKVKDLIVSSKKDGEPEYVLNVPRA
KQRGQGFRSEFKPFAITEDLGLLLENQAEEVIKKFESLLGRKLDPEEAKELPLFPDWERLKELSSSEELR
ELLKSDRLHITASSLTNTLKKIAKKLNVISERTGEPIHITARRFRYTLGTRAAREGHGELVIAELLDHSD
TQNVGVYVENTPEIAERIDKAVALQLAPLAQAFAGKLVDSESDAVRGNDPSSRIRNEDGKPVGSCGTHGF
CGAGAPIACYTCNHFQPWLDGPHEEVLDYLLAERERLLEITGDLRIASINDRTILAVAQVIQLC
>gnl|CDD|469390 NF041503, WZX_like, O-unit flippase-like protein
WGYLAQFLNIGSGFLLLPFILKYLPPEELGIWYIFLSMSSLVNLFDFGFSPTIIRNVSYVWSGAQKLKKE
GIDEIKSSDEINYSLLKRLISDIKKIYRIISLLALFILLTGGTIYIYSITPNDIKAEVLISWLIFSLSLI
LNLYYLYYTPLLLGRGEIKEANKANIISRLSWLLLSILGLLLGPGLLGLSLAFLLSVIINRILSYRFFNR
NEYIKELKKVKKEKKSTIPIIWHNAKKLGLVSLGAFLINRANILIAGAFLPLSAAGSYGLTLQIFMALSA
VSNVYFTTKIPKLSQLRVKGNSEELKKLISKAVLISLLIYILGFIGFVLLGPYILELIGSKVGLLPLKYL
LLLGVILLLELNHSICATIITTKNKVPFVKPSLISGFLIVLLSIILLKYTNLGILGLILAQGIVQLAYNN
WKWPLVVYK
>gnl|CDD|469391 NF041504, AccA_sub, carboxyltransferase subunit alpha
WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRH
NFGMARPEGYRKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVII
GEGGSGGALALANANRVLMLEHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPE
PLGGAHRDPAALIAALGDAIEEALAELAGLSADELIAQRREKFLAMG
>gnl|CDD|469392 NF041505, HrpD6, HrpD6 family protein
MFDAMTDSITQDMNKILQTKAEDPSGERLRNVEAALDATAQQIRQHWSAASDQAARNDFNVLHEGLNAAR
NIVAHIAGMP
>gnl|CDD|469393 NF041506, VapD, VapD family protein
RKAINFDLSTKELKKYFPDTRKAYNDIKEFMLENGFEHRQYSGYISKEPLSTLDIYKLMEKLGEKFPWLG
SCVKEFDVTDIGEQYSLKETI
>gnl|CDD|469394 NF041507, HrpE_Xanth, HrpE family protein
SLSSRFGQGMDGLTGGLSNGASGAAALAGSDGQMGSLLGDMGASDEAQERMNNKITMLKNELDFNVALNK
FIGKAGDNAKQLVGQ
>gnl|CDD|469395 NF041508, BacL2, BacL2 family protein
WEEVEELVDIYVNENDEEILEEIFECLEPYIKKCAKNAVFKAENYGVYIPFEDFYSNYLLALWEAIEDFR
SKTESTFKNIVLRRLFIAEKKVWRLYKKKGNDSNDKNGITYDSARWESLDRLSNTCESSLAEIIIEEALE
LKEILENFAKKNPRYAKFISLLSLGYSGKEAAKLLGIGDNYDAKVRKKVQRAKESFKKYL
>gnl|CDD|469396 NF041510, AMED_5909_fam, AMED_5909 family protein. Most members of this family of uncharacterized proteins are about 80 amino acids in length, and are found in members of the Actinomycetota, such as the genera Amycolatopsis, Lentzea, Pseudonocardiales, Saccharomonospora, and Saccharothrix. The family is named for one of its members, AMED_5909 from Amycolatopsis mediterranei (ADJ47652)
REPRTLAEAHEALVRLRPAPDAPPAEWRAFYRRSARVYARVAETDRGHHHEALYWAGREREKAEEIEAR
>gnl|CDD|469397 NF041511, PA2816_fam, PA2816 family glutamine-rich protein. Members of this family, including PA2816 from Pseudomonas aeruginosa, average about 140 amino acids in length, with an N-terminal signal peptide. The last 100 amino acids are extremely glutamine-rich. The family appears restricted to the genus Pseudomonas. The function is unknown
RILPLLLAGLLLVGAAQGADSWLYPSRPRPPPTPNLVIDPQQRQQDSLRRQAEQRRRQQQDQRLQYEDQR
LQMKQQQLKRQQDAQQRQRQQRRLQDQMIQRQQSDLQQFRLQQQQQQLDQQRQIIDNRRRQIQSQPIR
>gnl|CDD|469398 NF041512, PA2817_fam, PA2817 family protein. This family is named for uncharacterized protein PA2817 from Pseudomonas aeruginosa. Many members of the family have been annotated previously with the name dehydrogenase, but no source for that annotation, nor homology to any characterized enzyme or solved crystal structure, could be found as this HMM was built
MASPHLEHHLALLAHLRTILVALGEAEQVPEESHALFLERFDELLALLPQDPEESQYLGQDLICQVIRRY
PQIAHLVPRDLLWFFGGDCLHFMPDEEIELYQQLDERRYEAEQNGEPFDWNQEKQLLALLNDSPKH
>gnl|CDD|469399 NF041513, formate_DH_Act, formate dehydrogenase. Members of this family are the enzyme formate dehydrogenase, of a type found in the Actinomycetota, as in the genera Streptomyces, Nocardiopsis, Gordonia, and Saccharomonospora. Many are selenoproteins
TWLLSWPVYRQLTGGDPLGRGAAARSARTRALRPRTATADRVVRSVCPYCAVGCGQKVYVKDEKVVQIEG
DPDSPISRGRLCPKGSASLQLVTGPTRVTTVLYRRPYGTEWEELDLDTAMDMIADRVLDTRRETWQDEDD
DGRRLRRTMGIASLGGATLDNEENYLIKKLFTALGAVQVENQARIUHSSTVPGLGTSFGRGGATTFLQDL
ANSDCIVIQGSNMAEAHPVGFQWVMEAKARGATVIHVDPRFTRTSALADLHVPIRAGSDIAFLGGLINHV
LSNELYFREYVLAYTNAATIVSEDFRDTEDLDGLFSGFDPETGSYDPASWQYEGVEVAAAAGQRDQLYDS
RGGAHESARGEEHGSGGAPVAGAPRRDETLQDPRCVFQILKRHFARYTPEMVEEICGIPRELFLKVADAL
TANSGRERTTAFCYAVGWTQHTVGVQYIRAASILQLLLGNIGRPGGGIMALRGHASIQGSTDIPTLFNLL
PGYLPMPHAHKHEDLDSYVEANASQKGFWANMRAYTVSLLKAWWGDAATAENDFCFDYLPRLTGDHSTYQ
TVMAMLDGKVKGYFLMGENPAVGSANGRLQRLGMANLDWLVVRDFSLIESATFWKDGPEIETGELRTEDI
GTEVFFFPAAAHTEKSGTFTNTQRLLQWRHQAVEPPGDARSDLWFFYHLGRRIREKLAGSTDPRDRPLLD
LTWDYPTEGPHGEPDAEAVLAEINGYDLSGRPLSAYTELKDDGSTSCGCWIYCGVYADGVNQAARRKPGR
EQDWVAAEWGWAWPANRRILYNRASADPEGRPWSERKKYVWWDAEAGRWTGYDVPDFPVDKPPDYRPPPG
ATGPAALSGDDPFIMQADGKGWLFAPAGLVDGPLPTHYEPQESPVRNPLYGQQRNPARKVYPREDNRYHP
SGGEPGAEVYPYVFTTYRLTEHHTAGGMSRWLPYLAELQPEMFCEVSPELAAERGLENGGWATIVTARGA
IEARVLVTDRMTPLRVQGRTVHQIGLPYHWGPNGLVTGDAANELLGITLDPNVHIQESKALTCDIRPGRR
PRGPALLALVREYRRR
>gnl|CDD|469400 NF041514, Legion_RtxA_N, enhanced entry virulence factor RtxA, N-terminal domain. This HMM describes the N-terminal, non-repetitive portion of the Legionella virulence factor RxtA, named for the presence of tandem repeats-in-toxin (RTX) domains. RtxA can be four to six thousand amino acids long. In some isolates, the toxin is divided into two tandem ORFs but presumably re-form by recombination. RtxA is involved in adherence and cell entry
MLAESVIGIVRAVNGLLEKVNAQGQASLVKSGARLEEGDVLTLLSGEAYIQFIHGFPEALALEKPVKLDG
VSPTLQYGVEDLKEQMVQEAIAKGIDPSVILDVLGSAAAGAEAVGSGGDAFIIDPLFGFGQVTAGYPTGP
ISFAYEADTQQLFWFVPEETGVIAESELTTEPESIPQIPQFTTNQAVLTVFEDALPSGIPDSAGQARTAS
SSLSTLLTSSPDVAASFAFNTNLSALPTLKSGGIDLDYELSSDKRTLTASEPPGAEVMQFELTADGQLTQ
TLMDSIDHPTADSDDSEWMRLDLSPLIDVTFTRTSDGTVLESRTLPANAVVAGIQ
>gnl|CDD|469401 NF041515, GspC_delta, type II secretion system protein GspC, deltaproteobacterial-type. Members of this family are GspC (general secretion protein C), a component of type II secretion systems (T2SS), of a form found prmarily in deltaproteobacteria. This HMM is designed to be complementary to other HMMs that identify GspC rather that to separate a distinct subtype
KRYFWVVNLVLLALAAYFQASGVNALVAAALLPLPPAAAAPAAPPAAPPAAARRAKDADAILARNIFDSV
TGPLDPEPEEPAAPEEPPDGDDPAEPPPCSGRVRLVATVVSDDPEWSFAAIADGGGKTRLYRVGDEVDGA
TVVAIGWDRVWLRNGGRRCQLDLFDGAPPPAPAPPAAPAPAPPPPARAGGALPPEIASGIKKVSDTEYEI
DRSLVDKVLENQAELMRQARIVPEFENGKVVGFKLFGIRPGSLLGKLGLQNGDVLQSINGFDMTSPDKAL
EAYARLRSADHLTVSVERRGKPVTLDYNIR
>gnl|CDD|469402 NF041516, PA2928_fam, PA2928 family protein. This family is named for the locus PA2928 of Pseudomonas aeroginosa PAO1, as the family member most frequently cited in the literature, although PA2928 itself is significantly shorter at the N-terminus than most other members of this family, and is probably non-functional. WP_017001489.1 represents an intact equivalent to the PA2928 pseudogene
LFLLLLIPLVLFGGLFFGGSYLAGPEPSIEAQSGAVFYTVDGRDVALVPYERFGANGMSNGITSGMSQFR
LAAVDLATGEKLWDKKLSDELSWEAYLLGATDRYLYVATDKGLYVLDLATGKVVADEKELEGLGPALKDN
LSAARAAYAYDDDNRALYFYGLDGRYYQIDLDTLTATPADPATAPTYAGLLFAEEAAKGRPATFLSDKEE
AALEDERVALRERPRGALYGGVLVRVGGDGDLTPLGDTVFLDGGFLLDPTTLEGAADGHVLVVHKRTVND
DANLLLSAVDLETGKVTWTLPLGYSSPSRAFTLPDGLTLLGAGNPEGGDLLKIDLKDGKLTRYDV
>gnl|CDD|469403 NF041518, choice_anch_Q, choice-of-anchor Q domain
DPLLGPLADNGGPTQTHALLPGSPAIDAGDNAGCPATDQRGVARPQGTACDIGAYEFQ
>gnl|CDD|469404 NF041519, bluetail, bluetail putative surface-anchoring domain. Bluetail is a short protein domain, about 55 amino acids long, found primarily in Cyanobacteria (blue), at the extreme C-terminus of proteins (tail), that otherwise may differ in length and domain content. This pattern of occurrence suggests a role in anchoring proteins on the cell surface, although bluetail does not have the tripartide structure of signature motif, then transmembrane alpha helix, then cluster of Arg residues like the sorting domains PEP-CTERM, Gly-Gly-CTERM, MYXO-CTERM, etc
ALGANEAALFTFGSRTYLAVNDGTAGFSASTDLVIEVTGITGDAAAGTLTVNNYF
>gnl|CDD|469405 NF041520, flexitail, flexitail putative surface-anchoring domain. The flexitail domain is found several hundred proteins from metagenome-assembled genomes (MAGs) of Chloroflexi bacteria. As a rule, the flexitail domain, which averages about 110 amino acids in length, is located at the protein C-terminus, and is separated from other recognizable domains by stretches of low complexity sequences. This resembles the pattens seen for short, tripartite, C-terminal protein-sorting signals for surface-anchored proteins, such as PEP-CTERM, GlyGly-CTERM, or MYXO-CTERM, or the LPXTG signal in tripartite form as described by TIGR01167, or longer C-terminal sorting signals such as type IX secretion system (T9SS) signals. At the time of model creation, no example had yet appeared among the more than 200 million collected proteins from genomes of cultured prokaryotes in the RefSeq collection. This suggests that the flexitail domain may represent an adaptation to a lifestyle that has not been conducive to isolation in culture conditions known so far
DTDGDGCTDGRELGPDETLGGLRDPLNPWDFYDVNGPRDGVIDLPNDILGVILHFSPGGDDPPGYDVAFD
RGPSIGPNPWNMGPPDGVIDLPNDILGVILQFGHDC
>gnl|CDD|469406 NF041521, HhoA_HhoB_HtrA, HhoA/HhoB/HtrA family serine endopeptidase. Members of this family include the paralogous serine proteases HhoA, HhoB, and HtrA of the model cyanobacterial isolate Synechocystis sp. PCC 6803. They resemble the paralogous trio of serine proteases DegQ, DegP, and DegS of Escherichia coli
NFVAAAVEKVGPAVVRIDAERTVVTQVPPFFNDPFFRRFFGSDIPPPPPQERVERGTGSGFIISSDGIIL
TNAHVVDGADTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEAKNLPTVPLGNSDQLQPGEWAIAIGNPLG
LDNTVTLGIISATGRSSSQVGVPDKRVDFIQTDAAINPGNSGGPLLNARGEVIGINTAIRAGAQGLGFAI
PINTAQRIADQLIAGGKVEHPYLGIQMVTLTPELKQEINSDPNSGFTVPEDEGVLIVRVVPNSPAARAGL
RAGDVIQKINGQPVTTAEQVQQIVENSQVGQTLQLEVQRNGQTQTLTVRPGALP
>gnl|CDD|469407 NF041522, TPR_sll0314, Sll0314/Alr1548 family TPR repeat-containing protein. Members of this cyanobacterial family have signal peptides and are called periplasmic. The body of the protein contains regions of homology to tetratricopeptide repeats (TPR). Member protein Sll0314 was found to be upregulated as part of the iron deprivation stress regulon
SPALAGDPFRTSNPRPIGDKTEAAFKAIFKEGNYPAAKEYLQQALSSEPNEPLAYAMRASLAYTEQDWEG
LKTYAQKTLETAQKLIATDPLRGNLYTAVGHFLEGAYILKTEGTVKGAPQALSKLQQVFQYLDAAEAIDP
NDPELNLIKGYMDLMLAVNLPFSSPEQAIERLEKYAAPDYLAYRGIALAYRDLKQYDQALEYVNRALAAT
PDNPELYYLKAQILRKQGKKDKSQQLLQEALANFDKALAKKDQLPPSLVKQIERERRKAQNRLDN
>gnl|CDD|469408 NF041523, post_COAP_1, post-COAP-1 domain. Post-COAP-1 was identified as a C-terminal domain, about 115 amino acids in length, found in a subset of proteins with the choice-of-anchor P (COAP) domain (see NF040603). This domain is seen primarily in non-cultured prokaryotes with a broad taxonomic bacteria and archaea
FVTGGGWITTPSGAKANFGVAGGIKPGGFWGHLNYIDHGTGMKVKGTSVTGYTGVDPTTRRIEGTATING
QGGFTYTVDVTDNGEPGRGDTFSITLSNGYSASGTLAGGNIQLHK
>gnl|CDD|469409 NF041524, Gltr_6, family 6 glucosyltransferase
MKIGILYICTGKYSIFWKDFYLSCEKYFLPGAEKEYFVFTDPDDLYFKKNNNVHVIYQENLGWPLNTLLR
FSMFLKIKEELKEFDYLFFFNANALFVKPISAEILPTEEENGLVGVIHPGYYNKPPIEYPYERRKKSTAY
IPYGKGGYYFQGGLNGGKTKAYLKLIETCSLNIEKDLKNNIIAIWHDESHLNKYFLDKKPKILSPAYGYP
EGWNLPFEPKIIMRDK
>gnl|CDD|469410 NF041525, HrpD5, HrpD5 family protein
TKEIRVLTGRHAGARLDLSPGRYTIGADDDADIQISDWTAPPLQLEVDEDGQVRIRRSDAAPAVPLEDFV
PRRFGDIVLCVGPADAAWPSDLELLERLLSPAPAAAAAPAPRAVSRARRRRALRAAVGAALVGAALAAAA
LLPAANPAHASAAAPPPAPEPLLAQVRRALARLGLPELRVRQQGDRVLVEGLVASSADAAALRRALDRFA
PGRVVWRVAVADEVAQSLRESLGDPGLSVRYRGRGVFSVTGVAQHADRVRARLERLRADLGPLVRRIDVD
VTRQDPPDAPPANYDSALSVDGLHYVETPDGTKH
>gnl|CDD|469411 NF041526, Hpa3, Hpa3 family type III secretion system protein
AFFSQLGLHLGLPDDLVQRLGEGEPFLGPAGLLCRVHTQPQEGGWAAFPEVILPLAARELGGDEVVRLLA
LQEQLLTEYGWRLGLSDLGLLCLCPLLLARTPEDVAAALDRGQVLARVVLDAL
>gnl|CDD|469412 NF041527, SCO1860_LAETG, SCO1860 family LAETG-anchored protein. Members of this poorly characterized family, including SCO1860 from Streptomyces coelicolor, are surface proteins whose C-terminus contains a variant type sortase recognition and cleavage sorting signal. The sorting signal motif, LAETG, is compatible with processing by a SrtE family sortase enzyme
RLAAVAAAAALAAGPVALAGAAAAHATGDETTGRASAVVLRTGLDVSLLNKTVNVPLNATLNEVQAPASA
EKTALTVRLDGVDGGRPVSVLRADVATARATVDGGTAEGYANLARARVHVPGLPLLPLIEVEQVTSRAVC
EAGKRPVAESNLLGPVTVLGKKVTLSAGGTTTVDVPGVGEVRLDLSRTETTSRTAAATALELKVSVNPLK
LNVAEVEGTVTLAEATCETPAAPGEPPAEPSEPEEAPAEEATGTGPDVKPPGEAAADPGENLAETGGSSA
TPYIAGGAALLLAAGGGALALARRR
>gnl|CDD|469413 NF041528, strep_LAETG, LAETG motif sortase-processing domain. This HMM describes a Streptomyces-specific variant of the widespread LPXTG motif-containing sortase recognition and processing domain
DLAETGGSSATPYIAGGAALLLAAGGGAVFLARRR
>gnl|CDD|469414 NF041529, LvhB7, T4SS-associated protein LvhB7
MKWLLSVLLILLLTGCSKPPDLDAPCPDFGRYCPQYPINEDSLVE
>gnl|CDD|469415 NF041530, LvrD, T4SS-associated protein LvrD
LLKGLMVLLGALTLCACHHENPLKTHSKKDSLTFLLNASANAEKRLHFPIQKDSYGYAYLECMEGKQSPE
ISCDALYQGMVSFAKEGHYSGFQTLTLADLTDSNVFESLADDYAETAATHEPHFVS
>gnl|CDD|469416 NF041531, HrpV, HrpV family type III secretion system protein
MNDSCPQVDSLAAFLSLLQLHQSCRWSVQQGVELVALCGERGRELMLNLQPGQQPPGLYRRLLRRRAQQA
ERYDGCYLCLNGERVLSCWWQLPEEPADDKQQIAQLFSLAGITLPGL
>gnl|CDD|469417 NF041532, HprT, HrpT family type III secretion system protein
LAGCASRHQGCTGDSCSRPQSSARQLVIWWPPDMRNGPGPSGERADYTVVS
>gnl|CDD|469418 NF041533, trans_reg_TagK, transcriptional regulator TagK
EAHAPLMIDLLAYIEQHIGEAELGTESLQQAFALSRASLYRLFQSRGGVASYIREQRLCTAHRYLQAYPE
CSLTWLLYEMGFASERQFQRAFQQRFGMPPMQWRRQCRAAPQTHAPRRGHYMPMWRFMRELSQQDLPEDA
SVRNGSVNPTQPAPLLHTEALRRLAQPARRFAAQPEPM
>gnl|CDD|469419 NF041534, rodZ_Strepcoccus, cytoskeleton protein RodZ
MRKKTIGEVLRLARINQGLSLEDLQRKTDIQAKYLEALEYNDFDQLPSPFYARSFLRKYAWALDLDEAIL
LDAYETGSMVTYDEVGEDEEEDFRSRRSRKKKKSYLPLFYFLLAALSILIFVTYYVWNYIQNQAPETPSS
SSYSVVSQTSSSSSSSSSSSESSSSSSSSSSSEKLTVSGGGDNLTVTYKGAKEPVELTLSVSDTTSWVSV
SDTDLAGGVTLSPENPSVTTTLSPGTTATITLGVVKGVTVTIDGQKLDTSALTSQTGTITLTIEQ
>gnl|CDD|469420 NF041535, TonB_rec_PqqU, TonB-dependent receptor PqqU
VVVAAPPGLSELDTPAAVSVVNGDDMRQAAPQINLSESLGSVPGLQIQNRQNYAQDLQLSIRGFGSRSTY
GVRGVRIYVDGIPATMPDGQGQTSNIDLNSVDHVEVLRGPFSALYGNASGGVINVTTQTGSQPPTLEAGS
YYGSYGSWRNGVKASGATGDGTHAGDVNYTVSASRFTTHGYRDHSGAQKNLGNAKLGVRIDDVSTLTLLF
NSVDIDANDPGGLTESEWRDNPRQAPRADQYNTRKTVKQTQAGLRYQRQMSENDDLSVMTYAGERETTQY
QSIPVAPQLNPTHAGGVIDLTRHYQGIDTRWTHRGELGSVPVTLTGGLDYETMTEQRKGYENFTLNNGVP
ELGEKGALRRNERNLMWNLDPYLQTSWQLTDKLTLDAGVRYSTVWFDSNDHYITAGNGDDSGDASYHKWL
PAGSLKYAVTDAWNVYLSAGRGFETPTINELSYRSDGQSGLNFGLKPSTSNTVELGSKTRIGNGLLTAAL
FQTDTDNEIVVDSSSGGRTSYKNAGKTRRRGLELGLDQQFAYDWRLKMAWTLLDATYRSNVCGASQDCNG
NRIPGIARNMGYASLGWQPEEGWYAGADVRYMSDIQANDENTAQAPSYTVVGLNTGYKFNWDNWTLDLFG
RVDNLFDRRYVGSVIVNESNGRYYEPAPGRNYGVGLTLSYAFE
>gnl|CDD|469421 NF041536, ArsM_DUF2284_UU, arsenite methyltransferase/DUF2284 domain selenoprotein. Members of the seed alignment for this protein are selenoproteins with two selenocysteine-containing motifs. The first is in the N-terminal arsenite methyltransferase region, typically QUEGG, and the second is in a C-terminal DUF2284 domain, typically TUPSG
METQITADDKERIEAGIREKYIKVAKTPEGQFKYPTGRAGLEALGYDPSLLRSLPDAVAASYCGVGNPFS
LGKINEGEAVLDIGCGAGVDTILAAMMTGTTGKVVGVDLVPEMLDRAKKNLQMTDLKNVSFKKSSGEKLP
FPDNSFDVVISNGVINLIPDKERALTEAFRVLKPGGRLMIADQIATGELEKDLKARIDSWFQUEGGAIPG
KDFLALLQEAGFEDVELVAETGFNSSPKTKGVLIRAEKPMTLDKKQKPPKKDDISDEKKSSEPEKKKEPT
IEDVLEKAYELGAEKAKIIDTQTIVVEKWVRWKCLYGCPFYGKDGYHPPLAPDAEETKEVLKEYSKAILL
NGPKGKALTEIAVRLEGEAYHMGYYKAFALTALPSGAGGESNPGATUPSGENEAPCGPQKSEETKNRIRP
MMEACGIDVFKTARNNGFEIDTRKETFGRWNFFAMVLIE
>gnl|CDD|469422 NF041537, ArsM_AhpD_UU, arsenite methyltransferase/AhpD domain selenoprotein. Members of the seed alignment for this protein are selenoproteins, most with two selenocysteine-containing motifs. The first is in the N-terminal arsenite methyltransferase region, typically UXGGA, and the second is in the C-terminal AhpD-like region, typically GCEPU
MEAALSNEDRKRIEEGIREKYARVAVTPEGLFSYPTGREGLEALGYDPDILKDLPAAVLDSFCGVGNPFS
LGPIHPGESVLDIGCGGGVDALVAARLVGPEGRVVGIDLSPEMVGRAQENLAATDLKNVSFQEGSAEALP
FPDASFDVVVSNGVFNLIPDKEKALKEAFRVLKPGGRLLIADQVLVGPLPPDVKDRIDNWFRUEGGAIPG
RDFLALLKTAGFVRGELVGETGFNSSPITKGALFRADKPEAASEKGRSMSMETPLNKYQEFFEAAYAEGA
IDRKTKHLIALGASLAAGCEPUTRYCLAVARDLGATEEELQETLAVAMTVGATKIQLLQQRALAS
>gnl|CDD|469423 NF041538, PEP_EDSA_1, EDSAP-1 family PEP-CTERM protein. Members of this family, designated EDSA-1 (exosortase-dependent surface-anchored protein 1), have an N-terminal signal peptide and a C-terminal PEP-CTERM region for recognition and processing by an exosortase
KSLLAAAAAAALALGAAGPAQADVYAYSILDISNLRITNSGGAVLDASDFGTFTATATATLNGVTGNGSG
SGGSGGGSVDVATACVGLDCPAINANDFTPFGPGPGGTYARADSQISGSQLGGGGGGGASAQTIAEASLT
GNASASANINSGTGTTFTFTLGAAGTLTLSFDADPYLQAFLTAGAGPGSLAQANLSFSITITDLTGGTVF
NWAPDGLNGGGTGGETADPFSLNVGVTATTPGGNVYDSAGAGGSFSATTSLLAAGTYTLTINQTTSANAT
QAVPEPGTLALLGLGLLGLGAARRRR
>gnl|CDD|469424 NF041539, choice_anch_R, choice-of-anchor R domain. The most frequent C-terminal anchoring domain for members of this family is PEP-CTERM (see TIGR02595) or a PEP-CTERM-related variant sorting signal domain processed by one of the specialty exosortases. Some member proteins are found instead with dockerin-like C-terminal repeats and a GC motif at the extreme C-terminus. The GC-type dockerin domain occurs, so far, primarily in metagenome-assembled genomes from the taxonomic class Phycisphaerae, within the Planctomycetota, where it seems to anchor a number of otherwise unrelated proteins
SNLPQTDGTGSTVLSNTWLKAQGFTTGSNDGYTLTSVTLRLDTTAAGASLVVRLYSDSGGNPGSLLATLT
NPSLTSGTADYTFTPTSPFTLAANTTYWLVVDSTSGSGSFSWLLASSPAGGPTGWSIADTRLFSSNSGAS
WSSTSSGPNQFAVNGT
>gnl|CDD|469425 NF041540, dockerin_GC, GC-type dockerin-like domain. This domain begins and ends with a near invariant C, and GC, respectively. It occurs strictly at the C-terminus of proteins, and those protein are found almost exclusively in metagenome-assembled genomes of the taxonomic class Phycisphaerae, within the Planctomycetota. It shows apparent sequence homology to the type I dockerin domain (see PF00404), which likewise contains an internal repeat and which appears in strictly C-terminal positions of otherwise unrelated proteins. Type I dockerin domains occur in proteins that are organized by interaction with the cohesin domain (PF00963) in order to form the cellulosome. However, the GC-type dockerin domain described here is uncharacterized, and cohesin domains identifiable by PF00963 are not found in the same proteomes
CPADLTGSGGPGVPDGVVDADDFFAFLDLFAAGDPAADLTGSGDGVPDGVVDADDFFAFLNLFAAGC
>gnl|CDD|469426 NF041541, fosBx1_fam, FosBx1 family fosfomycin resistance bacillithiol transferase. Members of this family, found in Bacillus cereus and related species that synthesis bacillithiol rather than glutathione, are VOC family thiol transferases. They provide resistance to the antibiotic fosfomycin by transferring either bacillithiol or cysteine (but not glutathione) to fosfomycin, leaving it inactive. Note that this family is drawn rather narrowly, and several such families, all non-overlapping, appear in B. cereus and its close relatives. This family includes proteins that have been named FosBx1 (although the original source of that name is hard to trace), and the protein studied crystallographically by Thompson, et al. (see PMID:24004181)
MLKGINHLCFSVSNLEKSITFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFS
VEQEDFERLLQRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREEKPHMTFY
>gnl|CDD|469427 NF041542, fosX-Cc, fosfomycin resistance hydrolase FosXCC. FosXCC (FosX from Campylobacter coli) is rare, mobile antimicrobial resistance protein. Most members of the family are seen not only outside of the genus Campylobacter, but in Gram-positive species such as C. difficile
YGISHITFIVKDLDKATKFFKEIFEAKEIYSSEDKTFSISKEKFFLINDLWIAVMEGEKIEKSYNHIAFK
IDESDYEMYLKRIENLGLEIKSGRKRVIGEGNSIYFYDYDNHLFELHTGTLETRLLRYQK
>gnl|CDD|469428 NF041543, XopA_Hpa1, XopA/Hpa1 family type III secretion system protein
MNSLNTQFGANSSFLQIGPQQNTQSGSNQGNQGISEKQLDQLLAQFIMALLQQSNNAEEGQGQGGDSGQG
QGGNQQQAGQQNGPSPLTQMLMNIVGDILQAQNGGGFGGGLGGGFGGGLGSSLSSDTGSMQ
>gnl|CDD|469429 NF041544, ParC, ParC family partition-associated protein
VVGPTAFKELAAAGSVQGASIRAADKGLVIVLRVGGEDRVLGQYRGGPRYFQSFDGAASVLIQHGITEFE
ADTTGWIPRT
>gnl|CDD|469430 NF041545, GrdB_like_no_Se, GrdB-related putative oxidoreductase. Members of this family are not selenoproteins, but are homologs to the N-terminal domain of GrdB, a selenoprotein subunit in the glycine reductase complex. Members of this family are found in a different context, not near other glycine reductase subunits
KVILIFDQIQAGLGGKERADLPLGGKKGAIGSAEMFEPYLKKVDGKIIATLYCGDGYYLENKEEVSKKFT
AMAKKLKPDVVICGPAFNYPDYAEMAAELAKAINEKTDIPAIAAMSKENEEAIAKYKDKVTIVKMPKKGG
TGLNESLKNMCKLAKKKANKEDLTEFKKEYC
>gnl|CDD|469431 NF041546, ParA_partition, ParA family partition ATPase
IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVVGLARPTLHRELP
SLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNR
AIARTALGREVAEALAEYGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREIRALAKE
>gnl|CDD|469432 NF041547, GntR_LSA1692, GntR family transcriptional regulator, LSA1692 subfamily
YLYEEVADKIEKRIKDGVYGSHQKLPSEYDLAKEFEVSRLTIRKAIDLLIKQQVLVKDRGKGTYVMAQQK
IQSGRGGLQGFTEAAKAYGKTSHTKVLEFEELTNYPEEVKEKLELEENEPVWHIERLRFWDDEPMTVEEI
YIREKYLPELTEEDFEGSLFELIEKKIEIAYSHQEIEAVLVDEELSELLKVKVGSPLLLVHSVTYSVDGY
PILYDTSYYRADKYTFKNTLYRN
>gnl|CDD|469433 NF041548, PssE, PssE/Cps14G family polysaccharide biosynthesis glycosyltransferase
IFVTVGTTRFDSLIKAIDELIEGLIDYEVTFQIGDGKYIPKNGEYFDFLEEIDEYYKKADLIITHAGAGT
IYSLLELGKKVIVVPNLERVDDHQLDLAEYVEENGYALVCYDLDELEDAIKEAENFKPNPYEKNPFFIAD
EIIDFI
>gnl|CDD|469434 NF041549, PssD, PssD/Cps14F family polysaccharide biosynthesis glycosyltransferase
LLIYGSGGHLAQMLRLKPLLDKYDYFLVTEKSDSTKKLEWSYDVHYLLPESRNKNNGLKYLFKFLKNIIK
SFKILRKYRPDVVISTGPGIAIPMCLLAKLFGKKVIYIETWSRFTSKSLTGKIMYKIADKFYVQWEELLK
LYPKAIYGGRL
>gnl|CDD|469435 NF041550, CesT_sub, type III secretion system chaperone
MTSTELQALLERWLDSGEGELTLEIDDGPVALQRRAGGLLCLAALTLAARGDEALLERALRLSAPALRRF
GRDAAALALSPQDGQLWLLMRLEPDDVDALCRCLESLLNQRDVWQSLLAPAARKATPAPRPLHSLAFLQG
GRH
>gnl|CDD|469436 NF041551, YlcI_YnfO_N, YlcI/YnfO family protein. The seed alignment of this HMM (86 proteins after non-redundification to a maximum 80 percent amino acid identity) represents are a large expansion relative to PF13132.9 (3 proteins), named DUF3950. Members are small bacterial proteins, often from prophage regions. This model is short (42 amino acids), which high sequence diversity among seed members, and has relatively high cutoffs for its length. Some family members and additional apparent homologs scoring below the current cutoffs of the model include putative DNA-binding proteins such as HicB family antitoxin components of type II toxin-antitoxin systems
KSTRPTARVPHELREALEAVKLEGESLSQFIVTAVRREIKRR
>gnl|CDD|469437 NF041552, TF_PrdR, sigma-54 dependent transcriptional regulator PrdR
LIPEKYLVKDIMDKDFIKVDEDTTLSEAIDEMLKNNKKEVLVVDEKEKLKGIITITDIAKIVKDKNIFDK
PIKDYMKKDVITISKEESLREARNIMIKNNIGRLPVLENGKVIGVIRQEDIRDYFYMKLEEMGETLKHIL
DNIHEAVCVIDKEGIVILWNKSAEKLYGVKSEEIVGKPLEEFFPNALLLKVLKTKKPIENVYHSPKEGSY
VIISAVPIFINGEFIGVVSTDRDITEVKNLSKELEKAKEKLEYLEEEVKKISEDSFGKIIGKSKKIIKKI
EIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGRKGPFVPVNCSAIPEELFESEFFGYEEGAFTGALK
KGKIGKFELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKDLKKMVKEG
KFREDLYYRLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIPKIDKEVYDILQNYKWKGNIRELK
NTIEHLVVLSKNGTITKDSIPEYILESVKKKEDEEGDYPLDLNKAVEKLEIDTIKKALEMSNGNKAKAAK
LLNIPRSTLYYKLKQYG
>gnl|CDD|469438 NF041553, CBO2463_dom, CBO2463/CBO2479 domain. This domain occurs in proteins encoded typically between known subunits of the selenocysteine-containing D-proline reductase complex, a key contributor to Stickland metabolism. In Stickland metabolism, amino acids proline or glycine, or certain other compounds such as betaine or sarcosine, can be reduced, enabling energy-generating oxidation of various substrates such as other amino acids. Some members of this protein family have two copies of this domain
YEITPVLMGGVIVEVNDTAVKIDLKGRLGVIKVPRRWVITDYPLKVGQEVEFYFSYIEVL
>gnl|CDD|469439 NF041554, SA1362_fam, SA1362 family protein. Members of this family include SA1362 from Staphylococcus aureus. The N-terminal 50 amino acids are highly hydrophobic and suggest two transmembrane alpha-helical regions. The C-terminal region rich in basic residues, variable in length, and often somewhat repetitive. The family is widespread in Gram-positive species
SKIIFYVIIGLAAIGLVSQLFTNPGGLLRSILIIAVIGAIIYFIYYFFFLRRRGGGEQKKYKKAVKQSKK
>gnl|CDD|469440 NF041555, tannase_A, subtype A tannase
KRFLLLLALGAASVGILAACSPSQTTSTASSTSASATAATNVDVSNAKKLTLDMSKWRYDADNDVYYQLG
VSYCTKPQSKDYESLGIYVPGAYFTAKKNGNGTYTCTVNTKAKVGGYTAKTAPIVMPINTPGYSAQAAPT
SYSYSGLAKYTEAGFIYVYAGCRGRDNGDDYAGGAPWGVTDLKAAIRYLRYNAALLPGDTSKIFTFGHSG
GGAQSAILGASGDSKLYTPYLEAIGAAMADTSGKAISDAIYGAMAWCPITSLDTANEAYEWNMGQYASSG
TRASGTWTKALSNDLATAYASYINKLGLKDSDGKTLTLDKSNSGIYTSGSYYDYLKAEIETSLNNFLKDT
TFPYTASSQRQAGMGGGGGGSGTGEMPSGEKPSGKAPSGDTPSGSMPSGGATSTGGSQSSSTTYKTAQDY
IKSLNSDGTWVTYDAKTNTASITSLKAFVKHCKSASKDVGAFDALDRSQTENQLFGTGESSTLHFDSTMA
DLLSKNADTYAKLTGWKSSYAEAYTSDLKKTDTLGNDIETRVNMYNPLYYLSDYYKGYNTSNVAPYWRIR
TGIQQGDTALTTETNLALALKQYAGVKSVDFATVWGQGHTEAERTGNSTSNFISWVN
>gnl|CDD|469441 NF041556, tannase_B, subtype B tannase
LKFDPDKYTTKTVTVDGKTVKYRAYENIVYVAKPVDPAYQSLNIYVPEAYFNGGSINGYTAATAPIFLPN
SVGGYMPGKAGTPSGGNGRSGGRPNAILQALARGYVVASPGARGRTLKDASGKYTGKAPAAIVDLKAAVR
YLRFNDGRMPGDAERIISNGTSAGGALSALLGASGNSPDYEPYLKELGAADASDDIFAVSAYCPITNLEH
ADMAYEWQFNGINDYSRMDMSMLDYRPKRKTVAGTLTAAQQKLSAELKAQFPAYLNSLKLKDANGKPLTL
DADGNGSFKDYIKAYLMASAQTALDSGTDLSQNPWLTIKNGKVTDLDWDAYLKSVGRMKTPPAFDALDLS
SGENNLFGDATTDARHFTAFSQKHSTVGAKMADADTVKLMNPMNYIGKPNATTAKHWRIRHGTKDRDTSL
AIPAILAAKLQNAGKDVDFALPWDQPHSGDYDLDELFAWID
>gnl|CDD|469442 NF041557, AmoA_BACT, bacterial ammonia monooxygenase, subunit AmoA
AEAVRISRTFDLLLLVILFFVFLGSYHIHFMLTAGDWDFWIDWKDRQWWPTVTPIVGITFPAAVQAVLWT
KFRLPFGATFCVLGLLFGEWINRYFNFWGWTYFPINFVFPATLIPGALVLDIVLMLSGSWLVTAIVGGMG
WGLLFYPANWPIIAPYHVPVEYNGSLMSLADLIGYHYVRTGTPEYIRMVERGTLRTFGKDVTPVSAFFSA
FVSILMYFLWWFIGKWFATTKFIK
>gnl|CDD|469443 NF041558, NosP, nitric oxide-sensing protein NosP
AVSRARDPEAAAQELAAQLAHPDLGFVLFFCSAEYDLDALAAALEQAFGGVPVVGCTTAGEITPQGYGRG
SITAIGFDRRHFAIEAALIENLDRFSLADAQALVDSLLERCRSRALAPIKGHSFALTLLDGLSSREELVL
ATLNSALGSIPHFGGSAGDDLHLANTHVYYDGRFHTDAAVVVLVNTPLDFEVFSTHHIVSSDEKLVVTEA
DPESRTVYELNAEPAALEYARLVGLPVEELDPEVFALHPLAVRIGGEYYVRSIQRVNDDLSLTFYCAVDN
GIVLTAMRPGDLLENLEQLLERIEQRLGPPELVIGCDCFLRRLEIEQRGLLDEVSALLRRHRVIGFNTYG
EQFNGMHLNQTFTGVAIG
>gnl|CDD|469444 NF041559, BTH_I2691_fam, T6SS effector BTH_I2691 family protein
TGCNFCEKTGLPILPVRYAVVPDSVAAQLPPGALGKQVKGVALKEAKYTLRTLREGYLYVYYERGRNEWQ
AYAVTPDGYLWKFPPPEPPPAPLEFACKREGHSAPASFITIEDPDKAGKVWLAFSPDPWTKAVLKKYESN
AALRAKRMQKIDVAAWLGGGPQPHGLVTATLAQLAKQVAEYAPGDDLRSEATRYPFASSHGPYARATGGR
ATALAALLGNMFQEEPGKKGAVVALWDPVGIVQELNGLRNDAVAALQQFLEEPERAWKLAAQAIDGIEAA
VRQNAEQDVDREAEAAKAGLQAEKGGTYGGADQGPPVLKAEQLERAERKQAAEREKYREQIAEAEAEAAD
EAWEKRYDKYLEAARAAFRAEYQALLAEFQELLEQLAQDHVAWLKSPLLLAALDDYDDTDLESGLAYAEV
VALCIGGLNGTPPGAALLDKWLKLDLDDPDNLLWRALALNQKELIAELKSALKKEDDPLEPISKLFDEAQ
NALKKLLGAFAKASDALEAADLTAALLELLGGPLGSDRTVVTVGDAVGKWLLLGKVLDGVGEKLSKGALL
LVRGLLLAQAVDLALQSALLERALRWELEEALRALGRLGAPASELIAVALRIDLAKAGGALANTLRALWG
KLLATAEGGSALKELRIGGVVLIFQLLALGFALKSLKADGDKDPEARAKLAAAVLGLTAAVLEIVGKTLE
KLAKEAAAASANLAAAAAAALAAAIGGALGAVAGAIGAVQDIKDAVEALKKGDYLLAALYFAKAAAGIGL
GAAIVGGAALLAGGRVLLGLLGWAVLLGLVAIGILIAAYYKEDALEKWLERCVFGKEEESEKWKSAEEEM
KAFNAALL
>gnl|CDD|469445 NF041560, T6SS_Burk_ExIF, putative type VI secretion system effector, ExIF family. Members of this family are found typically in type VI secretion system (T6SS) regions of Burkholderia, Paraburkholderia, Acinetobacter, and related lineages, and may be effector proteins. The family is provisionally named ExIF after a motif well conserved across most family members
KLRGRISNLKKERSKIDFFFTEADQTNMGATAVGAALAGLGGAAAGLAAMAPATGEEADYVEFELDGKPV
KGWLWTSPFKEGDEVEVVAEPEEDGRYQVYAVLDPKDGILALYPHCSRGRKAHYKSSIKWSLIFGGSLFL
FISFILLLFFFFGSGDNWDGFLLILGGGGLIILVIFGFIAFRIGRKFKPFVRLAEQIFSVLGWKDVKNID
LRKITKKKKKPSDPPALGVMYFR
>gnl|CDD|469446 NF041561, PraA, alkane oxidation protein activator PraA
MKSSKTFVVLVALAALGLGAASMAQAATIEPAGTAFTAPGTISVSKPSSINGPVDCTITFSGKVSADGSY
ATITKVAFTGGLLCSVPEATNLPWKLTATSTTSGAVSGVGFTVHAFGLGGDCGPSTAEGSWSNATNKLTA
SNQSLAGGCTIKSLSVKPPPAFTVVP
>gnl|CDD|469447 NF041562, PraB, alkane oxidation protein activator PraB
MKSLKTLVSLSALALCLGAASMASAATIAPAGTPFSAPGTITVKSPSSFGAPVTCNITFSGTVAADGVAT
ITSATVSGGGLCGLPTLKGLPWTLTATSATTGTVSNVGFTIAGFPASNCGPTTINVSWNNSTNTLTASNQ
QLSGNCTVTSLSVKPSPALTVSP
>gnl|CDD|469448 NF041563, amorph_syn, (-)-alpha-amorphene synthase
MPFPFRSNPHESEAAAGVDAWLRTWGLTDEPGVAAMIARTRPAELASYNSPTVDSGVLQIVANQIAYQFV
FDDRAEEVGRRSPGRLLPMLCESIAILRDGRPPRTPLGAALADLHRQVRERCTPAQAARWAWNSREYVHG
LLYEAVAQAHPLPVRIGLCTSIRSLTAGVEPFYPLCEAAQPCELAPEELHHPAMRRLSRLSADAAVWIPD
LFSAVKEQRAGGMINLALAYQRAHRCSLPVAVTLAIRQINSTIREFERLYAEIKPELSPAGVGYVEGMAG
WIRGCYYWSRTVPRYADTAVAPAL
>gnl|CDD|469449 NF041564, eudesmol_syn, 7-epi-alpha-eudesmol synthase
MPQDVRFDLPFSTPVSDHLEYARERHLRWVREMGLVRSQAGFEEYLSWDLPQAAIRTYPHASADDMVVLM
NWFSLAFLFDDQFDAARPDRADRIAEVARELIVTPLRPAGSPPRVVCPITLAWAEVWEHLSDGMSLTWQT
RFAASWGRFLVAHCEEVDLAARGGTLGVAEYTAFRRRTVGIHHSIDAGERSRRFEVPAQAQAHPVMERLR
DAAADTIGFMNDIHSFEREKRRGDGHNLIAVLRRERGCSWEEATAEAYRMTEERLDEYLRLEARVPQMCD
ELRLSDDERVRVGMGVEAIRHWIGGNYEWALTTGRYAAAKETPAAAAELAGRGSVDDLLSV
>gnl|CDD|469450 NF041565, selin_dien_syn, selina-4(15),7(11)-diene synthase
LTVPPIYSPIPPAIHPRHAAIDARTAAWAETFSIGSPELRGRLVTHDIGTFAARILPEGREEVVSLLADF
VLWLFGVDDGYCEEGELGRRPGDLAGTLHRLLRVAQNPEAPMLLDDPLAEGLRDLRARVSRYGTAGQAAR
WVDALREYFFSVVWEASHRRAGTVPDLNDYTLMRLYDGATSVVLPLLEMGHGYELQPHERDHPAVRAAAE
MASFIITWDNDIFSHHKESRGGGYYLNVIRVLEHERGLTPDEALATAIAQRDRVMCLFLRLRDHLRAQGS
PQLRQYLDSLGHFIRGAQDWGISSVRYTTPDDPADLPSTFRDTPTDDSTEPLDIPAISWWWDLLP
>gnl|CDD|469451 NF041566, branchenz_Thermus, 1,4-alpha-glucan branching protein
MRFVLVLHAHLPYVRAHGMWPFGEETLYEAMAEVYLPLARALERLEADGVPAPLTLGITPILTEQLADAK
VKEGFRAYAQDRLERARGDLERYRGTDLAASARHQLAFWEGTLAQYEALGGDLVGFFARAQERGQIELIT
SSATHGYSPLLGSDEALWAQIKTGLETYRRHYRRDPTGYWLPEMAYRPRGPWTPPVEGAPAGMRAGVDEL
LMKAGLRYTFVDAHLVQGGQPLPPYAGPYGPLPNPVESSEAVYRVHELPSGLRVLARNPETTLQVWSADY
GYPGDGAYREFHRKDPISGLHHWRVTERKVDLGAKAPYDPEAAFARAEQHARHFVALLEELARKHPEGVI
CAAYDAELFGHWWYEGVAWLEAVYRELARSPNVRAVTAREAVRGPALRTALPEGSWGRGGDHEVWLNEAT
LDYWRTVYRAEAQMVEAARRCRRERLASRRALRQMMRELLLLEASDWPFLIETGQAEEYARERYEDHAAR
FFELYEMLRADGIDLERLAALEALDNPFPEADPSLYL
>gnl|CDD|469452 NF041567, mtaseRsmF_Thermus, 16S rRNA (cytosine(1407)-C(5))-methyltransferase RsmF
MAELLGEEFPAFLRALTSGDRSYGLRVNTLKLSPEQFQALSPWPLEPIPWCPEGFYYPPEARPGPHPFFY
AGLYYIQEPSAQAVGVLADPQPGERVLDLAAAPGGKTTHLAARMQGQGLLVANEVDGKRVRGLLENVERW
GARLAVVSAPVERLAEAWGAYFDRVLLDAPCSGEGMFRKDPEAVRHWGPGAPARAARVQRGLLAAAARLV
RPGGVLVYSTCTFAPEENEQVVAHFLRAHPEFELEDARLHPLFAPGVPAWGDGNPELAKTARLWPHRLRG
EGHFLARLRKTEGAEGTPPRERPPPLSREARALWRAFAEEHLKLPLEGPIWERAGHLYLLPEGLPSLAGL
RAPAPGLYLGKVQKGRFLPAKALAHALGPGEVGPRLALAPEDPRALAFALGEPVPAEGEDGWYLVALKTA
VGRFPLGWGKLKGGVLRPGRTGL
>gnl|CDD|469453 NF041568, Jag_EloR, RNA-binding cell elongation regulator Jag/EloR. Members of this family are nucleic acid-binding proteins (RNA or single-stranded DNA) with a KH domain at the N-terminus, an R3H domain at the C-terminus, and additional regions of homology. The founding member of this family was JAG (spoIIIJ Associated Gene) from Bacillus subtilis, but later work in other lineages, such as Streptococcus pneumoniae, as established a role in controlling cell elongation and the operation of the elongasome. The S. pneumoniae protein, a protein that undergoes regulatory phosphorylation and dephosphorylation, is also called RNA-binding cell elongation regulator EloR, and also KhpB
QVTATGKTVEEAVESALAELGVTRDRVEIEVLEEGSKGFLGLFGSKPAVVKVTLKPDPIEEAKEFLENVL
EAMGIDEVEIEEEEDDDVIKFNLSGEKLGLLIGKRGQTLDALQYLTNLVANRYSDEYVRVILDAENYRER
REETLEQLAERLADKVKRTKKPVVLEPMPSYERKIIHTALQNHPDVETYSEGEEPNRKVVIAP
>gnl|CDD|469454 NF041569, A-tRNAntase, A-adding tRNA nucleotidyltransferase
MDVITTHVNADFDCLGAMVAARKLYPEALMVFSGSQEKSMRDFFLKTTGYALDFTRLKDLDFDKITRLIL
VDCQHTSRIGRFAEVARRPGVEVHIYDHHPESSGDITPSGGEIRECGSSTTILTTLLMERGIEVTAVEAT
LMMLGIYEDTGNLTFPSTTGEDYQAASWLLERGANLNTVADFVSQELTAEQVSLLNDLLKSLQTTTVNGV
DISLAHASVDHYVGDIAVLAHMMRDMENLEALFLVVGMGERVYIVARSRIPEVDVGAILRELGGGGHATA
ASATVRDLTVIQVLERLEELLPEKVNPRRTARDLMSSPVKTLPASTTITEARELLTRYNVNAMPVMDGKR
MVGIISRRIVEKALYHGLGSLPVSEYMHTEFLRATPDTPIAAIQEYIVGQHRRLVPVFDGEELVGVITRT
DLLRYMYAGMQHNTEAVYDLGRENLPVRRREVVHLMNRQLPRDVVKMLRDLGKVGDELELPVYAVGGFVR
DLLLGIENDDIDVTVEGDGILFAETFAAKFGCRVKSHAKFGTAVIVFPDGTKIDVASTRLEYYETPGALP
TVERSSLKMDLYRRDFTINTLAIRLNSPDFGVLIDYFGAYRDLQEKVIRVLHNLSFVEDPTRVFRAIRFE
QRLGFHIARHTENLIKNAVKMGFLDKLGGRRLLNELVHILREREPVRAILRMASLGLLRFIHPDLFLTKP
VLRVLDEVKKVVTWFELLYLDRRVETWVVYFLALTSTLPDDEFLATCTRLSVSEHYREKLIDMRVHGEQM
LEIMQRKVARGIPVLRSDIYFWLRGLSPEVLLYIMAKTRSDEVRKFVSLYVTQLRGVRTMLTGKDLKRLG
VPAGPRYREILDVVLTARLNGEVLTREDEERLVRKRVGSV
>gnl|CDD|469455 NF041570, acyltasePE, acyltransferase PE
MKKLLAGATALLTVGATGCFGLGIATADETPPGPSGGTPAPGPPPIGTPGRAYALGGAHVLGIPYDEYIR
RTGADWFPGLKRQIVDYPAGQVQGHVLERLFPGIGRLDEIMPGLGLDGPSIGESVDVGEDNLDAAIREGG
PGTAIGLSEGALVLNAVQARLANDPAAPPPDQLSFATYGDPLARHAFGESFLTQNFPVGSVVPALDYRMP
PPVESQYDTYQFVSAYDSIADWPDRPDNLMSLANAVVGLATGHTAVAFTNPSMVPPQNIRTTVNSRGAKT
TTYLIPEQHLPLVLPFKYLGVDEDTLNKLDAVLKPMVDAGYSRNDDPLTAPITVDPVNGYDPAAVTAPAT
QAAF
>gnl|CDD|469456 NF041571, alkn_up_AupA, alkane uptake protein AupA
VLTPRFALRALCLAVAAASAGLSVPTSASMGNIGTTYGVMPIDVATAQSLSMFNSQVSATYYNPAYLTKD
ERGELTAGILHAEQELRASRPNADGDVVSDSPSQHVLIGMKTNLGSLTRFGHPIYLGFIAGVEKYGKEML
AFSSETSETGQFLQYGREPLFLNIGGATKIWRGISAGASVRITLEATANLDAVSTLGGETSRERLSVNAE
PSLKSILGTTIDWGDTFCPDSSCFLSGWETALAYRTKSSASTTVDSNVIVTQTIPDPGLSLAVSTIDSFQ
PEIIAFGTQYKGDGWRIGGSIEQQNWSELEDEFASDTIKDQGSVSSSNRIGFDDTLVPRIGGEYQLNKNF
AFRGGVAYEESPLKTTRNPELNYLDTDKIVVGLGLSATYERTRLLAYPVRFDLGYQYQQLQERDFTIVDF
DGNEQPVTADGDIHVVSGSITLKF
>gnl|CDD|469457 NF041572, rhamnosid_Flavobac, alpha-L-rhamnosidase
LFSLLLLLLLCFSCNEKSTSNSSLAFEKLTCNSKENPTAIESEQPLFSWVVNAEGFNKSQSAYHILVASS
EEKLNENDADLWNSGKVKSSKSTFVKYKGKKLQALQTYYWKVKIWDESGQASNWSEVQSFQMGLMDEANW
GDSKWITLNKDTRTSEHRFRDYKTGKMKKPIPVDGFAASYFRNEINIEKEIENAQAYICGLGYYELYLNG
EKVGDHVLDPAPSNYDKQAYYVNYDITEQLKSGKNAFGIILGNGFYGQNISWKRDPESERDLSYGPPTVR
LLVKLTYEDGSEADFYTDETWKESTGPIVFNNIYGGDTYDARYELGGWNTVGYNDSSWGNAKEVSPKVKK
ISAQQIPPIKKLKEFEPQNVFKGADGEWIVDFGQNIAGWVKLNVKEKEGQLIEIITTEALLTNGKDIFQG
STGGGANGMAQIYKYICKGDGLESWEPKFSYHGFRYAKIKGVSTKPDANMIKAVLVATDIQETGSFSSSD
ELLNKMHSISKWTIVDNVHGIPEDCPHREKCGWLGDAHAFCEYALYNYDMYDFYKKYMEDIRTQMRPTKG
HNNPEIKFQVPTMIAPGKRTSTYAKIDWGVATMYLPWYNYLYYGDDAIVKEYYEEMKGLTNFYLNFKGEN
GIMQDGMGDWCPPRWDRRKNPSAMECDPIISANAYFYDVLGIMETFAKMNNDAAYEAKMKKEKEALKTAF
NKEFLVEIPNTKHKWYQSQTATVQALQFGMVPETEIENVVNGLVYDIVEVKGGHHSTGIHGNRYIYTVLS
KYGKADLAYQILTTPDFPSQTYVMNSGFTTWPERQFEWEKMEGPTNSLNHPMHSGFAAYFYESLGGIKSS
KEKPGYKEFTVNPEFPSTITSTEVSVPTPYGDIKNSWSLKEGVLSMNLEVPFNTKAKLVLTENELESLKI
NGESFEDFQKENKVEIVENSNVILGSGKYKIEYKKS
>gnl|CDD|469458 NF041573, rhamnosid_Stmyc, alpha-L-rhamnosidase
KALRVTAPTVEYVRRPLGLDTPRPRLSWPLASAAPGARQSAYQIRVATSPGRLGRPDVWDSGKVASADSV
LVPYGGPELKPRTRYHWSVRVWDADGRASEWSEPSWWETGLMGAGDWSARWIAAPAALTGAPSLEGASWI
WFPEGDPASSAPAATRWFRGRVDVPEGVTRARLVITADDGYTVYVNGTEVAHTDADTDAENWRRPAVVDV
TDQLRPGANVLAVAATNATEGPAGLLGALELTTADGVRTVVTDAGWKATDKEPSGGWRSPDFDDSAWPAA
KVLAAWGAGPWGRVAPASSPAAQLRHEFRLRRKKVARARLYATALGLYEAHLNGRRVGEDRLAPGWTDYR
KRVQYQTYDVTELLRPGANALGVTLAPGWYAGNVGMFGPHQYGERPALLAQLEVTYADGSTERVVSGTDW
RAAAGPVTTADLLSGETYDARKETPGWTSPGFDDSGWLPAEADDDVPAAVVAQVDGPTRVERELTARKVT
EPKPGVFVFDLGQNMVGSVRLTVSGKAGTTVRLRHAEVLNPDGTLYTANLRTARATDTYTLKGGGKETYE
PRFTFHGFRYVEVTGFPGTPSADAVTGRVMHTSAPFTMDFETNVPMLNQLHSNITWGQRGNFLSVPTDTP
ARDERLGWTGDINVFAPTAAYTMESARFLTKWLVDLRDAQTSDGAFTDVAPDVGNVGNGAAGWGDAGVTV
PWALYQAYGDTRVLEDAWTSMVKWLGYLERHSDGLLRPADGYGDWLNVQDETPKDVIATAYFAHSADLVA
RTAEVLGKDPAPYRDLFGRVRDAFRAAYVSAGGRVKGDTQTAYVLALSMDLLPDADRGPAADRLVALIEA
KDWHLSTGFLGTPRLLPVLTDTGHTDVAYRLLTQRTFPSWGYQIDRGATTMWERWDSIRPDGSFQDAGMN
SFNHYAYGSVGEWMYANIAGIAPARPGFREILVRPRPGGGVTEARGTFDSVYGPVSTRWKTRSGGFRLTC
SLPANTTAEVWIPADAADQVTHGGATFLRMEDGCAVFAVGSGTHRFTT
>gnl|CDD|469459 NF041574, antitoxPezT_Strep, type II toxin-antitoxin system toxin PezT
MKLEDYSETEFQLALKRNIRSLTRGKTTSKQPKAILLGGQSGAGKTTIHRIKQKEFQGNIIIIDGDSYRS
LHPNYLALQEEYGKDSVEYTKDFAGKMVEHLVDELSKQGYHLLIEGTLRTVEVPRKTAQLLKSKGYQVSL
ALIATKPELSYLSTLIRYEELYAIDPNQARATPKEHHDGIVEHLVDNLRELEDEKIFDRIQIYQRDRSCV
YDSKKDKGSAADVLQECLFGKWSTVEKEMLKVGKERLNELR
>gnl|CDD|469460 NF041575, antitoxPezA_Strep, type II toxin-antitoxin system antitoxin PezA
MIGENIKSLRKTHDLTQLEFAQIIGISRNSLSRYENGTSSVSTELIDRICQKFNVSYVDIVGEEKLLTPI
EDYQLTLKIEVAKERGANLLSRLYRYQDSQGIAFDDESNPWILMSDDLADLIHTKIYLVDTFDEFERYNG
YLDGIERMLSMAKHQVVA
>gnl|CDD|469461 NF041576, bacphytchrmBphP, bacteriophytochrome BphP
MSAAPDPLDMDACAREPIHIPGSIQPYGVLLVIDPADGRVVQASATAADLLGVPDAQLLGQRWDALLTLD
EAQLPAAAPVEEPLHLAHAPVRFPQRATPPASRWVAAWHLYPEQWLVELEPRDAQASDVTLRDALPLLRL
VERDPSIAEAALRVAKEIRALIGYDRVMVYRFDEEWNGDVIAEARRPELESYLGLHYPASDIPAQARALY
LRNRVRQIADVGYRPSPIEPTLDPRDGQPVDLSDVSLRSVSPVHLEYLANMGVTATLVTSIVVNDALWGL
ISCHHYRPLFANHAMRDVTDAVSRALAGRIGALQAVARARVESVLLTVREKLITAFNEAETLTPEMLTDM
APDLMDVVDADGVAIFHGDQVSRHGTTPDVADLRRIRAQIESSHHEALREDAVGALHVDAIGRTFPELAD
LAPLAAGLIFVPLMPQARSALLWTRREQVRTVNWAGNPQLAKLEDIPNSRLSPRKSFDLWQQTVRGRARP
WSPLHLESARSLRVLIELMERKRFQQDFTLLEASLARLRQGVAIIERGGDTGISRLVFVNDAFARLAGTD
ASELIGRDLRTLYASDAAPAQLQGLETKLRQGEAAYVTLPLRVENAAPVPWQFDFEPLPSAS
>gnl|CDD|469462 NF041577, nside_bi_sphtase, 3',5'-nucleoside bisphosphate phosphatase
MLNVDLHCHSTVSDGLLSPAEVVRRAAARGVELLALTDHDDVGGLAEARAAAAELGLRFVNGVEISVTWG
GHTVHIVGLGIDPAHPALVAGLASIRAGRIERARRMAASLAKVGIEGAFEGAMRYADNPEMISRTHFARF
LVETGVAKDVRSVFKKYLVKGKPGYVEHEWASLADAVGWIRAAGGVAVIAHPGRYDLGRTTLERLLTEFK
ALGGEAIEVVSGSHSADDVGRFARLAREFGLLASRGSDFHGPGESYRDLGRLPPLPPGCTPVWERW
>gnl|CDD|469463 NF041578, betaarabinsidaseHypBA2, beta-L-arabinobiosidase HypBA2
THSSTRKRWLASIGAVAAVATLATGGATTAYAADALANPNADVAYPSFKGSDDPMKTAANGVAYNPTTSY
LAETFDKDVANGAGTDTDHDFWIDKILTRTGAQPNGKGTNDAGDYSYEGADGNNYLFTRGRAAYMYTHTP
ERLGFVGDTAYWDQTGNDGFTVTVSADGSKQTLNEDTSQRKQTPSYFTTVFQNGDKTLTVTEVKYITYNN
VMVANLTVESTTGGDVTLTAASPFATTGADGDTELTGRFNVKNNLTTIYPRFSGNGFTVKGGKLTSTLSL
EANEPQTTKLQLGLIANELPDSTTEYEARFNGDLKDPAASYKDSVTTYNQWWVDNAPYVDTPEDNIDKTV
VYRWWLSRFNMLDANMPGNTFQYPTSIEGVLGYNNQIVLTSGMFIMDTKWFRNPEYSYGTWLSAGDTAKK
GKSGYYYYHDNPGDPANWNHSYTQYITRAGWDSYKVHGGPSTVAEKLADQGAEDVQGLLNSQSEPDNNDN
QNNNKNSLIDWSWWSMTGNDADAVSFSEPGRSGQRMDRADGSANMWANANAAAQAYKAAGDTANAEKMQK
IADAIKQDVLDNLWDSDDKLLKHKWLNDGAFAKYKELNNYYPYSEGLMPTGNDDYNSALRLFEDADEFPI
FPFFTANQADKAALNFPGSNNFSIINAQPLLQIYSAGIRNYDAAKNGYITNEQFKKLLYWVAFAHYQGGD
NQYPDQNEFWNEDNNNAGDTIGDKNLDAAQNGGKITYRSWIHHTQLGTTNWTMVEDVAGMVPREDNKIEL
NPIEIPGWNYFTVNNLSYHGQDVSIVWDKDGSHYGGPAGYSLYVGGKLAFTSDKLAHLIYDPAAGTVEVA
DKSGATITGATGSTLPAANQVTFTADQRVTDLFAKSGTNVDSASKSTTNVAKGADVEATYEAKGYPATNA
VDGKNVMESFWGTKGSKNKTDSLTVTFKNGVQNIDDIRLYFYQTSSSQTISGYAEPANYKLEYQKEDGTW
HPLPNQVRTPNYAGANYNRVQFTPVVAKAIRATFTPQAGQAVGVKEIEAYNTGIKPTGTSENQAPQVDAY
VASSTSSGAQLVGTVKDDGLPADGDITTTWEQVSGPEGGTAKFVDATAASTTVTFNREGDYVLKLTASDG
EKTGFKEVTVHGIPSDGTVNVAPQSTASASYTNGYQPKDNAKKVIDGQVVYTNTPNETWNNWGDNTGVEP
WLQLAWAGKVPLKKAKLFFWTDGGGVPMVKSWKLQYADADGNWQDVKLADGQSYTTNQNEGNEVKFAETV
ETDKLRVVFPKGAIVGASEFEAYAIDPVSVDGVNRMVQTGSKAADLNLPKTVSASYTDGSRRDLAVTWGK
VTDDQLAADAEFDVKGTVAGALAGTVAHIGVRSDAQSQTAGNAQPVEQTVYQNAKSVDLPATVPVRFPNG
MLDDRKVTWKDADVAAIDLTKVGDYEVSGTAEDSSSAAKLTVHVVADPNGGSTPEPEPEPLTGWIEGKAT
DTTVSAEASWSPAEGKLNDGVVVDDTWPTTDDQDVNAKVWGSWGKAVDGMYAQYDFGKEVTVDSSRVQFW
ANFAETDDAKGGLEVPDAWKIQYLAEDGSWKDVENAQYTTVRNSPASRASTDADGWSVATFKPVTTTSLR
LVLTPHTGEGTFGAAVAEWGVHAADSTEPEPTPVDKSALESALNAANSLDQSKFTADSWAEFQQAIANAQ
KVYDDANATQEQVDAAVTALEDAQKTLV
>gnl|CDD|469464 NF041579, betaxyl_Flavo, beta-xylosidase
MRKIYLLGILLLVLFACGCSINNVKKSKEDSEIDKKVSTLISQMTLEEKIAELTQDAPANERLGIPMMKY
SECLHGLWLPGATVYPQAIALGSTWDPELVKKMTTQIAKEARAANLTHCYSPNLDVISGDGRYGRVEESY
GEDPYLVSRMGVAFIEGLQGTGDEQFDENHILATAKHFVGYPENRRGINGGFSDMSERRLREIYLPPFEA
AVKEAGVGSIMPGHQDFNGVPCHMNTWLLKDILRDELGFDGFIVSDNNDVSRLNTMHFIAENRTEAAVLG
LKAGVDMDLVIGKNPELAAYIMNVLKDTLTKNPELVKYIDKSVSRILKAKYKLGLFDQKDKDYVKPVVST
PESQEFALEIAKKAIILLKNENNLLPLDKSKIKSIAVIGPNAHEERPEGGTYTLLGGYSGIPPYYTSVLE
GIKQKVGNKVKINYAEGCDLLSNSKAGFAKAIAAAKKSDVVVLAVGGSTRTCGEGADRDDLDLFGVQNEL
VEAIHKTGKPVVVVLINGRPLSINYIAENIPSILETWYLGMRSGDAIADVLFGDVNPGGKLTVSFPRSVG
QIPVTYLERPDFVGSGKGLYKFSDKTPLFPFGFGLSYTTFKYSTPKLANATIAVDGTTTVSVDVTNTGEV
IGDEVVQMYVRDDFASVGRYNKMLKGFERITLKPGETKTVSFKLGFDNLSLYNQDMKKVVEPGTFTISVG
ASSLEKDLKTIKLRVK
>gnl|CDD|469465 NF041580, DidA, DNA damage-induced SOS-independent cell division inhibitor A
MTDIAMPSLFQAPRRPASVRFVRPGRPGGVLGAVNYAGVLLVWAALFVVDPPLALKVMAERRADSPIRRR
WRW
>gnl|CDD|469466 NF041581, SosA, DNA damage-induced cell division inhibitor SosA
MIKKYKSQILTYIIVFLVSMILFSIFFLSANQNAHTEQTYEMTDHQIKQKAINKTEQHEQKKENSEQQSN
PVFALVH
>gnl|CDD|469467 NF041582, malolactic, malolactic enzyme. Malolactic enzyme converts L-malate anaerobically to L-lactate and carbon dioxide
EILNDPFLNKGTAFTKEERKKLGLTGLLPPRVQTIEEQADQAYAQYQSKSSDLEKRHFLMEIFNTNRTLF
YYLFSQHVVEFMPIVYDPVIADSIEQYSELFVNPQNAAFLSIDHPENIEESLKNAADGRDIRLIVVTDAE
GILGIGDWGVNGVDISVGKLMVYTAAAGIDPSQVLPVVLDAGTNNQELLDDPLYLGNRHERVRGEKYYDF
VDKFVETAEKLFPNLYLHFEDFGRSNAAKILNKYKDKIPTFNDDIQGTGIIVLAGILGALNISKEKLTDQ
TYLCFGAGTAGAGIAKRIYDEMVQQGLSEEEARKHFYLVDKQGLLFDDTPDLTPEQKPFARKRSEFANAD
ELTNLEAVVKAVHPTILVGTSTQPGAFTEEIVKEMAAHTERPIIFPLSNPTKLAEATAEDLIKWTDGRAL
VATGIPADPVEYNGVTYEIGQANNALIYPGLGLGVIASTAKLLNDEMISAAAHSLGGIVDTTKPGAAVLP
PVSKLTEFSQTVAEAVAQSAIDQGLNREPITDAKKAVEDIKWEPEY
>gnl|CDD|469468 NF041583, SOS_SulA_aeru, SOS-induced cell division inhibitor SulA, Pseudomonas type. SulA, as found in Pseudomonas aeruginosa, is a cell division inhibitor induced by the SOS response. It interacts with FtsZ to halt cell division. SulA proteins, like FtsZ, differ greatly by lineage; SulA of Escherichia coli is architecturally somewhat different and is described by a different model, TIGR00623
MQFPQSLDRPQLPLFEAFLAQPLAPLLTEAPEPPPAAEPEVFSELSLRGAAGHCLHLLAPILRELSEEQD
ARWLTLIAPPASLTQAWLREAGLNRERILLLQPRGSQSALQLACEALRLGRSHTVVSWLHPLDRAARQQL
ARAARLGNAQSLNIRLG
>gnl|CDD|469469 NF041584, MqnP_SCO4491, menaquinone biosynthesis prenyltransferase MqnP, SCO4491 family. This model is one of three built to describe UbiA-like prenyltransferases thought to be menaquinone biosynthesis prenyltransferase MqnP. This family contains the founding protein SCO4491
GRVRAFLRLVMIEHSVFALPFAYIAALTAMFLADRSVHWGDLLLVTVAMVGLRTFAMAANRIIDREIDAR
NPRTAGRELVTGAVSVRTAWTGALVALVVFLGAAALLNPLCLALAPVAVVPMVVYPYGKRFTNFPHAILG
LAQAIGPIGAWLAVTGTWSWDAVLLGLAVGVWIGGFDLIYACQDVEADRAIGVRSVPARFGVPAALHGAR
VTHVVTTALLVWFGLATGAGAFWWVGLAIVAGAFVYEHSIVRPHDLSRLNRAFFTVNGFIGIALFVFALL
DLIVR
>gnl|CDD|469470 NF041585, MqnP_Cj_Hp, menaquinone biosynthesis prenyltransferase MqnP, HP1360 family
LKDFSELVMFEHSIFSLPFIFIAMIVASKQVNDSGWFGWKLLILGILAAVSARNFAMAFNRYADRDIDAK
NPRTKNRPSVDGRISKGSLLLFIVLNALIFIAVAYFINDLAFYLSFPILFILGGYSYFKRFSSLAHLVLG
VSLGLAPIAGVVAVSGEIPLWSVLLALGVMFWVAGFDLLYSLQDIEFDKKEGLHSIPSRFGEKATLFISR
LFHALAVLFWLLFVWEAGLGFFAYLGVIVSAVMLGYEHYLVRKDFKNIDKAFFTVNGYLGIVFFIFIILD
L
>gnl|CDD|469471 NF041586, MqnP_DT, menaquinone biosynthesis prenyltransferase MqnP, Deinococcus/Thermus-type
RTYLELVRFEHTLFALPFAYGGMLLAALGWPGWETFLWVTVAMVGARTAAMALNRLIDWRIDALNPRTAG
RHLPRGLVKPGEVLALAVVGLLLLAFAALNLNPLTARLLPVAVFFLVGYSYTKRFTWLCHYWLGLTIGAA
AAGGWIAVTGAFEPAAFALWAGVALWIAGFDILYATQDYDFDRANGVHSIPARFGIPAALRIARASHALT
WLLFLLTGLLYGAGWWYFLGVLLVGAILLYEHRLVRPDDLSRVNVAFFQANVVVSLGMLAFILLDTL
>gnl|CDD|469472 NF041587, YmgF, cell division-associated protein YmgF
MNKSNNLDYFTLYIIFSIAFMLLTFLVILFAKPSTWLGEVLVTINLINALVWLVINLINRLRGKLVSHRD
QH
>gnl|CDD|469473 NF041588, AQJ64_40280_fam, AQJ64_40280 family protein. Members of this family occur almost exclusively in the genus Streptomyces. The function is unknown. Some members, such as AQJ64_40280 (KUN75916.1) for which we name the family, previously were annotated as amine oxidase, but the source of that annotation could not be traced during model construction
MDATVEWVDARERLPRDGAPVAAAITGRYPADPADPDPASGEEFWLVLPMYFTRRHFVEDGTEHRDCFVD
SDGVVRLPYGGGSDEPVTHWAELPTLPGTTTHLVLGEEVRPALRAA
>gnl|CDD|469474 NF041589, PepG1, type I toxin-antitoxin system toxin PepG1
MSVLPKSLERRRLLIAYETIQTILGFGIFTIALIGLVVKLLKNSKK
>gnl|CDD|469475 NF041591, CxxC_VVA0879, VVA0879 family protein. Members of this rare but broadly distributed family average about 120 amino acids in length, including an apparent redox-active disulfide motif CxxC and two other invariant Cys residues. The family is named for VVA0879 from Vibrio vulnificus but occurs also in Gram-positive species such as Clostridium botulinum
TLEEWRAEGKARFGDDRKKWAFVCPSCGTVQSAQDFIDAGADEDDPPNYAGFSCIGRFTGAGSPRKKGRG
CNWTAGGLFGIGKLEVIDPDGKEHPVFEFA
>gnl|CDD|469476 NF041592, carboxyl_red, carboxylic acid reductase
ARRIAELYATDPQFAAARPDPAVTAAIDQPGLRLPQIVRTVLEGYADRPALGQRAVEFVTDPATGRTSAR
LLPRFETITYRELWDRVGAVAAALAGDPVRPGDRVAVLGFTSVDYTTIDLALIRLGAVAVPLQTSAPVAQ
LRPIVAETEPRVLAASVDLLDDAVELVLTGPAPRRLVVFDYHPEVDDHREALEAARARLADAGPVVVETL
AEVLERGRALPAAPPPASDDDDPLALLIYTSGSTGAPKGAMYTERLVANMWRGSARAGWGPRAVPSITLN
FMPMSHVMGRGTLYGTLARGGTAYFAARSDLSTLLEDLALVRPTELNFVPRVWDMLFQEYQSELDRRAAD
GADRAAAEAAVKAELREDLLGGRFVSAMTGSAPISAEMKAFVESLLDLHLHDGYGSTEAGGVFIDGRVRR
PPVLDYKLVDVPELGYFGTDRPHPRGELLVKTTTMFPGYYKRPEVTAEVFDEDGFYRTGDIVAELGPDQL
VYVDRRNNVLKLSQGEFVTVSKLEAVFGDSPLVRQIYVYGNSARAYLLAVVVPTEEALARHGDAAELKAL
IAESLQRVAREAGLQSYEIPRDFLIETTPFTLENGLLTGIRKLARPKLKERYGERLEQLYTELAAGQADE
LRALRRSGADRPVLETVGRAAAALLGAAAADLRPDAHFTDLGGDSLSALTFSNLLHEIFGVEVPVGVIVS
PATDLRALADYIEAERASGAKRPTFASVHGRDATEVRAADLTLDKFIDAATLAAAPSLPGPSGEVRTVLL
TGATGFLGRYLALEWLERLALVGGTLICLVRAKDDAAARARLDATFDSGDPELLAHYRELAADHLEVLAG
DKGEPDLGLDRATWQRLADTVDLIVDPAALVNHVLPYSQLFGPNVVGTAELIRLALTTRLKPFTYLSTIG
VGAQIEPGAFTEDADIREISPVRAIDDSYANGYGNSKWAGEVLLREAHDLCGLPVAVFRCDMILADTRYA
GQLNLPDMFTRLMLSLVATGIAPGSFYELDADGNRQRAHYDGLPVDFIAEAIATLGARVTDGFETYHVMN
PHDDGIGLDEFVDWLIEAGHPIQRIDDYADWLQRFETALRALPERQRQASLLPLLHNYRRPAPPIRGSIA
PTDRFRAAVQEAKIGPDKDIPHLTPALIVKYVTDLRLLGLL
>gnl|CDD|469477 NF041593, histid_kinase_PdhS, cell-division control histidine kinase PdhS
MSGSYPFIDIAALDHIREGFAKGDAQLVLTRDLSTVLWVNGPGAKLFGFDRIEDMIGGELDLPVATRRQI
AASSDENDGAPRIVAVRLGGGLRSELTRLHVSHITLPDGVEALLLAASKQDSKPEAIISGLGDDTTHVAL
IDAKAKVIAASPRFAALDISASTLEDLIVEAADASDRIVKRRIRAGKHSVPGAIARLTDNPALHLLCIIG
EAPAPAQTAAAPQLPSNAEEILEEMLPEQAEAPPKPKGFVFDRDGPPARFIWKTDADGSFTEVSPELGII
IGPNAADVIGRRFAEVANVFGFDTDGSIAALLEKRDTWSGKRLLWPVEGTNLRVPVELAALPVYSRDREF
IGFRGFGLVRPQEAEEDPEEIGLVLAGGIPQKREPEPEPQETASADDDDDVLALSEEVANDDHPEATLPK
PPLNLTPNPGRRDSDKVIELLNAAAREKVAADQAKLLKEKEHAERPEGGLTATERNAFREIADRLRKQGL
ANSRQEGDAVQPKPAAERVSPVTPVSEPPKAAQDETAAKDAGSAEKIHADETALLANLPVPVIIHSGDEI
HYVNQALLDLTGYEALDDIREAGGVDALFNSESDDGEKRQGMVLRHADGSEEPVDAHLNAINWRNGRALM
LSLMPVAPAVEVPAAPETASETNDEKQALQAHVEELKTILDTATDGVVLIDPEGRIRSMNHSASALFGYD
RDETEGKFFSMLFAIESQRAAMDYLHGLSGNGVLSVLNDGREVIGREAKGGFIPLFMTIGKLPHTRGFCA
VLRDITQWKRTEEELTNARKEAERASSQKTEFLARISHEIRTPLNAIIGFSELMADEKFGPIGNDRYRDY
LRDINRSGNHVLALVNDLLDISKIEAGALDMQFEAVSLNDAIGEAIALMQPQANRERVIIRSSFQSNLPD
IVADARSIKQVALNLLSNAVRFTATGGQVIVSTNYELNGDVVMRVRDTGIGMTKAEVEQALKPFRQVNAL
QRRQAESAKDWRNEGTGLGLPLTKAMVEANRAQFAIDSTPGQGTVVEIVFPPTRVLAD
>gnl|CDD|469478 NF041594, dam_ctlPhtase_Archglob, damage-control phosphatase
MKISPKCPACLLNRVYLEARMVTDDEEKISRAVEEALKILAEEYSKRGINAHIATRIHRKVYEVLGVEDP
YKEVKDRANEVAMRNLPLAKRFVERSDDRFRTAVIASIIGNTFDYGVMGHEVNESNFRDYFIRKFREGLA
IDDTEEIRELCSGKVVYLTDNAGEIVFDTLLMKEIKKICERLTVVVRGRPIISDATIEDAKLAGVDKIAD
EILTNGKGAIGIIEEELPEETLERLESADIIIAKGMANYECLSESSFKPIAFLLTAKCEPVARDIGVEVG
DMVAMLR
>gnl|CDD|469479 NF041595, dap_A_syn_DdaF, dapdiamide A synthase
MSILNNKEVIVIIDAWSGGKYLIPAFQALGYFCLHIQSLFLPEIFIADNQLAISRSDKHIVHDGNIETLL
NNLKPYAIKAILAGSESAVALADQLNDVLALPFSNQFELSAARRNKFLMQEQLARCGVASIEQQLISHKD
ELRHWLAKHNRWPVVLKPVQSAGTDGVFICHNIKQAEQAFDAILSKKDLFGNPNQEVLCQEFLEGEEFVV
NGIACQGKYFFTELWQSKKQQRKDFPVYETQYLYYQNDAKFDVLTAYTTQVCQALGIENGAFHAEVMMTS
RGPVLIEIGARVAGGADPYIIEECLGHSQIGKLVQAVLHPKKFLQEMRRRRDFSGHRRAAYVYMISPTKG
QVQRSPEEFFIKIEGVISVNYHYKPGDIQQETCDLLSSPGVVIVIRDNPYLLNQTIAEIRSLESDFYHKG
LIAY
>gnl|CDD|469480 NF041596, fum_diaprop_lig_DdaG, fumarate--(S)-2,3-diaminopropanoate ligase
MNLELLINQYSIDFPWYLQLLRNKKIDYSRLESLPLITEELLTQHYYHAEINFSGSYHSYLTSGTTSGKR
KRILYSDKDQHIYLQQRLAIIGHFCGGMNTRACADLGTGHAAATAGEIFQMMGCNVELIDFTQPIDQHIE
VLNRFKPDIFFTMPMILDSLIATGKLDFQPKKIILLGDVASQVWQRKVADYFNIDQTQILDLFGSIEIGS
IAFFNHLYGHYQFDSYILPEVVPVQSIYPDSNYQGRGGILLLTSFAREYFPAVRFVTNDLIEGFAQKKLK
GRTIYTYQRCLGRFANEFKHGEKINLSDISDAMANNLPYHKFDLDDQSGGLVIRIAAKIIPMSIIKAIKH
DLLARNPDVAQMISSGLVQDILIQCVDEKEINGNVSKRRY
>gnl|CDD|469481 NF041597, T3SS_coreg_PtrC, type III secretion system co-regulatory protein PtrC. PtrC (Pseudomonas type III repressor gene C), represented by locus PA2486 in Pseudomonas aeruginosa PAO1, is a small protein, typically around 64 amino acids, rich in charged residues. Overexpression represses T3SS expression, although the mechanism is not described and may depend on protein-protein interaction rather than direct interaction with DNA
SQNAYGVTYATLDDSGLHFESELAIHLEDGSLATLRMPTPPSERQAIRELIC
>gnl|CDD|469482 NF041598, small_PA2485, PA2485 family small membrane protein. Members of this family are small, uncharacterized, N-terminally hydrophobic proteins, 37 to 39 amino acids in length, regularly found encoded next the small regulatory protein PtrC (NF041597) in species of Pseudomonas. The family is named for Pseudomonas aeruginosa PAO1 protein PA2485, which originally was predicted to be longer
MSIYAALASFAAASAFQTVAPARPEQAAAAARDVRKS
>gnl|CDD|469483 NF041599, reg_PtrA_PA2808, co-regulatory protein PtrA N-terminal domain. This HMM describes a shared N-terminal region of several families of proteins, some of which contain a C-terminal DUF2790 (PF10976) domain. The founding member of this family, PA2808 of Pseudomonas aeruginosa PAO1, was found to suppress expression of the type III secretion system (T3SS) via a protein-protein interaction with the T3SS transcriptional activator ExsA. It was named PtrA (Pseudomonas type III repressor A). Homologs are found broadly throughout the Pseudomonas genus
MKSLKALLLVAALALSSLAMAEGGGDRTFARMEQAREKAMAAYQAA
>gnl|CDD|469484 NF041600, cyt_ox_CcoM, cytochrome c oxidase subunit CcoM
MYMDEVVIAGLATVGLMVAFFGGFGYFIWKDSKK
>gnl|CDD|469485 NF041601, PA5502_lipo, PA5502 family lipoprotein
MKPFASRYLLLAAFSLLLGACQSTPPAQPAPVDARADAFAQLQQNLASGELATAEDQLAALQAQAPGDPR
LEQYQRQLAEAYLQRSQIVLQKGDVNAAATALSRARALMPKAPALTGGVNGAIAQARKAELAKAEAALKA
AEAKPKAKVIDPTAESTTVALPILDSGNLRRQLDAIAADVVNYQCDVVIQVPRTKDYPWLATLLSKRVKK
LDPDFDLQLSHQIQRDQPAQVVLSPRK
>gnl|CDD|469486 NF041602, VF_A0006_fam, VF_A0006 family four-cysteine protein. Members of this family, including VF_A0006 of Vibrio fischeri, PSPA7_2531 of Pseudomonas aeruginosa, and BPSL3341 from Burkholderia pseudomallei, have an N-terminal signal peptide and four invariant Cys residues suggesting the formation of two disulfide bonds. The function is unknown
AALLLAPLSAAAAKDDKAAYDQCILQSLRNTENSAAAQLITNACDKLYRDGSMLLPRDKAYYQCLLQNLP
GVKNDEAAQQIKSACRRQH
>gnl|CDD|469487 NF041603, Cys_rich_47, PSPA7_2676 family Cys-rich small protein. Members of this family are small proteins, averaging 47 amino acids in length with four invariant Cys residues (two in a CxxC motif) and typically six overall. The richness in Cys residues, as in the motif CxCCxxC motif found in many members, suggests metal-binding activity
MTLVCLLRGCQWRSGLSTRVGVEGLLCQCCERCGALRYL
>gnl|CDD|469488 NF041604, CSP_NTE_dom, cold shock protein N-terminal extension domain. Members of this family have a C-terminal cold shock domain, but also a longer, hydrophobic N-terminal domain. Members are found primarily in the genus Pseudomonas, including in P. aeruginosa
MLKIVHLLTGAAALLLSFIPSLRSEALPYLQQPDALYLALFGLLNLLLAPVIPLWARGPRHQLQNLASAL
LVLAVALQALTLLAPLPEIAGQPAVLLSLLAALLAVLLHLAL
>gnl|CDD|469489 NF041605, gln_syn_GlnII, glutamine synthetase GlnII
MSYKAEYIWIDGTEPTAKLRSKTKILADGAELPIWGFDGSSTNQAEGHSSDCVLKPVFVCPDPIRGGDNV
LVLCEVLNTDGTPHPSNTRAALAPVAEKFAAQEPWFGIEQEYTFFKGGRPLGFPEGGFPAPQGGYYCGVG
ADEIFGREIVEKHLDNCLAAGLAISGINAEVMPGQWEFQVGPAGPLEVSDHLWVARWLLYRTAEEFGVSA
TLDPKPVKGDWNGAGAHTNFSTKAMREGYDPIITACEALGKEKALEHVKNYGAGIEDRLTGAHETAPWNE
YSYGVSDRGASVRIPWQVEVDKKGYIEDRRPNANVDPYVVTRLIVDTCCSALE
>gnl|CDD|469490 NF041606, dguan_cyc_DgcA, diguanylate cyclase DgcA
SDKIVSQEKQIYDLKQLLEISKSLNSVLEFDRLIEAILYTVMAQMKTLGAAIFTKKSFDDDCFVLNRNYY
GFDISPDAQYSIPENHPLLRLLDKENSCLSPEEIQKNIKPDKIVESLFSLNPSLFVPLKAKNHMVGFLLL
GEQIEAGEEYTPYEKEIIMNIASLAAIAINNALLLEMTTTDMMTHLKLKHYFYTVLMEKLDTINSQGEPL
SILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQDMAARYGGEEFVVMLSNTSSKTAKKIAERI
RKSIENLSILYDEQHIRVTISIGVAEYNFDVESAKSLVERADKALYESKQNGRNRVSISK
>gnl|CDD|469491 NF041607, dimeth_corrin_MtbC, dimethylamine corrinoid protein MtbC
LSDAIVSCKKDAVLAAVEKARGGLEASDIIEKGLAAGMNEVGVLFERGKLFLPHVMMAADAMTAGVKLLE
KDMPKGASGKKLGVIVNGTVEGDVHDIGKSIVSTMLQSAGFEVHDIGRDVPIQNFIDKAKEVNANMVGIS
ALMTTTLQGQKEVIELLKEEGMRDKVKVMVGGAPATQAWADKIGADCYAENASEAVNKAKELL
>gnl|CDD|469492 NF041608, methylcob_mtaseMtbA, methylcobamide:CoM methyltransferase MtbA
MAEYTPKERLARVLKGESVDRMPAICVTQTGTVEQMEACGAFWPEAHEDAEKMAKLAEAGHTVVGFEAVR
VPFDITAEAEFFGCGIKPGTKEQQPSVIGHVVKTAEDLEKLKGYDLSDGRIGVVCEAIKILADKYGDELP
IIGSMIGPFSLAQHLNGDSWFMNIMTDEEFGLALMDFTTEFNVAYAKKMVENGADTMVIIDPTASYELIG
AEFYEKFVVPYHKKIVDAMHELGVPTVLHICGDTTNGLPLMESSGVDAISVDQKVDVATAVENVKNAVIV
GNLDPVNTLWNGTPEEVKEESKKVLDAGVGLLAPGCGIVSKTPTANLQAMIECAKSHKY
>gnl|CDD|469493 NF041609, esterase_EstP, esterase EstP
MKRTLLPPAAACLLALACSSALAAPSPYSTMIVFGDSLSDAGQFPDADGPAGATLRFTNRTGPTYQDGSG
EIYGPVSPMLLGGKLGIAPGDLGASTSPVNAAQGLPDGNNWAVGGYRTDQILDSITGQSGVVIPDGTVLR
TRPGYLVGNGFRADPNALYYLTGGGNDFLQGRVTSPAQAQAAAGRLADSAQALQQAGARYIMVWLLPDLG
LTPALSGTPLQATTSALSAVFNQELVSQLAQIDAEIIPLNVPLLLSEVLADPARFGLATDQNLVGTCFSG
NGCTENPVYGINGATPDPTKLLFNDSVHPTIAGQRLIADYAYSLLAAPWELTLLPEMAHGTLRAHQDELR
NQWQADWENWQAVGQWRAFVAGGGQRLDFDDQDSSASADGRGYNLTVGGSYRLDEAWRVGLAAGFYRQKL
EAGAADSDYKLNSYLATAFAQYQQNRWWADAALTGGHLDYDDLKRKFALGVSERSEKGDTDGELWALSGR
LGYDIAQPGSPWHLSPFISADYARVEVDGYSEKGARSTALTFDDQTRKSRRLGAGLQGKYQLTPQTQLFG
EVAHEREFEDDTQDVTMALNSLPGNDFTLEGYTPQSNLNRASLGVSQKLTPDLALRGGYNWRKSDDDTQQ
GVNLALSLDF
>gnl|CDD|469494 NF041610, alph_arabinopyran, exo-alpha-(1-_6)-L-arabinopyranosidase
KDLTLEEKASLTSGADAWHLQGVESKGIPGYMITDGPHGLRKAASDTGATDLYDSVPATCFPPAAGLASS
WNPELVREVGEAMGEECIQEKVAVILGPGVNIKRNPLGGRCFEYWSEDPYLAGHEAVGIVEGVQSKGVGT
SLKHFAANNQETDRLRVSARVSERALREIYLPAFEHIVKTAQPWTVMCAYNRINGVHSSQNRWLLTDVLR
GEWGFDGIVMSDWGAVHDRVASLNAGLNLEMPPSGTDDQIVEAVRDGRLDPEQLDRMAQGMIDLVDKARP
AMSRDGYRYDVDAHDEIARRAAQESIVLLKNEDGILPLAKGAKIAVIGEFARTPRYQGGGSSHITPTRMT
SFLDALAERGIDADFAPGFTLDDAPQDPALTDEAVAAARGADTVLLFLGLPEEAESEGFDRTTLDLPAKQ
IELLEAVAAVNPNVVVVLSNGSVVSVAPWRDQAKGILESWLLGQAGGAALADVLFGDVNPSGKLAQTIPL
DLEDDPSMVNWPGEEGHVDYGEGVFVGYRYYDTFDKPVAYPFGYGLSYATFEISDVAVEKTGANSARVSA
TVTNTSDVDGAETVQVYVAPGKADVARPVHELKGFAKVFLKAGESKEVSIDLDERAFAYWSERFDDWHVE
AGTYGIEVGTSSRDIAATVDVELDGDGKAMPLNEWSTMGEWREDPVGGPIVQRMVAEGEAGRLPALPPDN
DMMRMFLDSMPINSMSVLLGKGGRRLTEFLLDEYAKAT
>gnl|CDD|469495 NF041611, exoglucan_CbhB, exoglucanase CbhB
MSSSTRRRSAWVALAALGVSSLLAVCGITPALAAAGPGPPATVAVPAAAPVLAAAEDGEYAQRFLTQYDK
IKDPANGYFSAQGIPYHSVETLIVEAPDYGHETTSEAYSYWIWLEALYGQVTGDWAPLNHAWATMEKYMI
PQSADQPTNSFYNPNSPATYASEFNHPSSYPSQLNSGVSVGTDPIAAELKATYGTSDIYGMHWLADVDNV
YGFGATPGAGCELGPTATGTSYINTFQRGPQESVWETVPQPSCEEFKYGGKNGFLDLFTKDASYAKQWKY
TNAPDADARAVEAVYWANQWATAQGKAADVAATVAKAAKMGDYLRYALFDKYFKTIGCTSPSCAAGTGKE
SAHYLLSWYYAWGGATDTSAGWAWRIGSSHAHFGYQNPLAAWALSTDAALTPKSATAKADWSKSLERQLE
FYRWLQAPNGGIAGGATNSWDGAYATPPAGTPTFYGMGYTEAPVYNDPPSNQWFGMQAWGVQRVAELYYA
SGNAQAKAILDKWVPWVVANISTDGASWKVPSELKWTGKPDTWNKAAPGANAGLSVEVKSYGQDVGVAGD
TARALLFYAAKSGDTAARDKAKALLDAIWANNQDPLGVSAVETREDYKRFDDTYVAGGDGVYIPAGWTGT
MPNGDVIKPGVSFLDIRSFYKNDPAWSKVQTYLDGGAAPTFRYHRFWAQTAIAGALADYDRLFDDGTPPV
DTTAPTVPTGLTAGTVTSTSATISWTASTDDVRVTGYDVYRGTTRVGSATGTTYTDTGLTAATAYSYTVR
AKDAAGNVSAPSTALSVTTKTGTTVDTTAPSVPTGLVATTVTETSVALTWTASTDTGSGVTGYDVYRGTT
RVGSTTTTSYTDTGLTAATAYSYTVRAKDAAGNVSAASAALSVTTKPTTPTGTCKVTYNASSWNSGFTAS
VRITNTGTTALSGWTLGFSFAGGQRVQQGWSAVWSQSGTAVTATNAPWNGTLAPGQTIDVGFNGSHTGQN
PNPTAFTLNGAPCT
>gnl|CDD|469496 NF041612, fdxn_Clost, 2Fe-2S ferredoxin
MVNPKYHIFVCTSCRINGKQQGFCFSKDSVDIVSAFMEEIESRDLSSEVMVTNTGCFGICNKGPIVVVYP
EGVWYGNVTADDVEEIVESHIENGEVVKRLQI
>gnl|CDD|469497 NF041613, fdxn_Azotob, 2Fe-2S ferredoxin
MAKPEFHIFICTQRRPEGHPRGSCGAKGAEAVFDAFAQALIQRNLQNRVALTGTGCLGPCQAGANVLIYP
GAVMYSWVEPEDAAKIIEQHLLEGEPYADKLTPAELW
>gnl|CDD|469498 NF041614, FeSrepair_DnrN, iron-sulfur cluster repair protein DnrN
MTDFTVWETAPFGATIDHILQRYHNVHRAQLEELVPLAQKVAQVHADTFPAEVAGLLADMRNELLSHMMK
EERMLFPMINQGIGRGAAMPISVMMHEHEEHDRAIARLRELTGNFHAPAGACGSWTRLYRLAEEMVNDLT
DHIHLENDILFARVLAS
>gnl|CDD|469499 NF041615, Feoxidase_Iro, iron oxidase
MSEKDKMITRRDALKNIAVVAGGIAVTTMMGVGTANAGTVSKASVQYQDHPHGKQHCSVCANFVAPHSCK
VVAGTIDPNGWCVAFVPKSA
>gnl|CDD|469500 NF041616, T2SS_C_SYNERG, type II secretion system protein GspC, SYNERG-CTERM-associated variant. This HMM describes the GspC subunit of a rare variant form of type II secretion system (T2SS) found exclusively in the Synergistota, with the SYNERG-CTERM protein-sorting system. SYNERG-CTERM is a C-terminal sorting signal with an invariant Cys residue in its signature domain. The sorting enzyme for SYNERG-CTERM proteins, MrtS (myxosortase S), is a homolog of the MYXO-CTERM-processing enzyme MrtX and of the eukaryotic CAAX prenyl protease Rce1. SYNERG-CTERM proteins are predicted to become surface-anchored by a lipid group attached to a C-terminal Cys sidechain
EAAAPWLGALLAALALAWLASGVLEGRLAPLLLDARIAAAIRASQAPPSDAEVEPAGGLRDFVAANPFGV
AQRPEEAVVKAPELEPETARVASLDGLSLAGTLPGVAAWIDGPGGTSLVLKGQEVGGFKLVEVKPDSVVL
VKGEEVHEVYLRLSGGTAAKAPAPSKGADSPAPPPAGSNSPASGVQAASPGQEGVVARELVDSLLMNPYD
ELKKVRLIPKFDGGKAQGMEVANIDPDSVLKELGVQKGDVIQSVNGVPIRNMGDVANAINSLMGGSRFDV
SVVRGGKPVMLNYVVR
>gnl|CDD|469501 NF041617, T2SS_L_SYNERG, type II secretion system protein GspL, SYNERG-CTERM-associated variant. This HMM describes the GspL subunit of a rare variant form of type II secretion system (T2SS) found exclusively in the Synergistota, with the SYNERG-CTERM protein-sorting system. SYNERG-CTERM is a C-terminal sorting signal with an invariant Cys residue in its signature domain. The sorting enzyme for SYNERG-CTERM proteins, MrtS (myxosortase S), is a homolog of the MYXO-CTERM-processing enzyme MrtX and of the eukaryotic CAAX prenyl protease Rce1. SYNERG-CTERM proteins are predicted to become surface-anchored by a lipid group attached to a C-terminal Cys sidechain
EAKGVLAYRGGKFYAVSEPAGGDLSRETRLLFVPYRTLSLRPFSFPFGRVSAIREALSLQFRPILGGLED
LEIFPQVTEQRGRLTRGAAWILSKEERSEVEEGVGRNGKSTVWPAPAAFAAEAGGNGAVVWADEEGICSL
LFEDGTPVLYRWQPRSEGTAEEEADWLRKYAGSAGREPPDSIRIDVAEDGERAELRRAAEATLAAFPSLA
SLSLSSRGLDTAEVTEALFKLWFRALKAASAAGLIFLALSFLSLIQNKLYLDRFRAAAVEIYRSAFGPGP
VRDPLSQARKRLAQLTGGGVSLTLEDTLALFGAAWKALEDGKDISLDTLRYGEEGTEIIGQAAKVEAIQA
LQDALAASNGFAVKLGDIQQIPGGGLRFTLTVRWSGR
>gnl|CDD|469502 NF041618, T2SS_M_SYNERG, type II secretion system protein GspM, SYNERG-CTERM-associated variant. This HMM describes the GspM subunit of a rare variant form of type II secretion system (T2SS) found exclusively in the Synergistota, with the SYNERG-CTERM protein-sorting system. SYNERG-CTERM is a C-terminal sorting signal with an invariant Cys residue in its signature domain. The sorting enzyme for SYNERG-CTERM proteins, MrtS (myxosortase S), is a homolog of the MYXO-CTERM-processing enzyme MrtX and of the eukaryotic CAAX prenyl protease Rce1. SYNERG-CTERM proteins are predicted to become surface-anchored by a lipid group attached to a C-terminal Cys sidechain
PSLPELRGMPREARRLLLALLLALLIWAAALSVWSDASSLDARNELQERRFEDLLDVAIQYRSLPQREGR
AAGKEDPLSAVSEIVDKLGLKDNVVQLSSSPRGLVVQLERLYGEELGRLLQELERRGLSVKSAELRALPS
QKDERLISVTLVVGGAR
>gnl|CDD|469503 NF041619, T2SS_N_SYNERG, type II secretion system protein GspN, SYNERG-CTERM-associated variant. This HMM describes the GspN subunit of a rare variant form of type II secretion system (T2SS) found exclusively in the Synergistota, with the SYNERG-CTERM protein-sorting system. SYNERG-CTERM is a C-terminal sorting signal with an invariant Cys residue in its signature domain. The sorting enzyme for SYNERG-CTERM proteins, MrtS (myxosortase S), is a homolog of the MYXO-CTERM-processing enzyme MrtX and of the eukaryotic CAAX prenyl protease Rce1. SYNERG-CTERM proteins are predicted to become surface-anchored by a lipid group attached to a C-terminal Cys sidechain
RRFVLGLLALALGLVLGLRVFFPWEAAAELAFARAARSLAESGIFLTASSFEVEGRFPPRFTYRGVRLDS
PLGSGRAGELKVTPSPIGSLLGGAPTASLELDRGALVLPGRQGAFWGGGSARLVLRPGRVMVEDIDLKGD
LSASGSAELSLETGKITEADLTLKTPAELDRALEMASSMLPLKREKPGEWRLKR
>gnl|CDD|469504 NF041620, MXAN_5187_fam, MXAN_5187 family protein
RLKFWVFALLVLGAGAAHLPFLSGPLSARAVEDADARALAAAAEAVRALLALRARARSVALALAALPDVV
RAVLAKAGAEPKRGGAEPPTAERFAAVRAAAEVPLPAALKGAAVVDAGGRVAAAVGVAGGEPSEDAALGG
YPAVADALAGYARDDAWGAPHRLYSVPVRPVEAEVTGRAVGAVVGLPLVDAAFLRAAAGGTGAAALLVAD
GDRVASTAGAEKFLEEGLAQLLAGGQSDAVLLAGKLFVLGLGKLPRVTSGGDVLGGAAALLVGAARVLGG
GGAAAVAAAQTAPPLALLAAYQQNALVGLALLLGLGLVWTLLGGGARAALLEAAPPLLAADDEFLRGAKG
AQAPLAAGPFGTAPAAILRAAPAAVAEPAAKGEAAPRRAADLEAVLGAIPAAPAPPAPSPPPAEPFAAPP
PPPEPDPSEFAAPAPTAPLPPAPPPRGAAFAFPDEPTAAYSLQQAADPPAAAAAQAPPPETTRVAAAPPP
LLAASAPPTTAAPPAPPGAAAAAAAAARAAAAVALSEEEAHWQEVFEEFVRTREECGEPTDGLTYEKFVQ
KLRKNKDQLVQKYACRTVRFQVYVKEGKAALKATPVK
>gnl|CDD|469505 NF041621, MXAN_5187_C_dom, MXAN_5187 C-terminal domain. This domain occurs at the C-terminus of MXAN_5187 from Myxococcus xanthus. Member proteins, most of which belong to Myxococcales branch of the Deltaproteobacteria, can have very different architectures outside of this domain
LEEAEVRQVYEEYVAAKRACGEPTDGLTYEKFARKLRKQKPKLMEKYGCRDVDFSVVVKDGKAALKARPV
>gnl|CDD|469506 NF041622, KwaA, anti-phage protein KwaA
KIGLYILSLWLLFVLIIIITIDIPICFGENCHFIGFYELLKSNIIPIICILLLIIGILFYFRFKYRLKGA
TSLPFKITKIENINYEHLTFLATYIIPLVSFDFDSIRYLIVLILLLVVIGAIYVKTDLFYANPTLALLGY
RIYKADGEFRDGIRENIILISKDKLKKNDKVQYIKLDDNIYF
>gnl|CDD|469507 NF041623, KwaB, anti-phage protein KwaB
LKEKLNTVILDDNIGIKVYFVLKDDEENEIKKADIENDALPELKTMFVESINNKIINNEELSILNLSTAD
ERKNVLYEYDLDELPEELSLLETVLENDDIDKFNFNNDDLSSIKGLIIKIGNEDNQIVLYKKHYPVSLLK
RGKFLLVKSNNRFEKLDDDILRINPKFDFLRVDGELYILDLKTLEKSFGFHDVIKNEATEGIEAIESLGL
VEDIEVLRELIDDISFARKLTKVAKNSPVLQKIPNETIISFAKNHPALKGKIKYNDDGSKIVLDTKVSKK
LFIKLLNDDFLTSELTKLYYESLAKD
>gnl|CDD|469508 NF041624, isoafr_syn, isoafricanol synthase
MTTTAASGPARPSPLTRRTALLDIPFPARLSPHAERARRHTLQWLRRFGLLTGEAATAEYDALRLERLMA
YFYPDATGADLALAADLNAWFFVFDDQFDGPLGRRPEAVARLVDTLVRTMTEDGAPAPAAPDGPLVESFR
DLWRRITAGRPPVWRDRFRHHWRAYLAAYHREALNRTADRLPSLEAFLAVRRHSIGVQPCLDLAERCGGY
TLPDELHGGFPLAEMREITDDVVIFVNDIVSLDKELAAGDVNNSVIVLREHTGCTLEEAVRHIAALANAR
VARFQELAARLPALLAEAGVPPEVRRHVDHYVDGMRHVMAGNLAWSLETARYDERGIAAVSGGRQRPWAG
L
>gnl|CDD|469509 NF041625, methfumCoahyd_Halo, 2-methylfumaryl-CoA hydratase
MTDWTDPETFAAALDRAETREKGNYFEDFAEGDTIEHDPGLRLTRHGNEQWMSQTLNHDPAYWRPDAARE
RGFDEPPIHPDYLLACVMGPSVEDLSEKGGYFLGRTDVRFHDDAVYPGTELRVESTVVATRTSSSRPDYG
IVTWETRGYDADTGEVLCSYERTNMIPRREPVATDGGESTRADSGGSSTDSDEDDDPDLPETLVAPDGPY
FEDFRAALDRAADRDAAVAYRHERGRTMDDVLVAGLPLATLNTAKQHHNADAMADSPSGEIVAYGDVTRS
VALGHARSDEATYREVGFDDERFHDFVTAGDTVYGFTRVLDADPDAGPDRAGAVTFEHVAFNQDDEPVYS
GTRTALIR
>gnl|CDD|469510 NF041626, malyCoAlyase_Halo, L-malyl-CoA/beta-methylmalyl-CoA lyase
RLCRTFQTAPAAVPKEDSAKYLRSGLTAEGFEAPDWLVPDLEDGTAPDMKDEALENTVELLEYAPDFAGE
IWPRVEWSYDDERLRERGREQIETLVREVGEHIDGVVVPKVGRLEDVERAASAVAEAEREYGYPEGSIEL
AVIVETARARSDLREIARFGEDSRLAGLVFGPVDYTAELGGRELDGGRPRWDGLLEALSNEASANDLVAI
GGPFDRLFRERAGVTFYNGDAYADQVEREARVGLDGSWSLHPKQTAQANRIHMPTPDELERDVRKIERFN
EAKSEGTGAVTIDGQMVDEATFKNFANTVETVRAIDDARPEQTAERYDDDLLERALALD
>gnl|CDD|469511 NF041627, NaLiK_antip_UmpA, Na,Li,K/H(+) antiporter subunit UmpA
LLSLLRQARDSLRDLAPVVLVIGFFQLVVIRQPLPDSLALVDLLIGLVLVVIGLTLFIKGLELGLFPIGE
SLARAFARKGSVFWLLLFAFALGFGTTVAEPALIAVAGKAAEVVAEGGLIADTDEAQARFAFELRMVVAL
SVGSAVVLGVLRILKGWPLHLMIIGGYVIVLLLTLIAPDAIIGIAYDSGGVTTSTITVPLVTALGVGLAS
SIKGRNPMLDGFGLIAFASVMPIIFVLLFGIFG
>gnl|CDD|469512 NF041628, NaLiK_antip_UmpB, Na,Li,K/H(+) antiporter subunit UmpB
MTLLTTFWSTLLDILPIVAIIFGFQYLVIRKPIKRLPQVLVGFLMVWVGLSLFLVGLEQALFPMGELMAE
QLTSEDFLPALAEGAQRHWSDYYWVYIFAFAIGASTTIAEPSLIAVSIKAGEISGGTINPLMLRIAVALG
MAFGITLGTWRIVMGLPLQWFVLAAYVLVILQTLRSPRSIIPLAFDSGGVTTSTITVPIIAALGLGLASS
IPGRSPLMDGFGMIALACLFPIITVMGYAQIAQWREKRHSQK
>gnl|CDD|469513 NF041629, anti_IS1548_end, IS1548 end spurious translation
MIDLKRNLFKIDVRAQKDEEKVFMRTA
>gnl|CDD|469514 NF041630, CBS_CbpB, cyclic-di-AMP-binding protein CbpB. CbpB (c-di-AMP-binding protein B) has two CBS (cystathionine beta synthase) domains (see PF00571). When levels of c-di-AMP are low, CbpB activates RelA, a bifunctional (p)ppGpp synthetase/hydrolase
KEIEELLLENIEDFLIPAEKVAHVQDTNNLEHALLVLTKVGYSKIPVLDKDKKFVGLISLSDITDYMLGL
ERIEFEKLSELKVADVMNTDVPTITDDYDLEEILHLLVDHPFLPVVDEDGIFLGIITRREILKAVNYLLH
EFE
>gnl|CDD|469515 NF041631, KRQAASG_repeat, KRQAASG repeat spurious translation. This AntiFam-like HMM describes spurious translations from an intergenic repeat common in Burkholderia
KRQAASGKRQAASGKRQAASG
>gnl|CDD|469516 NF041633, trifunc_aldol, KHG/KDPG aldolase/sugar kinase fusion protein. The N-terminal region of this protein resembles the bifunctional KHG/KDPG aldolase (4.1.2.14 and 4.1.3.16), while the C-terminal region resembles 2-dehydro-3-deoxygluconokinase and 2-dehydro-3-deoxygalactonokinase
KIFEKLKKNRLIALLAPESAEECVPAYEALRPGGIVLEIAFRTEAALDGIKAILKRYPDALVLAGTVLTK
EQAEAAIAAGAAGIVSADYIPEVVEACVEKDVMCVPGGLSDAGKQLVQKAELYGCSLEELREKYPYQWVY
KLFPAEAGGLGGLDLAKAWKGPYKDVTVIYTGGITLENLKEYLAKDPGGIFCASALTKHIDDPEKMKAEI
KRWLDILKPGRQKKPVSQPKKERASAGGPKVVTFGEIMLRLSPPGGRRFSQADTFEATFGGAEANVAVSL
AQFGLNSRFVTALPDNDIGQAAVNSLRKYGVDTSFIVRGGDRIGIYYLEHGASQRPSKVVYDRAGSAISE
ISPGDFDWEKIFEGAGWFHWTGITPALSDSAAEILLEALKAAKEKGITVSCDLNYRKKLWSEEKAREVMT
ELMEYVDVLIGNEEDAAKVFGIKAKGTDVEAGKLDEEGYKDVAEQLVERFGFKKVAITLRESLSASDNNW
SACLYDGKEFYFSPKYHVHIVDRVGGGDAFAAGLIYALLKGKTDQEALEFAVAASCLKHSIEGDFNLVSV
EEVERLAAGDGSGRVQR
>gnl|CDD|469517 NF041634, HAEPLYID, HAEPLYID family protein. This family is named for start of a long and nearly invariant motif near the protein N-terminus. Many members of this family previously carried an untraceable and probably incorrect annotation as phosphoribosylformylglycinamidine synthase
LLLLLLLAASQAASAQSDDSELDDVKKPPKVLHAEPLYIDLIRDLGARKGEKEWNVGLGLTDNKNYDEYE
ALVEYEWAPINRLGLEVELPFSFYSPTGSSTDDSIPSNRLESLKLAAQYTFLVSEKHQTSMALGYIHEFE
LTDFNNYGKEKLFKGNVYNPFFVAAKRWGSNFHTLLYTGPVIEHHFGSNHTETSYQINTSFHYMIPGTRN
FIGVEFNKEFSDGDFDMVLRPQMRVGIADNLLIGIVTGIPINRENERLSSFLRLIYEP
>gnl|CDD|469518 NF041635, STM3941_fam, STM3941 family protein
SKWKNILLLIGSLVFVLLGIFLLLNAFSSSPILIIIIGILGILFFGLCGLFFLYKLFRRKPLLIIDEEGI
TDNSSAKSAGTIPWKDIRGIRLIKIRGQKFIAIDVKDPEKYIARETSGFKKRLMRLNLKLGGAPINISAS
NLKMDGEELLELLNEYL
>gnl|CDD|469519 NF041636, slam_lipo, Slam-dependent surface lipoprotein
GVFSFAQVGDQDVYFGEWSKVGFGADDGNGTHYVFYVGDNTATSNMPTSGTATYSGQGINNYAPGGGDLL
SGTLNFTADFGSKTLSGSITNAAGGAVNINAADISGNSFSGTANASSGSSGGSVEGKFFGANAEELAGIA
TFNGKSYDTAFGGKK
>gnl|CDD|469520 NF041637, FGAM_small_mem, phosphoribosylformylglycinamidine synthase-associated small membrane protein. This small protein averages less than 40 amino acids, nearly all of which, for the last 30, are hydrophobic and suggest integration into membrane. Members are regularly found encoded between or next to PurS and PurQ subunits of phosphoribosylformylglycinamidine synthase. The family appears to occur only in the Hyphomicrobiales, a branch of the Alphaproteobacteria
DDTARAIRFMAIKAAIFILLPALAALLAVLFLL
>gnl|CDD|469521 NF041638, QRL_CxxC_CxxC, RRQRL motif-containing zinc-binding protein. Members of this family, found in multiple species of Streptomyces, are judged by be zinc-binding by the pair of CxxC motifs in the C-terminal region. The family is named for a near-invariant QRL motif (usually RRQRL) closer to the N-terminus
LPTFPWRLAPDGLATRRQLRARGLRPGGQPVAAQLLRRRRRLVAYLYRIDLAKPKRPMTPAQWAALDKAM
AARRTCPTCRRDAGYCIPRSLGMCLDCA
>gnl|CDD|469522 NF041639, YicS_fam, YicS family protein. Members of the YicS protein family, found in Escherichia coli and related species, average 100 amino acids in size, with a signal peptide and two widely spaced invariant Cys residues
KRITLLLLAVLLALPGVAHAESPYDGLKFALRKQQVLKDLRKHCTPPSALSDEKFANTVLSSEQNKLHVR
EAALALERNNQDNYWEAIGKVECPDM
>gnl|CDD|469523 NF041640, AmoB_BACT, bacterial ammonia monooxygenase, subunit AmoB
IKNLLALAVGLAGLLAAALLLTPTPAAAHGEKAQEPFLRMRTIQWYDVKWSKDKLAVNEEVVVTGKFHVF
EDWPEAVAKPDAAFLNVGTPGPVFIRTESYINGQPVPRSVALELGGDYEFKIVLKARRPGRYHIHPMFNV
EDAGPIIGPGQWVEITGSAADFTNPVKTLTGETIDLETYGLANGVFWHLFWMALGLAWLLWWVRRPLFIP
RYRMVEAGGEDELITPLDRKVGKAVLVAVLLLVLGGYASANSKYPITIPLQAGLDRIEPLPPAPNGPVSV
KVTRAEYRVPGRSMRMTLTITNNGDKPVRIGEFATANLRFLNPAVADVDPGYPDDLLAPDGLSVDDNSPI
APGETRTITITATDALWEVERLDDLIYDPDSRFGGLLFFYDESGERYIAEIGGPVIPVF
>gnl|CDD|469524 NF041641, AmoC_BACT, bacterial ammonia monooxygenase, subunit AmoC
MATTTEPSKRASGAAYDTWPLLDLKWYAFGLGLLLVFYIGVRWYQGAYGWSAGLDSFEPEFETYWMNLLY
IELVVEVLVASVLWGYLWKTRDRNLDALTPREELRRYFTLLMWLSVYAFAVYWGGSYFTEQDGSWHQVII
RDTDFTPSHIIEFYLSFPIYIILGGASFLYAMTRLPLYAKGISLPLVLAVVGPFMILPNVGLNEWGHTFW
FMEELFSAPLHWGFVIFGWFALAVGGVLLQIVARLSELLD
>gnl|CDD|469525 NF041642, RAxF_45, RAxF-45 family protein. Members of this family of small proteins are found broadly within the order Bacillales. The family is named for its best conserved motif, a nearly invariant RAxF motif, and its small size, about 45 amino acids in length
RAVLARGKWLEFLYICRAIFHAVAVNGIRLSFFSNLIAK
>gnl|CDD|469526 NF041644, CBO0543_fam, CBO0543 family protein. This family is named for an uncharacterized founding protein from Clostridium botulinum. The family is rather hydrophobic, about 165 amino acids in length, and found in genera such as Bacillus, Paenibacillus, Desulfosporosinus, and Weizmannia. The function is unknown
KKKWREYLLVFLFKQLISTILDLIVVEKGLWEYPVRLFPKIFPTSFLFDLFVYPVLCVLFNQYYPKKKSL
LKKILYYFLWSAIATLLEVLLEKYTDLIHYHKWNWYYSFISLFILF
>gnl|CDD|469527 NF041645, prot_kin_PA4780, PA4780 family RIO1-like protein kinase. Members of this family are putative serine/threonine-protein kinases, closely related to founding member PA4780 from Pseudomonas aeruginosa PAO1, which was shown to be upregulated by and important for the biodegradation of phenanthrene and naphthalene. Members belong more generally to the RIO1 atypical kinase family (see PF01163)
MKTPKRLQPLVDDGLIDEVLRQLMSGKEASVYVVRCGDEIRCAKVYKEANKRSFKQAVQYQEGRKVRNSR
RARAMEKGSRFGRKEQEEAWQNAEVDALYRLAAAGVRVPQPYGFFDGVLLMELVTDEEGDAAPRLNDVSL
TPEQAREYHALLIRYVVRMLCAGLVHGDLSEFNVLVDADGPVIIDLPQAVDAAGNNNARRMLERDVNNLA
AYFGQFAPELLDTQYAKEIWALYEAGELTPDTELTGHFEESTGPADVDSVLREIDAAREEEEAR
>gnl|CDD|469528 NF041646, VC0807_fam, VC0807 family protein. Members of this broadly distributed bacterial protein family are hydrophobic in nature, and apparently homologous to members of the DUF3159 (PF11361) family
KLLLDLLFNVVLPLLIYYKLSGAFGLGPVGALLAAAAVPLAYGLWDLVRRRKVNALALLVLVSLLLSLVL
SLLTGDPRLLLIKESAVPGLIGLAFLVSLLTRRPLVFYLARNFVALGGPEREAALERLWRSPAFRRALRR
LTLLWGVGFLLEAALRVVLAYSLPVDRMTALSTVVSAVPSGALIVGTLW
>gnl|CDD|469529 NF041647, ABC_perm_CPBP, ABC transporter permease subunit/CPBP intramembrane protease. The C-terminal region of this ABC transporter permease contains a CPBP family glutamic-type intramembrane protease domain, related to the eukaryotic type 2 CAAX prenyl protease Rce1
RLKIVKTIFRKELLDTLRDKRTLFMMIVLPILLYPLLFIGMSQLMSAQQAKLEERTSRVAVWGAAPAPLL
AEKLELALRLELEDEEKLEIVDSDDAPEAALEEGEIDAVVVIPPGFEEALAAGGSASVEIYYDSARDRSR
TARDRLRDALEEYRKELVEERLEEAGLPEGFLEPIEVESEDVAPPEKRGGSILGMILPFLLILMLLLGAF
YPAIDLTAGEKERGTLETLLTAPVSRLEIVMGKFLAVFTIALITALLNLLSMGLTFAFGLSQLGGGAGAG
LDFSLPPSALLIILLALIPLALLFSAVMMAVAVFARSFKEAQNYLTPVMLVVMLPAYVAMLPGIELNAAT
ALIPVVNVALLIKELLLGKADLELIFLVLLSTAAYAALALLLAARIFNREEVLFGEGGGSPLLLERRSNI
RPGGVPTPGDALLLFAVVLLLLFYVGSLLQLKGGRNLLVGLLVTQWGLILLPVLLLLYYKKDDFRKTLSL
RLPSLRALLGAVLLGAGAWVLVFALSALLSNRLLPPPPELAEALEELLSLLLSGAPLWLLLLVVALSPAI
CEELLFRGFILSGLRRRMSPWAAILLSALLFGLFHLSLYRLLPTALLGILLGYLVYRSGSIFPSMLMHFL
NNGLAVLLSRY
>gnl|CDD|469530 NF041648, spore_exo_CotA, CotA family spore coat protein. CotA, as the term is used in Clostridium difficile, is a spore coat protein also reportedly detected also in exosporium. Homologs are found in a number of related endospore-forming bacteria
CCCKKSMRRALELLCDPRLASLVDFNAFAFITDNFLVGTSLELPGASTAPYDNLGALTASFVRFTPCNCD
LIDISGTLYYPIPLTLPGGITTLATPVSQVSLCALDAVAFQYAGDTEETTAANYQALKQLLKQLLDGKDC
GCDCHPKCPDCCCNDGILNELATGNLSRTVSLTAGPLVLQNAEVLGRVGNVLVLANDTDNRIYFVCADSV
GFIG
>gnl|CDD|469531 NF041649, ceramidase_neut, neutral ceramidase
LSVGRGIADITGESADCGMLGYGKTDQRTAGIHLRLRSRAFVFDDGGDGHARLLLVVAELPLPMQNVTDE
VLRRLADSYGDTYTEQNTLITTTHTHSGPGGYCGHLLYNLSTSGFRPATFAAIVDGIVESVRHAHADLAP
AEVTLSHGELHDASINRSPSAFDRNPAADRAFFPDRIDPHTTLVRIDRGDRTVGAIHFFATHGTSMTNRN
RLISGDNKGFAAYHWERTVGGADYLAGQPDFIAAFAQTNPGDMSPHVDGPIAYGPARPEDELENTRRIGL
SQFEDAVEQLDNGTPIGAGVDARFTYVDLGSVLVRGEYTPDGQPHRTGRPMIAAATMAGTDEGEGFPGFH
QGRNPFWDKVSRGIYRLARRLRAAQAPKGIVVPAHLLNRLQPFVQEIVPVQLVRIGRLYLIGIPGEPTIV
AGLRLRRTVASIVGADLADVLCVGYSNAYIHYVTTPEEYLEQRYEGGSTLFGRWELPALMQTVAGLAEAM
RDGRPVTPGPRPRPTKPLSWLRDAPADTGSFGAVVAEPSATYRPGQVVEAVFVSALPNNDLHRNGTYLEV
VRRDGEQWVRVADDGDWSTTFRWQRQGRAGSRVTIRWDIPADAAPGRYRIVHHGTARDADGRLTPFTATT
REFTVG
>gnl|CDD|469532 NF041650, nod_mtase_NodS, nodulation methyltransferase NodS
YQLLERELAADDPWRLDSNPFERERHRQMLRLSLSQGPITNALEVGCAAGAFTEKLAPHCQRLTVIDVVP
QAIARTRERTKRPPHITWIVSDIQQFSTAELFDLIVVAEVLYYLGDVAEMRAAIRNLVRMLAPGGHLVFG
SARDANCRRWGHVAGAETVIAMLNEELVEVERVECQGQSVNEDCLLARFR
>gnl|CDD|469533 NF041651, nodul_NodU, nodulation protein NodU
MRICGIKLTHDGAIALVEDGRLVFCIEQEKRGNNPRYQAIDNLDAVVAALAEHGLDPRDVDQFVIDGWDG
EVESQFQVLSGAAPVTLKGAPYVERHAEGLLTSHDGSGLMLGGRSFPYRSYPHVTGHVASAYCTSPFAKA
GQPAFCLVWDGCIFPRLYHVERRGARFIECLFPMIGHAYAAAGHHFGPYKQANRTGWDLGVAGKLMAYIA
LGSVDEDIVAVFQELYEERFAGDTELARRYRANINSAESSLAAVHDFFEASALRLKAKRPEDVLASFHVF
LERLLVREMAIALQRHSGLPGPRNLCIAGGCGLNIKWNSALRATGLFDAVWVPPFPNDSGSAIGAACSAM
AADKGFVPLEWSVYSGPALQRGDVPPGWEAAPCSMRELAAILASNKPVVFLAGRAELGPRALGGRSILAA
ATSPGMKDHLNDIKLREHFRPVAPICLEDRAPEIFSPGTPDPYMLFDHQTRAEWRDKIPAVVHLDGSARL
QTISRTSQHKVAELLVEYEKLTGIPLLCNTSANLHGRGFFPDAAAACEWGRVEHVWCDGLLWTKTA
>gnl|CDD|469534 NF041652, Nud_hyd_Dein, Nudix hydrolase
MQHDERFHVPVTLRAAGVVILNEAGDILLVRERGVPGQPGKAGLWHIPSGTVEPGENPQDAAVREAWEET
GLRVRLVKFLNAYLGRFPDGALILRHAWLAEPLPGQTLRPAFTDEVAEARYVSRTEFDALYAAGQIRMYH
TKLFYEDALRER
>gnl|CDD|469535 NF041653, Nud_hyd_Meth, Nudix hydrolase
LITEVDENDNFLGLRPREDFYSGKHIHRASHLILLDPENRMLLQKRAPQKLWYPGRYTYSVSGTVADESY
EACIAREMLEEIGISVPFRKLFKIPCILENKGAFHMVFSGRCSEENASLIRHDPEEAVSVEWVELEELHR
AVKEEPENYTPALRAGIIKIFEEGCEKYIF
>gnl|CDD|469536 NF041654, GlcNAcase, beta-N-acetylglucosaminidase
LLLLLFGLLSSLTLFAQEFHLQPTPQQVVVQGDSIALPQQYQLIGGNSANAPHALSLLKSLLPKQTSKKG
FRIYIGEKGDKAVKKYAKKIPNKAEGYYLKIDKKKIVIAGADERGTYYGVQTLAQLLTLGKLPLGEITDY
PDVPYRGVVEGFYGTPWSHEARMRQLEFYGENKMNTYIYGPKDDPYHSSPNWRKPYPEKEAAQLKELVDV
ANENEVDFVWAIHPGQDIKWNDEDRDLLLAKFEKMYQLGVRSFAVFFDDISGEGTKADKQAELLNYLDDH
FVKVKKDVTPLIMCPTEYNKSWSNPEGGYLTTLGEKLNPSIQIMWTGDRVVADIDKETMEWINPLIKRKA
YIWWNFPVSDYVRDHLLLGPVYGNGTDIADDMSGFVSNPMEHAEASKIAIYSVADYTWNMEKYDSEASWK
RAIKDLMPEHAEALETFAAHNSDLGPNGHGYRRDESVAIQPAAEAFLKSYKENGEIDEAAYRQVQEEFRK
MVEAADILLASTENPPLIDEIRPWLKQFKLLGEYGLEVLAMQKALKAGDKEAFERSYKHAKALQQQMYEI
DQTYNQNPYQPGVKTGSKVLLPLIDALFATLTERYNKQYGTNLDTRANYNPHKLYSNVEQLKNLPLQLKG
KTLNISPSLEVIKWQAGGYLTIELDYAYTLKSIEIDLGKPEVAEWFRLEVSADGKEWKTVELKQKARKRL
KASVGGEKVKFVRFTNVSGQEQEVYLKRFRLTE
>gnl|CDD|469537 NF041655, MM0924_fam, MM0924 family protein. Members of this family occur in both archaea and bacteria, and share some sequence homology with the domain DUF2642 (PF10842)
MEEFLSHLLGKEVDVYCGGSATFRGKVVKVEDGVLTLEDEDDKYTYIAIDKIIAVWE
>gnl|CDD|469538 NF041656, CPBP_MmRce1, MmRce1 family CPBP family CAAX prenyl protease. MmRce1, an archaeal member of the same family CPBP integral membrane glutamic-type protease as the eukaryotic type II CAAX prenyl endopeptidase Rce1 (Ras and a-factor converting enzyme 1), was crystalized and studied to gain insights into Rce1 function. It was shown to act as an endopeptidase on the eukaryotic protein-derived synthetic substrate ARSGAKASGCLVS, only if Cys residue is farnesylated. This model substrate ends with a CAAX motif (Cys-Aliphatic-Aliphatic-Anything)
MIPNYKYKPKVYFAATFIVTYALWFAGAYLSFQDDKSGLYMLLMLPGLMAPFLISLFMIFTSKNSDLKKD
FINRLINLRLIRPKMLPVFFLIMPLSVLVSIFLSLPFGGSVSQFQFAEGFSFSSGFVPVLLLLLLAAGFE
ELGWRGYAFDSLQSRYTYFKASIIFSILWSLWHFPLIFVNNSYQYEIFHENIWYGVNFFVSIIPMGVIIS
WICIKNGKSIPAAILFHFIINISQEALNITQTTKCIETVVLIVVAAVIIALDKEMFFSKEH
>gnl|CDD|469539 NF041657, ompB_ricketsia, outer membrane protein OmpB
MAQKPNFLKKLISAGLVTASTATIVAGFAGSAMGAAIQQNRTTNAAATTVDGIGFDQTTAPANAGVAPNA
VITANNNNGINFNTPAGSFNGLFLDTANNLAVTVSEDTTLGFITNVAGQANTFNITLNAGKTLTITGQGI
TNQQAAATKNAQNVVAKVNGGAAIPVNDLSGLGPIDFGAAASVLVFNLANPTTQKAPLILGDNAKIVNGA
NGTLNITNGFIQVSDKTFATVKTININDGQGLMFNTNADAANNLNLQAGGNTINFNGTDGTGRLVLLSKN
GAATEFNVTGSLGGNLKGIIEFNTVAVLGQLIANAGAANAVIGTNNGAGRAAGFIVSVDNGNAATIDGQV
YAKDMVIQSANAGGQVTFRHIVDVGTGGTTAFKTAASKVTITQNSNFGGTDFGNLAAQIVVPNAKTLTGN
FTGDASNAGNTAGVITFNANGTLISASADANVAVTNNITAIEASGAGVVQLSGIHAAELRLGNAGSIFKL
ADGTVINGKVNQTALVGGALAAGTIQLDGSATITGDIGNGGGNAALQGITLANDASKTLTLGGANIIGAN
PGGAINFQANGGTIKLTSTQNNIVVDFDLAITTDQTGVVDASSLTNAQTLTINGKIGTIGANNKTLGQFN
IGSSKTILNDGDVAINELVIGNNGSVQFAHNTYLITKTTNAAGQGKIIFNPVVANNTTLAAGTNLGSAAN
PLAEINFASKAANADTILNVGKGVNLYATNITTTDANVGSFVFNAGGTNIVSGTVGGQQGNKFNTVALDN
GTTVKFLGNATFNGGTTIEANSTLQIGGNYTADFVASADNTGIVEFVNTDPITVTLNKQAAPVNALKQIT
VSGPGNVVINEIGNAGNEHGAVTDTIAFENASLGAVLFLPSGIPFNDAGNTIPLTIKSTVGNGTVGGFNV
PSVIVSGIDSVIADGQVIGDQNNIVGLGLGSDNGIIVNATTLYAGIRTTNNNQGTVTLSGGIPNTPGTIY
GLGIGNGAPKLKQVTFTTDYNNLGSIIATNATINDGVTVTTGGIAGTDFDGKITLGSVNGNANVRFVDGT
FSTSTSMIVTTKANNGTVTYLGNAFVGNIGSSDTPVASVRFTGNDSGAGLQGNIYSQVIDFGTYNLGILN
SNVILGGGTTAINGEIDLLTNTLTFASGTSTWGNNTSISTTLTVANGNIGHIVIAEGAQVNATTTGTTTI
NVQDNANANFSGTQTYTLIQGGARFNGTLGGPNFAVTGSNRFVNYGLIRAANQDYVITRTNDAANVVTND
IANSPFAGAPGVGQNVTTFVNATNTAAYNNLLLAKNSADSANFVGAIVTDTSAAVTNAQLDVAKDIQAQL
GNRLGALRYLGTPETAEMAGPEAGAVSAAVAAGDEAVDNVAYGIWAKPFYTDAHQSKKGGLAGYKAKTTG
VVIGLDTLANDNLMIGAAIGITKTDIKHQDYKKGDKTDVNGFSFSLYGAQQLVKNFFAQGSAIFSLNQVK
NKSQRYFFDANGNMSKQIAAGNYDNMTFGGNLTVGYDYNAMQGVLVTPMAGLSYLKSSDENYKETGTTVA
NKQVNSKFSDRTDLIVGAKVAGSTMNITDLAVYPEAHAFVVHKVNGRLSKTQSVLDGQVTPFISQPDRTA
KTSYNLGLSASIRSDAKMEYGIGYDAQIASKYTAHQGTLKVRVNF
>gnl|CDD|469540 NF041658, ornithlipidmtase_OlsG, ornithine lipid N-methyltransferase
MSDFTLFLGKFLRHGTAIASLAPSSPWLSRATVSNIDWDTARVVVELGAGTGPITRVLAERAHPDCRVLV
LERDPDFARLLRDRFAGRPNLEVVEGDVRDLAAILQDRGIARVDHIVSGLPVPSFPKDLQRDLFRVVGRV
LKPEGTYNQITEMPWVYRRFYRRFFDEVRFVFEPRNLPPAGAYFCRGVKPA
>gnl|CDD|469541 NF041659, Papain_Inhib, cysteine/serine endopeptidase inhibitor
MRATRRKALGAVAAAAALPLTAAGTAFAAIPFGQPMNGKATYYNDAGYGACGTQINASTQMLVAVPAAYW
TTANPNNDPLCRGVSVEVTYNGRTITVPVRDKCPSCDSTHIDLSLPAFAKLADPDLGVIN
>gnl|CDD|469542 NF041660, oxygluDhInhib_OdhI, oxoglutarate dehydrogenase inhibitor Odhl
MSDNTGIPEAQVETTSVFRADLLKEMESGAAAAPADSGAENLPAGAALLVVKRGPNAGARFLLDQPVTTA
GRHPESDIFLDDVTVSRRHAEFRITEGSFEVVDVGSLNGTYVNREPRNSQVLSTGDEVQIGKFRLVFLAG
P
>gnl|CDD|469543 NF041661, Cycl_ph_dihydrol, phosphoribosyl 1,2-cyclic phosphate 1,2-diphosphodiesterase
DLHVHTTMSDGSDTFEEVLEQARQRGIGRVAFTNHDTTRGLDEAAELGERLGVQVTGGIEVSAYDFERNR
KVHVLGLGLREGAPALAALCGPLLERRNANSLWQLDRLVEAGYPVDVERALALGRASTCLYKQHLMAALT
SEPYVSAAYRTLYRSLFKNGGICDRDIAYVDARDAVRAIAEDGGLPVLAHPGQLDSYDLVPELVECGLGG
IERFHPDHTPADHARCAQLAERYGLVCTGGSDYHGRFGSIPHVGFRVPA
>gnl|CDD|469544 NF041662, ampC_Kaer, CMY2-MIR-ACT-EC family cephalosporin-hydrolyzing class C beta-lactamase. This narrowly defined subfamily of AmpC class C beta-lactamases covers chromosomal ly encoded proteins apparently restricted to and universal in Klebsiella (previously Enterobacter) aerogenes. Strains encoding this enzyme tend to be resistant to penicillins and first and second generation cephalosporins
MMKKSLTGVLLLGASFSTFAAPQTAEQLRELVNQTITPLMKEQAIPGMAVAVIYHGKPYYFTWGQADVAG
QRPVTRQTLFELGSVSKTFTGVLGGDAVARGEIKLSDPAQKYWPQLTGQQWQGISLLHLATYTAGGLPLQ
VPDEVTDEAALLRYYQNWQPQWAPGSKRLYANASIGLFGALAVKPSGMSFEQAMSQRVLQPLKLSHTWIN
VPPAQSKDYAWGYRDGKAVHVSPGQLDAEAYGVKSSIEDMAHWVLANMNREAVQDKNLRQGIQLAQSRYW
RAGEMYQGLGWEMLNWPVSAEVLINGSDNKVALAATPVTAVNPPAPPVKASWVHKTGSTGGFGSYVAFIP
QQDLGIVMLANKSYPNPERVKAAYHILEALQ
>gnl|CDD|469545 NF041663, ampC_Sliq, cephalosporin-hydrolyzing class C beta-lactamase
MTKINRLAAALFAALILPAGHAADKADIDAIIQPLMQKYAVPGMAIAVSVEGKQQFYHYGVASRQTGKPI
TNQTLFEIGSLSKTFTATLATYAVSEGKMSFADPASRYLPALRGSAFDHVTLLNLATHTSGLPLFVPDDV
TNDAQLMAYYRQWQPPHAVGSYRVYSNLGIGMLGMITAKSLNQPFTQAMEKQLLPALGMNHTYIKVPAEE
MANYAQGYNKKDQPVRVTPGPLDAEAYGIKSNAQDLIRYLDANMQVVKVGDPWRKALAATHTGYYRTGVF
TQDLMWESYAYPEKLATLTEGNNAGMIMNGAPATAITPPKQDQGAAWYNKTGSTGGFSTYAVFIPSQKIA
VVMLANKWFPNDDRVAATYRIVQALDKR
>gnl|CDD|469546 NF041664, RNAP_arch_Epp, archaeal transcription elongation factor subunit Spt4. Spt4, an archaeal zinc-binding protein, averaging about 64 amino acids in length, forms a heterodimer with Spt5. The Spt4/5 heterodimer is now considered a transcription elongation factor, responsible for making the archaeal DNA-directed RNA polymerase (RNAP) processive. Previously, Spt4 was treated as a part of the RNAP itself and was designated subnit E''
KACRNCKRLVEEEVCPVCGSTDLSEDWSGLVIILDPEKSEIAKKLGITKPGKYALKV
>gnl|CDD|469547 NF041665, blaPSZ, PSZ family class C beta-lactamase
MKLISQTLIATALTSACSMAFAATPDVDAIVDQAIKPLMQQQAIPGMAVAVVVKGQPHYFTWGMADEKQQ
RPVTQDTLFELGSVSKTFTGVLSGVAVNKGEIALSDPASKYWPALNTPQWRDITLLQLATYTAGGLPLQV
PDAVTDEKALANFYQQWQPQWAPGNTRQYANSSIGLFGWLATKPSGLTFEQAMQQRVFTPLQLKHTFITV
PDTAKNAYAWGYREGKPVRVSPGMLDAEAYGVKSSIKDMARWMQANMDPQQVKDKTLQQALDFAQTRFYR
TDALYQGLGWEMLDWPAQAEMAVKGADNKVALGPQPVRDAKAHPRVTASWVHKTGATGGFGAYVAFIPEK
QVGIVILANKNYPNTERVKAAMQILKALQ
>gnl|CDD|469548 NF041666, ampC_Ecan, CMY2-MIR-ACT-EC family cephalosporin-hydrolyzing class C beta-lactamase. This HMM identifies a small subset of chromosomal class C beta-lactamases (AmpC) typical of Enterobacter cancerogenus
MKKKLVFCALLLGVSCSALASSLSEKELAKVVKRTVTPLMKAQSIPGMAVAVIYQGQPHYFTFGKADVAA
NIPVTPQTLFELGSVSKTFTGVLGGDAIARGEISLNDPVTRYWPELTGKQWQGIRLLDLATYTAGGLPLQ
VPDNVTDPAALLNFYQTWQPQWKPGTTRLYANSSIGLFGALAVKPSGMGFEQAMTTRVLKPLKLDHTWIQ
IPKSEEQHYAWGYRDGKAVHVSPGMLDGEAYGVKSNAEDMASWVMVNMALERVQATSLKQGIALAQSRYW
RVGSMYQGLGWEMLNWPVDGKTIIDGSDNKIALAALPAREVNPPAPPVKASWVHKTGSTGGFGSYVAFIP
EKQLGIVMLANKSYPNPARVEAAYQILNALQ
>gnl|CDD|469549 NF041667, GvpU, gas vesicle accessory protein GvpU
DSILEFFVKAANKHDFSLDITLNVNGALVTGTLISAKEYFEELSESFEDGNDVAQKISEQLSKASESAES
GDEEEANFIHLKNAKVYCGDSKPTPSKGKILWRGKLDEVDGFFLGKI
>gnl|CDD|469550 NF041668, trim_DfrL, trimethoprim-resistant dihydrofolate reductase DfrL
MGENIAEDCCGEIGKPGDLFVNAEDDMGHFGNSGDDDVNLMGDKKHEKIPTMDDKNRIGIKLTENIPVRA
DGAIICHSKEDNKNYLADGAIECHIHEDGGISAFEMFIDEPIHLHGGIIAEEFEGDEVMIEHDTIIDECF
DGADGMPDEDNKYFHCFDIADGKKDEDLKDPGGFLE
>gnl|CDD|469551 NF041669, GvpT, GvpT/GvpP family gas vesicle accessory protein
PIKRTIAGGIVGATVGYLATPENGKKLLARIDQEELKSKGKDLGKAAKEKSKQAAGSLKSSTANLFKKDK
DSEEEEDEENETEDEEEEETEEEDSEDYEELKEENKQLQDRLQKLEEKLNKL
>gnl|CDD|469552 NF041670, GvpQ, gas vesicle protein GvpQ
KKAAGKAAKKAIEKAPEPVKEKVKDEVKEKAKEKFEEKFKEGIQSKANEASEKLEEAKEENAEKVHEKAE
EAKEKVQDVLLSVREKLGKVKEAGEEFQEKISSSSKDDKDKIKGVNDIKGVSDIKSSSDIKSSTDIK
>gnl|CDD|469553 NF041671, peri_hyde_PaoC, aldehyde oxidoreductase molybdenum-binding subunit PaoC. PaoC is the molybdopterin-cytosine-dinucleotide cofactor-binding subunit of the periplasmic aldehyde oxidoreductase PaoABC. The enzyme is known formally as carboxylate reductase (EC 1.2.99.6)
MKFDTPAGTNPIDQLKVVGKPTDRIDGPLKTTGTAPYAYERHDVAPNAAYGYIVGAAIAKGRITSIDLAA
ARAAPGVLAVVTALNAGKLGKGKFNTAKLLGGPEIEHYHQAVAVVVAETFEQARAAAALVRVDYAREPGA
FDLAAAKDSAPLPPGDPGGPPDTRVGDFEGAFAAAPVKLDATYTTPDQSHAMMEPHASIAAWEGDKLTLW
TSNQMINWGRGDLAKTLGIPKENVRLISPYIGGGFGGKLFLRADAVLAALGARAAGRPVKVALPRPLIFN
NTTHRPATIQRIRIGATRDGKITAIAHESWSGNLPGGRPETAVQQTRLLYAGANRMTAMRLAVLDLPEGN
AMRAPGEAPGLMALEIAMDEMAEKLGMDPVEFRILNDTQVDPEKPERPFSQRQLVECLRTGAERFGWSRR
NAKPGQVREGRWLIGMGVAAAFRNNLLMKSGARVRLDRDGRVTVETDMTDIGTGSYTIIAQTAAEMMGVP
LDRVVVRLGDSSFPVSAGSGGQWGANSSTAGVYAACVKLREAVAQRLGFNSADAEFADGQVRAGNRSVPL
ADAAAGGELVAEDTIEFGDLAKKYQQSTFGAHFVEVGVDAATGETRVRRMLAVCAAGRILNPKTARSQVI
GAMTMGVGAALMEELAVDKRRGFFVNHDLAGYEVPVHADIPHQEVIFLDETDPVSSPMKAKGVGELGLCG
VAAAIANAVYNATGVRVRDYPITLDKLLDRLPEVA
>gnl|CDD|469554 NF041672, ADPriboarghdlase, ADP-ribosylarginine hydrolase Tri1
MIDLHSDDETLNDYAERYAHLLPPASRQLQQRMDYLSVDDAPWLSGAELPAWLESRPCTLSEEQALDRAK
GALVGLAVGDAVGTTLEFLPRDKAHVSDMVGGGPFRLKPGEWTDDTSMALCLAETYLEKGRLDITLFRNR
LVRWYRNGENSSNGRCFDIGNTTRYALEQYLKHGPSWFGNTEPNTAGNAAIIRLAPVAIFRRHSLLATWR
DSQAQSRATHCAVESLDSCQLLGLILHYLLNGADKEEAFSPHVMPLNPRVLIINAGEYKQKTRDQIRSSG
YVIDTLEAALWAVWNTDNFRDAILLAANLADDADSVAATAGQIAGALYGYSGIPQEWVDKLAQHERIATL
AEQLFDRAPE
>gnl|CDD|469555 NF041673, transregRamA, acetate metabolism transcriptional regulator RamA
MDQQRIKDDDDAIRSALTSLKNATGIPVTMYGAVLPDGRLQITQWVGLRTPALQNLVIEPGAGVGGRVVA
TRRPVGVSDYTRAKVISHEYDRAIQDEGLHSIVAVPVIVGRDIRGVLYVGVHSPVRLGDKVLEEVTMTAR
TLEQDLAVNDALRRSDAGDRRGAKSGRRMNGAEWEQVRATHSKLRMLANRVEDEELRRELEVLCDQMVSP
VRVKQTTKLSARELDVLACVALGHTNVEAAEEMGIGAETVKSYLRSVMRKLGAHTRYEAVNAARRIGALP
>gnl|CDD|469556 NF041674, RNA-bind_Rsr, RNA-binding protein Rsr
MKNLLNAINPLNRTQTERLDARQVRNNAGGFVYAVSDEARLTRFLVLGTDGGTFYASERAHTVQATDFVR
EFVQRDAARALRVTLDVVRRNRAPKADPALLVLALIAKTAPDLEDRKAAWNALPEVARTGTMLLHFLAFA
DALGGWGRLTRRGVANVYETAPVEKLALWAVKYKARDGWSQADALRLAHPKTDDAARNAVLKFMVDGVLP
DASDPALRVIEGHLLALQATSDADAAALMREYGLPIEAVPTHLRGAEVYRAAMETNGLTWLLRNLGNLGR
VGVLSVNDREVIRAVVARLTDPAALRRGRIHPLDVLKARLVYAQGRGVRGGGEWLPVPRVVDALEDAFYL
AFGNVQPAGTRHLLGLDVSGSMTCGLVAGVPGLTPNMAAAAMSLVALRTEPDALTMGFADAFRPLGITPR
DTLDAAMRKAQSASFGATDCALPMLWAAQNKVEVDTFVVYTDNETWAGKVHPTVALDQYRQKMGIAARLI
VVGLTATRFSIADPNRADMLDVVGFDSAAPGVMTAFARGEL
>gnl|CDD|469557 NF041675, sarc_dimgly_mtase, sarcosine/dimethylglycine N-methyltransferase
MSQYDDQAIETARQYYNSEDADNFYFHIWGGEDLHVGIYNDDEEPIFDASRRTVERMASKLRQLGPDSYV
LDVGAGYGGSARYLAHTYGCRVVALNLSERENERDRQMNKEQGVDHLIEVVDGAFEDIPYDDGTFDLVWS
QDSFLHSGDRERVMSEASRVLKSGGEFIFTDPMQADDCPEGVIQPILDRIHLETMGTPNFYRQELRKNGM
TELEFEDNTHQLPRHYGRVHKELERREGELDGHVSAEYIERMKKGLQHWVEGGNKGYLTWGIFHFRKG
>gnl|CDD|222768 PHA00002, A, DNA replication initiation protein gpA
SECHSDYFDKPAIEAIKPLVETAGMSVLAQSPNLRIWKQVDNRIKLLEEILYHYTNGIRRDNGDFWMNGH
LPQRAPEELHLDDEIGEDYRSTTLSLIDEMAECYKVLGQLDINNTIDHRPPGDAEWVLLYEKTVYKHWYK
LVAQRPLKLIRDEYNYAKAKGFKDECSKILEESTMKSRRGFTVQRLMNAMRTAHQKGWFVVFDTLTLADD
RLKAFYDNPNALRDYFRDIGRMVLTAEGRSVHDSSSDCYQYFCVPEYGTQHGRLHFHAVHLMRTLPLGSL
DPNFGRLVRNNRQINSLQNTWPYGYSMPIAVRYSQDAFSRAGWLWPVDKKGEPLKSTSYMAVGFYVAKYV
NKKSDQDQAAKGLGNKKWNNSLKTKMALLPKKEFRIRMSRNFGMKLLSMAHLSAEVLIELTQVGYDVTPF
NQILKQNAKKELRLRLGKLSVADVLEAQPVTTNLLKFMRNLTKKIGESNLQSFIASMTVKLTNGDISDET
KNYVIDAGITPADLRIKSKWTAGGK
>gnl|CDD|222769 PHA00003, B, internal scaffolding protein
MEQMTENQNGNLSQERISNQNQSQLRNEAAVNGSSVQGVANGTDPSGLRRDPVQQDLEAERQKRADIEAG
KAICARRFGGATCDDKSAKIYAQFDPNDRRVQPAEFYRFNDGEINKYGYF
>gnl|CDD|164773 PHA00006, D, external scaffolding protein
SMNNESDVNFATAVASIKLIQASAVLDLTEDDFDFLTGDKVWIATDRSRARRCVEACVYGTLDFVGYPRF
PAPVEFIAAVIAYYVHPVNIQTACLIMEGAEFTENIINGVERPVKAAELFAFTLRVRAGNKETVTDAEEN
ARQKLRAQGVM
>gnl|CDD|164774 PHA00007, E, cell lysis protein
MEHWTLSDTLAFLLLLSLLLPSLLIMFIPSTFKQHVSLWKALSLPKTLLMASSVRLKPLNSSRLPCVYAP
ETKKLLLTQKQTSVNNYALKE
>gnl|CDD|222770 PHA00008, J, DNA packaging protein
RKKSARRSPSRRKGARLWYVGGTQF
>gnl|CDD|164775 PHA00009, F, capsid protein
MSNVQTSAERIPHDLSHLVFDAGKIGRLKTISWTPVIAGDSFELDMVGAIRLSPLRRGLAVDSRVDIFTF
YIPHRHVYGQQWIQFMKDGVNATPLPPVTCSSGWDSAAYLGTIPSSNLKVPKFLHQGYLNIYNNYFKAPW
MPDLTYANPSNMPEDDYRYGVRCCNLKSIWTAPLPPETKTSEQMTTETNSIDIMGLQAAYAQLHTEQERD
YFMTRYRDIISSFGGSTSYDADNRPLLVMRSEFWASGYDVDGTDQSSLGQFSGRVQQTFKHSVPRFFVPE
HGVMMTLALVRFPPTHEMEMHYLVGKENLTYTDLACDPALMANLPPREISMKDLFHSGRSSAKFKIAEGQ
WYRTQPDRVAFPYNALDGFPFYSALPSTDLQERVLVRTDNYDECFQSMQLAHWNMQTKFNVTVYRHMPTT
RDSIMTS
>gnl|CDD|164776 PHA00010, G, major spike protein
MFQKFISKHNAPITSSRLAATGVTPAANAPVLNTPELGRSTTLLFASLTATSTHGGFAHVIRVDTSNPTD
NQVFSVAASLSFDVDSKYIACLVRFESADGQVPTALPALYDVYPIESFGSGGAYSVKDCVTIDVHPRTSG
NNVYVGVMLWSAAWTAGKVSGVVSLNQVNREVTVLQPLK
>gnl|CDD|222771 PHA00012, I, assembly protein
MAVYVVTGKLGAGKTLVAVSRIQDKLVKGCIVATNLNLRLHHLPQVGRFAKQPRVMRIPDKPTLEDLEAI
GRGNLSYDESKNGLLVLDECGTWFNSRSWNDKERQPVIDWFLHARKLGWDIIFIIQDISIMDKQAREALA
EHVVYCRRLDKITIPFIGTLYSVLTGGKLPLPKVHVGIVKYGDSPQSLTVDKWMYTGTDLYAAYDTKQIF
SSDYESGPYSYLTPYYSHGRYAVKRDAKYYMRLTKIYFKKYSRVLCLALGLGFGAAFFYKSQPKPEQLQL
VQAQSQQLSTSKTDKLSELLPRLTINSYTRMGYAVVVFFKDAKAKIINSDDLQKDGYRLDYIDRCHVTIK
KGNYNEQVTCE
>gnl|CDD|222772 PHA00019, IV, phage assembly protein
MIKSIFAKMLLFLLMFLSFSSFALPVELNNSPIREFVSWYSQQTGKSVVLGPDVKGNVTVYSADVNPANL
PQFFDSVLRANGFDLVAGGPAVVIKQNPNQEDYADDLRDSRDDVFYDNSVPSGAPEVPNDLIVRTFNINN
VRASDLLPLVKIFVKSNGAPGGSVTDLPGTNSLVVSGSASQLPALADFISAIDVPRRQVLIEALIFETSL
GDGVDLSFAAGLASGGKVAGGFNTARLTTVLSSAGGSFGIFNGNVLGLSVKALENSSNSRVLSRPRILTL
SGQSGYISVGQNVPFVTGRVTGEAANVNNPFQTIERKDVGVSLEVTPVVMGDGQLVLDIDTKADSLSDST
IASDIITNQRSLQTTVQVKDGQTLLLGGLISSNNTDGDSSVPFLSKIPLIGWLFRSKSDSNEQRTLYVLL
TARVIKAL
>gnl|CDD|164777 PHA00022, VII, minor coat protein
DFDTIYQVVIALGLVICFGLGAITGGQR
>gnl|CDD|106880 PHA00024, IX, minor coat protein
MMSYLGYFFGAYILGWALFYGILVFKKLSERIS
>gnl|CDD|222773 PHA00025, VIII, major coat protein
MKKSKVKKASGAVTLLVSAGSFAAEPNAATSYATEAMDSLKTQATDLIGQTWPVVTTVVVAGLGIRLFKK
FSSKAV
>gnl|CDD|133846 PHA00026, cp, coat protein
AANFRQFVLVDNGGTGDVTVAPSNFANGVAEWISNNSRSQAYKVTASVRASGADKRKYAIKLEVPKIATQ
TVGGVELPGAAWKAYANIDLTIPIFAANDDCELISKALAGLFKDGNPIAEAIAANSGFY
>gnl|CDD|133847 PHA00027, lys, lysis protein
MGLKAKHEDNLCRDQERSKRLYVLIALAIFLSDFTNIFLHSILEALILTLQTLMDLLT
>gnl|CDD|222774 PHA00028, rep, RNA replicase, beta subunit
MTKTDQIRRTLCIDYERDLSLSIANDLPSIQRGSSDPLSPDFFADEYLRAEILSKFPSFSLGEDAASRRA
VAIAKFLEAEQRCGQTNQRGYLYSYGEEFFFSELLRTARRLIGKLLGDFVYDVFTECRFSGGASTTSSRL
HGAPFKKFAGQAEVTARALPYLVAYRRGCAAWARKHIELMEMGVFRVVPGNRVFTVPKNNKTDRAIAKEP
DLNMFLQKGVGGFIRRRLRLAGIDLNDQSRNQELARLGSVDGSLATIDLSSASDSISLKLVWLLLPPHWY
SVLTDLRSSYGMLDGRLIEWEKFSSMGNGFTFELESLIFAAIARSFCLLFGGPGTISVYGDDIIVPTEVA
PPLINVLSYVGFMPNLKKTFWTGPFRESCGAHYFAGVDVTPFYIKRPLDNLPDLILILNSLRRWGTVTGI
SDPRLYPLYNKYRDLIPKTLVLPGGYDLGADTYLVSPDTYVDNYKKKRRKPDLADTKKDRVRDERIAYLY
ALFSHKEELCDDNGRYVVWLRDGTEAGVSHRARHTGLPDLSKRYRLRWIRSSSRVWGPYGDVPHFPQELG
S
>gnl|CDD|222775 PHA00080, PHA00080, DksA-like zinc finger domain containing protein
ADIIDRAAEIEELQRERALANRRNKYQAPSATHCEECGDPIPEARREAVPGCRTCVSCQEILELKSYQRG
AK
>gnl|CDD|106886 PHA00094, VI, minor coat protein
MPVLLGIPALARFLGTLAANLIGYFAKFFTRGIARNALAISLFIGLILGLNSALVALLSDLASILPPDFV
DAVSMVVPSNAIPCVYAIFSAKAAVFVFDVKDRILGYLDWQK
>gnl|CDD|164779 PHA00097, K, protein K
MKPKTTLILQELLLLTYELNRSGLLVENEEIQSQLKKLEKLLLCNLSPSSQRSGKN
>gnl|CDD|222776 PHA00098, PHA00098, hypothetical protein
MANILGIVIKTFPKRGTTIAELNVLRPVETVNVEKFAQYGLGLNTDIPFNKQPLRIEPTYAKRLIETRAF
VPNREYQLRFEINPEDPLAAIVTELIPVDDDIKKHFEASLKK
>gnl|CDD|164781 PHA00099, PHA00099, minor capsid protein
FKSIYSEKKSVKLKFTQKSLTQQHNKDECDINNIVKKLNATGVLEHVERRQPRYGDCMSPMDYQEALNVV
IEAQEAFDSLPAKIRERFGNDPEEMLDFLSDPENYDEAKALGLVYEDGPSGAPQTFFEAQPKDDQNVSNE
EPGLAQK
>gnl|CDD|177266 PHA00101, PHA00101, internal virion protein B
MCWMAAIPIAMMGAQAIMGANQQAKAEGAQIDAGRRQAMEMVKEMNIQNANLSLEARDKLEEASAELTEA
NMQKVRNMGTIRAAIGEGMLEGNSMDRIKRVTEGDFIREANGITENYRRDYASIFAQQLANTENTKSQIK
EIYKSEPKKKSKLEQVLDPLSLGMGGYAASAYASGAFDSKGTKKAPISAAKGTK
>gnl|CDD|222777 PHA00144, PHA00144, major head protein
VKQSLGITSNIDILNAIRNSASDDYQTYVPLATAANIAEVGAGILDDQTVQNEFITALVNRIGSTVIKAL
SLENPLAIFKKGTLEFGDTIEEIYTDITKEKTYDAEEAEQKVFKRAIPNVKTLFHTRNRQNFYKQTIQRD
SLKTAFVSDGNFDEFLSSIITSIYSSDEVDEYEYMKLLIDNYYSKGLFKTVKISDPITSTGAKDFVTEFL
KKLRATAKKMTLPQGTRDFNSMGVHTRTDIEDLYLIIDAEFSAELDVDVLAKAFNMDKADFLGRVIVVDG
FASTGLKPVAVLVSKDFFMVKDKLVKMETIRNPRGLYWNYYYHHWQVLSASRFANAVAFVTGDNTIVVTQ
VIVSPEIASLKQGKSQGFTAYIRAPDNKGHAVVWYVEGGSTGTSISNDGVLTIGANEPNQLTVKVTVDIG
TADGNKPVVGEAVISVRP
>gnl|CDD|133855 PHA00147, PHA00147, upper collar protein
MAYKRNNSYKSINEIQRSRGNRWFHHYRRYLMSLAYQLFEWEGLPNTIDPSFLEKSIHQNGYVAFYKDPM
FGYIACQGTLSGQLDHYNQPTGYRASSPGYQNYFKLYNYEDLKEKDMGVVIYNNDVREPTIDLLELFAAR
LAELKETIEVNQNAQKTPVIIAANDNNQLSMKNIYNKYEGNEPVIFAHENLDMDNIEVFKTDAPYVADKL
NAQKNAVWNEAMTFLGIKNANSEKKERMVVSEVSSNNGQIEASGEVFLKPRQEACELINELYGLNISVKF
RYDIVEQMRLYLQELENASRGGSGGGNN
>gnl|CDD|222778 PHA00148, PHA00148, lower collar protein
MSSYTMKLREYVEMWTQFDDGLSQAEKIEKGRPKLFDFNYPIFDESYRKEFETHFIKHFYNREIGFETIG
RFKFALEEWLDLNMPYFNKLFESELIKYDPLENTRIDDFSDTKSSRTGQDTRSKGSGNEHQGGSGSGTND
NFKRQINSDTPDGRLLIVTHDGKGVLEYATSIVEANTNGSSDTKTKNTSSSTSNSTGNQTSESWGKSGSQ
SYARLIMEYRAALLNIDDRIFNEMQELFMLVY
>gnl|CDD|222779 PHA00149, PHA00149, DNA encapsidation protein
MDKKLYYNPQKMLSYDRILNFVIGARGIGKTYALKKYLIKRFIKKGEQFIYLRRYKSELKKKSKFFADIA
QEFPNTEFEVKGRKIYIKGKLIGYAIPLSTWQALKSSAYPNVSTIFFDEFIREKDNKRYLPNEVDALLNL
IDTVFRARERVRCICLSNAVSIVNPYFLYFGLYPDINKRFNVYDEILIEFPNSEDFQSERRKTRFGKLIS
GTAYYEMSLDNKFSSNSDLFVEKRSKNSKFVFSIRYNGNYYTVWVDLTQMLVYIATAHDPSTKRVYALTV
DDLEEGMVLLINYKKNYLLRKLRSLFKKGMLRFDDQVTRNIFIEIFKKMRI
>gnl|CDD|177267 PHA00159, PHA00159, endonuclease I
AAGYAARGIAKVGAFRSGLEDKVSKQLEKKGVKFDYELWKIPYVIPASDHKYTPDFLLPNGIIIETKGLW
DSDDRKKHLLIREQYPELDIRFVFSSSRTKLYKGSPTSYAEWCEKHGILFADKLIPVDWLKEPKKEVPFD
KLKTKKGG
>gnl|CDD|222780 PHA00198, PHA00198, nonstructural protein
MHMKVFSIFDIKTEIYGQPFFMQATGAAIRAFSDMVNDDPSKNQFAAHPEDFDLYEIGSYDDSTGTFIPL
DVPKALGTGLDFKHKQ
>gnl|CDD|177268 PHA00201, PHA00201, major capsid protein
MANMTGGQQIGTNQGKGQSAGDKLALFLKVFGGEVLTAFARTSVTMNRHMVRSIQSGKSAQFPVLGRTKA
AYLAPGENLDDKRKDIKHTEKVITIDGLLTADVLIYDIEDAMNHYDVRSEYTAQLGESLAMAADGAVLAE
MAGLCNLPSASNENIAGLGKATVLEVGKKADLTDPVKLGKAIIAQLTIARAALTKNYVPAADRTFYTTPD
NYSAILAALMPNAANYAALIDPETGSIRNVMGFEVVEVPHLTAGGAGDTREDEPTGQKHAFPATASGDVK
VALDNVVGLFQHRSAVGTVKLKDLALERARRANFQADQIIAKYAMGHGGLRPEAAGALVFTKA
>gnl|CDD|164786 PHA00202, PHA00202, DNA replication initiation protein
SPTRPLNNVSTWGCLMTMATNILKSFDEQSVHIDYLCFTFAVKDLRHCHKAVRRLHKNEEYKGFAKSGTL
QRHCVFNPTVCSTSDEIDAYNKAFDICYRNYLEDCLRIFTNQVLGLSLSPMRGRGLHGYNDSMVITSMTG
QVECGLVGIGGNNDTVFFQINGTGCKHVFARRPTWSLHDWLTNVLGITRLVRLDLAVDDYTGNFDAKYAE
KCFYEGAFRTAPRGQGPSMVPHKRITSIGALMEEATIVGSRSSAIYWRIYNKKLEQKITDPDLIWYRNEV
ELKKCDIELLANPAASFAGICPFAASIECTPPVKFSRNKKAQGLEFMARIAWVRRQCGVALAEVIAMTQG
DLGEAFGMLIPHKHRRPDFELLGVPDSYGQLKNTILET
>gnl|CDD|164787 PHA00212, PHA00212, putative transcription regulator
MEVLMEQVVTHYGETIQQHSVEWYKKQLLKDFSVQFIKDSLLPQLFEWSNAYKAAVELTNKKP
>gnl|CDD|222781 PHA00276, PHA00276, phage lambda Rz-like lysis protein
LEFLKRAAPWVLAAMLFGLGYHLGSDSANAKWKQEVQNEYVKKVEATADTQAAINAVSKEYQEDLAALEG
STDRVIADLRSDNKRLRVRLKPTSGEVQSDGRCLPDGRAELDERDAKRLIGITQRGDAWIKALQDTIREL
QRKK
>gnl|CDD|106901 PHA00280, PHA00280, putative NHN endonuclease
MRKSYKQFYKAPRRHIQVWEAANGPIPKGYYIDHIDGNPLNDALDNLRLALPKENSWNMKTPKSNTSGLK
GLSWSKEREMWRGTVTAEGKQHNFRSRDLLEVVAWIYRTRRELHGQFARFR
>gnl|CDD|164789 PHA00327, PHA00327, minor capsid protein
MNPELVTNTAGAAVSGVASGLGMLPGIASGVLGYLGAQKQNATAKQIARRQMAFQERMSNTAYQRAMEDM
KKAGLNPLLAFGKGGASSPSGAGWSPNNPVESGLNSALAVQRLTYERKRMQAELQNLREQNRLINFNSAV
REGYLAERDLYMRFAGVPVATEVLDRTSGLESSSAKAFKNLFSRKGR
>gnl|CDD|222782 PHA00330, PHA00330, putative replication initiation protein
MACIRPIVCFIDKANQLFFSKGVKSSKPWDKVRELNSFEQDQPEEYRQRWVPMPCRKCSFCRLQNAKEWA
VRAMHEASSYSQNCFLTLTYDDEHLPENGSLVRDHIRLFIKRLREYIDRHYPHKIKYLGCGEYGDKLQRP
HYHLLIFNYDPDDEKKLLSKKRGNQLYTSEKLMRLWPFGFSTVGSVTRQSAGYVARYSLKKVNGDIDQDH
YGQRLPEKSLKPGIGLDWFEKYKRQVYKQDYVVLQDKGKGFRTRPPRYYDDLHSEFDPEYMNELRQKVVE
KYMALPELTSDKAEVDQFILNDRTKRLFRDLKEESY
>gnl|CDD|222783 PHA00350, PHA00350, putative assembly protein
MMIYAIVGRPGSYKSYEAVVYHIIPALKDGRKVITNIPGLNLDVFEKVFGEFPSTARLIRIVDRNLEGFE
SMNRPFSWRPRGALYVIDEAQMIFPKRLGFKMANIFKRPFTDFEPHLPEGPENFLEAFMRHRHYNWDIIL
LTPNIRKIHSDIRAMIEMTYYHKKNTAIGSKKRYEHYTKKVVIGPAKEDVVIEQRIYKDHYFLYYSTHTG
SAGQVGEAKALDINPKWKSLVALLLGILSFGYYFYALSGKVSDSVKTPAEHQAQTPSGVPTVSGPARPAQ
TGKPAPVLGPLGDGCTGSGCGNEPYHDFSLYVSGHAKQIAYKKLTFYHVYIEAYTPRGFSFSLDDIDLEK
MGYQFEALDDCVYRLTWESNSRVVTCIPRSRFAQQKAQTPPDHVPGLLF
>gnl|CDD|177271 PHA00360, II, replication initiation protein
MIDMLVLRIPFIDSLVCERLDSGGDLIAFVDLAEIARLSGLNLAAHTVEYAIDGDLTVSGLKHPFESLPS
HYAGIAFKIFEGGKNFEPCVEIKASPAKLLQGHNVFGPTDFALCGEAFFGAFAAALPCLYDLCDVNATTI
GRIDATFSAKAANDHIAKQVIDFLRNVSNGQTKKTRALDWESTVMWNEGSRHRTLVAYLKHHELQAQIKQ
LQKKKSAHLTIYEKECLEVLSNPDLLEFASGLVRFEARIHTRFFENFGLPLKFFDAIKFADDYESGGFDL
ICDLWKFSFKDLFDAFEGDDMNIYDDSAVLDAIINKFFSITKSGKISFAKANRLFGFYRRLVNEGYDNVA
LTMERNSFWRSLKALTECGIPKAQLMNLSTCNNVVPLVQFINVDFSQQRPDWYNEPVSIFNRSNVVSIKA
A
>gnl|CDD|222784 PHA00363, PHA00363, major capsid protein
MVRNRRLPSVMSHSFAQVPSARIQRSSFDRSCGLKTTFDAGYLIPIFCDEVLPGDTFSLKEAFLARMATP
IFPLMDNLRLDTQYFFVPLRLLWSNFEKFCGEQDNPDDSTDFLTPVLTAPSGGFAEGSIHDYFGLPTKVA
GIRCVALWHRAYNLIWNQYYRDENLQESVAVQMGDTTSDEVNNYKLLKRGKRYDYFTSCLPWPQKGPAVT
IGVGGIAPVTGLYGDVSSNNPIPAFVWDNSVNPTWFNSGGPTPTGTLGIVPVGQAYYIKKPGNDPTAQAA
NGEPATDSTPRLYADLGSTSPVTINSLREAFQLQKLYERDARGGTRYVEIIRSHFNVQSPDARLQRAEYL
GGSSTPVNISPVPQTSSTDSTSPQGNLAAYGTAIGSKRVFTKSFTEHGVILGLASVRADLTYQQGLDRMW
SRRTRWDFYWPALSHLGEQAVLNKEIYCQGPAVKDAGGVVVDEQVFGYQERFAEYRYKPSKITGKFRSNA
TGSLDSWHLAQEFENLPTLSPEFIEENPPMDRVLAVKTEPDFLLDFWFSLRCARPMPVYSVPGLIDH
>gnl|CDD|222785 PHA00368, PHA00368, internal virion protein D
DKYDKNKPSEYDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQFTKATAKALGLIVDDD
DRLDPELAIDAGARYLADLVGKYDGDELKAALAYNQGEGRLGAPQLEAYDKGDFASISEEGRNYLRNLLD
VAKSPKSGDLESFGGITPKAKGIPAEAAFEGIGKKGKVGTELPESHGFSVEGKEQEAPNVPFAKDFWEAT
GETLDEANSRSTFFGFGDATEAELSNSVLGVAFRAGRRDDGFDVFKDVFTPTRWNSHIWTPEELEKIRTE
VKNPAYINVVTGGSPENLDELIKLANENFEYDARAAEAGLGAKLSAGIIGAGVDPLSYVPMAGVTGKGFK
LVNKALVVGAQSAALNVASEGLRTSVAGGEAHYAEAALGGALFGGGMSAISDAVAAGLRRSGETEVVNEF
AGPAMRLEARETARNAGGEDLSRMPPSNDRFLSDHNGVPYADLPTEPGAVVLRDGSILSDSNPLNPKTLK
EFAEVDPERAAKGIKLGGFTEIGLKTLRSENAEVRGIASDLVRSPTGMQSGSSGKFGATASDIKERLHST
DQRTYNDLYDAMEDAMKDPEFSTGGAKMSREAARQEIYRRVALAIERPELQANLTKAERKVMDILKEHFD
LKREMMENPAIFGNTKAVSIFPGSRHKGTYVPHVYDRAAKALYIQRLGGPDGLQEAIAKSWLTSYRSRPE
VKARVDEFLKELHGIDVKEVTPEMVEKYAMDKAYGISHTDQFTRSSVIEENIEGLVGIENNSFLEARNLF
DSDMSVTLPDGQTFSVNDLRDFDMKRIMPAYDRRVNGDIAIMGGTGKTTKELKDEILALDKKAEGDGKLK
GEVEALKDTVKILTGRARRNPDTAFETALRSLNDLSFFAKNAYMGAQNITEIAGMLAKGNVRALLHGIPI
LRDLAFRNKPVSASELKELHGMLFGKELDQLIRPSRQDIVQRLRETTDTGPAVANVVGTLKYATQELAAR
SPFTKLLNGTTNYILDAARQGVLGDVVSAALTGKKTKWFKERFLKSASISPEQWEGIKQLIREHVTRGAD
GKFTIKDKQAFASDPRAMDLWRLADKVADETMLRPHKVSLQDSKAFGALVKMVLQFKSFVIKSLNSKFIR
SFYEATKNNRAIDMALTHVISMGLAGGYYVAQAHVKAYGLPEEQRKEYLKNALDPTMIAYAALSRSSHLG
APLSIANMVAGPLGFDDAKMVRSTILPKGEKERDPNKAMTSRDVAGNIGGNLLEQVPALGFAGNVGATGY
NAAGVLTAPNKPTERDYMTGLMNTTRELVPNDPLSQQLLLKIYEANGIHIKERKK
>gnl|CDD|164794 PHA00369, H, minor spike protein
MFGAIAGGIASALAGGLMSKLFGGGQSAASTGIQGDVLANDNNVIGMDDAGIKSAIQGSNVPNGQQAAPS
AISGVMADAGKDLLDGTTQAGSDKVKQALMDKLGLGKDAKDKGKDTRDYLAAAFPELNPWERAGAGASSA
GMEDAGFNNQKELTKMQLDNQKEIAKMQNDTQKQIAGIQSATSRQNTKDSVYAQNEMLQYNQKESQARVA
SILENTDLTKQQQTSEIMRQMLTQAQTTGQHFTNDQIMELTRKVYAEIDKVHQDTQNSRYGSSQVGATAK
DVSNMITDAASGIVDWFRGIDKAVADQWNNFFKDGKSDGIPSNTR
>gnl|CDD|164795 PHA00370, III, attachment protein
MKKKIIAISLFLPFYTHEQTPEEICLAKPPIDGVFNNVWKGDEGGRYANYEGCEYEATGVTVCQNDGTVC
NGSWKPTGSADKDGDGGGTGEGGSDTGGDTGGGNTGGGSGGGDTGGSGGGGSDGGGSEGGSTGKSLTKEG
VGAGDFDYPKMANANKDALTEDNDQNALQKDADEQLDKASASVSDAISGFMRGVGGLVDNGGGESGQFAG
SNSEMDQLGEGDGSPLESFLNDGALRPSLPEGHGCTPFVFAQGKVYEFIIGCDKINDFKGVFAFVLYCLT
FWYVFQSFTSILRKGEQ
>gnl|CDD|222786 PHA00371, mat, maturation protein
DFEELYYPEKTTYSDGGLSVQLTGYPQTEPGSFSDIYRGKGVWFERTPYIVTDWVHPSPYWRGKTTVEYT
PYTFTLRWEGGVDKVPHPSADPGFELVSYTHNREVDLEDFLGSVPAPFTFDLENRASVRVLAKLSASNVN
LGVLIAEGRETLKYLALQLIRLVRAYRAARRGDLKRVRKALRPPKDRRFVSKDVAGRWLELRYGWLPLFS
DIKGAYEYLTRVHLKIFKPHRFSRGVGQTTKVSSRLDYPVYPHFSLAAGIVIQRRHRWRGVYESRASVRT
FINFNIEPPRLWKASRLGLLNPLEVAWELTPYSFVVDWFLNVGNMLEALTALYGVDFISGTQTRDITCEL
VGSVRPPSGWFARWKDFPLGSLSLVHSYYSTDRSVLSTFPQPLPYVKTPFSSVHLIDAIALIRQRLKR
>gnl|CDD|133872 PHA00380, PHA00380, tail protein
MAYVPLSGTDVRIMSGVPFSNDYKHTRWFTSKAEQYVYFNNKTRVHQEAEVVFTGSKENRPYVTVDVPID
DLYDANYFMFNNKSYMNKWFYAFVTKLEYVNSSVTRMYFEIDVIQTWMFDIKFQPSYIVREHQTEWQSNG
KPVVNTIDEGLDYGTEYDTVYVEHFKPYEDLMFLVIISKSEMHTTEEGEQFKAGQISASFNGAPQPLVYY
LHPFYRDGTGPKPVIGVNHFERSPVEDVLKNIFKQESAVNNIVNIYVTDYIGLPMSYSGGNKTVNLTDEM
FEQARIADDKHDNVPTIQLKFAPNYEFLKIDTGDKYDVFTKPTESKLLMYPYCVTIITDFKGNRVEYKLE
YINGSKLKIQVRGSLGVSNKVSYSVQDYNADSELSGDQNLTASIEASLINNNPNDIAIVNDYLSAYLQGN
KNSLENQKDSILFNGIMNMIGSGISAVGSAAAGSALGTASSATGMVSTAGNAVLQIQGMQAKQADIANMP
PQLVKMGGNTAFDYGNGYRGVYVIKKQIKPEYRSKLSGFFKKYGYKSNRVKIPNLRTRTAFNYVQTKDCN
IKGNINNEDLQDIRTIFDGGITLWHVDDVGNYNVTNEVR
>gnl|CDD|164796 PHA00404, PHA00404, hypothetical protein
MVTPIRPLSPSLRKRSSGRFRRWSSRVTSVMVCLVRYSVLCS
>gnl|CDD|222787 PHA00405, PHA00405, hypothetical protein
MGTPQSSGLRSIQGAVRRTCTMATVWPLCSVLSTMRTLRHSLGNQLTPCASTVMTCVNVSWNTVRLASRY
SSCSTRTSVTPRSTR
>gnl|CDD|164797 PHA00406, PHA00406, hypothetical protein
LRLLLTLLRHRVTYRFLLVLAAALGYASLTDHLGQLETLVCSILTCSD
>gnl|CDD|164798 PHA00407, PHA00407, phage lambda Rz1-like protein
MSTLRKLRLRRILRLRSMKYRLSTKKTLRRWKAALIGLLLICVATISGCASESNLPVEPQKVTVDASLMV
EPNLTKEMLSVLSQ
>gnl|CDD|222788 PHA00415, 25, baseplate wedge subunit
MMNINQLYSDIDPNFKKSPWNKDVSAVKGARAIKNSLLGIVTTRKGERPFDPNFGCDISDQLFENMDPLT
ADTIERNIESAIRNYEPRVYNLNVEVIPVYDDNSIIVTIYFSIIDNPDDLEQIKFQLSRSR
>gnl|CDD|133878 PHA00422, PHA00422, hypothetical protein
MSEYLKVLAAIKSCPKTFQSNYVRNNASLVAEAASRGHISCLSTDGRNAGAWEITASGVRFLKQMGGCV
>gnl|CDD|164800 PHA00425, PHA00425, DNA packaging protein, small subunit
MNDKSLIKFLEMLDTEMAQRMLADLKDDEKRTPQLYNAIGKLLDRHKFQISKLQPDENILGGLAAALEEY
KEKVGADGLTDDDVYTLQ
>gnl|CDD|164801 PHA00426, PHA00426, type II holin
MLELDFNNEVIKAAPIVGTAGADGAARLFFGLSLNEWFYVAAIAYTVVQIGAKVVDTIIDWKKANKE
>gnl|CDD|222789 PHA00428, PHA00428, tail tubular protein A
TLETMTELDAVNDILASIGESPVTSLDETNPDVANARRILEEINRQLQSEGWWFNTEEGATLTPDPFTGL
IPLPSDYLSVYPASSDSQYVNRGGYVYDRSTGTDRFGSPVTVRIVLLRPFDEMPECFRYYIVTKAARQFY
TRFFGADEIYQVLAQEEQEARRQVNEYELDQGNYNMLDGDSFTRGLIRRSLRT
>gnl|CDD|222790 PHA00430, PHA00430, tail fiber protein
MANTIKTVRTYPLDGSNVDFNIPFEYLARKFVVVTLIGVDRKELILNQDYRFATKTTISTTKAWGPADGY
TLIEIRRFTSATDRLVDFTDGSILRAYDLNISQIQTLHVAEEARDLTADTIGVNNDGHLDARGRRIVNLA
DAVDDGDAVPLGQIKTWNQSAWNARNEANRSRNEADRARNQAERFNNESGASATNTKQWRSEADGSNSEA
NRFKGYADSMTSSVEAAKGQAESSSKEANTAGDYATKAAASASAAHASEVNAANSATAAATSANRAKQQA
DRAKTEADKLGNMNGFAGAIEKVDGTNVYWKGGIKHANGRLYITSDTFACGGYQQTFGGDIQRREWTTAI
TSNIQHVVNGQIIQQGGTMTGALKGQGGIALQLERASDKAQYILSKDNNENNWYIGRGSDNGNDCTFRSY
LYGTHLTLRADYAVVNKRFHVGQAVFPTDGNLQGTKWGGNLDKWLGAYLNDRYVRKSSGWTQVWTASAGM
YLIGGGVSDTLSQDLRFRNIWIQSRNNLWNDFRVGPDGIYFLSAMGGWLKFQIHNNGRVFKNIRDRDAVP
EAILVENV
>gnl|CDD|222791 PHA00431, PHA00431, internal virion protein C
MASKLEQALGQMRAPGTERLRGGTGGMQYQAATVQAEVGQSNLLESLGKFAKAGADAYGAYDERRKDKAD
ERSNEIIRKLTPEQRREAIKNGTLLYQDDPYAMEALRFKTGRNAAYLVDDEVAQKIKNGEFRTRQEMEEY
RHSRLQESAKSYAEQFGINPTDEEYQRGFNSDITERNIALYGAHDNFLSDQAQKGAILNSRVELNGVLND
PDVLRSPESGEFFMNYIDNGLVTGSIPSDAQAEQVISQTLKDVIQRPGGANFLQQLEDRKVTLNGAETTY
KELMGEEQWNALMVKAQETQFQNDAKLTEQFRLGINSALNQEDPSTGWEQLQGLKAELDKLQPGEEMTPQ
RQWLIQAEEQMQDRMKRETAAQAKEMDKQQKTMNKQLVIDQQFQKRINGENVSTDYKDMPTNENTGEFTH
SDMVNYANKKLAEIDAMDIPDEQKDRMKLAYLRADSKKGAFRTAFGTLITDAGQEWTAAVINGKMPEDTP
ALNELRRARNADPSLIAALYPDQAELFLTMDMMDKQGIDPQVLIDADKQRQSLTKEMRFEDDKAWASLKN
DSKAPELARMPASLDNSARKIYDSVKYRTGNADMAMQQVAKYLKENTVTFTGDDVDGDTIGVLSKNSLMV
NDDPKSWEQGRDIIEEARKGLIEANPWVTNKQLTVYTQGGSIYLMDTTGQVRVRYDKELLSKMYQENQQK
LAEEAREKALKDANKRAPIVAATQAREEVREKRKQTSGFMYGDVSG
>gnl|CDD|177277 PHA00432, PHA00432, internal virion protein A
MYIRQTTERDFDVFNPSFEDILEAKAYGIEPSFPPDSECVTLSLDGFVLAIGGNQGDQVWFVTSDQVWRL
TKKEKREFRKLIMEYRDMMLDQYPSLWNYVWVGNKSHIRFLKSIGAVFHNEFTGDGCQFQLFTITKR
>gnl|CDD|222792 PHA00435, PHA00435, capsid assembly protein
MGESNADVYASFGVNSAVVTGSTPTEHEQNMLALDVAARDGDDAIELAEPETSDDPYGNPDPFGEDDEGR
IEVRISEDGEEEEVEEGEEDEEEEGEEESEEFEPLGDTPEELTEASEQLEEHEEGFQAMVEQAVERGLSA
ETITRIQAEYEEEGGLSEESYAELAAAGYSKAFVDSYIRGQEALVEQYVESVVEYAGGRERFQAIYSHLE
ATNPSAAESLEAAIENRDLATVKAIINLAGASRAKKFGKKPKRSVTKRAKPAKPVAPKVEGFASQAEMIK
AMSDPRYRRDAKYRAEVEQKVIASSF
>gnl|CDD|222793 PHA00437, PHA00437, tail assembly protein
MGLFKKIKKAVKKVTKSVSKPVVGAVAGALGGGKDAPPVVVAAAPPPAQIVEVPEKDDVETEDEAQTESG
KKKARAGGKKSLSVARSSGGGINI
>gnl|CDD|133887 PHA00438, PHA00438, hypothetical protein
MLTPIKHLLENPNDIPDVPRAAAEYLQVRFNASYLEQSGEIRLLRQAGYSEAFIAGFLAGLQYASRTLDE
MEARREQLRES
>gnl|CDD|222794 PHA00439, PHA00439, exonuclease
EGMSDKGVLVMDGDYLVFQAMAAAEVETDWGEDIWTLECDHAKARQILEDSIKSYKTRKKAWKDAPIVLA
FTDSVNWRKEVVPTYKANRKAKRKPVGYRKFLEELMAREEWKSILEPGLEGDDVMGIIGTNPSLFGFKKA
VLVSCDKDFKTIPNCDFLWCTTGNILTQTPETADRWHLFQTIKGDSTDGYSGIPGWGDTAEAFLENPYIF
EQVEKVLKSGKRKGQTVTKWKKRAPEPEETLWDCIVTLGAKAGMTEEDAIKQAQMARILRAEDYDFIDKE
PILWTP
>gnl|CDD|133889 PHA00440, PHA00440, host protein H-NS-interacting protein
MAMTKKFKVSFDVTAKMDSETEAILEEDILDLAKQAGAGEEVNPKDKELLVQALTHGPEGAAAFAVRQGI
REAIKDMHEESTDKDLFKFSPATVREVF
>gnl|CDD|222795 PHA00441, PHA00441, hypothetical protein
MCFSPKIKTPKVDTNQVRAPEPAPLTEEPKSVDFGGDDDEDTTEGTSTSGRKSLKVKKDDSPAKSKASDN
GKAKTGSKSSIRKSAFGGK
>gnl|CDD|222796 PHA00442, PHA00442, host recBCD nuclease inhibitor
MSMSRDLVTITRDAWNDMQGYIDSLEKDNEFLKALRACGVDNWDGYMDAVEMVAEEDDK
>gnl|CDD|177281 PHA00446, PHA00446, hypothetical protein
IKFVANTIRLSDTADQWARRVHINVRNGKVTMVYRWKDHKSSKAHTQRMTLDDEQAGRLLAALTVAATVA
VGDNKVRNVALGKGVKEII
>gnl|CDD|177282 PHA00447, PHA00447, lysozyme
KVQFKPRSSTKAIFVHCSATKPSMDVGVREIRQWHKEQGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKG
YNSNSVGVCLVGGIDDKGKFDANFTPAQMQSLKSLLVTLKAKYPGAEIKAHHDVAPKACPSFDLQRWLKK
NE
>gnl|CDD|133894 PHA00448, PHA00448, hypothetical protein
MFKFINTLGKLVVKLYFVEAKRLNDKARKDATRARRLAKQSRELSDAASAGVTEAARIAAKAQQLSKFFE
>gnl|CDD|164812 PHA00450, PHA00450, host dGTPase inhibitor
MGRLYSGNLNAFKAATARLFEHDVAVIVEEFYYENPAKMCMSLRVEDRSGHLIASRTFEHHDEDVLYNMQ
TEWLNKMYDQLKDWK
>gnl|CDD|177283 PHA00451, PHA00451, protein kinase
MNYTDIQARLAAIKNLPICELDKRQPLLVALAADIVNAETSDGNDTDGNWGLEHQDWWQTLGALMRDAGF
NLLGNGHFSAAYSHELLPGRVIKVGFKKEDSGAAYTAFCRMHQGRAGIPNVYHVARHAGCYTVVLDYLNP
CYRESNDVHHHYAAAAYIIIECCSDAAEEYPGSQEFIETCKMIRKFFYGIASFDMHSGNIMFDQDGVPYI
TDPVSFSHDREREPGFPLDPDELIAEVEAIANQRMIERCKNRKAKRDPNGTFQVARKAAMKRRKRNRKLR
ARNAKELAAMRMEANQIRRNEPRARMLMGDKHWHNAWLHNNNLDFAKLEERAALAWQMADGLAIQWGKPL
PIDKYLDARLMG
>gnl|CDD|222797 PHA00452, PHA00452, T3/T7-like RNA polymerase
YGEDLAAEQLQLEEEAYGEGEERFRKALERQLEAGEADDNPVARRLLATLLPPVAEAIDAWKEEYKKRGR
AAKARGLLRLVDPEVLAVITLKVTLDMLLSKETPTAQAVATAIGRAIEDEIRFGRIEDLNPKYFKKVVEY
LKRSRTGSVYHIAFMMVVEADMVLLGEWDPWPKEDYIHVGKWLLEALIESTGLVELVRHTGGNGGKDHEY
LELSEEAVELLQDIAAAAAGISPMYQPMVVPPKPWTSIVGGGYHTEGRRPLAPLVRKTKKALRRYRQKQM
PEVYKAVNALQNTAWRINKDVLAVVNEVVNWGPVGDVLGIPRRPLPPKPEFLDENEEAFKAWKRAAAAWY
TKEKERVSKRRRLEFMLRVANKFADYKAIYFPYNMDWRGRVYAVSMLNPQGSDLQKALLRFAEGKPLGKR
GLYWLKVHGANCYGVDKVTFDERAAWVDENHDNILAAAEDPLNNTWWAEADSPLCFLAACFEYAAAVHSG
TSYVSGLPVAMDGTCSGLQHFSAMLRDEVGGRAVNLLPSDKPQDIYGIVAEVVNEKLERDAINGTDNTRA
LARLWLAYGITRSLTKRPVMTLPYGSTRFSCRDYILEDLLQPGIDEGDGAMFTNQAASYMAKLIWDAISE
TVPAAVEAMNWLQQAAKLLAAKGAEALHWTTPTGFPVWQEYRKPEEKRVRLRLMGVARVQLYVNTDTIDA
RKHASGIAPNFVHSLDASHLRLTVVACAEKGIESFAVIHDSFGTHAADADNLHRAIRETFVEMYEENDVL
ADFADQFGDQLQLKMPELPEKGSLDLEEVLDSDFFFC
>gnl|CDD|164815 PHA00453, PHA00453, hypothetical protein
MRNFEKMTKRSNRNAHDFEATKGRKFNKPLRDRAHKRAWEG
>gnl|CDD|222798 PHA00454, PHA00454, ATP-dependent DNA ligase
MLNIKTNPFRAVDFNESAIEKALEKAGYLIADVKYDGVRGNIVVDNTADHGWLSREGKTIPALEHLNGFD
RRWAKLLNDDRCIFPDGFMLDGELMVKGVDFNTGSGLLRRKWKVLFELHLKKLHVVVYDVTPLDVLESGE
DYDVMSLLMYEHVRAMVPLLMEYFPEIDWFLSESYEVYDMESLQELYEKKRAEGHEGLVVKDPSLIYRRG
KKSGWWKMKPECEADGTIVGVVWGTPGLANEGKVIGFRVLLEDGRVVNATGISRALMEEFTANVKEHGED
YEAMPYNGRACQVSYMERTPDGSLRHPSFDRFRDL
>gnl|CDD|133900 PHA00455, PHA00455, hypothetical protein
MRLHFNKSNGIFSVRRNDRSTVKASEKHAKLPLIGDTVPLAPRVHALITRGKFEKATQKSRPFVPVVVTK
WPRVRLFVERIKEVF
>gnl|CDD|164817 PHA00456, PHA00456, hypothetical protein
MTMRKPSEWCEAKWEKTANDAYQELYNLWKRRGQ
>gnl|CDD|222799 PHA00457, PHA00457, inhibitor of host bacterial RNA polymerase
MSNLNKGSLVNGEKKFIATVEGSGQSFEVPVYAKSLEEATELAEWQYVPAGFVVTRIRPEVKV
>gnl|CDD|222800 PHA00458, PHA00458, single-stranded DNA-binding protein
MAFAKKKVFTTPIGTAEPYAYIAKPDFGNEGFFNPRGVYKVSLTVSNDDPRCQKMIDEIVKAHEENYAAA
LEEYEANPPKVQRGKKPLKPYEGDMPFFDNGDGTVTFKFKCYASYKDKKTGENKPIVLRVVDSKGKRIED
VPAIGGGSKLKVKFSLFPYKWNAAVGASVKLQLESVMLVELAEFGGGGEDDWADEDEEDGYVASEAKARK
PQDEEEWDEDDEEESEEDEDGDF
>gnl|CDD|222801 PHA00476, PHA00476, hypothetical protein
MKKVVLFLLLTYVVLVLCANYLILSLPLSVTSKGICLTLSSFVFSSVALLVILVLLGTWSTTRKPDGLNR
LATLAEKEKEILAGKAKKTVRTSKGCPTLLSDCIGDPFPL
>gnl|CDD|133905 PHA00489, PHA00489, scaffolding protein
MPLSLEEHEAILNKLGDPELTESERTEALQQLRESYGSFHSEYEELTEALEKLTAEKEDLIVSNSKLFRQ
LGPTKEEEEEDKQKSFSETITIEDLEGNSPI
>gnl|CDD|133906 PHA00490, PHA00490, terminal protein
MARESRIRITKNDKAEYAKLVKNTKAKITRTKKKYGQDLTGEISPPSLDSFKTREQFNAWKKRAESFTNR
ANRDYQFVKNEYGVVASKAKIDEIESNTKEAQRVVDEILDRFNDKEVISGGKSQGTVGQRKELLSPPDVT
GFGRPEDFDFNKVRSYERLRTLEERMKKRSQPAYYEESMRQLQDNFIRSVEGSFNSYWEADELVEKLKKI
PPDDFYELFLIYNEISFENFDSEGALVEASESILEKIRSYLNDYFRGDSDLSLKGF
>gnl|CDD|222802 PHA00497, pol, RNA-dependent RNA polymerase
EKDAHHSEVTDMDRFVESVGDPLFEGSYNSHVNNPPSYMDDYPLFDGSDPKNPALFRAAANNSINKAVSF
RDFREGVIETLTGIYSFDPQYLRFQRELATALTDFFPAKQDELGVSGNGLRTNFGTMRTVSGFPMIPATA
PLVDNLKKRGDAGLAGPMTSRQMLIFRAMWRLVFSSLKPAALKIPKGSSTGPPRNTNDAEEKLQFALRLL
DHGEAAGWLSAFLKGDYSYAYRLYESAPIYYVVYRWQVDKPGKKRDGGDFVDKARVVADKEYPVTLKVAY
GSQVPDGFFAMRRRTAMAGPFTINAPIQCFAQGCRNAMYERYAYTWHHTTREDKIEKVYEWKFAEATDVS
DHDTFFSGWLIDLICDELPEMFAPWWMELARSLHRLPVYVRAPGPDDGGALLGDPDKLNPQLQVGLPSGH
GFTDLMGKLLWSVIYTLMVLDATAYHLRAQLACEFKDSLLKGREEFGMINKGDDAILGWKRGRDLAKFCK
LLEGQKEGDRYMKIEYEHGGAFLGDVLYQRTGPSKAVAVGNINTMLENTFCPERSVGSAFRPFAGLGNLE
RYNMRGSHPVFEDVWDVIDEIWAKHFGPTYRAYRLGILARDAKALPKELNNGVELFSLAGLNPIDIEVLA
DPSKLHYKWTESEIDPNVVESVMSGLEPSLTERFFHSVYRGNV
>gnl|CDD|133907 PHA00510, PHA00510, transcriptional regulator
MPVTQRGIYHNLKESEYVISNGDVTFFFSSELYLNKFLDGYQENREKFNKKISRLKDTPSNMDMLADITF
YSQVEKRGFHVWLKGDNATWQESHVYALRRMTKPKTLNWSRISKPKLRERRKIMV
>gnl|CDD|222803 PHA00514, PHA00514, dsDNA binding protein
MKKMMQREITTTTAKFAKMEMVDGQVQIEVLNEQTLLGNLTIEQAQKELSKQYKHGPVQVVSVEPNTKLY
ELPVLDFLELATVHGTVTESDEDLEVAP
>gnl|CDD|133909 PHA00515, PHA00515, hypothetical protein
MKADLINKRPKLYSTMFLKLVFSKKLPQAIRRTGQRASPVGQVSRREWQPRRD
>gnl|CDD|222804 PHA00520, PHA00520, packaging NTPase P4
MPVVPDPASIIKLGPAAQALMHSLAPGKWFDGPTNILTVVEKTAAVMELASKQGGALVSVDEITTVMVAN
NKIIGFHKGDVAVVESQVKVVRPGHRGWDVIITSVLTVACAPVVHRWIGHRIESGVEVVVGGTGSGKTPL
LNALAPDVGGGDKYAVIRWGEPLEGYDTDLHVFAALILAAMLDVDVVVVDSLRNVLFELGGNATSGGISR
GAYGLLTDLGNIAASRGCRVVATLNPMSDDEKIEAVVREVSKSNSGSMVVARDNVWRTLFRTGEGLIRIF
AVLATSFTDETVLTLHAPRSNSANRASGLASRTVLENNEIDAVDRNLTRS
>gnl|CDD|222805 PHA00527, PHA00527, hypothetical protein
MAKTKWPKLPRFFVPLFHSANVYLCRSKEEWQQACIHLGVDSGGNEMLAGATQSYCNTETGENLYLLGVF
NGKAATLVHECAHVAFYVCRDVGVTTEPGDANETYCYMLDRMFSHFLPFFHEPEKEGAK
>gnl|CDD|133910 PHA00540, PHA00540, hypothetical protein
MKKSLSLFAIFILSFLGLVIPFITLTAFRPLNEEQYTLKQESSTGKGINETDFINTMFLRSSFFENWSET
NYFINPTLKTSKNLLFNDKWYLDFLQDSYSTGVVYDKPSESFLNYYHQWHSLKNTYMVEKFYDVKKENFL
NDLTDFIYAFAVKYKMFDVSKEIVDNVDRYKENHYPRVKLKQDNWKLITDYNYFDKNIDDKWYFLILKDW
EKKEWRNLKFKNNSNNAYGINTYLRKGSIKGFYRWDGDGEPQTPTIDKNTGEITDWNSYQQNRVKEFIDL
SLYSVLQENIRVQQGGSADYENPNKVGTKRIIFDFETVDELDVKNIKKAIYRMILTVDEANLIISGSLEL
NNINNDDLSFNFSFMRTGMGEVFNFNGSIYSSLNSKDLKYYQQFSGQFDLSKFLQSFFASALVPVFQNRS
SFIENGYIDNLQYDTVLVNFFALKLQNFNNILLSENINDKLQFDKLLNSMFKISQKFYTNYLRTIFDLEN
NTYVQGYNKKYGLLVNNGFKIYPRYFYFSDKYKQLDIKLYSAFKNRFYTINNYGSVFNYDFSVANNYNIK
LNSGYVFGGDLQNKYGLQYKKIEEQKIGYNVFELQAQKENDMYRYYDFNFGIYNWQEINNGGLFPDKQWW
QVQYVTPKGWWDFGAHIKNAVIWIVNTIPGVKQVNELASGVGKVFETVYSFFSQIFEVWKFNPALYSTIT
NIFLLIIFMKFVRLI
>gnl|CDD|106954 PHA00542, PHA00542, putative Cro-like protein
MEKAMPATTPTIPAAYTQRPDELVCALIRAGWSQEQIADATDVSQPTICRIYSGRHKDPRYSVVEKLRHL
VLNLDDFQQVTR
>gnl|CDD|164822 PHA00547, PHA00547, hypothetical protein
MKKFIFFFKNYCYISGSMFLFSLIDLLLWIISLYCVGLVFWILFALQCIYFVWWLWKNIFYQLNAFRLVN
FIWDNPLSVIIGKLGTGKTLLLTYLSQTMKLLTDEIYSNYPLEDDKVKVLTFKNLDFTDRTKPVPPDDSV
ILFDESYLYIDGTSPHDEKKVHSGKIPWIVLARHFGNRALFTAQREGMIWNNIRQLASGIIIPISLKKPV
AKKGFNFFNRFFIMRIGIFQDITDYEIWKTKSVERTAEGKRVKHKSDVGLGIRFFKIIIPLEFANKYDSQ
WLKFVRDLKNDEIVNKKEYYWSEITKLSVKERLELFDIDILKKNLKPKKEKGNGKDD
>gnl|CDD|177288 PHA00616, PHA00616, hypothetical protein
MYQCLRCGGIFRKKKEVIEHLLSVHKQNKLTLEYFYIYFRVREK
>gnl|CDD|177289 PHA00617, PHA00617, ribbon-helix-helix domain containing protein
MKARVEYIKLPKSSYSRSYRKIEVTRKGDTIELTLTETMDVISFKLPPELNAKLEQVAIKMKKSKSEIIR
EALEKYLEEV
>gnl|CDD|177290 PHA00619, PHA00619, CRISPR-associated Cas4-like protein
LMSRLLTIIYNYEIVSQNDLQTIWVTELSRCLRRSWLMRKNGGVKLALEEAMKMHIGSGLHMRLQRILKK
HGFETECRVERKTALGFEIVGKIDVYDKEENTIYELKYTHMDDLDKGRLNNYLRQLNYYIEMANAMAGYL
IIVHADGRVEEIKRDWSETDLENRANAFGISVEENILPPKKSKPDSECIECPFYNVCWKRD
>gnl|CDD|106959 PHA00626, PHA00626, hypothetical protein
MSCPKCGSGNIAKEKTMRGWSDDYVCCDCGYNDSKDAFGERGKNEFVRINKERKGNEKS
>gnl|CDD|222806 PHA00645, PHA00645, hypothetical protein
MINLLVENNNSNWDKIFSFVFDIFLFIFDVIWNTKLPMTNTSIAYFLVFFMVIKLSIYAIHGTSTQYNNL
GSTVNNGVSQVYSSTVRKGINVGKGVYQNSNKQQVKREKKRQSIRAKAKNKRSNK
>gnl|CDD|133916 PHA00646, PHA00646, hypothetical protein
NDWQRVKEFFIQIFLFIDKTNVENIVMWNLTQNEYLTLMVGIWLVILFLTWFSLWMVFKIVGYFK
>gnl|CDD|106962 PHA00649, PHA00649, hypothetical protein
MSDQHCDTPACQEAADRAVKKVFAILGVDVDVPEQVEEFREDLRFGRRMRKAADHGFLALVGLVAVALGA
AVWAGITSKLGGH
>gnl|CDD|106963 PHA00650, PHA00650, hypothetical protein
MASPVINTREDLDALAGTPAHGEFLDYLRGSITRKQDAQTYPDGYDTPDYEGPTLDPVWQDVEDLSTIER
FGFTKAELLGGE
>gnl|CDD|106964 PHA00652, PHA00652, hypothetical protein
MEPIEEATKCYDQMLIVERYERVISYLYPIAQSIPRKHGVAREMFLKCLLGQVELFIVAGKSNQVSKLYA
ADAGLAMLRFWLRFLAGIQKPHAMTPHQVETAQVLIAEVGRILGSWIARVNRKGQAGK
>gnl|CDD|164824 PHA00653, mtd, major tropism determinant
MSTAVQFRGGTTAQHATFTGAAREITVDTDKNTVVVHDGATAGGFPLARHDLVKTAFIKADKSAVAFTRT
GNATASIKAGTIVEVNGKLVQFTADTAITMPALTAGTDYAIYVCDDGTVRADSNFSAPTGYTSTTARKVG
GFHYAPGSNAAAQAGGNTTAQINEYSLWDIKFRPAALDPRGMTLVAGAFWADIYLLGVNHLTDGTSKYNV
TIADGSASPKKSTKFGGDGSAAYSDGAWYNFAEVMTHHGKRLPNYNEFQALAFGTTEATSSGGTDVPTTG
VNGTGATSAWNIFTSKWGVVQASGCLWTWGNEFGGVNGASEYTANTGGRGSVYAQPAAALFGGSWNYTSL
SGSRAAYWYSGPSNSFANIGARGVCDHLILE
>gnl|CDD|106966 PHA00657, PHA00657, crystallin beta/gamma motif-containing protein
MSNEFDAAVAGTLGQQPAQDTTADPFDAAVAGVLRPDQGQAARAGFVLASDTDPDAYAEAQRVARRANLP
IETVLNQPKEAKRQDTIGAIDFDTLGKTSPATAALLADVEKAKIAHDNVDNMTGIESVLSSLGTAVKYLV
SAPDQKNTLMGDIGAGFAQANRGAAGLFQSVFELPNNLVGTILPANPLQPVADQFAQWGAQSKDLAKRLS
PPQSDTLGSGVSSGVQSLTSNLLMLPLALLPGGQPAALGGMASMTGGQSYQDARSQGLTPAQALPFAVSQ
ATIEYATEKLPVSRLIGDLHAGSPLLKTLAHQVATEVPGEQVATVLQDLNEWAVLPENKEKPFSAYLAER
PSAAAQTLIATLVGVGGNVAVMRGIDRTITTADQRTQRAQAAQQQAELLARLNQLAAADKVLARDPDTFE
QFVANAAENGPVQQVFIDANTLMQSGLAEQVAAVSPAVAAQLPEALQTGGQVAIPVEEYAARIAPTEATQ
GLLDHLKTEPEGFSRAEAQQYMQSQAEELRAEVERALGEQQGDDAFKQSAEAVRAAVKTQLDTAARFTPQ
VNDAYSSMVGNFYAVQAARLGTTPEALFQQYPLRVAAESVAGGQQFDQEHGPFGPVLRDFQGDAKGAIAK
LLEMKSGEAIGALHHPDIGDIDLVWGEEGTRRSDGYGLAKLAKWHPEVLDDLQGILSAMKVTSRTENRVN
LESADHRAGVRLTWDDQAKHWLLTAFQKKGGVAGTRTGTTDLFVEDGTARPDDASDAIVDQKIDKFYQGG
GRARGTFDPATLTVSLLKNADLSTFLHESGHFFLEVQLDIATRLAEKQRAGATLIDAETEVQRDAQTLLD
WFGVRDLAAWNDLDFEAKRAHHEQFARGFEAYLFEGKAPSIEMHGLFQRFRAWLLNVYRDLKALNVELTP
EVRNVFDRMLATGEQIALAEQGRSMMPLFATAEQAGMTPEEFAAYQALGVDATNDAIQDLQARGLRDMQW
LHNARGRIIKQLQKDAAARRADVRRQVAEEVNAQPVYRADRFLRYGELELPPGAPQNVRRAAEQANVDGA
KLSLPALKEMYGEGENAIWRYLPTGKNGLAASEGMHPDTVAELFGFTSGDELVRRLLEAPPRGEEIEALT
DVRMLEQFGELSTPEAIERAADSAIHNDARARFVATEANALARVAAGPTQQIGTDRRGRPIVRRVLPEAA
REYARALVSRLKVRDIRPGQYTNAEVRAARNADRAMKAGDLATAAAEKRNQLIQHQAARAAYDAQDEVER
GLRYLGKFAGDIKGIDVDYADQIANLLERFDLRKGQSLKAVDKRTALADWLRSQREAGFEPDIPAELENE
AYRTSYKNMTVEEFRGLVDSVRQIEHLGRLKRKLLTAADQRDYEAVRDEIAGSIRAHAQGRSADTRTPTT
NAGRAVQGLKRFWASHIKAATWARVMDGGKDGGPMWEYFVRSANERGDMETTMRAEATGKLSEILAPVFA
LGKMGGKGQHFPTIGRSLNREARLTIALNMGNEGNIQRLLGGEGWTPAQIAPVLQSLTAQEWQAVQAVWD
HFEGYRPQIAAKERRVYGKEPAWVEPRPLTITTADGQTLTLRGGYYPIKYDPAASQRAEEHSDAESARRQ
LQGAYTTATTRRSFTKSRVEEVSGRPLLYTLSGLYSGVNDVIHDLAWHEWLIDANRLLRSQTIDGAIREH
YGPEAKQQFKTWAADIAEGERGADAAVDIALSRLRQGVSASGLGFNVMSALMQPLGITQSIVRVGAPWVG
RGVMKYLAAPVGLTREINAKSSFMANRARTRFRELNELRNQVQDGSATKEWVGRNAYFLMMRCQQMVDVP
TWWGAYEKAVAEGNDETRAVSLADQAVIDSQGGGQTKDLSAIERGGPAQRLFTVFYSFMNTALNIGVAQT
MSADTPAKRAKLAADYAMLYVVPAVLGYFLKDALTPGDSGDDDPEKLAKKLLANQIDYLMGLMVVVREFG
EAAKTVTGANDMGRDYTGPAGLRLIADVGRFATQTHQGEFDDAFRKAAVNVVGDLFGLPSAQINRTVTGV
QALAEGKTQNPAAIGFGFQEAR
>gnl|CDD|106967 PHA00658, PHA00658, putative lysin
MPRVPVYDSPQVSPNTVPQARLATPSFATPTFRGADAPAFQDTANQQARQFSQGARQFSNDVGRIADSMV
QQANQLRVDDALNRAKEAALRLTYDKDTGFANLKGINALERPEGKPLADEYGDNLKKQLDEISGTLGNDA
QRRAFALHSNDILTSFRGQAVQHEASEYKTYALSTSEGIQSTALRDIALNWNNPDAINSAVDRIKAETFR
QAQLLGKSAEWQEAQARKLTSNAHKIALMSALEQNNPTYASAYLNKYSGQMDADDILTVRGHITKDMDGR
AGLAAATDAVGKVPIQVSDGERAFNIAVGTESGGRQFGADGKPLTSPKGAVGIAQVMPDTAPEAAKLAGL
PWDENRYRNDAAYNRALGMAYFQKQLRDFGGDLPKAYAAYNAGPGALQSALKDAKDGNWLALLPKETQDY
VVKNMQAYNAGQGRPARPTLADIEAQLQNDPRLAGNPERLKIARVEAERQFNMQTAALKQRDDEAVATAL
RGLYENGGRFSELPVSIRANIPPEKLTSVMGAAERIAKGDDTTSLWLYNKLTNSPDELARMSDNEFYALR
TSLSEADFKHFSQERAKRLGAAPSTNGPGDLNSQAIKAGLDTRLRMMGDDPTPKDGSSDAERVGAMRKFI
DGYFIAAQREAGKKFTDAEVEQHLDALFMKNATVRGWFSNSSVPILSMKVGDIDSATKDGIKAAYKRAGI
DSPTDAQILNAYWNLKVSRK
>gnl|CDD|133918 PHA00660, PHA00660, hypothetical protein
MGSGLVGSYYGARSQQSSLQFQSNIARINAGIANTNADTIESIGNANADAILATGDFNASIAELGAQSAL
EAGQQQIAAQTLKAGQLKGAQRAALAANGIDLGEGSAAEVQVSSDIVKQIDTDTLRANAARTAWGYRAQG
MEAQLQAGLQALNTRTQAKVQGINLRTGAGSMEADALLKSGSAAGISPVGAGFSSLLSGAGDVADSWYRY
SQSKG
>gnl|CDD|106970 PHA00661, PHA00661, hypothetical protein
SNVRVLQRSFGGGEISPELFGRIDDAKYQSGLAICRNFIVKPQGPAENRAGFRFVRAVKDSAKKVRLIPF
TYSVTQTYVLEFGAGYFRFHTNGGTLLNGAVPYEIATPYAEADLFNIHYTQSADVLTLVHPNYPPRELRR
LGATNWQLATVTFTSGPFEDINVDTPVSVTASANTGGTTLTASASVFALDAVGKLFYLEQPAVDSVPVWE
TSTESAPSSARRCTNNLYTNGGAGTIGTLRPSHTEGSAWDGSGGASRYNVYKEQGGEWEYIHSGTGTSLI
DDVIAPDLSVTPPIYDAVPSQVVGTLNASYKWAKYAFNSAGGYPAAVSYFEQRLCFAGTTNKPQNIWMTR
SGTESAMSYSLPVRDDDRIAFRVAARQANAIRHIVPLTSLLLLTSGGEWVIASVNSDAVTPTTISVRPQS
SVGSTDVQPVVVNNTTIFVQARGGHVRDLAYNFQADGYVTTDLTLRAAHLFDNLDILDMCFAKAPQSIVW
FIRSDGKLLGLTYVPEQQVGAWHQHDTAGVFESCAVVAEGNEDRLYAVVRRTINGQTVRYVERLASRLFD
AQADAFFVDSGLTYSGEPTSHISGLEHLEGKTVSILADGAVHPQRVVTDGAITLDVEAGTVHIGLPITAE
LQTLPVNMQLDGSFGQGKVKNINKLWLRVHRSSGIFAGPHADALTEVKQRESEPYGSPPALKSEEVPLVL
SSKWGDSGQLFVRQADPLPLMILSMSPELAIGAF
>gnl|CDD|222807 PHA00662, PHA00662, hypothetical protein
MASEVDICNRALAYIGDERTIASLNEGSKQAEYCARFYDFARDALLELHTWGFATKRAQLAAMGISPPEW
RYAYAQPADAIRIVAVLPHGAANIEAGIDNAQPFSCEIDNTGDIILTNQVNAVARYISRVTDTNKFDALF
VEALAWRLAAMLAGPLTGSAGAAESARCVGAMQIYLAQAMVSNANQRPTKPAHMDEWMRARGAGFVDGNI
PGLPN
>gnl|CDD|106972 PHA00663, PHA00663, hypothetical protein
MEVIALKQGYFGKLREPGDKFDVPDGAKASWFAPASAAQHAPRAGKAPKQPADKNPQGSDDKSGGDLV
>gnl|CDD|106973 PHA00664, PHA00664, hypothetical protein
MIIDKLLQFSDAQAVTASAASTDVIDLGSANPDIGMGDPLKMVITVDEAADAAGAATVTFSVQQSDDNAS
FSSVTDTGAIAKASLTAGKRVVIPMPTKLERYLRVNYTVATGPLTAGKFTAGIVLGVQQNVAYPDSPRIA
>gnl|CDD|106974 PHA00665, PHA00665, major capsid protein
MATLSTTNPTLADVAKRMDPNGKIDQIVEMLNQTNPILQDMTVIEGNLPTGHKTTVRSGLPTPTWRKLNY
GVQPEKSRTVQVTDSMGMLETYAEVDKALADLNGNTAAFRLSEDRAFIEGMNQTVAQTLFYGDSSIDPEK
FMGLSPRFNSLSAENAQNIIDAGGTGSDNASIWLVVWGPNTLHTIYPKGSKAGLQSEDLGQDTLIDANGG
RYEGYRTHYKWDIGLTLRDWRYVVRIANIDVSELTKNASAGADLIKLMVQAAERIPNLGMGRPVFYMNRT
IRSFLRLQITNKVAANLTMEEIAGKKVVSFDGIPIRRTDALLNTEARVV
>gnl|CDD|222808 PHA00666, PHA00666, putative protease
MNLFERLLMRRLCNEQPGDGGSQPAASEPAAGAGDNPAPQGDPTQEEGDKPQPAAGADKPEGDKKADGDK
PEEKKPGEKPEGAPEKYEFQAAEGVELDTGALGAFEPVARELNLTNEQAQKVVDLYTKILPVVQQRQAEA
WQKTTEQWAADSKADKEIGGDKLQENLSAAQRALDQFGTPELKEYLNKTGLGNHPELVKVFYKAGKAMSE
DRLVTGGNEPKQSDARRLYAASN
>gnl|CDD|106976 PHA00667, PHA00667, hypothetical protein
MSLEAAIQENTSALRDLIAAIKAGVPTTAAQVAAVAAEAPAAQQEASTEKKPRATSAKTTAATAPTPPTA
EVGAADAPESKAENSAPVQAGDAGQDAAAGDAAPTYQDTADAVTKLARVKGRDAAVAVLSKFGAAKLPDV
KPEQFADVLAACNQAMEG
>gnl|CDD|222809 PHA00669, PHA00669, hypothetical protein
MPLVNMKMTPKEAGTDSCCGEAGAPETTPEYPWGLCITLNNEALERLGIDALPAVGSVVMITARAVVCSV
SSRETGKGPDRSVDLQITDMDLAPRTQDDEKSAAQRLYGNGSMS
>gnl|CDD|106978 PHA00670, PHA00670, hypothetical protein
TENSKLLKRLGQLKTERQSVESHWDEISDYIMPRRSRFFSDDRNRGENRNRKIFDSTGTDALRTLSSGMM
SGITSPARPWFRLATRDPELNEDAEVKAWLENVTRDMYSAFQKSNFYLELNETYISLGGFGTAAMVVEED
EDEVVVFQSSPIGDYYFAEDNRGQVDTFYRQFRWTVAQMVQEFGDENTSESVQSKAEEGSNEAWVEVVHA
VEPRADRDPSKLDPRNMPFKSVYFEKGGDEVRLLRESGYREFPALAPRWRVSGGDVYGFSPAMLALGDVR
TLQREQKRKAQSIDKVINPPLMAPESGKNQDISLGPGGLTYVDDMESNGGIRKAFEVNARFDVLLADIQD
TRQTINRIYYVDLFQMLANKDSPAMTATEVQERYEEKLLMLGPVLERLENEFLSPLIQRTFNIMVRANKL
PEPPQELQGADLDVEYTSPLAQAQKAIQAASIERWVGSLGQLAQIKPEVLDKPDWDRMADMLADMLGVPP
TLIVPKEQVQSIRKQRAQQQQAAQQAAIAEAAANAAKALGKAQTSLQEAL
>gnl|CDD|106979 PHA00671, PHA00671, hypothetical protein
MSGAVTAVAVGAAVGVGASMYMSNKQEKAQRSAQQQAQQQAQQQADQAKAESDRLTQEYQKQTEAYQQQA
KIMQQQLLDSQQSFNRANQKQPNSQRALSAVGSAAKSGQSGTMLTGPQGVDQSALTLGKSTLLGQ
>gnl|CDD|133920 PHA00672, PHA00672, hypothetical protein
MTAIVAPRPHLPAMSAEAIDRVRRLEGALAELPQVEIPTAHLFHAGVYARTIRIPAGVALTGALIKVSTV
LIFSGHATVFIGGEAVELRGYHVIPASAGRKQAFVAHADTDLTMLFPSEARSVAEAEAEFTDEADLLLSH
QQGAETITFTGE
>gnl|CDD|106981 PHA00673, PHA00673, acetyltransferase domain containing protein
METAIVRRVAFAELADAPTFASLCAEYAHESANADLAGRAPDHHAYAGMEAAGVAHFLGVFRGEELVGFA
CLLVTPVPHFKGQLIGTTESIFVAAAHRPGGAGMALLRATEALARDLGATGLYVSGPTEGRLVQLLPAAG
YRETNRTFYRGLHA
>gnl|CDD|106982 PHA00675, PHA00675, hypothetical protein
MLKTVAVNDAGLRVGEDHPNAKLTDAEVERIRELHEVEGMSYAVLAEKFEQSKGAIAKICRYERRGQFAV
RVKTVPVR
>gnl|CDD|106983 PHA00676, PHA00676, hypothetical protein
MERANWVMVGGSKADGSVTLGIDVPAKYGVTETPVEWDINQANTEADRRCKNWGYSGADMYREGQFPILK
TCHAQGVSPCWSKTYRVQYQCLSLQS
>gnl|CDD|106984 PHA00679, PHA00679, hypothetical protein
MMIYYLTYLAAGVLLGLAVLPWKQRLGSREGVLLWLLAWACFWPYLLLYAAWQGLKAYRAAWWAYTGHKH
Q
>gnl|CDD|106985 PHA00680, PHA00680, hypothetical protein
MNLRTLTDEEFLRHALAVQDPLTSSAIEAECLRRFEALLDTHDSEAYELVTERELDASVLCETLDTLDAH
DIEPGALAQLCDAMLIGPANTAALLNALAAADLDAPESLKAELDLAKQFRALVEDAGDVFSRLSELTTTA
NKE
>gnl|CDD|222810 PHA00684, PHA00684, hypothetical protein
MIFVFGSNLAGAHGAGAAAAAHKEHGAAWGVGEGRTGHSYAIPTKAGTVISTLSLPDIGAAVNRFIAYAT
AHPHLNFQVTRVGCGLAGHLDADIAPMFRDAPDNCSFDEAWKPWLEDSSAAAQYWGTF
>gnl|CDD|106987 PHA00687, PHA00687, hypothetical protein
MKNRQPVQTTLPPEAMRLLQQAAQTPITRADPLARVKAIEKATERVKRQYPHFFKE
>gnl|CDD|106988 PHA00689, PHA00689, hypothetical protein
MTYFDEYDQDHDQEPRAVTCKRCGKTGLRWEDDGGEWVLMEGHYKIHRCDMRKAALDDFEAV
>gnl|CDD|106989 PHA00691, PHA00691, hypothetical protein
MTYREKDIAYENGRVWVLKKSDSYTVFVSGVTHSTSDSTYELSDAESGIAKARADYLARKLNPAGGLV
>gnl|CDD|106990 PHA00692, PHA00692, hypothetical protein
MTVRDNMLRVENARVRVQEHCMCARFHEDRTHYFVEYPPGFRFGGCRVSKGMGAARALDVLLTRMEQHWK
DEQL
>gnl|CDD|222811 PHA00724, PHA00724, hypothetical protein
MMSALGDVIYILGILIPLLGLIVRNYLVNLMGFVMGTIGFLVFVQNYTDITFSASTFYLSFLPLAFGLIN
FAFFFNWLREERI
>gnl|CDD|177293 PHA00725, PHA00725, hypothetical protein
MRWMSNGLTSPKNIRRNSPRFRFNYYHYCTTVQKAKAQEREINIKPQIHRVLSRHSVGIRLNRKSFCFLH
KFSRLLHGSIP
>gnl|CDD|177294 PHA00726, PHA00726, hypothetical protein
VLLVPKTYAEIVLVFDTIMLTTALLFRKPKPKKVKSTLNHRSIGYYLVISSVLALIVSHFVSYASLIDYF
MGLSLDSLMFYIGLRCLYN
>gnl|CDD|222812 PHA00727, PHA00727, hypothetical protein
MSDGKLVSAWEEELRKAQSLEELKQKYEEAQKQIADGKTLKRLYKVYEKREFELKKQQFEQLKAELSKKK
KKFKKEKVDVRVKVVKKWINSRLFTAEHYVAMLQQSKDGLQLLFLRRAKLVENQGYLMLEVKKMRKSWVL
NGEPLLLEKSKFPFGKKFVAVHFVLPDYPYTLDLTIDEKIRQLTLKTLNAPQIIHSIIKTKFFEALAKVG
SGPDLMMLIIGAIMGIGIGVAIGFGIANANLTHLLSQHVTNTTTTHLATTTTTTTSPSFTIPSNSSKG
>gnl|CDD|177296 PHA00728, PHA00728, hypothetical protein
MAKLTEVEQLKKENEELKKKLAELEALMNNESAEEDEELQEIENPYTVTNRAISELVEPKDTMFYLSGNQ
ISLILTAFEFARLPAYFGEEPVTELAEFAHKLKHYLVSKGGRGRRDILRVLRVSSGQVRENVNKSLFKQL
LQGGKDSDVKE
>gnl|CDD|177297 PHA00729, PHA00729, NTP-binding motif containing protein
MLWLAKKIVSAYNNNGFVSAVIFGKQGSGKTTYALKVARDVFWKLNNLSTKDDAWQYVQNSYFFELPDAL
EKIQDAIDNDYRIPLIIFDDAGIWLSKYVWYEDYMKTFYKIYALIRTRVSAVIFTTPSPEDLAFYLREKG
WYQIRVTMVNRKTMTARATLYSKDFGRNSKGEIVTQVKKKALDLFKVQIPNDIYKEYMQRRKETERKLLQ
ELRQILSTLNVKNNVN
>gnl|CDD|222813 PHA00730, int, integrase
GNKVYTFGDIRIREVKGKYYVYLIEKDNEGNRRDTYVGSLDQVVESYLKMKKLGVVGKCPGQGLPPGFEA
GTSGSNPRPETDLSRDSNNELKGVIIIDSNLTSDNNSEISASDLLFFEFALRQKKISEETCKEYINYIKK
PLKENNNSIKAWRNFYRFLGNRDPPKSLKTKKSKPDLRVPTLEEIKKTLQKVKEYENVYLLYRLLLESGS
RLSEALKVLNEYNPENDICENGFCIYTLNWTRGQKKVFYVFHITPLKKIKITKWYIDKFVRRLDLIPPKY
IRKFVATKMLELGIPSEVVDFIQGRTPSRILTKHYLDLLTLAKKEYKKYAEWLRQTL
>gnl|CDD|222814 PHA00731, PHA00731, hypothetical protein
MEPQEEKEKLVSQNSIFFLLTEGRKTYGKYLHLKIEINEDEKIEKKFFFTEKIALEEVLLKLKRLYEVYE
DSEDETQEAIRKEVLLEIAKLLYLFD
>gnl|CDD|177300 PHA00732, PHA00732, hypothetical protein
MFKCPICGFTTVTLFALKQHARRNHTLTKCPVCNKSYRRLNQHFYSQYDIEHLIYCYLFSTYKLPYHVRL
AIKRKLEVE
>gnl|CDD|177301 PHA00733, PHA00733, hypothetical protein
GGIMMESGSKKYLSNHKGIFIHVTLEELKRYHSLTPEQKRLIRAVVKTLIYNPQLLDESSYLYKLLTSKA
VSPYVCPLCLMPFSSSVSLKQHIRYTEHSKVCPVCGKEFRNTDSTLDHVCKKHNICVS
>gnl|CDD|177302 PHA00734, PHA00734, hypothetical protein
MLYDILLFYGFQFNDYWTTVLGLRVGAREANIIARLFMKNKWTLAIYKFDLATVALLLGLMLPTFHQTEI
FLLVDDVVECLVTLNNILTIRRHKR
>gnl|CDD|177303 PHA00735, PHA00735, hypothetical protein
MKWGLSLLLLTLLLLPIFANAIVTGPHPYFDGGGGFTGPFFVYSKTIQVGSSTFSSKYNGSTLSTAPWLN
PTYISVYNKYYLQVLPNQEYISNNVSLSLSSSQIALNVTWLLASSSNTGSYGSIAIGYGVNFPSGFTGSY
APASPYASDGIVVYMEKGSFPTYRLFVYFDGVKQLNVSVGSISVGQQIGLGFWYLPASNQLYVYYYNGTL
KTFSITPGQVINNQFYPLSLNTVNSNYVIDAQNVGPGYGYGQWVVITYSIFQSKTYTATLSYTSVIGNGY
QALAGFTGANNPLNISTNATSWSVVGIVKVVNFSVTGSQYPLSGSVSYLGKPKGIYLLLNVYPAGNVNTW
YLNVTVEFQFVTASSTVYMNITIPVFVAGFAVLVQVNLPQSSYLSGQTISVTNSTTIMYPSNAGYSLAVP
PKALINIQGLTNGFVPLPYSITANVVVPTTYYYTINIQLGQFSLGSATGTITIYPVSPLPVIFVSQYPHS
VQLGTKVTITFQFSYNTPVANVTMSAFTQTTTTFAWAYASIITSSSVVQFKAYWLSANDGILIITQSQNY
LIPFNFTGLTFYNNSVNTIQINIVNNALQLTINGGTLNIANSSKVIGLGFYYGAGKLVLNWFFVSGIILQ
SATANQAYVILTGTNPSTLTQYTTGYTNSSGFGQVTITLTYTPYELIDIYWAGVTKYVLLNISVTQPTTS
TTTTVNTSTLNYNYTQPFSNNISPNSSLYNFSAYQPWATIIGIVVTVVVALLGWKFGGKAGASGGVVMGL
IMTAYLGLIPWYIFYIFIFGIALLLAKVMVDKFMGSEE
>gnl|CDD|177304 PHA00736, PHA00736, hypothetical protein
MTDAISLALQTGLGPVIAIIIILAMMGLTYKMAGKIPAILVGIASTFTLMFMDFLPLFWGITVIFGLIAG
LVLGGRDGD
>gnl|CDD|177305 PHA00738, PHA00738, putative HTH transcription regulator
MDYNANEIRAKILRRKILELIAENYILSASLISHTLLLSYTTVLRHLKILNEQGYIELYKEGRTLYAKIR
ENSKEIQILNSELEGFKKLSENTDLTKDGHQVKTKDNT
>gnl|CDD|177306 PHA00739, V3, structural protein VP3
EEINLKQIIFLFIFILIGIVLFQPIISYVNNVTTSGTYTTIVSGTVTTSSFVSNPQYVGSSNATLVSLVP
LFYLLVLIIVPAVVAYKIYKEE
>gnl|CDD|222815 PHA00742, PHA00742, hypothetical protein
TNSFKLKYWGNQPEDYILPNPYLGREYLVLGKLLIKLSKWRAKGLLDFDVYIRPTGVGTLTNVINPEYYH
GLQDKYDLTLYVKAKDSYYPLVWIDITGSSWTEEQSKERYGESVYAILSTKVEVAKKYDVMGRVWFIHYN
DTEDKLKCISALQILNLERQGKIKKDKFERDAKSEYYLIPRSYWKNLTELRVSLKGFYQSFKEYLARVSG
K
>gnl|CDD|177308 PHA00743, PHA00743, helix-turn-helix protein
FLELDEDVRELLSIIHEIKIDIITQSYDKEKIEKAIFLSQKIQAELYQLLR
>gnl|CDD|164842 PHA00771, PHA00771, head assembly protein
MITFTPTRNIDLIETVGNHPDIIAGSNNGDGYDYKPECRYFEVNVHGQFGGIVYYNEIQPLTFDCHAMYL
PEIRGFSKEIGLAFWRYILTNTTVQCVTSFAARKFRHGQMYCAMIGLKRVGTIKKYFKGVDDVTFYSATR
EELIDFLNHGR
>gnl|CDD|107010 PHA00780, PHA00780, hypothetical protein
MAEIIPMTEEQKFQLEIYKLVMNQNAAAEEAFQFIGTDELKLELFKIHFQSGGANSDITTRTIEAVRKSK
EALDLFTTGA
>gnl|CDD|133939 PHA00781, PHA00781, hypothetical protein
MSRVINLGKEKKFPITQELYERLESVIHDYDGEISLCEAIGTLELLKQSLIEGAKESSP
>gnl|CDD|164843 PHA00821, PHA00821, hypothetical protein
MPTNTPITIPIANGVVSVPMAQGSKGQVEVQLFGPAPATGTLKVEGLQWTGTYQVLQGATAINLATALAG
GGTIALTEHGHYRALRFTFTGVTGSTGPLSGTAYVTDGAIADLAFQGLRALNVQGYVESNVKLGYQFYFQ
YMLPTIAGGGTNAVKIAFRTAAQPVLIKDRALYALGNSVGLQLFKAPTGISGGTAIPVQNYNDIIPQTST
VTVLGGVTTTSNGTAWGDPTHIYGASQAGGRTGSGLAPGADRVLAPNHDYLIVVTNLDTTTGTGGQALCD
YYLTWYEGALDLPRQ
>gnl|CDD|222816 PHA00911, 21, prohead core scaffolding protein and protease
MEPELLIETWGQPGEIISVVILEESKDGKKDLYIEGIFMQAEVVNRNGRLYPKKVLEKAVEDYIEEQVET
GQALGELNHPPRPNVDPDRAAIIIEDLWWEGNNVYGKARILDTPPGDKLAALIRAGWIPGVSSRGLGSLK
DQNKGYNIVQEGFKLTVAVDVVWGPSAPDAYVKPIMEGKEEITESQTAETDNSRESTDDAFMALAEALKK
LL
>gnl|CDD|222817 PHA00965, PHA00965, tail protein
MRKLSNFKFFYNTPFTDYQNTIHFNSNKERDAYFGRHFKSLEYSSQNPYNFMRDRMEINVDMQWEDAQGI
NYMTFLSDFENRRYYAFVNQIEYVNDVVVKISFVIDVIMTYTQGNVLEQLNNVNIERQHLTKREYNYNLP
MLRSNDDVLKVSNKNYVYNQMQQFLENLVLFQSSADLSKKFGTKKEPNLDTSKGTTYDNITSPVDLYVMD
YGDFINFMDKLSAYPWITQNIQKVQMLPKDFINTKDLEDVKTSEKITGDRAKVKTLKQGGKSKEWDLNDL
SLSYAKLQEMMLSKPIEFKHMIRNEYMTIEFTDWNGNTMLLDAGKISQKTGLKLRTKSIIGYHNEVRVYP
VDYNSAGNDRPILAKNKKILIDTGSYLNTAITFNSFAQIPILIDSGILGQAQQAYRRRNAESQLITNRID
TVLNNGSDPKSRFYNAVSVASNLSPTALFGKFNEEYNFYKQQQAEYKDLALQPPSVTESEMGNAFQIKNS
IFGLTLKISVPSQKEITFLKKYYMLFGYECNDYSTKIEPINSMTICNYLKCTGTYTLPNIDPMLMEMLRA
ILESGVRLWHNDGPMLQDPLNNKFRENV
>gnl|CDD|177310 PHA00979, PHA00979, putative major coat protein
MKRLNALKKFGKQAAATVTVAVLSVPAMAAEGGAADPFSAIDLSGVATKIGAAGLVIVGITMAYKSITLA
KRAVNKA
>gnl|CDD|222818 PHA01075, PHA01075, major capsid protein
MAQQSTKNETALLVAKSAKSALQDFNHDYSKSWTFGDKWDNSNTMFETFVNKYLFPKINETLLIDIALGN
RFNWLAKEQDFIGQYSEEYVIMDTVPINMDLSKNEELMLKRNYPRMATKLYGNGIVKKQKFTLNNNDTRF
NFQTLADATNYALGVYKKKISDINVLEEKEMRAMLVDYSLNQLSETNVRKATSKEDLASKVFEAILNLQN
NSAKYNEVHRASGGAIGQYTTVSKLKDIVILTTDSLKSYLLDTKIANTFQIAGIDFTDHVISFDDLGGVF
KVTKEFKLQNQDSIDFLRAYGDYQSQLGDTIPVGAVFTYDVSKLKEFTGNVEEIKPKSDLYAFILDINSI
KYKRYTKGMLKQPFYNGEFDEVTHWIHYYSFKAISPFFNKILITDQDVNPKPEEELQE
>gnl|CDD|107017 PHA01076, PHA01076, putative encapsidation protein
MNDDIDYYISISNRSDGKSFNYVSFFIYLAIKLDIKFTLLSRHYTLRDAYRDFIEEIIDENPLFKSKRVT
FRSARDYLAIIYQDKEIGVITDLNSATDLKYHSNFLKHYPIIIYDEFLALEDDYLIDEWDKLKTIYESID
RNHGNVDYIGFPKMFLLGNAVNFSSPILSNLNIYNLLQKHKMNTSRLYKNIFLEMRRNDYVNEKRNTRAF
NSNDDAMTTGEFEFNEYNLADDNLRNHINQNGDFFYIKTDDKYIKVMYNVDTFMTNIIVIPYTKQYEFCT
KIKDIDNHVTYLRDDMFYKENMERYYYNPSNLHFDNAYSKNYVVDNDRYLYLDMNKIIKFHIKNEMKKNM
SEFERKEKIYEDNYIENTKKYLMKQYGL
>gnl|CDD|222819 PHA01077, PHA01077, putative lower collar protein
MARYTMTLYDFIKSELIKKGFNEFVNDNKLTFYDDEFQFMQKMLKFDKDVLAIVNEKVFKGFSLKEDLSD
LLFKKSFTIHFLDREINRQTVEAFGMQVITVCITHEDYLNVVYSSSEVEKYLQSQGFTEHNEDTTNNTDE
TSNQNATSLDNSTGMTANRNAYVSLPQSEVNIDVDNTTLRFADNNTIDNGKTVNKSSNESNQNAKRNQNQ
KGNAKGTQFTKQYLIDNIDKAYDLRKKILNEFDKKCFLQIW
>gnl|CDD|164848 PHA01078, PHA01078, putative upper collar protein
MILGYVNNTYFNQAPNFSSNFNFQFQKRLTKEDIYFIVPDYLIPDDCLQIHKLYDNCMSGNFVVMQNKPI
QYNSDIEIIEHYTDELAEVALSRFSLIMQAKFSKIFKSEINDESINQLVSEIYNGAPFVKMSPMFNAEDD
IIDLTSNSVIPALTEMKREYQNKISELSNYLGINSLAVDKESGVSDEEAKSNRGFTTSNSNIYLKGREPI
TFLSKRYGLDIKPYYDDETTSKISMVDTLFKDESSDING
>gnl|CDD|164849 PHA01079, PHA01079, hypothetical protein
MYEGNNMRSMMGTSYEDSRLNKRTELNENMSIDTNKSEDEYGVQIHSL
>gnl|CDD|164850 PHA01080, PHA01080, hypothetical protein
MPVCALPNSQGFLAVTDKPLNECDGGYVAVTIQDYDYLMSYTRITPTDAGTAFSFGFMAVFALGYLSTYA
VYIGKKLINL
>gnl|CDD|133945 PHA01081, PHA01081, putative minor coat protein
MDWVIDLFNKLIEFLYRLLITLIDMLKDVFLWLIDGVLSAVNLLLEKALSLIEPMDVSQYLTGIPSGAAW
VISAIGIPQCLGMIMSAIIVRILLQLVPFTRLGS
>gnl|CDD|222820 PHA01082, PHA01082, putative transcription regulator
MLIKLPLLGVLSMNRSEMTKNFVFREFECGLSVEEAAKLCFKTVSEVKQWDAGEKIPPICKRLMRWHSRR
ELYYGDEWWGFRMEGGRLIFPTGDRVAPQQLLAAIAILQIQAPDDAMTRSKLLKYARAMARIK
>gnl|CDD|164851 PHA01083, PHA01083, hypothetical protein
MYTNKLLDAYKKAKNYVQYKQIAHDLGVSPQKISKMRTGVRTYISDEEAIFLAESAGIDPEIALLGCHAD
RNENPRAKAIWESIAKKQNGLGLRTISMLCGGLAVSISQFNEAVSYFALCRLMVKVAINANAYKTSAFGS
FINESKRND
>gnl|CDD|107025 PHA01159, PHA01159, hypothetical protein
MEYLYSALEFIANIGQTFLDFFDVAIDWIKNAFVYGAMWLISVWLDILIASIQIAYKIAQLLLEEYGVYT
MVESRFNALPSDIRYILTEFGVPQALRIIFDAFATALVMRFFNW
>gnl|CDD|107026 PHA01160, PHA01160, nonstructural protein
MARRRYRLPRRRSRRLFSRTALRMHPRNRLRRIMRGGIRF
>gnl|CDD|222821 PHA01327, PHA01327, hypothetical protein
MRTNFEPFTKRNNVINEHGEEWQERKDRMKKRHKTQRGNSEKRNWKEAL
>gnl|CDD|164853 PHA01346, PHA01346, hypothetical protein
MKHVNTLLMQELRLLICELKRLRLSAVSDPDFSQEKIHAELDSLLRKLSRHFD
>gnl|CDD|107029 PHA01351, PHA01351, putative minor structural protein
MFIILKRNILINMSFLGNLGELGTFFADEIENLENFTNWISSDFINFINAIVNDIKNIASFLGQAISDIP
TFMQNIATNFLTILQNFVQTAISTIQGFVSWFEQQIVGAFEFLSSIASDFINSAYSFFQNVANDFAQIIS
GVISDFLNFFGANMKHISNAISQLSQFLSPFIAPITIGKFLPVIVDKLAEILPEFEIDLAPVGLGGKIPI
KFGEIIKAFAETSVDFLNEIRDELATTLKEFIKEPFISDFKISAREIFNEIGLGDLPFADPPFQLIGRWV
AVRSFNEVKDHLKETILLTGYPAWFTDAYLESPVNDFVPQNPLFRPVGIRDLITGVQYGILNISDLEKYA
YNNLITPKTAKLMYQNQTARLLQRVVEQGIRQFVVTPQKAYEEIISNINLTGKELFLKTFTLEYEYAVQR
IVRQFLRSLLSRALSNFGRPYLDFKYLDSTIAKLFKDLGYPEEVRTVFDTMITQSQLIQTNQLLLRQLQQ
IVSLGIFDQKKIKEELKANKFNEQVALQILESELQFAQLQNQLKEYQFKLNNFLISPQDLEKDLKHLGFD
SAIISALIYENQVEQLIKFQLNNIESLAKKGYLSLDEIKKQFKAIGIIKEYEDAFINFYNQELQISAFLT
ILKSQLRQFQIDPKEAETELKKLNINEYLANQIIQEEYNINIAKLQLSVLETIAKTLYYDQQQLSGELKK
IHKDKTALELYITKFYYEYIYPKISNYHLQLARHGILSDISKLPKEVNDYEYKPAVLTYQTTLEIEYIKE
SLKDLEIKPKTAINELEKLGMQKDIAQLIVNTYIPTFYSPHTIIQNIIEGQLYKIGKVPINLGNAESELR
KLGIPDSQIKALLDQYESTFGLDIWRKHLPSLSIIENAIKYNYLDQKLIEYSFIPSELLNLYVNYYQHLL
VGQEVQSFKSEYITALIYNYQNLQLESLLKQYGINEALLSVLKLFAQVRKIVTGLQELYLTPSKALSISE
YVSNPQQLLQKVFAEFQIPQELQNTYFEYARNRRVSRYVNEIITTINLLFEKHKIDLDTAQSYLQQLKKY
GLTDEEIQLIKLNWQLRSAY
>gnl|CDD|107030 PHA01365, PHA01365, hypothetical protein
MTDYKNGIKKLLQKCFKDSSIDVIFMSCNNLSPHKKYMIIDPESKYYIGYILTDGIKIPFIAEVWHNNTT
RIYLDPRKDFYLALLVGDLNV
>gnl|CDD|222822 PHA01366, PHA01366, hypothetical protein
MSSTCYPITSFGTLLNKIAKQSLISSQAWNQIIQDLYTAYSVYKYINTGLQYQTESSDAYGNIVTLLDLF
NNLTLYIVNSKPYYFSPLITANPGLPLTVNYMNNLITAITKLANENNITLAKPLNFVQSNEIVKSRKWND
IIYAINQFLTFDFNLYFLLDCGGSGFDNLYNSLSAFLNVLIDNPSQNISTNNIYIKNLIINYLDTFLNFY
GYSAIDNVLVGNTYVFSEIHLYDNSFIYNLIFYSSYGLIATSDNSYIQNLYVYGDSNEITVYHGVNLYLC
GYENTVVFNGVNLYIIGPNNSTSGSIDNAITENLICKQNYGQIQISGNAQVINNNCQ
>gnl|CDD|133949 PHA01399, PHA01399, membrane protein P6
MGFFKSIKKAIKKVVDAVVKVVKAVVDAIVKAIKAIVKIIKKIVSVILDFISKIFSKIGIILIIILIIIA
AWFFFPAFAAFLQSAWASFVNFFQTAWAWVTKTAGAAWQAISSFASAAWGYIQAAWEWIAGAVAAIWKGA
GAAADAAWEAAKELGSAAGGVIGGIWDFIKDNPELIAGGAAAAWLGKDGLILAGLAVAAFFLLKSSSGGG
GGGKGEQKVTINTMGEAYAPSPYRTGQGAPRA
>gnl|CDD|164854 PHA01474, PHA01474, nonstructural protein
MWRIYESRTTYEYSRFSSFWSCARIILSPWNSFRSFRISWRTETKCDCEANC
>gnl|CDD|107034 PHA01486, PHA01486, nonstructural protein
MSKSLDIRRDLRSIAIRLRKLPASSDQMLQVL
>gnl|CDD|107035 PHA01511, PHA01511, coat protein
MALNEGQIVTLAVDEIIETISAITPMAQKAKKYTPPAASMQRSSNTIWMPVEQESPTQEGWDLTDKATGL
LELNVAVNMGEPDNDFFQLRADDLRDETAYRHRIQSAARKLANNVELKVANMAAEMGSLVITSPDAIGTN
TADAWNFVADAEELMFSRELNRDMGTSYFFNPQDYKKAGYDLTKRDIFGRIPEEAYRDGTIQRQVAGFDD
VLRSPKLPVLTKSTATGITVSGAQSFKPVAWQLDNDGNKVNVDNRFATVTLSATTGLKRGDKISFTGVKF
LGQMAKNVLAQDATFSVVRVVDGTHVEITPKPVALDDVSLSPEQRAYANVNTSLADAMAVNILNVKDART
NVFWADDAIRIVSQPIPANHELFAGMKTTSFSIPDVGLNGIFATQGDISTLSGLCRIALWYGVNATRPEA
IGVGLPGQTA
>gnl|CDD|164855 PHA01513, mnt, Mnt
MGRDDPQFNLRLPYELKEKLKQRAKANGRSLNAELVQIVQDALSKPSPVTGYRDDAERLADEQSELVKKM
VFDTLKDLYKKT
>gnl|CDD|107037 PHA01514, PHA01514, O-antigen conversion protein C
MKFNSNDRIFISIFLGLAIIYTFPLLTHQSFFVDDLGRSLYGGLGWSGNGRPLSDFIFYIINFGTPIIDA
SPLPLMLGIVILALALSCIREKLFGDDYITASLCFMMILANPFFIENLSYRYDSLTMCMSVAISIISSYV
AYQYKPINIIISSILTIAFLSLYQAALNTYAIFLLAFIISDVVKKNSISNITKNTASSVAGLIVGYFAYS
YFIAKRLVTGSYNIEHSKIIEINSSLFEGIISNVLSFYRMFSTILNGDNYLIYYSLFFALIISLIVIVLK
VIKRDENKKTKFLLVVLILLASMFFIIGPMIFLKSPIYAPRVLIGMGGFMFFCCLCVFYAFEDKQLISRI
YFSFILLISTIFSYGAYNAINAQFQLEESIVNRISQDIDHLGFGRDKKNIKFIGTEPYASINENIVIKHP
LMRELIPRIINNNWMWSEVLMQRNVFSRNYRLYDKEVKLENGWKKSGNNVYDIGVVGETIVVRFN
>gnl|CDD|107038 PHA01516, PHA01516, hypothetical protein
MKLRVWHIPQVPMKPFIVEVASVEEGVRVMDALADYDAFQYDNNIKPDYCNANGLQMWDESLTDQDLEEM
ELTDRWVDWYSECQCYDDPREYLESLKE
>gnl|CDD|107039 PHA01519, PHA01519, hypothetical protein
MTMDYSQLSDFEINRMVGDIIFKGLWACKPETSGNNTNKWYYGNADTTFEPLNHLPDYCNDPSASWPIIE
KHRISILDQLTEWCVDAKGVSPIFDTRPLRAAMIVFLMMQDANNA
>gnl|CDD|177311 PHA01547, PHA01547, putative internal virion protein A
AFWLPLLAAGGMSALQQGLANKEERNKIKAQNKARKKADLRNLGAAAQDVSNLGVQAGSYRKQAAKSLQE
AKRMAMLAGGSAAAQAAAAGVKGASVDAVALDIDREVGEALVQIDQNLDAQMYNLANQIRSIQAQAKAGL
LGQKSTTAGQRSPLLAGLMSAGSLYASQYFKFGSFGSTSTTGGTYGQSGVAVAGQAGFRATPKGGN
>gnl|CDD|222823 PHA01548, PHA01548, hypothetical protein
MENNTKQLNNEVNEIAVVMESSNTNDITTVDKVYPSIFEAFGGKKVFFSSIQKKDRKSAIKVYNAINSSE
NALKDHRGEVLEITDMVAHAITLEDEDTKEVVDALRVVLIDKDGKAYHAVSQGVVSSIQKIISIVGPAPW
TDEPLAIVPGEVKTRKGFKTLTLQLQG
>gnl|CDD|164858 PHA01622, PHA01622, CRISPR-associated Cas4-like protein
MNYEDHIKESFKVKYPIDTLFPSEVGICYRKSYLARNIEFERGINEIYLDLGEQYHERIEQYFKEKLNCQ
TEVEIKDEIEGIKISGRIDIVCNNDLLEIKTISYNYFQVKEYHLYQVALYYHILKKQNYQINNVYIVYLN
RNTREVKQFKIDEKVLETYYQKVIEWIKKFKEYLKETDYKKVPGVNNYICKSCEFKQKCIISLF
>gnl|CDD|222824 PHA01623, PHA01623, hypothetical protein
MQTQEQSTEKKQKAVFGIYMDKDLKTRLKVYCAKNNLQLTQAIEEAIKEYLQKREG
>gnl|CDD|222825 PHA01624, PHA01624, hypothetical protein
MEFEDLDVVLYVFFENPEMKSFEFEFKDLFETTEEGYRYLLGVPDSRNKIKSNGEIIEEFIYYQNDDIMY
KLEFYYTKGTNKIYIRKIYGWREKRLENEDEE
>gnl|CDD|164860 PHA01625, PHA01625, hypothetical protein
MEVKQRKKLNNLPKVFLDPYLNKFSLTKNYVNCAYYESRSGLTQEGCVEVSIVGNKIKVDTVKETRGIYY
TPHPSIINLTYRQKMIRDIDDLKQILESLNLSKVSLKTNKLLVKYSNYSIELYDIYFKGGIYEFPLLFSQ
GHLYVYNVPEPREVYLIYYENDNQKEEINKELFEEVSEFMIYNHAITFDKKVLKFKNLYVTPGQGALVYV
PEDVTVKLESPDHNKVEFFVYRDSWLLFSHPRPRRSGRD
>gnl|CDD|222826 PHA01627, PHA01627, DNA binding protein
GMLYLLNAFSLPMKPGEEYTVVIDKIDIEEAKELLENEEFVSAIGHDATANLLSNLCGVNLPKNRIEIKL
DKGDKALAIMLKQRLEEGKVLKTEEELEMIGYEIWVF
>gnl|CDD|164861 PHA01630, PHA01630, putative group 1 glycosyl transferase
IALVRDYPDHSFVRQKKLLEEHLKMLGHKVTVFEKPTLTKYQLPPGYPIYIYYTIFNSMLFWKGIPHVGK
NIVFEVADTDAISHTALYFFRNQPVDEIVVPSQWSKNAFYTSGLKIPQPIYVIPHNLNPRMFEYKPKEKP
HPCVLAILPHSWDRKGGDIVVKIFHELQNEGYDFYFLIKSSNMLDPRLFGLNGVKTPLPDDDIYSLFAGC
DILFYPVRGGAFEIPVIEALALGLDVVVTEKGAWSEWVLSNLDVYWIKSGRKPKLWYTNPIHVGYFLDPD
IEDAYQKLLEALANWTPEKKKENLEGRAILYRENYSYNAIAKMWEKILEKY
>gnl|CDD|164862 PHA01631, PHA01631, hypothetical protein
MKIFTFVGFTKHLDELDFDYVVVDKTFNDMTECQIPKYQEKIIWIMTNTEIRWLRIAKQLLTIVNFAKNI
EDDIIAIIDSDLIIPNLREIIPNERVFTPCYWLYYDWANEIRPFCSGTNYIFRKSLLPYLEYTINTYIEN
EYYKEIPVDIFIHNFIPHMNILKLGTIHYVKTPMEK
>gnl|CDD|133953 PHA01632, PHA01632, hypothetical protein
MISYQYDEKNKTLHIKIYILIEQVPQKPTEEELRKVLPKILKDYANMIENGKIKILDSKEWGIW
>gnl|CDD|107050 PHA01633, PHA01633, putative glycosyl transferase group 1
MKTAILTMNYSSISNVSEDIAEVLRENGEIVTITKNPFYIPKAEKLIVFIPFHPPSLNPYLYAYYQFKGK
KYFYTTCDGIPNIEIVNKYLLQDVKFIPNSKFSAENLQEVGLQVDLPVFHGINFKIVENAEKLVPQLKQK
LDKDFPDTIKFGIVSGLTKRKNMDLMLQVFNELNTKYPDIAKKIHFFVISHKQFTQLEVPANVHFVAEFG
HNSREYIFAFYGAMDFTIVPSGTEGFGMPVLESMAMGTPVIHQLMPPLDEFTSWQWNLLIKSSKVEEYYD
KEHGQKWKIHKFQIEDMANAIILAFELQDREERSMKLKELAKKYDIRNLYTRFLE
>gnl|CDD|133954 PHA01634, PHA01634, hypothetical protein
MSIEEYFRKLECDYWREYPHAYGMLNVYQRTIQIVGADCGSSALYFLLRGASFVVQYEKEEKLRKKWEEV
CAYFNICDKAVMKGEWNGEYEDVDIFVMDCEGCEEKLNVSMLKKYKQWCIGIHDWTKNRVELMRKMEGAT
FTYVSDDGREITLCKI
>gnl|CDD|222827 PHA01635, PHA01635, hypothetical protein
MRHLRADPKSIKVVSSIPQGATKLWENNELALYYTYGGSYGEVIWIFVNKTSDRKYVSLLRGAELNINGQ
QVTVPDYIFGNAFADVYFANGASTYINDLNDIPLYSLAVLNPPSRYTIGFVFSLPPNSVIHVPEYGFVNL
VSLSGRLIEVKPGSLNLYAIIYDYAEVVEYEQEAGINVASPPDPYAVFSYQFSIDELGYGVTPRVILEIP
QSDVNIANDLINFFKKIASLF
>gnl|CDD|107053 PHA01707, dut, 2'-deoxyuridine 5'-triphosphatase
MILSDRDIKYYINKGWLVIEPLSEDTIRENGVDLKIGNEIVRIKENMEKEVGDEFIIYPHEHVLLTTKEY
IKLPNDIIAFCNLRSTFARKGLLIPPTIVDAGFEGQLTIELVGSSIPVKLKSGERFLHLIFARTLTPVEK
PYNGKYQKQKGVTLAKED
>gnl|CDD|222828 PHA01732, PHA01732, proline-rich protein
MCIFRAPKPPEPPAPLPPAPVPPPPPAPPAPVPEPTVKPVNAEAPKIREAQSKRGQKQQKAGGTASLRIP
KQSGTQGSISAGGTSKTGGLNIPT
>gnl|CDD|107055 PHA01733, PHA01733, hypothetical protein
MSDNNRPATQADATEVAQNLRQEDREEIEGLGHSPLALHLSLDVSENVVAFVAPDGSLAGVAGLVEDMGN
RVGEIWMVCTPAIEKNPIALLRGAKWWLPKSRNYDLLWNIVDKRNLVHRKLLRKLGFKGLRYVQPGPLYL
PFIEFVKKCASSC
>gnl|CDD|222829 PHA01735, PHA01735, hypothetical protein
MAKRATEEQFDELHQLLTNELLSRIKSGEATTADLRAACDWLKSNDITGVAVDGSPLAKLAGLMPQLTFE
DVQERL
>gnl|CDD|133956 PHA01740, PHA01740, putative single-stranded DNA-binding protein
MAQYDNTNRGTLGKNRQPKNDKSPHFTGKVDIRGTVYWLAGWRQEDFMSDDHYISLSLTGKDDASLTGSG
RLENNRDKIGNRPDMVGRVIVEGAEYEISAWTKTHDNGKFLSIQVRAAGVRRPQDDKQFGTAYGDSHEDG
TRPKYNEPPMDFDDDIPF
>gnl|CDD|222830 PHA01745, PHA01745, hypothetical protein
MKIVFGIVSSQDLLIKINFPILINQLVNKKITWKNETWVDSGGYQIMLYNLKISVDDVLDKYKTYNAYAF
FSLDIPSIFEPLSRKNFEYFEYLYTKLEYIERIIPVIHLYPVREVDEAIDFYSQYTDYIAFGGIVASSKL
KILIYAFPWYYYIRKYVKRLHVLGMSAPYFRQVFYDADSMDTSTYTVKAIHREIFWFDGTRRYVGERKAR
TLTKEEEESLKEFLDKTNFPFPYDVSNWKILSLVNAWILKYNNWNIDNKYTIYAHKLRKMGLDSLVNEII
QNYKIANELKKEKQQNKKKNSIELEE
>gnl|CDD|107059 PHA01746, PHA01746, hypothetical protein
MASLKDIIDELKDQAKESNKIASRILKIKGIKRIVVQLNAVPQDGKIRYSMTIHSQNNFRKQIGITPQDA
GDLKLIAEFLEKYSDFLNEYVKFTPRNNNAIQEEEDDMEQQEEKEEKGREKGRKKNVEEEF
>gnl|CDD|222831 PHA01747, PHA01747, putative ATP-dependent protease
MTQLQEYLVSISFFYNPRDGERPLELILGLKGTEKDKLKAMRLGADNPYFLAKACYRGEAKFISKISSFK
LKDYLSATKFQNGFTGGLDPHELAESVDDFYDILNSYLYVSVVKKSNLWFVTDIEPIEPKNNVEIAEELL
EVADAEHVTYDDLLAAFGYDTDKMIRNDAVNRLTLPRLLPLFTSPVSKRPVHIIELSNRGTGKTTTFVIL
QELFNFRYYTEPPTYANLVYDAKTNALGLVFLSNGLIFDEIQTWKDSNMRAINSTLSTGMENCVWTRGAG
TESDAATIVRCIPIIFAGNPDSSTLDTYQTPNYIKNYLVSYELFQSLTKAILDRIAIIIVNEKKITYDDI
ISGRVLYPTILRGLISLVQSKINRMTKDLDCGNGESRRNEQAIDVLCVLQALDVDLDNFEVCDEFAKSVR
SGFLV
>gnl|CDD|222832 PHA01748, PHA01748, hypothetical protein
MMKVITFKIEEDLLELLDRYAIKHGLNRSEAIRKAIEKMVKDELKKETVPVAKVEKISLW
>gnl|CDD|177316 PHA01749, PHA01749, coat protein
MAKGHTPRSYSQRYAKWQAKFNAFSNPTVASTILSNVSPVAQQNFQTNVPKFTSVNENVSAVLTQYGITG
PNRAIYQGFGLKVARALNRIGSGPALVNMINGLKAYYISAFNANPQVLDAVVNIITGSPTGYVS
>gnl|CDD|107063 PHA01750, PHA01750, hypothetical protein
MSETVLVLTLMSTTATTLFAIIQLYLKIKQALKDAVKEIVNSELDNLKTEIEELKIKQDELSRQVEEIKR
KLDKK
>gnl|CDD|222833 PHA01751, PHA01751, hypothetical protein
MRIEDPFQNIFGVVRIAIDKIRELEQRGQIYGLSRFLPNSIIVMKTIDYPLIVDLYIPGFTFYFQFSIIQ
DQQTKQIFIDDFRVVYPQPYAKQINSTANFELSEEEGEDE
>gnl|CDD|177317 PHA01752, PHA01752, hypothetical protein
MILYDIYIHYAICEFIFLLEIYKLIAMGKRKGQRNIAAMKYHLYNKILNRKSFPAFSVMFDAGVESVLPT
PLENIQIPLGINTNYGIAYASIISSLLSALNNLAISVFNPNFNSQTFLNLGQSANFGISNGINLLNNYTS
LYDNYVELCNILYQPAVFDETYFDLSVYQPALATEYQNQSCGKIEQYFSSLTTTNVSVDITTLGIGITNI
PNVDNYMYNNIADTGIIDLLNALNINFNQLPDFAKFIIAFIPDLNSIINNGFALDVAWLDRCVLAPETEN
GIQLQNGMILQYFADVFGMILDYTPLDFAVLMPDFNPENVTQDDLIAILSADKTVISIFGNLFKMHLYDP
SPGGINIAYSSEIENYAVSYEQFLQIQKIVNKKYSNIWYAKMIASATIEIARYPYQQNYSYTSGKRTLPY
QDFLNYWKTKWKFYGLTDQDLQFAQQLGEQLQGQAKIENQIKLAQKSAKTKQYKPIFYYKNFQNIANR
>gnl|CDD|133958 PHA01753, PHA01753, Holliday junction resolvase
MNIRQSGKYYEYKTLEILESNGFKALRIPVSGTGKQALPDIIATKNNTIYPIEVKSTSKDVVTVDKFQIE
KLFRFCEIFSFCECKPLVMVRYKKYKQVIVYELTQDVRIKEKIKFKYGINS
>gnl|CDD|133959 PHA01754, PHA01754, hypothetical protein
MSEQKKISNLNTELTAKLYLALDDLTMALATEDKEEVRKSEVFQKALEVVKVVKEMRRLQVKPVEGEEK
>gnl|CDD|222834 PHA01755, PHA01755, hypothetical protein
MPLPYKVNYKLPLEYLSLQDWNNFVQNLIFINQYGTVKLLQYYNNGSFQNLNDVFAKYLYVWQLKVNGYN
VLYNLKPPLAYTFGNVFQELANKPKIVSPELYVPLSSINYKLPLVEKQIEALIPNLISKITIPNLIAGTQ
FTFSGSSNLASLTSQYFQSSYLQTWRSITLQNLGNSSVQINNSIYLMPKQCLKITVSNPQEVQISAQSST
LLSELIEFYVIPITAYTITITNSQPDPTPSPFQQLLILNLSNIISSPSQLLNLQFCLDSQCSTPLYAWIE
SYNSNLSTVYIWINLPISIPANSSITIYMFVRNSIQYPYTGMRPDLTSTYAQYDNGKNVFLIYFNGNEPL
SNFNQEGNTIQQISTFGPLGNTINAIYLSGYENNVGFVYTGKSETNQPVISEASSQRMPNQTGGLGAYNG
TAGIADSTNTAFINDIGVTMGEDTSYFSQYYYVNGGETGGSNYQGSAVSQWVYAWVQYQGSSASSWFGCI
APQLYSSPGGYCGTQNVNPLSSSTQLYLDVIGTVSSSNTWQTAWNFMRMRAYPPNGVMPSNTNPQLTTIY
VA
>gnl|CDD|107069 PHA01756, PHA01756, hypothetical protein
MSVTYTSISSLLASPFQRLTSSMWNTVVLLLYQLYETGGNIDRKILQNGNLYIPNNISALTGFFQKEVYV
SGQPVLTEQDPIYIAGFIGTANQQINQILYSNQQLYYSISNLPKEISYDLYVNLYRTISSLTSGLSSQIQ
QLQKTGINALYSIADFLAYTFTYFYLATVGLANTLNKLTLFLSPPTIEGLQISLSTSPSPIYSGSTLETV
RIILQNLSNYIVYIGNSLYNSFPILPGDSLEFHVRNPSNVYAWATGKCTVYALFEVVQ
>gnl|CDD|222835 PHA01757, PHA01757, hypothetical protein
MAITLLEGALYGFFAVTGALSASFIIGEIVHLYNEKQRNENFAKAIDQMSKSTVVATESIKDTTVTGINA
LLNMDTLRDVNDLAREKAKDQNPQKQAK
>gnl|CDD|222836 PHA01769, PHA01769, hypothetical protein
MAIRQHVRCRECTRRRALPKVLTLYLRVPRCDCGARNWRPDKWMNQRDTGATRCDCAGYWFPHRRGCLYC
HYRRDGTMRMFGDYDFADRNYDPELGWT
>gnl|CDD|177318 PHA01782, PHA01782, hypothetical protein
MTNAISKTVIAFRGAKEINRAIDAIAVRGKELDEAIQLTGLSILNHVDEHGDVTVAKKLYEAMPKGSRRN
ALAEWLVKFGKVQVNTDKKSAKEFPFVYNKFGKTDLEGATAKPWYKFKPEKALDQEFDLAAALAALKKQV
LQAQTKGKVIVGDELLGDLERLAAKAAPIAEQAKRAA
>gnl|CDD|164869 PHA01790, PHA01790, streptodornase
MSKKLRNSLARIVVAAFASFAVMAIPTYHHSTVLAKTVSVNQTYGEYKDYYTVIGESNIDQSAFPKIYKT
TERVYKGQGTSEKRVTVSDVVYNPLDGYKRSTGAYGVVTKDMIDMSKGYREKWETNPEPSGWFRFYNRAD
NEEISEKEYDSRRTKSYKVTNNVPVVLTTLKGKQYNSHLFVRSHLFADSLGGKSIRKNAITGTQMQNVGT
RKGGMQYIEKKVLSHITKNPDVYVFCSAIPEYQGTELLARSVLVSALSSDGVINETVRVFNTADGFNINY
EKGGLLTESPVSEIDNIEDSTTDEIENSVDDSEEIVYNDTTTEEEE
>gnl|CDD|222837 PHA01794, PHA01794, hypothetical protein
TLFKANNKLGTINPEGERNADGAGALFFNILERDESAIVDLVRLSAKKALTEDEILDAIADFVETFEDEE
GTTEGLFAELEKEMVDSGFFRAKIKKYIENMEKSARYLKAKDDTEATQAKAIKDLIGRMKKAVS
>gnl|CDD|177320 PHA01795, PHA01795, hypothetical protein
MDLLIEKESQATRLSDFGIYNIAIEDSAPLLSVSHRAVKGRSGYIYDGATFTTKTLKVKGRVTVSNVEQD
LDKQDELNALLVVDEPFYVTKMYPENSDLFNFELPGESTGDLQLIGSPHKPWKYRFKVILDDTINYEFIG
KTSQGLKYNLSFTLRTAELPFGETKPKDITLSGGSFAYRGTAKASQLEWPFIIELTPSGGQTNFYIEIDG
RRFEFKQNSQLQNSDKLLLTGIATTLNGNYVNAKTNYEYFIFNPNPNKRITYKTDFLGTIRILNFVELYK
>gnl|CDD|222838 PHA01806, PHA01806, hypothetical protein
MQAKHSDLLEGTKEIPEGLIAKALLLRLYSDARHSEGVALAGGAARDLMHGAEPKDIDIALYGMDDRQAE
LLIGCILPKLVSRFLRDGGWSQEYHDGGDGGIFKGVVSLKGCRGLEGMDVDFNYYDTDSVGEVMESFDYT
INQVGIAYNWPDPEGGPRLGAYLHKDVTWGVNKELRAGSRLPERAEKMRAKAAYYGWENN
>gnl|CDD|222839 PHA01807, PHA01807, hypothetical protein
MKSIWRVHAKAGTPSELQGLCWLAIQELEEFTLFRSKEEALERILDSTESNDRTELLVFRDGKLAGIAVL
VFEDDPHVGPCLGVQWQYVLPEYRNAGVAREFLRELIRLAGEGNLPLIAFSHREGEGRYTIHYRRVKPYG
QESQEGAGQDHHR
>gnl|CDD|164872 PHA01808, PHA01808, putative structural protein
MGKKVKKVLGKTIIGKLADGLLGTDLSGAQSDARNMEEQNRLMQQQADQLARNQQVDLTAENVAQVDLGA
MADATGTGTRRRRNQAGTGVSQTLGINY
>gnl|CDD|107079 PHA01809, PHA01809, hypothetical protein
MENETKNIELKHVFRFKNGSLCIALFDRTENEISFYDVDIDEIEDLNHNSVLRVISTLLGSDNNG
>gnl|CDD|177323 PHA01810, PHA01810, hypothetical protein
MVNVDNAPEEKGQAYTEMLQLFNKLIQWNPAYTFDNAINLVSACQQLLLNYNSSVVQFLNDELNNETKPE
SILSYIAGDDPIEQWNMHKGFYETYNVYVF
>gnl|CDD|177324 PHA01811, PHA01811, hypothetical protein
MKVDDIVTLRVKGYILHYLDDDNEYIEEFIPLHEYHLTKTQAKELLPDTCTLLSTTRTTKTIQVYYNDLL
QISIAESK
>gnl|CDD|177325 PHA01812, PHA01812, hypothetical protein
MTNVKDILSRHQNTLARFEFEEKEREFIKLSELVEKYGMKKEYIVRALFTNKESKFGEQGVIVTDDYNVN
LPNHLTELIKEMRADEDVVDIINAGEVQFTIYEYENKKGQKGYSINFGQVSF
>gnl|CDD|107083 PHA01813, PHA01813, hypothetical protein
MERKYKTVLLYCDEIKGHFPHQISMFEDLYDAKVVYSYYEYNLFTKKYAYIIEYIKEI
>gnl|CDD|107084 PHA01814, PHA01814, hypothetical protein
MKITTTLRTKKLINYILTNRDCFMNKITKFTSLSKKCVVFVNYGDISIEYYDDDTKNENDLFTLDIDIDI
KKHVFNCLKVYYIEHTEDINIIYKKGVYMGCTIDDVLSNFEKPLESDITIIYQNKVIYDNGKVIDHE
>gnl|CDD|107085 PHA01815, PHA01815, hypothetical protein
MNNLLNIAIVFLLAFLITLIILMTLHIRVSFGVLFTTLIIFYIIFLMVIYALYGG
>gnl|CDD|107086 PHA01816, PHA01816, hypothetical protein
MVRHTSEMDRWKKEREARKEQEKDLFLNDFSNVNFKFDDKDLQEAYIDTWKHFAHLPYFPKERNVSYVNA
VSLVRGSRHKKLNYILEIYNRNDDSNNKNAKKHKYALYNLQAKNNNSSMYKYIKEIDTLYKEIGKSDRPV
TNIDDEDVRYNFLYYATFDE
>gnl|CDD|177326 PHA01817, PHA01817, hypothetical protein
MNDQEKIDKFTHSYINDDFGLTIDQLVPKVKGYGRFNVWLGGNESKIRQVLKAVKEIGVSPTLFAVYEKN
EGFSSGLGWLNHTSARGDYLTDAKFIARKLVSQSKQAGQPSWYDAGNIVHFVPQDVQRKGNADFAKNMKA
GTIGRAYIPLTAAATWAAYYPLGLKASYNKVQNYGNPFLDGANTILAWGGKLDGKGGSPSDSSDSGSSGD
SGSSLLALAKQAMQELLKKVQDALQWDVHSIGSDKFFSNDYFTLQKTFNNTYHIKMTIGLLDSLKKLIDS
VQVDSGGSSSNPTDDDGDHKAISGKSVKPNGKSGRVIGGNWTYAQLPEKYKKAIGVPLFKKEYLYKPGNI
FPQTGNAGQCTELTWAYMSQLHGKRQPTDDGQITNGQRVWYVYKKLGAKTTHNPTVGYGFSSKPPYLQAT
AYGIGHTGVVVAVFDDGSFLVANYNVPPYVAPSRVVLYTLINGVPNNAGDNIVFFSGIA
>gnl|CDD|107088 PHA01818, PHA01818, hypothetical protein
MALNFTTITENNVIRDLTTQVNNIGEELTKERNIFDITDDLVYNFNKSQKIKLTDDKGLTKSYGNITALR
DIKEPGYYYIGARTLATLLDRPDMESLDVVLHVVPLDTSSKVVQHLYTLSTNNNQIKMLYRFVSGNSSSE
WQFIQGLPSNKNAVISGTNILDIASPGVYFVMGMTGGMPSGVSSGFLDLSVDANDNRLARLTDAETGKEY
TSIKKPTGTYTAWKKEFEPKDMEKYLLSSIRDDGSASFPLLVYTSDSKTFQQAIIDHIDRTGQTTFTFYV
QGGVSGSPMSNSCRGLFMSDTPNTSSLHGVYNAIGTDGRNVTGSVVGSNWTSPKTSPSHKELWTGAQSFL
STGTTENLSDDISNYSYVEVYTTHKTTEKTKGNDNTGTICHKFYLDGSGTYVCSGTFVSGDRTDTKPPIT
EFYRVGVSFKGSTWTLVDSAVQNSKTQYVTRIIGINMP
>gnl|CDD|107089 PHA01819, PHA01819, hypothetical protein
MTEFDEIVKPDDKEETSESTEENLESTEETSESTEESTEESTEDKTVETIEEENENKLEPTTTDEDSSKF
DPVVLEQRIASLEQQVTTFLSSQMQQPQQVQQTQPDVTESDKEDNDYSDEELVDKLDLD
>gnl|CDD|222840 PHA01886, PHA01886, TM2 domain-containing protein
MKSTAIAYVLWFFLGFFGIHRFYTGNIATGIIWLFTGGLFGIGWFIDLFLTAGLVQSSNVRWRLEQAEMN
FAIKNRGY
>gnl|CDD|177328 PHA01929, PHA01929, putative scaffolding protein
TTQNEQQLPPGLAGLVANVPPAAAPTPQPNPVIQPQAPVQPGQPGAPQQLAIPTQQPQPVPTSAMTPHVV
QQAPAQPAPAAPPAAGAALPEALEVPPPPAFTPNGEIVGTLAGNLEGDPQLAPSVSYLEAFSGLDKLDTV
RAFGKAAENRDPRFIDTHYLKEVLGEAQAQHVINVAKGVLTYVDAQTKAVVNETYAAVGGEAVWKQAAGL
FNQKADPATRAAIGRLMNSGDAQAMQYAAKQVAAFAQGSGAVVQATGQPLGAAAPALAALSAAEYRAEVS
KLPLNASEADMAALRERRKAGKAQGL
>gnl|CDD|222841 PHA01971, PHA01971, hypothetical protein
MSDKQIEKEIQAKGLTAPRITPQHIESIIASEHYFTAADGVEGANLYCTHADGETTNGPLEALSLLTFCV
LVLRNGFTVTGESACASPENFDAEIGRKIARENAVNKIWMLEGYLLKQKLSEQ
>gnl|CDD|222842 PHA01972, PHA01972, structural protein
MPQKCVEAVAQAAGRQLTADEIKGIEDRIKEAMRSVARKDPKGWKEESIAKRFYKTDADLARQELVHDAI
KKKKRVALAIAKQAEATKKINEVLTADKDPAAALLGMLSRDPNEEAKFLSVEQRINATRDVSKAKISDFM
AALDPTTRQIFAGIATGERRFDKAQQRLLDDIVHELYGRQTGNADAKKAAKGWKKVTEDLRARFNDAGGD
IGELDDWRLPQKHNRMKISKAGADAWVDDVWDLLDRSKYVKKDGKPMNDAELREALYSVYNTIATDGMNK
IDPGSKTGSGARANRGSAERVIHFKDADSHLQYQREFGDTSVYASMVGHLDGMSRDIGLVETFGPDPDRN
FNTLLDAVKTKKGTTSRQPTGAMKMVEPTFNMLMGYNMVEENPVWGRRVAGLRNLWTASKLGAAVLSALS
DSGTMSMAASYNAMPPARLLRNMLSEMMPGSKSEASRAQDFGLGAESLLDRVNRWGTDNLGGHRSRNLAE
AVMKVSGLTAWTDAARAAFQFEMMTALGEAADSDWSDLPESDRRILGRKGITESDWAIIAAAPRTNYGGA
KMLTPDAIYAVPRNMDAEAQTKLLGMVDGETMMAVPTPDARTRAIMAGGTKSGTFGGELHRSFFLFKSFP
IATIMRHWRRAFTGKGYPGAFDRMAYAAIMVASTTLLGAGSIQAKDLLNGKDPRSMTDPKFWIEALLKGG
SFGYYGDFLRNAHTGYGSDMTSYIGGPVLSYGDQLTKWVAMNPQDAAQGKAESAGADLLKFATQQTPFAN
LWYTKAATDRLIMDQLQELSSPGYDKKQLNRSRREFNQTYWWSPGIGTPQRIPSLFEA
>gnl|CDD|177330 PHA01976, PHA01976, helix-turn-helix protein
MSFAIQLIKARNARAWSAPELSRRAGVRHSLIYDFEADKRLPNLKTLLRLADALGVTLDWLCGRCGE
>gnl|CDD|177331 PHA02004, PHA02004, capsid protein
MSFLNDLTRPNWAGANADVDIHLEEHLGIVDKHFAYTSKFAPLMNIRSLRGSNTVRIDRLGNVEVKGRRA
GEELERSRVVNDKWNLTVDTVLYLRHQFDHQDEWTQSFDMRKEVAELDGQELARKFDQACLIQLIKAAAM
DAPAHLEPAFSDGVLEKATLTGLTAKAEANADKIVRAHRRGVETLIKRDLGDAVYSEGLTLVSPRIFSLL
LEHDKLMNVEFQATGATNDYVKSRVAILNGVKVVETPRFPTKAIAAHPLGRHFNVSAEEAERQMATFLPS
KTLITAQVHPVTAKLWEDEKEFSWVLDTFQMYNIGQRRPDTAAVIELTGIGA
>gnl|CDD|222843 PHA02030, PHA02030, hypothetical protein
MTQQLNALQALLALANAAAETATVDMSETSTGGGGGRILPAGTAMGRFCIYIELGKHAKEFQGKLKPPAP
NVRLGFALWGDVNPQAGNPQSRPDDLFHTYEADGNGKPGLIRTFEMTLGNNEKSKTKLAFDKMNWSGQHK
HFAQMLGQAFIIPIKRTKKGNNAGKERNDIDWGGILPPFDPVDGSPYNVPELDDDLLQLFLWDAPTKETW
DALHIEGTSDNGKSKNFLQETIRKATDFPGSALHILLGGGEDLIIKPKSKAAGSNLPAVPNVAADAGSAA
APAVPAAAAAVAQAAPSVPQVPNVAVLPDVPQVAPVAAPAAPEVPAVPVVPAAPQV
>gnl|CDD|222844 PHA02031, PHA02031, putative DnaG-like primase
MALMDDPWLRQAQRLAVGQTGRFRHCCGGGAAMTLYNNPDRWVAYCYRCKEGGKVEKTHVRRVQCADQER
FMPWPEDASDISQADAYQSLYGLLLSKGIDPNMMEPGLPLEYSERQGRLIFRTDAGWLGRATADQQPKWV
GYGYPAPDYVGWPPELSMPRPVVLTEDYLSALKVRWACNKPEVFAVALLGTRLRDRLAAILLQQTCPRVL
IFLDGDPAGVDGSAGAMRRLRPLLIEGQVIITPDGFDPKDLEREQIRELLIGRIDA
>gnl|CDD|222845 PHA02046, PHA02046, hypothetical protein
KKQAASAERLGELHELVCTAIEREFKWYRENDIPLPAADKAAIAKFLKDNEITCDPADTINIDRLREEFR
QAQAENRRIALEGFIAGLTDDDMERLYGH
>gnl|CDD|222846 PHA02047, PHA02047, phage lambda Rz1-like protein
MRRTIVAILVLVVVALGASYGFVQSYRALGIAHEEAKRQTARLEALEVRYATLQRHVQAVEARTNTQRQE
VDRALDQNRPWADRPVPPAVVDSLCKRLRCA
>gnl|CDD|177336 PHA02053, PHA02053, hypothetical protein
MNEIIDELMYQYRERCWSGRITEPKAKAIIEKYASKTKQQDTSNKLLNSLMILKLLIASGDDMPIDANTA
TEFQKAYRSWGVIYSRSLGSYDSVMWNLMHLDKLIWEVLSEEGIK
>gnl|CDD|177337 PHA02054, PHA02054, hypothetical protein
MPKIIAAVALLVATVHLVSANPEVGSYDEFMQGAMIVYTNDIVHSKDNSVQFLEYLDTKWGSVGCSDTCF
QLGYQEAKLFVAYNTEVQNGNKIQ
>gnl|CDD|177338 PHA02057, PHA02057, ADP-ribosylation superfamily-like protein
MFELDNIIKVEISDCVYQKKKSPSIGKLSEEAEPDYSNFTIDTINAPITLKEFIWAWSKCGSGAWLLGHM
PWMNLELGSYEQVRMIFDYHSDSQYHDTCVNIIHSCNRVLEERYSDSRSTVGSIEFDDHIHNYCDEGFAS
VAAGLRSGTFDSGSAGIFAKQCVEVMDRYMDDSIEFRKSVWRGMSMPVASYEQFRNNGSILFKNFVSTSI
APIMYNHGIVECRNLHINKPTQVVRYNGDFPNRQIKINMHIDCSGIKHIVPAKITGYPEECEIILDRNTV
IVIDEVFEYLDHPNSSTAKCLIRAKALPLSQFNGPTLVV
>gnl|CDD|164889 PHA02067, PHA02067, hypothetical protein
MKFLSVIALGLLSSSAMAASFDCNTTGLNSIEKAICKVPELSMMDQQLADAYKVVRHIPEVKADQKTFIK
DRNSAPSLGDLKDLMRDRIIELEIIAELEGVEAKPYSERQVKPAKPIGSSSVGQLITQFKNGNTAVYNGQ
YLDATYRRSDAPSWALGCSAKIVDNDVLPKWAAEASKNKLSSEFADVRWKFDVAMFNATLDNLLKNTDQS
KTMCDIINVGM
>gnl|CDD|177339 PHA02078, PHA02078, hypothetical protein
MGRYSLEEYYKENFALMQHHKYSLHELENMMPWEREIYAALLIQYIQEKNKKQQ
>gnl|CDD|164890 PHA02085, PHA02085, hypothetical protein
MKIRFKSEEHKAMFARRHDCNQWIADKMGTDWWECEYDADVYDDEASILILDEDVPLTGKYHAADDEDDD
DTAWVLFGERQYFEIVE
>gnl|CDD|107108 PHA02086, PHA02086, hypothetical protein
MTLYEELNNALERVCRINIRFMGDQQHADELTENVSGPLERLRIGQASRRDMGVLCASGIVHEANLFGAN
IPNVIDEMIEKMKAEVQY
>gnl|CDD|107109 PHA02087, PHA02087, hypothetical protein
MKIVRVKFKSPEHRKAFAESEWYNEEFEKFMPDEFWAKFDPNKLVQYMLVDSDGVKIELPESEGGGGITF
DDEEMFHFFDEVK
>gnl|CDD|107110 PHA02088, PHA02088, hypothetical protein
MFQIIFIAGLVLGLIACCFSTWDSRWRKKARNEQAKINTWLAKYGISMNFKNGVVGAFEKVVFFMPGGDN
AIFSECKGINFRKAYKMLEQIRKDDIANPDFDQTGNLMSILYLSQAKIEKTIWDK
>gnl|CDD|177340 PHA02090, PHA02090, hypothetical protein
MKIKMKLNVLPEYHAEYCKTQGQRLWASILELKSKEGDLRVIEVMEDGGWKTNAEFLGYAIGIPVNEQKF
FEEQFEVNV
>gnl|CDD|177341 PHA02091, PHA02091, hypothetical protein
MKIRLIDEKGFIDHCRKNIVDYKLARSIVDFAKTRELQIIQRDRGMWTLNVYGPLGKAQICRDQQKFFEV
NQ
>gnl|CDD|177342 PHA02092, PHA02092, hypothetical protein
MCRPNYRLLLAEEKSHGVEKELYELYTSMNAIGANNQDTFGKLFKTKAYKLAQTEIAEYNEKIRKVILKN
FPTSTRYQSELIGLRGIVDVSMKRGQRILIKLSYGELK
>gnl|CDD|177343 PHA02094, PHA02094, hypothetical protein
MIYEHFDKNSFWGSILIDGMKLNNKLSNTIMLPSTRKKLNEKYEFFAKSVGAMIGELHPTAKTWVAKPNP
FRDGVLVEIRE
>gnl|CDD|107115 PHA02095, PHA02095, hypothetical protein
RIAAFRKGGTNPVLLNFFSMTEGVIQNGYVENGSWEFSRVDGILCIEGDKEHPMPDFEHIVEVPDEMAGD
YNEIISWAEKQLEL
>gnl|CDD|107116 PHA02096, PHA02096, hypothetical protein
MKKYALQWKDPEGFCHFVSGNLHGAFGGVMFHDSWEEADVSLKNAKKSIEEYLKGTTVIKKRLFGPPTIV
SVNKPSGHLANMHKRMYDTMHIAEINIMPKQMR
>gnl|CDD|177344 PHA02097, PHA02097, hypothetical protein
MWKELDRDSQVVTSAMNTPGGVIIRIAHTFDVSNFKIQFIAGVKVVKDANYNGFELVHG
>gnl|CDD|107118 PHA02098, PHA02098, hypothetical protein
MKSDLYKRGYKWANKAYQDGDTLQDIEDKADNSFDFNDFDRGALDAVHDLRKENKT
>gnl|CDD|107119 PHA02099, PHA02099, hypothetical protein
MEFKIIVKSSAKGPVDQYIANLKNAGRVGPGESEMHILRNFEGVDIVFHAEGYNPDLYAELKRHVCYIVN
TVKTPTGASVIGWF
>gnl|CDD|107120 PHA02100, PHA02100, hypothetical protein
MSNQFIAVRNFTVHTCAAKFATDNILGNRISEEQIDAVENEVWEAATAAGVTGIGRQAIRSVIVQYISEE
FGTQALGHTPTHIGPKTMAEDAYKKYQGKARKIRQEIYGSKK
>gnl|CDD|177345 PHA02101, PHA02101, hypothetical protein
MMFTEAKCIVNRPRPVFNGKEYEGTSVGQMLKLIHVLHGPGDSYDVEYREMVENGHVKTRVGLASYEWIL
ARAFTPGVELTKVKPSEVTMSRWCSMDQWRH
>gnl|CDD|222847 PHA02102, PHA02102, hypothetical protein
MARSNELVEKALELQKLLKEVKDLASEQDYGVEINDDNEVRFEDWLSSSCYGEGGEAFVARSDGSVWMPS
SC
>gnl|CDD|222848 PHA02103, PHA02103, hypothetical protein
MQRLTLKFTPFKPKDDRNTFMVKMHFSDKFSDATLEYEIPAIDADRTKAEIVRLITFMDKCKAEYPRGKG
GQADFNHIPDYYRYFGEEAEGVELWEEYGVEGLCWPCHECDYPKNFKGYEIIYTGPDGNKFKVTR
>gnl|CDD|177347 PHA02104, PHA02104, hypothetical protein
MNMDINDYAKEFTREIGRNIHVNLLSTDPEQVKSTIFWTFPGITEVRIGSSTYFAQNGKIYNATIDYNAK
RVIMAGEANAEINTEIYTV
>gnl|CDD|133990 PHA02105, PHA02105, hypothetical protein
MQIKLTKEDWESAKYQNDQNEYPVELELFDQLKTVFSIPQIKYVYLSYEEFNSIMPFIPRRSGFSHVR
>gnl|CDD|177348 PHA02106, PHA02106, hypothetical protein
MNRIKELFDKAVKWYEQEWYYGKWIVSGNADSYLVKYLTFDGEFGLVPSFYSQYYDGHKLNRLRLFVVSI
EWGHVVYSKNQWEKEMKCKSN
>gnl|CDD|164900 PHA02107, PHA02107, hypothetical protein
MTKHKDLNRFLKNTHDTTGNKYRKSRDLNSRFADKHHFMRLLNNLLPSEMKWSSFGSRFGIAKISPNHIN
LAAVGTHSVCGTIWVNTSFESDCVTNRLQTLEAYGVFVEVARRTNGSNHVVTFSVDLPNGDKAPVKNVET
KTEVVSTVDYTEPAKEPDGQNIFFAPETMKAVQLVRGVFHFASVRISEIDEEIKELQARRKEIEDNIKSI
KNAIGA
>gnl|CDD|177349 PHA02108, PHA02108, hypothetical protein
MSTKNIVINIGYIASFGLFYAMYKGDAYFVLGCAAAVIGSTIIARLIK
>gnl|CDD|222849 PHA02109, PHA02109, hypothetical protein
MSSGKAIARTIKKHERRRFNDIAAIRNVLNSMTDPRLDCIHTRTVLRIMGVSGEKTQWPTHQFGSRFLPV
WFWTKVDRVMKETLLHPRGSVVETEYHYHAAKATVREIKLSLNDDAVKIARLLGIEIFSTNWAHYHNLAV
LTRTRRIETIEKKTRVRPAKPKAVEIHASTERIDQVERSHTGENLEGLTDKLKQISELTIKLEALSDEAC
QVKHKILNLRAEVKRRLSEDFGI
>gnl|CDD|107130 PHA02110, PHA02110, hypothetical protein
MELEIIKVYLESKIQLESLFGNSVGEVEIFKSHWMIRDGFVFIGDPPIDPDLCVVFEKVRYIHKSNEIHA
IMVDDYVSETHKIICLFPEKKICQVEKQ
>gnl|CDD|107131 PHA02114, PHA02114, hypothetical protein
MKLILRTANAGKTQEAIKSAFEAAQHHEVMFVSDEEPYTEILRRLNAFSSENPAIQNRYIISTCVEPATP
EMFDDLGAFDQYGTIVLDVNYAMSRAPWIKVISRLEEAGFNVVATQELVKPAAPTFH
>gnl|CDD|164902 PHA02115, PHA02115, hypothetical protein
MNIQKEIQEIEKRLGVEASEFKMPSVWKVARKPGWSYGAVFEQEFTAYEHKELGCFVAVYSERHRAQFVN
TEGEDVIGHTERVVSVQHVEPYKTRLGTSWRVVNA
>gnl|CDD|177351 PHA02117, PHA02117, glutathionylspermidine synthase domain-containing protein
MKRVSIEARKDWLPQLTSEGLLWTTTEEGPYWIEAMARPPYYSFTQAEQDELEGAANELHAMCGHALDWM
FSYPSEASRHPAFDMFNIPENARQMIKRSWTEDEWGLYGRFDLIMTPNGGPKMLEYNADTPTILIESAIS
QWNWLDDAHPRRQQFNEIHEALVNHWADMKKLNALNGCLNIVATGQVEDFVTIAYLAETATEAGAVVKFF
DIQEIQLSDRGPFFVDGEDAPIDMCFKLYPWEWMMEDEFSAEILVSQTRFIEPAWKMMLSNKGLLALLYE
RYPDCPWLVPAYVEDDFDRENLFTLENPKYVSKPLLSREGNNIHIFEYGGESEDTDGNYAEEPRVVQQLI
EWGRFDGCYPMIGVWMVGSEAAGLCIREDDPRITGNNSRFIPHVVEN
>gnl|CDD|107134 PHA02118, PHA02118, hypothetical protein
MQKQLKMGIMAAFVSAALSGCGQANTDDTFTYNGLGGEATPTVTAVSAQQCAELGGGSLEQCQSAFDKAK
MEHIDSAPKFNDQASCESGTEAICNRTQIQNSDGSFSDVFVPAMVGMIVGQMMSNNSRPMPVYAPARPED
RKNGFVTSGGAYVPPAKGSVGANTFSAPKTPGSFSKPSPSSKPSFSSKGGFGKSGSFGSSGG
>gnl|CDD|107135 PHA02119, PHA02119, hypothetical protein
MKSSDVYAQVLMAQQFATEELKRKLAPVGKFVADEMIRQRSFKISFDVAKFPAIMPKDIVDYLRSLGYDA
KSDSFRNESVITVTAKP
>gnl|CDD|177352 PHA02122, PHA02122, hypothetical protein
MAANKWQKPGPVMNRVFEEAFIGLLGDGCENIIIHSFKDDGDEVIVNFELVVNGKLIINQTRLIA
>gnl|CDD|107137 PHA02123, PHA02123, hypothetical protein
MKKSIATLIAIGMYGCSAVAPVTANVNEMFHFPQKSGVIQEFTDENGTYESALSASCDREVREQYDNCLG
IVFNSDYWLIDGARDDKNILVGTERVMISLNGIVQNVDYIRSGSAIVIRRMDNPTFNPIGDVLSITTSSG
KGEFTL
>gnl|CDD|133998 PHA02125, PHA02125, thioredoxin-like protein
MIYLFGAEWCANCKMVKPMLANVEYTYVDVDTDEGVELTAKHHIRSLPTLVNTSTLDRFTGVPRNVAELK
EKLGI
>gnl|CDD|222850 PHA02126, PHA02126, hypothetical protein
MNNVVCQCCNQIKPKIVTISDDNFFESVTVVNAHDTIATTVKLHKLSYDQLPGGALIVADRDIITSIRRA
GGNKPRMLDTLSFCRDKMHFELLGRPPVIIFNTQTPLTDIRIALYSKTGFSKSTEFTAYYVRYKESTMRN
LVNRFKNIFKNTI
>gnl|CDD|107140 PHA02127, PHA02127, hypothetical protein
MSNVTHLVNFGHGELAVKKVASYFHVLKSADPMLPVGTEFPIKDTVTLDADVIQLNA
>gnl|CDD|107141 PHA02128, PHA02128, hypothetical protein
MSIVKERFFNYKTFFIDAINRSYANKPSGCIQEMSQPKSSFLREHRTIHLNLGRMTGKTTGLLHLANEVS
AQGGARIITMNSANKRHVQDMVSYQWRGDIRISTISELTDRCPKVKFLMIDESEYTLTSRHQRQEIYDWA
GTHGVEFVIMT
>gnl|CDD|107142 PHA02130, PHA02130, hypothetical protein
MKTISPTGKEKTFKSWESLREWLDERFDSWDDDILSIPFKSTVYWDLCPYAQDIHNGKENFVWNTDKDLL
EKELESIAQEI
>gnl|CDD|107143 PHA02131, PHA02131, hypothetical protein
MKIYHPQHIAKVNGITKVDMIRGHYRFGISCWIMFKNDQVIDCTFKNDTAQFRSMEKAARQVAAEHQYTL
>gnl|CDD|107144 PHA02132, PHA02132, hypothetical protein
MNLLFELFILSVQYSIIAVMVYVLIHGFAFFDEWRQKRPDSKMPARSLCAVQVYGMIAGAWLPLAIYLVC
KLCEFTYIKVTEKIKK
>gnl|CDD|107145 PHA02135, PHA02135, hypothetical protein
MNCMKRFSSAILEDKYLVTMNDWTREAEFADKVISKFNDNTSNYPGISVPPMKGKPTMGYLGEMTRLFFI
QRYNKENNKDWRKWCRENPGKILVIEVVGDAKSEKPCQLEMQYEKGFWLRLM
>gnl|CDD|177353 PHA02141, PHA02141, hypothetical protein
MLPSLSSTISWLRNNVLYMIIIGLLGWMIKNQSEQIDNLETKIETIQKFQTSSVENAKPVQEAMLKAPKA
TRQMEKIAEKKPQLLEKHMNTGFRQLTDKIQETTK
>gnl|CDD|134000 PHA02142, PHA02142, putative RNA ligase
MIINNERQLASMRKIADLQPIPGADAIEVATIDGWEVVVKKGEFRVGDDCVYFEIDSLLPTDNPAFRFLE
TRARIYDGKMRARIKTIKLRGQISQGIALPTGAFTVGELLGGQEMDKTLDQMLGIIKYEPPQDGTGCNPG
GTFPIFIPKTDEERCQNIFNRYKEKYADVKFAKSLKLDGSSITMAWVTDPDLFLDLGTEDEPYAHDYDDA
QFIVASRNQVLRYNADSKWWKGVENYQIVDRLKELGMSVAIQGELMGPGIQKNRENFDKYRIFAFRAWFI
DEQRFATDEEFQDLCRTLGMEIVPQLGYSYPFQEFTNVKEMLAAADIPSINHKIAEGVVYKSVELVNGRM
VHFKAINNKFLLKCED
>gnl|CDD|107148 PHA02145, PHA02145, hypothetical protein
MSQRHGRFWSIGFNAVGYTGSLPAPNWGTQIRRFAGLNPVGNGLDPALSEFYFGQGAQPAGRWMSQYFNR
GRTPSRCFMWSGSRYPYNSWSGFDWGGELTQIANATIKIGWIGTGRASHRGGDMGYINLRWKWDNDLWQE
TRIFTTPDTYVSDWYGNRVMNLNRPGGGRGTLTFKIVGNVGDFDQHDVGDRGPNASWSPVVDMSVAGSGY
QGELFKSFQGHQTRQYNENN
>gnl|CDD|107149 PHA02146, PHA02146, hypothetical protein
MQIEIGKKYRVTDAERFMAEHGITNGTEFTVTNIDDDGDLYTYDISWNGRDGKSAFAPSEGWALLLNGRN
GNTDEKADYTGSIEEV
>gnl|CDD|107150 PHA02148, PHA02148, hypothetical protein
MNDKSWNLIKMFQMKKTKIEPTVTPLPISDLKVEAFELFKKIEERIAHDQTRLEELAKSRENELRRHEAA
IRLAMDSHSIKMDDLSLQEALISDSLKGGKYLKNIVAQAC
>gnl|CDD|134001 PHA02150, PHA02150, hypothetical protein
MLYRFVSEEQFNAWSSQNYAKEFAKHFKKWDDVFATEDLSCEGMTDWAEINGQYIMSSQWYPFVSDDLGS
RLVEVEE
>gnl|CDD|177354 PHA02151, PHA02151, hypothetical protein
MIPMAVRERIFTQLRHMQSFTIELIMHQIHSRLAKEPREWTSFFDRRMARIDSTVDYAIKEHAKAGGTLS
KAEIAERTGRSLDAELGIAYILGGLTGVMDWLDNDDITFDVPTPDFNLEIKTSFNRWPTMHTAGAEPYGR
ADGLCLYAGYKGNADVFLVLHMENVDGQTYFNPNYFFTKRAMEKYPYEIATRRMVDGAYINRNHDRYVHF
YKKWCTL
>gnl|CDD|107153 PHA02152, PHA02152, hypothetical protein
MSSPFTVEFYNDRNEKVDVRYGNHGWVSPSNIRYAENIINVVNGARFGEENKPVAEWFYFISSGRVYFKE
DYDKMATIVGLIKTFDPYEFSMELKQ
>gnl|CDD|107154 PHA02239, PHA02239, putative protein phosphatase
MAIYVVPDIHGEYQKLLTIMDKINNERKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTLLGNH
DDEFYNIMENVDRLSIYDIEWLSRYCIETLNSYGVSTVTLKYSSVEENLRNNYDFIKSELKKLKESDDYR
KFKILMVNCRKYYKEDKYIFSHSGGVSWKPVEEQTIDQLIWSRDFQPRKDGFTYVCGHTPTDSGEVEING
DMLMCDVGAVFRNIDFPFIKLEVKK
>gnl|CDD|107155 PHA02241, PHA02241, hypothetical protein
MKKIYILEEEIEEMDYDLWEEDTVYTTSYEILGYTDSLEDAEYIRDNYGTSNPIFINEYPYITKEKLIEE
QRYFRYNSYIELKRVNGYFEISEINDLQVTEDFSINKDDKNFDSPFSINMFSHNRNSIGIEFIMFSEYDD
KEDIIEKEKNSFLMKLKYLLKHSKEADIRSTSKIIDSIDKLT
>gnl|CDD|107156 PHA02243, PHA02243, hypothetical protein
MANEKEIIRMVNYLIDNMSMWHINYARAVLIPSEVEKIIKEHEKFDDLLKKRGEWLVKGSDTDNIDDLET
YNQIMNNQKDEMMIQEIDIYTQGKTITIDNEHYSSDDLGEVLNKLEQSEDIKIKSNYKSLYVGYTNVVGY
EVTYASSYEETFKNDLEKDL
>gnl|CDD|107157 PHA02244, PHA02244, ATPase-like protein
MAIQDSIEGLERLVEQQMETTKDLADKLGEKNSNPYEQAIIDAIREKAETEGKEIAIDDIKKEIEDSPEE
QFFELPVKIELQQEGKPAGDISGIDTTKIASNPTFHYETADIAKIVNANIPVFLKGGAGSGKNHIAEQIA
EALDLDFYFMNAIMDEFELKGFIDANGKFHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANKFFD
FADERVTAHEDFRVISAGNTLGKGADHIYVARNKIDGATLDRFAPIEFDYDEKIEHLISNGDEDLVNFVA
LLRHEMAEKGLDHVFSMRAIIHGKKFDGVFEADFLIENIIFKSLPKDDINQFARSLPEGIKETDADRKLL
GMQQEPKQEPRKSDKNNKDGKDFDTILDKKGLE
>gnl|CDD|177355 PHA02246, PHA02246, hypothetical protein
MDNLSHYLSILYAILITVGYIPGLVALVKAESVKGVSNYFWYLIVATVGISFYNLLLTDASVFQIVSVGL
NLTLGIVCLLVASYRKKDYFSIPFIIVFSLLLFLLSDFTALTQTVATITIILAYVTQITTFYKTKSAEGT
NRFLFLIIGLGLASLIVSMVLTHTYVHIIATEFVNFVLILICYLQANYYSRG
>gnl|CDD|134004 PHA02248, PHA02248, hypothetical protein
MKKINSVIKGEGKKVQTADVRKISYYVKDYNPCMTVDDANDYNATSQYLVSDNGKFIAKYNKDMNAVGFY
EESGDTVKHLTHTTPERLEGTVFTIEEETEIDLINDTLPQGDILIKFSDGSIYLPDNESVLDSVNYLADN
DWDSVDDIIYTGLSKGNSENCIVDFNYNNYDIGYDDVEDEDVCDNYPECECSNYCSSTGEYIGN
>gnl|CDD|177356 PHA02256, PHA02256, hypothetical protein
MNIITSLSVVFTCLSLLTLMIFVHSKFSSKNVFVLYVIYAIIGIGTYIVLTMFQTTSVLIKNDVIDSIEN
TEHYIGFNDPIIIFIISFIGAILGGIWYKMMKIIKKSNFKDKK
>gnl|CDD|107161 PHA02264, PHA02264, hypothetical protein
MSTFWSERRTTNKDRQVKKHYTQMSMYERKKCVELLQETITENRIINFTRHSAKKVKGKPTTNIPKLIGF
IFKNKFAYENIIEYNNTDYNGNIERRIVVKHPKVITVEGKPSYQFLTISLEDARVITVWYNSVDDTHRTL
DLNYYSKDLTIQ
>gnl|CDD|164905 PHA02265, PHA02265, hypothetical protein
MSQDKLRAIYTEMKVELHKFPKEVDITSKSTAIAINQILDKFKTLTEQAGKITRKYLEGQEILTIDYEYY
DSLQEYYIYLLRNSEKIEQSLQEITKRTGEYVK
>gnl|CDD|107163 PHA02275, PHA02275, hypothetical protein
MKKYREYLNKTDAENLAEDWEKVTEDLWKVFKDMKPKINTLDISNVVSKDLDKSKPILQFQDSDGVIENI
CNVEGLEDGLSKMKKIFDDSNFEKHYYNRVVDHDEYYWIDYGSHHCFFRVTKGDK
>gnl|CDD|107164 PHA02277, PHA02277, hypothetical protein
MEKNISTHTKGISQADMEKWIEAVVQGTVDGKQVDEKTAKQLDRIGSRSVSLEEATRIAKVLNAVTAQEV
TGDFNDAFNAIDLMMIIMEDELGVTQEKVGKAKDKLNEKREAYLKEKQEELRQKQQEEAQKKTESDSNEK
VIQLKKNDEQ
>gnl|CDD|177357 PHA02278, PHA02278, thioredoxin-like protein
MNSLVDLNTAIRQKKDVIVMITQDNCGKCEILKSVIPMFQESGDIKKPILTLNLDAEDVDREKAVKLFDI
MSTPVLIGYKDGQLVKKYEDQVTPMQLQELESL
>gnl|CDD|107166 PHA02283, PHA02283, hypothetical protein
MAKKNVNDVLQQESVTVADKYLQVKVNRDGYTRTHEGQYAYKVVSEGEELFLYPVQTDGKGTLNVMKKSP
IAYTDGDNIHFVVNTVVDPYNHSFIRTEDIKGLDKGKQLIQAFLAFVEDRFKFGVYNVFVANNKEDVLSI
VDPTDNDADEVKDSLEHAHEDVIADFPASPARKDVKGVDSGEGQGDTSEPSAPKNVQVTPKEDGADVSAE
>gnl|CDD|107167 PHA02284, PHA02284, hypothetical protein
MGIIVNSNHIQSDTLYEYDSFFDIEKVDTFEEGLLSIQDEPTVLAGFIYDDITFNKVINSNSDIDDYIKN
NDIYYVSDIGLLPDTFITVDSDRKYYSLLQQITELSKDPFPKWVEDDAKGLTKYYNFQDFEDVFDLNSFY
KKEVDMVREKCYNNGNVYLLYEVLPDYKLPLAYSLLSNKEHGIVIIGSQTRSNNDILTFYVKGMDAKAIA
SMFNVEHDYDSNIFHTFVNSHINILGNQITKFIREKGSSYE
>gnl|CDD|107168 PHA02290, PHA02290, hypothetical protein
MRNKKSFQEQLNDMRNKEKWVSEEEFTEEVAPPEEPEVEEEKLYTLNELKESLLDAQGLKDVVADFPASK
DLYEPNKLYICTIPKGYQSTEVQPGQYIGISTGLLSESEDFSHLRGQMPRNLYETSHVLKPLIRINNTNI
EYQQHELLEDIKDDKKIYDVELEDLRLATGEEVSHLEIVDNKFFESRINEVLDRYTELTDSNDLLKYYSK
LRELVGSDKMIYCSLLDKCVKIID
>gnl|CDD|177358 PHA02291, PHA02291, hypothetical protein
MSRKASIFYILVVIVLAFSISSYYISSFMYHDKAKNEVSTELSNTGKIKEEKNVEFVGDYTLKKVEDNKA
YFMETLPTYLPGRTGDNSIDMRYYKTSRFKEGVNFKLIRVYTEDGEDNPIHKYRFEAVPTKK
>gnl|CDD|177359 PHA02310, PHA02310, hypothetical protein
MSIPGANLLRMAFGVIGTQIVRYRKFEQRVKNPQAQYVSMFGEPFDLAASVQRVRRDQYVQFNLEFQRNY
VMIFANFEMVDLDRDMAGDQFIWTGRVFQLESQGSWFYQDGWGVCLAVDIGAAKLADDGK
>gnl|CDD|164907 PHA02324, PHA02324, hypothetical protein
AAKKPSLSGGKQIESKPKKTRQGQGKNTKYSATSRNNAKKPYRGQGK
>gnl|CDD|177360 PHA02325, PHA02325, hypothetical protein
MDTKICPKCGARWLDGQHYWSGTGKKGNPHDLAGLVCNKLGDDTCINPCKGSDSGVTWEKRLDELDKFHP
DI
>gnl|CDD|164909 PHA02334, PHA02334, hypothetical protein
MLSFLLPFASKIVSDAVNKIPDDEELGEKLIEICLLILGKAVKLTKTDMDDELLEVVKKAIRAR
>gnl|CDD|164910 PHA02335, PHA02335, hypothetical protein
MKFDELNEGNYMLFAIKNYNNPQSVTYDDFEEDLKRFKYIKRLFKRYLNTGELKTHLILNHIIILYNVFG
EAATPLLFYKLEAEYWPAIKSFLLFLNRLPIFPNEEVDQECLKQLNLI
>gnl|CDD|177361 PHA02337, PHA02337, putative high light inducible protein
MTPEAEIFNGWLAMIGFVAAVGAYATTGQIIPGIF
>gnl|CDD|164912 PHA02357, PHA02357, hypothetical protein
MQKIINGIAILSGLVSLAVVGGGAYVYVNKDTIVDSAKEKATEAITESVGGGLPGDLDIAMPELAIPAAA
LPDTTGPAVPF
>gnl|CDD|222851 PHA02358, PHA02358, hypothetical protein
WTKWIALGLGGLLGISHIGMLGYVATPDNSKVPKINIPVGDYSSYRVKAGKDGYEIEYRANDPKILFSTK
SLKNKGGFLGKGTETTQRTDEYTMDGTRNHGGAVSNGRTWIDPVAVGSLGEKKSSAKSEECIEADGGARS
TGRMVGSSIGAAAAPALSSIPFVGWVAAGWALMLGQNEGADIGGDVAEVFNDSC
>gnl|CDD|107178 PHA02360, PHA02360, hypothetical protein
MTTTSKFKKDLQILRAAANRELFLDVEYPKLYKKIRKYYEEEGIDFYGEPDEDYDILLDKLEEDLQSVEA
>gnl|CDD|107179 PHA02414, PHA02414, hypothetical protein
EMDKEINNLVSQVETLEDKIQEGELTDKGDNKELEVAVAELRDIVVSLDKDVAVNSEKQSHIYYQIERLE
EKISALAESNKKEDTEKKDTVEKVFMIVLGAVVTYVFSKFK
>gnl|CDD|177362 PHA02415, PHA02415, DNA primase domain-containing protein
MATIDELKQRIDLHDLADRLGLKRGRGGDKALYHSPQHEDKSPSLSIYVNHPKHGTGWRDHSADAGGSCI
DLVIHARGGTVADAVRYLHDAYGIPLDRPAPAERREKSTVEYIADRCLAERERVREYLGGRGISAAAIDA
AFAARSLGFNTWTSSKVAAGEVGHAGPAAAFIVREPADGRVVAVDMRYVDPALNGGVKTQTQGDKAGYGW
TADARRLDKAKRVFIVESAINALSIDTCAMPGAAALALRGLANVDAIDFSSLRGKQVVICLDNDEPFEDG
HPRAGHRPGPEAAWALYERLASLNISAVLVDQAGWLADLADGETKQQPINDVNDYLQLRGPEELARALEQ
LEPWLIAGLAGDATRRGRPRIFLPSHDFAQYWRFRVRPDFTSYITKMDRNEESGVETPVMTDLCGFRIAG
ISRVSVASATSTMTGDADQAPTVYFAVSVQTPRHGAQLIRRVMLDDQLHNVDQWGKFGPIWAPAPFKRMV
NILERGADLGARQAANFVGLAWRDGRLIVNEGPDCYFTEADKQCPYHNLTFPSGPTSDARRVIAAYQTTF
KQNAATIPLVWALGGHLKALLGFWPHITIQANKGAGKSTLIKRLERSLAFTMFSGQSLQTEFRLLTSISH
TSHPVGWEELSARRQDVIDKAVGLLQENYQYTVTRRGTDMTEYLLCAPVMLAGEDVPVRSLLGKLVRTTL
TGKRGPLLPDDLPRFPVRQWLEYLAGLDKRAVLEHYATLRDKALAKCIASGADDGANRMAANYAAVALAW
RYLCEFAGMDPSEGGFPHDLLAEMNAHVAETSADREPWVWIMETVLSEIDGGNYKHPYTFDTVDGEFCLL
LRTGHVMDHLAHTSALRDKWNGLPVKSDRVFKTQLKHAGVVVGEKEVERRIYTRRVPYLTPVSLERLAAF
GLHVSVREDLATDALERSHA
>gnl|CDD|107181 PHA02416, PHA02416, hypothetical protein
MPSKLFLYDANEANKDLLDYFKNKNYTRVALTNSTDFFWSQIDSVDNGGYLAIMSHGNNNTFEIAMGNPP
KDMRQDQIVPFGTSLNQRNVTLYLLSCHTGNDPLGRSLLGTGCNFAAPKGYALVKSSSAGVGVYSVVDPH
ASDVKYAGWTGTEGVIPNRDTKPLNIK
>gnl|CDD|164914 PHA02417, PHA02417, hypothetical protein
MARPLYRIRQFAQSRVRGGKLFCAGACQVQQRVAGLFWLEIAYCSDRTGAEAAIRAAVIARRRARLKPRV
LGLFDRDGQALGQ
>gnl|CDD|107183 PHA02436, PHA02436, hypothetical protein
MSEIYYKGFIIKETYGERNIEEVFKEAYESFYGVEVKVVKKELGTKRNSAAS
>gnl|CDD|177363 PHA02446, PHA02446, hypothetical protein
MNIDWFAVECAVNGTPMRLNTDERRMLVRRRPNLPEVELARRSFCTVRTIERDRADLPDAEQQQCPLCGQ
DAWVIHTGIVEAHPDKLLQECPLSGQSVATDWESQTAATVVWLSRRIRVGDSLGVWDYLTKLPEDQRTQL
LMAALAGIPDVEDPFAWITEEVEQVA
>gnl|CDD|164916 PHA02447, PHA02447, hypothetical protein
MSTETQTLTWEWFTGFVGPGRWRAVLPGDRRNAWINPSDVAGDFRWSVEDNTCARVLAWGYEETLDAAMA
AAAAAAAEYRLRKAAR
>gnl|CDD|107186 PHA02448, PHA02448, hypothetical protein
MSEPDVEGLAKLREPFPPNQIGKLPKGGITLDFLGHGYLTARFLDVDPLWTWEPFAVGDNGLPLLDEHGG
LWIRLTLCGVTRIGYGDAGGKKGPNAVKEAIGDALRNAGMRFGAALDLWCKGDPDAPAPPDPAVAERNAL
LHELGDACAALTLDEKTVAAQFYGKYKVTARNAKPAQLREFIDDLMENGAPA
>gnl|CDD|134010 PHA02450, PHA02450, hypothetical protein
MSGEINPEGFTRYGGDCTCGPIYTYGGHAEPGQFDPFCPDHGNPEYVASLEEA
>gnl|CDD|177364 PHA02451, PHA02451, hypothetical protein
PQTVHVLPVDDLIEHVESPDCPCDPELELIERTDDHFGQMYSHNAADGRNDEAE
>gnl|CDD|164918 PHA02456, PHA02456, zinc metallopeptidase motif-containing protein
MSLDLIKLVLLGWALLTRGAPNEWDVALQARVYWSLGAGGGLELAWDPVPIYFRALPQDLCGQFVGWIEI
DPDYANKGCRDTLAHELNHAWQFRTYGLVQPITYAFSAKVWEPEVPASGAEGMPAPRQLNYPLLKVWVPI
W
>gnl|CDD|164919 PHA02458, A, protein A*; Reviewed
MKSRRGFTVQRLMNAMRTAHTKGWYVVFDTLTLADDRLKDFYDNPNALRDYFRDIGRMVLTAEGRSVHDS
SSDCYQYFCVPEYGTQHGRLHFHAVHLMRTLPLGSLDPNFGKLVRNNRQINSLQNTWPYGYSMPIAVRYS
QDAFSRAGWLWPVDTKGEPLKATSYMAVGFYVAKYVNKKSDIDMAAKGLGNKEWNNSLKTKMALLPKKLF
RIRMSRNFGMKLLSMAHLSAECLIQLTQVGYDVTPFNNILKQNAKKELRLRLAKKSVADVLEAQPVTTNL
LKFMRNLTRTIGVSNLQSFIASMTQKLTNTDISDETKNYVDDAGITVADLRIKSKWTAGGK
>gnl|CDD|177365 PHA02503, PHA02503, putative transcription regulator; Provisional
KNQEKTINHLGQVVYQESVEFYKEKLSVYSKDFLQNSLIPQLYEWSNAYKAAVELTK
>gnl|CDD|107192 PHA02508, PHA02508, putative minor coat protein; Provisional
MAPLAAFLIALALGPFALKLFTSLGIGIFTYVGLDAAVDAALGAAKPMLAGLPAVAAAILAIAGVFEALS
IIAGAILARASIISAKAFLGKLT
>gnl|CDD|222852 PHA02510, X, gene X product; Reviewed
MNLYDDSQVIDAIINKFFSITKSGNLSSAKAMRYFGFYRRLVNEGYDNVADTMSRATFWRHRKVLKEFGI
DKAQLMNLSTNNNVVPLVRVINVDFSAQIPSWYDEPVFSSNRVSSF
>gnl|CDD|177367 PHA02513, V1, structural protein V1; Reviewed
VWSKLKVTHEALKVAKNPYKYFTKEQIAEATKIFYQTWDGNIISSARRFVEVAKANPKLTKGEGTNIGVL
LGLFIFILIGIVLLPVITSQVNNLTSGTAPSVTGTNATLLNLVPLFYILVLIIVPAVVAYKIYKD
>gnl|CDD|107197 PHA02515, PHA02515, hypothetical protein; Provisional
MSVQSTDRVAGPYPCNGLTTQFPFDFKVFNTGEVVAILSDADGVESTLTLGTDYTVALNDNQDSNPGGTL
TTLATYATGYKITLTSEVPNTQPETLTNQGGFYPKVIEHALDRLVIQIQQLADKLSRTVQAPISGGLSSS
EILEQLAEQLPLVSAVYGHLANIDAVATNEADIDTVAASVGAVDTVAGDLGGTWAAGVSYDFGSIAVPPI
GNTSPPGGNIVIVANSIGNVDTVAENIGDVSTVSTHLSSMLAVANDIDSVVSVAGDLENIDAVADNAANI
NTVAGANANVNTVASNILDVGTVAGNIDDVQAVAGNAANINVVADNADNINATAANQANINAAVGNADNI
NAAVANQANINAVVGNANNINAVAANEGNVNTVVDNLADVQTVAGIAADVSTVAENEAAVAALGNDLTGQ
PMVIDYGDLSPASNPAAPAGVLGAVWANAENIAAVAENIAVIIEAANNLPAILAALSGALVPANNLSDLA
DPAAARANIGLADLGGIA
>gnl|CDD|134016 PHA02516, W, baseplate wedge subunit; Provisional
MNRETGRALSDLEHIRQSIGDILLTPLGSRVMRREYGSLLPDLIDQPQNPALRLQIYAACAMALMRWEPR
ITLTRVQIERAADGRMTVDITGWHVDTGEPVSL
>gnl|CDD|222853 PHA02517, PHA02517, putative transposase OrfB; Reviewed
LGIAPSTYYRCQQQRHHPDKRRARAQHDDWLKSEILRVYDENHQVYGVRKVWRQLNREGIRVARCTVGRL
MKELGLAGVLRGKKVRTTISRKAVAAPDRVNRQFVATRPNQLWVADFTYVSTWQGWVYVAFIIDVFARRI
VGWRVSSSMDTDFVLDALEQALWARGRPGGLIHHSDKGSQYVSLAYTQRLKEAGIRASTGSRGDSYDNAP
AESINGLYKAEVIHRVSWKNREEVELATLEWVAWYNNRRLHERLGYTPPAEAEKAYYASIGNNDVAA
>gnl|CDD|222854 PHA02518, PHA02518, ParA-like protein; Provisional
KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPLIPVVRMGKSIRADL
PKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFII
SRAIKNTQLYREARKALAGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEIIQLVKELFRGIS
G
>gnl|CDD|107201 PHA02519, PHA02519, plasmid partition protein SopA; Reviewed
MSLINLLNSCIERGQEMTQAIAIAQFGDDSPEARAITRRWGITEVADLIGVTPQAIRDAEKSGRLPPPDF
ETRGRVERRAGYTIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLL
IEGNDPQGTASMYHGYVPDLHIHADDTLLPFYLGERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQY
HDAGKLPHPPHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTM
LLDLLATVDLGGFEPVVRLLLTKYSLTVGNQSRWMEEQIRNTWGSMVLRQVVRVTDEVGKGQIKMRTVFE
QAANQRSTLNAWRNAVAIWEPVCAEIFNDLIKPRWEN
>gnl|CDD|164924 PHA02523, 43B, DNA polymerase subunit B; Provisional
MELELFRDFNEEELTYLNTLSTDELQQMIARCEKEEQKRNTNQLNRKILINSLYGALGNNWFRYFDLRNA
EAITTYGQLAIRWIERKLNEYINELVKTTGVDYVCYIDTDSVYLNMEAVVNRVGIDKFRDTNHLIDFLDN
LGSKKLEPFIDDSYKELEEYMNHDHHLLLMDREAIFGAPLGSDGIGGFWTGKKRYALNVYDMEGTRYAEP
HLKIMGLETQRSSTPLACQKSLKESIRRLLQEGESSLQDYFKEFKDEFKNIPYQDVAAVSSANNIGKNGD
ALGFPIKGTPYHVKGVLAYNRIAKTDTAIPMISEGEKVMVLPLRDRNPFNEACFAWPSGTPIPPAVEADV
LKYLDINKLFDKTFVKPLSSICEATKTDYEFRNNLFDMFDI
>gnl|CDD|164925 PHA02524, 43A, DNA polymerase subunit A; Provisional
MRHYTNIEIIGNNIMERFVDNGKRQTRKVAYQPTLFQHAAPGVQTKHKDIYGRFCVPKKHENIWEAKQWI
KRMEEVGMDAMGMDDYGISYISDTYRGVIDFDRDDVVIDVVDIEVTAPEFPEPKYAKYEIDMISHVRLHN
GKKTYYIFDLVKDVGHWDPKKSVLEKYILDNVVYMPFEDEVDLLLNYIQLWKANTPDLVFGWNSEGFDIP
YIITRITNILGEKAANQLSPYGKITSKTITNLYGEKIIYKIHGIALMDYMDVFKKFSFTPMPDYKLGNVG
YREVKADKLDYEGPINKFRKADHQRYVDYCVRDTDIILLIDGRRCFIDLILSLSYYAKIRFDDVLGTIKV
WDSIIFNSLVESNVVIPAMKASPKQSFPGAYVKEPVPGGYRYGLSFDLTSLYPSILRLLNISPEMIAGMF
SPARLEDYINKVAPKPSDQFSCAPNGMMYKKGVVGVLPNETEKVFLQRKSEKKMMLAAIRNQEAIKKILA
SRGVKLDH
>gnl|CDD|177369 PHA02528, 43, DNA polymerase; Provisional
MMEFYTSVEQVGDNILERYIDDNGKERSRKVKYEPTLFVHANEESKYKDIYGKNCRPKKFDSMRDARKWM
KRMKDVGFEALGMDDFKLQYISDTYPGEIKYDRSKIRIANLDIEVTAEDGFPDPEEAKYEIDAITHYDSI
DDRFYVFDLGSVEEWDAKGDEVPQEILDKVVYMPFDTEREMLLEYINFWEENTPVIFTGWNVELFDVPYI
INRIKNILGEKTAKRLSPWGKVKERTIENMYGREEIAYDISGISILDYLDLYKKFTFTNQPSYRLDYIAE
VELGKKKLDYSDGPFKKFRETDHQKYIEYNIIDVELVDRLDDKRKLIELVLSMAYYAKINFEDVFSPIKT
WDAIIFNSLKEEKIVIPENKSHKKQKYAGAFVKEPVPGAYRWVVSFDLTSLYPSIIRQVNISPETIAGTF
HVAPVHEYINKTAPRPSDEYSCSPNGWMYRKDIRGVIPTEIKKVFDQRKIYKKKMLAAERNAELIKTILE
DLNDSVDTPIDVDYYFDFSDEFKAELKTLTKSSLKALLEECEKEIALCNTIQMARKILINSLYGALGNEH
FRYYDLRNAEAITLFGQLAIQWIERKMNEYLNKLCKTEDEDYVIYGDTDSIYVNLDPLVEKVGEDKFKDT
NHWVDFLDKFCKERMEPYIDSSYRELCEYMNNYEHLMFMDREAIAGPGFWTAKKRYALNVWDSEGTRYAE
PKLKIMGIETQRSSTPKAVQKALKEAIRRILQEGEESLQEYIKEFEKEFRKLDYEEIAFVSSANNIAKYS
DDKGIPGKGCPIHIRGALLYNRAVKGTLGYPPIQEGEKVMVLPLKEPNPIGENCIAWPSGTELPKEIRSD
LLKWVDYNLLFEKSFIKPLKNITEAIGWDYEKKASLEDLFG
>gnl|CDD|222855 PHA02529, O, capsid-scaffolding protein; Provisional
MKKKTKFFRIATEGATVDGREISAEWLTQMAETYDPEVYGARINLEHIRWAWPDGEFKNYGDVIELKAEE
IEDGKLALFAQIAPTDELVELNKAGQKLFTSIEIQPNFADTGKAYLVGLAVTDDPASLGTEYLKFSAKAK
HNPLARRKQNPENLFSVACEAKEEFEPEAELAALFEKVKKLFSRKKEDDAMTDEQFADVHEAVEGVAEKI
DHTSAQVATTETAEPPQEGKDTEENGETAEQFSALKETLDKLASKFNEEVPAPQRPPATGGGGAYADL
>gnl|CDD|222856 PHA02530, pseT, polynucleotide kinase; Provisional
MMKIILTVGVPGSGKSTWAREFAAKNPKAVNVNRDDLRQSLFGHGEWGEYKFTKEKEDLVTKAQEAAALA
ALKSGKSVIISDTNLNPERRRKWKELAKELGAEFEEKVFDVPVEELVKRNRKRGERAVPEDVLRSMFKQM
KEYRGLVWPVYTADPGLPKAVIFDIDGTLAKMGGRSPYDWTKVKEDKPNPMVVELVKMYKAAGYEIIVVS
GRDGVCEEDTVEWLRQTDIWFDDLIGRPPDMHFQREQGDKRPDDVVKEEIFWEKIAPKYDVLLAVDDRDQ
VVDMWRRIGLECWQVAPGDF
>gnl|CDD|222857 PHA02531, 20, portal vertex protein; Provisional
MNNFLGFFKPWAKLDEDVYKEQLKSDLESIAAPKNDDGASEIETNEPASAYAGLFQQFYGGIEPGIRNTK
ELINTYRSMMNNPEVDNAVDEIVNEAIVYEEDDEPVSVNLDNTEFSKSIKKKIREEFDYVLNLLDFDRKG
YEIFRRWYVDGRIFFHKIIDPKNPKGGIQELRQLDPRKIEKVREIITETEDGVKVVKGYKEYFIYNPGHD
SYYYNGQVYSANTKIKIPRDAIVYAHSGLMDCDGKYIIGYLHRAIKPANQLKLLEDALVIYRITRAPERR
VFYIDVGNLPKRKAEEYLNNVMQRYKNRVVYDANTGKVKNQQNNMSMTEDYWLPRREGKRGTEITTLPGG
QNLGDMEDVRYFNKKLYEALRVPLSRIPTEGGGVNGGAGTEITRDELKFNKFIRRLQKRFSEIFLDPLKT
NLILKGIITEEEWDDQINNIKVVFNRDSYFTELKEAEILERRINALTQIEPYIGKYVSHDYIMKNILQMT
DEEIKEEDKQIEEESKEGRFQDPD
>gnl|CDD|222858 PHA02533, 17, large terminase protein; Provisional
KDNKRTRYMGLPNLKRANIKTQWTKEMVAEWKKCRDDIVYFAENYCAITHIDYGTIKVQMRDYQKDMLKI
MHKNRFNACNLSRQLGKTTVVAIFLLHYVCFNKDKNVGILAHKASMAAEVLDRTKQAIELLPDFLQPGIV
EWNKGSIELENGSKIGAYASSPDAVRGNSFAMIYIDECAFIPNFIDFWLAIQPVISSGRSSKIIITSTPN
GLNHFYDIWTAAVEGKSGFVPYTVHWSSVPERLYNDGIFDDDEEWKSQTIANSSLAQFRQEHECEFLGSS
GTLISGMKLSKMTFIDVIPDNEGFYIYEKPVEGHKYIATLDVSEGRGQDYSALHIIDITEYPYKQVAVYH
NNTISPLILPDIIVDYLMEYNEAPVYIELNSTGVSVAKSLYYDLEYENVICDSMRGQGFSDLGMKQTKRV
KAVGCSNLKDLIEKDKLIINDKDTIQELRTFSEKGVSWAAEEGFHDDLVMSLVIFAWLVTQEKFKEFTDK
DDMRIASEIFARELEQMEDDMAPFGFVDDGLNTAEYGDKSHGMS
>gnl|CDD|222859 PHA02535, P, terminase ATPase subunit; Provisional
TAYDDDVRRAAKFLYWQGWTVAEIAEELGLKSRTIYSWKERDGWRDLLPEERIEESIEARLIQLIEKENK
TGGDYKEIDLLIRQHERLARVRRYSGTGNEADLNPNVANRNKGPKRKPVKNDISDEQTEKLIEAFLDSLF
DYQKHWYRAGLHHRTRNILKSRQIGATYYFAREALEDALLTGRNQIFLSASKAQAHVFKQYIIAFAREAA
DVELTGDPIILPNGAELHFLGTNANTAQSYHGNVYFDEYFWIPKFQELNKVASGMATHKHWRKTYFSTPS
SKTHEAYPFWSGELFNRGRPKRERIEIDTSHEALDGGRLCPDGQWRQIVTIEDALKGGCDLFDIEELRRE
YSAEDFANLFMCVFIDDAASVFPFSDLQRCMVDSWEEWEDYKPFAARPFGSREVWVGYDPAHTGDSAGLV
VVAPPAVPGGKFRVLERHQWRGLDFAEQAAEIRKLTEKYNVTYIGIDATGIGAGVYQLVKKFFPAAVAIN
YSPEVKTRLVLKAHDVIEHGRLEFDAGWTDIAASFMAIKKTSTASGRQMTYTAERSEETGHADLAWACMH
ALINEPLDGGTRRKSTWLEFY
>gnl|CDD|222860 PHA02536, Q, portal vertex protein; Provisional
MSKRKSRTPQTAAKTDNPSAGRAEVFSFGDPEPVLDRREILDYVECFSNGRWYEPPVSFKGLAKSARANA
HHSSALKVKANMLASTFIPHRLLSRADFSRFVLDYLVFGNAYLEKRRNRLGQVIRLEPLLAKYVRRGKDG
DFFYLVRNWQEPHEFAPGSVIHLLEPDINQEVYGLPEYLSALQSALLNESATLFRRKYYLNGAHAGFILY
MTDAAQKEEDEENLREAIKNSKGPGNFRNLFVYAPNGKKDGIQLIPVSEVATKDEFFNIKNISADDVLAA
HRVPPQLMGIIPTNTGGFGDPEKAAEVFARNEVIPLQERFAEANDWIGQEVERFKNYKLKFREQPA
>gnl|CDD|222861 PHA02537, M, terminase endonuclease subunit; Provisional
MTSPAQRHFLRVSAAQAAAATQPAAVARHATAYELMLAQLAADRRALKGIQSIERKAELKRDLLPKYLPW
VEGVLAAGAGYQDDVLMTVMVWRFDIGDFDGALEIAEYALEHGLTMPDQFRRTLANFVAEEVANAALKAA
SAGESVEPYFLRVFLDLTTEWDMPDEVRAKLYKAAGYLLLRNEKGEPIGDAETLQLALALLQRAFQLNDK
CGVKKDIERLERRLKALAES
>gnl|CDD|164934 PHA02538, N, capsid protein; Provisional
MRKETRQAFNAYAAQLAKLNGIPVSDVSKKFAVEPSVQQKLEEAIQESSEFLKRINVVPVDEIKGEKLGL
GVSGLIASRTDTTGFTKRQGVDPTALDGNKYECEETDSDTAITYAKLDQWAKFDDFQKLIREFIQKQQAL
DRIMIGWNGVSAAATTDRSANPLLQDVNKGWLQKYRERAAARVMTEGAKTSGKIRVFGKGGDYANLDALV
MDLTNNLIDPWHQDDPDLVVIVGRDLLADKYFPIVNKAQKPTEKIAADLIISQKRIGGLPAVRVPFFPAN
AMLVTTLENLSIYTQEGSRRRSLKDNPDKKRIENYESRNEAYVVEDYGCGCLVENIKVKDSTEPANHR
>gnl|CDD|222862 PHA02539, 18, tail sheath protein; Provisional
MALLSPGIEIKETDLQSTVVRASTGRAALVGKFAWGPAYQIFQITNEVELVDTFGQPNNQTADYFMSASN
FLQYGNDLRVVRVVDKETAKNAGALYNSIEYTITTAGSNYAVGDKITVKYNTAVVEEAGKVTKVDTDGKI
VAVFIPSAKIIAKAKSVGVYPTLGSNWTTEISSASGGVAATLTLGGIVTDSGITLTNAETAEAAITAVAF
QANIAKYGVPSVVALYPGEVGSTTEVEILSKAAYAKVGSALLTIYPGGGTRANTAQSVFNYGPQTDEQYA
IVVRRDGIVEESTVLSTAKGAKDIYGSNIYMDDFFANGGSNYIYATSSGWPQGFSGILNLAGGNSANADV
GAGDLMAAWDLFADRESLHVNLLIAGACAGEEAETASTVQKHVVSIADERQDCVAFVSPPRSLVVNIPVT
TAVDNLVNWRNGLISSTYAVIDGNYKYQYDKYNDVNRWVPLAGDIAGLCARTDNVSQPWMSPAGYNRGQI
LNVIKLAYEPRKAQRDRLYQNRINPVVGFAGGQGIVLFGDKTATAVPSAFDRINVRRLFNMLKKNIGDAA
KYKLFEQNDAFTRSSFRMEVSQYLQNIQALGGIYDFRVVCDTTNNTPDVIDRNEFVATIYVKPARSINYI
TLNFVATSTGVDFDEVIG
>gnl|CDD|222863 PHA02540, 61, DNA primase; Provisional
YIDIEFANRASPHLPKFKQVRRSSFYNFRCPICGDSQKDKNKARGWIYEKKDGGVFKCHNCGYHRPFGNF
LKDYEPDLYREYIMERFKERGTGKGRPVPKPKFEFKKEKKVIEKLPFCERLDTLPEDHPIIKYVENRCIP
KDKWKLLYFTREWQKLVNSIKPDTYKKEKPEPRLVIPIFNKDGKIESFQGRALRKDAPQKYITIKADEEA
TKIYGLDRIDPGKTVYVVEGPIDSLFLPNSIAITGGDLDLNEVPFKDTRVWVLDNEPRHPDTIKRISKLI
DAGEKVVIWDKCPWPSKDINDMIMKGGATPEDIMEYIKSNTYQGLMAKLRLSKWKKV
>gnl|CDD|177376 PHA02541, 23, major capsid protein; Provisional
MKKKELQEKWSPLLEHEGLPEIADASKQAVVAKILENQEKDIREEPVYRDEKIVEAFGSFLTEAEIGGDH
GYDATNIAAGQTSGAVTNIGPAVIGMVRRAIPNLIAFDICGVQPMTGPTGQVFALRSVYGKDPLAAGAKE
AFHPMYEPDAMFSGQGAAGAFAALAASTAIAVGDIVTHFFQETGTAYLQNVTAVTVTATAADAEALDAAV
TALMEAGTLAEIAEGMATSIAELQEGFNGSTDNPWNEMSFRIDKQVVEAKSRQLKAEYSIELAQDLRAVH
GMDADAELSGILATEIMLEINREVVDWINYTAQVGKSGNTQTVGAKAGVFDFQDPIDGRGARWAGESFKA
LLFQIDKEANEIARQTGRGAGNFIIASRNVVSALAMADTGISPAAQGLAGGLNVDTTKSVFAGVLGGKYK
VYIDQYARQDYFTVGYKGSNEMDAGIYYCPYVALTPLRGSDPKNFQPVMGFKTRYGIGINPFADSTTQAP
GARITSGMPSINSVGKNAYFRRVWVKGL
>gnl|CDD|222864 PHA02542, 41, 41 helicase; Provisional
IEETILSNLIFNEDYFRKVWPYLKAEYFESGPEKVIFKLIKKHVNEYNAIPTIEALSIALENRSLSEVTF
DGAKDLLSSLSDNPEDLDWLVKETEKWCQDRAMYNALSKAIEIQDNADKPLEKRNKKLPDVGAIPDIMQE
ALAISFDSSVGHDYFEDYEERYDSYQSKANKIPFKLEILNKITKGGAERKTLNVLLAGVNVGKSLGLCSL
AADYLQQGYNVLYISMEMAEEVIAKRIDANLLDVSLDDIDDLSKAEYKAKMEKLRSKTQGKLIIKQYPTG
GAHAGHFRALLNELKLKKNFKPDVIIVDYLGICASSRLRVSSENSYTYVKAIAEELRGLAVEHDVVVWTA
AQTTRSGWDSSDVDMSDTAESAGLPATADFMLAVIETEELAQMGQQLVKQLKSRYGDKNKFNKFLMGVDK
GNQRWYDVDQEAQKSPLDEADPQEAQQAHKKQVARQSESTRSDLDKLATVANF
>gnl|CDD|222865 PHA02543, regA, translation repressor protein; Provisional
LDYMVEIKLKEPDDFLKVRETLTRIGIANNKEKKLYQSCHILQKQGKYYIVHFKELLALDGRQVDLTEED
IQRRNNIAKLLEDWGLIEIVDPDQMEEVSPTNNFRVISHKQKGEWTLVPKYRIGR
>gnl|CDD|222866 PHA02544, 44, clamp loader, small subunit; Provisional
MITVNPNEFMWEQKYRPSTIDECILPAADKETFKSIVKKGRIPNMLLHSPSPGTGKTTVAKALCNEVGAE
VLFVNGSDCRIDFVRNRLTRFASTVSLTGGGKVIIIDEFDRLGLADAQRHLRSFMEAYSKNCSFIITANN
KNGIIEPLRSRCRVIDFGVPTKEEQIEMMKQMIVRCKGILEAEGVEVDMKVLAALVKKNFPDFRRTINEL
QRYASTGKIDAGILSEVTNSDIDDVVEALKAKDFKAVRALAPNYANDYASFVGKLYDELYPQVTPPSIIR
LIEIIGENNQYHGFAADQEIHLLYLLTQLMLECEFK
>gnl|CDD|177380 PHA02545, 45, sliding clamp; Provisional
MKLSKETIDILKNFSTINPSIVLKPGNFIMTKSVNGVIYAEATIEDEFDSEFAIYDLNSFLSILSLVGDD
AEITFDEDGNIVIRGGRSKIKYPYADPSTIVKPKKRVTFPVADVEFELKAEDLQQLLKASRVLGLDDLAI
TNIDGKIVINLFNEDDKNDTSNSYSLEVGEYDGDNEFNFIIKIENMKLVPGDYKVSISKKGAAKFEGENL
SYVIALEADSTHD
>gnl|CDD|222867 PHA02546, 47, endonuclease subunit; Provisional
MKILLIGDQHLGVRKDDPWFQNYQLKFIKQAIEYSKAHGITTWIQLGDTFDVRKAITQNTMNFVREKIFD
LLKEAGITLHVLVGNHDMYYKNTIRPNAPTELLGQYDNITVIDEPTTVDFDGCSIDLIPWICKENTEEIL
EFIKNSKSEYCVGHWELNGFYFYKGMKSDHGLDPDFLKKYKQVWSGHFHTISEKGNVTYIGTPYTLTAGD
ENDPRGFWVFDTETHKLEFIANPTTWHRRITYPDYDKIDIKDFKGKSVRLIVTEVDDDLTKFESELEKVV
HDLKIVEKVDDSSDVDDDEEEVKSTLTLLNEYIDEIDITDEDKSAVKAIMNELYAEATEA
>gnl|CDD|222868 PHA02547, 55, RNA polymerase sigma factor; Provisional
METKTKNNYVNNKELYQAICKWKQEVAEAKDPGKKPRMPDYIGLAIMKIAEGLSRRPNFSGYTQTWKEDM
IADGIEACIKGLHNFDETKYKNPHAYITQACFNAFVQRIKKEKKEMAIKYKYFLHNVYDEVDDDMVAIAD
ETFIQDIYDKMNQYEESIKKKKKRKEELPSLDFFYEDED
>gnl|CDD|177383 PHA02548, 24, capsid vertex protein; Provisional
MAKINELIRESTTTNANSNGRPNLVSLTRATNNLIYSDLVAIQETNQPVAALYGVRYLNPDGDMTFKTGA
TYAGEVGYRDRITIPELTDAYAKGDLFKFNDVVYEVLEAGPLASSETDLEEAIQEAVVLGKIRLVSDAAS
TEKFEDGDEEIAETSFQIDKWQVPVRSRKLKTSLTVELAQDLEANGFNAPNFIEDLLATVMAEEINKDII
QSLITVSKRYKVTGISPNGIIDLTSYDDAPEQGRTLYQYACEMNSEMQRTTSFEATYVVASSRVAAILAA
SGWMEEKDEDDPLAYGYLRNGLPVYADTNSPFDYVIVGCKHDIGEMEHVGSLFYSPYTEADHAGAFKVIV
DPDSLQPSVGILVRYALSANPYTVAKDQKEARIIDGDDWDKMAGRSDMSYLLGVKLPPIIID
>gnl|CDD|222869 PHA02550, 32, single-stranded DNA binding protein; Provisional
FSMFKRKDPAQLQAQLAALKGGSGFSKEDEREWKLTLDASGNGSAVIRFLPAKEDEELPFVKLVNHGFKG
NGGWYIENCSSTHGDYDSCPVCQYISNNDLYNTGKEEYKLRKRKTSYWANILVIKDPAAPENEGKVFKYR
FGKKIMDKITAAINPDFDMGEPPVDVTCPWEGANFVLKAKKVGGFPNYDDSKFAAPSPLPNIDDEAFQKE
IWEQMHDLSEFVAPDKFKSYEELETKFNKVMGTSAVGGAAASAADALASDLDSFDAQQAAFDAKPSADSA
QSSPDVSSSPVSDDDDLDSLLADL
>gnl|CDD|177385 PHA02551, 19, tail tube protein; Provisional
MDLTDITRAFESGDFARPNLFEVEIPFLGQNFKFKCKAAALPASTVEKIEVGFRNRKINIAGDRTFDDWT
ITVYNDDAHKIRQAFVDWQNMIHGMGNNITGDTPAGYKKDATVRQLDRDGKTVTREYTIYGLFPTNVGEI
DLDWDSNNEIETFEVTFALDYWE
>gnl|CDD|222870 PHA02552, 4, head completion protein; Provisional
MAYSGKYVPKNPSKYKGDPRKITYRSSWERWFMKWLDKNPSVIKWGSEEVVIPYFSNADGKRRRYFMDFY
VKVDNGQKFLIEVKPKKETQPPKKPAKMTTAAKKRFINEVYTWSVNTDKWKAARALCEKKGWKFKIITED
ELKKVFGWKGV
>gnl|CDD|222871 PHA02553, 6, baseplate wedge subunit; Provisional
NMIPDIFTSLDFDEIKSSLIEYLRTQDEFKDYDFEGSRLNVLIDLLAYNTLYIQQFANMALNESFLRSAT
LRSNVVQAAQDLGYLPRSKSAAQTTINLTVTDPLNPNTITLPRGTKFIGTVDGDSYNFVVSEDVVAIRDS
NNAYFSNVKLVQGRIVRTEYTVDTSKTSRILIPDPDIDRNTVKVRVDGAEWSDWTRTYNRVESIVNATGT
STVFYLRETVDGRYEIFFGDGEGGLKPEDGSVIVIEYLSTSGADANGARNFSYADTLTNIQGVSIDENPT
DDPDYVGADGGGDPESIERIRELAPRMREAQRRAVTASDYEAFVSERFGSIVQAVQCGGDSLKPPVYGYV
FIAVKPKSGLYLTDVQKEDIKNYLKKYNVASITPSIIDPNYLYIKINIKVTYDTNSLSESEQWLRGQVIS
AIDRYYTEEVEIFNSSFSKSKMLTYIDDADRSIIGSSATIKMVREVKPNFNKTPMYGISFGNQIKEGSVK
SSGFSFPSEEDDFSYDVRIVSTDDDTSTGIGKIVIGPFADKTAIDGRDLYYEVGTVDYVKGEISFDLGVL
NITSDRFEGVYIELTADPLDDNIFTTDGSLIVFENDLRPQYTTIALEPISQ
>gnl|CDD|177388 PHA02554, 13, neck protein; Provisional
SAYNPNNPRELKDYILRRLGAPIINVEVTEDQIYDCIQRALELYGEYHYDGVNKGYLKFKVTEEQARTGV
FDLSGSNVFAVTKILRTNAGSITSMDGTATYPWFTDFVLGLAGVNGGIGSSCSSFYGPNAFGADLGYFTQ
LMSYQLMMQDLLSPLPDYWYNSANGQLKVMGNFRKGDLIVIEVYVKSYLEVLDMVGNVAGYGQAGGNRQD
RLYLDIDWDNPYEDLSGMVDAYRGQDPDDKTGAYNNRWVKDYATALVKEQWGQILAKHQGMQLPGGVTLD
GRRLIEEARQEKEKLREELLLLYEPPPILMG
>gnl|CDD|222872 PHA02555, 14, neck protein; Provisional
MILNPYVNFYGYSGTQTLADDLVAESIQMRGVEVYYIPREYVNPDLIFGEDVQSKFTKAWKIAAYLNSFE
GYEGQGDFFSKFGMQINDEVTFSINPRLFKHQVDGGRPKEGDLIYFPMDNSLFEIKWVEPEDPFYQLGKN
YVRKITCEKFIYSGEEIDPGVQEIDGINITGFESLDLWPVRNLDGLADINIDQYAENDEFEDEADDFIES
NPFGVI
>gnl|CDD|222873 PHA02556, 15, tail sheath stabilizer and completion protein; Provisional
MFGYFYNSSIRRYIVLMGTLFNNIQVKRQRDTGDKFIKVPITYASKEKFLARLNKWTSINSDEDVAKVET
ILPRMNLELVDIQYNAQRKTSIAQKTKTQKDGTKVVSQYNPVPYKFIFELGIYTRYQDDMFQIIEQILPY
FQPHFNTTITELHDNEIKIDRDIPIVLQSIAPDEQIEGDFLSRRRIEWTLMFEVKGWLYPPVTDAKGEIR
TIYLDFFANSRELAPEGNFESVDHEVVPRAVEKEDWDGESVQTYSDDIPIPTGPEPPGPRGIE
>gnl|CDD|222874 PHA02557, 22, prohead core protein; Provisional
MMLKEQLLAEASNIVTDVSVALDSIFESVELSEEVKEKFSTVFEAAVKQHAVKLAESHIAEIAEKAEELV
EEALEEAVEAIETKLAEDADKYLDHLAKEWLAENKLAVDRGIKAELFESFLGGLKELFVEHNVVVPEEKV
DVVAEMEEELDEMEEELNELFEENVALEEYINEVKREVILSEVTKDLTESQKEKVASLAEGLEFSETFSK
KLTAIVEMVFKSKDKEQEIIENLDTDAAALNFEPEAVEEPAEKEEVSPSMAAYLKAASRWS
>gnl|CDD|222875 PHA02558, uvsW, UvsW helicase; Provisional
MMDIKIHFKNESHVRIECEPSIFYELRDYFSFEVPGYKFNPKFKYGGWDGKIRLLDYNGLLPYGLVGQLK
KFAKNRGYSIWVDPRIEENEDISREDFDEWVSSLEIYSGNKKIEPHWYQYDAVYEGLKNNRRLLNLPTSA
GKSLIQYLLSRYYLENYEGKVLIIVPTTSLVTQMIDDFVDYRLFPREAMHKIYSGTAKDTDAPIVVSTWQ
SAVKQPKEWFDQFGMVIVDECHLFTGKSLTSIITKLDNCKFKFGLTGSLRDGKANILQYVGLFGDIFKPV
TTSQLMEEGQVTDLKINSIFLRYPDEDRVKLKGEDYQEEIKYITSHTKRNKWIANLALKLAKKGENTFVM
FKYVEHGKPLYEMLKKVYDKVYYVSGEVDTEDRNEMKKIAEGGKGIIIVASYGVFSTGISIKNLHHVIFA
HPSKSKIIVLQSIGRVLRKHGSKSIATVWDIIDDLSVKPKSANAKKKYVHLNYALKHALERIKIYNEEKF
NYEIKKVNLKA
>gnl|CDD|222876 PHA02559, 59, 59 protein; Provisional
MIKLRMPPDPDRRINGKSVYKLYLMMKQHFAGKYDVIKYNWKMRASDAAFNKRRDKYFFEKLAEKYTLKE
LYDIFLSNFVANPDAWIGDISDADALTFYREYIGRLERFSYKFKEDVKNLYYFSKKVEVPLKKIFEYNKK
SHTSYIFKLLQSGEISFETFLILDSFLGIIDKHDKVLDDLIWQNYSTKLKAYRKLLVIDCEKAKKLFIQT
VKECKE
>gnl|CDD|164955 PHA02560, FI, major tail sheath protein; Provisional
MADDYHHGVEVIEINEGTRPIRTVSTAVVGLVCTAPDADATAFPLNTPVLITNVVDALGKAGAKGTLPRA
LDAIADQTKPPTVVVRVAEGADEAATTSNIIGGVDADGKYTGIKALLAAQNVLGVKPRILGAPGLDTQAV
AVALAAMAQKLRAFAYISAPGCKTKEEAAAYRENFGQREVMVIWPDFKVYDTATNATATAPASARAAGLR
AKIDNDVGWHKSLSNVGVLGVTGISRDVDWDLQDPSTDANLLNENGVTTLVRRNGFRFWGNRTCSDDPLF
AFENYVRTAQVIADTIAEAHMWAVDKPLTPSLVRDIVEGINAKFRDLVANGYILGGEAWFDPELNTKETL
KAGKLYIDYDYTPVPPLEHLTFRQRITDRYLVEFVEEV
>gnl|CDD|222877 PHA02561, D, tail protein; Provisional
MLIDTPLSAGLGPTPVFRLTVDGKDITNLIAPRLISLTLTDNRGFEADQLDIELDDTDGRLGLPRRGAVL
TLEIGWAGEPLVDKGDFTVDEVEHSGAPDTVTIRARSADFRGTLRSRREKSWHRTTLGDIVRAIAGRNNL
TPRVAPALAGIPIDHIDQTQESDASFLTRLAKRYDAVAKVKGGKLLFAPAGQGKTASGKQLPVITLTRSD
GDSHRFRIADRDNYAGVRAYYHNTKTGKRKGQKEPAAGKGKIAGGETENVKRLRHTYATKAEARRAARAE
WDRLQRGQATFSITLARGRADLAPELPVEVSGFKPEIDEGEWSIDKVTHRLNRGGGYTTSLELEVKLDDV
E
>gnl|CDD|222878 PHA02562, 46, endonuclease subunit; Provisional
MLKFKKIRYKNILSVGNQPIEIQLDKVKKTLITGKNGAGKSTMLEALTFALFGKPFRDIKKGQLINSINK
KDLLVELWFEYGEKEYYIKRGIKPNVFEIYCNGKLLDESASSKDFQKYFEQMLGMNYKSFKQIVVLGTAG
YVPFMQLSAPARRKLVEDLLDISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKK
NGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKM
YEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNK
QSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKDSGIKAS
IIKKYIPYFNKQINHYLQIMEADYNFTLDEEFNETIKSRGREDFSYASFSQGEKARIDLALLFTWRDVAS
KVSGVDTNLLILDEVFDGALDAEGTKALLSILDSLKDTNVFVISHKDHDPQKFDRHLKMEKVGRFSVMVE
NI
>gnl|CDD|222879 PHA02563, PHA02563, DNA polymerase; Provisional
MGKMNKKKHKPRKILACDFETTTINKDCRRWFWGEIDVEDFPSYYGGNSFDEFLQWIEDTTYKETECIIY
FHNLKFDGSFILKWLLRNGFNWILELRVRSSKNFDTTIFINGRWYTITDSFMKFRDSLKLLPFSLEKLKK
DFGLTILKKDIDLNKERPVGYEFTTFEKLDPEELEYIHNDCVIIAGMLDIHFSEGFTRFTTGSDAMTVYK
ELYQKIKIKYTHFPILDLGFDDFIRKFYRGGRTWYNPKYIGKLIEEGYVYDVNSLYPYVMYNAKLPYGEP
FYEKGKPAELKPDPLYIYNYGALFKLKKGYVPDDMLIQIKSNLDFNGRLVLKVGIVKYVNSGNEYVDLNL
NNLDLELEITHYDAFNEEVESGVVFECETGLFRDFIDHFYEIKTNSKGAKKQNMLAKLMLNSLYGKFALN
PDNTGKVPYLDDNGRLDLISNGEENKEPNYIPIAAFITARARSNLLSALQYLYEKFIYCDTDSIHLEGAE
TPKLPKDMIDPKELGKWDHEGEFIKAKYLRPKKYALYAEEVNGKLKIKCAGMPKNIKESVTFENFVIGYS
QRGKARPFFVNGGVVLKKFSIKIKINTISIYLSEMELVIGNVYEQKRDIELRLKYEFIKKEARENLDYDE
>gnl|CDD|222880 PHA02564, V, virion protein; Provisional
LGMALQPRGIRNNNPGNIVWSARNNWQGQLPHNPKIEPRFARFDTPHNGIRALAKLLLNYRKVYGLRTVE
SLIARWAPSNENDTRAYATAVANAMGVPPQAGLHLDQDTLAALVTAIIRHENGQQPYSAEQIAQGVREVL
Y
>gnl|CDD|177395 PHA02565, 49, recombination endonuclease VII; Provisional
MLLTGKSYKEEKQKLFEAQNGICPLCKRELDGDVSKNHLDHDHELNGPNAGRVRGLLCNLCNALEGQMKH
KFNRSGLKGRGVDYIEWLENLLVYLKSDYSDNNIHPQFVPDKVKRFSRLTKEEMIAEMDSRGFEYNDSDT
KAELIKKFKKQFRKALK
>gnl|CDD|222881 PHA02566, alt, ADP-ribosyltransferase; Provisional
MMELLNEVFDSAGKLPVVNLNPKAKVPQIFAIQAPGKENLVPRFCNYTSKGDAVKQVKPGDKFMHVVLMQ
LSEKGSLAELKGGLGSDPIGAMNSIFDVVMETMKKYRMDAVLFRFPTKKLKGQAKTVQRIAERLVRTRGG
GRFKVLPEMWQFSKKYTYILVYRKSANIEDIKGLPEIDPELYTKVESKVGDVYISKKTGEKVTKVEAIAA
SIAKEEEKRTDQAVITKTKISRRAIAKAQSLESDREAELFQKFENSANDYNKPAEAPLIPPAEEIKTNEG
SGAIKTMVAASRFESSDYELDYFRKFIFLRHIGEVDEKIKLKISEAIKQEDQTSIKNLEKFAASVDELLE
DYKDIVFENSLDALEWINDLNKGRKGMPDEVKAELTRSKWKQAKTKFLMRAIYKFARESASQMYEITGAR
DPKKLTPAESRAIREYCASGYIDINNFLLGRYKPEFYMDEEEAEKAIDNLDSAFKNGDKLPEGTTLYRGQ
SVTSKIYEALVKNKVFYFKNFVSTSLKPNIFGGFGKNYAAIDLLEPEVRDELAVDKGEEGGTISANELAQ
VGFAIDGAEKVPVIYPGNLSEHPEEAEIILPRGLLLKFNKVTDASMNDGSQNTYLIEAEVMSKSELDESE
VIYDGDHLMETGEVKPMTGFSSFVSSESKEKKEESLQILASLIDIDGMPPKFKQ
>gnl|CDD|222882 PHA02567, rnh, RnaseH; Provisional
MDLNSFMDEDDDKEGVNLIDFSQIIIATIMANFKPKDKINEAMVRHLVLNSIRYNVKKFKEEYPEIVLAF
DNSKSGYWRRDIAWYYKKNRKKDREESPWDWEGLFEAINKIVDEIKENMPYKVMKIDKAEADDIIAVLTK
KFSAEGRPVLIVSSDGDFTQLHKYPGVKQWSPMQKKWVKPKYGSPEKDLMTKIIKGDKKDGVASIKVRSD
YILTRVEGERAPSISTKELEAIADAEDPKVLLTEEEYERYDENRELIDFDFIPDDIADKIIEAYNSYKPP
PRGKIYSYFVKNGLSKLLQKVNEF
>gnl|CDD|164963 PHA02568, J, baseplate assembly protein; Provisional
MAIIDLSQLPAPDIVEVLDFETLLAERKAALISLYPEDQQAAIAATLALESEPLTKLLQENAYRELLLRQ
RVNEAARAVMLAYAEGSDLDAIAANFNVERLVVTPADPNAFPPVPAVMEDDDSLRERIQLAPEGLSVAGP
RLAYQFHARSADGRVADASATSPAPAEVVVTVLSREGNGTASEDLLAAVRAALNREDVRPVTDRVTVQSA
TIVPYQIRATLYLYPGPDSEVILAAAEARLQAYANDQHRLGRDITRSAIYAALHVAGVQKVELLSPAADL
VLTLTQAPYCTGIELTVGGV
>gnl|CDD|177398 PHA02569, 39, DNA topoisomerase II large subunit; Provisional
KDEFKVLSDREHILKRPGMYIGSVAYEAHERFLFGKFTQVEYVPGLVKIIDEIIDNSVDEAIRTNFKFAN
KIDVTIKNNQVTVSDNGRGIPQAMVTTPEGEEIPGPVAAWTRTKAGSNFDDTNRVTGGMNGVGSSLTNFF
SVLFIGETCDGKNEVTVNCSNGAENISWSTKPGKGKGTSVTFIPDFSHFEVNGLDQQYLDIILDRLQTLA
VVFPDIKFTFNGKKVSGKFKKYAKQFGDDTIVQENDNVSIALAPSPDGFRQLSFVNGLHTKNGGHHVDCV
MDDICEELIPMIKKKHKIEVTKARVKECLTIVLFVRNMSNPRFDSQTKERLTSPFGEIRNHIDLDYKKIA
KQILKTEAIIMPIIEAALARKLAAEKAAETKAAKKAKKAKVAKHIKANLIGKDAETTLFLTEGDSAIGYL
IEVRDEELHGGYPLRGKVLNTWGMSYADILKNKELFDICAITGLVLGEKAENMNYKNIAIMTDADVDGKG
SIYPLLLAFFSRWPELFEQGRIRFVKTPVIIAQVGKETKWFYSLDEFEKAKDSLKKWSIRYIKGLGSLRK
SEYRRVINNPVYDVVVLPDDWKELFEMLFGDDADLRKDWMSQ
>gnl|CDD|177399 PHA02570, dexA, exonuclease; Provisional
VVDFIIDFETFGNTPDGAVIDLAVIAFEHDPHNPPTFEELVSRGRRIKFDLKSQKGKRLFDKSTIEWWKN
QSPEARKNLKPSDEDVSTYEGHKKFFEYLEANGVDPWKSQGWCRGNSFDFPILVDVIRDIHNTRDTFKLE
PVKFWNQRDVRTAIEATLLTRGMTTCPLPKGTLDGFVAHDSIHDCAKDILMLIYAKRYALGLEDLPTEEE
PDPLSVKKKR
>gnl|CDD|177400 PHA02571, a-gt.4, hypothetical protein; Provisional
MLDESTDVEELTDEEVEELLSELQARNEAEAEKKAAKILKKNRREIKRLKKHAEEALFDNNKEQYVYAIK
KLRDIYKQPYTDELIETMWETSRQQILDMINSASKKVTA
>gnl|CDD|222883 PHA02572, nrdA, ribonucleoside-diphosphate reductase subunit alpha; Provisional
SMIINVIKSSGVSQPFDLEKIHKVLEWACEGTGVDPSELEENSKIQLRDGMTTKDIQEILIKSAADLISV
EEPDYQYVAARLLMFALRKQVYGQFEPPSFIDHISKCVNEGKYDPEILSKYSAEEITYLESFIDHDRDFE
FTYAGAMQLKEKYLVQDRSTGEIYETPQFAYMLIAMALHQDEPKEDRLEHVIRFYNAVSTRKISLPTPIM
AGVRTPTRQFSSCVVIESGDSLDSINKTAMAIVKYISKRAGIGINAGMIRAEGSKIRGGEVRHTGVIPFW
KHFQTAVKSCSQGGIRGGAATAYYPIWHLEVEDLLVLKNNKGVEENRIRHLDYGVQINDLMYERFIKNDY
ITLFSPHDVGGELYDAYFADQDRFRELYEALEKDPSVRKKRIKAQELFLLLLKERSETGRIYIMFIDHCN
NHSPFKDPIRQSNLCCEIALPTKPLNHIDGEGEIALCTLSAIVLGNFEDQDEIEELAEVAVRALDNLLDY
QDYPVPAALKAKKRRSLGVGVTNYAHYLAKNFASYEDANADLVHELFERLQYYLIKASNKLAKEKGACEY
FSDTKYSRGELPIDWYKKKVDELVAPKYNCDWESLREDLKKYGIRNSTLSALMPCESSSQVSNSTNGIEP
PRGPVSIKKSKEGPFNQVVPNVETLKDLYDLLWDLAKKGNKGYLTQVAIMQKFVDQAISANTSYDPENYP
NGKVPMSVMLDDLLYFYYYGGKTLYYHNTRDGKGTEDYEIETPKAEDCDSCKL
>gnl|CDD|222884 PHA02573, 30.3, hypothetical protein; Provisional
ELDIGSGFPYPSCALSNFAPHPFVMDGIQCGSMEGFLQSLKFKNPEMQRHIFGLSGKAAKFKGRKKKWAQ
DQTLYWKGVPIHRYSEAYQELIENAYFEMAIQNKGFRKALLATKNKVLTHSIGKLKKNETILTEQEFCSN
LNRLRDLL
>gnl|CDD|177403 PHA02574, 57B, hypothetical protein; Provisional
MKSFLEFSQGTYVAAKFSEATLDALERLQRTLRIPNPVPRDKLHSTIVYSRVYVPFIPASGSTEVASSGH
LEVWETQDKNALVLVLESEYLQCRHKYARALGATHDFDDYTPHITLSYDVGPLSFSGDVDIPVVLDHEYK
EPLDLDWTE
>gnl|CDD|222885 PHA02575, 1, deoxynucleoside monophosphate kinase; Provisional
MLIAISGKKRSGKDTVADFIIENYNAVKYQLADPIKEILAIAMGRYGADDLMFVPGLTYDDFDGIGYDRE
APLPLSNEDVIRIFEQALMLLNDKGTCYLLYAHYDKVYEIILNNNNPWSIRRLMQTLGTDIVVNFNKMYW
VKLFALKYLDKFKSDYDYFIVTDVRQDHEMELVRAMGATVIHVVRDTGLVDTHSTEAGLPIQPGDIVITN
NGTLEELKSKILNLIKF
>gnl|CDD|177405 PHA02576, 3, tail completion and sheath stabilizer protein; Provisional
MMQLFNQANPTNFRLDIPDSNGTKGFTLNVQGVTIPGIRIPPTDIPLGPQGLARAKIPGSTVEFDPLIVR
FLVDEELRSYLEVYKWMLSTNDYNTGNSTAWDKSQPEAITLHILDNSKTKIVATFNFYGAWPSDLGEIEL
SYTEDSDEAVVCTATFPFKYFEIEKDGKLIVPRPAIQ
>gnl|CDD|222886 PHA02577, 2, DNA end protector protein; Provisional
NEAEPQKPKEKPKRNEKQWSLEWFTETIKKDIRGHQVVKPQPGRLYTFEYDAKHKDTLPYWDRFPLIIFL
GSGQSKAHTLMYGLNLHYLPPKARQLFLEELLKQYASTPTLTNKTRLKINWSNVKGMRGADHMIKAYLPG
HIKGSLLEIAPKDWANAIFLPTQQFVSKGKRYDARKVWKET
>gnl|CDD|177407 PHA02578, 53, baseplate wedge subunit; Provisional
MLFSFFDPIEYNGKTTTDIFRNYRAYFNRVIPSYTLRTYYITGSPRPEQLAHELYGNQQLYWVLLMLNDN
YDPFYGWITSQEAAYQAAIQRYKNVGGNQVLYHVDENGEKYYNLVEDPDNPYNWYDKGDKARRYLQYHGA
LAAVDTYEDAVLRNEEKRKIKIISPSDINSFISDLIREMEK
>gnl|CDD|177408 PHA02579, 7, baseplate wedge subunit; Provisional
MMIKAPSVTSLRIDKLSANQVYLTWDDVGANFYYFVELAETRDADGELIPDDELRWINLGYTANNEWFED
KLQPNTYYKFRVAVAAQGFEQSDWVYTEEFETFETNAYTFSTMREFTPANKFIEEKFTKNNQNYVNFNTD
VIMASLMNEDFVFSPAYSNVSSISNFIVTDENYHEIQGHIEKVCKDINRTYLMESDGVLYLFERFQPMAK
VSNDKGQTWKYYKAFNDRVGNPVSRTVYYQSNTTTYVLGYDRIFYGRKSTDIRWSADDVRFSSDDITFAK
LGDDLGLGFDVEIFGTYARLPGDVSRKAEAMACSDDWIYVAARDKVRRIKTSNAPIDTDPGSPTYGEKIF
DPDVYTITGNPKAVVKKMDVIDGKLYALVTGEVKTLNADPTRPENVVPSDDKGVYRLDEDGKTWTRVFGN
TEEERRRIEHGYTNMSTDGEEVFISSSNFKFPGTVPDPELPAKYPEVIEAVKYELEPGYLADKHIHMMTF
RANESDGETWKPGPQAYYNEAFFSWMRRSGTRCWITNDNRALVVYPEIIYTKVIDDAGDSSPDRVNKEVW
DKGTVTIYAPNVKFTGFKKYASGVLFHKSTGEIIGYYEFPYRVRDTVPIIWKPTNVMLTAELQNQERETP
WVPAEEPGLQDPDLRPLITKMMPESYLLDDSNFEKFCEYYLQFLSDGSGTYYNNLLNLIRNKYPREEHAW
EYLWSEIYKRNIYLDKEKRDAVVRFFESRASDFYSTKGIEASYKFLFKLLYNEDVEIEIESSNGIEYDIV
VSSTNISEDIVGRTIYTPTGRANVTYIEREYENGKLRWRVTIHNLIGRFIEGQVIKSERTSFEGEIIRGV
RGKELLSNSIDYINRSRSYYVMKIKSNLPTSRYKDDVLRFVHPVGFGFIGITLLTMFINSGLSMKHTETI
IDILKNYRWDSGLPSEYPDRVAKLDPDGNIEFDSVTGEALYLPGPKAGEPFDLPPEYDAENNNSIFQGQL
PSERRFAMSPLFDQSAVTFSQFRELVDKRLKDDIGNPRDPKNPTQVKIGE
>gnl|CDD|177409 PHA02580, 8, baseplate wedge subunit; Provisional
MNDSSVIYRSIVTSKFRTENLLNFYNSVGDGPDKNTIYATFGRSEPWSDNENDPGFAPPYPNDSTDGVVD
MWTHMMGAVKIPKSMLDAVIPRKDWGDTRYPNPKTFFINDIVVVNSAPYNRTDSGAGWMVYRCVDVPDTG
SCSISSITNKVECIKLGGKWTPTHESVEPPRGTGDAIDMGDGYVWEYLYTIPPDVSINRCTNEHIVVPFP
EELIEDPARWGYENNITWYPDDYDLIYRVKANTLRFRAYLDSVYFPEASLPGNKGFRQISIILNPLEKKA
HPADPDVKATKDYYDPEDLERHSGEMIYMENRQPIIRSLDQTEEINIIFEF
>gnl|CDD|222887 PHA02581, 9, baseplate wedge tail fiber connector; Provisional
IQTGKKLIDTGEIGNPSTGDILYDGGVKLNDNINAIYNAFGDQRLTAAAEGGATGQILHATGYYQKHPRT
YYAGTPVELGSLHDIDTSTGGLTVTLPKGKLGEGVEFINSNGSISVTNPLEIRPQAGDSIKGVSGTLTIT
SPYSKVTLWCIKSEGSTSVWDYSIESMFGDKTMPVNKTYNIITSVPTDIPLFGKTEYSAAKLLVTAENAD
GTVTKTAETLLLIDNNANKVYSTEYAVIKNDNDEDELYNIRFRIGNGDVVYAIVSSTSDNIRFAIKAIDT
IKIG
>gnl|CDD|222888 PHA02582, 10, baseplate wedge subunit and tail pin; Provisional
MKQLINIGNVVDDGTGDYLRRGGQKINDNFTELYYELGDGDIPHAAGAWKTHSSDGPTLKPNFGKSWAIN
TSSGRITVNLPKGSVSDYNKVIRLRDVWSTWAANPVTLVPASGDTIKGSASPVELNKNFMDLELVYCAPG
RWEYVENKQVDKITTSDLSTVARKEFIATQGQTDFPDVFGGNSYNVANVEVYYRGNLLYYGDDLSDNSDY
GSPGANPGELVPLDGKSIRLRQPCNAGDTVQIVTYMDGIASWRSSYNRRTIRVYDTKLTTKTSVPGEIWV
GDLSTKKSFTFAEFGLSPNEPINPNSLEVLLNGTLLTKAGTADLPSFICEGADGDTETGCSANGGQWVPS
GTDYSLVFDDNGKVTSIKFGRALESGDIITIRWFNNDIGTLLEWDGDGGIKEKTDKIYLSNEDEVTLTGQ
IEYTDFDNPSQPNVEPVPEPYTGRINTIQSIFDSIYPIGTIYENANNPNNPATYMGFGSWKRYAEGRFLV
GWNSDAADPNFALNNNDLDSSGNPSHTAGGTGGSTSVTLKKENIPELQSDDKVLIADDNGNIIIGGCQVD
PDATGPGYTKYREDVAKVNKGNTTPANINNLPPYITVYRWLRVA
>gnl|CDD|222889 PHA02583, 11, baseplate wedge subunit and tail pin; Provisional
ITKTREKAGVISRLADFLEFDTGKKDPDVMGNRPIGGPTIDQLQKGVYYPNVQSAIDDLATLAELPVGGV
IITTENVSPEGVQQVETLTFSGTVTDSDPDGDKVIIHVYGIPVVVTVGTSAVEVCEKVLTKFTEMVAKSI
YFAEVSRKGTDGPKLEVKYIDSQEHILENYSQYGITVTGEIDSPARPGYGTWELLGEETKTLTTVTGPTT
LYYFKRIA
>gnl|CDD|222890 PHA02584, 34, long tail fiber, proximal subunit; Provisional
MADIKQAFRATSGLDAAGEKVINVAKADKNVLTDGVNVDFFIDENTIQQYDPTRGYDKDFAVIYNNRIYY
AKADITAPAGAFDPTKWKATRTDPKWITVNSTSGDLQLKSGEYIAADGRFANLTFTLPTNPTDGDTIVIK
DIGGKVGVNELLVNSSNQSIVRFRGNQSASVRITHPYSTNVFIFNGNLWQVYEAGYERRSVYVEPTGAGF
QAQSGDTVFRRTSGGTITLTLPKYANHGDMITTVDLDGLNSVNHTTVEVYPGSGHSIGENGVHSIESRTS
GDGFFIFDSTEKLWRVWDGDQKVRLRVIRDDTNLLPNEYVAVFGANNGTTQTVTLTLPTDVADGDRVKIS
MNYMRKGQNTVKIKAASGDKIASSKNLLQFPKRSEYPPTDEWVLVSELSFNANTDYVPYLELSYIEDDST
GRKYWVVAQNVPIVERVDSTDRARLGVIALATQAEANKNHEQNPSKELAITPETLANKTATETRRGIARI
ATTAEVNQNTTFTFLDDVIITPKKLNERTATETRRGVAEIATQAETNAGTDDTTIITPKKLHARQASETL
TGIVKLVSTAGTAPAAARGTAGTGVYNKNDHNRVVTPKALDEYKATETQQGVVYLATQAEVIAGTSASGN
APLLVTPETLHARTATDTRIGLIEIATQAETNAGTDDTRAVTPKTLNDRTATETLTGIAEIATQVEFDAG
TDDTRISTPLKIKTRFDNTARTSVDAASGLTESGTIWNGYTLDILLATETQRGTLRVATQTEANAGTDDD
TIITPKKLQGKKATETLEGIIRVATQAETVTGTSANLAVSPKNLKYIVQTEPTWRATEARRGFVKLATGS
NTFVGNDTVGSTQPLTNYEKDGYAVSPYGLNYALQNYLPLKATAQNSLKLDGLDSAQFIRRDIDQTVNGS
LTFTKNTNLSAPLVSSSTATFGGSVTANSTLTTQNTSNGTVVVVDETSIAFYSQNNTTGNIVFNIDGTVD
PINVNANGTLNATGVATNGRAVYAEGGGIARTNNAARAITGGFTIRNDGSTTVFLLTAAGDQTGGFNGLK
SLIINNANGQVTINDNYIINAGGTIMSGGLTVNSRIRSQGTKASYTRAPTADTVGFWSVDINDSATYNQF
PGYFQMVTKTKSPGTLTQFGNTLDSLYQDWSPDGRTTRYTRTWQKNKNAWTSFGEVYTKGNKPTAEDIGA
VPADGGTMGNLTIRDWIKIGNVRIIPNPVTKTVKFEWEE
>gnl|CDD|222891 PHA02585, 16, small terminase protein; Provisional
GLDINQLLDISGLPGIEDGEEVVVYEPLVLKEVESHPANRKPDLEDDYSLVRRNMHFQQQMLMDAAKIAL
ENAKNSESPRHVEVFATLMGQMTNTNKEILKIHKEMKDITEEQTGTKKGEPQGDQMNIENATVFMGSPTE
LMDEVGDAYEEEEKVINGETV
>gnl|CDD|222892 PHA02586, 68, prohead core protein; Provisional
MILIPEDYELVLELVEAVLPEAQGRVDILSEAFAKDEINGVIENMLDDEPDLALAMLSINENMSLNEAIV
KHVSSRGEVTRTKDRKTRERNAYQTTGLSKAKRRQIARKAAKTKRANPSIQRKAQRKRKKALKKRKALGL
>gnl|CDD|222893 PHA02587, 30, DNA ligase; Provisional
MILDILNELASTDSTKEKEAILKENKDNELLKEVFRLTYNKQINFGIKKWPKPGHVEGSDGMLSLEDLLD
FLEFDLATRKLTGNAAIEELAQILSSMNEDDAEVLRRVLMRDLECGASEKIANKVWKGLIPEQPQMLASS
FSEKLIKKNIKFPAYAQLKADGARCFADIDADGIEIRSRNGNEYLGLDLLKEELKKMTAEARQRPGGVVI
DGELVYVEVETKKPNGLSFLFDDSKAKEFVGVVADRATGNGIVNKSLKGTISKEEAQEIVFQVWDIVPLE
VYYGKEKSDMPYDDRFSKLAQMFEDCGYDRVELIENQVVNNLEEAKEIYKRYVDQGLEGIILKNTDGLWE
DGRSKDQIKFKEVIDIDLEIVGVYEHKKDPNKVGGFTLESACGKITVNTGSGLTDTTHRKKDGKKVVIPL
SERHELDREELMANKGKYIGKIAECECNGLQRSKGRKDKVSLFLPIIKRIRIDKTEANTLEDVFADLI
>gnl|CDD|222894 PHA02588, cd, deoxycytidylate deaminase; Provisional
MKDSTYLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDHANEQGWLDDEGKLKKEHR
PEHSAWSSKNEIHAELNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYDRNGPGWD
DILRKSGIEVIQIPKEELNKLNWESNQN
>gnl|CDD|222895 PHA02589, rnlA, RNA ligase A; Provisional
KKMQELYNNLMALCKDEKGKFFFKDDVTAMGTKYRIFSYNYASYSDWLKPDALECRGIMFEMDGDKPVRI
ASRPMEKFFNLNENPFTMGLDLNDVVYVMDKEDGSLISTYLDGGYLLLKSKASIKSEQANDANGLLYSPE
NEDLRERLTELAGDGFTVNMEYVAPTNRIVLAYQEPKLILLNVRHNETGEYVPYDDLFKDAALRPYLVER
YPIEEADEDDWVDEVRAAEGIEGYVAVMKDGQFFKLKTDWYVALHRTKDSINNNEKLFYTIVENATDDLR
ALFADDEYSLEKIEAFETAFLDYLDRAFALAFDAYNKHKGKDRKDYAIEAQADLKGDGRYLFGILMQAYQ
GDTDYEKVMDAIESVFLKNYKKFIPEKY
>gnl|CDD|164985 PHA02590, PHA02590, hypothetical protein; Provisional
MQVEEMQEKVINLAQKYTNQKRILRLIRRSNIEEKIIKEISEFYGIREDNIELFNNEIEFMFKKEYKNKD
EKIEVITSVKLKLKKENNKLKLLNIKMEKSISKIS
>gnl|CDD|164986 PHA02591, PHA02591, hypothetical protein; Provisional
MKVERYKCKKIEKTLNTSLCICYIGEKKMQKVVQVGQTRYFVESEDDLISVTHELARKGFTVEKIASLLG
VSVRKVRRYLESC
>gnl|CDD|222896 PHA02592, 52, DNA topisomerase II medium subunit; Provisional
MQLKERSLKSIVNNEALEYAMYTVEERAIPNLIDGLKPVQRFVIHRALEYAKGNKEKFDKVAAIAGGVAD
LGYHHGETSAQDAGALMANTWNNNIPLLDGQGNFGSRLVQKAAAARYIFARVHDNFRKIYKDEDLAPVHE
DPEHIPPAFYLPIIPMVLLNGVSGIATGYATNILPHSPKSVIKAVLAALNGKDITEPKVQFPEFKGEVVE
IEPGSYEIRGTYELNGKTKLHITEIPVKYDRETYVAVLDPLEEKGKIVSYDDCTEDGFRFKVTLKREENE
EATHEKIMKDFGLIERVSQNITVINENGKLKVYENAEDLIRDFVEIRKTYVQKRIQYEIKETEEAFDLAL
AKAEFIKRVIAGEIVLQGKTRSELTEELSDNKDFGEYADKLVAMNIYSMTSDEREKLQKEAEELEKEHEY
WKKTTAKKEYIKDLEELKK
>gnl|CDD|222897 PHA02593, 62, clamp loader small subunit; Provisional
MSLALFDDDEQLNEHEIAWRSKDWDAVQELADSFKEKAENELFAIIDDITYGKTPRNVANNSDYDKFFIN
NALSQHAECLYPAYVMNLIGSGLSDQAHFNYLLASVRKGKRYGKWAKLTEDSEEKLIIKLLAKAYSVNTD
DAREYLDILKKKGKLPDVLKRLKGLVTDEFLKGVTKNVKEQKQLKKLAKEW
>gnl|CDD|222898 PHA02594, nadV, nicotinamide phosphoribosyl transferase; Provisional
MSTFLANVNIILMTDSYKLSHWSQYPKGTDYVMFYLEPRGGKFFDKVVVFGIQYFVKKYFFEPITMEVVE
EAHELVKAHLGKDVFNREHWEALHDLGYLPIEVRAVPEGTVVPVKVPVLTIENTHPDFFWLAGYLETVIL
RGVWYPSTVATLSRECKKILKKYLKETSDNEDEVLDFQLHDFGARGMSSGESAALGGLAHLYNFKGTDTV
EALYMAKRYYGDDEVEMAGISVPAREHSTMCSYGAENEDEAFKNSLTLYGTGIYSIVSDTYDFKRAVTEI
LPELKDEIMARGGKLVIRPDSGDPVDIICGALETLGEIFGGTVNSKGYKVLDEHVRLIQGDGITLERINR
ILTRMKENGFASENVAFGMGGGLLQMVTRDTFKFAMKATAIKINGKWKGVFKNPKTDEGKKSKKGRLARV
KDGGSFKTVDGLEEQSEADLNDALVTYFDDGKLVRYQSLAEIRERSDIQA
>gnl|CDD|222899 PHA02595, tk.4, hypothetical protein; Provisional
MIVDYIKGDIVALFLQGKGNIAHGCNCFHTMGSGIAGQLAKAFPQILEADKLTTEGDVEKLGTFSVWEKY
VGGHKAYCFNLYTQFDPGPNLEYSALMNCFEELNEVFEGTLFKPTIYIPRIGAGIAGGDWDKIEAIIDEA
TPDIDIVVVEYEKS
>gnl|CDD|222900 PHA02596, 5, baseplate hub subunit and tail lysozyme; Provisional
EMINNNLKWFVGVVEDRMDPLKLGRVRVRVHGIHPAQKAKGDVYGIPTEDLPWMSVIQPITSAAISGIGQ
SPTGIVEGTHVYGHFLDKWKQNGLILGTYGGIYREKPNTNEGFSDPTGQYPRYVGNDVNVLARGGEVGYD
PSSVVIQDANTDVAINPDDTPLDEIPPDDNPDFTIEKMLRRDEGIRLKVYWDSEGYPTIGIGHLIIREKT
RDMAQINKLLSKQVGREVTGGRITAEEASKLFARDLAKVQRDISRHSKVGPVYNKLNRSRQMALENMAFQ
MGVGGVAKFKNMLAAMLAGDWKKAYDALRDSLWANQTPGRASRVSKIILTGNLESYGVMVPDPPGRSLST
IAAYKTAVATSSDPADPFTPGDTRIMFKEPKSSYSAEYPYNHVMESESGHIQEFDDTPGHERYRRVHPTG
TYEEIRPDGTRVVKIVGDDYYIVKQDRNVNVKGNLKVVVEGDAIYYNMGNVLQTIDGNVTIFVRGNVTKT
VEGNGTLYVKGNVTVQVDGNLDATVKGNATTLVEGNQTNTVNGNYKLKVEGNFDMTVGGNWSEQMAGMSS
IASGTYTIDGSRIDIG
>gnl|CDD|222901 PHA02597, 30.2, hypothetical protein; Provisional
MKPTILTDVDGVLLSWQSGLPYFAQKYNIPTDHILKMIQDERFRDPGELFGCDQELAKKLIEKYNNSDFI
RYLSAYDDALDVINKLKEDYDFVAVTALGDSIDALLNRQFNLNALFPGAFSEVLMCGHDESKEKLFIKAK
EKYGDRVVCFVDDLAHNLDAAHEALSQLPVIHMLRGERDHIPKLAHRVKSWNDIENA
>gnl|CDD|222902 PHA02598, denA, endonuclease II; Provisional
EILEEYGFIKYAELELDKNGRIDRSFIKCPNKKNVIYAIAVDDELVYIGKTKNLRKRIDYYRNSKNWRNT
NTSDITKSALLEEALKKGKKVEFYARQCFNLSITNPLGSMTIATMDLEEPKFIKKFNPEWNKQHKKKQ
>gnl|CDD|222903 PHA02599, dsbA, double-stranded DNA binding protein; Provisional
ETKAKKEKVEFNPAVHGERLAQLIKEASDHKTQIEAYGEMIKDIKDRAKTELGVDGKMFNKLFKLYHKQE
REQFEAENDEVVELYDTIFKA
>gnl|CDD|164995 PHA02600, FII, major tail tube protein; Provisional
MALPRKLKNFNVFNDGASYQGVVEEVTLPKLTRKLEAYRGGGMNGPVKVDMGLEDLELEWTVGGFEVELL
KQYGAVSVDGVPLRFAGSYQRDDTGEVDAVEVVVRGRHKEIDMGTAKAGEDTEFKVTTSLTYYKLTVNGE
ELIEIDTVNMVEKVNGVDLLEAHRRAIGL
>gnl|CDD|222904 PHA02601, int, integrase; Provisional
MAVRKLKDGKWLCEIYPNGRDGKRIRKRFATKGEALAFENYTMAEVDDKEWVGEKEDRRRLSELLQIWWD
LHGQTLEDGKARLAKLLILCKGLGDPIASEFTAKDFADYRARRLSGEFKVNKGRPIKPATVNRELAYLSA
VFNELIKLGKWSGPNPLDGIRPFKEAEPELAFLTKEEIERLLDACDGSRSPDLGLIAKICLATGARWSEA
ETLKRSQISPYKITFVKTKGKKNRTVPISEELYKMLPKRRGRLFKDAYESFERAVKRAGIDLPEGQATHV
LRHTFASHFMMNGGNILVLQRILGHATIEMTMAYAHFAPDHLEDAVSLNPLSN
>gnl|CDD|177427 PHA02602, 56, dCTP pyrophosphatase; Provisional
MAHFNECAHLINGLDKAENAYKDILAENKDPLQVMLDMQKSLQVRLANDKPEYNPHPDELKTCGEILDWL
RNQDDYIADETRELYTSLGGMSNGEKDASAVWKPWKANHGEARNRLFSDLSPEDQLEIKFELIDQLHFVL
NKFIALGMDAEEIFKLYYLKNAENFARQERGY
>gnl|CDD|222905 PHA02603, nrdC.11, hypothetical protein; Provisional
MKTVMKGLFGSHLYGTSTPESDVDYKGIFLPHPRDILLGNAKKHMSKSTGNTKSKNTKDDVDHELYSLKY
FIKLAADGETVALDMLHTPDDKVVKSPDVWQYIQDNRSRFYTTNMKAYLGYVRKQAAKYGVKGSRLAALR
QVLDVVNAIPEQWVDYQEDGERTKVEDIKHRLPSNEFCFWVFHNHEKTGPQTFYTVLGRKYQTTITFAEF
KQSLNKLWAEYGERARKAEANEGIDWKALSHAMRGGLQLLEIYKTGDLVYPLKDAPFILDVKAGKHPFKE
VQEFLEEIVDEVEAAADEASKNGMPQKVDMEFWDDFLEEVYLENVNSYYK
>gnl|CDD|177429 PHA02604, rI.-1, hypothetical protein; Provisional
MKFSDFSESGKTSKVDEFIGACLMSVAYFHSAHFETKSYARHKAYEFFYEEMPDLIDKFAEQYIGISGRK
YKPSLPSASELDTIAFLDELLQEAEEIYKELPSALQSTLDDITGLCYQTKYKLTLE
>gnl|CDD|177430 PHA02605, 54, baseplate subunit; Provisional
MYSLDEFNNQAANKDFQRSNLFSVVFATTPSSKSQALIDGFGGFLYNNLPLNNDFFGLTQGDISQGLTTL
VTAGTQSLIRKSGVSKYLIGAMSSRTVQSLLGQFEVGTYLLDFFNMAYYNSGLLIYSVKMPENRLGYEMD
YNHNSPNIRITGREYDPLVLSFRMDSEASNYRAMQDWVNAVQDPVTGLRALPDDVEADIQVNLHNRDGLP
HTVVMFNGCIPVSVSSPELSYEGNNEITTFDVTFAYRVMQTGAVGRQAALEWLEDAAINGIQGFFGNNGL
SASVSKLSRLGGAAGALRNIVTGQG
>gnl|CDD|222906 PHA02606, 5.1, hypothetical protein; Provisional
MANILPMSTDLPDIMEGESIDVTFTAQLETGETLVSINITEYEPNEGITVEGNRLYGTYESVFSLGNDAL
KYRLKDDEFKTASSWEDLPDPSTADLYLFKAPQNLQKTFTYEVTLIYDYQEPSESGGSGSGSNSSEGAGE
TNPPPAPVRKTLTKVYTQTVVGNWSVWANQLRDYVYRGP
>gnl|CDD|177432 PHA02607, wac, fibritin; Provisional
KLNLKELPFVDGVPDEGQTRINWIKNGECLSGASTKTGNDGSLNRAGVNVQKNVEQLDENTKKTKDKINE
VVDDVNTIQENLDVIGDISVIDQINQNVADIEVLKKDVSDTTDKLAGTTNEVDEIEADIGVFNPEADPVT
RTIRNDILWIKTELGAYPGFDINGNPDPGSTGTGMKYRIIDNTTALVDHGQRITELENDWADSDVGQLTR
EVNDLRAELGPSSLATGEPIYTRLNTLEDAITGINSDIDEIKTAIGFPGTTSIITRVTTLESNISSLNNQ
VNGPVTGIKPRLTAIETQIGSDSIPGSIKYRISNNTTDISDLNSIVGESSSDGLRGEVAWLNQRIGTDSS
PGSINGRLSVVETEVNQLTNSVQDLQVEIGNNSSGLKGTVIKLSTDVYGDNPSGDTFEERGLKKTVKDLE
TQIAGKLDDAPSDGSWYVRKNGAWVEVSTGLSPV
>gnl|CDD|177433 PHA02608, 67, prohead core protein; Provisional
MEDLIEAIKSGDLVEAKKEFASIMEARTEALIEEEKVEIARSVMIEGEEPEDDDDDEDDDDDDDKDDKDD
DDDDDDEDDE
>gnl|CDD|165004 PHA02609, uvsW.1, hypothetical protein; Provisional
MKSFKEFLYEAAIDSFMSKIASCQTLEGLEELEKYYKKRVKEVELKDSDDISVRDALAGRRAELESDDEE
EEEEDF
>gnl|CDD|165005 PHA02610, uvsY.-2, hypothetical protein; Provisional
DKICVVCKQPIEKALVVETEKGPVHPGPCYNYVEELPVSESSEEQLEETQLLM
>gnl|CDD|222907 PHA02611, 51, baseplate hub assembly protein; Provisional
MANIIRCKLPDGVHRFKPFTVKDYRDFLLVRNDMEGRSPEEQQEILDELLDEYFPEYPKTEQEYIFLNVY
TGSIGKTKIPVTFTCPKCKKEKTVLFNLKQEELKNPVLEVANLKLKFKFPEKYEDKAELFLETIQYVSDG
ENRYEWTELSEETQEALIDAISIEELEKIVKSMNPIKLELKISCCNRRDLKYTDLLELFKLLVNPDEIFE
FYKINHLLVKNNYSLESIMNMIPVERGIVLSLVEKDLKE
>gnl|CDD|222908 PHA02612, 27, baseplate hub subunit; Provisional
MKMLQRPGYPNVSIKLYQDYDAWLENRFVELAATFVTLTMRDSLNGRNEGLLQFYDAKNIHTKLTGREII
QVSVKNANTEIVENRIYGIKHSNVSVDSKGDNIITIQLGPIHSVENLKFSRSFFNNAVESITEMMGAIYQ
DRPLLTPPINGINVRVPPIPWVSTIEDYFDYVREVGQSVESDKFVYVWEDISGIFMMDYDEILNQEPIPM
IVGEPRLIGQYIQMVDNPFVFDFEWLTKANYHTRKPYKNATFYAHSFLDKKLTRIVTGDGENSIIVSRSG
AYYDMTYRNGFEEASRLQTMSQYDGYAKCKTYGNFDLTPGAKIEFYDSKNQFKGEFYVDEVIHEVSNNQS
LTHLYMFTNSEKLEDVEPVKVK
>gnl|CDD|222909 PHA02613, 48, baseplate subunit; Provisional
MKVKEIQDDVASLKKIKGEPSSGGQTTKNKLGQKTVTAQFPAERASGNDTAGDYNVNDLYKNGLLFTAYN
FSSRSSGSLRSLRSNQAAQNAKQILSSNTGGVSNKQLNIGNNRTTFDKEPIANILLPRSKSDVDTNSHRF
NDVGESLITKGGGTATGALSNMASTAVFGALESITGGIMADRGEQIYTTARSMYAGADNRTKVYTWTLTP
RSREDLMEIIKIYELFNYLSYGETGKSGTAAEIKGLVDAWYRSTLINPLTPEDAPKNKTLFEGITSFLSN
VIVVSNPTIWMIRNFGTTSSFDGRSDIFGPAQIQSIRFDKTPDGHFNGLAIAPNLPSSFVLEITFREIIT
LNRGSLYDETF
>gnl|CDD|222910 PHA02614, PHA02614, Major capsid protein VP1; Provisional
MAPKRKGSCPPCRPQPVPKLLIKGGVEVLDVKTGPDSITKIEAFLNPRMGQPQTTGHYYGFSDKLTVASS
FTNDTPDKDELPCYSLARINLPMLNEDLTCDTLLMWEAVSVKTEVVGVPSLLNVHSYGKRLHDGYGAGFP
VEGSNYHFFAVGGEPLDLQGLVPNYKTKYPEGVVAPKNATNTAQVLDPTAKAKLDKDGAYPVECWCPDPS
KNENTRYFGTYTGGANTPPVLQFTNTSTTVLLDENGVGPLCKGDGLYLSCADICGFFTYSSGKQVWRGLP
RYFRVTLRKRRVKNPYPVSSLLNSLFNRMMPRVQGQPMEGEDTQVEEVRVYEGTEGLPGDPDMIRYIDKF
GQQSTKPPANAAN
>gnl|CDD|222911 PHA02616, PHA02616, VP2/VP3; Provisional
MAMALWPIPEYQLETGIPGVPDWLFNLVASYLPELPSLQDVFNRIARGIWTSYYNAGRTVVNRTASRELQ
RLLSDLEYGFRRALASIGESDPVNAIVNQVRSAVTYNRERELLQILAGQPLDESRGVSALSAAAGALTEA
AYNFIYDASNLPKDGFNALSGGVHRLGQWISFSGETGGTPHYAIPDWILYVLEELNKDIYKIPTQAVKRK
QDELHPVSPTKKAALSKKSKWTGTKSSQSSKKRRGRSTGRSTTVRRNRI
>gnl|CDD|177439 PHA02620, PHA02620, VP3; Provisional
MGAALALLGDLVATVSEAAAATGFSVAEIAAGEAAAAIEVQIASLATVEGITSTEAIAAIGLTPQTYAVI
TGAPGAIAGFAALVQTVSGVSSVAQVGYKFFSDWDHKVSTVGLYQQPGMALELFNPEDYYDILFPGVNTF
VNNIQYLDPRHWGPTLFSAISQAFWHLVRDDLPRLTSQEIERRTQRFFRDSLARFLEETTWTIVNAPINL
YNSIQDYYSALSPIRPSMVRQVAEREGTQVSFGHSYSQSIDDADSIEEVTQRLDLRNQEPNVHSGEFIEK
TIAPGGANQRTAPQWMLPLLLGLYGTVTPALEAYEDGPNKKKRRMSRGSSQKAKGPRASSKTSYKRRSRS
SRS
>gnl|CDD|177440 PHA02621, PHA02621, agnoprotein; Provisional
MVLRQLSRQASVKVGKTWTGTKKRAQRIFIFILELLLDFCRGEDSVDGKKKKDSLTDKTETVTEKPES
>gnl|CDD|222912 PHA02624, PHA02624, large T antigen; Provisional
MDKTLSREESKELMDLLGLPMAAWGNLPLMRKAYLRKCKEYHPDKGGDEEKMKRLNSLYKKLQEGVKSAR
QSFGTQDSSEIPTYGTPEWEQWWEEFNEKWDEDLFCDEELSSSDDEDEPPPPSPPPSQEEESQSSSQATP
PKKKKKNPAPNDFPSCLLAFLSHAIFSNKTLTCFLIYTTKEKAELLYKKLLEKFNPTFISRHSYDGGALL
FIITPGKHRVSAVNNFCKKHCTVSFLICKGVKKEYELYSALCRDPFKLLEESIPGGLKEYEFNPEEEEEK
QVNWKLITDFALETNCDDVLLLLGLYLEFAVPPEECKKCQKKKLKTHFKYHEKHHENAKLFLDSKNQKTI
CQQAVDGVLAKRRVKLLTMTREELLAERFKKLLDKMDEIFKGSVDILQYMAGVAWLHCLLPNFDDVIYDI
LKLIVENVPKRRYWLFKGPVNSGKTTLAAALLDLCGGKSLNVNCPPDKLNFELGCAIDQFMVVFEDVKGQ
PADNKDLPSGQGMNNLDNLRDYLDGSVPVNLEKKHLNKRSQIFPPGIVTMNEYLIPQTVKARFAKVLDFK
PKPYLKKSLKKNEYLLEKRILQSGETLLLLLIWYRPVEDFAEEIQEKVVTWKERLDKEVSDTTFATMKEN
IHEGKDPLEKIVEEDSD
>gnl|CDD|177442 PHA02627, PHA02627, hypothetical protein; Provisional
MKHRVYSEGLGISTDFNSIISQLSTSDMDIEIDEDDITELLNILTELGCDVDFDEDFSDIADDVLESLME
QDM
>gnl|CDD|165015 PHA02629, PHA02629, A-type inclusion body protein; Provisional
MLRKIADLEKKLRDGGNGNGGNGCTSSCEFERKIIAVLEAELRKSMETIKALEKFMEFDRL
>gnl|CDD|165016 PHA02633, PHA02633, hypothetical protein; Provisional
MGKREADNDRIILIDNCNNMLILNPTQSDSGIYMCITKNETYSDMMKFDLCICLRIESNIDFI
>gnl|CDD|165017 PHA02634, PHA02634, hypothetical protein; Provisional
MEQLGITLGSDLEAYFMCKLQELNCDASILLNKASKNVMDRQLSKTPTR
>gnl|CDD|165018 PHA02635, PHA02635, ankyrin-like protein; Provisional
MESESDNISIKTEYENEYEYEYEFYDETQDQSTQLVGYDIKLKTNEDDFMACIDINVFHII
>gnl|CDD|165019 PHA02636, PHA02636, hypothetical protein; Provisional
MSTFIIIDQSTENTSIDTTVTINIIHLAIMKIIMNIIIIMMIMIELV
>gnl|CDD|222913 PHA02637, PHA02637, TNF-alpha-receptor-like protein; Provisional
MKSVLYSYILFLSCIIINGRDIAPHAPSDGKCKDNEYKRHNLCCLSCPPGTYASRLCDIKTNTQCTPCGS
GTFTSHNNHLPACLSCNGRCDRVTRLTIESVNALEAIIVFSKDHPDARHVFPKQNVE
>gnl|CDD|165021 PHA02638, PHA02638, CC chemokine receptor-like protein; Provisional
MDNSSTTLSSIILSSSTLSPTTFFTIETSMDESKSIISTFTEIIPTEIPTSESPSPNSNSSSSSSSSSSS
ITYDYEYENNITYELINIKNKCMYPSISEYIKIFYIIIFILGLFGNAAIIMILFCKKIKTITDIYIFNLA
ISDLIFVIDFPFIIYNEFDQWIFGDFMCKVISASYYIGFFSNMFLITLMSIDRYFAILYPISFQKYRTFN
IGIILCIISWILSLIITSPAYFIFEASNIIFSAQDSNETISNYQCTLIEDNEKNNISFLGRILQFEINIL
GMFIPIIIFAFCYIKIILKLKQLKKSKKTKSIIIVSIIIICSLICWIPLNIVILFATMYSFKGFNSIISE
HICGFIKLGYAMMLAEAISLTHCCINPLIYTLIGENFRMHLLMIFRNIFTNAKFSFRKSSISSSIIF
>gnl|CDD|165022 PHA02639, PHA02639, EEV host range protein; Provisional
MKIILYLFIGVCYVHGVKSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCIKDKNN
AIWSNKAPFCMLKECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNEKITCIQDKSWKPD
PPICKMINCRFPALQNGYINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPSIPTCVRNKP
IDDIIYLKPVDDNFDDLDNEDKINTILHNNDANSTRINQEKENGNIFTVIILLSIISFMFILGVLSLLCS
CMLKSSSKTSVYNKL
>gnl|CDD|165023 PHA02641, PHA02641, hypothetical protein; Provisional
MSDLTKVSTFEERNISFRMKNTEAGKDSTMMDDLMNDLMNDFSLMFLYDTADKINDHDSLENVLEDYFAW
RAHISKIDILPKNVGKLYLDLMDLDTFAKKMMGDLDILILDVLKLDEQDADVRLFNFISSMDINFNNCDT
CLILIGFIGYVCSFWGKHNLISEYLHSVMRGFLTHVNLETLENVKKYF
>gnl|CDD|165024 PHA02642, PHA02642, C-type lectin-like protein; Provisional
MFPELKMALKPTTEIVEMGKDDCCDTNSDKETETQKNYGQFTSFVTPEKLYCCIITICILITINLVPIII
LMAFKSDTQEPTIKYVTCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKD
SSDHWIGLNRESSNHPWKWADNSNYNASFVITGTGECAYLNDIRISSSRVYANRKWICSKTYTNIYIPSN
NSYNYP
>gnl|CDD|165025 PHA02643, PHA02643, hypothetical protein; Provisional
MEEYDNIAIKITSENGSTISVCCESKSKITIDIVTKKNQSVSTKSIIKKKKLENTKKDDEYNYNTDTEES
ENAMEIDCIKNS
>gnl|CDD|165026 PHA02644, PHA02644, hypothetical protein; Provisional
MLESYNTYAKVNINVSTKDQVIKIMIGSSPYMDVRIVSNKYDKIFISNEDEMKTTHEHIKKENEDEKKPE
KPENEDEKKPEKPENEDEKKPEKPENEDEKEFEDSDASDKKK
>gnl|CDD|165027 PHA02646, PHA02646, virion protein; Provisional
MMNLEEIKKITNIIHQFNIVCNVDIEKIYSSETIVLEMSLDGTINAIHIYDNIVSRFDNKTMLGIAKFIY
RNSEWILKLLFINDDIEKIINPIYPSKTITINSKPKLDEIMPSNIISLKIVLLNLFNSFKYGELCKKSLP
YYYSPFRKDIYDIILK
>gnl|CDD|165029 PHA02649, PHA02649, hypothetical protein; Provisional
MAEVLINKLRNIELDNYGNEKIIDCIIYEIENTQYVIVRPILRLIVDLMILLIVLNDVIIRVIKRNYKIL
LISSFCVSMLYFLIHKEENLNDNGS
>gnl|CDD|165030 PHA02650, PHA02650, hypothetical protein; Provisional
MDKLYAAIFGVFMSSTDDDFNNFIDVVKSVLSDEDGSKKTIKSVSWFNGQNFIFLIFSLIIVALFSFFVF
KGYTRNLNGRK
>gnl|CDD|165031 PHA02651, PHA02651, IL-1 receptor antagonist; Provisional
MKKLILLLVLYINIFNSKAAGMFMYNIWDVNQKIFYLRNNQLVAGHIQDNSLAEKITAKLIDGNDIFLGV
KNGEKSLECTEHGDKVTLSLSDKKTNSLDENQDKRFAFIRSDNGHTSTFESVAFPGWFLCTSSGDGIEPV
GLTYKGDKDDNDDDENNIYFYFEED
>gnl|CDD|165032 PHA02652, PHA02652, hypothetical protein; Provisional
MISDIYTEGLKISNELDKLLCGDDILNMEYDAVMNIISEIKVLIDLLENMYLLDDLLFDEAELQQLSTDK
>gnl|CDD|177443 PHA02653, PHA02653, RNA helicase NPH-II; Provisional
ENNLPDIFYFPNCVNIFPYKYSQKEFEEMSKTEKKNFSLAVFPVIKHRWKNAYVVKNNGVYKLSLEAKNR
LNEVSNPSLIDPVSINIAAKEYIIGNLKISFECYSYLKCIPGTEINDFDEYILRGLVEGGNALGIFSNNV
GSKKDTIGILGNPEPFSKIPLASLQPDVQLKIFEAWISRKPVVLTGGTGVGKTSQVPKLLLWFNYLFGGF
DNLDKIDPNFIERPIVLSLPRVALVRLHSITLLKSLGFDEIDGSPISLKYGSIPDELINTNPKPYGLVFS
THKLTLNKLFDYGTVIIDEVHEHDQIGDIIIAVARKHIDKIRSLFLMTATLEDDRDRIKEFFPNPAFVHI
PGGTLFPISEVYVKNKYNPKNKRAYIEEEKKNIVTALKKYTPPKGSSGIVFVASVSQCEEYKKYLEKRLP
IYDFYIIHGKVPNIDEILEKVYSSKNPSIIISTPYLESSVTIRNATHVYDTGRVYVPEPFGGKEMFISKS
MRTQRKGRVGRVSPGTYVYFYDLDLLKPIKRIDSEFLHNYILYAKYFNLTLPEDLFVIPSNLDRLRKTEE
YIDSFNISIEKWYEILSNYYVNMLEYAKIYVKGGILAEALDNFERTNILTSEVLEAIKSLNMRAKILNFR
KKKDTYIYTCKVLFGVYAGKNFNVYYRRPLTGYILMITDRIFIPD
>gnl|CDD|165034 PHA02655, PHA02655, hypothetical protein; Provisional
MVKTTKKTAVYYIYNDTIEKRINDWSHYFIITFLVSLFISICFIIKLDIKEIIKNQYTMLKFVVFTIYLI
PFVIVMISCIFLVIIYIKYHKQNI
>gnl|CDD|165035 PHA02656, PHA02656, viral TNFR II-like protein; Provisional
MIKYKLLTSFIFFITCYHVSKGSNYEEIQNKFTMFVDLTVYDKNLINRDVSCIRYDHDDFYSMYIIDKFN
VSITLSDCDDAGFTEAYYTNVRDNTMELGYFTPADKKYKGLNEDKKCIVKIIITCDGDDNNLVMTPKNFK
PKHPKHADHIEKLILYGKCIDGIKADITYDYGFTRDTSSIIYGTIHDISGLFPNSCVPK
>gnl|CDD|165036 PHA02657, PHA02657, hypothetical protein; Provisional
MANATEAPLTTLPADNYYYMKINFESILVFTIFIFVVCILIYLLIYLVDWSLVKDACNRFKTQVLKILSL
SKTHFTRLDGVYYTDEREVLGIDVE
>gnl|CDD|165037 PHA02658, PHA02658, hypothetical protein; Provisional
MNKLIMTIKNKLNTLSDKEIIQGNKFKYGELKPSEMYKKHHKYVCKNDTTGGESRPLISAVVKKVTNKKK
KKPYRVTYYINEDMDDNDDVFI
>gnl|CDD|165038 PHA02659, PHA02659, endothelin precursor; Provisional
MDSKIILPIILLTSSIMLCCCENDESYIISIDDNIDKPDENIPHIRTKRCACDSHDDKECLNFCELDAIW
>gnl|CDD|165039 PHA02660, PHA02660, serpin-like protein; Provisional
MKKYCILNNNIIKMSLDLGFCILKSLHRFNIVFSPESLKAFLHVLYLGSERETKNELSKYIGHAYSPIRK
NHIHNITKVYVDSHLPIHSAFVASMNDMGIDVILADLANHAEPIRRSINEWVYEKTNIINFLHYMPDTSI
LIINAVQFNGLWKYPFLRKKTTMDIFNIDKVSFKYVNMMTTKGIFNAGRYHQSNIIEIPYDNCSRSHMWI
VFPDAISNDQLNQLENMMHGDTLKAFKHASRKKYLEISIPKFRIEHSFNAEHLLPSAGIKTLFTNPNLSR
MITQGDKEDDLYPLPPSLYQKIILEIDEEGTNTKNIAKKMRRNPQDEDTQQHLFRIESIYVNRPFIFIIE
YENEILFIGRISIP
>gnl|CDD|177444 PHA02661, PHA02661, vascular endothelial growth factor like protein; Provisional
MKLITTLQFAVALLLCMYNVPWCFSGSTGSSSASSLSSWLDTSDKSSCQPRDTVVQLSDEYPGNTNDRYN
PRCVTVRRCGGCCNDESQICTPTETSNVTVTVMLTSVSGSTGATSNFQTISVEEHTKCKCEFKTTPPPTT
TTREPR
>gnl|CDD|177445 PHA02662, PHA02662, ORF131 putative membrane protein; Provisional
MPPRTPPTPPRPPEPTPAAPGSLYDVFLARFLRRLAARAAPASAACAVRVGAVRGRLRNCELVVLNRCHT
DAADALALASAALAETLAELPRADRLAVAKELGVDPEHPQLTPDPACAGESALAQNIDVQTLDLGDCGDP
RGRRLRVALVNSGHAAANCALARVATALTRRVPASRHGLAEGGTPPWTLLLAVAAVTVLGVVAVSLLRRA
LRIRFRYSKPLNTLRV
>gnl|CDD|177446 PHA02663, PHA02663, hypothetical protein; Provisional
MANRNDIDASAVVAAYLAGEYAAAVEEQLTPREREALEALRISGDEVRSPLLQELSNAGDYRANPENSHI
PAALVSALLEAPTSPGRMVTAVELCAQMGRLWTRGRQLIDFMRLVHVLFDRMPPTANEDLAAWLQTVARV
HRTRRRLHRSIGVGTVMAGVGLLFLGVRVLRR
>gnl|CDD|177447 PHA02664, PHA02664, hypothetical protein; Provisional
MDPAGQRLRNPGPWRLNPPTAAALEGAVLRPAAAAGADRCANARVDSRNMGVGEGREVPADVEGLMTEIH
LRYGMTRVHRNVHFVQFWHGEHVRRRPARHVFTVWVCLSGEVRIYAECCQAGHGFVLCRQMAAGYMFVTE
PTDSVTVSVPHRLRNSRSPVWLAAVFATRHFEPLPPPMYAVPGHVVLARSASMLCDCSPSDPQRRNVIFY
MRLSGTMVRVTVPGAELEIECTSGFRPDHFSIDDECVCCELRPHVARTAVWTLAEICRGATVVLAPPLPR
DRAAGLLAEIRLASGRWVRVRALRSGRGNVGPFPSVVWAAVFSAARLFLGGTVPAFAACVENGRAAYGMV
YVPPEEPRMDGLCVFPTPAEPAALFVDGNEVIAAGAAAAMIAAAERAANGARGSPMAAPEEGRAAAAAAA
ANAPADQDVEAEAHDEFDQDPGAPAHADRADSDEDDMDEQESGDERADGEDDSDSSYSYSTTSSEDESDS
ADDSWGDESDSGIEHDDGGVGQAIEEEEEEERAVLGAVAEMLGD
>gnl|CDD|177448 PHA02665, PHA02665, hypothetical protein; Provisional
MANRLVFLDPETLAEADGIPEQGVFEPGKKKCVFTKIRTSSSLACRYAVSDGGLIDELVMATYGTRRACR
LVRHLTISSEGVMTRPASNCAPHMVLICLRGVAAVSSEAMKFGRCIMERGTMFMVKSSHSAVVCGNPACE
LLVLFYDFFTPIPRVLSGDEVLFTRDLAHVDYDPNSAVVFKMEYDLATDVATLFVGGYIFRVTGLEMETR
EQVGDECDCCRHSSPVLVMDREKLMSSARMIPSLVPGQRDLCLRERGWLVASTDARGHCEPGLLRLALAG
LRLFAGCLRSAVGRYELMLFCYGIIPKFGGEFDDAPAPMEID
>gnl|CDD|222914 PHA02666, PHA02666, hypothetical protein; Provisional
MAGLFTTVRCVCNEIWKTMRGDGHHESCFHHRRRANSMESRRKSRPSRQHRSAERTPTTASSLTHENNTA
PSRHGKQHSCKASSRSSHNRGSTSSSHNHHAHRGPHQSAHRRSKHDAVRDTYQPCPQSPETDLYKGRLPG
ETERHYETPDHIYDVPEDVRCAAVEPRRDLALPPLHIPSSKPARRMRPGSMGDFPMKHTSAGKPNLQSDI
CTLCHDIETQLSALEKSLESELNFYRRYIQDTKSLLATRAANIGSKALIYTNDYNDSGNDGEEEHCSEEC
CKVEEVL
>gnl|CDD|177450 PHA02668, PHA02668, GM-CSF/IL-2 inhibition factor; Provisional
MACLRVFLAVSALCGSVHSYRWIGERDFCRAHAQDVFTRLQVWMRIDRNVTTADNASACALAIETPPSNF
DADVYVAAAGINVSVSAINCGFFDMRQVEVTYDTARRQMYVYLDTWDPWVLDYPQPLFSQEYENETLPYL
LEVLELNRVYIRVGCTVPGEQPFEVIDGIDYPHYSMEFLQHVIRPNRRFNPAKLHVDLEVDYRCVSAVNV
KAFLQDACSARKARTPLYFAGHGSNHPDKRPKNPVPRPQRVFSTSSRKCEMQTGR
>gnl|CDD|177451 PHA02669, PHA02669, hypothetical protein; Provisional
MMALVLIGIIVAVIYLTGAAIYLLIEIGLAAERANKRSRVKANMRKLATQLGNGTLDSTIGPCTISRDMG
FGCSRWDSDTEDGDTVSTTSTSGGGTLSRVWVGGGPRFQHPMYENFCGNGTHRHSPSNDPGYHSRETLCS
GPPRQANIPPVTPYPDEVSVGVGSGPSTEHGHYEGDGPEQDLEPEPVQIEVTVQGPGGEGEEEGEFFYDE
>gnl|CDD|222915 PHA02670, PHA02670, ORF112 putative chemokine-binding protein; Provisional
KSTVLLLALSGAFSAALPLVGNAPMDSDEKRNFCRTHKDELYARFRLYMRIGVRHSPVYPPSNMCMLDIE
NSNMDLDETDEVTNVSTATFEANGVNGSIALIGEEVSIPMSYIGVGFNPSLADYVYVNVSSWTPWEQSTT
DLAANDFWGLKQILNKEILAIQLGCDHQKFPEEPTPKPEPTPSTTPGPTLLETTLDLTDEPTTTPPVDTS
VDRKRNPDPVDFSLLVDTRCIKSVDLYVELKDACIAYKSQSPLKLKGQHGTGEQVRKEIKSLGTSHRTCS
LNTSPTA
>gnl|CDD|177453 PHA02671, PHA02671, hypothetical protein; Provisional
MSCLQILTSFGQIYAPDEARLREIARDLGICTISRAFGDMLYGEISFTSLPLTQVNMLMSDCYFAVNGNL
LPCTEDFRLRLPATEISAAYLTGTGKTILCGKDFNIVNPSGFKPSMRLRELSHVSALVEILEFYSESGEY
EFILGPSARFMLRLMEKENVCLFGSGWCIVDLRRLSVTI
>gnl|CDD|177454 PHA02672, PHA02672, ORF110 EEV glycoprotein; Provisional
MGCCRTPNRQSLRTLKKASCPVATLVTVLSLFTSLGAIIKYTDFFLKEACENGWVPIKDLCVLNTHVITN
VTLAHDICASMDGDPPATPNTMLLKGIMFLTGERSFWMTHHDAYTSVYEPKRGSYLPSYNEEYDKDKHVC
LLSLDGLMHHNCNQNTTVVCVKKMYG
>gnl|CDD|177455 PHA02673, PHA02673, ORF109 EEV glycoprotein; Provisional
MAHNTFDNDSEAANNANYVASVKRQKAIRRYIKLFFRLMAAIAIIVLAILVVILALALDDCRNTTCVIDT
NSYNRTCDGINAGNKCLTLKYPDTWTNANERCKELGQRLPSPSINKKYPWLTDYLVGTWGNIKERVFGTS
GGTESVTMDGSTNKYFCVDDN
>gnl|CDD|177456 PHA02674, PHA02674, ORF107 virion morphogenesis; Provisional
MEEDLNEAALLHMLTRIAQICGGDAAAAAAAIKMLMDLVNERIMILNKKAKKEMRQASPS
>gnl|CDD|177457 PHA02675, PHA02675, ORF104 fusion protein; Provisional
MEENDGENLLGPTTDEPNNDDNGVYAAGAPSKESVEERLVSLLDSYKTITDCCRETGARLDRLERHLETL
REALLKLNTKIDVQTGYSRY
>gnl|CDD|177458 PHA02676, PHA02676, A-type inclusion protein; Provisional
MESMESLVAEFKSLVQRHWHHPLNSVSCIPREDRKLIRDILREYIRLAPPIDGEKVAKRPVNLYFRKYVE
QNPMYRKIFVDDEWMSKHATTLGEHPKINIINVSTLGKLYLMVVYKIMTGHTTHNETIMDSRDVNEESDR
KVIDRQTDFFCYDFLNYMGTLASQYKNKAIYIGVPMYWWYGVDVKSVYLKLETHWNNYDTDEYTRGSLAF
IQFMSEVNGTDVSDKDHVKISFEKHKFQFVMSVPEFIMDGLCFTAWDTFSKYGTSFTMDIFINPSEHDGA
VYKSVDHDKQGVLEQLTKPDTIDCSAVRISYYPSFVHQSNDENDITPPGGYDLYYYEYGDPNNISRNYYE
RRDRLTYDGRCCEHHRVWTHIDNDGTTYLRMLWDRYDGNIKVTPFGDDEVGFDGSACVLPERVDKLLSPL
EKTLAEAKTCCESNRGAGKHLEHHIETMRQYAVLVSNKTDVHTCNRPGAEVTRHAIDGSLPPPHVLGNWG
ARSYCGRRRHYPRVSHGEKPWWWGRHAAIW
>gnl|CDD|222916 PHA02677, PHA02677, hypothetical protein; Provisional
MISLFLIICYFVLIFNILVPGIFEKLRQEHAAFDRLANAGDVYRCVDGRVVSYALGPTGIRARVMTDARG
APLPCSRAVEADPARFIRCGPDAELRDVCARAYAEVFL
>gnl|CDD|177460 PHA02678, PHA02678, hypothetical protein; Provisional
MFLDSDTVIVAVPGTRFPEGLFDRQGRPLGPGSTPTMEYEDSVPRDARALLLVNPTAGQLAAVAAGAPAG
VRVLVLVDVARCDMPFSVV
>gnl|CDD|177461 PHA02679, PHA02679, ORF091 IMV membrane protein; Provisional
MVSDYDPAVLVLIFCAALAANFYMPPQTKLSTIFVLQSVVFSWFLFHFVHSVI
>gnl|CDD|177462 PHA02680, PHA02680, ORF090 IMV phosphorylated membrane protein; Provisional
MDIFETLKSYYSGVLICGVLLLTAACVFAFVDFSKNTSNVTDYVWRALSVTCFIVGAVLLLGLFVFSMYR
KCSGSMPYERLNNTDIELTAR
>gnl|CDD|222917 PHA02681, PHA02681, ORF089 virion membrane protein; Provisional
MGLLDALLTVIVISIVCYIVIMMYRRSCVSAPAVPRNKDLLPPGASSFEDKMTDDQVRAFHALVTSSPED
DPAPAPAAVSPVARNRFSAASS
>gnl|CDD|177464 PHA02682, PHA02682, ORF080 virion core protein; Provisional
MDLRRRFAEDLAKTKLVLADTSSSLFTKCPQATIPAPAAPCPPDADVDPLDKYSVKEAGRYYQSRLKANS
ACMQRPSGQSPLAPSPACAAPAPACPACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPAC
PPSTRQCPPAPPLPTPKPAPAAKPIFLHNQLPPPDYPAASCPTIETAPAASPVLEPRIPDKIIDADNDDK
DLIKKELADIADSVRDLNAESLSLTRDIENAKSTTQAAIDDLRRLLTGGGVARRDTPSALRDRVDNTGTS
>gnl|CDD|177465 PHA02683, PHA02683, ORF078 thioredoxin-like protein; Provisional
MSWYAKYNVVLDPPRRCSKCASNLTEFINEDRENIRMVLESQPNKLRILKEFLATCRNKTFIYKILDDEI
RRVLT
>gnl|CDD|177466 PHA02684, PHA02684, ORF066 virion protein; Provisional
AAGSIYYCGGTHLVAAAPGAALVLLDALGAVAAAAPAGPRVFFAEYGLEKRAGAPITARLRKSGFRGAAG
AWASAADFEAGGRPSAWTLRAEEAARVPLPADAALVLAWGARAEPLRACVLARAADAEAPVGAALKEAAF
DARAPAAALFAALGAPALALPLKARLVAPPGAPPRSRLCANPAMLRAFAAGWFGAQLGADASENEKVFAA
FDKARSCLDDR
>gnl|CDD|177467 PHA02685, PHA02685, ORF065 virion protein; Provisional
SRVAMGGDLHALKSLVALAPSLDRVGAALAWRHVLVERDHRGAPARVHRFDRALRLDNRTALRAVKAVFG
HRKRMMRALFPSRAIFEALEPLPPAETLVLRAAREPPPDDGSPIDARETAAWLAELFNAFRAGGGAGAAP
WFCLPLAEDVQHVAL
>gnl|CDD|177468 PHA02686, PHA02686, hypothetical protein; Provisional
MDEALRVAARVVDGLSPLDVAVCLCQLRGEAPERRFPALDEASGEAFLDFEFAGGDVASRYLSMCTRELC
AAERREHMAAIARCVTEADLALAARPRGKARAALRVCRNREKVHRLARLLRDAESRGADFAFIRAAVL
>gnl|CDD|222918 PHA02687, PHA02687, ORF061 late transcription factor VLTF-4; Provisional
MSSWRLKMSKCSGSSGVQTLEDLRNRLRTEAMLGDDCTEPRDDLFPNGEECLDIDGPRPCEPSEQECQQE
QLPVPESVPPAPVKTPKRRTKKKAKADKPEKSPKAVEKLCPPDDRDDKNEEKEPTEEAQRNEESGDAEGG
ASGRSPSDDDNLDEMDDSDLMLAFSAILADFKDLTGRVKALSSVLTDVQASGVRRSFSGLGKALTEAAAI
AATGAKPPVAPRKKKAAAGKK
>gnl|CDD|222919 PHA02688, PHA02688, ORF059 IMV protein VP55; Provisional
PMANKIPIYVIPVVGRPPSEVIPELKSDINPAPIEFDDVKDAEVPPSAKNLSPPKDDPDGDHSYKYIQWT
KVESENYKHYFSGLCNLLCTEETKRSIARHLSLWESYANADIKDKEDEYIVVVEDDNTLRDITTLHPIIK
AMKEKNIDILQLRETLHNNNVRTLLNQEGNPALYSYTGGYDVSLSAYIIRVSTAKKLYDEIIKNGGVSTS
LSFEIYRIENELGINRQVLNNASKYVEHDYRLVSEKRVKEMKNSLWSRLGTWLAKRYPGFYYFLTTPLFS
FFGLFDINVIGVIIILFIIVLLIFDVNSKLLWFLAGTLFTYII
>gnl|CDD|177471 PHA02689, PHA02689, ORF051 putative membrane protein; Provisional
ATAKATPVVHLTPVFVEPTIAHSLLRAESYLAIAVLELLLALALALVFFRDELGALFRRAPRAPSPLDAY
LQASLVCDGDALMIELPEGRLPALALDGRPVAFPGCDGLLRRINGPRKVRLVDVLGGR
>gnl|CDD|222920 PHA02690, PHA02690, hypothetical protein; Provisional
MVRRVLLERVDGIVERARADRRYLEAIQRHLEGSTPLLRQMWRLLFDLLLTVFVVMYIVFRLIWRNPGAC
AMLALAAAVYYLFLCLFYWD
>gnl|CDD|177473 PHA02691, PHA02691, hypothetical protein; Provisional
MSWALEVALFAAFLAAAYVLTFLPTNKMQLAVRELADARAWRQRTDAQLDGVSESVLFPRPDAPQGSAVI
ASMDSRRARVTVAHGREKSTFDLKRRGDVQTLLPILLLSK
>gnl|CDD|177474 PHA02692, PHA02692, hypothetical protein; Provisional
MDKLYAGVFGSFLSNSDEDFEEFLNIVRTVMTEKPACDRSKGVPWTTVFLIGLIAAAIGVLLCFHYLKLV
>gnl|CDD|177475 PHA02693, PHA02693, hypothetical protein; Provisional
MLLYPKKARDAAAALAKKNFCAEKLSRAQLLSLLPCGLHGDLPMSVYDEAVAASPTNVMFFPPQHVKLPD
LITALKSTRTICKKMMPAVCFHKRALLAADDMEVLRVLLSAGLVYEPEVVDMVEKGRVPAVLALTCAPWT
ACPQLKLSRTEIETVCRAIDPALVNEMIPKLEISPEDLVALADKGNIPPLNRALREVDDVATCARLVCEW
PYFNIMKFLSPNMVASREFAQAVREGAMALCVRPVGADRMVGISKSRSRRLPEEHVDFHYDESDTADSCS
RSFSTQSTRSTRSTRSTRSGAETDTTDPDLDPDDDESFDEVGPLTRRFTATSFAPRASVRSSSASMRLHA
RGSTRISEPLMSSAARVPKVSMAPTLDTAEELMWHLSEEWRKGRHAKTATLEKLLQDFRLNATFPRTMLA
SEAPNELKRKMLKVVCGWQVVGEPTSAATAAIEGSTDQIMALLLTEHRHVGGLITLLSKPPLPPSCGCEF
CARHTAPGRSALRSASFGTGATPSPELDDAAILAAVADVTLLAMHGVVDPCFAGSVCWGPLSCALSGARH
MDAQRLVEALDYEKLIFANISADGVKDTNNLLRLSRLKISDFVPDAHVLNTRHAQALIAVGCVAEYLLAA
IFFRVTVLRRMSKIREFVAKVVSVAMEATGTTAPSIKVHDRVETEVRECSESGEVPFCTVGLVLRTVLAI
LEELLGDGGD
>gnl|CDD|177476 PHA02694, PHA02694, hypothetical protein; Provisional
MAGYLSDASASANHAHGGNPQYPQYYSHNHGHEGDRHDESENHIHITDDEHLVLSDDCLGNGASYCGHDH
GHAGHGHEGGGDRERQRAPRLYEDPVPANIIVPTLSLEQLLEESSVAEGLIGGNAEKDVEQLLEEFSALC
PGDQITALRCMAASFYRDALFAPYACMHLIASRMRVHYAREVVHVAEDLADAMSADSGVCFLRYRKRVLE
DMLAEEMGVYRYLAGANADICEDNLLSAVETLLRRFRRMGCYRSLCMLKILALQHEDLAGFIRNGIRKTC
NFAHARTHTTFV
>gnl|CDD|177477 PHA02695, PHA02695, hypothetical protein; Provisional
MLQLLKSFVGAAVAAGGVERAFAALSTSEAMSLMLDGVHPKHLPRRLYAPVSAEHPTHLHLFRPQHVTPE
DLLEELSRRRCGALFARHIEFHTPYLVQFADYALLCRCIPYMNITEDDVRLIEERFPDDVDDILLHVNAR
SVHNINAAFTDEMMEDIVEARPEMASALYTTRPLDLGFLKRMLADHRIPPVNAGLAAATPADAVEMLAQM
RGVYDVRRTLDGLRHSVLCSETVKAFALERIRAGQVQEYLHYAEDYLRDRVSDTGAFGPIFVDAATYLNV
DNLSHAELSAIADFPGKFDATFVWRKALEGGFGDVLGKLLRLADVDAVTEDVCVGIVESGHRVAVTDMCV
HTTRVAEACVRQNFPDVVDFLDTVPLRTLLAVGADPFASDYVFSTSWINDRPELAEEYVRRFAFSGERMS
RLLFGYALKPAALKRVHDALCAEEVLAPAVRESLGCLVSEGEMRLRSVHDVRRPRECEDPEEGYEQEIFS
SEHSARLAVCLTAYAVPGLRGYATADLAITRHASGNVILQALRVHRADSAVNKVVDHIFDIARMASYGLF
LIPDMFTPGWTPVLDLARGLPASPPPVLKMERLSFSPSELVQYRGIGRFALGCETAVGPCSDHQMAMDAL
FRCLFVHIAMGVRLVEQVDVVVLVRQIVNAFTDGLCAERFVEPVEFVEQELVELRAWGPNERTIESSKVC
MRNTTLLCQQVCARLALYNNRVFRK
>gnl|CDD|222921 PHA02696, PHA02696, hypothetical protein; Provisional
MGVVLCGCLFVWAGWLARRVRRLCIWLRRRVGREPGYVSVIQTCDDDYFTEEEFDDGKQVVALLRAVSRV
VAAPAGVTE
>gnl|CDD|222922 PHA02697, PHA02697, hypothetical protein; Provisional
MEVEVDENDERARRMAMILTTSFMESMGDIVRQEELARQFCYKNGMTPAVSVRVTGRVSADAIGEDTWDL
ARSHDVRHVVLFKASVVDWRVEELFLGFGEKLGGLDALYFVADGFYVDASPSRFKPVDGMETMLRCVLRD
VMDDVGGGAVHPREPSAASQCLMDRYMVPFGGLLAMYAHFTRREGRHPQVPAARLEASRGASVRRAILHG
YADTEMYNQALAEARRAGVRRRRRRARDDVLSLCRNLDCMTVDDD
>gnl|CDD|177480 PHA02698, PHA02698, hypothetical protein; Provisional
MLIYGPRLNVDELIDRMLDDVQVNGDLMPTPEPTPEEVPQCSPEDMSDMLDNFLEDIQYKSELQLLSQEE
MDELLVELEDLARLLSDFP
>gnl|CDD|165075 PHA02699, PHA02699, hypothetical protein; Provisional
MLWCGLARMSAFARLFGRFGRGRNQCVPRAGCMPLRRPRDGADDEDSEYDDDVEYGDDDDSADAAAPVEA
RPLVLTVPGANCPVLVDSVFERIIEDTSALVTHLGDWSEIRLFESPFHRAPARICRSEFARYIRDAEAHF
EVGDCQALKLKHDEWYMRHHMAPDMAAFVAIICIKNEGMAAIAVNNTKFLKTNIQEGDAIVFPAARGMFF
LPHIGGDAEYIILTLTPTADLLDLGFDVFPPSIDQDAQILTANAAETRKKACKIVNDIIKLRIDLEECYH
EICKLMIMISEFGDLYNDVGAKMITASVDAIAKGMGGVDVGGENCEVDGVAAATALCRQASSLRGRRPLS
AALNRNHSILEHGINGLFAMFAQCAEGTPHPDSLMARMEKDLQDLYARFSELWDDILEKAADLDSTLPRC
ECIEKFIHHMVCNSEAGIERNELVQRLTMIAGAGYRLTGSGEGVPV
>gnl|CDD|177481 PHA02700, PHA02700, ORF017 DNA-binding phosphoprotein; Provisional
MEAGGVHKRPFIVNVEGQGRVLVLRYVRMCEVPEAKCEGSRASCVLKVDPPRSPVCERRPQLPPSPPCPV
RTPPGSPLAAPLMPTQMLQGLFTTAKTNGEQMCRRQ
>gnl|CDD|177482 PHA02701, PHA02701, ORF020 dsRNA-binding PKR inhibitor; Provisional
MSCDCASLILTLLSSSGDKLPAKRIAKELGISKHEANRCLYRLLESDAVSCEDGCPPLWSVECEPDEKKE
EGSGSDTEPMETEAGCDTLFGGDIDVLTVSAVMRLKTLNPVSAVNEFCMRTHRPLEFCETRSGGHDHCPL
FTCTIVVSGKVVATASGCSKKLARHAACADALTILINNCGISF
>gnl|CDD|177483 PHA02702, PHA02702, ORF033 IMV membrane protein; Provisional
MESRDLGVAVGATILMLLIVVTGGATIARRGAPSLGIRSRGALRVLTVLDFVSLLTTIPCTIILYFLCMQ
ALNSRTEN
>gnl|CDD|165079 PHA02703, PHA02703, ORF007 dUTPase; Provisional
HEFLAMEFACTDALRVVRLSPNATIPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRI
APRSGLAVKHFIDVGAGVIDADYRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTD
RGAGGFGSTGSGACEGCGDTVWYIN
>gnl|CDD|165080 PHA02705, PHA02705, hypothetical protein; Provisional
TDTDVANVEDIMNEIDREKEEILKNVEMENNKNINKNHPSKYIREALVINTSSNSDSIDKEVIECISQDV
GI
>gnl|CDD|165081 PHA02706, PHA02706, hypothetical protein; Provisional
MQFENTLLVIAIIMMLLGIASIIIDTVIFINAYFVKKRKCINKKDEIEPLLDKTKYEK
>gnl|CDD|165082 PHA02707, PHA02707, hypothetical protein; Provisional
MLNFSLCLCPVFILDKLVFRTQSIILHTINNASIKKR
>gnl|CDD|177484 PHA02708, PHA02708, hypothetical protein; Provisional
MPSLRRLLAALALVALGFALGALFRPAAPALPAAFIEVGPARANGSASVTCLTVGDARHMAAVADAEGRL
LSPVYPAGEGMHASFSSARRGALLLHVVTVTVYDVRGLRDDFELTCVAVVGGFNAATAYARPVAEWRRQL
ERLRRAEL
>gnl|CDD|165084 PHA02709, PHA02709, hypothetical protein; Provisional
MFYLFIIKHIVKLFTDKYFIFSKIVVGKFLIYMFIPSINNEFID
>gnl|CDD|165085 PHA02711, PHA02711, Toll/IL-receptor-like protein; Provisional
MDIKIDISISGDKFTVTTRRENEERKKYLPLQKEKTTDVIKPDYLEYDDLLDRDDMFTILEEYFMYRGLL
GLRIKYGRLFNEIKKFDNDAEEQFGTIEELKQKLRLNSEEGADNFIDYIKVQKQDIVKLTVYDCISMIGL
CACVVDVWRKEKLFSRWKYCLRAIKLFIDDHMLDKIKSILQNRLVYVEMS
>gnl|CDD|165086 PHA02713, PHA02713, hypothetical protein; Provisional
MDIDDIKHNRRVVSNISNLLDDDILCDVIITIGDGEEIKAHKTILAAGSKYFRTLFTTPMIIRDLVTRVN
LQMFDKDAVKNIVQYLYNRHISSMNVIDVLKCADYLLIDDLVTDCESYIKDYTNHDTCIYMYHRLYEMSH
IPIVKYIKRMLMSNIPTLITTDAFKKTVFEILFDIISTNDNVYLYREGYKVTILLKWLEYNYITEEQLLC
ILSCIDIQNLDKKSRLLLYSNKTINMYPSCIQFLLDNKQNRNIIPRQLCLVCHDTKYNVCNPCILVYNIN
TMEYSVISTIPNHIINYASAIVDNEIIIAGGYNFNNPSLNKVYKINIENKIHVELPPMIKNRCRFSLAVI
DDTIYAIGGQNGTNVERTIECYTMGDDKWKMLPDMPIALSSYGMCVLDQYIYIIGGRTEHIDYTSVHHMN
SIDMEEDTHSSNKVIRYDTVNNIWETLPNFWTGTIRPGVVSHKDDIYVVCDIKDEKNVKTCIFRYNTNTY
NGWELITTTESRLSALHTILHDNTIMMLHCYESYMLQDTFNVYTYEWNHICHQHSNSYIMHNILPIY
>gnl|CDD|165087 PHA02714, PHA02714, CD-30-like protein; Provisional
MKMNYIFLSAIVTCLVYTSFGKTCPKDYYLEPEDGLCTACVTCLSNMVEKQSCGPDKPRKCQCGPGLKCT
VPAVNSCARCTPDTTTKKIEPEQCCTTPDNTKLCYHKYSS
>gnl|CDD|165088 PHA02715, PHA02715, hypothetical protein; Provisional
MINININTILIFASLFVASFANDYPPPGFFEDKYITDTFNYISIDFELYPVNVSSCNRLSTKQSSDIIST
SELTITVNSTDCDPVFVTEYYSIKDKTAIAGLFTDTTKKQNTSKMCTLNIEVKCNAETEPVLIGNFTRVP
EKASTHAENFTLIGNCLSDLHLYIAYVNTDEEFEEDTATIHIGNKIDINGIPPNMCATRTIN
>gnl|CDD|165089 PHA02716, PHA02716, CPXV016; CPX019; EVM010; Provisional
MASLTEHAIVNVRKLIYSIHFEDFDNRPSTNARINNEDPDDGYCSDGDIYSYNHTVVFKNIKVFKKKYYG
IDNRDRQQYTDSKTALIEIITRMILILKLDRKNKSLVDQYKQFYKQIIKDNKSKTANHVFDIPNNGDMDI
LYTYFNSPNTRGIDLDLIKYMVDVGIVNLNYVCKKTGYGILHAYLGNMYVDIDILEWLCNNGVNVNLQNN
HLITPLHTYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINIDNINPEITNIYIESLDGNKVKN
IPMILHSYITLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNISTDIIKLLHEYGNDLNEPDN
IGNTVLHTYLSMLSVVNILDPETDNDIRLDVIQCLISLGADITAVNCLGYTPLTSYICTAQNYMYYDIID
CLISDKVLNMVKHRILQDLLIRVDDTPCIIHHIIAKYNIPTDLYTDEYEPYDSTKIHDVYHCAIIERYNN
AVCETSGMTPLHVSIISHTNANIVMDSFVYLLSIQYNINIPTKNGVTPLMLTMRNNRLSGHQWYIVKNIL
DKRPNVDIVIIFLDKCYANGKFPSLLLSEDDIIKPTLRLALMLAGLDYCNKCIEYMERDIAILDNSHAMF
LALDKLVSIRDNIDKLTKLHINSRSNISIYDILVSKCYKEDIITHRENHNLVACCHGNDPLYDIINGYIT
DARSMYYIANDISRYIMDMYPVMCIPVSLLFSCIIGIFRLSYFKKIIIDRHHTSFINARLTDEA
>gnl|CDD|165090 PHA02718, PHA02718, hypothetical protein; Provisional
MIMSTDPNNILMRHLKNLTDDEFKCIIHRSSDFLYLSDRDYTSITKETLVSEIVEEYPDDCNKIIAIIF
>gnl|CDD|165092 PHA02723, PHA02723, hypothetical protein; Provisional
MDDAYYSGNLESVLGYVSDMHTELASISQLVIAKIETIDNDILNNDIVNFIMCRSNLNNIFIFFLDCIYT
IISQDIS
>gnl|CDD|165093 PHA02724, PHA02724, hydrophobic IMV membrane protein; Provisional
MISNYEPLLLLVITCCVLLFNFTISSKTKIDIIFAVQTIVFIWFIFHFVHSAI
>gnl|CDD|165094 PHA02725, PHA02725, hypothetical protein; Provisional
MHVFYAVIDNNIDLECLTLHKGIEYGCKLQLISKNTKTVNIKCIIEVYYSDHLLKPLMAYVNDKLIELDR
KKLRHKIVYSIDLTLYDEVTNMLVCSNMDPDLIDRYYANICLDFDNNVYTIKDKNYTNAVIEYPVVCNFR
RYSESDSDSDVDDRAELHKHNNDSDSDDYT
>gnl|CDD|165095 PHA02726, PHA02726, hypothetical protein; Provisional
MISYIINPILNIFYFMIRKISGIISLLLMRTIIFLFKLVNPYPNLLSPMKMLSIDSWNIFGGKKQPKTSG
FLSYLNPFRKEEPPKKGFFSGLFG
>gnl|CDD|165096 PHA02728, PHA02728, uncharacterized protein; Provisional
MSSIRFIACLYLISVFGNCHEDPYYQPFDKLNITLDIYTYEDLVPYTVDNDLPNPNDDTTSFVKIYFKKF
WITVMTKWCAPFIDTVSVYTSHDNLNIQFYSRDEYDTQSEDKICTIDVKARCKHLTKPEVTVQQEAYRYS
LSSDLSCFDSIDLDIDLIETNSTDTTVLKSYELMLPKRAKSIHN
>gnl|CDD|165097 PHA02729, PHA02729, hypothetical protein; Provisional
MDTIFDFSEARELFSLTNDDNRNIAWDTDKLDDDTDIWTPVTEDDYKFLSRLVLMAKLNRDTVFDYYVLT
GDIEQPTIFFFKVIRFHPLFNFLK
>gnl|CDD|165098 PHA02730, PHA02730, ankyrin-like protein; Provisional
MDCGRDCTILCRLLDEDVTYKKIKLEIETCHNLSKHIDRRGNNALHCYVSNKCDTDIKIVRLLLSRGVER
LCRNNEGLTPLGVYSKRKYVKSQIVHLLISSYSNASNELTSNINDFDLYSYMSSDNIDLRLLKYLIVDKR
IRPSKNTNYYIHCLGLVDIYVTTPNPRPEVLLWLLKSECYSTGYVFRSCMYDSDRCKNSLHYYILSHRES
ESLSKDVIKCLIDNNVSIHGRDEGGSLPIQYYWSCSTIDIEIVKLLIKDVDTCSVYDDISQPYIRGVLAD
YLNKRFRVTPYNVDMEIVNLLIEGRHTLIDVMRSITSYDSREYNHYIIDNILKRFRQQDESIVQAMLINY
LHYGDMVSIPILRCMLDNGATMDKTTDNNYPLHDYFVNNNNIVDVNVVRFIVENNGHMAINHVSNNGRLC
MYGLILSRFNNCGYHCYETILIDVFDILSKYMDDIDMIDNENKTLLYYAVDVNNIQFARRLLEYGASVNT
TSRSIINTAIQKSSYRRENKTKLVDLLLSYHPTLETMIDAFNRDIRYLYPEPLLACIRYALILDNDFPSK
VKYDIAGRHKELKRYRADINRMKNAYISGVSMFDILFKRNRRHRLRYAKNPTFINFVSNIKWYKKELTSI
ITETVKNSERIDSIVDNINTDDNLISKLPMEIQREILYYSIK
>gnl|CDD|177485 PHA02731, PHA02731, putative integrase; Provisional
KKKTDDDDIFDDILKPLGAGKIAGGFDRGIDFLDAAAKLKKGLKKAYKQLQDTELMANAKRFAGSRVAYI
AIALIQLKNCCRIREAIRAFKKFIESGNLNERVVVKIAKSEKDLIDREFKDKAHKHGNIRDMIFPDDLKD
KAIFKAILKTKYWTKFCDDDKLRARILDFALGHLEANTHSLRYAGINYLAKVEGIDMAIIAKFTGHANLD
QIILYTQTKAADEIFDRKIAD
>gnl|CDD|165099 PHA02732, PHA02732, hypothetical protein; Provisional
MKSGKLIIRLLLLNLFIIPIIIPPAASGIKADSGVAAAPIGEASISSAPYTSTSFILDTANLPWINPIAS
NIRFFEYPNLTGPIQAFVSQGWSPISSGSYPSSRVIKVVPGSGVSGVYPDQLFNGSMFRVGSVVESTDWE
TLPKPYWQGGLLVFNCPAAPAGGQYIAWRFTPPSNTFNVTIHITSWPSGIGNPYSPGIAIYSPNVGDQPT
DIGASGFLALLVDFYNGGIFYHEPNGGWTELSGSLPQPNPAYPFTFTVIFTENSAGNVTVAEVGINGTAT
TINVNTPFPWSQIGYIGIRGDIDDLFYTSYFAASSGSVFAQFVPSPFIGEAVKSLSLVESTDWFTLPKPY
WQGGELVINGTGAGAGGQYIAWRFIPSSNTFNVTIHITSFPSGIDGGNNPGIEIFSPNIGNQPYAQASGF
LALDVDFNGNTIWYHGISGIFGCDLLKSSALPQPNPAYPFTFTVIFTENSAGNVTVSEIGINGTAHTINL
NTPFPWSEIGYIGIRGDCGDLFYVSYFAASPSPEFAQFVPPRELQFPNFVESGDWGLKSKPYWQGGLLVF
NSTGASGNQYIAWAFTPPGNTINVTIHITSFPSGIPGGDIPGIAIFSPNLGDQLQDDILGPSGFLMLLVA
FYNGLIVGHGLNGFSLLKTFSSAFPQPNLAYPFTFSVIFTENSAGNVTVSEIGINGTATTLNFATPFPWS
QIGYIAIRGDPMDLFYVSYFAASQDQPGTYPVVFLPAYELNANPFPIFPFPGTIYLAAFPYPISYDVFTS
PAPFTSVPSTVITPTFSKATLPLTNVSIQQLSLFTSAGPIISSSQAMVIPNIGAWSGNTPLFLFPQMAVQ
EGIPTFGLVLPVWYYVSLGTGTIGVSLVQVPMILGNKLFAFLPEVESTSWGSLPKPYWEGGLLVLDGSAA
AAPGQYIAWRFMPSSNTLNVTIHITSFPEGAQYNPGISIYSPNIGDQPSDNAISGFLAILVDFYDGNIWY
HGPNANWQELRSSALPQPNPAYPFTFSVIFTENGAGNITISEVGINGTATTINVNTPFPWSEIGYVAIRV
DTDNIFYVSYFAASQGPSPFTFVSPSYIFLNSWASSYVAPGFLGSPYALPYFMNQTSALVGNTALPKGLN
VFSGYMFGAGTVASAFLYMNSTPQSPVLALLLAPYISYKFNALSLGFSITADAAIFSLFGIPAPQLLSSY
IPTGSVLYQDPIFTYIPPGIIGMSGTNTFTFKAAQLQLSAASSPPAATTPTPPPSSSSSSSAQSISTSPG
QIQIVLNGSTTIHINFLFFPALSTPKIGQILAMPIVNSSGAFISLYVNSAISANFNVTIEYVFSNGTVIK
RFTDEPGQIFPLPLINGDEEVIISVENESTTFNISANNLGSAQLALQLRNAISASLPGPFAFFGPILALP
IFLIFAGSFFISAALRNDLKFAGMGGIIYGFFIAPFLIDIGFPAFIVFGSAIGALAIGIFALWASKS
>gnl|CDD|165101 PHA02734, PHA02734, coat protein; Provisional
MAKEEPKKGDYAGGAAKILDGFEAGQLGFPEVSLKLAGEEANARKAGDANAKAAIHAIIKMIKDAMKPLR
NKGKGFKEAWVYFSQVPENAPPNSQAIPGEIAAQVKAKLEALYQQAKAFLAAPAAAAREAAKAEALSKGA
KGLAMAAAM
>gnl|CDD|165102 PHA02735, PHA02735, putative DNA polymerase type B; Provisional
MAKCDKNLDAIDLDPAYQAPRKAKFADGKLINAFDTETSDGDIFCISSAWEDEKPAVQHNDREELDAEQI
MDALTDHKARSNINIWYNLDFDANAILNGICSEEELAELVVSGTTLANSDRTYRQYMDTDKELAGGEYEI
FYIKGKFLEIKDENGHISPHYDAAQFFYTSLDNAAEEWLGENKAKDGIDAGKFDAKEYIKDNFDDILKYA
KIDAELTQDLAIEATNEAEELDIPMGRPFSTGYLAAEYLDANLEEKPGLGNEAMAKLAWESYAGGRFEVF
KRGNVGEVAAPDINSAYPAILADLPDPKTLNWKHYLNEVSDKEPFSHSAKHAGIEEIENADYGFMKAKVS
TDPSREIQPFACKDDKQDKLKFPAMQNKEITVIKDIFEFAVNNGLVTDFELIDAWIGNITDGTSFPFDFI
GDLYAERKTAEALKGKEKKGLLLKIVLNSMYGKTCQTTEKRHEHAEDKDGKKILEAHESQVPDFSLPKKI
REALGDDEIFIEELEAGARFNPFFASYITGLTRLELHKQICEHDIEDNTVMFATDCLMIEEEAFEESNFD
ENIHVPDDSLPESEFRKEAQDGLGAWDFDYEGDAFILGAGVYEIDFDTCQKGCKDNCNKFQGKHKTKTRG
FIEADLEDGLKGAAEKAKEAIEIDNERPLTIAEIIISNEELGQVGEFLENEKKIKPDFDDKRKWNRENPD
FHDLLNDCETSKPIDI
>gnl|CDD|165103 PHA02736, PHA02736, Viral ankyrin protein; Provisional
MWPPEEIIFASEPDIEGENILHYLCRNGGVTDLLAFKNAISDENRYLVLEYNRHGKQCVHIVSNPDKADP
QEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAK
MMNILRAKGAQCKV
>gnl|CDD|165104 PHA02737, PHA02737, hypothetical protein; Provisional
FFQREDMNKRAFHVAKFAELHFDGIDDYVCVPDSWIIRRKATDQKSIVAYFEGEDPFVTKDRTKKKEKCN
DE
>gnl|CDD|222923 PHA02738, PHA02738, hypothetical protein; Provisional
MSRCKFRELKYAEFLALMEKSDCEEVITREHQKVISEKVDGTFNAEKKNRKLNRYLDAVCFDHSRVILPA
ERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVE
QGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQ
KELAQESLQIGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIP
FQYFFCYRAVKRYVNLTVNKVSKKLIPNVQTVSFNKNLVL
>gnl|CDD|222924 PHA02739, PHA02739, hypothetical protein; Provisional
MSLKLIVPNEWKVLPPATLQTELLRIISAKQSTDQTATGVKGAYNGVTAESIEFSGYLWFRKLDDTNKKP
DFKCYSLMVIPFFESPASPSEDISSCSECDSEELLSDDECCSTCDE
>gnl|CDD|165107 PHA02740, PHA02740, protein tyrosine phosphatase; Provisional
MAIEDAVDINGMDFINFINKPDLLSCIIKEYRAIVPEHEDEANKACAQAENKAKDENLALHITRLLHRRI
KLFNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFNQFWSLKEG
CVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCA
DLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFC
YHLIAAYLKEKFDILKFI
>gnl|CDD|165108 PHA02741, PHA02741, hypothetical protein; Provisional
MESPHFMTCLEEMIAEKNSEGENFFHEAARCGCFDIIARFTPFIRGDCHAAALNATDDAGQMCIHIAAEK
HEAQLAAEIIDHLIELGADINAQEMLEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAI
DNEDVAMMQILREIVATSRGFSNENTDIV
>gnl|CDD|165109 PHA02742, PHA02742, protein tyrosine phosphatase; Provisional
MGAHCSKKNSFAKNCEQLIEESNLAEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVI
LKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWM
PHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAV
READLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLS
LPQQYIFCYFIVLIFAKLMADKC
>gnl|CDD|222925 PHA02743, PHA02743, Viral ankyrin protein; Provisional
MAENGTAGNNLGAVEIDEDEQNTFLRICRTGNIYELMEVAPFISGDGHLLHRYDHHGRQCTHMVAWYDRA
NAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQHETAYHIAYKMRD
RRMMEILRANGAVCDDPLSIGLSDET
>gnl|CDD|165111 PHA02744, PHA02744, hypothetical protein; Provisional
MFIDGKYHYICIAPKEWEEYKRKDLEKLILDSCKDHRKKTTCIHGANTNIAGVSTKLEYNDLKLWLKKQD
DISARPDQGDYFPMLLDI
>gnl|CDD|222926 PHA02745, PHA02745, hypothetical protein; Provisional
MALVGLSSHFFDDANNPLRLLHSPAIRPSVIKEPTRRNYLSNCSQVKKLLEDLFEDISGDLDIRTSTGDY
VSEEEHFGRVDTQEVDEFRGLNAKIRDKVLPIEDNKHDNSETRNPLNKIRQQIRKFTLPPEYDPNDSRWT
LKHRYPGSGLVELLPHSGVYINAINLSNCKELSKDCKSLARLLLLEIFTESALKICSLTGAKATAFDGEG
TDVRPGLDEDARTVLLRYVEIYGEKQRWCTEDHQAIINVIRNKMQESRRKDRHRV
>gnl|CDD|165113 PHA02746, PHA02746, protein tyrosine phosphatase; Provisional
MKDLCFEIFNAFDFFDKTNHAKFCEFVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVI
NAHESLKMFDVGDSDGKKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQV
IVSLTDIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPDW
PDNGIPTGMAEFLELINKVNEEQAELIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEV
CLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAIIEEAKKKFF
>gnl|CDD|165114 PHA02747, PHA02747, protein tyrosine phosphatase; Provisional
MDSNCFAECRAIDFLKRRNQLNCFGIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVIL
DSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTNGEEKCYQYW
CLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIKI
IDINRKKSGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIM
NFDDYLFIQPGYEVLHYFLSKIKAIDKIKFCG
>gnl|CDD|165115 PHA02748, PHA02748, viral inexin-like protein; Provisional
MLDLFSALRGLLKVQSVSIDNNFFRLHYKITVIILLAFSLLVTSRQYFGDPIDCDFPDYPNGSLNTYCYV
QSTFLVERKVTHTVNSTVPDPGVSGDTEEDELRYYGYYQWVFITLFLQAVFFYIPHYIWKAWEGGKMKML
AVELASPVLSKDCIEKNTQPLVDYFFMNLHSHNAYAYKYFTCELLNLINIVGQIQFMNIFIGEDFQLYGI
YVIFFNQEAGKSMTNPMERLFPTVTKCTYEKYGPSGTPENIEGICLLTQNSLNEKIYVFLWFWFHILAVI
SAFVVIYRIATLLSSSLRLYMFRSSSSLNRADDIAVVYNKLQIGDWFLLHMLRKNINPLAYKELISRLAQ
HFDVSVCDSA
>gnl|CDD|165116 PHA02749, PHA02749, hypothetical protein; Provisional
MDFLKILNATVAALFIASSIFFVNNIWLDIAIWIAILVSTAYATEINLALSNARIWFNVLVVSAAIALPQ
AIFAIKLAADGHILAAWIDTIASTIVDAIFVTAFTRRDIIGSDLIRKGLVVFFLFAWSIAALGLNILAWH
PEISAGFHFPLHLIAGAFIAIAGLLLPIIIVLTYRGEAGGIPPGRDILMLLFNAFAMLIASYFLSDALAQ
IHIAEQQLGITSTFLASLPDFITAFIIRALFAEILGSEAGDQEAMATMFAAAVHDQLSIPALILLLAPAA
AGMYPHLFNIVAVIAKFTLLDKKLFWFVGLPGGLAALIALAA
>gnl|CDD|165117 PHA02750, PHA02750, hypothetical protein; Provisional
DDPEELAAETESAIDEIESETSPGDQPKGSEPEEIEFWADAKARKAVEEGREVTNWADWIIGFRLPHAED
KKLEFMIEYTRTWGEEAADARPDIADALARGEAGLAFEATDFMADMVVAGKFGVLDPNIMREIYEYVRDF
EVAQFLFEARDMLKAAYPQIRRASDYYISIPAMELDAVADIIAEAKAKGENDDIRARAEAEAEEGLSPKS
LYFNLYYIARAIGDNEILEIAREIEKLRRK
>gnl|CDD|165118 PHA02751, PHA02751, hypothetical protein; Provisional
MPKIKIIDMMQGKIFDADLDPDKICLSSQISEMFGLPGQKCLPITPDRFAEIMKVAKPGADGLYAEALIL
PDTIRLFHADLFTFSFAETDIFEMFYDARLGAVGIIFGNAFMPLRINLENAKCDNVVGLGRLCVIFGALV
RDDGHAKHVGIITEEEYLEWLRAMAEKNLADSWEVIMIPLQIHEELLNELEEELAKCADKSAYELAVMVI
QQARNIMSQVQALMQIPRGCGQA
>gnl|CDD|177486 PHA02752, PHA02752, hypothetical protein; Provisional
AAAALAIIAGLAIAAFFLMGASGGGGGPNQQPTITGTSAPPAVTDLYPNAALANGFDGILIDDGHFNCDG
GQCSITASAVGSFRSIVAYGARPLSSANATNGIAVIKVGGYEIPLFGFAATNLAIVQDTAFSVYVFPAIK
CRLSTSGGYILYPKLGAAIALAHFQYNINDTNVHVVVPSKSQPATCALAGHHITIDNENATAFIDGTATG
IDIDTLPKQVRGVARAWLVSISAGGRYAFQFN
>gnl|CDD|165120 PHA02753, PHA02753, hypothetical protein; Provisional
MSAIADTIGKFGILGILAAFVPAFVHGAMAGALGLAGNGAIALIQIIALIAIIAHWANFSEADGFAAGAA
FGAGTTAFIGAHDLAIDAILFAIGTLINSIVDTIEKAFLLGIALGFLGFILAPAIFAGIAGFLFGLAAML
ILRLGGLLTEALELGIHALFKHLPEGYAALIAPFIGGIFIALPIAVLGGMFGFALALGLGAVVGGAIAGL
LFMAGEVSAFAGFIINIGLLVAALVIFKTFPKSKDIAEILLDLAAIFIFKFLVGYGIGPALWAAGYAAIS
TRHASRAFYFIALGAIGA
>gnl|CDD|165121 PHA02754, PHA02754, hypothetical protein; Provisional
FSKAEEIPKAIMEKDFKEAMRELKDILSEAGIYIDRIKAITTSGDKIVVITADAIKIELSETEKIIA
>gnl|CDD|165122 PHA02755, PHA02755, hypothetical protein; Provisional
MFRNISGGMAIGSYPDAVQGSPAAEAAEEKYKMKYALGICQALKEADPKAFEETFGAGEADLQKCALAAG
AFADLNFDIWKIKWGRALGAQIAAFA
>gnl|CDD|165123 PHA02756, PHA02756, hypothetical protein; Provisional
AEALKKAIIIFYLAFLGFSWLQLPWFFGIPSVGGFILTPSAHPYIPPLSLIITKPSNECEGWAVKFFEGN
WLGLFEIHLPVVHYFAGVGPVRYEIFNMRASFGNNVLDNIKHYFEAIIDPEMAAVPYNGPCAAEVIAIIP
APIVIIIFAIALGTAIYYGAKRVW
>gnl|CDD|165124 PHA02757, PHA02757, hypothetical protein; Provisional
MVWEFLKGSSKPPRNVCVITPSGPFDFNIACGVDQEKANEILDKDKACIIEIDEDSGMLFSQCDKGKAVA
ARIFD
>gnl|CDD|165125 PHA02758, PHA02758, hypothetical protein; Provisional
MDLRIISKASVEAAAISIAIVGFAILEFSLFSILAAGLAFLGILAIFDSWGLDAAKLPAPMQMFLYLLAF
FGAIGGTQFIIFAAVIIAAFALKEKPKLAAPSHAGLAEPLKLAALAAFVLLLGLILPIILFYDAAKKFRY
DVXGAIALKAAALLGAIGMGLFMFGAALSASTDKVHLLSFGGVFNDAFAGILGPLSEANPIYWVGAIGWE
EFIGRAIGPFANAMFAILHLPSRLAAGYKMTGSDLFAIGIAFGILLLINFGARWLWEIYKEGGIIASIIG
HAFYNAGVSAFADGIKGNPLLAIILIFLGLVGFLYALFKKP
>gnl|CDD|165126 PHA02759, PHA02759, virus coat protein VP2; Provisional
MIIPEGAGALAGLLAIAFFARKAIIFALIAIFISAALAGAAGAIYAAFMALMAAAIAIYAIRQEEGRIIE
KALALFLGLLAIWASDNSAAAQAFALIAYEIVKPFFDAINNVFGVIGAGGAFGALLAWSILAPRIISIAE
EEPLIGAGYVLLAASILAGAVAALPDYLALALAIALIGPFSQALKGDLEALEEIAPALFILATLIPIDTL
APIGAALAIIELAFGVLSKKHLAAAAMWAEAALLA
>gnl|CDD|165127 PHA02762, PHA02762, hypothetical protein; Provisional
LKILIDNDFGNLIIEFKRNVEKSFEGEAFVTIGIDENDKISYISIEPLDKDLKEGIKRIKVL
>gnl|CDD|177487 PHA02763, PHA02763, hypothetical protein; Provisional
MIFNSKIVQKYILNNAKAVATIRKKSFYKIGQKVILKVGDKRFPGKVIAKAPVTEYCLSKYVKFSGFENV
EEWLNEARRLHNDKIDPERYEIIVIWINGRLF
>gnl|CDD|165129 PHA02764, PHA02764, hypothetical protein; Provisional
MEFERKSSGIIKSFNILDIFSINLLYMGILSGISYPLFVSSLLKNVNLLFAILIGAVFEIPLLLMYYKLT
TKFPLNGGDYAYIRTAFSSKFYTIFGISLWLTYVLSQPILGDLVLLNFNIQNQFEQFLIVESLFPIVLLI
IANKKIYAKIVDILAIAQIIIAIFIAFKSFNFQYQNFTISNTLLSALLFDLSAFIFINAISYIAGEIKNI
KKSSMIGYFVSYGIVAILSIIDSYSNLNILFALMPIWFFSYMPIANKIQSRLIQTMSFDKVLPEKFSKIN
PNVLLLIFIAETIANVLENLLGFNISFGLDGLLFIFWNFIIVAFAYLKLMNDKILFFIVLTSLAIQIFLF
FYLGYQNIIFYKFVIAGNIEYTILRIIIIPIIGAIVYLLRKSKINVIPK
>gnl|CDD|165130 PHA02765, PHA02765, hypothetical protein; Provisional
LKKVLNFHFSYIYTYFITITTNYKYGDTEKIFKKFRQYIYNHDKNSHVFSIKETTKNSNGLHYHILVFTN
KKLDYSRVHKHMPPHSDIRIELVPKNISDIKNVYKYMLKTKKDIKMS
>gnl|CDD|165131 PHA02766, PHA02766, hypothetical protein; Provisional
LFFEDSIIQELSLKFKISFEINEEDYQQLIELAFSQFIYPLNDNIEIKINTKELADNEKALLYEIQILRT
KKL
>gnl|CDD|165132 PHA02767, PHA02767, hypothetical protein; Provisional
MEIDIKNECRKYIIQFRNWLESRYSDNIYFFNVFEDEEIILIQIKINMKKKEYEKAGMSILKYLVHTFKY
PNYIKVNWRYDKNMFKISAICGDINMSESEN
>gnl|CDD|165133 PHA02768, PHA02768, hypothetical protein; Provisional
MALLGYECPICGEIYIKRKSMITHLRKHNTNLKLSNCKRISLRTGEYIEIKAEEE
>gnl|CDD|165134 PHA02769, PHA02769, hypothetical protein; Provisional
MNPKYEIEEIKNKELIKLARMLIDYYHIQGMVKGGGAGRNSRYFIYLEKEDDKEYIVAVAWLHDNTPFRF
IAQQYNIPNDRSYFIRRITKTAPGDHLVNFLNDLAEKLKKDGFEVLWTLGFPDHSNALYKKAGFKLVGQT
SRTKHEVYVKYLNK
>gnl|CDD|165135 PHA02770, PHA02770, hypothetical protein; Provisional
MSQIEEIIKTLNKKDIKDIITKNISFLVEPQILFYAKKRNRITGYLEVNGRHYRFELIFSKDNSVSITIG
ELIVFGNGDLK
>gnl|CDD|165136 PHA02771, PHA02771, hypothetical protein; Provisional
MEFEELKSIIDKFFQDQTIIRINLMFNKEIIVSYNQFEEIIKDGDLTHRYADKNITSDFYEYRENIHSII
DYFWKDNKICIIEIDFWRSR
>gnl|CDD|165137 PHA02772, PHA02772, hypothetical protein; Provisional
MNLKKVKRIIDMFFKEKNLDELTLAFKRPLIISENEYNELVGRPNLSFEDKDPWVLSDEFVYYELSNRLV
KLIIHYFKEDDFIHILEIDLFREKR
>gnl|CDD|165138 PHA02773, PHA02773, hypothetical protein; Provisional
MSFYIMDIKVKEMSEEKQIKLRPKQKELLIRFFEIAEKDEDGDLCIPLYDSEGDLFLFKKDANKYQMFAY
FRIKRLIDKNIFFIKIKKVKRDKKFLCIHEDIIDQVKLLLES
>gnl|CDD|222927 PHA02774, PHA02774, E1; Provisional
MADDKGTDPEEGGSGWFLVEAEAECSDGEDELEDLFDTGSDISDLIDDAEVVQGGNSLALFHQQEAEEDE
QQIQALKRKYLSSPEKSPVADLSPRLEAISLSPRKKAKRRLFEEQDSGLGNSLEEESTDVVEEEGVESSG
GGEGGSETGQGGGNGLVLDLLRSSNRRATLLAKFKEAFGVSFTELTRPFKSDKTCCNDWVVAVFGVSEEL
LEASKTLLQQHCDYLQIQCLTCEWGFVALYLLRFKAAKSRETVRKLLSSLLNVPEEQLLLEPPKLRSVAA
ALFWYKKSMSNASYTHGELPEWIARQTLLSHQLAEAEQFDLSKMVQWAYDNDYTDESEIAYEYALLADED
SNAAAFLKSNNQAKYVKDCATMVRHYKRAEMREMSMSQWIKKRCDKVEGEGDWKPIVKFLRYQGVEFISF
LTALKDFLKGIPKKNCLVIYGPPDTGKSMFCMSLIKFLKGKVISFVNSKSHFWLQPLADAKIALLDDATH
PCWDYIDTYLRNALDGNPVSIDCKHKAPVQIKCPPLLITSNIDVKAEDRYKYLHSRITVFEFPNPFPLDE
NGNPVFELTDANWKSFFERLWSQLDLSDQEDEGEDGEPQRTFRCTARAANGSL
>gnl|CDD|165140 PHA02775, PHA02775, E6; Provisional
MAGAGQQGKASCCAQEKDHGTPLLPHTIRELCLAQGIEFPCIQLCCHYCKKCLSLLDIYAFDQSCLNLLW
GDGGPAAICSLCLRLLARLEFRARHEFSCAAQHIPHFIGQPFSDCEVRCVRCLALLQSVEKDFIAREDLS
VHFIGGILRGLCTHCMAGLF
>gnl|CDD|165141 PHA02776, PHA02776, E7 protein; Provisional
MHGKHPTLKDIVLDLQPPDPVGLHCNEQLVDSSEDEVDEQAGQASQATQRIKQAFQIVTCCCGCDNNVRL
VVECTEPDIQELHNLLLGSLNIVCPICAPKT
>gnl|CDD|165142 PHA02777, PHA02777, major capsid L1 protein; Provisional
MLARQRIKRANPEQLYATCKATGGDCPPDIIKKIEGNTPADKILKWGSTGVFFGGLGIGTGRGGGGTSLG
AGAIGSARPSIPAGAIGPGDIIPIDAEAGALAEEIELLPMAPISGRARDPFGEGFGEEPFDPIGIPPERP
NILHEQRFPTDAAPFDNGNTDIATIEGPHDPFGAGGDIAIIELPSVNDPGPSVTARTQYNNPAFEVEIHS
DIPSAETSSTDHIIVGAESGGSFVGDDAEFEIPLLDAERAILDDQADTSFIAHGEEEEAFLTSTPDPVLP
IQEAIAPIRPYGRQFGQVRVGDAAFLDRAAVLFQAENPAFDADISILFEDDLADAERLDDDFQDIQRLSR
PYYQRRATGLRLSRIGQREGIIQTRSGTQVGSAAHFFQDISPIGQAIEPIDAIELDSIGEHSGEGTIVRG
DPTPSIEQDIGLSAAADNIEEELQEADLLDADEEEDQEARDLQLLFSFASTGEDEEDDIIQIPIDAGGDD
KPSTAFFPDDGTHIAYPTPTKATTPLLPAQPIDDPYITLDLFQGSMDYDIHPSLLPRKKKKRKIL
>gnl|CDD|222928 PHA02778, PHA02778, major capsid L1 protein; Provisional
MALWLPSSGKLYLPPTPVAKVLSTDEYVTRTNIFYHASSDRLLTVGHPYFPIKDADKNKVTVPKVSGNQY
RVFRVKLPDPNKFALPDKSVYNPEKERLVWALRGLEVGRGQPLGVGVTGHPLFNKLKDTENPNKYPTAQG
TDDRQNVSFDPKQTQLFIVGCTPALGEHWDKAKPCADAPPQAGDCPPIELKNSVIEDGDMVDIGFGAMNF
KALQANKSDVPLDIVNSICKYPDYLKMANDPYGDSMFFFARREQMYARHFFTRAGTVGEAIPEDLYLKGA
SGQAQTLGSSVYFPTPSGSLVSSDAQLFNRPYWLQRAQGHNNGICWNNQLFVTVVDNTRNTNFTISVKTD
ETPQTTYKASNFKEYLRHVEEYELSFIFQLCKVPLTPEVLAHLHTMNPSILEDWNLGFVPPPSSSLEDTY
RYIQSLATKCPDNVPPKEKEDPYAKYTFWEVDLTERFSLDLDQFPLGRKFLFQAGLRRRTRRRKRKSTSS
SSSRSTKRRRRKR
>gnl|CDD|222929 PHA02779, PHA02779, E6 protein; Provisional
MESANASTTARTIDQLCKQCNLTMHTLQINCVFCKSILQTAEVYSFAYKELYVVWRGDFPFAACAKCLEF
YGKVNQYRHFDYAAYAPTVEEETGLTILDVRIRCYLCHKPLCPVEKVNHILKKARFIKLNCSWKGRCLHC
WTKCMEKGLP
>gnl|CDD|177490 PHA02780, PHA02780, hypothetical protein; Provisional
MKHRVYSEGLSISTDLNSIISQQSTMDTDMEIDEDEIMELLNILTELGCDVDFDENFSDIADDILESLIE
QDV
>gnl|CDD|165146 PHA02781, PHA02781, hypothetical protein; Provisional
MLLEMDKIKITVDSKIGNVVTISYNLEKITIDVTPKKKKEKDVLLAQSVAVEEAKDVKVEEKNIIDIEDD
DDMDVESA
>gnl|CDD|165147 PHA02782, PHA02782, hypothetical protein; Provisional
MAMFYAHAFGGYDENLHAFPGISSTVANDVRKYSVVSVYNNKYDIVKDKYMWCYSQVNKRYIGALLPMFE
CNEYLQIGDPIHDQEGNQISIVTYRHKNYYALSGIGYESLDLCLEGVGIHHHVLETGNAVYGKVQHDYST
IKEKAKEMSALSPGPIIDYHVWIGDCICQVTAVDVHGKEIMRMRFKKGAVLQIPNLVKVKLGENDTENLS
TSISALLNSGGGTIEVTSKEERVDYVLMKRLESIRHLWSVVYDHFNVVNGKERCYIHMHSSNQSPMPSTV
KTNLYMKTMGSCLQMDSMEALEYLSELKESGGRSPRPELPEFEYPDGVEDTGSIERLAEEFFNRSELQAG
ESVKFGNSINVKHTSVSAKQLRTRIRQQLPSILSSFANTEGGYLFIGVDNNTHKVIGFTVGQDYLKLVEN
DIEKYIKRLRVVHFCEKKEDIKYACRFIKVYKPGEETTSTYVCAIKVERCCCAVFADWPESWYMDTSGIK
KYSPDEWVSHIKF
>gnl|CDD|165148 PHA02783, PHA02783, uncharacterized protein; Provisional
MYKKLITFLFVIGAIASYSNNEYTPFNKLSVKLYIDGVDNIENSYTDNNELVLNFKEYTISIITESCDVG
FDSIDIDVINDYKIIDMYTIDSSTIQRRGHTCRISTKLSCHYDKHPYIHKYEGDERQYSITAEGKCYKGI
KYEISMMNDDTLLRKHTLKIGSTYIFDRHGHSNTYYSKYDF
>gnl|CDD|165149 PHA02785, PHA02785, IL-beta-binding protein; Provisional
MSILPVIFLPIFFYSSFVQTFNAPECIDKGQYFASFMELENEPVILPCPQINTLSSGYNILDILWEKRGA
DNDRIIPIDNGSNMLILNPTQSDSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGE
MVCPNINAFIASNVNADIIWSGHRRLRNKRLKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRI
VKLEVRDRIIPPTMQLPEGVVTSIGSNLTIACRVSLRPPTTDADVFWISNGMYYEEDDEDGDGRISVANK
IYTTDKRRVITSRLNINPVKEEDATTFTCMAFTIPSISKTVTISIT
>gnl|CDD|222930 PHA02786, PHA02786, uncharacterized protein; Provisional
MMIYGLIACLIFVTSSIASPLYIPVIPPITEDKSFNSVEVLVSLFRDDQKDYTVTSQFNNYTIDTKDWTI
NVLSTPDGLDIPLTNITYWSRFTIGRALFKSESEDIFQKNMSILGVSIECKKPSTLLTFLTVRKMTRVFN
RFPDMAYYRGDCLEVVYVTMTYKNTKTGETDYTYLSNVGIPEYYRLMNGVDG
>gnl|CDD|165152 PHA02789, PHA02789, uncharacterized protein; Provisional
MHIAIYAISLASLLSLIDCHKLAFNFNLEINGSDIHNTADILLDDSPIITFDGKDIRPSIAFMIGDEIFL
DFYKNIFSEFFRLFRRVPTSSPYEDLEYFYECDYTDNKPTFDQFYFYNGEEYTEIDKSKEATNKNMWLIT
SEFRLKKWFDGEDCIIHLRSLVRKMEDSKKNSG
>gnl|CDD|165153 PHA02790, PHA02790, Kelch-like protein; Provisional
MPIFVNTVYCKNILALSMTKKFKTIIEAIGGNIIVNSTILKKLSPYFRTHLRQKYTKNKDPVTRVCLDLD
IHSLTSIVIYSYTGKVYIDSHNVVNLLRASILTSVEFIIYTCINFILRDFRKEYCVECYMMGIEYGLSNL
LCHTKDFIAKHFLELEDDIIDNFDYLSMKLILESDELNVPDEDYVVDFVIKWYMKRRNRLGNLLLLIKNV
IRSNYLSPRGINNVKWILDCTKIFHCDKQPRKSYKYPFIEYPMNMDQIIDIFHMCTSTHVGEVVYLIGGW
MNNEIHNNAIAVNYISNNWIPIPPMNSPRLYASGVPANNKLYVVGGLPNPTSVERWFHGDAAWVNMPSLL
KPRCNPAVASINNVIYVIGGHSETDTTTEYLLPNHDQWQFGPSTYYPHYKSCALVFGRRLFLVGRNAEFY
CESSNTWTLIDDPIYPRDNPELIIVDNKLLLIGGFYRGSYIDTIEVYNNRTYSWNIWDGK
>gnl|CDD|165154 PHA02791, PHA02791, ankyrin-like protein; Provisional
MDLSRINTWKSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEFPLHQAAT
LEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWKTSFYHAVMLND
VSIVSYFLSEIPSTFDLAILLSCIHITIKNGHVDMMILLLDYMTSTNTNNSLLFIPDIKLAIDNKDLEML
QALFKYDINIYSVNLENVLLDDAEIAKMIIEKHVEYKSDSYTKDLDIVKNNKLDEIISKNKELRLMYVNY
VRKN
>gnl|CDD|165155 PHA02792, PHA02792, ankyrin-like protein; Provisional
MVNDKILYDSCKTFNIDACSAQSLIESGANPLYEYDGETPLKAYVTKKNNNIKNDVVILLLSSVDYKNIN
DFDIFEYLCSDNIDIELLKLLISKGLEINSIKNGINIVEKYATTSNPNVDVFKLLLDKGIPTCSNIQYGY
KIIIEQITRAEYYNWDDELDDYDYDYTTDYDDRMGKTVLYYYIITRSQDGYATSLDVINYLISHEKEMRY
YTYREHTTLYYYVDKCDIKREIFDALFDSNYSGNELMNILSNYLRKQYRNKNHKIDNYIVDKLLSGHDTF
YILELCNSLRNNIIISSILKRYTDSIQDLLSEYVSYHTVYINVIKCMIDEGATLYRFKHINKYFQKFDNR
DPKVVEYILKNGNVVVEDDDNIINIMPLFPTLSIHESDVLSILKLCKPYIDDINKIDKHGRSILYYCIES
HSVSLVEWLIDNGADINITTKYGSTCIGICVILAHACIPEIAELYIKILEIILSKLPTIECIKKTVDYLS
NDRYLLIGNKNKSLLKICIKYFILVDYKYTCDMYPSYIEYITDCEKEIADMRQIKINGTDMLTVMYKLNK
PTKKRYVNNPVFTEWAKKQYKFYNQIIYNANKLIEQSKKIDNMIDEVSADNNRLSTLPLELRHLIFSYAF
L
>gnl|CDD|165156 PHA02793, PHA02793, hypothetical protein; Provisional
MYYANICLDFDNNVYTIKDKNYTNAVIEYPVVCNFRRYSESDSGSDVDDRAELHKHNNDSDSDDYT
>gnl|CDD|165157 PHA02795, PHA02795, ankyrin-like protein; Provisional
MESADFMAVDEQFHDDLDLWSLSLVDDYKKHGLGVDCYVLEPVVDRKIFDRFLLEPICDPVDVLYDYFRI
HRDNIDQYIVDRLFAYITYKDIISALVSKNYMEDIFSIIIKNCNSVQDLLLYYLSNAYVEIDIVDFMVDH
GAVIYKIECLNAYFRGICKKESSVVEFILNCGIPDENDVKLDLYKIIQYTRGFLVDEPTVLEIYKLCIPY
IEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSVIARRETHLKILEI
LLREPLSIDCIKLAILNNTIENHDVIKLCIKYFMMVDYSLCNVYASSLFDYIIDCKQELEYIRQMKIHNT
TMYELIYNRDKNKHASHILHRYSKHPVLTQCITKGFKIYTEVTEQVTKALNRRALIDEIINNVSTDDNLL
SKLPLEIRDLIVSQAVI
>gnl|CDD|222931 PHA02798, PHA02798, ankyrin-like protein; Provisional
MDIDNLYNYITFSDNVKLSTVKLLIKSCNPNEIVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNE
YSTPLCTILSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMIENGADTTL
LDKDGFTMLQVYLQSNHHIDIEIIKLLLEKGVDINTHNNKEKYDTLHCYFKYNIDRIDADILKLFVDNGF
IINKENKSHKKKFMEYLNSLLYDNKRFKKNILDFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQL
GGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYYKLRKHILNVEGDFINQLEFDIIKKF
IAYVILYVKNFSIRNLTYPFIFTYFDDFIEKCTKSINEIHNTYVNNETIFQICFNKKYIPIKYINNKKLK
KYTKLFYYGNIIKKIIEKSKKRYENIYKVSCYITKICSNELSYWNYIPNEIKFKIINNLSNNDILETFF
>gnl|CDD|165159 PHA02800, PHA02800, hypothetical protein; Provisional
METNTLPFSKRYIHDFTDYDNFEKKNSFSMSYQLTGFLQYYFIWRFNGGKVDENTGKIFKEFFKYDTLAK
WRFSKRDFEQCKNMLLENDKNTSYVLDVPKPEKNDPLLNLKELIGFLAILSEEIKKDTKFFALFNIMNSL
FKHTKIDIVNCLKTELQFLYP
>gnl|CDD|165161 PHA02807, PHA02807, hypothetical protein; Provisional
MESEIKRLTNIIKERNIICPIDIEKIYNEKFLLLEKGLDETLYAIHIYDSMARFDNGTFFKIAKFLYRND
IDVLKKIFIDEKKIESTNALLPIYSVNIIERKNALIPLTEIPNGSEGILLILLHLFNSFKFNKLTNISTI
PYYLPFGKYINNIII
>gnl|CDD|222932 PHA02809, PHA02809, hypothetical protein; Provisional
MKEVYTNFNISLNTTKQKIEVMGSVPTIDGKDPSIDIRIVSKPNKEKNNFLDNGYDESFIKPNKVSYDET
NIDKGQKIEQTDNEKQLLSDFSDILNNDEKNHEDTIKNVVK
>gnl|CDD|165163 PHA02811, PHA02811, putative host range protein; Provisional
MGIRHELDILLVSENLALKNVELLKGDSYGCTINIKVNQQKKLDFIIILRPDWTEVRNVKKINMVCNGVV
IDTTLIKKSFYEEVYSSSVTVFQNTTVEFFSDTSKKYKEEYPIVNINTIKRYYEIKDSRMTCINFESPIS
DYDQVNYLKDYINISDDYYLYDACDYCIISSDDDDDNDNADNDEEDDEVNDIEDDYE
>gnl|CDD|165164 PHA02813, PHA02813, hypothetical protein; Provisional
ETISDGIIKVKTFNDDYFNNVKKIIMDMIKYKDIIWEESKVFDHEKGGEVINTNERQCKQYIIRGLDDIF
KVIRKKLLLSFEFPQKISDIILDNTITLIKYEKGDFFNNHRDFIHFKSKNCYCYHLVLYLNNTSKGGNTN
IHIKDNTIFSTKNDVLFDKTLNHSSDIITDGEKNIALINVVIKYNSNNDETIFKLPYLSENNLINFYEDE
GNRKFCYCLVTVNNYSTEVDTFGLILNRSGKCVLVNKYDKIITEKLIFENFDDMCMEIAFSYNDIIFDYL
KNEDGKNIAWKALSKSCDEMWYPKSKNDFDFLKDLVKYVNNNLKDKIDYYVLTGNCNSEIHYINFNVVRC
YFSI
>gnl|CDD|165165 PHA02815, PHA02815, hypothetical protein; Provisional
MVLIIVIVISLYLLFQLVNCFYLFKLFNKIKVKMMNITTKISFDELENVYYIDDTYTCVGVNVD
>gnl|CDD|222933 PHA02816, PHA02816, hypothetical protein; Provisional
MDKKIYCGIVFGYKLLKKSIKEKAIKCVSFIRKSNMKKAISIERVTLLDSDGANDSDSSSNTVSSDDNDT
KYNYNYKYKFTKRKTPHKVMYYINYDDSVSNDDVFL
>gnl|CDD|165167 PHA02817, PHA02817, EEV Host range protein; Provisional
MKNIHMLLILLCNKVYSLCDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNTRGVRYTLVGEKNII
CEKDGKWNKEFPVCKIIRCRFPALQNGFVNGIPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIP
KVPICSRDNITYNKIYINKVNIDDNFFNQINNSNTYYFDKILQINNVNRYTLIFFVVVSIKILFGFVFIF
FSCNKKPLDSIKYYK
>gnl|CDD|165168 PHA02818, PHA02818, hypothetical protein; Provisional
MAEILTNKLKSIDNENKYNEKFIECIIQEIEKQQYFILKPIVRFIIDVMIIVIVLNDLTIRLLKRNYKIL
FSILLLSILYDAFTHSDVSSDI
>gnl|CDD|165169 PHA02819, PHA02819, hypothetical protein; Provisional
MDKLYSAIFGVFMSSSDDDFNNFINVVKSVLNNENYNKKTKKSFLRYYLIIGLVTIVFVIIFIIFYLKVI
K
>gnl|CDD|222934 PHA02820, PHA02820, phospholipase-D-like protein; Provisional
MNPDNTIAVITETIPIGMQFDKVYLSTFNFWREILSNTTKTLDISSFYWSLSDEVGTNFGTMILNEIIQL
PKRGVRVRIAVNKSNKPLKDVELLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQ
VKELGIAIFNNSNLAADLTQIFEVYWYLGVNNLPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQ
LCTMERTNDLTALLSCIRNASKFVYVSVMNFIPIIYSKAGKILFWPYIEDELRRAAIDRKVSVKLLISCW
QRSSFIMRNFLRSIAMLKSKNINIEVKLFIVPDADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDT
CGVSINITPDDGLGLRQQLEDIFIRDWNSKYSYELYDTSPTKRCRLLKNMKQCTNDIYCDEIQPEKEIPE
YSLE
>gnl|CDD|222935 PHA02823, PHA02823, chemokine binding protein; Provisional
MKRLIVLACMCLAATAAPTSLQSSSSSCTEEENKHHMGIDVIIKVTKQDQTPTNDKICQSVTEVTESEDD
PSEEEEYEGDESFLEGFVIPTTYYTIVGGGLSMNFGFTKCPTIKSISESADGNTVNARLSSVSPGQGKDS
PAITREEALAMIKDCEVSIDIKCSEEEKDSTIKTHPVLGSNISHKKVSYEDIIGSTIVDTKCVKNLEFSV
RIGDMCKESSDLEVKDGFKYVDGSASEGATDDTSLIDSTKLKACV
>gnl|CDD|177491 PHA02825, PHA02825, LAP/PHD finger-like protein; Provisional
MEDVSLMDKCCWICKDEYDVVTNYCNCKNENKIVHKECLEEWINTSKNKSCKICNGPYNIKKNYKKCTKW
RCSFRDCHDSAIVNSLLCLIVGGITYLLVSFNIKKLIESEENSDLIKLFLVVAYLLPFVVTFITVIRICI
DLYTYFLATRKRNTIHTVYELE
>gnl|CDD|165173 PHA02826, PHA02826, IL-1 receptor-like protein; Provisional
MKVIIFFIIILQFISAFLCLYCKYRGGDLTPVYAKFGDPMVLLCTGKHYKKSIFFDKTFITSYNVTWSKT
DSLAFVRDSGARTKIKKITHNEIGDRSENLWIGNVINIDEGIYICTISSGNICEESTIRLTFDSGTINYQ
FNSGKDSKLHCYGTDGISSTFKDYTLTWYKNGNIVLYTDRIQLRNNNSTLVIKSATHDDSGIYTCNLRFN
KNSNNYNITKEYKVTII
>gnl|CDD|177492 PHA02827, PHA02827, hypothetical protein; Provisional
MSMTNYVYRNNFSDDDDITTAVQDYLYWSSLPFRSREPAGNVFAVFESFKRDASIVFGDDLTWFVKCMFL
DSKEGFDHSKSMIRAMLKKENYIREACAVIGLLARAAEYWGGESSPTPASAKVLELLMELLTDNDISHVK
SALIIRLKRL
>gnl|CDD|165175 PHA02828, PHA02828, putative transmembrane protein; Provisional
MFSFVINMIYNLFYYITSSVSKLFIFIVSKLILFMLQMVNPYSSYSIISYLNPFKKEEYSFFNPLRLINK
INPFYKEEKKEGILNWLGMKKTETKSWKLF
>gnl|CDD|165176 PHA02831, PHA02831, EEV host range protein; Provisional
MINLTKIIILLFISKTWCICVFNKNDAKYSNVDSYENKVYEENENLEYKCNNNFDKVFVTCNNGSWSTKN
MCIGKRNCKDPVTILNGYIKNKKDQYSFGDSVTYACKVNKLEKYSIVGNETVKCINKQWVPKYPVCKLIR
CKYPALQNGFLNVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWYPGIPKCVKDKVHNEIQPNYLF
DDLDEDFNNSTTNYNMQQNIITIIILLSIICFIFVLGLIALFLSCNKSTLKPSIYNKF
>gnl|CDD|165177 PHA02834, PHA02834, chemokine receptor-like protein; Provisional
METTVVVDNYSYYFEEECDFEMVNSDVNYFVIVFYILLFIFGLIGNVLVIAVLIVKRFMFVVDVYLFNIA
MSDLMLVFSFPFIIHNDLNEWIFGEFMCKLVLGVYFVGFFSNMFFVTLISIDRYILVVNATKIKNKSISL
SVLLSVAAWVCSVILSMPAMVLYYVDNTDNLKQCIFNDYHENFSWSAFFNFEINIFGIVIPLIILIYCYS
KILYTLKNCKNKNKTRSIKIILTVVTFTVVFWVPFNIVLFINSLQSVGLIDIGCYHFKKIVYSIDIAELI
SFVHCCVNPIIYAFVGKNFKKVFKNMFCRTNNIFIRQSSNNVI
>gnl|CDD|165178 PHA02835, PHA02835, putative secreted protein; Provisional
MILLIFLCIVITNLSPSYCNEYIDSTILVNIKLGKKTCCNGFTYLLDNNLEFYNIMYSNVNVSINIENCY
FNNSIFKNTKHKNISILLTSKSNIQKNIAIIPITCKITIDITCTKNGKKKCLAQEKLPKIPNLIYKTAEH
VNGIIDLNIYGSCVKYIYTRVNIYEISNGNLIYDQLDSNFLKLNTK
>gnl|CDD|165179 PHA02836, PHA02836, putative transmembrane protein; Provisional
MDLQDNGIINDYSLFFAYDTANTISANDSLKNILDDYFTWRAMVGRIGFVPVGIGNLFLKLMNLNTYFDK
DSINLLTSNLSKKGFISRFKKYLYSNYDVSYVSALTLIGIIGYISECCGKYGLEKYIQDLLLLLFNFLDD
NILFKLRYYLIKK
>gnl|CDD|165180 PHA02837, PHA02837, uncharacterized protein; Provisional
MIKITVSDKKVTIESNNEFSFLLTHNNGILNNCNFVNNIEKSYLLNDEIQDSDNIFNIISNYLWYRGFIG
LEHSKCGRLFKELLRFDLEAKRKYGSVKTIFNILNLDSNDGIFNLKKFILLQKTITKDFNVYHCIEIIGL
CGIIVEEWKKMGRYLNWLNISNNIFKALGLNVFTDLKKFLQNRLLYEELI
>gnl|CDD|165181 PHA02838, PHA02838, hypothetical protein; Provisional
MSLTTLTMTITIKEDSVNIMGSVPIKDNSNININILKENKKIDKNENLYIVVSDTDTISNDDTEKNKK
>gnl|CDD|165182 PHA02839, PHA02839, Il-24-like protein; Provisional
MKLYFYCIFFYKIIVTISLNCGIEHNELNNIKNIFFKVRNVVQADDVDHNLRILTPALLNNITVSETCFF
IYDMFELYLNDVFVKYTNTALKLNILKSLSSVANNFLAIFNKVKKRRVKKNNVNVLEIKKLLLIDNNCKK
LFSEIDIFLTWVMAKI
>gnl|CDD|165183 PHA02840, PHA02840, hypothetical protein; Provisional
METEFLSVKITSNSGNTISIYCETKTTVSIDITTKKNVDNVNTTLKKVKKKESTKNEEPKKNETSSDNED
SDNAMEIDSNKE
>gnl|CDD|165184 PHA02841, PHA02841, hypothetical protein; Provisional
MGDKYVKSIKRKIYSLNFFKKTFKKTYSPCKEIGVTSINNYGIFTHEQQMLLDEDNDQQILIDENDDQQM
LINDEQNIFSFKIIKKPYKVIRFMGNGDDEVFI
>gnl|CDD|165185 PHA02843, PHA02843, hypothetical protein; Provisional
MGNCSRKQNKNIKTSDDYDYYLDNFLDNEYFKFSCTNVNNNKLKNKNKNHTRRNNNNTIDSRKSYCSIKS
VYF
>gnl|CDD|165186 PHA02844, PHA02844, putative transmembrane protein; Provisional
MDKLYTAIFGVFLSSENEDFNNFIDVVKSVLSDDYDGVNKNNVCSSSTKIWILTIIFVVFATFLTFLYLK
AVPRT
>gnl|CDD|165187 PHA02845, PHA02845, hypothetical protein; Provisional
MAEVLFSKLKSIERENLLNESILDCIINEIENNHHYLFRPFIRLTIDLILLIIVMIFLMIRILKRNYFAL
FIIFLFYLFISFRNQIAIVFN
>gnl|CDD|165188 PHA02849, PHA02849, putative transmembrane protein; Provisional
MNNTKHLNDIEFDAGAVTVILVFVLVISFLAFMLLYLIKWSYVINFLNDMKIKLINLTTRRSFTHLNNVY
YTSDNIVGLNTD
>gnl|CDD|165189 PHA02851, PHA02851, EEV glycoprotein; Provisional
MIIPYIIVSCSLIILIVYLFLINKKYCKKFFKKKNKPVCIELKKIINTNKTLTLNSEDWTDMGSCEIYAN
FRSSKREKSFKLKDEQQNSSSTSSGDSEFDSTINTDDESEKLNWDNEEYKYDYDKSESTVYDLPQDNIAE
DTVYDVTDNVENITYDLPQDSIIYDLDEKSDVAVYDIPELEDNVYENNICLESCFDDVKYNSPLNNFNKN
YYSYNTNDFVSNV
>gnl|CDD|165190 PHA02852, PHA02852, putative virion structural protein; Provisional
MDQIKKINDIIQNCNAVFSNEVNLLYNEKFIFLEKNLNGLPFKAHIYNNVSRFDNKTIFRVVKYVYKNRP
KILKLIFPNNSFFESLEPLLPVKTINLSYNNTINDDLQDNTLSTKMILLELFNSFKFGKKSNYLVKYPYY
YLPLRKDINDIVT
>gnl|CDD|165191 PHA02854, PHA02854, putative host range protein; Provisional
MGITHELDIFVTNEDLALKNVELFKGNSYGCFINLKVKEEKKFNIIFVLKPDWSEIDSVKPIRMEVNNNS
VDVEKVSESLYEVVYSASFSINSDSYVKVFSDNPDKYKHMYPTVTINVPKKKFKVVDQGNTYMFIQSPID
DCDKEQFLKDEFEYYDSDNDFDDYEDCDKNRNDSFDDY
>gnl|CDD|222936 PHA02855, PHA02855, anti-apoptotic membrane protein; Provisional
MEDNCNFNESIKKVLNFYINDKALIGEKKSLNNYENKILNLIKECCEVIKKNYKTNFNEICNFIKVNDVT
EENINDIKSQIIESLNNDNRPSVKLAIISLISMIAEKKGYKNNNIVMSDLINEIANKISENSKDLISFIE
RDKKKNVDNDILFSVINFFVIVGIIILLYYLLKIIGKIRW
>gnl|CDD|165193 PHA02857, PHA02857, monoglyceride lipase; Provisional
SANCMFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEK
MMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNAEAVPRL
NLLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKT
PILILQGTNNEISDVSGAYYFMQHANCNREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRVKV
>gnl|CDD|165194 PHA02858, PHA02858, EIF2a-like PKR inhibitor; Provisional
MSSKSDLAFCYVFPNINEVTKGIVFVKDNIFYVKLIDYGLEALIVNYVNVNADRAEKLKKKLVGKTINVQ
VIRTDKLKGYIDVRHV
>gnl|CDD|165195 PHA02859, PHA02859, ankyrin repeat protein; Provisional
KEKLCSEYDYNDFTDYLFYRYCNPLFYYVEKDDIEGVKKWIKFVNDCNDLYETPIFSCLEKDKVNVEILK
FLIENGADVNFKTRDNNLSALHHYLSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRINV
IKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRNLFFNKQ
>gnl|CDD|165196 PHA02861, PHA02861, uncharacterized protein; Provisional
MEFCPGYCLVDCLNRDDDIRQIIVDYIYWSMYSYRSRSPAGKVFQVLKMFRRDSEIVFGENFRHIVKNFK
TLGIEDTVQAVKCFTVGKNALRESVSMVDLCASLAEYWGGEDLPTNDSLQALKLMTILLSDDDYSFIELC
LRVRLKKLK
>gnl|CDD|165197 PHA02862, PHA02862, 5L protein; Provisional
MSDICWICNDVCDERNNFCGCNEEYKVVHIKCMQLWINYSKKKECNLCKTKYNIKKTYVSFKKWNWCFND
KKTTLSKIFFILFALVFIFLTISLSNDMASLVTGINDTICSIIFLIVYTVVMLTSICFSVFVVAIVVDFL
LEAKEKNSFLTIREIV
>gnl|CDD|222937 PHA02864, PHA02864, hypothetical protein; Provisional
PSSCVIVKNFIKDYRSGRIIRKYIKKLSKDEFKQFCSIFMVNADFSFYDKRPNLKEVIKILREEFYGCDL
RLFYDIISVVPNKLNVCKIIKDENNNLLIKSNYLNKKINYIILDKVFKNHSIDDIIYMYFNWRKKYNNIV
SCGKVFKELMKYDEIAKKQYYKDIHKDINNFKLNNKYKINIYEKFNGDIINHCKVSIGFVSILFSKIPLD
YDFDTIFFNQVSIRYRLIFKKELISTLNYN
>gnl|CDD|165199 PHA02865, PHA02865, MHC-like TNF binding protein; Provisional
MKKLILILSSIVAYCNAITFLVYNYTVTLKDDTGLYDFVVTDYFNDQLIKRIKLNHETGRPENVNFRPTW
FNETKIPHYPGNDYNFNFWLNLMKETLEEINKNESTKYTSLSLIVGCTDLGQLFGSFGYVEVAGGILARF
DTKNKRFTKVTSKGFPKVGMLTVKSPFWKDVMKYLGSFVYLTCGLTANDYQKMAKGNIPKPVTPTVKVTG
EELGDNTTLFCTFDSHYPSSVAAKWYNSEDFAPEYRYGRYYPELGRDTDYEPGEPGFPTNTKKDNDKNTF
SSTPSVRVPTDMSNQIVCVVFHSTLEPQIYRCSEGCNGPLPDHQYRGDEEGDEEDEED
>gnl|CDD|165200 PHA02866, PHA02866, Hypothetical protein; Provisional
MEVITDGVLRLKSFRDDFKGIKEELKFMLNSWEDSDILRHRQFIPCEILVLEKSERTKQVFGAVKRVLAS
SLTDYDVYVCEHLTIVKCFKGVGFDNRFSILTEDRHRGREYTLVLHLSSPKNGGKTDVCVGDKTVISTAD
DFLLEKRSEQLSNVVQEGEKIVVAVKVFLLRKEADVIFTLARFSKDVKFYEKEGDRNLCYALVEVNSPFA
EVESFGVITDRSGRCLLVNRYQKLVKKVMVEKTFVDMCTEISFDGFYNLSNVEGKDMAWKELKAVKEDLW
VPSSEEDYKFLRELVDYVSSNLKTKVGYYVLSTCDDDETQYVSLNVIRCYFSI
>gnl|CDD|165201 PHA02867, PHA02867, C-type lectin protein; Provisional
MPILLKKQVSEVSCYAITVLGILCLILFTILVVVTCKWYYAFPYFSKVCPDEWIGYNSKCYYFTINETNW
NDSKKLCDVMDSSLIRFDNIETLNFVSRYGKGSYWIDINQNRKIPGINFSLYYEQGVNDICLLFDTSNII
EMSCIFHERTICVKEDRYTHWYTEYMR
>gnl|CDD|165202 PHA02869, PHA02869, C4L/C10L-like gene family protein; Provisional
MEFSCTGTNNQLAVHRFTETRFTSFKKELLVNLGISDLNDIKNICEDSKIFFPEKRTELLSIKDRKSKQI
VFENSLNDDLLKKLHALIYDELSTVVDSVTVENTVTLIMYEKGDYFARHRDFSTVFSKNIICVHLLLYLE
QPETGGETVIYIDNNTSVKLKTDHLFDKTIEHESITVESGRKCVALFDVLLEKKLSASTNVIGSIEYLGK
KINLYDRENDLQLCYCDMVIERMTEDKEYSLGMISDRSGRCIKSHHNGSIVRYRKEEYGSFDALCIYNMN
EVDEIWTGDKKHIIWSTIDKKTGTSFIPIDPVLYEKLKAISSKEHKEYKDLRGFCNSRTEYICCSVSKYY
FDLPTKTDLIHEVINSIDYDTKSVGTPDWYTLPIEVKQTILGNMSYEELFNIVRGNIALEEDNEYGCD
>gnl|CDD|165203 PHA02871, PHA02871, hypothetical protein; Provisional
MIVEKIAAWLLYPLCLLRCFICNSLCPATCKCIHCILYPFEVCCECMSETLDSLEHSCCYCCVLPLLIIR
EFWRRVILPTLKATCDCIRLPCILTRRFCKRTICPLAKAWCRCFCCPCEVFLRCLCFPCMMLRRLHRGKL
TGVREPGAFRDSRDPARRGTWVNDWCDDLCIWIWSPCCYVKRCIRTMCDTFTKKFFYWFIAPAGSPRMPD
EPSELSRKVFSS
>gnl|CDD|222938 PHA02872, PHA02872, EFc gene family protein; Provisional
MVLNFYVRYIGQESGKSILASASDPLNSENDHTGDGIFEAITIRNIDFCRPRYLCADAGDTVKIYFLEGK
GGLIFSVSDVGSPDNEEDSGYVNEGECVEFETDFACFITLACTSPINTVVYWLE
>gnl|CDD|165205 PHA02874, PHA02874, ankyrin repeat protein; Provisional
ASQDLRMCIYSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPH
PLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESI
KMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI
DHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDGSTPLHHAINPPCDIDIIDILLYHKAD
ISIKDNKGENPIDTAFKYINKDPVIKDIIANAVLIKEADKLKDSDFLEHIEIKDNKEFSDFIKECNEEIE
DMKKTKCGCDKNIFDLCLIRIKHKFDGNEDSIKDYLNCLDDNSHRMLKTIDINEFPIYSMYISRCISDNG
KILKDMGFCIHNNI
>gnl|CDD|165206 PHA02875, PHA02875, ankyrin repeat protein; Provisional
MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIES
ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLH
LAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAI
ENNKIDIVRLFIKRGADCNIMFMIEGEECTILDMICNMCTNLESEAIDALIADIAIRIHKKTIRRDEGFK
NNMSTIEDKEEFKDVFEKCIIELRRIKSEKIGKKNILDLCILEKNSHNLDENILARHSKKILGLNDEAHF
YKYLLKEAADIALKRAEAIESAIRVIDDEITGDESKWNILPHEIKYLILEKIGNKDIDIAIMK
>gnl|CDD|165207 PHA02876, PHA02876, ankyrin repeat protein; Provisional
MCPDDLYRIMCRGNCIDILSAIDNYDLHKHGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPELIYI
TDHKCHSTLHTICIIPNVMDIVISLTLDCDIILDIKYASIILNKHKLDEACIHILKEAISGNDIHYDKIN
ESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD
DLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHA
SQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAST
LDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTN
PYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGIV
NILLHYGAELRDSRVLHKSLNDNMFSFRYIIAHICIQDFIRHDIRNEVNPLKRVPTRFTSLRESFKEIIQ
SDDTFKRIWLRCKEELKDISKIRINMFYSLDIFIISKNMNLLHHLVNNPIIKEINTWHFCNYGDRLKTSI
SLASDRHEILEKSRSKLDEILDSSDWSKLPPDIKLSILEFIDNNELRKICNR
>gnl|CDD|222939 PHA02878, PHA02878, ankyrin repeat protein; Provisional
MDKLYKSMYTDNYETILKYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRD
LTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKS
KDDIIEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK
HYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSE
RKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDIKNSEGFIDNMDCITSN
KRLNQIKDKCEDELNRLASIKITNTYSFDDFLKCDNSTLLCKLVNNSIIDDILIDSFNIYGNIIKKNIYR
ARKRLLLIEGAIYSLDNIFFEKQNYMWNRLPLEIKHYIMELLDDASLCNMIEYEKHK
>gnl|CDD|222940 PHA02880, PHA02880, hypothetical protein; Provisional
MGNNSSMGSKKNNNSMIYSKKRTKLISKHHNYLMDVFDVLSDNGKVVMIDCMGHWLYNSWDYEPNLFLKS
LSDRSDIDSIYKERLVKNLEIINEYRNKFPRTVPDILSILKKIQDVISNNDIEIKKFNSVDYYEKENIIN
TIIDEFKKRGDFEPYLFLQTLERQYSQIEGNLRGKNDYFLNDAISYRKI
>gnl|CDD|165210 PHA02881, PHA02881, hypothetical protein; Provisional
MEAHEKCFSNIIAFLHDIDISMFSPNIIYSGLLDSYNFGFVDALLATNIDIGISKRRENLCAKCNNICIK
ENQFKLCLEFGYRDDKDCIKKGHMFIGFLNLDIIVHITALFPPCCNFMDAKVLNFNLLFPECDCFFIDAK
LNIAEEPNFNILQYLFVSPIQ
>gnl|CDD|165211 PHA02882, PHA02882, putative serine/threonine kinase; Provisional
MEGIPLIDITGKEWKIDKLIGCGGFGCVYETQCASDHCINNQAVAKIENLENETIVMETLVYNNIYDIDK
IALWKNIHNIDHLGIPKYYGCGSFKRCRMYYRFILLEKLVENTKEIFKRIKCKNKKLIKNIMKDMLTTLE
YIHEHGISHGDIKPENIMVDGNNRGYIIDYGIASHFIIHGKHIEYSKEQKDLHRGTLYYAGLDAHNGACV
TRRGDLESLGYCMLKWAGIKLPWKGFGHNGNLIHAAKCDFIKRLHEGKIKIKNANKFIYDFIECVTKLSY
EEKPDYDALIKIFD
>gnl|CDD|165212 PHA02884, PHA02884, ankyrin repeat protein; Provisional
MIIINLIDIITLLCRIFYIIFYIAIKKKNKICIANILYSSIKFHYTDIIDAILKLGADPEAPFPLSENSK
TNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTP
IELALMICNNFLAFMICDNEISNFYKHPKKILINFDILKILVSHFILQASNDRLNEKHNKNFNAGYNKNK
HLIIQSIILKQFKDLCIDDIDIMKNIKLGDDSNDMLSFFDILVENDLIKLLNNIDNIDILDIPKKLKVYN
NKIKLFLDEAIIYNNINEIL
>gnl|CDD|165213 PHA02885, PHA02885, putative interleukin binding protein; Provisional
KLFIVIILISILIIHGYMIDGNECPKDSNGCGIITASKDNSSSNSNFDRLLCSGCLNSEDGYIYWIGPNN
TSPGEYIFIENLEGANEGQDNTFALGDDCYKHTRELNISSADYTGKNFSCTSITESGTTFFNIIL
>gnl|CDD|165214 PHA02887, PHA02887, EGF-like protein; Provisional
MDELISPIEVKNEYKLIKNLLGKKFTLATSIIIVLLIFNIAFYGIRIHELAIIKRNFESHISKFNYKENA
NAQNFKRKNSMFFEKCKNDFNDFCINGECMNIIDLDEKFCICNKGYTGIRCDEVSI
>gnl|CDD|165215 PHA02888, PHA02888, hypothetical protein; Provisional
MISLPSSCQHIINRVINGECFFGKCENKKLAIKKAMTPQELAYIQEWLLEKHDLFIEFPIDLITMEHILM
HLASDVSTIKRKKSDINARRTHLKDV
>gnl|CDD|165216 PHA02889, PHA02889, hypothetical protein; Provisional
MNRSIIILVICSNINHSFPCKRSILDENGEANIIICPSTSIECIKWMYIEKKELKQHDFKTLGIFMFPDS
YHIKEPDELMNFTLDKITLKRWSKGDLYHISIGIKKKCMGKGQDSLQEIESIFIDDSLITKEDDFVKNLV
SETNSSEEYDNITNIIIEHTNNTTKNFFHNYKLYNLILIPICTLIIIIIVCYISCKHKTCFFKKKIDKID
DIEDFILIKLHPDKEPLFHDIDEIDVDSDDE
>gnl|CDD|165217 PHA02890, PHA02890, hypothetical protein; Provisional
MYKTINTSGISCVLKDLIPDKFDEEEDIDDGDLEKIKEFIEICINKCFSIKNISDITVLCIEPANTNKYS
ISTNHDKNEPHEENDIAMKKIECFFVACIEGSCKINVNIGDREISDHIHENQGFIMDVGLDHAIDSDNVG
LFITKFEVDAHIFYGQNVIIFPEENLFSQFNGPNFILYDITNQDFNLLLLITKDNIYNLCDDDVYDIFDL
KYLFDNCKLPMPLIPLSKYDFTFCDLNAIKSEDIESILRKVHACMESTHNEDTSLPLAIKVIYGTVII
>gnl|CDD|165218 PHA02891, PHA02891, hypothetical protein; Provisional
MDAINIMKDIKRGKDITPSMIKKFIELLDIEAAFNDPLPIKLGSKMITDKNIIYSEDHIKGMIQIFYGYI
PKIIKKKDFFNIISKLIIIPPDDALKRIFGDESEIDINIFAEKFLAELNR
>gnl|CDD|165219 PHA02892, PHA02892, hypothetical protein; Provisional
MDDINDYIDDINEDSINHMLSTLANVKDPEFSASISLMQEIIKIINSKIIEIDKKYKKNKPIINSMNNAS
SRISY
>gnl|CDD|165220 PHA02893, PHA02893, hypothetical protein; Provisional
DAASTAGAKKRKKKSRSATSTRKEEETAIPEDACTTCQICQSKLVMFSGVNKYKLKDYLNIGKAFSNSNI
KCIACGSSLCHLRDLSKS
>gnl|CDD|165221 PHA02894, PHA02894, hypothetical protein; Provisional
MYIENNSLVLIIPERINIIPQLFTIGDKKPICVCNRYSLIPSKKENVQISRIDDIHLYFKKFKNIYIVNP
RNHDIIKIFHFIKKNKWEGGFYLLFNV
>gnl|CDD|165222 PHA02896, PHA02896, A-type inclusion like protein; Provisional
MGRDGCGIDKCIRKFESLIIRTWDHDLNERSFLNRKDRKIIRNIFRCFIHYSCDNDLIHGIQAQLLYPKN
LDNHFLCEFIKYNNHGIKKLYNKIDMSNDRMPDISTKGRYILYFVMFLLYMGNNDTKFNYSDSGRNVSKK
ISEIVTDYLRLISSVHSRFKCKCMFIGLPTYYIHLMSADDIIMAMESVGDKPRNGPEEYERNSTIHIKEM
CAYQDFLNFIMASKKAKNKGLCIKLCGIPFETDYSISELIMDGLCYCFTDEVTIKKGHYDFVQLYTKCHI
GDSYEYIRLTDEFPSTKMSFSPNCDHDCSAIRIFKDKDNDFYQNRHMLFFPDDCRRWKWYLDDDKHPSYD
YSNDRERRPKDYKEYYIDNFECDKMKNCPSTNGTLNRDEDEDKIEEDNDDYNNDDEDDLIKDEAPILNRR
HGQMDDKYDKRDHRYKNNKYDIYDDESPRYKYKDDDYDDNDDNDDDHIIPKKANNLEDAKDFEDEMMDAI
ADDDYTPKSIRNRRNGYLLKDEDRYYYDRGHRNLGAEKDPEKPHPDKDEEYPEDKDKSDDDRLNDADKAM
RKLEADGFGDRYRKIKEKMDNLEDDYDDLRKHAIELPKKLDNQSGNGDRDEDKSWF
>gnl|CDD|165223 PHA02898, PHA02898, virion envelope protein; Provisional
MDPIGFFKNRPSYVVAFGIILLIVACICAYIELSKSEKPADSALRSISIISFILAIILILGIIFFKGYNM
FCGGNTTDEVSRYANSNDIEIQ
>gnl|CDD|222941 PHA02901, PHA02901, virus redox protein; Provisional
MSWYSKYNIVLDPPKRCSKCSDNLVEYLKEDRETIRAILESQPYKKKILKQFLATSRNKTFLYKILDPEI
RRVLT
>gnl|CDD|165225 PHA02902, PHA02902, putative IMV membrane protein; Provisional
GAIDTFVILAVIVIIFCLLIYAAYKRYKCIPSPDDRDERFGDTLEDDPLFKDSLTPDQIKALHRLVSLSI
>gnl|CDD|165226 PHA02907, PHA02907, hypothetical protein; Provisional
MNPRNSPEKYSPHKNSVSKMRPESSFNVSLYDASRIRASKHYPHTRFPNEDWTPKGILLRKYGKTKQSGN
TKDVLEKSPDSVSPRELPIEKSYYKSIVYKTAAVMLLVVKIRDRLRFIRKLFRYVGDKLYAKAALTLVNR
LVTPRIPVVKDLIPFYYAKKNFWKFALLYGLKKISDKAPKAR
>gnl|CDD|165227 PHA02909, PHA02909, hypothetical protein; Provisional
MDSKKQNPDPNYLMLSVDYGNGKKVYYTENTFCIMVSFILFVIIFLSMFTILACSYVYIAIIISLILLFF
GC
>gnl|CDD|165228 PHA02910, PHA02910, hypothetical protein; Provisional
MDKIPLIEKQNNSYNTRISTVRKISITSICVSLFLIGIIGGYIVGFYTTVSFNSNSGGEKRIGYHSWFCH
YGACYKEVLMPPSNYSHSKYVCEKLMNSKLPTRYDTIVMGLFSPIKNLENIWLTAEDGNDGIVNCSSVSY
TQSSYYHNVTTIPCNSKIATVCMVKPIYNIA
>gnl|CDD|177496 PHA02911, PHA02911, C-type lectin-like protein; Provisional
MEMLGPIEVLEEKMKFFADASSIYQKEKLALIIACLCLILTIIIICLFAALFKAVRDCKDDSEVVFIEDS
SPAITPEPSIATTCPDNLTIHCPEVPSPSEPICSRDWINHMGICLLSLGEEVGFRMEIAKRFCEKKDADL
IGKIDEEKKALENIWTGNDHSRFWIDNRAAASTFDPVNECAIGTQNHIPEVPEVLKSPCDERHSFICIKK
DND
>gnl|CDD|177497 PHA02913, PHA02913, TGF-beta-like protein; Provisional
DLILFKLNFINIIFLPHFDIFNCIDIINLENEASNIFGDDIIDFYELIIENQKFSINHESELLPRHKMDF
CDIDAICCIRDFNIDFKADMGMKWILKPEGTHANLCIGICSISNHKKINLMYGTAFKHHMPDNTIPFCCA
PIKMKNFIIAYKEGRKIKTDNIKNFKILECAC
>gnl|CDD|165230 PHA02914, PHA02914, Immunoglobulin-like domain protein; Provisional
KNILASLIIFAVCCASESYNIFLRNEDEELALTCILPAAKMADKVVLIKGNDMNNTKEIESSINNAGEDN
VCYCGDPDKEYSFIEENIGEHEDGDFKCIFYLGDNESHKHEILVRKAPKIDTTFLEFNDKHTCICCKIDK
PMNQDALKVFFVAGGVNVDGNFLGKKDFNNDPSNRTVKLCADKSHDDTAREALCGVEYFGALKELNISYD
GTNAVNISEILSKVCPENVINSKVCGDNGSKDSELLEDEEEEDDYEESGDYSEVTYDKKKFDEVMLEVGK
RVDIECFFSMCGNENISNAKWIDTGFEIGPLIGTVKSKDIVEGDFAEDDDFMISAHANYSDDLKNSTLTI
KKAHINNAGCYEAQAFMGKFKEECRHCFKVADHVFFKWNTEGDNETKVACYAAQYDMQPFSILWKSNGVS
FGGEIADALDEHEGAICDGCEASEIIIMDKRDKDTVKKLSCINITGQGYAIEYPIDFEGTKEHKFHKLEH
QEARILKNLV
>gnl|CDD|165231 PHA02917, PHA02917, ankyrin-like protein; Provisional
MFDYLENEEVALDELKQMLRDRDPNDTRNQFKNNALHAYLFNEHCNNVEVVKLLLDSGTNPLHKNWRQLT
PLEEYTNSRHVKVNKDIAMALLEATGYSNINDFNIFSYMKSKNVDVDLIKVLVEHGFDLSVKCENHRSVI
ENYVMTDDPVPEIIDLFIENGCSVLYEDEDDEYGYAYDDYQPRNCGTVLHLYIISHLYSESDTRAYVRPE
VVKCLINHGIKPSSIDKNYCTALQYYIKSSHIDIDIVKLLMKGIDNTAYSYIDDLTCCTRGIMADYLNSD
YRYNKDVDLDLVKLFLENGKPHGIMCSIVPLWRNDKETISLILKTMNSDVLQHILIEYMTFGDIDIPLVE
CMLEYGAVVNKEAIHGYFRNINIDSYTMKYLLKKEGGDAVNHLDDGEIPIGHLCKSNYGCYNFYTYTYKK
GLCDMSYACPILSTINICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIA
IAINESRNIELLKMLLCHKPTLDCVIDSLREISNIVDNAYAIKQCIKYAMIIDDCTSSKIPESISQRYND
YIDLCNQELNEMKKIMVGGNTMFSLIFTDHGAKIIHRYANNPELRAYYESKQNKIYVEAYDIISNAIVKH
NKIHKNIESVDDNTYISNLPYTIKYKIFEQQ
>gnl|CDD|165232 PHA02919, PHA02919, host-range protein; Provisional
MGIQHEFDIIINGDIALRNLQLHRGDNYGCKLKIISNDYKKLKFRFIIRPDWSEIDEVKGLTVFANNYAV
KVNKVDDTFYYVIYEAVIHLYNKKTEILIYSDDENELFKHYYPYISLNMISKKYKVKEENYSSPYIEHPL
IPYRDYESMD
>gnl|CDD|165233 PHA02920, PHA02920, putative virulence factor; Provisional
MRTLLIRYILWRNDGDPSYYNDDFKKLMLLDELVDDGDVCTLIKNMRMTLSDGPLLDRLNQPVNNVEDVK
RMIAISAKVARDIGERSEIRWEESFTILFRMIEKYFDDLMIDLYGEK
>gnl|CDD|165234 PHA02922, PHA02922, hypothetical protein; Provisional
MASPCAQFSPCHCHATKDSLNTVADVRHCLTEYILWVSHRWTHRESAGSLYRLLISFRTDATELFGSELK
EFSDSLPWDNIDNCVEIIKCFIRNDSMKTAKELRAIIGLCTQSAIVSGRVFNDKYIDILLMLRKILNEND
YLTLLDHIRTAKY
>gnl|CDD|165235 PHA02923, PHA02923, hypothetical protein; Provisional
MDTIKIFNHGEFDTIRNDLVNLLKVVKWNTINSNVTVSSTDTIDISECIREILYKQFKNVRNIEVSSTIS
FIKYNPFNDTTLTDDNMGYYLVIYLNRPKSGKTLIYPTPETVITSSEDIMFSKSLNFRFENVKRGYKLVM
CSISLSYKPSITRIQYDNDKYIDISDSQEGNNLCYCVITIDPHHLIDLETICVLVNRSGKCLLVNEHLGR
FRKKHIYDSFGDVCMDHIFELPETRELFTLTNDDGRNIAWDNDKLESDNDIWIPKTDDEYKFLSKLMNIA
KFNNTKFDYYVLVGDTDPCTVFTFKVTKYYINMNY
>gnl|CDD|222942 PHA02924, PHA02924, hypothetical protein; Provisional
MNAYNKADSFSLESDSIKDVIHDYICWLSMTDEMRPSIGNVFKAMETFKIDAVRYYDGNIYDLAKDINAM
SFDSFIRSLQNIASKKDKLTVYGTMGLLSIVVDINKGCDISNIKFAAGIIILMEYIFDDTDMSHLKVALY
RRIQRRYPIDDDEEDR
>gnl|CDD|165237 PHA02926, PHA02926, zinc finger-like protein; Provisional
MEFDPTKINISSIDHVTILQYIDEPNDIRLTVCIIQNINNITYYINITKINPHLANQFRAWKKRIAGRDY
MTNLSRDTGIQQSKLTETIRNCQKNRNIYGLYIHYNLVINVVIDWITDVIVQSILRGLVNWYIANNTYTP
NTPNNTTTISELDIIKILDKYEDVYRVSKEKECGICYEVVYSKRLENDRYFGLLDSCNHIFCITCINIWH
RTRRETGASDNCPICRTRFRNITMSKFYKLVN
>gnl|CDD|222943 PHA02927, PHA02927, secreted complement-binding protein; Provisional
MKVESVTFLTLLGIGCVLSCCTIPSRPINMKFKNSVETDANANYNIGDTIEYLCLPGYRKQKMGPIYAKC
TGTGWTLFNQCIKRRCPSPRDIDNGQLDIGGVDFGSSITYSCNSGYQLIGESKSYCELGSTGSMVWNPEA
PICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCSGGEWSDPPTCQIVKCPHPT
ISNGYLSSGFKRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKCVR
>gnl|CDD|165239 PHA02928, PHA02928, Hypothetical protein; Provisional
MIMSTDPNNILMRHLKNLTDDEFKCIIHRSSDFLYLSDRDYTSITKETLVSEIVEEYPDDCNKILAIIFL
VLDKDIDVDIETKLKLKPKPAVRFAILDKMTADIKLTDLVRHYFRYIEQDIPLGPLFKKIDSYRIRAINK
YSKELGLATEYFNKYGHLMFYTLPIPYNRFFCRNSIGFLAVLSPTIGHVKAFYKFIEYVSIDDRRKFKKE
LMSK
>gnl|CDD|222944 PHA02929, PHA02929, N1R/p28-like protein; Provisional
MDDSYDRNNFILLNGECIKIIILSSNNYINITKLCKPMKKSFCNWKNLKRSRQIIINISIEENIKVDKLS
FRIYKSKYTKQIHGVFIHPKLLKYVLNWISEEYCAKVLSIINEYNQKILKNKPSNDKINYIYMRKEEDMF
YAIINKKGKNYKKFLKTIPSVLSEYEKLYNRSKDKECAICMEKVYDKEIKNMYFGILSNCNHVFCIECID
IWKKEKNTCPVCRTPFISVIKSRFFTKG
>gnl|CDD|165241 PHA02930, PHA02930, hypothetical protein; Provisional
MTLVMGSCCGRFCDANKNKNKKEDVEEGGEGCYDYKNLNDLDEFETRVEFGPLYMINEEKSDINTLDIKR
RYRHAIESVYF
>gnl|CDD|165242 PHA02931, PHA02931, hypothetical protein; Provisional
MSKILTFVKNKIIDLINNDQIKYSRVIMIEESDSLLPVDEVHANHGFDCVEMIDENIINENLEQYKTDSF
FT
>gnl|CDD|222945 PHA02932, PHA02932, hypothetical protein; Provisional
LFVYILILLFCSASLSYSLEYKNTICRQDYRYWNLAAELTIGLNYDINETIIGECHMSESYIDRNSTIVL
TGYGLEINITITDIDQRFVAAAEGVGKNNKLSILLFTTQDLSKYHHNIKVTITCLEMDCDTTKYRQDLPE
SIHKNSSCEITINGSCVTCVNLETYPNKINPHYFHPKSKIVYRNYSYGTRGSYGVTFIDELNQCLLDIKK
VSYDICYRESR
>gnl|CDD|165244 PHA02933, PHA02933, unchracterized protein; Provisional
MATKSDYEDAVFYFVDDDEICSRDSIIDLIDEYITWRNHVIVFNKDITSCGRLYKELMKFDDVAIRYYGI
DKINEIVEAMSEGDHYINLTEVHDQESLFATIGICAKITEHWGYKKISESRFQSLGNITDLMTDDNINIL
ILFLEKKLN
>gnl|CDD|165245 PHA02934, PHA02934, Hypothetical protein; Provisional
MDNSMLSMFMCNNIVDYVDDIDDIDDIDDIDDIDDIDDIDNVQDIDNGIVQDIEDEASNNDDHNYVYPLP
ENMVYRFDKSTNILDYLSTERDHVMMAVQYYMSKQRLDDLYRQLPTKTRSYIDIINMYCDKVNNDYNRDM
NIMYDMASTESFTVYDINNEVNTILMDNKGLGVRLATISFITELGRRCMNPVETIKMFTLLSHTICDDCF
VDYITDISPPDNTIPNTSTREYLKLIGITAIMFATYKTLKYMI
>gnl|CDD|222946 PHA02935, PHA02935, Hypothetical protein; Provisional
MRISNSIKPILFYNKLKSKHLLSRIKMGTNVIRAFIILYLLAVCGCVEYDVDNNVQICTHAVVSHINYTS
WYYNDKVIALATEDRTSGYISSFIKRVNISLTCLNISSLRYEDSGSYKGVSHLKDGVIVTTTMNISVKAN
IIDLTGRVRYLTRNYCEVKIRCEIKSFALNGSITPLHMILGTLDRWKYLPFPTDDYRYVGELKRYISGNP
YPTESLALEISSTFNRFTIVKNLNDDEFSCYLFSQNYSFHKMLNARHICESEWEALNNNNDNSSSMPASH
NNLANDLSSMMSQLQNDNDDNNDYSAPMNVDNLIMIVLITMLSIIIIIIVVIAAIAMYKRSKYSHIDDN
>gnl|CDD|165247 PHA02937, PHA02937, hypothetical protein; Provisional
MAQTLIQTPKKKGGKIEKQYIKLYKLLKQVKEEVEQLLLSKANKTKDLQEYLDYNVNYVKNLIRVYMKDL
RDYLKEDFCNFCDWIEPDRHLVYLARIHAGLKIYAMLTGKDINKVMPKLTELEIEGYKTATLIYILVDNK
NKDRINIIQKIIKENAKIKVNNALEILSTIETKIMIEFRLVKDETIKMLLNVLLELAKILMKELQNFREE
KIEITSANDIILFLKKISQLLEDSALFTHLANLIDEIDEDVHEKLSIQYLADQAYESLLLILEDLRGDKI
ERYERVIEICAEEMLGKIYAIECPRLNEYQ
>gnl|CDD|165248 PHA02938, PHA02938, hypothetical protein; Provisional
MAYLEFIIPNSLLDKVKEEAERLNVKRKLLIKAAIIAFAENPPETIKPLPDLNYGFSKKDLIRVYLSLPK
DIIEKIRSYASSKGLSIRRVAESAVDDFLTLSDEQKKIYIDKEKRRLSEKRKRKLDEERLTQLLEAIASK
DPSAPVSASFKCVDDLHKLLEKEAIKRGTTASELVRRAIEEFLKKYGNNYEEIKKLYETAKDLFYEKGPW
KGRALKLPAYMLLQLTKIAEQTSVPRSALIRLAIMKYLNLLDKSPIKQQKVTRNEVFNCAASLPPMLEEP
QKKNNTALEAIIREAVKQLLQHSIDEIRELSREKPPDSETYVVSVKLPESLKTQLDPIAEKGRTVKKQLI
RTALAVYFRLV
>gnl|CDD|222947 PHA02939, PHA02939, hypothetical protein; Provisional
MAEPVTQTPNSGVNEQDIQLITKKLAYIAIQFQKILERMIFSDFARCDDEGCPRSKWESDFLRDLIPEEI
WYVRKAVKELYDPESTDDQREYAEHRLKGLLELLERNFNQLLEFCIDEKRREKYLKLIEEFNKVKEMIEK
TVLS
>gnl|CDD|165250 PHA02940, PHA02940, hypothetical protein; Provisional
TSQANQDKLIELKEKIGEYIKDLEDLKLDYDINDFDADDLRAELEYIQKEIVESYSITKSVKEAIELTYS
ILTDYYNDAKEKSKLLSDAYNKNAIKSMFDNAIELYANLAAINALLRLIRSFIKPEPTLTTPLFIDFTQK
AKDTVILLAGRYVQDVKKDDRRTIANKLSKELSWTIDYQENEPDLESDFKEIEEELEEKDDLSRGTYKVL
KRALDLMKEHYWKGIRLANEAKAMIKRDAYDADEEEYKPKNVDMRKIAWNLTETYATFTALQALYDILCN
DKYDVCYKWFNYILLFALEDAKDAIEVIREHYLRD
>gnl|CDD|222948 PHA02941, PHA02941, hypothetical protein; Provisional
MAMQPWEYVYDLLMPAKAPTDQKTFTKYIYLALAVPLTKEFEEKISKGDTKDLELPVYPVAFNTRPDRNK
WDRIATIKDLLTRSGLYDNDYDFVTPIKYLDFKSSFVPGYFPLAVLELHFERDITANPEDYGLKPIDGYK
WELDRDGSYKVTSGSLFNVREAKNSDRYSVLFLDDNPKEFNMLNGYGVVRFYIDLWNAPEEVYAKAKEEC
ESAGGIYQYDYPEGVAYCVLPLNKEANIKASEFILQLYEMIKSKITSEDFLKHVMVYQLKNEMVYQFPGP
KQIPVKPVIGKTFQEMVKVAAKDLILGGEEKEPKQESQEQLFNPFAIDEEMLEETQEQQEEEENEEEEEN
DTVKLS
>gnl|CDD|165252 PHA02942, PHA02942, putative transposase; Provisional
MARREKNPIRATVAMKIGLSDSLLAFVNNYVKALRFSIFWMKENVKNPNEKGALSKVHEGLYEKLKEDYN
LPPKVSADCYRDALAIYKSWYNNPKKGRFPRVYKPTVWLTPKQSYTVDLDKMTVKIASVGELPILGYPRN
LKEYANWDMKEARLTIKDGKAFLKVTFEKEEEKIKPKDSVAVDINMNDIVVGKDDSHYVRIPTRLHDAHH
FKSLAENLQKKYPRRWKENKRILHRARSFHHKAKLIMEDFARKVGKWVVEIAEDLGANVIKLEDLKNLIK
DVNKLPAEFRDKLYLMQYHRIQYWIEWQAKKHGMIVEFVNPSYSSVSCPKCGHKMVEIAHRYFHCPSCGY
ENDRDVIAIMNLNGRGSLTLSTAPQMRDVAPNR
>gnl|CDD|165253 PHA02943, PHA02943, hypothetical protein; Provisional
MPRGMSDTVHTRMIKTLRLLADGCKTTSRIANKLGVSHSMARNALYQLAKEGMVLKVEIGRAAIWCLDED
AYTNLVFEIKRELWRLVCNSRLKFITPSRLLRLIAKDTEAHNIFAKYVPVNSRHAHILSFLNSALEMLYG
EPYDKRQRTVYFHVTPRFCKKAPTL
>gnl|CDD|165254 PHA02944, PHA02944, hypothetical protein; Provisional
MASKIKPEEFPEKEATFLELKAGGAETEYRAVIEDLEAGGITMGGEDDVKEVLRRIAQAKADLPEDVIKA
AIESVAEHILSASELGLKDAGGGLGTEFGDGDKLAIMIKLQHLIDNERDERGWAGEIKAMFIGYDGLFAD
SKHTVIKRVEFYAGEDIDAAQLYNELIEAARHAYNAIGSA
>gnl|CDD|165255 PHA02945, PHA02945, interferon resistance protein; Provisional
MLAFCYSLPNVGDVLKGKVYENGYALYIDLFDYPHSEAILAESVQMHMNRYFKYRDKLVGKTVKVKVIRV
DYTKGYIDVNYKRMCRHQ
>gnl|CDD|165256 PHA02946, PHA02946, ankyin-like protein; Provisional
MDNIMSAEYYLSLYAKYNSKNLDVFRNMLQAIEPSGNYHILHAYCGIKGLDERFVEELLHRGYSPNETDD
DGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLVQYGAKINNSVDEE
GCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNT
PLHIVCSKTVKNVDIINLLLPSTDVNKQNKFGDSPLTLLIKTLSPAHLINKLLSTSNVITDQTVNICIFY
DRDDVLEIINDKGKQYDSTDFKMAVEVGSIRCVKYLLDNDIICEDAMYYAVLSEYETMVDYLLFNHFSVD
SVVNGHTCMSECVRLNNPVILSKLMLHNPTSETMYLTMKAIEKDKLDKSIIIPFIAYFVLMHPDFCKNRR
YFTSYKRFVTDYVHEGVSYEVFDDYF
>gnl|CDD|222949 PHA02947, PHA02947, S-S bond formation pathway protein; Provisional
MEETKQVNTLYNLFIERYLQNLSLYSVPTNTTCGIHIGEIKGQFKRCKLRIINKCLNNKRLSFTLLIKTF
KEVISTLPEKERRELANEIGIDLDNDDPSYVSELERNCNASADVNNIIDIQKFDIGECIAPEGKHILLQI
VNSGSAEANCGLNTIVKSLNKRYVPDPIIENRLPYSNKPWFIVGVVIILIIFVIAICSIKRKINLKYRYG
SFLYV
>gnl|CDD|165258 PHA02948, PHA02948, serine protease inhibitor-like protein; Provisional
MIALLILSLACTASAYRLQGFTNAGILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKT
MDLRKRDLGPAFTELISGLAKLKTSKYTYTDLTYQSFVDNTVCIKPSYYQQYHRFGLYRLNFRRDAVNKI
NSIVERRSGMSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTHNASFTNKYGTKTVPMMNVVTKLQ
GNTITIDDEEYDMVRLPYKDANISMYLAIGDNMTHFTDSITAAKLDYWSSQLGNKVYNLKLPRFSIENKR
DIKSIAEMMAPSMFNPDNASFKHMTRDPLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEFNT
PFVFIIRHDITGFILFMGKVESP
>gnl|CDD|165259 PHA02949, PHA02949, Hypothetical protein; Provisional
MEGSKRKHDSRRPQQEQEQHRPRTPPSYEEIAKYGHSFNVKRFTNEEMCLKNDYPRIISYNPPPK
>gnl|CDD|177499 PHA02951, PHA02951, Hypothetical protein; Provisional
SSILARRPTPKKMNYITKLENRLKKNSYIENTNQGNILMDSIFVSTMPIETLFGSYITDDSDDYELKDLL
NVTYSIKPVNVPDIKLDAVLDRDGNFRPADCFLVKLKHGNGFTKGALYLGHSAGFTATICLKNEGISGLY
IPGTSVLKINICQGDTIVSRSSRGVQFLPQIGGEAIYLVVSLCPTKKLVETGFVIPTISSNDNAKIAARI
ISERRLKIIAHIDTIIKYRQQLEKAYYNSCMLTEFLHIYDSYADTIKENLLKYTIQKDINIKHTNITTLW
NETTKLIKEIKSLLDKNHEDYDIINNYIIKEIKNCEGVKNRDEIVNNLSLSNLGFYL
>gnl|CDD|222950 PHA02952, PHA02952, EEV maturation protein; Provisional
MLLLVKLLLKRQNNLEEIRSALNKYPHSIILARTRDGKGVIIYADNLDLVKSMINLSSLEVVGITKYVEP
RPPPSKPISRLFIDEIDTDTYYSPKTSISPLLDILKKRAEELDDLAAALEKLGPEGNVSISEINYWLSDN
GLADYRFVNYKDVRKRYKKRNKYTLIDDMIIGYIGHHYIWVKDVEAYTRPEIDILPYDIKSIASKENWAP
LSISLEQLLKIIAISVNATITDTGPSPYMISTYPGKCFINFDSKKLILDFLKWLKEVMTNTSTIILVGYL
SSFFDFPLLKAYWPKDSGWTFIGNDYLVSKDGLRVILVDAAKFSCGLSLSDYCKHWGGKKVSRPKDLITK
AEAKRKIKALEKAASESAYYLYDAVNAQSAALNRLFSPCDMFSFSRLEDMFLTKAIHRAAENVNNNMYYP
SHPDAVNFIEQSIRLDYVKTVNVDAPKDSRKYRLKSVLDIIASGLYPVGKPYYVKTLTEGKLYIALCKVT
VKPDVKIPVLFDDDDESTLTFITVLTSVDIETAVRLGGYKIKELGALEWEDSIPVLKDGLEATIDAIREL
NIATTDNLLSRLANNPLLNNSLEIRSGRNSLFYAFAASYCRAAIHSLIERIDSHYLGEFVLKHNYKEIYV
RDSVKKDKEFLSEMIKLL
>gnl|CDD|165262 PHA02953, PHA02953, IEV and EEV membrane glycoprotein; Provisional
MKSLNRQTVNKIKKLSTPAAIFMILSTIVSGIGTVLKYKDELFPSACAKGWIPYDNYCYLDTNIQLSTYG
AVYLCNKYRARLPKPNFRHLKVLSLTYGKDFWVSLKKKNNRWLDINTNKTVDMNKNTELKKIKSKTKNDN
EACYIYKSGELKETVCNSVNYIICVKRFYK
>gnl|CDD|165263 PHA02954, PHA02954, EEV membrane glycoprotein; Provisional
MKTISVVTLLCVLPAVVYSTCTVPTMNNAKLTSTETSFNDKQKVTFTCDSGYYSLDPNAVCETDKWKYEN
PCKKMCTVSDYVSELYDKPLYEVNSTITLICKDETKYFRCEEKNGNTSWNDTVTCPNAECQPLQLEHGSC
QPVKEKYSFGEHITINCDVGYEVIGASYISCTANSWNVIPSCQQKCDIPSLSNGLISGSTFSIGGVIHLS
CKSGFTLTGSPSSTCIDGKWNPVLPICVRSNEEFDPVDDGPDDETDLSKLSKDVVQYEQEIESLEATYHI
IIVALTIMGVIFLISVIVLVCSCNKNNDQYKFHKLLP
>gnl|CDD|165264 PHA02955, PHA02955, hypothetical protein; Provisional
MENNQVISNLYYLFSEKYLEKLNKHPDTSNINCGIHIGRISGEAKNCIISIINACNSDEEKNFQLLIEAL
IETIENFPEKEQKEIAADIGINIDDYKAGKKTDLQLHCEAYANLTQHIDIQHFNIGTCYSPNDKYTDIKI
INTGSAISNCGVEIILNKIKRNNKIVPIDNKLSMDSFSIKWFIIYIVLCLLILIILGYIYRTVRIKYIYG
VYI
>gnl|CDD|165265 PHA02956, PHA02956, hypothetical protein; Provisional
MAICINPESTACVHSLDAEEACYKWLPIKNKYLPDYALIRFMIKKFNKLFIAKGLNIFAKYSWINFIEAA
ICIGEHRPWIMSFIHTISGKNIADFRLDRAYPDSRMNSIIIDSSSGKIICEGIGIIDKLRLHGIDFIKDK
LFSEDEIINHLVGVQKLKDICIKMINKTVKKDDCDKLELPRSLLKEIKK
>gnl|CDD|165266 PHA02957, PHA02957, hypothetical protein; Provisional
MIFFSVYKYNTNYAFKIIFLAILLIIPLELLLICHTCITASKLSREDNEIDDVPTCPRKMFNKKKGMGPI
VNMKAPDGDPTAPIMALDAWHKNTSCKYNDYCTFFDFCFAGATNIRFGKQKIELIYFFFIEAVTRDDYTK
ITQEITLKHLDDLRFKPLSVSFAALNKDFVKIPASHECMKGGFKKPVKDKCKADSKSAIDVCGEQG
>gnl|CDD|165267 PHA02961, PHA02961, hypothetical protein; Provisional
MAGLYPKDLRKSINEFIKSGLDFDLLHEKHAHRLIINNIFSKLPDKYYDFAKGLDINNILAFDHEIIELN
DLKKLIMKLPHIPDCFTDIIACHKKYLLLDAAIVFKLIESNIINLSDIRNIIDNRIKTPIEIALINSDLI
IPGTHFSLDDIKTIFDNKGADNTKELYKKIDTPIHNILLMEEKFSIPPIHSSIYQLMDIDKAIFLIKKYP
DDDIIDNINGIVKSHKDFIESIIDIIKDKLPDILPCINKWIATQLCPDKLLAEFGIYFYALFDWIDIPLY
IDKYLFLNITEDETKFICKHIDIYKKKSELFVNAFRWHLYYCDNMHPQKIFDPITCKKDKHEKYMIKESF
EYLDNEANIAILLNDFKYNYAIGKYILDSKASEELKLDAFKILQKQGTCIDNAKCFDLGALYSAIIKFPY
HPVDYVMHSDKCIDYMCDMSEFDNNISDIGLGKLASFLCNAAKKGIIDINFLKTNCLWSPLMYLIDDSCK
VDFSRFMMATKNIKADNIKYLKKKDENIDINFEHIDDIDIYKLLDYDRIHLYGINFIKKIIFANTIFEYI
FTLIIIRFKKSSYNFRRFIELLIYKCLKGFEIPPDLYKDVYVNEMNICCELENLINDSIIPFITHGIIIK
LLINIFNNLNGIGKHSFRIRIRKGKILI
>gnl|CDD|165268 PHA02962, PHA02962, hypothetical protein; Provisional
MFDINKLIDIYEDNDYVPGDYKHSQLQKAFLELPIIDIIDLIKLDFYPQCLPKKFYKAIAAFCVDKIYLF
KPEYIQLKDLFLVIDLFDDLSKYKEIILYYKYEILKSNNYQIIKKCKDIIGIHEDDNDNDIIEDISDKDL
MDKMIEFPGFMKIVYKKKILSIRILKEMYYKHKILPINKGITFIKEDDICFFIDALEDADDDDDTLYLIL
ECNDKILDSDEVKDAIIRKICKGENIDVLGYYVKHYFIDHAKLGIYYNIFFAERDIISEYGLKDDSLAII
CKYIDKYSKSIPSIAKLLIDNSNYSLLASIIDRIPDDMHNENLYMNIIRHSNDKKPKIKNFKADFFSECL
MVMCYLRGYEDIVDFLIALDVESIIKNRINPFNDYTFTTDWFNKNTELLKLYISFYFIDPTMMRKLLFEY
PLCEESTRIAIEEIKKARSFLSIKDNYNIDFHEEFDIIDLPRSFNIPIKEIADLKEFNNIIPFISDKSYK
FKIASQLLKYNILKSIKVENLCYHHIKNLHSFCFNITKESSISPGAIDNISRLIDQIGDIGRLFRHGFIS
FNDNHFGKWIPSLNSSKILDHFQYNGPDYILSWQIDKIDFKAFVKYKDFPIFFLKKYNIDFLLDKETLLY
SCIYSCILLYILVGSVIYTEQENIYYFISNIINSFIKGIGIDNAFDLELEDVVKEIIIIQKLPEGKRKLS
LIKPVNLLDLCKRICAFISNDG
>gnl|CDD|165269 PHA02963, PHA02963, hypothetical protein; Provisional
MFKNYKYQLLKDDDNEEEILIPGLEDDDEAGTIENIGFKDIKTKMFEDQVKDIVKKNYKNNYKNLLLLLE
KSNNDCNELELLYKIINIDPRICHRFNINRYDNIFGLFNKLHEFISKKKIKIFCDGNCISIMFIRDNTSL
EIDIDCDAEGQLMDIDYKIEFGDVIILQIGGIEIIFIDKFIILKDIIFIFCDDNKIVSNEDDFLLEIENT
>gnl|CDD|165270 PHA02965, PHA02965, hypothetical protein; Provisional
MDINNKQELADHDSGEESPAKLPILDINDEEDTANTTNTASFNELPFNFSDNPYYKLTKSDDEKININLL
VGCNIIKIHDIKGLLDDVNKLIPKTPSKTNLSGCIKIPIDDIKIDCLDDGNKYFEVKDIKILQLAHGNDL
MNIDKYDDGFFDFIAVICIKNSGRSMIMLKHCNGKQHSMQDGFCLIARSFYGINILPQIIGESRYLILKL
SPSDKFKDRWPEIFDSNKDKDKKFYIQDLKEDACIEKAKNMEKDIYKNIEAFIINSILLEDLKSRLDITK
ELNANIDKIFHHNNNTLFSDIIKLSEDIIDKDFKNMEIMSDILLADLKQISKTKNKIRDRLLKAAINSKD
VEEILCDIPSIEEGTIEQFKFNQRAIYDHYKKIIEDNNKRLDLGCMNIEHNYMANLYKVYGQNEYMITYI
LALINRIKKGMDAIKSNLGDIDEFNIDNINLIISERIKKNISGESL
>gnl|CDD|165271 PHA02966, PHA02966, hypothetical protein; Provisional
MADRGVKSNNINLAKKKIKKVRIKQPDPTTEEIDTFGADINIKLIQPNISIDQDDGEGQAIHIDDFK
>gnl|CDD|165272 PHA02967, PHA02967, hypothetical protein; Provisional
DDKNINFSPVFIEPRFKHEFLLSPNKYFYILVFEVIVALIIINFFFKEEILYAFFPLAKPPKNSINSLLD
KTFLKCEEDGSLMISRPSGIYPALNLDGNPIQISDCSLLLSSINGADRSTSPYSIFNR
>gnl|CDD|165273 PHA02968, PHA02968, hypothetical protein; Provisional
MISTKTFILDKKYSLDKFLIDEDNIRKERFIFDKFLSKFGNIIDIKLLNGIIGEKYTTISFKLDKFCLLI
LVLDLPYINDKIKIKVGIDNLKLCLKRLNANSYIVINNSEASNHIDITCISDEHIKINNNEEELQDLSLG
KNNKFKILICFFDREHINYKPIEQGNKKALIVGCGFIIGEWIIEKKKTEIIDDNIERITKKCITSEYYID
ENNHKVIDDSSIGASDICNPIKHSKIKISDILKRKDKSLIQALRWPLGKPSIIFFKLWFIGEYGRCNINL
DSIVRILKRITGKKITNNCGLGDILISAFGIVRKQANKLGIDCKRISFRNFWKDIALIQLIRYNKLKKRS
LLDKFKKQNAKLISPDIPDINDYKYLPFNPWMLDISKEVELWDDLKLNILDKEKWSNDWPALSR
>gnl|CDD|165274 PHA02969, PHA02969, hypothetical protein; Provisional
MSNVCIHFILNDYSDDDYKKIKSIDCHHIIIDKESDDSHKIISGYIELKDGALCSIIENINPNIIYEILK
DNCDFDIIKKKNIVDSFKSKGCYEEYKKPALIDLRIFDYYK
>gnl|CDD|222951 PHA02970, PHA02970, hypothetical protein; Provisional
NNIVEVNSVLNYDGISPCYFGKCSSDLVHDLSEYEVYNPKEINSLYISFLKHHNLLSIDDRKLNDDAIDH
IIYHFIEYLQKLKNTILTRNNICKRILNKDTGKGSKTRPSDYVFL
>gnl|CDD|165276 PHA02972, PHA02972, hypothetical protein; Provisional
MIDLPSILLMTSITLAIISSFIAVIMNNINIILAAIFIITLIVIHIRIAFNILFLYIFSCIFDINIIIII
FLGIIFIRKTGKFIINYIREVREINKKIKRRSLIILDKE
>gnl|CDD|165277 PHA02973, PHA02973, hypothetical protein; Provisional
MLFLIFFFILFLLLCYFFNFKRTNKMDIGINPIKKIPWSDNDHIFVSSLFHNKDKYLTGPMKLNYDPDKK
GAVIDFKGTKYTYDLDDFADARKLIPTLLLSK
>gnl|CDD|165278 PHA02974, PHA02974, putative IMV membrane protein; Provisional
MEIARETLIFIGITILVVLLIISGFSLILRLIPGVYSSVIRSSFTAGKILRFMEIFSTIMFIPGIIILYA
AYIRKIKMKNN
>gnl|CDD|165279 PHA02975, PHA02975, hypothetical protein; Provisional
MEKLFTGTYGVFLESNDSDFEDFIDTIMHVLTGKKEPKKKSSLSIILIIFIIFITCIAVFTFLYLKLMC
>gnl|CDD|165280 PHA02976, PHA02976, hypothetical protein; Provisional
MVIIREISDPEAASCFNDVTPIGNGMSFLQVNGTRPTPEDILKAFDDDTKCKFLRSCIIFNIFIGCFHDD
IEYSSGCFQYITRDEFLNMTDGSYEEEFYIEKLNSPLDEFCLAIAPLVINEDDIEHLNDDEKCKNVNDEE
MFKPTYDNYNDGRDYRSYEPENLIKCLNINDIREIKKIIIY
>gnl|CDD|165281 PHA02977, PHA02977, hypothetical protein; Provisional
AAGILCELEHILAKEKNNKKDAILMGLDVEVPWDYCNWASINFYDIRLDKDISDLENIAIKYMTGCDIFP
HITLGIANKDQCDNFENFKELIKDIDLQSISFTCKEEICFPQSNASKELGAKGCAVVMKLEASDDLKALR
NVLFNAVPCPKDIFGDILSDNPWCPHITIGYVKADDEDNKKRFIECAEAFRGQEIKVLGWY
>gnl|CDD|165282 PHA02978, PHA02978, hypothetical protein; Provisional
MDIIIEELEHDKDIINYIDKIKDLCSCHTMFPASINFIMGKLLGLRDKIEIIGMFRLNKINNCIHHIKSG
DEIIIYFSYADPDGISIQVSTPKCTKFIQADMLSIIAIKCNCDYLIECISENDFEVVIFGIRKIE
>gnl|CDD|165283 PHA02979, PHA02979, hypothetical protein; Provisional
MKTHMFSFICDIDLYTECERISDFYRRLINEEKIIDIFISDTIRKIIQPFLLDDEILAHIKLIMDANDYS
FETGNSSNFIIICICSDDCGLLIHNDGGCIPLRKNNIVKFSSCNYGKIDIKADIAKDKEYNIFVFFIERK
>gnl|CDD|165284 PHA02980, PHA02980, hypothetical protein; Provisional
MFEYRCDISYNVICILSMLISYNSIEKSEFYNYTKSNKHLIFPPYYVRFSLYIISYIFMGHGMYLIHTRR
RDSNELIAYYILQLSINLSWFIVFYEMHMLRLSIAISTFSICLSVYNIYLWRFETDIIDKYVLPYLVTSY
INLLLNYYIIRSKLNNDYKK
>gnl|CDD|165285 PHA02982, PHA02982, hypothetical protein; Provisional
KIANLFTIAIAIIIFFGLINIYDEEDLKEDTADVNATVDQEVKLQCLFKDADEISRAMWKGDAGFMLAQE
ANGGTGINAFNYVPGPYKDKYALSVSGNSSTFTMKKPDPQNLGCFTCEAKDAEGKEETCEKCLEIQKEDI
LYVVEEHNNETIITCFVGSKHGDVPRFIVAGIVTTGGPMSGEIPKGFNQDSEGYRYNSIKINESVTDHIE
KPYCRYWIDNDHAREFKIELGGDEQGKENELTDFKDVYGRW
>gnl|CDD|222952 PHA02983, PHA02983, hypothetical protein; Provisional
MEMDAYTVITSLGVLKITDKEISTVCSDLGINIIDFIGPYIIASLNIVPIPVNDIKQSDLQKCYISYNGK
IVHCSKDNRLRFPIYKVYRAYRSKNSIIICFDKCPKLDIDGKHQPFYISSSIDIFNATIIEVYNLYKKGD
YHFIINPSDNFLMKLSKKSNFCLTDKNGWIIIDGKNEINY
>gnl|CDD|165287 PHA02984, PHA02984, hypothetical protein; Provisional
MIKRINVPNWVIKYVKKLLLKEFISKSDEKIIKTIINEFINENHSVLNILNINSLTVNINNCEESNLIDF
KDVNIKPQRHISYYNNYTLESNEYMFVLCLNGKTSIECFNKGSKITNTIKKGEAFTLNLKTKYVTTTKDK
NLHLAVITYTSNCPFIHYKNIVFSEDSFVYNIFSGYKFALFRLFDDDDTLLEDIIILNGRYYNSNSMKKV
NIINIKSLLTKYSIKQNNFIDYIPKSSHKTSLEIVELSLDNETVNQISDGTYTKDVYSLSGIKYKLLITY
GVLCYN
>gnl|CDD|165288 PHA02985, PHA02985, hypothetical protein; Provisional
MKNKIFKIIPFFNISKIKNQVLYLANNGILKYYDPEHQKIILDEIEQYIDETVLVKNLISIEVFNKKKKY
YQNIPSRLSKIIICIQSAKKGGCIIIINNITNNKKIITLNINHIIILSPLSKYTVSKVSKGSLIIIVLDI
DIPSMRIVYSSINNIKYSNNLSLLNPIPKNDIVFIIKQLTDYNNKVICEQILINNEWYTIITTDDKKFYI
PSICFGKSILDFNYVYDNFDKDIINHIINLEIPFDLVYPQKQIYNSIPIYEKILYGKINVI
>gnl|CDD|222953 PHA02986, PHA02986, hypothetical protein; Provisional
MDLEEEIINILINNHGTSYLDFNDNEISFKYFSNLCKEFISNKKKTTLIKEEIKKILLEIPDSMISQVWY
PIANLCDCVTYYNCSNEKWINDQLNDIDESLSNYFNKTSYGNLARIAITYPFDDKGRKSINILNKALFGI
D
>gnl|CDD|165290 PHA02987, PHA02987, Ig domain OX-2-like protein; Provisional
MNILKLVNLLSLINYLQSISCFVKITVSEHVNVKISCNKTSSFNSILITWKKNNKTIAGYGPCGPVIVDK
FKNKIEYLSKSFNESTILIKNVSLKDNGCYTCIFNTLLSKNNEKGVVCLNVTTDSYTTTLIQIKINSNSF
TIKGNIIVTTTLYQYSSSSSYSSYTNTSSRGSRNLYQYFKVILAIKMIL
>gnl|CDD|165291 PHA02988, PHA02988, hypothetical protein; Provisional
QNIITRSYINDIKCIESDDIDKYTSVLIKENDQNSIYKGIFNNKEVIIRTFKKFHKGHKVLIDITENEIK
NLRRIDSNNILKIYGFIIDIVDDLPRLSLILEYCTRGYLREVLDKEKDLSFKTKLDMAIDCCKGLYNLYK
YTNKPYKNLTSVSFLVTENYKLKIICHGLEKILSSPPFKNVNFMVYFSYKMLNDIFSEYTIKDDIYSLGV
VLWEIFTGKIPFENLTTKEIYDLIINKNNSLKLPLDCPLEIKCIVEACTSHDSIKRPNIKEILYNLSLYK
FYI
>gnl|CDD|222954 PHA02989, PHA02989, ankyrin repeat protein; Provisional
MSSLYEYILYSDTVDKNALEFLLRTGFDVNEEYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGYIE
TPLCAVLRNREITSNKIKKIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCDMLRFLLSKGINVNDV
KNSRGYNLLHMYLESFSVKKDVIKILLSFGVNLFEKTSLYGLTPMNIYLRNDIDVISIKVIKYLIKKGVN
IETNNNGSESVLESFLDNNKILSKKEFKVLNFILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGD
DIYNVSKDGDTVLTYAIKHGNIDMLNRILQLKPGKYLIKKTFEYFSEHGINDLFFNEKKMLMMILLMQYS
FTIYPIFYKNCYEVRLAFPNIIERYEKDLLLMKKETVGKNLSVYDLVFNREKEIIPVKFLKNENFLKFKS
SILYGEKIKQIILNSYEYYNCLNKAIDVLNKYCNKKNYWMYLPIEIQINILEYLTFSDFKTILKFKKKSK
KYFL
>gnl|CDD|222955 PHA02991, PHA02991, HT motif gene family protein; Provisional
MDLEETSSKEELFWKEIGIGDIKTLEISNSEDVIRIFYSYHKITDQKFKNSDQLFQVGTYSSDKKYIFDS
YITESDYISNINPKALDNIYKIKIMPIKDVPDKEIRSIHENKKKLMKKEV
>gnl|CDD|222956 PHA02992, PHA02992, hypothetical protein; Provisional
MINVSPLREAFLSNNCHTLTKAFKKLRIDDAMRLIISGLHPTSLPKKWYNEVVETLPEKLYLFKPKHVLF
IDLISVITKQKNVELYASHINFHKNEILQKCDKSLIAKCIPYMTISDDDIRCLRSRFYNNSVDYILSFIN
KESIYRMSYQFSESLTEKIFIQDYSMYDPLYEHQSFTSDFLTDMLYKYGIVPNNDGILDEISIELIIEIL
QSIKRPRDAIRFLDMLPKEQLTDDKLKNYIINKIKNGKIDQYIPYAEEFLVDRKEDLGVYANIFFDDVAI
DLTKYDLTKTELEIICKYIDRYEIYIDYIINYLIKNNYIDLLASIIDKVPAEVLTEELCIRIVCESNNKV
RIKDLPIHSSLVMVMCIQMKYEDLVDLLDEIDIDTLIEKGANPITDYTFTTNWYNKNNELIDLFVKKYGF
CSAKMNKLMFEYPLTKEASDHLLNIMDENKGASMFYPKTICSLFYLLCTNYKLKVKKIPGENRNIPYKKD
NRKNCFDSLDNSAIKSLILISNIPGLDTYNMKDITYEKTRNGICIQFNPQNNILKEERRILNQLFDIAKL
ASYGLFYIPYRYLPSWLPVVDIIEGREYTNPQKIEHGVIFKLYPEDFVEYKDLGNYVSNLYALNEPISNF
HAAINSLMQTLLIYLVLGSKYSIKSTDEFIASLLNTFFTGMKINEILSEDVSSVCKELNLLKDYICDSGF
VFIKKNYLKNTLSLCEKVCVAIILDNNQ
>gnl|CDD|165295 PHA02993, PHA02993, hypothetical protein; Provisional
MNVSTLEDIIKLNPFKNMNKIKINQKDNCLLGNRCFVKIDEVRYIPSNSVETSKSIRIRGHKFTLSELLY
SPFHFQQPQYQYLLPGFVLTCIDEAKKNKKICKYCISNKGDDDSLNINIFIPTINKSIYIIIGLRIKDFW
SPKFEIE
>gnl|CDD|222957 PHA02994, PHA02994, hypothetical protein; Provisional
KSAAIVTSLISLFDASIQFQKTICRDYCNSLSMQVVKEIKEFGYINEKTLSSKTWEDIQNNKIDALVFYQ
VKQLSISVEKLYNSMMRNRIKPIKIYFVRDNLAFDGIPPSFRMVNIDVKIYNRKKIKDLIILINMKTCNK
KIIKDFINDNFGSVDTLLSIINSNVLWVTSVLNNSNKRGNKMLKIISFRKFVNKIKKLKTLKNSSIDNIC
NDMKSISI
>gnl|CDD|165297 PHA02995, PHA02995, DNA-binding virion core protein; Provisional
MNSHFYYAHTPFYIDTKEGRYLVLKAVKVCDIRTVECDGSKASCVLKVEKPSPTCERRPSSPCERAERSS
SPNNNQVPFMRTNMLEDMQANNRNVASRILG
>gnl|CDD|177503 PHA02996, PHA02996, poly(A) polymerase large subunit; Provisional
IIPEIIEEYLGRRPSLNEYHMLKSQVRNIQKILNFNKDIFISLIKKNKKRFFSDIDGSASEIKARILEYF
SKQRRTYKIGKLLTIIELQSVLVTTYTDVLGVLTTKAPDVFSSNIRYDYSSMEKLARDALNSYNVAVISE
KVMGRHNVSDLVGNVNKLMEEYLRRHNKSCICYGSYSLHLLNPEIEYGDIDILQTNSRTFLINLAFLIKF
ITGRNVVLLKVPYLKNYMVLKDEEDNHIIDSFNIRQDTMQAIPKILIDNIYIVDPTVQLLNMIKMFSQID
RLEDLAKNPEKLRARLATLLEYVRYKYGIIFDGGRNNMPMPCAFDIDKRIITVDTKAYNFSFKKCVVYLD
ENSLSSDILDLNADDAVDFESVSNSAFLIHDNTLYTYFSNTILLSDKDAIHEISARGLSAHILLYQILTK
GDYKQPLSDLLNSLMVREKRPIYSIIPRDKKTGKHGIIDIEKDIITH
>gnl|CDD|222958 PHA02998, PHA02998, RNA polymerase subunit; Provisional
NSMMMTEQDIRELLKKYVDDEAEAEDLLKWATDKASKYYIKNIVNTKSNIEETKFEPKNNIGIEYSKDAK
NKLSYRNKPSIETNLEYKDLCDMIRGTNGTEKEILRYLLFGIKCIKKGVEYDIDKIPDVDYDDYFNVLDE
KYNTPCPNCKSKNTTPMMIQTRAADEPPLVRHACRDCKKHFKPPKFRDKRNKQVT
>gnl|CDD|222959 PHA02999, PHA02999, Hypothetical protein; Provisional
EMDYLINSNEKGYEYACRLFKLFYGHKSYNLEKCFNLVRSKMSMYYQLIKDDIIWNKEILPYLYEYIAYK
QNASNPNFQNSDSVVNLTKKQISSEENTMKMDKKKYKLKKKIKKVREINDTIRFAHYDYETIKKGYIKFK
KMIRKDIATSIPNICQKILKIYSHLSAIGKVSVNPYSMTKSLMNYMFPNLFEDDKRHIFYRCNPMKGYCV
LSSKKINLIRILLENRFKINENKWRIIKKYIDTICATGKKNTILGVYPYLKLKPISRIKGNYNFSNVDTL
KQLVESSFSLVDLTEKITKKTFRNLFKNGESHKYRCYAENNFIGLDQLKLINMCNKIVLAVDPVDRNVVF
NACIETVNKYLENPLKIIGDNIDECIDIAKEI
>gnl|CDD|177505 PHA03000, PHA03000, Hypothetical protein; Provisional
MDFIRRKYLIYTIENNIDFLRDEVLSKVSNFSLNHVLALKYLVLNFPKDVITKDVLANTNFFVFLHMVRC
CEVYDAVLRHSFDAPTLYVKALIKNYSSFSNAIQTYKTLVQELLQDEKFLEVAKYSPEFADIIGVNYDLA
LNPLFHRGEPIKDMEIIYAKLFKKTDFKKVKKLEVIRLLIWAYLSKQDTGLEFADNDRQDIYTLFQKTGP
IVHSDMTETFKEYIFPGDKTSYWVWLNERIANDADIYLDRPAITMYDKILSYIYSEIKQGRVNKNMLKLV
YIFEPDEDIRSLLLQIIYDVPGDILSIIDSKDEDWKKYFISFYKENFIDGKTFTSDRTFNDDLFRVVAKI
DPEYFDPERIISIFDHDPEKVKRFDDMDINNTYISNIIYETNDIDLSAIENLKKCQIYNEDTEYFIKEYN
TYLYLNEEDPLVLDNGILVKLSDVPSSKRFSLFSKNILKYYLDGKLANLGLVLDDYKGDILVKIISHLKC
VEDVTTFVRFATCKNPSILPSVIRTILANFNISIIILFQKFLRENLYYVEEFLDKTNHLTKNDKKYILQI
IKHGRS
>gnl|CDD|222960 PHA03001, PHA03001, putative virion core protein; Provisional
MELVNIFLETDAGRVKLAIENPDKVCATKAEMRKAINKFLELLKKYIHVDKSTFYLVVKDKDIFYFKCDK
GSISQVENEFYTFDEELLFVDDYNEITGVEFIVTDTMPISIYPKNGYAVISYSNNSKFYNGL
>gnl|CDD|165303 PHA03002, PHA03002, Hypothetical protein; Provisional
MPSYMYPKRARKALSKIISKKLNIEKVSKKHIDVILEYGLHGNLPKSLYDEAINFDINNIRFFPPESIRV
TDLIKLLQNSSRIDTKLYNAVLVHRKSLIVSGINVIKLMIENNLLTIDDIEYIISEKIVTATYLLKINPM
LASKKMILSKDEIIDLVKDIPSYATPYLYNNLSIDLDTLLYISDTFNIPPTNDSLLKLTDEEKAIELVKK
YPNDNIINYISDDIKYNKTFIEKIHEIVNENFPNMLTGLNDFLYSVVSKEELIKEYGIKSVAMFSLNYET
DLDTLTDDDKIFIEVNISYYDSRCRQFANEFRDKIMIKENRVITMNKGDSIRKKPMKLKCSMKKIIKDEE
NSIEDILIHIDNARKKRKLSIEDIESLISPFRLNPCVVRNILLSNSDIKTKILALKIIKDWKSQTLTNIS
SFKKIKGVIIMDMMDYILSKILHNHKNIFDKLKSLENKEIMLVCNCSNCSNSKINHYKSKNSTIHKRSSD
DDLINCLYDLVRYAIHGMVNPNLIGQRGWGPLIGLLSGTRKIKLNLYNTMEYENLKIGDILLSGHNLVNK
LIPITSTPLFKLIPFTCFPLNDYYAKVVILFNIILEYMISFILYRLIIIQRYTNVKEFISKVVNTVLEAS
GVYFCQIKVNDNIETEIDELVINGSMPVYLIHLFLKVISIILEEINGTR
>gnl|CDD|177506 PHA03003, PHA03003, palmytilated EEV membrane glycoprotein; Provisional
MWPFSKPPPGAGCRIVETLPKSLGIATQHMSTYECFDEIISQAKKYIYIASFCCNLRSTPEGRLILDKLK
EAAESGVKVTILVDEQSGDKDEEELQSSNINYIKVDIGKLNNVGVLLGSFWVSDDRRCYIGNASLTGGSI
STIKTLGVYSTYPPLATDLRRRFDTFKAFNKNKSVFNRLCCACCLPVSTKYHINNPIGGVFFSDSPEHLL
GYSRTLDADVVLHKIKSAKKSIDLELLSLVPVIREDDKTTYWPDIYNALIRAAINRGVKVRLLVGSWKKN
DVYSMASVKSLQALCVGNDLSVKVFRIPNNTKLLIVDDEFAHITSANFDGTHYLHHAFVSFNTIDKELVK
ELSAIFERDWTSSYSKPLK
>gnl|CDD|177507 PHA03004, PHA03004, putative membrane protein; Provisional
AAVPSIDDIYKEAQRRNDDQETFFTRGLSPLMKNTYLYHNYAYGWIPETAIWSSRYANLDVTDYYPITLG
LLKKFEFMLSLYKGPILQYEEKINTEFISRGSFSGRYINYLRNFSILPTNEFISFLLLTSIPIYNILFWF
KNTQFDITKHTLFSAVYTDNAKHIELARYFRQTGDYKPLFSRLKENNIYTGPFPIGQSRINHPNLPRGRS
PSDYETLANLSAILYLTKYDPVLMFLAFYVPGLSVTTKITPAVEYLMDKLNLTKEDVTLV
>gnl|CDD|222961 PHA03005, PHA03005, sulfhydryl oxidase; Provisional
MNPKYWGRAIWTVIFIVISKAKLDGNIEACKRKLYTICSTLPCPACRRHAKEAIEKNNIMSSNDLNYIYF
FFISLFNNLASDPKYKIDLKKVKPLV
>gnl|CDD|165307 PHA03006, PHA03006, hypothetical protein; Provisional
MHISKLEEDNINNNNIDIENDENYPGKIPEFFFEQKIENVKELYNELDNDEFSIVEECQEDIISKCIPID
DDIEDNKDEEEECFDENILIDDNNDNDEDKINIEDHNIIPKKKKSSFSDIKPEINIFEENNTKEKLKNVI
NQFEKKQDPIKDLSKTEIIKKLKDENKELKKKQKKMEKSENLNELIKKLNGCCEELINKKKEIINFAIKL
DISLPIDDFEILDEDEIEEIYDIIENIKIHKNSFDISMIIIKLIFSCIEKCLVDTFKLNEFIDISKEITD
DFIDNKCKATKNFINNNISTPEIPFIDIGIQIIGIGIGNYFNF
>gnl|CDD|165308 PHA03007, PHA03007, hypothetical protein; Provisional
MEEDFDKISKPDIIYTPILIDFIEKYGIDKIFKNKCIINNSKFYILFIEMQDYDIYDKIGKEYKLFIHNF
IKQIMDPTDLKEYIAEIIDIDNTNMYKNFSDYIILKFWDKVYNIKPSNINDYIDIIKMINIKHILNKDND
YKLYTYDHNIITEFLIFAWYSKKDLAIEILTKDDADIDINFDEILEFINKDDSIFNYINHNNKDYPLFKP
SDDTIDSYANIKFEIIDNNIDPGYIWKMPELFEKLKNDGIAENFNDKFFSILYNYICNGFVTHNIICWTY
LFGYGILDPDLLKELFAIIKKIPIELSGIISDLLINKNFIAIDEIKEHDENKITYEIFQGQCNINIDDAL
NGIINNIIESIAEKDFEPKGYFINFDIDINKIKFNEKFFNFLFNNNPISKDIDDIKMKIELNYKKNECGL
DYIDKYIDIYNTVNLINNNNNDFEALIDYEFTIFDEINEKDIIEDLFELPIIKKEILKILFEEYSFIPDC
NIINLRKQYMEFIKKKSNLINIYEALINKDIEKITDDIICKDIYLNIIFM
>gnl|CDD|165309 PHA03008, PHA03008, hypothetical protein; Provisional
MHINAMSNINLPRNNKIDEICDIAFISNITHIHDHNIIKIFFDKFDDFDEIIFVPGDIDILFDDDITFND
ELHHHVHNRKILRHGILKTYNENIDDNELDIIILRDDLIEFDFFDDIIKIYGQSHIEDKKFKNSHIHKAL
EGIAHIKKNDDEINYRNHIPKCDILITASPPFAILDDDLACGDLFSKVIKIKPKFHIFNGLTQFSHPNIF
IYKDIIFINSNINHNKKHFTEIEY
>gnl|CDD|165310 PHA03010, PHA03010, hypothetical protein; Provisional
FAKIKLAIFAFLILKIKSEFICDKQVHPDIIIKLPDILNCKDIEPIEADIILKKINDDEYESNAIIFSAI
DFICTEHASINIFSAFKETFIDHIILEKNDIIKMNETCHFKNEELIYNEDDNKYILGKAKHECVHYLFHQ
HTTEKEYINLKPGKMYYKKGLMHSEIANLPNCEYSSKFCKIFNDDVITWDIDENAKKDYKDSDAIDVDII
DENDNMHIIFIDNDLKNNISLIIDDIKYELDKDNFINTNEFAFKIKFLKILDLDAHKREITNYGSKRSYD
SSDATDVIQYISDIIQEEFNQIFELCEEISIMILELYAICAVNAKQCISSLINDKNINVNIVGNKYIIKK
CLDADIIEFKPSAEEYGCFCFEKIEIIFQIGNKIFNCYYNTESEEIFSSSKLIKKCKCENDIRFISCLDD
PDNLCIYNHFLGGIESFKIDKIINLGFKNNINELLKTIEPNNFNIPNFGSKPTLKDIAPFINSNIHFNDF
AEFNHESTIEKHGLQLNAILAIVILCIILIFMFVFSIAIIAIFAIKFLHKNFIKSN
>gnl|CDD|165311 PHA03011, PHA03011, hypothetical protein; Provisional
MKLFFILIILISSIIIIILYKIINIPPYESNILNKFDDEYLANLIFEPEQIFDFKEGDINAIIEILDELI
AQYNELLDEYNLIENEIKDLEIIIQDNDDEIHFLRAEIDKLKENIANLSI
>gnl|CDD|165312 PHA03012, PHA03012, hypothetical protein; Provisional
MIDISDFLTIDNIECNIECIILEDDCKDFIAFNKDYILEYKNIFDNIIKLISKIDEKTKFKIHKFFTNNI
NKLHLFKIKTLLPCYIALYYLSEDKIILNAAGCKYIFIIDIKQKKINEIINIASEIEKKKIDYDNMKNDI
SYIIKGWCYIIDLHICKNFFKFYDVLFDIIGRIFIFNLQLNINLKDKIKNIPTHFDIYKKIDNYIFIALQ
LISNYKIFFCHDDKIEEIIKVISKMCIKKSHNKIIYIKYIIDIFKNEYIFPIIQKDINNEDDEDCCLCD
>gnl|CDD|165313 PHA03013, PHA03013, hypothetical protein; Provisional
MLFKFIINIIIIIAFIISLIIIYFPLNIYELMSFSTIYDPIIAINNKFNDNKLKIITLFLSKNTIYKAQG
IITFDLIKDTITFKFRGNSYIFDIINDIDKFIAMIILAN
>gnl|CDD|165314 PHA03014, PHA03014, hypothetical protein; Provisional
MYKYYFGYGANQNINYLIHMHKLKIDFLNIKIGIILGHSFKLCYSKEIDSVIASIKKDDNGIVFGILYEF
NESIMKKFDKQEFIDKNIYKLAKMNVLDLEDEKIIEAQAYKAILDDDNNMFYDAPNFNIYKDIIIDALIE
NNILDYPLWYIKHINNIFKEYEK
>gnl|CDD|165315 PHA03016, PHA03016, hypothetical protein; Provisional
MLDDFIDLINDEKFNLLSMKDLNDDINDNIFNNFNANELFLSKLYNMIKNIFVKDKLIIKDGIAEQLILQ
IDNQNFRGDLDIEINIEPEKFKKIILDNIKNKNKESYKIEDIFENIIDEKIINDISQIMENYKIEFEEIL
DDIDFNDIVPERSKLNNNIYIAGADEKIYNEFINIEKGKFNMKNIIKFNINIVDDKFILFRCYFDIDFAC
NKIEHHDSFEIEKDKTFCKFLFLDILFTPDKKIEINNIEISNNIFLIDNKQNVINDQIQNLFHSFIKKHK
IIKEINNFIILFNKYKDELSFNINQNLKIIDNKILLNKIKNIFNDENILENYFAFKDLINNDKFIYLIED
ILDFEEIDTKIIDICPKKYIKKALKKAIKIIDAIINNNIEAGINDKEYEYDENILDKIANEFNLNKIECD
KIKKNKDLYKRYLKIYHLIDI
>gnl|CDD|165316 PHA03017, PHA03017, hypothetical protein; Provisional
MDDILIFDSANIADSFFKDICFDNTEKNNKYIIFIDWNNSIVDKKEDGFVIFRNGNGKSADDYNNIIKDK
KCKGFYIINDNIQESEDAHFELENLDIDIDLFFKLNKLDNKISDNNNIIYEIDFSGIIKPKDDKLNTHNI
IDNFLKDNFININNFIKNKLSIYIITGNMCNIIDILIFSKIKKHIFYIPSRDDEILFIDKIDKNHCNGGN
ILCGIINDLINIIKIAKK
>gnl|CDD|165317 PHA03018, PHA03018, hypothetical protein; Provisional
MDECNVNELKKIYNFIDLDHFLEIKIENFNKIFEDIDLDISDYNFDSDDIGLLIININDKKKMLVEKIHI
PDKYLDEDKIKIDKLFDNDKIKSLSEDEKLKDNIFIEIEKQKNNFNYEEDESNDNNLIIDCFPEECKICN
NKIKIDNEFNNDNVEMQIICDKNKDHIFKIDDYC
>gnl|CDD|165318 PHA03019, PHA03019, hypothetical protein; Provisional
MADFIFDIDYDNINIAANDIIKCDECEKNFNDALLAEENLKNLNDHCINKFLDFKKNHEPNIDLILDEEV
KIKLLNK
>gnl|CDD|165319 PHA03020, PHA03020, hypothetical protein; Provisional
MDDNEFLNNIIFGKDLPLINDLLKNIFIKKDCDKAILSKLTDGDNFNEDRIKIFALYTSILNDCIACFND
KLNKELIIEDLSIFSHELFCWENLSDKTEKRESIGFPLIYKHILNNENGKCGFDILFESGIIQINFNPVY
DLTFGNRNRIDQIKFQKLLISYTLFKNNIFYDGKLHFDEFNIPEAIITFKIQDLYFNFDINTFVILSCKT
KLYTADGINSIIESIYICDALAQFKEKTEYNFIEYFILAFIKLIDLNCIPIGFPIIIKDLENINERPIKG
IIVKFRLNNDKFNYGILADYFDCNYIIYIITESKKKKFEFLEHIVSSREDIFIAEDIIAIIKGYIIGKND
LC
>gnl|CDD|165320 PHA03022, PHA03022, hypothetical protein; Provisional
MFIKFKIECLRDRIKILSIFNPNGTLWCDGKKCEIVFTSDFKCCIRIPFIETNIQELLGFDICYDKIGDL
SLKNSIADKIILKFKDNGIMTEEEIFENNIFIIDPDYIDIKSISQINKKIDNNFNMFASAENIDDEPDIN
DTDKIISDKLELKKHDSGDLNIGYMAHDKFTLNKDNEYKYMIDPNGYNKTAAIFKIDLDILTEFIKKLIA
TKGASIEIEFFKNTIKFKAYRNDNIKNNIIDESCFYCSIINLYKPILRKYKIALENFALLKKLNISISDF
KAKDKKIYKSIQFNAIIDNNNEDLLIGLCIYPGMAGDEHKEEIKDYFIFMPIEKY
>gnl|CDD|165321 PHA03023, PHA03023, hypothetical protein; Provisional
MIFLFFMIYFFILIINIIFNKELNKLELDKKIFENAEDDLKTTISCINDHWFIVKRNSRFLDLLALKRDN
EYLNCNTNPIASDFLDSCGLNAKFNNKKEPCSAALLELLFLL
>gnl|CDD|165322 PHA03024, PHA03024, hypothetical protein; Provisional
MFLVIFNTFIIIILLAAIIGIYIFTFLFNIDFLINNNKIIALNANAIAINNINLLNLYDYSDDIFLINDN
IIKGIEVSQANNLKDIEIFNGDDISKISNQLNFYSASSGDQNILLGIRKAINIDINPFILFRNSIIAIVF
NNNEICHCFIGSNQNSDADDIIAHIEFIKENYNKFVIIGEIPIENNIQFLNILINNDFAIITNKKIIDKD
NQIFSFLEIDPGILFTIGP
>gnl|CDD|165323 PHA03025, PHA03025, hypothetical protein; Provisional
MIFDLLECQGIDMTHYLYLKDIGKENAKKLAEICEKIKNNMIIIKLETTIRKNTIQNKDKPIDMISPI
>gnl|CDD|165324 PHA03026, PHA03026, hypothetical protein; Provisional
MKIINSIIDSILQIIKLCFPKCEDEFEEFKCFEHIDIDNKKSDEIIKIFKEIEHEIANFLHTELSKLNLN
DYIIIFNKIENTFNDLNIPFELTPDEKNFIHDGLFRIHCCFDNDHMDKLIFIIKEDFIAIFMCIIFSFIK
HAIINYLETIKIINDVKKKDRNIKKLIMLKKGIIEIILKKICPILLSIYKHDTSNLPNAFKYNPLDDNEF
DTNKINKIIDCLKEEIEKNMFNIIAGAKKYNMESINNMINALEGIKDNCDKLCDKDEAKEFINFLKDPHT
QKIICDNADIDLPFDETIKDINSKILDDEEFISLNIFNELLDTDIGHKLLQIFSGKSPEEISGIIFGAEE
KANNGDILEDNSFGFKDGDIVLISVLECLDAIKACANNCKNCCMKIPNGSITVNVNTPISDIKIDDTEFK
L
>gnl|CDD|165325 PHA03027, PHA03027, hypothetical protein; Provisional
INDDEINEEKDSELELIENKDFDGKKIFNECGEIFKEMTEKKIDCIICDDIKCCIHCIVCNDENCIDHSI
GNLLKLNKCKFNNEHCTFVVNVEHQNFALINSIFGGNVLFMALDKFNIVKHKKKDSFSDNYSCIEIKNHH
MIDDMIECIENKIFETEKLIVDKDDGESFKDFDEVLRGIDKHNDTSFNHDAENGDFIIYIDRNKDYNKIN
FICGDKKCEFKIDAICNIFKDLDEDIKKFFKEFKLNGCILPNCFLFPKIDAKFILKFKFNVFIKLKAEFI
NIKKEDIDEENQNLEDEIIEEVFIDKLTANDKIKKDEEEKKDNNF
>gnl|CDD|165326 PHA03028, PHA03028, hypothetical protein; Provisional
MKPILINLIDILKTKTFVIDQYENKENIIYFDGDSYKKVKDKCDEEKDHIILITEIKDSIIEYNIMKNIK
NHFDINENDIYPEPIIMLDNIISNQKKIHNEFDMEILCIHHPTMMKQDNKKIEFIPDVNDGIENLKPSAD
SLCIDYKILYHPEIFKELKDRLIIAYKRSDMNILTEDDYRKCKPI
>gnl|CDD|165327 PHA03029, PHA03029, hypothetical protein; Provisional
MDDAEIVFLIIAIIIYIILILAIIGIIWGFLLSINKIRAAIDQNIRSRRKGLYWFLNFLFWLLPFALAAA
FYFFSIWFIMNPQAKIYWFPHP
>gnl|CDD|165328 PHA03030, PHA03030, hypothetical protein; Provisional
LNCIFLILIFLFIFLFIFFYIRIIKRDNFELETHETDEIANEFKDEIDNFDNDLINKFIQDMIIETRIKE
IEEEIENIISELNDKEEEKELIELDQPKEIDDEIVRKKLIDAKDEIENDEDE
>gnl|CDD|165329 PHA03031, PHA03031, hypothetical protein; Provisional
MYYSNHNILEDFIKIKFLIPKIYIISSNKNINDIEKIVKVHNKLAKNINKALRKDLPKRIDIDEIVLFDL
IIDNRKIIIKNYPYVYYEIGIKNCFFLNEIYKKDIIKAYIYTDGIDCIIFHKILKKSDIILFIIHANFGG
EKKSSGRCKRLEYCFNIWDAIHKIDYNLYCKINLCIKKIDNIDIICCIISKDNNIDMEEIYINIMNGINM
HCEFDIKIIFYDINKIRHFNDFLIFKNLEEYDIKLDIAEIIFTDKKKKIFLCIKKISKVCKIINKELDCN
NLSLDLIFEDKIGTKVYKILLKDIHFLHYYDINKDIFIYLDNNNIIKFFSNEINFDGLIDIDHKIFEFNF
KIYNKNNEFEKICIANNIIDKTEDEFKNINITHDDDIETSIEKIKKINNIELFKILNKLINKSIKDHMQI
ISENKEIDININDIKFDFLLHIFKGKNSD
>gnl|CDD|165330 PHA03033, PHA03033, hypothetical protein; Provisional
MKIEYINENIWDFLSDDDNINIISFISADFILCKDDCFIYIKKKYNSIKELKKQKKKKGEVAYIYKNNKY
IIYIIIADYIEDIVDDINILRALDNFKEIIEKDKIADIMSHMKFIEDNYETDKLLKYIRDHIPEEKNLYI
CL
>gnl|CDD|165331 PHA03034, PHA03034, hypothetical protein; Provisional
MIWYFIIDGKNIIFGNEAQLYIDKCFDLHPFCSLKEIDKKYKCFGCIIYIDFIIKKIFWEHDLFKTFDLF
NKNIAPYGNGFIIDEMIPACSISDFFFPHHNKLFYNIIINKTCEHKNNCHDRFCIEHNSHLIGVNFPFAK
NKHDE
>gnl|CDD|165332 PHA03035, PHA03035, hypothetical protein; Provisional
MDEDIIIKHFSVLAFIDNDKLNELLNKKRAGSNNDFLKEHCWKKIKNMDIAALAYEDNDKKKYFVSKLEK
TLPMNQSIDQQSGSAIKDDDDDIGINSADAYGGKSKKNGKKNKKNNKLNNANPSGNGKRKKNTKKAANST
DDSDHKQNLMGDMIDEDE
>gnl|CDD|222962 PHA03036, PHA03036, DNA polymerase; Provisional
MDIKCINWFESKGEKRFLFLKARCKDGETIFIRFPYYFYYVVTDELYKSLAPPPFESRFLGNMKIIDIDE
IISYYVNIEERKKTTADLWLIKEPKKRNIEKAFMDEFLNITWFYVLNNISPDGCYRIDIDKLEKINNKCY
HCDDPKKCFANKIPRFDIPRSYLFLDIECHFDKKFPSVFINPVSHISCCYIDLSGKEKRFTLINEDMLSE
DEIEEAVKRGYYEIESLLDMDYSKELILCSEIVLLRIAKKLLELEFDYVVTFNGHNFDLRYISNRLELLT
GEKIIFRSPDGKETVHLCIYERNLSSHKGVGGVANTTYHINNNNGTIFFDLYTFIQKTEKLDSYKLDSIS
KNAFNCNAKVLSENNNEVTFIGDNTTDAKGKASIFSEVLSTGNYVTINDDDICKILDKDIIENSFTVKVI
CKNNYIPGDTYTLSFGKDDVDLSDMYKNYNLEIALEMARYCIHDACLCKYLWEYYGIETKIDAGASTYLL
PQSMVFEYRASTLIKGPLLKLLLEEKTILVRSETKNKFPYEGGKVFAPKQKMFDNNVLIFDYNSLYPNVC
IFGNLSPETLVGVVVNDNRLEAEINKQELRRKYPYPRYIYVHCEPRSPDLVSEIAVFDRRIEGIIPKLLK
TFLEERARYKKLLKEATSSVEKAIYDSMQYTYKIVANSVYGLMGFRNSALYSYASAKSCTAIGRNMIKYL
NSVLNGSKLINGKLILANCPINPFFKDDRSIDTNYDTNLPVEYNFTFRSVYGDTDSVFLEINTKDVDKSI
KIAKELERIINEKVLFDNFKIEFEAVYKNLIMQSKKKYTTLKYIASSTDGSVPERVNKGTSETRRDVSKF
HKYMIKIYKTRLLDMLSEGNMNSNQVCIDILRSLEKDLIIEFDSRSAPLEMFLLSRTHHCNYKSPDNPNM
YLVNEYNKNNPEKIEIGERYYFAYICPINLPWQKKLVNIKTYERIIDRSFKLKSNERIFYEVYFKRLATE
VVNLLDNKVLCTSFFERMFGSRPI
>gnl|CDD|222963 PHA03041, PHA03041, virion core protein; Provisional
MDFMKKYSKELETTAKNKKDEEINSNKPEISSGDVDTMLKSKEHQYQQMIIDQLEEKKMLKIKNIVIPAK
SNKNNPQCSDVKSNDVPKKIRSISIEEIIKELESIKDETSSLQNESDSLVDDISTAKDTTFDAINAIMKD
LKKKFQLGNLDGN
>gnl|CDD|222964 PHA03042, PHA03042, CD47-like protein; Provisional
SIMFLFLLLYIYIIFSLSENKVSTYIYTTCNKTIVIVCNLNLLIYYNISNIHINWKFNNKVIFKKNNTNT
SSLKFNFSKNLSGNYTCEAINKFNKIKNTIELQYVIKWFTSEEINVILSLLSIYIIILWGTIITLTFKIN
KLKKIIYLYAISIWITLIMLVGQYMIGLNTNYIFVKIQGIILIQVSIFSSIFLQIILYKKIKNSYLLIIV
IILKVISYIISFIVIILSFIGCYNSIYGYLFIYKLLFINILELSSLVILFILPLGTNIKYKKLHIIEDEL
FLFSIE
>gnl|CDD|165336 PHA03043, PHA03043, hypothetical protein; Provisional
MGNKKNDYIKDIIKEYIRWRGNSDICEEHPLNIFFEKLMKFDSFAKKKIGESDYDFIKSMKLSLDDGPRL
DKLPTNLLDGLNAEEIIGLCGILAEKVVHSTYTVNWDRVFESLFNILDEKDLNYIKTKIM
>gnl|CDD|165337 PHA03044, PHA03044, IMV membrane protein; Provisional
MSEEDINESNFIHLLTNLSNNSDDSEFSATLSTIKEIISQINLKVLSINKKSKKNFRSNDQQLSYVSRRE
NNRY
>gnl|CDD|177510 PHA03045, PHA03045, IMV membrane protein; Provisional
MITLFLILCYFILIFNIIVPAISEKLRREYDAYTKYKQLKKNFICVDDRLFSYDFTTSGIKAKMAVDNNG
VPLPCSKINEVNKNNYLSCDDDDDIPDFRRSCSRAYLDLFFTT
>gnl|CDD|165339 PHA03046, PHA03046, Hypothetical protein; Provisional
MDRILSIFPGDDDEENDRNEHREKTSEEDGHYKKRLDVEEEEPNLINIRNEIKKIINEKYSTFPIHEDDI
SDILKDSFIHKDEMDIKDFVLRLLVLEKLFQLSIKRCKSLNNIIKRLENHTETVRKNMITLSKKIDVQTG
RI
>gnl|CDD|165340 PHA03047, PHA03047, IMV membrane receptor-like protein; Provisional
MITNYEPLILLGIICIALLANIKLSSKVKIDIIFFIQSILFMWFIFHFVHSVF
>gnl|CDD|165341 PHA03048, PHA03048, IMV membrane protein; Provisional
MDIMGMISNYFSTALIGGIILLAASCIFAFVDFSKNKATVTVWRALSGIAFVLGIVMTIGMLIYSMWGRY
CTPSKVVIDNGRYNSSQIELNGQ
>gnl|CDD|165342 PHA03049, PHA03049, IMV membrane protein; Provisional
MIGDIILVIICVVIIGLIVYGIYNKKTTTSQNPPSQEKYEKMEDLKTGYVDKLKSSHLNSFYKLFSSK
>gnl|CDD|165343 PHA03050, PHA03050, glutaredoxin; Provisional
MAEEFVQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRGAYEIVDIKEFKPENELRDYFEQITGGRTV
PRIFFGKTSIGGYSDLLEIDNMDALGDILSSIGVLRTC
>gnl|CDD|165344 PHA03051, PHA03051, Hypothetical protein; Provisional
MLYLHIYIYINICIIKHICNNQHHFSNIFYGNNSRCPLFKSLISKALMSAPYNICVYVTSNKCINIGGHH
FTSRSLIYYLRILNKIYI
>gnl|CDD|165345 PHA03052, PHA03052, Hypothetical protein; Provisional
MQLPEGIVTSLGSNLTITCKVSLRPPTTDADVFWISNGMYYEEDDDDGDGRISIANKIYTTDKRRLIHL
>gnl|CDD|165346 PHA03054, PHA03054, IMV membrane protein; Provisional
MDKLYAAIFGVFMGSPEDDLTDFIEIVKSVLSDEKTVTSTNNTGCWGWYWLIIIFFIVLILLLLIYLYLK
VV
>gnl|CDD|165347 PHA03055, PHA03055, Hypothetical protein; Provisional
MADAITVLTAIGITVLMLLMVISGTAMIVKELNPNDIFTMQSLKFNRAVTIFKYIGLFIYIPGTIILYAT
YVKSLLMKS
>gnl|CDD|165348 PHA03056, PHA03056, putative myristoylated protein; Provisional
MGTAATIQTPTKLMNKENAEMILEKIVDHIVMYISDESRDENNPEYIDFRNRYGDYRSLIIKSDHEFVKL
CKDHAEKSSPETQQMIIKHIYEQYLIPVSEVLLKPMMSMGDIITYNGCKDNEWMLEQLSTLNFNNLHTWN
SCSIGNVTRLFYTFFSYLMKDKLDI
>gnl|CDD|222965 PHA03057, PHA03057, Hypothetical protein; Provisional
MLCIFYLARLCNLIIYSLYSLLMYPMKKLISFMFGELNPFCDVLPDPKKDDDDADVFPDDLPIMPKEPDK
PKLKDQAEKPPKSENNNDANTYKLNANEFNGVFDFMKIPNPFKRYYEYCKKNNNNPQPVSEPPKKGFFEK
MMEMVE
>gnl|CDD|222966 PHA03058, PHA03058, Hypothetical protein; Provisional
MELRSAIITVLENLTDYQFKMLIFLTQDDLNIEEEEKEKLDRIDLAEKISEKYPGIRSIYFLKKVISEIP
NTEYVDSLLSRAIKDFNVTDVTFGKVQKTIKRKHRFRNPKVLKNLSSSERRKLF
>gnl|CDD|222967 PHA03060, PHA03060, Hypothetical protein; Provisional
MSEKLKKINKVVVNGKPYNSSSSSSTPTKDEIKKYGYCLNIKKPSSNDKSETYLHNNYPSIISTNNLFYN
T
>gnl|CDD|177511 PHA03061, PHA03061, putative DNA-binding virion core protein; Provisional
EEDDQLVLNSISARALKAYFTSKINEIVDELVTRKYPQKKKSQAKKPETRIPVDLIKSDFVKKFKLDNYK
NGVLSSLINSLVENNYFSKDGKLNDGAKKELVLTDIEKRILSKIPKSSPLYIDVSDVKVLAARLKTSASS
FEFNGHTYHLENDKIEDLINQLVKNGAIILDEKSSIKDSMYVISDELLDVLKTRLFRCPQVKDNLISRTR
LYDYFTRVTKRDESKIYVILKDKRIADILGIETVKLGSFIYTKHSMLVNAISSNVDRYSKKFQESFYEDI
AEFVKDNEKVNVSKVVECLTVPNIKIESNAE
>gnl|CDD|177512 PHA03062, PHA03062, putative IMV membrane protein; Provisional
MALSTKEIFSAIGLTLLALLMIVSGGALLFKSLAPHRVVMMRSATFNKVVSFLEYVAILIFVPGTIALYS
AYIKTLFF
>gnl|CDD|222968 PHA03065, PHA03065, Hypothetical protein; Provisional
MGIKNLKTLLLETGSLTKLDNNLKDRFNGIFVDTMSVFMSIAYSVNNLDELRSTFEEYVQQWVKKAGKVT
LFVDRGSIPIKQSLREKRRKASKNTIKRKREEIEKLEDDIKNLDVDDEMYEEIKTDLELKIDKLSFQLFL
ANSNNLKRLLESALARLGENVEIVYCDGVDAEFVMCARAKELAATTGEWPLLISTDQDTLLFSSCDRLPK
IIKTANQLYKFIPCAKTRYLSKLVALVNGCDFFPGLYGISITPKSLNRIQLFDDFTIDNVVRSLAIKNYS
LKTTDRTVDVDNIIDFINRYASLDESVYREVPPCACTVQEFIFSALAEKWADFKDTYLLTGVSLCAQLIC
ALEPRKEISVEEVETLLSLIDSARNKKVTINDIASVASIFGYELNKDKNIVFGILNLKNLMLCFNDSFYF
NNENIIENTKKNNIINIG
>gnl|CDD|165355 PHA03066, PHA03066, Hypothetical protein; Provisional
ASSLLYLLFFIIFLCISYYFNYYPTNKLQMAVKELNRENAIIKQRNDEFPTTLNTIIFTDPETVISTQVN
TYYNSSIGTVTMLSNNKKRTFNLYFDEDVRTLLPILLLSK
>gnl|CDD|222969 PHA03067, PHA03067, hypothetical protein; Provisional
MNNFIKQIASKVRKPTKKLTPPDGEIKLKECIISFNFPNFYYNNENLFNKPENTLDDVLKSLLIMESFKY
EKYVIKGLIRILKKYAHVNDIYFLPVGWLAGIDPDPETHVVIKIIFSSSLIAIKNKVKEYLSPHDILDLS
LAQTDKELSINRFSTPDAPPVAVISFFPFDPEYILIVLFFGRYNDSYCGISYIAPKENLYYIIEILKPLV
SEINLLSDEIGRFTSTRLFNSTGSKKKFPENKITSICEIVHIFDKLKFPAAKSVTPLNLTPFVPKKIVSL
IDLPSNVEIKCASRNGIDFITHIDNKRLDTILIIAKDDFLKNVTFSGTFKKENIIWKGKYTYRITESSFD
VPTLKVVSSKKKICKKHCFDNSTYTTRTLSYIL
>gnl|CDD|177515 PHA03068, PHA03068, DNA-binding phosphoprotein; Provisional
MKKAIKKSVVTPKRPPNEEDSLFTCAGVIEYAKSLSKSNEKCIESVTLTPSQYPSCSNISINLVESLASK
MTSTYIMVEGEAKIYKNKKKDFRREDGYFLKIKPTAASPMLYQLLECIYGNIKDGKRIPPSLCSLSVETM
EEKTFKDGCIYINKLNGAIVEYTSNGEVSIVRSISEELESLSKRDPQMAKAILVPIVFYRNGNETKVTFA
LKKLIMERECSATVIDLDGESERVSMSETTEEDIVRGLGVVDIDDECIEDDDLESSLFNV
>gnl|CDD|165358 PHA03069, PHA03069, DNA-binding protein; Provisional
MEESAGTPFHDPKYFVSPFILNTDDGRYLVLKAIKLCNVKTIDCMKKESSCVLKVDKPKSPCPISAPDSA
PKCIIQQTQQPNQQPNQQRQAPQLRFINTGALSNIFANTTDKAARMINQ
>gnl|CDD|177516 PHA03070, PHA03070, DNA-binding virion core protein; Provisional
MSLLLENLFDEDALFAAGITRYDDLELVIAGAKVKFPRSFLSIFNIVPRNMTKYELELVQTENITGAVFT
TAYNIRKNLGLGDEKLTIEAIENYYLDPNNDVLTLMINNTSLSAVAPYKKRRRRNKNPVIFRQGSAPLLL
IFESRKKVNIYKENMESASSSSYTKIGDNIALISKYANTNLLDVHSPSASLTLNAVYGFTNKNELRKLSS
DKELEEYQSTPLQEPIRLNDFIGLFDCVKKNIPLTNIPI
>gnl|CDD|165360 PHA03071, PHA03071, late transcription factor VLTF-1; Provisional
MSLRIKIDKLRQIVAYFSEFSEEVSINVDSTSNLMYIFAALGGSVNIWAIVPLSASVFYDGDENIVFNLP
VSKVKSCLCSFHNDAIIEIEPDLENNLVKLSSYHVVSVDCNKELMPIRTDTSISLKIDQKKSYIFNFHKY
EEKCCGRTVIHLELLLGFIKCISQYQYLTILFKDDNIILKTPGNLDTFSREYSMTECSPELQKFSFKIAI
SSLNKLRGFKKRVNVFETRIVMDNDDNILGMLFSDRLGSFRINIFMAFQD
>gnl|CDD|222970 PHA03072, PHA03072, putative viral membrane protein; Provisional
MDKTTLSVNGLELEYAREKATKSIRAAKTSTLIFFVIILAISVLLLWFQTSDNSVFSELTKYARIKNNVK
SWRPLVESKTKLESDRGRLLAAGRDDLFEFNCVDFGSYFLPVRLDKKTFLPQAIRRGTGDGWMVKKAAKV
DPSAQQFCEYLIKHKSNNVITCGLEMMNELGYSGYFESSHWCSDFLNLLN
>gnl|CDD|177518 PHA03073, PHA03073, late transcription factor VLTF-2; Provisional
MAKRVSLPDIVISAPKAVAKPAKDESISCILPKYYNSVADVRLKTNSDNDYCWFCKQDLIIAPLFIETLK
GGAVGYFCSKICRDSFASMVKSHVALREEPKITLLPLVFYEDPEEVINIINLLRNKEGVYGSCFYKENDQ
SIDISLRSLL
>gnl|CDD|165363 PHA03074, PHA03074, late transcription factor VLTF-3; Provisional
MMNLKLCSGCRHNGIVSEKDYEFCIFCESVFQTSSKVQKKSNFHVSNKLIHLRNVLRRLLSNQCSGEIIS
ELLELMNKNQISTKDVDANFVSSFLKAKERINKKDYKLVFEIINQVKDEKLNLTTEKINEVVEIFKHLVF
FCQENTPSKTINYSFFLDKIFDITNVTKNLKPQTVKNYTKNNSNQLIWENFLIHMRNKKKATTIIDYGHE
YVFVPNNFITCSLEV
>gnl|CDD|177519 PHA03075, PHA03075, glutaredoxin-like protein; Provisional
MKKTLILFGKPLCSVCESISEALKELEDEYDILRVNILSFFSKDGQVKVLGMDKGYTLINNFFKHLGNEY
VSLFKYDPETKQMAFVDISKFLVLAQIDKSFVDLDQLKEEIEKAPYGVWPPPK
>gnl|CDD|222971 PHA03078, PHA03078, transcriptional elongation factor; Provisional
RDLILFHLSKFLLTEDEESLRMFISLCRGFNIDLEELITEFYNKKYLKKITKVLECADLLPELSLEFPDD
ILRELVRLRLYKFSKTIKRSYKLPNNMKGIAVIKDRNVYVRRANDELLDFLFKEYNPQIYTYAEGKPDSL
PGSKLILCGYSKVTFFAYTTTRITTNKDLDVVVTEKCIDKLLQPQNAQLLKNLFDKGSGVINKALRKIFY
SVLGGGQTP
>gnl|CDD|165366 PHA03079, PHA03079, hypothetical protein; Provisional
MEVIADRLDDIVKQNIADEKFVDFVIHGLEHQCPAILRPLIRLFIDILLFVIVIYIFTVRLVSRNYQMLL
ALVALVITLTIFYYFIL
>gnl|CDD|222972 PHA03080, PHA03080, putative virion core protein; Provisional
MMAEQKQSRIFDIVSKAIVKSVLKGLSINSEYIEAKAKQLCYCNNSSYKESIINSIYNCCESNIRITDIE
HLKKILDNLRRHSVYVCNSTEFWRLYNSLYRFTHCKSFFNTCMPTIRATLATLITLILSNKLLYAAEMVE
YIETYLFSSNKPPAQELADLLEMKYGLINLVQYKIFPIILGEKDCCDEIFAAGASGISDYSVEIERLLEL
PVKTDIISRVYDFLSRKGINTSNNYAEYVAGLKIEELPEANSNDIKNPVSIQPANINENNIAKASKLLDT
AEKYSKGHVLDGAVTSPLTKNATIVDQIPFSASDMEKFTILEYLYIMRVLANCIKKKNSGKKNGGITLNI
NSPFKTITVPGTPSVK
>gnl|CDD|222973 PHA03081, PHA03081, putative metalloprotease; Provisional
MIVLSNGVRIFINPSMKKDIYLGISNFGFENDIGEILGIAHLLEHILISFDSSKFVANASTARSYMSFWC
KSIRGRSYIDAIRTLISWFFDNGKLKDNFSLSKIRNHIKELENEYYFRNEVFHCMDVLTFLGGGDLYNGG
RIDMLDNLNDVRDMLSNRMHRISGPNIVIFVKELNPNTLSLLNNTFGTLPSCPETIPPPILVSIGGKIVM
MPSPFYTVMVRVDPTLDNILAILCLYETYHLIDYETVGNQLYVTISFVDEDDYESFLRGIKILDFEAYPR
INLNYGDDYLMNIYLNFPWLSHDIFDYITTINDNSKSLLKSLERDIYASIRERDYIVIYPNFSKSIFNTR
DRQRHKIVVLDCPDNNNIGRNHKPKRSIPLMKKQTSNEIFIRYGDASLIDYVTLALGYKDNKLKRTNEGI
RIRHQFSADDIKAIMESDTFLKYSKSKPAAMYQYIFLSFFVSGNSIEDILENRESTLKLSKRYKNKILFG
KNTRYDITTKSSFVCGIVKGKSLSNESLTNMMWDLKKKGLIYSLEFTKLLSKNTFYLFMFTIYPEEVFRY
LTTNKLFSSHCLVVSTKGDVEDFSSLKKDVVIKLG
>gnl|CDD|222974 PHA03082, PHA03082, DNA-dependent RNA polymerase subunit; Provisional
MVFQLVCSTCGRDLSEERYRLLIKKKSLKKVLRTVKNSCCRLKLSTQIEPQRNLTVQPLLDIN
>gnl|CDD|222975 PHA03083, PHA03083, poxvirus myristoylprotein; Provisional
MGGSVTLPKRDPPPPVPTSEMNLNVDDMLDTIATLAKIDERVPIGILTKDKKAQLKKRFPEFLFIESGPG
GLYELLRSSYLGDPKYCCKNFNLTHYWEDNDGKISDKYKPNAVLNSCDPDLQDSGICDNTLFRWCQDDTS
DKNICNDWIGSAFNRRNTSSEGIQLNNKFISLCSKNANNPICEDWLHALRVKNTEEFDNLIDYVLYQQSD
DFKSKYMRCSFPSEDTLEESLKVAEPRECWDPECANSNVNFLLTENYTNLGLCTISRCNISINNLNMDSK
SSLRMSCNNNDLLSPSPVNKEKVILHNVDRSFELKIHLITILSLLVIWLLIVAI
>gnl|CDD|222976 PHA03087, PHA03087, G protein-coupled chemokine receptor-like protein; Provisional
MNYTLTINTTIENTTDYYYDTYYDEDYADCDLNIGYDTNSTILIVVYSTIFFFGLVGNIIVIYVLTKTKI
KTPMDIYLLNLAVSDLLFVMTLPFQIYYYILFQWSFGEFACKIVSGLYYIGFYNSMNFITVMSVDRYIAI
VHPVKSNKINTVKYGYIVSLVIWIISIIETTPILFVYTTKKDHETLICCMFYNNKTMNWKLFINFEINII
GMLIPLTILLYCYSKILITLKGINKSKKNKKAIKLVLIIVILFVIFWLPFNVSVFVYSLHILHFKSGCKA
VKYIQYALHVTEIISLSHCCINPLIYAFVSEFFNKHKKKSLKLMFTSSGKSISIG
>gnl|CDD|222977 PHA03089, PHA03089, late transcription factor VLTF-4; Provisional
MSWSINLGNGGDNFKTLDEIRAHVKSTTESVDKVNDDIFPEDVEIPSKKTSKKKKTTPRKKKTTKKTKKK
KKEKEEVPELAAEELSDSEENEENDKKVDYELPKVQNTAAEVNHEDVIDLSDLKLATENIIKDLKKINSR
VSAVSTVLEDVQAASISRQYTSLIKEIDKLKDLVNLGKSKVVRKKVRKTKK
>gnl|CDD|222978 PHA03091, PHA03091, putative alpha aminitin-sensitive protein; Provisional
MTSSQKKKLETKYIECIYDATEKKFVTEFKKVFYFSDFDITKDLIVKIFLEEPSKMTFSIIKCISRHIME
NLKLIYELKIDGVYSSNIIFKVWKDYKLINSMSDVNFNAMMDRYFMMRKNNNNNTIGKIIKEFMTYDQMA
IDHYGQGYINAIIYQIRKRPNQHYSFSLFKRFKRTIDDTIKVDIEFIKKMIGFVSILSKYDKVSNPYSYI
FFDDISYDERKCFIKYLETKYP
>gnl|CDD|165374 PHA03092, PHA03092, semaphorin-like protein; Provisional
MIPLLFILFYFANGIEWHKFETSEEIISTYLIDDVLYTGVNGAVYTFSNNKLNKTGLANTNYITTSIKVE
DKDTLVCGTNNGNPKCWKIDGSDNTIKRSFGHRPYRIYFIKENIIYSFYTKSKQTRSIQVDADL
>gnl|CDD|222979 PHA03093, PHA03093, EEV glycoprotein; Provisional
MDTPDSDENQTSFFGSTIYGDKLKKKKNKKKVKCIGICIRISIIISILSLIAITATLALQLNKCKSANES
AITDAALDNAASSTYSDDADSTTQYKHKESCKGIVYDGSCYIFHSEPKTFSDAKADCAKKSSTLPNSNLM
TTWLSDYLEDTWGEDGNGLTKETNDLEDIDVSTEMRKYFCVKSFN
>gnl|CDD|165376 PHA03094, PHA03094, dUTPase; Provisional
MSNSPVRCVKLSNFAKIPTRSSPKSAGYDLYSAYDYTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSL
NYGIDIGGGVIDEDYRGNIGVIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGS
SGLR
>gnl|CDD|222980 PHA03095, PHA03095, ankyrin-like protein; Provisional
DEEDESVDIIMEAALYDYLLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLL
EAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINPKVIRLLLR
KGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVRELIR
AGCDPAATDMLGNTPLHSMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG
ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDATRLCVAKVVLRGA
FSLLPEPIRAYHADFIRECEAEIAVMRTTRIGTGVSLLDILFARNPDILLVSNASLRKKARLTVYGKALR
ARIEEMRKRSKLVERIIKLICPCALPPEIVMRILDFLPDDDLRNLLRCLKL
>gnl|CDD|222981 PHA03096, PHA03096, p28-like protein; Provisional
MDDIIICCIDEKFSYIKYNDVELIIMKSNGYVNVTKLCKSRNKDFTRWKRLSSSKRLIETIKKNNSVDGD
DPIIYVERGYNNEINGFYVHPDLLPYIAKWISPDFAIKVSKLINYYNANVYMNVEKDEDNCYKGKYCEYL
HGDICDICEKYLLHPTDIKQRYNEQKTCLSYQLRLLLSKICGICLENIKAKYIIKKYYGILSEIKHEFNI
FCIKIWMTESLYKETEPENRRLNTVIVFIEKINEDLKNNIPSRYWIDDKYDKNLLSFRYKKMHIRKVCIE
LYKS
>gnl|CDD|222982 PHA03097, PHA03097, C-type lectin-like protein; Provisional
EEEKKCCKVTVHWILVPCGSIIIALIALVIILSCKLSPGDRSGLNCRSGWVGYNNKCYTFSENITNKHLA
IERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGIEKKKGDDDDREVLDKVVKPPKSGKCAYLKDKTII
SSNCNATKGWICFDRLP
>gnl|CDD|222983 PHA03098, PHA03098, kelch-like protein; Provisional
MYSFELQKFCDESIIIVNGGGIIKVHKIILSSSSEYFKKMFKNNFKENEINLNIDYDSFNEVIKYIYTGK
INITSNNVKDILSIANYLIIDFLINLCINYIIKIIDDNNCIDIYRFSFFYGCKKLYSAAYNYIRNNIELI
YNDPDFIYLSKNELIKILSDDKLNVSSEDVVLEIIIKWLTSKKNNKYKDICLILKVLRITFLSEEGIKKL
KRWKLRIKKKKIVFNKRCIKIIYSKKYNLNKILPRSSTFGSIIYIHITMSIFTYNYITNYSPLSEINTII
DIHYVYCFGSVVLNNVIYFIGGMNKNNLSVNSVVSYDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGG
IYNSISLNTVESWKPGESKWREEPPLIFPRYNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSK
GSPLPISHYGGCAIYHDGKIYVIGGISYIDNIKVYNIVESYNPVTNKWTELSSLNFPRINASLCIFNNKI
YVVGGDKYEYYINEIEVYDDKTNTWTLFCKFPKVIGSLEKNIFT
>gnl|CDD|165381 PHA03099, PHA03099, epidermal growth factor-like protein (EGF-like protein); Provisional
MSMKYLMLLFAAMIIRSFADSGNAIETTSPEITNATTDIPAIRLCGPEGDGYCLHGDCIHARDIDGMYCR
CSHGYTGIRCQHVVLVDYQRSEKPNTTTSYIPSPGIVLVLVGIIITCCLLSVYRFTRRTKLPLQDMVVP
>gnl|CDD|222984 PHA03100, PHA03100, ankyrin repeat protein; Provisional
LYSYIVLTKSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNST
PLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSD
GENLLHLYLESNKIDLKILKLLIDKGVDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKY
LLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETLLYFKDKDLNTITKIKMLKKSIM
YMFLLDPGFYKNRKLIENSKSLKDVINECEKEIERMKEIKLNKVTVYDIIFNKNINFLSRYVNNKSVTKY
TTSKIYGKYIKKVINKAIERKKLIKKIIKKLNNLCKNTYWNILPIEIKYKILEYLSNRDLKSLIENFTVN
KT
>gnl|CDD|222985 PHA03101, PHA03101, DNA topoisomerase type I; Provisional
MRALFYKDGKLFEDKEFTNPVSDDNPTYEILKKVKIPPHLTDVVVYEQTYEEALTGLIFVGSDSKGRKQY
FYGKLHVKNRNANRDKIFVRVHNVIKKINCFIDKNIKIKKKNDVNFQLAVFLLMETSFFIRTGKMKYLKE
NETVGLLTLKNKHITISNDKILIKFVGKDKVSHEFVVHKSNRLYKPLLKLIDKTNPDDFLFNKLSERKVY
KFMKQFGIRLKDLRTYGVNYTFLYNFWTNVKSLDPLPSIKKLISLSIKQTAEIVGHTPSISKSAYMATTV
LELLKDSNILETIKDTTFDEFLNIVVDYVKNSTT
>gnl|CDD|222986 PHA03102, PHA03102, Small T antigen; Reviewed
REESKELMDLLGLPRSAWGNLPLMRKAYLRKCLEFHPDKGGDEEKMKELNTLYKKFRESVKSLRDLDGEE
DSSSEEEDVPSGYVGATFGDRVNALYCKDWDTCLKNLSSLCKCIFCLLRKQHRLKQKLRPEPLVWGECYC
YKCFRQWFGLDIT
>gnl|CDD|222987 PHA03103, PHA03103, double-strand RNA-binding protein; Provisional
MSKIYIDEVDIYELVKKEVKNLGLGEGITAIEISRKLNIEKSEVNKQLYKLQREGMVYMSDSNPPKWFKT
TEADNDDNDDVSREKSMREDNKSFSDTIPYKKIISWKDKNPCTVINEYCQITSRDWSINITSSGPSHSPT
FTASVIISGIKFKPAIGSTKKEAKNNAAKLAMDKILNYVIIKF
>gnl|CDD|222988 PHA03105, PHA03105, EEV glycoprotein; Provisional
MGIVIVVYVVVPLSFIVLILYIFFICKNTIKKFLKKKKGKNICIRLNSITYSTNSIEKEDIKTGSSTISE
SDWSNSSGEIYANFRSSKKEKSFKIKNEKENIEVEIKDCDNEFEEDSNNNEENLNWDDNNNGVYDLPPPP
DNIDLSSNDDCLYSLPPDNVSNIEEKITKLIAESVSNSDYYNCCNSLV
>gnl|CDD|165387 PHA03108, PHA03108, poly(A) polymerase small subunit; Provisional
MEAVSMDKPFMYFDEIDNELDYDPESANEKPKKFPYQGQLKLLLGELFFLSKLQRHGILDGSTIVYIGSA
PGTHIRYLRDHFYSLGVVIKWMLIDGRKHDPILNGLRDVTLVTRFVDEAYLRRLKKQLHPSKIILISDIR
SKRGGNEPSTEDLLSNYALQNIMVSILKPVASSLKWRCPFPDQWIKDFYIPHGNEMLQPFAPSYSAEMRL
LSIYSGEPIRLRCITKSDAVKYEKKMFYLNKIVRNKIVLNFDYPNQEYDFFHMYFMLKTVYCNKEFSSTK
AKVLFLQQSIFRFLKIPITN
>gnl|CDD|222989 PHA03111, PHA03111, Ser/Thr kinase; Provisional
MGVANDNSPECQWESCDDLSDDTTILGDDIYFDYVYSQLDLHQSWAPSVRLLRYFKNFNKETLDKIAEND
YINPSFFQQKDKRFYPINDDFYHISTGGYGIVFKIDKYVVKFVFEPNKGYSPMETTAEYTIPKFLYNNLK
GDEKKLIVCAWAMGLNYKLTFLHTLYKRVLYMLLLLIQTMDGQELSLEYSHKYFLKSFNEKKDSIKFVKL
LSYFYPIVVQSNINVINYFNHMFHFFEHEKRANYLYDRGNIIIFPLARCSADKVTEENAAELGFKSLVEY
IKFIFLQIALLYIKIYELPCCDNFLHVDLKPDNILIFDSDEPISITLKDATYVFNEPIKACLNDFDFSQV
ANIINKKIKNSIKVEHNWYYDFHFFAHTLLKTYPEIEKDPEFSSALEEFIMCCNKSTCDKFRLKVSILHP
ISFLEKFVRRDIFSKWINGGNDAS
>gnl|CDD|222990 PHA03112, PHA03112, IL-18 binding protein; Provisional
MMIVMIILFLIIYIYSVDSYVDCVKTRDVNIYIPTKETEKVVLECRGCSYFPKFSYVYWLIGNNKSDVDQ
KPIEHYGEGIYESEKPRTCDNEPRTDLIVYNVTDEMKFTKLTCVLMDLDGPIKKSIILNNIWDCFNTTSE
N
>gnl|CDD|177532 PHA03115, PHA03115, hypothetical protein; Provisional
MSRKFMQVYEYDREQYLDEFIEDRYNDSFITSPEYYSAEKYMCRYTTLNHNCVNVRRCALDSKLLHDIIT
NCKIYNNIELVRATKFVYYLDLIKCNWVSKVGDSVLYPVIFITHTSTRNLDKVSVKTYKGVKVKKLNRCA
DHAIVINPFVKFKLTLPNKTSHAKVLVTFCKLRTDITPIEAPLPGNVLVYTFPDINKRIPGYIHVNIEGC
IDGMIYINSSKFACVLKLHRSMYRIPPFPIDICSCCSQYTNDDIEIPIHDLIKDVTIFKNKEMVYYLKLN
NKTIARFTYFNNIDTAITQEHEYVKIALGIVCKLMINNMHSIVGVNHSNTFVNCLLEDNV
>gnl|CDD|165391 PHA03118, PHA03118, multifunctional expression regulator; Provisional
EAAASIPCDPDIMACICDDFMHLLPEDDPIDDFALEVQDWAEESVPNSVQIDDDEAAGEILGEDEETPNP
ADVCEDADRAYTNPNFEKKAHGRREGYHHDDEKCLVTFLDDINHHGGRDTEPGHAHIENGERKSPKSYNQ
QSRKKHRDESLRNKHGRPSGPPAMSPGEHFDQTHDAEYRLRFNERDARRDRIRKEYDIPTDKITEQAIET
LKIAGASISIDSVLEFDETIEALIRRMATFYDEDGNIEEGDSWADGGCFPGIEENISWAELMLYGHELYQ
TFESYKMDIKIARALRERIIRGESLIEALESADELITWIKLLAAKNLPIWTNNPIVATSKSLLENLKLKL
GPFMRCLLLNRDGDEELSRTFPELLHQQRFSDITCIPTFMFVMIARIANAVLRGDKCIAYDDISCNAQVL
EEYTPGSCKAGVLEAIITHGRECGIPECRISCWAEFLPDAHHHGKFFKCSTFEC
>gnl|CDD|222991 PHA03119, PHA03119, helicase-primase primase subunit; Provisional
AQPFDGSTIRILFATKGCAISDSLMLLTGQISFRPIYVVSYTWTEDLNDVFYEDGWADNMTPTKRLRMMA
DEDSHHHLAAVLLEHGVHVIFYLIGGLPTGGCKPRTWPVFFCRFQTPMDSIALAKALWYGDPLSTGLLSD
TLDEERTFAIHDDLIQALAITTKQLVPRLGCTTDSANPETSLKTLSKKMNGRRGLTSLYAHYERAVLAAY
RRIYWGYNCTPFWYVARFGPGEKTLVLATRYYLLQTTTSYLTHTGACYDLQAIKDLICTYNVPVTDNTSG
YDISDLASFAKLSRFCCSSGYTRGSAAANACDYIHYRITADISEISTVGEYITNDRKGLRVSDREFVDYI
YLAHFECFNRKQIRDHLRAVTLTDIALIPDVVSASSLGRSAIENFFSHVRSRLNISDYISKNVICDVVVL
NEKLGRKYAASKTYPIVNSLTAQSGGYIGMCDVAGALTKRIEGIEKSFARRGWPSTITSQTQGIFSQHDN
PSGSTVSVEAIKAANQANSINSHKPAWEYSSSITRRLLFFVASTSISEQNSLTATYKSPVNALLGRRDLH
GPIPVYRISLPEGKQAFAVIHQDDWSIVTRRYTSVNSLNLLPESLKNITGKDEHTAALRDMYLTHVLHQR
VKSTSGIASSIPSSQMYINRNELFNGGLLISNIILDVDFHLRKPIPLGVLHAGMRAFRHGVLTALQLLFS
EAVVDWNSHPCYFYKTSCPPQPRHTICDINSQDINEIQDFMWDADILYQDVELNELHDEGAYDLNFKVSE
DVVNMESKEQLGKLDTTYVCGCTEKLGFRVCIPIPPPYLLFGSSTLKGMARIIQQAVLLERTFVETMGPY
LKDFSFIDTGVYSHGHSLRLPFFSKVTDGGTFNGLLLPFYVVPIGCKDILTFLYAHTNPNNFHFHSMPAY
NTPTHIILHNLGGEYASFFERKVASNKTAFLSPKTSLRKALQKLGIQPDDAETIEAFIDSIVLESITGYI
RVHFPGRDREYQATSSKCIVLKRDWVLLQLVRTGCYSRMQGFTCLRYPHRGGRTAPRTFVSLRVDHHNRL
CASLSQQCFATKCDSNRMHTIFTLEVPNTCRGDVN
>gnl|CDD|165393 PHA03120, PHA03120, tegument protein VP22; Provisional
MASPDGDRICRSNAVRRKHMDAQYVNVPYSGKPRNPVARRSVVVGFPDDSDDSLGYIATVEADSPPLFYA
DLSFEHDKRHPRMHIPNDSSDSDDDFEDIDEVIAAFKEARLKHEHVEDAVYENPLHGEAPPRMFQKHAAV
KPKDEDSPKRAPPGAGAIASGRPISFSTAPKNATSAWCGPTPAYNKRVFCEAIRRIAAAQAQKAAEAAWN
SNPPRNNAELDRLLAGAVIRITVHEGLNLIQAANDADLGEGAPDRKQGHARKKGDIQGDMDDEPMYAQVR
KIKSRGDQPTSGRITNRARARSASKPDGRK
>gnl|CDD|165395 PHA03123, PHA03123, dUTPase; Provisional
MNEAQFDAIIAAAENRERTDIFCRQRIPNECLKDEILIDVGMECADDFNCALDDDCGRHQPLLLRNHKKI
ELPSDEAMECGDFYIQQLDLGVKAAPPNEYALLLIQCIDSALADEDDFFIANGVIDAGYRGRICALLYYK
KGVTIILPGDLMIYLFPVKLAQSRLLNKNVDKHLDPIFAEHMCQPLSNSPSGKEKIAIKEFADINNAIKQ
GEPCHKDHAEYTETHIDIPLIFKHTIFKPKRQEDAGYDICAPFEITLKANEFIKITLPFIQDLDLNHPNI
DAYIFGRSSKNRIGIIVCPTAWIAGEHCEFYIFNATGDDIIIKPGDKIAQVLLIDHNNQSIHIHHDIINN
FEAFPSAIFGKCGIEGLNSPDVYPKWHFTKMFDLIAPPSDRGNKGFGSTDKE
>gnl|CDD|165396 PHA03124, PHA03124, dUTPase; Provisional
MEATTEKMALIEIGKGWAAFCLDALQCVISNEEAIIAEPRADSPVLKIDSAIRTALPPGYGIVISDTAEG
HAAAWEIIPGLVDADYTGLLGILLVLTDDGGNTLAGGEAGDGIVIFPPGGVHARLNVIKLANDDILGACG
AGAARLLLETAIDSFKGDDDLLGEGFDHCIESLASIPPDILHAKIDCPGNFGCMGCKAFYRRLFECLEEQ
PLDAACNDHIVILNGAAPENINRFAAADDIKFVAMVGHHIIIGAAESLNEDLTVELRDDDDCPAALFPFH
DIFAPKEAEDAGYDIRAPEDCTILPGGSTRIILPQKLACGKFRAAFILGRSSMNLKGLLVDPEHVQDDDW
ISFNITNIRDAAAFFHAGDRIAQLIALEDKLEFLGEPDALPWKIVNSVQDEKKNLSSRGDGGFGSSGK
>gnl|CDD|222992 PHA03125, PHA03125, dUTPase; Provisional
MYSIISEKISETITLQRQTSSRYIEFFVFRNVDINELWTTDISEDKTHDVWPAINEKSFKKFLENELTSY
QRPISLLGIPQNGTVSKTCKIEKQRETDCVNYERKYGNPVTFYPRHRAKRNANTDTCISEEPSILVSHHR
NSKMDVFMDTNKITLVNRELIWVPHDQVRIVKLDISLNIPDGFFGVITGHSNDVFCECVTEIITDETDIS
VFLMNLSEHSLMLLPGDVEFSINFLPCYIPEPWEMINLSPPEFAKFHLKTNREFIVKPNSYTIQNFDAMY
VCADELKALMIPSKEILKLGLLIETYIWNKDTIPSIKIFNSTRKTIYIPTGICIARIIFTCGHFCLSLMP
ERAINRLQVLDATSMFLFHYAAESNA
>gnl|CDD|165398 PHA03126, PHA03126, dUTPase; Provisional
MASVTNLVDSIVVVECGNRWRARAEAAGRLLVLINNHTVELSAEHGSAGEFYSVLTDVGVRVACSSGYAI
VLTQISGLLPVEPEPGNFSNVTFPGNSAKYYTAYGIVDSGYRGVVKAVQFAPGVNTSVPPGQMSLGLVLV
KLATETIHVTSIGSTEDGRSSEANLFYDYFAPKRVEDAGYDISAPTDATIEPDESHFVDLPIVFASSNPA
VTPCIFGRSSMNRRGLIVLPTRWVAGRTCCFFILNVNKYPVSITKGQRVAQLLLTEDIDDALIPTTVNYD
TPFPTYSPTGATKAPQSPVLWKFTTDFDREAPSSLRADGGFGSTGL
>gnl|CDD|222993 PHA03127, PHA03127, dUTPase; Provisional
MATSAATSTTVSDKRSILVVELKATAAAWRLLVCCEPDSLALWGPIALAAMDREAPNGDILYSRLVNLGL
RAAAPGGYAILMSQMCSGQTPSRPPAVAVGIVDSGYRGILRAIVWAPPCIETIPEAGLALRLTLARLAKT
TPRLAACDDTARAGQGAGVEVPFFETFAPKRDEDAGYDIAMPYTAVLAPGENLHVRLPVAYAAGAHAAAP
YVFGRSSLNLRGIVVLPTAWPPGEPCRFVIRNVTQEPVVAAAGQRVAQLLLLEEPLEWLPTELNDREPFP
TTPRAAPPAPMAHRLRWRFVADFAAVAPSSARGDRGFGSTGL
>gnl|CDD|165400 PHA03128, PHA03128, dUTPase; Provisional
MLTVLTDRIDSQLVLSRQHKSRFQRFWERPSLIKKDERQPPQDILAEKSVNMRYCVRFASDLDFQNVFTH
PEQHPGEDESNSPLPRPKVPYKWIPSSFIVKQCHTQLAFYNKHIIWLSRERKTPTSLGISLYIPEGFFGI
TFYKCLDAQFVCMPELIEPGLQNPQMDVVNLNYTFQAIFPGTIEGDIGVFPCFCPEPWQLMNIPPPNEHY
FFGLRTRQTIIIQPGHTQTVYFDAAYVHAPGICALIVGTRQFSQSDLIIRPTIWLPGTVATVTVVNTSST
TVCISPTTTVAKVVFTTRRFVYLLVGSHPIGQLIVPPTPDTGFTHTPEHALLQRLLACENEDVDETEEDE
KSSDAESPVNTSDVIFDVGPKPPRHP
>gnl|CDD|222994 PHA03129, PHA03129, dUTPase; Provisional
MDTGNCHPRKRVILELRSSEATSVPWRLQFRVDEAIYAHDPEGWTCYIEERDPRCLRVINNCAISLPKSD
RKRKYQICLLDLGVRVAVPQNYVVVLAKLTDPDPTSRGIPVIRVANGVIDSGYRGTIRAVLFYEKSCTIP
KNGLAIRLALVKLASPNINSRILFDLSDITPHLECGPKFSESIATAARSGSPETQPLLPPSGAKIWPGTG
CRALVCLYSDRASAATHYTSSDKNVAFAVRYNDSTVVLGLKDVPKKEAKTFVRFYTSGQFATLIPFFETF
NPKRLEDAGYDIPAPRDIELEPLSSTTIKIQQRYNCKDSSVIPCIFGRSSMNLRGLIVLPSRWLPNSWLT
LTICNLTEKTVFIKAGDRIAQLLLVDQDAATLIPPENNTTDCFPTVGKCSRPYVTYGEPVWRETLHFDTE
AMTSERQEGGFGSTGI
>gnl|CDD|222995 PHA03130, PHA03130, dUTPase; Provisional
DSQWGAPAILIAPNGATRGAEGDWRVGVAACASSVRLSLANRREVAFTPAGGGASGWAVGRVPLDLRVAM
PTDFCAVVHAPPTAGAPYRVALGLIDSGYRGTVQAVVLAPGETRRFAPGELRVDLTFLRVSGSPLGLTEP
AFLCSFPGLKRPRRTEPGAPHANPWLGRALAARGARRRGGSVTYAGELREEAPGEHGDGAVEAPAFLPKR
AEDAGIDIVVHKRVEVPAGGTVVIQPSLRVLLAAGGPEAYYVLGRSSLNARGVLVTPTRWLPGRQCAFSV
HNITGAPVTLEAGSKVAQLLVAGSDALPWVPPDNVPGDGALRAYPRGVSPARATPAPPALPCLVFTAEFD
AEAPPSERGTGGFGSTGI
>gnl|CDD|222996 PHA03131, PHA03131, dUTPase; Provisional
RMAQRPEVYYAFEPSKFLITSPAEESRLTLVNKTPILVRPGEPTVVPLGLYIRRPPGFAFILWGSTSKNV
TCHTGLIDPGYRGELKLILLNKTKYNVTLRPGELKVSLLAFTYATPILTDDSLLNPPQYPDDAGFDVSLP
QDLVIFPTTTFTFTLSLCCPPISPHFVPVIFGRSGLASKGLTVKPTKWRRSGLQLKLYNYTDETIFLPAG
SRICQVVFMHKDHLPSFFNPLLSARCLGPRILFRWARVSFEDIPKDPCTSSKTLRQSEDGDSDPSRGTKG
FGSSGL
>gnl|CDD|222997 PHA03132, PHA03132, thymidine kinase; Provisional
GPGKPRGQPGRWNYDSSDESPEGSRDENFDAERDDFLTPLGSTSEATSEDDDDLYPPRETGSGGGVATST
IYTVPRPPRGPEQTLDKPDSLPASRELPPGPTPVPPGGFRGASSPRLGADSTSPRFLYQVNFPVILAPIG
ESNSSSEELSEEEEHSRPPPSESLKVKNGGKVYPKGFSKHKTHKRSEFSGLTKKAARKRKGSFVFKPSQL
KELSGSLKNLLHLDDSAETDPATRQVPVPVHVLYPPLLTEYVPYKPACFLFLEGVMGVGKTTLLNHMRGI
LGDNVLVFPEPMRYWTEVYSNCLKEIYKLVKPGKHGKTSTSAKLLACQMKFATPFRALATRTRRLVQPES
VRRPVAPLDNWVLFDRHLLSATVVFPLMHLRNGMLSFSHFIQLLSTFRAHEGDVIVLLKLNSEENLRRVK
KRGRKEEKGINLTYLKELNWAYHAVYCAWLLLQYFTPEDIVQVCLGTTTITTVCHSSGTVAIKHLTAEKL
WKNSIFNTLRDVIQPFRHDCTLLEVCLTFCKELSKLQFVVVDASEFQDDVPGLWTEIYTQILKNPAIKTR
FVDWAALEKLISTFNSQERS
>gnl|CDD|165405 PHA03133, PHA03133, thymidine kinase; Provisional
MASHAGQQDAPALDRAAGSPGHNNRRAASRPRRQQKASALLRIYVDGPHGLGKTTTAAALAAALGRRDDI
EYVPEPMAYWQVLGGSETIARIFDAQHRLDRGEISAGEAAVAMTSAQVTMSTPYAVTEAAVAPHIGGELP
PGHAPHPNIDLTLVFDRHPVAPLLCYPAARYLMGSLSLPAVLSFAALLPPTTPGTNLVLGALPEAAHAER
LAQRQRPGERLDLAMLSAIRRVYDMLGNTIRYLQTGGSWRADWGRLSGAAPAAESRRPERIGPRPEIEDT
LFALFCAPELLDPTGELYRVFAWTLDLLAERLRPMHLFVLDYNQAPRHCWMDLMELTPEMTPTLVTTPGS
ITTLRDLAREFAREMGPA
>gnl|CDD|177537 PHA03134, PHA03134, thymidine kinase; Provisional
SASGAPPRRQVRIVRIYLDGAYGIGKSTTGRVMASAASGGGPTLYFPEPMAYWRTLFETDVVSGIYDAQN
RKQQGSLAAEDAAGITAHYQARFATPYLILHDRLSTLFGPPSLARGGRPDVTLVFDRHPVASCVCFPLAR
YLLGDMSACALLALAATLPREPPGGNLVVTTLNPDEHLRRLRARARIGEQIDAKLIAALRNVYAMLVNTC
AFLRSGRVWRDGWGELPWFDATYRHRLAQMDAFQERPSPELRDTLFAAFKARELLDDRGVLLEVHAWALD
ALMLKLRNLEVFTLDLSGTPRQCAAAVEALRPLMSSTLSDSASGSTLERAARTFNAEMGV
>gnl|CDD|165407 PHA03135, PHA03135, thymidine kinase; Provisional
MASQMTSAQLIRVYLDGPFGIGKTSMLNEMPDHSPDGVPVLKVFEPMKYWRCYFTDLVVAVNDTPERRRR
GELSLFQSSMIVAALQAKFADPYLVFHERLSSKCHGKIGTRGNPSLILILDRHPVSATVCFPIARHLLGD
CSLEMLISSIIRLPLEPPGCNLVITILPDEKEHVNRLSSRNRPGETTDRNMLRALNAVYSSLVDTVKYAN
LICPYSKDEWEMEWLGLPWFDESLAETFISRPRPVYSGSRVSLDHTLLAIFKRKELCSEDGSLLTQYSWI
LWGLLMKLRNINVERFDISGMSRRKCAEAIMDTMPERLSTHMSWNDLFEIEADVIAYNKEMCN
>gnl|CDD|177538 PHA03136, PHA03136, thymidine kinase; Provisional
MALADACERLIRRAFSSGGMPFCSEFENDDSDFRRLVLLYLDGPFGTGKTTTAKLLMEMPDTLAARLYLA
EPMAAWRNHFGGADMIKEINEIQELKARGDIACRDAKAIAAAELQLQFAAPLRIFHHVASNLFGSERCYS
AAARGPDDILFIIDRHPLAACLCFPAAQFLSGALEFGDLIALISGIPDEPHGGNIVIMDLDECEHAERII
ARGRPGEAIDVRFLCALHNIYICFMNTITYAKQAPIMWDADKKDKDALSSAIFDDDKKECLEAADSPEIV
GGKKNPSIDQTLFAIFAFDELCDEGERLKKVHEFNLQCAAIKLADLCAFFLDAHGKSPEACAAECLEAAE
AADFLRLKFAAAADLEDAVEQYNADMGI
>gnl|CDD|165410 PHA03138, PHA03138, thymidine kinase; Provisional
AQHDKCDDKMCILRIYLDGAFGIGKTTAAEAFLHGFAINPNRIFFIGEPLMYWRNLAGDDAICGIYGTQT
RRKNGDISDEDAQRLTAHFQGLFCSPHAILHAKILALMDQNPNDLALKFFKEPVAIFLSDRHPIASNICF
PISRYLVGDMSPAALPGFLFALPAEPEGTNLIVCTVSLPNHLSRISKRARPGEIIDLPFILVLRNVYIML
INTIIFLKAKNDWHADWFKLPFCNDSFKQKLQEKECIKIQENPGIEDTLFAVFKIPELCDEFGEILDLWA
WGMETLANCLKNISCFVLSLDQTPQDAAIELCKLLPNMTPANLSPGALAILKELSDAVND
>gnl|CDD|165411 PHA03139, PHA03139, helicase-primase primase subunit; Provisional
MTIVVFATEYDAANVIFSILCRSPSEHLIFPIIVKYKPSNNVSFCLQTQKCKNSKRIDTVFVCHAEKLNL
SHYIQTASPIKAEDVANSLNDKETENLYVDMILSQTGKESEDVEFKYMAYFHKSLIIKYLTGKFLLPTSP
FWFLSTYGQTEGMLLLTMYYYLFEEQKSTITTTKNYVQCFTENTGDMVFTYSSMSEFINITLKSKFRKLF
ADFSTYARQKNLRDKEEFKYLDTQINLFRKSSHLTNTFRVHYIYIAYNTALETTKFVNYCNLTSYDSNLP
IGQQCQRNMHILGNSLHENLLCIMKQYFNADCYFKTYIDIKRLKNPKLNVTEYEYALNSKKKTIQALTSE
QITRAIAKCNKNGEGLFSPVKPGLQGLLEISASDKYVQIQDKRIYRRQHLHKDYHRPFPVFRVQLLHKNI
FCFGNSEDWYENMGFNRILQYLPDEYISDEALTRAIWLQDTHFLCDDIEKQFYTTRHEIFNERIPVTNYI
GDLDLPLQDTATITEETFFSMCRLIRLTLINAWKKIFPSIDTDTHPIFFFKTQCDTTNDPLDYTEDPTEI
KQFCVCRKKIGLRISIPLPNGTAIAGGEPLKQLSKILNHVMCLDQELSQILNSVTFPGECFDIGIYHTGH
CIRIGYMYKTDMDKGKMLHGRLTPIFIVPEGYRNSCKTFIQMQMDLNNLLHHGTKKAPIEELIYSITDKG
CPKENLSFMDLKSRQLWNKVNIATETLITKYLNTHGFNNNATSADDSLLSFIRLIGWPIIKTQLITHYET
RIAQQFSQVTFLKIDSKNLQIKKTQFGRVSDFSCLNRQHRGNRDNVLVYIQLKADGNRLILILWSTCFAT
KCQSNSKQVHCSIALEQLKN
>gnl|CDD|222998 PHA03140, PHA03140, helicase-primase primase subunit; Provisional
NETNCMPVSYETGCICAASIYSAWTQGGDRAREYPYVLLYLLCKRGDGGYDPVFAEITVLAEDLCRYSRH
AGDVTAATLASLCRAASSAAPDAWPLEPLGNADTWRCLYGSALATLRRRLGFFSFYSPVRFGTDTATGLL
VKAEPAPDATADAAPSTGVLRAALRVAIEESAVRACAAAAPGGSLAYARLCALKDGHANAPGTALEFELT
TKTARIYRSYASIFSPPRERAGRLSDVFNLREYRVCTSGGRATVVRVLLPVGFDCLVTDARVTSPLSALL
VYRQWYAAAFGKPGGPRQILAYLGPELSPGGEERDYFCTVGFPGWTTLRTSTPDAESVRDALEAYVETDG
LWPVTGIHAFHYLAPWDFHPPLPVAGLDRRIAAARRALPAGGGSGDGADWPAGRISTILDSPVCVRDLWL
AKFDFSAFFPTIYCALFPEHARLARIIRARRRRGRPCLKPALVTFFGGLRHIHPPAYKAIIALANAISAC
VERAANERNFAICTYVKDGFWGAFGDLVPGAVSRDAARAAALALRDDCERAVEAVLRDDLGLRPAEGAEP
HLRFEGVFTHAVSWCTTGYWLWNATTGESEHLVGVPCRSEAARDAKESLAGLLCRAVAIRERLYASTWTV
SNYITWPGDTVAAAAAACDALVHAAFERRGDVRYWSATAPIGDWGAVPRSALSGGDMLDKDHKPRQYVLV
RGHIPEAAPFPLPWTLYRAPVCLPPIDCRAHLAPLLQTFARMINGALAAGNDFGEPPTKFEYDLADYDFL
FA
>gnl|CDD|177540 PHA03141, PHA03141, helicase-primase primase subunit; Provisional
LPLYFANRHNTKFWLVPRAFVTSKPQKPPIPSDCLAPTLFLLTTEGPVCWHQKLPLPLNIDFAAYLHEAL
SVFSKVGGEAGTINKETDHKLEGFKKILCLL
>gnl|CDD|222999 PHA03142, PHA03142, helicase-primase primase subunit BSLF1; Provisional
MSAPPVVKALFATDGDCAEAIADILTGTPTSGFFFCVLHNCFSYPILGEEVSLSLCLPAKRPGGGERCLE
VFQLRLPAEEALPFLFGGKPLTADDIQTYLDRAAALKSFKPILELLTLSGKKQQPQGDFKSKVAWFRAKF
VNALRKLYKMTPSPYWMISTFGSFEAQFVLVSAFYFFEKHECTVETLSHLARLFSPKQGQSLAAVTTLAE
LGEVFGTSPWLDRVPAFAAYVKEKLARDSLESEAIDRTINEFRGQLMLSNQDLVHYIYLSFFQCFNKQTF
LRYSRLTSPDNINTLPPEGPILTRLLDEEFKEKMATYYNKSTYLSTHVRIRSVKLPGPYGYDPDPCDGLL
RAYWAGQSRDVAALLKEINVWHPHLCLPEELQGLLDLAALDTSSGVWGNPKDFLFPEALRLPVYRCEFLN
KHYFVMVAADNLEAYWKKHVLLPTDSNWCGLPDTRLTRAITYTELYYSLNTLKEQLLVSRHEYFNPRLPV
FNLVLDLDLPIKEPGRTLEEIYNLCLTLRESILDVLQLLGPVEPDHPVYFFKSACPPPEEDNMEDPLPFC
TCTKKLGLRIITPLPRGVAIVGSEPLISLVKILNRTIKLDKRLREMYPKIQETEGPFDVGIYHRGRCIRL
PHTYKVGSGGGLERLLKLFVCHPEEPDKRSYVKNALNLQNLLHHSLSVGWPGPLKFVYHIEDINEDFLSQ
KTQEQLPRTSENVAEKIETLTGLDLTDWVLSKVWPKLFDTIKSYFPEDKLQQFLHVTFEQTGHNIVQVKP
LRGNNFSCLRHNHRNKSKSVRVFLVLHLTSEDEVTVTFMSQCFANKCNSNKPTAHFSVSVPISRK
>gnl|CDD|223000 PHA03144, PHA03144, helicase-primase primase subunit; Provisional
MMEDGVAWAEGSVCATSLYSLWTPPRTPDRLHALVYLLCRDAAGDYTARFAEVSVSSNELQTGFRGPADV
TAARAVAAARAAAAPAAWPLEPLGDPALWKALYASVLAALRRQVGRFAFYSPLRFGVDPQTGLVVRIEPA
PGGGEPAAPRAAILNVTAKVDLDPLALAAHAASSPGASLARARLAAIRDGYFTPSCASDASLEVEITTKT
ARFAREYDTLQFPPVKREGAMADLFEVRERTLRPRGHQRVTARVLVPRGFDCFVACAEGFSAPALMALYR
QWHATVFAAPGALVPIFAFLGPELEPRGEEVDYFCVLGFPGWPTLKVSAAAAEAVREALAAYVLLDGLWP
ALGARAFHPLAPWAPEDRAAAGSLTPRLREAAARLQNGLRDKWPAGRVSCILDHPAVIGGVWLAKFDFSA
FFPTLYLALFPGHERLARAVRARARREKPWLKAALVSFFGGLQHICPAAYRALIALANAVSRALERAANA
VGFAVCTYVKDGFWGVLGVDPQDAVSADALAAAERARAACQAAAEAVLADMGLLLPEGAPLHLRLEGLYT
HAVSWSQHGYWLWNRRTDTEDFVGFPLRSAAARAAKAALRALLRAAVADSADAETLRQAAREACDRLVLE
AFARRLDAEFWSVPTPISDPSDPLPAAAFRGGALLDADHGSRRVVRVCGGDCEPVPVPWDLYPRPLVLPP
IDCAHHLRPILAEAESMLNGALSALWGEDEPFEVTYPFEDFAFLFA
>gnl|CDD|165416 PHA03145, PHA03145, helicase-primase primase subunit; Provisional
EARAAGPPVEVTALYATDGCVITSSIALLTNCLLGAEPLYVFSYDAYLPDDPTGTASEQARYERSLALYR
ASGGLSGESFRVTFCLLGTEAGGVGHHARARGRVRPMFVCRFERADDVAALQEALGRGAPLAPAHVARTL
DAEATFAIHTPLILALTVAVNGASPRTGRTAAAAEYAPGESLRSLVARAPLGQRGLTTLFVHHEARVLAA
YRRAYYGSAQNPFWFVSKFGPDEKSLVLVARYYLLQALRLGGAGATYDLQAIKDVCATYAVPHAPRADAP
SAAALTSFAAVTRFCCTSQYARGPAAAGFPLYVERRIAADVRETGALKEFIAHDRGCLRVSDREFITYIY
LAHFECFSPPRLAGHLRAVTTRDPDPAAATDRPSGLGREAVERFFSHVRAQLNIREYVRQNVTPREAVLR
GATAEAYLRARTYAPAALEPAPRYRGAVDSATGMLGRLAEAERLLVPHGWPAFAPPKPGEGDGGATAPPG
CGIVRRLLRLAATEQQADTPPAIAALTRDARTQTPLPVYRIAMAPRGQAFAALARDDWARITRDARLPAA
DVSAAAAAAPRDPGALGLRLTWRVHARNPVTAPPTGPTAAGQMYVNRNEIFNGALAVTNIILDLDVALRE
PIPFERLHEALGHFRRGALAAVALLFPAARVDPDAYPCYFFKSACRPRAAAVDPGLGPDGEYDGDGPWFP
AGGGPGDEEDDEDPDAEALAHGGVDEEAAYLDALHEQPPAEAAPAEPESPRCTCADKIGLRVCLPVPAPY
VVHGSLTMRGVARVIQQAVLLDRDFVEAVGGYVRDFLLVDTGVYAHGHSLRLPYFAKVTDEGLACGRLLP
VFVVPPACPDVPAFVAAHADPRRFHFHAPPATAPDAGELRVLHSLGGDYISFFERKASHNAIEHFGRRET
LAEVLGRYDARLGAGETVEAFALELLGRIVACLETHFPEHAHEYQSVSVQRAVVQDDRALLQLVPSRGGL
QQGLSCLRFKHGRASRATARTFLALSVGARNGLCVSLCQQCFASKCDSNRLRTLFTVDAGPPPCSPCAPC
GTSPPSAS
>gnl|CDD|177543 PHA03146, PHA03146, helicase-primase primase subunit; Provisional
MAPANPEPTIRVLYATDGCAITYSLMLLTGQEPSEGAYVVSYDWSSELDDLFGGQGDGWDSTEQSDPDDV
AAALLERRPSVSFCLLGGPVGGASEAQPRVRPMFVCAFSTATGARALARTLLHGHPLSARILLQALTEGA
TFALHNDLILALAITTEQVTPRTGRTAAAAKYDPQRGSVKAALRAHSTGRRGLTSLYIHHENKTLAAFRR
LYSNNNTTPFWFLSKFGPGEKTLVLATRYYLFQAIRSGDGGTYDLQAVKDFLATYNVPAPPNPSGLDLTH
LTSFAALSAFCCQSGYARGPVAAAAPRYVDLRIQADVAEVSALREYIAHDRQSLKVSDREFVTYVYLAHF
ESFNRRQLYEHLLAVSITDPADIPRITGTSSLKERAIEAFFRHVRAQLNIRDYIAQNVAPAVVRLPPAIG
EQYARDRTYAPLATTMSTGNAPRGICDTATALLKLLDRVESSLAGHGWVQTSVSANKPQGVDAAPPLDAP
DGEELSPGVPSQCGVSRRLLELAAAPPRDGAHLPLEVLFGQRGTAGPAPVYRVELPSKRQAFAVIAGDRW
ETVTQNAALDPGEVAYEVAAALAGAAEMDDDALAERDLQLTRAAGGVCRTALASSNPSAQMYVNRNEIFN
ARLAVTNIVLDVDFRLKRPVPLGMLHLAMRGFRRGILTALALLFPEAAVDWDAHPCYFYKSACPPAAARA
LAAGEASSLSDYVDGVEECYMESDFLDDYAAMEEDEGWDDYEMAVAREGEAQYACDDVEVPAGGTPPNKA
GAKTPLQRAAETDACGCTEKMGFRVTVPVPPPYLLAGPEALRGLARIIQQAVVLERTFTESMCSYLRDFS
FVDTGVYSHGRSLRLPFFCKVGDSGEVYGGLLPFYVVPPRCNDVAEFVAAHSDPANFHFHAAPRAPTVTH
VITDLGGEYVSFFERKAARNREAFMTKRATLESLLSSVNVSIKSREAVEAFVADVVLAEVVPHLAAHFPQ
AAGEYQGAGAHTVVAKPDWILAQLNRSGAAYRSQGFSCLRAKHLRSARGLARTFVSLSVDAHDRLCASLS
QQCFATKCGSNKMCTIFTLEVSRAK
>gnl|CDD|165418 PHA03147, PHA03147, hypothetical protein; Provisional
MPEAIPNILYVSREEDGRIVEMILTEKRKKKYVYYPYTNPWVVETEDTKDAFLSNSHNIIRMITYCLFYL
QAVIYLALYLWPLNPYRVPGNSVEGGLGQRVPPTVVHINPAEIFEGCDDAIFCKLPLPMPIINTTHGRIY
PNFTKTGGSPANYKLALERLFGLMNNQQCNGEIISQKETQFASRNHTEFENLKAMFILALLVLQKNCHPE
AVEIVKGKIKLENYGINYPQSMPQYFTPCNASWEDVINNTYYAFKGSCDPCNINYLWRNLSHVPYIINFK
>gnl|CDD|223001 PHA03148, PHA03148, hypothetical protein; Provisional
MLKIKDPGARLVGGAVHLPSGTYVFHVIHSPSLASALGLPGSDVPPPLLFKRFGTTVSNSLPLYSTRNPI
LSLLRLMLSPHPYILNSHLCVGLTQYARIFYAISLKTPKLGNCPAAPYNTVTIMNRSHNSLRLVPSLDIN
PLQHLFLKHVLLKRLGLENIVQDFEALYGSVLPPVSPEQIESFEKLVEETKRRVEDIVFCLNSICAHSFR
PRVRPDVTNPVLSLAMEKYFLMFPPKDKKNAVNFAASIVEIICQGAPFSKVLQFLAKYIDIKKETTMTNL
IKIYALLTI
>gnl|CDD|165420 PHA03149, PHA03149, hypothetical protein; Provisional
MGTLCSICKRRPNPLDTEGKVINLPDDFEELSETEIMLACPHDKKLCKKNKESMYKTKHKSNKHDI
>gnl|CDD|223002 PHA03150, PHA03150, hypothetical protein; Provisional
MARINALDCHVLGIYFYNVILEKKLIIWQVNLITCGIQHESAFCFVVDLLSNTDRDSIPALNSHQPTIQE
HGVNLMQWELKLRLSNPIIQTLMSNQPGPVNVLMSTDKVVLEVRPVALKHACSGYLKGAYLYCDCTQTFA
LVSKVSPTRMIDFWYPYMLSNSTVEDIEVYIKCTEGLYYCSSSAEPPLKKTQDGALGIEDIFKIEDHSFQ
VAKQKYTLRTAIAIFHLLWVNVECKWNGCLPEFFRALHNKVFGDFEGIAPTLTYLFPGGCPEATPFDIYF
CAFPFVNLNFGRPRRIDLCAVPRLHCPQILLSWPPNKDSILGDDLLCPGIDIPLPSTPPIWPLNVEDVNS
KLCEEETEEVARINDPHIIVEIDFLSLLCHHLGCHRAFKKDEIENIIKFGSSDLNLFLQTWYNWFISTIF
KWAAARGLTWAAITQTKVYLKSPQLSSEVSKVCPSL
>gnl|CDD|177546 PHA03151, PHA03151, hypothetical protein; Provisional
MAMFLDTEAKVSFSDKDRRKLAPLPGAPREKLTNVFKFPTDEDDSTPSENTKAESSSIDEDGLLTSSGSD
SVFNSTDYESTPEPSKTPGFSDSNVSDSNNDKDFDFKPQDEDTSSDDSSAPDFITSLVSSDCEARGLSSS
EEDGEPYSKQKMSQPLTIDAKTEEITSEEDCCVQEDSSDSEEDVVEAFIRQRAQMAGKKKKGKRSISTSD
DEPPRKSRRKRHSHRISSSTDSDDEEPRHKMTGTPPMTGNKCYVWPWLN
>gnl|CDD|165423 PHA03152, PHA03152, hypothetical protein; Provisional
MKWLLFGALGCICLAKILDAIIANPCCKIFALNETLIPSIYDINWIYITDPHTCGGFSIAQVFQRRSAQH
MSTLYVCSNGFNVISFLLAVLKKLPLNAEEQNFKNHLITLQNSFLSKLGPDTTGAIKFKRKHGQLAKT
>gnl|CDD|165425 PHA03154, PHA03154, hypothetical protein; Provisional
MSRLYQPQRYSLISDLHKNFHYVDINVIKAEFKNVILDTVVPKFSQPATHLEKGDFLLKICQLLMIHREE
EQEIINKAKSNIIYFLNEILNAEYGEVKELAKNILCDVEIDKPDCELSAYLAQEIPKLIVLKYPTHFKVC
EEIIPNGRWCLHNLLGIEPYYKDFSDIVLHDPEISLGSVHAFSRLSKCLFWCDSFMNKIYPCNAFNSSIN
QVVLWSTMFHFYSIAHCNDCINESIGFTEALLKQEVSAFYEWCLEQEDYEADRMAKFIKFSADQITILST
HTDLQGLAEYIYSYKKCFINRRFD
>gnl|CDD|165426 PHA03155, PHA03155, hypothetical protein; Provisional
MASGRACADVEELEKELQKLKIENKALKKKLLQHGNPEDELLTPAQKDAIINSLVNKLTKKAEEKIRERV
LKDLLPLVSKNQCMEAIADIKYRIDVSIDESQDLPRKPACKLKTK
>gnl|CDD|165427 PHA03156, PHA03156, hypothetical protein; Provisional
MTRGLFICFLIFFKICLRAAQLTDKAATTSGAILHNNNFYSNSCSADTFVPSIKTFSSIWAILNGIIFFC
ASLFFLRHLCFVKFISHLTK
>gnl|CDD|165429 PHA03158, PHA03158, hypothetical protein; Provisional
MALALKLKKHLLYRISGPPPVWANFKFGIIILIMLCLALLTDSEPIPTPAAPILNITQPPSLNITHTLEA
TIFSTSRPNILEPSENCKNCSTFLDLFWQQLGEGASIKDLMLNLQLEEVHGLKWPKSSLPLANPNSEAEA
QKLQLPRNLLPTAVGPPHVKYKFGNRLWEAPKGADVNGKKIKFDDPPLPYTGAYNDDGILMVNINGKHVR
FDDLPFMERIKRSGPPWCIKTAKEKAAILKQLLKAAKKCCKNSEHEKELEEEIEELEKSLAKP
>gnl|CDD|165430 PHA03159, PHA03159, hypothetical protein; Provisional
MSSIKFQKIIENILKECQDCHHQQDSIVRAIHSVIHQYNKFEALMPDFSICAHDRIKFTGEAILLTTEHN
TNWGKVVAMISFSAAALQTIDEDYKCVATSMLSSYIAKSVGANWFIDHGGEKGLVEFCDSILPKNNFNFL
NFLLPAILAGIILIGTLLIK
>gnl|CDD|165431 PHA03160, PHA03160, hypothetical protein; Provisional
MPIVYVAGFVDVVAYPKVDPVLYLNLDDVSKCLPLAKPIPLNIEHLPESTIGHTIGLYAVTHGVFCVGVI
HSEKFLHFAENLFSNSCVAKATNKFLPHQPLLEILHTWLPALSLSSLCPNAQNAANDNMFQHVSLCALGR
RRGTVAVYSMNLEDAISQFCSISQAEVENIYQDSKNIDINSLPKPVFNIDPHILMAKAIDAGFIKDRLQL
LKTDKGVAKIKKLTYLKASEIGKLGIEDISEDMNQHGITPQGSDDLISVPKSTFLSMLQNNLDNFKQHPR
PACFPPYFPPQGAYMPYELYNHPPYLGDNIGYMLPNGSYVPAIFPSRPNKRKREDFDDCVFPGESSLYKD
VLNLTKNISQLQDDLKDLKQAAINQPNRIIPHHFSNPYSFDPGHAPFFRYAPYGAPKNDHHLLPPLACSQ
QLPMQPLHVQQAPMQAPHVAPPPMQPPHVQQPRVLPSTDGASNEAPKPSAQEPVHIDASFAQDPVSKIQK
LFCDELLNK
>gnl|CDD|165432 PHA03161, PHA03161, hypothetical protein; Provisional
MNSNKKEFLCSAFEAEINKKASVSLFDRFGEKNCIFLHQLDHTKKSLIKHENLKKQKSIEGMLQAVDLSI
QEKKKELSLLKAFDRHKLSAAEDLQDKILELKEDIHFEIEALNHGQPSSQEEENSSENSIPDTIMQWRIE
ALPRVPSATF
>gnl|CDD|165433 PHA03162, PHA03162, hypothetical protein; Provisional
GAGGSKKCPKAQPTMEDLAAEIAKLQLENKALKKKIKEGTDDDPLPGDPILTPAAKEAMIGAATAALTRQ
AAKKIEAKIRHETLKATTKEEFEAAIANIRFRVDLSMADLGGRASSDSLKASKPKGRGKHAAEKQ
>gnl|CDD|165434 PHA03163, PHA03163, hypothetical protein; Provisional
MAMGWARHGIFLLICLCLLDNVSQVLCQNNSTTPHDFDMFHQYDCNADRFAPQLLSFSSIWAILNVLIML
IACIIYCIYMCFNKFVADMTKL
>gnl|CDD|177547 PHA03164, PHA03164, hypothetical protein; Provisional
MDTPRTPPPSYSEVLMMDVMDGQVSPHQENDTSFVECLPPPQISRTAWNLWNNRRKTFTFLVLTGLAIAM
ILFIIFVLYVFNVNRGGT
>gnl|CDD|165436 PHA03165, PHA03165, hypothetical protein; Provisional
MLLISKTLFPIPRGADEFWEGTYILVVAFVLAFLVYSDFLSNLSPFGEILSSPCIST
>gnl|CDD|177548 PHA03166, PHA03166, hypothetical protein; Provisional
DSASSRLCRKPEDLRTFLQPSSPFRSVKMNPHAVIQIRRSYLKNSRFATAAGKYGIRGLTLPWDLAVWGL
LRAIPLVPDPNPFRWPNAAAFARLLARVEFRPEASDVAKRMARAVATGQYAVSTLFDYKYPGSLSHYLRF
LCYETEELYRRLEGASSTLSLFLDAEDRELIQRCLPERLCRQLGVPYSGHRQAVFFDDEYYARVEAALER
LYDRLCECGECRDRRVERTAAARARANGDKRRLRPRDGARFEEAELRLENYPELGVLRLPAIRHLSVDEQ
LRVCQSVRRDLMYDKGFGVWSQTLVDDYLPLPFGLACGLPDRAYALYLASNAVFLLFLIRLLRAVIRHEQ
RACVRLLSGLVQELSRALRRQADLLRKGGLAQSPAQRRELSRLRRHVHDLKRLTFGGGSVGGFLEAFCDF
LKLVTAIPDYRALSERQKREELLLHTFFLRRVYDDPSLETFRGERLVWYYLRHGDASPQDPARLRAFVVT
LSDAELSNDRQDDWNANRCRRKAPFEEVDTIRGISVRYQTHIMEFERLYVRRDALPPDYTSDGSSGGAAK
GRSGSDGERFRPHEVGGHAT
>gnl|CDD|223003 PHA03169, PHA03169, hypothetical protein; Provisional
MSRQRRKAKRSRHTLRSSCRGHCKRHGGTREQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTE
SDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSP
PSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDE
PGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHRSHSYTVVGWKPSTRPGGVPKLCLRCTSHP
SHRSRLPEGQQSEDKVPRKYQARRRFFRQVLPSILPPRPGPWCWVVFCWGDPYSLYRLSRCLQFPGAVSS
GVQTFPDAPGSPVIWAYCITVFCQSRGTAKAVIKAQKKYEKKYPRSAHLKASLVRMSRGLPIQ
>gnl|CDD|165441 PHA03170, PHA03170, UL37 tegument protein; Provisional
MKKLTMESLFVYLFVMGVCFTSNLTCEQKIVLIQENKLEAICISTCYVNGVLAGNSSCVSVRTSYLINLA
MLTEGFKAMSVGNITSISEKTAFLRVIINYYFRGVMLRALIAKRLPNAARLSSTVNCWLEGHSAGGVMTL
FYGTERIVLQSSTEINASKWRSDGKDANGTLNILNERVSLDCYFLSMICPQLSDEIYKKKVLHPKYFSLI
KNDTIPKKFLRNTWKSAWLNWYKYKEIEDLLDFSNDYENFSEITQSMSAAGLFFLAGGAFTMLLLLCCLS
MITRKHVVKDLGY
>gnl|CDD|165442 PHA03171, PHA03171, UL37 tegument protein; Provisional
MSLPYVHLLGGVGLLAFWYFSYRWIQRKRAEDPLPPWLRKEKACALRQQRRHRLQRQHGVIDGENSETER
PRDLTAALFAEAGEEAEEEDNDRECPDTEAEEEDEEEEIEAPDPEVNPLDAEGLSGLAREACDALKKALL
RHRFLWQRRRQARCEQHNGPQQSHHAAVFCRVAEKRGFQVFISLLALLSACVLTGHGVSAGCTYHAPDIN
TDRNAGFMNCKLNCTCNGTQIYCGPCAGAEKALPLNMTFPRKGNRHWHARMLNFGFQFHLEGLFPLRILN
ESDLDINVSEVDGAIACNTSFIDDRNITMGLLTLNLTTLGIGYVLRAAANTDPFERHVNWEETNVTDNAN
DSDNATDTVKSVLSRHAESDYIFLQDMCPRFLKRFQKLAKNNIRNTTFNGGNNNSLAEWTLNDCEGWGMW
SKLSIMWKNRRSAFLRAKSRALGHWALISICSAAAGSIAILSLFCILLFGLRRDLIEDFRYICQDDDHFF
IDNDVDNAV
>gnl|CDD|165443 PHA03172, PHA03172, UL37 tegument protein; Provisional
KQACKDALAACAAALHSACKKDTSSGSTRNSAPELTSALADILISRDDIPLEDLEATEARKHLAEGIFAA
CKLAPFAVADVALKLAARAIIRRISVPWNAGEDFRIIQRLREAFLGLQDDFDNASKKEFNALFDPCSEYK
DLIGGWLTEFGNAARLTMDEQQLFDDAGDRLEPPELLAPLIENYPLLIDHQMVQDGIDYLGGKLQGLVAY
HALLNCATAPHELGKTKALAALSMVAEYFDPETKPAYRKFPQKALAAFDLDLTDEVVSSLVYDDAAAPVI
AKDLDSLPFSESLLFAEAARSRDMLALLQPSATWEGSGAALRNAAGDAKKRHQQAAPGAGMAWRCDLDAL
FSIPIEHLALDVPAIMQLFEDAPNDIPAEQEEALSAYATDTADAIAKFPDLAASGGPEAVIRSLALRGFT
KSNCELYIFAAEAFLEEDADGTIIGDFLAAVIYASLIGLAAHSLYAYNPHTIFYPEHYAGLIKDTGDAHA
HLLDMMGLAESDALIPLRAFAPAPPHNAFNIIRDTLAAFIDGSDGGAEAFGDLGVFDFVQHLIADFGGGI
HENEDWLEERDAAIRQRMEIAAADKGEADAAGQRPGLGFDELAALVQAIEIGGAEPEAICERAGADAGAA
MAGALFSALFAAAILRDIMEAAAAIPFEADALAHANKALSGIEDFALRWKMPDGQHYRRAIIAFQAAIHP
FITGKIGTDAISIEQARAIEKALGDISAACDRSFDALPEPFKGGLQKAAAPDRMHSKFIAQAFENAAMGD
LEELSKTLAKAAEEISKAVQDLLSKLANARDLFSQRANADDKGAVSFDAAGPDGKELGHWEDDSVMQAIW
KAVNFAEAAIRHTEKAIRALDATKRETHALEESYWQLAGGRDGAGNAAQPREHICQKVAAELSEIADARN
AVVQRARSLCRAIAGTGLKRARDFVKAWKLFLDAEAALAKQ
>gnl|CDD|223004 PHA03173, PHA03173, UL37 tegument protein; Provisional
PEDGPLQALLDALESLSGETDSADPWPPAAAAEARAAISEFLLSTGTISIAQVRSLWRPLQELACRAYAA
TGTPEAAMLAENLPGLILWRLSVAWDDESAFEAMDRLRDLVLVMTGEETTAWLTAAGLRTSAAFGPSNMR
RLVSEWIDRFEEAVTSALAATPDVLLSARRGMSPEESAAPLLTHPRFALIYDMPFVQEGLRFLARAANWL
TPFSIMVRRTQDAALTPLTRALFTLALVDEYFPTRDRGATAPSRLLEQFAEDVREIDPAALVPPGEANAT
PRTAYEVRVSAALAYQDPFVRETQPGMVAERVRTDADILPDDPLLSSSALAIHVPAVLRLLSSGEPDDAS
AAAKARVAEHARQTWEAIQASTSPSQVIEALIEAGFTRQHCRLLERALEDYLSRGRNRRTPEGPALDDAQ
QVVGCVAVVGGVVFGLLESYGPGADYVRAYTRTISALEPVYGDLLEALGLPDGGLEQTLRRCMAPRPPTD
YIAAARAALVAEIETAERRFTVGGGAGAHSAARESLLTWFDFRAQSRWGITPPADATPSSALLRPAAPPG
HSESDLIAAATKIRFPADAPPTSVLDDPSFAPYILATVVLDALSATTTASFSPRSIAQALRVLAWARDYG
AGYIPNVDGYRTKLTALIALLEPFADAAAPVPTTAHAENIEALLGELHSVVRAAIELLPPEVRPPVPPRP
SVSNSLFLASMYATALRGRLQDLAARTDALVDSIADAIVLLASHMLTLKAFFACRFESVGGGQTVTIYAR
GGERAPRFGTWRLADVVDAVGGYYGEYNDARADLRADLAALRTVIAETTAALQECEALAAQTSGDSAGNL
FSTLLADHAGLTRLQTGLALRAGKLLSGSEVPGLRHVGTFLARWRRLSAAYRRARDSTGERDVASLVEEL
RGVWDGIQEDRALAAPAPRASTADDLEAAVLELMGDYPEVAPPDSDTSGVVLTSRHNLGDWDDVNLGPLR
KRTVAPDDVDSANALADLLTKPWLTMDDLLAEVDGVFNASAFAPGAGP
>gnl|CDD|177551 PHA03175, PHA03175, UL43 envelope protein; Provisional
MEAGNKPRDRIPCITNMPADTRGRTRPGRPASNPQRRPACIGDFRRRSASLSFLDFPDDAAPEELERRDA
GTAARAAQFDEILRRRQSGLDEMKERSLEDALAAELVNETFRCSVAPDARKDLQKLVRRVSGTVLHIGWP
FGWFFTYCDLLRLDYFGHLNIKGLEKTFLCCDKFLLPVGTACQCEAIGRAPLAIFIGEGGRVYCYAPSGD
CLYLISRSGFHGFVQEGLRNFAPLREELGWTHFDSGGDLGREFMLARDLLALWRLCMKHEGSIFSWRDGN
EALTTCVLNGGQTYEDPAHGNWLKDTCSLNVLQIFTVKAVPVEPHQRLDISILVNECGAVFGVHPDTNQA
HFLARGLLGFFNVGFLRFCNNYCFARDCFSHPESVAPAFRATGCPRDLFCRRLRKKKGLFAGR
>gnl|CDD|223005 PHA03176, PHA03176, UL43 envelope protein; Provisional
MPSVANSSPPPAYTSAAETYGHCLSAFSCAYPPCTATRGHGQSGNRCIKCIVVTVCSLVSIAAHLAVTVS
CVALIPLIDQNRAYGNCTVCAIAGFLATFAARLTIRSSETLMLIGKPAQFIFALIASIADTLINNEALAI
SNTTYKTALRAIEVTSLACFVMLGAIIASYHYVCIATSGDLTWKAGFLMLTAGTILGITAPYGHISPLAG
FLAVYTILAINIARDASATLMNTCYYRNCRERTILRPSRLGHGRTIPSPDADATYEEDVSSFDTAKGHIP
SIFLSYAMGLTIPLIIALQKYMAGIKNSSTWTDTLQGMCGLLVGSSVSIFIPSRNNEALIRPIQILLLII
GAMAITLAGFGLILGPTLFSASAAALSCYTCINIRNANKGIKQLAAASVVKSILGFIISSMLVCVLLPLS
>gnl|CDD|177552 PHA03178, PHA03178, UL43 envelope protein; Provisional
MMYQPGREPGEDSCLVLSSFSVQRCTGSRAGCMPCTWAATKALVGIGLQAGVLTASIAHVDLLTRNTTCL
ALMLISAYVLSLIRVAISTMERLVTVCRLAQALAVAIAAAVWAAGPAVKPEHLLGVLTVCIAFVAVCGAQ
IHLFYFICAANGTGTHFRAALLAMTCGCLLGVSAKLVEARKEVLIGLGIAIAIIVSCADFGLALRDTCHY
RIGRYACMRTFTDLGRGINYRWVTEAEAVPKIEEVAEDKVSLFKFFREAPGVIFSPAVGLHATPIIWIVL
RALGYGGSNVWQTPAYVVFCVTVGHVSAMALEQCLVYRRNYTAEASLGIHVTAHAVGAVLALFGYGVGAP
LSLAFATSGTLLGALYLRKRGTGAARLAATHISRWLHVAVYVAAGLCYATIIT
>gnl|CDD|223006 PHA03179, PHA03179, UL43 envelope protein; Provisional
NMGSGAVDAEDPQGRPDDPCRPLACAGALARGFAHVWTQAAALGFVGSVVLPRDAYAASPLPGLLLAGVA
GLGFAPTHAPRARPAARVCAWLRLVAGGAAVAAWVLAGPGPATRWFALAAAYAALLVLADDVHPLFAAPR
PLFLVTLGVVAGGFAAGASARFWWIGGRGAAALAAALVAGLGASSARDRFSAACPAHRRGCVIGAGESLS
RRPPEDAERPTAPDPEPPPRRVRPEHVWIPLATFLVAAALAAEFARAHPAWAGAPAPRLWLQVFVLGHAA
AGLTELCQALVPRDLTTPLLGVHAGLLVANHGLSFFVPGPALYAMLGGAVWISLAQVLGLHRRLREGGPG
AGGYATAAVRGLFLSVYVLGFAVGTAVLVPRSTGRRS
>gnl|CDD|165451 PHA03180, PHA03180, helicase-primase primase subunit; Provisional
NSDFSESEDSGIKVLFAVDGCAVSFSLALLTGQVPSTNDVYIISYWDPGDRLSQNTFLEHDSNGAERIST
DFAALPAVISSLRVEFCLLNQMTSGMGGADLKLRTRPIFVCRFTSESEINSIYASIMHGKPIQADLLAAT
LSEDDTFMLHDDFNLALHVSLGGLSSKRRNSKDSAKSLTTNSVSSLSSTFPGGKRGLAALYLQHEQKVTA
AYRRIYGGSTTTAFWYVSKFGPDEKSLVLALRYYLLQAQDECTGIATDYDLQAIKDICGTYAVPVGPNPT
GFSTADLTSFARLSRFCCSSNYARGRIARAFPTYVERRIAADVAEVDALREYIERDRPSLKISDLEFVKY
IYLAYFECYNREQLKRHLNDVTVREPEEDIYKKSSLGKRAVENFFTHVRSRLNVNDHIAQNVSPEQVELG
NDLARAFVRARTYHPDTMTHGSTFTGICECATVIAKRLDKLEAKLQKYGWPESRPDGPNLMSDNQNDPSD
SSYDRDRCDGLQLEQPDTHPRGGPMIVKRLLALVSADPRAGTIGPANMLMGISSASNGPLPVYRIGMSKG
KQAFGVLTADCWERIIPSPGTFKAHLSKLGMSEGLSTDDLIARDMFITSEVERSFGNVQELPYIACGPAE
EQQYINRNEVFNGNLAIGNIILDVDVHLKQAVPLILLHAAMRGFRSGALRALSLLLPKANIDHGSYPCYF
YKSSCKKSRVVKTAKWMDNTHESALDYDGSPFESADFDLEMGIDDPLLIDQIDESPSRWCSESAESIDSD
ADLPCGCHDKIGMRVCIPVPPPYLLVGSKTMVGIARIIQQAVLLERSFVETIGPYLKNYDIIDSGVYGHG
RSLRLPFFGKIDEEGLISGRLLPFIVIPESCNDVESFILSHFEPRNFHFHSPPPVEEMASHVIKSLGGEY
AGFFEKKITVNRDRFFGPRLSLSEALRERGVDINDSAAIEEFVTDFILEDIIRYMEEHIPDHAHEYKNAS
VSCCVVKADWILLQLIPNKTASRLHGFTCVRYKHTRTTRGSARSYLALNVDAHGRLCACVIQQCFATKCG
NNKLRTLFTVDIDSKCRSEHR
>gnl|CDD|165452 PHA03181, PHA03181, helicase-primase primase subunit; Provisional
MSTMAEMNTISAQELRGCICYTTLYRLWTSSNRTEGLTALCYLLFRNVCGNYSAHYSTVNFSGKSLAKAW
GLNPDTITDATLASMANAASVTGRWPSCNADQHTLWKALLAFTLAKLRHRLGYHAYYTPVNMYVDKITGL
VLSCEPLNGERYKPRPGLLKTDGTINVEESSLLSTAMKFTEGATLAHIKLSALKNIETIPEFDARIEIQT
KEDRFYREYKSVSSRTKKTKLHNSNNIFHVVEKPLILDGSQAPVRTLTLVPTSFDCLVTTPAEFSLSALL
AIYAKWHEKLYSTAGGSEKILTPIFTYIGPETNPRGEDVDYACIIGFPGWPMVKSSTASHLAIKEAIDSY
AATDGLWPLAGPRTFHLLAPWRPENHPSPTIDICHYLKAESNVARGRIADDWTEGRITCIFREPTLIENA
AIAKFDFSAFFATLYLGLFPCHSRLRDAVKARLRREKDWLKRPIVEFGGLLKHFREDVYKAIIGIGNHIS
LEVEATASTLMFAPCTYVKDGMWGTFIDKANNVIVSPEGNENIFETLRVACNESANRLATSIGLRFPDGI
NLQMRLEGVYTHAMSWNANCYWLWNRNTRESDFVGFPKQPEFATHAKEALSTLLEEICLCNDTDESLLTI
QEKVQKVFEELLYMAFKKRGDASFWSCPTESYDDTLYIVALGSKAAARFDTSAFRREMVQTVTTDGNIVP
VTCSLFEGTHFILPAISCIDHMKPILSAFSRLLISVLASKWPNVDQGSFTFDVEHYRFMFIRNK
>gnl|CDD|177553 PHA03185, PHA03185, UL14 tegument protein; Provisional
MDRGPGRAALRRRLAETHLRAEVYREETLRLHREGVGTQDPRFVGAFMAAKAAHRELEARLKSRARLEML
RQHAACVKIRVEEQAERRDFLIAHRRYLDPALGERLDEAEDRLADQEEQLEEAAANACLLSGDGDPADGW
MSPEDSDLLIMWQLGSAPAVRPGDLSGPGSRPTSGPVAGGLPGGGAPAPPTPPRPGPTDPASESDCGRDS
RDGD
>gnl|CDD|223007 PHA03187, PHA03187, UL14 tegument protein; Provisional
MSFSARSRRRRLQLEEAYQREMIFKMRTLDLVREGVDKRSPAFVRAFTSAKEASLDLDRYMQAHSRVGRV
EQNARALAQRVEAQAAVGEILDRHRRFLHPDFIDKFDSREDSIVEREERLGDVLSDINCDGGGGEVGDPQ
EWLGHEDEALLMRWMLEEAPRVSTRIAQDPHSPRSTCPAPRKAPEDARCGARGSGKVNNITPSAQPRSPE
TTVDGLATPDEGLRPGDQTRDLEHHSTAPMGTFRLVTHPNVLASERRRLDVVHQREKSSESQESATRSKA
IVGPADQEWLGGIPPLSDEELQVDMGIPTMNGPIYPDPHHRA
>gnl|CDD|165458 PHA03188, PHA03188, UL14 tegument protein; Provisional
MSGHTPLSAAHRRNRVHLLEAHHRAGLFKERTLDLIRGGASTQDPAFVHAFTAAKDACADLNNNIRSAAR
IAAVEQKIADIQEKVEEQTSIQKILNANRRYIAPDFIEGLDKIEDDNCDGIDKLEDAVGGDIEHDHHEGW
FCEDDEALLTQWMLTTHPSPIPHAPPSKNLLLEDCCTCSTINTDKNDMKNAMINIHEMP
>gnl|CDD|223008 PHA03189, PHA03189, UL14 tegument protein; Provisional
MARRPVGAPRPYLWLVLLIAILTIVCVSSSYWDQLLHPPVARGPILQTMWDENYERNSPAPLLVPYGDRV
TVPCTFPTHDWPEVSIRARFCYSPERSRELVVDADSGGELHNDLTYRLPEASWKFEDLGAAQRLTLTFRV
STSTAGMYECVLRNETHGLVLQRFVIVTDVETLRRPDEPCCDPALGRHSQGKYIWSPTPWRLRSHDCGWE
RERGFQRLVHYIAAPGESGLEPSCPEEEPDRCWPVIQQYLLDGNCYRSQREDREFIPRGPPLEPTEATPV
PIFTGRSPWATRGMAGMLIFGVCFACYLVYLTLCGRLCYKRLLGWRHGEGYRRLPTYDEYPGGREMKA
>gnl|CDD|165460 PHA03190, PHA03190, UL14 tegument protein; Provisional
MDSARDRRIQARAEIMEYIKGQAYKAAVIEMMSAGVPPMHPAFRHAFAKAREHEAAAEIAAQSDKRLSSV
RCHIARIKAATEGQRALALELDGYRRYLRNDFLDTFAAEADAIADAEIDLECAEAEIALHIPADEDRRDS
LDCEEDDLLLKWQLEGANPPSLLPIPHAPSGESRGNSPKSPPGPSPTFQDAECPRE
>gnl|CDD|165461 PHA03191, PHA03191, UL14 tegument protein; Provisional
MFAVAAMRRRRRQILAECRTRETIYKERTLELLSQGVETDDPEFIETFTSARNAHSDYKAQLRSNMRLEN
TERKLRIIQRHIDEQVDRRLILDTNRRFLNPELQSQLDQAEEDILDKEDILTQACDDITLADSSEDIEEL
DEEAEALLTKWILEQKPRPRLPTAKTAPPHTRDGTRTTEKARVPTGVQDTNSQATDQNLPPPTTSTPSIS
REHVIHPNAISPEVDTTEDASPATLGDV
>gnl|CDD|177555 PHA03193, PHA03193, tegument protein VP11/12; Provisional
MDRLACAEMSLELFDPDSPEPETDSLALNSRSRGSPTRVQEYPCILPEELGTSASAIRALEDALIEKLPS
GFLLAIRESLLCDALSNKVPECIIVHLALGDAREEYIRLYRANIARRLKKAALTPASVKDCYQASYMNYL
CKRRDGCCADLPETCDPARREAALLFYPAINRNALTKKPFQLAKDNALFLKCWAEIRDALEFIQKYAYYM
RPDDITAPSADTSARLELLFGYVKTLYMWAMWLMDLLDLRACPNKFGPRAPIDFDNIFLALAEAMGSLPS
DKWADTALLCHFIEHLLAPLIHIGALWTCCAWRESKEGEMLRPIVAIVALVGLLHHHCQYIINITFNGYA
RWLEGGLANPMLRRAIRQQKRFECFLGELFPSINPCAWADLEFSIAAWFEHALAKSMVIHGSLLKKSIVS
NNVLEPAAKGGDSQIGCLHDSPFQRKRAMPEDGGEIHEALANNGQAIFPECFSGDLPPIAQALLSADELP
NDTTASTSNEMKGDAECPAAQDAAAILPASFQIENGGAADGSGLAIPAAMCDATAVESPSTVAETPPERL
LAAESGPRCKATAKHKGGSSKVEEILRRLRMASD
>gnl|CDD|177556 PHA03195, PHA03195, tegument protein VP11/12; Provisional
MDGGGSSSWTHVSKNLIERRAVKGCLLPTPSDVMDAAVMALKDVTENVVGQQLFSVDRTNALSVIHTNEV
PESIITTAIARDTSEEYRREYEMAAKCNLAATDLSQDGMWEVVIKSYWRYLRESSGAEVVDRGAVGQATQ
SVLSVLLLQSTFGKKRLSKNPFKHKGPNVGYKSNLEDLRSAFTKIEKYMYYMRPNDPMTKSEDTELRLHE
LLAYVATCYRWLLWFMDLTDAKVLRNIDKGPVITHGPRESRPPDELVRRHLKSGPAISAGTGVALTLSTA
TADALIVLLRMSVSWTSHSWKSNTHGVTGAIVAAVELVTLIHHHLQYIINTVFAGYVCWLDGGVENSYLN
SALRSQGRFDHFVGKLVPIMATLSWANMEKGTVMWFKYALAKSIVCHGSPTQHYLTVLESIASKRTGSCP
PQGATFGRNPSGFPGQFCCPPQGPLPAPPNSKTRGTFRRPRPGSVRGSRQLPASPPSNIVSPRTNPAAEG
STAAKNGQGAETIQVRSSGEFNDCIWYLNGAYPHQRSDSSSSDNSTCSSTETQYITLPSTPSPTGEVVYT
NPLLGPDEEVDASPQPVDPVSDYSAPKNPDYMRPRSTLVEEIWQLRDSDYTPYMRPSRAGRPRVRVEDQT
LEPGSPKGCYPPANSPENDVKDNLPDSPPISPEVVYGTFRPRARCVDDQYGLTALAALSASRAKARRTRL
GPTPTSANERTEESATPRADGFIRRTMSTTGPPRKHPEQTERVSSL
>gnl|CDD|165466 PHA03199, PHA03199, uracil DNA glycosylase; Provisional
MCFRCEKRICANAFANEMKLADRCDITNLAHPTRKKKRFRPCGIPLGVILDPDCFKLKDMPHHYDTETFT
CEQNQADSTELFDEFCIDPEWHDLLRDEFEEPYAKGIFEEYNQLLNNGEEIFPIKGDIFAWTRFCGPEKI
RVVIIGQDPYHGAGHAHGLAFSVKRGIPIPPSLKNIFAALMESYPHLPLPTHGCLDNWARQGVLLLNTTL
TVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFMLWGAHAQKTIQPNPRCHLVLTHAHPSPLSRSEFR
NCKHFLQANEYFLKKGEPEIDWSI
>gnl|CDD|165467 PHA03200, PHA03200, uracil DNA glycosylase; Provisional
MALRQWMLENIADEKKCMLNESPDEQAELFGINEDWLRFLNLSDHDISQLRRIVDAVDRDRQRLTVYPPP
EDVHRWSRLCSPEDVKVVIVGQDPYHDGSACGLAFGTVRGRSAPPSLKNVFRELERTVPNFSRPDSGCLD
SWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKHLI
LKSAHPSPRVKGARTPFIGNNHFVLANEYLSTHGKRPIDWNILNG
>gnl|CDD|165468 PHA03201, PHA03201, uracil DNA glycosylase; Provisional
MKRARSRSPSPPRRPSPPRPTPPRSPDASPEETPPSPPGPGAEPPPGRAAGPAAPRRRPRGCPAGVTFSS
SAPPRPPLGLDDAPAATPPPLDWTEFRRRFLVGDAWRPLLEPELANPLTARLMAEYERRCRTEEVLPPRE
DVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTPAPPSLRNILAAVRNCCPDARMSGHGCLE
KWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFMLWGAHAQNAIRPDPRVHRVL
TYSHPSPLSKVPFGSCRHFCLANQYLRERSLAPIDWST
>gnl|CDD|165469 PHA03202, PHA03202, uracil DNA glycosylase; Provisional
MSSACDHKTKASTVNIPETKPEENGQRSSTPTSEAGQPACVVSPAPCETGAPPPKRRRPCGLPQGVSLIN
TSVSTHPLFTTNCQSSWEDVEREFNIAPSWRPILEREMQQPYVRLLLNEYKLRCAREEVFPPKEDIFAWT
RFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPVPPSLRNIYSAVQKSYPSFRPPMHGFLEKWAEQG
VLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWGAHAQKSCSPNRQHHLVLTYGHPS
PLSRVNFRDCPHFLEANAYLTKTGRKPVDWQIE
>gnl|CDD|165471 PHA03204, PHA03204, uracil DNA glycosylase; Provisional
MARVMARCTSTDLSETSMTTIGECHAETKHPDLKRCAEPPMVEGLGRPKKRRRPEGPPPGFIPARTKSDK
SCDGGEESSHQCNVETESKAKAWEHIASVYNIDCRWKEILLPELCCPTGSKILAEYERRARYEEVYPPKS
DIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPIPPSLKNILAAVKACYPSIELGSHGCLE
DWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWGAQAQTMYFQTDNDDRHL
VLKYSHPSPLSRKPFAHCTHFKDANEFLCKMGKGAIDWSLTA
>gnl|CDD|165473 PHA03207, PHA03207, serine/threonine kinase US3; Provisional
MECHTDSSKVSDSNINLGYEAIFSLTGGTDTSDSKDTTGDKFDDCDELGDSDDVTHATDYDADEESLSPQ
TDVCQEPCETTSSSDPASVVRMQYNILSSLTPGSEGEVFVCTKHGDEQRKKVIVKAVTGGKTPGREIDIL
KTISHRAIINLIHAYRWKSTVCMVMPKYKCDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRD
VKTENIFLDEPENAVLGDFGAACKLDAHPDTPQCYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEM
SVKNVTLFGKQVKSSSSQLRSIIRCMQVHPLEFPQNGSTNLCKHFKQYAIVLRPPYTIPPVIRKYGMHMD
VEYLIAKMLTFDQEFRPSAQDILSLPLFTKEPINLLNITPSD
>gnl|CDD|177557 PHA03209, PHA03209, serine/threonine kinase US3; Provisional
SESMDTTPPLPPRSYSGGAADEDLYSDISDGDLEYSDDDSASESDDDDDDGLIPTKQKAREVVASLGYTV
IKTLTPGSEGRVFVATKPGQPDPVVLKIGQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYS
SDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVA
PAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLAYPSTIFEDPPSTPEEYVKSCHSHLLKIIS
TLKVHPEEFPRDPGSRLVRGFIEYASLERQPYTRYPCFQRVNLPIDGEFLVHKMLTFDAAMRPSAEEILN
YPMFAQL
>gnl|CDD|165476 PHA03210, PHA03210, serine/threonine kinase US3; Provisional
MRFRFICPRVCRSRAARAEERKRRREHPHDRKRCAILDDFDEDGRLAHIAEILPNAEECAEAAEKVSIMA
PERADPTGAHRALEDAAPAGELLVPRSNADLFASAGDGPSGAEDSDASHLDFDEAPPDAAGPVPLAQAKL
KHDDEFLAHFRVIDDLPAGAFGKIFICALRASTEEAEARRGVNSTNQGKPKCERLIAKRVKAGSRAAIQL
ENEILALGRLNHENILKIEEILRSEANTYMITQKYDFDLYSFMYDEAFDWKDRPLLKQTRAIMKQLLCAV
EYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEREAFDYGWVGTVATNSPEILAGDGYCEITD
IWSCGLILLDMLSHDFCPIGDGGGKPGKQLLKIIDSLSVCDEEFPDPPCKLFDYIDSAEIDHAGHSVPPL
IRNLGLPADFEYPLVKMLTFDWHLRPGAAELLALPLFSAEEEEEILFIHGLKSGAAHFKPIKPACRIESD
TAALPLSMSDD
>gnl|CDD|223009 PHA03211, PHA03211, serine/threonine kinase US3; Provisional
MACRKFRRVYAGATEDAGREEAVEPETTTRCVFPPETFYNPPRGVCFPPPPEHDPPSPHGARDEAARLCQ
IQELLAEMRSSEEYPDSGAEAEDDDDDDAPDDVAYPDEYAEDDFLPGDGAPDHDPAPCGPAPPGGLTPEE
LERLDREAARAISRGCKPPSEVAKVVAGLGFAIHRALTPGSEGCVFESSHPDYPQRVVVKAGWYASSVHE
ARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYRSDLYTYLGARLRPLGLAQVTAVARQLLSAIDYIHGEG
IIHRDIKTENVLVNGPEDICLGDFGAACFARGSWSTPFHYGIAGTVDTNAPEVLAGDPYTPSVDIWSAGL
VIFEAAVHTASLFSASRGDERRPYDAQILRIIRQAQVHVDEFPQHAGSRLVSQYRHRAARNRRPAYTRPA
WTRYYKLDLDVEYLVCRALTFDGARRPSAAELLRLPLFQSK
>gnl|CDD|165478 PHA03212, PHA03212, serine/threonine kinase US3; Provisional
MNDICALDSFSDQGKFHGAASHSPNHIMQQCFFCDQMFPSEMNPGIESDDDCLYEDKHMDIDIFDIFADE
DESDADASLALCAEARAGIEKAGFSILETFTPGAEGFAFACIDNKTCEHVVIKAGQRGGTATEAHILRAI
NHPSIIQLKGTFTYNKFTCLILPRYKTDLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKA
ENIFINHPGDVCLGDFGAACFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCH
DSLFEKDGLDGDCDSDRQIKLIIRRSGTHPNEFPIDAQANLDEIYIGLAKKSSRKPGSRPLWTNLYELPI
DLEYLICKMLAFDAHHRPSAEALLDFAAFQDIPDPYPNPME
>gnl|CDD|165479 PHA03214, PHA03214, nuclear protein UL24; Provisional
MSLTGLPDIRKKIGQFHHLRIYKQILSLQGNFARLNYFLGDVFPANLRSASVSVFFEVRLGPRIPDCIVL
LKSVDAKDEFAFHCYFFEFKTTLGKSTMQSVHHNCIHQAQYLQGLRQLRQSISFLDQYLIADEVLWNVVP
VICFFRQWGLKLDFFKKFSGKTKRLSFSFICDLFARSQDGAVQSLLSIPNYTNFRRACQKHTDLYRGRYA
KAPKSVLTKTSGENRSRASRQVAKNAPKNRIRRTAKKDAKRQ
>gnl|CDD|223010 PHA03215, PHA03215, nuclear protein UL24; Provisional
MARRTGSPIERRRILLAGVRSHVRFYKALAREIREFNATRVCGTLLTLLNKSLQGRSVFEATRVTLICEV
DLGARRPDCLCVFEFANDKTLGGVCVIIELKTCKFISSGDTASKREQRATGLSQLRDSVKLVQALAPPGH
RTVYLCPVLLFVSQKTLRVSRVTRLVPQKITGDVTATVRTLQGLSTYAVPLEPRTTRRGRRRGARRPRSR
RRPRGGAAGPPVPAEPAAPERPPADPTPTSARGGGVLQKIAALFCVPVSRTE
>gnl|CDD|177558 PHA03216, PHA03216, nuclear protein UL24; Provisional
MKREQRLTARSRLRAGIRCHNRFYNAMVQDLASAKANGVYGDRLAPLFSELVPAETLKTAKGVSLAFEVN
LGQRRPDCVCTVQFGHGSDAKGVCILIELKTCRFSKNMNTASKNLQRKGGMRQLHDSCRLLAKTLPPGSG
EITLAPVLVFVAQRGMRVLRVTRLSPQVVYSNAAVLSCTISRLAEYNPPESGGSTRRRCVSKRTNSKAFR
AKTTTGSIQPITPASPSAVAAVTSLFPASSCANTTNAANTLQPIGSSESNPLAWVASLFPPK
>gnl|CDD|223011 PHA03218, PHA03218, nuclear protein UL24; Provisional
MSSERALPTTAARPTCTRRSKCKPRRYGRAGSAGNCLRGKHAGNVLMKRLLAAGVRCHNRFYKKLYAENM
DLQSQAGDWVGRTLQKILGKIMPSDVFKGATDFRLVFEVNLGRRRPDCICMFTLPRGLWEEGCDGVCVII
ELKTCRFSRNLKTASKNEQRLTGTKQLLDSKTLIERMAPRGSDHIIICPVLVFVARRKLVVLRVTCLKKK
AICTDFHRLASMMYLASEYKLGMCDPMRKICRRNKRTVSTVRRMRCGISDTGVLPIEKHHVDNRGKDLGT
SGIQPGAGETIMQRMANIISHLVRRH
>gnl|CDD|165484 PHA03219, PHA03219, nuclear protein UL24; Provisional
MSDLASLALTAEFGLGCLEAYVRINSGQKIPVPWPPGWYLVLQELEADEDFKPEDVKAWSYYLCCQTRLA
FVGRVVGEPVLSPDQQKKTLIILVSEEGYVFCYVREDFAVYYVARNLMEFARVGLRAVEVLHCPRYLRSS
LVKRYFRPLRRAWSLGPDAVARFIIRNHGNYLPLTYPPGAELRLCNLKCFEVTVTGGHLLRSIKSHFGDR
VIGLGTVDLKGEMPPFPYLRWPVTRVPIVLVYTGRVYACDLRNLRYIRLGDNLTAFMCLGLNLLFENRRF
SGHNGLHDRVPDCPKGRQHN
>gnl|CDD|165485 PHA03222, PHA03222, single-stranded binding protein UL29; Provisional
MGDENRPRLARRKRAAAPETFCARDLADLCMRRDSEGLKRYLLRFEGACVSLGWPAQCAFVVGGMHSPYA
ITEIDLEHCQNDFFGEFRDLHLIGTVSHAACKYPVFLDACGAVFAYDAKEDCLYELASDLGDFFAKGMIR
CDPVHESICARLQPDVSLLHPAHKAELCERSRISARERYLHSLLCFRELLACGDDPEARSAYVEEHRDAK
LILIWPENHHLLVANAQDLELSAIAIRRFQRFLYGREPILALGEIEGEEGKTFFNHVKIFCGDSGAVYAA
LVGHDKLTKIARDLKAFVRIGLALLIDDFRYENIGPIDHHSLHELNPELKLPFKKRR
>gnl|CDD|165486 PHA03225, PHA03225, DNA packaging protein UL33; Provisional
MASLIGAGTAARLDELIDEEELAERPLSELFRDYIESAGEPRYEIWFFDLSPPEIELALPTTDAKLNYLA
HTANLAAALRYDCAGDLDGGRMCAHAELIARRRERFAKILNKFLDLHQILGAIEP
>gnl|CDD|223012 PHA03229, PHA03229, DNA packaging protein UL33; Provisional
MSSGRPRPRTLREAIPDCALLSRSLESLEARYVSRDDADGGAGDAAVWFEDLTPVELEVVFPTTDAKLNY
LSRTQRLASLLAYAGDIKAPDAADAGQTRDPACAHAELLAQKRGRFAAVINRFLDLHQILRG
>gnl|CDD|223013 PHA03230, PHA03230, nuclear protein UL55; Provisional
MTSASLSSLFLRCKPDLLPNISHVVAPLALDATWQSEKALHTPTPSGSYVTTRTYTIRATCNTSGDLHAF
FFGLFTDSKPSEQPSLPDLRNFCRLLNNPRVLRELRTKHELCSAPFSAATIKDSLDDGYLEYTINGLCYH
CHCKNPFSLECWQGAFAASAHIASLCRSIRAAGAAEARRK
>gnl|CDD|223014 PHA03231, PHA03231, glycoprotein BALF4; Provisional
SPHTTSTPAASADPTTTSPTLRETVREITAANEKYPFRVCSPPTGGDLVRFEPPRTCPSYKLGKNHTEGI
AVVYKENIVPYTFKVRTYYKIVTFTTVYAGWTYDAITNRYEDRVPVPVYEIDLIDSKGQCYSSARYVRNG
VYVAYHDRDEVNKTVPLKPSDGLTPGSRRYHTTKETYAAPGWLWLYRTRTTVNCIVTEMEARSVYPYDYF
VLSTGDTVEMSPFYGGRNGETFAEHTSYAADRFRQRENYTMVDLDTRGTAPTPVKRNFLETPDYTVSWDW
EPKRTSVCSLTKWKEVDRAIRTEYNGSYHFVARELTATFVTNKTEFNLSDTHLGDCVKDEANETIDRIFR
KKYNSTHVKNGDVQYYLTTGGLLLAWQPLLSKSLAELYLLELLRTNRTEAAPNATSASSRRRRSVSSGPA
GTPTIKTTSSIEFAQLQFAYDHLRDHINDMLGRLAEAWCLLQNRELTVWHELSKINPSSIMSAIYGRPVA
ARLLGDVIAVSKCVEVDQSSVSLQKSMRVPGSPGTCYSRPLVTFSFVNSSELVEGQLGEDNEILLGRHLT
EPCQANSRRYFLFGNEYYYYEDYTFVRTIPLSDIETLDTFIALNLTLLENIDFKPLELYSRDELRDSNVF
DLEEIFREYNLYKQRFYDIDNVIDNDRNAFVRGLAEFMQGLGAVGKAVGNVVSGVAGAVGSIVSGVISFL
KNPFGGLAIGLLVIAVLVAVFLAYRRVRRLRQNPMKMLYPYTTKALPSEATGEYGNGDESEESDFDEYKL
EEAREMLLAMHLLSAEERQEKKAKKKNSGPALLSSALDRLRRRRRGGYQRLPDEDEDED
>gnl|CDD|223015 PHA03232, PHA03232, DNA packaging protein UL32; Provisional
ASPMGFLRSAAEVGTELGSGWKEGAFERPYVAFDPALLALNDSLCDELLFAAHLIQIPPPEALEEDVEAD
PEDPDGEGHPDTAPFVEAAADTLALDRPCLVCRTIDLYRRKFGLSPEWMADYAMLCAKCLAAPPCATATF
VAAFEFVYIMDKHFLRRHGATLVGAFARRVLTLVDIQRHFFLHGCFRTDGGVPGRRPSEPPPPKAGSPGA
AKVQYSNYSFLVQSATRAMLLTLADGQANDAGANGAEAGAAGGSGPQGPKPQSLAVALMNWKECARLLDC
SGSERRRGGGESCCERAAAEDDEYEREATAALAGAGAARATPSKWGYADLALLLLAGTGATWEDGERTNA
AAEARRATVEEYWAAHRAALARDTAPRFARFAGEDAEPDLALGPVLATTLKHARGRGRTGGECLLCNLLL
TRAYWLALRRLKRDVVAYSANNTSLFDCIEPVLDAWEAEGYTQPGDGGRFLALLKAAGPEAIYKHLFCDP
MCAISELQTNPRVLFGHPPASDPEELELYKARLASENRFEGRVCAGLWALAYTFKTYQVFPPKPTALAAF
IRDAGALLRRHSISLISLEHTLCTYV
>gnl|CDD|223016 PHA03233, PHA03233, DNA packaging protein UL32; Provisional
ADSMYKGWSPELTTIDSELVNELLLYAHPTQSPPAPAEATTASSTDNTTSASVTDSQASRGGGGGAAAAC
DLEAELARIEESLNLEELKRLCTPLEIDTRCNLCAIVSICLRQDPDQAWLLDYSLLCYKCSYAPRTALST
LIVATEFLHLLQRHFPDINFDNLFRNRILTIFDFHVHFFINRCFANTVGDPVQNENITLNHMAVVRALLL
KEDTVPYTKIRRFLQKKKKPAAAEEELLRLLKKHTRPSKTRFTRLLFYMWSGTNVFFNTPLTDLAIKKHH
RLKALYSRKSEIEKSVGPIYLSPVPVFITKNQTTTVCLLCELMACSYQDNLFLRELYERITNYCQNNLKM
IDRIQLVLADILPTRICTTPKGLKNKDVSKYVLDNEPSFSADDAPFRLDAHTYLILRQVGVTGIYKHFFC
DPQCAANIRTTNPEVLFGTVPAEYLQELKLAICYDNEYPSSVERRVWLYIHLFKAFQIIKRNFKNKTQLA
DFLRDFTQLLELHEFKLVDPSFTVDKYV
>gnl|CDD|177562 PHA03234, PHA03234, DNA packaging protein UL33; Provisional
MDTLIDFQKILHDEEFKGNASCISTPTLKKAQILESAINGIMLTLIIPMIIIVICTLIIYHKVAKHNATS
FYLITLFASDFLHMLCVFFLTLNREALFNFNQAFCQCVLFIYHASCSYSICMLAIIATIRYKTLHRRKKN
DKKNNHIGRNIGILFLASAMCAIPAALFVKTEGKKGNYGKCNIHISSKKAYDLFIAIKIVFCFIWGIFPT
MIFSFFYVIFCKALHALTEKKHKKTLFFIRILILSFLCIQIPNIAILICEIAFLYIANNSCFGLAQREIL
QIIIRLMPEIHCFSNPLVYAFTGGDFRLRFTACFQDFFKCNLCNSQKKKDRDALEHDN
>gnl|CDD|223017 PHA03235, PHA03235, DNA packaging protein UL33; Provisional
DVLLVHNETNDENDLLHVNDTCVPTEGLSAARTTETFINLLIISVGGPLNLIVLVTQLLANRVHGFSTPT
LYMTNLYLANLLTVFVLPFIMLSNQGLLSGSVAGCKFASLLYYASCTVGFATVALIAADRYRVIHQRTRA
RSSAYRSTYKILGLTWFASLICSGPAPVYTTVVAHDDVDPEAPGYETCVIYFRADQVKTVLSTFKVLLTL
VWGIAPVVMMTWFYTFFYRTLKRASYKKRSRTLTFVCILLLSFLCLQTPFVAIMIFDSYATLIWPSDCEH
INLRDAVSTLSRLVPNLHCLLNPILYAFLGNDFLKRFRQCFRGELFSRRAFLRSRQKCGATAISTVCALP
SKTSTLSTSSGTRQQKIKRSQSLNLPNATPKNKPKTRCAQNDTDNATRLSQSHHNLSRV
>gnl|CDD|223018 PHA03236, PHA03236, DNA packaging protein UL33; Provisional
QTRVKSTVRLRDAIPNEDLQSLDLDALEEKYLIDDDFQYRIWFEYLIPDEIEAIFPTTDSKLNYLSFTRR
LASVLRHGRIRVDGGNVNSFGATAVVCEHGASLTGRRERFASVINRFLDLHQILKDC
>gnl|CDD|223019 PHA03237, PHA03237, envelope glycoprotein M; Provisional
MEEPLRPEPATRGIGRIDYIHWRLWLVQVACFALAVLVLFITLITASIPLTGFPCFYAAVVDYTQVNTSL
VHGGWTNPRLGGVVPTLFFETKSTVAFFYYTTLVLVALACYLIVGAVIIRREARGCTAYAGCGAFVASLI
ASPATLLLGTLATWLLQAVVLLLSHKLIVLAAATYLVHFSALTFFYGYFCGRGVDSAQYAEDVRILKTND
PRLHRLAGPGRAVMINLVSGVYGLSLIIASLMLGMLLANSFHLTLWQTITVAIGVFVALTLMYLLIVEFV
VSRYVHVLPGPALGLLIAYGMLAVTTHDYFNRFYYAVGVQAPNLRLACKLVLAIFAVIIVIMLVVRLVRA
CLYHRRRSTRFYGRVKTVQQKVKRYLNRVRGGRRRPKSLVEDERGLLLTEDSETDDEEPIYDVVYSEFES
EWYD
>gnl|CDD|177565 PHA03239, PHA03239, envelope glycoprotein M; Provisional
MGNLRFGGKKPHEIVEDRQDVESELERISWRIWLTEAACFILGALLFLLAIFAALSEFTGFPCFVAAVGD
SELFGADLDGGGMAGAKGDGAKIFFLEPPSILAFTFSAAFVMLAVAIYLIAGAIRIHMCGKNFDELRGAS
EIARAIATMTSLFLGLFSAWAEHAFLILLAYKQLGIAATAFVGIFIAFLLFMGCFAGGGKIPDNNAKFEL
DIKEVCKDLHALIGAAKAVFLNLFCALFGIDHLILCLLGALIMALHFGLDIPKATSGALSMFIVLGIIYL
MMAELTVAHYVHVLIGPHLGMIIACAIAGTAAHAYADRLYDEIMIASPKLIQGAAGILAAFAVISIALAI
LRATRAYKFHKAANSKFLGQVARVAQKVKGRAQKEKNGPHSHKKYVDARPLDAYADDPRDNIPFERRSRE
GDADDDIYE
>gnl|CDD|165499 PHA03240, PHA03240, envelope glycoprotein M; Provisional
MPFGNHIVNCDFFRWFVLSAMFFYEFSEACEEHTTREGDPLLLGGGHGLGAGQKAHWYKHKCDGITGNGD
KLHPICTYDPPKNGKGKTLDESAENSFILYECHNSTLIIAHLNLSDAGEYCRKKCPPKGDCEFPTMSCFR
LILRPISKTTSKKPEQGPTLLRLKTTPNKHTQHKRRTKRTSPDDYNVTGLEEGFADSFTGNFEAHRSKDA
AHIAWIFIAIIIIIVIILFFFKIPQKLFDKWDLHGSLYAGTDGFPAFD
>gnl|CDD|177566 PHA03242, PHA03242, envelope glycoprotein M; Provisional
MGRVSPRGSAAMAGDAQVARVAWRVWCVQVGAFAVSALCLLGTLIAASSFRAGFPCFYAAVASYGLANDT
AEGGVWSGNGYSAPPLFLETPSLVAFYAYTATLLLAVAAYAVAGAVTIRRERRNQDAAELLAAARMVVPP
ATLLLGNLCAWLLQATVLLLAHKQSGLAATVYVLHFACLVYFAAHFCTRGVLSGTYLRQVHGLRDASPTH
HRVVGPVRAVMTNALLGGVALCTATAALMLGTIAANNFHLSLPGTLVCLTAVFALLVVLLLVVVEGVLSH
YVRVLPGPHLGALVAAGIVGVAAHRYFTQGYYVAETQWPGAQTGVRVALALVALFALAMAVLRLVRAYLY
HRRHRSRFYGHVRDARHRARSYIRRVRSSMRNSREAPYAGESDVGRDDDYASTDGEPIYDEVAPDEDEVL
YARIQHEW
>gnl|CDD|177567 PHA03244, PHA03244, large tegument protein UL36; Provisional
MDDLRDTLGYYGCIADRAFDFNRLNKFLSQECGSRLHVSWPERCSIQLRSRSALGPFVGKMGTVCSQGAY
VCCQEYFHPIGFLEGPGFMRYQFIVLYGSRGGVYCYDDLEDCVYELADTMKSFLRDGFRRCDAFYTMRDY
QRPMVLYDDYWNSLMLYRSDVESTSAEAANRGYSSYPIDDPFDECPDTHFAFWTHHGEVMKFKETSFSVV
SLGGTIQTMELMINTVPRISCYHQLLGALGHEVAERAEFHVRQYVLMDPFGAVYGYDPALDAVYRLAEDV
VMFTCVMGKKGLRNHRFSPRREAAVRLEKTPHCQHPKKTPDPMIMFDPDDNFDIEPQPRGHDAHEEAENR
FFDAIRENRNQCSKGVVTDSQIATHLWPQELDALLDGPCLPMARDPRVREDVEKVRQKLRARTGSLHHFE
LSIRFDDEDPETYMGFLWDDPPCRRCVRRRREKVCDRGRRHIIPGAANGMPPLTPPHA
>gnl|CDD|223020 PHA03246, PHA03246, large tegument protein UL36; Provisional
MAASESRGSTTRPSKKSTRLQPSPSTRRLETSDNSMEAVRSNMYKRNSLLGSTMGDSEVILDEWAKMVVD
TTDFTIVAVGIRNQFAPDLSPGSSVSCLRSSLAFLRIVFAYGLDTVLSADAIDRLLLQGKDWTIHTSDDG
VYTTCVPHDLPNRILSKDPGGNLCVAFSSSYGESEFYLDENTPTILDTQISARTFIERVWKQKRGDIYCL
IVIGVLGIGVYRSEDGIYIFDPHGHGHIGQACIVRVSEGYFYQYLTSYADPSGMPDWSATFVYFVSTASS
APPKEEIISAVSRLYGTADIVLDLGRADEEDNLKVVSADFDPPSRPQPWQTKIVIGTADSYADSSPKLHS
ESTDLTPHEHGEYDPSTLVGGASTNINISDPPARTDCRRYSEGSVIHESVDSHIEDVTEATSVVAAWSDA
FSDISEDYSHLTRPDLPATAHDVSKNGHDTKSDRRSRGSNSRHKRRRPSWTPPSSSENVSSDGPTFSQSR
KPSRKSKRALDLDYGHLSNEPSDVDGENSDSPAGAISNIPDNVSFNEFISSQARAEDSIEHLSLRNRPVF
NPHTVTGNLDNTLRDSLWNDEYSGSYPLSDISDMIDDITESIADGMRLVVHTSHRGDYDGGLLDVCIMDV
FTRLFNYIIENGARTTTDRASVVEPEMAALTKAFTTPSHFSTFISSTGMSLSEASESADLIESVLTENSK
IGKLALSKLTLVALEVEEATDTLHKSLDAIEREASTADPDRIYERMATVLVDTFYRNSGKLYSETTSYNS
DQTLTDRVVSLCEFIRDRENVATRKAELILAEIEALDAGVRWMNTKFDAFIMGGSGGMSPAKGLSAIAKT
STDVVTQRLESIGKAAIDIVGNALREYYLKCALYSAKALRADMKETSRFKIVVTEQLEKMTRLLSSLSVI
DDVILLIASRSDARVPVPVSKALESQLLGDLLEIGSHLDVPENLVTWKGLMVSVQTGGWISRRELDLLLK
EVDAVNDNAARRETALTELERLHELESRIASYTDLETTVDLQKLDEALKLANSIVKLTKGLDGAKLASSL
SSDIREKIRQKRSETETLIARLSARYAEVKAAVDGLYSSIRKLLRPLQNFAGLRALDSTVKTITDSIPPG
MGSFESFLASAPPDVIGALRSDLWVLFTQYKTILSRPSTGTAAELSGLGGPFALAIRVILGPEGEYPAAS
VFFGKHADVLSAALAAAASEPMSVEKTSAAVSVLKEAISDINRADATIPQQGIMADLSTERADAFSFLHA
LLSDAEGAADVASRGAYLSTLIRTVRDSLEAVIDSITKIKSLDPKTYTYNTDASVIVSAKAEVSAATQQA
GDCKDALTALENEPLTYNPHIQRKIAELNKLIESVNQRVGELDIALQTYERNRISAERSRSEDLWTSSIT
SLLVNAEIKSEFDAMEINSLEETARNAGYDTIRFKSRAEKIVSAHARVVENAIETVLKFNPYSTTNIIHG
LKPPIAALKNITWGDAFFAAAPYYTKLFGVNCDVLISLLKILFAILRHASAHPGNLDYYFLVGEIESDLR
AIPSLAKYVDFYRRGHDSFEGFLARLEQMRVEALHASGRVSIEISDALETLARTHSPEGARRALEYGVSI
VIPSANTIMSIADALQKEKITELDGTAYAEYSAHILRRDNDAIKSITQRVTTAIEAAKSRGESILKDLAE
ASYAADRETAEQLANLKNLLRLVAMPAHIAKAIDKAETANDIVTQAALLLTKVEETKELDTQTVEWLKHA
ESVIDSHDLTVRIDESGPMTIYAERIDALVRLENRLAELKSELALAEVAWDDTWSTFIHDKDRIDKSSEG
FSAARESAARAKVSTNAINALRNNAEYNRLPAKIIGLIDSKYRDRTVVLDAFLDSMKEIEDTQKQMEILC
SKIPLTFSLNDLRAISSQFDDIAKRLPKWYVKQVGRYSRLIKLRLALYAAYSNASTGPIGDPPLLPFDTG
RANIAANMAPSVGLVDRYLKHRVAAWIRPKVVATLQEAFSEIDMPGLTTYLDSTDTPLRYSICYRTVGEK
LAACLCEPSAVNIKPRIPTNLISTVEMESAAGMLNDIMILRLGFVQACADRFQLFTKYVRTGIHDWSPDY
CIKAHGTIYCALIAITLTRKTGSNLSDIYFIPGQYGPTIDKKELKKFAANGRRRQVVRLDPADVMVTIMA
CTPGHVLTFSKLDLINQYDFMDKTLYNVLTDSISTVAFVNCLSTQLSKDGKVDPNCRPLSLTGGEWDPSG
GSLFAIRYSDWKQGRLSDTDPLKPWEDISGDEGAGLAKIRAVVPSSLLTTTTVLARMCIPPTALAVMWSS
LLPDGIEQTCKSYDDVVTARGDGASTLDVTTSTIDHTGVKNIQTNLDCPNLYEYTGTATTFTVVSTPPSR
VLKVNAMDIAACATLFGARIVIAAECPEAYSSDSGLSLCIRLFDSRSGSKGCFLEPGAVSSDITSWGAKL
LAADSNPIENACLGQQLEHLSHLIASKPLSSAPPCLVIVDAGMVPVKVLWAKEELDPIPIIRLTSADDAL
ISELPYIDAGIRGETGADFQHMHVLDAQEASRFFSDESRIYPTPTYNKGVDQHNSRDGDEDVLSIGTASE
DESIPGNFFSIDPESMWDTGSEELPVYSDAEQDGLIGGGINDREDRAVPENVEYPALATQGDQDGFVSKV
GSAMKYKPPNVTAMAQSIVQPDTQKSSIKKKTDIRLAGYRTMPADNRQKGNGLRHKPKTGRSHTTIKNVE
VYPSPPRWTRTAAAQKRHGEILGQVSPPIVTLDNATPVNGIRHEKHSIPYDRLDEHRTDPDALSTPPVIA
APSPSLIYKELSGGIGKNILKMGRKQINSRSKERMSSKASNSPRKNNISRSTADILVGMASTTSSHSPLL
QRADDMYINIKNIPVPEVKEEGNWKGCKKRNNHVPEVETRLYDNESFPPPPNIIASWKQRVVRFWEILPH
TPRGNAHRKKVSQTTHKPPNATTAKHDHLSMYRGPVLTEAESGENKFNNVNVDPIRKRSESESLSSTDSD
SDDSRSTVYNSNSTDTDMSSTSRVIIADTLLTRRDFRKASRGALYALTKACEKIARQITQTRDQLRSRVI
TLAIEIFKIKMLLTG
>gnl|CDD|223021 PHA03247, PHA03247, large tegument protein UL36; Provisional
MARRGDRGIVVTGARNQFAPDLEPGGAVSCMRSSLSFLSLVFDAGLRDALSAEAVDGCLVEGGAWTRASA
GSGPPRMCSIVELPTFLEYPSGRGLRCVFSRVYGEVAFFGEPAPGLLETQCPAHDFFAGPWARRPLSYTL
VTIGALGMGLYRDGDTAYLFDPHGLREGSPAFVAKVRAGEVYTYLTYYTQDHPEARWAGAMVFFVPSGPG
PAAPADLTAAALHLYGASETYLQDEPFVERRVVISHPLRGDIAAPAPPPVVGEGADRAPETARGATGPPP
PPEAAAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGAMEVVSPLPRPRQHYPLG
FPKRRRPTWTPPSSLEDLSAGRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPVPASVPTPAP
TPVPASAPPPPATPLPSAEPGSDDGPAPPPERQPPAPATEPAPDDPDDATRKALDALRERRPPEPPGADL
AELLGRHPDTAGTVVRLAAREAAIAREVAECSRLTINALRSPFPASPGLLQHCVIFLFERVLAFLIENGA
RTHAGAGAEGPAAALLDLTLSLLPRRTAVGDFLASTRMTLADVAAHLPLIQPVLDEGSGVGRLALAKLVL
VARDVIRETDAFHGELAELERQLRATPPAEVYARLSEWLLERSRAGPDTLFAPATPTHPEPLLQRVQALA
GFARGEEIRAAAEDREVRGALDALARGVDAVARRAGPLTVAPAPAAPGGQGAPRPPPLSPEAIRVRLEQV
RAQGQRAIEGAVKEYFHRGAVYSAKALLAGDARDRRFHVASAPVVPVVQLLESLPAFDAHVREVAQRARV
PAPPPLATSPQAILLRELLQRGQDLEAPADLAAWLASLGDAAGQGLVERKELDELARAIHKINERQVRRS
SGLAELERFEALDAALRQELESEAAFVPAPGAAPYADAGGLSPETRRLAEDALRQAKAMAAAKLTDELSP
EARERLRARARAIEAMLEEARERAEAARAARERFFQKLQGVLRPLPDFGGLRAAPAVLATLRADLPGGWT
DLPDAAQAAPPEVRAALRADLWGLLGQYREALEHPTPDTATALSGLHPNFVEVLRDLFPAAPETPLLVQF
FSDHAPRIARAVSEAINAGSAAVATASPESTVDAAVRAHGVLADAVAALSPAVRDPACPLAFLVALADSA
AGYVKATRLALDARRAIARLGALGAAAADLAVAVRRENPQAEGDRAALLEAAARAVTAAREGLAACEGEF
GGLLHAEGSAGDPSPSGRALQELGKVVGATRRRADELEAAAADLAEKMAARRARASRERWAADVEAALDR
VENRAEFDAVELRRLQALAATHGYNPRDFRKRAEQALAANAKTATLALEAAFAFNPYTPENQRHPMLPPL
AAIHRIDWGPAFGAAAETYAEMFRVDTEPLARLLRLAGGLLELAQAGGGFIDYHEAVSRLAEDLNGVPSL
RRYVPFFRRGHAEYLELCDRLDALRADVHRALGGVPLDLAAAAEQTSRLRNDPAAAAELVRTGVTLACPS
EDALAACVGALERVDQSPVKDTAYAEYVAFVARRDLAEAKDALVRAKQQRAEATDRVTAALREALAAHER
RAQSEAESLANLKTLLRVAAIPATAAKTLDQARSVAEIVDQIELLLEQTEKAAELDVAAVDWLEHARRVF
EAHPLTAARGGGPDPLARLHARLDALGETRRRTEALRRSLEAAEAEWDEVWGRFGRVRGGAWKSPEALRA
AREQLRALQTATNTVLGLRADAHYERLPAKYQGALGAKSAERAGAVEELGAAVARHDGLLARLREEVVAR
VPWEMNADALGRLLAEFDALAGDLAPWAVDEFRGARALVQHRLGLYSAYAKARAQTGAGGAAPPAPLLVD
LRALEARARSPPERHEPDPRMVRRRGEAYLRASGDPGPLELREATSELDLPFATSYLAPDGTPLQYALCF
PAVTDKLGALLMRPEAARARPPLPTEGLESTQTLAAMCTVPLITRLQLALSDAQGAGFRLFGRFVRHRQP
AWRDSMAAAAELYAALVATTLTREFGCRWDELGWARGAAAPAPLAEPAGSRRPRVTFNENDVMVALVAGT
PEHIYNFWRLDLVLQHEYMHLTLPAAWETGAGSILFVQRLTPHPDPEVRVLPAVPAGPPPATGLLFGTRL
ADWRHGKLSESDPLAPWRAAPELAAGGAAAALGGLSGPRALVAVSVLGRMCLPSAALAALWSCMFPDGYS
EYDSLDALLAARLGSGRTPDPQGGREDSPAPPAHALYRPSGQRVLVRGGAPDPAARVTVMDLVLAATLLG
APVVVALRSDPAFSRGSELELCVTLFDSRARGADAALREVVSSDVETWAVDLLHADLNPIENACLAAQLP
ALSALIAARPLARSPPCLVLVDISMAPLFVLWEQPDPPGPPDVRFVGSEEIEELPFVSPGGDVLAGLAAD
GDPFFARTILGAPFSLSLLLGELFPGAPVYRRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAIL
PDEPVGEPVHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPD
APPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGR
VSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQ
ASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPS
PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRS
PAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ
PPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASS
LALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGAR
ESPSSQFGPPPLSANAALSRRYVRSTGRSALAVLIEACRRIRRQLRRTRHALLDRSGAVLTGLYHVRMLL
G
>gnl|CDD|223022 PHA03248, PHA03248, DNA packaging tegument protein UL25; Provisional
MRPRYEFDALSVDLHDPGRRFIVADARNFIAPPFPLEFWTEPAFTLSRETAAARLALLEARNRAAAAALD
NLAGQAATIPVEVDRRLRPIERQLEEVADALADLEEAAAAAEEADAAADERKAAAGDGDGRAAGEDDEAR
EVQIVKNDPPLRYDTNLQVDLLTMVYAGRGAGGSSGVVFGTWYRTLQDRLIAERPLAARSIDYRDGRMSR
TFMTTAITSLQSCGRLYVGNRHYSAFECAVLCLYLYHRTASNINDRHPSTFEGLIEQLPTYLDALSEAIG
DEWGRVSYRFDRDRLPKDQFAAPGGGRYERGALSGHSVLAALKRLGVLPAAPGDVPRGAIADVDPDQVAY
VDEVNRAAAAFLGRAQNLFLMEDQTLLRATINTITALLLLRRLLWNGNVYADRLRNNFQLGALVPGAVPS
AALARGASGDDSGAVKSGDNNLTFLCERYVAPLYRADPRVELTQLFPGLAALCLDAQAGRHGAPARRVVD
VSSGRYQASLVRLIALELENRSRTNTVPVAEVIAAHDAVALQYERGLGLLMQQPRLRAALEETRRLGQFN
VESDYDLLYFLCLGYIPQFTSAA
>gnl|CDD|223023 PHA03249, PHA03249, DNA packaging tegument protein UL25; Provisional
MSSRRRSSSRRSGEGATVIYIPSSLEDEVFLDPRPRAPTEDLDRMEAGLSSYSSSSDNKSSFEVVSETDS
GSEAEAERGRRAGMGGRNKATKPSRRNKTTQCRPTSLALATAATMPATPSSGKSPKVSSPPSIPSLSEED
EGAERNSGGDDSSHTDNESTQSQPEADDEPDLAEGHEFSFCDSDIEDFEQECFERSLADNLGFEPSVVSP
PNVEFLKFVLYDFSVQHITRVNQCIPMPAFALTSLVDPVAKNVSPGERDLTRGIVTHAVLINYYYQAKAK
ARHMQCALNATIHGQTVRNIAAYVTNQTRGGRAAALALHFLMSQKAVTDGQYQACLRRLDEELRKRGTTE
SPSLTEVYETLRDYNVLFPIAHYTNRGALYLYRQNLQKLNNGHRGVLKLLSSEKLNEEHTLNDLAFLVGV
ELMLVHFERTIRVLRCYIQHQLQNLSELIYIIYVQLPSLRGDYIQLTEAIYWATSSHGDEPLFQSTTALF
DFLRAVRNQDAFICTDYVMCALRLWACPDREAEEDDGPGDSYDNPVGDFMFRDPLLRDPRCGDTRTKLLT
RDLCFTRMQARPTSRHTPVEHVLVPTASLNKPFLRCPPEEREEDTLRNLALKAFMETNGNHPESQLQHQQ
HPSSPPPGNGDRARAGGSGPSSP
>gnl|CDD|165509 PHA03250, PHA03250, UL35; Provisional
MSEAPSEPDPPRIPELPIDERLNFRPDLLSDEHIRLLLDALTQGCLGYVGALNSGLPMPPYELEALIDVQ
VRHQFTKVRQVAEPVIRICILANHYYNSRRILVDLTAALDRLYGPPDKQRLERGLRRLCRALNSDDNPYD
LSEALGDTDLPTGVYKQHLRHLYRLRDALGLDVEPEARRDYSTLTVFNLLYLPPLFTTQEAVELYAENLA
DITQRNNRPFRLLTVIKRSKDPEDVLNDMMFLLSLRHLQFRHQEELQALRKWIVLKLNRLCSDLYFAYTQ
VPETRQTFRNLARELHLLRQSRSPEDPAFRPVLANLLQFLRQLHEADVYLCPGYLHFAIFALLLRLYNLR
DATHCAGLDDDLEGQESAELEVDPTSPYSEAFYLAKNPYGNSNLFRCPRDLSRYLGRGLIRRTMTQEIIY
NATDGTVTYETYELDSQYSLIMEGAARQLGLTPEQLMAYLEATPAPLGTDTEPDGEPEADLFADVSRRPA
RPSSKDLERPPGGRRRMASVPGFRPYSVARRGRRRPPPPAPRGPAHTSAQGPDSSGSESGSDLEDPRDRL
AEAL
>gnl|CDD|223024 PHA03252, PHA03252, DNA packaging tegument protein UL25; Provisional
MSLLRTFYQLPIVPIYEGHVRNILRCPEEDLRRLRDDSALRLRRYREDLLRDRLLRRRLGEELDDLQKRL
QTECEDLRSRVSEAEALLLHDASGGEGGGATNGGEVNVDGGADRTWLAQSPERPADGGPSGERVNQFGIT
QNDPFIRFTTDFRGELINTMFNNAQMWTFSFGAWYYRLKRWLYNQPRWRRVYKLTQVDSLSISQELLMGV
VNALEQVTVYPTYDCVLSDLEAAACLLAAYYAALEDGRDDPTSVVGVLTELPRLLRRLADDIAAEIAASP
GGGAANYFAYRDPPGMKYYVPLSKGRHYAPGTFDEHVLVRVLLKRGVIQQLPGYKASTSRVVEERLSGQV
RDDVLSLWTRRLLRPKLGGEVPIFVHEQQYLRSGLTAIESLLLLWKILNSESVFAGRAGKFTLTDVFPQL
AGADDALPPGEEEGFSGGNVRNFEFLMEHYVVPWYARDPAVTISQLFPGLVLLAVNESVRSGWDHSRRDD
DQASASGGASGAALVQQSKSNPVVEYMFAQSEKQYADLARLEAHDALLFHYENGLGRLLSVALPRHRVLA
LGSSLFNVNDVYDFLYFLVLGFLPVVAVT
>gnl|CDD|223025 PHA03253, PHA03253, UL35; Provisional
MVTHAMEQQKTFNIPTFVLDENCNFIPEVLSRANAKFIKDVLIADSYNSVCLANSFIPMPIQTLEQIMVI
ITKFKFSRSRDLLFPVIRLGVHINRFYAGKKQVKHMITMMKSLFDTEEAMRRLDRALMGLFVDARTNSYM
PLIALSLHENGLPDSKFMKAVKLIYTTGNSFHNRPDADIEQYAEKLRAYNYLYKIPKYTLKEAVDLYSEN
LKDLSIGVNKKPTLLFTSSDDFYLSHIYNDVLFLTSTWNMIYNCKKEIRRLFTWIKYEINSIMENVVLVG
FQLPDLKETILDLAALISNMNLVKPDKDLFPHYKLILNKLFEIGIFATKANICILPSFIKSHLIEFEDVL
KRSNDDEDLNYLLLKSKDSDDEYDEDKPPIQVDPGRVDNVLTDSDFFNVTPENAFSSIAIMPISYDKIID
VENNNIQVLEVEMQSLSAVVYGAVAQKYGLSLKQVIERLNVNEGRSSSRASPSHSTSTIPYSPPQSGRST
PTSILRQRTPIRSNSRSSSVSFSQGDSNRSHYSDETNISDYSYPMADLDLEDEEPMEDHPHSPQSISSNN
SMSRTSRALQNSQRRRPPTMFPSSSERQQNNARLRRRTRRSTETNDERL
>gnl|CDD|165513 PHA03255, PHA03255, BDLF3; Provisional
MAHARDKAGAVLAMILICETSLIWTSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPITT
TAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGTGTSTGVTSNVTTRSSSTTSATT
RITNATTLAPTLSSKGTSNATKTTAELPTVPDERQPSLSYGLPLWTLVFVGLTFLMLILIFAAGLMMSAK
NKPLDEALLTNAVTRDPSLYKGLV
>gnl|CDD|165514 PHA03256, PHA03256, BDLF3; Provisional
MSAPGCSERQDKKRGTIGEREFGELLSWDPTDLPRTVARVYVAVGGLFEQEVSEVQRLENICTLLDLAGV
ECQTKAD
>gnl|CDD|177569 PHA03257, PHA03257, Capsid triplex subunit 2; Provisional
MTSDGFEVEILLPGGLSRADASALQKCEGRIVFLPTLRRRVALADVALKSFYVNGAEPDTLSLLAAYRRR
FPAVITRVLPGRMSAVALGVGPLPPGLFLQNTGPFDLCNGDAVCLLPPIFGGEDRLRLESVGLELLFPMT
VPLALARELIAKVVARAIEALNRNQRPAGRLRGADVVFYNGRRYDLTPDIQSLDAVNAAARTLVLNMIFA
INEGCLLLLSLIPNLLTLGAQDGYVNALLQMQSATREAGQLINPPPPPPPQDGARRFPVYEALSAWISMA
SRLGDALGLKPVLRVCTFDGPSTVRPGDLAPVIVPL
>gnl|CDD|165516 PHA03258, PHA03258, Capsid triplex subunit 2; Provisional
MAVDKKIVVSLTSRLFADEIAKLQEKIGCILPLQDSHGLQNLQSLGLGQVYSRETVPDYVAMYNYLSKCT
LAILEEVNPDSLVLTRIDPGQTYQIKNKYQPFFQWDSHTQLSVIPPVFGREQATVKLESNGFDLVFPMVV
PTPLAQEVLQKLLLYNIYSRVVAAEPNDVNMAEVLLYTTNVSYMGRHYVLDLDEVNPSGALALLDNLALY
LCILSALLPRACLRLLTALMRHEQHELLNVFRGMVPDEVARIDLNALSVGDDITRMGVFMTYLQSLSSIF
NLGPRLHLSAYSSETLTATCWLSS
>gnl|CDD|165517 PHA03259, PHA03259, Capsid triplex subunit 2; Provisional
METTVFCTFEQKLTLSDVGKLAKLIGAVIPIPQRHHLIGHTQLGLYQIVDSTRDYARIRTLLRNMTLTIL
RRVEGNQLLLGVPTHGHLYTIKNTGPVLWEKGDTLTLLPPLFTGSQEKLLSLGNWELVLPWIVPTPLATE
INQRLLCIGLLSLDRSYEEVRAAIAQLRTIQYRDATFTLPDVVNDDTLLYDMKTACISMSMIANLASDLV
QTYVRKLALEDSSMLLIKCQELLARRTRDRGGGGENLPGRRSGHTSPKDELAKLSALFVMIRQINDLINE
QPAFVVCDVSPDNKSATCIFKG
>gnl|CDD|165518 PHA03260, PHA03260, Capsid triplex subunit 2; Provisional
MGFFGLMSDGWIAAQSLHGAEFKAPPLGEKMIEDLPPRIVASMGIFVRLMARNDEGAKLFHPSFHGEKRN
VVNAHFPAHHDGPKDRVAFVQDDLAGDLSAGLIHAECTPMKQQMVVHTGADPLIPCEDCFVVSAPDCDDM
AAQQKCVWLNDALAPAGGSAIHNLMIKLAGGLLATQKIAADAVDDLGHKMKRDIDLFNALDQEAAHTVGC
DALQFALHQLYSAFKLHAIFIDGAAQPTTAAAIIAAYADFVEGKNAEPPSLDEMKGLIADAKLKMLMCDG
MAAMVDYYKLIKQDTCGTVLSSFFNNPPCIAGEAMVGPQCGHVDCGSAFIAFIFKFNGI
>gnl|CDD|223026 PHA03261, PHA03261, Capsid triplex subunit 1; Provisional
FIQIGNGLRMLKPLPRFAGVGAALREAAGSLGLHSVLRPIGAPRDGGGLTRGAANPRLTGTLLWLLGLLT
VTPRSITIANMDGIQITSAATLVAALLRAISPLLDTSQPRNVLTRQVTLTDFCQPDAERPGSPVLALRHP
LDIIGLAASSTPPGRDPRDLEEAWRALSEACGLGVTRTEGGGLRASLVSLNFLVAARAAEYRDKCAAEAL
RAHVIANYGDRRMEARLDRFGECLQAMVRCHVFPHRFLSFFGGLLSWVTQDELASVTAVVRGPQEAARTG
QTARPRSSVYVPACAFLDLDAELILGDDGVKFLYLVFVYTQRLGREGVRVYVAKSQLPERGFEDALGFLF
GRLRAENTIRGTEGADAPAPGRNAAFPLAQLANDPAAPRCSPGRLTNPDATARLYQWAPDLRGRPTRNSC
MYAAYCRLGTLPSDSPRPTRRTERFGSVDVPVVWLEGVVWDPGDWRECY
>gnl|CDD|223027 PHA03262, PHA03262, Capsid triplex subunit 1; Provisional
VRSILARYLYGADHQAITARFFVPEGLLEPEQANLGMLMFRLETGAESPRYLLVSLFFLAINAFNVSAAT
RTALAALYTSSPVDAVLAWLDTGSYRLHRKVSPVGCTNSVSPGITCLLTCVMQGHVYNTLKTEIYPLVVP
KDMYLELDWEERQGEIQYVYLVIVYDYNGPEGKPGIYVVLSSVRHRHTLVDLLRQRFAKERFLFLNRLIN
RPNQILLCFGVVQRLGWCLTDDIKSGVLTYKGIQLSVVRLEKFYVDLGEFKEFV
>gnl|CDD|223028 PHA03263, PHA03263, Capsid triplex subunit 1; Provisional
MVKSREDNYRKLQRDLLRLLPPPTHKLSLTRGNKFARGVRDLVSKYVSSIGGPESMFRDGFLDPPFRQPL
YGDFLVHAKTFSNQEPRGTPLFCFKQEDPGSSIDVLFTPISLFRLSGLPADAAPGVHRIANVWYGSDSGL
EDLIPNLRELLEERNFHTFLTPVGPLVENIKSTFVNKITSVVKGPVVSNESPQENVKLVLPSDLFVDLDA
CCPSGLGRQPSPLRSTYYVALTYVRVGNRPKMALTFFKSNKGLCEVMNLLRDYYSDVIRNKYIVLQDDLY
INGLTFGAVCRLGTSSSDSGPRRQSLHFRGSSLPVVEIPDFVADPGPWTVIL
>gnl|CDD|223029 PHA03264, PHA03264, envelope glycoprotein D; Provisional
RRLALLMVLGALLAAAVALPTPAPRVTVYVDPPAYPPPRYNYTERWHTTGPIPSPFVDGREQPVEVRYAT
SAAACDMLALIADPQVGRTLWEAVRRRRRTYNATVIWYKIESGCARPLYYMEYAECDPRKHFGYCRYRTP
PFWDTFLAGFAYPTDDELGLLMAAPARLNEGQYRRALYIDGVVAYTDFMVSLPAGDCWFSKLGAHRGYTF
GACFPDEDYEQRKVLRLTYLTQYYPQEAHKAIVDYWFMRHGGVVPPYFEESKGYEPPPAPSGGSPAPPGD
DRPEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDADRPEGWPSLEAITFPPPT
PATPAVPRARPVIVGTGIAAAAIACVAAAGAVAYFVYTRRRGAGPLPTKEKKLLAFGNVNYSALPG
>gnl|CDD|165523 PHA03265, PHA03265, envelope glycoprotein D; Provisional
MSTFKLMMDGRLVFAMAIAILSVVLSCGTCEKAKRAVRGRQDRPKEFPPPRYNYTILTRYNATALASPFI
NDQVKNVDLRIVTATRPCEMIALIAKTNIDSILKELAAAQKTYSARLTWFKIMPTCATPIHDVSYMKCNP
KLSFAMCDERSDILWQASLITMAAETDDELGLVLAAPAHSASGLYRRVIEIDGRRIYTDFSVTIPSERCP
IAFEQNFGNPDRCKTPEQYSRGEVFTRRFLGEFNFPQGEHLTWLKFWFVYDGGNLPVQFYEAQAFARPVP
PDNHPGFDSVESEITQNKTDPKPGQADPKPNQPFKWPSIKHLAPRLDEVDNVIEPTTKPPPTSKSNSTFV
GISVGLGIAGLVLVGVILYVCLRRKKELKKSAQNGLTRLRSTFKDVKYTQLP
>gnl|CDD|165527 PHA03269, PHA03269, envelope glycoprotein C; Provisional
MKPFIIILIITIACINLIIANLNTNIPIPELHTSAATQKPDPAPAPHQAASRAPDPAVAPTSAASRKPDL
AQAPTPAASEKFDPAPAPHQAASRAPDPAVAPQLAAAPKPDAAEAFTSAAQAHEAPADAGTSAASKKPDP
AAHTQHSPPPFAYTRSMEHIACTHGGIQFIPYFHKFILPCYLQIFTGQGAAFKQHELPKTYEEDFLDPEG
ANITRWKPLIRPDLHIEIWFKKHLIDPHRQDGNALIQMPDLPLILLSNNADLNLIMNPDIFNHAKEKYII
PDRKTTSDFSLHILSLDASTEGTYIWRVIHTANKNVINEHHITVMSYKRPNITVIGDPVLLGNPYAAYCK
VNKYYPPHSVIVKWTSNFGNIGKNFITDAIKENADGLFSSVSALHIPAQKNADYPPPAIQCNVLWIRDGV
SHMKYSAAVTPDVYPFPNVSIEIIDGHIVCLAKCVPRGVVHFNWWINDIPIEHENSEILGVCDNNKRFVN
LQSSCDTSELDGPITYSCHLDGYPKKFPPFSAVYTYDASSSASTFPLIAAIIGIISIIGILGLIALIATL
CIRCCK
>gnl|CDD|165528 PHA03270, PHA03270, envelope glycoprotein C; Provisional
MGWRAAGLGLGLWSLLWLLCAGAGAPRGAVSNASEAPTSGSPGSAEGPRTTPTPTRGKGTPTGPASPPKS
GPPKSPPAPFRCKRPDVLARYGSRVQIRCRFPRPTAEFRLQIWRVAAAPSEEIRPAPIEPGAVLVNVTAP
PGGELVYDSAPNRTDPRVRWAEGAGPGARPRLYSVEGTFPTQRLVIQELTLATQGMYYWARGPADRPHRY
GTWTRVRMFRRPSLSIRPHAVLEGEPFGATCVAANYYPGDRAAFRWFEGGDEVFAPERVRTRVDAQRDGF
SATSTLTSEARAGLAPPRNLTCEFTWHRDSVSFSRRNATGAPTVLPRPTIEMEFGGDEAVCTAACVPEGV
TLAWLLGADPAPAEKAAVAGGPCPGRPGLARVRSALPLSREHSEYTCRLVGYPATVPVLEHHGRHEPPPR
DPVGQQVTTALEWAGIAAGVLAAIGLAVGVGVYVRRASERRRRVRR
>gnl|CDD|223030 PHA03271, PHA03271, envelope glycoprotein C; Provisional
MHASRVLRALGWTGLLFLVLSSGRVLSASLNPDLATPPVLAFNPSSISADGGPLAEVPASPPTELSTTVA
TKTAVPTTGEKSESHKNANDAHKMPSIVCDKEEVFVFLNKTGRFVCTLKVDPPSDNEWSNFALDLIFNPI
EYHANEKNVEAARIAGLYGVPGSDYAYPRPSELISSIRRDPQGTFWTSPSPHGNKYFIWINKTTNTMGVE
IRNVDYADNGYIQVIMRDPFNRPLLDKHIYIRVCQRPASVDVLAPPVLSGENYKASCIVRHFYPPGSVYV
SWRQNGNIATPRKDRDGSFWWFESGRGATLVSTITLGNSGIDPPPKISCLVAWKQGDMISTTNATAIPTV
YHHPRISLAFKDGYAICTIECVPSGITVRWLVHDEPQPNTTYDTVVTGLCRTIDRHRNLISRIPVQDNWQ
KTKYTCRLIGYPFDEDKFQASEYYDATPSARGSPMVLTITAVLGLALILGMGIILTALCFYASGRKYILL
>gnl|CDD|223031 PHA03273, PHA03273, envelope glycoprotein C; Provisional
MWLPNLVRFIAVAYIICAGAILTYASGASTSSSIENSDNSTAEMQSTPATPTHTTSNLTSPFGTGTDNST
NANGTESTTQASQPHSHETTITCTKSLISVPYYKSVDMNCTTSVGVNYSEYRLEIYLNQRTPFSGTPPGD
EENYVNHNATKDQTLLLFSTAERSVKSRRGGQLGVIPDRLPKRQLFNLPLHTEGGTKFPLTIKSVDWRTA
GVYVWSLYAKNGTLVNSTSVTVSTYNAPLVDLSVHPSLKGENYRAVCVVASYFPHSSVKLRWYKNAKEVD
FTKYVTNASSVWVDGLITRISTLSIPVDPDEEYTPSLRCSIEWYRDEVSFARIAKAGTPSVFVAPTVSVT
VEDGDAVCTAKCVPSTGVFVSWSVNDHLPGVPSQDMTTGVCSSHPGLVNMQSRRPLSEENGEREYSCIIE
GYPDGLPMFSDTVVYDASPIVEDEPVLTSIIAVTCGAAALALVVLITAVCFYCSKPSQAPYKKADF
>gnl|CDD|177573 PHA03275, PHA03275, envelope glycoprotein K; Provisional
MLLGGRTEHLIILCLLTAYAAFTLWYTLRAQFHNPCVYATASIDGGAVRWELYNSSLVYVTPENNHSTFL
DGLSGYDYSCRENLVNGDKLDVLKNSKPLHDKVRIVLGTRNCRAYLWCVQLKMIIGAWLVYIAFLQLRQE
RRMFGPFRNQCEFLSPTSYTLNYATYVLATTVLKTPYTKLARLLCEVSLRRVALSKTFKRDPIGFLCEHK
AALLLIALEVFAHIVARCLVLGTVGIVHTPCSLLYPLYLKIAAWVFVALVAIVELVAIVYEKPPKTGSSN
NGPTGATHGIRGVCTSCCSTVLAGLAVKCVYLALFAGAVIILLHYEQRVQVSLLGESFSS
>gnl|CDD|165533 PHA03276, PHA03276, envelope glycoprotein K; Provisional
MLAVRSLRHLTTLCLVTAYGLVLGWYVVFGASPAHRCIYAVRPAGASNDTAPVWMRVNKSLLFLSGPRAP
PEDPRDPAALCRADVIGGHAVSLPAPPGGMGRRVMNVHEAVNCLAALWDTQVRLVAVSWFLYLAFVALHQ
RRCMFGVVSPAHKMVAPATYLLNYAGRVVSSVLLRYPYTKITRLLCELSVQRQSLVEIFEADPVTFLYHR
PAIGTAVGCEILLRFASQGLIVSTAIIPWGACAITYPLFLNITTWCFVSAILLAELYFVLRGGSAPPGAE
KGPRPPRRGGLAGVCGRCCSIILSGIAVRLCYVAVVAVVVVVAFRYEQEIQRRIFDA
>gnl|CDD|177574 PHA03278, PHA03278, envelope glycoprotein K; Provisional
MLLGGRIAHIAILLLITTYAVLLVWYGSTLAKLGHGCVYAVLPLGELSDGKNFTWEAYNSTLIYVPLGNK
NALDFSGFDDICRTDLVNRTAIGGLAGDEALRGRIRIVVGARNCVAYLWKVHIRLATLAWLLYVAFVYLR
QWRRMFGVFRNDADFISPTGYTLNYAARVIAATLLHCTYTKMARLMCELSIRRNALSRDFKEDPITFAFR
HPTAAILILLEGLIRLGAQCALMGTVSVFFVPCAAVYPLYFKIITGIFVGIVICLELSLLLYPGPARKKA
MGGEAAERKGGRVMSGAHGVCSNCCATLLSGIFVKALYLLFIIGLVVLLLRYERALQIALFGRAYLP
>gnl|CDD|165536 PHA03279, PHA03279, envelope glycoprotein K; Provisional
MLRPECLKLAAIIAGIIHIIFLVWFVCSKISLDNKDDCLYALANIAAQVQLGELGANMSTETKLLIPGAA
AFEPVHQGPATFNRSLVYVINKDAQLLYNNRENHDGRCFAGAFFENDMAAIMKLIPDAKEQVLSLEMADC
MAHLVFFDQRCASAAILHMLAFLADNCQRRGFGPWLCRANALRADAYHLNYWTAFAARLFLKVPYLKLQR
FLREFEHRRDCKSLNFSADPLGFCICHPGALLLKAIEIGLYFASLIASAMTLRICFDPCAVILHEHVKIF
AWVFVAALAALELLSAIDHLRRETRPAKDAAAAIKPPNIIAACCANIASHLLLRALCGAAIALIVIGAFK
YEQEIQNKLFG
>gnl|CDD|165538 PHA03281, PHA03281, envelope glycoprotein E; Provisional
MGTVKHPMLGLICGTLSFGIIIGTLAIANAIKAEVLRYDDFDMDEDGLDGDDIYEPYYHSDHAESSWVNR
GDSINAAYDHERPFIQDKNDHKMETYTDGFLENAHEHDGQINQERGIDSGERLMQPTNMIAAEDLGDDNG
EHVDLTLNGDDKHKIMKHDHRNFGDASILFKGVHDINHKHAGQRLIEVSVAENHPFLLKAHIPQENEHRY
TERWSFLPAAPCKGDAAPAIQHICIKHGACFHDVVVDVDCAAESKEDQLAEIGYRFHAKKAADPPWIVVN
ISEDFAELEFDPPDIEPGVLKFEHMEAHHAGVYIWNLQGSDGENMYATFLVKLKGDEENHIDLPAVTPKP
KGAEFHMWHYHSHVFSVGDTFSLAMHLQYKIHDAPFDLLLEWLYVPIDPTCQPMRLYSACLYHENAPQCL
SHENPECTFASPHIAQRVANTVYQNCEHADNYTADCLAISHMEPGFGLEIHDGGSALKFVDAAESLSGLY
VFIIHFNGHVEAVAYTVVSTIDHFVNAIEEHGFPPEAGNPPAPSKPKEIANNDVISEPGTFPFKRYAAIT
GGFAALALLCLAIALICTAKKFGHKAYRSDKAAYGQSMYYAGLPVDDFEDDEETDTDEEFGNAIGAECGG
SGYTVYIDKRTR
>gnl|CDD|165539 PHA03282, PHA03282, envelope glycoprotein E; Provisional
MDRGLLVAWLLGAWVVAAAPETTWKHASAGDDVVLFPLPAGRPGAPPRKLLWAFEPMDACGPLRPSWVSL
RPPGQVLETVVDAACVRAPVLLAAWYGRPDPAATGGLAPGPEFAWPPRVAVVNGTLVLREARETDSGMYV
LSVSRAPNSTAARAVVFLVVGPRPVPTPPGGTPPPDDDEGDEAGAPATPAPPLHPPPAPHPHPIAEVAHV
RGVTVSLRTQTAILFSPGDTVHTNVSIHPIAHDDDPYVMEVVWVRFDVPEECGEMRIYEPCLYHPQLPEC
RSPADAPCAASVWTERLAVRRYGPCSRTVPPPRCPADAAMEPRPGLGWYGHTVNLQLRDASEASGGLYVC
VVYVNGHVHAWGHVVISTAARYRNAVVERSLPRYRPPPVEPTPSARPPGPRPAARGALRLVGVLGAALGL
AAAGLSVWACVTCRRARAWRAVKSRDSGTPTYIRLADDELYADLSSDGEGEDSEVYDSDPDRLPGTDSPP
KRGSGFQILSGTKPDPWSPGARSRRDLTTFRSDDPDRYRDSQAPDPPHRR
>gnl|CDD|223032 PHA03283, PHA03283, envelope glycoprotein E; Provisional
MELLRAARALAFFALITVLDAWGVHQVELSEGAWAMIDGRGVLTPTNTTTRVTKAWTFLETPPGCAGDVS
VKKVCVSTSLCEDDIVIGKHCNLLTGEHGIALAEFNVVNGSLQRTKDVYFVNGTVFPILTPERSVLQIQR
ATPNIAGVYTLHVSSDGMMKHSVFFVTVKKPPKQPQTPPAPLVPQVPARHHTDFHVRGYHSRVYSPGDSF
DLSVHLESDIGDPSFSATIDWYYMNTSSSCDLFRVYETCIFHPTAMACLHPEDPACSFTSPARATKILHR
VYGNCSPRGDRWPSRCHSTLLGNRPHFIQPAQNRVDLLFKNAPASASGLYVFVLLYNGHPEAWTYTLLST
AAHFMNVITDLTRPRLGEHAIYTDLGHGVTTPHPSAATTNELGAWTRHYLAFLLAIICTCAALLVALVVW
GCILYRRSNRKPYEVLNPFETVYTSVPSNDPEVLVFERLASDSDDSFDSSSDEELEPPPPPGPAGQLGPY
VSLDAEDAFSGRSGFKVWFRDTEEASPVPLHKPTVTGPDYSRVASRLKSILK
>gnl|CDD|177576 PHA03286, PHA03286, envelope glycoprotein E; Provisional
MRACRLSILILLLQTISASMINHIDLPEGQSATVDIPRYPPVVDGTIYTETWTWISNICNETATGYVCLD
SATCFQDLILGTSCVRYGEEKILRTDRFVVNSGSLKRIESSQLHYIPNVIIGTGRGKELTILNASSQNAG
IYIRYSRNGTRTAVMDVLVVWVSGHGRARDPTMNIPITPPSTRVDLSLKNFKAFLYNVGDTVDASVTAHL
TNWAGAFSLEFRVLFLPYNPKCKYLTIYEPCIFHPKEPECIMVPEHSECRFASNMDVLQIAAARSDNCSV
GVRGCTYDTSVDESVQGRLAFLESDIPSFRLANAQPTDAGLYVVVALYNGRPLAWTYVYLSTLETILNVF
EDVHKPGFGYNAVSANDPGNFTAAPTHTIAFKEGPTVIYSLLVSSMAAGAILVVLLFALCIAGLYRRRRR
HRTNGYFQAYPKYMSLPSNDEGDFNSPLSNTCEGLSRGLANEKSRTPKQKGSRYHAWLADGGPAARIRRR
EV
>gnl|CDD|165546 PHA03289, PHA03289, envelope glycoprotein I; Provisional
CMVCVTLILFCLIIGTQSMVYTGTSVSTSTDQSAQVAFCGLDKVVNVYGKLLFLGDQYLEESYSGTTEIL
KWNEANKCYSVAHATYYADCPIISSTVFRGCRDAVVYARPHDRVHPQYEKGLLLTIIEPRMSDTGIYYIR
VSLAGRNKSDIFRTSVFVCSSSSGSCSHPRQKVQDEMCIRYVDRIAFENYLIGHVGRLLYGDSELHAIYN
DTPTSAPTYRTIRRTTFNEGLLTAKSSPDIDLNATNLPLPISNYTDYMSVILRRVLPRLIYMSAYLVLCI
IALLIVTVCSACKSPRRRIYIGNEPSDLTSLINSAVNEKFGCNPETKNVPSDISEAELLERLEKKIEMLE
TE
>gnl|CDD|165547 PHA03290, PHA03290, envelope glycoprotein I; Provisional
AFIIQCLISAMIFGIQCAAAIIFKGDHISLQVNSSATSIFIKMGNDNDAEIKGQFLFIGDQFPTGNNYNG
TLELLHADQTAFCFQPLQRIMYDECPRIRTGAFIACRVKHSWHYENATDRILTDPDAEIIFKINKPGIED
AGIYLLLVQLDHSRLFDGFFLGLNVYPAGDHHNIEDVIYFPPSLQNGYSPRAIFNQAKICDKFATHKGME
QSIFQHILDLDADKELEDLPWLHDDLGSTEKKSVVKEGFENDVKPNDMHELPEKLLEDPADNFLIAIPIT
ASLLIILAIIIVITIGIKRRRSIEKHKIYRPKRKKEQAITEKNARPESDVLLEAAIAQLATIQEENPPHS
VINPFTK
>gnl|CDD|223033 PHA03291, PHA03291, envelope glycoprotein I; Provisional
MGRPLGFLLALGLWACAAGVVVRGPTISLVSDSLLAAGAVGADGSVLEDLEVPGELHFLGPQVPHTTYYD
GAVELFHYPPGDRCPRVVLVEELTACPRRPAVAFTLCRSTRRTQSPAYATLTLDLARQPLLRARGAARAV
VGLYVLRVWVEGATNASLFPLGLAAFPAEGTLAAPPLGEGSADGSCDPALPLSAPRLGPADVFVPATPRP
TPRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPQAGTTPEAEGTPAPPTPGGGEAPPANATPAPEASR
YELTVTQIIQIAIPASIIACVFLGSCACCLHRRCRRRRRRPARIYRPPSPVAPSISAVNEAALARLGDEL
KRHPPESPRRSKRRSSQTMVPSLTAISEESEAPAVVELSRSPRRPGGPTAR
>gnl|CDD|177577 PHA03292, PHA03292, envelope glycoprotein I; Provisional
MAKCALLFWAAILLAIAACATGIVYRGEHVSLYLDASSEFAVYPTDASLVLVGHLIFLDGQRLPTTNYNG
TIELIHYNYSSDCYVVIQTISYESCPRVANNAFRSCLHKTSRHNRDYFRVNASVETNVLLNITGPQPADS
GAYILRVKLDHAPTADVFGLSAFVYDFDSPTVPDPEPTTARPEPAAGYVATPTPRYLNAVTTSTYSRSMS
SQPAGAATATPTPTLDTGLTTVAPPNETVVTGETALLCHWFQPSTRVPTLYLHLLGTTGNLTEDVLLTED
SEILRTPPPDPSSSRSPGAGDDFKQTNSTSPKRRNKIVAMIVIPTACVVLLLLAVVGAIINGAVRKHLLS
CASRRIYRPRQGGASSSERRRLTCGPTPAASSESLADDTTVSPPSSKPKAKPKRKLEAIKEES
>gnl|CDD|223034 PHA03293, PHA03293, deoxyribonuclease; Provisional
MASSPLAKRDSPPLESRRRPREILWSAVALPSALPPGVAAETFEDYLLGLLRGVDSPLDVEPLYHRLAYI
RDLVKRLESEGLVDGGLASHLLGLERPALFTSGTNTPAEELSSNLPAADARDILLFVEAATRNQAECDLW
ALLRRGLLTASTLKWGANGPCFPPQWCKVNTGARGIPQSAAVAFGRTNEPLARALIEAYCVGPSTDDGGT
DPDDGEFFVFDEPVGSPPEEAYACGLLIDARTGMVGASLDMLVCDRDPHGVLAPHPTQTTLEFFEIKCRA
KYAFPPDDGSPLSQAYERLLARRTAAALRAFLRSIRNPGVEYFAPDRVPGAAEALITCDDAWKPGRAAGE
ARIRCSAFDRRHLALNRNVSSRVWLFGEPDLETNTITPAAWDTGELALEVPIFANPRHPNFKQILVQAYV
LSGYFPDRPLRPHLVTFIGRHRRPCEEGRTFRLEDGPGALYAALKCSIPPEQAIPVLLIITPVIVDREIY
EDIESAGREAFDETVKELWASRSPAADSAAAAS
>gnl|CDD|223035 PHA03294, PHA03294, envelope glycoprotein H; Provisional
MMRRLAVLALLLLALAALAGATPAPATPDEGGRATYWVGQVDAWFRARDDFRDTNFGRLWIPSLPNGADL
STIFLRPPAEFVLTGASSPLGQLLFVLPTALLGQPTFAKLPARAPTGRLPPPVAPLSGLLGNPNLAPYLR
TRHLVDFSVVPDPRSLTRWVFDRSDTAATKAHPSGVALPPPRAPPPRNTTDPATIKPNDHLNPATTFFLD
AELLLRTPKRSVYVSPFAAVWPVDYWHTGELVFGCDAALVRARIGVGFMGLSISMRSSPPLEIIVVPADV
NLRMITPPTSGLPLEPPGPPPGPRYRVYVLGSGNNASDGSMYKAMREVAAYPEESLDYRYHLSRAHAEAL
LMLAEAESLDDRPYYFYRIAARLATALFAFVEAARASGYVSLDELIDVDANLRLLARLLMRGAAGCAADT
IFLGTDLWDAQADVLLELRLKLFADISVGRALRSPVYEALLLRSAYALSDPKASAAVLPLAARLIDALYA
EFLRDRILWNPTARHALFFAVASLLQPAAGAPEWEALERARRALLLATAMCTAEHAAAAALDLQEALARL
DARGTPFSLLDVFSPCMASLRFDLAEEAHVLDLLSAVPRRPALDEALEQQTDGGEIKELEAKAVGSLTTR
RAHDIALLRAFAPELFSCSDGPSLNAEALLVLPITGNASYVITRRAPRRGLTYTLDGVDVANPLFITYLR
ATCESTSGNIEPVRLPRPGNLKDCLYCGCVFMRYTPSGAIMDLIYIDSKDTQRQLAAGGNSTIPVFNPTL
HGGPSTALLLFPNGTVVHLLAFESHRVATISPTYLAASVGGALLAVAILYGIAKMLCSNVRNRGY
>gnl|CDD|223036 PHA03295, PHA03295, envelope glycoprotein H; Provisional
MRRMLILLLVLLLLTPCYAAYGAGPRSPPGPIHFLRSNSTRCCVNNETRNQTVVREGLITFNFYEDGNTY
RVYQVPRCLFGTPVAEELLNSVDLTETLESYRRRFTRYFIVSNDYGAYRLFGHSLQADLSLPTQALTVPP
PELLPMQDVYMTGSPYVVNVSEIHRPAFNQTCCLFPNHPLLFPMTVPCSHQTLNWEQYVVTLSLTPDFFV
LTIQIDDTDLLLIFGDVRRIDFKAPYRKSNFILRQTERHDLLLVVKKDTVNVRYPFLKDQDFLDDTLSGN
YLDLSALLRVFNRLAIQVLLEGLCGKPLDRDTVEMMFLYGLLLFSASTTNTGPVPVLRALDRQSALLLAG
DFLNRCFDVSPPGNTYPKYPTALQLARSDLSTITRDLSIPSLARLAYLLRAQNQQVLIPKWALEQILNFT
LSIHKTHLFSPLSPFARQELYLLAEIIHSMLNHSRERRHIFALLTSLCSPRELYHWTHMLASDAHLYLSD
IYSPCASSGRRDYTLERLAELFPYATLPETRPAALSILSVLRPKRLETFPELSCLPDSEPFAALTLSNVT
YVISSRYILKGTSFPVTNTVVGTSLIITVTPLNSTCVLTRSKHATGSITVLKNITSEDCEFCQSALMEYD
DVDGITNIMYIPDIDDLLFLTDPDNNILVASPRTHYLLLTKNGTVFEVTDVLVDITQTSIILVIIYVLIA
IIALFGLYRLCRLC
>gnl|CDD|165553 PHA03296, PHA03296, envelope glycoprotein H; Provisional
HFLALSAFLAARALAAQQLAPMAHACAAFFAILAILCAAAGDDKAKAKIVFMHATRENLAPKDEFIAAAT
AIDNGDIRLLCHADKNLIFGAPGSAARALAEALDLLGELYVAYAYSRWGAADDAPIAPGKFANDPKLEHR
LLSGPGGNAIKPAEERNFFPLNGSHRGESIIAPIKVIFNDPLQTLFPFVFTRYISIALSGDIDIKINIGK
NVASLCIASPASPPIEMIATPRSAKLKESRFKQWPRMLKAEDQELSVLINVAAGPNYKPNLFNATLAAAK
AFLELANFDEHIAAGHFLTIKKLAIAGCNNEIDEPFFVAAAAHFGAAWFRFAAFAADAYVTDAEILEFIA
ETETWADQVALCFGAAAPQLGAANPASNIAFIQGRGGADEGLINIPSAILKIMHDRPWEEMIKNHNELLT
ILNAILGSADQDGAAAFLASADGVAPHAFAAEIIDNSYHEIIRGKAMDKADRKLLAAATRIFLAAKADSI
PHARNFLRHMTILCSEDQAADPINDIHGQIDAAFGHGEAFCIDDLFSPCAAALRFDIEPQANRPSGIIIS
ASAPFRFFYGKIFLSGEGELETAALLDDSARAIAAAQALGGPKALADAFFPELAKCFDWDLEHHIVFFIA
ISAHASWILTSRPPSGGMRYRLPDTSIAANLFLTFFNASCNKEPFAARTAKIEDGHLNLHGAAIACILCG
HAILQYGLGGFEDAFFIDSADEERELLAGANSSIAFFKAMDPEFFNYALLDPHGSALRILAFDHGIIAFD
KAYIIGIAVGALAGLFALAFAARAIYKFCLGRANQFRLLRLDSD
>gnl|CDD|165554 PHA03297, PHA03297, envelope glycoprotein L; Provisional
MRRFMRCWARLELIYMLAWLVTTKLVKATRLDFTWGPGEPKRILEASCGSGPIMKGQLFTSPNIKNLLNR
TTGIMVKAHCNPPEAILWVDTPPKPVWVNPFAVIQGLAEDVTNGNMPQDFKEKLLFALDDSLSQSQSSPD
EILGPPPLGCFTGPFFLSPPKSKDIAEGLKDSCIPASYYANLQKT
>gnl|CDD|165555 PHA03298, PHA03298, envelope glycoprotein L; Provisional
MGAGAAIAFFAAALIALCSSCAAPGAFKDPSLAAAAACDSIGRLIDGAEQLVSMRCMTSFEHDAAARIFG
PEYLPGGDMFEDLLTIIFKPLCSNPEAIFWYKNGTAAKVNPYLGCRILQDALEANGLAAAKFLARGLIAE
HAGGPLINFRWPETNILHPEKDAAGGP
>gnl|CDD|165556 PHA03299, PHA03299, envelope glycoprotein L; Provisional
VSMSVACVLLVYVLRVFFASAEAVLNWSDRDLTYGFVRVPNVSSIMHLDCIPNSKLSSARYAELSSDDVP
TGIFIKTNCSLPEFILWYERKGVAAWVNPIIGTSLMMEDVLKSGLDDSVKAGLGTFLKRIAELIPTSHLR
NRGAGCINLYAPHDGSCYGSVRLDRFERDAEDDNRGMFCRAKTPRLRNGGRPRET
>gnl|CDD|223037 PHA03301, PHA03301, envelope glycoprotein L; Provisional
MGFLGLVGLAPLGVFPCSTPGGSPPTEYVIRSVAARTVGDILKVPCLRLPADGVTWRYEAPRSIDYARID
GIFLRYHCPGLDTVLWDGHAQRAYWVNPFLFAAGFLEDLSHALFPANALETTTRRALYKEVRLALASRSQ
AASHTPVPPGCVNFEYSRTRRCVGRRTPGPANEPRTRRPLSAPDDEASPQPKSLATPPPVAAPSRRTPRP
RRKPRGNRTRPSRPRN
>gnl|CDD|223038 PHA03302, PHA03302, envelope glycoprotein L; Provisional
MMHLLLFVLLLILIVFSAAASLNNSVAEYREADCIEAVINCTNGETFSRSEDDSPLRPLIQAPHRNGDLS
SLIRYRPPTGELRSPIEVDDEFLDQLALLHNNPDQLRTLLTLLRSDSAPDWMKFLNGYSQCGDSSTIYTC
VDDVCRQYDLERLTYTNDIFVENVLGFELNPPVNMSVLVALRNEATKTTRVVRIPVNSLTLFDALYNLVK
TFLLRHGLDTDLLRRLEKYNARLPAVFRSSPPTRLIRPTLSRY
>gnl|CDD|165560 PHA03303, PHA03303, envelope glycoprotein L; Provisional
MAGHKFLLQIVFFFTITIAHCLHIEDDDPIFFGAKPISDVSLIITEPCISFQEEAWDYAAPPVPNLKEAI
SGFVLKSKCPIPELIIWFKDKHMAYWTNPYVMLHGLANSIGEEEKEDDIRDALLDALSGALQDRGDISTD
IPDIGCVFGADNLFQRLCL
>gnl|CDD|223039 PHA03307, PHA03307, transcriptional regulator ICP4; Provisional
SDNAPDLYDLIEAAAEGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTG
PPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRP
VGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRS
SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSS
RPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRS
PSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAG
AASGAFYARYPLLTPSGEPWPGSPPPPPGRVRYGGLGDSRPGLWDAPEVREAAARYEASPGPVPVYVPEM
GDSAKQYAALVRLLYTPDREAMGWLQNPKLTGPDQALDQFCQKKFQAPRGSGSFITGSVARPVPHIGDAM
AAGNALWALPHAAAAVAMSRRYDRAQKGFLLQSLRRAYAPMAYPENAADTGAGAAAPAPAAPRPDAAAAG
GASARPLRELADACVLACRAVLEALLEGPDGLSAVPGLAFPRPACPPRALEACPARLESWLRELRDLRDA
VYLARLRGDLPVAGGREERVAAVRAVSLVARTVAPLVRYSPRRARARASAWDITDALFSNPSLVPAKLAE
ALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARPPG
AAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPR
VKLGPMPPGGPDPRGGFRRVPPGDLHTPAPSAAALAAYCPPEVVAELVDHPLFPEPWRPALAFDPEALAE
IAARCGGPPPRSGSAFGPLRASGPLRRRAAWMRQIPDPEDVRVVVLYSPLPGEHLFGVPAPDASPGGPAW
SPERGGLSFLLAALGNRLCLPDSHAWAGNWTGAPDVSALNAQGVLLLSTRDLAFAGAVEYLCLRLGSARR
RLIVLDTVDPEDWPADGPAVSQYHVYLRCAVLPRAQCAVRWPAARDLARAVLTSSRVFGPGLFARVEAAF
ARLYPDAPPLRLCRGANVRYTVRTRLGPRTRVPLPPREYRQAVLPALDGCKDMAAQAEGLGLGAPDFLEG
EAHSHRAANRWGLGAPLRPVYLAEGRRAAIAGPDELPAVVRAFCRAALLEPDPEAPPLVLPPSAAAEAAH
ARAPRVTWAKSEAASDDEDGGD
>gnl|CDD|165563 PHA03308, PHA03308, transcriptional regulator ICP4; Provisional
MSSDSSTPSNLAAPIVDESGFSTGPPSDLFTFLRADKSGRYDSLGSPIPNPPNAPTCETTTDSFSYSTPP
LFSSEDELFHSVIAENAAQDAAQDVDGREMSLRDLIAMLNDMDPENINSIEPCPNATSDVVALDINVDTD
QPGVYTVIDSLAHPCETPMEQQHVECPCPLPAVEKTTAVRRQEVVRKSERVARSRSRRPWRDLWSNRRPV
PSPQRTSKDRLPKRGKREFSKKMGPSHLTSSSSSSSSSFSLSGRRGRLARRLESAGSEKSTESPDRDSAQ
LVLPGECPDVALEPLWRVLREWVETDGTDGSVQSVTAPTELPDLGRGITLNVLSRALAVDLHSSEARVFV
PEAIIPSPPSRGQVYHGSGYRQSLVDDPQVREAAAEFHANPKSASVYLEEYGMPVEQLERLVEEFMVHPL
SRVSYGYGGPKLSPRDKRLCELCALRGPGSSEGGLSRSAVPTCLPHVAHAMRDGRVSLALPHLTELVRVC
RRYDHPQKTYLLAALRRAFVPFVFPGAAVDPTAASASGDHPVLVGARRIARATRELEAAAKEPPAATPEK
LSSSALLRHTRTCIVAAADLMAALTAIDCPPVTINPAKRRPDLYQALSRAPKTVFTWERAMPYCAASLWS
RLVIGSLPLPSTDDVTLLVEAMEAAVGVLGCSDEGDVRPSIAYAASGWRMIATMLGDDSAPGSEHVTDDC
PADDDTHHHDRRKRRGGRRTTCRYDLPPGTPDRAAHLLLYGSPGGGDGAEPSAAQESPANPWPRAPPCDE
QEPLSVSPYGPEPDRPPDDDFETRKGLKRKSSEDHADPIPEGNATKKTCGLQGLPDSLPPAVPETDRDNP
LLPPCPITPEGPPCPPREEPQQPQEPQEPQSPSFHISEIGEALFHSTPVSPTILFAPEGFIPNQGDVYRP
HGKNLGVALSAGEPYVPAHRARPALERLANYLRGLSSGPAGSYSATGPADWLPAFARDPVALGEFCKRIS
PVNRGGRCVLEERLSWTLRHPADKIYDLIILVSERAPGEFLERAYAYAALCGRACMPGGACWPESWTRGE
YPYIPPDEKDPGRSVAILCTTDLGYAGAVEWMLERALSTSGRACVVVDARDPGDEDSRSGPRIPTGRRGV
VYARTSPPSHAYLVKLFTGPAAERLERGGLNVGHVVMDRRLTVSWPLSVGKTDNDDEGTGDREKCPPVKH
PFLTHVTLRRLRDVARAMDAGWSHSEIGKASAVLYPYMAQPHVGAGAMPPCPDLSESSSTMHSSSSSSSS
SCSSSSSSSDSSSSEEDGDEKNEKEDRERAGGGKRRGRQRLPIRDRVYRGRDYRVRTPCADIVGGTSASF
RAVAAWGRDTVIPALPLAASWSDPSKIPQEVLRIISDYYPDAPGARARRNPLHVEGLALMRARNPAPLAL
LLGDDYSHYHTPRNRSPMCCCWSAPRGATPESLRCTGHTRTRRPRLSVSSGRGETRTLVPRLD
>gnl|CDD|165564 PHA03309, PHA03309, transcriptional regulator ICP4; Provisional
MFWHQPRQQQLRQLQRAASGAGKHQRRSPPQTLGDDGDAAAQVPPSPTGALLAFLNQHASEEGGAAAASA
DGRVSVSPGFCSSILPEHSQDLFAFSDPTSASPQPVPMDASLSLFTPPVPDCGRDVGEEAEGAVAPSWRA
PLPAPQWRPVHGPSWWLSSSSPSGSSRGSVTSPQYSGEETSDAASGAPTPPPQSSGSSYVYGQALADLMA
MIQEIPAPPRSVPDCRRGEPVSEDGMADRCETDASCYTTDEPMEAEPSEPAGGVSWLGERADRMRADQSP
RGLGAEPHVAEAGRPSSCVGEERADVVAIAAVEERKEAARRSPDAERNDDEEEYESLPCAQEFFTSQELA
EINARAIAESDEAEDEDAGSPAARSQSSPFPSLGPAVFVLAPTSAKSSRGMRKKAIAVSRVVPDNDGEPD
PCADGPGRDHVSSAQSAGANGALETETSVPRSATAPAGAVAACAQNTKRGYWRGAAAGHAEEETDSDDED
VLVVDVSACAEPFESFAQRQQPRQQQHAPRNKPARQRLRAGAIVAAASGNTLTVPSEPPHPSLAPLWKML
NLWLSEEWPAQGGGQDEGEAAVSASLLAPGSLPELPDMCPRVAVGIISHALAVDLSAPGGRITVDEALLP
KPPAADYVYYGKTGYRPSMAAHPDVRRAAEEFSASDAAARVYVEEFGMAVEQHERLVAEFMLQPLSRVSH
SYGGSRLNKTEKNLCKICLPPDGGDDRDGGGKSRGGRGGGSKDASRTAMATGVPHIVHAMRDGRAALALP
HLMDVIRVCRRYDASQKTYLLSCLRLAFAPLVFPGASPPVGADDSPWPTSPIRECAAALREGFRALNDIR
AEQDPPADERSRELALPLDRAITAARRVAATAAGLLNAVGASVVHDGRVGLPAFFLRGVTERREDLFSAA
RRCPRALYSWERSMRATTAALWGHLASRGPIAAPVADLEELSQALSAVLSVTSVPDGGDVRYAFAEADEG
WRALAVMLGGGAVRTSSGESGDAETDAAYALLAPGKQSSAGVNHPRGRPGRATASSPRTPASRPPHGSAA
APPSGRDSPPGALNVPEAAEEELRLAAARDTTGDLLSDEAGTDDDGDAPVVISYVGPSSPPGVEDPSPDG
LAALRPLPEGYVPRPGDVLRGDPGADENDDDARAPCRVGDASPPRQLPSSSSFASSSLASAVPGDPYLPR
SVAEPTLCRLAEHLQSDDGWTRAFANDPVGLAEFARRSTPGRRLGGQRRLDQLLSWTRRHSPRRRYSLIV
LVSEKRPGDFRERAYAAAALAGRACVPGSACDPETWRDAEDHPSPSADAQSPLRSRPSRDCFPPRIAQPE
ASDDDDVGEGGTALLSAGDIGFAGAVESMLRRALSRQGQACAVVDARDDKDVLSAAAPRFPRGKPGLIYL
RVAPPSEACVANLPSLGPSASPHRGVGGKHRDKRPCLAEGTPSAPSCRDAARATAPLSGDPVAHRLLMHR
PAKPLVGEEACAALLGGKAGRRGQDVPLPFLTAATLRKVARVARELDPGWGHGDLGCESAVVFPPAAPPG
PELADRHADRRRSTKGPQRPGGKRPRSSSSSSSASHDRSPSSSSRRRDGRPSSRRRPSRRMSARPPSRPP
AAVILRASWRYAEEVAREMLDAAASRFDEADGEDPLPPAACGGKPIAPETLVALCEQRGRGPTSLPRAPT
PRSGEALAAPRRSGAKDPRQGQYCPSARRSEAPHSPSPRDVALRLLERQQELNRQLLLELRRGSCEISPS
PRRRDAEGRRFGCRQDDDDGYDYEGGRESPERVLGRRQSRRDSVPVRRRSGAANCGGRWMISAGRSSSSS
SSSSSSSSSSPSSRPSRSATPSLSPSPSPPRRAPVDRSRSGRRRERDRPSANPFRWAPRQRSRADHSPDG
TAPGDAPLNLEDGPGRGRPIWTPSSATTLPSRSGPEDSVDETETEDSAPPARLAPSPLETSRAEDSEDSE
YPEYSNPRLGKSPPALKSREARRPSSKQPRRPSSGKNGHTDVSAASAFFLGRPAPGSCGRRPLGARVRGG
TER
>gnl|CDD|223040 PHA03311, PHA03311, helicase-primase subunit BBLF4; Provisional
PSSEGSRRMERFSDEFILNMTSMAKIRPIVDRIRSLSERRVSPADVPPLSWFRSEFDPETPLDLPPPFLP
FSVYLITGTAGAGKSTSIQTLNENLDCVITGATRVAAQNLSAKLSRATSAYINTIFQEFGFKSNHVQAQL
RKYQYVCASTPPSIEELQKRDLSYYWPVLSDITRRFLKAKKRGQYGSLSRLAFEVLGSLPALWRSNIIVI
DEAGLLGRHILTAVVFCYWFYNALYDTPLYRQGAVPCIVCVGSPTQTDALESTFEHSTQRCSVRESENVL
TALICNPTLREYVDLSNNWAIFINNKRCTDPEFGHLLKTLEYGLPLTEEHMEYVDRFVVPESYIRNPANL
PGWTRLFLSHAEVKAYMSRLHAHLKVSGENRFVLFTLPVYCEVFNEAFEEYKELTGQPSLTPEKWLRANL
GRLSNYSQFRDQDMSAVRTEEHSAQGLTLVTYDITYVLNSQVSVTTKTKKCVFGFSGTFESFKEVLQDDS
FIETHGEEQPEYAYSFLSGLLFSGMYNFYNFLSPFKVEEALRRLAALTLPLLPADLFYCNYEFPPPASSA
SFEEIVAQYTMLKDIFLGRYAILQELFGGEFGKSPFSTYVDNVSFRGCEEFTSSERGFHGLLSYASQTDS
YTLEGYTFAPVFFFAEELQRIAELLLERGLPRLVVRDQHGFISVLNNNVSKFVESVEGKELHMCTTVDYG
ISSKLAMTIAKSQGLSLDKVAICFGNHKNLKLSHVYVAMSRVTSSNFLVMNLNPLREPYERDTVISEHIL
AALRNPNTLLVY
>gnl|CDD|177582 PHA03312, PHA03312, helicase-primase subunit BBLF2/3; Provisional
MMETPAESVRARVSSVTFYNVTQTAGRWWAIWVVGIVPIKREDVETLIVVQACQPPLGGSLEPPVVNAPS
TTELNFLRWERELRRSGGLIAMLADAAEKDLFDLSFRTRDRRLLSAARVEDEQGLIFQPLFPAQVVCQSC
SGDDGRDQQPPPVDGFGSEMEGEQTCPHAQRHSESPGQLDVYIRTPRGDVFTYSTETPDDPSPVPFRDIL
RPVTYEVDLVSSDGATGRGGDARRHRVSLKILEPAGGFESWLVNSWSMAGGGLYAFLRSIYASCYANHRG
TKPIFYLLDPELCPGGSDFQPYVPGFPFLPIHYVGRARPAFWHRAPHSEGLLLLDLNLGVSGTPLADALL
GLDARSGQRRGSLLLQQIWPPTRKEINPRHVCTREGGEGGGEDETTVVGRAEATAILEADATWWLYELAR
CHLSARGAPVGTPDGGGQARDAQTWLRALHRYGTSDTRRALGGLYTAVTRVLLHAAADLGLTWAYADEFI
LGFVAPTSAHPSEEPLAQAFLQGVKDSEDASRLDRDVMGGEATVARRHIRVKARRGPGCLLMAIFQGDLY
VGGCREHSGPFLVWHEAFSWTLDQLAARPEADKAPPSHDHLLTLVRDLTRRLAPGRRRNRFWALPRAWLQ
RLRRAGLRLSGSHVCLLDKDGARPAPCQTATEHGLSPTAYFREIMAFLLDVISALHPGYTIPMEITRETD
LLMTVLSLF
>gnl|CDD|223041 PHA03321, PHA03321, tegument protein VP11/12; Provisional
MQRRARGTSSLRLASCLAPAGLAHRADAGVAETRIFGGCLLPTPEGLLGAAVGALRQRSDDLQPAFLTGA
DRAAQLAARRHNSVPESLVVDGITGDPHCEYIKHYAAAALESLAEAGASSGQLSRAILAQYWKYLQAVVS
SGLRIPEDPPGDCDPSLQVLLRPALVPKLLARTPFKSGAQSARYAAAVAGLRDATHRLQQYMFFMRPDDP
SRPSADTALRLGEILAYSSALYRWASWMVQTADAQVCRRLGPTGRRCRAPARSAEAPADAFARHLDRGPG
GTTGSMQCMALRAAVSDVFGHLRRLAHLWERGKRSSGTYGTVDTIVSTVEVVSIVHHHAQYLINATLAGY
VVWASDSLNNEYLRAAVERQERFCRTTAPLFPTMTASSWARMERSIKAWFEAALATELFRTGVPSEHYEA
SLRLLSSRQPPGAPAPRRDNDPPPPPRARPGSTPACARRARAQRARDAGPEYVDPLGALRRLPAGAAPPP
EPAAAPSPATYYTRMGGGPPRLPPRNRATETLRPDWGPPAAAPPEQMEDPYLEPDDDRFDRRDGAAAAAT
SHPREAPAPDDDPIYEGVSDSEEPVYEEIPTPRVYQNPLPRPMEGAGEPPDLDAPTSPWVEEENPIYGWG
DSPLFSPPPAARFPPPDPALSPEPPALPAHRPRPGALAPDGPANLAALSAMLTKLRHDRRHSWR
>gnl|CDD|223042 PHA03322, PHA03322, tegument protein VP11/12; Provisional
MSSSAQSYSLRIPELRSSRCGWSTLSQRIIAERLRDGCLIPTPQDALESAVKALEEKTEKITPFQLFSTE
RTEVLLGTHHNNVPESLIVSCMSSDTNGAYISNYASEIQACLDDTKLSKGASWSVYENTYWKYLRHTTGA
DIPVNSETSNKKAKSTVLLFRSTFEPKPISKRPFKGKKVNSSYREQLQELKENFGAVQKYMYFMRPDDPM
QASIDTRIRLQEIAAYNSTGYGWMLWFLDLFDSRVLRAMKLVFTGTNGPRESVQPEDLFGRHLKSGPAVT
DGTGNAVILAATTASVLTSLLKISVLWSSSEWRSGLNGTASAIVAAVELITMLHHHFQYLVNMMLAGYAC
WGDGGAKDTYILSALRSQGRFLYFAGRLVPTMSVHSWVELEKSTHAWFKMAVARSILTHGGPPTHYYTTV
GSVDDPFADTVLNRDDDDTETLNDPYITRYRSNILRSSRASGPGGLECVCLVGNSKSDSEEDLSHVIHMD
SPKSPLSISSFKSRARRVLVRPSTSTDTTRNDPSYWFADGDDGRIRDKTYPLNYTLNKATYEGPVSGPGT
SEDGEYVDETNNDTATGPKCESPDHVYENIEPAESNYSYENDTDFDSVASDLGRNHRSTDGGSPVQFPDD
EPVQCQVTETFAAFTPRAHCLGKRDRERELAAVQRVMNRLSFGK
>gnl|CDD|223043 PHA03323, PHA03323, nuclear egress membrane protein UL34; Provisional
KDYPGRRGDSGGGLIQRIRLVVPGNLRCGEGDAGLYEPKRPPARCVFQFSGQDGSDETFPVEYVLRLMAD
WADVPCDPYIRIQNTGVSVLFQGFFFRPPNAPGAAITAEQNNVILKSTESTGLSLSDLERIKRRGGLDPR
PLQAMMWISCFVRMPRVQLSFRFMGPEDPSRTQRLLDRATEFALAKRRRRRRDGSIAGDRKNGDAASPGC
PPIPPRAASPPLPAAGAARGWASLASPLRAPRSVPTVRISAAPIILVILGVLLGARLWWAYG
>gnl|CDD|165570 PHA03324, PHA03324, nuclear egress membrane protein UL34; Provisional
MQGDKYCQLVRFVNAGLGAAGTSASLVYIRDNARLAPTGDIFTLLAKLDGPPIPAEYILEAMNSFLNIGE
AWLRIQNTGQAVIVAGCFTKNAHCGDQIWEAPAPTISLAAAKSLWVSASAVKEMKRIQKIKNAPLAAMMF
ICFYRGGKNDITIRFAFYKSDSEPNLIKISKCVQEAIDAAAQENLPKPRGFDSPKCAALAKKMLMEGAAE
GGDRESSAESHPPAAIAEHVMQHARAHKKWGALGPRLFHKKNLGWILFGCALPAAAAFLIAYII
>gnl|CDD|223044 PHA03325, PHA03325, nuclear-egress-membrane-like protein; Provisional
MNFIITTRDFSNDSSVTRTKAERAEMADNFARSISKAYKGTNRAEGKKRLLSNHLPDCICSKRNTNSFIF
CTSRDYRKFEQGIAQLKRQPDIVDPSRIDQVTQSIRCRLRKHPRSPPLPADQRLIRAVRRVCVLFNRLTF
TARLRHYCDHDSRLVAYLRDELTKRCGEGSRLGEHIRQLISLVDHERHRDLCHVLVGMLHQTPHMWARSI
RLLGRLKIFYQNSFLKLLADSGLDIPDVFEPCYHSEAYRLLFQIGQLTSSAFMLNSSLPTSAPKRRSRRA
GAMRAAAGETADLADDDGSEHSDPEPLPASLPPPPVRRPRVKHPEAGKEEPDGARNAEAKEPAQPATSTS
SKGSSSAQNKDSGSTGPGSSLAAASSFLEDDDFGSPPLDLTTSLRHMPSPSVTSAPEPPSIPLTYLSD
>gnl|CDD|223045 PHA03326, PHA03326, nuclear egress membrane protein; Provisional
MELKKKVYADLVSATRRILKLGPHELRVTDYALICKNPNYSLCDAMLKTDTVYSLEYLLSYWESRTKQEP
CFVFKNTGCAVSLSCYVHAPVKLESLRRVREFNVLRVNESLIVTLKDIEAIKPSAYGVLTKCVVRRSNSG
SAYNIELVAFGPENESEYIALLREIYAKKARSGPQHLRSHRSCGSLRDRSSHALAAAPFGSATRTGAKAS
APPTSDASINQRRRRAGSARFPVAFWVLSRRAIRVALVGAVVLALLLVCYVLWKAAPRAASGPRV
>gnl|CDD|223046 PHA03328, PHA03328, nuclear egress lamina protein UL31; Provisional
MDDLALRRSSSSLRRSRRAARRSRRDGRVGSRGRSRYRSRRRSSRRSSTRRAELADTERDRYRAYFAYLA
SSPSDELALVRSLSVPLIKTTPVSLPFDLNQTVADNCLSLSGMGYYLGIGGCCPTCSVSGEPRLGRTDRA
ALILAYVQQLNNIYEYRVFLASLRVLAGRSGVGSYENEPLERLLANVLAQPELFFAYYVLRDGGSRDVRV
LFYRDPDGSGYMMYVVFPGKSLHLHYRLIDRLLTACPGYRIIAHVWQTTFVLVVRRDAERQTTDADVPAV
SAEDIYCKMCDLNFDGELLLEYKRLYATFDDFPPPR
>gnl|CDD|165574 PHA03330, PHA03330, putative primase; Provisional
MESAASHDACHTVAPAAFPCGADMRLVYLGRILIPNAGEDVYGLLEAHPKIKKIGFAIWLKAAKKAKEGE
KIIPKNHFTWWPEEFHDPAALEAAGALQDFALQLGKSQASLEDFVSELFVEHVKTLALSLERTKEKANAI
IGKACADAIDPAFHSSMVREHLGGAHYEDAVEAERAFAGPKCQILRNVQKQKLAGFDSRLIPELFHDLLL
SIHEEMAAAAAKEMDDELPPCADEIGAMADAALIHFREIQDMIAARLQFPNLARPGNCAAAGFYHIPMVL
FKAFDKEVKHKFGKSCFDALVDYCGGEGLQEDERQFLKLPAPEEWGDSAPALLSCDAEPRQYIICDPDHL
DEEWEAETAEGAQCCWHEVCLPGRSITNILLDIDIRAAGAEPHPEDDADIGASLAQLLACIVKMLELNFE
GKPDEGEAGAFVFFHRPCAPEEGKLSFRILWKLPLQLCAMDIGGRLVEEARRLSLAQRLPHLMAEAALHA
ADHGMEGLSQYCLLDHKGRRTFGDDLEDECCWHCVRGDINLEDCPFELQGINGADKLKADAGAHLHLNLK
RAAHRADEMAVHCALDVGPYGARKSLRLPLCDKPHEGGRFALHRTRNACFPDELEFFSNPGQSPSACLAA
VPADDLRIFLPRLSSGMLEQLEKEEEGAQEDAAHQMPALDEANAEIAIDRLAAFAGCNAVYFSARGEGII
YPPQADYVICGLHGREHKDKAKHYFAAKNPDTLFLLCFKPAAQGEAKFLKLRWDDHFGAYFPRDWPSNIS
A
>gnl|CDD|223047 PHA03332, PHA03332, membrane glycoprotein; Provisional
KKTLLALILVPALYAVLGETVADDEAFFLSCPVLDGTLIDPDGTDAVITGSTLMNTLYKIPTVSATHTLR
EVGRVAKSVNSTAATLCTHLCVDGTVLKLSVQATRSFLYNGASLVCALPVITNMHELNETCASCSYYCEE
VISHRTSDNMLSSTDACYSSNDLKKALTELSTFWKTWTQGCLIARALTLLMESASMDPRVLSILRGTSYT
CLLSYVGISEPEPNSPCVTTLGPMCYGPLCISAGANPRGFTDRPVSTGVDCTVGSVADLQQCRLTKGLFA
ELGCDLVFSLCDLCVYEPLATAAEFELHVECLSSYRVSGFPGECPDVGLELAFNNFGLENLIRTTADRLT
ILTRGILDIRNNKLNGLVFPWIPTPELLDTFQCPGFDGYRHLSYAVRYLLGHMSLEKLTLGVVVSCQLWG
RRVRQYDTNWYFQDNLVTELTTGTDVIYNNMTYVTQLNGCHGVFGPELDILLPSPDAAPVAVLLYRQPLD
LEDAVPFSMALGITRFSIEGALGDVYMDSSENLKTVRTVHEGFTVRMGAHAMMEEMLGEGGLAAFDESMI
WANVTRSTGTATTSVSKRGALDTQGPDGVNYTIPFSASVQSGTSYYYVGTGPKIVCPGIIAYVGDLLFTR
TPYQNTYRVPFFQNYYVLQNFTCATGSKPEPLPVITQATKVPPVFAIDINTLQTVNSSEYYVVLYDGTNL
CQYSPTVKQSCTFINTNRTFNQTLYLINGRFTGFVIDAGTYFLGVSAYIKIISDNTDVVEYIPVDQTCMN
YSNSSIPSCLATVCAGNVTECTPRATLVCSMDVSVRVSIAGLLLEFEYSNERYKNTLSVLDLWHETVKMF
APRRFGGSVMAGDAIGLSAAAFTMASAALNAATQALAVATLYVNQLLQATAATAEMASKIGGLNARVDKT
SDVITKLGDTIAKISATLDNNIRAVNGRVSDLEDQVNLRFLAVATNFNTLATQLKELGTTTNERIEEVMA
AALYYQQLNSLTNQVTQSASKLGYQVGMYRTCLKSLLAGTLAGCPTDAPFLRDNPDYTMVKSVYGALYRG
QKLFIVYKVPDSLEARALYVILVKPTIVNGKVCVPDSKNVVMGPDGKFYAKPECEGRYCSPPILHTDFQE
CLSAIQSSDCAQVAGFCYLLPCYNRDCEDRSIIFETVTGALSVPDLPSGLFNFISQIVSMEGEIQDLKLP
LLTLVKINTSAHMENITGDLDAMKKTIEDYRAEMTQFSAQVMAKLRRTGFGEWIKYFTGPAIGIYAILGV
ISIGGLIAIIFMAVKLLCSACGGCYQKRALLSLTGGGPCVATAPAPCIACCALQCYQPLPTREMGMMY
>gnl|CDD|223048 PHA03333, PHA03333, putative ATPase subunit of terminase; Provisional
MEYPTEFDTGHKSTDKLGNMCLQEQLVDGFFRHVALLVASQAIEKDRVAAARKLTDELRAPLLRAMLIWG
IGSDAISLMETELEREAATQRDPGKRKFRRLCLMIDCIFHLLRDHGGFRLEPFQLELLRGFVLGVAERQL
GDDLFKYKHKLLDLLGLASPDVVAFNPEAPSPRTLREIDRIFDEYGKCYTAATVPRRCGKTTIMAIILAA
MISFLEIDIVVQAQRKTMCLTLYNRVETVVHAYQHKPWFPEEFKIVTLKGTDENLEYISDPAAKEGKTTA
HFLASSPNAARGQNPDLVIVDEAAFVNPGALLSVLPLMAVKGTKQIHISSPVDADSWISRVGEVKDETGK
TLVHVIDQQFKCDAHAQDPGITCPCNDVFCPDHITVDEGLKELLNLVSPGAFETELTGGHVAGVRGRDVA
SPPFETLVTNFMTNAVPVVDQSGISRVYISVDPTYSNGTMSSIGVCTFVRLNTTSGPKMLVVGLDEVAIG
EMRSISMKAHELVLMAHVMYSRGLFPRKDLPIIFLPEQNTFAFDNSNLWSTLAGWAERSFGIKVLIYRDF
NKSGTSQPGKTVSRNKLSQVIKFANAMEQDKIGHVDVVFSVGDMVLKAFKRRDKVLESYLRADTVTTATG
GETATLDPRDALANPETASDFKLPPADSREYIFRYLGGLDVALMPAKDDLFKAGTENLTKLCAQLMNVKI
DESTGKQPKVITGGKKKSAGSYSRDDLLSAFFLGTLVADRPDNPTNRLFIVR
>gnl|CDD|223049 PHA03334, PHA03334, putative DNA polymerase catalytic subunit; Provisional
RNFKLYGLFSDRLPKFFFSQVFYITAGDEDLIYIASLRLIEDSFRVFACEPDDGREKCIWIKPREWNCLV
TDLNFMLYLPSVPIENPGIRQLASTLPLPERGPITVFNGDTKEDVDCRLFLFGTKAERKAFIKALRKVLP
SLGADVLTFGRHVSNMDGNAPAILNRLMCCCYYRTKYKVASRPDVIALTELYYDDKLDQGLLNSLHPHVY
ETPYREAAFDIETIVDENALDPNLNVQPDLYFANAFAIMDRNKRCAGVGGLLPPPFVSILRDYGEITSIS
LVYCTTKPKGPKKKKRYVFYNAALVEGPEPLHLDSSYDVVTRIEFVACADELEMLLAFLNRLRKSVNVLY
VYNAEFDVQVIQSRLNYYAFKQRPHPLTKALMEAWEAFLSKDPQLVPAQLLFGSDILNSNYLELLDVIES
HKAQFKATCRKAAARKEEIGSYMKTRDTVQDFNDNDKKYLNSTSHGFGAHIIDLMRVCNTKSIKAKCSSR
KLDTVARLIISKSKPHKNPPKIGKMDDVKYTEMDGMFTAGGAALARYLIYNLVDSELLIRIAKNLDPVIE
FLNRLRATYNIDYVAHGRGVMNFCGFVQSTKSVEVPLLKARLRIGIFVATGRIAESLCMPEKYARDCRQK
IKLKGGYVFAPLTGLTFAGPYQGTELTLDFASLYPSNMCDANISPEAIVDPDCTARVRGWVVFDWKKIDR
GFGKATLMYTILRTKPEEPSWRRFTTYTTSSLNHYLSMRTEYKGAMKQAKDPKLKSYHNQLQNEMKICAN
SHYGVAPHACQHLITTLGRHKIKLVEEFIKKEPGMTVNYGDTDSVMFQLPPDDAETYLEDTVTLEDEERA
PLEYTLEEWSAEAVNHVTKAKTKREGETVQSILSDLNTVLYDDMIERLRYVDEGGSVEPFKDGEDWWVVD
PLDGIWTYVRDPFSSELITKLCYENTSTVTCRLAKKMYIYTNHELNNGPLGNTKIKMRGMQANKSSAAGA
TRRITNDFVNLIFKGGALRVTKHFEALQAVTWAKVSAGDDVKLHFSEPPVDENGVCTNYNSITLEWCRVT
AVTRLPCPDIKGYELVYVDLRESTSGKFSYLCATDANGINLTHTFSLAEQRRRCLSFETIAKYRAFAVSA
GFTDWRNLVQYSGLIPRKKAELKSKRTNYGLFNGKNNKIPYVTLHKLKNGVYNIVKEDYPKEWIKQDPAA
AFLRRYPFDVKLEVMDRDMFGASLKCTLATFTPPKNRVSRDRSRGRAHPTVLKHAVSLHYLTEDTNFLAH
VLLDRACPTSCYIPDGWPLKAMLQSGLAMIRDTQDRMQLLAAKGQKLFSMFFNTPPPDMNNLDISIDRND
FTDTFTRPQNDSGGVPGLIYGRPEDIYTRMITLMEALLPAIGELVEFKLVEEVSSSKGPCLSLPAILRDL
LPVPPRLVPLTDDTGHPDLIALARKIYLYTILLGGAKAYNENEVDRHILRGENLETQTGTEVLGEPPKHA
TKAELKEFFRRLQKALVALEEASDAPSTHCAGCRDYWETHGDIPKFVEDMYRVVNGGLYVRKRKKICLGE
SLDVA
>gnl|CDD|223050 PHA03335, PHA03335, hypothetical protein; Provisional
MAPRMGTADLIHPDCLDSTLNSEFLLYAHKKINPHITQNEKKRAIFQSLTMDRALKSGFSETDLSIELPL
YVSSVSFRKGYGLDLDAPIVFRLVILLQFYRFLARYGLASQCITQRASTAVDCSGFLRTAETGATPRTIK
LYLPRVYKISRQGRLHRQLFQICKQYTPSLTPEYNLELQVVVDIMRRRTVEDPLDLIPTIYPWTLPILRG
IMSQLQRNIWAGGQNRKEKITELVEELAKVKRGAANLEHTMCLIYHVLNAYINWFAFNRQQFVNPGITLP
SSELSQEALDLRCSGCWRLLSIRSLRKTGKPKNMEILYCTDDHGLISSCCKASVLKAPLSIGKVALVINT
PFKQRYGICACGTMCVEDPIKNTELKCEACVYNDL
>gnl|CDD|223051 PHA03336, PHA03336, uncharacterized protein; Provisional
MERVLRQLSTGSYGGRRCGGIEERIERWSRTTNSGTNTAGGWIDPPPASFLIGNTVLRLHGSPGFFIHVK
HVNTVYNRQQRVRTVRKGVMPHKTIQNSTVRRATNKFVTDKKKIFTVDGVKSTRIEFTTAEHRSSNYTAN
APPLHHPTYHSFFDLLCQSHGECVIHTHPDVINNLNYTSYLYGVTNPMSTMVDLSMKQKNFLRPFFFPSI
INAGPAETRHQLFISMYINSQKLTPETIYRLGKTLYPIYSLVEVDTKLNWFCNMIFLFLRCFLNTPNKIG
ILWMNERYHLENPTENPTASTENEYRKFMLEKYAPLLNGFSGAFAQRTNQYVYKNCTFVHIAPFFLAAAL
EEGIDKVWPVVLSYGERLLNAGKIKTLKELVLMLSVCPAAPRLTVTQTDGRTDVYRTGELVLTDVKVRAS
DRLVLGKKINQYLKCKIGDHCDQVYYTVLSSDEKEAASHAGN
>gnl|CDD|165582 PHA03338, PHA03338, US22 family homolog; Provisional
MDDPGKACPAFDAACEPLGDDAEADDTAVRSVSPSAALLCDFADAAARGSDALRAKIALFAGGLLPLAWP
AGAGILFDPDIAGWEPQPGRRNRLLQHCCCDVFVYPIGRAAGLKAADDLDVLMDVFGRFYAYRGGADDAI
YLLAASAEDFAAIGFRFFYPIHCRAGLGEIGILLGRLWLLIRQGADADAVARFVVRAHGESVGVARRLPG
RREVLRLCSLGCLRWRAKRDAHARGGGGLAPAPPPDGDDATVPLGRVKKGCPPAFGIAVFVGLPSGRVFA
GDACDGSYVLIADSIPGFSGIGASRFFENRRFALIDLGAPPEDEEEERDSGRNCERPPPCLADF
>gnl|CDD|165586 PHA03342, PHA03342, US22 family homolog; Provisional
MERPVSANAAAAYKRVIDAFSRLLADGEDADARAEAAEEFDGKMIPLGFPDDWFLACGAGKSCWEALTDR
ANALLCCEEALIPLGLCGRTNDPEDPLGLRDYGTRLMLAGEQGRIYVYCARDDTLHLVARDIEEFARFGI
SRRAFAYIEDMDAILPPADLECLNWIASCDVHDGAPGMELLVVFADPEADAATHVGYTRALDGGFVELTT
PGYGPSALFLAKDPGELRGIWPFRGLCDNEFKRCWKAVSDALHCAWCLIGVLGYRAGGAPDAEFRADHVI
IADKFGAVYSLLLYSGAGLTRRVADNVAEFFQIGMLKRLFSSGFEFHAKERRKEKLEGAPRCPHRIADKF
ELAEEHCKDFFCEPTDDEDYVPADCMAEHCAWLAQATDKTHSCRPWDLDDPNVAARALKTEADNGDPMKE
YEDNLELAIAHVKLAAAATAADRERGGGRAGEGLARVPCVYKLSFVPAHYFAKACHETEDMEIEEVNACR
QRQFFCDLIVPAHGARPGPGE
>gnl|CDD|165587 PHA03343, PHA03343, US22 family homolog; Provisional
CASCRQLAMAREIGYTLAVTARWRRNGPGLPAAFGMRGECLADACFRPGPRIIGTLDTRGEAHAIAAVGF
SAPRGHDWSPSDDLTALIDKLTPRERPFRKKGPGGETAAAAAAAAAAEKGEEEEEAGDKIEPPAVRGSVS
PIRGHETVEGAAAAATAATSAAACDGDDGGGEDGGEDGGKGIGGACAPPTFPDLFELRDDFVEKLAAKLA
AVDADMILCSDETLFIHELAAAGDIARLNCLIRRFHGHCVLLAWPPGWVFTVIDAIRSPRLQKAGAAVVR
DGHVCCDQNIIAIGVVHDLGREHSEAEFPVILLGDDGFVYLYDDGGVGPVLHLLTKCGFADFCRRGLRER
AGIDLDAGSTPIDYGEDPFKSILECRHSIDDLVGARDRLLGAEAAIFHSDNMWTFLRISNLCDLGYDQED
FECWKHESGHCRLEPMFMVKACVDGVWVDAPILISDAGTLFYVDPGHGNIKFLAADLFTFLVLGLMRFRN
NNCFLPGAFPARRGEANRPGQDITRQRNQTRAHAGARRGGPSGAVAEKPAFCPLGPRCLRGGARRSIIGR
AWHWLCGKWGWMTGCCRG
>gnl|CDD|165588 PHA03344, PHA03344, US22 family homolog; Provisional
MWSLRGALRRDLRFDGQDHHEMPTEVWDDPCAAEEDCFDEDFGCVDDDLDEKHIPLIRSPVYPPDDFIID
GFSFGLPLDEEDREAGTRSGPLTGHDNCAALAEPDDEIAQAALDGEGREAAGHRDHESDSDFDLESDSDL
SDDEDAAGAYVQGHPWKSSALTVSKEAVEEHEKKKLAQRFFALTLRDFKSFHLALSFNPGEIAAAIRHLL
GKALTLRFPEHWYLIPQPMNEIRVLFGVDLRAYICCDDAAARDVELIPLGACAARSPDLHFRETPCAILM
DEEGRFFLYDAESDGLFLAAENIDELAHKGLSACEPAYRDGGATISLPKPKTAVKKILSAAVIGLENVAA
AATAFRGSAIALCDPASGREEIFQIFDASDLKRKPPFSELDDESCGAMMDYIEFRLAEAWTVIGAIGEYD
DSDGFVFEVDIVVLLGARGAVYGFCLEENDVFRIADDISTFFKRGGVSGGAAEPNRFDRDALGELRLERP
ALCPHEDEGTRGDREPIATSLASQEIARRDLEDWLRWQLGAGPDLDDCVAFAHLEEAKRQFRHPAKGIPV
CIVTAESYHPKGDPEEAFESLAEGRRNFRCPRTCDAPLDEERCRDRDFYQRMMCAMDMFDGGKEESEREI
IAERAARLAALQKSGTPLKLPAISRATQAGRTSNNGEPGSDR
>gnl|CDD|223052 PHA03346, PHA03346, US22 family homolog; Provisional
MWRTRWESGPPTFTRPDPFPYCHTRRSTFLRVMADFRDLFRRQDNPEVLADWVRRRAGERLSLGIPHNWF
LELRPASQMPELRDQLLDDLLCCDERLIVLGKCVVRVTDRYEETELVLCMGAETRLYIYEPSQDILILVA
PHLDELARYGLLHSECVYRQPQTPYATRVPHDVVSGLLERCDDLDELAACVGEYHGRDVNLHTPGRHAQP
LKLLSNFGCLRRCWPFEAMDPDDLAECRMYITLRLRCRWFALGAVGAYRAGGFFHVSHLLVVDRFGAVYT
VIVRRGEFYRVADDLWELFRAGLMKVYVRRRFDHGLRRIARLERRVICRHLGETYRLHFTMFDSGVERDY
ERQHRWLCRDDRFRADMLRTWDDWDAFALWHARVLRGEFAERRRPRGPPENEDEADGGGGLAPPPEPPRP
PPPPFPDDDDEGDDEDDDDWEDLGFDLDEDDVYDLKDVDEWRLERRIATAERWELGQRLLDAYMTEAEVT
EAEVEARRVRLNEDLSPSWVKSFDFRSHFP
>gnl|CDD|177588 PHA03347, PHA03347, uracil DNA glycosylase; Provisional
MDAWLKTHVWSKLQRQQEVGDEDLLLSDPWLDFLQLSPFLKQKLLALLNCVRELRKQTVIYPPEDRIMAW
SYLCDPEDIKVVILGQDPYHGGQANGLAFSVAYGFPVPPSLRNIFAELHRSVPDFSPPDHGCLDAWARQG
VLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKASLINSQKHLVLKAQHP
SPLAANSTRSSTWPKFLGCNHFVLANKYLTQHGKGPIDWNLE
>gnl|CDD|177589 PHA03348, PHA03348, tegument protein UL21; Provisional
MEFKYASTIHHNGVVFYVTDDGNRAYFVCGGCLISVPRPRADEPGEIAKFGLVLRGTGPGDRVVANYVRS
ELNRRGLKWAAPSGEDEVFVDSLALLSPGGVSSERDLCGAFDLEVYDPYLAEYMVSLRVSSGLVLTTGRD
RPQDRVLHLFEVPTITNASSGFVYTPNRAAFALVQARLTELPSSLEDLVEGLFDGIPVPRPPLSGDERPR
RTDVIITGKRAARTMAVKAGRRAGRRGAKRTTVSNFVQVRYIPRVCNIWAPRSPPSSPASLQELWELFCG
ADEVLLKADAWAGLDEELNEARSTIVEAVWALFGREGARPFFGAGSAAKGLSPLQKFALCQYILSRWGLP
NCYAALEELCRSYIAAVPEAVPPPDDDHTLADAVNELFREALFLGALAEILLRFDLPPPPVYKSVSSDAR
ADATTLLRLAANQTGLETGPVPADESERHEAKLAAILDGLYAGRGILAAALRACRLLGTASPVAAVIDVS
RLTAFDRAPAARRGAAYLYALLDARLKRAGCGQIVN
>gnl|CDD|177590 PHA03349, PHA03349, tegument protein UL16; Provisional
ARRLTPDAAADLVEALTEDVCVWRLVRSDSRLKIFRAVTALTPRLARFAPPPPDPTRAKFVEIFLYLTRP
KALRLPPKTFHVLFLFNGERAYCLTARVRIVPLPLGGTLFDATFSDVSAAPLPEDLPDPAAEPLPTAPAA
HLDLSAFLVPAQPPKDPYACCVLSPGAWWSYPKRRIYYLAMDEALLALCPAGWRARSLGAVLARLLNHPG
GCATCRFREHVDALNATWEPGAVAEACPCWAPCMWRKARQRDLPVEGDSSLFRVLFMDAVDRVRLLGSRR
NPRITANLSEVIVGIGAAGRQIPVNSAGWRLVALDEDASRLLICGCPALRRLCADAASSDWLS
>gnl|CDD|177591 PHA03351, PHA03351, tegument protein UL16; Provisional
MAKDRGSVPMMGIAWIFFVLCLSASSGCAFDLGDKEKNSNCRLNATELAEIHPGETWTLHGICISICYYE
NVSDDEIIGVAFTSQHNESVTDAWLYKNDTEIRNFSDIQTNILQDGLKMRHVPVTKLYTHRIINNHTAGR
YDCFRCENGTLEIIERLYVKLGSLYKRLEESGLAKHPSMSADEDSELPANLARDIMIVSAITLFFFLLAL
RIPQRLCQRLKIRFMFQRQRLRDED
>gnl|CDD|223053 PHA03352, PHA03352, tegument protein UL16; Provisional
MATSRLSIGDLRSLRAFLQNECNWFLVCKKARHREYRAVATSSPIFSLVNTDDGRCLHCQLILLKRDGEF
VLCLAVNGIHAGQFGCGGVKRRRRVIDGLLPVYYLLELGPLTPADLGFIPYYNSVKSVMSSRGITPDVIY
ENCSLVGPEEAKRVTVKGPGAVKLVPLGGVGAWCLKRGGGLYLYTFVLCYDLYTACCDRSTFPSLAKIYA
AMVACGQDGCVFCRDHGRHVDPTGCFVGCVPDQGTCFCYTPCRKTMAPISNPELLPFLCDQEDAKIDLLY
GRKTDGQKSLSLDISEYVGVRDSEGDPVPLKTDVWQLVKVDPALSRLIVLSCPVLKRLVM
>gnl|CDD|177593 PHA03354, PHA03354, Alkaline exonuclease; Provisional
MGQATSYLTDTFRRCCKRNTLLTKSGQVIELDDENYDTVDLDELRYSDPLEEAKIVLLDRPIGRGKRINK
NERDYENHPIL
>gnl|CDD|177594 PHA03356, PHA03356, tegument protein UL11; Provisional
MGLAGSRARPCCCRRNVLVTDRGETVSLTAHEFDAVDLESDAGGNFYISPELRVVTQPPGRQPPRPSGPP
SRHTRHWSPSGARPAPTFPPPMS
>gnl|CDD|177595 PHA03357, PHA03357, Alkaline exonuclease; Provisional
MGQSSSSGRGGICGLCKRYNELVTCDGETLALNADCFEDFDFDENTNEAADKPDFPKPNFIDPKNKKKLS
GKSSHSKCAKC
>gnl|CDD|177596 PHA03358, PHA03358, Alkaline exonuclease; Provisional
MGALWSLCRRRVNSIGDVDGGIINLYNDYEEFSLETTKLIAAEEGRACGETNEGLEYDDDSENDELLFLP
NKKPN
>gnl|CDD|223054 PHA03359, PHA03359, UL17 tegument protein; Provisional
MEAHIANETKHSLTRGGGRTPSLVHIIISDACLVAAGIDPALLKDAAPGSPSAAGFRVEVQTRYHATGEC
SPWRSVFAAYVPSGALDSVLIPTVPADHPRLFRITPDPGGLFVSLPVACDAGGRFDPFTVVALRIAIGDA
AEEYYDLLFTYDELVPPGTRYNADGPRLAALCRQFCAYVRSHAALPPAAKEAAAHLEACLGEDGRSNGDP
VLSADAYIDPEEQLTAPGGFDTPAADARIEEDDREILSLIRRAAEVVASRHPVRAAAPREVGGAVASGLR
QGARALGAAGAAGAASGAADADAVLAGLEPPGKGRFVGSGNPRVPDPEGPVLEDVLLLTPGSQKPLSPLE
WLDAGHAALAGGDTPADLWRRRPISIVPRRHYNTGEPFVVVSYENSVAWGGRRAPAPRLPGSLAPALAEA
CAAEGVDHPRNLSPAARAELLRRFPALAAPLGDEEPPLAAFDAAAEVALLERFKAACVRALIAAIREALQ
TEPRLSQLIEYDIPPRQRDWITEIARRAPDLLEALLRAIQNESAEEFSNSALMSAVLAHLAARSTRGRGR
GYVPYHRASLARLAGGDDVYLFDYYSTGGEVIRLSKRPVAVILRGPGNRGQLSCRFIEGAPSASRRTCER
YLPGESYAYICVGFNRRLHALVVFPGGFALEADAAAHLVWPAALIEAVLSRFCRSV
>gnl|CDD|177598 PHA03360, PHA03360, tegument protein; Provisional
METHLYYDTLYQYQGGVYPAHICLPTDDVLPMRVDCIESLYFRCVFFKEGMHYTEWSKLKFTVISREIKF
KDVLKNADIDEVFTGLVVMTIPIPIVDFHFDIDSVILKLVYPHLVHREIVLRLYDLICGRPRSQRPSEVS
AKNIEKDFYQLTSKLNKQTPDEEKRCLFFQQGPLEPPSTVRGLKASGNVKPMQFPAHRNEKMTESFLSDS
WFSQKVRCKKILDFTQTYVVVVCWYELSFSREMQIENNLLSASQLKRVNAADFWDRTNRYLRDIGSRVLT
HIVKTLQIHNRQFKQKFNCNFPINFSFTHLLSFMQLGKDFWILNLTLDSCIIKAIICFLGFKNGGKSFLA
QDEVWGDLIDCSKGSVIYGEKIQWILDSTNNLYSTFREKQNKSWELYVDCCALYVSEKLELDFVLPGGFA
ITGKFALTDGDIDFFNWRFGLS
>gnl|CDD|223055 PHA03361, PHA03361, UL7 tegument protein; Provisional
MEAEGRMIAHPLDESSTLDALLRAALAGDRSLVEVVEELSWQALPRFVCEVREVPGRPPRFTATSVTRLR
VDNPGGRLMLTLDGREGAEVSSEDYFAQCLAQPAFRGFAFAVLTAAEDRVHSLAVPPLVLPHRLVLFRPE
DLLDFALCLLQMYLENCPRSRATASLFVQLSAFLRRAWRRITPLDKMRRLLYIGATWLLNTLMFMVDLSP
FDDERVLPHYAMAKYLLSASNPPPVLTALYSAGPGSVFNLPGPPPCPSGIVRYNPGLLNGPLASEWFRDA
VYRWWTSDRKKLTPESLFYRYY
>gnl|CDD|223056 PHA03362, PHA03362, single-stranded binding protein UL29; Provisional
MEEDDKTVLLPVGPLGYVYARPRDDEDLEELSLLSARSRDSDVAVAPLIRGLTVERDFVVNVAVVAGSKT
TGLGGGGITLKLTPSHFHPNVFVFHGGECISPSSEAPNLTRLCEEARRRFGFSSYAPPPVDNAVETTGEA
ICARLGLDPERTLLYLVVTEGFKEAVYACNTFLHYGGADTVTIGSAEVRRIPLYPVQLFMPDVNRLAADP
FNAKSRSIGEGFVYPKPFYNDALCRLLHGYVLGPAAVALRVRNLDAVARGAAHLAFDENHEGAVLPADKT
FTGFDSTQGKSGRGDGSGGKLSAGGGDERRLASVMAADLALSIESVVSDSVYDEPPPDVSEWPMLCGAEG
HAERLEALGAYMARLAGLVGAMVFSSNSVLYMTEVDDGGAADGKDGGSNPSFYRFYLIAAPHLAGNPQVD
RDGRVLPGTRDVPAAGTSGSDQEFSPDHLALACGFSPQLLARLLFYLERCDAGAFGGRGDLDALKYVASS
LDADVPCELCDGRTRHACAHTTLHRLRTRLPRFGAPLRGPIGVFGTMNSAYSDCDVLGNYAPYSALKRGG
GGEAARAVMQDTYRATLERVMDYLEKEGLIDPDTPTSGEDTSIIRDRASFMTALSNLNRTVDEEAEQFMR
NLVEARDYKIREGLAEANHTFSLSLDPYSSGFCPVLSFLYRRTVLAVVQDLALSQCHGVFAGQQVEGRNF
RNQFQPVLRRRFMDLLNKGFLTTKTVTVTLSESAVMAPDLTASQTEPAIKSMEGDLARVSVEVLRELRVK
NRVVFSGGGANASEAARARVAGMASAYQRPDKRVNILNGPLGFLLKQFHDALFPNGKPPGSDTPNPQWFW
TLLQRNQLPASLLSKEDIETIAFVKRFTDEYAAINFINLTPNNIGELAQFYFANLILKYCDHSQYFINTL
TAILVGSRRPRDPAALAGGPDVESAAEYVLEKLAGRPAAWTATFSSTNLVRSVMATRPLVVLGLSISKYH
GMAGNNRVFQAGNWGGLNGGKNVCPLLSFDRTRRFVLACPRVGFVCESGGFGSGFREDTLREQVRAILDS
GGAAVQTAVYAAALKMLGERGQHMELDDWLALVDDEYLAASLVELNARVIERGGGDWSVEAALEVLKELE
AGATAGGGPAGGGEAFDFGACDDDDEDAADAGAISAPAAGGVKRPGDDDDLFDLPAPPEKRPGLTLDML
>gnl|CDD|223057 PHA03364, PHA03364, hypothetical protein; Provisional
MVRLGRFVRLGDAMSPGILHITEKLLRGQPLNSLRLEELRFLHLVCCKMYNRGLNILLLRETLANTGVRD
NVVLGRKVPVEYWKLLYDALKEMGVSEEMLFSESRAAQLWLHLNSRPALLGGLCRFVFRELGLTHAVKIP
PENLRDGNILFNLGSVYPHRLLRLARFCLRFWGAEEHEPWVRVICQKLWFLYLIITGKLRISRSAFEQQR
SEHYAGLFEFICEDYRTFTGTLPRSPPPLAKSPELDLLFLFNNNPLFYETLAGD
>gnl|CDD|177602 PHA03365, PHA03365, hypothetical protein; Provisional
AYPGSAHAALASRPKSFRGSFRRLRPSEHPETKFQRGVWKFSIHDSYIKITNKQVLQLTADCQCLPPCPS
VGQILKKQIPNFSFNSTTYGSRGTTTAFYAFGDEDNPVKIKPMFVESSDQEIILRLLNPLELMIPAGSLK
FYILPITLVKLDGLYLRCLPDRSPIIMTTSCSQEGTRLNTEEPQVFLSGSPVSSQDEPLPFLLAQKTKPF
LKKFARVHTVQGEVCPVNAVRLGKNYVRVSVDKPSEKLDRPLPVKVGLTLTNDAIIAFRYNPYPKSPWRW
DGASTPIVYFGPPVIIPPNCSTVVEYNNTYYSPLSLKITAIIVNHETNPDFYIYDCEWKPGQTAKLMVTN
TSNFPITISTGTHLGQAIFILAPKFGLSTILSRRYLQRLSTALTLPGGVTVNSSKLPKFERLNKSKNGN
>gnl|CDD|223058 PHA03366, PHA03366, FGAM-synthase; Provisional
MRMPFQLTLLFFADADLSPEEERLVALLLDRPGPLTLISGPLQSEHLLLVTVRGSASDPRPRRQRREELA
LILALLSPLLEYTPLTTESRGKGGSRTLSFSYGPDLNRRPTTFSRELVALLQTLGLREVLRIELGRHLTF
KLLQSPLEHHMDQLLEALLLPDSLLRPYIEGQESRGLVTAPLAPPALTAPLSDPLDKVCNGVMGDLPLGG
DALPVAIQASSPLPGYTVAYYLSLTPTCTSVRSNYLTRGAHSVETGFLHTHGSIQTMGPQLTGLLFQPSL
LPGGLPRASALGWYVTTPSGGGPLSPLAPRQIAETLEAQARSLNCSGVPVVGGFLRTIPTTLALISPLPN
NMLTFTSLLSTISTIALDTARYRPGQYIVALGSFEPSSGPDTPPYLYRDSGLEANKILQALKLFYSLLPG
PCISGSSRPLGPASVLEHLLALCPPGGLLLFLSALPEDVVSGLKPFSASNRETNEEIVKQYFLNVYCSVV
FLVIKNTHEGGEGVTPLDALKRACRLAGCPVHILGRTVPLPGIHFVNDLGNPVYGELRDDQFKPTFPLQP
SRPLSPVSATSEDTRPSPQDESIDWALFNLNSTLLQILSHPTVGSKEYIVRHIDRCGNGRVAQQPGVGPL
DLPVSDYSIVVHSSVKTRRAIETPSSTEDLTYQEADELINSPLTWFDPDDESVLHPAVPGTCSALGEQGY
KVQLDPILGAKYAIVEALTNLMLAPVANLEDITITLSVTWPPTDQAASELYRALAACKEFCRELGVNFTF
TSASSSPRQDQPPQPGPLFNTIVFTASAPVPSSTPRLTPDLKKPGSALVHLSISPEYTLAGSVFEQIFGL
KSGTLPDISPSYLKNLFRAVQHLISEGLVVSGHDVSDGGLIACLAEMALAGGRGVTITVPAGEDPLQFLF
SETPGVVIEVPPSHLSAVLTRLRSRNIICYPIGTVGPSGPSNTFSVSHNGTVLFRESLSSLRSTWRSFSD
EQFELLRPDLTEESMYRKDYGNNEVDLGPLEEGLTTSPLRLYTCPDKRHRVAVLLLPGCPGPHALLAAFT
NAGFDPYPVSIEELKDGTFLDEFSGLVIGGSSGAEDSYTGARAAVAALLSNPAVRDALLRFLNRPDTFSL
GCGELGCQILFALKAVGSTAPSPVPGTETEEQWPITLEPNASGLYESRWLNFYIPETTKSVALRPLRGSV
LPCWAQGTHLGFRYPNDGMEYILRNSGQIAATFHGADVDPGNPARHYPRNPTGNSNVAGLCSADGRHLAL
LFDPSLSFHPWQWQHVPPENGPLKVSPWKLMFQDLHLWCLKHRH
>gnl|CDD|223059 PHA03367, PHA03367, single-stranded DNA binding protein; Provisional
ASEDNLGSQAPVGPCGYIYFYPKETFPLEEASLLGLGYRGSSVVSLPLLCGLTVEPDFSFNVKAPHKKID
PGTVLVKVTSFHREAIVFHNTDKFPPIFEGPGLERLCEETREKFGYTSFVPPGSRGPTDLADLCPAGLDP
DEVIGAVVVTEGFKERLYAGNLVPCVSEAQQVQIGGCEAVKVPLYDETLFEKTSFVQLRGFYNPAVSEYL
FYSLYTSWAQALRVRDVKELIEALEKQFVQDQYKTAKLAPLKEYPAQKLSAPDKDALMLVDSVACELAFS
YGLSFLEAPQEPSAILNYDSWPIFENCETPEDRIKALTEWNAHLAIHVAAQLFSTNSVLYVTRVAKQASV
NTGKGQENLLNSFYMQHGLGSLCEDTYNENGLPKFSGVPGKDLDGSSYTLHHLAYAASFSPQLLARYCYY
LQFCQHQKSSLNQSYEIPNYVGTAANSPLCELCGGKCPAVCINTLFYRLRDRFPPVLKTQRRDPYVVTGV
SGFYNDLDILGNFGRFRDKEDDGNQREETPSYTYWQLNQNILEYLSKMGLIDVTGEDTKLITGIRDFVKV
FKDIDAIVDAEVSKFINEMVKNNINFRESIKSCHHVLQYDCNPYAQAPCPVFLNLYYRSILTIIQDIALP
ICMSYEVDNPLTGNSPSEWLKQHYQTLWTNFKSSCIDKGVLTGKEVKVVHNEDFCDLFDLDAALNGTYAP
VKMQVRLSRASMLCPKNIKIKNRIIFSNSKEALQNGFFKSTHKRDNYIVAGPYMKFLNSYHKRLFPNTKI
SCLYLWHKFSSNKQPPVLPGGSAEELNEFAKFVETNSRAHEEINVLDVVPDCLLTYAKQRLNNAILRACG
QTQFYATTLHGLTPKLQTVPAEEYPHVLGTQPFSSVAEYLLHVKNLTATTVQSPLRESVATVFKSRPIVT
VPLVVNKYTGVNGNNQIFQFGNLGYFMGRGVDRNLLPNSPFKKQQDSSFMRKRHVFATPLVDVLVKRSRR
EAVTFEIETIRRRVQAILEDKDNENVVDPVVLELVKILGDRCASLTSDDVLFYLGGYEILADSVMEKLQT
LADSGVDWSLENARSVLEAVADAPGGDELEFVAVEEPQSVGVQAGDEFLLPGGGSGLLAGKKRRL
>gnl|CDD|223060 PHA03368, PHA03368, DNA packaging terminase subunit 1; Provisional
MFGRQLGEETRRYFERLRRERQERLGAREAPAEASARGGDDLRVPFLNFAIAVPQRHQTVVPGVGTLHDC
CEHAPIFSAVARRLLFTSLVSSQLRESGPDFGLDRATAEAFLSPELRRALSSLRFAEYDPAEAAAHRNAY
YSVMNTFRAMRTSDAFAQLAHFVRRFARLLKTSFRDAGLDEDGGPAKKRAKVDVPTYGKTRGTLELFQKM
ILMHATYFLASVLLGDHAERVERFLRTVFNTPLFSDAAVRHFRQRATVFLVPRRHGKTWFLVPLIALALA
TFRGIKIGYTAHIRKATEPVFEEIGARLRQWFGASRVDHVKGETISFSFPDGSRSTIVFASSHNTNGIRG
QDFNLLFVDEANFIRPDAVQTIMGFLNQTNCKIIFVSSTNTGKASTSFLYNLKGAADELLNVVTYICDEH
MPRVVAHTNATACSCYVLNKPVFITMDGAMRRTAELFLPDSFMQEIIGGGVRERAARDRPVFTKTAGDRF
LLYRPSTVANQGILSPDLYVYVDPAFTANTRASGTGIAVVGRYRDDWIVFGLEHFFLRALTGSSADEIAR
CVAQCLAQVCALHPGRFRSVRVAVEGNSSQDSAVAIATRIARELASLRASGVAPMPPSLLFYHCRPPGSA
VAYPFFLLQKQKTPAFDHFIKRFNSGRVMASQELVSNTVRLQTDPVEYLTKQLKNLTEVVTGGSDTRTFS
GKRGGASDDLMVALVMAVYLSALPPPDAAFAPLTRAVP
>gnl|CDD|223061 PHA03369, PHA03369, capsid maturational protease; Provisional
TQPPRRSMSLGAGRRTEKIETGESVYVKRPDGTTGAYDTGSFLNVSCQEDEAEADTLPSLTPRSDEHFVP
VFCDRCFGTTLEEYELVRFGISADQSGYYVVGTAGVFSPGDPVDPSLYPSTSAGDMDPEHMRKYHLPREN
AEYMVHVAPGRLLYSHKGIPIGKVLCYWHVHENDRCGVNALVGIDNSEDTGKRCVETFTEACGLSWTTLD
VGLNDVIVELSAVVIPARRGCLAKLFTRATVSDGLLEKFGFGSNVLRQGEAPLNALLEILKAKNAEMPGT
LNPSFGSSDESPEWKTFYEALADQLNNLYKLLRTIYKHKDETVIEQYLIEGRKLFSTINGLKAHNEILKT
ASLTAPSRVLAAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPGLVSPYN
PQSPGTSYGPEPVGPVPPQPTNPYVMPISMANMVYPGHPQEHGHERKRKRGGELKEELIETLKLVKKLKE
EQESLAKELEATAHKSEIKKIAESEFKNAGAKTAAANIEPNCSADAAAPATKRARPETKTELEAVVRFPY
QIRNMESPAFVHSFTSTTLAAAAGQGSDTAEALAGAIETLLTQASAQPAGLSLPAPAVPVNASTPASTPP
PLAPQEPPQPGTSAPSLETSLPQQKPVLSKGAF
>gnl|CDD|177607 PHA03370, PHA03370, virion protein US2; Provisional
MGVSMITIVTLLDECDRLPGRSRDAASTLWIFLIKQCMEQIDDDVGVPVVVRPADLFRFAKPFLVLPRRH
RPIVRTKPPDGTGARGTGLAGTRDSFIVRLFEDVGGCSTEWQDVLSGYLMLESEVSGNHSYSLWIVGAAD
ICRPAIEQIPLPKRLLAIKVPGTWSGMPWAIPDGIQTLLTSTWEPKFDTTEDKAHFEDSGMKCVYKIIGS
PPDPPKPPELEPSKDSSCPNRPFCCIACCKKHDDDASIPMGYKTTDKNCITKRGKFNSR
>gnl|CDD|177608 PHA03371, PHA03371, circ protein; Provisional
MGARCSTPSARSPSLEALASETEVLLRSLAGRTVDLPGGDELRIFADCGTTTVNFGKFVRPGSSRLAYVK
FIGRAYAIGSGRKFVIYLSRNGSVYGYENGTGLHFLAKSLHDFLTTKGLSQRDLMVVDGTFLDSQMRPLT
FPIRSTSDTEELLAEEATTNYTSTENLLGRRSSPPTQPLSLCSKSDGGRRGCRLSSRRESNTSTCPCDAH
EGNIPSTLDTLTPEMPGCDSASSSVASVFF
>gnl|CDD|177609 PHA03372, PHA03372, DNA packaging terminase subunit 1; Provisional
MLRGCDIAAIQERYEELIWKKERRTSVISTEFPNVAILCKKRFQMLHPELGLAHSCNEAVLPLMAFCGRY
RDYNSEERRKLTISDALKSALDELKFRPCSEEQRQYQQKLEALTGLYRDPQFLQINSFITDFRKWIDGGF
DTAGGGTRRIYLEPFQKNLLIHVIFFIAVTKLPVLANRVLEYLLHVFDIEFLSESSLNIFKQKATVFLVP
RRHGKTWFIIPIISFLLKNIIGISIGYVAHQKHVSQFVLKEVEFRCRRMFPRKHTIENKDNVISIDHRGA
KSTALFASCYNTNSIRGQNFHLLLVDEAHFIKKDAFNTILGFLAQNTTKIIFISSTNTTNDATCFLTKLN
NSPFDMLNVVSYVCEEHLHSFNEKGDATACPCYRLHKPTFISINSEVRKTANMFLEGAFMDEIMGGTNKI
VENTVLITDQGREEFDIFRYSTINKNLIPFLGKTLYVYLDPAFTSNRRASGTGIAAVGTYRDQYIIYGLE
HYFLRDLLESSETAIAECAAHMILSVLSLHPFFTEVRIAIEGNSNQAAAVRIACIIKQSIQCNKLIRVTF
FHTPDQNQIEQPFYLLGREKRLAVEQFISNFNSGYIKASQELVSFTIKITYDPVEYLLEQIKNIHRITVN
EYVTYSAKKQNCSDDLIIAIIMATYLCSENHAISFREI
>gnl|CDD|223062 PHA03373, PHA03373, tegument protein; Provisional
GNCARRLCDFVLCRRRAPDGAEYVLLRPSEDVELAELEAFLEENFKDFGITQADIRSLSRDTEVVKHLLQ
LLPIYKQCKSRYTFLERCLANGCPPHVRPAAEVECMKSKRILEALDVVILKLLVGEFTMSETDSLNRLLE
KFSTDQSTLCEVEKINRLVDMDGENSKRLLTELASADEAEVESASDPLLHEETGLPQAPPNLQQDEREGT
GPPVTEQPSGRRKSRRKRSEGGARSTRELRGVRKKRI
>gnl|CDD|223063 PHA03374, PHA03374, hypothetical protein; Provisional
SPQPLREQGCEYQGFNSQLEIFCCLATNKSLTTAELNLDQLDTAMGPESTFYTCRAVRRLLLGERLYPFI
QELPPGLIGLTGPRYPGPGLIITGDGIYTFANIDTDTYLPVVYSLELTDPPLEPSGLRALLYFPALLTTT
IDYSSMFRIICRYLSMYEFEECFEQFCATLPPHLQNTCKKNYLKLLEHLKNPSLTALPTSSATAQLEFHK
FSILSFLLSWPNNACLAELRQKIIANVESHPHLLKTLSKQSSFTPIKVTNLALLKYQAAVNQTLPNLHIV
ILKRDPGKRPLKIAVSTPGGPASFWLQYPPSGAMLRVAMCMAVAPHVSHECTELSPGWDQLGDGDTARAL
VALFRRIDYAPKDPPLRKAGMIRNPGPAKDIDENYEARDETPPPLFDSFQPVKHLSINNFKVNVFNTNMV
INTKIVCHPPPWTYRSILDIPRLTNNFVIKKYSVKEPSFTVSVFYSDNVCNGAAININISGDYLHFLFAM
GNLKCFLPIKTIFPVSIANWNSTLDLHGLENQSLVRTGRRDVFWTTNFPSVVSTKDGLNVSWFKAATATI
SKIHGRTLVKQVIREVSPILTHRNARINLIKNRLFTTLESRNRSQIQTLHKRFLECLYECCSFLRLDPHA
VNRLAQEGLFDFSKRIISHSKNKHECALLGYKKCNLIPKILINNKKTRLDELGRNANFLTFIHSTGHHVS
KIKAKLLRHILRRLGLHWRHFKHELKDLLA
>gnl|CDD|223064 PHA03375, PHA03375, hypothetical protein; Provisional
SHGKRVTKAGSDPLLVVSSDFVNFRVRSVPVFVNSYNLTAELSEIEDARLARPVPVDLERIDGIFEALYA
ASPPHVATDKDRAKIVLCRLLLGPVAVPCYCDEWDVNEYLAKTACNCRGPLLYIHRSRCRCGGDGPALLF
TIMEDHYATHVFRGLLSLSEWNAHLPNVFCACSLFRSDRYVMAVLPKDLSIYLEYYPYFLVYLCRYLTVP
EIDDCTNAMIAHLGPQIAPRIIIHYKLLFGFNARPAAPVALSANEDFFLLELQKLWLGVSYHNAVTTDFF
NVVFAAFHRDKGRVMLALRLPSRTVPHLSRFCLSRFKKQVLYFNLKVRYGKNKRESARNGLVYRKTSVVF
ADSDLVWRNLFYVYYEYSLDDNVGGRPRTARLSAPPPSAAPPVPRSGSSPSSLSSSSSSAPPPATDPSSD
PTRRYVRIISRLSFVRYRERLRRRAADPAFDFTPQRPRRRPLAHRREESLAVDGPAPDRRKVPGGREFAE
ITSVSLGRVAVNAFNTNRVINLKAALSKPAVCRVHRIPKNMTHSFVMYKHTFKEPACTVSTFVSNDAADT
NSLNVNIRGSYLEFLYALGVYRLHVNIEDFFLPAAVCNSNSSLDLHGLEDQSVVRSERSKVYWTTNFPCM
ISNTDNVNVGWFKAATAIIPRVSGRDLENVLLKELSCIKEIRDLCIDYGLHRLFTLLELRNSYQIPFLSK
QFILFLRASLLRLHGRERRLKVDRLVFRAISDGLFDYSKNTVAHTKIKHTCALVGTRLANNVPKILVRNK
KIKLDHLGRNANVLTVCRHVDASRIPPIRLTVLRKVLEYLAETSGTAHTKEEINRLLARLCGKVPPTSHR
NAQR
>gnl|CDD|177613 PHA03376, PHA03376, BARF1; Provisional
MARFIAQLLLLASCVAAGQAVTAFLGERVTLTSYWRRVSLGPEIEVSWFKLGPGEEQVLIGRMHHDVIFI
EWPFRGFFDIHRSANTFFLVVTAANISHDGNYLCRMKLGETEVTKQEHLSVVKPLTLSVHSERSQFPDFS
VLTVTCTVNAFPHPHVQWLMPEGVEPAPTAANGGVMKEKDGSLSVAVDLSLPKPWHLPVTCVGKNDKEEA
HGVYVSGYLSQ
>gnl|CDD|177614 PHA03377, PHA03377, EBNA-3C; Provisional
MESFEGEGDSIQSPDNERGDNVQRTGEHVQDPGPGPQAGGASEGLVQREECSRDQQQRGQARGDENRGWM
QRIRRRRRRRAALSGHLLDGEDNVPPWLPPHDITPYSARNIRDAACEAVKQSHLQALSNLILDSGLDTQH
MLCFVMAARQRLQDIRRGPLVAEGGVGWRHWLLTSPSVSWYMGYRTATLRTLTPVPNRVGADSIMLTATF
GCQNGARNENTFSATVWTPPLAGPREQERYAREAEVRFLRGKWQRRYRRIFDLIELCGSLHHIWQNRLQT
EENLLDFVRFMGVMSSCNNPAVNYWFHKTIGNFKPYYPWNAPPNENPYHARRGIKEDVIQTAFRKAQRQG
LSMLATGGEPRGDATSETSSDEDTGRQGSDVELESSDDELPYIDPNMEPVQQRPVMFVSRVPWRKPRTLP
WPTPKTHPVKRTLVKTSGRSDEAEQAQSTPERPGPSDQPSVPVEPAHLTPVEHTTVILHQPPQSPPTVAI
KPAPPPSRRRRGACVVYDDDIIEVIDVETTEEEESVTQPAKPHRKVQDGFQRSGRRQKRATPPKVSPSDR
GPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPSTGPRQQAKCKDGPPASGPHEKQPPSSAPRDMAPSVV
RMFLRERLLEQSTGPKPKSFWEMRAGRDGSGIQQEPSSRRQPATQSTPPRPSWLPSVFVLPSVDAGRAQP
SEESHLSSMSPTQPISHEEQPRYEDPDDPLDLSLHPDQAPPPSHQAPYSGHEEPQAQQAPYPGYWEPRPP
QAPYLGYQEPQAQGVQVSSYPGYAGPWGLRAQHPRYRHSWAYWSQYPGHGHPQGPWAPRPPHLPPQWDGS
AGHGQDQVSQFPHLQSETGPPRLQLSQVPQLPYSQTLVSSSAPSWSSPQPRAPIRPIPTRFPPPPMPLQD
SMAVGCDSSGTACPSMPFASDYSQGAFTPLDINAQTPKRPRVEESSHGPARCSQATTEAQEILSDNSEIS
VFPKDAKQTDYDASTESELD
>gnl|CDD|223065 PHA03378, PHA03378, EBNA-3B; Provisional
MKKAWLSRAQQADAGGASGSEDPPDYGDQGNVGQVGSNPISPEIGPFELSAASEDDPQSGPVEENLDAAA
REEEEPAEQEHNGGDDPLAVHTRQPRFVDVNPTQAPVIQLVHAVYDSMLQSDLRHLGSLFLEQNLNIEEF
IWMCMTVRHRCQAIREKPLPIAKQRRWKLLSPQRTWRMGYRTRHLMVNSFELGGDSVHPVLVTATLGCEE
GERHAVTYSAGIVQPPRMSDQNQKIETAFLMARRARSLSAERYTLFFDLVSSGNTLYAIWIGLGTRNRVA
FVEFVGWLCKKDHTHIREWFRQCTGRPRPTKPWLRAHPVAVPYDDPLTSEEIDLAYARGLAMEIEAVRLP
DDPIIVEDDDESEEIESECDPDEDKSGAEALASIPQTLPDPPTVYGRPKVFARKADLKSTKKCRAIVTDP
SVIKAIEEEHRKKKAARTEQPRATPHSQAPTVVLHRPPTQPLEGPTGPLSVQAPLEPWQPLPHPQVTPVI
LHQPPAQGVQAHGSMLDLLEKDDEDMEQRVMATLLPPSPPQPRAGRRAPCVYTEDLDIESDEPASTEPVH
DQLLPAPGLGPLQIQPLTSPTTSQLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRP
IPMRPLRMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRA
PTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAA
PGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGRPSL
KKPAALERQAAAGPTPSPGSGTSDKIVQAPVFYPPVLQPIQVMRQLGSVRAAAASTVTQAPTEYTGERRG
VGPMHPTDIPPSKRAKTDAYVESQPPHGGQSHSFSVIWENVSQGQQQTLECGGTTKQERAMLGTGDIAVS
SPSSSETSNDE
>gnl|CDD|223066 PHA03379, PHA03379, EBNA-3A; Provisional
MDKDRPGLPAPDDNIEEVPSTSGVQEQASGGDWENVLIEDSDSSSEEEAEDAHLEPPQKGKKRKRVDDDA
GGSAPAQPPCPPQLDLPGREAILGRFPLDLRKLLQAIGAAATHPDTRAIDQFFGSQISNTQRYLMYAMAI
RQAIRDRRRNPASRRCQNKWRLTTLAAGWPMGYQAYSSWMYSYTDDQRTPTRIHLQATLGCEEGRRCHVT
FSAGTFKPPRCSPGDRQWLYVQSCVGELVQSCNPIYSIFFDYMAIHRSLTKIWEEVLTPDQRVPFMEFLG
FLQRTDLIYIKSFVSEALGTTSIQTPWLDENPSTETAQAWNAGLLRGRAYGLDLLRTEGEHDEGATGETR
EESEDTESDGDDEELPRIVSREGTKRKRPPIFLRRLHRLLLMRAGKLTERAREALEKASEPTYGTPRPPV
EKPRPEVPQSLETATSHGSAQVPEPPPVHDLEPGPLHDQHSMAPCPVAQLPPGPLQDLEPGDQLPGVVQD
GRPACAPVPAPAGPIVRPWEASLSQVPGVAFAPVMPQPMPVEPVPVPTVALERPVCPAPPLIAMQGPGET
SGIVRVRERWRPAPWTPNPPRSPSQMSVRDRLARLRAEAQPYQASVEVQPPQLTQVSPQQPMEYPLEPEQ
QMFPGSPFSQVADVMRAGGVPAMQPQYFDLPLQQPISQGAPLAPLRASMGPVPPVPATQPQYFDIPLTEP
INQGASAAHFLPQQPMEGPLVPERWMFQGATLSQSVRPGVAQSQYFDLPLTQPINHGAPAAHFLHQPPME
GPWVPEQWMFQGAPPSQGTDVVQHQLDALGYVLHVLNHPGVPVSPAVNQYHVSQAAFGLPIDEDESGEGS
DTSEPCEALDLSIHGRPCPQAPEWPVQGEGGQDATEVLDLSIHGRPRPRTPEWPVQGEDGQNVTGAESRR
VVVSALVHMCQDDEFPDLQDPPDEA
>gnl|CDD|223067 PHA03380, PHA03380, transactivating tegument protein VP16; Provisional
MLMLVDDFIADFDESLLGPPESETAPAPYATSAPSSAQLALPPPRPASPAALYQRLLTELGFSEGPALLS
ALETWNEDLFSCLPTNEDLYREAALLSTSPSEVVEAGDAPTPTRSPIDLNAHGSEPFPEPPATEDELPAY
VEAVQRFFLSELRAREESYARLLAGYCRALLRYLRASARRLHRGARAGDRDRDLQERLRQLIADRYYREA
ARLARLLYLHLYLSVTREVSWRLHASQVMRQDVFVSLRYDWEQRRQFTCLFQPVLFNHGVVILEGRPLTA
AELREVNYRRRELGLPLIRCGLIEEPGSPLVAEPPFSGNLPRASGYLTHLIRAKLEAYSEAHPSEPLSVL
REHTYARRREKPNYGSTIEALLDPPSPSAVLPGDPVPPLTVSVASTAADAAMPPALALDDFELDLLEYEQ
MFTDALNDMFGG
>gnl|CDD|177618 PHA03381, PHA03381, tegument protein VP22; Provisional
MASRRSPRPKPHGTDEVEADVYYDFISPDASPARVSFEEPADRARRGAGQARGRSQAERRFHHYDEARAD
YPYYTGSSSEDERPADPRPSRRPHAQPEASGPGPARGARGPAGSRGRGRRAESPSPRDPPNPKGASAPRG
RKSACADSAALLDAPAPAAPKRQKTPAGLARKLHFSTAPTSPTAPWTPRVAGFNKRTFCAAVGRVAATHA
RMAAAQLWDLSHPRNDEELNDLLGATNIRIIVCEGLNLVPRANELISPEVAQDVDAAVRGRATARARAPA
RSASRRRPPE
>gnl|CDD|177619 PHA03383, PHA03383, PCNA-like protein; Provisional
MEDDNVLFHIRTIQGSVIKSLFDVLKEILHDVNIFFRPTGVYISALDGAKVSLVHMKLDAESFEEYHCDQ
TYEIGVNVSNMFKLLRTAGSHDSILFRYLKNSPHFLEITIQNFEKNSLTKFQLKLIEIDSSRIEVPDVEF
DTIIILPSNYFQRLCRDMSNITDDLEITKKGKEVSFRSDYTCVTDFASQETIIGDSDNGQITCNESPDYT
GKFSLKYLTSFTKASGMSSSVEIYLKESNPLILKYNVGSLGNLKFVIAPKVS
>gnl|CDD|223068 PHA03384, PHA03384, early DNA-binding protein E2A; Provisional
MRGRGSSSDSPYSSDDSPSLEPPELPPKKKGRRRVSPVEEEEEEEEAEVVAVGFSYPPVRISRGKDGKRP
VRPLKEEKDSEKKASTEAAVRNPLSDPLESKWQKAMEIVAKLMEPLKVDTKGFTLLPDQGECFKKICQTW
LNEEHRGIPLTFSTQKSFLTVMGRFLYAFILKYAGLAPKFWNPTGCVVWRHGCQEGTLKCLHGLPMINKE
HIVEMDVTSENGQRALKENPERAKITQNRWGRNVVQLRNEDARCCVHDAGCGFNQFSGKSCGLFFSDGAK
AQQAFKQIEAFQKALYPNMKRGEEMLLIPLKCECNYGGDLVPILGRQTCKMTPFALSGAEDIDVDLVDDP
VALASVKHPAVLVFQCCNPVYRNSRAQNPGKNCDFKISAPDLLGALQLARQLWQENMGEPPPLVIPEFKW
SPRYQFKNTVLPSGHEDSDDNPFDF
>gnl|CDD|177621 PHA03385, IX, capsid protein IX,hexon associated protein IX; Provisional
MGTAASFEGGVFSPYLTTRLPSWAGVRQNVMGSTVDGRPVLPANSSTLTYATVSSSSLDTAAAAAAAAAA
STARGMALDFGYYPSSNSSSSASRSSLAEDKLLVLLAQLEALSQQLQELSQQVAQLREQTQSAVA
>gnl|CDD|177622 PHA03386, P10, fibrous body protein; Provisional
MSKPSVLTQILDAVQEVDTKVDALQTQLNGLEEDSQPLDGLPAQLTELDTKVSDIQSILTGDEVPDPPDP
PLPLLPEPEFELDSDIPRGRRSRK
>gnl|CDD|177623 PHA03387, gp37, spherodin-like protein; Provisional
MIVLIIVLFALVLAPAVRSHGYLSYPAARQYKCFRDGNFWWPDNGDNIPDPACRNAYKTVYAKYRSAGES
SGVAANAAQYMFQQYYEYAALAGPNYDDFEHIKRNVVPHTLCAAGANDRSAVFGDKSGMDEPFPNWRPDT
LYKNKYQSGHQTNLHFCPTAVHEPSYFEVFVTKPEYDYRNELTWNDLELIGGNGSQLVPNDGSDELCASS
QVYSIPVRVPFRSGKFVLYVRWQRIDVVGEGFYNCADVVFDDYNLEHRYARAAKAVR
>gnl|CDD|177624 PHA03388, ORF1_granulin, Granulin; Provisional
MGYNKSLRYSRHDGTTCVIDNKHLKSLGSVLGDVRRKKDRIREAEYEPIKDIANQYMVTEDPFRGPGKNV
RITLFKEIRRVQPDTMKLVCNWSGKEFLRETWTRFISEEFPITTDQEIMDLWFELQLRPMQPNRCYKFTM
QYALGAHPDYVAHDVIRQQDPYYVGPNNIERINLSKKGFAFPLTCLQSVYNDNFEEFFDDVLWPYFHRPL
VYVGTTSAEIEEIMIEVSLLFKIKEFAPDVPLFTGPAY
>gnl|CDD|177625 PHA03389, polh, polyhedrin; Provisional
MYTRYSYNPTLGRTYVYDNKYYKNLGSVIKNAKRKKHLLEHEKEEKELDPLDKYLVAEDPFLGPGKNQKL
TLFKEIRNVKPDTMKLVVNWSGKEFLRETWTRFMEDSFPIVNDQEVMDVFLVINMRPTRPNRCYRFLAQH
ALRCDPDYVPHEVIRIVEPSYVGSNNEYRISLAKKGGGCPVMNLHSEYTNSFEEFINRVIWENFYKPIVY
IGTDSAEEEEILLEVSLVFKIKEFAPDAPLYTGPAY
>gnl|CDD|223069 PHA03390, pk1, serine/threonine-protein kinase 1; Provisional
NMDKSLSELVQFLKNCEIVKKLKLIDGKFGKVSVLKHKPTQKLFVQKIIKAKNFNAIEPMVHQLMKDNPN
FIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENV
LYDRAKDRIYLCDYGLCKIIGTPSCYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDE
DEELDLESLLKRQQKKLPFIKNVSKNANDFVQSMLKYNINYRLTNYNEIIKHPFLKI
>gnl|CDD|223070 PHA03391, p47, viral transcription regulator p47; Provisional
MFARYYHTTSQPLPQCCKYLADELSLYLLYLNGVDYYVALPYVVVNEVVVDAEGFVRLHCTFVRFDLENL
ETSTPEDLEDYVDVTRGKNLSDHDKRLLKLLLRDRWYKGDFVRLRKILQQPDVSKLIKFACNVLWERGYE
DHYTLGQQLSIRITTKLIQSGLDFKHQQDNDAIVSVRGWNDKKFEKFLSSITSISDIIKRHKFSKKYIVL
ELDANNWTAIKELLQDEFFTVIENAHTNNVCAIEVDDDKNSLQYLRKLSPLIKNKIINVLFVTDVEFYLK
TNNYMFYLYNSLKFYYYCLKNKFVFEYDDYETIFLLYTIVSLEWFNGGHLNSFTLEKSPIYNPLELSTRR
LNSLKRAAAQNRTLCNDSEIKIDFIKGKRIKTGTHYGHRIVQIDL
>gnl|CDD|223071 PHA03392, egt, ecdysteroid UDP-glucosyltransferase; Provisional
MYMTIIILLLLLLLLSGVRAARILAVFPTPAYSHHSVFKVYVEALAERGHNVTVIKPTLRVYYASHLCGN
ITEIDASLSVEYFKKLVKSSAVFRKRGVVADSSTVTADNYMGLVRMISDQFDLPNVKNLIANKNNKFDLL
VTEAFLDYPLVFSHLFGDAPVIQISSGYGLAENFETMGAVSRHPVYYPNLWRSKFGNLNVWETINEIYTE
LRLYNEFSLLADEQNKLLKQQFGPDTPTIRELRNRVQLLFVNVHPVFDNNRPVPPSVQYLGGLHLHKKPP
QPLDDYLEEFLNNSTNGVVYVSFGSSIDTNDMDNEFLQMLLRTFKKLPYNVLWKYDGEVEAINLPANVLT
QKWFPQRAVLKHKNVKAFVTQGGVQSTDEAIDALVPMVGLPMMGDQFYNTNKYVELGIGRALDTVTVSAA
QLVLAIVDVIENPKYRKNLKELRHLIRHQPMTPLHKAIWYTEHVIRNKHGNTSLKTKAANVSYSDYFMSY
ILVPLVTFTVMNHLQQL
>gnl|CDD|223072 PHA03393, odv-e66, occlusion-derived virus envelope protein E66; Provisional
MMIVLILVIIVVVIIIIILLWQSNNNNNTPNPPNPPPNPPPPPPPPPTPEDYHDDLDTFERYYKNTLTQK
FLQKAEKIANPTRQFSDDDNIFDGLSPWTSANDFGTLCHTLIGYCVRYNNPNDALYQDPELAYNLINALR
LIYSHLPDPAPHQQAPWGPVADWYHFSITMPECFMNTCIVLRGYYDAAELTVKILGLYLPEPTFSMGWRR
TAGNAMRMCLPYIYGQLLRGYSLAEIAQEPSVQYVLDLIAFPLVAEGNGIHYDYIYFDHTDVRAYGYLIN
SYFTFSYYNFLFGDNVVNMDNLTRSINLVGSPEGIVNPALMSRNGTLYSNVIGNFIDYPNGVHSADFSKV
LTVRNDTYFGSVVGQTPRLAYYEADPTNNTHAPLWAMTRRIWNRNGRIINYRSNTLGFESGVLLLQNLNG
IVRVPSTTTSTQSFRPAIGYTAIAKTDNAGAMLSHAKFEELNLEFYSYTLYHRTGMFQLYDNIKALPPSN
RNARCVVLTRDTLSFETQRPANTNSSNGTTYNGVTAKHHNITNYKNLPNFTVRTLDNLVQTVEQIISADD
INAGTGVACYSLNVQGHTDNTRVVRVPDTNEFLIVTNGNSIKCVFDFPYVVLKDNETRQVTINNATSSSR
EDHTLPFDVITRLLSLISLSVDNLPVSCTIKRTGNAFVLNNSHGNQFKFKFV
>gnl|CDD|223073 PHA03394, lef-8, DNA-directed RNA polymerase subunit beta-like protein; Provisional
MTDVVRDFNHLYDKLENKYNLQFYLNCKDKEKNENSLKYLQERKSYFCCAVDSLKRCVLHKCVVVVFGTW
LDKRFRDIDEDEQNFGGTFMIDGRHLSFPNIMMNNNILIHNFYDKLYSKDCKRMFLYGNVDEEKDINRAI
QLVYDKQDDVLFVRDVYAKDYVVTEDLNKVLETYLKNSGKWEPLDFLFDFDKGQSIQLVDQIKRIMSVDI
NYSIDSLSNKIIYKHSYLLELTYKPLLKKYQNMLAKDPDAQSAIKRKKNQTILFPKESKKIVDTIVNGKL
IYSVSKTFSKQKKNFPNQQDNSSNNNIEINPPVLKYRIGNEVLRITNDNMRQDMLKQKSDFVKFVDSFFH
GEMTVAGKKFFLCRNVRLPNVDYEMVARKFTSLIESNLIYTNDDEDNDELLIAFNNRPTKYYCRRTDLIK
IFYALKRNRSPIELKLANNILFVNHHEGMICIKKKLRIDNTVRINTLLTPYEYHNENSLLRTKIDLQIEE
NDDVTSLMSKLTQYYYKNYTHIFATIPVPKLIVSLTNLKNAMPVFRYGELEPSDSLPVGNSVVVDPSIYC
NDKMFKLWTLVRDNKLKTAEDPYIPHVNLPIRLYNNKINKLKGKLTYGKNENPVVKFTKSNDNNCVDVEG
GNVLCMAGVVVSNVKINWIYDGKRYKIESCTNKNFYVYKIYVYFRQIKNQRIERLDSEMTVINDTVYLKI
RLVTSTSDLEGLKICGIHGQKGVLNGSEDLTEWMAEDGTHAQICLSPISYLSRQTNFDDIERKYVVRGGD
HSDPNAKRYPIFNIPYMLFNNTPDNIYKEFIKKNYTGHEKVEGTRLDQWTINQSFVGNRLAESLQCVRGG
SNLPQNSGEYNVFSSLLHCNNTIMK
>gnl|CDD|177631 PHA03395, p10, fibrous body protein; Provisional
MSQNILLLIRQDIKAVSDKVDALQAAVDDVRANLPDVTEINEKLDAQSASLDTISSAVDNITDILNPDIP
DVPDVPVKPNRKVKNKK
>gnl|CDD|223074 PHA03396, lef-9, late expression factor 9; Provisional
SATMIEFETKSPTSFDLLTDPNKLDNVFFINIEEFKKFLRNLISDLKKIKINYFNSLIEQLISVYQECEL
RNEHTDLLSKIILATNVVVTDLPSNVFLKKLKTNKFTDNIDYLILPNFILWDHNFIIFLNKKFNSKHENG
LVDISGALQKIKLTHGVIKDQIQNKNGYAGQYLYSTFLNTASFYANVQCLNGANEIVPPKASIERYYGRD
VDNVRAWTTRHPNISQLSTQVSRVDQNDDYTDWNVKVGLGTFPGANRDCDGDKEVITFLPYPNSLIDLEC
LLYGDPRYSFICFDKNRLSFVSQQIYYLYKNRDKVEALLKKMPLIYKLWQNYKNEKFSKRLELLLRDVAL
VLSSNVSYLLFKKLTDLIDDEEMVCGDEELFNLNGQFEDIIESGAKGSKDLIKSTRKYKKTKYTDIDTVA
ERAIKSLNSYISSHNRVKVCGGDIYHNTTVLQNVYLKNNYICYKNDNRVIGSICALPSEFLFPEHLLDLF
IEI
>gnl|CDD|177633 PHA03397, vlf-1, very late expression factor 1; Provisional
NMTNNVRNENNYNIWKLVIQNHPRFEEVFDLAIDRQKCTPDEVKNNSLWSKYMFTKPFAPSTLKSYKSRF
IKIIYCLIDDNHLDNYGWYDLDREFDSIEQQTPLVDPEEFCRRLLELRSVTKKTLQLTINFYTNAMGLPE
YKIPKNVMLPRDKELKNIRAKEKNIVLKDIIDPVLNYIEKKIKYLNSNYVHNRGLIRGAIVFCIILGTGL
RITEARQITLDDLNKLIKKGEHKVNNINLKRKKSRFNYLNCIKKKPLELAREIYQKHPTLLKISKNSSTP
FKDFKRLLEEAGVEMDRPRSNMIRHYLASNMYNSGVPLQKVSKLMNHESVSATRHYLNKYHPGPSLVLDE
SDDDDEEEDDEDD
>gnl|CDD|223075 PHA03398, PHA03398, viral phosphatase superfamily protein; Provisional
MMCSWTCLRNRNALVKRHVLVLAEYADLKYVGFRHLEYFEYVVFAFVVDAQISKIIDTSNYKMQVFKCAD
DMRDIRKNLKTAFKTSYLGHVFVLNEKPPMYAFLKEWYVQNYLEVYQLKSESLVWEIPHVIVFDLDSTLI
TDEEPVRIRDPFVYDSLDELKERGCVLVLWSYGNREHVVHSLKETKLEGYFDIIICGGRKAGEYSRRVIV
DNKYKMVFVKKPFYLDVTDVKNLPKSPRVVLWYLRKKGVNYFKTITLVDDLKSNNYSYDYFVNVKRCPEP
VNDWDKYHDQIVDNIEEYDNTFK
>gnl|CDD|223076 PHA03399, pif3, per os infectivity factor 3; Provisional
MIWGLLVLLIILLIVYYYTLKFVQQLNLNDDEARSRANPPMNLVFERNGIVDCSLTRLPCVTDQQCRDNC
AIGSAAGVMTCDGGFCSARDALVNGQPPDFECDASLGLIKVFTASEFVVNQLCISTYRDIVDDDGELRPY
VCENGTLDIDLENRPFSVDDCVCASGYTKMIFNQTALARTIPVCIPNRLANLYSRIYNTV
>gnl|CDD|223077 PHA03402, PHA03402, hypothetical protein; Provisional
MEELECMSIKITSENGSTISIYCESKSKISLDITTKKNNIKPITTKKSIKKIEKNDDDDLCTDQENAMEI
DGDHATDNNKL
>gnl|CDD|177637 PHA03405, PHA03405, hypothetical protein; Provisional
MGTKLIINVIFFDIILAILMMSFASIQPPNISTPPTTAEAMAQANITWNLSIGNISWDWIWPLFYFVDWL
IWIVTSIFAVVVFIFNVFTTSLSLLASAPVVGPFLLMFAVVINFVLIWEIIKLIRGYDNI
>gnl|CDD|223078 PHA03410, PHA03410, hypothetical protein; Provisional
MVGMGTKLIVYVLLFDVFLSLMVGAYSGITPPSIPPEPSYSFAQAIASSIVWTVGWGPLTLWGPVTLIPP
FSILGANFPGLTLPGLTIPGVTLFSISFSWLAPILYLANWIIWIFQVISSVVGYLFSIFTSSISLLANVP
VVGPFLTAFVLIVNFILIWELVKLIRGYGP
>gnl|CDD|177639 PHA03411, PHA03411, putative methyltransferase; Provisional
MARLSKQEQKLHDRVMELINSDRPLTYEEKEFCYNNYHGDGLGGSGAFFTPEGLAWDFTIDAHCTGKVLD
LCAGIGRLSFCMLHRCKPEKIVCVELNPEFARIGKRLLPEAEWITSDVFEFESNEKFDVVISNPPFGKIN
TTDTKDVFEYTGGEFEFKVMTLGQKFADVGYFIVPTGSAGFAYSGRPYYDGTMKSNKYLKWSKQTGLVTY
AGCGIDTSIYRDEWHSTNVLTEVVEVRYYEKEAVEAPKSRPNEQIEESKEITLPKQESESGTLSDLFDI
>gnl|CDD|177640 PHA03412, PHA03412, putative methyltransferase; Provisional
VESDKALTYEEKLFIIENFHEGAFTNNSELGAFFTPIGLARDFTIDACTSGSVVDLCAGIGGLSFAMVHM
MMYAKPREIVCVELNHTYYKLGKRIVPEATWINADALTTEFDTLFDMAISNPPFGKIKTSDFKGKYTGAE
FEYKVIERASQIARQGTFIIPQMSANFRYSGTHYFRQDESTTSSKCKKFLDETGLEMNPGCGIDTGYYLE
DWKGVKPLCEVVCMEFNEPEPAQNLFTFTIE
>gnl|CDD|177641 PHA03413, PHA03413, putative internal core protein; Provisional
MAIFLNQEPNPQGAGLESEADGAKGADLDAAAERIAWEDAGDLGLNAAERAALLAQAETPAATGLESFAA
GMGNSIIAAAIRKASAPAFDEDPNFDAGQTLSADTRAKLLAPNEEEIEFIGDSRSLDDYNYRKEAMEDQR
DRDGLMADNMFAGFAGMLAGDAPFILAPMGAAGIAGRAGLAARAAIRAADLASAFYAQDQLGQAAAVTAL
AAGLAGLDQLWDMSRAAKAVRAAANAAEVESRALGSATEHVFTAETGLAAKAQTGGVLSDAPEIVPDVVK
PEVAAEPMFDPDAPTNETAEDAKVPGTGEGEESFPILDKPLDERIQASRNGRASVNIKAQDLVQFLKNMD
HLSAGAKAILDALGDAINDIDFKLMAASANRSRYTFAQQDLAKREEIKLRAPAKADGSTFKTVGDALNAM
DADTSRVAVHELIHAATAKAIFQASKGDSAPEIADAIKDLDALHASIAADREFAPKMRYAASNNHEFLAE
LADKPEMVEDLAKLPGVPAGKNALQALAEKILKALGFKAKGSALDDALDAFEDAAKWQAKDNADKANAFF
SDAFADLADDANRGANAAERAKALEDGAKKKLKQMFALWDNIAQGNEDLAKLLVSDASAMGERAPSVVDH
KRNLTLEMDARAAAVEDAILAALKDKHGIGTFDMFFHRAKARAARAAEEDKLSKYLDAAYSADKAGRAIP
TPDADIAPLVDAYRDSGWAEKWHEHLLKAGLIDADAFPKSDYYFPRQYSYDKMRNGIAQGIELDDVKALF
RFALQDTYPNMDGELAARVADEMVDGIVNGRAGQGGPMWKNLINGMDNDELFMALRDAGVDDDAINEFLA
GNVPESGSTAPAKNLRNRLDFNLDKEFDIDGDSLRLQDILDTDTAGLMHGYTNRMSGRVAFANAGIQDLG
ALDKMIDESKHALADGAESWEKAVDDTIDFILGGAPADSGDIPELLRAAGNLANATMLKNSGLYQLTDIA
IAMKEFGLARVLRGLADQGLFKEADAAIADPDMAARLDSILNGAIQKEARFRHIHTYADDNLDLTNQAAA
FNTTQNLGQAARHANGFSMVHRLMANLNAGIIADELENMFKGDAEAFKALEEFGLTPEIADQAIAANAAN
PGALFPPDLQMEIEIVGTRAMDSLMQNIRTGETSHFAQFNPIGKIIVGYQSFAIAATNKILRRELNDADW
AGLAHIMAYQFPLMLLATHAKHALDGKDADSPKELISESALGMSAIGGVSLLQDIFLGDSPRHSLASLGY
VTGLIGAVQDLVSDGNMDIKRFSKILPFAQEFAPLRAIINNFGD
>gnl|CDD|177642 PHA03414, PHA03414, virion protein; Provisional
MAKQFKGRMTPKYPLDQAQLDEAQVQGQLDAVPTVGFDALTGGEIGERNVAAGQRANARELERIVADQEL
PALDRASALWNQSTLVGRWGDALQLDADLAANSTGEVDPNFDAGTYGVQALQAAGIQPTDNYLQIMARAG
NAEDAAYLLSRIQRYEQDEQIVRDNPYWNFAAGMLDPAALAVDAVTFGAGRALRLGRAGMAAAGGAGQVG
YVAGLDAAGADVDAGTYIVAGALGAGVGALLGSGAGRIAAEAPTQPHVPEVSAPTVGLPEVAMTAEEAAA
RGFKAGDVVDLLDEGTVLSRVSARVEQAEIPAIPRRDTAFGDELHSLSGRKLSEVVDHLKTHAEVPKPLQ
GIAAKVADTLKTLEGLGQRTAFRVVQGGDTASSAFLKPGTAGLHSTQGLDTLVQVRGSTAPGRVGTNPVT
VLHEAVHAATVGVMNAALRNPGAMSPKVAQAMQTLENVRGNVLNALKQDRAAGRQLSEFEETLLAGNSNT
LANVKELVAWGLTDTRFQRTLNRLRYSDGGPGLWSRFVEGIRSLLGLRSDADTALSRVLAASETIMDAMP
GYTKAQAKWANKGAPVTEEASLETIVRSTRERAREGAGFVNRFFSEADLLAQPGEGARRLLSRLIDDPVR
RDGFSTNDNAASYLRRYRNEFEGYVKSYDEMMAKAMAEQGVGLTARALNSRRAMAVRDQLNEQVTRELLR
RDREWTAYGSVRVDPNLPPTIKALADRSDEIHGLMGQRAREAGVRGFEDFAPRPGYFHRSWNWSKMAQMD
EAAPGLARRAISEAVFRGIPGLERADADTIAQAIVQRARDRATGIRSEFMGAMGVADTAFIRQALEEANV
SQAKFDSIMAKIEQKQSDQGTVKYGKGRLSLDMTAEINHNGTVYRVQDLIDRDLDRLMENYAGSMSGRSA
LARAGMPGDSEIEAFIREYQREAAHLGTDKVQELTGQLRGVFGDFTGNVPREHQLGPVAQRASGLTSATM
LGFSGVYQLAELATMAHRQGVFNVMKAMLNSRMGDFVGAMRRNPDLADEMQTVLGLNLANDIRMKPWKRQ
FDTFLASQDTFMDRFLHAGKQAVPVLNGMKFIHNWQSRMNANLTLNKVARAAQGDEAALRVLQQYGKDVD
WTPVLARVRGYVTYRGRNAQSMNWGAWSQADVNTVMNTALRIMDDSLLYGRVGQNSGFARSPVGQILGQF
RSFVAFAHNKLLRGTYENSGVLGVASLLAFQYPLTALMMGAKAAINGKFDTSDEGIRKMAIDGIGYTAGL
GFTADMWGVVTGHSRMSAPVFGLAEHSNEVFRGVKDLVTGDDPAAATGDIVSGAAGALPFVNVFPATKLL
LESIKGE
>gnl|CDD|177643 PHA03415, PHA03415, putative internal virion protein; Provisional
MAGPLKPKIQLPADEFQAALNAAAASGLSGDNSLVDGGLAGAAAEDKAQALAAAPLEEAKADAKLSTTDK
VQAAAQETETAYILEAMDDDRDEMFNDFDPNFDGKREAGDILNAHGIEDTDDHLEALAKAGSEEEAIEIA
QGIADHEANEAILAKHGAVAFASGMLDPAMIIADIATFGASKALKLGRLGAAAAGASGATAVSAAADVAG
KDTEAFDYAINAGLTAGAFALFAGGARLPGLDGGLPGAGAAGAAGGMFRGLNAFLSETDKLIAASAEAAA
VLANLVDDPVRRAGILTNDNAASFFRMNSNEADGLFAAWDDGLEKEIAKREGFGTAQIKLDASGRYADAK
DALERKVADELARRDAEWSRFGAVMADPNLDPDIARLADESDAFHGQGAELAKDAGLAGFEDFTARPGYF
HRAWNDSKFQAAEDAYEKGIVKKLLAESIERGIKGLDKDEADAIAGAILQRTHDKAAGLRPDFMGALGKA
DTDAIREMLEAAGTDAARIESIMGKIEQKADDAGKSKYGKHRLPLDMSAKIKAKDGRTIRVADLIDRDLD
RIAENYGQQLAGRSALAAAGIAADDAGIEAFKGRYLASIVNAKLPDADIADLMLQFDGLLGDFTGHRPDA
NILGANAQRAKSLADATMLAASGLWQVAEYATLAQRHGAAETGAEFFKQFPGIAGLLQKAGRDPDLADEL
HSVLGLDLARDVRLRPWKRQHDAFLESRDTLLDRILHAGKQATPILNAMKFIHSHQSRLNANLTLNKFAR
AAKGDRKALAEIREYALDDLAWAKAEKAIDDNAEFNGKNAQEFNWDGWAPDAVDAALNAAARIMDDAILY
GRAGQGASFARSQLGQILGQFRSFVSFAHNKLLRGTINADGPKGLASLLAFQYPLTFLMVAANEARKGES
LDLESEAGLKKLAKKAIGYTAAIGFIGDAAGILGLTGGRGGLSAPLLGLADALGRATGGIAHLAGISRDT
SGEGEGREAAADIGKAARMALPFLGVMPGTALALEALKD
>gnl|CDD|177644 PHA03416, PHA03416, hypothetical E4 protein; Provisional
YIIPTLCLALPSAPRYPLLRLLTDCNDPQRPTPTPAPCATKTGGSHHLPKSHEGKQTPTPTQCGPWTVTA
TPYSLELRTTQQGTQITLTVSL
>gnl|CDD|177645 PHA03417, PHA03417, E4 protein; Provisional
MGAHCIGKYVLAAQLYVLLHLYLALCKKYPFLGLLHTPPPLHRPPPLCPPAFQKNQCKRRLGNDHEDLHN
LQEKPNSPLATLCVTPTLDPLTVETTTSSITITASTKDGTTVTVLLHL
>gnl|CDD|177646 PHA03418, PHA03418, hypothetical E4 protein; Provisional
EILNIIMCCLLMMPIDTVNLANGRSELIRKLCLPLLPAPHHPNPQEDPDKNPSPPPDPPLTPRPPAQPNG
HNKPPVTKQPGGEGTEEDHQAPLAADADDDPRPGKRSKADEHGPAPGRAALAPFKLDLDQDPLHGDPDPP
PGATGGQGEEPPEGGEESQPPLGEGEGAVEGHPPPLPPAPEPKPHNGDATHGLLGTVACLLGTWEESFRQ
LVEDIQEDLDDYWRKLGIPQ
>gnl|CDD|223079 PHA03419, PHA03419, E4 protein; Provisional
QRENISTTTLDLKQMLTDLALLDCGKCMLTKILCLPLLLALRRQLETGYPFCPPTTPHPSSQPPPCPPSP
GHPPQTNDTHEKDLALQPPPGGKKKEKKKKETEKPAQGGEKPDQGPEAKGEGEGHEPEDPPPEDTPPPPG
GEGEVEGGPSPGPGPGPLDQEGLLPGVALRLQKWEQQFDQLVDNIVVDLRDYWQRLRTPQ
>gnl|CDD|177648 PHA03420, PHA03420, E4 protein; Provisional
MTVHLYLAPPLHHPWDTPYYRRLLDGRAENQHIQREGGNHRTWDPADYLDRPHHHPHRHQQDDHHLQDRQ
HLPQQHLQRPHHPLSPQCQQNVTGKPVLQQEPKVGQEVVIPVEDSVTVTVTVGVGNGPELTLTFQLS
>gnl|CDD|177649 PLN00009, PLN00009, cyclin-dependent kinase A; Provisional
MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVV
HSEKRLYLVFEYLDLDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTN
ALKLADFGLARAFGIPVRTFTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEI
DELFKIFRILGTPNEETWPGVTSLPDYKSAFPKWPPKDLATVVPTLEPAGVDLLSKMLRLDPSKRITARA
ALEHEYFKDLGDAP
>gnl|CDD|215027 PLN00010, PLN00010, cyclin-dependent kinases regulatory subunit; Provisional
MGQIQYSEKYFDDTYEYRHVVLPPEVAKLLPKNRLLSENEWRAIGVQQSRGWVHYAIHRPEPHIMLFRRP
LNYQQQQEAQAAQQLQ
>gnl|CDD|177651 PLN00011, PLN00011, cysteine synthase
MEDRCLIKNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKS
TLIEATAGNTGIGLACIGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSK
TPGGYIPQQFENPANPEIHYRTTGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPV
ESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAAL
KVAKRPENAGKLIVVIFPSGGERYLSTKLFESVRYEAENLPIE
>gnl|CDD|215028 PLN00012, PLN00012, chlorophyll synthetase; Provisional
LAVADRSLASSMQALRASARSRRPSRPSTLSSPSPRRRLVVRAAETDTDKVKSQAPDKAPEKSDGGSAVN
QLLGIKGAAQETDIWKIRLQLTKPVTWPPLVWGVLCGAAASGNFHWTLEDVAKSIVCMLMSGPFLTGYTQ
TINDWYDREIDAINEPYRPIPSGAISENEVITQIWVLLLGGLGLAYTLDVWAGHDFPIVFYLALGGSLLS
YIYSAPPLKLKQNGWIGNYALGASYISLPWWAGQALFGTLTPDVVVLTLLYSIAGLGIAIVNDFKSIEGD
RALGLQSLPVAFGVETAKWICVGSIDITQLSVAGYLLAIGKPYYALALLGLIIPQIFFQFKYFLPDPVKN
DVKYQASAQPFLVFGLLVTALATGH
>gnl|CDD|177653 PLN00014, PLN00014, light-harvesting-like protein 3; Provisional
MISMSLSRASSSTLVVSKPNPQSRSSRSLGAKSEGSLVSVTVASTDGGGISERKPSPLERGGTLEGEAAA
GKDPGPAAAAKTSLAVSVGKFEDPRWKNGTWDLNQFKKDGKTDWDAVIDAEVVRRKWLEDNPETSSNDEP
VLFDTSIIPWWAWVKRFHLPEAELLNGRAAMVGFFMAYLVDSLTGVGLVDQMGNFFCKTLLFVTVAGVLL
IRKNEDLDTLKKLADEATFYDKQWQATWKDQDRPSTSSSE
>gnl|CDD|177654 PLN00015, PLN00015, protochlorophyllide reductase
IITGASSGLGLATAKALAETGKWHVVMACRDFLKAERAAKSAGMPKDSYTVMHLDLASLDSVRQFVDNFR
RSGRPLDVLVCNAAVYLPTAKEPTFTADGFELSVGTNHLGHFLLSRLLLDDLKKSDYPSKRLIIVGSITG
NTNTLAGNVPPKANLGDLRGLAGGLNGLNSSAMIDGGEFDGAKAYKDSKVCNMLTMQEFHRRYHEETGIT
FASLYPGCIATTGLFREHIPLFRLLFPPFQKYITKGYVSEEEAGKRLAQVVSDPSLTKSGVYWSWNGGSA
SFENQLSQEASDAEKAKKVWEISEKLVG
>gnl|CDD|215029 PLN00016, PLN00016, RNA-binding protein; Provisional
ALSSSRLRSSSASSLLSSSSSSSISPALAARAQGSRRASQVAGAAAAAAVEKKKVLIVNTNSGGHAFIGF
YLAKELVKAGHEVTLFTRGKEPSQKMKKEPFSRFSELSSAGVKTVWGDPADVKSKVAGAGFDVVYDNNGK
DLDEVEPVADWAKSPGLKQFLFCSSAGVYKKSDEPPHVEGDAVKPKAGHLEVEAYLQKLGVNWTSFRPQY
IYGPGNNKDCEEWFFDRLVRGRPVPIPGSGIQLTQLGHVKDLASMFALVVGNPKAAGQIFNIVSDRAVTF
DGMAKACAKAAGFPEEIVHYDPKAVGFGAKKAFPFRDQHFFASPRKAKEELGWTPKFDLVEDLKDRYELY
FGRGRDRKEADFETDDKILEKLGVPVAA
>gnl|CDD|177656 PLN00017, PLN00017, photosystem I reaction centre subunit VI; Provisional
AGAVSAKYGDKSVYFDLGDLENTTGSWDLYGSDAPSRYNPLQSKFFETFAAPFTKRGLLLKFLALGGGSA
LAYVGAKGSKDALPIKKGPQ
>gnl|CDD|215030 PLN00019, PLN00019, photosystem I reaction center subunit III; Provisional
SATIPANLSKPVLAKAARVAAPRRSARVVCSASKASAAGKFAAALALAAILLAAPMVAPPEALADIAGLT
PCKESKAFAKREKQEIKKLESRLKLYAPDSAPALALNATIEKTKRRFDNYGKAGLLCGADGLPHLIVDGD
QAHLGEFITPGLGFLYIAGWIGWVGRSYLIAVSTEAKPTEKEIIIDVPLALRLMFRGFIWPVAAYRELRN
GTLVAKDSNITVS
>gnl|CDD|215031 PLN00020, PLN00020, ribulose bisphosphate carboxylase/oxygenase activase -RuBisCO activase (RCA); Provisional
VGAVNRASLSLSAVASGASSPPSSAFLGSKVKVSSRRTSSARKSKSSVPVSEEDESKQSEQSSWRGLAQD
ISGDDYDITRGKGMVDSLFQGPFGLGTDSDIASSYDYLQRTRSFDNLVGGYYIAPAFMDKVAVHIAKNFL
ALPNIKVPLILGIWGGKGQGKSFQCELVFKKMGIEPIVMSAGELESENAGEPGKLIRQRYREAADIIKKK
GKMSCLFINDLDAGAGRFGTTQYTVNNQMVNGTLMNIADNPTNVSLGGDWREKEEIPRVPIIVTGNDFST
LYAPLIRDGRMEKFYWAPTREDRIGVVHGIFRDDGVSREDVVKLVDTFPGQPLDFFGALRARVYDDEVRK
WIAEVGVENLGKKLVNSKKGPPTFEPPKMTLEKLLEYGNMLVREQENVKRVQLSDEYLKNAAL
>gnl|CDD|177659 PLN00021, PLN00021, chlorophyllase
TAAQEASPSSAVATSVFETGKFPVELITVDESSRPSPPKPLLVATPSEAGTYPVLLFLHGYLLYNSFYSQ
LLQHIASHGFIVVAPQLYTLAGPDGTDEIKDAAAVINWLSSGLAAVLPEGVRPDLSKLALAGHSRGGKTA
FALALGKAAVSLPLKFSALIGLDPVDGTSKGKQTPPPVLTYAPHSFNLDIPVLVIGTGLGGEPRNPLFPP
CAPDGVNHAEFFNECKAPAVHFVAKDYGHMDMLDDDTSGIRGKITGCMCKNGKPRKPMRRFVGGAVVAFL
KAYLEGDTGDLDAIVDGPSLAPVKLDPVEFIEE
>gnl|CDD|215032 PLN00022, PLN00022, electron transfer flavoprotein subunit alpha; Provisional
TRSAFRAGLAPRAISSRSSIASQSRQISTLVVAEHEGGSVKPQSLSAVAAAKSLLGESSPISLLLAGSGP
SLQQAASHAASSHPSVSEVLVADSDKLTHPLAEPWAKLVVLAQQKGGYSHILAASTSFGKNVLPRAAALL
DVSPITDVVRILDSNTFVRPIYAGNALATVRYKGSGPCMLSIRPTSFPVTPALANSESNEAPISQVDLSL
LDEDSVGKSRWVGLSVQDTERPDLGSAKVVVTGGRGLKSAENFKMLEKLADKLGGAVGASRAAVDAGFVP
NDLQVGQTGKIVAPELYIAVGISGAIQHLAGMKDSKVIVAINKDADAPIFQVADYGLVADLFEAVPELLE
KLPEKK
>gnl|CDD|177661 PLN00023, PLN00023, GTP-binding protein; Provisional
MFWRDRERENKEQNGGPPCGQVRVLVVGDSGVGKSSLVHLIVKGSSIARPPQTIGCTVGVKHITYGSPGS
SSNSIKGDSERDFFVELWDVSGHERYKDCRSLFYSQINGVIFVHDLSQRRTKTSLQKWASEVAATGTFSA
PLGSGGPGGLPVPYIVIGNKADIAPKEGTRGSSGNLVDAARQWVEKQGLLPSSEELPLTESFPGNGGLIA
AAKEARYDKEALIKFFRMLIRRRYFSDELPAPSPWSLSPQRSSQRLDENTSDDDQFYKRTSLAGDPYKYN
TLPPLPAQRNLTPPPTLYPQQPVSSSENYRIPRFSLSSSPESSNARSKRMDINV
>gnl|CDD|215033 PLN00025, PLN00025, photosystem II light harvesting chlorophyll a/b binding protein; Provisional
AMALSSTAFAGQAALKPPNELSRKVGNGRVTMRKTVAKAAGSGSIWYGPDRPKYLGPFSGETPSYLTGEF
PGDYGWDTAGLSADPETFARNRELEVIHARWAMLGALGCVTPELLAKNGVKFGEAVWFKAGAQIFSEGGL
DYLGNPSLVHAQSILAIWACQVVLMGAVEGYRVNGGPLGEGLDPLYPGGSFDPLGLADDPDTFAELKVKE
IKNGRLAMFSMFGFFVQAIVTGKGPLENLADHLADPVANNAWAYATNFVPGK
>gnl|CDD|177663 PLN00026, PLN00026, aquaporin NIP; Provisional
MDNEEVPSAPSTPATPGTPGGPLFGGFRVDSLSYGDRKLLPSCKCFPVEALEWGRLPTCFCDLPPPDVSL
TRKLGAEFVGTFILIFAATAGPIVNQKYDGAETLIGNAACAGLAVMIVILSTGHISGAHLNPSLTIAFAA
LRHFPWKHVPAYIAAQVSASICASFALKGVFHPFMSGGVTVPSVSTGQAFALEFIITFNLLFVVTAVATD
TRAVGELAGIAVGATVMLNILVAGPSTGGSMNPVRTLGPAVAAGNYRAIWIYLVAPTLGALAGAGTYTAV
KLREEDGDPPRPVRSFRR
>gnl|CDD|177664 PLN00027, PLN00027, aquaporin TIP; Provisional
MPIRRIAIGTPGEASHPDALKAALAEFISTLIFVFAGEGSGMAFNKLTDNGSTTPAGLVAAALAHAFALF
VAVSVGANISGGHVNPAVTFGAFIGGNITLLRGILYWIAQLLGSVVACLLLKFSTGGLETSAFSLSSGVG
VWNAFVFEIVMTFGLVYTVYATAVDPKKGDLGIIAPIAIGFIVGANILAGGAFDGASMNPAVSFGPAVVS
WTWTNHWVYWAGPLIGGGIAGLVYELIFIGSTTHEQLPTTDY
>gnl|CDD|177665 PLN00028, PLN00028, nitrate transmembrane transporter; Provisional
QPASPDPKYSKFALPVDSEHKATEFRLFSFARPHMRAFHLSWISFFTCFVSTFAAAPLLPIIRDNLNLTK
SDIGNAGIASVSGSIFSRLAMGPVCDLYGPRYGSAFLLMLTAPAVFCMSLVSSATGFIAVRFFIGFSLAT
FVSCQYWMSTMFNGKIVGTANGIAAGWGNLGGGVTQLLMPLVFPLIKDAGAPSFTAWRIAFFVPGLLHII
MGILVLTLGQDLPDGNYRELKKSGTMPKDSFSKVLRYGVTNYRTWILALTYGYSFGVELTMDNIIAEYFY
DRFGLSLETAGAIAASFGLMNLFARPAGGYLSDVAARRFGMRGRLWALWIVQTLGGVFCIWLGRANSLGA
AIVVMILFSIFVQAACGATFGIVPFVSRRSLGVISGLTGAGGNVGAVLTQLLFFTGSSYSTETGISLMGV
MIIACTLPVAFIHFPQWGGMFFGPSKDAVEEDYYASEWTEEEKEKGLHQGSLKFAE
>gnl|CDD|215034 PLN00032, PLN00032, DNA-directed RNA polymerase; Provisional
MIIPVRCFTCGKVIGNKWDTYLDLLQADYSEGDALDALGLVRYCCRRMLMTHVDLIEKLLNYNTLEKSEN
S
>gnl|CDD|215035 PLN00033, PLN00033, photosystem II stability/assembly factor; Provisional
GAVLFTASSSFFASNNRAAFSTVSKTVSSNVNELSSNSSENRRSFLRQTATAAAALLLLPLLGPSAPADA
AEQSSEWEQVDLPIDPGVVLLDIAFVPDDPTHGFLLGTRQTLLETKDGGKTWVPRSIPSAEDEDFNYRFN
SISFKGKEGWIIGKPAILLHTSDGGETWERIPLSPKLPGEPVLIKATGPKSAEMVTDEGAIYVTSNAGRN
WKAAVEETVSATLNRTVSSGISGASYYTGTFSTVNRSPDGDYVAVSSRGNFYLTWEPGQPYWQPHNRASA
RRIQNMGWRADGGLWLLTRGGGLYVSKGTGLTEEDFDFEEADIKSRGFGILDVGYRSKKEAWAAGGSGIL
LRSTDGGKSWKRDKGADNIAANLYSVKFFDDKKGFVLGNDGVLLRYLG
>gnl|CDD|215036 PLN00034, PLN00034, mitogen-activated protein kinase kinase; Provisional
MKPIQPPPGVPLPSTARHTTKSRPRRRPDLTLPLPQRDPSLAVPLPLPPPSSSSSSSSSSSASGSAPSAA
KSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQICREIEILRDVNHPNVVKCHDM
FDHNGEIQVLLEFMDGGSLEGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIA
DFGVSRILAQTMDPCNSSVGTIAYMSPERINTDLNHGAYDGYAGDIWSLGVSILEFYLGRFPFGVGRQGD
WASLMCAICMSQPPEAPATASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGGPNLHQLLP
PPR
>gnl|CDD|177669 PLN00035, PLN00035, histone H4; Provisional
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKIFLENVIRDA
VTYTEHARRKTVTAMDVVYALKRQGRTLYGFGG
>gnl|CDD|177670 PLN00036, PLN00036, 40S ribosomal protein S4; Provisional
MARGLKKHLKRLNAPKHWMLDKLGGAFAPKPSSGPHKKRECLPLLLILRNRLKYALTYREVQAILMQRHV
KVDGKVRTDKTYPAGFMDVISIPKTNENFRLLYDTKGRFRLHRINDEEAKFKLCKVRKIQFGQKGIPYLN
THDGRTIRYPDPLIKANDTIKIDLETNKIVDFIKFDVGNLVMVTGGRNRGRVGVIKNREKHKGSFEIIHV
KDATGHEFATRLGNVFVIGKGTKPWISLPKGKGIKLSIIEEARKRLAAGQA
>gnl|CDD|177671 PLN00037, PLN00037, photosystem II oxygen-evolving enhancer protein 1; Provisional
APSRASAQLRSSASVSKAFGLEPASARLTCSLQSDLKDFADKCVDAGKAAGFALAASALVASGASAEGVP
KRLTYDEIQSLTYLEVKGTGTANQCPTVDGGDESFSFKPGKYALKKFCLEPTSFTVKAESVFKNGEPEFQ
NTKLMTRLTYTLDEIEGPLKVGSDGSVKFEEKDGIDYAAVTVQLPGGERVPFLFTIKELVATGKPESFGG
DFLVPSYRGSSFLDPKGRGGSTGYDNAVALPAGGRGDEEELAKENNKNTAASTGNITLSVAKSNPETGEI
AGVFESIQPSDTDLGSKVPKDVKIQGIWYAQLE
>gnl|CDD|215037 PLN00038, PLN00038, photosystem I reaction center subunit XI (PsaL); Provisional
VQAAKPKAQVIQPINGDPFIGSLETPVTSSPLIAWYLSNLPAYRTAVSPLLRGVEVGLAHGFLLVGPFVK
LGPLRNTDVAGLAGSLSAAGLVLILTLCLTIYGAASFQEGEPSIAPSLTLTGRKKEPDPLQTADGWAKFT
GGFFFGGISGVAWAYFLLYVLNLPY
>gnl|CDD|177673 PLN00039, PLN00039, photosystem II reaction center Psb28 protein; Provisional
PSIQFIKGTDETTVPDVRLTRSRDGTNGTAIFVFDQPSVFDSSGELGDITGLYMIDEEGVLQTVDVSAKF
VNGKPAGIEAKYVMRSPREWDRFMRFMERYAEENGLGFVKK
>gnl|CDD|215038 PLN00040, PLN00040, Protein MAK16 homolog; Provisional
MQHDEVIWQVINHNHCSFKAKIDTGNFCRNKYNVTGLCNRSSCPLANSRYATIREEDGRFYLYMKTIERA
HMPNKLWEKVKLSRNYEKALEQIDKHLAYWPKFLVHKNKQRLTKMTQYLIRMRKLALKTREKIVTTPRKL
LKRERRRESKAQKAAQLEKSIEKELLERLKSGTYGDIYNFPSKSYNKVLEMEEVEEAEEELPKSDKNPNS
KKKSRVHVEIEYEDEIEYKSLMS
>gnl|CDD|215039 PLN00041, PLN00041, photosystem I reaction center subunit II; Provisional
TTITTPASSGRKLVPWASFLSKSTSKAPASLSATRAVRAAAAAEEAAAKEAPVGFTPPTLNPNTPSPIFG
GSTGGLLRKAQVEEFYVITWESPKEQIFEMPTGGAAIMRQGPNLLKLARKEQCLALGTRLRSKYKITYQF
YRVFPNGEVQYLHPKDGVYPEKVNPGRVGVGQNMRSIGKNVNPIEVKFTGKQAYDL
>gnl|CDD|177676 PLN00042, PLN00042, photosystem II oxygen-evolving enhancer protein 2; Provisional
MASTACFLHQSALKSAAALASSSSASARAVSASRPSQVVCRAQEEDNSAVSRRAALALLAGAAAAGAKVS
PANAAYGESANVFGKPKTNTGFLPYNGDGFKLLVPSKWNPSKEREFPGQVLRFEDNFDATSNLSVMVTPT
DKKSITDYGSPEEFLSKVSYLLGKQAYSGETASEGGFDANAVATAAVLESSTQEVGGKPYYYLSVLTRTA
DGDEGGKHQLITATVSDGKLYICKAQAGDKRWFKGARKFVEGAASSFSVA
>gnl|CDD|165621 PLN00043, PLN00043, elongation factor 1-alpha; Provisional
MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERG
ITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLA
FTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDW
YKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSV
EMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLD
CHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVETFSEYPPLGRFAVRDMRQT
VAVGVIKSVEKKDPTGAKVTKAAAKKK
>gnl|CDD|165622 PLN00044, PLN00044, multi-copper oxidase-related protein; Provisional
ILGILFLLLLAAALALAPAPAGAGDPYAYYDWEVSYVSAAPLGGVKKQEAIGINGQFPGPALNVTTNWNL
VVNVRNALDEPLLLTWHGVQQRKSAWQDGVGGTNCAIPAGWNWTYQFQVKDQVGSFFYAPSTALHRAAGG
YGAITINNRDVIPIPFGFPDGGDITLFIADWYARDHRALRRALDAGDLLGAPDGVLINAFGPYQYNDSLV
PPGITYERINVDPGKTYRFRVHNVGVATSLNFRIQGHNLLLVEAEGSYTSQQNYTNLDIHVGQSYSFLLT
MDQNASTDYYVVASARFVDAAVVDKLTGVAILHYSNSQGPASGPLPDAPDDQYDTAFSINQARSIRWNVT
ASGARPNPQGSFHYGDITVTDVYLLQSMAPELIDGKLRATLNEISYIAPSTPLMLAQIFNVPGVFKLDFP
NHPMNRLPKLDTSIINGTYKGFMEIIFQNNATNVQSYHLDGYAFFVVGMDYGLWTDNSRGTYNKWDGVAR
STIQVFPGAWTAILVFLDNAGIWNLRVENLDAWYLGQEVYINVVNPEDNSNKTVLPIPDNAIFCGALSSL
QKEQSHRFQYSEASPITPLWGKTVKLLFFLACFALW
>gnl|CDD|177677 PLN00045, PLN00045, photosystem I reaction center subunit IV; Provisional
VVRAAEDAEPATSSSAASPAAAAAPAAAPAAKPKPPPIGPKRGSKVKILRPESYWFNDVGKVVAVDQDPG
VRYPVVVRFEKVNYAGVSTNNYALDEIEEVK
>gnl|CDD|215040 PLN00046, PLN00046, photosystem I reaction center subunit O; Provisional
MAATAATASTVSGLGSSSLSAPRRLSSGFVKGPVTVRRRAVLARASGSKKTFDRDWLRKDLNVIGFGLIG
WLAPSSIPAIGGNSLTGLFFDSIGTELAHFPTGPALDSKFWLWLITWHLGLFLCLTFGQIGFKGRKQGYF
N
>gnl|CDD|177679 PLN00047, PLN00047, photosystem II biogenesis protein Psb29; Provisional
MAAVCSVSFPALGQSSKARPAPVSAARSFASRFEVASRSTSRRVVHCMAAVTDVPPTVAETKAKFLKSYK
RPIPSIYSTVLQELLVQQHLMRYKKTYRYDPVFALGFVTVYDQLMEGYPSDEDRDAIFKAYIKALGEDPE
QYRKDAAKLEEWARSQTGSSLVDFSSKEGEIEGILKDIAERAGSKGKFSYSRFFAIGLFRLLELANATEP
TALEKLCAALNINKRSVDRDLDVYRGLLSKLVQAKELLKEYVEREKKKQEERAESQKANEAVTKCLGELE
QAG
>gnl|CDD|177680 PLN00048, PLN00048, photosystem I light harvesting chlorophyll a/b binding protein 3; Provisional
TSGVQTARRALSSSAARSSSAKKARFVVRAEATPPAKQGADRQLWFASKQSLSYLDGTLPGDFGFDPLGL
SDPEGAGGFIEPQWLAYGEVINGRFAMLGAAGAIAPEILGKAGLIPQETALPWFQSGVIPPAGTYDYWAD
PYTLFVLEMALMGFAEHRRAQDYYKPGSMGKQYFLGLEKGLGGSGNPAYPGGPFFNPLGFGKDEKSMKEL
KLKEVKNGRLAMLAILGYFIQALVTGVGPFQNLLDHLADPVNNNVLTNLKFH
>gnl|CDD|177681 PLN00049, PLN00049, carboxyl-terminal processing protease; Provisional
ALTEENLLFLEAWRTVDRAYVDKTFNGQSWFRYRENALKNEPMNTREETYAAIRKMLATLDDPFTRFLEP
EKFKSLRSGTKGAVTGVGLEVGYPTGSDGPPAGLVVVAPAPGGPAARAGIRPGDVILAIDGTSTEGLSLY
EAADRLQGPEGSSVELTLRRGPETRLVTLTREKVSLNPVKSRLCEVPGPGAGSPKIGYIKLTTFNQNASS
AVKEAIETLRANGVDAFVLDLRDNSGGLFPAGIEIAKLWLDKGVIVYIADSRGVRDIYDADGSSAIATSE
PLAVLVNKGTASASEILAGALKDNKRAVVLGEPTFGKGLIQSVFELSDGSGLAVTVARYQTPAGTDIDKV
GITPDHPLPESLPKDEEAFCGCLADPAAACYLNAPQLFS
>gnl|CDD|165628 PLN00050, PLN00050, expansin A; Provisional
MECLGYTIVALLSILKIVEGYGSGWTGAHATFYGGGDASGTMGGACGYGNLYSQGYGTNTAALSTALFNN
GLSCGACFEIKCVNDNIWCLPGSIIITATNFCPPNLALPNNDGGWCNPPQQHFDLSQPVFQKIAQYKAGI
VPVQYRRVACRKSGGIRFTINGHSYFNLVLITNVGGAGDIVAVSIKGSKSNWQAMSRNWGQNWQSNSYLN
GQALSFKVTTSDGRTVISNNAAPSNWAFGQTYTGMQF
>gnl|CDD|177682 PLN00051, PLN00051, RNA-binding S4 domain-containing protein; Provisional
ILAAAAAGDADSALLGVVDPAHREEVKRILEMAERASDRWEVEHTDFLTPPIVKDSMAALEKLADVKAVA
WGGYAQAERCRLSIGRPEVLTSQPDIVAALSVSGNFMFDPASHGDFLGAILGTGITRDKVGDILVQGERG
AQVLVVPELVEFLSSSLTKVRTVPVECRAIPLSALEVEPPRVESFKSVEASLRLDALASAGFRMSRSKLV
DLISSGDVRVNWREVTKNGTTLKTGDVVSVSGKGRLEVGEINTTKKGKFAVELIRYL
>gnl|CDD|177683 PLN00052, PLN00052, prolyl 4-hydroxylase; Provisional
KRLRGALLALALLLAATAVVPLLLLGEAGDDGVGAVAAAPPFNASRVKAVSWQPRIFVYKGFLSDAECDH
LVKLAKKKIQRSMVADNKSGKSVMSEVRTSSGMFLDKRQDPVVSRIEERIAAWTFLPEENAENIQILRYE
HGQKYEPHFDYFHDKINQALGGHRYATVLMYLSTVDKGGETVFPNAEGWENQPKDDTFSECAHKGLAVKP
VKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIHIRSYEHPPVVPKDTEGCADKSAHCAEWAA
AGECEKNPVYMVGAEGAPGNCRKSCGVCDS
>gnl|CDD|215041 PLN00053, PLN00053, photosystem II subunit R; Provisional
VRGLPPLSRTARSFKVTASGGKKIKTDQPYGPSGGMNLKDGVDASGRKGKGKGVYQFVDKYGANVDGYSP
IYTPDEWSPSGDVYVGGTTGLLIWAVTLAGLLAGGALLVYNTSALAQ
>gnl|CDD|215042 PLN00054, PLN00054, photosystem I reaction center subunit N; Provisional
GAVSQMKMPVIKAQRVVRATGAVVDASDGRRAALVGLAATLFSTAAAAASANAGVISDLLAKSKANKELN
DKKRLATSGANFARSRTVQDGTCKFPENFTGCEDLAKQKKVPFISEDLALECEGKDKKKCGSKVFWKWP
>gnl|CDD|177686 PLN00055, PLN00055, photosystem II reaction center protein H; Provisional
MATQSVEGSSRSGPRRTIVGDLLKPLNSEYGKVAPGWGTTPLMGVAMALFAVFLSIILEIYNSSVLLDGI
SVN
>gnl|CDD|177687 PLN00056, PLN00056, photosystem Q(B) protein; Provisional
MTAILERRESESLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGS
LLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMR
PWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSL
FSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPV
VGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAVEAPS
TNG
>gnl|CDD|177688 PLN00057, PLN00057, proliferating cell nuclear antigen; Provisional
MLEARLVQGSLLKKVLEAIKDLVSDANFDCSETGLSLQAMDSSHVALVALLLRADGFEHYRCDRNLSMGI
NLANMSKILKCAGNDDIITIKADDGGDTVTFMFESPKQDRISDFELKLMDIDSEHLGIPETEYSAIVRMP
SAEFQRICKDLSSIGDTVVISVTKEGVKFSTSGDIGTANIVLRQNTTVDKPEEKTVIEMQEPVSLTFALR
YLNSFTKATPLSDTVTLSLSKELPVVVEYKIAEMGYIRYYLAPKIEEDEDMDE
>gnl|CDD|177689 PLN00058, PLN00058, photosystem II reaction center subunit T; Provisional
MASMTMTATFLPAVAKLPSATGGRRLSVVRASTSDNTPSLEVKEQQSTTMRRDLMFTAAAAAVCSLAKVA
MAEEEEPKRGTEAAKKKYAQVCVTMPTAKICRY
>gnl|CDD|177690 PLN00059, PLN00059, PsbP domain-containing protein 1; Provisional
MASSAFAFPSYIITIGASTDSCKPTSLASSRSLVTDFHLLFSRPISSGPKHQSAKSAKPDSPVAINCLTD
AKQVCAVGRRKSMMMGLLMSGLIVSEANLPTAFASIPVFREYIDTFDGYSFKYPQNWIQVRGAGADIFFR
DPVVLDENLSVEFSSPSSSKYTSLEDLGSPEEVGKRVLRQYLTEFMSTRLGVKREANILSTSSRVADDGK
LYYQVEVNIKSYANNNELAVMPQDRVARLEWNRRYLAVLGVENDRLYSIRLQTPEKVFLEEEKDLRRVMD
SFRVEK
>gnl|CDD|177691 PLN00060, PLN00060, meiotic recombination protein SPO11-2; Provisional
MAEAAVAAASLFGSDERLSSADILSPEEARARIEVAVLNFLAALNSPDPAISDLPLISRNCSNVLLRRGL
LQGDVSSIFLSHLFCKRSLTKAGSAKAFVRVWKVMEMCYQILGEGKLVTQRELFYKLLCDSPEYFSCQRH
VNQTVQDVVSLLRCSRYSLGIMASSRGALIGRLVLQEPNEEPVDCSILGISGHAITGDLNLLSNLILSSD
ARYIIVVEKDAIFQRLAEDRFFNHIPCILITAKGYPDLATRFILHRLSQTFPNLPILALVDWNPAGLAIL
CTYKFGSIGMGLEAYRYACNVKWLGLRGDDLQLIPPEAFVELKPRDLQIAKSLLSSKFLQNRYREELTLM
VQTGKRAEIEALYSHGYDYLGKYVARKIVQGDYI
>gnl|CDD|215043 PLN00061, PLN00061, photosystem II protein Psb27; Provisional
ASFAASLTLNGQMTPLQARAEEEAKVEEGEGVVGAIKSLFDPNEKTKSGKKLPKAYLKSAREVVKTLRES
LKEDPKDEAKFRRTADAAKESIREYLGNWRGQKTVAEEESYVELEKAIRSLASFYSKAGPSAPLPEDVKS
EILDDLNKAE
>gnl|CDD|177693 PLN00062, PLN00062, TATA-box-binding protein; Provisional
VPTLQNIVSTVNLDCKLDLKKIALQARNAEYNPKRFAAVIMRIREPKTTALIFASGKMVCTGAKSEHDSK
LAARKYARIIQKLGFPAKFKDFKIQNIVGSCDVKFPIRLEGLAYAHGAFSSYEPELFPGLIYRMKQPKIV
LLIFVSGKIVITGAKVREEIYTAFENIYPVLTEFRKRQQ
>gnl|CDD|215044 PLN00063, PLN00063, photosystem II core complex proteins psbY; Provisional
MATMAALATKCLSINARKNPNPSKTKTKPIILLSMQNKPKGLTISKSADNTNVAGTAIAGAIFSALSSSE
PALAAQQIAELAEGDNRGLALLLPIIPAIAWVLFNILQPALNQVNKMRETKGVVAGLGLGGLAASGFMAA
PPEASAAEEIAMIAAAASDSRGLLLLIVVAPAILWVLYNILQPALNQINKMRSD
>gnl|CDD|215045 PLN00064, PLN00064, photosystem II protein Psb27; Provisional
TPASKPKPLSLIKPPTATAAAVSPPLPPPRRNHLLRREFLSLATTILTSAALLPVAPAFAASDEEYVKET
KDVIGKVRSTINMDKTDPNVADAVAELRETSNSWVAKYRREKALLGRPSFRDMYSALNAVSGHYISFGPT
APIPAKRKARILEEMDTAEKALLRGR
>gnl|CDD|215046 PLN00066, PLN00066, PsbP domain-containing protein 4; Provisional
PSITFSTAFSHLAPSRSSRVHSRPACTNRAVRIADEETEDVATAVSRRSALASGAAAASSAVLAFPGEGL
AVKQGLLAGRVPGLSEPDENGWRTYRRPEGKSGGHGVGWSEITPYSFKVPQGWEEVPVSIADLGGTEIDL
RFASDKEGRLKVVVAPVLRFADNLGDNATIEEIGPPEKVISGFGPELIGEPVEEGKVLSMEVAEHSGRTY
YQFELPPHTLVTATAAGNRVYIFSVTANGLQWKRHYKDLKRIAKSFRVVTEL
>gnl|CDD|177697 PLN00067, PLN00067, PsbP domain-containing protein 6; Provisional
MATASLSPLSLSFSVSSSTSASSSASSPLAVASSVSPRAAVVIHRRELLLGLALAPLILIAPEPPAEARE
VEVGSYLPPSPSDPSFVLFKASPKDTPALRAGNVQPYQFILPPTWKQTRVANILSGNYCQPKCAEPWVEV
KFEDEKQGKVQVVASPLIRLTNKPNATIEEIGSPEKLIASLGPFVTGNSYDPDELLETSVEKIGDQTYYK
YVLETPFALTGSHNLAKATAKGNTVVLFVVSASDKQWQSSEKTLKAILDSFQA
>gnl|CDD|177698 PLN00068, PLN00068, photosystem II CP47 chlorophyll A apoprotein; Provisional
MGLPWYRVHTVVLNDPGRLLSVHIMHTALVAGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLG
ITNSWGGWSITGGTVTNPGIWSYEGVAGAHIVFSGLCFLAAIWHWVYWDLEIFCDERTGKPSLDLPKIFG
IHLFLSGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQPVNPAWGAEGFDPFVPGGIASHHIAAGTLGI
LAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYF
QQEIYRRVSSGLAENQSLSEAWSKIPEKLAFYDYIGNNPAKGGLFRAGSMDNGDGIAVGWLGHPVFRDKE
GRELFVRRMPTFFETFPVVLVDGDGIVRADVPFRRAESKYSVEQVGVTVEFYGGELNGVSYSDPATVKKY
ARRAQLGEIFELDRATLKSDGVFRSSPRGWFTFGHASFALLFFFGHIWHGARTLFRDVFAGIDPDLDAQV
EFGAFQKLGDPTTKRQAV
>gnl|CDD|215047 PLN00070, PLN00070, aconitate hydratase
YRAASSSLSSSSSSPFSLRAQIRAASPVIERFQRKFASMASENPFKGILTSLPKPGGGEFGKYYSLPALN
DPRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSPKQVEIPFKPARVLLQDFTGVPAVVDLA
CMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNML
VVPPGSGIVHQVNLEYLGRVVFNTDGILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMV
LPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMG
FFPVDHVTLQYLKLTGRSDETVAMIEAYLRANKMFVDYNEPQQERVYSSYLELDLEDVEPCISGPKRPHD
RVPLKEMKADWHSCLDNKVGFKGFAVPKEAQSKVAKFSFHGQPAELRHGSVVIAAITSCTNTSNPSVMLG
AGLVAKKACELGLEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVA
SAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVDIDFEKEPIGTGKDGKDVFFRD
IWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPKSTYIHEPPYFKNMTMSPPG
PHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIMARGTFANIR
IVNKLLKGEVGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIA
KSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIDLPSNISEIKPGQDVTVTTDNGKSFTCTLR
FDTEVELAYFDHGGILPYVIRNLIKQ
>gnl|CDD|177700 PLN00071, PLN00071, photosystem I subunit VII; Provisional
MSHPVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPTDFLSVRVYLG
HETTRSIGLAY
>gnl|CDD|177701 PLN00072, PLN00072, 3-isopropylmalate isomerase/dehydratase small subunit; Provisional
MAASQQSANPTLAPSLASTNKSSSSATPRPFLRFSSTSSIFPFKPLTTSSGTSSPTISDSAESTSSTTFH
GLCFVVGDNIDTDQIIPAEYLTLVPSKPDEYEKLGSYALIGLPAFYKTRFVEPGEMKTKYSIIIGGENFG
CGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGEVYPLESEVRICEECKTGDVVTVELGNSVLINH
TTGKEYKLKPIGDAGPVIDAGGIFAYARKTGMIPSA
>gnl|CDD|215048 PLN00074, PLN00074, photosystem II D2 protein (PsbD); Provisional
MTIALGKFTKDENDLFDIMDDWLRRDRFVFVGWSGLLLFPCAYFALGGWFTGTTFVTSWYTHGLASSYLE
GCNFLTAAVSTPANSLAHSLLLLWGPEAQGDFTRWCQLGGLWTFVALHGAFGLIGFMLRQFELARSVQLR
PYNAIAFSGPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAAL
LCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGL
WMSALGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHENLIFPEEVLPRG
NAL
>gnl|CDD|215049 PLN00075, PLN00075, Photosystem II reaction center protein K; Provisional
ICLNFALYSSSFLFTKLLEAYAFLNPIIDVMPVIPLFFFLLAFVWQAAVSFR
>gnl|CDD|215050 PLN00077, PLN00077, photosystem II reaction centre W protein; Provisional
MATVSAAAATCVVARAAAARPVLGLPQLRARSERVRCSYEKKAANKADVNKLAGASLLVTSAATMAYAHP
AFALVDERMSTEGTGLSLGLSNNLLGWILLGVFGLIWSLYTTYTSDLPEDEEDSGLSL
>gnl|CDD|165653 PLN00078, PLN00078, photosystem I reaction center subunit N (PsaN); Provisional
MDPIRRPFTAASSFHRSAAKHLHPAAMLAQRNGISRRCLLTFLTSTAAIPEAGSESRKALLQEYLKKSEE
NKEKNDKERLDDYYKRNYKDYFGLIEGPAREKKEDELTESEKGILEWLDKNK
>gnl|CDD|165655 PLN00081, PLN00081, photosystem I reaction center subunit V (PsaG); Provisional
MAAASLSPPSVAGLRLAPSPRVRAARVAFRAAPARRRSVAARAELSASLVISLSTGVSLFLGRFVFFNFQ
RENVAKQVPAQNGKTHFDAGDERAKEFAALLKSNDPVGFNLVDVLAWGSLGHIVAYYILATCSNGYDPNF
F
>gnl|CDD|215051 PLN00082, PLN00082, photosystem II reaction centre W protein (PsbW); Provisional
AATMAYAHPALALVDERLSTEGTGLGLGVSNGKLTWILVGVTALIWALYFSYSSTLPEGDDDSGLSL
>gnl|CDD|177706 PLN00083, PLN00083, photosystem II subunit R; Provisional
MANSSGPKRGTKAAGGQAGVGYKGSTEAGSAPKTRSGKAGYVYKLGLRNGKANVDEYSPIYTPQEFKTDG
DKYEGDLKLAAAAVAGVIGTGALAILLTSAL
>gnl|CDD|177707 PLN00084, PLN00084, photosystem II subunit S (PsbS); Provisional
MLGFFFTTVGDVVTRGAGPLEQLRDEEMFIGAHASSVLFHPPRFTLVMNHINPAEIAKDALEVAGFYVES
VFILWLCLAAAFIAAVQQGNALAKPVRTYSSKKSANAAAAEAGAERLDAILAGVKDAIDDQVREQKPYEL
FNGRLAMLGFAFAIAGDAVTGGMGPLEQFNGETGVPVIDEELFAAFFLFGVFFNVVATGANVGKRAWAKG
KKVM
>gnl|CDD|177708 PLN00085, PLN00085, photosystem II reaction center protein M (PsbM); Provisional
MSAIAAAGLIPLKAAPVRRAAKAKSSKAVVAPRAAARQEVVAKASPKKLAASVAAAFPAFAAAPAAFAAE
ELNQVALADVNILGVIATALFIIIPTSFLIILYVKSASEGNVSGGFSQKYYDDSKKRGDKKTNEAAILKG
KGLGMRPEK
>gnl|CDD|177709 PLN00088, PLN00088, predicted protein; Provisional
MACAAMASVSSAATAPLATLVWEAKLLSRQGLALAAPSGKKQVSVAISNRSRVVMSLPAKEDHNVASLTS
LALLAAAVVPEIAEAAQPGVSPSLKNLLLSVVAGGVVITVIGVAVAGVSTFDPVKRK
>gnl|CDD|177710 PLN00089, PLN00089, fucoxanthin-chlorophyll a/c binding protein; Provisional
MKFAIFAALCASAAAAAPAQKSRTRPATPTAAAEDDCPGAIGFAAKEFMFIGKTGSKKFDPLGLAEKVEE
FLPWFRESELKHGRAAMLAVAGFIAPDFVRIPGEAYSFAAIPKTIDAHDALLKSGAMIQIFAWIGFVDLA
VSAPAAAAAAEFDRTPGDFGFDLLALYPKDAAKMEKKKDKELKNGRLAMVAIGGIATGSAITGHGFPYI
>gnl|CDD|165663 PLN00090, PLN00090, photosystem II reaction center M protein; Provisional
MKSFQILTLFALIAASLAFAPNKAPQQAAKAAESGFDFKKAAGAAIPAAIAAPAFALDSIVEALPTNTLA
LEVQFGAYLAVALGTFLPCLFLINLFIQTESRKAGRAGGIDAE
>gnl|CDD|215052 PLN00091, PLN00091, photosystem I reaction center subunit V (PsaG); Provisional
MATSALLSTPTFSKAIHHHNLTPSSISFQGLRPLSKAKTTSLLPKISTTAPRKSSAAVVRAELNPSLVIS
LSTGLSLFLGRFVFFNFQRENVAKQVPEQNGLTHFEAGDDRAKEYVSLLKSNDPVGFNIVDVLAWGSIGH
IVAYYILATSSNGYDPSFFG
>gnl|CDD|177712 PLN00092, PLN00092, photosystem I reaction center subunit V (PsaG); Provisional
MATITASTPTTSLVRAALVHKPSVGITSSPVLGLPAMAKKKGRVRCSMEEKPSVQDKSSNMGMGASLMAA
ACAVAMSASPAMALVDERMSTEGTGLPFGLSNNLLGWILLGVFGLIWSLYFVYTSTLEEDEESGLSL
>gnl|CDD|177713 PLN00093, PLN00093, geranylgeranyl diphosphate reductase; Provisional
LSHVSSFLPSAPSSAAKSVSRPGLRVLAAAASKKLSGRKLRVAVIGGGPAGACAAETLAKGGIETFLIER
KLDNAKPCGGAIPLCMVGEFDLPLDIIDRKVTKMKMISPSNVAVDIGKTLKPHEYIGMVRREVLDSFLRE
RAQSNGATLINGLFTRIDVPKDPNGPYVIHYTSYDSGSGAGTPKTLEVDAVIGADGANSRVAKDIDAGDY
DYAIAFQERIKIPDDKMEYYEDLAEMYVGDDVSPDFYGWVFPKCDHVAVGTGTVVNKPAIKKYQRATRNR
AKDKIAGGKIIRVEAHPIPEHPRPRRVRGRVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAIVEGSENG
TRMVDEADLREYLRKWDKKYWPTYKVLDILQKVFYRSNPAREAFVEMCADEYVQKMTFDSYLYKRVVPGN
PLDDIKLLVNTIGSLVRANALRREMEKLSV
>gnl|CDD|215053 PLN00094, PLN00094, aconitate hydratase 2; Provisional
MNVRAAHRTLQSLVRVRSFGLLGTRLSRCTSDTARSSTTLLPLLRTRSTGVIPVISLQSSASATVSASGF
LAEYEAHVAERAQEGIAPKPLDAKQVSELIAQLEAPKSEDADRLVDLLVNRVPPGVDEAAYVKASWLAAV
AKGETRSPLISRARAVEILGTMQGGYNISPLVDALDDDELGRIAADQLSHTLLVFDAFHDVQAKAKKGNA
YATQVMESWADAEWFTKKPPVPEKITVTVFKVTGETNTDDLSPAQDAWSRPDIPLHALAMLKNPREGIQG
PIAQIEELKKKGHPLAYVGDVVGTGSSRKSATNSVLWFMGDDIPNVPNKRTGGVCIGGKIAPIFFNTMED
SGALPIEMDVKNLNMGDVIDIYPYEGVVKRHGTDEVITTFSLKTPVLLDEVRAGGRIPLIIGRGLTSKAR
EALGLDASDVFRMPSVPESKPKGFTLAQKMVGKACGVDEGILPGTYCEPRMTTVGSQDTTGPMTRDELKD
LACLGFSADLVMQSFCHTAAYPKPVDVVTHHTLPDFIRNRGGVSLRPGDGVIHSWLNRMLLPDTVGTGGD
SHTRFPIGISFPAGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVHAIPYTAIQDGLLTVEK
KGKKNVFSGRILEIEGLPHLKCEQAFELSDASAERSAAGCTIKLDKEPIIEYLNSNVVMLKWMIAEGYGD
RRTLERRIARMQQWLADPELLEADPDAEYAAVIEIDMDEIKEPILCAPNDPDDARLLSEVTGDKIDEVFI
GSCMTNIGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMGNQA
RVAEKSTVVSTSTRNFPNRLGKGANVYLASAELAAVAAILGRLPTVEEYLSYMEKLDATASDTYRYLNFD
ELPEYVESAEKVEISEEMREAAKKLSIG
>gnl|CDD|165668 PLN00095, PLN00095, chlorophyllide a oxygenase; Provisional
AARAGPAAANAPAAAMARAEARCAAGARSRAARAQRAGAKAKKGAVDDDASTRARGAPGVDGAGATADAR
AHWFPVAFAAGLRDEDALIAFDLFNVPWVLFRDADGEAGCIKDECAHRACPLSLGKLVDGKAQCPYHGWE
YETGGECAKMPSCKKFLKGVFADAAPVIERDGFIFLWAGESDPADFVGPEAACESIDDDVLAANEPGMFA
PGEGFTPMAEVIADIKLDADEVLERLLAIGERARREATVSFDVSDAKRGRDALFPVDGTKIIAKVLRGGR
DAVPQSATFKPACVIASTIALEDGPGGGDGTDMNVEQLHVCLPAKPGLCRLLFRLAFDFVAVPEGAQAAA
GDVWANLAMMVLKEELEDVRAAGLDDEERSIAVEEFKVFKRGDF
>gnl|CDD|177715 PLN00096, PLN00096, isocitrate dehydrogenase (NADP+); Provisional
MVYVAGEEMTRYTMDLILAKWIEPHVDTSAWEFFDLRAKNRDDTEDQVLRDVIEAGARLKAIFKEPTITP
TADQVKRLGLKKAWGSPNGAMRRGWNGITISRDTIHIDGVELGYKKPVFFERHAVGGEYSAGYKIVGKGT
LVTTFVPEEGGKPIVVDDRTITDDLNAVVTYHNPLDNVHHLARIFFGRCLDAGIVPYVVTKKTVFKWQEP
FWEIMKKVFDEEFKSKFVDKGVMKSGDELVHLLSDAATMKLVVWTDGGFGMAAHNYDGDVLTDELAQVHK
SPGFITSNLVGVDENGTLIKEFEASHGTVTDMDEARLRGEETSLNPLGMVEGLIGAMNHAADVHGGKERV
HPFTAKLRAVIHKLFREGRGTRDLCGAGGLTTEQFIDAVAEEL
>gnl|CDD|165670 PLN00097, PLN00097, photosystem I light harvesting complex Lhca2/4, chlorophyll a/b binding; Provisional
MASIMAIQLAAGLKQKSRTVRPRGVASKARASRGPGAVAAAADRPTWLPGKAAAAHLDGSLPCDYGFDPL
NLGADPEMLKWFVQAELMHARWAMLGLAGCVAPELLTKIGMADLPNWIDAAKWDGYWAGAGPLFFIQMAM
FNWAEIRRWQDMKAPGSMNEDPLFGANKGDTNTDVGYPKGLFDKFGWAKDEKKAAELKLKEIANGRLAML
AFLGCCAQAIQTGTGPVDNLFSHLADPGHNGIFG
>gnl|CDD|177716 PLN00098, PLN00098, light-harvesting complex I chlorophyll a/b-binding protein (Lhac); Provisional
MALAIASSALSSLTLSTRRVPQKALRRPIVASQSGTGGRMKVRLNATKGGVSSVCEPLPPDRPLWFPGSS
PPEWLDGSLPGDFGFDPLGLGSDPELLKWFAQAELMHSRWAMLAVAGILIPECLERLGFIENFSWYDAGA
REYFADPTTLFVVQMVLMGWAEGRRWADLIKPGCVDIEPKLPNKTNPKPDVGYPGGLWFDPMMWGRGSPE
PVMVLRTKEIKNGRLAMLAFVGFCFQAVYTGEGPIENLMAHLADPGHCNVFSAFTSH
>gnl|CDD|177717 PLN00099, PLN00099, light-harvesting complex IChlorophyll A-B binding protein Lhca1; Provisional
MASNTLMSCGIAAVFPSLLSSSKSKFASSVPLPNANGSSRVTMSADWMPGQPRPPYLDGSAPGDFGFDPL
RLGEVPENLERYKESELIHCRWAMLAVPGILVPEALGLGNWVKAQEWAAIPGGQATYLGNPVPWGTLPTI
LAIEFLAIAFVEHQRSMEKDPEKKKYPGGAFDPLGYSKDPKKFEEYKVKEIKNGRLALLAFVGFCVQQSA
YPGTGPLENLATHLADPWHNNIGDIIIPRSISP
>gnl|CDD|215054 PLN00100, PLN00100, light-harvesting complex chlorophyll-a/b protein of photosystem I (Lhca); Provisional
MASLTTASAGANRVRVSAGVSTTRRPRVRVAARARPMWYPGATAPKYLDGTMAGDYGFDPLRLGANPETL
PYLQEAELMNGRWAMAATAGILFTDAVGLPKFWEAGAEKYGLDLQTLVLIQVVVMAVLEAARYRGFMKTG
ESGVLSFFPFDPTGMDSPEMKVKEVKNGRLAMLAFLGMVSQYAVTGKSPLEGLKAHMANPGHVNIFTSSV
GPETVATVAFLSVAPTIIEATKTLNPGDEEFRPIPW
>gnl|CDD|215055 PLN00101, PLN00101, Photosystem I light-harvesting complex type 4 protein; Provisional
MATVTTQASAAVFRPCSSKSRFLSGSSSKLNRELSFKPMPSSATRSFKVEAKKGEWLPGLASPGYLNGSL
PGDNGFDPLGLAEDPENLKWFVQAELVNGRWAMLGVAGMLLPEVFTKIGIINAPQWYDAGKAEYFASSST
LFVIEFILFHYVEIRRWQDIKNPGSVNQDPIFKQYSLPPNEVGYPGGIFNPLNFAPTEEAKEKELANGRL
AMLAFLGFVVQHNVTGKGPFENLLQHLSDPWHNTIVQTLS
>gnl|CDD|177720 PLN00103, PLN00103, isocitrate dehydrogenase (NADP+); Provisional
MAFEKIKVANPIVEMDGDEMTRVIWKSIKDKLIFPFLDLDIKYFDLGLPNRDATDDKVTVESAEATLKYN
VAIKCATITPDEARVKEFGLKQMWKSPNGTIRNILNGTVFREPIICKNIPRLVPGWTKPICIGRHAFGDQ
YRATDAVIKGPGKLKLVFVPEGKDEKTELEVYNFTGAGGVALSMYNTDESIRAFAEASMNTAYQKKWPLY
LSTKNTILKKYDGRFKDIFQEVYEAQWKSKFEAAGIWYEHRLIDDMVAYALKSEGGYVWACKNYDGDVQS
DFLAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHYRVHQKGGETSTNSIASIFAWSRGLAHRAKLDG
NARLLDFTEKLEAACVGTVESGKMTKDLALLIHGPKVSRDQYLNTEEFIDAVAEELKARL
>gnl|CDD|215056 PLN00104, PLN00104, MYST -like histone acetyltransferase; Provisional
SMEAPATEDAGRPAAPAASDDAAATDGAGANAAAPAAPAESDPSKKRPGVMLPLEVGTRVMCRWRFDGKY
HPVKVIERRRGGSGGPNDYEYYVHYTEFNRRLDEWVKLEQLDLDTVETVGDEKVEDKVASLKMTRHQKRK
IDETHVEEGHEELDAASLREHEEFTKVKNIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKR
KEQLQRHMKKCDLKHPPGDEIYRHPTRQEGLSMFEVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLF
YVLCECDDRGCHMVGYFSKEKHSEEDYNLACILTLPPYQRKGYGKFLIAFSYELSKREGKVGTPERPLSD
LGLVSYRGYWTRVLLEILKKHKGNISIKELSDMTAIKAEDIVSTLQSLNLIQYRKGQHVICADPKVLEEH
LKAAGRGGLEVDPSKLIWTPYKEQPPRKPF
>gnl|CDD|215057 PLN00105, PLN00105, malate/L-lactate dehydrogenase; Provisional
LKETTRKAIKTYGYDDEDAEVLLDVMMYAQLRGNNQGLIKVTTKGILAPDPNATPITIEHETKTSAAVDG
NKNAGMLVLHHAMDMAIDKAKTHGVGIVGTCNTSTSTGALGYYAEKVAQQGLIGLVFANSPEFVAPAGGI
EPIFGTNPIGVGIPSSDGFPFVLDMATSAYSFFGLLEAKTAGKKLPRGVAIDKQGILTTDPNEVLDGGAI
DTFGGYKGSGLALTVELLAGALVGAAWGEDVTGKMSAKNWGHLFVAIDPKLLGQDDFEKNAAEVTQAVKD
SKKAPGVDEIWLPGERGNDARVERTAQGGMKVPIPLWKNMKALAETRPGL
>gnl|CDD|215058 PLN00106, PLN00106, malate dehydrogenase
SMEASSLRACRAKGGAPGFKVAVLGAAGGIGQPLSLLMKMNPLVSELHLYDIANTPGVAADVSHINTPAQ
VRGFLGDDQLGDALKGADLVIIPAGVPRKPGMTRDDLFNINAGIVKTLCEAVAKHCPNALVNIISNPVNS
TVPIAAEVLKKAGVYDPKKLFGVTTLDVVRANTFVAEKKGLDPADVDVPVVGGHAGITILPLLSQATPKV
SFTDEEIEALTKRIQNGGTEVVEAKAGAGSATLSMAYAAARFADACLRGLNGEADVVECSYVQSEVTELP
FFASKVRLGRNGVEEVLGLGPLSEYEQKGLEALKPELKASIEK
>gnl|CDD|165679 PLN00107, PLN00107, FAD-dependent oxidoreductase; Provisional
IARLAAGHLAKQRRGVIPPFPGAAVIGSQDRIMSSGACLDGADDGLITACPWDPRIKHGEFFFQSAISVP
LSGAAAFINDIKALRDIEPDALCGLELNYGVLLRYVRASPAHLGKEEDALDFDLTYYRSKDDPAAPRLHE
DAMEEIEQMAILKYGALPHWGKNRNAAFDGAIAKYKKAGEFLKVKERLDPEGLFSSEWSDKILGLAGAGG
VSIVKDGCALEGLCICSDDAHCAPEKGYLCRPGKVYKEARVCRLVAA
>gnl|CDD|177724 PLN00108, PLN00108, unknown protein; Provisional
MENLNHKWDRCSSSHQTPLAFKGNQKQIGQAHREVFTHFVSLPLAIYPDLKKNIEAFQNSVLGNNDKDPL
KFQSTLAEMGIEKSIFVSPKTFHLTVVMLKLENNESVVKAQNILKSICSNVRQALKDRPVFIRLRGLDCM
NGSLDKTRVLYAPVEEVGHEGRLLNACHVIIDAFENAGFAGKDAKSRLKLHATLMNASYRKDKSKKMDTF
DAREIHKEFENKDWGTYLIREAHISQRYKYDPNGYFHCCASLPFPHK
>gnl|CDD|177725 PLN00110, PLN00110, flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
TSLLLELAAATLLFFITRFFIRSLLPKPSRKLPPGPRGWPLLGALPLLGNMPHVALAKMAKRYGPVMFLK
MGTNSMVVASTPEAARAFLKTLDINFSNRPPNAGATHLAYGAQDMVFADYGPRWKLLRKLSNLHMLGGKA
LEDWSQVRTVELGHMLRAMLELSQRGEPVVVPEMLTFSMANMIGQVILSRRVFETKGSESNEFKDMVVEL
MTTAGYFNIGDFIPSIAWMDIQGIERGMKHLHKKFDKLLTRMIEEHTASAHERKGNPDFLDVVMANQENS
TGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPY
LQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKN
AKIDPRGNDFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLPDGVELNMDEAFGLALQKAVPLS
AMVTPRLHQSAYAA
>gnl|CDD|215059 PLN00111, PLN00111, accumulation of photosystem one; Provisional
LLPSSIPSLRKLKLSLSFRCSSQLHRRKLSSVIRSEYPQNADLPRPYSKREKKPYPRPMKLLRREAREKK
KLRKLQPERPLDPPKNGLLVKRLVPVAHEVYKARKLLISGVSKLLKVVPVHACKFCSEVHVGKVGHLIRT
CRGPGSGARNGLHEWIPGSVEDVLVPVESYHLYDRFGKRIKHDERFDVPRIPAIVELCIQAGVDIPEYPT
KRRTKPIYRIGGRIVDFEDESEEPDPPPEGPSSPLLTELDDSEIEAPSSEEELKELAEETLEAWEKVRSG
VKKLMRKYPVKVCGYCPEVHVGPSGHKVRLCGAFKHQQRDGQHGWQEATVDDLVPPNYVWHVRDQDGPPL
VNELRRYYGKAPAVVELCVQAGAIVPDKYKSMMRLDVVIPDSDEADLVA
>gnl|CDD|215060 PLN00112, PLN00112, malate dehydrogenase (NADP); Provisional
MAVAELSTPKVTSPFLNTSSRLRSSQLGLSRTHLSNHFRRALLPRRRATNARISCSVNQASQAPAAVQEK
GVKTKKECYGVFCLTYDLKAEEETKSWKKLINVAVSGAAGMISNHLLFKLASGEVFGPDQPIALKLLGSE
RSKQALEGVAMELEDSLYPLLREVSIGIDPYEVFQDAEWALLIGAKPRGPGMERADLLDINGQIFAEQGK
ALNEVASRNVKVIVVGNPCNTNALICLKNAPNIPAKNFHALTRLDENRAKCQLALKAGVFYDKVSNVTIW
GNHSTTQVPDFLNAKINGLPVKEVITDHKWLEEEFTPKVQKRGGVLIKKWGRSSAASTAVSIADAIKSLV
TPTPEGDWFSTGVYTDGNPYGIAEGLVFSMPCRSKGDGDYEIVKDVEIDDYLRERIKKSEAELLAEKRCV
AHLTGEGGAFCDLRPEDTMLPGEM
>gnl|CDD|215061 PLN00113, PLN00113, leucine-rich repeat receptor-like protein kinase; Provisional
MAKKGPQHCPYLIFMLFFLFLNFSMLHAEELELLLSFKSSINDPLKYLSNWNSSADVCLWQGITCNNSSR
VVSIDLSGKNISGKISSAIFRLPYIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNNNFTGSIPRGSIP
NLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQ
MKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSI
FSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSGEIPK
NLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGEL
PSEFTKLPLVYFLDISNNNLQGRINSRKWDMPSLQMLSLARNKFFGGLPDSFGSKRLENLDLSRNQFSGA
VPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQNQLS
GEIPKNLGNVESLVQVNISHNHLHGSLPSTGAFLAINASAVAGNIDLCGGDTTSGLPPCKRVRKTPSWWF
YITCTLGAFLVLALVAFGFVFIRGRNNLELKRVENEDGTWELQFFDSKVSKSITINDILSSLKEENVISR
GKKGASYKGKSIKNGMQFVVKEINDVNSIPSSEIADMGKLQHPNIVKLIGLCRSEKGAYLIHEYIEGKNL
SEVLRNLSWERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIIIDGKDEPHLRLSLPGLLCTDTKCFI
SSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPADAEFGVHGSIVEWARYCYSDCHLDMWIDPSIR
GDVSVNQNEIVEVMNLALHCTATDPTARPCANDVLKTLESASRSSSSCVTGLKFSSLF
>gnl|CDD|177729 PLN00115, PLN00115, pollen allergen group 3; Provisional
MSSLSFLLLAVALAALFAVGSCATEVTFKVGKGSSSTSLELVTNVAISEVEIKEKGAKDWVDDLKESSTN
TWTLKSKAPLKGPFSVRFLVKGGGYRVVDDVIPESFKAGSVYKTGIQV
>gnl|CDD|177730 PLN00116, PLN00116, translation elongation factor EF-2 subunit; Provisional
MVKFTAEELRRIMDKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITI
KSTGISLYYEMTDESLKDFKGERDGNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTE
TVLRQALGERIRPVLTVNKMDRCFLELQVDGEEAYQTFSRVIENANVIMATYEDPLLGDVQVYPEKGTVA
FSAGLHGWAFTLTNFAKMYASKFGVDESKMMERLWGENFFDPATKKWTTKNTGSPTCKRGFVQFCYEPIK
QIINTCMNDQKDKLWPMLEKLGVTLKSDEKELMGKALMKRVMQTWLPASDALLEMIIFHLPSPAKAQRYR
VENLYEGPLDDKYATAIRNCDPNGPLMLYVSKMIPASDKGRFFAFGRVFSGTVATGMKVRIMGPNYVPGE
KKDLYVKSVQRTVIWMGKKQESVEDVPCGNTVAMVGLDQFITKNATLTNEKEVDAHPIKAMKFSVSPVVR
VAVQCKNASDLPKLVEGLKRLAKSDPMVQCTIEESGEHIIAGAGELHLEICLKDLQDDFMGGAEIKVSDP
VVSFRETVLEKSCRTVMSKSPNKHNRLYMEARPLEEGLAEAIDDGRIGPRDDPKIRSKILAEEFGWDKDL
AKKIWCFGPETTGPNMVVDMCKGVQYLNEIKDSVVAGFQWATKEGALAEENMRGICFEVCDVVLHADAIH
RGGGQIIPTARRVIYASQLTAKPRLLEPVYLVEIQAPEQALGGIYSVLNQKRGHVFEEMQRPGTPLYNIK
AYLPVIESFGFSGTLRAATSGQAFPQCVFDHWDMMSSDPLEAGSQAAQLVADIRKRKGLKEQMPPLSEYE
DKL
>gnl|CDD|215062 PLN00118, PLN00118, isocitrate dehydrogenase (NAD+)
MAAQLLRRLLGNRLAQILGASSSSSGAFSSSARAFSSSSTPITATLFPGDGIGPEIAESVKQVFTAAGVP
IEWEEHYVGTTVDPRTGSFLTWESLESVRRNKVGLKGPMATPIGKGHRSLNLTLRKELGLYANVRPCYSL
PGYKTRYDDVDLVTIRENTEGEYSGLEHQVVRGVVESLKIITRQASLRVAEYAFHYAKTHGRKRVSAIHK
ANIMKKTDGLFLKCCREVAEKYPEIVYEEVIIDNCCMMLVKNPALFDVLVMPNLYGDIISDLCAGLIGGL
GLTPSCNIGENGLALAEAVHGSAPDIAGKNLANPTALLLSAVMMLRHLKLNEQAEQIHNAILNTIAEGKY
RTADLGGSSTTTDFTKAICDHL
>gnl|CDD|177732 PLN00119, PLN00119, endoglucanase
LKNGSSQCLWTLSICIVLLVMSMARGAVSTNYGEALTKSLLYFEAQRSGKLPSNQRVTWRGDSALRDGSD
AHVDLTGGYYDAGDNMKFGFPLAFTTTMLAWSNIEMGSQLKAHHELGNALAALKWATDYLIKAHPQPNVL
YGQVGDGNSDHACWMRPEDMTTPRTSYRIDAQHPGSDLAGETAAAMAAASIAFAPSDPAYASILIGHAKD
LFEFAKAHPGLYQNSIPNAGGFYASSGYEDELLWAAAWLHRATNDQTYLDYLTQASNTGGPRTVFAWDDK
FVGAQVLVAKLALEGKVESNGKIVEYKSMAEQFICNCAQKGSNNVKKTPGGLLWFLPWNNLQYTTAASFV
LSAYSKYLEAAKASIQCPNGALQASDLLQLARSQVDYILGSNPKNMSYMVGYGTNYPKKPHHRGASIVSI
KKDKTPVTCSGGFDAWYNNPAPNPNVLMGAIVGGPDDNDVYGDERSNFQQAEPATVTVAPFVGVLAAVA
>gnl|CDD|215063 PLN00120, PLN00120, fucoxanthin-chlorophyll a-c binding protein; Provisional
MKSALFASLIASAAAFAPAQVAKARTSVATNMAFENELGAQAPLGFFDPLGLVDDGDQEKFDRLRYVEIK
HGRISMLAVVGYLVTEAGIRLPGDIDYSGTSFSDIPNGFAALDAIPTAGLLQILAFIGFLELAVMKDITG
EGEFVGDFRNGYIDFGWDSFDEETKLKKRAIELNQGRAAQMGILALMVHEQLGVELPIIPSL
>gnl|CDD|177733 PLN00121, PLN00121, histone H3; Provisional
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQR
LVREIAQDFKTDLRFQSSAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
>gnl|CDD|215064 PLN00122, PLN00122, serine/threonine protein phosphatase 2A; Provisional
SSSASSGSSAPAVNSSPSSSSSGKSSNSSKSASSAVNPASVVAGYEPLPSFRDVPNSEKQNLFVRKLVAE
RALFLWNNDHIVNLIAQNRQVILPIIFPALEKNTRGHWNQAVHGLTLNVRKMFSEMDPELFEECLRKFEE
DEAKAKEVEEKREATWKRLEEAAAAKAITS
>gnl|CDD|215065 PLN00123, PLN00123, isocitrate dehydrogenase (NAD+)
LLKRLLSNALGSKAQRRSVTYMPRPGDGAPRAVTLIPGDGIGPLVTGAVEQVMEAMHAPVYFERYEVHGD
MKKVPEEVLESIRRNKVCLKGGLATPVGGGVSSLNVQLRKELDLFASLVNCFNLPGLPTRHENVDIVVIR
ENTEGEYSGLEHEVVPGVVESLKVITKFCSERIAKYAFEYAYLNNRKKVTAVHKANIMKLADGLFLESCR
EVAKKYPGIKYNEIIVDNCCMQLVSKPEQFDVMVTPNLYGNLVANTAAGIAGGTGVMPGGNVGADHAVFE
QGASAGNVGNEKLVEQKKANPVALLLSSAMMLRHLQFPSFADRLETAVKRVIAEGKYRTKDLGGSSTTQE
VVDAVIANLD
>gnl|CDD|177736 PLN00124, PLN00124, succinyl-CoA ligase [GDP-forming] subunit beta; Provisional
MLRGLLNKLASRSLSVAGKWQHQQLRRLNIHEYQGAELMSKYGVNVPKGAAASSLDEVKKALEKMFPDEG
EVVVKSQILAGGRGLGTFKNGLKGGVHIVKKDKAEELAGKMLGQILVTKQTGPAGKPVNKVYLCEKMSLV
NEMYFAILLDRASAGPLIIACSKGGTSIEDLAEKFPEKIIKVPIDIFKGITDEDAAKVVDGLAPKVADRN
DAIEQVKKLYKLFCKCDCTMVEINPLAETADGQLVAADAKLNFDDNAAFRQKEIFALRDTSQEDPREVAA
AKADLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGSPANFLDVGGNASEQQVVEAFKILTSDDKVKAIL
VNIFGGIMKCDVIASGIVNAAKQVGLKVPLVVRLEGTNVDQGKRILKESGMTLITAEDLDDAAEKAVKAL
AI
>gnl|CDD|215066 PLN00125, PLN00125, Succinyl-CoA ligase [GDP-forming] subunit alpha
ASPPPAVFVDKNTRVICQGITGKNGTFHTEQAIEYGTKMVGGVTPKKGGTEHLGLPVFNTVAEAKAETKA
NASVIYVPPPFAAAAILEAMEAELDLVVCITEGIPQHDMVRVKAALNRQSKTRLIGPNCPGIIKPGECKI
GIMPGYIHKPGRIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFVKDPQTEGII
LIGEIGGTAEEDAAAFIKESGTEKPVVAFIAGLTAPPGRRMGHAGAIVSGGKGTAQDKIKALREAGVTVV
ESPAKIGVAMLEVFKERGLL
>gnl|CDD|165695 PLN00126, PLN00126, succinate dehydrogenase, cytochrome b subunit family; Provisional
MEKYNSNARFAPLSDAPFALRGALGSSNSSFNNIDHLRQSSNLEQARGYTSSPLGAQRPKMSPSGSRPLH
TSRPLSAPVANRPLSPHLPLKKPQLSATFSISHRIFGAALGAAIISIPLATKFSLMFDV
>gnl|CDD|177738 PLN00127, PLN00127, succinate dehydrogenase (ubiquinone) cytochrome b subunit; Provisional
MQSLAASTSFSAQQFRFIGGTRVPEILGKPKDGSGTEFLGTPKNHRMLLEKRPLSPDVMDIDGKSTHYKF
PVVALSSITNRVTGCVLSGGAAGGGVLALVGGSEAVPATMEGFKSGGPLIVFPAKFAVSFPFVYHTLGGL
RHLVWDKTTEGLDNPSVEASSYGLFGASAALSAAAAVL
>gnl|CDD|177739 PLN00128, PLN00128, Succinate dehydrogenase [ubiquinone] flavoprotein subunit
MWRRCVARGLRLLASSSASSSLASASLRTALSRFFSTGGGRSSYTIVDHTYDAVVVGAGGAGLRAAIGLS
EHGFNTACITKLFPTRSHTVAAQGGINAALGNMTEDDWRWHMYDTVKGSDWLGDQDAIQYMCREAPKAVI
ELENYGLPFSRTEDGKIYQRAFGGQSLDFGKGGQAYRCACAADRTGHAMLHTLYGQAMKHNTQFFVEYFA
LDLIMDSDGACQGVIALNMEDGTLHRFRAHSTILATGGYGRAYFSATSAHTCTGDGNAMVARAGLPLQDL
EFVQFHPTGIYGAGCLITEGSRGEGGILRNSEGERFMERYAPTAKDLASRDVVSRSMTMEIREGRGVGPE
KDHIYLHLNHLPPEVLKERLPGISETAAIFAGVDVTKEPIPVLPTVHYNMGGIPTNYHGEVVTIKGDDPD
AVVPGLMAAGEAACASVHGANRLGANSLLDIVVFGRACANRVAEIAKPGEKQKPLPKDAGEKTIAWLDKL
RNANGSLPTSKIRLNMQRVMQNNAAVFRTQETLEEGCKLIDEAWDSFHDVKVTDRSLIWNSDLIETLELE
NLLINACITMHSAEARKESRGAHAREDFTKRDDENWMKHTLGYWEEGKVRLDYRPVHMNTLDDEVETFPP
KARVY
>gnl|CDD|215067 PLN00129, PLN00129, succinate dehydrogenase [ubiquinone] iron-sulfur subunit
MAAGLLRRLAGAKAGLLAPAAAASAAASAETKASSKGSKPSNLKEFQIYRWNPDNPGKPHLQSYKVDLND
CGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIK
DLVVDMTNFYQQYKSIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFL
GPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLGLG
>gnl|CDD|177741 PLN00130, PLN00130, succinate dehydrogenase (SDH3); Provisional
MAATALFRSIRRRDVVSAPLSVYKSLAGNAQPSWGSSYIGQNYASFSRAFGSKPVVNDILGTGLGTNNAI
REEREKSKSTEAAIVGAQLTRSFRALDVGTSKRLFSTISGDIKTTQEEPKIKSFRPLSPHLSVYQPQMNS
MLSIFNRISGVYLTGVTFAGYLLYLKMGMICLTYPSFYQVLYHTQQQLPVITSVTALAAIYHTIKSTHSL
LTH
>gnl|CDD|165700 PLN00131, PLN00131, hypothetical protein; Provisional
MHILRPLSPHLPIYKPQLTSAFPIFRRCFFFFMRKGGIVSLILVYMTPLLFNWGLTWGAPFFIFFAEWID
FLLSSMEGFPLSIGGGGSDAGPSRRPVLDLNSTPQPELDLNQPAAHEQEPEPAPPLDDQDLLTKRKRVSE
ELRLLLQIGAVKRKNKIADQLLDWMGLDNETDRTLLDDLYNHLYDLSEEQGRRVGQPQMFSSKGIKSLKL
WFLNRKER
>gnl|CDD|215068 PLN00133, PLN00133, class I-fumerate hydratase; Provisional
MVMLATLLRSVRSHGSALLPSLGTARAKSSAAPWRKASPAFDYQPLFDSNAKKTVPWRKLTGDHVSVVEA
AGEKYLKVAPEALTLLSDTAMRDVAHLLRPGHLQQLRNILDDPEASDNDRFVALELLKNANIAAGRVLPG
CQDTGTAIVMGKRGQRVLTDGEDEEHLSRGVYDAYTDTNLRYSQVAPLDMFEEKNTGTNLPAQIDLYAAK
GDEYHFQFIAKGGGSANKTFLYQQTKALLNEGSLEAFLEEKIKTIGTSACPPYHLAIVIGGLSAEQNLKT
VKLASTRYYDTLPTSGNALGRAFRDLEWEEKILKMTRGLGIGAQFGGKYFCHDVRVIRLPRHGASCPVGI
GVSCSADRQALGKITKDGVFLEALETDPSKYLPDVTEDSLSDDVVKVDLNRPMSEIRETLSAHPVRTRLS
LTGTLVVARDIAHAKLLERLEAGEGLPQYAKDHIIYYAGPAKTPEGYASGSFGPTTAGRMDSYVDRFMAA
GGSFVTLAKGNRSAQVTNACKKHGGFYLGSIGGPAAILAQNCIKKVEVLENPELGMEAVWKIEVEDFPAF
IVVDDKGNDFFKKWQG
>gnl|CDD|215069 PLN00134, PLN00134, fumarate hydratase; Provisional
MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAAD
EVAEGKLDDHFPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAM
HIAAATEIHSRLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCT
LPRLYELAQGGTAVGTGLNTKKGFDEKIAAAVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSL
MKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNHVAITVGGSAGHFEL
NVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLMLVTALNPKIGYDKAAAVAKKA
HKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGPSDLP
>gnl|CDD|177744 PLN00135, PLN00135, malate dehydrogenase
MIARGVMLGPDQPVILHMLDIPPAAEALNGVKMELIDAAFPLLKGVVATTDVVEACKGVNIAVMVGGFPR
KEGMERKDVMSKNVSIYKSQASALEKHAAPDCKVLVVANPANTNALILKEFAPSIPEKNITCLTRLDHNR
ALGQISERLGVPVSDVKNVIIWGNHSSTQYPDVNHATVKTPSGEKPVRELVADDAWLNGEFITTVQQRGA
AIIKARKLSSALSAASSACDHIRDWVLGTPEGTWVSMGVYSDGSYGVPPGLIYSFPVTCEKGEWSIVQGL
SIDEFSRKKMDATAKELKEEKELAYSCLS
>gnl|CDD|215070 PLN00136, PLN00136, silicon transporter; Provisional
MALASLPKVVLGSLAFGVFWMLAVFPSVPFLPIGRTAGALLSAVLMIVFHVISPDDAYASIDLPILGLLF
ATMVVGSYLKNAGMFKHLGRLLAWRSQGGRDLLCRVCVVTALASALFTNDTCCVVLTEFVLELAAERNLP
AKPFLLALASSANIGSSATPIGNPQNLVIAFNSKITFPKFLLGILPAMLAGMAVNMVMLLCMYWKDLDGG
AELSVDGKQMEAVEEGRSPASAKSTKQQSPALLQAGLNGDGNGDMSSMMSENISTKHPWFMQCTEHRRKL
FLKSFAYVVTVGMVVAYMVGLNMSWTAITTAIALVVVDFRDAEPCLDTVSYSLLVFFSGMFITVSGFNKT
GLPGAIWNFMAPYSKVNSVGGISVLSVIILLLSNLASNVPTVLLMGDEVAAAAALISPAAVTRSWLLLAW
VSTVAGNLSLLGSAANLIVCEQARRAPRNAYDLTFWQHIVFGVPSTLIVTAIGIPLIGKINI
>gnl|CDD|215071 PLN00137, PLN00137, NHAD transporter family protein; Provisional
AANQGLAMALVFGAGYAGIIFEESLAFNKSGVALLMAVSLWVIRAIGAPSLEIVTLELRHALAEVSEIVF
FLLGAMTIVEIVDAHQGFKLVTDSITTRSPRTLLWVVGFITFFLSSILDNLTTTIVMVSLLRKLVPPSEY
RKLLGAVVVVAANAGGAWTPIGDVTTTMLWIHGQISTLPTMQGLFLPSAVSLAVPLALMSLTSEENGSPQ
DSSPLLASEQMAPRGQLVFGVGVGALLFVPVFKALTGLPPYMGMLLGLGVLWILTDAIHYGESERQALKV
PQALSRIDTQGILFFLGILLSVGSLDAAGILRELANYLDANIPNVELIASAIGVASAIIDNVPLVAATMG
MYDLTDYPMDSELWQLIALCAGTGGSLLVIGSAAGVAFMGMEKVDFFWYLRKVSGFAFAGYVAGIAAYLA
VNGF
>gnl|CDD|165706 PLN00138, PLN00138, large subunit ribosomal protein LP2; Provisional
MKVVAAYLLAVLGGNTCPSAEDLKDILGSVGADADDDRIELLLSEVKGKDITELIASGREKLASVPSGGG
VAVAAAAAPAAGGAAAPAAEAKKEEKVEEKEESDDDMGFSLFD
>gnl|CDD|165707 PLN00139, PLN00139, hypothetical protein; Provisional
EISYKDFKVGKCEGQKVVDGETMPLVLQPPEPNKSDTESLVSALKQNKDWFEQMLIKNSAVLLRGFDVKN
AEDFNDIIEAFGWDDIRYVGPAPRTHVYKRIWTANEGPLSEFIYYHHEMVLIKESPKKVILFCEIPPPEG
GQTPFVPSFRVTERMLEEFPEAVEEVEAKGLKYTFTALSKNDTSSMRGRGWEDAFGTSDKAEAERRAKAL
GMDMEWLPNGGVKTILGPRSLTKVFDGRKGRRMWFNTVVGMHGKESSSAMLADGTEIPENFVKRCGQIIE
EESIQFKWEKGDVLFLDNLALLHGRRPSLPPRKVLVATCK
>gnl|CDD|165708 PLN00140, PLN00140, alcohol acetyltransferase family protein; Provisional
MEVSIISRELIKPSSPSIHHLKPFKLSLLDQLTPTTYIPMIFFYPTNNNQNFKGLQISIQLKRSLSETLS
TFYPFSGRVKDNLIIDNYEEGVPFFETRVKGSLSDFLKHPQLELLNKFLPCQPFSYESDPEAIPQVAIQV
NTFDCGGIALGLCFSHKIIDAATASAFLDSWAANTRGHYSEVINPDLFEASSFFPPLNSFPVQFLLLMEE
NWFFKENYITKRFVFDAKAIATLRAKAKSKRVPNPSRIETLSCFIWKCCTAASRSISAAPRPSISVHAVN
IRQRTKPPMSRYSIGNLFWWALAAADPADTKIELNELVSLTRESIANYNSDYLKSLQGENGLEGMSEYLN
QLVGIFSEEPEIFLFSSWLNFGLNDVDFGWGKPIWVGLLGEVGPAFRNLTVFKETGDNNGIEAWITLDEK
IMAILERDPEFLAFATPNPSISMP
>gnl|CDD|215072 PLN00141, PLN00141, Tic62-NAD(P)-related group II protein; Provisional
TMEGAEASEEDAENVKTKTVFVAGATGRTGKRIVEQLLAKGFAVKAGVRDVDKAKTSLPQDPSLQIVRAD
VTEGSDKLVEAIGDDSDAVICATGFRRSFDPFAPWKVDNFGTVNLVEACRKAGVTRFILVSSILVNGAAM
GQILNPAYIFLNLFGLTLVAKLQAEKYIRKSGINYTIVRPGGLTNDPPTGNIVMEPEDTLYEGSISRDQV
AEVAVEALLCPESSYKVVEIVARADAPKRSYKDLFASIKQK
>gnl|CDD|215073 PLN00142, PLN00142, sucrose synthase
AAAAPVLTRSHSIRERVPDALSQHRNELKALLSRYVAQGKGILQPHQLIDELEAVIDDDEERKKLLDGPF
GDILRSTQEAIVLPPFVALAVRPRPGVWEYVRVNVSELSVEELTVSEYLKFKEELVDGSWNDNFVLELDF
EPFNASFPRPTLSSSIGNGVQFLNRHLSSKLFRDKESLEPLLDFLRAHNHKGETLMLNDRIQTLSKLQSA
LRKAEEYLSKLPKDTPYSEFEHRFQELGLEKGWGDTAERVLETIHLLLDLLQAPDPSTLEKFLGRIPMVF
NVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENEMLLRIKQQGLDIKPQILIVTRLIPDAKGTTC
NQRLEKVSGTEHSHILRVPFRTEKGILRKWISRFDVWPYLETFAEDAASEILAELQGKPDLIIGNYSDGN
LVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFIITSTYQEIAGS
KDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQ
NDEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFIDPSKSKDREEIAEIKK
MHSLIEKYNLKGQFRWIAAQTNRVRNGELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCQGG
PAEIIVDGVSGFHIDPYHGDEAANKIADFFEKCKEDPSYWNKISDAGLQRIYECYTWKIYAERLLTLGGV
YGFWKYVSKLERRETRRYLEMFYNLKFRELAKTVPLAVDDPQPPK
>gnl|CDD|165711 PLN00143, PLN00143, tyrosine/nicotianamine aminotransferase; Provisional
EGIGNLKTEPPSYSIDDAVKFLKENFNEDDHRLAISFGFGDPSCFECFRTTNIAEDAIVEAVRSAKFNSY
APTGGILPARRAIADYLSNDLPYQLSPDDVYLTLGCKHAAEIIIKVLARPEANILLPRPGFPDVETYAIF
HHLEIRHFDLLPEKGWEVDLDAVEAIADENTIAMVIINPGNPCGSVYSYEHLNKIAETARKLGILVIADE
VYGHIVFGSKPFVPMGLFASIVPVITLGSISKRWMIPGWGLGWLVTCDPSGLLQICEIADSIKKALNPAP
FPPTFIQAAIPEILEKTTEDFFSKTINILRAALAFCYDKLKEIPCIMCPQKAEGAFFALVKLNLLLLEDI
EDDMEFCLKLAKEESLIILPGVTVGLKNWLRITFAVEQSSLEDGLGRLKSFCGRHAKKP
>gnl|CDD|177748 PLN00144, PLN00144, acetylornithine transaminase
FVSGKGCKLYDVEGKEYLDMAAGIAVNALGHGDPDWVKAVAEQAGTLAHVSNVYHTIPQVELAKRLVASS
FADRVFFCNSGTEANEAAIKFARKYQRVRAPDKKDPAASSATEFVSFSNSFHGRTLGALALTSKEQYRTP
FEPLMPGVTFVEYGNLEAARKLIQKGKTAAVFVEPVQGEGGIYPATKEFLQGLRALCDEAGALLVFDEVQ
CGLGRTGYLWAHEAYGVEPDIMTLAKPLAGGLPIGAVLVTEKVASAINPGDHGSTFAGGPLVCNAALAVL
DKISKPGFLASVAKKGEYLRELLRRKLGGNPHVKEVRGVGLLVGIQLDVPAGPLVDACRDSGLLVLTAGK
GDVVRLVPPLVISEAELEQAVEILADCLPALD
>gnl|CDD|215074 PLN00145, PLN00145, tyrosine/nicotianamine aminotransferase; Provisional
MEGGGGGGGGGHATARWRFERANAALAAAGALSIRAVLNRVKACVDAGGGPRPVLPLGHGDPSAFPCFRT
APEAEDAVAAALRSGKYNSYSTCVGLLPARRAIAEYLSRDLPYELSTDDIYLTAGCAQAIEIIMSVLAQP
GANILLPRPGYPLYEARAVFSGLEVRHFDLLPERGWEVDLEGVEALADENTVAMVIINPNNPCGSVYSYE
HLAKIAETARKLGILVIADEVYDHLTFGSKPFVPMGVFGEVAPVLTLGSISKRWVVPGWRLGWIATCDPN
GILKETKVVDSIRNYLNISTDPATFVQGAIPQIIANTKEEFFTKTLGLLKETADICYEKIKEIKCITCPH
KPEGSMFVMVKLDLSCLSGIKDDMDFCCKLAKEESVVVLPGSALGMKNWLRITFAIDPPSLEDGLERLKS
FCLRHAKLAN
>gnl|CDD|215075 PLN00146, PLN00146, 40S ribosomal protein S15a; Provisional
MVRRSVLNDALKTMYNAEKRGKRQVLIRPSSKVVIKFLKVMQKHGYIGEFEVVDDHRSGKIVVELNGRLN
KCGVISPRFDVKVKEIEAWTARLLPSRQFGYIVLTTSAGIMDHEEARRKNVGGKVLGFFY
>gnl|CDD|215076 PLN00147, PLN00147, light-harvesting complex I chlorophyll-a/b binding protein Lhca5; Provisional
AVSMAGGTTGGFLHQPRDSSSHCTRSISSVAASSGGINPVVAQERPTWLPGLDPPPHLDGTLAGDFGFDP
LGLGEDPESLKWYVQAELVHSRFAMAGVAGILFTDLLRVTGIRNLPVWYEAGAVKFEFASTRTLFVVQLL
LMGFAETKRYMDFVSPGSQAKEGSFFGLEAALEGLEPGYPGGPLFNPLGLAKDIENAHDWKLKEIKNGRL
AMVAMLGFFVQASVTHTGPIDNLLTHLSDPWHKTIIQTLSHS
>gnl|CDD|215077 PLN00148, PLN00148, potassium transporter; Provisional
MEAESGVSPSRNPSQLSWVNLSRNLLLAYQSFGVVYGDLSTSPLYVYKSTFSGKLQKHQNEETIFGAFSL
IFWTFTLIPLLKYVTILLSADDNGEGGTFALYSLLCRHAKLSLLPNQQAADEELSAYKYGPSTQTVGSSP
LKRFLEKHKRLRTALLLVVLFGACMVIGDGVLTPAISVLSSVSGLQVTETKLTDGELVLLACVILVGLFA
LQHCGTHRVAFMFAPIVIIWLLSIGSIGLYNIIHWNPKIIHALSPYYIIKFFRVTGKDGWISLGGILLSI
TGTEAMFADLGHFTAASIRLAFATVIYPCLVVQYMGQAAFLSKNIPSIPNSFYDSIPDPVFWPVFVIATL
AAIVGSQAVITATFSIVKQCHALGCFPRVKVVHTSKHIYGQIYIPEINWILMILTLAVTIGFRDTTLIGN
AYGLACMTVMFITTFLMALVIIFVWQKSIILAALFLLFFGFIEGVYLSAALMKVPQGGWVPLVLSAIFMS
IMYIWHYGTRKKYNFDLHNKVSLKWLLGLGPSLGIVRVPGIGLIYSELATGVPAIFSHFVTNLPAFHKVL
VFVCVKSVPVPYVSPEERFLIGRVCPRPYRMYRCIVRYGYKDIQRDDGDFENMLVQSIAEFIQMEAEEPQ
SSASESSSNDGRMAVISTRDVQSSSLLMVSEQELADIDDSIQSSKSLTLQSLQSAYEDENPGQSRRRRVR
FQLPENPGMDPSVREELMDLIEAKEAGVAYIMGHSYVKARRSSSFLKKLAIDIGYSFLRKNCRGPAVALN
IPHISLIEVGMIYYV
>gnl|CDD|177753 PLN00149, PLN00149, potassium transporter; Provisional
MDLEGGSPQNHVKKESWRTVLTLAYQSLGVVYGDLSTSPLYVYKSTFAEDIQHSETNEEIFGVLSFVFWT
LTLIPLLKYVFIVLRADDNGEGGTFALYSLLCRHARVNSLPNCQLADEELSEYKKDSGSSSMPLSGFGSS
LKSTLEKHRVLQRFLLVLALIGTCMVIGDGVLTPAISVFSAVSGLELSMSKEHHKYVEVPVACIILIGLF
ALQHYGTHRVGFLFAPVVLTWLLCISAIGVYNIFHWNPHVYQALSPYYMYKFLKKTQRGGWMSLGGILLC
ITGSEAMFADLGHFSQLSIKIAFTSLVYPSLILAYMGQAAYLSKHHVIESDYRIGFYVSVPEKLRWPVLV
IAILAAVVGSQAIITGTFSIIKQCSALGCFPKVKIVHTSSKIHGQIYIPEINWTLMLLCLAVTVGFRDTK
RLGNASGLAVITVMLVTTCLMSLVIVLCWHKSVLLAICFIFFFGTIEALYFSASLIKFLEGAWVPIALSF
IFLLVMYVWHYGTLKRYEFDVQNKVSINWLLSLGPSLGIVRVRGIGLIHTELVSGIPAIFSHFVTNLPAF
HQVLVFLCIKSVPVPHVRPEERFLVGRIGPKEYRLYRCIVRYGYRDVHKDDMEFEKDLVCSIAEFIRSEK
PEPNGAPENEEGEDERMTVVGTCSTHLEGIQLREDDSDKQEPAGTSELREIRSPPVSRPKKRVRFVVPES
PKIDRGAREELQELMEAREAGMAYILGHSYVRAKQGSSMMKKLVINYGYDFLRRNSRGPRYALSVPHAST
LEVGMVYHV
>gnl|CDD|215078 PLN00150, PLN00150, potassium ion transporter family protein; Provisional
MSTTMISESNQGRLWDLDQRITRPLGVDADSVRSMYFSSPNWPKVIMHLAYQSLGVVYGDLGTSPLYVFK
STFANVGVKNNDDIIGALSLIIYTLTIIPLIKYVFIVLRANDNGEGGSFALYSLLCRYCNISLLPNQHPT
DVELTTYVVDNMNRKTRIQRKLENSRVWQNVLLLIVLLGTCMVIGDGILTPSISVLSAVVGIKAASSGLD
TNLVTIISCVILVILFSLQRFGTHKVSFLFAPIFLCWFFSLALIGCYNIIKWDKSVFLAFNPLYIVSFFI
RNGRQGWESLGGIVLCMTGTEAMFADLGHFTVKSMQIAFTSLVYPCLLLTYLGQAAYLVKHMEDVNDPFY
RSLPKPIYWPIFVLATCSAMIASQAMISATFSIVKQAMALGCFPRVKIVHTSNKVHGQVYIPEINWILMV
LCLVITAGFRDTDEIGNAYGIAVVGVMIITTCLMTLVMIIIWRKHILLALLFFTVFAIIEGIYFSAVLFK
VTQGGWVPLVIAAVFGTVMYTWHYGTRKRYLYEMQHKVSVGWLLGLGPSLGLVRVPGIGLMYTDLAHGVP
PLFSHFITNLPAIHSTVVFVCIKYLPVNTVPQDERFLIRRIGPRAYSMYRCAARYGYTDLEKKDDNFEQL
LIASLERFIEIESFREQSDLESMAASWTPEELMGEGNSVGSGLFTQYDQSDINFATSQEWKRPSSQEDSV
SGHSSDTQDEVAFLNKCKEAGVVYILGNNDVKARKDSGFFKKVIINYIYTFLRRISRDSEVVLNIPHECL
LKVGMVYYV
>gnl|CDD|215079 PLN00151, PLN00151, potassium transporter; Provisional
MEEESSGGIGSSSNGSGGLVGTDSGESRWVDGSEDDSEDPASLDDDDDDRDSGGGMLEEEEDGNMRRRLI
RTPPRVDSFDVEAMEIPGAHRHDSEDLSVGRTLALAFQTLGVVFGDVGTSPLYTFSVMFSKVPIKSEEDV
LGALSLVLYTLILIPLAKYVLVVLWANDDGEGGTFALYSLICRHAKVSLLPNQLPSDERISSFRLKLPTP
ELERSLKIKERLETSSLLKKLLLLLVLAGTSMVIGDGVLTPAMSVMSAVSGLKVGVPGFGQDAVVMISVA
FLVILFSVQRFGTSKVGFAFGPALALWFCSLGGIGIYNLVKYDSSVFRAFNPVYIYYFFKRNSTKAWSAL
GGCVLCATGSEAMFADLGYFSVRSIQLAFTCLVLPCLLLAYMGQAAYLMKNPDSAEQIFFSSVPSSLFWP
VFLIANLAALIASRAMTTATFSCIKQSMALGCFPRLKIIHTSRKFMGQIYIPVINWFLLVMCLVVVCSFR
SITDIGNAYGIAEVGVMMVSTILVTLVMLLIWQTNIFLVLCFPVVFLSVELVFFSSVLSSVGDGGWIPLV
FASVFLCIMYIWNYGSKLKYQSEVRQKLSMDLMRELGSNLGTIRAPGIGLLYNELVKGIPAIFGHFLTTL
PAIHSTIIFVCIKYVPVPVVPQEERFLFRRVCPKDYHMFRCIARYGYKDVRKENHQAFEQLLIESLEKFI
RREAQERALESDGNDDTDDEDSVTSSRVLIAPNGSVYSLGVPLLADYRLTSKPIPEASTSEEVSPVLPSS
SMSSDEDQSLEYELSFIREAKESGVVYLLGHGDVRARKNSWFIKKLVINYFYAFLRKNCRRGIANLSVPH
SNIMQVGMTYMV
>gnl|CDD|177755 PLN00152, PLN00152, DNA-directed RNA polymerase; Provisional
DYNDMDMGYEDEPSEPEIEEGAEEDSESNNNDEVKGSIGENEDKEEQEPVQRPRKTTPYMTKYERARILG
TRALQISMNAPVMVELEGETDPLEIAMKELRERKIPFTIRRYLPDGSYEDWGVDELIVED
>gnl|CDD|165721 PLN00153, PLN00153, histone H2A; Provisional
MAGRGKGKTSGKKAVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYLTAEVLELAGNAA
RDNKKNRIVPRHIQLAIRNDEELGKLLGEVTIASGGVLPNIHAVLLPKKTKGGKGEETA
>gnl|CDD|177756 PLN00154, PLN00154, histone H2A; Provisional
MSGKGGKGLLAAKTTAAAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAIL
EYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKSTKK
>gnl|CDD|165723 PLN00155, PLN00155, histone H2A; Provisional
MAGRGKGKTSGKKAVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYL
>gnl|CDD|215080 PLN00156, PLN00156, histone H2AX; Provisional
GAGSGTTKGGRGKPKATKSVSRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLSAVLEYLAAEVLEL
AGNAARDNKKNRIVPRHIQLAVRNDEELSKLLGSVTIAAGGVLPNIHQTLLPKKVGKGKGDIGSASQEF
>gnl|CDD|177758 PLN00157, PLN00157, histone H2A; Provisional
MSGRGKRKGGGGGKKATSRSAKAGLQFPVGRIARYLKAGKYATRVGAGAPVYLAAVLEYLAAEVLELAGN
AARDNKKSRIVPRHIQLAVRNDEELSKLLGGVTIAAGGVLPNIHSVLLPKKSGKSKGEPKDP
>gnl|CDD|215081 PLN00158, PLN00158, histone H2B; Provisional
MAKTPSKKPAKKAAKGAKKKGSKSKTETYKIYIYKVLKQVHPDTGISSKAMSIMNSFINDIFEKIATEAG
KLARYNKKPTVTSREIQTAVRLILPGELAKHAVSEGTKAVTKFTSA
>gnl|CDD|165727 PLN00160, PLN00160, histone H3; Provisional
MRPGEKALKEIKMYQKSTDLLIRRLPFARLVREIQMEMSREAYRWQGSAILALQEAAEAHLVGLFEDSNL
CAIHGKRVTIMPKDMQLARRIRGQTRE
>gnl|CDD|215082 PLN00161, PLN00161, histone H3; Provisional
MARRLQGKRFRKGKKPQKEASGVTRQELDKKPHRYRPGTVALREIRKYQKSTELLIRKLPFARLVREISN
EMLREPFRWTAEALLALQEATEDFLVHLFEDCNLCAIHAKRVTIMPKDMQLARRIRGPIYGISSN
>gnl|CDD|215083 PLN00162, PLN00162, transport protein sec23; Provisional
MDFAELEAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCRTCRAVLNPYCRVD
FQAKIWICPFCFQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGGAPSPPVFVFVVDTCMIEEEL
GALKSALLQAIALLPENALVGLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPA
GGGIAGARDGLSSSGVNRFLLPASECEFTLNSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVP
GTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFAC
SLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNGTFEVNCSKDVKVQGAI
GPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSNPQPPGQQFFLQFLTRYQHSN
GQTRLRVTTVTRRWVEGSSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDY
RKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNG
PPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERF
PVPRLVVCDQHGSQARFLLAKLNPSATYNSANAMGGSDIIFTDDVSLQVFMEHLQRLAVQS
>gnl|CDD|165730 PLN00163, PLN00163, histone H4; Provisional
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRTVL
>gnl|CDD|215084 PLN00164, PLN00164, glucosyltransferase; Provisional
MAAPTVVLLPVWGSGHLMSMLEAGKRLLASSGGGALSLTVLVMPPPTPESASEVAAHVRREAASGLDIRF
HHLPAVEPPTDAAGVEEFISRYIQLHAPHVRAAIAGLSCPVAALVVDFFCTPLLDVARELAVPAYVYFTS
TAAMLALMLRLPALDEEVAVEFEEMEGAVDVPGLPPVPASSLPAPVMDKKSPNYAWFVYHGRRFMEAAGI
IVNTAAELEPGVLAAIADGRCTPGRPAPTVYPIGPVISLAFTPPAEQPPHECVRWLDAQPPASVVFLCFG
SMGFFDAPQVREIAAGLERSGHRFLWVLRGPPAAGSRHPTDADLDELLPEGFLERTKGRGLVWPTWAPQK
EILAHAAVGGFVTHCGWNSVLESLWHGVPMAPWPLYAEQHLNAFELVADMGVAVAMKVDRKRDNFVEAAE
LERAVRSLMGGGEEEGRKAREKAAEMKAACRKAVEEGGSSYAALQRLAREIRHGAVAPTR
>gnl|CDD|165732 PLN00165, PLN00165, hypothetical protein; Provisional
MSHMGKAWIVAASVGAVEALKDQGFCRWNYTLRSIHQHAKNNLRSFSQAKKLSSSSSAMVSSRVREEKAK
QSEESLRTVMYLSCWGPN
>gnl|CDD|165733 PLN00166, PLN00166, aquaporin TIP2; Provisional
MVKIEFGSLGDSFSVASLKAYLSEFIATLLFVFAGVGSAIAFAKLTSDAALDPAGLVAVAVAHAFALFVG
VSIAANISGGHLNPAVTLGLAIGGNITIITGFFYWIAQCLGSIVACLLLVFVTNGESVPTHGVAAGLGAI
EGVVMEIVVTFALVYTVYATAADPKKGSLGTIAPIAIGFIVGANILAAGPFSGGSMNPARSFGPAVVSGD
FSQIWIYWVGPLVGGALAGLIYGDVFIGSYAAAPTSEDYA
>gnl|CDD|215085 PLN00167, PLN00167, aquaporin TIP5; Provisional
MRKMAPTSLSARFQQSVTRNALRSYLAEFISTFFFVFAAVGSAMSSRKLMPDAASDPSSLLIVAIANAFA
LSSAVYIAANISGGHVNPAVTFGMAVGGHISVPTAMFYWISQMLASVMACLFLKVTTVGQHVPTYKIAEE
MTGFGASVLEGVLTFGLVYTVYAAGDPRRGLLGAIGPLAIGLVAGANVLAAGPFSGGSMNPACAFGSAVV
AGSFKNQAVYWVGPLLGGAVAGLLYDNVVFPTQDDRGSSTGDAVGV
>gnl|CDD|215086 PLN00168, PLN00168, Cytochrome P450; Provisional
MDATQLLLLAALLLLPLLLLLLGKHGGRGGKKGRRLPPGPPAVPLLGSLVWLTNSSADVEPLLRRLIARY
GPVVSLRVGSRLSVFVADRRLAHAALVERGAALADRPAVASSRLLGESDNTITRSSYGPVWRLLRRNLVA
ETLHPSRVRLFAPARAWVRRVLVDKLRREAEDAAAPRVVETFQYAMFCLLVLMCFGERLDEPAVRAIAAA
QRDWLLYVSKKMSVFAFFPAVTKHLFRGRLQKALALRRRQKELFVPLIDARREYKNHLGQGGEPPKKETT
FEHSYVDTLLDIRLPEDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAK
TGDDQEEVSEEDVHKMPYLKAVVLEGLRKHPPAHFVLPHKAAEDMEVGGYLIPKGATVNFMVAEMGRDER
EWERPMEFVPERFLAGGDGEGVDVTGSREIRMMPFGVGRRICAGLGIAMLHLEYFVANMVREFEWKEVPG
DEVDFAEKREFTTVMAKPLRARLVPRRTT
>gnl|CDD|177765 PLN00169, PLN00169, CETS family protein; Provisional
MSPRDRDPLVVGRVVGDVLDPFTRSISLRVTYGSREVNNGCELKPSQVVNQPRVDIGGEDLRTFYTLVMV
DPDAPSPSNPNLREYLHWLVTDIPATTGATFGQEVVCYESPRPTAGIHRFVFVLFRQLGRQTVYAPGWRQ
NFNTRDFAELYNLGSPVAAVYFNCQRESGSGGRRP
>gnl|CDD|215087 PLN00170, PLN00170, photosystem II light-harvesting-Chl-binding protein Lhcb6 (CP24); Provisional
SAAATSGAVLNGLGSSFLTGGKRSLALLVGTGAAKVGARTLLVVAAAAQPKKSWIPAVKGGGNLVDPEWL
DGSLPGDYGFDPLGLGKDPAFLKWYREAELIHGRWAMAAVVGIFVGQAWSGIPWFEAGADPGAIAPFSFG
SLLGTQLLLMGWVESKRWVDFFNPDSQSVEWATPWSRTAENFANATGLQGYPGGKFFDPLGLAGTVKDGV
YIPDFEKLERLKLAEIKHARLAMVAMLIFYFEAGQGKTPLGALGL
>gnl|CDD|215088 PLN00171, PLN00171, photosystem light-harvesting complex -chlorophyll a/b binding protein Lhcb7; Provisional
PAPSVSSSSSSFSGQHSLPRILASKPRRRRATRRPASSCRASWQELAGVLVFSAIPFTAVKAIANSSLGE
SLQRRLEETKKAAVEESSAFKAAAQKARNESFWYGEERPRWLGPIPYDYPDHLTGELPGDYGFDIAGLGK
DPVAFDKYFNFEILHARWAMLAALGVVIPEVLDLFGAVHFAEPVWWRVGYAKLQGDTLDYLGIPGLHIAG
SQGVIVIAICQALLMVGPEYARYCGIEALEPLGIYLPGDINYPGGALFDPLGLSKDPVAFEDLKVKEIKN
GRLAMVAWLGFYIQAAVTGKGPVQNLVDHLSDPLHNNLLSSLKL
>gnl|CDD|177768 PLN00172, PLN00172, ubiquitin conjugating enzyme; Provisional
MATKRIQKEHKDLLKDPPSNCSAGPSDENLFRWTASIIGPSDSPYAGGVFFLSILFPPDYPFKPPKVQFT
TKIYHPNINSNGSICLDILRDQWSPALTVSKVLLSISSLLTDPNPDDPLVPEIARVFKENRSRYEATARE
WTQRYAT
>gnl|CDD|177769 PLN00174, PLN00174, predicted protein; Provisional
MYNEPRTFIPNHILVSMGLVSTFMVIICLGYTYKLLQDLSTDTVNPVEVCDKVNQLKVPEYLAHLFLSIA
FVIRGWWIVGFLNFPFIFYNFAQWYEGKHQLDSAQIFNVLSRELRVIKAKSAFFIIIVIYTIWEWMIWVP
PDYVSAGEGYHVVKQIQVSH
>gnl|CDD|215089 PLN00175, PLN00175, aminotransferase family protein; Provisional
MAATSQKASTVGKDAASAQAAATASTQQPLQVAKRLEKFKTTIFTQMSSLAIKHGAINLGQGFPNFDGPD
FVKEAAIQAIRDGKNQYARGFGVPELNSAIAERFKKDTGLVVDPEKEVTVTSGCTEAIAATILGLINPGD
EVILFAPFYDSYEATLSMAGAKIKTVTLRPPDFAVPEDELKAAFTSKTRAILINTPHNPTGKMFTREELE
LIASLCKENDVLAFTDEVYDKLAFEGDHISMASLPGMYERTVTMNSLGKTFSLTGWKIGWAIAPPHLTWG
VRQAHSFLTFATATPMQWAAVAALRAPESYYEELKRDYSAKKDILVEGLKEVGFKVYPSSGTYFVMVDHT
PFGFENDIAFCEYLIEEVGVAAIPPSVFYLNPEDGKNLVRFAFCKDEETLRAAVERMKTKLKR
>gnl|CDD|215090 PLN00176, PLN00176, galactinol synthase
MAPELTVKKIAASPKALAKPAKRAYVTFLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRI
LVSQGCIVREIEPVYPPENQTQFAMAYYVINYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLPDGYF
YAVMDCFCEKTWSHTPQYKIGYCQQCPDKVTWPAELGPPPPLYFNAGMFVFEPSLSTYEDLLETLKITPP
TPFAEQDFLNMFFRDIYKPIPPVYNLVLAMLWRHPENVELDKVKVVHYCAAGSKPWRYTGKEENMDREDI
KMLVKKWWDIYNDESLDYKNFVPADEEEVKLQPFIAALSEAGVVSYVPAPSAA
>gnl|CDD|177772 PLN00177, PLN00177, sulfite oxidase; Provisional
MPGLRGPSDYSQEPPRHPSLKINAKEPFNAEPPRSALVSSYITPVDLFYKRNHGPIPIVDDIERYSVTIT
GLIENPRKLSMKDIRKLPKYNVTATLQCAGNRRTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVG
IPKLTSITSSGGKHVEFVSVDKCKEENGGPYKASIPLSQATNPEADVLLAYEMNGEVLNRDHGYPLRVVV
PGVIGARSVKWLDSINIIAEECQGFFMQKDYKMFPPSVNWDNINWSTRRPQMDFPVQSAICSLEDVNAIK
PGKVTVAGYALSGGGRGIERVDISVDGGKTWVEASRYQKPGVPYISDDISSDKWAWVLFEATVDVPQSTE
IVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRVGHSNM
>gnl|CDD|177773 PLN00178, PLN00178, sulfite reductase
ASKSSSAVSLLLARQSAATTAFSTGPSRSRSGRLVIRAVATPVKKPTTEPPKRSKVEIIKENSNFLRHPL
NEELATEAPNINEDAVQLIKFHGSYQQDNREKRGGKAYQFMLRTKQPAGKVPNRLYLVMDDLADEFGIGT
LRLTTRQTFQLHGVLKKDLKTVMSSIIKNMGSTLGACGDVNRNVLAPAAPFARKDYLFAQELAKNIAALL
APQSGAYYDIWVDGEKIMSAEPPEVTKARNDNSHGTNFEDSPEPIYGTQFLPRKFKIAVTVPGDNSVDIL
TNDIGVVVVSDEAGEPQGYNIYVGGGMGRTHRNETTFPRLADPLGYVPKEDILYAVKAIVATQRDYGRRD
DRKQSRMKYLVHSWGIEKFRSVVEQYYGKKFEPFRELPEWEFKSYLGWHEQGDGKLFYGVHVDNGRIKGE
AKKALREVIEKYNLPVRLTPNQNLILCDIRPAWKEPITAALAAAGLLEPEEVDPLNRTAMACPALPLCPL
AITEAERGIPDILKRVRAMFNKVGLKYDESVVVRMTGCPNGCARPYMAELGFVGDGPNSYQIWLGGTPNQ
TRLAEPFMDKVKVDDLEKVLEPLFYMWKQQRQEKESFGDFTNRVGFEALKEYIESYAGSVVAP
>gnl|CDD|215091 PLN00179, PLN00179, acyl- [acyl-carrier protein] desaturase
LKLNPLAAQPSPPPAARLRPRRSTRSSSSSVVAARVEAAKKPFAPPREVHVQVTHSMPPEKLEIFKSLEG
WAEENLLPLLKPVEKSWQPQDFLPDPASEGFYDQVKELRERAAELPDDYFVVLVGDMITEEALPTYQTML
NTLDGVRDETGASATPWARWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGMDPKTENNP
YLGFIYTSFQERATFISHGNTARLAKEHGDAKLAKICGTIAADEKRHETAYTRIVEKLFEIDPDGAVLAF
ADMMRKKITMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDYADILEHLVRRWKVEELTGLSGEGRRAQD
YVCGLPPRIRRLEERAQDRAKKAKPPSIPFSWIFDREVRL
>gnl|CDD|177775 PLN00180, PLN00180, NDF6 (NDH-dependent flow 6); Provisional
AITPFTKTKPHIPSSYAHSTKQDSGPCHGLLAQCSSGRFLSGWVNEKRSKNSKRGSLCKVNALPHDLPLM
AVMVEHVEGQRDYITHKSIWHLSDAAIKNVYTFYIMFTCWGCLFFGSMKDPFYDSEEYRGDGGDGTGHWV
YERQEDIEESARAELWREELIEEIEQKVGGLRELEEAVTK
>gnl|CDD|177776 PLN00181, PLN00181, protein SPA1-RELATED; Provisional
MKGSSESNSRGLNNTSGVSEFCTDGSKSLSHIDYVRSLLGSHKEGNLDGLDDDSIVRALECEDVSLRQWL
DNPDRSVDAFECFHVFRQIVEIVNAAHSQGIVVHNVRPSCFVMSSFNHVSFIESASCSDSGSDEDATTKS
REIGSSRREEILSERRIEKLEEVKKQPFPMKQILAMEMSWYTSPEEDNGSSSNCASDVYRLGVLLFELFC
PVSSREEKSRTMSSLRHRVLPPQILLNWPKEASFCLWLLHPEPSCRPSMSELLQSEFINEPRENLEEREA
AMELRDRIEEQELLLEFLFLIQQRKQEAADKLQDTISLLSSDIDQVVKRQLVLQQKGSDVRSFLASRKRI
RQGAETLAAEEENDDNSSKLDDTLESTLLESSRLMRNLKKLESVYFATRYRQIKAAAAAEKPLARYYSAL
SENGRSSEKSSMSNPAKPPDFYINDSRQGGWIDPFLEGLCKYLSFSKLRVKADLKQGDLLNSSNLVCAIG
FDRDGEFFATAGVNKKIKIFECESIIKDGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNFEGVVQVW
DVARSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFPSESG
RSLAFGSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMSISGINETP
LHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYHKAFPMPVLSYKFKTIDPVSGLEVDDASQFISSVC
WRGQSSTLVAANSTGNIKILEMV
>gnl|CDD|165748 PLN00182, PLN00182, putative aquaporin NIP4; Provisional
MTSHSDEIEEEQISRIEKGNGKDSQGGIETAICTSPSIVCLTQKLIAEMIGTYFIIFSGCGVVVVNVLYG
GTITFPGICVTWGLIVMVMIYSTGHISGAHFNPAVTVTFAIFRRFPWYQVPLYIGAQLTGSLLASLTLRL
MFNVTPEAFFGTTPTDSSGQALVAEIIISFLLMFVISGVATDSRAVGELAGIAVGMTIILNVFVAGPISG
ASMNPARSLGPAIVMGRYKGIWVYIVGPFVGIIAGGFVYNLIRFTDKPLRELTKSASFLRSVSQKHNASK
SKG
>gnl|CDD|215092 PLN00183, PLN00183, putative aquaporin NIP7; Provisional
MSSSARSRDVDQEAGSTASTLNGDDHPKRQRLFGCLPYDMDLNPARMVLAEMVGTFILMFCVCGIIASTQ
LSGGEVGLLEYAATAGLTVVVVVFSIGSISGAHVNPSVTIAFATFGHFPWSKVPLYITAQTVGSVLATYV
GVSVYGVKADLMTTKPAQGCSSAFWVEFIATFIVMFLAASLTSQPQSLGHLSGFVIGIAIGLAVLITGPV
SGGSMNPARSLGPAIVSWDFKDIWIYITAPTIGAVAGALMFHLLRLRTQPCSPNSSPNTSLLLH
>gnl|CDD|177778 PLN00184, PLN00184, aquaporin NIP1; Provisional
MADISGNGYGNAREGVVMVNLKEEVEHQQEMEAIHNPKPLKKQDSLLSVSVPFLQKLIAEVLGTYFLVFT
GCASVVVNMQNDNVVTLPGIAIVWGLTIMVLIYSLGHISGAHINPAVTIAFASCGRFPLKQVPAYVISQV
IGSTLAAATLRLLFGLDHDVCSGKHDVFIGSSPVGSDLQAFVMEFIVTFYLMFIISGVATDNRAIGELAG
LAIGSTVLLNVLIAAPVSSASMNPGRSLGPAMVYGCYKGIWIYIVAPTLGAIAGAWVYNTVRYTDKPLRE
ITKSGSFLKTVRIGSS
>gnl|CDD|177779 PLN00185, PLN00185, 60S ribosomal protein L4-1; Provisional
AAAAARPLVSVQSLDGDMATDKSATVALPDVMTAPIRPDIVNFVHTNISKNSRQPYAVSKKAGHQTSAES
WGTGRAVSRIPRVPGGGTHRAGQGAFGNMCRGGRMFAPTKTWRRWHRKVNVNQKRYAVVSALAASAVPSL
VMARGHKIENVPEVPLVVSDSAESIEKTSAAIKILKQIGAYADVEKAKDSKGIRAGKGKMRNRRYVSRKG
PLVVYGTEGAKIVKAFRNIPGVELCSVDRLNLLQLAPGGHLGRFVIWTKSAFEKLDSIYGTFEKPSEKKK
GYVLPRAKMVNADLARIINSDEVQSVVNPIKKDVKRAPLKKNPLKNLNAMLKLNPYAKTARRMALLAEAA
RVKAKKEKLAKKRKQVSKEEAAAIKAAGKAWYKTMISDSDYTEFDNFTKWLGVSQ
>gnl|CDD|215093 PLN00186, PLN00186, ribosomal protein S26; Provisional
MTKKRRNGGRNKHGRGHVKRIRCSNCGKCVPKDKAIKRFLVRNIVEQAALRDVQEACVYDGYTLPKLYAK
VQYCISCAIHSRVVRVRSRENRRIREPPPRFRRRKDDTP
>gnl|CDD|177781 PLN00187, PLN00187, photosystem II light-harvesting complex II protein Lhcb4; Provisional
TAAAAAASSFMGTRVPDVASNSGRIVARFGFGKKKKAAKKAKKKSSKVGADRPLWFPGAKAPEWLDGSLV
GDYGFDPFGLGKPAEYLQFDLDSLDQNLAKNLAGDVIGTRTEASEIKSTPFQPYSEVFGLQRFRECELIH
GRWAMLATLGALSVEALTGVTWQDAGKVELVDGSSYLGQPLPFSITTLIWIEVLVIGYIEFQRNAELDPE
KRLYPGGKFFDPLGLAADPEKKETLQLAEIKHARLAMVAFLGFAVQAAATGKGPLNNWATHLSDPLHTTI
IDTFSS
>gnl|CDD|215094 PLN00188, PLN00188, enhanced disease resistance protein (EDR2); Provisional
ASKVVYEGWMVRYGRRKIGRSYIHMRYFVLESRLLAYYKKKPQDNQVPIKTLLIDGNCRVEDRGLKTHHG
HMVYVLSVYNKKEKYHRITMAAFNIQEALIWKEKIESVIDQHQDSQVPNGNKYASFEYKSGMDNGRTASS
SDHESQFSAQEDEEDTHRDLLRRTTIGNGPPDSVLDWTKEFDSELSNQNSNNQAFSRKHWRLLQCQNGLR
IFEELLEVDYLPRSCSRAMKAVGVVEATCEEIFELVMSMDGTRFEWDCSFQYGSLVEEVDGHTAILYHRL
QLDWFPMFVWPRDLCYVRYWRRNDDGSYVVLFRSREHENCGPQPGFVRAHLESGGFNISPLKPRNGRPRT
QVQHLMQIDLKGWGVGYIPSFQQHCLLQMLNSVAGLREWFSQTDERGAPPRIPVMVNMASASVSSKKNQK
PQESSPSLDQTNAASRNSVMMDEDSDDDEEFQIPESEQEPETTKNETKDTAMEEEPQDKIDLSCFSGNLR
RDDRDKARDCWRISDGNNFKVRSKNFCYDKSKIPAGKHLMDLVAVDWFKDTKRMDHVARRKGCAAQVAAE
KGLFSFVVNLQVPGSTHYSMVFYFVTKELVPGSLLQRFVDGDDEFRNSRLKLIPSVPKGSWIVRQSVGST
PCLLGKAVDCNYIRGPKYLEIDVDIGSSTVANGVLGLVIGVITTLVVDMAFLVQANTYEELPERLIGAVR
VSHVELSSAIVPKLDPDTS
>gnl|CDD|177783 PLN00189, PLN00189, 40S ribosomal protein S9; Provisional
MVHVSFYRNYGKTFKKPRRPYEKERLDAELKLVGEYGLRNKRELWRVQYALSRIRNAARMLLTLDEKNPR
RIFEGEALLRRMNRYGLLDESQNKLDYVLALTVENFLERRLQTLVFKSGMAKSIHHARVLIRQRHIRVGK
QIVNVPSFMVRVDSQKHIDFSLTSPLGGGRPGRVKRKNQKAASGGGDGDEEDEE
>gnl|CDD|177784 PLN00190, PLN00190, 60S ribosomal protein L21; Provisional
MPAGHGLRSRTRDLFARPFRKKGYIPLTTYLRTFKVGDYVDIKVNGAIHKGMPHKFYHGRTGIVWNVTKR
AVGVEVNKQVGNRIIRKRIHVRVEHVQPSRCREEFLLRKKSNDEAKAEAKAKGEKISTKRQPKGPKPGFM
VEGATLETVTPIPYDVVN
>gnl|CDD|215095 PLN00191, PLN00191, enolase
VNAAVRAKTPDPVLFIANHLKKAVMATITKVKARQIIDSRGNPTVEVDLHTSKGMFRAAVPSGASTGIYE
ALELRDGDKDYLGKGVLKAVKNVNEIIAPALIGMDPTDQTQIDNFMLELDGTPNKGKLGANAILAVSLAV
CKAGAAEKGVPLYKHIADLAGNKKLVLPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFKEAMQMGSEV
YHHLKAVIKKKYGQDACNVGDEGGFAPNIQDNKEGLELLKEAIEKAGYTGKIKIGMDVAASEFYTKDKKY
DLDFKEENNDGSNKKSGDELIDLYKEFVSDYPIVSIEDPFDQDDWEHWAKLTSLEDVQIVGDDLLVTNPK
RVAKAIQEKACNALLLKVNQIGTVTESIEAVKMSKAAGWGVMTSHRSGETEDSFIADLAVGLATGQIKTG
APCRSERLAKYNQLLRIEEELGDEAVYAGENFRKPVW
>gnl|CDD|215096 PLN00192, PLN00192, aldehyde oxidase
SSNMSLVFAVNGERFELSSVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVLLSKYDPVLDQVEDFTV
SSCLTLLCSVNGCSITTSEGLGNSKDGFHPIHKRFAGFHASQCGFCTPGMCISLFSALVNADKTDRPEPP
SGFSKLTVVEAEKAVSGNLCRCTGYRPIVDACKSFAADVDIEDLGLNSFWKKGESEEAKLSKLPPYNHSD
HICTFPEFLKKEIKSSLLLDSSRYRWYTPVSVEELQSLLESNNFDGVSVKLVVGNTGTGYYKDEELYDKY
IDIRHIPELSMIRRDEKGIEIGAVVTISKAIEALREESKSEYVFKKIADHMEKIASRFVRNTGSIGGNLV
MAQRKQFPSDIATILLAAGSTVNIQNASKREKLTLEEFLERPPLDSKSLLLSVEIPSWTSSSGSDTKLLF
ETYRAAPRPLGNALPYLNAAFLAEVSQDASSGGIVVNDCRLAFGAYGTKHAIRARKVEEFLTGKVLSDSV
LYEAVRLLKGIVVPEDGTSHPEYRSSLAVGFLFDFLSPLIESNAKSSNGWLDGGSNTKQNPDQHDDVKKP
TLLLSSKQQVEENNEYHPVGEPIKKVGAALQASGEAVYVDDIPSPKNCLYGAFIYSTKPLARVKGIKFKS
NLVPQGVLAVITFKDIPKGGQNIGSKTIFGPEPLFADEVTRCAGQRIALVVADTQKHADMAANLAVVEYD
TENLEPPILTVEDAVKRSSLFEVPPFLYPKPVGDISKGMAEADHKILSAEIKLGSQYYFYMETQTALALP
DEDNCIVVYSSTQCPEYVHSVIARCLGIPEHNVRVITRRVGGGFGGKAVKSMPVATACALAAFKLQRPVR
MYLNRKTDMIMAGGRHPMKITYSVGFKSDGKITALHLDILINAGISPDISPIMPRNIIGALKKYDWGALS
FDIKVCKTNLSSRSAMRAPGEVQGSYIAEAIIEHVASTLSMDVDSVRKINLHTYESLKLFYGDSAGEPSE
YTLPSIWDKLASSSEFKQRTEMVKEFNRSNKWKKRGISRVPIVHEVMLRPTPGKVSILSDGSIAVEVGGI
EIGQGLWTKVKQMAAFGLGMIKCDGGEDLLDKIRVIQSDTLSMIQGGFTAGSTTSESSCEAVRLCCVILV
ERLKPIKERLQEQMGSVTWDMLISQAYMQSVNLSASSYYTPDPSSMEYLNYGAAVSEVEVDLLTGETTIL
RSDIIYDCGQSLNPAVDLGQIEGAFVQGIGFFMLEEYTTNSDGLVVTDGTWTYKIPTVDTIPKQFNVEIL
NSGHHKKRVLSSKASGEPPLLLAASVHCATRAAIREARKQLLSWGGIDGSDSTFQLPVPATMPVVKELCG
LDVVERYLEWKIAS
>gnl|CDD|215097 PLN00193, PLN00193, expansin-A; Provisional
MSKSLLGLAILLQFCCYLFINVNAFTPSGWTKAHATFYGGSDASGTMGGACGYGNLYSTGYGTRTAALST
ALFNDGASCGQCYRIMCDYQADSRWCIKGASVTITATNFCPPNYALPNNNGGWCNPPLQHFDMAQPAWEK
IGIYRGGIVPVLFQRVPCKKHGGVRFTINGRDYFELVLISNVGGAGSIQSVSIKGSKTGWMAMSRNWGAN
WQSNAYLDGQSLSFKVTTTDGQTRFFLNVVPANWGFGQTFSSSVQF
>gnl|CDD|215098 PLN00194, PLN00194, aldose 1-epimerase; Provisional
MASAAEEKPGIYELKNGNISVKLTNYGATITSLILPDKNGKLADVVLGFDSVEPYKNDSPYFGAIVGRVA
NRIKGAKFTLNGVTYKLPPNNGPNSLHGGPKGFSKVVWEVAKYKKGEKPSITFKYHSFDGEEGFPGDLSV
TVTYTLLSSNTLRLDMEAKPLNKATPVNLAQHTYWNLAGHNSGDILSHKIQIFGSHITPVDENLIPTGEI
LPVKGTPFDFTTPKKIGSRINELPKGYDHNYVLDGEEKEGLKKAAKVKDPKSGRVLELWTNAPGMQFYTS
NYVNGVKGKGGAVYGKHAGLCLETQGFPDAVNQPNFPSVVVNPGEKYKHTMLFEFSA
>gnl|CDD|165762 PLN00196, PLN00196, alpha-amylase; Provisional
MANRRLSMILLLVLLGLSSNLAAGQVLFQGFNWESWKQNGGWYNFLMGKVDDIAAAGITHVWLPPPSHSV
SEQGYMPGRLYDLDASKYGNEAQLKSLIEAFHGKGVQVIADIVINHRTAEHKDGRGIYCLFEGGTPDSRL
DWGPHMICRDDTQYSDGTGNLDTGADFAAAPDIDHLNKRVQRELIGWLLWLKSDIGFDAWRLDFAKGYSA
EVAKVYIDGTEPSFAVAEIWTSMAYGGDGKPEYDQNAHRQELVNWVDRVGGAASPATVFDFTTKGILNVA
VEGELWRLRGADGKAPGVIGWWPAKAVTFVDNHDTGSTQHMWPFPSDKVMQGYAYILTHPGNPCIFYDHF
FDWGLKEEIAALVSIRNRNGITPTSELRIMEADADLYLAEIDGKVIVKIGSRYDVSHLIPEGFQVVAHGN
GYAVWEKI
>gnl|CDD|215099 PLN00197, PLN00197, beta-amylase; Provisional
MAMNITHQIGALAGTPIKSGEITSTSTLSAKPPSPRMRCPKAMARNYEQKSQPTSPCMSPILGGMRADLS
VACRAFATENDVVTIEEQREEREYRIGGTKEKGKGVPVYVMMPLDSVTMGNTVNRRKAMKASLQALKSAG
VEGIMMDVWWGLVERESPGVYNWGGYNELLEMAKRHGLKVQAVMSFHQCGGNVGDSCTIPLPKWVVEEVD
KDPDLAYTDQWGRRNYEYVSLGCDTLPVLKGRTPVQCYADFMRAFRDNFKHLLGDTIVEIQVGMGPAGEL
RYPSYPEQNGTWKFPGIGAFQCYDKYMLSSLKAAAEAAGKPEWGSTGPTDAGHYNNWPEDTRFFKKEGGG
WNSPYGEFFLSWYSQMLLDHGERILSSAKSIFENTGVKISVKIAGIHWHYGTRSHAPELTAGYYNTRFRD
GYLPIAQMLARHGAIFNFTCIEMRDHEQPQDALCAPEKLVRQVALATREAEVPLAGENALPRYDDYAHEQ
ILQASSLNIDGNSEDREMCAFTYLRMNPHLFQPDNWRRFVAFVKKMKEGKDSHRCREQVEREAEHFVHVT
RPLVQEAAVALMH
>gnl|CDD|215100 PLN00198, PLN00198, anthocyanidin reductase; Provisional
MATLTPTGKKTACVIGGTGFLASLLIKLLLQKGYAVNTTVRDPENQKKIAHLRALQELGDLKIFGADLTD
EESFEAPIAGCDLVFHVATPVNFASEDPENDMIKPAIQGVHNVLKACAKAKSVKRVILTSSAAAVSINKL
SGTGLVMNEKNWTDVEFLTSEKPPTWGYPASKTLAEKAAWKFAEENNIDLITVIPTLMAGPSLTSDIPSS
LSLAMSLITGNEFLINGLKGMQMLSGSISITHVEDVCRAHIFLAEKESASGRYICCAANTSVPELAKFLI
KRYPQYQVPTDFGDFPSKAKLIISSEKLISEGFSFEYGIEEIYDQTVEYFKAKGLLKA
>gnl|CDD|177791 PLN00200, PLN00200, argininosuccinate synthase; Provisional
LRGKLNKVVLAYSGGLDTSVILKWLRENYGCEVVCFTADVGQGIEELEGLEAKAKASGAKQLVVKDLREE
FVRDYIFPCLRANAIYEGKYLLGTSMARPLIAKAMVDIAKEVGADAVAHGATGKGNDQVRFELTFFALNP
ELKVVAPWREWDIKGREDLIEYAKKHNIPVPVTKKSIYSRDRNLWHISYEGDILEDPANEPKEDMFMMSV
SPEAAPDQPEYIEIEFEKGLPVAINGKTLSPATLLTKLNEIGGKHGIGRIDMVENRFVGMKSRGVYETPG
GTILFAAHRELESLTLDRETMQVKDSLALKYAELVYNGFWFDPERESMDAFMEKITETTTGSVRLKLYKG
NVSVAGRKSPYSLYRQDISSFEEGGGIYNQADAAGFIRLYALRLRTRAMLRKKI
>gnl|CDD|177792 PLN00202, PLN00202, beta-ureidopropionase
MNSEEASTSADGSICGYESLHRLLSANLPPELFQEVSRLLLGLNCGRPVEMIALPEAAKALSKAHDFDLQ
AFRFTADKEQLRAPRVVRVGLIQNSIALPTTAPFADQKRAIMDKVKPMIDAAGAAGVNILCLQEAWTMPF
AFCTREKRWCEFAEPVDGESTKFLQELARKYNMVIVSPILERDVNHGETLWNTAVVIGNNGNIIGKHRKN
HIPRVGDFNESTYYMEGNTGHPVFETAFGKIAVNICYGRHHPLNWLAFGLNGAEIVFNPSATVGDLSEPM
WPIEARNAAIANSYFVGSINRVGTEVFPNPFTSGDGKPQHKDFGHFYGSSHFSAPDASCTPSLSRYKDGL
LISDMDLNLCRQLKDKWGFRMTARYEMYADFFAEYLKPDFKPQVISDPLLHKKSL
>gnl|CDD|215101 PLN00203, PLN00203, glutamyl-tRNA reductase
MAVSAAAALAPAAETSSAPPSSSSSSSSATRRGLKSNVTLPSVVGSAAGLATAVDSASSKAASASALEQL
KNSAADRYTKEKSSIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCSLNHIEEAAVLSTCNRMEIYVV
ALSWHRGVKEVTEWMSKTSGIPVSELRQHLFLLYDKDATQHLFEVSGGLDSLVLGEGQILAQVKQVVKVG
QGVDGFGRNLSGLFKHAITAGKRVRTETNIASGAVSVSSAAVELALMKLPESSHASARVLVIGAGKMGKL
LVKHLVSKGCTKMVVVNRSEERVAALREEFPDVEIIYKPLDEMLACAAEADVVFTSTSSETPLFLKEHVE
ALPPASDTVGGKRLFVDISVPRNVGACVSELESARVYNVDDLKEVVAANKEDRLRKAMEAQTIIREESKN
FEAWRDSLETVPTIKKLRSYAERIRAAELEKCLSKMGDDLTKKQRKAVEDLSRGIVNKLLHGPMQHLRCD
GSDSRTVSETLENMHALNRMFDLETEIAG
>gnl|CDD|215102 PLN00204, PLN00204, CP12 gene family protein; Provisional
MATIAGLNLSTPRVLARATDRPKAQGPVKLNNPWKRGSRLGSGRMQVRPVRAAPEGISEKVEKSIKEAEE
TCADDPASGECVAAWDEVEELSAAASHARDKKKGSDPLEEYCKDNPETDECRTYED
>gnl|CDD|177795 PLN00205, PLN00205, ribisomal protein L13 family protein; Provisional
KKALAGLRRINLEGLRWRVFDAKGQVLGRLASQISTVLQGKDKPTYAPNRDDGDICIVLNAKDISVTGRK
LTDKFYRWHTGYIGHLKERSLKDQMAKDPTEVIRKAVLRMLPRNRLRDDRDRKLRIFAGSEHPFGDKPLE
PFVMPPRQVREMRPRARRAMIRAQKKAEQREQAANEKRKGKKKEVEVEVTA
>gnl|CDD|215103 PLN00206, PLN00206, DEAD-box ATP-dependent RNA helicase; Provisional
MNEEGCNPHEDDVVKERSIEQREALPGEPKCVVCGRYGEYICDETDDDICSLECKQALLRRVAKSRVAVG
APKPKRLPATDECFYVRDPGSTSGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAG
YEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEQRNPLAMVLTPTRELCV
QVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD
CMLERGFRDQVMQIFQALSQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETK
QKKQKLFDILKSKQHFKPPAVVFVSSRLGADLLANAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVP
VIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSS
GAAIPRELANSRYLGSGRKRKKKRRYGS
>gnl|CDD|215104 PLN00207, PLN00207, polyribonucleotide nucleotidyltransferase; Provisional
MLANPSALHHLLRSPLPPSRNLPRFHDSESSPSISSSLPEAGLLKSSIKKARSVRALLRPVDSEDTSSVG
EGPGPFPQQFSVKIPVGDRHILVETGHIGRQASGSVTVTDGETIVYTSVCLADVPSEPSDFFPLSVHYQE
RFSAAGRTSGGFFKREGRTKDHEVLICRLIDRPLRPTMPKGFYHETQILSWVLSYDGLHSPDSLAVTAAG
IAVALSEVPNLKAIAGVRVGLIGGKFIVNPTTKEMEESELDLIMAGTDSAILMIEGYCNFLPEEKLLEAV
EVGQDAVRAICKEIEVLVKKCGKPKMLDAIKLPPPELYKHVKEIAGDELVKALQIRGKIPRRKALSSLEE
KVLSILTEEGYVSKDESFGTSETRADLLEDEDEDEEVVVDGEVDEGDVHIKPIPRKSSPLLFSEVDVKLV
FKEVTSKFLRRRIVEGGKRSDGRTPDEIRPINSSCGLLPRAHGSALFTRGETQALAVVTLGDKQMAQRID
NLVDADEVKRFYLQYSFPPSCVGEVGRIGAPSRREIGHGMLAERALEPILPSEDDFPYTIRVESTITESN
GSSSMASVCGGCLALQDAGVPVKCPIAGIAMGMVLDTEEFGGDGSPLILSDITGSEDASGDMDFKVAGNE
DGITAFQMDIKVGGITLPIMERALLQAKDGRKHILAEMSKCSPPPSKRLSKYAPLIHIMKVKPEKVNMII
GSGGKKVKSIIEETGVEAIDTQDDGTVKITAKDLSSLEKSKAIISSLTMVPTVGDIYRNCEIKSIAPYGA
FVEIAPGREGLCHISELSSNWLAKPEDAFKVGDRIDVKLIEVNDKGQLRLSRRALLPEANSEKSSQKQQG
GSTKDKAPQKKYVNTSSRPRRAAQAEKNSAENAAVPKKKDYKRATSGSKDE
>gnl|CDD|177798 PLN00208, PLN00208, translation initiation factor (eIF); Provisional
MPKNKGKGGKNRKRGKNEADDEKRELIFKEDGQEYAQVLRMLGNGRCEALCIDGTKRLCHIRGKMRKKVW
IAAGDIILVGLRDYQDDKADVILKYMPDEARLLKAYGELPENTRLNEGIAGDLDEEEDGEGDDYIEFEDE
DIDKI
>gnl|CDD|165774 PLN00209, PLN00209, ribosomal protein S27; Provisional
MVLQNDIDLLNPPAELEKRKHKLKRLVQSPNSFFMDVKCQGCFNITTVFSHSQTVVVCGSCQTVLCQPTG
GKARLTEGCSFRKKGD
>gnl|CDD|177799 PLN00210, PLN00210, 40S ribosomal protein S16; Provisional
ATESVQCFGRKKTAVAVTYCKRGRGLIKINGCPIELVQPEILRFKAFEPILLLGRHRFAGVDMRIRVKGG
GHTSQIYAIRQSIAKALVAYYQKYVDEQSKKEIKDILLRYDRTLLVADPRRCEPKKFGGRGARARFQKSY
R
>gnl|CDD|215106 PLN00212, PLN00212, glutelin; Provisional
ASSAFSRLSICFCVLLLCHGSMAQLFSQSTNPWQSPRQGSFRECRFDRLQAFEPLRKVRSEAGVTEYFDE
KNEQFQCTGVFVIRRVIEPQGLLLPRYSNTPGLVYIIQGRGSMGLTFPGCPATYQQQFQQFLTEGQSQSQ
KFRDEHQKIHQFRQGDVVALPAGVAHWFYNDGDAPVVALYVYDINNNANQLEPRQREFLLAGNNNRQQQV
YGRSIEQHSGQNIFSGFSTELLSEALGINAQVAKRLQSQNDQRGEIIRVKNGLQLLQPTLTQQQEQAQQQ
QQRLYQQVQYQQSQQTSGRWNGLDENFCTIKVRLNIENPSRADTYNPRAGRITRLNSQKFPILNLIQMSA
TRVNLYQNALLSPFWNVNAHSVVYITQGRARVQVVSNNGKTVFNGVLRPGQLLIIPQHYAVLKKAEREGC
QYIAFKTNANAMVSHIAGKNSIFRALPVDVIANAYRISREEARRLKNNRGDELGAFTPRFQQQSYQGFSN
ESE
>gnl|CDD|165778 PLN00213, PLN00213, predicted protein; Provisional
MSIKNVFLLLAVLCIIVSVNAQLPQFPAQLPFLFPFQLIPGLPDITKCFSSVMDIPGCIAEISQSIFTGK
FGNLGPACCKAFLDADNCIPKIPFIPFFPPMLKEQCSRVAGATPPIPK
>gnl|CDD|177800 PLN00214, PLN00214, putative protein; Provisional
MSKFSSQITTLFIVVALVCAFVPVFSVEEAEAKSLWNTCLVKITPKCALDIIAVVFENGTLIDPCCNDLV
KEGKVCHDTLIKYIADKPMLIAHETEYLKKSDDLWNHCVSISKSA
>gnl|CDD|165780 PLN00215, PLN00215, predicted protein; Provisional
MKNIKGGKTRAGKPKKNDLTTRYTRPAPIDEPNRGKGCTMHLSLPPPMSKRRSAAKMIPGQGGQWVLRRG
TSRDCKPDLPMATSSCAPISKTERLWPRRWAWDTRFLNTS
>gnl|CDD|165781 PLN00216, PLN00216, predicted protein; Provisional
MIPAAAKKIPPLEKRPPHQPLPARTNPGKKKERWRSFRTPQGRNRTGANTRITRPSQKIKARSRTPGSL
>gnl|CDD|165782 PLN00217, PLN00217, predicted protein; Provisional
MVRIFKRREMGWNVQPTSRGSTGHLLRRILKTRHGQLNNYRIQHPIRPGSPCAERIVSNRCRERTPLTKL
VATTRLQGITSTPREWYPWSQRLLSPRSSYKEEARGEEDNMPRRPPCSPLNWTLRPEESDYSNTHTDSNR
TRAANLREGHQKGSSDGKPSRPKTLSFSHNIQQKRTRIRHLTSPLQRLEKGGTSSSRTHTLFPIVKPLGV
>gnl|CDD|165783 PLN00218, PLN00218, predicted protein; Provisional
MRRERVCSYFPYFRYFFLFFFFFFWRESSLVFLFFFFLAFHEEVLVCFDVFIWRLFPPLGSISLILNVLL
PALGFCGFQRGGSSWVVERCVISFFFLILSLRGRWSLDRKMCKRKACPSLRGERRDSSSSLSRPWVGCSI
HLSISLRHPMV
>gnl|CDD|165784 PLN00219, PLN00219, predicted protein; Provisional
MTDRHPSCHPYSPVFNFYQEKKEMFTHSSAKQVTRMPDSKERSKTHLSQHPEESLDQFTITKGQN
>gnl|CDD|215107 PLN00220, PLN00220, tubulin beta chain; Provisional
MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEP
GTMDSVRSGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLG
GGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDI
CFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQ
YRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIPNNVK
SSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEEGEYEDEEEEEEYEE
>gnl|CDD|177802 PLN00221, PLN00221, tubulin alpha chain; Provisional
MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDL
EPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNA
VGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIY
DICRRSLDIERPTYTNLNRLISQVISSLTASLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPVISAEK
AYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTG
FKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDLAALEKDYEEVGAESAEGEGDEGEEY
>gnl|CDD|215108 PLN00222, PLN00222, tubulin gamma chain; Provisional
MPREIITLQVGQCGNQIGMEFWKQLCLEHGISKDGILEDFATQGGDRKDVFFYQADDEHYIPRALLIDLE
PRVINGIQNSEYRNLYNHENIFVSDHGGGAGNNWASGYHQGEQVEEDIMDMIDREADGSDSLEGFVLCHS
IAGGTGSGMGSYLLEALNDRYSKKLVQTYSVFPNQMETSDVVVQPYNSLLTLKRLTLNADCVVVLDNTAL
NRIAVDRLHLENPTFAQTNSLVSTVMSASTTTLRYPGYMNNDLVGLLASLIPTPRCHFLMTGYTPLTVER
QANVIRKTTVLDVMRRLLQTKNIMVSSYARTKEASQAKYISILNIIQGEVDPTQVHKSLQRIRERKLANF
IEWGPASIQVALSRKSPYVQTAHRVSGLMLANHTSIRHLFSKCLSQYDKLRKKQAFLDNYRKFPMFADND
LSEFDESREIVESLVDEYKACESPDYIKWGMEDP
>gnl|CDD|165788 PLN00223, PLN00223, ADP-ribosylation factor; Provisional
MGLSFTKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGG
QDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEIT
DKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSNNIANKA
>gnl|CDD|215109 PLN00410, PLN00410, U5 snRNP protein, DIM1 family; Provisional
MSYLLPHLHSGWAVDQAILAEEERLVVIRFGHDWDETCMQMDEVLASVAETIKNFAVIYLVDITEVPDFN
TMYELYDPCTVMFFFRNKHIMIDLGTGNNNKINWALKDKQEFIDIVETVYRGARKGRGLVISPKDYSTKY
RY
>gnl|CDD|177805 PLN00411, PLN00411, nodulin MtN21 family protein; Provisional
MAGTVSLWRREAVFLTAMLATETSVVGISTLFKVATSKGLNIYPFLGYSYLLASLLLLPSLFFTNRSRSL
PPLSVSILSKIGLLGFLGSMYVITGYIGIEYSNPTLASAISNITPALTFILAIIFRMEKVSFKERSSVAK
VMGTILSLIGALVVIFYHGPRVFVASSPPYLNFRQLSPPLSSSNSDWLIGGALLTIQGIFVSVSFILQAH
IMSEYPAAFTVSFLYTVCVSIVTSMIGLVVEKNNPSVWIIHFDITLITIVTMAIITSVYYVIHSWTVRHK
GPLYLAIFKPLSILIAVVMGAIFLNDSLYLGCLIGGILITLGFYAVMWGKANEEKDQLLSFSGKEKTPLL
LNGKNDQI
>gnl|CDD|215110 PLN00412, PLN00412, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
MAGTGFFAEILDGDVYKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWA
KTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEGKFLVS
DSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHL
AGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDTGIAISKKAGMVPLQMELGGKDACIVLEDADLD
LAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEG
LVMDAKEKGATFCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQ
GCVFTRDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKSTVINLPK
PSYTMG
>gnl|CDD|165792 PLN00413, PLN00413, triacylglycerol lipase
MSQPKNYFVLDPREATVSDLIHLLFSSDLEDRKFIDSSEENIEDDLCEFRGRWIIFVSIVIQKLIIIFKK
PLSFLGFALACWLNLLSSNGGFFKIFLNLFKGNFIWPEKASATFASINGNLDQKVELGLGPKIEIGDERY
KALLSIMASKLAYENEHFIRSVLHDHWKMDLLGFYSCPNDFDKQRSTEVIVIKDTKDDPNLIIVSFRGTD
PFDADDWCTDLDLSWHEVKNVGKIHGGFMKALGLPKEGWPEEINLDETQNATSLLAYYTILRHLKEIFDQ
NPTSKFILSGHSLGGALAILFTAVLIMHDEEEMLERLEGVYTFGQPRVGDEDFGIFMKDKLKEFDVKYER
YVYCNDMVPRLPFDDKTLMFKHFGACLYCDSFYKGKVEEEEPNKNYFNIFWVIPKIINALWELIRSFIIP
CWKGGEFREGWFLRCFRLVALLIPGLPAHFPNEYINVALLGNFPPQVPDSQDLPDDDLD
>gnl|CDD|177807 PLN00414, PLN00414, glycosyltransferase family protein
MGSKFHAFMYPWFGFGHMIPYLHLANKLAEKGHRVTFFLPKKAHKQLQPLNLFPDSIVFEPLTLPPVDGL
PFGAETASDLPNSTKKPIFDAMDLLRDQIEAKVRALKPDLIFFDFVHWVPEMAKEFGIKSVNYQIISAAC
VAMVLAPRAELGFPPPDYPLSKVALRGHDANVCSLFANSHELFGLITKGLKNCDVVSIRTCVELEGNLCD
FIERQCQRKVLLTGPMLPEPQNKSGKPLEDRWNHWLNGFEPGSVVFCAFGTQFFFEKDQFQEFCLGMELT
GLPFLIAVMPPKGSSTVQEALPEGFEERVKGRGIVWEGWVEQPLILSHPSVGCFVNHCGFGSMWESLVSD
CQIVFIPQLADQVLITRLLTEELEVSVKVQREDSGWFSKESLRDTVKSVMDKDSEIGNLVKRNHKKLKET
LVSPGLLSGYADKFVEALENEVNNTK
>gnl|CDD|177808 PLN00415, PLN00415, 3-ketoacyl-CoA synthase
MFIAMADFKLLLLILILLSLFELDLLHFHHDFFSPFPVKIGLLLISIFFYAYSTTRSKPVYLVDFSCHQP
TDSCKISSETFFNMAKGAQLYTEETIQFMTRILNRSGLGDDTYSPRCMLTSPPTPSMYEARHESELVIFG
ALNSLFKKTGIEPREVGIFIVNCSLFNPNPSLSSMIVNRYKLKTDVKTYNLSGMGCSAGAISVDLATNLL
KANPNTYAVIVSTENMTLSMYRGNDRSMLVPNCLFRVGGAAVMLSNRSQDRVRSKYELTHIVRTHKGSSD
KHYTCAEQKEDSKGIVGVALSKELTVVAGDTLKTNLTALGPLVLPLSEKLRFILFLVKSKLFRLKVSPYV
PDFKLCFKHFCIHAGGRALLDAVEKGLGLSEFDLEPSRMTLHRFGNTSSSSLWYELAYVEAKCRVKRGDR
VWQLAFGSGFKCNSIVWRALRTIPANESLVGNPWGDSVHKYPVHVT
>gnl|CDD|177809 PLN00416, PLN00416, carbonate dehydratase
MATESYEAAIKGLNDLLSTKADLGNVAAAKIKALTAELKELDSSNSDAIERIKTGFTQFKTEKYLKNSTL
FNHLAKTQTPKFLVFACSDSRVCPSHILNFQPGEAFVVRNIANMVPPFDQKRHSGVGAAVEYAVVHLKVE
NILVIGHSCCGGIKGLMSIEDDAAPTQSDFIENWVKIGASARNKIKEEHKDLSYDDQCNKCEKEAVNVSL
GNLLSYPFVRAEVVKNTLAIRGGHYNFVKGTFDLWELDFKTTPAFAFS
>gnl|CDD|177810 PLN00417, PLN00417, oxidoreductase, 2OG-Fe(II) oxygenase family protein
MEKPKFKTVQEVVAAGEGLPERYLHTPTGDGEGQPLNGAVPEMDIPAIDLSLLLSSSDDGREELSKLHSA
LSTWGVVQVMNHGITEAFLDKIYKLTKQFFALPTEEKQKCAREIGSIQGYGNDMILSDDQVLDWIDRLYL
TTYPEDQRQLKFWPQVPVGFRETLHEYTMKQRLVIEKFFKAMARSLELEENCFLEMYGENATMDTRFNMY
PPCPRPDKVIGVKPHADGSAFTLLLPDKDVEGLQFLKDGKWYKAPIVPDTILINVGDQMEIMSNGIYKSP
VHRVVTNREKERISVATFCIPGADKEIQPVDGLVSEARPRLYKTVKKYVELFFKYYQQGRRPIEAALI
>gnl|CDD|177811 PLN02150, PLN02150, terpene synthase/cyclase family protein
MRRGEVANGVNCYMKQHGVTKEEAVSELKKMIRDNYKIVMEEFLTIKDVPRPVLVRCLNLARLIDVYCYN
EGDGFTYPHGKLKDLITSLFFHPLPL
>gnl|CDD|177812 PLN02151, PLN02151, trehalose-phosphatase
MVRFIEENTTKMLETKTISNSEVLYVGRDDGDTSPKTKALHDFQINNGGGLIRSWVDSMRACSPTRPKSF
NKQSCWIKEHPSALNMFEEILHKSEGKQIVMFLDYDGTLSPIVDDPDRAFMSKKMRNTVRKLAKCFPTAI
VSGRCREKVSSFVKLTELYYAGSHGMDIKGPEQGSKYKKENQSLLCQPATEFLPVINEVYKKLVEKTKSI
PGAKVENNKFCASVHFRCVEENKWSDLANQVRSVLKNYPKLMLTQGRKVLEIRPIIKWDKGKALEFLLES
LGYANCTDVFPIYIGDDRTDEDAFKILRDKKQGLGILVSKYAKETNASYSLQEPDEVMEFLERLVEWKQL
RCGA
>gnl|CDD|177813 PLN02152, PLN02152, indole-3-acetate beta-glucosyltransferase
MAPPHFLLVTFPAQGHVNPSLRFARRLIKTTGTRVTFATCLSVIHRSMIPNHNNVENLSFLTFSDGFDDG
VISNTDDVQNRLVNFERNGDKALSDFIEANLNGDSPVTCLIYTILPNWAPKVARRFHLPSVLLWIQPAFV
FDIYYNYSTGNNSVFEFPNLPSLEIRDLPSFLSPSNTNKAAQAVYQELMEFLKEESNPKILVNTFDSLEP
EFLTAIPNIEMVAVGPLLPAEIFTGSESGKDLSVRDQSSSYTLWLDSKTESSVIYVSFGTMVELSKKQIE
ELARALIEGKRPFLWVITDKLNREAKIEGEEETEIEKIAGFRHELEEVGMIVSWCSQIEVLRHRAVGCFV
THCGWSSSLESLVLGVPVVAFPMWSDQPANAKLLEEIWKTGVRVRENSEGLVERGEIRRCLEAVMEEKSV
ELRESAEKWKRLAIEAGGEGGSSDKNVEAFVKTLC
>gnl|CDD|177814 PLN02153, PLN02153, epithiospecifier protein
MAPTLQGGWIKVEQKGGKGPGPRCSHGIAVVGDKLYSFGGELKPNEHIDKDLYVFDFNTHTWSIAPANGD
VPRISCLGVRMVAVGTKLYIFGGRDEKREFSDFYSYDTVKNEWTFLTKLDEEGGPEARTFHSMASDENHV
YVFGGVSKGGLMKTPERFRTIEAYNIADGKWVQLPDPGENFEKRGGAGFAVVQGKIWVVYGFATSILPGG
KSDYESNAVQFFDPASGKWTEVETTGAKPSARSVFAHAVVGKYIIIFGGEVWPDLKGHLGPGTLSNEGYA
LDTETLVWEKLGECGEPAMPRGWTAYTTATVYGKNGLLMHGGKLPTNERTDDLYFYAVNSA
>gnl|CDD|215111 PLN02154, PLN02154, carbonic anhydrase
MAFTLGRRARRLVSATSVHQNGCLHKLQQTGSDRFQLGEAKAIRLLPRRTNMVQELGIREEFMDLNRETE
TSYDFLDEMRHRFLKFKRQKYLPEIEKFKALAIAQSPKVMVIGCADSRVCPSYVLGFQPGEAFTIRNVAN
LVTPVQNGPTETNSALEFAVTTLQVENIIVMGHSNCGGIAALMSHQNHQGQHSSLVERWVMNGKAAKLRT
QLASSHLSFDEQCRNCEKESIKDSVMNLITYSWIRDRVKRGEVKIHGCYYNLSDCSLEKWRLSSDKTNYG
FYISDREIWS
>gnl|CDD|165802 PLN02155, PLN02155, polygalacturonase
MTKSAITFPLLFTLLTFIDVSSSASNVFNVVSFGAKPDGVTDSTAAFLKAWQGACGSASSATVVVPTGTF
LLKVITFGGPCKSKITFQVAGTVVAPEDYRTFGNSGYWILFNKVNRFSLVGGTFDARANGFWSCRKSGQN
CPPGVRSISFNSAKDVIISGVKSMNSQVSHMTLNGCTNVVVRNVKLVAPGNSPNTDGFHVQFSTGVTFTG
STVQTGDDCVAIGPGTRNFLITKLACGPGHGVSIGSLAKELNEDGVENVTVSSSVFTGSQNGVRIKSWAR
PSTGFVRNVFFQDLVMKNVENPIIIDQNYCPTHEGCPNEYSGVKISQVTYKNIQGTSATQEAMKLVCSKS
SPCTGITLQDIKLTYNKGTPATSFCFNAVGKSLGVIQPTSCLNR
>gnl|CDD|177816 PLN02156, PLN02156, gibberellin 2-beta-dioxygenase
MVIVLQPATFDSNLYVNPKCKPVPVLIPVIDLTDSDAKTQIVKACEEFGFFKVINHGVRPDLLTQLEQEA
IGFFALPHSLKDKAGPPDPFGYGTKRIGPNGDVGWLEYILLNANLCLESHKTTAVFRHTPAIFREAVEEY
MKEMKRMSSKVLEMVEEELKIEPKEKLSKLVKVKESDSCLRMNHYPEKEETPEKVEIGFGEHTDPQLISL
LRSNDTAGLQICVKDGTWVDVPPDHSSFFVLVGDTLQVMTNGRFKSVKHRVVTNTKRSRISMIYFAGPPL
SEKIAPLSCLVPKQDDCLYNEFTWSQYKLSAYKTKLGDYRLGLFEKQPPFSLSTV
>gnl|CDD|177817 PLN02157, PLN02157, 3-hydroxyisobutyryl-CoA hydrolase-like protein
MHNAKGLLGRIVRDKLWRFGYRRSFCSLKLTPEDLDYQVLVEGSGCSRTAILNRPPALNALTTHMGYRLQ
KLYKNWEEDPNIGFVMMKGSGRAFCAGGDIVSLYHLRKRGSPDAIREFFSSLYSFIYLLGTYLKPHVAIL
NGVTMGGGTGVSIPGTFRVATDRTIFATPETIIGFHPDAGASFNLSHLPGRLGEYLGLTGLKLSGAEMLA
CGLATHYIRSEEIPVMEEQLKKLLTDDPSVVESCLEKCAEVAHPEKTGVIRRIDLLEKCFSHDTVEEIID
SLEIEAGRRKDTWCITTLRRLKESSPLSLKVALRSIREGRLQTLDQCLIREYRMSLQGLIGPMSGNFCEG
VRARLIDKDEAPKWDPPSLEKVSEDMVDDYFCALTPTEPDLDLPVKLRESI
>gnl|CDD|177818 PLN02159, PLN02159, Fe(2+) transport protein
MALMKLVFILLILVSFAVSPATSTAPEECDSESANPCINKAKALPLKIIAIVAILTTSMIGVTAPLFSRY
VSFLRPDGNIFTIVKCFASGIILGTGFMHVLPDSFEMLSSKCLEDNPWHKFPFAGFVAMLSGLVTLAIDS
MATSLYTSKNSVGPMPDHGHSHGHGVVLKTKDDGNAQLLRYRVIAMVLELGIIVHSVVIGLSLGATNDTC
TIKGLIAALCFHQMFEGMGLGGCILQAEYTNVKKFLMAFFFAVTTPFGIFLGIALSSIYRDNSPTALITV
GLLNACSAGLLIYMALVDLLAAEFMGPKLQGSIKLQIKCFFAALLGCGGMSIVAKWA
>gnl|CDD|177819 PLN02160, PLN02160, thiosulfate sulfurtransferase
MSQSISSSTKAEEVVSVDVSQAKTLLQSGHQYLDVRTQDEFRRGHCEAAKIVNIPYMLNTPQGRVKNQEF
LEQVSSLLNPADDILVGCQSGARSLKATTELVAAGYKKVRNKGGGYLAWVDHSFPINQEEEEPSAN
>gnl|CDD|177820 PLN02161, PLN02161, beta-amylase
MAETGVIGCGCRGVTGGNFFHPGGFSLKSCFLEQSTKRNRNFFRSVSMIPPFKRGRFITKWRSVAGNSRI
FSMDAREKSRSFVLVSSRHKRVPVFVMMPVDTFGIDASGCPKIKRLKALTVSLKALKLAGVHGIAVEVWW
GIVERFSPLEFKWSLYEELFRLISEAGLKLHVALCFHSNMHLFGGKGGISLPLWIREIGDVNKDIYYRDK
NGFSNNDYLTLGVDQLPLFGGRTAVQCYEDFMLSFSTKFEPYIGNVIEEISIGLGPSGELRYPAHPSGDG
RWKFPGIGEFQCHDKYMMEDLMAVASQEGKPQWGSRDPPNTGCYNSFPSGVPFFEEGNDSFLSDYGRFFL
EWYSGKLICHADAILAKAADVLRRRQESEKSSVMLVAKIGGIYWWYKTSSHPAELTAGYYNTALRDGYDP
VASVLSRHGAALHIPCLDMADSETPEKYLCSPEGLRQQIHDVSKKWTIHVTGRNTSERFDEMGLRQIREN
CVQPNGDTLRSFTFCRMNEKIFRAENWNNFVPFIRQMSADM
>gnl|CDD|177821 PLN02162, PLN02162, triacylglycerol lipase
MKFCNSYFLVDPTKASFLDLLLLLFSFNLTSARFIDSPPDTLKGFRRSFASRWILALAIFLQKVLMLLSK
PFAFIGQKLTYWLNLLTANGGFFNLILNLLSGKLVKPDKSSATYTSFIGCSDRRIELDEKIDVGSIEYKS
MLSIMASKISYESKPFINSVVKNTWKMDLVGNYDFYNAFQESKLTQAFVFKTSSTNPDLIVVSFRGTEPF
EAADWCTDLDLSWYELKNVGKVHAGFSRALGLQKDGGWPKENISLLHQYAYYTIRQMLRDKLARNKNLKY
ILTGHSLGGALAALFPAILAIHGEDELLDKLEGIYTFGQPRVGDEDFGEFMKGVVKKHGIEYERFVYNND
VVPRVPFDDKLLFSYKHYGPCNSFNSLYKGKVREDAPNANYFNLLWLIPQLLTGLWEFIRSFILQFWKGD
EYKENWLMRFVRVVGIVFPGGSNHFPFDYVNSTRLGGLVRPPPSTTPEDKLALIA
>gnl|CDD|177822 PLN02164, PLN02164, sulfotransferase
MESKTLNDTVTTVPSHEEAVTEPTEFEKNQKRYQDLIATLPHKKGWRPKEPLIEYGGHWWLQPLLEGLLH
AQEFFQARPNDFLVCSYPKTGTTWLKALTFAIANRSRFDDSSNPLLKRNPHEFVPYIEIDFPFFPSVDVL
KDKGNTLFSTHIPYGLLPDSVVKSGCKMVYIWRDPKDTFISMWTFLHKERSQQGPLNSLEESFDMFCRGL
SVYGPYLDHVLGYWKAYQENPDRILFLKYETMRADPLPYVKRLAEFMGYGFTAEEEEKGVVEKVVKLCSF
ETLKNLEANKGEKDREDRPAVYANSAYFRKGKVGDWQNYLTPEMAARIDGLMEEKFKGTGLLEHDS
>gnl|CDD|177823 PLN02165, PLN02165, adenylate isopentenyltransferase
MQNLKFLFVSPPLLPITIPRRKLPPPRSVVTMTSVAMEQNCKDKVVVIMGATGSGKSRLSVDLATRFPSE
IINSDKMQVYDGLKITTNQITIQDRRGVPHHLLGELNPDDGELTASEFRSLASLSISEITSRQKLPIVAG
GSNSFIHALLADRFDPEIYPFSSGSSLISSDLRYDCCFIWVDVSEPVLFEYLSKRVDEMMDSGMFEELAE
FYDPVKSGSEPLGIRKAIGVPEFDRYFKKYPPENKMGKWDQARKAAYEEAVREIKENTCQLAKRQIEKIM
KLKSAGWDIKRVDATASFRAVMRKKGKKKKWREIWEKDVLEPSVKIVKRFLVED
>gnl|CDD|165812 PLN02166, PLN02166, dTDP-glucose 4,6-dehydratase
MKQLHKQMSVNHRRDEEIPTSQSSPYSPKTLKHPRSLPRSINYLFKEQRLLFILVGILIGSTFFILQPSL
SRLGPAESTSLITRSVSIAVTDSPPSSSTFNSSGGGGRTGRVPVGIGRKRLRIVVTGGAGFVGSHLVDKL
IGRGDEVIVIDNFFTGRKENLVHLFGNPRFELIRHDVVEPILLEVDQIYHLACPASPVHYKYNPVKTIKT
NVMGTLNMLGLAKRVGARFLLTSTSEVYGDPLEHPQKETYWGNVNPIGERSCYDEGKRTAETLAMDYHRG
AGVEVRIARIFNTYGPRMCLDDGRVVSNFVAQTIRKQPMTVYGDGKQTRSFQYVSDLVDGLVALMEGEHV
GPFNLGNPGEFTMLELAEVVKETIDSSATIEFKPNTADDPHKRKPDISKAKELLNWEPKISLREGLPLMV
SDFRNRILNEDEGKGL
>gnl|CDD|215112 PLN02167, PLN02167, UDP-glycosyltransferase family protein
KKEAELIFVPFPSTGHILVTIEFAKRLINLDRRIHTITILYWSLPFAPQADAFLKSLIASEPRIRLVTLP
EVQDPPPMELFVKASEAYILEFVKKMVPLVRDALSTLVSSRDESDSVRVAGLVLDFFCVPLIDVGNEFNL
PSYIFLTCNAGFLGMMKYLPERHRKTASEFDLSSGEEELPIPGFVNSVPTKVLPPGLFMKESYEAWVEIA
ERFPEAKGILVNSFTELEPNAFDYFSRLPENYPPVYPVGPILSLKDRTSPNLDSSDRDRIMRWLDDQPES
SVVFLCFGSLGSLPAPQIKEIAQALELVGCRFLWSIRTNPAEYASPYEPLPEGFMDRVMGRGLVCGWAPQ
VEILAHKAIGGFVSHCGWNSVLESLWFGVPIATWPMYAEQQLNAFTMVKELGLAVELRLDYVSAYGEIVK
ADEIAGAVRSLMDGEDVPRKKVKEIAEAARKAVMDGGSSFVAVKRFIDDLLGDHS
>gnl|CDD|215113 PLN02168, PLN02168, copper ion binding / pectinesterase
MRHVFVEVFVLISLVILELSYAFAPIVSYQWVVSYSQRFILGGNKQVIVINDMFPGPLLNATANDVINVN
IFNNLTEPFLMTWNGLQLRKNSWQDGVRGTNCPILPGTNWTYRFQVKDQIGSYFYFPSLLLQKAAGGYGA
IRIYNPELVPVPFPKPDEEYDILIGDWFYADHTVMRASLDNGHSLPNPDGILFNGRGPEETFFAFEPGKT
YRLRISNVGLKTCLNFRIQDHDMLLVETEGTYVQKRVYSSLDIHVGQSYSVLVTAKTDPVGIYRSYYIVA
TARFTDAYLGGVALIRYPNSPLDPVGPLPLAPALHDYFSSVEQALSIRMDLNVGAARSNPQGSYHYGRIN
VTRTIILHNDVMLSSGKLRYTINGVSFVYPGTPLKLVDHFQLNDTIIPGMFPVYPSNKTPTLGTSVVDIH
YKDFYHIVFQNPLFSLESYHIDGYNFFVVGYGFGAWSESKKAGYNLVDAVSRSTVQVYPYSWTAILIAMD
NQGMWNVRSQKAEQWYLGQELYMRVKGEGEEDPSTIPVRDENPIPGNVIRCGKVS
>gnl|CDD|177826 PLN02169, PLN02169, fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
MAMLGLLEFFVAFIFFLVCLFTCFFIHKKPHGQPILKNWPFLGMLPGMLHQIPRIYDWTVEVLEASNLTF
YFKGPWLSGTDMLFTADPKNIHHILSSNFGNYPKGPEFKKIFDVLGEGILTVDFELWEDLRKSNHALFHN
QDFIELSLSSNKSKLKEGLVPFLDNAAHENIIIDLQDVFMRFMFDTSSILMTGYDPMSLSIEMLEVEFGE
AADIGEEAIYYRHFKPVILWRLQNWIGIGLERKMRTALATVNRMFAKIISSRRKEEISRAETEPYSKDAL
TYYMNVDTSKYKLLKPKKDKFIRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTKFDNED
LEKLVYLHAALSESMRLYPPLPFNHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWGEDALDFKPE
RWISDNGGLRHEPSYKFMAFNSGPRTCLGKHLALLQMKIVALEIIKNYDFKVIEGHKIEAIPSILLRMKH
GLKVTVTKKI
>gnl|CDD|215114 PLN02170, PLN02170, probable pectinesterase/pectinesterase inhibitor
MMASSSSISNHKFPITLMFLLILNFLYLSAVVFASNSNSHFSKFSRHPNSDSSSRSSPSSSSKQGFLSSV
QESMNHALFARSLAFNLTLSHRTVQTHTFDPVNDCLELLDDTLDMLSRIVVIKHADHDEEDVHTWLSAAL
TNQETCEQSLQEKSSSYKHGLAMDFVARNLTGLLTNSLDLFVSVKSKHSSSSKGGRKLLSEQDFPTWVSS
SERKLLEAPVEELKVHAVVAADGSGTHKTIGEALLSTSLESGGGRTVIYLKAGTYHENLNIPTKQKNVML
VGDGKGKTVIVGSRSNRGGWTTYQTATVAAMGDGFIARDITFVNSAGPNSEQAVALRVGSDKSVVYRCSV
EGYQDSLYTHSKRQFYRETDITGTVDFIFGNSAVVFQSCNIAARKPSGDRNYVTAQGRSDPNQNTGISIH
NCRITAESMTYLGRPWKEYSRTVVMQSFIDGSIHPSGWSPWSGSFALKTLYYGEFGNSGPGSSVSGRVKW
SGYHPSLTLTEAQKFTVAGFIDGNMWLPSTGVSFDSGLV
>gnl|CDD|215115 PLN02171, PLN02171, endoglucanase
MEKFARVILLALLLLAAAQLCFPVAFGGHDYGQALSKSILFFEAQRSGVLPPNQRVTWRANSGLFDGKAS
GVDLVGGYYDAGDNVKFGLPMAFTVTMMSWSIIEYGKQMAAAGELGHAMDAVKWGTDYFIKAHPEPNVLY
GEVGDGDTDHYCWQRPEDMTTDRQAYRIDPQNPGSDLAGETAAAMAAASIVFRRSNPGYANELLTHAKQL
FDFADKYRGKYDSSITVAQKYYRSVSGYGDELLWAAAWLYQATNNQYYLDYLGNNGDALGGTGWSMTEFG
WDVKYAGVQVLVAKFLMQGKAGEHAAVFQRYQQKAEFFMCSCLGKGARNVQKTPGGLIYRQRWNNMQFVT
SASFLLTVYSDYLASSGRALRCAAGNAAPSQLLAFAKSQVDYILGDNPRATSYMVGYGANYPRQVHHRGS
SIVSIKVDPSFVSCRGGYATWFSRKGSDPNLLTGAIVGGPDAYDNFADERDNYEQTEPATYNNAPLLGVL
ARLAGGHGGYNQLLVVVPAPSEVAINRTPAPQRRPPTPAPASTSSPIEIEQKATASWKAKGRTYYRYSTT
VTNRSAKTLKELHLGISKLYGPLWGLTKAGYGYVLPSWMPSLPAGKSLEFVYVHSASPADVWVSGYKLA
>gnl|CDD|215116 PLN02172, PLN02172, flavin-containing monooxygenase FMO GS-OX
MAPAQNPINSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVYTPKSESDPLSLDPTRSIVH
SSVYESLRTNLPRECMGYRDFPFVPRFDDESRDSRRYPSHREVLAYLQDFAREFKIEEMVRFETEVVRVE
PVDGKWRVQSKNSGGFSKDEIFDAVVVCNGHYTEPNVAHIPGIKSWPGKQIHSHNYRVPDPFKNEVVVVI
GNFASGADISRDIAKVAKEVHIASRASESDTYEKLPVPQNNLWMHSEIDTAHEDGSIVFKNGKVVYADTI
VHCTGYKYHFPFLETNGYMRIDENRVEPLYKHVFPPALAPGLSFIGLPAMGIQFVMFEIQSKWVAAVLSG
RVTLPSEDKMMEDINAWYASLEALGIPKRYTHKLGKIQSEYLNWIAEECGCPLVEHWRYQEVDRGYQRLV
SQPETYRDEWDDDDLMEEAYEDFARKKLISSHPSYFLESGR
>gnl|CDD|177830 PLN02173, PLN02173, UDP-glucosyl transferase family protein
MEKMRGHVLAVPFPSQGHITPIRQFCKRLHSKGFKTTHTLTTFIFNTIHLDPSSPISIATISDGYDQGGF
SSAGSVPEYLQNFKTFGSKTVADIIRKHQSTDNPITCIVYDSFMPWALDLAREFGLAAAPFFTQSCAVNY
INYLSYINNGSLTLPIKDLPLLELQDLPTFVTPTGSHLAYFEMVLQQFTNFDKADFVLVNSFHDLDLHEN
ELLSKVCPVLTIGPTVPSMYLDQQIKSDNDYDLNLFDLKEAALCTDWLDKRPQGSVVYIAFGSMAKLSSE
QMEEIASAISNFSYLWVVRASEESKLPPGFLETVDKDKSLVLKWSPQLQVLSNKAIGCFMTHCGWNSTME
GLSLGVPMVAMPQWTDQPMNAKYIQDVWKVGVRVKAEKESGIAKREEIEFSIKEVMEGEKSKEMKENAGK
WRDLAVKSLSEGGSTDININTFVSKIQIK
>gnl|CDD|177831 PLN02174, PLN02174, aldehyde dehydrogenase family 3 member H1
MAAKKMFGAADASILVTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVY
EVSLLRNSIKLALKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAG
NAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAK
HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCNNGQACISPDYILTTKEYAPKVIDAMKKELETF
YGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILLDVPLDSLIMSEEIFG
PLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGE
SGMGAYHGKFSFDAFSHKKAVLYRSLFGDSAVRYPPYSRGKLRLLKALVDSNIFDIFKVLLGLS
>gnl|CDD|177832 PLN02175, PLN02175, endoglucanase
MTSPFFFVFLFSSLLIENTDANPNYKEALSKSLLFFQGQRSGPLPRGQQLSWRASSGLSDGSAAHVDLTG
GYYDAGDNVKFNFPMAFTTTMLSWSALEYGKRMGPELENARVNIRWATDYLLKCARATPGKLYVGVGDPN
VDHKCWERPEDMDTPRTVYSVSPSNPGSDVAAETAAALAAASMVFRKVDSKYSRLLLATAKKVMQFAIQY
RGAYSDSLSSSVCPFYCSYSGYKDELMWGASWLLRATNDPYYANFIKSLGGGDQPDIFSWDNKYAGAYVL
LSRRALLNKDSNFEQYKQAAENFICKILPDSPSSSTQYTQGGLMYKLPQSNLQYVTSITFLLTTYAKYMK
STKHTFNCGNSVIVPNALISLSKRQVDYILGDNPIKMSYMVGFSSNFPKRIHHRASSLPSHALRSNSLGC
NGGFQSFYTQNPNPNILTGAIVGGPNQNDGYPDQRDDYSHAEPATYINAAFVGPLAYFAAGRSP
>gnl|CDD|215117 PLN02176, PLN02176, putative pectinesterase
MKGVTFHSFCYSYFKVCLLVMTLAYGSAEYDAASSQIAKTIIVNPNDARYFKTVQSAIDSIPLQNQNWIR
ILIQNGIYREKVTIPKEKGYIYMQGKGIEKTIIAYGDHQATDTSATFTSYASNIIITGITFKNTYNIASN
SSRPTKPAVAARMLGDKYAIIDSSFDGFQDTLFDGKGRHYYKRCVISGGIDFIFGYAQSIFEGCTLKLTL
GIYPPNEPYGTITAQGRPSPSDKGGFVFKDCTVTGVGKALLGRAWGSYARVIFYRSRFSDVILPIGWDAW
RAKGQERHITFVEFGCTGVGADTSKRVPWLKKASEKDVLQFTNLTFIDEEGWLSRLPIKF
>gnl|CDD|215118 PLN02177, PLN02177, glycerol-3-phosphate acyltransferase
GAMGASRRFEPISKCSSEGRSNQTVAADLDGTLLISRSAFPYYLLVALEAGSLLRALILLLSVPFVYFTY
LFISESLAIKTFVFIAFAGLKIRDIELVSRSVLPKFYAEDVHPETWRVFNSFGKRYIITASPRIMVEPFV
KTFLGADKVLGTELEVSKSGRATGFMKKPGVLVGDHKRDAVLKEFGDALPDLGLGDRETDHDFMSICKEG
YMVPRTKCEPLPRNKLLSPVIFHEGRLVQRPTPLVALLTFLWMPIGFILSLLRVYLNIPLPERIARYNYK
LLGIRLIVKGNPPPPPKKGQPGVLFVCNHRTVLDPVVTAVALGRKISCVTYSISKFSELISPIKAVALSR
EREKDAANIKRLLEEGDLVICPEGTTCREPFLLRFSALFAELTDRIVPVAINTKQSMFHGTTVRGYKLLD
PYFVFMNPRPTYEITFLNQLPKELTCKGGKSPIEVANYIQRVLAGTLGFECTNLTRKDKYAILAGTDGRV
PSKKEKK
>gnl|CDD|177834 PLN02178, PLN02178, cinnamyl-alcohol dehydrogenase
MVDQNKAFGWAANDESGVLSPFHFSRRENGENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVG
IATKVGKNVTKFKEGDRVGVGVIIGSCQSCESCNQDLENYCPKVVFTYNSRSSDGTRNQGGYSDVIVVDH
RFVLSIPDGLPSDSGAPLLCAGITVYSPMKYYGMTKESGKRLGVNGLGGLGHIAVKIGKAFGLRVTVISR
SSEKEREAIDRLGADSFLVTTDSQKMKEAVGTMDFIIDTVSAEHALLPLFSLLKVSGKLVALGLPEKPLD
LPIFPLVLGRKMVGGSQIGGMKETQEMLEFCAKHKIVSDIELIKMSDINSAMDRLAKSDVRYRFVIDVAN
SLLPESSAEILTEHVDHGVSITSRF
>gnl|CDD|177835 PLN02179, PLN02179, carbonic anhydrase
MDPNTKTIFFFVVFFIDLFFPNILLVYAREIGNKPLFTYKQKTEKGPAEWGKLNPQWKVCSTGKYQSPID
LTDERVSLIHDQALSRHYKPAPAVIQSRGHDVMVSWKGDAGKITIHQTDYKLVQCHWHSPSEHTINGTSY
DLELHMVHTSASGKTAVVGVLYKLGEPDEFLTKLLNGIKGVGKKEINLGIVDPRDIRFETNNFYRYIGSL
TIPPCTEGVIWTVVKRVVWFFDFNV
>gnl|CDD|177836 PLN02180, PLN02180, gamma-glutamyl transpeptidase 4
MGDAIIADPLLAIDHETVAEKKKKKQSKNLKIALFLLLIILAASGGFSFNDKITTVFLSRQAIDDDHSLS
HGTISDMVESENGVVAADDARCSEIGASVLRRGGHAVDAAVAITLCIGVVNPMSSGIGGGSFLIVSSQKD
SKAEAFDMRETAPLAASKDMYKNDASAKSLGALSMGVPGEIAGLYEAWKRYGRLPWKPLFEPAIELARDG
FVVHPYLGKAISSHAAMILKDPGLRSVFSRNGQVLKPGETCYNPELAQSLETISEQGPGAFYNGTIGEKL
VKDVKKAGGIITMDDLRSYEVLVTDAMSVDVMGYTIHGMPPPSGGTLGFSMVIDILDSYSNLYTASGREL
GLHRLIEAMKHMFAARMDLGDPEFVNITNAMNQMLSKAHAEEIQKRIFDNTTFPPEYYLNRWSQLRDQGT
SHFCIVDADRNSVSMTSTVNYGFGAGVLSPSTGIVLNNEMDDFSTPAEITPDMLPPAPTNFIEPNKRPLS
SMTPLVITKDGEFVAALGGAGGMHIIPAVLQVFLNCFVLNMKPKEAVESARIYHRLIPNVVSYENFTAIN
GDHIGVSEDTKMFLAERGHELKALSGGAIVQLIVQSFKEEKEEEMIIEIGRKIGKKSKPLKGLLTAVCDP
RKDGKPAAV
>gnl|CDD|177837 PLN02182, PLN02182, cytidine deaminase
MAQRPNLLSHLQDLVTKFKNMTMAQDRFKFVFTANEAAAEGVTDPIRLPNLIRKAMCLARAPISKYKVGA
VGRASSGRVYLGVNVDFPGLPLHHSIHAEQFLVTNLALNSEKDLCELAVAISTDGKEFGTPCGHCLQFLM
EMSNALDIKILSKPKHEAGSFSSLRHLLPNVLPKGSPFLLEKRDNCLTLSGPAGEICSLDCSHLKCKALA
AANNSFSPYTESPSGVALLDNDGKWYRGWYIESVASNPSFGPVQAALVDFVARSRGKMFNKIVQAVLVEK
NNAIVSQERTAKIILDTIAAPNCDFKVFHCSVDCAKRLKYLRDTLVIDTSLGDYTGLHY
>gnl|CDD|165828 PLN02183, PLN02183, ferulate 5-hydroxylase
MDSPLQSLLTSPSFFLILISLFLFLGLISRLRRRLPYPPGPKGLPIIGNMLMMDQLTHRGLANLAKQYGG
LFHMRMGYLHMVAVSSPEVARQVLQVQDSVFSNRPANIAISYLTYDRADMAFAHYGPFWRQMRKLCVMKL
FSRKRAESWASVRDEVDSMVRSVSSNIGKPVNIGELIFTLTRNITYRAAFGSSSNEGQDEFIKILQEFSK
LFGAFNVADFIPWLGWIDPQGLNKRLVKARKSLDGFIDDIIDDHIQKRKNQNADNDSEEAETDMVDDLLA
FYSEEAKVNESDDLQNSIKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVG
LNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWED
PDTFKPSRFLKPGVPDFKGSHFEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWELPDGMKPSELDM
NDVFGLTAPRATRLVAVPTYRLQCPL
>gnl|CDD|177838 PLN02184, PLN02184, superoxide dismutase [Fe]
MAASSAVTANYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTELEGKPLEHIIHSTYN
NGDLLPAFNNAAQAWNHEFFWESMKPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLA
YSNEKLKVVKTPNAVNPLVLGSFPLLTIDVWEHAYYLDFQNRRPDYIKTFMTNLVSWEAVSARLEAAKAA
SA
>gnl|CDD|215119 PLN02187, PLN02187, rooty/superroot1
MSEEQPHANLAVPAFKTEKEPITQTRNGQSSVWRFGGSDKAAKASTVTLRGVIYMLFDNCGKDVNKTILP
LGHGDPSVYPCFRTCIEAEDAVVDVLRSGKGNSYGPGAGILPARRAVADYMNRDLPHKLTPEDIFLTAGC
NQGIEIVFESLARPNANILLPRPGFPHYDARAAYSGLEVRKFDLLPEKEWEIDLEGIEAIADENTVAMVV
INPNNPCGNVYSHDHLKKVAETARKLGIMVISDEVYDRTIFGDNPFVSMGKFASIVPVLTLAGISKGWVV
PGWKIGWIALNDPEGVFETTKVLQSIKQNLDVTPDPATIIQAALPAILEKADKNFFAKKNKILKHNVDLV
CDRLKDIPCVVCPKKPESCTYLLTKLELSLMDNIKDDIDFCVKLAREENLVFLPGDALGLKNWMRITIGV
EAHMLEDALERLKGFCTRHAKKTETETNSLQALKLSDNNLEM
>gnl|CDD|215120 PLN02188, PLN02188, polygalacturonase/glycoside hydrolase family protein
MEFRLLLLLVVVFIVNALVLSSAGGGSVVKGSSTFLFDVRSFGARANGHTDDSKAFMAAWKAACASTGAV
TLLIPPGTYYIGPVQFHGPCTNVSSLTFTLKAATDLSRYGSGNDWIEFGWVNGLTLTGGGTFDGQGAAAW
PFNKCPIRKDCKLLPTSVKFVNMNNTVVRGITSVNSKFFHIALVECRNFKGSGLKISAPSDSPNTDGIHI
ERSSGVYISDSRIGTGDDCISIGQGNSQVTITRIRCGPGHGISVGSLGRYPNEGDVTGLVVRDCTFTGTT
NGIRIKTWANSPGKSAATNMTFENIVMNNVTNPIIIDQKYCPFYSCESKYPSGVTLSDIYFKNIRGTSSS
QVAVLLKCSRGVPCQGVYLQDVHLDLSSGEGGTSSSCENVRAKYIGTQIPPPCP
>gnl|CDD|215121 PLN02189, PLN02189, cellulose synthase
MEASAGLVAGSHNRNELVVIHGHEEPKPLRNLDGQVCEICGDEIGLTVDGDLFVACNECGFPVCRPCYEY
ERREGTQNCPQCKTRYKRLKGSPRVEGDDDEEDIDDIEHEFNIDDEQDKNKHITEAMLHGKMSYGRGPDD
DENNQFPPVITGVRSRPVSGEFPIGSGYGHGEQMLSSSLHKRVHPYPVSEPGSAKWDEKKEGGWKERMDD
WKMQQGNLGPDPDDYDADMALIDEARQPLSRKVPIASSKVNPYRMVIVARLVVLAFFLRYRILHPVHDAI
GLWLTSIICEIWFAVSWILDQFPKWFPIDRETYLDRLSLRYEREGEPNMLSPVDIFVSTVDPLKEPPLVT
ANTVLSILAMDYPVDKISCYVSDDGASMLTFEALSETAEFARKWVPFCKKFSIEPRAPEFYFSLKVDYLK
DKVQPTFVKERRAMKREYEEFKVRINAIVAKAQKVPPEGWIMQDGTPWPGNNTRDHPGMIQVFLGHSGGH
DTEGNELPRLVYVSREKRPGFQHHKKAGAMNALIRVSAVLTNAPFMLNLDCDHYINNSKAVREAMCFLMD
PQIGRKVCYVQFPQRFDGIDTHDRYANRNTVFFDINMKGLDGIQGPVYVGTGCVFRRQALYGYDPPKGPK
RPKMVTCDCCPCFGRRKKKHAKNGLNGEVAALGGMESDKEMLMSQMNFEKKFGQSAIFVTSTLMEEGGVP
PSSSPAALLKEAIHVISCGYEDKTDWGLELGWIYGSITEDILTGFKMHCRGWRSIYCMPKRAAFKGSAPI
NLSDRLNQVLRWALGSVEIFFSRHSPLLYGYKGGNLKWLERFAYVNTTIYPFTSLPLLAYCTLPAICLLT
GKFIMPPISTFASLFFIALFMSIFATGILELRWSGVSIEEWWRNEQFWVIGGVSAHLFAVVQGLLKVLAG
IDTNFTVTSKATDDDEFGELYAFKWTTLLIPPTTLLIINIVGVVAGISDAINNGYQSWGPLFGKLFFAFW
VIVHLYPFLKGLMGRQNRTPTIVVIWSVLLASIFSLLWVRIDPFVLKTKGPDVKQCGINC
>gnl|CDD|215122 PLN02190, PLN02190, cellulose synthase-like protein
MADSSSSLPPLCERISHKSYFLRAVDLTILGLLFSLLLYRILHMSENDTVWLVAFLCESCFSFVWLLITC
IKWSPAEYKPYPDRLDERVHDLPSVDMFVPTADPVREPPIIVVNTVLSLLAVNYPANKLACYVSDDGCSP
LTYFSLKEASKFAKIWVPFCKKYNVRVRAPFRYFLNPPVATEDSEFSKDWEMTKREYEKLSRKVEDATGD
SHWLDAEDDFEAFSNTKPNDHSTIVKVVWENKGGVGDEKEVPHLVYISREKRPNYLHHYKAGAMNFLVRV
SGLMTNAPYMLNVDCDMYANEADVVRQAMCIFLQKSKNSNHCAFVQFPQEFYDSNTNELTVLQSYLGRGI
AGIQGPIYIGSGCFHTRRVMYGLSSDDLEDDGSLSSVATREFLAEDSLAREFGNSKEMVKSVVDALQRKP
NPQNSLTNSIEAAQEVGHCHYEYQTSWGNTIGWLYDSVAEDLNTSIGIHSRGWTSSYISPDPPAFLGSMP
PGGPEAMVQQRRWATGLIEVLFNKQSPLIGMFCRKIRFRQRLAYLYVFTCLRSIPELIYCLLPAYCLLHN
SALFPKGVYLGIIVTLVGMHCLYTLWEFMSLGFSVQSWYVSQSFWRIKATSSWLFSIQDIILKLLGISKT
VFIVTKKTMPETKSGSGSGPSQGEDDGPNSDSGKFEFDGSLYFLPGTFIVLVNLAALAGFLVGLQRSSYS
HGGGGSGLAEACGCILVVMLFLPFLKGLFEKGKYGIPLSTLSKAAFLAVLFVVFSV
>gnl|CDD|177843 PLN02191, PLN02191, L-ascorbate oxidase
MAMIVWWIVTVVAVLTHTASAAVREYTWEVEYKYWWPDCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTN
KLTTEGLVIHWHGIRQKGSPWADGAAGVTQCAINPGETFTYKFTVEKPGTHFYHGHYGMQRSAGLYGSLI
VDVAKGPKERLRYDGEFNLLLSDWWHESIPSQELGLSSKPMRWIGEAQSILINGRGQFNCSLAAQFSNGT
ELPMCTFKEGDQCAPQTLRVEPNKTYRIRLASTTALASLNLAVQGHKLVVVEADGNYITPFTTDDIDIYS
GESYSVLLTTDQDPSQNYYISVGVRGRKPNTTQALTILNYVTAPASKLPSSPPPVTPRWDDFERSKNFSK
KIFSAMGSPSPPKKYRKRLILLNTQNLIDGYTKWAINNVSLVTPATPYLGSVKYNLKLGFNRKSPPRSYR
MDYDIMNPPPFPNTTTGNGIYVFPFNVTVDVIIQNANVLKGVVSEIHPWHLHGHDFWVLGYGDGKFKPGI
DEKTYNLKNPPLRNTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEGLNRIGKIPDEALG
CGLTKQFLMNRNRN
>gnl|CDD|215123 PLN02192, PLN02192, 3-ketoacyl-CoA synthase
MSEVNQKTPLIEPSSSRKLPDFKKSVKLKYVKLGYHYLITHGMYLFLSPLVVVIAAQLSTFSIQDLHDLW
EHLKFNLISVILCSTLLVFLSTLYFLTRPRPVYLVDFSCYKPDDSRKCTRKIFMDRSKLTGSFTEENLEF
QRKILERSGLGESTYLPEAVLNVPPNPCMAEARKEAETVMFGAIDQLLAKTSVKPKDIGILIVNCSLFNP
TPSLSAMVINHYKLRGNILSYNLGGMGCSAGLISIDLAKHLLQVHPNSYALVISMENITLNWYFGNDRSM
LVSNCLFRMGGAAILLSNKRSDRRRSKYQLVHTVRTHKGADDKCFACVTQEEDSAGKIGVSLSKDLMAVA
GDALKTNITTLGPLVLPMSEQLLFFATLVGKKLFKMKLKPYIPDFKLAFEHFCIHAGGRAVLDELEKNLQ
LSDWHMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRTWQIAFGSGFKCNSAVWKALRTVNPAKE
KNPWMDEIHEFPVDVPKVSTI
>gnl|CDD|177844 PLN02193, PLN02193, nitrile-specifier protein
MAQKLEAKGGETGDVWDDGVYDNVRKVYVGQGQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEIDA
DDYIVYVEGYREKVNDMTSEMITFLSFKTYKGKTSHPIEKRPGVKFVLQGGKIVGFHGRSTDVLHSLGAY
ISLPSTPKLLGKWIKVEQKGEGPGLRCSHGIAQVGNKIYSFGGEFTPNQPIDKHLYVFDLETRTWSISPA
TGDVPHLSCLGVRMVSIGSTLYVFGGRDASRQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEEN
VYVFGGVSATARLKTLDSYNIVDKKWFHCSTPGDSFSIRGGAGLEVVQGKVWVVYGFNGCEVDDVHYYDP
VQDKWTQVETFGVRPSERSVFASAAVGKHIVIFGGEIAMDPLAHVGPGQLTDGTFALDTETLQWERLDKF
GEEEETPSSRGWTASTTGTIDGKKGLVMHGGKAPTNDRFDDLFFYGIDSA
>gnl|CDD|177845 PLN02194, PLN02194, cytochrome-c oxidase
MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGARLLSLGLIFILYTMFVWWRDVLRESTL
EGHHTKVVQLGPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPIL
PSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFH
VIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWWGGI
>gnl|CDD|215124 PLN02195, PLN02195, cellulose synthase A
MMESGAPICATCGEEVGVDSNGEAFVACHECSYPLCKACLEYEIKEGRKVCLRCGGPYDAENVFDDVETK
HSRNQSTMASHLNDTQDVGIHARHISSVSTVDSELNDEYGNPIWKNRVESWKDKKNKKKKSAKKKEAHKA
QIPPEQQMEEKPSADAYEPLSRVIPIPRNKLTPYRAVIIMRLIILGLFFHYRITNPVDSAFGLWLTSVIC
EIWFAFSWVLDQFPKWSPINRETYIDRLSARYEREGEPSQLAAVDFFVSTVDPLKEPPLITANTVLSILA
VDYPVDKVSCYVSDDGAAMLSFESLVETAEFARKWVPFCKKYSIEPRAPEFYFSQKIDYLKDKVQPSFVK
ERRAMKRDYEEYKVRVNALVAKAQKTPEEGWTMQDGTPWPGNNTRDHPGMIQVFLGETGARDIEGNELPR
LVYVSREKRPGYQHHKKAGAENALVRVSAVLTNAPYILNLDCDHYVNNSKAVREAMCFLMDPVVGRDVCY
VQFPQRFDGIDRSDRYANRNVVFFDVNMKGLDGIQGPVYVGTGCVFNRQALYGYGPPSLPRLPKSSSSSS
SCCCPTKKKPEQDPSEIYRDAKREDLNAAIFNLREIDNYDEYERSMLISQMSFEKTFGLSSVFIESTLME
NGGVPESANPSTLIKEAIHVISCGYEEKTEWGKEIGWIYGSVTEDILTGFKMHCRGWRSIYCMPVRPAFK
GSAPINLSDRLHQVLRWALGSVEIFLSRHCPLWYGYGGGRLKWLQRLAYINTIVYPFTSLPLIAYCTLPA
ICLLTGKFIIPTLSNLASMLFLGLFISIILTSVLELRWSGVSIEDLWRNEQFWVIGGVSAHLFAVFQGFL
KMLAGLDTNFTVTAKAADDTEFGELYMVKWTTLLIPPTSLLIINLVGVVAGFSDALNKGYEAWGPLFGKV
FFAFWVILHLYPFLKGLMGRQNRTPTIVVLWSVLLASVFSLVWVKINPFVGKTDTTTLSNNCISIDC
>gnl|CDD|177847 PLN02196, PLN02196, abscisic acid 8'-hydroxylase
MDFSALFLTLFAGALFLCLLRFLAGFRRSSSTKLPLPPGTMGWPYVGETFQLYSQDPNVFFASKQKRYGS
VFKTHVLGCPCVMISSPEAAKFVLVTKSHLFKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLRAFMPD
AIRNMVPDIESIAQESLNSWEGTQINTYQEMKTYTFNVALLSIFGKDEVLYREDLKRCYYILEKGYNSMP
INLPGTLFHKSMKARKELAQILAKILSKRRQNGSSHNDLLGSFMGDKEGLTDEQIADNIIGVIFAARDTT
ASVLTWILKYLAENPSVLEAVTEEQMAIRKDKEEGESLTWEDTKKMPLTSRVIQETLRVASILSFTFREA
VEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFEVAPKPNTFMPFGNGTHSCPGNELAKLE
ISVLIHHLTTKYRWSIVGTSNGIQYGPFALPQNGLPIALSRKP
>gnl|CDD|177848 PLN02197, PLN02197, pectinesterase
MIGKVVVSVASILLIVGVAIGVVAFINKNGDANLSPQMKAVQGICQSTSDKASCVKTLEPVKSDDPNKLI
KAFMLATKDAITKSSNFTGQTEGNMGSSISPNNKAVLDYCKRVFMYALEDLSTIVEEMGEDLNQIGSKID
QLKQWLTGVYNYQTDCLDDIEEDDLRKTIGEGIANSKILTSNAIDIFHSVVSAMAKLNNKVDDFKNMTGG
IPTPGAPPVVDESPVADPDGPARRLLEDIDETGIPTWVSGADRKLMAKAGRGANAGGGGGGKIKATHVVA
KDGSGQFKTISQAVMACPDKNPGRCIIHIKAGIYNEQVTIPKKKNNIFMFGDGARKTVISYNRSVKLSPG
TTTSLSGTVQVESEGFMAKWIGFKNTAGPMGHQAVAIRVNGDRAVIFNCRFDGYQDTLYVNNGRQFYRNI
VVSGTVDFIFGKSATVIQNSLIVVRKGSKGQYNTVTADGNEKGLAMKIGIVLQNCRIVPDKKLTAERLTV
ASYLGRPWKKFSTTVIISTEIGDLIRPEGWTIWDGEQNHKSCRYVEYNNRGPGAFTNRRVNWVKVARSAA
EVNGFTVANWLGPINWIQEANVPVTLGL
>gnl|CDD|177849 PLN02198, PLN02198, glutathione gamma-glutamylcysteinyltransferase
MSLVRTVTIVLFIIAFLQNAAAQKRQQSIVASHGAVATDDGRCSVIGMNVLREGGNAIDASVAAALCLGV
VSPASSGIGGGAFTLIKLANGEEIAYDSRETAPLSATENMYGGNVELKKKGALSVGVPGEVAGLFTAWKQ
HGKLPWKRLVRPAEKLAAEGFKISKYLYMQMNATRSDILADKGLSDLFVSNGELKKPGTICHNPKLALTL
RLIGEYGPKAFYNGTVGVNLVRDIQKSGGIITLKDLQSYRVKVKEPLSADILGYRVLGMPPPSSGGAAMM
LILNILAQYGIPSGVSGPLGVHRLIEALKHAFAVRMNLGDPDFVDVTKVVSDMLSPKFAQDLKSKINDNK
TFDPKHYGGRWNQIDDHGTSHLSIIDSERNAVSMTSTINGYFGALMLSPSTGIVLNNEMDDFSIPMKSGG
NLDVPPPAPANFIRPGKRPLSSMTPTIVLKDGKVKAAVGASGGANIIAGTTEVYLNHFFLKMDPLSSVLA
PRIYHQLIPNRASYENWTTVYNDHFEIPKATRVVLEKKGHVLSPIAGGTIAQFIVQESGENSGGRSELVA
VSDPRKGGFPSGY
>gnl|CDD|177850 PLN02199, PLN02199, shikimate kinase
MEAAITQRIQYPSWVDCRKVECKPQRGSLRYSQQVKVDRRFRGLSLARLQPERRNDQRRAVSPAVSCSDN
NSSALLETGSVYPFDEDILKRKAEEVKPYLNGRSMYLVGMMGSGKTTVGKLMSKVLGYTFFDCDTLIEQA
MNGTSVAEIFVHHGENFFRGKETDALKKLSSRYQVVVSTGGGAVIRPINWKYMHKGISIWLDVPLEALAH
RIAAVGTDSRPLLHDESGDAYSVAFKRLSAIWDERGEAYTNANARVSLENIAAKRGYKNVSDLTPTEIAI
EAFEQVLSFLEKEETMEIPDGDL
>gnl|CDD|215125 PLN02200, PLN02200, adenylate kinase family protein
MFMSSSKPLKLSQAASGLKIWESFSTEIITLEERGSSSKEKTPFITFVLGGPGSGKGTQCEKIVETFGFK
HLSAGDLLRREIASNSEHGAMILNTIKEGKIVPSEVTVKLIQKEMESSDNNKFLIDGFPRTEENRIAFER
IIGAEPNVVLFFDCPEEEMVKRVLNRNQGRVDDNIDTIKKRLKVFNALNLPVIDYYSKKGKLYTINAVGT
VDEIFEQVRPIFAACEAMKESSHV
>gnl|CDD|177852 PLN02201, PLN02201, probable pectinesterase/pectinesterase inhibitor
MSTLIFFLILLTLSLCVSSKEAFSSTDLLQMECLKVPPSEFVSSLKTTVDVIRKVVSIVSQFDKVFGDSR
LSNAISDCLDLLDFAAEELSWSISASQNPNGKDNSTGDVGSDLRTWLSAALSNQDTCIEGFDGTNGIVKK
LVAGSLSQVGSTVRELLTMVHPPPSKGKSKPIGGGTMTKKHSGSSKFPSWVKPEDRKLLQTNGVTPDVVV
AADGTGNFTTIMDAVLAAPDYSTKRYVIYIKKGVYLENVEIKKKKWNIMMVGDGIDATVITGNRSFIDGW
TTFRSATFAVSGRGFIARDITFQNTAGPEKHQAVALRSDSDLSVFYRCAMRGYQDTLYTHTMRQFYRECR
ITGTVDFIFGDATAVFQNCQILAKKGLPNQKNTITAQGRKDPNQPTGFSIQFSNISADTDLLPYLNTTAT
YLGRPWKLYSRTVFMQNYMSDAIRPEGWLEWNGNFALDTLYYGEYMNYGPGAGLGRRVKWPGYHVLNNSA
QANNFTVSQFIQGNLWLPSTGVTFSAGLVV
>gnl|CDD|177853 PLN02202, PLN02202, carbonate dehydratase
MKIMMMIKLCFFAIALICIAPADAQTEGVVFGYKGKNGPNQWGHLNPHFTKCAVGKLQSPIDIQRRQIFY
NHKLESIHRDYYFTNATLVNHVCNVAMFFGEGAGDVIIDNKNYTLLQMHWHTPSEHHLHGVQYAAELHMV
HQAKDGSFAVVASLFKIGTEEPFLSQMKDKLVKLKEERFKGNHTAQVEVGKIDTRHIERKTRKYFRYIGS
LTTPPCSENVSWTILGKVRSMSKEQVELLRSPLDKSFKNNSRPCQPLNGRRVEMFHDHERVDKKDTGNKK
KKPN
>gnl|CDD|165847 PLN02203, PLN02203, aldehyde dehydrogenase
EEAPGETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGV
LTKSANLALSNLKKWMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVV
LKPSELAPATSAFLAANIPKYLDSKAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTP
VALELGGKCPCIVDSLSSSRDTKVAVNRIVGGKWGSCAGQACIAIDYVLVEERFAPILIELLKSTIKKFF
GENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGP
LLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACDSLPFGGVGES
GFGRYHGKYSFDTFSHEKAVLRRSLLTEFEFRYPPWNDFKLGFLRLVYRFDYFGLLLLLLGLKR
>gnl|CDD|215126 PLN02204, PLN02204, diacylglycerol kinase
MEEGRDDEHISFSLSGDRSVLSSCLFLDHVGDVSLTLNSDGLSWKCLDSSDNDGTTCLGIKFCEKSETEI
KFSDVYAVEFINYGLIHSPKLSHAKGCFRERLSETQEMYRFTVHGFQRSRKEPCLWVLAVYTFGHKDLQT
CQSWVDRLNASLNKEVGRPKNLLVFVHPLSGKGSGSRTWETVSPIFIRAKVKTKVIVTERAGHAFDVMAS
ISNKELKSYDGVIAVGGDGFFNEILNGYLLSRLKVPYPPSPSDSVHSVQSRGSSSVHEPNETVHECDNED
HSPLLSDSVQEVMNFRTENGSCEGDQDSDFPFPNERFRFGIIPAGSTDAIVMCTTGERDPVTSALHIILG
RRVCLDIAQVVRWKTTSTSEIEPYVRYAASFAGYGFYGDVISESEKYRWMGPKRYDYAGTKVFLKHRSYE
AEVAYLETESEKSKASSEARKRTGPKKSEKIVCRTNCSVCNTKVSTNSPSTTPNSCPEETRWLRSKGRFL
SVGAAIISNRNERAPDGLVADAHLSDGFLHLILIKDCPHPLYLWHLTQLAKRGGEPLNFEFVEHHKTPAF
TFTSFGDESVWNLDGEIFQAHQLSAQVFRGLVNLFASGPEV
>gnl|CDD|177855 PLN02205, PLN02205, alpha,alpha-trehalose-phosphate synthase [UDP-forming]
MVSRSYSNLLELASGESPSFGRMNRRIPRIMTVAGIMSDIDDDPSESVCSDPSSSSVPKDRIIIVANQLP
IRAQRKSDGSKGWIFSWDENSLLLQLKDGLGDDEIEVIYVGCLKEEIHLNEQEEVSQILLETFKCVPTFL
PPDLFTRYYHGFCKQQLWPLFHYMLPLSPDLGGRFNRSLWQAYVSVNKIFADRIMEVINPEDDFVWIHDY
HLMVLPTFLRKRFNRVKLGFFLHSPFPSSEIYKTLPIREELLRALLNSDLIGFHTFDYARHFLSCCSRML
GLSYESKRGYIGLEYYGRTVSIKILPVGIHMGQLQSVLSLPETEAKVKELIKQFCDQDRIMLLGVDDMDI
FKGISLKLLAMEQLLMQHPEWQGKVVLVQIANPARGKGKDVKEVQAETHSTVKRINETFGKPGYDPIVLI
DAPLKFYERVAYYVVAECCLVTAVRDGMNLIPYEYIISRQGNEKLDKLLGLEPSTPKKSMLVVSEFIGCS
PSLSGAIRVNPWNIDAVADAMDSALEMAEPEKQLRHEKHYRYVSTHDVGYWARSFLQDLERTCRDHSRRR
CWGIGFGLSFRVVALDPNFRKLSMEHIVSAYKRTTTRAILLDYDGTLMPQASIDKSPSSKSIDILNTLCR
DKNNMVFIVSARSRKTLADWFSPCEKLGIAAEHGYFLRLKRDVEWETCVPVADCSWKQIAEPVMQLYTET
TDGSTIEDKETALVWCYEDADPDFGSCQAKELLDHLESVLANEPVTVKSGQNIVEVKPQGVSKGLVAKRL
LSIMQERGMLPDFVLCIGDDRSDEDMFEVITSSMAGPSIAPRAEVFACTVGQKPSKAKYYLDDTAEIVRL
MQGLASVSEQILPE
>gnl|CDD|177856 PLN02206, PLN02206, UDP-glucuronate decarboxylase
MASELINRRHEETQPTADAYYPKPIKPWFVVTRPIRYMLREQRLVFVLVGIAIATLVFTIFPSSSQPSPY
SVDPLSGYGIRPDESYVPAIQAQRKPSLEYLNRIGNSGGKIPLGLKRKGLRVVVTGGAGFVGSHLVDRLM
ARGDSVIVVDNFFTGRKENVMHHFSNPNFELIRHDVVEPILLEVDQIYHLACPASPVHYKFNPVKTIKTN
VVGTLNMLGLAKRVGARFLLTSTSEVYGDPLQHPQVETYWGNVNPIGVRSCYDEGKRTAETLTMDYHRGA
NVEVRIARIFNTYGPRMCIDDGRVVSNFVAQALRKEPLTVYGDGKQTRSFQFVSDLVEGLMRLMEGEHVG
PFNLGNPGEFTMLELAKVVQETIDPNAKIEFRPNTEDDPHKRKPDITKAKELLGWEPKVSLRQGLPLMVK
DFRQRVFGDQKEGSSTTATSTS
>gnl|CDD|177857 PLN02207, PLN02207, UDP-glycosyltransferase
MRNAELIFIPTPTVGHLVPFLEFARRLIEQDDRIRITILLMKLQGQSHLDTYVKSIASSQPFVRFIDVPE
LEEKPTLGGTQSVEAYVYDVIEKNIPLVRNIVMDILSSLALDGVKVKGFVADFFCLPMIDVAKDVSLPFY
VFLTTNSGFLAMMQYLADRHSKDTSVFVRNSEEMLSIPGFVNPVPANVLPSALFVEDGYDAYVKLAILFT
KANGILVNSSFDIEPYSVNHFLDEQNYPSVYAVGPIFDLKAQPHPEQDLARRDELMKWLDDQPEASVVFL
CFGSMGRLRGPLVKEIAHGLELCQYRFLWSLRTEEVTNDDLLPEGFLDRVSGRGMICGWSPQVEILAHKA
VGGFVSHCGWNSIVESLWFGVPIVTWPMYAEQQLNAFLMVKELKLAVELKLDYRVHSDEIVNANEIETAI
RCVMNKDNNVVRKRVMDISQMIQRATKNGGSSFAAIEKFIHDVIGIKT
>gnl|CDD|177858 PLN02208, PLN02208, glycosyltransferase family protein
MEPKFHAFMFPWFAFGHMIPFLHLANKLAEKGHRVTFLLPKKAQKQLEHHNLFPDSIVFHPLTIPPVNGL
PAGAETTSDIPISMDNLLSEALDLTRDQVEAAVRALRPDLIFFDFAQWIPEMAKEHMIKSVSYIIVSATT
IAHTHVPGGKLGVPPPGYPSSKVLFRENDAHALATLSIFYKRLYHQITTGLKSCDVIALRTCKEIEGKFC
DYISRQYHKKVLLTGPMFPEPDTSKPLEEQWSHFLSGFPPKSVVFCSLGSQIILEKDQFQELCLGMELTG
LPFLIAVKPPRGSSTVQEGLPEGFEERVKGRGVVWGGWVQQPLILDHPSIGCFVNHCGPGTIWESLVSDC
QMVLIPFLSDQVLFTRLMTEEFEVSVEVSREKTGWFSKESLSNAIKSVMDKDSDLGKLVRSNHTKLKEIL
VSPGLLTGYVDKFVEELQEYLI
>gnl|CDD|177859 PLN02209, PLN02209, serine carboxypeptidase
MSLILKFMLLILLVSSHHVRSGSIVKFLPGFKGPLPFELETGYIGIGEEENVQFFYYFIKSDKNPQEDPL
IIWLNGGPGCSCLSGLFFENGPLALKNKVYNGSVPSLVSTTYSWTKTANIIFLDQPVGSGFSYSKTPIER
TSDTSEVKKIHEFLQKWLIKHPQFLSNPFYVVGDSYSGMIVPALVHEISKGNYICCNPPINLQGYVLGNP
ITHIEFEQNFRIPYAHGMSLISDELYESLKRICKGNYFSVDPSNKKCLKLVEEYHKCTDNINSHHTLIAN
CDDSNTQHISPDCYYYPYHLVECWANNESVREALHVDKGSIGEWIRDHRGIPYKSDIRSSIPYHMNNSIN
GYRSLIFSGDHDITMPFQATQAWIKSLNYSIIDDWRPWMIKGQIAGYTRTYSNKMTFATVKGGGHTAEYL
PEESSIMFQRWISGQPL
>gnl|CDD|215127 PLN02210, PLN02210, UDP-glucosyl transferase
MGSSEGQETHVLMVTLAFQGHINPMLKLAKHLSLSSKNLHFTLATTEQARDLLSTVEKPRRPVDLVFFSD
GLPKDDPRAPETLLKSLNKVGAKNLSKIIEEKRYSCIISSPFTPWVPAVAAAHNIPCAILWIQACGAYSV
YYRYYMKTNSFPDLEDLNQTVELPALPLLEVRDLPSFMLPSGGAHFNNLMAEFADCLRYVKWVLVNSFYE
LESEIIESMADLKPVIPIGPLVSPFLLGDDEEETLDGKNLDMCKSDDCCMEWLDKQARSSVVYISFGSML
ESLENQVETIAKALKNRGVPFLWVIRPKEKAQNVQVLQEMVKEGQGVVLEWSPQEKILSHMAISCFVTHC
GWNSTIETVVAGVPVVAYPSWTDQPIDARLLVDVFGIGVRMRNDAVDGELKVEEVERCIEAVTEGPAAAD
IRRRAAELKHVARLALAPGGSSARNLDLFISDITIA
>gnl|CDD|215128 PLN02211, PLN02211, methyl indole-3-acetate methyltransferase
MAEENGEEVTDMKPNRQPPHFVLIHGISGGSWCWYKIRCLMENSGYKVTCIDLKSAGIDQSDADSVTTFD
EYNKPLIDFLSSLPENEKVILVGHSAGGLSVTQAIHRFPKKICLAVYVAATMLKLGFQTDEDMKDGVPDL
SEFGDVYELGFGLGPDQPPTSAIIKKEFRRKILYQMSPQEDSTLAAMLLRPGPILALRSARFEEETGDID
KVPRVYIKTLHDHVVKPEQQEAMIKRWPPSQVYELESDHSPFFSTPFLLFGLLIKAAASVGCH
>gnl|CDD|165857 PLN02213, PLN02213, sinapoylglucose-malate O-sinapoyltransferase/ carboxypeptidase
MANIIFLDQPVGSGFSYSKTPIDKTGDISEVKRTHEFLQKWLSRHPQYFSNPLYVVGDSYSGMIVPALVQ
EISQGNYICCEPPINLQGYMLGNPVTYMDFEQNFRIPYAYGMGLISDEIYEPMKRICNGNYYNVDPSNTQ
CLKLTEEYHKCTAKINIHHILTPDCDVTNVTSPDCYYYPYHLIECWANDESVREALHIEKGSKGKWARCN
RTIPYNHDIVSSIPYHMNNSISGYRSLIYSGDHDIAVPFLATQAWIRSLNYSPIHNWRPWMINNQIAGYT
RAYSNKMTFATIKAGGHTAEYRPNETFIMFQRWISGQPL
>gnl|CDD|177862 PLN02214, PLN02214, cinnamoyl-CoA reductase
MPVDVASPAGKTVCVTGAGGYIASWIVKILLERGYTVKGTVRNPDDPKNTHLRELEGGKERLILCKADLQ
DYEALKAAIDGCDGVFHTASPVTDDPEQMVEPAVNGAKFVINAAAEAKVKRVVITSSIGAVYMDPNRDPE
AVVDESCWSDLDFCKNTKNWYCYGKMVAEQAAWETAKEKGVDLVVLNPVLVLGPPLQPTINASLYHVLKY
LTGSAKTYANLTQAYVDVRDVALAHVLVYEAPSASGRYLLAESARHRGEVVEILAKLFPEYPLPTKCKDE
KNPRAKPYKFTNQKIKDLGLEFTSTKQSLYDTVKSLQEKGHLAPPPPSSSQESLENGIKIGS
>gnl|CDD|215129 PLN02216, PLN02216, protein SRG1
MEAKGATQWSSIIVPSVQEMVKEKMITTVPPRYVRSDQDKTEIAVDSGLSSEIPIIDMKRLCSSTAMDSE
VEKLDFACKEWGFFQLVNHGIDSSFLDKVKSEIQDFFNLPMEEKKKLWQRPGEIEGFGQAFVVSEDQKLD
WADMFFLTMQPVRLRKPHLFPKLPLPFRDTLETYSAEVKSIAKILFAKMASALEIKPEEMEKLFDDDLGQ
SIRMNYYPPCPQPDQVIGLTPHSDAVGLTILLQVNEVEGLQIKKDGKWVSVKPLPNALVVNVGDILEIIT
NGTYRSIEHRGVVNSEKERLSVATFHNTGMGKEIGPAKSLVERQKAALFKSLTTKEYFDGLFSRELDGKA
YLDAMRI
>gnl|CDD|215130 PLN02217, PLN02217, probable pectinesterase/pectinesterase inhibitor
MSYGYDDDAKRKKRYVIISISSVLLISMVVAVTIGVSVNKSDNEGKGEITTSVKAIKDVCAPTDYKETCE
DTLRKDAKNTSDPLELVKTAFNATMKQISDVAKKSQTMIELQKDPRTKMALDQCKELMDYAIGELSKSFE
ELGKFEFHKVDEALIKLRIWLSATISHEQTCLDGFQGTQGNAGETIKKALKTAVQLTHNGLAMVSEMSNY
LGQMQIPEMNSRRLLSQEFPSWMDQRARRLLNAPMSEVKPDIVVAQDGSGQYKTINEALNFVPKKKNTTF
VVHIKAGIYKEYVQVNRSMTHLVFIGDGPDKTVISGSKSYKDGITTYKTATVAIVGDHFIAKNIGFENTA
GAIKHQAVAIRVLSDESIFYNCKFDGYQDTLYAHSHRQFYRDCTISGTIDFLFGDAAAVFQNCTLLVRKP
LLNQACPITAHGRKDPRESTGFVLQGCTIVGEPDYLAVKETSKAYLGRPWKEYSRTIIMNTFIPDFVPPE
GWQPWLGDFGLNTLFYSEVQNTGPGAAITKRVTWPGIKKLSDEEILKFTPAQYIQGDAWIPGKGVPYIPG
LFAGNPGSTNSTPTGSAASSNTTFSSDSPSTVVAPSTSPPAGHLGSPPATPSKIVSPSTSPPASHLGSPS
TTPSSPESSIKVASTETASPESSIKVASTESSVSMVSMST
>gnl|CDD|177865 PLN02218, PLN02218, polygalacturonase ADPG
MARCCRLVTVFLLWALLMFSWCKASRISPNGYDHSYKRFKSDSLIKRNDDITGLRSFVRASLRTPTTVSV
SDFGAKGDGKTDDTQAFVNAWKKACSSNGAVNLLVPKGNTYLLKSIQLTGPCKSIRTVQIFGTLSASQKR
SDYKDISKWIMFDGVNNLSVDGGSTGVVDGNGETWWQNSCKRNKAKPCTKAPTALTFYNSKSLIVKNLRV
RNAQQIQISIEKCSNVQVSNVVVTAPADSPNTDGIHITNTQNIRVSNSIIGTGDDCISIESGSQNVQIND
ITCGPGHGISIGSLGDDNSKAFVSGVTVDGAKLSGTDNGVRIKTYQGGSGTASNIIFQNIQMENVKNPII
IDQDYCDKSKCTSQQSAVQVKNVVYRNISGTSASDVAITFNCSKNYPCQGIVLDNVNIKGGKATCTNANV
VDKGAVSPQCN
>gnl|CDD|165863 PLN02219, PLN02219, probable galactinol--sucrose galactosyltransferase 2
MTVTPKISINNGNLVVQGKTILTGVPDNIVLTPGSGNGFVAGAFIGATASHSKSLHVFPVGVLEGLRFMC
CFRFKLWWMTQRMGSCGKDIPLETQFMLLESKDEVEGGNGDDAPTIYTVFLPLLEGQFRAVLQGNDKNEI
EICLESGDKAVETNQGLHLVYMHAGTNPFEVIRQAVKAVEKHMQTFLHREKKKLPSFLDWFGWCTWDAFY
TDVTAEGVDEGLKSLSEGGTPPKFLIIDDGWQQIENKEKDENCVVQEGAQFATRLTGIKENAKFQKNDQK
NEQVSGLKHVVDDAKQRHNVKQVYVWHALAGYWGGVKPAAAGMEHYDSALAYPVQSPGVLGNQPDIVMDS
LSVHGLGLVNPKKVFNFYNELHAYLASCGVDGVKVDVQNIIETLGAGHGGRVSLTRSYQQALEASIARNF
TDNGCISCMCHNTDGLYSAKQTAVVRASDDFYPRDPASHTIHISSVAYNTLFLGEFMQPDWDMFHSLHPA
AEYHGAARAVGGCAIYVSDKPGNHNFDLLRKLVLPDGSVLRAQLPGRPTRDCLFADPARDGTSLLKIWNV
NKCTGVVGVFNCQGAGWCKIEKKTRIHDTSPGTLTGSVCADDVDQIAQVAGEDWSGDSVVYAYKSGEVVR
LPKGASIPVTLKVLEYELFHFCPLKEIATNISFAPIGLLDMFNSGGAVEQFEIHMVSDKAPELFDGEISS
ELSTSLSENRSPTATIALSVRGCGRFGAYSSQRPLKCAVGSTETDFTYDAEVGLLTLTLPVTEEEMYRWH
VEIQV
>gnl|CDD|177866 PLN02220, PLN02220, delta-9 acyl-lipid desaturase
MSDTTKDDGSSQSKAVRKEKRAFFFRKWTRLDVVRASAVGTVHFLCLLAPFNYKWEALRFGLILYIVTGL
SITFSYHRNLAHRSFKLPKWLEYPFAYSALFALQGDPIDWVSTHRFHHQFTDSDRDPHSPIEGFWFSHVL
WIFDTSYIREKCGGRDNVMDLKQQWFYRFLRKTIGLHILMFWTLLYLWGGLPYLTWGVGVGGAIGYHVTW
LINSACHIWGSRTWKTKDTSRNVWWLSLFTMGESWHNNHHAFESSARQGLEWWQIDITWYLIRFFEVLGL
ATDVKLPTEAQKRKMAIVR
>gnl|CDD|177867 PLN02221, PLN02221, asparaginyl-tRNA synthetase
MGDEIVPPANQLAAVSLENDGSTVQKAQFSDRVLIRSILDRPDGGAGLAGQKVRIGGWVKTGREQGKGTF
AFLEVNDGSCPANLQVMVDSSLYDLSTLVATGTCVTVDGVLKVPPEGKGTKQKIELSVEKVIDVGTVDPT
KYPLPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDCEGAGEMF
QVTTLINYTERLEQDLIDNPPPTEADVEAARLIVKERGEVVAQLKAAKASKEEITAAVAELKIAKESLAH
IEERSKLKPGLPKKDGKIDYSKDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEF
WMVEPEIAFADLEDDMNCAEAYVKYMCKWLLDKCFDDMELMAKNFDSGCIDRLRMVASTPFGRITYTEAI
ELLEEAVAKGKEFDNNVEWGIDLASEHERYLTEVLFQKPLIVYNYPKGIKAFYMRLNDDEKTVAAMDVLV
PKVGELIGGSQREERYDVIKQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDV
IPFPRYPGKADL
>gnl|CDD|177868 PLN02222, PLN02222, phosphoinositide phospholipase C 2
MSKQTYKVCFCFRRRFRYTASEAPREIKTIFEKYSENGVMTVDHLHRFLIDVQKQDKATREDAQSIINSA
SSLLHRNGLHLDAFFKYLFGDNNPPLALHEVHHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDAL
KKGVRVIELDIWPNSDKDDIDVLHGMTLTTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHLTPDLQSKVA
EMVTEIFGEILFTPPVGESLKEFPSPNSLKKRIIISTKPPKEYKEGKDDEVVQKGKDLGDEEVWGREVPS
FIQRNKSVDKNDSNGDDDDDDDDGEDKSKKNAPPQYKHLIAIHAGKPKGGITECLKVDPDKVRRLSLSEE
QLEKAAEKYAKQIVRFTQHNLLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRAN
GGCGYIKKPDLLLKSGSDSDIFDPKATLPVKTTLRVTIYMGEGWYFDFRHTHFDQYSPPDFYTRVGIAGV
PGDTVMKKTKTLEDNWIPAWDEVFEFPLTVPELALLRLEVHEYDMSEKDDFGGQTCLPVWELSQGIRAFP
LHSRKGEKYKSVKLLVKVEFV
>gnl|CDD|165867 PLN02223, PLN02223, phosphoinositide phospholipase C
MLLRKKFEMHPANQPDLILNFFGNEFHGYDDDMPELLPRFIELLDTEKDEDGAGLNAAEKIAAELKRRKC
DILAFRNLRCLELDHLNEFLFSTELNPPIGDQVRHHDMHAPLSHYFIHTSLKSYFTGNNVFGKLYSIEPI
IDALEQGVRVVELDLLPDGKDGICVRPKWNFEKPLELQECLDAIKEHAFTKCRSYPLIITFKDGLKPDLQ
SKATQMIDQTFGDMVYHEDPQHSLEEFPSPAELQNKILISRRPPKELLYAKADDGGVGVRNELEIQEGPA
DKNYQSLVGFHAVEPRGMLQKALTGKADDIQQPGWYERDIISFTQKKFLRTRPKKKNLLINAPYKPQRAW
MHGAQLIALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNAGPSGVFYPTENPVVVKILKVKIYMGDG
WIVDFKKRIGRLSKPDLYVRISIAGVPHDEKIMKTTVKNNEWKPTWGEEFTFPLTYPDLALISFEVYDYE
VSTADAFCGQTCLPVSELIEGIRAVPLYDERGKACSSTMLLTRFKWS
>gnl|CDD|177869 PLN02224, PLN02224, methionine-tRNA ligase
MAARINTSLHNALSFLKAFNTPLNTKPFSFCRNCFRFSKKLPYYSQFSSGKRALYCTSSSQESTVDEADT
FVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDII
SQSYRTLWKDLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKELLENNC
CPVHQMPCVARKEDNYFFALSKYQKPLEDILAQNPRFVQPSYRLNEVQSWIKSGLRDFSISRALVDWGIP
VPDDDKQTIYVWFDALLGYISALTEDNKQQNLETAVSFGWPASLHLIGKDILRFHAVYWPAMLMSAGLEL
PKMVFGHGFLTKDGMKMGKSLGNTLEPFELVQKFGPDAVRYFFLREVEFGNDGDYSEDRFIKIVNAHLAN
TIGNLLNRTLGLLKKNCESTLVEDSTVAAEGVPLKDTVEKLVEKAQTNYENLSLSSACEAVLEIGNAGNT
YMDQRAPWFLFKQGGVSAEEAAKDLVIILEVMRVIAVALSPIAPCLSLRIYSQLGYSEDQFNSITWSDTK
WGGLKGGQVMEQASPVFARIELNPEKEEDEKKPKVGKKTGKAKVKVVEQTPTVAEA
>gnl|CDD|177870 PLN02225, PLN02225, 1-deoxy-D-xylulose-5-phosphate synthase
MGSASIGYQFGISARFYGNFNLSSDITVSSLPCKLDVSIKSLFSAPSSTHKECSNRARVCCSLPNTDEYC
DEKFETPILDSIETPLQLKNLSVKELKLLADEIRTELHSVLWKKTQKSMNPSFAAIELTLALHYVFRAPV
DNILWDAVEQTYAHKVLTRRWSAIPSRQKNGISGVTSQLESEYDSFGTGHGCNSISAGLGLAVARDIKGK
RDRVVAVIDNATITAGQAYEAMSNAGYLDSNMIVILNDSRHSLHPNMEEGSKASISALSSIMSKIQSSKI
FRKFRELAKAMTKRIGKGMYEWAAKVDEYARGMVGPTGSTLFEELGLYYIGPVDGHNIEDLVCVLREVSS
LDSMGPVLVHVITEENRDAETGKNIMVKDRRTYSDCFVEALVMEAEKDRDIVVVHAGMEMDASLITFQER
FPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPSAFLQRAYDQVVHDVDRQRKAVRFVITSAGLVGSDG
PVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAYVTDRPVCFRFPRGSIVNMNYLVPTGLPIEIGR
GRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHKFLITVEEGCV
GGFGSHVAQFIALDGQLDGNIKWRPIVLPDGYIEEASPREQLALAGLTGHHIAATALSLLGRTREALLLM
S
>gnl|CDD|177871 PLN02226, PLN02226, 2-oxoglutarate dehydrogenase E2 component
MMLRAVIRRASTRGSSPSLFGKSLQSSRVAASSPSLLSGSETGALLHRGNHAHSFHNLALPGNSGISRSA
SLVSSTLQRWVRPFSSESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASP
ASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQVTPSQKIPETTDPKPSPPAEDKQKPKVESAPVAEKP
KAPSSPPPPKQSAKEPQLPPKERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKD
AFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNF
AEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSV
VPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI
>gnl|CDD|177872 PLN02227, PLN02227, fructose-bisphosphate aldolase I
MASSTATMLKASPVKSDWVKGQSLLLRQPSSVSAIRSHVAPSALTVRAASAYADELVKTAKTIASPGHGI
MAMDESNATCGKRLASIGLENTEANRQAYRTLLVSAPGLGQYISGAILFEETLYQSTTDGKKMVDVLVEQ
NIVPGIKVDKGLVPLVGSYDESWCQGLDGLASRTAAYYQQGARFAKWRTVVSIPNGPSALAVKEAAWGLA
RYAAISQDSGLVPIVEPEIMLDGEHGIDRTYDVAEKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAEATD
RATPEQVASYTLKLLRNRIPPAVPGIMFLSGGQSELEATLNLNAMNQAPNPWHVSFSYARALQNTCLKTW
GGKEENVKAAQDILLARAKANSLAQLGKYTGEGESEEAKEGMFVKGYTY
>gnl|CDD|177873 PLN02228, PLN02228, Phosphoinositide phospholipase C
MSESFKVCFCCSRSFKEKTREPPVSIKRLFEAYSRNGKMSFDELLRFVSEVQGERHAGLDYVQDIFHSVK
HHNVFHHHGLVHLNAFYRYLFSDTNSPLPMSGQVHHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIV
QALRKGVKVIELDLWPNPSGNAAEVRHGRTLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHLPPNLQA
QVAKMLTKTFRGMLFRCTSESTKHFPSPEELKNKILISTKPPKEYLESKTVQTTRTPTVKETSWKRVADA
ENKILEEYKDEESEAVGYRDLIAIHAANCKDPLKDCLSDDPEKPIRVSMDEQWLETMVRTRGTDLVRFTQ
RNLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGHGKQLWIMQGMFRANGGCGYVKKPRILLDEHTL
FDPCKRLPIKTTLKVKIYTGEGWDLDFHLTHFDQYSPPDFFVKIGIAGVPRDTVSYRTETAVDQWFPIWG
NDEFLFQLRVPELALLWFKVQDYDNDTQNDFAGQTCLPLPELKSGVRAVRLHDRAGKAYKNTRLLVSFAL
DPPYTFR
>gnl|CDD|177874 PLN02229, PLN02229, alpha-galactosidase
KMKDSVLFLVVLLLSLSVLVSQSIAGRVKAPLLQSVFSKSFNSIYDTSMYGRLQLNNGLARTPQMGWNSW
NFFACNINETVIKETADALVSTGLADLGYIHVNIDDCWSNLKRDSKGQLVPDPKTFPSGIKLLADYVHSK
GLKLGIYSDAGVFTCQVRPGSLFHEVDDADIFASWGVDYLKYDNCYNLGIKPIERYPPMRDALNATGRSI
FYSLCEWGVDDPALWAGKVGNSWRTTDDINDTWASMTTIADLNNKWAAYAGPGGWNDPDMLEVGNGGMTY
EEYRGHFSIWALMKAPLLIGCDVRNMTAETMEILSNKEVIAVNQDPLGVQGRKIQANGKNGCQQVWAGPL
SGDRLVVALWNRCSEPATITASWDVIGLESSISVSVRDLWKHKDLSENVVGSFGAQVDAHDCHMYIFTPQ
TVSHSDV
>gnl|CDD|177875 PLN02230, PLN02230, phosphoinositide phospholipase C 4
MEGKKEMGSYKFCLIFTRKFRMTESGPVADVRDLFEKYADGDAHMSPEQLQKLMAEEGGGEGETSLEEAE
RIVDEVLRRKHHIAKFTRRNLTLDDFNYYLFSTDLNPPIADQVHQNMDAPLSHYFIFTGHNSYLTGNQLS
SNCSELPIADALRRGVRVVELDLWPRGTDDVCVKHGRTLTKEVKLGKCLDSIKANAFAISKYPVIITLED
HLTPKLQFKVAKMITQTFGDMLYYHDSEGCQEFPSPEELKEKILISTKPPKEYLEANDAKEKDNGEKGKD
SDEDVWGKEPEDLISTQSDLDKVTSSVNDLNQDDEERGSCESDTSCQLQAPEYKRLIAIHAGKPKGGLRM
ALKVDPNKIRRLSLSEQLLEKAVASYGADVIRFTQKNFLRIYPKGTRFNSSNYKPQIGWMSGAQMIAFNM
QGYGRALWLMEGMFRANGGCGYVKKPDFLMDAGPNGQDFYPKDNSCPKKTLKVKVCMGDGWLLDFKKTHF
DSYSPPDFFVRVGIAGAPVDEVMEKTKIEYDTWTPIWNKEFIFPLAVPELALLRVEVHEHDINEKDDFGG
QTCLPVSEIRQGIHAVPLFNRKGVKYSSTRLLMRFEFV
>gnl|CDD|177876 PLN02231, PLN02231, alanine transaminase
MRRFLINQAKGLVDHSRRQHHKSPSFLSPQPRPLASLSRFSSTSEMSASDSTSSLPVTLDTINPKVLKCE
YAVRGEIVTIAQRLQEELKTNPGSYPFDEILYCNIGNPQSLGQQPITFFREVLALCDHPSLLDKSETHGL
FSADAIERAWQILDQIPGRATGAYSHSQGIKGLRDAIAAGIEARDGFPADPNDIFLTDGASPAVHMMMQL
LIRSEKDGILCPIPQYPLYSASIALHGGTLVPYYLDEATGWGLEISELKKQLEDARSKGITVRALVVINP
GNPTGQVLAEENQRDIVEFCKQEGLVLLADEVYQENVYVPDKKFHSFKKVARSMGYGEKDISLVSFQSVS
KGYYGECGKRGGYMEVTGFTSDVREQIYKVASVNLCSNISGQILASLVMSPPKPGDESYESYMAEKDGIL
SSLARRAKTLEDALNSLEGVTCNKAEGAMYLFPRIHLPQKAIKAAEAAKTAPDAFYCKRLLNATGIVVVP
GSGFGQVPGTWHFRCTILPQEDKIPAIVSRLTEFHKSFMDEFRD
>gnl|CDD|165876 PLN02232, PLN02232, ubiquinone biosynthesis methyltransferase
MGLDFSSEQLAVAATRQSLKARSCYKCIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRV
LKPGSRVSILDFNKSNQSVTTFMQGWMIDNVVVPVATVYDLAKEYEYLKYSINGYLTGEELETLALEAGF
SSACHYEISGGFMGNLVAMR
>gnl|CDD|177877 PLN02233, PLN02233, ubiquinone biosynthesis methyltransferase
MALLLGIVSPVTFTGKLAGNSRSRRRDVVKCANERQALFNRIAPVYDNLNDLLSLGQHRIWKRMAVSWSG
AKMGDRVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAASRQELKAKSCYKNIEWIEGDATDLP
FDDCYFDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQPFTTSMQEWMIDNVVVPVATGY
GLAKEYEYLKSSINEYLTGEELEKLALEAGFSSAKHYEISGGLMGNLVATR
>gnl|CDD|177878 PLN02234, PLN02234, 1-deoxy-D-xylulose-5-phosphate synthase
MSYQTQINKFSQMALSVFAFPSYINRNPSLKYLKPSSMSSTKYSKVRATTFSEKGEYYSNRPPTPLLDTI
NHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYP
HKILTGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGA
MTAGQAYEAMNNAGYLHSNMIVILNDNKQVSLPTANLDGPTQPVGALSCALSRLQSNCGMIRETSSTLFE
ELGFHYVGPVDGHNIDDLVSILETLKSTKTIGPVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQF
KNISKTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLAC
EGLKPFCTIYSSFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPS
DEAELFNMVATAAAIDDRPSCFRYHRGNGIGVSLPPGNKGVPLQIGRGRILRDGERVALLGYGSAVQRCL
EAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLDGKLKV
YRTWITNGSTS
>gnl|CDD|177879 PLN02235, PLN02235, ATP citrate (pro-S)-lyase
MARKKIREYDSKRLLKEHLKRLAGIDLPIRSAQVTESTDFNELANKEPWLSSTKLVVKPDMLFGKRGKSG
LVALNLDLAQVATFVKERLGKEVEMGGCKGPITTFIVEPFVPHDQEFYLSIVSDRLGCSISFSECGGIEI
EENWDKVKTIFLPTEAPLTSEICAPLIATLPLEIRGKIEEFIKGVFAVFQDLDFTFLEMNPFTLVDGEPY
PLDMRGELDDTAAFKNFKKWGNIEFPLPFGRVMSPTESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGG
ASVIYADTVGDLGYASELGNYAEYSGAPNEEEVLQYARVVIDCATANPDGRKRALLIGGGIANFTDVAAT
FNGIIRALREKESKLKAARMHIFVRRGGPNYQKGLAKMRALGEEIGVPIEVYGPEATMTGICKQAIDYIT
AAA
>gnl|CDD|177880 PLN02236, PLN02236, choline kinase
MGMVEKTVGLSSGRIPDELKRILHSLASKWGDVVDDEALQVIPLKGAMTNEVFQIKWPTKEGNLGRKVLV
RIYGEGVELFFDRDDEIRTFECMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLRE
FHSLDMPGPKNVLLWDRLRNWLKEAKNLCSPEEAKEFRLDSLEDEINLLEKELSGDDQEIGFCHNDLQYG
NIMIDEETRAITIIDYEYASYNPVAYDIANHFCEMAADYHSETPHILDYSKYPGEEERRRFIRTYLSSSG
EEPSDEEVEQLLDDVEKYTLASHLFWGLWGIISGHVNKIDFDYMEYARQRFEQYWLRKPELLGS
>gnl|CDD|215131 PLN02237, PLN02237, glyceraldehyde-3-phosphate dehydrogenase B
THAALASSRIPATTRLPSKASHKRLEVAEFSGLRASSCVTFAKNAREASFFDVVASQLAPKVAGSTPVRG
ETVAKLKVAINGFGRIGRNFLRCWHGRKDSPLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKIVDDET
ISVDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGADIPTYVVG
VNEDDYDHEVANIVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAAL
NIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEKKGITAEDVNAAFRKAADGPLKGI
LAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNEWGYSQRVVDLAHLVAAKWPGGAAAGS
GDPLEDFCKTNPADEECKVYDA
>gnl|CDD|215132 PLN02238, PLN02238, hypoxanthine phosphoribosyltransferase
PEYEVDIEKVLWTAEDISARVAELAAQIASDYAGKSPVVLGVATGAFMFLADLVRAIQPLPRGLTVDFIR
ASSYGGGTESSGVAKVSGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARR
KVKYELVGDGKEYVGFECPDEFVVGYGLDFAEKYRNLPYVGVLKPEVYQ
>gnl|CDD|177883 PLN02240, PLN02240, UDP-glucose 4-epimerase
MSLMGRTILVTGGAGYIGSHTVLQLLLAGYKVVVIDNLDNSSEEALRRVKELAGDLGDNLVFHKVDLRDK
EALEKVFASTRFDAVIHFAGLKAVGESVAKPLLYYDNNLVGTINLLEVMAKHGCKKLVFSSSATVYGQPE
EVPCTEEFPLSATNPYGRTKLFIEEICRDIHASDPEWKIILLRYFNPVGAHPSGRIGEDPKGIPNNLMPY
VQQVAVGRRPELTVFGNDYPTKDGTGVRDYIHVMDLADGHIAALRKLFTDPDIGCEAYNLGTGKGTSVLE
MVAAFEKASGKKIPLKLAPRRPGDAEEVYASTEKAEKELGWKAKYGIDEMCRDQWNWASKNPYGYGSSPE
TS
>gnl|CDD|215133 PLN02241, PLN02241, glucose-1-phosphate adenylyltransferase
PKSVAAIILGGGAGTRLFPLTKRRAKPAVPIGGNYRLIDIPMSNCINSGINKIYVLTQFNSASLNRHLSR
AYNFGNGGNFGDGFVEVLAATQTPGEKGWFQGTADAVRQFLWLFEDAKNKNVEEVLILSGDHLYRMDYMD
FVQKHRESGADITIACLPVDESRASDFGLMKIDDTGRIIEFSEKPKGDELKAMQVDTTVLGLSPEEAKEK
PYIASMGIYVFKKDVLLKLLRWRFPTANDFGSEIIPGAIKEGYNVQAYLFDGYWEDIGTIKSFYEANLAL
TKQPPKFSFYDPDAPIYTSPRFLPPSKIEDCRITDSIISHGCFLRECKIEHSVVGLRSRIGEGVEIEDTV
MMGADYYETEEEIASLLAEGKVPIGIGENTKIRNAIIDKNARIGKNVVIINKDGVQEADREEEGYYIRSG
IVVILKNAVIPDGTVI
>gnl|CDD|215134 PLN02242, PLN02242, methionine gamma-lyase
GMSEKEKKSPAESKEEDPAAALASARHEFGEHGGVNMSIEASATFTVMEPDTMRRMFSGELGPDRDFYIY
SRHFNPTVLNLGRQMAALEGTEAAYCTASGMSAISSVLLQLCSSGGHVVASNTLYGGTHALLAHFLPRKC
NITTTFVDITDLEAVKKAVVPGKTKVLYFESISNPTLTVADIPELARIAHEKGVTVVVDNTFAPMVLSPA
RLGADVVVHSISKFISGGADIIAGAVCGPAELVNSMMDLHHGALMLLGPTMNPKVAFELSERLPHLSLRM
KEHCRRAMEYAKRMKELGLKVIYPGLEDHPQHALLKSMANKGYGFGGLLCLDMDTEERANRLMRYLQNST
QFGFMAVSLGYYETLMSCSGSSTSSELDPEEKAAAGISPGLVRMSVGYTGTLEQRWSQFEKALSAMKL
>gnl|CDD|177886 PLN02243, PLN02243, S-adenosylmethionine synthase
METFLFTSESVNEGHPDKLCDQISDAVLDACLAQDPDSKVACETCTKTNMVMVFGEITTKAKVDYEKIVR
DTCREIGFVSDDVGLDADKCKVLVNIEQQSPDIAQGVHGHLTKKPEEIGAGDQGHMFGYATDETPELMPL
THVLATKLGARLTEVRKNGTCPWLRPDGKTQVTVEYKNEGGAMVPIRVHTVLISTQHDETVTNDEIAADL
KEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDR
SGAYIVRQAAKSVVAAGLARRCIVQVSYAIGVPEPLSVFVDTYGTGKIPDKEILKIVKENFDFRPGMIAI
NLDLKRGGNGRFQKTAAYGHFGRDDPDFTWEVVKPL
>gnl|CDD|215135 PLN02244, PLN02244, tocopherol O-methyltransferase
SPAAALASRSSSSATTSRSGSRSTRLSRPSSSASGVRRTLARLEDAASPAPAATADLKEGIAEFYDESSG
VWEDVWGEHMHHGYYDPGASRGDHRQAQIRMIEESLAWAGVPDDDEKRPKRIVDVGCGIGGSSRYLARKY
GANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQPFEDGQFDLVWSMESGEHMPDKRKFVQELA
RVAAPGGRIIIVTWCHRDLEPGETSLKPDEQKLLDKICAAYYLPAWCSTSDYVKLAESLGLQDIKTEDWS
EHVAPFWPAVIKSALTLKGLFGLLTSGWATIRGALVMPLMIKGFKKGLIKFAVITCRKPL
>gnl|CDD|215136 PLN02245, PLN02245, ATP phosphoribosyl transferase
LSLLSQSPSLSSLPSSSPLLSPPSSRASRLIAPRRRCLRLATACVSQVQSSVVAGSTDSASSVVSSRTQI
RLGLPSKGRMAEDTLDLLKDCQLSVKKVNPRQYVAEIPQLPNLEVWFQRPKDIVRKLLSGDLDLGIVGYD
MLREYGQGNEDLVIVHDALGFGDCHLSIAIPKYGIFENINSLKELAQMPQWTEERPLRVVTGFTYLGPKF
MKDNGFKHVTFSTADGALEAAPAMGIADAILDLVSSGTTLRENNLKEIEGGVVLESQAVLVASRRALLER
KGALEVVHEILERLEAHLRAEGQFTVTANMRGSSAEEVAERVLSQPSLSGLQGPTISPVYCKRDGKVAVD
YYAIVICVPKKALYESVQQLRKIGGSGVLVSPLTYIFDEETPRWRQLLSNLGL
>gnl|CDD|215137 PLN02246, PLN02246, 4-coumarate--CoA ligase
EASASEEFIFRSKLPDIYIPNHLPLHDYCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKL
GIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLA
EDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQ
QVDGENPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVP
PIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEAGPVLAMCLAFAKEP
FPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIG
YIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEIT
EDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKLAAG
>gnl|CDD|165890 PLN02247, PLN02247, indole-3-acetic acid-amido synthetase
MLPSYDPNDNEAGLKLLEDLTTNACQIQQQVLEEILTQNAGTEYLRSFLDGESDKQSFKNKVPVVNYEDI
KPCIERIANGESSSIISAQPITELLTSSGTSGGQPKLMPSTAEELDRKTFFYNLLVPVMNKYVDGLDQGK
GMYLLFIKPEISTPSGLMARPVLTSYYKSSNFRNRPFNRYNVYTSPDETILCQDSKQSMYCQLLCGLVQR
DEVLRVGAVFASAFLRAIKFLEDHWKELCSNIRTGCVSDWITDPSCRNAVSSILSKPNSELADLIESECS
GKSWEGIIKRLWPRTKYIEVIVTGSMAQYIPTLEFYSGGLPLVSTMYASSECYFGINLKPLSDPSDVSYT
LLPNMAYFEFLPVDKNNGEVIHFVQCNGTDDDDDALKEDLEIVDLVDVKVGHYYELVVTTFTGLYRYRVG
DILMVTGFYNNAPQFRFVQRRNVVLSIDTDKTNEEDLLKAVTQAKLLLEPLGFLLTEYTSYADTSSIPGH
YVLFWELKTRGSNDPPELDPKIMEQCCSTVEESLDSVYRRCRKRDKSIGPLEIRVVKHGTFDALMDFCVS
QGSSVNQYKTPRCIKSEEALKILDSRVIGRFFSKRVPFWEPFGMET
>gnl|CDD|215138 PLN02248, PLN02248, cellulose synthase-like protein
MASSSSKPSRKSLSSSSSSAGPPSNNSSSPQSVKFARRTSSGRYVSLSRDDLDLSGELSSSDYLNYTVHI
PPTPDNQPMAGKAEEQYVSNSIFTGGFNSVTRAHLMDKVIESEVSHPQMAGAKGSSCAMPGCDGKVMRDE
RGEDLLPCECGFKICRDCYIDAVKSGGICPGCKEPYKVTDLDDEVPDESSGALPLPPPGGSKMDRRLSLM
KSNSLLMRSQTGDFDHNRWLFETKGTYGYGNAVWPKDDGYGDDGGGGGPGEFMDKPWRPLTRKVKISAAI
LSPYRLLILIRLVVLGLFLTWRVRNPNEDAMWLWGMSVVCEIWFAFSWLLDQLPKLCPINRATDLAVLKE
KFETPSPSNPTGRSDLPGIDVFVSTADPEKEPPLVTANTILSILAADYPVEKLACYLSDDGGALLTFEAM
AEAASFARIWVPFCRKHDIEPRNPESYFSLKRDPTKNKVRPDFVKDRRRVKREYDEFKVRINGLPDSIRR
RSDAYNAREEIKAKKKQRESGGGDPSEPLKVPKATWMADGTHWPGTWLSSAPDHSRGDHAGIIQVMLKPP
SDEPLMGSADDENLIDFTDVDIRLPMLVYVSREKRPGYDHNKKAGAMNALVRASAIMSNGPFILNLDCDH
YIYNSLAIREGMCFMMDRGGDRICYVQFPQRFEGIDPSDRYANHNTVFFDVNMRALDGLQGPVYVGTGCL
FRRIALYGFDPPRAKEHSGCFGSCKFTKKKKKETSASEPEEQPDLEDDDDLELSLLPKRFGNSTMFAASI
PVAEFQGRPLADHPSVKNGRPPGALTVPREPLDAATVAEAISVISCWYEDKTEWGDRVGWIYGSVTEDVV
TGYRMHNRGWRSVYCVTKRDAFRGTAPINLTDRLHQVLRWATGSVEIFFSRNNALLASRRLKFLQRIAYL
NVGIYPFTSIFLIVYCFLPALSLFSGQFIVQTLNVTFLVYLLIITITLCLLAVLEIKWSGITLEEWWRNE
QFWLIGGTSAHLAAVLQGLLKVIAGIEISFTLTSKSAGDDEDDEFADLYIVKWTSLMIPPITIMMVNLIA
IAVGVSRTIYSEIPQWSKLLGGVFFSFWVLAHLYPFAKGLMGRRGRTPTIVYVWSGLLSITISLLWVAIS
PPSGAAQIGGGFQFP
>gnl|CDD|177891 PLN02249, PLN02249, indole-3-acetic acid-amido synthetase
MAVDSPLQSRMASPTTSEKDVKALKFIEEMTRNPDSVQEKVLGEILSRNSNTEYLKRFDLNGAVDRKTFK
SKVPVVTYEDLKTEIQRISNGDRSPILSSHPITEFLTSSGTSAGERKLMPTIEEDIDRRQLLGSLLMPVM
NLYVPGLDKGKGLYFLFVKSESKTSGGLPARPALTSYYKSDHFRTSDYDNVYTSPNEAILCSDSSQSMYA
QMLCGLLMRHEVLRLGAVFPSGLLRAISFLQNNWKELAQDISTGTLSSKIFDPAIKNRMSKILNKPDQEL
AEFLIGVCSQENWEGIITKIWPNTKYLDVIVTGAMAQYIPMLEYYSGGLPMASTIYASSESYFGINLNPM
CKPSEVSYTIMPNMAYFEFLPHNHDGDGALDETSLVELADVEVGKEYELVITTYAGLYRYRVGDILRVTG
FHNSAPQFKFIRRKNVLLSIESDKTDEADLQKAVENASRLLAEQGTRVIEYTSYAETKTIPGHYVIYWEL
LGRDQSNALPSDEVMAKCCLEMEESLNSVYRQSRVSDKSIGPLEIRVVQNGTFEELMDYAISRGSSINQY
KVPRCVSLTPIMELLDSRVVSAHFSPSLPHWSPERRH
>gnl|CDD|215139 PLN02250, PLN02250, lipid phosphate phosphatase
MPEIQLGAHTIRSHGVKVARTHMHDWLILLLLVVIEVVLNVIEPFHRFVGKDMLTDLSYPLQDNTIPFWA
VPLIAILLPFAVILVYYFIRRDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGKGVF
HPVTTDVLCTGAKSVIKEGHKSFPSGHTSWSFAGLGFLSLYLSGKIRVFDRRGHVAKLCIVFLPLLVAAL
VGVSRVDDYWHHWQDVFAGALIGLTVASFCYLQFFPPPYDIDGWGPHAYFQMLAESRNGAQSSNGINHLS
VQQTELESVYIDSQHGMETSRVNTRDTSPILEGL
>gnl|CDD|215140 PLN02251, PLN02251, pyrophosphate-dependent phosphofructokinase
AAALAVNNGANAAGSSANAPASGRDASVYSEVQSSRIDHALPLPSVLKGPFKIVDGPPSSAAGNPEEIAK
LFPNLFGQPSVMLVPSQADALSSDQKLKIGVVLSGGQAPGGHNVISGIFDYLQEHAKGSVLYGFKGGPAG
IMKCKYVELTAEFIYPYRNQGGFDMICSGRDKIETPEQFKQAEETATKLDLDGLVVIGGDDSNTNACLLA
EYFRAKNLKTRVIGCPKTIDGDLKSKEVPTSFGFDTACKIYSEMIGNVMIDARSTGKYYHFVRLMGRAAS
HITLECALQTHPNITIIGEEVAAKKLTLKNVTDYIVDVICKRAELGYNYGVILIPEGLIDFIPEVQHLIA
ELNEILAHDVVDEEGHWKKKLKPQSLQLFDFLPHAIQEQLMLERDPHGNVQVAKIETEKMLIQMVETELE
KRKQEGSYKGHFKGQSHFFGYEGRCGLPTNFDATYCYALGYGAGALLHSGKTGLISSVGNLAAPVEEWTV
GGTALTSLMDVERRHGKFKPVIKKAMVELEGAPFKKFASLRDEWALKNRYISPGPIQFSGPGSDATNHTL
KLELGAQA
>gnl|CDD|215141 PLN02252, PLN02252, nitrate reductase [NADPH]
MAASVDPPVSGSTRRADAPARALDFLPLLKGPVSSPKVPSDDEDEDDDEDEADYEDLIVKENVEVEPSVV
DPRDEGTPDEWIPRHPSLVRLTGKHPFNCEPPLARLMEHGFITPAPLHYVRNHGAVPRADWDEWTVEVTG
LVKRPARLTMDELVRFPARELPVTLVCAGNRRKEQNMVKQTIGFNWGAAGVSTSVWRGVRLRDVLRRCGV
MSRKGGALNVCFEGAEDLPGGGGSKYGTSITLERAMDPARDVILAYMQNGEPLTPDHGFPVRLIIPGFIG
GRMVKWLKRIIVTTAESDNYYHYRDNRVLPSHVDAELANAEGWWYKPEYIINELNINSVITTPAHDEILP
INASTTQRPYTMKGYAYSGGGRKVTRVEVSLDGGETWRLCDLDHPEKPTKYGKYWCWCFWSLDVEVLDLL
GAKEIAVRAWDESMNTQPEKLIWNLMGMMNNCWFRVKVNVCKPHKGEIGLVFEHPTQPGNQSGGWMAKQK
HLETASAAAPALKKSVSTPFMNTNTGSKQYTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSIL
INAGTDCTEEFDAIHSDKAKKMLEDYRIGELVTTGAAASSSASSHPLSAISTASALAAASPAPGRPVALN
PREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFEL
VIKVYFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVNGKPKFAKKLAMLAGGTGI
TPMYQVIQAILRDPEDKTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQVKREGWKYSVGRV
TEAMLREHLPEGGDETLALMCGPPPMIEFACQPNLEKMGYDKDSILVF
>gnl|CDD|177895 PLN02253, PLN02253, xanthoxin dehydrogenase
MATASSSASSLPSQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVCF
FHCDVTVEDDVSRAVDFTVDKFGTLDIMVNNAGLTGPPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAAR
IMIPLKKGSIVSLCSVASAIGGLGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHL
PEDERTEDALAGFRAFAGKNANLKGVELTVDDVANAVLFLASDEARYISGLNLMIDGGFTCTNHSLRVFR
>gnl|CDD|215142 PLN02254, PLN02254, gibberellin 3-beta-dioxygenase
MPSTLSDAFRSHPLHLNHIIPLDFTSLQTLPDSHVWTPKDDLLFSSAPSPSTTDESIPVIDLSDPNALTL
IGHACETWGVFQVTNHGIPLSLLDDIESQTRRLFSLPAQRKLKAARSPDGVSGYGVARISSFFNKKMWSE
GFTIMGSPLEHARQLWPQDHTKFCDVMEEYQKEMKKLAERLMWLMLGSLGITEEDIKWAGPKSGSQGAQA
ALQLNSYPVCPDPDRAMGLAPHTDSSLLTILYQSNTSGLQVFREGVGWVTVPPVPGSLVVNVGDLLHILS
NGRFPSVLHRAVVNKTRHRISVAYFYGPPSDVQISPLPKLVDPNHPPLYRSVTWKEYLATKAKHFNKALS
LIRNCNPE
>gnl|CDD|215143 PLN02255, PLN02255, H(+) -translocating inorganic pyrophosphatase
MAILSELATEVLIPVAALIGIAFALLQWYLVSRVKVSPDSGASSNGGGGGGGYGDYLIEEEEGLNDHNVV
AKCAEIQNAISEGATSFLFTEYKYVGIFMVIFAAVIFVFLGSVEGFSTKSQPCTYDKGKLCKPALANAAF
STVAFLLGALTSVVSGFLGMKIATYANARTTLEARKGVGKAFITAFRSGAVMGFLLAANGLLVLYIAINL
FKLYYGDDWEGLYEAITGYGLGGSSMALFGRVGGGIYTKAADVGADLVGKVERNIPEDDPRNPAVIADNV
GDNVGDIAGMGSDLFGSYAESSCAALVVASISSFGINHDFTAMCYPLLISSVGIIVCLITTLFATDFFEI
KAVKEIEPALKKQLIISTVLMTVGIAVVSWLALPSSFTIFNFGTQKVVKNWQLFFCVAIGLWAGLIIGFV
TEYYTSNAYSPVQDVADSCRTGAATNVIFGLALGYKSVIIPIFAIAVSIYVSFSLAAMYGIAVAALGMLS
TIATGLAIDAYGPISDNAGGIAEMAGMSHRIRERTDALDAAGNTTAAIGKGFAIGSAALVSLALFGAFVS
RAGISTVDVLTPKVFIGLIVGAMLPYWFSAMTMKSVGSAALKMVEEVRRQFNTIPGLMEGTAKPDYATCV
KISTDASIKEMIPPGALVMLTPLIVGTLFGVETLSGVLAGALVSGVQIAISASNTGGAWDNAKKYIEAGA
SEHARSLGPKGSDPHKAAVIGDTIGDPLKDTSGPSLNILIKLMAVESLVFAPFFAAHGGLLFKWL
>gnl|CDD|215144 PLN02256, PLN02256, arogenate dehydrogenase
RPLSRRPRSLRVRAIDAAQPFDYESRLQEELEKSRKLKIGIVGFGNFGQFLAKTFVKQGHTVLATSRSDY
SDIAAELGVSFFRDPDDFCEEHPDVVLLCTSILSTEAVLRSLPLQRLKRSTLFVDVLSVKEFPKNLLLQV
LPEEFDILCTHPMFGPESGKGGWAGLPFVYDKVRIGDEGEREARCERFLDIFEEEGCRMVEMSCEEHDRY
AAGSQFITHTVGRILGKMELESTPINTKGYETLLRLVENTSSDSFDLYYGLFMYNPNATEELERLELAFD
SVKKQLFGRLHDVLRKQLFEGSPL
>gnl|CDD|177899 PLN02257, PLN02257, phosphoribosylamine--glycine ligase
LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPDLDISDSAAVISFCRKWGVGLVVVGP
EAPLVAGLADDLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPI
VVKADGLAAGKGVVVAMTLEEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESA
QDHKRVGDGDTGPNTGGMGAYSPAPVLTPELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSGL
PKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSGVSLTWSPDSAMVVVMASNGYPGSYKKGTVI
KNLDEAEAVAPGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEARARAYDAVDQIDWPGGFFRRDI
GWRAVARLQVANKR
>gnl|CDD|215145 PLN02258, PLN02258, 9-cis-epoxycarotenoid dioxygenase NCED
SSSSNPTSRSQSHASSSSSSSSQSSPPSSTSPRPRRRKPSASSLLHTPSILPLPKLSSPSPPSVTLPPAA
TTQTPQLNPLQRAAAAALDAVESALVSHLERQHPLPKTADPAVQIAGNFAPVPEQPVRHNLPVTGRIPDC
IDGVYVRNGANPLFEPVAGHHLFDGDGMVHAVRIGNGSASYACRFTETNRLVQERALGRPVFPKAIGELH
GHSGIARLMLFYARGLFGLVDASRGTGVANAGLVYFNGRLLAMSEDDLPYQVRITGDGDLETVGRYDFDG
QLDSSMIAHPKVDPVTGELFALSYDVVKKPYLKYFRFSPDGEKSPDVEIPLDQPTMMHDFAITENFVVIP
DQQVVFKLSEMIRGGSPVVYDKNKTSRFGVLPKNATDASEIQWVEVPDCFCFHLWNAWEEPETDEVVVIG
SCMTPPDSIFNESDESLRSVLSEIRLNLRTGESTRRPIISGEQVNLEAGMVNRNLLGRKTRYAYLAIAEP
WPKVSGFAKVDLSTGEVKKYIYGEGRYGGEPFFVPRGSGSEAEDDGYILAFVHDEEKGKSELQVVNAVNL
ELEATVKLPSRVPYGFHGTFISAEDLLKQA
>gnl|CDD|177901 PLN02259, PLN02259, branched-chain-amino-acid aminotransferase 2
MIKTITSLRKTLVLPLHLHIRTLQTFAKYNAQAASALREERKKPLYQNGDDVYADLDWDNLGFGLNPADY
MYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKLGAER
MLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKE
GMAALNLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSVKKKYLEEASSCNVFVV
KGRTISTPATNGTILEGITRKSVMEIASDQGYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTITYQEK
RVEYKTGDESVCQKLRSVLVGIQTGLIEDNKGWVTDIN
>gnl|CDD|215146 PLN02260, PLN02260, probable rhamnose biosynthetic enzyme
MATYEPKNILITGAAGFIASHVANRLIRNYPDYKIVVLDKLDYCSNLKNLNPSKSSPNFKFVKGDIASAD
LVNYLLITEGIDTIMHFAAQTHVDNSFGNSFEFTKNNIYGTHVLLEACKVTGQIRRFIHVSTDEVYGETD
EDADVGNHEASQLLPTNPYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYGPNQFPEKLIPKFILLAMQG
KPLPIHGDGSNVRSYLYCEDVAEAFEVVLHKGEVGHVYNIGTKKERRVIDVAKDICKLFGLDPEKSIKFV
ENRPFNDQRYFLDDQKLKKLGWQERTSWEEGLKKTMEWYTSNPDWWGDVSGALLPHPRMLMMPGVRLFDG
SEEIKLSSSGSQTGLVVVTKPAGSSPGKPSLKFLIYGRTGWIGGLLGKLCEKQGIAYEYGKGRLEDRSSL
LADIRNVKPTHVFNAAGVTGRPNVDWCESHKVETIRANVVGTLTLADVCRENGLLMMNFATGCIFEYDAK
HPEGSGIGFKEEDKPNFTGSFYSKTKAMVEELLREYDNVCTLRVRMPISSDLSNPRNFITKISRYNKVVN
IPNSMTVLDELLPISIEMAKRNLRGIWNFTNPGVVSHNEILEMYKDYIDPGFKWSNFTLEEQAKVIVAPR
SNNEMDASKLKKEFPELLSIKESLIKYVFEPNKKTPAK
>gnl|CDD|215147 PLN02262, PLN02262, fructose-1,6-bisphosphatase
MDHAADAHRTDLMTITRFVLNEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQG
EEQKKLDVLSNDVFIKALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFG
IYMLKDGGEGTVEDVLQPGKEMVAAGYCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGK
IYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRV
LYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEEIKALYAAEAAK
>gnl|CDD|177904 PLN02263, PLN02263, serine decarboxylase
HLPEKLEILSVDIDPDLLVSDPLPVATYNVAVVAEYGDLGGEREIVLGRNVHTTCLAVTEPEADDEFTGD
KEAYMASVLARYRKTLVERTKHHLGYPYNLDFDYGALGQLQHFSINNLGDPFIESNYGVHSRQFEVGVLD
WFARLWEIEKNEYWGYITNCGTEGNLHGILVGREVFPDGILYASRESHYSVFKAARMYRMECVKVDTLVS
GEIDCADFKAKLLANKDKPAIINVNIGTTVKGAVDDLDLVIKTLEECGFSQDRFYIHCDGALFGLMMPFV
KRAPKVTFKKPIGSVSVSGHKFVGCPMPCGVQITRMEHINVLSSNVEYLASRDATIMGSRNGHAPIFLWY
TLNRKGYRGFQKEVQKCLRNAHYLKDRLREAGISAMLNELSSTVVFERPKDEEFVRRWQLACQGNIAHVV
VMPSVTIEKLDYFLKELVEKRSTWYPDGKVQPPCVAKDVGEENCLCSLHK
>gnl|CDD|215148 PLN02264, PLN02264, lipoxygenase
MALAKEIMGGRLIFERSSFVSSSKHFRNSKRTQRTQFSINPFRQEQLRRVVKSGVVAAISEDLVKTLRVS
TVRKSEEEEEKAVKFKVRAVVTVRNKNKEDLKETLVKHLDAFTDKIGRNVVLELISTQVDPKTKEPKKSK
AAVLKDWSKKSNIKAERVHYTAEFTVDSAFGSPGAITVTNKHQKEFFLESITIEGFACGPVHFPCNSWVQ
SQKDHPGKRIFFTNQPYLPSETPAGLRALREKELRNLRGDGKGVRKLSDRIYDFDVYNDLGNPDKSRELA
RPTLGGKKIPYPRRCRTGRLPTDSDMMAESRVEKPLPMYVPRDEQFEESKQDTFAAGRLKAVLHNLIPSL
KASILAEDFANFGEIDSLYKEGLLLKLGFQDDIFKKFPLPKVVTTLQESSEGLLKYDTPKILSKDKFAWL
RDDEFARQAIAGINPVNIERVKVFPPVSNLDPEIYGPQHSALTEDHIIGHLDGLSVQQALEENRLFMVDY
HDIYLPFLDRINALDGRKAYATRTIFFLTRLGTLKPIAIELSLPPSGPNSRSKRVVTPPVDATSNWMWQL
AKAHVCSNDAGVHQLVNHWLRTHACLEPFILAAHRQLSAMHPIFKLLDPHMRYTLEINALARQTLISADG
VIESCFTAGQYGMEISAAAYKNSWRFDMEGLPADLIRRGMAVPDPTQPHGLKLLIEDYPYANDGLLLWSA
IQTWVRTYVERYYPDPSLICTDKELQAWYSESINVGHADLRDADWWPKLSTVDDLVSILTTLIWLASAQH
AALNFGQYPYGGYVPNRPPLMRRLIPDESDPEYASFLADPQKYYFSSMPSLLQTTKFMAVVDTLSTHSPD
EEYIGERQQPSIWTGDAEIVEAFYGFSAEIGRIEKEIEKRNADPSRRNRCGAGVLPYELLAPSSEPGVTC
RGVPNSVSI
>gnl|CDD|215149 PLN02265, PLN02265, probable phenylalanyl-tRNA synthetase beta chain
MPTVSVGRDRLFAALGRTYTQEEFDELCFEFGIELDDVTTEKAIIRKEKHLDEEEDGGADDDEEVIYKID
VPANRYDLLCLEGLARALRVFLGTEPIPTYRLAEISKGSILKMHVKPETSLIRPFVVCAVLRGVTFDEAR
YNSFIDLQDKLHQNICRRRTLVAIGTHDLDTLQGPFTYEALPPEDINFVPLKQTKSFRADELMEFYKSDM
KLKKFLHIIENSPVFPVIYDSNRTVLSLPPIINGAHSAITLDTKNVFIECTATDLTKAKIVLNTMVTMFS
EYCARKFEVEPVEVVYPDGKSTVYPDLSVRTMEVDLSYINSSIGVSLDAEEVASLLNKMQLQAEQSSDDG
CTIRVSVPPTRSDILHPCDVAEDVAIAYGYNNIPKRKPKSMTVGKQQPLNQFSDLLRAEVAMAGFTEVLT
WILCSHKENFAMLNREDDGNSAVIIGNPRSADFEVVRTSLLPGLLKTLGHNKDAPKPIKLFEVSDVVLLD
ESKDVGARNSRRLAALYCGTTSGFEVIHGLVDRIMEVLGIPFVEIGDNNGYYVEPSNEPEYFPGRQASII
YKGKHVGTFGIVHPEVLNNFDIPDPCSFLELDLEPLL
>gnl|CDD|215150 PLN02266, PLN02266, endoglucanase
LSMALSSTLLRLFIFLAFSLLLCNGFSSSSNNPFHHRHHPRLASHNYRDALTKSILFFEGQRSGKLPSSQ
RMTWRRDSGLSDGSAMHVDLVGGYYDAGDNVKFGFPMAFTTTMLSWSVIEFGGLMKSELQNAKDAIRWAT
DYLLKATAHPDTIYVQVGDANKDHACWERPEDMDTPRSVFKVDKNTPGSDVAAETAAALAAASLVFRKSD
PTYSKLLVRRAIRVFQFADKYRGAYSNGLKPDVCPFYCSYSGYQDELLWGAAWLHKATKNPTYLNYIQVN
GQILGADEFDNTFGWDNKHVGARILLSKAFLVQKVQSLHEYKGHADNFICSVIPGAPFSSTQYTPGGLLF
KMSDSNMQYVTSTSFLLLTYAKYLTSAKTVVNCGGTVVTPARLRSIAKKQVDYLLGDNPLKMSYMVGYGP
RYPRRIHHRGSSLPSVAAHPAKIQCSQGFSIMNSQSPNPNVLVGAVVGGPDQHDRFPDERSDYEQSEPAT
YINAPLVGALAYLAHSYGQL
>gnl|CDD|215151 PLN02267, PLN02267, enoyl-CoA hydratase/isomerase family protein
MCTLEKRGNLFILTLTGDGEHRLNPTLIDSIRSALRQVKSQATPGSVLITTAEGKFFSNGFDLAWAQAAG
SAPSRLHLMVAKLRPLVADLISLPMPTIAAVTGHASAAGFILALSHDYVLMRKDRGVLYMSEVDIGLPLP
DYFMALLRAKIGSPAARRDVLLRAAKLTAEEAVEMGIVDSAHDSAEETVEAAVRLGEELAARKWNGEVYA
SIRKSLLPEVCGKLGLDEEVEESHTTSKL
>gnl|CDD|177909 PLN02268, PLN02268, probable polyamine oxidase
PSVIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHTDYSFGFPVDMGASWLHGVCNENPLAPLIG
RLGLPLYRTSGDNSVLYDHDLESYALFDMDGNQVPQELVTKVGETFERILEETEKVRDEHEEDMSLLQAI
SIVLERHPELRLEGLAHEVLQWYLCRMEGWFAADADTISLKSWDQEELLEGGHGLMVRGYDPVINTLAKG
LDIRLNHRVTKIVRRYNGVKVTVEDGTTFVADAAIIAVPLGVLKANIIKFEPELPEWKEEAISDLGVGIE
NKIALHFDSVFWPNVEFLGVVAPTSYGCSYFLNLHKATGHPVLVYMPAGRLARDIEKLSDEAAANFAMSQ
LKKMLPDATEPVQYLVSRWGSDPNSLGCYSYDLVGKPHDLYERLRAPVDNLFFAGEATSSDFPGSVHGAY
STGVMAAEECRMRLL
>gnl|CDD|215152 PLN02269, PLN02269, Pyruvate dehydrogenase E1 component subunit alpha
STDPITIETPVPFKGHLCDPPSRTVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEA
VAVGMEAAITKEDAIITAYRDHCTHLGRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIV
GAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAA
KSPAYYKRGDYVPGLKVDGMDVLAVKQACKFAKEHALSNGPIVLEMDTYRYHGHSMSDPGSTYRTRDEIS
GVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTNVYVKGLGVESY
GADRKEVRVVLP
>gnl|CDD|165912 PLN02270, PLN02270, phospholipase D alpha
MAQILLHGTLHATIYEVDKLHSGGGPGFLGKLVANVEETVGVGKGESQLYATIDLEKARVGRTRKIENEP
KNPRWYESFHIYCAHMASNIIFTVKDDNPIGATLIGRAYIPVEEILDGEEVDRWVEILDNDKNPIHGGSK
IHVKLQYFEVTKDRNWGRGIRSAKFPGVPYTFFSQRQGCKVSLYQDAHIPDNFVPKIPLAGGKNYEPHRC
WEDVFDAITNAKHLIYITGWSVYTEISLVRDSRRPKPGGDVTIGELLKKKASEGVRVLLLVWDDRTSVDL
LKKDGLMATHDEETENFFRGTDVHCILCPRNPDDGGSIVQDLQISTMFTHHQKIVVVDSEMPNGGSQRRR
IVSFVGGIDLCDGRYDTPFHSLFRTLDTAHHDDFHQPNFTGASITKGGPREPWHDIHSRLEGPIAWDVLF
NFEQRWSKQGGKDILVQLRELEDVIIPPSPVMFPDDHEVWNVQLFRSIDGGAAFGFPETPEAAAEAGLVS
GKDNIIDRSIQDAYIHAIRRAKDFIYIENQYFLGSSFAWSADGIKPEDINALHLIPKELSLKIVSKIEAG
EKFTVYVVVPMWPEGIPESGSVQAILDWQRRTMEMMYKDVIQALRAKGLEEDPRNYLTFFCLGNREVKKS
GEYEPSEKPEPDTDYIRAQEARRFMIYVHTKMMIVDDEYIIIGSANINQRSMDGARDSEIAMGGYQPYHL
STRQPARGQIHGFRMSLWYEHLGMLDETFLDPESEECIQKVNQIADKYWDLYSSETLEHDLPGHLLRYPI
GVASEGDITELPGTEFFPDTKARVLGAKSDYLPPILTT
>gnl|CDD|215153 PLN02271, PLN02271, serine hydroxymethyltransferase
LSRIAQSDLSLGFHSHPSPSPAPIADDSITLQIDSSFRSSSNPMPPIPLQLLEQKEEKEEDAGEEGDEDE
EEQGEDEHFSILGHPMCLKRPRDGDSSSSSSSSSSKRAAVDSGLESRRAAVRAWGNQPLPEADPDIHELM
EKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFGLD
SEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTPGGKKVSGASIFFESLPYKVNP
QTGYIDYDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFD
YCDIVTSTTHKSLRGPRGGIIFYRKGPKLRKQGMLLSHGDDNSHYDFEEKINFAVFPSLQGGPHNNHIAA
LAIALKQVATPEYKAYMQQVKKNAQALASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCH
ITLNKTAIFGDNGTISPGGVRIGTPAMTSRGCLESDFETIADFLLRAAQIASAVQREHGKLQKEFLKGLQ
NNKDIVELRNRVEAFASQFAMPGFDV
>gnl|CDD|177912 PLN02272, PLN02272, glyceraldehyde-3-phosphate dehydrogenase
MAFSSLLRSAATAPAAAARGSDFSSSSSDPSKVSSVGFSSSLSFSGSSSGASSSLQSCSARSVQPIKATA
TEAPPAVLKSSSSGKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKG
TINVVDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSAD
APMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWR
GGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASE
GPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNRVLDLIEHMALVAAS
H
>gnl|CDD|215154 PLN02274, PLN02274, inosine-5'-monophosphate dehydrogenase
SDMSAFEDGFSAEKLFNQGVSYTYDDVIFHPGYIDFPADAVDLSTRLSRNIPLSIPCVSSPMDTVTESDM
AIAMAALGGIGIVHYNNTAEEQAAIVRKAKSRRVGFVSDPVVKSPSSTISSLDELKASRGFSSVCVTETG
TMGSKLLGYVTKRDWDFVNDRETKLSEVMTSDDDLVTAPAGIDLEEAEAVLKDSKKGKLPLVNEDGELVD
LVTRTDVKRVKGYPKLGKPSVGKDGKLLVGAAIGTRESDKERLEHLVKAGVDVVVLDSSQGDSIYQLEMI
KYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRVGMGSGSICTTQEVCAVGRGQATAVYKVASIAAQH
GVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQDGVRVKKYRGMGSLEAMTKGSDQR
YLGDTAKLKIAQGVSGAVADKGSVLKFVPYTMQAVKQGFQDLGASSLQSAHELLRSGTLRLEVRTGAAQV
EGGVHGLVSYEKKAF
>gnl|CDD|215155 PLN02275, PLN02275, transferase, transferring glycosyl groups
MGRRGRAAVVVLGDFGRSPRMQYHALSLARQASFQVDVVAYGGSEPIPALLNHPSIHIHLMVQPRLLQRL
PRVLYALALLLKVAIQFLMLLWFLCVKIPRPDVFLVQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTL
LALSLGRSHPLVRLYRWYERHYGKMADGHLCVTKAMQHELDQNWGIRATVLYDQPPEFFRPASLEIRLRP
NRPALVVSSTSWTPDEDFGILLEAAVMYDRRVAARLNESDSASGKQSLYPRLLFIITGKGPQKAMYEEKI
SRLNLRHVAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKD
GKNGLLFSSSSELADQLLELL
>gnl|CDD|215156 PLN02276, PLN02276, gibberellin 20-oxidase
KREQGSLVFDASVLQKQSNIPAQFIWPDEEKPSAAVPELAVPLIDLGGFLSGDEAATAEAARLVREACLK
HGFFQVVNHGVDAALIRAAHEYMDAFFKLPLSEKQRAQRKPGESCGYASSHTGRFSSKLPWKETLSFGYH
ADGGSSPVVVDYFKSVLGEDFEQFGKVYQEYCEAMKTLSLKIMELLGISLGVDRGYYRKFFEDGDSIMRC
NYYPPCQEPELTLGTGPHCDPTSLTILHQDQVGGLQVFVDNKWRSVRPRPGALVVNIGDTFMALSNGRYK
SCLHRAVVNSERERRSLAFFLCPKEDKVVRPPQELVDREGPRKYPDFTWSDLLEFTQKHYRADMNTLQAF
SNWLQSSNNKA
>gnl|CDD|177916 PLN02277, PLN02277, H(+) -translocating inorganic pyrophosphatase
TVCIISLLFSLYLTKWVLAKDEGPPEMVEISDAIRDGAEGFFRTQYGTISKMAVVLAFVILGIYLFRSLT
PQQEAAGLGRATSAYITVASFLLGALCSGIAGYVGMWVSVRANVRVSSAARRSAREALQIAVRAGGFSAL
VVVGMTVLGVAILYATFYVWLGVDSPGGMKVTDLPLLLVGYGFGASFVALFAQLGGGIYTKAADVGADLV
GKVEQGIPEDDPRNPAVIADLVGDNVGDCAARGADLFESIAAEIISAMILGGTMAKRCKIEDPSGFILFP
LVVHSFDLVVSSIGILSIKGTRDSSVKSPVEDPMAVLQKGYSVTIILAVVTFGASTRWLLYTEQAPSAWF
NFALCGLVGIITAYAFVWISQYYTDYKYEPVRTLALASTTGHGTNIIAGVSLGLESTALPVLVISVAIIS
AYWLGNTSGLVDENGNPTGGLFGTAVATMGMLSTAAYVLTMDMFGPIADNAGGIVEMSQQPESVREITDL
LDAVGNTTKATTKGFAIGSAALASFLLFSAYMDEVSAFAGVPFKEVDIAIPEVFVGGLLGSMLIFLFSAW
ACAAVGRTAQEVVNEVRRQFAERPGIMDYKEKPDYGRCVAIVASAALREMIKPGALAVISPIVVGLVFRI
LGYATGQPLLGAKVVAGMLMFATVSGILMALFLNTAGGAWDNAKKYIETGALGGKGSEAHKAAVTGDTVG
DPFKDTAGPSIHVLIKMLATITLVMAPMFL
>gnl|CDD|215157 PLN02278, PLN02278, succinic semialdehyde dehydrogenase
PSTRASSMDAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIAS
AHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRV
YGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELA
LQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFD
DADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAA
VQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAI
ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK
YVCLGNMN
>gnl|CDD|177918 PLN02279, PLN02279, ent-kaur-16-ene synthase
MSINLRSSGCSSPISATLEPRLKTWTQTRANNVSFEGTKERIKKMFDKVELSVSSYDTAWVAMVPSPNSQ
QAPLFPECVKWLLENQLEDGSWGLPHDHPLLVKDALSSTLASILALKKWGVGEEQINKGLQFIELNSASV
TDEKQHKPIGFDIIFPGMIEYAKDLDLNLPLGSEVVDAMLHKRDLDLKSGGGSNTKGREAYLAYVSEGIG
KLQDWEMVMKYQRKNGSLFNSPSTTAAAFSHLQNAGCLRYLRSLLQKFGNAVPTVYPLDQYARLSMVDTL
ERLGIDRHFRKEIKSVLDETYRYWLQGEEEIFLDLATCALAFRILRLNGYDVSSDPLKQFAEDHFSDSLG
GYLKDTGAVLELFRASQISYPDESLLEKQNSWTSHFLEQGLSNWSKTADRLRKYIKKEVEDALNFPYYAN
LERLANRRSIENYAVDDTRILKTSYRCSNICNQDFLKLAVEDFNFCQSIHREELKQLERWIVENRLDKLK
FARQKLAYCYFSAAATLFSPELSDARLSWAKNGVLTTVVDDFFDVGGSEEELENLIQLVEKWDVNGSPDF
CSEQVEIIFSALRSTISEIGDKAFTWQGRNVTSHIIKIWLDLLKSMLTEAQWSSNKSTPTLDEYMTNAYV
SFALGPIVLPALYLVGPKLSEEVVDSPELHKLYKLMSTCGRLLNDIRGFKRESKEGKLNAVSLHMIHGNG
NSTEEEAIESMKGLIESQRRELLRLVLQEKGSNVPRECKDLFWKMSKVLHLFYRKDDGFTSNDMMSLVKS
VIYEPVSLQEESLT
>gnl|CDD|215158 PLN02280, PLN02280, IAA-amino acid hydrolase
MNNLRNLNLLSLSLTISFVSLTISSSSSSSDADPPSLSFFEVKYPNVNSFGMLLRNSPKKNQSSGLPAKP
SSDECEVWTKACSEAVLRLAYQPDTVAWLKSVRRKIHENPELAFEEYKTSELVRSELDRMGIMYRYPLAK
TGIRAWIGTGGPPFVAVRADMDALPIQEAVEWEHKSKVAGKMHACGHDAHVAMLLGAAKILKSREHLLKG
TVVLLFQPAEEAGNGAKRMIGDGALDDVEAIFAVHVSHEHPTAVIGSRPGPLLAGCGFFRAVISGKKGRA
GSPHHSVDLILAASAAVISLQGIVSREANPLDSQVVSVTTMDGGNNLDMIPDTVVLGGTFRAFSNTSFYQ
LLKRIQEVIVEQAGVFRCSATVDFFEKQNTIYPPTVNNDAMYEHVRKVAIDLLGPANFTVVPPMMGAEDF
SFYSQVVPAAFYYIGIRNETLGSTHTGHSPYFMIDEDVLPIGAAVHAAIAERYLIEHS
>gnl|CDD|177920 PLN02281, PLN02281, chlorophyllide a oxygenase
MNAAVFSPSALSLPISFSKTRSSFLSRKKGVKGEFRVFAVFGDESGLVEKKSQWRPLFDVEDPRSKAPPY
KGKFLDVNQAIEVARFDIQYLDWRARQDLLTIMILHDKVVDVLNPLAREYKSIGTVKKELAGLQEELSKA
HQQVHISEARVSTALDKLAHMEELVNDRLLPGRVVTELDKPSSSTTASAVELDREKTNTGAKSLNVSGPV
PPYSPHLKNFWYPVAFTADLKHDTMVPIECFEQPWVIFRGEDGKPGCVRNTCAHRACPLDLGTVNEGRIQ
CPYHGWEYSTDGECKKMPSTKLLKVKIKSLPCLEQEGMIWIWPGDEPPAPILPSLQPPSGFLIHAELVMD
LPVEHGLLLDNLLDLAHAPFTHTSTFAKGWSVPSLVKFLTPTSGLQGYWDPYPIDMEFKPPCIVLSTIGI
SKPGKLEGKSTQQCATHLHQLHVCLPSSKNKTRLLYRMSLDFAPILKNLPFMEHLWRHFAEQVLNEDLRL
VLGQQERMLNGANIWNLPVAYDKLGVRYRLWRNAVDRGDDKLPFSG
>gnl|CDD|165923 PLN02282, PLN02282, phosphoglycerate kinase
MATKRSVGTLKEADLKGKRVFVRVDLNVPLDDNSNITDDTRIRAAVPTIKYLMGHGARVILCSHLGRPKG
VTPKYSLKPLVPRLSELLGVEVVMANDCIGEEVEKLVAELPEGGVLLLENVRFYKEEEKNDPEFAKKLAS
LADVYVNDAFGTAHRAHASTEGVAKYLKPSVAGFLMQKELDYLVGAVANPKKPFAAIVGGSKVSTKIGVI
ESLLEKVDILLLGGGMIFTFYKAQGYSVGSSLVEEDKLDLATSLIEKAKAKGVSLLLPTDVVIADKFAPD
ANSKVVPASAIPDGWMGLDIGPDSIKTFSEALDTTKTIIWNGPMGVFEFEKFAAGTEAIAKKLAELSGKG
VTTIIGGGDSVAAVEKVGLADKMSHISTGGGASLELLEGKPLPGVLALDDA
>gnl|CDD|177921 PLN02283, PLN02283, alpha-dioxygenase
MLFSASLSWFIHPDLHEVVSKMSLFDRFLFLIVHFVDKLGLWHRLPVFLGLAYLALRRHLHQRYNLLNVG
QTPNGQRYDPAEYPYRTADGKCNDPFNEGAGSQGTFFGRNMPPVDQKDKLLDPHPSVVATKLLARKKFID
TGKQFNMIAASWIQFMIHDWIDHLEDTQQIELTAPKEVASQCPLKSFKFYKTKEVPTGSPDIKTGSLNIR
TPWWDGSVIYGSNEKGLRRVRTFKDGKLKISEDGLLLHDEDGIPISGDVRNSWAGVSLLQALFVKEHNAV
CDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVELLKTDTLLAGMRANWYGLLGKKFKDTFGHIG
GPILSGLVGLKKPNNHGVPYSLTEEFTSVYRMHSLLPDHLILRDITAAPGENKSPPLIEEIPMPELIGLK
GEKKLSKIGFEKLMVSMGHQACGALELWNYPSWMRDLVPQDIDGEDRPDHVDMAALEIYRDRERGVARYN
EFRRNLLMIPISKWEDLTDDEEAIEVLREVYGDDVEKLDLLVGLMAEKKIKGFAISETAFFIFLLMASRR
LEADRFFTSNFNEKTYTKKGLEWVNTTESLKDVIDRHYPEMTDKWMNSSSAFSVWDSPPNPHNWIPLYLR
PPP
>gnl|CDD|177922 PLN02284, PLN02284, glutamine synthetase
MSLLSDLINLNLSDSTDKIIAEYIWIGGSGMDLRSKARTLPGPVTDPSKLPKWNYDGSSTGQAPGEDSEV
ILYPQAIFKDPFRGGNNILVMCDAYTPAGEPIPTNKRAKAAKIFSHPDVAAEEPWYGIEQEYTLLQKDVK
WPLGWPVGGYPGPQGPYYCGVGADKAFGRDIVDAHYKACLYAGINISGINGEVMPGQWEFQVGPVVGISA
GDQLWVARYILERITEIAGVVVSFDPKPIPGDWNGAGAHTNYSTKSMREDGGYEVIKKAIEKLGLRHKEH
IAAYGEGNERRLTGKHETADINTFSWGVANRGASIRVGRDTEKEGKGYFEDRRPASNMDPYVVTSMIAET
TILW
>gnl|CDD|215159 PLN02285, PLN02285, methionyl-tRNA formyltransferase
AGSGRKKRLVFLGTPEVAATVLDALLDASQAPDSAFEVAAVVTQPPARRGRGRKLMPSPVAQLALDRGFP
PDLIFTPEKAGEEDFLSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQ
DGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPLLFELGTKLLLRELPSVLDGSAKDKATPQ
DDSKATHAPKISPEESWLSFDEEARVLHNKVRAFAGWPGTRAKFQLVDDGDGEREVLELKIITTRVCEAG
GEQTGSADAVTFKKDSLLVPCGGGTWLEVLEVQPPGKKVMKAKDFWNGLRGQTL
>gnl|CDD|215160 PLN02286, PLN02286, arginine-tRNA ligase
RELAKLFEASLRLTVPDEPSVEPLVAACTNPKFGDYQCNNAMGLWSKLKGKGTSFKNPRAVAQAIVKNLP
ASEMIESTSVAGPGFVNVRLSASWLAKRIERMLVDGIDTWAPTLPVKRAVVDFSSPNIAKEMHVGHLRST
IIGDTLARMLEFSGVEVLRRNHVGDWGTQFGMLIEHLFEKFPNWESVSDQAIGDLQEFYKAAKKRFDEDE
EFKARAQQAVVRLQGGDPEYRAAWAKICEISRREFEKVYQRLRVELEEKGESFYNPYIPGVIEELESKGL
VVESDGARVIFVEGFDIPLIVVKSDGGFNYASTDLAALWYRLNEEKAEWIIYVTDVGQQQHFDMVFKAAK
RAGWLPEDTYPRLEHVGFGLVLGEDGKRFRTRSGEVVRLVDLLDEAKSRSKAALIERGKDSEWTPEELEQ
AAEAVGYGAVKYADLKNNRLTNYTFSFDQMLDLKGNTAVYLLYAHARICSIIRKSGKDIDELKKTGKIVL
DHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVNGSEEETSRLLLCEATAIV
MRKCFHLLGITPLYRL
>gnl|CDD|215161 PLN02287, PLN02287, 3-ketoacyl-CoA thiolase
MEKAINRQRVLLRHLRPSSSEPSSLSASACAAGDSAAYHRTTAFGDDVVIVAAYRTPICKAKRGGFKDTY
PDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPVRTVNRQCSSGLQA
VADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQ
DQAAVESHRKAAAATASGKFKDEIVPVHTKIVDPKTGEEKPIVISVDDGIRPNTTLADLAKLKPVFKKNG
TTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDD
IDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGKDCRFGVVSM
CIGTGMGAAAVFERGDSVDELSNARKVEGNNL
>gnl|CDD|215162 PLN02288, PLN02288, mannose-6-phosphate isomerase
MLRLRCAVQNYDWGRIGSESEVARLAAANSGSDVDPDKPYAELWMGTHPSGPSFVVATGKGSVLLKEWIA
ENPAALGDRVVERWGGDLPFLFKVLSVAKALSIQAHPDKKLAEKLHAEQPNVYKDDNHKPEMALALTEFE
ALCGFVTIQELKAVLRTVPELRELVGSEAADQLLALPEHDGEEDVKSVLRSAFTALMTASKDVVTEAVSK
LKARLHAESQARELTDKEELVLRLEKQYPGDVGVLSAFFLNYVKLNPGEALYLGANEPHAYLSGECIECM
ATSDNVVRAGLTPKFRDVQTLCSMLTYKQGFPEILTGVPVDPYTTRYLPPFDEFEVDHCDVPPGASVVFP
AVPGPSVFLVIEGEGVLSTGSSEDGTAAKRGDVFFVPAGTEIHV
>gnl|CDD|215163 PLN02289, PLN02289, ribulose-bisphosphate carboxylase small chain
MASSMLSSAAVATSPAQATMVAPFTGLKSSAAFPVTRKANNDITSIASNGGRVSCMQVWPPIGKKKFETL
SYLPDLTDEELAKEVDYLLRNKWVPCLEFELEHGFVYREHHRSPGYYDGRYWTMWKLPMFGCTDSAQVLK
ELEEAKKAYPNAFIRIIGFDNTRQVQCISFIAYKPP
>gnl|CDD|215164 PLN02290, PLN02290, cytokinin trans-hydroxylase
MLGVVLKVLLVIFLTLLLRVAYDTISCYFLTPRRIKKIMERQGVRGPKPRPLTGNILDVSALVSQSTSKD
MDSIHHDIVGRLLPHYVAWSKQYGKRFIYWNGTEPRLCLTETELIKELLTKYNTVTGKSWLQQQGTKHFI
GRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQMLQSLQKAVESGQTEVEIGEYMTRLTADI
ISRTEFDSSYEKGKQIFHLLTVLQRLCAQATRHLCFPGSRFFPSKYNREIKSLKGEVERLLMEIIQSRRD
CVEIGRSSSYGDDLLGMLLNEMEKKRSNGFNLNLQLIMDECKTFFFAGHETTALLLTWTLMLLASNPTWQ
DKVRAEVAEVCGGETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLHIPKGLSIWIPVL
AIHHSEELWGKDANEFNPDRFAGRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTISDN
YRHAPVVVLTIKPKYGVQVCLKPLNP
>gnl|CDD|177928 PLN02291, PLN02291, phospho-2-dehydro-3-deoxyheptonate aldolase
VHAAEPSKTPVSSAGGPKKWSPDSWRSKKALQLPEYPDQAELEEVLKTLEAFPPLVFAGEARSLEERLAE
AAMGRAFLLQGGDCAESFKEFNANNIRDTFRVLLQMGVVLMFGGQMPVVKVGRMAGQFAKPRSDPFEEKD
GVKLPSYRGDNINGDAFDEKSRRPDPQRMVRAYSQSAATLNLLRAFATGGYAAMQRVTQWNLDFTEHSEQ
GDRYRELAHRVDEALGFMAACGLTTDHPIMTTTEFWTSHECLLLPYEQALTREDSTSGLYYDCSAHMLWV
GERTRQLDGAHVEFLRGVANPLGIKVSDKMDPEELVKLIEILNPQNKPGRLTIIVRMGAEKLRVKLPHLI
RAVRRAGQIVTWVSDPMHGNTIKAPSGLKTRPFDAIRAEVRAFFDVHEQEGSHPGGVHLEMTGQNVTECI
GGSRTVTFDDLSSRYHTHCDPRLNASQSLELAFIIAERLRKRRIRSGANTALAS
>gnl|CDD|215165 PLN02292, PLN02292, ferric-chelate reductase
MSLGEENKDVIKGVIKFLMMVILMGTIVIWIMMPTSTYKTIWLPSMRAKLGKSTYFGAPGVNLLVYMFPM
ILLACLGCIYLHLKKQTTVNQFNREVRKKGGKFGALRRPMLVKGPLGIVTVTEVMFLAMFMALLLWSLAN
YMYNTFVTITPQSAATDGESLWQARLDSIAVRLGLVGNICLAFLFYPVARGSSLLAAVGLTSESSIKYHI
WLGHLVMTLFTSHGLCYIIYWISMNQVSQMLEWDRTGVSNLAGEIALVAGLVMWATTYPKIRRRFFEVFF
YTHYLYIVFMLFFVFHVGISFALISFPGFYIFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPML
MYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSVMIKSQGKWSTKLYHMLSSSDQIDRLAVSVEGP
YGPASTDFLRHESLVMVSGGSGITPFISIIRDLIYTSSTETCKIPKITLICAFKNSSDLSMLDLILPTSG
LETELSSFIDIQIKAFVTREKEAGVKESTGNMNIIKTLWFKPNLSDQPISPILGPNSWLWLAAILSSSFL
IFIIIIAIITRYHIYPIDQNSNKYTLAYKSLIYLLVISISVVATSTAAMLWNKKKYYKKSSQQVDNVDSP
REIESSPQQLLVQRTNIHYGERPNLNKLLVGLKGSSVGVLVCGPKKMRQKVAKICSSGLAENLHFESISF
SW
>gnl|CDD|177930 PLN02293, PLN02293, adenine phosphoribosyltransferase
MFAMENGDQGDPRLQGISSAIRVVPDFPKPGIMFQDITTLLLDPKAFKDTIDLFVERYRDMGISVVAGIE
ARGFIFGPPIALAIGAKFVPLRKPGKLPGEVISEEYVLEYGTDCLEMHVGAVEPGERALVIDDLIATGGT
LCAAINLLERAGAEVVECACVIELPELKGREKLNGKPLFVLVESRGI
>gnl|CDD|177931 PLN02294, PLN02294, cytochrome c oxidase subunit Vb
MWRRIVSSHLKTLAASVVAASPRRTVVATTRPLYLSRSRSSISASSSVFSRYFSSESADTAVKKRVEDVM
PIATGHEREELEAELEGRKLLDIDFPEGPFGTKEAPAVVKSYYDKRIVGCPGGEGEDEHDVVWFWLEKGK
SFECPVCTQYFELEVVGPGGPPDGHGDDDDHHHH
>gnl|CDD|215166 PLN02295, PLN02295, glycerol kinase
FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNV
DSGLKAIGITNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRKHFVETCGLPISTYFSA
TKLLWLLENVDAVKEAVKSGDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLE
ALGIPAEILPKIVSNSEVIGTIAKGWPLAGVPIAGCLGDQHAAMLGQRCRPGEAKSTYGTGCFILLNTGE
EVVPSKHGLLTTVAYKLGPDAPTNYALEGSVAIAGAAVQWLRDNLGIIKSASEIEALAATVDDTGGVYFV
PAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDAMRKDAGEEKSHKGLFLLRVDG
GATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASEKWKNTTTFRPKLDEEER
AKRYASWCKAVERSFDLADLSI
>gnl|CDD|215167 PLN02296, PLN02296, carbonate dehydratase
MGTLGRAIYTVGFWIRETGQALDRLGCRLQGNYYFREQLSRHRTLMNIFDKAPVVDKDAFVAPSASVIGD
VQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHVAKTNLSGKVLPTIIGDNVTIGHSAVLHGCTVE
DEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSNL
AQVHAAENAKSFDEIEFEKVLRKKFARRDEEYDSMLGVVRETPPELILPDNILPDKAPK
>gnl|CDD|177934 PLN02297, PLN02297, ribose-phosphate pyrophosphokinase
TAAAVKRASSKKNKKQVHLFYCEETEELARKIAAESDAIELGSINWRKFPDGFPNLFINNAHGIRGQHVA
FLASFSSPAVIFEQLSVIYALPKLFVASFTLVLPFFPTGTSERVEREGDVATAFTLARILSNIPISRGGP
TSLVIFDIHALQERFYFGDNVLPCFESGIPLLKKRLQQLPDSDNIVIAFPDDGAWKRFHKQFEHFPMVVC
TKVREGDKRIVRIKEGNPAGRHVVIVDDLVQSGGTLIECQKVLAAHGAAKVSAYVTHGVFPNESWERFTH
DNGGPEAGFAYFWITDSCPQTVKAVRGKAPFEVLSLAGSIADALQI
>gnl|CDD|165939 PLN02298, PLN02298, hydrolase, alpha/beta fold family protein
MEDMSDHATETEVHFWGETPEEEYYALKGIKGSKSFFTSPRGLSLFTRSWLPSSSSPPRALIFMVHGYGN
DISWTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSFFNSVKQREEFQGLPRFLYG
ESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPIPQILTFVARFLPTLAIVPTADLLEKSVKV
PAKKIIAKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEAKSE
DKTIKIYDGMMHSLLFGEPDENIEIVRRDILSWLNERCTGKATPSEDSIS
>gnl|CDD|215168 PLN02299, PLN02299, 1-aminocyclopropane-1-carboxylate oxidase
MAKMESFPVIDMEKLNGEERAATMELIKDACENWGFFELVNHGISHELMDEVEKMTKEHYKKCMEQRFKE
MVASKGLEGVQTEVEDLDWESTFFLRHLPESNLADIPDLDDEYRKVMKDFALELEKLAEELLDLLCENLG
LEKGYLKKAFHGSKGPTFGTKVSNYPPCPKPDLVKGLRAHTDAGGIILLFQDDKVSGLQLLKDGEWVDVP
PMRHSIVVNLGDQLEVITNGKYKSVMHRVVAQTDGNRMSIASFYNPGSDAVIYPAPALVEKEAEEEQVYP
KFVFEDYMKLYAGLKFQAKEPRFEAMKAMETTVNLNPIATA
>gnl|CDD|215169 PLN02300, PLN02300, lactoylglutathione lyase
ASAAASTAAEAEDLLEWPKKDKRRMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGP
EDSNFVVELTYNYGVDKYDIGTGFGHFGIAVEDVAKTVELVKAKGGKVTREPGPVKGGKSVIAFVKDPDG
YKFELIQRGPTPEPLCQVMLRVGDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYGPEDKTTVLELT
YNYGVTEYTKGNAYAQIAIGTDDVYKTAEAIKLVGGKITREPGPLPGINTKITACLDPDGWKTVFVDNID
FLKELE
>gnl|CDD|215170 PLN02301, PLN02301, pectinesterase/pectinesterase inhibitor
MSTSNQPLLSSPKSSSHHKTLCLVLSFVAILSSAALFTAPLISTNSSSPPSLLQTLCDRAHDQDSCQAMV
SEIATNTVMKLNRVDLLQVLLKESTPHLQNTIEMASEIRIRINDPRDKAALADCVELMDLSKDRIKDSVE
ALGNVTSKSHADAHTWLSSVLTNHVTCLDGINGPSRQSMKPGLKDLISRARTSLAILVSVSPAKEDLLMP
LSGDFPSWLTSKDRKLLESSPKNIKANVVVAKDGSGKYKTVKEAVASAPDNSKTRYVIYVKKGTYKENVE
IGKKKKNLMLVGDGMDSTIITGSLNVIDGSTTFRSATVAAVGDGFIAQDIWFQNTAGPEKHQAVALRVSA
DQAVINRCRIDAYQDTLYAHSLRQFYRDSYITGTVDFIFGNAAVVFQNCKIVARKPMAGQKNMVTAQGRT
DPNQNTGISIQKCDIIASSDLEPVKGSFKTYLGRPWKEYSRTVVMQSYIDDHIDPAGWSPWDGEFALSTL
YYGEYANRGPGAGTSKRVNWPGFHVITDPKEARKFTVAELIQGGAWLKSTGVSFTEGL
>gnl|CDD|215171 PLN02302, PLN02302, ent-kaurenoic acid oxidase
MELGSIWVWLAAIVAGVFVLKWVLRRVNSWLYEPKLGEGQPPLPPGDLGWPVIGNMWSFLRAFKSSNPDS
FIASFISRYGRTGIYKAFMFGQPTVLVTTPEACKRVLTDDDAFEPGWPESTVELIGRKSFVGITGEEHKR
LRRLTAAPVNGPEALSTYIPYIEENVKSCLEKWSKMGEIEFLTELRKLTFKIIMYIFLSSESELVMEALE
REYTTLNYGVRAMAINLPGFAYHRALKARKKLVALFQSIVDERRNSRKQNISPRKKDMLDLLLDAEDENG
RKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAKKRPPGQKGLTLKDVRKM
EYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYT
PKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLERLNPGCKVMYLPHPRPKDNCLARITKVASE
>gnl|CDD|215172 PLN02303, PLN02303, urease
MKLSPREIDKLLLHQAGFLAQKRLARGLRLNYTEAVALIATQILEFIRDGDKSVAELMDLGKQLLGRRQV
LPAVPHLLHTVQVEGTFPDGTKLVTVHDPISSEDGNLELALHGSFLPVPSLDKFPEDEEEPIPGEIITGD
GSIIINAGRKAVKLKVTNTGDRPIQVGSHYHFIETNPYLVFDRRKAYGMRLNIPAGTAVRFEPGETKTVT
LVSIGGNKVIRGGNGIVDGPVDDSRLTKIMERVSSRGFGHVEEDDASEGVIGEDPDFTTTISREKYANMY
GPTTGDKIRLGDTNLYAEIEKDFTVYGDECKFGGGKVLRDGMGQATGYGAADSLDTVITNAVIIDYTGIY
KADIGIKDGLIVGIGKAGNPDVMDGVTSNMIVGVNTEVIAGEGMIVTAGGIDCHVHFICPQLATEAIASG
ITTLVGGGTGPAHGTCATTCTPAPSHMKLMLQSTDDLPLNFGFTGKGNTAKPEGLHEIIKAGAMGLKLHE
DWGTTPAAIDNCLDVAEEYDIQVTIHTDTLNESGCVEHSIAAFKGRTIHTYHSEGAGGGHAPDIIKVCGV
KNVLPSSTNPTRPYTKNTIDEHLDMLMVCHHLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSD
SQAMGRIGEVITRTWQTAHKMKSQRGALEPRGADNDNFRIKRYIAKYTINPAIAHGMSHFVGSVEVGKLA
DLVLWKPAFFGAKPEMVIKGGQIAWAQMGDPNASIPTPEPVIMRPMFGAFGKAGSSNSIAFVSKAALDAG
VKQLYGLTKRVEAVGNVRGLTKLDMKLNDALPVITVDPETYEVTADGEVLTCAPATSVPLSRNYFLF
>gnl|CDD|215173 PLN02304, PLN02304, probable pectinesterase
STTLFKTSPAAPLLGHLIELSLISFSSKIATSYPHSIHHHSHHHHHHKHPDDGKKVSICDDFPPDFPPPD
TNTTSILCVDPNGCCNFTTVQSAVDAVGNFSQKRNVIWINSGIYYEKVTVPKTKPNITFQGQGFDSTAIA
WNDTAKSANGTFYSASVQVFASNFIAKNISFMNVAPIPKPGDVGAQAVAIRIAGDQAAFWGCGFFGAQDT
LHDDRGRHYFKDCYIQGSIDFIFGDARSLYENCRLISMANPVPPGSKSINGAVTAHGRTSKDENTGFSFV
NCTIGGTGRIWLGRAWRPYSRVVFAYTSMTDIIAPEGWNDFNDPTRDQTIFYGEYNCSGPGANMSMRAPY
VQKLNDTQVSPFLNTSFIDGDQWLQPYDL
>gnl|CDD|215174 PLN02305, PLN02305, lipoxygenase
VASPISPNFSGVSLRASPAFSALGRRRRTRVPISRSPVAGSIRAVISSEDKAVEESGGESANKSVDGSSL
LPSSRSKYAGGIDVRAVITIRKKIKEKITEKFEDQWEYFMNGIGQGILIQLVSEEIDPVTGSGKSVESSV
RGWLPKPSNDPHIVEYAADFTVPFDFGKPGAVLVTNLHGKEFYLMEIVIHGFDDGPIFFPANTWIHSRKD
NPESRIIFRNQAYLPSQTPPGIKDLRREDLLSLRGNGKGERKPHDRIYDYAPYNDLGNPDKDEDLARPVL
GGEEWPYPRRCRTGRPPTKKDPLCESRIEKPHPVYVPRDETFEEIKRNTFSAGRLKALLHNLIPSIAAAL
SSSDIPFTCFSDIDKLYNDGILLKTEEPKDIGLNPFLGNFMKQVLSVSERLLKYDIPAVIKRDRFAWLRD
NEFARQALAGVNPVNIEILKEFPILSKLDPAVYGPPESALTEELIERELEGMTVEKAIEEKRLFILDYHD
MLLPFIEKMNSLPERKAYASRTVFFYSKAGALRPIAIELSLPPTPSSPGNKFVYTHGHDATTHWIWKLAK
AHVCSNDAGVHQLVNHWLRTHACMEPYIIATHRQLSAMHPIYKLLHPHMRYTLEINALARQSLINGGGII
EACFSPGKYAMELSSAAYKSMWRFDMEALPADLIRRGMAEEDPSMPCGVRLVIEDYPYAADGLLIWSAIK
EWVESYVDHFYSEPNSITSDLELQAWWDEIKNKGHYDKRNEPWWPKLNTKEDLSGILTTMIWIASGQHAA
INFGQYPFGGYVPNRPTLMRKLIPQENDPDYEKFIRNPQYTFLSSLPTQLQATKVMAVQDTLSTHSPDEE
YLGELRHLHSHWINDHEVVKLFNKFSARLEEIEKTINERNKDIRLKNRNGAGIPPYELLLPTSGPGVTGR
GIPNSISI
>gnl|CDD|177941 PLN02306, PLN02306, hydroxypyruvate reductase
MAKPVSIEVYNPNGKYRVVSTKPMPGTRWINLLVDQDCRVEICTEKKTILSVEDIIALIGDKCDGVIGQL
TEDWGETLFSALSKAGGKAFSNMAVGYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVE
ADEFMRAGLYEGWLPHLFVGNLLKGQTVGVIGAGRIGSAYARMMVEGFKMNLIYYDLYQSTRLEKFVTAY
GQFLKANGEQPVTWKRASSMEEVLREADVISLHPVLDKTTYHLINKERLALMKKEAVLVNASRGPVIDEV
ALVEHLKANPMFRVGLDVFEDEPYMKPGLADMKNAVVVPHIASASKWTREGMATLAALNVLGKLKGYPVW
GDPNRVEPFLNENAPPPAASPSIVNAKALGLPVSKL
>gnl|CDD|177942 PLN02307, PLN02307, phosphoglucomutase
SSSLAAMASFKVSSVPTKPIEGQKPGTSGLRKKVKVFMQENYLANFVQALFNALPAEKVKGATLVLGGDG
RYFNKEAIQIIIKIAAANGVRRVWVGQNGLLSTPAVSAVIRERDGSKANGGFILTASHNPGGPEEDFGIK
YNYESGQPAPESITDKIYGNTLTIKEYKMAEDIPDVDLSAVGVTKFGGPEDFDVEVIDPVEDYVKLMKSI
FDFELIKKLLSRPDFTFCFDAMHGVTGAYAKRIFVEELGAPESSLLNCVPKEDFGGGHPDPNLTYAKELV
KRMGLGKTSYGDEPPEFGAASDGDGDRNMILGKRFFVTPSDSVAIIAANAQEAIPYFSGGLKGVARSMPT
SAALDVVAKKLNLPFFEVPTGWKFFGNLMDAGKLSICGEESFGTGSDHIREKDGIWAVLAWLSILAHKNK
DVLPGGKLVTVEDIVREHWATYGRNFYSRYDYENVDSEAANKMMDHLRDLVNKSKKGIKYGVYTLAFADD
FEYTDPVDGSVSSKQGIRFLFTDGSRIIFRLSGTGSAGATIRLYIEQYEKDPSKHGRDAQEALKPLIDVA
LKLSKLKEFTGRSKPTVIT
>gnl|CDD|177943 PLN02308, PLN02308, endoglucanase
MAVKSLAAPAIVLLLLLFSPPVIGAGHDYRDALRKSILFFEGQRSGKLPPDQRLKWRRDSALHDGSSAGV
DLTGGYYDAGDNVKFGFPMAFTTTLMSWSIIDFGRTMGPELENAVKAVKWATDYLMKATAIPNVVYVQVG
DAYSDHNCWERPEDMDTLRTVYKIDPSHPGSDVAGETAAALAAASIVFRKRDPAYSRLLLDRAVRVFAFA
DKYRGAYSSSLHAAVCPFYCDFNGYQDELLWGAAWLHKASRRREYREYIVKNEVILGAGDTINEFGWDNK
HAGINVLISKEVLMGKAEYFQSFKQNADGFICSLLPGISHPQVQYSPGGLLFKVGGSNMQHVTSLSFLLL
AYSNYLSHANKVVPCGESTASPALLRQVAKRQVDYILGDNPLRMSYMVGYGSRFPQRIHHRGSSLPSVAA
HPARIGCKEGSRYFLSPNPNPNLLVGAVVGGPNVTDAFPDSRPYFQQSEPTTYINAPLVGLLAYFSAHPN
PA
>gnl|CDD|215175 PLN02309, PLN02309, 5'-adenylylsulfate reductase
SSSSSAISSSGSSRSGASSESKAKQIGSLRLLDRGGLSARAYSLSGKRSSAAKPLNAQPAARQAMIPSAA
TAVAEVPEEEGEVEDFEKLAKELENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFS
LDTGRLNPETYRLFDAVEKHYGIRIEYMFPDAVEVQALVRNKGLFSFYEDGHQECCRVRKVRPLRRALKG
LRAWITGQRKDQSPGTRAEVPVVQVDPVFEGLDGGPGSLVKWNPLANVTGNEVWNFLRTMDVPVNSLHAQ
GYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNIKEEDNGAANDNGNAAVADIFNSQNVVAL
SRAGIENLLKLENRKEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSGVKVAKFRADGDQKEFAKQELQL
GSFPTILLFPKNSSRPIKYPSEKRDVDSLLSFVNSLR
>gnl|CDD|215176 PLN02310, PLN02310, triacylglycerol lipase
MTPTRYLEENMSNKWHEIHGSSNWEHLLDPLHPWLRREILKYGEFAQATYDAFDFDPLSEYCGSCRYNRH
KLFETLGLTKHGYKVKKYIYALSHVDVPHWLKRSQATWSKDSNWMGYVAVSRDEESQRIGRRDIMVAWRG
TVAPSEWFLDLETKLEHIDNTNVKVQEGFLKIYKSKDESTRYNKLSASEQVMQEVKRLVNFYRGKGEEVS
LTVTGHSLGGALALLNAYEAATTIPDLFVSVISFGAPRVGNIAFKEKLNELGVKTLRVVVKQDKVPKLPG
LLNKMLNKFHGLTGKLNWVYRHVGTQLKLDAFSSPYLKRESDLSGCHNLELYLHLIDGFHSEDSKFRWNA
RRDLALVNKGSDMLIEDLGIPEFWYQFPYKGLMLNTYGRWVKPGRVDQEDIFSSI
>gnl|CDD|215177 PLN02311, PLN02311, chalcone isomerase
LRMSCRNTDNAESIYHFPGKSPNRVSVLQTGNTVSDSPNSLLKHRHCNEISRVIVKSAAFSVGSAEYAEE
TATSVKFQRSLTLPGCSSPLSLLGTGYREKVFAIIGVKVYAAGLYVNPSILSGLSAWKGRSADEIQRDSS
LFSSIFQAPAEKSLQIVLVRDVDGKTFWDALDEAISPRIKAPSPDDTSALSTFRSIFQNRSLNKGTVIFL
TWINPSKMLVCISSEGLPSSVDATIESGNVTSALFDVFFGDSPVSPSLKASVANGLATTLK
>gnl|CDD|215178 PLN02312, PLN02312, acyl-CoA oxidase
MMAGMSPSAAARRAHVLANHLAQSPPSPNSSLTPSPCLQYSPPELNESYAFDVKEMRKLLDGHNLEDRDW
LFGLMMQSDLFNSKRRGGRVFVSPDYNQTMEQQREITMKRILYLLERGVFRGWLTETGPEAELRKLALLE
VIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYD
PKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHINGKNEGVHAFIAQIRDQDGNICPNIRIADCGH
KIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSGRVTIAVSAIYSS
KVGLAIAIRYSLSRRAFSVTPNGPEVLLLDYPSHQRRLLPLLAKTYAMSFAANDLKMIYVKRTPESNKAI
HVVSSGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEYV
SAKKRNKPFKGLGLEHMNGPRPVIPTQLTSSTLRDSQFQLNLFCLRERDLLERFASEVSELQSKGESREF
AFLLSYQLAEDLGRAFSERAILQTFLDAEANLPTGSLKDVLGLLRSLYVLISLDEDPSFLRYGYLSPDNV
ALVRKEVAKLCGELRPHALALVSSFGIPDAFLSPIAFDWIEANSWSSVQH
>gnl|CDD|177947 PLN02313, PLN02313, Pectinesterase/pectinesterase inhibitor
MAPIKKFISKFSDFKNNKKLILSSAAIALLLVAAVVGIAAGTTNQNKNRKITTLSSTSHAVLKSVCSSTL
YPELCFSAVAATGGKELTSQKEVIEASLNLTTKAVKHNYFAVKKLIAKRKGLTPREVTALHDCLETIDET
LDELHVAVEDLHQYPKQKSLRKHADDLKTLISSAITNQGTCLDGFSYDDADRKVRKALLKGQVHVEHMCS
NALAMIKNMTETDIANFELRDKSSSFTNNNNRKLKEVTGDLDSEGWPTWLSVGDRRLLQGSTIKADATVA
ADGSGDFTTVAAAVAAAPEKSNKRFVIHIKAGVYRENVEVTKKKKNIMFLGDGRGKTIITGSRNVVDGST
TFHSATVAAVGERFLARDITFQNTAGPSKHQAVALRVGSDFSAFYQCDMFAYQDTLYVHSNRQFFVKCHI
TGTVDFIFGNAAAVLQDCDINARRPNSGQKNMVTAQGRSDPNQNTGIVIQNCRIGGTSDLLAVKGTFPTY
LGRPWKEYSRTVIMQSDISDVIRPEGWSEWSGSFALDTLTYREYLNRGGGAGTANRVKWKGFKVITSDTE
AQKFTAGQFIGGGGWLASTGFPFSLSL
>gnl|CDD|215179 PLN02314, PLN02314, pectinesterase
MDSINSFKGYGKVDEAEEQAFRRKTRKRLIIIVVSVVVLVAIIIGAVVGTVVHKRKNESNPSPPPELTPA
TSLKAVCSVTRYPESCISSISSLPTSNTTDPETLFKLSLKVAIDELSKLSDLPQKLINETNDERLKSALR
VCETLFDDAIDRLNDSISSMQVGEGEKILSSSKIDDLKTWLSATITDQETCIDALQELSQNKYANSTLTN
EVKTAMSNSTEFTSNSLAIVSKILGILSDLGIPIHRRLLSFHHDLSSGFPSWVNIGDRRLLQEEKPTPNV
TVAKDGSGDVKTINEAVASIPKKSKSRFVIYVKEGTYVENVLLDKSKWNVMIYGDGKDKTIISGSLNFVD
GTPTFSTATFAAAGKGFIAKDMGFINTAGAAKHQAVAFRSGSDMSVFYQCSFDAFQDTLYAHSNRQFYRD
CDITGTIDFIFGNAAVVFQNCNIQPRQPLPNQFNTITAQGKKDPNQNTGISIQRCTISAFGNLTAPTYLG
RPWKDFSTTVIMQSYIGSFLNPLGWISWVSGVDPPSTIFYAEYQNTGPGSDVDKRVKWAGYKPNITDDEA
AKFTVATFIQGADWLPATSVTFQSSL
>gnl|CDD|177949 PLN02315, PLN02315, aldehyde dehydrogenase family 7 member
MGFARKEYEFLSEIGLSSRNLGCYVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAK
IWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIP
SERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEK
NNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDAD
IQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKN
FEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSV
PQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRST
CTINYGNELPLAQGINFG
>gnl|CDD|215180 PLN02316, PLN02316, synthase/transferase
MSTSKPKGSAPRGFAPRTTVESSQKRIQQNNGDKEDSSTSTSSLSVSAVEKTSNAKEEIQVDFQHNSESA
VEEVEAEDEIEVEQNQSDVLKSSSIVKEESISTDMDGIDDDSLDRKLKLERENLRKREIEELAEENFSRG
NKLFVYPQVVKPDSDIEVYLNRSLSTLANEPDVLIMGAFNGWRWKSFTERLEKTELGGDWWSCKLHIPKE
AYKMDFVFFNGQNVYDNNDHKDFCVEIEGGMDEHSFEDFLLEEKRRELEKLAKEEAERERQAEEQRRREE
EKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNVWYIEPSEFKAGDTVKLYYNRSSGPLAHSTEIWI
HGGYNNWIDGLSIVEKLVKSEEKDGDWWYAEVVVPERALVLDWVFADGPPGNARNYDNNGRQDFHAIVPN
NIPEELYWVEEEHQIYRKLQEERRLREEAIRAKAEKTARMKAEMKEKTLKMFLLSQKHIVYTEPLEVQAG
TTVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMVPADNGSHLKATVKVPLDAYMMDFVFSEK
EEGGIFDNRNGLDYHIPVFGGIAKEPPMHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPK
YDCLNLSHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVYFLEPQNGMFWAGCVYGCRNDGERFGFFCHAAL
EFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAHYGLSKARVVFTIHNLEFGANHIGKAMAYADKATTVSP
TYSREVSGNSAIAPHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLKQADL
PLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHSSHHDRARLCLTYDE
PLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTVFDVDHDKERAQAQGLEPNGFSF
DGADAAGVDYALNRAISAWYDGRDWFNSLCKRVMEQDWSWNRPALDYMELYHSARK
>gnl|CDD|215181 PLN02317, PLN02317, arogenate dehydratase
PQRLPPRTPRSGSSSFPARWASRRAAWQSSCAILSSKVRSPEGDAPPSRPAVESSGGAGLVVATQSVSFH
RDLSGLPRPLSITDLSPSPMHGSKLRVAYQGVPGAYSEAAARKAYPNCEAVPCEQFEAAFQAVELWLADR
AVLPIENSLGGSIHRNYDLLLRHRLHIVGEVQLPVHHCLLALPGVRKEELKRVISHPQALAQCENTLTKL
GVVREAVDDTAGAAKMVAANGLRDTAAIASARAAELYGLDILAEGIQDDSDNVTRFLMLAREPIIPRTDR
PFKTSIVFSLEEGPGVLFKALAVFALRDINLTKIESRPQRKRPLRVVDDSNSGTAKYFDYLFYVDFEASM
ADPRAQNALAHLQEFATFLRVLGSYPMDMTPL
>gnl|CDD|177952 PLN02318, PLN02318, phosphoribulokinase/uridine kinase
MAQDTSGAESPRRRHGLLKDQVQLVKRKDSDRYEIVPIQDPLSFEKGFFVVIRACQLLAQKNDGIILVGV
AGPSGAGKTVFTEKVLNFMPSIAVISMDNYNDSSRIIDGNFDDPRLTDYDTLLDNIHDLKAGKSVQVPIY
DFKSSSRVGYRTLEVPSSRIVIIEGIYALSEKLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEII
HQISETVYPMYKAFIEPDLQTAHIKIVNKFNPFSGFQNPTYILKSSRSVTVEQIKAVLSEDHTETTEETY
DIYLLPPGEDPETCQSYLRMRNRDGKYSLMFEEWVTDEPFIISPRITFEVSVRLLGGLMALGYTIATILK
RSSHVFSDDKVCVKIDWLEQLNRKYVQVQGKDRLVVKDVAEQLGLEGSYIPRTYIEQIQLEKLVNEVMAL
PEDLKTKLSLDDDLVSSPKEALSRASADRRNKNLKSGLSHSYSTQRDKNLSKLTGLAVTNRRFDERNSES
PAALNQGAITQLSEQISSLNERMDEFTSRIEELNSKLSIKKNSPSQQNLALQAEACNGSAPTSYFVSGLG
NGSLTGSILPLSSSSSQLAKESPLMEEILGIARGQRQVMHQLDNLSNLLHESLGERSGRNRRNSRLLNVD
SSQLPLILSLAIGGIGIFLFKRLKNV
>gnl|CDD|177953 PLN02319, PLN02319, aminomethyltransferase
ALWQLGQSLTRRAAQADKKALSRRYFASEANLKKTALYDFHVANGGKMVPFAGWSMPIQYKDSIMDSTLN
CRQNGSLFDVSHMCGLSLKGKDAIPFLETLVVADIAGLKDGTGTLSVFTNEKGGIIDDTVITKVTDDHIY
LVVNAGCRDKDLAHIEEHMKAFKAKGGDVSWHVHDERSLLALQGPLAAPVLQHLTKEDLSKMYFGDFRIT
DINGADCFLTRTGYTGEDGFEISVPSEHAVDLAKALLEKSEGKVRLTGLGARDSLRLEAGLCLYGNDLEE
HITPVEAGLAWTIGKRRRAEGGFLGADVILKQLKEGVSRRRVGFISSGAPARSHSEILDESGEKIGEVTS
GGFSPCLKKNIAMGYVKSGFHKAGTEVKVEVRGKMYDAVVTKMPFVPTKYYKPP
>gnl|CDD|177954 PLN02320, PLN02320, seryl-tRNA synthetase
SSRFIFLKPFTNTLTLGPFSRLTVSLLQRPHKPLLVRAFSASAAVQDIPATQKSDSSVARPQWKAAIDFK
WIRDNKEAVAINIRNRNSNANLELVLELYENMLALQKEVERLRAERNAVANKMKGKLEPSERQALVEEGK
NLKEGLVTLEEDLVKLTDELQLEAQSIPNMTHPDVPVGGEDSSAVRKEVGSPREFSFPIKDHLQLGKELD
LFDFDAAAEVSGSKFYYLKNEAVLLEMALVNWTLSEVMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNTQV
YSIDGSDQCLIGTAEIPVGGIHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFV
ICRPEESESFHEELIQIEEDLFTSLGLHFKTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTD
YQSRRLGIRYRPSEPPQTNPKKGKGSLGPTKFVHTLNATACAVPRMIVCLLENYQQEDGSVVIPEPLRPF
MGGLELIKPKSK
>gnl|CDD|215182 PLN02321, PLN02321, 2-isopropylmalate synthase
ILRSPNLSSATAASPAKSLSAFTPAPTRSSASSARFPAFLARPAAARSPSLASRASSALAASPSRPQVAR
RPRPEYIPNRIDDPNYVRIFDTTLRDGEQSPGATLTSKEKLDIARQLAKLGVDIIEAGFPIASPDDLEAV
KTIAKEVGNEVDEDGYVPVICGLSRCNKKDIDAAWEAVKHAKRPRIHTFIATSEIHMEHKLRKTPDEVVE
IARDMVKYARSLGCEDVEFSPEDAGRSDPEFLYRILGEVIKAGATTLNIPDTVGYTLPSEFGQLIADIKA
NTPGIENVIISTHCQNDLGLSTANTLAGAHAGARQVEVTINGIGERAGNASLEEVVMAIKCRGDEQLGGL
YTGINPVHITPTSKMVSEYTGMQVQPHKAIVGANAFAHESGIHQDGMLKHKGTYEIISPEDIGLFRGNDA
GIVLGKLSGRHALKSRLKELGYELDDDELDDVFKRFKAVAEKKKGVTDEDLIALVSDEVFQPEVVWKLLD
LQVTCGTLGLSTATVKLIGPDGVEHIACSVGTGPVDAAYKAVDLIVKEPVTLLEYSMNAVTEGIDAIATT
RVVIRGENSYSSTHAQTGESVQRTFSGSGADMDIVVSSVRAYVSALNKMLGFKEASKAKSASERSTSVVA
GE
>gnl|CDD|177956 PLN02322, PLN02322, acyl-CoA thioesterase
SASSNTKAIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKR
VAGIQLSINHLKSADLGDLVFAEATPVSTGKTIQVWEVKLWKTTDKDKANKILISSSRVTLICNLPIPDN
AKDAANMLRMQAKL
>gnl|CDD|215183 PLN02323, PLN02323, probable fructokinase
SMTAPSTAESSLVVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDE
FGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIF
HYGSISLITEPCRSAHLAAMKIAKEAGALLSYDPNLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEF
LTGGDDPDDDTVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLSQLAK
DLSLLEDEERLREALRFANACGAITTTERGAIPALPTKEAVLKLLKKAVA
>gnl|CDD|177958 PLN02324, PLN02324, triacylglycerol lipase
MVEGIPKRWKVLSGQNKWKGLLDPLDPDLRRYIIHYGEMSQVGYDAFNWDRKSKYAGDCYYSKNELFART
GFLKANPFRYEVTKYIYATASIKLPICFIVKSLSKDASRVQTNWMGYIAVATDQGKAMLGRRDIVVAWRG
TLQPYEWANDFDFPLESAISVFPVTDPKDNPRIGSGWLDIYTASDSRSPYDTTSAQEQVQGELKRLLELY
KNEEISITFTGHSLGAVMSVLSAADLVYGKKNKINISLQKKQVPITVFAFGSPRIGDHNFKNLVDSLQPL
NILRIVNVPDVAPHYPLLLYTEIGEVLEINTLNSTYLKRSLNFRNYHNLEAYLHGVAGMQDTQGEFKLEI
NRDIALVNKGLDALEDKYLVPGHWWVLENKGMVQSDDGTWKLNGDRSKKKQEEEDEKEENNCKFP
>gnl|CDD|215184 PLN02325, PLN02325, nudix hydrolase
METGEPIPRVAVVVFLLKGNSVLLGRRRSSIGDSTFALPGGHLEFGESFEECAAREVKEETGLEIEKIEL
LTVTNNVFLEEPKPSHYVTVFMRAVLADPSQVPQNLEPEKCYGWDWYEWDNLPEPLFWPLEKLVGSGFNP
FPHG
>gnl|CDD|215185 PLN02326, PLN02326, 3-oxoacyl-[acyl-carrier-protein] synthase III
PILRSGPVACASSRFAKRVRCSSVTTVDGASRPSASKYRRPRRVGSGSKLVGCGSAVPKLLITNDDLSKL
VDTSDEWIATRTGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCTSSPDDLFGSAPQVQA
ALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDRGTCILFGDGAGAVVL
QACDDDEDGLLGFDMHSDGNGHKHLHATFKGEDDDSSGGNTNGVGDFPPKKASYSCIQMNGKEVFKFAVR
CVPQVIESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAV
RSGKVKKGDVIATAGFGAGLTWGSAIVRW
>gnl|CDD|215186 PLN02327, PLN02327, CTP synthase
MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLD
LGNYERFLDVTLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPA
DVCVIELGGTVGDIESMPFIEALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLT
PHILACRSTKPLEENVKEKLSQFCHVPAENILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVAREPD
LEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKALLHASVACSRKLVIDWVAASDLEDETAKETP
DAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLGMQIAVIEFARSVLGLKDANS
TEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRHRYEVNPEMVPR
LEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLNSS
>gnl|CDD|215187 PLN02328, PLN02328, lysine-specific histone demethylase 1 homolog
METETKEPEDPADNVNDVVSEASSPETDLSLSPSQSEQNIENDGQNSPETQSPLTELQPSPLPPNTTLDA
PVSDSQGDESSSEQQPQNPNSTEPAPPPKKRRRRKRFFTEINANPAFRRHRVRGGLGKEVDVEALIAISV
GFPVDSLTEEEIEANVVSTIGGTEQANYIVVRNHILARWRSNVSNWLTRDHALESIRAEHKNLVDSAYNF
LLEHGYINFGVAPVIKEAQLRSFEGVEPANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTM
KMKGDGVVAAADLGGSVLTGINGNPLGVLARQLGLPLHKVRDICPLYLPDGKAVDAEIDSKIEASFNKLL
DRVCKLRQAMIEEVKSVDVNLGTALEAFRHVYKVAEDPQERMLLNWHLANLEYANASLMSNLSMAYWDQD
DPYEMGGDHCFIPGGNDTFVRELAKDLPIFYERTVESIRYGVDGVIVYAGGQEFHGDMVLCTVPLGVLKK
GSIEFYPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYSYSSVSGGP
LLIALVAGDAAVKFETLSPVESVKRVLQILRGIFHPKGIVVPDPVQAVCTRWGKDCFTYGSYSYVAVGSS
GDDYDILAESVGDGRVFFAGEATNKQYPATMHGAFLSGMREAANILRVARRRSLCIDDKVNNDEEEDDCL
DQLFDTPDLTFGSFSILFDPRSNDPESLSLLRVKFQGEKPDSCFLCLYGLVSRKQAIELGELDDDGKRNE
YLYEKFQVVLVGRKGLSQEGESLISSIKEARLNLQVFD
>gnl|CDD|215188 PLN02329, PLN02329, 3-isopropylmalate dehydrogenase
MAAFLQTNIRLNSIKIVPGRYSSLTDHQFRAPYRIRCAAASPGKKRYNIALLPGDGIGPEVISVAKNVLQ
KAGSLEGLEFDFQEMPVGGAALDLVGVPLPEETFTAAKQSDAILLGAIGGYKWDKNEKHLRPEMALFYLR
RDLKVFANLRPATVLPQLVDASTLKKEVAEGVDMMIVRELTGGIYFGEPRGITINENGEEVGVSTEIYAA
HEIDRIARVAFETARKRRGKLCSVDKANVLDASILWRKRVTALASEYPDVELSHMYVDNAAMQLIRDPKQ
FDTIVTNNIFGDILSDEASMITGSIGMLPSASLGESGPGLFEPIHGSAPDIAGQDKANPLATILSAAMLL
KYGLGEEKAAKRIEDAVVDALNKGFRTGDIYSPGNKLVGCKEMGEEVLKSVDSKVPATV
>gnl|CDD|215189 PLN02330, PLN02330, 4-coumarate--CoA ligase-like 1
CHMEIQKQEDNEHIFRSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAK
ALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGK
VKGLGLPVIVLGEEKIEGAVNWKELLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLV
ANLCSSLFSVGPEMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAP
IVPPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHGD
PEKGHGIAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLH
TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINP
KAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSINKAN
>gnl|CDD|177965 PLN02331, PLN02331, phosphoribosylglycinamide formyltransferase
KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDEL
VDALRGAGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKGYYGIKVHKAVIASGARYSGPTV
HFVDEHYDTGRILAQRVVPVLATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDGVPLIRSKE
>gnl|CDD|215190 PLN02332, PLN02332, membrane bound O-acyl transferase (MBOAT) family protein
QRAVMESLASAIGVSVPVLRFLLCFVASIPLSALWRFIPSGTLRHLYAALSGAFLSYLSFGFSSNLHFVV
PMIAGYLAMALARRRCGAITFLFAFAYLIYCHVFYMSGDAWKEGGIDFTGALMVLTLKVISCAMNYQDGL
LKEEGLREAQKKNRLIQLPSLIEYLGYCLCCGSHLAGPVFEFRDYLDWTEGKGLWDPNAKGKCPSPYGAT
LRALLQAAICMGLYLYLTPQFPLSRFTEPDYQEWGFWHRFGYQYMSGFTARWKYYFIWSISEAAIIISGL
GFSGWDGEGKPKAKWDRAKNVDILGVELAKSAVQIPLVWNIQVSTWLRHYVYERLVPKGKKPGFFQLLAT
QTVSAVWHGLYPGYILFFVQSALMIAGSRVIYRWQQAIPPSMALARNLLVFINFLYTVLVLNYSCVGFML
LSLDETLAAYGSVYYIGTIIPVVLILLGSVVKPKRKARPKSRKEE
>gnl|CDD|215191 PLN02333, PLN02333, glucose-6-phosphate 1-dehydrogenase
MATLSSSHSCPYARSYSYSLSPSSSSSHSSVVDPHRSLSFLSAIPQGLNPAKLCVRSQRNSYQNVVLMQD
GAVATPSNPVENDSSFKKLKDGLLSSIPSSEEDKVVAEFDGNKDESTVSITVVGASGDLAKKKIFPALFA
LYYEGCLPEHFTIFGYARSKMTDAELRNMVSKTLTCRIDKRENCGEKMEEFLKRCFYHSGQYDSQEHFAE
LDKKLKEHEGGRVSNRLFYLSIPPNIFVDAVKCASSSASSVNGWTRVIVEKPFGRDSESSAALTKSLKQY
LEEDQIFRIDHYLGKELVENLSVLRFSNLIFEPLWSRQYIRNVQFIFSEDFGTEGRGGYFDNYGIIRDIM
QNHLLQILALFAMETPVSLDAEDIRNEKVKVLRSMRPIQLEDVVIGQYKSHTKGGVTYPAYTDDKTVPKG
SLTPTFAAAALFIDNARWDGVPFLMKAGKALHTKSAEIRVQFRHVPGNLYNRNFGTDLDQATNELVIRVQ
PDEAIYLKINNKVPGLGMRLDRSNLNLLYAARYSKEIPDAYERLLLDAIEGERRLFIRSDELDAAWALFT
PLLKELEEKKIIPEYYPYGSRGPVGAHYLAARYKVRWGDLSIEQ
>gnl|CDD|215192 PLN02334, PLN02334, ribulose-phosphate 3-epimerase
DKFSKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDC
HLMVTNPEDYVPDFAKAGASIFTFHIEQASTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKGLV
DMVLVMSVEPGFGGQSFIPSMMDKVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPD
YAEVISGLRASVEKAAVAV
>gnl|CDD|177969 PLN02335, PLN02335, anthranilate synthase
MAESNSIPSVVINSSKQNGPIIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISP
GPGTPQDSGISLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSPVHYDEKGEEGLFSG
LPNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQGVQFHPESIITTEGKTIVRNFI
KIIEKKESEKLT
>gnl|CDD|177970 PLN02336, PLN02336, phosphoethanolamine N-methyltransferase
KEHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIES
VIKKNESINGHYKNVKFMCADVTSPDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFF
RESCFHQSGDSKRKNNPTHYREPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLW
QKVSSTNDKGFQRFLDNVQYKSSGILRYERVFGEGFVSTGGLETTKEFVDKLDLKPGQKVLDVGCGIGGG
DFYMAENFDVHVVGIDLSVNMISFALERAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRDTILHIQDKPA
LFRSFFKWLKPGGKVLISDYCRSPGTPSPEFAEYIKQRGYDLHDVQAYGQMLKDAGFDDVIAEDRTDQFL
QVLQRELDAVEKEKDEFISDFSEEDYNDIVGGWKAKLVRSSSGEQKWGLFIAKKK
>gnl|CDD|215193 PLN02337, PLN02337, lipoxygenase
MLGGIIDAITGSNNKTKKEKIKGTVVLMKKNVLDFNDFNASVLDRVHELLGKGVSLQLISSTVVDPENGL
RGKLGKEAYLEKWITTITSLTAGESAFKVTFDWDEKIGVPGAFIIKNNHHSEFYLKTVTLEDVPGHGRVH
FVCNSWIYPAKRYRYDRVFFSNKTYLPSQTPAPLRPYREEELVNLRGDGKGELKEWDRVYDYDYYNDLGD
PDKGNPYARPVLGGSQEYPYPRRGRTGRKPTKTDPNSESRLPLLSLNIYVPRDERFGHLKMSDFLAYALK
AIAQVLVPELEALFDKTPNEFDSFEDVLKLYEGGIKLPNGPLLEELRKNIPLEMLKELLRTDGEYLLKFP
MPQVIKEDKSAWRTDEEFAREMLAGVNPVVIRRLTEFPPKSKLDPKKYGDQNSSITEEHIEKNLEGLTVQ
EALEKNRLFILDHHDALMPYLRRINSTSTKTYATRTLLFLKDDGTLKPLAIELSLPHPQGDKFGAVSKVY
TPAEDGVEGSVWQLAKAYVAVNDSGYHQLISHWLNTHAVIEPFVIATNRQLSVLHPIHKLLHPHFRDTMN
INALARQILINAGGILESTVFPGKYALEMSSVVYKNWNFTEQALPADLIKRGVAVEDPSSPHGVRLLIED
YPYAVDGLEIWSAIETWVKEYCAFYYPTDDMVQGDTELQSWWKEVREEGHGDLKDEPWWPKMQTVAELIE
SCTIIIWIASALHAAVNFGQYPYAGYLPNRPTVSRRFMPEPGTPEYEELEKNPDKAFLKTITAQLQTLLG
ISLIEILSRHSSDEVYLGQRDTPEWTSDAEPLEAFKRFGERLVEIENRIVDMNKDPRLKNRVGPVKMPYT
LLYPNTSDYTGEGGLTGKGIPNSVSI
>gnl|CDD|177972 PLN02338, PLN02338, 3-phosphoshikimate 1-carboxyvinyltransferase
AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSEN
NRAVVEGCGGKFPVSGDSKEDVELFLGNAGTAMRPLTAAVTAAGGNASYVLDGVPRMRERPIGDLVDGLK
QLGADVECTLGTNCPPVRVNAAGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVE
MTLKLMERFGVSVEHSDSWDRFFIKGGQKYKSPGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQ
GDVKFAEVLEKMGAKVEWTENSVTVTGPPRDAFGGKHLKAIDVNMNKMPDVAMTLAVVALFADGPTAIRD
VASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAEIDTYDDHRMAMAFSLAACGDVPVTI
NDPGCTRKTFPTYFDVLESIAKH
>gnl|CDD|177973 PLN02339, PLN02339, NAD+ synthase (glutamine-hydrolysing)
MRLLKVATCNLNQWAMDFDGNLKRIKESIAEAKAAGAVYRVGPELEITGYGCEDHFLELDTVTHSWECLA
EILVGDLTDGILCDIGMPVIHGGVRYNCRVFCLNRKILLIRPKMWLANDGNYRELRWFTAWKHKKKVEDF
QLPEEIAEATSQKSVPFGDGYLQFLDTAVAAETCEELFTPQAPHIDLALNGVEIISNGSGSHHQLRKLNT
RLDLIRSATHKCGGVYLYANQRGCDGGRLYYDGCACIVVNGEVVAQGSQFSLQDVEVVTACVDLDAVVSF
RGSISSFREQASSKKRVPSVAVPFKLCPPFSLSLVPSSPLKIRYHSPEEEIALGPACWLWDYLRRSGASG
FLLPLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGNYADGEVPTDSKEFAKRIFYTVYMGS
ENSSEETRSRAKQLADEIGSSHLDVKIDGVVSAVLSLFQTLTGKRPRYKVDGGSNAENLALQNIQARIRM
VLAFMLASLLPWVRGKSGFLLVLGSANVDEGLRGYLTKYDCSSADINPIGGISKQDLRSFLRWAATNLGY
PSLAEVEAAPPTAELEPIRDDYSQTDEEDMGMTYEELGVYGRLRKIFRCGPVSMFKNLCHEWNGRLSPSE
VAAKVKDFFKYYSINRHKMTTLTPSYHAESYSPDDNRFDLRQFLYNTRWPYQFRKIDELVEELDGETVAE
>gnl|CDD|215194 PLN02340, PLN02340, endoglucanase
MRKTSLSLGGAALLLLVLAAAASAAAEAFNYGGALDKTLLFFEAQRSGKLPANQRVKWRGDSGLKDGFLQ
GVDLVGGYYDAGDHVKFGLPMAFAVTMLSWGAVDFRKEITALNQMQRTLWAIRWGTDYFIKAHTQPNVLW
GQVGDGDSDHYCWERAEDMTTPRTAYKLDQNHPGSDLAGETAAALAAASKAFKPYNSSYSDLLLVHAKQL
FSFADKFRGLYDDSIQNAKKFYTSSGYSDELLWAAAWLYRATGDEYYLKYVVDNAVYMGGTGWAVKEFSW
DNKYAGVQILLSKILLEGRGGAYTSTLKQYQAKADYFACACLQKNGGYNIQLTPGGLMYVREWNNLQYAS
SAAFLLAVYSDYLSAANAKLRCPDGLVQPQELLDFARSQADYILGKNPKGMSYMVGYGPKYPIHVHHRGS
SIPSIFALHSTVGCVQGFDSWYRRKEADPNVIYGALVGGPDANDNFSDDRSNYEQTEPTLSGNAPLVGLF
AKLQSASETADAYGSYKPTPNTSSPKQSGAPVEFVHSITNTWTAGGTTYYRHKVIIKNKSQKPITDLKLV
IEDLSGPIWGLNPTKEKNTYELPQWQKVLQPGSQLSFVYVQGGPQAKVSVLSYN
>gnl|CDD|215195 PLN02341, PLN02341, pfkB-type carbohydrate kinase family protein
MQAHRLIGQLGAFSPHPGLSSPPSPHGHLVPRRVCSRCRASARASSRARAGARSRARRRLGDTEVGSAAG
KEIDVATLGNLCVDIVLPVPELPPPSREERKAYMEELAASPPDKKSWEAGGNCNFAIAAARLGLRCSTIG
HVGDEIYGKFLLDVLAEEGISVVGLIEGTDAGDSSSASYETLLCWVLVDPLQRHGFCSRADFGPEPAFSW
ISKLSAEAKMAIRQSKALFCNGYVFDELSPSAIASAVDYAIDVGTAVFFDPGPRGKSLLVGTPDERRALE
HLLRMSDVLLLTSEEAEALTGIRNPILAGQELLRPGIRTKWVVVKMGSKGSILVTRSSVSCAPAFKVNVV
DTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGAATAMGCGAGRNVATLEKVLELLRASNLNEDDTFWA
ELLKNSDCSEISFLSKMAINGGSNGIVRVAATKVVSELLPSLEEARERGI
>gnl|CDD|177976 PLN02342, PLN02342, ornithine carbamoyltransferase
MFFSLRRARSPSAVSSSSRARRGLVVCAASSSAAAPSPIKGKSKPKHFLHIDDFDKEEILGLLDRAKEVK
ALLKSGDRSFQPFKGKSMAMIFTKPSMRTRVSFETGFFLLGGHALYLGPDDIQLGKREETRDIARVLSRY
NDIIMARVFAHQDVLDLAEYSSVPVINGLTDYNHPCQIMADALTIIEHIGRLEGTKVVYVGDGNNIVHSW
LLLAAVLPFHFVCACPKGYEPDAKTVEKARAAGISKIEITNDPAEAVKGADVVYTDVWASMGQKEEAEKR
KKAFQGFQVNEALMKLAGPQAYFMHCLPAERGVEVTDGVMEAPNSIVFPQAENRMHAQNAIMLHQLGK
>gnl|CDD|177977 PLN02343, PLN02343, allene oxide cyclase
FHRSSLLGFSRSFQNLGISSNGPDFSSRSSFTTSKNLTVTRALFSNKANENPRPTKVQELSVYEINERDR
GSPAFLKLSKKSVENALGDLVPFTNKLYTGDLKKRLGITAGLCVLIQHVPEKKGDRYEAIYSFYFGDYGH
ISVQGPYLTYEDTYLAITGGSGIFEGAYGQVKLHQIVFPFKLFYTFYLKGIPDLPEELTGTPVPPSPDVE
PAPEAKACEPSSVIPNFTN
>gnl|CDD|177978 PLN02344, PLN02344, chorismate mutase
SRSLVPKSAARASLSLSASASAMSLTGKDRVDESEVLSLDSIRSSLIRQEDTIIFSLIERAQFPYNAPTY
DPNAFGVPGFHGSLVEFMVRETEALHAKVGRYKSPDEHPFFPEDLPEPVLPPLQYPQVLHPAADSININK
AIWDMYFNDLLPLLVKEGDDGNYGSTAVCDLACLQALSKRIHYGKFVAEAKFRESPEEYEPAIRAQDADG
LMKLLTFEAVEEAVKKRVEKKARTFGQEVTLSGEEDGADPKYKVDPSLVARLYGEWIMPLTKEVQVEYLL
RRLD
>gnl|CDD|177979 PLN02345, PLN02345, endoglucanase
ALKIALQFFDIQKSGKLENNPIPWRGDSALLDGSDAGLDLSKGMYDAGDHMKFGFPMAFTATVLSWSILE
YGDQMNAANQLDSAKDSLKWITDYLINAHPSENVLYIQVGDPKLDHKCWERPETMDEKRPLTKINTSSPG
SEVAAETAAAMAAASLVFKSSDSTYSDTLLKHAKQLFNFADKYRGSYSESIPEVQDYYNSTGYGDELLWA
ASWLYHATGDKTYLAYVTGKNGKEFADWGSPTWFSWDDKLAGTQVLLSRLTFFGPKGASNTVNSGLQMYK
KTAEAVMCGLLPDSPTATTSRTDGGLIWVSEWNALQHAVNSAFLAVLYSDYMLSSGIAKLSCSGKSFKPS
DLRKFAKSQADYILGKNPMKMSYLVGYGDKYPQYVHHRGASIPADAKTGCKDGFKWLHSSEPNPNVATGA
LVGGPFQNDTFVDSRDNSMQNEPTTYNSALLVGLLSSLVTTSSVLQSFT
>gnl|CDD|215196 PLN02346, PLN02346, histidine biosynthesis bifunctional protein hisIE
PRSSVFSPASPCRRDRKISAASKAAAGSKTLAEPALEPKVESLLDSVKWDDKGLAVAIAQNVDTGAILMQ
GFANREAISATISSRKATFYSRSRSGLWTKGETSGNFINVHDIYLDCDRDSIIYLGTPDGPTCHTGAETC
YYTSVDDALQNGGPHGNKLALTTLYSLEETIQQRKEEAVPQGGKPSWTKRLLQDPELLCSKIREEAGELC
QTLEENEGKERTASEMADVLYHAMVLLAKQGVKMEDVLEVLRKRFSQSGIEEKASRPPKSK
>gnl|CDD|215197 PLN02347, PLN02347, GMP synthetase
MESEAAKSYLDVVLILDYGSQYTHLITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPHSVHVEG
APTVPEGFFDYCRERGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFGDLPSGETQTV
WMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFLFDVCGVTADWK
MQDVLEEQIELIKATVGPDEHVICALSGGVDSTVAATLVHKAIGDRLHCVFVDNGLLRYKEQERVMETFK
RDLHLPVTCVDASERFLSKLKGVTDPEKKRKIIGAEFIEVFDEFAHKLEQKLGKKPAFLVQGTLYPDVIE
SCPPPGSGRTHSHTIKSHHNVGGLPKDMKLKLIEPLKLLFKDEVRKLGRLLGVPEAFLKRHPFPGPGLAV
RVLGDVTEGNALDILRQVDEIFINSIKDAGLYDEIWQAFAVFLPVKSVGVQGDQRTHSHVVALRAVTSED
GMTADWYHFEHKFLDDVSRKICNEVRGVNRVVYDITSKPPSTIEWE
>gnl|CDD|215198 PLN02348, PLN02348, phosphoribulokinase
MAFATVSSTASLNATSSITTPTKSNLGSRRSKSPAASSVVVALAADDGTVVIGLAADSGCGKSTFMRRLT
SVFGGAAKPPKGGNPDSNTLISDTTTVICLDDYHSLDRTGRKEKGVTALDPRANNFDLMYEQVKALKEGK
AVEKPIYNHVTGLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAWKIQRDMAERGH
SLESIKASIEARKPDFDAYIDPQKQYADVVIEVLPTQLIPDDNEGKVLRVRLIMKEGVKNFDPVYLFDEG
STISWIPCGRKLTCSYPGIKFFYGPDTYFGHEVSVLEMDGQFDKLDELIYVESHLSNTSTKFYGEVTQQM
LKHADFPGSNNGTGLFQTIVGLKIRDLYERIVAKRKVAAGEATAA
>gnl|CDD|215199 PLN02349, PLN02349, glycerol-3-phosphate acyltransferase
SSSSVSVAPARTAILPALLSLRLSTSKATLPPLRATGRVSARGRSPLVTDKESSVAASIAAAETATSSPL
EDLKSHTFKDARSEQELLAGIKKEVEAGRLPANVAAGMEELYANYKNAVLSSGAPNADEIVVSNMASILD
RVLLGVEDPFTFPPYHKALREPFDYYMFGQNYIRPLIDFRNSYLGNRSRFDKVEEQLQQGHNVVLLSNHQ
SEADPAVIALLLEKSHPYLAENVTYVAGDRVVTDPLCKPFSMGRNLICVHSKKHMNDDPELKEMKRKANT
RTLKEMALLLREGGQLIWIAPSGGRDRPDPLTGEWTPAPFDPSAVDNMRRLTEKSKAPGHFYPLAMLSYD
IMPPPPQVEKEIGERRLVGFTGVGLSVGEEIDFSDITAACEGGAEAREAFTQAAYASVVEQYAVLKSAIH
GGQGLA
>gnl|CDD|215200 PLN02350, PLN02350, phosphogluconate dehydrogenase (decarboxylating)
MASAALSRIGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETVERAKKEGNLPLYGFKDPEDFVLSI
QKPRSVIILVKAGAPVDQTIKALSEYMEPGDCIIDGGNEWYENTERRIKEAAEKGLLYLGMGVSGGEEGA
RNGPSLMPGGSFEAYKNIEDILEKVAAQVDDGPCVTYIGPGGAGNFVKMVHNGIEYGDMQLISEAYDVLK
SVGGLSNEELAEVFAEWNKGELESFLIEITADIFSVKDDKGDGYLVDKILDKTGMKGTGKWTVQQAAELS
VAAPTIAASLDARYLSGLKEERVAAAKVFKEAGLEDILSADSGVDKKQLIDDVRQALYASKICSYAQGMN
LIRAKSVEKGWNLNLGELARIWKGGCIIRAVFLDRIKKAYDRNPDLASLLVDPEFAKEMVERQAAWRRVV
SLAINAGISTPGMSASLAYFDTYRRARLPANLVQAQRDYFGAHTYERVDRPGSFHTEWTKLARKSKIITG
RTA
>gnl|CDD|215201 PLN02351, PLN02351, cytochromes b561 family protein
MATVDSSSLLPLLLFARLSGLVVAVLVLYWALFFKSSFLPQSTSQEDLVYAVLHPLLMVIGFILISGEAI
LVHRWLPGSRKTKKSVHLWLQGLALASGVFGIWTKFHGQDGIVANFYSLHSWMGLICVSLFGAQWLTGFM
SFWHRGEMRTTRTTVLPWHVFLGLYTYGLAVATAETGLLEKLTFLQTKRNVSKHGSESMVVNGLGLGLAL
LSGIVILAAVLPKYQSHSSKLVYSSQDKCLSS
>gnl|CDD|215202 PLN02352, PLN02352, phospholipase D epsilon
MEEKQKFFHGTLEATIFDATPYTPPFPFNCIFLNGKATYVTIKIGNKKVAKTSHEYDRVWNQTFQILCAH
PLDSTITITLKTKCSILGRFHIQAHQIVTEASFINGFFPLIMENGKPNPELKLRFMLWFRPAELEPTWCK
ILENGSFQGLRNATFPQRSNCHVILYQDAHHCSTFQPPVDLCGSPRKLWEDVYKAIEGAKHLIYIAGWSF
NPKMVLVRDPETDIPHARGVKLGELLKRKAEEGVAVRVMLWDDETSLPIIKNKGVMGTHDEDAFAYFKHT
KVVCKLCPRLHKKFPTLFAHHQKTITVDTRANDSISEREIMSFVGGLDLCDGRYDTEEHSLFRTLNTESH
CQDFYQTSIAGAKLQKGGPREPWHDAHACIVGEAAWDVLTNFEQRWTKQCNPSVLVPTSSIRNLVHQPGS
SESNNRNWKVQVYRSIDHVSASHMPRNLPVERSIHEAYVEAIRRAERFIYIENQYFIGGCHLWEKDNHCG
CTNLIPIEIALKIASKIRAKERFAVYILIPMWPEGVPESEPVQDILHWTRETMAMMYKLIGEAIQESGEP
GHPRDYLNFFCLANREEKRKGEFVPPYSPHQKTQYWNAQKNRRFMVYVHSKLMIVDDTYILIGSANVNQR
SMDGCRDTEIAIGCYQSKNGTNTNNPRDIQAYRMSLWYEHTGLDEESFLEPESLECVRRLRTIGEQMWEI
YSGEEVVDMEGVHLVNYPISVTKDGAVEDLADGDGNFPDTKTPVKGRRSKMLPPVFTT
>gnl|CDD|177986 PLN02353, PLN02353, probable UDP-glucose 6-dehydrogenase
MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFST
DVEKHVAEADIVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKI
LTHNSKGINFQILSNPEFLAEGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLW
SAELSKLAANAFLAQRISSVNAMSALCEATGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNL
VYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFNTVSGKKIAVLGFAFKKDTGDTRETPAIDVC
KGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRHLQPMSPTAVKQVSVVWDAYEATKGAHGICILT
EWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGKPLDPWL
>gnl|CDD|177987 PLN02354, PLN02354, copper ion binding / oxidoreductase
MMGGRLLAVLLCLAAAVALVVRAEDPYFFFTWNVTYGTASPLGVPQQVILINGQFPGPNINSTSNNNIVI
NVFNNLDEPFLLTWSGIQQRKNSWQDGVPGTNCPIPPGTNFTYHFQPKDQIGSYFYYPSTGMHRAAGGFG
GLRVNSRLLIPVPYADPEDDYTVLIGDWYTKSHTALKKFLDSGRTLGRPDGVLINGKSGKGDGKDEPLFT
MKPGKTYRYRICNVGLKSSLNFRIQGHKMKLVEMEGSHVLQNDYDSLDVHVGQCFSVLVTANQAPKDYYM
VASTRFLKKVLTTTGIIRYEGGKGPASPELPEAPVGWAWSLNQFRSFRWNLTASAARPNPQGSYHYGKIN
ITRTIKLVNSASKVDGKLRYALNGVSHVDPETPLKLAEYFGVADKVFKYDTIKDNPPAKITKIKIQPNVL
NITFRTFVEIIFENHEKSMQSWHLDGYSFFAVAVEPGTWTPEKRKNYNLLDAVSRHTVQVYPKSWAAILL
TFDNAGMWNIRSENWERRYLGQQLYASVLSPERSLRDEYNMPENALLCGKVKGLPKPPPYSI
>gnl|CDD|215203 PLN02355, PLN02355, probable galactinol--sucrose galactosyltransferase 1
MTVGAGISVADGNLVVLGNRVLHDVHDNVLVTPASGGALINGAFIGVRSDQVGSRRVFPVGKLEDLRFMC
VFRFKLWWMTQRMGTCGQDIPFETQFLIVEARDGSHLGNGGEGGEDQSSVYTVFLPILEGDFRAVLQGNE
HNELEICLESGDPAVDEFEGSHLVFVAAGSDPFDVITNAVKAVEKHLQTFSHRERKKMPDMLNWFGWCTW
DAFYTNVTAEGVKQGLESLEKGGVTPKFVIIDDGWQSVGMDPTGIECLADNSANFANRLTHIKENHKFQK
NGKEGHRVDDPALGLGHIVTEIKEKHSLKYVYVWHAITGYWGGVKPGVAGMEHYESKMSYPVSSPGVQSN
EPCDALESITTNGLGLVNPEKVFSFYNELHSYLASAGIDGVKVDVQNILETLGAGHGGRVKLARKYHQAL
EASIARNFPDNGIISCMSHNTDGLYSAKRTAVIRASDDFWPRDPASHTIHIASVAYNTIFLGEFMQPDWD
MFHSLHPMAEYHAAARAVGGCAIYVSDKPGQHDFNLLKKLVLPDGSILRAKLPGRPTRDCLFSDPARDGK
SLLKIWNLNEFTGVIGVFNCQGAGWCRVGKKNLIHDEQPGTITGVIRAKDVDYLPKVADDEWTGDSIVYS
HLGGEVVYLPKDASLPVTLKSREYEVFTVVPVKELSNGVKFAPIGLVKMFNSGGAIKELRYDEDTNATVR
MKVRGSGLVGAYSSSRPRRVTVDSKEVEFRYEEGSGLVTFDLGVPEEELYLWNVTVEL
>gnl|CDD|215204 PLN02356, PLN02356, phosphateglycerate kinase
MAPVNMTGAVVAAASLLMLLSYSFLLCNSRKRKTKKPLSKKKPRNGLIDAIGNTPLIRINSLSEATGCEI
LGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGCKCHVVIPDDVAI
EKSQILEALGATVERVRPVSITHKDHYVNIARRRALEANELASKRRKGSETDGIHLEKTNGCISEEEKEN
SLFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKC
FLIDPPGSGLFNKVTRGVMYTREEAEGRRLKNPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMS
RYLLKNDGLFVGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLSKFHDPQYLSQHGLTPTATGLEF
LGI
>gnl|CDD|215205 PLN02357, PLN02357, serine acetyltransferase
LRSSSPHISLHSFLLPPFSCTSTFSLPKSRPMAACIDTCRTGTSQLSPKHHDDDSHFYYIKNFCRPSFSP
FSGNHTKTIHTRPVEDDLDRDDDVWLKIQEEAKSDVEQEPILSSYYYASILSHRSLESALANHLSVKLSN
LNLPSNTLFDLFIGVLEESPEIIESVKQDLRAVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGR
KILALLIQNRVSEAFAVDIHPGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPK
IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIGGKENPIKHDKIPSLTMDQTS
HISEWSDYVI
>gnl|CDD|165999 PLN02358, PLN02358, glyceraldehyde-3-phosphate dehydrogenase
MADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHELKVKDDKT
LLFGEKPVTVFGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVN
EHEYKSDLDIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNI
IPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGY
TEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYSSRVVDLIVHMSKA
>gnl|CDD|166000 PLN02359, PLN02359, ethanolaminephosphotransferase
MGYIGAHGVAALHRYKYSGVDHSYVAKYVLQPFWSRFVNFFPLWMPPNMITLMGFMFLLTSALLGYIYSP
HLDTPPPRWVHFAHGLLLFLYQTFDAVDGKQARRTNSSSPLGELFDHGCDALACAFETMAFGSTAMCGRD
TFWFWVISAVPFYGATWEHFFTNTLILPVINGPTEGLMLIYCAHFFTAIVGAEWWAQDFGKSIPFLSWVP
FVSEIQTYRIVLFLMIAFAVIPTVAFNVSNVYKVVQARKGSMLLALAMLYPFVTLLGGVLIWDYLSPSDL
MRNYPHLVVLGTGLAFGFLVGRMILAHLCDEPKGLKTNMCMSLLYLPFAIANALTARLNDGVPLVDEFWV
LLGYCAFTVSLYLHFATSVIHEITTALGIYCFRITRKEA
>gnl|CDD|166001 PLN02360, PLN02360, probable 6-phosphogluconolactonase
MAHSYVHKDRGEIRVHENLDELSTDLAEYIAELSEASVKERGVFAIALSGGSLISFMGKLCEAPYNKTVD
WAKWYIFWADERVVAKNHADSNYKLAKDGLLSKVPVVPSHVYSINDTVTAEEAATDYEFAIRQLVKTRTI
GVSDISDCPKFDLILLGMGSDGHVASLFPNHPALEEKDDWVTFITDSPKPPPERITFTLPVINSASNVAV
VATGESKANAVHLAIDDVTEGPDAPSLPARMVQPTKGKLVWFLDKPAASKLDGFQFSE
>gnl|CDD|177990 PLN02361, PLN02361, alpha-amylase
TDNGAVIRNGREILLQAFNWESHKHDWWRNLEGKVPDLAKSGFTSAWLPPPSQSLAPEGYLPQNLYSLNS
AYGSEHLLKSLLRKMKQYNVRAMADIVINHRVGTTQGHGGMYNRYDGIPLPWDEHAVTSCTGGLGNRSTG
DNFNGVPNIDHTQHFVRKDIIGWLIWLRNDVGFQDFRFDFAKGYSAKFVKEYIEAAKPLFSVGEYWDSCN
YSGPDYRLDYNQDSHRQRIVNWIDGTGGLSAAFDFTTKGILQEAVKGQWWRLRDAQGKPPGVMGWWPSRA
VTFIDNHDTGSTQAHWPFPSDHIMEGYAYILTHPGIPTVFYDHFYDWGGSIHDQIVKLIDIRKRQDIHSR
SSIRILEAQSNLYSAIIDEKLCMKIGDGSWCPSGREWTLATSGHRYAVWHK
>gnl|CDD|215206 PLN02362, PLN02362, hexokinase
MGKVAVGLAAAAAVAACAVAAVMVGRRVKSRRKWRRVVGVLKELEEACETPVGRLRQVVDAMAVEMHAGL
ASEGGSKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTS
EVLFDFIASSLKQFVEKEENGSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAEC
LQGALNRRGLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGLLTTSGSMV
VNMEWGNFWSSHLPRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIFGPVSSRLST
PFVLRTPSVAAMHEDDSPELQEVARILKETLGISEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKI
GRDGSGGITSGRSRSDIQIMRRTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVILKATEDGSGIG
SALLAASYSSYSVDTVQLL
>gnl|CDD|215207 PLN02363, PLN02363, phosphoribosylanthranilate isomerase
SKTSKSGLSNRKVSFSRVGYAQNRKLSCSVSSENVAPKDDERGKDRPLVKMCGITSARDAAMAVEAGADF
IGMILWPKSKRSISLSVAKEISQVAREGGAKPVGVFVDDDANTILRAADSSDLELVQLHGNGSRAAFSRL
VRERKVIYVLNANEDGKLLNVVPEEDCHLADWILVDSATGGSGKGFNWQNFKLPSVRSRNGWLLAGGLTP
ENVHEAVSLLKPTGVDVSSGICGPDGIRKDPSKISSFISAVKSVAY
>gnl|CDD|166005 PLN02364, PLN02364, L-ascorbate peroxidase 1
MTKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGA
NSGIHIALRLLDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDH
LRDVFAKQMGLSDKDIVALSGAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKA
LLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELGFADA
>gnl|CDD|177993 PLN02365, PLN02365, 2-oxoglutarate-dependent dioxygenase
MAEVNIPTIDLEEFPGQIEKLREACERWGCFRVVNHGVSLSLMAEMKKVVRSLFDLPDEVKRRNTDVILG
SGYMAPSEVNPLYEALGLYDMASPQAVDTFCSQLDASPHQRETIKKYAKAIHDLAMDLARKLAESLGLVE
GDFFQGWPSQFRINKYNFTPETVGSSGVQIHTDSGFLTILQDDENVGGLEVMDPSSGEFVPVDPLPGTLL
VNLGDVATAWSNGRLCNVKHRVQCKEATMRISIASFLLGPKDDDVEAPPEFVDAEHPRLYKPFTYEDYRK
LRLSTKLHAGEALALITAKS
>gnl|CDD|215208 PLN02366, PLN02366, spermidine synthase
AAAPESEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLT
ERDECAYQEMITHLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAV
GFDDPRVNLHIGDGVEFLKNAPEGTYDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMW
LHMDLIEDLIAICRETFKGSVNYAWTTVPTYPSGVIGFVLCSKEGPAVDFKHPVNPIDKLEGAGKAKRPL
KFYNSEVHRAAFCLPSFAKRELESLLTS
>gnl|CDD|177995 PLN02367, PLN02367, lactoylglutathione lyase
SYSIATAISRLSPLILIVKPYSSGSSFITCFCNSTRKPKRFDRLRVFSMASEPKESPANNPGLSTSPDEA
TKGYIMQQTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDTASAPTDPTERTVWTFGQK
ATIELTHNWGTESDPDFKGYHNGNSEPRGFGHIGITVDDVYKACERFEELGVEFVKKPNDGKMKGIAFIK
DPDGYWIEIFDLKTIGTTTVNAA
>gnl|CDD|177996 PLN02368, PLN02368, alanine transaminase
MSLKALDYESLNENVKKCQYAVRGELYLRASELQKEGKKIIFTNVGNPHALGQKPLTFPRQVVALCQAPF
LLDDPNVGLLFPADAIARAKHYLSLTSGGLGAYSDSRGLPGVRKEVAEFIERRDGYPSDPELIFLTDGAS
KGVMQILNAVIRGEKDGVLVPVPQYPLYSATISLLGGTLVPYYLEESENWGLDVNNLRQSVAQARSKGIT
VRAMVIINPGNPTGQCLSEANLREILKFCYQERLVLLGDEVYQQNIYQDERPFISAKKVLMDMGPPISKE
VQLVSFHTVSKGYWGECGQRGGYFEMTNIPPKTVEEIYKVASIALSPNVSGQIFMGLMVNPPKPGDISYD
QFVRESKGILESLRRRARMMTDGFNSCKNVVCNFTEGAMYSFPQIKLPPKAIEAARM
>gnl|CDD|215209 PLN02369, PLN02369, ribose-phosphate pyrophosphokinase
PALSQEIACYLGLELGKITIKRFADGEIYVQLQESVRGCDVFLVQPTCPPANENLMELLIMIDACRRASA
KRITAVIPYFGYARADRKTQGRESIAAKLVANLITEAGADRVLACDLHSGQSMGYFDIPVDHVYGQPVIL
DYLASKTISSPDLVVVSPDVGGVARARAFAKKLSDAPLAIVDKRRQGHNVAEVMNLIGDVKGKVAIMVDD
MIDTAGTITKGAALLHQEGAREVYACATHAVFSPPAIERLSSGLFQEVIVTNTIPVSEKNYFPQLTVLSV
ANLLGETIWRVHDDCSVSSIFD
>gnl|CDD|215210 PLN02370, PLN02370, acyl-ACP thioesterase
MVATAATSSFFPVPSPSGDAKAKKFGSGSASLGGIKSKSASSGALQVKANAQAPPKINGSPVGLTGSVEI
VKTDEDVVSSPAPRTFINQLPDWSMLLAAITTIFLAAEKQWMMLDWKPRRSDMLIDPFGIGRIVQDGLVF
RQNFSIRSYEIGADRTASIETLMNHLQETALNHVKTAGLLGDGFGSTPEMSKRNLIWVVTRMQVLVDRYP
TWGDVVQVDTWVSASGKNGMRRDWLVRDCKTGETLTRASSVWVMMNKLTRRLSKIPEEVRGEIEPYFLNS
DPVVNEDSRKLPKLDDKTADYIRKGLTPRWSDLDVNQHVNNVKYIGWILESAPPPIMESHELAAITLEYR
RECGRDSVLQSLTAVSGTGIGNLGTAGDVECQHLLRLEDGAEIVRGRTEWRPKHATNFGIMGQIPAESA
>gnl|CDD|215211 PLN02371, PLN02371, phosphoglucosamine mutase family protein
SSLAPTVPSDLLPATSGKLSTSLSQSVTAPAPSSPSLKLTRARTGTAAAASSSTESPVVDKDDIRKLQNG
SDIRGVAVEGVEGEPVTLTPPAVEAIGAAFAEWLLEKKKADGSGELRVSVGRDPRISGPRLADAVFAGLA
SAGLDVVDMGLATTPAMFMSTLTEREDYDAPIMITASHLPYNRNGLKFFTKDGGLGKPDIKDILERAARI
YKEWSDEGLLKSSSGASSVVCRVDFMSTYAKHLRDAIKEGVGHPTNYETPLEGFKIVVDAGNGAGGFFAE
KVLEPLGADTSGSLFLEPDGMFPNHIPNPEDKAAMSATTQAVLANKADLGIIFDTDVDRSAVVDSSGREI
NRNRLIALMSAIVLEEHPGTTIVTDSVTSDGLTTFIEKKGGKHHRFKRGYKNVIDKGVRLNSDGEETHLM
IETSGHGALKENHFLDDGAYLAVKIIIELVRMRAAGAGGGLGDLIEDLEEPLEAVELRLKILDEGKDFKA
YGEEVLEHLRNSIESDGKLEGAPVNYEGVRVSDEGEGFGGWFLLRQSLHDPVIPLNIESSSPGGAQKMAL
VVLTWLKEFAALDASALDKFLDI
>gnl|CDD|215212 PLN02372, PLN02372, violaxanthin de-epoxidase
SMTRAAAARISFFSSSSSTSRTHSSVSRSNHRAVLAPRRRSMSAISSRTSSRSSRASASLRKSDSEEEFD
FVGLSSLNELKEWSRLLLLKALGLLACALLSVPSADAADALKTCACLLKECRLELAKCIANPKCAANVAC
LQTCNGRPDETECQIKCGDLFENKVVDEFNECAVTRKKCVPQKSDDGEFPVPDPSALVQNFDTADFNGRW
YITSGLNKTFDTFDCQLHEFTAEDPDKLVGNLNWRINTPDGGFFTRSAVQRFVQDPNQPGILYNHDNEYL
HYQDDWYILSSKIENKPDDYVFVYYRGRNDAWDGYGGAVVYTRSSTLPESIVPELEKAAKKVGRDFSDFV
RTDNTCGPEPPLLERLEKDVEEGEKTIVKEARQIEEELEKEVEKLGKEEESLFKRVALEEGLKELEQDEE
NFLKELSKEEKELLEKLKMEASEVEKLFGRALPVR
>gnl|CDD|178001 PLN02373, PLN02373, soluble inorganic pyrophosphatase
SMSRRSVAAHPWHDLEIGPGAPAIFNCVVEITKGSKVKYELDKKTGLIKVDRVLYSSVVYPHNYGFIPRT
LCEDNDPLDVLVLMQEPVLPGCFLRARAIGLMPMIDQGEKDDKIIAVCADDPEYRHYTDIKELPPHRLAE
IRRFFEDYKKNENKEVAVNDFLPAEAAIEAIQYSMDLYAEYIVESLRR
>gnl|CDD|215213 PLN02374, PLN02374, pyruvate dehydrogenase (acetyl-transferring)
MAAAFAATSLLVPVPARSSRDDAPSSPLRGALKRSSAFTGSTSKLSSLRGLNAANGRRRSTVVAVSAVVK
EKNSKASASDLLVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLKKDDS
VVSTYRDHVHALSKGVPARAVMSELFGKATGCCRGQGGSMHMFSKEHNLLGGFAFIGEGIPVATGAAFSS
KYRREVLKEESCDDVTLAFFGDGTCNNGQFFECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWK
KGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVECETYRFRGHSLADPDELRDPAEKAHYAAR
DPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPLPPRSQLLENVFADPKGFGIGPDGRYR
CEDPKFTAGTAQV
>gnl|CDD|178003 PLN02375, PLN02375, molybderin biosynthesis protein CNX3
MISTLRRAVFLRRFPAVVSPIKRAFSSRIDDEFDPQIMNINELNQEMQSIFGQEPSPDGPGTMDFSELKS
SKIEPLRSKNIDFRQQIEYHKSTHSSKNDSQAIEQYAKVASDMSKLTHVGIAGEAQMVDVSSKDNSKRTA
LACCKVILGKRVFDLVLANQMGKGDVLGVAKIAGINGAKQTSSLIPLCHNIALTHVRVDLRLNPEDFSVD
IEGEASCTGKTGVEMEAMTAVSVAGLTVYDMCKAASKDISITDVRLERKTGGKSGSWSRL
>gnl|CDD|178004 PLN02376, PLN02376, 1-aminocyclopropane-1-carboxylate synthase
MGLPAKNKGAILSKIATNDQHGENSEYFDGWKAYDKDPFHLSRNPHGIIQMGLAENQLCLDLIKDWVKEN
PEASICTLEGIHQFSDIANFQDYHGLKKFRQAIAHFMGKARGGKVTFDPERVVMSGGATGANETIMFCLA
DPGDVFLIPSPYYAAFDRDLRWRTGVEIIPVPCSSSDNFKLTVDAADWAYKKAQESNKKVKGLILTNPSN
PLGTMLDKDTLTNLVRFVTRKNIHLVVDEIYAATVFAGGDFVSVAEVVNDVDISEVNVDLIHIVYSLSKD
MGLPGFRVGIVYSFNDSVVSCARKMSSFGLVSSQTQLMLASMLSDDQFVDNFLMESSRRLGIRHKVFTTG
IKKADIACLTSNAGLFAWMDLRHLLRDRNSFESEIELWHIIIDKVKLNVSPGSSFRCTEPGWFRICFANM
DDDTLHVALGRIQDFVSKNKNKIVEKASENDQVIQNKNAKKLKWRQSNLRLSFRRLYEDGLSSPGIMSPH
SPLLRA
>gnl|CDD|166018 PLN02377, PLN02377, 3-ketoacyl-CoA synthase
MDSGGEIRIHQTRMLPDFLQSVNLKYVKLGYHYLISNLLTLCFIPLIIIISIEASQMNPDDLRQLWIHLQ
YNLVSIIICSAFLVFGLTVYIMTRPRPVYLVDYSCYRAPDHLKAPFARFMEHSRLTGDFDDSSLEFQRKI
LERSGLGEDTYVPEAMHYIPPRPSMAAAREEAEQVMFGALDNLFANTNVNPKDIGILVVNCSLFNPTPSL
SAMIVNKYKLRGNIRSFNLGGMGCSAGVIAVDLAKDMLQVHRNTYAVVVSTENITQNWYFGNKKSMLIPN
CLFRVGGSAVLLSNKSRDKRRSKYKLVHVVRTHRGADDKAFRCVYQEQDDAGKTGVSLSKDLMAIAGEAL
KTNITTLGPLVLPISEQLLFFATLVVKKLFNKKMKPYIPDFKLAFDHFCIHAGGRAVIDELEKNLQLLPV
HVEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRKGNRVWQIAFGSGFKCNSAVWEALRHVKPSNNSPWE
DCIDKYPVKLVY
>gnl|CDD|166019 PLN02378, PLN02378, glutathione S-transferase DHAR1
MALEICVKAAVGAPDHLGDCPFSQRALLTLEEKSLTYKIHLINLSDKPQWFLDISPQGKVPVLKIDDKWV
TDSDVIVGILEEKYPDPPLKTPAEFASVGSNIFGTFGTFLKSKDSNDGSEHALLVELEALENHLKSHDGP
FIAGERVSAVDLSLAPKLYHLQVALGHFKSWSVPESFPHVHNYMKTLFSLDSFEKTKTEEKYVISGWAPK
VNP
>gnl|CDD|178005 PLN02379, PLN02379, pfkB-type carbohydrate kinase family protein
VAPAPCMGAAGALGDGPRPPLVLGLQPVALVDHVARVDWSLLDQIPGDRGGSIRVTIEELEHILREVNAH
ILPSPDDLSPIKTMAGGSVANTIRGLSAGFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGPT
AQCVCLVDALGNRTMRPCLSSAVKLQADELTKEDFKGSKWLVLRYGFYNLEVIEAAIRLAKQEGLSVSLD
LASFEMVRNFRSPLLQLLESGKIDLCFANEDEARELLRGEQESDPEAALEFLAKYCNWAVVTLGSKGCIA
RHGKEVVRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALGGEVTPENWQW
MYKQMQLKGLPVPDLRN
>gnl|CDD|178006 PLN02380, PLN02380, 1-acyl-sn-glycerol-3-phosphate acyltransferase
MAIPAALVILPLGLLFLLSGLIVNLIQAVCFILVRPLSKSLYRRINRAVAELLWLELIWLVDWWAGVKVQ
LYADEETFELMGKEHALVISNHRSDIDWLVGWILAQRSGCLGSALAVMKKSSKFLPVIGWSMWFSEYVFL
ERSWAKDENTLKSGFQRLKDFPRPFWLALFVEGTRFTQAKLLAAQEYAASRGLPVPRNVLIPRTKGFVSA
VSNMRSFVPAIYDVTVAVPKGQPAPTMLRIFRGQSSVVHVHIKRHSMKELPETDDGIAQWCKDVFVAKDA
LLDKHFAEDTFGDQEYQDIGRPKKSLIVVISWACLLILGAIKFLQWLSLLSSWKGIASLAAGLVIVTILM
QILIESSQSERSTPAKAANAKVKKEA
>gnl|CDD|215214 PLN02381, PLN02381, valyl-tRNA synthetase
GSRTESEAEKKILTEEELERKKKKEEKAKEKELKKLKAAQKEAKAKLQAQQASDGTNVPKKSEKKSRKRD
VEDENPEDFIDPDTPFGQKKRLSSQMAKQYSPSAVEKSWYAWWEKSGYFGADAKSSKPPFVIVLPPPNVT
GALHIGHALTAAIEDTIIRWKRMSGYNALWVPGVDHAGIATQVVVEKKLMRERHLTRHDIGREEFVSEVW
KWKDEYGGTILNQLRRLGASLDWSRECFTMDEQRSKAVTEAFVRLYKEGLIYRDIRLVNWDCTLRTAISD
VEVDYIDIKERTLLKVPGYDKPVEFGVLTSFAYPLEGGLGEIVVATTRIETMLGDTAIAIHPDDERYKHL
HGKFAVHPFNGRKLPIICDAILVDPNFGTGAVKITPAHDPNDFEVGKRHNLEFINIFTDDGKINSNGGSE
FAGMPRFAAREAVIEALQKKGLYRGAKNNEMRLGLCSRTNDVVEPMIKPQWFVNCSSMAKQALDAAIDGE
NKKLEFIPKQYLAEWKRWLENIRDWCISRQLWWGHRIPAWYVTLEDDQLKELGSYNDHWVVARNESDALL
EASQKFPGKKFELSQDPDVLDTWFSSGLFPLSVLGWPDDTDDLKAFYPTSVLETGHDILFFWVARMVMMG
MQLGGDVPFRKVYLHPMIRDAHGRKMSKSLGNVIDPLEVINGISLEGLHKRLEEGNLDPKELVVAKEGQK
KDFPNGIAECGTDALRFALVSYTAQSDKINLDILRVVGYRQWCNKLWNAVRFAMSKLGDDYTPPATLSVE
TMPFSCKWILSVLNKAISKTVSSLDAYEFSDAASTVYSWWQYQFCDVFIEAIKPYFAGDNPEFASERAAA
QDTLWICLDTGLRLLHPFMPFVTEELWQRLPQPKDHTRKDSIMISEYPSAVEAWTNEKVEYEMDLVLSTV
KCLRSLRAEVLEKQKNERLPAFALCRNQEIAAIIKSHQLEILTLANLSSLKVLLSENDAPPAGCAFENVN
ENLKVYLQAQGAVNAEAELEKLRNKMDEIQKQQEKLEKKMNASGYKEKVPANIQEEDARKLTKLLQELEF
FEKESKRLEAETSNSG
>gnl|CDD|178008 PLN02382, PLN02382, probable sucrose-phosphatase
MDRLSGSPRLMIVSDLDHTMVDHHDPENLSLLRFNALWEAEYRHDSLLVFSTGRSPTLYKELRKEKPLLT
PDITIMSVGTEIAYGESMVPDHGWVEYLNKKWDREIVVEETSKFPELKLQPETEQRPHKVSFYVDKKKAQ
EVIKELSERLEKRGLDVKIIYSGGIDLDVLPQGAGKGQALAYLLKKLKAEGKAPVNTLVCGDSGNDAELF
SVPDVYGVMVSNAQEELLQWYAENAKDNPKIIHATERCAAGIIQAIGHFNLGPNVSPRDVSDFLYGKLDN
VNPAHEVVKFYLFYEKWRRGEVENSDEVFQRLKSSCAPNGVFVHPSGVEKSLHDSIDELRSCYGDKKGKK
FRVWVDRVLSTQLGPDTWLVKFDKWEQSGDERKCCLTTALLTSKEDTPNGLEWMHVHQTWLEG
>gnl|CDD|178009 PLN02383, PLN02383, aspartate semialdehyde dehydrogenase
MALTENGPSVAIVGVTGAVGQEFLSVLTDRDFPYSSLKMLASARSAGKKVTFEGRDYTVEELTEDSFDGV
DIALFSAGGSISKKFGPIAVDKGAVVVDNSSAFRMEEGVPLVIPEVNPEAMKHIKLGKGKGALIANPNCS
TIICLMAVTPLHRHAKVKRMVVSTYQAASGAGAAAMEELEQQTREVLEGKPPTCNIFAQQYAFNLFSHNA
PMQENGYNEEEMKLVKETRKIWNDDDVKVTATCIRVPVMRAHAESINLQFEKPLDEATAREILASAPGVK
IIDDRANNRFPTPLDASNKDDVAVGRIRQDISQDGNKGLDIFVCGDQIRKGAALNAVQIAELLL
>gnl|CDD|215215 PLN02384, PLN02384, ribose-5-phosphate isomerase
MAIAYPPFIGSEKDSMEVGSMLSPSSPVILTQDELKKIAAYKAVEFVESGMVLGLGTGSTAKHAVDRIGE
LLRQGKLKNIIGIPTSKKTHEQAVSLGIPLSDLDSHPVVDLAIDGADEVDPNLNLVKGRGGSLLREKMIE
GACKKFVVIVDESKLVKHIGGSGLAMPVEVVPFCWKFTAEKLQSLFEYAGCVAKLRTKNNGEEPFVTDNG
NYIVDLYFKRDIGDLKVASDAILRLAGVVEHGMFLDMATTVIVAGELGVTIKDK
>gnl|CDD|215216 PLN02385, PLN02385, hydrolase; alpha/beta fold family protein
ASAIVAKAPSAIEGVSEELNRILDANLDEAPARRRARDAFKDIQLQLDHCLFKTPPSGIKTEESYEVNSR
GVEIFSKSWLPENSRPKAAVCFCHGYGDTCTFFFEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFD
DLVDDVIEHYSKIKGNPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPPLVL
QILILLANLLPKAKLVPQKDLAELAFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSL
PLLILHGEADKVTDPSVSKFLYEKASSSDKKLKLYEDAYHSILEGEPDEMIFQVLDDIISWLDSHSTQK
>gnl|CDD|166027 PLN02386, PLN02386, superoxide dismutase [Cu-Zn]
MVKAVAVLNSSEGVKGTIFFTQEGDGPTTVTGSLSGLKPGLHGFHVHALGDTTNGCMSTGPHFNPAGKEH
GAPEDENRHAGDLGNVTVGDDGTATFTIVDKQIPLTGPNSIVGRAVVVHADPDDLGKGGHELSKSTGNAG
GRVACGIIGLQG
>gnl|CDD|215217 PLN02387, PLN02387, long-chain-fatty-acid-CoA ligase family protein
MGAYIVGVLVPLLLTLLLRGSKKGKKRGVPVDVGGEPGYAIRNARFPELVETPWEGATTLAALFEQSCKK
YSDKRLLGTRKLISREFETSSDGRKFEKLHLGEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADT
RAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLIDISSQLETVKRVIYMDD
EGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVA
GVMTVVPKLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGYGSPLTLTDTSNKIKKGTKGDASALKPTL
MTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIEGSWFGAWGLEKLLWDALVFKKIRAVLGG
RIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEE
GGYLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDERGMRWFYTGDIGQFHPDGCLEIIDRKKDI
VKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDYSNFAELCEKE
EAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE
>gnl|CDD|215218 PLN02388, PLN02388, phosphopantetheine adenylyltransferase
MVTVKDSVADSKLSPPNSYGAVVLGGTFDRLHDGHRLFLKAAAELARDRIVIGVCDGPMLSKKQFAELIQ
PIEERMHNVEEYIKSIKPELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKI
EVVDIVPEESTGNKLSSTTLRRLEAEKAVKQKQPAEE
>gnl|CDD|215219 PLN02389, PLN02389, biotin synthase
MALLRSVFRSQLRPPPSSSLSSESSSSSSAAAIAAERAIREGPRNDWTRDEIKEVYDSPLLDLLFHGAQV
HRHAHDPREVQQCTLLSIKTGGCSEDCSYCPQSSRYDTGVKAQKLMSKDDVLEAAKRAKEAGSTRFCMGA
AWRDTVGRKTNFNQILEYVKEIRGMGMEVCCTLGMLEKEQAAQLKEAGLTAYNHNLDTSREYYPNVITTR
SYDDRLETLEAVREAGISVCSGGIIGLGEAEEDRVGLLHTLATLPEHPESVPINALVAVKGTPLEDQKPV
EIWEMVRMIATARIVMPKAMVRLSAGRVRFSMAEQALCFLAGANSIFTGDKLLTTPNNDFDADQAMFKEL
GLIPKPPSFGEDEERASEAERCEEAVSSS
>gnl|CDD|178014 PLN02390, PLN02390, molybdopterin synthase catalytic subunit
DPQAGAIATFSGTTRDTFEGKTVLELRYEAYVPMALRELRKICDEARSRWSLHKIAVAHRLGPVPVGETS
VFVAVSSVHRADALDACKFLIDELKASVPIWKKEVYDDGEV
>gnl|CDD|178015 PLN02392, PLN02392, probable steroid reductase DET2
MALSDQSLFHYSLLALYLIGPPTFISLKFLQAPYGKHNRLGWGPTVSPPLAWFLMESPTLWLTLLLFPLG
QHFTNPKALLLMSPYLLHYFHRTCIYPLRLYRSTSQQNTKGFPVSMALLAFGFNLLNAYLQARWVSHYKD
DYEDGGWFWWRFFGGLVVFLWGMRINVWSDRVLVGLKREGGGYKVPRGGWFELVSCPNYFGEIVEWLGWA
VMTWSWAGFGFFLYTCSNLVPRACANHKWYLEKFGEDYPKGRKAVIPFLY
>gnl|CDD|215220 PLN02393, PLN02393, leucoanthocyanidin dioxygenase like protein
MMNCLQDWPEPIVRVQSLSESGLPTIPDRYVKPPSQRPNSSNTTSAPAEINIPVIDLSSLFSDDARLRDA
TLRAISEACREWGFFQVVNHGVRPELMDRAREAWREFFHLPLEVKQRYANSPATYEGYGSRLGVEKGAIL
DWSDYYFLHYLPSSLKDPNKWPSLPPSCRELIEEYGEEVVKLCGRLMKVLSVNLGLEEDRLQNAFGGEDG
VGACLRVNYYPKCPQPDLTLGLSPHSDPGGMTILLPDDNVAGLQVRRDDAWITVKPVPDAFIVNIGDQIQ
VLSNAIYKSVEHRVIVNSAKERVSLAFFYNPKSDLPIEPLKELVTPDRPALYPPMTFDEYRLFIRTKGPR
GKSQVESLKSPR
>gnl|CDD|215221 PLN02394, PLN02394, trans-cinnamate 4-monooxygenase
LLLLEKTLLGLFVAIVLALLVSKLRGKKLKLPPGPAAVPIFGNWLQVGDDLNHRNLAEMAKKYGDVFLLR
MGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGDHWRKMRRIMTVPFFTNKV
VQQYRYGWEEEADLVVEDVRANPEAATEGVVIRRRLQLMMYNIMYRMMFDRRFESEDDPLFLKLKALNGE
RSRLAQSFEYNYGDFIPILRPFLRGYLKICQDVKERRLALFKDYFVDERKKLMSAKGMDKEGLKCAIDHI
LEAQKKGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTH
KLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFL
EEEAKVEANGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLPPPGQSKIDVSEKGGQFSLHI
AKHSTVVFKPRSA
>gnl|CDD|166036 PLN02395, PLN02395, glutathione S-transferase
MVLKVYGPAFASPKRALVTLIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGDYKIFESRAIM
RYYAEKYRSQGPDLLGKTIEERGQVEQWLDVEATSYHPPLLNLTLHILFASKMGFPADEKVIKESEEKLA
KVLDVYEARLSKSKYLAGDFVSLADLAHLPFTEYLVGPIGKAYLIKDRKHVSAWWDDISSRPAWKEVLAK
YSLPV
>gnl|CDD|178018 PLN02396, PLN02396, hexaprenyldihydroxybenzoate methyltransferase
MLASLLSNQLQRLLLSARRLSSSRIIPPSRLLHQRLFSTSDTDDSAASFSSSHPKMQTLEGKASNKSRST
STTTSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKDPSSAKPFEGLKFIDIGC
GGGLLSEPLARMGATVTGVDAVDKNVKIARLHADMDPVTSTIEYLCTTAEKLADEGRKFDAVLSLEVIEH
VANPAEFCKSLSALTIPNGATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRA
SVDVKEMAGFVYNPITGRWLLSDDISVNYIAYGTKRKDLGDI
>gnl|CDD|215222 PLN02397, PLN02397, aspartate transaminase
SNPFLKAKSRSRSSMAAAAASSRFEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNV
VRKAEQRLLAGSRNKEYLPIEGLAEFNKLSAKLAYGADSPAIKENRVATVQCLSGTGSLRLGAEFLARFY
PGSTIYIPNPTWGNHHNIFRDAGVPVRTYRYYDPKTRGLDFDGLLEDLKAAPDGSFVLLHACAHNPTGVD
PTPEQWEQISDLIKSKNHLPFFDSAYQGFASGDLDADAQSVRMFVEDGHEILVAQSYAKNMGLYGERVGA
LSVVCKSADVAVRVKSQLKLIARPMYSNPPIHGASIVATILGDPELFSEWTKELKGMADRIISMRQKLYD
ALEARGSPGDWSHITKQIGMFSFTGLNKEQVDRMTKEYHIYMTRDGRISMAGLSSKNVPYLADAIHAVVT
NAS
>gnl|CDD|215223 PLN02398, PLN02398, hydroxyacylglutathione hydrolase
MQMISKASSAMSSFRCSRRIRGQLCVRPGVRQLCLRKSLLYGVMKLLSMPLKTLRGAGRTLKVAQFCSVS
NVSSSLQIELVPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLE
LKARYGAKVIGSAVDKDRIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFS
LSCGKLFEGTPEQMLSSLQKIISLPDDTNIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLP
TIPTTVKMEKACNPFLRTSSTDIRKSLSIPDTADEAEALGIIRRAKDNF
>gnl|CDD|178021 PLN02399, PLN02399, phospholipid hydroperoxide glutathione peroxidase
MVSLTTSSSSYASFKTVFNSSPPPPSMAFLVPSLKSSTGISKSAFLSNGFSLKSPNSPGFLSKSRSFGVY
ARAATEKSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPC
NQFGGQEPGSNPEIKQFACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKN
GKVVERYPPTTSPFQIEKDIQKLLAA
>gnl|CDD|215224 PLN02400, PLN02400, cellulose synthase
MEANAGMVAGSYRRNELVRIRHDSDSGPKPLKNLNGQICQICGDDVGVTETGDVFVACNECAFPVCRPCY
EYERKDGTQCCPQCKTRYRRHKGSPRVEGDEDEDDVDDLENEFNYAQGNGKARHQWQGEDIELSSSSRHE
SQPIPLLTHGQPVSGEIPCATPDNQSVRTTSGPLGPAERNANSSPYIDPRQPVPVRIVDPSKDLNSYGLG
NVDWKERVEGWKLKQDKNMMQMTNKYHEGKGGDMEGTGSNGDELQMADDARLPMSRVVPIPSSRLTPYRI
VIILRLIILGFFLQYRVTHPVKDAYGLWLTSVICEIWFALSWLLDQFPKWYPINRETYLDRLALRYDRDG
EPSQLAPVDVFVSTVDPLKEPPLVTANTVLSILAVDYPVDKVSCYVSDDGSAMLTFEALSETAEFARKWV
PFCKKHNIEPRAPEFYFAQKIDYLKDKIQPSFVKERRAMKREYEEFKVRINALVAKAQKIPEEGWTMQDG
TPWPGNNPRDHPGMIQVFLGHSGGLDTDGNELPRLVYVSREKRPGFQHHKKAGAMNALIRVSAVLTNGAY
LLNVDCDHYFNNSKALKEAMCFMMDPAIGKKTCYVQFPQRFDGIDLHDRYANRNIVFFDINLKGLDGIQG
PVYVGTGCCFNRQALYGYDPVLTEEDLEPNIIVKSCCGSRKKGKGSKKYNIDKKRAMKRTESNVPIFNME
DIEEGVEGYDDERSLLMSQKSLEKRFGQSPVFIAATFMEQGGIPPSTNPATLLKEAIHVISCGYEDKTEW
GKEIGWIYGSVTEDILTGFKMHARGWISIYCMPPRPAFKGSAPINLSDRLNQVLRWALGSIEILLSRHCP
IWYGYNGRLKLLERLAYINTIVYPITSIPLLAYCVLPAFCLITNKFIIPEISNYASMWFILLFISIFATG
ILELRWSGVGIEDWWRNEQFWVIGGTSAHLFAVFQGLLKVLAGIDTNFTVTSKASDEDGDFAELYVFKWT
SLLIPPTTVLLVNLVGIVAGVSYAINSGYQSWGPLFGKLFFAIWVIAHLYPFLKGLLGRQNRTPTIVIVW
SILLASIFSLLWVRIDPFVSDTTKAAANGQCGVNC
>gnl|CDD|215225 PLN02401, PLN02401, diacylglycerol o-acyltransferase
SPGGSSNGGGRDGGEGRANADAKFTYRPSAPAHRRVKESPLSSDAIFKQSHAGLFNLCIVVLIAVNSRLI
IENLMKYGWLIRTGFWFSSRSLRDWPLFMCCLSLPVFPLAAFLVEKLAYRKYISEPVVIFLHIIITTAEV
LYPVLVILRCDSAVLSGVTLMLLACIVWLKLVSYAHTNYDMRALAKSIDKGEAPSTSANPEVSYDVTFKS
LAYFMVAPTLCYQPSYPRSACIRKGWVVRQFVKLVIFTGFMGFIIEQYINPIVQNSQHPLKGNLLYAIER
VLKLSVPNLYVWLCMFYCFFHLWLNILAELLRFGDREFYKDWWNAKTVEEYWRMWNMPVHKWMVRHIYFP
CLRNGISKGVAILIAFFVSAVFHELCIAVPCHMFKLWAFLGIMFQVPLVFITNYLQNKFKSSMVGNMIFW
FFFCILGQPMCVLLYYHDLMNRKGST
>gnl|CDD|178024 PLN02402, PLN02402, cytidine deaminase
MDGPIFVIEASEAESMAKQSGLTVLQLLPSLVKSAQSLARPPISKYHVGAVGLGSSGRIFLGVNLEFPGL
PLHHSVHAEQFLITNLTLNAEPHLKYVAVSAAPCGHCRQFFQEIRDAPDIKILITGDSNSNDSYKNSLAD
SQQFEPLSCLLPHRFGPDDLLDKDVPLLLEPHHNHLSFVGDDKLPNGISASSDDLKNEALEAANKSHAPY
SNCPSGVALMDCEGKVYRGSYMESAAYNPSMGPVQAALVAYVAGGRGGGYERIVAAVLVEKEGAVVRQEQ
TARLLLKEISPKCEFKVFHCSSA
>gnl|CDD|178025 PLN02403, PLN02403, aminocyclopropanecarboxylate oxidase
MEIPVIDFDQLDGEKRSKTMSLLHQACEKWGFFQVENHGIDKKLMEKVKQLVNSHYEENLKESFYESEIA
KALDNEGKTSDVDWESSFFIWHRPTSNINEIPNLSEDLRKTMDEYIAQLIKLAEKLSELMSENLGLDKDY
IKEAFSGNKGPSVGTKVAKYPECPRPELVRGLREHTDAGGIILLLQDDQVPGLEFLKDGKWVPIPPSKNN
TIFVNTGDQLEVLSNGRYKSTLHRVMADKNGSRLSIATFYNPAGDAIISPAPKLLYPSNYRFQDYLKLYS
TTKFGDKGPRFESMKKMANGHSS
>gnl|CDD|178026 PLN02404, PLN02404, 6,7-dimethyl-8-ribityllumazine synthase
SLLDGEGLRFGVVVARFNEIITKNLLEGALETFKRYSVKEENIDVVWVPGSFEIPVVAQRLAKSGKYDAI
LCIGAVIRGDTTHYDAVANSAASGVLSAGLNSGVPCIFGVLTCDDMEQALNRAGGKAGNKGAEAALTAVE
M
>gnl|CDD|215226 PLN02405, PLN02405, hexokinase
MGKVAVGAAVVCAAAVCAAAALVVRRRMKSSGKWARAMEILKEFEEDCATPIGKLRQVADAMTVEMHAGL
ASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSS
DALFDFIAAALAKFVATEGEDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGE
LTKAMERVGLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMV
INMEWGNFRSSHLPLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLK
IPFILRTPDMSAMHHDTSPDLKVVGSKLKDILEIPNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKK
LGRDTVKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLKELLGEEVSESIEVEHSNDGSGIGAALLAASHS
LYLEVEE
>gnl|CDD|215227 PLN02406, PLN02406, ethanolamine-phosphate cytidylyltransferase
MSISSAKYVASCLIGGLMLGASVLGLSLAGFGSSLPYAWPDLGIFKKKKKKKPVRVYMDGCFDMMHYGHA
NALRQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAITEEFMNKLFNEY
NIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERSISDSHNHSSLQRQF
SHGHSQFEDGGSGSGTRVSHFLPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGDF
LLVGIHTDQTVSAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTVAENN
DFLKGEDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESEKRYYESKSFVSGD
>gnl|CDD|178029 PLN02407, PLN02407, diphosphomevalonate decarboxylase
VVMVTAQAPTNIAVIKYWGKRDEKLILPINSSISVTLDPDHLCATTTVAVSPSFDQDRLWLNGKEISLSG
GRYQNCLREIRARATDVEDEEKGIKITKKDWEKLHVHIASYNNFPTAAGLASSAAGFACLVFALAKLMNV
KEDFPGELSAIARQGSGSACRSLYGGFVKWNMGKKEDGSDSIAVQLADEKHWDDLVIIIAVVSSRQKETS
STSGMRESVETSPLLQHRAKEVVPKRILQMEEAIKNRDFASFAKLTCADSNQFHATCLDTSPPIFYMNDT
SRRIISLVEKWNRSEGTPQVAYTFDAGPNAVLIALNRKVAAQLLQRLLYYFPPSSDTDLSSYV
>gnl|CDD|215228 PLN02408, PLN02408, phospholipase A1
MEYQGIRNWDGLLDPLDDNLRGEILRYGDFVEAAYKSFDFDPSSPTYATCRFPKSTLLERSGLPNTGYRL
TKHLRATSGIQLPRWIEKAPSWVATQSSWIGYVAVCQDKEEIARLGRRDVVIAFRGTATCLEWLENLRAT
LTRLPNAPTDMNGSGDGSGPMVESGFLSLYTSGTAMGPSLQEMVREEIARLLQSYGDEPLSLTITGHSLG
AALATLTAYDIKTTFKRAPMVTVISFGGPRVGNRSFRRQLEKQGTKVLRIVNSDDVITKVPGFVIDGEND
VAKKRDVNVAGLPSWIQKRVEDTQWVYAEVGRELRLSSKDSPYLNSINVATCHDLKTYLHLVNGFVSSTC
PFRATAKRVLGRHHR
>gnl|CDD|178031 PLN02409, PLN02409, serine--glyoxylate aminotransaminase
MDYVYAPGRNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGT
GAWESALTNTLSPGDKVVSFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQDTNHKIKA
VCVVHNETSTGVTNDLAGVRKLLDCAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLG
IVCASPKALEASKTAKSPRVFFDWADYLKFYKLGTYWPYTPSIQLLYGLRAALDLIFEEGLENVIARHAR
LGEATRLAVEAWGLKLCTKKPEWRSDTVTAVVVPEGIDSAEIVKNAWKKYNLSLGLGLNKVAGKVFRIGH
LGNVNELQLLGALAGVEMVLKDVGYPVKLGSGVAAAQAYLQKTTPLIPSRI
>gnl|CDD|178032 PLN02410, PLN02410, UDP-glucoronosyl/UDP-glucosyl transferase family protein
MEEKPARRRVVLVPVPAQGHISPMMQLAKTLHLKGFSITIAQTKFNYFSPSDDFTDFQFVTIPESLPESD
FKNLGPIEFLHKLNKECQVSFKDCLGQLVLQQGNEIACVVYDEFMYFAEAAAKEFKLPNVIFSTTSATAF
VCRSVFDKLYANNVLAPLKEPKGQQNELVPEFHPLRCKDFPVSHWASLESIMELYRNTVDKRTASSVIIN
TASCLESSSLSRLQQQLQIPVYPIGPLHLVASAPTSLLEENKSCIEWLNKQKKNSVIFVSLGSLALMEIN
EVMETASGLDSSNQQFLWVIRPGSVRGSEWIESLPKEFSKIISGRGYIVKWAPQKEVLSHPAVGGFWSHC
GWNSTLESIGEGVPMICKPFSSDQKVNARYLECVWKIGIQVEGDLDRGAVERAVKRLMVEEEGEEMRKRA
ISLKEQLRASVISGGSSHNSLEEFVHFMRTL
>gnl|CDD|178033 PLN02411, PLN02411, 12-oxophytodienoate reductase
MTAAQGNSNETLFSPYKMGRFDLSHRVVLAPMTRCRALNGIPNAALAEYYAQRSTPGGFLISEGTLISPT
APGFPHVPGIYSDEQVEAWKKVVDAVHAKGSIIFCQLWHVGRASHQVYQPGGAAPISSTNKPISERWRIL
MPDGSYGKYPKPRALETSEIPEVVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGS
IENRCRFLMQVVQAVVSAIGADRVGVRVSPAIDHLDATDSDPLNLGLAVVERLNKLQLQNGSKLAYLHVT
QPRYTAYGQTESGRHGSEEEEAQLMRTLRRAYQGTFMCSGGFTRELGMQAVQQGDADLVSYGRLFISNPD
LVLRFKLNAPLNKYIRKTFYTQDPVVGYTDYPFLSQPFSRL
>gnl|CDD|166053 PLN02412, PLN02412, probable glutathione peroxidase
MAEESPKSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPC
NQFLGQEPGSNEEIQQTVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKE
GKVVQRYAPTTSPLKIEKDIQNLLGQA
>gnl|CDD|215229 PLN02413, PLN02413, choline-phosphate cytidylyltransferase
ARKNAGASTAAASSGSATPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTH
KYKGKTVMTEDERYESLRHCKWVDEVIPDAPWVITQEFLDKHRIDYVAHDALPYADASGAGKDVYEFVKK
IGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNLARGYSRKDLGVSYVKEKRLRVNMGLKKLREKVKEQQ
EKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLEKFEEGCHKMGTAIKDRIQERLMRQQSSGLLELLQNG
DVDSDDDDDEYYDE
>gnl|CDD|178035 PLN02414, PLN02414, glycine dehydrogenase (decarboxylating)
MERARRLANRGLLRRLVNEQTRSISVEALKPSDTFPRRHNSATPEEQKAMAEYCGFDSLDALIDATVPKS
IRLDSMKLSKYDEGLTESQMLEHMKSLASKNKVFKSYIGMGYYNTHVPPVILRNILENPGWYTQYTPYQA
EIAQGRLESLLNYQTMITDLTGLPMSNASLLDEGTAAAEAMAMCNNILKGKKKKFLIASNCHPQTIDVCQ
TRADGLGLEVVVADEKDFDYSSGDVCGVLVQYPATDGEVLDYAEFVKNAHANGVKVVMATDLLALTMLKP
PGEWGADIVVGSAQRFGVPMGYGGPHAAFLATSQEYKRLMPGRIIGVSVDSSGKPALRMAMQTREQHIRR
DKATSNICTAQALLANMAAMYAVYHGPEGLKTIAQRVHGLAGVFAAGLKKLGFQVQSLPFFDTVKVKCSD
ADAIADAAAKVGINLRVVDANTVTVSFDETTTLEDVDKLFKVFAGGKPVPFTAESLAPEVDSSIPSSLAR
ESPYLTHPIFNQYHSEHELLRYLHRLQNKDLSLVHSMIPLGSCTMKLNATTEMMPVTWPEFANIHPFAPV
DQAQGYQEMFEDLGDLLCEITGFDSFSLQPNAGAAGEYAGLMVIRAYHLSRGDHHRNVCIIPVSAHGTNP
ASAAMCGMKIVVVGTDAKGNINIEELRKAAEAHKDNLAALMVTYPSTHGVYEEGIDEICDIIHDNGGQVY
MDGANMNAQVGLTSPGFIGADVCHLNLHKTFCIPHGGGGPGMGPIGVKKHLAPFLPSHPVVPTGGIPRPE
KTQPLGTISAAPWGSALILPISYTYIAMMGSEGLTDASKIAILNANYMAKRLEGHYPVLFRGKNGTCAHE
FIIDLRPFKNTAGIEPEDVAKRLMDYGFHAPTMSWPVPGTLMIEPTESESKAELDRFCDALISIREEIAD
IENGKADRENNVLKGAPHPPSLLMADKWDKPYSREYAAFPAPWVRASKFWPTTGRVDNVYGDRNLVCTLP
SAAEEEEAAAATA
>gnl|CDD|178036 PLN02415, PLN02415, uricase
EADGFLLEQRHGKARVRVGRVWRADGGIHHFVEWNVSISLLSDCLPAYVRDDNSDIVATDTIKNTVYVKA
KECTQRLSVEEFAILLAKHFTSTYPQVTTAIVSIEQKPWERVSIDGKPHDHGFKLGSEKHTAEVTVSKSG
ALDVTSGITGLSLLKTTQSGFEGFIRDKYTALPETRERILATEVTASWRYSSVSSIPTKPLCYTEAYLDV
KKVLADTFFGPPKSGVYSPSVQYTLYQMAKAVLNRFPDISSIQLNMPNLHFLPVNLPTKENSIVKFNDDV
YLPTSEPHGSIEATVSRKTPTSKL
>gnl|CDD|178037 PLN02416, PLN02416, probable pectinesterase/pectinesterase inhibitor
MAFSSLNLLLFLLFFSPFFFSSAWYSNASYTTSLDPHLSSLTSFCKSTPYPDACFDSLKLSISINISPNI
LNFLLQTLQTAISEAGKLTNLLSGAGQSSNIIEKQRGTIQDCKELHQITVSSLKRSVSRIQAGDSRKLAD
ARAYLSAALTNKNTCLEGLDSASGPLKPKLVNSFTSTYKHVSNSLSMLPKSRRSTKGTKNRRLLGFPKWV
SKKDRRILQSDGYDEYDPSEVLVVAADGTGNFSTITDAINFAPNNSNDRIIIYVREGVYEENVEIPIYKT
NIVLIGDGSDVTFITGNRSVVDGWTTFRSATLAVSGEGFLARDITIENTAGPEKHQAVALRVNADLVALY
RCTINGYQDTLYVHSFRQFYRECDIYGTIDYIFGNAAVVFQACNIVSKMPMPGQFTVITAQSRDTPDEDT
GISIQNCSILATEDLYSNSNSVKSYLGRPWRVYSRTVVLESYIDDFIDPSGWSKWNGNEGLDTLYYGEYD
NNGPGSGTENRVTWQGYHVMDYEDAFNFTVSEFITGDEWLDSTSFPYDDGI
>gnl|CDD|178038 PLN02417, PLN02417, dihydrodipicolinate synthase
KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGK
IKVIGNTGSNSTREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMGPTIIYNVPGRTGQD
IPPEVIFKIAQHPNFAGVKECTGNDRVKQYTEKGILLWSGNDDECHDARWDYGADGVISVTSNLVPGLMH
KLMFAGKNKELNDKLLPLMDWLFCEPNPIGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIGRE
>gnl|CDD|215230 PLN02418, PLN02418, delta-1-pyrroline-5-carboxylate synthase
MMEEEDRSRAFLRDVKRVVIKVGTAVVTRDDGRLALGRLGALCEQIKELNSDGYEVILVSSGAVGVGRQR
LRYRRLVNSSFADLQKPQMELDGKACAAVGQSELMALYDTLFSQLDVTASQLLVTDSDFRDPDFRKQLSE
TVESLLDLRVIPIFNENDAVSTRRAPYEDSSGIFWDNDSLAALLALELKADLLILLSDVEGLYTGPPSDP
SSKLIHTYIKEKHQDEITFGEKSRVGRGGMTAKVKAAVNAASAGIPVVITSGYALDNIRKVLRGERVGTL
FHQDAHLWAPSKEVGAREMAVAARESSRKLQALSSEERKKILLDVADALEANEELIKAENELDVAAAQEA
GYEKSLVSRLTLKPGKIASLAASIRQLADMEDPIGRVLKRTEVADGLVLEKTSCPLGVLLIIFESRPDAL
VQIASLAIRSGNGLLLKGGKEAARSNAILHKVITDAIPKTVGGKLIGLVTSRDEIPDLLKLDDVIDLVIP
RGSNKLVSQIKASTKIPVLGHADGICHVYVDKSADMDMAKRIVVDAKTDYPAACNAMETLLVHKDLVQNG
GLNDLLVALRSAGVTLYGGPRASKLLNIPEAQSFHHEYSSLACTVEIVDDVHAAIDHIHRHGSAHTDCIV
TEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEGLLTTRWILRGNGQV
VDGDKGVVYTHKDLPLQS
>gnl|CDD|166060 PLN02419, PLN02419, methylmalonate-semialdehyde dehydrogenase [acylating]
MVRVKQKNLESYRSNGTYPPTWRNPTTSFAPDQHRVSIHSSLKSKTKRRRLYKEADDNTKLRSSSSTTTT
TTTMLLRISGNNLRPLRPQFLALRSSWLSTSPEQSTQPQMPPRVPNLIGGSFVESQSSSFIDVINPATQE
VVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG
DIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTF
ILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAK
GKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKALKVT
CGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKE
EIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTG
NKASFAGDLNFYGKAGVDFFTQIKLVTQKQKDIHSPFSLAIPIL
>gnl|CDD|178040 PLN02420, PLN02420, endoglucanase
MTVMDHRHKPCHFLLLLLLLITVFSAALAGVSSETDVGRFDYGEALSKSLLYFEAQRSGRLPYNQRVTWR
DHSGLTDGLEQGVDLVGGYHDAGDHVKFGLPMAFTVTMLSWSVIEYGDQLASTGELSHALEAIKWGTDYF
IKAHTSPNVLWAEVGDGDTDHYCWQRPEDMTTSRRAFKIDENNPGSDIAGETAAAMAAASIVFRSTNPHY
SHLLLHHAQQLFEFGDKYRGKYDESLKVVKSYYASVSGYMDELLWGATWLYRATDNEHYMSYVVDMAHQL
GGLSWAMSEFSWDVKYAGVQLLASMLLKEEKHKQHSKVLQQYKSKADHYLCSILNKNINGTNVQRTPAGL
LYVRQWNNMQYVSTASFLLTVYSDHLRKSNTDLECHEGTVTPDEMLGFAKSQIDYILGSNPMETSYLVGY
GPKYPTRVHHRGASIASFKEHKGFIGCTQGYDNWYGRSEPNPSVLVGALVGGPDCQDNFDDRRGNYVQTE
ACTYNTAPLVGVFARLIELEEQKLEEEDVSLVATY
>gnl|CDD|215231 PLN02421, PLN02421, phosphotransferase, alcohol group as acceptor/kinase
VCKALFKGWSDLDDSDFSVERISGGITNLLLKVSVKEENGNEVSVTVRLFGPNTDYVIDRERELQAIKYL
SAAGFGAKLLGVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVEIPGSKEPQLWNDIFKFYE
KASTVKFEDPEKQKKYETISFEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLMLNEDEGKLYFIDFEY
GSYSYRGYDIGNHFNEYAGFDCDYSLYPSKEEQYHFFRHYLRPDDPEEVSDAELEELFVETNFYALASHL
YWAIWAIVQAKMSPIDFDYLGYFFLRYKEYKRQKEKLLSLVRSYLSGSSK
>gnl|CDD|215232 PLN02422, PLN02422, dephospho-CoA kinase
MRVVGLTGGIASGKSTVSNLFKSSGIPVVDADKVARDVLKKGSGGWKRVVAAFGEDILLPDGEVDREKLG
QIVFSDPSKRQLLNRLLAPYISSGIFWEILKLWLKGCKVIVLDIPLLFETKMDKWTKPVVVVWVDPETQL
ERLMARDGLSEEQARNRINAQMPLDWKRSKADIVIDNSGSLEDLKQQFQKVLEKIRAPLTWKEFLRSRQG
AFSVLASVIAGVLVCRKVLLRS
>gnl|CDD|178043 PLN02423, PLN02423, phosphomannomutase
MAARKPGVIALFDVDGTLTAPRKEATPEMLEFMKELRKVVTVGVVGGSDLSKISEQLGKTVINDYDYVFS
ENGLVAHKDGKLIGTQSLKSFLGEDKLKEFINFTLHYIADLDIPIKRGTFIEFRSGMLNVSPIGRNCSQE
ERDEFEKYDKVHNIRPKMVSVLREKFAHLNLTYSIGGQISFDVFPQGWDKTYCLQFLEDFDEIHFFGDKT
YEGGNDHEIFESERTIGHTVTSPDDTREQCTALFL
>gnl|CDD|215233 PLN02424, PLN02424, ketopantoate hydroxymethyltransferase
MSNLPEDTVYGGPKPQNPAQRVTLRTLRQKYRRGEPITMVTAYDYPSAVHVDSAGIDVCLVGDSAAMVVH
GHDTTLPITLDEMLVHCRAVARGANRPLLVGDLPFGSYESSTDQAVESAVRMLKEGGMDAVKLEGGSPSR
VTAAKAIVEAGIAVMGHVGLTPQAISVLGGFRPQGRTAESAVKVVETALALQEAGCFAVVLECVPAPVAA
AITSALQIPTIGIGAGPFCSGQVLVYHDLLGMMQHPHHAKVTPKFCKQYAKVGEVINKALAEYKEEVENG
AFPGPAHSPYKISSAEVDGFAEALQKRGLDKAAEAAAAAAEKEESSDSEGSP
>gnl|CDD|215234 PLN02425, PLN02425, probable fructose-bisphosphate aldolase
MASASFVKLNAASSTWIGQRSFGQRSSSSSTRRVSFRIRAGSYSDELVQTAKSVASPGRGILAIDESNAT
CGKRLASIGLDNTETNRQAYRQLLLTTPGLGEYISGAILFEETLYQSTTDGKKFVDCLRDQNIVPGIKVD
KGLVPLPGSNNESWCQGLDGLASRSAEYYKQGARFAKWRTVVSIPCGPSALAVKEAAWGLARYAAISQDN
GLVPIVEPEILLDGDHPIERTLEVAEKVWSEVFFYLAQNNVLFEGILLKPSMVTPGAEHKEKASPETIAK
YTLTMLRRRVPPAVPGIMFLSGGQSEVEATLNLNAMNQSPNPWHVSFSYARALQNSVLKTWQGRPENVEA
AQKALLVRAKANSLAQLGRYSAEGESEEAKKGMFVKGYTY
>gnl|CDD|215235 PLN02426, PLN02426, cytochrome P450, family 94, subfamily C protein
MEAASSWLMSLAASFAFVFFFFTICFSAFALLLLLLRLKPWCNCEVCRAYLTASWAKDFDNLCDWYAHLL
RRSPTGTIHVHVLGNTITANPENVEYMLKTRFDNYPKGKPFSAILGDLLGRGIFNVDGDSWRFQRKMASL
ELGSVSIRSYAFEIVASEIESRLLPLLSSAADDGEGAVLDLQDVFRRFSFDNICKFSFGLDPGCLELSLP
ISEFADAFDTASKLSAERAMAASPLLWKIKRLLNIGSERKLKEAIKLVDELAAEVIRQRRKLGFSASKDL
LSRFMASINDDKYLRDIVVSFLLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGPNQEAASFEEM
KEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLPDGTFVAKGTRVTYHPYAMGRMERIWGPDCLEFKPER
WLKNGVFVPENPFKYPVFQAGLRVCLGKEMALMEMKSVAVAVVRRFDIEVVGRSNRAPRFAPGLTATVRG
GLPVRVRERVRT
>gnl|CDD|178047 PLN02427, PLN02427, UDP-apiose/xylose synthase
MAARLDLDGKPIKPLTICMIGAGGFIGSHLCEKLMTETPHKVLALDVYNDKIKHLLEPDTVPWSGRIQFH
RINIKHDSRLEGLIKMADLTINLAAICTPADYNTRPLDTIYSNFIDALPVVKYCSENNKRLIHFSTCEVY
GKTIGSFLPKDHPLRQDPAFYVLKEDESPCIFGSIEKQRWSYACAKQLIERLIYAEGAENGLEFTIVRPF
NWIGPRMDFIPGIDGPSEGVPRVLACFSNNLLRREPLKLVDGGQSQRTFVYIKDAIEAVLLMIENPARAN
GHIFNVGNPNNEVTVRQLAEMMTEVYAKVSGEPALEEPTVDVSSKEFYGEGYDDSDKRIPDMTIINKQLG
WNPKTSLWDLLESTLTYQHKTYAEAIKKAMSKPTAS
>gnl|CDD|215236 PLN02428, PLN02428, lipoic acid synthase
VTSTSTTAPQTPQTLAALRARLASESPSLGDFVSLGPYTLGSYGRDKPLPKPKWLRQRAPGGEKYTEIKE
KLRELKLNTVCEEAQCPNIGECWNGGGTGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPDEPENVAE
AIASWGVDYVVLTSVDRDDLPDGGSGHFAETVRRLKQLKPEILVEALVPDFRGDLGAVETVATSGLDVFA
HNIETVERLQRIVRDPRAGYKQSLDVLKHAKESKPGLLTKTSIMLGLGETDEEVVQTMEDLRAAGVDVVT
FGQYLRPTKRHLPVKEYVTPEKFEFWREYGEEMGFRYVASGPLVRSSYKAGEFFIKSMIREDRAKAAAA
>gnl|CDD|166070 PLN02429, PLN02429, triosephosphate isomerase
MAATSLTAPPSFSGLRRISPKLDAAAVSSHQSFFHRVNSSTRLVSSSSSSHRSPRGVVAMAGSGKFFVGG
NWKCNGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISV
EQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAF
ADAVPSWDNIVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAEL
AKEEDIDGFLVGGASLKGPEFATIVNSVTSKKVAA
>gnl|CDD|178049 PLN02430, PLN02430, long-chain-fatty-acid-CoA ligase
MKSFAAQVEEGVKGKDGKPSVGPVYRNLLSKKGFPPIDSDITTAWDIFSKSVEKYPDNKMLGWRRIVDGK
VGPYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAV
DYIVDHAEIDFVFVQDKKIKELLEPDCKSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKEN
PSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQFEDKMTHDDVYLSFLPLAHILD
RMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYK
YKLAWMNRGYSHKKASPMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET
LGPTTLGFPDEMCMLGTVGAPAVYNELRLEEVPEMGYDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM
KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVV
VPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVT
ATLKKRRNNLLKYYQVEIDEMYRKLAEKRI
>gnl|CDD|178050 PLN02431, PLN02431, ferredoxin--nitrite reductase
SAMSSFRFLCTLSSTLLRSTSARRVSAVRAVEREVAAAATVSPPATAAVDADRLEPRVEERDGYWVLKEE
FRKGINPQEKVKLEKEPMKLFMENGIEELAKTPFEEIDKSKLSKDDIDVRLKWLGLFHRRKHQYGRFMMR
LKLPNGVTTSAQTRYLASVIEKYGEDGCADVTTRQNWQIRGVVLPDVPAILKGLEEVGLTSLQSGMDNVR
NPVGNPLAGIDPHEIVDTRPYTNLLSDYITNNGRGNPEITNLPRKWNVCVVGSHDLFEHPHINDLAYMPA
TKDGRFGFNLLVGGFFSPKRCAEAIPLDAWVPADDVVPLCKAILEAFRDLGTRGNRQKTRMMWLIDELGV
EGFRSEVEKRMPNGELERAASEDLVDKKWERRDYLGVHPQKQEGLSYVGLHVPVGRLQAADMDELARLAD
EYGSGELRLTVEQNIIIPNVPNSKVEALLAEPLLQRFSPNPGLLLKGLVACTGNQFCGQAIIETKARALK
VTEELERLVEVPRPVRMHWTGCPNSCGQVQVADIGFMGCMARDENGKAVEGADIFVGGRVGSDSHLAEEY
KKGVPCDELVPVVADILIEEFGAKERE
>gnl|CDD|178051 PLN02432, PLN02432, putative pectinesterase
STSSIDLSTAILIRVDQSGKGDFRKIQDAIDAVPSNNSQLVFIWVKPGIYREKVVVPADKPFITLSGTQA
SNTIITWNDGGDIFESPTLSVLASDFVGRFLTIQNTFGSSGKAVALRVAGDRAAFYGCRILSYQDTLLDD
TGRHYYRNCYIEGATDFICGNAASLFEKCHLHSLSPNNGAITAQQRTSASENTGFTFLGCKLTGAGTTYL
GRPWGPYSRVVFALSYMSSVVAPQGWDDWGDSSKQSTVFYGEYKCYGPGADRSKRVEWSHDLSQDEAAPF
LTKDMIGGQSWLR
>gnl|CDD|215237 PLN02433, PLN02433, uroporphyrinogen decarboxylase
LLRAARGEKVERPPVWLMRQAGRYMKEYRELCKKYPSFRERSETPDLAVEISLQPWRAFKPDGVILFSDI
LTPLPAMGIPFDIVKGKGPVIPNPIRSEEDVKRLHPLDPEEKLPFVGEALKILRKEVGNEAAVLGFVGAP
WTLATYIVEGGSSKNYKVIKKMAFTAPEVLHALLDKLTDAVIEYVDYQIDAGAQVVQIFDSWAGHLSPVD
FEEFSKPYLEKIVDEVKARHPDVPLILYANGSGGLLERLAGTGVDVIGLDWTVDMADARRRLGSDVAVQG
NVDPAVLFGSKEAIEKEVRDVVKKAGPQGHILNLGHGVLVGTPEENVAHFFDVARELRYEMIAQA
>gnl|CDD|178053 PLN02434, PLN02434, fatty acid hydroxylase
MVAQKFTVDLNKPLVFQVGHLGEDYEEWVHQPIVSKEGPRFFESDVLEFLTRTVWWAVPLIWLPVVCWCL
VKSVRMGLPLSAVVLMVAFGVFIWTLLEYILHRFLFHIKTKSYWGNTAHYLLHGCHHKHPMDGLRLVFPP
AATAILCVPFWNLIALFATPATAPALFGGGLLGYVMYDCTHYFLHHGQPSTDVLRNLKKYHLNHHFRDQD
KGFGITSSLWDRVFGTLPPSKAAKKKR
>gnl|CDD|215238 PLN02435, PLN02435, probable UDP-N-acetylglucosamine pyrophosphorylase
MKEPVVENEAVTAPGPWGAAPPQALLERLKDYGQEDAFALWDELSPEERDLLVRDIESLDLPRIDRIIRC
SLRSQGLPVPAIEPVPENSVSTVEERTPEDRERWWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFN
IGLPSGKSLFQLQAERILCVQRLAAQASSEGPGRPVTIHWYIMTSPFTDEATRKFFESHKYFGLEADQVT
FFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLLEDMASRGIKYVDCYGVDNALVRVADP
TFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRRGKGGPLTVVEYSELDQAMASAINQQTGRLRYCWSNVC
LHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIHGYTMGLKLEQFIFDAFPYAPSTALFEVLREEEFAPVK
NANGSNFDTPESARLLVLRLHTRWVVAAGGFLTHSVPLYATGVEVSPLCSYAGENLEAICRGRTFHAPCE
ISF
>gnl|CDD|215239 PLN02436, PLN02436, cellulose synthase A
MNTGGRLIAGSHNRNEFVLINADEIARIRSVQELSGQTCQICGDEIELTVDGEPFVACNECAFPVCRPCY
EYERREGNQACPQCKTRYKRIKGSPRVEGDEEEDDIDDLENEFDYGNNGLDPEQVAEAMLSSRLNTGRHS
NVSGIATPSELDSAPPGSQIPLLTYGEEDVEISSDRHALIVPPSTGHGNRVHPMPFPDSSASLQPRPMVP
QKDLAVYGYGSVAWKDRMEEWKKKQNEKLQVVKHEGGNDGGNNDGDELDDPDLPMMDEGRQPLSRKLPIP
SSKINPYRMIIILRLVILGLFFHYRILHPVNDAYGLWLTSVICEIWFAVSWILDQFPKWYPIERETYLDR
LSLRYEKEGKPSELASVDVFVSTVDPMKEPPLITANTVLSILAVDYPVDKVACYVSDDGAAMLTFEALSE
TSEFARKWVPFCKKFSIEPRAPEWYFSQKMDYLKNKVHPAFVRERRAMKREYEEFKVKINALVATAQKVP
EDGWTMQDGTPWPGNNVRDHPGMIQVFLGHSGVRDVEGNELPRLVYVSREKRPGFDHHKKAGAMNSLIRV
SAVLSNAPYLLNVDCDHYINNSKALREAMCFMMDPQSGKKICYVQFPQRFDGIDRHDRYSNRNVVFFDIN
MKGLDGIQGPIYVGTGCVFRRQALYGYDAPKKKKPPGKTCNCWPKWCCLCCGSRKKKKKKKSKEKKKKKN
REASKQIHALENIEEGIEGSNNEKSSETPQLKLEKKFGQSPVFVASTLLENGGVPRNASPASLLREAIQV
ISCGYEDKTEWGKEIGWIYGSVTEDILTGFKMHCHGWRSVYCIPKRPAFKGSAPINLSDRLHQVLRWALG
SVEIFLSRHCPIWYGYGGGLKWLERFSYINSVVYPWTSIPLIVYCTLPAICLLTGKFIVPEISNYASILF
MALFISIAATGILEMQWGGVGIDDWWRNEQFWVIGGVSSHLFALFQGLLKVLAGVNTNFTVTSKAADDGE
FSELYLFKWTSLLIPPTTLLIINIIGVIVGVSDAINNGYDSWGPLFGRLFFALWVIVHLYPFLKGLLGKQ
DRMPTIILVWSILLASILTLLWVRVNPFVSKGGPVLEICGLDCD
>gnl|CDD|178056 PLN02437, PLN02437, ribonucleoside--diphosphate reductase large subunit
MYVVKRDGRQETVHFDKITARLKKLSYGLSQDHCDPVLVAQKVCAGVYKGVTTSQLDELAAETAAAMTTN
HPDYAILAARIAVSNLHKNTKKSFSETVKDMYNHVNERSGLKAPLIADDVYDIIMKNAARLDSEIIYDRD
FDYDYFGFKTLERSYLLKVNGKVVERPQHMLMRVSVGIHKDDIESAIKTYHLMSQRWFTHASPTLFNAGT
PRPQLSSCFLICMKDDSIEGIYDTLKECAVISKSAGGIGLSVHNIRATGSYIRGTNGTSNGIVPMLRVFN
DTARYVDQGGGKRKGAFAIYLEPWHADIFEFLDLRKNHGKEEHRARDLFYALWIPDLFMERVQSNGDWSL
FCPNEAPGLADCWGEEFERLYTKYEREGKAKKVVQAQQLWFAILESQIETGTPYMLFKDSCNRKSNQQNL
GTIKSSNLCTEIIEYTSPTETAVCNLASIALPRFVREKGVPLESHPSKLVGSLGSKNRYFDFEKLAEVTA
VVTRNLNKIIDVNYYPVETARRSNMRHRPIGIGVQGLADAFILLGMPFDSPEAQQLNKDIFETIYYHALK
ASSELAAREGPYETYAGSPVSKGILQPDMWGVTPSGRWDWAALREMISKNGVRNSLLVAPMPTASTSQIL
GNNECFEPYTSNIYSRRVLSGEFVVVNKHLLHDLTEMGLWTPTLKNKIIAENGSVQKIPEIPDDLKAIYK
TVWEIKQRTLVDMAADRGCYIDQSQSLNIHMDQPNFGKLTSLHFYAWSKGLKTGMYYLRSRAAADAIKFT
VDTASLKPSATGVAAPEEEDVETKMAQMVCSLDNREECLACGS
>gnl|CDD|178057 PLN02438, PLN02438, inositol-3-phosphate synthase
MFIESFKVESPNVKYTEDEIHSVYDYETTELVHENRNGKYQWVVKPKTVKYEFKTDRRVPKLGVMLVGWG
GNNGSTLTAGVIANKEGISWATKDGVQKANYFGSLTQASTIRVGSFNGEEIYAPFKSLLPMVNPNDIVFG
GWDISDMNLADAMERAKVLDIDLQKQLRPYMENMVPLPGIYDPDFIAANQGSRANNVIKGTKKEQMDQIR
KDIREFKEKNKVDKVVVLWTANTERYSNVVVGLNDTMENLLASIEKDEAEISPSTLYALACILEGVPFIN
GSPQNTFVPGVIELAVKKNSLIGGDDFKSGQTKMKSVLVDFLVGAGIKPTSIVSYNHLGNNDGMNLSAPQ
TFRSKEISKSNVVDDMVASNSILYEPGEHPDHVVVIKYVPYVGDSKRAMDEYTSEIFMGGKNTIVMHNTC
EDSLLAAPIILDLVLLAELSTRIQLKAEGEEKFHSFHPVATLLSYLTKAPLVPPGTPVVNALAKQRAMLE
NILRACVGLAPENNMLLEYK
>gnl|CDD|215240 PLN02439, PLN02439, arginine decarboxylase
LIVRFPDVLKNRLESLQSAFDYAIQSQGYNSHYQGVFPVKCNQDRFLVEDIVKFGSPFRFGLEAGSKPEL
LLAMSCLCKGSPDAFLICNGYKDAEYVSLALLARKLGLNTVIVLEQEEELDLVIEASQRLGVRPVIGVRA
KLRTKHSGHFGSTSGEKGKFGLTATEIVRVVRKLRKEGMLDCLQLLHFHIGSQIPSTSLLKDGVSEAAQI
YCELVRLGAPMRVIDIGGGLGIDYDGSKSGSSDMSVAYSLEEYANAVVAAVRDVCDRKGVKHPVICSESG
RALVSHHSVLIFEAVSASKRGVPAADDDDQYLLLGLTEELRADYENLYAAADRGDYEECLLYADQLKQEC
VRLFKEGLLSLEQRAAVDGLCELVSKRVGASDPVATYHINLSVFTSIPDFWAIGQLFPIVPLHRLDERPT
VRGILSDLTCDSDGKIDKFIGGEGSLPLHELEKNGGGPYYLGMFLGGAYQEALGSLHNLFGGPSVVRVSQ
SDGPGGFAVTRAVPGQSCADVLRAMQHEPELMFETLKHRAEEYVHKGGLSGAVAANLARSFHNMPYLSA
>gnl|CDD|215241 PLN02440, PLN02440, amidophosphoribosyltransferase
ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIG
HVRYSTAGASSLKNVQPFVANYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKA
RPFFSRIVDACEKLKGAYSMVFLTEDKLVAVRDPHGFRPLVMGRRSNGAVVFASETCALDLIGATYEREV
NPGEVIVVDKDKGVSSQCLMPHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDCDVVI
PVPDSGRVAALGYAAKLGVPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSI
VRGTTSSKIVRMLREAGAKEVHMRIASPPIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPL
EDLKKSLGEESPRFCYACFSGDYPVLPKRVGGDIDDGYLESLEEAGRGWGRKGRRQEAQ
>gnl|CDD|215242 PLN02441, PLN02441, cytokinin dehydrogenase
AKSLMLSLRLLLILFLSSLTSSVGLCSSPSSLLPKLLSLDGHLSFDPVSTASASKDFGNLVHSLPAAVLY
PSSVEDIASLVRAAYGSSSPLTVAARGHGHSLNGQAQAPGGVVVDMRSLRGGVRGPPVIVVSGDGPYVDV
SGGELWIDVLKATLKHGLAPRSWTDYLYLTVGGTLSNAGISGQAFRHGPQISNVLELDVVTGKGEVVTCS
PTQNSDLFFAVLGGLGQFGIITRARIALEPAPKRVRWIRVLYSDFSTFTRDQERLISRPPENSFDYVEGF
VIVNRNGLINNWRSSFFSPSDPVRASSLPSDGGVLYCLEVAKYYDEDTSDTVDQEVESLLKRLSFIPGLL
FTTDVSYVDFLDRVHVEELKLRSKGLWEVPHPWLNLFVPKSRIADFDDGVFKGILLDGTNGPILVYPLNR
SKWDNRTSAVIPDEDIFYLVALLRSALPSGDDLEHLLAQNKEILRFCEKAGIGVKQYLPHYTTQEEWKRH
FGPKWETFVRRKAKFDPLAILSPGQRIFNRASSSL
>gnl|CDD|178061 PLN02442, PLN02442, S-formylglutathione hydrolase
MAAALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQ
RAAAARGIALVAPDTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWKNWRMYDYVVKELPKLLSDNFDQL
DTSRASIFGHSMGGHGALTIYLKNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELV
SKFNDVSATILIDQGEADKFLKEQLLPENFEEACKEAGAPVTLRLQPGYDHSYFFIATFIDDHINHHAQA
LKS
>gnl|CDD|178062 PLN02443, PLN02443, acyl-coenzyme A oxidase
MEGVDHLAGERNKAQFDVDAMKIVWAGSRHAFEVSDRMARLVASDPVFSKDNRTRLSRKELFKNTLRKAA
HAWKRIIELRLTEEEAGKLRSFVDEPGYTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTEL
GHGSNVQGLETTATFDPKTDEFVIHSPTLTSSKWWPGGLGKVSTHAVVYARLITNGKDHGIHGFIVQLRS
LDDHSPLPGVTVGDIGMKFGNGAYNTMDNGFLRFDHVRIPRDQMLMRLSKVTREGKYVQSDVPRQLVYGT
MVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGPETQVIDYKTQQSRLFPLLASAYAFRFVGEW
LKWLYTDVTQRLEANDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPA
CTYEGDNVVLLLQVARFLMKTVSQLGSGKKPVGTTAYMGRVQHLLQCRCGVQTAEDWLNPSVVLEAFEAR
AARMAVTCAQNLSKFENQEAGFQELSADLVEAAVAHCQLIVVSKFIEKLQQDIPGKGVKKQLQNLCYIYA
LYLLHKHLGDFLSTGCITPKQASLANDQLRSLYSQVRPNAVALVDAFNYTDHYLGSVLGRYDGNVYPKLY
EEAWKDPLNDSVVPDGYEEYLRPLLKQQLRTARL
>gnl|CDD|215243 PLN02444, PLN02444, HMP-P synthase
TLLSVVCNNANSSAPLKLPNSSLLPGFDVVVRAQALAVSAARLKKESTATRATLTFDPPTGNSEKAKQTK
PTVDPSAPDFLPIPSFEECFPKSTKEYKEVVHEESGHVLKVPFRRVHLSGDEPHFDNYDTSGPQNIDPRI
GLPKLRKEWIDRREKLGTPRYTQMYYAKQGIITEEMLYCATREKLDPEFVRSEVARGRAIIPSNKKHLEL
EPMIVGRNFLVKVNANIGNSAVTSSIEEEVYKLQWATMWGADTVMDLSTGRHIHETREWILRNSPVPVGT
VPIYQALEKVDGIAENLTWEVFRETLIEQAEQGVDYFTIHAGVLLRYIPLTAKRMTGIVSRGGSIHAKWC
LAYHKENFAYEHWDDILDICNQYDIALSIGDGLRPGSIYDANDTAQFAELLTQGELTRRAWEKDVQVMNE
GPGHVPLHKIPENMQKQLEWCNEAPFYTLGPLTTDIAPGYDHITSAIGAANIGALGTALLCYVTPKEHLG
LPNRDDVKAGVIAYKIAAHAADLAKGHPHAQAWDDALSKARFEFRWMDQFALSLDPVTAMSFHDETLPSE
GAKVAHFCSMCGPKFCSMKITEDVRKYAEEHGYGSAEEAVKQGMDAMSAEFLAAKKTISGEQHGESGGEI
YLPESYVASKNP
>gnl|CDD|215244 PLN02445, PLN02445, anthranilate synthase component I
FKEAAKGGNLVPLYRRIFSDHLTPVLAYRCLVKEDDREAPSFLFESVEPGSQSSNVGRYSVVGAQPAMEI
VAKENKVTIMDHEKGTRTEEIVEDPMEIPRRISEKWNPQLIDGLPDVFCGGWVGYFSYDTVRYVEKKKLP
FSGAPEDDRNLPDIHLGLYDDVIVFDHVEKKAYVIHWVRLDRYSSVEEAYEDGMKRLEALVSRLQDINPP
KLSPGSVKLSTNQFGPSLEKSNMTSEEYKNAVLQAKEHILAGDIFQIVLSQRFERRTFADPFEVYRALRI
VNPSPYMIYLQARGCILVASSPEILTRVKKNKIVNRPLAGTRRRGKTPEEDKALEKDLLADEKQCAEHIM
LVDLGRNDVGKVSKAGSVKVEKLMNIERYSHVMHISSTVTGELLDHLTSWDALRAALPVGTVSGAPKVRA
MELIDELEVTRRGPYSGGFGGVSFTGDMDIALALRTMVFPTAARYDTMYSYKDTNSRREWVAHLQAGAGI
VADSDPEDEYRECVNKAAGLARAIDLAESAFVK
>gnl|CDD|215245 PLN02446, PLN02446, (5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase
VRFRPCIDIHKGKVKQIVGSTLKDSKDGSEDGSELVTNFESDKSAAEFAEMYKRDGLTGGHVIMLGADDA
SLAAALEALRAYPGGLQVGGGVNSENAMSYLDAGASHVIVTSYVFRDGQIDLERLKDLVRLVGKQRLVLD
LSCRKKDGRYYVVTDRWQKFSDLAVDEETLEFLAAYCDEFLVHGVDVEGKRLGIDEELVALLGEHSPIPV
TYAGGVRSLDDLERVKVAGGGRVDVTVGSALDIFGGNLPYDDVVAWHKQQKT
>gnl|CDD|215246 PLN02447, PLN02447, 1,4-alpha-glucan-branching enzyme
ALSEHVLSPDGLPDSAPSPSPAVDEPRPEDPGSPATEAPYPAKTEDNSAAASPPPPGDGLGIYEIDPMLE
PYEDHLRYRYSRYRRRREEIEKNEGGLEAFSRGYEKFGFNRSEGGITYREWAPGAKAAALIGDFNNWNPN
AHWMTKNEFGVWEIFLPDADGSPAIPHGSRVKIRMETPDGRWVDRIPAWIKYAVQAPGEIGAPYNGVYWD
PPEEEKYVFKHPRPPRPAALRIYEAHVGMSSEEPKVNSYREFADDVLPRIKALGYNAVQLMAIQEHAYYG
SFGYHVTNFFAVSSRSGTPEDLKYLIDKAHSLGLRVLMDVVHSHASKNTLDGLNGFDGTDGSYFHSGPRG
YHWLWDSRLFNYGNWEVLRFLLSNLRWWLEEYKFDGFRFDGVTSMLYHHHGLQMAFTGNYNEYFGMATDV
DAVVYLMLANDLLHGLYPEAVTIAEDVSGMPTLCRPVQEGGVGFDYRLAMAIPDKWIELLKEKRDEDWSM
GDIVHTLTNRRYTEKCVAYAESHDQALVGDKTIAFWLMDKEMYDGMSTLTPATPVVDRGIALHKMIRLIT
MALGGEGYLNFMGNEFGHPEWIDFPREGNGWSYDKCRRRWDLADADHLRYKFLNAFDRAMMHLDEKYGFL
TSEHQYVSRKDEGDKVIVFERGDLVFVFNFHPTNSYSDYRVGCDKPGKYKIVLDSDAWEFGGFGRVDHDA
DHFTPEGNFDNRPHSFMVYAPSRTAVVYAPVDEDDEPADRKPVGINGLAGRDLGGYED
>gnl|CDD|215247 PLN02448, PLN02448, UDP-glycosyltransferase family protein
DAVGSSPTTSCHVVAMPYPGRGHINPMMNLCKLLASRKPDILITFVVTEEWLGLIGSDPKPDNIRFATIP
NVIPSELVRAADFPGFLEAVMTKMEAPFEQLLDRLEPPVTAIVADTYLFWAVGVGNRRNIPVASLWTMSA
TFFSVFYHFDLLPQNGHFPVELSESGEERVDYIPGLSSTRLSDLPPIFHGNSRRVLKRILEAFSWVPKAQ
YLLFTSFYELEAQAIDALKSKFPFPVYPIGPSIPYMELKDNSSSSNNEDNEPDYFQWLDSQPEGSVLYVS
LGSFLSVSSAQMDEIAAGLRDSGVRFLWVARGEASRLKEICGDMGLVVPWCDQLKVLCHSSVGGFWTHCG
WNSTLEAVFAGVPMLTFPLFWDQPLNSKLIVEDWKIGWRVKREVGEETLVGREEIAELVKRFMDLESEEG
KEMRRRAKELQEICRGAIAKGGSSDTNLDAFIRDISQGR
>gnl|CDD|178068 PLN02449, PLN02449, ferrochelatase
TALSSGVRPLACSKSSSPPRAGSSSRSLSLIQCVSSFRSASSSSSSLALRSSSLRLRANLAASSTSASAV
DSPDDDEAVADHPKVSEEKVGVLLLNLGGPETLDDVQPFLYNLFADPDIIRLPRLFRFLQKPLAQFISNL
RAPKSKEGYASIGGGSPLRKITDEQAEALAKALEAKNLPAKVYVGMRYWHPFTEEAIDQIKADGITKLVV
LPLYPQFSISTSGSSLRLLESIFREDEYLVNMQHTVIPSWYQREGYVKAMADLIKKELAKFSDPEEVHIF
FSAHGVPVSYVEEAGDPYKAQMEECVDLIMEELKARGILNRHTLAYQSRVGPVEWLKPYTDETIVELGKK
GVKSLLAVPISFVSEHIETLEEIDMEYRELALESGIENWGRVPALGCEPTFISDLADAVIEALPYVGAMA
VSNLEARQSLVPLGSVEELLATYDSQRRELPPVAVWEWGWTKAAMLAVLLLLVLEVTSGFGNLHQ
>gnl|CDD|178069 PLN02450, PLN02450, 1-aminocyclopropane-1-carboxylate synthase
MKLLSRKATCNSHGQDSSYFLGWEEYEKNPYDEIKNPSGIIQMGLAENQLSFDLIESWLAKNPDAAGLKR
NGQSIFRELALFQDYHGLPAFKNALAEFMSEIRGNKVTFDPNKLVLTAGATSANETLMFCLAEPGDAFLL
PTPYYPGFDRDLKWRTGVEIVPIHCSSSNGFQITESALEEAYQQAQKLNLKVKGVLITNPSNPLGTTTTR
TELNLLVDFITAKNIHLISDEIYSGTVFDSPGFVSVMEVLKDRKLENTDVSNRVHIVYSLSKDLGLPGFR
VGAIYSNDEMVVSAATKMSSFGLVSSQTQYLLSALLSDKKFTKNYLEENQKRLKQRQKKLVSGLEAAGIK
CLKSNAGLFCWVDMRHLLKSNTFEAEMELWKKIVYEVKLNISPGSSCHCTEPGWFRVCFANMSEETLDLA
MKRLKSFVESDSGRRINKSSHQRLKNLRRKTVSKWVFRLSFHDREPEE
>gnl|CDD|215248 PLN02451, PLN02451, homoserine kinase
MAAICFQSPSKPISSSPSTSKTSPPLFARRSVRRVRCNVSLTGKVEPEPVFTSVKAFAPATVANLGPGFD
FLGCAVDGLGDFVTARVDPGVRPGEVSISEITGDTGRLSKDPLRNCAGIAAIATMKLLGIRSVGLSLSLH
KGLPLGSGLGSSAASAAAAAVAVNELFGSPLGKDDLVLAGLESEAKVSGYHADNIAPALMGGFVLIRSYE
PLHLIPLRFPSAKDLFFVLVSPDFEAPTKKMRAALPKEIPMKHHVWNCSQAAALVAAILQGDAVLLGEAL
SSDKIVEPTRAPLIPGMEAVKKAALEAGAYGCTISGAGPTAVAVIDDEEKGEEVGERMVEAFRKAGNLKA
TASVKKLDRVGARLVESVSR
>gnl|CDD|178071 PLN02452, PLN02452, phosphoserine transaminase
SQGSQGRVFNFSAGPATLPANVLAKAQAELYNWEGSGMSVMEMSHRGKEFLSIIQKAEADLRELLDIPDN
YEVLFLQGGASTQFAAIPLNLCKPGDKADFVVTGSWSKKAAKEAKKYCKTNVIASGKDEKYTKIPSVSEW
ELTPDAKFVHICANETIHGVEFKDYPDVGNVPLVADMSSNFLSKPVDVSKYGVIYAGAQKNVGPSGVTIV
IIRKDLIGNARPITPGMLDYKIHAENDSLYNTPPCFGIYMCGLVFEDLLAQGGLKAMEKRNIRKADLLYD
AIDESNGFYVCPVEKSVRSLMNVPFTLGGSELEAEFVKEAAKAGMVQLKGHRSVGGMRASIYNAMPLAGV
EKLVAFMKDFQAKHA
>gnl|CDD|178072 PLN02453, PLN02453, complex I subunit
QSAPRTAASRMLRGRQRSQLRSRGAGGPGRWFAPGHEEGPNGYLFNETPPPPGQSRKWEDWELPCYITSF
LTIVILGVGLNAKPDTRIETWAHQKALERLEAEEL
>gnl|CDD|215249 PLN02454, PLN02454, triacylglycerol lipase
GVGQGSASWPELLGSANWDGLLDPLDLSLRELILRCGDFCQATYDSFNNDQNSKYCGASRYGKSSFFDKV
MLEAASDYEVAAFLYATARVSLPEAFLLHSMSRESWDRESNWIGYIAVTSDERTKALGRREIYVAWRGTT
RNYEWVDVLGAKLTSADPLLPGPEQDGVVSGSSSDSDDDDEKGPKVMLGWLTIYTSDDPRSPFTKLSARS
QLLAKIKELLERYKDEKLSIVLTGHSLGASLATLAAFDIVENGVSGADIPVTAIVFGSPQVGNKEFNDRF
KEHPNLKILHVRNTIDLIPHYPGGLLGYVNTGTELVIDTRKSPFLKDSKNPGDWHNLQAMLHVVAGWNGK
KGEFELKVKRSLALVNKSCAFLKDECLVPGSWWVEKNKGMVRGEDGEWVLAPPAEEDLPVPEVV
>gnl|CDD|178074 PLN02455, PLN02455, fructose-bisphosphate aldolase
MSAFVGKYADELIKNAKYIATPGKGILAADESTGTIGKRLASINVENVESNRQALRELLFTAPGALQYLS
GVILFEETLYQKTSDGKPFVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKYYEAGARF
AKWRAVLKIGPTEPSELAIQENAQGLARYAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYK
ALNDHHVLLEGTLLKPNMVTPGSDSPKVSPEVIAEYTVRALQRTVPPAVPGIVFLSGGQSEEEATLNLNA
MNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQAAFLVRCKANSEATLGKYKGDAAGGEGASES
LHVKDYKY
>gnl|CDD|215250 PLN02456, PLN02456, citrate synthase
AAAVSCTSSSLSRAAPGGGSGSLTIVDNRTGKDYESPLSELGPVQAERLKKIKAGKDDLGLKTVDPGYRN
TAPVLSEISLIDGDEGILRFRGYPIEELAEKSPFEEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVL
DVIDALPHDAHPMTQLVSGVMALSTFSPDANAYLRGQHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMYG
RGPVIPDNSLDYAENFLYMLGSLGDRSYKPDPRLARLLDLYFIIHADHEGGCSTAAARHLVGSSGVDPYT
SVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIPEYVEGVKNSKKVLPGFGHRVYKNYDPRAKCIREFA
LEVFKHVGDDPLFKVASALEEVALLDEYFKVRKLYPNVDFYSGVLLRALGFPEEFFTVLFAVSRAAGYLS
QWDEALGLPDERIMRPKQVYTGEWLRHYCPKAERT
>gnl|CDD|215251 PLN02457, PLN02457, phenylalanine ammonia-lyase
VGAASSEGFCIGGADPLNWGKAAEALKGSHLDEVKRMVAEYRKPVVKLEGETLTIAQVAAVARRGAGGVR
VELSESARARVKASSDWVMESMMKGTDSYGVTTGFGATSHRRTKQGGALQRELIRFLNAGIFGTGESGHT
LPASATRAAMLVRINTLLQGYSGIRFEILEAITKLLNANVTPCLPLRGTITASGDLVPLSYIAGLLTGRP
NSKAVTPDGEKVTAAEAFKLAGIEGGFFELQPKEGLALVNGTAVGSALASTVLFDANVLAVLAEVLSAVF
CEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEHILDGSSYMKAAKKLHETDPLQKPKQDRYALRTSPQWL
GPQIEVIRAATKSIEREINSVNDNPLIDVARDKALHGGNFQGTPIGVSMDNTRLAIAAIGKLMFAQFSEL
VNDFYNNGLPSNLSGGRNPSLDYGFKGAEIAMASYCSELQYLANPVTNHVQSAEQHNQDVNSLGLISARK
TAEAVDILKLMSSTYLVALCQAIDLRHLEENLKSAVKNTVSQVAKKTLTTGANGELHPSRFCEKDLLKVV
DREPVFSYIDDPCSATYPLMQKLRQVLVEHALANGEAEKNASTSVFRKIGAFEEELKAALPKEVEAAREA
YENGTAPIPNRIKECRSYPLYRFVREELGTELLTGEKTRSPGEEFDKVFDAICQGKLIDPLLECLKEWNG
APLPIC
>gnl|CDD|215252 PLN02458, PLN02458, transferase, transferring glycosyl groups
MGSLERSKKKVQLWKKAVVHFSLCFVMGFFTGFAPAGKASFFSSHEAASNKSQFSPQPVEMLHVATTPHH
SNLNRTLINAQTPVPAPARSAESETASLLEKEEEEPKLAPRRLVIIVTPISTKDRYQGVLLRRLANTLRL
VPPPLLWIVVEGQSDSEEVSEMLRKTGIMYRHLVFKENFTDPEAELDHQRNLALRHIEHHKLSGIVHFAG
LSNVYDLDFFDEIRDIEVFGTWPMALLSANRNKVIIEGPVCDSSQVIGWHLKKMNNETETRPPIHISSFA
FNSSILWDPERWGRPSSVQGTSQNSIKFVKQVALEDETKLKGIPPEDCSKIMLWRLNFPTRTRLSR
>gnl|CDD|215253 PLN02459, PLN02459, probable adenylate kinase
LSERDAKSTSALADDLASACDRSLAKGRNVNWVFLGCPGVGKGTYASRLSKLLGVPHIATGDLVREEIKS
SGPLGAQLKEIVNQGKLVPDEIIFSLLSKRLEAGEEEGESGFILDGFPRTVRQAEILEGVTDIDLVVNLK
LREEVLVEKCLGRRICSECGKNFNVADIDLKGEDGRPGIVMPPLLPPPECASKLITRADDTEEVVKARLR
VYKEESQPVEDFYRKRGKLLEFELPGGIPETWPRLLQALNLDDEDKRSAAA
>gnl|CDD|215254 PLN02460, PLN02460, indole-3-glycerol-phosphate synthase
ASKSGSALYDDMFNALEVKEWEVGMSQNEIAASQGIRIRRRPPTGPPLHYVGPFQFRLQNEGNTPRNILE
EIVWYKDVEVAQMKERKPLYLLKKALQNAPPARDFVGALRAAHKRTGQPGLIAEVKKASPSRGVLRENFD
PVEIAQAYEKGGAACLSVLTDEKYFQGSFENLEAIRNAGVKCPLLCKEFIVDAWQIYYARSKGADAILLI
AAVLPDLDIKYMLKICKSLGMAALIEVHDEREMDRVLGIEGVELIGINNRSLETFEVDISNTKKLLEGER
GEQIREKGIIVVGESGLFTPDDVAYVQNAGVKAVLVGESLVKQDDPGKGIAGLFGKDI
>gnl|CDD|215255 PLN02461, PLN02461, Probable pyruvate kinase
MANIDIEGILKGLPADGLRRPKTKIVCTLGPASRSVPMLEKLLRAGMNVARFNFSHGSHEYHQETLDNLR
QAMANTGILCAVMLDTKGPEIRTGFLKDGKPVQLKQGQEITITTDYSIKGDENMIAMSYKKLAVDVKPGS
VILCADGTITLTVLSCDVEAGTVRCRCENSAMLGERKNVNLPGVVVDLPTLTEKDKEDILQWGVPNKIDF
IALSFVRKGSDLVEVRKVLGEHAKSILLISKVENQEGLDNFDDILAESDAFMVARGDLGMEIPIEKIFLA
QKMMIYKCNLAGKPVVTATQMLESMIKSPRPTRAEATDVANAVLDGTDCVMLSGETAAGAYPELAVKTMA
RICREAEASLDYGALFKEIMRSAPLPMSPLESLASSAVRTANKVKASLIVVLTRGGTTARLVAKYRPAVP
ILSVVVPEITTDSFDWSCSDEAPARHSLIYRGLIPVLAEGSAKATDSESTEEILEAAIEHAKKKGLCKPG
DSVVALHRIGGASVIKILTVK
>gnl|CDD|215256 PLN02462, PLN02462, sedoheptulose-1,7-bisphosphatase
SLEEFLAKATPDKKLRRLIMCMGEACRTIAFKVRTASCTGTACVNSFGDEQLAVDMLADKLLFEALKYSH
VCKYACSEEVPEVQDMGGPVEGGFSVAFDPLDGSSIVDTNFAVGTIFGVWPGDKLTGVTGRDQVAAAMGI
YGPRTTYVVALKDGPGTHEFLLLDDGKWQHVKETTEIGEGKIFSPGNLRATFDNPGYEKLINYYVSEKYT
LRYTGGMVPDVYQIIVKEKGVFTNVTSPKSKAKLRLLFEVAPLGLLVEKAGGKSSDGVQGGSVLDKQINN
LDQRTQVAYGSKNEVIRFEETLYG
>gnl|CDD|178082 PLN02463, PLN02463, lycopene beta cyclase
ALLELVPETKKENLDFELPRFDPSKSRVVDLVVVGGGPAGLAVAQQVSEAGLSVCCIDPSPLSIWPNNYG
VWVDEFEALGLLDCLDTTWPGAVVYIDDGKKKDLDRPYGRVNRKKLKSKMLERCIANGVQFHQAKVKKVV
HEESKSLVVCDDGVKIQASLVLDATGFSRCLVQYDKPFNPGYQVAYGILAEVDSHPFDLDKMLFMDWRDS
HLGNNPELRARNSKLPTFLYAMPFSSNRIFLEETSLVARPGLPMDDIQERMVARLRHLGIKVKSVEEDEK
CVIPMGGPLPVIPQRVLGIGGTAGMVHPSTGYMVARTLAAAPIVADAIVEYLGSSRSNSFRGDELSAEVW
NDLWPIERRRQREFFCFGMDILLKLDLDGTRRFFDAFFDLEPHYWHGFLSSRLFLPELLLFGLSLFSHAS
NTSRLEIMAKGTVPLVKMINNLIQDRI
>gnl|CDD|215257 PLN02464, PLN02464, glycerol-3-phosphate dehydrogenase
MSLARLRRLAAGAAATAAGGAVYLSPQPASSDKGGGPALDSLRDRIADPNASVPSRSAQESALIGATAAE
PLDVLVVGGGATGAGVALDAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFQLDYGQLKLVF
HALEERKQLIENAPHLCHALPIMTPCYDWFEVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLA
KKGKDGSLKGTVVYYDGQMNDSRLNVALACTAALAGAAVLNYAEVVSLIKDESTGRIVGARVRDNLTGKE
FDVYAKVVVNAAGPFCDEVRKMADGKAKPMICPSSGVHIVLPDYYSPEGMGLIVPKTKDGRVVFMLPWLG
RTVAGTTDSKTPITMLPEPHEDEIQFILDAISDYLNVKVRRSDVLSAWSGIRPLAVDPSAKSTESISRDH
VVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKSGKLSPTNGCVTTDLPLVGAEGYEPSLFTQLAQQYVR
MKRTYGGKVVPGAMDTAAAKHLAHAYGGRADRVAEIAQNEGLGKRLAHGYPFLEAEVAYCARHEYCESAV
DFIARRTRLAFLDTDAAVRALPRVVEILAAEHGWDKSRKKQELQKAKEFLETFKSSKNAQFNDGKHN
>gnl|CDD|215258 PLN02465, PLN02465, L-galactono-1,4-lactone dehydrogenase
SGAAAGNFAGPLAPPPPKPTQGPRSFARGALSSAGGEPASAATVRRYLGYAALLLFSAAATYYSFPFPEN
AKHKKAAPLPEDLHTVSNWSGTHEVQTRRYHQPESLEELEDIVKEAHEKGRRIRPVGSGLSPNGLAFSRE
GMVNLALMDKVLEVDKEKKRVTVQAGARVQQVVEALRPHGLTLQNYASIREQQIGGFIQVGAHGTGARIP
PIDEQVVSMKLVTPAKGTIELSKEDDPELFRLARCGLGGLGVVAEVTLQCVPAHRLVEHTFVSNRKEIKK
NHKKWLSENKHIRYMWIPYTDTVVVVTCNPLSKWKEPPKIKPKYSEDERVQPLRDLYKESAGTKSSENPE
PDIQEMGFGELRDKLLALDPLDPDHVKRVNAAEAEFWRRSEGYRVGWSDEILGFDCGGQQWVSEVCFPAG
TLAKPSMKDLEFMEELLALIEKEGIPAPAPIEQRWTASSSSPMSPASSPSPDDLHSWVGIIMYLPTEDER
QRKEITEEFFHYRKKTQRNLWDKYSAYEHWAKIEVPKDKEELEALRERLRKRFPVDAFNKARKELDPKGI
LSNNLLEKLFPKS
>gnl|CDD|215259 PLN02466, PLN02466, aldehyde dehydrogenase family 2 member
MAARRISSLLSRSLSASSSALLRSRGRNGGRGRGIRRFSTAAAAVEEPITPPVQVSYTQLLINGQFVDAA
SGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDELA
ALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLL
MFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAF
TGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHER
VYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQP
TVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWV
NCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTPLKNPAWL
>gnl|CDD|215260 PLN02467, PLN02467, betaine aldehyde dehydrogenase
MAIPVPRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRNKGKDWARTT
GAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPM
ETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGV
LNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVE
WAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFIS
TAKSEGATILCGGKRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYG
LAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQVTKYIS
DEPWGWYPPPSKL
>gnl|CDD|178087 PLN02468, PLN02468, putative pectinesterase/pectinesterase inhibitor
FKAYGKVDEAEQARLEARRKTRKRITIISLSSIILVAIVVAAVVGTTASSGNSEKTGNNGKSISTSVKAV
CDVTLYKDSCYETLAPAPKASQLQPEELFKYAVKVAINELSKASQAFSNSEGFLGVKDNMTNAALNACQE
LLDLAIDNLNNSLTSSGGVSVLDNVDDLRTWLSSAGTYQETCIDGLAEPNLKSFGENHLKNSTELTSNSL
AIITWIGKIADSVKLRRRLLTYADDAVPKWLHHEGRKLLQSSDLKKKADIVVAKDGSGKYKTISEALKDV
PEKSEKRTIIYVKKGVYFENVRVEKKKWNVVMVGDGMSKTIVSGSLNFVDGTPTFSTATFAVFGKGFMAR
DMGFRNTAGPIKHQAVALMSSADLSVFYRCTMDAFQDTLYAHAQRQFYRECNIYGTVDFIFGNSAVVFQN
CNILPRRPMKGQQNTITAQGRTDPNQNTGISIQNCTILPLGDLTSVKTFLGRPWKNYSTTVIMHSMMGSL
IDPKGWLPWTGDTAPPTIFYAEFQNFGPGASTKNRVKWKGLKTITNKEASKFTVKPFIDGGKWLPATGVS
FKPGL
>gnl|CDD|178088 PLN02469, PLN02469, hydroxyacylglutathione hydrolase
MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLV
PGIKVYGGSLDNVKGCTHPVENGDKLSLGKDVNILALHTPCHTKGHISYYVTGKEGEDPAVFTGDTLFIA
GCGKFFEGTAEQMYQSLCVTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLP
TVPSTIEEELETNPFMRVDLPEIQEKVGCESPVEALREVRKMKDNWKG
>gnl|CDD|215261 PLN02470, PLN02470, acetolactate synthase
ETFQSRFAPDEPRKGADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGY
AKASGKVGVCIATSGPGATNLVTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYL
VMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDIQQQLAVPNWNQPMKLPGYLSRLPKPPEKSQLEQIVR
LISESKRPVVYVGGGCLNSSEELREFVELTGIPVASTLMGLGAFPASDELSLQMLGMHGTVYANYAVDSA
DLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSVCADVKLALQGLNKLLEERKAKRP
DFSAWRAELDEQKEKFPLSYPTFGDAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWL
TSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQWE
DRFYKANRAHTYLGDPDAEAEIFPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQE
HVLPMIPGGGTFKDIITEGDGRTKY
>gnl|CDD|215262 PLN02471, PLN02471, superoxide dismutase [Mn]
MALRTLASRKTLGGLKETSSRLLSFRGLQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKA
LEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFWKNLAPVSEGGGEPPHGSLGWAIDEHFGSLEALV
KKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGPSLVPLLGIDVWEHAYYLQYKNVRPDYL
KNIWKVMNWKYASEVYEKECN
>gnl|CDD|215263 PLN02472, PLN02472, uncharacterized protein
ATSLARIARRALTSTAAAQLRRGFAAEAAAAATPITPSPDRVKWDYRGQRQIIPLGQWVPKVAVDAYVAP
NVVLAGQVTVWDGASVWNGAVLRGDLNKITVGFCSNVQERCVLHAAWNSPTGLPAETLIDRYVTIGAYSL
LRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFVRTLTNEETLEIPKL
AVAINDLSQSHFSEFLPYSTAYLEVEKLKKSLGIAL
>gnl|CDD|166114 PLN02473, PLN02473, glutathione S-transferase
MVVKVYGQIKAANPQRVLLCFLEKGIEFEVIHVDLDKLEQKKPEHLLRQPFGQVPAIEDGDLKLFESRAI
ARYYATKYADQGTDLLGKTLEHRAIVDQWVEVENNYFYAVALPLVINLVFKPRLGEPCDVALVEELKVKF
DKVLDVYENRLATNRYLGGDEFTLADLTHMPGMRYIMNETSLSGLVTSRENLNRWWNEISARPAWKKLME
LAAY
>gnl|CDD|178092 PLN02474, PLN02474, UTP--glucose-1-phosphate uridylyltransferase
AATADEKLPQLRSAVAGLDQISENEKSGFISLVSRYLSGEAQHIEWSKIQTPTDEVVVPYDKLAPVPEDP
EETKKLLDKLVVLKLNGGLGTTMGCTGPKSVIEVRNGLTFLDLIVIQIENLNKKYGCNVPLLLMNSFNTH
DDTQKIVEKYTNSNIEIHTFNQSQYPRVVADDFVPWPSKGKTDKDGWYPPGHGDVFPSLMNSGKLDALLS
QGKEYVFIANSDNLGAIVDLKILNHLIQNKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHV
NEFKSIEKFKIFNTNNLWVNLKAIKRLVEADALKMEIIPNPKEVDGVKVLQLETAAGAAIRFFDNAIGIN
VPRSRFLPVKATSDLLLVQSDLYTLVDGFVIRNKARTNPSNPSIELGPEFKKVANFLSRFKSIPSIVELD
SLKVSGDVWFGSGIVLKGKVTITAKSGVKLEIPDGAVLENKDINGPEDL
>gnl|CDD|215264 PLN02475, PLN02475, 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLD
TTAMLGAVPPRYGWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNE
YKEAKALGVDTVPVLVGPVSYLLLSKPAKGVDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPAL
VMDLESHKLQAFKTAYAELESTLSGLNVLVETYFADVPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLIKK
AGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGKDKLVVSTSCSLLHTAVDLVNETKLDKELKS
WLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRRSSPRVTNEAVQKAAAALKGSDHRRATPVSAR
LDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQEELDIDVLVHG
EPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT
GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVH
SFRITNCGVQDTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYD
IHSPRIPSTEEIADRINKMLAVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQLASAK
>gnl|CDD|178094 PLN02476, PLN02476, O-methyltransferase
MSTGLALNRCSFSVCRTATTLLNRPTVSVCRSLKFSRRLIGNCSIAPADPVVVANDDKYGNKQVISLTPR
LYDYVLSNVREPKILRQLREETSKMRGSQMQVSPDQAQLLAMLVQILGAERCIEVGVYTGYSSLAVALVL
PESGCLVACERDSNSLEVAKRYYELAGVSHKVNVKHGLAAESLKSMIQNGEGSSYDFAFVDADKRMYQDY
FELLLQLVRVGGVIVMDNVLWHGRVADPLVNDAKTISIRNFNKKLMDDKRVSISMVPIGDGMTICRKR
>gnl|CDD|178095 PLN02477, PLN02477, glutamate dehydrogenase
MNALAATNRNFREAARLLGLDSKLEKSLLIPFREIKVECTIPKDDGTLASFVGFRVQHDNARGPMKGGIR
YHPEVDPDEVNALAQLMTWKTAVANIPYGGAKGGIGCDPRDLSESELERLTRVFTQKIHDLIGIHTDVPA
PDMGTNAQTMAWILDEYSKFHGFSPAVVTGKPIDLGGSLGREAATGRGVVFATEALLAEHGKSIAGQTFV
IQGFGNVGSWAAQLIHEKGGKIVAVSDITGAVKNENGLDIPALRKHVAEGGGLKGFPGGDPIDPDDILVE
PCDVLIPAALGGVINKENAADVKAKFIVEAANHPTDPEADEILRKKGVVVLPDIYANSGGVTVSYFEWVQ
NIQGFMWEEEKVNRELDRYMTDAFKALKEMCKTHNCSLRMGAFTLGVNRVARATVLRGWE
>gnl|CDD|215265 PLN02478, PLN02478, alternative oxidase
GLCNRLVSSASSASHMKSPLFPAAPMRIGDRAPRFGGFRIGSKHAQEEKKLAEEEESSGKATENKDEGST
VKGGQKAIVSYWGIEPAKITKEDGTEWKWNCFRPWETYKADLSIDLKKHHVPKTLLDKIAYWTVKSLRVP
TDLFFQRRYGCRAMMLETVAAVPGMVGGMLLHLKSLRRFEHSGGWIKALLEEAENERMHLMTFMEVAKPK
WYERALVIAVQGVFFNAYFLGYLISPKFAHRIVGYLEEEAIHSYTEFLKDLDAGKIENVPAPAIAIDYWR
LPADATLRDVVTVVRADEAHHRDVNHFASDIHYQGKELKEAPAPIGYH
>gnl|CDD|178097 PLN02479, PLN02479, acetate-CoA ligase
MAKERDIDDLPKNAANYTALTPLWFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPG
STVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAE
KKKSSFKPPLLIVIGDPTCDPKSLQYALGKGAIEYEKFLETGDPEFAWKPPADEWQSIALGYTSGTTASP
KGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAALCGTNICLRQVTAKAIYSAIA
NYGVTHFCAAPVVLNTIVNAPKSETILPLPRVVHVMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETYGPS
TVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDVVDTKTMKPVPADGKTMGEIVMRGNMVMKGYLKNP
KANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDER
WGESPCAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVFGPLPKTATGKIQKHVLRAKAKEMG
PVKKSRL
>gnl|CDD|178098 PLN02480, PLN02480, Probable pectinesterase
MASPMLLPLRMAAVAAVVVSSPSGSKAAKKSQTVVDSPLLTEKIGTNRTIIVDINGKGDFTSVQSAIDAV
PVGNSEWIIVHLRKGVYREKVHIPENKPFIFMRGNGKGRTSIVWSQSSSDNAASATFTVEAPHFVAFGIS
IRNDAPTGMAFTSENQSVAAFVGADKVAFYHCAFYSTHNTLFDYKGRHYYHSCYIQGSIDFIFGRGRSIF
HNCEIFVIADRRVKIYGSITAHNRESEDNSGFVFIKGKVYGIGEVYLGRAKGAYSRVIFAKTYLSKTIVP
AGWTNWSYTGSTENLYQAEYKCHGPGAETTNRVPWSKQLTQEEAESFLSIDFIDGKEWLPVWL
>gnl|CDD|215266 PLN02481, PLN02481, Omega-hydroxypalmitate O-feruloyl transferase
MMGDGKVKSFQLVVKQKEPELVPPAEETPKGLYFLSNLDQNIAVIVRTVYCFKSEERGSNEDPVDVIKKA
LSKVLVHYYPLAGRLTISSEGKLIVDCTGEGVVFVEAEANCSIEEIGDITKPDPETLGKLVYDVPGAKNI
LEIPPLTAQVTRFKCGGFVLGLCMNHCMFDGIGAMEFVNSWGETARGLPLSVPPFLDRSILRARNPPKIE
FPHQEFAEIEDVSGTSKLYDDEELVYKSFCFDPEKLEKLKSMALEDGVIKKCSTFEALTAFVWRARTKAL
KMLPDQQTKLLFAVDGRSRFNPPLPKGYFGNGIVLTNALTTAGELLENPLSHAVGLVQDAIKMVNDGYMR
SAIDYFEVTRARPSLASTLLITTWSRLSFHTTDFGWGEPVLSGPVGLPEKEVILFLSHGKERKSINVLLG
LPASAMKTFQELMEII
>gnl|CDD|178100 PLN02482, PLN02482, glutamate-1-semialdehyde 2,1-aminomutase
MAAALAGSALGLSCSAKPSARRSSSQRRRAVRSSVIKMAVSVEEKKKFTTTKSEEIFKAAKELMPGGVNS
PVRAFKSVGGQPIVFDRVKGSYAWDVDGNEYIDYVGSWGPAIIGHADDEVLAALAETMKKGTSFGAPCLL
ENVLAEMVIDAVPSVEMVRFVNSGTEACMGVLRLARAYTGREKIIKFEGCYHGHADSFLVKAGSGVATLG
LPDSPGVPKAATSATLTAPYNDLEAVKKLFEANKGEIAAVILEPVVGNSGFIVPKKEFLEGLREITKENG
ALLVFDEVMTGFRIAYGGAQEYFGITPDLTTLGKVIGGGLPVGAYGGRREIMEMVAPAGPMYQAGTLSGN
PLAMTAGIHTLKRLQQPGTYEYLDKITKKLIQGILEAGKKAGHEMCGGYISGMFGFFFTEGPVYNFADAK
KSDTAKFARFHRGMLEEGVYLAPSQFEAGFTSLAHTEEDIDFTIAAAERVLARI
>gnl|CDD|178101 PLN02483, PLN02483, serine palmitoyltransferase
MITIPYLTALTTYFSYGLLFAFGQLRDFFRAILDWWKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRP
IASAPDAWFDVVERVSNDNNKTLKRTTKTRRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRV
DGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIR
VFQHNTPSHLEEVLREQIAEGQPRTHRPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHS
IGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQ
VISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNDSPVMPIMLYNPAKIPAFSRECLK
QNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAEPKKQEQVKKFIKLE
>gnl|CDD|178102 PLN02484, PLN02484, probable pectinesterase/pectinesterase inhibitor
MGYGRLGPSGASGPNQTSTATALPELRRRRKTKLVLFSIVLLIVSAVAAAIFAGVRAKASGQTSPKSLHR
KPTQAISKTCSKTRFPNLCVDSLLDFPGSLTASESDLIHISFNMTLQHFSKALYLSSTISYVQMPPRVRS
AYDSCLELLDDSVDALSRALSSVVPSSGGGSPQDVVTWLSAALTNHDTCTEGFDGVNGGEVKDQMTGALK
DLSELVSNCLAIFSASNGGDFSGVPIQNRRRLLTEEEDISFPRWLGRRERELLGMPVSAIQADIIVSKDG
NGTFKTISEAIKKAPEHSSRRTIIYVKAGRYEENNLKVGRKKTNLMFIGDGKGKTVITGGKSIFDNLTTF
HTASFAATGAGFIARDMTFENWAGPAKHQAVALRVGADHAVVYRCNIIGYQDTLYVHSNRQFFRECDIYG
TVDFIFGNAAVVLQNCSIYARKPMAQQKNTITAQNRKDPNQNTGISIHACRILAASDLAASKGSFPTYLG
RPWKLYSRTVYMMSYMGDHIHPRGWLEWNTTFALDTLYYGEYMNYGPGSGVGQRVKWPGYRVITSTVEAS
KFTVAQFIYGSSWLPSTGVSFLAGLSQ
>gnl|CDD|215267 PLN02485, PLN02485, oxidoreductase
MATDFKSIPVIDISPLVAKCDDPDMAEDPDVAEVVRQLDKACRDAGFFYVKGHGISDSLIKKVREVTHEF
FELPYEEKLKIKMTPAAGYRGYQRIGENVTKGKPDMHEAIDCYREFKPGKYGDLGKVMEGPNQWPENPQE
FKALMEEYIKLCTDLSRKILRGIALALGGSPDEFEGKMAGDPFWVMRIIGYPGVSNLNGPPENDIGCGAH
TDYGLLTLVNQDDDITALQVRNLSGEWIWAIPIPGTFVCNIGDMLKIWSNGVYQSTLHRVINNSPKYRVC
VAFFYETNFDAAVEPLDICKEKRTGGSQVFKRVVYGEHLVNKVLTNFAN
>gnl|CDD|178104 PLN02486, PLN02486, aminoacyl-tRNA ligase
QVVTPWEVSAKDGGKIDYDKLVDKFGCQRLDPSLIDRVERLTGRPAHPFLRRGVFFAHRDLEEILDAYEK
GEKFYLYTGRGPSSEALHLGHLIPFMFTKYLQDAFKVPLVIQLTDDEKFLWKNLSVEESQRLARENAKDI
IACGFDVERTFIFSDFDYVGGAFYKNMVKIAKCVTLNQVRGIFGFSGEDNIGKISFPAVQAAPSFPSSFP
HLFGGKDKLRCLIPCAIDQDPYFRMTRDVAPRLGYYKPALIESRFFPALQGESGKMSASDPNSAIYVTDT
PKEIKNKINKYAFSGGQDTVEEHRELGANLEVDIPWKYLNFFLEDDAELERIKKEYGSGRMLTGEVKKRL
IEVLTEIVERHQRARAAVTDEMVDAFMAVRPLP
>gnl|CDD|215268 PLN02487, PLN02487, zeta-carotene desaturase
TAALSGCVLAAATPAKLVTSSSSLRSPVAGAVLRSPLKSARLSVSSSLDSNVSDMSVNAPKGLFPPEPEA
YKGPKLKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVGSFVDKNGNHIEMGLHVFFGCYNNLF
RLMKKVGADENLLVKDHTHTFVNKGGDVGELDFRFPVGAPLHGIKAFLTTNQLEPYDKARNALALATSPV
VRALVDPDGAMRDIRDLDDISFSDWFTSHGGTRMSIKRMWDPIAYALGFIDCDNISARCMLTIFSLFATK
TEASLLRMLKGSPDVRLSGPIAKYITDRGGRFHLRWGCREILYDKSPDGETYVTGLKVSKATEKEIVKAD
AYVAACDVPGIKRLLPEQWREYEFFDNIYKLVGVPVVTVQLRYNGWVTEMQDLELSRQLRRAAGLDNLLY
SADADFSCFADLALTSPEDYYKEGEGSLIQAVLTPGDPYMPLSNDKIVEKVHKQVLELFPSSRGLEVTWS
SVVKIGQSLYREAPGMDPFRPDQKTPISNFFLAGSYTKQDYIDSMEGATLSGRQAAAYICEAGEELAGLR
KKLAAEESA
>gnl|CDD|178106 PLN02488, PLN02488, probable pectinesterase/pectinesterase inhibitor
VIGVCKGYDDKQSCQNLLLELKTVSSSLSEMRCRDLLIIVLKNSVWRIDMAMIGVMEDTKLLEEMENDML
GVKEDTNLFEEMMESAKDRMIRSVEELLGGESPNLGSYENVHTWLSGVLTSYITCIDEIGEGAYKRRVEP
ELEDLISRARVALAIFISISPRDDTELKSVVPNGPSWLSNVDKKYLYLNPEVLKKIADVVVAKDGSGKYN
TVNAAIAAAPEHSRKRFVIYIKTGVYDEIVRIGSTKPNLTLIGDGQDSTIITGNLSASNGKRTFYTATVA
SNGDGFIGIDMCFRNTAGPAKGPAVALRVSGDMSVIYRCRIEGYQDALYPHRDRQFYRECFITGTVDFIC
GNAAAVFQFCQIVARQPMMGQSNVITAQSRESKDDNSGFSIQKCNITASSDLDPVKATVKTYLGRPWRKY
STVAVLQSFIGDLVDPAGWTPWEGETGLSTLYYGEYQNRGPGAVTSKRVKWTGFRVMTDPKEATKFTVAK
LLDGESWLKASGVPYEKGL
>gnl|CDD|215269 PLN02489, PLN02489, homocysteine S-methyltransferase
GGYVLPQMSSLLEDLLRQAGGCAVIDGGFATELERHGADLNDPLWSAKCLITSPHLIRKVHLDYLEAGAD
IIITASYQATIQGFESRGLSREESETLLRKSVEIACEARDIFWDKCQKGSTSRPGRELSYRPILVAASIG
SYGAYLADGSEYSGDYGPSVTLEKLKDFHRRRLQVLAEAGPDLIAFETIPNKLEAQAYVELLEEENIKIP
AWISFNSKDGVNVVSGDSLLECASIADSCKKVVAVGINCTPPRFIHGLILSIRKVTSKPIVVYPNSGETY
DGEAKEWVESTGVSDEDFVSYVNKWRDAGASLIGGCCRTTPNTIRAISKALSERL
>gnl|CDD|215270 PLN02490, PLN02490, MPBQ/MSBQ methyltransferase
MASSMLNGAENLRLIRGITPKGLGFSGSDLHGRSFPKKLLSSSRRSPRLRTLAARCSSSSSRPASQPRFI
QHKKEAFWFYRFLSIVYDHIINPGHWTEDMRDDALEPADLSDRNLKVVDVGGGTGFTTLGIVKHVDAKNV
TILDQSPHQLAKAKQKEPLKECKIIEGDAEDLPFPTDYADRYVSAGSIEYWPDPQRGIKEAYRVLKIGGK
ACLIGPVHPTFWLSRFFADVWMLFPKEEEYIEWFTKAGFKDVKLKRIGPKWYRGVRRHGLIMGCSVTGVK
PASGDSPLQLGPKAEDVSKPVNPFSFLLRFILGTIAATYYVLVPIYMWLKDQIVPKGQPI
>gnl|CDD|215271 PLN02491, PLN02491, carotenoid 9,10(9',10')-cleavage dioxygenase
PEKMQESGVQGGSPVVVVNPRPSKGLTSKAVDLLEKLIVKLMHDASQPLHYLSGNFAPVRDETPPVKDLP
VRGHLPECLNGEFVRVGPNPKFSPVAGYHWFDGDGMIHGMRIKDGKATYVSRYVKTSRLKQEEFFGGAKF
MKIGDLKGLFGLLMVNMQQLRAKLKVLDFSYGNGTGNTALIYHHGKLLALSEADKPYVVKVLEDGDLQTL
GLLDYDKRLKHSFTAHPKVDPFTGEMFTFGYSHEPPYITYRVISKDGAMHDPVPITISEPIMMHDFAITE
NYAIFMDLPLYFRPKEMVKEKKFIYTFDATKKARFGVLPRYAKDELMIRWFELPNCFIFHNANAWEEEDE
VVLITCRLENPDLDMVNGKVKEKLENFGNELYEMRFNMKTGAASQKKLSASAVDFPRVNESYTGRKQRYV
YGTILDSIAKVTGIIKFDLHAEPETGKKKLEVGGNVKGIFDLGPGRFGSEAIFVPREPGTTSEEDDGYLI
FFVHDENTGKSSVNVIDAKTMSADPVAVVELPHRVPYGFHAFFVTEEQLQEQAKL
>gnl|CDD|215272 PLN02492, PLN02492, ribonucleoside-diphosphate reductase
EPLLAENPDRFCMFPIKYPQIWEMYKKAEASFWTAEEVDLSADLKDWEKLTDDERHFISHVLAFFAASDG
IVLENLAARFMKEVQVPEARAFYGFQIAIENIHSEMYSLLLDTYIKDPKEKDRLFNAIETIPCVAKKADW
ALRWIDSSASFAERLVAFACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLL
KNKLSEERVKEIVCEAVEIEKEFVCDALPCALVGMNADLMSQYIEFVADRLLVALGYEKVYNVVNPFDWM
ELISLQGKTNFFEKRVGEYQKAGVMSSLNGGGADNHVFSLDEDF
>gnl|CDD|166134 PLN02493, PLN02493, probable peroxisomal (S)-2-hydroxy-acid oxidase
MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKIS
MPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQL
VRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLGKMDEANDSGLASYVAGQIDRT
LSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRI
PVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEIS
RNHITTEWDTPRPSARL
>gnl|CDD|178111 PLN02494, PLN02494, adenosylhomocysteinase
SSGREYKVKDMSQADFGRLEIELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALG
AEVRWCSCNIFSTQDHAAAAIARDSAAVFAWKGETLQEYWWCTERALDWGPGGGPDLIVDDGGDATLLIH
EGVKAEEEFEKDGTLPDPTSTDNAEFKIVLTIIKDGLKVDPKKYHKMKERLVGVSEETTTGVKRLYQMQK
NGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDGLMRATDVMIAGKVAVICGYGDVGKGCAAAMKAAGARV
IVTEIDPICALQALMEGYQVLTLEDVVSEADIFVTTTGNKDIIMVDHMRKMKNNAIVCNIGHFDNEIDML
GLETYPGVKRITIKPQTDRWVFPDTGSGIIVLAEGRLMNLGCATGHPSFVMSCSFTNQVIAQLELWNEKK
SGKYEKKVYVLPKHLDEKVAALHLGKLGAKLTKLSKDQADYINVPVEGPYKPAHYRY
>gnl|CDD|215273 PLN02495, PLN02495, oxidoreductase, acting on the CH-CH group of donors
SLGLAASEPDLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKVINVTPRYAR
LRAGANGSAKGRVIGWQNIELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETG
VDALEINFSCPHGMPERKMGAAVGQDCDLLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEG
VAAINTIMSVMGINLDTLRPEPCVEGYSTPGGYSSKAVRPIALAKVMAIAKMMKSEFPEDRSLSGIGGVE
TGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSSIEDFRGASLPYFTTHTDLVQRQ
KEAIRQRKAIRKGLASDKDWTGDGFVKETESMVSN
>gnl|CDD|215274 PLN02496, PLN02496, probable phosphopantothenoylcysteine decarboxylase
AEPLSPEVDAMEVNTAPRKPRILLAASGSVAAIKFGNLCHCFSEWAEVRAVVTKASLHFIDRASLPKDVT
LYTDEDEWSSWNKIGDSVLHIELRRWADVMVIAPLSANTLGKIAGGLCDNLLTCIVRAWDYSKPLFVAPA
MNTFMWNNPFTERHLMSIDELGISLIPPVTKRLACGDYGNGAMAEPSLIYSTVRLFLESRAQSQSGGVS
>gnl|CDD|178113 PLN02497, PLN02497, probable pectinesterase
MGTHRIIIGLIALCCFCLPHLIEAKPFGVYQQQVFVDQSGHGNFTTIQSAIDSVPSNNKHWFCINVKAGL
YREKVKIPYDKPFIVLVGAGKRRTRIEWDDHDSTAQSPTFSTLADNTVVKSITFANSYNFPSKGNKNPRV
PAVAAMIGGDKSAFYSCGFAGVQDTLWDSDGRHYFKRCTIQGAVDFIFGSGQSIYESCVIQVLGGQLEPG
LAGFITAQGRTNPYDANGFVFKNCLVYGTGSAYLGRPWRGYSRVLFYNSNLTDVVVPEGWDAWNFVGHEN
QLTFAEHGCFGSGANTSKRVSWVKKLSGSAVQNLTSLSFINREGWVEDQPI
>gnl|CDD|215275 PLN02498, PLN02498, omega-3 fatty acid desaturase
MASWVLSECGLRPLPRIYPRPRTGFISKNNLSKFRFLPSSKSYKRLPFDLFSRGCSRERNWALNVSAPLT
VPSGEEEEDEEGVNGVGEDEEGEFDPGAPPPFNLADIRAAIPKHCWVKNPWRSMSYVVRDVAVVFGLAAA
AAYFNNWVVWPLYWFAQGTMFWALFVLGHDCGHGSFSNNPKLNSVVGHLLHSSILVPYHGWRISHRTHHQ
NHGHVENDESWHPLSEKIYKSLDKVTRTLRFTLPFPMLAYPFYLWSRSPGKKGSHFHPDSDLFVPKERKD
VITSTACWTAMAALLVCLSFVMGPIQMLKLYGIPYWIFVMWLDFVTYLHHHGHEDKLPWYRGKEWSYLRG
GLTTLDRDYGWINNIHHDIGTHVIHHLFPQIPHYHLVEATEAAKPVLGKYYREPKKSGPLPFHLLGSLIR
SMKQDHYVSDTGDVVYYQTDPQLSGSSKEE
>gnl|CDD|178115 PLN02499, PLN02499, glycerol-3-phosphate acyltransferase
MEQSGTTSYSVVSELEGTLLKDADPFSYFMLVAFEASGLIRFALLLFLWPIIRLLDMLGMGDAALKLMIF
VATAGVHESEIESVARAVLPKFYMDDVDMEAWKVFSSCDKRVVVTRMPRVMVERFAKEHLRADEVIGSEL
VVNRFGFATGFIRGTDVDQSVANRVANLFVDERPQLGLGRISASSSFLSLCKEQIHPPFPANYNGDNQQQ
LVRPLPVIFHDGRLVKRPTPATALLILLWIPLGIILAVIRIFVGIMLPMWAIPYVSRIFGGKVIVKGKPP
PPASGGNSGVLFVCTHRTLMDPVVLSTVLGRSIPAVTYSISRLSEILSPIPTVRLTRIRDVDAEKIKREL
ARGDLVVCPEGTTCREPFLLRFSALFAELTDRIVPVAMNYRVGFFHATTARGWKGLDPIFFFMNPRPVYE
VTFLNQLPVEATCSSGKSPHDVANYVQRILAATLGFECTNFTRKDKYRVLAGNDGTVSYLSFLDQLKKVV
STFKPFLH
>gnl|CDD|215276 PLN02500, PLN02500, cytochrome P450 90B1
MAMMMSHTELLLFLLPSILSLLLVFILTKRRPKQKRFNLPPGNMGWPFLGETIGYLKPYSATSIGEFMEQ
HISRYGKIYRSNLFGEPTIVSADAGLNRFILQNEGRLFECSYPRSIGGILGKWSMLVLVGDMHRDMRSIS
LNFLSHARLRTHLLKEVERHTLLVLDSWKENSTFSAQDEAKKFTFNLMAKHIMSMDPGEEETEQLKKEYV
TFMKGVVSAPLNFPGTAYRKALKSRATILKFIERKMEERIEKLKEEDESVEEDDLLGWVLKHSNLSTEQI
LDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIARAKKQSGESELNWEDYKKMEFTQCVI
NETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNNRGGSSG
SSSATTNNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWELAEADQAFAFPFVDFPKGLPIRVRRIL
>gnl|CDD|215277 PLN02501, PLN02501, digalactosyldiacylglycerol synthase
SSLSMTLSSTNAFSFLSKGWREVRDSADADLQLMRARANSFKNLASSFDREIENFFNSASRSSFPVGSPS
ASSFPTEIDFVKKLQPKISEFRRVYSAPEISRKVLEKWGPRAKLGIDLSAIKNAIVAEMELDDRGGIVEF
DRVRRRRNSRVRFTEFWGEAKEEGEGQFGEWEPIRALKTRFRELEKRSESLEIFGGFKNSEFVEKLKSSL
KAIYKEPQESKDVPPLDVPELLAYLVRQSEPFLDQLGVRKDICDKIVESLCSKRKNQLLLRSLSAGESSL
LESDNHNDELDLRIASVLQSTGHCYDGGFWTDSSKHELSDGKRHVAIVTTASLPWMTGTAVNPLFRAAYL
AKSAKQNVTLLVPWLCKSDQELVYPNNLTFSSPEEQESYIRNWLEERIGFKADFKISFYPGKFSKERRSI
IPAGDTSQFIPSKDADIAILEEPEHLNWYHHGKRWTDKFNHVVGVVHTNYLEYIKREKNGALQAFFVKHI
NNWVTRAYCHKVLRLSAATQDLPKSVICNVHGVNPKFLKIGEKVAEERELGQQAFSKGAYFLGKMVWAKG
YRELIDLLAKHKNELDGFNLDVFGNGEDAHEVQRAAKRLDLNLNFLKGRDHADDSLHGYKVFINPSISDV
LCTATAEALAMGKFVVCADHPSNEFFRSFPNCLTYKTSEDFVAKVKEALANEPQPLTPEQRYNLSWEAAT
QRFMEYSDLDKVLNNGDDAKLSKSGGKSITKSVSMPNLSEMVDGGLAFAHYCLTGNEFLRLCTGAIPGTR
DYDKQHCKDLHLLPPHVENPIYGW
>gnl|CDD|215278 PLN02502, PLN02502, lysyl-tRNA synthetase
AESNGEPLSKNALKKRLKAKQAEEEKAAKEEAKAAAAAAAAKGRSRKSAAADDETMDPTQYRANRLKKVE
ALRAKGVEPYPYKFDVTHTAPELQEKYGSLENGEELEDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQL
YADKKRLDLDEEEFEKLHSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQET
RYRQRYLDLIANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLY
LRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKEL
TGSYKIKYHGIEIDFTPPFRRISMISLVEEATGIDFPADLKSDEANAYLIAACEKFDVKCPPPQTTGRLL
NELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERFELFINGRELANAFSELTDPVDQRERFEE
QVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFPAMKPQD
>gnl|CDD|215279 PLN02503, PLN02503, fatty acyl-CoA reductase 2
MGSLFLSSPSVASNKLIRVSSKCDWSTLRLKKRVVPVFCQGGGGGDGIRSSGLSSVLAERSRVGSSQQHV
AACRDAGSLVLSPNGKGQPEIAVKDLVPYGSSSAVEMADGIGIAEFLRGKNFLITGATGFLAKVLIEKIL
RTNPDVGKIYLLIKAKDKEAAIERLKNEVIDAELFKCLQETHGKSYQSFMLSKLVPVVGNVCESNLGLEP
DLADEIAKEVDVIINSAANTTFDERYDVAIDINTRGPCHLMSFAKKCKKLKLFLQVSTAYVNGQRQGRIM
EKPFRMGDCIARELGISNSLPHNRPALDIEAEIKLALDSKRHGFQSNSFAQKMKDLGLERAKLYGWQDTY
VFTKAMGEMVINSMRGDIPVVIIRPSVIESTWKDPFPGWMEGNRMMDPIVLYYGKGQLTGFLADPNGVLD
VVPADMVVNATLAAMAKHGGAAKPEINVYQIASSVVNPLVFQDLARLLYEHYKSSPYMDSKGRPIHVPPM
KLFSSMEDFSSHLWRDALLRSGLAGMSSSDRKLSQKLENICAKSVEQAKYLASIYEPYTFYGGRFDNSNT
QRLMERMSEEEKAEFGFDVGSIDWRDYITNVHIPGLRRHVMKGRG
>gnl|CDD|178120 PLN02504, PLN02504, nitrilase
MSSTADMPAVEPEVDMGADASSSTVRATVVQASTVFYDTPATLDKAERLIAEAAAYGSQLVVFPEAFIGG
YPRGSTFGLAIGDRSPKGREDFRKYHASAIDVPGPEVDRLAAMAGKYKVYLVMGVIERDGYTLYCTVLFF
DPQGQYLGKHRKLMPTALERLIWGFGDGSTIPVYDTPIGKIGAVICWENRMPLLRTAMYAKGIEIYCAPT
ADSRETWQASMRHIALEGGCFVLSANQFCRRKDYPPPPEYLFSGTEEDLTPDSIVCAGGSVIISPSGTVL
AGPNYEGEGLITADLDLGEIARAKFDFDVVGHYSRPDVLSLTVNEHPLKPVTFTSSPEKAEDDSEK
>gnl|CDD|178121 PLN02505, PLN02505, omega-6 fatty acid desaturase
MGAGGRMSVPTSSKKGSASAVKRVPSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLYYVA
TNYIPLLPGPLSYVAWPLYWAAQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYS
HRRHHSNTGSLERDEVFVPKKKSALPWYSKYLNNPPGRLLHIVVQLTLGWPLYLAFNVSGRPYDRFACHF
DPYSPIFNDRERLQIYISDAGILAVSFGLYRLAAAKGLAWVLCVYGVPLLIVNAFLVLITYLQHTHPALP
HYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHHLFSTMPHYHAMEATKAIKPILGEYYQFDGTP
VYKALWREAKECIYVEPDEGGKGVFWYNNKF
>gnl|CDD|215280 PLN02506, PLN02506, putative pectinesterase/pectinesterase inhibitor
MGFANFLLILMLLPVHLESLETTSSSPYQELNFQALIAQACQFVENHSSCVSNIQAELKKSGPRTPHSVL
SAALKATLDEARLAIDMITKFNALSISYREQVAIEDCKELLDFSVSELAWSLLEMNKIRAGHDNVAYEGN
LKAWLSAALSNQDTCLEGFEGTDRHLENFIKGSLKQVTQLISNVLAMYTQLHSLPFKPSRNETETAPSSK
FPEWMTEGDQELLKHDPLGMHVDTIVALDGSGHYRTITEAINEAPNHSNRRYIIYVKKGVYKENIDMKKK
KTNIMLVGDGIGQTVVTGNRNFMQGWTTFRTATVAVSGRGFIARDITFRNTAGPQNHQAVALRVDSDQSA
FYRCSMEGYQDTLYAHSLRQFYRECEIYGTIDFIFGNGAAVLQNCKIYTRVPLPLQKVTITAQGRKSPHQ
STGFSIQDSYVLATQPTYLGRPWKQYSRTVFMNTYMSQLVQPRGWLEWYGNFALGTLWYGEYRNYGPGAL
LSGRVKWPGYHIIQDKRTAKFFTVGQFIDGRSWLPSTGVKFTAGLAN
>gnl|CDD|215281 PLN02507, PLN02507, glutathione reductase
MARKMLIDGEVAKVNADEANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICELPFHPISSESIGGVG
GTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVK
LYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQRPNIPGKELAITSDEALSLEELPKRAVVLG
GGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVI
TDHGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDVTNRINLTPVAL
MEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKGDILVFTSSFNPMKNTISGRQE
KTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTMRSVTRRVT
AKGKPKTNL
>gnl|CDD|178124 PLN02508, PLN02508, magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase
MRKGIKEAIKETLLTPRFYTTDFDEMEQLFNTEINKNLDMAEFEALLQEFKTDYNQTHFVRNEEFKAAAD
KIQGPLRQIFIEFLERSCTAEFSGFLLYKELGRRLKKTNPVVAEIFTLMSRDEARHAGFLNKALSDFNLA
LDLGFLTKNRKYTFFKPKFIFYATYLSEKIGYWRYITIYRHLQANPDYQLYPIFKYFENWCQDENRHGDF
FSALLKAQPQFLNDWKAKLWSRFFCLSVYVTMYLNDHQRTAFYEGIGLNTKQFNMHVIIETNRTTARIFP
AVLDVENPEFKRKLDRMVVINQKLVAIGESNDPSFVKNLKRIPLIARLASEILAAYLMPPVESGSVDFAE
FEPQLVY
>gnl|CDD|178125 PLN02509, PLN02509, cystathionine beta-lyase
MTSSLSLHSSFVPSFADLSDRGLVSKNSPTSVSISKVPTWEKKQISNRNSFKLNCVMEKSVDVSTSAVVD
GVADCLNEMNIKEEASVSTLLVNLDNKFDPFDAMSTPLYQTATFKQPSAIENGPYDYTRSGNPTRDALES
LLAKLDKADRAFCFTSGMAALSAVTHLIKNGEEIVAGDDVYGGSDRLLSQVVPRSGVVVKRVNTTNLDEV
AAAIGPQTKLVWLESPTNPRQQISDIRKIAEMAHAQGALVLVDNSIMSPVLSRPLELGADIVMHSATKFI
AGHSDVMAGVLAVKGEKLAKEVYFLQNSEGSGLAPFDCWLCLRGIKTMALRIEKQQENARKIAMYLSSHP
RVKKVYYAGLPDHPGHHLHFSQAKGAGSVFSFITGSVALSKHLVETTKYFSIAVSFGSVKSLISMPCFMS
HASIPAEVREARGLTEDLVRISAGIEDVDDLISDLDIAFRTGPL
>gnl|CDD|178126 PLN02510, PLN02510, probable 1-acyl-sn-glycerol-3-phosphate acyltransferase
LESDSGPKHRPLTPLRRLRGLICLLVLLSTAFMMLVYLAPVSAVLLRLFSVHYSRKATSFFFGSWLALWP
FLFEKINKTKVVFSGDKVPPEERVLLIANHRTEVDWMYLWDLALRKGCLGYIKYVLKSSLMKLPVFGWAF
HIFEFIPVERKWEVDEPNIRQMLSSFKDPRDPLWLALFPEGTDYTEAKCQRSQKFAAEHGLPILNNVLLP
KTKGFVSCLQELRCSLDAVYDVTIGYKHRCPSFLDNVFGIDPSEVHIHIRRIPLKQIPTSEDEVSAWLMD
RFQLKDQLLSDFYAQGHFPNEGTEGELSTLKCLANFLAVIALTTVFTYLTLFSSVWFKIYVSLSCAYLTS
ATHFNWRPPPLIESLENSLKLVNK
>gnl|CDD|215282 PLN02511, PLN02511, hydrolase
TSRAHFSVAAILAPGQTREHSSLEVIGGGRDSFLPKFKSLERPYDAFPLLGNRHVETIFASFFRSLPAVR
YRRECLRTPDGGAVALDWVSGDDRALPADAPVLILLPGLTGGSDDSYVRHMLLRARSKGWRVVVFNSRGC
ADSPVTTPQFYSASFTGDLRQVVDHVAGRYPSANLYAAGWSLGANILVNYLGEEGENCPLSGAVSLCNPF
DLVIADEDFHKGFNNVYDKALAKALRKIFAKHALLFEGLGGEYNIPLVANAKTVRDFDDGLTRVSFGFKS
VDAYYSNSSSSDSIKHVRVPLLCIQAANDPIAPARGIPREDIKANPNCLLIVTPSGGHLGWVAGPEAPFG
APWTDPVVMEFLEALEEGKSSTPAFNSSDEQVGRSVDG
>gnl|CDD|178128 PLN02512, PLN02512, acetylglutamate kinase
MNLFRAGLTIAATSSASAATAANAASTNLSRVDILSEALPFIQRFRGKTVVVKYGGAAMKDPELKAGVIR
DLVLLSCVGLRPVLVHGGGPEINSWLKKVGIEPQFKNGLRVTDAETMEVVEMVLVGKVNKSLVSLINKAG
GTAVGLSGKDGRLLRARPSPNSADLGFVGEVTRVDPTVLRPLVDDGHIPVIATVAADEDGQAYNINADTA
AGEIAAALGAEKLILLTDVAGVLEDKDDPGSLVKELDIKGVRKLIADGKIAGGMIPKVECCVRSLAQGVK
TAHIIDGRVPHSLLLEILTDEGAGTMITG
>gnl|CDD|178129 PLN02513, PLN02513, adenylosuccinate synthase
LSQVSAVLGTQWGDEGKGKLVDILAQHFDIVARCQGGANAGHTIYNDEGKKFALHLVPSGILNEKTTCVI
GNGVVVHLPGLFEEIDGLESNGVSCEGRLLVSDRAHLLFDFHQEVDGLREAELAGSKIGTTKRGIGPAYS
SKATRNGLRVGDLRHMDTFAEKLRELLADAAARFEGFEYDASMVEEEVEAYKKFAERLEPFITDTVHYLN
EAIQAGKKILVEGAQATMLDIDFGTYPFVTSSNPSAGGICTGLGIAPRKLGDIIGVVKAYTTRVGSGPFP
TELFGELGDLLREAGQEFGTTTGRPRRCGWLDIVALKYSCQINGFTSLNLTKLDVLSGLPEIKIGVAYKT
PDGKVVKSFPADLDTLEQVEVVYEVLPGWQEDISSVRNYDDLPAAAQAYVERIEELVGVPVHYIGVGPGR
DALIVKP
>gnl|CDD|166155 PLN02514, PLN02514, cinnamyl-alcohol dehydrogenase
MGSLEAEKKTTGWAARDPSGHLSPYTYTLRKTGPEDVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHE
VVGEVVEVGSDVSKFTVGDIVGVGVIVGCCGECSPCKSDLEQYCNKRIWSYNDVYTDGKPTQGGFASAMV
VDQKFVVKIPEGMAPEQAAPLLCAGVTVYSPLSHFGLKQSGLRGGILGLGGVGHMGVKIAKAMGHHVTVI
SSSDKKREEALEHLGADDYLVSSDAAEMQEAADSLDYIIDTVPVFHPLEPYLSLLKLDGKLILMGVINTP
LQFVTPMLMLGRKVITGSFIGSMKETEEMLEFCKEKGLTSMIEVVKMDYVNTAFERLEKNDVRYRFVVDV
AGSNLDA
>gnl|CDD|178130 PLN02515, PLN02515, naringenin,2-oxoglutarate 3-dioxygenase
MAPGTLTALAGESTLQSSFVRDEDERPKVAYNQFSDEIPVISLAGIDEVGGRRGEICRKIVEACEDWGIF
QVVDHGVDANLVADMTRLARDFFALPAEEKLRFDMSGGKKGGFIVSSHLQGEAVQDWREIVTYFSYPVRT
RDYSRWPDKPEGWRAVTEEYSEKLMGLACKLLEVLSEAMGLEKEALTKACVDMDQKVVVNYYPKCPQPDL
TLGLKRHTDPGTITLLLQDQVGGLQATRDGGKTWITVQPVEGAFVVNLGDHGHYLSNGRFKNADHQAVVN
SNCSRLSIATFQNPAPDATVYPLKVREGEKPILEEPITFAEMYRRKMSRDLELARLKKLAKEEDQQKEVP
KPIDQILA
>gnl|CDD|178131 PLN02516, PLN02516, methylenetetrahydrofolate dehydrogenase (NADP+)
MASPSDHVAQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIK
SFDVDLPENISEAELISKVHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMK
GREPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVRE
ADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSDPSKKSGYRLVGDVDFAEVSKVAGWITPVPGGVGPM
TVAMLLKNTVDGAKRVFAQ
>gnl|CDD|178132 PLN02517, PLN02517, phosphatidylcholine-sterol O-acyltransferase
SSKSKKPKKREKKKWSCVDSCCWFIGYICTAWWLLLFLYNAMPASFPQYVTEAITGPLPDPPGVKLRKEG
LTAKHPVVFVPGIVTGGLELWEGHQCAEGLFRKRLWGGTFGEVYKRPLCWVEHMSLDNETGLDPPGIRVR
AVSGLVAADYFAPGYFVWAVLIANLARIGYEEKNMYMAAYDWRLSFQNTEVRDQTLSRLKSNIELMVATN
GGKKVVVVPHSMGVLYFLHFMKWVEAPAPMGGGGGPGWCAKHIKAVMNIGGPFLGVPKAVSGLFSAEAKD
IAVARAIAPGVLDSDLFGLQTLQHVMRMTRTWDSTMSMLPKGGETIWGDLDWSPEEGYNCDGKKQKNNDT
QLANQDNGNSDVKQKEPVNYGRIISFGKDVAEAPSSQIERIDFKDAVKGNSVASNTSCGDVWTEYHEMGR
EGIKAVAEYKVYTAGSVLDLLRFVAPKMMQRGDAHFSYGIADNLDDPKYQHYKYWSNPLETKLPNAPEME
IYSLYGVGIPTERSYVYKLSPSDECSIPFQIDTSADGGDEDSCLKGGVYFVDGDETVPVLSAGFMCAKGW
RGKTRFNPSGIRTYIREYQHSPPANLLEGRGTQSGAHVDIMGNFALIEDVLRVAAGATGEELGGDRVYSD
IFKWSEKINLKL
>gnl|CDD|215283 PLN02518, PLN02518, pheophorbide a oxygenase
MAVLLGIACNSLTLTSSTPKSTPFFIPARTIPFVSSSRPRRGKIFTPLRVAAPPSVPSEAALQQDEGEEQ
RVEQELGQESSDSKFSWRDHWYPVSLVEDLDPSVPTPFQLLGRDLVLWKDPNQGEWVAFDDKCPHRLAPL
SEGRIDENGHLQCSYHGWSFDGCGSCTRIPQAAPEGPEARAVKSPRACAIKFPTMVSQGLLFVWPDENGW
ERAQATKPPMLPDEFDDPEFSTVTIQRDLFYGYDTLMENVSDPSHIDFAHHKVTGRRDRAKPLPFKVESS
GPWGFAGANSDNPRITAKFVAPCYYINKIEIDTKLPIVGDQKWVIWICSFNVPMAPGKTRSIVCSARNFF
QFSMPGPAWWQLVPRWYEHWTSNKVYDGDMIVLQGQEKIFLSKSGEGSADVNAQYTKLTFTPTQADRFVL
AFRNWLRRHGNSQPEWFGETSSQQPLPSTVLSKRQMLDRFEQHTLNCSSCKGAYKAFQTLQKVLIGATVV
FAATAGIPSDVQLRLILAGLALISAASAYALKELEKNFVFVDYVHAEID
>gnl|CDD|215284 PLN02519, PLN02519, isovaleryl-CoA dehydrogenase
MLLSAAKARRRGLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVNLWKLMGD
FNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISG
EHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSKGITAFIIE
KGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQAC
LDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERA
TQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKEE
>gnl|CDD|178135 PLN02520, PLN02520, bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
TVSTASLASDDLQGSGGVRRNPTLICVPIMADSVDKMLIEMAKAKELGADLVEIRLDFLKNFNPREDLKT
LIKQSPLPTLVTYRPKWEGGQYEGDENKRQDALRLAMELGADYVDVELKVAHEFINSISGKKPEKCKVIV
SSHNYENTPSVEELGNLVARIQATGADIVKIATTALDITDVARMFQITVHSQVPTIGLVMGERGLISRIL
CPKFGGYLTFGTLEAGKVSAPGQPTIKDLLDLYNFRQIGPDTKVYGIIGKPVGHSKSPILHNEAFKSVGF
NGVYVHLLVDDLAKFLQTYSSPDFAGFSCTIPHKEDALKCCDEVDPIAKSIGAINTIIRRPSDGKLVGYN
TDYIGAISAIEDGLRASGSSPASGSPLAGKLFVVIGAGGAGKALAYGAKEKGARVVIANRTYERAKELAD
AVGGQALTLADLENFHPEEGMILANTTSVGMQPNVDETPISKHALKHYSLVFDAVYTPKITRLLREAEES
GAIIVSGTEMFIRQAYEQFERFTGLPAPKELFREIMSKY
>gnl|CDD|215285 PLN02521, PLN02521, galactokinase
MAKHEEEPVPVFSSLEPVYGDGSLLEEARLRYARLKAAFVEVYGAKPDLFARSPGRVNLIGEHIDYEGYS
VLPMAIRQDTIVAIRRAEGSKKLRIANVNDKYTTCTFPADPDQEVDLANHKWGNYFICGYKGVFEFLKSK
GVDVGPPVGLDVVVDGTVPTGSGLSSSAALVCSAAIAIMAALGLNFTKKEVAQFTCKCERHIGTQSGGMD
QAISIMAQQGVAKLIDFNPVRATDVQLPAGGTFVIANSLAESNKAVTAATNYNNRVVECRLAAIVLAVKL
GMSAEEAISKVKTLSDVEGLCVSFAGSHGSSDPAVAVKELLHEGPYTAEEIEEILGESLTSIFKNSPTSL
AVLKAAKHFKLHQRAVHVYSEAKRVHAFRDTVSSSLSEEEKLKKLGDLMNESHYSCSVLYECSCPELEEL
VKVCRDNGALGARLTGAGWGGCAVALVKEAIVPQFILALKEKFYKSRIEKGVIKEEDLGLYVFASKPSSG
AAILKFI
>gnl|CDD|178137 PLN02522, PLN02522, ATP citrate (pro-S)-lyase
MATGQLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINPGSEGFQKLFFGQEEIAIPVHGSIE
AACKAHPTADVFINFASFRSAAASSMEALKQPTIRVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVG
GIQAGAFKIGDTAGTLDNIIQCKLYRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTL
SDHVLRFNNIPQIKMIVVLGELGGRDEYSLVEALKQGKVSKPVVAWVSGTCARLFKSEVQFGHAGAKSGG
DMESAQAKNKALKDAGAIVPTSFEALEAAIKETFEKLVEEGKIIPVKEVTPPQIPEDLNSAIKSGKVRAP
THIVSTISDDRGEEPCYAGVPMSSIIEKDYGVGDVISLLWFKRSLPRYCTKFIEMCIMLCADHGPCVSGA
HNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKGIRVPGIGHRI
KSRDNRDKRVELLQKYARTHFPSVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQE
IDEIVEIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYTK
>gnl|CDD|215286 PLN02523, PLN02523, galacturonosyltransferase
MAVAHRGGRGGGGPGGLRSFFSYRILASAIFLFLFLATTSVLLNTSPHPPHHDHLLPSSGNAYGQRTFLA
LKSDPLKTRLDQIRKQADDHRTLVNAYAAYARKLKLDNSKLLRLFADLSRNFTDLISKPSYRALLSSDGS
AIDEDVLRQFEKEVKERVKVARQMIAESKESFDNQLKIQKLKDTIFAVNEQLTKAKKNGAFASLIAAKSI
PKSLHCLAMRLMEERIAHPEKYKDEGKPPPPELEDPSLYHYAIFSDNVIAASVVVNSAVKNAKEPWKHVF
HVVTDRMNLAAMKVMFKMRDLNGAHVEVKAVEDYKFLNSSYVPVLRQLESANLQKFYFENKLENATKDSS
NMKFRNPKYLSMLNHLRFYLPEMYPKLHRILFLDDDVVVQKDLTGLWKIDMDGKVNGAVETCFGSFHRYA
QYLNFSHPLIKEKFNPKACAWAYGMNIFDLDAWRREKCTEQYHYWQNLNENRTLWKLGTLPPGLITFYST
TKPLDKSWHVLGLGYNPSISMDEIRNAAVIHFNGNMKPWLDIAMNQFKPLWTKYVDYDMEFVQACNFGL
>gnl|CDD|215287 PLN02524, PLN02524, S-adenosylmethionine decarboxylase
MPVSAIGFEGFEKRLEITFFEPPVFADPNGRGLRALTRSQLDEILRPAECTIVSSLSNDQFDSYVLSESS
LFVYPYKIIIKTCGTTKLLLSIPPLLELAARLSLSVRSVKYTRGSFIFPGAQPFPHRSFSEEVSVLDGHF
GKLGLGGKAYVMGDPDKGQKWHVYSASAHNSSNSNEPVYTLEMCMTGLDREKASVFFKDSSLSSAEEMTK
ASGIRKILPESEICDFAFDPCGYSMNGIEGDAISTIHVTPEDGFSYASFEAMGYDPGDLDLSQLVERVLA
CFKPKEFSVAVHANVGGEAGSWGCSLDPDGYSCKGRSCQELPGGGSVVYQTFTATGGCGSPRSTLKWSEN
ESCES
>gnl|CDD|215288 PLN02525, PLN02525, phosphatidic acid phosphatase family protein
MEGIPPWFFSGLSCVVSVPFYTAFLPLLFWSGHGKLARQMTLLMAFCDYVGNCIKDVVSAPRPSCPPVRR
VTATKDEEENAMEYGLPSSHTLNTVCLSGYLLHYVLSYLQNVDASVIFAGLALFCLLVALVGFGRLYLGM
HSPIDIIAGLAIGLVILAFWLTVDEYVDAFITSGQNVTPFWAALSFLLLFAYPTPEFPTPSFEYHTAFNG
VAFGIVAGVQQTYSQFHHEAAPRIFSPQLPIAAFLGRVAVGIPTILAVKFCSKALAKWLLPVVCNALGIP
IRSTSYVPSLKGSVSGKKSDEPKQSVGYLQKLCFFSSQDSFDVDTGIRFLQYAGLAWSVVDLVPSIFSYL
NL
>gnl|CDD|178141 PLN02526, PLN02526, acyl-coenzyme A oxidase
DVSVAFPQATPASIFPPSVSDYYQFDDLLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLG
SLGIAGGTIKGYGCPGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQL
DTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARNTTTNQINGFIVKKGA
PGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQDTNKVLAVSRVMVAWQPIGISMGVYDMC
HRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWITKKARETV
ALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIASFKPAASTRSRL
>gnl|CDD|178142 PLN02527, PLN02527, aspartate carbamoyltransferase
SDVIEAQQFDREMLELLFEVAREMEKVERGSPGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLT
TENAGEFSSAAKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATAEIPVINAGDGPGQHPTQALLDVY
TIQREIGRLDGIKVGLVGDLANGRTVRSLAYLLAKYEDVKIYFVAPDVVKMKDDIKDYLTSKGVEWEESS
DLMEVASKCDVLYQTRIQRERFGERIDLYEAARGKYIVDKKVMDVLPKHAVVMHPLPRLDEITTDVDSDP
RAAYFRQAKNGLFIRMALLKLLLGGW
>gnl|CDD|215289 PLN02528, PLN02528, 2-oxoisovalerate dehydrogenase E2 component
VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLL
KIMVEDSQHLRSDSLLLPTDSSNIVSLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVL
KEDVLKYAAQKGVVKDSSSAEEATIAEQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHF
HYVEEINVDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGV
AMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLP
EVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHMR
>gnl|CDD|178144 PLN02529, PLN02529, lysine-specific histone demethylase 1
MDTPGQDGTAPKRSLRKKAGLKNYDENLMDELIEKHLGGSFKKKNRTKQDLEKETETEAMIALSVGFPID
ALLEEEIRAGVVRELGGKEQNDYIVVRNHILARWRSNVGIWLSKGQIKETVSSEYEHLISAAYDFLLYNG
YINFGVSPSFASPIPEEGTEGSVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTQKMGRKGQF
AAVDLGGSVITGIHANPLGVLARQLSIPLHKVRDNCPLYKPDGALVDKEIDSNIEFIFNKLLDKVTELRQ
IMGGFANDISLGSVLERLRQLYGVARSTEERQLLDWHLANLEYANAGCLSDLSAAYWDQDDPYEMGGDHC
FLAGGNWRLINALCEGVPIFYGKTVDTIKYGNDGVEVIAGSQVFQADMVLCTVPLGVLKKRTIRFEPELP
RRKLAAIDRLGFGLLNKVAMVFPSVFWGEELDTFGCLNESSNKRGEFFLFYGYHTVSGGPALVALVAGEA
AQRFENTDPSTLLHRVLSVLRGIYNPKGINVPDPIQTICTRWGSDPLSYGSYSHVRVQSSGSDYDILAES
VSGRLFFAGEATTRQYPATMHGAFLSGLREASRILHVARSQQSNSRKSMQRNSGVSNDVLIDLFKRPDLA
FGKFSFIFNPLTEDPKSMGIMRVTFDNSGDDLNLPLQLYTVLSREQAHKLQLDEGSNESKLSCLMKNLGL
KLMGPSSLVNTGGSLISTIANARRGRGRNRVVAGQCFI
>gnl|CDD|178145 PLN02530, PLN02530, histidine-tRNA ligase
TAIASSATRVSASAIRRPSLPLSSRCSFLLSASSPRGGRCAASAAAGGGRSGGTTAPPSVQEDGKPKIDV
NPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEITDQLYNFEDKGGRRV
ALRPELTPSLARLVLQKGKSLSLPLKWFAIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAI
VTFFKRVGITSSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKELDTLGVSEEAI
EGILDVLSLKSLDDLEALLGADSEAVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGFDRAG
KLRAICGGGRYDRLLSTFGGEDTPACGFGFGDAVIVELLKEKGLLPELPHQVDDVVFALDEDLQGAAAGV
ASRLREKGRSVDLVLEPKKLKWVFKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDELE
>gnl|CDD|215290 PLN02531, PLN02531, GTP cyclohydrolase I
MGALDEGHFNLELDNGVKLDCLELGFEDQPETLAIESAVKVLLQGLGEDVNREGLKKTPLRVAKALREAT
RGYKQSAKDIVGGALFPEAGLDDGVGHGGGCGGLVVVRDLDLFSYCESCLLPFQVKCHIGYVPSGQRVVG
LSKLSRVAEVFAKRLQDPQRLADEICSALHHGIKPAGVAVVLECSHIHFPNESLGSLDLSSHQGWVKASV
CSGSGVFEDESGNLWEEFVSLLQFRGINVDKRCRKDSSSPCWCPSQDSSSASPEPNPAMVSAVESILRSL
GEDPLRKELVLTPSRFVRWLLNSTQGSRMGRNLEMKLNGFACEKMDPLHANLNEKTMHTELNLPFWSQCE
HHLLPFYGVVHVGYFCAEGGRGNRNPISRSLLQSIVHFYGFRLQVQERLTRQIAETVSSLLGGDVMVVVE
ASHTCMISRGVEKFGSSTATIAVLGRFSSDAKARAMFLQSIATTNSSGT
>gnl|CDD|215291 PLN02532, PLN02532, asparagine-tRNA synthetase
KSSTGKTHQSSHEGDTTASPITPSKYSNRVVLKTILGRSDGGAGLVGKRVVVGGWVKSAKEVKKEPAPPP
PPQSPSSAGDQSPGHKDVRCTEILQSRVPIFRSIAKVLSGGGSTYPVREKTEIAIQKSAPPPPSVAYLLI
SDGSCVASLQVVVDSALAPLTQLMATGTCILAEGVLKLPLPAQGKHVIELEVEKILHIGTVDPEKYPLSK
KRLPLDMLRDFSHFRPRTTTVASVTRVRSALTHATHTFFQDHGFLYVQVPIITTTDATGFGEMFRVTTLL
GKSDDKEEKKPVHETEGISLEAVKAAIKEKTNLVEELKRSESNREALVAAEQDLRKTNQLASQLEAKEKL
KTGTSVKADKLSFSKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEM
AFSELEDAMNCAEDYFKFLCKWVLENCSEDMKFVSKRIDKTISTRLEAIISSSLQRISYTEAVDLLKQAT
DKKFETKPEWGIALTTEHLSYLADEIYKKPVIIYNYPKELKPFYVRLNDDGKTVAAFDLVVPKVGTVITG
SQNEERMDILNARIEELGLPREQYEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRSWGK
ANN
>gnl|CDD|215292 PLN02533, PLN02533, probable purple acid phosphatase
MVKVLGLVAILLIVLAGNVLSYDRPGTRKNLVIHPDNEDDPTHPDQVHISLVGPDKMRISWITQDSIPPS
VVYGTVSGKYEGSANGTSSSYHYLLIYRSGQINDVVIGPLKPNTVYYYKCGGPSSTQEFSFRTPPSKFPI
KFAVSGDLGTSEWTKSTLEHVSKWDYDVFILPGDLSYANFYQPLWDTFGRLVQPLASQRPWMVTHGNHEL
EKIPILHPEKFTAYNARWRMPFEESGSTSNLYYSFNVYGVHIIMLGSYTDFEPGSEQYQWLENNLKKIDR
KTTPWVVAVVHAPWYNSNEAHQGEKESVGMKESMETLLYKARVDLVFAGHVHAYERFDRVYQGKTDKCGP
VYITIGDGGNREGLATKYIDPKPDISLFREASFGHGQLNVVDANTMEWTWHRNDDDQSVASDSVWLKSLL
TEPGCNI
>gnl|CDD|215293 PLN02534, PLN02534, UDP-glycosyltransferase
KAVSKAKQLHFVLIPLMAQGHMIPMIDMARLLAERGVIVSLVTTPQNASRFAKTIDRARESGLPIRLVQI
PFPCKEVGLPIGCENLDTLPSRDLLRKFYDAVDKLQQPLERFLEQAKPPPSCIISDKCLSWTSKTAQRFN
IPRIVFHGMCCFSLLSSHNIRLHNAHLSVSSDSEPFVVPGMPQSIEITRAQLPGAFVSLPDLDDVRNKMR
EAESTAFGVVVNSFNELEHGCAEAYEKAIKKKVWCVGPVSLCNKRNLDKFERGNKASIDETQCLEWLDSM
KPRSVIYACLGSLCRLVPSQLIELGLGLEASKKPFIWVIKTGEKHSELEEWLVKENFEERIKGRGLLIKG
WAPQVLILSHPAIGGFLTHCGWNSTIEGICSGVPMITWPLFAEQFLNEKLIVEVLRIGVRVGVEVPVRWG
DEERVGVLVKKDEVEKAVKTLMDDGGEEGERRRRRAQELGVMARKAMELGGSSHINLSILIQDVLKQQSL
Q
>gnl|CDD|215294 PLN02535, PLN02535, glycolate oxidase
MADEIVNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYT
ISAPIMIAPTAMHKLAHPEGEIATARAAAACNTIMVLSFMASCTVEEVASSCNAVRFLQLYVYKRRDIAA
QLVQRAEKNGYKAIVLTADVPRLGRREADIKNKMISPQLKNFEGLLSTEVVSDKGSGLEAFASETFDASL
SWKDIEWLRSITNLPILIKGVLTREDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVP
VLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITR
SHVRTERERLQSML
>gnl|CDD|178151 PLN02536, PLN02536, diaminopimelate epimerase
VDNRDSSEPKLTPEQAVKLCDRNFGIGADGVIFAMPGVNGTDYTMRIFNSDGSEPEMCGNGIRCFARFIA
ELENLQGKNSYKIHTGAGLIIPEMQADGQVKVDMGEPILKGPEVPTKLAATKDGAVVQAELDVDGKTWLV
TCVSMGNPHCVTFGEKELKVDDLPLEKIGPKFEHHEMFPARTNTEFVQVVSRSHLKMRVWERGAGATLAC
GTGACALVVAAVLEGRADRNCTVDLPGGPLEIEWRESDNHIYMTGPAELVFYGEIRL
>gnl|CDD|178152 PLN02537, PLN02537, diaminopimelate decarboxylase
LYCEGLRVQDIMESVEKRPFYLYSKPQITRNYEAYKEALEGLRSIIGYAIKANNNLKILEHLRELGCGAV
LVSGNELRLALRAGFDPTRCIFNGNGKLLEDLVLAAQEGVFVNVDSEFDLENIVEAARIAGKKVNVLLRI
NPDVDPQVHPYVATGNKNSKFGIRNEKLQWFLDAVKAHPNELKLVGAHCHLGSTITKVDIFRDAAVLMVN
YVDEIRAQGFELSYLNIGGGLGIDYYHAGAVLPTPRDLIDTVRELVLSRDLTLIIEPGRSLIANTCCFVN
RVTGVKTNGTKNFIVIDGSMAELIRPSLYDAYQHIELVSPPPPDAEVSTFDVVGPVCESADFLGKDRELP
TPPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWVEEDGSITKIRHAETFDDHLRFFEGL
>gnl|CDD|215295 PLN02538, PLN02538, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
PAQSGDTDWKLAPHPKIPKGKPLLLIVLDGWGENAPDEFNAIHVAPTPTMDSLKAGAPERWRLVKAHGTA
VGLPSDDDMGNSEVGHNALGAGRIFAQGAKLVDLALASGKIFEGEGFKYIKEAFATGTLHLIGLLSDGGV
HSRLDQLQLLLKGAAERGAKRIRVHVLTDGRDVPDGSSVGFVETLEKDLAELREKGCDARIASGGGRMYV
TMDRYENDWNVVKRGWDAHVLGEAPHKFKSALEAVKKLREEPPPANDQYLPPFVIVDEDGKPVGPIEDGD
AVVTFNFRADRMVMIAKALEYEDFDKFDRVRVPKIRYAGMLQYDGELKLPSHYLVSPPLIERTSGEYLVA
NGVRTFACSETVKFGHVTFFWNGNRSGYFNEKLEEYVEIPSDNGIPFNVQPKMKALEIAEKARDALLSGK
FDQVRVNLANGDMVGHTGDLEATIVACEAVDAAVKEILDAVEQVGGIYLVTADHGNAEDMVKRDKSGKPL
LDKDGNPQILTSHTLAPVPVAIGGPGLPPGVRFRDDLPTAGLANVAATVMNLHGFEAPADYEPSLIEV
>gnl|CDD|178154 PLN02539, PLN02539, glucose-6-phosphate 1-dehydrogenase
RNDSFVKEYEKVVETGCLSIIVLGASGDLAKKKTFPALFNLYRQGFLPPDEVHIFGYARSKITDEELRDR
IRGYLKDEKNAPAEAVSKFLQLIKYVSGAYDSEEGFRRLDKEISEHEISKNSAEGSSRRLFYLALPPSVY
PPVCKMIKKCCMNKSGLWTRIVVEKPFGKDLESAEELSSQIGELFDESQLYRIDHYLGKELVQNLLVLRF
ANRFFLPLWNRDNIANVQIVFREDFGTEGRGGYFDEYGIIRDIIQNHLLQVLCLVAMEKPVSLKPEHIRD
EKVKVLQSVEPIKDEEVVLGQYEGYRDDPTVPDDSNTPTFASVVLRINNERWEGVPFILKAGKALDSRKA
EIRVQFKDVPGDIFKCQKQGRNEFVIRLQPSEAMYMKLTVKQPGLEMSTVQSELDLSYGQRYQDVVIPEA
YERLILDTIRGDQQHFVRRDELKAAWEIFTPLLHRIDAGKVKPIPYKQGSRGPAEADELLEKAGYVQTHG
Y
>gnl|CDD|215296 PLN02540, PLN02540, methylenetetrahydrofolate reductase
FSFEFFPPKTEEGVDNLFERMDRMVAHGPLFCDITWGAGGSTADLTLDIANRMQNMICVETMMHLTCTNM
PVEKIDHALETIKSNGIQNILALRGDPPHGQDKFVQVEGGFACALDLVKHIRSKYGDYFGITVAGYPEAH
PDVIGGDGLATPEAYQKDLAYLKEKVDAGADLIITQLFYDTDIFLKFVNDCRQIGITCPIVPGIMPINNY
KGFLRMTGFCKTKIPAEITAALEPIKDNDEAVKAYGIHLGTEMCKKILAHGIKGLHLYTLNLEKSALAIL
MNLGLIDESKVSRPLPWRPPTNVFRTKEDVRPIFWANRPKSYISRTTGWDQYPHGRWGDSRSPAYGALSD
HQFMRPRARDKKLQAEWGVPLKSVEDVYEVFAKYCLGKLKSSPWSELDGLQPETKIINEQLVKINRKGFL
TINSQPAVNGEKSDSPSVGWGGPGGYVYQKAYLEFFCSPEKLDALVEKCKAFPSLTYIAVNKAGEWISNV
GPGDVNAVTWGVFPAKEIIQPTVVDPASFMVWKDEAFELWSSEWANLYPEGDPSRKLLEEIKDSYYLVSL
VDNDY
>gnl|CDD|215297 PLN02541, PLN02541, uracil phosphoribosyltransferase
VAPSRSSRLTRTVRASADAAASEPSPKAPQQMLVFVPPHPLIKHWLSVLRNEQTPPPIFRSAMAELGRLL
IYEASRDWLPTMTGEVQTPMGVADVEFIDPREPVAVVPILRAGLVLLEHASSVLPATKTYHLGFVRDEET
LQPSMYLNKLPDKFPEGSRVLVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCAVAAPPALKKLSEKFP
GLHVYAGIIDEEVNEKGYIVPGLGDAGDRSFGTE
>gnl|CDD|215298 PLN02542, PLN02542, fructose-1,6-bisphosphatase
AATTTSSHLLLSSSRSVAPASQCQLSSFDSLTLNSFPRSPGSKKHHSAAGVRCAAAAAAAAATASPAATK
KSGYEIQTLTTWLLKQEQAGVIDAELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLD
VISNEVFSNCLRSSGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNDE
CLADIGDDSTLDSVEQRCIVNVCQPGSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENI
QIPKAGKIYSFNEGNYQLWDDKLKKYIDDLKDPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKS
KNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQPTEIHQRVPLYIGSVEEVEKLEKYLA
>gnl|CDD|215299 PLN02543, PLN02543, pfkB-type carbohydrate kinase family protein
MAPFLLLPHLHHSYSSLDRREKTCLRSSQKTRRFPKPKASLHPSIKRSRPGRCSTNGAAVPESPKPSRRG
RKKKPTSSPPKAKTTRRRTKKTDQELDPEGAEEDQEAAEDGEDYDDGIDFPYDDPPLVCCFGAVQKEFVP
TVRVHDNQMHPDMYSQWKMLQWDPPEFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNK
ERVQTRAVKFDENAKTACSRMKIKFRDGGKMVAETVKEAAEDSLLASELNLAVLKEARMFHFNSEVLTSP
SMQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRELIKKAWNEADIIEVSRQELEFLLDEDYYERK
RNYPPQYYAESFEQTKNWRDYYHYTPEEIAPLWHDGLKLLLVTDGTLRIHYYTPKFDGVVVGTEDVLITP
FTCDRTGSGDAVVAAIMRKLTTCPEMFEDQDVLERQLRFAVAAGIISQWTIGAVRGFPTESATQNLKEQV
YVPSMW
>gnl|CDD|178159 PLN02544, PLN02544, phosphoribosylaminoimidazole-succinocarboxamide synthase
VSSLRTLPEFMKPASPSSGVGGASGKFRAQQLPSPALSLDDLSSSGRRPEVLGAIKEALSNCLTETNLDL
TVPGLGSRRRGKVRDIYDLGDYLVLVTTDRQSAFDRVLASIPFKGQVLNQTSAWWFNNTKHITPNALVSS
PDPNVTIAKKCSVFPVEFVVRGYMTGSTSTSLWTVYNKGVRNYCGNDLPDGMVKNQKLPANILTPTTKAA
DHDVPISPEEIVEEGLMTQEDFDEVSSKALALFAFGQEVAAEHGLILVDTKYEFGKDADGTILLIDEVHT
PDSSRYWLADSYEERHAAGLEPENIDKEFLRLWFKENCDPYKDEVLPEAPAELVCELSWRYIKLYETITG
EKFEVPDTQEPIHERISRNV
>gnl|CDD|215300 PLN02545, PLN02545, 3-hydroxybutyryl-CoA dehydrogenase
MAEIKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATLG
RIRCTTNLEELRDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGM
HFMNPPPIMKLVEIIRGADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVA
SKEDIDTGMKLGTNHPMGPLHLADFIGLDTCLSIMKVLHEGLGDSKYRPCPLLVQYVDAGRLGRKSGRGV
YHYDGKKRGDPPRLS
>gnl|CDD|215301 PLN02546, PLN02546, glutathione reductase
AAATLPSTSKLTSSPSLQTLYRKLPLRLPLPSSSSSSHLPLPKTLTRLSSPRPLSHHHRRRSVSRAAAPN
GAESERHYDFDLFTIGAGSGGVRASRFASNFGASAAVCELPFATISSDTLGGVGGTCVLRGCVPKKLLVY
ASKYSHEFEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDV
DGKLYTARNILIAVGGRPFIPDIPGIEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHV
FIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNKGTVEGFSHVMFATGRKP
NTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNEPTKPDY
RAVPSAVFSQPPIGQVGLTEEQAIEEYGDVDVFTANFRPLKATLSGLPDRVFMKLIVCAKTNKVLGVHMC
GEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTMRTPTRKIRKDSPSEGKTKDEVKAAAGV
>gnl|CDD|215302 PLN02547, PLN02547, dUTP pyrophosphatase
PAVQEPPPKIQKPSPLLRVKKLSEKATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTY
ARIAPRSGLAWKHSIDVGAGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLD
ATVRGAGGFGSTGVALS
>gnl|CDD|178163 PLN02548, PLN02548, adenosine kinase
MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG
ATSYMGCIGKDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVEHLKKP
ENWALVEKAKFYYIAGFFLTVSPESIMLVAEHAAANNKTFMMNLSAPFICEFFKDQLMEALPYVDFLFGN
ETEARTFAKVQGWETEDVEEIALKISALPKASGTHKRTVVITQGADPTVVAEDGKVKEFPVIPLPKEKLV
DTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCTYPEKPDFS
>gnl|CDD|178164 PLN02549, PLN02549, asparagine synthase (glutamine-hydrolyzing)
MCGILAVLGCSDDSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLAIMDPESGDQPLYNEDKTI
VVTANGEIYNHKELREKLKLHKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHI
GITPLYIGWGLDGSVWFASEMKALCDDCERFEEFPPGHYYSSKAGGFRRWYNPPWFSESIPSTPYDPLVL
REAFEKAVIKRLMTDVPFGVLLSGGLDSSLVASIAARHLAETKAARQWGQQLHSFCVGLEGSPDLKAARE
VADYLGTVHHEFHFTVQEGIDAIEDVIYHLETYDVTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEIFG
GYLYFHKAPNKEEFHKETCRKIKALHQYDCLRANKSTSAWGLEARVPFLDKEFIDVAMSIDPEWKMIRPG
EGRIEKWVLRKAFDDEEDPYLPKHILWRQKEQFSDGVGYSWIDGLKAHAEKHVSDEMFANASFRYPHNTP
TTKEAYYYRMIFEKHFPQDAARLTVPGGPSVACSTAKAVEWDAAWSKNLDPSGRAALGVHVAAYEEDVAA
DGAPAVPKAKKSKAPAIG
>gnl|CDD|178165 PLN02550, PLN02550, threonine dehydratase
MSSVGLPTAGSPLRSHIGSPSKPVVGSTPFSRSRIPAAVDSADETSMAPPPPPSPLPLLKVSPNSLQYPA
GYLGAVPERTNEAENGSIPEAMEYLTNILSAKVYDVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFK
LRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVG
DSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIFVPVGGGGLIAGIAAYVK
RVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVSRDAIC
ASIKDMFEEKRSILEPAGALALAGAEAYCKYYGLKDENVVAITSGANMNFDRLRIVTELADVGRQQEAVL
ATFMPEEPGSFKRFCELVGPMNITEFKYRYSSEKEALVLYSVGVHTEQELQALKKRMESAQLRTVNLTSN
DLVKDHLRYLMGGRAIVKDELLYRFVFPERPGALMKFLDAFSPRWNISLFHYRGQGETGANVLVGIQVPP
EEMQEFKSRANALGYEYQDECDNEAFQLLMH
>gnl|CDD|178166 PLN02551, PLN02551, aspartokinase
SVPVGGGSARRRSVGSSCRNIVLRVNCSAGRVEALVEAPSETRQGGGTEKQLTVVMKFGGSSVASAERMR
EVADLILSFPDERPVVVLSAMGKTTNNLLLAGEKAVSCGVTNVSEIEELSAIRELHLRTADELGVDESVV
EKLLDELEQLLKGIAMMKELTPRTRDYLVSFGERMSTRIFAAYLNKIGVKARQYDAFDIGFITTDDFTNA
DILEATYPAVAKRLHGDWIDDPAVPVVTGFLGKGWKTGAITTLGRGGSDLTATTIGKALGLREIQVWKDV
DGVLTCDPRIYPNAVPVPYLTFDEAAELAYFGAQVLHPQSMRPAREGDIPVRVKNSYNPTAPGTLITKTR
DMSKAVLTSIVLKRNVTMLDIVSTRMLGQYGFLAKVFSTFEDLGISVDVVATSEVSISLTLDPSKLWSRE
LIQQELDHLVEELEKIAVVNLLQGRSIISLIGNVQRSSLILEKVFRVLRTNGVNVQMISQGASKVNISLI
VNDDEAEQCVRALHSAFFEGDCLVEVEEGPL
>gnl|CDD|215303 PLN02552, PLN02552, isopentenyl-diphosphate delta-isomerase
MGTMADATWAGMDAVQRRLMFEDECILVDENDNVVGHDSKYNCHLFEKIEPRGLLHRAFSVFLFNSKYEL
LLQQRAATKVTFPLVWTNTCCSHPLYGQDPNEVDRESELIDGNVLGVKNAAQRKLLHELGIPAEDVPVDQ
FTFLTRLHYKAADDVTHGPDGKWGEHELDYLLFIRPVRDVKVNPNPDEVADVKYVNREELKEMMRKESGL
KLSPWFRLIVDNFLMKWWDDLEKGTEAVDMKTIHKLM
>gnl|CDD|178168 PLN02553, PLN02553, inositol-phosphate phosphatase
MAQNDDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIG
EETTAASGGTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGA
FLNGKPIKASSQSELGKALLATEVGTKRDKATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDI
FYEIGFGGPWDVAAGAVIVKEAGGLVFDPSGGPFDIMSRRVAASNGHLKDAFVEALRQTE
>gnl|CDD|215304 PLN02554, PLN02554, UDP-glycosyltransferase family protein
MKIELVFIPSPGIGHLRPTVELAKLLVDSDDRLSITVIIIPSRSGDDASSSAYIASLSASSEDRLRYEVI
SAGDQPTTEDPTFQSYIDNQKPKVRDAVAKLVDDSSTPSSPRLAGFVVDMFCTSMIDVANEFGVPSYMFY
TSNATFLGLQLHVQMLYDEKKYDVSELEDSEVELDVPSLTRPYPVKCLPSVLLSKEWLPLFLAQARRFRE
MKGILVNTVAELEPQALKFFSGSSGDLPPVYPVGPVLHLENSGDDSKDEKQSEILRWLDEQPPKSVVFLC
FGSMGGFSEEQAREIAIALERSGHRFLWSLRRASPNIMKEPPGEFTNLEEILPEGFLDRTKDIGKVIGWA
PQVAVLAKPAIGGFVTHCGWNSILESLWFGVPMAAWPLYAEQKFNAFEMVEELGLAVEIRKYWRGDLLAG
EMETVTAEEIERGIRCLMEQDSDVRKRVKEMSEKCHVALMDGGSSHTALKKFIQDVTKNIA
>gnl|CDD|178170 PLN02555, PLN02555, limonoid glucosyltransferase
MESESSLVHVMLVSFPGQGHVNPLLRLGKLLASKGLLVTFVTTESWGKKMRQANKIQDGVLKPVGDGFIR
FEFFEDGWAEDDPRRQDLDLYLPQLELVGKREIPNLVKRYAEQGRPVSCLINNPFIPWVCDVAEELGIPS
AVLWVQSCACFSAYYHYYHGLVPFPTETEPEIDVQLPCMPLLKYDEIPSFLHPSSPYPFLRRAILGQYKN
LDKPFCILIDTFQELEKEIIDYMSKLCPIKPVGPLFKMAKTPNSDVKGDISKPADDCIEWLDSKPPSSVV
YISFGTVVYLKQEQIDEIAYGVLNSGVSFLWVMRPPHKDSGVEPHVLPEEFLEKAGDKGKIVQWCPQEKV
LAHPSVACFVTHCGWNSTMEALSSGVPVVCFPQWGDQVTDAVYLVDVFKTGVRLCRGEAENKLITREEVA
ECLLEATVGEKAAELKQNALKWKEEAEAAVAEGGSSDRNFQEFVDKLVRKSVEIVDNGSH
>gnl|CDD|178171 PLN02556, PLN02556, cysteine synthase/L-3-cyanoalanine synthase
MAALLSRLKRRSSIPPSSHTLRKLFSTVGSPSFAQRLRDLPKDLPGTKIKTDASQLIGKTPLVYLNKVTE
GCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTTLIEPTSGNMGISLAFMAAMKGYKMILT
MPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIW
EDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILD
MDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSV
LFQELRKEAENMQPVSVD
>gnl|CDD|178172 PLN02557, PLN02557, phosphoribosylformylglycinamidine cyclo-ligase
SSACYSSQAAPARASFSSSSSLPPLRRSAAQAARARRKRARLSPSKAGRSNKDDSEEGLTYKDAGVDIDA
GSELVRRIAKMAPGIGGFGGLFPFGDSYLVAGTDGVGTKLKLAFETGIHDTIGIDLVAMSVNDIVTSGAK
PLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSVKKDAVID
GKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPGASVTIGEALMAPTVIYVKQVLDIISKG
GVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSP
EAADRILEEGAYPAYRIGEVINGEGVVYV
>gnl|CDD|166199 PLN02558, PLN02558, CDP-diacylglycerol-glycerol-3-phosphate/ 3-phosphatidyltransferase
PQQLSSKVLTLPTVLTLGRVAAVPLLVATFYVDSWWGRTATTSIFIAAAITDWLDGYLARKMKLGTAFGA
FLDPVADKLMVAAALILLCSRPLEVAVLGEVPWLFTVPAIAIIGREITMSAVREWAASQNGKLLEAVAVN
NLGKWKTATQMISLTILLASRDSSLEGPGILVPSGVGLLYISAGLSIWSLAVYMSKIWKVLLK
>gnl|CDD|178173 PLN02559, PLN02559, chalcone--flavonone isomerase
FPAVTEVQVEGVTFPPSVKPPGSSNPLFLGGAGVRGLEIQGKFIKFTAIGVYLEGNAVPSLAKKWKGKTA
EELADSVAFFRDVVTGDFEKFTRVTMILPLTGEQYSEKVTENCVAIWKSLGIYTDAEAKAVEKFKEAFKE
ETFPPGSSILFTHSPTGSLTVAFSKDSSVPEVGNAVIENKLLCEAVLESIIGKHGVSPAAKLSLAARLSE
LLKKEKEGENAAAESVPVSA
>gnl|CDD|178174 PLN02560, PLN02560, enoyl-CoA reductase
MKVTVVSRSGREIIKGGLEVPDSATVADLKKAIHKRKKKYYPSRQRLTLPLPPGKTRPTVLDDSKSLKDY
GLGDGGTVVFKDLGPQVSYRTLFFFEYLGPLLIYPLFYFFPQVYKYFGYPARRVIHPVQTYAMYYWCFHY
AKRILETFFVHRFSHATSPLFNVFRNCAYYWTFGAYIAYFVNHPLYTPVSETQMKVGFGFGLVCQLANFY
CHIILRNLRKPDGKGGYQIPRGFLFNYVTCANYTTEIYQWLGFNIATQTVAGYLFLAVAAAIMTNWALAK
HRRLKKLFDGKDGRPKYPRRWVILPPFL
>gnl|CDD|178175 PLN02561, PLN02561, triosephosphate isomerase
MARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSEDVVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVK
KGGAFTGEISAEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGST
MDVVAAQTKAIADKVSDWANVVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYG
GSVTGANCKELAAQPDVDGFLVGGASLKPEFIDIIKSATVKKS
>gnl|CDD|215305 PLN02562, PLN02562, UDP-glycosyltransferase
MKVTQRPKIILVPYPAQGHVTPMLKLASAFLSRGFEPVVITPEFIHRRISATLDPKLGITFMSISDGQDD
DPPRDFFSIENSMENTMPPQLERLLHKLDEDGEVACMVVDLLASWAIGVADRCGVPVAGFWPVMLAAYRL
IQAIPELVRTGLISETGCPRQLEKICVLPEQPLLSTEDLPWLIGTPKARKARFKFWTRTLERTKSLRWIL
MNSFKDEEYDDVKNHQASYNNGQNPQILQIGPLHNQEATTITKPSFWEEDMSCLGWLQEQKPNSVIYISF
GSWVSPIGESNVRTLALALEASGRPFIWVLNPVWREGLPPGYVERVSKQGKVVSWAPQLEVLKHQAVGCY
LTHCGWNSTMEAIQCQKRLLCYPVAGDQFVNCAYIVDVWKIGVRISGFGQKEVEEGLRKVMEDSGMGERL
MKLRERAMGEEARLRSMMNFTTLKDELK
>gnl|CDD|178177 PLN02563, PLN02563, aminoacyl-tRNA ligase
LSLQTRAPPPSASSAFRFTSLRLSLFLVVSSAQTPASASSYFRRSRRGGVSRSLTRRAFAAPSALTSTTA
KTTPAAKRAYPFHEIEPKWQRYWEENRTFRTPDDVDTSKPKFYVLDMFPYPSGAGLHVGHPEGYTATDIL
ARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLKNIARFRSQLKSLGFSYDWDREISTTEPEY
YKWTQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEVVDGLSERGGHPVIRKPMRQWMLKITAYADRL
LEDLDDLDWPESIKEMQRNWIGRSEGAELDFSVLDGEGKERDEKITVYTTRPDTLFGATYLVVAPEHPLL
SSLTTAEQKEAVEEYVDAASRKSDLERTELQKEKTGVFTGSYAINPATGEAIPIWVADYVLGSYGTGAIM
AVPAHDTRDFEFAQKFDLPIKWVVKPADGNEDDAEKAYTGEGVIVNSSSSGLDINGLSSKEAAKKVIEWL
EETGNGKKKVNYKLRDWLFARQRYWGEPIPVVFLEDSGEPVPVPESDLPLTLPELDDFTPTGTGEPPLAK
AVSWVNTVDPSSGKPARRETNTMPQWAGSCWYYLRFMDPKNSNALVDKEKEKYWMPVDLYVGGAEHAVLH
LLYARFWHKVLYDIGVVSTKEPFQCLVNQGMILGEVEYTAFKDSDGEYVSADTADRLGELQQEKIPEEKV
IKSGDSFVLKDDPSIRLIARAHKMSKSRGNVVNPDDVVSEYGADSLRLYEMFMGPLRDSKTWSTSGVEGV
HRFLGRTWRLVVGAPLPDGSFRDGTVVTDEEPSLEQLRLLHKCIAKVTEEIESTRFNTAISAMMEFTNAA
YKWDKVPREAIEPFVLLLSPYAPHLAEELWFRLGHSNSLAYEPWPEANPSYLVDDTVVLPVQINGKTRGT
IEVEEGCSEDDAFALASQDEKLSKYLDGKEIKKRIYVPGKILNVILKQQNVKV
>gnl|CDD|178178 PLN02564, PLN02564, 6-phosphofructokinase
GSSKPKIVTGDAGYVLEDVPHLTDYLPDLPTYPNPLQDNPAYSVVKQYFVNEDDTVAQKIVVHKDSPRGT
HFRRAGPRQKVYFESDEVRACIVTCGGLCPGLNTVIREIVCGLSYMYGVTRILGIDGGYRGFYSRNTIPL
TPKVVNDIHKRGGTILGTSRGGHDTSKIVDSIQDRGINQVYIIGGDGTQKGASVIYEEIRRRGLKVAVAG
IPKTIDNDIPVIDKSFGFDTAVEEAQRAINAAHVEAESVENGIGLVKLMGRYSGFIAMYATLASRDVDCC
LIPESPFYLEGKGGLFEFIEKRLKENGHMVIVVAEGAGQDLIAESMESSDLQDASGNKLLLDVGLWLSQK
IKDHFTKVKKMPINLKYIDPTYMIRAIPSNASDNVYCTLLAHSAVHGAMAGYTGFTVGPVNGRHAYIPFY
RITEKQNKVVITDRMWARLLSSTNQPSFLSPKDVLEAKREDEEAEKLDDGPLSSIDVTGVTASS
>gnl|CDD|166206 PLN02565, PLN02565, cysteine synthase
EKSSIAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVL
IEPTSGNTGIGLAFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTP
NSYILQQFENPANPKIHYETTGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVES
AVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKI
AKRPENAGKLIVVIFPSFGERYLSSVLFESVKKEAENMVFEP
>gnl|CDD|215306 PLN02566, PLN02566, amine oxidase (copper-containing)
MNIPILALVFILQCCFVASLYHPLDPLNPQEINKIRLIVQKSHLGNLPNLTFHFLDLEEPEKRDVLKWLS
SNPSNKSPPPRRAKVVVRAGGETYELIVDLATGSITSSRVYTGHGYPPLTFIELFQASKLPLKYPKFKKS
ILRRGLNISEVSCIPFTVGWYGETVTKRALKISCFYRGGSVNVFARPIEGISILIDVDSMQIIKYSDRFR
APLPKAEGTDFRTKHKPFSFPCNVSDSGFTILGHRVKWANWDFHVGFDARAGVTISTASVFDAKVKRFRR
VLYRGHVSETFVPYMDPTSEWYFRTFMDIGEFGFGRSAVTLQPLIDCPANAVYLDGYVAGADGQAQKMTN
VICIFERYSGDVAFRHTEINVPGRVIRSGEPEISLVVRMVATLGNYDYILDWEFKKSGSIKVGVDLTGVL
EMKATSYTNNDQITKDVYGTLVAENTIAVNHDHFLTYYLDLDVDGNGNSFVKAKLQTARVTAVNASSPRK
SYWTVVKETAKTEAEGRIRLGSEPAELLIVNPNKKTKLGNQVGYRLITGQPVTSLLSDDDYPQIRAAYTK
YQVWVTAYNKSERWAGGFYADRSRGDDGLAVWSSRNREIENKDIVLWYTVGFHHIPYQEDFPVMPTLHGG
FELRPANFFESNPLLR
>gnl|CDD|215307 PLN02567, PLN02567, alpha,alpha-trehalase
VVPTTPLLTFLVRVQSTALASFGGEDTFDPKLYVDLPLKFSLSETEKAFDALPRSNINGSVPVEELEEFV
AEYFDVAGSDLLPYTPPDFVPEPPGFLPKVENPEAREWALKVHSLWKNLARKVSDSVEERPDRHTLLPLP
NPVVVPGSRFREVYYWDSYWVIRGLLASKMYETAKGVVENLLYLVDTYGFVPNGARAYYTNRSQPPLLSA
MVLAVYAATKDVELVRRALPALLKEHAFWTSGRHTVTIRDANGVVHVLSRYYAMWDKPRPESSRIDKEVA
SKFSSSSEKQQLYRDIASAAESGWDFSSRWMRDGSNLTTLRTTSILPVDLNAFLLKMELDIAFFAKLLGD
KATAERFLKAAKARKRAINAVLWNEEMGQWLDYWLPPNGATCQESYTWDAENQNTNVYASNFVPLWCGVV
PPGDAKVEKVVESLKSSGLVLPAGIATSLRNTGQQWDFPNAWAPLQHMIVEGLAASGSKEGKALAEDIAR
RWLRSNYVAYKKTGAMHEKYDARYCGEVGGGGEYIPQTGFGWSNGVVLSLLEEFGWPEDKKLDC
>gnl|CDD|215308 PLN02568, PLN02568, polyamine oxidase
MVAKKPRIVIIGAGMAGLTAANKLYTSSAANDMFELTVVEGGDRIGGRINTSEFGGERIEMGATWIHGIG
GSPVYKIAQEAGSLESDEPWECMDGFPDRPKTVAEGGFEVDPSIVESISTLFRGLMDDAQGKLIEPSEVD
EVDFVKLAAKAARVCESGGGGSVGSFLRRGLDAYWDSVSADEQIKGYGGWSRKLLEEAIFTMHENTQRTY
TSADDLSTLDLAAESEYRMFPGEEITIAKGYLSVIEALASVLPPGTIQLGRKVTRIEWQDEPVKLHFADG
STMTADHVIVTVSLGVLKAGIGEDSGLFSPPLPDFKTDAISRLGFGVVNKLFVELSPRPDGSPEDVAKFP
FLQMAFHRSDSEARHDKIPWWMRRTASICPIHKNSSVLLSWFAGKEALELEKLSDEEIIRGVQTTLSSFL
KRRVAGLGSQSHPLCNGGASSNDGSRWKFVKVLKSKWGTDPLFLGSYSYVAVGSSGDDLDRMAEPLPRIS
DHDQAGGPPLQLLFAGEATHRTHYSTTHGAYFSGLREANRLLQHYKCVG
>gnl|CDD|178182 PLN02569, PLN02569, threonine synthase
VASVTRAVISDPPPIKSATKFTADENIRDEARRGPPAPPDEFSAKYVPFLECPLTGEKYSLDEVVYRSKS
GGLLDVRHDMEALKRYDGKYWRALFDSRVGKTTWPYGSGVWSKKEWVLPEIDDDDIVSLFEGNSNLFWAE
RLGKEFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMAKPVVGVGCASTGDTSAALSAYCAAAG
IPSIVFLPADKISIAQLVQPIANGALVLSIDTDFDGCMRLIREVTAELPIYLANSLNSLRLEGQKTAAIE
ILQQFDWEVPDWVIVPGGNLGNIYAFYKGFKMCKELGLVDRLPRLVCAQAANANPLYRAYKSGWEEFKPV
KANPTFASAIQIGDPVSIDRAVYALKESNGIVEEATEEELMDAQAEADKTGMFLCPHTGVALAALKKLRA
SGVIGPTDRTVVVSTAHGLKFTQSKIDYHSKEIPDMACRFANPPVSVKADFGSVMDVLKKYLSL
>gnl|CDD|215309 PLN02571, PLN02571, triacylglycerol lipase
KGKKKKEKEEKLIVVRSIAKRWRHLSGQNHWKGLLDPLDQDLREYIIHYGEMAQATYDTFNIQKASKFAG
SSLYAKKDFFAKVGLEKGNPYKYKVTKFLYATSQIHVPEAFILKSLSREAWSKESNWMGYVAVATDEGKA
LLGRRDIVIAWRGTVQTLEWVNDFEFNLVSASKIFGESNDQPKVHQGWYSIYTSDDERSPFNKTSARDQV
LNEVGRLVEKYKDEEISITICGHSLGAALATLNAVDIVANGFNRSKSRPNKSCPVTAFVFASPRVGDSDF
KKLFSGLKDLRVLRVRNLPDVIPNYPLIGYSDVGEELPIDTRKSKYLKSPGNLSTWHNLEAYLHGVAGTQ
GSKGGFRLEVNRDIALVNKSVDGLKDEYLVPGSWRVQKNKGMVQQADGSWKLMDHEEDDNEDL
>gnl|CDD|215310 PLN02572, PLN02572, UDP-sulfoquinovose synthase
MKMAHLLSTSTSSKAFTSASPASAQSTPAVTELATPSAPGSSSSSKKKKVMVIGGDGYCGWATALHLSKR
GYEVAIVDNLCRRLFDHQLGLDSLTPIASIHERVRRWKEVSGKEIELYVGDICDFEFLSEAFKSFEPDAV
VHFGEQRSAPYSMIDRSRAVFTQHNNVIGTLNVLFAIKEFAPDCHLVKLGTMGEYGTPNIDIEEGYITIT
HNGRTDTLPYPKQASSFYHLSKVHDSHNIAFTCKAWGIRATDLNQGVVYGVRTDETMMDEELINRLDYDG
VFGTALNRFCVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIEIAIANPAKPGEFRVFNQFTEQFSVNELA
KLVTKAGEKLGLDVEVISVPNPRVEAEEHYYNAKHTKLCELGLEPHLLSDSLLDSLLNFAVKYKDRVDTT
LILPAVSWKKIGVKPKTIAAKA
>gnl|CDD|215311 PLN02573, PLN02573, pyruvate decarboxylase
QSSAPKPATPVSSSDATLGRHLARRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAA
DGYARARGVGACVVTFTVGGLSVLNAIAGAYSENLPVICIVGGPNSNDYGTNRILHHTIGLPDFSQELRC
FQTVTCYQAVINNLEDAHELIDTAISTALKESKPVYISVSCNLAAIPHPTFSREPVPFFLTPRLSNKMSL
EAAVEAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADASGYPVAVMPSAKGLVPEHHPHFIGTYWGAV
STPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTIGNGPAFGCVLMKDFLEALAKR
VKKNTTAYENYKRIFVPEGEPLKSEPGEPLRVNVLFKHIQKMLSGDTAVIAETGDSWFNCQKLKLPEGCG
YEFQMQYGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGYTIEVE
IHDGPYNVIKNWNYTGLVDAIHNGEGKCWTAKVRTEEELIEAIATATGEKKDCLCFIEVIVHKDDTSKEL
LEWGSRVSAANSRPPNPQ
>gnl|CDD|215312 PLN02574, PLN02574, 4-coumarate--CoA ligase-like
IMPNLKAQTSHNNPPFWYSPETGIYSSKHPPVPLPSDPNLDAVSFIFSHHNHNGDTALIDSSTGFSISYS
ELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSV
GLAFTSPENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTT
GASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFD
ASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQ
GYGMTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPK
ATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKE
CGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVSSRL
>gnl|CDD|215313 PLN02575, PLN02575, haloacid dehalogenase-like hydrolase
MADSIAATSLVGHRPLCGRLSVKDESYRRKSQSSCRFPVKEFVGRRLVASSPMLQRVKKDRLVVTSIKAL
AMELTKEAYSYREEERIPRTWNYRLDTGADRKPGLWPPENRADNPSLHNPLLRQERMGCGWLGAIFEWEG
VIIEDNPDLENQAWLTLAQEEGKSPPPAFILRRVEGMKNEQAISEVLCWSRDPAELRRMATRKEEIYQAL
QGGIYRLRTGSQEFVNVLMNYKIPMALVSTRPRKTLENAIGSIGIRGFFSVIVAAEDVYRGKPDPEMFIY
AAQLLNFIPERCIVFGNSNQTVEAAHDARMKCVAVASKHPIYELGAADLVVRRLDELSIVDLKNLADIES
PEFGPPEPELEMEKEEDRELPSSAGVDDIFW
>gnl|CDD|215314 PLN02576, PLN02576, protoporphyrinogen oxidase
SAIAEGSAAASSKDVAVVGAGVSGLAAAYALASKHGVNVLVTEARDRVGGNITSVSEDGFIWEEGPNSFQ
PSDPELTSAVDSGLRDDLVFPDPQAPRYVVWNGKLRPLPSNPIDLPTFDLLSAPGKIRAGLGAFGWKRPP
PPGREESVGEFVRRHLGDEVFERLIDPFVSGVYAGDPSSLSMKAAFPKLWNLEKRGGSIIGGAIKAIQEA
KKNPKPEPRDPRLPKPKGQTVGSFRGGLQTLPDALAKRLGKDKVKLNWKVLSLSKNDDGGYSLTYDTPEG
KVNVTAKAVVMTAPLYVVSEMLRPKSPAAADALPEFYYPPVAAVTTSYPKEAVKRERLIDGPLEGFGQLH
PRKQGVKTLGTIYSSSLFPDRAPEGRVLLLNYIGGSRNTGIASASEEELVEAVDRDLRKLLLKPGAPPPK
VVGVRVWPKAIPQYLLGHLDVLEAAEKMEKDLGLPGLFLGGNYRGGVALGKCVESGYEAADLVISYLESS
AYKKMF
>gnl|CDD|178189 PLN02577, PLN02577, hydroxymethylglutaryl-CoA synthase
MPKNVGILAMEVYFPPTCVQQEALEAHDGVSKGKYTIGLGQDCMAFCTDVEDVISMSLTVVKSLLEKYNI
DPKQIGRLEVGSETVIDKSKSIKTFLMQLFEESGNTDIEGVDSTNACYGGTAALLNCVNWVESSSWDGRY
GLVVAADSAVYAEGPARPTGGAGAVAMLVGPNAPIVFESKYRGSHMAHVYDFYKPDLASEYPVVDGKLSQ
TCYLMALDSCYKRFCEKYEKLEGKQFSISDADYFVFHAPYNKLVQKSFARLVYNDFQRNASSVDEDAKEK
LAPFAGLSSDESYQNRDLEKVSQQVAKPLYDAKVQPTTLIPKQVGNMYTASLYAALASLVHNKHSELAGK
RILMFSYGSGLTATMFSLRLHEGQHPFSLSNIAKVMDVSEKLKSRHEVSPEKFVETLKLMEHRYGAKDFV
PSKDVSLLAPGTYYLTEVDSLYRRFYDRKALNGSIANGH
>gnl|CDD|215315 PLN02578, PLN02578, hydrolase
RARLFSSGSNLFAIARWRSSIDRPLLGINRRIFIFGGIVASGVSVMGSSSASQSVQGLERLPFKKEGYNF
WTWRGHKIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRD
QVADFVKEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESREKEEAIVVEETVLTRF
VVKPLKEWFQRVVLGFLFWQAKQPSRIESVLKSVYKDKSNVDDYLVESITEPAADPNAGEVYYRLMSRFL
FNQSRYTLDSLLSKLSCPLLLLWGDLDPWVGPAKAEKIKAFYPDTTLVNLQAGHCPHDEVPEQVNKALLE
WLSS
>gnl|CDD|215316 PLN02579, PLN02579, sphingolipid delta-4 desaturase
MSEEEEEGVMATDFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGW
PKILLVAYFFGGFLNHNLFLAIHELSHNLAFKTPVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVD
GIDMDIPSQGEARLVRNTLSKIVWVFLQLFFYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKS
LAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYSYYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKE
IAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRKPPKKSD
>gnl|CDD|215317 PLN02580, PLN02580, trehalose-phosphatase
MDLKSNHSSPVLTDPAPINKSRLGIRSNLLPYSSAGASFSSNLFLTIPRKKTGKLDDVRSNGWLDAMKSS
SPPRKKLNKDFNVELASPDTDFAYRTWMLKYPSALTSFEQIANFAKGKKIALFLDYDGTLSPIVDDPDRA
LMSDAMRSAVKNVAKYFPTAIISGRSRDKVYELVGLTELYYAGSHGMDIMGPVRESVSNDHPNCIKSTDQ
QGKEVNLFQPASEFLPMIDEVFRSLVESTKDIKGAKVENHKFCVSVHYRNVDEKNWPLVAQCVHDVLKKY
PRLRLTHGRKVLEVRPVIDWNKGKAVEFLLESLGLSNCDDVLPIYIGDDRTDEDAFKVLREGNRGYGILV
SSVPKESNAFYSLRDPSEVMEFLKSLVTWKKSEA
>gnl|CDD|215318 PLN02581, PLN02581, red chlorophyll catabolite reductase
RFIEFPKVSPAHRELMVDLASAVEARLGSLLLPSSLPPDVRSFQNQSGNAQGSLHIRSGAQGSKIDFVLG
SWLHCKLPTGGALNITSLSAFLNPSTDAPHFLVELIQSSPTSLVLILDLPPRKDLVLHPDYLKTYYEDTQ
LDAHRQKLEKLPQVQPYVSPSLYVRSVVSPTAILVKIDCEEGGEERLEEIVRDQVAPVAKEVLEIWLDSC
ACLGREMEEEERAYLEKRDRMIRSKSVEVDLSSNMPRLFGQEVADRVVAAIRKAFRV
>gnl|CDD|178194 PLN02582, PLN02582, 1-deoxy-D-xylulose-5-phosphate synthase
NRNLRSNRPSGVCASLSPEESAEYPSQRPPTPLLDTINYPIHMKNLSVKELKQLADELRSDVIFNVSKTG
GHLGSSLGVVELTVALHYVFNAPQDKILWDVGHQSYPHKILTGRRDKMHTMRQTNGLSGFTKRAESEYDC
FGTGHSSTTISAGLGMAVGRDLKGKKNNVVAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNKQVSLP
TATLDGPAPPVGALSSALSRLQSSRPLRELREVAKGVTKQIGGPMHELAAKVDEYARGMISGSGSTLFEE
LGLYYIGPVDGHNIDDLVTILREVKSTKTTGPVLIHVVTEKGRGYPYAERAADKYHGVVKFDPATGKQFK
VKAKTQSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACE
GLKPFCAIYSSFLQRGYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTYMACLPNMVVMAPSD
EAELFHMVATAAAIDDRPSCFRYPRGNGIGVQLPPNNKGIPIEVGKGRILLEGERVALLGYGTAVQSCLA
AASLLERHGLSATVADARFCKPLDRALIRSLAKSHEVLITVEEGSIGGFGSHVAQFMALDGLLDGKLKWR
PLVLPDRYIDHGAPADQLAEAGLTPSHIAATVLNVLGQTREALQIMS
>gnl|CDD|178195 PLN02583, PLN02583, cinnamoyl-CoA reductase
SFDESSKSVCVMDASGYVGFWLVKRLLSRGYTVHAAVQKNGETEIEKEIRGLSCEEERLKVFDVDPLDYH
SILDALKGCSGLFCCFDPPSDYPSYDEKMVDVEVRAAHNVLEACAQTDTIEKVVFTSSLTAVIWRDDNIS
TQKDVDERSWSDQNFCRKFKLWHALAKTLSEKTAWALAMDRGVNMVSINAGLLMGPSLTQHNPYLKGAAQ
MYENGVLVTVDVNFLVDAHIRAFEDVSSYGRYLCFNHIVNTEEDAVKLAQMLSPLIPSPPPYEMQGSEVY
QQRIRNKKLNKLMEDFA
>gnl|CDD|178196 PLN02584, PLN02584, 5'-methylthioadenosine nucleosidase
QQEEMRPISTVLIVIAMQAEAMPLVNALGLVEDVDSPFPKGVPWVRYSGTHKGLRVHVVCPGKDKALGVD
SVGTVPASLVTYAAIQALKPDLIINAGTAGGFKAKGAAIGDVFLATAVANHDRRIPIPVFDKYGVGTRDA
FPTPNLIKALGLKEGVLSTGNSLDMTEQDEESIKANDATVKDMEGAAVAYVADLLKVPAIFVKAVTDIVD
GDKPTAEEFLENLSAAAAALQGAVPKVLDFISGKCLSEL
>gnl|CDD|215319 PLN02585, PLN02585, magnesium protoporphyrin IX methyltransferase
MPFAPSALSASSSVAQFLPPFPNATLFAVPPRSRAATVAAASVADLAGVDSTTFAVGGGGAVAALAAALS
LTDPERRRQLQAEEVGGDDKEVVREYFNTTGFERWRKIYGETDEVNKVQLDIRLGHAQTVEKVLLWLAED
GSLAGVTVCDAGCGTGSLAIPLALEGAIVSASDISAAMVAEAERRAKEALAALPPEVLPKFEANDLESLS
GKYDTVTCLDVLIHYPQDKADGMIAHLASLAEKRLIISFAPKTLYYDILKRIGELFPGPSKATRAYLHAE
ADVERALKKAGWKVARREMTATQFYFSRLLEAVPV
>gnl|CDD|166227 PLN02586, PLN02586, probable cinnamyl alcohol dehydrogenase
MAKSPEEEHPQKAFGWAARDPSGVLSPFHFSRRENGDEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVP
GHEIVGIVTKLGKNVKKFKEGDRVGVGVIVGSCKSCESCDQDLENYCPKMIFTYNSIGHDGTKNYGGYSD
MIVVDQHFVLRFPDNLPLDAGAPLLCAGITVYSPMKYYGMTEPGKHLGVAGLGGLGHVAVKIGKAFGLKV
TVISSSSNKEDEAINRLGADSFLVSTDPEKMKAAIGTMDYIIDTVSAVHALGPLLGLLKVNGKLITLGLP
EKPLELPIFPLVLGRKLVGGSDIGGIKETQEMLDFCAKHNITADIELIRMDEINTAMERLAKSDVRYRFV
IDVANSLSQP
>gnl|CDD|178198 PLN02587, PLN02587, L-galactose dehydrogenase
LRELGSTGLKVSSVGFGASPLGSVFGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKAL
GIPREKYVVSTKCGRYGEGFDFSAERVTKSVDESLARLQLDYVDILHCHDIEFGSLDQIVNETIPALQKL
KESGKVRFIGITGLPLAIFTYVLDRVPPGTVDVILSYCHYSLNDSSLEDLLPYLKSKGVGVISASPLAMG
LLTENGPPEWHPAPPELKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAAT
ELETSGIDEELLSEVEAILAPVKNKTWPSGIQEN
>gnl|CDD|215320 PLN02588, PLN02588, glycerol-3-phosphate acyltransferase
MSGNKISTLQALVFFLYRFFILRRWCHRNPKQKYQKCPSHGLHQYQDLSNHTLIFNVEGALLKSNSLFPY
FMVVAFEAGGVIRSLFLFVLYPFISLMSYEMGLKTMVMLSFFGVKKESFRAGKAVLPKYFLEDVGLEMFQ
VLKRGGKRVGVSDLPQVMIDVFLRDYLEIEVVVGRDMKMVGGYYLGIMEDKKKHELAFDKVVQEERLNSG
RLIGITSFNSPSHRSLFSQFCQEIYFVRNSDKKSWQTLPRDQYPKPLIFHDGRLAIKPTPLNTLVLFMWA
PFAAALAAARLVFGLNLPYSLANPFLAFSGIHLTLTVNDLISSDRKKGCLFVCNHRTLLDPLYISYALRK
KNIKAVTYSLSRLSELLAPIKTVRLTRDRVKDGQAMEKLLSQGDLVVCPEGTTCREPYLLRFSPLFSEVC
DVIVPVAIDSHVTFFYGTTASGLKAFDPIFFLLNPFPSYTVQLLDPVSGSSSSTCQDPDNGKLKFEVANH
VQHEIGNALGFECTNLTRRDKYLILAGNNGVVKKK
>gnl|CDD|166230 PLN02589, PLN02589, caffeoyl-CoA O-methyltransferase
MANNEEQQQSQAGRHQEVGHKSLLQSDALYQYILETSVYPREPESMKELRELTAKHPWNIMTTSADEGQF
LNMLLKLINAKNTMEIGVYTGYSLLATALALPEDGKILAMDINRENYELGLPVIQKAGVAHKIDFREGPA
LPVLDQMIEDGKYHGTFDFIFVDADKDNYINYHKRLIDLVKVGGVIGYDNTLWNGSVVAPPDAPMRKYVR
YYRDFVLELNKALAADPRIEICMLPVGDGITLCRRIS
>gnl|CDD|178200 PLN02590, PLN02590, probable tyrosine decarboxylase
MYDREFGTGNGYSNGNGYTNGNGHTNGNGNYNGNGHVNGNGKANGAKVVKMKPMDSELLREQGHIMVDFI
ADYYKNLQDSPQDFPVLSQVQPGYLRDMLPDSAPERPESLKELLDDVSKKIMPGITHWQSPSYFAYYASS
TSVAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQLPDHFLSTGNGGGVIQGTGCEAVLVV
VLAARDRILKKVGKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKTDSSTNYGMPPESLEEAISH
DLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFIDGIENADSFN
MNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRL
YGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTTRYFSLVCFRLAPVDGDEDQCNERNRELLAAVNSTG
KIFISHTALSGKFVLRFAVGAPLTEEKHVTEAWQIIQKHASKFTRNDHY
>gnl|CDD|178201 PLN02591, PLN02591, tryptophan synthase
KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISML
KEVAPQLSCPIVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTP
TTPTERMKAIAEASEGFVYLVSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGW
GADGVIVGSAMVKALGEAKSPEEGLKRLEKLAKSLKAALP
>gnl|CDD|215321 PLN02592, PLN02592, ent-copalyl diphosphate synthase
SSSFSSGVPLFVAKDKRRNGNIHCRCSAISKPRTQEYADVFEVQNGLPLINKWHEIVEDDIEEEASKGSV
SNEIKERVKTVKSMLSSMEDGEISISAYDTAWVALVEDINGSGTPQFPSSLQWIANNQLSDGSWGDAYLF
SAHDRLINTLACVVALKSWNLHPEKCEKGMSFFRENICKLEDENAEHMPIGFEVAFPSLLEIAKNLDIEV
PYDSPVLKEIYAQRNLKLTRIPKDIMHKVPTTLLHSLEGMPGLDWEKLLKLQCQDGSFLFSPSSTAFALM
QTKDENCLEYLNKAVQRFNGGVPNVYPVDLFEHIWAVDRLQRLGISRYFEPEIKECIDYVHRYWTENGIC
WARNSHVHDIDDTAMGFRLLRLHGHQVSADVFKHFEKGGEFFCFAGQSTQAVTGMFNLYRASQVLFPGEK
ILENAKEFSSKFLREKQEANELLDKWIIMKDLPGEVGFALEIPWYASLPRVETRFYIEQYGGEDDVWIGK
TLYRMPYVNNNEYLELAKLDYNNCQALHQLEWDNFQKWYEECNLGEFGVSRSELLLAYFLAAASIFEPER
SHERLAWAKTTVLVEAISSYFNKETSSKQRRAFLHEFGYGYKINGRRSDHHFNDRNMRRSGSVKTGEELV
GLLLGTLNQLSLDALEAHGRDISHLLRHAWEMWLLKWLLEGDGRQGEAELLVKTINLTAGRSLSEELLAH
PQYEQLAQLTNRICYQLGHYKKNKVHINTYNPEEKSKTTPSIESDMQELVQLVLQNSSDDIDPVIKQTFL
MVAKSFYYAAYCDPGTINYHIAKVLFERVA
>gnl|CDD|178203 PLN02593, PLN02593, adrenodoxin-like ferredoxin protein
ISVTFVDKDGEERTVKAPVGMSLLEAAHENDIELEGACEGSLACSTCHVIVMDEKVYNKLPEPTDEENDM
LDLAFGLTETSRLGCQVIAKPELDGMRLALPAATRNFAVDGHVPKPH
>gnl|CDD|215322 PLN02594, PLN02594, phosphatidate cytidylyltransferase
ILMARELFNLARKAREERQLPGFRLLNWHFFFTAMFFVYGRFLKQQLVNTVTSDKFLYRLVSGLIKYHMA
ICYSLYIAGFVWFILTLKKGMYKYQFGQYAWTHMILIVVFTQSSFTVANIFEGIFWFLLPASLIVINDIA
AYLFGFFFGRTPLIKLSPKKTWEGFIGASVTTLISAFYLANIMGKFQWLTCPRKDLSTGWLECDPDPLFK
PETYPLPGWIPRWFPWKEVSVLPVQWHALSLGLFASIIAPFGGFFASGFKRAFKIKDFGDSIPGHGGITD
RMDCQMVMAVFAYIYYQSFIVPQSVSVGKLLDQILTLLTDEEQKELYVKLGQMLQERGLGLG
>gnl|CDD|178205 PLN02595, PLN02595, cytochrome c oxidase subunit VI protein
MATAIVRSALSRAVTRAAPKTSVAPKRNFSSSAGHDDAYEAAKWEKITYLGIASCTALAVYVLSKGHHHG
EDPPAYPYMHIRNKEFPWGPDGLFEVKHNKEH
>gnl|CDD|178206 PLN02596, PLN02596, hexokinase-like
MMRKEVVVAATVATVAAVAAAVLMGRWKRRKERQWKHTQRILRKFARECATPVSKLWEVADALVSDMTAS
LTAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIPSNVLNGT
SQELFDYIALELAKFVAEHPGDEADTPERVKKLGFTVSYPVDQAAASSGSAIKWKSFSADDTVGKALVND
INRALEKHGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSPSPESQEIV
ISTEWGNFNSCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLT
TPYLLRSPDMAAMHQDTSEDHEVVNEKLKEIFGITDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKK
LGRIENKKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSELSDNVVIEHSHGGSGAGALFLAACQTGEPDS
>gnl|CDD|178207 PLN02597, PLN02597, phosphoenolpyruvate carboxykinase [ATP]
PKVVRGDPARKKEPPKSVVAPTIDVSDSGLKFTHVLYNLSPAELYEQAIKYEKGSFITSTGALATLSGAK
TGRSPKDKRVVRDETTEDELWWGKGSPNIEMDEETFLVNRERAVDYLNSLDKVFVNDQFLNWDPENRIKV
RIVSARAYHSLFMHNMCIRPTPEELEDFGTPDFTIYNAGQFPCNRYTHYMTSSTSIDLNLKRKEMVILGT
QYAGEMKKGLFSLMHYLMPMRGILSLHSGCNMGKDGDVALFFGLSGTGKTTLSTDPNRYLIGDDEHCWSD
NGVSNIEGGCYAKCIDLSEEKEPDIWNAIKFGTVLENVVFDEHTREVDYSDKSVTENTRASYPIEYIPNA
KIPCVGPHPKNVILLACDAFGVLPPVSKLTLAQTMYHFISGYTALVAGTEDGIKEPTATFSACFGAAFIM
LHPTKYAAMLAEKMQKHGATAWLVNTGWSGGSYGVGKRMSLAYTRKIIDAIHSGSLLNAEYVKTPIFGLE
VPTEIEGVPSEILDPENTWSDKKAYDETLNKLAGLFKKNFEVFADYKIGVDGKLTEEILAAGPKF
>gnl|CDD|215323 PLN02598, PLN02598, omega-6 fatty acid desaturase
MASRIADAVFAFSGSQRALVRRAKLPAFLRLAAAARKRRQGNIQAVAVPVAPPSAEERKQLAESYGFTQI
GEPLPDNVTLKDVVKTLPKEVFEIDDFKAWKTVAITVTSYALGLAAIAVAPWYLLPLAWAWLGTAITGFF
VIGHDCGHNSFSKNQLVEDIVGTIAFTPLIYPFEPWRIKHNTHHAHTNKLVMDTAWQPFRPHQFDNADPL
RKAMMRAGMGPLWWWASIGHWLFWHFDLNKFRPQEVPRVKISLAAVFAFMALGLPPLLYTTGPVGFVKWW
LMPWLGYHFWMSTFTMVHHTAPHIPFKQAREWNAAQAQLNGTVHCDYPAWIEFLCHDISVHIPHHISSKI
PSYNLRKAHASLQENWGKHLNKATFNWRLMKTILTQCHVYDKEKNYVPFDNLAPEESQPIAFLRKVMPDY
A
>gnl|CDD|178209 PLN02599, PLN02599, dihydroorotase
AVATAGRSRASISSASAAEGTELTITRPDDWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTAR
ALAYRERIMKALPPGSSFEPLMTLYLTDNTTPEEIKAAKASGVVFAVKLYPAGATTNSQAGVTDLGKCLP
VLEEMAEQGMPLLVHGEVTDPSVDIFDREKVFIDTILAPLVQKLPQLKIVMEHITTMDAVEFVESCGDGN
VAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGSKKFFLGTDSAPHPKRAKEASC
GCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVPEAYSFGGGTVV
PMFAGETIPWSVVS
>gnl|CDD|178210 PLN02600, PLN02600, enoyl-CoA hydratase
PDSGIVELRLDRPEAKNAIGKEMLRGLRSAFEKIQADASARVVMLRSSVPGVFCAGADLKERRKMSPSEV
QKFVNSLRSTFSSLEALSIPTIAVVEGAALGGGLELALSCDLRICGEEAVFGLPETGLAIIPGAGGTQRL
PRLVGRSRAKELIFTGRRIGAREAASMGLVNYCVPAGEAYEKALELAQEINQKGPLAIKMAKKAINEGSE
VDMASGLEIEEECYEQVLKTKDRLEGLAAFAEKRKPVYTGK
>gnl|CDD|178211 PLN02601, PLN02601, beta-carotene hydroxylase
MAAGLSTIAVTLKPLHRSDFRLNHPISLAVFPPSLRFNGFRRRKILTVCFVVEERKQSSPMENDEKPEST
TSSSEILMTSRLLKKAEKKKSERFTYLIAAVMSSFGITSMAIMAVYYRFSWQMKGGEVSMLEMFGTFALS
VGAAVGMEFWARWAHRALWHDSLWNMHESHHKPREGAFELNDVFAIVNAVPAIGLLYYGFFNKGLVPGLC
FGAGLGITVFGMAYMFVHDGLVHKRFPVGPIANVPYLRKVAAAHQLHHTDKFKGVPYGLFLGPKEVEEVG
GKEELEKEISRRIKLYNKGSSTS
>gnl|CDD|178212 PLN02602, PLN02602, lactate dehydrogenase
MKKSSSASSLGPGGLDLSQAFFKPIHNSSPPSPTRRHTKVSVVGVGNVGMAIAQTILTQDLADELALVDV
NPDKLRGEMLDLQHAAAFLPRTKILASTDYAVTAGSDLCIVTAGARQIPGESRLNLLQRNVALFRKIIPE
LAKYSPDTILLIVSNPVDVLTYVAWKLSGFPANRVIGSGTNLDSSRFRFLIADHLDVNAQDVQAYIVGEH
GDSSVALWSSVSVGGVPVLSFLEKQQIAYEKETLEEIHRAVVDSAYEVIKLKGYTSWAIGYSVASLVRSL
LRDQRRIHPVSVLAKGFHGIDEGDVFLSLPAQLGRNGVLGVVNVHLTDEEAERLRKSAKTLWEVQSQLGL
>gnl|CDD|178213 PLN02603, PLN02603, asparaginyl-tRNA synthetase
AMAAAAPATSLRLTPGSTLRRLSFPPKSNPSALSLPLPPTFHHLAALSGLPRRRRFCAAASASLQSPESA
KVEAAKGAFGEAVGEFRKKLRIADVKGGEDEGLARVGKTLNVMGWVRTLRAQSSVTFIEVNDGSCLSNMQ
CVMTPDAEGYDQVESGLITTGASVLVQGTVVSSQGGKQKVELKVSKIVVVGKSDPSYPIQKKRVSREFLR
TKAHLRPRTNTFGAVARVRNALAYATHKFFQENGFVWVSSPIITASDCEGAGEQFCVTTLIPNSAENGGS
LVDDIPKTKDGLIDWSQDFFGKPAFLTVSGQLNGETYATALSDVYTFGPTFRAENSNTSRHLAEFWMIEP
ELAFADLNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKGIIDRLSDVVEKNFVQLSYTDAIELLLK
AKKKFEFPVKWGLDLQSEHERYITEEAFGGRPVIIRDYPKEIKAFYMRENDDGKTVAAMDMLVPRVGELI
GGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVP
GSAEF
>gnl|CDD|215324 PLN02604, PLN02604, oxidoreductase
TMRFLALFFLLFSVLNFPAAEARIRRYKWEVKYEYKSPDCFKKLVITINGRSPGPTILAQQGDTVIVELK
NSLLTENVAIHWHGIRQIGTPWFDGTEGVTQCPILPGETFTYEFVVDRPGTYLYHAHYGMQREAGLYGSI
RVSLPRGKSEPFSYDYDRSIILTDWYHKSTYEQALGLSSIPFDWVGEPQSLLIQGKGRYNCSLVSSPYLK
AGVCNATNPECSPYVLTVVPGKTYRLRISSLTALSALSFQIEGHNMTVVEADGHYVEPFVVKNLFIYSGE
TYSVLVKADQDPSRNYWVTTSVVSRNNTTPPGLAIFNYYPNHPRRSPPTVPPSGPLWNDVEPRLNQSLAI
KARHGYIHPPPLTSDRVIVLLNTQNEVNGYRRWSVNNVSFNLPHTPYLIALKENLTGAFDQTPPPEGYDF
ANYDIYAKPNNSNATSSDSIYRLQFNSTVDIILQNANTMNANNSETHPWHLHGHDFWVLGYGEGKFNMSS
DPKKYNLVDPIMKNTVPVHPYGWTALRFRADNPGVWAFHCHIESHFFMGMGVVFEEGIERVGKLPSSIMG
CGESKG
>gnl|CDD|215325 PLN02605, PLN02605, monogalactosyldiacylglycerol synthase
VLILMSDTGGGHRASAEAIKDAFQLEFGDEYQVFIVDLWKEHTPWPFNQLPRSYKFLVKHPQLWKMTYHG
TNPRLIHQSYFAATSAFVAREVAKGLMKYKPDIIVSVHPLMQHVPLRVLRWQGKELGKKIPFTTVVTDLG
TCHPTWFHKGVTRCFCPSEEVAKRALKRGLEPSQIRVYGLPIRPSFARAVRPKDELRRELGMDEDLPAVL
LMGGGEGMGPLEETARALGDSLYDKNLGKPIGQVVVICGRNKKLQSKLESRDWKIPVKVRGFVTNMEEWM
GACDCIITKAGPGTIAEALIRGLPIILNGYIPGQEEGNVPYVVDNGFGAFSESPKEIARIVAEWFGDKSD
ELEAMSENALKLARPEAVFDIVHDLHELVRQR
>gnl|CDD|215326 PLN02606, PLN02606, palmitoyl-protein thioesterase
MEKSFQRSALLVTLSLFFFSIPVSLSVPFVLFHGFGGECSNGKVSNLTQFLINHSGYPGTCVEIGNGVQD
SLFMPLRQQASIACEKIKQMKELSEGYNIVAESQGNLVARGLIEFCDNAPPVINYVSLGGPHAGVAAIPK
GCNSTFCELLKAVFAVIYTDFAQDHTAPSGYVKKPMEIKNYLEHSKYLPKLNNERPGERNPTFKDRFTSL
HNLVLVMFQGDTVLIPRETSWFGYYPDGASTPLLSPQSTKLYTEDWIGLKTLDDAGKVKFISVPGGHIEI
AEEDLVKYVVPYLQNESAFMSEHEEI
>gnl|CDD|215327 PLN02607, PLN02607, 1-aminocyclopropane-1-carboxylate synthase
MMAIEIAQPAVGLSKVAVSETHGEDSPYFAGWKAYDEDPYDESHNPSGVIQMGLAENQVSFDLLEEYLKQ
HPEASSWGGKGAPGFRENALFQDYHGLKSFRQAMASFMEQIRGGKARFDPDRIVLTAGATAANELLTFIL
ADPGDALLVPTPYYPGFDRDLRWRTGVKIVPIHCDSSNNFQVTPQALEAAYQEAEAANIRVRGVLITNPS
NPLGATVQRSVLEDILDFVVRKNIHLVSDEIYSGSVFSASEFVSVAEIVEARGYKGVAERVHIVYSLSKD
LGLPGFRVGTIYSYNDKVVTTARRMSSFTLVSSQTQHLLASMLSDEEFTENYIRTNRERLRKRYEMIVQG
LRRAGIECLKGNAGLFCWMNLSPLLETPTREGELALWDSILREVKLNISPGSSCHCSEPGWFRVCFANMS
EDTLEVALKRIHRFMDRRKTASSQQQE
>gnl|CDD|178218 PLN02608, PLN02608, L-ascorbate peroxidase
MAAPVVDAEYLKEIEKARRDLRALIASKNCAPIMLRLAWHDAGTYDAKTKTGGPNGSIRNEEEYSHGANN
GLKIAIDLCEPVKAKHPKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNACPEEGRLPDAKKGAKHLR
DVFYRMGLSDKDIVALSGGHTLGRAHPERSGFDGPWTKEPLKFDNSYFVELLKGESEGLLKLPTDKALLE
DPEFRPYVELYAKDEDAFFRDYAESHKKLSELGFTPPSSAFKKKSTSTSTVLAQSAVGVAVAAAVVILSY
FYEVRKKMK
>gnl|CDD|215328 PLN02609, PLN02609, catalase
MDPYKYRPSSAYNSPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGAS
AKGFFEVTHDISNLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNF
PVFFIRDGMKFPDMVHALKPNPKTHIQEPWRILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTY
KLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQDLYDSIAAGNYPEWKLFIQTMDPEDED
KFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGIYYSDDKLLQTRIFAYAD
TQRHRLGPNYLQLPVNAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRFDPVRHAERVPIPHPPLSGRREKC
KIEKENNFKQPGERYRSWSPDRQERFIKRWVDALSDPRVTHEIRSIWISYWSQCDKSLGQKLASRLNVKP
SM
>gnl|CDD|215329 PLN02610, PLN02610, probable methionyl-tRNA synthetase
MEDEGKSPPKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTA
TETKALEENCTPKEICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQL
YCDTCQKFLADRLVEGTCPTEGCNYDSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELP
LLKDKLVEYINETSVAGGWSQNAIQTTNAWLRDGLKPRCITRDLKWGVPVPLEKYKDKVFYVWFDAPIGY
VSITACYTPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTLLGTGENWTMMKTISVTEYLNYEGGKFS
KSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLNNLGNFINRVLSFIAKPP
GAGYGSVIPDAPGAESHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQESQFWKLY
KEDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLSLSDEKGEVARAKRPWELVPAGH
KIGTPEPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKLAKQLKKKALSDGGKKKQGKKAGGGGKS
KAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLEEMQNRKVCVLCN
LKPAAMRGIKSQAMVLAASNSDHTKVELVEPPESAAVGERVTFPGFEGEPDDVLNPKKKVWETLQPDLHT
NSELVACYKDVPFTTSAGVCKVASIANGSIR
>gnl|CDD|178221 PLN02611, PLN02611, glutamate--cysteine ligase
MALVSAAGRARHVSAPSSDSRRRTTRRGRSVIVAASPPTEEAVVATEPLTKEDLVAYLASGCKPKEKWRI
GTEHEKFGFELATLRPMKYDQIAQLLEGLAERFGWEKIMEGDNIIGLKQDGQSVSLEPGGQFELSGAPLE
TLHQTCAEVNSHLYQVKAVAEEMGIGFLGIGFQPKWSVADIPIMPKGRYKIMRNYMPKVGSLGLDMMFRT
CTVQVNLDFSSEQDMVRKFRVGLALQPIATALFANSPFTEGKPNGYLSYRSHIWTDTDKDRTGMLPFVFD
DDFGFERYVDYALDVPMYFVYRNGKYIDCTGMSFRDFMAGKLPQLPGELPTLNDWENHLTTIFPEVRLKR
YLEMRGADGGPWRRLCALPAFWVGLLYDEESLQSALDMIADWTPEEREMLRNKVPKTGLKTPFRDGTLKD
VAEEVLKLAKDGLERRGYNEEGFLNALAEIVRTGVTPAERLLELYEGKWGRSVDPVFEELLY
>gnl|CDD|215330 PLN02612, PLN02612, phytoene desaturase
VVFGNVSALNLSWHSGFLDAQALAFRGSESMGHSLRVPTSSSSRTRRRRNSGRGPLQVVCVDYPRPELEN
TVNFLEAAALSASFRSAPRPAKPLKVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKVAAWKDEDG
DWYETGLHIFFGAYPNVQNLFGELGINDRLQWKEHSMIFAMPNKPGEFSRFDFPEVLPAPLNGIWAILRN
NEMLTWPEKIKFAIGLLPAIVGGQAYVEAQDGLSVKEWMRKQGVPDRVNDEVFIAMSKALNFINPDELSM
QCILIALNRFLQEKHGSKMAFLDGNPPERLCMPIVDHFQSLGGEVRLNSRIKKIELNDDGTVKHFLLTNG
SVVEGDVYVSATPVDILKLLLPDQWKEIPYFKKLDKLVGVPVINVHIWFDRKLKNTYDHLLFSRSPLLSV
YADMSTTCKEYYDPNKSMLELVFAPAEEWISRSDEDIIDATMKELAKLFPDEISADQSKAKILKYHVVKT
PRSVYKTVPNCEPCRPLQRSPIEGFYLAGDYTKQKYLASMEGAVLSGKLCAQSIVQDYELLAARGPRKLS
EATVSSS
>gnl|CDD|215331 PLN02613, PLN02613, endoglucanase
MGKLLVLMLVGMFLAFESLVALESPDYGDALNKSILFFEGQRSGKLPTNQRVKWRADSALSDGKPENVNL
TGGYYDAGDNVKFGWPMAFTVTLLSWAAIEYQNEISSVNQLGYLRSAIRWGTDFILRAHTSPTTLYTQVG
DGNADHQCWERPEDMDTPRTLYKITSSSPGSEAAGEAAAALAAASLVFKDVDSSYSSKLLNHARSLFEFA
DKYRGSYQASCPFYCSYSGYQDELLWAAAWLYKATGEKKYLNYVISNKGWSQAVNEFSWDNKFAGAQALL
ASEFYGGANDLAKFKTDVESFVCALMPGSSSVQIKTTPGGLLFTRDSSNLQYVTTATTVLFIYSKTLTKA
GVGGIQCGSAQFSASQIRNFAKSQVDYILGNNPMKMSYMVGFGTKYPTQIHHRGSSIPSIQVLPEKVDCN
GGFSSYYNSDTPNPNVHVGAIVGGPDSNDQYSDKRSDYSHAEPTTYINAAFVGSVAALIKQVSRLEEPTD
SSSSVDSV
>gnl|CDD|166255 PLN02614, PLN02614, long-chain acyl-CoA synthetase
MSQQKKFIFQVEEGKEGSDGRPSVGPVYRSIFAKDGFPNPIEGMDSCWDVFRMSVEKYPNNPMLGRREIV
DGKPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGA
GAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLG
EGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAALTVKDVYLSYLPLAH
IFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDS
AFSYKFGNMKKGQSHVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGL
TESCAGTFVSLPDELDMLGTVGPPVPNVDIRLESVPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTK
EVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLV
AIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERD
LLTPTFKKKRPQLLKYYQSVIDEMYKTTNEKLASRG
>gnl|CDD|178224 PLN02615, PLN02615, arginase
MVAIGRRGIHYLQRLIAASVPASLLEKGQNRVIDASLTLIRERAKLKGELVRALGGAKASSCLLGVPLGH
NSSFLQGPAFAPPRIREAIWCGSTNSTTEEGKELNDPRVLTDVGDVPVQEIRDCGVDDDRLMNVISESVK
LVMEEEPLRPLVLGGDHSISYPVVRAVSEKLGGPVDILHLDAHPDIYHAFEGNKYSHASSFARIMEGGYA
RRLLQVGIRSITKEGREQGKRFGVEQYEMRTFSKDREKLENLKLGEGVKGVYISIDVDCLDPAFAPGVSH
IEPGGLSFRDVLNILHNLQGDVVGADVVEFNPQRDTVDGMTAMVAAKLVRELTAKMSK
>gnl|CDD|215332 PLN02616, PLN02616, tetrahydrofolate dehydrogenase/cyclohydrolase, putative
MASLMFTDCSSSTTSRLIHFNRISTPFNGTFLLRRCVGPLRVRTTASGRGCCINSSSSPSPVINADTGSE
GGAKVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRL
PEDSTEQEVLKFISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLF
VPCTPKGCIELLHRYNVEIKGKRAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIIS
AVGQPNMVRGSWIKPGAVVIDVGINPVEDASSPRGYRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLL
SNTLTSAKRIHNFQ
>gnl|CDD|178226 PLN02617, PLN02617, imidazole glycerol phosphate synthase hisHF
ASNSADSEVTLLDYGAGNVRSVRNAIRHLGFTIKDVQTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAE
ALREYIQNDRPFLGICLGLQLLFESSEENGPVEGLGVIPGVVGRFDSSNGLRVPHIGWNALQITKDSELL
DGVGGRHVYFVHSYRATPSDENKDWVLATCNYGGEFIASVRKGNVHAVQFHPEKSGATGLSILRRFLEPK
SSATQKPTEGKASKSLAKRVIACLDVRSNDKGDLVVTKGDQYDVREHSEGREVRNLGKPVELAGQYYKDG
ADEVAFLNITGFRDFPLGDLPMLEVLRRASENVFVPLTVGGGIRDFTDANGRYYSSLEVASEYFRSGADK
ISIGSDAVYAAEEYIASGVKTGKTSIEQISRVYGNQAVVVSIDPRRVYVKDPSDVPFKTVKVTNPGPNGE
EYAWYQCTVKGGREGRPIGAYELAKAVEELGAGEILLNCIDCDGQGKGFDIELVKLVSDAVTIPVIASSG
AGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETRI
>gnl|CDD|215333 PLN02618, PLN02618, tryptophan synthase, beta chain
EPPGSDPTGFQRPDSFGRFGKFGGKYVPETLMTALSELEAAFNALATDPEFQEELAGILKDYVGRETPLY
FAERLTEHYKRADGEGPEIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCA
RFGLECIVYMGAQDMERQALNVFRMRLLGAEVRPVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGP
HPYPMMVRDFHSVIGKETRRQAMEKWGGKPDVLVACVGGGSNAMGLFHEFIDDEDVRLIGVEAAGFGLDS
GKHAATLTKGEVGVLHGAMSYLLQDEDGQIIEPHSISAGLDYPGVGPEHSFLKDTGRAEYYSVTDEEALE
AFQRLSRLEGIIPALETSHALAYLEKLCPTLPDGTKVVVNCSGRGDKDVNTAIKYLQVSS
>gnl|CDD|178228 PLN02619, PLN02619, nucleoside-diphosphate kinase
MSSQICRSASRAARSLLSSAKNASFLSEGRAVAAAAAVSAGGKPPLLASAFGRATGSSTASAQWISGALA
LPAAVYMLQEQEAHAAEMERTFIAIKPDGVQRGLISEIISRFERKGFKLVAIKVVVPSKEFAQKHYHDLK
ERPFFNGLCDFLSSGPVVAMVWEGEGVIKYGRKLIGATDPQKSEPGTIRGDLAVVVGRNIIHGSDGPETA
KDEINLWFKPEELVSYTSNAEKWIYGVN
>gnl|CDD|166261 PLN02620, PLN02620, indole-3-acetic acid-amido synthetase
MPEAPKNSLLEVGDYNLAEKNKKALQFIEDVTSNADEVQKRVLEEILSRNAHVEYLQRHGLNGRTDRETF
KKVMPVITYEDIQPDINRIANGDTSPILCSKPISEFLTSSGTSGGERKLMPTIEEELGRRSLLYSLLMPV
MSQFVPGLEKGKGMYFLFIKSEAKTPGGLVARPVLTSYYKSSHFKDRPYDPYTNYTSPNETILCPDSYQS
MYSQMLCGLCQHKEVLRVGAVFASGFIRAIRFLEKHWTLLCRDIRTGTIDSQITDPSVREAVMKILKPDP
KLADFVEAECRKESWQGIITRLWPNTKYVDVIVTGTMSQYIPTLDYYSNGLPLVCTMYASSECYFGVNLN
PLCKPSEVSYTLIPTMAYFEFLPVHRNNGVTNSISLPKSLNEKEQQELVDLVDVKLGQEYELVVTTYAGL
YRYRVGDVLRVAGFKNKAPQFSFICRKNVVLSIDSDKTDEVELQNAVKNAVNHLVPFDASLTEYTSYADT
STIPGHYVLFWELCLNGSTPIPPSVFEDCCLTIEESLNSVYRQGRVSDKSIGPLEIKIVEPGTFDKLMDY
AISLGASINQYKTPRCVKFAPIIELLNSRVVSNYFSPKCPKWVPGHKQWCSN
>gnl|CDD|178229 PLN02621, PLN02621, nicotinamidase
MAASSYKKYETRKRDPDPKQAALLVIDMQNYFSSMAEPILPALLTTIDLCRRASIPVFFTRHSHKSPSDY
GMLGEWWDGDLILDGTTEAELMPEIGRVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLC
CETTAREAFVRGFRVFFSTDATATANEELHEATLKNLAYGFAYLVDCDRLEAGLLKK
>gnl|CDD|166263 PLN02622, PLN02622, iron superoxide dismutase
CNSSVPTSSCFVTDSDLSIRLKSPKLLNLRNKQRRRSLQRASKVVAYYGLKTPPYPLDALEPYMSRRTLE
VHWGEHHRGYVEGLNKQLAKDDILYGYTMDELVKVTYNNGNPLPEFNNAAQVWNHDFFWESMQPGGGDMP
ELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREERRLEVVKTSNAINPLVWDDIPIICLDV
WEHAYYLDYKNDRGKYVNAFMNHLVSWNAAMARMARAEAFVNLGEPKIPIA
>gnl|CDD|215334 PLN02623, PLN02623, pyruvate kinase
AAAQVVATRSIDSSILSSSSGSVSLDLLSPLSFASKVLGSEARARRRVAVRRRAVTAASLRSKSQETEVI
PVSPEDGGANFVEDNEEVLLEIQQLGETAVGMWSKPSVRRKTKIVCTIGPSTNTREMIWKLAEAGMNVAR
LNMSHGDHASHQKVIDLVKEYNAQSKDNVIAIMLDTKGPEVRSGDLPQPIMLEEGQEFTFTIKRGVSTED
CVSVNYDDFVNDVEVGDMLLVDGGMMSLAVKSKTSDSVKCEVVDGGELKSRRHLNVRGKSATLPSITEKD
WEDIKFGVENKVDFYAVSFVKDAQVVHELKDYLKSCNADIHVIVKIESADSIPNLHSIITASDGAMVARG
DLGAELPIEEVPLLQEEIIRRCRSMGKPVIVATNMLESMIVHPTPTRAEVSDIAIAVREGADAVMLSGET
AHGKFPLKAVKVMHTVALRTEATLPEGTTPPNLGQAFKNHMSEMFAFHATMMANTLGTSIIVFTRTGFMA
ILLSHYRPSGTIFAFTNEKRIQQRLALYQGVCPIYMQFSDDAEETFARALSLLLNKGMVKEGEEVALVQS
GRQPIWRSESTHHIQVRKVQA
>gnl|CDD|215335 PLN02624, PLN02624, ornithine-delta-aminotransferase
SMALARRLLQRLARRSRRLRRRSYGALPEGSAPSLSDSSAHLIELEEKYSAHNYHPIPVVFSRAKGSRIW
DPEGKKYLDFLSAYSAVNQGHCHPKIIKALTEQAEKLTLSSRAFYNDKFPEFAEYLTSMFGYDMVLPMNT
GAEGVETAIKLARKWGYEKKGIPKNEAIIVSCCGCFHGRTLAAISMSCDNEATRGFGPLLPGHLKVDFGD
LDALEKIFEEDGDRIAAFLFEPIQGEAGVVIPPDGYLKAVRELCSKHNVLMIADEIQTGLARTGKMLACD
WEEVRPDVVILGKALGGGVIPVSAVLADKDVMLCIKPGEHGSTFGGNPLASAVAMAALQVVQDEKLAERS
AKLGQELRDQLQKIQKQFPKLIKEVRGRGLLNAVVLNSPKLGPVSAYDVCLKLKERGLLAKPTHDTIIRL
APPLSISEDELQECSKALSDVLEHDLPKLQSAKKEKTPKAAPTPCDRCGRNLYA
>gnl|CDD|178232 PLN02625, PLN02625, uroporphyrin-III C-methyltransferase
ENDIASQLPELEGPGNVFLVGTGPGDPDLLTLKALRLLQTADVVLYDRLVSPDILDLVPPGAELLYVGKR
GGYHSRTQEEIHELLLSFAEAGKTVVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELG
IPLTHRGVATSVRFLTGHDREGGTDPLDVAEAAADPDTTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAV
ERGTTPEQRVVFGTLEDIAEDVAAAGLVSPTVIVVGEVVALSPLWPWAAEESS
>gnl|CDD|215336 PLN02626, PLN02626, malate synthase
SKVEAYDAPVGVRIRGPYDAEFAKILTRDALQFVADLQREFRPRRKYLLECRREAQRRYDAGALPGFDPA
TRAVREGDWRCAPVPPAVADRRVEITGPVERKMVINALNSGAKVFMADFEDSLSPTWENLMRGQVNLRDA
VRGTITFTDKARGKVYKLNDKTAKLFVRPRGWHLPEAHILVDGEPATGSLFDFGLYFFHNYAAFRAKQGG
FGPFFYLPKMEHSREARLWNDVFEAAEKMAGIPRGSIRATVLIETLPAVFQMEEILYELRDHSAGLNCGR
WDYIFSFVKTFRAHPDRLLPDRVQVGMTQHFMKSYVDLLIKTCHKRGVHAMGGMAAQIPIKDDPAANEAA
LALVRKDKLREVRAGHDGTWAAHPGLIPLAMEVFDGHMPTPNNQQLHKRRDDVNVTEADLLQVPRGVRTL
EGLRLNTRVGIQYLAAWLTGTGSVPLYNLMEDAATAEISRVQNWQWIKYGAELDGDGVGVRVTAELFGRV
VEEEMARIEREVGKERFKKGKYKEAAKLFARQCTAPELDDFLTLDAYNHIVTHHPDGSSRL
>gnl|CDD|178234 PLN02627, PLN02627, glutamyl-tRNA synthetase
AMSLVGGTPIRLLPELAPPFLRRSRSSRRRFSVRAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNY
LFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPYRQSERNAIYKQYAEKL
LESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEGSVKIDD
LIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRF
AHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINK
SGAVFDSTKLKWMNGQHLRLLPEEELVKLVGERWKSAGILKESDGSFVKEAVELLKDGIELVTDADKELL
NLLSYPLAATLSSPEAKTVVEDNFSEVADALIAAYDSGELAAALEEGHDGWQKWVKAFGKALKRKGKRLF
MPLRVALTGKMHGPDVGESLVLLHKAGTPDSVTEQAGFVPLEDRF
>gnl|CDD|215337 PLN02628, PLN02628, fructose-1,6-bisphosphatase family protein
MASAPPLYTAARGAEGVCTLMEFLGTEGSNVGDDLVVLMAHIQAACKRIAALLASPFNSELGKTSSGASG
ASGSGRDAPKPLDIVSNEIILSSLRNSGKVAVMASEEDDAPIWIGDDGPYVVVFDPLDGSRNIDASIPTG
TIFGIYNRLVEADHLPVEEKAQLNVLQRGSRLVAAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTH
PDIKIPERGQIYSVNDARYFDWPEGLRKYIDTVRQGKGQYPKKYSARYICSLVADLHRTILYGGIAMNPR
SHLRLVYEANPLSFLVEQAGGRGSDGKRRILSIQPVKLHQRLPLFLGSSEDVLELESYGDVQQKVNPGYE
V
>gnl|CDD|215338 PLN02629, PLN02629, powdery mildew resistance 5
SSCLLLGSCFSFLFFLVLLQPEIASSALILSLKNHHNHHSNRRPSLQANQSTCALFVGTWVRDDSYPLYQ
SSDCPGVIDPEFNCQMYGRPDSDYLKYRWQPLNCELPRFNGLEFLLKMKGKTVMFVGDSLGRNQWESLIC
LISSSVPSTRTQMSRGDPLSTFKFLDYGVSISFYKAPYLVDIDAVQGKRVLKLEEISGNANAWRDADVLI
FNTGHWWSHQGSLQGWDYIESGGTYYQDMDRLVALEKALRTWAYWVDTNVDRSRTRVFFQSISPTHYNPS
EWSAGASTTTKNCYGETTPMSGMTYPGAYPDQMRVVDEVIRGMHNPAYLLDITLLSELRKDGHPSIYSGD
LSPSQRANPDRSADCSHWCLPGLPDTWNQLFYTALFF
>gnl|CDD|178237 PLN02630, PLN02630, pfkB-type carbohydrate kinase family protein
MTNHSKRPIPQRRVLIVGNYCHDVLIQNGSVTAESLGGAASFISNVLDALSVECELVSKVGPDFLYQVSH
PPIVIPDSKTTEFHADFDQGIDGNGHEDRVLKRVCACDPIEPSDIPDMRYEFGMAVGVAGEILPETLERM
VEICDVVVVDIQALIRVFDPVDGTVKLVKLEETGFYDMLPRIGFLKASSEEALFIDVEEVRQKCCVIVTN
GKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVGIPKF
DLRQLQRVKDEVQRRKMQCELSFLKPNGHNQFHASLSAAKLIPVDSQQEPKLLVS
>gnl|CDD|178238 PLN02631, PLN02631, ferric-chelate reductase
MGNMRSLVKMLMVVLFLGWIFVWIMISTNLFKSKWTPKLAKNLNTTYFGPQGTNLVLLTVPMMFIAVLSC
VYLHTQKKPTQPQREWKLKRRMGRVIMVMNPLGIVTATELTFSLLFVALLAWSLYNYLYLSYHVHLHNDD
NAKIWQAKFRAFGLRIGYVGHICWAFLFFPVTRASTILPLVGLTSESSIKYHIWLGHVSNFLFLVHTVVF
LIYWAMINKLMETFAWNPTYVPNLAGTIAMVIGIAMWVTSLPSFRRKKFELFFYTHHLYGLYIVFYVIHV
GDSWFCMILPNIFLFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISK
LQWHPFTITSSSNLEKDTLSVVIRRQGSWTQKLYTHLSSSIDSLEVSTEGPYGPNSFDVSRHNSLILVSG
GSGITPFISVIRELIFQSQNPSTKLPDVLLVCSFKHYHDLAFLDLIFPLDISVSDISRLNLRIEAYITRE
DKKPETTDDHRLLQTKWFKPQPLDSPISPVLGPNNFLWLGVVILSSFVMFLLLIGIVTRYYIYPVDHNTG
SIYNFSYRGLWDMFLGSVCIFISSSIVFLWRKKQNKEGDKESKKQVQSVEFQTPTSSPGSWFHGHERELE
SVPYQSIVQATSVHFGSKPNLKKILLEAEGSEDVGVMVCGPRKMRHEVAKICSSGLAKNLHFEAISFNW
>gnl|CDD|215339 PLN02632, PLN02632, phytoene synthase
RAVAPAAASSEEKVYEVVLKQAALVRKAARRSVRPRATSLSPALLEEAYDRCGEVCAEYAKTFYLGTLLM
TPERRKAIWAIYVWCRRTDELVDGPNASHITPAALDRWEARLEDLFDGRPYDMLDAALADTVSKFPLDIQ
PFRDMIEGMRMDLVKSRYENFDELYLYCYYVAGTVGLMSVPVMGIAPESKASTESVYNAALALGIANQLT
NILRDVGEDARRGRVYLPQDELAQFGLTDEDIFAGKVTDKWRAFMKFQIKRARMYFAEAEEGVSELDPAS
RWPVWASLLLYRQILDAIEANDYDNFTKRAYVGKWKKLLALPLAYARALFPPSS
>gnl|CDD|178240 PLN02633, PLN02633, palmitoyl protein thioesterase family protein
MEKGLKRSCVMVVVAFLAMVHVSVSVPFIMLHGIGTQCSDATNANFTQLLTNLSGSPGFCLEIGNGVGDS
WLMPLTQQAEIACEKVKQMKELSQGYNIVGRSQGNLVARGLIEFCDGGPPVYNYISLAGPHAGISSLPRC
GTSGLICKIANELIKGDVYSDFIQDHLAPSGYYKIPKDVTEYLKGSKYLPKLNNEIPDQRNQTYKDRFTS
LQNLVLVKFQNDTVIVPKDSSWFGFYPDGEFEHLLSVQQTKLYTEDWIGLKTLDDAGKVKFVSVPGGHLI
MADEDVVKYVVPYLQDQQSAAQRLNRKTKEPLHP
>gnl|CDD|215340 PLN02634, PLN02634, probable pectinesterase
LTNSLNYLFALSLILFLSFHCLCFRFPLVAACSASTDDQQIQHHHHHKWVGPSGHKVITVDANGHGDFRS
VQDAVDSVPKNNTMSVTIKINAGFYREKVVVPATKPYITFQGAGRDVTAIEWHDRASDRGANGQQLRTYQ
TASVTVYANYFTARNISFKNTAPAPMPGMQGWQAVAFRISGDKAFFFGCGFYGAQDTLCDDAGRHYFKEC
YIEGSIDFIFGNGRSMYKDCELHSIASRFGSIAAHGRTCPEEKTGFAFVGCRVTGTGPLYVGRAMGQYSR
IVYAYTYFDAVVAHGGWDDWDHTSNKSKTAFFGVYNCWGPGAAAVRGVSWARELDYESAHPFLAKSFVNG
RHWIAPRDA
>gnl|CDD|215341 PLN02635, PLN02635, disproportionating enzyme
AVLSSLSLGEDLPPDYEDWLPKRDAARRRAGILLHPTSLPGPYGIGDLGDEAFRFLDWLASTGCSVWQVL
PLVPPGRKGGEDGSPYSGQDANCGNTLLISLEELVKDGLLEEDELPEPVPVGKVDFSAVAELKDPLIAKA
AERLLLSDGELKEELEDFRKDPEISSWLEDAALFAAIDNTLNAKAWWDWPEPLRDRHPAALEAIRQSHKD
FIDEFIAQQFLFQRQWQAVRSYANEKGISIIGDMPIYVGGHSADVWANRKLFLLNKTGFPLLVSGVPPDA
FSETGQLWGSPLYDWKAMAKDGYSWWAGRMRRALELYDEFRIDHFRGFAGYWAVPADAKTAMNGRWKVGP
GKSFFDAIKKAVGKIDIIAEDLGVITEDVVELRKAIGAPGMAVLQFAFGGDADNPHLPHNHEENQVVYPG
THDNDTVVGWWDKLDEEEKSKVRKYLGIADEDDIAWELIRAALSSVARTAVIPMQDVLGLDNSARMNTPA
TQAGNWAWRIGSSGIFDSLEPEAEKLRELLHLYNRLPRSLEEHEKKEE
>gnl|CDD|215342 PLN02636, PLN02636, acyl-coenzyme A oxidase
MESKNQNPRAEDDGEIAARRIQRLSLHLSPVPLPKEEQLSRLVCARSIKLSVNTEKLSLYMRGKHRDIQE
KIYEFFNSRPDLQTPVEISKDEHRELCMRQLTGLVREAGIRPMKYLVEDPAKYFAITEAVGSVDMSLGIK
LGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINTPN
DGAIKWWIGNAAVHGKFATVFARLKLPTHDSKGVSDMGVHAFIVPIRDMKTHQVLPGVEIRDCGHKVGLN
GVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSSLPTINKRFAATLGELVGGRVGLAYGSVGVLKASNT
IAIRYSLLRQQFGPPKQPEISILDYQSQQHKLMPMLASTYAFHFATEYLVERYSEMKKTHDDQLVADVHA
LSAGLKAYITSYTAKALSTCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQYKEK
FQGGTLSVTWNYLRESMNTYLSQPNPVTTRWEGEEHLRDPKFQLDAFRYRTSRLLQTAALRLRKHSKTLG
SFGAWNRCLNHLLTLAESHIESVILAKFIEAVERCPDRSTRAALKLVCDLYALDRIWKDIGTYRNVDYVA
PNKAKAIHKLTEYLSFQVRNVAKELVDAFGLPDHVTRAPIAMQSGAYSEYTQYVGF
>gnl|CDD|215343 PLN02638, PLN02638, cellulose synthase A (UDP-forming), catalytic subunit
MESEGETGAKPMKHGGGQVCQICGDNVGKTVDGEPFVACDVCAFPVCRPCYEYERKDGNQSCPQCKTKYK
RHKGSPAILGDEEEDGDADDGASDFNYPSSNQDQKQKIAERMLSWRMNSGRGEDVGAPNYDKEVSHNHIP
LLTNGQSVSGELSAASPERLSMASPGAGGKRIPYASDVNQSPNIRVVDPVREFGSPGLGNVAWKERVDGW
KMKQDKNTIPMSTGTAPSEGRGGGDIDASTDVLMDDALLNDEARQPLSRKVSIPSSRINPYRMVIVLRLV
ILCIFLHYRITNPVRNAYALWLISVICEIWFALSWILDQFPKWLPVNRETYLDRLALRYDREGEPSQLAA
VDIFVSTVDPLKEPPLVTANTVLSILAVDYPVDKVSCYVSDDGAAMLTFEALSETSEFARKWVPFCKKYN
IEPRAPEWYFAQKIDYLKDKVQPSFVKDRRAMKREYEEFKVRINGLVAKAQKVPEEGWIMQDGTPWPGNN
TRDHPGMIQVFLGHSGGLDTEGNELPRLVYVSREKRPGFQHHKKAGAMNALVRVSAVLTNGPFLLNLDCD
HYINNSKALREAMCFLMDPNLGKSVCYVQFPQRFDGIDRNDRYANRNTVFFDINLRGLDGIQGPVYVGTG
CVFNRTALYGYEPPIKPKHKKPGFLSSLCGGSRKKSSKSSKKGSDKKKSGKHVDPTVPVFNLEDIEEGVE
GAGFDDEKSLLMSQMSLEKRFGQSAVFVASTLMENGGVPQSATPESLLKEAIHVISCGYEDKTDWGSEIG
WIYGSVTEDILTGFKMHARGWRSIYCMPKRPAFKGSAPINLSDRLNQVLRWALGSVEILFSRHCPIWYGY
GGRLKWLERFAYVNTTIYPITSIPLLLYCTLPAVCLLTGKFIIPQISNIASIWFISLFLSIFATGILEMR
WSGVGIDEWWRNEQFWVIGGVSAHLFAVFQGLLKVLAGIDTNFTVTSKASDEDGDFAELYMFKWTTLLIP
PTTLLIINLVGVVAGISYAINSGYQSWGPLFGKLFFAFWVIVHLYPFLKGLMGRQNRTPTIVVVWSILLA
SIFSLLWVRIDPFTTRVTGPDVEQCGINC
>gnl|CDD|178245 PLN02639, PLN02639, oxidoreductase, 2OG-Fe(II) oxygenase family protein
MATKLLSTGIRHTTLPESYVRPESERPRLSEVSTCENVPVIDLGSPDRAQVVQQIGDACRRYGFFQVINH
GVSAELVEKMLAVAHEFFRLPVEEKMKLYSDDPTKTMRLSTSFNVRKEKVHNWRDYLRLHCYPLDKYVPE
WPSNPPSFKEIVSTYCREVRELGFRLQEAISESLGLEKDYIKNVLGEQGQHMAVNYYPPCPEPELTYGLP
AHTDPNALTILLQDQQVAGLQVLKDGKWVAVNPHPGAFVINIGDQLQALSNGRYKSVWHRAVVNTDKERM
SVASFLCPCDDAVISPAKKLTDDGTAAVYRDFTYAEYYKKFWSRNLDQEHCLELFKN
>gnl|CDD|215344 PLN02640, PLN02640, glucose-6-phosphate 1-dehydrogenase
MATHFMSPCSSSSTNFLASSCFKETVPLFSRSITFPRKSTFVSQIHSRIHARKHFQLKSSNGHPLNAVSL
QDGENHLTEEHAEKGESTLSITVVGASGDLAKKKIFPALFALFYEDWLPENFTVFGYARTKLTDEELRDM
ISSTLTCRIDQRENCGDKMDQFLKRCFYHSGQYDSEEDFAELNKKLKEKEAGKLSNRLFYLSIPPNIFVD
VVRCASLRASSENGWTRVIVEKPFGRDSESSGELTRCLKQYLTEEQIFRIDHYLGKELVENLSVLRFSNL
VFEPLWSRNYIRNVQLIFSEDFGTEGRGGYFDNYGIIRDIMQNHLLQILALFAMETPVSLDAEDIRNEKV
KVLRSMKPLQLEDVIVGQYKGHSKGGKSYPAYTDDPTVPKHSLTPTFAAAALFINNARWDGVPFLMKAGK
ALHTRRAEIRVQFRHVPGNLYKRNFGTDLDKATNELVLRVQPDEAIYLKINNKVPGLGMRLDRSDLNLLY
RARYPREIPDAYERLLLDAIEGERRLFIRSDELDAAWALFTPLLKELEEKKIIPELYPYGSRGPVGAHYL
AAKYNVRWGDLSE
>gnl|CDD|215345 PLN02641, PLN02641, anthranilate phosphoribosyltransferase
IASFRQLIESLIQGTDLTEEEAEAALDFLLDDADEAQISAFLVLLRAKGETFEEIAGLARAMIKRARKVD
GLVDAVDIVGTGGDGANTVNISTGSSILAAACGAKVAKQGNRSSSSACGSADVLEALGVAIDLGPEGVKR
CVEEVGIGFMMAPKYHPAMKIVAPVRKKLKVKTVFNILGPMLNPARVPHAVVGVYHESLVEKMAKALQRF
GMKRALVVHSEGLDEMSPLGPGDVLEVTPEKIEEFSFDPLDFGIPRCTLEDLRGGDPDYNAKVLRDVLSG
EKGAIADALILNAAAALLVSGLAKTLAEGVALARETQESGKAIKTLDSWIKISQELKAAEKVA
>gnl|CDD|178248 PLN02642, PLN02642, copper, zinc superoxide dismutase
MEAPRGNLRAVALIAGDNNVRGCLQFVQDIFGTTHVTGKISGLSPGFHGFHIHSFGDTTNGCISTGPHFN
PLNRVHGPPNEEERHAGDLGNILAGSDGVAEILIKDKHIPLSGQYSILGRAVVVHADPDDLGKGGHKLSK
STGNAGSRVGCGIIGLQSSADAKL
>gnl|CDD|215346 PLN02643, PLN02643, ADP-glucose phosphorylase
MAELRKDPVTNRWVIFSPARGKRPTDFKSKSPQNPNGNHSSGCPFCIGHEHECAPEIFRVPDDASAPDWK
VRVIENLYPALSRDLEPPCTEGQGEDYGGRRLPGFGFHDVVIETPVHSVQLSDLPARHIGEVLKAYKKRI
NQLQSDSRFKYVQVFKNHGASAGASMSHSHSQIIALPVVPPSVSARLDGSKEYFEKTGKCSLCEVVKKDL
LIDESSHFVSIAPFAATFPFEIWIIPRDHSSNFHEIDDDKAVDLGGLLKLMLQKISKQLNDPPYNYMIQT
SPLGVEESNLPYTHWFLQIVPQLSGVGGFELGTGCYINPVFPEDAAKVLREVNLPV
>gnl|CDD|215347 PLN02644, PLN02644, acetyl-CoA C-acetyltransferase
RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAAL
GAGLPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVD
GMLKDGLWDVYNDFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRP
SVIVDKDEGLGKFDPAKLRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYA
DAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHP
IGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELMQ
>gnl|CDD|178251 PLN02645, PLN02645, phosphoglycolate phosphatase
SSNVTPAAMAAAAQLLTLENADELIDSVETFIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNS
TKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAYLKSINFPKDKKVYVIGEEGILEELELAGFQYLGGPED
GDKKIELKPGFLMEHDKDVGAVVVGFDRYINYYKIQYATLCIRENPGCLFIATNRDAVTHLTDAQEWAGA
GSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQICMVGDRLDTDILFGQNGGCKTLLVLSGVTS
ESMLLSPENKIQPDFYTSKISDFLTLKAATV
>gnl|CDD|215348 PLN02646, PLN02646, argininosuccinate lyase
ASTSMSASEEEAAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDR
DSILDGLDEIEKEIEAGKFEWRPDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAID
VIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLG
SCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEEFGF
VTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNRDLQEDKEPLFDSVDTVS
DMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAVALAESKGCELSDLT
LEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLEITS
>gnl|CDD|215349 PLN02647, PLN02647, acyl-CoA thioesterase
PEFASNSPRPIPVVSTFASPSLSPGNGSIDAGSSTRKPLSLWPGMYHSPVTNALWEARSSIFERLLDPPK
DAPPQSELLTKTPSQSRTSILYKFSSDFILREQYRNPWNEVRIGKLLEDLDALAGTISVKHCSDDDSTTR
PLLLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESNTSDSVALTANFTFVARD
SKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKREFENGEAERLEALLAEGRVFCDMPALAD
RNSILIRDTRLENSLICQPQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRPVDVG
DFLRFKSCVLYTELENSEQPLINVEVVAHVTRPELRSSEVSNTFYFTFTVRPEAAMKNGFKIRNVVPATE
EEARRILERMDAEHLVS
>gnl|CDD|215350 PLN02648, PLN02648, allene oxide synthase
PSSSSSSSSSSSSLPLREIPGSYGLPFLGAIKDRLDYFYFQGEDEFFRSRVEKYKSTVFRVNMPPGPFIA
PDPRVIALLDQKSFPVLFDVSKVDKRDVFTGTYMPSTAFTGGYRVLSYLDPSEPKHAKLKSFLFELLKSR
HRRFIPEFRAAFAELFDTWEAELAKKGKAEFNDPLDQMAFNFLCKALTGKDPSETALGSDGPALIQKWLA
LQLAPLASTGLPHVLEELLLHTFPLPFFLVKSDYDKLYDFFRASATEALDLAEKFGISREEALHNLLFVL
GFNAFGGFKIFFPALLKWVGRAGEELQARLAEEVRSAVKAGGGGVTFAALEKMPLVKSVVYEALRIEPPV
PFQYGRAREDFVIESHDAAFEIKKGEMLFGYQPLVTRDPKVFDRPEEFVPDRFMGEEGEKLLKYVFWSNG
RETESPTVGNKQCAGKDFVVLVARLFVAELFLRYDSFEIEVDTSGLGSSVTFTSLKKASF
>gnl|CDD|215351 PLN02649, PLN02649, glucose-6-phosphate isomerase
TTKKTLLISDTPAWKRLVAHVYQIKKTHLRELLNDAERCQSMIAEFDGIYLDYSRQRVTDETMELLFPLA
EAANLFEKIEAMFSGEIINSTEDRAVLHVALRAPRLAPILVDGKNVVPEVWEVLDKIKAFSEDVRSGKWK
GATGKRFTNVVSIGIGGSFLGPLFVHEALATDPEALKSAKGRKLRFLANVDPVDIARQIAQLDPETTLVV
VVSKTFTTAETMLNARTVRKWLRDALGGLAVAKHMVAVSTNLLLVNKFGIDPWNAFPFWDWVGGRYSVCS
AVGLLPLSLQYGFDVVEEFLEGAASMDEHFRTAPLKENIPVLLGLLSVWNSSFLGYPARAILPYSQALLK
FAPHIQQLDMESNGKGVDLDGNPLPVNTGEIDFGEPGTNGQHSFYQLIHQGRNIPCDFIGVVRSQQPVHL
WLGEGVSNHDELMSNFFAQPDALAYGKTPEQLRAEGVPEELIPHKVFAGNRPSLSILLPELTAYTVGQLL
ALYEHRVAVQGFIWNINSFDQWGVELGKALAKRVRAVLNEARTKGEPVEGFNSSTTALLNHYLANKRALI
>gnl|CDD|178256 PLN02650, PLN02650, dihydroflavonol-4-reductase
MGSQKETVCVTGASGFIGSWLVMRLLERGYTVRATVRDPANVKKVKHLLDLPGATTRLTLWKADLAVEGS
FDDAIRGCTGVFHVATPMDFESKDPENEVIKPTVNGMLSIMKACAKAKTVRRIVFTSSAGTVNVEEHQKP
VYDEDCWSDLDFCRRKKMTGWMYFVSKTLAEKAAWKYAAENGLDFISIIPTLVVGPFISTSMPPSLITAL
SLITGNEAHYSIIKQGQFVHLDDLCNAHIFLFEHPAAEGRYICSSHDATIHDLAKMLREKYPEYNIPARF
PGIDEDLKSVEFSSKKLTDLGFTFKYSLEDMFDGAIETCREKGLIPLSHAKQSIGEAKGNTKDPNIDVKA
G
>gnl|CDD|178257 PLN02651, PLN02651, cysteine desulfurase
LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGAT
ESNNLAIKGVMHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTA
LVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGAL
YVRRRPRVRLEPLMSGGGQERGRRSGTENTPLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLG
GVRVNGPRDPEKRYPGTLNLSFAYVEGESLLMGLKEVAVSSGSACTSASLEPSYVLRALGVPEEMAHGSL
RLGVGRFTTEEEVD
>gnl|CDD|215352 PLN02652, PLN02652, hydrolase; alpha/beta fold family protein
GGGGSGEMMMLTSGASGRIIPVFRSLLSRRALRRCLVFLHSLFLWLLLLLRLRPRRRVSPLSSPEAGAVP
APSRRWRRRMAWKLEEEDTRRRRALAEGVEMVEDGEGTRWATSLFYGARRNALFCRSWAPAAGEMRGILI
IIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIRSENPGVPC
FLFGHSTGGAVVLKAASYPSIEDKLEGIVLTSPALRVKPAHPIVGAVAPIFSLVAPRFQFKGANKRGIPV
SRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEA
ASRHKDIKLYDGFLHDLLFEPEREEVGRDIIDWMEKRLDLVNGSA
>gnl|CDD|178259 PLN02653, PLN02653, GDP-mannose 4,6-dehydratase
PGDPPRKVALITGITGQDGSYLTEFLLSKGYEVHGIIRRSSNFNTQRLDHIYIDPHPNKARMKLHYGDLS
DASSLRRWLDDIKPDEVYNLAAQSHVAVSFEMPDYTADVVATGALRLLEAVRLHGQETGRQIKYYQAGSS
EMYGSTPPPQSETTPFHPRSPYAVAKVAAHWYTVNYREAYGLFACNGILFNHESPRRGENFVTRKITRAV
GRIKVGLQKKLFLGNLDASRDWGFAGDYVEAMWLMLQQEKPDDYVVATEESHTVEEFLEEAFGYVGLNWK
DHVEIDPRYFRPAEVDNLKGDASKAREVLGWKPKVGFEQLVKMMVDEDLELAKREKVLVD
>gnl|CDD|215353 PLN02654, PLN02654, acetate-CoA ligase
VLGESLASEENDLVFPSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWEGDEVCSENL
DVRKGPISIEWFKGGKTNICYNCLDRNVEAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDV
GVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTIN
LKDIVDAALDESAKNGVSVGICLTYENQLAMKREDTKWQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFL
LYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFE
GAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNV
VGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSWP
GAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQ
CAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIM
RRILRKIASRQLDELGDTSTLADPGVVDQLIALADS
>gnl|CDD|215354 PLN02655, PLN02655, ent-kaurene oxidase
VPAVPGLPVIGNLLQLKEKKPHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKL
SKALTVLTRDKSMVATSDYGDFHKMVKRYVMNNLLGANAQKRFRDTRDMLIENMLSGLHALVKDDPHSPV
NFRDVFENELFGLSLIQALGEDVESVYVEELGTEISKEEIFDVLVHDMMMCAIEVDWRDFFPYLSWIPNK
SFETRVQTTEFRRTAVMKALIKQQKKRIARGEERDCYLDFLLSEATHLTDEQLMMLVWEPIIEAADTTLV
TTEWAMYELAKNPDKQERLYREIREVCGDERVTEEDLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTT
LGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYESADMYKTMAFGAGKRVCAGSLQAMLIA
CMAIARLVQEFEWRLREGDEEKEDTVQLTTQKLHPLHAHLKPRGSM
>gnl|CDD|178262 PLN02656, PLN02656, tyrosine transaminase
MENGADTTKTITIKGILSLLMESIDDEENGKRVISLGMGDPTAYSCFHTTHVAQEAVVDALQSNKFNGYA
PTVGLPQARRAIAEYLSRDLPYKLSLDDVFITSGCTQAIDVALSMLARPGANILLPRPGFPIYELCAAFR
HLEVRYVDLLPEKGWEVDLDAVEALADQNTVALVIINPGNPCGNVYSYQHLKKIAETAEKLKILVIADEV
YGHLAFGSNPFVPMGVFGSIVPVLTLGSLSKRWIVPGWRLGWFVTTDPSGSFRDPKIVERIKKYFDILGG
PATFIQAAVPTILEQTDESFFKKTINILKQSSDICCDRIKEIPCITCPHKPEGSMAVMVKLNLSLLEDIS
DDIDFCFKLAREESVIILPGTAVGLKNWLRITFAADPSSLEEALGRIKSFYLRHSKTQY
>gnl|CDD|178263 PLN02657, PLN02657, 3,8-divinyl protochlorophyllide a 8-vinyl reductase
HLSSSLFSLRAAAAASSSPSNRLAASLGGALVRRAAAASRGSRATAAAAAQSFRSKEPKDVTVLVVGATG
YIGKFVVRELVRRGYNVVAVAREKSGIRGKNGKEDTKKELPGAEVVFGDVTDADSLRKVLFSEGDPVDVV
VSCLASRTGGVKDSWKIDYQATKNSLDAGREVGAKHFVLLSAICVQKPLLEFQRAKLKFEAELQALDSDF
TYSIVRPTAFFKSLGGQVEIVKDGGPYVMFGDGKLCACKPISEADLASFIADCVLDESKINKVLPIGGPG
KALTPLEQGEMLFRILGKEPKFFKVPIQIMDFAIGVLDFLAKIFPSLEDAAEFGKIGRYYAAESMLVLDP
ETGEYSAEKTPSYGKDTLEEFFERVAREGMAGQELGEQAV
>gnl|CDD|215355 PLN02658, PLN02658, homogentisate 1,2-dioxygenase
YQSGFGNHFSSEALPGALPRGQNNPLLCPYGLYAEQLSGTAFTAPRKLNRRSWLYRIKPSVTHEPFKPRV
PAHEKLVGEFDPSNSCETTPTQLRWRPFPVPDSPVDFVDGLFTVCGAGSPFLRHGYAIHMYVANKSMDDC
AFCNADGDFLIVPQQGRLWIKTELGKLQVSPGEIVVIPRGFRFAVDLPDGPSRGYVLEIFGGHFQLPDLG
PIGANGLANPRDFLHPVAWFEDGSRPGYTIVQKFGGELFTAKQDFSPFNVVAWHGNYVPYKYDLSKFCPV
NTVLFDHADPSINTVLTAPTDKPGVALADFVIFPPRWLVAEHTFRPPYYHRNCMSEFMGLIYGSYEAKAD
GFLPGGASLHSCMTPHGPDTATYEATIARPCADAPSKLTGTLAFMFESSLIPRVCPWALESPFRDRDYYQ
CWIGLKSHFSREDAD
>gnl|CDD|215356 PLN02659, PLN02659, Probable galacturonosyltransferase
MQLHISPSLRHVTVLPGKGVREFIKVKVGSRRVSYRMLFYSLLFFTFLLRFVFVLSTVDTIDGETKCSTL
GCLGKRLGPRILGRRLDSANVPEVMYQVLEQPLSNDELKGRSDIPQTLEEFMDEVKNSRSDARAFALKLR
EMVTLLEQRTRTAKIQEYLYRHVASSSIPKQLHCLALRLANEHSTNAAARLQLPLAELVPALVDNSYFHF
VLASDNILAASVVANSLVQNALRPHKFVLHIITDRKTYSPMQAWFSLHPLSPAIIEVKALHHFDWFAKGK
VPVLEAMEKDQRVRSQFRGGSSAIVANNTEKPHVIAAKLQALSPKYNSVMNHIRIHLPELFPSLNKVVFL
DDDIVVQTDLSPLWDIDMNGKVNGAVETCRGEDKFVMSKKLKSYLNFSHPLIAKNFDPNECAWAYGMNIF
DLEAWRKTNISSTYHHWLEENLKSDLSLWQLGTLPPGLIAFHGHVHVIDPFWHMLGLGYQENTSLADAES
AGVVHFNGRAKPWLDIAFPQLRPLWAKYIDSSDKFIKSCHIRAS
>gnl|CDD|178266 PLN02660, PLN02660, pantoate--beta-alanine ligase
EVIRDKAAMRAWSRAQRAQGKRIALVPTMGYLHEGHLSLVRAARARADVVVVSIYVNPGQFAPGEDLDTY
PRDFDGDLRKLAALGVDAVFNPHDLYVYVSCLEEGGAGHETWVRVERLEKGLCGKSRPVFFRGVATIVTK
LFNIVEPDVAVFGKKDYQQWRVIRRMVRDLDFDIEVVGSPIVREADGLAMSSRNVRLSAEEREKALSISR
SLARAEELVEEGETDADELKEQVRQAIAEAGGEVDYVEIVDQETLQPVEEIKSPVVIAVAAWFGSVRLID
NIEL
>gnl|CDD|178267 PLN02661, PLN02661, Putative thiazole synthesis
AAIAAAASATSLSSSRELKSSFASSSSSFAGVRLVTSVRAPLADASAPARSSSSSSTAPYDLNNFKFAPI
KESIVSREMTRRYMTDMITYADTDVVIVGAGSAGLSCAYELSKNPNVKVAIIEQSVSPGGGAWLGGQLFS
AMVVRKPAHLFLDELGVPYDEQENYVVIKHAALFTSTIMSKLLARPNVKLFNAVAAEDLIVKGDRVGGVV
TNWALVAQNHDTQSCMDPNVMEAKVVVSSCGHDGPFGATGVKRLKSIGMIDSVPGMKALDMNAAEDAIVR
LTREVVPGMIVTGMEVAEIDGSPRMGPTFGAMMISGQKAAHLALKALGLPNALDGTYKPNLHPELVLAAD
DDETADA
>gnl|CDD|178268 PLN02662, PLN02662, cinnamyl-alcohol dehydrogenase family protein
SGEGKVVCVTGASGYIASWLVKLLLQRGYTVKATVRDPNDPKKTEHLLALDGAKERLHLFKANLLEEGSF
DSVVDGCEGVFHTASPFYHDVTDPQAELIDPAVKGTLNVLRSCAKVPSVKRVVVTSSMAAVAYNGKPLTP
DVVVDETWFSDPAFCEESKLWYVLSKTLAEEAAWKFAKENGIDMVTINPAMVIGPLLQPTLNTSAEAILN
LINGAQTFPNASYRWVDVRDVANAHIQAFEIPSASGRYCLVERVVHYSEVVKILHELYPTLQLPEKCADD
KPYVPTYQVSKEKAKSLGIEFIPLEVSLKDTVESLKEKGFLS
>gnl|CDD|166304 PLN02663, PLN02663, hydroxycinnamoyl-CoA:shikimate/quinate hydroxycinnamoyltransferase
MIINVRESTMVRPAEETPRRGLWNSNVDLVVPRFHTPSVYFYRPTGASNFFDPQVMKEALSKALVPFYPM
AGRLRRDEDGRIEIDCNAEGVLFVEADTPSVIDDFGDFAPTLELRQLIPTVDYSGGISSYPLLVLQVTHF
KCGGVSLGVGMQHHAADGFSGLHFINTWSDMARGLDLTIPPFIDRTLLRARDPPQPAFHHVEYQPPPSMK
TPLETSKPENTTVSIFKLTRDQLNTLKAKSKEDGNTISYSSYEMLAGHVWRSACKARGLPDDQETKLYIA
TDGRSRLRPQLPPGYFGNVIFTATPIAVAGELQSKPTWYAAGKIHDALVRMDDDYLRSALDYLELQPDLS
ALVRGAHTFRCPNLGITSWVRLPIYDADFGWGRPIFMGPGGIAYEGLSFILPSPTNDGSLSVAISLQSEH
MKLFEKFLYEI
>gnl|CDD|178269 PLN02664, PLN02664, enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase
MESYKTLEIIQKSPNSSVFHLNLNRPSQRNALSLDFFTEFPKALSSLDQNPNVSVIILSGAGDHFCSGID
LKTLNSISEQSSSGDRGRSGERLRRKIKFLQDAITAIEQCRKPVIAAIHGACIGGGVDIVTACDIRYCSE
DAFFSVKEVDLAITADLGTLQRLPSIVGYGNAMELALTGRRFSGSEAKELGLVSRVFGSKEDLDEGVRLI
AEGIAAKSPLAVTGTKAVLLRSRELSVEQGLDYVATWNSAMLVSDDLNEAVSAQIQKRKPVFAKL
>gnl|CDD|215357 PLN02665, PLN02665, pectinesterase family protein
MMTSIAIIACAIAALVVLVSPTVSSDDTTPIPADKSQLNQWFQANVKPYAQRKGTLDPALEAAEAAPRII
KVRKDGSGDFKTITDAIKSIPAGNTQRVIIDIGPGEYNEKITIDRSKPFVTLYGSPGAMPTLTFDGTAAK
YGTVYSATLIVESDYFMAANIIIKNSAPRPDGKRKGAQAVAMRISGDKAAFYNCRFIGFQDTLCDDKGRH
FFKDCYIEGTVDFIFGSGKSLYLNTELHVVGDGGLRVITAQARNSEAEDSGFSFVHCKVTGTGTGAYLGR
AWMSRPRVVFAYTEMSSVVNPEGWSNNKHPERDKTVFYGEYKCTGPGANPSGRVKFTKQLDDKEAKPFLS
LGYIEGSKWLLPPPNL
>gnl|CDD|215358 PLN02666, PLN02666, 5-oxoprolinase
SMGSRGSRKFRFCIDRGGTFTDVYAEVPGGSDFRVLKLLSVDPANYDDAPREGIRRILEEVTGKKIPRSA
KIPTERIEWIRMGTTVATNALLERKGERIALCVTKGFKDLLQIGNQARPNIFDLTVSKPSNLYEEVVEVD
ERVVLALEEDGDDAGGSVVKGVTGELVEVVKPLDEEALRPLLQGLLDKGIRSLAVVLMHSYTYPAHERAV
GKLARSMGFKQVSLSSALVPMVRAVPRGHTASVDAYLTPVIKEYLSGFLSGFDDGLGDVNVLFMQSDGGL
TPESRFSGHKAILSGPAGGVVGYAQTTFGLETEKPVIGFDMGGTSTDVSRYDGSYEQVLETQTAGVIIQA
PQLDINTVAAGGGSKLKFQFGAFRVGPESVGAHPGPVCYRKGGELAVTDANLVLGRVIPDYFPSIFGPNE
DEPLDLEATRAAFEALAAQINSYRKSQDPSAKDMSVEEVALGFVRVANEAMCRPIRQLTEMKGYETANHA
LACFGGAGPQHACAIARALGMSEVFVHRYCGILSAYGMGLADVVAEAQEPYAAVYGPESLAEASRREDAL
AEKVRQKLQEQGFREDNITTETYLNLRYEGTDTAIMVAEPENGDGSDGDYAAAFVKLFRREYGFKLQNRD
ILIDDVRVRGIGVTNILKPLPLDAASGGLPEPERTTKVYFENGWHDTPVYKLENLGPGHEIPGPAIIMNG
NSTVVVEPGCKAIVTKYGNIKIEVENSAEQSAEETVKAAEKKADVVQLSIFNHRFMGIAEQMGRTLQRTS
ISTNIKERLDFSCALFGPDGGLVANAPHVPVHLGAMSSTVRWQLEYWGENLNEGDVLVTNHPQAGGSHLP
DITVITPVFRDGKIVFFVASRGHHADIGGITPGSMPPFSKTIWEEGAAIKAFKLVEGGVFQEEGITKLLQ
APGSDETAPKIPGTRRLQDNLSDLRAQVAANQRGISLIKELIDEYGLGTVQAYMGHVQANAELAVREMLK
SVAARVSSESPTFGDGSSVTLEAEDYMDDGSPIHLTLTIDRRKGSAVFDFEGTSPEVYGNWNAPPAVTAA
AVIYCLRCLVDVDIPLNQGCLAPVTIRIPPGSFLSPSDKAAVVGGNVLTSQRVTDVVLTAFQACACSQGC
MNNLTFGDDTFGYYETIAGGAGAGPTWDGTSGVQCHMTNTRITDPEILERRYPVLLHRFGLREGSGGDGL
HRGGDGVVREIEFRRPVTVSILSERRVHAPRGLAGGGDGARGANLLIRKDGRRVNLGGKNTVHVEAGERL
RILTPGGGGYGSKPS
>gnl|CDD|215359 PLN02667, PLN02667, inositol polyphosphate multikinase
DLKVPEHQVAGHRASDGKLGPLVDDSGRFYKPLQDDSRGEREAAFYESFSSDTRVPDHIRRFFPVFHGTQ
LVEASDGSGLLVLEDLLAGYTKPCVMDVKMGSRTWYPEASEEYIQKCLKKDRETTTVSLGFRVSGFKVYD
HKESEFWKAERKLVKGLDADGVRLALRKFVSSNSPADPNPDCAFASAVYGGSHGILAQLLELKSWFEEQT
LYHFFSASILIVYEGEAILKGNPEDSRVEVKLVDFAHVLDGNGVIDHNFLGGLCSLIKFISEILTSPDES
ATSGES
>gnl|CDD|178273 PLN02668, PLN02668, indole-3-acetate carboxyl methyltransferase
MAPKGDNVVVSNMKLEKLLCMKGGKGEGSYANNSQAQALHARSMLHLLEETLDNVHLNSSPEVPFTAVDL
GCSSGSNTIHIIDVIVKHMSKRYESAGLDPPEFSAFFSDLPSNDFNTLFQLLPPLANYGGSMEECLAASG
HRSYFAAGVPGSFYRRLFPARSIDVFHSAFSLHWLSQVPESVTDKRSAAYNKGRVFIHGASESTANAYKR
QFQADLAGFLRARAQEMKRGGAMFLVCLGRTSVDPTDQGGAGLLFGTHFQDAWDDLVQEGLVTSEKRDSF
NIPVYAPSLQDFKEVVEANGSFAIDKLEVFKGGSPLVVNEPDDAAEVGRAMANSCRSVAGVLVDAHIGEE
LSNELFLRVERRATSHAKELLEKLQFFHIVASLSFA
>gnl|CDD|178274 PLN02669, PLN02669, xylulokinase
DLSLPEDSLFLGFDSSTQSLKATVLDSNLRIVASEIVHFDSDLPHYGTKDGVYRDPKVNGRIVSPTLMWV
EALDLLLQKLAKEKFPFHKVVAISGSGQQHGSVYWRKGASAVLKSLDPSKSLVAQLQDAFSTKDSPIWMD
SSTTKQCREIEEAVGGAAELSKLTGSRAYERFTGPQIRKIYETQPEVYHDTERISLVSSFMASLLVGDYA
SIDETDGAGMNLMDIEKRCWSKAALEATAPGLEEKLGKLAPAHAVAGKIHPYFVQRFGFSSNCLVVQWSG
DNPNSLAGLTLSTPGDLAISLGTSDTVFGITREPQPSLEGHVFPNPVDPESYMVMLCYKNGSLTREDIRN
RCADGSWDVFNKLLEQTPPLNGGKLGFYYKEHEILPPLPVGFHRYILENFSGEALDGLVEEEVGEFDPPS
EVRAIIEGQFLSMRAHAERFGMPVPPKRIIATGGASANQSILKLIASIFGCDVYTVQRPDSASLGAALRA
AHGWLCNEQGSFVPISCLYEGKLEATSLSCKLAVKAGDQELLSQYGLLMKKRMEIEQQLVEKLGRC
>gnl|CDD|178275 PLN02670, PLN02670, transferase, transferring glycosyl groups
MKREEVLHVAMFPWLAMGHLIPFLRLSKLLAQKGHKISFISTPRNLHRLPKIPSQLSSSITLVSFPLPSV
PGLPSSAESSTDVPYTKQQLLKKAFDLLEPPLTTFLETSKPDWIIYDYASHWLPSIAAELGISKAFFSLF
TAATLSFIGPPSSLMEGGDLRSTAEDFTVVPPWVPFESNIVFRYHEVTKYVEKTEEDETGPSDSVRFGFA
IGGSDVVIIRSSPEFEPEWFDLLSDLYRKPIIPIGFLPPVIEDDEEDDTIDVKGWVRIKEWLDKQRVNSV
VYVALGTEASLRREEVTELALGLEKSETPFFWVLRNEPGTTQNALEMLPDGFEERVKGRGMIHVGWVPQV
KILSHESVGGFLTHCGWNSVVEGLGFGRVLILFPVLNEQGLNTRLLHGKKLGLEVPRDERDGSFTSDSVA
ESVRLAMVDDAGEEIRDKAKEMRNLFGDMDRNNRYVDELVHYLRENRSSRLK
>gnl|CDD|178276 PLN02671, PLN02671, pectinesterase
MKVEAFIPAVLLLCFGCFKSSCALQIGNNDLKNFISWEDLRVVEDGALLASKYDTNVSRVIVVDKNGGGD
SLTVQGAVDMVPDYNSQRVKIYILPGIYREKVLVPKSKPYISFIGNESRAGDTVISWNDKASDLDSNGFE
LGTYRTASVTIESDYFCATGITFENTVVAEPGGQGMQAVALRISGDKAFFYKVRVLGAQDTLLDETGSHY
FYQCYIQGSVDFIFGNAKSLYQDCVIQSTAKRSGAIAAHHRDSPTEDTGFSFVNCVINGTGKIYLGRAWG
NYSRTVYSNCFIADIITPSGWSDWNYPERQRTVMFGEYNCSGRGADRGGRVPWSKTLSYEEVRPFLDREF
IYGDQWLRL
>gnl|CDD|215360 PLN02672, PLN02672, methionine S-methyltransferase
TTGSDAEVDEFLDQCKQSGDAAYGAFKGVLERLEDPTTRSDARKLLSAVEKRVAASEAGEDCFATYHFRI
HDLVLDDYEGFRNRKKLTMMEIPSIFIPEDWSFTFYEGLNRHPDSIFRDKTVAELGCGNGWISIAIAEKW
LPSKVYGLDINPRAVKVAWINLYLNALDDDGLPVYDGEGKTLLDRVEFYESDLLGYCRDNNIELDRIVGC
IPQILNPNPEAMSKLVTENASEEFLYSLSNYCALQGFVEDQFGLGLIARAVEEGISVIKPMGIMIFNMGG
RPGQAVCERLFERRGFRITKLWQTKINQAADTDISALVEIEKNSRHRFEFFMGLVGDQPICARTAWAYGK
AGGRISHALSVYSCQLRQPNQVKTIFKFLKNGFHEVSGSLDLSFEDESVADEKIPFLAYLASALKGLSYF
PCEPPAGSKRFRNLIAGFMRIYHHIPLTPDNVVVFPSRAVAIENALRLFSPRLAIVDEHLTRWLPKKWLT
SLAIENATSDSKSDDVITVIEAPRQSDLVIELIKKLKPQVVVTGMADFEMRTSTAFEHLLNVTAEIGARL
FLDISDHLELSSLPGSNGVLKYLAGHPLPSHAAIICGLVKNQVYSDLEVAFVISENEAVLKALSKTGEVL
EGRTAIISQFYYGCLFHELLAFQLADRHTPQERLPEEEESSKFIGFSSSARSALKEAELSVSGSQESSLI
HMDVDESFLPVPSAVKASIFESFVRQNISESETDPRPSILQFIKSNYGFPTDSCTEFVYGDTSLALFNKL
VLCCVQEGGTLCFPAGSNGTYVSAAKFLKANFRRIPTKSSDGFKLTAKTLASTLETVKKPWVYISGPTIN
PTGLLYSNSEIEEILSVCAKYGARVIIDTSFSGLEYDTSGWGGWDLKSILSRLKSSNPSFAVALLGGLST
ELLSGGHEFGFLALNDSVLIDAFHSAPGLSRPHSTLKYTIKKLLGLKNQKSSDLLDGVAEQKKILKSRAE
RLKETLEACGWDVLEPQGGISMVAKPSAYLGKTVKLKSIDGDTGIKLDSSNIREAILKSTGLCINSSSWT
GIPGYCRFSFALEDSEFDRALKAIARFKELVL
>gnl|CDD|215361 PLN02673, PLN02673, quinolinate synthetase A
ASSSPTSSSSSSFLSLLPNPSPNFRTTHPNFGSQRRIGTINPLFKSFKCIQSPPPDSAPSNASPFSCSAV
AFSPSQTTELVPCKLQRLIKEFKSLTEPVDRVKRLLHYASLLPPLPESSRVESNRVMGCTAQVWLEAELD
QDGKMRFWADSDSEITKGFCSCLIWVLDGASPEEVLELKTEDLAALNVGLPGGERSRVNTWHNVLVSMQK
RTRRLVAEREGKPSFDPFPSLVLTADGIEAKGSFAQAQARYLFPEESKVEELVNVLKEKKIGVVAHFYMD
PEVQGVLTAAQKHWPHISISDSLIMADSAVKMAKAGCQFITVLGVDFMSENVRAILDQAGFGEVGVYRMS
NERIGCSLADAASTPAYMNYLEAASASPPSLHVVYINTSLETKAYAHELVPTITCTSSNVVQTILQAFAQ
MPELNIWYGPDSYMGANIVKLFQQMTLMTDEEIANIHPKHNLDSIKSLLPRLHYYQDGTCIVHHLFGHEV
VEKINYMYCDAFLTAHLEVPGEMFSLAMEAKRRGMGVVGSTQNILDFIKQRVQEALDRNVNDHLQFVLGT
ESGMVTSIVAAVRSLLGSSKSSKSADVKVEIVFPVSSDSMTKTSSNSSLGRNSIKVGDVILPVIPGVASG
EGCSIHGGCASCPYMKMNSLSSLLKVCHHLPDEKNVLGGYEAERFKLQTPNGKSIADVGCEPILHMRHFQ
ATKELPEKLVSQVLSCESNGRSTS
>gnl|CDD|178279 PLN02674, PLN02674, adenylate kinase
SSAAAANLEDVPSVDLMTELLRRMKCSSKPDKRLILIGPPGSGKGTQSPIIKDEYCLCHLATGDMLRAAV
AAKTPLGIKAKEAMDKGELVSDDLVVGIIDEAMKKPSCQKGFILDGFPRTVVQAQKLDEMLAKQGAKIDK
VLNFAIDDAILEERITGRWIHPSSGRTYHTKFAPPKVPGVDDVTGEPLIQRKDDTAAVLKSRLEAFHKQT
EPVIDYYAKKGVVANLHAEKPPKEVTAEVQKALS
>gnl|CDD|215362 PLN02676, PLN02676, polyamine oxidase
MLLLLSLSVLLAVHLFAVAAMDAKPSPSVIIVGAGMSGISAAKTLSEAGIEDILILEATDRIGGRMRKAN
FAGVSVELGANWVEGVGGPESNPIWELANKLKLRTFYSDFDNLSSNIYKQDGGLYPKKVVQKSMKVADAS
DEFGENLSISLSAKKAVDISILTAQRLFGQVPKTPLEMVIDYYNYDYEFAEPPRVTSLKNTEPNPTFVDF
GEDEYFVADPRGYESLVYYLAEQFLSTKSGKITDPRLKLNKVVREISYSKNGVTVKTEDGSVYRAKYVIV
SVSLGVLQSDLIKFKPPLPDWKIEAIYQFDMAVYTKIFLKFPYKFWPSGPGTEFFLYAHERRGYYPFWQH
LENEYPGSNVLFVTVTDEESRRIEQQPDSETKAEIMEVLRKMFGPNIPEATDILVPRWWSNRFFKGSYSN
WPIGVSRYEFDQIRAPVGRVYFTGEHTSEKYNGYVHGAYLAGIDTANDLLECIKKKKCRKNVQQKPK
>gnl|CDD|215363 PLN02677, PLN02677, mevalonate kinase
MEVKARAPGKIILAGEHAVVHGSTAVAAAIDLYTYVSLRFPPSAENDDTLKLQLKDLGLEFSWPLARIKE
ALPDLGTPCPSTPTSCSEETLKSIAALVEEQNIPEAKIWLSSGVSAFLWLYTSILGFNPATVVVTSELPL
GSGLGSSAAFCVALSAALLAASDSISVSTGGNGWSSLDETDLELVNKWAFEGEKIIHGKPSGIDNTVSTY
GNMIKFKSGELTRLQSNMPLKMLITNTRVGRNTKALVAGVSERALRHPDAMKSVFNAVDSISEELATIIQ
SPAEDELSITEKEEKLKELMEMNQGLLQCMGVSHSSIETVLRTTLKYKLVSKLTGAGGGGCVLTLLPTLL
SGTVVDKVIAELESSGFQCFTAGIGGNGVQICYGGCS
>gnl|CDD|215364 PLN02678, PLN02678, seryl-tRNA synthetase
MLDINLFREEKGGDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAK
EDATELIAETKELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEANNAVVRTWGEKRQEPKL
KNHVDLVELLGIVDTERGADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKC
AQLAQFDEELYKVTGEGDDKYLIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIF
RVHQFEKVEQFCITSPNGNESWEMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPAS
KTYRELVSCSNCTDYQSRRLEIRYGQKKSNEQTKQYVHLLNSTLTATERTLCCILENYQTEDGVRVPEVL
QPFMGGIEFLPFKKKPPAKGKGKKKKKK
>gnl|CDD|178283 PLN02679, PLN02679, hydrolase, alpha/beta fold family protein
MRALAATAMHHHFMLSSSTSASTTRRIGLRRDRACVRATASGSTAVSSSGGVEAELEEIYERCKKWKWKG
EYSINYLVKGSPEVTSSGPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPPGFSYTMET
WAELILDFLEEVVQKPTVLIGNSVGSLACVIAASESTRDLVRGLVLLNCAGGMNNKAVVDDWRIKLLLPL
LWLIDFLLKQRGIASALFNRVKQRDNLKNILLSVYGNKEAVDDELVEIIRGPADDEGALDAFVSIVTGPP
GPNPIKLIPRISLPILVLWGDQDPFTPLDGPVGKYFSSLPSQLPNVTLYVLEGVGHCPHDDRPDLVHEKL
LPWLAQLPST
>gnl|CDD|215365 PLN02680, PLN02680, carbon-monoxide oxygenase
MAVPVIRFPIFMLVRLLGVIVAALVLTWTVHYRGGLALSSDNKDLIFNVHPVLMVIGLVLLNGEAMLAYK
TVPGTKNLKKLVHLTLQFLAFCLSLIGVWAALKFHNEKGIDNFYSLHSWLGLACLFLFSLQWAAGFVTFW
YPGGSRNSRASLLPWHVFFGIYIYALAVATATTGILEKATFLQSNKVISRYSTEAMLVNSLGILIVVLGG
FVILAIVTPLNGKGDVLRGSTE
>gnl|CDD|215366 PLN02681, PLN02681, proline dehydrogenase
PAGPAATVPPAVTSTTTPASDDVLDFSDHAALFAGLSTSELLRSLLVLQLCAIGPLVDLGEWLLTSPLMV
LGRAIVLALVKATFYSHFCAGEDAEEAARTVRRLWELGLGGILDYAAEDAGDNAACDRNLEKFLAAIRAA
ATLPPSSSSAAVKITALCPPSLLERVSDLLRWQDRDPNGKLPWKQWSFPLFADSSPLYHATSEPEPLTAE
EERLLELAHERLQKLCERAAQLGVPLLIDAEYTSLQPAIDYITYDLAREFNKGKDRPIVYGTYQAYLKDA
RERLRLDLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPSPVHDTIQDTHACYNRCAEFLLEKASNGD
GEVMLATHNVESGELAAAKMNELGLHKGDPRVQFAQLLGMSDNLSFGLGNAGFRVSKYLPYGPVEEVIPY
LLRRAEENRGLLSGSAIDRQLLRKELKRRLKAAVL
>gnl|CDD|215367 PLN02682, PLN02682, pectinesterase family protein
MSAPFNFLACLLLLVFLLPSSQTGCQPLAPDNSTRVQAPEEQFMKWVRFMGSLKHSVFQKAKNKLFPSYT
IVVDKKPAAGDFTTIQAAIDSLPVINLVRVVIKVNAGTYREKVNIPPLKAYITLEGAGADKTIIQWGDTA
DTPGPGGRPLGTYGSATFAVNSPYFIAKNITFKNTAPVPPPGALGKQAVALRISADTAAFYGCKFLGAQD
TLYDHLGRHYFKDCYIEGSVDFIFGNGLSLYEGCHLHAIARNFGALTAQKRQSVLEDTGFSFVNCKVTGS
GALYLGRAWGTFSRVVFAYTYMDNIIIPRGWYNWGDPNREMTVFYGQYKCTGPGANFAGRVAWSRELTDE
EAKPFISLSFIDGSEWLKL
>gnl|CDD|215368 PLN02683, PLN02683, pyruvate dehydrogenase E1 component subunit beta
MLGQLLRRTRPAAAAAARGYASAAKEMTVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQK
YGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTFNFSMQAIDHIINSAAKTNYMSAGQISVPIVFRG
PNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSSEDARGLLKAAIRDPDPVVFLENELLYGESFPVSAEV
LDSSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT
NRLVTVEEGWPQHGVGAEICASVVEESFDYLDAPVERIAGADVPMPYAANLERLALPQVEDIVRAAKRAC
YRSVPM
>gnl|CDD|166325 PLN02684, PLN02684, Probable galactinol--sucrose galactosyltransferase
MTIKPAVRISDGKLIVKNRTILTGVPDNVIATSGSESGPVEGVFVGAVFDKENSKHVVSLGTLRDVRFMA
CFRFKLWWMAQKMGDMGRDIPLETQFLLVETKDGSHLESDGANEENQKVYTVFLPLIEGSFRACLQGNVN
DELELCLESGDVDTKRSSFTHSLFIHAGTDPFQTITDAIRAVKLHLKSFRQRHEKKLPGIVDYFGWCTWD
AFYQEVTQEGVEAGLKSLAAGGTPPKFVIIDDGWQSVGGDPTVEAGDEKKEQPLLRLTGIKENEKFKKKD
DPNVGIKNIVNIAKEKHGLKYVYVWHAITGYWGGVRPGVKEMEEYGSVMKYPNVSKGVVENDPTWKTDVM
TLQGLGLVNPKKVYKFYNELHSYLADAGIDGVKVDVQCILETLGAGLGGRVELTRQYHQALDASVARNFP
DNGCIACMSHNTDALYCSKQTAVVRASDDFYPRDPVSHTIHIAAVAYNSVFLGEFMQPDWDMFHSLHPAA
EYHASARAISGGPLYVSDAPGKHNFELLKKLVLPDGSILRARLPGRPTRDCLFSDPARDGVSLLKIWNMN
KYTGVLGVYNCQGAAWSSTERKNIFHQTKTDSLTGSIRGRDVHLIAEAATDPNWNGDCAVYCHSRGELIT
MPYNASLPVSLKVLEHEIFTVTPIKHLAPGFSFAPLGLINMYNAGGAIEGLKYEVKKGKVVMEVKGCGKF
GAYSSVKPRRCVVESNEIAFEYDSSSGLVTFELDKMPEEGKRLHLVEVEL
>gnl|CDD|215369 PLN02685, PLN02685, iron superoxide dismutase
AVTATPASLSLSPALLPSQGPSRRMQWKGKRRTCTRKAVSGVITAKFELKPPPYPLDALEPHMSRETLEY
HWGKHHRAYVDNLNKQIVGTELDGMSLEDVVLITYNKGDMLPAFNNAAQAWNHEFFWESMKPGGGGKPSG
ELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAYKANRLDVGNAVNPCPSEEDKKLVVVKSPNAVNP
LVWDYSPLLTIDVWEHAYYLDFQNRRPDYISTFMEKLVSWEAVSARLESAKARAAQREQEETRTEDEEEP
DSEAVEMYLDSDIDVSEVD
>gnl|CDD|215370 PLN02686, PLN02686, cinnamoyl-CoA reductase
MGVLRSTESMEAEVEEFRAALLLSRGGDDDGWRGSRGGGKEANAGDAGADAEARLVCVTGGVSFLGLAIV
DRLLRHGYSVRIAVDTQEDKEKLREMEMFGEMGRSNDGIWTVMANLTEPESLHEAFDGCAGVFHTSAFVD
PAGLSGYTKSMAELEAKASENVIEACVRTESVRKCVFTSSLLACVWRQNYPHDLPPVIDEESWSDESFCR
DNKLWYALGKLKAEKAAWRAARGKGLKLATICPALVTGPGFFRRNSTATIAYLKGAQEMLADGLLATADV
ERLAEAHVCVYEAMGNKTAFGRYICFDHVVSREDEAEELARQIGLPINKIAGNSSSDDTPARFELSNKKL
SRLMSRTRRCCYDESYP
>gnl|CDD|215371 PLN02687, PLN02687, flavonoid 3'-monooxygenase
MDLPLPLLLGTVAVSVLVWCLLLRRGGSGKHKRPLPPGPRGWPVLGNLPQLGPKPHHTMAALAKTYGPLF
RLRFGFVDVVVAASASVAAQFLRTHDANFSNRPPNSGAEHMAYNYQDLVFAPYGPRWRALRKICAVHLFS
AKALDDFRHVREEEVALLVRELARQHGTAPVNLGQLVNVCTTNALGRAMVGRRVFAGDGDEKAREFKEMV
VELMQLAGVFNVGDFVPALRWLDLQGVVGKMKRLHRRFDAMMNGIIEEHKAAGQTGSEEHKDLLSTLLAL
KREQQADGEGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSE
SDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRP
DRFLPGGEHAGVDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGQTPDKLNMEEA
YGLTLQRAVPLMVHPRPRLLPSAYGIE
>gnl|CDD|178291 PLN02688, PLN02688, pyrroline-5-carboxylate reductase
FRVGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVK
PQVVKDVLTELRPLLSKDKLLVSVAAGITLADLQEWAGGRRVVRVMPNTPCLVGEAASVMSLGPAATADD
RDLVATLFGAVGKIWVVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAK
MVLETGKHPGQLKDMVTSPGGTTIAGVHELEKGGFRAALMNAVVAAAKRSRELSKS
>gnl|CDD|215372 PLN02689, PLN02689, Bifunctional isoaspartyl peptidase/L-asparaginase
MGGWAIALHGGAGDIDPNLPRERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRG
SVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDN
SYFITEENVERLKQAKEANSVQFDYRIPLDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLV
NKMVGRIGDTPIIGAGTYANHLCAVSATGKGEAIIRGTVARDVAAVMEYKGLPLQEAVDYVIKERLPEGP
AGLIAVSATGEVAMAFNTTGMFRACATEDGFMEVGIWP
>gnl|CDD|178293 PLN02690, PLN02690, Agmatine deiminase
GRATPKELGYRMPAEWEPHAGCWMGWPERPDNWRDNAKPAQQQFAAVAKAISKFEPVTVCASPAQWENAR
EQLPGVSNVRVVEMSMNDSWFRDTGPTFVVRDVPVDSSSGEREVAGIDWDFNAWGGALKGCYPDWSLDLL
VARKILEAERLPRFPHSMILEGGSIHVDGEGTCLTTEECLLNPNRNPHLTKEEIEEELKEYLGVEKVIWL
PRGLYGDDDTNGHVDNMCCFARPGVVLLSWTDDEDDPQYERSVEALSILSNTTDARGRKLQVIKLHVPGP
LYMTFEEASGVAQDGAAKPRLAGERLAASYVNFYIANGGIVAPQFGDAKWDKEAIEVLSEAFPNHKVVGV
ESAREIVLGGGNIHCITQQQPAEL
>gnl|CDD|215373 PLN02691, PLN02691, porphobilinogen deaminase
KVWRLAPGLSRRRCRGRTRRRHCAVVRAAVAVEASSGKTDVAPIRIGTRGSPLALAQAYETRDLLKAAHP
ELAEEGALEIVIIKTTGDKILDQPLADIGGKGLFTKEIDDALLSGRIDIAVHSMKDVPTYLPEGTILPCN
LPREDVRDAFISLKAKSLAELPAGSVVGTASLRRQSQILHKYPHLKVVNFRGNVQTRLRKLQEGVVDATL
LALAGLKRLDMTEHATSILSTDEMLPAVAQGAIGIACRTDDDKMLEYLASLNHEETRLAVACERAFLAAL
DGSCRTPIAGYARRDKDGNCDFRGLVASPDGKQVLETSRKGPYVIDDAVAMGKDAGKELKSKAGPGFFDC
L
>gnl|CDD|178295 PLN02692, PLN02692, alpha-galactosidase
MERRAMVIKMALLLILISVMVMVMVESSRSVNNKEFDDDSEILRRNLLANGLGITPPMGWNSWNHFSCKI
DEKMIKETADALVSTGLSKLGYTYVNIDDCWAEIARDEKGNLVPKKSTFPSGIKALADYVHSKGLKLGIY
SDAGYFTCSKTMPGSLGHEEQDAKTFASWGIDYLKYDNCNNDGSKPTVRYPVMTRALMKAGRPIFFSLCE
WGDMHPALWGSKVGNSWRTTNDISDTWDSMISRADMNEVYAELARPGGWNDPDMLEVGNGGMTKDEYIVH
FSIWAISKAPLLLGCDVRNMTKETMDIVANKEVIAVNQDPLGVQAKKVRMEGDLEIWAGPLSGYRVALLL
LNRGPWRNSITANWDDIGIPANSIVEARDLWEHKTLKQHFVGNLTATVDSHACKMYILKPIS
>gnl|CDD|178296 PLN02693, PLN02693, IAA-amino acid hydrolase
MALNNFLTFQLLLLLLRVSSESPWIAGDVSQIQINLLELAKSPEVFDWMVRIRRKIHENPELGYEEFETS
KLIRSELDLIGIKYRYPVAITGIIGYIGTGEPPFVALRADMDALPIQEAVEWEHKSKIPGKMHACGHDGH
VAMLLGAAKILQEHRHHLQGTVVLIFQPAEEGLSGAKKMREEGALKNVEAIFGIHLSPRTPFGKAASRAG
SFMAGAGVFEAVITGKGGHAAIPQHTIDPVVAASSIVLSLQQLVSRETDPLDSKVVTVSKVNGGNAFNVI
PDSITIGGTLRAFTGFTQLQQRIKEIITKQAAVHRCNASVNLTPNGREPMPPTVNNMDLYKQFKKVVRDL
LGQEAFVEAAPEMGSEDFSYFAETIPGHFSLLGMQDETNGYASSHSPLYRINEDVLPYGAAIHATMAVQY
LKEKASKGSVSGFHDEL
>gnl|CDD|178297 PLN02694, PLN02694, serine O-acetyltransferase
MMPAGELRHPSPPKTNSATTADEEAAWLWTQIKAEARRDAESEPALASYLYSTILSHSSLERSLSFHLGN
KLCSSTLLSTLLYDLFLNTFSSDPSLRAATVADLRAARVRDPACVSFSHCLLNYKGFLACQAHRVAHKLW
TQSRRPLALALHSRISDVFAVDIHPAAKIGKGILFDHATGVVIGETAVIGNNVSILHHVTLGGTGKACGD
RHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVGGKEKPAKHEECPGESM
DHTSFISEWSDYII
>gnl|CDD|178298 PLN02695, PLN02695, GDP-D-mannose-3',5'-epimerase
ESYGAYTLAELEREPYWPSEKLRICITGAGGFIASHIARRLKAEGHYIIASDWKKNEHMSEDMFCHEFHL
VDLRVMENCLKVTKGVDHVFNLAADMGGMGFIQSNHSVIMYNNTMISFNMLEAARINGVKRFFYASSACI
YPEFKQLETNVSLKESDAWPAEPQDAYGLEKLATEELCKHYTKDFGIECRIGRFHNIYGPFGTWKGGREK
APAAFCRKALTSTDEFEMWGDGKQTRSFTFIDECVEGVLRLTKSDFREPVNIGSDEMVSMNEMAEIALSF
ENKKLPIKHIPGPEGVRGRNSDNTLIKEKLGWAPTMRLKDGLRITYFWIKEQIEKEKAEGSDAAAYSSSK
VVGTQAPVQLGSLRAADGKE
>gnl|CDD|215374 PLN02696, PLN02696, 1-deoxy-D-xylulose-5-phosphate reductoisomerase
TPLPKLPGGFTTKRSSSRQSRGRRAKCSVAGWSQNSPPPAWPGRAVVEPGRKGWDGPKPISLLGSTGSIG
TQTLDIVAENPDKFKVVALAAGSNVTLLADQVRKFKPKLVAVRNESLVDELKEALADLDDKPEIIPGEEG
IVEVARHPEAVTVVTGIVGCAGLKPTVAAIEAGKDIALANKETLIAGGPFVLPLAKKHGVKILPADSEHS
AIFQCIQGLPEGGLRRIILTASGGAFRDWPVEKLKEVKVADALKHPNWSMGKKITVDSATLMNKGLEVIE
AHYLFGADYDDIDIVIHPQSIIHSMVETQDSSVLAQLGWPDMRLPILYTMSWPDRVPCSEITWPRLDLCK
LGSLTFKAPDNVKYPSMDLAYAAGRAGGTMTGVLSAANEKAVEMFIDEKIGYLDIFKVIELTCEAHKEEL
VTSPSLEDILHYDLWAREYAAELVESGGLSPVVA
>gnl|CDD|215375 PLN02697, PLN02697, lycopene epsilon cyclase
MECLGARNFAAMAVSTSPGWSSRRRRPVRRGNDVRSSRGLSCTVVATRGGKSGSESCVVVDEEFADEEDY
IKAGGSELLFVQMQANKSMDEQSKIADKLPPISIGDGTLDLVVIGCGPAGLALAAESAKLGLNVGLIGPD
LPFTNNYGVWEDEFKDLGLEDCIEHVWRDTIVYLDDDKPIMIGRAYGRVSRTLLHEELLRRCVESGVSYL
SSKVDRITEASDGLRLVACEDGRVIPCRLATVASGAASGRLLQYEVGGPRVCVQTAYGVEVEVENNPYDP
SLMVFMDYRDYFKEKVSHLEAEYPTFLYAMPMSSTRVFFEETCLASKDAMPFDLLKKRLMSRLETMGIRI
LKTYEEEWSYIPVGGSLPNTEQKNLAFGAAASMVHPATGYSVVRSLSEAPKYASVIARILKNVSSGGKLG
TSNSSNISMQAWNTLWPQERKRQRAFFLFGLALILQLDTEGIRTFFVTFFRLPKWMWQGFLGSTLSSVDL
ILFALYMFVIAPNQLRMQLVRHLISDPTGATMIKTYLTL
>gnl|CDD|178301 PLN02698, PLN02698, Probable pectinesterase/pectinesterase inhibitor
MIDMVIFWVLGASSRNMPFAYQNEVQRECSFTKYPSLCVQTLRGLRHDGVDIVSVLVNKTISETNLPLSS
SMGSSYQLSLEEATYTPSVSDSCERLMKMSLKRLRQSLLALKGSSRKNKHDIQTWLSAALTFQQACKDSI
VDSTGYSGTSAISQISQKMDHLSRLVSNSLALVNRITPNPKPKTKSRGLSEEQVFPRWVSAGDRKLLQGR
TIKANAVVAKDGTGNYETVSEAITAAHGNHGKYSTVIVGDDSVTGGTSVPDTATFTITGDGFIARDIGFK
NAAGPKGEQAIALSITSDHSVLYRCSIAGYQDTLYAAALRQFYRECDIYGTIDFIFGNAAAVFQNCYLFL
RRPHGKSYNVILANGRSDPGQNTGFSLQSCRIRTSSDFSPVKHSYSSYLGRPWKKYSRAIVMESYIDDAI
AERGWIEWPGSGSEVLKSLYFAEYSNYGPGARTSKRVTWPGFHLIGFEEATKFTVVKFIAGESWLPSTGV
KFISGLQ
>gnl|CDD|215376 PLN02699, PLN02699, Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
GGGKTEMISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGE
YPVITESRAGNDGLGVTLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKRVRILSQASKGQDI
RPVGCDIEKDAKVLKAGERLGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTLGRGQIRDSN
RAMLLAAAIQQQCKVVDLGIARDDEEELERILDEAISSGVDILLTSGGVSMGDRDFVKPLLEKRGTVYFS
KVLMKPGKPLTFAEIDAKSAPSNSKKMLAFGLPGNPVSCLVCFNLFVVPAIRYLAGWSNPHLLRVQARLR
EPIKLDPVRPEFHRAIIRWKLNDGSGNPGFVAESTGHQMSSRLLSMKSANALLELPATGNVLSAGTSVSA
IIISDISSKSLDESSTSSDPHSSRHGSTSKSIEAQNPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVNSS
SEKLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTGFTPRDVTPEATKEVIQKETPGLLYV
MMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHALKQIKGDKREKHPRHIPHA
QATDPVDTWERSYKAASGQGGEPGCSCSH
>gnl|CDD|215377 PLN02700, PLN02700, homoserine dehydrogenase family protein
MKKIPVLLLGCGGVGRHLLRHIVSCRSLHAKQGVRIRVVGVCDSKSLVLAEDVLNEELDDALLSEVCLAK
SKGSPLSALGALAGGCQVFNNSELSRKVIDIATLLGKSTGLVVVDCSASMETIGALNEAVDLGCCIVLAN
KKPLTSTLEDYDKLAAHPRRIRHESTVGAGLPVIASLNRILSSGDPVHRIVGSLSGTLGYVMSELEDGKP
FSEVVKQAKSLGYTEPDPRDDLGGMDVARKALILARLLGKRINMDSIKVESLYPEEMGPDLMSTDDFLHS
GLVELDLPIEERVKEASLKGCVLRYVCVIEGSSCQVGIRELPKDSALGRLRGSDNVVEIYSRCYSEQPLV
IQGAGAGNDTTAAGVLADILDLQDLFH
>gnl|CDD|178304 PLN02701, PLN02701, alpha-mannosidase
VDITTKDLYDRIEFLDKDGGAWKQGWRVKYRGDEWDREKLKVFVVPHSHNDPGWILTVEEYYQEQSRHIL
DTIVESLSKDPRRKFIWEEMSYLERWWRDASPSKKEAFTKLVKNGQLEIVGGGWVMNDEANSHYFAIIEQ
ITEGNMWLNDTIGVAPKNSWAIDPFGYSSTMAYLLRRMGFENMLIQRTHYEVKKELAQNKNLEYIWRQSW
DAEETTDIFVHMMPFYSYDIPHTCGPEPAICCQFDFARMRGFQYELCPWGKHPVETNDENVQERAMKLLD
QYRKKSTLYRTNTLLVPLGDDFRYISIDEAEAQFRNYQKLFDYINSNPSLKAEVKFGTLEDYFSTLRDEA
DRINYSRPGEVGSGEVPGFPSLSGDFFTYADRQQDYWSGYYVSRPFFKAVDRVLEQTLRAAEILFSFLLG
YCRRFQCEKLPTSFSYKLTAARRNLALFQHHDGVTGTAKDHVVVDYGTRMHTSLQDLQIFMSAAVEVLLG
IRHEKSDQTPSWFEPEQSRSKYDMLPVHKVINLREGKAHRVVFFNPLEQTREEVVMVVVDRPAVCVFDSN
WTCVPSQISPEWQHDGEKLFTGRHRLYWKASVPALGLETYFIANGNVSCEKAVPAKLKVFNSDDKFPCPE
PYSCSKLEGDTVEISNSHQTLGFDVKTGLLRKIKIHKNGSETVVGEEIGMYSSQGSGAYLFKPDGEAQPI
VQAGGLVVVSEGPLVQEVHSVPKTKWEKSPLSRSTRLYHGGKSVQDLSVEKEYHVELLGHDFNDKELIVR
FKTDIDNKRVFYSDLNGFQMSRRETYDKIPLQGNYYPMPSLAFLQGSNGQRFSVHSRQSLGVASLKNGWL
EIMLDRRLVQDDGRGLGQGVMDNRPMNVVFHLLLESNISSSPPASNPLPLQPSLLSHRVGAHLNYPMHAF
LAKKPQATSVENPQDTSFAPLAKPLPCDLHIVNFKVPRPSKYSQQEAEDPRFGLLLQRRGWDSSYCRKGG
TQCTTLANEPVNLFDMFKDLAVSKVKATSLNLLHDDAEMLGYRKQAGSAAQEGIVLISPMEIQAYKLDLR
>gnl|CDD|215378 PLN02702, PLN02702, L-idonate 5-dehydrogenase
MGKGGMSSGEGSGVEEENMAAWLVGVNTLKIQPFKLPPLGPHDVRVRMKAVGICGSDVHYLKTMRCADFV
VKEPMVIGHECAGIIEEVGSEVKHLVVGDRVALEPGISCWRCNLCKEGRYNLCPEMKFFATPPVHGSLAN
QVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRANIGPETNVLVMGAGPIGLVTMLAARAFGAPRIV
IVDVDDERLSVAKQLGADEIVLVSTNIEDVESEVEEIQKAMGGGIDVSFDCVGFNKTMSTALEATRAGGK
VCLVGMGHNEMTVPLTPAAAREVDVVGVFRYRNTWPLCLEFLRSGKIDVKPLITHRFGFSQKEVEEAFET
SARGGNAIKVMFNL
>gnl|CDD|178306 PLN02703, PLN02703, beta-fructofuranosidase
MAASETVLRVPLGSLSQSCYLASFFVNSTPNLSFKPVSYNRKKVRCTNSHEYSSVSACQDADGSFHSSNE
CLKGKKFVQMRCKCQKHDVEESIRSTLLPSDGLKSDLDEMPLPVNGSFSSNGNAQSVGTKSIEDEAWDLL
RQSVVFYCGSPIGTIAANDPSSTSVLNYDQVFIRDFIPSGIAFLLKGEYDIVRNFILYTLQLQSWEKTMD
CHSPGQGLMPCSFKVKTVPLDGDDSMTEEVLDPDFGEAAIGRVAPVDSGLWWIILLRAYGKCTGDLSVQE
RVDVQTGIKMILKLCLADGFDMFPTLLVTDGSCMIDRRMGIHGHPLEIQALFYSALVCAREMLTPEDGSV
DLIRALNNRLVALNFHIREYYWLDLKKINEIYRYQTEEYSYDAVNKFNIYPDQIPSWLVDFMPNRGGYLI
GNLQPAHMDFRFFTLGNLWSIVSSLATNDQSHAILDLIEAKWAELVADMPLKICYPAMEGEEWRIITGSD
PKNTPWSYHNGGAWPTLLWQLTVASIKMGRPEIAEKAVELAERRISLDKWPEYYDTKRARFIGKQARLYQ
TWSIAGYLVAKLLLANPAAAKFLTSEEDSDLRNAFSCMISANPRRTRGPKKAQQPFIV
>gnl|CDD|166345 PLN02704, PLN02704, flavonol synthase
MEVERVQAIASSSLLKETIPEEFIRSEKEQPAITTFHGVDPQVPTIDLSDPDEEKLTRLIAEASKEWGMF
QIVNHGIPSEVISKLQKVGKEFFELPQEEKEVYAKPPDSKSIEGYGTKLQKEPEGKKAWVDHLFHRIWPP
SAINYQFWPKNPPSYREVNEEYAKYLRGVADKLFKTLSLGLGLEEDELKEAVGGEELEYLLKINYYPPCP
RPDLALGVVAHTDMSAITILVPNEVQGLQVFRDDHWFDVKYIPNALVIHIGDQIEILSNGKYKSVLHRTT
VNKEKTRMSWPVFLEPPSELAVGPLPKLINEDNPPKFKTKKFKDYVYCKLNKIPQ
>gnl|CDD|178307 PLN02705, PLN02705, beta-amylase
MHTLNNTITTTTGSQDPNLDPIPQPDPFPNRNRNQPQSRRPRGFAATAAAAAIAPTENDVNNGNISSGGG
GGGGGKGKREREKEKERTKLRERHRRAITSRMLAGLRQYGNFPLPARADMNDVLAALAREAGWTVEADGT
TYRQSPQPSHVGSFPVRSVESPLSSSTLKNCAKAAIESQQHSVLRIDESLSPVSLDSVVIAESDHPGNGR
YTSTSPITSVGCLEADQLIQDVHSGEHENDFTETFYVPVYVMLAVGIINNFCQLVDPEGVRQELSHMKSL
NVDGVVVDCWWGIVEGWNPQKYVWSGYRELFNIIREFKLKLQVVMAFHEYGGNASGNVMISLPQWVLEIG
KDNQDIFFTDREGRRNTECLSWSIDKERVLKGRTGIEVYFDFMRSFRSEFDDLFVEGLITAVEIGLGASG
ELKYPSFPERMGWIYPGIGEFQCYDKYSQQNLRKAAKSRGHSFWARGPDNAGQYNSRPHETGFFCERGDY
DSYYGRFFLHWYSQLLIDHADNVLSLANLAFEETKIIVKIPAVYWWYKTASHAAELTAGYYNPTNQDGYS
PVFETLKKHSVTVKFVCSGLQMSPNENDEALADPEGLSWQVLNSAWDRGLTVAGENAITCYDREGCMRLI
EIAKPRNHPDHYHFSFFVYQQPSPLVQGTTCFPELDYFIKCMHGDIRDKQF
>gnl|CDD|178308 PLN02706, PLN02706, glucosamine 6-phosphate N-acetyltransferase
GDTGEKFKVRRLEISDKSKGFLELLQQLTVVGDVTEEEFEARFQELASLGDDHLICVIEDAASGRIIATG
SVFVERKFIRNCGKVGHIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENKAFYEKCGYV
RKEIQMVKYF
>gnl|CDD|178309 PLN02707, PLN02707, Soluble inorganic pyrophosphatase
RARLAPAQVPSRARPPVSRRLFSCASAVNAAYAVEEEGEAETLDYRVFFSDGSGKKVSPWHDIPLHAGDG
TFNFVVEIPKETSAKMEVATDEPFTPIKQDTKKGKLRDYPYNINWNYGLLPQTWEDPTHANPEVEGAFGD
NDPVDVVEIGERAAKIGEVLKVKPLGVLAMIDEGELDWKVVAISADDPKASLVNDVDDVEKHFPGTLTAI
RDWFRDYKIPDGKPANKFGLDNKPMDKDYALKVIEETNEAWAKLVKRSIPAGELSLV
>gnl|CDD|215379 PLN02708, PLN02708, Probable pectinesterase/pectinesterase inhibitor
MASLLLLLLLSLLLFHSPSSSSNRHHHHHTPSPSPPPPSSPSTPPQILLACNATRFPDTCVSSLSNAGRV
PPDPKPIQIIQSAISVSRENLKTAQSMVKSILDSSAGNVNRTTAATNCLEVLSNSEHRISSTDIALPRGK
IKDARAWMSAALLYQYDCWSALKYVNDTSQVNDTMSFLDSLIGLTSNALSMMASYDIFGDDTGSWRPPKT
ERDGFWEPSGPGLGSDSGLGFKLGVPSGLTPDVTVCKDGNCCYKTVQEAVNAAPDNNGDRKFVIRIKEGV
YEETVRVPLEKKNVVFLGDGMGKTVITGSLNVGQPGISTYNTATVGVLGDGFMARDLTIQNTAGPDAHQA
VAFRSDSDLSVIENCEFLGNQDTLYAHSLRQFYKSCRIQGNVDFIFGNSAAVFQDCAILIAPRQLKPEKG
ENNAVTAHGRTDPAQSTGFVFQNCLINGTEEYMKLYRSNPKVHKNFLGRPWKEYSRTVFIGCNLEALITP
QGWMPWSGDFALKTLYYGEFENSGPGSNLSQRVTWSSQIPAEHVDVYSVANFIQGDEWIPTSS
>gnl|CDD|178311 PLN02709, PLN02709, nudix hydrolase
MSSTTTDSTELQNLIKLFQNCETHLRQHFPAKSSAVLVCLYQEQREDKNELRVILTKRSSTLSSHPGEVA
LPGGKRDEEDKDDIATALREAREEIGLDPSLVTIISVLEPFVNKKGMSVAPVIGFLHDKKAFKPLPNPAE
VEEIFDVPLEMFLKDKNKRAEEREHEGERYLLQYFDYYSEDKERNFIIWALTAGILIRVASIVYQRLPEF
QERKPRFWNQPN
>gnl|CDD|215380 PLN02710, PLN02710, farnesyltranstransferase subunit beta
RVSSELPRLTVTQREQWKVEAKVFDIYRSFASAPPNAQSVMLELWREKHLEYLTRGLRQLGPSFSVLDAN
RPWLCYWILHSIALLGESLDDELENDTIDFLSRCQDPNGGYGGGPGQLPHLATTYAAVNTLVTIGGERAL
SSINREKLYTFLLRMKDPSGGFRMHDGGEMDVRACYTAISVASLLNILDDELVKGVGDYILSCQTYEGGI
GGEPGAEAHGGYTFCGLAAMILINEVDRLDLPSLINWVVFRQGVEGGFQGRTNKLVDGCYSFWQGGVFAL
LQQLVTIVDEQLQTGGSSIMFEELEDDACETSSSGKDDAGDTDSADYSKVGFDFIKASNQQMGPLFHSIA
LQQYILLCSQVLDGGLRDKPGKSRDYYHTCYCLSGLSVAQYSASKDEDSPPLPRHVLGPYSNLLEPIHPL
YNVVLDKYHEAIEFFSSKA
>gnl|CDD|215381 PLN02711, PLN02711, Probable galactinol--sucrose galactosyltransferase
MAPSLSKSNSGAMGLVDGLNPSLITLEGSNFLANGHPFLSDVPDNITLTPSPYLPDNKPITVGAGSFVGF
DAGEPKSRHVVPIGKLKNIRFMSIFRFKVWWTTHWVGSNGRDVENETQMMILDKSDSGRPYVLLLPLIEG
PFRASLQPGEDDNVDICVESGSTKVCGSEFRSVLYMHAGDDPYKLVKDAMKVVRVHLGTFKLLEEKTPPG
IVDKFGWCTWDAFYLTVHPQGVWEGVKGLVDGGCPPGLVLIDDGWQSICHDEDPISDQEGMNRTVAGEQM
PCRLLKFEENYKFRDYVSPKSLSNKGMGAFIRDLKEEFKTVDYVYVWHALCGYWGGLRPNVPGLPESKVV
APKLSPGLKMTMEDLAVDKIVNNGVGLVPPELAYQMYEGLHSHLQSVGIDGVKVDVIHLLEMLCEEYGGR
VELAKAYYKALTASVRKHFNGNGVIASMEHCNDFMFLGTEAISLGRVGDDFWCTDPSGDPNGTFWLQGCH
MVHCAYNSLWMGNFIHPDWDMFQSTHPCAEFHAASRAISGGPIYVSDSVGKHNFPLLKRLVLPDGSILRC
QYYALPTRDCLFEDPLHDGKTMLKIWNLNKFTGVIGAFNCQGGGWCRETRRNKCASQFSHTVTAKASPKD
IEWNSGKSPISIEGVQVFAVYLFQSKKLVLSKPSENLEISLEPFNFELITVSPVTTLPGKSIQFAPIGLV
NMLNTGGAIQSLAYDDAESSVQIGVKGSGEMRVFASEKPRSCKIDGEEVEFGYEDCMVVVQVPWSGSSGL
SLIEYLF
>gnl|CDD|215382 PLN02712, PLN02712, arogenate dehydrogenase
SPPPPPQPPPSLFPTSKPTTMSPRLSLSIKSQSATATDKQPLPNSNPDNTTQLKIAIIGFGNYGQFLAKT
LISQGHTVLAHSRSDHSLAARSLGVSFFLDPHDLCERHPDVILLCTSIISTENVLKSLPLQRLKRNTLFV
DVLSVKEFAKNLLLDYLPEDFDIICSHPMFGPQSAKHGWDGLRFVYEKVRIGNEELRVSRCKSFLEVFER
EGCKMVEMSCTEHDKYAAESQFITHTVGRVLEMLKLESTPINTKGYESLLDLVENTCGDSFDLYYGLFMY
NKNSLEMLERLDLAFEALRKQLFGRLHGVVRKQLFGNEEKKVHVQPNHAENHTYGAAFLSSLDMMRFQGV
AQKYEYNAQVSGCVNDGSKLKIAIVGFGNFGQFLAKTMVKQGHTVLAYSRSDYSDEAQKLGVSYFSDADD
LCEEHPEVILLCTSILSTEKVLKSLPFQRLKRSTLFVDVLSVKEFPRNLFLQHLPQDFDILCTHPMFGPE
SGKNGWNNLAFVFDKVRIGSDDRRVSRCDSFLDIFAREGCRMVEMSCAEHDWHAAGSQFITHTMGRLLEK
LGLESTPINTKGYETLLNLVENTAGDSFDLYYGLFMYNVNAMEQLERLDLAFESLKKQLFGRLHGVLRKQ
LFKSSEKSQVLREESLVSKVSQKTAALLTSLDSVQNN
>gnl|CDD|215383 PLN02713, PLN02713, Probable pectinesterase/pectinesterase inhibitor
MSSKLILLTTLALLLLLFFSSSSASDPPPSTPVSPSTICNTTPDPSFCKSVLPHNQPGNVYDYGRFSVRK
SLSQSRKFLSLVDRYLKRNSTLLSKSAIRALEDCQFLAGLNIDFLLSSFETVNSSSKTLSDPQADDVQTL
LSAILTNQQTCLDGLQAASSAWSVRNGLAVPLSNDTKLYSVSLALFTKGWVPKKKKGRPKTKRKAHFKPF
RAFRNGRLPLKMTEKTRAVYESVSRRKLLDGDANAVLVSDIVTVNQNGTGNFTTINDAVAAAPNNTDGSN
GYFVIYVTAGVYEEYVSIPKNKKYLMMIGDGINQTVITGNRSVVDGWTTFNSATFAVVGQNFVAVNITFR
NTAGPAKHQAVALRSGADLSTFYSCSFEAYQDTLYTHSLRQFYRECDIYGTVDFIFGNAAVVFQNCNLYP
RLPMQGQFNTITAQGRTDPNQNTGTSIQNCTIKAADDLASSNYTVKTYLGRPWKEYSRTVVMQSYIDGLI
DPAGWMPWSGDFALSTLYYAEYNNTGPGSDTTNRVTWPGYHVINATDAANFTVSNFLLGDGWLPQTGVPF
TSGLIS
>gnl|CDD|178316 PLN02714, PLN02714, thiamin pyrophosphokinase
ALVVLNQRLPRFTPLLWEHAKLRVCADGGANRLYDEMPLLFPDEDPLAVRNRYKPDVIKGDMDSIRPEVL
DFYSNLGTKIVDESHDQDTTDLHKCIAYIRDSTPDLDKSNLCILVLGALGGRFDHEAGNINVLYRFPDLR
IVLLSDDCLIRLLPATHRHEIHIDSSVEGPHCGLIPIGGPSASTTTTGLQWNLDNTEMRFGGLISTSNIV
KEDKVTVESDSDLLWTISI
>gnl|CDD|178317 PLN02715, PLN02715, lipid phosphate phosphatase
MTIGSFFSSLLFWRNSQDQEAQRGRIQEIDLGVHTIKSHGGRVASKHKHDWIILVILIAIEIGLNLISPF
YRYVGKDMMTDLKYPFKDNTVPIWSVPVYAVLLPIILFVCFYLKRRCVYDLHHSILGLLFAVLITGVITD
SIKVATGRPRPNFYWRCFPDGKELYDALGGVICHGKAAEVKEGHKSFPSGHTSWSFAGLTFLSLYLSGKI
KAFNGEGHVAKLCLVIFPLLAACLVGISRVDDYWHHWQDVFAGALIGILVAAFCYRQFYPNPYHEEGWGP
YAYFKAAQERGVPVASSQNGDALRAMSLQMDSTSLENMESGTSTAPR
>gnl|CDD|178318 PLN02716, PLN02716, nicotinate-nucleotide diphosphorylase (carboxylating)
MAAEMAMAIPPPSHPTYDIEAVIKLALAEDAGDRGDVTCLATIPGDMEAEATFLAKADGVLAGIALADMV
FEEVDPSLKVEWAAIDGDFVHKGLKFGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAKPACIL
ETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDNHIAAAGGITNAVQSADKYLEEKGLSMKIEVET
RTLEEVKEVLEYLSDTKTSLTRVMLDNMVVPLENGDVDVSMLKEAVELINGRFETEASGNVTLDTVHKIG
QTGVTYISSGALTHSVKALDISLKIDTE
>gnl|CDD|178319 PLN02717, PLN02717, uridine nucleosidase
KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLK
GGTKPRIADFVHGSDGLGNTNLPPPKGKKIEKSAAEFLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSF
AKKVGQIVVLGGAFFVNGNVNPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRDSK
GKYAQFLCDICKFYRDWHRKSYGIDGIYLHDPTALLAAVRPSLFTYKEGVVRVETEGICRGLTLFDNGLK
RWNGENAWTGRPPVKVAVTVDAPAVVELVKERLMAS
>gnl|CDD|178320 PLN02718, PLN02718, Probable galacturonosyltransferase
MKQVRRWQRILILSLLSLSVFAPLIFVSNRLKSITPVGRKEFIEELSTIRYRTDDLRLSAIEQEEGEGLK
GPKLVIYQDGDFNSVVSYNSSDKNNDSLESEVDGGNNHKPKEEQAQVSQKTTVSSSEEVQISARDIQLNH
KTQFNPPTVKHEKNTRVQPRRATDEKVKEIRDKIIQAKAYLNLAPPGSNSQLVKELRLRTKELERAVGDA
TKDKDLSKSALQRMKSMEVTLYKASRVFPNCPAIATKLRAMTYNTEEQVRAQKNQAAYLMQLAARTTPKG
LHCLSMRLTAEYFALDPEKRQLPNQQRYNDPDLYHYVVFSDNVLACSVVVNSTISSSKEPEKIVFHVVTD
SLNYPAISMWFLLNPPGKATIQILNIDDMNVLPADYNSLLMKQNSHDPRYISALNHARFYLPDIFPGLNK
IVLFDHDVVVQRDLSRLWSLDMKGKVVGAVETCLEGEPSFRSMDTFINFSDPWVAKKFDPKACTWAFGMN
LFDLEEWRRQKLTSVYHKYLQLGVKRPLWKAGSLPIGWLTFYNQTVALDKRWHVLGLGHESGVGASDIEQ
AAVIHYDGVMKPWLDIGIGKYKRYWNIHVPYHHPYLQQCNIHE
>gnl|CDD|178321 PLN02719, PLN02719, triacylglycerol lipase
MATIPSHNFHLRLPHMINQRTQYSLSFKPHFSHSTLITFPARASPARAMSRTDEEASISTRLEPESYGLT
TAEDIRRRDGEAKESKRLRDTWRKIQGEDDWAGLMDPMDPVLRSELIRYGEMAQACYDAFDFDPFSRYCG
SCRFTRRHLFDSLGIIDSGYEVARYLYATSNINLPNFFSKSRWSKVWSKNANWIGYVAVSDDDEATRCRL
GRRDIAIAWRGTVTRLEWIADLKDFLKPVSGNGFRCPDPAVKAESGFLDLYTDKDTCCNFSKFSAREQVL
TEVKRLVERYGDEEGEELSITVTGHSLGGALAVLSAYDVAEMGLNRTRKGKVIPVTAFTYGGPRVGNIRF
KERIEELGVKVLRVVNEHDVVAKSPGLFLNERAPQALMKLAGGLPWCYSHVGEMLPLDHQKSPFLKPTVD
LSTAHNLEALLHLLDGYHGKGQRFVLSSGRDPALVNKASDFLKDHFMVPPYWRQDANKGMVRNTDGRWIQ
PDRIRADDHHAPDIHQLLTQLHHPSQLL
>gnl|CDD|178322 PLN02720, PLN02720, complex II
MSESFFKKHWEGLKDFWRDRFSFLENYARFSKRDKPLPPWSDSDVDEFIASDPVYGPQLKTMREAATFAV
TGAAVGAVSTAGVAWKYSKSPHGAALAFLGGGVFGWAFGQEVANHWLQLYKFDTMAANVKFLDWWERKNG
>gnl|CDD|178323 PLN02721, PLN02721, threonine aldolase
GRMVSRVVDLRSDTVTKPTDAMRAAMANAEVDDDVLGYDPTALRLEEEMAKIFGKEAALFVPSGTMGNLI
SVLVHCDVRGSEVILGDNSHIHLYENGGISTLGGVHPRTVKNNEDGTMDLDAIEAAIRPKGDDHFPTTRL
ICLENTHANCGGRCLSVEYTDKVGELAKRHGLKLHIDGARIFNASVALGVPVHRLVKAADSVSVCLSKGL
GAPVGSVIVGSKSFIRKAKRLRKTLGGGMRQVGVLAAAALVALQENVPKLEDDHKKAKLLAEGLNQIKGL
RVNVAAVETNIVYFDITDGSRITAEKLCKSLEEHGVLLMPGNSSRIRVVTHHQISDSDVQYTLSCFQQAA
LTL
>gnl|CDD|166363 PLN02722, PLN02722, indole-3-acetamide amidohydrolase
MATNPDYGAFMEKFVLSPTSSSHDLPLHGLTFAVKDIFDVEGYVTGFGNPDWARTHSAATSTAPAVLAVL
RGGATCVGKTIMDEMAYSINGENAHYGTPTNPIAPDRVPGGSSSGSAVAVGAKLVDFSLGTDTGGSVRVP
ASYCGIFGFRPSHGAVSTVGVIPMAQSFDTVGWFARDPVILKRVGHVLLQQPDVNPIKPSQIIIAEDCFQ
LSSIPHDRLVQVLVKSVEKLFGGGDIVKHVNLGDYVEDKVPSLKHFMSKEIKEQEYNIPSLAALSSAMRL
LQRYEFKINHGEWITAVKPEFGPGISERIWEAVRTTEEKIDACQSVKTELRAALTTLLGEFGVLVIPTVP
GPPPKLQADPTTLESFRARAFSLLSIAGVSGFCQVSIPLGLHDNLPVSVSLLAKHGSDGFLLNLVESLYG
TI
>gnl|CDD|178324 PLN02723, PLN02723, 3-mercaptopyruvate sulfurtransferase
MASSGSETKANYSTQSISTNEPVVSVDWLHANLREPDVKVLDASWYMPDEQRNPIQEYQVAHIPGALFFD
LDGISDRTTDLPHMLPSEEAFAAAVSALGIENKDGVVVYDGKGIFSAARVWWMFRVFGHEKVWVLDGGLP
KWRASGYDVESSASGDAILKASAASEAIEKVYQGQTVSPITFQTKFQPHLVWTLEQVKKNIEDKTYQHID
ARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSQTLLPAEELKKRFEQEGISLDSPIVASCGTGV
TACILALGLHRLGKTDVPVYDGSWTEWGALPDTPVATSTS
>gnl|CDD|215384 PLN02724, PLN02724, Molybdenum cofactor sulfurase
KESFLKEFGGYYGYPDGPKPIDELRATEFARLKGVVYLDHAGATLYSESQLEAALADFSSNVYGNPHSQS
DSSMRSSDTIESARQQVLEYFNAPPSDYACVFTSGATAALKLVGETFPWSSESHFCYTLENHNSVLGIRE
YALEKGAAAIAVDIEEAANQPTNSQGSVVVKSRGLQRRNTSKLQKREDDGEAYNLFAFPSECNFSGAKFP
LDLVKLIKDNQHSNFSKSGRWMVLLDAAKGCGTSPPDLSRYPADFVVVSFYKIFGYPTGLGALLVRRDAA
KLLKKKYFGGGTVAASIADIDFVKRRERVEQRFEDGTISFLSIAALRHGFKLLNRLTISAIAMHTWALTH
YVANSLRNLKHGNGAPVCVLYGNHTFKLEFHIQGPIVTFNLKRADGSWVGHREVEKLASLSGIQLRTGCF
CNPGACAKYLGLSHKDLQANFEAGHVCWDDQDVIHGRPTGAVRVSFGYMSTFEDCQKFIDFIISSFVSTP
KKRGNVTLRSKRTIPLPVLERKESFDSHRLKSITVYPIKSCAGFSVERWPLSETGLLYDREWMIQSLTGE
ILTQKKVPEMCLITTFIDLESGKLVVRAPRCDHKLEIPLESDSQHEESGEVILCGNRAESMSYGTEINEW
FTNALGRRCTLVRKSSSNTRVCRNRNPSHSPCGDDESRLSFANEGQFLLISEASVEDLNRRLATGQEDAK
IRLDPTRFRPNLVVSGGEAYAEDEWQSLSIGDAEFTVLGGCNRCQMINIDQETGLVNPSNEPLATLASYR
RVKGKILFGILLRYEISDKRDQWIAVGSRVNPRIE
>gnl|CDD|178326 PLN02725, PLN02725, GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase
FVAGHRGLVGSAIVRKLEALGFTNLVLRTHKELDLTRQADVEAFFAKEKPTYVILAAAKVGGIHANMTYP
ADFIRENLQIQTNVIDAAYRHGVKKLLFLGSSCIYPKFAPQPIPETALLTGPPEPTNEWYAIAKIAGIKM
CQAYRIQYGWDAISGMPTNLYGPHDNFHPENSHVIPALIRRFHEAKANGAPEVVVWGSGSPLREFLHVDD
LADAVVFLMRRYSGAEHVNVGSGDEVTIKELAELVKEVVGFEGELVWDTSKPDGTPRKLMDSSKLRSLGW
DPKFSLKDGLQETYKWYLENYETGGK
>gnl|CDD|215385 PLN02726, PLN02726, dolichyl-phosphate beta-D-mannosyltransferase
MEAPGEGAMKYSIIVPTYNERLNIALIVYLIFKALQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRI
LLRPRPGKLGLGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGW
DLRRKLTSRGANVLAQTLLWPGVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEV
PITFVDRVYGESKLGGSEIVQYLKGLLYLLLTT
>gnl|CDD|215386 PLN02727, PLN02727, NAD kinase
MARLSPVTGILSSCLCSVKLNSDGKLLGFGFGFWQRKEPLKRRLKFVVSAELSKSFSSNLGLDSQNFQSR
DLSQLPWIGPVPGDIAEVEAYCRIFRAAERLHAALMDTLCNPLTGECPVSYDFTSEEKPLLEDKIVSVLG
CMLSLLNKGREEVLSGRSSIMSSFRGSEVSAMEDKLPPLAIFRGEMKRCCESLHVALENYLTPDDDRSLD
VWRKLQRLKNVCYDAGFPRSDDYPCHTLFANWNPVYLSTSKEDIDSKESEAAFWRGGQVTEEGLKWLLEK
GFKTIVDLRAEIVKDNFYQAAVDDAISSGKIEVVKIPVEVRTAPSAEQVEKFASLVSDSSKKPIYLHSKE
GVWRTSAMVSRWKQYMTRSAERLLGQNSVVNGNGKLDQETGSLQETNDKDSSSNGSESGESCSIKDETGR
SNLEAYNSLPSDQSTQQGEMVGTGVESQSNFNMESDPLKAQVPPCDVFSKKEMSKFFRSKKIYPPTYLNY
RRKGFEKLPVPQFTGVTQGSKIDDTDSISRLVETGRSNGLVSEKNSSPKYQSSEFDNGKSSNGSSFASDG
SLSVASSITNGNPSNNGASSSTVSDNLERSVASVSVRESQRSNGKASLGSSDDELGAIEGNMCASATGVV
RVQSRRKAEMFLVRTDGFSCTREKVTESSLAFTHPSTQQQMLMWKSTPKTVLLLKKLGQELMEEAKEVAS
FLYHQEKMNVLVEPDVHDIFARIPGFGFVQTFYSQDTSDLHERVDFVACLGGDGVILHASNLFRGAVPPV
VSFNLGSLGFLTSHYFEDFRQDLRQVIHGNNTLDGVYITLRMRLRCEIFRNGKAMPGKVFDVLNEVVVDR
GSNPYLSKIECYEHDRLITKVQGDGVIVATPTGSTAYSTAAGGSMVHPNVPCMLFTPICPHSLSFRPVIL
PDSARLELKIPDDARSNAWVSFDGKRRQQLSRGDSVRISMSQHPLPTVNKSDQTGDWFRSLIRCLNWNER
LDQKAL
>gnl|CDD|215387 PLN02728, PLN02728, 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
SRLTSTALASAADDETSAVVKEKSVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKE
IVVVCDPSYRDVFEEAVENIDVPLKFALPGKERQDSVFNGLQEVDANSELVCIHDSARPLVTSADIEKVL
KDAAVHGAAVLGVPVKATIKEANSDSFVVKTLDRKRLWEMQTPQVIKPELLRRGFELVEREGLEVTDDVS
IVEALKHPVFITEGSYTNIKVTTPDDMLVAERILNERSDAEV
>gnl|CDD|215388 PLN02729, PLN02729, PSII-Q subunit
MAHLANLNGLTETLPAIPKLRNLQRTRKRGKIIGFLCKKAENFQEDSFQTTRRLALGLASIALIGNSGNG
VSLAEDNGFWLDGPLPVPSVDNKIVNEKTGTRSFLKKGIYMADIGTKGRMYRVKKYAFDLLALEDLIGPD
TLNYVRKYLRLKSTFMYYDFDKLISAAPVDDKQPLTDLANRLFDNFEKLEDASKRKNLSETESSYKDTKT
LLQEVMDRMA
>gnl|CDD|178331 PLN02730, PLN02730, enoyl-[acyl-carrier-protein] reductase
SGLPIDLRGKRAFIAGVADDNGYGWAIAKALAAAGAEILVGTWVPALNIFETSLRRGKFDESRKLPDGSL
MEITKVYPLDAVFDTPEDVPEDVKTNKRYAGSSNWTVQEVAESVKADFGSIDILVHSLANGPEVTKPLLE
TSRKGYLAAISASSYSFVSLLQHFGPIMNPGGASISLTYIASERIIPGYGGGMSSAKAALESDTRVLAFE
AGRKYKIRVNTISAGPLGSRAAKAIGFIDDMIEYSYANAPLQKELTADEVGNAAAFLASPLASAITGATI
YVDNGLNAMGLALDSPTLEDLDI
>gnl|CDD|178332 PLN02731, PLN02731, Putative lipid phosphate phosphatase
MARFSFPCFPNFGGFNQHRMREAQLGGHTLRSHGMTVARTHMHDWIILVLLVILECVLLIIHPFYRFVGK
DMMTDLSYPLKSNTVPIWSVPVYAMLLPLVIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAV
GRPRPDFFWRCFPDGKALYDSLGDVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLSGKIQAFDGK
GHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICYLQFFPPPYHTEGWGPYAYFQV
LEAARVQGAANGAVQQPPPQVNNGEEEDGGFMGLHLVDNPTMRREEDVETGRG
>gnl|CDD|215389 PLN02732, PLN02732, Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit
MALTVVKSALEAIREKGLGGFLRMLREEGYLRCLADGNLLQTKIHNIGATLVGVDKFGNKYYQKLGDTQY
GRHRWVEYAEKSRYNASQVPAEWHGWLHFITDHTGDELLMLKPKRYGLEHKENFSGEGEEYIYHSKGHTL
NPGQKDWTRYQSWQPTKTQ
>gnl|CDD|215390 PLN02733, PLN02733, phosphatidylcholine-sterol O-acyltransferase
ELWLPLIKKGQDPYVDPDLDPVLLVPGIGGSILNAVDKDGGNEERVWVRIFAADHEFRKKLWSRYDPKTG
KTVSLDPKTEIVVPDDRYGLYAIDILDPDVIIRLDEVYYFHDMIEQLIKWGYKEGKTLFGFGYDFRQSNR
LPETMDGLKKKLETVYKASGGKKVNIISHSMGGLLVKCFMSLHSDVFEKYVNSWIAIAAPFQGAPGFITD
SLLTGVSFVEGWESEFFVSKWSMHQLLIECPSIYELMANPDFKWEEPPELQVWRKKSDNDGNSSVVLESY
GPLESIEVFEDALSNNTLNYDGEKIPLPFNFDILKWANETRRILSSAKLPKGVKFYNIYGTSLDTPFDVC
YGSEKSPIEDLSEILHTEPEYTYVDGDGTVPVESAKADGLNAVARVGVPGDHRGILRDEHVFRILKHWLK
VGEPDPFYNPINDYVILPTA
>gnl|CDD|178335 PLN02734, PLN02734, glycyl-tRNA synthetase
SEDSLRDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGDGAAS
KEAFRQAVVNTLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPE
VVLKASGHVDKFTDLMVKDEKTGTCFRADHLLKDFCEEKLEKDLTISAEKAAELKDVLAVLDDLSAEELG
AKIKEYGIKAPDTKNPLSDPYPFNLMFQTSIGPSGLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQ
IGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEVADLEFLLFPREEQLGGQKAKPMRLGEA
VSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIECSYGWIECVGIADRS
AYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEKEAMEMKAKLE
SKGEAEFYVCTLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLN
VFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVD
SDGSVTIRERDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYPAHSSAADDE
>gnl|CDD|215391 PLN02735, PLN02735, carbamoyl-phosphate synthase
SSLADTVTRAWSAATKAGKRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATI
MTDPETADRTYIAPMTPELVEQVIAKERPDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIK
KAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGEFPLIIRPAFTLGGTGGGIAYNKEEFETICK
AGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQR
LRDYSVAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTLD
QIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLET
GFSGWGCAKVKELDWDWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQ
FLKSRSLSELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMY
SSYDGECESAPTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDR
LYFEPLTVEDVLNVIDLERPDGIIVQFGGQTPLKLALPIQKYLDKNPPPSASGNGNVKIWGTSPDSIDAA
EDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAV
EVDPERPVLVDKYLSDATEIDVDALADSEGNVVIGGIMEHIEQAGVHSGDSACSLPTQTIPSSCLATIRD
WTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSGKSLKDLGFT
EEVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGTVFISLN
DLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEGRPHAGDMLANGQIQLMVITSSGD
ALDQKDGRQLRRMALAYKVPIITTVAGALATAQAVKSLKECPIEMIALQDFF
>gnl|CDD|178337 PLN02736, PLN02736, long-chain acyl-CoA synthetase
EFVHEQGYSVVLPEKLQTGKWNVYRSARSPLKLVSRFPDHPEIGTLHDNFVYAVETFRDYKYLGTRIRVD
GTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPD
AVKFIVNHAEVAAIFCVPQTLNTLLSCLSEIPSVRLIVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRS
SPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQ
IVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQ
ALENGKNPSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGM
DEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQPYPRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLH
TGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEV
LKAWAASEGIKYEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKV
KRPQAKAYFAKAISDMYAELA
>gnl|CDD|215392 PLN02737, PLN02737, inositol monophosphatase family protein
MSLRFSRLPRSATPLRFPASCIPRTFARQHRSRLAALRAGSSRSLARRPTPAVLSETPNQAKYPRVGAAS
TGPIPAEELLAVAELAAKTGAEVVMEAVNKPRNISYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGE
EGGVIGDSSSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEFVGGPMCWNTRTFSASAGG
GAFCNGQKIHVSQTDKVERSLLVTGFGYEHDDAWATNIELFKEFTDVSRGVRRLGAAAVDMCHVALGIVE
AYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGKFSVFDRSVLVSNGVLHPKLLDRIGPATEKLKSKGIDF
SLWFKPEGYRTDF
>gnl|CDD|215393 PLN02738, PLN02738, carotene beta-ring hydroxylase
MAMNFPLSATPISAFAMAATSSAAAQAPRPCRLHLRLLPPAKPAAASRRRRLVLRCASSNGRGPGGESVE
DGVKSVERLREEKRRAELSARIASGEFTVQKPGFPATLRNGLAKLGPPGELLAFLFTWVEAGEGYPKIPE
AKGSISAVRGEAFFIPLYELFLTYGGIFRLTFGPKSFLIVSDPSIAKHILRDNSKAYSKGILAEILEFVM
GKGLIPADGEIWRVRRRAIVPALHQKYVAAMISLFGQASDRLCQKLDAAASDGEDVEMESLFSRLTLDII
GKAVFNYDFDSLSNDTGIVEAVYTVLREAEDRSVSPIPVWEIPIWKDISPRQRKVAEALKLINDTLDDLI
AICKRMVEEEELQFHEEYMNERDPSILHFLLASGDDVSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSK
EPSVVAKLQEEVDSVLGDRFPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLENDMLGGYPIKRGEDI
FISVWNLHRSPKHWDDAEKFNPERWPLDGPNPNETNQNFSYLPFGGGPRKCVGDMFASFENVVATAMLVR
RFDFQLAPGAPPVKMTTGATIHTTEGLKMTVTRRTKPPVIPNLPMTPISDSPENVSSTTSMPSSAGEVSS
AES
>gnl|CDD|215394 PLN02739, PLN02739, serine acetyltransferase
MACINGENCDFSCSSSLSSLPMIVSRNFSARDDGETGDEFPFERGFPVYARGTLNPVADPVLLDFTNSRY
DPIWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRG
IQSSIRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHP
AARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGA
GAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLTMEYDATREFFQNVAVAYRETIPNGSSVSGSC
REKRH
>gnl|CDD|178341 PLN02740, PLN02740, Alcohol dehydrogenase-like
ASETQGKVITCKAAVAWGPGEPLVMEEIRVDPPQKMEVRIKILYTSICHTDLSAWKGENEAQRAYPRILG
HEAAGIVESVGEGVEDLKAGDHVIPIFNGECGDCRYCKRDKTNLCETYRVDPFKSVMVNDGKTRFSTKGD
GQPIYHFLNTSTFTEYTVLDSACVVKIDPNAPLKKMSLLSCGVSTGVGAAWNTANVQAGSSVAIFGLGAV
GLAVAEGARARGASKIIGVDINPEKFEKGKEMGITDFINPKDSDKPVHERIREMTGGGVDYSFECAGNVE
VLREAFLSTHDGWGLTVLLGIHPTPKMLPLHPMELFDGRSITGSVFGDFKGKSQLPNLAKQCMQGVVNLD
GFITHELPFEKINEAFQLLEDGKALRCLLHL
>gnl|CDD|178342 PLN02741, PLN02741, riboflavin synthase
LFTGIVEEMGEVKSLGVTDDGGFDLKIEASTVLDGVKLGDSIAVNGTCLTVTEFDGDEFTVGLAPETLRK
TSLGELKTGSLVNLERALRPGSRMGGHFVQGHVDGTGTIVEQEPEGDSLWVKVKADPELLKYIVPKGFIA
VDGTSLTVVDVDDEEGCFNFMLVPYTQQKVVIPLKKVGDKVNLEVDILGKYVER
>gnl|CDD|215395 PLN02742, PLN02742, Probable galacturonosyltransferase
MRRRPADFRRPVRRRLSQWIWWLLGGFSVLGLVLFVHKHSEIEPRPPLSERNYRKEEVNHEGLNFTEEML
SATSFSRQLADQITLAKAYVVIAKEHNNLQLAWELSAQIRNCQLLLSKAATRGEPITVEEAEPIIRDLAA
LIYQAQDLHYDSATTIMTLKAHIQALEERANAATVQSTKFGQLAAEALPKSLYCLGVRLTTEWFKNPKLQ
RKAEEKRNSPRLVDNNLYHFCVFSDNILATSVVVNSTVSNAKHPDQLVFHLVTDEVNYGAMQAWFAMNDF
KGVTVEVQKIEEFSWLNASYVPVLKQLQDSDTQSYYFSGSQDDGKTEIKFRNPKYLSMLNHLRFYIPEIY
PALEKVVFLDDDVVVQKDLTPLFSIDLHGNVNGAVETCLETFHRYHKYLNFSHPLISSHFDPDACGWAFG
MNVFDLVAWRKANVTAIYHYWQEQNVDRTLWKLGTLPPGLLTFYGLTEPLDRRWHVLGLGYDTNIDPRLI
ESAAVLHFNGNMKPWLKLAIERYKPLWERYVNYSHPYLQQCNFH
>gnl|CDD|215396 PLN02743, PLN02743, nicotinamidase
MVSDTVDLLKKELPVEQESLVLNGDVRTGLVLVDEVNGFCTVGAGNLAPREPDKQISKMVDESARLAREF
CERKWPVLAFLDSHHPDKPEHPYPPHCIVGTGEENLVPALQWLENDPNVTLRRKDCIDGFVGAIEKDGSN
VFVDWVNNNKIKVILVVGICTDICVLDFVASALSARNHGILPPLEDVVVYSRGCATYDLPLHVAKTIKGA
LAHPQELMHHMGLYMAKGRGAKVVSKVSF
>gnl|CDD|215397 PLN02744, PLN02744, dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
AYASRIINHSKKLRNVSNLLRREHAALVRYFSNSTRSSLGKGDDIAKRRGYPPLERRSQPKVSSLGLFGS
NISRTARKNGSPMTGSGLFKSLSSSQMQSARGFSSSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKV
SPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEEDIGKFKDYKPSSSAAPAA
PKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVK
ADIEDYLASGGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALR
SQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDA
DKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQFCAIINPPQSAILAVGSAEKRVI
PGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL
>gnl|CDD|178346 PLN02745, PLN02745, Putative pectinesterase/pectinesterase inhibitor
MAFQDFDKISERRNAERQQKFRKRIIIGAVSALVVVAAVAGGVFAYVSYENKSQNQSGNGNNSSKDSPVK
SESPVSQVDKIIQTVCNATLYKQTCENTLKKGTEKDPSLAQPKDLLKSAIKAVNDDLDKVLKKVLSFKFE
NPDEKDAIEDCKLLVEDAKEELKASISRINDEVNKLAKNVPDLNNWLSAVMSYQETCIDGFPEGKLKSEM
EKTFKSSQELTSNSLAMVSSLTSFLSSFSVPKVLNRHLLAKESNSPSLEKDGIPSWMSNEDRRMLKAVDV
DALKPNATVAKDGSGNFTTISDALAAMPAKYEGRYVIYVKQGIYDETVTVDKKMVNVTMYGDGSQKTIVT
GNKNFADGVRTFRTATFVALGEGFMAKSMGFRNTAGPEKHQAVAIRVQSDRSIFLNCRFEGYQDTLYAQT
HRQFYRSCVITGTIDFIFGDAAAIFQNCLIFVRKPLPNQQNTVTAQGRVDKFETTGIVLQNCRIAPDEDL
KPVKTEVKSYLGRPWKEFSRTIVMESTIEDVIDPVGWLRWEGDFALDTLYYAEYNNKGPGGATTARVKWP
GYHVINKEEAMKYTVGPFLQGDWISAIGSPVKLGLY
>gnl|CDD|178347 PLN02746, PLN02746, hydroxymethylglutaryl-CoA lyase
SRGSTSTVSGTLGSSWSFKEHQYSSSSNEVGVAHMHNKLLKGLPKFVKIVEVGPRDGLQNEKNIVPTSVK
VELIQRLVSSGLPVVEATSFVSPKWVPQLADAKDVMAAVRNLEGARFPVLTPNLKGFEAAIAAGAKEVAV
FASASESFSKSNINCSIEESLVRYREVALAAKKHSIPVRGYVSCVVGCPIEGPVPPSKVAYVAKELYDMG
CYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDKLAVHFHDTYGQALANILVSLQMGISTVDSSVAGLGGC
PYAKGASGNVATEDVVYMLNGLGVSTNVDLGKLMAAGDFISKHLGRPSGSKTAVALSARITAAASKI
>gnl|CDD|215398 PLN02747, PLN02747, N-carbamolyputrescine amidase
MGMGRKVVVAALQFACSDDRAANVDKAERLVREAHAKGANIILIQELFEGYYFCQAQREDFFQRAKPYEG
HPTIARMQKLAKELGVVIPVSFFEEANNAHYNSIAIIDADGTDLGLYRKSHIPDGPGYQEKFYFNPGDTG
FKVFDTKFAKIGVAICWDQWFPEAARAMVLQGAEVLLYPTAIGSEPQDPGLDSRDHWKRVMQGHAGANLV
PLVASNRIGTEILETEHGPSKITFYGGSFIAGPTGEIVAEADDKAEAVLVAEFDLDQIKSKRASWGVFRD
RRPDLYKVLLTLDGNK
>gnl|CDD|215399 PLN02748, PLN02748, tRNA dimethylallyltransferase
AMLLNPSPGAGEEGSPKQKGKAKVVVVMGPTGSGKSKLAVDLASHFPVEIINADSMQVYSGLDVLTNKVP
LHEQKGVPHHLLGVISPSVEFTAKDFRDHAVPLIEEILSRNGLPVIVGGTNYYIQALVSPFLLDDMAEET
EDCTFVVASVLDEHMDVESGLGNDDEDHGYELLKELDPVAANRIHPNNHRKINRYLELYATTGVLPSKLY
QGKAAENWGRISNSRFDCCFICVDADTAVLDRYVNQRVDCMIDAGLLDEVYDIYDPGADYTRGLRQAIGV
REFEDFLRLYLSRNENGELTSSSNNDKVMKENSRKILNFPHDDKLKILLDEAIDQVKLNTRRLVRRQKRR
LHRLNTVFGWNIHYIDATEAILCKSEESWNAKVVKPAVEIVRRFLSDDTSSGPDASSGKSVSRELWTQYV
CEACGNKVLRGAHEWEQHKQGRGHRKRVQRLKQKQTQKNRLVQEAELD
>gnl|CDD|178350 PLN02749, PLN02749, Uncharacterized protein At1g47420
LRRRFSEDVSHLPEISDPEILKAFKDLMAASWDELPDSVVNDAKKALSKNTDDKAGQEALKNVFRAAEAV
EEFGGTLVSLRMEIDDLIGLSGENVKPLPDYIENALETAYQRYAAYLDSFGPEENYLKKKVEMELGTKMI
HLKMRCSGLGSEWGKVTLLGTSGLSGSYVEQRA
>gnl|CDD|178351 PLN02750, PLN02750, oxidoreductase, 2OG-Fe(II) oxygenase family protein
MGEIDPAFIQAPEHRPKFHLTNSDEEIPVIDLSVSTSHDKTEVASKIGEACKKWGFFQVINHGVPSELRQ
RVEKVAKEFFDQTTEEKRKVKRDEVNPMGYHDSEHTKNIRDWKEVFDFLVQDPTLVPASPDPEDTELRKL
TNQWPQNPSHFRELCQEYARQVEKLAFKLLELISLSLGLPADRLNGYFKDQISFARFNHYPPCPAPHLAL
GVGRHKDGGALTVLAQDDVGGLQISRRSDGEWIPVKPIPDAFIINIGNCMQVWTNDLYWSAEHRVVVNSQ
KERFSIPFFFFPSHYVNIKPLDELINEQNPPKYKEFNWGKFFASRNRSDYKKLEVENIQIDHFKA
>gnl|CDD|215400 PLN02751, PLN02751, glutamyl-tRNA(Gln) amidotransferase
MALTLLRGVQTPVPSRRGPRLFRRASSRFSVRATTATSAAAAESKQAPKKSEALDKIEQDFEAVIGIETH
VQLSTLTKAFCSCPYNYGAEPNTTVCPVCMGLPGTLPVLNSKVVEKAVKLGLALNCKISLKSKFDRKQYF
YPDLPKGYQISQFDIPIAEGGYVDVDLPVEFGGGHRRFGITRVHMEEDAGKLLHSGNGSYSQGSALVDLN
RAGVPLLEIVSEPDMRTGIEAAEYGAELQRLVRYLGVSNGNMQEGSLRCDVNVSIRPVGQEEFGTKVEIK
NMNSFSAMSRAIDFEISRQILLHRQGQGDEIVQETRLWDEGAQKTVTMRKKEGLADYRYFPEPDLPEVVL
TEEYVDSIRASMPELPEAKRRRYENMGLSMQDVLFLANDKNVAEFFDATLAKGADAKLAANWIMGDIAAY
LKNEKVSISEIKLTPKELAELIASIKDGTISGKIGKEILPELLAKGGTVKGLVEEKGLVQISDPAEIEAM
VDKVLEENPKQLEQYRGGKTKLQGFFAGQVMKASKGKANPGLLNKILMEKLNAK
>gnl|CDD|215401 PLN02752, PLN02752 [acyl-carrier protein] S-malonyltransferase
PAAAAFAARRASASRVSMSVSVGSQATAADALFADYKPTTAFLFPGQGAQAVGMGKEAAEVPAAKALFDK
ASEILGYDLLDVCVNGPKEKLDSTVVSQPAIYVASLAAVEKLRARDGGQAVIDSVDVCAGLSLGEYTALV
FAGALSFEDGLKLVKLRGEAMQAAADAGPSGMVSVIGLDSDKVQELCAAANEEVGEDDVVQIANYLCPGN
YAVSGGKKGIDAVEAKAKSFKARMTVRLAVAGAFHTSFMEPAVDALEAALAAVEIRTPRIPVISNVDAQP
HSDPATIKKILARQVTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGIVKRVDKGAKIENVTV
>gnl|CDD|178354 PLN02753, PLN02753, triacylglycerol lipase
MAAIPSHNNLLTINHKNSITGHHSSSLNTKFSEINFPAKFQVATRALSRTDESSLSAVISRLERERRERQ
GLLIDEAEGAGELWLTAEDIRRRDKKTEEERRLRDTWRKIQGEDDWAGLIDPMDPILRSELIRYGEMAQA
CYDAFDFDPASKYCGTSRFSRLDFFDSLGMIDSGYEVARYLYATSNINLPNFFSKSRWSKVWSKNANWMG
YVAVSDDETSRNRLGRRDIAIAWRGTVTKLEWIADLKDYLKPVSENKIRCPDPAVKVESGFLDLYTDKDT
TCKFAKFSAREQILTEVKRLVEEHGDDDDSDLSITVTGHSLGGALAILSAYDIAEMGLNRSKKGKVIPVT
VLTYGGPRVGNVRFKDRMEELGVKVLRVVNVHDVVPKSPGLFLNESRPHALMKIAEGLPWCYSHVGEELA
LDHQNSPFLKPSVDLSTAHNLEAMLHLLDGYHGKGERFVLSSGRDHALVNKASDFLKEHLQIPPFWRQDA
NKGMVRNSEGRWIQAERLRFEDHHSPDIHHHLSQLRLDHPC
>gnl|CDD|215402 PLN02754, PLN02754, chorismate synthase
RRLSSASVQISLRSRTRKNLQIQAAGSTFGTYFRVTTFGESHGGGVGCVIDGCPPRIPLTEEDMQFDLDR
RRPGQSRITTPRKETDTCEILSGVSEGMTLGTPIAVFVPNTDQRGQDYSEMSVAYRPSHADATYDFKYGV
RAVQGGGRSSARETIGRVAAGAVAKKILKQFAGTEILAYVSQVHDVVLPEDLVDHETLTLEQIESNIVRC
PDPEYAEKMIAAIDAVRVRGDSVGGVVTCIVRNVPRGLGSPVFDKLEAELAKAMMSLPATKGFEIGSGFA
GTLLTGSEHNDEFYMDEHGRIRTRTNRSGGIQGGISNGEIIVMRIAFKPTSTIGKKQNTVTRDGQETELR
ARGRHDPCVVPRAVPMVEAMVALVLVDQLMAQYAQCELFPINPVLQEPLGIASPAAAGAAVQS
>gnl|CDD|178356 PLN02755, PLN02755, complex I subunit
MGGGMEVNKNKFIEEWGAARENLEFNFRWTRRNLAVVGIFGIAVPILVYKGIVREFHMQDEDAGRPERKF
L
>gnl|CDD|166397 PLN02756, PLN02756, S-methyl-5-thioribose kinase
MAFSEFRPLDEKSLVEYIKATPALSSKIGNDLDDLKIKEVGDGNLNFVYIVVSSSGSFVIKQALPYIRCI
GESWPMTKERAYFEATALREHGRLCPDHVPEVYHFDRTMALIGMRYLEPPHIILRKGLIAGIEYPLLAEH
MSDYMAKTLFFTSLLYHDTTEHKRAVAEFCGNVELCRLTEQVVFSDPYKVSQYNRWTSPYLDRDAEAVRE
DNILKLEIAELKSMFCERAQALVHGDLHTGSVMVTPDSTQVIDPEFAFYGPMGFDIGAFLGNLILAYFAQ
DGHADQANDRKTYKEWILKTIEQTWNLFHKKFTALWDEHKDGSGEAYLPEIYNNPELLQLVQKKYMQDLL
HDTLGFGAAKMIRRIVGVAHVEDFESIEDASKRANCERQALDFAKMLLKERRKFQSIGEVVSAIQQLQ
>gnl|CDD|215403 PLN02757, PLN02757, sirohydrochlorine ferrochelatase
GRSGGNGNGVGDKDGVVIVDHGSRRKESNLMLEEFVAMYKQKTGHPIVEPAHMELAEPSIKDAFGRCVEQ
GASRVIVSPFFLSPGRHWQEDIPALTAEAAKEHPGVKYLVTAPIGLHELMVDVVNDRIKYCLSHVAGDAD
ECDVCAGTGKCRLY
>gnl|CDD|215404 PLN02758, PLN02758, oxidoreductase, 2OG-Fe(II) oxygenase family protein
MAPVPISPIKVGQIDDVQELRKSKPTTVPERFIRDMDERPDLASDTLHAPDDIPVIDFSRLVKGDNDELF
SEILKLRLACEEWGFFQVINHGIELELLEEIEKVAREFFMLPLEEKQKYPMAPGTVQGYGQAFVFSEDQK
LDWCNMFALGVEPHFIRNPKLWPTKPARFSETLEVYSREIRELCQRLLKYIAMTLGLKEDRFEEMFGEAV
QAVRMNYYPPCSRPDLVLGLSPHSDGSALTVLQQGKGSCVGLQILKDNTWVPVHPVPNALVINIGDTLEV
LTNGKYKSVEHRAVTNKEKDRLSIVTFYAPSYEVELGPMPELVDDENPCKYRRYNHGEYSRHYVTSKLQG
KKTLEFAKILS
>gnl|CDD|178359 PLN02759, PLN02759, Formate--tetrahydrofolate ligase
MTMSSSRRKLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGY
YVVVAGITPTPLGEGKSTTTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNL
HLTGDIHAITAANNLLAAAIDTRVFHEATQSDKALFNRLCPANKEGKRSFAAVMFRRLKKLGISKTDPDE
LTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVGQGPEEKGMTRETGFDITVASEIMAVLALTTSL
ADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTLEGTPVLVHAGPFANIAHGNSSI
VADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMHGGGPAVVAGKPL
DHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTHHA
HGGKGAVDLGEAVQKACEGNSQPFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFS
NLPICMAKTQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTET
GKVLGLS
>gnl|CDD|215405 PLN02760, PLN02760, 4-aminobutyrate:pyruvate transaminase
MIARNLLRSSARSTQVNLLKHYAATASLAPASARIFSTEASLQKEDSEENGFKGHDMLAPFTAGWQSTDL
EPLVIEKSEGSYVYDINGKKYLDALAGLWCTALGGSEPRLVAAATEQLNKLPFYHSFWNRTTKPSLDLAK
ELLEMFTARKMGKVFFTNSGSEANDTQVKLVWYYNNALGRPNKKKFIARSKSYHGSTLISASLSGLPALH
QKFDLPAPFVLHTDCPHYWRFHLPGETEEEFSTRLADNLENLILKEGPETIAAFIAEPVMGAGGVIPPPA
TYFEKIQAVLKKYDILFIADEVICAFGRLGTMFGCDKYNIKPDLVSLAKALSSAYMPIGAVLVSPEISDV
IHSQSNKLGSFAHGFTYSGHPVSCAVALEALKIYKERNIPEHVNKIAPRFQDGIKAFSGSPIIGEIRGTG
LILGTEFVDNKSPNDPFPAEWGVGAYFGAECKKRGMLVRVAGDNIMMSPPLIITPEEVDELISIYGKALK
ATEERVAELKSQKK
>gnl|CDD|215406 PLN02761, PLN02761, lipase class 3 family protein
MASASLPITLKNPRFFSSSPNKIFKTQPQTLILTTKFKTCSIICSSSCTSISSSTTQQKQSNKQTHVSDN
KREEEPEEELEEKEVSLREIWREVQGCNNWEGLLDPMNNHLRREIIRYGEFAQACYDSFDFDPHSKYCGS
CKYHPSDFFQNLDLHLHKGYTITRYLYATSNINLPNFFQKSKLSSIWSQHANWMGYVAVATDEEEVKRLG
RRDIVIAWRGTVTYLEWIYDLKDILCSANFGDDPSIKIELGFHDLYTKKEDSCKFSSFSAREQVLAEVKR
LVEYYGTEEEGHEISITVTGHSLGASLALVSAYDIAELNLNHVPENNYKIPITVFSFSGPRVGNLRFKER
CDELGVKVLRVVNVHDKVPSVPGIFTNEKFQFQKYVEEKTSFPWSYAHVGVELALDHKKSPFLKPTKDLG
CAHNLEALLHLVDGYHGKDEEAEKRFCLVTKRDIALVNKSCDFLRSEYHVPPCWRQDENKGMVKASDGRW
VLPDRPRLEPHGPEDIAHHLQQVLGKVNDDNFKPTTT
>gnl|CDD|215407 PLN02762, PLN02762, pyruvate kinase complex alpha subunit
SDSSGIDVDVVTEAELRENGFRSTRRTKLVCTIGPACCGFEQLEALAMGGMNVARLNMCHGTREWHRDVI
RRVRRLNEEKGFAVAVMMDTEGSEIHMGDLGGASSAKAEDGEEWTFTVRKFDGSRPEFTIQVNYDGFAED
VKVGDELVVDGGMVRFEVIEKIGPDVKCKCTDPGLLLPRANLTFWRDGSLVRERNAMLPTISSKDWLDID
FGISEGVDFIAVSFVKSAEVIKHLKSYIAARSRDSDIGVIAKIESLDSLKNLEEIIRASDGAMVARGDLG
AQIPLEQVPSVQEKIVRLCRQLNKPVIVASQLLESMIEYPTPTRAEVADVSEAVRQRADALMLSGESAMG
LYPEKALSVLRSVSLRMELWSREEKRHEALELPQLSSSLSDRISEEICNSAAKMANNLGVDAIFVYTKHG
HMASLLSRNRPDCPIFAFTDTTSVRRRLNLQWGLIPFRLDFSDDMESNLNKTFSLLKARGMIKSGDLVIA
VSDLTPSSMLQSIQVRNVP
>gnl|CDD|215408 PLN02763, PLN02763, hydrolase, hydrolyzing O-glycosyl compounds
MTSTDMIFMPILEEGVFRFDCSEDARKAAFPSLSFKNPKLREEPIESHNVPAFIPTFECDGDQQIVTFEL
PSGTSFYGTGEVSGPLERTGKRVYTWNTDAWGYGQNTTSLYQSHPWVFVVLPNGEALGVLADTTRRCEID
LRKESIIRIIAPASYPVITFGPFPSPEALLTSLSHAIGTVFMPPKWALGYQQCRWSYESAKRVAEIARTF
REKKIPCDVVWMDIDYMDGFRCFTFDKERFPDPKGLADDLHSIGFKAIWMLDPGIKAEEGYFVYDSGCEN
DVWIQTADGKPFVGEVWPGPCVFPDFTNKKTRSWWANLVKDFVSNGVDGIWNDMNEPAVFKTVTKTMPET
NIHRGDEELGGVQNHSHYHNVYGMLMARSTYEGMLLANKNKRPFVLTRAGFIGSQRYAATWTGDNLSNWE
HLHMSIPMVLQLGLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPFARGHSEQGTIDHEPWSFGEECE
EVCRLALKRRYRLLPHFYTLFYKAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGPLLISASTLPDQGSD
NLQHVLPKGIWQRFDFDDSHPDLPLLYLQGGSIIPLGPPIQHVGEASLSDDLTLLIALDENGKAEGVLYE
DDGDGFGYTKGDYLLTHYEAELVSSEVTVRVASTEGSWKRPKRRLHVRLLLGGGAMVDAEGIDGEELRIK
LPTESEVSKLVSTSREQFKSHLENTKLIPEYEEVHGIKGVGLSKEPIELSSGDWFLKVVPWIGGRIISMI
HKPSGYQWLHSRIEIGGYEEYSGTEYRSAGCTEEYKVVERDLEQAGGEESLGLEGDIGGGLVLAREISIP
KDSPKVVKISSSIVARSVGAGSGGFSRLVCLRVHPTFKLLHPTESFVSFTAIDGSKHELWPEFGEQFYEG
NDRPNGEWMLVDKETGLAVVNRFDVKEVEKCHVHWGPGTVNLELWSEERPVSKETPLSISHEYEVIDT
>gnl|CDD|178364 PLN02764, PLN02764, glycosyltransferase family protein
MGGLKFHVLMYPWFATGHMTPFLFLANKLAEKGHTVTFLLPKKALKQLEHLNLFPHNIVFRSVTVPHVDG
LPVGTETVSEIPVTSADLLMSAMDLTRDQVEVVVRAVEPDLIFFDFAHWIPEVARDFGLKTVKYVVVSAS
TIASMLVPGGELGVPPPGYPSSKVLLRKQDAYTMKNLEPTNTIDVGPNLLERVTTSLMNSDVIAIRTARE
IEGNFCDYIEKHCRKKVLLTGPVFPEPDKTRELEERWVKWLSGYEPDSVVFCALGSQVILEKDQFQELCL
GMELTGSPFLVAVKPPRGSSTIQEALPEGFEERVKGRGVVWGGWVQQPLILSHPSVGCFVSHCGFGSMWE
SLLSDCQIVLVPQLGDQVLNTRLLSDELKVSVEVAREETGWFSKESLRDAINSVMKRDSEIGNLVKKNHT
KWRETLASPGLLTGYVDNFIESLQDLVSGTSHF
>gnl|CDD|215409 PLN02765, PLN02765, pyruvate kinase
MQSSHLLLEEPIRLASILEPSKPSFFPALTKIVGTLGPKSRSVEVIEACLKAGMSVARFDFSWGDAEYHQ
ETLENLKIAVKNTKKLCAVMLDTVGPELQVINKTEKPISLKAGNTVTLTPDQSKEASSEVLPINFPGLAK
AVKPGDTIFVGQYLFTGSETTSVWLEVDEVKGDDVVCTVKNSATLAGSLFTLHVSQVRIDLPTLSEKDKE
VISTWGVPNKIDFLSLSYTRHAEDVREAREFLSSLGLSQTQIFAKIENVEGLTHFDEILQEADGIILSRG
NLGIDLPPEKVFLFQKAALYKCNMAGKPAVVTRVVDSMTDNLRPTRAEATDVANAVLDGADAILLGAETL
RGLYPVETISTVGRICAEAEKVFNQDLYFKKTVKYVGEPMSHLESIASSAVRAAIKVKASVIIVFTSSGR
AARLIAKYRPTMPVLSVVIPRLKTNQLKWSFTGAFQARQCLIVRGLFPMLADPRHSAESTSATNESVLKV
ALDHGKAAGVIKSHDRVVVCQKVGDSSVVKIIELDD
>gnl|CDD|215410 PLN02766, PLN02766, coniferyl-aldehyde dehydrogenase
MGSNGNCGGASGVKVPEIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREA
FDHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIH
GETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKL
AGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNLKQVSLELGGKSPLLIFDD
ADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQF
EKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKA
NNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKS
VVTPLYNSPWL
>gnl|CDD|215411 PLN02768, PLN02768, AMP deaminase
MEPYALHLALAALVGASFVAVSAYYMHRKTLDQLLEFAKTLDRNREGDEPQNPTSQVRRKGNDYYRRGSA
SLPDATAFSGGGDDGDEPRDGHHVYVDGIPPGLPRLHTGPEGKASVHGAGSTKRVGSFIRPTSPKSPVAS
ASAFESVEGSDDEDNLTDNEKLDTTYLHTNGNVELPDHADANGEQIPIPASSMIRSHSVSGDLHGVQPDP
IAADILRKEPEQETFVRLNITPLEVPSPDEVEAYKVLQECLELRKRYVFREEVAPWEKEIISDPSTPKPN
PNPFSYTPEGKSDHYFEMQDGVVHVYANKDSKEELFPVADATTFFTDLHHILRVIAAGNIRTLCHHRLNL
LEQKFNLHLMLNADREFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDG
TYLTLKEVFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAEL
TKQVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNELYSENVVWLIQLPRLYNVYKEMGIVTSFQ
NILDNIFIPLFEVTVDPDSHPQLHVFLKQVVGLDLVDDESKPERRPTKHMPTPAQWTNVFNPAFSYYVYY
CYANLYTLNKLRESKGMTTIKFRPHSGEAGDIDHLAATFLTCHNIAHGINLRKSPVLQYLYYLAQIGLAM
SPLSNNSLFLDYHRNPFPMFFLRGLNVSLSTDDPLQIHLTKEPLVEEYSIAASVWKLSSCDLCEIARNSV
YQSGFSHALKSHWIGKEYYKRGPDGNDIHKTNVPHIRVEFRDTIWKEEMQQVYLGKAKIPEEVDK
>gnl|CDD|215412 PLN02769, PLN02769, Probable galacturonosyltransferase
GGKGGHNLTPPGKRRWRGLVIAVLALVLCSMLVPLAFLLGLHHNGFHSTGRVAVQPVSSPEFSHVGSARE
NGTKKTQNQVSEGVDEILKESGLTSSKPSDIVISSRSKLKKVFPDPKLNPLPVKPHSVPVPSSDTKNKST
AIDKENKGQKADEDENEKSCELEFGSYCLWSEEHKEVMKDSIVKRLKDQLFVARAYYPSIAKLPGQEKLT
RELKQNIQEHERVLSESITDADLPPFIQKKLEKMEQTIARAKSCPVDCNNVDRKLRQILDMTEDEAHFHM
KQSAFLYQLGVQTMPKSHHCLSMRLTVEYFKSSSLDMEDSNSEKFSDPSLRHYVIFSKNVLAASVVINST
VVHSRESGNIVFHVLTDAQNYYAMKHWFDRNSYKEAAVQVLNIEDLILKDLDKFALKQLSLPEEFRVSFR
SVDNPSSKQMRTEYLSVFSHSHFLLPEIFKKLKKVVVLDDDVVVQRDLSFLWNLDMGGKVNGAVQFCGVR
LGQLKNYLGDTNFDTNSCAWMSGLNVIDLDKWRELDVTETYLKLLQKFSKDGEESLRAAALPASLLTFQD
LIYPLDDRWVLSGLGHDYGIDEQAIKKAAVLHYNGNMKPWLELGIPKYKKYWKRFLNRDDRFMDECNVN
>gnl|CDD|215413 PLN02770, PLN02770, haloacid dehalogenase-like hydrolase family protein
MTVSSGENSVESKSSLSGLAPLEAVLFDVDGTLCDSDPLHYYAFREMLQEINFNGGVPITEEFFVENIAG
KHNEDIALGLFPDDLERGLKFTDDKEALFRKLASEQLKPLNGLYKLKKWIEDRGLKRAAVTNAPRENAEL
MISLLGLSDFFQAVIIGSECEHAKPHPDPYLKALEVLKVSKDHTFVFEDSVSGIKAGVAAGMPVVGLTTR
NPESLLMEAKPTFLIKDYEDPKLWAALEELDQKGAAGV
>gnl|CDD|178370 PLN02771, PLN02771, carbamoyl-phosphate synthase (glutamine-hydrolyzing)
EAMATRPLGFVLPTSLSSQPSFDRRGGVRVSVIRCSSSPLTSDGAGVVERPWKTSDARLVLEDGSVWKAK
SFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVIRSLSIS
TSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDEELLKMSRSWDIVGIDLI
SGVSCKSPYEWVDKTNPEWDFNTNSRDGESYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKM
KPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRT
GRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF
>gnl|CDD|215414 PLN02772, PLN02772, guanylate kinase
MGEAPAFFVDHLENGYTNGFGVKPKNRETSVTIGDKTYVIGGNHEGNTLSIGVQILDKITNNWVSPIVLG
TGPKPCKGYSAVVLNKDRILVIKKGSAPDDSIWFLEVDTPFVREQKKLLGTEVVAWSKGVRGNAEKPIVI
SGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGN
LYGTSIEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRL
RNAEAELEQGKSSGIFDHILYNDNLEECYKNLKKLLGLDGLAAVNGVEAPEGINLPKEHSVSKMDDKIII
QETGEKTSNKLIVLDLSSLNGGAPGRTRGLDVDAVKSFSDFLNGINQS
>gnl|CDD|178372 PLN02773, PLN02773, pectinesterase
QMARRVLRVAQDGSGDYCTVQDAIDAVPLCNRCRTVIRVAPGVYRQPVYVPKTKNLITLAGLSPEATVLT
WNNTATKIDHHQASRVIGTGTFGCGTVIVEGEDFIAENITFENSAPEGSGQAVAIRVTADRCAFYNCRFL
GWQDTLYLHYGKQYLRDCYIEGSVDFIFGNSTALLEHCHIHCKSAGFITAQSRKSSQESTGYVFLRCVIT
GNGGSGYMYLGRPWGPFGRVVFAYTYMDACIRPVGWNNWGKAENERTACFYEYRCFGPGSCPSNRVTWAR
ELLDEEAEQFLSHSFIDPDQDRPWLCQRMALKIPYSA
>gnl|CDD|178373 PLN02774, PLN02774, brassinosteroid-6-oxidase
VLLVVLGVLVIIVCLCSALLRWNEVRYSKKGLPPGTMGWPLFGETTEFLKQGPDFMKNQRLRYGSFFKSH
ILGCPTIVSMDPELNRYILMNEGKGLVPGYPQSMLDILGTCNIAAVHGSTHRYMRGSLLSLISPTMIRDH
LLPKIDEFMRSHLSGWDGLKTIDIQEKTKEMALLSALKQIAGTLSKPISEEFKTEFFKLVLGTLSLPIDL
PGTNYRSGVQARKNIVRMLRQLIQERRASGETHTDMLGYLMRKEGNRYKLTDEEIIDQIITILYSGYETV
STTSMMAVKYLHDHPKALQELRKEHLAIRERKRPEDPIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKT
TQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKSLESHNYFFLFGGGTRLCPGKELGI
VEISTFLHYFVTRYRWEEVGGDKLMKFPRVEAPNGLHIRVSPY
>gnl|CDD|178374 PLN02775, PLN02775, Probable dihydrodipicolinate reductase
EASTASPPGSAIPIMVNGCTGKMGHAVAEAAVSAGLQLVPVSFTGPAGVGVTVEVCGVEVRLVGPSEREA
VLSSVKAEYPNLIVVDYTLPDAVNDNAELYCKNGLPFVMGTTGGDRDRLLKDVEESGVYAVIAPQMGKQV
VAFQAAMEIMAEQFPGAFSGYTLEVVESHQATKLDTSGTAKAVISSFRKLGVSFDMDQIELIRDPKQQLE
GVGVPEEHLNGHAFHTYRLTSPDGTVSFEFQHNVCGRSIYAEGTVDAVLFLAKKIAEGADKRIYNMIDVL
REGNMR
>gnl|CDD|215415 PLN02776, PLN02776, prenyltransferase
LSKARLSALVVATSGAGFVLGSGEAIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPS
GRISVPHAVAWAVVVGAAGVALLAYKTNMLTAGLGAGNILLYAFVYTPLKQIHPANTWVGAVVGAIPPLM
GWAAASGQLDAGAMVLAAALYFWQMPHFMALAYMCRDDYAAGGYRMLSLADATGRRTALVALRNCLYLAP
LGFLAYDWGVTSSPFALEAALLTAYLAASAASFYREPTNANARKMFHGSLLYLPAFMALLLLHRVPNDNQ
VDLRQESELTESLDGRAKGREETSLEQVSKRRAPGRVARPPVAYASAAPFPFLPAPSYASP
>gnl|CDD|178376 PLN02777, PLN02777, photosystem I P subunit (PSI-P)
MTPLSISSSSTLIDSKAPRSSAAASPQCVSLPTLPPPPVQSHNRPAKATAYCRKIARNVVTMATGEAPAE
VETTELPEIVKTVQEAWDKVEDKYAVSSLAFAGVVALWGSAGMISAIDRLPLVPGVLELVGIGYTGWFAY
KNLVFKPDREALIEKIKDTYKEIIGSS
>gnl|CDD|178377 PLN02778, PLN02778, 3,5-epimerase/4-reductase
SNGTAGSATLKFLIYGKTGWIGGLLGKLCQEQGIDFHYGSGRLENRASLEADIDAVKPTHVFNAAGVTGR
PNVDWCESHKVETIRANVVGTLTLADVCRERGLVLTNYATGCIFEYDDAHPLGSGIGFKEEDTPNFTGSF
YSKTKAMVEELLKNYENVCTLRVRMPISSDLSNPRNFITKITRYEKVVNIPNSMTILDELLPISIEMAKR
NLTGIYNFTNPGVVSHNEILEMYRDYIDPSFTWKNFTLEEQAKVIVAPRSNNELDTTKLKREFPELLPIK
ESLIKYVFEPNKKTKKAV
>gnl|CDD|215416 PLN02779, PLN02779, haloacid dehalogenase-like hydrolase family protein
AASSSSARLASASRTRAGRRRRRRSRSTARVASASASALPEALLFDCDGVLVETERDGHRVAFNDAFKEF
GLRPVEWDVELYDELLNIGGGKERMTWYFNENGWPTSTIEKAPKDEEERKELVDSLHDRKTELFKELIES
GALPLRPGVLRLMDEALAAGIKVAVCSTSNEKAVSKIVNTLLGPERAQGLDVFAGDDVPKKKPDPDIYNL
AAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCIVTKSSYTADEDFSGADAVFDCLGDVPLEDFDLLFCES
LLTKQQ
>gnl|CDD|166421 PLN02780, PLN02780, ketoreductase/ oxidoreductase
MELCFVDKLKSQPLWLLVLFVLGSLSILKFFFTILNWVYVYFLRPAKNLKKYGSWALVTGPTDGIGKGFA
FQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTQIKTVVVDFSGDIDEGVKRIKETIEGLDVGVLINNV
GVSYPYARFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIPSDPLYAVYAA
TKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIRRSSFLVPSSDGYARAALRWVGYEPRCTPYWP
HSLIWGLISALPESAVDSWRLKFCLQIRKKGQQKDSRKKE
>gnl|CDD|215417 PLN02781, PLN02781, Probable caffeoyl-CoA O-methyltransferase
MANVLPPKGILKSEALKQYIMETSAYPREHELLKELREATVQKYGNLSEMEVPVDEGLFLSMLVKIMNAK
NTLEIGVFTGYSLLTTALALPEDGRITAIDIDKEAYEVGLEFIKKAGVDHKINFIQSDALSALDQLLNND
PKPEFDFAFVDADKPNYVHFHEQLLKLVKVGGIIAFDNTLWFGFVAQEEDEVPEHMRAYRKALLEFNKLL
ASDPRVEISQISIGDGVTLCRRLV
>gnl|CDD|215418 PLN02782, PLN02782, Branched-chain amino acid aminotransferase
NYLLCPSRAFSTRLHSSSRRLNFPPPSSLSLRHSNSSVSSNPISSKAISLTRCDAVSSSSYTEVTELADI
DWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFR
PEENAIRMRNGAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYT
FLIYVSPVGNYFKEGVAPINLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCVHK
KYLEEVSSCNIFIVKDNVISTPAIKGTILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEVFCTGTA
VVVSPVGSITYKGKRVSYGEGGFGTVSQQLYTVLTSLQMGLIEDNMNWTVELS
>gnl|CDD|178380 PLN02783, PLN02783, diacylglycerol O-acyltransferase
MDGSRGMRLAGGSNSVLSILAVAIWLGAIHFNVALVLASLFFLPSPVALTVLALLLLLMFIPAHPTSKLG
RKIARFICKYACAYFPVRLHVEDEEAFDPNRAYVFGYEPHSVLPIGVIALADLSGFLPLPKIRALASSAV
FYTPFLRHIWTWLGLDPASRKNFTSLLKAGYSCIIVPGGVQECLYMEHGSEVAYLKSRKGFVKIAMETGA
PLVPVFCFGQTRAYKWWKPGGPLVPKLSRAIGFTPIVFWGRYGSPIPHRTPMHVVVGKPIEVKKNPQPSQ
EEVAEVLEQFVEALQDLFEKHKARAGYGDLELVVL
>gnl|CDD|215419 PLN02784, PLN02784, alpha-amylase
MSTVCIESLLHHSGLEKNSKIGRGKRSPSSLNLSLKSLTNGKSFCNFKMSVGVSSTTRRASSSDTALVET
AQSDDVFFKETFPVKRTEKVEGKIYVRLEEKNEKNWKLSVGCSIPGKWILHWGVSYVGDTGSEWDQPPEE
MRPPGSIAIKDYAIETPLKKSSEGDSFYEVTIDLDPNSSIAAINFVLKDEETGAWYQHKGRDFKVPLVDD
LPDGGNNVGAKKGFGIWPGALGQLSNILLKDEGSPSKEQDKSSSELDSAAERKGLKGFYEEMPIVKRVAV
DNSVTVTVRKCPETAKNLVYLETDLPGDVVVHWGVCKDGAKTWEIPPEPHPPETSLFKNKALQTMLQQKD
DGNGSSGLFSLDGELEGLLFVLKLNEGTWLRCNGNDFYVPLLTSSSLPTQTEQGQSEGKTAKTNKEVSKS
AYTDGIIGEIRNLVIDISSEKGQKTKTKELQESILQEIEKLAAEAYSIFRSTIPTFSEESVLEAERIQKP
PIKICSGTGSGFEILCQGFNWESHKSGRWYMELGEKAAELSSLGFTVVWLPPPTESVSPEGYMPKDLYNL
NSRYGTIDELKDLVKSFHEVGIKVLGDAVLNHRCAHFQNQNGVWNIFGGRLNWDDRAVVADDPHFQGRGN
KSSGDNFHAAPNIDHSQDFVRKDLKEWLCWMRKEVGYDGWRLDFVRGFWGGYVKDYMEASEPYFAVGEYW
DSLSYTYGEMDYNQDAHRQRIVDWINATNGTAGAFDVTTKGILHSALERCEYWRLSDQKGKPPGVVGWWP
SRAVTFIENHDTGSTQGHWRFPEGKEMQGYAYILTHPGTPAVFYDHIFSHYHPEIASLISLRNRQKIHCR
SEVKITKAERDVYAAIIDEKVAMKIGPGHYEPPNGPQNWSVALEGQDYKVWETS
>gnl|CDD|215420 PLN02785, PLN02785, Protein HOTHEAD
MALKLFLFLLLLCLPTSSSSQGKSHFTPYRYPFIDKASSFSSSSSSSSSSGGDSAYDYIVVGGGTAGCPL
AATLSQNFSVLLLERGGVPFGNANVSFLENFHIGLADTSPTSASQAFISTDGVINARARVLGGGTCINAG
FYSRASTRFIQKAGWDAKLVNESYPWVERQIVHWPKVAPWQAALRDSLLEVGVSPFNGFTYDHVYGTKVG
GTIFDEFGRRHTAAELLAAGNPNKLRVLLHATVQKIVFDTSGKRPRATGVIFKDENGNQHQAFLSNNKGS
EIILSAGAIGSPQMLLLSGIGPKKELKKHKIPVVLHNEHVGKGMADNPMNSIFVPSKAPVEQSLIQTVGI
TKMGVYIEASSGFGQSPDSIHCHHGIMSAEIGQLSTIPPKQRTPEAIQAYIHRKKNLPHEAFNGGFILEK
IAGPISTGHLSLINTNVDDNPSVTFNYFKHPQDLQRCVYGIRTIEKIVKTNHFTNFTQCDKQTMEKVLNM
SVKANINLIPKHTNDTKSLEQFCKDTVITIWHYHGGCHVGKVVDQNYKVLGVSRLRVIDGSTFDESPGTN
PQATVMMMGRYMGVKILRERLGRAAGV
>gnl|CDD|178383 PLN02786, PLN02786, isochorismate synthase
SSRLLLLARLSRKTSCSQSMNGCQGDPKVPVGTVETRTLPAVLSPADATERLISAVSELKSQPPPFSSGI
LRLQVPIPQQIGAIDWLHAQNELLPRCFFSRRSDTGDRPDLLLDSSNGNGNGSDHNLVSVAGVGSAVFFR
DLDPFSHDDWRSIKRFLSSKSPLIRAYGAIRFDPNGKISVEWEPFGSFYFIVPQVEFNELGGSSMLAATI
AWDDALSWTWENAIEALQETMLQVSSVVMKLRKESLGVSVLSKNHVPSKGAWHLAVNKALQIIKRKSSPL
KKVVLARSSRIITDTDIDPIAWLACLQVEGQNAYQFCLQPPDAPAFIGNTPEQLFHRKGLGVCSEALAAT
RPRGGSSARDLQIELDLLTSPKDDLEFSIVRENIREKLEAICDRVVVEPHKAIRKLARVQHLYAQLAGRL
RSEDDEFDILAALHPTPAVCGHPTEEARLLIAETESFDRGMYAGPVGWFGGGESEFAVGIRSALVEKGLG
ALIYAGTGIVEGSNPSSEWNELELKISQFTKSLEHESALSPQN
>gnl|CDD|215421 PLN02787, PLN02787, 3-oxoacyl-[acyl-carrier-protein] synthase II
MASASAASPLCTWLVAACMSVSCAGEDAHQAVALQSGGRSRRRRKRRKCSSASGSASILVTSCLAFGPCT
HYNSSGGNALSSLFGSNSVSLNRNQRRRNRAARSGKAMAVAVQPEKEVETKKKPLTKQRRVVVTGMGVVS
PLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAGKKA
LADGGITEDVMKELDKTKCGVLIGSAMGGMKVFNDAIEALRISYRKMNPFCVPFATTNMGSAMLAMDLGW
MGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPW
DMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGV
SKEDVNYINAHATSTKAGDLKEYQALMRCFGQNPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVH
PNINLENPESGVDTKVLVGPKKERLDIKVALSNSFGFGGHNSSILFAPYK
>gnl|CDD|215422 PLN02788, PLN02788, phenylalanine-tRNA synthetase
PFSSSALVTPATAKSSSRRYRAPAVSAVEIGGVAIARDEVVREDDPTNNVPDHIFSKIGMQLHRRPDHPL
GILKNAIYDYFDENYSNKFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQA
ELLRAGHTHFLVTGDVYRRDSIDATHYPVFHQMEGVRVFSPEEWEASGLDGTDLAAEDLKKTLEGLARHL
FGDVEMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFD
IPDIRLFWSDDERFTSQFKEGQLGVKFKPYSKYPPCYKDISFWISDEFTENNLCEVVRGIAGDLVEEVKL
IDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR
>gnl|CDD|215423 PLN02789, PLN02789, farnesyltranstransferase
DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGN
YTVWHFRRLCLEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAK
NYHAWSHRQWVLRTLGGWEDELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAI
LANPRNESPWRYLRGLFKDDKEALVSDPEVSSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVD
TLAEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKLPKA
>gnl|CDD|215424 PLN02790, PLN02790, transketolase
IRFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGY
DSVQMEDLKQFRQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDHKIVDHYT
YCILGDGCQMEGISNEAASLAGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGN
TDYDEIRAAIKEAKAVTDKPTLIKVTTTIGYGSPNKANSYSVHGAALGEKEVDATRKNLGWPYEPFHVPE
DVKSHWSKHTKEGAALEAEWNAKFAEYKKKYPEEAAELKSLISGELPSGWEKALPTFTPEDPADATRNLS
QKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFQKDTPEERNVRFGVREHGMGAICNGIALHSSGLIP
YCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNILMLRPADGNET
AGAYKVAVTNRKRPTVLALSRQKVPNLPGTSIEGVEKGGYVISDNSSGNKPDLILIGTGSELEIAAKAAK
ELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTARVSVEAGSTFGWEKYVGSKGKVIGVDRFGASA
PAGILYKEFGFTVENVVAAAKSLL
>gnl|CDD|215425 PLN02791, PLN02791, Nudix hydrolase homolog
MMEEHLDVLTAAGEKTGVSKPRGEVHRDGDYHRAVHVWIYSESTQELLLQRRADCKDSWPGQWDISSAGH
ISAGDTSLLSAQRELEEELGIILPKDAFELLFVFLQECVINDGKFINNEYNDVYLVTTLDPIPLEAFTLQ
ESEVSAVKYMSIEEYKSALAKEDPAYVPYDVNGEYGQLFSIIEKRYKVNTEARSLTLQKQLNRYAPVNLE
AELTGLSEGDRKALSYIIKAAKILDDIFYEQVWNSNPALRDWLKAHAEASELDKLKWAYYSINKSPWSCL
DENEAFLTTADSAVKLLPGATKSVSGWKGLEYRAAFPVEKPPGANFYPPDMDKMEFELWKSGLTEKEQED
ATGFFTVIKRHSELSLDASDQLDGSTQTDTSHDLFSVPYSEEYKPFLKKAAELLHKAGDCADSPSLKRLL
KSKAEAFLSNDYYESDIAWMELDSKLDVTIGPYETYEDGLFGYKATFEAFIGIRDDKATAQLKLFGDNLQ
TLEDNLPLDDVYKSTNVSAAPIRVIQLLYNSGDVKGPQTVAFNLPNDERIVKERGTSMVMLKNVSEAKFK
HILKPIAEVCISEEQKGYVDFESFFTHTICHECCHGIGPHTITLPDGQKSTVRLELQEVHSALEEAKADI
VGLWALHFLIDKGLLSKSLEKSMYVSFLAGCFRSIRFGLEEAHGKGQALQFNWLYEKGAFVLHSDGTFSV
DFAKVEDAVESLSREILTIQAKGDKAAAISLLQKYATLTPPLRVALEKLEDVQVPVDIVPTFPTAEKLLA
>gnl|CDD|178389 PLN02792, PLN02792, oxidoreductase
MMMTTTIISFVKADDTLFYNWRVTYGNISLLTLPRRGILINGQFPGPEIRSLTNDNLVINVHNDLDEPFL
LSWNGVHMRKNSYQDGVYGTTCPIPPGKNYTYDFQVKDQVGSYFYFPSLAVQKAAGGYGSLRIYSLPRIP
VPFPEPAGDFTFLIGDWYRRNHTTLKKILDGGRKLPLMPDGVMINGQGVSYVYSITVDKGKTYRFRISNV
GLQTSLNFEILGHQLKLIEVEGTHTVQSMYTSLDIHVGQTYSVLVTMDQPPQNYSIVVSTRFIAAKVLVS
STLHYSNSKGHKIIHARQPDPDDLEWSIKQAQSIRTNLTASGPRTNPQGSYHYGKMKISRTLILESSAAL
VKRKQRYAINGVSFVPSDTPLKLADHFKIKGVFKVGSIPDKPRRGGGMRLDTSVMGAHHNAFLEIIFQNR
EKIVQSYHLDGYNFWVVGINKGIWSRASRREYNLKDAISRSTTQVYPESWTAVYVALDNVGMWNLRSQFW
ARQYLGQQFYLRVYSPTHSLKDEYPLPKNALLCGRASNKNMSIITP
>gnl|CDD|215426 PLN02793, PLN02793, Probable polygalacturonase
MSYSRGGTEVLCLLLLVVASSLAFVCNQGSFESLLQLPQRQSARTRPRSERVLHVGDFGAKGDGVTDDTQ
AFKEAWKMACSSKVKTRIVIPAGYTFLVRPIDLGGPCKAKLTLQISGTIIAPKDPDVWKGLNPRKWLYFH
GVNHLTVEGGGTVNGMGHEWWAQSCKINHTNPCRHAPTAITFHKCKDLRVENLNVIDSQQMHIAFTNCRR
VTISGLKVIAPATSPNTDGIHISASRGVVIKDSIVRTGDDCISIVGNSSRIKIRNIACGPGHGISIGSLG
KSNSWSEVRDITVDGAFLSNTDNGVRIKTWQGGSGNASKITFQNIFMENVSNPIIIDQYYCDSRKPCANQ
TSAVKVENISFVHIKGTSATEEAIKFACSDSSPCEGLYLEDVQLLSSTGDFTESFCWEAYGSSSGQVYPP
PCFSDSTSFIKQKVQSGSTSFFL
>gnl|CDD|178391 PLN02794, PLN02794, cardiolipin synthase
MAIYRSLNTLIRKNPINKPRSFLTLAAAAAASSSIIPSPFSPLALHFSHRVSPLSKWFIPFGGPLFLSSP
PWKLLQSATPLTLRGNGVVLKKVEALNLRLRRARALAGGGGQGVLDAVVWELRRIDRDESEVADGGIVKS
FVNLPNLISISRLVSGPVIGWMIVNEMYLSAFVGLAISGASDWLDGYVARKMGINSVVGSYLDPLADKVL
IGCVALAMVEKDLLHPGLVGLVVLRDVALVGGAVYKRASSLGWKWNSWSDFFNLDGTRPEKVEPLFISKV
NTVFQLMLVAAALLQPEFGTEETQNYITYLSWLVASTTVASTAAYGVQYMKNRPRLLAKKS
>gnl|CDD|178392 PLN02795, PLN02795, allantoinase
MESALLQLRILPLLALLATLVFFFLFAPALPLQGRDRCSLLPWPHFVLYSKRVVTPAGVIPGAVEVEGGR
IVSVTKEEEAPKSQKKPHVLDYGNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPLN
SFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPENAHNASVLEELLDAGALGLKSFMCPSGINDFPMTT
ATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKDTRPG
GVAEGAHVHIVHLSDAESSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCAPPIRDAANREL
LWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYGLTLEQLARWWSER
PAKLAGLDSKGAIAPGKDADIVVWDPEAEFVLDESYPIYHKHKSLSPYLGTKLSGKVIATFVRGNLVFLE
GKHAKQACGSPILAK
>gnl|CDD|215427 PLN02796, PLN02796, D-glycerate 3-kinase
GSLFPSTPPDVSDVADLREFICSGPLISKLGLTAEDVAESIDEWIAHGLRLCRLLQFDELSLSASQKARV
YHYYLPVYLWCEDQLEAHRSKFKDGDEIPPLVIGISAPQGCGKTTLVFALVYLFNATGRRAASLSIDDFY
LTAADQAKLAEANPGNALLELRGNAGSHDLALGVETLEALRKLNKEGSKMKVPRYDKSAYGGRGDRADPS
TWPEVEGPLDVVLFEGWMLGFKPLGPDAVKAVDPQLEVVNKNLEAYYDAWDKLVDSWIVIKVDDPSWVYE
WRLQAEIAMRAKGKPGMSDEEVADFVSRYMPAYKAYLPGLYAEGPGGSDPDNVLVIEIDENRNPLGV
>gnl|CDD|178394 PLN02797, PLN02797, phosphatidyl-N-dimethylethanolamine N-methyltransferase
MGLLAAVGVLLPFPFYWWLWTNPQSWVNLCGGGRDPSHVMAQVSHALKALQFLSLFSVASFSWPPPLYFW
PLFAFGQFLNFRVYQLLGEAGTYYGVRFGKNIPWVTEFPFGVIRDPQYVGSILSLLACLSWVPFQYILLW
CLGYVFMMFVESKEDPATRAKSIS
>gnl|CDD|215428 PLN02798, PLN02798, nitrilase
MSTAATAGSSVRVAVAQMTSTNDLAANFATCSRLAKEAAAAGAKLLFLPECFSFIGDKDGESLAIAEPLD
GPIMQRYRSLARESGLWLSLGGFQEKGPDDSHLYNTHVLIDDSGEIRSSYRKIHLFDVDVPGGPVLKESS
FTAPGKTIVAVDSPVGRLGLTVCYDLRFPELYQQLRFEHGAQVLLVPSAFTKPTGEAHWEVLLRARAIET
QCYVIAAAQAGKHNEKRESYGHALIIDPWGTVVARLPDRLSTGIAVADIDLSLLDSVRTKMPIAEHRRSL
EFWSAT
>gnl|CDD|215429 PLN02799, PLN02799, Molybdopterin synthase sulfur carrier subunit
SVEIKVLFFARARELTGVSDMTLELPAGSTTADCLAELVAKFPSLEEVRSCCVLALNEEYTTESAALKDG
DELAIIPPISGG
>gnl|CDD|215430 PLN02800, PLN02800, imidazoleglycerol-phosphate dehydratase
AILSASSSAAQLLRPKLSFIDLLPRRAAIVSSPSSSLPRFLRMESQLRQSISCAASSSSSNALGRIGEVK
RVTKETNVSVKINLDGTGVADSSTGIPFLDHMLDQLASHGLFDVHVKATGDLWIDDHHTNEDVALAIGTA
LLKALGDRKGINRFGDFSAPLDEALIEVVLDLSGRPYLGYNLEIPTERVGDLDTEMVEHFFQSLVNNSGM
TVHIRQLAAGKNSHHIIEATAKAFGRALRQCAEVDPRRAGTVASSKGTLSV
>gnl|CDD|215431 PLN02801, PLN02801, beta-amylase
MQNTTTYEEKMLANYVPVYVMLPLGVVTADNVLEDEEGLEKQLKRLKEAGVDGVMVDVWWGIVESKGPKQ
YDWSAYRSLFELVQSFGLKIQAIMSFHQCGGNVGDAVNIPIPQWVRDVGDSDPDIFYTNRSGNRNKEYLS
IGVDNLPLFHGRTAVEMYSDYMKSFRENMADFLEAGVIIDIEVGLGPAGELRYPSYPETQGWVFPGIGEF
QCYDKYLKADFKEAATEAGHPEWELPDDAGEYNDTPEDTGFFKSNGTYLTEEGKFFLTWYSNKLLLHGDQ
ILDEANKAFLGCKVKLAAKVSGIHWWYKHHSHAAELTAGYYNLKGRDGYRPIARMLSRHYGILNFTCLEM
RDTEQPAEALSAPQELVQQVLSGAWREGIEVAGENALSRYDRRGYNQILLNARPNGVNKDGKPKLRMFGV
TYLRLSDELLEETNFSLFKTFVRKMHADQDYCPDPAKYGHEIVPLERSNPEISIEDILEATEPVPPFPWD
KETDMSVDGGLAELLDSVLDKIESIFL
>gnl|CDD|215432 PLN02802, PLN02802, triacylglycerol lipase
LHLFQARRASFRCQPSPLNPNSTAPPSASSASPAANSAATTRAHLANLEKLLQKPPPEPRTSSNSPASQV
GPGVANEGTTPNNQRKGLLNALNLSRFWPFARKAAAEEMSPRSLNRLQRLLSKSEEPSPRGTIASRWREL
HGENGWEGLLDPLDENLRRELVRYGEFVQAAYHAFHSNPAMSAEAPGRPRHVALPDRSYRVTKSLFATSS
VGLPKWADDVAPDGWMTQRSSWVGYVAVCDSPREIRRMGRRDIVIALRGTATCLEWAENLRAGLVPMPGD
DDDAGDQEQPKVECGFLSLYKTAGAHVPSLSESVVGEVRRLMEKYKGEELSITVTGHSLGAALALLVADE
LATCVPAAPPVAVFSFGGPRVGNRAFADRLNARGVKVLRVVNAQDVVTRVPGIAPREELHKWAYAHVGAE
LRLDSKMSPYLRPDADVACCHDLEAYLHLVDGFLGSNCPFRANAKRSLLRLLNEQRSNVKKLYTSKARAL
GLNLERPGDAGSGCLPSPS
>gnl|CDD|178400 PLN02803, PLN02803, beta-amylase
MALTLRSSTSFISPKDTKSLKTPDDFSGTICFAPIKPSCYRLQAKNSMQEAQLTHEEIFTPEGRKSENWE
KLHALSGPHSKNDSGVPVFVMLPLDTVTMGGNLNKPRAMNASLMALRSAGVEGVMVDAWWGLVEKDGPMK
YNWEGYAELVQMVQKHGLKLQVVMSFHQCGGNVGDSCSIPLPPWVLEEMSKNPDLVYTDRSGRRNPEYIS
LGCDSLPVLRGRTPIQVYSDYMRSFRERFKDYLGGVIAEIQVGMGPCGELRYPSYPESNGTWRFPGIGEF
QCYDKYMRASLEASAEAIGKKDWGRGGPHDAGEYKQFPEETGFFRRDGTWNTEYGQFFLEWYSGKLLEHG
DRILAAAEGIFQGTGAKLSGKVAGIHWHYRTRSHAAELTAGYYNTRNHDGYLPIARMFSKHGVVLNFTCM
EMRDGEQPEHANCSPEGLVRQVKMATRTAGTELAGENALERYDSAAFAQVVATSRSDSGNGLTAFTYLRM
NKRLFEGDNWRQLVEFVKNMSEGGRNRRLPECDTEGSDLYVGFIKDKDAEKTTEAALV
>gnl|CDD|178401 PLN02804, PLN02804, chalcone isomerase
TEMVMVEDIPFPPQITTSSKPLSLLGHGITDIEIHFLQIKFTAIGVYLEPSVKGHLQSWKGKPGSELAED
DDFFQALIQAPVEKLIRIVVIKEIKGSQYGVQLESSVRDRLAEDDKYEEEEEEALEKVVEFFQSKYFKKN
SIITYHFPATSGIVEISFSTEGKEESKLTVENANVVEMIQKWYLGGENGVSPSTISSVADSIAAEL
>gnl|CDD|178402 PLN02805, PLN02805, D-lactate dehydrogenase [cytochrome]
RLRSLLRTSRPNRALPSFPKSTLDVTVTTPVKGRRRLPTSWSSSLLPLAIAASAGSLAYLNQSNPSLCDS
SDLDSRVGGKGSTEFVVKGEHKLVPQELIDELKAILQDNMTLDYDERYFHGKPQNSFHKAVNIPDVVVFP
RSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGGVCIDMSLMKSVKALHVEDMDVVVEPGIGWLE
LNEYLEPYGLFFPLDPGPGATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAG
YDLTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIATMLSGIQVSRVELLDEVQIR
AINMANGKNLPEAPTLMFEFIGTEAYAREQTLIVQKIASKHNGSDFVFAEEPEAKKELWKIRKEALWACF
AMEPKYEAMITDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILFDPSQEDQRREAERLN
HFMVHTALSMEGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIPPHVCF
>gnl|CDD|178403 PLN02806, PLN02806, complex I subunit
MVATATVVGALLGLGTQLYSNALRKLPLMRHPWEHVLAMGLGAVFANQLVKWEVKLKEDLDKMLAKARAA
NNARYMDEDRD
>gnl|CDD|215433 PLN02807, PLN02807, diaminohydroxyphosphoribosylaminopyrimidine deaminase
TASHPSIRTAESRRFGRRTSVRCSARAAGDDDSFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEG
FHPKAGQPHAEVFALRDAGDLAENATAYVSLEPCNHYGRTPPCTEALIKAKVKRVVVGMVDPNPIVASKG
IERLRDAGIEVTVGVEEELCRKLNEAFIHRMLTGKPFVTLRYSMSMNGCLLNQIGEGADDAGGYYSQLLQ
EYDAVILSSALADADPLPLSQEAGAKQPLRIIIARSESSPLQIPSLREESAAKVLVLADKESSAEPVLRR
KGVEVVVLNQINLDSILDLCYQRGLCSVLLDLRGNVGGLESLLKDALEDKLLQKVVVEVLPFWSGSQGQS
IASFGGSQSFKLKRLTSREVGGSVVLEGYF
>gnl|CDD|166449 PLN02808, PLN02808, alpha-galactosidase
AFCGGAPTLTLTQITDGFISRNLLDNGLGLTPQMGWNSWNHFQCNINETLIKQTADAMVSSGLAALGYKY
INLDDCWAELKRDSQGNLVPKASTFPSGIKALADYVHSKGLKLGIYSDAGTLTCSKTMPGSLGHEEQDAK
TFASWGIDYLKYDNCENTGTSPQERYPKMSKALLNSGRPIFFSLCEWGQEDPATWAGDIGNSWRTTGDIQ
DNWDSMTSRADQNDRWASYARPGGWNDPDMLEVGNGGMTTEEYRSHFSIWALAKAPLLIGCDIRSMDNET
FELLSNKEVIAVNQDKLGVQGKKVKKDGDLEVWAGPLSKKRVAVVLWNRGSSRATITARWSDIGLNSSAV
VNARDLWAHSTQSSVKGQLSALVESHACKMYVLTPR
>gnl|CDD|178405 PLN02809, PLN02809, 4-hydroxybenzoate nonaprenyltransferase
YLPPSLRPYAKLARLDKPIGTWLLAWPCMWSIALAAPPGSLPDLKMLALFGCGALLLRGAGCTINDLLDR
DIDKKVERTKLRPIASGALTPFQGVGFLGAQLLLGLGILLQLNNYSRILGASSLLLVFTYPLMKRFTFWP
QAFLGLTFNWGALLGWAAVKGSLDPAVVLPLYASGVCWTLVYDTIYAHQDKEDDLKVGVKSTALRFGDDT
KLWLTGFGAASIGGLALSGYNAGLGWPYYAGLAAAAGHLAWQIQTVDLSSRADCNRKFVSNKWFGAIVFA
GIVLGKLFS
>gnl|CDD|178406 PLN02810, PLN02810, carbon-monoxide oxygenase
MAVGINALPLTFVAHALAVIGAIMVLVWSIYYRGGLAWEATNKNLIFNLHPVLMLIGLIIIGGEAIMSYK
SLPLKKEVKKLIHLVLHAIALILGIFGICAAFKNHNESGIANLYSLHSWLGIGIISLYGIQWIYGFIVFF
FPGGSTNLRSGSLPWHVLFGLFVYILAVGNAALGFLEKLTFLESGGLDKYGSEALLVNFTAIITILYGAF
VVLTALAQSPSDEDDYSYSAI
>gnl|CDD|178407 PLN02811, PLN02811, hydrolase
MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSDSLSPEDFLVEREAML
QDLFPTSDLMPGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAP
DIFLAAARRFEDGPVDPGKVLVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEE
WGLPPFPDSS
>gnl|CDD|178408 PLN02812, PLN02812, 5-formyltetrahydrofolate cyclo-ligase
DEIREQKKALRKEVRRALKALSPEQRAQEDAAIQSRLLELPWFKSSKRLCAYVSCAKLREVDTSKILSEI
LQNPDKRLYVPRVEDKNSNMRMLHITDMADDLVANSMNILEPTPVDADGNPREDVLQAPEPLDLLLLPGL
AFDRSGRRLGRGGGYYDTFLSKYQELAKEKGWKQPLLVALSYSPQILDEGSVPVDETDVLVDALVTPSGV
I
>gnl|CDD|215434 PLN02813, PLN02813, pfkB-type carbohydrate kinase family protein
CASSSTASTSPSLYVPKPNRRLRRVTSQRGAPGLFRIHSRANNAALAIQQDEEQPEGFGPIPEKAVPERW
DVLGLGQAMVDFSGMVDDEFLERLGLEKGTRKVINHEERGKVLRALDGCSYKASAGGSLSNTLVALARLG
SQSAAGPALNVAMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGTTGTVIVLTTPDAQRTMLSYQGTSS
TVNYDSCLASAISKSRVLVVEGYLWELPQTIEAIAQACEEAHRAGALVAVTASDVSCIERHRDDFWDVMG
NYADILFANSDEARALCGLGSEESPESATRYLSHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCVPVDTC
GAGDAYAAGILYGLLRGVSDLRGMGELAARVAATVVGQQGTRLRVEDAVELAESFALHLDGSDMRSDVGS
GHISNF
>gnl|CDD|215435 PLN02814, PLN02814, beta-glucosidase
MKHFSLLSIFLVIVLATSYIDAFTRNDFPEDFLFGAATSAYQWEGAVDEDGRTPSVWDTTSHCYNGGNGD
IASDGYHKYKEDVKLMAEMGLESFRFSISWSRLIPNGRGLINPKGLLFYKNLIKELRSHGIEPHVTLYHY
DLPQSLEDEYGGWINRKIIEDFTAFADVCFREFGEDVKLWTTINEATIFAIGSYGQGIRYGHCSPNKFIN
CSTGNSCTETYIAGHNMLLAHASASNLYKLKYKSKQRGSIGLSIFAFGLSPYTNSKDDEIATQRAKAFLY
GWMLKPLVFGDYPDEMKRTLGSRLPVFSEEESEQVKGSSDFVGIIHYTTFYVTNRPAPSIFPSMNEGFFT
DMGAYIISAGNSSFFEFDATPWGLEGILEHIKQSYNNPPIYILENGMPMKHDSTLQDTPRVEFIQAYIGA
VLNAIKNGSDTRGYFVWSMIDLYELLGGYTTSFGMYYVNFSDPGRKRSPKLSASWYTGFLNGTIDVASQD
TIQLQRNFSGSSSL
>gnl|CDD|215436 PLN02815, PLN02815, L-aspartate oxidase
RSAIAATRKPIGAERASSASRLDDESTKYFDFLVIGSGIAGLRYALEVAEYGTVAIITKDEPHESNTNYA
QGGVSAVLDPSDSVESHMRDTIVAGAFLCDEETVRVVCTEGPERVKELIAMGASFDHGEDGNLHLAREGG
HSHHRIVHAADMTGREIERALLEAVKNDPNITFFEHHFAIDLLTSQDGGSIVCHGADVLDTRTGEVVRFI
SKVTLLASGGAGHIYPSTTNPLVATGDGIAMAHRAQAVVSNMEFVQFHPTALADEGLPIKPAKARENAFL
ITEAVRGDGGILYNLAGERFMPLYDERAELAPRDVVARSIDDQLKKRNEKYVLLDISHKPREEILSHFPN
IAAECLKRGLDITKQPIPVVPAAHYMCGGVRTGLQGETNVQGLYAAGEVACTGLHGANRLASNSLLEALV
FARRAVQPSIDHMARALRDVSAAAAWARPVAPTALADSVMDEILEWTAVVRKELQRIMWNYVGIVRSTER
LETAERKLEELEAEWEAILFRHGWKPTMVGLEACEMRNLFCVAKLVVSSALARKESRGLHYTTDYPELVE
SERKPTVIFPSVPTAGTWSSRSLHRPKRGSRSSR
>gnl|CDD|215437 PLN02816, PLN02816, mannosyltransferase
MDIRKRKNAGGDGDGGADGASVNVGDEPDSFGGRIGSPRRIFLFCLAFRVVNALLIQTYFNPDEHWQSLE
VAHRTIFGYGYMTWEWKRGIRSYLHPMLFAFLYKLLQVTGLDTPYIMIKAPRLMQSIFSAIGDLYLYKLS
DALYGGNVATWSLFCQMANWFIFFCLNRTFSNCLETVLTIMGLYYWPCIRDSSIDYPVNRKWGLVIAALA
CAIRPTSAVIWLYVGMLELFLTPNKVKFIILEVIPIGSLVLGFTCLLDRLMYGSWVIVPLNFLKFNFLSS
GGDYYGTHPWHWYFTQGFLVMLFTFTPFSIAGIIKSKNQKLSALILWVLAIYSILGHKEFRFVLPVLPIA
LIFSGYAFAQMEVSGSSSSSSVTKKKQVPRQNHTKWSPKLRLSVYFLLATNIPMALYMSLFHQRGTEDAM
NYLSDEAYKGRVKSILFLMPCHSTPYYSTLHRNIPMQFLDCTPSAEKGELDESDQFLVNPLGFASELARN
WSEPPSHIVLFASEETKLRDFMIQHSFKEVRRFFHAHFKVDRDLQSSVVVYVVNHT
>gnl|CDD|166458 PLN02817, PLN02817, glutathione dehydrogenase (ascorbate)
MSSVRIPTTAGAVSATIKHAGYNPRFGTSHGGAKGVKRVGGRRRKYLTAITMSSPLEVCVKASLTVPNKL
GDCPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKYPDP
PLATPPEKASVGSKIFSTFIGFLKSKDPGDGTEQALLDELTSFDDYIKENGPFINGEKISAADLSLGPKL
YHLEIALGHYKNWSVPDSLPFVKSYMKNIFSMESFVKTRALPEDVIAGWRPKVMG
>gnl|CDD|215438 PLN02818, PLN02818, tocopherol cyclase
ALRTPHSGYHFDGTPRRFFEGWYFKVSLPEVKQSFAFMYSIEDPAFRERMSGLEELLHGSRFTGVGAQIL
GPDDKYLCQFTEDSTKFWGSRHELALGNTFAPKNGSTPPRSEVPPDEFYRRVEEGFQVTPFWHQGRLRDD
GRSPYAKTVKTARWEYSTRPVYGWGDVGSKQKSTAGWLAALPVFEPHWQICMAHGLATGWIEWGGERYEF
EDAPSYSEKNWGGGFPSKWFWVQCNVFDGASGLSLTAGGGLRGLPLLPGVFEEVALIGVHYDGKFYEFVP
WNGEVEWDVSPWGRWKLRAENETHEVELEATTAKEPGTVLRAPTTDVGLAPFCRDTFAGKLKLQLWERSW
DGSKGKLILDATSSMAAVEVGGGPWWSTWKGTARMKEPLKSLLGLPVDVESIF
>gnl|CDD|215439 PLN02819, PLN02819, lysine-ketoglutarate reductase/saccharopine dehydrogenase
MKLGNGVVGILAETVNKWERRAPLTPSHCARLLHSGKDRTVSRIIVQPSSKRIHHDAQYEDVGCEISEDL
SDCGLILGVKQPKLEMLLPDRAYAFFSHTHKAQPENMPLLDKILEERVSLFDYELIVGDHGKRLVAFGKY
AGRAGMIDFFRGLGQRLLSLGYSTPFLSLGSSYMYSSLAAAKAAVISVGEEIASSGLPLGICPLVFVFTG
SGNVSQGAQEIFKLLPHTFVEPSKLPELKGISQNKISTKRVYQVYGCVVTSQDMVEHKDPSKQFDKADYY
AHPEHYNPVFHEKIAPYASVIVNCMYWEKRFPRLLTTKQLQDLTRKGGCPLVGVCDITCDIGGSIEFLNK
TTSIEKPFFRYNPSNNSYHDDMDGDGILCMAVDILPTEFAKEASQHFGNILSPFVGSLASMKELAELPSH
LRRACIAHRGSLTPLFEYIPRMRNSNAELAQDTVSSQSTFNILVSLSGHLFDKFLINEALDVIEAAGGSF
HLAKCQVGQSADAESYSELEVGADDKEVLDQIIDSLTRLANPNEDYISPAREANKIFLKIGKVQQENECN
EKAEVTKKSQNVLILGAGRVCRPAAEYLASVKTISYYGDDSEEPTDVHVIVASLYLKDAKETVEGIENAE
AVQLDVSDSESLLKYVSQVDVVISLLPASCHAVVAKACIELKKHLVTASYVSEEMSALDSKAKEAGITIL
CEMGLDPGIDHMMAMKMIDDAHERGGKVKSFTSYCGGLPSPEAANNPLAYKFSWNPAGAIKAGQNPAVYK
SNGQIIHVDGENLFASAVRFRLPNLPAFALECLPNRDSLVYGELYGIEKEAATIFRGTLRYEGFSMIMAT
LSKLGLFDSENHPLLSTGKRTTYGALLDALLLQDGHNENGPLAGEEEISKRLAKLGHSKNRETAAKAAKT
IVFLGLDEETEVPKSCKSIFDVTCYRMEEKLAYSGNEQDMVLLHHEVEVEFPDSKRIEKHSATLLEFGEI
KNGRTTTAMAKTVGIPAAIGALLLLEGKIKTRGVLRPLEPEVYVPALEILQAYGIKLMEKVE
>gnl|CDD|178415 PLN02820, PLN02820, 3-methylcrotonyl-CoA carboxylase, beta chain
IQQVAFRPRTSSTPASASFFRLGKRSFCLGVLPDGVDRNSDAFSANSKAMEGLLSELRSHVAKVRAGGGP
EAVKRHRSRNKLLPRERIDRLLDPGSPFLELSQLAGHELYGEDLPSGGIVTGIGPVHGRLCMFVANDPTV
KGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDHFGRIFYNQARMSSAGIPQIA
LVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSDHFAQDE
LHALAIGRNIVKNLHLAAKQGMENTLGSKNPEYKEPLYDVKELRGIVPADHKQSFDVRSVIARIVDGSEF
DEFKKNYGTTLVTGFARIYGQPVGIIGNNGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSE
ASGIAKAGAKMVMAVACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQ
IERENKKRQGIQWSKEEEEAFKAKTVEAYEREANPYYSTARLWDDGVIDPADTRRVLGLCLSAALNRSPE
DTKFGVFRM
>gnl|CDD|215440 PLN02821, PLN02821, 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase
MAVVLQLLRVSLRSAFSSLSGSFRRRAPRSVRCSASVVQSSSASEEEESDFDKKEFRHNLTRSDNYNRRG
FGHKKETLELMGVEYSTSDLVKTLKENGNVYTWGDVTVKLAKAYGFCWGVERAVQIAYEARKQFPDEKLW
ITNEIIHNPTVNKRLEEMNVQFIEVEEGGKDFSVVGEGDVVILPAFGASVEEMQTLNDKNVQIVDTTCPW
VSKVWNTVEKHKKKDYTSVIHGKYAHEETVATASFAGKYIIVKNMKEATYVCDYILGGQLDGSSGTKEEF
LEKFKNAVSKGFDPDTDLVKVGIANQTTMLKGETEEIGKLLEKTMMQKYGVENVNDHFMSFNTICDATQE
RQDAMYKLVEEKLDLMLVVGGWNSSNTSHLQEIAEHKGIPSYWIDSEERIGPGNTIAHKLNHGELVEKEN
WLPEGPVTIGVTSGASTPDKVVEDVLDKVFDIKREEALQL
>gnl|CDD|178417 PLN02822, PLN02822, serine palmitoyltransferase
MALNVLNLVNAALERVTMLLEAPLARAVVFGVHIGGHLVVEGLLIVVIVFLLSQKSYKPPKRPLTEKEID
ELCDEWTPEPLIPPITEEMRPEPPVLESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYG
VGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGL
YLSRSTIVYFKHNDMESLRNTLEKLTAENKRKKKLRRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLL
DESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSASLPP
YLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVFLHLEKSTGSAKEDLSLLE
HIADRMLKEDSVLVVVSKRSTLDKCRLPVGIRLFVSAGHTESDILKASESLKRVAASVLKK
>gnl|CDD|178418 PLN02823, PLN02823, spermine synthase
AVEIVHGNGTSHITAVATPTAALASNYAKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFG
KVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVV
DFCRKHLTVNREAFCDKRLELIINDARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSFYERIVKPKL
NPGGIFVTQAGPAGILTHKEVFSSIYNTLRQVFKYVVPYTAHVPSFADTWGWVMASDHPFADLSAEELDS
RIKERIDGELKYLDGETFSSAFALNKTVRQALANETHVYTEENARFIHGHGTAAKA
>gnl|CDD|178419 PLN02824, PLN02824, hydrolase, alpha/beta fold family protein
TVKPEPQVETRTWRWKGYNIRYQRAGTSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSD
KPNPRSAPPNSFYTFETWGEQLNDFCSDVVGDPAFVICNSVGGVVGLQAAVDAPELVRGVMLINISLRGL
HIKKQPWLGRPFIKAFQNLLRETAVGKAFFKSVATPETVKNILCQCYHDDSAVTDELVEAILRPGLEPGA
VDVFLDFISYSGGPLPEELLPAVKCPVLIAWGEKDPWEPVELGRAYANFDAVEDFIVLPGVGHCPQDEAP
ELVNPLIESFVARH
>gnl|CDD|215441 PLN02825, PLN02825, amino-acid N-acetyltransferase
FVRWFREAWPYIQGHRGSTFVVVISGEVVAGPHLDNILQDISLLHGLGIKFVLVPGTHVQIDKLLAERGR
EPKYVGAYRITDSAALQASMEAAGKIRVMIEAKLSPGPSIPNLRRHGDNSRWHEVGVSVASGNFLAAKRR
GVVNGVDFGATGEVKKIDVSRIKERLDSNCIVLLSNLGYSSSGEVLNCNTYEVATACALAIGADKLICIV
DGPILDENGRLIRFMTLEEADMLIRKRAKQSEIAANYVKAVGGEDYSYSLGLDSVNTTPFNNNGRGFWGS
GSATDSFQNGVGFDNGNGLSGEQGFAIGGEERLSRLNGYLSELAAAAFVCRGGVQRVHLLDGTIEGVLLL
ELFTRDGMGTMIASDMYEGTRMARVEDLAGIRQIIRPLEESGILVRRTDEELLRALDSFVVVEREGSIIA
CAALFPFFEEKCGEVAAIAVSPECRGQGQGDKLLDYIEKKAASLGLEKLFLLTTRTADWFVRRGFSECSI
ESLPEARRKRINLSRGSKYYMKKLL
>gnl|CDD|178421 PLN02826, PLN02826, dihydroorotate dehydrogenase
GRLLTGALIGLAIAGGAYVSTVDEATFCGWLFNATKLVNPLFRLLDPETAHSLAISAAARGLVPREKRPD
PSVLGVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSVTPLPQPGNPKPRVFRLREEGAIIN
RYGFNSEGIVAVAKRLGAQHGKRKLDETSSSSFSSDDVKAGGKAGPGILGVNLGKNKTSEDAAADYVQGV
RALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAARDEMQWGEEGPPPLLVKIAPDLSKEDLED
IAAVALALGIDGLIISNTTISRPDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGV
SSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQEAVGADHR
>gnl|CDD|215442 PLN02827, PLN02827, Alcohol dehydrogenase-like
SSSSISQPNVITCRAAVAWGAGEALVMEEVEVSPPQPLEIRIKVVSTSLCRSDLSAWESQALFPRIFGHE
ASGIVESIGEGVTEFEKGDHVLTVFTGECGSCRHCISGKSNMCQVLGLERKGVMHSDQKTRFSIKGKPVY
HYCAVSSFSEYTVVHSGCAVKVDPLAPLHKICLLSCGVAAGLGAAWNVADVSKGSSVVIFGLGTVGLSVA
QGAKLRGASQIIGVDINPEKAEKAKTFGVTDFINPNDLSEPIQQVIKRMTGGGADYSFECVGDTGIATTA
LQSCSDGWGLTVTLGVPKAKPEVSAHYGLFLSGRTLKGSLFGGWKPKSDLPSLVDKYMNKEIMIDEFITH
NLSFDEINKAFELMREGKCLRCVIHMPK
>gnl|CDD|178422 PLN02828, PLN02828, formyltetrahydrofolate deformylase
LSDCIASRGGNILGVDVFVPENKNVFYSRSEFIFDPVKWPRAQMDEDFQEISKHFKALKSVVRVPGLDPK
YKIAVLASKQDHCLIDLLHRWQDGRLPVDITCVISNHERGPNTHVMRFLERHGIPYHYLPTTKENKREDE
ILELVKGTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEE
LDAGPIIEQMVERVSHRDNLRSFVQKSENLEKQCLAKAIKSYCELRVLPYGTNKTVVF
>gnl|CDD|215443 PLN02829, PLN02829, Probable galacturonosyltransferase
MRMRLRNLVLGLLLLTVLSPILLYTDRLSASFTPSSKRDFLEDVTALTLGGDASKLNVLPQESSSSLKEP
IGIVYSDNSSKTIEPDSQDLLLDKRGEHKARVLSATDDDTHSQTDDIIKQVTQKAGQDDSDQQEKNSQSQ
SASQAESLEHVQQSAQTSEKVDEKEPLLTKTDKQTDQTVMPDARVRQLRDQLIKAKVYLSLPATKANPHF
TRELRLRIKEVQRVLGDASKDSDLPKNANEKLKAMEQTLAKGKQMQDDCSIVVKKLRAMLHSAEEQLRVH
KKQTMFLTQLTAKTLPKGLHCLPLRLTTEYYNLNSSEQQFPNQEKLEDPQLYHYALFSDNVLAAAVVVNS
TVTNAKHPSKHVFHIVTDRLNYAAMRMWFLVNPPGKATIQVQNIEEFTWLNSSYSPVLKQLGSQSMIDYY
FRAHRANSDSNLKYRNPKYLSILNHLRFYLPEIFPKLNKVLFLDDDIVVQKDLTGLWSIDLKGNVNGAVE
TCGESFHRFDRYLNFSNPLISKNFDPHACGWAYGMNVFDLDEWKRQNITEVYHSWQKLNHDRQLWKLGTL
PPGLITFWKRTYPLDRSWHVLGLGYNPNVNQRDIERAAVIHYNGNMKPWLEIGIPKYRNYWSKYVDYDQV
YLRECNINP
>gnl|CDD|215444 PLN02830, PLN02830, UDP-sugar pyrophosphorylase
SALSVASKSDSSVPSLHSNLALLSPDQRALVRRLLELGQSHLFEHWPEPGVDDDDKRRLLEQVARLDESY
PGGLAAYVSNAKELLADSKEGVNPFEGWTPSVPEGEVLEYGSEEFVELEEAGLREAGNAAFVLVAGGLGE
RLGYSGIKVALPTETATGTCYLQLYIESILALQERAKKRKAKKGRKIPLVIMTSDDTHARTLKLLERNDY
FGMDPDQVTLLKQEKVACLMDNDARLALDPNDPYKIQTKPHGHGDVHALLYSSGLLDKWLSAGKKWVVFF
QDTNGLVFKAIPAALGVSATKGFDMNSLAVPRKAKEAIGAIAKLTHKDGREMVINVEYNQLDPLLRATGH
PDGDVNDETGYSPFPGNINQLILKLGPYVKELAKTGGVIEEFVNPKYKDATKTAFKSPTRLECMMQDYPK
TLPPSAKVGFTVFDNWLAYSPVKNSPADGAAKVPEGNPTHSATSGEMAIYGANCLILRKAGADVEEPVED
VVFNGIEVEVGPRIVLKPAFALTFSELKKKVAPGSVKISQRSTLVLEGADIVIENLSLDGALVVRAVPGA
EVTVGGLRVKNKGWTWEPVDKGTSAPEEIRIRGFVIKKVETAELVFDKPGKYTVP
>gnl|CDD|215445 PLN02831, PLN02831, Bifunctional GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone-4-phosphate synthase
DSASFGTLAAEITPTTDDFFVSDAEGDPDRPTEGFSSIAEALEDIRQGKFVVVVDDEDRENEGDLIMAAS
LVTPEAMAFLVKHGSGIVCVSMKGEDLDRLRLPLMVPSKENEEKMATAFTVTVDAKHGTTTGVSASDRAK
TILALASPDSKPEDFRRPGHIFPLRYREGGVLKRAGHTEAAVDLAVLAGLPPVGVLCEIVNDEDGSMARL
PQLRKFAEEHGLKIISIADLIRYRRKREKLVERTAVARLPTKWGLFTAYCYRSKLDGIEHIAFVKGDIGD
GQDVLVRVHSECLTGDIFGSARCDCGNQLALAMQLIEKAGRGVLVYLRGHEGRGIGLGHKLRAYNLQDEG
RDTVEANEELGLPVDSREYGIGAQILRDLGVRTMRLMTNNPAKYTGLKGYGLAVVGRVPLLTPITKENKR
YLETKRTKMGHVYGSDLGGHVSGLESAETN
>gnl|CDD|215446 PLN02832, PLN02832, glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
MMAIGVLALQGSFNEHIAALRRLGVEAVEVRKPEQLEGVSGLIIPGGESTTMAKLAERHNLFPALREFVK
SGKPVWGTCAGLIFLAERAVGQKEGGQELLGGLDCTVHRNFFGSQINSFETELPVPELAASEGGPETFRA
VFIRAPAILSVGPGVEVLAEYPLPSEKALYSSSTDAEGRDKVIVAVKQGNLLATAFHPELTADTRWHSYF
VKMVSESEEYASSSELAVAKVDESSISLEPPKDLPIFQ
>gnl|CDD|215447 PLN02833, PLN02833, glycerol acyltransferase family protein
DADRDSEELLRSRSELDLDRPNIEDYLPSGSSIQEPSGKLLLRDLLDISGVLTEAASAIVDDSFTRCFKS
NPPEPWNWNIYLFPLWCVGVVIRYGILFPVRVLLLAIGWIIFLSAFIPVHFLLKGHKLRKKIERKLVELI
CSAFVASWTGVIKYHGPRPSRRPKQVFVANHTSMIDFIVLEQMTPFAVIMQKHPGWVGFLQNTILESVGC
IWFNRTEAKDREVVAKKLRDHVQDPDRNPLLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKYNKIFV
DAFWNSRKQSFTMHLLRLMTSWAVVCDVWYLEPQTLRPGETPIEFAERVRDMIAKRAGLKKVPWDGYLKY
YRPSPKHTEKKQQSFAESLLRRLEEK
>gnl|CDD|215448 PLN02834, PLN02834, 3-dehydroquinate synthase
KKSSSADNSESNTPTVLSRSPSDAFFDQNSSIESSKEGDLTEVIHEKCPVSGANKSEVTKTASATVTTVV
KVDLGDRSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPELTVESVILPDG
EKYKDMETLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGK
TGVNHPLGKNMIGAFYQPQCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDP
GALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRL
GWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKSLMAVDKKVADGLLRLILLKGELGNCVFTGDFDREA
LEETLRAFCKSDH
>gnl|CDD|178429 PLN02835, PLN02835, oxidoreductase
MGSAVNLHLLLGVLAVLSSVSLVNGEDPYKYYTWTVTYGTISPLGVPQQVILINGQFPGPRLDVVTNDNI
ILNLINKLDQPFLLTWNGIKQRKNSWQDGVLGTNCPIPPNSNYTYKFQTKDQIGTFTYFPSTLFHKAAGG
FGAINVYERPRIPIPFPLPDGDFTLLVGDWYKTSHKTLQQRLDSGKVLPFPDGVLINGQTQSTFSGDQGK
TYMFRISNVGLSTSLNFRIQGHTMKLVEVEGSHTIQNIYDSLDVHVGQSVAVLVTLNQSPKDYYIVASTR
FTRQILTATAVLHYSNSRTPASGPLPALPSGELHWSMRQARTYRWNLTASAARPNPQGSFHYGKITPTKT
IVLANSAPLINGKQRYAVNGVSYVNSDTPLKLADYFGIPGVFSVNSIQSLPSGGPAFVATSVMQTSLHDF
LEVVFQNNEKTMQSWHLDGYDFWVVGYGSGQWTPAKRSLYNLVDALTRHTAQVYPKSWTTILVSLDNQGM
WNMRSAIWERQYLGQQFYLRVWNQVHSLANEYDIPDNALLCGKAIGRHP
>gnl|CDD|215449 PLN02836, PLN02836, 3-oxoacyl-[acyl-carrier-protein] synthase
PPLPTRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLKMKSEDEETQLYTLDQLPSRVAALV
PRGTGPGDFDEELWLNSRSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQ
LICEKRLRRLSPFFVPRILINMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGG
TESSIDALSIAGFSRSRALSTKFNSCPTEASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVR
GYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAHATSTPLGDAVEARAIKTVFSEHATS
GGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFVPLTASKAMLIRAALSN
SFGFGGTNASLLFTSPP
>gnl|CDD|215450 PLN02837, PLN02837, threonine-tRNA ligase
VSAAAASAATEEASAAAASDEKGPGEAEPERVVLPTNESSEKLLKIRHTCAHVMAMAVQKLFPDAKVTIG
PWIENGFYYDFDMEPLTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMAINEPYKLEILEGIKEE
PITIYHIGEEWWDLCAGPHVERTGKINKKAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQLKAYLHF
KEEAKRRDHRRLGQDLDLFSIQDDAGGGLVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLW
KTSGHLDFYKENMYDQMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGL
FRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSKYEINLSTRPEKSVGSDDIWEKATTALRD
ALDDKGWEYKVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRA
ILGSLERFFGVLIEHYAGDFPLWLAPVQARVLPVTDNELEYCKEVVAKLKAKGIRAEVCHGERLPKLIRN
AETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFINRIQLAVENRTSL
>gnl|CDD|166479 PLN02838, PLN02838, 3-hydroxyacyl-CoA dehydratase subunit of elongase
MAGFGSLLRRLYLTVYNWVVFIGWAQVLYLAVTTLKESGHEAVYAAVERPLQLAQTAAVLEILHGLVGLV
RSPVSATLPQIGSRLFLTWGILWSFPEVRSHILVTSLVISWSITEIIRYSFFGMKEAFGFAPSWLLWLRY
STFLLLYPTGITSEVGLIYIALPYMKASEKYCLRMPNKWNFSFDYFYASILVLAIYVPGSPHMYSYMLGQ
RKKALSKSKRE
>gnl|CDD|178432 PLN02839, PLN02839, nudix hydrolase
MASGFCSLCPTVTSLFSSHALIPTLRWRSSSMSRSPLRHSRAVSAATTVPISSSFTWDDVIETGRAEYVP
QNSSDLTGFLEKVDRCNRGSEKLGEFIPFVIEEQIVGYIHKGFTEYLREFHDIFTFSQNGSCPDRVDGHV
TLNLMLQKPEDRTRAVADVIKILGDKGIIPGIRNELYPVKPSFNAPVFFSLERAAAPYFGIKGYGVHMNG
YVERDGQKFLWIGKRSLSKSTYPGMLDHLVAGGLPHGISCGENLVKECEEEAGISKAIADRAIAVGAVSY
MDIDQYCFKRDVLFCYDLELPQDFVPKNQDGEVESFKLIPVAQVANVIRKTSFFKANCSLVIIDFLFRHG
FIRPESSGYLDLYRRLRNGDCS
>gnl|CDD|215451 PLN02840, PLN02840, tRNA dimethylallyltransferase
RRFCAATTALSGSGASKTKKEKVIVISGPTGAGKSRLALELAKRLNGEIISADSVQVYRGLDVGSAKPSL
SERKEVPHHLIDILHPSDDYSVGAFFDDARRATQDILNRGRVPIVAGGTGLYLRWYIYGKPDVPKSSPEI
TSEVWSELVDFQKNGDWDAAVELVVNAGDPKARSLPRNDWYRLRRSLEIIKSSGSPPSAFSLPYDSFREQ
LVTEDTDSSLEDGSSAETELDYDFLCFFLSSPRLDLYRSIDLRCEEMLAGTNGILSEASWLLDLGLLPNS
NSATRAIGYRQAMEYLLQCRQNGGESSPQEFLAFLSKFQTASRNFAKRQMTWFRNEPIYHWLDASQPLEK
ILQFIYDAYHSRTARVVVPESLRMKKEVSCSRESSELKTYRSKNRHFVSREDCSHVLEWIRRTQCKASAS
C
>gnl|CDD|178434 PLN02841, PLN02841, GPI mannosyltransferase
EASAAMTLRSLLLASALLRVALIVYGEWQDAHMEVRYTDVDYLVFSDAAALVASGKSPFARDTYRYSPLL
ALLLVPNSLLHRSWGKFLFSAADLLVGLFIHTILRLRGVPEKVCTWSVMVWLFNPFTFTIGTRGNCEPIV
CAVILWILICLMNGRLLQAAFWYGLVVHFRIYPIIYALPIILVLDKQYFGPGGRPALTKWNSKQNKTPSS
NTEATSFLFNLWTFLTSLFSRERIMFGLISGGVFFALTGVSFYLYGWEFLNEALLYHLTRTDPRHNFSIY
FYHIYLHHEQGFSLVERLASFLPQFLVQLALILCFSQDLPFCLFLQTVAFVAFNKVITAQYFVWFFCLLP
LILPWSRMKLKWKGLLCILVWMGSQLHWLMWAYLLEFKGRNVFLQLWIASLLFLAANTFVLLMIIQHHRF
SPLFQRLESSSSSKNPKKKE
>gnl|CDD|178435 PLN02842, PLN02842, nucleotide kinase
MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAGTDIGKRAKEFMNSGRLVPDEIVIAMVTGRLS
REDAKEKGWLLDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKNFPPES
EEIKARLITRPDDTEEKVKARLQIYKKNAEAILSTYSDIMVKIDGNRPKEVVFEEISSLLSQIQKDATKM
IKTKKASPVQDKWRGIPTRLNNIPHSREIRAYFYDDVLQATQRAVNDGRTRLKVEINIPELNPEMDVYRI
GTLMELVRVLALSFADDGKRVKVCVQGSMGEGALAGMPLQLAGTRKILEFMDWGDYGAKGTFVKIGAIGA
KEVDEEDDMFILVAPQNAVGNCIIDDLQAMTTAAGKRPVILVNPRLKDLPGSSGIMQTMGREQRLEYAAS
FENCYSFRLLYYAGTQYPIMGALRMSYPYRYELYKRVDEENGKEKYIILATFSERPTPDEINDAFSGRSR
DQAKKASGIWGFLSI
>gnl|CDD|215452 PLN02843, PLN02843, isoleucyl-tRNA synthetase
MRANSVTREPEIQKLWEENQVYKRVSDRNNGESFTLHDGPPYANGDLHIGHALNKILKDFINRYQLLQGK
KVHYVPGWDCHGLPIELKVLQSLDQEARKELTPIKLRAKAAKFAKKTVDTQRESFKRYGVWGDWENPYLT
LDPEYEAAQIEVFGQMFLNGYIYRGRKPVHWSPSSRTALAEAELEYPEGHVSKSIYVAFPVVSPSETSPE
ELEEFLPGLSLAIWTTTPWTMPANAAVAVNDKLQYSVVEVQSFSEDESTSGGNKKKRPGNVLKEQQKLFL
IVATDLVPALEAKWGVKLVVLKTFPGSDLEGCRYIHPLYNRESPVVIGGDYITTESGTGLVHTAPGHGQE
DYITGLKYGLPLLSPVDDAGKFTEEAGQFSGLSVLGEGNAAVVEALDEAGSLLMEEAYGHKYPYDWRTKK
PTIFRATEQWFASVEGFRQAALDAIDKVKWIPAQGENRIRAMVSGRSDWCISRQRTWGVPIPVFYHVETK
EPLMNEETIAHVKSIVAQKGSDAWWYMDVEDLLPEKYRDKASDYEKGTDTMDVWFDSGSSWAGVLGSREG
LSYPADLYLEGSDQHRGWFQSSLLTSVATKGKAPYKSVLTHGFVLDEKGFKMSKSLGNVVDPRLVIEGGK
NQKQEPAYGADVLRLWVASVDYTGDVLIGPQILKQMSDIYRKLRGTLRYLLGNLHDWKPDNAVPYEDLPS
IDKYALFQLENVVNEIEESYDNYQFFKIFQILQRFTIVDLSNFYLDVAKDRLYVGGTTSFTRRSCQTVLA
AHLLSLLRAIAPILPHLAEDAWQNLPFQEDGSAAESVFEAGWPTPNEEWLSFPAEDVDFWSLLLEVRDEV
NKVLESARNGKLIGASLEAKVYLHASDASLAARLAELCGASNGADELRRIFITSQVEVVSSEDDETAACG
SYTGEYVEGAGRVWVGVSRADGSKCERCWNYSPAVGSFSDHPTLCERCYPVVIAQPPPLAAAAV
>gnl|CDD|215453 PLN02844, PLN02844, oxidoreductase/ferric-chelate reductase
MAKALTLLVLKLLMILIFAGWIALWILKPTNLWTRKWKQAEDSARHTVFGYYGLNFAVYTFPPIALAIIG
LVYLSLLSQEPHRRRGARSATIGVSNPVIVNSFIGILSCLEILAVLLFFLFLAWTFYARISNDFKKLMPV
KSLNLNLWQLKYLRVATRFGLLAEACLALLLLPVLRGLALFRLLGIQFEASVRYHVWLGTSMIFFATVHG
ASTLFIWGISHHIQDEIWKWQKTGRIYLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFF
LFHAGDRHFYMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDPGLKYAPTSVIFMKIP
SISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIPVAIEGPYGPASVDF
LRYDSLLLVAGGIGITPFLSILKEIASQSSSRYRFPKRVQLIYVVKKSQDICLLNPISSLLLNQSSNQLN
LKLKVFVTQEEKPNATLRELLNQFSQVQTVNFSTKCSRYAIHGLESFLWMAAMVALTSITFLVFLIGLNH
IFIPSEHKSHSGVKMAASGEMKTAKEKTPSWVVDLLLIVSFIIAITCSTFVAIILRWRRLKKEIPRVSQK
QGIKPEEGSMEKRGPVLEEHEIHFGGRPNFQDIFSKFPKETRGSDIGVLVCGPETMKESVASMCRLKSQC
FNVGDDGKRKMYFSFHSLNFTL
>gnl|CDD|215454 PLN02845, PLN02845, Branched-chain-amino-acid aminotransferase-like protein
SPSVVPGSRTKVPPLLSAAEMIQRLQSKWSDAKKQNFGAMYSSVVGGITTDPAAMVIPLDDHMVHRGHGV
FDTATIRDGHLYELDAHLDRFLRSAAKAKIPLPFDRATLRRILLQTVAASGCRNGSLRYWLSAGPGGFSL
SPSGCSEPAFYAVVIEDTYAQDRPEGVKVVTSSVPIKPPQFATVKSVNYLPNALSQMEAEERGAFAGIWL
DEEGFVAEGPNMNVAFLTNDGELVLPPFDKILSGCTARRVLELAPRLVSPGDLRGVKQRKISVEEAKAAD
EMMLIGSGVPVLPIVSWDGQPIGDGKVGPITLALHDLLLDDMRSGPPGVRTPVPYG
>gnl|CDD|166487 PLN02846, PLN02846, digalactosyldiacylglycerol synthase
MQKKQHIAIFTTASLPWMTGTAVNPLFRAAYLAKDGDREVTLVIPWLSLKDQKLVYPNKITFSSPSEQEA
YVRQWLEERISFLPKFSIKFYPGKFSTDKRSILPVGDISETIPDEEADIAVLEEPEHLTWYHHGKRWKTK
FRLVIGIVHTNYLEYVKREKNGRVKAFLLKYINSWVVDIYCHKVIRLSAATQDYPRSIICNVHGVNPKFL
EIGKLKLEQQKNGEQAFTKGAYYIGKMVWSKGYKELLKLLHKHQKELSGLEVDLYGSGEDSDEVKAAAEK
LELDVRVYPGRDHADPLFHDYKVFLNPSTTDVVCTTTAEALAMGKIVVCANHPSNEFFKQFPNCRTYDDG
KGFVRATLKALAEEPAPLTDAQRHELSWEAATERFLRVADLDLPSSAKPNKSSLKNFMSTSPNLKKNMED
ASAYLHNVASGFETSRRAFGAIPGSLQPDEQQCKELGLALQT
>gnl|CDD|178439 PLN02847, PLN02847, triacylglycerol lipase
MAAATMATAVGAAVLLYYVLSRRLAAEDGEDGGGGGDGSSGRSGRRRIARRPAQAPATWLETITTLSETL
RFTYSETLGKWPIGDLAFGINYLMRRQGNLQVASVYAGSNCIELKGPEIIAELIVLLRLLTLCMLFSKKP
FPVFLELAGFSQEDVLIQKPKAGILKPAFTIIRDENSKCFLLLIRGTHSIKDTLTAATGAVVPFHHSVLH
DGGVSNLVLGYAHCGMVAAARWIAKLSTPCLLKALDEYPDFKIKIVGHSLGGGTAALLTYILREQKEFSS
TTCVTFAPAACMTWDLAESGKHFITTIINGSDLVPTFSAASVDDLRSEVTASSWLNDLRDQVEHTRVLNV
VYRSATALGSRLPSIASARARVAGAGALLRPVSSSTQVVMKRAQNVAQAVVRTRSSLSSWSCMGPRRRSV
GSVANSKKEDLPEATHVTSSVNSESLVTEVKTTKSVEHKSESSSSDGSGHDDEEEEEPLLSEDRVITSSV
EEEVTEGELWYELEKELQRQETEVDAQAQEEEAAAAKEITEEENVLAKAVESKTSITSSDLSESQQFYPP
GRIMHIVSMPPSDSENDDDEVATEEHVGIYETPRELYSKIRLSRTMINDHYMPMYKKMMELLIEELENDE
DSS
>gnl|CDD|178440 PLN02848, PLN02848, adenylosuccinate lyase
SRDLELSNLTALSPLDGRYWSKVKDLRPIFSEFGLIRYRVLVEVKWLLKLSQIPEVTEVPPFSDEANSFL
EGIIAGFSVDDALEVKKIERVTNHDVKAVEYFLKQKCKSHPELAKVLEFFHFACTSEDINNLSHALMLKE
GVNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLSEVKIKGKF
AGAVGNYNAHMSAYPEVDWPAVAEEFVTSLGLTFNPYVTQIEPHDYMAELFNAVSRFNNILIDFDRDIWS
YISLGYFKQITKAGEVGSSTMPHKVNPIDFENSEGNLGLANAELSHLSMKLPISRMQRDLTDSTVLRNMG
VGLGHSLLAYKSTLRGIGKLQVNEARLAEDLDQTWEVLAEPIQTVMRRYGVPEPYEKLKELTRGRAVTKE
SMREFIEGLELPEEAKDQLLKLTPHTYIGAAAALALNI
>gnl|CDD|215455 PLN02849, PLN02849, beta-glucosidase
MELILSLFTIFLLLALSSGKCSSDYSRSDFPEGFVFGAGTSAYQWEGAFDEDGRKPSVWDTFLHSRNMSN
GDIACDGYHKYKEDVKLMVETGLDAFRFSISWSRLIPNGRGSVNPKGLQFYKNFIQELVKHGIEPHVTLF
HYDHPQYLEDDYGGWINRRIIKDFTAYADVCFREFGNHVKFWTTINEANIFTIGGYNDGITPPGRCSSPG
RNCSSGNSSTEPYIVGHNLLLAHASVSRLYKQKYKDMQGGSIGFSLFALGFTPSTSSKDDDIATQRAKDF
YLGWMLEPLIFGDYPDEMKRTIGSRLPVFSKEESEQVKGSSDFIGVIHYLAASVTNIKIKPSLSGNPDFY
SDMGVSLGKFSAFEYAVAPWAMESVLEYIKQSYGNPPVYILENGTPMKQDLQLQQKDTPRIEYLHAYIGA
VLKAVRNGSDTRGYFVWSFMDLYELLKGYEFSFGLYSVNFSDPHRKRSPKLSAHWYSAFLKGNSTFLGSQ
GITQLQSNFSSSF
>gnl|CDD|215456 PLN02850, PLN02850, aspartate-tRNA ligase
SSQEAVEESGEKISKKAAKKAAAKAEKLRREATAKAAAASLEDEDDPLASNYGDVPLEELQSKVTGREWT
DVSDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVSEVTVSKGMVKYAKQLSRESVVD
VEGVVSVPKKPVKGTTQQVEIQVRKIYCVSKALATLPFNVEDAARSESEIEKALQTGEQLVRVGQDTRLN
NRVLDLRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQ
LHKQMAICGDFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERC
KKELEAIREQYPFEPLKYLPKTLRLTFAEGIQMLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTDFYIL
HRYPLAVRPFYTMPCPDDPKYSNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRY
GAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP
>gnl|CDD|178443 PLN02851, PLN02851, 3-hydroxyisobutyryl-CoA hydrolase-like protein
MQRVKALRRVAVPLQWVRFGSVSYGRSFSALPNYAANDDLQDQVLVEGRAKSRAAILNRPSSLNALTIPM
VARLKRLYESWEENPDIGFVLMKGSGRAFCSGADVVSLYHLINEGNVEECKLFFENLYKFVYLQGTYLKP
NVAIMDGITMGCGAGISIPGMFRVVTDKTVFAHPEVQMGFHPDAGASYYLSRLPGYLGEYLALTGQKLNG
VEMIACGLATHYCLNARLPLIEERLGKLLTDDPAVIEDSLAQYGDLVYPDKSSVLHKIETIDKCFGHDTV
EEIIEALENEAASSYDEWCKKALKKIKEASPLSLKVTLQSIREGRFQTLDQCLAREYRISLCGVSKWVSG
DFCEGVRARLVDKDFAPKWDPPSLGEVSKDMVDCYFTPLDESESELELPTAQREPYM
>gnl|CDD|215457 PLN02852, PLN02852, ferredoxin-NADP+ reductase
MSRLRARTWLSRALSFSNSSSSTSEPLHVCVVGSGPAGFYTADKLLKAHDGARVDIIERLPTPFGLVRSG
VAPDHPETKNVTNQFSRVATDDRVSFFGNVTLGRDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGV
LSAREFVWWYNGHPDCVHLPPDLKSSDTAVVLGQGNVALDCARILLRPTDELASTDIAEHALEALRGSSV
RKVYLVGRRGPVQAACTAKELRELLGLKNVRVRIKEADLTLSPEDEEELKASRPKRRVYELLSKAAAAGK
CAPSGGQRELHFVFFRNPTRFLDSGDGNGHVAGVKLERTVLEGAAGSGKQVAVGTGEFEDLPCGLVLKSI
GYKSLPVDGLPFDHKRGVVPNVHGRVLSSASGADTEPGLYVVGWLKRGPTGIIGTNLTCAEETVASIAED
LEQGRLRGVASPPKPGRDGLLELLESRGVRVVPFSGWEKIDSAEKEAGRARGKPREKITSIEEMLKAANE
K
>gnl|CDD|215458 PLN02853, PLN02853, Probable phenylalanyl-tRNA synthetase alpha chain
AAMAEEALLGALSNNEEISDSGQFAASHGLDHNEVVGVIKSLHGFRYVDAQDIKRETWVLTEEGKKYAAE
GSPEVQLFAAVPAEGSISKDELQKKLDPAVFDIGFKQAMKNKWLEMGGKPQVSRKVQHVEDEVKELLLAI
QEGKEVDDKDIDALKKRRKLITLETWKGYSIKKGPNYAPERKKAATDLTREMLQSGDWKDLEFKEYNFNA
LGAPPEGGHLHPLLKVRQQFRKIFLQMGFEEMPTNNFVESSFWNFDALFQPQQHPARDSHDTFFLKAPAT
TRQLPEDYVERVKTVHESGGYGSIGYGYDWKREEANKNLLRTHTTAVSSRMLYKLAQKGFKPKRYFSIDR
VFRNEAVDRTHLAEFHQVEGLVCDRGLTLGDLIGVLEDFFSRLGMTKLRFKPAYNPYTEPSMEIFSYHEG
LKKWVEVGNSGMFRPEMLLPMGLPEDVNVIAWGLSLERPTMILYGIDNIRDLFGHKVDLGLIKRNPICRL
GI
>gnl|CDD|215459 PLN02854, PLN02854, 3-ketoacyl-CoA synthase
MDKERLTAEMAFKDSSSAVIKIRQRLPDFLQSVKLKYVKLGYGYSCNPATILFFLIILPLTIATLVQITG
LEFDTVSELWSNQALHLDTATRLTGSAFLLFLLGLYWAKRSKPVYLVDFACYKPEDERKISVDSFLTMTE
ENGSFEDETVQFQRRISTRSGLGDETYLPRGITSRPPNLCMEEARAEAEAVMFGALDSLFSKTGVKPRDI
GILIVNCSLFNPTPSLSAMIVNHYKLRTDIKSYNLGGMGCSAGLISIDLANDLLKANPNSYAVVVSTENI
TLNWYFGNDRSMLLCNCIFRMGGAAVLLSNKARDRKRSKYQLVHTVRTHKGADDKNYNCVYQREDDKGTI
GVSLARELMAVAGDALKTNITTLGPLVLPLSEQFMFFVTLVRRKLLKAKVKPYIPDFKLAFEHFCIHAGG
RAVLDELQKNLQLSDWHMEPSRMTLHRFGNTSSSSLWYELAYTEAKGRVSAGDRVWQIAFGSGFKCNSAV
WKALREIPTGESTGNPWADSIDRYPVKVPVA
>gnl|CDD|215460 PLN02855, PLN02855, Bifunctional selenocysteine lyase/cysteine desulfurase
SSAPAASAASVSLGAETRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHAL
SAKATDAYELARKKVAAFINASTSREIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQ
LVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDA
CQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESMPPFLGGGEMISDVFLDHSTYAPPPS
RFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRIYGPKPSEGVGRAALCAF
NVEGIHPTDLSTFLDQQHGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHALKDTIAFFS
SFKG
>gnl|CDD|215461 PLN02856, PLN02856, fumarylacetoacetase
SPSPLKSFIDVAPDSDFPIQNLPYGVFSPESGATPRPGVAIGDYVLDLSALSEAGLFDGPLLSDSDCFSQ
PTLNKFMAMGRPAWKEARSTLQRLLSADEPALRDNSELRKKAFHPMSDVEMLLPAVIGDYTDFFSSREHA
TNVGTMFRGPENALNPNWLHLPIGYHGRASSVVPSGTDIRRPRGQLHPNDGSSRPYFGPSAKLDFELEMA
AFVGPGNELGKPIPVNEAKDHIFGLVLMNDWSARDIQKWEYVPLGPFLGKSFATTISPWIVTLDALEPFR
CDAPAQDPPPLPYLAEKNRKSYDISLEVAIKPAGQSKASVVCRSNFKHLYWTLAQQLAHHTVNGCNLRPG
DLLGSGTISGPEPGSLGCLLELTWAGSREVSLEGGTRRKFLEDGDEVVLSGWCKGDGYRVGFGTCSGKVL
PALP
>gnl|CDD|215462 PLN02857, PLN02857, octaprenyl-diphosphate synthase
MSMSCRNIDLGTSLVACGCSSNASSRRRVVRNGATPVCKSCSRSYASSLVTSRRDIGRCRVVSPSPETSL
VNGIGQGPTVALDLKAESKEPISLSELFEPVADDLQQLNDNLQSIVGAENPVLMSAAEQIFGAGGKRMRP
ALVFLVSRATAELAGLKELTTEHRRLAEITEMIHTASLIHDDVLDESDMRRGKETVHQLYGTRVAVLAGD
FMFAQSSWYLANLDNLEVIKLISQVIKDFASGEIKQASSLFDCDVTLDEYLLKSYYKTASLIAASTKSAA
IFSGVDSSVKEQMYEYGKNLGLAFQVVDDILDFTQSTEQLGKPAGSDLAKGNLTAPVIFALEKEPELREI
IESEFCEEGSLEEAIELVNEGGGIERAQELAKEKADLAIQNLECLPRGAFRSSLEDMVDYNLERIY
>gnl|CDD|215463 PLN02858, PLN02858, fructose-bisphosphate aldolase
AQSAGVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSH
PDQVDDVFFGDEGAAKGLQKGAVILIRSTILPLQLQKLEKKLTERKEQIFLVDAYVSKGMSDLLNGKLMI
IASGRSDAITRAQPFLSAMCQKLYTFEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYD
IISNAAGSSWIFKNHVPLLLKDDYIEGRFLNVLVQNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQG
DDTATSLAKVWEKVFGVNILEAANRELYKPEDLAKQITMQAKPVKRIGFIGLGAMGFGMASHLLKSNFSV
CGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAVSALPAGASIVLSSTV
SPGFVIQLERRLENEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLYVIKGGC
GAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSAL
DIFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYETLTGVKVEGRLPVLKKED
VLTSLPAEWPEDPIDDICHRLNMGNSKTLVVLDDDPTGTQTVHDVEVLTEWSVESISEQFRKKPACFFIL
TNSRSLSPEKASELIKDICRNLCAAAKSVGNVDYTIVLRGDSTLRGHFPEEADAAVSVLGEMDAWIICPF
FLQGGRYTINDIHYVADSDRLVPAGETEFAKDASFGYKSSNLREWVEEKTKGRISANSVQSISIQLLRKG
GPDAVCEHLCSLKKGSTCIVNAASERDMAVFAAGMIQAELKGKRFLCRTAASFVSARIGIIPKPPVLPKD
LESNKESSGGLIVVGSYVPKTTKQVEELKSQCGQSLRSIEVSVEKVAMKSSEVRDEEISRAVEMADAFLR
AGKDTLIMTSRELITGKTPSESLDINSKVSSALVEIVRRISTRPRYILAKGGITSSDLATKALEARRAKV
VGQALAGVPLWKLGPESRHPGVPYIVFPGNVGDSTALAEVVKSWARPARSSTKELLLNAEKGGYAVGAFN
VYNLEGIEAVVAAAEAEKSPAILQVHPGALKQGGIPLVSCCIAAAEQASVPITVHFDHGTSKHELLEALE
LGFDSVMVDGSHLSFTENISYTKSISSLAHSKGLMVEAELGRLSGTEDGLTVEEYEAKLTDVDQAKEFID
ETGIDALAVCIGNVHGKYPASGPNLRLDLLKELRALSSKKGVLLVLHGASGLPESLIKECIENGVRKFNV
NTEVRTAYMEALSSPKKTDLIDVMSAAKEAMKAVVAEKLRLFGSAGKA
>gnl|CDD|178450 PLN02859, PLN02859, glutamine-tRNA ligase
KDANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVH
RPTLLSYIVSSKIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKIL
EQRYRTNVGDLLGQVRKRLPWADPKIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVAA
APPSEEELNPYSIFPQPEENFKVHTEVFFSDGSVLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIG
HAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVEL
IRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNMYD
LIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLYQPYVWEY
SRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLIRMDRL
EHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFR
LKDSKDYYGLAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPL
KVEVRLFDKLFLSENPAELEDWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEK
LVFNRTVTLKDSYGKGGK
>gnl|CDD|215464 PLN02860, PLN02860, o-succinylbenzoate-CoA ligase
MANHSQAHICQCLTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLY
LEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEELQNDRLPSLMWQVFLESPSS
SVFIFLNSFLTTEMLKQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGY
GEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRK
SMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQTV
NQTKSSSVHQPQGVCVGKPAPHVELKIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGD
IGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWI
WSDNEKENAKKNLTLSSETLRHHCREKNLSRFKIPKLFVQWRKPFPLTTTGKIRRDEVRREVLSHLQSLP
SNL
>gnl|CDD|178452 PLN02861, PLN02861, long-chain-fatty-acid-CoA ligase
MAETYTVKVEESRPATGGKPSAGPVYRSIYAKDGLLDLPADIDSPWQFFSDAVKKYPNNQMLGRRQVTDS
KVGPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANA
VEFIINHAEVSIAFVQESKISSILSCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSL
DCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVATEEDSYFSYLPLAHVYD
QVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYN
YKLGNLRKGLKQEEASPRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTES
CGGCFTSIANVFSMVGTVGVPMTTIEARLESVPEMGYDALSDVPRGEICLRGNTLFSGYHKRQDLTEEVL
IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVV
VPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLIT
PTFKLKRPQLLKYYKDCIDQLYSEAKGGKA
>gnl|CDD|178453 PLN02862, PLN02862, 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
ASSAPYAAFVVLSATPSGRRRSKASRSSRATRSTITAAASTTAEVENALTPSKAAPTLPFRVGHGFDLHR
LEPGLPLIIGGIDIPHDRGCEAHSDGDVLLHCVVDAILGALGLPDIGQIFPDTDPKWKGADSSVFIKEAV
RLMHEAGYEIGNLDATLILQRPKLSPHKEAIRSNLSKLLGADPSVVNLKAKTHEKVDSLGENRSIAAHTV
VLLMKK
>gnl|CDD|215465 PLN02863, PLN02863, UDP-glucoronosyl/UDP-glucosyl transferase family protein
MTELNKPAGTHVLVFPFPAQGHMIPLLDLTHRLALRGLTITVLVTPKNLPFLNPLLSKHPSIETLVLPFP
SHPSIPSGVENVKDLPPSGFPLMIHALGELYAPLLSWFRSHPSPPVAIISDMFLGWTQNLACQLGIRRFV
FSPSGAMALSIMYSLWREMPTKINPDDQNEILSFSKIPNCPKYPWWQISSLYRSYVEGDPAWEFIKDSFR
ANIASWGLVVNSFTELEGIYLEHLKKELGHDRVWAVGPILPLSGEKSGLMERGGPSSVSVDDVMTWLDTC
EDHKVVYVCFGSQVVLTKEQMEALASGLEKSGVHFIWCVKEPVNEESDYSNIPSGFEDRVAGRGLVIRGW
APQVAILSHRAVGAFLTHCGWNSVLEGLVAGVPMLAWPMAADQFVNASLLVDELKVAVRVCEGADTVPDS
DELARVFMESVSENQVERERAKELRRAALDAIKERGSSVKDLDGFVKHVVELGLEEK
>gnl|CDD|178455 PLN02864, PLN02864, enoyl-CoA hydratase
RMPPISPFDPDLVLAHKFPEVTYSYTERDVALYALGVGACGRDAVDEDELKYVYHRDGQQFIKVLPTFAS
LFNLGSLDGFGLDLPGLNYDPSLLLHGQQYIEIYKPIPSSASVRNKVSIAGLHDKGKAAILELETLSYEK
DSGELLCMNRSTIFLRGAGGFSNSSQPFSYSNYPTNQVSAVKIPKSQPDAVFEDQTQPSQALLYRLSGDY
NPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCFCNGDPTAVKTISGRFLLHVYPGETLVTEMWLEG
LRVIYQTKVKERNKAVLSGYVDLRHLTSSL
>gnl|CDD|215466 PLN02865, PLN02865, galactokinase
TCLGSWPSANELDEIRERVAAMSGRNSGEVRVVVSPYRICPLGAHIDHQGGTVSAMTINKGILLGFVPSG
DPEVLLRSAQFEGEVRFRVDEIQHPIANVSSDSKEESNWGDYARGAVYALQSRGHALSQGITGYISGSEG
LDSSGLSSSAAVGVAYLLALENANNLTVSPEDNIELDRLIENEYLGLRNGILDQSAILLSRYGCLTFMDC
KTLDHKLVSLQFQQPGGEKPFKILLAFSGLRHALTNKPGYNLRVSECQEAARFLLEASGNDELEPLLCNV
EPEVYEAHKCKLEAVLARRAEHYFSENMRVIKGVEAWASGNLEEFGKLISASGLSSIENYECGCEPLIQL
YEILLKAPGVYGARFSGAGFRGCCVAFVDAEMAEEAASFVRDEYEKAQPELASNINGDKPVLICEAGDCA
RVL
>gnl|CDD|215467 PLN02866, PLN02866, phospholipase D
SLPESCRIFDELPKATIVSVSRPDAGDISPVLLSYTIELQYKQFKWTLYKKASQVLYLHFALKKRAFIEE
LHEKQEQVKEWLQNLGIGDHPAVVQDDDEPDDGTVPLHHDESAKNRDVPSSAALPVIRPALGRQQSISDR
AKVAMQEYLNHFLGNLDIVNSREVCKFLEVSKLSFSPEYGPKLKEGYVMVKHLPKIPKSDDSRGCFPCCC
FSCCNDNWQKVWAVLKPGFLALLEDPFDAKPLDIIVFDVLPASNGNGEGQISLAKEIKERNPLRFGFKVT
CGNRSIRLRTKSSAKVKDWVAAINDAGLRPPEGWCHPHRFGSFAPPRGLTEDGSQAQWFIDGHAAFEAIA
SAIENAKSEIFITGWWLCPELYLRRPFHDHESSRLDSLLEAKAKQGVQIYILLYKEVALALKINSVYSKR
RLLGIHENVKVLRYPDHFSSGVYLWSHHEKLVIVDYQICFIGGLDLCFGRYDTPEHRVGDCPPVIWPGKD
YYNPRESEPNSWEDTMKDELDRRKYPRMPWHDVHCALWGPPCRDVARHFVQRWNYAKRNKAPNEQAIPLL
MPHHHMVIPHYLGGSEEEEIESKNQEDNQKGIARQDSFSSRSSLQDIPLLLPQEADATDGSGGGHKLNGM
NSTNGSLSFSFRKSKIEPVLPDTPMKGFVDDLGFLDLSVKMSSAERGSKESDSEWWETQERGDQVGSADE
VGQVGPRVSCRCQVIRSVSQWSAGTSQVEESIHAAYCSLIEKAEHFIYIENQFFISGLSGDDTIQNRVLE
ALYRRILRAHKEKKCFRVIIVIPLLPGFQGGVDDGGAASVRAIMHWQYRTICRGKNSILHNLYDLLGPKT
HDYISFYGLRAYGRLFEGGPLATSQIYVHSKIMIVDDRAALIGSANINDRSLLGSRDSEIGVVIEDKEFV
DSSMNGKPWKAGKFAHSLRLSLWSEHLGLRAGEIDKIIDPVCDTTYKDLWMATAKTNTDIYQDVFSCIPN
DLIHSRAALRQSMASRKEKLGHTTIDLGIAPEKLESYENGDIKSSDPMERLKSVRGHLVSFPLDFMCQED
LRPVFNESEYYASPQVFH
>gnl|CDD|178458 PLN02867, PLN02867, Probable galacturonosyltransferase
MKFYISTTGIKKVTISNPGSGKGSGGCAAAAAAAAARRFSGRTLLPVLLLLAIVLPFLFVRIAFLVLESA
SACNSPLDCIGLRLFGGSDTSLKLREELTRALVEAKEQDDGGRGTKGSTESFNDLVKEMTSNRQDIKAFA
FRTKAMLLKMERKVQSARQRESIYWHLASHGIPKSLHCLCLKLAEEYAVNAMARSRLPPPESVSRLTDPS
FHHVVLLTDNVLAASVVISSTVQNAANPEKLVFHIVTDKKTYTPMHAWFAINSIKSAVVEVKGLHQYDWS
QEVNVGVKEMLEIHRLIWSHYYQNLKESDFQFEGTHKRSLEALSPSCLSLLNHLRIYIPELFPDLNKIVF
LDDDVVVQHDLSSLWELDLNGKVVGAVVDSWCGDNCCPGRKYKDYLNFSHPLISSNLDQERCAWLYGMNV
FDLKAWRRTNITEAYHKWLKLSLNSGLQLWQPGALPPALLAFKGHVHPIDPSWHVAGLGSRPPEVPREIL
ESAAVLHFSGPAKPWLEIGFPEVRSLWYRHVNFSDKFIRKCRIMG
>gnl|CDD|178459 PLN02868, PLN02868, acyl-CoA thioesterase family protein
MNTESVVEFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGPAEEES
RPEFLLKRYDYFGYGLSGSVHSADVVAVSELTCLVLPHEHCHLLSPKSIWDSDKTPKDCSLVERILHLEP
LEVDIFRGITLPDAPTFGKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDG
HNFATRRVDAIQKGKVIFTLFASFQKEEQGFEHQESTMPHVPPPETLLSREELRERRLTDPRLPRSYRNK
VAAKPFVPWPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHRT
KGLKFAALSLDHSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL
>gnl|CDD|166510 PLN02869, PLN02869, fatty aldehyde decarbonylase
MASKPGILTDWPWKPLGSFKYVVLAPWVIHSIYSFVVKDEKERDLSYFLIFPFLLWRMLHNQLWISLSRY
RTAKGNNRIVDKGIEFEQVDRERNWDDQILFNGILFYVGYMILPGASHMPLWRTDGVLITILLHMGPVEF
LYYWLHRALHHHYLYSRYHSHHHSSIVTEPITSVIHPFAEHIAYFLLFAIPLLTTIFTGTASIAAFFGYI
SYIDFMNNMGHCNFELIPKWLFSIFPPLKYLMYTPSYHSLHHTQFRTNYSLFMPIYDYIYGTMDKSSDTL
YEKSLKRPEEIPDVVHLTHLTTPDSIYHLRLGFASLASKPYISKWYLRLMWPVTSWSMMLTWIYGRTFVL
ERNRFNKLNLQTWVIPKYKIQYLLKWQNESINSLIEEAILEADKRGVKVLSLGLLNQGEELNRYGELYIH
RNPKLKIKVVDGSSLAVAVVLNSIPKGTTQVLFRGNLSKVAYFIASALCQRGIQVATFREDEYEKLNKKL
PNTECGSKLLLSKNYSEKIWLVGDGLTEEEQKKASKGTLFIPFSQFPPKRLRKDCFYHTTPAMMSPKSFE
NVDSCENWLPRRAMSAWRVAGILHALEGWNVHECGYTMFDIEKIWEASLQHGFRPLLIPS
>gnl|CDD|215468 PLN02870, PLN02870, Probable galacturonosyltransferase
MQLHISPSMRSITISSSNGFIDLMKIKVAARHISYRTLFHTILILAFLLPFVFILTAVVTLEGVNKCSSF
DCLGRRLGPRLLGRVDDSERLVRDFYKILNEVNTEEIPDGLKLPDSFSQLVSDMKNNHYDAKTFAFVLRA
MMEKFERELRESKFAELMNKHFAASSIPKGIHCLSLRLTDEYSSNAHARKQLPSPELLPVLSDNSYHHFV
LSTDNILAASVVVSSTVQSSLKPEKIVFHVITDKKTYAGMHSWFALNSVSPAIVEVKGVHQFDWLTRENV
PVLEAVESHNGIRNYYHGNHIAGANLSETTPRTFASKLQARSPKYISLLNHLRIYLPELFPNLDKVVFLD
DDVVIQRDLSPLWDIDLGGKVNGAVETCRGEDEWVMSKRFRNYFNFSHPLIAKNLDPEECAWAYGMNIFD
LRAWRKTNIRETYHSWLKENLKSNLTMWKLGTLPPALIAFKGHVHPIDPSWHMLGLGYQSKTNIESVKKA
AVIHYNGQSKPWLEIGFEHLRPFWTKYVNYSNDFIRNCHILES
>gnl|CDD|215469 PLN02871, PLN02871, UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
SSTTSSARSRVKLRSGDAGRFSARSSSYRNAAVLVSVRRVASSEAPPPLLDTDSRSRPRRIALFVEPSPF
SYVSGYKNRFQNFIRYLREMGDEVLVVTTDEGVPQEFHGAKVIGSWSFPCPFYQKVPLSLALSPRIISEV
ARFKPDLIHASSPGIMVFGALFYAKLLCVPLVMSYHTHVPVYIPRYTFSWLVKPMWDIIRFLHRAADLTL
VTSPALGKELEAAGVTAANRIRVWNKGVDSESFHPRFRSEEMRARLSGGEPEKPLIVYVGRLGAEKNLDF
LKRVMERLPGARLAFVGDGPYREELEKMFAGTPTVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLE
AMASGVPVVAARAGGIPDIIPPDQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEKWDW
RAATRKLRNEQYSAAIWFWRKKRAQLLGPVQWLPAQLFPAPEVNS
>gnl|CDD|215470 PLN02872, PLN02872, triacylglycerol lipase
VAVLISLFISTSAGGVLTGQSNLLRRSPVESLCAQLIHPAGYSCTEHTIQTKDGYLLALQRVSSRNPRLG
SQRGPPVLLQHGLFMAGDAWFLNSPEQSLGFILADHGFDVWVGNVRGTRWSYGHVTLSEKDKEFWDWSWQ
ELALYDLAEMIHYVYSITNSKIFIVGHSQGTIMSLAALTQPNVVEMVEAAALLCPISYLDHVTAPLVLRM
VFMHLDQMVVAMGIHQLNFRSDVLVKLLDSICEGHMDCNDLLTSITGTNCCFNASRIDYYLEYEPHPSSV
KNLRHLFQMIRKGTFAHYDYGIFKNLKLYGQVNPPAFDLSLIPKSLPLWMGYGGTDGLADVTDVEHTLAE
LPSKPELLYLENYGHIDFLLSTSAKEDVYNHMIQFFRSLGKSSSS
>gnl|CDD|215471 PLN02873, PLN02873, coproporphyrinogen-III oxidase
PGGGGGISRVLQDGNVFEKAGVNVSVVYGTMPPEAYRAATGRGSRKGGDPAGGVPFFAAGLSSVMHPKNP
MAPTFHFNYRYFETDAPKDVPGAPRQWWFGGGTDLTPSYLFEEDVKHFHGTYKDVCDKHDPEFYPRFKKW
CDDYFYIKHRGERRGLGGIFFDDLNDRDQEDLLAFATDVANSVVPAYLPIVEKRKDDPFTEEQKAWQQLR
RGRYVEFNLVYDRGTTFGLKTGGRIESILVSLPPTARWEYDHQPEEGSEEAELLDALRNPREWV
>gnl|CDD|178462 PLN02874, PLN02874, 3-hydroxyisobutyryl-CoA hydrolase-like protein
MAQQVQNPAEEVVLGEEKGRVRVITLNRPRQLNVISLSVVSLLAEFLEQWEKDDSVELIIIKGAGRAFSA
GGDLKMFYDGRESDDSCLEVVYRMYWLCYHIHTYKKTQVALVHGLVMGGGAGLMVPMKFRVVTEKTVFAT
PEASVGFHTDCGFSYILSRLPGHLGEYLALTGARLNGKEMVACGLATHFVPSEKLPELEKRLLNLNSGDE
SAVQEAIEEFSKDVQADEDSILNKQSWINECFSKDTVEEIIKAFESEASKTGNEWIKETLKGLRRSSPTG
LKITLRSIREGRKQSLAECLKKEFRLTMNILRSTVSDDVYEGIRALVIDKDNAPKWNPSTLDEVTDEKVD
LVFQPFKAREELQLPEEEENRWSGKYEHS
>gnl|CDD|215472 PLN02875, PLN02875, 4-hydroxyphenylpyruvate dioxygenase
FHHVEFWCGDATNTARRFSWGLGMPLVAKSDLTTGNTTYASYLLRSGDLVFLFTAPYSPKIGAGDDDPAS
TAPHPSFSSDAARRFFAKHGLAVRAVGVLVEDAEEAFRTSVAHGARPVLEPTELGDEASGGKAVIAEVEL
YGDVVLRYVSYKGFDGAKFLPGYEPVESSSSFPLDYGLRRLDHAVGNVPNLLPAVNYIAGFTGFHEFAEF
TAEDVGTVDSGLNSMVLASNNEMVLLPLNEPTFGTKRKSQIQTYLEHNEGPGLQHLALKSDDIFGTLREM
RARSHIGGFEFMPPPPPTYYKNLKKRVGDVLTEEQIKECEELGILVDKDDQGVLLQIFTKPVGDRPTLFL
EIIQRIGCMEKDEEGKEYEQAGGCGGFGKGNFSELFKSIEEYEKTLDA
>gnl|CDD|215473 PLN02876, PLN02876, acyl-CoA dehydrogenase
MAKRTSDLLVPVQSAHRFDEDALLRYAAANVAGFPVPPSTFKVSQFGHGQSNPTFLLEVGNGGSVKRYVL
RKKPPGKLLQSAHAVEREYQVLRALGEHTDVPVPKVYCLCTDASVIGTAFYIMEYLEGRIFVDPKLPGVA
PERRRAIYRATAKVLAALHSADVDAIGLGKYGRRDNYCKRQVERWAKQYLASTGEGKPPRNPKMLELIDW
LRENIPAEDSTGAGTGIVHGDFRIDNLVFHPTEDRVIGILDWELSTLGNQMCDVAYSCLPYIVDINLDNQ
QVGKGFEFTGIPEGIPSLPEYLAEYCSASGKPWPAANWKFYVAFSLFRGASIYAGVYSRWLMGNASGGER
ARNAGKQANFLVDSALDYIARKNVLPEHPPSGQFGREPEYSSLSKESGRFVPSEKVLELRKKLIKFMEDH
IYPMENEFYKLAQSSSRWTVHPEEERLKELAKKEGLWNLWIPLDSAARARKLLFEDNKHMVSGDSADQLL
GAGLSNLEYGYLCEIMGRSVWAPQVFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQ
VASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVMGKTDFNAPKHKQQSMILVDIQTPGVQI
KRPLLVFGFDDAPHGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQ
RALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIIAMAKVAAPNMALKVL
DMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKLELQRAKL
>gnl|CDD|215474 PLN02877, PLN02877, alpha-amylase/limit dextrinase
MALLLTPSPAVHLAPAPCVARPRASSAAFVLRSRWLRSRGATSISFVAHRGRNFRVRIPSATSLAMATRP
SSASSFFTLELSVPTSLFQDDLLYSRAYWVTESIIAWNVDVGDGSCFLYASKTAGLSVSDDGVEGYDLVV
KLEEDSGGLPPNVIEKFPHIRGYRAFKVPSTVDVKDLLKCQLAVAAFDADGKCTDATGLQLPGVLDDLFA
YDGPLGAHFSKDAVSLYLWAPTAQAVSLCLYDDPRGKEPLEIVQLKESNGVWSVEGPKSWEGCYYVYEVS
VYHPSTGKVETCYANDPYARGLSADGRRTLLVDLDSDDLKPEGWDNLAKEKPCLLSFSDISIYELHVRDF
SANDETVHPDFRGGYLAFTSQDSAGVLHLKKLADAGLTHVHLLPTFQFGSVDDEKENWKCVDPKELEKLP
PDSEEQQAAITAIQDDDGYNWGYNPVLWGVPKGSYASNPDGPCRIIEFRKMVQALNRIGLRVVLDVVYNH
LHSSGPFDENSVLDKIVPGYYLRRNSDGFIENSTCVNNTASEHYMVDRLIVDDLLNWAVNYKVDGFRFDL
MGHLMKRTMVRAKDALQSLTLERDGVDGSSIYLYGEGWDFGEVAKNGRGVNASQFNLAGTGIGSFNDRIR
DAMLGGSPFGHPLQQGFVTGLFLQPNGHDQGGEDVQELMLATAKDHIQVGMAGNLKDYVLTNREGKEVKG
SEVLTHDGKPVAYASSPTETINYVSAHDNETLFDIISLKTPMEISVDERCRINHLATSIIALSQGIPFFH
AGDEILRSKSLDRDSYNSGDWFNRLDFSYDSNNWGVGLPPKEKNEDNWPLIKPRLADPSFKPSKEHILAA
LDNFLDLLRIRYSSPLFRLRTANAIQERVRFHNTGPSSIPGVIVMSIEDGHEGVPGLSQLDPIYSRIVVI
FNARPTEVSFESPALKGRTLELHPVQVMSADEVVKKSVYEASSGVFTVPPRTTAVFVEHR
>gnl|CDD|178466 PLN02878, PLN02878, homogentisate phytyltransferase
LGITSVSLLAVESLSDFSPLFFTGLLEALVPALLMNIYIVGLNQLYDIEIDKVNKPYLPLASGEFSVATG
VAIVTSFAIMSFGMGWIVGSWPLFWALFVSFVLGTAYSINLPLLRWKRSAVAAASCILAVRAVVVQLAFF
LHMQTHVLGRPAVFTRPLIFATAFMCFFSVVIALFKDIPDVEGDRIFGIRSFSVRLGQKRVFWLCVNLLE
MAYAAAILVGASSSFLWSKIITVLGHGILASILWQRAQSVDLSSKAAITSFYMFIWKLFYAEYFLIPLVR
>gnl|CDD|178467 PLN02879, PLN02879, L-ascorbate peroxidase
MVKKSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHD
ANNGLDIAVRLLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVD
HLRDVFGRMGLNDKDIVALSGGHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKA
LLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLSELGFADKE
>gnl|CDD|215475 PLN02880, PLN02880, tyrosine decarboxylase
GGGEEWLRPMDAEQLRECGHRMVDFIADYYKSIENFPVLSQVQPGYLRELLPDSAPNQPETLDQVLDDVQ
AKILPGVTHWQSPNYFAYYPSNSSVAGFLGEMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLLNLPEQ
FLSTGNGGGVIQGTASEAVLVVLLAARDRVLRKVGKNALEKLVVYASDQTHSALQKACQIAGIHPENCRL
LKTDSSTNYALAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAG
SACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSLSTNPEFLKNKASQANSVVDY
KDWQIPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVVTPRIFSLVCFRLVPP
KNNEDNGNKLNHDLLDAVNSSGKIFISHTVLSGKYVLRFAVGAPLTEERHVTAAWKVLQDEASKLLGKSS
>gnl|CDD|215476 PLN02881, PLN02881, tetrahydrofolylpolyglutamate synthase
MAGMATEDDAPTSDSYEEALDALSSLITKKSRADPSNPGDQFDLLFDYLKILELEEAISRLKVIHVAGTK
GKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRYFWWCWDRLKEKTTEDLPMPA
YFRFLTLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQKPVVCGITSLGYDHMEILGDTLGKIAGEKAGI
FKPGVPAFTVPQPDEAMRVLEERASELGVPLQVVEPLDSYGLSGLKLGLAGEHQYLNAGLAVALCSTWLQ
RTGHEEFEALLQAGTLPEQFIKGLSTASLQGRAQVVPDSYINSEDSGDLVFYLDGAHSPESMEACARWFS
SAIKGDEQSPGSGYGPHGGGGKSEDTESNKISEQILLFNCMSVRDPQLLLPPLANTCASNGVPFKKALFV
PNISVYNKVGSGLPVDDPQVDLSWQFTLQRVWESLIRGKAGAPADAVCEESASSGLNDGKSDENSAVFPS
LPLAIKWLRDCARENPSLRFQVLVTGSLHLVGDVLRLLKK
>gnl|CDD|215477 PLN02882, PLN02882, aminoacyl-tRNA ligase
EVCEGKDFSFPKQEEKILSLWSEIDAFKTQLKRTEGLPEYIFYDGPPFATGLPHYGHILAGTIKDIVTRY
QSMTGHHVTRRFGWDCHGLPVEYEIDKKLGIKRRDDVLKMGIDKYNEECRSIVTRYSKEWEKTVTRTGRW
IDFENDYKTMDPKFMESVWWVFKQLFEKGLVYKGFKVMPYSTACKTPLSNFEAGLNYKDVSDPAVMVSFP
IVGDPDNASFVAWTTTPWTLPSNLALCVNPNFTYVKVRNKYTGKVYIVAESRLSALPTAKPKSKKGSKPE
NAAEGYEVLAKVPGSSLVGKKYEPLFDYFSEFSDTAFRVVADDYVTDDSGTGVVHCAPAFGEDDYRVCLA
NGIIEKGGNLPVPVDDDGCFTEKVTDFSGRYVKDADKDIIAAIKAKGRLVKSGSITHSYPFCWRSDTPLI
YRAVPSWFVKVEEIKDRLLENNKQTYWVPDYVKEKRFHNWLENARDWAVSRSRFWGTPLPIWISDDGEEV
VVIGSIAELEKLSGVKVTDLHRHFIDHITIPSSRGPEFGVLRRVDDVFDCWFESGSMPYAYIHYPFENKE
LFEKNFPADFVAEGLDQTRGWFYTLMVLSTALFDKPAFKNLICNGLVLAEDGKKMSKSLKNYPDPNEVID
KYGADALRLYLINSPVVRAEPLRFKEEGVFGVVKDVFLPWYNAYRFLVQNAKRLEVEGGAPFVPLDLAKL
QNSANVLDRWINSATQSLVKFVREEMGAYRLYTVVPYLVKFIDNLTNIYVRFNRKRLKGRTGEEDCRTAL
STLYNVLLTSCKVMAPFTPFFTEVLYQNLRKVLPGSEESIHYCSFPQVDEGELDERIEQSVSRMQTVIEL
ARNIRERHNKPLKTPLKEMVVVHPDAEFLDDITGKLKEYVLEELNVRSLVPCNDPLKYASLRAEPNFSVL
GKRLGKSMGLVAKEVKAMSQDDILEFEKAGEVTIAGHTLKAGDIKVVRDFKRPEGVSKEDIDAAGDGDVL
VILDLRVDESLLEAGVAREVVNRIQKLRKKAGLEPTDKVEVFFESLDEVDESALSQVLKSQAQYIRESLG
SPLLPSSMMPSHAVVIAEESFHGVSGLSFKISLARPALAFNEDALLALCSGDEELAEGVEAVLLSRDHSN
LKSEFQAGKIKLSCRENGPEVDVVLGKHFHLSVSDSVLS
>gnl|CDD|178471 PLN02883, PLN02883, Branched-chain amino acid aminotransferase
MALRRCLPQSSTTSSYLSKIWGFRMHGTKAAASVVEEHVSGAEREDEEYADVDWDKLGFSLVRTDFMFAT
KSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRMKIGAERMCMH
SPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGTAA
LNLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNI
IVTPATSGTILGGITRKSIIEIALDLGYKVEERRVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEY
KVGDGIVTQQLRSILLGIQTGSIQDTKDWVLQIA
>gnl|CDD|178472 PLN02884, PLN02884, 6-phosphofructokinase
GYVNNDDRVLLKVIKYSSPTSAGAECIDPDCSWVEQWVHRAGPRKKIYFEPEEVKAAIVTCGGLCPGLND
VIRQIVFTLEIYGVKNIVGIPFGYRGFFEKGLSEMPLSRKVVQNIHLSGGSLLGVSRGGAKTSDIVDSIE
ARGINMLFVLGGNGTHAGANAIHNECRKRKMKVSVVGVPKTIDNDILLMDKTFGFDTAVEEAQRAINSAY
IEAHSAYHGIGLVKLMGRSSGFIAMHASLASGQVDICLIPEVPFTLDGPNGVLRHLEHLIETKGSAVVCV
AEGAGQDLLQKTNATDASGNPVLGDIGVHLQQEIKKHFKDIGVPADVKYIDPTYMIRACRANASDAILCT
VLGQNAVHGAFAGFSGITVGICNTHYVYLPIPEVIAYPRRVDPNSRMWHRCLTSTGQPDFH
>gnl|CDD|178473 PLN02885, PLN02885, nicotinate phosphoribosyltransferase
VIPRPTNPMVTPLLTDLYQFTMAYAYWKAGKHLDRAVFDLFFRKNPFGGEYTVFAGLEECLRFIANFKFT
DDDIDFLRSVMPSGCEDAFFDYLRGLDCSDVEVYAIPEGSVVFPRVPLMRIEGPLAVVQLLETTFLTLVN
YASLVATNAARHRLVAGKSKVLLEFGLRRAQGPDGGISASKYCYLGGFDATSNVEAGRLFGIPVRGTHSH
AFVSSYMGLDEIVDKTLRSADGSSVCEDFVSLVQEWLSKLQESSSLRGVFSETNQSELAAFTSYALAFPN
SFLALVDTYDVMKSGIPNFCAVALALNDLGYKAVGIRLDSGDLAYLSLEARKFFRTIEEELGVPGFGKMS
ITASNDINEETLDALNKQGHEIDAFGIGTHLVTCYAQPALGCVYKLVEINGQPRIKLSEDVEKVTIPCKK
RCYRLYGKEGYPLVDLMTGENEPPPKVGERILCRHPFNESKRAYVVPQRVEELLKCYWDGSSGKPREELP
SLKEIRERCMKQLERMRPDHMRRLNPTPYKVSVSAKLYDFIHFLWLNEAPVGELQ
>gnl|CDD|215478 PLN02886, PLN02886, aminoacyl-tRNA ligase
SSLGSLGRLLSKPGPLSGSASSASCCSAATAATAPEKEAPPKVARKKRVVSGVQPTGSIHLGNYLGAIKN
WVALQETYDTFFCVVDLHAITLPHDPRELGKATRSTAAIYLACGIDPSKASVFVQSHVPAHAELMWLLSC
STPIGWLNKMIQFKEKSRKAGDENVGVGLLTYPVLMASDILLYQADLVPVGEDQKQHLELTRDIAERVNN
LYGGRKWKKLGGRGGSVFKVPEALIPPAGARVMSLTDGTSKMSKSAPSDQSRINLLDPPDVIANKIKRCK
TDSFPGLEFDNPERPECNNLLSIYQLVTGKTKEEVLAECGDMRWGDFKPLLTDALIEHLSPIQVRYEEIM
SDPSYLDSVLKEGADAAAEIADRTLANVYQAMGFVQRRR
>gnl|CDD|215479 PLN02887, PLN02887, hydrolase family protein
MLPMLSRVSLPLRLPRLFPAAAREMPPAARLLLQPSSLSFSPKTSNFNRLDVTSTEFSSFRKGFHAFRST
KPRGRVWAAHRGYRKIRRRAPPPKKEQELELSVSICIEEDLPDDPEILNIAELLRLNVPMAMKLAFDGLK
DSKYKTRDTDISDVGGYDSVELSVMLCNDDFIRKLNKEWRGEDHATDVLSMSQHVPGLKLPVLMLGDIVI
SVETAARQAEERGHTLLDEIRILVVHGLLHLLGFDHEISNEAEAEMEKEEELLLKSLGWKGKGLIQSAYD
AEKTQTDQLEKSDDRKKEGSLRFYKPKFSYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGK
ARPAVIDILKMVDLAGKDGIISESSPGVFLQGLLVYGRQGREIYRSNLDQEVCREACLYSLEHKIPLIAF
SQDRCLTLFDHPLVDSLHTIYHEPKAEIMSSVDQLLAAADIQKVIFLDTAEGVSSVLRPYWSEATGDRAN
VVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLASLGVALSNGAEKTKAVAD
VIGVSNDEDGVADAIYRYAF
>gnl|CDD|215480 PLN02888, PLN02888, enoyl-CoA hydratase
TMTQTVSENLILVPKSRNGIATITINRPKALNALTRPMMVELAAAFKRLDEDDSVKVIILTGSGRAFCSG
VDLTAAEEVFKGDVKDVETDPVAQMERCRKPIIGAINGFAITAGFEIALACDILVASRGAKFIDTHAKFG
IFPSWGLSQKLSRIIGANRAREVSLTAMPLTAETAERWGLVNHVVEESELLKKAREVAEAIIKNNQGMVL
RYKSVINDGLKLDLGHALQLEKERAHDYYNGMTKEQFQKMQEFIAGRSSKKPSKL
>gnl|CDD|215481 PLN02889, PLN02889, oxo-acid-lyase/anthranilate synthase
MKFTFCSTSSELKFPSFEGLRCSDLNSVFSKGFLKVKKDNVKVSNCQARKVFVSSHLVPGHLEGLSMGKK
QLEEPSQKLEFVRTLLIDNYDSYTYNIYQELSIVNGVPPVVVRNDEWTWEEVYHYLYEEKAFDNIVISPG
PGSPTCPADIGICLRLLLECRDIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIPS
GRNSGFKVVRYHSLVIDAESLPKELVPIAWTSSSDTLSFLESQKSGLVPDAYESQIGQSGSSDPFSSKLK
NGTSWPSSHSERMQNGKILMGIMHSTRPHYGLQFHPESIATCYGRQIFKNFREITQDYWLRLRSTSLRRR
NSNLTANMQVPDASQLFKVPRRGQLGNGEDALGNRELSRRAQLRGSVDVFSLLNLSEPSSGVKFLKLKWR
KFNKLAAQVGGARNIFCELFGKNKAENTFWLDSSSTEKKRGRFSFMGGKGGSLWKQMTFRLSHQSDMDSK
GGGHLSIEDSQGSIESTFLEKGFLDFLNKELLSIRYDEKDFEGLPFDFHGGYVGYIGYDLKVECGMASNR
HKSTTPDACFFFADNVVVIDHHYDDVYILSLHEGSTATTQWLDDTEQKLLGLKASATRKLEVQTSPTATF
SPSKAGFLADKSREQYIKDVQKCLKYIKDGESYELCLTTQMRKRIGEIDSLGLYLHLREKNPAPYAAWLN
FSNENLCICSSSPERFLKLDRNGMLEAKPIKGTIARGSTPEEDEQLKLQLQYSEKDQAENLMIVDLLRND
LGRVCEPGSVHVPNLMDVESYTTVHTMVSTIRGKKRSNMSPVDCVRAAFPGGSMTGAPKLRSMELLDSLE
SSSRGIYSGSIGFFSYNQTFDLNIVIRTVVIHEGEASIGAGGAIVALSNPEDEYEEMILKTRAPANAVIE
FQKDQRSN
>gnl|CDD|178478 PLN02890, PLN02890, geranyl diphosphate synthase
MLLSRRVARISATSGGGRGAYGCSQSLASSRAALLGRHGHPLSQSTSKVVGCRGTYSVSSRWLHGFQYQV
RHQSSSLVEEQLDPFSLVADELSLLANKLRSMVVAEVPKLASAAEYFFKVGVEGKRFRPTVLLLMATALN
VPLPESTEGGVLDIVASELRTRQQNIAEITEMIHVASLLHDDVLDDADTRRGVGSLNVVMGNKLSVLAGD
FLLSRACVALAALKNTEVVSLLATAVEHLVTGETMQITSSREQRRSMDYYMQKTYYKTASLISNSCKAVA
ILAGQTAEVAVLAFEYGRNLGLAFQLIDDVLDFTGTSASLGKGSLSDIRHGVITAPILFAMEEFPQLREV
VDRGFDNPANVDIALEYLGKSRGIQRTRELAREHANLAAAAIESLPETDDEDVLTSRRALIDLTERVITR
NK
>gnl|CDD|178479 PLN02891, PLN02891, IMP cyclohydrolase
MAASATAARAPAQPQSSPSSGKKQALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVE
ELTNFPEMLDGRVKTLHPAVHGGILARRDQEHHMEALNEHGIGTIDVVVVNLYPFYDTVTSGGISFEDGV
ENIDIGGPAMIRAAAKNHKDVLVVVDPADYPALLEYLKGKQDDQQDFRRKLAWKAFQHVASYDSAVSEWL
WKQINGGGKFPPSLTVPLTLKSSLRYGENPHQKAAFYVDKSLSEVNAGGIATAIQHHGKEMSYNNYLDAD
AAWNCVSEFSNPTCVVVKHTNPCGVASRGDILEAYRLAVRADPVSAFGGIVAFNCEVDEDLAREIREFRS
PTDGETRMFYEIVVAPKYTEKGLEVLKGKSKTLRILEAKPRKKGRLSLRQVGGGWLAQDSDDLTPEDITF
TVVSEKVPTESELEDAKFAWLCVKHVKSNAIVVAKNNRMLGMGSGQPNRVESLRIALEKAGEEAKGAALA
SDAFFPFAWNDAVEEACQAGVKVIAEPGGSMRDQDAIDCCNKYGVALLFTGVRHFRH
>gnl|CDD|215482 PLN02892, PLN02892, isocitrate lyase
MAASFSVPSMIMEEEGRFEAEVAEVEAWWRSERFKLTRRPYSARDVAALRGTLKQSYASNEMAKKLWRTL
KTHQANGTASRTFGALDPVQVAQMAKHLDTIYVSGWQCSSTATSTNEPGPDLADYPMDTVPNKVEHLFFA
QLYHDRKQREARMSMSREERARTPYVDYLKPIIADGDTGFGGTTATVKLCKLFVERGAAGVHIEDQSSVT
KKCGHMGGKVLVATSEHINRLVAARLQFDVMGVETVLVARTDAVAATLIQSNIDARDHQFILGATNPALR
GKPLATLLAEAMAAGKSGAELQAIEDEWLAQAQLMTFSEAVADAIKSMNISENEKRRRLNEWMASVPKCL
SNEQARRIAAKLGVANVFWDWDLPRTREGFYRFRGSVKACIVRGRAFAPYADLIWMETASPDLAEATKFA
EGVKAKHPEIMLAYNLSPSFNWDASGMTDEQMAEFIPRLARLGYCWQFITLAGFHANALVVDTFARDYAR
RGMLAYVERIQRQERTNGVETLAHQKWSGANYYDRYLKTVQGGISSTAAMGKGVTEEQFKETWTRPGAEG
GSEVVAKSRM
>gnl|CDD|215483 PLN02893, PLN02893, Cellulose synthase-like protein
METHTTASTGAPPLHTCHPMRRTIANRVFAVVYSCAILALLYHHVIALLHSTTTLITLLLLLADIVLAFM
WATTQAFRMCPVHRRVFIEHLEHYAKESDYPGLDVFICTADPYKEPPMGVVNTALSVMAYDYPTEKLSVY
VSDDGGSKLTLFAFMEAAKFATHWLPFCKKNKIVERCPEAYFSSNSHSWSPETEQIKMMYESMKVRVENV
VERGKVSTDYITCDQEREAFSRWTDKFTRQDHPTVIQVLLESGKDKDITGHTMPNLIYVSREKSKNSPHH
FKAGALNTLLRVSATMTNAPIILTLDCDMYSNDPQTPLRALCYLLDPSMDPKLGYVQFPQIFHGINKNDI
YAGELKRLFQINMIGMDGLAGPNYVGTGCFFRRRVFYGGPSSLILPEIPELNPDHLVDKSIKSQEVLALA
HHVAGCNYENQTNWGSKMGFRYGSLVEDYYTGYRLQCEGWKSIFCNPKRPAFLGDSPINLHDVLNQQKRW
SVGLLEVAFSKYSPITFGVKSIGLLMGLGYAHYAFWPIWSIPITIYAFLPQLALLNGVSIFPKASDPWFF
LYIFLFLGAYGQDLLDFLLSGGTIQRWWNDQRMWMIRGLSSFLFGLVEFLLKTLGISTFGFNVTSKVVDE
EQSKRYEQGIFEFGVSSPMFLPLTTAAIINLVSFLWGIAQIFRQRNLEGLFLQMFLAGFAVVNCWPIYEA
MVLRTDDGKLPVKITLISIVLAWALYLASSFAFK
>gnl|CDD|215484 PLN02894, PLN02894, hydrolase, alpha/beta fold family protein
MKVQLRGHEIPGHGAASSAAASAAASAETSRTRSLWPSPLRWIPTSTDHIIAAEKRLLSLVKTPYVQEQV
NIGSGPPGSKVRWFRSASNEPRFINTVTFDSKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQL
GWGGSSRPDFTCKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPA
GFSSESDDKSEWLTKFRATWKGAVLNHLWESNFTPQKIIRGLGPWGPNLVRRYTTARFGAHSTGDILSEE
ESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWKVPTTFIYGRHDWMNYEGAVEARKRM
KVPCEIIRVPQGGHFVFLDNPSGFHSAVLYACRKYLSPDREERALPEGLTSA
>gnl|CDD|215485 PLN02895, PLN02895, phosphoacetylglucosamine mutase
MDEIQRASLLAASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTGAATGLMITASHNP
VSDNGVKIVDPSGGMLPQAWEPFADALANAPDPDALVQLIREFVKKENIPAVGGNPPAEVLLGRDTRPSG
PALLAAALKGVRAIGARAVDMGILTTPQLHWMVRAANKGMKATESDYFEQLSSSFRALLDLIPNGSGDDR
ADDKLVVDGANGVGAEKLETLKKALGGLDLEVRNSGKEGEGVLNEGVGADFVQKEKVPPTGFASKDVGLR
CASLDGDADRLVYFYVSSAGSKIDLLDGDKIASLFALFIKEQLRILNGNGNEKPEELLVRLGVVQTAYAN
GASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLFSERFLDWLEAAAAELSSKAKGS
EAHKAARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNALYQDLPSRQLKVKVADRTAITTTD
AETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLGGVGP
PP
>gnl|CDD|178484 PLN02896, PLN02896, cinnamyl-alcohol dehydrogenase
MELEGRESATGTYCVTGATGYIGSWLVKLLLQRGYTVHATLRDPAKSLHLLSKWKEGDRLRLFRADLQEE
GSFDEAVKGCDGVFHVAASMEFDVSSDHNNIEEYVQSKVIDPAIKGTLNVLKSCLKSKTVKRVVFTSSIS
TLTAKDSNGRWRAVVDETCQTPIDHVWNTKASGWVYVLSKLLTEEAAFKYAKENGIDLVSVITTTVAGPF
LTPSVPSSIQVLLSPITGDSKLFSILSAVNSRMGSIALVHIEDICDAHIFLMEQTKAEGRYICCVDSYDM
SELINHLSKEYPCSNIQVRLDEEKRGSIPSEISSKKLRDLGFEYKYGIEEIIDQTIDCCVDHGFLPQNRK
LNH
>gnl|CDD|178485 PLN02897, PLN02897, tetrahydrofolate dehydrogenase/cyclohydrolase, putative
ALASAHTKAFRLATRDVHCFSSILVSPPLVSLDLPENWIPYSDPPPPVSFETEQKTVVIDGNVIAEEIRT
KIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILSALRKFN
EDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRSGV
EIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGA
VVIDVGTTPVEDSSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRIFL
>gnl|CDD|215486 PLN02898, PLN02898, HMP-P kinase/thiamin-monophosphate pyrophosphorylase
VGTESPMKVPHVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQL
KSVLSDMPVDVVKTGMLPSAEIVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLAT
IVTPNVKEASALLGGDPLETVADMRSAAKELHKLGPRYVLVKGGHLPDSLDAVDVLYDGTEFHELRSSRI
KTRNTHGTGCTLASCIAAELAKGSDMLSAVKVAKRYVETALEYSKDIGIGNGAQGPFNHLFFLKSWAKKS
SRQSRFNPRNLFLYAVTDSGMNKKWGRSTVDAVRAAIEGGATIVQLREKEAETREFIEEAKACLAICRSY
GVPLLINDRVDVALACDADGVHLGQSDMPVRLARSLLGPGKIIGVSCKTPEQAEQAWKDGADYIGCGGVF
PTNTKANNKTIGLDGLREVCEASKLPVVAIGGISASNAASVMESGAPNLKGVAVVSALFDQEDVLKATRK
LHAILTEALSES
>gnl|CDD|178487 PLN02899, PLN02899, alpha-galactosidase
KRAQIFFILFCLLSLSLWIGASSQQQLASFPPRGWNSYDSFSWIVSEEEFLQNAEIVSQRLLPFGYEYVV
VDYLWYRKKVEGAYVDSLGFDVIDEWGRPIPDPGRWPSSRGGKGFTEVAEKVHAMGLKFGIHVMRGISTQ
AVNANTPILDAVKGGAYEESGRQWRAKDIALKERACAWMSHGFMSVNTKLGAGKAFLRSLYDQYAEWGVD
FVKHDCVFGDDFDLEEITYVSEVLKELDRPIVYSLSPGTSATPTMAKEVSGLVNMYRITGDDWDTWGDVA
AHFDVSRDFAAAGLIGAKGLRGRSWPDLDMLPLGWLTDPGSNVGPHRACNLTLDEQKTQMTLWAMAKSPL
MYGGDLRKLDQATYSLITNPTLLEINSHSSNNMEFPYVTSTRRNKKKSHSQHSTGVGKSDPSVLGLTSCK
DSKANGWSIRSLDKDLDQICWNEKMGRRGEEPLCLYKTKPLLASDEEIIHNSEYQGKLHLLTSDGGELCL
DASPKQKRTSKDFRSGSFSPCRWDANQMWELNNNGTLISSYSGLCATVNSVVAEVATGGVRSWIATGRKG
EIYVAFFNLNQEKTKISAKISDLAKALPGSKNLRTSSCTGHEVWSGKDFGVIKDSISATVEIHGCALFVL
HCS
>gnl|CDD|215487 PLN02900, PLN02900, alanyl-tRNA synthetase
MPEDDAPEKEWPGDRIRRTFLSFFESKGHTFLPSSPLVPVDDPTLLFTNAGMNQFKPIFLGTADPNTPLR
KLPRATNTQKCIRAGGKHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAIGWAWELLTKVYGLPADRLY
ATYFGGDEKQAPDDEARAIWLDYLPEERVLPFGCKDNFWEMGDTGPCGPCSEIHYDRIGERDAADLVNND
DPRFIEIWNLVFIQFNREADGSLKPLPAKHVDTGMGLERLASILQNKPSNYDTDLFMPIFDAIQEATGAR
PYAGKVGAEDDDRVDMAYRVVADHIRTLSFAIADGVVPSNEGRGYVLRRLLRRAVRYGRLLLGAEEGFFP
ALVEVVVELSGDVFPEVKKNEKRITEIIAEEELSFGKTLEKGIEKFKKALAAAKANGGPVLSGKDAFLLY
DTYGFPVDLTELMAEERGVTVDMEGFEAAMEEARERSRAAHLKAGGGAIELAAEATSWLQKQGVAATDDF
LKYDWLSDHEAVVKAILTGGGFVESVSEGDEVGIVLDKTSFYAESGGQIGDTGVLEGSGGAVVEVSDVQK
AGGFVLHIGTVTEGSVSVGDAVTCKVDYDRRRRIAPNHTATHLLNSALKEVLGDHVDQKGSLVAFEKLRF
DFSHGKPMTPEELREVESLVNEWIGDALPVEAKEMPLADAKRINGLRAVFGEKYPDPVRVVSVGGVYSME
LCGGTHVSNTAEAEAFKLLSEEGIAKGIRRITAVTGGAAVEAINAADSLERELDSALKVEGSDLEKKVAS
LKSRVDAAVIPAAKKEEIRARVSALQKELRAAQKEAAALRAKLAVAKATELASKALSAGKSVLVARLDVG
VDAAALKEAAEKVIAKLGDPAAVVLSSDEEKGKVSLVAAVPPGVVKKGLKAGKWLGAIAKLCGGGGGGKP
GFAQGQGRDAEKLDAALEKARAFAVA
>gnl|CDD|215488 PLN02901, PLN02901, 1-acyl-sn-glycerol-3-phosphate acyltransferase
MLVQHPFVLLFDRYRRKAQHFINKVWATLSTSPFYKIEVEGLENLPSPDEPAVYVSNHQSFLDIYTLFHL
GRPFKFISKTSIFLIPIIGWAMYMTGHIPLKRMDRRSQLECLKRCMELLKKGASVFFFPEGTRSKDGKLA
AFKKGAFSVAAKTGVPVVPITLVGTGKIMPNGKEGILNPGSVKVVIHPPIEGSDADELCNEARKVIAESL
VQNS
>gnl|CDD|215489 PLN02902, PLN02902, pantothenate kinase
GGEGERDMAPATAGTSIHRSGSRPQLDLSKAAIQGNLEERDPTILLPNQSDDISHLALDIGGSLIKLVYF
SRHEDRSTDDKRKRTIKERLGITNGNRRSYPILGGRLHFVKFETSKINECLDFISSKQLHRGGIHSWLSK
APPNGNGVIKATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGANFLLKAIRHEAFTHMEGEKEFVQIDQ
NDLFPYLLVNIGSGVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFDELLELSQRGDNSAIDML
VGDIYGGMDYSKIGLSASTIASSFGKVISENKELSDYRPEDISLSLLRMISYNIGQISYLNALRFGLKRI
FFGGFFIRGHAYTMDTISFAVHFWSKGEAQAMFLRHEGFLGALGAFMSYEKHGLDDLMAHQLVERFPMGA
PYTGGNIHGPPLGDLNEKISWMEKFVQKGTEITAPVPMGPPGTTGLGGFEVPSSRGGSLRSDASALNVGV
LHLVPTLEVFPLLADPKTYEPNTIDLSDQSEREYWFKVLSEHLPDLVDKAVASEGGTDDAKRRGDAFARA
FSAHLARLMEEPAAYGKLGLANLLELREECLREFHFVDAYRSIKQRENEASLAVLPDLLAELDSMTEETR
LLTLIEGVLAANIFDWGSRACVELYHKGTIIEIYRMSRNKMQRPWRVDDFDAFKERMLGSGGKKPKPHKR
ALLFVDNSGADVVLGMLPLARELLRRGTEVVLVANSLPALNDVTAMELPDIVAEAAKHCDILRRAAEAGG
LLVDAMVNTDDGSKDDSTSVPLMVVENGCGSPCIDLRQVSSELAAAAKDADLIVLEGMGRALHTNFNARF
KCEALKLAMVKNQRLAEKLINGNIYDCVCRYEPASK
>gnl|CDD|215490 PLN02903, PLN02903, aminoacyl-tRNA ligase
SASSLPTLFSLNPYHAPKPLARKRTTLLSTSSAASSAATVIPVVSAVDSMSSQLTWPSRSHLCGALSVND
VGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPEAHRTANRLRNEYVVAVEGTVRSRPQES
PNKKMKTGSVEVVAESVDILNVVTKSLPFLVTTADEQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVV
KLIRRYLEDVHGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIAR
CFRDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKGVQLPNPFPRLTYAEAMSKYGSDK
PDLRYGLELVDVSDVFAESSFKVFAGALESGGVVKAICVPDGKKISNNTALKKGDIYNEAIKSGAKGLAF
LKVLDDGELEGIKALVESLSPEQAEQLLAACGAGPGDLILFAAGPTSSVNKTLDRLRQFIAKTLDLIDPS
RHSILWVTDFPMFEWNEDEQRLEALHHPFTAPNPEDMGDLSSARALAYDMVYNGVEIGGGSLRIYRRDVQ
QKVLEAIGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFPKTTTAQCALTR
APSEVDDKQLQDLSIASTAPPP
>gnl|CDD|178492 PLN02904, PLN02904, oxidoreductase
MEETNKSVLDDSFTSAMTLTNSGVPHVPDRYVLPPSQRPMLGSSIGTSTITLPVIDLSLLHDPLLRSCVI
HEIEMACKGFGFFQVINHGIPSSVVKDALDAATRFFDLPVDEKMLLVSDNVHEPVRYGTSLNHSTDRVHY
WRDFIKHYSHPLSKWINLWPSNPPCYKEKVGKYAEATHVLHKQLIEAISESLGLEKNYLQEEIEEGSQVM
AVNCYPACPEPEIALGMPPHSDFGSLTILLQSSQGLQIMDCNKNWVCVPYIEGALIVQLGDQVEVMSNGI
YKSVVHRVTVNKDYKRLSFASLHSLPLHKKISPAPELVNENKPAAYGEFSFNDFLDYISSNDITQERFID
TLKKNNL
>gnl|CDD|178493 PLN02905, PLN02905, beta-amylase
MATDMQKLIGTSEEDDEEEMDMDVKEEDDGDRRNREKHIPVTGMVSVDGAAVSSSGNDEFMHQQSIQEQV
GTPGGGGSRRSRPLEEKERTKLRERHRRAITARILAGLRRHGNYNLRVRADINDVIAALAREAGWVVLPD
GTTFPSRSQGTRPAGGTSAVAATSSSSHLVSQQTPPPSLRGVSSGYRSSVEYNACRMKGVFVPASSPYDV
SPSQSSELVVVMGDRGSQNENHGLIGGSVDAINSKQILDIPPKLTERDFAGTPYVPVYVMLPLGVINMKC
ELADPDGLLKQLRILKSINVDGVKVDCWWGIVEAHAPQEYNWNGYKRLFQMVRELKLKLQVVMSFHECGG
NVGDDVCIPLPHWVAEIGRSNPDIFFTDREGRRNPECLSWGIDKERILRGRTALEVYFDYMRSFRVEFDE
FFEDGVISMVEVGLGPCGELRYPSCPVKHGWRYPGIGEFQCYDQYLLKSLRKAAEARGHLFWARGPDNTG
SYNSQPHETGFFCDGGDYDGYYGRFFLNWYSQVLVDHGDRVLSLAKLAFEGTCIAAKLPGVHWWYKTASH
AAELTAGFYNPCNRDGYAAIASMLKKHGAALNFVCGEVQMLNRPDDFSEALGDPEGLAWQVLNAAWDVDT
PVASENSLPCHDRVGYNKILENAKPLNDPDGRHFSSFTYLRLSPLLMERHNFVEFERFVKRMHGEAVLDL
QL
>gnl|CDD|215491 PLN02906, PLN02906, xanthine dehydrogenase
HQTLLEYLRDLGLTGTKLGCGEGGCGACTVMVSHYDRKTGKCVHYAVNACLAPLYSVEGMHVITVEGIGN
RRDGLHPVQEALASMHGSQCGFCTPGFIMSMYALLRSSKTPPTEEQIEECLAGNLCRCTGYRPILDAFRV
FAKTDDALYTGVSSLSLQDGEPICPSTGKPCSCGSKTTSAAGTCKSDRFQPISYSEIDGSWYTEKELIFP
PELLLRKLTPLKLLGNGGLTWYRPTSLQHLLELKAEYPDAKLVVGNTEVGIEMRFKNAQYPVLISPTHVP
ELNAIKVKDDGLEIGAAVRLSELQNLFRKVVKERPAHETSACKAFIEQLKWFAGTQIRNVASIGGNICTA
SPISDLNPLWMAAGATFVIISCDGDIRSVPASDFFLGYRKVDLKPDEILLSVFLPWTRPFEYVKEFKQAH
RRDDDIAIVNAGMRVKLEEKDGEWIVSDASIAYGGVAPLSVSARKTEEFLIGKPWNKETLQDALKVLQKD
ILIKEDAPGGMVEFRKSLALSFFFKFFLWVSHQLEADGSTIETFPESHLSAAQPFPRPSSVGMQDYETVK
QGTAVGQPEVHLSAELQVTGEAEYADDIPMPPNTLHAALVLSTKPHARILSIDDSEAKSSPGFAGIFLAK
DVPGDNMIGPVVHDEELFATDVVTCVGQVIGVVVADTQENAKAAARKVKVEYEELPAILSIEEAIEAGSF
HPNTERRLEKGDVELCFASGQCDRIIEGEVQMGGQEHFYLEPNSSLVWTSDSGNEVHMISSTQAPQKHQK
YVAHVLGLPMSKVVCKTKRIGGGFGGKETRSAFIAAAAAVPAYLLNRPVKLTLDRDVDMMITGQRHAFLG
KYKVGFTNEGKILALDLEIYNNGGNSLDLSGAVLERAMFHSDNVYEIPNVRIVGNVCFTNFPSNTAFRGF
GGPQGMLITENWIQRIAVELNKSPEEIREMNFQGEGSVTHYGQVLQHCTLPQLWDELKVSCDFLKRREEV
DEFNAKNRWKKRGVAMVPTKFGISFTTKFMNQAGALVHVYTDGTVLVTHGGVEMGQGLHTKVAQVAASAF
NIPLSSVFISETSTDKVPNASPTAASASSDMYGAAVLDACEQIKARMEPVASKLNFSSFAELVTACYFQR
IDLSAHGFYITPDIGFDWKTGKGNPFNYFTYGAAFAEVEIDTLTGDFHTRRVDIVMDLGYSINPAIDIGQ
IEGAFVQGLGWVALEELKWGDAAHKWIRPGSLFTCGPGTYKIPSVNDIPFKFNVSLLKGAPNPKAIHSSK
AVGEPPFFLAASVFFAIKDAIKAARAEVGLHGWFPLDTPATPERIRMACGDEITAPFAS
>gnl|CDD|215492 PLN02907, PLN02907, glutamate-tRNA ligase
MEAKLSFPPDSPPLAVIAAAKVAGVPLTIDPSLKSGSAPTLLFSSGEKLTGTNVLLRYIARSASLPGFYG
QDAFESSQVDEWLDYAPTFSSGSEFENACEYVDGYLASRTFLVGYSLTIADIAIWSGLAGSGQRWESLRK
SKKYQNLVRWFNSISAEYSDILNEVTAAYVGKRGAGKPAAAKSKEKVADAGKADGAKDKGSFEVDLPGAE
EGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD
AVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNNSVEENLRLWKEMIAGSERGL
QCCVRGKLDMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNA
QYYRILEDMGLRKVHIWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQF
ILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEGRVLLTLTDGPETPFVRIIPRHKKYEGAGKK
ATTFTNRIWLDYADAEAISEGEEVTLMDWGNAIIKEITKDEGGAVTALSGELHLEGSVKTTKLKLTWLPD
TNELVPLSLVEFDYLITKKKLEEDDNFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPF
VRSSKPIVLFAIPDGRQQKSGK
>gnl|CDD|178496 PLN02908, PLN02908, threonyl-tRNA synthetase
MAMPAATASAAAPSHPSDEEYLSAVIKKRIELFEKIQARQLARLESAGGDPIKVTLPDGAVKDGKKWVTT
PMDIAKEISKGLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGC
KLCIGPCTTRGEGFYYDAFYGDRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEI
INDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLK
EYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYN
MDLWETSGHAAHYKENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGAL
TGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAAL
TEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIERPVMI
HRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDRKIQK
KVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEFK
>gnl|CDD|178497 PLN02909, PLN02909, Endoglucanase
TSNRAGRANVLAALTLLGLYGIPSLVVAVGTHFNYKDALTKSIIFLEAQRSGKLPPNNRVPWRGDSALDD
GKLANVDLVGGYYDAGDNVKYGLPMAFTVTTLAWSTLAYEKELRATGELENVRAAIRWGTDYFLKAASRK
NRLYVQVGDPNLDHQCWVRPENMKTPRTVLEIDEKTPGTEIAAETAAAMAASSMVFRHVDHKYSRRLLNK
AKLLFKFAKAHKGTYDGECPFYCSYSGYNDELLWAATWLYKATKKQMYLKYIKHEAISASVAEFSWDLKY
AGAQVLLSKLNFEGEKGLQSYKQQADSFVCSVLPGSPFHQVFITPGGMIHLRDGANSQYVTSTAFLFSVY
SDILRRHNQKVMCGNQQFDSTRLMAFAKQQIDYLLGANPQGRSYMVGFGPNPPKQPHHRGASVPVLPANT
PVNCGLSFVEWFNKDRPNPNELTGAIVGGPDRQDNFVDKRWNSSYTEPCTYINSLAVGVLAKLAAR
>gnl|CDD|215493 PLN02910, PLN02910, polygalacturonate 4-alpha-galacturonosyltransferase
MTTFSRSAAFLLLVFVLHAYRPLQDNNLDEVYASSAAGVGNDPDEKDINIVATYSDTSGNIRLGRVKMKD
LSASWVLENPADKVHDQPKGSQRLEDSSSFQNGTGEEDNVSHSTTNQTDESGIQFPNKLPASPVKLQRQI
LRQERRDLRTAELIQQDKEADSQTQAAAIERSKSLDTSVKGKYSIWRRDYESPNSDSILKLMRDQIIMAK
AYANIAKSNNVTNLYVSLMKQFRENKRAIGEATSDAELHSSALDQAKAMGHVLSIAKDQLYDCHTMARKL
RAMLQSTERKVDALKKKSAFLIQLAAKTVPKPLHCLPLQLAADYFLLGFQNKDYVNKKKLEDPSLYHYAI
FSDNVLATSVVVNSTVLHAKEPQKHVFHIVTDKLNFAAMKMWFIINPPAKATIQVENIDDFKWLNSSYCS
VLRQLESARIKEYYFKANHPSSLSAGADNLKYRNPKYLSMLNHLRFYLPEVYPKLEKILFLDDDIVVQKD
LTPLWSIDMQGMVNGAVETCKESFHRFDKYLNFSNPKISENFDPNACGWAFGMNMFDLKEWRKRNITGIY
HYWQDLNEDRTLWKLGSLPPGLITFYNLTYPLDRSWHVLGLGYDPALNQTEIENAAVVHYNGNYKPWLDL
AIAKYKPYWSRYVQYDNPYLQLCNISE
>gnl|CDD|178499 PLN02911, PLN02911, inositol-phosphate phosphatase
VVVRRRASLAMASNSSRANVSMDAASALSDAVLDRFVDVAHKLADAAGEVTRKYFRTKFEIIDKEDLSPV
TIADRAAEEAMRSIILENFPSHAIFGEEHGLRCGEGSSDYVWVLDPIDGTKSFITGKPLFGTLIALLYKG
KPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYTTSPHMFSGDAEDAFARVRDKVKVP
LYGCDCYAYGLLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDWKGRKLRWEPSPGSLATSFNVVAA
GDARLHKQALDILEWQ
>gnl|CDD|178500 PLN02912, PLN02912, oxidoreductase, 2OG-Fe(II) oxygenase family protein
SATSKLLVSDIASVVDHVPSNYVRPVSDRPNMSEVETSGDSIPLIDLRDLHGPNRADIINQFAHACSSYG
FFQIKNHGVPEETIKKMMNVAREFFHQSESERVKHYSADTKKTTRLSTSFNVSKEKVSNWRDFLRLHCYP
IEDFIEEWPSTPISFREVTAEYATSVRALVLTLLEAISESLGLEKDRVSNTLGKHGQHMAINYYPPCPQP
ELTYGLPGHKDANLITVLLQDEVSGLQVFKDGKWIAVNPIPNTFIVNLGDQMQVISNDKYKSVLHRAVVN
TDKERISIPTFYCPSEDAVIGPAQELINEEEDSLAIYRNFTYAEYFEKFWDTAFATESCIDSFKASTA
>gnl|CDD|178501 PLN02913, PLN02913, dihydrofolate synthetase
IERISIANLRRNRNLLFSSSTEEPELGDFLRYLDSLKNYEKSGVPKDAGTDSDDGFDLGRMRRLMDRLGN
PHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERISVGKLGKPVSTNTLNDLFHGI
KPILDEAIQLENGSLTHFEVLTALAFKLFAQENVDIAVIEAGLGGARDATNVIDSSGLAASVITTIGEEH
LAALGGSLESIALAKSGIIKQGRPVVLGGPFLPHIESILRDKASSMNSPVVSASDPGVRSSIKGIITDNG
KPCQSCDIVIRVEKDDPLFIELSDVNLRMLGSHQLQNAVTAACAALCLRDQGWRISDASIRAGLENTNLL
GRSQFLTSKEAEVLGLPGATVLLDGAHTKESAKALVDTIKTAFPEARLALVVAMASDKDHLAFASEFLSG
LKPEAVFLTEADIAGGKSRSTSASALKEAWIKAAPELGIETLLAENNSLLKSLVDASAILRKARTLDPSS
VVCVTGSLHIVSAVLASLQG
>gnl|CDD|178502 PLN02914, PLN02914, hexokinase
MFSSPVVTPAIGSFTFSSRPRRRPRSRMAVRSNAVSVAPILTKLQKDCATPLPVLRHVADAMAADMRAGL
AVDGGGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTS
EELFDFIASGLANFVAKEGGKFHLPEGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVAC
LNEAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKSSSGRTI
INTEWGAFSDGLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLST
PFALRTPHLCAMQQDNSDDLQAVGSILYDVLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKME
EDSKGMIFGKRTVVAMDGGLYEKYPQYRRYMQDAVTELLGLELSKNIAIEHTKDGSGIGAALLAATNSKY
>gnl|CDD|215494 PLN02915, PLN02915, cellulose synthase A [UDP-forming], catalytic subunit
MDDEDRPPTRQSADAKTCRVCGDEVGVKEDGQPFVACHVCGFPVCKPCYEYERSEGNQCCPQCNTRYKRH
KGCPRVEGDDEEGNDMDDFEDEFQIKSPQDHEPVHQNVFAGSENGDYNAQQWRPGGPAFSSTGSVAGKDL
EAEREGYGNAEWKDRVDKWKTRQEKRGLVNKDDSDDGDDKGDEEEYLLAEARQPLWRKVPIPSSKINPYR
IVIVLRLVILCFFFRFRILTPAYDAYPLWLISVICEIWFALSWILDQFPKWFPINRETYLDRLSMRFERD
GEPNRLAPVDVFVSTVDPLKEPPIITANTVLSILAVDYPVDKVSCYVSDDGASMLLFDTLSETAEFARRW
VPFCKKHNIEPRAPEFYFSQKIDYLKDKVQPTFVKERRAMKREYEEFKVRINALVAKAQKKPEEGWVMQD
GTPWPGNNTRDHPGMIQVYLGSEGALDVEGKELPRLVYVSREKRPGYNHHKKAGAMNALVRVSAVLTNAP
FMLNLDCDHYINNSKAVREAMCFLMDPQLGKKLCYVQFPQRFDGIDRHDRYANRNVVFFDINMKGLDGIQ
GPVYVGTGCVFNRQALYGYDPPVSEKRPKMTCDCWPSWCCCCCGGGRRGKSKKSKKGKKGRRSLLGGLKK
RKKKGGGGGSMMGKKYGRKKSQAVFDLEEIEEGLEGYDELEKSSLMSQKNFEKRFGQSPVFIASTLMEDG
GLPEGTNPAALIKEAIHVISCGYEEKTEWGKEIGWIYGSVTEDILTGFKMHCRGWKSVYCMPKRPAFKGS
APINLSDRLHQVLRWALGSVEIFMSRHCPLWYAYGGKLKWLERLAYINTIVYPFTSIPLLAYCTIPAVCL
LTGKFIIPTLNNLASIWFLALFLSIIATSVLELRWSGVSIEDLWRNEQFWVIGGVSAHLFAVFQGLLKVL
GGVDTNFTVTSKAADDEADEFGELYLFKWTTLLIPPTTLIILNMVGVVAGVSDAINNGYGSWGPLFGKLF
FAFWVIVHLYPFLKGLMGRQNRTPTIVVLWSILLASIFSLVWVRIDPFLPKQTGPILKQCGVEC
>gnl|CDD|178504 PLN02916, PLN02916, pectinesterase family protein
TDLITIMFLLAIAATISASCTAELDVLETARTAVLQARRWFGSSLVLEATSEVASGSYYNLGEALSDCEK
LYDESEARLSKLLVSHENFTVEDARTWLSGVLANHHTCLDGLEQKGQGHKPMAHNVTFVLSEALALYKKS
RGHMKKGLPRRPKHRPNHGPGREVHPPSRPNQNGGMLVSWNPTTSRADFVVARDGSGTHRTINQALAALS
RMGKSRTNRVIIYVKAGVYNEKVEIDRHMKNVMFVGDGMDKTIITNNRNVPDGSTTYSSATFGVSGDGFW
ARDITFENTAGPHKHQAVALRVSSDLSVFYRCSFKGYQDTLFVHSLRQFYRDCHIYGTIDFIFGDAAVVF
QNCDIFVRRPMDHQGNMITAQGRDDPHENTGISIQHSRVRASPEFEAVKGRFKSFLGRPWKKYSRTVFLK
TDLDGLIDPRGWREWSGSYALSTLYYGEYMNTGAGASTSRRVKWPGFHVLRGTEEASPFTVSRFIQGESW
IPATGVPFSAGI
>gnl|CDD|215495 PLN02917, PLN02917, CMP-KDO synthetase
SPSSSSSSSSSSSTKSWIVHGIVAGAAIAAAIGAGAYLRRSRKFRSRVVGIIPARFASSRFEGKPLVHIL
GKPMIQRTWERAKLATTLDHIVVATDDERIAECCRGFGADVIMTSESCRNGTERCNEALKKLEKKYDIVV
NIQGDEPLIEPEIIDGVVKALQAAPDAVFSTAVTSLKPEDASDPNRVKCVVDNQGYAIYFSRGLIPYNKS
GKVNPQFPYLLHLGIQSYDAKFLKIYPELPPTPLQLEEDLEQLKVLENGYKMKVIKVDHEAHGVDTPEDV
EKIEALMRERNIS
>gnl|CDD|215496 PLN02918, PLN02918, pyridoxine (pyridoxamine) 5'-phosphate oxidase
NIKSTATMTFTFLLQSLLPLPISPPPPHSSSLSSSPSPTQRFLTPSQGSRLPPRRRALCTKSQDPRWRRA
MASLAVIPNMQDSGSPPLSYLTQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGEYSRVLA
ICGPGNNGGDGLVAARHLHHFGYKPFVCYPKRTAKPLYTGLVTQLESLSVPFVSVEDLPADLSKDFDIIV
DAMFGFSFHGAPRPPFDDLIRRLVSLQNYEQTLKHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAP
KLCAKKFRGPHHFLGGRFVPPSIVEKYKLHLPPYPGTSMCVRIGKPPSVDISALRENYISPELLEEQVET
DPTDQFRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDKNGFVWYTNYESQKGSDLSENPSA
ALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYQEYKELEKKYSD
GSVIPKPKNWGGYRLKPNLFEFWQGQQSRLHDRLQYSLQEVNGKPVWKIHRLAP
>gnl|CDD|215497 PLN02919, PLN02919, haloacid dehalogenase-like hydrolase family protein
MALKLASPPSLFSWPRRHCAGDFPPALAFASSIRGRRSRSGVWLGKNGGARSKSCAKVEEKSRGAEIATE
EWGKVSAVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTVEDFVPFMGTGEANFLGGVASVKGVKGFDPD
AAKKRFFEIYLEKYAKPNSGIGFPGALELITQCKNKGLKVAVASSADRIKVDANLAAAGLPLSMFDAIVS
ADAFENLKPAPDIFLAAAKILGVPTSECVVIEDALAGVQAARAAGMRCIAVTTTLSEEILKDAGPSLIRK
DIGNISLSDILTGGSDATPNVTGMDWINTILDTGSILGFQGSRRDILRYGSLGIALSCLYFAATNWKAMQ
YASPKALWNALFGVDDPSFAQNSGEGCVQQFVSYISDLESKKTATKVPEFPPKLDWLNTAPLQFRRDLKG
KVVILDFWTYCCINCMHVLPDLEFLEKKYKDQPFTVVGVHSAKFDNEKDLEAIRNAVLRYNISHPVVNDG
DMYLWRELGVSSWPTFAVVSPNGKLIAQLSGEGHRKDLDDLVEAALQYYGEKKLLDSTPLPLSLEKDNDP
RLLTSPLKFPGKLAIDLLNNRLFISDSNHNRIVVTDLDGNFIVQIGSTGEEGLRDGSFEDATFNRPQGLA
YNAKKNLLYVADTENHALREIDFVNETVRTLAGNGTKGSDYQGGKKGTSQVLNSPWDVCFEPVNEKVYIA
MAGQHQIWEYNISDGVTRVFSGDGYERNLNGSSGTSTSFAQPSGISLSPDLKELYIADSESSSIRALDLK
TGGSRLLAGGDPTFSDNLFKFGDHDGVGSEVLLQHPLGVLCAKDGQIYVADSYNHKIKKLDPATKRVTTL
AGTGKAGFKDGKALKAQLSEPAGLALGENGRLFVADTNNSLIRYLDLNKGEAAEILTLELKGVQPPRPKS
KSLKRLRRRSSADTQVIKVDGVTSLEGDLQLKISLPPGYHFSKEARSKFEVEVEPENAVDIDPDEGTLSP
DGRASLHFKRSSASASTGRISCKVYYCKEDEVCLYQSLVFEVPFEEENGGESSSSITLKYTVKPKAPQPS
LQLPITR
>gnl|CDD|215498 PLN02920, PLN02920, pantothenate kinase 1
MERNREDEGDGNSSPIQISHLALDIGGSLIKLVYFSRNSGDSEDPRNDSSVKSDGVNGRLHFAKFETRKI
NDCLEFISSNKLHHGGFQHHENPTHDKNFIKATGGGAYKFADLFKEKLGISLDKEDEMDCLVTGANFLLK
AVHHEAFTYLDGQKEFVQIDHNDLYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKC
KSFDELLELSHQGNNRVIDMLVGDIYGGMDYSKIGLSSTTIASSFGKAISDNKELEDYKPEDVARSLLRM
ISNNIGQISYLNALRFGLKRIFFGGFFIRGHSYTMDTISVAVHFWSKGEAKAMFLRHEGFLGALGAFMSY
EKHSLDDLMVNQVVQLPVNASSGTDTNHNPLTGDLNDSESIQCSVYLA
>gnl|CDD|178509 PLN02921, PLN02921, naphthoate synthase
MDAARRRLARVANHLVPSANPASMAAARSSSATAPPDSYRRVHGDVSSEPVVWRKVPDGSGKEFTDIIYE
KAVGEGIAKITINRPERRNAFRPRTVKELQRAFNDARDDSSVGVIILTGKGTKAFCSGGDQAVRGKDGYV
GPDDAGRLNVLDLQIQIRRLPKPVIAMVAGYAVGGGHILHMVCDLTIAADNAVFGQTGPKVGSFDAGYGS
SIMARLVGQKKAREMWFLARFYTASEALKMGLVNTVVPLDELEGETVKWCREILRNSPTAIRVLKSALNA
ADDGHAGLQELGGNATLLFYGSEEGNEGRTAYLEGRAPDFSKFPRLP
>gnl|CDD|215499 PLN02922, PLN02922, prenyltransferase
EVTASDEDGEELSRATLWWRAIKLPMYSVALVPLTVGAAAAYLQTGLFDARRYGTLLLSSVLVITWLNLS
NDAYDADTGVDKNKKESVVNLVGSRRGVLAAAIGCLALGAAGLVWASLVAGNIRVILLLAAAILCGYVYQ
CPPFRLSYKGLGEPLCFAAFGPLATTAFYLALASGAGGSEMAILPLTPTVLSASVLVGLTTTLILFCSHF
HQIDGDRAVGKMSPLVRLGTEKGSRVVRWAVLLLYSLLAALGLLKALPLPCALLCFLTLPLGKLVVDFVE
KNHKDNAKIFMAKYYCVRLHALFGAALALGLVLAR
>gnl|CDD|178511 PLN02923, PLN02923, xylose isomerase
MKGGSILLLLLCALLCLSGVIAAQPPTCPADLGSKCSDSDEWEGEFFPGIPKIKYEGPSSKNPLAYKWYN
AEEEILGKKMKDWMRFSVAFWHTFRGTGGDPFGAPTKYWPWEDGTNSLAMAKRRMRANFEFLKKLGVDRW
CFHDRDIAPDGKTLEESNANLDEVVALAKELQEGTKIRPLWGTAQLFKHPRYMHGAATSSEVGVYAYAAA
QVKKAMEVTHYLGGENYVFWGGREGYQTLLNTDMERELDHLARFLEAAVAYKKKIGFNGTLLIEPKPQEP
TKHQYDWDAATAANFLRKYGLIDEFKLNIECNHATLSGHSCHHELETARINGLLGNIDANTGDAQTGWDT
DQFLTDIAEATMVMLSVIKNGGLAPGGFNFDAKLRRESTDVEDLFIAHISGMDTMARGLRNAAKLLEEGS
LPELVRKRYASFDSELGAQIEAGKADFEELEKKALEWGEPKVPSAKQELAEMIFQSAL
>gnl|CDD|178512 PLN02924, PLN02924, thymidylate kinase
FFSMGMETESSVESRGALIVLEGLDRSGKSTQCAKLVSFLKGLGVAAELWRFPDRTTSVGQMISAYLSNK
SQLDDRAIHLLFSANRWEKRSLMERKLKSGTTLVVDRYSYSGVAFSAAKGLDLEWCKAPEVGLPAPDLVL
YLDISPEEAAERGGYGGERYEKLEFQKKVAKRFQTLRDSSWKIIDASQSIEEVEKKIREVVLDTVQRCLA
GKPLSRLWSS
>gnl|CDD|178513 PLN02925, PLN02925, 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
MATGVLPAPLSGLKTSDSKLGFGKSMDFVRICDVRSVSVIRNSNTGPDLVELQPASEGSPLLVPRQKYCE
SIHKTVRRKTRTVMVGNVALGSEHPIRIQTMTTTDTKDVEATVDQVMRIADKGADIVRITVQGKKEADAC
FEIKNTLVQKGYNIPLVADIHFAPSVALRVAECFDKIRVNPGNFADRRAQFEKLEYTEDDYQKELEHIEE
VFTPLVEKCKKYGRAMRIGTNHGSLSDRIMSYYGDSPRGMVESAFEFARICRKLDYHNFVFSMKASNPVV
MVQAYRLLVAEMYVLGWDYPLHLGVTEAGEGEDGRMKSAIGIGTLLQDGLGDTIRVSLTEPPEEEIDPCR
RLANLGMKAAALQQGVAPFEEKHRDYFDFQRRTGQLPVQKEGEEVDYRNVLHRDGSVLMSVSLDQLKAPE
LLYRSLAAKLVVGMPFKDLATVDSILLRELPPVDDEEARLALKRLIDVSMGVIAPLSEQLTKPLPNAMAL
VNLKELSSGAHKLLPEGTRLAVTLRGDEPYEELEILKDVDATMLLHDVPFTEDKVSRVHAARRLFEYLSS
NSLNFPVIHHIQFPAGIHRDDLVIQAGSQAGALLVDGLGDGVLLEAPDQDFDFLRNTSFGLLQGCRMRNT
KTEYVSCPSCGRTLFDLQEVSAEIREKTSHLPGVSIAIMGCIVNGPGEMADADFGYVGGAPGKIDLYVGK
EVVKRGIAMEEATDALIQLIKDHGRWVDPEVEE
>gnl|CDD|215500 PLN02926, PLN02926, histidinol dehydrogenase
CSMKSYRLSELSASEVDSLKARPRIDFSSILETVNPIVENVRSRGDAAVKEYTSKFDKVALDSVVERVSD
LPDPVLDADVKEAFDVAYDNIYAFHLAQKSTEKLEVETMPGVRCRRVARPIGAVGLYVPGGTAVLPSTAL
MLAVPAQIAGCKTVVLATPPRKDGSICPEVLYCAKKAGVTHILKAGGAQAIAAMAWGTDSCPKVDKIFGP
GNQYVTAAKMILQNSEAMVSIDMPAGPSEVLVIADKTANPVHVAADLLSQAEHGPDSQVVLVAVGDVDLD
AIEEEVEKQCQSLPRGEIASKALGHSFIVVARDMAEAISFSNLYAPEHLIVNVEDAESWLDKIDNAGSVF
LGRWTPESVGDYASGTNHVLPTYGYARMYGGVSLDSFLKYMTVQSLTEEGLQNLGPYVARMAEVEGLEAH
KRAVTLRLGDI
>gnl|CDD|178515 PLN02927, PLN02927, antheraxanthin epoxidase/zeaxanthin epoxidase
MGSTLFCYSINPSPSKLDFTRTHVFSPVAKQFYLDLSSFSGKPGGGLSGFRSRKALLGVKAATALVEKEE
KREAVTEKKKKSRVLVAGGGIGGLVFALAAKKKGFDVLVFEKDLSAIRGEGKYRGPIQIQSNALAALEAI
DIDVAEQVMEAGCITGDRINGLVDGISGSWYVKFDTFTPAASRGLPVTRVISRMTLQQILARAVGEDVIR
NESNVVDFEDSGDKVTVVLENGQRYEGDLLVGADGIWSKVRNNLFGRSEATYSGYTCYTGIADFIPADIE
SVGYRVFLGHKQYFVSSDVGGGKMQWYAFHEEPAGGADAPNGMKKRLFEIFDGWCDNVLDLLHATEEDAI
LRRDIYDRSPGFTWGKGRVTLLGDSIHAMQPNMGQGGCMAIEDSFQLALELDEAWKQSVETNTPVDVVSS
LKRYEESRRLRVAIIHAMARMAAIMASTYKAYLGVGLGPLSFLTKFRVPHPGRVGGRFFVDIAMPLMLDW
VLGGNSEKLEGRPPSCRLTDKADDRLREWFEDDDALERTIKGEWYLIPHGDDCCVSETLCLTKDEDQPCI
VGSEPDQDFPGMRIVIPSSQVSKMHARVIYKDGAFFLMDLRSEHGTYVTDNEGRRYRATPNFPARFRSSD
IIEFGSDKKAAFRVKVIRKTPKSTRKNESNNDKLLQTA
>gnl|CDD|215501 PLN02928, PLN02928, oxidoreductase family protein
SSKSVKIDKRVHHSDMRPTRVLFCGPEFPASYSYTREYLQKYPFIQVDAVAREDVPDVIANYDICVPKMM
RLDADIIARASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPSEGTGNAASCAEMAIYLMLGLLRKQNEM
QISLKARRLGEPIGDTLFGKTVFILGYGAIGIELAKRLRPFGVKLLATRRSWTSEPEDGLLIPNGDVDDL
VDEKGGHEDIYEFAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGH
LGGLAIDVAWSEPFDPDDPILKHPNVIITPHVAGVTEYSYRSMGKIVGDAALQLHAGRPLTGIEFVN
>gnl|CDD|215502 PLN02929, PLN02929, NADH kinase
PFDVYPFRQLEGSGRATNPKVLEYLEDRHKVHKDTVNFCKDILQQKSVDWECVLRNELSQPIRDVDLVVA
VGGDGTLLQASHFLDDSIPVLGVNSDPTQKDEVEEYSDEFDARRSTGHLCAATAEDFEQVLDDVLFGRLK
PTELSRISTVVNGTLLETPALNDVLIAHPSPAAVSRFSFRVGRQGGSSGPLINVRSSGLRVSTAAGSTAA
MLSAGGFPMPLLSRDLQYMVREPISPGHPPKSLMHGFYKPGQHMQVRWNSRKGTIYIDGSHVMHSIKLGD
TIEISSDAPPLKVFLSHWFLR
>gnl|CDD|178518 PLN02930, PLN02930, CDP-diacylglycerol-serine O-phosphatidyltransferase
AYKPHTISLLLIGACFLIWASGALDPESTTSGDLVTSVKRGVWAMIAVFLAYCLLQAPSTVLIRPHPAIW
RLVHGMAVVYLVALTFLLFQKRDDARQFMKFLHPDLGVELPERSYGADCRIYTPEHPSSRFKNVYDTLFD
EFVVAHILGWWGKAIMIRNQPLLWVLSIGFELMELTFRHMLPNFNECWWDSIVLDVLICNWFGIWAGMHT
VKYFDGKTYEWVGISRQPNIIGKVKRTLGQFTPAQWDKDEWHPLQGPWRFLQVLFLCVVFLTVELNTFFL
KFCLWIPPRNPLIVYRLILWWLIAIPTIREYNSFLQDRKPVKKLGAFCWLSLAICIVELLICIKFGHGLF
PKP
>gnl|CDD|215503 PLN02931, PLN02931, nucleoside diphosphate kinase family protein
ISRSTLQPLFLLLLASFPIRCSSSGASEEERTLAMIKPDGLSGNYTERIKEVILESGFSIVKEMTTQLDE
DRASLFYAEHSSRSFFPSLVKYMTSGPVLVMVLEKENAVSDWRTLIGPTDARKAKISHPNSIRAMCGLDS
EKNCVHGSDSPESAEREISFFFGDVSSGDVASQHDEL
>gnl|CDD|178520 PLN02932, PLN02932, 3-ketoacyl-CoA synthase
FNYLMAHRFKLCFLPLMVGIAMEASRLSTQDLQNFYLYLQNNLTSLTMFFLYLALGSTLYLMTRPKPVYL
VDFSCYLPPSHLKASIQTIMGHVRRVREAGAWKQESDYLMDFCEKILERSGLGQETYIPEGLQCLPLQQN
LAVSRKETEEVIIGAVDNLFRNTGISPSDIGILVVNSSTFNPTPSLSSILVNKFKLRDNIKSLNLGGMGC
SAGVIAIDAAKSLLQVHRNTYALVVSTENITQNLYLGNNKSMLVTNCLFRIGGAAILLSNRSRDRKRAKY
ELVHTVRVHTGADDRSYECATQEEDEDGIVGVSLSKNLPMVAARTLKINIATLGPLVLPLSEKFHFFVRF
VKKKFFNPKLKHYIPDFKLAFEHFCIHAGGRALIDEMEKNLHLTPLDVEASRMTLHRFGNTSSSSIWYEL
AYTEAKGRMKKGDRIWQIALGSGFKCNSSVWVALRNVKPSANNPWEDCLHKYPVEIDI
>gnl|CDD|178521 PLN02933, PLN02933, Probable pectinesterase/pectinesterase inhibitor
NNHPMREKPKHIIFNLLSLIFFLIFLSTVVSSQSPSYTTHKTQRLTETKTIPELIIADLNLTILKVNLAS
SNFSDLQTRLGPNLTHRERCAFEDCLGLLDDTISDLTTAISKLRSSSPEFNDVSMLLSNAMTNQDTCLDG
FSTSDNENNNDMTYELPENLKESILDISNHLSNSLAMLQNISGKIPGPKSSEVDVEYPSWVSGNDRRLLE
APVQETNVNLSVAIDGTGNFTTINEAVSAAPNSSETRFIIYIKGGEYFENVELPKKKTMIMFIGDGIGKT
VIKANRSRIDGWSTFQTATVGVKGKGFIAKDISFVNYAGPAKHQAVALRSGSDHSAFYRCEFDGYQDTLY
VHSAKQFYRECDIYGTIDFIFGNAAVVFQNCSLYARKPNPNHKIAFTAQSRNQSDQPTGISIISSRILAA
PDLIPVKENFKAYLGRPWRKYSRTVIIKSFIDDLIHPAGWLEWKKDFALETLYYGEYMNEGPGANMTNRV
TWPGFRRIENVTEATQFTVGPFIDGSTWLNSTGIPFTLGF
>gnl|CDD|215504 PLN02934, PLN02934, triacylglycerol lipase
MDDASPTTGTNYLIVRPDKGGFLDLFRYLVRGDQGSGAKFLESSDERVPGEEAVDHRWVILVSIIIRKII
ALFGTPMEYTGFVVDFFLNLFSQNGGFLGLLLNLLQGKVVIPQRGSETFISTIGHLDGRIDLYKTPNLVE
QLDDSVSNHNSKIKGELGNRALMDLCIMASKLAYENAKVVENVVDHHWKMHFVAFYNCWNDFQKQMSTQV
FIFCDKPKDANLIVISFRGTEPFDADDWGTDFDYSWYEIPKVGKVHMGFLEAMGLGNRDDTTTFQTSLQT
KATSELKEEESKKNLLEMVERSAYYAVRSKLKSLLKEHKNAKFVVTGHSLGGALAILFPTVLVLQEETEV
MKRLLGVYTFGQPRIGNRQLGKFMEAQLNYPVPRYFRVVYCNDLVPRLPYDDKTFLYKHFGVCLYYDSRY
FGQKMDEEPDRNPFGLRNAISAHLNAVWELWRSFIMGYTHGPEYKEGWFSIFFRIMGLVLPGVAAHSPTD
YVNSVRLGRERVVPMSSLKSFARGY
>gnl|CDD|215505 PLN02935, PLN02935, Bifunctional NADH kinase/NAD(+) kinase
SQPDNGFSDSLSLFHSEKAVQELLQQTPIQDTDDHLVEFSEALRTVAKALRRVAEGKALAQAEAAEWKRK
YELERARNQQLEHKELSSGECNEESNDQRLENLANQPMLYNEAINCCGMEGICSHEVLQDGSTDSDNRSV
LNKVMRKASFKLSWGCKGDKSDQHKHDIVSFERGNITTAERSSKQISLKWESDPQTVLIITKPNSTSVRV
LCAEMVRWLREQKGLNIYVEPRVKKELLSESSYFNFVQTWEDEKEILLLHTKVDLVITLGGDGTVLWAAS
MFKGPVPPVVPFSMGSLGFMTPFHSEQYRDCLDAILKGPISITLRHRLQCHIIRDAAKNEYETEEPILVL
NEVTIDRGISSFLTNLECYCDNSFVTCVQGDGLILSTTSGSTAYSLAAGGSMVHPQVPGILFTPICPHSL
SFRPLILPEYVTIRVQVPFNSRGQAWASFDGKDRKQLSAGDALVCSMAPWPVPTACQVESTNDFLRSIHD
GLHWNLRKTQSFDGPRST
>gnl|CDD|178524 PLN02936, PLN02936, epsilon-ring hydroxylase
WVSPDWLTSLNRLWGDDSGIPVADAKLEDVTDLLGGALFLPLFKWMNEYGPVYRLAAGPRNFVVVSDPAI
AKHVLRNYGSKYAKGLVAEVSEFLFGSGFAIAEGELWTARRRAVVPSLHRRYLSVMVDRVFCKCAERLVE
KLEPVALSGEAVNMEAKFSQLTLDVIGLSVFNYNFDSLTTDSPVIQAVYTALKEAETRSTDLLPYWKVDF
LCKISPRQIKAEKAVTVIRETVEDLVDKCKEIVEAEGEVIEGEEYVNDSDPSVLRFLLASREEVSSVQLR
DDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPPTYEDIKELKYLTRCINESMRLY
PHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGPVPNETNTDFRYI
PFSGGPRKCVGDQFALLEAIVALAVLLQRLDLELVPDQDIVMTTGATIHTTNGLYMTVSRRRVPDGDSV
>gnl|CDD|215506 PLN02937, PLN02937, Putative isoaspartyl peptidase/L-asparaginase
MAGDGADQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCIDAVSAAIQVLEDDPST
NAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEG
ARQWAKSKGIDLPETVEEAEKWLVTERAKEQWKKYKTMLASAIAKSSCDSQSTSKLSELEAPRSNPSNGT
GGGQSSMCTASDEDCIMDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGAPF
IVGCCVSGAGEYLMRGFAARECCVSSSLSQAGPASACMKVLRSVIQGSSAKTTDKDAGILLVQADASVMA
PGNSPSLKAVEIAAAYSSLSFGIGYFGSSMERPKVSILRSTKQQSKTGIDHFEARIDLSAKCSL
>gnl|CDD|178526 PLN02938, PLN02938, phosphatidylserine decarboxylase
MKFRVSSKLPLLARYSLLRHQHHHQSSRASVNGGSGSSQGNSFLLPGATVATLLMLGALHARRLYEDKKV
EEAREKGIEPEFSPDTKASFLRLLPLRSISRLWGSLTSVELPVWMRPYVYKAWARAFHSNLEEAALPLEE
YASLREFFVRSLKEGARPIDPDPNCLVSPVDGIVLRFGELKGPGTMIEQVKGFSYSVSALLGANSLLPMT
AEGKEEKEEETLKDKSSKSWLRVSLASPKLRDPVSASPMKGLFYCVIYLGPGDYHRIHSPSDWNIEVRRH
FSGRLFPVNERATRTIRNLYVENERVVLEGEWQEGFMAMAAVGATNIGSIELFIEPELRTNRPKKKIFNS
EPPEERVYEPEGCGLCLKKGDEVAVFNLGSTVVLVFEAPVEVEPLFKVLDQSSSDFRFCVRKGDRIRVGQ
ALGRWMEE
>gnl|CDD|215507 PLN02939, PLN02939, transferase, transferring glycosyl groups
AAAAESAALLSHGCGPIRSRAPFYLPSRRRLAVSCRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTD
ENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNA
EKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNEL
LIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKF
IVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSS
YKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEHPADDMPSEFWSRIL
LLIDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGKNEREAVENFLKLTLSGTSSGLHIVHIAAE
MAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQYDQIRNLKVLDVVVESYFDGNLFKNKIWTGT
VEGLPVYFIEPQHPSKFFWRAQYYGEHDDFKRFSYFSRAALELLYQSGKKPDIIHCHDWQTAFVAPLYWD
LYAPKGFNSARICFTCHNFEYQGTAPASDLASCGLDVHQLDRPDRMQDNAHGRINVVKGAIVYSNIVTTV
SPTYAQEVRSEGGRGLQDTLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNANDLQGKAANKAALRKQL
GLSSADASQPLVGCITRLVPQKGVHLIRHAIYKTAELGGQFVLLGSSPVPHIQREFEGIADQFQSNNNIR
LILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSVFDFDDETIPVELRNG
FTFLTPDEQGLNSALERAFNYYKRKPEVWKQLVQKDMNIDFSWDSSASQYEELYQRAVARARAAANR
>gnl|CDD|178528 PLN02940, PLN02940, riboflavin kinase
MSAAKPLKKLVSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIVGKTPLEAAATVVEDYGL
PCSTDEFNSEITPLLSEQWCNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHQGWKESFSVI
VGGDEVEKGKPSPDIFLEAAKRLNVEPSNCLVIEDSLPGVMAGKAAGMEVIAVPSIPKQTHLYSSADEVI
NSLLDLQPEKWGLPPFNDWIEGTLPIEPWHIGGPVIKGFGRGSKVLGIPTANLSTENYSDVLSEHPSGVY
FGWAGLSTRGVYKMVMSIGWNPYFNNTEKTIEPWLLHDFGEDFYGEELRLVIVGYIRPEANFPSLESLIA
KIHEDRRIAEKALDLPLYAKYKDDPYLTNSLL
>gnl|CDD|215508 PLN02941, PLN02941, inositol-tetrakisphosphate 1-kinase
MGERAGAAASAPLSSSSQQKRFVVGYALTPKKVKSFLQPSLEALARSKGIDLVAIDPSRPLSEQGPFDVI
LHKLYGKEWRQQLEEYREKHPDVTVLDPPDAIQRLHNRQSMLQVVADLKLSDGYGSVGVPKQLVVYDDES
SIPDAVALAGLKFPLVAKPLVADGSAKSHKMSLAYDQEGLSKLEPPLVLQEFVNHGGVLFKVYVVGDYVK
CVRRFSLPDVSEEELSSAEGVLPFPRVSNAAASADDADNGGLDPEVAELPPRPFLEDLARELRRRLGLRL
FNFDMIREHGTGDRYYVIDINYFPGYAKMPGYETVLTDFLLSLVQKKY
>gnl|CDD|178530 PLN02942, PLN02942, dihydropyrimidinase
GASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPF
MGTETIDDFFSGQAAALAGGTTMHIDFVIPVNGNLLAGYEAYEKKAEKSCMDYGFHMAITKWDDTVSRDM
ETLVKEKGINSFKFFMAYKGSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEG
HALSRPPLLEGEATARAIRLAKFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWD
PDFTIASKYVMSPPIRPAGHGKALQAALSSGILQLVGTDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMH
LVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILNPNSTFTISAKTHHSRIDTNV
YEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFSYLFDGIQKADAAYLSSLRAPVKRT
>gnl|CDD|215509 PLN02943, PLN02943, aminoacyl-tRNA ligase
MALSRPSSALLSCSSIRRLNPLLLSACRRRAWAPRRAARRFCAAAASENDVFTSPETAKSFDFTSEERIY
NWWESQGYFKPNFDRGGDPFVIPMPPPNVTGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGIA
TQLVVEKMLASEGIKRTDLGRDEFTKRVWEWKEKYGGTITNQIKRLGASCDWSRERFTLDEQLSRAVVEA
FVRLHEKGLIYQGSYMVNWSPNLQTAVSDLEVEYSEEPGTLYYIKYRVAGGSEDFLTIATTRPETLFGDV
AIAVNPEDDRYSKYIGKMAIVPMTYGRHVPIIADRYVDKDFGTGVLKISPGHDHNDYLLARKLGLPILNV
MNKDGTLNEVAGLYWFEAREKLWSDLEETGLAVKKEPHTLRVPRSQRGGEVIEPLVSKQWFVTMEPLAEK
ALKAVENGELTIIPERFEKIYNHWLSNIKDWCISRQLWWGHRIPVWYIVGKDCEEDYIVARSAEEALEKA
REKYGKDVEIYQDPDVLDTWFSSALWPFSTLGWPDVSAEDFKKFYPTTVLETGHDILFFWVARMVMMGIE
FTGTVPFSYVYLHGLIRDSQGRKMSKTLGNVIDPLDTIKEFGTDALRFTLALGTAGQDLNLSTERLTSNK
AFTNKLWNAGKFVLQNLPSQSDTSAWEHILACKFDKEESLLSLPLPECWVVSKLHELIDSVTTSYDKYFF
GDVGREIYDFFWSDFADWYIEASKTRLYHSGDNSALSRAQAVLLYVFENILKLLHPFMPFVTEELWQALP
YRKEALIVSPWPQTSLPKDLKSIKRFENLQSLTRAIRNARAEYSVEPAKRISASIVASAEVIEYISKEKE
VLALLSRLDLQNVHFTDSPPGDANQSVHLVASEGLEAYLPLADMVDISAEVERLSKRLSKMQTEYDALAA
RLSSPKFVEKAPEDVVRGVREKAAEAEEKIKLTKNRLAFLKSTSLVSQ
>gnl|CDD|178531 PLN02945, PLN02945, nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
MDVPLPTEKLSCGANSTGPRTRVVLVATGSFNPPTYMHLRMFELARDALMSEGYHVLGGYMSPVNDAYKK
KGLASAEHRIQMCQLACEDSDFIMVDPWEARQSTYQRTLTVLARVETSLNNNGLASEESVRVMLLCGSDL
LESFSTPGVWIPDQVRTICRDYGVVCIRREGQDVEKLVSQDEILNENRGNILVVDDLVPNSISSTRVREC
ISRGLSVKYLTPDGVIDYIKEHGLYM
>gnl|CDD|178532 PLN02946, PLN02946, cysteine-tRNA ligase
LNLAKSCRPLTPLRLSSPPRSQLRIAFPLRPPKERQYRSCFFSASALASNGAPASRGRELHLYNTMSRKK
ELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANELG
EDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFPEYG
KLSGRKLEDNRAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDI
HGGGMDLVFPHHENEIAQSCAACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFL
LGTHYRSPINYSDVQLESASERIFYIYQTLHDCEESLQQHDSTFEKDSVPPDTLNCINKFHDEFVTSMSD
DLHTPVALAALSEPLKTINDLLHTRKGKKQEKRLESLAALEKKIRDVLSVLGLMPTSYSEALQQLREKAL
RRAKLTEEQVLQKIEERTVARKNKEYEKSDAIRKDLAAVGIALMDSPDGTTWRPAIPLALQEQVAAT
>gnl|CDD|215510 PLN02947, PLN02947, oxidoreductase
MSPAMAAEVAEEANIEEDDESSKYQKGVKHLCDSGITKVPAKYILPASDRPGLTRDEAIAASGNLKLPVI
DLAELRGSNRPHVLATLAAACREYGFFQVVNHGVPSEVIGGMIDVARRFFELPLEERAKYMSADMRAPVR
YGTSFNQNKDAVFCWRDFLKLVCHPLSDVLPHWPSSPADLRKVAATYAKATKRLFLELMEAILESLGIVK
RGSDELLEEFEAGSQMMVVNCYPACPEPELTLGMPPHSDYGFLTLLLQDEVEGLQIMHAGRWVTVEPIPG
SFVVNVGDHLEIFSNGRYKSVLHRVRVNSTKPRISVASLHSLPFERVVGPAPELVDEQNPRRYMDTDFAT
FLAYLASAEGKHKNFLESRKLITI
>gnl|CDD|178534 PLN02948, PLN02948, phosphoribosylaminoimidazole carboxylase
ASHDASPSSENRSVKPVHGVSETVVGVLGGGQLGRMLCQAASQMGIKVKVLDPLEDCPASSVAARHVVGS
FDDRAAVREFAKRCDVLTVEIEHVDVDTLEALEKQGVDVQPKSSTIRIIQDKYAQKVHFSKHGIPLPEFM
EIDDLESAEKAGDLFGYPLMLKSRRLAYDGRGNAVAKTEEDLSSAVAALGGFERGLYAEKWAPFVKELAV
MVARSRDGSTRCYPVVETIHKDNICHVVEAPANVPWKVAKLATDVAEKAVGSLEGAGVFGVELFLLKDGQ
ILLNEVAPRPHNSGHYTIEACYTSQFEQHLRAVLGLPLGDTSMKVPAAIMYNILGEDEGEAGFRLAHQLM
GRALNIPGASVHWYGKPEMRKQRKMGHITVVGPSAAEVEARLDQLLAEESADPDALPKGTPLVGIIMGSD
SDLPTMKDAAEILDSFGVPYEVTIVSAHRTPERMFSYARSAHSRGLQVIIAGAGGAAHLPGMVASMTPLP
VIGVPVKTSHLDGLDSLLSIVQMPRGVPVATVAIGNATNAGLLAVRMLGASDPDLLDKMEAYQEDMRDMV
LEKAEKLEELGWEEYLN
>gnl|CDD|215511 PLN02949, PLN02949, transferase, transferring glycosyl groups
MAIWLILYHLLTSIVLLLVAIALSVLRARRSRKRAVGFFHPYTNDGGGGERVLWCAVRAIQEENPDLDCV
IYTGDHDASPDSLAARARDRFGVELLSPPKVVHLRKRKWIEEETYPRFTMIGQSLGSVYLAWEALCKFTP
LYFFDTSGYAFTYPLARLFGCKVVCYTHYPTISSDMISRVRDRSSMYNNDASIARSFWLSTCKILYYRAF
AWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPERIKRVYPPCDTSGLQALPLERSEDPPYIISVAQFRPE
KAHALQLEAFALALEKLDADVPRPKLQFVGSCRNKEDEERLQKLKDRAKELGLDGDVEFHKNVSYRDLVR
LLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVLDEDGQQTGFLATTVEEYADAILEVL
RMRETERLEIAAAARKRANRFSEQRFNEDFKDAIRPILNSASR
>gnl|CDD|215512 PLN02950, PLN02950, 4-alpha-glucanotransferase
SGKKSLKSVTLSFRIPYYTQWGQSLLVCGSEPLLGSWNVKKGLLLSPVHQGDELVWEGSVSVPEGFSCEY
SYYVVDDNKNVLRWEAGKKRKLVLPEGLQGGELVELHDLWQKSGPEALFFRSAFKDVIFRHSWGVNTERP
LGALNKPPAPDEIVVRFKIACPRLEEGTSVYVTGSIAQLGNWQVDDGLKLNYTGDSIWEADCLVPKSDFP
IKYKYALQTAEGLVSLELGVNRELSLDSSSGKPPSYIVASDGAFREMPWRGAGVAVPVFSIRSEEDVGVG
EFLDLKLLVDWAVKSGLHLVQLLPVNDTSVHGMWWDSYPYSSLSVFALHPLYLRVQALSERLPEDLKAEI
QKARKQLDKKDVDYEATLATKLSIAKKVFDLEKDLTLNSSSFKKFFSENEHWLKPYAAFCFLRDFFETSD
HSQWGRFSDFSDEKLEKLVSPGSLHYDTICFHYYIQYHLHSQLSEAAEYARKKGVVLKGDLPIGVDRNSV
DTWVYPNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFF
RIWELPAHAVTGLVGKFRPSIPLSQEELEQEGIWDFDRLSRPYIRQEFLQEKFGDRWTEIASNFLNEYQK
GCYEFKEDCNTEKKIAAKLKRLAEKSWLLEEEEKIRRGLFDLLQNVVLIRDPEDPRKFYPRFNLEDTSSF
QDLDDHSKNVLKRLYYDYYFHRQEDLWRENALKTLPALLNSSDMLACGEDLGLVPACVHPVMQELGLLGL
RIQRMPSEPGLEFGIPSQYSYMTVCAPSCHDCSTLRAWWEEDEERRERFYKHVLGSDGPPPSQCVPDVAH
FILQQHVEAPSMWAIFPLQDLLALKEEYTTRPANEETINDPTNPKHYWRFRVHVTLESLLADKDLLATI
>gnl|CDD|215513 PLN02951, PLN02951, Molybderin biosynthesis protein CNX2
LSKLADLRLGFRSSSFQLQEPGSSIFSASSSYAADQVDPEASNPVSDMLVDSFGRRHNYLRISLTERCNL
RCQYCMPEEGVELTPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLA
MTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKVNCVVMR
GFNDDEICDFVELTRDKPINVRFIEFMPFDGNVWNVKKLVPYAEMMDRIEQRFPSLKRLQDHPTDTAKNF
RIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALRSGADDDELREIIGAAVKRK
KAAHAGMFDLAKTANRPMIHIGG
>gnl|CDD|178538 PLN02952, PLN02952, phosphoinositide phospholipase C
MGKEKKTESYNNDSGSYNYKMFNLFNRKFKITEAEPPDDVKDVFCKFSVGGGHMGADQLRRFLVLHQDEL
DCTLAEAQRIVEEVINRRHHVTRYTRHGLNLDDFFHFLLYDDLNGPITPQVHHDMTAPLSHYFIYTGHNS
YLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGSTKDEILVLHGRTLTTPVPLIKCLKSIRDYAFSSSP
YPVIITLEDHLTPDLQAKVAEMATQIFGQMLYYPESDSLVQFPSPESLKHRIIISTKPPKEYLESSGPIV
IKKKNNVSPSGRNSSEETEEAQTLESMLFEQEADSRSDSDQDDNKSGELQKPAYKRLITIHAGKPKGTLK
DAMKVAVDKVRRLSLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFN
MQGYGKSLWLMHGMFRANGGCGYLKKPDFLMKKGFHDEVFDPKKKLPVKKTLKVKVYLGDGWRLDFSHTH
FDSYSPPDFYTKMYIVGVPADNAKKKTKIIEDNWYPAWNEEFSFPLTVPELALLRIEVREYDMSEKDDFG
GQTCLPVSELRPGIRSVPLHDKKGEKLKNVRLLMRFIFV
>gnl|CDD|178539 PLN02953, PLN02953, phosphatidate cytidylyltransferase
MASFAELVLSTSRCTCPCRSFSKKPLILPPLSGLRLVGGDTKPLFRSGLGPISVKRRFLTAVARAESDQL
GDDDHAKEIDRIHDLQNVEDKQKKASQLKKRVIFGIGIGLPVGCVVLAGGWFFTVALAASVFIGSREYFE
LVRSRGIAKGMTPPPRYVSRVCSVICALMPILTLYFGNIDILVTSAAFLVAIALLVQRGSPRFAQLSSTM
FGLFYCGYLPCFWVKLRCGLAAPALNTGKLSPFISLKFSIGKTWPILLGGQAHWTVGLVATLISFSGVIA
TDTFAFLGGKAFGRTPLTSISPKKTWEGTFVGLVGCIAITILLSKSLSWPQSLFSSIAFGFLNFFGSVFG
DLTESMIKRDAGVKDSGSLIPGHGGILDRVDSYIFTGALAYSFIKTSLKLYGV
>gnl|CDD|215514 PLN02954, PLN02954, phosphoserine phosphatase
PSKDVLELWRSADAVCFDVDSTVCVDEGIDELAEFCGAGEAVAEWTAKAMGGSVPFEEALAARLSLFKPS
LSQVEEFLEKRPPRLSPGIPELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIPPENIFANQILFGDSGE
YAGFDENEPTSRSGGKAEAVQHIKKKHGYKTMVMIGDGATDLEARKPGGADLFIGYGGVQVREAVAAKAD
WFVTDFQDLIEVLD
>gnl|CDD|178541 PLN02955, PLN02955, 8-amino-7-oxononanoate synthase
MADHSWDKWVEEAVNVLESRQILRSLRPICMSRQNEEEIVKSRANGGDDYEVFDGLCQWDRTSVEVSVSI
PTFQKWLHDIPSNGEEIFSGDALAEERKGRFKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSA
LICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIGSVASLLAASGKPLKNEKVAIFSDALNH
ASIIDGVRLAERQGNVEVFVYRHCDMYHLNSLLSSCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGF
LLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTA
IPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFKALSGVDISSPIISLVVGNQEKALKASRYLLKSGFHV
MAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLDFDNTATYIPSFLFPKL
>gnl|CDD|215515 PLN02956, PLN02956, PSII-Q subunit
MALRLAVQALSATHLSPAFICCLKPTFPSKGNTSRRPLRSISRRRGALAAVAGVLLAQLEASFNVAIAFG
FDLRLTAPERTVEEAESGVRGHAENLLRVKALIESESWKEAQKALRRSASNLKQDLYAIIQAKPGKDRPQ
LRRLYSDLFNSVTKLDYAARDKDETRVWEYYENIVASLDDIFSRI
>gnl|CDD|215516 PLN02957, PLN02957, copper, zinc superoxide dismutase
GALPELLTEFMVDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARLI
GQGDPEDFLVSAAVAEFKGPDIFGVVRFAQVSMELARIEAAFSGLSPGTHGWSINEYGDLTRGAASTGKV
YNPSDDDTDEEPLGDLGTLEADENGEATFSGTKEKLKVWDLIGRSLAVYATADKSGPGIAAAVIARSAGV
GENYKKLCSCDGTVIWESTNSDFVASKV
>gnl|CDD|215517 PLN02958, PLN02958, diacylglycerol kinase/D-erythro-sphingosine kinase
ENDELPSPAIISDRVLVNGVLTPLTLTAEGKLRWTDSGQRCLTVEKEVLGFVIEGSKIRVKTIVEKGGGI
CCRGSAGALARKDFVFEPLSDESRRLWCQKLRDYLDSLGRPKRLLVFVNPFGGKKSASKIFFDVVKPLLE
DADIQLTIQETKYQLHAKEVVRTMDLSKYDGIVCVSGDGILVEVVNGLLEREDWKTAIKLPIGMVPAGTG
NGMAKSLLDSVGEPCSATNAVLAIIRGHKCSLDVATILQGETKFFSVLMLAWGLVADIDIESEKYRWMGS
ARLDFYGLQRILCLRQYNGRISFVPAPGFEAYGEPTSYNGESTSKEESGKDKQHGYQGPDVKLENLDWRT
IKGPFVSVWLHNVPWGGEDTLAAPDAKFSDGYLDLILIKDCPKLALLALMTKLSDGTHVKSPYVMYLKVK
AFVLEPGPRTDDPTKGGIIDSDGEVLARGNGSYKCDQKALMSYDKLQISVDQGLATLFSPV
>gnl|CDD|215518 PLN02959, PLN02959, aminoacyl-tRNA ligase
MMAEGGKSTARRDRLLEIEVAVQKWWEEEKVFEAEAGDEPPKPGEKFFGNFPYPYMNGLLHLGHAFSLSK
LEFAAAYHRLRGANVLLPFAFHCTGMPIKASADKLAREIQQYGNPPVFPEEDEDEAAAVAAAKAEAEAAA
APPDKFKGKKSKAVAKSGTQKYQWEIMRSFGLPDSEIAKFQDPYHWLSYFPPLAKEDLKAFGLGCDWRRS
FITTDVNPYYDAFVRWQFRKLKKKGKIVKDKRYTIYSPLDGQPCADHDRASGEGVGPQEYVLIKMEVLPP
FPGKLKALEGKKVFLAAATLRPETMYGQTNCWVLPDGKYGAYEINDTEVFILTARAALNLAYQNFSKVPG
KPTCLVELTGYDLIGLPLKSPLAFNEVIYALPMLTILTDKGTGVVTSVPSDSPDDYMALSDLKAKPALRA
KYGVKDEWVLPFEVVPIINIPEFGDKSAEKVCEDLKIKSQNDKEKLAEAKRLTYLKGFTDGTMLVGEYAG
RKVQEAKPLIKKKLIEAGQAILYSEPEKKVMSRSGDECVVALTDQWYLTYGEEEWKKKAEKCLSKMNLYS
DETRHGFEHTLGWLNQWACSRSFGLGTRIPWDEQFLIESLSDSTIYMAYYTVAHLLQGGDMYGKDKSSIK
PEQMTDEVWDFVFCGGPLPKSSDIPAELLEKMKQEFEYWYPFDLRVSGKDLIQNHLTFAIYNHTAIWAEE
HWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFALADAGDGVDDANFVFETANAAILRLT
KEIAWMEEVLAAESSLRTGPPSTYADRVFENEINIAIAETEKNYEAMMFREALKSGFYDLQAARDEYRLS
CGSGGMNRDLVWRFMDVQTRLITPICPHYAEHVWREILKKEGFAVTAGWPVAGEPDLTLKRANKYLQDSI
VSFRKLLQKQLAGSKKAKKGGAPVTLPEKKLAGLIYVAEKYDGWKEECLRILQSKFDSQSRTFAPDAEIL
EALKESSVGQEANFKQVQKLCMPFVKFKKDEAIAVGPQALDLKLPFDEIEVLQENLELIKRQLGLEEVEI
LSASDPDAVAKAGAHASLLKQNPPSPGNPVAIFV
>gnl|CDD|215519 PLN02960, PLN02960, alpha-amylase
MVSLSLFLRFPRPPNPLVHAEPRRLGASRVNLPRKIGFKITCFAAPRPRQPKQKKKRQQEPGSDAEAGVD
PVGFLTRLGISDRAFAQFLRERHKALKDLKWEIFKRHIDLKEFASGFELLGMHRHPEHRVDFMEWAPGAR
YCSLVGDFNNWSPTENRAREGYFGHDDFGYWFIILEDKLREGEEPDELYFQEYNYVDDYDKGDSGIDIEE
LFQKMNDEYWEPGEDRFIKNRLEVPAKLYEQMFGPNGPQTLEELGDIPDAETRYKEWKKEHKDDDPSNLP
PLDIIDTGQPYDIFNVVTDPVWREKFLEKKPPLPYWEETRKGRKAWLKKYIPAIPHGSKYRVYFNTPDGP
LERVPAWATYVLPDPDGKQWYAIHWEPPPEEAYKWKFERPKVPKSLRIYECHVGISGSEPKISSFKEFTQ
KVLPHVKKAGYNAIQLIGVQEHKDYSSVGYKVTNFFAVSSRFGTPDDFKRLVDEAHGLGLLVFLDIVHSY
AAADEMVGLSLFDGSNDCYFHSGKRGHHKRWGTRMFKYGDHEVLHFLLSNLNWWVTEYRVDGFQFHSLGS
MLYTHNGFASFTGDLDEYCNQYVDRDALIYLILANEMLHQLHPNIITIAEDATFYPGLCEPTSQGGLGFD
YYVNLSPSEMWLSLLENVPDQEWSMSKIVSTLVKNKENADKMLSYAENHNQSISGGKSFAEILLGKNKES
SPAVKELLLRGVSLHKMIRLITFTLGGSAYLNFMGNEFGHPERVEFPRASNNFSFSLANRRWDLLEDGVH
AHLFSFDKALMALDEKYLILSRGLPNIHHVNDTSMVISFTRGPLLFAFNFHPTNSYEEYEVGVEEAGEYE
LILNTDEVKYGGQGRLTEDQYLQRTKSKRIDGLRNCLELTLPSRSAQVYKLARILRI
>gnl|CDD|178546 PLN02961, PLN02961, alanine-tRNA ligase
GRIALVLDRTIFHPQGGGQPSDTGRIVISGGDTKFSVQDVRRKDGVVYHYGVFEGSNPESASPFEAGDEV
TVTVDESRRKLHSRLHSAGHLLDVCMARVGLGPLEPGKGYHFPDGPFVEYKGKIPQGELDSKQDELEAEA
NELIAEGGKVSAAVLPYDEAAELCGGSLPDYIAKDSTPRIVKIGDSPGCPCGGTHVADVSEITSVKVTQI
RVKKGVTRVSYTI
>gnl|CDD|178547 PLN02962, PLN02962, hydroxyacylglutathione hydrolase
SSSSSSSSSKLLFRQLFEKESSTYTYLLADVSHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHV
HADHVTGTGLLKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPDQ
PQPRMAFTGDALLIRGCGRTDFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPR
LTKDEETFKTIMENLNLPYPKMIDVAVPANMVCGLQDPPAK
>gnl|CDD|215520 PLN02964, PLN02964, phosphatidylserine decarboxylase
MGNGNSREAKESRRSKLRQKLQKFRIRRRHLRCSRGSSSGSVSQRAVSAEDFSGIALLTLVGAEMKFKDK
WLACVSFGEQTFRTETSDSTDKPVWNSEKKLLLEKNGPHLARISVFETNRLSKNTLVGYCELDLFDFVTQ
EPESACESFDLLDPSSSNKVVGSIFVSCSIEDPVETERSFARRILAIVDYDEDGQLSFSEFSDLIKAFGN
LVAANKKEELFKAADLNGDGVVTIDELAALLALQQEQEPIINNCPVCGEALGVSDKLNAMIHMTLCFDEG
TGNQVMTGGFLTDKQASYGWMFKLSEWAHLSTYDVGLNTGSSASHILVFDRKSKRLVEELIDSKIVLSMR
AIYQSKIGLRLMDQGAKEILQRLSEKQGKKMNSVESAQDIPKFLEFFKDQINMDEVKYPLEHFKTFNEFF
IRELKPGARPIACMDNDDVAVCAADCRLMAFQSVDDSTRFWIKGRKFSIKGLLGKKVHSDAFLDGSLVIF
RLAPQDYHRFHVPVSGVIEKFVDVPGSLYTVNPIAVNSKYCNVFTENKRAVCIISTAEFGKVAFVAIGAT
MVGSITFVKKEGDHVKKGDELGYFSFGGSTVICVFEKDAIDIDEDLLANSERSLETLVSVGMTLGVSTRT
FARQVLEKSRPTIR
>gnl|CDD|178549 PLN02965, PLN02965, Probable pheophorbidase
MPEIHFVFVHGASHGAWCWYKLATLLDAAGFKSTCVDLTGAGISLTDSNTVSSSDQYNRPLFALLSDLPP
DHKVILVGHSIGGGSVTEALCKFTDKISMAIYVAAAMVKPGSIISPRLKNVMEGTEKIWDYTFGEGPDKP
PTGIMMKPEFVRHYYYNQSPLEDYTLSSKLLRPAPVRAFQDLDKLPPNPEAEKVPRVYIKTAKDNLFDPV
RQDVMVENWPPAQTYVLEDSDHSAFFSVPTTLFQYLLQAVSSLQR
>gnl|CDD|178550 PLN02966, PLN02966, cytochrome P450 83A1
MEDIIIGVVALAAVLLFFLYQKPKTKRYKLPPGPSPLPVIGNLLQLQKLNPQRFFAGWAKKYGPILSYRI
GSRTMVVISSAELAKELLKTQDVNFADRPPHRGHEFISYGRRDMALNHYTPYYREIRKMGMNHLFSPTRV
ATFKHVREEEARRMMDKINKAADKSEVVDISELMLTFTNSVVCRQAFGKKYNEDGEEMKRFIKILYGTQS
VLGKIFFSDFFPYCGFLDDLSGLTAYMKECFERQDTYIQEVVNETLDPKRVKPETESMIDLLMEIYKEQP
FASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGSTFVTEDDVKNL
PYFRALVKETLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWGPNPDEFRPERFLE
KEVDFKGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPNGMKPDDINMDVMTGLAMHKSQ
HLKLVPEKVNKY
>gnl|CDD|215521 PLN02967, PLN02967, kinase
MASLSFTQFLSFPRCNADVPCLLQSLGFNKFRGERWRLQNKFLLAAGSRKKIESALAVDEEPDENGAVSK
KKPTRSVKRATKKTVVEISEPLEEGSELVVNEDAALDKESKKTPRRTRRKAAAASSDVEEEKTEKKVRKR
RKVKKMDEDVEDQGSESEVSDVEESEFVTSLENESEEELDLEKDDGEDISHTYGWPPLVCCFGAAQHAFV
PSGRPANRLLDYEIHERMKDAFWAPEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLN
VNKVQTRSVCIDGKRATAVSTMKIAKRGRLKTTCVKPCAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPT
MRSTTLRAIKISKKLGGVIFYDLNLPLPLWSSSEETKSFIQEAWNLADIIEVTKQELEFLCGIEPTEEFD
TKDNDKSKFVHYSPEVVAPLWHENLKVLFVTNGTSKIHYYTKEHNGAVHGMEDAPITPFTSDMSASGDGI
VAGLMRMLTVQPHLITDKGYLEKTIKYAIDCGVIDQWLLARTRGFPPKEDMEDEVEPDPNGIRSITEKEY
RTLEPYSEPEGPYVMKPVEER
>gnl|CDD|215522 PLN02968, PLN02968, Probable N-acetyl-gamma-glutamyl-phosphate reductase
LLFADSVGSKGLASRASVTSSPQSVVSSASSSVKSEEKKRIFVLGASGYTGAEVRRLLANHPDFEITVMT
ADRKAGQSFGSVFPHLITQDLPNLVAVKDADFSDVDAVFCCLPHGTTQEIIKALPKDLKIVDLSADFRLR
DIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLPLVPLVKAGLIEPDNIII
DAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLADAAGSKVTPSFTPHLMPMSRGMQST
VYVHYAPGVTAEDLHQHLKERYEGEEFVKVLERGAVPHTDHVRGSNYCELNVFADRIPGRAIIISVIDNL
VKGASGQAVQNLNLMMGLPETTGLLQQPLFP
>gnl|CDD|215523 PLN02969, PLN02969, 9-cis-epoxycarotenoid dioxygenase
PSHPIPTKFPPPLKLPPIHHHPSPPPLAPPRAISISTPDSTALARTGTEDDSTSAAFWDYQFLFVSQRSE
TKDPVRLRVVEGAIPSDFPSGTYYLAGPGLFTDDHGSTVHPLDGHGYLRAFHIDGGDRPVQYSARYVKTE
AKKEEHDPETRTWRFTYRGPFSVLKGGKRVGNVKVMKNVANTSVLKWGGRLLCLWEGGEPYEIDSGTLET
IGRFDLAPDDDSSKDDRLQGSDAWDLAARLLKPILTGVFKMPKKRLLSHYKIDGRRNRLLVVTCNAEDML
LPRSNFTFYEFDADFKLVQRKEFKLDDHLMIHDWAFTDTHYVLLANRVKLDVPGSLLAMAGLSPMISALA
VDPSRPSSPVYLLPRFPEKEAGGRDWRVPVEVPSQLWLIHVGNAYEERDDRGNLRIQLHASACSYQWFSF
HRMFGYDWQNKKLDPSVMNNAKGKELLPHLVQVSIDLDRTGDCRSCDVEPLSNQWEKPADFPVINPSFSG
QKNEYTYAAAASGSRKTLPHFPFDSVVKLDVPDGSARSWSTGARRFVGEPVFVPRKSSQGGGEEDDGYVL
VVEYAVSDERCYLVILDAKRIGERDAVVAKLEVPKHLTFPMGFHGFWADE
>gnl|CDD|215524 PLN02970, PLN02970, serine racemase
EAASEKYAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLS
DDQAEKGVVTHSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAAR
VQQETGAVLIHPYNDGRVISGQGTIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEP
KGADDAAQSKAAGEIITLPVTNTIADGLRASLGDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVV
EPSGAIGLAAALSDSFRSNPAWKGCKNVGIVLSGGNVDLGVLWESFSK
>gnl|CDD|166612 PLN02971, PLN02971, tryptophan N-hydroxylase
MDTLASNSSDLTTKSSPGTSSFTNMYLLTTLQALVAITLLMILKKLKSSSRNKKLHPLPPGPTGFPIVGM
IPAMLKNRPVFRWLHSLMKELNTEIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNG
YKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGN
AIKRLMFGTRTFSEKTEPDGGPTLEDIEHMDAMFEGLGFTFAFCISDYLPMLTGLDLNGHEKIMRESSAI
MDKYHDPIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWA
MAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGY
HIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCAAPALGTAITT
MMLARLLQGFKWKLAGSETRVELMESSHDMFLSKPLVMVGELRLSEDLYPTVK
>gnl|CDD|215525 PLN02972, PLN02972, Histidyl-tRNA synthetase
EAAESAVITLGGKGSSLTSASVYALATGVAQPRIDSSATCLARVVDAVAALSCEAAKADVAAFDVLDSGD
GLSDKDEADVAGDMKVLLNGSKLVGKAQAEVFSKIPKINGIFREAVKAVHAVVRIELNSPVKLGKRDAIQ
TGEGLARAVQALGKLSVARAKLCLEVIGDEELRKKLTSGVVLDNLYGLLLKVSIEEDAVSFLHGVNNLLG
IVWDIVAWEAAAAFAVLEGGELIEKPQAEAENEAGKSDKKDKKSKKKKVLGKGTSAVLQLIKDRVTNGGG
VSSDSLQVLAEWATQLLLLFDPKCPGFDSLVDKVKEIVESNEVRRLPKIPKGTRDFAKEQMAIREKAFSI
ITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKR
YQIAKVYRRDNPSKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGML
EICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPPLELLSKLRQEGSEF
LGNASSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGAQVGSIAAGGRYDNLVG
MFSGKQVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAEY
KVSTRKAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELLKL
>gnl|CDD|178556 PLN02973, PLN02973, beta-fructofuranosidase
MSSFNLSVDVNQNGNIKNVDSLSTLDDIDDIDFAKLLEKPRPLNIDRLRSLDERSLTELTGSPQLRNADN
ASRAPDHADYVISPSFGRRSGFNTPRSQPGFESHPMVGEAWDALRRSMVYFRGQPVGTIAAVDNSEEKLN
YDQVFVRDFVPSALAFLMNGEPDIVKNFLLKTLRLQSWEKKIDRFQLGEGVMPASFKVFHDPVRNHETLI
ADFGESAIGRVAPVDSGFWWIILLRAYTKSTGDSSLADMPECQKGIRLILSLCLSEGFDTFPTLLCADGC
CMIDRRMGVYGYPIEIQALFFMALRCALLLLKHDGEGKEMVEQIVKRLHALSYHMRSYFWLDLKQLNDIY
RYKTEEYSHTAVNKFNVIPDSLPEWVFDFMPPHGGFFIGNVSPARMDFRWFALGNCIAILSSLATPEQST
AIMDLIESRWEELVGEMPLKVCYPAIESHEWRIVTGCDPKNTRWSYHNGGSWPVLLWLLTAACIKTGRPQ
IARRAIEVAEARLHKDHWPEYYDGKVGRYVGKQSRKNQTWSVAGYLVAKMMLEDPSHVGMVCLEEDKQMK
PVMRRSNSWTC
>gnl|CDD|215526 PLN02974, PLN02974, adenosylmethionine-8-amino-7-oxononanoate transaminase
LHMLRSLIGLRRRSSSSSAAGALPLSCPAFAVWGANTAVGKTLVSAGLAAAAASRRSPVLYVKPVQTGFP
DDSDARFVFRKADSLSRRSESLFASNRTLFLSPPAAKSALGGVSSMGAHAAVNAGAEAGVTSSALWCHTL
FAWRRAVSPHLAARREGRGVSDDEVLEAVNRSLREVGANESGGGRVLALVETAGGVASPGPSGTLQCDLY
RPLRLPAILVGDGRLGGISATLAAYESLLLRGYDVVAVVIEDHGLSNEKALLSYLSNRVPVFVLPPVPED
PGDDLDEWFDDSKSTFDALLDALQSWHSGRLQRLQSMPKEAGEVLWWPFTQHALVPRDSVTVIDSRCGED
FSVYKPKTNSTCSIVQQFDACASWWTQGPDPTLQPELARAVAYAAGRYGHVMFPENVHEPALRAAELLLG
GPGKGWASRVFFSDNGSTAIEVALKMAFRKFIVDHGFLENSGNEKRGGDLIELKVLALDGSYHGDTLGAM
EAQAPSVFTGFLQQPWYSGRGLFLDPPTVGMRNGRWNISLPEGFSSGLEGEETTWESRDEVFDKTRDSTP
LAKAYRSYIEQQLDEYEASAKNGHIAALIIEPVLHGAGGMLLIDPLFQRALVQVCRSRKIPVIFDEVFTG
LWRLGVESAWELLGCKPDIACYAKLLTGGLVPLAATLATEEVFEAFRGPSKLDALLHGHSYTAHPMGCAA
AAKALQWYKDPSTNPNLIPPGSRLRELWDEELVRAISSLPNVERVVSLGTVLALELDAEGSGSGYSSLYA
RSVVRRLRREDGIYARPLGNVVYLMCGPTTSPETCTRLLRKVYRRLS
>gnl|CDD|166616 PLN02975, PLN02975, complex I subunit
DITASDKPEYPVVDRNPTFTKVVGNFSALDYLRFATITGVSVTVGYLSGIKPGIRGPSMVTGGLIGLMGG
FMYAYQNSAGRLMGFFPNEGEVARYQK
>gnl|CDD|215527 PLN02976, PLN02976, amine oxidase
MKDKERKSGSKRGLKVIQIGDDSDDDEPIGSLFKLKRPKNSKKVKVGLESTGKREEKLSALDEDSEGMDD
TLASFRKRLKGPKKGVGSVSARMSQGALLENQEEVDTVLNEGSKRSLDGNLEDSLSAFLREAQAGLSRKS
CANSCGKQLNRVQGLEAGLSPGSEKVKTVSNEREGNGFHQISYHTEEAEDGISEVAATKDRVSKSSDDRH
GESSEVNHPALESHSGVIEDENMVDPSIAPTQEEPLGEPCSEDRICDKKGLVLCSCGKQPTFEIKSALSQ
QSKGVSTKCISSAEQQASVSSDNKETSSTEVHKANFTMQMNHNGGSLEVNTLEDSPSHDIVGSHPVCNGA
SPVSITPEENESYVEDAVSLPDSEIKDGKLSKLQRVTRKAKKRKLGDMAYEGDADWETLINEQGFLENPS
ACDSDRSFKTRDKSDSSSVSKEGENGGAAAVSAGLKARAVGPIEKIKFKEVLKRKGGLQEYLECRNMILG
LWSKDVSRILPLADCGVTDTPSEDESPRASLIREVYLFLDQRGYINAGIASEKEKAEPSTNHNYKLVEEK
TLEESSGASVADSEDGVSFILGQVKSSESSTEGKDCVLVDDENDASGDLPNVCECSELLASDIQQCGASN
EKLNNGLVSLDALSASPSSSVLDSPETLSVIKPELRNELQSVQSNSCIEMGGNHCVLCDSVDRKKIIVVG
AGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDRSSLSVPVDLGASIITGVEADVATERRPDPSSLIC
AQLGLELTVLNSDCPLYDVVTGEKVPADLDEALEAEYNSLLDDMVLLVAQKGEHAMKMSLEDGLEYALKR
RRMPRPGVDIDETELGNAADDLYDSASTGVDGGHCEKESKEDVLSPLERRVMNWHFAHLEYGCAALLKEV
SLPYWNQDDVYGGFGGAHCMIKGGYSNVVESLAEGLDIHLNHVVTDVSYGSKDAGASGSSRKKVKVSTSN
GSEFLGDAVLITVPLGCLKAETIKFSPPLPDWKYSSIQRLGFGVLNKVVLEFPEVFWDDSVDYFGATAEE
TDLRGQCFMFWNVKKTVGAPVLIALVVGKAAIDGQSMSSSDHVNHALMVLRKLFGEALVPDPVASVVTDW
GRDPFSYGAYSYVAIGASGEDYDILGRPVENCLFFAGEATCKEHPDTVGGAMMSGLREAVRIIDILNTGN
DYTAEVEALETAQRHSESERDEVRDITKRLEAVELSNVLYKNSLDADPILTREALLQEMFFSAKTTAGRL
HLAKELLNLPVETLKSFAGTKEGLATLNSWILDSMGKDGTQLLRHCVRLLVLVSTDLLAVRLSGIGKTVK
EKVCVHTSRDIRAIASQLVSVWLEVFRREKASNGGLKLLRQATANESSKRRKLNSPSTDTKGKLSSLENV
KTDKSKSESLKSVGRQDIEEEEGNQIPMSEEEKAAFAAAEAARAAAEAAAQAYAEAKHNTSLQLPKIPSF
HKFARREQYMDESDLRKKWSGGVLGRQDCISEIDSRNCKVRDWSDAACVDLDSSRISVDNYSQQSHSNEI
ACHSNESAAVDSSLFTRAWVDTAGSDGIKDYHAIERWQSQAAAADSEFFNRTRHIKDEEDSHDQRANESS
VSQVTVNKEPHKNHIRGAERIKQGVVDFVASLLMPLYRAKKIDREGYKSIMKKTATKVMEQATDVEKAMA
VSEFLDSKRKNKIRSFVDKLVDKHMAMVPVPKP
>gnl|CDD|215528 PLN02977, PLN02977, glutathione synthetase
EAPIIDVPGLTKELLQDLVEEALVWSSLHGLVVGDRSDQRSGTVPGVGLVHAPISLLPTPFPRAAFKQAC
ELAPLFNELVDRVSRDGEFLQETLARTRKVDEFTSRLLDIHEKMGERNKREDIRLGLHRSDYMLDEPTGL
LLQVELNTISSSFPGLSSLVSQLHRSLLSRYGRVLGLDPERVPENPALEQFADALAAAWKEFGNPSAVVL
MVVQPEERNMYDQRWLSFALWERHGIRTIRKTLAEIAAEGSLDEDGTLTVDGQPVAVVYFRAGYAPTDYP
SEAEWRARLLLERSSAVKCPSIAYHLAGTKKVQQELAKPGVLERFLDDKEDIAKLRKCFAGLWSLDDEAA
AEIVKLAIEKPELFVLKPQREGGGNNIYGDDLRETLERLQKEGGEDLAAYILMQRIFPPVSRTYLVRNGV
CEEGETISELGIYGAYLRNGDKVIINEQSGYLLRTKAASSDEGGVAAGFAVLDSPYLT
>gnl|CDD|215529 PLN02978, PLN02978, pyridoxal kinase
MAPPVLSLALPSSTGRVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGE
QLWALIEGLEANGLLFYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGKLYVPPELVP
VYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDIDGKLLLVGSHRKEK
GARPEQFKIVIPKIPAYFTGTGDLMAALLLGWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKRAGADPK
SSSLELRLVQSQDDIRHPQVRFKAERYS
>gnl|CDD|166620 PLN02979, PLN02979, glycolate oxidase
MDQSRECKRFCKDPMHFSFLFVRQEILFTIGFFKRCDALLGGFCDFRPRILIDVSKIDMTTTVLGFKISM
PIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQLV
RRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLGKMDEANDSGLASYVAGQIDRTL
SWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIP
VFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISR
NHITTEWDTPRPSARL
>gnl|CDD|215530 PLN02980, PLN02980, 2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
ELEVNLDDDLVVEVCITRTLPPALTLELGLESLKEAVNELKLNPPASSSGVLRFQVAVPPSAKALKWFCS
QPTSSDVFPVFFLSKETTEPSYKSLYVKRPHGVFGIGNAICFVHSSSLDSNGHSMIRRYLSSESAMVTAY
GFMDINFNKESSSVNSKAGSFYFFVPQIELDEHEEVSILSATLAWDDSLSYTFEQAISSYESSIYQVSSH
FWPTAEDHWFKLLKSSLAKASVEEIHPAELVYMGFFTLSGRDQAAVKELKSIQSSCQFHCRLSPDVVFSS
NMLDHEGEVSNFLKDYANINAVWASLIIEECTRLGLTYFCVAPGSRSSPLAIAASNHPLTTCIACFDERS
LAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLTADRPPELQDAGANQAINQVNHFG
SFVRFFFNLPPPTDLIPARMVLTTLDSAVHWATSSPCGPVHINCPFREPLDGSPTNWMSSCLKGLDMWMS
NAEPFTKYIQMQSSKADGDTTGQITEVLEVIQEAKRGLLLIGAIHTEDDIWAALLLAKHLMWPVVADILS
GLRLRKLFKSFPEFELNILFVDHLDHALLSDSVRNWIQFDVVIQIGSRITSKRVSQMLEKCFPFSYILVD
KHPCRHDPSHLVTHRVQSNIVQFADCLLKAQFPRRRSKWHGHLQALDGMVAQEISFQIHAESSLTEPYVA
HVISEALTSDSALFIGNSMAIRDADMYGCSSENYSSRIVDMMLSAELPCQWIQVAGNRGASGIDGLLSTA
IGFAVGCNKRVLCVVGDISFLHDTNGLSILSQRIARKPMTILVINNHGGAIFSLLPIAKRTEPRVLNQYF
YTSHDISIENLCLAHGVRHLHVGTKSELEDALFTSQVEQMDCVVEVESSIDANAAFHSTLRKFACQAAEH
ALGILSESSCLHSIIDGVFLCKISGMEYSLYRIQLCAPPTSASVDFSQFHREGFILSLSLEDGSVGFGEV
APLEIHEEDLLDVEEQLRFLLHVIKGAKISFMLPLLKGSFSSWIWSELGIPPSSIFPSVRCGLEMAILNA
IAVRHGSSLLNILDPYQKDENGSEQSHSVQICALLDSNGSPLEVAYVARKLVEEGFSAIKLKVGRRVSPI
QDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPVQDEDDLIKFCEETGLPVAL
DETIDKFEECPLRMLTKYTHPGIVAVVIKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAYIQ
FASYLEMQNAKASREMNKGTCPSVAHGLGTYRWLKEDVTMNPLGIFRSPYSGFIEASVADASRNLQKFQI
NNDVIVRTFKEEQVRTYELRVDVDGFSCLIKVHEVGQNAEGSVVLFLHGFLGTGEDWIPIMKAISGSARC
ISIDLPGHGGSKIQNHAKETQTEPTLSVELVADLLYKLIEHITPGKVTLVGYSMGARIALYMALRFSDKI
EGAVIISGSPGLKDEVARKIRSAKDDSRARMLIDHGLEIFLENWYSGELWKSLRNHPHFNKIVASRLLHK
DVPSLAKLLSDLSIGRQPSLWEDLKQCDTPLLLVVGEKDVKFKQIAQKMYREIGKSKESGNDKGKEIIEI
VEIPNCGHAVHLENPLPVIRALRKFLTRLHNSSTPGELSQKLLLA
>gnl|CDD|215531 PLN02981, PLN02981, glucosamine:fructose-6-phosphate aminotransferase
MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLESSSPLVFREEGKIESLVRSVY
EEVAETDLNLDLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGF
TFESDTDTEVIPKLAKFVFDKLNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLL
GVKELPEEKNSSAVFTSEGFLTKNRDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFEN
EKGRGGGGLSRPASVERALSTLEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLIRGGSGKAKRVLL
GGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQS
GETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQIVAMTMLALALG
EDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVKEVA
LMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDASSVCPSGG
CRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ
>gnl|CDD|215532 PLN02982, PLN02982, galactinol-raffinose galactosyltransferase/ghydrolase, hydrolyzing O-glycosyl compounds
MAPPNDSTSSISKVIESKPSPNYFDLSDGKLSVKGVPLLSDVPNNVTFTPFSSISISSDAPLPLLQRVQS
NSHKGGFLGFTKESPSDRLTNSLGKFEGRDFLSIFRFKTWWSTMWIGSSGSDLQMETQWVLLKVPEIDSY
VLIIPLIEGSFRSALHPGEDGHVMICAESGSTKVKASSFNSIAYVHVSDNPYNLMKEAYSALRVHLNTFR
LLEEKALPKIVDKFGWCTWDAFYLTVDPVGVWHGVKEFAEGGVPPRFLIIDDGWQSINFDGDNPNEDAKN
LVLGGTQMTARLYRFDECEKFRNYKGGSMLGPDPPHFDPKKPKMLIYKAIEREHAEKARKKAIESGVTDL
SEFDAKIKQLKKELDAMFDGEEKSVSSESESSGSCKVSGSGMKAFTRDLRTKFKGLDDIYVWHALCGAWG
GVRPGTTHLNAKVVPARLSPGLDGTMNDLAVDKIVEGGIGLVHPSQAGDFYDSMHSYLASVGITGVKVDV
IHTLEYVCEEYGGRVELAKAYYDGLSESLAKNFNGTGIIASMQQCNDFFFLGTKQISMGRVGDDFWFQDP
NGDPMGVYWLQGVHMIHCAYNSMWMGQIIQPDWDMFQSDHLCAEFHAGSRAICGGPVYVSDSVGGHDFDL
LKKLVFPDGTIPRCQHYALPTRDCLFKNPLFDKKTILKIWNFNKFGGVIGAFNCQGAGWDPKEHRIKGYS
ECYKPVSGSVHVSDIEWDQKPEASQMGEAEEYAVYLNQAEELLLMTPKSEAIQITLQPSSFELFSFVPVT
KLGSSAKFAPIGLTNMFNSGGTIQEMEYGESGGECSVKVKVKGGGRFLAYSSEAPKKCYLNGKEVGFEWE
EEGKLSFFVPWTEESGGISDVSFIF
>gnl|CDD|215533 PLN02983, PLN02983, biotin carboxyl carrier protein of acetyl-CoA carboxylase
MASLSVPCAKTAAAAANVGSRLSRSSFRLQPKPNISFPSKGPNPKRSAVPKVKAQLNEVAVDGSSNSAKS
DDPKSEVAPSEPKDEPPSNSSSKPNLPDEESISEFMTQVSSLVKLVDSRDIVELQLKQLDCELVIRKKEA
LPQPPPPAPVVMMQPPPPHAMPPASPPAAQPAPSAPASSPPPTPASPPPAKAPKSSHPPLKSPMAGTFYR
SPAPGEPPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPLFVIEP
>gnl|CDD|215534 PLN02984, PLN02984, oxidoreductase, 2OG-Fe(II) oxygenase family protein
MSNSESYPPEFRPLMSEIHGPAEGEEGTPVLDRSKDIDIPVIDMECLDMEKLREACKDWGIFRLENHGIP
LTLMSQLKEISESLLSLPFESKRELFGVNSPLSYFWGTPALTPSGKALSRGPQESNVNWVEGFNIPLSSL
SLLQTLSCSDPKLESFRVLMEEYGKHLTRIAVTLFEAIAKTLSLELSGDQKMSYLSESTGVIRVYRYPQC
SNEAEAPGMEVHTDSSVISILNQDEVGGLEVMKDGEWFNVKPIANTLVVNLGDMMQVISDDEYKSVLHRV
GKRNKKKERYSICYFVFPEEDCVIKSSKYKPFTYSDFEAQVQLDVKTLGSKVGLSRFKSNP
>gnl|CDD|178566 PLN02985, PLN02985, squalene monooxygenase
FTHVCLWTLLAFVLTWTVFYVTNRKKKATELADAVAEERKDGATDVIIVGAGVGGSALAYALAKDGRRVH
VIERDLREPERMMGEFMQPGGRFMLSKLGLEDCLEGIDAQKATGMAVYKDGKEAVAPFPVDNNNFPYEPS
ARSFHNGRFVQRLRQKASSLPNVRLEEGTVKSLIEEKGVIKGVTYKNSAGEETTALAPLTVVCDGCYSNL
RRSLNDNNAEVLSYQVGYISKNCRLEEPEKLHLIMSKPSFTMLYQISSTDVRCVFEVLPDNIPSIANGEM
STFVKNTIAPQVPPKLRKIFLKGIDEGAHIKVVPTKRMSATLSDKKGVIVLGDAFNMRHPAIASGMMVLL
SDILILRRLLQPLSNLGNANKVSEVIKSFYDIRKPMSATVNTLGNAFSQVLVASTDEAKEAMRQGCYDYL
CSGGFRTSGMMALLGGMNPRPLSLIYHLCAITLSSIGHLLSPFPSPLRIWHSLRLFGLALKMLVPHLKAE
GVSQMLFPANAAAYRKSYMAATAL
>gnl|CDD|178567 PLN02986, PLN02986, cinnamyl-alcohol dehydrogenase family protein
MNGGGKLVCVTGASGYIASWIVKLLLLRGYTVKATVRDLTDRKKTEHLLALDGAKERLKLFKADLLEESS
FEQAIEGCDAVFHTASPVFFTVKDPQTELIDPALKGTINVLNTCKETPSVKRVILTSSTAAVLFRQPPIE
ANDVVDETFFSDPSLCRETKNWYPLSKILAENAAWEFAKDNGIDMVVLNPGFICGPLLQPTLNFSVELIV
DFINGKNLFNNRFYRFVDVRDVALAHIKALETPSANGRYIIDGPIMSVNDIIDILRELFPDLCIADTNEE
SEMNEMICKVCVEKVKNLGVEFTPMKSSLRDTILSLKEKCLL
>gnl|CDD|166628 PLN02987, PLN02987, Cytochrome P450, family 90, subfamily A
MAFSAFLLLLSSLAAIFFLLLRRTRYRRMRLPPGSLGLPLVGETLQLISAYKTENPEPFIDERVARYGSL
FMTHLFGEPTVFSADPETNRFILQNEGKLFECSYPGSISNLLGKHSLLLMKGNLHKKMHSLTMSFANSSI
IKDHLLLDIDRLIRFNLDSWSSRVLLMEEAKKITFELTVKQLMSFDPGEWTESLRKEYVLVIEGFFSVPL
PLFSTTYRRAIQARTKVAEALTLVVMKRRKEEEEGAEKKKDMLAALLASDDGFSDEEIVDFLVALLVAGY
ETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAMKSDSYSLEWSDYKSMPFTQCVVNETLRVANIIGGIF
RRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNVFTPFGGGPRLCPG
YELARVALSVFLHRLVTRFSWVPAEQDKLVFFPTTRTQKRYPINVKRRDVAT
>gnl|CDD|178568 PLN02988, PLN02988, 3-hydroxyisobutyryl-CoA hydrolase
MAVEMASQSQVLVEEKSSVRILTLNRPKQLNALSFHMISRLLQLFLAFEEDPSVKLVILKGHGRAFCAGG
DVAAVVRDIEQGNWRLGANFFSDEYMLNYVMATYSKAQVSILNGIVMGGGAGVSVHGRFRIATENTVFAM
PETALGLFPDVGASYFLSRLPGFFGEYVGLTGARLDGAEMLACGLATHFVPSTRLTALEADLCRIGSNDP
TFASTILDAYTQHPRLKPQSAYHRLDVIDRCFSRRTVEEIISALEREATQEADGWISATIQALKKASPAS
LKISLRSIREGRLQGVGQCLIREYRMVCHVMKGEISKDFVEGCRAILVDKDKNPKWEPRRLEDMKDSMVE
QYFERVEEEEEWDDLKLPPRNNLPALAIAKL
>gnl|CDD|178569 PLN02989, PLN02989, cinnamyl-alcohol dehydrogenase family protein
MADGGKVVCVTGASGYIASWIVKLLLFRGYTINATVRDPKDRKKTDHLLALDGAKERLKLFKADLLDEGS
FELAIDGCETVFHTASPVAITVKTDPQVELINPAVNGTINVLRTCTKVSSVKRVILTSSMAAVLAPETKL
GPNDVVDETFFTNPSFAEERKQWYVLSKTLAEDAAWRFAKDNEIDLIVLNPGLVTGPILQPTLNFSVAVI
VELMKGKNPFNTTHHRFVDVRDVALAHVKALETPSANGRYIIDGPVVTIKDIENVLREFFPDLCIADRNE
DITELNSVTFNVCLDKVKSLGIIEFTPTETSLRDTVLSLKEKCLV
>gnl|CDD|215535 PLN02990, PLN02990, Probable pectinesterase/pectinesterase inhibitor
MGVDGELKKKKCIIAGVITALLVIMVVAVAIVTSRNTSHNSEKIVPVQIKTTTKAVEAVCAPTDYKETCV
NSLMKASPDSTQPLDLIKLGFNVTIRSINDSIKKASGELKAKAANDPETKGALELCEKLMNDATDDLKKC
LDNFDGFSIDQIEDFVEDLRVWLSGSIAYQQTCMDTFEEIKSNLSQDMLKIFKTSRELTSNGLAMITNIS
NLLGEFNITGLTGDLGKYARKLLSTEDGIPSWVGPNTRRLMATKGGVKANVVVAQDGSGQYKTINEALNA
VPKANQKPFVIYIKQGVYNEKVDVTKKMTHVTFIGDGPTKTKITGSLNFYIGKVKTYLTATVAINGDHFT
AKNIGFENTAGPEGHQAVALRVSADYAVFYNCQIDGYQDTLYVHSHRQFFRDCTVSGTVDFIFGDAKVVL
QNCNIVVRKPMKGQSCMITAQGRSDVRESTGLVLQNCHITGEPAYIPVKSINKAYLGRPWKEFSRTIIMG
TTIDDVIDPAGWLPWNGDFALNTLYYAEYENNGPGSNQAQRVKWPGIKKLSPKQALRFTPARFLRGNLWI
PPNRVPYMGNFQ
>gnl|CDD|215536 PLN02991, PLN02991, oxidoreductase
MEVKSVNTTAMILGLLFLISFVAAEDPYRFFEWHVTYGNISPLGVAQQGILINGKFPGPDIISVTNDNLI
INVFNHLDEPFLISWSGIRNWRNSYQDGVYGTTCPIPPGKNYTYALQVKDQIGSFYYFPSLGFHKAAGGF
GAIRISSRPLIPVPFPAPADDYTVLIGDWYKTNHKDLRAQLDNGGKLPLPDGILINGRGSGATLNIEPGK
TYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTHTIQTPFSSLDVHVGQSYSVLITADQPAKDYYIVVSSR
FTSKILITTGVLHYSNSAGPVSGPIPDGPIQLSWSFDQARAIKTNLTASGPRPNPQGSYHYGKINITRTI
RLANSAGNIEGKQRYAVNSASFYPADTPLKLADYFKIAGVYNPGSIPDQPTNGAIFPVTSVMQTDYKAFV
EIVFENWEDIVQTWHLDGYSFYVVGMELGKWSAASRKVYNLNDAVSRCTVQVYPRSWTAIYVSLDNVGMW
NLRSELWERQYLGQQFYMRVYTTSTSLRDEYLIPKNALLCGRATGHHTTTPGP
>gnl|CDD|178572 PLN02992, PLN02992, coniferyl-alcohol glucosyltransferase
MHITKPHAAMFSSPGMGHVIPVIELGKRLSANHGFHVTVFVLETDAASAQSKFLNSTGVDIVGLPSPDIS
GLVDPSAHVVTKIGVIMREAVPTLRSKIAEMHQKPTALIVDLFGTDALCLGGEFNMLTYIFIASNARFLG
VSIYYPTLDKDIKEEHTVQRKPLAMPGCEPVRFEDTLDAYLVPDEPVYRDFVRHGLAYPKADGILVNTWE
EMEPKSLKSLQDPKLLGRVARVPVYPIGPLCRPIQSSKTDHPVLDWLNKQPNESVLYISFGSGGSLSAKQ
LTELAWGLEMSQQRFVWVVRPPVDGSACSAYFSANGGETRDNTPEYLPEGFVSRTHDRGFVVPSWAPQAE
ILAHQAVGGFLTHCGWSSTLESVVGGVPMIAWPLFAEQNMNAALLSDELGIAVRSDDPKEVISRSKIEAL
VRKVMVEEEGEEMRRKVKKLRDTAEMSLSIDGGGVAHESLCRVTKECQRFLERVRCLARGA
>gnl|CDD|215537 PLN02993, PLN02993, lupeol synthase
MWKLKIGEGNGEDPYLFSSNNFVGRQTWEFDPKAGTPEERAAVEEARRSFLDNRSRVKGCSDLLWRMQFL
KEAKFEQVIPPVKIDRGEEITYETATNALRRGVSFFSALQASDGHWPGEITGPLFFLPPLVFCLYITGHL
EEVFDAEHRKEMLRHIYCHQNEDGGWGLHIESKSVMFCTVLNYICLRMLGEGPNGGRENACKRARQWILD
HGGVTYIPSWGKFWLSILGIYDWSGTNPMPPEIWLLPSFLPIHLGKTLCYTRMVYMPMSYLYGKRFVGPI
TPLIMLLREELHLQPYEEINWNKARRLCAKEDMYYPHPLVQDLIWDTLHNFVEPFLTRWPLNKLVREKAL
QVAMKHIHYEDENSHYITIGCVEKVLCMLACWIENPNGDHFKKHLARIPDYMWVAEDGMKMQSFGSQLWD
TGFAIQALLASDLSDETDDVLRRGHNYIKKSQVRENPSGDFKSMYRHISKGAWTLSDRDHGWQVSDCTAE
ALKCCMLLSMMPADVVGQKIDPEQLYDSVNLLLSLQSENGGVTAWEPVRAYKWLELLNPTDFFANTMVER
EYVECTSAVIQALVLFKQLYPDHRTKEIIKSIEKAVQFIESKQTPDGSWYGNWGICFIYATWFALGGLAA
AGKTYNDCLAMRKGVHFLLTIQRDDGGWGESYLSCPEQRYIPLEGNRSNLVQTAWAMMGLIHAGQAERDL
IPLHRAAKLIITSQLENGDFPQQEILGAFMNTCMLHYATYRNTFPLWALAEYRKAAFITHADL
>gnl|CDD|166635 PLN02994, PLN02994, 1-aminocyclopropane-1-carboxylate synthase
MGACENQLLSKLALADKHGEASPYFAGWKAYDLNPFDLLHNPQGIIQMGLAENQLCSDLIEEWIEENPHA
DICTAEGTIDSFKDIALFQDYHGLANFRKAIANFMAEARGGRVKFDADMIVLSAGATAANEIIMFCIADP
GDAFLVPTPYYAA
>gnl|CDD|178574 PLN02995, PLN02995, Probable pectinesterase/pectinesterase inhibitor
MNMMMQKISFLSLHLLLLLLLCVHPLTTVADGNSTDIDGWCDKTPYPDPCKCYFKNHNGFRQPTQISEFR
VMLVEAAMDRAISARDELTNSGKNCTDFKKQAVLADCIDLYGDTIMQLNRTLQGVSPKAGAAKRCTDFDA
QTWLSTALTNTETCRRGSSDLNVSDFITPIVSNTKISHLISNCLAVNGALLTAGNNGNTTANQKGFPTWV
SRKDRRLLRLVRANLVVAKDGSGHFNTVQAAIDVAGRRKVTSGRFVIYVKRGIYQENINVRLNNDDIMLV
GDGMRSTIITGGRSVKGGYTTYNSATAGIEGLHFIAKGITFRNTAGPAKGQAVALRSSSDLSIFYKCSIE
GYQDTLMVHSQRQFYRECYIYGTVDFIFGNAAAVFQNCIILPRRPLKGQANVITAQGRADPFQNTGISIH
NSRILPAPDLKPVVRTVKTYMGRPWMKFSRTVVLQTYLDNVVSPVGWSPWIEGSVFGLDTLFYAEYKNTG
PASSTRWRVRWKGFHVLGRASDASAFTVGKFIAGTAWLPGTGIPFTSGL
>gnl|CDD|215538 PLN02996, PLN02996, fatty acyl-CoA reductase
EEGSCVQFLENKTILVTGATGFLAKIFVEKILRVQPNVKKLYLLLRASDAKSATQRLHDEVIGKDLFKVL
REKLGENLNSLISEKVTPVPGDISYDDLGVKDSNLREEMWKEIDIVVNLAATTNFDERYDVALGINTLGA
LNVLNFAKKCVKVKMLLHVSTAYVCGEKSGLILEKPFHMGETLNGNRKLDINEEKKLVKEKLKELNEQDA
SEEEITQAMKDLGMERAKLHGWPNTYVFTKAMGEMLLGNFKENLPLVIIRPTMITSTYKEPFPGWIEGLR
TIDSVIVGYGKGKLTCFLADPNSVLDVIPADMVVNAMIVAMAAHAGGQGSEIIYHVGSSLKNPVKFSNLH
DFAYRYFSKNPWINKEGSPVKVGKGTILSTMASFSLYMTIRYLLPLKALQLVNIILPKRYGDKYTDLNRK
IKLVMRLVDLYKPYVFFKGIFDDTNTEKLRIKRKETGKEEADMFDFDPKSIDWEDYMTNVHIPGLVKYVL
K
>gnl|CDD|178576 PLN02997, PLN02997, flavonol synthase
MEEERDHNTSESSLPSLSKQLASSTLGGSAVDVPVVDLSVSDEDFLVREVVKASEEWGVFQVVNHGIPTE
LMRQLQMVGKQFFELPEAEKETVAKEEDFEGYKRNYLGGINNWDEHLFHRLSPPSIINYKYWPKNPPQYR
EVTEEYTKHMKRLTEKILGWLSEGLGLPRETFTQSIGGETAEYVLRVNFYPPTQDTELVIGAAAHSDMGA
IALLIPNEVPGLQAFKDEQWLDLNYINSAVVVIIGDQLMRMTNGRFKNVLHRAKTDKERLRISWPVFVAP
RADMSVGPLPELTGDENPPKFETLIYNDYIDQKIRGWALEDLPVY
>gnl|CDD|215539 PLN02998, PLN02998, beta-glucosidase
MKLLSNSLMFLPLLALALTAVSSLKYSRNDFPPGFVFGSGTSAYQVEGAADEDGRTPSIWDVFAHAGHSG
VAAGNVACDQYHKYKEDVKLMADMGLEAYRFSISWSRLLPSGRGPINPKGLQYYNNLIDELITHGIQPHV
TLHHFDLPQALEDEYGGWLSQEIVRDFTAYADTCFKEFGDRVSHWTTINEVNVFALGGYDQGITPPARCS
PPFGLNCTKGNSSIEPYIAVHNMLLAHASATILYKQQYKYKQHGSVGISVYTYGAVPLTNSVKDKQATAR
VNDFYIGWILHPLVFGDYPETMKTNVGSRLPAFTEEESEQVKGAFDFVGVINYMALYVKDNSSSLKPNLQ
DFNTDIAVEMTLVGNTSIENEYANTPWSLQQILLYVKETYGNPPVYILENGQMTPHSSSLVDTTRVKYLS
SYIKAVLHSLRKGSDVKGYFQWSLMDVFELFGGYERSFGLLYVDFKDPSLKRSPKLSAHWYSSFLKGTLH
HPSYASS
>gnl|CDD|178577 PLN02999, PLN02999, photosystem II oxygen-evolving enhancer 3 protein (PsbQ)
MSSFTTTNTPPPYLLRKIYHRRVNQPFSVVCCTGEPQQDIFTRRRTLTSLITFTVIGGATSSALAQEKWG
TRSFIKEKYFMPGLSPEDAAARIKQTAEGLRDMREMLDHMSWRYVIFYIRLKQAYLSQDLTNAMNILPES
RRNDYVQAANELVENMSELDYYVRTPKVYESYLYYEKTLKSIDNVVELLA
>gnl|CDD|178578 PLN03000, PLN03000, amine oxidase
MVSFSAPKKRRRGRSQRSASSLNSLPVPNVGTLPGNTNFVSSSASSSGRFNVESVNGSNQTTKSYPGIGD
EIITINKEATTEALLALTAGFPADSLTEEEIEFGVVPIVGGIEQVNYILIRNHIISKWRENISSWVTKEM
FLGSIPKHCSSLLDSAYNYLVTHGYINFGIAQAIKDKFPAQSSKSSVVIVGAGLSGLAAARQLMRFGFKV
TVLEGRKRPGGRVYTKKMEANRVGAAADLGGSVLTGTLGNPLGIIARQLGSSLYKVRDKCPLYRVDGKPV
DPDVDLKVEVAFNQLLDKASKLRQLMGDVSMDVSLGAALETFRQVSGNDVATEEMGLFNWHLANLEYANA
GLVSKLSLAFWDQDDPYDMGGDHCFLPGGNGRLVQALAENVPILYEKTVQTIRYGSNGVKVIAGNQVYEG
DMVLCTVPLGVLKNGSIKFVPELPQRKLDCIKRLGFGLLNKVAMLFPYVFWSTDLDTFGHLTEDPNYRGE
FFLFYSYAPVAGGPLLIALVAGEAAHKFETMPPTDAVTRVLHILRGIYEPQGINVPDPLQTVCTRWGGDP
FSLGSYSNVAVGASGDDYDILAESVGDGRLFFAGEATTRRYPATMHGAFVTGLREAANMAQSAKARGIRK
RIDRNPSKNAHSCAILLADLFRDPDLEFGSFAIIFSRRNPDPKSPAILRVTLSEPRKRNEDPKADQHSNK
ILFQQLQSHFNQQQQIQVYTLLTRQQALDLREVRGGDEKRLNYLCETLGVKLVGRKGLGPGADSVIASIK
AERTGNKLPSSSTSGTKSGMKPKAAGSKRKKVVSNVGGLMPRNSNMRNGNSSIPPSNNMGNGSGLVPRPN
LNMGNGSGLVPSSNLNMTSGLLPPSNLSIGNGSGFTPAILN
>gnl|CDD|166642 PLN03001, PLN03001, oxidoreductase, 2OG-Fe(II) oxygenase family protein
MRSLGLSFFKDSPMEEKLRYACDPGSAASEGYGSRMLLGAKDDTVLDWRDFFDHHTFPLSRRNPSHWPDF
PPDYREVVGEYGDCMKALAQKLLAFISESLGLPCSCIEDAVGDFYQNITVSYYPPCPQPELTLGLQSHSD
FGAITLLIQDDVEGLQLLKDAEWLMVPPISDAILIIIADQTEIITNGNYKSAQHRAIANANKARLSVATF
HDPAKTAKIAPASALSTESFPPRYCEIVYGEYVSSWYSKGPEGKRNIDALLL
>gnl|CDD|178579 PLN03002, PLN03002, oxidoreductase, 2OG-Fe(II) oxygenase family protein
MENHTKDSTMKVSSLNCIDLANDDLNHSVASLKQACLDCGFFYVINHGINEEFMDDVFEQSKKFFALPLE
EKMKVLRNEKHRGYTPVLDEKLDPKNQINGDHKEGYYIGIEVPKDDPHWDKPFYGPNPWPDADVLPGWRE
TMEKYHQEALRVSMAIAKLLALALDLDVGYFDRTEMLGKPIATMRLLRYQGISDPSKGIYACGAHSDFGM
MTLLATDGVMGLQICKDKNAMPQKWEYVPPIKGAFIVNLGDMLERWSNGFFKSTLHRVLGNGQERYSIPF
FVEPNHDCLVECLPTCKSESDLPKYPPIKCSTYLTQRYEETHAKLSIYHQQT
>gnl|CDD|178580 PLN03003, PLN03003, Probable polygalacturonase At3g15720
MKKKTWFLNFSLFFLQIFTSSNALDVTQFGAVGDGVTDDSQAFLKAWEAVCSGTGDGQFVVPAGMTFMLQ
PLKFQGSCKSTPVFVQMLGKLVAPSKGNWKGDKDQWILFTDIEGLVIEGDGEINGQGSSWWEHKGSRPTA
LKFRSCNNLRLSGLTHLDSPMAHIHISECNYVTISSLRINAPESSPNTDGIDVGASSNVVIQDCIIATGD
DCIAINSGTSNIHISGIDCGPGHGISIGSLGKDGETATVENVCVQNCNFRGTMNGARIKTWQGGSGYARM
ITFNGITLDNVENPIIIDQFYNGGDSDNAKDRKSSAVEVSKVVFSNFIGTSKSEYGVDFRCSERVPCTEI
FLRDMKIETASSGSGQVAQGQCLNVRGASTIAVPGLECLELSTDMFSSAQLLEQTCMSAQSVQPRTTTQP
MQDPIWVFQSRGKQLRVYNIAILVSFISLVTYILAR
>gnl|CDD|178581 PLN03004, PLN03004, UDP-glycosyltransferase
MGEEAIVLYPAPPIGHLVSMVELGKTILSKNPSLSIHIILVPPPYQPESTATYISSVSSSFPSITFHHLP
AVTPYSSSSTSRHHHESLLLEILCFSNPSVHRTLFSLSRNFNVRAMIIDFFCTAVLDITADFTFPVYFFY
TSGAACLAFSFYLPTIDETTPGKNLKDIPTVHIPGVPPMKGSDMPKAVLERDDEVYDVFIMFGKQLSKSS
GIIINTFDALENRAIKAITEELCFRNIYPIGPLIVNGRIEDRNDNKAVSCLNWLDSQPEKSVVFLCFGSL
GLFSKEQVIEIAVGLEKSGQRFLWVVRNPPELEKTELDLKSLLPEGFLSRTEDKGMVVKSWAPQVPVLNH
KAVGGFVTHCGWNSILEAVCAGVPMVAWPLYAEQRFNRVMIVDEIKIAISMNESETGFVSSTEVEKRVQE
IIGECPVRERTMAMKNAAELALTETGSSHTA
>gnl|CDD|178582 PLN03005, PLN03005, beta-fructofuranosidase
MEGLGLRAVGSHCSLSEMDDLDLTRALDKPRLKIERKRSFDERSMSELSTGYSRHDGIHDSPRGRSVLDT
PLSSARNSFEPHPMMAEAWEALRRSMVFFRGQPVGTLAAVDNTTDEVLNYDQVFVRDFVPSALAFLMNGE
PDIVKHFLLKTLQLQGWEKRVDRFKLGEGVMPASFKVLHDPIRETDNIVADFGESAIGRVAPVDSGFWWI
ILLRAYTKSTGDLTLSETPECQKGMKLILSLCLAEGFDTFPTLLCADGCSMIDRRMGVYGYPIEIQALFF
MALRSALSMLKPDGDGREFIERIVKRLHALSFHMRNYFWLDHQNLNDIYRFKTEEYSHTAVNKFNVMPDS
IPEWVFDFMPLRGGYFVGNVGPAHMDFRWFALGNCVSILSSLATPDQSMAIMDLLEHRWEELVGEMPLKI
CYPCLEGHEWRIVTGCDPKNTRWSYHNGGSWPVLLWQLTAACIKTGRPQIARRAVDLIESRLHRDCWPEY
YDGKLGRYVGKQARKYQTWSIAGYLVAKMLLEDPSHIGMISLEEDKLMKPVIKRSASWPQ
>gnl|CDD|178583 PLN03006, PLN03006, carbonate dehydratase
MAATPTHFSVSHDPFSSTSLLNLQTQAIFGPNHSLKTTQLRIPASFRRKATNLQVMASGKTPGLTQEANG
VAIDRQNNTDVFDDMKQRFLAFKKLKYMDDFEHYKNLADAQAPKFLVIACADSRVCPSAVLGFQPGDAFT
VRNIANLVPPYESGPTETKAALEFSVNTLNVENILVIGHSRCGGIQALMKMEDEGDSRSFIHNWVVVGKK
AKESTKAVASNLHFDHQCQHCEKASINHSLERLLGYPWIEEKVRQGSLSLHGGYYNFVDCTFEKWTVDYA
ASRGKKKEGSGIAVKDRSVWS
>gnl|CDD|178584 PLN03007, PLN03007, UDP-glucosyltransferase family protein
MNHEKLHILFFPFMAHGHMIPTLDMAKLFSSRGAKSTILTTPLNAKIFEKPIEAFKNLNPGLEIDIQIFN
FPCVELGLPEGCENVDFITSNNNDDSGDLFLKFLFSTKYFKDQLEKLLETTRPDCLVADMFFPWATEAAE
KFGVPRLVFHGTGYFSLCASYCIRVHKPQKKVASSSEPFVIPDLPGDIVITEEQINDADEESPMGKFMKE
VRESEVKSFGVLVNSFYELESAYADFYKSFVAKRAWHIGPLSLYNRGFEEKAERGKKANIDEQECLKWLD
SKKPDSVIYLSFGSVASFKNEQLFEIAAGLEGSGQNFIWVVRKNENQGEKEEWLPEGFEERTKGKGLIIR
GWAPQVLILDHQATGGFVTHCGWNSLLEGVAAGLPMVTWPVGAEQFYNEKLVTQVLRTGVSVGAKKLVKV
KGDFISREKVEKAVREVIVGEEAEERRLRAKKLAEMAKAAVEEGGSSFNDLNKFMEELNSRK
>gnl|CDD|178585 PLN03008, PLN03008, Phospholipase D delta
MAEKVSEDVMLLHGDLDLKIVKARRLPNMDMFSEHLRRLFTACNACARPTDTDDVDPRDKGEFGDKNIRS
HRKVITSDPYVTVVVPQATLARTRVLKNSQEPLWDEKFNISIAHPFAYLEFQVKDDDVFGAQIIGTAKIP
VRDIASGERISGWFPVLGASGKPPKAETAIFIDMKFTPFDQIHSYRCGIAGDPERRGVRRTYFPVRKGSQ
VRLYQDAHVMDGTLPAIGLDNGKVYEHGKCWEDICYAISEAHHMIYIVGWSIFHKIKLVRETKVPRDKDM
TLGELLKYKSQEGVRVLLLVWDDKTSHDKFGIKTPGVMGTHDEETRKFFKHSSVICVLSPRYASSKLGLF
KQQASPIFSIYVMTVVGTLFTHHQKCVLVDTQAVGNNRKVTAFIGGLDLCDGRYDTPEHRILHDLDTVFK
DDFHNPTFPAGTKAPRQPWHDLHCRIDGPAAYDVLINFEQRWRKATRWKEFSLRLKGKTHWQDDALIRIG
RISWILSPVFKFLKDGTSIIPEDDPCVWVSKEDDPENWHVQIFRSIDSGSVKGFPKYEDEAEAQHLECAK
RLVVDKSIQTAYIQTIRSAQHFIYIENQYFLGSSYAWPSYRDAGADNLIPMELALKIVSKIRAKERFAVY
VVIPLWPEGDPKSGPVQEILYWQSQTMQMMYDVIAKELKAVQSDAHPLDYLNFYCLGKREQLPDDMPATN
GSVVSDSYNFQRFMIYVHAKGMIVDDEYVLMGSANINQRSMAGTKDTEIAMGAYQPNHTWAHKGRHPRGQ
VYGYRMSLWAEHLGKTGDEFVEPSDLECLKKVNTISEENWKRFIDPKFSELQGHLIKYPLQVDVDGKVSP
LPDYETFPDVGGKIIGAHSMALPDTLTT
>gnl|CDD|166650 PLN03009, PLN03009, cellulase
KLHLRPLSLVFLFFLILRRPTMESNQHDYSDALSKSILFFEGQRSGYLPNDQRMTWRANSGLSDGWTHNT
DLTGGYYDAGDNVKFGFPMAFTTTMLAWSVIEFGDLMPSSELRNSLVAIRWATDYLLKTVSQPNRIFVQV
GDPIADHNCWERPEDMDTPRTVYAVNAPNPASDVAGETAAALAASSMAFRSSDPGYSETLLRNAIKTFQF
ADMYRGAYSDNDDIKDGVCPFYCDFDGYQDELLWGAAWLRRASGDDSYLNYIENNGETLGANDNINEFGW
DNKHAGLNVLVSKEVLEGNMYSLQSYKASADSFMCTLIPESSSSHVEYTPGGLIYKPGGSNLQHATTISF
LLLVYANYLSRSSQSVNCGNLTIGPDSLRQQAKRQVDYILGDNPMGLSYMVGYSERYPQRIHHRGSSLPS
IKDHPEAIACKEGSVYFNSSNPNPNVLVGAVVGGPGEDDSYEDDRDDFRKSEPTTYINAPFVGVLAYFAA
NPGSS
>gnl|CDD|215540 PLN03010, PLN03010, polygalacturonase
MVTIQKNGDIPAVTTQWHGLMSFMETILRISILINFICFGLVNGQNYNVLKFGAKGDGQTDDSNAFLQAW
NATCGGEGNINTLLIPSGKTYLLQPIEFKGPCKSTSIKVQLDGIIVAPSNIVAWSNPKSQMWISFSTVSG
LMIDGSGTIDGRGSSFWEALHISKCDNLTINGITSIDSPKNHISIKTCNYVAISKINILAPETSPNTDGI
DISYSTNINIFDSTIQTGDDCIAINSGSSNINITQINCGPGHGISVGSLGADGANAKVSDVHVTHCTFNQ
TTNGARIKTWQGGQGYARNISFENITLINTKNPIIIDQQYIDKGKLDATKDSAVAISNVKYVGFRGTTSN
ENAITLKCSAITHCKDVVMDDIDVTMENGEKPKVECQNVEGESSDTDLMRDCFKNNSTS
>gnl|CDD|166653 PLN03012, PLN03012, Camelliol C synthase
MWKLKIAEGNGDDPYLFSTNNFAGRQTWEFDPDAGSPEELAAVEEARRIFYDDRFHVKASSDLIWRMQFL
KEKKFEQRIAPAKVEDAEKITFEIATNALRKGIHFFSALQASDGHWPAENAGPLFFLPPLVFCLYITGHL
DEIFTQDHRKEILRYIYCHQKEDGGWGLHIEGHSTMFCTTLNYICMRILGEGPDGGHDNACGRARDWILD
HGGATYIPSWGKTWLSILGVFDWSGSNPMPPEFWILPSFFPIHPAKMWCYCRLVYLPMSYLYGKRFVGPI
SPLILQLREEIYLQPYAEINWMKARHLCAKEDAYCPHPLIQDLIWDCLYIFAEPFLACWPFNKLLREKAL
GLAMKHIHYEDENSRYITIGCVEKALCMLACWVEDPNGDHFKKHLLRISDYLWIAEDGMKMQSFGSQLWD
SGFALQALLASNLSNEIPDVLRRGHDFIKNSQVGENPSGDFKNMYRHISKGAWTFSDRDHGWQASDCTAE
GFKCCLLFSMIAPDIVGPKMDPEQLHDAVNILLSLQSKNGGMTAWEPAGAPEWLELLNPTEMFADIVIEH
EYNECTSSAIQALILFKQLYPDHRTEEINAFIKKAAEYIENIQMLDGSWYGNWGICFTYGTWFALAGLAA
AGKTFNDCEAIRKGVHFLLAAQKDNGGWGESYLSCPKKIYIAQEGEISNLVQTAWALMGLIHAGQAERDP
IPLHRAAKLIINSQLENGDFPQQEATGAFLKNCLLHYAAYRNIFPLWALAEYRARVPLP
>gnl|CDD|178587 PLN03013, PLN03013, cysteine synthase
MVAMIMASRFNREAKLASQILSTLLGNRSCYTSMAATSSSALLLNPLTSSSSSSTLRRFRCSPEISSLSF
SSASDFSLAMKRQSRSFADGSERDPSVVCEAVKRETGPDGLNIADNVSQLIGKTPMVYLNSIAKGCVANI
AAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVLVEPTSGNTGIGLAFIAASRGYRLILTMPASMS
MERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYETTGPEIWDDTKGK
VDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDE
VIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASGRDIYTPRCSSLSG
KRWRKCSLR
>gnl|CDD|178588 PLN03014, PLN03014, carbonic anhydrase
MSTAPLSGFFLTSLSPSQSSLQKLSLRTSSTVACLPPASSSSSSSSSSSSRSVPTLIRNEPVFAAPAPII
APYWSEEMGTEAYDEAIEALKKLLIEKEELKTVAAAKVEQITAALQTGTSSDKKAFDPVETIKQGFIKFK
KEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKVKYGGVGAAI
EYAVLHLKVENIVVIGHSACGGIKGLMSFPLDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRC
EREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGAFELWGLEFGLSETSSVKDVATILHWKL
>gnl|CDD|178589 PLN03015, PLN03015, UDP-glucosyl transferase
MDQPHALLVASPGLGHLIPILELGNRLSSVLNIHVTILAVTSGSSSPTETEAIHAAAARTTCQITEIPSV
DVDNLVEPDATIFTKMVVKMRAMKPAVRDAVKSMKRKPTVMIVDFFGTALMSIADDVGVTAKYVYIPSHA
WFLAVMVYLPVLDTVVEGEYVDIKEPLKIPGCKPVGPKELMETMLDRSDQQYKECVRSGLEVPMSDGVLV
NTWEELQGNTLAALREDMELNRVMKVPVYPIGPIVRTNVHVEKRNSIFEWLDKQGERSVVYVCLGSGGTL
TFEQTVELAWGLELSGQRFVWVLRRPASYLGASSSDDDQVSASLPEGFLDRTRGVGLVVTQWAPQVEILS
HRSIGGFLSHCGWSSVLESLTKGVPIVAWPLYAEQWMNATLLTEEIGVAVRTSELPSEKVIGREEVASLV
RKIVAEEDEEGQKIRAKAEEVRVSSERAWSHGGSSYNSLFEWAKRCYLVS
>gnl|CDD|178590 PLN03016, PLN03016, sinapoylglucose-malate O-sinapoyltransferase
MSLKIKFLLLLVLYHHVDSASIVKFLPGFEGPLPFELETGYIGIGEDENVQFFYYFIKSENNPKEDPLLI
WLNGGPGCSCLGGIIFENGPVGLKFEVFNGSAPSLFSTTYSWTKMANIIFLDQPVGSGFSYSKTPIDKTG
DISEVKRTHEFLQKWLSRHPQYFSNPLYVVGDSYSGMIVPALVQEISQGNYICCEPPINLQGYMLGNPVT
YMDFEQNFRIPYAYGMGLISDEIYEPMKRICNGNYYNVDPSNTQCLKLTEEYHKCTAKINIHHILTPDCD
VTNVTSPDCYYYPYHLIECWANDESVREALHIEKGSKGKWARCNRTIPYNHDIVSSIPYHMNNSISGYRS
LIYSGDHDIAVPFLATQAWIRSLNYSPIHNWRPWMINNQIAGYTRAYSNKMTFATIKAGGHTAEYRPNET
FIMFQRWISGQPL
>gnl|CDD|178591 PLN03017, PLN03017, trehalose-phosphatase
SASQNVVVSETTTSSIIPNNVSNSSNSSSQKLPPGLISISKKKLLKNIDIINGGGQRINAWVDSMRASSP
THLKSLPSSISSQQQLNSWIMQHPSALEMFEQIMEASRGKQIVMFLDYDGTLSPIVDDPDKAFMSSKMRR
TVKKLAKCFPTAIVTGRCIDKVYNFVKLAELYYAGSHGMDIKGPAKGFSRHKRVKQSLLYQPANDYLPMI
DEVYRQLLEKTKSTPGAKVENHKFCASVHFRCVDEKKWSELVLQVRSVLKNFPTLKLTQGRKVFEIRPMI
EWDKGKALEFLLESLGFGNTNNVFPVYIGDDRTDEDAFKMLRDRGEGFGILVSKFPKDTDASYSLQDPSE
VMDFLARLVEWKQMQQ
>gnl|CDD|178592 PLN03018, PLN03018, homomethionine N-hydroxylase
MMSFNTSFQILLGFIVFIASITLLGRILSRPSKTKDRSRQLPPGPPGWPILGNLPELIMTRPRSKYFHLA
MKELKTDIACFNFAGTHTITINSDEIAREAFRERDADLADRPQLSIMETIGDNYKSMGTSPYGEQFMKMK
KVITTEIMSVKTLNMLEAARTIEADNLIAYIHSMYQRSETVDVRELSRVYGYAVTMRMLFGRRHVTKENV
FSDDGRLGKAEKHHLEVIFNTLNCLPGFSPVDYVERWLRGWNIDGQEERAKVNVNLVRSYNNPIIDERVE
LWREKGGKAAVEDWLDTFITLKDQNGKYLVTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRK
ALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVCRP
GLGRNPKIWKDPLVYEPERHLQGDGITKEVTLVETEMRFVSFSTGRRGCVGVKVGTIMMVMMLARFLQGF
NWKLHQDFGPLSLEEDDASLLMAKPLLLSVEPRLAPNLYPKFRP
>gnl|CDD|166660 PLN03019, PLN03019, carbonic anhydrase
MVPFWTTVSRNGSSDSETTLQSASKATKQYKYPSLRPSHRLSLLFLFPFHLSANGACFRCTCFSHFKLEL
RRMGNESYEDAIEALKKLLIEKDDLKDVAAAKVKKITAELQAASSSDSKSFDPVERIKEGFVTFKKEKYE
TNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFHPGDAFVVRNIANMVPPFDKVKYAGVGAAIEYAVL
HLKVENIVVIGHSACGGIKGLMSFPLDGNNSTDFIEDWVKICLPAKSKVLAESESSAFEDQCGRCERAVN
VSLANLLTYPFVREGVVKGTLALKGGYYDFVNGSFELWELQFGISPVHSI
>gnl|CDD|215541 PLN03020, PLN03020, low-temperature-induced protein; Provisional
TGRPHGHHYEEDPHNVGLHSATEGEDHHEKKSVLKKVKDKAKKIKDTITKHGHGHHHDEHRVPDDHDLYE
EDDDEDEEMAEDPQIHGGSAYESAAIKNRSVPGQELYLGQPGPTYGRTTAMKEDPLGPKDATTTPFKSFL
PGKEVTLGRTTAIKEVPHAPDNTPATFSPEPVEQTRLAEPPKEGNPEQSRSRGQPEVNLGAPMGLEEDPH
APKDRPEDVDPSNYQTKVADPTGDGGEEVGITPILSSFDKMNIQDEPEQPFATEDLPTRPHDKSIFPTGS
HDQFSPEPLSPAETKSTEDPQSTSNAEKPSNQKTYTEKISSATSAIADKAISAKNVVASKLGYGGTDNNE
KEHEMHVGGGDQTAKKTSSVVEYGKKIANTVTEKLSPVYEKVAEAGSAVMSKVQGTGSEREGEKEHDKGG
EDKGVSVKDYFAEKLRPGDEDRALSEVISEALQKRKQEPELETKSKPMGKVTESEEVARRLGSEEENSGE
ASDSGSVKIPSGGGVVDKLKGAVGSWLGKGGESQTSPQSIAGNEGFSTSGASGEEQGEKRLQEKRN
>gnl|CDD|178593 PLN03021, PLN03021, Low-temperature-induced protein; Provisional
MESQLTRPYGHEQAEEPIRIHHPEEDEHHEKGASKVLKKVKEKAKKIKNSLTKHGNGHDHDVEDDDDEYD
EQDPEVHGAPVYESSAVRGGVTGKPKSLSHAGETNVPASEEIVPPGTKVFPVVSSDHTKPIEPVSLQDTS
YGHEALADPVRTTETSDWEAKREAPTHYPLGVSEFSDRGESREAHQEPLNTPVSLLSATEDVTRTFAPGG
EDDYLGGQRKVNVETPKRLEEDPAAPGGGSDYLSGVSNYQSKVTDPTHKGGEAGVPEIAESLGRMKVTDE
SPDQKSRQGREEDFPTRSHEFDLKKESDINKNSPARFGGESKAGMEEDFPTRGDVKVESGLGRDLPTGTH
DQFSPELSRPKERDDSEETKDESTHETKPSTYTEQLASATSAITNKAIAAKNVVASKLGYTGENGGGQSE
SPVKDETPRSVTAYGQKVAGTVAEKLTPVYEKVKETGSTVMTKLPLSGGGSGVKETQQGEEKGVTAKNYI
SEKLKPGEEDKALSEMIAEKLHFGGGGEKKTTATKEVEVTVEKIPSDQIAEGKGHGEAVAEEGKGGEGMV
GKVKGAVTSWLGGKPKSPRSVEESPQSLGTTVGTMGFSDSGGSELGGSGGGKGVQDSGN
>gnl|CDD|215542 PLN03023, PLN03023, Expansin-like B1; Provisional
FPLSHYCCFLCVIVLLPLLCKSQDFTYSRATYYGSPDCLGTPTGACGFGEYGRTVNGGNVAGVSRLYRNG
TGCGACYQVRCKAPNLCSDDGVNVVVTDYGEGDKTDFILSPRAYARLARPNMAAELFAYGVVDVEYRRIP
CRYAGYNLFFKVHEHSRFPDYLAIVMLYQAGQNDILAVEIWQEDCKEWRGMRKAYGAVWDMPNPPKGPIT
LRFQVSGSAGQTWVQAKNVIPSDWKAGVAYDSNIQLD
>gnl|CDD|178595 PLN03024, PLN03024, Putative EG45-like domain containing protein 1; Provisional
MSKRILIFSTVLVFLFSVSYATPGIATFYTSYTPSACYRGTSFGVMIAAASDSLWNNGRVCGKMFTVKCK
GPRNAVPHPCTGKSVTVKIVDHCPSGCASTLDLSREAFAQIANPVAGIINIDYIP
>gnl|CDD|178596 PLN03025, PLN03025, replication factor C subunit; Provisional
LPWVEKYRPTKLDDIVGNEDAVSRLQVIARDGNMPNLILSGPPGTGKTTSILALAHELLGPNYKEAVLEL
NASDDRGIDVVRNKIKMFAQKKVTLPPGRHKIVILDEADSMTSGAQQALRRTMEIYSNTTRFALACNTSS
KIIEPIQSRCAIVRFSRLSDQEILGRLMKVVEAEKVPYVPEGLEAIIFTADGDMRQALNNLQATHSGFGF
VNQENVFKVCDQPHPLHVKNIVRNCLKGKFDDACDGLKQLYDLGYSPTDIITTLFRVVKNYDMPEFLKLE
YLREIGFAHMRICDGVGSLLQLSGLLAKLCLVRETAKAP
>gnl|CDD|178597 PLN03026, PLN03026, histidinol-phosphate aminotransferase; Provisional
VSRAQSSATAMSEVKQSTSGDSFIRKHILQLAPYQPILPFEVLSAQLGRKPEDIVKLDANENPYGPPPEV
LEALGNMKFPYVYPDPESRRLRAALAEDSGLESENILVGCGADELIDLLMRCVLDPGDKIIDCPPTFGMY
VFDAAVNGAEVIKVPRTPDFSLDVPRIVEAVETHKPKLLFLTSPNNPDGSIISDDDLLKILELPILVVLD
EAYIEFSTQESRMKWVKKYDNLIVLRTFSKRAGLAGLRVGYGAFPLSIIEYLWRAKQPYNVSVAAEVAAC
AALSNPKYLEDVKNALVEERERLFGLLKEVPFLEPYPSDANFILCRVTSGRDAKKLKEDLAKMGVMVRHY
NSKELKGYIRVSVGKPEHTDALMEALKQLY
>gnl|CDD|215543 PLN03028, PLN03028, pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Provisional
PRELSGLQKLRSLYQPELPPCLQGTTVRVELGDATTAADPADAHAISRAFPHTYGQPLAHFLRATAKVPD
AQVITEHPAVRVGVVFCGRQSPGGHNVIWGLHDALKAHNPNSVLLGFLGGTEGLFAQKTLEITDDVLSTY
KNQGGYDLLGRTKDQIRTTEQVNAALAACEALKLDGLVIIGGVTSNTDAAQLAETFAEAKCKTKVVGVPV
TLNGDLKNQFVETNVGFDTICKVNSQLISNVCTDALSAEKYYYFIRLMGRKASHVALECALQSHPNMVIL
GEEVAASKLTLFDITKQICDAVQARAEQDKNHGVILIPEGLIESIPEVYALLQEIHGLLKQGVSVDNISS
QLSPWASALFEFLPPFIKKQLLLHPESDDSAQLSQIETEKLLAQLVETEMNKRTKEGTYKGKKFNAICHF
FGYQARGSLPSKFDCDYAYVLGHICYHILAAGLNGYMATVTNLKSPVNKWRCGAAPITAMMSVKRWSRGP
GASQIGKPAIHPAPVDLKGKAYELLRQNASSFLMDDLYRNPGPLQFDGPGADAKPITLCVEDQDYMGRIK
KLQEYLDKVRTIVKPGCSQEVLKAALSSMASVTDVLTVMSSPSNRGLTPL
>gnl|CDD|215544 PLN03029, PLN03029, type-a response regulator protein; Provisional
MGITTESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEDDRSNPDTPSVSPNSHQE
VEVNLIITDYCMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNR
LKPHMMKTKSKNQKQENQEKQEKLEESEIQSEKQEQPSQQPQSQPQPQQQPQQPNNNKRKAMEEGLSPDR
TRPRYNGITTVV
>gnl|CDD|215545 PLN03030, PLN03030, cationic peroxidase; Provisional
GQRFIVILFFLLAMMATTLVQGQGTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVR
GCDASILIDGSNTEKTALPNLLLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPT
GRRDGRVSLASDASNLPGFTDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTGNG
ADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGILESDQKLWTDASTRTFVQR
FLGVRGLAGLNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN
>gnl|CDD|215546 PLN03031, PLN03031, hypothetical protein; Provisional
MGFSKKSQVDGGLESDGKKWVIAGISIRAPLKPISTKPVAKEEDEEEDECSTTPTAKEARIPERLPCPPA
PRKRKPSLKCNYNGVREFFTPPDLETVFIQRA
>gnl|CDD|166673 PLN03032, PLN03032, serine decarboxylase; Provisional
TGERDAYMADILASYDKLLAEKSSVHFGYPYNLDFDYGELSQLMKYSINNLGDPFIESNYGVHSRQFEVG
VLDWFARLWELEKDEYWGYITTCGTEGNLHGILVGREVFPDGILYASRESHYSVFKAARMYRMEAVKVPT
LPSGEIDYDDLERALAKNRDKPAILNVNIGTTVKGAVDDLDRILRILKELGYTEDRFYIHCDGALFGLMM
PFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTRKKHVKALSQNVEYLNSRDATIMGSRNGHAPLY
LWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLTEAGLTCRLNELSSTVVFERPMDEAFIKKWQLACEGDIA
HVVVMPNVTVEKLDEFVEELVEVR
>gnl|CDD|178601 PLN03033, PLN03033, 2-dehydro-3-deoxyphosphooctonate aldolase; Provisional
MASSSLLYNQLKAAEPFFLLAGPNVIESEEHILRMAKHIKDISTKLGLPLVFKSSFDKANRTSSKSFRGP
GMAEGLKILEKVKVAYDLPIVTDVHESSQCEAVGKVADIIQIPAFLCRQTDLLVAAAKTGKIINIKKGQF
CAPSVMRNSAEKVRLAGNPNVMVCERGTMFGYNDLIVDPRNLEWMREANCPVVADITHSLQQPAGKKLDG
GGVASGGLRELIPCIARTAVAVGVDGIFMEVHDDPLSAPVDGPTQWPLRHLEELLEELIAIARVTKGKQR
FQIDLTPYRD
>gnl|CDD|178602 PLN03034, PLN03034, phosphoglycerate kinase; Provisional
MASAAAPTALSLLKSTAAAASTAASRASLLPVPSTGLSATSLRRLGFSAAADSRFSVHVASKVRSFRGKG
SRGVVSMAKKSVGDLTSADLKGKKVFVRADLNVPLDDNQNITDDTRIRAAIPTIKYLISNGAKVILSSHL
GRPKGVTPKFSLAPLVPRLSELLGIQVVKADDCIGPEVEKLVASLPEGGVLLLENVRFYKEEEKNEPEFA
KKLASLADLYVNDAFGTAHRAHASTEGVTKFLKPSVAGFLLQKELDYLVGAVSNPKRPFAAIVGGSKVSS
KIGVIESLLEKCDILLLGGGMIFTFYKAQGLSVGSSLVEEDKLELATSLLAKAKAKGVSLLLPTDVVIAD
KFAPDANSKIVPASAIPDGWMGLDIGPDSVKTFNEALDTTQTVIWNGPMGVFEFEKFAVGTEAVAKKLAE
LSGKGVTTIIGGGDSVAAVEKVGVADVMSHISTGGGASLELLEGKELPGVVALDEATPVAV
>gnl|CDD|178603 PLN03036, PLN03036, glutamine synthetase; Provisional
MAQILAPSPQCQMRVPKNSAVAAPMTSKLWSSLVLKQKKKGTAKVSGKFRVLALQSENSTVNRVEDLLNL
DTTPYTDRIIAEYIWIGGSGIDLRSKSRTISKPVEHPSELPKWNYDGSSTGQAPGEDSEVILYPQAIFKD
PFRGGNNILVICDTYTPAGEPIPTNKRHRAAEIFSNKKVVDEVPWFGIEQEYTLLQQNVKWPLGWPVGAY
PGPQGPYYCGAGADKSFGRDISDAHYKACLYAGINISGTNGEVMPGQWEYQVGPSVGIDAGDHIWCSRYI
LERITEQAGVVLTLDPKPIEGDWNGAGCHTNYSTKSMREEGGFEVIKKAILNLSLRHKEHISAYGEGNER
RLTGKHETASIDTFSWGVANRGCSIRVGRDTEKKGKGYLEDRRPASNMDPYIVTSLLAETTILWEPTLEA
EALAAQKLSLNV
>gnl|CDD|215547 PLN03037, PLN03037, lipase class 3 family protein; Provisional
MENALVKTPVTSRKLRRRKTKRVWKLKLAWKAIKKAVKSHLKKHLLHMKCRKEEKQLSQVSDGGQLQAER
IKKISNHSTKSLAFLLQLPYTADDFIDRGDLMTPTRSPRENISKMWREIHGSNNWENLLDPLHPWLRREV
VKYGEFVEATYDAFDFDPLSEFCGSCRYNRHKLFEELGLTKHGYKVTKYIYAMSHVDVPQWFLRSATGET
WSKDSNWMGFVAVSGDRESQRIGRRDIVVAWRGTVAPTEWFMDLRTSLEPFDCDGDHGKNVVKVQSGFLS
IYKSKSELTRYNKLSASEQVMEEVKRLVNFFKDRGEEVSLTITGHSLGGALALLNAYEAARSVPALSNIS
VISFGAPRVGNLAFKEKLNELGVKVLRVVNKQDIVPKLPGIIFNKILNKLNPITSRLNWVYRHVGTQLKL
DMFSSPYLKRESDLGGAHNLEVYLHLLDGFHGKKLGFRWNARRDLALVNKSTDMLIEELRIPEFWYQVPH
KGLVLNKQGRWVKPVRAPEDIPSPFSTGPKPIYIL
>gnl|CDD|166679 PLN03039, PLN03039, ethanolaminephosphotransferase; Provisional
MGFMFLLTSALLGYIYSPKLDSPPPRWVHFAHGLLLFLYQTFDAVDGKQARRTNSSSPLGELFDHGCDAL
ACAFEAMAFGSTAMCGRDTFWFWVISAIPFFGATWEHYFTNTLILPVINGPTEGLALIFCGHFFTAIVGA
EWWAQPFGKSIPLFSWVPFLNEIQMSRAILFMMIAFAVIPTLAFNTSNVYKVVHSRNGSMLLALAMLYPF
VTLIAGVLIWDYLSPIDLIANYPHLVVLGTGLAFGFLVGRMILAHLCDEPKGLKTNMCMSLLYLPFALAN
ALTARLNAGVPLVDEFWVLLGYCIFTLSLYAHFATSVIHEITEALGIYCFRITRKEA
>gnl|CDD|215548 PLN03042, PLN03042, Lactoylglutathione lyase; Provisional
MASASKESAANNPGLCGNPDEATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLG
YEDSETAPTDPPERTVWTFGRKATIELTHNWGTESDPEFKGYHNGNSDPRGFGHIGITVDDVYKACERFE
KLGVEFVKKPDDGKMKGLAFIKDPDGYWIEIFDLKRIGGITAGAA
>gnl|CDD|178606 PLN03043, PLN03043, Probable pectinesterase/pectinesterase inhibitor; Provisional
SPSLACKSTLYPKLCRSILSTVKSSPSDPYEYGKFSVKQCLKQARRLSKVINYYLTHENQPGKMTHEEIG
ALADCGELSELNVDYLETISSELKSAELMTDALVERVTSLLSGVVTNQQTCYDGLVDSKSSFAAALGAPL
GNLTRLYSVSLGLVSHALNRNLKKYKGRKGKIHGGGNKTVREPLETLIKVLRKSCDKSKDCRRGERNLGE
LGETSGGSILVSDAVIVGPYGTDNFTTITDAIAAAPNNSKPEDGYFVIYAREGYYEEYVVVPKNKKNIML
IGDGINKTIITGNHSVVDGWTTFNSSTFAVSGERFVAVDVTFRNTAGPEKHQAVALRNNADLSTFYRCSF
EGYQDTLYVHSLRQFYRECDIYGTVDFIFGNAAAIFQNCNLYARKPMANQKNAFTAQGRTDPNQNTGISI
INCTIEAAPDLAMDPNSTMNFLGRPWKPYSRTVYMQSYIGDLIQPVGWLEWNGTVGLDTIYYGEFDNYGP
GANTSMRVQWPGYNLMNLAQAMNFTVYNFTMGDTWLPQTDIPFYGGLL
>gnl|CDD|215549 PLN03044, PLN03044, GTP cyclohydrolase I; Provisional
MEQAVRTILECLGEDVEREGLLDTPKRVAKALLFMTQGYDQDPEVVLGTALFHEPEVHDGHEEMVVVRDI
DIHSTCEETMVPFTGRIHVGYIPNAGVILGLSKLARIAEVYARRLQTQERLTRQIADAIVESVEPLGVMV
VVEAAHFCMVMRGVEKHGASTTTSAVRGCFASNPKLRAEFFRIIRGGM
>gnl|CDD|178608 PLN03046, PLN03046, D-glycerate 3-kinase; Provisional
MAVASSLSSLISSNLQHYMNPIHAADYPIPCASAAAFNFNPISNPFNLKRRPYSPSSHKFNDRVAASCSS
YPSSKLSSRKTHLSCPGCGCSWIQDNSMVHDYATTAATSKRCSSLPTSSPALVSSVQDLYEFICSGPLVD
KIGYTPEKIAQSIDKWLLYGSQLCRLFQLNELKLTEPQKARIYHYYIPVFIWCEDQIAEHRSKFKDGDDI
PPLVIGFSAPQGCGKTTLVFALDYLFRVTGRKSATLSIDDFYLTAEGQAELRERNPGNALLELRGNAGSH
DLQFSVETLEALSKLTKEGIKMKVPRYDKSAYSGRGDRADPSTWPEVEGPLEVILFEGWMLGFKPLPNEV
VKAVDPQLEVVNKNLEAYYDAWDKFIDAWVVIKIQDPSCVYQWRLQAEIAMRADGKPGMSDEEVMDFVSR
YLPAYKAYLPTLYAEGPSGSDPDHVLVIDIDEERNPILAN
>gnl|CDD|215550 PLN03049, PLN03049, pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
VAVQHLHNPDSISYLSQREAIAIDEHLMGPLGFSVDQLMELAGLSVASAIAEVYSPSEYRRVLALCGPGN
NGGDGLVAARHLHHFGYKPSICYPKRTDKPLYNGLVTQLESLSVPFLSVEDLPSDLSSQFDIVVDAMFGF
SFHGAPRPPFDDLIQKLVRAAGPPPIVSVDIPSGWHVEEGDVNGEGLKPDMLVSLTAPKLCAKMFKGPHH
FLGGRFVPPAIVEKFKLHLPPYPGTSMCVRIGKTPSVDIAALRENYVGPELLEEQVNADPIDQFKEWFDD
AVAAGLREPNAMTLATAGEDGRPSARIVLLKGVDKRGFVWYTNYDSRKAHELSANPKASLVFYWDGLHRQ
VRVEGSVEKVSEEESDQYFHSRPRGSQIGALVSKQSTVIPGRHILDQSYKELEAKYADSSAIPKPKHWGG
YRLKPELIEFWQGRESRLHDRLQYTREEINGKSVWKIDRLAP
>gnl|CDD|215551 PLN03050, PLN03050, pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
MSNIQTGYLNAQDAAALDEELMSTPGFSLEQLMELAGLSVAEAVYEVADGEKASNPPGRHPRVLLVCGPG
NNGGDGLVAARHLAHFGYEVTVCYPKQSSKPHYENLVTQCEDLGIPFVQAIGGTNDSSKPLETTYDVIVD
AIFGFSFHGAPRAPFDTLLAQMVQQQKSPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKK
FEGRHFVGGRFLPPAIAEKYGLQKPPYPGVSQVMEV
>gnl|CDD|215552 PLN03051, PLN03051, acyl-activating enzyme; Provisional
MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAPA
KAIVLPAAGEPVAVPLREQDLSWCDFLGVAAAQGSVGGNEYSPVYAPVESVTNILFSSGTTGEPKAIPWT
HLSPLRCASDGWAHMDIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLALYGGAPLGRGFGKFVQDAGVT
VLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYKPVIEYCGGTELASGYI
SSTLLQPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVGEVALAPPMLGASDRLLNADHDKVYYKGMPM
YGSKGMPLRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRAVAGIAETAAVGVAPPDGG
PELLVIFLVLGEEKKGFDQARPEALQKKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLRDQLK
KELSGRSKL
>gnl|CDD|215553 PLN03052, PLN03052, acetate--CoA ligase; Provisional
AGMAGKSVDEITVGDLEAAGLSPEEAEKFFKELQVILTRAGASPPSIWRRISQSLLTPSHPFALHQLMYY
SCYKNWDSDTLGPPPAWFPSPEIAKLTNLGRLLEARGKELLGSKYKDPISSFSEFQRFSVENPEVYWSIV
LDELSLVFSVPPRCILDTSDESNPGGQWLPGAVLNVAECCLTPKPSKTDDSIAIIWRDEGSDDLPVNRMT
LSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISK
AKAIFTQDVIVRGGKSIPLYSRVVEAKAPKAIVLPADGKSVRVKLREGDMSWDDFLARANGLRRPDEYKA
VEQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHLDIRKGDIVCWPTNLGWMMGPWLVYASLL
NGATLALYNGSPLGRGFAKFVQDAKVTMLGTVPSIVKTWKNTNCMAGLDWSSIRCFGSTGEASSVDDYLW
LMSRAGYKPIIEYCGGTELGGGFVTGSLLQPQAFAAFSTPAMGCKLFILDDSGNPYPDDAPCTGELALFP
LMFGASSTLLNADHYKVYFKGMPVFNGKILRRHGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERV
CNAADESVLETAAIGVPPPGGGPEQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAVVIVP
SFPRTASNKVMRRVLRQQLAQELSRSKL
>gnl|CDD|178613 PLN03055, PLN03055, AMP deaminase; Provisional
IDAPSDEEEEVCAMMQECLELRDKYLFREKLPPWRKGIFESSTSKPNPDPFRYEPEPPSQHVFRMVDGVM
HVYAPDDAKEELFPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSA
PHRDFYNVRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDL
LDVHADKNTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIY
GRKQSEWDQLASWIVNNRLYSENVVWLIQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQL
HVFLKMVVGFDMVDDESKPERRPTKHMQTPEQWDIPFNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFR
PHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFAR
GLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNSVLQSGFPHASKKHWVGDNYWLRGP
AGNDIHKTNVPHMRVEFRHEVWKEELQYVFLGVAKISDKIDP
>gnl|CDD|166697 PLN03058, PLN03058, dynein light chain type 1 family protein; Provisional
MEGAELELERRSKFLSSLIQKKKAKEQQDQKDELNVRVRASDMPLVLQNRAFSCARDILDAMPGKLDSKR
LALALKKEFDSAYGPAWHCIVGTSFGSYVTHSTGGFLYFSIDKVYILLFKTAVEPLDQ
>gnl|CDD|166698 PLN03059, PLN03059, beta-galactosidase; Provisional
MLRGSLVVFLLLFLLFLLSSSWVSHGSASVSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKD
GGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVVQAAGLYVHLRIGPYICAEWNFGGFPVWLKYVPG
IEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEYGPVEWEIGAPGKAYTKWAADMAV
KLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFKPNKDYKPKMWTEAWTGWYTEFGGAVPNRPAEDLAFSV
ARFIQNGGSFINYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEPALV
SVDPTVTSLGSNQEAHVFKSKSACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLG
AQSSQMKMNPVGSTFSWQSYNEETASAYTDDTTTMDGLWEQINVTRDATDYLWYMTEVHIDPDEGFLKTG
QYPVLTIFSAGHALHVFINGQLAGTVYGELSNPKLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETWN
AGVLGPVTLKGLNEGTRDLSGWKWSYKIGLKGEALSLHTITGSSSVEWVEGSLLAQKQPLTWYKTTFDAP
GGNDPLALDMSSMGKGQIWINGQSIGRHWPAYTAHGSCNGCNYAGTFDDKKCRTNCGEPSQRWYHVPRSW
LKPSGNLLIVFEEWGGNPAGISLVKRTTDSVCADIFEGQPALKNWQIIASGKVNSLQPKAHLWCPPGQKI
SKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIGKQSCSVTVAPEVFGGDPCPDSMKKLSVEAVCS
>gnl|CDD|215554 PLN03060, PLN03060, inositol phosphatase-like protein; Provisional
DVPTVADTKASFLKAYRKPIPSIYSNVIQELLVQQHLMRYNATYKYDPIFALGFVTVYDQLMDGYPNATD
RDAIFKAYIEALGEDPDQYRKDAKKLEEWASSQSASGIADFNSGDGEVEAVLKDIAERAAGKTKFHYSRF
FAIGLFRLLECAKASDPAVLEKLSKALNVSKRSVDRDLDVYRNLLSKLAQAKELIKEYIDRSVCSV
>gnl|CDD|215555 PLN03063, PLN03063, alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional
MNYDDARGERPRLLVVANRLPVSAKRTGEDSWSLEMSPGGLVSALLGVKEFETKWIGWPGVDVHDEIGKA
ALTESLAEKGCIPVFLNEVFDQYYNGYCNNILWPIFHYMGLPQEDRHDATRTFESQYDAYKKANRMFLDV
VKENYEEGDVVWCHDYHLMFLPQYLKEYNNKMKVGWFLHTPFPSSEIYKTLPSRSELLRAVLTADLIGFH
TYDFARHFLSACTRILGVEGTHEGVVDQGKVTRVAVFPIGIDPERFINTCELPEVKQHMKELKRFFAGRK
VILGVDRLDMIKGIPQKYLAFEKFLEENPEWRDKVMLVQIAVPTRNDVPEYQKLKSQVHELVGRINGRFG
SVSSVPIHHLDCSVDFNYLCALYAITDVMLVTSLRDGMNLVSYEFVACQKAKKGVLVLSEFAGAGQSLGA
GALLVNPWNITEVSSAIKEALNMSDEERETRHRHNFQYVKTHSAQKWADDFMSELNDIIVEAELRTRNIP
LELPEQDVIQQYSKSNNRLLILGFYGTLTEPRNSQIKEMDLGLHPELKETLKALCSDPKTTVVVLSRSGK
DILDKNFGEYNIWLAAENGMFLRHTSGEWVTTMPEHMNLDWVDGVKNVFKYFTDRTPRSYVEKSETSLVW
NYEYADVEFGRAQARDMLQHLWAGPISNASVDVVRGQKSVEVHAIGVTKGAAIGRILGEIVHNKSMTTPI
DFVFCSGYFLEKDEDVYTFFEPEILSKKKSSSSNYSDSDKKVSSNLVDLKGENYFSCAIGQARTKARYVL
DSSNDVVSLLHKLAVANTTMTDSFSDV
>gnl|CDD|215556 PLN03064, PLN03064, alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional
MPGNKYNGQSSVNPTSRVERLLRERELRKSERSSNANDDLDTNAGSEAFENDLRLSEGDNDSSSHVEQLL
EGAAAESALPDGCERQEGRRPLRQRLLVVANRLPVSAVRRGEDSWSLEISAGGLVSALLGVKEFEARWIG
WAGVNVPDEVGQKALTKALAEKRCIPVFLDEEIVHQYYNGYCNNILWPLFHYLGLPQEDRLATTRSFQSQ
FAAYKKANQMFADVVNEHYEEGDVVWCHDYHLMFLPKCLKEYNSNMKVGWFLHTPFPSSEIHRTLPSRSE
LLRSVLAADLVGFHTYDYARHFVSACTRILGLEGTPEGVEDQGRLTRVAAFPIGIDSDRFIRALETPQVQ
QHIKELKERFAGRKVMLGVDRLDMIKGIPQKILAFEKFLEENPEWRDKVVLLQIAVPTRTDVPEYQKLTS
QVHEIVGRINGRFGTLTAVPIHHLDRSLDFHALCALYAVTDVALVTSLRDGMNLVSYEFVACQDSKKGVL
ILSEFAGAAQSLGAGAILVNPWNITEVAASIAQALNMPEEEREKRHRHNFMHVTTHTAQEWAETFVSELN
DTVVEAQLRTRQVPPQLPPEDAIQRYLQSNNRLLILGFNATLTEPVDTPGRRGDQIKEMELRLHPELKEP
LRALCSDPKTTIVVLSGSDRSVLDENFGEFDMWLAAENGMFLRHTKGEWMTTMPEHLNMDWVDSVKHVFE
YFTERTPRSHFETRETSLVWNYKYADVEFGRLQARDMLQHLWTGPISNAAVDVVQGSRSVEVRPVGVTKG
AAIDRILGEIVHSKSMTTPIDYVLCIGHFLGKDEDIYTFFEPELPSDSPAIARSRSPDGLKSSGDRRPSG
KLPSSRSNSKNSQGKKQRSLLSSAKSGVNHAASHGSDRRPSPEKIGWSVLDLKGENYFSCAVGRKRSNAR
YLLGSSDDVVSFLKELANASSSFP
>gnl|CDD|178617 PLN03065, PLN03065, isocitrate dehydrogenase (NADP+); Provisional
MLNKLMLRLLAYRPALALMPSSSSSAAANPLLASNPCRGIFNGGLSKNRRAFHVQFHRASSVRCFASAAA
ADRIKVQNPIVEMDGDEMTRVIWQMIKDKLIFPYLDLDIKYFDLGILNRDATDDKVTVESAEATLKYNVA
IKCATITPDEARVKEFGLKSMWRSPNGTIRNILNGTVFREPILCKNIPRLVPGWKKPICIGRHAFGDQYR
ATDTVIKGPGKLKMVFVPEDGNAPVELDVYDFKGPGVALAMYNVDESIRAFAESSMAMALQKKWPLYLST
KNTILKKYDGRFKDIFQEVYEEQWKQKFEEHSIWYEHRLIDDMVAYAVKSEGGYVWACKNYDGDVQSDLL
AQGFGSLGLMTSVLLSSDGKTLEAEAAHGTVTRHFRLHQKGQETSTNSIASIFAWTRGLEHRAKLDKNEE
LLDFVHKLESACIETVESGKMTKDLAILIHGPKVSREFYLNTEEFIDAVAQTLATKRGEPAVV
>gnl|CDD|215557 PLN03069, PLN03069, magnesiumprotoporphyrin-IX chelatase subunit H; Provisional
LFTQTNPEVRRIVPEDRRGRPTVKVVYVVLEAQYQSSLSAAVQNLNATSRKVCFEVVGYLVEELRDADNY
ETFKKDVEDANIFIGSLIFVEELAEKVKEAVEPERDRLDAVLVFPSMPEVMRLNKLGSFSMSQLGQSKSA
FAQFMKKKKQENGGFEEGMLKLVRTLPKVLKYLPSDKAQDARNFMMSLQFWLGGSPDNLENFLLMISGSY
VPALKGVKIEYADPVLFLDTGIWHPLAPTMYEDVKEYLNWYDTRRDMNFALKDKDAPVVGLVLQRSHIVT
GDDGHYVAVVMELEARGAKVVPIFAGGLDFSGPVERFFYDPITKKPIVDSVVSLTGFALVGGPARQDHPK
AIEALKKLDVPYLVALPLVFQTTEEWLDSTLGLHPIQVALQVALPELDGGLEPIVFAGRDSRTGKSHALH
DRVEQLCTRAIKWANLKRKTKAEKKLAITVFSFPPDKGNVGTAAYLNVFGSIFSVLKDLKRDGYNVGGLP
ETEEALIESVLHDKEAKFSSPNLNVAYKMSVREYQKLTPYAEALEENWGKPPGNLNSDGQNLLVYGKQYG
NVFIGVQPTFGYEGDPMRLLFSKSASPHHGFAAYYTFLEKIFKADAVLHFGTHGSLEFMPGKQVGMSDAC
YPDSLIGNIPNVYYYAANNPSEATIAKRRSYANTISYLTPPAENAGLYKGLKQLSELISSYQSLKDSGRG
PQIVSSIISTAKQCNLDKDVDLPEEAAELSADERDLVVGKVYSKIMEIESRLLPCGLHVIGEPPSAEEAV
ATLVNIAALDRPEDNISGLPGILAEAVGREIEDVYRGNDKGILADVELLQEITEASRAAVRAFVEKTTNS
KGQVVNVANKLTSLLGFGVKEPWVEALSNTKFYDADREKLRTLFDFLGFCLKQVVADNELGGLKEALEGQ
YVEPGPGGDPIRNPKVLPTGKNIHALDPQAIPTTAALASAKVVVDRLLERQKDENGGKYPETIALVLWGT
DNIKTYGESLAQVLWMVGVRPVADALGRVNKVEPVSLEELGRPRIDVVVNCSGVFRDLFINQMNLLDRAV
KMVAELDEPAEMNFVRKHALEQAEELGVSIREAATRVFSNASGSYSSNVNLAVENSSWNDEKQLQDMYLS
RKSFAFDSDAPGAGMEEKRDVFESALSTADVTFQNLDSSEISLTDVSHYFDSDPTKLVQSLRKDKKKPSS
YIADTTTANAQVRTLLRQLYMEVEDKIEGV
>gnl|CDD|178619 PLN03070, PLN03070, photosystem I reaction center subunit psaK 247; Provisional
MASTMMTTLPQFNGLRASSAAPVKSLVAVQPMRRKGKGALGARCDYIGSSTNLIMVTSTTLMLFAGRFGL
APSANRKATAGLKLEARDSGLQTGDPAGFTLADTLACGAVGHIIGVGVVLGLKNIGAL
>gnl|CDD|178620 PLN03071, PLN03071, GTP-binding nuclear protein Ran; Provisional
MALPNQQTVDYPSFKLVIVGDGGTGKTTFVKRHLTGEFEKKYEPTIGVEVHPLDFFTNCGKIRFYCWDTA
GQEKFGGLRDGYYIHGQCAIIMFDVTARLTYKNVPTWHRDLCRVCENIPIVLCGNKVDVKNRQVKAKQVT
FHRKKNLQYYEISAKSNYNFEKPFLYLARKLAGDPNLHFVESPALAPPEVQIDLAAQQQHEAELAAAAAQ
PLPDDDDDA
>gnl|CDD|178621 PLN03072, PLN03072, 60S ribosomal protein L12; Provisional
MPPKLDPSQVVEVYVRVTGGEVGAASSLAPKIGPLGLSPKKIGEDIAKETAKDWKGLRVTVKLTVQNRQA
KVSVVPSAAALVIKALKEPERDRKKVKNIKHNGNISLDDVIEIAKIMRPRSMAKELAGTVKEILGTCVSV
GCTVDGKDPKDLQQEIDDGEVEIPEA
>gnl|CDD|215558 PLN03073, PLN03073, ABC transporter F family; Provisional
AGMTEVASSVVLEVLGRRIRDVDSPIIDYIINVLADEDFDFGPEGEGAFDALGELLVAAECVSDDAECRL
VCSKLAEKFGKHGLVKPKPSVRSLAAPVRMSDGMDDSEVAKKKPEPDDGPLLSERDLAKIERRKRKEERQ
REVQYQAHVAEMEAAKAGMPGVYVNHDGNGGGPAIKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVG
RNGTGKTTFLRYMAMHAIDGIPKNCQILHVEQEVVGDDTTALQCVLNTDIERTQLLEEEAQLVAQQRELE
FETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWR
MRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLV
TYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVND
PDYKFEFPTPDDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQ
PSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSG
GQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEG
KVTPFHGTFHDYKKTLQS
>gnl|CDD|215559 PLN03074, PLN03074, auxin influx permease; Provisional
MMAGKQAETAIVGNYVEMEVEGGGEKEEGGGGGGKSRLKSLLWHGGSVYDAWFSCASNQVAQVLLTLPYS
FSQLGMLSGILFQIFYGLLGSWTAYLISVLYVEYRARKEREKVDFKNHVIQWFEVLDGLLGPYWKNVGLA
FNCTFLLFGSVIQLIACASNIYYINDNLDKRTWTYIFGACCATTVFIPSFHNYRIWSFLGLLMTTYTAWY
MTIAALSHGQVEGVKHSGPTKLVLYFTGATNILYTFGGHAVTVEIMHAMWKPQKFKYIYLAATLYVLTLT
LPSAAAVYWAFGDELLTHSNAFSLLPRSGWRDAAVILMLIHQFITFGFACTPLYFVWEKAIGVHDTKSIC
LRALARLPVVVPIWFLAIIFPFFGPINSAVGALLVSFTVYIIPSLAHMLTYRSASARQNAAEKPPFFLPS
WTGMYVVNAFVVVWVLVVGFGFGGWASMTNFVRQIDTFGLFAKCYQCPPPSPA
>gnl|CDD|178624 PLN03075, PLN03075, nicotianamine synthase; Provisional
SEEMGCQEELLVEKICDLYAQISKLESLKPSKEVNTLFTQLVSTCIPPSSIDVTKLCEEIQEMRSKLIKL
CGEAEGLLEAHFSTILGSFDNPLDHLNLFPYYNNYLKLSKLEFDLLSQHVNGVPTKVAFVGSGPLPLTSI
VLAKHHLPTTSFHNFDIDPSANDVARRLVSSDPDLSKRMFFHTADVMDVTESLKEYDVVFLAALVGMDKE
EKVKVIEHLGKHMAPGALLMLRSAHGARAFLYPVVDPCDLRGFEVLSVFHPTDEVINSVIIARKPGGPVG
SGVAGIGGVVSLPCNC
>gnl|CDD|215560 PLN03076, PLN03076, ARF guanine nucleotide exchange factor (ARF-GEF); Provisional
MASSEADSRLGKVVSPALEKIIKNASWRKHSKLAHECKAVIERLNSPEKNPPSTSSAAADSASASSLPGP
LHDGGSIEYSLAESELILSPLINACGTGSAKIVDPALDCIQKLIAHGYLRGEADPSGGPEALLLAKLIES
VCKCHDLGDEGIELLVLKTLLSAVTSTSLRIHGDCLLQAVRTCYDIYLGSKNVVNQTTAKASLIQMLVIV
FRRMEADSSTVPIQPIVVAELMEPAEKSDSDTSMTQFVQGFITKIMQDIDGVLNPATAGKSSGSGAHDGA
FETTATVETTNPADLLDSTDKDMLDAKYWEISMYKSALEGRKGELADGEVEKDDDLEVQIGNKLRRDAFL
VFRALCKLSMKTPPKEALADPQLMRGKILALELLKILLENAGAVFRTSDRFLGAIKQYLCLSLLKNSASS
LMIIFQLSCSIFISLVSRFRAGLKAEIGVFFPMIVLRVLENVAQPNFQQKMIVLRFLDKLCVDSQILVDI
FINYDCDVNSSNIFERMVNGLLKTAQGVPPGVETTLLPPQEAAMKLEAMKCLVAILRSMGDWMNKQLRLP
DPASLKKLDAVENNLEPGSLPVANGNGDENGEGSDSHSELSSETSDAATIEQRRAYKLELQEGISLFNRK
PKKGIEFLINANKVGESPEEIAAFLKDASGLNKTLIGDYLGEREDLSLKVMHAYVDSFDFQGMEFDEAIR
AFLQGFRLPGEAQKIDRIMEKFAERYCKCNPKAFSSADTAYVLAYSVIMLNTDAHNPMVKNKMSADDFIR
NNRGIDDGKDLPEEFMRSLYERISKNEIKMKEDDLVPQQKQSANSNRILGLDSILNIVIRKRGEDSYMET
SDDLIKHMQEQFKEKARKSESVYYAATDVVILRFMVEVCWAPMLAAFSVPLDQSDDEVVTFQCLEGFRHA
IHVTAVMSMKTHRDAFVTSLAKFTSLHSPADIKQKNIDAIKAIVSIADEDGNYLQEAWEHILTCVSRFEH
LHLLGEGAPPDATFFAAPQNESDKSKQAKSPILPVLKRKGPGKLQYAAAAVRRGSYDSAGVGGKASGVVT
SEQMNNLVSNLNMLEQVGSFEMNRIFTRSQKLNSEAIIDFVKALCKVSMEELRSPSDPRVFSLTKIVEIA
HYNMNRIRLVWSSIWHVLSDFFVTIGCSENLSIAIFAMDSLRQLSMKFLEREELANYNFQNEFMKPFVIV
MRKSNAVEIRELIIRCVSQMVLSRVNNVKSGWKSMFMVFTTAAYDDHKNIVLLAFEIIEKIIREYFPYIT
ETETTTFTDCVNCLIAFTNSRFNKDISLNAIAFLRFCATKLAEGDLGSSSRNKDKEAPPSSPQSGKDGKQ
ESGEFTDKDDHLYFWFPLLAGLSELSFDPRPEIRKSALQVLFDTLRNHGHLFSLPLWERVFESVLFPIFD
YVRHAIDPSGGDEPEGQGVDGDQGELDQDAWLYETCTLALQLVVDLFVKFYPTVNPLLKKVLMLLVSFIK
RPHQSLAGIGIAAFVRLMSNAGHLFSDEKWLEVVLSLKEAANATLPDFSYVVSGEYMPAENIQDSENAEA
ASSSTADNDAEAERSRRLYAAISDAKCRAAVQLLLIQAVMEIYNMYRPRLSAKNTLVLFDALHTVASHAH
KINSDTALRSKLQELGSMTQMQDPPLLRLENESYQICLTFLQNLILDKPPLAKEAEVESRLVELCEEVLQ
FYIETSTAGQDSEDSSSQQPRWLIPLGSGKRRELAARAPLVVATLQAVCGLGDSSFEKNLVRFFPLLAGL
ISCEHGSNEVQVALSDMLSSWVGPVLLQSC
>gnl|CDD|215561 PLN03077, PLN03077, Protein ECB2; Provisional
AQPPHFYLNPGKPNLFQLASHKAPNVLPYWNFHGRKRSRGLSVAASSSSSTHDSNSQLRALCSHGQLEQA
LKLLESMQELRVPVDEDAYVALFRLCEWKRAVEEGSRVCSRALSSHPSLGVRLGNAMLSMFVRFGELVHA
WYVFGKMPERDLFSWNVLVGGYAKAGYFDEALCLYHRMLWAGVRPDVYTFPCVLRTCGGIPDLARGREVH
AHVVRFGFELDVDVVNALITMYVKCGDVVSARLVFDRMPRRDCISWNAMISGYFENGECLEGLELFFTMR
ELSVDPDLMTITSVISACELLGDERLGREMHGYVVKTGFAVDVSVCNSLIQMYLSLGSWGEAEKVFSRME
TKDAVSWTAMISGYEKNGLPDKALETYALMEQDNVSPDEITIASVLSACACLGDLDVGVKLHELAERKGL
ISYVVVANALIEMYSKCKCIDKALEVFHNIPEKDVISWTSIIAGLRLNNRCFEALIFFRQMLLTLKPNSV
TLIAALSACARIGALMCGKEIHAHVLRTGIGFDGFLPNALLDLYVRCGRMNYAWNQFNSHEKDVVSWNIL
LTGYVAHGKGSMAVELFNRMVESGVNPDEVTFISLLCACSRSGMVTQGLEYFHSMEEKYSITPNLKHYAC
VVDLLGRAGKLTEAYNFINKMPITPDPAVWGALLNACRIHRHVELGELAAQHIFELDPNSVGYYILLCNL
YADAGKWDEVARVRKTMRENGLTVDPGCSWVEVKGKVHAFLTDDESHPQIKEINTVLEGFYEKMKASGLA
GSESSSMDEIEVSKDDIFCGHSERLAIAFGLINTVPGMPIWVTKNLYMCENCHNTVKFISKIVRREISVR
DTEQFHHFKDGECSCGD
>gnl|CDD|215562 PLN03078, PLN03078, Putative tRNA pseudouridine synthase; Provisional
AVSFLRAPWPLWRFWSSTSLLRRVNPRILRTSSSASSSPSSTSLSPPSSDPPLTDNSDQGGGMKWESARK
KKVVLRVGYVGTDYRGLQKQRDLSSLSTIEGELETAIFKAGGIRESNYGNLHKIGWARSSRTDKGVHSLA
TMISLKMEIPENAWKDDPDGIALAKFINSHLPDNIRVFSILPAQRSFDPRRECDLRKYSYLLPAEVIGIK
SGFSSEEIDEHISEFNSILNGFEGEHPFHNYTARSKYRKKLPGKHKQRNGAVSRRAKSSKEMSSSESEEN
HGEISEEDEEDLSFSSIPSGSSDENEDILKFQSSQVQIRARWLHEPDETDRISASHFRKIFRCSCGKLEK
SLGFDFVELSIWGESFMLHQIRKMVGTAVAVKRELLPRDIIRLSLTKFSRIVLPLAPSEVLILRGNSFSV
RKKPGNIKRPGMETMNESEEILKGVEEFYRAVMLPQVSKFLDPSKPPWKEWVENLDRFTSIPDAQLDEVR
KAWKVWKADYDRMKMARKSASSE
>gnl|CDD|178628 PLN03079, PLN03079, Uncharacterized protein At4g33100; Provisional
MVFKRSKSSSSRSSTSPCAELRTAYHNCFNRWYSEKFVKGQWDKEDCVAEWHKYRACLSEHLEDKHLSQI
LEVDGTSAPYKQADADSSSGQ
>gnl|CDD|178629 PLN03080, PLN03080, Probable beta-xylosidase; Provisional
MNTQLRPLFLLLFLLALGATFKAADAHPQFPCKPPTFSAYPFCNASLPIPARARSLVSLLTLDEKIAQLS
NTAAGVPRLGIPPYEWWSESLHGLADNGPGVSFNSGPVSAATSFPQVILSAASFNRSLWRAIGSAIAVEA
RAMYNAGQAGLTFWAPNINIFRDPRWGRGQETPGEDPAVASAYSVEFVKGFQGGKWKKVRDDGEDGKLML
SACCKHYTAYDLEKWGNFSRYTFNAVVTEQDMEDTYQPPFKSCIQEGKASCLMCSYNQVNGVPACARKDL
LQKARDEWGFQGYITSDCDAVATIFEYQTYTKSPEDAVADVLKAGMDINCGSYMLRHTQSAIEKGKVQEE
DIDRALFNLFSVQLRLGLFDGDPRNGWYGKLGPNNVCTKEHRELALEAARQGIVLLKNDKKFLPLNKSEV
SSLAIIGPMANDPYNLGGDYTGVPCQPTTLFKGLQAYVKKTSFAAGCKDVSCNSDTGFGEAIAIAKRADF
VVVVAGLDLSQETEDHDRVSLLLPGKQMDLISSVASVSKKPVVLVLTGGGPVDVSFAKQDPRIASILWIG
YPGEVGGQALAEIIFGDYNPGGRLPMTWYPESFTAVPMTDMNMRADPSRGYPGRTYRFYTGDVVYGFGYG
LSYTKFSYKILSAPKKLSLSRSSVQDSISRKPLLQRRDELDYVQIEDIASCESLRFNVHISVSNVGEMDG
SHVVMLFSRSPPVVPGVPEKQLVGFDRVHTASGRSTETEIVVDPCKHLSVANEEGKRVLPLGDHVLMLGD
LEHSLSIEI
>gnl|CDD|215563 PLN03081, PLN03081, pentatricopeptide (PPR) repeat-containing protein; Provisional
MEIPLARYQSIRLDEIRDSLSNPRLLHSPRKFSLRGRRTKTPFSSISCSSVEQGLKPRPRLKPEPIRIEV
SESKDARLDDTQIRKSGVSLCSQIEKLVACGRHREALELFEILEAGCPFTLPASTYDALVEACIALKSIR
CVKAVYWHVESSGFEPDQYMMNRVLLMHVKCGMLIDARRLFDEMPERNLASWGTIIGGLVDAGNYREAFA
LFREMWEDGSDAEPRTFVVMLRASAGLGSARAGQQLHCCVLKTGVVGDTFVSCALIDMYSKCGDIEDARC
VFDGMPEKTTVAWNSMLAGYALHGYSEEALCLYYEMRDSGVSIDQFTFSIMIRIFSRLALLEHAKQAHAG
LIRTGFPLDIVANTALVDLYSKWGRMEDARNVFDRMPRKNLISWNALIAGYGNHGRGTKAVEMFERMIAE
GVAPNHVTFLAVLSACRYSGLSEQGWEIFQSMSENHRIKPRAMHYACMIELLGREGLLDEAYAMIRRAPF
KPTVNMWAALLTACRIHKNLELGRLAAEKLYGMGPEKLNNYVVLLNLYNSSGRQAEAAKVVETLKRKGLS
MHPACTWIEVKKQDHSFFSGDRLHPQSREIYQKLDELMKEISEYGYVAEENELLPDVDEDEEKVSGRYHS
EKLAIAFGLINTSEWTPLQITQSHRICKDCHKVIKFIALVTKREIVVRDASRFHHFKLGKCSCGDYW
>gnl|CDD|215564 PLN03082, PLN03082, Iron-sulfur cluster assembly; Provisional
MASSMSRSLLRRVAPLLAGRIRQNHRLLNFSSSSALKEASTSSSSPSSSASLDAVHMTDNCIRRLKELQT
SEPSAEDKMLRLSVETGGCSGFQYVFELDDKTNSDDRVFEKDGVKLVVDNISYDFVKGATVDYVEELIRS
AFVVSTNPSAVGGCSCKSSFMVK
>gnl|CDD|215565 PLN03083, PLN03083, E3 UFM1-protein ligase 1 homolog; Provisional
MDAELLELQRQFEFAQQAKSSVRLSERNVVELVQKLQELGIIDFDLLHTVSGKEYITQDQLRNEIEAEIK
KLGRVSLVDLADTIGVDLYHVERQAQQVVSDDPGLMLVQGEIISQSYWDSIAEEINERLQECSQIALAEL
ARQLQVGSELVTSMLEPRLGTIVKARLEGGQLYTPAYVARVTAMVRGAARGITVPTNLSSLWNSLQQLLR
EMDGAGGVTVEGSFFQSIFNGLVKEEEVLGSLRAGTHWTPAVFAHAQKESVDAFFSQNSYITYDTLQKLG
ISQPKQFLQSRYPDGIALDAVFVHSSMIEMLDSAAEDAIEGGSWIDSLSVLPSSFGSQDAGKLLLLCPSV
QSALKDSKALILGESCVLSNGFIKGIYDQIEKEMDAFSIQASSAGLIGSSEKSLGSNESSPAASNSDKGS
KKKKGKSTSTKGGTAESIPDDEEDAPKKGKKNQKKGRDKSSKVPSDSKAGGKKESVKSQEDNNNIPPEEW
VMKKILEWVPDLEEDGTEDPGSILKHLADHLRPMLINSLKERRKALFTENAERRRRLLDNLQKKIDESFL
NMQLYEKALDLFEDDQSTSVVLHRHLLRTTAAEIADTLLHTLDIHNKLKNGTEVEDSKTQDTVLLSSAER
TALAKNLPGSLSSKALALVEALEGKRVDAFMSTLRDLAEESGLRLKKLDKKLERTLLHSYRKDLTSQVST
ESDPVALLPKVVSLLYVQVHNKALQAPGRAISAAISRLKDKLPDSAYKTLTDYHSATVTLLALMSAATGE
EHDCSSDRILTKRELLESLMPPLKSLVLGDSQP
>gnl|CDD|178633 PLN03084, PLN03084, alpha/beta hydrolase fold protein; Provisional
MAVQAHNPNSFHSHHFASAPPSSYLRSPHSARKSLSFICKSSDEDDYLIDAPVSVGDGFSFSGGKYSDEP
SPSDEWFAQGKFVKAHSVQGSGNKAKDPIFGLKMGAQSQASSDLFRWFCVESGSNNNPPVLLIHGFPSQA
YSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLIDELKSDKVSLVVQGYFSPP
VVKYASAHPDKIKKLILLNPPLTKEHAKLPSTLSEFSNFLLGEIFSQDPLRASDKALTSCGPYAMKEDDA
MVYRRPYLTSGSSGFALNAISRSMKKELKKYIEEMRSILTDKNWKTPITVCWGLRDRWLNYDGVEDFCKS
SQHKLIELPMAGHHVQEDCGEELGGIISGILSK
>gnl|CDD|215566 PLN03085, PLN03085, nucleobase:cation symporter-1; Provisional
LALGGAASRRLIRKSALNQGHLLYKTRCASFSSASSSWWSSSPDLTASSKRKEKKAPHRLSAVIDAVNDR
KLPPELRGRRNSVRSETDIINVVEQRIWHSMEEGHFENLPGKGKPLNLSTNPHADPAEDTLYRILSKNGC
APEWVELNKEIRGQINEWRSALKKAWANRCEGDDSQWIEDSRLLQEQLRQINNKVFRYNLIVPFGRQMFG
LKWEKEVDRLK
>gnl|CDD|178635 PLN03086, PLN03086, PRLI-interacting factor K; Provisional
MDFELRRAREKLEREQRERKQRAKLKLERERKAKEEAAKQREAIEAAQRSRRLDAIEAQIKADQQMQESL
QAGRGIVFSRIFEAVSFQGNGDKIKLPPSCFTELSDQGAFDKGPLYFRLSVVHQEGSGEMKDTDSQKTTH
SGVLEFTAEEGSVGLPPHVWSNLFPSDPPDVPLVEVRYIWLPKGTYAKLQPDGVGFSDLPNHKAVLETAL
RQHATLSEDDVLVVNYGQLTYKLKVLELKPASSVSVLETDIEVDIVGPDSVSNEENQHVLKPLEFGKSES
GMVEEGNYRYYKFSIDEDTWEKVASGDARVEVKIDAETSGGDTDLYVSKHPLVFPTRHQHEWSSHDMGSK
VLILKSKDASLSSGTYSIGVYGFKGTTKYQVSVSVQDNNNQKVGEQASSSSSMDVDTVECRNCKHYIPSR
SIALHEAYCSRHNVVCPHDGCGIVLRVEEAKNHVHCEKCGQAFQQGEMEKHMKVFHEPLQCPCGVVLEKE
QMVQHQASTCPLRLITCRFCGDMVQAGGSAMDVRDRLRGMSEHESICGSRTAPCDSCGRSVMLKEMDIHQ
IAVHQKS
>gnl|CDD|215567 PLN03087, PLN03087, BODYGUARD 1 domain containing hydrolase; Provisional
MAAAKARSALMGAGRALNEAVSFVVFSLLDILDFLLCFVYKVADYFFEAEWKPCYCSSAKEAIAASGKIL
VSERGGESKVVSLSSTKLHLEEISDTLYTRPSLLSDASKLTVNELKKLKMEGKCVGSCEKTSNKRKRGTK
KSTLTVNSTIVEMLRGKIGGQQLHPAPRWSDCDCKFCTSWLSSSNESLFVHVQQPKDNKAKEDVLFIHGF
ISSSAFWTETLFPNFSDAAKSTYRLFAVDLLGFGRSPKPADSLYTLREHLEMIERSVLERYKVKSFHIVA
HSLGCILALALAVKHPGAVKSLTLLAPPYYPVPKGVQATQYVMRKVAPRRVWPPIAFGASVACWYEHISR
TICLVICKNHRLWEFLTRLLTRNRMRTFLIEGFFCHTHNAAWHTLHNIICGSGSKLDGYLDHVRDQLKCD
VAIFHGGDDELIPVECSYAVKAKVPRARVKVIDDKDHITIVVGRQKEFARELEEIWRRSSG
>gnl|CDD|215568 PLN03088, PLN03088, SGT1, suppressor of G2 allele of SKP1; Provisional
MAKDLEDKAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLA
KAYLRKGTACMKLEEYQTAKAALEKGASLAPGDSRFTKLIKECDEKIAEEEKDLVQPVPSDLPSSVTAPP
VEEADATPVVPPSKPKYRHEFYQKPEEVVVTVFAKGVPAENVNVDFGEQILSVVIEVPGEDAYHLQPRLF
GKIIPDKCKYEVLSTKIEIRLAKAEPITWASLEYGKGPAVLPKPNVSSEVSQRPAYPSSKKKKDDWDKLE
AEVKKEEKDEKLDGDAALNKFFREIYQNADEDTRRAMMKSFVESNGTVLSTNWKEVGSKKIEGSPPDGME
LKKWEY
>gnl|CDD|215569 PLN03089, PLN03089, hypothetical protein; Provisional
MALMHSLLLLLLLLLCAAAASAAPVTDGLLPNGDFETPPKKSQMNGTVVIGKNAIPGWEISGFVEYISSG
QKQGGMLLVVPEGAHAVRLGNEASISQTLTVTKGSYYSLTFSAARTCAQDESLNVSVPPESGVLPLQTLY
SSSGWDSYAWAFKAESDVVNLVFHNPGVEEDPACGPLIDAVAIKTLFPPRPTKDNLLKNGGFEEGPYVFP
NSSWGVLLPPNIEDDTSPLPGWMIESLKAVKYIDSAHFSVPEGKRAVELVSGKESAIAQVVRTVPGKSYN
LSFTVGDANNGCHGSMMVEAFAGKDTQKVPYESQGKGGFKRASLRFKAVSNRTRITFYSSFYHTKSDDFG
SLCGPVVDDVRVVPVRAPRAGKP
>gnl|CDD|178639 PLN03090, PLN03090, auxin-responsive family protein; Provisional
MAIKKSNKLTQTAMLKQILKRCSSLGKKQGYDEDGLPLDVPKGHFPVYVGENRSRYIVPISFLTHPEFQS
LLQQAEEEFGFDHDMGLTIPCEEVVFRSLTSMIR
>gnl|CDD|215570 PLN03091, PLN03091, hypothetical protein; Provisional
MGRHSCCYKQKLRKGLWSPEEDEKLLRHITKYGHGCWSSVPKQAGLQRCGKSCRLRWINYLRPDLKRGTF
SQQEENLIIELHAVLGNRWSQIAAQLPGRTDNEIKNLWNSCLKKKLRQRGIDPNTHKPLSEVENGEDKNP
PTDDKSDKASSVVSNELNLLKADNSKPLAALQEKRSSSISPAGYQLEVESSSSSKINNSNNNNHSNSNLM
TPTPNKDFFLDRFTTSHESSTTSCRPSDLVGHFPFQQLNYASNARLSTNPNPTLWFSQNSKSFEMNSEFS
SSMTPSILPPSVTSSFLPTPMSYKPSISLPSDNPSIPSFTVNGVRNWEAGAFSNNSNSSNGSSSSIELQS
NSSFFENSIFSWGLADCGKSDKEAQIHLLESDPEDIKWPEYLQNPFLMAATLQNQTPQPLYNEIKPETHF
ITEGSSTMWPHNQQQQEPLQNPDIYTKDLQRLTAAFGQI
>gnl|CDD|178641 PLN03093, PLN03093, Protein SENSITIVITY TO RED LIGHT REDUCED 1; Provisional
KELTVDNSSSNGEWTVVLPRRGKRRRKPKPKGTPEEEQQPWVPTDLESDPERQAKLIQKMEICIKKVESS
QFYQAFLEQVKSPEVLDSFHLVLGSELKMQMVIYGIGSIESYETPRFQLSLAILMKREFDWIGDIEVFDP
VLSATESRVLESLGCSVLSVNEQGRREATKPTLFFMPHCEAELYNNLLQANWRMERLNHIALFGNSFEMY
EEQVSEFFNSEVVDSTKHILAARKFTSEFAIKTVSDDYFAAFHDSSWHFFSPGIDTELPLFKN
>gnl|CDD|178642 PLN03094, PLN03094, Substrate binding subunit of ER-derived-lipid transporter; Provisional
LPPSSSMISSLPSSSNGLPFLPPKPQTRLLLVRAMSNATAAAASPPSSEGSKNPLAVVLEVPRNIWRQTL
KPLSDFGFGKRSVWEGGVGLFLLSGAALLALTLAWLRGFQLRSKFRKYQAVFEFPQACGICVGTPVRIRG
VTVGNVVRVRPSLEKIDVVVEVEDDKIVIPRNSLVEVNQSGLIMETLIDITPRDPIPKPSVGPLDPECEK
EGLIVCDRERIKGEQGVSLDELVGICTRLAREMEAIGVAKMYALAERAADLMEEARPLLLKIQAMAEDLQ
PLLSEVRDSGLLKEVEKLTRVAAEASEDLRRLNSSILTPENTELLRQSIYTLTKTLKHIESISSDISGFT
GDEATRRNLKQLIQSLSRLL
>gnl|CDD|215571 PLN03095, PLN03095, NADH:ubiquinone oxidoreductase 18 kDa subunit; Provisional
NVLVLASRAGRLVGEDEFGNKYYENPSYQSGRHRWVEYADKDDYNASNIPPEWHGWLHYVNDEPGELEDR
TAPRYQLEFIAGGTTTGTQYMYHPKGHFLSKRPRNWKRYTPWSPP
>gnl|CDD|215572 PLN03096, PLN03096, glyceraldehyde-3-phosphate dehydrogenase A; Provisional
FSAAKPSLQAGSKGFSEFSGLKSSSAVTFGKRSDSLDFVVFATSAVSSSGGARRAVTEAKIKVAINGFGR
IGRNFLRCWHGRKDSPLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKPVGDDAISVDGKVIKVVSDRN
PLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADDYKHSDPIISNA
SCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVL
PNLKGKLNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDV
SSTIDSSLTMVMGDDMVKVVAWYDNEWGYSQRVVDLADIVANKWK
>gnl|CDD|178645 PLN03097, FHY3, Protein FAR-RED ELONGATED HYPOCOTYL 3; Provisional
MDIDLRLPSGDHDKEDEEPNGVDNMLSEVKLHNGDMEIGNVVDVAEEVLSIDGGDMNSPTGELVEFKEDT
NLEPLSGMEFESHGEAYSFYQEYARSMGFNTAIQNSRRSKTSREFIDAKFACSRYGTKREYDKSFNRPRA
RQTKQDPENGTGRRSCAKTDCKASMHVKRRPDGKWVIHSFVKEHNHELLPAQAVSEQTRKMYAAMARQFA
EYKNVVGLKNDSKSSFDKGRNLGLEAGDTKILLDFFTQMQNMNSNFFYAVDLGEDQRLKNLFWVDAKSRH
DYGNFSDVVSFDTTYVRNKYKMPLALFVGVNQHYQFMLLGCALISDESAATYSWLMQTWLRAMGGQAPKV
IITDQDKAMKSVISEVFPNAHHCFFLWHILGKVSENLGQVIKQHENFMAKFEKCIYRSWTEEEFGKRWWK
ILDRFELKEDEWMQSLYEDRKQWVPTYMRDAFLAGMSTVQRSESINAFFDKYVHKKTTVQEFVKQYETIL
QDRYEEEAKADSDTWNKQPALKSPSPLEKSVSGVYTHAVFKKFQVEVLGAVACHPKMESQDETSITFRVQ
DFEKNQDFTVTWNQTKLEVSCICRLFEYKGYLCRHALVVLQMCQLSAIPSQYILKRWTKDAKSRHLLGEE
SEQVQSRVQRYNDLCQRALKLSEEASLSQESYNIAFRALEEAFGNCISMNNSNKSLVEAGTSPTHGLLCI
EDDNQSRSMTKTNKKKNPTKKRKVNSEQEVTTVAAQDSLQQMDKLSSRAVALESYYGTQQSVQGMVQLNL
MAPTRDNYYGNQQTIQGLGQLNSIAPSHDGYYGTQQSIHGLGQMDFFRTPAGFSYDIRDDPNVRTAQLHD
DASRHA
>gnl|CDD|215573 PLN03098, LPA1, LOW PSII ACCUMULATION1; Provisional
MAVATAPALNMHLLCFSSCPRSRVKQRRSWLPPGDATLVNLRRGRAPRRLLFGRSSSSPSSSPAKDGSEA
DVKTAEDAVNLGLSLFSKGRVKDALAQFETALELNPNPDEAQAAYYNKACCHAYREEGKKAADCLRTALR
DYNLKFSTILNDPDLAPFRASPEFKELQEEARKGGEDIGSSFRRDLKLISEVQAPFRGVRKFFYVAFTAA
AGISTFFTVPRLIRAIQGGDGAPDVLETAGNAAINIGGIVAFVSLFLWENKKEEEQMSQITRDETLSRLP
VRLSTNRIVELVQLRDITRPVILAGTKESVTLAMQKAERYRTELLKRGVLLIPVVWGENKDPQPKKKGFG
RSSKAAASLPSIGDDFEKRAQSAAAKSVLKGEKRFKAEVVSPAEWERWIRDQQESEGVTPGEDVYIILRL
DGRVRRSGRGMPEWQEIVKELPPLDSLLSKLER
>gnl|CDD|215574 PLN03099, PIR, Protein PIR; Provisional
MAVPVEEAVAALSTFSLEDEQPDVQGLAVTLSAGRAATESPIDYSDVAAYQLSLSEDTKAINQLNTLIQE
GKEMVSILYTYRSCVKALPQLPESMKHSQADLYLETYQVLDLEIGRLREIQRWQSSAASKLAADMQRFSR
PERRINGPTVTHMWSMLKLLDVLLQLDHLKNAKASIPNDFSWYKRTFTQVSTQWPDTDTMREELDDLQIF
LSTRWAILLNLQAEMFRVNNVEDILQVLIVFCLESLESDFVLLYSERHILLRVLPVLVVLATSSEKEGES
LFKRIKINRLINIFQREYLIVNHMGAIRAEHDDFCIRFASAMNQLQLLKSADGVDTAWSREIKENMYDVV
VEGFQLLSEWTGRIWEQCAWKFSRPAKDATPDPERSGSVTDYEKVVRCNYTAEERKALVELIGYIKGVGS
MLERCDTLVADALWETIHAQVQDFVQNKLATMLRTTFRKKKELSRILSDMRTIAADWMANTRPEEKMPSR
QRENDESRPNFFYPRPVAPTAAQLHCLQFLIHELVSGGSPKKPGGFFGNNGSEIPVNDLKQLETFFNKLA
FFPHILDYRATIGHLTDLGFLWFREFYLETSRVIQFPIECSLPWMLVDYILESQDAGLLESVLLPFDIYN
DSAQHALRVLKQRFLYDEIEAEVDLCFDQLVSKLSESIFTYYKSRAASKLLDPSFLAAVDNGEKFSVQPK
RYDALFKMRRVKILGRTIDLASLIAQRMNKIFRENLDFLFERFESQDLCSVVELQRLVEILRLTHELLSE
HLSIDPFSLMLGEMQENISLVSFSSRLASQIWSEMQNDFLPNFILCNTTQRFVRSSKVPQRPTRRPSVPS
AKPSFLCGTQDLNMAHQSFAELHSKFFGLPHMFAIVKLLGSRSLPWLIRALLDHLSQKITTLEPMIEDLR
EAMPKAIGLPSFDGGVAGCMKIFREQLQWGTKYEGKSEVLRGLKEIGSLIFWMSLLDIAMREVETVQFMQ
VAPWLGLVPGKEGQLQQADDNESPLVSLFKEATSAVVSSPGCLNPSAFVSMSKQAEVADLLYKSNLNTGS
VLEYTLAFTSAVLDRHRSKWSAPPKTGFIDITTSKDFYRIYSGLQYVYLEEISAEGSAFHERLGDSVAWG
GCTIVYLLGQQLRFELLDFIYHVLSVSEVESASASHTHRNERLKSPSYHQGWEGFLENARKARRLNNHVF
SLLRARCPLEDKLASMIKQSGAPVHRVKYPNTPSAFETLPQK
>gnl|CDD|215575 PLN03100, PLN03100, Permease subunit of ER-derived-lipid transporter; Provisional
LRQRRLYVNLNANDGHPSMSALEEETSSENNEPSSEAELPLSKWSPPKYLWRGLSTLLLAGQVILRILKG
KIHWRNTLQQLERVGPKSLGVSLLTSSFVGMVFTIQFVREFTKLGLTRSIGGVLALAFSRELSPVVTAIV
LAGRVGSAFAAELGTMQVSEQTDTLRVLGTDPVDYLVTPRVIACCLALPILTLMCFTVGMAASALLADSV
YGVSANIILDSAARALRPWDIVSAMIKSQVFGAIISVISCAWGVTTTGGAKGVGESTTSAVVISLVGIFI
ADFFLSSFFFQG
>gnl|CDD|215576 PLN03102, PLN03102, acyl-activating enzyme; Provisional
MDNLALCEANNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVL
APNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLN
LPVIFIHEIDFPKRPSSEELDYECLIQRGEPTPSLVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRG
AYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCC
VPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDEWN
RLPENQQMELKARQGVSILGLADVDVKNKETQESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAFKHG
WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVV
LEKGETTKEDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLVVEDE
DNVIKKVHQRPVEHFSSRL
>gnl|CDD|215577 PLN03103, PLN03103, GDP-L-galactose-hexose-1-phosphate guanyltransferase; Provisional
MLTIKRVPTVVSNYQDDDELGGCGRNCLGKCCLPGAKLPLYAFKKVSKDDSGKLGSFSSKPEPSVSFLDS
LLLAQWEDRMARGLFRYDVTACETKVIPGKYGFIAQLNEGRHLKKRPTEFRVDKVLQPFDGKKFNFTKVG
QEEVLFQFEQGEDDIPEFFPSAPIDASNSPNVVAINVSPIEYGHVLLVPRVLDCLPQRIDPDSFLLALYM
AAEANNPYFRVGYNSLGAFATINHLHFQAYYLANPFPVEKAPTVRIPHGTAKSGVKVSELVDYPVRGLVF
EGGSDLEDLANSVADACICLQDNNIPYNLLISDCGKRVFLFPQCYAEKQALGEVSQELLDTQVNPAVWEI
SGHIVLKRKEDYERATEEYAWRLLAEVSLSEERFQEVKALCFAASAADCLVMQ
>gnl|CDD|215578 PLN03104, FHL, FAR-RED-ELONGATED HYPOCOTYL1-LIKE; Provisional
VEVDNNNEKPSEINSNILTFMIVAVESLDVSKKRKLQAEESDLLPLPKHFCFENQASLVNSSVPSSIIDY
AECSYAMEYTKTSDEASSSASFTGPSLYMFKDSIYSTGSSSSGYAATSSIEQCFSKVDHKTQEDFSDFTH
MEFIYHDSEFAVEDLQEVLNPVASYVLSSARWSVNNQDSTEATTKPTIDQEFEQYFSTLMM
>gnl|CDD|178652 PLN03105, TCP24, transcription factor TCP24 (TEOSINTE BRANCHED1, CYCLOIDEA, AND PCF FAMILY 24); Provisional
MEVDEDIELQKHQEQQSRKLQRFSEDNTGLMRNWNNPSSRIIRVSRASGGKDRHSKVLTSKGLRDRRIRL
SVATAIQFYDLQDRLGFDQPSKAVEWLINAASDSITDLPLLNTNFDHLDQNQNQTKSACSSGTSESSLLS
LSRTEIRGKARERARERTAKDRDKDLQNAHSSFTQLLTGGFDQQPSNRNWTGGSDCFNPVQLQIPNSSSQ
EPMNHPFSFVPDYNFGISSSSSAINGGYSSRGTLQSNSQSLFLNNNNNITQRSSISSSSSSSSPMDSQSI
SFFMATPPPLDHHNHQLPETFDGRLYLYYGEGNRSSDDKAKERR
>gnl|CDD|215579 PLN03106, TCP2, Protein TCP2; Provisional
MEVEEIQTQPCKFSRVGNGRNDATKIGQKGNGQYPDNEEDGEVVDGGGGGSVNNRLRRWHHSSRIIRVSR
ASGGKDRHSKVLTSKGLRDRRVRLSVSTAIQFYDLQDRLGYDQPSKAVEWLIKAAEDSISELPSLNNSFP
DTPKQLSDEKRTSDGTEQGFDSDDEEHENQTLTQNQAQHNSLSKSACSSTSDTSKGSGLSLSRSELRDKA
RERARERTAKEKEKEDHNHAAHHNNNNPISQNSSFTELLTGGIDPVNNNRQWMASAPSGQKAAAARQWPS
PMDYFGSGLLGGSSSRTHHSSGFPGQIQLGNSIPQPISTNSHPFSSIGDHHHHHHHQHQHFSFVPDHLIP
VATSNASGGDFNLNFTISSGLAGFNRGTLQSNSTSHQSLLPHLQRFSTSEPIDGSNVPFFFGAAPAENHH
HNHQFPPGQLYYGDGCRHSDQKGKGKN
>gnl|CDD|215580 PLN03107, PLN03107, eukaryotic translation initiation factor 5A; Provisional
MSDEEHHFESADAGASKTYPQQAGTIRKGGYIVIKGRPCKVVEVSTSKTGKHGHAKCHFVAIDIFTGKKL
EDIVPSSHNCDVPHVNRTDYQLIDISEDGFVSLMDESGNTKDDLKLPTEDDTLAEQIKDGFDEGKDLVVT
VMSAMGEEQICALKEIGPK
>gnl|CDD|178655 PLN03108, PLN03108, Rab family protein; Provisional
MSYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDNKPIKLQIWDTAGQESFRS
ITRSYYRGAAGALLVYDITRRETFNHLASWLEDARQHANANMTIMLIGNKCDLAHRRAVSTEEGEQFAKE
HGLIFMEASAKTAQNVEEAFIKTAAKIYKKIQDGVFDVSNESYGIKVGYGAIPGASGGRDGTSSQGGGCC
>gnl|CDD|215581 PLN03109, PLN03109, ETHYLENE-INSENSITIVE3-like3 protein; Provisional
MGHLAILAAELGDSSDFEVDGIRCDNLTENDVSDEEIEAEDLERRMWKDRIKLKRIKERQKKLQQAALEK
SKPKKISDQARRKKMSRAQDGILKYMLKLMEVCKARGFVYGIIPEKGKPVSGASDNIRAWWKEKVKFDKN
GPAAIAKYEAECLAMGEAESSGNNSQHSLQDLQDATLGSLLSSLMQHCDPPQRKYPLEKGVPPPWWPSGN
EDWWVKLGLPKGQSPPYKKPHDLKKMWKVGVLTAVIKHMSPDFDKIRRHVRQSKCLQDKMTAKESLIWLG
VLNREESLIRQPSSDNGTSGITETPRGGHEDRNKDAISSDSDYDVDGLEDAPGSVSSKDDRRNLQPVAQE
PERARDDAPNQVVPDKEKTKKPRKRKRPRGRSTVAEQEVEVTQEHPPAESRNALPDMNHVDAQGMEYQIT
GTSHENDTVTALQALGNGQEGFHLLPPAEFNNYNSNPSANANPSSIYVGGRPLLYPNNDNSELHSGNSYP
GFYNPSSVYQHNPDKQPLPLSIMDHQVPPPGTGALADSSSYRLHILGLSGNSNTIVGGELQQLMSDPFPG
EQDGSPFEGLPFDYGGFSSPFPDIDDLLDDDDLIQYFGA
>gnl|CDD|178657 PLN03110, PLN03110, Rab GTPase; Provisional
MAHRVDHEYDYLFKIVLIGDSGVGKSNILSRFTRNEFCLESKSTIGVEFATRTLQVEGKTVKAQIWDTAG
QERYRAITSAYYRGAVGALLVYDITKRQTFDNVQRWLRELRDHADSNIVIMMAGNKSDLNHLRSVAEEDG
QALAEKEGLSFLETSALEATNVEKAFQTILLEIYHIISKKALAAQEAAANSGLPGQGTTINVADTSGNNK
RGCCST
>gnl|CDD|215582 PLN03111, PLN03111, DNA-directed RNA polymerase II subunit family protein; Provisional
MDTGSEESTRLYLVRRTVLEMLRDRGYLVSDSELNLTLSEFREKFGEKPKREDLRISAPKRSDPSKKILV
FFPEEEKVGVKTIKTYAERMKDENVSRAILVLQSKLTPFAKQALSEFNSKFKIEVFQETELLVNITKHVL
VPKHQVLTDEEKKTLLKRYTVKETQLPRIQVSDPIARYYGLKRGQVVKIIRPSETAGRYVTYRCVV
>gnl|CDD|215583 PLN03112, PLN03112, cytochrome P450 family protein; Provisional
MDSFLLSLLFSVLIFNVLIWRWLNASMRKSLRLPPGPPRWPIVGNLLQLGPLPHRDLASLCKKYGPLVYL
RLGSVDAITTDDPELIREILLRQDDVFASRPRTLAAVHLAYGCGDVALAPLGPHWKRMRRICMEHLLTTK
RLESFAKHRAEEARHLIQDVWEAAQTGKPVNLREVLGAFSMNNVTRMLLGKQYFGAESAGPKEAMEFMHI
THELFRLLGVIYLGDYLPAWRWLDPYGCEKKMREVEKRVDEFHDKIIDEHRRARSGKLPGGKDMDFVDVL
LSLPGENGKEHMDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQES
DLVHLNYLRCVVRETFRMHPAGPFLIPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPE
RHWPAEGSRVEISHGPDFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSPPDGLRPEDIDTQEVY
GMTMPKAKPLRAVATPRLAPHLYG
>gnl|CDD|215584 PLN03113, PLN03113, DNA ligase 1; Provisional
MSSRPSAFDALMSNARAAAKKKQPQTQSQSSSPKKRKIGETQDANLGKTNVSEGTLPKTEDTIEPKSDSA
KPRSSTSSIAEDSKTGTKKAQTLSKPKKDEMKSKIGLLKKKPNDFDPEKVAYWEKGERVPFLFVALAFDL
ISNETGRIVITDIVCNMLRTVMATTPEDLVAVVYLLANRIAPAHEGVELGIGEATIIKALAEAFGRTEKQ
VKKQYKELGDLGLVAKASRSSQSMMRKPEPLTVVKVFNTFQQIAKESGKDSQEKKKNRIKALLVAATDCE
PLYLIRLLQTKLRIGLAGQTLLAALGQAAVYNEEHSTPPPNIQSPLEEAAKIVKQVYSVLPVYDKIVPAL
LSGGVWNLPKTCSFTPGVPVGPMLAKPTKGVSEIVNKFQDMEFTCEYKYDGERAQIHFLEDGSVEIYSRN
AERNTGKYPDVVVAISRLKKPSVKSFILDCELVAYDREKKKILPFQILSTRARKNVVMSDIKVDVCIFAF
DMLYLNGQPLIQEQLKIRREHLYESFEEDPGFFQFATAITSNDLEEIQKFLDAAVDASCEGLIIKTLNKD
ATYEPSKRSNNWLKLKKDYMESIGDSLDLVPIAAFHGRGKRTGVYGAFLLACYDSNKEEFQSICKIGTGF
SEAVLEERSASLRSQVIPTPKSYYRYGDSIKPDVWFEPTEVWEVKAADLTISPVHRAAVGIVDPDKGISL
RFPRLVRVREDKSPEQATSSEQVADMYNAQKHNHPSNQDDNDDD
>gnl|CDD|178661 PLN03114, PLN03114, ADP-ribosylation factor GTPase-activating protein AGD10; Provisional
MASENLNDKISVFKKLKAKSDNKICFDCNAKNPTWASVTYGIFLCIDCSAVHRSLGVHISFVRSTNLDSW
SSEQLKMMIYGGNNRAQVFFKQYGWSDGGKTEAKYTSRAADLYKQILAKEVAKSKAEEELDLPPSPPDST
QVPNGLSSIKTSEALKESNTLKQQEKPDVVPVSPRISRSVKKPLGAKKTGKTGGLGARKLTTKSSGTLYD
QKPEESVIIQATSPVSAKSARSSFSSRFDYADNVQNREDYMSPQVVSHVAPPKSSGFFEEELEMNGGRFQ
KKPITSSSKLQIQETDEARKKFTNAKSISSAQYFGNDNNSADLEAKSSLKKFSGSSAISSADLFGDSDGD
FTLDLTAGDLLNRLSLQAQQDISSLKNMAEETKKKLGSVASSLWV
>gnl|CDD|215585 PLN03115, PLN03115, ferredoxin--NADP(+) reductase; Provisional
MAAAVNAAVSLPSSKSSSLPARTSAISPERIRLKKGPLYYRNNVSSGKRVVSIRAQVTTETTTEAPAKVV
KVSKKNEEGVVVNKFRPKEPYTGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIPDGIDKNG
KPHKLRLYSIASSALGDFGDSKTVSLCVKRLVYTNDQGEIVKGVCSNFLCDLKPGAEVKITGPVGKEMLM
PKDPNATIIMLATGTGIAPFRSFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENF
RLDFAVSREQTNAKGEKMYIQTRMAEYAEELWELLKKDNTYVYMCGLKGMEKGIDDIMVSLAAKDGIDWF
EYKKQLKKAEQWNVEVY
>gnl|CDD|215586 PLN03116, PLN03116, ferredoxin--NADP+ reductase; Provisional
VAVKPLELEDAKEPPLNLYKPKAPYTATIVSVERIVGPKAPGETCHIVIDHGGNVPYWEGQSYGVIPPGT
NPKKPGAPHNVRLYSIASTRYGDDFDGKTASLCVRRAVYYDPETGKEDPAKKGVCSNFLCDAKPGDKVQI
TGPSGKVMLLPEEDPNATHIMVATGTGIAPFRGFLRRMFMEDVPAFKFGGLAWLFLGVANSDSLLYDDEF
ERYLKDYPDNFRYDYALSREQKNKKGGKMYVQDKIEEYSDEIFKLLDNGAHIYFCGLKGMMPGIQDTLKR
VAEERGESWEEKLSGLKKNKQWHVEVY
>gnl|CDD|178664 PLN03117, PLN03117, Branched-chain-amino-acid aminotransferase; Provisional
MAPSSSPLPTSKADEKYANVKWEELGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQ
GLFEGLKAYRTEDGRITLFRPDQNALRMQTGADRLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYI
RPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHKASSGLNLKVDHKHRRAHSGGTGGVKSCTNYSPVVKSL
IEAKSSGFSDVLFLDAATGKNIEELSACNIFILKGNIVSTPPTSGTILPGVTRKSISELARDIGYQVEER
DVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEALSTKLHLILTNIQMGVVEDKKGWMVEI
DRCQG
>gnl|CDD|215587 PLN03118, PLN03118, Rab family protein; Provisional
MGSSSGQSSGYDLSFKILLIGDSGVGKSSLLVSFISSSVEDLAPTIGVDFKIKQLTVGGKRLKLTIWDTA
GQERFRTLTSSYYRNAQGIILVYDVTRRETFTNLSDVWGKEVELYSTNQDCVKMLVGNKVDRESERDVSR
EEGMALAKEHGCLFLECSAKTRENVEQCFEELALKIMEVPSLLEEGSTAVKRNILKQKPEHQPPPNGGCC
S
>gnl|CDD|178666 PLN03119, PLN03119, putative ADP-ribosylation factor GTPase-activating protein AGD14; Provisional
MGSKREEERNEKIIRGLMKLPPNRRCINCNSLGPQYVCTTFWTFVCMACSGIHREFTHRVKSVSMSKFTS
KEVEVLQNGGNQRAREIYLKNWDHQRQRLPENSNAERVREFIKNVYVQKKYAGANDADKPSKDSQDHVSS
EDMTRRANSYHSYSQSPPYDYQYEERRYGKIPLGFTGKSASVKGLHAKASSFVYSPGRFSDHMFEDQFSN
EDSAPRASDYSVSSAGDPFRSDIQSPNFQQEAEFRSPQFQHSNAPPSENLFPGRQHQRTTSSGSVRSVDS
NFMSIKSYTSGGLGEAVSESRQNTGSQQGKTSNHVPLVAESTKAPIDLFQLPGAPVAQSVDTFQPSIAPR
SPPVNLQQAPQTYSFTPANSFAGNLGQQPTSRPSELSAPKNEGWASFDNPMPAAKSTNVITSPGDFQLEL
KIEEILQPSTSMQLPPYPSTVDQHALSIPSPWQEDLSNVLKDVVDNPQPWNAFPDSIEANPLDSSRNIHQ
QVDGASTSSYNTDHQHLESQVLEELSNDGTQTTRIPAGSSAFGFPGNIGMAPSYSEEAWQHVNEQKSANP
FDLPYDSEFDSNDMFLDMSSLQGALPDIQTPQAFLNGVSQPWLAADSVPSYLPAPAVAQGGLAYMAGQAS
TNSAAQGPVAFTGGNPFA
>gnl|CDD|215588 PLN03120, PLN03120, nucleic acid binding protein; Provisional
VMQVRTVKVSNVSLKATERDIKEFFSFSGDIEYVEMQSENERSQIAYVTFKDPQGAETALLLSGATIVDQ
SVTITPAEDYQLPPEALAPLSSNSPASGAESAVKKAEDVVSSMLAKGFILGKDAVNKAKAFDEKHQLTST
ASAKVASLDKKIGLSEKLSAGTAVVNEKVKEVDQKYQVSEKTKSALAAAEQKVSSAGSAIMKNRYVLTGA
SWVTGAFNKVAKAAEEVGQKTKEKVGAAEEEQQVVDAYANIHLSESPKAV
>gnl|CDD|215589 PLN03121, PLN03121, nucleic acid binding protein; Provisional
MYPGGYTAEVTNLSPKATEKDVYDFFSHCGAIEHVEIIRSGEYACTAYVTFKDAYALETAVLLSGATIVD
QRVCITRWGQYEDEFDFWNRPSWDTEDISTHNYETNQFASTPGEAVTVAQEVVKTMLAKGYVLGKDALSK
AKAFDESHQVSATAAAKVAELSKRIGLTDKIFAGMEAVRSVDEKYHVSEFTKSAATATGRTAAAAANAVV
NSSYFSKGALWVSDALTRAAKAAADLGAHGSNQ
>gnl|CDD|178669 PLN03122, PLN03122, Poly [ADP-ribose] polymerase; Provisional
KVHETRSQAHAPAAEEGKGGTRKQKAENKEHEGEQSPKKAKKEKKQDDSGNGNGKSAEDAVKEFEEFCKA
IEEHLSIEQMREILEENGQDSSGSDDAVLPRCQDQLFYGPLEKCPLCGGALECDGHRYTCTGFISEWSSC
TFSTKNPPRKEEPLKIPDSVKNSFITKLLKKHQDPSKRPKRELGAPGKPFSGMMISLSGRLSRTHQYWKK
DIEKHGGKVANSVEGVTCLVVSPAERERGGSSKIAEAMERGIPVVREAWLIDSIEKQEAQPLEAYDVVSD
LSVEGRGIPWDKQDPSEEAIESLSAELKLYGKRGVYKDSKLQEEGGKIFEKDGILYNCAFSICDLGRGLN
EYCIMQLITVPDSNLHLYYKKGRVGDDPNAEERLEEWEDVDAAIKEFVRLFEEITGNEFEPWEREKKFEK
KRLKFYPIDMDDGVDVRAGGLGLRQLGVAAAHCKLDPKVANFMKVLCSQEIYRYAMMEMGLDSPDLPMGM
LSDFHLKRCEEVLLEFAEFVKSEKETGQKAEAMWLDFSNKWFSLVHSTRPFVIRDIDELADHAASALETV
RDINVASRLIGDMTGSTLDDPLSDRYKKLGCSISPVDKESDDYKMIVKYLEKTYEPVKVGDVSYSVSVEN
IFAVESSAGPSLDEIKKLPNKVLLWCGTRSSNLLRHLAKGFLPAVCSLPVPGYMFGKAIVCSDAAAEAAR
YGFTAVDRPEGFLVLAVASLGDEVLELTKPPEDVKSYEEKKVGVKGLGRKKTDESEHFKWRDDITVPCGR
LIPSEHKDSPLEYNEYAVYDPKQVSIRFLVGVKYEEKGAEMVTAE
>gnl|CDD|215590 PLN03123, PLN03123, poly [ADP-ribose] polymerase; Provisional
MAAPPKPWKAEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQFDGFMPMWNHASCILKKKNQIKSIDDVE
GIDSLRWEDQQKIRKYVESGGTGTGTASDAAASSFEYGIEVAKTSRATCRRCSEKILKGEVRISSKPEGQ
GYKGLAWHHAKCFLEMSPSTPVEKLSGWDTLSDSDQEAVLPLVKKSPSEAKEEKAEERKQESKKGAKRKK
DASGDDKSKKAKTDRDVSTSTAASQKKSSDLESKLEAQSKELWSLKDDLKKHVSTAELREMLEANGQDTS
GSELDLRDRCADGMMFGALGPCPLCSGPLLYSGGMYRCQGYLSEWSKCSYSTLEPERIKKKWKIPDETDN
QYLRKWFKSQKSKKPERLLPPSSSNESSGKQAQSNSSDSESEFLGDLKVSIVGASKEKVTEWKAKIEEAG
GVFHATVKKDTNCLVVCGELDDEDAEMRKARRMKIPIVREDYLVDCFKKKKKLPFDKYKLEASGTSSSMV
TVKVKGRSAVHEASGLQDTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRVG
NEKIGGNKLEEMSKSDAIHEFKRLFLEKTGNPWESWEQKTNFQKQPGKFYPLDIDYGVNEQPKKKAASGS
KSNLAPRLVELMKMLFDVETYRAAMMEFEINMSEMPLGKLSKANIQKGFEALTEIQNLLKENDQDPSIRE
SLLVDASNRFFTLIPSIHPHIIRDEDDLKSKVKMLEALQDIEIASRLVGFDVDEDDSLDDKYKKLHCDIS
PLPHDSEDYKLIEKYLLTTHAPTHTDWSLELEEVFSLEREGEFDKYAPYKEKLKNRMLLWHGSRLTNFVG
ILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEVALGEIYELKKAKYMDKP
PRGKHSTKGLGKTVPQESEFVKWRDDVVVPCGKPVPSKVKASELMYNEYIVYNTAQVKLQFLLKVRFKHK
R
>gnl|CDD|215591 PLN03124, PLN03124, poly [ADP-ribose] polymerase; Provisional
MANKLKVDELRAALAKRGLDTTGLKAALVRRLDDAIAEDAKTASKSGTKSSAGRKKRRERQDDGDDEPVS
PKRIAIDEVKGMTVRELREAASERGLATTGRKKDLLERLCAALESDVKVGSANGTGEDEKEKGGDEEREK
EEKIVTATKKGRAVLDQWLPDHIKSNYHVLEEGDDVYDAMLNQTNVGDNNNKFYVLQVLESDDGSKYMVY
TRWGRVGVKGQDKLHGPYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEMDYEDEEESKKDK
PSVSSEDKNKQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRIAEVIS
RSDRETLEELSGEFYTVIPHDFGFKKMRQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIGEQDDPLY
AHYKRLNCELEPLDTDSEEFSMIAKYLENTHGQTHSGYTLEIVQIFKVSREGEDERFQKFSSTKNRMLLW
HGSRLTNWTGILSQGLRIAPPEAPSTGYMFGKGVYFADMFSKSANYCYASAANPDGVLLLCEVALGDMNE
LLQADYNANKLPPGKLSTKGVGRTVPDPSEAKTLEDGVVVPLGKPVESPYSKGSLEYNEYIVYNVDQIRM
RYVLQVKFNYKRG
>gnl|CDD|215592 PLN03126, PLN03126, Elongation factor Tu; Provisional
MAISASAASSSSSLLLPSSSSSSPSSSTFSFKSTSGKLKSLTLSSSFLSPFSTTTTSTSQRRRRSFTVRA
ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYE
TENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQV
DDEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEALMENPNIKRGDNKWVDKIYELMDAVDSYIP
IPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALA
GDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGK
VTSIMNDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGAGVIQSIIE
>gnl|CDD|178673 PLN03127, PLN03127, Elongation factor Tu; Provisional
MASVVLRNPNSKRLLPFSSQIYCACRGSAPSTSASISAADDRQSPSPWWRSMATFTRTKPHVNVGTIGHV
DHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKN
MITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY
KFPGDEIPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVAT
GRVEQGTIKVGEEVEIVGLRPGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPG
SIKTYKKFEAEIYVLTKDEGGRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPV
PLEPGQRFALREGGRTVGAGVVSKVLS
>gnl|CDD|215593 PLN03128, PLN03128, DNA topoisomerase 2; Provisional
KTIEETYQKKTQLEHILLRPDTYIGSTEKHTQTLWVYEGGEMVNREVTYVPGLYKIFDEILVNAADNKQR
DPSMDSLKVDIDVEQNTISVYNNGKGIPVEIHKEEGVYVPELIFGHLLTSSNFDDNEKKTTGGRNGYGAK
LANIFSTEFTVETADGNRGKKYKQVFTNNMSVKSEPKITSCKASENWTKITFKPDLAKFNMTRLDEDVVA
LMSKRVYDIAGCLGKKLKVELNGKKLPVKSFQDYVGLYLGPNSREDPLPRIYEKVNDRWEVCVSLSDGSF
QQVSFVNSIATIKGGTHVDYVADQIVKHIQEKVKKKNKNATHVKPFQIKNHLWVFVNCLIENPTFDSQTK
ETLTTRPSSFGSKCELSEEFLKKVEKCGVVENILSWAQFKQQKELKKKDGAKRQRLTGIPKLDDANDAGG
KKSKDCTLILTEGDSAKALAMSGLSVVGRDHYGVFPLRGKLLNVREASHKQIMKNAEITNIKQILGLQFG
KTYDEENTKSLRYGHLMIMTDQDHDGSHIKGLIINFFHSFWPSLLKIPGFLVEFITPIVKATKGGKSLSF
YTMPEYEAWKESLEGETKGWTIKYYKGLGTSTSEEAKEYFSNLDIHKKEFLWQSDEDGDLIDMAFSKKRV
EDRKIWLNNYEPGTFLDQTGNGISYSDFINKELILFSQADLARSIPSMVDGLKPSQRKVLFACFKRNLKS
EIKVAQLSGYVAEHSAYHHGEASLASTIIGMAQDFVGSNNINLLTPSGQFGTRLQGGKDAASARYIFTRL
SPITRALFPKDDDVLLNYLNEDGQSIEPEWYCPIIPMVLVNGSEGIGTGWSTFIPNYNPRDIIANIRRLL
RGEELEPMHPWYRGFKGTITEVSTSRSGSYTVTGIIEQIGDTTIRITELPVRKWTQDYKEFLEALLTGTK
KKEPEIKDFKENHTDTTVHFTVTLSEEKMARALAEGLEKKFKLSTTISTSNMHLFDKDGKIKKYDSPEDI
LEEFFHLRLDLYVKRKEVLLENLEYELKKLDNKARFILAVVKGEIVVNNRKRAELLAELEEKGFDKFPKT
AKISETNVVGDRDGEASEEEEASDNELAKSYDYLLGMPISSLTLEKVDELRAERAKKETEVEELKKTTPE
DLWRKDLDAFEEALD
>gnl|CDD|215594 PLN03129, PLN03129, NADP-dependent malic enzyme; Provisional
ASSSLADARRRRSAAGGVEDVYGEDAATEEQPVTPWVRVASGYDLLRDPRYNKGLAFTETERDRLGLRGL
LPPAVLSQELQVKRFMENLRALESPLAKYRALMDLQERNERLFYRVLIDNIEELLPIVYTPTVGEACQKY
GSLFRRPRGLYISLKDKGRVLSMLKNWPERDVQVIVVTDGERILGLGDLGVQGMGIPVGKLDLYTAAGGI
RPSAVLPVCIDVGTNNEKLLNDPFYIGLRQPRLTGEEYDELVDEFMEAVKQRWGPKVLVQFEDFANKNAF
RLLQRYRTTHLCFNDDIQGTAAVALAGLLAALRATGGDLADQRILFAGAGEAGTGIAELIALAMSRQTGI
SEEEARKRIWLVDSKGLVTKSRKDSLQPFKKPFAHDHEPGASLLEAVKAIKPTVLIGLSGVGGTFTKEVL
EAMASLNERPIIFALSNPTSKAECTAEEAYTWTGGRAIFASGSPFDPVEYNGKTFHPGQANNAYIFPGIG
LGALLSGAIRVTDDMLLAAAEALAAQVTEEELAKGAIYPPFSRIRDISAHVAAAVAAKAYEEGLATRLPR
PEDLVEYAESCMYSPVYRPYR
>gnl|CDD|215595 PLN03130, PLN03130, ABC transporter C family member; Provisional
MGFEPLDWYCRPVPNGVWAKKVDNAFGAYTPCATDSLVINISHLVLLGLCLYRIWLIKKDHKVQRFCLRS
KWYNYFLALLAAYCTAEPLFRLVMGISVLNLDGQTSLPPFEIVSLIVEALTWCSMLVMIGVETKIYIREF
RWYVRFAVIYVLVGDAVMLNLVLSVKEYYSSFVLYLYISEVAAQVLFGILLLVYFPNLDPYPGYTPIGSE
SVDDYEYEELPGGEQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCW
DEELKKPKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGEPAWIGYIYAFSIFVG
VVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHT
LWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMD
TVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGDLTPARAFTS
LSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGLPAISIKNGYFSWDSKAER
PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVPQVSWIFNATVRDNIL
FGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA
LDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENA
GKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNA
LGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTPKTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMS
SLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGI
VSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGR
SMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAENQAAFASTMGLLLSYALNITSLLT
AVLRLASLAENSLNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSF
EISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVR
FNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDE
ATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM
VQSTGAANAQYLRSLVFGGDEDRLAREESKALDGQRKWLASSRWAAAAQFALAVSLTSSQNDLQSLEIED
ENSILEKTKDAVITLQSVLEGKHDKEIDESLNQRQVPRDGWWSSLYRMVEGLAVMSRLARNRMQQSDHNF
EGKSIDWDNVEM
>gnl|CDD|178677 PLN03131, PLN03131, hypothetical protein; Provisional
MGSRKEEERNEKIIRGLMKLPPNRRCINCNSLGPQFVCTNFWTFICMTCSGIHREFTHRVKSVSMSKFTS
QDVEALQNGGNQRAREIYLKDWDQQRQRLPDNSKVDKIREFIKDIYVDKKYAGGKTHDKPPRDLQRIRSH
EDETRRACSYHSYSQSPPYDFQYEDRRYGKQAGILTRKPGSDRGLNVGKMASFICSPTRLNDRMFEDRFA
NEGSVSGVSDYSVSSGGDLVRSGAESPNFQKDIAFSPPIQPPKDILGEDVQQRRIDLFSAALCKQGAEGC
PHIQRSASLGSIGSFDSLSVSIKSFNSGSLADIVAEAEQAAGNHQDKMPAFPRMAGSGSHASLDHFKAPV
APEAAAPMAPPIDLFQLPATSPAPPVDLFEIPPLDPAPAINAYQPPQTSLPSSIDLFGGITQQQSINSLD
EKSPELSIPKNEGWATFDGIQPIASTPGNENLTPFSIGPSMAGSANFDQVPSLDKGMQWPPFQNSSDEES
ASGPAPWLGDLHNVEAPDNTSAQNWNAFEFDDSVAGIPLEGIKQSSEPQTAANMPPTADQLIGCKALEDF
NKDGIKRTAPHGQGELPGLDEPSDILAEPSYTPPAHPIMEHAQSHANDHKSINPFDLPYDSDLEPGNMFL
DMSSLEAALPDAHLPSAFLGSGMTEPWFPQDLAMTYIPAAPQGGLAYMAGQAPNPQLGNVQTQGPVAFVG
GNPFA
>gnl|CDD|178678 PLN03132, PLN03132, NADH dehydrogenase (ubiquinone) flavoprotein 1; Provisional
ALRAFSTQAAATAATPQPPPPPPPPEKTHFGGLKDEDRIFTNLYGLHDPFLKGAMKRGDWHRTKDLVLKG
PDWIVNEMKKSGLRGRGGAGFPSGLKWSFMPKVSDGRPSYLVVNADESEPGTCKDREIMRHDPHKLLEGC
LIAGVGMRARAAYIYIRGEYVNERLNLERARHEAYAAGLLGKNACGSGYDFDVYIHYGAGAYICGEETAL
LESLEGKQGKPRLKPPFPANVGLYGCPTTVTNVETVAVSPTILRRGPEWFASFGRKNNAGTKLFCISGHV
NKPCTVEEEMSIPLKELIERHCGGVRGGWDNLLAIIPGGSSVPLLPKKICDDVLMDFDALKAVQSGLGTA
AVIVMDKSTDVVDAIARLSYFYKHESCGQCTPCREGTGWLWDIMERMKVGNAKLEEIDMLQEVTKQIEGH
TICALGDAAAWPVQGLIRHFRPELERRIKERAERELLAAAA
>gnl|CDD|215596 PLN03133, PLN03133, beta-1,3-galactosyltransferase; Provisional
MKKWYGGVLVVSLFMLLVLRYVLLKNPIGESYLQSVFPSNTTNPLEWLDPTNPPAVQNPENSSQVISTDT
IVSSLFATRNISNEEQQSLLTWNHLKHLVDHAQVLPNGVEAIKEAGVAWESLMASVEEEKLGYTNESSLR
KSKEKQCPYFLNKMNATELGDSGYKLKIPCGLTQGSSITIIGIPDGLLGNFRIDLTGEPLPGEPDPPIIL
HYNVRLLGDKITEDPVIVQNTWTAAHDWGEEERCPSPDPDKNKKVDDLDQCNKMVGRDDKRVLSTSLHSN
GSRRSPMSQEATKARRYFPFKQGYLSVATLRVGTEGIQMTVDGKHITSFAYRETLEPWLVSEVRISGDLK
LISVLASGLPTSEDSEHVIDLEALKSPPLSPKKPLDLFIGVFSTANNFKRRMAVRRTWMQYDAVRSGAVA
VRFFVGLHKNQMVNEELWNEARTYGDIQLMPFVDYYSLITWKTLAICIFGTEVVSAKYVMKTDDDAFVRV
DEVLASLKRTNVSHGLLYGLINSDSQPHRNPDSKWYISPEEWPEETYPPWAHGPGYVVSRDIAKEVYKRH
KEGRLKMFKLEDVAMGIWIAEMKKEGLEVKYENDGRIYNEGCKDGYVVAHYQSPREMLCLWQKLQEGKRA
TCCGEW
>gnl|CDD|178680 PLN03134, PLN03134, glycine-rich RNA-binding protein 4; Provisional
MAFCNKLGGLLRQNISSNGNVPVTSMLGSLRLMSTKLFIGGLSWGTDDASLRDAFAHFGDVVDAKVIVDR
ETGRSRGFGFVNFNDEGAATAAISEMDGKELNGRHIRVNPANDRPSAPRAYGGGGGYSGGGGGYGGGGDG
GGGF
>gnl|CDD|178681 PLN03136, PLN03136, Ferredoxin; Provisional
MASTALSSAIVSTSFLRRQQTPISLRSLPSANTQSLFGLKSSTARGGRVTAMATYKVKFITPEGEQEVEC
EEDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQISEGYVLTCVAYPTSDVVIE
THKEEAIM
>gnl|CDD|215597 PLN03137, PLN03137, ATP-dependent DNA helicase; Q4-like; Provisional
MARESHIKKNVMSSSHLPEVNKSRGPQTNWSQHAKALENISSQRKFLSSNFLYSLESQKDREMAARSINC
APVNVQTLASPQIEKAWHALSSLSINNNYLRPGKTPPIDNGSTDLSSDVGQSTTKVSSSTGGSYYEHNHP
HQNQREVSGTNSSFASFSSSSVGDDNATAEKVPRGNSEIRASVPNNTHSNGVEGSFIKNSAHTAQQKESR
EASLDEIDDDDILENIDVDQIVMEHYQSTCTPQPSVSKFPPITPTVDTFASRREEEQFLPPELCSNCSHG
IKLGLCPEASTHVEQMKDMLLAISNELLDNAADLSPDQVEQLRQDRLQLKKQIQQLEIHIRDKERQKSQF
SASTATRNFQYETPQSTNYKIDPMQTDAQVHLRNEQGRYEKDNWNTPRDSFSSVDRYGISSGPVEREPYV
PKFIDVTYTEGSNDKKWSSRNFPWTKKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSL
TYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTP
EKVAKSDSLLRHLENLNSRGLLARFVIDEAHCVSQWGHDFRPDYQGLGILKQKFPNIPVLALTATATASV
KEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKCLEDIDKFIKENHFDECGIIYCLSRMDCEKVAERL
QEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGR
AGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSPMAMGYNRMASSGRILETNTENLLRMVSYCENEVDC
RRFLQLVHFGEKFDSTNCKKTCDNCSSSKSLIDKDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQY
VKKHRHETLSLHGAGKHLSKGEASRILHYLVTEDILAEDVKKSDLYGSVSSLLKVNESKAYKLFSGGQTI
IMRFPSSVKASKPSKFEATPAKGPLTSGKQSTLPMATPAQPPVDLNLSAILYTALRKLRTALVKEAGDGV
MAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKYGDRLLETIESTINEYYKTDKNSSSSNDSPDS
GKRRRDENINPNVAEDDDFTKSTSQSKKKTVKNKNKGVEHGNSRETDRRNQCDDDLDFKDSDHDEERNGS
AVLPW
>gnl|CDD|215598 PLN03138, PLN03138, Protein TOC75; Provisional
GRSSSTMVSAAASTSLSSSRPQLSSFSSRSPQSATRSPRASSIKCSASASASSSATSSSASLVANGAVAL
LSASAISGGGGGGGGGFGGFGGGGGGGGGGGGGWRFWLRLFAPADAHADEEQSGDWDSHGLPVNITVPLS
KLSGFKRYKVSEIEFFDRRRNTTVGTEDSFFEMVTLRPGGVYTKAQLQKELETLASCGMFEKVDLEGKTK
PDGTLGLTISFTESTWQSADSFRCINVGLMSQSKPIEMDEDMTDKEKMEYYRSQEKDYKRRIRKARPCLL
PKSVRREVLGMLRDQGKVSARLLQRIRDRVQKWYHDEGYACAQVVNFGNLNTNEVVCEVVEGDITKVVIQ
FQDKLGNVVEGNTQLPIIDRELPKQLRQGHIFNIEAGKQALRNINSLALFSNIEVNPRPDEKNEGGIVVE
IKLKELEPKSAEVSTEWSIVPGRGGRPTLASIQPGGTVSFEHRNIQGLNRSILGSVTSSNLLNPQDDLSF
KLEYVHPYLDGVYNPRNRTFRASCFNSRKLSPVFTGGPGVDEVPPIWVDRAGFKANITENFTRQSKFTYG
LVVEEITTRDETSHICTHGQRVLPSGGLSADGPPTTLSGTGIDRMAFLQANITRDNTKFVNGAVVGDRHI
FQVDQGLGIGSKFPFFNRHQLTVTKFIQLNKVEKGAGKPPPPVLVLHGHYGGCVGDLPSYDAFTLGGPYS
VRGYNMGELGAARNILEVAAELRIPVRNTHVYAFAEHGTDLGSSKDVKGNPTEFFRRAGHGSSYGVGVKL
GLVRAEYAVDHNAGTGAIFFRFGERF
>gnl|CDD|178684 PLN03139, PLN03139, formate dehydrogenase; Provisional
AMRRAAQVAIRAFSSSSPAHLLTRALASSSLHASAGSKKIVGVFYKAGEYADKNPNFVGCVENALGIRDW
LESQGHQYIVTDDKEGPDCELEKHIPDLHVLITTPFHPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAA
AAAGLTVAEVTGSNVVSVAEDELMRILILLRNFLPGYHQVVSGEWNVAGIAYRAYDLEGKTVGTVGAGRI
GRLLLQRLKPFNCNLLYHDRLKMDPELEKETGAKFEEDLDAMLPKCDVVVINTPLTEKTRGMFNKERIAK
MKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPAPKDHPWRYMPNHAMTPHISGTTIDAQL
RYAAGVKDMLDRYFKGEDFPAQNYIVKEGKLASQYQ
>gnl|CDD|215599 PLN03140, PLN03140, ABC transporter G family member; Provisional
ARSRGGSMRRSISRSVSRSSRNMEDVFSGGSQSRRRTSSVDEDEEALKWAAIEKLPTYSRLRTSIMKSFV
ENDVYGNQLLHKEVDVTKLDGNDRQKFIDMVFKVAEEDNEKFLKKFRNRIDRVGIKLPTVEVRFEHLTVE
ADCYIGSRALPTLPNAARNIAESALGMLGINLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLA
LAGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKETLDFSARCQGVGTRYDLLSELA
RREKDAGIFPEAEVDLFMKATAMEGVKSSLITDYTLKILGLDICKDTIVGDEMIRGISGGQKKRVTTGEM
IVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDDIILLSEGQIVYQG
PRDHILEFFESCGFKCPERKGTADFLQEVTSKKDQEQYWADRNKPYRYISVSEFAERFKSFHVGMQLENE
LSVPFDKSQSHKAALVFSKYSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTEMH
TRNEEDGALYIGALLFSMIINMFNGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISIIESV
VWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILP
KGEIPNWWEWAYWVSPLSYGFNALAVNEMFAPRWMNKMASDNSTRLGTAVLNIFDVFTDKNWYWIGVGAL
LGFTILFNVLFTLALTYLNPLGKKQAIISEETAEEMEGEEDSIPRSLSSADGNNTREVAIQRMSNPEGLS
KNRDSSLEAANGVAPKRGMVLPFTPLAMSFDDVNYFVDMPAEMKEQGVTEDRLQLLREVTGAFRPGVLTA
LMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFL
RLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL
DARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAIP
GVPKIKEKYNPATWMLEVSSLAAEVKLGIDFAEHYKSSSLYQRNKALVKELSTPPPGASDLYFATQYSQS
TWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGTKRSNANDLTMVIGAMYAAVLFVGI
NNCSTVQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWF
YFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTVY
GLIVSQYGDVEDTIKVPGGAPDPTIKWYIQDHYGYDPDFMGPVAAVLVGFTVFFAFIFAFCIRTLNFQTR
>gnl|CDD|215600 PLN03141, PLN03141, 3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
SSKKKSRLPKGSLGWPVIGETLDFISCAYSSRPESFMDKRRSLYGKVFKSHIFGTPTIVSTDAEVNKVVL
QSDGNAFVPAYPKSLTELMGKSSILLINGSLQRRVHGLIGAFLKSPHLKAQITRDMERYVSESLDSWRDD
PPVLVQDETKKIAFEVLVKALISLEPGEEMEFLKKEFQEFIKGLMSLPIKLPGTRLYRSLQAKKRMVKLV
KKIIEEKRRAMKNKEEDETGIPKDVVDVLLRDGSDELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSD
CPVALQQLTEENMKLKRLKADTGEPLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEIKGYLIP
KGWCVLAYFRSVHLDEENYDNPYQFNPWRWQEKDMNNSSFTPFGGGQRLCPGLDLARLEASIFLHHLVTR
FRWVAEEDTIVNFPTVRMKRKLPIWVTRIDDS
>gnl|CDD|215601 PLN03142, PLN03142, Probable chromatin-remodeling complex ATPase chain; Provisional
EEEQVNTQANEEEDEEELEAVARSAGSDSDDDEVPAEDEDEDEEDDEEAESPAKAEISKREKARLKELKK
QKKQEIQKILEQQNAAIDADMNNKGKGRLKYLLQQTEIFAHFAKGDQSASAKKAKGRGRHASKLTEEEED
EEYLKEEEDGLGGSGGTRLLVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLG
YLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMA
IKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFS
SAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQK
DLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRV
LIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATAD
IVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKT
VNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDDTAELYDFD
DEDDKDENKLDFKKIVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFNVQ
RLTELYEKEVRYLMQAHQKGQLKDTIDVAEPEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRACE
KYGRNDIKSIASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRY
KNPWLELKIQYGQNKGKLYNEECDRFMLCMVHKLGYGNWDELKAAFRTSPLFRFDWFVKSRTPQELARRC
DTLIRLIEKENQEYDERERQARKEKKLAKNATPSKRPSGRQANESPSSLKKRK
>gnl|CDD|215602 PLN03143, PLN03143, nudix hydrolase; Provisional
RFTLLPSRPLALPSRMAHKEASSSSSSSPLTHSITLPGQPGQPVLVVAAPGISSSDFRKAIDSSLFRQWL
KNLQSESGILAYGSMSLKQVLIQGVDMFGKRIGFLKFKADIIDKETGQKVPGIVFARGPAVAVLILLESE
GETYAVLTEQVRVPVGKFVLELPAGMLDDDKGDFVGTAVREVEEETGIKLKLEDMVDLTAFLDPSTGCRM
FPSPGGCDEEISLFLYRGHVDKETIRQLQGKETGLRDHGELIKVHVVPYRELWRMTADAKVLMAIALYEM
AKREGLLPSSP
>gnl|CDD|178689 PLN03144, PLN03144, Carbon catabolite repressor protein 4 homolog; Provisional
MLSVVRVHLPSDIPIVGCELTPYVLLRRPDGTLTTDDVPESAPLDGYFLRYRWYRIQSDRKVAVCSVHPS
EPATLQCVGCVKAKLPVSKSYHCSPKCFSDAWRHHRVLHERAASAVRENGNEEDELFGRFNSSGSGVLST
SDSGSASSASLTNGSVPLYPSGIEQKTQVGGETWIEVGRSKTYTPTADDVGHVLKFECVVVDAETGLPVG
HPQSILTSRVIPAPSPTPRRLIQVNGLDGMGHLDLDGRTSSAGTFTVLSYNILSDLYATSDMYSYCPPWA
LSWTYRRQNLLREIVGYRADILCLQEVQSDHFEEFFAPELDKHGYQALYKKKTTEVYTGNTYVIDGCATF
FRRDRFSLVKKYEVEFNKAAQSLTEALIPSAQKKAALNRLLKDNVALIVVLEAKFGNQGADNGGKRQLLC
VANTHIHANQELKDVKLWQVHTLLKGLEKIAASADIPMLVCGDFNSVPGSAPHCLLATGKVDPLHPDLAV
DPLGILRPASKLTHQLPLVSAYSSFARMPGSGSGLEQQRRRMDPATNEPLFTNCTRDFIGTLDYIFYTAD
SLTVESLLELLDEESLRKDTALPSPEWSSDHIALLAEFRCKPRTRR
>gnl|CDD|215603 PLN03145, PLN03145, Protein phosphatase 2c; Provisional
ETKGISGGGEGGSSGGGRPPNPSVAACCKPSLVRHSSLVKTPASDISVENELTFENMDTEFIPVVRSGAW
ADIGSRSSMEDVYICVDNFMSDFGLKNSEDGPSAFYGVFDGHGGKHAADFACYHLPRFIVEDEDFPREIE
KVVSSAFLQTDTAFAEACSLDASLASGTTALAALVVGRSLVVANAGDCRAVLCRRGKAIEMSRDHKPMCS
KERKRIEASGGYVYDGYLNGQLNVARALGDWHMEGMKGSDGGPLSAEPELMTTQLTEEDEFLIIGCDGIW
DVFRSQNAVDFARRRLQEHNDPVMCSKELVDEALKRKSGDNLAVVVVCFQSQPPPNLVAPRPRVQRSISA
EGLRELQSFLDSLAN
>gnl|CDD|178691 PLN03146, PLN03146, aspartyl protease family protein; Provisional
FSVLLALCLFSFSELSAAEAPKGGFTVDLIHRDSPKSPFYNPSETPSQRLRNAFRRSISRVNHFRPTDAS
PNDPQSDLISNGGEYLMNISIGTPPVPILAIADTGSDLIWTQCKPCDDCYKQVSPLFDPKKSSTYKDVSC
DSSQCQALGNQASCSDENTCTYSYSYGDGSFTKGNLAVETLTIGSTSGRPVSFPGIVFGCGHNNGGTFDE
KGSGIVGLGGGPLSLISQLGSSIGGKFSYCLVPLSSDSNGTSKINFGTNAIVSGSGVVSTPLVSKDPDTF
YYLTLEAISVGSKKLPYTGSSKNGVEEGNIIIDSGTTLTLLPSDFYSELESAVEEAIGGERVSDPQGLLS
LCYSSTSDIKLPIITAHFTGADVKLQPLNTFVKVSEDLVCFAMIPTSSIAIFGNLAQMNFLVGYDLESKT
VSFKPTDCTKM
>gnl|CDD|178692 PLN03147, PLN03147, ribosomal protein S19; Provisional
QAIWKGAFVDAFLARIKKKRDLLLGKKIWSHRSSILPDFVDCSVLIYNGKTHIRCKITEGKVGHKFGEFA
FTRKRRPHRAIIAKGNKGKGKK
>gnl|CDD|178693 PLN03148, PLN03148, Blue copper-like protein; Provisional
SAHLLLFCFFALFSASATTATDHIVGANKGWNPGINYTLWANNQTFYVGDLISFRYQKTQYNVFEVNQTG
YDNCTTEGAAGNWTSGKDFIPLNKAKRYYFICGNGQCFNGMKVTILVHPLPPPPSHTAAANGAKSHSAAP
AAFHKGLVALRGLVLWMASIWFGSGWI
>gnl|CDD|178694 PLN03149, PLN03149, peptidyl-prolyl isomerase H (cyclophilin H); Provisional
SAGAGNVEWHLRPPNPKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKAGLPQGYKG
CQFHRVIKDFMIQGGDFLKGDGTGCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCD
WLDNKHVVFGRVLGDGLLVVRKIENVATGPNNRPKLACVISECGEM
>gnl|CDD|178695 PLN03150, PLN03150, hypothetical protein; Provisional
LRLWLLAASALLAVLASLASPEPFTMRISCGARVNVRTAPTNTLWYKDFAYTGGIPANATRPSFIAPPLK
TLRYFPLSDGPENCYNINRVPKGHYSVRVFFGLVAEPNFDSEPLFDVSVEGTQISSLKSGWSSHDEQVFA
EALVFLTDGSASICFHSTGHGDPAILSIEILQVDDKAYNFGPSWGQGVILRTAKRLSCGAGKSKFDEDYS
GDHWGGDRFWNRMQTFGSGSDQAISTENVIKKASNAPNFYPESLYQSALVSTDTQPDLSYTMDVDPNRNY
SVWLHFAEIDNSITAEGKRVFDVLINGDTAFKDVDIVKMSGERYTALVLNKTVAVSGRTLTIVLQPKKGT
HAIINAIEVFEIITAESKTLLEEVSALQTLKSSLGLPLRFGWNGDPCVPQQHPWSGADCQFDSTKGKWFI
DGLGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLT
SLRILNLNGNSLSGRVPAALGGRLLHRASFNFTDNAGLCGIPGLRACGPHLSVGAKIGIAFGVSVAFLFL
VICAMCWWKRRQNILRAQRIAAREAPYAKARTHFSRDVQMTRHHRQNHGSARTAAENGPSLLS
>gnl|CDD|215604 PLN03151, PLN03151, cation/calcium exchanger; Provisional
MKAVNFLYSSKNPKFRGVFNGICALVLLFLFFDRSDILRNPLLRNSSFVNDGSGSTSGGFNSFTVIRRRL
SDIDVNSSYFSDNSSLSGDSPVLCSGLHEHEGYADQCEFLKAHPICSSGGFFDYLKFFYCSCEDFRILGY
AVLGVWLVALFYLLGNTAADYFCCSLEKLSKLLRLPPTVAGVTLLPLGNGAPDVFASIAAFVGKDAGEVG
LNSVLGGAVFVTCVVVGIVSLCVADKEVQIDKRCFIRDLCFFLFTLVSLLVILMVGKVTVGGAIAFVSIY
VVYAFLVAANEILRKHARRLKLDVVTPLLPVQGSIFSPSVEEDESMYSPLLESDTESDVPRLQTSLPQWM
WASNVAIYSNHFAKGSVHDEERPPWGWTDEGAEVESSLFSCSKLFSLLEMPLTIPRRLTIPIVEEDRWSK
TYAVASASLAPVLLAFLWSSQDDVSLQARIAAYFIGVAIGSTLGFLAYKYTEPDRPPRRFLIPWVLGGFI
MSIVWFYMIANELVALLVAFGVIFGINPSILGLTVLAWGNSMGDLMSNVALAMNGGDGVQIAMSGCYAGP
MFNTLVGLGMSMLLGAWSKSPESYMLPEDSSLFYTMGFLVSGLIWALVVLPRNDMRPNKTLGVGLIALYL
IFLTFRVSTAMGFIPWAGLS
>gnl|CDD|178697 PLN03152, PLN03152, hypothetical protein; Provisional
MAALLLSLSPHPPNPQNPNPRKPKPLSRCGASRRDFILHTASLCASSLAAQNPLPPSLADPSKPSKPLLS
GIANTKSWFQFYGDGFSIRVPPSFEDIMEPEDYNAGLSLYGDKAKPRTFAARFASPDGSEVLSVVIRPSN
QLKITFLEAKDITDLGSLKEAAKIFVPGGATLYSARTIKVKEEEGIRTYYFYEFGRDEQHVALVATVNSG
KAYIAGATAPESKWDDDGVKLRSAAISLTVL
>gnl|CDD|215605 PLN03153, PLN03153, hypothetical protein; Provisional
SSSPHRPCSSPLSLSRTRSRRWRHSRTGTAVVAVAALLLSTTAWLSLVFSGTTARCWHRFKDWEGSPDTL
LWNKRYHHPIVTPLPPPPSSPSLPSSLLLDHFRNRSLSEIERLKVEAELSLNHIMFGIAGSSQLWKRRKE
LVRLWWRPNQMRGHVWLEEQVSPEEGDDSLPPIMVSEDTSRFRYTNPTGHPSGLRISRIVLESFRLGLPD
VRWFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGGPSESHSANSYFSHNMAFGGGGIAISYPLAEALSRI
LDDCLDRYPKLYGSDDRLHACITELGVPLSREPGFHQWDIRGNAHGLLSSHPIAPFVSIHHVEAVDPFYP
GLSSLDSLKLFTRAMKVDPRSFLQRSICYDHTHHLTFSISLGYVVQVFPSIVLPRDLERSELTYSAWNKI
SHRNEFDLDTRDPIKSVCKKPILFFLKDVGREGNATLGTYSRARMKDDLKRKVFCFPRSLPLPYVEKIQV
LGFPLSKNWHLVPRRLCCRLNQTSDELLTLTVGQCEKGSLGSFIDSV
>gnl|CDD|215606 PLN03154, PLN03154, putative allyl alcohol dehydrogenase; Provisional
MMEGQVVENKQVILKNYIDGIPKETDMEVKLGNKIELKAPKGSGAFLVKNLYLSCDPYMRGRMRDFHDSY
LPPFVPGQRIEGFGVSKVVDSDDPNFKPGDLISGITGWEEYSLIRSSDNQLRKIQLQDDIPLSYHLGLLG
MAGFTAYAGFYEVCSPKKGDSVFVSAASGAVGQLVGQLAKLHGCYVVGSAGSSQKVDLLKNKLGFDEAFN
YKEEPDLDAALKRYFPEGIDIYFDNVGGDMLDAALLNMKIHGRIAVCGMVSLNSLSASQGIHNLYNLISK
RIRMQGFLQSDYLHLFPQFLENVSRYYKQGKIVYIEDMSEGLESAPAALVGLFSGKNVGKQVIRVAKE
>gnl|CDD|178700 PLN03155, PLN03155, cytochrome c oxidase subunit 5C; Provisional
MAGHKIAHATLKGPSVVKELCIGLTLGLAAGGLWKMHHWNEQRKTRSFYDLLEKGEISVVVEE
>gnl|CDD|178701 PLN03156, PLN03156, GDSL esterase/lipase; Provisional
MQMHLFLIFFLLLAQLLVLVAETCAKVPAIIVFGDSSVDAGNNNQISTVAKSNFEPYGRDFPGGRPTGRF
CNGRIAPDFISEAFGLKPAIPAYLDPSYNISDFATGVCFASAGTGYDNATSDVLSVIPLWKELEYYKEYQ
TKLRAYLGEEKANEIISEALYLISIGTNDFLENYYTFPGRRSQYTVSQYQDFLIGIAENFVKKLYRLGAR
KISLGGLPPMGCLPLERTTNLMGGSECVEEYNDVALEFNGKLEKLVTKLNKELPGIKLVFSNPYDIFMQI
IRNPSAYGFEVTSVACCATGMFEMGYLCNRNNPFTCSDADKYVFWDSFHPTEKTNQIIANHVVKTLLSKF
Q
>gnl|CDD|178702 PLN03157, PLN03157, spermidine hydroxycinnamoyl transferase; Provisional
MVVILKASYTVKPAKPTWTGRRSLSEWDQVGTITHVPTIYFYSPPWNTSSGSIIEILKDSLSRALVPFYP
LAGRLRWIGGGRLELECNAMGVLLIEAESEAKLDDFGDFSPTPEFEYLIPSVDYTKPIHELPLLLVQLTK
FSCGGISLGLGISHAVADGQSALHFISEWARIARGEPLGTVPFLDRKVLRAGEPPLSAPVFDHAEFSHPP
LLIGEQDNVEERKKKTTVAMLKLSKDQVEKLKDKANESRSSDNGRPYTRYETVAGHVWRSACKARGHEPE
QPTALGICVDSRSRMQPPLPDGYFGNATLDVIAESTSGELVSKPLGYASSKIREAIEKVTNEYVQSAIDY
LKNQEDLTRFQDLHALGGAEGPFYGNPNLGVVSWLTLPIYGLDFGWGKEIYMGPGTHDFDGDSLLLPGQN
EDGSVILALCLQVAHMEAFKKFFYEDI
>gnl|CDD|215607 PLN03158, PLN03158, methionine aminopeptidase; Provisional
MEEALTTSPLACARCSKPAHLQCPKCLELKLPREGASFCSQDCFKAAWSSHKSVHTKAKLSSIGQNSDAP
AEGWLYCLKKGQARTSKLPDFDWTGPLRPYPISPRRVVPDHIPKPDWALDGTPKIEPNSDLQHSVEIKTP
EQIQRMRETCRIAREVLDAAARAIKPGVTTDEIDRVVHEATIAAGGYPSPLNYHFFPKSCCTSVNEVICH
GIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKCTYECLEKAIAIVKPGVRYREVG
EVINRHATMSGLSVVKSYCGHGIGELFHCAPNIPHYARNKAVGVMKAGQVFTIEPMINAGVWRDRMWPDG
WTAVTADGKRSAQFEHTLLVTETGVEVLTARLPSSPDVFPWLKPSS
>gnl|CDD|215608 PLN03159, PLN03159, cation/H(+) antiporter 15; Provisional
STSQMSTGKNPSTASSVVCYAPMMITTNGIWQGDNPLDFSLPLFILQLTLVVVTTRLLVFILKPFRQPRV
ISEILGGVILGPSVLGQSEVFANTIFPLRSVMVLETMANLGLLYFLFLVGVEMDISVIRRTGKKALAIAI
AGMALPFCIGLAFSFIFHQVSRNVHQGTFILFLGVALSVTAFPVLARILAEIKLINTELGRIAMSAALVN
DMCAWILLALAIALAENDSTSLASLWVLLSSVAFVLFCFYVVRPGIWWIIRRTPEGETFSEFYICLILTG
VMISGFITDAIGTHSVFGAFVFGLVIPNGPLGVTLIEKLEDFVSGLLLPLFFAISGLKTNVTKIQGPATW
GLLVLVIIMASAGKIMGTIIIAFFYTMPFREGITLGFLMNTKGLVEMIVLNVGRDQEVLDDESFAVMVLV
AVAMTALITPVVTVVYRPARRLVGYKRRTIQRSKHDAELRMLVCVHTPRNVPTIINLLEASHPTKRSPIC
IYVLHLVELTGRASAMLIVHNTRKSGRPALNRTQAQSDHIINAFENYEQHAGCVSVQPLTAISPYSTMHE
DVCNLAEDKRVSLIIIPFHKQQTVDGGMEATNPAFRGVNQNVLANAPCSVGILVDRGLSGATRLASNQVS
HHVAVLFFGGPDDREALAYAWRMSEHPGITLTVMRFIPGEDAAPTASQPASSPSDPRIPTVETDGKKERQ
LDEEYINEFRARNAGNESIVYTEKVVSNGEETVAAIRSMDSAHDLFIVGRGQGMISPLTAGLTDWSECPE
LGAIGDLLASSDFAATVSVLVVQQYVGTGPQPDDLGTPESPAHSPEQYYSYNLNNRRPPSQR
>gnl|CDD|215609 PLN03160, PLN03160, uncharacterized protein; Provisional
MAETEQVRPLAPAAFRLRSDEEEATNHLKKTRRRNCIKCCGCITATLLILATTILVLVFTVFRVKDPVIK
MNGVTVTKLELINNTTLRPGTNITLIADVSVKNPNVASFKYSNTTTTIYYGGTVVGEARTPPGKAKARRT
MRMNVTVDIIPDKILSVPGLLTDISSGLLNMNSYTRIGGKVKILKIIKKHVVVKMNCTMTVNITSQAIQG
QKCKRHVDL
>gnl|CDD|178706 PLN03161, PLN03161, Probable xyloglucan endotransglucosylase/hydrolase protein; Provisional
MASLKTLLVALFAALAAFDRSFVEADFSKSMYFTWGADHSSMLGNGDNLQLVLDQSSGSGIKSKRAFLFG
SIEMLIKLVPGNSAGTVTAYYLSSTGSRHDEIDFEFLGNVSGQPYTIHTNIYTQGNGSREQQFRPWFDPT
ADFHNYTIHWNPSEVVWYVDGTPIRVFRNYENEGIAYPNKQGMRVYSSLWNADNWATQGGRVKIDWTLAP
FVARGRRFRARACKWNGPVSIKQCADPTPSNWWTSPSYSQLTNAQLTQMKKVRDNFMIYDYCKDTKRFNG
VMPPECFKPQF
>gnl|CDD|178707 PLN03162, PLN03162, golden-2 like transcription factor; Provisional
MAMDMARIDEEPAVEVHNLSNNLLVHCVLDALPDSSPCLKSSETSFEAAVAEEDEEGGRPLFGDEEDIIN
NSNDHDASPSCDAAAAAHEDFAECLNFVTEADCGDVGVQCFEDFDKLPDCGDAGESRKAEEEGCVRIGGD
GEQGELLESMSLDCSRNSENLELGDLGELLEGSERLDSVPGNEVGEEEALLLAEAAKATGDVVSASDSGE
CSSVDRKDNQASPKSCKNAAPGKKKAKVDWTPELHRRFVHAVEQLGVEKAFPSRILELMGVQCLTRHNIA
SHLQKYRSHRRHLAAREAEAASWTHRRAYTQAPWPRSSRRDGLPYLVPIHTPHIQPRPSMAMAMQPQLQT
PHHPISTPLKVWGYPTVDHSNVHMWQQPAVATPSYWQAADGSYWQHPATGYDAFSARACYPHPMQRVPLG
TTHAGLPIMAPGFPDESCYYGDDMLAASMYLCNQSYDSEIGRAAGVAACSKPIETHLSKEVLDAAIGEAL
ANPWTPPPLGLKPPSMEGVIAELQRQGINTVPPSTC
>gnl|CDD|215610 PLN03164, PLN03164, 3-oxo-5-alpha-steroid 4-dehydrogenase, C-terminal domain containing protein; Provisional
GTLPIVIASLPSSKLNSFRGLVLGFARRGKILHSSSQKFTVPQRFFSHFYVVGVVWTTLLLAATWLYAYK
MAPLSSEEFQYSDIASQLAGGSHIFSFHKSRSTPVEHRYRVWRSVFLLLLMEIHVLRRLYESLYVFKYSP
SARMHILGYLTGLFFYVAAPLSLCCNCAPEVAKFVGNQVAEFIVKGKSAMSAIEFDWWDFVSPLMKLGWF
QWIGAAIFLWGWIHQYRCHAILGSLREHKKQADEYVIPYGDWFEMVSCPHYLAEIVIYAGLLIASGGTDL
TIWLLFGFVVANLTFAAAETHRWYLQKFENYPRNRYAIIPFVY
>gnl|CDD|178709 PLN03165, PLN03165, chaperone protein dnaJ-related; Provisional
VDLDQNTIVAISVGVVSIAVGIGIPVFYETQIDNAAKRENTQPCFPCSGTGAQVCRFCVGSGNVTVELGG
GEKEVSKCINCDGAGSLTCTTCQGSGIQPRYLDRREFKDDD
>gnl|CDD|178710 PLN03166, PLN03166, 60S ribosomal protein L34; Provisional
MVQRLTYRKRHSYATKSNQHRVVKTPGGKLVYQTTKKRASGPKCPVTGKRIQGIPHLRPAEYKRSRLSRN
RRTVNRAYGGVLSGSAVRERIIRAFL
>gnl|CDD|215611 PLN03167, PLN03167, Chaperonin-60 beta subunit; Provisional
MASTFTATSSVGSLAAPNGHKSDNRLSSFASISSSSFGRRQSVRLRRSRSPKVKAAKELHFNKDGSAIKK
LQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAKTNDLA
GDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSELADVAAVSAGNNY
EVGNMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKK
ITNARDLIGILEDAIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILT
GGTVIREEVGLSLDKVGKEVLGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLN
ERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEGIVVGGGCTLLRLASKVDAIKDTLEND
EQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNPKFGYNAATGKYEDLMAAGIIDPTKVVRCC
LEHAASVAKTFLTSDCVVVEIKEPEPVPAGNPMDNSGYGY
>gnl|CDD|178712 PLN03168, PLN03168, chalcone synthase; Provisional
TRAALPRGQPRAEGPACVLGIGTAVPPAEFLQSEYPDFFFNITNCGEKEALKAKFKRICDKSGIRKRHMF
LTEEVLKANPGICTYMEPSLNVRHDIVVVQVPKLAAEAAQKAIKEWGGRKSDITHIVFATTSGVNMPGAD
HALAKLLGLKPTVKRVMMYQTGCFGGASVLRVAKDLAENNKGARVLAVASEVTAVTYRAPSENHLDGLVG
SALFGDGAGVYVVGSDPKPEVEKALFEVHWAGETILPESDGAIDGHLTEAGLIFHLMKDVPGLISKNIEK
FLNEARKCVGSPDWNEMFWAVHPGGPAILDQVEAKLKLTKDKMQGSRDILSEFGNMSSASVLFVLDQIRQ
RSVKMGASTLGEGSEFGFFIGFGPGLTLEVLVLRAAANV
>gnl|CDD|215612 PLN03169, PLN03169, chalcone synthase family protein; Provisional
MSNGSSSASKAGSRRAANPGKATILALGKAFPSQLVPQEYLVDGYFRDTKCDDPALKEKLERLCKTTTVK
TRYVVMSKEILDKYPELATEGTPTIKQRLDIANEAVTQMAVEASLACIKEWGRPVSDITHLVYVSSSEAR
LPGGDLYLAKQLGLSPDVQRVMLYFLGCSGGVAGLRVAKDIAENNPGSRVLLTTSETTILGFRPPSPDRP
YDLVGAALFGDGAAAVIIGADPIPVSESPFFELHTAIQQFLPGTEKTIDGRLTEEGINFKLGRELPQKIE
DNIEGFCKKLMKKAGLVEKDYNDLFWAVHPGGPAILNRLEKKLKLAPEKLECSRRALMDYGNVSSNTIVY
VLEYMREELKKKGEEDEEWGLILAFGPGITFEGILARNLTA
>gnl|CDD|178714 PLN03170, PLN03170, chalcone synthase; Provisional
MAGATVTVEEVRKAQRATGPATVLAIGTATPANCVHQADYPDYYFRITKSEHMTELKEKFKRMCDKSQIR
KRYMHLTEEYLAENPNMCAYMAPSLDARQDIVVVEVPKLGKAAAQKAIKEWGQPKSKITHLVFCTTSGVD
MPGADYQLTKMLGLRPSVNRLMMYQQGCFAGGTVLRVAKDLAENNRGARVLVVCSEITAVTFRGPSESHL
DSMVGQALFGDGAAAVIVGADPDERVERPLFQLVSASQTILPDSEGAIDGHLREVGLTFHLLKDVPGLIS
KNIERSLEEAFKPLGITDYNSIFWVAHPGGPAILDQVEAKVGLEKERMRATRHVLSEYGNMSSACVLFIL
DEMRKRSAEDGQATTGEGFDWGVLFGFGPGLTVETVVLHSVPITTGAAITA
>gnl|CDD|178715 PLN03171, PLN03171, chalcone synthase-like protein; Provisional
MGSAAAPANLGEICRAQRADGLAAVLAIGTANPANCVPQDEFPDFYFRATKSDHLTALKDKFKRICQELG
VQKRYLHHTEELLSAHPEFLDHDAPSLDARLDIAADAVPELAAEAAKKAIAEWGRPAADITHLVVTTNSG
AHIPGVDFRLVPLLGLRPSVRRTMLHLNGCFAGAAALRLAKDLAENNRGARVLVVAAEITLLLFNGPDEG
CFQTLLNQGLFGDGAAAVIVGADADAAERPLFEIVSAAQAIIPESDDAINMHFTEGGLDGNIGTRQVPGL
IGDNIERCLLDAFAPLLGGDGGAEWNDLFWAVHPGSSAILDQVDAALGLEPEKLAASRRVLSDYGNMFGA
TVIFALDELRRQMEEAAAAGAWPELGVMMAFGPGLTVDAMLLHASGHPA
>gnl|CDD|178716 PLN03172, PLN03172, chalcone synthase family protein; Provisional
APSIAEIRKAQRAEGPATILAIGKATPANCVSQADYPDYYFRITNSEHMTELKEKFKRMCDKSMIKKRYM
HLTEEILKENPNMCAYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGA
DYQLTKLLGLKPSVKRFMMYQQGCFAGGTVLRLAKDLAENNAGSRVLVVCSEITAVTFRGPSDTHLDSLV
GQALFGDGAAAVIIGADPDTKIERPLFEIVSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIE
KSLVEAFAPIGINDWNSIFWIAHPGGPAILDQVEIKLDLKEEKLRATRHVLSDYGNMSSACVLFILDEMR
KKSIEEGKGSTGEGLEWGVLFGFGPGLTVETVVLHSVPAEAAH
>gnl|CDD|178717 PLN03173, PLN03173, chalcone synthase; Provisional
MVTVDEIRKAQRAEGPATIMAIGTSTPPNCVDQSTYPDYYFRITNSEHKVELKEKFKRMCEKSMIKKRYM
HLTEEILKENPSVCEYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGA
DYQLTKLLGLRSSVKRFMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLV
GQALFGDGAAAIIIGSDPVLGVEKPLFELVSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNVE
KSLTEAFKPLGISDWNSLFWIAHPGGPAILDQVEAKLALKPEKLRATRHVLSEYGNMSSACVLFILDEMR
KKSAEDGLKSTGEGLEWGVLFGFGPGLTVETVVLHSVAPTI
>gnl|CDD|215613 PLN03174, PLN03174, Chalcone-flavanone isomerase-related; Provisional
MVSLRFPFSFSQPPRAPSFFAAAAAVAAAAAAAAAAAAAIAASRNPPHPFLQNALNFHNSSSPPWASISL
ADPSPPSVVESKTGVSFPAEIGDSRRLLGVGLRKKSILGLKNIDVYAFGVYADDDDLKKLLGEKYGKLSA
SELKGNKEFIDDLMEADIKMTVRLQIVYGKLSIRSVRSAFEESVGSRLQKFGGSDNKELLQSFTSLFKDE
YKIPKGSVIDLSREPGHVLRTTIDGKEVGSIQSKLLCRSILDLYIGEDPFDKNAKEDIEENLASLLQD
>gnl|CDD|178719 PLN03175, PLN03175, hypothetical protein; Provisional
SNLDHNSGYLFPIDSPLSHDLGLGLFSHVGTFVDNSLHQSRQICIPGSLAFQEAFSCISKFAGALLFWFS
RASNPKLSRRLSGGQGSSSRASQSHIAQVKSCMQNLAGLPFGSQSKEEHAGQLLFAKISSFTIGRLWNEA
ERLHSCNVLSLAAALVPPLENISPKVLAMPLGNDDVQVSEPTDQRYCEVEHSGCSGLSFPDLNWTRDAVE
PRTGIEFPMLLDENNSSLTSEVLVGTGSRTMKIIRIKSLKVYAFGFYVHPNSVCEKLGPKYASVPASELK
KCPDFYEDLLREDIVMTVRLVVNYNGLKINTVRDAFEKSLRNRLQKMNPNTDYNCLKTFGSFFTEDIPIP
AGTKIDFRRTSDGQLITEIGGNQIGAVRSKDLCRAFFDMYIGDVPVSEQTKEEIGQNVAGIIRRC
>gnl|CDD|178720 PLN03176, PLN03176, flavanone-3-hydroxylase; Provisional
MAPSTLTALAEEKTLQASFVRDEDERPKVAYNQFSNEIPVISIAGIDDGGEKRAEICNKIVEACEEWGVF
QIVDHGVDAKLVSEMTTLAKEFFALPPEEKLRFDMSGGKKGGFIVSSHLQ
>gnl|CDD|215614 PLN03178, PLN03178, leucoanthocyanidin dioxygenase; Provisional
MTAAVPRVEALASSGVSSIPKEYIRPPEERPSIGDVFEEEKKAAGPQVPVVDLSNIESDDEVVREACVEA
VRAAAAEWGVMHLVGHGIPADLLDRVRKAGEAFFRLPIEEKEKYANDQARGAAQGYGSKLAANASGQLEW
EDYFFHLTLPEDKRDPSLWPKTPPDYVPATSEYSRSLRSLATKLLAILSLGLGLPEDRLEKEVGGLEELL
LQMKINYYPRCPQPDLALGVEAHTDVSALTFILHNMVPGLQVLYEGKWVTAKCVPDSIVVHIGDTLEILS
NGRYKSILHRGLVNKEKVRISWAVFCEPPKEKIILKPLPELVSKEEPPKFPPRTFGQHVSHKLFKKPQDE
RNIDAADISN
>gnl|CDD|215615 PLN03180, PLN03180, reversibly glycosylated polypeptide; Provisional
ASVSPAPLLKDELDIVIPTIRNLDFLEMWRPFFQPYHLIIVQDGDPSKEIKVPEGFDYELYNRNDINRIL
GPKASCISFKDSACRCFGYLVSKKKYIFTIDDDCFVAKDPSGKLINALEQHIKNLLSPSTPFFFNTLYDP
YREGADFVRGYPFSLREGVPTAVSHGLWLNIPDYDAPTQLVKPLERNTRYVDAVMTIPKGTLFPMCGMNL
AFDRELIGPAMYFGLMGDGQPIGRYDDMWAGWCAKVICDHLGLGVKTGLPYIWHSKASNPFVNLKKEYKG
IFWQEEIIPFFQSVRLPKEAVTVEDCYIELAKQVKEKLGKVDPYFTKLADAMVTWIEAWKELNSPS
>gnl|CDD|215616 PLN03181, PLN03181, glycosyltransferase; Provisional
MAAPEASPFHYSPMPMGKYGGARTRASCFSDGVLFLGGAVVAFLLVWSLASILSPSPNPSLVSSSTNARA
SSCPVAGSGVNLGYDPPDPTFYDDPDLSYSIEKPIKNWDEKRAEWLKLHPSFAPGAEERVVMVTGSQPTP
CKNPIGDHLLLRFFKNKVDYCRIHGYDIFYNNALLHPKMNSYWAKLPVVRAAMLAHPEAEWIWWVDSDAV
FTDMDFKLPLHRYRDHNLVVHGWPKLIYEKRSWTALNAGVFLIRNCQWSLDFMDAWASMGPASPEYAKWG
KILRSTFKDKLFPESDDQSALVYLLYKHKEKWGDKIYLEGEYYFEGYWAEIVGRLDNITERYLEMEREDA
TLRRRHAEKVSERYAAFREEALKGPAGGGKGSWRRPFVTHFTGCQPCSGDHNKMYSGDSCWNGMRRALNF
ADNQVLRAYGFVHADLLDSSTVQPLPFDYPAEA
>gnl|CDD|215617 PLN03182, PLN03182, xyloglucan 6-xylosyltransferase; Provisional
MLQRCLGTPRGRQLQRTLNNLKITILCGFVTILVLRGTIAGKFGTPEQDFVELRAHFLSARRIEEPSRVL
AEIRFDDDLTDLDEVEEERWDPNTPYTLGPKISDWDEQRRRWLRKNPGFPSFVNGKPRVLLVTGSQPKPC
ENPVGDHYLLKSLKNKIDYCRLHGIEIFYNMAHLDAEMAGFWAKLPLLRKLMLAHPEVEWIWWMDSDALF
TDMTFEIPLEKYEGYNLVIHGWDELVYDQKSWIGLNTGSFLIRNCQWSLDLLDAWAPMGPKGPIRDEAGK
ILTAELKGRPAFEADDQSALVYLLLTQRERWGDKVYLENSYYLHGYWVGLVDRYEEMMEKYHPGLGDDRW
PFVTHFVGCKPCGGYGDYPVERCLKQMERAFNFADNQVLELYGFRHKSLASAEVKRVRNDTSNPLEAKDE
LGLRHPAFK
>gnl|CDD|178725 PLN03183, PLN03183, acetylglucosaminyltransferase family protein; Provisional
MGSVNVEKRWVFPLVITSLVCVFLLATSFNMGLVSSLRTINSIFSIFPLSRTNQTRLEFAESKVNQSPHP
PPVQDKLPRFAYLVSGSKGDLEKLWRTLRALYHPRNQYVVHLDLESPAEERLELASRVENDPMFSKVGNV
YMITKANLVTYRGPTMVANTLHACAILLKRSKDWDWFINLSASDYPLVTQDDLIHTFSTLDRNLNFIEHT
SQLGWKEEKRAMPLIIDPGLYSTNKSDIYWVTPRRSLPTAFKLFTGSAWMVLSRSFVEYCIWGWDNLPRT
LLMYYTNFVSSPEGYFHTVICNVPEFAKTAVNHDLHYISWDNPPKQHPHTLSLNDTEKMIASGAAFARKF
RRDDPVLDKIDKELLGRKNGSFTPGGWCSGKPKCSRVGDPAKIKPGPGAQRLKGLVSRLVLEAKLGQNQC
K
>gnl|CDD|215618 PLN03184, PLN03184, chloroplast Hsp70; Provisional
FGGRLAPFSTPTAAFLKMGKRRGNGARRRAGGPLRVVAEKVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQ
RTTPSVVAYTKNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSEVDEESKQVSYRVVRDENGNVKLDC
PAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAGLEVLRIINEPT
AASLAYGFEKKSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNFKKDE
GIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADGPKHIDTTLTRAKFEELCSDLLDRCKT
PVENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEVSD
IVLLDVTPLSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFR
LDGIPPAPRGVPQIEVKFDIDANGILSVSATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKE
KRDAVDTKNQADSVVYQTEKQLKELGDKVPADVKEKVEAKLKELKDAIASGSTQKMKDAMAALNQEVMQI
GQSLYNQPGAGGAGPAPGGEAGSSSSSSSGGDGDDVIDADFTD
>gnl|CDD|215619 PLN03185, PLN03185, phosphatidylinositol phosphate kinase; Provisional
GELVLSNGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSG
TYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGGKMSGKGT
LTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVFYPAGSRVPAVQEFYLNALRKRGV
LPDLRRQNQVLSSHNSEQLSRGVSSDKLSKGSLLPLEQSRNRNVSLERRWSLEVSIEKVIGHDYSGSSSA
VLDEGSEVEYKANRPILEREYMQGVLISELVLNNSFSSTSRRAKRRQKKLVKEIKRPGETIIKGHRSYDL
MLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFWMNFPKAGSQLTPSHQSEDFKWKDYCPMVFRNLREM
FKIDAADYMMSICGNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTL
ITKFFGLHRIKPSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDENTTLKDLDLNYSFYL
EPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHFRAPQHLRSLLPYSRSITADGLEVVAEEDTIEDEEL
SYPEGLVLVPRGADDGSTVPGPHIRGSRLRASAAGDEEVDLLLPGTARLQIQLGVNMPARAERIPGREDK
EKQSFHEVYDVVLYLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFIQKVFP
>gnl|CDD|178728 PLN03186, PLN03186, DNA repair protein RAD51 homolog; Provisional
MAQAVAAAAAQAMQEEEEEEAAHGPFPIEQLQASGIAALDIKKLKDAGIHTVESLAYAPKKDLLQIKGIS
EAKVEKILEAASKLVPLGFTTASQLHAQRQEIIQITTGSRELDKILEGGIETGSITEIYGEFRTGKTQLC
HTLCVTCQLPLDQGGGEGKAMYIDTEGTFRPQRLIQIAERFGLNGADVLENVAYARAYNTDHQSELLLEA
ASMMAETRFALMIVDSATALYRTEFSGRGELSARQMHLGKFLRSLQRLADEFGVAVVITNQVVAQVDGSA
FFAGPQLKPIGGNIMAHASTTRLALRKGRGENRICKVISSPCLPEAEARFSISSEGVTDVKD
>gnl|CDD|215620 PLN03187, PLN03187, meiotic recombination protein DMC1 homolog; Provisional
MSASAQADEGAQLQLVEAEEVDEEEDLFESIDKLISQGINAGDVKKLQDAGIYTCNGLMMHTKKNLTGIK
GLSEAKVDKICEAAEKLLNQGFITGSDALLKRKSVVRITTGSQALDELLGGGIETRCITEAFGEFRSGKT
QLAHTLCVTTQLPTEMGGGNGKVAYIDTEGTFRPDRIVPIAERFGMDADAVLDNIIYARAYTYEHQYNLL
LGLAAKMAEEPFRLLIVDSVIALFRVDFTGRGELAERQQKLAQMLSRLTKIAEEFNVAVYMTNQVIADPG
GGMFISDPKKPAGGHVLAHAATIRLMLRKGKGEQRVCKVFDAPNLPEAEAEFQITSGGIMDAKD
>gnl|CDD|215621 PLN03188, PLN03188, kinesin-12 family protein; Provisional
MKHFMLPRNAILRETSSGEEQSPNPSSHKSKPSSRKLKSSKENAPPPDLNSLTSDLKPDHRSASAKLKSP
LPPRPPSSNPLKRKLSAETAPENGVSDSGVKVIVRMKPLNKGEEGEMIVQKMSNDSLTINGQTFTFDSIA
DPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPANGLLEEHLSGDQQGLTPRVFERL
FARINEEQIKHADRQLKYQCRCSFLEIYNEQITDLLDPSQKNLQIREDVKSGVYVENLTEEYVKTMKDVT
QLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGD
RLKEAGNINRSLSQLGNLINILAEISQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSE
TFSTLRFAQRAKAIKNKAVVNEVMQDDVNFLREVIRQLRDELQRVKANGNNPTNPNVAYSTAWNARRSLN
LLKSFGLGPPPSLPHVDEDGDEEMEIDEEAVERLCVQVGLQPAGAAEGNNVDMGRVESIHSSDQQSIIKQ
GSEDTDVDMEEAISEQEEKHEITIVDCAEPVRNTQNSLQIDTLDHESSEQPLEEKNALHSSVSKLNTEES
PSKMVEIRPSCQDSVSESGVSTGVSVADESNDSENELVNCASPSSLSIVPVEVSPVLKSPTLSVSPRIRN
SRKSLRTSSMLTASQKDSEDESKLTPEDAEPSFAKSMKNNSSSALSTQKSKSFLAPTEHLAASLHRGLEI
IDSHRQSSALRRSSFRFSFKPADSKPITLVSKADVGVQTLPQADEISEENSKEFLCSNCKCRTQLDAKDA
DDSSNLQLVPVDGSESAEKSKKQVPKAVEKVLAGAIRREMALEEFCTKQASEITQLNRLVQQYKHERECN
AIIGQTREDKIIRLESLMDGVLSKEDFLEEELASLMHEHKLLKEKYENHPEVLRTKIELKRVQDELEHYR
NFYDMGEREVLLEEIQDLRSQLQYYIDSSLPSARKRNSLLKLTYSCEPSQAPPLNTIPESTDESPEKKLE
QERLRWTEAESKWISLAEELRTELDASRALAEKQKHELDTEKRCAEELKEAMQMAMEGHARMLEQYADLE
EKHIQLLARHRRIQEGIDDVKKAAARAGVRGAESKFINALAAEISALKVEREKERRYLRDENKSLQAQLR
DTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTLNQLVAESRLPKE
AIRPACNDDCMAKYDAGEPLSEGDQQWREEFEPFYKKEDGELSKLAEPSSWFSGYDRCNI
>gnl|CDD|215622 PLN03189, PLN03189, Protease specific for SMALL UBIQUITIN-RELATED MODIFIER (SUMO); Provisional
MGALTSNHKRSDECFNNPLSNSPDFHISKKPRFSMAQTPDSGNQHSSNSTASRISRYPEVKSPLRREVHA
PCRILKFGRDKSTDSSEKKQGLGNVMGNFLSRKYDMAKRSALDALRYYRKDKEVVDVGDELGKVEMISDD
SSIEEVEAVEMDVDEVEEKAEMGNGLSSDVKIVTKNGNLRVEDTSKMLDSLVLNRPETDVLSVEAYRKLL
QSAERRNSKLKDLGFEIELNEKRLSSLRQSRPKPKEPVEEVPREPFIPLTREEETEVKRAFSANNRRKVL
VTHENSNIDITGEILRCLKPGAWLNDEVINLYLELLKEREAREPKKFLKCHFFNTFFYKKLVSGKSGYDY
KAVRRWTTQKKLGYHLIDCDKIFVPIHQEIHWTLAVINKKDQKFQYLDSLKGRDPKILDALAKYYVDEVK
DKSEKDIDVSSWEQEFVEDLPEQKNGYDCGMFMIKYIDFYSRGLGLCFGQEHMPYFRLRTAKEILRLKAD
>gnl|CDD|215623 PLN03190, PLN03190, aminophospholipid translocase; Provisional
MDSQNPIEKPPSHEPILGSSSRRSVSSKDSRSVREVTFGDLGSRPVRHGSRGADSEMFSMSQKEISDEDA
RLVYLNDPEKSNERFEFAGNSIRTAKYSVFSFLPRNLFEQFHRVAYIYFLVIAVLNQLPQLAVFGRGASI
LPLAFVLLVTAVKDAYEDWRRHRSDRIENNRLAWVLVDDQFQEKKWKDIRVGEIIKIQANDTLPCDMVLL
STSDPTGVAYVQTINLDGESNLKTRYAKQETLSKIPEKEKINGLIKCEKPNRNIYGFQANMEVDGKRLSL
GPSNIILRGCELKNTAWAIGVAVYCGRETKAMLNNSGAPSKRSRLETRMNLEIIILSLFLIALCTIVSVC
AAVWLRRHRDELDTIPFYRRKDFSEGGPKNYNYYGWGWEIFFTFLMSVIVFQIMIPISLYISMELVRVGQ
AYFMIRDDQMYDEASNSRFQCRALNINEDLGQIKYVFSDKTGTLTENKMEFQCASIWGVDYSDGRTPTQN
DHAGYSVEVDGKILRPKMKVKVDPQLLELSKSGKDTEEAKHVHDFFLALAACNTIVPIVVDDTSDPTVKL
MDYQGESPDEQALVYAAAAYGFMLIERTSGHIVIDIHGERQRFNVLGLHEFDSDRKRMSVILGCPDKTVK
VFVKGADTSMFSVIDRSLNMNVIRATEAHLHTYSSLGLRTLVVGMRELNDSEFEQWHFSFEAASTALIGR
AALLRKVASNVENNLTILGASAIEDKLQQGVPEAIESLRTAGIKVWVLTGDKQETAISIGYSSKLLTNKM
TQIIINSNSKESCRKSLEDALVMSKKLTTVSGISQNTGGSSAAASDPVALIIDGTSLVYVLDSELEEQLF
QLASKCSVVLCCRVAPLQKAGIVALVKNRTSDMTLAIGDGANDVSMIQMADVGVGISGQEGRQAVMASDF
AMGQFRFLVPLLLVHGHWNYQRMGYMILYNFYRNAVFVLVLFWYVLFTCFTLTTAINEWSSVLYSVIYTA
LPTIVVGILDKDLSRRTLLKYPQLYGAGQRQEAYNSKLFWLTMIDTLWQSAVVFFVPLFAYWASTIDGSS
IGDLWTLAVVILVNLHLAMDIIRWNWITHAAIWGSIVATFICVIVIDAIPTLPGYWAIFHIAKTGSFWLC
LLAIVVAALLPRFVVKVLYQYFTPCDVQIAREAEKFGTFRESQPVEVEMNPILEPPRR
>gnl|CDD|215624 PLN03191, PLN03191, Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
MRTRRGKRPEAFWPSIVMKKWLNIKPKVYDFSEDEYDTETESEDDACSVKDVRVNVDEDHANRRQGNQSV
FGNQISDGGVSVSKGYSSKHRRGKSETLRAQYINTKDIRVTIGTWNVAGRLPSEDLEIEDWLSTEEPADI
YIIGFQEVVPLNAGNVLGAEDSRPIPKWEAIIRRTLNKSNKPESKHKSYSAPPSPVLRTSIVADELAEEV
DSLPLEMMNNEFIDAATGCPSLEPERNKNIGWPEHSLDATPQVVSSNSKLRRVFSSSARLGFKWPENPSL
FSPQRFALNARGLKRSHRSFGNLGLSWNEIKQRSEVPEVPEVIDSLSDVSDRSSEAEDDTFKEVPSYQLP
EDLIKDCRKVKQKYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQS
RLCFVCSHLTSGHKDGAEQRRNADVYEIIRRTRFSSVLDTDQPQTIPSHDQIFWFGDLNYRLNMLDTEVR
KLVAQKRWDELINSDQLIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRYVGENPKEGEKKRSPAWCDRI
LWLGKGIKQLCYKRSEIRLSDHRPVSSMFLVEVEVFDHRKLQRALNVNSAAASAVHPEPSF
>gnl|CDD|215625 PLN03192, PLN03192, Voltage-dependent potassium channel; Provisional
FQSTGSAGGGRGKGTGEEDDSGSLSLRNLSKVILPPLGVPSYNQNHIGSDGWIISPMDSRYRWWETLMVV
LVAYSAWVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTW
FLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWIRCARLLSVTL
FLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEMIF
IIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAESL
NQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYI
VVSGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDN
VVILKNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRT
PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAA
KRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSPTELRELLQ
KRELGHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLRNERCCNEAGKLINLP
PSLEELKAIAGEKLGFDARKAMVTNEEGAEIDSIEVIRDNDKLFVVEDEDSRR
>gnl|CDD|178735 PLN03193, PLN03193, beta-1,3-galactosyltransferase; Provisional
MSTKSRGEEYSSRSVVSRKWTLLLCLGCFCAGMLFTDRMWTIPESKGISRTTVTEAERLKLVSEGCDPKT
LYQKEVKRDSKDIIGEVSKTHNAIQTLDKTISNLEMELAAARAAQESILNGSPISEDLKKTQSSGKRRYL
MVVGINTAFSSRKRRDSVRATWMPQGEKRKKLEEEKGIIIRFVIGHSATSGGILDRAIEAEDRKHGDFLR
LDHVEGYLELSAKTKTYFATAVAMWDADFYVKVDDDVHVNIATLGETLVRHRKKPRVYIGCMKSGPVLSQ
KGVRYHEPEYWKFGENGNKYFRHATGQLYAISKDLASYISINQHVLHKYANEDVSLGSWFIGLDVEHIDD
RRLCCGTPPDCEWKAQAGNICVASFDWSCSGICRSADRIKEVHRRCGEGENALWSATF
>gnl|CDD|215626 PLN03194, PLN03194, putative disease resistance protein; Provisional
MKRSSTAQLNNRLFLHYPSSSSSAKPCDVFINHRGIDTKRTIATLLYDHLSRLNLRPFLDNKNMKPGDKL
FDKINSAIRNCKVGVAVFSPRYCESYFCLHELALIMESKKRVIPIFCDVKPSQLRVVDNGTCPDEEIRRF
NWALEEAKYTVGLTFDSLKGNWSEVVTMASDAVIKNLIELEEEKSVR
>gnl|CDD|215627 PLN03195, PLN03195, fatty acid omega-hydroxylase; Provisional
MKFPVSGMSGVLFIALAVLSWIFIHRWSQRNRKGPKSWPIIGAALEQLKNYDRMHDWLVEYLSKDRTVVV
KMPFTTYTYIADPVNVEHVLKTNFANYPKGEVYHSYMEVLLGDGIFNVDGELWRKQRKTASFEFASKNLR
DFSTVVFREYSLKLSSILSQASFANQVVDMQDLFMRMTLDSICKVGFGVEIGTLSPSLPENPFAQAFDTA
NIIVTLRFIDPLWKLKKFLNIGSEALLSKSIKVVDDFTYSVIRRRKAEMDEARKSGKKVKHDILSRFIEL
GEDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSELKALEKERAKEEDPEDSQ
SFNQRVTQFAGLLTYDSLGKLQYLHAVITETLRLYPAVPQDPKGILEDDVLPDGTKVKAGGMVTYVPYSM
GRMEYNWGPDAASFKPERWIKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQMKMALALLCRFFKFQLVP
GHPVKYRMMTILSMANGLKVTVSRRS
>gnl|CDD|215628 PLN03196, PLN03196, MOC1-like protein; Provisional
ARAFSSASASRSLPSSGSSRSSRPGRSQRAPLRAKQSSSPSLYERPSVTWGLLEMKKEKLVNREKVLDFL
RGIGIDPDELDGLELPSTVDVMRERVEFLHKLGLTIEDINEYPLVLGCSVKKNMIPVLDYLEKLGVTRSS
LPELLRRYPQVLHASVVVDLAPVVKYLQGLDVKRQDIPRVLERYPELLGFKLEGTMSTSVAYLVSIGVAP
RDIGPMLTRFPEILGMRVGNNIKPKVDYLESLGLPRLAVARILEKRPYILGFDLEETVKPNVECLLEFGV
RKEALPSVIAQYPDILGLDLKAKLAEQQYWLTSKLKIDPEDFGRVIEKLPQIVSLNRNVALKHVEFLRGR
GFSAQDVAKMVVRCPQILALNLEIMKPSLEFFKKEMKRPLKELVEFPAYFTYGLESRIKPRYERVAKKGI
KCSLAWFLNCSDDKFEQRMSGDFIEGEEMEPLFSMGGKLEMPGSESVSDEEDDDDDDEVLYRRTVSL
>gnl|CDD|178739 PLN03198, PLN03198, delta6-acyl-lipid desaturase; Provisional
MVFAGGGLQQGSLEENIDVEHIASMPLFGDFFNVIIGSVGSWSFHGIQGLKRLTSKKRVSDSAAVQCISA
EVQKNSNSQEAAEALAESVVKPTRRRSSKEKKSKSHLLSEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPG
GSVISTYFGRDGTDAFSSFHAASTWKILQDFYIGDVDNVEPTPELLKDFRDLRALFLREQLFKSSKLYYV
FKLLTNIAIFAASIAIICCSKSISAVLASACMMALCFQQCGWLSHDFLHNQVFETRWLNEVVGYLIGNAV
LGFSTGWWKEKHNLHHAAPNECDQLYQPIDEDIDTLPLIAWSKDILATVENKTFLRILQYQHLFFMALLF
FARGSWLFWSWRYTSTAKLAPADRLLEKGTILFHYFWFIGTACYLLPGWKPLVWMAVTELMCGMLLGFVF
VLSHNGMEVYNKSKEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIK
HGLVYEDVSIAAGTCKVLKALKEVAEAAAEQHAAAS
>gnl|CDD|178740 PLN03199, PLN03199, delta6-acyl-lipid desaturase-like protein; Provisional
MGKGGDAAAAKGRSAALKLAEKPQKISWQEVKKHASPDDAWIIHQNKVYDVSNWHDHPGGAVIFTHAGDD
MTDIFAAFHAPGSQALMKKFYIGDLIPESTEHKDPQQIAFEKGYRDLRAKLIMMGMFKSNKMFYAYKCLF
NMAIWAAACALVFYSDRFAMHIASALLLGLFFQQCGWLAHDFLHHQVFKKRKHGDLGGIFWGDLMQGFSM
QWWKNKHNGHHAVPNLHCSSADAQDGDPDIDTMPLLAWSLKQAQSFREINADGKDSGFVKFAIKFQAFFY
FPILLLARISWLNESFKCAFGLGAASENAALELEAKGLQYPLLEKAGILLHYAWMFTLSSGFGRFSFAYS
AFYFFTATASCGFFLAIVFGLGHNGMATYDADARPDFWKLQVTTTRNIIGGHGFPQAFVDWFCGGLQYQV
DHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEADLVDGTMEVLHHLGKVADDFLVDFVKDFPAM
>gnl|CDD|215629 PLN03200, PLN03200, cellulose synthase-interactive protein; Provisional
RTSEMDDPDGTLASVAQCIEQLRAKSSSPQEKELTTARLLELAKTREEARKAIGSHSQAMPLLVSLLRSG
TLGAKVNAAAVLGVLCKEEDLRVKVLLGGCIPPLLSLLKSGSAEAQKAAAEAIYAVSSGGLSDHVGSKIF
STEGVVPSLWDQLQPGNKQDKVVEGLLTGALRNLCGSTDGFWSATLEAGGVDILVKLLSSGNSDAQANAA
SLLARLMMAFESSISKVLDAGAVKQLLKLLGQGNEVSVRAEAAGALEALSSQSKEAKQAIADAGGIPALI
NATVAPSKEFMQGEFAQALQENAMGALANICGGMSALILYLGELSESPRSPAPIADTLGALAYALMVFDS
SAESTRAFDPTVIEQILVKLLKPRDTKLVQERIIEALASLYGNAYLSRKLNHAEAKKVLVGLITMATADV
QEELIRALSSLCCGKGGLWEALGGREGVQLLISLLGLSSEQQQEYAVALLAILTDEVDESKWAITAAGGI
PPLVQLLETGSQKAKEDSATVLWNLCCHSEDIRACVESAGAVPALLWLLKNGGPKGQEIAAKTLTKLVRT
ADAATISQLTALLLGDLPESKVHVLDVLGHVLSVASLEDLVREGSAANDALRTLIQLLSSSKEETQEKAA
SVLADIFSSRQDLCESLATDEIINPCIKLLTNNTEAVATQSARALAALSRSIKENRKVSYAAEDAIKPLI
KLAKSSSIEVAEQAVCALANLLSDPEVAAEALAEDIILPLTRVLREGTLEGKRNAARALAQLLKHFPVDD
VLKDSVQCRGTVLALVDLLNSTDLDSSATSEALEALALLARTKGGANFSHPPWAVLAEVPSSLEPLVRCL
AEGHPLVQDKAIEILSRLCRDQPVVLGDLIANASKCISSLADRIINSSSLEVKIGGTALLICAAKEHRQL
VMEALDESGYLKLLIQALVDMLKQNSKKESLSIEIQTPRGFLESNLFADGDDFEVPDPATILGGTVALWL
LSVIASHDAKSKLAIMEAGGIEVLTEKLASYTSNRQAEFEDSESIWISALLLAILFQDRDVVRAPATMRA
IPSLANLLKSEETIDRYFAAQALASLVCNGSRGTLLAVANSGAVGGLISLLGCAESDISNLVALSEEFSL
VRNPDQVALERLFRVEDIRVGATARKAIPLLVDLLKPIPDRPGAPPLALGLLTQLAEGSDVNKLAMAEAG
ALDALTKYLSLGPQDSTEEAASELLRILFSSPELRRHESAFGAVNQLVAVLRLGSRSARYSAARALQELF
SAEHIRDSELARQAVQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAIADVEGNALENLCKILSSDS
SLELKEDAAELCRVLFTNTRIRSTPAAARCIEPLISLLVSESSTAQEAGVCALDRLLDDEQLAELVAAHG
AVVPLVGLVVGTNYVLHEAAISALIKLGKDRPPCKLDMVKAGIIERVLDILPEAPDSLCSAIAELLRILT
NNSSIAKGQSAAKVVEPLFLLLTRPDLGTWGQHSALQALVNILEKPQCLASLTLTPSQAIEPLIPLLESP
SQAVQQLAAELLSHLLAEEHFQQDITTQNAVVPLVRLAGIGILSLQQRAVKALESISLSWPKAVADAGGI
FELSKVILQADPQPPHALWESAASVLSNILRFSSEYYFEVPVAVLVKLLRSTSESTVVVALNALLVLERD
DSSSAEQMAESGAIEALLELLRSHQCEEAAARLLEALFNNVKVREMKATKYAIAPLSQYLLDPQTRSQQA
RLLAALALGDLFQHEGLARSTDAVSACRALVSLLEDQPTEEMKMVAICALQNLVMHSRTNKRAVAEAGGV
QVVQELLLSSNPDTSGQAALLIKLLFSNHTIQEYASSELIRALTAALEKDLWSTATVNEEVLRALNVLFS
NFPKLRATEAATLCIPHLVGALKSGSEAAQEAALDTLFLLRQSWSAMPAEVARAQAMAAAEAIPVLQMLM
KSGPPRFHERAESLLQCLPGSLTVTIKRGNNLKQSMGNTNAFCKLTLGNGPPRQTKVVSHSSSPEWKEGF
TWAFDSPPKGQKLHISCKSKNTFGKSSLGKVTIQIDRVVMEGTYSGEYSLNPESNKDGSSRTLEIEFQWS
NR
>gnl|CDD|215630 PLN03201, PLN03201, RAB geranylgeranyl transferase beta-subunit; Provisional
TSGPMGELVVDKHVRYIKSLEKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQH
ESGGFGGNTGHDPHILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCAL
CCLSLLKRLDKINVEKAVDYIVSCKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLC
ERQVKSGGLNGRPEKLPDVCYSWWVLSSLIIIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFH
TFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRIGLR
>gnl|CDD|215631 PLN03202, PLN03202, protein argonaute; Provisional
KDALPPPPPVVPPNVVPIKLEPTKKPSKPKRLPMARRGFGSKGQKIQLLTNHFKVSVNNPDGHFFHYSVS
LTYEDGRPVDGKGIGRKVIDKVQETYSSDLAGKDFAYDGEKSLFTVGALPQNKLEFTVVLEDVSSNRNNG
NGSPVGNGSPNGGDRKRSRRPYQSKTFKVEISFAAKIPMQAIANALRGQESENSQDALRVLDIILRQHAA
KQGCLLVRQSFFHNDPKNFVDLGGGVLGCRGFHSSFRTTQGGLSLNIDVSTTMIVQPGPVVDFLIANQNV
RDPFQIDWSKAKRMLKNLRVKVSPSNQEYKITGLSEKPCKEQTFSLKQRNGNGNEVETVEITVYDYFVKH
RGIELRYSGDLPCINVGKPKRPTYFPIELCSLVSLQRYTKALSTLQRSSLVEKSRQKPQERMKVLTDALK
SSNYDADPMLRSCGISISSQFTQVEGRVLPAPKLKVGNGEDFFPRNGRWNFNNKKLVEPTKIERWAVVNF
SARCDIRHLVRDLIKCGEMKGINIEPPFDVFEENPQFRRAPPPVRVEKMFEQIQSKLPGPPQFLLCILPE
RKNSDIYGPWKKKNLSEFGIVTQCIAPTRVNDQYLTNVLLKINAKLGGLNSLLAIEHSPSIPLVSKVPTI
ILGMDVSHGSPGQSDVPSIAAVVSSRQWPLISRYRASVRTQSPKVEMIDSLFKPVGDKDDDGIIRELLLD
FYTSSGKRKPEQIIIFRDGVSESQFNQVLNIELDQIIEACKFLDESWSPKFTVIVAQKNHHTKFFQAGSP
DNVPPGTVVDNKICHPRNNDFYMCAHAGMIGTTRPTHYHVLLDEIGFSADDLQELVHSLSYVYQRSTTAI
SVVAPVCYAHLAAAQMGQFMKFEDMSETSSSHGGITSAGAVPVPELPRLHENVASSMFFC
>gnl|CDD|178744 PLN03205, PLN03205, ATR interacting protein; Provisional
MAGNDDEDEDDFIKAIDIIEAIEAKADMYRLLPPPSLPTFLPAPPVSEMTTPSTKISSSLSHPMQLQSSA
GQKRDQIQVPDPFISYSPPRELSQRVVGGFNDALMDYSNSTVVTAAKPISPNSSNRCCDSEKDLEIDRLK
KELERVSKQLLDVEQECSQLKKGKNKEMESKNLCADDNKGQCSTVHASKRIDLEPDVATSSVIHRENDSR
MALDDKKSFKTAGVQADLANHADLSKKLLDIWRTSNYQDPRKNLISELLLACSTDLQIIFSFMKISAPPH
EIDKQEAKTSSDIQSSKALESEKVYHLYSAVTKISYGFVNLKSLVEPLLDLCKAETAVLVHRSLRVLHVL
LEHICGDEKRFEASWDANWHSLFELMNQIASIRTEEDVKLEALSIMNIIVMSTDAYTARESFVSKEVFES
ISLLLRKEGGLHVRKEAIHLFYLLLNCPKLYDRFDSLHEEKNSSDTENDSEGNFFALEAFGKIFEGLADC
LTSPRKTSEDLELCRNVIMILALAASSGNSGYELLSNHKLPQDSNFLMLILHLLVAEIDSESTEFHPKAE
IFKARTLLMREILILLNRLVSGLSSSATILKELTKSRDMASLTVDAATRLSRKRNLLGKPENSVERMRNT
EIMDLARIFKKRVFAFLGDNTI
>gnl|CDD|178745 PLN03206, PLN03206, phosphoribosylformylglycinamidine synthase; Provisional
AELLRKVQTKVSNDIVSIETEQCFNVGLESPLSAEKLETLKWLLRETFEPENLGTESFLEAKKSEGLNAV
VVEVGPRLSFTTAWSTNAVSICSACGLTEVTRLERSRRYLLFSSSPLDESQINAFAAMVHDRMTECVYPQ
PLTSFESGVVPEPVYTVPVMEEGRAALEEINKEMGLAFDEQDLDYYTRLFRDDIKRDPTNVELFDIAQSN
SEHSRHWFFSGKLVIDGQPMPKTLFQMVKDTLKANPNNSVIGFKDNSSAIRGFVVQPLRPVSPGSPSPLA
PVDRDLDILLTAETHNFPCAVAPYPGAETGAGGRIRDTHATGRGSFVVAGTAGYCVGNLRIEGSYAPWED
SSFVYPSNLASPLQILIDASNGASDYGNKFGEPLIQGYTRTFGMRLPNGERREWLKPIMFSGGIGQIDHT
HLTKGEPDIGMLVVKIGGPAYRIGMGGGAASSMVSGQNDAELDFNAVQRGDAEMSQKLYRVVRACVEMGE
DNPIVSIHDQGAGGNCNVVKEIIYPKGAEIDIRAVVVGDHTLSVLEIWGAEYQEQDALLIKPESRDLLQS
ICDRERCSMAVIGTIDGSGRVVLVDSAAPEKCEANGLPPPPPAVDLDLEKVLGDMPQKTFEFKRVANKLE
PLDIPPGITVMDALKRVLRLPSVCSKRFLTTKVDRCVTGLVAQQQTVGPLQIPLADVAVIAQTHTGLTGG
ACAIGEQPIKGLVDPKAMARLAVGEALTNLVWAKVTALSDVKASGNWMYAAKLDGEGADMYDAAVALRDA
MIELGVAIDGGKDSLSMAAQAGGEVVKAPGNLVISAYVTCPDITKTVTPDLKLGDDGVLLHVDLGKGKRR
LGGSALAQAYDQIGDDCPDLDDVAYLKKAFEATQDLIAKRLISAGHDISDGGLVVTLLEMAFAGNCGINV
DLPSSGHSAFETLFAEELGLVLEVSRKNLDAVMEKLAAAGVTAEVIGQVTASPLIEVKVDGATCLSEKTA
SLRDMWEETSFQLEKLQRLESCVAQEKEGLKSRKAPTWKLSFTPAFTDKKIMNATSKPKVAIIREEGSNG
DREMAAAFYAAGFEPWDVTMSDLLNGRISLDDFRGIVFVGGFSYADVLDSAKGWAGSIRFNEPLLQQFQE
FYNRPDTFSLGVCNGCQLMALLGWVPGPQVGGGLGAGGDPSQPRFVHNESGRFECRFTSVTIEDSPAIML
KGMEGSTLGVWAAHGEGRAYFPDESVLDEVLKSNLAPVRYCDDDGEPTEQYPFNPNGSPLGIAALCSPDG
RHLAMMPHPERCFLMWQFPWYPKEWGVDPAGPSPWLKMFQNAREWCE
>gnl|CDD|215632 PLN03207, PLN03207, stomagen; Provisional
MANECMTATTRCLTLFFLLFFLLLGAYVIQGSRNQSILPYDQSISYPHQETVKLLNGGHLSKSSRRLMIG
STAPTCTYNECRGCRYKCRAEQVPVEGNDPINSAYHYKCVCHR
>gnl|CDD|178747 PLN03208, PLN03208, E3 ubiquitin-protein ligase RMA2; Provisional
MEIEKDEDDTTLVDSGGDFDCNICLDQVRDPVVTLCGHLFCWPCIHKWTYASNNSRQRVDQYDHKREPPK
CPVCKSDVSEATLVPIYGRGQKAPQSGSNVPSRPSGPVYDLRGVGQRLGEGESQRYMYRMPDPVMGVVCE
MVYRRLFGESSSNMAPYRDMNVRSRRRAMQAEESLSRVYLFLLCFMFMCLFLF
>gnl|CDD|178748 PLN03209, PLN03209, translocon at the inner envelope of chloroplast subunit 62; Provisional
MEGTSLQSSAITTIPTSLTKCGFIEKPFLHGQLLRFPGFSKHPHSRKLRSLDIKAQASGATKFSSAAIEA
IPKELDTKDEDLAFVAGATGKVGSRTVRELLKLGFRVRAGVRSAQRAESLVQSVKQMKLDVEGTQPVEKL
EIVECDLEKPDQIGPALGNASVVICCIGASEKEVFDVTGPYRIDYLATKNLVDAATVAKVNHFILVTSLG
TNKVGFPAAILNLFWGVLCWKRKAEEALIASGLPYTIVRPGGMERPTDAYKETHNLTLSEEDTLFGGQVS
NLQVAELMACMAKNRRLSYCKVVEVIAETTAPLTPMEELLAKIPSQRVPPKESDAADGPKPVPTKPVTPE
APSPPIEEEPPQPKAVVPRPLSPYTAYEDLKPPTSPIPTPPSSSPASSKSVDAVAKPAEPDVVPSPGSAS
NVPEVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATAATDAAAPP
PANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRPLSPYTM
YEDLKPPTSPTPSPVL
>gnl|CDD|215633 PLN03210, PLN03210, Resistant to P. syringae 6; Provisional
MASSSSSSRNWVYDVFPSFSGEDVRITFLSHFLKELDRKLIIAFKDNEIERSQSLDPELKQAIRDSRIAV
VVFSKNYASSSWCLNELLEIVRCKEELGQLVIPVFYGLDPSHVRKQTGDFGEAFEKTCQNKTEDEKIQWK
QALTDVANILGYHSQNWPNEAKMIEEIANDVLGKLNLTPSNDFEDFVGIEDHIAKMSSLLHLESEEVRMV
GIWGSSGIGKTTIARALFSRLSRQFQSSVFIDRAFISKSMEIYSSANPDDYNMKLHLQRAFLSEILDKKD
IKIYHLGAMEERLKHRKVLIFIDDLDDQDVLDALAGQTQWFGSGSRIIVITKDKHFLRAHGIDHIYEVCL
PSNELALEMFCRSAFKKNSPPDGFMELASEVALRAGNLPLGLNVLGSYLRGRDKEDWMDMLPRLRNGLDG
KIEKTLRVSYDGLNNKKDKAIFRHIACLFNGEKVNDIKLLLANSDLDVNIGLKNLVDKSLIHVREDIVEM
HSLLQEMGKEIVRAQSNEPGEREFLVDAKDICDVLEDNTGTKKVLGITLDIDEIDELHIHENAFKGMRNL
LFLKFYTKKWDQKKEVRWHLPEGFDYLPPKLRLLRWDKYPLRCMPSNFRPENLVKLQMQGSKLEKLWDGV
HSLTGLRNIDLRGSKNLKEIPDLSMATNLETLKLSDCSSLVELPSSIQYLNKLEDLDMSRCENLEILPTG
INLKSLYRLNLSGCSRLKSFPDISTNISWLDLDETAIEEFPSNLRLENLDELILCEMKSEKLWERVQPLT
PLMTMLSPSLTRLFLSDIPSLVELPSSIQNLHKLEHLEIENCINLETLPTGINLESLESLDLSGCSRLRT
FPDISTNISDLNLSRTGIEEVPWWIEKFSNLSFLDMNGCNNLQRVSLNISKLKHLETVDFSDCGALTEAS
WNGSPSEVAMATDNIHSKLPSTVCINFINCFNLDQEALLQQQSIFKQLILSGEEVPSYFTHRTTGASLTN
IPLLHISPCQPFFRFRACAVVDSESFFIISVSFDIQVCCRFIDRLGNHFDSPYQPHVFSVTKKGSHLVIF
DCCFPLNEDNAPLAELNYDHVDIQFRLTNKNSQLKLKGCGIRLSEDDSSLNNTLPNVEEADDDNPVNGSE
HWEDCEDSALERESERTKDREMRDRLLKKDLNR
>gnl|CDD|215634 PLN03211, PLN03211, ABC transporter G-25; Provisional
MPVFDGVENQNDGPDRSKPPSQDSRDLPSLLLSSCYPITLKFMDVCYRVKFENMKNKGSNIKRILGHKPK
ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILK
RTGFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGG
ERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVL
SEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANGVCQTDGVSEREKPNVKQSLVASYNTLLAP
KVKAAIEMSHFPQANARFVGSASTKEHRSSDRISISTWFNQFSILLQRSLKERKHESFNTLRVFQVIAAA
LLAGLMWWHSDFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGD
LPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAF
VLTGGFYVHKLPSCMAWIKYISTTFYSYRLLINVQYGEGKRISSLLGCSLPHGSDRASCKFVEEDVAGQI
SPATSVSVLIFMFVGYRLLAYLALRRIKH
>gnl|CDD|178751 PLN03212, PLN03212, Transcription repressor MYB5; Provisional
MMSCGGKKPVSKKTTPCCTKMGMKRGPWTVEEDEILVSFIKKEGEGRWRSLPKRAGLLRCGKSCRLRWMN
YLRPSVKRGGITSDEEDLILRLHRLLGNRWSLIAGRIPGRTDNEIKNYWNTHLRKKLLRQGIDPQTHKPL
DANNIHKPEEEVSGGQKYPIEPISSSHTDDTTVNGGDGDSKNSINVFGGEHGYEDFGFCYDDKFSSFLNS
LINDDADPFGNIIPISQPLQMDDCKDEIVGASSSSLGHD
>gnl|CDD|178752 PLN03213, PLN03213, repressor of silencing 3; Provisional
MEEKSSGGGGVRLHVGGLGESVGRDDLLKIFSPMGTVDAVEFVRTKGRSFAYIDFSPSSTNSLTKLFSTY
NGCVWKGGRLRLEKAKEHYLARLKREWEAASSTSDNTIKAPSDSPPATHLNIFFPRLRKVKAMPLSGTGK
HKYSFQRVPLSSSLPKSFCDCEEHSNNSLTPREIHLHDLEALNVGRNEAEVNVMNSVMNKLFEKNNIDIA
EEDNEIEADQDNLIINVASSGNDMDSALDKLSRKRKSILNEKTPSEEGYSEGRKGNHIHPSKKRQTISLE
ESGRQESSQAIREKKKPSEVVPDKSLDEPSRTKDLEQSIDNISWSQKSSWKSLMANGNSNDFSVSSFLPG
VGSSKAVQPAPRNTDLAELPSRENLKEKTKRKRVTSTIMAEDLPVPDDIKRDDSDTMADDIERDDSAAVE
YYTACESMADDAANDSVAERDDSDAVECDTAIDSMADDTAIDSMADDAASDAVAESDDGDAVENDTAIDS
MADDTASNSMAESDDGDNVEDDTAIDSMADDTANDDVGSDDSESLADTVIDTSVDAVPLDFVANTEGDSG
DGKSNVEKHENGAEDLNAEKESLVVKENVVDEEEAGKEPLKACNKSTGGSSWLQKASWTQLVSDKNTSSF
SITQLFPDLSSDKGEAAGVINNVENQFSNSHKTASAMKQTDYACSSGGFVAAGVPVASTPVRSLDENRHH
LNGKNLSEGAKLGAKKKIIKRKVGSGDTCTFMRSSTSLKEWAKAKKALSEPRRKKNGED
>gnl|CDD|215635 PLN03214, PLN03214, probable enoyl-CoA hydratase/isomerase; Provisional
MPAPSPPGATPGVRVDRRPGGIAVVWLAKEPVNSMTLAMWRSLDDALTALENDPTVRGVVFASGLRRDVF
TAGNDIAELYAPKTSAARYAEFWLTQTTFLVRLLRSRLATVCAIRGACPAGGCAVSLCCDYRLQTTEGTM
GLNEVALGIPVPKFWARLFMGRVIDRKVAESLLLRGRLVRPAEAKQLGLIDEVVPAAALMEAAASAMERA
LKLPSAARAATKALLREEFSAAWEAYYEEEAKGGWKMLSEPSIIKALGGVMERLSSGKEKKQNPAAKL
>gnl|CDD|178754 PLN03215, PLN03215, ascorbic acid mannose pathway regulator 1; Provisional
MADWSTLPEELLHMIAGRLFSNVELKRFRSICRSWRSSVSGVGKKNPFRTRPLILFNPINPSETLTDDRS
YISRPGAFLSRAAFFRVTLSSSPSKGWLIKSDMDVNSGRFHLLNPLSRLPLRHSSESVDLLEFTVSEIRE
AYQVLDWAKRRETRPGYQRSALVKVKEGDNHRDGVLGIGRDGKINYWDGNVLKALKQMGYHFSDIIVHKG
QTYALDSIGIVYWINSDLEFSRFGTSLDENITDGCWTGDRRFVECCGELYIVERLPKESTWKRKADGFEY
SRTVGFKVYKFDDELAKWMEVKTLGDNAFVMATDTCFSVLAHEFYGCLPNSIYFTEDTMPKVFKLDNGNG
SSIETTISESSQSSFEMFVPSFL
>gnl|CDD|178755 PLN03216, PLN03216, actin depolymerizing factor; Provisional
MAFKMATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYA
VFDFDFVTVDNCRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRA
K
>gnl|CDD|178756 PLN03217, PLN03217, transcription factor ATBS1; Provisional
MSGRRSRSRQSSGTSRISEDQINDLIIKLQQLLPELRDSRRSDKVSAARVLQDTCNYIRNLHREVDDLSE
RLSELLANSDTAQAALIRSLLTQ
>gnl|CDD|215636 PLN03218, PLN03218, maturation of RBCL 1; Provisional
MMASASSPLSLSRHSRLLTLPSTIPPILPASTLRRDFLGCSHNLRPPNSASRLRGGKSKSIRSRIRSPRL
VVNASLGSGLVLVVVAVTAFSAISFAYLQHTRRRKSSPLVATPSGGGISTLNREDVQSLDGDVHKGTSTE
INVGFRDLVEEVEHTEEEKTHQAQERALMEEESVVVEGSESSRESVRVVADEHTLSDESASSRVVHGSVA
LLSLSFGVENPELQNGNSPDQTKLELDLSQLVVGRHSIAESLFTQTVLDSLDYDSYEYNGLLQEAAISSG
KGIFAESKREELYTFYEEKQSRAKSSRLPNVKGLRKGVSSATNSLSLDKKNNGVKDAELPGQSSGQAASD
VEEENSLAAYNGGVSGKRKSPEYIDAYNRLLRDGRIKDCIDLLEDMEKRGLLDMDKIYHAKFFKACKKQR
AVKEAFRFAKLIRNPTLSTFNMLMSVCASSQDIDGALRVLRLVQEAGLKADCKLYTTLISTCAKSGKVDA
MFEVFHEMVNAGVEANVHTFGALIDGCARAGQVAKAFGAYGIMRSKNVKPDRVVFNALISACGQSGAVDR
AFDVLAEMKAETHPIDPDHITVGALMKACANAGQVDRAKEVYQMIHEYNIKGTPEVYTIAVNSCSQKGDW
DFALSIYDDMKKKGVKPDEVFFSALVDVAGHAGDLDKAFEILQDARKQGIKLGTVSYSSLMGACSNAKNW
KKALELYEDIKSIKLRPTVSTMNALITALCEGNQLPKALEVLSEMKRLGLCPNTITYSILLVASERKDDA
DVGLDLLSQAKEDGIKPNLVMCRCITGLCLRRFEKACALGEPVVSFDSGRPQIENKWTSWALMVYRETIS
AGTLPTMEVLSQVLGCLQLPHDATLRNRLIENLGISADSQKQSNLSTLVDGFGEYDPRAFSLLEEAASLG
VVPSVSFKKSPIVIDAEELPVFAAEVYLLTILKGLKHRLAAGAKLPNVTILLPTEKKEIYTPKGEKTINL
AGRVGQAVAALLRRLGLPYQGSESHGKLRINGLSLRRWFQPKLKSPFSGKPEDLSSSQSRLGKGIADQQR
AIRLGNLSLE
>gnl|CDD|178758 PLN03219, PLN03219, uncharacterized protein; Provisional
MGLMRSMLPNAKQIFKSQSMRNKNGSSSPSSSTTTSGLVPKGHVAVYVGEQMEKKRFVVPISYLNHPLFR
EFLNRAEEECGFHHSMGGLTIPCREESFLHLITSHQLH
>gnl|CDD|178759 PLN03220, PLN03220, uncharacterized protein; Provisional
MGLSRFAISNATKQILKLNSLANRNRTSSSSSDHVPKGHVAVYVGEQIEMEKKRFVVPISFLNHPSFKEF
LSRAEEEFGFNHPMGGLTIPCREEVFLDLIASRLH
>gnl|CDD|178760 PLN03221, PLN03221, rapid alkalinization factor 23; Provisional
MRGLSRNSGAAAIFAILLILAVHFWSVAVSSQSIEFAGDFPPFETECRGTIAECSVSAALGDDGDLFYGG
GEMGAEFEMDSEINRRILATRRYISYGALRRNTIPCSRRGASYYNCRRGAQANPYSRGCSAITRCRR
>gnl|CDD|178761 PLN03222, PLN03222, rapid alkalinization factor 23-like protein; Provisional
MRGLSTKPGAIIIAILTVHFLFAAVTSQSTGFSGDFMPIDSKCNGTIAECSLSTAEEEFEMDSEINRRIL
ATTKYISYGALRRNTVPCSRRGASYYNCRRGAQANPYSRGCSAITRCRR
>gnl|CDD|215637 PLN03223, PLN03223, Polycystin cation channel protein; Provisional
MSMQKAKAYAVEGLEEGGDDPKTAQDVVHALYAKYKKNYSTRTDYVALFSFLVFVAFYLAILFLQRKAEE
AYSLTSTLTSAIIPGAKTMQSTNEVYNWIDSLVTESWKDPVCGDGRCEAPFEFPEYGRFGCKADCGKLNE
KQNLTKIQIDVYYNFSHPKGSVSPIDLMNDASWNLCPLETDENIGPKKIFHGADCYYEEDQGFERQVGHQ
IRVIDDVPDGEWTIVVKKDIFNKVRGAVRDRTNVTKEATYKRLLVAAHYAQTERKFELDLYNQALSDLSE
DNWTYANSKINAGYLNETEYYAATWVSNATCWCKTVQNEGTAFNSSNATLYALMEGNLAQSVSATEAAMP
FNDTLVDWAYRANGYCCANSPDLMPSTWYGYNFNHSSAWTANFSNTGIASGNVYWTRNLFNVNMMNNTAC
RCWCVAGLDLSFCWRTGLTNATEGTCDKCEKAKELACVETLRWIRRLWDQRLTGKITQRNNVRTDAKADA
DANFPEVKSWLSSESPVTFFEINTVAGTDPIKLRLASLDPLKDDGVINEYNLDPQAAAVNAARRASTVYL
LPLRDRITARRNELQDPQASTPIFPYPAPSNFTFTNITAGDVKYVAALAPGYDLTAPTDLSLVEYNPVVL
LRNDYAFMRCDLEDRAPEYAGQCVAMNNTCEATTAGAIITPVVANPENRTACEEPCLRQFRFQKLCNTIC
ECGRQGCAAGEYCVCEACLKLNQYAYVDYPFVDTSRRKLLQEQAAAAESVASHGHKSHHDRRATRANRRR
LQQTNAAATLTNILTQVGTLSTTQTSLDTQIETLKTQQDRANQEAEAHHADNSLETLINAGFTDIKAGQA
ALEAKLDEILGKQQQALAAAQESLAIQQRTNGLAERQAAAIEKLAKAVEKQLSSIKSAYTYGAFISLTQY
LAIQERARRTRELTAKANFLSNMPCTSKVMYNTFSLDNFQNAVDTTASRERNIGLNNRVIAGMLLYQTRK
NLTACDSSRFDKIDKTCSGGRDISSYGVDPVFKRGTPLYKPDYDNVNTMKVLNVYNCTELSNPTYGISPT
YNTSGIKGETIGPYCKELFNPQGLPYGFRFKPLPGYADGFPYFFDINLSAAEAQTWLDYMIYGLMIDDVK
TRKVTAQVVVYNAELGYFGNVMVFFEFTDGGKIEVTHRLNTIRVELYETYEDWVRFAMEILLAIGAVYSV
YEEAMDFGSSKKTRGSYLAYFLSGWNYVDFASIGLHLATIMMWFVFSWSYARAFEPDIHYDIYKNLSASA
NFTALRIPNELPEMNDMFLEMKNLVDYFQWYMTLSGINIILLLGRILKLMDFQPRLGVITRTLWLAGADL
MHFFVIFGMVFVGYAFIGHVIFGNASVHFSDMTDSINSLFENLLGDITYFNEDLKNLTGLQFVVGMIYFY
SYNIFVFMILFNFLLAIICDAFGEVKANAAETVSVHTELFPMLRDKWRSMFKGWFYKNHIPEARVRRQLR
IWKGENPDEEEEEAFREEKEKVFTYLNKELDEAGLKRVLRRCVIETYQKTDKSKVLLRLRVGNVGKGKKK
ETLATADEIDQAAHMLMDQVGQVPDDEDDDEDGDVLEKEVDQLQQSLERLAEVQRELAEGQVKVIEGQKQ
MAERQSRLSQLENKILGVLEKPPS
>gnl|CDD|178763 PLN03224, PLN03224, probable serine/threonine protein kinase; Provisional
MQAQLPSQGGLRRASAGSQQQATAPSRAAAFKPCSFKCKREGGHMIRPVVSTQATGPELASIADAVQSVV
AAAAAAAPAPLQPAVATIGGDLAALATLSPTLPGIGRLTALYYLLFSKPNPLFNIWDFYVGAPLADGANS
RWSSDDFQLRDKLGGGNFGITFEGLRLQADDQGVTQRSKLTAEQKKRRVVLKRVNMDRQGVRQDFLKTGT
LAKGSAETGMVEAYMCAKIKRNPIAAASCAEYLGYFTSNTADGAFTKGSQWLVWKFESDATLGDALDGKL
GPFPGCLEEFMMAGKKIPDNMPQDKRDINVIKGVMRQVLTGLRKLHRIGIVHRDIKPENLLVTVDGQVKI
IDFGAAVDMCTGINFNPLYGMLDPRYSPPEELVMPQSCPRAPAPAMAALLSPFAWLYGRPDLFDSYTAGV
LLMQMCVPELRPVANIRLFNTELRQYDNDLNRWRMYKGQKYDFSLLDRNKEAGWDLACKLITKRDQANRG
RLSVGQALSHRFFLPEF
>gnl|CDD|215638 PLN03225, PLN03225, Serine/threonine-protein kinase SNT7; Provisional
MATAVAVAGASGSPSRFLGRKLSSRRLSRAPARRSRARALTAAAGGELIDAVHNLFVGVGVGLPCTVMEC
GDVIYRSTLPRSNGLTITAPGAALALLAATYLWATPGVAPGFVDMFVLAPLEGLFRPSFKKDDFVLGKKL
GEGAFGVVYKASLVNKQSKKEGKYVLKKATEYGAVEIWMNERVRRACPNSCADFVYGFLEPVSSKKEDEY
WLVWRYEGESTLADLMQSKEFPYNVEPYLLGKVQDLPKGLERENKIIQTIMRQILFALDGLHSTGIVHRD
VKPQNIIFSEGSGSFKIIDLGAAADLRVGINYIPKEFLLDPRYAAPEQYIMSTQTPSAPSAPVATALSPV
LWQLNLPDRFDIYSAGLIFLQMAFPNLRSDSNLIQFNRQLKRNDYDLVAWRKLVEPRASPDLRRGFEVLD
LDGGAGWELLKSMMRFKGRQRISAKAALAHPYFDREGLLGLSVMQNLRLQLFRATQQDYGEAAAWVVFLM
AKSGTEKEGGFTEAQLQELREKEPKKKGSAQRNALASALRLQRKGVKTVARTVDEIPGGQGAKKSVWWNR
WIPGEE
>gnl|CDD|215639 PLN03226, PLN03226, serine hydroxymethyltransferase; Provisional
EKSMVSVPKWGNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGAR
YYGGNEYIDQIETLCQKRALEAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSH
GYQTDGKKISATSIYFESMPYRLDESTGLIDYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKV
GALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRGGMIFFRKGPKPPKGQGEGAVYDYEDKI
NFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSKGYKLVTGGTDNHLVLWD
LRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEFLHRAVTIA
LKIQKEHGKKLKDFKKGLESNDFSKDIEALRAEVEEFATSFPMPGFDKESMKYKE
>gnl|CDD|178766 PLN03227, PLN03227, serine palmitoyltransferase-like protein; Provisional
LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGAST
TSSTVAAFAKRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQDVALKRKPTDQRR
FLVVEGLYKNTGTLAPLKELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPMVHAEIVTFSLEN
AFGSVGGMTVGSEEVVDHQRLSGSGYCFSASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYSTLTN
SSHPYALKLRNRLVITSDPISPIIYLRLSDQEATRRTDETLILDQIAHHSLSEGVAVVSTGGHVKKFLQL
VPPPCLRVVANASHTREDIDKLLTVLGEAVEAILCKIIDENK
>gnl|CDD|178767 PLN03228, PLN03228, methylthioalkylmalate synthase; Provisional
MASLLLTSSGMITTTGPTVVGRSVLPIGSSLPSLRLTRPYGKPTLFRSCCSSESKKVATSATDLKPIVER
WPEYIPNKLPDKNYVRVLDTTLRDGEQSPGGSLTPPQKLEIARQLAKLRVDIMEVGFPGSSEEEFEAVKT
IAKTVGNEVDEETGYVPVICGIARCKKRDIEAAWEALKYAKRPRILAFTSTSDIHMKYKLKKTKEEVIEM
AVSSIRYAKSLGFHDIQFGCEDGGRSDKEFLCKILGEAIKAGATSVGIADTVGINMPHEFGELVTYVKAN
TPGIDDIVFSVHCHNDLGLATANTIAGICAGARQVEVTINGIGERSGNASLEEVVMALKCRGAYLMNGVY
TGIDTRQIMATSKMVQEYTGMYVQPHKPIVGANCFVHESGIHQDGILKNRSTYEILSPEDIGIVKSQNSG
IVLGKLSGRHAVKDRLKELGYELDDEKLNEVFSRFRDLTKEKKRITDADLKALVVNGDEISSEKLNSKGS
NNLMSSPQISSVV
>gnl|CDD|178768 PLN03229, PLN03229, acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
MASISHSSVAFGGATGASASDLLRSSSNGVNGVPLKTLGRARFSTRRRDLAVVAKIRKGKKHEYPWPADP
DPNVKGGVLSYLSHFKPLKEKPKPVTLDFEKPLVDLEKKIVDVRKMANETGLDFSDQIISLESKYQQALK
DLYTHLTPIQRVNIARHPNRPTFLDHIFNITDKFVELHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGR
NTKENIMRNFGMPTPHGYRKALRMMYYADHHGFPIVTFIDTPGAYADLKSEELGQGEAIAHNLRTMFGLK
VPIVSIVIGEGGSGGALAIGCANKLLMLENAVFYVASPEACAAILWKSAKAAPKAAEKLRITAQELCRLQ
IADGIIPEPLGGAHADPSWTSQQIKIAINENMDELGKMDTEELLKHRMLKFRKIGGFQEGVPVDPERKVN
MKKREAVKTPVRELEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKKEIDLEYTEAVIAMGLQERLEN
LREEFSKANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLK
AEINKKFKEVMDRPEIKEKMEALKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSMGLEVIG
VTKKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEAL
EQQIKQKIAEALNSSELKEKFEELEAELAAARETAAESNGSLKNDDDKEEDSKEDGSRVEVN
>gnl|CDD|178769 PLN03230, PLN03230, acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
MQVGKSKNLVSDRGAAPRAAQKASVVRPAKIVKGKKRLEHEYPWPEKLPQGELTTGALKILNRFKPLKNK
PKPVTLPFEKPIVDLENRIDEVRELANKTGVDFSAQIAELEERYDQVRRELYSRLTPVQRLSVARHPNRP
TFLDHVLNMTDKWVELHGDRAGFDDPAIVCGIGSMEGMSFMFIGHQKGRNTKENIYRNFAMPQPNGYRKA
LRFMRHAEKFGFPILTFVDTPGAYAGIKAEELGQGEAIAFNLREMFGLRVPIIATVIGEGGSGGALAIGC
GNRMLMMENAVYYVASPEACAAILWKSAAAAPKAAEALRITAAELVKLGVVDEIVPEPLGGAHSDPLQAS
KNIKEVILRHMKELMKMDPEELLQDRAAKFRKIGEFDEFGVVDPHIKRNMKKRDAPVEDRERRQLPSGQV
HASKPAPASSN
>gnl|CDD|178770 PLN03231, PLN03231, putative alpha-galactosidase; Provisional
PPRGWNSYDSFSFTISEEQFLENAKIVSETLKPHGYEYVVIDYLWYRKLKHGWFKTSAKSPGYDLIDKWG
RPLPDPKRWPSTTGGKGFAPIAAKVHALGLKLGIHVMRGISTTAVKKKTPILGAFKSNGHAWNAKDIALM
DQACPWMQQCFVGVNTSSEGGKLFIQSLYDQYASWGIDFIKHDCVFGAENPQLDEILTVSKAIRNSGRPM
IYSLSPGDGATPGLAARVAQLVNMYRVTGDDWDDWKYLVKHFDVARDFAAAGLIAIPSVVGGKSWVDLDM
LPFGRLTDPAAAYGPYRNSRLSLEEKKTQMTLWAVAKSPLMFGGDLRRLDNETLSLLTNPTVLEVNSHST
GNRNAQG
>gnl|CDD|215640 PLN03232, PLN03232, ABC transporter C family member; Provisional
MGFEALNWYCKPIAEGFWEKTVDGAFGAYTPCAIDSLVMIVSHSVLLGLCFYRIWIILDNAKAQIYVLRK
KYYNCVLGILACYCVVEPVLRLVMGISLFDMDEETDLPPFEVASLMVEAFAWFSMLVLIGLETKQYVKEF
RWYVRFGVVYVLVADAVLLDLVLPLKNSINRTALYLCISSRCCQALFGILLLVYIPELDPYPGYHILNNE
SLDNVEYDALRGGENICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCW
TEESRRPKPWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDPAWVGYVYAFLIFFG
VTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHG
LWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMD
TVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFTS
LSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFSWDSKTSK
PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENIL
FGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA
LDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENA
GKMDATQEVNTNDENILKLGPTVTIDVSERNLGSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGG
LWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLH
AAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVST
ISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMD
NNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAGFASTMGLLLSYTLNITTLLSGVL
RQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVS
PSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI
DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATA
SVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS
TGPANAQYLSNLVFERRENGMSLGG
>gnl|CDD|178772 PLN03233, PLN03233, putative glutamate-tRNA ligase; Provisional
MNALEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDL
GKIEIKPDSVSFTSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMFKEM
CSGKEEGGAWCLRAKIDMQSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRT
TEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGI
DIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIDKADHTALTVTNADEEADFAFSETDC
HPKDPGFGKRAMRICDEVLLEKADTEDIQLGEDIVLLRWGVIEISKIDGDLEGHFIPDGDFKAAKKKISW
IADVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETDVIGDAGLKTLKEHDIIQLERRGFYRVD
RPYMGEEKPLILFMIPDGKKKAMSGLDGKLAHR
>gnl|CDD|178773 PLN03234, PLN03234, cytochrome P450 83B1; Provisional
MDLFLIIAALVAAAAFFFLRSTTKKSLRLPPGPKGLPIIGNLHQMEKFNPQHFLFRLSKLYGPIFTMKIG
GRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGFGQYTAYYREMRKMCMVNLFSPNRVA
SFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEMKRFIDILYETQAL
LGTLFFSDLFPYFGFLDNLTGLSARLKKAFKELDTYLQELLDETLDPNRPKQETESFIDLLMQIYKDQPF
SIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYL
KAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDNPNEFIPERFMKEHK
GVDFKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLPKGIKPEDIKMDVMTGLAMHKKEH
LVLAPTKHI
>gnl|CDD|178774 PLN03236, PLN03236, 4-alpha-glucanotransferase; Provisional
MSALRDGADTPEAAAAAKACPLDDDPRTETPARVLGDRAAATERRIIHRDGHFRHGGAWKGSGMALPVFS
LRSAESVGAGDFGDLEALVDFAAEAGMSVVQLLPVNDTCVHGTFWDSYPYSSLSVHALHPLYLKLKELVE
EAANAAAAGPDAGRLAALAAEIDAAKHALDLKEIDYEATMKEKLMFAKRAFEADGAKFLASDACERFVKA
NASWLKPYAVFCALRDLFGTAEHWRWGDLFATFAAAILAKIDCPGGDLYESTRFFFYLQYHLDRQLRRAA
AHAAAKGVILKGDLPIGVDKASVDTWMHPKLFRMDTSTGAPPDAFDANGQNWGFPTYDWEEMAEDDYAWW
RARMQHLEQFFSAIRIDHILGFFRIWELPAHAKTGRLGRFRPSLPIRKDELAARGLWDLDRLCEPWIQSE
ELEALFGDNDGEAAGRFFEETDAETKPDGTTRGLWKFRKEFDTEQAIFASEALKPRDDFPDHLNDEQEEL
RAGLMQLFQNRCLLRDPDDADAFYPRFEFEETTSFQALDDWARDALRDLSDDYFFARQDATWRENARKTL
PALLKCTEMLVCGEDLGFTPMCVPPVLDELGILGLRIQRMPHDGESGEFGRPERYPYETVCSPSCHDTMT
TRAWWEADAARRARYAELFQAGNDDACEPHVMRAILRQHIASPSSIAIFPAQDLLALDEEYAKRPAEEET
INDPTNPKHYWRFRIHVACEDLLANAAFLGEIKDLVREGGQMPMT
>gnl|CDD|215641 PLN03237, PLN03237, DNA topoisomerase 2; Provisional
MAEKLPLQESNSANVAAAPAASSGGKTIEEMYQKKSQLEHILLRPDTYIGSIEKHTQTLWVYETDKMVQR
SVTYVPGLYKIFDEILVNAADNKQRDPKMDSLRVVIDVEQNLISVYNNGDGVPVEIHQEEGVYVPEMIFG
HLLTSSNYDDNEKKTTGGRNGYGAKLTNIFSTEFVIETADGKRQKKYKQVFSNNMGKKSEPVITKCKKSE
NWTKVTFKPDLAKFNMTHLEDDVVALMKKRVVDIAGCLGKTVKVELNGKRIPVKSFSDYVDLYLESANKS
RPENLPRIYEKVNDRWEVCVSLSEGQFQQVSFVNSIATIKGGTHVDYVTNQIANHVMEAVNKKNKNANIK
AHNVKNHLWVFVNALIDNPAFDSQTKETLTLRQSSFGSKCELSEDFLKKVMKSGIVENLLSWADFKQSKE
LKKTDGAKTTRVTGIPKLEDANEAGGKNSEKCTLILTEGDSAKALAVAGLSVVGRNYYGVFPLRGKLLNV
REASHKQIMNNAEIENIKQILGLQHGKQYESVKSLRYGHLMIMTDQDHDGSHIKGLLINFIHSFWPSLLK
VPSFLVEFITPIVKATRRGKKVLSFYSMPEYEEWKESLGGNATGWSIKYYKGLGTSTAKEGKEYFKNLGK
HKKDFVWEDEQDGDAIELAFSKKKIEARKNWLRQYEPGTHLDQTQKDVKYSDFVNKELILFSMADLQRSI
PSMVDGLKPGQRKILFCSFKRNFVKEAKVAQLSGYVSEHSAYHHGEQSLASTIIGMAQDFVGSNNINLLL
PNGQFGTRLQGGKDHASARYIFTRLSPITRFLFPKDDDILLDYLNEDGQSIEPTWYMPIIPTVLVNGAEG
IGTGWSTFIPNYNPRDIVANIRRLLNGESMEPMHPWYRGFKGTIEKTASKEGGCTYTITGLYEEVDETTL
RITELPIRRWTDDYKEFLESLKTDNNKNKDPFIKDVKAYNDDTTVHFEVILSEENMLAAKQEGLLKKFKL
TTTISTSNMHLFDSKGVIKKYDTPEQILEEFFHLRLEYYEKRKEVLLKNLEFELLKLENKVRFILAVVDG
EIIVNNRKKADLVEELRQKGFTPFPKKAKSVEAAVAGATDDAAEEEEEIDVSSSSGVRGSDYDYLLSMAI
GTLTLEKVQELCADRDKLNIEVEDLKKTTPKSLWLKDLDALEKELDKLDKEDAKAEEAREKLQRAAARGE
SGAAKKVSRQAPKKPAPKKTTKKASESETTEETYGSSAMETENVAEVVKPKGRAGAKKKAPAAAKEKEEE
DEILDLKDRLAAYNLDSAPAQSAKMEETVKAVPARRAAARKKPLASVSVISDSDDDDDDFAVEVSLAERL
KKKGGRKPAAANKKAAKPPAAAKKRGPATVQSGQKLLTEMLKPAEAIGISPEKKVRKMRASPFNKKSGSV
LGRAATNKETESSENVSGSSSSEKDEIDVSAKPRPQRANRKQTTYVLSDSESESADDSDFDDDED
>gnl|CDD|215642 PLN03238, PLN03238, probable histone acetyltransferase MYST; Provisional
DPVLAELEREHEETTKVKNIEMIELGKYEMDTWYYSPYPEPYASCTKLYICEYCLKYMRKKKSLLRHLAK
CDIRQPPGGGIYGAVTEGPLSVFEVDGKKAKVYCQNLCLLAKLFLDHKTLYYDVDPFLFYVMTEVDDHGS
HIVGYFSKEKVSAEDYNLACILTLPPYQRKGYGKFLISFAYELSKREGKVGTPERPLSDLGKVSFRSYWT
RVLLEQLRDVKGDVSIKDLSLATGIRGEDIVSTLQSLNLIKYWKGQHVIHVDQRVLDEHWAKFAHQRVIE
VDCLHWQPLP
>gnl|CDD|178777 PLN03239, PLN03239, histone acetyltransferase; Provisional
YYVHYKDFNRRMDEWISKDKSNEEILALPSDHLATHTVGEDVVATIAAPELDEHEGLDDAALKEHEEVTK
VKNVAFLELGPYQMDTWYFSPLPKELFKAGGFIDVLYVCEFSFGFFARKSELLRFQAKELPKERRHPPGN
EIYRCGDLAMFEVDGFEERIYCQNLCYIAKLFLDHKTLYFDVDPFLFYVLCEVDERGFHPVGYYSKEKYS
DVGYNLACILTFPAHQRKGYGRFLIAFSYELSKKEEKVGSPEKPMSDLGQQAYIPYWGSTIVDFLLNHSG
NDSSLSIMDIAKKTSIMAEDIVFALNQLGILKFINGIYFIAAEKGLLEELAEKHPVKEPRVDPSKLHWTP
F
>gnl|CDD|178778 PLN03240, PLN03240, putative Low-temperature-induced protein; Provisional
MDSQAQLQRPHGHHQAEEPIRIHHPEEEGHHEKGPSKVLKKVKEKAKKIKNVLTKHGHGHEHDRGEHIPD
DHDLDQEDDEDDYNDNQLHGGAPARGKAHIPVKEEIVPPGSKAFPVVSSSHTKHSEPIRGVGHEAMSHPI
KHSGVPDKEERRGAATLTPHNTPVSLLSATEDVTRTFVPDEDKSRDQRKVNIDRPKGLDQDPAAPGSHGG
LSNDQSKVTDPIGKSTGEIGAASTVSAIGRLGLGTDLQKKSHGLDTKPAAPGSHGGMSNYQSKVTDHAGK
EAGEQPRVAAFGRRNETGEDDHMGLGRDLGEKSHGFDTKSRPEMGKHIPAGDYGSRLGKESPERSDEFDL
GKDLLTRTQGIQKPAGFDSKGQERGDEMHQPNQSSYTDKIALATSVVADKAVAAKNAVASKLGYSGEAGH
ENRVEGAENPSSAGGYGSTVAGMVTPVYEKVKETGASVMTKLPFSGTGTEQGQDKGVSAKEFLTEKLSPG
EEDKALSEVVAEKLHLGGGGGETAPPKKGIVTQSEEVEKRLGGFKDPSSEAATKHGEAYAEEGEGGIAEK
LRGAVTSWIAGTTEEVTQKSTESVQDSTQSLGSTIGNKMGISGSGGEEAGNGGSMPLQKRFQESGK
>gnl|CDD|215643 PLN03241, PLN03241, magnesium chelatase subunit H; Provisional
CGNVVDGLVPVQTASTRTLLGSRRSARRPAGSRPCHAAPTFAALAAVAEADEDSAGSPQPKKHNTARTRR
IVLVSGFESFNVGLYKQAARLLKRRCPNVDLVVFSDRDIESDRERFAAALDGADVFFGSLLFDYDQVEWL
RARLEKVPPRLVFESALELMSCNSVGSFSMKAAPGGKKAGPPPAVKAVLSKFGSGKEEDKLVGYLSFLKI
GPALLKFVPGEKASDLRNWLTVYRYWNQGGKENVEEAFAYIADQYLAPPSTVTPPSYAPPPLVETPALGL
YHPDRERQQAPYFESPAEYLEWYARQGAFVLAPADAPRVAILLYRKHVITKQPYLADLVRQMEESGVLPV
PIFINGVEAHTIVRDLLTSVHEQDLRARGELGRDSTYLKSDAVVVDAVVSTIGFPLVGGPAGSMEAGRQA
EVAQTILGAKNVPYVVAAPLLIQDIASWKRSGVGGLQSVVLYSLPELDGAIDTVPLGGLVGDDIYLVPER
VRKLANRLKSWVSLRKTPPSERKVAVMLYGFPPGVGATGTAALLNVPKSLENLLRRLRDEGYDLGDSGTD
PNPSGESLVAALRTLEENPVIAGGATRMQTAIEHPRTRAHDGDATVRHTLAPPLGGAQVVGKDISIDHLE
EMLGDVLVKKMERAWGELERYPGLNTPGKGSFDGYGADAVIHFGMHGTVEWLPGQPLGNDRLSWSDELLG
GLPNVYVYAANNPSESIVAKRRGYGTIVSHNVPPYGRAGLYLQLANLKELLNEYREDEETNSAALRESIF
DLVTRAGLDSDCPLVDASSSEGSRITSESVELRSLSAEVFDDYASRLYAYLGVLENRLFSEGLHVLGAAP
TDEQLGSYLAAYNCPTSSQTQEAVEIRDLLSRNTEELSGVLKALGGEYVPPAPGGDLLRDGPGVLPTGRN
IHALDPYRMPSAAAWARGARVAAAIIEQHRAANDGAYPETVAVNLWGLDAIKTKGESVAIVLALVGARPV
KEGTGRVVRYELIPLSELGRPRVDVLCNMSGIFRDSFANVVDLLDDLFARAADADESDEMNFIKKHAREM
EAEGVDNTAARLFSNPPGDYGSMVNERVGTGDWEDSRELGDTWAGRNAYSYGRGDERGTARPEVLQKLLK
TTERVVQEIDSVEYGLTDIQEYYANTGALKAAAEAAKEIDGPTGKKKKVACSVVEAFGGAGGNDDVPPKD
LEEVLRLEYRSKLLNPKWADAMAQQGSGGAYEISQRMTALVGWGATSGFAENWVFDGAAERYVLDEEMAS
KLRKANPQAFRNVVRRMLEAAGRGMWSADEETLAKLKSLYSDADDELEGVQTFRA
>gnl|CDD|178780 PLN03242, PLN03242, diacylglycerol o-acyltransferase; Provisional
YRPSLPAHRRSKESPLSSDAIFTQSHAGLFNLCIVVLVASNSRLIIENIMKYGFLIQAEVLFSSKSLKDW
PLVMCGLSLLAFPLAAYVIEKMLARRYFPATFVMPLHLINLAAALLYPIYVIWMLISDPLSGAVLMLIAT
ITWLKLVSYAHTNADYRASKKDGGKIELPSDAPNIDYPQNVTLKNIAYFMAAPTLCYQISYPRSPRIRTG
WVLRQLGKLIVFNGFMGFIIAQYVNPILRNSVHPLKGNYLYAIERVLKLSIPNLYVWLLMFYCFFHLWLN
IVAELLCFGDREFYKDWWNASEVSEYWRLWNMPVHYWLVRHVYFPCLRLGMPKQLAILVVFFISAVFHEV
CIAVPCHMIRGWAFLGIMFQVPLVLVTKVLQRKFPSSMVGNMIFWFFFCIVGQPMCVLLY
>gnl|CDD|215644 PLN03243, PLN03243, haloacid dehalogenase-like hydrolase; Provisional
PRDRADDLSLNNPLLRQHRLGCGWLGVVLEWEGVIVEDDSELERKAWRALAEEEGKRPPPAFLLKRAEGM
KNEQAISEVLCWSRDFLQMKRLAIRKEDLYEYMQGGLYRLRPGSREFVQALKKHEIPIAVASTRPRRYLE
RAIEAVGMEGFFSVVLAAEDVYRGKPDPEMFMYAAERLGFIPERCIVFGNSNSSVEAAHDGCMKCVAVAG
KHPVYELSAGDLVVRRLDDLSVVDLKNLSDLDSPEFQIPEPQLEEEVEEE
>gnl|CDD|178782 PLN03244, PLN03244, alpha-amylase; Provisional
MTSLSLPTQFSCHPNASNLPFSEKNRLAINGVNFPKKKIKLKIRCFAAEQPQQEKQKKKSQSKPQADADA
GIDPVGFLTKLGIADKIFAQFLRERHKALKDLKDEIFKRHFDFQDFASGFEILGMHRHMEHRVDFMDWAP
GARYCAIIGDFNGWSPTENAAREGHFGHDDYGYWFIILEDKLREGEEPDELYFQQYNYVDDNDKGDSGVS
AEEIFKKANDEYWEPGEDRFIKNRFEVAAKLYEQIFGPNGPETEEELEDIPDAETRYKAWKEEHKDDPPS
NLPPCDIIDKGQGKEYDIFNVVDDPEWREKFRAKEPPIAYWLESRKGRKAWLKKYIPAIPHGSKYRLYFN
TPDGPLERIPAWATYVLPDDDGKQAFAIHWEPPPEAAHKWKNMKPKVPESLRIYECHVGISGSEPKISSF
EEFTEKVTNFFAASSRYGTPDDFKRLVDEAHGLGLLVFLDIVHSYAAADEMVGLSLFDGSNDCYFHTGKR
GHHKHWGTRMFKYGDLDVLHFLISNLNWWITEYQIDGFQFHSLASMIYTHNGFASFNGDLDDYCNQYVDK
DALMYLILANEILHALHPKIITIAEDATYYPGLCEPTSQGGLGFDYYVNLSAPDMWLDFLDNIPDHEWSM
SKIVSTLIANKEYADKMLSYAENHNQSISGGRSFAEILFGAIDEDPLGGKELLDRGCSLHKMIRLITFTI
GGHAYLNFMGNEFGHPERIEFPMPSNNFSFSLANRCWDLLENEVHHHLFSFDKDLMDLDENEGILSRGLP
NIHHVKDAAMVISFMRGPFLFIFNFHPSNSYEGYDVGVEEAGEYQIILNSDETKYGGQGIIEEDHYLQRS
INKRIDGLRNCLEVFLPSRTAQVYKLSRILRI
>gnl|CDD|215645 PLN03246, PLN03246, 26S proteasome regulatory subunit; Provisional
SPRGIEKVVVHPLVLLSIVDHYNRVAKDTRKRVVGVLLGSSFRGRVDVTNSFAVPFEEDDKDPSIWFLDH
NYLESMFGMFKRINAKEHVVGWYSTGPKLRENDLDIHELFNDYVPNPVLVIIDVQPKELGIPTKAYYAVE
EVKENATQKSQKVFVHVPSEIGAHEAEEIGVEHLLRDVKDTTVSTLATEVTGKLTALKGLDARLREIRSY
LDLVVEGKLPLNHEILYHLQDVFNLLPNLNVEELVKAFAVKTNDMMLVIYLSSLIRSVIALHNLINNKIL
NKEHEKAEDAKPAAKPAKKGSGK
>gnl|CDD|234568 PRK00006, fabZ, 3-hydroxyacyl-ACP dehydratase FabZ
TTETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMA
QAAGVLALKSEENKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAEL
MFAIRDK
>gnl|CDD|234570 PRK00009, PRK00009, phosphoenolpyruvate carboxylase; Reviewed
EMNEKDAPLREDVRLLGRLLGDTIREQEGDEVFDLVETIRKLSKSSRRGDDAAREELLKLLKNLSNDELL
PVARAFSQFLNLANIAEDYHHIRRRREHASGSQPQPGSLAETLRRLKAAGVSPEELARALEELDIEPVLT
AHPTEVQRRTLLDKQREIAALLRQLDDVDLTPRERAKIERRLRRLIAQLWQTDEIRQFRPTVVDEIKNGL
AYYENSLWQAVPKLYRELEEALEEHFGLQLPLDAAPLRFGSWIGGDRDGNPNVTAEVTREVLLLQRWVAL
DLYLKELHALGSELSMSTRLVEVSPELRALAGASPDQSPHRRDEPYRRALKGIRARLAATADWLEARLAG
EEAPPPADPYASAEELLADLDLIYQSLRACGMGILANGRLLDLLRRVEVFGFHLARLDIRQESSRHEDAV
AELTRYLGLGDYASLSEAEKQAFLLRELNSRRPLIPPNWEYSELTSKELAEFLAARRLIAEFGAEAIGAY
IISMAETVSDVLEVLLLLKEAGLLDPAAARAPLPVVPLFETIEDLRNAADVMRQLLSLPWYRGLIAGRGN
LQEVMLGYSDSNKDGGFLASNWALYRAQEALVELAEKHGVRLTLFHGRGGTVGRGGGPAYAAILSQPPGS
VKGRIRVTEQGEVIRSKYGLPEVARRNLELLTAATLEASLLPPPEPKPEWREIMDELSDRSCKAYRGLVR
ENPDFVDYFRAATPIQEIGKLNIGSRPASRKPTGGIESLRAIPWVFSWSQNRLMLPGWYGVGSALQAAID
DEPPGRLALLREMYQDWPFFRTLLSNLEMVLAKADLNIAERYAQLLVDKELRPRLFERIRDELELTIKVV
LAITGQDELLADNPWLARSIRLRNPYLDPLNHLQVELLKRLRAQEGDPDEEVERAIHLTINGIAAGLRNT
G
>gnl|CDD|178791 PRK00010, rplE, 50S ribosomal protein L5; Validated
MPRLKEKYKEEIVPALMKEFGYKNVMQVPKLEKIVLNMGVGEAVADKKLLENAVEDLTLITGQKPVVTKA
KKSIAGFKLREGMPIGCKVTLRGERMYEFLDRLINIALPRVRDFRGLSPKSFDGRGNYTLGIKEQIIFPE
IDYDKIDKIRGMDITIVTTAKTDEEARALLKAFGFPFRK
>gnl|CDD|234571 PRK00011, glyA, serine hydroxymethyltransferase; Reviewed
FFMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVD
VVEQLAIDRAKELFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNV
VSYGVDEETGLIDYDEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAG
VHPSPVPHADVVTTTTHKTLRGPRGGLILTNDEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPE
FKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDP
RSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKEEVKELCKRFPLYKYL
>gnl|CDD|234573 PRK00013, groEL, chaperonin GroEL; Reviewed
MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGA
QLVKEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDK
EEIAQVATISANGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKM
EAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGF
GDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKA
QIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGIVPGGGVALLR
AAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKGYGYNAATGEYVDMIE
AGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAAPPMGGGGMGGM
>gnl|CDD|234574 PRK00015, rnhB, ribonuclease HII; Validated
RLEPMLSFERALLKQGLGLIAGVDEAGRGPLAGPVVAAAVILDPDRPIEGLNDSKKLSEKKREELYEEIK
EKALAYSVGIASPEEIDELNILEATLLAMRRAVEGLVKPDYVLVDGNRVPKLPIPQEAIVKGDAKSPSIA
AASILAKVTRDRLMEELDKEYPGYGFAKHKGYGTKEHLEALAKYGPTPIHRRSFAPV
>gnl|CDD|234576 PRK00019, rpmE, 50S ribosomal protein L31; Reviewed
MKKDIHPKYEEVTVTCSCGNVFETRSTLGKDEINVDVCSKCHPFYTGKQKIVDTGGRVERFNKRFGKKGK
KK
>gnl|CDD|234577 PRK00021, truA, tRNA pseudouridine(38-40) synthase TruA
MMRIALTIEYDGTNFHGWQRQPNGRTVQGELEKALSKLAGEPVRVIGAGRTDAGVHALGQVAHFDTPAPR
PPEKWRRALNALLPDDIAVLWAEEVPDDFHARFSAKARRYRYRIYNRPARPPFLRGYVWHYPYPLDVDAM
NEAAQYLLGEHDFTSFRASGCQSKSPVRTIYEADVTREGDFIVFDISANGFLHNMVRNIVGTLLEVGKGK
RPPEDIKELLEAKDRTLAGPTAPAEGLYLVEVDY
>gnl|CDD|178801 PRK00024, PRK00024, DNA repair protein RadC
MRIKDWPEEERPRERLLKYGAAALSDAELLAILLRTGTKGKSVLDLARELLQRFGSLRGLLDASLEELQS
IKGIGPAKAAQLKAALELARRILAERLREREVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADE
ELFIGTLNSSIVHPREIVKRALKLNAAALILAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIII
GDGEYVSFAERGLL
>gnl|CDD|234581 PRK00026, trmD, tRNA (guanine-N(1)-)-methyltransferase; Reviewed
MRIDVLTLFPEMFPGPLEYSILGRALEKGLLELEVHNPRDFTTDKHRTVDDTPYGGGAGMVMKPEPLFDA
IDAAKAAAGEKAKVILLSPQGKPFTQADARELAKEEHLILLCGRYEGIDERVIEHYVDEEISIGDYVLTG
GELAAMVLIDAVVRLLPGVLGNEESAEEDSFSDGLLEYPHYTRPAEFRGMKVPEVLLSGNHAKIARWRRK
QSLERTKLRRPDLLEKLALTKEDKKLLAELKKEL
>gnl|CDD|234583 PRK00029, PRK00029, YdiU family protein
TMNPLLALPFDNRFARLGPAFYTRVAPTPFPAPRLRFRNDELAALLGLDPEELDDPEFAEVFGGNALLPG
MEPLAMVYHGHQFGVYNPQLGDGRGILLGEVRDADGRLYDLQLKGAGRTPYSRMGDGRAVLRSSIREYLA
SEAMHALGIPTTRALSLVETGEPVYRESPERGAVLTRVAPSHIRFGTFERFAYRGDPELLRQLADYVIAR
HYPELADAEDPYLALFAEVVERTARLIAQWQAVGFVHGVMNTDNMSILGETIDYGPYGFLDDYDPGFTCN
HSDHQGRYAFGNQPAIALWNLARLAQALLPLIAVEALQAALDRFGDAYQAAYRARMRAKLGLFTEEEEDN
ALLNALLALMARSRADYTLTFRRLSLAEDASAASPLRDLFIDRAAFDAWLARYRARLAQEPVSDAERQQA
MRAVNPKYVLRNYLAEQAIEAAEEGDWSELERLLEVLRRPYDEQPEFEAYAARPPDWGKHLEVSCSS
>gnl|CDD|178807 PRK00031, lolA, outer membrane lipoprotein chaperone LolA
AAALLASLVAASAWADAASELKARLSKVKSFSADFTQTVTSGSGKVVQEGSGTLWVKRPNLFRWHYTKPD
EQLIVSDGKTLWIYDPDLEQVTITWLKDATGNTPFALLTRNNSSDWKQYDVKQKGDTFTLTPKAKDTNFK
QFTIGFRNGTLASFSLVDQDGQRTLITFSNIQKNPALDADKFTFTPPKGVDVDDQ
>gnl|CDD|178809 PRK00033, clpS, ATP-dependent Clp protease adaptor protein ClpS; Reviewed
MGKTNDWDDMSALVLEKVEPKLKPPPMYKVLLHNDDYTPMEFVVYVLQKFFGYDRERATQIMLEVHNEGK
AVVGVCTREVAETKVEQVHQHGLLCTMEKD
>gnl|CDD|178810 PRK00034, gatC, Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC
MAITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEVDTEGVEPTTHPLDMKNVLREDVVTES
LPREEALKNAPESEDGYFKVPKVIE
>gnl|CDD|234585 PRK00035, hemH, ferrochelatase; Reviewed
MAMPKDAVLLLNLGGPETPEDVRPFLKNFLSDRRVIDLPRPLWQPLLAGIILPERLPKVAKHYASIGGGS
PLNVITRRQAEALQAELAARGPDLPVYLGMRYWNPSIEEALEALKADGVDRIVVLPLYPQYSYSTTASYF
EDLARALAKLRLQPEIRFIRSYYDHPGYIEALAESIREALAKHGEDPEPDRLLFSAHGLPQRYIDKGDPY
QQQCEETARLLAEALGLPDEDYDLTYQSRFGPEPWLEPYTDDTLEELAEKGVKKVVVVPPGFVSDHLETL
EEIDIEYREIAEEAGGEEFRRIPCLNDSPEFIEALADLVRENLQGWPPRLLGG
>gnl|CDD|134052 PRK00038, rnpA, ribonuclease P protein component
MPRATLPAEARLHRPSEFAAALKGRRLARGAFFIVSASPCAPADDQPARARLGLVIAKRFAARAVTRNTL
KRVIREAFRARRLALPAQDYVVRLHSKLTPASLTALKRSARAEVDAHFTRIAR
>gnl|CDD|234587 PRK00039, ruvC, Holliday junction resolvase; Reviewed
MMRILGIDPGLRRTGYGVIEVEGRRLSYVASGVIRTPSDLDLPERLKQIYDGLSELIDEYQPDEVAIEEV
FFNKNPQSALKLGQARGVAILAAAQRGLPVAEYTPLQVKKAVVGYGRADKEQVQHMVKRLLNLPEIPKPD
DAADALAIAICHAHRRQSLARRRG
>gnl|CDD|234589 PRK00042, tpiA, triosephosphate isomerase; Provisional
RKPIIAGNWKMNKTLAEAKALVEELKAALPDADGVEVAVAPPFTALASVKEALKGSNIKLGAQNVHPEDS
GAFTGEISAEMLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEE
VVARQLEAALAGLSAEQFANLVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGEVAEKVRILYGG
SVKPDNAAELMAQPDIDGALVGGASLKAEDFLAIVKAAAA
>gnl|CDD|234590 PRK00043, thiE, thiamine phosphate synthase
MMMMKLLRLYLITDSRDDSGRDLLEVVEAALEGGVTLVQLREKGLDTRERLELARALKELCRRYGVPLIV
NDRVDLALAVGADGVHLGQDDLPVADARALLGPDAIIGLSTHTLEEAAAALAAGADYVGVGPIFPTPTKK
DAKAPQGLEGLREIRAAVGDIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRA
AR
>gnl|CDD|234591 PRK00044, psd, phosphatidylserine decarboxylase; Reviewed
MLDRLKILLQYLLPKHLLTRLAGWLASSRAGWLTTAVIRLFIKKYKVDMSEAQKPDPAAYKTFNDFFTRA
LKDGARPIDEDPNALVSPADGAISQLGPIEDGQIFQAKGHSYSLEALLGGDAALADPFRNGSFATIYLSP
RDYHRVHMPCDGTLREMIYVPGDLFSVNPLTARNVPNLFARNERVVCLFDTEFGPMAQVLVGATIVGSIE
TVWAGTVTPPREGIIKRWDYPEAGDGAITLKKGAEMGRFKLGSTVINLFPPGKVQLAEQLQAGSVVRMGQ
PLAHITET
>gnl|CDD|234592 PRK00045, hemA, glutamyl-tRNA reductase; Reviewed
MSLLAVGLNHKTAPVELREKLAFSEDELEEALESLLASPSVLEAVILSTCNRTEIYAVVDQFHAGREAII
RWLAEYHGLDLEELRPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYALAQEAGTVGTILNR
LFQKAFSVAKRVRTETGIGAGAVSVASAAVELAKQIFGDLSGKKVLVIGAGEMGELVAKHLAEKGVRKIT
VANRTLERAEELAEEFGGEAIPLDELPEALAEADIVISSTGAPHPIIGKGMVERALKARRHRPLLLVDLA
VPRDIEPEVGELPGVYLYDVDDLQEIVEENLAQRQEAAEKAEAIVEEEVAEFMEWLRSLEVVPTIRALRE
QAEEIREEELERALKKLGPGEDEEEVLEKLARSLVNKLLHAPTVRLKEAAEEGDDEYLEALRELFGLDPE
SVE
>gnl|CDD|234593 PRK00046, murB, UDP-N-acetylmuramate dehydrogenase
MQLQMNHSLKPLNTFGIDARARHLVEAESEEQLLEALADARAAGLPVLVLGGGSNVLFTEDFDGTVLLNR
IKGIEVLSEDDDAWYLHVGAGENWHDLVLWTLQQGMPGLENLALIPGTVGAAPIQNIGAYGVELKDVCDY
VEALDLATGEFVRLSAAECRFGYRDSIFKHEYPDRYAITAVGFRLPKQWQPVLDYGDLARLDPDTVTAQD
VFDAVCAIRRSKLPDPKVLGNAGSFFKNPVVSAEQFEALLAQYPDIPHYPQADGSVKLAAGWLIDQCGLK
GFQIGGAAVHEKQALVLVNYGNATGADVLALARHIQQDVREKFGVELEPEPRFI
>gnl|CDD|234594 PRK00047, glpK, glycerol kinase GlpK
MMMKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGI
SPDQIAAIGITNQRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGT
KIKWILDNVEGARERAEKGELLFGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDI
PRSMLPEVRPSSEVYGKTNPYGFFGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKA
VKSENGLLTTIAWGIDGKVVYALEGSIFVAGSAIQWLRDGLKIISDASDSEALARKVEDNDGVYVVPAFT
GLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLM
QFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDEEEREKLYAGWKKA
VKRTLAWA
>gnl|CDD|234596 PRK00049, PRK00049, elongation factor Tu; Reviewed
MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEY
ETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDM
VDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAID
KPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGAL
LRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGV
EMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE
>gnl|CDD|234598 PRK00051, hisI, phosphoribosyl-AMP cyclohydrolase; Reviewed
PKILDRLKFDADGLVPAIAQDAETGEVLMVAWMNEEALAKTLETGRAHYWSRSRQKLWRKGETSGHVQKV
HEVRLDCDGDAVLLKVEQVGAACHTGRRSCFYRKLEGGLWVTVDPVLFDPDEVYK
>gnl|CDD|234599 PRK00052, PRK00052, prolipoprotein diacylglyceryl transferase; Reviewed
LMMLIFPSIDPVAFSLGPLAIRWYGLMYLLGILLAYWLARRRAKRRGLSGWTPDQLDDLLFWAVLGVILG
ARLGYVLFYNPPYYLAHPLEIFKIWEGGMSFHGGLIGGILAMLLFCRKKKLSFLQLLDFIAPAVPIGQAI
GRIGNFINGELYGRPTDLPWGMIFPGSGPEDPRHPSQLYESLLEGLVLFILLWLFSRKRKKLLKPGAVFG
LYLIGYGLGRFFIEFFREPDAQLGGGLTMGQILSIPMILLGIILLIWAYRKKRRKPKYP
>gnl|CDD|234600 PRK00053, alr, alanine racemase; Reviewed
MRPATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELR
EAGITAPILILGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEA
EAALERLLACPNVRLEGIFSHFATADEPDNSYTEQQLNRFEAALAGLPGKGKPLRHLANSAAILRWPDLH
FDWVRPGIALYGLSPSGEPLGLDFGLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYA
DGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPDPQDKVGDEVTLWGEALTAEDVAEIIGTINYEL
LCKLSPRVPRVYV
>gnl|CDD|234601 PRK00054, PRK00054, dihydroorotate dehydrogenase electron transfer subunit; Reviewed
MMKPENMKIVENKEIAPNIYTLVLDGEKVFDMKPGQFVMVWVPGVEPLLERPISISDIDKNEITILYRKV
GEGTKKLSKLKEGDELDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTK
DEVIFEEEFAKVGDVYVTTDDGSYGFKGFVTDVLDELDSEYDAIYSCGPEIMMKKVVEILKEKKVPAYVS
LERRMKCGIGACGACVCDTETGGKRVCKDGPVFSGGELVL
>gnl|CDD|234602 PRK00055, PRK00055, ribonuclease Z; Reviewed
MMELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGL
PGLLSTRSLSGRTEPLTIYGPKGIKEFVETLLRASGSLGYRIAEKDKPGKLDAEKLKALGVPPGPLFGKL
KRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKEYGH
STARQAAEIAKEAGVKRLILTHFSPRYTGDPEELLKEAREIFPNTELAEDLMRVEVPFRR
>gnl|CDD|234605 PRK00059, prsA, peptidylprolyl isomerase; Provisional
MKSIKKLVASLLVGVFIFSAVGCNMIEKTPEAIAKSTVATVNGEKITRGDLDKDPKMQQVLEQLKQQYGD
NYEKNEQVKEQIKQQKEQILDSLITEKVLLQKAKELKLIPSEEELNKEVDKKINEIKKQFNNDEEQFEEA
LKATGFTEETFKEYLKNQIIIEKVINEVVKDVKVTDKDAQKYYNENKSKFTEKPNTMHLAHILVKTEDEA
KKVKKRLDKGEDFAKVAKEVSQDPGSKDKGGDLGDVPYSDSGYDKEFMDGAKALKEGEISAPVKTQFGYH
IIKAIKKKEYPVKPFDSVKEDIKKQLLQEKQSEVFKKKIEEWKKALKVKKYEKNLL
>gnl|CDD|234606 PRK00061, ribH, 6,7-dimethyl-8-ribityllumazine synthase; Provisional
MNIIEGNLVAKGLRIGIVVARFNDFITDALLEGALDALKRHGVSEENIDVVRVPGAFEIPLAAKKLAESG
KYDAVIALGAVIRGETPHFDYVANEVAKGLADVSLETGVPVGFGVLTTDTIEQAIERAGTKAGNKGAEAA
LAALEMANLLKQLK
>gnl|CDD|234607 PRK00062, PRK00062, glutamate-1-semialdehyde 2,1-aminomutase
MSKSEELFERAKKLIPGGVNSPVRAFKSVGGTPRFIERAKGAYLYDVDGNEYIDYVGSWGPMILGHAHPE
VVEAVIEAAEKGLSFGAPTELEVELAELVIELVPSIEMVRMVNSGTEATMSAIRLARGYTGRDKIIKFEG
CYHGHADSLLVKAGSGAATLGLPDSPGVPEDFAKHTLTAPYNDLEAVEELFEEYGDEIAAVIVEPVAGNM
GVVPPKPGFLEGLRELCDEHGALLIFDEVMTGFRVALGGAQGYYGVTPDLTTLGKIIGGGLPVGAFGGRR
EIMEQLAPLGPVYQAGTLSGNPLAMAAGLATLKLLKEPGFYEELEALTKRLAEGLKEAAKKAGIPLTVNR
VGSMFGLFFTDEPVTNYADAKKSDTERFARFFHAMLDEGVYLAPSQFEAGFVSAAHTDEDIEKTLEAARK
AFAALA
>gnl|CDD|234608 PRK00064, recF, recombination protein F; Reviewed
MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRSHRTARDKELIRFGAEAAVI
HGRVEKGGRELPLGLEIDKKGGRKVRINGEPQRKLAELAGLLNVVLFTPEDLRLVKGGPSERRRFLDRLL
FQIEPVYASALSQYERALKQRNALLKQADYAWLDVWDEQLAELGAAIAAARLEYLERLAPLAAKTHQEIS
PEFELASLSYQSSVEDDAEKIEEDLLEALAKNRERDRARGRTLVGPHRDDLRFRINGLPAADFGSTGQQK
LLLLALKLAEAELLKEETGEAPILLLDDVASELDDGRRAALLERLKGLGAQVFITTTDLEDLADLLENAK
IFHVEQGKITD
>gnl|CDD|178836 PRK00066, ldh, L-lactate dehydrogenase; Reviewed
MMKKQHNKVVLVGDGAVGSSYAYALVNQGIADELVIIDINKEKAEGDAMDLSHAVPFTSPTKIYAGDYSD
CKDADLVVITAGAPQKPGETRLDLVEKNLKIFKSIVGEVMASGFDGIFLVASNPVDILTYATWKLSGFPK
ERVIGSGTSLDSARFRYMLSEKLDVDPRSVHAYIIGEHGDTEFPVWSHANVAGVPLEEYLEENEQYDEED
LDEIFENVRDAAYEIIEKKGATYYGIAMALARITKAILNNENAVLPVSAYLEGQYGEEDVYIGVPAVVNR
NGIREIVELPLNDDEKQKFAHSADVLKEIMDEAFL
>gnl|CDD|234609 PRK00068, PRK00068, hypothetical protein; Validated
MRPTARMPKLMRRSKILIIIALIIILLLLFGPRLVDFYIDWLWFGEVGYRSVFFTKLVTRIVLFIPVGLL
VGGIVFISLWLAYRSRPVFVPKADSNDPVARYRAVVEKRLRLFLIGIPSFIGLLAGIFAQSYWYRIQLFL
NGVDFGVKDPQFGKDLSFYAFKLPFYRSLLSYLLVLLILAFIITLIAHYILGGIRKGIRLAGRKGGISRF
ARKQLAVLAGLLMLLKAVGYWLDRYNLLYSTRGVFTGASYTDINAVLPAKLILLVIAVICAIAVFSSIVL
RDLRIPAIASVLLILSSIIVGAAWPLIVEQFSVKPNAAEKESEYISRNIDATRKAYGLTDDEVTYRNYGG
KGNLTAQDVAADKATISNIRLLDPTILSPFFTQVQQIRNFYGFPDQLDIDRYNINGKLRDYVVAARELNP
DALIDNQRDWINRHLVYTHGNGFVASPANSVTGVARDPNSNGGYPDFVVKDIPPNNKTVSDGIKLDNPRI
YFGEVIATNDYAIVGTKGDGEFDYPTGDDNKTYTYTGKGGVKIGNFLNRLLFAANYAERNFLLSDDIGSN
SKILFNRDPRDRVEKVAPWLTTDSDPYPAIVDGRIYWIVDGYTTLDNYPYSELTSLSSATADSNEVARLL
PDDNVNYIRNSVKATVDAYDGTVNLYIQDEKDPVLKAWMKIFPGLVKPKSEISPELREHLRYPEDLFKVQ
RKLLAKYHVDDPGVFFSGEDFWDVPKDPKATEGSKNTNQPPYYVVALPPDTNKESFQLISYFNRLKRDNL
AALMSASSDPENYGKLTVYKLPTDKTVYGPKLAQNAINQDPAISKELSLWNDGGNDVQYGNLLTLPVGGS
LLYVEPVYLRAGGQNSYPELKRVLVSYNDKVGYAPTIREALTQLFGDGAGATATGEAPGETKTPPDPPPT
AAPPPPTGPVTLSPAKAAALKEAQDAYNKAIEAQKSGDFAEYGEALKELDDALNKYNKAK
>gnl|CDD|234610 PRK00070, acpS, 4'-phosphopantetheinyl transferase; Provisional
MIVGIGIDIVEIERIEKALERTGDRFAERVLTPKERAKFKSGKRPAEFLAGRFAAKEAFSKALGTGIGKG
VSFRDIEVLNDELGKPIVRLSGEAAERLEKLGGARIHLSISHDGDYAVAFVILESL
>gnl|CDD|234611 PRK00071, nadD, nicotinate-nucleotide adenylyltransferase
EMMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNP
RFSVSDIELERPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPL
EALALPALQQLLEAAGAITLLDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYRS
>gnl|CDD|234613 PRK00073, pgk, phosphoglycerate kinase; Provisional
KKTLDDLDLKGKRVLVRVDFNVPVKDGKITDDTRIRAALPTIKYLLEKGAKVILLSHLGRPKGEDPEFSL
APVAKRLSELLGKEVKFVDDCIGEEAREAIAALKDGEVLLLENVRFNKGEEKNDPELAKKLASLGDVFVN
DAFGTAHRAHASTVGIAKFLKPAAAGFLMEKELEALGKALENPERPFVAILGGAKVSDKIGVLENLLEKV
DKLIIGGGMANTFLKAQGYNVGKSLVEEDLIDTAKELLEKAKEKGVKIPLPVDVVVAKEFSDAEATVVSV
DEIPDDWMILDIGPKTIELFAEIIKDAKTIVWNGPMGVFEFENFAKGTKAVAKAIAESTAFSIIGGGDTA
AAVEKLGLADKFSHISTGGGASLEFLEGKELPGVAALEE
>gnl|CDD|234614 PRK00074, guaA, GMP synthase; Reviewed
IHHDKILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRADPE
IFELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPE
GFKVIASTENCPIAAIANEERKFYGVQFHPEVTHTPQGKKLLENFVFDICGCKGDWTMENFIEEAIEEIR
EQVGDKKVILGLSGGVDSSVAAVLLHKAIGDQLTCVFVDHGLLRKNEAEQVMEMFREHFGLNLIHVDASD
RFLSALAGVTDPEEKRKIIGREFIEVFEEEAKKLGGVKFLAQGTLYPDVIESGGTKKAATIKSHHNVGGL
PEDMKLKLVEPLRELFKDEVRKLGLELGLPEEIVYRHPFPGPGLAIRILGEVTKEKLDILREADAIFIEE
LRKAGLYDKIWQAFAVLLPVKSVGVMGDGRTYDYVVALRAVTSIDGMTADWARLPYDFLEKISNRIINEV
KGVNRVVYDITSKPPATIEWE
>gnl|CDD|234615 PRK00075, cbiD, cobalt-precorrin-6A synthase; Reviewed
YVRSDGKKLRRGYTTGSCAAAAAKAALLALLTGEFPDTVEIDLPKGLRLEIPVESVELDGEQALAIVRKD
AGDDPDVTHGAEIWARVRLNDSPGIVIRGGEGVGTVTRPGLGVPVGEPAINPVPRRMIEENVREVLPEGG
AEVTISVPEGEELAKKTLNPRLGIVGGISILGTTGIVEPMSEEAYLASIKQELDVARANGLDHVVLVTGN
NGEDYARKLLGLPEDAIIKMGNFVGPMLKAAARLGVKKVLLVGHPGKLIKLAAGIFHTHSHVADARLEIL
AALAALAGAPLELLEKILAANTTEEALELLEEAGGEKLYDRIAERILERAREYVGGSIEVGVVLFDRDGQ
ILGRSGEGDEL
>gnl|CDD|234617 PRK00077, eno, enolase; Provisional
MSKIEDIIAREILDSRGNPTVEVEVTLEDGAFGRAAVPSGASTGEREAVELRDGDKSRYLGKGVLKAVEN
VNEEIAPALIGLDALDQRAIDKAMIELDGTPNKSKLGANAILGVSLAVAKAAADSLGLPLYRYLGGPNAK
VLPVPMMNIINGGAHADNNVDIQEFMIMPVGAPSFKEALRMGAEVFHTLKKVLKEKGLSTAVGDEGGFAP
NLKSNEEALDLILEAIEKAGYKPGEDIALALDCAASEFYKDGKYVLEGEGLTSEEMIDYLAELVDKYPIV
SIEDGLDENDWEGWKLLTEKLGDKVQLVGDDLFVTNTKRLKKGIEKGAANSILIKVNQIGTLTETLDAIE
LAKRAGYTAVVSHRSGETEDTTIADLAVATNAGQIKTGSLSRSERIAKYNQLLRIEEELGDAARYAGKKA
FKNLK
>gnl|CDD|234618 PRK00078, PRK00078, Maf-like protein; Reviewed
MKIILASASERRQELLKRILEDFQVIVSDFDESSVPFKGNIESYVMNLAEGKARSVSKKLDQESSIVIGC
DTIVAFNGKVLGKPKDEEDAFEMLKALSGNEHEVYSGIAILDTKSNKIIKDFVCTEVKFSKLTDRQIRKY
INTGEPMDKAGAYGIQGKGGVFVEEINGCYYNVVGLPLNKLYKMLEEMGVNL
>gnl|CDD|234619 PRK00080, ruvB, Holliday junction branch migration DNA helicase RuvB
RLVSPETLEEEEDEIERSLRPKSLDEFIGQEKVKENLKIFIEAAKKRGEALDHVLLYGPPGLGKTTLANI
IANEMGVNIRITSGPALEKPGDLAAILTNLEEGDVLFIDEIHRLSPVVEEILYPAMEDFRLDIMIGKGPA
ARSIRLDLPPFTLIGATTRAGLLTSPLRDRFGIVQRLEFYTVEELEKIVKRSARILGVEIDEEGALEIAR
RSRGTPRIANRLLRRVRDFAQVKGDGVITKEIADKALDMLGVDELGLDEMDRKYLRTIIEKFGGGPVGLD
TLAAALGEERDTIEDVYEPYLIQQGFIQRTPRGRVATPKAYEHLGLNP
>gnl|CDD|234623 PRK00087, PRK00087, bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1
MEIILAKKAGFCFGVKRAVDTAIKTAEELKGKIYTLGPLIHNNQVVEKLKKKGIKPIEDIDELNEGDTII
IRSHGVPPEVLEELKDKGLKVIDATCPFVKNIQKLAKKYYEEGYQIVIVGDKNHPEVIGINGWCNNSAII
VEDGEEAEKLPFDKKICVVSQTTEKQENFEKVLKELKKKGKEVKVFNTICNATEVRQEAAEKLAKKVDVM
IVVGGKNSSNTTKLYEICKSNCTNTIHIENAGELPEEWFKGVKIIGVTAGASTPDWIIEEVIKKMSELDN
MEEVEENEQLEYMNELEKQIRRGDIVKGTVVSVNENEVFVDVGYKSEGVIPLRELTLDEISSLKESVKVG
DEIEVKVLKLEDEDGYVVLSKKEADREKAWKELEEAFENGEPVKGKVKEVVKGGLLVDYGGVRAFLPASH
VELGYVEDLSEYKGQELEVKIIEFNRKRRKKVVLSRKAILEEEKEKKKEETWNSLEEGDVVEGEVKRLTD
FGAFVDIGGVDGLLHVSEISWGRVEKPSDVLKVGDEIKVYILDIDKENKKLSLSLKKLLPDPWENVEEKY
PVGSIVLGKVVRIAPFGAFVELEPGVDGLVHISQISWKRIDKPEDVLSEGEEVKAKILEVDPEEKRIRLS
IKEVEEEPGDIEKVELE
>gnl|CDD|234624 PRK00089, era, GTPase Era; Reviewed
MGFKSGFVAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIHKPKRAL
NRAMNKAAWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKDKEELLPLLEELS
ELMDFAEIVPISALKGDNVDELLDVIAKYLPEGPPYYPEDQITDRPERFLAAEIIREKLLRLLGDELPYS
VAVEIEKFEERGLVRIEATIYVERDSQKGIIIGKGGAMLKKIGTEARKDIEKLLGKKVFLELWVKVKKGW
RDDEKALRELGY
>gnl|CDD|234627 PRK00092, PRK00092, ribosome maturation protein RimP; Reviewed
MMSPLEEQLTELIEPVVEALGYELVDVEYVKEGRDSTLRIYIDKEGGIDLDDCEEVSRQISAVLDVEDPI
PGAYTLEVSSPGLDRPLKKARDFRRFIGREVKVKLYEPIDGRKKFQGILLAVDGETVTLEVEGKEKEVEI
PLDNIAKARLVVEF
>gnl|CDD|234628 PRK00093, PRK00093, GTP-binding protein Der; Reviewed
KPVVAIVGRPNVGKSTLFNRLTGKRDAIVADTPGVTRDRIYGEAEWLGREFILIDTGGIEPDDDGFEKQI
REQAELAIEEADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPDEEADAYEFYSLGLGEPY
PISAEHGRGIGDLLDAILEELPEEEEEDEEDEPIKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTTRD
SIDTPFERDGQKYTLIDTAGIRRKGKVTEGVEKYSVIRTLKAIERADVVLLVIDATEGITEQDLRIAGLA
LEAGRALVIVVNKWDLVDEKTMEEFKKELRRRLPFLDYAPIVFISALTGQGVDKLLEAIDEAYENANRRI
STSVLNRVLEEAVERHPPPLVKGRRLKIKYATQVGTNPPTFVLFVNDPELLPFSYKRYLENQLREAFDFE
GTPIRLEFREKKNKL
>gnl|CDD|234629 PRK00094, gpsA, NAD(P)H-dependent glycerol-3-phosphate dehydrogenase
MMKIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADRENPRYLPGIKLPDNLRATTDLAEALA
DADLILVAVPSQALREVLKQLKPLLPPDAPIVWATKGIEPGTGKLLSEVLEEELPDLAPIAVLSGPSFAK
EVARGLPTAVVIASTDEELAERVQELFHSPYFRVYTNTDVIGVELGGALKNVIAIAAGIADGLGLGDNAR
AALITRGLAEITRLGVALGANPETFLGLAGLGDLVLTCTSPLSRNRRFGLALGQGKSLEEALAEIGMVAE
GVRTAKAVYELAKKLGVEMPITEAVYAVLYEGKDPREAVEDLMGR
>gnl|CDD|234630 PRK00095, mutL, DNA mismatch repair endonuclease MutL
MPIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLAL
ALARHATSKIASLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVYEGGEIVEVKPAAHPV
GTTIEVRDLFFNTPARRKFLKSEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAA
ILGREFAENALPIDAEHGDLRLSGYVGLPTLSRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRY
PAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAIQEALAQSGLIPAAAGANQVLEPAEPEPLP
LQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASAEAAAAAPAAAPEPAE
AAEEADSFPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELS
EDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQELEELIRDLLDELAEEGDSDTLKERELLA
TMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSLSDLEKLFKRI
>gnl|CDD|234631 PRK00098, PRK00098, GTPase RsgA; Reviewed
MEGLIIKALGGFYYVESEDGQVYQCRARGKFRKKTNTPAVGDRVEFSAENNDEGVILEIHERKNLLVRPP
IFKSKLIAANVDQAVLVFAAKEPDFSTDLLDRFLVLAEANGIKPIIVLNKIDLLDDLEEARELLALYRAI
GYDVLELSAKEGEGLDELKPLLAGKVTVLAGQSGVGKSTLLNALAPDLELKTGEISEALGRGKHTTTHVE
LYDLPGGGLLIDTPGFSSFGLHDLEAEELEHYFPEFRPLSGDCKFRNCTHLHEPGCAVKAAVEEGEIAPS
RYESYLQILEEIENRRER
>gnl|CDD|234632 PRK00099, rplJ, 50S ribosomal protein L10; Reviewed
MNREEKKEIVAELAEKLKKAQSAVVADYRGLTVAQMTELRKKLREAGVEYKVVKNTLARRALEGTGFEGL
DDLLKGPTAIAFSYEDPVAAAKVLKDFAKDNKKLEIKGGAIEGKVLDAEEVKALAKLPSREELLAKLLGV
LQAPATKLAGVLNAPPSKLARVLKALAEKKEA
>gnl|CDD|234634 PRK00103, PRK00103, rRNA large subunit methyltransferase; Provisional
MKITIIAVGKLKPKWLKDGIAEYLKRFPRYLKLELIEIPDEKRPKNADAEQIKAKEGERILAALPKGARV
IALDERGKQLSSEEFAQELERWRDDGRSDVAFVIGGADGLSPAVKKRADQSLSLSKLTLPHQLVRVLLAE
QLYRAWSILAGHPYHRE
>gnl|CDD|234635 PRK00104, scpA, segregation and condensation protein A; Reviewed
MEMNIKLKNFEGPLDLLLHLIKKYEIDIYDIPIVEITEQYLAYIHTMQEMELEVASEYLVMAATLLLIKS
KMLLPKVEEFEEEEEDPRQELLEKLIEYKKFKEAAEELKEQEEERAQYFSKPPSDLEEFDAELDEDELDG
DVTLLDLFLAFSKLMERKKANKPRHTKIERDEYKIEDRMLYILELLESKKRLSFSELFKEPSKNEFVVTF
LALLELIKLQEIIVEQEENFGEIYLEKGEEEE
>gnl|CDD|234636 PRK00105, cobT, nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase; Reviewed
PDAAAMAAAQARIDQLTKPPGSLGRLEELAVQLAGIQGTEPPRVERPAVVVFAGDHGVAEEGVSAYPQEV
TAQMVANFLAGGAAINVLARQAGADLEVVDLGVDAPEPLPGLINMRVARGTGNIAKEPAMTREEAEAALA
AGAALADEAADAGTDLLGVGEMGIGNTTPAAALVAALTGGDPEEVVGRGTGIDDAGLARKIAVVRRALAR
HRPALQDPLDVLAKVGGFEIAAMAGAILGAAVRRIPVLLDGFISTAAALVAVRLAPGVRDYLIFSHRSAE
PGHRLALEHLGLEPLLDLGMRLGEGTGAALALPLVRAAVAFYNEMATFAEAGVSD
>gnl|CDD|178867 PRK00106, PRK00106, ribonuclease Y
MINIIILVVSALIGLVIGYVLISIKMKSAKEAAELTLLNAEQEAVNLRGKAERDAEHIKKTAKRESKALK
KELLLEAKEEARKYREEIEQEFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKH
IDEREEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDKMAKDLLA
QAMQRLAGEYVTEQTITTVHLPDDNMKGRIIGREGRNIRTLESLTGIDVIIDDTPEVVVLSGFDPIRREI
ARMTLESLIKDGRIHPARIEELVEKNRLEMDNRIREYGEAAAYEIGAPNLHPDLIKIMGRLQFRTSYGQN
VLRHSVEVGKLAGILAGELGENVALARRAGFLHDMGKAIDREVEGSHVEIGMEFARKYKEHPVVVNTIAS
HHGDVEPESVIAVIVAAADALSSARPGARNESMENYIKRLRDLEEIANSFDGVQNSFALQAGREIRIMVQ
PEKISDDQVTILAHKVREKIENNLDYPGNIKVTVIRELRAVDYAK
>gnl|CDD|234639 PRK00109, PRK00109, Holliday junction resolvase RuvX
MPSGRILGLDVGTKRIGVAVSDPLGGTAQPLETIKRNNGTPDWDRLEKLIKEWQPDGLVVGLPLNMDGTE
GPRTERARKFANRLEGRFGLPVVLVDERLSTVEAERALADVGSRKKLRKGVIDSLAAVIILQSYLDSL
>gnl|CDD|234640 PRK00110, PRK00110, YebC/PmpR family DNA-binding transcriptional regulator
MAGHSKWANIKHRKGAQDAKRGKIFTKLIREITVAAKLGGGDPEGNPRLRLAIDKAKAANMPKDNIERAI
KKGTGELDGANYEEIRYEGYGPGGVAIIVEALTDNRNRTAAEVRHAFSKNGGNLGETGSVSYMFDRKGVI
VIEPLDEDELMEAALEAGAEDVETDDESFEVITAPEDFEAVRDALEAAGLEAESAEVTMIPQNTVELDEE
TAEKLLKLIDALEDLDDVQNVYHNAEISDEVMAKL
>gnl|CDD|234641 PRK00111, PRK00111, hypothetical protein; Provisional
MTMTDPIEQAFERIRAEAMRRNGSVPDLNKNDAFRRPPAPAGGVEKRKKGRATGLDGRRKRYVRGAESLG
SVLNKEIQRRGWGKDIAGGWVTSHWDELVGAKIAQHTKVEMIKDKKLFITCDSTAWATNLRMMQRQILQV
IAEKVGPDIITELRIFGPQAPSWRKGPLHVKGRGPRDTYG
>gnl|CDD|234643 PRK00114, hslO, Hsp33 family molecular chaperone HslO
MADYLVRALAEDGAVRGEAVDTTETVQEAQERHDYPPTATAALGRTLTATSLLTATLKFDGDITVQIQGD
GPLGLIVVDANADGQVRGYVRNPGVDLELNADGKLDVGQAVGNGYLVVTKDPGLGEPYQGVVPLVSGEIG
EDLAYYFARSEQTPSAVGLGVLVNEDDSIKAAGGFLLQVLPGAAEDFEHLATLEERIKEEELFSLLLESG
LTAEELLYRLYHEEDVKILEPQPVEFKCDCSRERSANALKSLGKEELQEMIAEDGGAEMVCQFCGNKYLF
DEEDLEELIAEAS
>gnl|CDD|234645 PRK00116, ruvA, Holliday junction branch migration protein RuvA
MIGYLKGKLVEKGPDYVVIEVNGVGYEVQVPMRTLYELPEVGEEVKLYTHLVVREDAILLYGFLTKEERE
LFRLLISVSGVGPKLALAILSGLSPEELVQAIANGDVKALTKVPGIGKKTAERIVLELKDKLAAAASAAA
AAAAASSALEEAVSALVALGYKPKEASKAVAKILKEAASVEELIREALKLLS
>gnl|CDD|234646 PRK00117, recX, recombination regulator RecX; Reviewed
LEDTARRRMYASARARALRLLARREHSRAELRRKLAAKGFSEEVIEAVLDRLKEEGLLDDERFAESFVRS
RARKGYGPRRIRQELRQKGVDREIIEEALAELDIDWEELARELARKKFRRPLPDDAKEKAKLVRFLARRG
FSMDVIQRVLRNALDDE
>gnl|CDD|234647 PRK00118, PRK00118, putative DNA-binding protein; Validated
LEKTLRMNLLFDFYGSLLTEKQRNYMELYYLDDYSLGEIAEEFNVSRQAVYDNIKRTEKLLEDYEEKLHL
YEKFIERNELFDKIAYLKEKYPDDEELKKLIEIL
>gnl|CDD|234648 PRK00120, PRK00120, dITP/XTP pyrophosphatase; Reviewed
MKIVLASHNAGKLRELKALLAPFGIEVVSQGELGVPEPEETGTTFVENALIKARHAAKATGLPALADDSG
LCVDALGGAPGVYSARYAGEGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRPDPTPLVAEGRWEGE
ILWEPRGENGFGYDPIFFPPGYGKTFAELTPEEKNAISHRGKALKLLLEALRELLA
>gnl|CDD|234649 PRK00121, trmB, tRNA (guanine-N(7)-)-methyltransferase; Reviewed
LRSFVRRRGRLTKGQQRAIEELWPRLSPAPLDWAELFGNDAPIHLEIGFGKGEFLVEMAKANPDINFIGI
EVHEPGVGKALKKIEEEGLTNLRLLCGDAVEVLLDMFPDGSLDRIYLNFPDPWPKKRHHKRRLVQPEFLA
LYARKLKPGGEIHFATDWEGYAEYMLEVLSAEGGFLVSEAGDYVPRPEGRPMTEYERKGLRK
>gnl|CDD|234650 PRK00122, rimM, 16S rRNA-processing protein RimM; Provisional
MSKPEDLLVVGKIVSAHGIKGEVKVKSFTDFPERIFDYGPWLLGKGGEWQEVEIESGRFHKGFLIVKFEG
VDDRNAAEALKGCELFVPRSQLPELEEDEYYWHDLIGLEVVDEDGEELGKVTDILETGANDVLVVLKDKK
EERLIPFVEEVVKEVDLEAKRITVDWPEGLLD
>gnl|CDD|178882 PRK00124, PRK00124, YaiI/YqxD family protein
MKIYVDADACPVKDIIIRVAERHGIPVTLVASFNHFLRVPYSPFIRTVYVDAGFDAADNEIVQLAEKGDI
VITQDYGLAALALEKGAIVLNPRGYIYTNDNIDQLLAMRDLMATLRRSGIRTGGPKPFTQEDRSRFEAEL
DKLIRRIKRLR
>gnl|CDD|234651 PRK00125, pyrF, orotidine 5'-phosphate decarboxylase; Reviewed
TFIDRLREAVARRGSLCVGLDPHPSLLPAWGLSGDADGLFEFCRIIVDATADLVAAFKPQIAYFEAHGAE
GLAQLERTIAYLREAGVLVIADAKRGDIGSTAEAYAKAAFESPLEADAVTVSPYMGFDSLEPYLEYAEEH
GKGVFVLCRTSNPGGSDLQFLRTADGRPLYQHVADLAAALNNLGNCGYGSIGLVVGATFPPELAAVRKIL
GGMPLLIPGIGAQGGDAEATVRAGGAAGNGGIPNSSRAILYAGPGKDFAEAARRAAERTRDAINAARA
>gnl|CDD|234653 PRK00129, upp, uracil phosphoribosyltransferase; Reviewed
MMKVHVVDHPLIQHKLTLLRDKNTSTKRFRELLEELGRLLAYEATRDLPLEEVEIETPLGKTTGKRIAGK
KLVIVPILRAGLGMVDGVLKLIPSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSA
IAAIDLLKKRGAKNIKVLCLVAAPEGIKALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGTK
>gnl|CDD|234654 PRK00131, aroK, shikimate kinase; Reviewed
MLKGPNIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLIEARAGKSIPEIFEEEGEAAFRELEEEVLAEL
LARHNLVISTGGGAVLREENRALLRERGTVVYLDASFEELLRRLRRDRNRPLLQTNDPKEKLRDLYEERD
PLYEEVADITVETDGRSPEEVVNEILEKLEAAWRR
>gnl|CDD|178888 PRK00132, rpsI, 30S ribosomal protein S9; Reviewed
MAEVQYYGTGRRKTAVARVRLKPGSGKITVNGRDLEEYFPRETLRMVVRQPLELTETEGKFDVYVTVKGG
GISGQAGAIRHGIARALLEYDPDLRPALKKAGFLTRDARMVERKKYGLKKARRAPQFSKR
>gnl|CDD|234655 PRK00133, metG, methionyl-tRNA synthetase; Reviewed
MRKILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELI
ARYHAEHKRDFAGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKG
TCPKCGAEDQYGDNCEVCGATYSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWITRSGELQP
NVANKMKEWLEEGLQDWDISRDAPYFGFEIPGAPGKVFYVWLDAPIGYISSTKNLCDKRGGLDWDEYWKK
DSDTELYHFIGKDIIYFHTLFWPAMLEGAGYRLPTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPD
YLRYYLAAKLPETIDDLDFNWEDFQQRVNSELVGKVVNFASRTAGFINKRFDGKLPDALADPELLEEFEA
AAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQDGERLQAVCSVGLNLFRALAIYLKPVL
PELAERAEAFLNLEELTWDDAQQPLAGHPINKFKILFTRIEDKQIEALIEASKEAAAAKAAAAAAAAPLA
EEPIAETISFDDFAKVDLRVAKIVEAEKVEGADKLLKLTLDLGEETRQVFSGIKSAYDPEELVGKLVVMV
ANLAPRKMKFGVSEGMVLAAGPGGGDLFLLEPDEGAKPGMRVK
>gnl|CDD|234656 PRK00134, ccrB, fluoride efflux transporter family protein
MQKLPQGLLVGAGAALGACVRLALTSQLGDAPWPILLINVLGAFLMGWLRPNAFWGTGFLGGFTSFSAFA
LLLAALSWLNAVAYYLVTVVGCIAAWLLGDRLAA
>gnl|CDD|234657 PRK00135, scpB, segregation and condensation protein B; Reviewed
QKMNYKSIIEALLFVSGEEGLSLEQLAEILELEPTEVQQLLEELQEKYEGDDRGLKLIEFNDVYKLVTKE
ENADYLQKLVKTPIKQSLSQAALEVLAIIAYKQPITRIEIDEIRGVNSDGALQTLLAKGLIKEVGRKEVP
GRPILYGTTDEFLDYFGINSLDELPKLSEFEEQAEEFDLFDSQREEDE
>gnl|CDD|234658 PRK00136, rpsH, 30S ribosomal protein S8; Validated
SMTDPIADMLTRIRNAQMAKHETVSMPASKLKVAIAEILKEEGYIKDYEVEEDGKQGILRITLKYGEGEP
VIEGIKRVSKPGLRVYKKKDELPKVLNGLGIAIVSTSKGVMTDREARKAGVGGEVLCYVW
>gnl|CDD|234660 PRK00139, murE, UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
MASMKLRDLLAPVEITGLTYDSRKVKPGDLFVALPGHKVDGRDFIAQAIANGAAAVVAEADGEAGTGVPV
IIVPDLRKALALLAAAFYGHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTALIGTLGNGIGGELIP
SGLTTPDALDLQRLLAELVDAGVTYAAMEVSSHALDQGRVDGLKFDVAVFTNLSRDHLDYHGTMEDYLAA
KARLFSELGLAAVINADDEVGRRLLALPDAYAVSMAGADLRATDVEYTDSGQTFTLVTEVESPLIGRFNV
SNLLAALAALLALGVPLEDALAALAKLQGVPGRMERVDAGQGPLVIVDYAHTPDALEKVLEALRPHAKGR
LICVFGCGGDRDKGKRPLMGAIAERLADVVIVTSDNPRSEDPAAIIADILAGIYDVIEDRAEAIRYAIAQ
AKPGDVVLIAGKGHEDYQIIGGVKIPFDDREVAREALAER
>gnl|CDD|234661 PRK00140, rplK, 50S ribosomal protein L11; Validated
MAKKVVGYIKLQIPAGKANPAPPVGPALGQRGVNIMEFCKAFNARTQDQKGLPIPVVITVYEDRSFTFIT
KTPPASVLLKKAAGIEKGSGEPNKEKVGKITRAQVREIAETKMPDLNAADIEAAMRMIAGTARSMGIVVE
G
>gnl|CDD|234663 PRK00142, PRK00142, rhodanese-related sulfurtransferase
MKPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFA
DIRFKISEDDGHAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYE
IGHFENAIEPDIETFREFPPWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYG
EDPETQGLLWDGKLYVFDERMAVPINDEVPIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCC
SEECCEHPRNRYVEQRGRRRERENELLIFNKERH
>gnl|CDD|234664 PRK00143, mnmA, tRNA-specific 2-thiouridylase MnmA; Reviewed
KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDETGKGGCCAEEDIADARRVADKLGIPHYVVD
FEKEFWDRVIDYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDGRELLRGVDP
NKDQSYFLYQLTQEQLAKLLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQ
PGEIVDLDGKVLGEHKGLMYYTIGQRKGLGIGGDGEPWYVVGKDPETNTVVVGQGEALYSRELIASDLNW
VGGEPPEEPFECTAKIRYRQKPVPATVELEDDRVEVEFDEPQRAVTPGQAAVFYDGDRVLGGGIIE
>gnl|CDD|234665 PRK00145, PRK00145, putative inner membrane protein translocase component YidC; Provisional
MMRYLNNAFVQFFKFIHGFVSSVISNPNFSYGIAIILVTLIIRLLILPLNIKQTKSSLRMNEIQPEIKKL
QAKYKNDPQKLQQEMMKLYKEKGVNPLGGCLPLLIQWPILIALYYVFNNLTGINGVSFLWIKDLAKPDIT
WILPILSGATTYLSGYLMTKADSSQAGQMKTMNIGMSIFMGVMSWKFKSALVLYWVIGNLIQIIQTYFIK
KLELKKKVEAKAA
>gnl|CDD|234666 PRK00147, queA, S-adenosylmethionine:tRNA ribosyltransferase-isomerase; Provisional
MKLSDFDFDLPEELIAQYPLEPRDASRLLVLDRKTGEIEHRHFRDLPDYLNPGDLLVFNDTRVIPARLFG
RKKETGGKIEVLLLRRLDEDRWLALVRPAKRPKPGTKLYFGDGLKAEVLERLEDGGRILRFLYEGIFLEL
LEELGHMPLPPYIKRPDEDADRERYQTVYAKEPGAVAAPTAGLHFTEELLEKLKAKGVEIAFVTLHVGAG
TFRPVRVEDIEEHKMHSEWYEVPQETADAINAAKARGGRVIAVGTTSVRTLESAARAGGELKPFSGWTDI
FIYPGYRFKVVDALITNFHLPKSTLLMLVSAFAGRERILAAYKHAVAEKYRFFSYGDAMLIL
>gnl|CDD|234667 PRK00149, dnaA, chromosomal replication initiator protein DnaA
NLQSLWEKVLERLKDELSEQEYETWIKPLKALSLEDNTLTLYVPNRFVKDWIEKNYLDLIEEALQLNPKY
TFDNFVVGKSNRLAHAAALAVAENPGKAYNPLFIYGGVGLGKTHLLHAIGNYILEKNPNAKVVYVTSEKF
TNDFVNALRNNTMEEFKEKYRSVDVLLIDDIQFLAGKERTQEEFFHTFNALHEAGKQIVLTSDRPPKELP
GLEERLRSRFEWGLTVDIEPPDLETRIAILKKKAEEEGIDLPDEVLEFIAKNITSNVRELEGALNRLIAY
ASLTGKPITLELAKEALKDLLAAQKKKITIENIQKVVAEYYNIKVSDLKSKSRTRNIARPRQIAMYLAKE
LTDLSLPEIGRAFGGRDHTTVLHAVRKIEKLLEEDPELKEDVEELKRKLKS
>gnl|CDD|234668 PRK00150, def, peptide deformylase; Reviewed
MAILPILRYGDPVLRKVAKPVEEVDDELRKLIDDMFETMYAAPGVGLAAPQVGVSKRIIVIDVEDKEGEP
LVLINPEIISESSEEYLTYEEGCLSVPGVYGEVPRPERVTVKALDRDGKPFELEADGLLARCIQHEIDHL
NGVLFIDRLSPLKRFRIKKKLKKIE
>gnl|CDD|234670 PRK00155, ispD, D-ribitol-5-phosphate cytidylyltransferase
MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKD
PKVTVVAGGAERQDSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRS
DDGGGIVDTPDRSGLWAAQTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKIT
TPEDLALAEAILKRRIA
>gnl|CDD|178907 PRK00159, PRK00159, putative septation inhibitor protein; Reviewed
MPKSKVRKKNDFTVSSVSRTPVKVKAGPSSVWYVVLMLGLMLIGLAWLVVNYLAGPAIPWMADLGPWNYA
IGFALMITGLLMTMRWR
>gnl|CDD|178908 PRK00162, glpE, thiosulfate sulfurtransferase GlpE
MDQFECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNS
SQGAAQYLLQQGFDVVYSIDGGFEAWRRTFPAEVASGA
>gnl|CDD|234672 PRK00164, moaA, GTP 3',8-cyclase MoaA
PVPMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEELLSLEEIERLVRAFVALGVRKVR
LTGGEPLLRKDLEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGR
DRLDQVLAGIDAALAAGLTPVKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHL
SGAEIRARLAERGWTLQPRARSGGPAQYFRHPDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAE
DGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHDGNTGPTRHMSYIGG
>gnl|CDD|234673 PRK00166, apaH, symmetrical bis(5'-nucleosyl)-tetraphosphatase
MATYAIGDIQGCYDELQRLLEKIDFDPAKDTLWLVGDLVNRGPDSLEVLRFVKSLGDSAVTVLGNHDLHL
LAVAAGIKRNKKKDTLDPILEAPDRDELLDWLRHQPLLHVDEELGLVMVHAGIPPQWDLATALALAREVE
AVLRSDDYRDFLANMYGNEPDRWSPDLTGLERLRYIINAFTRMRFCTPDGRLDFKCKGPPDEAPAGLKPW
FEVPGRKTRDYTIVFGHWAALEGLTTPPNIIALDTGCVWGGKLTALRLEDKQIFQVPCLKAKDPG
>gnl|CDD|234675 PRK00170, PRK00170, azoreductase; Reviewed
MSKVLVIKSSILGDYSQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDGEVVGALGKSAETLTPRQ
QEAVALSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGPVGLVTGKKALLITS
RGGIHKDGPTDMGVPYLKTFLGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAADELAAA
>gnl|CDD|178914 PRK00173, rph, ribonuclease PH; Reviewed
MRPDGRAADQLRPVTITRNFTKHAEGSVLVEFGDTKVLCTASVEEGVPRFLKGQGQGWVTAEYGMLPRAT
HTRNDREAAKGKQGGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVIQADGGTRTASITGAYVALADA
LNKLVARGKLKKNPLKDQVAAVSVGIVDGEPVLDLDYEEDSAAETDMNVVMTGSGGFVEVQGTAEGAPFS
REELDALLDLAEKGIAELVALQKAALAD
>gnl|CDD|234677 PRK00174, PRK00174, acetyl-CoA synthetase; Provisional
VFPPPAEFAANALIDMEQYKALYQESVEDPEGFWAEQAKRLDWFKPFDTVLDWNAPFIKWFEDGELNVSY
NCLDRHLKTRGDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAM
LACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCPSVEKVIVVR
RTGGDVDWVEGRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKY
VFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAI
RALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATP
LKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDG
ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEP
SDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEEILGDTSTLADPSVVEKLI
EARQNRK
>gnl|CDD|234678 PRK00175, metX, homoserine O-acetyltransferase; Provisional
ASFPMDSVGPVGPQTLHFDEPLPLESGAVLPPVELAYETYGTLNADRSNAVLICHALTGDHHVAGPHSPD
DPKPGWWDNMVGPGKPIDTDRYFVICSNVLGGCKGSTGPSSINPDTGKPYGSDFPVITIRDWVRAQARLL
DALGITRLAAVVGGSMGGMQALEWAIDYPDRVRSALVIASSARLSAQNIAFNEVARQAILADPDWHGGDY
YEHGVVPERGLAVARMIGHITYLSDDELDEKFGRELQSGELPFGFDVEFQVESYLRYQGDKFVERFDANS
YLYLTRALDYFDPARGRGGDLAAALARIKARFLVVSFTSDWLFPPARSREIVDALLAAGADVSYAEIDSP
YGHDAFLLDDPRYGRLVRAFLERAARERG
>gnl|CDD|234679 PRK00179, pgi, glucose-6-phosphate isomerase; Reviewed
KNINLTQTPAWQALQAHADEIKDVHLRDLFAADPDRFERFSLTAGGLLLDYSKNRITDETLALLLDLARE
AGLEGARDAMFAGEKINTTEDRAVLHTALRNPSNTPILVDGQDVMPEVHAVLARMKAFAEAVRSGEWKGY
TGKAITDVVNIGIGGSDLGPVMVTEALRPYADPGLRVHFVSNVDGAHLAETLKKLDPETTLFIVASKTFT
TQETLTNAHSARDWFLAAGGDEAAVAKHFVAVSTNAEAVAEFGIDPDNMFGFWDWVGGRYSLWSAIGLSI
ALAIGPDNFEELLAGAHAMDEHFRTAPLEKNLPVLLALIGVWYRNFFGAQSHAVLPYDQYLHRFPAYLQQ
LEMESNGKSVDRDGTPVDYQTGPIIWGEPGTNGQHAFFQLLHQGTKLVPADFIAPAQPHNPLGDHHDLLL
ANCFAQTEALMFGKTAEEVRAELRAKGLDEAEAEELAPHKVFPGNRPSTTILLDRLTPFTLGALIALYEH
KVFVQGVIWGINSFDQWGVELGKQLAKRILPELEGDSEASAHDSSTNGLINRYRAWRG
>gnl|CDD|234680 PRK00180, PRK00180, acetate kinase A/propionate kinase 2; Reviewed
MKILVLNAGSSSLKFQLIDMPNEEVLASGLVERIGLPDSRIKIKVDGGEKEEEELPIPDHAEALKFLLNT
LTDGKLGLIKDLDEITAVGHRVVHGGEKFTESVLIDDEVLAAIEELSPLAPLHNPANLIGIEAARKLLPN
VPQVAVFDTAFHQTMPEEAYLYALPYELYEKYGIRRYGFHGTSHRYVSQRAAELLGKPLEELNLITCHLG
NGASIAAIKNGKSVDTSMGFTPLEGLVMGTRSGDIDPAIIPYLMEKLGMSVDEIDNLLNKKSGLLGLSGV
SSDMRDIEAAAEEGDERAKLALDVFVYRLAKYIGSYAAALNGRLDAIVFTAGIGENSALVREKVLEGLEF
LGIELDPEKNLAARFGKEGDISTPDSKVKVLVIPTNEELMIARDTLRLLGKK
>gnl|CDD|234681 PRK00182, tatB, Sec-independent protein translocase subunit TatB
MFSSVGWGEILLLLIVGLIVIGPERLPRLIEDVRAALLAARTAINNAKQQLDGDFGEEFDEFRKPLNQIA
SYRRMGPKTAITKALFDGDDSFLDDFDPKKIMADGTEGEAQRQQQASAGRADNNANVVTRPADGSQPRSS
QNDPKGGPPYAGGYSWDDIT
>gnl|CDD|166842 PRK00183, PRK00183, hypothetical protein; Provisional
MSVSICPCGSGDLLDACCGRYHAGHPAPCAEALMRSRYSAYVLGLVDYLVATTLPAQQAGLDRAAIAAWS
AQSTWLGLEVESSEVLGGQPEHAFVTFTARWHDADGEHSHRERSAFVQHQGRWYFIDPTVPLKAGRNDPC
PCGSGQKFKKCCAPYLG
>gnl|CDD|166843 PRK00187, PRK00187, NorM family multidrug efflux MATE transporter
MQVPPTTELKAILRLAGPLIASQLAHMLMVFTDTLMMGRLGPEALAGGGLGAASYSFVSIFCVGVIAAVG
TLVAIRHGAGDIEGATRLAQAGLWLAWLLALVAALLLWNLKPLLLLFGQAPQNVDAAMQFLHLLPFALPG
YLSFMALRGFTSALGRAGPVMVISLAGAVANLLLNYALIEGWFGLPKLGLMGIGLVTALVSNGMALALAL
YIRRHPAYAAYPLRKGLSRPSRAALRELWRLGLPIGGTYAVEVGLFTFAALCMGALGSTQLAAHQIALQI
VSVAFMVPVGLSYAVTMRVGQHYGAGRLLEARRAGRVGIGFGAVVMLLFAGLFWLLPEAIIGLFLDRNDP
AFAEIVQLAVSLLAVAAWFELFDGTQTIAMGAIRGLKDARTTFLIGLACYWLVGAPLAWLLAFTLGWGAV
GVWWGLALGLACAAVALTLAFEWKTARLLRKARASEAVALSAAQ
>gnl|CDD|234682 PRK00188, trpD, anthranilate phosphoribosyltransferase; Provisional
MTMKELLEKLVEGEDLSEEEAEELMDAIMSGEATPAQIAAFLTALRVKGETVDEIAGAARAMREHAVPVP
DPDDAVDIVGTGGDGANTFNISTAAAFVAAAAGVKVAKHGNRSVSSKSGSADVLEALGVNLDLSPEQVAR
CLEEVGIGFLFAPLYHPAMKHVAPVRKELGIRTIFNLLGPLTNPARPKRQLIGVYSPDLLEPMAEVLKRL
GSKRALVVHGSDGLDEISLTGPTTVAELKDGEIREYTLTPEDFGLPRAPLEDLRGGDPEENAAILRAVLQ
GKGPGAARDAVLLNAAAALYVAGKADDLKEGVELAREAIDSGAALAKLEELVAFSQELK
>gnl|CDD|234683 PRK00191, tatA, twin arginine translocase protein A; Provisional
MSLGPWEIGIIVLLIIVLFGAKKLPDAARSIGRSMRIFKSEVKEMSKDDQTPEQQQQQPQQQIAPNQIEA
PQPNFQQHYQGQQV
>gnl|CDD|234684 PRK00192, PRK00192, mannosyl-3-phosphoglycerate phosphatase; Reviewed
DMMKLLVFTDLDGTLLDHHTYSYEPAKPALKALKEKGIPVIPCTSKTAAEVEVLRKELGLEDPFIVENGA
AIYIPKNYFPFQPDGERLKGDYWVIELGPPYEELREILDEISDELGYPLKGFGDLSAEEVAELTGLSGES
ARLAKDREFSEPFLWNGSEAAKERFEEALKRLGLKVTRGGRFLHLLGGGDKGKAVRWLKELYRRQDGVET
IALGDSPNDLPMLEAADIAVVVPGPDGPNPPLLPGIADGEFILASAPGPEGWAEAINKLLSKL
>gnl|CDD|178923 PRK00194, PRK00194, ACT domain-containing protein
MMKAIITVIGKDKVGIIAGVSTVLAELNVNILDISQTIMDGYFTMIMLVDISESKKDFAELKEELEELGK
ELGVKIRIQHEEIFDAMHRI
>gnl|CDD|234685 PRK00197, proA, gamma-glutamyl phosphate reductase; Provisional
DIMEYLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDLAAARANGLSAAMLDRL
LLTEARIEGIAEGLRQVAALPDPVGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPNVTVDAAALCLKS
GNAVILRGGSEAIHSNRALVAVIQEALEEAGLPADAVQLVETTDRAAVGELLKLDGYVDVIIPRGGAGLI
RRVVENATVPVIEHGDGICHIYVDESADLDKALKIVLNAKTQRPSVCNALETLLVHEAIAEEFLPKLAEA
LAEAGVELRGDEAALALLPDVVPATEEDWDTEYLDLILAVKVVDSLDEAIAHINRYGSGHTEAIVTEDYA
AAERFLNEVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELTTYKYIVLGDGQIRA
>gnl|CDD|178925 PRK00199, ihfB, integration host factor subunit beta; Reviewed
MTKSELIERLAARNPHLSAKDVENAVKEILEEMSDALARGDRIEIRGFGSFSLHYRPPRVGRNPKTGEKV
ELEEKYVPHFKPGKELRERVNIYG
>gnl|CDD|234686 PRK00202, nusB, transcription antitermination factor NusB
AARRKAREAAVQALYQWELSGNDIAEIIEAQLLEEQYDKADPAYFRSLVRGVVENQAELDELISPYLKDW
TLERLDPVERAILRLALYELLFRDDVPYKVVINEAIELAKKFGDEDSHKFVNGVLDKIAKELRPAEK
>gnl|CDD|178927 PRK00203, rnhA, ribonuclease H; Reviewed
MKQVEIYTDGACLGNPGPGGWGAILRYKGHEKELSGGEALTTNNRMELMAAIEALEALKEPCEVTLYTDS
QYVRQGITEWIHGWKKNGWKTADKKPVKNVDLWQRLDAALKRHQIKWHWVKGHAGHPENERCDELARAGA
EEATLEDTGY
>gnl|CDD|178928 PRK00207, PRK00207, sulfurtransferase complex subunit TusD
MRYAIAVTGPAYGTQQASSAYQFAQALLAEGHELVSVFFYQDGVLNANALTVPASDEFDLVRAWQQLAAE
HGVALNVCVAAALRRGVVDEEEAERLGLAAANLAPGFELSGLGELAEASLTADRVVQF
>gnl|CDD|234687 PRK00208, thiG, thiazole synthase; Reviewed
MLTIAGKTFSSRLLLGTGKYPSPQVMQEAIEASGAEIVTVALRRVNLGQGGDNLLDLLPPLGVTLLPNTA
GCRTAEEAVRTARLAREALGTNWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFVVLPYCTDDPVLAKRL
EEAGCAAVMPLGAPIGSGLGLLNPYNLRIIIEQADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVA
GDPVAMARAFKLAVEAGRLAYLAGRIPKRDYASASSPLTG
>gnl|CDD|178930 PRK00211, PRK00211, sulfurtransferase complex subunit TusC
MKRIAFVFRQAPHGTASGREGLDALLATSAFTEDIGVFFIDDGVFQLLPGQQPDAILARDYIATFKLLPL
YDIEQCYLCAASLRERGLDPNTDFVLDVEPLDAAALRRKLDNYDVVLTF
>gnl|CDD|234689 PRK00216, ubiE, bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE
FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALA
KAVGKTGEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKA
LREMYRVLKPGGRLVILEFSKPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELA
AMLEEAGFERVRYRNLTGGIVALHVGYKP
>gnl|CDD|234690 PRK00218, PRK00218, lysogenization regulator HflD
MAKNYQDRTLALAGICQAAQLVQQLARTGQCDEDALETSLNSLLVTNPSSTLDVYGGEANLRLGLETLLN
QLNSSRQGLDAELTRYALSLLALERKLSKNPDALNTLGERINQIQRQLEHFDLLHENVIANLAGIYVDTI
SPLGPRIQVTGNPAYLQQPQVQAKIRALLLAGIRSAVLWRQVGGSRWQLLFSRKKLLKQAKQLLAHL
>gnl|CDD|234691 PRK00220, PRK00220, glycerol-3-phosphate 1-O-acyltransferase PlsY
MSMIALLLILLAYLLGSIPFALLVGKLFGLPDPREHGSGNPGATNVLRIGGKKAAIATLLGDALKGTLAV
LLAYLFGLDPISLGLIALAAVLGHIFPVFFKFKGGKGVATAAGVLLGIGPLLALILAATWLLVALLTRYS
SLAALVAALIAPIYVWWFPPDWQFTIPVALLSVLIIYRHRDNIQRLLAGTESKIGWKK
>gnl|CDD|234693 PRK00226, greA, transcription elongation factor GreA; Reviewed
MMKKIPMTQEGYEKLEEELEELKTVERPEIIEAIAEAREHGDLSENAEYHAAKEEQGFIEGRIRELEDKL
SNAEVIDPSKLSGGKVKFGSTVTLKDLDTDEEETYQIVGSDEADPKQGKISIESPIARALIGKKVGDTVE
VTTPGGEYEYEILSVEY
>gnl|CDD|178937 PRK00227, glnD [protein-PII] uridylyltransferase
MNTPAQLREDAEASALALLGSLQLPPGTALAATGSLARREMTPYSDLDLILLHPPGATPDGVEDLWYPIW
DAKKRLDYSVRTPQECAAMISADSTAALALLDLRFVAGDEQLTASTRAKILEKWRRELNKNFDAVVDTAI
ARWRRSGSVVAMTRPDLKHGRGGLRDIELIRALALGHLCDAPPLDSQHQLLLDVRTLLHVHARRARDVLD
PEFAVDIALDLGFVDRYHLSREIADAARAIDDALTAALATARGALPRRTAFRNAVRRPLDVDVVDANGTI
ALSRTPDLDDPALPLRVAAAAARTGLPVSESVWKRLEECPELPEPWPASAAGDFFRLLSSPVNSRRVIKQ
MDRHGLWERIVPEWDRIRGLMPREPSHIHTIDEHSLNTVANCALETVTVARPDLLLLGALYHDIGKGYPR
PHEQVGAEMVARAARRMGLNLRDRAVVQTLVAEHTTLARIAGRLDPTSEEAVDKLLDAVRYDLLTLNLLE
VLTEADAEGTGPGVWTARLEQGLRIVCSRARARLTDIRPVAPMFAARSDIGLVEEDGFFTVIWHGDYPRE
LVRVLALIAAKGWNILSARMVANGPWSAEFDVRANGPQDFDPQEFLQAYKSGVYSELPDPAPGITATFWH
GNILEVRTEDRRGALGALLGVLPDLLWITASTPGATMIVQAALKPGFDRATVERDVTRVLAGG
>gnl|CDD|234694 PRK00228, PRK00228, YqgE/AlgH family protein
MMKPPEPMNLQGQLLIAMPDLQDPNFARSVIYICEHNENGAMGLVINRPSELDVAEVLPQLDILATPPEI
RLDQPVFLGGPVQTDRGFVLHSPRDGFDSSIRVSDGLVLTTSRDVLEALATGPGPEGVLVALGYAGWGAG
QLEQEIEENAWLTAPADPEILFDTPPEDRWRAALRRLGIDLALLSTQAGHA
>gnl|CDD|234695 PRK00230, PRK00230, orotidine-5'-phosphate decarboxylase
MDDRLIVALDFPSKEEALAFLDQLDPAVLFVKVGMELFTAGGPQFVRELKQRGFKVFLDLKLHDIPNTVA
KAVRALAKLGVDMVNVHASGGPRMMKAAREALEPKSRPLLIAVTVLTSMDEEDLAELGINLSLEEQVLRL
AKLAQEAGLDGVVCSAQEAAAIREATGPDFLLVTPGIRPAGSDAGDQKRVMTPAQAIAAGSDYIVVGRPI
TQAADPAAAYEAILAEIAGA
>gnl|CDD|234696 PRK00232, pdxA, 4-hydroxythreonine-4-phosphate dehydrogenase; Reviewed
MMMKPRIAITPGDPAGIGPELVAKLLAQPDVRWPAELVVIADRALLERRAAILGLPLDLRPYSPDAPAQP
QEAGTLTVLPVPLAPAVVAGQLDAANGRYVLETLARALDGCLAGEFDAICTAPVNKGAINDAGIPFSGHT
EFFAELSGTTGVVMMLATEGLRVALVTTHLPLRDVADAITPERLEEVIRILHADLRRKGIAEPRIAVCGL
NPHAGEGGHFGREEIDIIIPALEELRAEGINLVGPLPADTLFQPAYLGDADAVLAMYHDQGLPVLKYLGF
GRGVNITLGLPFIRTSVDHGTALDLAGKGIADVGSFITALNLAIRMAANRRE
>gnl|CDD|234697 PRK00235, cobS, cobalamin synthase; Reviewed
REMLRLFLAALSFLTRLPVPGSVGGDPEDLRRAARAFPLVGLLLGALAALVYWLLQLGLPPLLAALLAVA
ALLLLTGGLHLDGLADTADGLGGGRDRERRLEIMKDSRIGTFGVLALVLVLLLKILALAALRPAGALAAL
ILAPAASRAAAVLLIARLPYARPEGLGAPFAGKLSGRQLLLALALGLALLLPLLGGWAGLLALLVALVAA
FLLGRLFVRRLGGQTGDTLGAAQELTELAFLLALALVLS
>gnl|CDD|234698 PRK00236, xerC, site-specific tyrosine recombinase XerC; Reviewed
MADADLPAALEAFLEYLRVERGLSPHTLRAYRRDLRAFLAFLEEHGISSLQDLDAADLRSFLARRRRQGL
SARSLARRLSALRSFYRWLVRRGLLKANPAAGLRAPKIPKRLPKPLDVDQAKRLLDAIDEDDPLALRDRA
ILELLYGSGLRLSELVGLDIDDLDLASGTLRVLGKGNKERTVPLGRAAREALEAYLALRPLFLPDDDALF
LGARGGRLSPRVVQRRVKKLGKKAGLPSHITPHKLRHSFATHLLESGGDLRAVQELLGHASLSTTQIYTH
VDFQHLAEVYDAAHPRA
>gnl|CDD|234699 PRK00241, nudC, NAD(+) diphosphatase
RWMRRDLEALDAGWWVVSHEQQLWLPDGELPFGAAANLDLPGLRALQIGEWQGEPVWLVRQDPLRGHEMG
SLRQLLDLDDGLFQLLGRAVQLAEFYRSHRFCGYCGHPMHPSKTEWAMLCPHCRERYYPRIAPCIIVAVR
RGDEILLARHPRHRNGVYTVLAGFVEVGETLEQCVAREVMEESGIKVKNLRYVGSQPWPFPHSLMLGFHA
DYDSGEIVFDPKEIADAQWFRYDELPLLPPSGTIARRLIEDTVALC
>gnl|CDD|178945 PRK00247, PRK00247, putative inner membrane protein translocase component YidC; Validated
MLDIFIYPVSGVMKLWHLLLHNVLGLDDSLAWFASLFGLVITVRAIIAPFTWQQYKSGRTAAHIRPKRKA
LREEYKGKTDEASIRELQQKQKDLNKEYGYNPLAGCVPALIQIPVFLGLYQVLLRMARPEGGLENPVHQP
IGFLTSEEVESFLQGRVFNVPLPAYVSMPAEQLAYLGTTQATVLAFVLPLFIAAAVFTAINMAMSTYRSF
QTNDHDSGFAVGMLKFLIVMAILAPIFPLSLGLTGPFPTAIALYWVANNLWTLIQNIIMYLILERKYPLT
DEFKEHHAEQRAQYREKQKEKKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKTRTAEKNEAKARKKEI
AQKRRAAEREINREARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESKGSPPQVEATTTAE
PNREPSQED
>gnl|CDD|234700 PRK00249, flgH, flagellar basal body L-ring protein FlgH
LLLLLLLAGCASIPRLPLVGGAPAAAPVEAPTPLPNPAPNGSIFQAGSLWNYGYQPLFKDRRARNVGDIL
TVVLQENTSASKSNSTNRSRDSSTNFGLPSLFGYLNGLDANASLETSSDNSFKGKGSASRSNTLTGTITV
TVTQVLPNGNLVIRGEKEVRVNQGTEFLRVSGVVRPRDISGDNTISSTRIADARISYGGRGYISDAQQPG
WLQRFFDSLSPF
>gnl|CDD|178948 PRK00253, fliE, flagellar hook-basal body protein FliE; Reviewed
MMDIQGIEGVLSQLQATAMEASGQAKPAQGAAVGTADFAGQLKAALDKVNDTQQAARTLAEKFELGDPGV
SLNDVMIALQKASVSFQAGIQVRNKLVAAYQEIMNMQV
>gnl|CDD|234702 PRK00254, PRK00254, ski2-like helicase; Provisional
MKVDELRVDERIKRVLKERGIEELYPPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGGK
AVYLVPLKALAEEKYREFKDWEKLGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRHGSSWIKDVK
LVVADEIHLIGSYDRGATLEMILTHMLGRAQILGLSATVGNAEELAEWLNAELVVSDWRPVKLRKGVFYQ
GFLFWEDGKIERFPNSWESLVYDAVKKGKGALVFVNTRRSAEKEALELAKKIKRFLTKPELRALKELADS
LEENPTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRY
SNFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEPSKLMERYIFGKPEKLFSMLSNESAFRSQVL
ALITNFGVSNFKELVNFLERTFYAHQRKDLYSLEEKAKEIVYFLLENEFIDIDLEDRFIPLPLGIRTSQL
YIDPLTAKKFKDAFPKIEKNPNPLGIFQLIASTPDMTPLNYSRKEMEDLLDEAYEMEDRLYFNIPYWEDY
KFQKFLRAFKTAKVLLDWINEVPEGEIVETYNIDPGDLYRILELADWLMYSLIELYKLFEPKQEVLDYLE
TLHLRVKHGVREELLELMRLPMIGRKRARALYNAGFRSIEDIVNAKPSELLKVEGIGAKIVEGIFKHLGV
EKEVKIKKKPRKGTLDYFLK
>gnl|CDD|166874 PRK00257, PRK00257, 4-phosphoerythronate dehydrogenase PdxB
MKIVADENIPLLDAFFAGFGEIRRLPGRAFDRAAVRDADVLLVRSVTRVDRALLEGSRVRFVGTCTIGTD
HLDLDYFAEAGITWSSAPGCNARGVVDYVLGSLLTLAEREGVDLAERTYGVVGAGHVGGRLVRVLRGLGW
KVLVCDPPRQEAEGDGDFVSLERILEECDVISLHTPLTKEGEHPTRHLLDEAFLASLRPGAWLINASRGA
VVDNQALREALLSGEDLDAVLDVWEGEPQIDLELADLCTIATPHIAGYSLDGKARGTAQIYQALCRFFGI
PARVSLTDLLPPPWLAQIDLDASADPAWALATLCRAVYDPRRDDAAFRRSLTGDVAQQRAAFDALRKHYP
LRREIEGLRVRLTGESPELAQLVRALGAQLV
>gnl|CDD|234703 PRK00258, aroE, shikimate 5-dehydrogenase; Reviewed
ITGKTRLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVPPEDLEDAVKGFFALGGRGANVTVPFKE
AAFALADELSERARLIGAVNTLVLEDGRLIGDNTDGIGFVRALEERLGVDLKGKRILILGAGGAARAVIL
PLLDLGVAEITIVNRTVERAEELAKLFGALGKAELDLELQEELADFDLIINATSAGMSGELPLPPLPLSL
LRPGTIVYDMIYGPLPTPFLAWAKAQGARTIDGLGMLVHQAAEAFELWTGVRPPVEPMLAALRAALAA
>gnl|CDD|234704 PRK00259, PRK00259, intracellular septation protein A; Reviewed
MKQLLDFLPLILFFAAYKLYGIYAATAALIVATVIQLAISWIRYRKVEKMQLISLVVVVVFGGLTLVFHD
DTFIKWKPTIIYWLFALALLGSQFIFKKPLIKRMLGKELTLPDPVWRKLNLAWALFFIFCGLLNLYVARN
FSTDTWVNFKVFGLTGLTLVFTLLQGPYLYRHLPEEDKS
>gnl|CDD|234709 PRK00275, glnD, PII uridylyl-transferase; Provisional
MPQVDPELFDRGQFQAELALKASPIAAFKKAIRQAREVLDERFRSGRDIRRLIEDRAWFVDQILQQAWHQ
FDWSDDADIALVAVGGYGRGELHPYSDIDLLILLDSADHEEFREPIERFLTLLWDIGLEIGQSVRSVDEC
AEEARADLTVITNLMESRTIAGPESLRQRMLEVTSSEHMWPSKEFFLAKRAEQKARHHKYNDTEYNLEPN
VKGSPGGLRDIQTILWVAKRQFGTLNLHALVGEGFLTESEYGLLASGQEFLWKVRYALHMLAGRAEDRLL
FDHQRSIATLLGYEDSDAKLAVEQFMQKYYRVVMALAELNDLILQHFEEVILAADDSGTIQPLNSRFQLR
DGYIEATHPNVFKRTPFALLEIFVLMAQHPEIKGVRADTIRLLREHRHLIDDAFRNDIRNTSLFIELFKC
PIGIHRNLRRMNRYGILGRYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKNLRKLRYPEVSEKFPLASKL
MGRLPKPELLYIAGLYHDIGKGRGGDHSELGAVDAEAFCQRHQLPAWDTRLVVWLVENHLLMSTTAQRKD
LSDPQVIHDFALKVGDQTHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREE
QIRQTQSAALDILVRKGTDPDDAEQLWSQLGDDYFLRHTAGDIAWHTEAILQHPDDGGPLVLIKETTQRE
FEGGTQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDDDGEPIGDNPARIEQIR
EGLTEALRNPDDYPTIIQRRVPRQLKHFAFPTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDL
SLQNAKIATLGERVEDVFFITDADNQPLSDPQLCSRLQDAICEQLDARNEKDTSP
>gnl|CDD|178954 PRK00276, infA, translation initiation factor IF-1; Validated
MAKEDVIEMEGTVVEALPNAMFRVELENGHEVLAHISGKMRKNYIRILPGDKVTVELSPYDLTKGRITYR
HK
>gnl|CDD|178955 PRK00277, clpP, ATP-dependent Clp protease proteolytic subunit; Reviewed
MPIMMNLVPMVIEQTSRGERSYDIYSRLLKERIIFLGGEVEDHMANLIVAQLLFLEAEDPDKDIYLYINS
PGGSVTAGLAIYDTMQFIKPDVSTICIGQAASMGAFLLAAGAKGKRFALPNSRIMIHQPLGGFQGQATDI
EIHAREILKLKKRLNEILAEHTGQPLEKIEKDTDRDNFMSAEEAKEYGLIDEVLTKRKEA
>gnl|CDD|234710 PRK00278, trpC, indole-3-glycerol phosphate synthase TrpC
MMDILDKIVAYKREEVAARKAQVPLAELKARAAAAPPPRDFAAALRAGKPAVIAEVKKASPSKGVIREDF
DPVEIAKAYEAGGAACLSVLTDERFFQGSLEYLRAARAAVSLPVLRKDFIIDPYQIYEARAAGADAILLI
VAALDDEQLKELLDYAHSLGLDVLVEVHDEEELERALKLGAPLIGINNRNLKTFEVDLETTERLAPLIPS
DRLVVSESGIFTPEDLKRLAKAGADAVLVGESLMRADDPGAALRELLGAK
>gnl|CDD|234711 PRK00279, adk, adenylate kinase; Reviewed
MRLILLGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAGTELGKEAKSYMDAGELVPDEIVIGLVKE
RLAQPDCKNGFLLDGFPRTIPQAEALDEMLKELGIKLDAVIEIDVPDEELVERLSGRRICPACGRTYHVK
FNPPKVEGKCDVCGEELIQRADDNEETVRKRLEVYHKQTAPLIDYYKKKGKLKKIDGTGSIDEVFADILK
ALGKL
>gnl|CDD|234712 PRK00281, PRK00281, undecaprenyl-diphosphate phosphatase
DMMDLLKAIILGIVEGLTEFLPISSTGHLILVGHLLGFEDDFGKTFDVVIQLGAILAVVVYFRRRLWRLL
GGSGKGGRGDREDRRLLLLVIVATIPAGVLGLLFKDFIKEHLFSPIVVAIALIVGGILLLWAEKRKGPRV
RSLDDLTYKDALLIGLAQCLALIPGTSRSGATISGGLLLGLSREAAAEFSFLLAIPAMLGASLLDLLKLF
HLLSAADLPLLAVGFVVAFVVALIAIKWLLKYIKRHSFTPFAIYRIILGALLLILLFT
>gnl|CDD|234713 PRK00283, xerD, tyrosine recombinase
MMMADRALIEQFLDALWVERGLAENTLSSYRRDLELFAEWLAARGLSLAEATRDDLQAFLAELAEGGYKA
TSSARRLSALRRFFQFLLREGLREDDPSALLDSPKLPRRLPKTLSEAQVEALLDAPDIDTPLGLRDRAML
ELLYATGLRVSELVGLTLDDVSLRQGVVRVTGKGNKERLVPLGEEAVYAIERYLERGRPALLNGRSSDAL
FPSARGGQLTRQTFWHRIKHYAKRAGIDPKKLSPHVLRHAFATHLLNHGADLRVVQELLGHSDISTTQIY
THVATERLKELHAQHHPRA
>gnl|CDD|178960 PRK00284, pqqA, pyrroloquinoline quinone precursor peptide PqqA
AWTKPAYTELRVGMEVTMYFSAR
>gnl|CDD|178961 PRK00285, ihfA, integration host factor subunit alpha; Reviewed
MTLTKADLAEALFEKVGLSKREAKELVELFFEEIRDALENGEQVKLSGFGNFQLRDKNQRPGRNPKTGEE
IPISARRVVTFRPSQKLKSRVENAAPKKQ
>gnl|CDD|234715 PRK00290, dnaK, molecular chaperone DnaK; Provisional
MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIK
RLMGRRDEEVQKDIKLVPYKIVKADNGDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITV
PAYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKKGDEKILVYDLGGGTFDVSILEIGDGVFE
VLSTNGDTHLGGDDFDQRIIDYLADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFIT
ADASGPKHLEIKLTRAKFEELTEDLVERTIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF
GKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFS
TAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGKEQ
SITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKIEA
AIKELKEALKGEDKEAIKAKTEELTQASQKLGEAMYQQAQAAQGAAGAAAKDDDVVDAEFEEVKDDK
>gnl|CDD|234716 PRK00292, glk, glucokinase; Provisional
MKPALVGDIGGTNARFALCDWANGEIEQIKTYATADYPSLEDAIRAYLADEHGVQVRSACFAIAGPVDGD
EVRMTNHHWAFSIAAMKQELGLDHLLLINDFTAQALAIPRLGEEDLVQIGGGEPVPGAPIAVIGPGTGLG
VAGLVPVDGRWIVLPGEGGHVDFAPRSEEEAQILQYLRAEFGHVSAERVLSGPGLVNLYRAICKADGREP
ELLTPADITERALAGSCPLCRRTLSLFCVILGRVAGNLALTLGARGGVYIAGGIVPRFLEFFKASGFRAA
FEDKGRFSAYLADIPVYVITHPQPGLLGAGAYLRQA
>gnl|CDD|234717 PRK00293, dipZ, thiol:disulfide interchange protein precursor; Provisional
MKRLLTLILLLCSTLAFASAGLFDAPGRSDFLPVDQAFAFDFQQQGDQLNLRWQIADGYYLYRKQIKITP
EPADLGEPQLPAGEPHEDEFFGEVEVYRDRLDLPVPLNQAAAGATLTVTYQGCADAGFCYPPETRTVPLS
AVAANSAPAPAPAPAGQATASLASLPWSLLWFFLIGIGLAFTPCVLPMYPILSGIVLGGKQRLSTARALL
LSFVYVQGMALTYTLLGLVVAAAGLQFQAALQHPYVLIGLSILFVLLALSMFGLFTLQLPSSLQTRLTLL
SNRQQGGSLGGVFVMGAISGLICSPCTTAPLSGALLYIAQSGDLLLGGLTLYLLALGMGLPLILITTFGN
KLLPKSGPWMNQVKTAFGFVLLALPVFLLERVLPGVWGLRLWSLLGVAFFGWAFIQSLKAKRGWMRLLGQ
ILLLAALLASVRPLQDWAFGGAAAGAQTQAHLNFQRIKTVAELDQALAEAKGKGKPVMLDLYADWCVACK
EFEKYTFSDPQVQQALADTVLLQADVTANNAEDVALLKHYNVLGLPTILFFDAQGQEIPDARVTGFMDAA
AFAAHLRQLQP
>gnl|CDD|166894 PRK00294, hscB, co-chaperone HscB; Provisional
MGTPCHFALFDLQPSFRLDLDQLATRYRELAREVHPDRFADAPEREQRLALERSASLNEAYQTLKSPPRR
ARYLLALSGHEVPLEVTVHDPEFLLQQMQLREELEELQDEADLAGVATFKRRLKAAQDELNESFAACWDD
AARREEAERLMRRMQFLDKLAQEVRQLEERLDD
>gnl|CDD|166895 PRK00295, PRK00295, hypothetical protein; Provisional
MSLEERVTELESRQAFQDDTIQALNDVLVEQQRVIERLQLQMAALIKRQEEMVGQFGSFEEEAPPPHY
>gnl|CDD|234718 PRK00296, minE, cell division topological specificity factor MinE; Reviewed
MSLLDFFRSRKKSTANVAKERLQIIVAHERSSRGEPDYLPQLRKEILEVIAKYVQIDPDKVSVQLDKDGD
ISTLELNVTLPEAEEK
>gnl|CDD|178967 PRK00299, PRK00299, sulfurtransferase TusA
MTDLFSSPDHTLDALGLRCPEPVMMVRKTVRNMQPGETLLIIADDPATTRDIPSFCRFMDHELLAQETEQ
LPYRYLIRKGL
>gnl|CDD|234719 PRK00300, gmk, guanylate kinase; Provisional
MMRRGLLIVLSGPSGAGKSTLVKALLERDPNLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEF
LEWAEVFGNYYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTD
SEEVIARRLAKAREEIAHASEYDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELIEELLA
>gnl|CDD|234721 PRK00302, lnt, apolipoprotein N-acyltransferase; Reviewed
LLLRGWLRLLLALLAGALGTLAFAPFDLWPLALLSLAGLLWLLLGASPKQAALIGFLWGFGYFGSGLSWI
YVSIHTFGGMPAWLAPLLVLLLAAYLALYPALFAALWRRLWPKSGLRRALALPALWVLTEWLRGWLLTGF
PWLALGYSQIPDGPLAQLAPIFGVYGLSFLVVLVNALLALALIKRRWRLALLALLLLLLAALGYGLRRLQ
WTTPAPEPALKVALVQGNIPQSLKWDPAGLEATLQKYLDLSRPALGPADLIIWPETAIPFLLEDLPQAFL
KALDDLAREKGSALITGAPRAENKQGRYDYYNSIYVLGPYGILNRYDKHHLVPFGEYVPLESLLRPLAPF
FNLPMGDFSRGPYVQPPLLAKGLKLAPLICYEIIFPEEVRANVRQGADLLLNISNDAWFGDSIGPYQHFQ
MARMRALELGRPLIRATNTGITAVIDPLGRIIAQLPQFTEGVLDGTVPPTTGLTPYARWGDWPLLLLALL
LLLLALLLALRRRRK
>gnl|CDD|166901 PRK00304, PRK00304, hypothetical protein; Provisional
MLIPYDQLEADTLTRLIEDFVTRDGTDNGDETPLETRVLRVRQALTKGQAVILFDPESQQCQLMLKHDVP
RELLD
>gnl|CDD|234723 PRK00311, panB, 3-methyl-2-oxobutanoate hydroxymethyltransferase; Reviewed
RVTISDLQKMKQEGEKIVMLTAYDYPFAKLFDEAGVDVILVGDSLGMVVLGYDSTLPVTLDDMIYHTKAV
ARGAPRALVVADMPFGSYQASPEQALRNAGRLMKEAGAHAVKLEGGEEVAETIKRLVERGIPVMGHLGLT
PQSVNVLGGYKVQGRDEEAAEKLLEDAKALEEAGAFALVLECVPAELAKEITEALSIPTIGIGAGPDCDG
QVLVWHDMLGLFSGFKPKFVKRYADLAGSIREAVKAYVAEVKSGSFPGEEHSFK
>gnl|CDD|178974 PRK00312, pcm, protein-L-isoaspartate(D-aspartate) O-methyltransferase
ARLMESERFARLVLRLRAEGILDERVLEAIEATPRELFVPEAFKHKAYENRALPIGCGQTISQPYMVARM
TELLELKPGDRVLEIGTGSGYQAAVLAHLVRRVFSVERIKTLQWEAKRRLKQLGLHNVSVRHGDGWKGWP
AYAPFDRILVTAAAPEIPRALLEQLKEGGILVAPVGGEEQQLLTRVRKRGGRFEREVLEEVRFVPLVKGE
LA
>gnl|CDD|234724 PRK00315, PRK00315, potassium-transporting ATPase subunit KdpC
MMSLLRPALVLFVFLTLITGVAYPLLTTGIGQAAFPWQANGSLIRKDGKVVGSALIGQNFTGPGYFHGRP
SATAPMPYNPQASGGSNLAPSNPALDDAIKARVAALRAANPGASSPVPVDLVTASGSGLDPHISPAAAAY
QIPRVAAARQLPVEQVAQLVAAYTQGPLFGFLGEPVVNVLELNLALDALQEAK
>gnl|CDD|234725 PRK00317, mobA, molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
MPPITGVILAGGRSRRMGGVDKGLQELNGKPLIQHVIERLAPQVDEIVINANRNLARYAAFGLPVIPDSL
ADFPGPLAGILAGLKQARTEWVLVVPCDTPFIPPDLVARLAQAAGKDDADVAWAHDGGRLHPTFALYSVA
LLPDLEAYLAAGERKVMAFYARHGGVAVDFSDPKDAFFNINTPEDLAQLEELL
>gnl|CDD|234726 PRK00321, rdgC, recombination associated protein; Reviewed
MWFKNLTVYRLTRPWSLDAEELEEQLAKFAFTPCGSQDMSSFGWVSPLGRESDPLVHSVNGQILLCLRKE
EKILPASVIKQALEEKVAEIEAEEGRKLGKKEKDELKEEVTHELLPRAFSRRSQTFAWIDPVNGLIVVDA
ASAKKAEDVLALLRKSLGSLPVVPLSTEQSPEATMTEWLASGEAPAGFTLDDECELKSALEDGAVVRCKR
QDLDSDEIRQHIEAGKQVTKLALTWQDRLSFVLTDDLTIKRLKFLDVLREQNDDIDGEDAAARFDADFAL
MTGELARLIPDLIEALGGEAERA
>gnl|CDD|234727 PRK00325, algL, polysaccharide lyase
MRRLAAPTLLALALLAGSAAAAAPLVPPQGYYAPVEKLKTGDGAFACPAVPPPYTGSLQFRSKYEGSDAA
RATLNPAAEKAFRDQTADITRFEKGLAKMVDQYMRSGRPGDLACALSWLDAWARADALLSKDANHTGKSM
RKWALGAMAGAYLRSTSRPLAAHQAQSRAIEAWLAKLADQVVADWDNLPLEKINNHSYWAAWAVMATGVA
TDRRDLFDWAVKEYRVGINQIDDDGFLPNEMKRGQRALAYHNYALPPLVMIAEFAQANGVDLYEENNGAL
QRLAERVAAGVRDPGTFEERTGVQQDMTPLKVDWKLAWLEPYCALYSCDPRLLELKHARQPFKSFRLGGD
LTRVYDPEG
>gnl|CDD|234728 PRK00326, PRK00326, transcriptional regulator MraZ
MFRGEYAHNLDAKGRLSIPAKFRDELGEEADGRLVITKGLDGCLLLYPLPEWEKIEEKLAALPLTNPEAR
AFQRLLLGGAVEVELDKQGRILIPPNLREYAGLEKEVVLVGQGNKFEIWDPEAWEAYLAEAEEDFADDL
>gnl|CDD|178979 PRK00329, PRK00329, GIY-YIG nuclease superfamily protein; Validated
MAEMKPWFLYLLRCADGSLYTGITTDVERRFAQHQSGKGAKYTRGRPPLTLVFVEPVGDRSEALRAEYRF
KQLTKKQKERLVAEGE
>gnl|CDD|234729 PRK00331, PRK00331, isomerizing glutamine--fructose-6-phosphate transaminase
MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIG
HTRWATHGKPTERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEG
GDLLEAVRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLED
GEIAVLTRDGVEIFDFDGNPVEREVYTVDWDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDELGEGE
LADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETA
DTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVLYLLALALAKARG
TLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEGALKLKEISYIH
AEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEVAEEADDVIEV
PEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE
>gnl|CDD|166914 PRK00341, PRK00341, DUF493 domain-containing protein
MTDPDVKSPKIEFPCEDYPIKVIGDTGVGFKDLVIEILQKHADVDLSTLAERQSSNGKYTTVQLHIVATD
EDQLQDINSALRATGRVHMVL
>gnl|CDD|234732 PRK00346, surE, 5'(3')-nucleotidase/polyphosphatase; Provisional
MRILLTNDDGIHAPGIRALAEALRELADVTVVAPDRERSGASHSLTLTRPLRVEKVDNGFYAVDGTPTDC
VHLALNGLLDPKPDLVVSGINHGANLGDDVLYSGTVAAAMEGALLGIPAIAVSLAVSEGSRGWRDFETAA
KVARELVRKLLEKPLPPGTLLNVNVPDLPPEEIKGIRVTRLGKRHYAEEVIKRVDPRGRPYYWIGGAGLE
EDAGEGTDFHAVAEGYVSITPLQLDLTAYAALDELKDWLL
>gnl|CDD|234734 PRK00349, uvrA, excinuclease ABC subunit UvrA
MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQM
DKPDVDSIEGLSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDR
VLELPEGTRLQILAPVVRGRKGEHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLV
VKEDIRQRLADSIETALKLSDGLVVVEVMDDPEAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACP
TCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSSSYYFQMLKSLAEHYGFDLDTPWKDLPEEVQDII
LYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREELEKYMSERPCPSCKGKRLKPE
ALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDYLTLSRSAGTL
SGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYI
VDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDV
EIPLGKFTCVTGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRS
NPATYTGVFDPIRELFAGTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGK
RYNRETLEVKYKGKNIADVLDMTVEEALEFFEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVK
LAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGG
DGGGEIVATGTPEEVAKVEASYTGRYLKPVLER
>gnl|CDD|178985 PRK00357, rpsS, 30S ribosomal protein S19; Reviewed
MARSLKKGPFVDGHLLKKVEKANESGDKKVIKTWSRRSTILPEFVGLTIAVHNGRKHVPVYVTENMVGHK
LGEFAPTRTFRGHAADKKAKRK
>gnl|CDD|178988 PRK00364, groES, co-chaperonin GroES; Reviewed
MNLKPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRLDNGERVPLDVKVGDKVLFGKY
AGTEVKIDGEEYLILRESDILAIVE
>gnl|CDD|234737 PRK00366, ispG, flavodoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase
MRPSTPIPRRKTRQVKVGNVPIGGDAPIVVQSMTNTDTADVEATVAQIKRLARAGCEIVRVAVPDMEAAA
ALPEIKKQLPVPLVADIHFDYRLALAAAEAGADALRINPGNIGKRDERVREVVEAAKDYGIPIRIGVNAG
SLEKDLLEKYGEPTPEALVESALRHAKILEELGFDDIKISVKASDVQDLIAAYRLLAKRCDYPLHLGVTE
AGMGFKGTVKSAAGLGALLQEGIGDTIRVSLTADPVEEVKVGQEILQSLGLRSRGPEVISCPTCGRTEFD
VIQELAEVEQRLEHIKMPLKVAVMGCVVNGPGEAKEADIGIAGGNPKGPVFVDGEKIKTLPEENIVEELE
AEIEAYAEER
>gnl|CDD|234738 PRK00369, pyrC, dihydroorotase; Provisional
MILWIKGKAYLGKEIKEICINFDRRIKEIKSRCKPDLDLPQGTLILPGAIDLHVHLRGLKLSYKEDVASG
TSEAAYGGVTLVADMPNTIPPLNTPEAITEKLAELEYYSRVDYFVYSGVTKDPEKVDKLPIAGYKIFPED
LEREETFRVLLKSRKLKILHPEVPLALKSNRKLRRNCWYEIAALYYVKDYQNVHITHASNPRTVRLAKEL
GFTVDITPHHLLVNGEKDCLTKVNPPIRDINERLWLLQALSEVDAIASDHAPHSSFEKLQPYEVCPPGIA
ALSFTPPFIYTLVSKGILSIDRAVELISTNPARILGIPYGEIKEGYRANFTVIQFEDWRYSTKYSKVIET
PLDGFELKASVYATIVQGKLAYLEGEVFPVKGINPFGERKRS
>gnl|CDD|178991 PRK00373, PRK00373, V-type ATP synthase subunit D; Reviewed
MARLNVKPTRMELINLKRRLKLAERGHKLLKDKRDELIMEFFDILDEAKKLREEVEEELEEAYKDFLMAR
AVEGSLAVEEAAASPKESLEVDVSSKNIMGVVVPVIELSVKRTLPERGYGFLGTSAELDEAAEKFEELLE
KILELAEVEKTIQLLADEIEKTKRRVNALEYVIIPRLEETIKYIKMKLDEMERENFVRLKKIKS
>gnl|CDD|234740 PRK00377, cbiT, cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
MEWKYVIPGIPDEEFERDEEIPMTKEEIRALALSKLRLRKGDMILDIGCGTGSVTVEASLLVGETGKVYA
VDKDEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTINEKFDRIFIGGGSEKLKEIISASWEIIKKGGR
IVIDAILLETVNNALSALENIGFNLEITEVIIAKGMKTKVGTAMMTRNPIFIISGEKQ
>gnl|CDD|178993 PRK00378, PRK00378, nucleoid-associated protein NdpA; Validated
MSLDINQIILHQLIKRDEQPLELVLRDSLLANSAAVENMLAELHRVYNAKAKAYGLFSEESEFAQALREY
REGELDFLAFSRAATGRLRDELAKYPFAEGGFLLFCHYQYLATDYLLIALLNSSESMRVNEELDISPTHY
LDINQADIAARIDLTEWETNPESNRYLSFIKGRVGRKVADFFMDFLGAEEGLNTKAQNRTLLQAVSDFCA
SADLDKEERQEVRKQVYDYCNEQLKAGEEIELEELSEELPELGEKSFYDFAREQGYELEESFPADRSTLR
QLTKFSGSGGGLTISFDAHLLGERIFYDPATDTLTIKGTPPNLRDQLQRRLKGE
>gnl|CDD|234742 PRK00389, gcvT, glycine cleavage system aminomethyltransferase GcvT
MLKRTPLYDLHVALGAKMVDFGGWEMPVQYGSIIEEHHAVRTDAGLFDVSHMGEVDVTGPDALAFLQYLL
ANDVSKLKPGKAQYTCMLNEDGGVIDDLIVYKLSEDEYLLVVNAANREKDLAWIKSHAAGFGVEVTDRSD
DLAMIAVQGPKAREKLQKLTDADLSELKPFFGAQGAEVGGGDVLVARTGYTGEDGFEIYLPAEDAEALWD
ALLEAGVKPCGLGARDTLRLEAGMPLYGQDMDETITPLEAGLGWTVKLEEKRDFIGREALEAQKEAGVER
KLVGLELEERGIPRHGYPVLADGEEIGEVTSGTFSPTLGKSIALAYVPAGVGDEVEVEIRGKQVPAKVVK
PPFVRRGKR
>gnl|CDD|234744 PRK00392, rpoZ, DNA-directed RNA polymerase subunit omega; Reviewed
MARPTIEDLLEKVDNRYELVLLAAKRARQLRAGAKPPVDKSSDKPVVIALREIAEGKVTYEILEEVEIE
>gnl|CDD|234745 PRK00393, ribA, GTP cyclohydrolase II RibA
MQLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQ
LEAALERIAEEGRGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKAL
GVKKVRLLTNNPKKVEALTEAGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLSLD
>gnl|CDD|234746 PRK00394, PRK00394, transcription factor; Reviewed
IKIENIVASTDLGQELDLEKVAEDLPNAEYNPEQFPGLVYRLEDPKIAALIFRSGKVVCTGAKSVEDLHE
AVKIIIKKLKELGIKVIDEPEIKVQNIVASADLGVELNLNAIAIGLGLENIEYEPEQFPGLVYRLDDPKV
VVLLFGSGKLVITGAKSEEDAEKAVEKILEKLEELGLLE
>gnl|CDD|179001 PRK00395, hfq, RNA-binding protein Hfq; Provisional
MAKGQNLQDPFLNALRKERVPVTIYLVNGIKLQGQIESFDNFVVLLRNTGKSQLVYKHAISTVVPARPVS
LHEDEEEEE
>gnl|CDD|234747 PRK00398, rpoP, DNA-directed RNA polymerase subunit P; Provisional
MAEYKCARCGREVELDEYGTGVRCPYCGYRILFKERPPVVKRVKAR
>gnl|CDD|179005 PRK00400, hisE, phosphoribosyl-ATP diphosphatase
MMDTLERLAATIEERKGADPEGSYTAKLLDKGLDKILKKVGEEATEVVIAAKDGDREELVYEIADLLYHL
LVLLAARGISLEDVLAELERREGLSGLEEKASRKI
>gnl|CDD|234748 PRK00402, PRK00402, 3-isopropylmalate dehydratase large subunit; Reviewed
MGMTLAEKILARHSGRDVSPGDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVIVFDHFVPAK
DIKSAEQQKILREFAKEQGIPNFFDVGEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGST
DMAAAMATGKTWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERM
TLANMAIEAGAKAGIFAPDEKTLEYLKERAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVK
PVSEVEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAG
AVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSPESEVYLASPAVAAASAVTGKITDPREVL
>gnl|CDD|234749 PRK00405, rpoB, DNA-directed RNA polymerase subunit beta; Reviewed
MVYSYTGKKRIRKSFGKIKEVLELPNLLEIQLDSFDWFLQLDVPPEDEGLEEVFRSIFPIEDFNGNLSLE
FVSYELGEPKYDVEECKERGLTYSAPLRVKLRLINKETGEIKEQEVYMGDIPLMTENGTFIINGTERVIV
SQLHRSPGVYFDHDKDKTSSGKLLYSARIIPYRGSWLEFEFDPKDILYVRIDRRRKLPVTVLLRALGYSD
EEILDLFYEKEEFGKEIEVPVEYLLGKVLAEDIVDEETGEVLAEANDEITEELDGPYIRNTLEKDPTSSR
EEALVEIYRRLRPGEPPTVEAARSLLENLFFDPKRYDLSKVGRYKLNKKLGLDEDEDVRVLTKEDIIATI
KYLINLRNGKGEVDDIDHLGNRRVRSVGELLQNQFRIGLSRMERAVRERMSLQDLDTLTPQDLINAKPVV
AAIKEFFGSSQLSQFMDQTNPLSELTHKRRLSALGPGGLTRERAGFEVRDVHPTHYGRICPIETPEGPNI
GLINSLATYARVNEYGFIETPYRKVVDGKVTDEIVYLTADEEDNYVIAQANAPLDEDGRFVDELVTARYK
GEFVLVPPEEVDYMDVSPKQVVSVAASLIPFLEHDDANRALMGSNMQRQAVPLLRPEAPLVGTGMERRVA
RDSGAVVVAKRDGVVEYVDASRIVVRVEELDPGEDGVDIYNLIKFQRSNQNTCINQRPIVKVGDRVEKGD
VLADGPSTDNGELALGQNVLVAFMPWNGYNFEDAILISERLVKEDVFTSIHIEEYEIEARDTKLGPEEIT
RDIPNVSEEALRNLDESGIVRIGAEVKPGDILVGKVTPKGETELTPEEKLLRAIFGEKARDVKDTSLRVP
HGEEGTVIDVKVFTRIEQGDELPPGVNKLVKVYIAQKRKIQVGDKMAGRHGNKGVVSRILPVEDMPYLED
GTPVDIVLNPLGVPSRMNIGQILETHLGWAAKGLGIKFATPVFDGAKEEEIKELLEEAGLPEDGKTTLYD
GRTGEPFDRPVTVGYMYMLKLHHLVDDKIHARSTGPYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAA
YTLQEMLTVKSDDVVGRTKVYEAIVKGENIPEPGIPESFNVLVKELQSLGLDVELLDEDGNE
>gnl|CDD|179008 PRK00407, Archease, Archease protein family (MTH1598/TM1083). This archease family of proteins, has two SHS2 domains, with one inserted into another. It is predicted to be an enzyme. It is predicted to act as a chaperone in DNA/RNA metabolism
MRSYEFFEHTADIGIRAYGRTLEEAFENAALAVFDVITDTSKVEPKEEREIEIEGYDLENLLYRWLEELL
YYYDSEGLVFSKFDVKIDEDDMTLKAKAWGEKFDPEIHERRTVVKAMTYHDMEIEKEDGCWMAQFVVDI
>gnl|CDD|234750 PRK00409, PRK00409, recombination and DNA strand exchange inhibitor protein; Reviewed
MQEKTLRVLEFNKIKEQLKTFAASELGKEKVLQLDPETDFEEVEELLEETDEAAKLLRLKGLPPFEGVKD
IDDALKRAEKGGVLSGDELLEIAKTLRYFRQLKRFIEDLEEEEELPILEEWVAKIRTLPELEQEIHNCID
EEGEVKDSASEKLRGIRRQLRRKKSRIREKLESIIRSKSLQKYLQDTIITIRNDRYVLPVKAEYKHAIKG
IVHDQSSSGATLYIEPQSVVELNNEIRELRNKEEQEIERILKELSAKVAKNLDFLKFLNKIFDELDFIFA
RARYAKALKATFPLFNDEGKIDLRQARHPLLDGEKVVPKDISLGFDKTVLVITGPNTGGKTVTLKTLGLA
ALMAKSGLPIPANEPSEIPVFKEIFADIGDEQSIEQSLSTFSGHMTNIVRILEKADKNSLVLFDELGAGT
DPDEGAALAISILEYLRKRGAKIIATTHYKELKALMYNREGVENASVEFDEETLRPTYRLLIGIPGKSNA
FEIAKRLGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKL
QEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQ
KEKQEELKVGDEVKYLSLGQKGEVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKP
RTVSLELDLRGMRYEEALERLDKYLDDALLAGYGEVLIIHGKGTGKLRKGVQEFLKKHPSVKSFRDAPPN
EGGFGVTIVELK
>gnl|CDD|234751 PRK00411, cdc6, ORC1-type DNA replication protein
SLDDIFEDLLMWDETIFKDEEVLEPDYVPENLPHREEQIEELAFALRPALRGSRPLNVLIYGPPGTGKTT
TVKKVFEELEEIAVKVVYVYINCQIDRTRYAIFSEIARQLFGHPPPSSGLSFDELFDKIAEYLDERDRVL
IVALDDINYLFEKEGNDVLYSLLRAHEEYPGARIGVIGISSDLTFLYILDPRVKSVFRPEEIYFPPYTAD
EIFDILKDRVEEGFYPGVVDDEVLDLIADLTAREHGDARVAIDLLRRAGLIAEREGSRKVTEEDVRKAYE
KSEIVHLSEVLRTLPLHEKLLLRAIVRLLKKGGDEVTTGEVYEEYKELCEELGYEPRTHTRFYEYINKLD
MLGIINTRYSGKGGRGRTRLISLSYDPEDVLERLLEDYILKRLK
>gnl|CDD|179012 PRK00414, gmhA, D-sedoheptulose 7-phosphate isomerase
MYQDLIRNELNEAAETLANFLKDDANIHAIQRAAVLIADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRY
RENRPGYPAIAISDVSHLSCVSNDFGYDYVFSRYVEAVGREGDVLLGISTSGNSGNIIKAIEAARAKGMK
VITLTGKDGGKMAGLADIEIRVPHFGYADRIQEIHIKVIHILIQLIEKEMVK
>gnl|CDD|179013 PRK00415, rps27e, 30S ribosomal protein S27e; Reviewed
LIPQPRSRFLKVKCPDCGNEQVVFSHASTVVRCLVCGKTLAEPTGGKAKIKGEILEVLE
>gnl|CDD|234754 PRK00418, PRK00418, DNA gyrase inhibitor YacG
MSETITVNCPTCGKPVEWGEISPFRPFCSKRCQLIDLGEWAAEEKRIPSSGDLSESDDWSEE
>gnl|CDD|234755 PRK00419, PRK00419, DNA primase small subunit PriS
MEERTREYLKSRFRDYYRRAELPLPPDLEKREFGFIPFGEGPSDTMVRHLSFSDLGELRDYLRRTAPRHV
YYSVARYELPSARTMEEKGWLGADLIFDLDADHLPGVRCEEDSYCECLERAKEEALRLLDFLEDDFGFED
IHVVFSGGRGYHVHVRDEDVLELDSDERREIVDYVSGAGLPFEELIREEAVRGTGRPSGWGRRFARRLGY
FIDHLRELALERLEEFDGIGEGTAKKILKAARDNTEFLRKGNLDAFHGIGPRLAARLFAESVRFSKAPID
EPVTIDIKRLIRLPGSLHGKSGLIVTELDRKNLEDFDPLKDAVPPFRGREIKVEYTKPGEVELLGRSFTL
EEGVQSVPEYAAVFLMLRGRAEVGAE
>gnl|CDD|234756 PRK00420, PRK00420, hypothetical protein; Validated
MMESEDIVKKAAELLLKGAKMLSKHCPVCGLPLFELKDGEVVCPVHGKVYIVKSDEEEKKVESKETLKEV
EEVLIEKINYLAKKLKEDEDIERITEIIRYLEVLERIRKIKE
>gnl|CDD|234758 PRK00423, tfb, transcription initiation factor IIB; Reviewed
NLKLVLEEEEKLVCPECGSDKLIYDYERGEIVCADCGLVIEENIIDQGPEWRAFDPEQREKRSRVGAPMT
YTIHDKGLSTDIDWRNKDSYGKSISGKNRAQLYRLRKWQRRIRVSNAAERNLAFALSELDRIASQLGLPR
SVREEAAVIYRKAVEKGLIRGRSIEGVVAAALYAACRRCKVPRTLDEIAEVSRVSRKEIGRCYRFLLREL
NLKLPPTDPIDYVPRFASELGLSGEVQKKAIEILQKAKEKGLTSGKGPTGLAAAAIYIASLLLGERRTQR
EVAEVAGVTEVTVRNRYKELAEKLDIKIPL
>gnl|CDD|179020 PRK00430, fis, DNA-binding transcriptional regulator Fis
QRVNSDVLTVSTVNSQDQVTQKPLRDSVKQALKNYFAQLNGQDVNDLYELVLAEVEAPLLDMVMQYTRGN
QTRAALMLGINRGTLRKKLKKYGMN
>gnl|CDD|234759 PRK00431, PRK00431, ADP-ribose-binding protein
MGMRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPCPTGEAVITSA
GRLPAKYVIHTVGPVWRGGEDNEAELLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKT
VREFLTRHKSPEEVYFVCYDEEAYRLYERLLTQQGDE
>gnl|CDD|234760 PRK00432, PRK00432, 30S ribosomal protein S27ae; Validated
KKMAKREYYEVDGGKVKRKNKFCPRCGSGFMAEHLDRWHCGKCGYTEFKK
>gnl|CDD|179023 PRK00435, ef1B, elongation factor 1-beta; Validated
MGDVLAVLKVMPESPEVDLDELKEKIKEVLPEGYKINGIEEEPIAFGLKALKLYVIMPDEEGGTEPVEEA
FANVEGVESVEVEEVSRI
>gnl|CDD|234762 PRK00439, leuD, 3-isopropylmalate dehydratase small subunit; Reviewed
KGRVWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIA
LKAAGVSAVIAKSFARIFYRNAINIGLPVLECDEAVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPE
FMLEILKAGGLIEYLKKKGRFPG
>gnl|CDD|234763 PRK00440, rfc, replication factor C small subunit; Reviewed
AMMEEIWVEKYRPRTLDEIVGQEEIVERLKSYVKEKNMPHLLFAGPPGTGKTTAALALARELYGEDWREN
FLELNASDERGIDVIRNKIKEFARTAPVGGAPFKIIFLDEADNLTSDAQQALRRTMEMYSQNTRFILSCN
YSSKIIDPIQSRCAVFRFSPLKKEAVAERLRYIAENEGIEITDDALEAIYYVSEGDMRKAINALQAAAAT
GKEVTEEAVYKITGTARPEEIREMIELALNGDFTEAREKLRDLMIDYGLSGEDIIKQIHREVWSLDIPEE
LKVELIDAIGEADFRITEGANERIQLEALLAKLALLGKK
>gnl|CDD|179027 PRK00441, argR, arginine repressor; Provisional
MKVSRHAKILEIINSKEIETQEELAEELKKMGFDVTQATVSRDIKELKLIKVLSNDGKYKYATISKTESN
LSDRLVNIFSNTVISVENVDNMIVIKTISGSASAAAEAIDTLNFDGIAGTIAGDNTIFVLVRSEEKAQEI
VEKIKKLIK
>gnl|CDD|234764 PRK00442, tatA, twin-arginine translocase TatA/TatE family subunit
MGIFDWKHWIVILVVVVLVFGTKKLKNLGSDVGESIKGFRKAMNEDEKEDKPAEQPAPPAQPVPPVQNTA
PLNQPHTIDGQAQKVEEPQRKD
>gnl|CDD|179028 PRK00443, nagB, glucosamine-6-phosphate deaminase; Provisional
MRLIILKTAEEVGKWAARHIANRINAFLPTKERPFVLGLATGSSPLETYKALIELHKAGKVDFSRVTTFN
LDEYVGLPADHPESYRYFMRENFFDHVDIPPENINLLNGNAPDPEAECRRYEEKIKSAGGIDLQILGIGE
NGHIAFNEPGSSFASRTRIKTLTEDTRIANSRFFDGDIEQVPKYALTVGVGTILDAKEIMLLAPGHNKAE
AVKAAVEGPVNHMWPASILQLHPKATLVLDEAAASELKVKTVKYFTELEAE
>gnl|CDD|234765 PRK00446, cyaY, frataxin-like protein; Provisional
MNDSEFHQLADALWQAIEEQLDDDGDADIDCERNGGVLTLTFENGSKIIINRQEPLHELWLAAKSGGFHF
DYKDGEWICDRSGEEFWALLEEAATQQAGEPVSFR
>gnl|CDD|234766 PRK00447, PRK00447, hypothetical protein; Provisional
GMVEVEVEAEVRPTEDEEKVKKAILNFFDFEKFEAEDEGEYKILVGEARTLKSLQKLHRLLRGERILDTA
RKYLMKGIEGNEITFMVHKQAAYVGVLSFVDSDEESPLGPITITIRYKNPQEVIDWLAPRTARGVPLWEN
PIPP
>gnl|CDD|234767 PRK00448, polC, DNA polymerase III PolC; Validated
NEMQEKFKKLLDQINIPDDLQSEALESAEIEKVVVDKKSKKWEFHLKFPNILPIEDFKLFKEKLKQSFSH
IADIKVTFSIEVENITFTEELLLDYWNEIIEKAKKNSPLFKSLLKKQKVEVEGNKLIIKVNNEIERDHLK
KKHLPKLIKQYEKFGFGILKIDFEIDDSKEELEKFEAQKEEEDEKLAKEALEAMKKLEAEKKKQSKNFDP
KEGPVQIGKKIDKEEITPMKEINEEERRVVVEGYVFKVEIKELKSGRHILTFKITDYTSSIIVKKFSRDK
EDLKKFDEIKKGDWVKVRGSVQNDTFTRDLVMNAQDINEIKHPERKDTAEEEKRVELHLHTKMSTMDAIP
SVSELVKRAAKWGHKAIAITDHGVVQAFPEAYNAAKKAGIKVIYGVEANLVDDGVPIVYNEVDRDLKDAT
YVVFDVETTGLSAVYDEIIEIGAVKIKNGEIIDKFEFFIKPGHPLSAFTTELTGITDDMVKDAPSIEEVL
PKFKEFCGDSILVAHNASFDVGFINTNYEKLGLEKIKNPVIDTLELSRFLYPELKSHRLNTLAKKFGVEL
EHHHRADYDAEATAYLLIKFLKDLKEKGITNLDELNKKLGSEDAYKKARPKHATILVKNQVGLKNLFKLV
SLSNTKYFYRVPRIPRSLLDKYREGLLIGSACEEGEVFDAVLQKGDEELEEIAKFYDYIEIQPPANYQHL
IERELVKDEEELKEIIKNLIELGKKLNKPVVATGDVHYLDPEDKIYRKILVASQGGGNPLNRHPLPELHF
RTTDEMLDEFAFLGEELAKEIVVENTNKIADLIEEIEPIKDKLYTPKIEGAEEEIRELTYKKAHEIYGEP
LPEIVEKRIEKELNSIIGNGFAVIYLISQKLVKKSLEDGYLVGSRGSVGSSFVATMIGITEVNPLPPHYV
CPNCKYSEFFTDGSVGSGFDLPDKDCPKCGTKLKKDGHDIPFETFLGFKGDKVPDIDLNFSGEYQPVAHN
YTKVLFGEDHVFRAGTIGTVAEKTAYGYVKKYEEDTGKFYRNAEIDRLAQGCTGVKRTTGQHPGGIIVVP
KYMDIYDFTPIQYPADDVNSEWKTTHFDFHSIHDNLLKLDILGHDDPTMIRMLQDLTGIDPKTIPMDDPK
VMKLFSSTEALGVTPEQIGCETGTLGIPEFGTKFVRQMLEETKPKTFAELVQISGLSHGTDVWLGNAQEL
IKEGIATLSDVIGCRDDIMVYLIHKGLEPKLAFKIMESVRKGKGLTEEEEELMKENNVPDWYIESCKKIK
YMFPKAHAAAYVLMAWRIAYFKVHYPLAYYAAYFSVRADDFDLETMSKGKEAIKAKMKEIKSKGNDASNK
EKDLLTVLEIALEMLERGFKFQKVDLYKSDATEFIIEGDSLIPPFNALPGLGENVAKSIVEAREEGEFLS
KEDLRKRTKVSKTLIEKLDELGVLDDLPETNQLSLFD
>gnl|CDD|234769 PRK00451, PRK00451, aminomethyl-transferring glycine dehydrogenase subunit GcvPA
GMPYIPHTEEDIREMLDAIGVKSIDELFADIPEELRLKRPLDLPPGLSEMELLRHLRELAAKNKTAEEYP
SFLGAGAYDHYIPAVVDHIISRSEFYTAYTPYQPEISQGTLQAIFEYQTMICELTGMDVANASMYDGATA
LAEAALMAVRITKRKKVLVSGAVHPEYREVLKTYLKGQGIEVVEVPYEDGVTDLEALEAAVDDDTAAVVV
QYPNFFGVIEDLEEIAEIAHAGGALFIVGVDPVSLGLLKPPGEYGADIVVGEGQPLGIPLSFGGPYLGFF
ATRKKLVRQMPGRLVGETVDADGKRGFVLTLQAREQHIRREKATSNICTNQALNALAAAIYMSLLGPEGL
RELAEQNHQKAHYLAERLAEIGGVELFDGPFFNEFVVRLPKPAEEVNEALLEKGILGGYDLGRYYPELGN
HLLVCVTEKRTKEDIDALVAALGEVLA
>gnl|CDD|234771 PRK00455, pyrE, orotate phosphoribosyltransferase; Validated
MKMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSGIEFDVVAG
PATGGIPLAAAVARALDLPAIFVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAG
AEVVGVAVIVDRQSAAQEVFADAGVPLISLITLDDLLEYAEEGPLCKEGLPAVKAYRRNYGV
>gnl|CDD|179039 PRK00465, rpmJ, 50S ribosomal protein L36; Reviewed
MKVRASVKKICEKCKVIKRKGVVRVICENPKHKQRQG
>gnl|CDD|166979 PRK00466, PRK00466, acetyl-lysine deacetylase; Validated
MQQEKELVKQKAKELLLDLLSIYTPSGNETNATKFFEKISNELNLKLEILPDSNSFILGEGDILLASHVD
TVPGYIEPKIEGEVIYGRGAVDAKGPLISMIIAAWLLNEKGIKVMVSGLADEESTSIGAKELVSKGFNFK
HIIVGEPSNGTDIVVEYRGSIQLDIMCEGTPEHSSSAKSNLIVDISKKIIEVYKQPENYDKPSIVPTIIR
AGESYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQECGLKIVDETPPVKVSINNPVVKALMRALLKQ
NIKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLEHTNQEKITLDEIYIAVKTYMLAIEELWQKS
>gnl|CDD|179040 PRK00468, PRK00468, KH domain-containing protein
MKELVETIAKALVDNPDAVQVNEIEGEQSVILELKVAPEDMGKVIGKQGRIAKAIRTVVKAAAIKENKRV
VVEII
>gnl|CDD|179041 PRK00474, rps9p, 30S ribosomal protein S9P; Reviewed
MMKVVITSGKRKTAIARATIREGKGRVRINGVPLELIEPELARLKIMEPLILAGEDLRSKVDIDVNVEGG
GIMGQADAARTAIARGLVEWTGDMELKDAFLAYDRTLLVGDPRRTEPKKWGGKGARAKRQKSYR
>gnl|CDD|234775 PRK00476, aspS, aspartyl-tRNA synthetase; Validated
HMMRTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPDAEAFEVAESLRSEYVI
QVTGTVRARPEGTVNPNLPTGEIEVLASELEVLNKSKTLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKN
LKLRSKVTSAIRNFLDDNGFLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVAGFD
RYYQIARCFRDEDLRADRQPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLGVDLPTPFPRMTYAEAM
RRYGSDKPDLRFGLELVDVTDLFKDSGFKVFAGAANDGGRVKAIRVPGGAAQLSRKQIDELTEFAKIYGA
KGLAYIKVNEDGLKGPIAKFLSEEELAALLERTGAKDGDLIFFGADKAKVVNDALGALRLKLGKELGLID
EDKFAFLWVVDFPMFEYDEEEGRWVAAHHPFTMPKDEDLDELETTDPGKARAYAYDLVLNGYELGGGSIR
IHRPEIQEKVFEILGISEEEAEEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFPKTQS
AQDLLTGAPSPVDEKQLRELGIRLRKKE
>gnl|CDD|234776 PRK00478, scpA, segregation and condensation protein ScpA
MIKLIWCEDLNFGIAKNNQIPWKIDEELNHFHQTTTNHTIVMGYNTFQAMNKILANQANIVISKKHQREL
KNNNELFVFNDLKKLLIDFSNVDLFIIGGKKTIEQFIKYADQLIISKLNADYKCDLFVNLNYDDFSLVQT
KEYDQFVVEYWEKKPNTKKPFNVSFKHFSGPLDLLLHLLKDKKMDIMAVDIFEITNQYLAYINKHMNKKA
IELITDYLVITSEILRIKADNLLPNFEDETKLEYDLNNNDERDKIVARLVEYKRYSESLPSFEKLRLNRL
AYFSKENDWDVFILTSNDQLVLLEDPLPNYVSVLKLKHAMNKLFEKLKIKTLTNKNIVIEELSIEQVQNE
ILSIIKQFLYNQVSLKRVLLKINHKISLMYFVTAFVALLVLVNNQKIDLEQKNDDEELYICLLDPTKIVN
SQESPQEMVQRQQEQEQALKESIKQIQEERAISNFQKREEYLKKKYGEYYLSREQYQKLTPEEKINIRIN
QRKIDLIKLDDEQEN
>gnl|CDD|234777 PRK00481, PRK00481, NAD-dependent deacetylase; Provisional
MRIEELAEILDKAKRIVVLTGAGISAESGIPDFRSANGLWEEHRPEDVASPEGFARDPELVWKFYNERRR
QLLDAKPNAAHRALAELEKLGKLVTVITQNIDGLHERAGSKNVIELHGSLLRARCTKCGQTYDLDEYLKP
EPPRCPKCGGILRPDVVLFGEMLPELAIDEAYEALEEADLFIVIGTSLVVYPAAGLPYEAREHGAKTVEI
NLEPTPLDSLFDLVIHGKAGEVVPELVEELLA
>gnl|CDD|234778 PRK00484, lysS, lysyl-tRNA synthetase; Reviewed
EELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVMG
KASFATLQDGSGRIQLYVSKDDVGEEALEAFKKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRP
LPDKFHGLTDVETRYRQRYVDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARP
FITHHNALDIDLYLRIAPELYLKRLIVGGFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMD
LTEELIRHLAQAVLGTTKVTYQGTEIDFGPPFKRLTMVDAIKEYTGVDFDDMTDEEARALAKELGIEVEK
SWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHREDPGLTERFELFIGGREIANAFSELNDPI
DQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFPLMRPE
K
>gnl|CDD|234779 PRK00485, fumC, fumarate hydratase; Reviewed
MMETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKA
DAIVAAADEVIAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSS
NDTFPTAMHIAAVLAIVERLLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEH
GIERIEAALPHLYELALGGTAVGTGLNAHPGFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGA
LKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNDAAVTFA
GSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKELLERSLMLVTALNPHIGYDK
AAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPGK
>gnl|CDD|234783 PRK00504, rpmG, 50S ribosomal protein L33; Validated
MMRKKITLACTECKSRNYTTTKNKKNTPERLELKKFCPRCNKHTLHKETK
>gnl|CDD|234785 PRK00509, PRK00509, argininosuccinate synthase; Provisional
MKKKVVLAYSGGLDTSVIIKWLKETYGCEVIAFTADVGQGEELEPIREKALKSGASEIYVEDLREEFVRD
YVFPAIRANALYEGKYPLGTALARPLIAKKLVEIARKEGADAVAHGCTGKGNDQVRFELGIAALAPDLKV
IAPWREWDLKSREELIAYAEEHGIPIPVTKKSPYSIDANLWHRSIEGGILEDPWNEPPEDVYEWTVSPED
APDEPEYVEIEFEKGVPVAINGEALSPAELIEELNELAGKHGIGRIDIVENRLVGIKSRGVYETPGGTIL
IKAHRALESLTLDREVAHFKDELEPKYAELVYNGLWFSPLREALQAFIDETQEHVTGEVRLKLYKGNAIV
VGRKSPNSLYDEDLATYEEDDVYDQKDAEGFIKLWGLPSKIAALVNKKK
>gnl|CDD|179052 PRK00513, minC, septum formation inhibitor; Reviewed
METMKKQNVTIKGTKDGLTLILDDNCSFDELLQELKEKLSKGKYFWKGKATVHVKVGNRLLDEEQLQELK
DVITERRQTAVAAFESNVITKEEAFSGKEEGETKYLRKTVRSGQVVRVPGNLLIIGDVNPGGEVIAGGNI
IVLGALRGIAHAGATGNKEAVIAALQLEPTQLRIADVIARAPEDKEKPNYPEVAYIKDGGIVVERLQPLK
KIRP
>gnl|CDD|234786 PRK00517, prmA, 50S ribosomal protein L11 methyltransferase
MKWIELTLNTTPEAAEALSDILMELGALAALANLAGLGLDLGEPTYTIEEVEDEDWEREWKKYFHPIRIG
DRLWIVPSWEDPPDPDEINIELDPGMAFGTGTHPTTRLCLEALEKLVLPGKTVLDVGCGSGILAIAAAKL
GAKKVLAVDIDPQAVEAARENAELNGVELNVYLPQGDLKADVIVANILANPLLELAPDLARLLKPGGRLI
LSGILEEQADEVLEAYEEAGFTLDEVLERGEWVALVGKKK
>gnl|CDD|234787 PRK00521, rbfA, 30S ribosome-binding factor RbfA
MMAESQRALRVAEQIQRELAEILQREIKDPRLGMVTVTDVEVSPDLAHAKVYVTVLGDEEDKEEALAALK
KAAGFLRSELGKRLRLRYVPELRFVYDESLEYGNRIDELLRKAKKEDDED
>gnl|CDD|179055 PRK00522, tpx, thiol peroxidase
MATVTFKGNPVTVAGSLPQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFNQE
AAELDNTVVLCISADLPFAQKRFCGAEGLENVITLSDFRDHSFGKAYGVAIAEGPLKGLLARAVFVLDEN
NKVVYSELVPEITNEPDYDAALAALKA
>gnl|CDD|179056 PRK00523, PRK00523, hypothetical protein; Provisional
GLAIGLALGLGIPLLIVGGIIGYFVSKKMFKKQIRENPPITENMIRAMYMQMGRKPSESQIKQVMRSVKN
AK
>gnl|CDD|179057 PRK00528, rpmE, 50S ribosomal protein L31; Reviewed
MKKDIHPDYHPIKVVMTDGTEYETRSTWGKTGPELRLDIDSGNHPAWTGGTQKLLDTGGRVAKFNKKFGG
L
>gnl|CDD|234788 PRK00529, PRK00529, elongation factor P; Validated
MISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREM
QYLYNDGDGYVFMDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGV
KGDTASGGTKPATLETGAVVQVPLFINEGEKIKVDTRTGEYVERAK
>gnl|CDD|134311 PRK00536, speE, spermidine synthase; Provisional
MWITQEITPYLRKEYTIEAKLLDVRSEHNILEIFKSKDFGEIAMLNKQLLFKNFLHIESELLAHMGGCTK
KELKEVLIVDGFDLELAHQLFKYDTHVDFVQADEKILDSFISFFPHFHEVKNNKNFTHAKQLLDLDIKKY
DLIICLQEPDIHKIDGLKRMLKEDGVFISVAKHPLLEHVSMQNALKNMGDFFSIAMPFVAPLRILSNKGY
IYASFKTHPLKDLMLQKIEALKSVRYYNEDIHRAAFALPKNLQEVFKDNIKS
>gnl|CDD|179059 PRK00539, atpC, F0F1 ATP synthase subunit epsilon; Validated
MQMLRFLVLSPSGIKLDEKIISAQVKTTEGYAGLNRNRAPLIAAIQSHVCKITFADKTKRSAIIGAGLLL
IKKTEAKIFTENFVFADELDYDETLKRKKELERKIKHTKDTKLNIKIEQNLMFELLKLSEKKR
>gnl|CDD|234789 PRK00549, PRK00549, competence damage-inducible protein A; Provisional
MKAEIIAVGTELLLGQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGGLG
PTKDDLTKETVAKFLGRELVLDEEALAKIEDYFAKRGREMTENNRKQALIPEGATVLPNPVGTAPGMIIE
VDGKTYIVLPGPPSELKPMFEEYVVPYLSSAKGTGEVLYSRVLRFFGIGESQLATTLRDLIDNQTNPTIA
PYAKDGEVTLRLTAKARSEEEAEKLIDPLEEEIRDRVGDYFYGYDEDSLEEVVAKLLKEKGLTIATAESC
TGGLLAARLTDFPGSSSYFKGGVVTYSNEAKAKLLGVPPETLEEHGAVSEETAEEMAEGARKLLGADIGI
SITGVAGPDGGTEEKPVGTVYIGLATPGGETVVKELILGGSRSDIRERAVTYALDLLRRALLGI
>gnl|CDD|234790 PRK00550, rpsE, 30S ribosomal protein S5; Validated
MRMMRIEKNKLELEEKVVAINRVTKVVKGGRRFSFSALVVVGDGKGRVGFGYGKAREVPEAIRKAVEDAK
KNMIKVPLVGGTIPHEVIGKFGAAKVLLKPASEGTGVIAGGAVRAVLELAGVKDVLAKSLGSNNPINVVR
ATFDALKQLRSPEEVAAKRGKSVEEILG
>gnl|CDD|179062 PRK00553, PRK00553, ribose-phosphate pyrophosphokinase; Provisional
MHLSIDKSNHVIFSLSKAKKLVDSICRKLSMKPGEIVIQKFADGETYIRFDESVRNKDVVIFQSTCSPVN
DSLMELLIAIDALKRGSAKSITAILPYYGYARQDRKTAGREPITSKLVADLLTKAGVTRVTLTDIHSDQT
QGFFDIPVDILRTYHVFLSRVLELLGKKDLVVVSPDYGGVKRARLIAESLELPLAIIDKRRPKHNVAESI
NVLGEVKNKNCLIVDDMIDTGGTVIAAAKLLKKQKAKKVCVMATHGLFNKNAIQLFDEAFKKKLIDKLFV
SNSIPQTKFEKKPQFKVVDLAHLYEEVLLCYANGGSISAIYTRHIEWIKKHV
>gnl|CDD|179063 PRK00555, PRK00555, galactokinase; Provisional
MTVRYAAPGRINLIGEHTDYNLGFALPIALPQRTVVTFTPEHTDAITASSDRADGSARIPLDTTPGQVTG
WAAYAAGVIWALRGAGHPVPGGAMSITSDVEIGSGLSSSAALECAVLGAVGAATGTRIDRLEQARLAQRA
ENEYVGAPTGLLDQLAALFGAPKTALLIDFRDLTVRPVAFDPDAAGVVLLLMDSRARHRHAGGEYAARRA
SCERAAADLGVSSLRAVQDRGLAALGAIADPIDARRARHVLTENQRVLDFAAALADSDFTAAGQLLTASH
ASMRDDFEITTERIDLIADSAVRAGALGARMTGGGFGGCVIALVPADRAEDVADTVRRAAVTAGYPEPAV
SRTYAAPGAGECR
>gnl|CDD|234791 PRK00556, minC, septum formation inhibitor; Reviewed
LKTNQKNVRVFEIEKQDPEEVIEFLEKNHPLLQYFLLIFKGDIEPEIKAFLQKHGLLFLETNRALNGRTI
KTMSLKEETNHEKVKKSKTEPKTTIYDRVIRSGEEIYSANDLIFLGRINNGAKIISEGNVSVYGECEGAI
ECFGEYLILKKIKSGQIIFQGKILSLKELDRLLVNKNLKIITKNDDIIDIKEIL
>gnl|CDD|234792 PRK00558, uvrC, excinuclease ABC subunit UvrC
KEFLKEKLKTLPDSPGVYRMKDANGTVIYVGKAKNLKNRVRSYFRKSHDSPKTRAMVSEIADIEYIVTRS
ETEALLLENNLIKKYKPRYNVLLRDDKSYPYIKITTNEEFPRLAITRGVAKDKGRYFGPYPSAGAVRETL
DLLQKLFPLRTCEDSVFKNRKRPCLLYQIGRCLAPCVGLISKEEYAELVDEAKLFLSGKTDEVLKELEEK
MEEASENLEFERAARYRDQIQALRRVQEKQKVSLKDGEDADVIAIAVDGGWACVQVFFVRGGKLLGRRSY
FPKVSETELEEILEAFLGQFYLQKSIPKEILVPHELDDEELAEALLAGRKVKIRVPQRGDKKELLELAEK
NAREALERKLSDQSTQQQALEELAELLGLPEPPYRIECFDISHIQGTATVASMVVFEDGGPDKSEYRRYN
IKGVTGGDDYAAMREVLTRRYSRLLKEFGPLPDLILIDGGKGQLNAAKEVLEELGLDIPVVGLAKGDKRK
AGTEELFFPGEPEPIILPPDSPALYLLQRIRDEAHRFAITFHRKKRSKARLTSALDDIPGIGPKRRKALL
KHFGSLKAIKEASVEELAKVPGISKKLAEAIYEALHKK
>gnl|CDD|167003 PRK00560, PRK00560, molybdenum cofactor guanylyltransferase MobA
MKNPMIDNIPCVILAGGKSSRMGENKALLPFGSYSSLLEYQYTRLLKLFKKVYISTKDKKFEFNAPFLLE
KESDLFSPLFGIINAFLTLQTPEIFFISVDTPFVSFESIKKLCGKENFSVTYAKSPTKEHYLISLWHQSL
LNALIYALKTQNYRLSDLVKNTSSQAVHFEDEEEFLNLNTLKDYELALQILKSRAN
>gnl|CDD|100598 PRK00561, ppnK, NAD(+) kinase
MKYKIFASTTPQTEPVLPKLKKVLKKKLAVEDGADYLFVLGGDGFFVSTAANYNCAGCKVVGINTGHLGF
YTSFNETDLDQNFANKLDQLKFTQIDLLEVQIDDQIHLVLNELAVYTNTAYPINIFIDNEFWEKYRGSGL
LIGPRTGSTALAKSAKGAVIFPRIDVIQIIELNPLLHPNQTTIQSPIILPIDTKVEFEIKKAFDHDQFPR
FYADGAKLRLGNSDTTIEISLVRSQAMFVASLKTRDFIQKLKSTFIKQS
>gnl|CDD|179066 PRK00564, hypA, hydrogenase nickel incorporation protein; Provisional
MHEYSVVSSLIALCEEHAKKNQAHKIEKVVVGIGERSGMDKSLFVSAFETFREESLVCKDAILDIVDEKV
ELECKDCSHVFKPNALDYGVCEKCHSKNVIITQGNEMRLLSLEMLAE
>gnl|CDD|234794 PRK00566, PRK00566, DNA-directed RNA polymerase subunit beta'; Provisional
DVNKQDFDAIKIGLASPEKIRSWSYGEVKKPETINYRTLKPERDGLFCERIFGPTKDYECLCGKYKRVRY
KGIICERCGVEVTRSKVRRERMGHIELAAPVAHIWFFKSLPSRIGLLLDMSLKDLERVLYFESYVVIDPG
DTPLEKKQLLTEEEYREALEEYGDEFVAKMGAEAIKELLKNIDLEAEAEELREELKETGSEQKRKKALKR
LKVVEAFRKSGNKPEWMILDVLPVIPPDLRPLVQLDGGRFATSDLNDLYRRVINRNNRLKRLLELGAPEI
IVRNEKRMLQEAVDALFDNGRRGRPVTGPNNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPE
LKLHQCGLPKKMALELFKPFIMKKLVERGLATTIKSAKKMVEREDPEVWDVLEEVIKEHPVLLNRAPTLH
RLGIQAFEPVLIEGKAIQLHPLVCTAFNADFDGDQMAVHVPLSLEAQAEARVLMLSSNNILSPANGKPII
VPSQDMVLGLYYLTREREGAKGEGMVFSSPEEALRAYENGEVDLHARIKVRITSKKLVETTVGRVIFNEI
LPEGLPFINVNKPLKKKEISKIINEVYRRYGLKETVIFLDKIKDLGFKYATRSGISIGIDDIVIPPEKKE
IIEEAEKEVAEIEKQYRRGLITDGERYNKVIDIWSKATDEVAKAMMKNLSKDQESFNPIYMMADSGARGS
ASQIRQLAGMRGLMAKPSGEIIETPIKSNFREGLTVLEYFISTHGARKGLADTALKTADSGYLTRRLVDV
AQDVIVREDDCGTDRGIEVTAIIEGGEVIEPLEERILGRVLAEDVVDPETGEVIVPAGTLIDEEIADKIE
EAGIEEVKIRSVLTCETRHGVCAKCYGRDLATGKLVNIGEAVGVIAAQSIGEPGTQLTMRTFHTGGVDIT
GGLPRVAELFEARKPKGPAIIAEIDGTVSFGKETKGKRRIVITPDDGEEREYLIPKGKHLLVQEGDHVEA
GDKLTDGSIDPHDILRVLGVEAVQNYLVNEVQKVYRLQGVKINDKHIEVIVRQMLRKVRITDPGDTDFLP
GELVDRSEFEEENRKLIAEGKEPATGRPVLLGITKASLATESFLSAASFQETTRVLTEAAIKGKVDPLRG
LKENVIIGRLIPAGTGLARYRNIKVEPAVDEEEAEA
>gnl|CDD|234795 PRK00567, mscL, large-conductance mechanosensitive channel protein MscL
MLKEFKEFAMRGNVVDLAVGVIIGAAFGKIVSSLVDDIIMPPIGLLIGGVDFSNLAIVLGEAQGDAPAVV
INYGVFINAVIDFLIIAFAIFLLVKLINKLRRKKEEPAAPPAPTTEEVLLTEIRDLLKAQRCPS
>gnl|CDD|134322 PRK00568, PRK00568, carbon storage regulator; Provisional
MLILSRKVNEGIVIDDNIHIKVISIDRGSVRLGFEAPESTLILRAELKEAIVSENQKASASVDESLLENI
KKVIKP
>gnl|CDD|234796 PRK00571, atpC, F0F1 ATP synthase subunit epsilon; Validated
MATLTVDIVSPEGLIYSGEVEEVVVPGTEGELGILPGHAPLLTALKPGVVRIKKDDGEEEVIAVSGGFLE
VQPDKVTVLADSAERADDIDEARAEEAKERAEEALENKHDDVDYARAQAALARAIARLRVAEKLR
>gnl|CDD|234797 PRK00575, tatA, Sec-independent protein translocase subunit TatA
MGSLSPWHWAILAVVVILLFGAKKLPDAARSLGKSLRIFKSEVKEMQSDNKAEASAAAAQAPYQVATPTP
VQSQRVDPAAASGQDSTEARPA
>gnl|CDD|234798 PRK00576, PRK00576, molybdopterin-guanine dinucleotide biosynthesis protein A; Provisional
MGRDKATLPLPGGTTTLVEHVVGIVGQRCAPVFVMAAPGQPLPELPAPVLRDELRGLGPLPATGRGLRAA
AEAGARLAFVCAVDMPYLTVELIDDLARPAAQTDAEVVLPWDGRDHYLAAVYRTDLAERVDALVGAGERS
MRALVDASDAQRIVMPESRPLTNVNTAADLPAPMQPGR
>gnl|CDD|234801 PRK00591, prfA, peptide chain release factor 1; Validated
KPSMLDKLEALEERYEELEALLSDPEVISDQKRFRKLSKEYAELEPIVEAYREYKQAQEDLEEAKEMLEE
ESDPEMREMAKEELKELEERLEELEEELKILLLPKDPNDDKNVILEIRAGTGGDEAALFAGDLFRMYSRY
AERQGWKVEILSASEGELGGYKEVIAEISGDGVYSKLKFESGVHRVQRVPATESQGRIHTSAATVAVLPE
AEEVEVEINPKDLRIDTFRSSGAGGQHVNTTDSAVRITHLPTGIVVECQDERSQHKNKAKAMKVLRARLY
DAERQKAQAEEAATRKSQVGSGDRSERIRTYNFPQGRVTDHRINLTLYKLDEVMEGDLDELIDALIAEDQ
AEKLAALGE
>gnl|CDD|179075 PRK00595, rpmG, 50S ribosomal protein L33; Validated
AAKGMRVKIKLESTEGTGRFYTTTKNKRNTPEKLELKKYDPVLRKHVLHKETK
>gnl|CDD|179076 PRK00596, rpsJ, 30S ribosomal protein S10; Reviewed
MAKQKIRIRLKAFDHRLLDQSAKKIVETAKRTGAQVRGPIPLPTKKERFTVLRSPHVNKDSREQFEIRTH
KRLIDIVDPTPKTVDALMKLDLPAGVDVEIKL
>gnl|CDD|234802 PRK00601, dut, dUTP diphosphatase
MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPDGYEAQILPRS
GLAHKHGIVLGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERG
AGGFGSTGRH
>gnl|CDD|100616 PRK00611, PRK00611, putative disulfide oxidoreductase; Provisional
MIKFLRSYALYFAWLISCIGTLMSIYYSYILNVEPCVLCYYQRICLFPLVVILGIAAYREDSSIKIYALP
LALVGFGIAIYQVCLQEIPGMTLDICGRVSCSTKLFLFGFITMPMASAAAFCAIACLLVLATKSK
>gnl|CDD|234803 PRK00615, PRK00615, glutamate-1-semialdehyde aminotransferase; Provisional
MPSIQEMTHTFSEACQYFPGGVNSPVRACRSVGITPPIVSSASGDIFIDSLGKTFIDFCGSWGSLIHGHS
HPKICDAIQQGAERGTSYGLTSEQEILFAEELFSYLGLEDHKIRFVSSGTEATMTAVRLARGITGRSIII
KFLGCYHGHADTLLQGISFSETSLDTLTHLVDTDLAHPLTLSLPYNDFQIFQTVMNSLGHRVAGVIFEPI
CANMGVVLPKPGFIEGIIQTCRRTGSLSIMDEVVTGFRVAQGGAAAIYHVKPDITVYGKILGGGLPAAAV
VAHKSIMDHLAPEGTIFQAGTLSGNPLAMAAGKASINLCREQGFYTQLSTLEQNFLSPIEEMIRSQGFPV
SLVRYGSMFSFFFNENRPNNLAEAQLSDIEAFQTFYQSAFSKGVYLSPSPFEASFLSSAHSMENLDYAQN
VLIDSLEKVFSLV
>gnl|CDD|167014 PRK00624, PRK00624, glycine cleavage system protein H; Provisional
KMWYSDYHVWIEPIHSRIVRLGLTSKMQENLGNILHIDLPSVGSFCKEGEVLVILESSKSAIEVLSPVSG
EVIEVNTALEDDIQPINNAPESEGWFVVVQLDEDFDSENLSLEP
>gnl|CDD|134335 PRK00625, PRK00625, shikimate kinase; Provisional
MQIFLCGLPTVGKTSFGKALAKFLSLPFFDTDDLIVSNYHGALYSSPKEIYQAYGEEGFCREEFLALTSL
PVIPSIVALGGGTLMIEPSYAHIRNRGLLVLLSLPIATIYQRLQKRGLPERLKHAPSLEEILSQRIDRMR
SIADYIFSLDHVAETSSESLMRACQSFCTLLLS
>gnl|CDD|234804 PRK00629, pheT, phenylalanyl-tRNA synthetase subunit beta; Reviewed
MKFSLSWLKEYVNPDISSEELAEALTMIGLEVEGVEDVAAGLSGVVVGKVLECEKHPNADKLRVCQVDVG
EEPLQIVCGAPNVRAGDKVPVALPGAVLPGGFKIKKAKLRGVESEGMLCSASELGLSDDHDGIIELPEDA
PVGTDAREYLGLDDTVIEISLTPNRADCLSVRGIARELAALLGLPLKLPEIEPVPATIDDKLPVEIEDPD
LCPRYAGRVIKGVKNIAPSPLWLQERLRAAGIRPINNVVDITNYVMLELGQPLHAFDLDKIGGGIVVRRA
KEGEKLTTLDGKERTLDPEDLVIADDKKPLALAGVMGGEDSEVTENTTNVLLESAYFDPVSIRKTARRLG
LRTDASYRFERGVDPALTLLALERATALILELGGGEVVEGVVDVYPLPKEPTITLRLERINRLLGTEISD
EEIVDILKRLGFEVTEVDGDGLTVTVPSWRFDIEIEEDLVEEVARIYGYDNIPSTPPVAALTMGGLTEAQ
RLLRRLRRALAALGYQEVITYSFVSPEDAKLFGLNPEPLLLLNPISEELSVMRTSLLPGLLEAVAYNLNR
GNKDVALFEIGRVFLPDGDLPREPEHLAGVLTGNRVEESWGGKRPVDFFDLKGDVEALLEALGLPEVEFV
AEFEAAALHPGRSAEIYLDGKVIGFIGELHPKVLKKLDLPGRTYVFELDLDALLEAARKLPKYKPISKFP
AVRRDLALVVDEDVPAADILKAIKKAGGKLLESVELFDVYEGKGIGEGKKSLAFRLTFQDPDRTLTDEEI
NAAMDKIVAALEEKFGAELRG
>gnl|CDD|234805 PRK00630, PRK00630, nickel responsive regulator; Provisional
MDTPNKDDSIIRFSVSLQQNLLDELDNRIIKNGYSSRSELVRDLIREKLVEDNWAEDNPNDESKIAVLVV
IYDHHQRELNQRMIDIQHASGTHILCTTHIHMDHHNCLETIILRGNSFEIQRLQLEIGGLKGVKFAKLTK
ASSFEYNE
>gnl|CDD|234806 PRK00635, PRK00635, excinuclease ABC subunit A; Provisional
MPSLPVRLSGITVRNLKNISIEFCPREIVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSL
PDPSVEKIEGLSPTIAVKQNHFSQHSHATVGSTTELNSHLALLFSLEGQARDPVTLHPLTLYSKEKILST
IAAIPDGTQITLLAPLPAKDILAIRECLRQGFTKVRIDGEISPIYKFLTSGIPEDVPVDIVVDTLIKNES
NTARLKVSLFTALDIGHGECSLHFDNQKRTFSTQATIPETQQTYTPLTPQLFSPHSLEDRCPQCQGSGIF
ISIDDPSLIQQNLSIEENCCPFAGNCSTYLYHTIYQSLADSLGFSLSTPWKDLSPEIQNIFLYGKEGLVL
PVRLFDGTLGKKTLTHKVWRGVLNEIGEKVRYSNKPSRYLPKGTSATSCPRCQGTGLGDYANAATWHGKT
FAEFQQMSLQELFIFLSQLPSKSLSIEEVLQGLKSRLSILIDLGLPYLTPERALATLSGGEQERTALAKH
LGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPGAGIFGGE
VLFNGSPREFLAKSDSLTAKYLRQELTIPIPEKRTNSLGTLTLSKATKHNLKDLTISLPLGRLTVVTGVS
GSGKSSLINDTLVPAVEEFIEQGFCSNLSIQWGAISRLVHITRDLPGRSQRSIPLTYIKAFDDLRELFAE
QPRSKRLGLTKSHFSFNTPLGACAECQGLGSITTTDNRTSIPCPSCLGKRFLPQVLEVRYKGKNIADILE
MTAYEAEKFFLDEPSIHEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKKPTLYVLDEPT
TGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPEGGNLGGYLLASCSPEELIHLHTP
TAKALRPYLSSPQELPYLPDPSPKPPVPADITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFD
ILYAAGNIAYAELFPPYIRQALIKKTPLPSVDKVTGLSPVIAIEKTSASKNSNHSVASALEISNGLEKLF
ARLGHPYSPLSGDALRKITPQTIAEELLTHYTKGYVTITSPIPKEEDLFIYLQEKLKEGFLKLYANEQFY
DLDEPLPTSLENPAIVIQHTKISEKNLSSLLSSLTLAFSLSSSICLHIEYAGTSLSLTYRLGWQDSSGNL
YPNITTPLLSRDHEEGLCPLCHGKGFILKCSLLPHKEKIAHYTPLSLFTLFFPNQDPKPVYPLLKELGIP
SIALFQELDTLSFESLCLGTQQHPGLNALLMEAMLMESEEPLPPPLISKTPCNQCQGLGVYTYAHCVRIH
NTSLSDIYQEDVTFLKKFLLTIHDDEEPSIIQDLLNRLTFIDKVGLSYITLGQEQDTLSDGEHYRLHLAK
KISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEHADHLIHLGPGSGPQGG
YLLSTSALKQSQPDLHNTRSSEETPTLSVSLSIHTIQNLNVSAPLHSLVAISGVSGSGKTSLLLEGFYKQ
ACALIEKGPSVFSEIIFLDSHPQISSQRSDISTYFDIAPSLRNFYASLTQAKALNISASMFSTNTKQGQC
SDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEVAETFPFLKKIQKPL
QALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYLPPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVS
LGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKILFSGPPKDISASKDSLLKTYMCNL
>gnl|CDD|179080 PRK00642, PRK00642, inorganic pyrophosphatase; Provisional
MSKFPLSRAHPWHGLSLGPDAPESVCCYIEITPFDTVKYELDKATGYLKVDRPQKFSNFCPALYGFIPRT
YCGDLSGKLSGEQSGREDIKGDGDPLDICVLTEKNITHGNILLQARPIGGLRMIDGGEADDKIIAVLEDD
LVYGEIKDISECPGTLLDRLQHYFLTYKATPGELIKGVEIVGIYGKEEAQKVIQLAHEDYANKFG
>gnl|CDD|100624 PRK00647, PRK00647, hypothetical protein; Validated
MLEGFWILEVKVTPKARENKIVGFEGGILKVRVTEVPEKGKANDAVIALLAKFLSLPKRDVTLIAGETSR
KKKVLLPRSIKAILFEQFPSESSSTT
>gnl|CDD|234807 PRK00648, PRK00648, Maf-like protein; Reviewed
MKYKIILASSSPRRKEILEGFRIPFEVVPSPFVEESYPYSLDPEEITLELARLKAEAVRSDLFPDELIIT
ADTIVWYDGKVLGKPKDEEEAVEMLRTLSGKTHEVITGVCLLHNGKLLSGSETTQVTFRELSDEEIEYYI
DTYKPLDKAGAYGIQEWGGLIVKKIEGSYYNVMGLPIQTLYEELKELGISL
>gnl|CDD|234808 PRK00652, lpxK, tetraacyldisaccharide 4'-kinase; Reviewed
MASMIPRFWYKRSPLAWLLLPLSWLYGLIAALRRLLYRLGLKKPYRAPVPVIVVGNITVGGTGKTPVVIA
LAEQLQARGLKPGVVSRGYGGKLEKGPLLVDPDHTAAEVGDEPLLIARRTGAPVAVSPDRVAAARALLAA
HGADIIILDDGLQHYRLARDIEIVVVDGQRGFGNGFLLPAGPLREPPSRLKSVDAVIVNGGGDARAGEIP
MRLEPGEAVNLTGERRPLASLQRVVAFAGIGNPQRFFATLRALGIEVVKTHAFPDHYPFTKADLEALVSK
GLTLLMTEKDAVKCRAFAQDNWWYLPVDAELSPDFPDALLEKLDR
>gnl|CDD|234809 PRK00654, glgA, glycogen synthase GlgA
MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKLRDAQVVGRLDLFTVLFGHL
EGDGVPVYLIDAPHLFDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGLIPALLKEKY
WRGYPDIKTVFTIHNLAYQGLFPAEILGELGLPAEAFHLEGLEFYGQISFLKAGLYYADRVTTVSPTYAR
EITTPEFGYGLEGLLRARSGKLSGILNGIDYDIWNPETDPLLAANYSADDLEGKAENKRALQERFGLPDD
DAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALA
HRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPIVRRTGGLADTVIDYNPEDGEATGFVFDDFNAEDLLR
ALRRALELYRQPPLWRALQRQAMAQDFSWDKSAEEYLELYRRLLGK
>gnl|CDD|179084 PRK00665, petG, cytochrome b6-f complex subunit PetG; Reviewed
MIEPLLCGIVLGLIPVTLAGLFVAAWNQYKRGNQLGL
>gnl|CDD|179085 PRK00668, ndk, mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
MERTFSIIKPDAVQRGLIGEIISRFEKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMTSGPV
VVMVLEGENAIAKVRELMGATNPAEAAPGTIRGDFALSIGENVVHGSDSPESAAREIALFFSEE
>gnl|CDD|234810 PRK00676, hemA, glutamyl-tRNA reductase; Validated
MVLGVVGISYREAALKEREQVIQILQQFEGSLFFRQRFFGEEGDFVLLLTCHRAELYYYSVSPAELQSSL
LSEITSLGVRPYFYRGLDCFTHLFCVTSGMDSLILGETEIQGQVKRAYLKAARERKLPFALHFLFQKALK
EGKVFRSKGGAPYAEVTIESVVQQELRRRQKSKKASLLFIGYSEINRKVAYYLQRQGYSRITFCSRQQLT
LPYRTVVREELSFQDPYDVIFFGSSESAYAFPHLSWESLADIPDRIVFDFNVPRTFPWSETPFPHRYLDM
DFISEWVQKHLQCRKEVNNKHKLSLREAAYKQWESYEKKLSRIDCVQANAPRPSVLSY
>gnl|CDD|234811 PRK00685, PRK00685, metal-dependent hydrolase; Provisional
MKITWLGHSAFLIETGGKKILIDPFITGNPLADLKPEDVKVDYILLTHGHGDHLGDTVEIAKRTGATVIA
NAELANYLSEKGVEKTHPMNIGGTVEFDGGKVKLTPALHSSSFIDEDGITYLGNPTGFVITFEGKTIYHA
GDTGLFSDMKLIGELHKPDVALLPIGDNFTMGPEDAALAVELIKPKIVIPMHYNTFPLIEQDPEKFKALV
EGLGTKVVILKPGESIEL
>gnl|CDD|234812 PRK00694, PRK00694, 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Validated
MMATPCIQNAFRRKTHPVRIGNLFVGSEHSIKIQSMTTTATTDVDGTVRQICALQEWGCDIVRVTVQGLK
EAQACEHIKERLIQQGISIPLVADIHFFPQAAMHVADFVDKVRINPGNYVDKRNMFTGKIYTDEQYAHSL
LRLEEKFSPLVEKCKRLGKAMRIGVNHGSLSERVMQRYGDTIEGMVYSALEYIEVCEKLDYRDVVFSMKS
SNPKVMVAAYRQLAKDLDARGWLYPLHLGVTEAGSGTDGIIKSAVGIGTLLSEGLGDTIRCSLTGCPTNE
IPVCISLLKHTTEYLELPEKDNPFALHHSEQFVSATRKTLKTTPWGNVYGVFIKLTDVHLLTAEPEELLE
CLGIDPTTGKKDFTTPEGVVVPKAMRSSPIVSELEKHLLVFHHHDVPCLYEMNEEIWLSEEVLSAPFVHF
HATDPFIHTARRFFSKRQHSTQPVKLVFSLDPDSKNEAAIDIATEFGALLLDGLGECVLLDLPNIKLSDV
RTIAFGTLQSAGVRLVKTEYISCPGCGRTLFDLLEVTQRIRERTQHLPGLKIAVMGCIVNGPGEMADADF
GFVGSKTGMIDLYVKHTCVKAHIPMENAEEELVQLLKEHGVWKDPE
>gnl|CDD|234813 PRK00696, sucC, ADP-forming succinate--CoA ligase subunit beta
MNLHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKAGGVKLAKSPEEAR
EFAKQILGMTLVTHQTGPKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEET
PEKIHKVAIDPLTGLQPFQAREIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLI
ALDAKINFDDNALFRHPDLAELRDLSEEDPLEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYG
GEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFGGITRCDVIAEGIIAAVKEVGVTVPLVVRLE
GTNVELGKKILAESGLNIIAADTLDDAAQKAVEAAKGK
>gnl|CDD|234815 PRK00701, PRK00701, divalent metal cation transporter MntH
MMSLPRTATAPFSLSEVNGSVAVSSGRSFWKRLLAFLGPAFLVAVGYMDPGNWATNIQGGSQFGYTLLWV
ILLSNLMAMLLQSLSAKLGIATGRDLAQACRDRYPRPVVWFLWIQAELAIMATDLAEVIGAAIALKLLFG
IPLLQGALITALDTFLILMLQRRGFRPLEAIIGGLLLVIAAAFIVELFLAQPDWAAVLKGFIPSSEILPN
PEALYLAAGILGATVMPHNLYLHSSLVQTRVVGRTGEEKREALRFTRIDSAIALTIAGFVNAAMLILAAA
AFHASGHTDVADIEDAYLLLSPLLGAAAATLFGIALLASGLSSTVVGTLAGQIVMEGFLRLRIPLWVRRL
ITRGLAMVPALIVILLGGELDPTRLLVLSQVVLSFGLPFALIPLLLFTSDRKLMGELVNPRWVKIIAWII
AVLIVALNIYLLYQTFTGL
>gnl|CDD|234816 PRK00702, PRK00702, ribose-5-phosphate isomerase RpiA
MTQDELKKAAAEAAAEYVEDGMIVGLGTGSTAAYFIDALGERVKEGLIIGGVPTSEASTELAKELGIPLF
DLNEVDSLDLYVDGADEIDPHLNLIKGGGAALTREKIVAAAAKRFICIVDESKLVDVLGKFPLPVEVIPF
ARSAVARELEKLGGQPELRMDEPVVTDNGNYILDVHFGRIPDPEALEKELNNIPGVVEHGLFANRADVVL
VGTPDGVKTL
>gnl|CDD|234817 PRK00704, PRK00704, photosystem I reaction center protein subunit XI; Provisional
WVVPPVGDPCVGNLATPVNSSYFTKAFINNLPIYRPGLSPNFRGLETGMAHGYLLYGPFAKLGPLRDTEF
ANLAGLLAAIGLVLILTALLSLYGAVGKQPNVAPPDVTVPNPPADLFTREGWSDFTSGFWLGGCGGAVFA
YFLLETLDTIDPIIRGLWNV
>gnl|CDD|234819 PRK00711, PRK00711, D-amino acid dehydrogenase
MRVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPALETSFANAGQISPGYAAPWAAPGVPLKAIKWLFQ
RHAPLAIRPDGDPFQLRWMWQMLRNCTASRYAVNKSRMVRLAEYSRDCLKALRAETGIQYEGRQGGTLQL
FRTQQQLDAAAKDIAVLEEAGVPYELLDRDELAAVEPALAGVRHKLVGGLRLPNDETGDCQLFTQRLAAM
AEQLGVKFRFNTPVDGLLVEGGRITGVQTGGGVITADAYVVALGSYSTALLKPLGVDIPVYPLKGYSLTV
PITDEDRAPVSTVLDETYKIAITRFDDRIRVGGMAEIVGFDLRLDPARRETLEMVVRDLFPGGGDLSQAT
FWTGLRPMTPDGTPIVGATRYKNLWLNTGHGTLGWTMACGSGQLLADLISGRKPAIDADDLSVARY
>gnl|CDD|234820 PRK00714, PRK00714, RNA pyrophosphohydrolase; Reviewed
MIDDDGYRPNVGIILLNRQGQVFWGRRIGQGHSWQFPQGGIDPGETPEQAMYRELYEEVGLRPEDVEILA
ETRDWLRYDLPKRLVRRSKGVYRGQKQKWFLLRLTGDDSEINLNTTSHPEFDAWRWVSYWYPLDQVVPFK
RDVYRRVLKEFARLLM
>gnl|CDD|234821 PRK00719, PRK00719, alkanesulfonate monooxygenase; Provisional
MNVFWFLPTHGDGRYLGTSEGARAVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASLIPVTQRL
KFLVALRPGLMSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGDGLFLDHDERYEASAEFLRIWRRL
LEGETVDFEGKHIQVKGAKLLFPPVQQPYPPLYFGGSSDAAQELAAEQVDLYLTWGEPPAQVKEKIEQVR
AKAAAHGRKVRFGIRLHVIVRETNEEAWQAAERLISHLDDETIARAQAAFARMDSVGQQRMAALHGGKRD
NLEISPNLWAGVGLVRGGAGTALVGDPPTVAARIKEYAALGIDTFILSGYPHLEEAYRVAELLFPLLDVA
IPEKPQPQPSGPFGEVVANDYLPKKAQS
>gnl|CDD|234822 PRK00720, tatA, twin-arginine translocase TatA/TatE family subunit
MGSFSIWHWLIVLAVVLLLFGRGKISELMGDVAKGIKSFKKGMADDDAPPAEPPEPVRTIDHKADEPVAP
VKKDVGSK
>gnl|CDD|179097 PRK00723, PRK00723, phosphatidylserine decarboxylase; Provisional
MIKYYNRKTKKYEIEKVAGEKYLKWLYSSPIGKNLLELLIKKKIFSKIYGWYCDSRLSRKKIKPFVNDFN
IDMSESEKPLSDFKSFNDFFTRKLKPEARPIDQGENILISPGDGRLLAYENIDLNSLFQVKGKTYSLKEL
LGDPELAKKYAGGTCLILRLCPTDYHRFHFPDSGICEETRKIKGHYYSVNPIALKKIFELFCENKREWSI
FKSENFGDILYVEVGATCVGSIIQTYKPNKKVKKGDEKGYFKFGGSTVILFFEKNKIKIDADILEQSKLG
YETKVLMGESIGRKFSS
>gnl|CDD|234823 PRK00724, PRK00724, formate dehydrogenase accessory sulfurtransferase FdhD
MMGPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPED
IESIDIVESCNGVEVQLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLD
RAMAQLQDAQPLFQLTGGVHAAALLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRAS
SEMVQKAAMAGIPILVAVSAPTSLAVELAEELGLTLVGFARGGRFNIYTHPQR
>gnl|CDD|234824 PRK00725, glgC, glucose-1-phosphate adenylyltransferase; Provisional
EKNDSLMLARQLTRDTLALILAGGRGSRLKELTDKRAKPAVYFGGKFRIIDFALSNCINSGIRRIGVLTQ
YKAHSLIRHIQRGWSFFREELGEFVDLLPAQQRVDEENWYRGTADAVYQNLDIIRRYDPKYVVILAGDHI
YKMDYSRMLADHVESGADCTVACLEVPREEASAFGVMAVDENDRITAFVEKPANPPAMPGDPDKSLASMG
IYVFNADYLYELLEEDAEDPNSSHDFGKDIIPKIVEEGKVYAHPFSDSCVRSDPEEEPYWRDVGTLDAYW
QANLDLASVTPELDLYDRNWPIWTYQEQLPPAKFVFDRSGRRGMAINSLVSGGCIISGAVVRRSVLFSRV
RVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVIPEGMVIGEDPEEDAKRFRRSEEGIVLVTREMLDK
LGGKQ
>gnl|CDD|234825 PRK00726, murG, undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
MKKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANL
KAPFKLLKGVLQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKV
ATAFPGAFPEFFKPKAVVTGNPVREEILALAAPPARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLP
EALQVIHQTGKGDLEEVRAAYAAGINAEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPL
PHAADDHQTANARALVDAGAALLIPQSDLTPEKLAEKLLELLSDPERLEAMAEAARALGKPDAAERLADL
IEELARK
>gnl|CDD|179101 PRK00732, fliE, flagellar hook-basal body complex protein FliE
MATPLSAANAYASLARMAVPSGGGGGGDKGGPSFGALLKDAMGSVLEAGRKSDAQTAAMASGKANLMDVV
TAVAETDVAVSTLVSVRDRVIQAYEEIMRMPI
>gnl|CDD|234827 PRK00733, hppA, membrane-bound proton-translocating pyrophosphatase; Validated
VLKQPAGTERMQEIAGAIQEGAMAYLKRQYKTIAIFGVVVAVLLFLPAGGLFLGWLTAVAFLVGAVFSAL
AGYIGMRVATRANVRTAQAARKGLGKALKVAFRGGAVMGLLVVGLGLLGVAGLYLVFGLGANPDDAPDAL
VGFGFGASLIALFARVGGGIFTKAADVGADLVGKVEAGIPEDDPRNPAVIADNVGDNVGDCAGMGADLFE
SYAVTIVAAMVLGAAAADAAFGVAGVLFPLLIAAVGIIASIIGIFFVRLGKGGNPMKALNRGLIVTAVLS
IVLTYFATYWLLGDGADGFTWLNLFGAVLIGLVVGALIGLITEYYTSTEYRPVKEIAEASRTGPATNIIS
GLAVGMESTALPVLVIVAAILGAYLLGMAGAGLYGIALAAVGMLSTAGIIVAVDAYGPITDNAGGIAEMA
GLPPEVRKITDALDAVGNTTKAVTKGFAIGSAALAALALFAAYIDELAGLLGGGGILSLDLSNPYVLVGL
LIGGMLPFLFSALAMTAVGRAAGAMVEEVRRQFREIPGIMEGTAKPDYARCVDISTKAALKEMILPGLLA
VLAPIAVGFLLGPEALGGLLAGAIVTGLLLAIFMANAGGAWDNAKKYIEDGNHGGKGSEAHKAAVVGDTV
GDPFKDTAGPALNPLIKLMNIVALLIAPLLVHLSLG
>gnl|CDD|179103 PRK00736, PRK00736, hypothetical protein; Provisional
MDAEERLTELEIRVAEQEKTIEELSDQLAEQWKTVEQMRKKLDALTERFLSLEEQAAPDVPVTKPPHW
>gnl|CDD|179104 PRK00737, PRK00737, small nuclear ribonucleoprotein; Provisional
MAQRPLDVLNNALNSPVLVRLKGGREFRGELQGYDIHMNLVLDNAEEIQDGEVVRKLGKVVIRGDNVVYV
SP
>gnl|CDD|179105 PRK00741, prfC, peptide chain release factor 3; Provisional
SELAQEVAKRRTFAIISHPDAGKTTLTEKLLLFGGAIQEAGTVKGRKSGRHATSDWMEMEKQRGISVTSS
VMQFPYRDCLINLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTPIFTFINK
LDRDGREPLELLDEIEEVLGIACAPITWPIGMGKRFKGVYDLYNDEVELYQPGEGHTIQEVEIIKGLDNP
ELDELLGEDLAEQLREELELVQGASNEFDLEAFLAGELTPVFFGSALNNFGVQEFLDAFVEWAPAPQPRQ
TDEREVEPTEEKFSGFVFKIQANMDPKHRDRIAFVRVCSGKFEKGMKVRHVRTGKDVRISNALTFMAQDR
EHVEEAYAGDIIGLHNHGTIQIGDTFTQGEKLKFTGIPNFAPELFRRVRLKNPLKQKQLQKGLVQLSEEG
AVQVFRPLDNNDLILGAVGQLQFEVVAHRLKNEYNVEAIYEPVGVATARWVECDDAKKLEEFKRKNRSNL
AKDGGDNLVYLAPNEVNLRLAQERYPDVKFHATREH
>gnl|CDD|234828 PRK00742, PRK00742, chemotaxis-specific protein-glutamate methyltransferase CheB
MMKIRVLVVDDSAFMRRLISEILNSDPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEK
IMRLRPTPVVMVSSLTERGAEITLRALELGAVDFVTKPFLGISLGMDEYKEELAEKVRAAARARVRALPP
RAAAAARAAAAAPAALAAAPLLSSKLVAIGTSTGGPEALQKVLTPLPANFPAPILIVQHMPAGFTKSFAE
RLNRLCQIEVKEAEDGERLKPGHAYIAPGGKHMMVARSGANYRIKLDDGPPVNRHRPSVDVLFRSAAKAA
GRNALGVILTGMGRDGAAGLLEMKQAGATTIAQDEASCVVYGMPKAAIEAGAVDEVLPLDQIAERILKEV
AAGR
>gnl|CDD|179107 PRK00745, PRK00745, 4-oxalocrotonate tautomerase; Provisional
MPTFHIELFEGRTVEQKRKLVEEITRVTVETLGCPPESVDIIITDVKRENWATGGKLWSDPK
>gnl|CDD|179108 PRK00748, PRK00748, 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
MIIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIV
KAVDIPVQVGGGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVVGLDARDGKVATDGW
LETSGVTAEDLAKRFEDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKG
LGAVEGVIVGRALYEGKFDLAEA
>gnl|CDD|234829 PRK00750, lysK, lysyl-tRNA synthetase; Reviewed
AEKSKHWADEEAEKIIKRLGKKPPVVVETGIGPSGLPHIGNFREVARTDMVRRALRDLGIKTRLIFFSDD
MDGLRKVPDNVPNQEMLEEYLGKPLTEIPDPFGCHESYAEHFNAPLREFLDRFGIEYEFISATECYKSGR
YDEAILTALENRDEIMEILLPYLGEERQATYSPFLPICPKCGKVLTTPVISYDAEAGTVTYDCECGHEGE
VPVTGGHGKLQWKVDWPMRWAALGVDFEPFGKDHASASYDTSKKIAREILGGEPPEPFVYELFLDKKGEK
ISKSKGNVITIEDWLEYAPPESLRLFMFARPKPAKRLDFDVIPKLVDEYDRFERKYFGQEEKKEEEELAN
PVYHIHNGNPLPVPFRLLLNLAQIANAEDKEVLWGFLKRYAPGATPETHPRLDRLVEYAINWYRDFVAPE
KKYRAPTEKERAALEDLDDALRELADGADAEEIQNEIYEVAKKELGVNPRDWFKALYEVLLGQSQGPRLG
SFIALLGIDFVIALIREALA
>gnl|CDD|134373 PRK00753, psbL, photosystem II reaction center L; Provisional
MERNPNPNKQPVELNRTSLYLGLLLVFVLGILFSSYFFN
>gnl|CDD|179110 PRK00754, PRK00754, signal recognition particle protein Srp19; Provisional
MKDKGRIVIWPAYIDSTRSRSEGRIISRKLAVKEPRLEEIIEAAEKLGLNPEVEPDKAYPRSWWEVSGRV
LVDKVGSKTNTLRMIAKEIKKLRGG
>gnl|CDD|179111 PRK00756, PRK00756, acyltransferase NodA; Provisional
MSSQVRWKLCWENELELSDHAELAEFFRKTYGPTGAFNAKPFEGGRSWAGARPELRAIAYDSHGVAAHMG
LLRRFIKVGEVDLLVAELGLYGVRPDLEGLGIAHSIRAMYPVLQELGVPFAFGTVRHALRNHVERLCRNG
LATIVTGVRVRSTLPDVYLDLPPTRTEDVLVVVFPIGRPMSEWPSGTLIERNGPEL
>gnl|CDD|179112 PRK00758, PRK00758, GMP synthase subunit A; Validated
KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKAFEDGLILSGGPDIERAGNCPEYLKELDVPI
LGICLGHQLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIRVWASHADEVKELPDGFEILARS
DICEVEAMKHKEKPIYGVQFHPEVAHTEYGEEIFKNFLEICGKY
>gnl|CDD|179113 PRK00762, hypA, hydrogenase maturation nickel metallochaperone HypA
MHELSMACEIVEAVIDTAEKNNATEVTEVTLEIGRLTMLNPEQLRFMLDVLAEGTIAEDADLIVEMIPVE
IECECGYEGVVDEDEIDHYAAVIECPVCGNKRAHILGGRECNVKNIKIEKEDEN
>gnl|CDD|234830 PRK00766, PRK00766, hypothetical protein; Provisional
MIRKVKPEIRVLGIDDGTFLFKSSEKVILVGVVMRGGDWVDGVLSRWITVDGLDATEAIIEMVNSSRHKG
QLRVIMLDGITYGGFNVVDIEELYRETGLPVIVVMRKKPDFEAIESALKKHFSDWEERIKLIKKAGKIVE
LITRGPLYIQAAGIDPETAAEIVRLTSTRSLIPEPLRLAHLIASGVMLGESRGE
>gnl|CDD|179115 PRK00767, PRK00767, transcriptional regulator BetI; Validated
MPKVGMEPIRRQQLIDATLRAIGEVGLLDATIAQIARRAGVSTGIISHYFGGKDGLLEATMRHLLRQLGD
AVLARLAAAADTPRARLRAIVEANFDASQFSSPAMKTWLAFWASSMHSPDLRRLQRINSRRLYSNLLFEF
RRLLPREQAREAAEGLAALIDGLWLRGALSGDPEDAEAARALAYDYIDQQLAQYGSN
>gnl|CDD|234831 PRK00768, nadE, ammonia-dependent NAD(+) synthetase
TLQQEIIAELGVKPTIDPEEEIRRRVDFLKDYLKKSGLKSLVLGISGGQDSTLAGRLAQLAVEELRAETG
DDDYQFIAVRLPYGVQADEDDAQDALAFIQPDRVLTVNIKPAVDASVAALEAAGIELSDFVKGNIKARER
MIAQYAIAGATGGLVVGTDHAAEAVTGFFTKFGDGGADILPLFGLNKRQGRALLAALGAPEHLYEKVPTA
DLEDDRPGLPDEVALGVTYDQIDDYLEGKPVSEEAAETIENWYLKTEHKRHLPITIFD
>gnl|CDD|179117 PRK00770, PRK00770, deoxyhypusine synthase
MSKLLGKKIAPIPISPNISVVDLIDVYFTAYNSARLREACQLLAQRMIDDGVTVGLTLSGAMTPAGFGVS
ALAPLIEAGFIDWIISTGANLYHDLHYALGLPLFAGHPFVDDVKLREEGIIRIYDIIFDYDVLLETDAFI
REILKAEPFQKRMGTAEFHYLLGKYVREVEKQLGVPHKSLLATAYEYGVPIYTSSPGDSSIGMNVAALAL
EGSELVLDPAIDVNETAAIAYNAKESEGKSGAVILGGGSPKNFLLQTQPQIHEVLGLEERGHDYFIQITD
ARPDTGGLSGATPSEAVSWGKVDPDELPDTVVCYTDSTIALPLLTAYALNTCKPRPLKRLYDRREEMYEK
LQKDYLAAKDQPVAKVEPTSGEVATYPCGTPIPR
>gnl|CDD|179118 PRK00771, PRK00771, signal recognition particle protein Srp54; Provisional
LGESLRDALKKLAGKSRIDEKTVKEVVKDIQRALLQADVNVKLVKELSKSIKERALEEEPPKGLTPREHV
IKIVYEELVKLLGEETEPLVLPLKPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYD
QLKQLAEKIGVPFYGDPDNKDAVEIAKEGLEKFKKADVIIVDTAGRHALEEDLIEEMKEIKEAVKPDEVL
LVIDATIGQQAKNQAKAFHEAVGIGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPD
RFISRLLGMGDLESLLEKVEEALDEEEEEKDVEKMMKGKFTLKDMYKQLEAMNKMGPLKQILQMLPGLGG
KLPDEALEVTEEKLKKYKAIMDSMTEEELENPEIINASRIRRIARGSGTTVEDVRELLKYYKMMKKAMKQ
LKKGKGKMGKLMKQFGF
>gnl|CDD|234832 PRK00772, PRK00772, 3-isopropylmalate dehydrogenase; Provisional
MTYKIAVLPGDGIGPEVMAEAVKVLDAVAEKFGFDFEFEEALVGGAAIDAHGVPLPEETLEACRAADAVL
LGAVGGPKWDNLPPDVRPERGLLALRKELGLFANLRPAKLYPGLADASPLKPEIVAGLDILIVRELTGGI
YFGEPRGREGLGGEERAFDTMVYTREEIERIARVAFELARKRRKKVTSVDKANVLESSRLWREVVTEVAK
EYPDVELSHMYVDNAAMQLVRNPKQFDVIVTENLFGDILSDEAAMLTGSLGMLPSASLGESGPGLYEPIH
GSAPDIAGKGIANPIATILSAAMMLRYSLGLEEAADAIEAAVEKVLAQGYRTADIAEGGGKVSTSEMGDA
ILAALAEG
>gnl|CDD|234833 PRK00773, rplX, 50S ribosomal protein LX; Validated
EMKIYRVKGTFLAGDEWQKFTKEVRALNEKDALEKVYSLFGSKHKVKRTQIKIEEVSEISPEEAEDPRVR
ELAKLD
>gnl|CDD|234834 PRK00777, PRK00777, pantetheine-phosphate adenylyltransferase
MMKVAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNLKKFLKAVEYDR
EYEIVKIDDPYGPALEDDFDAIVVSPETYPGALKINEIRRERGLKPLEIVVIDFVLAEDGKPISSTRIRR
GEIDEHGNLIKER
>gnl|CDD|234835 PRK00779, PRK00779, ornithine carbamoyltransferase; Provisional
MLMGRHFLSLDDLSPEELEELLDLAAELKKKRKAGEPHPPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGG
HAIFLSPRDTQLGRGEPIEDTARVLSRYVDAIMIRTFEHETLEELAEYSTVPVINGLTDLSHPCQILADL
LTIYEHRGSLKGLKVAWVGDGNNVANSLLLAAALLGFDLRVATPKGYEPDPEIVEKIAKETGASIEVTHD
PKEAVKGADVVYTDVWVSMGQEAEAEERLKAFAPYQVNEELMALAKPDAIFMHCLPAHRGEEVTDEVIDG
PQSVVWDEAENRLHAQKALLAWLL
>gnl|CDD|234836 PRK00782, PRK00782, MEMO1 family protein
MMRYPAVAGQFYPLSPEELLKMLSEFFRDLGEESRKIIGAVVPHAGYVYSGRTAARVYAALPEAETFVII
GPNHTGLGSPVAVSPEGWKTPLGDVEVDEELAKALASGIIDLDELAHKYEHSIEVQLPFLQYLFGKDFKI
VPICLGMQDEETAREVGEAIAEAIEELGKKVVVIASSDFTHYEPAERAKEKDMILIEAILDLDVDGFYDE
IYRMNATACGYGPIAAMMTYSKKLGASKAELLHYATSGDVSGDTSAVVGYAAIVFRR
>gnl|CDD|234837 PRK00783, PRK00783, DNA-directed RNA polymerase subunit D; Provisional
MEIEILELDDRSARFVVEGVTPAFANAIRRAMIADVPTMAIDDVRFYENTSVLFDEILAHRLGLIPLTTD
LDKYKPPEECTCEGEGCPDCTVTLSLEVEGPKTVYSGDLKSSDPDVKPVDPNIPIVKLKEGQKLVLEAYA
RLGRGKEHAKWQPGSACGYKYYPRIEVSEDCDECEKCVEACPRGVLELKEGKLVVTDLLNCSLCKLCERA
CPGKAIRVSDDENKFIFTVESDGSLPVEEILLEALKILKRKADELIEALEELA
>gnl|CDD|234838 PRK00784, PRK00784, cobyric acid synthase
MAKALMVQGTASDAGKSTLVAGLCRILARRGYRVAPFKAQNMSLNSAVTADGGEIGRAQALQAEAAGVEP
SVDMNPVLLKPQSDRGSQVIVQGKPVGNMDARDYHDYKPRLLEAVLESLDRLAAEYDVVVVEGAGSPAEI
NLRDRDIANMGFAEAADAPVILVADIDRGGVFASLVGTLALLPPEERARVKGFIINKFRGDISLLEPGLD
WLEELTGVPVLGVLPYLDDLRLPAEDSLALLERAARAGGGALRIAVIRLPRISNFTDFDPLRAEPGVDVR
YVRPGEPLPDADLVILPGSKNTIADLAWLRESGWDEAIRAHARRGGPVLGICGGYQMLGRRIADPDGVEG
APGSVEGLGLLDVETVFEPEKTLRQVTGLLLGSGAPVSGYEIHMGRTTGPALARPFLRLDDGRPDGAVSA
DGRVFGTYLHGLFDNDAFRRALLNWLGARKGLAPASALDYAALREAQLDRLADLVEEHLDLDALLALL
>gnl|CDD|179126 PRK00790, fliE, flagellar hook-basal body complex protein FliE
MIMDIRSVSALSAYAALSETVAEKSAAAAPAAAPAAPGASFASVLGQMAGDAVQTLKAAEATSIQAIKGK
ADTREVVDAVMQAEQALQTAVAIRDKVVEAYLEILRMPI
>gnl|CDD|179127 PRK00794, flbT, flagellar biosynthesis repressor FlbT; Reviewed
MSGLKLSLKPGERIFINGAVLRNDRKVSLELLNDATFLRERDVLQPEDATTPLRQLYFIAQLMLIGPAGA
EDARAEFARRLEQLLAVFTDPDILAGLKAIDELVEAGRYYEALKALRGLYPIEAELLAAVAS
>gnl|CDD|234839 PRK00801, PRK00801, hypothetical protein; Provisional
MYMLTDEEGEFAVRLARRAIEEYLRTGKVIEPPKDLPPVFWEKRGVFVTLNKHGVLRGCIGFPYPDSPLV
EAIIDSAISAATRDPRFPPVKLEEMDEITVEVTVLTPPELIEGPPEELPEKIEVGRHGLIVKKGIYSGLL
LPQVAPEWGFDSEEFLSHTCLKAGLPPDCWLDDAEVYRFEGQIFKEEEPRGEVVEKKLVSC
>gnl|CDD|234840 PRK00802, PRK00802, DNA-3-methyladenine glycosylase
MGMPLPREFFARDALEVARDLLGKVLVHEGGVSGRIVETEAYIGADDPASHSYRGRTPRTEVMFGPPGHA
YVYFIYGMHHCLNVVCGPEGTGAAVLIRALEPLEGIALMRRRRGGKRPEKNLCNGPGKLCKALGITLADN
GADLFDASPLYIEDGKEPPEIVAGPRIGISKARDLPWRFWIPGSPFVS
>gnl|CDD|234841 PRK00805, PRK00805, putative deoxyhypusine synthase; Provisional
MKPTVPIEVKERSISELLDAMADTGFQGRKLGESVRVWTEMLKDPDNTIFMGLSGAMVPAGMRKIIKWLI
RNRYVDVLVSTGANIFHDIHEALGFKHYKGSHHVDDEELFKEGIDRIYDVFAYEEEFRKADNLIAEFAET
LPGFKSYSSREFLYLLGKWLNEKDIDSIVAAAYRANVPIFVPALCDSSIGIGLVIARRRGHRVVIDQIKD
VDEITEIVEKSKKTGVIYIGGGVPKNFIQQTEVIASILGEDVEGHEYAIQYTTDAPHWGGLSGCTFEEAV
SWGKVAPKAKKVQVFVDATIALPLVAHALIEKGIKRRKAPDFSWLGKEL
>gnl|CDD|179131 PRK00807, PRK00807, 50S ribosomal protein L24e; Validated
TRTCSFCGKEIEPGTGKMYVKKDGTILYFCSSKCEKNYKLGRVPRKLKWTKA
>gnl|CDD|179132 PRK00808, PRK00808, bacteriohemerythrin
MALLVWQSDLNTGIDVIDQQHKRIVDYINHLHDAQDSPDRLAVAEVIDELIDYTLSHFAFEESLMEEAGY
PFLVPHKRVHELFIKRVEEYRERFQAGEDVADELHGMLSRWLFNHIRNDDAAYVDAVKANMDGISREKEG
GGWLARTLKR
>gnl|CDD|179133 PRK00809, PRK00809, hypothetical protein; Provisional
MTYWLCITNEDNWEVIKDKNVWGVPERYKNTIEKVKPGDKLIIYVSQEYGAERLPGKIVGIYEVVSEWYE
DSTPIFPAEPVRPKEIYPYRVKLKPVKIFEEPIDFKPLIPKLKFIENKKQWSGHLRNRAMRPIPEEDYKL
IEEC
>gnl|CDD|234842 PRK00810, nifW, nitrogenase stabilizing/protective protein NifW
SMTDMTDILDQLKRLSSAEEFFQLLGVPYDPKVVNVARLHILKRMGQYLAQEDFAGLPEAEARARCRAVL
ERAYADFVASSPLDQRVFKVLKDAVAPKKRAFVPLDSLKASEP
>gnl|CDD|234843 PRK00811, PRK00811, polyamine aminopropyltransferase
SMELWFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVP
LFAHPNPKRVLIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDG
IKFVAETENSFDVIIVDSTDPVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKE
VFPIVRPYQAAIPTYPSGLWSFTFASKNDDLKFLPLDVIEARFAERGIKTRYYNPELHKAAFALPQFVKD
ALK
>gnl|CDD|234844 PRK00816, rnfD, electron transport complex protein RnfD; Reviewed
AFKIASSPHTHNQRQTSRIMLWVILAALPGIAAQTYFFGWGTLIQILLAIVTALLAEAAVLKLRKRPVAA
TLKDNSALLTALLLAVSIPPLAPWWMIVIGTVFAIIIAKQLYGGLGQNPFNPAMVGYVVLLISFPVQMTS
WLPPIELAAEPPGFLDALSLIFTGHTADGFDMHQLRLGIDGISQATPLDTFKTSLRAGHTVEEILQQPIF
SGILAGVGWQWVNLAYLAGGLFLLWQKAIRWHIPVAFLATLALCATLGWLFSPDTLASPLLHLFSGATML
GAFFIATDPVTASTTPRGRLIFGALIGLLVYLIRSFGGYPDGVAFAVLLANICVPLIDYYTRPRVYGHRK
>gnl|CDD|179136 PRK00819, PRK00819, RNA 2'-phosphotransferase; Reviewed
LDGKRLEKLSKFLSGVLRHKPEAIGLTLDEEGWVDIDALIEALAKAYKWVTRELLEAVVESDDKGRFEIS
GDRIRARQGHSVDVDLDLEEDTPPAVLYHGTSSEELDSILEEGLKPMKRHYVHLSTDIETAREVGARHGS
PVILEVDAECMRKRGIKFYKAENGVWLTEYVPPEYLKEV
>gnl|CDD|234845 PRK00823, phhB, pterin-4-alpha-carbinolamine dehydratase; Validated
MMAEKLSDEEIAELLPQLPGWTLVGDRDAIERTFKFKNFNEAFAFMNRVAEIAEEEDHHPDWFNVYNRVT
VTLTTHDAGGLTENDFILAAKIDALAG
>gnl|CDD|179138 PRK00831, rpmJ, 50S ribosomal protein L36; Validated
MKVRNSLKSLKNRHRDCQVVRRKGRVYVINKKNPRFKARQG
>gnl|CDD|179139 PRK00843, egsA, NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
MFEKSHWIQLPRDVVVGHGVLDDIGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLEDAGDVEVVIVDE
ATMEEVEKVEEKAKDVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGKPV
SVKAKPPLAVIADTEIIAKAPYRLLAAGCGDIISNYTAVKDWRLAHRLRGEYYSEYAAALSLMTAKMLIE
NADIIKPGLEESARLVVKALISSGVAMSIAGSSRPASGSEHLFSHALDRLAPGPALHGEQCGVGTIIMMY
LHGGDWRKIRDALKKIGAPTTAKELGIDDEYIIEALTIAHTIRPERYTILGDRGLTREAAEKAARITGVI
>gnl|CDD|234846 PRK00844, glgC, glucose-1-phosphate adenylyltransferase; Provisional
RAMPKVLAIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHI
SQTWRLSGLLGNYITPVPAQQRLGKRWYLGSADAIYQSLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFH
IESGAGVTVAAIRVPREEASAFGVIEVDPDGRIRGFLEKPADPPGLPDDPDEALASMGNYVFTTDALVDA
LRRDAADEDSSHDMGGDIIPRLVERGRAYVYDFSTNEVPGATERDRGYWRDVGTIDAYYDAHMDLLSVHP
VFNLYNREWPIYTSSPNLPPAKFVDGGGRVGSAQDSLVSAGSIISGATVRNSVLSPNVVVESGAEVEDSV
LMDGVRIGRGAVVRRAILDKNVVVPPGATIGVDLEEDRRRFTVSEGGIVVVPKGQRV
>gnl|CDD|179141 PRK00846, PRK00846, hypothetical protein; Provisional
HEQLSLRDQALEARLVELETRLSFQEQALTELSEALADARLTGARNAELIRHLLEDLGKVRSTLFADPAD
EPPPPHY
>gnl|CDD|234848 PRK00854, rocD, ornithine--oxo-acid transaminase; Reviewed
PMNTSEDLIATEQRLGAHNYKPLDVVLTRGEGVWVWDTDGNRYLDCLSAYSAVNQGHCHPKILAAMVEQA
GRLTLTSRAFRNDQLAPLYEELAALTGSHKVLPMNSGAEAVETAIKAVRKWGYEVKGVPEGQAEIIVCAD
NFHGRTLSIVGFSTDPDARGGFGPFTPGFRVVPFGDAEALEAAITPNTVAFLVEPIQGEAGVIIPPAGYF
TRVRELCTANNVTLILDEIQTGLGRTGKLLAEEHEGIEADVTLIGKALSGGFYPVSAVLSNSEVLGVLKP
GQHGSTFGGNPLACAVARAALKVLTEEGMIENAAEMGAYFLEGLRSIRSNIVREVRGRGLMLAVELEPEA
GGARQYCEALKERGLLAKDTHDHTIRLAPPLVITREQVDWALEQIAKVLAH
>gnl|CDD|179143 PRK00855, PRK00855, argininosuccinate lyase; Provisional
MMSNKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILE
EIEAGKFEFSPELEDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKA
LLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPID
RERTAELLGFDGVTENSLDAVSDRDFALEFLSAASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSS
IMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRDLQEDKEPLFDAVDTLKLSLEAMAGMLET
LTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEERGVDLADLSLEELQAFSPLIT
EDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKARLA
>gnl|CDD|234849 PRK00856, pyrB, aspartate carbamoyltransferase catalytic subunit
NPLKMKHLLSIEDLSREEIELLLDTAEEFKEVLRREVKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRL
GADVINFSASTSSVSKGETLADTIRTLSAMGADAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQA
LLDLLTIREEFGRLEGLKVAIVGDIKHSRVARSNIQALTRLGAEVRLIAPPTLLPEGMPEYGVHTDLDEV
IEDADVVMMLRVQKERMDGGLLPSYEEYKRSYGLTAERLALAKPDAIVMHPGPVNRGVEIASDVADGPQS
VIFEQVTNGVAVRMAVLELLLGGRL
>gnl|CDD|234850 PRK00861, PRK00861, putative lipid kinase; Reviewed
MTRSACLIFNPVAGQGNPEVDLALIRAILEPEMDLDIYLTTPEIGADQLAQEAIERGAELIIASGGDGTL
SAVAGALIGTDIPLGIIPRGTANAFAAALGIPDTIEEACRTILQGKTRRVDVAYCNGQPMILLAGIGFEA
ETVEEADREAKNRFGILAYILSGLQQLRELESFEVEIETEDQIITTNAVAVTVANAAPPTSVLAQGPGAV
IPDDGLLDVTIVAPKNLAEAVAASYHLLQTALQGNPAERDDIGYLRAKQVKITTDPPQKVVIDGEVVGTT
PIEIECLPRSLKVFAPLQAE
>gnl|CDD|234851 PRK00865, PRK00865, glutamate racemase; Provisional
MSMMNAPIGVFDSGVGGLTVLREIRRLLPDEHIIYVGDTARFPYGEKSEEEIRERTLEIVEFLLEYGVKM
LVIACNTASAVALPDLRERYDIPVVGIVPAIKPAAALTRNGRIGVLATPGTVKSAAYRDLIARFAPDCQV
ESLACPELVPLVEAGILGGPVTLEVLREYLAPLLAAGIDTLVLGCTHYPLLKPEIQQVLGEGVTLIDSGE
AIARRVARLLEELNLLASSDENPAHRFFTTGDPEAFKRLAQRWLGLLEKVE
>gnl|CDD|179147 PRK00870, PRK00870, haloalkane dehalogenase; Provisional
MDVLRTPDSRFENLPDYPFAPHYVDVDDGDGGPLRMHYVDEGPADGPPVLLLHGEPSWSYLYRKMIPILA
AAGHRVIAPDLIGFGRSDKPTRREDYTYARHVEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRF
ARLVVANTGLPTGDGPMPDAFWAWRAFSQYSPVLPVGRLVNGGTVRDLSDAVRAAYDAPFPDESYKAGAR
AFPLLVPTSPDDPAVAANRAAWAVLERWDKPFLTAFSDSDPITGGGDAILQKRIPGAAGQPHPTIKGAGH
FLQEDSGEELAEAVLEFIRATP
>gnl|CDD|234852 PRK00871, PRK00871, glutathione-regulated potassium-efflux system oxidoreductase KefF
MILIIYAHPYPHHSHANKRMLEQARTLEGVEIRSLYQLYPDFNIDIAAEQEALSRADLIVWQHPMQWYSI
PPLLKLWIDKVLSHGWAYGHGGTALHGKHLLWAVTTGGGESHFEIGAHPGFDVLSQPLQATALYCGLNWL
PPFAMHCTFICDDETLEGQARHYKQRLLEWQEAHHG
>gnl|CDD|179149 PRK00872, PRK00872, hypothetical protein; Provisional
MDQPMAPTPELEYVFTITVRVGPPVEAGETGHGVRRIIPIIGGEVSGPGLSGRVLPGGADWQIIRPDGLT
DLEARYAIETDDGAVIYVENVGIRHGPPEVLQRLARGEPVDPKEYYFRTVPRFETGHPKYDWLMRHIFVG
SAARHPDRVVIDVYKVL
>gnl|CDD|179150 PRK00876, nadE, NAD(+) synthase
AAFSRDVLKIDAAAEAERIRAAIREQVRGTLRRRGVVLGLSGGIDSSVTAALCVRALGKERVYGLLMPER
DSSPESLRLGREVAEHLGVEYVVEDITPALEALGCYRRRDEAIRRVVPEYGPGWKSKIVLPNLLDGDGLN
VFSLVVQDPDGEVTRKRLPANAYLQIVAATNFKQRTRKMVEYYHADRLNYAVAGTPNRLEYDQGFFVKNG
DGAADLKPIAHLYKTQVYALAEHLGVPEEIRRRPPTTDTYSLPQTQEEFYFALPYDRMDLCLYALNHGVP
AEEVAAALGLTPEQVERVYRDIEAKRRTTRYLHAPPLLVEPVREIE
>gnl|CDD|234853 PRK00877, hisD, bifunctional histidinal dehydrogenase/ histidinol dehydrogenase; Reviewed
MIIIRWLSLSDAEFRAALPRRAREDDEDVEAAVREILEDVRERGDAALLEYTEKFDGVELESLRVSEEEI
EAAYERLDPELREALEEAAENIRAFHEAQKPESWDVETAPGVRLGQRWRPIERVGLYVPGGKAAYPSSVL
MNAIPAKVAGVKEIVMVTPPPDGEINPAILAAAALAGVDEVYKVGGAQAIAALAYGTESIPKVDKIVGPG
NIYVTAAKRLVFGVVGIDMIAGPSEILVIADETADPDFVAADLLSQAEHDPDAQSILVTTSEELAEAVAA
EVERQLATLPRAEIARASLEGQGAIILVDDLEEAIELSNAYAPEHLEIQTEDPRALLDRIRNAGAIFLGP
YTPESLGDYAAGPNHVLPTSGTARFSSGLSVYDFLKRSSVIELSKEGLKALGPAIVTLAEAEGLDAHARA
VRVRL
>gnl|CDD|234854 PRK00881, purH, bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
RRMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHP
KIHGGILARRDNPEHVAALEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNH
KDVAVVVDPADYDAVLEELKANGSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVGEEFPETLNLSFEK
KQDLRYGENPHQKAAFYRDPNAEGGVATAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCG
VAVGDTILEAYDKAYACDPVSAFGGIIAFNREVDAETAEAIHKIFLEVIIAPSFSEEALEILAKKKNLRL
LECPFPGGWEGDFKSVSGGLLVQDRDLGMVDPADLKVVTKRQPTEQELKDLLFAWKVVKHVKSNAIVYAK
DGQTVGIGAGQMSRVDSARIAIEKAGDAGLDLKGAVLASDAFFPFRDGVEAAAKAGITAIIQPGGSIRDE
EVIAAADEHGIAMVFTGVRHFRH
>gnl|CDD|234857 PRK00886, PRK00886, 2-phosphosulfolactate phosphatase family protein
MKIDVFHTAEDIPDGRLKPKTAVVIDVLRATSTIATALNNGAEAVIPFSDVEEALEKAKKWPAEKRLLGG
ERGGLKIEGFDLGNSPLEYTPEVVEGKRLFMTTTNGTRALKRVRKAKRILIAALINRSAVAEYLLSLNED
VWIVGSGTEGGFSLEDFLCAGALADRLLNNLEDELNDEAKAALALYEQWENDLEEILKKASHGQRLKSLG
LEEDLEYCAQKDILDVVPEQKEGGILKSAD
>gnl|CDD|179156 PRK00888, ftsB, cell division protein FtsB; Reviewed
MRLLTLLLLALLVWLQYSLWFGKNGILDYWRVNDQVAAQQQTNAKLKARNDQLFAEIDDLKGGQEAIEER
ARNELGMVKPGETFYRIVPDASKRAAAAGQPPRTA
>gnl|CDD|179157 PRK00889, PRK00889, adenylylsulfate kinase; Provisional
KQRGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVAN
LLTRHGVIVLVSAISPYRETREEVRANIGNFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPY
EPPLNPEVECRTDLESLEESVDKVLQKLEELGYLV
>gnl|CDD|234858 PRK00892, lpxD, UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
MSLTLAELAELLGAELVGDGDIEITGVASLEEAGPGQISFLANPKYRKQLATTKAGAVIVSPDDAEFVPA
GNALLVVKNPYLAFARLAQLFDPPATPSPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIG
AGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIGSDGFGFANDRGGWVKIPQLGRVIIGDDV
EIGANTTIDRGALDDTVIGEGVKIDNLVQIAHNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHL
EIGDGVTITAMSGVTKSIPEPGEYSSGIPAQPNKEWLRTAARLRRLDELRKRLKALEKKVEQL
>gnl|CDD|234859 PRK00893, PRK00893, aspartate carbamoyltransferase regulatory subunit; Reviewed
TMKNELQVEAIKNGTVIDHIPAGKGLKVLKLLGLTETDQRVTIGMNVPSKKLGRKDIIKIENRFLSEEEV
DQLALIAPNATINIIRDYEVVEKRKVELPEEIEGVLKCPNPNCITNTNEPVESRFYVVDKEPIKLRCKYC
EKEFSEDIVLEL
>gnl|CDD|234860 PRK00901, PRK00901, methylated-DNA--protein-cysteine methyltransferase; Provisional
MNNIYFYETPIGKIGIAENGTAITHLCFGEDKIPKDVTILETDLLKEANKQLEEYFEGKRKKFDLPLAPQ
GTEFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGG
LDIKEKLLKLEKENS
>gnl|CDD|179161 PRK00907, PRK00907, hypothetical protein; Provisional
MEIKSDNPDHGFQFPGTFELSAMGTAERGLETELPRLLAATGVELLQERISWKHSSSGKYVSVRIGFRAE
SREQYDAAHQALRDHPEVKWTL
>gnl|CDD|234861 PRK00911, PRK00911, dihydroxy-acid dehydratase; Provisional
MRSDMITKGVERAPHRSMLRATGLTDEDFDKPFIGIANSWNEITPCNIHLNELADAVKEGVRAAGGVPFE
FNTIGVSDGIAMGHEGMKYSLVSREVIADSIETVVNAHWFDGLVAIPGCDKNMPGMLMAAARLNVPSIFV
YGGPILPGRLKGKDLTLVSVFEAVGAYAAGKISEEELKEIERNACPGAGSCGGMFTANTMACLIEALGMS
LPGSGTIPAVDAERDELAREAGEAVVELLEKDIKPRDILTREAFENAIAVDMALGGSTNAVLHLLAIAHE
AGVDLTLDDFNRISKRTPHLADLKPSGKYVMEDLHEAGGIPAVMKELLDAGLLHGDCLTVTGKTLAENLA
DAPDPDQDVIRPLDNPISPTGGLAILKGNLAPEGAVVKIAGVKPEMFTGPARVFDSEEEAMEAILAGKIK
AGDVVVIRYEGPKGGPGMREMLAPTSAIVGAGLGDDVALITDGRFSGGTRGLCVGHVSPEAAVGGPIALV
EDGDIITIDAPNRTLDVLVSDEELARRRAAWKPPEPKYKRGVLAKYAKLVSSASTGAVTDPP
>gnl|CDD|234862 PRK00912, PRK00912, ribonuclease P protein component 3; Provisional
MKFYDLNVHAVPDGYDTVLRLISEASHLGYSGIALSNHSDKYPESKPELEDLLGFEIFRGVEIVASNPSK
LRGLVGKFRKKVDVLAVHGGDEKVNRAACENPRVDILSHPYTKRKDSGINHVLAKEAARNNVAIEFNLRD
ILKSRGGRRARTLSNFRDNLALARKYDFPLVLTSGAMSCYDLRSPREMIALAELFGMEEDEALKALSYYP
ESIIKKNRNRKNYVIEGVEIVEGESDF
>gnl|CDD|234863 PRK00913, PRK00913, multifunctional aminopeptidase A; Provisional
MEFSVKSGSPEKQKSDCLVVGVPERLSPAAEQLDKASDGYLSALLKRGDFKGKAGETLLLHAVPGVLAER
VLLVGLGKEEELDEEQLRKAAGKAARALKKTKVKEAVIFLTELHTYWKARAAAEGALLGLYRFDKYKSKK
EPRRPLEKLVFLVPTRLTEAEKAIAHGEAIAEGVNLARDLVNEPPNILTPAYLAERAKELAKEYGLEVEV
LDEKEMEKLGMGALLAVGQGSANPPRLIVLEYKGGKKPIALVGKGLTFDSGGISLKPAAGMDEMKYDMGG
AAAVLGTMRALAELKLPVNVVGVVAACENMPSGNAYRPGDVLTSMSGKTIEVLNTDAEGRLVLADALTYA
ERFKPDAIIDVATLTGACVVALGHHTAGLMSNNDELADELLKAGEESGERAWRLPLGDEYQEQLKSPFAD
MANIGGRPGGAITAACFLSRFVEKYPWAHLDIAGTAWNSKAWGYNPKGATGRGVRLLVQFLEN
>gnl|CDD|234864 PRK00915, PRK00915, 2-isopropylmalate synthase; Validated
MMDRVIIFDTTLRDGEQSPGASLTVEEKLQIAKQLERLGVDVIEAGFPASSPGDFEAVKRIARTVKNSTV
CGLARAVKKDIDAAAEALKPAEAPRIHTFIATSPIHMEYKLKMSREEVLEMAVEAVKYARSYTDDVEFSA
EDATRTDLDFLCRVVEAAIDAGATTINIPDTVGYTTPEEFGELIKTLRERVPNIDKAIISVHCHNDLGLA
VANSLAAVEAGARQVECTINGIGERAGNAALEEVVMALKTRKDIYGVETGINTEEIYRTSRLVSQLTGMP
VQPNKAIVGANAFAHESGIHQDGVLKNRETYEIMTPESVGLKANRLVLGKHSGRHAFKHRLEELGYKLSD
EELDKAFERFKELADKKKEVFDEDLEALVEDETQQEEPEHYKLESLQVQSGSSGTPTATVKLRDIDGEEK
EEAATGNGPVDAVYNAINRIVGSDIELLEYSVNAITGGTDALGEVTVRLEYDGRIVHGRGADTDIVEASA
KAYLNALNKLLRAKEVAKPKQRK
>gnl|CDD|234865 PRK00923, PRK00923, sirohydrochlorin nickelochelatase
MLGLLLVGHGSRLPYNKEVVTKIAEKIKEKHPFYIVEVGFMEFNEPTIPEALKKLIGTGADKIIVVPVFL
AHGVHTKRDIPRILGLDEGEKEEIEEDGKDVEIVYAEPLGADERIADIVLKRANEA
>gnl|CDD|179169 PRK00924, PRK00924, 5-keto-4-deoxyuronate isomerase; Provisional
MEVRYAIHPEDAKTLDTEGLREEFLIEKLFVADEITLVYSHYDRIIVGGAMPVTKPLKLEAGKQLGVSYF
LERRELGIINIGGAGTVTVDGETYELGHRDALYVGKGAKEVVFASADAANPAKFYLNSAPAHTTYPTKKI
TIADASPVTLGDLETSNRRTINKYIHPDVLETCQLVMGLTELEPGSVWNTMPCHTHDRRMEVYFYFDMPE
DARVFHFMGEPQETRHIVVHNEQAVISPSWSIHSGVGTSNYTFIWGMAGENQDFDDMDHVAMKDLR
>gnl|CDD|234866 PRK00927, PRK00927, tryptophanyl-tRNA synthetase; Reviewed
KKRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYECFFCIADLHALTVPQDPEELRENTRELAADYLACGI
DPEKSTIFVQSHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKAD
LVPVGEDQKQHLELTRDIARRFNNLYGEVFPVPEPLIPKVGARVMGLDGPTKKMSKSDPNDNNTINLLDD
PKTIAKKIKKAVTDSERLREIRYDLPNKPEVSNLLTIYSALSGESIEELEAEYEAGGKGYGDFKKDLAEA
VVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASKTLKEVREAMGLLRK
>gnl|CDD|234867 PRK00933, PRK00933, ribosomal biogenesis protein; Validated
MIITTSRKPSQRTRSLVKDLARFLNCKYVNRGKMSLQELLEECEARYLLIIGEYKGNPGALKFYDVEGNK
LLSYRLSVKLQREISGPVFKNRRPIKSAFDVGGDELAELFDYFLFYDLDEVRGLFDTVCLIEDGDIVLEF
LGSDKSLFIGPRLKIKGIKKMDYRE
>gnl|CDD|234868 PRK00934, PRK00934, ribose-phosphate pyrophosphokinase; Provisional
MIIGGSASQLLASEVARLLNTELALVETKRFPDGELYVRILGEIDGEDVVIISTTYPQDENLVELLLLID
ALRDEGAKSITLVIPYLGYARQDKRFKPGEPISARAIAKIISAYYDRIITINIHEPSILEFFPIPFINLD
AAPLIAEYIGDKLDDPLVLAPDKGALELAKEAAEILGCEYDYLEKTRISPTEVEIAPKNLDVKGKDVLIV
DDIISTGGTMATAIKILKEQGAKKVYVACVHPVLVGDAILKLYNAGVDEIIVTDTLESEVSKISVAPLIA
DLLKK
>gnl|CDD|179173 PRK00939, PRK00939, stress response translation initiation inhibitor YciH
SEICPVCGLPKELCVCEEVAKEQQRIKIKVDKRRYGKEVTIIEGIDPKDIDLKELAKKLKSKLACGGTVK
DGRIELQGDHRERVKELLIKMGFSEENIE
>gnl|CDD|234869 PRK00942, PRK00942, acetylglutamate kinase; Provisional
MIDALEKAEVLSEALPYIQRFMGKTIVIKYGGNAMTDEELKEAFARDIVLLKQVGINPVVVHGGGPQIDE
LLKKLGIESEFVNGLRVTDAETMEVVEMVLAGKVNKELVSLINKHGGKAVGLSGKDGGLITAKKLEEDED
LGFVGEVTPVNPALLEALLEAGYIPVISPIGVGEDGETYNINADTAAGAIAAALGAEKLILLTDVPGVLD
DKGQLISELTASEAEELIEDGVITGGMIPKVEAALDAARGGVRSVHIIDGRVPHALLLELFTDEGIGTMI
VPD
>gnl|CDD|234870 PRK00943, PRK00943, selenide, water dikinase SelD
MSEEAIRLTQYSHGAGCGCKISPKVLETILASEQAKFVDPNLLVGNETRDDAAVYDLNDGTGIISTTDFF
MPIVDDPFDFGRIAATNAISDIYAMGGKPIMAIAILGWPINKLPPEVAREVLEGGRAACRQAGIPLAGGH
SIDAPEPIFGLAVTGVVPPERVKRNATAQAGDKLFLTKPLGIGILTTAEKKSKLKPEHYGLAIEAMCQLN
RPGADFAKLPGVHAMTDVTGFGLLGHLLEMCQGAGLTARVDYAAVPLLPGVEEYIAQGCVPGGTGRNFAS
YGHLIGELPDEQRALLCDPQTSGGLLVAVAPEAEAEVLAIAAEHGIELAAIGELVEARGGRARVEVR
>gnl|CDD|234871 PRK00944, PRK00944, hypothetical protein; Provisional
MSAAGAEFRVRRASFWLLAALAVLALQALILYAMGRVPICECGYVKLWHGVVNSSENSQHLSDWYTPSHI
IHGFLFYGLGHLVLRRKPLGARLLLATLIESAWELLENSPLIIERYRAATISLDYYGDSILNSVMDTLAM
VLGFLFAARLPVWLTVAIAIFFEIFTGWLIRDNLTLNVLMLVWPVEAIKQWQAGL
>gnl|CDD|234873 PRK00951, hisB, imidazoleglycerol-phosphate dehydratase HisB
MMRTAEVERKTKETDISVELNLDGTGKSDIDTGVGFLDHMLDQFARHGLFDLTVKAKGDLHIDDHHTVED
VGIVLGQALKEALGDKKGIRRYGHAYVPMDEALARVAVDLSGRPYLVFDVEFTREKIGTFDTELVREFFE
AFANNAGITLHIRVLYGRNAHHIIEALFKAFARALRMAVEIDPRVAGVPSTKGVL
>gnl|CDD|179181 PRK00956, thyA, thymidylate synthase; Provisional
IMLCIKKKSVASAWERLVPKIMNEGEEITDERGSKTKEIMNTIIEITNPKLKSIPEKYPLGEEALEEYTK
QLLSGSAQGFVYTYGERLREYPGEVDQIDYIIEKLKENKNSRRATAVTWNPYIDTKVDEVPCLQLVDFLI
RDGKLYLTVLFRSNDAGGAFHANAIGLIKLGEYVAEKVGVELGTYTHHSVSAHIYERDWDYLEKIFKG
>gnl|CDD|234875 PRK00957, PRK00957, methionine synthase; Provisional
IMITTVVGSYPVVKGEPETLKDKIKGFFGLYDPYKPAIEEAVADQVKAGIDIISDGQVRGDMVEIFASNM
PGFDGKRVIGRVEPPAKPITLKDLKYAKKVAKKKDPNKGVKGIITGPSTLAYSLRVEPFYSDNKDEELIY
DLARALRKEAEALEKAGVAMIQIDEPILSTGAYDLEVAKKAIDIITKGLNVPVAMHVCGDVSNIIDDLLK
FNVDILDHEFASNKKNLEILEEKDLIGKKIGFGCVDTKSKSVESVDEIKALIEEGIEILGAENILIDPDC
GMRMLPRDVAFEKLKNMVEAAREIR
>gnl|CDD|234876 PRK00960, PRK00960, seryl-tRNA synthetase; Provisional
LKFKLKGKIIFSKDVTEEAKKDIEEFLEEANRDILLKGVPEGKEKEAAKIKSYEFEGNTLKLEIESGRYV
RAHEALLRLRKPLAEKLGRKYRIGIRGIEIDNYVITIPADGEKVIELEGLKVPPCVVEIEGEKGTIILIF
KDVGESELKRNIIDRAIKLVEEKLEKLEDLTFYVGKAEPGTIVSESKKREITFDGDPTEEAEKLGWVKRF
PGRGQWFYTPPMTKLFRAFEKLVIEEVLKPLGFDECLFPKLIPLEVMYKMRYLEGLPEGMYYVCPPKRDP
EYFEEFVDEMMVKKEVPIEKLKEKLRDPGYVLAPAQCEPFYQFFQGETVDVDELPIKFFDRSGWTYRWEG
GGAHGLERVNEFHRIEIVWLGTPEQVEEIRDELLKYAHILAEKLDLEYWREVGDDPFYLEGRGLEDRGIE
FPDVPKYEMELWLPYRGDERKWVAVTSANVHGTHFVEGFNIKDYKGRKLWTGCTGYGLERWVIGFLAQKG
FDPENWPEEIRKRVGELPEGPKFLTWP
>gnl|CDD|179184 PRK00961, PRK00961, H(2)-dependent methylenetetrahydromethanopterin dehydrogenase; Provisional
MKVAILGAGCYRTHAASGITNFSRACEVAKEVGKPEIAMTHSTITMGAELLHLAPGVDEVVVSDPCFAEE
PGFVVIDDFDYKEVMEAHLAGNPEKVMPKIREKVKAKAKELPKPPKGCIHFVHPEDLGLKVTTDDREAVA
DADIVITWLPKGGMQPDIIEKFADDIKEGAIVTHACTIPTTKFAKIFKDLGRDDLNVTSYHPGAVPEMKG
QVYIAEGYADEEAVEKLYEIGKKARGNAFKMPANLIGPVCDMCSAVTAIVYAGILAYRDAVTQILGAPAD
FAQMMADEALTQITALMREEGIDNMEEALDPGALLGTADSMCFGPLADILPTALKVLEKHKK
>gnl|CDD|179185 PRK00962, PRK00962, hypothetical protein; Provisional
MITVATAECFTHGKIGREIHKIACGYPELEKKSNYSEINGNVSVVASMFIPSLSGIESLLDIEPPEPDYV
YKYIKAYNEENDLLVAKLMAEALKNKTNCDIAIGTTAGIGRGAICIVTDKNEYLFTSDVYADLITAENIL
KRQKNGIEKALKKFLEILKKEYFLK
>gnl|CDD|234877 PRK00964, PRK00964, tetrahydromethanopterin S-methyltransferase subunit A; Provisional
MADKKEPAEGWPIVKGDYVVGDPESPVAVVTLGSHLLDQPIIDAGAAISGPCHTENLGIEKVIANVISNP
NIRFLILCGSEVQGHITGQSLKALHENGVDDDGRIIGAKGAIPFLENVPDEAVERFQEQIEIVDLIDTED
PGAITAKIKECIAKDPGAFDEEPMVVELEEIGGEEEEEEGGPKADPAEEAVEARIRAIERKIEGIGRLNK
YSAGVYAGKIEGIMI
>gnl|CDD|179187 PRK00965, PRK00965, tetrahydromethanopterin S-methyltransferase subunit B; Provisional
MPIVKIAPEINLVMDPDTGLIAEMREDIIVVDMDPIEEEINKLEALADDLENSLDPRNPPLNSYPGREGT
YYIAGIFTNMFYGFWIGLAILFLLAI
>gnl|CDD|179188 PRK00967, PRK00967, hypothetical protein; Provisional
MLVTTTENIPGKEIIEVIGEVFGLTTQSKNIVRDIGAGLKNVVGGEIKGYTEMLTEARDIAIDRMKEEAK
QKGANAIVGMRFDSSSIRDGMQSVAAYGTAVKIED
>gnl|CDD|234880 PRK00971, PRK00971, glutaminase; Provisional
MMLMQAILEEILEEVRPLIGQGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFS
LALALQHYGEEEVWQRVGKEPSGDPFNSLVQLELEQGKPRNPMINAGAIVVTDLLQGRLSEEPCERLLEF
VRQLAGNPDILYDEVVASSELEHADRNAAIAYLMKSFGNIENDVETVLDTYFHQCALEMSCVDLARAGLF
LANGGVSPHTGERVVSPRQARQVNALMLTCGMYDASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSP
ELDAKGNSLAGTAALERLSQRLGLSIF
>gnl|CDD|179193 PRK00973, PRK00973, glucose-6-phosphate isomerase; Provisional
MMLKFDFSNVFEPNIGGGISIEDIESVKEKITSAVENLMEKEPNGELGFLELPYDRSLDSYEELKEWSKN
FDNVVVLGIGGSALGNLALHYALNPLNWNELSKEERNGPRVFVLDNVDPEKTASILDVIDLEKTLFNVIS
KSGNTAETLANYLIIRGILEKLGLDPKKHLVFTTDPEKGKLKKIAEKEGYRTLEIPENVGGRFSVLTPVG
LAPAAALGIDIEELLEGAKEMDKICEKEDIFKNPALLNALIHYLYYNRGKNISVMMPYSERLKYFGDWYR
QLWAESLGKKGVGQTPVKALGATDQHSQLQLYMEGPKDKIITFLKVEKYRRDVEIPYEYEDIEELSYLGG
HKLSELINSEQKGTEIALTENGRPNVKITLDELNEYTVGQLFYMYEMQTAFMGELLNINAFDQPGVELGK
KITYALLGRSGYEEEKKEIEKKVIIE
>gnl|CDD|179195 PRK00977, PRK00977, exodeoxyribonuclease VII small subunit; Provisional
TMPAKKSKPLSFEEALAELEEIVTRLESGDLPLEESLAAFERGVALARQCQKKLQQAEQRVEKLLDEDGK
EASLEPFDPD
>gnl|CDD|234883 PRK00979, PRK00979, tetrahydromethanopterin S-methyltransferase subunit H; Provisional
MFKFDKEQKVYDIGGVKIGGQPGEYPTVLIGSIFYAGHKIVSDEKKGIFDKEKAEALINRQEELSDKTGN
PALLDVVGESPEAMEKYIDFVSEITDLPFLIDSTSPEARIAAAKYATELGLADRAIYNSINPSIEEEEIE
ALKESDIKAAIVLAFDPMDPSVEGRLKMLEEGGKGQDKGMLPLAEEAGIERPLVDTAVTPLPGSGAAIRA
IFAVKAKFGYPVGCAPHNAPSAWDWLREFKGKEAFAVCDIGANLVARILGADFLLYGPIENAEEAFPAVA
MTDIFIAEAAKELGGEPVDENHPLNKLF
>gnl|CDD|179197 PRK00982, acpP, acyl carrier protein; Provisional
MSEIFEKVKKIIVEQLGVDEEEVTPEASFVDDLGADSLDTVELVMALEEEFGIEIPDEDAEKIKTVGDAV
DYIEKHQK
>gnl|CDD|234884 PRK00984, truD, tRNA pseudouridine synthase D; Reviewed
MMEFGNLLYLHGKPGITGRLKANPEDFVVREILGFEPSGEGEHLLVRIRKRGWNTLFVARALAKFLGISL
RDVGYAGLKDRHAVTTQWFSIHLPGKEEPDLSAFQLEGLEILELGRHNRKLRLGDLKGNRFTIRLREVSK
DRDKVEQRLEEIAAGGVPNYFGEQRFGSGGKNLQEALRWANGEKKVLDRNLRSFFLSAAQSYLFNRILSE
RLEKGLPLNQVLEGDALQLAGRGSWFVAEELEEELQRRLKRGDLHITAPLPGSGELGTQGEALAIEQEIL
AEETALFALLGREKVEGARRAILLYPQNLSWNDDETLELEFWLPKGSYATSVLRELLKTDP
>gnl|CDD|234885 PRK00994, PRK00994, F420-dependent methylenetetrahydromethanopterin dehydrogenase
MVVKIGIIKLGNIGMSPVIDLLLDERADREDIDVRVVGSGAKMGPEEVEEVVKKMLEEWKPDFVIVISPN
PAAPGPKKAREILKAAGIPCIVIGDAPGKKVKDAMEEQGLGYIIVKADPMIGARREFLDPVEMALFNADV
LKVLAGTGAVRLVQEELDKVIDQVKEGKEIELPKIVITAEKAVEAAGFSNPYAKAKAMAAYEIAEKVADI
DVKGCFMTKEMEKYIPIVASAHEMMRAAAKLADEAREIEKANDTVLRKPHAKDGKILSKTKLMEKPE
>gnl|CDD|234887 PRK01001, PRK01001, putative inner membrane protein translocase component YidC; Provisional
MNKRTLLFVSLVSAAFLGCQIFFGYRDFRSCQDLAEKQRAISEQILAATESVGLSVVPWTTSLEEEESKN
QYAVRVGDRLLLLTQGGSAPSVYSSGTSWSFIEQTSTFDNIHVALYGEQGQSVLPSKTGSVFLPNQRDAL
PVLVVEFRSNQEPLVFLGEYKDGKISNKDSAIYGTALVFLRSGNGYLPLGIYNSKEECLESLDLPMTRAV
VFADKEDAAKPTASGSYYVLSNEYMQLVVSQESGAIEGINLPFASDENNKSIVNEIGFDRELASQHPSEA
SFPGLSSITPQRQQIKNFVGGYYPLLRRGLLSDSKKQVPPQYHALNIVSGRELAEPVALGYRVVSFDNKS
IILESNDRSIRKTYSLGEPEEQPYAFELAIQLTGDSEDLWITSGVPEVEIMSNAFAPAIKYRVIKKNKSE
LDKVKLPKAKDPLAVRSGVYPQWILNSNGYFGIILTPLTPIPAGYASSYIPGNVVPTRLSQLSPKNQAYP
ASKYPGYEAMLPLPKEAGTYRFLVYAGPLADPTLKTLDRAYTNSKGENPEYLDSITFRGFFSFITEPFAA
LLFIIMKFFKFLTGSWGISIILLTVFLKLLLYPLNAWSIRSMRRMQKLSPYIQEIQQKYKKEPKRAQMEI
MALYKTNKVNPITGCLPLLIQLPFLIAMFDLLKSSFLLRGASFIPGWIDNLTAPDVLFSWETPIWFIGNE
FHLLPILLGVVMFAQQKISSLKRKGPVTDQQRQQEAMGTMMALLFTFMFYNFPSGLNIYWLSSMLLGVIQ
QWVTNKILDSKHLKNEVVPNKKKHR
>gnl|CDD|179203 PRK01002, PRK01002, nickel responsive regulator; Provisional
MTEMMRISISLPDKLLGEFDEIIEERGYASRSEGIRDAIRDYIIKYKWMNSMEGERVGTISVIYDHHSTG
VMEKLTDIQHDYSDLIVASLHIHLDHDHCLEVIVVRGDAKEIRELTEKLMALKGVKHVKLTTMVPGGNIP
E
>gnl|CDD|179204 PRK01005, PRK01005, V-type ATP synthase subunit E; Provisional
MADLSAQDKLKQICDALREETLKPAEEEAGAIVHNAKEQAKRIIAEAQEEAEKIIRSAEETADQKLKQGE
SALVQAGKRSLESLKQAVENKIFRESLGEWLEHVLTDPEVSAKLIQALVQAIEAQGISGNLTAYIGKHVS
ARAVNELLGKEVTKKLKEKGVSVGSFVGGAQLKVEEKNWVLDLSSQTLLDLLTRYLQKDFREMIFQG
>gnl|CDD|134464 PRK01008, PRK01008, queuine tRNA-ribosyltransferase; Provisional
MALKFELLHQSKKSRARVGRIETAHGIIDTPAFVPVATNGALKGVLDHSNIPLMFCNTYHLLVHPGTEAI
AAMGGLHQFIGRNAPIITDSGGFQIFSLAYGSVAEEIKSCGKKKGGSSILKITDEGVWFKSYRDGRKLFL
SPEISVQAQKDLGADIIIPLDELLPFHADPTYFLQSCQRTYVWEKRSLDYHLKNPRHQSMYGVIHGGIDP
DQRKIGCKFVEDLPFDGSAIGGSLGKNLQEMVEVVGVTTSNLSKERPVHLLGIGDLPSIWATVGFGIDSF
DSSYPTKAARHGLILTKQGPLKINNQRYSSDLNPIEPGCSCLACSSGISRAYLRHLFKVHEPNAGIWASI
HNLHHMQQVMKEIREQILNDRI
>gnl|CDD|179205 PRK01018, PRK01018, 50S ribosomal protein L30e; Reviewed
MMDFNRELRVAVDTGKVILGSKRTIKAIKLGKAKLVIVASNCPKDIKEDIEYYAKLSGIPVYEYEGSSVE
LGTLCGKPFTVSALAIVDPGESDILELIK
>gnl|CDD|167141 PRK01021, lpxB, lipid-A-disaccharide synthase; Reviewed
MFPQKLVLWLYPLGLFANLFFGSAFCIQWFLSKKRKYSYVPKIFWILSSIGAVLMICHGFIQSQFPIALL
HSFNLIIYFRNLNIASSRPLSVSKTLSLLVLSATAITLPFAIGTRYYPNMTWMASPNIFHLPLPPANLSW
HLIGCIGLTIFSLRFFIQWFYLEYNNQSALPALFWKASLLGGSLALLYFIRTGDPVNILCYGCGLFPSLA
NLRIAYKEARRKPFSNTSCFISAGEHSGDTLGGNLLKEIKALYPDIHCFGVGGPQMRAEGFHPLFNMEEF
QVSGFWEVLLALFKLWYRYRKLYKTILKTNPRTVICIDFPDFHFLLIKKLRKRGYKGKIVHYVCPSIWAW
RPKRKTILEKYLDLLLLILPFEQNLFKDSPLRTVYLGHPLVETISSFSPNLSWKEQLHLPSDKPIVAAFP
GSRRGDILRNLTIQVQAFLASSLASTHQLLVSSANPKYDHLILEVLQQEGCLHSHIVPSQFRYELMRECD
CALAKCGTIVLETALNQTPTIVTCQLRPFDTFLAKYIFKIILPAYSLPNIILGSTIFPEFIGGKKDFQPE
EVAAALDILKTSQSKEKQKDACRDLYQAMNESASTMKECLSLIFETAS
>gnl|CDD|234888 PRK01022, PRK01022, hypothetical protein; Provisional
AGAMTKGELGEKLKEEALEYSIYDLMKARVFLEKDIKYLPEKYREKYIESFFEYLFGTLNEIKSGSFSEI
EDPEIDEEEFKEFLARIEDQCENPDPGEPRFRLLYKLVSPYLIFILKEPLHPVGTPFPGGFKVEEKNGVY
YCPVKDKQKDVDFSLCEFCPAKQTPEL
>gnl|CDD|179207 PRK01024, PRK01024, Na(+)-translocating NADH-quinone reductase subunit B; Provisional
MLKKFVDSLWKICQKDKFQRFTPIADAIDTFCYEPIHTPSSPPFIRDAVDVKRWMMLVVIALFPAIFVAI
WNSGLQALVYQSGDPRLMEAFLHISGFKSYFSFVSKEIGIGSILWAGCKIFLPLLFISYAVGGTCEVLFA
IIRKHKIAEGLLVTGILYPLILPPTIPYWMAALGIAFGVVVGKELFGGTGMNILNPALSGRAFLFFTFPA
KMSGDVWVGSNPSRIKESLLKMNSLAGKSHIDGFSQSTCLQTLNSTPPSVKRVHVDAIASNILHLEHVPT
QDVIQSQFSTWTESHPGLTLDQLTLEQLQNFVTTPLAEGGLGLLPTQFDSAYSITDVIYGIGKFSTGNLF
FGNILGSLGETSTFACLLGAIFLILTGIASWRTMLSFGLGAFFTAWLFKIMSILIVGNAGAWAPAKFFIP
AYRHLFLGGLAFGLVFMATDPVSSPTMKLAKWIYGAFIGFMTIVIRLINPAYPEGVMLAILLGNVFAPLF
DYFAVRKYRQRRI
>gnl|CDD|179208 PRK01026, PRK01026, tetrahydromethanopterin S-methyltransferase subunit G; Provisional
MAEDEKIPQVVVDPKDFKEIQKRLDEIEEKVEFTNAEIFQRIGKKVGRDIGILYGLVIGLLIVLVYIILS
PIFMIIK
>gnl|CDD|234889 PRK01029, tolB, Tol-Pal system protein TolB
MLRSLVFLRFLFCLLCLLPSLYAEELEVRVRSESSLLPIAVSLLTSPKDAKQQSYLRSLEDIFAFDLALG
DLLQPTKESKESSAPLFIFIEAHYPELVFSLKKEGKNPQKLFSLELSGDLSKDRQKIHEAADTIHYALTG
VPGISSGKIIFSLSTTNSDTELKQGELWSVDYDGQNLRPLTQEHSLSITPTWMHIGSGFPYLYVSYKLGV
PKIFLGSLENPAGKKILALQGNQLMPTFSPRKKLLAFISDRYGNPDLFIQSFSLETGAIGKPRRLLNEAF
GTQGNPSFSPDGTRLVFVSNKDGRPRIYIMQIDPEGQSPRLLTKKYRNSSCPAWSPDGKKIAFCSVIKGV
RQICVYDLATGRDYQLTTSPENKESPSWAIDSLHLVYSAGNSNESELYLISLITKKTRKIVIGSGEKRFP
SWGAFPSQ
>gnl|CDD|234892 PRK01037, trmD, tRNA (guanine-N(1)-)-methyltransferase/unknown domain fusion protein; Reviewed
MEIDILSLFPDYFDSPLQASILGRAIKQGLLSVQSRDIREFGLGKWKQVDDAPFNGEGMLLMAEPVVQAI
RSVRREKSKVIYLSPQGQLLTAKKSRELASCSHLILLCGHYEGIDERALESEVDEEISIGDYVLTNGGIA
ALVLIDALSRFIPGVLGNQESAEYDSLENGLLEGPQYTRPRVFEGKEVPEVLLQGDHQAIADWRKQVSLE
RTRERRPDLYLQYLYGRSADCLFTQEDLPKIEVFSPKTFSVVLEVQDLRRAKKFYSKMFGLECWDGDKLF
LLGKTSLYLQQTKAEKKNRGTTTLSLELECEHDFVRFLRRWEMLGGELGEQADGHFPLRLVFDLDGHIWV
VSCVQKK
>gnl|CDD|234893 PRK01045, ispH, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Reviewed
MKILLANPRGFCAGVDRAIEIVERALEKYGAPIYVRHEIVHNRYVVERLEKKGAIFVEELDEVPDGAIVI
FSAHGVSPAVREEAKERGLTVIDATCPLVTKVHKEVARMSREGYEIILIGHKGHPEVEGTMGQAPGGVYL
VESPEDVAKLEVKDPDKLALVTQTTLSVDDTAEIIAALKERFPEIQGPPKDDICYATQNRQEAVKELAPQ
ADLVIVVGSKNSSNSNRLREVAEEAGAPAYLIDDASEIDPEWFKGVKTVGVTAGASAPEWLVQEVIARLK
ELGATVVEEVEGREENIV
>gnl|CDD|234894 PRK01059, PRK01059, ATP:guanido phosphotransferase; Provisional
MKLPNDALSNWMKGDGPDSDIVLSSRIRLARNLKDIPFPNKLSEEEARDIIELVEKAFLNNEIEGFGEFE
LLKLKDLDPLEKEVLVEKHLISPDLAENPEGGAVLLNEDETISIMINEEDHLRIQCIDPGLQLEEALEKA
NQIDDLLEEKLDYAFDEKLGYLTSCPTNVGTGLRASVMLHLPALVLTKRINRILQAINQLGLTVRGIYGE
GSEALGNIYQISNQITLGKSEEEIISNLRSVVNQIISQERAAREKLVKENKIELEDRVYRSYGILTNARL
ISSKEALDLLSDVRLGIDLGIIKDISNNKLNELMVLIQPAHLQKYAGRELDPEERDIKRAKLIRER
>gnl|CDD|179214 PRK01060, PRK01060, endonuclease IV; Provisional
MKLIGAHVSAAGGLEGAVAEAAEIGANAFMIFTGNPQQWKRKPLEELNIEAFKAACEKYGISPEDILVHA
PYLINLGNPNKEILEKSRDFLIQEIERCAALGAKLLVFHPGSHLGDIDEEDCLARIAESLNEALDKTQGV
TIVLENTAGQGSELGRRFEELARIIDGVEDKSRVGVCLDTCHAFAAGYDLREDFEGVLAEFDRIVGLDRL
KVMHLNDSKNEFGSRKDRHANLGEGTIGFDALRYIVHDPRFDGIPKILETPYVGEIWKEEIAMLREQQFD
P
>gnl|CDD|234895 PRK01061, PRK01061, Na(+)-translocating NADH-quinone reductase subunit E; Provisional
MWLGDYSWLNLFGIFLQATFIQNILLSNFLGMCSYLACSSRLSTANGLGMSVALVLTVTGSINWFVHAFI
TGPGALTWLSPALANVNLSFLELIIFIVVIAAFTQILELLLEKVSRNLYLSLGIFLPLIAVNCAILGGVL
FGITRNYPFIPMMIFSLGAGCGWWLAIVLFATIREKLAYSDVPKNLQGMGISFITTGLIAMAFMGLTGID
ISKPSTSIQRAPLETAVVENIATPSPQPNSKSQS
>gnl|CDD|179216 PRK01064, PRK01064, hypothetical protein; Provisional
MKEFLAYIVKNLVDRPEEVHIKEVQGTHTIIYELTVAKPDIGKIIGKEGRTIKAIRTLLVSVASRNNVKV
SLEIMEEK
>gnl|CDD|167150 PRK01066, PRK01066, porphobilinogen deaminase; Provisional
DCYNDPFLSDFCLGKRPLRIASRQSSLAVAQVHECLRLLRSFFPKLWFQISTTTTQGDLDQKTPLHLVEN
TGFFTDDVDFLVLSGQCDLAIHSAKDLPEPPKLTVVAITAGLDPRDLLVYAEKYLSQPLPRRPRIGSSSL
RREELLKLLFPSGIILDIRGTIEERLKLLEEKKYDAIVVAKAAVLRLGLRLPYTKELPPPYHPLQGRLAI
TASKHIRSWKGLFLPLGITED
>gnl|CDD|179217 PRK01076, PRK01076, L-rhamnose isomerase; Provisional
MTTQIEQAYELAKQRYAAVGVDVEAALRQLDRIPVSMHCWQGDDVTGFENPEGSLTGGIQATGNYPGKAR
NADELRADLEKALSLIPGKHRLNLHAIYLESDTPVDRDEIEPEHFKNWVEWAKENGLGLDFNPTCFSHPL
SADGFTLSHPDPEIRQFWIEHCKASRRISAYFGEELGTPCVMNIWIPDGMKDIPVDRLAPRQRLLESLDE
IISEKLDPAHHIDAVESKLFGIGAESYTVGSHEFYMGYATSRQTALCLDAGHFHPTEVISDKISAAMLYV
PRLLLHVSRPVRWDSDHVVLLDDETQAIASEIVRHDLLDRVHIGLDFFDASINRIAAWVIGTRNMKKALL
RALLEPTDQLRKLELEGDYTARLALLEEQKSLPWGAVWDMYCQRHDVPVGSDWLDEVREYEKEVLSKRG
>gnl|CDD|234896 PRK01077, PRK01077, cobyrinate a,c-diamide synthase
MRMPALVIAAPASGSGKTTVTLGLMRALRRRGLRVQPFKVGPDYIDPAYHTAATGRPSRNLDSWMMGEEL
VRALFARAAQGADIAVIEGVMGLFDGAGSDPDEGSTADIAKLLGAPVVLVVDASGMAQSAAALVLGFATF
DPDVRIAGVILNRVGSERHYQLLREALERCGIPVLGALPRDAALALPERHLGLVQASEHGDLEARLDALA
DLVEEHVDLDALLALARAAPPPPPAAAPPPPAPPGVRIAVARDAAFNFYYPENLELLRAAGAELVFFSPL
ADEALPDCDGLYLGGGYPELFAAELAANTSMRASIRAAAAAGKPIYAECGGLMYLGESLEDADGERHPMV
GLLPGEASMTKRLQALGYREAEALEDTLLGKAGERLRGHEFHYSTLETPEEAPLYRVRDADGRPLGEEGY
RRGNVLASYLHLHFASNPDAAARFLAACRRF
>gnl|CDD|234897 PRK01096, PRK01096, deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
MDWDTLLSRERLGKKGKTSKDELGRSPFHKDYDRIIFSGSFRRLQRKTQVHPLAKNDHIHTRLTHSLEVS
CVGRSLGMRVGETLKEEKLPDWISPADIGAIVQSACLAHDIGNPPFGHFGEDAIREWFQDAAGRGFLDDL
SPQERADFLNFEGNAQGFRVLTKLEYHQDDGGMRLTYATLGTYIKYPWSSRHANKQQIKKKKFGCYQSEL
PLFEQIAEALGLPQLGEQRWCRHPLTYLLEAADDICYALIDLEDGLEMGLLNYQEVEALFLELIGDKEKY
RQLGPQDSRRQKLARLRGKAIGRLVNAVAEAFVENYDAILAGTLPGDLIEHCDPDAKRCVQQAKDLAREK
IFQHKRKVELEIGAYTILEILLDAFVPAALYYDSGTTPSFKDKRLLDLLGDNAPDPTMKLYLRLLRVLDF
ISGMTDSYAKELAQELTGRS
>gnl|CDD|179220 PRK01099, rpoK, DNA-directed RNA polymerase subunit K; Provisional
SMGPMKLTRFERARIIGARALQISMGAPVLIDIPESTDPLDIAEEEFKRGVLPITVKRPLPN
>gnl|CDD|234898 PRK01100, PRK01100, accessory gene regulator ArgB-like protein
MSNFTAKVPLSERMADVLISKLNDRWKDDEEGYLKVKYGLEIILINVSKFAIVYLIALVTGLLLQTVTVH
LSFLWLRRYSFGLHATNSINCTLISLTMFVLGAFIFQNIPSNNWMVLGTFGFILLNLFLYAPADTESLPL
IGEKLRKTLKRKAMIGGLILMGITLLIPFAEMKTLIMVGSLFQVISINPITYKLLNRRYKNYEKYERNID
>gnl|CDD|234899 PRK01103, PRK01103, bifunctional DNA-formamidopyrimidine glycosylase/DNA-(apurinic or apyrimidinic site) lyase
MPELPEVETVRRGLEPHLVGKTITRVEVRRPKLRWPVPEDFAERLSGQTILAVGRRGKYLLLDLDDGGTL
ISHLGMSGSLRLLPEDTPPEKHDHVDFVLDDGTVLRYNDPRRFGAMLLTPKGDLEAHPLLAHLGPEPLSD
AFDGEYLAAKLRKKKTAIKPALLDQTVVVGVGNIYADEALFRAGIHPERPAGSLSRAEAERLVDAIKAVL
AEAIEQGGTTLRDYVNADGKPGYFQQSLQVYGREGEPCRRCGTPIEKIKQGGRSTFFCPRCQKR
>gnl|CDD|234900 PRK01109, PRK01109, ATP-dependent DNA ligase; Provisional
MEFSELAEYFERLEKTTSRTQLTKLLADLLKKTPPEIIDKVVYLIQGKLWPDWLGLELGVGEKLLIKAIS
MATGISEKEVENLYKKTGDLGEVARRLKSKKKQKSLLAFFSKEPLTVKEVYDTLVKIALATGEGSQDLKI
KLLAGLLKDASPLEAKYIARFVEGRLRLGVGDATILDALAIAFGGAVARELVERAYNLRADLGYIAKILA
EGGIEALKKVKPQVGIPIRPMLAERLSSPKEILKKMGGEALVEYKYDGERAQIHKKGDKVKIFSRRLENI
THQYPDVVEYAKEAIKAEEAIVEGEIVAVDPETGEMRPFQELMHRKRKYDIEEAIKEYPVNVFLFDLLYV
DGEDLTDKPLPERRKKLEEIVKENDKVKLAERIITDDVEELEKFFHRAIEEGCEGLMAKSLGKDSIYQAG
ARGWLWIKYKRDYQSEMADTVDLVVVGAFYGRGRRGGKYGSLLMAAYDPKTDTFETVCKVGSGFTDEDLD
ELPKMLKPYKIDHKHPRVVSKMEPDVWVEPKLVAEIIGAEITLSPLHTCCLGVVEKGAGLAIRFPRFIRW
RDDKSPEDATTTEEILEMYKRQKKKKEEEP
>gnl|CDD|234902 PRK01112, PRK01112, 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
MALLILLRHGQSVWNAKNLFTGWVDIPLSQQGIAEAIAAGEKIKDLPIDCIFTSTLVRSLMTALLAMTNH
SSGKIPYIVHEEDDKKWMSRIYSDEEPEQMIPLFQSSALNERMYGELQGKNKAETAEKFGEEQVKLWRRS
YKTAPPQGESLEDTGQRTLPYFQNRILPHLQQGKNVFVSAHGNSLRSLIMDLEKLSEEEVLSLELPTGKP
IVYEWTGQKFEKHKEVLG
>gnl|CDD|234903 PRK01115, PRK01115, DNA polymerase sliding clamp; Validated
MMKAVYPDAKDFKYIIDAISKLVDEAKFKFTEDGIRLRALDPAKVAMVDLELPKEAFEEYEVDEEEKIGV
DLEDLKKILKRAKKGDKLELELDEEENKLKITFGGEKTREFSLPLLDVSSEEPPEPNLELPVKAVILGDD
LKDAIKDAELVSDHIELEADEDKFYIEAEGEGEDEVELSLDSGPLIELSVEEPAKSSYSLDYLKDMVKAT
SASDEVTIEFGSDMPLKLEFEIAGGGKVTYLLAPRIE
>gnl|CDD|234904 PRK01117, PRK01117, adenylosuccinate synthetase; Provisional
MKNVVVVGTQWGDEGKGKIVDLLSERADVVVRFQGGHNAGHTLVIDGKKYKLHLIPSGILRPGKTCVIGN
GVVLDPEALLKEIDELEARGVDVRERLRISERAHLILPYHRALDKAREKARGKKKIGTTGRGIGPAYEDK
VARRGIRVGDLLDPETFAEKLEENLEYKNFLLTKYYGAEAVDFEEILDEYLEYAERLKPYVTDTSLLLND
ALKAGKRVLFEGAQGTLLDIDHGTYPFVTSSNTTAGGAATGSGVGPTKIDYVLGIAKAYTTRVGSGPFPT
ELFDEVGEHLRERGHEFGTTTGRPRRCGWFDAVALRYAVRVNGLTGLALTKLDVLDGLEEIKICVAYELD
GKRIDYFPASLEDLARCEPIYEELPGWSESTTGVRSFDDLPENARKYIKRIEELTGVPISIISTGPDRDQ
TIILRDPFAA
>gnl|CDD|179228 PRK01119, PRK01119, putative heavy metal-binding protein
MIVTTSPNIEGKQIIEYKKIVFGEVITGVNFMKDIGAGLRNFFGGRSQGYEDELINAREEAIREMEQRAK
DIGANAVIGVDIDYEVLGADNGMLMVTASGTAVVIE
>gnl|CDD|234907 PRK01130, PRK01130, putative N-acetylmannosamine-6-phosphate 2-epimerase
EQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDS
EVYITPTLKEVDALAAAGADIIALDATLRPRPDGETLAELVKRIKEYPGQLLMADCSTLEEGLAAQKLGF
DFIGTTLSGYTEETKKPEEPDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEE
ITKWFVDALKK
>gnl|CDD|234908 PRK01143, rpl11p, 50S ribosomal protein L11P; Validated
MKKVVEVLVEGGKATPGPPLGPALGPLGLNVKQVVQEINEKTKDFKGMQVPVKVIVDTDTKKFEIEVGIP
PTTALIKKELGIEKGSGEPGHEVVGNLSFEQVVKIAIMKKDDLLSYDLKAAVKEVLGTCVSMGVTVEGKD
PKEVQKEVDEGKYDDLLAKYEKE
>gnl|CDD|234909 PRK01146, PRK01146, DNA-directed RNA polymerase subunit L; Provisional
MEIKVLEKEDNELELEIEGEDHTLMNLLKEELLEDPGVEAASYDIDHPLISNPVLKIKTDGGIDPLEALK
EAAKRIIDLCDEFLD
>gnl|CDD|179234 PRK01151, rps17E, 30S ribosomal protein S17e; Validated
GNIRPKYIKRTAEELLEKYPDLFTTDFETNKKLVEELTNIESKKVRNRIAGYITRKVK
>gnl|CDD|179235 PRK01153, PRK01153, nicotinamide-nucleotide adenylyltransferase; Provisional
MRALFIGRFQPFHKGHLEVIKWILEEVDELIIGIGSAQESHTLKNPFTAGERILMIRKALEEEGIDLSRY
YIIPIPDIEFNSIWVSHVESYTPPFDVVYTGNPLVARLFREAGYEVRQPPMFNREEYSGTEIRRRMIEGD
PWEELVPKSVAEVIKEIDGVERIRELATTDAEEH
>gnl|CDD|100796 PRK01156, PRK01156, chromosome segregation protein; Provisional
MIIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDKRTEKIEDMIKKGKNNLEVE
LEFRIGGHVYQIRRSIERRGKGSRREAYIKKDGSIIAEGFDDTTKYIEKNILGISKDVFLNSIFVGQGEM
DSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDE
KSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEE
RHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDD
LNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD
ISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEI
EVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKL
EDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANN
LNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARL
ESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRKYL
FEFNLDFDDIDVDQDFNITVSRGGMVEGIDSLSGGEKTAVAFALRVAVAQFLNNDKSLLIMDEPTAFLDE
DRRTNLKDIIEYSLKDSSDIPQVIMISHHRELLSVADVAYEVKKSSGSSKVIPLR
>gnl|CDD|234910 PRK01158, PRK01158, phosphoglycolate phosphatase; Provisional
MKIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKLIGTSGPVIAENGGV
ISVGFDGKRIFLGDIEECEKAYSELKKRFPEASTSLTKLDPDYRKTEVALRRTVPVEEVRELLEELGLDL
EIVDSGFAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAAD
YVTEKSYGEGVAEAIEHLLL
>gnl|CDD|234911 PRK01160, PRK01160, hypothetical protein; Provisional
MDFYFKLTPELRQELKKPLGELVRGDIPEPYLKIKEELEKHPLITVGDVVTENLLRVGLKPFLAIYDLKT
KRREYKPSIFEHEEVSITVRNPPGTITLALLRAIKKAFSLIERGKKVRIEVNGEEDLAVIPAVLYAPLGT
VVAYGQPDEGMVLIKVTPECKRRCAEILRKMEVVRDGD
>gnl|CDD|234912 PRK01170, PRK01170, bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase
MITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNKVYPIPYEDRKRKLENFIKKFTNKFRI
RPIDDRYGNTLYEEDYEIIVVSPETYQRALKINEIRIKNGLPPLKIVRVPYVLAEDLFPISSTRIINGEI
DGNGKRLKPLKINISTTNPAKINAVRRFFESLMKNFIVVKNIDYKLETQQPFGEETMKGATNRAMKALKD
NDYSVGIESGLFYNEFSKKYFDVHFCAVIDRYGNVTRGYSSGFEIPDKIIDMIKRGMEVSDAYEKYSGIK
DIDKKMGIIGKISKGKIRREDLIAESIRMAFIPRIDPDFYDL
>gnl|CDD|100801 PRK01172, PRK01172, ATP-dependent DNA helicase
MKISDLGYDDEFLNLFTGNDFELYDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKSIY
IVPLRSLAMEKYEELSRLRSLGMRVKISIGDYDDPPDFIKRYDVVILTSEKADSLIHHDPYIINDVGLIV
ADEIHIIGDEDRGPTLETVLSSARYVNPDARILALSATVSNANELAQWLNASLIKSNFRPVPLKLGILYR
KRLILDGYERSQVDINSLIKETVNDGGQVLVFVSSRKNAEDYAEMLIQHFPEFNDFKVSSENNNVYDDSL
NEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRYLSN
MEIKQMIGRAGRPGYDQYGIGYIYAASPASYDAAKKYLSGEPEPVISYMGSQRKVRFNTLAAISMGLASS
MEDLILFYNETLMAIQNGVDEIDYYIESSLKFLKENGFIKGDVTLRATRLGKLTSDLYIDPESALILKSA
FDHDYDEDLALYYISLCREIIPANTRDDYYAMEFLEDIGVIDGDISAAKTAMVLRGWISEASMQKITDTY
GIAPGDVQARASSADWISYSLARLSSIYKPEMRRKLEILNIRIKEGIREDLIDLVLIPKVGRVRARRLYD
AGFKTVDDIARSSPERIKKIYGFSDTLANAIVNRAMKISSMYYR
>gnl|CDD|234913 PRK01175, PRK01175, phosphoribosylformylglycinamidine synthase I; Provisional
MESIRVAVLRMEGTNCEDETVKAFRRLGVEPEYVHINDLAAERKSVSDYDCLVIPGGFSAGDYIRAGAIF
AARLKAVLRKDIEEFIDEGYPIIGICNGFQVLVELGLLPGFDEIAEKPEMALTVNESNRFECRPTYLKKE
NRKCIFTKLLKKDVFQVPVAHAEGRVVFSEEEILERLIENDQIVFRYVDENGNYAGYPWNPNGSIYNIAG
ITNEKGNVIGLMPHPERAFYGYQHPYWEKEEDYGDGKIFFDSLINYLRKVH
>gnl|CDD|167170 PRK01177, PRK01177, hypothetical protein; Provisional
MMKITLVGEKLAKPGLEFIFYGPAEPCKTCRLANVCFGNLEPGRRYKILKVREIEHPCPLHEGKVRVVEV
VEPAIEVNIEPRRAIEGSKITLKFVTCPDIEKCNLVRPEGLFEGDKVKIKEILGDVECPGKGYKMVKVMR
>gnl|CDD|179239 PRK01178, rps24e, 30S ribosomal protein S24e; Reviewed
MEIKIISDKENPLLGRREIKFEVYHEGSATPSRKDVRKKLAAMLNADKELVVVRKIKTEYGMGKSKGYAK
VYDDKERARKIEPKYILERNKIEEEEEEE
>gnl|CDD|234914 PRK01184, PRK01184, flagellar hook-basal body complex protein FliE
MKIIGVVGMPGSGKGEFSKIAREMGIPVVVMGDVIREEVKKRGLEPTDENIGKVAIDLRKELGMDAVAKR
TVPKIREKGDEVVVIDGVRGDAEVEYFRKEFPEDFILIAIHAPPEVRFERLKKRGRSDDPKSWEELEERD
ERELSWGIGEVIALADYMIVNDSTLEEFRARVRKLLERILRSRN
>gnl|CDD|179241 PRK01185, ppnK, NAD(+) kinase
MKVAFVIRKDCKRCIKIAKSIIELLPPDWEIIYEMEAAKALGMDGLDIEEINADVIITIGGDGTILRTLQ
RAKGPILGINMGGLGFLTEIEIDEVGSAIKKLIRGEYFIDERMKLKVYINGERLEDCTNEAVIHTDRIAK
IRQFKIYYDGHFLDTFKADGVIVATPTGSTSYSSSAGGPILLPNLEGMVISYIAPYSSRPKSVVVPSEST
VEIKIAGDQSSLLILDGQYEYKISKGDTVEISKSENYARFISFRESPYDRIREKLIKHVVN
>gnl|CDD|100807 PRK01189, PRK01189, V-type ATP synthase subunit F; Provisional
MMSCITVIGERDVVLGFRLLGIGDTIEAEGKDLVKKFLEIFNNPKCKYIFVSESTKNMFDKNTLRSLESS
SKPLVVFIPLPGISEEESIEEMAKRILGIDIGDV
>gnl|CDD|234916 PRK01192, PRK01192, 50S ribosomal protein L31e; Reviewed
SAKEVEERIYTIPLRDVKKVPRTKRADRAVKLVREFLARHFKADEDKVKIDPSINEKIWERGREKPPSKV
RVRVAKKGEDGVVEAELAE
>gnl|CDD|100810 PRK01194, PRK01194, V-type ATP synthase subunit E; Provisional
MSLEDVIKDIEKSREEKKKEINDEYSKRIEKLEKECDSKIQSIKEYYEKKMRAEISRLKKSIIDKANIEA
RSIKREKRREILKDYLDIAYEHLMNITKSKEYDSILNKMIEVAIKTLGEDCIIKVSESDKKKINNAKIKF
ADIDPYGGILAYSRDGKRELDLRLSSIFENILEDLKVYFYENIEE
>gnl|CDD|234917 PRK01198, PRK01198, V-type ATP synthase subunit C; Provisional
TIRPMMDSAPYAYVNARVRVREAKLLDREKYERLLEMKSLEEIIRFLEETEYKEEIDELGSRYSGPDLIE
KALNRNLAKTYELLLEISPGRLKELVDVYLRKWDIHNIKTLLRGKILGLDAEEIEELLIPAGELDLEKLK
ELLEAKSVEEIVKILEGTEYYEVLEEALEDYEETGDLQPIENALDKYYYENLLEIASPKDIDEKLLLEYV
RTEIDITNIKTLLRLKAQGLSADFIEKVLIPGGSLDEEKLKELLAEDIEELVSALEGTKYGDVLSEALEE
YEETGSLSVFEKALDNYLLEYMKKLSKRYPFSVEPILGYILAKEREVKNLRIIARGKENGLSPEEIRERL
VI
>gnl|CDD|234918 PRK01202, PRK01202, glycine cleavage system protein GcvH
MMNIPADLKYTKSHEWVRVEGDTATVGITDHAQEQLGDIVFVELPEVGDEVKAGETFGVVESVKAASDIY
APVSGEVVEVNEALEDSPELVNEDPYGEGWLFKIKPSDESELDDLLDAEAYEALIEE
>gnl|CDD|100814 PRK01207, PRK01207, methionine synthase; Provisional
MAALITQEIGSFRKPEYLSREFHKIEGTDKFYELAERATLETLDVFENAGLDNIGIGGEMFRWEMYEHPA
ERIKGIIFYGMVRSFDNRYYRKGSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFNDFY
RDRYDLAMEFARIINEELKDIKSAWDRKSPGRKLEIQIDEPATTTHPDEMDIVVDSINKSVYGIDNEFSI
HVCYSSDYRLLYDRIPELNIDGYNLEYSNRDTLEPGTSDEKRPGFQDLKYFAEHNESLQRKKFIGLGVTD
VHIDYVEPVKLIEDRIRYALKIIKDPELVRLNPDCGLRTRSREIGEQKLRNMVAAKNNILKEL
>gnl|CDD|234919 PRK01209, cobD, cobalamin biosynthesis protein
MMMTLLLLLLALLLDRLLGDPRRWPHPVVGFGRLISRLERRLRRGCRGLRIAGVLAWLVVVGPSGLLAWL
LLALAARLWLGVALEVLLLYTALAGRSLADHARAVARALRAGDLEEARRAVSMIVGRDTSQLDEEGIARA
AIESVAENTSDGVIAPLFYAALGGLPGALLYRAVNTLDSMVGYKNERYRRFGWAAARLDDVLNYIPARLT
ALLLALAAPLLGGDPRGALRIWRRDARKHPSPNAGWPEAAMAGALGVQLGGPNVYHGEVVERPTLGDGGR
PLTAEDIERALKLVRRAVLLWLALFAALLLLL
>gnl|CDD|179247 PRK01211, PRK01211, dihydroorotase; Provisional
MAICGNFYYKGKFDYLEIEVEDGKIKSIKKDAGNIGKKELKGAILPAATDIHVHFRTPGETEKEDFSTGT
LSAIFGGTTFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNALILDERSIGLKVYMGGT
TNTNGTDIEGGEIKKINEANIPVFFHAELSECLRKHQFESKNLRDHDLARPIECEIKAVKYVKNLDLKTK
IIAHVSSIDVIGRFLREVTPHHLLLNDDMPLGSYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHT
EEDKQEFEYAKSGIIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGIKKGKIEEGYDADFMAFDF
TNIKKINDKRLHSKCPVSPFNGFDAIFPSHVIMRGEVVIDNYELISERTGKFVPKGGES
>gnl|CDD|234920 PRK01212, PRK01212, homoserine kinase; Provisional
MMMVKVRVPATSANLGPGFDSLGLALSLYDEVLVGDVVSVEAEFSIEVIGEGADKLPLDPEKNLVYQAAL
KFLEKLGKPPGLRIELEKNIPLGRGLGSSAASIVAGLVAANELAGLPLSKEELLQLATEGEGHPDNVAPA
LLGGLVLALEENGVISVKIPVFDDLKWVVAIPNIELSTAEARAVLPKQYSLKDAVFNSSRAALLVAALYT
GDYELAGRAMKDVLHEPYRAKLIPGFAEVRQAALEAGALGAGISGAGPTVFALCDKEDAEKVADALQKAF
LQGIEGFVHVLRLDTAGARVL
>gnl|CDD|234921 PRK01213, PRK01213, phosphoribosylformylglycinamidine synthase subunit PurL
TPDTEELYAEMGLTDDEYERIREILGREPNFTELGMFSVMWSEHCSYKSSKPLLRKFPTKGPRVLQGPGE
NAGVVDIGDGQAVVFKIESHNHPSAVEPYQGAATGVGGILRDIFSMGARPIALLDSLRFGELDHPKTRYL
LEGVVAGIGGYGNCIGVPTVGGEVYFDESYNGNPLVNAMCVGLVRHDDIVLAKASGVGNPVVYVGAKTGR
DGIGGASFASAELSEESEEKRPAVQVGDPFMEKLLIEACLELIKTGLVVGIQDMGAAGLTCSSSEMAAKG
GLGIELDLDKVPLREEGMTPYEIMLSESQERMLLVVKPGKEEEVLAIFEKWDLDAAVIGEVTDDGRLRVY
HHGEVVADVPAEALADEAPVYDRPYKEPAYLDELQADPEDLKEALLKLLSSPNIASKEWVYEQYDHEVQT
NTVVKPGGDAAVLRIRGGGKGLALTTDCNPRYVYLDPYEGAKLAVAEAARNLAAVGATPLAITDCLNFGN
PEKPEVMWQFVEAVRGLADACRALGTPVVGGNVSLYNETGGTAIYPTPVIGMVGLIDDVSKRTTSGFKKE
GDLIYLLGETKDELGGSEYLKVIHGHVGGRPPKVDLEAEKRLQELVREAIREGLVTSAHDVSEGGLAVAL
AEMAIAGGLGAEVDLSDGLRPDALLFSESQGRYVVSVPPENEEAFEALAEAAGVPATRIGVVGGDALKVK
GNDTESLEELREAWEGALPRLLGG
>gnl|CDD|179250 PRK01215, PRK01215, nicotinamide mononucleotide deamidase-related protein
MDKWFAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTG
GLGPTYDDKTNEGFAKALGVELELNEDALRMILEKYEKRGIPLTPERKKMAMMPPGAVPLENPVGTAPGI
LIEHGGKDIVALPGVPREMEAIFENFVEPLLKNRPPLKYYEDSILVEGVMESDLAPYVKELVKKYDRVYV
KSHPKGYEVSKPILEIQIAGSGEREEEAKVKVEKVLEELKELIKKLGGIIRESL
>gnl|CDD|179251 PRK01216, PRK01216, DNA polymerase IV; Validated
MIILFVDFDYFFAQVEEVLNPSLKGKPVVVCVYSGRFEDSGAVATANYEARKLGIKAGMPIVEAKKILPN
AVYLPMRKEVYQQVSNRIMKLLREYSEKIEIASIDEAYLDISDKVKNYQDAYNLGLEIKNKILEKEKITV
TVGISKNKVFAKIAADMAKPNGIKVIDDEEVKRFINELDIADIPGIGDITAEKLKKLGVNKLVDTLRIEF
DELKGIIGEAKAKYLFSLARNEYNEPVRARVRKSIGRYVTLPRNTRDLEEIKPYLKRAIEEAYYKLDGIP
KAIHVVAIMEDLDIVSRGRTFTHGISKETAYREAVRLLQKILEEDERKIRRIGVRFSKIIEAIGLDKFFD
T
>gnl|CDD|179252 PRK01217, PRK01217, hypothetical protein; Provisional
MSEEEGDVIVVTSEYIPGYRIVEVLGVVWGITVRSRGLGGNIVAGLRSLAGGEIKEYVEMAEQARNQALE
RMIDHAKELGANAVINVRFDSNEISQVMDEIIAYGTAVVVEPEE
>gnl|CDD|179253 PRK01220, PRK01220, malonate decarboxylase subunit delta; Provisional
METLTFEFPAGQPPRGRALVGVVGSGDLEVLLEPGDAGKLSIQVVTSVNGSAARWKALFERFFTAQTPPA
ANIDIHDFGATPGVVRLRLEQALEEIGHD
>gnl|CDD|234922 PRK01221, PRK01221, deoxyhypusine synthase
MNREDLLKEPVEDIRLDDLTSISDLIEVYRKIGGFMAGHIVRASEILKEMISDADLRFLSFTANLVSTGL
RGLIADLIKRGLFNVVITTCGTLDHDIARSFGGVYYKGSFDIDDAMLKDLGIHRLGNVLIPVESYGPLIE
KFVRKFLEELYKDKKEWSTYELLWEFGKRINDENSILRAAYEKGVPVFVPGIVDGAFGTQLFTFSQRFGG
FKINLLEDEELLSDLVFSSKKLGALIIGGGISKHHTIWWNQFKDGLDYAVYITTAVEYDGSLSGARPREA
ISWGKIKPEAKHVTIYGDATIILPILAASLLS
>gnl|CDD|234923 PRK01222, PRK01222, phosphoribosylanthranilate isomerase
MRMRVKICGITTPEDAEAAAELGADAIGFVFYPKSPRYVSPEQAAELAAALPPFVKVVGVFVNASDEEID
EIVETVPLDLLQLHGDETPEFCRQLKRRYGLPVIKALRVRSAGDLEAAAAYYGDADGLLLDAYVGLPGGT
GKTFDWSLLPAGLAKPWILAGGLNPDNVAEAIRQVRPYGVDVSSGVESAPGIKDPEKIRAFIEAVKSADS
>gnl|CDD|234924 PRK01229, PRK01229, N-glycosylase/DNA lyase; Provisional
KEMLEEIEEIKNEVKDRVEERIEEFKLLGEKGDEEDLFSELSFCILTANSSAEGGIKAQKEIGDGFLYLS
EEELEEKLKEVGHRFYNKRAEYIVEARKLYGKLKEIIKADKDQFEAREFLVKNIKGIGYKEASHFLRNVG
YEDLAILDRHILRFLKRYGLIEEIPKTLSKKRYLEIEEILREIAEELGISLGELDLYIWYKETGKVLK
>gnl|CDD|179257 PRK01231, ppnK, NAD(+) kinase
MPSFRNIGLIGRLGSSSVVETLRRLKDFLLDRGLEVILDEETAEVLPGHGLQTVSRKLLGEVCDLVIVVG
GDGSLLGAARALARHNVPVLGINRGRLGFLTDIRPDELEFKLAEVLDGHYQEEERFLLEAEVRRGGEVIG
QGDALNDVVLHPGKSTRMIEFELYIDGQFVCSQRSDGLIVSTPTGSTAYALSGGGPIMHPKLDAIVLVPM
FPHTLSSRPIVVDGNSEIKIVISKDNRTYPRVSCDGQNSVTLAPGDTVTIRKKPQKLRLIHPLDYNYYET
CRTKLGWGSRLGGGD
>gnl|CDD|234927 PRK01237, PRK01237, triphosphoribosyl-dephospho-CoA synthase; Validated
MMAAQLQAQTKSLAERLADLAVDALIDEVTLSPKPGLVDRRGSGAHPDLDLFLMIRSALSLWPYFKAMAE
AAAQHGEVLLALREQLGQLGREGEKAMFAATGGVNTHRGAIWSLGLLVAAAALAPQRLDAAEVAARAAQI
ALLTDRFAPKQTLSHGERVFLRYGVGGAREEAQQGFPHVVDVGLPQLQRSRGAGAGENQARLDALLAIMA
ALDDTCVLKRAGNVGLEAMQQGAQAVLDLGGSATLAGRRALRELNQDLLALNASPGGAADLLAATLFLDR
LEQLLAGAS
>gnl|CDD|179261 PRK01242, rpl39e, 50S ribosomal protein L39e; Validated
MRNKPLGKKLRLAKALKQNRRVPAWVIVKTNRRVRRHPKRRHWRRSKLKV
>gnl|CDD|179262 PRK01250, PRK01250, inorganic diphosphatase
MSLNKIPAGKDLPEDINVIIEIPANSDPIKYEVDKESGALFVDRFLYTAMFYPCNYGFIPHTLSLDGDPV
DVLVVTPYPLVPGSVIRCRPVGVLKMEDESGEDAKIIAVPHDKLSPEYDHIKDVNDLPELLKAQIKHFFE
HYKDLEKGKWVKVEGWGGAEEAKAEIVEAIERAKKK
>gnl|CDD|179263 PRK01253, PRK01253, preprotein translocase subunit Sec61beta
MKKKKEGGGLMSSAGLIRYFEEETEAIKIDPKTVIAIGLALGIFVLVLNALFPP
>gnl|CDD|234929 PRK01259, PRK01259, ribose-phosphate diphosphokinase
MKLFAGNANPELAEKIAKYLGIPLGKASVGRFSDGEISVEINENVRGKDVFIIQSTCAPTNDNLMELLIM
IDALKRASAGRITAVIPYFGYARQDRKARSRVPITAKLVANLLETAGADRVLTMDLHADQIQGFFDIPVD
NLYGSPILLEDIKQKNLENLVVVSPDVGGVVRARALAKRLDADLAIIDKRRPRANVSEVMNIIGDVEGRD
CILVDDMIDTAGTLCKAAEALKERGAKSVYAYATHPVLSGGAIERIENSVIDELVVTDSIPLSEEAKKCD
KIRVLSVAPLLAEAIRRISNEESVSSLFD
>gnl|CDD|234930 PRK01261, aroD, 3-dehydroquinate dehydratase; Provisional
MPLYSGDKISIGKFVIGNMQPIVVESIFFKDIKEMKERFKTKVLSDKNLYEIRFDLFHDHSIESEPEIIS
ALNEMDIDYIFTYRGVDARKYYETAIDKMPPAVDLDINLIGKLEFRPRNTMLMVSYHTNNSDNMPAILDI
MNEKNPDYVKVACNYNDNKKFVDDLQYILMKKDEKYKPIVFIPMGREFLRIFSGYYVSDIVYARYDNETA
PGQPKRDYYESAFIKYGYR
>gnl|CDD|234931 PRK01265, PRK01265, heat shock protein HtpX; Provisional
MNWEVIKLRLNMALAGLGIVLLGFALAYAVAYYAFGAQFGVGLILGILIFVFFLNIIQWLFGPYMINAAY
RTVEVTPTDPVYGWLYSIVAEVAKYNGIRVPKVYIADVPFPNAFAYGSPIAGKRIAITLPLLKILNRDEI
KAVAGHELGHLKHRDVELLMAIGLIPTLIYYLGYSLFWGGMFGGGGGGRGNNGGLLFLIGIALMAVSFVF
NLLVLSINRMREAYADVNSALTVPGGAENLQTALAKITLSMDPGALERFKKKSTTNQMASMLFFSNAIEE
VPTWDARELVEYWKTTKVPWYADIFSDHPHPAKRIQLLEKLSKS
>gnl|CDD|179269 PRK01271, PRK01271, tautomerase PptA
MPHIDIKCFPRELDEEQKAALAADITDVIIRHLNSKDSSISIALQQIQPESWQAEVWDAEIAPQMDALIK
KPGYSM
>gnl|CDD|179270 PRK01278, argD, acetylornithine transaminase protein; Provisional
MSISPLLPVYNRADLAFERGEGVWLIDEDGERYLDFASGIAVNSLGHAHPHLVEALKEQAEKLWHVSNLY
RIPEQERLAERLVENSFADKVFFTNSGAEAVECAIKTARRYHYGKGHPERYRIITFEGAFHGRTLATIAA
GGQEKYLEGFGPLVPGFDQVPFGDIEALKAAITPNTAAILIEPIQGEGGIRPAPDEFLKGLRQLCDENGL
LLIFDEVQCGMGRTGKLFAHEWAGVTPDIMAVAKGIGGGFPLGACLATEEAAKGMTPGTHGSTYGGNPLA
MAVGNAVLDVILAPGFLDNVQRMGLYLKQKLEGLVDRFPDVIEEVRGKGLLLGLKCVVPNRDLVQALRDE
GLLTVGAGDNVVRLLPPLIITEEEIDEALERLERAAESL
>gnl|CDD|234933 PRK01285, PRK01285, pyruvoyl-dependent arginine decarboxylase; Reviewed
FVPKKIFFTAGVGEGKTKLNAFDLALLDAGIGNVNLVRVSSILPPNCEIIPLEEKLLPPGSLVPTVYARN
SSNEPGRLIAAAVGVAIPKDKELYGYISEHHGFGEKEEAEDLAATMLEEGFKMRGKILDEIKITASEHGV
EGIWTTVAAAAVWYP
>gnl|CDD|234934 PRK01286, PRK01286, deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
ATLAPYAALSANSRGRLRPEEPCPIRTEFQRDRDRIIHSKAFRRLKHKTQVFINPEGDHYRTRLTHTLEV
AQIARTIARALRLNEDLTEAIALGHDLGHTPFGHAGEDALNELMKEYGGFEHNEQSLRVVDKLEKRYDGL
NLTWEVREGILKHSGPRNAPLGTAATLEGQIVRLADEIAYNNHDIDDGIRAGLITLEDLPEDVRRLLGET
HRRRINTLVVDLIKNTQRNLAEGAAAPPLVSFSEEVAEAMKELRRFLFENVYRHPKVKREREKAKRIVQD
LFEYYMEDPELLPPEYQNIAEEEGLERAVADYIAGMTDRYALREYRRLFVPKPWLY
>gnl|CDD|234935 PRK01287, xerC, site-specific tyrosine recombinase XerC; Reviewed
MANRKPRKGSLLTVAHDPKTLRQLLERFLAWLQERNWSERTLKVYTEHLYPFILWCEERGLYYAADVTLP
VLERYQRYLYGYRKANGEPLSTRTQRTQLSPLRVWFRWLLKRHHILYNPAEDLELPKEEKRLPRQILSEA
ETEQVLASPDLTTLQGLRDRALLELLWSTGIRRGELARLDLYDVDASRGVVTVRQGKGNKDRVVPVGERA
LAWLQRYLQDVRPQLAVRPDSGALFVAMDGDGLARNTLTNMVGRYIRAAGIEKAGACHLFRHAMATQMLE
NGADTRHIQAILGHAKLETTQIYTRVSIGHLQAVHASTHPAERKADEKLRDADEVGLLADLYADDNADTP
TPPDSSEP
>gnl|CDD|234936 PRK01293, PRK01293, phosphoribosyl-dephospho-CoA transferase; Provisional
VMMATPRPHDLLWGMTRAALPDDAPAWVREALAAGLPVVVRRAVDAAGRVAVGVRGAGREQRYAAWMPAA
DIVRVVTPEALAEASAALRSPLPALPALQALAALLDALGLAWGVTGSAGFELATGIPVLHADSDLDLLIR
APQPLARDQARELLQLLDQAPCRVDLQLETPAGGFALREWARDGGRVLLKTAHGPRLVADPWSREEV
>gnl|CDD|234937 PRK01294, PRK01294, lipase secretion chaperone
MKKKRALSLGLVGLVAIGAVWLWPGDPANSSAGAASAAAAAAAAALSAAAAPAAADAAVAALPASLAGTS
VPGLPLDAQGHLADTRALRDFFDYFLSALGELDLAAIDALVEREIAAQLPEPADSQALDLWLRYKAYLSA
LAQLEDDGPGKLDLQALQQLLDARLALRARFFSDWEIQAFFGEENQYQRYALERLRIAQDPSLSDAQKAA
RLAALEAQLPEDLRAALQESQRQQALLQQLAQLQASGASPQELRLMRAQLVGPEAAQRLEQLDQQRAAWQ
QRYDDYLAQRAQILNAAGLSPQDRQAQIAQLRQQRFSPQEALRLAALERIHDAGQT
>gnl|CDD|167205 PRK01295, PRK01295, phosphoglyceromutase; Provisional
MSRTLVLVRHGQSEWNLKNLFTGWRDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCQLIL
EELGQPGLETIRDQALNERDYGDLSGLNKDDARAKWGEEQVHIWRRSYDVPPPGGESLKDTGARVLPYYL
QEILPRVLRGERVLVAAHGNSLRALVMVLDGLTPEQILKLELATGVPIVYRLNADSTVASKEVLAA
>gnl|CDD|234938 PRK01297, PRK01297, ATP-dependent RNA helicase RhlB; Provisional
MLKALKKIFGKGEAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRAEKPKKDKPRRERKPKPA
SLWKLEDFVVEPQEGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAA
FLISIINQLLQTPPPKERYMGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLE
ARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRKEERQTLLFSATF
TDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRR
IEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYV
HRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAELLKPVPRKH
>gnl|CDD|234939 PRK01305, PRK01305, arginyl-tRNA-protein transferase; Provisional
MMMLPLSTLQFYLTAPHPCSYLPGRQERKLVADPSHPIAAELYDELLQAGFRRSGNIAYRPHCDGCRACV
SVRIPVAEFVPSRSQRRVLKRNADLVVRVLPPEFTEEHYALYRRYLRARHADGGMDPPSRDQYAQFLEDS
WVNTRFIEFRGDGKLVAVAVTDVLDDGLSAVYTFYDPDEEHRSLGTFAILWQIELAKRLGLPYVYLGYWI
KGSRKMNYKARFRPLEILIDGGWQRLEEPE
>gnl|CDD|167208 PRK01310, PRK01310, hypothetical protein; Validated
MSEPWRYSADGLRLAVRLTPRGGRDAIDGIETLADGRAVLKVRVRAVPEGGEANRALIELLAKALGVPKS
SVRLLSGATSRLKQLRIDGDPEDLGEALRALTAA
>gnl|CDD|234941 PRK01315, PRK01315, putative inner membrane protein translocase component YidC; Provisional
MDGLADFGSAIMTPLYWVISGILVLFHTLLGFLFGPDSGLTWVLSIVGLVIVIRALLIPLFVKQIKSQRN
MQEIQPKMKKIQEKYKGDRERMSQEMMKLYKETGTNPLSSCLPLLLQMPIFFALYRVLDSAASRGDGIGP
INPPLLESFRHAHIFGAPLAATFLQALNAGNTAVQVVAAVLIILMSASQFITQLQLMTKNMPPEAKTGPM
AQQQKMLLYLFPLMFLVSGIAFPVGVLFYWLTSNVWTMGQQFYVIRNNPTPGSPAAIAREERLAKKGKDH
GESEGKVVAPEGAVAQTTEVREQTKRQTVQRQQPKRQSRAKRQKGGAAT
>gnl|CDD|234942 PRK01318, PRK01318, membrane protein insertase; Provisional
MDNKRLLLAIALSFVIFLGWQYWQQDKAQAAAQAPAPQARITVETDVLRLSIDTKGGRIDDLLLKKYKET
LDSSPPVVLLSPSTEHPYFAQSGLTGADGPDNVPNPDRTLYTADGDSLVLADGQNELPVTLTWTNGNGLT
FTKTYTLDRGDYMFTVEYSVNNNSGAPVNLSPYGQLKRTGSSNFASYTFHGGAIGTPDEKYEKYTYKDID
DNLNISSKGGWVAILDKYFATALIPQNGQNNFYSKNLGNGLYQVGFKSPPVTVAPGQSASTTARLYAGPK
EVKLLAKEIAPGLDLAVDYGWLWFITKPLFWLLDFLHSFVGNWGWAIILLTIIVKLLLFPLTYKSYVSMA
KMKVLQPKMQELKEKYKDDPQKMQQEMMELYKKEKVNPLGGCLPILIQIPIFFALYKVLLVSIELRHAPF
IGWIHDLSAPDPYFILHIGLLPILMGITMFLQQKLNPTPTDPMQAKIMKFMPLIFTFFFLSFPAGLVLYW
IVNNLLTIIQQYLINRRLEKKKLLAANKKKK
>gnl|CDD|179280 PRK01322, PRK01322, 6-carboxyhexanoate--CoA ligase; Provisional
MMYSIKMRASKNGKHISGAERIVEFEKIEETVSELLKRALFHENGKPDFINIKIEKIEEPIQYIKALPIK
TIDVKSVEEARALARELLQEEGVSEEAIEKAFELIKEGTNMRGAILLDAISGERLEPDKERGVRVTNIDF
EDRLKEKILLLGLLTERTVDALALASKVIAHPGVIAELCWSDDPDYTTGYVATKKLGYHRITNLKEEGTP
YGGRIFFVDDSIDLEELISYLENKPVLIVYEG
>gnl|CDD|179281 PRK01326, prsA, foldase protein PrsA; Reviewed
MKKKLIAGAVTLLSVATLAACSKTNENTKVISMKGDTITVSDFYNQVKNNPSAQQAMLNLTISRVFEKQY
GDKVSDKEVEKAYAKTAKQYGASFSRALAQAGLTPETYKAQIRTSKLVEYAVKEAAKKELTDEAYKKAYE
EYTPEVTAQIIRLDNEDKAKSVLEEAKAEGADFAQIAKENTTTKEKKGEYKFDSGSTNVPEQVKKAAFAL
DEDGVSDVISVLDPTAYQSKYYIVKVTKKTEKKSDWKDYKKRLKAIILAQKQNDSNFQNKVIAKALDKAN
VKIKDKAFANILAQYANLGDSSSSSSTSST
>gnl|CDD|234943 PRK01343, PRK01343, zinc-binding protein; Provisional
AKVEPLRPTRPCPECGKPSTREAYPFCSERCRDIDLNRWLSGSYVIPGAPDEEDDEE
>gnl|CDD|234944 PRK01345, PRK01345, heat shock protein HtpX; Provisional
MNYFRTAMLLAGMTALFMGVGYLIGGAGGMMIALVIAAGMNLFSYWNSDKMVLRMYGAQEVDERSAPELY
RMVRDLARRAGLPMPKVYIIDNPQPNAFATGRNPENAAVAATTGLLQRLSPEEVAGVMAHELAHVKNRDT
LTMTITATLAGAISMLANFAFFFGGNRENNNGPLGLVGTLAAMIVAPLAAMLVQMAISRTREYAADRRGA
EICGNPLWLASALGKIERGAHGVPNEEAERNPATAHMFIINPLSGEGMDNLFSTHPATENRIAALQRMAG
EMGGRSAAPTAAAAAPRQSRGPWGQGSGGGRRRGPWS
>gnl|CDD|234945 PRK01346, PRK01346, enhanced intracellular survival protein Eis
ATRDMAITIRTATEEDWPAWFRAAATGFGDSPSDEELEAWRALVEPDRTLGAFDGDEVVGTAGAFDLRLT
VPGGAVLPAAGVTAVTVAPTHRRRGLLTALMREQLRRIRERGEPVAALTASEGGIYGRFGYGPATYSQSL
SVDRRRARLRPDVPDGGRVRLVDPAEARDLLPAVYERWRRARPGALSRPPAWWDDVLADRESRRGGGSPL
RALVHPDDGEVDGYALYRVDDTWGFRGPDGTVEVEELVAATPAAYAALWRFLLSLDLVERVRAGIAPPDD
PLPHLLADPRAARTTGVSDGLWLRIVDVPAALEARRYAADGDVVLEVTDPLGWAGGRFRLDVGDGGASCT
PTDAAADLALDVADLGSLYLGGHRASTLAAAGRVRELDPGALARADAAFATDRAPHCGTVF
>gnl|CDD|234946 PRK01355, PRK01355, azoreductase; Reviewed
MSKVLVIKGSMVAKEKSFSSALTDKFVEEYKKVNPNDEIIILDLNETKVGSVTLTSENFKTFFKEEVSDK
YINQLKSVDKVVISCPMTNFNVPATLKNYLDHIAVANKTFSYKYSKKGDAIGLLDHLKVQILTTQGAPLG
WYPWGSHTNYLEGTWEFLGAKVVDSILLAGTKVEPLSNKTPKEIVEEFDKEIIEKAKNF
>gnl|CDD|167217 PRK01356, hscB, co-chaperone HscB; Provisional
MQNYFQLLGLPQEYNIDLKILEKQYFAMQVKYHPDKAKTLQEKEQNLIIASELNNAYSTLKDALKRAEYM
LLLQNINLNDEKTRSLLSPLELSIFWDEMERIENTILFSDLEKIKNKYELMYKNEIDSLKQAFEEQNLSD
ATIKTSKLKYIGTLLNKLQEKIKSCK
>gnl|CDD|179287 PRK01371, PRK01371, Sec-independent protein translocase protein TatB
MFGIGPGELVVLVVLAVLVFGPDKLPKAARDAGRTLRQLREMANNARNDLRSELGPEFADLDLRDLNPKT
FVRKHLLEDLDDDIDEIKLGLKTVRSGLDLGDEDPAVPAAGNGRRPEASSSVPSAPAVAAPFDPEAT
>gnl|CDD|234948 PRK01372, ddl, D-alanine--D-alanine ligase; Reviewed
PKMFGKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAHPIDPGEDIAAQLKELGFDRVFNALHGRGGE
DGTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP
AREGSSVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKGRELTVAVLGGKALPVIEIVPAGEFYDYEAK
YLAGGTQYICPAGLPAEIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNTQPGMTSHSLVPM
AARAAGISFSELVDRILEDALCDR
>gnl|CDD|134546 PRK01379, cyaY, iron donor protein CyaY
MNNSEFSKIAETTIAYIADKIEEQDKEASIDVDLQGDILNLDTDKGIYVINKQSAAKEIWLSSPVSGPYH
FFYEQGKWKNRAGLELMAILTEELNIKFDTRPT
>gnl|CDD|234949 PRK01388, PRK01388, arginine deiminase; Provisional
MMMTPIGVHSEIGKLRTVLLHRPGLELERLTPSNCDELLFDDVPWVERAQKEHDAFAQTLRDRGVEVLYL
EDLLAETLANPEAREWFLDRQISEARVGLGLADELRAYLESLDNRELAEKLIGGVAKSELPESKAKSLVR
LMHDPYDFVLDPLPNLLFTRDPSAWIGGGVTINPMAWPARRRETLLTEAIYKHHPRFAGADVPVWDDRHG
NATLEGGDVLVLGKGVVAIGMSERTSPQAIEQLARSLFKKGAAKRVLAVEIPKSRAFMHLDTVFTMVDYD
KFTVYPEIVGDLNAFSLTPDDDGGGLDIREEKAPFLEVLAEALGLDKLRVIETGGDDIAAEREQWNDGNN
TLAIAPGVVVAYDRNTVTNALLRKAGIEVITIPGSELGRGRGGPRCMSCPIERDPI
>gnl|CDD|234951 PRK01392, citX, 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase; Reviewed
ELASGHAVSLPEMLAARDERQARQHALLKRHPEVSLLSVTMVIPGPIKTSPKLRRIFNHVVTALQTLLAD
QQIQEQAALLSATGPEGYLAIALPARDLKLAMIALEQSHPLGRLWDLDVLTLEGEIPHQLSRTDLGLPPR
RCLLCGQDAKVCARSRTHSLTEMQTAIEALLHDFDSCNNN
>gnl|CDD|179293 PRK01395, PRK01395, V-type ATP synthase subunit F; Provisional
KTMYKIGVVGDKDSILPFKALGIDVFPVIDEQEAINTLRKLAMEDYGIIYITEQIAADIPETIERYDNQV
LPAIILIPSNQGSLGIGLSRIQDNVEKAVGQNIL
>gnl|CDD|179294 PRK01397, PRK01397, 50S ribosomal protein L31; Provisional
MKSGIHPEYKKFLIKVGSDVFETMSTHPTGEILMDVDFRKHPAWNKDSGNVVNQSNKSVSDFNKRFSGLS
FGSKKEAS
>gnl|CDD|234952 PRK01402, hslO, Hsp33-like chaperonin; Reviewed
MAEDAASLGPSDFAGDDAVLPFQVEGLDVRGRAVRLGPALDEILTRHDYPEPVARLLGEAVVLTVLLGSS
LKFEGRFILQTQGDGPVDMLVVDFSTPDRLRAYARFDEERLAAAIAAGETSPEALLGKGHLAMTIDQGPD
MQRYQGIVALDGSTLEEAAHQYFRQSEQIPTRVRLAVAELITGGGAGKPRWRAGGLLIQFLPQAPERARQ
ADLHPGDAPEGTEIAVPEDDAWVEARSLVETIEDDELIDPTVSSERLLYRLFHERGVRVFDPQPVIARCS
CSREKIAGVLKGFSAEERADMVEDGKISVTCEFCSRVYRFDPAEVGVE
>gnl|CDD|167229 PRK01415, PRK01415, hypothetical protein; Validated
MNEKIAILSAYSFVNIEEPANLIPKLLLIGKRKYVRGTILLANEGFNGSFSGSYENVNLVLEELIKLTGP
KDVNVKINYSDVHPFQKLKVRLKKEIVAMNVDDLNVDLFKGEYIEPKDWDEFITKQDVIVIDTRNDYEVE
VGTFKSAINPNTKTFKQFPAWVQQNQELLKGKKIAMVCTGGIRCEKSTSLLKSIGYDEVYHLKGGILQYL
EDTQNKNNLWQGECFVFDDRRAVTDDLSPVERHWLQR
>gnl|CDD|234954 PRK01424, PRK01424, S-adenosylmethionine:tRNA ribosyltransferase-isomerase; Provisional
MKLSDFDFDLPSELIAQYPSSERDNSDLLIAVTPPIKTKFYNIIDYLKEGDLLVFNNSKVIKAKLNLGKN
ITINLNQKLSDDSWSAFAKPARKLHVGDEFYFDNHKVIITEKLAMGEIKVKFELNNISVFEFLDKYGEMP
LPVYIRRSHSLCHPVATTTGSKTYLNNDWIPWSNHGMTNTKNDNDRYQTVYSQIEGSVAAPTAGLHFTKD
ILDKLKAKGIQTAFLTLHVGAGTFLPVKTENIHEHKMHTEYCSITPETAEIINKAKQEGRRIIAVGTTTL
RTLESSCNNGIVKAGSFETDIFITPGFKFQTADMLLTNFHFPKSTLFMLICAFAGFKEMHELYKYAIKEK
MRFFSYGDATLLYRKV
>gnl|CDD|234955 PRK01433, hscA, chaperone protein HscA; Provisional
MQIIEIREPEQADFKQERQIAVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGNNK
GLRSIKRLFGKTLKEILNTPALFSLVKDYLDVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTN
ITKAVITVPAHFNDAARGEVMLAAKIAGFEVLRLIAEPTAAAYAYGLNKNQKGCYLVYDLGGGTFDVSIL
NIQEGIFQVIATNGDNMLGGNDIDVVITQYLCNKFDLPNSIDTLQLAKKAKETLTYKDSFNNDNISINKQ
TLEQLILPLVERTINIAQECLEQAGNPNIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGA
ALQAENLIAPHTNSLLIDVVPLSLGMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGER
EMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGILSVSAYEKISNTSHAIEVKPNHGIDKTEIDIM
LENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSESEISIINSLLDNIKEAVHARDIILIN
NSIKEFKSKIKKSMDTKLNIIINDLLKGKNINQIK
>gnl|CDD|167232 PRK01441, PRK01441, Maf-like protein; Reviewed
MAGRPKLVLASGSPRRVELLNQAGIEPDRLMPADIDETPKRAEHPRSLARRLSREKAEAALEALQGDDDW
RGAYILAADTVVAVGRRILPKAELVDEASQCLRLLSGRNHRVYTGVCLVTPDGKLRQKLVETRVRFKRLS
REDIEAYLASGEWRGKAGGYAIQGIAGSFVVKLVGSYTNVVGLPLYETVSLLAGEGFPVRAGWLEGK
>gnl|CDD|179298 PRK01470, tatA, twin arginine translocase protein A; Provisional
MGMSFSHLLIVLLIIFVLFGAGKLPQVMSDLAKGLKAFKDGMKDDGSDNDK
>gnl|CDD|100879 PRK01474, atpC, F0F1 ATP synthase subunit epsilon; Validated
MNETILVKIITPLSIAFEKQAKMVTMPGEEGMFGVLPSHVPMIVSLKAGLVQVYIDDMHKSENTYLISGG
VTEVTGNYINIATETAINVTNLSEAEIATKLLDLQKTLSDQH
>gnl|CDD|134562 PRK01482, fliE, flagellar hook-basal body complex protein FliE
VDSFFTDNNVYLVKKNPLHFDVNNFSSFDVAKNKKAKTFKDTLLNAIDDVNNSQLNVSKVTEQAILDPES
VDVHDVTIAMAKANMNLSIAKAVVERSIKAYQDIINIR
>gnl|CDD|134567 PRK01530, PRK01530, hypothetical protein; Reviewed
MDKFYNYNSSSHQALLNLKVKPNAKQNLISNFVIINNIPYLKLSIKAIPEQGKANEEIINYLAKEWKLSR
SNIEIIKGHTHSLKTILIKNINEDYLNLIINSYIK
>gnl|CDD|234958 PRK01544, PRK01544, bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed
MQYSIKQILSDATDKLNKIGISSPQLEARILLQHVINKPIEYLLINLDEQLNEAEIEAFEKLLERRLKHE
PIAYITGVKEFYSREFIVNKHVLIPRSDTEVLVDVVFQCHSRESGNPEKKQLNPCFRGNDISSNCNDKFL
NILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTDRIQIIHSNWFENIEKQKFDFI
VSNPPYISHSEKSEMAIETINYEPSIALFAEEDGLQAYFIIAENAKQFLKPNGKIILEIGFKQEEAVTQI
FLDHGYNIESVYKDLQGHSRVILISPINLNRSYARRIGKSLSGVQQNLLDNELPKYLFSKEKLVNEKRKV
FLEIGFGMGEHFINQAKMNPDALFIGVEVYLNGVANVLKLAGEQNITNFLLFPNNLDLILNDLPNNSLDG
IYILFPDPWIKNKQKKKRIFNKERLKILQDKLKDNGNLVFASDIENYFYEAIELIQQNGNFEIINKNDYL
KPHDNYVITKYHQKAI
>gnl|CDD|100891 PRK01546, PRK01546, hypothetical protein; Provisional
MLSHELVERINFLAKKAKAEGLTEEEQRERQSLREQYLKGFRQNMLNELKGIKVVNEQGTDVTPAKLKAL
KKQDNAKLN
>gnl|CDD|179302 PRK01558, PRK01558, V-type ATP synthase subunit E; Provisional
MQFEVKDLINKIKKDGLEEAERLANEIILEAKEEAEEIIAKAEEEAKELKAKAEKEANDYKRHALEASRQ
AGRDLLISFEKSIKSLFKAALKDEVAEVYDSNFLRELIIRVVDSWVKGDKLEIILNESDLSELESILRAA
LGNKLKKGIELKPFKGISKGFKIQQKDGSLYYDFSAEAIADILFSYLNPRFKEVIKLV
>gnl|CDD|234961 PRK01581, speE, polyamine aminopropyltransferase
MPKHRKQSKIKIYRITSYKKDKRSELDSNKFELEQQLVENKQDKQGKQYKQDRGIQYAETKQDNQVQSEN
VVIVPTDSHNLDIWDEISLKEIQAGEHTNLFAEKSNYQNINLLQVSDIRLYLDKQLQFSSVDEQIYHEAL
VHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHVDLVDLDGSMINMARNVPELVSLNKSAFFDNRVN
VHVCDAKEFLSSPSSLYDVIIIDFPDPATELLSTLYTSELFARIATFLTEDGAFVCQSNSPADAPLVYWS
IGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAANSAYVLDQIEQLYVVPTPRTLPSLLFPLFQFKEEHLEQ
RNFALLNSESNLILHQCYKKEMEF
>gnl|CDD|234962 PRK01584, PRK01584, alanyl-tRNA synthetase; Provisional
MTLDELRKKYIDFFKSKGHVEIAGKSLIPENDPTVLFTTAGMHPLVPYLLGEPHPSGTRLVDVQKCLRTG
DIDEVGDLSHLTFFEMLGNWSLGAYFKEESIKYSFEFLTSPDYLNIPKDKLYVTVFEGDEEIPRDEETAS
VWESLGIPKDRIFYLSREHNWWGPVGETGPCGPDTEIFVDTGKPKCSVNCRPTCSCGKYFEIWNNVFMQY
NKDEDGNYEELKRKCVDTGMGIERTIAFLQGKSSVYDTEAFTPIIKRIEKISGKIYGQNEEDDRSIRIIA
DHIRAACFILGDPFVVLPSNVGQGYVLRRLIRRSIRHAKKLGIESHFLADLVDSVEEIYGSFYPELTEKK
DFIKEELNKEEEKFFKTLRKGEQEFIKLIPNLGSSKIIPGDIAFKLYDTYGFPYEITEELASEYGFTVDR
EGFDEHFKKHQKVSKKGADKVFKGGLADHSYETTKLHTATHLLHKALRLVLGDHVRQKGSNITAERLRFD
FSHPEKMTDDEIKKVEDIVNLQIKNDLSVKKEVMSLEEAREKGAMALFGEKYEDIVKVYEIDGFSKEVCG
GPHVENTGELGTFKIQKEQSSSSGVRRIRAILID
>gnl|CDD|234963 PRK01610, PRK01610, putative voltage-gated ClC-type chloride channel ClcB; Provisional
MFRRLLIATVVGILAALAVAGFRHAMLLLEWLFLSNDSGSLVNAATNLSPWRRLLTPALGGLAAGLLLWG
WQKFTQQRPHAPTDYMEALQTDGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFTP
RQEWKLWIACGAAAGMASAYHAPLAGSLFIAEILFGTLMLASLGPVVISAVVALLTTNLLNGSDALLYNV
QLSVTVQARDYALIISTGLLAGLCGPLLLTLMNASHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGN
GYSVVQSFLTAPPLLMLIAGIFLCKLLAVLASSGSGAPGGVFTPTLFVGLAIGMLYGRSLGLWLPDGEEI
TLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVISRTLRRDSIYRQHTAEHS
>gnl|CDD|234964 PRK01611, argS, arginyl-tRNA synthetase; Reviewed
MMMDIKELLAEALAAALEAGGLPELPAVLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEAIEK
VEIAGPGFINFFLDPAALAELVLAILEAGERYGRSDIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDAL
ARILEFAGYDVTREYYVNDAGTQIGMLIASLELLWRKAVDISLDEIKEDLDRLGVHFDVWFSESELYYNG
KVDEVVEDLKEKGLLYVESDGALWVRLTEFGDDKDRVLIKSDGTYTYFTRDIAYHLYKFERFDRVIYVVG
ADHHGHFKRLKAALKALGYDPDALEVLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLDEAVGRARELIEE
KEIAEAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPPYVQYAHARICSILRKAAEAGIDLLLALLT
EEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVLLKDEEEELRNARLALVKATAQ
VLKNGLDLLGISAPERM
>gnl|CDD|234965 PRK01614, tatE, Sec-independent protein translocase subunit TatA
MEGLSITKLLVVGILIVLLFGTSKLRTLGADLGAALKGFKKAMRNDDEVSTSVLGETKMSAETKTVAETK
AASDSQAAASVERKD
>gnl|CDD|234966 PRK01617, PRK01617, hypothetical protein; Provisional
MSQLCPCGSALEYSLCCQPYLSGEKVAPDPEHLMRSRYCAFVMKDADYLIKTWHPDCHAAAWRAEIIAGF
ANTEWLGLTVFEHTWGDADNEGFVEFVARFTEGGKTGRTAIIERSRFLKENGQWYYIDGTRPQFGRNDPC
PCGSGKKFKKCCGQ
>gnl|CDD|179310 PRK01622, PRK01622, membrane protein insertase YidC
MLKSYRAVLVSLSLLLVLVLSGCSNAAPIDAHSDGFFDHYFVYPFSFLIQFVAHHIGGSYGIAIIIVTLI
IRSLMIPLAVSQYKSQRGMQEKMAVMKPELDKIQAKLKVTKDLEKQKEYQKEMMELYKSGNINPLAMGCL
PLLIQMPILSAFYYAIRRTEEIASHSFLWFNLGHADHILPIIAGLTYFIQMKVSQSNGTSPEQVQMLKIQ
GIMMPAMILFMSFAAPSALVLYWITGGLFLMGQTIVLRKVMEREEK
>gnl|CDD|179311 PRK01625, sspH, acid-soluble spore protein H; Provisional
MDVKRVKQILSSSSRIDVTYEGVPVWIESCDEQSGVAQVYDVSNPGESVHVDVTALEEK
>gnl|CDD|167247 PRK01631, PRK01631, hypothetical protein; Provisional
MKNILFRINELSKKEKATGLTVDEKQEQQMLRQNYTQTFRGSLDSILLNTKIVDQNGLNVTPAALQDAQI
RLKLSK
>gnl|CDD|179312 PRK01636, ccrB, fluoride efflux transporter CrcB
MTREFIMLSVPRLADGFPLDIFVANVVAAFLLGLTTSLHKRDKISQYVHLMIGTGIMGGLSTFSSFVYGA
VEMAKSPGEVLVSICYLVASLIVGYIAVELGLMIGKKEKPKDPQVASE
>gnl|CDD|179313 PRK01637, PRK01637, virulence factor BrkB family protein
ARHRLRPLWAFLKLLWQRIDEDNITVLAGYLAYVTLLSLVPLVAVVFSLFSAFPVFSEVSGQLKHFIFAN
FVPAAGDVVQEYIEQFVANSSKMTAVGICGLIVVALMLISSIDKALNTIWRSKRKRPKVYSFAVYWMILT
LGPLLAGASLAISSYLLSLRWFEASDLSGVIDNLLRILPLLLSWLSFWLLYSVVPNKKVPFRHALVGALV
AALLFELGKKGFALYITTFPSYQLIYGALAVIPILFVWVYLSWCIVLLGAEITATLGEYRKLKQAAEQEE
DDEPKK
>gnl|CDD|179314 PRK01641, leuD, 3-isopropylmalate dehydratase small subunit
MEKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDDGQPNPDFVLNQPRYQGASI
LLAGDNFGCGSSREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEANPGAE
LTVDLEAQTVTAPDKTFPFEIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKRPAFRPWL
>gnl|CDD|234967 PRK01642, cls, cardiolipin synthetase; Reviewed
FYTVLSWLGILLYWLLIAGVTLRILMKRRTVQGAIAWLLILYILPYVGIIAYLLFGELYLGKRRAERARL
MWPSTAKWLRDLKACKHIFAEENSEVAAPLFRLCERLQGIPGLKGNQLRLLTNGDETFQAIIRDIELARH
YILMEFYIWRPDGLGDQVAEALIAAAKRGVRVRLLYDSIGSFAFFRSPYPEELRNAGVEVVEFLKVNLGR
VFRRRLDLRNHRKIVVIDGYIAYTGSMNVVDPEYFKQDPGVGQWRDTHVRIEGPVVTALQLIFAEDWEWE
TGERILPPPPDVLIMPFEEASGHTVQVIASGPGDPEETIHQFLLTAIYSARERLWITTPYFVPDEDLLAA
LKTAALRGVDVRIIIPSKNDSLLVFWASRAFFTELLEAGVKIYRYEGGLLHTKSVLVDDELALVGTVNLD
MRSFWLNFEITLVIDDTGFAADLAAMQEDYFARSRELDLEEWRKRPLWQRIAERVARLFSPLL
>gnl|CDD|179316 PRK01655, spxA, transcriptional regulator Spx; Reviewed
MVTLFTSPSCTSCRKAKAWLEEHDIPFTERNIFSSPLTIDEIKQILRMTEDGTDEIISTRSKVFQKLNVD
VESLSLQDLIKLISDNPGLLRRPIIIDEKRLQVGYNEDEIRAFLPRKVRTFELREAQRRAN
>gnl|CDD|167253 PRK01658, PRK01658, CidA/LrgA family holin-like protein
MKFVKLLVQIALLYVFALVGTWIQEQLHLPIPGSIIGIFLLLLLLSFKILKLKWIELGAETLLAELPLFF
IPSAVGVMNYGDFLSSKGISLFLVVVISTFVVMIVTGYLTQLLAKRKEREQR
>gnl|CDD|234968 PRK01663, PRK01663, C4-dicarboxylate transporter DctA; Reviewed
MKKPLYKSLYFQVLVAIIIGILLGHFYPELGAQMKPLGDGFIKLIKMIIAPIIFCTVVTGIAGMGDMKKV
GRVGGKALLYFEIVSTIALIIGLIVVNVVQPGAGMNIDPATLDAKAVAQYAAQAHEQGTVDFLMDIIPTT
VVGAFASGDILQVLLFAVLFGFALARLGEKGKPVFDFIESLSHVLFGIVNMIMKLAPIGAFGAMAFTIGK
YGVGSLVQLGQLIGCFYITCILFVFVVLGAIARLTGFSIFKFIRYIKEELLIVLGTSSSESALPRMMEKM
EKLGCKKSVVGLVIPTGYSFNLDGTSIYLTMAAVFIAQATNTPLSIGHQITLLAVLLLTSKGAAGVTGSG
FIVLAATLSAVPHIPVAGLALILGIDRFMSEARALTNLIGNGVATVVVAKWEKELDREKLDRVLNGRAPD
GKTEEVSV
>gnl|CDD|234969 PRK01678, rpmE2, type B 50S ribosomal protein L31
MKKGIHPEYRPVVFHDTSTGFKFLTGSTITTDETIEWEDGKTYPLVKVEISSASHPFYTGKQKFVDTEGR
VEKFNKRFGRFASKKKK
>gnl|CDD|234970 PRK01683, PRK01683, trans-aconitate 2-methyltransferase; Provisional
MSDWNPSLYLKFEDERTRPARDLLARVPLENPRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAE
ARSRLPDCQFVEADIASWQPPQALDLIFANASLQWLPDHLELFPRLVSLLAPGGVLAVQMPDNLDEPSHV
LMREVAENGPWEQNLPDRGARRAPLPPPHAYYDALAPAACRVDIWHTTYYHPMPSAQAIVEWVKGTGLRP
FLDPLTESEQAAFLAAYLARIAEAYPLQADGKVLLAFPRLFIVARRKE
>gnl|CDD|179322 PRK01699, fliE, flagellar hook-basal body complex protein FliE
MKIQPMLNTQPFGAIQSIGAPKTSQTSVVEGKKFIDLLEDMNQTQNNAQTAVYDLLTKGVGETHDVLIQQ
KKAESQMKTAALVRDNLIENYKSLINMQI
>gnl|CDD|234973 PRK01712, PRK01712, carbon storage regulator CsrA
MLILTRKVGESLMIGDDIEVTVLGVKGNQVRIGINAPKEVSVHREEIYQRIQAENSTALKQSSY
>gnl|CDD|167263 PRK01713, PRK01713, ornithine carbamoyltransferase; Provisional
MAFNLKNRHLLSLVNHTEREIKYLLDLSRDLKRAKYAGTEQQRLKGKNIALIFEKTSTRTRCAFEVAAYD
QGAQVTYIDPNSSQIGHKESMKDTARVLGRMYDAIEYRGFKQSIVNELAEYAGVPVFNGLTDEFHPTQML
ADVLTMIENCDKPLSEISYVYIGDARNNMGNSLLLIGAKLGMDVRICAPKALLPEASLVEMCEKFAKESG
ARITVTDDIDKAVKGVDFVHTDVWVSMGEPLETWGERIKLLMPYQVTPELMKRTGNPKVKFMHCLPAFHN
SETKVGRQIAEKYPELANGIEVTEDVFESPMNIAFEQAENRMHTIKAVMVASLA
>gnl|CDD|234975 PRK01723, PRK01723, 3-deoxy-D-manno-octulosonic-acid kinase; Reviewed
TMQIIQTGNGAILFDAERLRDPDPALFDPDFWQQQARVVGSAKGRGTTWFVQTPGVNWVLRHYRRGGLIG
KLSKDRYLFTGLERTRAFAEFRLLAQLYEAGLPVPRPIAARVVRHGLFYRADILIERIEGARDLVALLQE
APLSEEQWQAIGQLIARFHDAGVYHADLNAHNILLDPDGKFWLIDFDRGELRTPTRWKQANLARLLRSFN
KEQGKRPILAFSEQDWQALLAGYQAAWGR
>gnl|CDD|234976 PRK01736, PRK01736, hypothetical protein; Reviewed
SIQNTLPGYNELNQELKQQGVALTPAEMHGLLSGMICGGNNDSSWQPLLHDLTNEGMAFPHALAQPLRQL
HQATSDALTDDGFLFQLLLPEGEDSVFDRADALAGWVNHFLLGLGLAQPKLDKVSGETGEAIDDLRNIAQ
LGYDEDEDQEELAQSLEEVIEYVRVAALLCHDEFTRPQPTAPEDQKPTLH
>gnl|CDD|234978 PRK01747, mnmC, bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC
MMDSIQPATLEFNEDGTPVSRQFDDVYFSNDNGLEETRYVFLGGNGLPERWAEHPRRRFVIAETGFGTGL
NFLATWQAFDQFRQRHPPARLKRLHFISFEKFPLTRADLARAHQHWPELAPLAEQLQAQWPLLLPGCHRL
LFDDGRVTLDLWFGDANELLPQLDARADAWFLDGFAPAKNPDMWSPNLFNALARLARPGATLATFTSAGF
VRRGLQEAGFTVRKVKGFGRKREMLVGELEQTLPAPLAAPWFARPGSPKARDAAIIGGGIAGAALALALA
RRGWQVTLYEADEAPAQGASGNRQGALYPLLSKDDNALSRFFRAAFLFARRFYDALPAAGVAFDHDWCGV
LQLAWDEKSAEKIAKMLALGLPAELARALDAEEAEELAGLPVPCGGIFYPQGGWLCPAELCRALLALAGQ
QLTIHFGHEVARLEREDDGWQLDFAGGTLASAPVVVLANGHDAARFAQTAHLPLYSVRGQVSHLPTTPAL
SALKQVLCYDGYLTPQPANGTHCIGASYDRDDTDTAFREADHQENLERLAECLPQALWAKEVDVSALQGR
VGFRCASRDRLPMVGNVPDEAATLAEYAALANQQPARDAPRLPGLYVAGALGSRGLCSAPLGAELLASQI
EGEPLPLERDLLAALHPNRFWVRKLLKGKAVK
>gnl|CDD|234979 PRK01749, PRK01749, disulfide bond formation protein DsbB
MLRFLNQCSQGRGAWLLLAFTALALELTALYFQHVMLLKPCVMCIYERVALFGILGAGLIGAIAPKTPLL
RWLALLIWLYSAWKGLQLALEHTDYQLNPSPFNTCDFFVEFPSWLPLDKWLPSVFVASGDCSERQWQFLG
LEMPQWLVVIFAAYLVVAVLVLISQFFKAKKRDLFG
>gnl|CDD|179332 PRK01752, PRK01752, YchJ family protein
TALLLEACPCQSGKHYADCCGPFHLRQAFPETAEQLMRSRYAAYVLKNIDYIVETTVPSQQTLLDPAALQ
TWAENTTWLGLEILAHESLTKIHSAVEFKAIFQGEEGEQAHHERSLFVKIDNRWYFVDPTVPLPTMKQPC
VCGSGKKFKHCCGGYL
>gnl|CDD|234980 PRK01759, glnD, bifunctional uridylyltransferase/uridylyl-removing protein GlnD
LLTPSAVKIQKENLKQFELENFSQEDVFELIENRSDFYDQLLIHLWQQFGLEEQSDLALIAVGGYGRREM
FPLSDLDILILTEQPPDEETEEKINQFFQFLWDCGFEVGASVRTLAECESEGRADITIATNLLESRFLTG
NEKLFDALVELLQQADFWSKEAFFQAKIQEKIERYQRYHNTSYNLEPDIKYSPGGLRDLHLLYWIALRHS
GAKSLEEILQSGFIYPEEYAELQQSQQFLFKVRFALHLILKRYDNRLLFDRQLKVSELLGFQGEGNQGVE
KMMKSFFQALQSISLLSDLLVKHYREHFLQPNQNVEIQPLDDDFYLINNAICLRNPDCFEQQPESILDLF
FYLTQYPQAEIHSTTLRQLRLALEQLQQPLCELPAARERFLRLFNQPNAIKRALVPMHQYGVLTAYLPQW
KGIVGLMQFDLFHIYTVDEHTLRVMLKLESFLDEESAEQHPICHQIFSQLSDRTLLYIAALFHDIAKGRG
GDHAELGAVDMRQFAQQHGFDQREIETMAWLVQQHLLMSVTAQRRDIHDPEVVMNFAEEVQNQVRLDYLT
CLTVADICATNETLWNSWKRSLFATLYQFTNQQFQQGMDELLDYQEKAEENRQQALELLQQKYSALSETQ
IEQLWQRCPEDYFLRNTPKQIAWHALLLLDFRGDLLVKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGA
KKLSIHDAQIITSQDGYVLDSFIVTELNGKLLEFDRRRQLEQALTKALNTNKLKKLNLEENHKLQHFHVK
TEVRFLNEEKQEQTEMELFALDRAGLLAQVSQVFSELNLNLLNAKITTIGEKAEDFFILTNQQGQALDEE
ERKALKSRLLSNLS
>gnl|CDD|234981 PRK01766, PRK01766, multidrug efflux protein; Reviewed
MKETQKYKSEARQLLALALPILLAQVAQTAMGFVDTVMAGGVSATDLAAVAIGTSIWLPVILFGHGLLLA
LTPIVAQLNGAGRRERIAHQVRQGLWLALFLSVLIMLVLYNAVPPILNMMNLEPEVADIAVGYLHALLWG
IPAYLLYQVLRSFIDGLGKTKPTMVIGFLGLLINIPLNYIFIYGKFGFPELGGVGCGVATAIVYWVMFLA
MLIYIKRARRFRDFRLFKGLYKPDWAVIKRLLKLGLPIGLAIFFEVSLFAVVTLLVSPLGTVTVAAHQIA
LNFSSLLFMLPLSLAMALTIRVGFELGAGRTLDARQYAYIGLAVGLGMALLTAIFLVLFREQIALLYTDD
PEVVALASHLLLFAALFQFSDAIQVIGSGALRGYKDTRVIFFITFIAYWVLGLPLGYILALTDPMGPFGF
WIGLIIGLTAAAILLLLRLRKLQRQPSAIILQRAAR
>gnl|CDD|179335 PRK01773, hscB, Fe-S protein assembly co-chaperone HscB
MNNPFALFDLPVDFQLDNALLSERYLALQKSLHPDNFANSSAQEQRLAMQKSAEVNDALQILKDPILRAE
AIIALNTGEQQNLEEKSTQDMAFLMQQMEWREQLEEIEQQQDEDALTAFSKEIKQEQQAILTELSTALNS
QQWQQASQINDRLRFIKKLIIEIERVEEKLFDF
>gnl|CDD|234982 PRK01777, PRK01777, RnfH family protein
MGKIRVEVVYALPERQYLQRLTLQEGATVEEAIRASGLLELRTDIDLAKNKVGIYSRPAKLTDVLRDGDR
VEIYRPLLADPKELRRKRAEQAKKK
>gnl|CDD|179337 PRK01810, PRK01810, DNA polymerase IV; Validated
PKKGRVIFHVDMNSFFASVEIAYDPSLQGKPLAVAGNEKERKGIIVTCSYEARAYGIRTTMPLWEAKRLC
PQLIVRRPNFDRYREASRQMFQILSEFTPLVQPVSIDEGYLDITDCYALGSPLEIAKMIQQRLLTELQLP
CSIGIAPNKFLAKMASDMKKPLGITVLRKRDVPEMLWPLPVGEMHGIGEKTAEKLKDIGIQTIGDLAKAD
EHILRAKLGINGVRLQRRANGIDDRPVDPEAIYQFKSVGNSTTLSHDMDEEKELLDVLRRLSKSVSKRLQ
KKTVVSYNVQIMIRYHDRRTITRSKTLKNPIWEKRDIFQAASRLFKQHWNGDPVRLLGVTATDLEWKTEA
VKQLDLFSFEEDAKEEPLLAVIDQINDKYGMPLLQRGSQLLRKQEKTFGTSFEKDFM
>gnl|CDD|179338 PRK01816, PRK01816, hypothetical protein; Provisional
VGFFSLFKRGQHYMKTWPLEKRLAPVFPENRVIKATRFAIRFMPPLAVFTLCWQIALGGQLGPAVATALF
ALSLPLQGLWWLGKRSVTPLPPALLNWFYEVREKLQEAGQALAPVEGKPTYQALADLLKRAFKQLDKTFL
DDL
>gnl|CDD|234983 PRK01821, PRK01821, hypothetical protein; Provisional
MSKMLNIIWQYLRAFVLIYACLYAGIFIASLLPITIPGSIIGMLILFVLLALQILPAKWVKPGCSLLIRY
MALLFVPIGVGVMQYYDLLRAQFGPIVVSCIVSTLVVLLVVGWSSHYVHGERKVIGQKGKEEK
>gnl|CDD|234984 PRK01827, thyA, thymidylate synthase; Reviewed
MKQYLDLLRKILDEGTKKNDRTGTGTLSVFGAQMRFDLSKGFPLLTTKKVHFKSIIHELLWFLRGDTNIA
YLQENGVHIWDEWADENGDLGPVYGKQWRSWPTPDGRHIDQISKVIEQLKTNPDSRRLIVSAWNPGELDK
MALPPCHALFQFYVADGKLSCQLYQRSADVFLGVPFNIASYALLTHMIAQQTGLKVGEFVHTIGDAHIYS
NHLEQAREQLSREPRPLPKLVINPDIKSIFDFEFEDFELEGYDPHPAIKAPVAV
>gnl|CDD|167284 PRK01833, tatA, Sec-independent protein translocase subunit TatA
MGGISIWQLLIIVAIIVLLFGTKKLRTLGTDLGESVKGFKKAMADDKPKDAEFEKVEAKEAASTEQKAKE
KEQA
>gnl|CDD|234985 PRK01842, PRK01842, hypothetical protein; Provisional
MQPATMAPARPDACPCGGAAPGAAANARAPRYAACCGRFIDGGAAAPTALELMRSRYSAYVLGATDYLRA
TWDPSTCPADLDADPAAADAPRWLGLAIKRHAQLDATHAEVEFVARYKVGGRAHRLHETSRFVRDEQGRW
RYVDGDVSE
>gnl|CDD|100947 PRK01844, PRK01844, YneF family protein
MPIWLGILVGVVALVAGVALGFFIARKYMMNYLQKNPPINEQMLKMMMMQMGQKPSQKKINQMMSAMNKQ
QM
>gnl|CDD|234987 PRK01862, PRK01862, voltage-gated chloride channel ClcB
VLSFLLKLRTRAQTLFRLSDAHTMLIWSAIVGIGGAFATTAFREGIELIQHLISGHSGSFVEMAKSLPWY
VRVWLPAAGGFLAGCVLLLANRGARKGGKTDYMEAVALGDGVVPVRQSLWRSASSLLTIGSGGSIGREGP
MVQLAALAASLVGRFAHFDPPRLRLLVACGAAAGITSAYNAPIAGAFFVAEIVLGSIAMESFGPLVVASV
VANIVMREFAGYQPPYEMPVFPAVTGWEVLLFVALGVLCGAAAPQFLRLLDASKNQFKRLPVPLPVRLAL
GGLLVGVISVWVPEVWGNGYSVVNTILHAPWTWQALVAVLVAKLIATAATAGSGAVGGVFTPTLFVGAVV
GSLFGLAMHALWPGHTSAPFAYAMVGMGAFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTAR
ALGTTSMYEITLRRHQDEAERERLRTTQMRELIQPAQTVVPPTASVADMTRVFLEYPVKYLYVVDDDGRF
RGAVALKDITSDLLDKRDTTDKTAADYAHTPFPLLTPDMPLGDALEHFMAFQGERLPVVESEASPTLAGV
VYKTSLLDAYRRMN
>gnl|CDD|179345 PRK01885, greB, transcription elongation factor GreB; Reviewed
AMKTNYITREGYARLKQELDYLWREERPEVTQKVSWAASLGDRSENADYIYGKKRLREIDRRVRFLTKRL
ENLKVVDYSPQQEGKVFFGAWVEIENEDGEEKRFRIVGPDEIDGRKGYISIDSPMARALLKKEVGDEVTV
NTPAGEAEWYVNEIEYV
>gnl|CDD|234988 PRK01889, PRK01889, GTPase RsgA; Reviewed
SMNQNSLQSLGWDPFFQQQFAPYEEEGLEPGRVVEEHRSGYVVATEEGEVRAEVSGKWRHEAFPPGDRPA
VGDWVLLDNEKKARIVRLLPRRSLFSRKAAGTRSEEQLIAANVDTVFIVCSLNHDFNLRRIERYLALAWE
SGAEPVIVLTKADLCEDAEEKIAEVEALAPGVPVLAVSALDGEGLDVLAAWLSGGKTVALLGSSGVGKST
LVNALLGEEVQKTGAVREDDSKGRHTTTHRELHPLPSGGLLIDTPGMRELQLWDAEDGVEETFSDIEELA
AQCRFRDCAHEAEPGCAVQAAIENGELDERRLQSYRKLQREQAYNAAKLAARLARAERKKWKKISKQVKK
MKRKKR
>gnl|CDD|234989 PRK01903, rnpA, ribonuclease P protein component
MHTNTLRKHEILRKKKVISLLFEGGKSFKGFPLRVVYLSLEEGGSESAPASVLFSVSKKRVPRAVKRNRI
KRLMREAYRLEKHVLLDRLETDAGAKNRQLAIAFLYTGRSDEIPSLAEFRREMRKLLQRIREK
>gnl|CDD|234990 PRK01904, PRK01904, DUF2057 domain-containing protein
MKLRKAALAVATLLTSTASFAGMVTTSSNIDFLAIDGQKASKSLLKEAKSFNINDTQVHQVVVRVSEIVR
SGSDRSLFESDPIIVTFQGTTEDIVISAPKLTNERDIDKFKKSPNITVKTASGKEISTKQDYLKQEGFFP
NSNLIDNLSEYNASGAVASVPAFATATSMVAGAAGNAKANKGKVVVQGENVAEQQLQYWFQQADKETQTR
FLNWAKKQK
>gnl|CDD|179348 PRK01905, PRK01905, Fis family transcriptional regulator
MSKHNIEQCIRDSLDQYFRDLDGSNPHDVYDMVLSCVEKPLLEVVMEQAGGNQSLAAEYLGINRNTLRKK
LQQHGLL
>gnl|CDD|179350 PRK01908, PRK01908, electron transport complex protein RnfG; Validated
MRKHGITLALFAALCTGLTAVVNQLTKDTIAEQAALQQKALLDQVIPAERYDNDLQESCYLVTDPALGKD
GPHRVYIARKDGKPVAAAIEATAPDGYSGAIQLLVGADFNGTVLGVRVLEHHETPGLGDKIELRISDWIT
HFSGKKISGENDKHWAVKKDGGDFDQFTGATITPRAVVNAVKRAALYAQTLPAQLSSLPACGEVQ
>gnl|CDD|234991 PRK01909, pdxA, 4-hydroxythreonine-4-phosphate dehydrogenase PdxA
MTPQPLQIAITTGEPAGVGPELTVRALADAAARWPDARFTVLGDAALLAARAAAVGADWARLAAGGHVTV
AHRPLAAPAEAGKLDAANGRYVLDLLDAAIDGALAGRYDAIVTAPLQKSTINDAGVPFTGHTEYLAERTH
TPRVVMMLAGTGPRPLRVALATTHLPLKDVSAALTIDGLVETLAIIDRDLRRDFGLAAPRILVTGLNPHA
GENGYLGREEIDVIEPALARARAAGIDARGPYPADTLFQPRYLEDADCVLAMFHDQGLPVLKYATFGEGI
NVTLGLPIIRTSVDHGTALDLAGTGRADPGSMIAAIDTAVTMARHRRAS
>gnl|CDD|179352 PRK01911, ppnK, inorganic polyphosphate/ATP-NAD kinase; Provisional
MKIAIFGQTYQESASPYIQELFDELEERGAEVLIEEKFLDFLKQDLKFHPSYDTFSDNEELDGSADMVIS
IGGDGTFLRTATYVGNSNIPILGINTGRLGFLATVSKEEIEETIDELLNGDYTIEERSLLQLESNPKLFG
ELNFALNEIAILKRDTSSMITVHTYLNGEYLNSYWADGLIVATPTGSTGYSLSCGGPIIVPDAKSFVITP
IAPHNLNVRPLVIPDDTEITLEVESRSDNFLVSLDSRSETVDNGTELTIKKADFTIKLVELNNHSFLKTL
RNKLLWGEDKRN
>gnl|CDD|179353 PRK01917, PRK01917, cation-binding hemerythrin HHE family protein; Provisional
MPVPEWSEELHLGDPFTDATHAEFVQLLNAVARADDADFLQALDAWIDHTRHHFAQEERWMEATKFGPRH
CHRAEHDEVLAVAADVREKVARDGDFELGRRLVAELPEWFDQHVRTMDAMMVSHLKMLGFDMVEVPAEA
>gnl|CDD|179355 PRK01964, PRK01964, 4-oxalocrotonate tautomerase; Provisional
MPIVQIQLLEGRPEEKIKNLIREVTEAISATLDVPKERVRVIVNEVPSSHWGVAGVPKSELKEN
>gnl|CDD|234993 PRK01966, ddl, D-alanine--D-alanine ligase
MMKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGITKDGRWYLIDADNMELADDDNDKEDLS
LLILPSGGSEEVDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAP
YVVLTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGR
EIECAVLGNDPKASVPGEIVKPDDFYDYEAKYLDGSAELIIPADLSEELTEKIRELAIKAFKALGCSGLA
RVDFFLTEDGEIYLNEINTMPGFTPISMYPKLWEASGLSYPELIDRLIELALE
>gnl|CDD|179358 PRK02001, PRK02001, ribosome assembly cofactor RimP
MIKKKVVELLVEELLEGPELFLVDLTISPDNKIVVEIDGDEGVWIEDCVELSRAIEHNLDREEEDFELEV
GSAGLTSPLKVPRQYKKNIGRELEVLTKNGKKIEGELKSADENDITLEVKAREPKEGGKGKVTVEKEETI
TYDDIKEAKVII
>gnl|CDD|179360 PRK02047, PRK02047, hypothetical protein; Provisional
GAIIPPKESLIEYPSDFPIKVMGKAHPEFADTIFKVVSVHDPEFDLEKIEERPSSGGNYTGLTITVRATS
REQLDNIYRALTGHPMVKVVL
>gnl|CDD|179361 PRK02048, PRK02048, 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Provisional
MDLFNYSRRKTSVVNIGATPLGGPNPIRIQSMTNTSTMDTEACVAQAKRIIDAGGEYVRLTTQGVREAEN
LMNINIGLRSQGYMVPLVADVHFNPKVADVAAQYAEKVRINPGNYVDPGRTFKKLEYTDEEYAQEIQKIR
DRFVPFLNICKENHTAIRIGVNHGSLSDRIMSRYGDTPEGMVESCMEFLRICVEEHFTDVVISIKASNTV
VMVRTVRLLVAVMEAEGMHYPLHLGVTEAGDGEDGRIKSAVGIGALLADGIGDTIRVSLSEEPEAEIPVA
RKLVDYIRSRENHPYIPGMEAPGFDYLSPSRRKTRAVRNIGGDHLPVVIADRMDGDFEFDPQFLPDYIYA
GRELPEQREPGVQYILDADVWKEEPNTWPAFNYAQLELMETCAAELKFLFLPYMALTDEVLACLKAHPEV
VVILQSNHPNRVGEHRALAHQLMVAGLENPVIFFQHYAETTAEDLQLKAAADMGALIFDGLCDGIFLFNQ
GKLSHVVVDATAFGILQAGRLRTSKTEYISCPGCGRTLYDLQSTIARIKEATSHLKGLKIGIMGCIVNGP
GEMADADYGYVGAGRGKISLYKQKECVEKNIPEEEAVERLIELIKANGDWE
>gnl|CDD|179362 PRK02079, PRK02079, pyrroloquinoline quinone biosynthesis peptide chaperone PqqD
DRNQVPTLRPGYRFQWEPAQNCHVLLYPEGMIKLNESAGEILGLIDGKRTVAAIIAELQQQFPDVPGLDE
DVLEFLEVARAKHWIELV
>gnl|CDD|234997 PRK02090, PRK02090, phosphoadenylyl-sulfate reductase
LNALNALPKADLALDLAELNAELEGASAQERLAWALENFGGRLALVSSFGAEDAVLLHLVAQVDPDIPVI
FLDTGYLFPETYRFIDELTERLLLNLKVYRPDASAAEQEARYGGLWEQSVEDRDECCRIRKVEPLNRALA
GLDAWITGLRREQSGTRANLPVLEIDGGRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPC
TRPVEPGEDERAGRWWGGLKKECGLHEGNLP
>gnl|CDD|234999 PRK02101, PRK02101, peroxide stress protein YaaA
MLILISPAKTLDYDGPLDTDRLSQPELLDQSQELLDALRELSPDDLASLMKISDKLAGLNAARFQDWQPE
FTTANARPAILAFTGDVYDGLDADSLSEADLDYAQQHLRILSGLYGLLRPLDLIQPYRLEMGTKLPNPRG
KNLYAFWGDIITQALNEAAQGDEVLVNLASSEYFKAVKPKKLKARVITPVFLEEKNGKYKVISFYAKKAR
GLMARYLIENRITTPEDLKDFNFAGYAFDEELSTDDELVFVRKEQ
>gnl|CDD|179366 PRK02102, PRK02102, ornithine carbamoyltransferase; Validated
MAFNLKGRSFLKLLDFTPEEIEYLIDLSIELKAAKKAGIEHQYLEGKNIALIFEKTSTRTRCAFEVAAID
LGAHVTYLGPNDSQLGKKESIEDTARVLGRMYDGIEYRGFKQEIVEELAKYSGVPVWNGLTDEWHPTQML
ADFMTMKEHFGPLKGLKLAYVGDGRNNMANSLMVGGAKLGMDVRICAPKELWPEEELVALAREIAKETGA
KITITEDPEEAVKGADVIYTDVWVSMGEEDEWEERIKLLKPYQVNMDLMKATGNPDVIFMHCLPAFHDTE
TKVGKEIAEKYGLKGLEVTDEVFESKYSIVFDEAENRMHTIKAVMVATLGD
>gnl|CDD|179367 PRK02103, PRK02103, malonate decarboxylase acyl carrier protein
METLNYRFTARRRAKGARAAALVGVVASGNLEVLVERVLPGGECEVEIRTAAVGFGAVWQAVVADFVERR
SPGGLRISINDGGARPDTVSLRLAQAVRAIEGAAA
>gnl|CDD|235000 PRK02106, PRK02106, choline dehydrogenase; Validated
MTTMEYDYIIIGAGSAGCVLANRLSEDPDVSVLLLEAGGPDYRWDFFIQMPAALAFPLQGKRYNWAYETE
PEPHMNNRRMECPRGKVLGGSSSINGMVYIRGNAMDYDNWAELPGLEGWSYADCLPYFKKAETRDGGEDD
YRGGDGPLSVTRGKPGTNPLFQAFVEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTNGRRWSAARAYLDPA
LKRPNLTIVTHALTDRILFEGKRAVGVEYERGGGRETARARREVILSAGAINSPQLLQLSGIGPAEHLKE
LGIPVVHDLPGVGENLQDHLEVYIQYECKQPVSLYPALKWWNKPKIGAEWLFTGTGLGASNHFEAGGFIR
SRAGVDWPNIQYHFLPVAIRYDGSNAVKGHGFQAHVGPMRSPSRGSVKLKSADPRAHPSILFNYMSTEQD
WREFRDAIRLTREIMAQPALDPYRGREISPGADVQTDEEIDAFVREHAETAYHPSCTCKMGTDPMAVVDP
EGRVHGVEGLRVVDASIMPTITNGNLNAPTIMIAEKAADLIRGRTPLARSNAPYYVAGDWPVRQRAQRPR
>gnl|CDD|235002 PRK02110, PRK02110, disulfide bond formation protein B; Provisional
MNNDTLMLRRERRLLVLLGLICLALVGGALYLQYVKGEDPCPLCIIQRYAFLLIAIFAFLAAAMRNTRGV
WVLEGLIVLSALGGIAVAGRHVYIQLNPGFSCGIDALQPIVDSLPPAKWLPGVFKVDGLCETPYPPILGL
SLPGWALIAFVLIAVAVAVSLIRNRRRLR
>gnl|CDD|179371 PRK02113, PRK02113, MBL fold metallo-hydrolase
MKIRILGSGTSTGVPEIGCTCPVCTSKDPRDNRLRTSALVETEGARILIDCGPDFREQMLRLPFGKIDAV
LITHEHYDHVGGLDDLRPFCRFGEVPIYAEQYVAERLRSRMPYCFVEHSYPGVPNIPLREIEPDRPFLVN
HTEVTPLRVMHGKLPILGYRIGKMAYITDMLTMPEEEYEQLQGIDVLVMNALRIAPHPTHQSLEEALENI
KRIGAKETYLIHMSHHIGLHADVEKELPPHVHFAYDGLEIIF
>gnl|CDD|235003 PRK02114, PRK02114, formylmethanofuran--tetrahydromethanopterin formyltransferase; Provisional
MEINGVEIEDTFAEAFPMKVTRVLITAATKKWAKIAATEATGFATSVIGCPAEAGIERFLSPEETPDGRP
GVIILIFAMSKKELEKQLLERIGQCVLTAPTTAVFNGLEDAEEKIKLGKKLRFFGDGYEISKEIGGRRYW
RIPIMDGEFLIEETVGYVKGVAGGNFLILAESQAAALEAAEAAVDAIKEVPGVITPFPGGIVRSGSKVGS
KYKFMGASTNDAYCPTLKGKVEDSELPEGVNAVYEIVIDGLDEEAVAEAMRAGIEAACAVPGVVKISAGN
YGGKLGPHHFHLHELLA
>gnl|CDD|179373 PRK02118, PRK02118, V-type ATP synthase subunit B; Provisional
MQKIYTKITDITGNVITVEAEGVGYGELATVERKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFL
GRPMQVTYSESLLGRRFNGSGKPIDGGPELEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVES
QKIPIFSVSGEPYNALLARIALQAEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVE
CLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVD
FEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRGRIDPFGSLSRLKQLVIGKKTREDHGDLMN
AMIRLYADSREAKEKMAMGFKLSNWDEKLLKFSELFESRLMDLEVNIPLEEALDLGWKILAQCFHPEEVG
IKEQLIDKYWPKNCLH
>gnl|CDD|235004 PRK02119, PRK02119, hypothetical protein; Provisional
MQIQQNLENRIAELEMKIAFQENLLEELNQALIEQQFVIDKMQVQLRYMANKLKDMQPSNIASQAEETPP
PHY
>gnl|CDD|235005 PRK02122, PRK02122, glucosamine-6-phosphate deaminase-like protein; Validated
ITLNRIPSRYYRPANAFEKSEETRFEKIPTDIFESSEEASRAVAQEIATLIRERQAEGKPCVLGLATGSS
PIGVYAELIRMHREEGLSFKNVITFNLDEYYPMQPDSLQSYHRFMKENLFDHVDIPPENIHIPDGTIPKE
EIDEYCRDYEEKIEAAGGIDFQLLGIGRTGHIGFNEPGSGRNSRTRLVTLDHITRRDAASDFFGEENVPR
KAITMGVGTILKARRIVLLAWGEHKAPIIKRAVEGEISDEVPASYLQEHPNATFVLDLAAASELTRIKTP
WLVTSCEWTDKLIRRAVVWLCQKLGKPILKLTDKDYNENGLSDLLAQYGSAYNVNIKVFNDLQHTITGWP
GGKPNADDTNRPERALPYPKRVIIFSPHPDDDVISMGGTFRRLVEQGHDVHVAYQTSGNIAVFDEEVLRF
ADFINDFNQIFGISSDELKKKYEEIIEFLKNKKPGEIDSPEVRKLKGLIRRGEARAACRYVGLPDEHVHF
LDLPFYETGTVRKNPIGEADVEIVMDLLEEIKPHQIFVAGDLADPHGTHRVCLDAIFAALDRLKEEEWMK
DCRVWLYRGAWQEWEIHEIEMAVPLSPEELLRKRNAIFKHQSQKDSAPFPGDDEREFWQRAEDRNRGTAD
LYDQLGLAEYEAMEAFVRYKFM
>gnl|CDD|235006 PRK02126, PRK02126, ribonuclease Z; Provisional
MFRLLEPRLVNGPFDDPGLYVDFLFERRALLFDLGDLHHLPPRELLRISHIFVSHTHMDHFIGFDRLLRH
CLGRPRRLRLFGPPGFADQVEHKLAGYTWNLVENYPTTFRVHEVELHDGRIRRALFSCRRAFAREAEEEL
SLPDGVLLDEPWFRVRAAFLDHGIPCLAFALEEKAHINIDKNRLAELGLPPGPWLRELKHAVLRGEPDDT
PIRVLWRDGGGEHERVRPLGELKERVLRIEPGQKIGYVTDIGYTEENLARIVELAAGVDLLFIEAVFLDE
DAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQGRGAELYREARAAFAG
>gnl|CDD|235007 PRK02134, PRK02134, chitin disaccharide deacetylase
MERLLIVNADDFGLSKGQNYGIIEAHRNGVVTSTTAMVNMPAIDHAVQLSREYPSLGVGMHFVLTAGKPL
TAMPSLTDRDGLLGKWIWQLAEEGTLPLEEIAQELAAQYERFLSLFGRKPTHLDSHHHVHMLPQIFPIVA
RFAAEYGVPLRIDSNAGDLPANLRSSDGFSSDFYGEEVSEDLFLQLLDRSKHRGEQSLEVMCHPAFIDNT
LRQSAYCYPRLTELEVLTSASLKEAIAERGYRLGSYLDL
>gnl|CDD|235008 PRK02135, PRK02135, hypothetical protein; Provisional
MRQFVIIAHKAPTDPDFSLKDLPGSAGRLDILCRCVNSAFFLSHDIRRDVRVHLVLEGTPDPPKTIRFEG
SELRRLNPDERSTAALIKKALDASEGMIGEQEREVTPGIYVRRRGFEDLLEELAEGKTLYYLHEDGEDIR
DVEFPENPVFVLGDHIGFTEEEENLLKRLGAEKISLGPKMLHADHCITLIHNELDRRGYER
>gnl|CDD|235009 PRK02141, PRK02141, Maf-like protein; Reviewed
MPDTVCRPPRLILASSSRYRRELLERLRLPFDVVSPDIDETPLAGETPAATALRLAAAKARAVAATIDAP
PGALVIGSDQVATFDGLQIGKPGTHERALAQLQAMRGRTVEFHSALCLYDSRTGETQSEDVVTRVRFRTL
TDAELDAYLRAETPYDVAGSAKSEGLGIALLDAIDSDDPTALVGLPLIALTRMLRAAGYPLFAAPAA
>gnl|CDD|179379 PRK02155, ppnK, NAD kinase
MKSQFKTVALIGRYQTPGIAEPLESLAAFLAKRGFEVVFEADTARNIGLTGYPALTPEEIGARADLAVVL
GGDGTMLGIGRQLAPYGVPLIGINHGRLGFITDIPLDDMQETLPPMLAGNYEEEERMLLEARVVRDGEPI
FHALAFNDVVVNRSGFSGMVELRVSVDGRFMYNQRSDGLIVATPTGSTAYALSAGGPILHPQLPGWVLVP
IAPHTLSNRPIVLPDDSEVAIQIVGGRDVSVNFDMQSLTSLELGDRIEVRRSPHTVRFLHPVGYSYYATL
RKKLHWNEGPS
>gnl|CDD|167325 PRK02166, PRK02166, hypothetical protein; Reviewed
MPIQNSPYEAFAALLSSSGHPVSPAELHGLLLGRSCAGAGFDADAWLADAAELLEGEPGDNVRAALIGLQ
EMVKGELTADDVAVVLLLPDDDAPLTERAAALGQWCQGFLAGFGLNAGGKDLSGEAKEVLQDLAAISQVQ
DALEESEDGETDYMEVMEYLRVAPLLLFTEFAKPAAPAPKPSLH
>gnl|CDD|235010 PRK02186, PRK02186, argininosuccinate lyase; Provisional
MTGIFVFIESNTTGTGELLLRKALLRGFTPYFLTANRGKYPFLDAIRVVTISADTSDPDRIHRFVSSLDG
VAGIMSSSEYFIEVASEVARRLGLPAANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDG
LTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAGTRAALVQAYVEGDEYSVETLTVARGHQVLGIT
RKHLGPPPHFVEIGHDFPAPLSAPQRERIVRTVLRALDAVGYAFGPAHTELRVRGDTVVIIEINPRLAGG
MIPVLLEEAFGVDLLDHVIDLHLGVAAFADPTAKRYGAIRFVLPARSGVLRGLLFLPDDIAARPELRFHP
LKQPGDALRLEGDFRDRIAAVVCAGDHRDSVAAAAERAVAGLSIDIGDAARAAALNDAGAGAARPGLPPE
AQAIVYGPGASEAPLAELDHLAAIDEAHLVMLGDTGIVAPERARPLLDAHRRLRDAGFAPLLARPAPRGL
YMLYEAYLIERLGEDVGGVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPI
YSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGAGAGGGTTFPIDPEFVARLLGFEQPAP
NSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTGGSSMLPQKKNPFLLEFVK
GRAGVVAGALASASAALGKTPFSNSFEAGSPMNGPIAQACAAIEDAAAVLVLLIDGLEADQARMRAHLED
GGVSATAVAESLVVRRSISFRSAHTQVGQAIRQSLDQGRSSADALAALDPQFVSRAPLEWARSHRFGGGP
GAADLNAGLARACAALRDDEAVFRRRQDVWREAEAMRRGAVQQLAGD
>gnl|CDD|235011 PRK02190, PRK02190, agmatinase; Provisional
QADESLYSNAFSFLRRPLNFTPYLSGADWVVTGVPFDMATSGRPGARFGPAAIRQASTNLAWEDRRYPWN
FDLFERLAVVDYGDLVFDYGDAEDFPEALEAHAEKILAAGKRMLTLGGDHFITLPLLRAHAKHFGPLALV
HFDAHTDTWADGGSRIDHGTMFYHAPKEGLIDPAHSVQIGIRTEYDKDNGFTVLDARQVNDRGVDAIIAQ
IKQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIGGLTSAQALKILRGLKGLNIVGMDVVEVAPAYDHAEIT
ALAAATLALEMLCLQAAKKGE
>gnl|CDD|179381 PRK02193, truB, tRNA pseudouridine synthase B; Provisional
MIKLLYKPKGISSFKFIKNFAKTNNIKKIGHTGTLDPLASGLLLVATDEDTKLIDYLDQKDKTYIAKIKF
GFISTTYDSEGQIINVSQNIKVTKENLEEALNNLVGSQKQVPPVFSAKKVNGKRAYDLARQGKQIELKPI
EIKISKIELLNFDEKLQNCVFMWVVSRGTYIRSLIHDLGKMLKTGAYMSDLERTKIGNLDKNFLNQSLNP
LDLIDLEQVKLDKEELELLLQGKKISFFANSEEYALIFKDEIVGIGKIINNVLKSKKLFGNKIKKILND
>gnl|CDD|179382 PRK02195, PRK02195, V-type ATP synthase subunit D; Provisional
MMSKIKLTKNSLKKQKKQLKMLERYLPTLKLKKAQLQAEVRRAKAEAAELEQEYQKLRQAIEAWISLFSE
PLYFDEDLIKVKKVEKDYENIAGVEVPILDSIEFEIIEYSLLNTPIWVDTGIELLKELVQLKIEAEVLQE
RLLLLEEELRKTTQRVNLFEKVLIPETKANIKKIKIFLGDQETAAVVRQKIAKKKIEKRKE
>gnl|CDD|235012 PRK02201, PRK02201, putative inner membrane protein translocase component YidC; Provisional
MKKIRSKAYDYFNSASNNNKKKKKKKIFKKVWKWLKIFFYIFLFGIGLTGCVQSFVVKSSTNVGSGLEFY
TNKESKNNYRYLFISSNTGPYNPITSWTWKYGPFYGLFVYPIAQIILSIMASQSLSELYGWSTILAIIVV
VLIIRLISFLITFKSTFNQEKQEELQGKKAKIDAKYKDYKKDKQMKQRKQQEIQELYKKHNISPFSPFVQ
MFVTLPIFIAVYRVVQSLPSIKVTTWLGIDLSATSWQEIFAGNWIYLPILIIVVPVQALSQLLPQILNKK
KNKERTLNVKEKEALKKQNKTQNIISIVFIFFGVIFAAGVQIYWIIGGIWTILQTLGIHYFKKRKFYKQK
YEPKLRA
>gnl|CDD|235013 PRK02220, PRK02220, 4-oxalocrotonate tautomerase; Provisional
MPYVHIKLIEGRTEEQLKALVKDVTAAVSKNTGAPAEHIHVIINEMSKNHYAVGGKRLSDK
>gnl|CDD|179385 PRK02224, PRK02224, DNA double-strand break repair Rad50 ATPase
MRFDRVRLENFKCYADADLRLEDGVTVIHGVNGSGKSSLLEACFFALYGSKALDDTLDDVITIGAEEAEI
ELWFEHAGGEYHIERRVRLSGDRATTAKCVLETPEGTIDGARDVREEVTELLRMDAEAFVNCAYVRQGEV
NKLINATPSDRQDMIDDLLQLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNG
LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEE
VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED
ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE
RDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEE
VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAA
AEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLA
EKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERR
EALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLERMLNETFDLVYQNDAYSHIELDGEYELTVY
QKDGEPLEPEQLSGGERALFNLSLRCAIYRLLAEGIEGDAPLPPLILDEPTVFLDSGHVSQLVDLVESMR
RLGVEQIVVVSHDDELVGAADDLVRVEKDPTTNRSSVERG
>gnl|CDD|235014 PRK02227, PRK02227, (5-formylfuran-3-yl)methyl phosphate synthase
MRLLVSVRNLEEALEALAGGADIIDVKNPKEGSLGANFPWVIREIVAAVPGRKPVSATIGDVPYKPGTIS
LAALGAAATGADYVKVGLYGGKTAEEAVEVMKAVVRAVKDLDPGKIVVAAGYADAHRVGSVSPLSLPAIA
ADAGFDGAMLDTAIKDGKSLFDHMDEEELAEFVAEARSHGLMSALAGSLKFEDIPALKRLGPDILGVRGA
VCGGGDRTGRIDPELVAELREALRAPAR
>gnl|CDD|179387 PRK02228, PRK02228, V-type ATP synthase subunit F; Provisional
MEIAVIGSPEFTTGFRLAGIRKVYEVPDDEKLDEAVEEVLEDDDVGILVMHDDDLEKLPRRLRRTLEESV
EPTVVTLGGGGGSGGLREKIKRAIGVDLWK
>gnl|CDD|179388 PRK02230, PRK02230, inorganic pyrophosphatase; Provisional
MKKIIEVTIEIPKGSNIKYEYDRKTNKIVVDRILRGDFVYPANYGFIKEALDWDGDELDVLVYSDQKFLP
GTVLNARIIGAMKMIDDGETDTKLIAVHDDDYRLDHINSLKDLPQHWLDEIEYFFSNYKNWKRKGITKVK
GFEDEKWALKEYKECVELMKKYGKLPKDEFIKKMMKEHPEKYQK
>gnl|CDD|167337 PRK02231, ppnK, NAD(+) kinase
MHKNLFHWLKERGYQVLVEKEIAEQLNLPENHLASLEEIGQRAQLAIVIGGDGNMLGRARVLAKYDIPLI
GINRGNLGFLTDIDPKNAYEQLEACLERGEFFVEERFLLEAKIERNGKIIATSNALNEVVIHPAKIAHMI
DFHVYIDDKFAFSQRSDGLIISTPTGSTAYSLSAGGPILTPNLNAIALVPMFPHTLSSRPLVIDGDSKIS
LRFAEYNTPQLEVSCDSQIALPFTPDDRVHVQKSPDKLRLLHLKNYNYYNVLSSKLGWLKKL
>gnl|CDD|235015 PRK02234, recU, Holliday junction-specific endonuclease; Reviewed
MINYPNKKSSQVQKTKKKKVTYANRGMSLEKDINETNDYYLSNGIAVIHKKPTPIQIVKVDYPKRSKAVI
KEAYFRQASTTDYNGVYKGKYIDFEAKETKNKTSFPLKNFHEHQIEHMKQVLKQGGICFVIIRFSTLDET
YLLPASKLIKFWERQKDGGRKSIPLEEIKKNGYEIPLGYPPRIDYLKIIDKLILG
>gnl|CDD|235016 PRK02237, PRK02237, YnfA family protein
MMLKSILLFVLAALAEIGGCYLPWLWLREGKSAWWLLPGALSLALFGWLLTLQPDAAFGRVYAAYGGVYV
AGSLLWLWVVDGVRPDRWDWIGAAICLVGMAVIMYAPRG
>gnl|CDD|179391 PRK02240, PRK02240, GTP cyclohydrolase IIa
MIQITLIQIDNYGPWTVTPNPRRESDLQALQSRLYADLAQQFGARDGYVFFTRFDNMIAVTNGIDLEDHA
RIQESIRNRYPVTVSMGIGTAETPYEAQKLATEALQEAGSAQDENRKEVLAGDDVANEDRTDGYVQIAHF
DINDITGTYTDIENAFDTFLEIEQAYLALMRELRKAHDALSFFVGGDNFMAPCPGLSEGDFLDAIEHVRE
EVGVELKVGIGRGKTAEDAGNLAKHALETIREGRVDGSVYTLKD
>gnl|CDD|179392 PRK02249, PRK02249, DNA primase regulatory subunit PriL
DRELLARYPFLSEARDYVETAGVSLDDLLASDAYGSAVERARERVERALTGETVKEPSDLDRPEVELLSY
PVARVLVSCVDDPYLTRRYARAEAKAAYDLLRAEEPDDDLRELARDLGIPARVEGDGFAVHVTDYLRLAA
RLKDPKWRLVNRPVVKGYVYVTREEFARLLREAIRERILDGLPLAVPEEIAEALLPLLEEIREELEELDL
ETEFGTVDPELFPPCMKALLSALQAGENLPHTARFAITSFLLNIGMSVDEIVELFRNAPDFDEEKTRYQV
EHIAGETGGTEYTPPSCETMRTYGLCVGKDDLCEKVKHPLSYYRRKLRDKDKEEKEDWREEEK
>gnl|CDD|179393 PRK02250, PRK02250, hypothetical protein; Provisional
AMSCPCGSTQTYSQCCEPIHLNHASAQTPEQLMRSRYSAHVLGLVDYVVETYHPSCNAEEQREGIAESIH
SDWLKLEVIKTEAGSTPNEGFVEFKAYFDEEGKRYCLEERSRFLKENGLWYYIDGTFPEEEPEQDPRLNQ
SVSSLKQGRNDPCICGSGKKFKKCCG
>gnl|CDD|179394 PRK02251, PRK02251, cell division protein CrgA
MPKSQVRKMADRQAPPTKRAEESIKGTKSNPRWFVPLFVALMIIGLIWLVVYYLSNGSLPIPALGAWNLV
IGFGLIMAGFGMTTQWK
>gnl|CDD|179395 PRK02253, PRK02253, deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
SLLSKEELRKLIRSGKFVAEHVVDLEDDQVQPNGVDLTLGEVEEQEGPGRIDFDNRKLPEREPLEFDDDG
WIRLEPGIYKVRYNEVVNIPEDHVGFAYPRSSLLRNGCTLETAVWDAGYEGRGEGLLVVHNPHGIRLERG
ARIAQLVFATLDHETEGYSGSYQGENL
>gnl|CDD|235018 PRK02256, PRK02256, putative aminopeptidase 1; Provisional
MEKKLTYKKKNAWEKYSEEEKEEIFAFAEDYKDFLSKCKTEREAVKEIIELAEEKGFINLEEIIGLKPGD
KVYAVNRGKSVALAVIGKEPLEEGLNIIGAHIDSPRLDLKPNPLYEDEGLALLKTHYYGGIKKYQWVAIP
LALHGVVVKKDGTKVEIVIGEDENDPVFTISDLLPHLAKDQMEKKASEAIEGEKLNILIGSIPLEDEEKE
KVKLNILKLLNEKYGITEEDFVSAELEVVPAGKARDVGLDRSLIGAYGQDDRVCAYTSLEALLELENPEK
TAVVLLVDKEEIGSEGNTGAQSRFFENFVAELLAKTEGNYSDLKLRRALANSKALSADVSAAFDPNYPSV
HEKQNAAYLGYGVVFTKYTGSRGKYGANDANAEFVAEVRNLFNKNNVVWQTAELGKVDQGGGGTIAKFLA
NYGMEVIDCGVALLSMHSPFEIASKADIYETYKAYKAFLEEA
>gnl|CDD|235019 PRK02259, PRK02259, aspartoacylase; Provisional
KINRVAIVGGTHGNEITGIYLVKKWQQQPNLINRKGLEVQTVIGNPEAIEAGRRYIDRDLNRSFRLDLLQ
NPDLSGYEQLRAKELVQQLGPKGNSPCDFIIDLHSTTANMGLSLILYGRRPFDLALAAYLQSRLPLPIYL
HEKDEDQTGFLVELWPCGLVIEVGPVPQGVLDAEIFEQTELLIESILDYLEKYNQGKLPLPNEQLVVYRH
LGSIDYPRDENGQIAAMIHPQLQGRDWQPLKPGDPLFLTFDGKTIFYEGDSTVYPVFINEAAYYEKGIAM
SLTKKEVI
>gnl|CDD|179399 PRK02260, PRK02260, S-ribosylhomocysteine lyase
MPLVESFTLDHTKVKAPYVRLAGTKDGPKGDVITKFDLRFCQPNKEAMPTAGIHTLEHLLAGFLRNHLDG
GVEIIDISPMGCRTGFYLILIGTPDEEDVADALKATLEDVLDDQEEVPGANEYQCGNYKDHSLEGAKEIA
RKILDQGISVNPNEELAL
>gnl|CDD|179400 PRK02261, PRK02261, methylaspartate mutase subunit S; Provisional
MKKKTVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSLYGHGEID
CRGLREKCIEAGLGDILLYVGGNLVVGKHDFEEVEKKFKEMGFDRVFPPGTDPEEAIDDLKKDLNQR
>gnl|CDD|179402 PRK02265, PRK02265, acetoacetate decarboxylase; Provisional
MKIEDVRSKAFAMPLTSPAYPPGPYRFVNREYLIITYRTDPDALRAVVPEPLEVDEPLVKYEFIRMPDST
GFGDYTESGQVIPVRYEGEPGGYTHAMYLDDHPPIAGGRELWGFPKKLASPKLEVDSDTLVGTLDYGSVR
VATGTMGYKHRELDLEEVLASLAKPNFLLKIIPHVDGTPRICELVRYYLTDITVKGAWTGPARLELFPHA
LAPVADLPVLEIVSASHIVADLTLGLGEVVHDYLAQ
>gnl|CDD|235021 PRK02268, PRK02268, hypothetical protein; Provisional
MMRYWIGVVSAEHVRRGVEGGFMQVCHGKAAPLRRMKPGDWIIYYSPKTTFGGKDKLQAFTAIGKVKDDE
PYQVEMAPGFIPWRRDVDYYPCAETPIRPLLDHLDFTEDRKNWGYQFRFGHFEISKHDFETIASAMTVDP
E
>gnl|CDD|167353 PRK02269, PRK02269, ribose-phosphate diphosphokinase
MSYSDLKLFALSSNKELAEKVAQEIGIELGKSSVRQFSDGEIQVNIEESIRGHHVFILQSTSSPVNDNLM
EILIMVDALKRASAESINVVMPYYGYARQDRKARSREPITSKLVANMLEVAGVDRLLTVDLHAAQIQGFF
DIPVDHLMGAPLIADYFDRRGLVGDDVVVVSPDHGGVTRARKLAQFLKTPIAIIDKRRSVDKMNTSEVMN
IIGNVKGKKCILIDDMIDTAGTICHAADALAEAGATEVYASCTHPVLSGPALDNIQKSAIEKLVVLDTIY
LPEERLIDKIEQISIADLLGEAIIRIHEKRPLSPLFEMGK
>gnl|CDD|235022 PRK02271, PRK02271, methylenetetrahydromethanopterin reductase; Provisional
MKFGIEFVPNHPVKKIAYLAKLAEDNGFDYAWITDHYNNRDVYMTLAAIAAATDTIKLGPGVTNPYTRHP
AITASAIATLDEISGGRAVLGIGPGDKATLDALGIEWEKPLRTVKEAIEVIRKLWAGERVEHDGTFKAAG
AKLNVKPVQGEIPIYMGAQGPKMLELAGEIADGVLINASNPKDFEWAVPLIKKGAEEAGKSRGEFDVAAY
ASVSVDKDEDKAREAAKPVVAFIAAGSPPPVLERHGIDLEAVEKIGEALSKGDFGEAFGAVTDEMIDAFS
IAGTPEDVVEKIEALLEMGVTQIVAGSPIGPDKEKAIKLIGKAII
>gnl|CDD|235023 PRK02277, PRK02277, orotate phosphoribosyltransferase-like protein; Provisional
MKNIEELIEKAAELKNKGLSTGEIADELNVSRETATWLLTRAKKLEKAPAPKDIHIDWSSIGSSSSRLRY
IASAMADMLEKEDEEVDVVVGIAKSGVPLATLVADELGKDLAIYHPKKWDHGEGEKKTGSFSRNFASVEG
KRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDKSGIDEIDGVPVYSLIRVVRVD
>gnl|CDD|235024 PRK02287, PRK02287, DUF367 family protein
MMKLYVYHANQDDPKKCTARKLVRFGLARLVRSIRKIPRGSIVLNPFAEKALSPADRDIVEKRGIVALDC
SWNEAERVFFKLLRGHHRRLPFLVAANPVNYGKPFKLSSVEALAAALYILGFKEEAEKILSKFKWGHTFL
ELNKEPLEAYARAKDSEEIVEIQKEYLGKIL
>gnl|CDD|179406 PRK02289, PRK02289, 4-oxalocrotonate tautomerase; Provisional
MPFVRIDLFEGRSQEQKNALAREVTEVVSRIAKAPKEAIHVFINDMPEGTYYPQGEMKTK
>gnl|CDD|235025 PRK02290, PRK02290, 3-dehydroquinate synthase II family protein
MKFVWIKARPDWEERKEVVTTALESGVDGVVVDEEDVERVRELGRIKVAADDPDADAVVISGSAGEDGAY
VEIRDKEDEEFAAELAKEVDYVIVEGRDWTIIPLENLIADLGQSGKIIAGVADAEEAKLALEILEKGVDG
VLLDPDDPNEIKAIVALIEEAREKLELVPATVTRVEPVGMGDRVCVDTCSLMEEGEGMLVGSSSRGMFLV
HAETEENPYVASRPFRVNAGAVHAYVRVPGDKTRYLSELRSGDEVLVVDADGNTREAIVGRVKIEKRPLL
LIEAEYGGKRIRTILQNAETIRLVTPDGKPVSVVDLKPGDEVLGYLEEAARHFGMAIEETIIEK
>gnl|CDD|235026 PRK02292, PRK02292, V-type ATP synthase subunit E; Provisional
MSLETVVEDIRDEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREIEQLREQELSSAKLEA
KRERLNARKEVLEDVRNQVEDEIASLDGDKREELTKSLLDAADADGVRVYSRKDDEDLVKSLLSDYDGLE
YAGNIDCLGGVVVESEDGRVRVNNTFDSILEDVWEDNLKEISDRLFGE
>gnl|CDD|235027 PRK02301, PRK02301, deoxyhypusine synthase
MDTPTREKFCHDPVKQAEVRPGMTVGELVREYGGAGFGAGRLAEAVDIYEEMLADDDVTKFFGLAGAMVP
AGMRGIVSDLIRDGHIDVLVTTGANLTHDVIEAIGGHHHHGTAHAHDEELRDEGIDRIYDVYLPQEHFAD
FEEFLQDVFPGLEEEGTVSIRDLLTEIGRDLDDDSGILAAAYECDVPVYCPAIQDSVLGLQAWLYSQTNK
FTVDAFADMTELMDICYEAERAGALLVGGGVPKNYILQSMLVTPKAFDYAVQLTMDRPETGGLSGATLDE
ARSWGKLGEDAKNVTVYGDATITLPLLVAAVRERIE
>gnl|CDD|179410 PRK02302, PRK02302, hypothetical protein; Provisional
MFEKQERIGLIVYLYYNRDARKLSKYGDIVYHSKRSRYLVLYVNKEDVEQKLEELSKLKFVKKVRPSAID
EIDQNFVGNLYRDETNVHQ
>gnl|CDD|235028 PRK02304, PRK02304, adenine phosphoribosyltransferase; Provisional
MMLEDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALA
YKLGIGFVPVRKPGKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERL
GAEVVGAAFVIELPDLGGREKLEGYPVKSLVKFDG
>gnl|CDD|235029 PRK02308, uvsE, putative UV damage endonuclease; Provisional
MLMRLGYVCMTVTLNASPSRTMTLKQFQKLSDREREEKLEEIALSNLENLLRILKYNIAHGIGLFRLSSS
LIPLATHPELEGWDYIEPFKEELREIGEFIKEHNIRLSFHPDQFVVLNSPKPEVVENSIKDLEYHAKLLD
LMGIDDSSKINIHVGGAYGDKEKALERFIENIKKLPESIKKRLTLENDDKTYTVEELLYICEKLGIPVVF
DYHHHMCNPDGESLEEALELAFETWEHEDLPPKVHISSPREGKKPRAHADYIDVDDFPSFLHEAIVPDID
IMIEAKQKELALFKLMRELSEIR
>gnl|CDD|235030 PRK02315, PRK02315, adaptor protein MecA
MEIERINENTIKVFITYDDLEERGFEREDLLYNREKIEEFFYSMMDEVDEEDDFADEGPLWFQVTPNEKG
LEVFVTKSKLDLPLNFEDLIDLPSDEDIEDLFPEDFFKLLEQSLEDKDDLDATAKQEKEEKEAEDEVQLT
YVLKFDDFEDVISLAKTLKVEDLASELYKYEGRYYLTVLFDDENYPEEEIDDMLAILLEYANESDLTIHR
LQEYGKVIMSHDALEQIRKYFPG
>gnl|CDD|235031 PRK02318, PRK02318, mannitol-1-phosphate 5-dehydrogenase; Provisional
MKAVHFGAGNIGRGFIGKLLADNGFEVTFVDVNQELIDALNKRKSYQVIVVGENEQVETVSNVSAINSAD
EEAVIEAIAEADLVTTAVGPNILPFIAPLIAKGLKKRKAQGNTKPLNIIACENMIRGTSFLKKHVLKALS
EDEKAWLEEHVGFVDSAVDRIVPAQKNEDPLDVTVEPFSEWIVDKTQFKGALPKIKGMEYVDNLMPFIER
KLFTVNTGHATTAYLGYLKGYKTIREAILDPSIRAVVKGALEESGAVLIKKYGFDKEEHAAYIEKILGRF
ENPYLSDDVERVGRQPLRKLGANDRLIKPLLGLKEYGLPHSNLLKGIAAALHFDDENDPQAVELQALIAE
KGLEAALAEITGLDADSELVEEIVKAYNALK
>gnl|CDD|235032 PRK02362, PRK02362, ATP-dependent DNA helicase
MKIAELPLPEGVIEFYEAEGIEELYPPQAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIARGGKA
LYIVPLRALASEKFEEFERFEELGVRVGISTGDYDSRDEWLGDNDIIVATSEKVDSLLRNGAPWLDDITC
VVVDEVHLIDSANRGPTLEVTLAKLRRLNPDLQVVALSATIGNADELADWLDAELVDSEWRPIDLREGVF
YGGAIHFDDSQREVEVPSKDDTLNLVLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELA
ELAEEIREVSDTETSKDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRV
IIRDYRRYDGGAGMQPIPVLEYHQMAGRAGRPGLDPYGEAVLLAKSYDELDELFERYIWADPEDVRSKLA
TEPALRTHVLSTIASGFARTRDGLLEFLEATFYATQTDDTGRLERVVDDVLDFLERNGMIEEDGETLEAT
ELGHLVSRLYIDPLSAAEIIDGLEAAKKPTDLGLLHLVCSTPDMYELYLRSGDYEWLNEYLYEHEDELLG
DVPSEFEDDEFEDFLSAVKTALLLEDWIDEVDEERITERYGVGPGDIRGKVETAEWLLHAAERLASELDL
DLARAARELEKRVEYGVREELLDLVGLRGVGRVRARRLYNAGIESRADLRAADKSVVLAILGEKIAENIL
EQAGRRDPSMGASSEDDDEESDEKGEDDGQSTLGDFG
>gnl|CDD|179417 PRK02382, PRK02382, dihydroorotase; Provisional
MRDALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREPGYTH
KETWYTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTGNWDPLESLWERG
VFALGEIFMADSTGGMGIDEELFEEALAEAARLGVLATVHAEDEDLFDELAKLLKGDADADAWSAYRPAA
AEAAAVERALEVASETGARIHIAHISTPEGVDAARREGITCEVTPHHLFLSRRDWERLGTFGKMNPPLRS
EKRREALWERLNDGTIDVVASDHAPHTREEKDADIWDAPSGVPGVETMLPLLLAAVRKNRLPLERVRDVT
AANPARIFGLDGKGRIAEGYDADLVLVDPDAAREIRGDDLHSKAGWTPFEGMEGVFPELTMVRGTVVWDG
DDINAKRGRGEFLRGRGYERDED
>gnl|CDD|179418 PRK02391, PRK02391, heat shock protein HtpX; Provisional
RMRWKRDRGLTGRMFLTMFLLFALYLVFVAVLIALGVSLVLIVVIAGGFLLAQYFFSDKLALWSMGARIV
SEDEYPELHAMVERLCALADLPKPRVAVADSDVPNAFATGRSPKNAVVCVTTGLMRRLDPDELEAVLAHE
LSHVKNRDVAVMTIASFLSTIAFLIVRWGFYFGGFGGRGGGGGGGGILVVILVSLVVWAISFLLIRALSR
YREFAADRGAAIITGRPSALASALMKISGRMDRVPTEDLREAEGMNAFFIIPALSGGSLGRLFSTHPPLE
KRIAQLEKLERELGTA
>gnl|CDD|235034 PRK02395, PRK02395, hypothetical protein; Provisional
MQALVLVGHGSHLNPDSALPTYAHAETIRARGLFDEVREGFWKEEPSLRQVLRTVESDEVYVVPLFISEG
YFTEQVIPRELGLGHDGPVADRGTLRALDGKTVHYTGPVGTHPAMADVIAARARSVTGDPDVGEDTALAV
VGHGTERNENSAKAIYYHADRLRERGRFAEVEALFLDEEPEVDDWPDLFEADDVVVVPLFIADGFHTQED
IPEDMGLTDDYRTGYDVPTAVDGHRIWYAGAVGTEPLMADVILERAADAGADVGRAGDLVREHTEAWAA
>gnl|CDD|179420 PRK02399, PRK02399, hypothetical protein; Provisional
AMMKRIYIAGTLDTKGEELAYVKDLIEAAGLEVVTVDVSGLGEPPFEPDISAEEVAEAAGDGIEAVFCGG
DRGSAMAAMAEGAAAFVRELYERGDVAGVIGLGGSGGTALATPAMRALPIGVPKLMVSTMASGDVSPYVG
ASDIAMMYSVTDIAGLNRISRQVLSNAAGAIAGMVKFEQPAPSDDKPLIGLTMFGVTTPCVQAAREELEA
RGYEVLVFHATGTGGRAMEKLIDSGLIAGVLDLTTTEVCDELFGGVLAAGPDRLEAAARTGIPQVVSPGA
LDMVNFGAPDTVPEKFRGRLLYKHNPQVTLMRTTPEENRQIGRWIAEKLNRAKGPVAFLIPLGGVSALDR
PGQPFHDPEADAAFFDALEETVTETRRLIEVPAHINDPEFAEAAVEAFEELMARGR
>gnl|CDD|235035 PRK02406, PRK02406, DNA polymerase IV; Validated
MDCFYAAVEMRDNPELRGKPVAVGGSPGRRGVISTCNYEARKFGVRSAMPTAQALKLCPDLIFVPGRFDV
YKEVSRQIREIFRRYTDLIEPLSLDEAYLDVTDNKLCIGSATLIAQEIRQDIFEELGLTASAGVAPNKFL
AKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHALGIYTCADLQKYDLAELIRHFGKF
GRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRLERAKPDKRIKTVGV
KLKFADFQQTTKEHTADPLDKADLIELLAQALLRRLGGRGVRLLGVGVTLLEPQLERQLLLDL
>gnl|CDD|235036 PRK02412, aroD, type I 3-dehydroquinate dehydratase
MKTVTVKNLVIGEGAPKIIVPIMGKTLEEVLAEALAISKYDADIIEWRADFLEKISDVESVLAAAPAIRE
KFAGKPLLFTFRTAKEGGEIALSDEEYLALIKAVIKSGLPDYIDVELFSGKDVVKEMVAFAHEHGVKVVL
SYHDFEKTPPKEEIVERLRKMESLGADIVKIAVMPQSEQDVLTLLNATREMKELYADQPLITMSMGKLGR
ISRLAGEVFGSSWTFASLDKASAPGQISVEDLRRILEILHKAI
>gnl|CDD|235037 PRK02427, PRK02427, 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
MMMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEIEDDEV
VVEGVGGGGLKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGR
DEGYLPLTIRGGKKGGPIEYDGPVSSQFVKSLLLLAPLFAEGDTETTVIEPLPSRPHTEITLRMLRAFGV
EVENVEGWGYRRIVIKGGQRLRGQDITVPGDPSSAAFFLAAAAITGGSEVTITNVGLNSTQGGKAIIDVL
EKMGADIEIENEREGGEPVGDIRVRSSELKGIDIDIPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKET
DRIAAMATELRKLGAEVEETEDGLIITGGPLAGVVDSYGDHRIAMAFAIAGLAAEGPVTIDDPECVAKSF
PDFFEDLASLGANIE
>gnl|CDD|235038 PRK02436, xerD, site-specific tyrosine recombinase XerD
MKNYIEPFLASKQLSENSQKSYRYDLQQFLQLVGERVSQEKLKLYQQSLANLKPSAQKRKISAVNQFLYF
LYQKGELDSFFKLKETAKLPESKKEKLEILDLSSFYQETPFPEGQLIALLILELGLTPSEIAGLKVADID
LDFQVLTIEKAGGKRVLTLPEALLPFLEAILNQTYLFEHKGKPYSRQWFFNQLKSFVKSIGYPGLSAQKL
REQFILKQKEAGKSIYELARLLGLKSPVTLEKYYK
>gnl|CDD|235039 PRK02458, PRK02458, ribose-phosphate pyrophosphokinase; Provisional
MTERYADKQIKLFSLNSNLEIAEKIAQAAGVPLGKLSSRQFSDGEIMINIEESVRGDDIYIIQSTSFPVN
DHLWELLIMIDACKRASANTVNVVLPYFGYARQDRIAKPREPITAKLVANMLVKAGVDRVLTLDLHAVQV
QGFFDIPVDNLFTVPLFAKHYCKKGLSGSDVVVVSPKNSGIKRARSLAEYLDAPIAIIDYAQDDSEREEG
YIIGDVAGKKAILIDDILNTGKTFAEAAKIVEREGATEIYAVASHGLFAGGAAEVLENAPIKEILVTDSV
ATKERVPKNVTYLSASELIADAIIRIHERKPLSPLFAYNKKGK
>gnl|CDD|235040 PRK02463, PRK02463, OxaA-like protein precursor; Provisional
MKKTLKRILFSGLALSMLLTLTGCVGRDKHGNPTGFIWNFLGAPMSYFIDYFANNLGLGFGLAIIIVTII
VRLIILPLGLYQSWKATYQSEKMAYLKPVFEPINERLKNATTQEEKMAAQTELMAAQRENGISMLGGIGC
LPLLIQMPFFSALYFAAQYTKGVSTSTFLGIDLGSPSLVLTAIIGVLYFFQSWLSMMGVPEEQREQMKAM
MYMMPIMMVVFSFSSPAGVGLYWLVGGFFSIIQQLITTYILKPRLRKQIAEEFAKNPPKAYKSPSGRKDV
TPSQNQAIASLPKKKKKNRNAGKQRKR
>gnl|CDD|179427 PRK02471, PRK02471, bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB
MMLLKLIQKLHLRPLLLQANFGLEKESLRVDSDGKLALTPHPKAFGSRSFHPYIQTDFSESQLELITPVA
DSIEEVYRFLGALHDVASRSLDEDEYLWPLSMPPILPDEEEIPIAQLDNREDVQYREYLAKKYGKKKQMI
SGIHYNFSLGEALIQRLFEEQSEQQDYKDFKNDLYLKVARNFLRYRWLLTYLFGASPVAEADFFKQNKEY
LNQDVRSLRNSKYGYVNKEDVYVSYNSLEDYVSSLENAVESGQLISEKEFYSPVRLRGAKQDRSLLEKGI
TYLEFRLFDLNPFEPYGISQETLDFVHLFLLYLLWLDEPEDTDQWVELADENNNLIALEHPLEALALAAE
AELILDAMEDLVQHLGLPDEYQDLIKQLKEQLTDPEKTLSGRLLKQIKQESYVAFGLEQAKQYKEYAWER
PYALKGYEDMELSTQILLFDAIQRGIQVEILDEQDQFLKLQKGDHVEYVKNGNMTSKDNYISPLIMENKV
VTKKILAEAGFPVPAGDEFTSLEEALADYSLFADKAIVVKPKSTNFGLGISIFKEPASLEDYEKALEIAF
REDSSVLVEEFIVGTEYRFFVLDGKVEAVLLRVPANVVGDGIHTVRELVAQKNQDPLRGTDHRTPLEKIQ
LGEIERLMLKQQGLTPDSIPKKGEIVYLRENSNISTGGDSIDMTDDMDDSYKQIAVKAAKALGAKICGVD
LIIPDLTQPASPEHPNYGIIELNFNPAMYMHCFPYKGKGRRITPKILDKLFP
>gnl|CDD|167380 PRK02478, PRK02478, Maf-like protein; Reviewed
MTVKLILASKSPFRRALLENAGLEFSAAAADIDERAVEAPLEESGATPEDVALVLAEAKAIDVSERFPGA
LVIGCDQTMSLGDEVFHKPKDMEEARRHLQKLSGKTHQLNSAVVLVRDGKVLWRHVSIAHMTMRDLDAGF
IGRHLARVGEKALSSVGAYQLEGEGIQLFEKIEGDYFTILGLPLLPLLAKLRELGAIDG
>gnl|CDD|179430 PRK02487, PRK02487, heme-degrading domain-containing protein
TMDLAQDLAQIAAQEQALVFPHFDNDDAWQLGSLLVELARERGLPIAIDITLNGQPLFYAALPGTTPDNT
DWIRRKRNVVARFGRSSYAVGLRLQRAGTSLEEKYGLSDADYAAHGGGFPIRVKGAGVIGAVTVSGLPQR
EDHNLVVEALAEHLGQDALALAL
>gnl|CDD|179431 PRK02491, PRK02491, putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed
MTEKIYEYKDEQNWFIGKMSGFNLISGWGVKHTDIKKIDDLLDGIAATLDEENPFGYDVTVVRYQSPLRL
ISFIVDMINQETQRNLKVTQHAGAILLTENDKLLAVHLPKEGVSTADFFGTSKQGFGDTILIATRNEGKT
KEFRKLFGKLGYKVENLNDYPDLPEVAETGMTFEENARLKAETISRLTGKMVLADDSGLKVDALGGLPGV
WSARFSGPDATDAENNAKLLHELAMVFDLKDRSAQFHTTLVVAAPNKDSLVVEADWPGYIATEPKGENGF
GYDPLFLVGETGRHAAELTAEEKNQLSHRGQAVKKLMEVFPAWQAKQS
>gnl|CDD|235043 PRK02492, PRK02492, deoxyhypusine synthase
MMSNSNTKAELLQEPVEHIDIKSFDAVPIIDAMGKMAFQSRDLARAADIYDMMLQDKECAVILTLAGSLS
SAGCMQVYIDLVRNNMVDAIVATGANIVDQDFFEALGFKHYQGSPFVDDAVLRDLYIDRIYDTYIDEEEL
QVCDHTIAEIANSLEPRPYSSREFIWEMGKYLEENAKKENSLVQKAYEKGVPIFCPAFSDSSAGFGLVHH
QVKNPDPHVTIDSVKDFRELTDIKIAAGTTGLFMIGGGVPKNFAQDTVVAAEVLGYEVSMHKYAVQITVA
DVRDGALSSSTLKEASSWGKVDTAYEQMVFAEATSALPLIASYAYHKGNWEGREARRFNKLFDKEQV
>gnl|CDD|179433 PRK02496, adk, adenylate kinase; Provisional
MTRLIFLGPPGAGKGTQAVVLAEHLHIPHISTGDILRQAIKEQTPLGIKAQGYMDKGELVPDQLVLDLVQ
ERLQQPDAANGWILDGFPRKVTQAAFLDELLQEIGQSGERVVNLDVPDDVVVERLLARGRKDDTEEVIRR
RLEVYREQTAPLIDYYRDRQKLLTIDGNQSVEAVTTELKAALAP
>gnl|CDD|235044 PRK02504, PRK02504, NAD(P)H-quinone oxidoreductase subunit N
MPSELLASQLNAGAILPEGIVILTLLGVLLVDLIGGRTASRWLPYLAIAGLGAALVALALQWDNPNPISF
LGSFNADNLSIAFRAIIALSTLVTLLMSWRYVEQSGTPLGEFAAILLTATLGGMFLSGATELVMIFISLE
TLSIASYLLTGYMKRDPRSNEAALKYLLIGAASSAIFLYGSSLLYGLSGGSTQLSAIALALITSPSLGLA
LALVFVIAGIAFKISAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAIRLLVTAFPSFDEQWKLLFT
ALAILSMVLGNVVALAQTSMKRMLAYSSIGQAGFVMIGLVAGTEAGYASMVFYLLAYLFMNLGAFACVIL
FSLRTGTDQISDYAGLYQKDPLLTLGLSLCLLSLGGIPPLAGFFGKIYLFWAGWQAGLYLLVLVGLVTSV
ISIYYYIRVIKMMVVKEPQEMSDVVKNYPEINWNLPGMRPLRVGLVLCVIATALAGILSNPLFTLANTSV
AGTPFLQQAIALTNQSSAGTLSP
>gnl|CDD|235045 PRK02506, PRK02506, dihydroorotate dehydrogenase 1A; Reviewed
STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMG
LPNLGFDYYLDYVLELQKKGPNKPHFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVPGKPQIAY
DFETTEQILEEVFTYFTKPLGVKLPPYFDIVHFDQAAAIFNKFPLAFVNCINSIGNGLVIDPEDETVVIK
PKNGFGGIGGDYIKPTALANVRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAV
FERLTKELKAIMAEKGYQSLEDFRGKLKYL
>gnl|CDD|235046 PRK02507, PRK02507, proton extrusion protein PcxA; Provisional
MKLKSFLMRANQWLLKTPERALERAYEAALKIKAIEDEHFGGRKISPENASYGKSVQSYFQSELRRELKI
IRMRLAEFKASRLFLNLSELAKAGEEQITETIILEKLQFIDSVISRYRSKSDQESPPLAASSQIETSTSS
PSTSNPVNDPSSKSESISQKTGVLPRSILRTFDRIRRELDPEAEEEVVQGFRRSRDRTLISIRFLLLLII
VPLLTQQLSKTFIVSPLVDHFFPALPFEIFINPELEEEALEELRRFKEELEFEALLGLAPPLSPEEIEEK
LKEKAEELAEEARYESLNAIKNVFADLFSLIAFAVVLIFSREEIEVLKSFLDEIVYGLSDSAKAFIIILF
TDIFVGFHSPHGWEVILEGIARHFGLPENRNFIFLFIATFPVILDTIFKYWIFRYLNRISPSAVATYRNM
NE
>gnl|CDD|235047 PRK02509, PRK02509, hypothetical protein; Provisional
WKWLFRLLLVLLGIWLGLELLSRLIAEILWFQEVGYLSVFLKRLAWQLLLWILVSGVSAGFLFGNLRLAQ
RLKWHQSPKIESVRREEVSLGPPLPPTPESRSLGLRWLLPLVVGLGLLLGLMLLYYGQVALQYWTPDFTL
PNVSPPLPSPFRLEWLWNLLTQILSQLWKLGLILLLAILILIRPKFLLRGIAIILSLAFGLILSGNWARV
LQYFHSTPFNETDPLFGRDISFYIFQLPLWELLEFWLMGLFLYGFIAVTLTYLLSADSLSQGKFPGFSRQ
QLRHLYGLGGALMLTLALSHWLARYELLYSTRGVVYGAGYTDVHVQLPVYTILSILAGIIAFWLLWRAIF
GSLKQRKSRRFPFLPYPLILYLGILLIGWLLPEVVQSLIVQPNELARERPYIQRSIALTRAAFDLDKIEV
RTFDPQGNLTAADLAANRLTIRNIRLWDTRPLLETNRQLQQIRLYYRFPDADIDRYTLKTENDDNRSIST
EKQQVLIAARELDYSAVPQQAQTWVNEHLVYTHGYGFTLSPVNTVAPGGLPEYFVKDIGTNTNEGALQTS
SEAIRASIPIGNPRIYYGELTNTYVMTPTRVQELDYPSGQDNVYNTYDGKGGIAIGSWWRRLLFALYLRD
WQMLFTQNFTPETRVLFRRNINQRIRAIAPFLRFDSDPYLVTADVQSEESPANPSTLYWIIDAYTTSDRY
PYSDPGERPFNYIRNSVKVVIDAYNGDVQFYVADPNDPLIQTWSKIFPQLFKPLSAMPVSLRSHIRYPVD
LFKAQSERLLTYHMTDPQVFYNREDQWRIPQEIYGEEQQPVEPYYLITSLPTADTEEFILLLPYTPTSRN
NLIAWLAARSDGENYGKLLLYQFPKQRLIYGPEQIEALINQDPVISQQISLWNRQGSRAIQGNLLVIPIE
QSLLYVEPLYLEAEQNSLPTLARVIVAYENRIVMAPTLEEALQAIFQPETTPAPAIIRPVETT
>gnl|CDD|235048 PRK02515, psbU, photosystem II complex extrinsic protein PsbU
MKRLLSLLTGFSLLLGLLGWLGTPQSAQAAELPLLAVPQNVADAKLGEFGEKIDLNNSSVRAFRQFPGMY
PTLAGKIVKNAPYDSVEDVLNLPGLSERQKELLEANLDNFTVTEPEIALNEGDDRINNGQYR
>gnl|CDD|134722 PRK02529, petN, cytochrome b6-f complex subunit PetN; Provisional
MLFTLGWASLAAIFTFSIAMVVWGRNGDGSIDF
>gnl|CDD|179440 PRK02539, PRK02539, DUF896 family protein
MDPKKIARINELAKKKKTEGLTGEEKVEQAKLREEYIEGYRRSVRHHIEGIKIVDEEGNDVTPEKLRQVQ
REKGLHGRSLDDPNS
>gnl|CDD|179441 PRK02542, PRK02542, photosystem I assembly protein Ycf4; Provisional
MAAPATTSSDLVLEQEVLGSRRLSNYLWASMVTIGGIGFLLAGLSSYLGRNLLPVGDPSTLIFIPQGLAM
GFYGVAGTLLALYLWLVIAIDVGGGYNEFDKETGKVTIFRWGFPGKNRRIEVEYPLEDIQAVKVEIREGL
NPRRRLYLRLKGRRDIPLTRVGQPLPLAELENQGAELARFLGVPLEGL
>gnl|CDD|235050 PRK02546, PRK02546, NAD(P)H-quinone oxidoreductase subunit 4; Provisional
MNLANFPWLTTIILFPIVAALLIPFIPDKGDGKTVRWYALIVGLIDFLITVYAFYTGYDFSNPGLQLVES
YSWLPQLGLTWSVGADGLSMPLILLTGFITTLAVLAAWPVTFKPKLFYFLMLAMYGGQIAVFAVQDMLLF
FLAWELELIPVYLLLAIWGGKKRQYAATKFILYTAGSSLFILLAALAMAFYGDTPTFDMTALAAKDFGLG
FQLLCYAGLLIAYGVKLPIVPLHTWLPDAHGEATAPVHMLLAGILLKMGGYALLRMNAGMLPDAHAQFAP
LLIVLGVVNIIYAALTSFAQRNLKRKIAYSSISHMGFVLIGIGSFTDLGTSGAMLQMISHGLIGASLFFL
VGATYDRTHTLMLDEMGGVGQKMRKMFAMWTACSLASLALPGMSGFVAELMVFVGFATSDAYTLPFRVVV
VFLAAVGVILTPIYLLSMLREIFFGPENKELVSHEKLVDAEPREVFIIACLLVPIIGIGLYPKLVTQSYD
ATTNQLVARDRDSVPSLAQPTQSLVPAILQAPTIG
>gnl|CDD|179443 PRK02551, PRK02551, flavoprotein NrdI; Provisional
MKTITLVYISLSGNTRSFVKRLSDYLATQHKDIEVNPINIKDLIHETTDFFPETEPFVAFLPTYLEGGNG
IDNGDVEILTTPLGDFIAYHDNAKRCLGIIGSGNRNFNNQYCLTAKQYAKRFGFPMLADFELRGTPSDIE
RIAAIIAELYAAEK
>gnl|CDD|167396 PRK02553, psbK, photosystem II reaction center protein K; Provisional
METLLLLAKLPEAYQAFDPLVDVLPLIPLFFLLLAFVWQAAVGFK
>gnl|CDD|179444 PRK02557, psbE, cytochrome b559 subunit alpha; Provisional
MAGSTGERPFFDIITSIRYWVIHAITIPALFIAGWLFVSTGLAYDAFGTPRPDEYFTQSRSKAPIVSDRY
EAKQQLDEFLK
>gnl|CDD|235051 PRK02561, psbF, cytochrome b559 subunit beta; Provisional
MAPNNANQPRSYPIFTVRWLAVHALGVPTVFFLGAIAAMQFIQR
>gnl|CDD|179446 PRK02565, PRK02565, photosystem II reaction center protein J; Provisional
MWTEGRIPLWLVATVAGMGVIFVVGLFFYGSYAGLGSSL
>gnl|CDD|235052 PRK02597, rpoC2, DNA-directed RNA polymerase subunit beta'; Provisional
PIFRNRVVDKKALKNLIAWAFKNYGTARTAQMADNLKDLGFRYATQAGVSISVDDLKVPPAKRDLLEQAE
EEITATEERYRRGEITEVERFQKVIDTWNETNERLKDEVVKNFRQNDPLNSVYMMAFSGARGNMSQVRQL
VGMRGLMANPQGEIIDLPIKTNFREGLTVTEYVISSYGARKGLVDTALRTADSGYLTRRLVDVSQDVIVR
EEDCGTTRGIVVEAMDDGDRVLIPLGDRLLGRVLAEDVVDPEGEVIAERNTAIDPDLAKKIEKAGVEEVM
VRSPLTCEAARSVCRKCYGWSLAHNHLVDLGEAVGIIAAQSIGEPGTQLTMRTFHTGGVFTGEVARQVRS
PFAGTVEFGKKLRTRPYRTRHGVEALQAEVDFDLVLKPSGKGKPQKIEITQGSLLFVDDGQTVEADQLLA
EVAAGAVKKSTEKATKDVICDLAGEVRFADLIPEEKTDRQGNTTRKAQRGGLLWVLSGDVYNLPPGAEPV
VSNGDRVEEGDVLAETKLVSEHGGVVRLRESSGDSREVEIITASVLLDQAKVLEESTHGREQYNLETKDG
QRFRLNATPGTKVQNGEVVAELIDDRYRTKTGGLVKYAGLEVKKAGSAKNGYEVSKGGTLLWIPEETHEV
NKDISLLMVEDGQYVEAGTEVVKDIFCQTSGVVEVTQKNDILREIIIKPGELHLCDDPEALERFTGDGQL
VNPGEEVLPGVVTDELRYVEWVETPEGPGLLLRPVEEFTIPDEPQVPSQGSVKQEKGRSIGLRAVQRLPY
KDGERVKSVEGVELLRTQLVLEIFDTTPQLTADIELIPDEKDKEIQRLQLVILESLLVRRDTASDSSHGS
THTELLVKDGQQIKPGDVVARTQILCKEAGEVRGIRVGGEAVRRLLVERDEDTITIPLSGKPTVKVGDLV
VAGDELAPGVPAPESGEVEAVSGGSVTLRLGRPYRVSPGAVLHVRDGDLVQRGDNLALLVFERAKTGDII
QGLPRIEELLEARKPKESCILAKKPGTVQIKYGDDESVDVKVIESDGTITEYPILPGQNVMVSDGQQVDA
GEPLTDGPINPHELLEIFFEDLRDRKGLYEAALEALQKLQRFLVNEVQNVYQSQGVDISDKHIEVIVRQM
TSKVRIDDGGDTTMLPGELIELRQVEQVNEAMAITGGAPAEYTPVLLGITKASLNTDSFISAASFQETTR
VLTEAAIEGKSDWLRGLKENVIIGRLIPAGTGFSGFEEELSAEAGPHPDILAEDPAGYRRMQNLRPDYTV
DMPARPYASSLDDPSDEDLEATRSRHGIDPSSSNFAAFARPDADDELLIDDQLPDPAALEGLQEEGLLSD
E
>gnl|CDD|179448 PRK02603, PRK02603, photosystem I assembly protein Ycf3; Provisional
MPRTQRNDNFIDKSFTVMADLILKILPINKKAKEAFVYYRDGMSAQADGEYAEALENYEEALKLEEDPND
RSYILYNMGIIYASNGEHDKALEYYHQALELNPKQPSALNNIAVIYHKRGEKAEEAGDQDEAEALFDKAA
EYWKQAIRLAPNNYIEAQNWLKTTGRSNIDVY
>gnl|CDD|235053 PRK02610, PRK02610, histidinol-phosphate transaminase
MLPFLRSDLAQLKAYHPHPSGDADDAVIQLDRLDTNEFPYDLPPDLKQKLAWLYQQGIESNRYPDGGHEA
LKQAIAEYVNESAAGSSQITPANISVGNGSDELIRSLLIATCLGGEGSILVAEPTFSMYGILAQTLGIPV
VRVGRDPETFEIDLAAAQSAIEQTQNPPVRVVFVVHPNSPTGNPLTAAELEWLRSLPEDILVVIDEAYFE
FSQTTLVGELAQHPNWVILRTFSKAFRLAAHRVGYAIGHPELIAVLEKVRLPYNLPSFSQLAAQLALEHR
QELLAAIPEILQERDRLYQALQELPQLRVWPSAANFLYLRLSQDAALAALHQALKAQGTLVRHTGGGLRI
TIGTPEENQRTLERLQAALTQLEP
>gnl|CDD|235054 PRK02615, PRK02615, thiamine phosphate synthase
VTMDEDLRIARILDANLDRAREGLRVLEEWCRFGLENEDLVERCKDLRQELGRWHTEELRQARDTPTDPG
TGLSHPQEEQRSTLEQVVSANAARVQEALRVLEEYGKLYDPELAAAAKQIRYELYTLESELLNASLGKKR
RQRLKDARLYLITSPSENLLEVVEAALKGGVTLVQYRDKTADDRQRLEEAKKLKELCHRYGALFIVNDRV
DIALAVDADGVHLGQEDLPLAVARQLLGPEKIIGRSTTNPEEMAKAIAEGADYIGVGPVFPTPTKPGKAP
AGLEYLKYAAKEAPIPWFAIGGIDKSNIPEVLQAGAKRVAVVRAIMGAEDPKQATQELLKQLSRENA
>gnl|CDD|179451 PRK02624, psbH, photosystem II reaction center protein PsbH
MAQRTRLGDLLKPLNSEYGKVVPGWGTTPVMAVFMVLFLVFLLIILQIYNQSLLLQGFSVDWNG
>gnl|CDD|235055 PRK02625, rpoC1, DNA-directed RNA polymerase subunit gamma; Provisional
SNLRTENRFDYVKIGLASPERIRQWGQRTLPNGQVVGEVTKPETINYRTLKPEMDGLFCEKIFGPSKDWE
CHCGKYKRVRHRGIVCERCGVEVTESRVRRHRMGFIKLAAPVTHVWYLKGIPSYVAILLDMPLRDVEQIV
YFNCYVVLDPGNHKNLKYKQLLTEDQWLEIEDQIYAEDSELEGEEVVGIGAEALKRLLEDLNLEEEAEQL
REEIANSKGQKRAKLIKRLRVIDNFIATGSRPEWMVLDVIPVIPPDLRPMVQLDGGRFATSDLNDLYRRV
INRNNRLARLQEILAPEIIVRNEKRMLQEAVDALIDNGRRGRTVVGANNRPLKSLSDIIEGKQGRFRQNL
LGKRVDYSGRSVIVVGPKLKMHQCGLPKEMAIELFQPFVIHRLIRQGIVNNIKAAKKLIQRADPEVWQVL
EEVIEGHPVLLNRAPTLHRLGIQAFEPILVEGRAIQLHPLVCPAFNADFDGDQMAVHVPLSLEAQAEARL
LMLASNNILSPATGEPIVTPSQDMVLGCYYLTAENPGAQKGAGRYFASLEDVIMAFEQGRIDLHAWVWVR
FNGEVEDDDEDTEPLKTETLEDGTRIEQYRYRRDRFDEDGNLISQYILTTVGRVIMNKTIQDALAAT
>gnl|CDD|235056 PRK02627, PRK02627, acetylornithine aminotransferase; Provisional
MTSEAIIELEKKYLMNTYGRLPIAFVRGEGARLWDDDGKEYLDFLAGIAVNNLGHCHPKLVEAIQEQAAK
LIHTSNLYYIEPQEELAEKLVELSGMDKVFFCNSGAEANEAAIKLARKYGHKKGIEKPEIITAENSFHGR
TLATLSATGQPKYQEGFEPLVEGFIYVPFNDIEALKAAITDKTAAVMLEPIQGEGGVNPADKEYLQALRE
LCDENGILLILDEVQTGMGRTGKLFAYQHYGIEPDIMTLAKGLGGGVPIGAVLAKEKVADVFTPGDHGST
FGGNPLACAAALAVIEIIEEEGLLENAAEVGEYLRAKLRELLEKYPGIKEVRGLGLMIGIELDRPAAEIV
KKALEKGLLINVTGDNVLRLLPPLIISKEEIDEAVDRLEEVLKELL
>gnl|CDD|235057 PRK02628, nadE, NAD synthetase; Reviewed
MMDFFSIYRHGFVRVAAATPKVRVADPAFNAARILALARRAADDGVALAVFPELSLSGYSCDDLFLQDTL
LDAVEDALATLVEASADLDPLLVVGAPLRVRHRLYNCAVVIHRGRILGVVPKSYLPNYREFYEKRWFAPG
DGARGETIRLCGQEVPFGTDLLFEAEDLPGFVFGVEICEDLWVPIPPSSYAALAGATVLANLSASNITVG
KADYRRLLVASQSARCLAAYVYAAAGVGESTTDLAWDGQTLIYENGELLAESERFPREEQLIVADVDLER
LRQERLRNGSFDDNARHRDESAPFRTIPFALDPPAGDLGLRRPVERFPFVPSDPARLDQRCYEAYNIQVS
GLAQRLRATGLKKVVIGISGGLDSTHALLVAAKAMDRLGLPRKNILAYTMPGFATTDRTKNNAVALMKAL
GVTAREIDIRPAALQMLKDIGHPFARGEPVYDVTFENVQAGERTQILFRLANQHGGIVIGTGDLSELALG
WCTYGVGDHMSHYNVNASVPKTLIQHLIRWVIASGQFDEAVSEVLLDILDTEISPELVPADKEGEIVQST
EDIIGPYELQDFFLYYFLRYGFRPSKIAFLAWHAWKDAERGAWPGFPEDKRPAYDLATIKKWLEVFLRRF
FSSQFKRSALPNGPKVGSGGSLSPRGDWRAPSDASAAAWLDELERLVPE
>gnl|CDD|179455 PRK02645, ppnK, NAD(+) kinase
MQLKQVIIAYKAGSSQAKEAAERCAKQLEARGCKVLMGPSGPKDNPYPVFLASASELIDLAIVLGGDGTV
LAAARHLAPHDIPILSVNVGGHLGFLTHPRDLLQDESVWDRLQEDRYAIERRMMLQARVFEGDRSNEEPV
SESYYALNDFYLKPASEDRSPTCILELEIDGEVVDQYQGDGLIVSTPTGSTAYTMAAGGPILHPGIDAII
VTPICPMSLSSRPIVIPPGSRVVIWPLGDYDLNIKLWKDGVLATSIWPGQRCVIQKARHPAKFIILEESY
SYYRTLREKLHWAGSLIHYNNNHRN
>gnl|CDD|179456 PRK02649, ppnK, NAD(+) kinase
MPKAGIIYNDGKPLAVRTAEELQDKLEAAGWEVVRASSSGGILGYANPDQPVCHTGIDQLVPPGFDSSMK
FAIVLGGDGTVLSAARQLAPCGIPLLTINTGHLGFLTEAYLNQLDEAIDQVLAGQYTIEERTMLTVSVMR
GDQLRWEALSLNEMVLHREPLTSMCHFEIAIGRHAPVDIAADGVILSTPTGSTAYSLSAGGPVITPDVPV
LQLTPICPHSLASRALVFSDSEPVTVFPATPERLVMVVDGNAGCYVWPEDRVLIRRSPYPVRFIRLQDPE
FFRVLREKLGWGLPHIAKPTSVELP
>gnl|CDD|235058 PRK02654, PRK02654, putative inner membrane protein translocase component YidC; Provisional
MDFGIGFISNNVMLPILDFFYGIVPSYGLAIVALTLVIRFALYPLSAGSIRNMRRMKIAQPVMQKRQAEI
QERYKNDPQKQQEEMGKLMKEFGNPLAGCLPLLVQMPILFALFATLRGSPFADVNYTVNLQVLPSEQIAA
VQPQPFKSKPQNIFITDGVHFPVIASLPGGTKLGVGESVKIQLQTTEGKPFSQLLAEYPNSKLSPTWKVT
KGEERVKVSEDGTIEALAPGDATIQGTIPGLAANSGFLFIKALGQVGFYDVDGAINWDILIMVLGFGVSL
YLSQVLSGQGMPANPQQSTANKITPVMFSGMFLFFPLPAGVLLYMVIANIFQTLQTFLLSREPLPENLQK
ILDEQSKVAKAEAAEKGRERLPFEP
>gnl|CDD|179459 PRK02655, psbI, photosystem II reaction center protein I
MLALKISVYIVVFFFVGLFVFGFLSSDPTRNPGRKDLE
>gnl|CDD|179460 PRK02693, PRK02693, apocytochrome f; Reviewed
LMKRILLAFAGSLLLLASDLILPQSAAAYPFWAQQNYESPREATGKIVCANCHLAQKPTEVEVPQSVLPD
SVFKAVVKIPYDTDVQQVGADGSKVGLNVGAVVMLPDGFKLAPQDRWTEEIKEETEGVYFTPYSEDQENI
ILVGPLPGDQYQEIVFPVLSPDPATDKNIHFGKYSVHVGGNRGRGQVYPTGEKSNNNVFTASAAGTITSI
ETGEDGGYVVTITTEDGEAVTETIPAGPELIVKEGDTVEAGDPLTNDPNVGGFGQLDTEIVLQSPVRVKG
LIAFFAAVMLAQILLVLKKKQVEKVQAAEGNF
>gnl|CDD|235061 PRK02714, PRK02714, o-succinylbenzoate synthase
MNYRFAFRPYQRPFRQPLQTAHGLWRIREGIILRLTDETGKIGWGEIAPLPWFGSETLEEALAFCQQLPG
EITPEQIFSIPDALPACQFGFESALENESGSRSNVTLNPLSYSALLPAGEAALQQWQTLWQQGYRTFKWK
IGVDPLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAKRWLQLCDRRLSGKIEFIEQPLPPDQFDEML
QLSQDYQTPIALDESVANLAQLQQCYQQGWRGIFVIKPAIAGSPSRLRQFCQQHPLDAVFSSVFETAIGR
KAALALAAELSRPDRALGFGVTHWFSDEEEDWLQALWERP
>gnl|CDD|235062 PRK02724, PRK02724, 30S ribosomal protein PSRP-3
TPKADEGRFILKVLWLDDNVALAVDQIVGKGTSPLTAYFFWPRNDAWEQLKTELESKHWITENERVEVLN
KATEVINYWQEEGKGKPLAEAQLKFPEVTFCGTA
>gnl|CDD|235063 PRK02726, PRK02726, molybdenum cofactor guanylyltransferase
SKTVKNNLVALILAGGKSSRMGQDKALLPWQGVPLLQRVARIAAACADEVYIITPWPERYQSLLPPGCHW
LREPPPSQGPLVAFAQGLPQIKTEWVLLLACDLPRLTVDVLQEWLQQLENVPEEAIAALPKQEKGWEPLC
GFYRRRCLPSLEQFIQQGGRSFQGWLAQVPVQELALSDPDMLFNCNTPEDLATIQGIGRD
>gnl|CDD|235065 PRK02733, PRK02733, photosystem I reaction center subunit IX; Provisional
MLGLTKFLSTAPVVAAIWLTLTAGILIEFNRFFPDLLFHPMG
>gnl|CDD|235066 PRK02746, pdxA, 4-hydroxythreonine-4-phosphate dehydrogenase PdxA
MSNEDSDPRPRLAITLGDPAGIGPEVILKALASPELPENCQPTLVGCRSLLEQTYQRLKSQGIEPLADPA
NLDILDIPLDSTIIPGKGNAASGAASFAYLTTAIEITLAGEFDAIVTAPIAKSAWHAAGHHYPGQTEVLA
ELAGVERFGMLFTARSPHTGWRLRTLLATTHIPLCQVPKTLTPELITSKLDLLIDFLQRDFGIEKPRIAI
AGLNPHAGEQGQLGTEEKDWLIPWLESWRQKNPDIQLLGPIPPDTCWVSPAQAWYGKGVAEAPDGYLALY
HDQGLIPVKLMAFDRAVNTTIGLPFIRTSPDHGTAFDIAGKGIARPQSMKAAIKLAWELSKQRRL
>gnl|CDD|179468 PRK02749, PRK02749, photosystem I reaction center subunit IV; Provisional
MAISRGDKVRILRPESYWYNEVGTVASVDKSGIKYPVIVRFDKVNYNGFSGVDGGINTNNFAESELEEVE
A
>gnl|CDD|235067 PRK02759, PRK02759, bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE
TEQQIEELDFDKNDGLIPAIVQDALTGEVLMLGYMNREALEKTLETGEVTFFSRSKQRLWTKGETSGNTQ
KVVSIRLDCDNDTLLVLVEPIGPACHTGTRSCFYREKKAAPPWDFLSQLEQLIAERKNAPPEGSYTAKLF
ASGTKRIAQKVGEEAVEVVLAAKNNDKEELINEAADLLYHLLVLLADQGLSLSDVIAELKERH
>gnl|CDD|235068 PRK02769, PRK02769, histidine decarboxylase; Provisional
MGLSPADQKEIEDFWLYLRHNQYFNVGYPEAADFDYSALKRFFSFSINNCGDPYSKSNYPLNSFDFERDV
MNFFAELFKIPFNESWGYITNGGTEGNLYGCYLARELFPDGTLYYSKDTHYSVSKIARLLRIKSRVITSL
PNGEIDYDDLISKIKENKNQPPIIFANIGTTMTGAIDNIKEIQEILKKIGIDDYYIHADAALSGMILPFV
NNPPPFSFADGIDSIAISGHKFIGSPMPCGIVLAKKKYVERISVDVDYIGSRDQTISGSRNGHTALLLWA
AIRSLGSKGLRQRVQHCLDMAQYAVDRLQANGIPAWRNPNSITVVFPCPSERIWKKWHLATSGNQAHIIT
MPHHNKQQIDSLIDELIFDLKNPNKIDFSN
>gnl|CDD|179472 PRK02793, PRK02793, phi X174 lysis protein; Provisional
MQDSSLEARLAELESRLAFQEITIEELNVTVTAHEMEMAKLRDHLRLLTEKLKASQPSNIASQAEETPPP
HY
>gnl|CDD|179473 PRK02794, PRK02794, DNA polymerase IV; Provisional
MPGLCRDCLADQDGAARRCPACGSPRLVRHPELYTLSIAHIDCDAFYASVEKRDNPELRDKPVIIGGGKR
GVVSTACYIARIHGVRSAMPMFKALKLCPDAVVIKPDMEKYVRVGREVRAMMQALTPLVEPLSIDEAFLD
LSGTERLHGAPPAVVLARFARRVEREIGITVSVGLSYNKFLAKIASDLDKPRGFSVIGRAEALAFLAPKP
VGIIWGVGPATAARLARDGIRTIGDLQRADEADLMRRFGSMGLRLWRLARGIDDRKVSPDREAKSVSAET
TFETDLSDFEDLEPILWRLSEKVSRRLKAAGLAGRTVTLKLKTADFRLRTRRRTLEDPTQLADRIFRTAR
ELLEKETDGTAFRLIGIGVSDLSPADEADPPDLLDPQATRRAAAERAIDALRAKFGAAAVETGRALRGP
>gnl|CDD|235070 PRK02797, PRK02797, TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
MVVGKDNGLSDSCPALDIQFFSSKKALAEAVIAKAKANRAQRFFLHGQFNPTLWLALLSGKIKPKQFYWH
IWGADLYEESKGLKFRLFYPLRRLAQKRVGHVFATRGDLSYFAQRHPKVPGSLLYFPTRMDPSLNTMAND
RQRAGKMTILVGNSGDRSNRHIEALRALHQQFGDNVKIIVPMGYPANNQAYIEEVRQAGLALFGAENFQI
LTEKLPFDDYLALLRQCDLGYFIFARQQGIGTLCLLIQLGKPVVLSRDNPFWQDLTEQGLPVLFTGDDLD
EDIVREAQRQLASVDKNIIAFFSPNYLQGWRNALAIAAGEVA
>gnl|CDD|235072 PRK02812, PRK02812, ribose-phosphate pyrophosphokinase; Provisional
MTSFATAARAEQLPLLSDNNRLRLFSGSSNPALAQEVARYLGMDLGPMIRKRFADGELYVQIQESIRGCD
VYLIQPTCAPVNDHLMELLIMVDACRRASARQITAVIPYYGYARADRKTAGRESITAKLVANLITKAGAD
RVLAMDLHSAQIQGYFDIPCDHVYGSPVLLDYLASKNLEDIVVVSPDVGGVARARAFAKKLNDAPLAIID
KRRQAHNVAEVLNVIGDVKGKTAILVDDMIDTGGTICEGARLLRKEGAKQVYACATHAVFSPPAIERLSS
GLFEEVIVTNTIPVPEERRFPQLKVLSVANMLGEAIWRIHEESSVSSMFR
>gnl|CDD|235073 PRK02813, PRK02813, putative aminopeptidase 2; Provisional
MMDARAFAQDLLDFIDASPSPFHAVANVAQRLEAAGFTELDETDAWKLEPGGRYYVVRNGSSLIAFRVGE
GAPAETGFRIVGAHTDSPGLRVKPNPDTGEAGYLQLNVEVYGGPILNTWLDRDLSLAGRVVLRDGNKPES
RLVNIDRPILRIPNLAIHLNREVNEGLKLNPQKHLLPILLNGVGEKEGDFLELLAEELGVDADDILDFDL
FLYDTQPGALIGANGEFISSGRLDNLSSCHAGLEALLAAASDATNVLAAFDHEEVGSATKQGADSPFLED
VLERIVLALGGDREDFLRALARSFLISADMAHAVHPNYPEKHDPTHRPLLNKGPVIKINANQRYATDAES
AAVFKLLCEKAGVPYQEFVNRSDMPCGSTIGPITAARLGIRTVDVGAPMLAMHSARELAGVKDHAYLIKA
LTAFFSGA
>gnl|CDD|179478 PRK02816, PRK02816, phycocyanobilin:ferredoxin oxidoreductase; Validated
MLSTSLSLRKQLHPLILQLAERIRSHWQQLLDLSPYALPPDLGYIEGKLEGEKLFIENECYQAPGFRKLH
LELARLGNGLDILHCVMFPDPRYDLPIFGADLVAGRGGISAAIVDLSPVSRTLPDAYIKALSALPKPAFS
QPRELPEWGDIFSPYCLFIRPTNAEEENQFLDRVDEYLSIHCQLAIAAQPDSDSEQIIERLAGQKNYCLQ
QKRNDKTRRVLEKAFGPEWADRYITTVLFDLPP
>gnl|CDD|179479 PRK02821, PRK02821, RNA-binding protein
MLADAVEHLVRGIVDNPDDVRVDSHTNRRGRTLEVRVHPDDLGKVIGRGGRTATALRTVVAAIGGRGVRV
DVVDTDR
>gnl|CDD|235075 PRK02833, PRK02833, phosphate-starvation-inducible protein PsiE; Provisional
SNKRFSKIAKLLQTILNIGLIILGIILVIFLFKETIHLAQLLFSPNSQTSSYKLLEEIVVFFLYFEFIAL
IVKYFKSGGHFPLRYFIYIGITAIIRLIIVDHESPMDTLLYAGAILLLVIALFLANSKRLKRE
>gnl|CDD|235076 PRK02842, PRK02842, ferredoxin:protochlorophyllide reductase (ATP-dependent) subunit N
MAAEPSSLTFLKETGQRHVFCGLTSVVWLHRKIQDAFFLVVGSRTCAHLLQSAAGVMIFAEPRFGTAILE
EGDLAGLADANEELDRVVEELIKRRPNISVLFLVGSCPSEVIKLDLEGLAERLSTEFAGVPVLNYSGSGL
ETTFTQGEDAVLAALVPFCPEAPADHPSLVLVGSLADVVEDQLTLEFKKLGIGVVGFLPARRFTELPAIG
PGTVVALAQPFLSDTARALRERGAKVLTAPFPLGPEGTRAWLEAAAAAFGIDPDGLEEREAPAWERARKA
LEPYRELLRGKRVFFLPDSQLEIPLARFLSRECGMELVEVGTPYLNRRFLAAELALLPDGVRIVEGQDVE
RQLDRIRALRPDLVVCGLGLANPLEAEGITTKWSIEFVFTPIHGFEQAGDLAELFTRPLRRRAALKVLGW
DKLVEEE
>gnl|CDD|235077 PRK02853, PRK02853, hypothetical protein; Provisional
SSTPADGRNRLVDVELDEASIGRSTPDVEHERAVAIFDLLEENSFAPEGDDGGPYRLHLSLQENRLVFDI
RREDGEPVATHILSLTPFRRVVKDYFMICESYYQAIRTATPSQIEAIDMGRRGLHNEGSELLQERLEGKI
EVDFDTARRLFTLICVLHWRG
>gnl|CDD|179484 PRK02854, PRK02854, primosomal protein DnaT
MSSRILTSDVIGIDALVHDHQTVLAKAEGGVVAVFANNAPAFYAVTPARLAELLALEEKLARPGSDVALD
DQLYQEPQAAPVAVPMGKFAMYPDWQPDADFIRQAALWGVALREPVTAEELASFIAYWQAEGKVFHHIQW
QQKLARSLQISRASNGGQPKRDINTVSEPDSQIPPGFRG
>gnl|CDD|179486 PRK02862, glgC, glucose-1-phosphate adenylyltransferase; Provisional
MKRVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLIDIPISNCINSGINKIYVLTQFNSASLNRHISQ
TYNFDGFSGGFVEVLAAQQTPENPSWFQGTADAVRKYLWHFQEWDVDEYLILSGDQLYRMDYRLFVQHHR
ETGADITLAVLPVDEKDASGFGLMKTDDDGRITEFSEKPKGDELKAMAVDTSRLGLSPEEAKGKPYLASM
GIYVFSRDVLFDLLNKNPEYTDFGKEIIPEAIRDYKVQSYLFDGYWEDIGTIEAFYEANLALTQQPNPPF
SFYDEKAPIYTRARYLPPSKLLDATITESIIAEGCIIKNCSIHHSVLGIRSRIESGCTIEDTLVMGADFY
ESSEEREELRKEGKPPLGIGEGTTIKRAIIDKNARIGNNVRIVNKDNVEEADREDQGFYIRDGIVVVVKN
AVIPDGTVI
>gnl|CDD|235079 PRK02866, PRK02866, cyanate hydratase; Validated
MKREELTEKILAAKKEKGLTWADIAEAIGLSEVWVTAALLGQMTLPAEEAEKVAELLGLDEDAVALLQEV
PYRGSLPPAVPTDPLIYRFYEMVQVYGTTLKALIHEKFGDGIMSAIDFKLDVDKVEDPKGDRVVITLDGK
FLPYKPW
>gnl|CDD|235080 PRK02868, PRK02868, hypothetical protein; Provisional
TANSLYRDTGNFFRNQFITILLLSLLTAFITVLLGHAFSPSDEQLSILENGIPISGSSGLFELVQNMSPE
QQQILLKASAASTFSGLIGNTLLLGGILTLIQLVSAGQRVSALRAIGASAPILPKLLILIFLTTLLIQLG
FMLVVVPGILLAIALSLSPVILVTEKMGIFASMRASMRLAWANMRLVAPAVLLWLLAKTLLLLLASSFAV
LTPNVAAVLLNTLSNLISAILLIYLFRLYMLLRQV
>gnl|CDD|235081 PRK02870, PRK02870, heat shock protein HtpX; Provisional
SSIDDLEAGSVDWRKVIRRNRLKTRAVIATYLAIFLFIGLLVDAIRIASEYPAASLGKALLALLTFQIFP
TATLIMSLVAVISILVTFQNFDKIMLSGTEYKEITPENALSLQERQLYNVVEELLVAAGLRFMPKVYIID
APYMNAFASGYSEKSAMVAITTGLLEKLDRDELQAVMAHELSHIRHGDIRLTLCVGVLSNIMLIVADFLF
YSFMGNRRNSGANRARMIILILRYVLPILTVLLMLFLSRTREYMADAGAVELMRDNEPMARALQKISNDH
AQNDEQYAYKHTDHESTRRAAYLFDPAGISPGSLSDAFSTHPSIENRLAALGGKLK
>gnl|CDD|179490 PRK02877, PRK02877, hypothetical protein; Provisional
MQFSTTPTLEGQTIVEYCGVVTGEAILGANIFRDFFAGIRDIVGGRSGAYEKELRKAREIAFEELGEQAR
ALGADAVVGIDIDYETVGQNGSMLMVSVSGTAVKTR
>gnl|CDD|179491 PRK02886, PRK02886, hypothetical protein; Provisional
MENNRQGIIVWLHSLKQAKQLRKFGNVHYVSKRLKYAVLYCDMEQVEDIMNKLSSLPFVKRVEPSYRPFL
KTEFESKPDKAKEYDYK
>gnl|CDD|235082 PRK02888, PRK02888, nitrous-oxide reductase; Validated
SEDEAPSGLSRRQFLGTAALAGAAGAAGSTGLLGGALAAGAAAAAAAAAAAAGGKYEVAPGELDEYYGFW
SGGHSGEVRILGLPSMRELMRIPVFNRDSATGWGITNESKKVLGEGARGGKYLNGDTHHPHMSFTDGTYD
GRYLFINDKANTRVARIRLDVMKCDKITELPNVQGIHGLRPQKIPRTGYVFCNGEFRIPLPNDGKDLDDP
KKYRSLFTAVDAETMEVAWQVMVDGNLDNVDTDYDGKYAFSTCYNSEEGVTLAEMMAAERDWVVVFNIAR
IEEAVKAGKFKTIGGSKVPVVDGRKAANAGSALTRYVPVPKNPHGVNTSPDGKYFIANGKLSPTVTVIDV
RKLDDLFDGKIKPRDAVVAEPELGLGPLHTAFDGRGNAYTTLFLDSQIVKWNIEAAIRAYKGEKVDPIVQ
KLDVHYQPGHNHASMGETKEADGKWLVSLNKFSKDRFLPVGPLHPENDQLIDISGDKMKLVHDGPTFAEP
HDAIIVHRSKINPKQVWDRDDPFFADAVKQAKADGVDLEEDSKVIRDGNKVRVYMTSQAPAFGLREFTVK
QGDEVTVIVTNLDKVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHALHMEMRGRM
LVEPK
>gnl|CDD|179494 PRK02898, PRK02898, energy-coupling factor ABC transporter substrate-binding protein
KMKKNLLLLLLVILLAVLPLFIYSGSGEDGGEFGGADGQAEEAITEIAPDYEPWFEPLWEPPSGEIESLL
FALQAALGAGIIGYILGYYKGRSKRRNRAG
>gnl|CDD|179495 PRK02899, PRK02899, genetic competence negative regulator
MRLERLNYNKIKIFLTFDDLSERGLTKEDLWRDAPKVHQLFRDMMQEANKELGFEADGPIAVEVFSLQAQ
GMVVIVTKEHQEDDTDDEFEDDYIEMQVTLDESDHILYEFATFEDVINLSHRLYNLGVTGGKLYSYDGRF
YLWLEEEELIQLLKADFIAILAEYGNPSTVTIYRLEEYGKELMASQAVEQIHRYFVK
>gnl|CDD|235084 PRK02901, PRK02901, O-succinylbenzoate synthase; Provisional
MMMLPSLDDLLDRAHVVALPMRVRFRGITVREAVLIEGPAGWGEFSPFLEYDPAEAAAWLASAIEAAYGG
PPPPVRDRVPVNATVPAVDAAQVPEVLARFPGCRTAKVKVAEPGQTLADDVARVNAVRDALGPDGRVRVD
ANGGWSVDEAVAAARALDADGPLEYVEQPCATVEELAELRRRVGVPIAADESIRRAEDPLRVARAGAADV
AVLKVAPLGGVRAALDIAEQIGLPVVVSSALDTSVGIAAGLALAAALPELDHACGLATGGLFEEDVADPL
LPVDGFLPVRRVTPDPARLAALAADPDRRQWWIDRVRACYALLEQRL
>gnl|CDD|179497 PRK02909, PRK02909, flagellar transcriptional regulator FlhD
MHTSELLKEIYDINLSYLLLAQRLIRQDKASAMFRLGISEEMADILAALTLAQMVKLAETNQLLCRFRFD
DHATLSALTQDSRVDDLQQIHTAILLAGQLLEQVA
>gnl|CDD|235085 PRK02910, PRK02910, ferredoxin:protochlorophyllide reductase (ATP-dependent) subunit B
MRLAYWTYEGPAHVGAMRIATSMKGVHYVLHAPQGDDYADLLFTMLERRGKRPPVTYSTVQARDLARGTA
ELLKDTLRRADERFQPDLIVVGPSCTAELLQEDLGGLAKHAGLPIPVLPLELNAYRVKENWAADETFYQL
VRALAKKAAELPQPKTARPSVNLLGPTALGFHHRDDLTELRRLLATLGIDVNVVAPLGASPADLKRLPAA
WFNVVLYREIGESAARYLEREFGQPYVKTVPIGVGATARFIREVAELLNLDGADLEAFILDGLSAPSRLP
WFSRSVDSTYLTGKRVFVFGDATHAVAAARILSDELGFEVVGAGTYLREDARWVRAAAKEYGDEALITDD
YLEVEDAIAEAAPELVLGTQMERHSAKRLGIPCAVISAPTHVQDFPARYSPQMGFEGANVIFDTWYHPLM
LGLEEHLLDMFGDDFEFYDGAAAAAAAASAGHDTKEVATKAAAADSELVWTPEAEAELKKIPFFVRGKVR
RNTEKFARERGLPEITLEVLYDAKAHFGA
>gnl|CDD|179499 PRK02913, PRK02913, hypothetical protein; Provisional
MTDIVLILFIALLLAYAIYDQFIMPRRKGKTLLKVPLKRRGRIDSLIFVGLIAILIYNNVTNHGAPLTTY
LLSALALLAIYIFFIRSPKLLFKEKGFFYANVFIEYSRIKAMNLSEDGILVIDLEQRRLLIRVRNLDDLE
KIYKFFIEYQ
>gnl|CDD|235086 PRK02919, PRK02919, oxaloacetate decarboxylase subunit gamma; Provisional
MNNAELLGEGFTLMFLGMGFVLAFLFLLIFAIRGMSALINRFFPEPVAAPAPRPVPVAPVDDFTRLKPVI
AAAIHHHRRLNA
>gnl|CDD|179501 PRK02922, PRK02922, cell surface composition regulator GlgS
MNDHSLYSLNNFDFLARSFARMHAEGRPVDIQAVTGNMDEEHRTWFCARYAWYCQQMMQARELELEH
>gnl|CDD|235087 PRK02925, PRK02925, glucuronate isomerase; Reviewed
MMAFLDEDFLLPNEIARRLYHDAKDLPIIDYHCHLDPKEIAENKPFKNITELWLKGDHYKWRAMRSNGVD
EELITGDASDREKFRAWAKTVPLFIGNPLYHWTHLELRRVFGITELLSPETADEIWDEINELLATPEFRP
RALIERFNVEVICTTDDPLDDLEYHKAIAEDGSFDGRVLPTFRPDKAFNIEHEGFADYVEKLGEVTGTDI
TTFDGLLEALRKRRDYFAAHGCRSSDHGLDTVVTAELSEAEADAIFAKALAGGTLTEEEIAQFRTAMLTE
LARMYAEDGWVMQLHIGALRNNNTRMFKKLGPDTGFDSIGDTPIAEALSPLLDALGNENDLPKTILYTLN
PTDNEELATMAGNFQGLGIPGKMQFGAGWWFNDQKDGMERQMEQLAETGLLSNFVGMLTDSRSFLSYARH
EYFRRILCNFLGRWVEEGELPADEELLGEMVKDICYNNAKRYFKLE
>gnl|CDD|179503 PRK02929, PRK02929, L-arabinose isomerase; Provisional
MTIFKQYEVWFVTGSQHLYGEETLRQVAEHAEEIVDGLNASGKLPVKIVLKPVLTTPDEITAVCREANYD
DNCAGVITWMHTFSPAKMWIRGLSALQKPLLHLHTQFNAEIPWDTIDMDFMNLNQSAHGDREFGFIGARL
RKQRKVVVGHWQDPEVQERIGAWMRVAAAWQESRHLKVARFGDNMRNVAVTEGDKVEAQIKFGWSVNTWG
VGDLVEVVNAVSDGDVDALVDEYESLYDLTPALQDGGEKRQSLREAARIELGLKRFLEDGGFTAFTTNFE
DLHGLKQLPGLAVQRLMAQGYGFGGEGDWKTAALVRIMKVMGTGLPGGTSFMEDYTYHFEPGNELVLGSH
MLEVCPSIAEEKPRLEVHPLGIGGKEDPARLVFTGKAGPAVNASLIDMGDRFRLIVNEVDAVEPPHPLPK
LPVARALWKPQPDLKTAAEAWILAGGAHHTVFSQALTLEQLRDFAEMAGIELVVIDEDTTLRAFKDELRW
NEVYYRLAR
>gnl|CDD|179504 PRK02935, PRK02935, hypothetical protein; Provisional
MSIKYSNKINKIRTFALSLVFIGFIVMYLGIFFRESIIIMTIFMLLGFLAVIASTVVYFWIGMLSTKAVQ
VICPSCEKPTKMLGRVDACMHCNQPLTLDRSLEGKEFDEK
>gnl|CDD|179505 PRK02936, argD, acetylornithine transaminase
MSHLFPTYGRFPIDIVKGKGTKVTDNNGKTYLDFTSGIAVCNLGHCHPTVTKAVQEQLDDIWHVSNLFTN
SLQEEVASLLAENSAGDLVFFCNSGAEANEAALKLARKHTGKSKIVTFEQSFHGRTFGTMSATGQEKIKE
GFGPLLPGFTHVPFNDIKALKEVMNEEVAAVMLEVVQGEGGVIPADPAFLQEVQTLCKKFGALLIIDEVQ
TGIGRTGTLFAYEQFGLDPDIVTVAKGLGNGIPVGAMIGKKELGTAFGPGSHGSTFGGNPLAMAAAKEVL
QVIKQPSFLEEVQEKGEYFLQKLQEELEHLECVKNIRGKGLMIGIECTEEVAPVIEQLREEGLLVLSAGP
NVIRLLPPLVVTKEELDQAVYLLKKVL
>gnl|CDD|179506 PRK02939, PRK02939, YnfC family lipoprotein
MKKKLLLTLLAILLTGCDRTEALESFTPEMASFSNEFDFDPLRGPVKDFTQTLMDEQGEVTKRVSGTLSE
EGCFDTLELLDLENNTGLALVLDANYYRDAETLEKRVRLQGKCQLAELPSAGVSWETDDNGFVIKASGKE
MQVEYRYDDEGYPLGKTTKSNDKTLSVSATPSADPRKKLDYTAVTTLNNQQVGNVKQSCEYDSHANPVDC
QLLIVDESVKPAVERTYTIKNTIDYY
>gnl|CDD|235088 PRK02943, PRK02943, secA regulator SecM
IGILNRWRQFGRRYFWPHLLLGMVAASLGLPALSNAAEPNTPATASSQSRQNSAKVNFDQLALLEASTRR
PSFSVDYWHQHAIRTVIRHLSFALAPQALPVAEESAPLQAQHLALLDTLNALLTQEGTPPEIIRRTSYAH
FTPQASFSTGLWLAQVQGIRAGPQRLS
>gnl|CDD|179508 PRK02944, PRK02944, YidC family membrane integrase SpoIIIJ
MKKKLGLLAMVVALMAILAGCSEVNQPITPKSTGFWNEYFVYPLSQLITYFANLFGSNYGLAIIVVTLLI
RLLILPLMIKQTKSTKAMQALQPEMQKLKEKYSSKDQATQQKLQQEMMQLFQKNGVNPLAGCLPIFIQMP
ILIAFYHAIMRTSEISKHSFLWFDLGQADPYYILPIVAGITTFIQQKLMMAGTAGQNPQMAMMLWLMPIM
ILIFAINFPAALSLYWVVGNIFMIAQTYLIKGPEIKASKAGGSKK
>gnl|CDD|235089 PRK02946, aceK, bifunctional isocitrate dehydrogenase kinase/phosphatase protein; Validated
LSSDLALLIAQTILQGFDAHYARFREITAGAQQRFEQADWHAVQRAAKERIHLYDHRVGEVVEQLRAELD
AESTDDEFWQRVKLHYIGLLPDHPQPELAETFFNSVYCRLFHHRYFDNDFLFVRPAQPTERFRTIPRPLY
RDYYPDGGLAATLERILSDFPLRLPFEDLDRDIAYIAAALREALGPFDALANFQIEVLNSLFYRNKGAYL
VGRIINGDRTLPFLLPILHNEDGGLFIDAVLTDRDELSIVFSFARSYFMVDMPVPAALVEFLRELLPGKP
TAELYTAIGLQKQGKTEFYREFLHHLRHSSDQFIIAPGIKGMVMLVFTLPSFPYVFKVIKDRFAPPKEMT
RAQVKAKYQLVKEHDRVGRMADTQEYSNVAFPKARFSPALLAELLEEAPSKLEDLGDELVIRHLYIERRM
TPLNLYLEQASDAQLRDAVEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYLTECNFRD
IPPPRYPEDEMSSEPWYSVGPGDVFPEEFRPFLLGDPRVRRAFEEHHADLFDADYWQGLQQRIREGHVED
VFPYRRSQRFSVRYG
>gnl|CDD|179510 PRK02947, PRK02947, sugar isomerase domain-containing protein
TDMIDEYFDAVIELLERVRETQAEAIEKAADLIADSIRNGGLIYVFGTGHSHILAEEVFYRAGGLAPVNP
ILEPSLMLHEGAVASSYLERVEGYAKAILDRYDIRPGDVLIVVSNSGRNPVPIEMALEAKERGAKVIAVT
SLAYSASVASRHSSGKRLAEVADVVLDNGAPKGDAVLEIPGLEAPVGPVSTVVGAAILNAIFAEVAERLV
ERGITPPVFLSANVDGGDEHNQALVEKYRDRIPRLA
>gnl|CDD|179511 PRK02948, PRK02948, IscS subfamily cysteine desulfurase
MIYLDYAATTPMSKEALQTYQKAASQYFGNESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGT
ESNYLAIQSLLNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTV
LASIQHANSEIGTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAV
YINPQVRWKPVFPGTTHEKGFRPGTVNVPGIAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPLPI
EVEGHSTSCLPHIIGVTIKGIEGQYTMLECNRRGIAISTGSACQVGKQEPSKTMLAIGKTYEEAKQFVRF
SFGQQTTKDQIDTTIHALETIGNQFYRGVKI
>gnl|CDD|235090 PRK02951, PRK02951, DNA replication terminus site-binding protein; Provisional
MARYDLVERLNTTFRQLEQELAALSQLLEQLPLLAARVFSLPPVEKGDEHDPLNRIEVTQHLGNEALELA
LRHFRDLFIQHQSENRSSKAAVRLPGVLCFSVDNAQQAALVALIQRINALKATLEEIITVESGLPSEARF
EFVHRHLPGLITLNAYRTITLLHDPASVRFGWANKHIIKNLTRDELLAQLEKSLKSGRAVAPWTREQWQE
KLEQEIQDIASLPEDAKLKIKRPVKVQPIARVWYAGQQKQVQHACPMPLIALCNEDNGAGVPDLGELLNY
DADNIQHRYKPQAQPLRLLIPRLHLYVAD
>gnl|CDD|179513 PRK02955, PRK02955, small acid-soluble spore protein SspI; Provisional
MSFNLRGAVLANVSGNSKEELEGTIVDAIQSGEEKMLPGLGVLFEVIWKNADENEKDEMLETLEQGLK
>gnl|CDD|235091 PRK02958, tatA, Sec-independent protein translocase subunit TatA
MGSFSIWHWLIVLVIVVLVFGTKKLRNIGSDLGGAVKGFKDGMKEGETPQEAQAQQLPDSGTIDVEAKEK
SKS
>gnl|CDD|235092 PRK02963, PRK02963, carbon starvation induced protein CsiD
VQNNAVDLAQDYSGFTLAPSAQSPRLLELTFTEQTTKQFLEQVAEWPVQALEYKSFLRFRVAKILDDLCG
NQLQPLLLKTLLDRAEGAFLINAVGIDDVAQADEMVKLATAVAHLIGRSNFDAMSGQYYARFVVKNVDNS
DSYLRQPHRVMELHNDGTYVEEITDYVLMMKIDEQNMQGGNSLLLHLDDWEHLDHFFRHPLARRPMRWAA
PPSKNVSKDVFHPVFDVDQQGRPVMRYIDQFVQPKDFEEGVWLSELSDALETSKGILSVPVPVGKFLLIN
NLFWLHGRDRFTPHPDLRRELMRQRGYFAYATHHYQ
>gnl|CDD|235093 PRK02967, PRK02967, nickel-responsive transcriptional regulator NikR
MQRVTITLDDDLLETLDSLIARRGYQNRSEAIRDLLRAALAQERTQEHQGTQCVAVLSYVYDHEKRDLAS
RLVSTQHHHHDLSVATLHVHLDHDDCLEVAVLKGDTGDVQHFADDVIAERGVRHGHLQCLPKEDQHHHH
>gnl|CDD|235094 PRK02971, PRK02971, 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF; Provisional
MMGYLWGLASVLLASVAQLSLKWGMSRLPLLSHAWDFIAALLAFGLALRAVLLGLAGYALSMLCWLKALR
YLPLSRAYPLLSLSYALVYLAAMLLPWFNETFSLKKTLGVACIMLGVWLINLPTTKARY
>gnl|CDD|179518 PRK02975, PRK02975, O-antigen assembly polymerase
MTLLQFSGLFVVWLLSTLFIATLTWFEFRRVRFNFNVFFSLLYLLTFYFGFPLTSVLVFRFDVGVAPPEI
LLQALLSATCFYAIYYVTYKTRLRKRVADVPRRPLFTMNRVETNLTWVILMLIALVSVGIFFMHNGFLLF
KLHSYSQIFSSEVSGVALKRFFYFFIPAMLVVYFLRQDSKAWLFFLVSTVAFGLLTYMIVGGTRANIIIA
FALFLFIGIIRGWISLWMLAAAGVLGIVGMFWLALKRYGLNVSGDEAFYTFLYLTRDTFSPWENLALLLQ
NYDKIDFQGLAPIVRDFYVFIPSWLWPGRPSMVLNSANYFTWEVLNNHSGLAISPTLIGSLVVMGGALFI
PLGAIVVGLIIKWFDWLYELGNRETNRYKAAILQSFCFGAIFNMIVLAREGLDSFVSRVVFFCVIFGACL
LVAKLLYWLFESAGLIHKRTKSSLRTQVEG
>gnl|CDD|235095 PRK02983, lysS, bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX
ARPASRRRWVPAAAGWTVGVIATLSLLASVSPLLRWIIRVPREFVDDYLFNFPDTSLAWAFVLALLAAAL
RRRKRAAWWVLLAYLVLAALLNVALLALGVNTAAETFGENSLSIIGFAVHVVAIVLLVLARREFPARVRR
GALRKALAVLVGGLAVGILVGWGLVELFPGSLAPPERLGWALNRVVGFALADPDLFTGHPPVWVNALLGL
FGAAALIAALIVLFRSQRADNALTGEDELAIRGLLLLYGEDDSLGYFATRRDKSVVFAPSGRAAITYRVE
VGVCLASGDPVGDPEAWPQAIDAWLALARTYGWAPAVMGASEAGARAYREAGLSALELGDEAILDTADFT
LSGPDMRPVRQAVTRVRRAGYTVRIRRHRDLPAEEMAQVIARADAWRDTETERGFSMALGRLGDPADGDC
LLVEAHDADGQVVALLSFVPWGRRGLSLDLMRRSPDAPNGVIELMVAELALEAESLGITRISLNFAVFRS
AFEEGARLGAGPVLRLWRGLLLFFSRWWQLESLYRSNVKYQPDWVPRYLCYEDARLLPRVGVASGIAEGF
LPLPFSRRNRVHTGHHPAVPERLAASGLLHHDGSAPDVAATAPDAPEPRLPEQVRVRLAKLEALRAAGVD
PYPVGVPPTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEQGSLADFRA
AVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEARDLL
RARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVER
VFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMRPDGDGVLEPVD
ISGPWPVVTVHDAVSEALGEEIDPDTPLAELRKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFY
TDFPTSVSPLTRPHRSDPGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDED
FLQALEYAMPPTGGLGMGVDRLVMLLTGRSIRETLPFPLVKPRQ
>gnl|CDD|179520 PRK02984, sspO, acid-soluble spore protein O; Provisional
MGKRKANHVIPGMNAASAQGQGAGYNEEFANEPLTEAERQNNKKRKKNQ
>gnl|CDD|235096 PRK02991, PRK02991, D-serine dehydratase; Provisional
ANINKLIAQYPLLKDLIALEETFWFNPNYTSLAEGLPYVGLTEADVQDAEARLKRFAPYLAKAFPETAAT
GGIIESPLVAIPAMQKALEKEYGQPISGRLLLKKDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLTLD
DDYSKLASPEFRQFFSQYSIAVGSTGNLGLSIGIMSAALGFKVTVHMSADARQWKKDKLRSHGVTVVEYE
GDYGVAVEEGRKAAESDPNCYFIDDENSRTLFLGYAVAGLRLKAQLAEQGIVVDADHPLFVYLPCGVGGG
PGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLMTGLHDQISVQDIGIDNLTAADGLAVGRASGFVGRAM
ERLLDGVYTVSDETLYRLLGLLADTEGIRLEPSALAGMAGPVRVCASVAYLQRHGLSEQLKNATHLVWAT
GGSMVPEEEMEQYLAKGRALL
>gnl|CDD|179522 PRK02998, prsA, peptidylprolyl isomerase; Reviewed
MKKKKLFLGTIISCVVLALSACGSSDNVVTSKVGNITEKELSKELRQKYGESTLYQMVLSKALLDKYKVS
DEEAKKQVEEAKDKMGDNFKSTLEQVGLKNEDELKEKMKPEIAFEKAIKATVTEKDVKDNYKPEMKVSHI
LVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVK
TTYGYHIIKVTDKKELKPFDEVKDSIRKDLEQQRLQDTTGKWKQQVVNDLLKDADIKVNDKEFKDTFKFL
EKK
>gnl|CDD|235097 PRK02999, PRK02999, malate synthase G; Provisional
MTERVQVGGLQVAAVLYDFVNNEALPGTGVDADAFWAGFAAIVHDLAPKNRALLAKRDELQAKIDAWHRA
HPGPPHDLAAYKAFLTEIGYLVPEPEDFTITTENVDPEIATQAGPQLVVPVMNARYALNAANARWGSLYD
ALYGTDAIPEEGGAEKGKGYNPVRGAKVIAYARAFLDEAAPLASGSHADVTGYAVEDGQLVVTLKDGSET
GLADPAQFVGYQGDAAAPSAILLKNNGLHIEIQIDRNHPIGKTDPAGVKDVVLESALTTIMDCEDSVAAV
DAEDKVLVYRNWLGLMKGDLTEEFEKGGKTFTRRLNPDREYTAPDGGELTLHGRSLLFVRNVGHLMTNPA
ILDADGNEIPEGILDAVVTSLIALHDLKGNGRRRNSRTGSVYIVKPKMHGPEEVAFANELFGRVEDLLGL
PRNTLKVGIMDEERRTSVNLKACIRAAKDRVVFINTGFLDRTGDEIHTSMEAGPMVRKGDMKSSPWIAAY
EDNNVDIGLACGLRGRAQIGKGMWAMPDLMADMLEQKIAHPKAGANTAWVPSPTAATLHALHYHQVDVFA
VQAELAKTRPRASLDDLLTIPLAENANWSAEEIQQELDNNAQGILGYVVRWVDQGVGCSKVPDIHDVGLM
EDRATLRISSQHIANWLRHGVVTEEQVMESLKRMAAVVDQQNAGDPAYRPMAPDFDNSIAFQAACDLVFK
GREQPNGYTEPLLHARRLEAKAKQAA
>gnl|CDD|179524 PRK03001, PRK03001, zinc metalloprotease HtpX
FNWVKTAMLMAAITALFIVIGGMIGGSQGMLIALLFALGMNFFSYWFSDKMVLKMYNAQEVDENTAPQFY
RMVRELAQRAGLPMPKVYLINEDQPNAFATGRNPEHAAVAATTGILRVLSEREIRGVMAHELAHVKHRDI
LISTISATMAGAISALANFAMFFGGRDENGRPVNPIAGIAVAILAPLAASLIQMAISRAREFEADRGGAR
ISGDPQALASALDKIHRYASGIPFQAAEAHPATAQMMIINPLSGGGLANLFSTHPSTEERIARLMAMART
GRF
>gnl|CDD|101162 PRK03002, prsA, peptidylprolyl isomerase PrsA
MRGKHIFIITALISILMLSACGQKNSSATVATATDSTITKSDFEKQLKDRYGKDMLYEMMAQDVITKKYK
VSDDDVDKEVQKAKSQYGDQFKNVLKNNGLKDEADFKNQIKFKLAMNEAIKKSVTEKDVKDHYKPEIKAS
HILVSDENEAKEIKKKLDAGASFEELAKQESQDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNP
VKSPNGYHIIKLTDKKDLKPYDEVKDSIRKNLEEERTADPIFGKKLLQSELKKANIKINDSELEDTFTIV
SPQGN
>gnl|CDD|179525 PRK03003, PRK03003, GTP-binding protein Der; Reviewed
YDDDEAEMRADGTWADESDWELDDEDLAELEAAEGGPLPVVAVVGRPNVGKSTLVNRILGRREAVVEDVP
GVTRDRVSYDAEWNGRRFTVVDTGGWEPDAKGLQASVAEQAEVAMRTADAVLFVVDATVGATATDEAVAR
VLRRSGKPVILAANKVDDERGEADAAALWSLGLGEPHPVSALHGRGVGDLLDAVLAALPEVPRVGSASGG
PRRVALVGKPNVGKSSLLNKLAGEERSVVDDVAGTTVDPVDSLIELGGKTWRFVDTAGLRRRVKQASGHE
YYASLRTHAAIEAAEVAVVLIDASEPISEQDQRVLSMVIEAGRALVLAFNKWDLVDEDRRYYLEREIDRE
LAQVPWAPRVNISAKTGRAVDKLVPALETALESWDTRIPTGRLNAWLGELVAATPPPVRGGKQPRILFAT
QASTRPPTFVLFTTGFLEAGYRRFLERRLRETFGFEGSPIRISVRVREKRGR
>gnl|CDD|235098 PRK03007, PRK03007, deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
MSAMPQDPYDDFDRERRVPEPPKSAGLPTEGQHRTDFARDRARVLHSAALRRLADKTQVVGPREGDTPRT
RLTHSLEVAQIGRGIAAGLGCDPDLVDLAGLAHDIGHPPYGHNGERALDEVAADCGGFEGNAQTLRILTR
LEPKVLDPDGRSAGLNLTRASLDAACKYPWTRGEADGSPRRKFGFYDDDREVFAWVRQGAPAGRPCLEAQ
VMDWADDVAYSVHDVEDGVVSGRIDLRVLADPVELAALAELGAAWFSGVDADELLAAADRLSELPVVAAV
GKFDGSLRSSAALKNLTSELVGRFASAAITATRAAAGPGPLTRYDADLVVPELVRAEVALLKTLALQFVM
SDPRHLARQARQRERIHRVADALWAGAPGALDPQFRAAFNEAADDAARLRVVVDQIASLTESRLERLHAR
LCGRSAFL
>gnl|CDD|235099 PRK03011, PRK03011, butyrate kinase; Provisional
MMRILVINPGSTSTKIAVFEDEKPIFEETLRHSAEELEKFKTIIDQYEFRKQAILDFLKEHGIDLSELDA
VVGRGGLLKPIPGGTYRVNEAMLEDLKNGKYGEHASNLGAIIAYEIAKELGIPAFIVDPVVVDEMEPVAR
ISGLPEIERKSIFHALNQKAVARRVAKELGKKYEELNLIVAHLGGGISVGAHRKGRVIDVNNALDGEGPF
SPERAGGLPVGDLVELCFSGKYTKEELKKKLVGKGGLVAYLGTNDAREVEKRIEEGDEKAKLVYEAMAYQ
IAKEIGAMAAVLKGKVDAIVLTGGLAYSKRLVERIKERVSFIAPVIVYPGEDEMEALAEGALRVLRGEEE
AKEYSPEA
>gnl|CDD|179529 PRK03057, PRK03057, hypothetical protein; Provisional
VSDLEKRQFLTWFLNNHRLKHPDARFVLLYLLQHPHLLENVHFTETEQKRARTLIISTAQSDEPGFVFYR
GGQKSESLAAAMGDLALNPNEPLYLILHFPGKARNHSYLQLLDHQAFENVKRHKQFQKYAKETEQVLDEV
LKRNEVSRLRMQIDQALDRKDMEEFQRLTEKLKKLEGQSQ
>gnl|CDD|235101 PRK03059, PRK03059, PII uridylyl-transferase; Provisional
SATAAPPPPAASLRAELKAAKAALLARFRQAPNVTALLHALSRLVDQALRRLWQECGLPAGAALVAVGGY
GRGELFPYSDVDLLVLLPDAPDAALDARIERFIGLCWDLGLEIGSSVRTVDECIEEAAQDVTVQTSLLEA
RLLTGSAALFERFQRRYRAALDPRAFFQAKLLEMRQRHAKFQDTPYSLEPNCKESPGGLRDLQTILWIAR
AAGLGSSWRELAKRGLITDREARQLRRNERFLKTLRARLHLLAGRREDRLVFDLQTALAESFGYRPTAAK
RASEQLMRRYYWAAKAVTQLNTILLQNIEARLFPSTSGITRVINERFVEKQGMLEIASDDLFERHPHAIL
EAFLLYQQTPGLKGLSARTLRALYNARDVMNAAFRRDPVNRALFMQILQQPRGITHALRLMNQTSVLGRY
LPNFRRIVGQMQHDLFHVYTVDQHILMVLRNLRRFAMAEHAHEYPFCSQLIANFDRPWLLYVAALFHDIA
KGRGGDHSTLGAVDARRFCRQHGLAREDAELVVWLVEHHLTMSQVAQKQDLSDPEVIARFAELVGDERRL
TALYLLTVADIRGTSPKVWNAWKGKLLEDLYRATLRVLGGAAPDAHSELEARKEEALALLRLEALPDDAH
EALWDQLDVGYFLRHDAADIAWHTRHLYRHVDTDTPIVRARLSPAGEGLQVMVYTPDQPDLFARICGYFD
RAGFSILDARVHTTRHGYALDTFQVLDPEEDVHYRDIINLVEHELAERLAEQAPLPEPSKGRLSRQVKHF
PITPRVDLRPDERGQYYILSVSANDRPGLLYAIARVLAEHRVSVHTAKINTLGERVEDTFLIDGSGLSDN
RLQIQLETELLDALAV
>gnl|CDD|179531 PRK03065, hutP, anti-terminator HutP; Provisional
MLLQGTHRIGRLAMLLALADENESPVLSILEADGWKYCTGKVGSMESQKVVAAIETAAKSNQVIETDVYR
ETHALYHAIMEALHGVTRGQIQLGDVLRTVGLRFAIVRGTPYDGKKEGEWIAVALYGTIGAPVKGSEHEA
IGLGINHI
>gnl|CDD|235102 PRK03072, PRK03072, heat shock protein HtpX; Provisional
WHRHANGLKTALLLGGMSALIVFIGALFGRTGLGIAVLIAVGMNAYVYWNSDKLALRAMHAQPVSEVQAP
AMYRIVRELSTAARQPMPRLYISPTAAPNAFATGRNPRNAAVCCTEGILQILNERELRGVLGHELSHVYN
RDILISSVAGALASVITYLANMAMFAGMFGGRRDNDGPNPLALLLVSLLGPIAATVIQLAISRSREYQAD
ESGAELTGDPLALASALRKISGGVQAAPLPPEPQLASQAHLMIANPFRAGGIGRLFSTHPPMADRIARLE
QMAGRMPG
>gnl|CDD|235103 PRK03080, PRK03080, phosphoserine transaminase
MTTLTIPALRPADPRFSSGPCKKRPGWQLEALADALLGRSHRQKPVKALLKRVIEGTRELLSLPEGYEVG
IVPGSDTGAWEMALWSLLGARRVDHLAWESFGSKWATDVVKQLKLEDPRVLEADYGSLPDLSAVDFDRDV
VFTWNGTTTGVRVPVARWIGADREGLTICDATSAAFALPLDWSKLDVYTFSWQKVLGGEGGHGMAILSPR
AVERLESYTPARPIPKFFRLTKGGKAIENSFKGQTINTPSMLTVEDYLDQLDWANSIGGLDALIARTAAN
ASVLYDWAEKTPWATPLVADPATRSNTSVTLDFVDAQAAVDAAAVAKLLRENGAVDIEPYRDAPNGLRIW
CGPTVEPADVEALTPWLDWAFERLKAAL
>gnl|CDD|179534 PRK03081, sspK, small, acid-soluble spore protein K
RNKQAEFPNQNNSKFEGEPRAKSRYASKRPNGTINTHPQERMRASNQREE
>gnl|CDD|179535 PRK03092, PRK03092, ribose-phosphate diphosphokinase
LAEEVAKELGVEVTPTTAYDFANGEIYVRFEESVRGCDAFVLQSHTAPINKWLMEQLIMIDALKRASAKR
ITVVLPFYPYARQDKKHRGREPISARLVADLFKTAGADRIMTVDLHTAQIQGFFDGPVDHLFAMPLLADY
VRDKYDLDNVTVVSPDAGRVRVAEQWADRLGGAPLAFIHKTRDPTVPNQVVANRVVGDVEGRTCVLVDDM
IDTGGTIAGAVRALKEAGAKDVIIAATHGVLSGPAAERLKNCGAREVVVTDTLPIPEEKRFDKLTVLSIA
PLLARAIREVFEDGSVTSLFDGLA
>gnl|CDD|179536 PRK03094, PRK03094, hypothetical protein; Provisional
MAKIGVEQSLTDVQQALKQKGYEVVQLRSEQDAQGCDCCVVTGQDSNVMGIADTSTKGSVITASGLTADE
ICQQVESRLQ
>gnl|CDD|179537 PRK03095, prsA, peptidylprolyl isomerase PrsA
MKKAMLALAATSVIALSACGTSSSDKIVTSKAGDITKDEFYEQMKTQAGKQVLNNMVMEKVLIKNYKVED
KEVDKKYDEMKKQYGDQFDTLLKQQGIKEETLKTGVRAQLAQEKAIEKTITDKELKDNYKPEIKASHILV
KDEATAKKVKEELGQGKSFEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQ
FGYHIIKVTDIKEPEKSFEQSKADIKKELVQKKAQDGEFMNDLMMKEIKKADVKVDDKDLKDLFEEKKAD
AKKEEKK
>gnl|CDD|235104 PRK03103, PRK03103, DNA polymerase IV; Reviewed
MERVILLVDMQSFYASVEKAANPELKGRPVIVSGDPERRSGVVLAACPLAKAYGVKTAERLWEAQQKCPD
LVVVKPRMQRYIDVSLQITRILEDFTDLVEPFSIDEQFLDVTGSQKLFGSPLEIAQKIQQRIMRETGVYA
RVGIGPNKLLAKMACDNFAKKNPDGLFTLDKEDVPADLWPLPVRKLFGVGSRMEKHLRRMGIRTIGQLAN
TPLERLKKRWGINGEVLWRTANGIDYSPVTPHSLDRQKAIGHQMTLPRDYRGFEEIKVVLLELCEEVCRR
ARAKGYMGRTVSVSLRGADFDWPTGFSRQMTLPEPTNLAMEVYEAACKLFHRHWDGKPVRRVGVTLSNLV
SDDVWQLSLFGDRERKRSLGYVMDDIKNRFGPTAILRASSLTEAGQAFERAAKIGGHYK
>gnl|CDD|179540 PRK03113, PRK03113, putative disulfide oxidoreductase; Provisional
MGREKKQENALLTAWGASFIATLGSLYFSEIMKFEPCVLCWYQRIFMYPFVLWLGIAVVKKDYRIASYSL
PISSIGACISLYHYAIQKIPFFSAAAASCGRVPCTGEYINWFGFVTIPFLALIAFITIAVCSFIVIKNK
>gnl|CDD|179541 PRK03114, PRK03114, DUF84 family protein
MKIAVGSKNKTKVGAVEKVWKDAEITSVSVPSGVAAQPFSDEETMQGAINRAKRALEEGEADIGIGLEGG
VMKTEGGLFLCNWGALATSDGKVFVAGGARITLPDDFLAPLEAGKELSEVMEEYVQRKDIRSHEGAIGIF
TDGYVDRTEMFVHVVKLLVGQYKYDEKQA
>gnl|CDD|179543 PRK03137, PRK03137, 1-pyrroline-5-carboxylate dehydrogenase; Provisional
MVVPYKHEPFTDFSVEENVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKA
TKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDF
LEYYARQMLKLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDT
PVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWL
KRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVG
NPEDNAYMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPV
VAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSG
TDSKAGGPDYLLLFLQAKTVSEMF
>gnl|CDD|179544 PRK03140, PRK03140, phosphatidylserine decarboxylase; Provisional
MRKTLYRLLIELTNGRFTSYLLRKFAQSRLSSILIPSYAKVYQINQDEMEKGLKEYRTLHELFTRKLKEG
KRPIDTDASSIVSPVDGVFADVGPIEDDKTFDVKGKRYSIAEMLGNEERAQRYAGGTYMVLYLSPSHYHR
IHSPISGTVTEQFVLGRKSYPVNALGLEYGKRPLSKNYRSVTEVNSDGEHMALVKVGAMFVNSIELTHER
DTVQKGEEMAYFSFGSTVVLLFEKDMIEPDQELKSGQEVRLGEKIGTRL
>gnl|CDD|179545 PRK03147, PRK03147, thiol-disulfide oxidoreductase ResA
MKKNRLLFRTIILLILLAAVGYTIYSNFFADKEKVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWG
TWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVDETELAVKNFVNRYGLTFPVAIDKGRQVIDAYGVGPLP
TTFLIDKDGKVVKVITGEMTEEQLEEYLEKIKP
>gnl|CDD|179548 PRK03174, sspH, small acid-soluble spore protein H
MNTQRAQEIAESPDMANVTYNGVPIYIQHVDEQNGTARIHPLDNPNQEQSVPLASLKEH
>gnl|CDD|235108 PRK03180, ligB, ATP-dependent DNA ligase; Reviewed
MLLADVAATSAAVAATSSRLAKVARLAELLRRADPAEVAIVVAWLSGELRQRRIGVGWATLRSLPAPAAE
PTLTVADVDAALSEIAAVAGAGSQARRAALLAALFAAATEDEQRFLRRLLTGELRQGALDGVMADAVARA
AGVPAAAVRRAAMLAGDLPAVAAAALTGGAAALARFRLEVGRPVRPMLAQTATSVAEALARLGGPAAVEA
KLDGARVQVHRDGDDVRVYTRTLDDITARLPEVVEAVRALPVRSLVLDGEAIALRPDGRPRPFQVTASRF
GRRVDVAAARATQPLSPFFFDALHLDGRDLLDAPLSERLAALDALVPAAHRVPRLVTADPAAAAAFLAAA
LAAGHEGVMVKSLDAPYAAGRRGAGWLKVKPVHTLDLVVLAAEWGSGRRTGKLSNLHLGARDPATGGFVM
LGKTFKGMTDAMLAWQTERFLELAVGRDGWTVYVRPELVVEIAFDGVQRSTRYPGGVALRFARVLRYRPD
KTPAEADTIDTVRALLPG
>gnl|CDD|235109 PRK03187, tgl, transglutaminase; Provisional
MIVISGSIVHPYDINASEPLNAEERQILSQMASSQEVYSYRSLDELSFELNLRVNIVESARELFQSGAQF
ATFRQSRCNPEYWKRTSEGGFELKPGVPPSDAIQDIFKNGKLYGFECATAIVIIFYKALLDTIGEETFNR
LFADLYLYDWHYDRDLKLITKTGGDFLPGDCVYFKNPDFNPATPEWQGENVIYLGNGLYYGHGIGIKTAE
EIIYALNERRKPGATQSAYLTDQITRLDSRYLSQFARPFSPQTSIGRDDAIVATVGSTTYVY
>gnl|CDD|235110 PRK03188, PRK03188, 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Provisional
VTVRAPAKVNLHLGVGPLRDDGYHELATVFQAVSLYDEVTVTAADVLSVEVSGEGADQVPTDESNLAWRA
AELLAEHVGRAPDVHLHIDKGIPVAGGMAGGSADAAAALVACDALWGLGLSRDELLELAAELGSDVPFAL
LGGTALGTGRGEQLAPVLARGTFHWVLAFADGGLSTPAVFRELDRLREAGDPPRLGEPDPLLAALRAGDP
AQLAPLLGNDLQAAALSLRPSLRRTLRAGEEAGALAGIVSGSGPTCAFLCADADSAVDVAAALSGAGVCR
TVRVATGPVPGARVVSGPSE
>gnl|CDD|179552 PRK03195, PRK03195, DUF721 family protein
TGSVDRPDQNPPEHLMELKGMDLVRRTLEEARAAARAQGKDVGRGRVAPVARRRVAGRRRSWSGPGPDIR
DPQPLGALARDLAKKRGWSAKVAEGTVLGQWSAVVGEQIAAHATPTALNDGVLSVSAESTAWATQLRMMQ
AQLLAKIAAAVGDGVVTSLKITGPAAPSWRKGPRHIAGRGPRDTYG
>gnl|CDD|235111 PRK03202, PRK03202, ATP-dependent 6-phosphofructokinase
MKRIGVLTSGGDAPGMNAAIRAVVRTAISEGLEVYGIYDGYAGLLEGDIVKLDLKSVSDIINRGGTILGS
ARFPEFKDEEGRAKAIENLKKLGIDALVVIGGDGSYMGAKRLTEHGIPVIGLPGTIDNDIAGTDYTIGFD
TALNTAVEAIDRLRDTASSHERVFIVEVMGRHAGDLALHAGIAGGAEVILIPEVPFDIEELCAKIKKGRE
RGKKHAIIVVAEGVMPAEELAKEIEERTGLETRVTVLGHIQRGGSPTAFDRVLASRMGAHAVELLLEGKG
GRMVGIQNNKIVHVPIEEAVENMKHPFDKDLYELAKKLSI
>gnl|CDD|179554 PRK03204, PRK03204, haloalkane dehalogenase; Provisional
MSIDFTPDPQLYPFESRWFDSSRGRIHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLG
FGLSERPSGFGYQIDEHARVIGEFVDHLGLDRYLSMGQDWGGPISMAVAVERADRVRGVVLGNTWFWPAD
TLAMKAFSRVMSSPPVQYAILRRNFFVERLIPAGTEHRPSSAVMAHYRAVQPNAAARRGVAEMPKQILAA
RPLLARLAREVPATLGTKPTLLVWGMKDVAFRPKTILPRLRATFPDHVLVELPNAKHFIQEDAPDRIAAA
IIERFG
>gnl|CDD|235112 PRK03244, argD, acetylornithine transaminase
TKTMTTTAELLQRWQAVMMNNYGTPPLALVRGEGAVVWDVDGKEYLDLLGGIAVNALGHAHPAVVEAVTR
QLATLGHVSNLFATEPQIALAERLVELLGAPEGGRVFFCNSGAEANEAAFKLARLTGRTKIVAAEGGFHG
RTMGALALTGQPAKRAPFEPLPGGVEHVPYGDVDALAAAVDDDTAAVFLEPIQGEAGVVPPPAGYLAAAR
EITDRHGALLVLDEVQTGIGRTGAWFAHQHDGVTPDVVTLAKGLGGGLPIGACLAFGPAADLLTPGLHGS
TFGGNPVACAAALAVLDTIASEGLLENAERLGEQLRAGIEALGHPLVDHVRGRGLLLGIVLTAPVAKAVE
AAAREAGFLVNAVAPDVIRLAPPLIITDAQVDAFVAALPAILDAAAAA
>gnl|CDD|235114 PRK03298, PRK03298, endonuclease NucS
MRLVIARCSVDYVGRLTAHLPSARRLLLVKADGSVSVHADDRAYKPLNWMSPPCTLTEEPPGGVEEVWRV
ENKAGEQLRITIEEILHDSSHDLGVDPGLVKDGVEAHLQELLAEHIETLGEGYTLVRREYPTAIGPVDLL
CRDADGGTVAVEIKRRGEIDGVEQLTRYLELLNRDPLLAPVRGVFAAQEIKPQARTLAEDRGIRCVTLDY
DALRGIDDDELRLF
>gnl|CDD|235115 PRK03317, PRK03317, histidinol-phosphate aminotransferase; Provisional
PSVTLDDLPLRDDLRGKSPYGAPQLDVPVRLNTNENPYPPSPALVADIAEAVAEAAAGLNRYPDRDAVAL
RADLAAYLTAQTGVGLTVENVWAANGSNEILQQLLQAFGGPGRTALGFVPSYSMHPIIARGTHTEWVEGP
RAADFTLDVDAAVAAIAEHRPDVVFLTSPNNPTGTALPLDDVEAILDAAPGIVVVDEAYAEFRRSGTPSA
LTLLPEYPRLVVSRTMSKAFAFAGGRLGYLAAAPAVVDALRLVRLPYHLSAVTQAAARAALRHADELLAS
VAALRAERDRVVAWLRELGLRVAPSDANFVLFGRFADRHAVWQGLLDRGVLIRDVGIPGWLRVTIGTPEE
NDAFLAALAEVLATELAA
>gnl|CDD|179559 PRK03321, PRK03321, putative aminotransferase; Provisional
MTARLRPDLAGIPAYVPGKTVPGAIKLSSNETPFGPLPSVRAAIARAAAGVNRYPDMGAVELRAALAEHL
GVPPEHVAVGCGSVALCQQLVQATAGPGDEVIFAWRSFEAYPILVQVAGATPVQVPLTPDHTHDLDAMAA
AITDRTRLIFVCNPNNPTGTVVTPAELARFLDAVPADVLVVLDEAYVEYVRDDDVPDGLELVRDHPNVVV
LRTFSKAYGLAGLRVGYAVGHPEVIAALRKVAVPFSVNSLAQAAAIASLAAEDELLERVDAVVAERDRVR
AALRAAGWTVPPSQANFVWLPLGERTADFAAAAAEAGVVVRPFAGEGVRVTIGAPEENDAFLRAARAWRA
GL
>gnl|CDD|179560 PRK03333, coaE, dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional
MLRIGLTGGIGAGKSTVAARLAELGAVVVDADVLAREVVEPGTEGLAALVAAFGDDILLADGALDRPALA
AKAFADDEARAVLNGIVHPLVGARRAELIAAAPEDAVVVEDIPLLVESGMAPLFHLVVVVDADVEVRVRR
LVEQRGMAEADARARIAAQASDEQRRAVADVWLDNSGTPDELVEAVRALWADRLLPFAHNLRARRRAARA
PPRLVPADPSWPAQAQRIVARLKTAAGHKALRVDHIGSTAVPGLDAKDVIDIQVTVESLAVADELAEPLA
AAGFPRLPGITQDTPKPDDPDPALWGKRLHASADPGRPVNLHVRVDGWPGQRFALLFRDWLRADPAARAE
YLAVKRRAARRADGDTAAYADAKEPWFLDAYPRAWEWADATGWRP
>gnl|CDD|235116 PRK03341, PRK03341, arginine repressor; Provisional
AAPTAGPTVPATRAARQARIVAILSRQSVRSQAELAALLADEGIEVTQATLSRDLDELGAVKLRGADGGL
GVYVVPEEGGPRRGVAGGTERLRRLLGELLVSADASANLAVLRTPPGAAQYLASAIDRAALPEVVGTIAG
DDTVLVIARDPMTGAELAARLLRLAERR
>gnl|CDD|235117 PRK03343, PRK03343, transaldolase; Validated
MMNPLQALSALGQSIWLDDLSRDRLTSGNLARLIDEKGVVGVTSNPAIFQKAIAGGDAYDAQIAELAAAG
ADVEEAYEELTTADVRNACDVLRPVYEATGGVDGRVSIEVSPRLAHDTEATIAEARRLWAAVDRPNLMIK
IPATPEGLPAIEALIAEGISVNVTLIFSVERYRAVADAYLRGLEKRLAAGHDLSKIHSVASFFVSRVDTE
VDKRLEAIGTDEALALRGKAAIANARLAYQAYEEVFASPRWAALAAAGARPQRPLWASTGTKNPAYSDTL
YVDELVAPDTVNTMPEATLDAFADHGEVADTLTGDYEEAQAVLAALAALGIDLDDVTAVLEEEGVDKFEA
SWNELLASLEAKLDALAA
>gnl|CDD|235118 PRK03348, PRK03348, DNA polymerase IV; Provisional
MRAQRWVLHLDMDAFFASVEQLTRPTLRGRPVLVGGLGGRGVVAGASYEARVFGARSAMPMHQARRLVGN
GAVVLPPRFVVYRAASRRVFDTLRELSPVVEQLSFDEAFVEPAELAGASAEEVEAFAERLRARVREETGL
PASVGAGSGKQIAKIASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGPVTEEKLHRLGIETIGDLAAL
SEAEVANLLGATVGPALHRLARGIDDRPVAERAEAKQISAESTFAVDLTTRAQLREAIERIAEHAHRRLL
KDGRGARTVTVKLRKSDFSTLTRSATLPYATDDAAVLAATARRLLLDPDEIGPIRLVGVGFSGLSDVRQE
SLFPELDLARETAPAEEVETESAAGPSDSPAAARVEAPAWRAGQDVAHPEYGHGWVQGAGHGVVTVRFET
RTTGPGPVRTFPVDDPDLTPADPLDSLDWPDYVA
>gnl|CDD|179564 PRK03352, PRK03352, DNA polymerase IV; Validated
TAMPRWVLHVDLDQFIAAVELLRRPELAGLPVIVGGNGDPTEPRKVVTCASYEARAFGVRAGMPLRTAAR
RCPDAVFLPSDPAAYDAASEEVMATLRDLGVPVEVWGWDEAFLGVDTDDPEALAEEIRAAVLERTGLSCS
VGIGDNKLRAKIATGFAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTAKRLAALGITTVADLAAADPA
ELAATFGPTTGPWLLLLARGGGDTEVSAEPWVPRSRSREVTFPQDLTDRAEVESAVRELARRVLDEVVAE
GRPVTRVAVKVRTATFYTRTKIRKLPEPTTDPDVIEAAALDVLDRFELDRPVRLLGVRLELAMPDE
>gnl|CDD|179566 PRK03354, PRK03354, crotonobetainyl-CoA dehydrogenase; Validated
MDFNLNDEQELFVAGIRELMASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTL
AAVWMELGRLGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTY
TRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLEKLGLRMDSCCEI
TFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQ
EKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRF
WRDLRVDRVSGGSDEMQILTLGRAVLKQYR
>gnl|CDD|179567 PRK03355, PRK03355, glycerol-3-phosphate 1-O-acyltransferase
MTKPAADAAAVLTAEDTLVLASTSSPVEMELLMDWLAQQRARHPDSKPDVLKLPPRDAPPAALAALVESL
EADEDRLVVPVRVVWLPPADPSRAVKVAALLSGRDPYHPGQRQQRRILRRDPRRARVLAGEPAKVSELRQ
RWRDTTVGENSRDFARFVRRRAALALERAERRILGPQYKVPRLVKPEILASARFRAGLAKIAAKLGRPPG
ATVREAGKMLDELVAGWSRVSVDLVSVLGRLFSRGFDPEIDYDEYELAALRALLEEHPAVLLFSHRSYID
GLVVPVAMQENRLPPVHVFGGINLSFGPMGPIMRRSGMIFIRRNIGDDPLYKYVLREYVGYLVEKRFNLS
WYIEGTRSRTGKLLPPKLGLLSYVADAYLDGRSDDVLLQPVSISFDQLHEIGEYAAEARGGEKTPEGLRW
LYNYIKAQGERNYGKIYVRFGEPVSMRQYLGAPHGPLTQDPDAKRLALQKMAFEVAWRINQVTPVTATSL
VSLLLLGTRGRALTLDELHHTLQDSLDYLERRQLPVSTSALRLRDPEGVRAALDALSNGGPVTRVDSGRE
PVWYIAPDDHLVAAFYRNSVIHAFLERAIVELALAAAAHVDEGDRLAAFWDQAMRLRDLLKFEFFFADSD
AFRANLRAEMAWIDPDWEDRLAAGGDEIDALLRAKRPLMAHAMLRPFFEAYEVVADVLRDAPPDTIDEKE
LTALALGLGRQYVLQGRVRSSESVSTLLFATARQLARDQGLLEPAPDLAERRVAFRAELRGILRDFDYVE
RIAREQFDAREGK
>gnl|CDD|179568 PRK03356, PRK03356, L-carnitine/gamma-butyrobetaine antiport BCCT transporter
MKNEKKKTGIEPKVFFPPLIIVGILCWLTVRDLDAANVVINAVFSYVTNVWGWAFEWYMVVMLFGWFWLV
FGPYAKKRLGDEKPEFSTASWIFMMFASCTSAAVLFWGSIEIYYYISTPPFGLEPNSTGAKELGLAYSLF
HWGPLPWATYSFLSVAFGYFFFVRKMDVIRPSSTLVPLVGEKHAKGLFGTIVDNFYLVALIFAMGTSLGL
ATPLVTECMQWLFGIPHTLQLDAIIITCWIILNAICVACGLQKGVRIASDVRSYLSFLMLGWVFIVGGTS
FIMNYFTDSVGMLLMYLPRMLFYTDPIGKGGFPQGWTVFYWAWWVIYAIQMSIFLARISRGRTVRELCFG
MVLGLTASTWILWTVLGSNTLLLMDKNIINIPNLIEQYGVARAIIETWAALPLSTATMWGFFILCFIATV
TLINACSYTLAMSTCREVRDGEEPPLLVRIGWSILVGIIGIVLLALGGLKPIQTAIIAGGCPLFFVNIMV
TLSFIKDAKQNWKD
>gnl|CDD|179569 PRK03359, PRK03359, putative electron transfer flavoprotein FixA; Reviewed
MKIITCYKCVPDEQDIAVNNADGSLDFSKADAKISQYDLNAIEAACQLKQQAAEAQVTALSVGGKALTNA
KGRKDVLSRGPDELIVVIDDQFEQALPQQTASALAAAAQKAGFDLILCGDGSSDLYAQQVGLLVGEILNI
PAINGVSKIISLTDDTLTVERELEDEVETLSIPLPAVIAVSTDINSPQIPSMKAILGAAKKPVQVWSAAD
IGFNAEPAWSEQQVAAPKQRERQRIVIEGDGEEQIAAFAENLRKII
>gnl|CDD|235120 PRK03363, fixB, electron transfer flavoprotein subunit alpha/FixB family protein
MNTFSQVWVFSDTPSRLPELMNGAQALANQINAFVLNDADGAQAIQLGANHVWKLSGKPDDRMIEDYAGV
MADTIRQHGADGLVLLPNTRRGKLLAAKLGYRLKAAVSNDASTVSVQDGKATVKHMVYGGLAIGEERIAT
PYAVLTISSGTFDAAQPDASRTGETHTVEWQAPAVAITRTATQARQSNSVDLDKARLVVSVGRGIGSKEN
IALAEQLCKAIGAELACSRPVAENEKWMEHERYVGISNLMLKPELYLAVGISGQIQHMVGANASQTIFAI
NKDKNAPIFQYADYGIVGDAVKILPALTAALAR
>gnl|CDD|179572 PRK03371, pdxA, D-threonate 4-phosphate dehydrogenase
MTKIIAVTMGDPAGIGPEIIIKSLSEGGLNGAPLVVVGCLATLRRILAKGITPQVELRAIERVAEARFAP
GIINVIDEPLAQPEALEPGVVQAQAGDLAYRCVKRATELALRGEVQAIATAPLNKEALHLAGHNYPGHTE
LLATLTHSRDYAMVLYTDKLKVIHVSTHIALRKFLDTLNTARVETVIGIADTFLKRVGYVKPRIAVAGVN
PHAGENGLFGDEEIRIVTPAIEAMRAKGMDVYGPCPPDTVFLQAYEGQYDMVVAMYHDQGHIPLKLLGFY
DGVNITAGLPFIRTSADHGTAFDIAWTGKAKSESMAVSIKLAMQLA
>gnl|CDD|235121 PRK03372, ppnK, inorganic polyphosphate/ATP-NAD kinase; Provisional
DMTASRRVLLVAHTGRDEATEAARRVAKQLGDAGIGVRVLDAEAVDLGATHPAPDDFRAMEVVDADPDAA
DGCELVLVLGGDGTILRAAELARAADVPVLGVNLGHVGFLAEAEAEDLDEAVERVVDRDYRVEERMTLDV
TVRVGGEIVWRGWALNEASLEKADREGMLEVVLEVDGRPVSSFGCDGVLVSTPTGSTAYAFSAGGPVVWP
DLEALLVVPLNAHALFARPLVVSPTSTVAVEILADTSDAVLWCDGRRSVDLPPGARVEVRRGATPVRLAR
LDSAPFTDRLVRKFRLPVTGWRGPAP
>gnl|CDD|235122 PRK03378, ppnK, inorganic polyphosphate/ATP-NAD kinase; Provisional
MNNHFKCIGIVGHPRHPTALTTHEMLYHWLTSKGYEVIVEQQIAHELQLKNVKTGTLAEIGQQADLAIVV
GGDGNMLGAARVLARYDIKVIGINRGNLGFLTDLDPDNALQQLSDVLEGHYISEKRFLLEAQVCRHGQQK
RISTAINEVVLHPGKVAHMIEFEVYIDDNFAFSQRSDGLIISTPTGSTAYSLSAGGPILTPSLDAITLVP
MFPHTLSARPLVIDSSSTIRLKFSPNRSDLEISCDSQIALPIQPGEEVLIRRSDYHLNLIHPKDYSYFNT
LRTKLGWSKKLF
>gnl|CDD|179575 PRK03379, PRK03379, vitamin B12-transporter protein BtuF; Provisional
RALVALLFLAPLWLNAAPRVITLSPANTELAFAAGITPVGVSSYSDYPPQAKKIEQVATWQGMNLERIVA
LKPDLVLAWRGGNAERQVDQLASLGIKVMWVDATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAAL
KAQYADKPKKRVFLQFGTNPLFTSGKHSIQSQVLSLCGGENIFADSRVPWPQVSREQVLARKPQAIVITG
GPDQIPKIKQFWGPQLKIPVIPLNSDWFERASPRIILAAQQLCNALSQVD
>gnl|CDD|235123 PRK03381, PRK03381, PII uridylyl-transferase; Provisional
PMTAGSPAAAGDLAAARRQLLSGGHLDGAALRAALADLHEFWLAGLAAEAGIADGSGVALVAVGGLGRRE
LLPYSDLDLVLLHDGRPADDVAEVADRLWYPLWDAGIRLDHSVRTVPEALKVAGSDLKAALGLLDARHIA
GDADLSALLIGGVRRQWRNGARRRLPELVELTRARWERSGEIAHLAEPDLKEGRGGLRDVQLLRALAAAQ
LADAPGGGLDAAHRRLLDVRTELHRVSGRGRDRLLAQEADEVAAALGLGDRFDLARALSDAARTISYAVD
VGWRTAANALPRRGLSALRRRPVRRPLDEGVVEHAGEVVLARDARPARDPGLVLRVAAAAATTGLPIAAA
TLSRLAASAPPLPTPWPAEARDDLLVLLGAGPAAVAVIEALDRTGLWGRLLPEWEAVRDLPPRDPVHRWT
VDRHLVETAVRAAALTRRVARPDLLLLGALLHDIGKGRGGDHSVVGAELARQIGARLGLSPADVALLSAL
VRHHLLLPETATRRDLDDPATIEAVAEALGGDPVLLELLHALTEADSLATGPGVWSDWKASLVGDLVRRC
RAVLAGEPLPEPEPLDPAQLALAADGGVHVEIAPADPHMVEVTVVAPDRRGLLSKAAGVLALHRLRVRSA
SVRSHDGVAVLEFVVSPRFGSPPDAALLRQDLRRALDGDLDVLARLAAREAAAAAVPVRRPAAPPRVLWL
DGASPDATVLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAGGPLADARAAVEQ
AVLA
>gnl|CDD|235125 PRK03430, PRK03430, hypothetical protein; Validated
MFDVLMYLFETYIHNEAELRVDQDKLEDDLTDAGFHREDIYNALLWLEKLADLQEGLAEPMQLASDPLSM
RIYTPEECERLDASCRGFLLFLEQIQVLNLETREMVIDRVMALDTAEFDLEDLKWVILMVLFNIPGCENA
YQQMEELLFEVNEGMLH
>gnl|CDD|179579 PRK03437, PRK03437, 3-isopropylmalate dehydrogenase; Provisional
MAKTMKLAVIPGDGIGPEVVAEALKVLDAVAAGGPGVETTEYDLGARRYLRTGETLPDSVLAELRQHDAI
LLGAIGDPSVPSGVLERGLLLKLRFALDHYVNLRPSKLYPGVTSPLAGPGDIDFVVVREGTEGPYTGNGG
ALRVGTPHEVATEVSVNTAFGVERVVRDAFERAQKRPRKHLTLVHKTNVLTFAGDLWQRTVDEVAAEYPD
VTVDYQHVDAATIFMVTDPSRFDVIVTDNLFGDIITDLAAAVTGGIGLAASGNINPTGTNPSMFEPVHGS
APDIAGQGIADPTAAILSVALLLDHLGEEDAAARIEAAVEADLAERGKMGRSTAEVGDRIAARL
>gnl|CDD|179580 PRK03449, PRK03449, putative inner membrane protein translocase component YidC; Provisional
MLDFIYYPVSAILWFWHKLFSFVLGPDNGFAWALSVMFLVFTLRALLYKPFVRQIRTTRKMQELQPQIKA
LQKKYGNDRQKMALEMQKLQKEHGFNPILGCLPMLAQIPVFLGLFHVLRSFNRTGTGFGQLGMSVEENRN
TPNYVFSAEDVQSFLDARLFGAPLSAYITMPRSGLDAFVDFTRTNIILVGVPLMIIAGVATHFNSRASVA
RQSAEAAANPQTAMMNKLALWVFPLGVLVGGPFLPLAILLYWVSNNIWTFGQQHYVFGKIDKEEEAKKQA
KAERRAANAPKPGAKPKRSKKKAP
>gnl|CDD|235126 PRK03459, rnpA, ribonuclease P; Reviewed
MLPEQHKLRSSMQFRTTVRKGRRAGRRTVVVHLFDSAEAGEVASFGGPRFGLVVSKAVGNAVIRHRVSRR
LRHICADIVDQVPETHHVVIRALPGAATASSAELERDVRAGLGKLNRVRTVK
>gnl|CDD|235127 PRK03467, PRK03467, hypothetical protein; Provisional
MNNMDTLTAISRWLAKQHVVTLCVGQEGELWCANCFYVFDAQKVAFYLLTEEKTRHGQMMGPNAQVAGTV
NGQPKTVALIRGVQFKGEIRRLEGEESDAARKRYNRRFPVARALSAPVWELRLDEIKMTDNTLGFGKKLH
WLRD
>gnl|CDD|179583 PRK03482, PRK03482, phosphoglycerate mutase GpmB
MLQVYLVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVAERAKELGITHIISSDLGRTRRTAEIIAQAC
GCDIIFDPRLRELNMGVLEKRHIDSLTEEEEGWRRQLVNGTVDGRIPEGESMQELSDRMHAALESCLELP
QGSRPLLVSHGIALGCLVSTILGLPAWAERRLRLRNCSISRVDYQESPWLASGWVVETAGDVSHLDAPAL
DELQR
>gnl|CDD|179584 PRK03501, ppnK, NAD kinase
DRRNLFFFYKRDKELVEKVKPLKKIAEEYGFTVVDHPKNANIIVSIGGDGTFLQAVRKTGFREDCLYAGI
STKDQLGFYCDFHIDDLDKMIQAITKEEIEVRKYPTIEVTVDGSTSFYCLNEFSIRSSIIKTFVIDVYID
DLHFETFRGDGMVVSTPTGSTAYNKSVRGAVVDPLIPCFQVSELASLNNNTYRTLGSPFILSHERKLTLK
IVQDGNDYPIIGMDNEALSIKHVEKIDIRLSDKQIKTVKLKDNSFWEKVKRTFL
>gnl|CDD|179586 PRK03512, PRK03512, thiamine phosphate synthase
MYQPDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFIND
YWRLAIKHQAYGVHLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMP
SAPQGLAQLARHVERLADYPTVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGD
E
>gnl|CDD|179587 PRK03515, PRK03515, ornithine carbamoyltransferase subunit I; Provisional
MNQFYQRHFLRLLDFTPAELNSLLQLAAKLKADKKNGKEEQKLTGKNIALIFEKDSTRTRCSFEVAAYDQ
GARVTYLGPSGSQIGHKESIKDTARVLGRMYDGIQYRGYGQEIVETLAEYAGVPVWNGLTNEFHPTQLLA
DLLTMQEHLPGKAFNEMTLAYAGDARNNMGNSLLEAAALTGLDLRLVAPKACWPEAALVTECRALAQKNG
GNITLTEDIAEGVKGADFIYTDVWVSMGEPKEVWAERIALLRPYQVNSKMMQLTGNPQVKFLHCLPAFHD
DQTTLGKKMAEEYGLHGGMEVTDEVFESAHSIVFDQAENRLHTIKAVMVATLSKDL
>gnl|CDD|235128 PRK03522, rumB, 23S rRNA (uracil(747)-C(5))-methyltransferase RlmC
MVVSGSVERPLLGILHRDGTPVDLCDCPLYPASFAPVFAALKPFIARAGLTPYNVARKRGELKYILLTES
QSDGELMLRFVLRSETKLARLRRALPWLQAQLPQLKVISVNIQPVHMAILEGEEEIFLTEQQALPERFNG
VPLFIRPQSFFQTNPAVAAQLYATARDWVRELPPRSMWDLFCGVGGFGLHCATPGMQLTGIEISAEAIAC
AKQSAAELGLTNVQFQALDSTQFATAQGEVPDLVLVNPPRRGIGKELCDYLSQMAPRFILYSSCNAQTMA
KDLAHLPGYRIERVQLFDMFPHTAHYEVLTLLVRQ
>gnl|CDD|179589 PRK03525, PRK03525, L-carnitine CoA-transferase
MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALS
LNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWEHNPKLVIAHLSGFGQYGTEEYTNLPAY
NTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAALAALHKARETGKGESIDIAMYEVMLRMGQY
FMMDYFNGGEMCPRMTKGKDPYYAGCGLYKCADGYIVMELVGITQIKECFKDIGLAHLLGTPEIPEGTQL
IHRIECPYGPLVEEKLDAWLAAHTIAEVEARFAELNIACAKVLTIPELESNPQYVARESITQWQTMDGRT
CKGPNIMPKFKNNPGQIWRGMPSHGMDTAAILKNIGYSEEDIQELVAKGLAKVED
>gnl|CDD|235129 PRK03537, PRK03537, molybdate ABC transporter substrate-binding protein
MAHPQALLAAGRAEQVVPFARNRLCAIARADVMLTSDNLLDLLLDPDIRLGTSTPGADPSGDYAWQLFDR
AEALHAGAGEALRTKALQLVGGPNSAPIPAGRNAAEWLIENKQADIFIGYASNAPLAQREVPSLQVVDLP
EPLAVGAEYGLAILKDASPQAKRLADFLLSPKGQAILAQYGFSPPPKM
>gnl|CDD|179591 PRK03545, PRK03545, putative arabinose transporter; Provisional
TVSRKVAWLRVVTLALAAFIFNTTEFVPVGLLSDIAQSFHMQTAQVGLMLTIYAWVVALMSLPLMLLTSN
VERRKLLIGLFVLFIASHVLSALAWNFTVLLISRIGIAFAHAIFWSITASLAIRVAPAGKKAQALSLLAT
GTALAMVLGLPLGRVIGQYLGWRTTFLAIGGGALITLLLLIKLLPLLPSEHSGSLKSLPLLFRRPALVSL
YLLTVVVVTAHFTAYSYIEPFVQQVAGLSENFATLLLLLFGGAGIIGSVLFSRLGNRHPSGFLLIAIALL
LVCLLLLLPAANSEWHLSVLSIFWGIAIMCIGLAMQVKVLKLAPDATDVAMALFSGIFNIGIGAGALLGN
QVSLHLGLSSIGYVGAALALAALVWSILIFRRFPVTLEEQ
>gnl|CDD|179592 PRK03554, tatA, Sec-independent protein translocase subunit TatA
MGGISIWQLLIIAVIVVLLFGTKKLGSIGSDLGASIKGFKKAMSDDEPKQDKTSQDADFTAKTIADKQAD
TNQEQAKTEDAKRHDKEQV
>gnl|CDD|235130 PRK03557, PRK03557, CDF family zinc transporter ZitB
MAHSHSHTSSHLPEDNNARRLLYAFGVTAGFMLVEVIGGFLSGSLALLADAGHMLTDAAALLFALLAVQF
SRRPPTIRHTFGWLRLTTLAAFVNAIALVVITILIVWEAIERFRTPRPVAGGMMMAIAVAGLLANILSFW
LLHHGSEEKNLNVRAAALHVLGDLLGSVGAIIAALIIIWTGWTPADPILSILVSVLVLRSAWRLLKESVN
ELLEGAPVSLDIAELKRRLCREIPEVRNVHHVHVWMVGEKPVMTLHVQVIPPHDHDALLDRIQDYLMHHY
QIEHATIQMEYQPCHGPDCHLNQGVSGHSHHH
>gnl|CDD|235131 PRK03562, PRK03562, glutathione-regulated potassium-efflux system protein KefC; Provisional
MMDSHTLIQALIYLGAAVLIVPIAVRLGLGSVLGYLIAGCIIGPWGLRLVTDVESILHFAEFGVVLMLFV
IGLELDPQRLWKLRRSIFGGGALQMVACGGLLGLFCMLLGLRWQVALLIGLGLALSSTAIAMQAMNERNL
MVTQMGRSAFAILLFQDIAAIPLVAMIPLLAASGASTTLGAFALSALKVAGALALVVLGGRYVTRPALRF
VARSGLREVFTAVALFLVFGFGLLMEEVGLSMALGAFLAGVLLASSEYRHALESDIEPFKGLLLGLFFIA
VGMSIDFGTLLENPLRILILLLGFLAIKIAMLWLLARPLGVPRKQRRWFAVLLGQGGEFAFVVFGAAQMA
NVLEPEWAKLLTLAVALSMAATPLLLVLLDRLEQSRTEEAREADEIDEQQPRVIIAGFGRFGQIVGRLLL
SSGVKMTVLDHDPDHIETLRKFGMKVFYGDATRMDLLESAGAAKAEVLINAIDDPQTSLQLVELVKEHFP
HLQIIARARDVDHYIRLRQAGVEKPERETFEGALKSGRLVLESLGLGPYEARERADRFRRHNLQMVEEMA
PHENDTKKRAAVAKQTSAMLSEIITEDREHLSLIQRHGWQGTEEGKHTGNMADEPETKPSS
>gnl|CDD|179595 PRK03564, PRK03564, formate dehydrogenase accessory protein FdhE; Provisional
MSIRIIPQDELGSSEKRTADMIPPLLFANLKNLYNRRAERLRQLAENNPLGDYLRFAALIAEAQEVVLYD
HPLEMDLTARIKEAAAQGKPPLDIHVFPRDKHWQKLLMALIAELKPEASGPALAVIENLEKASTQELEDM
ASALLASDFSSVSSDKAPFIWAALSLYWAQMAQQIPGKARAEYGEQRQFCPVCGSMPVSSVVQIGTTQGL
RYLHCNLCESEWHVVRVKCSNCEQSGKLHYWSLDSEQAAVKAESCGDCGTYLKILYQEKDPKVEAVADDL
ASLVLDARMEQEGFARSSINPFLFPGEGE
>gnl|CDD|179596 PRK03573, PRK03573, transcriptional regulator SlyA; Provisional
MESPLGSDLARLVRIWRALIDHRLKPLELTQTHWVTLHNIHQLPPEQSQIQLAKAIGIEQPSLVRTLDQL
EEKGLISRQTCASDRRAKRIKLTEKAEPLISEVEAVINKTRAEILHGISAEEIEQLITLIAKLEKNIIEL
QSKG
>gnl|CDD|235132 PRK03577, PRK03577, acid shock protein
MKKVLALVVAAAMGLSSAAFAAETATTAAPAATTTTAAPAKTTHHHKKQHKKAPEQKAQAAKKHHKNKKE
QKAPEQKAQAAKKHAKKHSHKTAAKPAAQPAA
>gnl|CDD|235133 PRK03578, hscB, Fe-S protein assembly co-chaperone HscB
MVSLKDDHFSLFGLPARFALDEAALDAAYRTVQAQVHPDRFAAAGDAEKRVAMQWATRANEAYQTLRDPL
KRARYLLHLRGVDVQAENNTAMPPAFLMQQMEWREAIEDARAARDVDALDALLAELRDERRERYAELGAL
LDSRGDDQAAAEAVRQLMFIEKLAQEIGAAIERLED
>gnl|CDD|179599 PRK03580, PRK03580, crotonobetainyl-CoA hydratase
MSESLHTTRNGSILEITLDRPKANAIDAKTSFAMGEVFLNFRDDPELRVAIITGAGEKFFSAGWDLKAAA
EGEAPDADFGPGGFAGLTEIFDLDKPVIAAVNGYAFGGGFELALAADFIVCADNASFALPEAKLGIVPDS
GGVLRLPKRLPPAIANEMVMTGRRMDAEEALRWGIVNRVVPQAELMDRARELAQQLVNSAPLAIAALKEI
YRETSEMPVEEAYRYIRSGVLKHYPSVLHSEDALEGPRAFAEKRDPVWKGR
>gnl|CDD|235134 PRK03584, PRK03584, acetoacetate--CoA ligase
MGDPLWTPSAERIAASRMTAFIRWLAARRGLSFDDYAALWRWSVEDLEAFWQSVWDFFGVIGSTPYTVVL
AGRRMPGARWFPGARLNYAENLLRHRRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGD
RVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRRAKVA
ELRAALPSLEHVVVVPYLGPAAAAAALPGALLWEDFLAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKC
IVHGHGGILLEHLKELGLHCDLGPGDRFFWYTTCGWMMWNWLVSGLLVGATLVLYDGSPFYPDPNVLWDL
AAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKADVWLASISGGT
DICSCFVGGNPLLPVYRGEIQCRGLGMAVEAWDEDGRPVVGEVGELVCTKPFPSMPLGFWNDPDGSRYRD
AYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGD
VRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVELPVKKLLHGRPVKK
AVNRDALANPEALDWFADLAELRAA
>gnl|CDD|235135 PRK03592, PRK03592, haloalkane dehalogenase; Provisional
FGVEPPGEMRRVEVLGSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKP
DIDYTFADHARYLDAWFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPAV
RELFQALRSPGEGEEMVLEENVFIERVLPGSILRPLSDEEMAVYRRPFPTPESRRPTLSWPRELPIDGEP
ADVVALVEEYAQWLATSDVPKLLINAEPGAILTTGAIRDWCRSWPNQLEITVFGAGLHFAQEDSPEEIGA
AIAAWLRRLRLAVSA
>gnl|CDD|235136 PRK03598, PRK03598, putative efflux pump membrane fusion protein; Provisional
MKKKVVIGLAVVVLAAAVAGGWWWYQSRQDNGLTLYGNVDIRTVNLGFRVGGRLASLAVDEGDAVKAGQV
LGELDAAPYENALMQAKANVSVAQAQLDLMLAGYRDEEIAQARAAVKQAQAAYDYAQNFYNRQQGLWKSR
TISANDLENARSSRDQAQATLKSAQDKLSQYREGNRPQDIAQAKASLAQAQAALAQAELNLQDTELIAPS
DGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVS
PTAEFTPKTVETPDLRTDLVYRLRIVVTDADDALRQGMPVTVRFADEAGHE
>gnl|CDD|235137 PRK03601, PRK03601, HTH-type transcriptional regulator HdfR
MDTELLKTFLEVSRTRHFGRAAESLYLTQSAVSFRIRQLENQLGVNLFTRHRNNIRLTAAGERLLPYAET
LMNTWQAAKKEVAHTSQHNELSIGASASLWECMLTPWLGRLYQNQEALQFEARIAQRQSLVKQLHERQLD
LLITTEAPKMDEFSSQLLGHFTLALYTSAPSKKKSELNYIRLEWGADFQQHEAGLIGADEVPILTTSSAE
LARQLLATLNGCAFLPVHWAKEKGGLHTVPDSTTLSRPLYAIWLQNSDKQALIRDLLKTPVLDEV
>gnl|CDD|235138 PRK03604, moaC, bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
THLDEEGRVRMVDVSGKPGTLRTARASGIIVTSPETIELLRQGDLPKGDVLTTAKIAGIQAAKRTSELIP
LCHPLPLSWVDVEFEIEDDRIRIEATVKTIGKTGVEMEALTAVSVAALTIYDMLKPVDKALEIGGIRLLE
KTGGKSGHKRRFRPRTSAAVLVLSDSIAAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAA
WIAEGYALIITTGGTGLGPRDVTPEALAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVA
LPGSPGGASDALAVLLPALFHAFAMVKGEGHH
>gnl|CDD|179606 PRK03606, PRK03606, ureidoglycolate lyase
MRTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGGRALISIFRAQPRALPLEI
RMLERHPLGSQAFIPLNGRPFLVVVAPDGDGDPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVV
DRGGPGDNLEEHFFPEDELIIA
>gnl|CDD|179607 PRK03609, umuC, translesion error-prone DNA polymerase V subunit UmuC
MFALCDVNSFYASCETVFRPDLRGKPVVVLSNNDGCVIARSAEAKALGIKMGDPWFKQKDLFRRCGVVCF
SSNYELYADMSNRVMSTLEELSPRVEIYSIDEAFCDLTGVRNCRDLTDFGREIRATVLQRTHLTVGVGIA
QTKTLAKLANHAAKKWQRQTGGVVDLSNLERQRKLLSLQPVEEVWGVGRRISKKLNAMGIKTALDLADTN
IRFIRKHFNVVLERTVRELRGEPCLSLEEFAPTKQEIVCSRSFGERITDYESMRQAICSYAARAAEKLRG
EHQYCRFISTFVKTSPFALNEPYYGNSASVKLLTPTQDSRDIIAAATRALDAIWRDGHRYQKAGVMLGDF
FSQGVAQLNLFDDNAPRPGSEQLMKVLDTLNAKSGKGTLYFAGQGIAQQWQMKREMLSPRYTTRWSDLLR
VK
>gnl|CDD|235139 PRK03612, PRK03612, polyamine aminopropyltransferase
STPQAAAPSPLSPRDRALLLAAVFVCAACGLVYELLLGTLASYLLGDSVTQFSTVIGLMLFAMGVGALLS
KYLLRDAAAGFVAVELLLALLGGLSALILYAAFAFQGLSRLLLYVLVLLIGLLIGMEIPLLMRILQRIRD
QHLGHNVATVLAADYLGALVGGLAFPFLLLPRLGLIRTAALTGSLNLLAALVFLWLFRHELRRRKLLLAA
AALVLGLLAAGFVLADRIETTAEQLLYGDPVVYAEQTPYQRIVVTRRGNGRGPDLRLYLNGRLQFSSRDE
YRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYPDVEQVTLVDLDPAMTELARTSPALRALNGGA
LDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPSNPALGKLYSVEFYRLLKRRLAPDGLLVVQSTSPYF
APKAFWSIEATLEAAGLATTPYHVNVPSFGEWGFVLAGAGARPPLAVPTELPVPLRFLDPALLAAAFVFP
KDMRRREVEPNTLNNPVLVRYYREEWREYLR
>gnl|CDD|235140 PRK03619, PRK03619, phosphoribosylformylglycinamidine synthase subunit PurQ
MKVAVIVFPGSNCDRDMARALRDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMK
AVKEFAEKGKPVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPI
AHGEGNYYADEETLKRLEGNGQVVFRYCDENPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGL
KLFESLLKS
>gnl|CDD|235141 PRK03620, PRK03620, 5-dehydro-4-deoxyglucarate dehydratase; Provisional
QELKQILGSGLLSFPVTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAV
ETTAGRVPVIAGAGGGTAQAIEYAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYNR
DNAVLTADTLARLAERCPNLVGFKDGVGDIELMQRIVRALGDRLLYLGGLPTAEVFAAAYLALGVPTYSS
AVFNFVPEIALAFYRALRAGDHATVDRLLDDFFLPYVALRNRKKGYAVSIVKAGARLVGLDAGPVRAPLT
DLTPEELAELAALIAKGGAQLPE
>gnl|CDD|235142 PRK03624, PRK03624, putative acetyltransferase; Provisional
DAMEIRVFRQADFEAVIALWERCDLTRPWNDPEMDIERKLNHDPSLFLVAEVGGEVVGTVMGGYDGHRGW
AYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDRISLGKRLIED
>gnl|CDD|179612 PRK03625, tatE, twin-arginine translocase subunit TatE
MGEISITKLLVVAALVVLLFGTKKLRTLGGDLGAAIKGFKKAMNDDDAAAKKGADVDLQAEKLSHKE
>gnl|CDD|179614 PRK03633, PRK03633, putative MFS family transporter protein; Provisional
MSTYTRPVLLLLCGLLLLTLAIAVLNTLVPLWLAQEHLPTWQVGVVSSSYFTGNLVGTLLAGYVIKRIGF
NRSYYLASLIFAAGCAGLGLMVGFWSWLAWRFVAGIGCAMIWVVVESALMCSGTSRNRGRLLAAYMMVYY
LGTVLGQLLVSKVSTELMSVLPWVTGLVLAAILPLLFTRILNQQAENHDSTSIWPMLKLRQARLGVNGCI
ISGIVLGSLYGLMPLYLNHQGMSDASIGFWMALLVSAGILGQWPIGRLADRFGRLLVLRVQVFVVILGSI
AMLSQAAMAPALFILGAAGFTLYPVAMAWACEKVEHHELVAMNQALLLSYTVGSLLGPSFTAMLMQNYSD
NLLFIMIASVSFIYLLMLLRKAGHTPTPVAH
>gnl|CDD|179615 PRK03634, PRK03634, rhamnulose-1-phosphate aldolase; Provisional
MQNILDSWFVQGMIKVTSDLWLKGWDERNGGNISLRLTEEEVAPYGDDFHQQPRYIPLSQPMPELAGTYF
LVTGSGKFFRNVQLDPAANLGVIRIDSDGAGYHILWGLTNGGKPTSELPAHLMSHIARLKATNGKDRVIM
HCHATNLIALTYVLELDEAVFTRTLWEMSTECLVVFPDGVGIVPWMVPGTDEIGQATAEKMQKHDLVLWP
KHGVFGSGPTLDEAFGLIDTAEKSAEIYVKVLSMGGMKQTITDEELIALGERFGVTPLASALAL
>gnl|CDD|235144 PRK03635, PRK03635, ArgP/LysG family DNA-binding transcriptional regulator
MLDYKQLEALAAVVREGSFERAAQKLHITQSAVSQRIKALEERVGQVLLVRTQPCRPTEAGQRLLRHARQ
VRLLEAELLGELPALDGTPLTLSIAVNADSLATWFLPALAPVLARSGVLLDLVVEDQDHTAELLRRGEVV
GAVTTEPQPVQGCRVDPLGAMRYLAVASPAFAARYFPDGVTAEALAKAPAVVFNRKDDLQDRFLRQAFGL
PPGSVPCHYVPSSEAFVRAALAGLGWGMIPELQIEPELASGELVDLTPGRPLDVPLYWQHWRLESRLLDR
LTDALLAAAAQVLR
>gnl|CDD|235145 PRK03636, PRK03636, hypothetical protein; Provisional
TPVSVNEKKDFLRWFLNNYQLKRRECVWILNYLMSHDQLMEKVHFVENAEYCPRGLVMSAHGVDDVPFRF
FKGNVMTTDAEKSFHDIRLNRDEDIYIQLNFREAFQSPEYVAVLEENPYLPKNEEVNEKDRLLAEQFLEQ
SVFQFRREKLLKQIDEALDRRDKEAFHRLSDELNQLRTQ
>gnl|CDD|235146 PRK03640, PRK03640, o-succinylbenzoate--CoA ligase
METMPNWLKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIH
ALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMNGPKEEAEIQEEFDL
DEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRV
VLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKGIP
VYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNRE
DATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDK
WGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM
>gnl|CDD|179619 PRK03641, PRK03641, DUF2057 family protein
MKTGIVTTLLALCLPVSVFATTLKLSPDIDLLVLDGKKVSGSLLRGADSLELDNGPHQLVFRVEKTIRLP
TGEERLYISPPLIVSFNTQLISQVNFRLPRLENEREANHFSAAPRYQLLDGDATPIPVKLDILAITSTAK
SIDYEVEMERYNKSAKRASLPQFATMMADDSTLLSGVSELDTIPPQSQNLTEQRLKYWFKQADPQTRNRF
LQWAEKQPSS
>gnl|CDD|179620 PRK03642, PRK03642, putative periplasmic esterase; Provisional
MKRTLLYTSLLAFSCSASAAKYPVLTEASPEKAGFNSEKLNQMDRWISQQIDAGYPGVNLLIIKDNQIVY
RKAWGYAKKYDGSTLLAHPVKATTNTMYDLASNTKMYATNFALQKLVSEGKLDVNDLISKYIPGFKDSPG
DKIKGKNTLRIIDLLHHSAGFPADPQYPNKAVAGALYSQDKSTTLEMIKKTPLEYQPGSKHIYSDVDYML
LGFIVESITGQPLDRYVEESIYRPLGLTHTVFNPLQKGFKPQQIAATELNGNTRDGVIHFPNIRTNTLWG
QVHDEKAFYSMGGVSGHAGLFSNTGDMAVLMQVMLNGGGYGNVQLFDAETVKMFTTSSKEDATFGLGWRV
NGNASMTPTFGTLASPQTYGHTGWTGTVTVIDPVNHMAIVMLSNKPHSPVADPQKNPNVFESGLLPIATY
GWVVDQIYAALK
>gnl|CDD|235147 PRK03643, PRK03643, tagaturonate reductase
MKTLNRRDFPGAQYPEKILQFGEGNFLRAFVDWQIDLLNEHTDFNGGVVVVQPIDTGFPPSLNEQDGLYT
LIIRGLNEGEAVSEARLIRSISREINPYSDWDEFLKLARNPELRFVFSNTTEAGISYHAEDKFDDAPPVS
FPAKLTALLYERFKHFNGAADKGLIIIPCELIDYNGEKLKEIVLRYAQEWNLPEAFIQWLEEANTFCSTL
VDRIVTGYPRDEAAALEEELGYEDGLLDTAEPFYLWVIEGPKSLAKELPFDKAGLNVLIVDDIKPYRERK
VRILNGAHTALVPVAYLAGLDTVGEAMEDAEIGAFVEKAIYEEIIPVLDLPEDELESFAEAVLDRFRNPF
IKHQLLSIALNSMSKFRTRILPQLLAYQERKGTLPARLTFALAALIAFYRGERNGETYPIQDDAHWLERF
KQLWSQVDDGEISLAELVAAVLSDEKHWGQDLTQVPGLVEQVTEYLQAILE
>gnl|CDD|179622 PRK03646, dadX, catabolic alanine racemase
TRPIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSALGATDGFAVLNLEEAITLRERG
WKGPILMLEGFFHAQDLELYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPERVQTV
WQQLRAMGNVGEMTLMSHFARADHPDGISEAMARIEQAAEGLECERSLSNSAATLWHPQAHFDWVRPGII
LYGASPSGQWRDIANTGLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAP
TGTPVLVDGVRTRTVGTVSMDMLAVDLTPCPQAGIGTPVELWGKEIKIDDVAAAAGTIGYELMCALALRV
PVVTV
>gnl|CDD|235148 PRK03655, PRK03655, putative ion channel protein; Provisional
MLHPRARTMLLLSLPALAIGIASSLILIVVMKIASVLQNLLWQRLPGTLGIAQDSPLWIIGMLTLTGIAV
GLVIRFSPGHAGPDPATEPLIGAPVPPSALPGLLLALILGLAGGVSLGPEHPIMTVNIALAVAIGARLLP
RVNRMDWTILASAGTIGALFGTPVAAALIFSQTLNGSNEVPLWDRLFAPLMAAAAGALTTGLFFHPHFSL
PIAHYGQMEMTDILSGAIVAAIAIAAGMVAVWCLPRLHALMHRLKNPVLVLGIGGFILGILGVIGGPLTL
FKGLDEMQQMAANQAFSASDYFLLAVVKLAALVVAAASGFRGGRIFPAVFVGVALGLMLHAHVPAVPAAI
TVSCAILGIVLVVTRDGWLSLFMAAVVVPDTTLLPLLCIVMLPAWLLLAGKPMMMVNRPKQQPP
>gnl|CDD|235149 PRK03657, PRK03657, 2-oxo-tetronate isomerase
DKIVQLADADTIENLTKALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDEAKMKI
LSVSQQSLERYSAVSEAVVAEMATGAIERADADISIAISGYGGPEGGEDGTPAGTVWFAWNIKGQTYTAR
MHFAGDCETVLAKAVRFALAQLLQLLLKWA
>gnl|CDD|179625 PRK03659, PRK03659, glutathione-regulated potassium-efflux system protein KefB; Provisional
MEGSDLLTAGVLFLFAAVVAVPLAQRLGIGAVLGYLLAGIAIGPWGLGFISDVDEILHFSELGVVFLMFI
IGLELNPSKLWQLRRSIFGVGAAQVLLSAAVLAGLLMLTDFSWQAAVVGGIGLAMSSTAMALQLMREKGM
NRSESGQLGFSVLLFQDLAVIPALALVPLLAGSADEHFDWMKIGMKVLAFAGMLIGGRYLLRPLFRFIAA
SGVREVFTAAALLLVLGSALFMDALGLSMALGTFIAGVLLAESEYRHELEIAIEPFKGLLLGLFFISVGM
ALNLGVLYTHLLWVLISVVVLVAVKGLVLYLLARLYGLRSSERMQFAGVLSQGGEFAFVLFSAASSQRLL
QGDQMALLLVVVTLSMMTTPLLMKLIDKWLARRLNGPEEEDEKPWVEDDKPQVIIVGFGRFGQVIGRLLM
ANKMRITVLERDISAVNLMRKYGYKVYYGDATQLELLRAAGAEKAEAIVITCNEPEDTMKIVELCQQHFP
HLHILARARGRVEAHELLQAGVTQFSRETFSSALELGRKTLVSLGMHPHQAQRAQQHFRRLDMRMLRELM
PQHNGDVVQISRAKEARRELEEIFQREMQQERRQLDGWDEF
>gnl|CDD|179627 PRK03661, PRK03661, nicotinamide-nucleotide amidase
MTDSELMQLSEQVGQALKARGATVTTAESCTGGWVAKVITDIAGSSAWFERGFVTYSNEAKAQMIGVREE
TLAQHGAVSEPVVVEMAIGALKAARADYAVSISGIAGPDGGSEEKPVGTVWFGFASASGEGITRRECFSG
DRDAVRRQATAYALQTLWQQFLQN
>gnl|CDD|179628 PRK03669, PRK03669, mannosyl-3-phosphoglycerate phosphatase-related protein
MLSLQDPLLIFTDLDGTLLDSHTYDWQPAAPWLTRLREAQVPVILCSSKTAAEMLPLQQTLGLQGLPLIA
ENGAVIQLDEQWQDHPDFPRIISGISHGEIRQVLNTLREKEGFKFTTFDDVDDATIAEWTGLSRSQAALA
RLHEASVTLIWRDSDERMAQFTARLAELGLQFVQGARFWHVLDASAGKDQAANWLIATYQQLSGTRPTTL
GLGDGPNDAPLLDVMDYAVVVKGLNREGVHLQDDDPARVYRTQREGPEGWREGLDHFFSAR
>gnl|CDD|167581 PRK03670, PRK03670, competence damage-inducible protein A; Provisional
MFAEIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKPEVLVISGGL
GPTHDDVTMLAVAEALGRELVLCEDCLERIKEFYEELYKKGLIDDPTLNEARKKMAYLPEGAEPLENTEG
AAPGAYIEHKGTKIFVLPGMPREMKAMLEKEVLPRLGERKFVQKKFLAEITDESKLAPILEEALERFNVK
IHSSPKGFGKYIGIIIFAEDEEEIEKAVEFMEERGIKFEEGW
>gnl|CDD|179629 PRK03673, PRK03673, nicotinamide mononucleotide deamidase-related protein YfaY
MLRVEMLSTGDEVLHGQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGGL
GPTSDDLSALAAATAAGEGLVLHEEWLAEMERFFAERGRVMAPSNRKQAELPASAEMIDNPVGTACGFAL
QLNRCLMFFTPGVPSEFKVMVEQEILPRLRERFSLPEPPLCLRLTTFGRSESDLAQSLDPLPLPPGVVMG
YRSSMPIIELKLTGPASQRQAMEQLWQQVRRVAGQSVIFEGTEGLPAQIARRLQERQLSLTLSEQFTAGL
LALQLSRAGAPLLAGEVLPSQEETLAQTAHWATERRANHFAGLALAVSGLENEHLNFALHTPDGTFAQRV
RFSATRYSLAIRQEVCAMMALNMLRRWLNGQDVASEHGWIEVVESL
>gnl|CDD|179630 PRK03681, hypA, hydrogenase/urease nickel incorporation protein HypA
MHEITLCQRALELIEQQAAKHGAKRVTGVWLKIGAFSCVETSSLAFCFDLVCRGTVAEGCKLHLEEQEAE
CWCETCQQYVTLLTQRVRRCPQCHGDMLRIVADDGLQIRRIEID
>gnl|CDD|179631 PRK03692, PRK03692, putative UDP-N-acetyl-D-mannosaminuronic acid transferase; Provisional
NTTAPKYTLRGLQLIGFRDMQHALDYLFADGQLKTGTLVAINAEKVLTAEDDAELRELINAAEYKYADGI
SVVRSIRKKYPQAQVSRVAGADLWEALMARAGKEGTPVFLVGGKPEVLAQTEAKLRTQWNVNIVGSQDGY
FTPEQRQALFERIHASGAKIVTVAMGSPKQEIFMRDCRLVYPDALYMGVGGTYDVFTGHVKRAPKIWQNL
GLEWLYRLLSQPSRIRRQLRLLRYLRYHYTGRL
>gnl|CDD|235150 PRK03695, PRK03695, vitamin B12-transporter ATPase; Provisional
MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARH
RAYLSQQQTPPFAMPVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAV
VLQVWPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK
LLASGRRDEVLTPENLAQVFGVNFRRLDVEGHPMLIST
>gnl|CDD|235151 PRK03699, PRK03699, putative transporter; Provisional
TNSNRIKLTWISFLSYALTGALVIVTGMVMGPIAEYFNLPVSSMSNTFTFLNAGILISIFLNAWLMEIIP
LKRQLIFGFALMILAVAGLMFSHSLALFSIAMFVLGVVSGITMSIGTFLITHVYEGKQRGSRLLFTDSFF
SMAGMIFPIIAAYLLARSIEWYWVYACIGLVYVAIFILTLFSEFPALGKHAPKADKPVAKEKWGIGVLFL
AIAALLYILAQLTFISWVPEYAQKKFGMSLEDAGNLVSNFWMAYMVGMWIFSFIVRFFDLQRILTVLAGL
ALVLMYLFVNTDDPSHLLYAILGLGFFSSAIYTTIITLGSQQTKVASPKLVNFILTCGTIGTMLTFVVTS
PIVAHFGLQAALLTANGLYAVVFVMCILLGFVSKHRQHGALTAH
>gnl|CDD|235152 PRK03705, PRK03705, glycogen debranching protein GlgX
MTQLAIGKPTPLGAHYDGQGVNFTLFSAHAERVELCVFDENGQEQRYDLPARSGDIWHGYLPGARPGLRY
GYRVHGPWQPAQGHRFNPAKLLIDPCARQVEGEVKDDPRLHGGHDEPDYRDNAAIAPKCVVVDDHYDWED
DAPPRTPWGSTVIYEAHVRGLTYLHPEIPVEIRGTYAALGHPVMIAYLKQLGITALELLPVAQFASEPRL
QRMGLSNYWGYNPLAMFALDPAYASGPETALDEFRDAVKALHKAGIEVILDVVFNHSAELDLDGPTLSLR
GIDNRSYYWIREDGDYHNWTGCGNTLNLSHPAVVDWAIDCLRYWVETCHVDGFRFDLATVLGRTPEFRQD
APLFTAIQNDPVLSQVKLIAEPWDIGPGGYQVGNFPPPFAEWNDHFRDAARRFWLHGDLPLGEFAGRFAA
SSDVFKRNGRLPSASINLVTAHDGFTLRDCVCFNQKHNEANGEENRDGTNNNYSNNHGKEGLGADLDLVE
RRRASIHALLTTLLLSQGTPMLLAGDEHGHSQHGNNNAYCQDNALTWLDWSQADRGLTAFTAALIHLRQR
IPALTQNRWWEEGDGNVRWLNRQAQPLSADEWQQGPKQLQILLSDRWLIAINATLEVTEIVLPEGEWHAI
PPFAGEDNPVITAVWHGPAHGVCVFQRQ
>gnl|CDD|179635 PRK03708, ppnK, NAD(+) kinase
MRFGIVARRDKEEALKLAYRVYDFLKVSGYEVVVDSETYEHLPEFSEEDVLPLEEMDVDFIIAIGGDGTI
LRIEHKTKKDIPILGINMGTLGFLTEVEPEETFFALSRLLEGDYFIDERIKLRVYINGENVPDALNEVVI
LTGIPGKIIHLKYYVDGELADEVRADGLIISTPTGSTAYAMSAGGPFVDPRLDAILIAPLCPFKLSSRPM
VVPSSSRIDVKLLRTGREIILVIDGQYYEELPPDTEITIKKSPRKTKFVRFSKEIYPKYTMKIKERF
>gnl|CDD|179636 PRK03715, argD, acetylornithine transaminase protein; Provisional
MPFNDYPIDSLMYITNRPDIVFTHGKGSWLYDHNGKRYLDFIQGWAVNCLGHCNPGMVEALAAQAEKLIN
PSPAFYNEPMAKLAGLLTQHSCFDKVFFANSGAEANEGAIKLARKWGRKHKNGAYEIITFDHSFHGRTLA
TMSASGKPGWDTIFAPQVPGFPKAELNDIASVEKLITDKTVAVMLEPVQGEGGVIPATREFMQQLRALTK
QHGLLLIVDEVQTGCGRTGTLFAYELSGIEPDIMTLGKGIGGGVPLAALLAKAEVAVFEAGDQGGTYNGN
PLMTAVGVAVISQLLAPGFLEGVRARGEYLKEKLLELSEERGLEGERGEGLLRALLLGKDIGPQIVEKAR
DMQPDGLLLNAPRPNLLRFMPALNVTTEEIDQMIAMLRSVLDKLA
>gnl|CDD|167589 PRK03717, PRK03717, ribonuclease P protein component 2; Provisional
MREKPKTLPPTLRDKNRYIAFQVIGERPFTKDEIKKAIWEASLSTLGELGTARAKPWFIKFDEKTQTGIV
RCDRKHVEELRFALTLVTEINGSKAIIRTLGVSGTIKRLKRKFLSEFGWK
>gnl|CDD|179637 PRK03719, PRK03719, ecotin; Provisional
MMKKMKTIAPAVLLAAFAAASAWAPAASSSYQPLEKIKPYPQAEKGMKRQVITLPPQEDESDYKVELLIG
QTLEVDCNQHRLGGELEEKTLEGWGYDYYVVDKVSGPPSTMMACPDGKKEEKFVTALGDGLMLRYNSRLP
IVVYLPKGVEVRYRVWKAEEKVQNAV
>gnl|CDD|235153 PRK03731, aroL, shikimate kinase AroL
MTQPLFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTSNMTVAEIVEREGWAGFRARESAALEAVTA
PSTVIATGGGIILTEENRHFMRNNGIVIYLCAPVSVLANRLEANPEEDQRPTLTGKPISEEVAEVLAERE
ALYREVAHHIIDATQPPSQVVSEILSALAQS
>gnl|CDD|167593 PRK03732, PRK03732, hypothetical protein; Provisional
MMETIEGIIVVTTETIPGYRIVEVKGIARGGIVKATHLGRDIMALLRNIKGGEVKEYTQMMAEAREEALR
RMALHAKELGANAVVNFRFATSNVGSSMAEVYAYGTAVVVEKEE
>gnl|CDD|179639 PRK03735, PRK03735, cytochrome b6; Provisional
MLSKVYDWFDERLDITPIWRDIADHEVPEHVNPAHHFSAFVYCFGGLTFFCFVIQILSGMFLTMYYVPDI
KNAYESVYYLQNEVAFGWIVRGMHHWGASLVIVMMFLHTLRVFFTGGYKKPRELNWVVGVLIFFVTVGLG
FTGYLLPWDQKAYFATKVGSQIAEAIPVIGDFIKTLLRGGEIVGAQTLTRFFAIHVFFLPWALAVLMLAH
FLMIRKQGISGPL
>gnl|CDD|235154 PRK03739, PRK03739, 2-isopropylmalate synthase; Validated
MLKMPATKYRPFPPVDLPDRTWPSKTITKAPIWCSVDLRDGNQALIEPMSPERKLRMFDLLVKIGFKEIE
VGFPSASQTDFDFVRELIEEGLIPDDVTIQVLTQAREHLIERTFEALEGAKRAIVHLYNSTSPLQRRVVF
GKDRDGIKAIAVDGARLVKELAAKYPETEWRFEYSPESFTGTELDFALEVCDAVIDVWQPTPERKVILNL
PATVEMSTPNVYADQIEWMCRNLARRDSVILSLHPHNDRGTGVAAAELALMAGADRVEGCLFGNGERTGN
VDLVTLALNLYTQGVDPGLDFSDIDEIRRTVEYCNQLPVHPRHPYAGDLVFTAFSGSHQDAIKKGFAAQK
ADAIVWEVPYLPIDPADVGRSYEAVIRVNSQSGKGGVAYLLEQDYGLDLPRRLQIEFSRVVQAVTDAEGG
ELSAEEIWDLFEREYLAPRGRPVLLRVHRLSEEDGTRTITAEVDVNGEERTIEGEGNGPIDAFVNALSQA
LGVDVRVLDYEEHALGAGSDAQAAAYVELRVGGRTVFGVGIDANIVTASLKAVVSAVNRALA
>gnl|CDD|179641 PRK03743, pdxA, 4-hydroxythreonine-4-phosphate dehydrogenase PdxA
MKKPIIAIPIGDPAGIGPEIVVKTLADKEVYDECKPFLIGDAPVIERAMKICGVDLNINKIKKPAEGKFE
WGTIDLIDLGNYDCDSIKWGKVQALAGKAAFEYIKKSVELAMEGKVDAVATTPINKEALKAAGVKYIGHT
EILADLTGTEDPLTMFEVRNLRVFFLTRHVSLKKACDYVTKERVLDYIQRCTKALEKLGIKNPKIAVAGL
NPHSGEHGLFGDEEVDEIIPAVEAAQEMGINVEGPVPADSVFHLALQGRYDAVLSLYHDQGHIATKTLDF
ERTIAITNGLPFLRTSVDHGTAFDIAGTGKASSVSMEEAILLAAKYAPMFKK
>gnl|CDD|235155 PRK03745, PRK03745, signal recognition particle protein Srp19; Provisional
MGRFVVWPSELDSRLSRKYGRIVPKNLAVERPTLEEIVDAAEALGFKVIEVDREKLNPRLSGIDEELRTR
GRIVIESPYGKSKSLKMIAQKIREFRKRRR
>gnl|CDD|179642 PRK03757, PRK03757, YceI family protein
MKKTLLGLALGSLLFSAGSAVAADYKIDTEGQHAFINFKISHLGYSWLYGRFNDFDGTFSFDEKNPAASK
VNVTINTTSVDTNHAERDKHLRSADFLNVAKFPQATFTSTSVKKDGDGTLDITGDLTLNGVTKPVTIEAK
LIGEGDDPWGGYRAGFEGTTTIKLKDFGIKTDLGPASQEVELILSVEGVRQ
>gnl|CDD|235156 PRK03759, PRK03759, isopentenyl-diphosphate Delta-isomerase
PMMETELVVLLDEQGVPTGTAEKAAAHTADTPLHLAFSCYLFDADGRLLVTRRALSKKTWPGVWTNSCCG
HPQPGESLEDAVIRRCREELGVEITDLELVLPDFRYRATDPNGIVENEVCPVFAARVTSALQPNPDEVMD
YQWVDPADLLRAVDATPWAFSPWMVLQAANLEARELLLAFAQRN
>gnl|CDD|235157 PRK03760, PRK03760, hypothetical protein; Provisional
MIINKTKGKSWHGAVRFADTFIKRFRGLMLVRNVNYALVFILPAETRFNASIHMFFMLSSIDVIFLDSNR
RVVDFKTLKPWRIYVPKKPARYIIEGPVGKIRVLKVEVGDEIEWIDE
>gnl|CDD|235158 PRK03761, PRK03761, LPS assembly outer membrane complex protein LptD; Provisional
MKKRSPTLLATMIATALYSQQALADLASQCMLGVPSYDRPLVTGDPNQLPVTIEADHAEANYPDDAVYTG
NVDIKQGNSRLTADEVQLHQQENPGQAEPVRTVDALGNVHYDDNQIILKGPKAWSNLNTKDTNVWNGDYQ
MVGRQGRGKADLMKQRGQNRYTILENGSFTSCLPGDNSWSVVGSEIIHDREEEVAEIWNARFKVGGVPVF
YSPYLQLPIGDKRRSGFLIPNAKYSSKNGFEFELPYYWNIAPNYDATITPHYMSRRGWQWENEFRYLTQA
GAGLMAGEYLPSDRVYEDEPNDDNSSRWLFYWNHSGVMDQVWRFNVDYTKVSDPRYFTDFDSKYGSSTDG
YATQKFSVGYAQQNWNATLSTKQFQVFDEQNNSPYRAEPQLDFNYYQNDLGPFDFRLYGQAVRFTNDNKN
MPEATRVHLEPTLNLPLSNRWGSLNTEAKLLATHYQQDNLDWYNSNNTTKLEESVNRVIPQFKVDGKMVF
ERDMDLAPGYTQTLEPRVQYLYVPYRDQSNIYNYDSTLLQSDYYGLFRDRTYSGLDRIASANQVTTGVTT
RFYDDAAVERFNISVGQIYYFTPSRTGDNNTWENDDKTGSSVWAGDTYWRISDRWGLRGGIQYDTRLDSV
ALANSSLEYRRDEDRLIQLNYRYASPEYIQATLPSYYSAEIYQQGISQVGAVASWPIADRWSIVGAYYYD
TKANKPAEQLLGLQYNSCCWAIGVGYERKLTGWDNDKQHSVYDNKIGFNIELRGLSSNYGLGTQEMLRSN
ILPYQRAF
>gnl|CDD|179647 PRK03767, PRK03767, NAD(P)H:quinone oxidoreductase; Provisional
MAKVLVLYYSMYGHIETMAEAVAEGAREVAGAEVTIKRVPETVPEEVAKKAGGKTDQAAPVATPDELADY
DAIIFGTPTRFGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQHGGQETTITSTHTTLLHHGMVI
VGLPYAFQGQMDVDEVTGGSPYGATTIAGGDGSRQPSENELAGARYQGRHVAEIAAKLAG
>gnl|CDD|179648 PRK03776, PRK03776, phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase
MSELLSFALFLASVLIYAWKAGRNTWWFAATLTVLGLFVVLNITLFASDYFTGDGINDAVLYTLTNSLTG
AGVSKYILPGIGIVLGLVAVFGALGWILRRRRHHPHHFGYSLLALLLALGSVDASPAFRQITELVKSQSR
DGDPDFAAYYKEPAKTIPNPKLNLVYIYGESLERTYFDNEAFPGLTPELGALKNEGLDFSHTQQLPGTDY
TIAGMVASQCGIPLFAPFEGNASASVSSFFPQNICLGDILKNSGYQNYFVQGANLRFAGKDVFLKSHGFD
HLYGSEELKSVVADPHYRNDWGFYDDTVLDEAWKKFEELSRSGQRFSLFTLTVDTHHPDGFISRTCNRKS
YDFDGKPNQSFSAVSCSQENIAALINKIKASPWFKNTVIVVSSDHLAMNNTAWKYLNKQDRNNLFFVIRG
DKPQQETLAVKRNTMDNGATVLDILGGDNYIGLGRSSLSGQSLSEIFLNIKEKTLAWKPDIIRLWNFPKE
IKDFTIDQQKNMIAFSGSHFRLPLLLRVSDKRVEPLPESEYSAPLRFQLADFAPRDNFVWVDRCYKMAQL
WAPELALSTDWCVSQGQLGGQQIVQHVDKANWKGKTAFKDTVIDMARYQGNVDTLKIVDNDIRYKADSFI
FNVAGAPEEVKQFSGISRPESWGRWSNAQLGDEVKIEYKHPLPKKFDLVITAKAYGNNASRPIPVRVGNE
EQTLVLGNEVTTTTLHFDNPTDANTLVITPPEPVSTNEGNILGHSPRKLGIGMVEIKVVEVE
>gnl|CDD|235159 PRK03784, PRK03784, vtamin B12-transporter permease; Provisional
MSMLTLARQQQRRNRRWLLGLSVLLLLALLLSLCAGEQWISPGDWLSPRGELFVWQLRLPRTLAVLLVGA
ALAVSGAVMQALFENPLAEPGLLGVSNGAGVALVAAVLLGQGLLPPWALSLCAIAGALLITLILLRFARR
HRLSTSRLLLAGVALGIICSALMTWAVYFSTSLDLRQLMYWMMGGFGGVDWRQSWLMLALLPVLIWLCCQ
GRPLNMLALGEISARQLGLPLWFWRNLLVLATGWLVGVSVALAGAIGFIGLVIPHILRLCGLTDHRVLLP
GCALAGASLLLLADIVARLALASAELPIGVVTATLGAPVFIWLLLRSHRAR
>gnl|CDD|235161 PRK03814, PRK03814, oxaloacetate decarboxylase subunit gamma; Provisional
MTDIGSLLVDAATLMLTGMGVVFIFLTLLVYLVQLMSKLIPQEVPEPIAAPKKSKKQQPTSSAVSPQVVA
AISAAVHQHRASKAK
>gnl|CDD|235163 PRK03817, PRK03817, galactokinase; Provisional
MKVKSPGRVNLIGEHTDYNDGYVLPFAINLYTFLEIEKSEKFIFYSENFNEEKTFELDKLEKLNSWADYI
KGVIWVLEKRGYEVGGVKGKVSSNLPIGAGLSSSASLEVAVAYALNEAYNLNLSKLELALLAREAENEFV
GVPCGIMDQFAVAFGKKDHAIFLDTMTLEYEYVPFPEDYEILVFDTGVKRELASSEYNERRQECEEALKI
LGKKSSKEVTEEDLSKLPPLLRKRAGYVLRENERVLKVRDALKEGDIETLGELLTESHWDLADNYEVSCE
ELDFFVEFALELGAYGARLTGAGFGGSAIALVDKGKFESIGEELLEEYKKRFGIDPKYFVVESSDGVRKI
E
>gnl|CDD|179654 PRK03818, PRK03818, putative transporter; Validated
MSDIALTVSILALVAVVGLWIGNIKIRGVGLGIGGVLFGGIIVGHFVSQFGLTLDSDMLHFIQEFGLILF
VYTIGIQVGPGFFSSLRKSGLRLNLFAVLIVILGGLVTAILHKLFGIPLPVMLGIFSGAVTNTPALGAGQ
QILRDLGTPGDLVDQMGMGYAMAYPFGICGILLSMWLIRLIFRINVDKEAQEFESSSGNGHELLQTINIR
VENPNLHGKAIKDVPILNGDKFVCSRLKRGDTLMVPSPDTIIQLGDLLHLVGQPEDLHKAQLVIGEEVDT
SLSTRGTDLRSERVVVTNEKVLGKKLRDLHLKNKYGVVISRLNRAGVELVASPDLSLQFGDILNLVGRPE
AIDAVANVLGNAQQKLQQVQMLPVFIGIGLGVLLGSIPFFIPGFPAALKLGLAGGPLIVALILGRIGSIG
KLYWFMPPSANLALRELGIVLFLAVVGLKSGGDFVDTLVNGEGLSWIGYGFLITAVPLLIVGILARMLAK
MNYLTLCGMLAGSMTDPPALAFANNLHPTSGAAALSYATVYPLVMFLRIITPQLLAVLFWSL
>gnl|CDD|179655 PRK03822, lplA, lipoate-protein ligase A; Provisional
MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLAR
RSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTSIVLNALNSLGVSAEASGRNDLVVKTAEGDRKVSGSAY
RETKDRGFHHGTLLLNADLSRLANYLNPDKKKLQAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFA
HYGERVEAEVISPDKTPDLPGFAETFARQSSWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQ
IFTDSLNPAPLEALAGRLQGCLYRADALQQECEALIVDFPEQEKELRELSAWLAGAVR
>gnl|CDD|235164 PRK03824, hypA, hydrogenase nickel incorporation protein HypA
MHEWALAEAIVRTVIDYAQKEGASKVKALKVVLGELQDVDKEIVEFALNELLKGTILEGAEIIFEEEEAV
LKCRNCGNEWSLKEVKESLDEEIREAIHFIPEVVHAFLKCPKCGSRDFEIVKGRGVYIEEIKIEK
>gnl|CDD|235165 PRK03826, PRK03826, 5'-nucleotidase; Provisional
KQSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAVIKNRKFGGNLNAERIALLAMYHDAS
EVLTGDLPTPVKYFNPEIAHEYKKIEKIAEQKLLDMLPEELQEDFRPLLDSHAASEEEKAIVKQADALCA
YLKCLEELSAGNNEFNLAKKRLEKTLEARRSPEMDYFMEVFVPSFTLSLDEISQD
>gnl|CDD|235166 PRK03837, PRK03837, transcriptional regulator NanR; Provisional
GRNLRSRPIARKKLSEEVEERLEQMIRSGEFGPGDQLPSERELMAFFGVGRPAVREALQALKRKGLVQIS
HGERARVSRPSADTIIGQLSGMAKDFLSQSPDGLAHLKQARLFFESSLARYAAEHATDEQIALLRKALER
NSQSLGDNAAFIRSDMEFHRVIAEIPGNPIFMAIHEALLDWLIEARPEVVILHGHENVTLQEHIAIVDAI
RAHDPDEADRALQSHLNRVSALYHALGQTTN
>gnl|CDD|179660 PRK03839, PRK03839, putative kinase; Provisional
MIIAITGTPGVGKTTVSKLLAEKLGYEYVDLTEFALKKGIGEEKDDEMEIDFDKLAYFIEEEFKEKNVVL
DGHLSHLLPVDYVIVLRAHPKIIKERLKERGYSKKKILENVEAELVDVCLCEALEEKEKVIEVDTTGKTP
EEVVEEILELIKSGKKRKVGIVDWSEVYDEIFPYLRLGID
>gnl|CDD|179661 PRK03846, PRK03846, adenylylsulfate kinase; Provisional
DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSD
LGFSDADRKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDP
KGLYKKARAGEIRNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDIIRS
>gnl|CDD|235167 PRK03854, opgC, glucans biosynthesis protein MdoC
MNPVPAQREYFLDSIRAWLMLLGIPFHISLIYSSHTWHVNSAEPSLWLTLLNDFIHAFRMQVFFVISGYF
SYMLFLRYPPKRWLKVRLERVGIPMLTAIPLLTLPQFIMLQYVKGKAEDWPTLSLYEKYNTLAWELISHL
WFLLVLVVLTLLCVAIFKRLRRNLENSDPRPATFGSLGKLSLIFLLLGLGYAAIRRTIFIVYPPILSSGL
FNFIVMQTLFYLPFFLLGALAFIFPALKALFTTPSRGCTLGAALAFVAYLLNQRYGSGDAWMYETESVIT
MVMGLWMVNVVFSLGHRLLNFPSPRVTYLVNASLFIYLVHHPLTLFFGALITPHISSNWLGFLLGLVFVF
GIAFALYEIHLRIPLLRFLFSGKPP
>gnl|CDD|179663 PRK03858, PRK03858, DNA polymerase IV; Validated
RADASILHADLDSFYASVEQRDDPALRGRPVIVGGGVVLAASYEAKAYGVRTAMGGRQARRLCPQAVVVP
PRMSAYSRASKAVFEVFRDTTPLVEGLSIDEAFLDVGGLRRISGTPVQIAARLRRRVREEVGLPITVGVA
RTKFLAKVASQVAKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVTAAKLRAHGITTVGDVAELPESALVS
LLGPAAGRHLHALAHNRDPRRVETGRRRRSVGAQRALGRGPNSPAEVDAVVVALVDRVARRMRAAGRTGR
TVVLRLRFDDFTRATRSHTLPRPTASTATLLAAARDLVAAAAPLIAERGLTLVGFAVSNLDDDGAQQLEL
PFGLRRPGSALDAALDAVRDRFGNAAVTRAVLLGRDPGLEVPMLPD
>gnl|CDD|235168 PRK03868, PRK03868, glucose-6-phosphate isomerase; Provisional
MLNNSLFFKQSDIKTISSYFERINKEKESGEIGYYHLPDQSTSLIEESLKFVKDKESIKNIVVIGIGGSS
LGVKAIYSFLKNEKNNKKELHFLENTDPISINKTLSKINLENTLFIVISKSGTTIETISIFKYLLSHFKL
DQELKKNFLFITDPDSKLEQFAKENNIKCFNIPKNVGGRFSVLSAVGIVPLALCGYDIKALLEGAKACKD
SFFEQKEDHILKKAYFYATHKNAYNINVLFSYSDALKGFNDWYVQLWGESLGKKQGYKTRVGLTPIGLIG
SRDQHSFLQLIMEGPRDKTVTFIKIKDFQNAPKIPNISLKGLESLDFVNGVSFNELINAQCDATMEALIA
EDIPVDVITLEKLDEFSIGYLIYYYELLTSAVGKMLGINTYDQPGVEVGKRILKEKLQSK
>gnl|CDD|235169 PRK03879, PRK03879, ribonuclease P protein component 1; Validated
MMITPSNILRHELIGLKVEVVDSTNPSLVGIKGRVVDETRNTLVIETDGKEWMVPKDGATFEFELGRDDV
VKVKVDGRLLVGRPEDRLKKKIKKLR
>gnl|CDD|167628 PRK03887, PRK03887, methylated-DNA--protein-cysteine methyltransferase; Provisional
MLSVEKFQIKGREIWIGVIFEEKIQGITFSFDGEEFLRERISNLAEFLKKRGVKVSLKERPSDYPELVFK
VLIGKISNEEGLEELSFEGLTPFERKVYEWLTKNVKRGEVITYGELAKALNTSPRAVGGAMKRNPYPIIV
PCHRVVGRKNPGLYTPKPEYKKFLLEVEGVKEWTS
>gnl|CDD|179667 PRK03892, PRK03892, Ribonuclease P protein component 3
MAGGGGVKFVEMDVRSEEAYELAKEWFDEVVFTKKLVLEDSPDFGSLKEELKELKKEYGKVAILLVTPKP
SLIREVKQRFLNYLIYVQGGDLRVNRYAIERGVDAIISPWVGRKDPGIDHVLARMAAKRGVAIGFSLSPL
LRANPYERANILRFMMKAWQLVNKYKVPRFITSSAESKWEVRGPRDLMSLGINIGMEIPQAKASLSFYPR
IILKRL
>gnl|CDD|179668 PRK03893, PRK03893, putative sialic acid transporter; Provisional
MSTTTQNIPWYRHLNRAQWKAFSAAWLGYLLDGFDFVLITLVLTEVQGEFGLTTVQAASLISAAFISRWF
GGLLLGAMGDRYGRRLAMVISIVLFSVGTLACGFAPGYWTLFIARLVIGMGMAGEYGSSATYVIESWPKH
LRNKASGFLISGFSIGAVVAAQVYSLVVPVWGWRALFFIGILPIIFALWLRKNLPEAEDWKEKHAGKAPV
RTMVDILYRGEHRIINILLTLAAAAALWFCFAGNLQNAAIVAVLGLLCAAIFISFMVQSSGKRWPTGVML
MVVVLFAFLYSWPIQALLPTYLKTDLGYDPHTVANVLFFSGFGAAVGCCVGGFLGDWLGTRKAYVCSLLI
SQLLIIPVFAIGGANVWVLGLLLFFQQMLGQGISGLLPKLIGGYFDTEQRAAGLGFTYNVGALGGALAPI
LGALIAQRLDLGTALASLSFSLTFVVILLIGLDMPSRVQRWLRPEALRTHDAIDGKPFSGAVPFGSAKNA
LVKTKS
>gnl|CDD|179669 PRK03902, PRK03902, transcriptional regulator MntR
MPTPSMEDYIEQIYLLIEEKGYARVSDIAEALSVHPSSVTKMVQKLDKDEYLIYEKYRGLVLTPKGKKIG
KRLVYRHELLEQFLRIIGVDESKIYNDVEGIEHHLSWNAIDRIGDLVQYFEEDPDRLETLRAVQKANEEK
EE
>gnl|CDD|235171 PRK03903, PRK03903, transaldolase; Provisional
AYKDEIAKLKGKKAKEIYEELAIKDIKKAADKLLPLYEKPDDGFISIEIDPFLEDDAAGSIEEGKRLYKT
IGRPNVMIKVPATKAGYEAMSALMKKGISVNATLIFSPEQAKECAEALNEGLKKNTKDPKAVISVFVSRF
DRLLDPKLAPKNLQAKSGIMNATKCYNQIEQHANKNIRTLFASTGVKGDDLPKDYYIKELLFKNSINTAP
LDTIEAFLKDGNTEPKKPLKIEEIEAFFKELKSHNIDLENTYQKLLKDGLEAFKQAFEDILKSL
>gnl|CDD|235172 PRK03906, PRK03906, mannonate dehydratase; Provisional
MEMTWRWFGPNDPVTLEDIRQPGATGIVTALHDIPVGEVWPVEEILARKAEIEAAGLEWSVVESVPVHED
IKTGTPNRDRYIENYKQTLRNLAAAGIKVVCYNFMPVFDWTRTDLAYELPDGSTALRFDQIDFAAFDPHI
LKRPGAEADYGEEEIAQAAARFAAMSEEDKARLTRNIIAGLPGWEEPYTLEQFRALLELYKDIDEEKLRE
NLAYFLKAIIPVAEEVGVKMAIHPDDPPRPIFGLPRIVSTEEDLQRLLDAVDSPANGLTLCTGSLGARPD
NDLPAMIREFGDRIHFAHLRNVKREGPGSFHEAAHLSGDVDMYAVVKALLDEEFRIPMRPDHGRMIWDDL
GKKTNPGYGLYGRALGLAELRGLWEALEKAAKRKA
>gnl|CDD|235173 PRK03907, fliE, flagellar hook-basal body complex protein FliE
PFNNLNTDNRTKNEESGSTFKEQKGGEFSKLLKQSINELNKTQEQSEKALADIATGQVKDLHQAAIAIGK
AETSMKLMLEVRNKAISAYKEILRTQI
>gnl|CDD|179673 PRK03910, PRK03910, D-cysteine desulfhydrase; Validated
MNLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITA
GAIQSNHARQTAAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELA
EELRAQGRRPYVIPVGGSNALGALGYVACALEIAQQLAEGGVDFDAVVVASGSGGTHAGLAAGLAALGPD
IPVIGVTVSRSAAEQEPKVAKLAQATAELLGLPTEIPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTE
GILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAPALFAYADAFAL
>gnl|CDD|235174 PRK03911, PRK03911, HrcA family transcriptional regulator
KLNKKDLLLDSIIQTYLQDNEPIGSNELKSLMNLKISAATIRNYFKKLSDEGLLTQLHISGGRIPTIKAM
KNYWQKSLDFEDEVLIVDEKRLKELSKEFELFCLVKGPSSERLKEVLNLNDRFLILDFEAFEIVLKYSVK
MEKFLQELVGLSLKEIRKIAAQVNALELARKIAELKYSSNEITAFGLMGLKTLLNSELFFDILDGKVLDR
FKEGLHFEPLFEEGFMGLKRDIEFLGKDAQMLCAGSLYCDYEKFLQTIKE
>gnl|CDD|235175 PRK03918, PRK03918, DNA double-strand break repair ATPase Rad50
MKIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSG
TEIELKFEKNGRKYRIVRSFNRGESYLKYLDGSEVLEEGDSSVREWVERLIPYHVFLNAIYIRQGEIDAI
LESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN
EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE
KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL
EKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE
IKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK
KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE
LEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK
AFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK
EELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFEELTEGKYSGVRVKAEE
NKVKLFVVYQGKERPLTFLSGGERIALGLAFRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERY
LRKIPQVIIVSHDEELKDAADYVIRVSLEGGVSKVEVVSL
>gnl|CDD|179676 PRK03922, PRK03922, hypothetical protein; Provisional
MPDYLVVLEAAWIVRDVESVDDAIGVAISEAGKRLNPEDLDYVEVEVGLTICPKCGEPFDSAFVVADTAL
VGLLLEMKVFNAESEEHASRIAKSEIGKALRDIPLEVVEVEEL
>gnl|CDD|179677 PRK03926, PRK03926, mevalonate kinase; Provisional
MVLCSAPGKIYLFGEHAVVYGKPAIACAIDLRTYVRAEFNDDSIYIESDYGKTGEKHPYVSAAIEKMREE
ADKDGVTVSITSQIPVGSGLGSSAAVTVATIGALNRLLGLGLSLEEIAKLGHKVELLVQGAASPTDTYVS
TMGGFVTIPDRKKLPFPECGIVVGYTGSSGSTKELVANVRKLKEEYPELIEPILSSIGKISEKGEELILS
GDYVSLGELMNINQGLLDALGVSTKELSELIYAARTAGALGAKITGAGGGGCMVALAAPEKQSEVATAIK
IAGGKPIITKITDEGLRIEEVR
>gnl|CDD|235176 PRK03932, asnC, asparaginyl-tRNA synthetase; Validated
MMRVSIKDILKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYFEEIKKLTTGSS
VIVTGTVVESPRAGQGYELQATKIEVIGEDPEDYPIQKKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLA
QAIHEFFNENGFVWVDTPIITASDCEGAGELFRVTTLDLDFSKDFFGKEAYLTVSGQLYAEAYAMALGKV
YTFGPTFRAENSNTRRHLAEFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGD
IERLENFIESPFPRITYTEAIEILQKSGKKFEFPVEWGDDLGSEHERYLAEEHFKKPVFVTNYPKDIKAF
YMRLNPDGKTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGL
GFERLVAYITGLDNIRDVIPFPRTPGRAEF
>gnl|CDD|235177 PRK03934, PRK03934, phosphatidylserine decarboxylase; Provisional
MNLSNALSRIFGKFAGYKFPKFIQKFINASYVKIFKIDMSEFKPPENYKSLNALFTRSLKKPREFDEDPN
IFISPCDSLITECGSLEEDKALQIKGMEYSIEELLGESNSELVNGFDYINFYLSPKDYHRYHAPCDLEIL
EARYIPGKLYPVNLPSLEKNKNLFVKNERVVLKCKDKKGKRLYFVFVGALNVGKMRFNFDERIQTNAKAR
FIQTYEYENLKLKKGEELGNFEMGSTIVLFSQKGSLEFNLKAGKSVKFGESIGEI
>gnl|CDD|235178 PRK03941, PRK03941, NTPase; Reviewed
MKVAVGSTNPVKVEAVENVFGKIFDDVEVVGVEVDSGVPDQPFGEETVKGAINRAKNAYSPDFDFSVGIE
AGLFRVPGTITGYVDFQVCAIYDGEKITIGFGPGFEYPPLVVEEVLKGKEVGDVMSELTGIKELGRKIGA
IGFLSRGMLDRTDLTEIAVLMALIPRLNPELYGL
>gnl|CDD|179681 PRK03946, pdxA, 4-hydroxythreonine-4-phosphate dehydrogenase; Provisional
KKKIAISIGDINGIGLEIALKSHDEVSKICEPLYCINEELLEQAAKLLNLKTPNDFEIDFPVGLLFEIKP
GKVSAKSGAYSFESFKKAVELADSKEVDAIVTLPINKKAWQKAGIPYKGHTDALRDRFKKEAIMMLGCEE
LFVALFTDHIPLKKVSQLIKVKKLVKFLLDFYKSTKFKKIGVLGLNPHAGDNGVIGGEEEEIKKAIKKAN
QFLGFEIFFGPLVPDSAFTPNKRKKFNYYVAMYHDQGLAPLKALYFDESINVSLNLPILRTSVDHGTAFD
IAYKNAKANTKSYLNAIKYAINLLSKK
>gnl|CDD|235180 PRK03954, PRK03954, ribonuclease P protein component 4; Validated
MKKKFIRRWEQREKKRIARERIDTLFTLAERVFPYSPELANRYVELALAVQQKAKVKLPRKWKRRYCKRC
HSFLVPGVNARVRLRQKRMPHVVITCLECGHIMRYPYLREVKERRKKKMEG
>gnl|CDD|179684 PRK03955, PRK03955, DUF126 domain-containing protein
MELKGRIISKGKAEGEVIVSKKPISFLGGVDPETGIVIDKEHDLYGESIKGKILVFPHGKGSTVGSYVIY
QLAKNGTAPKAIINLEAEPIVATGAIISGIPLVDKVDISKLKDGDRVVVDGDEGEVEILEQ
>gnl|CDD|179685 PRK03957, PRK03957, V-type ATP synthase subunit F; Provisional
MKIAVVGDRDTVTGFRLAGLTEVYEVKNPEEAKNAIKELVENDEIGIIIITERIAEEIRDLISVALPIIV
EIPDKSGSIERENDPVKELVRRAIGVEMKR
>gnl|CDD|235181 PRK03958, PRK03958, tRNA 2'-O-methylase; Reviewed
MEIVVLRLGHRPERDKRITTHVGLTARALGADKIILASNDEHVKESVEDIVERWGGPFEVEVTKSWKKEI
REWKDGGIVVHLTMYGENIQDVEPEIREAHRKGEPLLIVVGAEKVPREVYELADWNVAVGNQPHSEVAAL
AVFLDRLFEGKELEREFEDAKLKVVPQERGKRVIEN
>gnl|CDD|167649 PRK03963, PRK03963, V-type ATP synthase subunit E; Provisional
MEGAELIIQEINREAEQKIEYILEEAQKEAEKIKEEARKRAESKAEWILRKAKTQAELEKQRIIANAKLE
VRRKRLAVQEELISEVLEAVRERLAELPEDEYFETLKALTKEAVEELGEDKVVVRSNERTLKLIDSRLEE
IRDELGDVEIELGEPIETIGGVIVETKDGTIRVDNTFEARMERLESELRAKIAKALFG
>gnl|CDD|235182 PRK03968, PRK03968, DNA primase large subunit PriL
MVESSMLDPFSEEAKEIVREFGSINDLLEAIPSLVDIELAIERVKWYLEKKPEKNFDHSDYEYLFDLLSF
YALLGALAFSPYGREAELVVESNGKIYEERLRRAKEIEETEIPVKVVNAIEIPEKDRKILERVRGRELPP
EELEDLLPEYKIKWKDLLDLIGSGSLTDLYIRNGRVYLRREEFLKLWSKAFEKNLERAVNRLYEIRDELP
EFYLELAEEIRETAEEEFSERGGAYGSAGAGKLRPEAFPPCIRNTLEGVPSGGRNYAITVLLTSFLSYAR
LCPNPPRRDVKVSDCDPDLRIIEEEILPLIIEAANRCSPPLFEDQPQEIKNIWYHLGFGMTDEPELEDSG
NSTWYFPPNCEKIKAHAPQLCKPDKDCRYIKNPLTYYLRKLYLEGKKKG
>gnl|CDD|179688 PRK03971, PRK03971, deoxyhypusine synthase
MDDPKDIVLKESEELEGIDVEGPDLDGDIDLEEVLDYYAKIGFQATHLGKAIKIWKKIEEKRKKEEATVF
LGYTSNIVSSGLREIIAYLVKEKKVDVIVTTAGGVEEDFIKCLKPFILGEWDVDGAELREKGINRIGNIF
VPNDRYIEFEEYMYEFFEELLAKQREEGKIITASEFCYELGRFMDEKLGKEKEKSILYWAYKNNIPIFCP
AITDGSIGDMLYFFKKEGKDSELGIDIANDIVKLNDLAITAKETACIVLGGSLPKHSIINANLFRGGTDY
AIYITTAMPWDGSLSGAPPEEGVSWGKIKAKADYVEIWADATLVFPLLVYGVFK
>gnl|CDD|179689 PRK03972, PRK03972, ribosomal biogenesis protein; Validated
MMLITTSHRPTRRTRSFGHDLERVFPNSLYLTRGKKTIQDLLMEAYDRGYERLLIINVWKGNPLKMTFIK
VGPEDWGYLGYLYLHGIKLQREMGFRNLRPIREDMPLVITTAKRVGLDHMAFAQVFAELTGGKFVPRGGK
SLQDIADKYNTDVLGVIERHPRGMAVNFYRLDVTKERPVGPLIFVKIWIMEDGRRWDYKEALGIKLKP
>gnl|CDD|179690 PRK03975, tfx, putative transcriptional regulator; Provisional
DAMESFLTERQIEVLRLRERGLTQQEIADILGTSRANVSSIEKRARENIEKARETLAFAETLNAPVRVTI
PAGTDLFDIPKRIYKEADEAGIKVPYDTPELINFIREAAPEAIRGREVKEDFTIYLTSDGDIYVRECDLE
E
>gnl|CDD|235183 PRK03976, rpl37ae, 50S ribosomal protein L37Ae; Reviewed
MMSRTKKVGSAGRFGARYGRKIRKRVADIEEKMRAKHVCPVCGRPKVKRVGTGIWECRKCGAKFAGGAYT
PETPAGKTVTRAIRRAVEEK
>gnl|CDD|235184 PRK03979, PRK03979, ADP-specific phosphofructokinase; Provisional
MEILEHLEDFSNVSIFTAYNSNVDAIKYLNDEDIQKLIEEFNEEEIIERIEEYPREINEPLDFVARLIHA
MKTGKPAEVPLKNEELHEWFDEHLKYDEERMGGQAGIISNLLAILDLKKVIAYTPWLSKKQAEMFVDSDN
LLYPVVENGKLVLKKPREAYKPNDPLKINRIFEFKKGLEFKLGGEKIIVPRSNRFIVSSRPEWLRIEIKD
ELKEFLPEIGKMVDGAILSGYQGIKEEYSDGKTAEYYLKRAKEDIKLLKKKNKDIKIHVEFASIQNREIR
KKIITYILPHVDSVGMDETEIANILNVLGYEELSERILKESRIEDVIEGAKILLDELNLERVQVHTLYYI
MYICKKDNPLSEEELRKSLEFATILAATKAKLGDIKSIEDLKVGLEVPYNEYGELLKERFEEAKKECRLE
EYKIVLIPSRLVENPKSTVGLGDTISAGAFVSYLSLLKKKKKK
>gnl|CDD|235185 PRK03980, PRK03980, flap endonuclease-1; Provisional
MDSKGRITSHLSGIFYRTINLLENGIKPVYVFDGKPPELKAEEIEERREVREEAEEKYEEAKEEGDLEEA
RKYAQRSSRLTDEIVEDSKKLLDLMGIPYVQAPSEGEAQAAYMAKKGDAWAVGSQDYDSLLFGAPRLVRN
LTISGKRKLPGKNVYVEVKPELIELEEVLKELGITREQLIDIAILVGTDYNPGIKGIGPKTALKLIKKHG
DLEKVLEERGFEIENYDEIREFFLNPPVTDDYELKWKEPDKEGIIEFLVEEHDFSEERVKKALERLEKAV
KEKKQTTLDSWF
>gnl|CDD|235186 PRK03982, PRK03982, heat shock protein HtpX; Provisional
MMNQLKTGLLMALLTGLLYAIGYLLGGSIGPIIAILLALIPNLISYYYSDKIVLASYNARIVSEEEAPEL
YRIVERLAERANIPKPKVAIVPTQTPNAFATGRDPKHAVVAVTEGILNLLNEDELEGVIAHELTHIKNRD
TLIQTIAATLAGAIMYLAQWLSWGLWFGGGGRDDRNGGNPIGSLLLIILAPIAATLIQFAISRQREFSAD
EGGARLTGNPLALANALQKLEKGVRYIPLKNGNPATAHMFIINPFRGQFLANLFSTHPPTEERIERLLEM
AQEMGYLF
>gnl|CDD|235187 PRK03983, PRK03983, exosome complex exonuclease Rrp41; Provisional
LQVEPPKLILEDGLRLDGRKPDELRPIKIEVGVLKNADGSAYLEWGNNKIIAAVYGPREMHPRHLQLPDR
AVLRVRYNMAPFSVDERKRPGPDRRSIEISKVIREALEPAIMLELFPRTVIDVFIEVLQADAGTRVAGIT
AASLALADAGIPMRDLVAGCAVGKVDGVIVLDLNKEEDNYGEADMPVAIMPRLGEITLLQLDGNLTREEF
LEALELAKKGIKRIYQLQREALKSKYGEIAEEGE
>gnl|CDD|235188 PRK03987, PRK03987, translation initiation factor IF-2 subunit alpha; Validated
KRKEWPEEGELVVGTVKEVKDFGAFVTLDEYPGKEGFIHISEVASGWVKNIRDHVKEGQKVVCKVIRVDP
RKGHIDLSLKRVNEHQRREKIQEWKNEQKADKWLELAAEKLGKSLEEAWEEVGYKLEDEFGDLYDAFEEA
AIEGEEALDDLGVPEEWADALVEIARENIEVPKVKISGYVDLTSPEPDGVEIIKKALKAAEKANKYEDVE
VEIYYVGAPRYRIDVTAPDYKTAEKALKKIAERAIKVIKKLGGEGSFVREEK
>gnl|CDD|235189 PRK03988, PRK03988, translation initiation factor IF-2 subunit beta; Validated
MSDYYDYEELLDRAYEKLPEKVFKESRFEVPKPDVRIEGNRTIIRNFKEIADRLNRDPKHVAKFLLKELG
TAGNIEGGRLILQGKFSPRVINEKIDRYVKEYVICPECGSPDTKLIKEGRIWVLKCEACGAETPVKPL
>gnl|CDD|235190 PRK03991, PRK03991, threonyl-tRNA synthetase; Validated
MRLLLIHSDYIEYEAKKKTKVAEEIEEEPKSGRLEEALVVFIAVEKGDESNPEGVVEKAVEEIEKVAEQV
KAENIVLYPYAHLSSDLASPKTAVEVLKKLEEELKSEGYEVLRAPFGWYKAFKISCKGHPLSELSRTIRP
EVSEAEKEEEEIESYWYILTPDGELHDPEEFDFSGYEDLKALVDYEVGKKELVGGEPPHVKLMREKELAD
YEPASDVGHMRYYPKGRLIRDLLEDYVYNLVVELGAMPVETPIMYDLSHPAIREHADKFGERQYRVKSDK
KDLMLRFAACFGQFLMLKDMTISYKNLPLKMYELSTYSFRLEQRGELVGLKRLRAFTMPDMHTLCKDMEQ
AMEEFEKQYEMILETGEDLGRDYEVAIRFTEDFYEENKDWIVELVKREGKPVLLEILPERKHYWVLKVEF
AFIDSLGRPIENPTVQIDVENAERFGIKYVDENGEEKYPIILHCSPTGSIERVIYALLEKAAKEEEEGKV
PMLPTWLSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKE
MESGKLTVTIREESEKVEMTLEELIERIKEETKGYPYRPLPLPRLLSKRPKFR
>gnl|CDD|179699 PRK03992, PRK03992, proteasome-activating nucleotidase; Provisional
ERLEALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVK
SSGGPQFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQI
REVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGA
RLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRI
DILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGM
FAIRDDRTEVTMEDFLKAIEKVMGKEEKDSMEEPGVMFA
>gnl|CDD|235191 PRK03995, PRK03995, D-aminoacyl-tRNA deacylase
MMYLIVYSKKDPASQNIKELLIELFGFKETGKFDANPVYVKGGYVIEEIDEDVIYFDYLDEKKGEYIIFL
SRHSSKAKKPSLTVHTPGNPGEASYGGKPKELAIANPRLMTSLLRNLKKLAKELGFEVTFEATHHGPTEL
KVPSVFVEIGSTEEEWKNERAGEILAEAVIEVLDSIEYEKFKPAIGIGGGHYAPKFTKLALESEYCFGHI
IPKYALDHLSEEVLIQAIEKSTPEIDRIVIDWKGVKSEDRERIIEFLEELGIEVEKI
>gnl|CDD|235192 PRK03996, PRK03996, archaeal proteasome endopeptidase complex subunit alpha
MMMQPQQMGYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIF
KIDDHIGAASAGLVADARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLI
AGVDDGGPRLFETDPSGAYLEYKATAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPE
NVEIAYIDVETKKFRKLSVEEIEKYLEKLLK
>gnl|CDD|235193 PRK03999, PRK03999, translation initiation factor IF-5A; Provisional
MSKKQVEVGELKEGSYVVIDGEPCKIVEISKSKPGKHGSAKARIVAIGIFDGQKRSLVQPVDAKVEVPII
EKKTGQVLSIMGDVVQLMDLETYETFEIPIPEELKDKLEPGVEVEYWEAMGRRKIMRVK
>gnl|CDD|235194 PRK04000, PRK04000, translation initiation factor IF-2 subunit gamma; Validated
MMWEKVQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATIRKCPDCEEPEAYTT
EPKCPNCGSETELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIK
NIVIVQNKIDLVSKERALENYEQIKEFVKGTVAENAPIIPVSALHKVNIDALIEAIEEEIPTPERDLDKP
PRMYVARSFDVNKPGTPPEKLKGGVIGGSLIQGVLKVGDEIEIRPGIKVEEGGKTKWEPITTKIVSLRAG
GEKVEEARPGGLVGVGTKLDPSLTKADALAGSVAGKPGTLPPVWESLTIEVHLLERVVGTKEELKVEPIK
TGEPLMLNVGTATTVGVVTSARKDEAEVKLKRPVCAEEGDRVAISRRVGGRWRLIGYGIIK
>gnl|CDD|235195 PRK04004, PRK04004, translation initiation factor IF-2; Validated
EKKLRQPIVVVLGHVDHGKTTLLDKIRGTAVAAKEAGGITQHIGATEVPIDVIEKIAGPLKKPLPIKLKI
PGLLFIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRIPGWK
STEDAPFLESIEKQSQRVQQELEEKLYELIGQLSELGFSADRFDRVKDFTKTVAIVPVSAKTGEGIPDLL
MVLAGLAQRYLEERLKIDVEGPGKGTVLEVKEERGLGTTIDVILYDGTLRKGDTIVVGGKDGPIVTKVRA
LLKPRPLDEMRDPEDKFKPVDEVVAAAGVKISAPDLEDALAGSPLRVVRDEDVEEVKEEVEEEIEEIRIE
TDEEGVVVKADTLGSLEALVNELREEGIPIRKADVGDISKRDVIEASTVAEKDPLYGVILAFNVKVLPDA
EEEAEKSDVKIFTGDVIYQLIEDYEKWVKEQKEAEKEKILEKIVRPAKIRILPGYVFRQSDPAIVGVEVL
GGTIKPGVPLIKEDGKRVGTIKQIQDQGENVKEAKAGMEVAISIDGPTVGRQIKEGDILYVDIPEEHAKI
LEQELKDELSDDEKEALKEILEIKRK
>gnl|CDD|235196 PRK04005, PRK04005, 50S ribosomal protein L18e; Provisional
RLRKLIRDLKKASRENGAPIWKDVAERLEKPRRRRAEVNLSKINRYAKEGDTVVVPGKVLGSGKLDHKVT
VAALSFSETAKEKIEEAGGKALTIEELVEENPKGSNVRIMR
>gnl|CDD|235197 PRK04007, rps28e, 30S ribosomal protein S28e; Validated
MAEEEGTPAEVIEIIGRTGMTGEVTQVKCRILEGRDKGRIITRNVKGPVRVGDILMLRETEREARKLGTR
>gnl|CDD|179708 PRK04012, PRK04012, translation initiation factor IF-1A; Provisional
MKKKQDDEEVTRVRLPMPEEGEVFGVVEQMLGANRVRVRCMDGVERMGRIPGKMKKRMWIREGDVVIVAP
WDFQDEKADIIWRYTKPQVDWLRRKGYISE
>gnl|CDD|101376 PRK04013, argD, acetylornithine/acetyl-lysine aminotransferase; Provisional
MSLYRKRLRLVRGEGIYVWDSQGRRYLDLIAGIGVNVLGHNHPEWVEEMSEQLEKLVVAGPMFEHEEKEE
MLEELSKWVNYEYVYMGNSGTEAVEAALKFARLYTGRKEIIAMTNAFHGRTMGALSATWKPKYREDFEPL
VPGFKHIPFNDVEAAKEAITKETAAVIFEPIQGEGGIVPAKEEFVKTLRDLTEDVGALLIADEVQSGLRT
GKFLAIEHYKVEPDIVTMGKGIGNGVPVSLTLTNFDVERGKHGSTFGGNPLACKAVAVTLRILRRERLVE
KAGEKFIEIKGERVVTTRGRGLMIGIVLKKPVGKYVEELQNRGYLVHTAGQRVIRLLPPLIISKDTMEEA
KSAIEGVINDILGG
>gnl|CDD|235199 PRK04015, PRK04015, DNA/RNA-binding protein AlbA
MAEENVVLVGKKPVMNYVLAVLTQFNQGAKEVVIKARGRAISKAVDVAEIVRNRFLPDVEIKEIKIGTEE
VTSEDGRESNVSTIEIVLEKK
>gnl|CDD|235200 PRK04016, PRK04016, DNA-directed RNA polymerase subunit N; Provisional
MMIPVRCFTCGKVIAEKWEEFKERVEAGEDPGKVLDDLGVKRYCCRRMLLSHVELIDEVIPY
>gnl|CDD|179711 PRK04017, PRK04017, hypothetical protein; Provisional
MYRENYERFEEIIEELKEFSEAGAPIIVEGKRDVESLRKLGVEGEIIKVSRTPLAEIAELIASRGKEVII
LTDFDRKGEELAKKLSEYLQGYGIKVDTEIRRELFSIVKKDIKDIESLYSYVEKLRLIVGPP
>gnl|CDD|179712 PRK04019, rplP0, acidic ribosomal protein P0; Validated
TEHVPEWKKEEVEELKELIKSYPVVGIVDLEGIPARQLQEIRRKLRGKAELKVSKNTLIKRALEEAGEED
LEKLEDYLEGQVALIFTNMNPFKLYKLLEKSKTPAPAKPGDIAPEDIVVPAGPTGFPPGPILSELQKLGI
PARIQKGKIVIKKDTVVAKAGEVISPELANVLQKLGIKPIEVGLDLKAAYEDGVIYTPEVLAIDEEKYRS
DIQEAAQNAFNLAVNAAYPTPETLETLIQKAFREAKALAVEAGIVTPETADDILSKAVAQALALAAALAD
KDALDEELKEVLSAQAQAAAAEEEEEEEEEEEEEEPSEEEAAAGLGALFG
>gnl|CDD|167678 PRK04021, PRK04021, hypothetical protein; Reviewed
MLKETKEGVILQVYVQPKAKENEIEGVDEWRGRLKVKIKAPPVKGKANKELVKFFSKLLGAEVEIIRGET
SREKDLLVKGISLEEVKKKLKL
>gnl|CDD|235202 PRK04023, PRK04023, DNA polymerase II large subunit; Validated
ASEEMEDYFERLEKELDELYEIAEKARSKGLDPSDEVEIPLAKDMAERVEGLVGIKGVAERIRELEKEMS
REEAALEIAKEIAEGKVGEFDSKEEAADQAVRTALAILTEGVVAAPLEGIAKVKIKKNDDGTEYLAIYYA
GPIRSAGGTAQALSVLVGDYVRRKLGLDRYKPTDDEIERYVEEIELYKEVTSLQYSPSDEEIRLIVRNIP
VEIDGEPTEDEEVSGHRDLERVETNRIRGGMLLVLAEGIALKAPKILKYVDKLKIDGWEWLEELISGKKE
KEEEEEKKKIKPKDKYLRDIIAGRPVFSHPSRKGGFRLRYGRSRNTGFATAGIHPATMYLLDDFIAVGTQ
LKVERPGKAACVVPVDSIEGPTVRLKNGDVVRIDDVEEAKEIRDDVEEILDLGEILINYGDFLENNHPLL
PSSYCEEWWIQELEAAGAEYEPEFDLENPSQEEALKISEEYGVPLHPKYTYLWHDISKEELEALRNALAG
GGILEEGVLVLDLSEGVKRILEKLGVPHRVRDGKIVIEEAYPLLYSLGLDELEELKKKLDDGSNVLEAVN
ELSGFEIRPKAPTRIGARMGRPEKAKERKMKPPVHVLFPIGNAGGSTRDINKAAKYKGTIEVEIGRRKCP
SCGKETFYRRCPFCGTHTEPVYRCPRCGIEVEEDECEKCGREPTPYSKRKIDLKELYDRALENLGERKNF
DEVKGVKGLTSKDKIPEPLEKGILRAKHDVYVFKDGTVRYDMTDLPLTHFRPREIGVSVEKLRELGYTHD
IYGNPLESEDQIVELKVQDVIISRDAAEYLLRVAKFIDDLLEKYYGLEPFYNVEKREDLIGHLVIGLAPH
TSAGVVGRIIGFTKANVGYAHPYFHAAKRRNCDGDEDCVMLLLDGLLNFSRSYLPDKRGGQMDAPLVLTT
RIDPKEVDDEAHNMDVVWRYPLEFYEATLEGADPKEVEDIMDTVEDRLGTPEQYEGFMFTHDTSDIAAGP
KVSAYKTLGSMEEKMEAQLELARKIRAVDERDVAERVISSHFLPDLIGNLRAFSRQEFRCTKCGAKYRRP
PLSGKCPKCGGNLILTVHKGSVEKYLEVSKKLAEEYGVSDYTKQRLELLERGIKSLFENDKSKQSGLSDF
F
>gnl|CDD|235203 PRK04024, PRK04024, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
KMMKILLIILDGLGDRPVKELGGKTPLEAANTPNMDKLAKEGICGLMDPISPGVRPGSDTAHLAILGYDP
YKYYTGRGPFEALGVGLDLKPGDVAFRCNFATVDENGVVVDRRAGRISEETEELAKAINEKEEIDGVEII
FKSSTGHRAALVLRGPGLSDKVSDTDPHKEGKKVKESKPLDDSPEAKKTAEILNELTKKAYEVLDDHPVN
KERRKQGLPPANIILLRGAGEVPEIPKFTEKYGLKAACVAGTALIKGIARMVGMDVITVEGATGGKDTNY
MAKAKAAVELLKEYDFVLLNIKGTDEAGHDGDFEGKVEVIEKIDKMLGYILDNLDLDEVYIAVTGDHSTP
VEVKDHSGDPVPILIYGPGVRVDDVEKFNELSAAKGGLGRIRGLDVMPILLDLMNRAEKFGA
>gnl|CDD|235204 PRK04027, PRK04027, 30S ribosomal protein S7P; Reviewed
PESEEAEPMEIKLFGKWDVEEVEVRDPSLKRYINLTPVLVPHTGGRHAKKQFGKAEVPIVERLINKLMRT
ERNTGKKQKAYNIVKEAFEIIEKRTKQNPIQVLVDAIENAAPREETTRIKYGGISYPKAVDVSPQRRVDL
ALRFIAEGARQASFKNKKSIEEALAEEIIAAANNDPKSYAVRKKEEIERVAKSAR
>gnl|CDD|235205 PRK04028, PRK04028, Glu-tRNA(Gln) amidotransferase subunit GatE
MSELDYEELGLKVGLEIHQQLDTKRKLFCNCPTELRDDEPDFEFERYLRPTQSELGEIDRAALEESKKGR
KFIYEAYNDTTCLVEADEEPPHELNEEALDIALAIAKLLNMKPVDEIHVMRKIVIDGSNTSGFQRTALVA
LGGYIETSEGKVGIETICLEEDAARKIEEKGDGVVYSLDRLGIPLIEISTAPDIHSPEQAKEVALKIGML
LRSTGKVKRGLGTIRQDVNVSIAGGARVEIKGVQKLDLIPKVVEYEVQRQLNLLKIRDELKERGASVEDE
IVDVTELFKDTKSKIIKKALKKGGKVLAIKLPGFKGLLGREIQPGRRLGTELADYAKAWGVGGIFHTDEL
PAYGITEEEVEALREALGAGENDAFILVADEEEKAEKALEAVIERAKEALEGVPEETRGALPDGTTRYLR
PLPGAARMYPETDIPPIRITEELLEKIKKNLPELPEEKVERLIKEYGLSEELAEQLAYSERLDLFEELVK
KGVDPTLIASTLENTLKELRREGVDVENITDEHIEEVFKLVSEGKIAKEAIEEILKELAENPGKSAEEAA
EELGLKGLSEEEVEKIIDEIVEENIDFVKEKGMGAFGPLMGEVMAELRGKADGKLVSEILREKLKEILNK
>gnl|CDD|235206 PRK04031, PRK04031, DNA primase; Provisional
MDPDTTKYLIHAEIEADGVVEKPDVVGAIFGQTEGLLGDELDLRELQKTGRIGRIDVEIRSKGGKSKGEI
TIPSSLDRVETAILAAALETIDRVGPCRAKIEVTEIEDVRAEKRKKIVERAKEILKKWFDEKVPDSKEII
EEVREAVRVEEITEYGPEKLPAGPNVDDSDAIIVVEGRADVLNLLRYGIKNAIAVEGTNVPETIIELSKK
KTVTAFLDGDRGGELILKELLQVADIDYVARAPPGKEVEELTKKEIAKALRNKVPVEQYLEELGKKAQKA
AEKVKEEEEKPEKEPAEQPEPEEKEPAPVPAEKEETVREHIKELKGTLEARLLDENWNVIKEVPVRDLVD
KLEEAEDKVYAIVFDGIITQRLLDLASEKGVKYLIGARIGNIVKKPANLRIITFDDLI
>gnl|CDD|235207 PRK04032, PRK04032, CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase
ILPAYVANGSAVLFGGGTPIDFGKTFVDGRRILGDGKTWRGLIGGILFGTLVGLIQNLLVPAYIGALGVA
IILAFLLSFGALLGDMLGSFIKRRLGLERGAPAPLLDQLDFVVGALLFAYLVAPVWTLPVIILILVITPL
LHLLTNIIAYKLGLKDVPW
>gnl|CDD|179721 PRK04034, rps8p, 30S ribosomal protein S8P; Reviewed
MVLLDPLANALSTIKNAEMVGKKEVIIKPASKLIGNVLRVMQDEGYIGEFEYIDDGRAGKFKVELLGRIN
KCGAIKPRYPVKYDEFEKWEKRYLPARDFGILIVSTSKGVMSHKEAREKGIGGVLLAYVY
>gnl|CDD|235208 PRK04036, PRK04036, DNA-directed DNA polymerase II small subunit
TAEIVRKFLERGYLLSPEAYELLKELDEDDLSELIEKIKEGKPDKADVIVIDSEDLEEFLSSADLEEERE
EEEEESESIRESVNPKINTIAKDIEVDIEVEVLSDVTGKSTCTGEVEDFVAYFRDRYEKLSKIIRGRVNH
RPIESLKKLKRGGEEVSIIGMVSDIRSTKNGHKIVELEDTTGTFPVLIMKDREDLAELADELLLDEVIGV
EGTLSGDGGLIFADEIIRPDVPRTKEPPTKDEKVYAVFISDVHVGSKEFLEDAFEKFIDWLNGEVGNEEE
IASRVKYLIIAGDLVDGIGIYPGQEEELEIVDIYEQYEAAAEYLKQIPEDIKIIISPGNHDAVRQAEPQP
AFPEEIRSLFPEHNVTFVSNPALVNLHGVDVLIYHGRSIDDVISLIPGASYEKPGKAMEELLKRRHLAPI
YGGRTPIAPEKEDYLVIDEVPDIFHTGHVHINGYGKYRGVLLINSGTWQAQTEFQKRVNIVPTPARVPIV
DLDTLEVTVLDFDE
>gnl|CDD|235209 PRK04038, rps19p, 30S ribosomal protein S19P; Provisional
PKRWKEFTYRGYTLEELQEMSLEEFAELLPARQRRSLKRGLTPEQRKLLEKIRKARREKKKGRVIRTHVR
DMIILPEMVGLTIAVYNGKEFVEVEIVPEMIGHYLGEFALTRKRVQHGSPGIGATRSSKFVPLK
>gnl|CDD|235210 PRK04040, PRK04040, adenylate kinase; Provisional
MMKVVVVTGVPGVGKTTVLNKALEKLKEDYKIVNFGDVMLEVAKEEGLVEHRDEMRKLPPEEQKELQREA
AERIAEMAGEGPVIVDTHATIKTPAGYLPGLPEWVLEELNPDVIVLIEADPDEILMRRLRDETRRRDVET
EEDIEEHQEMNRAAAMAYAVLTGATVKIVENREGLLEEAAEEIVEVLR
>gnl|CDD|235212 PRK04043, tolB, Tol-Pal system protein TolB
MKILWLFLLFSISLFAVDATLDIVKKGQKLPKIVVEDASDLNDANLKKKFFKILVNDLKVSSHFEVSENK
DQSSGDINYNELKDKKVDLVFRYSLANKNGNKLSLRVKLYDVNTGSLKFEKDYTINSLDRYPFLAHKSAI
DINDYLKAPSIDWMKRKVVFSKYTGPKKSNIVLADYTLTYQKVIVKGGLNIFPKWANKEQTAFYYTSYGE
RKPTLYKYNLYTGKKEKIASSQGMLVVSDVSKDGSKLLLTMAPKGQPDIYLYDTNTKTLTQITNYPGIDV
NGNFVEDDKRIVFVSDRLGYPNIFMKKLNSGSVEQVVFHGKNNSSVSTYKNYIVYSSRETNNEFGKNTFN
LYLISTNSDYIRRLTANGVNQFPRFSSDGGSIMFIKYLGNQSALGIIRLNYNKSFLFPLKVGKIQSIDW
>gnl|CDD|235213 PRK04044, rps5p, 30S ribosomal protein S5P; Reviewed
VMKFNIEEWEPKTRLGRLVKEGKITSIDEIFDSGLPIKEPEIVDVLLPDLEDEVLDINMVQRMTDSGRRV
RFRVVVVVGNRDGYVGVGQGKAKQVGPAIRKAIRNAKLNIIKVRRGCGSWECGCGEPHSVPFKVTGKAGS
VEVTLKPAPRGLGLVAGDVAKKVLELAGIKDVWTRTFGETRTTVNFAKATFNALKNTYKVRTPPDWAEKR
G
>gnl|CDD|179728 PRK04046, PRK04046, translation initiation factor IF-6; Provisional
MIRRLSIFGSPNIGVYARATDDYALVPPDLDEKTVEKIEETLGVEVVETTIAGSSLVGSLAAGNSNGILV
PSIVLDEELELLKEALDLNVEVLPSKLTALGNLILANDKGALVHPELSDEARKVIEDTLGVEVERGTIAG
LKTVGSAGVVTNKGGLVHPDATDEELKFLEDLFKVEVDIGTVNFGSPLVGSGLVANSKGAVVGSDTTGPE
LGRIEDALGFIE
>gnl|CDD|235214 PRK04049, PRK04049, 30S ribosomal protein S8e; Validated
MMIWQGRSLRKPTGGRKRPARKKRKYELGREPTETTVGEDKRKIVRVRGGNRKVRLLRANYANVADPKTG
KTKKVKILTVVENPANPHYARRNIITKGAIIETELGKAKVTSRPGQDGVVNAVLIEE
>gnl|CDD|179730 PRK04051, rps4p, 30S ribosomal protein S4P; Validated
MGDPKKPRKKYETPNHPWQKERIAEERELLGKYGLRNKRELWKAQSILRKYRRQARSLLALPPEERAKEE
EQLLGKLKRYGILKENATLDDVLSLTVEDILERRLQTIVYRKGLARTPKQARQFIVHGHIAVNGRRVTSP
SYLVSVEEEDLIDYYPTSPLADELHPERAEAQAEAEV
>gnl|CDD|235215 PRK04053, rps13p, 30S ribosomal protein S13P; Reviewed
MMEEEFKYIVRIAGTDLDGTKPVEYALTGIKGIGRRTARAIARKLGLDPNAKLGYLSDEEIEKIEEALED
PAEEGIPSWMLNRRKDYETGEDLHLIGSDLILTVREDINRMKKIRSYRGIRHELGLKVRGQRTRSTGRTG
GTVGVSRKK
>gnl|CDD|179732 PRK04056, PRK04056, septum formation inhibitor Maf
MIILASSSSTRANLLKEAGIEFEQKSLDFDEESIKKTSPKEFVYLAVKGKLEQFLKKYGNECNLLVADSV
VSCGNKILRKAKDKEEAREMLKLQSGNEISVLTCMILKSPEKEWLDLSVTTYRFKKFDEDDLEKYLESGL
WQGKAGACMVEGFHKKYIKSVSGNESTAMGLNVEKLKGFL
>gnl|CDD|235216 PRK04057, PRK04057, 30S ribosomal protein S3Ae; Validated
RVKDKWKEKKWYTVYAPEFFGGVEIGETPADDPEKLIGRVVETTLGDLTGDFSKQNVKLYFKIDNVEGDK
AYTRFIGHELTRDYLRSLVRRRTSKIDAIVDVTTKDGYKVRVKPVALTTKRARTSQKHAIRKIMEEIIEE
KASELTFEEFVQEIVFGKLASEIYKEAKKIYPLRRVEIRKSKVLARPEEVEAEEEVAVAAEEA
>gnl|CDD|179734 PRK04059, rpl34e, 50S ribosomal protein L34e; Validated
MPAPRYRSRSLRRVYVRTPGGRTVIHYERKKPSKAKCAICGKPLNGVPRGRPVEIRKLGKTEKRPERPYG
GYLCPKCLKRLIKAKARN
>gnl|CDD|235217 PRK04069, PRK04069, serine-protein kinase RsbW; Provisional
MMEKFDKIEMKIPAKAEYVSIIRLTLSGVANRMGFSYDDIEDMKIAVSEACTNAVQHAYKEDEVGEIHIR
FEIYEDRLEIVVADNGVSFDYETLKSKLGPYDISKPIEDLREGGLGLFLIETLMDDVTVYKDSGVTVSMT
KYINREQVENNGERISTSESQ
>gnl|CDD|179736 PRK04073, rocD, ornithine--oxo-acid transaminase; Provisional
MTKSEKIIELTNHYGAHNYHPLPIVISEAEGVWVKDPEGNRYMDMLSAYSAVNQGHRHPKIIQALKDQAD
KVTLTSRAFHSDQLGPWYEKVAKLTGKDMVLPMNTGAEAVETAIKAARRWAYDVKGVEPNKAEIIACEGN
FHGRTMAAVSLSSEEEYKRGFGPMLPGIKKIPYGDLEALKAAITPNTAAFLVEPIQGEAGINIPPEGFLK
AARELCKEENVLFIADEIQTGLGRTGKLFACDWDNVTPDMYILGKALGGGVFPISCVAANRDILGVFTPG
SHGSTFGGNPLACAVSIAALEVLEEEKLPERSLELGEYFKEQLKEIDNPMIKEVRGRGLFIGVELNEPAR
PYCEALKEEGLLCKETHETVIRFAPPLVITKEELDWAFEKIKAVLS
>gnl|CDD|235218 PRK04081, PRK04081, hypothetical protein; Provisional
MKHIKKISDYAIVGGLGALVMVGLVGCGSNSDQNQKENSSLQASQQQGAFVIIEEQADGSYKILEEYPSS
ETRVVLRDLDGTERVLSQEEIDKLIKEEEAKIDNGTSNLTNPNNSNSSGGMGLGGTILASAAGAILGSWI
GNKLFNNQNYQNQRQRTYKSPQAYQRSQNSFNKAASASSSSGSSSKKSGFFGGSSSASSSSSSSFGS
>gnl|CDD|179740 PRK04101, PRK04101, metallothiol transferase FosB
MLKGINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLWIALNEEKDIPRNEIHQSYTHIAFS
IEEEDFDHWYQRLKENDVNILPGRERDERDKKSIYFTDPDGHKFEFHTGTLQDRLNYYKEEKPHMTFYD
>gnl|CDD|235220 PRK04115, PRK04115, hypothetical protein; Provisional
MDIVEKILKKEIRRVNSHLPRKRKTLCELLKEDKPHVILRDGSRHRIKRRELEFLKELLDEDACRLRLPI
ILEIDSSLGEGAIVVRGKEEVKVISKILGKEDIFSEEDILYLYRPELREVRRKLPTTTQYAFRVSLR
>gnl|CDD|235221 PRK04123, PRK04123, ribulokinase; Provisional
MMAYVIGLDFGTDSVRALLVDCATGEELATAVVEYPHWVKGRYLDLPPNQALQHPLDYIESLEAAIPAVL
KEAGVDPAAVVGIGVDFTGSTPAPVDADGTPLALLPEFAENPHAMVKLWKDHTAQEEAEEINRLAHERGE
ADLSRYIGGIYSSEWFWAKILHVLREDPAVYEAAASWVEACDWVVALLTGTTDPQDIVRSRCAAGHKALW
HESWGGLPSADFFDALDPLLARGLRDKLFTETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAV
GAGAEPGTLVKVMGTSTCDILLADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIFAWFARLLVPPEY
KDEAEARGKQLLELLTEAAAKQPPGEHGLVALDWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEA
TAFGTRAIMECFEDQGVPVEEVIAAGGIARKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGA
YPDIPEAQQAMASPVEKTYQPDPENVARYEQLYQEYKQLHDYFGRGGNAVMKRLKAIR
>gnl|CDD|235222 PRK04125, PRK04125, antiholin-like protein LrgA
MSAKKVYSFLHQAFIFAAIMLISNIIASFLPIPMPASVIGLVLLFVLLCTKVVKLEQVESLGTALTNNIG
FLFVPSGISVINSLGVMSQYPVQIIGVIIVATILLLACTGLFSQFILGKTEKEKEDKKEKKVKIKGRQHG
K
>gnl|CDD|167709 PRK04128, PRK04128, 1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase
MMRIYPAIDLMNGKAVRLYKGRKEEVKVYGDPVEIALRFSEYVDKIHVVDLDGAFEGKPKNLDVVKNIIR
ETGLKVQVGGGLRTYESIKDAYEIGVENVIIGTKAFDLEFLEKVTSEFEGITVSLDVKGGRIAVKGWLEE
SSIKVEDAYEMLKNYVNRFIYTSIERDGTLTGIEEIERFWGDEEFIYAGGVSSAEDVKKLAEIGFSGVII
GKALYEGRISLEELLEVQ
>gnl|CDD|235223 PRK04132, PRK04132, replication factor C small subunit; Provisional
EVKVLEKPWVEKYRPQRLDDIVGQEHIVKRLKHYVKTGSMPHLLFAGPPGVGKCLTGDTKVIANGELFEI
GELVEKISNGKFGPTPVNGLKVLGIDEDGKLREFEVQYVYKDKTNRLIKIKTRLGRELKVTPYHPLLVNR
KNGEIKWVKAEELKPGDKLAIPRFLPAIEGENPLAEWLGYFIGDGYADSKENVITFTNEDPKLRQRFMEL
TEKLFKDAKIKERIHKDRTPDVYVNSKEAWELVDSLGLRRIPKEGWKGLRSFLRAYFDCNGGIEKDAIVL
STASKEMAEQIVYALAGFGIIAKLREKYHVIISGSENLKRFLDEIGFSQEEKLEKALKLIKKENPNLDGL
TIDKELISYVRDRLKLKFTRDKRNWSYRKAREISWELMKEIYYRLEELERLKKALSESILIDWNEVAKRR
KEIAEKTGIRADRILEYIKGKRKPSLKNYIKIAKALGINLEKTIEAMRIFAKKYSSYAEIGRMLGTWNSS
VKIILESNTQEIEKLEEIRKIELKLIKEILNDEKLKEGIAYLIFLAQNELYWDEITEVEELKGDFIIYDL
HVPGYHNFIGGNLPTVLHNTTAALALARELFGENWRHNFLELNASDERGINVIREKVKEFARTKPIGGAS
FKIIFLDEADALTQDAQQALRRTMEMFSSNVRFILSCNYSSKIIEPIQSRCAIFRFRPLRDEDIAKRLRY
IAENEGLELTEEGLQAILYIAEGDMRRAINILQAAAALDDKITDENVFLVASRARPEDIREMMLLALKGN
FLKAREKLREILLKQGLSGEDVLVQMHREVFNLPIDEPKKVELADKIGEYNFRLVEGANEMIQLEALLAQ
FTLMGK
>gnl|CDD|179745 PRK04135, PRK04135, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
ELVQKNDSKIVLLVLDGLGGLPHPENGKTELEAAKTPNLDALAKESDLGLLIPVLPGITPGSGPGHLGLF
GYDPLKYQIGRGILEALGIGFELGEGDVAARGNFATVDGEGIIVDRRAGRPSTEENAKLVAKLSEAIKEI
EGVEVFFYPGKEHRFVVVFRGEGLSDKVTDTDPQKTGVPPLEAKALDEESEKTARIVNEFLKRAAEVLKD
EPKANFALLRGFSKKPDFPSFEEVYKLKAAAIASYPMYRGLAKLVGMDVLPTGQTLEDEIKTLKENWNDY
DFFFLHVKKTDSYGEDGNFEEKVKVIEEVDALLPEILALKPDVLVITGDHSTPAVLKGHSWHPVPLLLYS
KYCRPDLSQRFTERECARGGLGHIPAVDLMPLALAHALRLEKYGA
>gnl|CDD|179746 PRK04136, rpl40e, 50S ribosomal protein L40e; Provisional
PAKFEEAEKRVFNKKICMRCNARNPWRATKCRKCGYKNLRPKAKELRG
>gnl|CDD|235224 PRK04140, PRK04140, transcriptional regulator
MREALISEVIALLEDAGFKVSDRCPIRPSCFDLVARRGDLLLLLKILYNIDSLSEEQAEELKRLAKYLKA
SPLIIGLRTRNEELEDGVVYERHGIPALSPDTLYDDFVEGEPPLIYAAPGGFYVKIDGDVLREAREELGL
SLGELASELGVSRRTISKYENGGMNASIEVAIKLEEILDVPLTKPIDILEKVRDDEVTPEDPEEDPFEKE
ILNVLTRLGFDVLPTKKAPFDAVSEDEKDENILLTGISEFNEETEKRARIVSSISEVTNSRSVFILEEKT
KRESVKGTPVISKEELEKIDDADELLELIEERKKNIK
>gnl|CDD|235225 PRK04143, PRK04143, protein-ADP-ribose hydrolase
MPSQKARLEYLINYLQKEQLTSDVLPLPNDLEEQQDLLRALANVRPALPLSDEYLNLQDAYLQDENAERG
VVDLKDLQPIKYDNIFLWQGDITRLKVDAIVNAANSRLLGCFQPNHDCIDNAIHTFAGVQLRLDCAEIMT
EQGRKEATGQAKITRAYNLPAKYVIHTVGPIIRKQPVSPIRADLLASCYRSCLKLAEKAGLKSIAFCCIS
TGVFGFPKEEAAEIAIKTVLSWLKENPSKLKVVFNVFTDEDLELYQKALNKENN
>gnl|CDD|179749 PRK04147, PRK04147, N-acetylneuraminate lyase; Provisional
AKNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEA
KGKVKLIAQVGSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPA
LTGVNLSLDQFNELFTLPKVIGVKQTAGDLYQLERIRKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYN
VNGWRARQIFEAAKAGDIQEAQELQHECNDVIDLLIKNGVYPGLKEILHYMGVDAGLCRKPFKPVDEKYL
PALKALAAKYLKE
>gnl|CDD|235226 PRK04148, PRK04148, hypothetical protein; Provisional
MDTIAEFIAENYEKGKNKKIVELGIGFYFKVAKKLKESGFDVIVIDINEKAVEKAKKLGLNAFVDDLFNP
NLEIYKNAKLIYSIRPPRDLQPFILELAKKINVPLIIKPLSGEEPIKELKLINYKGKPIYVWKP
>gnl|CDD|235227 PRK04149, sat, sulfate adenylyltransferase; Reviewed
MMLIPPHGGELVNRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEE
MRLANGLVWSIPITLDVSEEDAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPG
VKKLYEQGDVYLAGPVTLLNRKFHEPFPRFWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQKCAL
EIVDGLLLNPLVGETKSGDIPAEVRMEAYEALLKNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYG
CTHFIVGRDHAGVGDYYGPYDAQEIFDEFTEEELGITPLKFEEAFYCPKCGGMASEKTCPHGKEDRVHLS
GTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKYGYPSPFV
>gnl|CDD|179752 PRK04151, PRK04151, IMP cyclohydrolase; Provisional
MYVGRFLVVGKTEEGKPFAAYRVSSRSFPNRRAVVRDNTVAIVPKDDAEETKNPYISYNCVRIVDDTAVV
TNGSHTDPIAEKLELGYPARDALAYSLLAMDYEKDDYNTPRIAGVVGKDEAYIGIVRKDALRVRKVELED
GEAYLVATYEKDEPEPIELDAETAEEAAKFIYDLEFEHPVCAAGAVRDGDGWELATY
>gnl|CDD|235228 PRK04155, PRK04155, protein deglycase HchA
QMTVQTSKNPTPDPAEDNAFFPSPYSLSQYTSPKSDLDGVDYPKPYRGGKKILMIAADERYLPMDNGKLF
STGNHPVETLLPMYHLHKAGFEFDVATLSGNPVKFEYWAMPHEDEAVMGFYEKYKSKFKQPKKLADVVAN
LLAPDSDYAAVFIPGGHGALIGLPESEDVAAALQWALDNDRFIITLCHGPAALLAAGVDHGDNPLNGYSI
CAFPDALDKQTPEIGYMPGHLTWLFGEELKKMGVNIVNDDITGRVHKDRKLLTGDSPLASNALGKLAAQE
LLAAVAG
>gnl|CDD|235229 PRK04156, gltX, glutamyl-tRNA synthetase; Provisional
LREEIEELIYKYALQNAVKHGGKANVKAVMGKIMGENPELRSKAKEIIPIVKEVVEEVNSLSLEEQRERL
EELAPELLEEEEEKKEEKKGLPPLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRF
EDTDPRTKRPDPEAYDMILEDLKWLGVKWDEVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRD
AGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVW
PTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWEYPETIHYGRLKIEGFVLSTSKIRKGIEE
GEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPIANRYFFVRDPV
ELEIEGAEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEAEGKMVRLMDLFNVEITGVSVDKARYHS
DDLEEARKNKAPIIQWVPEDESVPVRVLKPDGGDIEGLAEPDVADLEVDDIVQFERFGFVRIDSVEDDEV
VAYFAHK
>gnl|CDD|235230 PRK04158, PRK04158, GTP-sensing pleiotropic transcriptional regulator CodY
MMSLLEKTRKINRLLQKSAGEPVDFNEMAEVLSDVIDCNVYIVSRKGKILGYSMKEKIENDRVEQMLEER
QFPEEYNEKLLNVYETEANLDVESELTVFPVENKCLFPDKLTTIVPIIGGGERLGTLILARFDKEFTDDD
LILAEYAATVVGMEILREKAEEIEEEARKKAVVQMAINTLSYSELEAVEHIFEELDGNEGLLVASKIADR
VGITRSVIVNALRKLESAGVIESRSLGMKGTYIKVLNDKLLDELKK
>gnl|CDD|235232 PRK04161, PRK04161, tagatose 1,6-diphosphate aldolase; Reviewed
MTISANKRHYLEKVSNSQGIISALAFDQRGALKRMMAAHQEGEATVTQIETLKVLVSEELTPYASSILLD
PEYGLPATKVRANQTGLLLAYEKTGYDATTTSRLPDCLVEWSVKRLKEAGADAVKFLLYYDVDGDEEIND
QKQAYIERIGSECTAEDIPFFLELLTYDERISDNNSAAYAKLKPHKVNGAMKVFSDKRFGVDVLKVEVPV
NMAYVEGFTEGEVVYSQEEAIKAFKDQEAATHLPYIYLSAGVSAKLFQETLVFAAEAGAQFNGVLCGRAT
WAGSVPVYITEGEEAARKWLCTEGFQNIDELNRVLEETASPWTEKIEVK
>gnl|CDD|235233 PRK04163, PRK04163, exosome complex protein Rrp4
MKIFVEDRKIVVPGDLLAEGEFKAGRGTYKENGKIYSTVVGLVDIKDDKVRVIPLEGKYIPKVGDLVIGK
VTDVTFSGWEVDINSPYKAYLPVSEVLGRPVNVEGTDLRKYLDIGDYIIAKVKDVDRTRDVVLTLKGKGL
GKIEGGTIVEIKPVKVPRVIGKKGSMINMLKEETGCDIIVGQNGRIWIKGPDEEDEEIAIEAIKKIEREA
HTSGLTDRIKEFLEEELGERGESSE
>gnl|CDD|235234 PRK04164, PRK04164, hypothetical protein; Provisional
FITFNPLLMALLIFIIRIIYVSILTIRTILTVKGYRYLAALLGFLEVLIYVVALGLVFQNLDNPQNIIAY
ALGFAVGIYVGMKIEEKLALGYITVRVITKEYELELANELRELGYGVTVFDAEGRDGPRMVLFILTKRKR
EKELLEIIKELDPKAFIISYEPRSFKGGFWTKGVRKRKKKD
>gnl|CDD|235235 PRK04165, PRK04165, acetyl-CoA decarbonylase/synthase complex subunit gamma; Provisional
MALTGLDIYKLLPKTNCGECGEPTCLAFAMKLASGKAELDDCPYLSEEAKEKLEEASAPPIREVKIGTGE
RAVKIGGETVLYRHEKTFFNPTGIAVDVSDTMDDEEIDARLKKINNFQFERVGEILKLDMVALRNASGDP
EKFAKAVKKVAETTDLPLILCSEDPAVLKAALEVVADRKPLLYAATKENYEEMAELAKEYNCPLVVKAPN
LEELKELVEKLQAAGIKDLVLDPGTENIKETLDDFVQIRRAAIKKGDRPLGYPIIAFPIEAWMSDPMKEA
AIASTLIAKYADILVLHDIEPWELLPLLTLRQNIYTDPQKPVAVEPGIYEIGNPDENSPVLVTTNFALTY
FTVEGDIESSKVPCYLLVVDTEGLSVLTAWAAGKFTGEKIADFIKESGIEEKVNHRKLIIPGLAAVLSGD
IEELTGWEVLVGPRESSGIPAFLKKNWPPK
>gnl|CDD|235236 PRK04168, PRK04168, tungstate ABC transporter substrate-binding protein WtpA
MKMKVKIILIILLLLLVLAFAGCVTAFAEPKGKLKIFHAGSLSVPFEEYEKEFEAYHPNVDVQREAGGSV
KCVRKITELGKKADIMASADYTLIPKMMMPDYADWYVRFATNEIVLAYTDKSKYADEINSDNWYEILQRP
DVKFGFSDPNDDPCGYRSLMVLQLAELYYNDPTIYDKLIAKNTNIKVNENLIISPKEIEVNTDKVFVRPK
EVELLSLLETGNMDYAFIYKSVAVQHNLKYIELPDEINLGNYKYADFYKKVSVTVTGTGKTITAKPIVYG
ITVPKNAPNREAAIEFLKYLLSEPGGEVLENNGQPPIVPAIAFGNVPEELKDLV
>gnl|CDD|235237 PRK04169, PRK04169, heptaprenylglyceryl phosphate synthase
MMIDWKGWLHVTLLDPDKPLPDEALEAICESGTDAIIVGGSDGVTEENVDELVKAIKEYDLPVILFPGNI
EGISPGADAYLFPSVLNSRNPYWIIGAHVEAAPIIKKGGLEVIPEGYIVLNPGSKVAVVGTAAPIPLDKP
DIAAYAALAAEYLGMPIVYLEYGGGAGDPVPPEMVKAVKKALDITPLIYGGGIRSPEQARELMAAGADTI
VVGNIIEEDPKKTVKAIKKAIK
>gnl|CDD|235238 PRK04171, PRK04171, 16S rRNA (pseudouridine)(914)-N(1))-methyltransferase Nep1
MLNLVLAESALELVPREIWNHPAVVKNARRRGKKPEEMLLDSSLHYHAMKKLEDKEKRGRPDIVHISLLV
ALDSPLNKEGKLRVYIHTRDDKVIYVNPETRLPKNYNRFVGLMEQLLKEGRVPPNGEPLLEIENKSLEEL
LEEIGPDRIILLSEKGELVKPKELGKENENIAVGIGGFPHGDFSEKVLELAKKKYSIYGEPLTAWTVVCR
VIAAYERLLGLL
>gnl|CDD|235239 PRK04172, pheS, phenylalanine--tRNA ligase subunit alpha
MMELHPNEKKVLKALKELKEATLEELAEKLGLPPEAVMRAAEWLEEKGLVKVEERVEEVYVLTEEGKKYA
EEGLPERRLLNALKDGGEVSLDELKEALLDKKEVGIALGNLARKGWAKIEKGKVILKPDAYEDPEEKALK
ALAEGDKEELSEEDLKVLKELKKRKLVEEKERTERSVELTDAGLELLKEGIELKEEITQLTPELLKSGEW
KEKEFRPYNVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNFDALFQPQDHPAREM
QDTFYLKYPGIGDLPEELVERVKEVHEHGGDTGSRGWGYKWDEDIAKRLVLRTHTTALSARYLASRPEPP
QKYFSIGRVFRPDTIDATHLPEFYQLEGIVMGEDVSFRDLLGILKEFYKRLGFEEVKFRPAYFPFTEPSV
EVEVYHEGLGWVELGGAGIFRPEVLEPLGIDVPVLAWGLGIERLAMLRLGLDDIRDLYSSDIEWLRERP
>gnl|CDD|235240 PRK04173, PRK04173, glycyl-tRNA synthetase; Provisional
MDKMEKIVSLAKRRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQEREDVVGIDSPIIMPP
EVWEASGHVDNFSDPLVECKKCKKRYRADHLIEELGIDAEGLSNEELKELIRENDIKCPECGGENWTEVR
QFNLMFKTFIGPVEDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTR
EFEQMELEFFVKPGTDNEWFAYWIELRKNWLLDLGIDPENLRFREHLPEELAHYSKATWDIEYKFPFGRF
WGELEGIANRTDYDLSRHSKHSGEDLSYFDDETTGEKYIPYVIEPSAGLDRLLLAFLEDAYTEEELGGGD
KRTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAELRKDFNVDYDDSGSIGKRYRRQDEIGTPFCITV
DFDTLEDNTVTIRDRDTMEQVRVKIDELKDYLAEKL
>gnl|CDD|235242 PRK04179, rpl37e, 50S ribosomal protein L37e; Reviewed
MSKGTPSMGKRNKGKTHIRCRRCGRHSYNVRKKYCAACGFGRSKRIRRYSWQNKKVNGKRIK
>gnl|CDD|179769 PRK04180, PRK04180, pyridoxal 5'-phosphate synthase lyase subunit PdxS
LETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIM
DAVSIPVMAKARIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAE
GAAMIRTKGEAGTGNVVEAVRHMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFA
AGGIATPADAALMMQLGADGVFVGSGIFKSGDPEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDID
ELPPEERLQERGW
>gnl|CDD|235243 PRK04181, PRK04181, 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Provisional
MVMKAYAKVNIFLKILGKRGNYHELISRFVLVKDLFDEIEFVPKSAESFELIGNFDCPLEENIIYKAYQE
LKNKGFSNELIEFFKKKAIEVEKNIPTGAGLGGGSSDAATFLLMLNEILNLKLSLEELAEIGSKVGADVA
FFISGYKSANVSGIGEIVEEFEEEILNLEIFTPNIFCSTKAVYKAYREEFYDFISFNQAKELLKLSSLEL
LKNFKNTELNDLLAPALKLYPALKDYLGEDWFFSGSGSSFFRVKRAQ
>gnl|CDD|235244 PRK04182, PRK04182, cytidylate kinase; Provisional
MIITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFRELAKERGMSLEEFNKYAEEDPEIDKEIDRRQLEI
AEKEDNVVLEGRLAGWMAKDYADLKIWLKAPLEVRAERIAEREGISVEEALEETIEREESEAKRYKEYYG
IDIDDLSIYDLVINTSRWDPEGVFDIILTAIDKLLKAKDE
>gnl|CDD|235245 PRK04183, PRK04183, Glu-tRNA(Gln) amidotransferase subunit GatD
LGMEVGDRVRVEKDDVVYEGILMPSYEDDHIVIKLDNGYNIGIDIDKIAEIELLEKGEKPKQEPPPKEIE
KDPGLPNVSILSTGGTIASKVDYRTGAVTPAFTAEDLLRAVPELLDIANIRGRVLFNILSENMTPEYWVE
IAEAVYEEIKNGADGVVVAHGTDTMHYTAAALSFMLKTPVPIVFVGAQRSSDRPSSDAAMNLICAVLAAT
SDIAEVVVVMHGTTSDDYCALHRGTRVRKMHTSRRDAFQSINDKPLAKVDYKEGKIEFLRKDYRKRGEKE
LELNDKLEEKVALIKFYPGMDPEILDFYVDKGYKGIVIEGTGLGHVSTDLIPSIKRATDDGIPVVMTSQC
LYGRVNMNVYSTGRDLLKAGVIPGEDMLPEVAYVKLMWVLGNTYDLEEVRELMLTNLAGEINERSRLDL
>gnl|CDD|235246 PRK04184, PRK04184, DNA topoisomerase VI subunit B; Validated
MAIAEELAKEKFREISVAEFFEKNKELLGFDNPARALYTTVKELVDNSLDACEEAGILPDIKIEIKRVDE
GKDHYRVTVEDNGPGIPPEEIPKVFGKLLYGSKFHNLRQSRGQQGIGISAAVLYAQMTTGKPVRVISSTG
GSKKAYYFELKIDTKKNEPIILEREEVDWDRWHGTRVELEIEGDWYRAKQRIYEYLKRTAIVNPHARITF
KDPDGEILVFPRATDKLPKPPKEIKPHPHGVDLGTLKRMAARTKRRTLKEFLVEEFSRVGDKTADEILEK
AGLDPNKKPKELTREELERLVEAFKKYKFMAPPTACLSPIGEELIEKGLKKILKPEFVAAVTRKPKVYSG
HPFIVEVGIAYGGEIPPDDKPELLRFANRVPLLYDEGSCVITKAVESIDWKRYGIEQPPQAPLVVLVHVA
STKVPYTSEGKEAIADVPEIEKEIRLALQEVARKLKKYLSRKRKEEEAKKKAKTFEKYIPEIARKLAEIL
EKEEPDIEEVLAKLIGKKLEEEEVEEEEEEEAVVVESAKNYTEKD
>gnl|CDD|179774 PRK04190, PRK04190, glucose-6-phosphate isomerase; Provisional
MELKEPIGPQVDLETGVLPGATKKYQRRLSDLAGLFADEEAFRAMPATEDTVVYEVYAIEPEETEGDLNF
GTTRLYPGKVGDEYFMTKGHFHAKADRAEIYYGLKGKGLMLLQDPEGEARWIEMEPGTVVYVPPYWAHRS
VNTGDEPLVFLACYPADAGHDYGTIAEKGFSKIVIEENGEVKVVDNPRWKA
>gnl|CDD|235247 PRK04191, rps3p, 30S ribosomal protein S3P; Reviewed
MAIEKKFVEEGLKKVMIDEYLAKELYRAGYGGMEIKKTPLGTRITIYAERPGMVIGRGGKNIRELTEILE
KKFGLENPQIDVKEVENPELNARVVAFRLANALERGWHFRRAAHSAIRRIMEAGALGVEIIISGKLTGER
ARTEKFTEGYIKKSGEPAEELVDRGFAIAKLKLGIIGVEVRIMPPDAKLPDEIEIKEPVEVEEVVEE
>gnl|CDD|235248 PRK04192, PRK04192, V-type ATP synthase subunit A; Provisional
MMTKGKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGE
PLSVELGPGLLGSIFDGIQRPLDELAEKSGDFLERGVYVPALDREKKWEFTPTVKVGDKVEAGDILGTVQ
ETPSIEHKIMVPPGVSGTVKEIVSEGDYTVDDTIAVLEDEDGEGVELTMMQKWPVRRPRPYKEKLPPVEP
LITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELID
PKTGRPLMERTVLIANTSNMPVAAREASIYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEM
PGEEGYPAYLASRLAEFYERAGRVKTLGGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELA
DRRHFPAINWLTSYSLYLDQVAPWWEENVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLIL
EVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKGVPVSEILELEVRDRIARLKYI
PENEYLEKIDEIFEKLEEELEELIAE
>gnl|CDD|235250 PRK04195, PRK04195, replication factor C large subunit; Provisional
MMPWVEKYRPKTLSDVVGNEKAKEQLREWIESWLKGKPKKALLLYGPPGVGKTSLAHALANDYGWEVIEL
NASDQRTADVIERVAGEAATSGSLFGARRKLILLDEVDGIHGNEDRGGARAILELIKKAKQPIILTANDP
YDPSLRELRNACLMIEFKRLSTRSIVPVLKRICRKEGIECDDEALKEIAERSGGDLRSAINDLQAIAEGY
GKLTLEDVKTLGRRDREESIFDALDAVFKARNADQALEASYDVDEDPDDLIEWIDENIPKEYDDPEDIAR
AYDALSRADIFLGRVKRTQNYDLWRYASDLMTAGVALAKEKKKRGFTRYQPPSYWRLLSKTKEKRETRDS
IAKKIAEKLHTSKRKVRREVLPFLSIIFKHNPELAARLAAFLELTEEEIEFLTGSKKATKKIKKIVEKAE
KKREEEKKEKKKKAFAGKKKEEEEEEEKEKKEEEKEEEEEEAEEEKEEEEEKKKKQATLFDF
>gnl|CDD|235251 PRK04196, PRK04196, V-type ATP synthase subunit B; Provisional
LKEYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVR
FTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTL
VRGQKLPIFSGSGLPHNELAAQIARQAKVLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFL
NLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDL
ATIYERAGRIKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRL
MKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQGFDENR
SIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRGKE
>gnl|CDD|235252 PRK04199, rpl10e, 50S ribosomal protein L16
MPLRPARCYRHISKPAYTRREYIGGVPGPKIVKFDMGNLSGDFPVEVSLVVEEPCQIRHNALEAARIAAN
KYLTKTVGRSNYHLKIRVYPHHVLRENKMATGAGADRVSDGMRLAFGKPVGTAARVEKGQKIFTVRVNPE
HLEAAKEALRRAAMKLPTPCRIVVEKGKELLK
>gnl|CDD|179781 PRK04200, PRK04200, cofactor-independent phosphoglycerate mutase; Provisional
MKYIILIGDGMADEPIEELGGKTPLQAAKTPNMDKMAREGRVGLAKTVPEGFPPGSDVANMSILGYDPRK
YYTGRGPLEAASMGVELGPDDVAFRCNLVTLEDGKMKDYSAGHISSEEARELIEALNEELGSDRVKFYPG
VSYRHLLVIKGGFTADLKCTPPHDITGKPVADYLPRGEGSAELNELMLSSQEILEDHPVNLKRIEEGKLP
ANSIWLWGQGYAPKMPSFKEKYGLKGAVISAVDLLKGIGIYAGLDVIEVPGATGYLDTNYEGKAEAALEA
LKTHDFVFVHVEAPDEAGHEGDLEAKIKAIEDIDERVVGPILEALKKYEDYRILVLPDHPTPIELKTHTA
DPVPFLIYGEGIEPDGVQTFDEKSARKGGLGLVEGCELMELLLKK
>gnl|CDD|235253 PRK04201, PRK04201, zinc transporter ZupT; Provisional
MSNVSVALLLTLLAGLATGIGSLIAFFGKKPNNRFLSFSLGFAAGVMLYVSFMEILPKALAALTEAYGEG
MGPWLGYGAFFGGILGIFLIDRLVPHENPHELMQKEEMEFQQPLPKSLKRTGILTALAISIHNFPEGIAT
FVAALSNPELGFPIALAIAIHNIPEGIAVAVPVYYATGSKKKAFLYSFLSGLAEPLGAVLGYLLLGPFIS
PVVMGAIFAAVAGIMVFISLDELLPAAKEYGPHHLPSYGLIAGMAVMALSLVLLQ
>gnl|CDD|235254 PRK04203, rpl1P, 50S ribosomal protein L1P; Reviewed
LMDREKIEEAVKEALEEAPKRNFTQSVDLIVNLKDIDLKKPENRIDEEVVLPHGRGKEVKIAVIAKGELA
LQAKEAGADYVITREELEELGGDKRAAKKLANEYDFFIAEADLMPLIGRYLGPVLGPRGKMPTPLPPNAD
IKPLVERLKNTVRIRTKDQPTFHVRVGTEDMSPEELAENIDAVLNRIESKLEKGRQNIKSVYVKTTMGPA
VKVEL
>gnl|CDD|235255 PRK04204, PRK04204, RNA 3'-terminal phosphate cyclase
RMIEIDGSYGEGGGQILRTALALSAITGKPFRITNIRANRPNPGLLRQHLTAVKAAAEICNAEVEGAELG
SQELVFIPGPIRGGDYRFDIGTAGSITLVLQTVLPALLFADGPSRVTITGGTDVPWAPPIDYIRRVTLPL
LRRMGIEAEIELLRRGFYPAGGGEVALEVEPSKLRPLELLERGELLRIRGISHVANLPEHVAERQAKAAA
ELLALSLGLIEIEINVEELSRGLGPGSGIVLWAESEHITEGFDALGERGKPAEVVGEEAAEELLRYLASG
AAVDEHLADQLILPMALAGGEGSFTVAELTSHLLTNIWVVEKFLPVKFEVEEYDGVVIKVEGE
>gnl|CDD|179786 PRK04207, PRK04207, type II glyceraldehyde-3-phosphate dehydrogenase
MIKVGVNGYGTIGKRVADAVAAQPDMELVGVAKTKPDYEARVAVEKGYPLYVADPEREKAFEEAGIPVAG
TIEDLLEKADIVVDATPGGVGAKNKELYEKAGVKAIFQGGEKAEVAGVSFNALANYEEALGKDYVRVVSC
NTTGLCRTLCALDRAFGVKKVRATLVRRAADPKEVKRGPINAIVPDPVTVPSHHGPDVKTVLPDLDITTM
AVKVPTTLMHMHSVNVELKKPVTKEEVLEALENTPRILLVRASDGIDSTAELIEYARDLGRPRGDLYENA
VWEDSITVDGNELYLMQAVHQESIVVPENIDAIRAMLGLEDDEEKSIEKTNKALGIGKGKL
>gnl|CDD|179787 PRK04208, rbcL, ribulose bisophosphate carboxylase; Reviewed
MAKERYDAGVKEYRQMYWDPDYTPKDTDLLACFRITPQEGVDPEEAAAAVAAESSTGTWTTVWTDLLTDL
DKYKAKAYRIEDVPGDDGSYYAFIAYPLDLFEEGSIPNLLASIAGNVFGFKAVKALRLEDIRFPVAYVKT
FKGPPFGIQVERERLDKYGRPLLGTTPKPKLGLSAKNYGRVVYEALRGGLDFTKDDENLNSQPFNRWRDR
FLFVMEAIDKAEAETGERKGHYLNVTAPTMEEMYKRAEFAKELGSPIVMIDVVTAGWTALQSLREWCRDN
GLALHAHRAMHAAFTRNPNHGISFRVLAKLLRLIGVDHLHTGTVVGKLEGDRAEVLGYYDILREDFVPED
RSRGIFFDQDWGSIKPVFPVASGGIHPGHMPALLDIFGDDVVLQFGGGTHGHPDGTAAGATANRVALEAC
VEARNEGRDIEKEGPDILEEAAKWSPELAAALEKWGEIKFEFDTVDTL
>gnl|CDD|235256 PRK04210, PRK04210, phosphoenolpyruvate carboxykinase (GTP)
SLLKPAPTKNPKLLEWVAEVAELTQPDRVVWCDGSEEEYDRLRDQAVEAGTEIKLNPEKRPNSFLARSDP
SDVARVEDRTFICSEKEEDAGPTNNWMDPAEMRETLKGLFKGCMRGRTMYVVPFSMGPLGSPFAKIGVEI
TDSPYVVHSMRIMTRMGKAVLDVLGEDGEFVPCVHSVGAPLEPGQKDVPWPCNDTKYIVHFPETREIWSY
GSGYGGNALLGKKCFALRIASVMARDEGWLAEHMLILGVTSPEGRKTYFAAAFPSACGKTNLAMLIPPIP
GWKVETVGDDIAWIRPGEDGRLYAINPEAGFFGVAPGTNEKTNPNAMATLKPGNVIFTNVALTDDGDVWW
EGMTEEPPAHLIDWQGNDWTPGSGEPAAHPNARFTVPASQCPNLDPEWEDPAGVPISAIIFGGRRSDTVP
LVTEAFDWQHGVYMGATMGSETTAAAEGKVGVVRRDPMAMLPFCGYNMGDYFQHWLDFGKKLGSKLPKIF
GVNWFRKDEDGKFLWPGFGENMRVLKWIVDRVEGEADAVETPIGYLPKYEDLDLLGLDYSEEDYEKLFSV
DVDEWLAELELIEELFEKFGDRLPKELFEELEALKKRLLAA
>gnl|CDD|235257 PRK04211, rps12P, 30S ribosomal protein S12P; Reviewed
GKKSPNGLFAARKLKLKRKKFRWSDRRYKRRMLGLKEKADPLEGAPMARGIVLEKVGVEAKQPNSAIRKC
VRVQLIKNGKQVTAFCPGDGAINFIDEHDEVVIEGIGGPKGRSMGDIPGVRYKVIKVNGVSLKELVKGKK
EKPVR
>gnl|CDD|179790 PRK04213, PRK04213, GTP-binding protein EngB
MFETRPDRKPEIVFVGRSNVGKSTLVRELTGKKVRVGKRPGVTRKPNHYDWGDFILTDLPGFGFMSGVPK
EVQEKIKDEIVRYIEDNADRILAAVLVVDGKSFIEIIERWEGRGEIPIDVEMFDFLRELGIPPIVAVNKM
DKIKNRDEVLDEIAERLGLYPPWRQWQDIIAPISAKKGGIEELKEAIRKRLHEAKRDDLFK
>gnl|CDD|179791 PRK04214, rbn, ribonuclease BN/unknown domain fusion protein; Reviewed
MTRLQRLHLWKERARTCSFARFLWRRFLDDRLFQAAASLTFTTLLALVPLATVVFGVLSAFPVFDEWSDQ
FVDFVFSNFVPQAARSVFDYLNQFREQAGRLTAAGSVALVVTLLILLHTIEQTFNRIWRVNSARPWLTRF
LVYWTVLTLGPLLLGASIAFSAGVFALPLLATTAPQWLAELARLAPLAFETVCLTLLYRVVPNHFVPLRH
ALPGALLTAVLLELVKWGFGFYLGNFQTYQRIYGAFAAVPILLLWIYLLWVLVLLGASLTSSLSYWRGQP
FRRRLPSGGRFYDLLRLLGRLDQARKHGKALDVDEIRRLEPMGYDELGELLCELARIGLLRRGERGQWVL
ARDLDSVPLAELYELFVLRPLPCRDDHVGQAADAALTQLRQPLRETLAEFVADLYTRQPGDP
>gnl|CDD|235258 PRK04217, PRK04217, hypothetical protein; Provisional
MPFGWGRGRGRRRKMRMIGFIPQVRHFYPAIPPVGPPKPPIFMTYEEFEALRLVDYEGLTQEEAGKRMGV
SRGTVWRALTSARKKVAQMLVEGRELIILPQGNEVPRDEE
>gnl|CDD|235259 PRK04219, rpl5p, 50S ribosomal protein L5P; Reviewed
MSILEDWEMNPMRKPRIEKVVVNIGVGESGERLTKAEKLLEELTGQKPVRTRAKKTIPDFGIRKGEPIGV
KVTLRGEKAEEFLKTALEAVGNRLKASSFDETGNVSFGIEEHIDFPGVKYDPEIGIFGMDVCVTLERPGY
RVARRRRKRRKIPSRHRVTKEEAIEFLEENFGVEVVE
>gnl|CDD|179793 PRK04220, PRK04220, 2-phosphoglycerate kinase; Provisional
MIMIRIIVKGKKYEMPFSKGILARSLTAAGMKPSIAYEIASEIEEELKKEGIKEITKEELRRRVYYKLIE
KDYEEVAEKYLLWRRIRKSKEPIIILIGGASGVGTSTIAFELASRLGIRSVIGTDSIREVMRKIISKELL
PTLHESSYTAWKSLRRPPPPEPPVIYGFERHVEPVSVGVEAVIERALKEGISVIIEGVHIVPGFIKEKYL
ENPNVFMFVLTLSDEEAHKARFYARARVSRRPAERYLKNFEIIREINDYIVEKAKKHGVPVIENISIEET
VDKILEIITERLSKIIEEEGL
>gnl|CDD|179794 PRK04223, rpl22p, 50S ribosomal protein L22P; Reviewed
MARINYSVKADPEKTAKAMGRELPISPKHSVEIAREIRGMKLDEAKAYLEDVIALKRAVPFKRHNKKVGH
RKGIDGWPAGRYPVKAAKAFLKLLENAEANAEYKGLDTEKLVIVHIAAHKGRVIKGYMPRAFGRATPKNT
ETVNIEVILEEVE
>gnl|CDD|235260 PRK04231, rpl3p, 50S ribosomal protein L3P; Reviewed
MRKIHRPRRGSLAFSPRKRAKSIVPRIRSWPEIDGEPKLLGFAGYKAGMTHVIMIDDRPNSPTEGKEIFV
PVTVLETPPMRVAAIRAYEKDPYGLKVLTEVWAEDLDKELERRITLPKKDEKKKAFEKLLKLLEEGKIVD
VRVIVHTQPKLVTGVPKKKPEIMEIRIGGGSVEERLEYAKELLGKEISISDVFKEGQLVDVIAVTKGKGF
QGVVKRWGVKLLPRKHKRRGGSRHIGTLGPWNPSRVMWTVPQAGQMGFHQRTEYNKRILKIGDDGDEITP
KGGFLHYGLVRNDYVLIKGSVPGPAKRLIRLRPAIRPPEPPVEAPEITYVSTESKQG
>gnl|CDD|235261 PRK04233, PRK04233, hypothetical protein; Provisional
MMPSTPTDPCPCGRPADYARCCGPYHAGAAAPDAETLMRARYSAYVRRDADYLLASWHPSTRPAELSLDE
GGRTTWLGLTVQRTLETGADTAEVVFLARYRIGGGSAVRMTEHSRFVREDGRWYYLDAR
>gnl|CDD|235262 PRK04235, PRK04235, hypothetical protein; Provisional
MMMWEERKREALERLERALEIGYVDEDIIPLLDLINSLKNYYTTSSCSGRIGIIEAEMPSKGDKKNSRWL
GKWHHPVTPEEVLEALKKKQVGRLWLIVQGPILHVAARDLETAKKLLELAREAGFKHSGIKSISDKRVLV
EIRTTERMDAPLGEDGKLVVDEEYLKFLVEVANEKLLRGKERLNRLEEELEELKEN
>gnl|CDD|179798 PRK04239, PRK04239, DNA-binding protein
EELEEIRRRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAILRQILTPEARERLNRIKLVKPEFAEQVE
QQLIQLAQSGRIQGPIDDEQLKEILEQLTPQKREFKITRR
>gnl|CDD|235263 PRK04243, PRK04243, 50S ribosomal protein L15e; Validated
MAMSMYSYIREAWKRPKESYVGELMWQRLQEWRREPAVVRIERPTRLDRARALGYKAKQGIVVVRVRVRR
GGLRKPRPKGGRRPKRMGVNKITPAKSIQRIAEERAARKYPNLEVLNSYWVGEDGKYKWYEVILVDPHHP
AIKNDPDLNWICDKSHRGRVFRGLTSAGKKGRGLRKKGKGTEKVRPSIRANERRGK
>gnl|CDD|235264 PRK04247, PRK04247, endonuclease NucS
MMVEVLENPSIEEAADLLEEAIEKRALVTIFGRCEVEYEGRAASELGPGDRLIIIKPDGTFLVHEDEKRE
PVNWQPPGSKTEAYVDDGRLVLESIRRRPKERLEVRFHEVYYVTAFDVEDYEELELTGSEADMVDRILEN
PDLIEEGFRPLAREYPTPAGIIDILGRDKDGNLVVLELKRRRAGLSAVSQLKRYVEALRELHGDKVRGIL
VAPSITDRARRLLEKEGLEFVKLEPPKL
>gnl|CDD|235265 PRK04250, PRK04250, dihydroorotase; Provisional
VLEGKFLLKGRIVEGGIGIENGRISKISLRDLKGKEVIKVKGGIILPGLIDVHVHLRDFEESYKETIESG
TKAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKIFMGA
STGGIFSENFEVDYACAPGIVSVHAEDPELIREFPERPPEAEVVAIERALEAGKKLKKPLHICHISTKDG
LKLILKSNLPWVSFEVTPHHLFLTRKDYERNPLLKVYPPLRSEEDRKALWENFSKIPIIASDHAPHTLED
KEAGAAGIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIKNYGIEEGNYANFAVFDMKKEWTI
KAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKPRGVRI
>gnl|CDD|179802 PRK04257, PRK04257, hypothetical protein; Provisional
MLKEVLNKILWHPDYNEEDYYIVILHRGAYGNKKKIPLENIELGHSYLVYGETHIPYHRILEIVNKKTGE
ILYKKRKL
>gnl|CDD|179803 PRK04260, PRK04260, acetylornithine transaminase
MTYLFQNYKRAAIEFVKAEGNYLIDTDGKKYLDFSSGIGVTNLGFHPQVQQALQKQAGLIWHSPNLYLNS
LQEEVAQKLIGDKDYLAFFCNSGAEANEAAIKIARKATGKQEIITFQNSFHGRTFGSMSATGQDKIKDGF
GDGVPHFSYAIFNDLNSVKALVNKNTAAVMLELVQGESGVLPADKDFVKALADYCQETGILLIVDEVQTG
MGRTGKLYAFEHYGIEPDIFTLAKGLANGVPVGAMLAKSSLGGAFGYGSHGSTFGGNKLSMAAASATLDI
MLTAGFLEQALENGNYLQEQLQKALQDKETVTTVRGLGYMIGIETTADLSQLVEAARDKGLIVLTAGTNV
IRLLPPLTLTKEEIEQGIAILSEVF
>gnl|CDD|235266 PRK04262, PRK04262, hypothetical protein; Provisional
MMVGIVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAGIDP
KEIGAVYVGSESHPYAVKPTATIVAEALGATPDLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGA
DTAQGAPGDALEYTAAAGGAAFIIGKEEVIAEIEATYSYTTDTPDFWRREGEPYPRHGGRFTGEPAYFKH
IISAAKGLMEKLGLKPSDYDYAVFHQPNGKFPLRVAKMLGFTKEQVKPGLLTPYIGNTYSGSALLGLAAV
LDVAKPGDRILVVSFGSGAGSDAFSITVTDAIEEKRDLAPTVEDYLERKKYIDYAVYAKYRGKIKMY
>gnl|CDD|235267 PRK04266, PRK04266, fibrillarin-like rRNA/tRNA 2'-O-methyltransferase
MVKKKEIFEGVYEVEFEDGSKRLATKNLVPGKRVYGERLIKWEGVEYREWNPRRSKLAAAILKGLKNFPI
KKGSKVLYLGAASGTTVSHVSDIVEEGVVYAVEFAPRPMRELLEVAEERKNIIPILADARKPERYAHVVE
KVDVIYQDVAQPNQAEIAIDNAEFFLKDGGYLLLAIKARSIDVTKDPKEIFKEEIRKLEEGGFEILEVVD
LEPYHKDHAAVVARKK
>gnl|CDD|179806 PRK04270, PRK04270, RNA-guided pseudouridylation complex pseudouridine synthase subunit Cbf5
AETNPEYGCPPEKRPIEELIKFGVVNLDKPPGPTSHEVAAWVRDILGVEKAGHGGTLDPKVTGVLPVALG
KATKVVQALLESGKEYVCVMHLHGDVPEEDIRKVFKEFTGEIYQKPPLKSAVKRRLRVRTIYELEILEID
GRDVLFRVRCESGTYIRKLCHDIGLALGTGAHMQELRRTRTGPFTEEDLVTLQDLADAYYFWKEDGDEEE
LRRVILPMEYALSHLPKIIIKDSAVDAIAHGAPLYAPGIAKLEKGIKKGDLVAVFTLKGELVALGKALMD
SDEILKAEKGIVVDLERVFM
>gnl|CDD|179807 PRK04280, PRK04280, transcriptional regulator ArgR
NKGQRHIKIREIITNNEIETQDELVDRLREEGFNVTQATVSRDIKELHLVKVPLPDGRYKYSLPADQRFN
PLQKLKRALMDSFVKIDGAGNLLVLKTLPGNANSIGALIDNLDWDEILGTICGDDTCLIICRTEEDAEEV
KDRFLNML
>gnl|CDD|235268 PRK04282, PRK04282, exosome complex protein Rrp42
TPSNQEIIPEIKKDYILSLLKKGKRIDGRKLDEYRPIEIETGVIKKAEGSALVKLGNTQVLAGVKLEIGE
PFPDTPNEGVLIVNAELLPLASPTFEPGPPDENAIELARVVDRGIRESKAIDLEKLVIEPGKKVWVVFID
VYVLDHDGNLLDASMLAAVAALLNTKVPAVEEGEDGVVDKLGEDFPLPVNDKPVTVTFAKIGNYLIVDPT
LEEESVMDARITITTDEDGNIVAIQKSGIGSFTEEEVDKAIDIALEKAKELREKLKEALGI
>gnl|CDD|235269 PRK04284, PRK04284, ornithine carbamoyltransferase; Provisional
MKNLRNRSFLTLLDFTPKEIEYLLDLSEDLKRAKYAGIEVQKLKGKNIALIFEKDSTRTRCAFEVAAYDQ
GAHVTYLGPTGSQMGKKESTKDTARVLGGMYDGIEYRGFSQRTVETLAEYSGVPVWNGLTDEDHPTQVLA
DFLTAKEHLKKPYKDIKFTYVGDGRNNVANALMQGAAIMGMDFHLVCPKELNPDDELLNKCKEIAAETGG
KITITDDIDEGVKGSDVIYTDVWVSMGEPDEVWEERIKLLKPYQVNKEMMKKTGNPNAIFEHCLPSFHDL
DTKVGKEIFEKYGLKEMEVTDEVFESKASVVFDEAENRMHTIKAVMVATLGE
>gnl|CDD|235270 PRK04286, PRK04286, hypothetical protein; Provisional
MKIIPLASESLGVRSMATFVETKDVRILIDPGVSLAPRRYGLPPHPIELERLEEVREKILEYAKKADVIT
ISHYHYDHHTPFYEDPYELSDEEIPKEIYKGKIVLIKDPTENINWSQRRRAPRFLKAVKDIAKKIEYADG
KTFRFGGTTIEFSPPVPHGADGSKLGYVIMVRISDGDESFVFASDVQGPLNDEAVEFILEKKPDVVIIGG
PPTYLLGRRLSEEDLEKGIENLEEIVKNTPETLILDHHLLRDKNYREKLKELYERAEDRGVRVLTAAEFL
GLEPELLEAYRKELYKEE
>gnl|CDD|179810 PRK04288, PRK04288, antiholin-like protein LrgB; Provisional
INHLSTMTPYFGILVSLIAFGIGTILFKKSKGFFLFTPLFVAMVLGIAFLKLTGISYEEYNIGGDIISFF
LEPATIAFAIPLYKKRDVLKKYWWQILGGIVVGSVCSVLIIYLVAKLIQLDNAVMASMLPQAATTAIALP
VSAGIGGIKEITSFAVIFNAVIIYALGAKFLKLFRIKNPIAKGLALGTSGHALGVAVGIEMGEVEAAMAS
IAVVVVGVVTVAVVPVFVPIIG
>gnl|CDD|235271 PRK04290, PRK04290, 30S ribosomal protein S6e; Validated
MADFKVVVSDPKTGKAYQIEIDGAEANRLIGKKIGDEIDGSIVGLDGYKLKITGGSDKSGFPMRPDVPGP
VRRRILLSGGPGFRPKEKGERRRKTVRGNTISDDIVQINAKVVEY
>gnl|CDD|179812 PRK04293, PRK04293, adenylosuccinate synthetase; Provisional
MTCTIVVGGFFGDEGKGKIIAYLALKDKPSIIARGGVGPNAGHTVEYNGKKYGLRMIPSGFVNKDAKLAI
GAGVLVDPEVLLKEVEELNVGGRVFVDYRCGIIEEKHVEEDRSDEHLSKKIGSTGTGCGPANADRVLRRL
KLAKDVEELEKYLTDVPEEVNEALDRGENVLIEGTQGFGLSLYYGTYPYVTSKDTTASGIASDVGVGPTK
VDEVIVVFKSYPTRVGEGPFPTELSLEEAEKLGLVEYGTVTGRRRRVGPFDFELARRAARINGATQIAIT
KLDKLDKEAYGVTEYDKLPPEAKKFIEEIEEELGVPVTLISTGPELEDTIDLR
>gnl|CDD|235272 PRK04296, PRK04296, thymidine kinase; Provisional
MAKLEFIYGAMNSGKSTELLQRAYNYEERGMKVLVFKPAIDDRYGEGKVVSRIGLSREAIPVSSDTDIFE
LIEEEGEKIDCVLIDEAQFLDKEQVVQLAEVLDDLGIPVICYGLDTDFRGEPFEGSPYLLALADKVTELK
AICVHCGRKATMNQRLIDGGPAVYEGPQVLVGGNESYEAVCRKHYKEALK
>gnl|CDD|235273 PRK04301, radA, DNA repair and recombination protein RadA; Validated
EKMKEKDLEDLPGVGPATAEKLREAGYDTVEAIAVASPKELSEAAGIGESTAAKIIEAAREAADIGGFET
ALEVLERRKNVGKITTGSKELDELLGGGIETQSITEFYGEFGSGKTQICHQLAVNVQLPEEKGGLEGKAV
YIDTEGTFRPERIEQMAEALGLDPDEVLDNIHVARAYNSDHQMLLAEKAEELIKEGENIKLVIVDSLTAH
FRAEYVGRGNLAERQQKLNKHLHDLLRLADLYNAAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRI
YLRKSKGNKRIARLVDSPHLPEGEAVFRITEEGIRDA
>gnl|CDD|235274 PRK04302, PRK04302, triosephosphate isomerase; Provisional
MKYPIILVNFKTYPEATGKDALEIAKAAEKVSKETGVRIAVAPQALDIRRVAEEVDIPVYAQHVDPVEPG
SHTGHILPEAVKDAGAVGTLINHSERRLTLADIEAVVERAKKLGLESVVCVNNPETSAAAAALGPDYVAV
EPPELIGTGIPVSKAKPEVVEDAVEAVKKVNPDVKVLCGAGISTGEDVKAALELGADGVLLASGVVKAKD
PEAALRDLVSPLA
>gnl|CDD|235275 PRK04306, PRK04306, 50S ribosomal protein L21e; Reviewed
MMKKSHGFRSKTRKKLSKSPRERGLSPLSRALQEFEEGDKVHIVIDPSVHKGMPHPRFHGKTGTVVGKRG
RAYIVEVKDGGKEKTLIVRPEHLRPQKG
>gnl|CDD|235276 PRK04307, PRK04307, protein-disulfide oxidoreductase DsbI
IKGMWRDLRARPVDTLVRWQDQRFLWLLMAIAMGGLIILAHSFFQIYLYMAPCEQCVYIRFAMFVMAIGG
VIAAINPKNIILKLIGYIAAFYGSILGIKFSIKLNGIHHAVHNDDPLFGVQGCSTDPTFPFNLPLAEWAP
EWFKPTGDCGYDAPIVPDGVTLSSVQQWFVDLYSEGWYLLPPWHFMNMAQACLLAFGLCLVLLVVMSGAW
ALKLARGK
>gnl|CDD|235277 PRK04309, PRK04309, DNA-directed RNA polymerase subunit A''; Validated
MMSEETLEEKLEDASLELPQKLKEELREKLEERKLTEEEVEEIIEEVVREYLRSLVEPGEAVGVVAAQSI
GEPGTQMTMRTFHYAGVAEINVTLGLPRLIEIVDARKEPSTPMMTIYLKDEYAYDREKAEEVARKIEATT
LENLAKDISVDLANMTIIIELDEEMLEDRGLTVDDVKEAIEKKKGGEVEIEGNTLIISPKEPSYRELRKL
AEKIRNIKIKGIKGIKRVIIRKEGDEYVIYTEGSNLKEVLKVEGVDATRTTTNNIHEIEEVLGIEAARNA
IIEEIKNTLEEQGLDVDIRHIMLVADMMTWDGEVRQIGRHGVSGEKASVLARAAFEVTVKHLLDAAVRGE
VDELKGVTENIIVGQPIPLGTGDVELTMDPPLR
>gnl|CDD|179820 PRK04313, PRK04313, 30S ribosomal protein S4e; Validated
MMRHLKRLAAPKSWPIPRKEYKWTVKPSPGPHSIEESIPLLVVLRDVLGYADTAREAKKIINEGKVLVDG
RVRKDYKFPVGLMDVISIPETGEYYRVLPDEKGRLVLIPISEEEAKLKLCKIENKTTVKGGKIQLNLHDG
RNILVDVEDDYKTGDSLLISLPEQEIVDHIPFEEGNLAIITGGKHVGEIGKIKEIEVTKSSKPNIVTLED
KDGEKFETILDYVFVIGKEKPVIKLPE
>gnl|CDD|235279 PRK04319, PRK04319, acetyl-CoA synthetase; Provisional
MKVETLPVIKGEPNLKDYEETYATFSWEEVEKEFSWLETGKVNIAYEAIDRHADGGRKDKVALRYLDASR
KEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDR
LEDSEAKVLITTPALLERKPADDLPSLKHVLLVGEDVEEGPGTLDFNALMEQASDEFDIEWTDREDGAIL
HYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGG
RFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGLP
IHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMRGIWN
NPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPD
PVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWELGL
PEGDLSTMED
>gnl|CDD|235280 PRK04322, PRK04322, peptidyl-tRNA hydrolase; Provisional
QVIVVRTDLKMGKGKLAAQVAHAAVSAYEKADKSNREWLEEWLNEGQKKVVLKVNSEEELLELKEKAERL
GLPTALIRDAGLTQLPPGTVTALGIGPAPEEKIDKITGDLKLL
>gnl|CDD|179823 PRK04323, PRK04323, hypothetical protein; Provisional
MAIKLINIGFGNIVSANRIIAIVSPESAPIKRIIQEARERGMLIDATYGRKTRAVIITDSGHVILSAIQP
ETIAHRLSSKEEDIEEGEEED
>gnl|CDD|179824 PRK04325, PRK04325, hypothetical protein; Provisional
MDAVQEMEDRITELEIQLAFQEDLIDGLNATVARQQQTLDLLQAQLRLLYQQMRDANPDAAEPYSLRDEI
PPHY
>gnl|CDD|179825 PRK04326, PRK04326, methionine synthase; Provisional
MDHDKLPFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRR
EEMVEYFAERIEGFKFYGPVRVWGNNYFRKPSVVGKIEYKEPMLVDEFEFAKSVTYTRPVKVPITGPYTI
AEWSFNEYYKDKEELVFDLAKVINEEIKNLVEAGAKYIQIDEPALATHPEDVEIAVEALNRIVKGINAKL
GLHVCYGDYSRIAPYILEFPVDQFDLEFANGNYKLLDLLKEYGFDKELGLGVIDVHSARVESVEEIKEAI
KKGLEYVPPEKLYINPDCGLKLLPREIAYQKLVNMVKATREVREELDKGG
>gnl|CDD|235281 PRK04328, PRK04328, hypothetical protein; Provisional
MVKRVKTGIPGMDEILYGGIPERNVVLLSGGPGTGKSIFSQQFLWNGLQMGEPGVYVALEEHPVQVRRNM
RQFGWDVRKYEEEGKFAIVDAFTGGIGSAAKREKYVVKDPDDVRELIDVLRQAIKDIGAKRVVIDSVSTL
YLTKPAMARSIVMQLKRVLSGLGCTAIFVSQVSVGERGFGGPGVEHAVDGIIRLDLDEIDGELKRSLIVW
KMRGTKHSMRRHPFEITDKGIVVYPDKVLKITRWSVSIE
>gnl|CDD|235282 PRK04330, PRK04330, hypothetical protein; Provisional
MAKMYDNEEKIKQAIQMLEEIINDTSVPRNIRRAATEAKEILLNEEESPGVRAATAISILDEISNDPNMP
LHTRTLIWNIVSQLETIK
>gnl|CDD|235283 PRK04333, PRK04333, 50S ribosomal protein L14e; Validated
MPAIEVGRVCVKTAGREAGRKCVIVDIIDKNFVLVTGPSLTGVKRRRCNIKHLEPTDKKVDIEKGASDEE
VKKALEAAGLTEYM
>gnl|CDD|235284 PRK04334, PRK04334, hypothetical protein; Provisional
NPAAAGLLIGFRVHLKETPIDIIAEADDPELAEAAKAAILRFRGELEEYIAEDPEFRTSLEPVECPPDAP
EVARRMAAAARPAGVGPMAAVAGAIAQEVVEALVEAGSKRAIVENGGDIALHSDRDRRVGLYAGDSPLSG
RLGFRIKPGASPLGICTSSGTVGHSLSFGIADAVTVFARDAALADAAATAIANAVDPLGPEDVERALERA
DAIAEGVDGVGVIKGDKLGLWGKIPLLVRADVKEDLITKGE
>gnl|CDD|179831 PRK04337, PRK04337, 50S ribosomal protein L35Ae; Validated
MRMKGVILSYRRGKNTQYNRQVIIKPLGVDDREEAAKLIGRKVIWKDPTGNKYVGKIVRVHGNRGEVRAR
FKPGLPGQALGDYVEII
>gnl|CDD|235286 PRK04338, PRK04338, N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
LMIITEGKVKIEVPDPSTYSKDGKFPPSWAPVFYNPRMELNRDISVLVLRAFGPKLPRESVLDALSASGI
RGIRYALETGVEKVTLNDINPDAVELIKKNLELNGLENEKVFNKDANALLHEERKFDVVDIDPFGSPAPF
LDSAIRSVKRGGLLCVTATDTAPLCGAYPKSCLRKYGAVPLKTEFYHEMGLRILIGYIAREAAKYDKGLE
PLFSHSTDHYYRVFLKVERGAKKADKALENLGYVYYCPKCLYREEVEGLPPEECPVCGGKFGTAGPLWLG
PLHDKEFVEEMLEEAAKELGTSKKALKLLKTIEEESKLDTPTFYDLHELAKKLKVSAPPMDEILEALREA
GFEASRTHFSPTGFKTDAPYDEIKEAIKSLSS
>gnl|CDD|235287 PRK04342, PRK04342, DNA topoisomerase IV subunit A
MAKSKRDKEDREKALKKLRELAEKIYEDIEKGKRPVLEIPKRTLSNIEYDEKKGLLVLGDKKSKRSFLNV
KQAKKFMQTVLMAEFIKELLEENKSSTLRELYYMSKHWIPGLKENTFDDQDESDAVIEDLEVALGVLREE
LHIRPEEDGSVVGPLRIRDGTDEIDCSKLGEGGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEGF
WKKYNAILVHLKGQPARATRRFIKRLNEELGLPVYVFTDGDPWGYYIYSVVKYGSIKLAHLSERLATPDA
KFIGVTPSDIVEYERDLPTIKLKDSDIKRAKELLNYPWFQTDFWQKEINLFLKIGKKAEQQALASKGLKF
VTDEYLPEKLEEKDWLD
>gnl|CDD|235288 PRK04346, PRK04346, tryptophan synthase subunit beta; Validated
TYTLPDENGYFGEFGGRFVPETLMPALEELEEAYEKAKNDPEFQAELDYLLKNYVGRPTPLYFAERLSEH
LGGAKIYLKREDLNHTGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAE
DVERQALNVFRMKLLGAEVVPVTSGSRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSV
IGEEAKAQILEKEGRLPDAVVACVGGGSNAIGIFHPFIDDESVRLIGVEAAGKGLETGKHAATLTKGRPG
VLHGAKTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLKDIGRAEYVSITDDEALEAFQLLSRLEGIIP
ALESSHALAYALKLAPTLGKDQIIVVNLSGRGDKDVFTVAKLLGVIL
>gnl|CDD|235289 PRK04350, PRK04350, thymidine phosphorylase; Provisional
TGRENVIYNRRDAHVCRSEGFHAGDRVEVRAGGRSIIATLNITDDDLVGPGEIGLSESAFRRLGVSEGDE
VEVSHAPPPESLSAIRKKIDGEKLDKEEIEAIIRDIVAGRYSDIELSAFLTASAINGLDMDEIEALTRAM
VETGERLDWDRPPVVDKHSIGGVPGNRTTLIVVPIVAAAGLTIPKTSSRAITSPAGTADTMEVLAPVDLS
VEEIKRVVEKVGGCLVWGGAVNLSPADDILIRVERPLSIDPRGQLVASILSKKIAAGSTHVVIDIPVGPT
AKVRSVEEARRLARLFEEVGDRLGLRVECAITDGSQPIGRGIGPALEARDVLAVLENDPDAPNDLREKSL
RLAGILLEMGGVAPGGEGYALAREILESGKALEKFQEIIEAQGGDSEDIPLGDHTHDVTAPRDGYVTAID
NRRLARIARLAGAPKDKGAGIDLHVKVGDKVKKGDPLYTIHAESEGELDYAIELARRHPPIIVEGMLLER
>gnl|CDD|235290 PRK04351, PRK04351, SprT family protein
MTNQELQRLVEEISLEYFGKPFRHQAYFNKRLRTTGGRYLLKDHHIEFNPKMLEEYGLEELIGIIKHELC
HYHLHLEGKGYQHRDRDFKELLKQVGGPRYCPPLPSQKKNYLYECQSCGQQYLRKRRINTKRYRCGKCRG
KLKLINQLK
>gnl|CDD|235291 PRK04358, PRK04358, hypothetical protein; Provisional
MLKQRFVLDTSAFTDPDVREQFGVEDLEEAVEKFLDLIARARLKLGISCYMPPSVYKELRGFLERNGCSP
EVIAKLDTWIVKKSPNRYEIKIPAEIFYEYIEDMRERINKGLRVAEEAVREAALECYDLSKEEIEREVVG
KIISKLREKYREALRKGILDSAEDLDVLLLAKELDAAVVSADEGIRKWAERLGLRFVDARKFPRMLEEYL
RHVGRHE
>gnl|CDD|235292 PRK04366, PRK04366, aminomethyl-transferring glycine dehydrogenase subunit GcvPB
ARWDEPLIFELSRPGRRGYSLPELDVPEVLESLLPEELLRKEPPELPEVSELEVVRHYTRLSQKNYGVDT
GFYPLGSCTMKYNPKINEKVARLPGFAELHPLQPEETVQGALELMYELQEWLKEITGMDAVTLQPAAGAH
GELTGLLMIRAYHEARGDTKRTEVIVPDSAHGTNPASAAMAGFKVVEIPSNEDGLVDLEALKAAVGEDTA
ALMLTNPNTLGLFERNILEIAEIVHEAGGLLYYDGANLNAILGKARPGDMGFDVVHLNLHKTFSTPHGGG
GPGSGPVGVKEELAPFLPVPVVEKDGDRYRLDYDRPKSIGRVRAFYGNFGVLVRAYAYIRSLGAEGLREV
SEDAVLNANYLKARLKDIYDLPYDRPCMHEFVLSGKKLKETGVRTLDIAKRLLDYGFHPPTIYFPLIVPE
ALMIEPTETESKETLDAFIAAMKQIAEEAKENPELVKEAPHNTPVRRLDEVKAARKPVLRW
>gnl|CDD|179839 PRK04374, PRK04374 [protein-PII] uridylyltransferase
MTDTPADRPDPGVAGDADWAAAARPLLVHADMRLCKRFDQGEPIERLLALRARAVDQLMRNAWTRCIPAD
SGLSLHAVGGYGRGELFPRSDVDLLVLGETAAQQRHEQALARLFALLWDVGLPISHAVRSPAQCTAAAAD
QTVLTALIESRPLVADAAARAALAAAIAPQQVWPPRAFFQAKREELLARHQRFGDTADNLEPDIKDGPGG
LRDLQTLGWMALRAFGVKDLEALVGLGHVGCDEAAALRREREELARLRFGLHLVANRPEERLRFDYQKTL
AERLGFADDPESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEATPEPLGGGFSLRRGYLAADADS
WPDGDVLQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDVADATARERFMALLRGPRAVETLNRM
ARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSIAHEVWPRLRKPELLL
LAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFA
TLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARA
LMQAQGHDDATIDRQFAGMPDENFLRFRPEQLAWQAASLIEVEIGQTLVKARRAVPDNDALEVFVYSPDR
DGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQDTYADGDPQRLAAALRQVLAGDLQKVRPAR
RAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQF
QITDEHDRPLSESARQALRDALCACLDPV
>gnl|CDD|235293 PRK04375, PRK04375, protoheme IX farnesyltransferase; Provisional
VSSSSSRATLKDYLALTKPRVISLNLFTALGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRD
IDAKMERTKNRPLVTGRISPREALIFGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLWLKRRTP
QNIVIGGAAGAMPPLIGWAAVTGSLSWEALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIR
VTKRQILLYTVLLVAVSLLPVLLGMAGLLYLVVALLLGAWFLYYAWRLYRKDDRKWARKLFRYSINYLTL
LFVALLVDHLLLLSLL
>gnl|CDD|179841 PRK04387, PRK04387, hypothetical protein; Provisional
MEYQYPLDLDWSTEEMISVLHFFNAVEKAYEKGVDAEELLDAYRRFKEIVPSKAEEKQIDREFEKVSGYS
IYRAVQKAKEIEEGKISLGK
>gnl|CDD|235294 PRK04388, PRK04388, disulfide bond formation protein B; Provisional
MNPFRWSFRAQFLLGFLACAGLLAYAIFVQLHLGLEPCPLCIFQRIAFAALALLFLIGALHGPRNAGGRK
AYGVLAFIAAGVGMGIAARHVWVQIRPKDMMSSCGPPLSFLSETMGPFEVFRTVLTGTGDCGNIDWRFLG
LSMPMWSMVWFVGLALWALYAGFKARRRSLLF
>gnl|CDD|235295 PRK04405, prsA, peptidylprolyl isomerase; Provisional
MKKKMKKWALAAASAGLALSLAGCSSNQATVATYSGGKITQSQYYKEMKQSSAGKTVLANMIIYRALEKQ
YGKKVSTKKVDKQYNSYKKQYGSSFDSVLSQNGMTTSSFKQNLRTNLLSEAALKKLKKVTNSQLKKAWKS
YQPKVTVQHILVSKKSTAETVIKKLKDGKDFAKLAKKYSTDTATKNKGGKLSAFDSTDTTLDSTFKTAAF
KLKNGEYTTTPVKTTYGYEVIKMIKHPAKGTFSDHKKALTKQIYAKWASDSSVMQRVISKVLKKANVSIK
DKDLKDALSSYLSSSSSS
>gnl|CDD|235296 PRK04406, PRK04406, hypothetical protein; Provisional
MTEKTIEQLEERINDLECQLAFQEQTIEELNDALSQQQLLITKMQDQMKYVVGKVKNMDSSNLADPAEET
PPPHY
>gnl|CDD|235297 PRK04423, PRK04423, LPS-assembly protein LptD
MRRALRLLPLPLSIAICLPAMAAEKPLNWGLCPAVDPLPGFDGAPAADPKAAEMRQQLPTDIEGDQLSGT
STTPQYQGNVALKRGDQFLGADNLRMDTETGNYIAEGNVRYQDTSIRMVADRAEGNQDTDTHKITNIQYQ
LVSRRGNGDAESVDLQGQVGQMHRSTYTTCDPSQPIWRLRAPEIDVDNDEGFGTARNAVLQIGKVPVLYF
PWFKFPIDDRRQTGLLFPQFGLSGRNGFDYLQPIYLNLAPNYDATLLPRYMSKRGFMFGTEFRYLYDGGR
GEVTGNYLPNDKLRDKDRGRVFYSGYHNVNSHWQARASLSWVSDTRYVEDFTSRLNGMGSASSLQSTVGI
YGTGETWTAGLMADRWQLTDYTLDERALPYNRQPRAYFNWEKPVFGIFEAGVYAEAVRFTHDDSYLVQPP
NDGDDDNYVRTGIVNREYGSGSRLDVKPYVSMPLSGAAWFVTPTLAWRYTAYQLDSTLAETAPLTGDRSP
SRSLPIASLDAGLYFDRETSLFGTNYLNTLEPRLYYLYVPYRNQDDLPVFDTRPFTFSWGQLFRDSRYTG
ADRQNDANQLTLAVTSRWLRQDDGKEKLSLSAGQILYFDDSLVTINNSEQTIEQGKSAWVADANYMINDR
WTLGATYQWNPNSRREDLASLRTRYLLPNDGIINLAYRYRRNLIDNSDQLKQADFSFLYPINPRWSAVGR
YYYSLLDKKPLEIIGGVQWDSCCLAVRALVRRFVRNRDGEMDNSIQIEFVLKGLSSFGQDTDRTLRRAIL
GYYRDDLYLVPPSNTTTNPDDYDPNLIP
>gnl|CDD|179847 PRK04424, PRK04424, transcription factor FapR
MKLSKKERQKALQELIEENPFITDEELAEKFGVSIQTIRLDRMELGIPELRERIKHVAEKNYDKVKSLPE
EEVVGELIDLELGRSAISILEITEEMVFSKTGIARGHHLFAQANSLAVAVIDAELALTGVANIRFKRPVK
LGERVVAKAEVVRKKGNKYIVEVKSYVGDELVFRGKFIMYRSSEE
>gnl|CDD|179848 PRK04435, PRK04435, ACT domain-containing protein
NKMKKKFYLVREDVLPEAVEKTLKAKELLKSGKVKSINEAVKQVGISRSAFYKYKDYVFPFDEMVKGKII
TLSLLLEDRSGTLSKVLNVIAEAGGNILTINQSIPLQGRANVTISIDTSSMEGDIDELLEKLRNLDGVEK
VELIGME
>gnl|CDD|235298 PRK04439, PRK04439, methionine adenosyltransferase
MRNIVVEELNRTPVEEQPVEIVERKGIGHPDTICDGIAEAVSRALSRYYLEKFGAILHHNTDKVLLVGGR
SAPKFGGGEVIEPIYIILGGRATKEVGGEEIPVGEIAIEAAKEYLRENLRNLDPERHVIIDVRLGPGSTD
LVDVFERESIVPLANDTSFGVGYAPLSETERLVLETERYLNSEEFKKRFPEVGEDIKVMGLRNGDEITLT
IAMALVDRYVNDVDEYFEVKEEVKEKVEDLAQKYTDRDVEVHINTADDPDEGGVYLTVTGTSAEMGDDGS
VGRGNRVNGLITPNRPMSMEAAAGKNPVNHVGKIYNVLANRIAREIYEEVEGVKEVYVRLLSQIGKPIDE
PLVASIQVIPEDGVLISDVEKEVEEIVDEELANITKITELLLEGKVPVF
>gnl|CDD|235299 PRK04443, PRK04443 [LysW]-lysine hydrolase
MTISALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREAWVDEAGNARGPAGDGPPLVLLLGHIDT
VPGDIPVRVEDGVLWGRGSVDAKGPLAAFAAAAARLEALVRARVSFVGAVEEEAPSSGGARLVADRERPD
AVIIGEPSGWDGITLGYKGRLLVTYVATSESFHSAGPEPNAAEDAIEWWLAVEAWFEANDGRERVFDQVT
PKLVDFDSSSDGLTVEAEMTVGLRLPPGLSPEEAREILDALLPTGTVTFTGAVPAYMVSKRTPLARAFRV
AIREAGGTPRLKRKTGTSDMNVVAPAWGCPMVAYGPGDSDLDHTPDEHLPLAEYLRAIAVLTDVLERL
>gnl|CDD|235300 PRK04447, PRK04447, hypothetical protein; Provisional
IYTQIEGANSWLERLKGKNPLFVLVLGTTETSLIPGISAAGATPELTRYTPAADAELLLYGKPLSLPPLP
VTPTGCPTPALITRAVLELLGIPVLVVDAGLYVKPKVPYIDLGGGPGGDIRTGKAMPRVEELFERGRLLG
KSLSRPYDYLVIGESVPGGTTTALAVLTALGYDAAGKVSSSSPENPHELKRKVVEEGLKRAGLEPKDDPL
EAVAAVGDPMQAVVAGLAIGASSGGPVLLAGGTQMLAVAALIKAIGKEDLENIAIATTRWVAEDKSADFK
GLAEQIGVPLLASDLDFSNSKHPGLRAYERGYVKEGVGAGGAALLALLNGLSPEELLEAIEELYERLLGL
G
>gnl|CDD|235301 PRK04452, PRK04452, acetyl-CoA decarbonylase/synthase complex subunit delta; Provisional
MAFEIPKEEYAGKIREVTLGGTGPKTVKLGGETALPFYHFEGPMPNPPVIAMEVFDMPPEDWPEAVKEPF
GDVMNDPAAWAKKCVEEYGADMITLHLISTDPNGKDKSPEEAAKTVEEVLQAVDVPLIIGGSGNPEKDAE
VLEKVAEAAEGERCLLGSAEEDNYKKIAAAAMAYGHAVIAWSPLDINLAKQLNILLTELGVPRERIVMDP
TTGALGYGIEYSYSVMERIRLAALKGDEMLQMPMISGVGFEAWKAKEAWMPEEEDPEWGPREYRGILWEA
VTALTLLLAGADIFMMRHPESVKTLKEIIDTLMGKNAYV
>gnl|CDD|235302 PRK04456, PRK04456, acetyl-CoA decarbonylase/synthase complex subunit beta; Reviewed
MFEDIPVEISPMFEGERIRKADMYVELGGPKSEGFELVKVRDVDEVEDGKVEVIGPDLKDMEEGKRYPFA
IIVEVAGELLEEDLESVIERRIHEFCNYIQGVMHLNQRYDIWIRVSKDAHAKGLRSLEHIGKALMMLFKN
ELPFIEKIQVTIITDEEKVEEELEKAREIYKKRDERARDLHEEDVDVFYGCTLCQSFAPTHVCVITPDRP
SLCGAINWFDGRAAAKIDPEGPIFEIPKGELLDPETGEYSGVNEAVKERSQGEVDRVKLHSFFEYPHTSC
GCFEAVAFYIPEVDGIGIVHREYKGETPNGLPFSTMAGQTSGGKQVEGFLGISIEYMRSPKFLQADGGWE
RVVWMPKELKERVKEFIPEELRDKIATEEDVKDIEELKKFLKEKEHPVVERWAAEEEEEEEEEEEEEEEP
VAEVMMMPAPEMQLPASGGIKIILKNAKIYAEKVIIKKKEEKK
>gnl|CDD|179854 PRK04457, PRK04457, polyamine aminopropyltransferase
MARHPYRRLRPAKAGFPEVGVSEEGGVRSLHLGSDTVQSSMRIDDPSELELAYTRAMMGFLLFNPRPQHI
LQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVARNHFELPENGERFEVIEADGAEYIAVHRHSTDVI
LVDGFDGEGIIDALCTQPFFDDCRNALSSDGIFVVNLWSRDKRYDRYLERLESSFEGRVLELPAESHGNV
AVFAFKSAPKELRWDKLRKRAKKLENEHGLDFHRFVAKLKASNPNTGKRLLL
>gnl|CDD|179855 PRK04460, PRK04460, nickel-responsive transcriptional regulator NikR
ETIRFGVSLDSDLLEKFDELIEEKGYQNRSEAIRDLIRDFLVEHEWEEGDEEVAGTVTLVYNHHVSDLAQ
KLTEIQHDHHDEIISSLHVHLDHHNCLEVLVLKGKAKEIKKIADRLISTKGVKHGKLVMTTTGEDLV
>gnl|CDD|235303 PRK04517, PRK04517, hypothetical protein; Provisional
MKPIKPLTCLLALCFSGSASADVTMEVPDDVDLLVANGSKPKLSGGFFASTKTLELPDGENQIVFRYSPY
FSQGNDRIIVESDVIIATFDAANTELTFDMPKYRDARQAEKAIKTMQWQLVDEQGKAVEVRQDKLIKEGM
QIGRDYEREAAEYNKTGGVAALATPVTLSAMAVQPVAQQEISNATADNTAEEMLHFWYNKADAETKARFK
AYVNQQ
>gnl|CDD|235304 PRK04523, PRK04523, N-acetylornithine carbamoyltransferase; Reviewed
MSLKHFLNTQDWSRAELDALLTQAAAFKRNKLGSALKGKSIALVFFNPSLRTRTSFELGAFQLGGHAVVL
QPGKDAWPIEFELGAVMDGETEEHIREVARVLSRYVDLIGVRAFPKFVDWSKDRQDQVLNSFAKYSTVPV
INMETITHPCQELAHALALQEHFGTTLRGKKYVLTWTYHPKPLNTAVANSALLIATRLGMDVTLLCPTPD
YILDERYMDWAEQNAAESGGSLTVSHDIDSAYAGADVVYAKSWGALPFFGNWEPEKPIRDQYQHFIVDER
KMALTNNGVFSHCLPLRRNVKVTDAVMDSPNCIAIDEAENRLHVQKAIMAALASQ
>gnl|CDD|235305 PRK04527, PRK04527, argininosuccinate synthase; Provisional
SSKDIVLAFSGGLDTSFCIPYLQERGYAVHTVFADTGGVDAEERDFIEKRAAELGAASHVTVDGGPAIWE
GFVKPLVWAGEGYQGQYPLLVSDRYLIVDAALKRAEELGTRIIAHGCTGMGNDQVRFDLAVKALGDYQIV
APIREIQKEHTQTRAYEQKYLEERGFGVRAKQKAYTINENLLGVTMSGGEIDRWEAPGEGARGWCAPRSA
WPTEALTVTIKFVEGEAVALDGKPLPGAQILAKLNKLFAQYGVGRGVYTGDTVIGLKGRIVFEAPGLVSL
LTAHRALEDAVLTKQQNRFKPDVARKWVELVYEGFYHDPLKTDIEAFLKSSQAKVNGEVTLETRGGRVDA
VAVRSPHLLNSKGATYAQSADWGVEEAEGFIKLFGMSSTLYAQVNRSLRS
>gnl|CDD|235306 PRK04531, PRK04531, acetylglutamate kinase; Provisional
QANMKTRQIIVRLLSSMASAKEISQYLKRFSQLDAERFAVIKVGGAVLRDDLEALASSLSFLQEVGLTPI
VVHGAGPQLDAELDAAGIEKETVNGLRVTSPEALAIVRKVFQRSNLDLVEAVESSLRAGSIPVIASLGET
PSGQILNINADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSINLSTEYDHLMQQPWINGGMKLKLE
QIKELLDRLPLESSVSITSPSDLAKELFTHKGSGTLVRRGERILRATDWDELDLERLNLLIESSFGRTLK
PDYFDTTQLLRAYVSENYRAAAILTETGGGPYLDKFAVLDDARGEGLGRAVWNVMREETPQLFWRSRHNN
TINKFYYAESDGCIKQEKWKVFWYGLDDFEQIPKCVAHCANRPPTLES
>gnl|CDD|235307 PRK04537, PRK04537, ATP-dependent RNA helicase RhlB; Provisional
MSDKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNR
LLSRPALADRKPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIA
TPGRLIDYVKQHKVVSLHACEICVLDEADRMFDLGFIKDIRFLLRRMPERGTRQTLLFSATLSHRVLELA
YEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERH
GYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTAR
LGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPVTAELLTPLPRPPRVPVEGEEADDEAGDSVGTIFRE
AREQRAAEEQRRGGGRSGPGGGSRSGSVGGGGRRDGAGADGKPRPRRKPRVEGEADAAAAGAETPVVAAA
AAQAPGVVAADGERAPRKRRRRRNGRPVEGAEPVSTPVPAPAAPRKPTQVVATPVRAAAKSSGSPSLLGR
IGRRLRSLVSGN
>gnl|CDD|179862 PRK04539, ppnK, inorganic polyphosphate/ATP-NAD kinase; Provisional
MNSPFHNIGIVTRPNTPDIQDTAHTLITFLKQHGFTVYLDEVGIKEGCIYTQDTVGCHIVNKTELGQYCD
LVAVLGGDGTFLSVAREIAPRAVPIIGINQGHLGFLTQIPREYMTDKLLPVLEGKYLAEERILIEAALIR
EGKTAERALALNDAVLSRGGAGQMIEFEVFVNREFVYTQRSDGLIVSTPTGSTAYSLAAGGPIMQAGLHA
FTLVPICPQSMTNRPIAIPDTSEIEILVTQGGDARVHFDGQTHIDVQNLDRITIRRYRNPLRILHPTDYQ
YFKTLRQKLHWGEQLV
>gnl|CDD|179863 PRK04542, PRK04542, elongation factor P; Provisional
MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRR
PVTFSYIDGDEYVFMDNEDYTPYTFKKDQIEDELLFIPEGMPGMQVLTVDGQPVALELPQTVDLEIVETA
PSIKGASASARTKPATLSTGLVIQVPEYISTGEKIRINTEERKFMGRAD
>gnl|CDD|179864 PRK04561, tatA, twin arginine translocase protein A; Provisional
MGSFSIWHWLVVLVIVLLVFGTKRLTSGAKDLGSAVKEFKKGMHDDDKPAGQLGDDSRSAEQAREAQAER
DRDAR
>gnl|CDD|179867 PRK04598, tatA, twin-arginine translocase subunit TatA
MGGISIWQLLIIAVIVVLLFGTKKLRGIGSDLGSAVKGFKKAMSEEESAKANKKDADFEPKNLEQAKTEA
AAEKKKDKEQA
>gnl|CDD|179868 PRK04612, argD, acetylornithine transaminase
MSAAADSPLSLAHYYLPVYRPRQVVLERGQGSRVWDDQGREYLDLAAGIAVCGLGHNDPDLVAALTEQAG
KLWHTSNVFYSAPPLKLAEELVTASRFAEKVFLCNSGTEANEAAIKLVRKWASSQGRPADKRVIVTFRGS
FHGRTLAAVTATAQPKYQEGYEPLPGGFRYVDFNDVEALEAAMAGGDVAAVMLEPIQGEGGVMPAAPGFL
ARVRALCDQHDALLVLDEIQCGMGRTGTLFAHWQEQVTPDIVTLAKALGGGFPIGAMLAGPKVAETMQFG
AHGTTFGGNPLAAAVARVALRKLASPQIAANVARQSAALRAGLEALNAEFGVFAQVRGRGLMLGAVLAPA
HAGQAGAILDLAAEHGLLLLQAGPDVLRFVPALNLTDAELADGLARLRLALADYVAQR
>gnl|CDD|135173 PRK04654, PRK04654, sec-independent translocase; Provisional
MFDIGVGELTLIAVVALVVLGPERLPKAARFAGLWVRRARMQWDSVKQELERELEAEELKRSLQDVQASL
REAEDQLRNTQQQVEQGARALHDDVSRDIDIRTSATPVATPLELAHADLSASAQVDAAAGAEPGAGQAHT
PVPAPAPVIAQAQPIAPAPHQTLVPAPHDTIVPAPHAAHLPSAPATPVSVAPVDAGTSASPTPSEPTKIQ
EKQP
>gnl|CDD|179873 PRK04694, PRK04694, Maf-like protein; Reviewed
MLYLASRSPRRRELLQRLDVPFQTLQLDVPEVRAADESPDHYVQRVALEKAHAGLALVQAADADAIVLGS
DTEVVLGERVFGKPVDVDDAIAMLRALSGRTHQVLTAVVLVCAQRAPAQALVVSEVTFDLLDDAQIAAYA
ASGEPMGKAGAYAIQGRAERFIRHLSGSYSGVMGLPLYQTSQLLTAFGAH
>gnl|CDD|235310 PRK04750, ubiB, putative ubiquinone biosynthesis protein UbiB; Reviewed
PMELFRLYKIIRVFLRYGLDELILSHRLTRPLRLWRRSLFWMPNRHKDKPRGERLRLALEELGPIFVKFG
QMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARL
KDNGREVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGRRLKPREVVAEFEKTLHDELDLMREAANA
SQLRRNFEDSDMLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDG
FFHADMHPGNIFVSYDPPENPRYIALDFGIVGSLNKEDKRYLAENFLAFFNRDYRRVAELHVESGWVPPD
TRVEELEFAIRAVCEPIFDKPLAEISFGHVLLRLFNTARRFNVEIQPQLVLLQKTLLNVEGLGRQLDPQL
DLWKTAKPFLERWMKEQVGPRALVRALKEEAPFWAEKLPELPRLVHDSLRQGKLLQHSVDLLAEQLRTNR
LRQGQSRYLLGVGATLLLAGTLLLLSRPELMPGAAGLVAWLVGWRRT
>gnl|CDD|179875 PRK04758, PRK04758, hypothetical protein; Validated
MMDLPDVAAVQNESQQLGLASSAAELHGGLCGWLAGGGADGADWLARILADAGQVAPAQGSALDQLRQAT
VAQLEDRDFAFELLLAEDGAPLAARADALFDWCRAFLGGFGLAAQQRPALSEEGEEALQDLARLAQASSD
DFDAAEEDDTALAEIEEFVRVAVLLLHGDCVMGPRFRQRLN
>gnl|CDD|179876 PRK04761, ppnK, inorganic polyphosphate/ATP-NAD kinase; Reviewed
ASPTPEAQAALEELVKRYGDVPIEEADVIVALGGDGFMLQTLHRYMNSGKPVYGMNRGSVGFLMNEYSED
DLLERIAAAEPTVLHPLRMTATDVSGEVHEALAINEVSLFRQTRQAAKLRISIDGKVRMEELVCDGVLVA
TPAGSTAYNLSAHGPILPLGSNLLALTPISPFRPRRWRGALLPNSATVRFDVLEPDKRPVSAVADNTEVR
DVVEVTIREDKDITVTLLFDPGHSLEERILAEQFGY
>gnl|CDD|179877 PRK04778, PRK04778, septation ring formation regulator EzrA; Provisional
GMIYLIIAIVVIIIIAYLAGLILRKRNYKRIDELEERKQELENLPVNDELEKVKKLNLTGQSEEKFEEWR
QKWDEIVTNSLPDIEEQLFEAEELNDKFRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNRE
EVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVELTESGDYVEAREILDQLEEELAAL
EQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDHLDIEKEIQDLKEQIDENLALLEELDLDEA
EEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESV
RQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKL
ERYRNKLHEIKRYLEKSNLPGLPEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEE
ETEELVENATLTEQLIQYANRYRSDNEEVAEALNEAERLFREYDYKAALEIIATALEKVEPGVTKRIEDS
YEKEKETIR
>gnl|CDD|235313 PRK04813, PRK04813, D-alanine--poly(phosphoribitol) ligase subunit DltA
IMDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFL
GAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEILGIPVITLDELKDIFATGNPYDFDHAV
KGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGG
TLVALPKDMTANFKQLFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKL
LERFPSATIYNTYGPTEATVAVTSIEITDEMLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVIS
GPSVSKGYLNNPEKTAEAFFTFDGQPAYHTGDAGYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQS
SYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNG
KIDRKALIEEVNK
>gnl|CDD|179883 PRK04833, PRK04833, argininosuccinate lyase; Provisional
MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVR
ANPQQILASDAEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALV
ETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDRE
QLAGWLGFASATRNSLDSVSDRDHVLELLSDASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLM
PQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHMAALVLDGIQ
VKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLEDLPLAELQKFSSVIGDD
VYPILSLQSCLDKRAAKGGVSPQQVAQAIAAAKAR
>gnl|CDD|235314 PRK04837, PRK04837, ATP-dependent RNA helicase RhlB; Provisional
SKTHLTEQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYL
LSHPAPEDRKVNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGT
TGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFE
HMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGH
RVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAG
ASGHSISLACEEYALNLPAIETYIGHSIPVSKYDSDALLTDLPKPLRLTRPRTGNGPRRSGAPRNRRRRK
RSG
>gnl|CDD|235315 PRK04841, PRK04841, HTH-type transcriptional regulator MalT
MLIPSKLSRPVRLHNTVVRERLLAKLSGANNYRLVLVTSPAGYGKTTLISQWAAGKNNLGWYSLDESDNQ
PERFASYLIAALQQATNGHCSKSEALAQKRQYASLSSLFAQLFIELADWHQPLYLVIDDYHLITNPEIHE
AMRFFLRHQPENLTLVVLSRNLPPLGIANLRVRDQLLEIGSQQLAFDHQEAQQFFDQRLSSPIEAAESSR
LCDDVEGWATALQLIALSARQNNSSLHDSARRLAGINASHLSDYLVEEVLDNVDLETRHFLLRCSVLRSM
NDALIVRVTGEENGQMRLEELERQGLFIQRMDDSGEWFRYHPLFASFLRHRCQWELAQELPELHRAAAEA
WLAQGFPSEAIHHALAAGDAQLLRDILLQHGWSLFNQGELSLLEECLNALPWEVLLENPRLVLLQAWLAQ
SQHRYSEVNTLLARAEQELKDRNIELDGTLQAEFNALRAQVAINDGDPEEAERLAELALAELPLTWYYSR
IVATSVLGEVHHCKGELARALAMMQQTEQMARQHDVYHYALWSLLQQSEILFAQGFLQAAYETQEKAFQL
IEEQHLEQLPMHEFLLRIRAQLLWEWARLDEAEQCARKGLEVLSNYQPQQQLQCLAMLAKISLARGDLDN
ARRYLNRLENLLGNGRYHSDWIANADKVRLIYWQMTGDKEAAANWLRQAPKPEFANNHFLQGQWRNIARA
QILLGQFDEAEIILEELNENARSLRLMSDLNRNLILLNQLYWQQGRKSEAQRVLLEALKLANRTGFISHF
VIEGEAMAQQLRQLIQLNTLPELEQHRAQRILREINQHHRHKFAHFDEAFVEKLLNHPDVPELIRTSPLT
QREWQVLGLIYSGYSNEQIAGELDVAATTIKTHIRNLYQKLGIAHRQEAVQHAQDLLKMMGYG
>gnl|CDD|179886 PRK04860, PRK04860, SprT family zinc-dependent metalloprotease
LQQAVMRRLRECLAQANLYFKRTFPEPKVSYTQRGTSAGTAWLQSNEIRLNPVLLLENQQAFIDEVVPHE
LAHLLVYQLFGRVAPHGKEWQWMMESVLGVPARRTHQFEVQSVRGKTFPYRCKCQEHQLTVRRHNRVVRG
EAVYRCRRCGETLVFKGEQR
>gnl|CDD|235316 PRK04863, mukB, chromosome partition protein MukB
MIERGKFRSLTLVNWNGFFARTFDLDELVTTLSGGNGAGKSTTMAAFVTALIPDLTLLHFRNTTEAGATS
GSRDKGLHGKLKAGVCYAALDVVNSRGQRVLVGVRLQQVAGRDRKVDIKPFAIQGLPDSVQPTDLLTETV
NERQARVLTLNELKDKAAALEGVQFKQFNSITDYHSLMFDLGIIPRRLRSSSDRSKFYRLIEASLYGGIS
SAITRSLRDYLLPENSGVRKAFQDMEAALRENRMTLEAIRVTQSDRDLFKHLITESTNYVAADYMRHANE
RRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKI
ERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAV
QALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVS
RSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQ
EELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVT
EYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVLLSEIYDDVSLEDAP
YFSALYGPARHAIVVPDLSDAAEQLAGLEDCPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRY
SRFPEVPLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEAELR
QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAK
RFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEML
AKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPA
DSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCA
VLRLVKDNGVERRLHRRELAYLSADELRSMSDKALGALRLAVADNEHLRDVLRLSEDPKRPERKVQFYIA
VYQHLRERIRQDIIRTDDPVEAIEQMEIELSRLTEELTSREQKLAISSESVANIIRKTIQREQNRIRMLN
QGLQNISFGQVKSVRLNVNVRETHAMLLDALSEQQEQHQDLFNSARLTFSEALAKLYQRLNPHIDMGQRT
PQTIGEELLDYRNYLELEVEVNRGADGWLRAESGALSTGEAIGTGMSILVMVVQSWEEESRRLRGKDISP
CRLLFLDEAARLDAKSIATLFELCERLDMQLLIAAPENISPEKGTTYKLVRKVFNNREHVHVVGLRGFAQ
LLPDTLPGQDEAESGA
>gnl|CDD|235317 PRK04885, ppnK, inorganic polyphosphate/ATP-NAD kinase; Provisional
MKVAIISNGDPKSKRVASKLKKYLKDFGFILDEKNPDIVISVGGDGTLLSAFHRYENQLDKVRFVGVHTG
HLGFYTDWRPFEVDKLVIALAKDPGQVVSYPLLEVKITYEDGEKEKYLALNEATIKRIEGTLVADVYING
VLFERFRGDGLCVSTPTGSTAYNKSLGGAVLHPSIEALQLTEIASINNRVFRTLGSPLILPKHHTITLKP
VNDDDYQITVDHLTIKHKNVKSIEYRVANEKIRFARFRHFPFWKRVKDSFIGEVE
>gnl|CDD|235318 PRK04897, PRK04897, heat shock protein HtpX; Provisional
MLYEQIASNKRKTVFLLVVFFLLLALVGAAVGYLFLNSGLGGLIIALIIGVIYALIMIFQSTNVVMSMNH
AREVTEEEAPELWHIVEDMAMVAQIPMPRVFIIDDPSPNAFATGSSPKNAAVAVTTGLLAIMNREELEGV
IGHEISHIRNYDIRLSTIAVALASAITLLSDIAGRMMWWGGGSRRRDDDRDGGGLQIILLIVSLLLLILA
PLAATLIQLAISRQREYLADASSVELTRNPQGLISALEKISNSQPMKHPVDDASAALYISDPLKKKGLSK
LFDTHPPIEERIERLKNM
>gnl|CDD|235319 PRK04914, PRK04914, RNA polymerase-associated protein RapA
PFALGQRWISDTESELGLGTVVAVDGRTVTLLFPATGENRLYARNDAPLTRVMFNPGDTITSHEGWQLTV
EEVEEENGLLTYHGTRLDTEEEGVALRETFLDSKIRFNKPQDRLFAGQIDRMDRFALRYRALKHQSEQFQ
SPLRGLRGARASLIPHQLYIAHEVGRRHAPRVLLADEVGLGKTIEAGMIIHQQLLTGRAERVLILVPETL
QHQWLVEMLRRFNLRFSLFDEERYAEAQHDADNPFETEQLVICSLDFLRRNKQRLEQALAAEWDLLVVDE
AHHLVWSEEAPSREYQVVEQLAEVIPGVLLLTATPEQLGQESHFARLRLLDPDRFHDYEAFVEEQQQYRP
VADAVQALLAGEKLSDDALNALGELLGEQDIEPLLQAANSDSEEAQAARQELISELLDRHGTGRVLFRNT
RAAVKGFPKRELHPIPLPLPEQYQTAIKVSLEARARDMLYPEQIYQEFEDNATWWNFDPRVEWLIDFLKS
HRSEKVLVICAKAATALQLEQALREREGIRAAVFHEGMSIIERDRAAAYFADEEDGAQVLLCSEIGSEGR
NFQFASHLVLFDLPFNPDLLEQRIGRLDRIGQKHDIQIHVPYLEGTAQERLFRWYHEGLNAFEHTCPTGR
ALYDEFGDELIPYLASPDDTDGLDELIAETREQHEALKAQLEQGRDRLLELNSCGGEKAQALAEAIAEQD
DDTNLVNFALNLFDIIGINQEDRGENAIVLTPSDHMLVPDFPGLPEDGVTITFDRDQALSREDMQFLTWE
HPLIRGGLDLILSGDTGSTAVALLKNKALPAGTLLLELIYVVEAQAPKSLQLTRFLPPTPVRLLLDKNGN
DLSAQVEFESLNRQLSAVNRHTASKLVKAVQQDIHKLLQKAEAQAEAQARELIEQAKQEADEKLSAELSR
LEALKAVNPNIRDDEIEALESQRQEVLEALDQAQLRLDAIRLIVVT
>gnl|CDD|179893 PRK04923, PRK04923, ribose-phosphate diphosphokinase
MQDQRNLLVFSGNANKPLAQSICKELGVRMGKALVTRFSDGEVQVEIEESVRRQEVFVIQPTCAPSAENL
MELLVLIDALKRASAASVTAVIPYFGYSRQDRRMRSSRVPITAKVAAKMISAMGADRVLTVDLHADQIQG
FFDVPVDNVYASPLLLADIWRAYGTDNLIVVSPDVGGVVRARAVAKRLDDADLAIIDKRRPRANVATVMN
IIGDVQGKTCVLVDDLVDTAGTLCAAAAALKQRGALKVVAYITHPVLSGPAVDNINNSQLDELVVTDTIP
LSEAARACAKIRQLSVAELLAETIRRIAFGESVSSLYVD
>gnl|CDD|235320 PRK04926, dgt, deoxyguanosinetriphosphate triphosphohydrolase; Provisional
MAMIDFRKKINWQRRYRSPQGVKTEHEILRIFESDRGRIINSAAIRRLQQKTQVFPLERNAAVRSRLTHS
LEVQQVGRYIAKEILSRLKEQKLLEAYGLDELTGPFESIVEMACLMHDIGNPPFGHFGEAAINDWFRQRL
DPDAESQPLTDDRCSVAALRLRDGEEPLNELRRKIRQDLCHFEGNAQGIRLVHTLLRLNLTYAQVACILK
YTRPAWWRGPTPASHHYLMKKPGYYLSEEAYVARLRKELNLAPYSRFPLTYIMEAADDISYCIADLEDAV
EKRIFSVEQLYHHLHEAWGEHEKGDLFSLVVENAWEKSRANSLSRSSEDQFFMYLRVNTLNKLVPYAAQR
FIDNLPAIFAGTFNQALLEDASPASRLLKTFKNVARKHVFSHPEVEQLELQGYRVISGLLDIYSPLLALP
LEDFTELVEKERHKRYPIETRLFHKLSTRHRLAYVEAVSKLPSDSPEFPLWEYYYRARLIQDYISGMTDL
YAWDEYRRLMAVE
>gnl|CDD|179895 PRK04930, PRK04930, glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
MMSQPPKVLLLYAHPESQDSVANRVLLKPAQQLEHVTVHDLYAHYPDFFIDIPHEQALLREHDVIVFQHP
LYTYSCPALLKEWLDRVLSRGFASGPGGNALAGKYWRSVITTGEPESAYRYDGYNRYPMSDILRPFELTA
AMCRMHWLSPIIIYWARRQSPEELASHARAYGDWLANPLSAGGR
>gnl|CDD|179896 PRK04940, PRK04940, hypothetical protein; Provisional
MIIYLHGFDSTSPGNHEKVLQLQFIDPDVRLISYSTLHPKHDMQHLLKEVDKMLQLSDDERPLICGVGLG
GYWAERIGFLCGIRQVIFNPNLFPEENMEGKIDRPEEYADIATKCVTNFREKNRDRCLVILSRNDEVLDS
QRTAEELHPYYEIVWDEEQTHKFKNISPHLQRIKAFKTLG
>gnl|CDD|235321 PRK04946, PRK04946, endonuclease SmrB
MKKKDSLSEDDLALFRQLIKGTKKIKQDTIVHRPPRKKIKKKPEKRLLQEQADASHYFSDEFQPLLNTEG
PVRYVREDVDHFELKKLRRGDYSPELFLDLHGLTQLQAKQELGALIAACRKEHVFCACVMHGHGKHILKQ
QTPLWLAQHPDVMAFHQAPKEWGGDAALLVLIEIEEWPPRR
>gnl|CDD|179898 PRK04949, PRK04949, putative sulfate transport protein CysZ; Validated
SSSTSQPRSGFHYFIQGWKLILQPGLRRFVILPLLVNILLFGGAFWWLFTQLDAWIDWLMSQLPDWLSWL
SYLLWPLAVLSVLLVFSFFFSTLANFIAAPFNGLLAEKVEARLTGETLPDTGIAGLVKDVPRILKREWQK
LAYYLPRAIVLLLLSFIPVVGQTVAPVLWFLFSAWMMAIQYCDYPFDNHKVSFKDMRAALRQKRGTSLQF
GALVSLFTMIPLLNLVIMPVAVCGATAMWVDEYRDKHANWR
>gnl|CDD|235322 PRK04950, PRK04950, ProP expression regulator; Provisional
MENQPKLTSSKEVIAYLAERFPLCFSAEGEAKPLKIGIFQDLAERLADDEKVSKTQLRSALRLYTSSWRY
LYGVKAGAQRVDLDGNPCGELEEEHVEHARKQLEEAKAKVQAQRAEQQAKKREAAGEKEKAPRRERKPKP
KAPRKKRKPRAQKPEPQHTPVSDISELTVGQAVKVKAGKSAMDATVLEITKDDVRVQLDSGLSMIVRAEH
LVF
>gnl|CDD|235323 PRK04960, PRK04960, universal stress protein UspB; Provisional
MISTVALFWALCVVCIVNMARYFSSLRALLVVLRGCDPLLYQYVDGGGFFTSHGQPNKQVRLVWYIYAQR
YLDHHDPEFIRRCERVRRQFILTSALCGLVVVSLIALMIWH
>gnl|CDD|179901 PRK04964, PRK04964, hypothetical protein; Provisional
MYKYCELVRKRYAEIGSGDLGYVPDALGCVLKALNEIAADEALPESVREKAAYAAANLLVSDYVDE
>gnl|CDD|179902 PRK04965, PRK04965, NADH:flavorubredoxin reductase NorW
MSNGIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHVFSQGQRADDLTRQSAGEFAEQ
FNLRLFPHTWVTDIDAEAQVVKSQGNQWQYDKLVLATGASAFVPPIPGRELMLTLNSQQEYRAAETQLRD
AQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLE
KTDSGIRATLDSGRSIEVDAVIAAAGLRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAEINGQ
VLPFLQPIQLSAMALAKNLLGQNTPLKLPAMLVKVKTPELPLQLAGETQRQDLRWQINAESQGMVAKGVD
EAGQLRAFVVSEDRMKEAFPLLKELPV
>gnl|CDD|179903 PRK04966, PRK04966, hypothetical protein; Provisional
MIIPWQDLAPETLENLIESFVLREGTDYGEHERSLEQKVADVKRQLQSGEAVLVWSELHETVNIMPKSQF
RE
>gnl|CDD|235324 PRK04968, PRK04968, SecY interacting protein Syd; Provisional
MSVAQALDDFTQRYCDAWQEEHGELPRSEELYGVPSPCIIETSEDAVYWQPQPFEPEGNFNNVERALEIT
LHPDIHAFYTTQFAGDMTAQFGGGELTLLQVWSEDDFERLQENLIGHLVMQKRLKLPPTLFIATTDEEDE
VISVCNLSGEVILETLGTRKRTVLAPSLAEFLNQLEPLLAP
>gnl|CDD|179905 PRK04972, PRK04972, putative transporter; Provisional
MNINVADLLNGNYILLLFVVLALGLCLGKLRLGSIQLGNSIGVLVVSLLLGQQHFSINTDALNLGFMLFI
FCVGVEAGPNFFSIFFRDGKNYLMLALVMVGSALVIALGLGKLFGWDIGLTAGMLAGSMTSTPVLVGAGD
TLRHSGAESRQLSLALDNLSLGYALTYLIGLVSLIVGARYLPKLQHQDLQTSAQQIARERGLDTDAQRKV
YLPVIRAYRVGPELVAWTDGKNLRELGIYRQTGCYIERIRRNGILANPDGDAVLQMGDEIALVGYPDAHA
RLDPSFRNGKEVFDRDLLDMRIVTEEIVVKNHNAVGKRLSQLKLTDHGCFLNRVIRSQIEMPIDDNVVLN
KGDVLQVSGDARRVKTIADRIGFISIHSQVTDLLAFCAFFIIGLMIGMITFQFSNFSFGIGNAAGLLFAG
IMLGFLRANHPTFGYIPQGALNMVKEFGLMVFMAGVGLSAGSGINNGLGAVGGQMLIAGLIVSLVPVVIC
FLFGAYVLRMNRALLFGAIMGARTCAPAMEIISDTARSNIPALGYAGTYAIANVLLTLAGTLIVIVWP
>gnl|CDD|235325 PRK04974, PRK04974, glycerol-3-phosphate 1-O-acyltransferase PlsB
MSGWRRLYYKLLNLPLKLLVKSKVIPADPAEELGLDPSRPIVYVLPYNSLSDLLTLRKQCLKLGLPDPLE
PLEINGLQLPRYVFLHGGPRLFGYRTPKEESSPLFHRLLDLHRQNPELDVQLVPVSVFWGRAPGKEDSEL
RLLNGDNWAVPGRLRKLFAILWLGRDTFVRFSPPVSLRYMADEHGTDKRIARKLARVARVHFRRQRLAAI
GPDLPHRQALFNKLLASPAIKKAIEDEAKSKKISHEKARQNAIAYMDEIAADYSYSAIRLADRFLTWLWN
RLYQGINVHNAERVRQLAQDGHEIVYVPCHRSHMDYLLLSYVLYHQGLVPPHIAAGINLNFWPAGPIFRR
GGAFFIRRSFKGNKLYSTVFREYLGELFARGYSVEYFVEGGRSRTGRLLQPKTGMLAMTLQAMLRGSRRP
ITLVPVYIGYEHVMEVGTYAKELRGAPKEKESLFQVLRGIRKLRNFGQGYVNFGEPIPLNDYLNQHVPEW
RESIDPIEEQRPAWLTPAVNNLANQVMVRINNAAAANPVNLCALALLASRQRALDREQLIEQLDLYLQLL
RNVPYSSDTTVPEGSGEELIDHALSLNKFEVEKDTLGDIISLDREQAVLMTYYRNNILHLFVLPSLIASI
VTHNRRISRDELLRIVNALYPFLKAELFLRWDEEELPEVIDQIIDELVRQGLITLDDDELHINPPRSREL
QLLAAGVRETLQRYAITLSLLSGSPNISRSELEKESHLLAQRLSVLHGINAPEFFDKALFSSFIQTLREE
GYIRDDDSGDLEFEETLEIYAILKRLLSPEVRLTIEQVAQAEEEEEAK
>gnl|CDD|235326 PRK04976, torD, chaperone protein TorD; Validated
MQMTTLTNEQRACVYAWLSSLFAKELDDEQLAQLQSAEFASFFALLASEPPLTASVNELQNALATLTDRD
DAQLELAADFCGLFLLTDKHSALPYASAYLQEGLLFGEPHQEMKELLVEAGLQVNSDFNEPADHLAVYLE
LLSHLIFSSGERQQLLFIQTALLSWLPEFAAKCTQYDSFGFYAALSQLLLAFVQLDHQNLDG
>gnl|CDD|179908 PRK04980, PRK04980, hypothetical protein; Provisional
QPNKITFFERFEADILAGRKTITIRDESESHFKPGDVLRVGTFEDDRYFCTIEVLSVSPVTFDELNEKHA
EQENMTLPELKQVIAEIYPNLDQLYVIEFKLL
>gnl|CDD|179909 PRK04984, PRK04984, fatty acid metabolism transcriptional regulator FadR
MVIKAQSPAGFAEEYIIESIWNNRFPPGSILPAERELSELIGVTRTTLREVLQRLARDGWLTIQHGKPTK
VNNFWETSGLNILETLARLDHDSVPQLIDNLLSARTNISAIFIRTAFRNNPEKALEVLATAEELEDTAEA
FAEFDYNLFRGLAFASGNPIYGLILNGLKGLYTRVGRYYFSNPEARELALGFYHKLSALCEEGNHDQVPE
CVRQYGIESGEIWHRMQKNLPGDLAEQGR
>gnl|CDD|235327 PRK04987, PRK04987, fumarate reductase subunit FrdC
MTTKRKPYVRPMTPTWWKKLPFYRFYMLREATAVPAVWFSLVLIYGLFALKNGPEAWAGFVSFLQNPIVV
ILNIITLAAALLHTKTWFEMAPKAANIIVKDEKMGPEPIIKALWAVTAVVSLVILVVALL
>gnl|CDD|235328 PRK04989, psbM, photosystem II reaction center protein M; Provisional
MEVNDLGFVASLLFVLVPTVFLIILYIQTNSREES
>gnl|CDD|179912 PRK04998, PRK04998, hypothetical protein; Provisional
MMKTKLKELLEFPCSFTYKVMGLARPELVDQVVEVVQRHAPGDYTPTVKPSSKGNYHSVSITITATSIEQ
VETLYEELAKIEGVRMVL
>gnl|CDD|235329 PRK05007, PRK05007, bifunctional uridylyltransferase/uridylyl-removing protein GlnD
QYANTALPTLPGQPQSPLTWPDDELTVGGLKQHLDTFQQWLGDAFDAGISAEQLVEARTEFIDQLLQRLW
IEAGFDQIPDLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELITLLWDLKLEVGHSVRTLE
ECLLEGLSDLTVATNLIESRLLCGDVALFLELQKHIFSDGFWPSEKFYAAKVEEQNERHQRYHGTSYNLE
PDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECQHFLWRIRFALHLVLSRYDNR
LLFDRQLSVAQLLGYEGEGNEPVERMMKDYYRTTRRVSELNQMLLQLFDEAILALTADEKPRPIDDEFQL
RGTLIDLRDETLFQRQPEAILRMFYLMARNSNITGIYSTTLRQLRHARRHLNQPLCEIPEARKLFMEILR
HPGAVSRALLPMHRHSVLSAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLLKLESFADEETRQRHPLCVE
LYPRLPKKELLLLAALFHDIAKGRGGDHSILGAQDALEFAELHGLNSRETQLVAWLVRNHLLMSVTAQRR
DIQDPDVIKQFAEEVQDENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMENPPDMR
ERVRHHQLQALALLRMDNIDEEALHQIWSRCRADYFLRHTPNQLAWHARHLLQHDLDKPLVLLSKQATRG
GTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTSRDGMAMDTFIVLEPDGSPLSQDRHQVIRKALEQ
ALTQSSPQPPKPRRLPAKLRHFNVPTEVSFLPTHTDRRSYMELIALDQPGLLARVGKIFADLGISLHGAR
ITTIGERVEDLFILATADRRALNEELQQELRQRLTEALNPNDKG
>gnl|CDD|179914 PRK05014, hscB, co-chaperone HscB; Provisional
MDYFTLFGLPARYDIDTQLLASRYQELQRQFHPDKFANASERERLLAVQQAATINDAYQTLKHPLKRAEY
LLSLHGFDLAHEQHTVRDTAFLMEQMELREELEDIEQSKDPEAALESFIKRVKKMFKTRLQQMVEQLDNE
AWDAAADTVRKLKFLDKLRSEVEQLEEKLLD
>gnl|CDD|235330 PRK05015, PRK05015, aminopeptidase B; Provisional
MKITLSTQPADARWGEKALLSFNEDGATIHLNGKDDLGLIQRAARKLDGQGIKHVALAGEGWDLERCWAF
WQGFRTPKGTRKVEWPDLDDAQQQELDARLKIIDWVRDTINAPAEELGPEQLAQRAADLICSVAGDAVSY
RIIKGEDLREQGYMGIHTVGRGSERPPVLLALDYNPTGDPDAPVYACLVGKGITFDSGGYSIKPSAGMDS
MKSDMGGAATVTGALALAITRGLNKRVKLFLCCAENLISGNAFKLGDIITYRNGKTVEVMNTDAEGRLVL
ADGLIDASEQGPPLIIDAATLTGAAKTALGNDYHALFSFDDELAQRLLASAAQENEPFWRLPLAEFHRSQ
LPSNFADLANSGSGAGPAGASTAAGFLSHFVENYQQGWLHIDCSATYRKSAVDQWAAGATGLGVRTIANL
LLAK
>gnl|CDD|235331 PRK05022, PRK05022, nitric oxide reductase transcriptional regulator NorR
FSLDALLPIALDLSRGLPHQDRFQRLLTTLRQVLPCDASALLRLDGDQLVPLAIDGLSPDVLGRRFALEE
HPRLEAILRAGDPVRFPADSELPDPYDGLIPGVQESLPVHDCMGLPLFVDGRLIGALTLDALDPGQFDAF
SDEELRALAALAAATLRNALLIEQLESQAELPQDVAEFLRQEALKEGEMIGQSPAMQQLKKEIEVVAASD
LNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELA
DGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRL
SVFPLSVPPLRERGDDVLLLAGYFLEQNRARLGLRSLRLSPAAQAALLAYDWPGNVRELEHVISRAALLA
RARGAGRIVTLEAQHLDLPAEVALPPPEAAAAPAAVVSQNLREATEAFQRQLIRQALAQHQGNWAAAARA
LELDRANLHRLAKRLGLKD
>gnl|CDD|235332 PRK05031, PRK05031, tRNA (uracil-5-)-methyltransferase; Validated
MTPECLPPEQYEAQLAEKVARLKELFAPFSAPEPEVFRSPPSHYRMRAEFRIWHEGDDLYYAMFDQQTKQ
RIRIDQFPIASELINALMPALLAALRANPVLRHKLFQVDFLSTLSGEILVSLLYHKKLDEEWEQAAKALR
DALFNVHLIGRSRKQKIVLDQDYVDERLPVAGREFIYRQVENSFTQPNAAVNEKMLEWALDATKGSKGDL
LELYCGNGNFTLALARNFRRVLATEISKPSVAAAQYNIAANGIDNVQIIRMSAEEFTQAMNGVREFNRLK
GIDLKSYNFSTIFVDPPRAGLDDETLKLVQAYERILYISCNPETLCENLETLSQTHKVERFALFDQFPYT
HHMECGVLLEKK
>gnl|CDD|235334 PRK05035, PRK05035, electron transport complex protein RnfC; Provisional
QIRKGKLWDFPGGIHPPEMKTQSNGTPIRQAPLPQRLVIPLKQHIGAEGELCVKVGDRVLKGQPLTQGDG
RMSLPVHAPTSGTVVAIEPHPTAHPSGLAELCVVIEPDGEDRWIERQPWADYRQLSPEELIERIRQAGIA
GLGGAGFPTAVKLQPGGDKIETLIINGAECEPYITADDRLMRERADEIIEGIRILAHLLQPKEVLIGIED
NKPEAIAALRAALAGADDIRVRVIPTKYPSGGEKQLIQILTGKEVPSGGRPADIGVLMQNVGTAYAIKRA
VIDGEPLIERVVTLTGEAVARPGNVWARLGTPVRHLLNQAGFKPDADQRVIMGGPMMGFTLPSLDVPVVK
TTNCLLAPSATELPPPPPEQPCIRCGACADACPASLLPQQLYWFAKAEEHDKAQEYNLFDCIECGACAYV
CPSNIPLVQYYRQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAKDKDAVAA
ALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAK
KAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAE
QQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ
>gnl|CDD|179920 PRK05054, PRK05054, exoribonuclease II; Provisional
MFQDNPLLAQLKQQLHSQTPRVEGVVKATEKGFGFLEVDAQKSYFIPPPQMKKVMHGDRIIAVIHTEKDR
EIAEPEELIEPFLTRFVGRVQKKDDRLSIVPDHPLLKDAIPCRAAKGLNHEFKEGDWVVAELRRHPLKGD
RGFYAEITQFITDADDHFAPWWVTLARHNLEREAPAGGVAWEMLDEGLEREDLTALDFVTIDSASTEDMD
DALYVEKLPDGGLQLTVAIADPTAYIAEGSKLDKAARQRAFTNYLPGFNIPMLPRELSDDLCSLRPNERR
PALACRVTIDADGTIEDDIRFFAAWIESKAKLAYDNVSDWLENGGDWQPESEAIAEQIRLLHQFCLARSE
WRKQHALVFKDRPDYRFELGEKGEVLDIVAEPRRIANRIVEESMIAANICAARVLRDKLGFGIYNVHSGF
DPANAEQAVALLKEHGLHFDAEELLTLEGFCKLRRELDAQPTGYLDSRIRRFQSFAEISTEPGPHFGLGL
EAYATWTSPIRKYGDMINHRLLKAVIKGETAERPQDEITVQLAERRRLNRMAERDVGDWLYARYLKDKAG
TDTRFAAEIIDISRGGMRVRLLENGAVAFIPASFLHAVRDELVCNQENGTVQIKGETVYKLGDVIDVTLA
EVRMETRSIIARPV
>gnl|CDD|235335 PRK05057, aroK, shikimate kinase AroK
MAEKRNIFLVGPMGAGKSTIGRQLAQQLNMEFYDSDQEIEKRTGADIGWVFDVEGEEGFRDREEKVINEL
TEKQGIVLATGGGSVKSRETRNRLSARGVVVYLETTIEKQLARTQRDKKRPLLQVDDPREVLEALANERN
PLYEEIADVTIRTDDQSAKVVANQIIHMLESN
>gnl|CDD|179922 PRK05066, PRK05066, transcriptional regulator ArgR
MRSSAKQEELVKAFKALLKEEKFGSQGEIVTALQEQGFDNINQSKVSRMLTKFGAVRTRNAKMEMVYCLP
AELGVPTTSSPLKNLVLDIDHNDALIVIHTSPGAAQLIARLLDSLGKAEGILGTIAGDDTIFITPASGFT
IKELLEAILELFEQEL
>gnl|CDD|179923 PRK05070, PRK05070, DNA mismatch repair protein; Provisional
SPPQSEEELLARAQQLAGLTLGELAAEAGLPVPKDLKRDKGWVGQLLELALGASAGSKPEQDFAHLGIEL
KTIPIDSSGKPLETTFVCVAPLTGNSGVTWETSHVRHKLKRVLWIPVEGERSIPLAERRVGSPLLWSPNE
EEERQLRQDWEELMDLIVLGQVERITARHGEVLQLRPKAANSKALTEAIGENGEPILTLPRGFYLKKNFT
AAILARHF
>gnl|CDD|235336 PRK05074, PRK05074, non-canonical purine NTP phosphatase
AMYHVIVASTNPAKINAILQAFSEIFPEGSCHIEGVAVPSGVPDQPMGSEETRAGARNRVKNARQLRPEA
DFWVAIEAGIDGDATFAWMVIENAQQRGESRSASLPLPAVVLEALRQGEELGDVMDRLFGTDNIKQKGGA
IGLLTAGKLTRESVYHQALILALAPFHNPEYYP
>gnl|CDD|235337 PRK05077, frsA, esterase FrsA
MTQANLSETLFKPRFKHPETSTLVRRFNHGSQPPIQSALDGKTVPHWYRMINRLMWIWRGIDPIEIEEVL
ARIAMSDAERTDDELLDTVIGYRGGNWIYEWAKQAMEWQQKACAEEDPEEAGRHWLHAANLYSIAAYPHL
KGDELAEQAQVLANRAYEEAAKRLPGELKELEFPIPGGGPITGFLHLPKGDGPFPTVLVCGGLDSLQTDY
YRLFRDYLAPRGIAMLTIDMPSVGFSSKWKLTQDSSLLHQAVLNALPNVPWVDHTRVAAFGFRFGANVAV
RLAYLEPPRLKAVACLGPVVHTLLTDPKRQQQVPEMYLDVLASRLGMHDASDEALRVELNRYSLKVQGLL
GRRCPTPMLSGYWKNDPFSPEEDSRLIASSSADGKLLEIPFKPVYRNFDKALQEISDWLEDRLC
>gnl|CDD|235338 PRK05082, PRK05082, N-acetylmannosamine kinase; Provisional
MTTLAIDIGGTKIAAALVGEDGQIRQRRQIPTPASQTPEALRQALSALVSPLQAQADRVAVASTGIINDG
ILTALNPHNLGGLLHFPLVQTLEQLTDLPTIALNDAQAAAWAEYQALPDDIRNMVFITVSTGVGGGIVLN
GKLLTGPGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGWLAGCDAKTIFERAGQGDEQA
QALINRSAQAIARLIADLKATLDCQCVVLGGSVGLAEGYLELVQAYLAQEPAIYHVPLLAAHYRHDAGLL
GAALWAQGEKL
>gnl|CDD|235339 PRK05084, xerS, site-specific tyrosine recombinase XerS; Reviewed
MEKEKYLKLIDKLKAKMPWYVQEYYQSKLATPYSPTTLYEYLTEYRRFFNWLISEGLSDASKIKDIPLST
LENLTKKDVEAFILYLRERPLLNGHSTKKGNSQTTINRTLSALKSLFKYLTEEAENEDGEPYFYRNVMKK
IELKKKKETLAARAHNLKQKLFLGDEDYEFLDFIDNEYEQKLSNRALSSFKKNKERDLAIIALILGSGLR
VSELVNLDLSDLNLKQMTIDVTRKGGKRDSVNIAPFALPYLEEYLKIRASRYKAEKQEKALFLTKYRGKP
NRISARAIEKMVAKYSEAFGVRLTPHKLRHTLATRLYDATKDQVLVADQLGHTSTETTDLYTHIVNDEQK
EALDRLE
>gnl|CDD|179929 PRK05087, PRK05087, D-alanine--poly(phosphoribitol) ligase subunit DltC
MDFKEQVLDILEELTGEDIVSENMDEDLFEEGILDSMGTVELLVELENRFDIEVPVSEFDRDDWNTPNKI
IAKVEELQ
>gnl|CDD|235341 PRK05089, PRK05089, cytochrome C oxidase assembly protein; Provisional
MSAMAQKRSNRRLVFKLLLVVVGMFGFGFALVPLYDVFCEVTGINGTTQAARVEAASQVDLSRTITVEFD
ANVNGGLPWEFKPEQRSVDVHPGELNLVFYEAENLSDRPIVGQAIPSVTPGQAGAYFNKIECFCFTQQTL
QPGETREMPVVFYVDPDLPKDVKTITLSYTFFDVTAPAPAAAAAAGAA
>gnl|CDD|179931 PRK05090, PRK05090, hypothetical protein; Validated
MSAVTWDGDGLVLRLYIQPKASRDQIVGLHGDELKVAITAPPVDGQANAHLLKFLAKQFRVAKSQVVIEK
GELGRHKQVRIINPQQIPPEIAALL
>gnl|CDD|235342 PRK05092, PRK05092, PII uridylyl-transferase; Provisional
PDPPMAPRPLSLSEIFDRAALRAELDALAADAAGDPDALRAAVLALLKQALARGRAEARERLEADGSGRA
CARRLAYLTDELIRALYDFATTHLYPADNPSEGERLAVLAVGGYGRGELAPGSDIDLLFLLPYKQTAWAE
SVVEYMLYMLWDLGLKVGHATRSIDECIRLAREDMTIRTALLEARFLAGDRALFEELETRFDKEVVKGTA
AEFVAAKLAERDERHRRAGDSRYLVEPNVKEGKGGLRDLHTLFWIAKYVYRVRDAAELVKLGVFTREEYR
LFRRAEDFLWAVRCHLHFLTGRAEERLSFDLQPEIAERMGYTDHPGLSGVERFMKHYFLVAKDVGDLTRI
FCAALEAQHAKRAPGLNRFARRRRKALDSDGFVVDNGRINLADPDVFERDPVNLIRLFHLADRHGLDIHP
DAMRLVTRSLRLIDAALREDPEANRLFLDILTSRRNPERVLRRMNEAGVLGRFIPDFGRIVAMMQFNMYH
HYTVDEHTIRAIGVLAEIERGELADEHPLASELMPKIESRRALYVAVLLHDIAKGRPEDHSIAGARIARR
LCPRLGLSPAETETVAWLVEHHLLMSDTAQKRDLSDPKTIEDFADAVQSPERLKLLLILTVADIRAVGPG
VWNGWKAQLLRTLYYETEEVLTGGFSELNRAERVAAAKEALREALSDWPKADRDAYLARHYPAYWLAVDL
DTQARHARFIRDADDAGRPLATEVRPDPARGVTEVTVLAADHPGLFSRIAGACAAAGANIVDARIFTTTD
GRALDTFWIQDAFGRDEDEPRRLARLAKAIEDALSGEVRLPEALAKRTKPKKRARAFHVPPRVTIDNEAS
NRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRAL
LAALAEGEAEARAARPPGAVA
>gnl|CDD|179933 PRK05093, argD, acetylornithine/succinyldiaminopimelate transaminase
TEQTAVTRATFDEVMVPNYAPAEFIPVRGEGSRVWDQQGKEYIDFAGGIAVTALGHCHPALVKALKEQGE
KLWHISNVFTNEPALRLAKKLIDATFAERVFFANSGAEANEAAFKLARRYACDRHGPEKTEIIAFHNSFH
GRTLFTVSVGGQPKYSDGFGPKPADITHVPFNDLAAVKAVIDDHTCAVVVEPIQGEGGVIPATPEFLQGL
RELCDQHNALLIFDEVQTGMGRTGDLFAYMHYGVTPDILTSAKALGGGFPIGAMLTTAEIASHFKVGTHG
STYGGNPLACAVAEAVFDIINTPEVLEGVKARRQRFVDGLQKINQKYGVFSEIRGMGLLIGAELKPQYKG
RARDFLNAAAEEGVMVLVAGPDVLRFAPSLVIEEADIDEGLARFEKAVAKVVA
>gnl|CDD|179934 PRK05094, PRK05094, dsDNA-mimic protein; Reviewed
MDLNNRLTEDETLEQAYDIFLELAADNLDPADILLFNLQFEERGGAELVDPAEDWQEHVGFDVDPDFFAE
VWIGLANSEDDEIDDVFARFLISREKDHKLCHILWKE
>gnl|CDD|235343 PRK05096, PRK05096, guanosine 5'-monophosphate oxidoreductase; Provisional
MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFD
ILTAVHKHYSVEEWAAFVNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQ
FVAKAREAWPDKTICAGNVVTGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAH
GLGGQIVSDGGCTVPGDVAKAFGGGADFVMLGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVG
GVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTFIRVQEQENRVFNN
>gnl|CDD|235344 PRK05097, PRK05097, macrodomain Ter protein MatP
MKYQQLENLESGWKWKYLVKKHREGELITRYIEASAAQEAVDELLKLENEPVKVLEWIDKHMNPELVNRM
KQTIRARRKRHFNAEHQHTRKKSIDLEYRVWQRLAGLAQRRGKTLSETIVQLIEDAERKEKYANQMSSLK
QDLKALLGKE
>gnl|CDD|179937 PRK05101, PRK05101, galactokinase; Provisional
MSLKQKTQSLFAQQFGYPPTHTIQAPGRVNLIGEHTDYNDGFVLPCAIDYQTVISCAKRDDRIVRVIAAD
YDNQQDEFSLDAPIVPHPEQQWANYVRGVVKHLQERNPDFGGADLVISGNVPQGAGLSSSASLEVAVGQT
FQQLYHLPLSGAEIALNGQEAENQFVGCNCGIMDQLISALGKKDHALLIDCRSLETKAVPMPEGVAVVII
NSNVKRGLVDSEYNTRRQQCETAARFFGVKALRDVTLEQFNAVAAELDPVVAKRARHVITENARTLEAAS
ALAAGDLKRMGELMAESHASMRDDFEITVPQIDTLVEIVKAVIGDQGGVRMTGGGFGGCIVALVPEELVE
AVRQAVAEQYEAKTGLKETFYVCKASQGAGQC
>gnl|CDD|235345 PRK05105, PRK05105, O-succinylbenzoate synthase; Provisional
MRSAQLYRYQIPMDAGVPLRKQRLKTRDGLVVQLREGEREGWGEIAPLPGFSQETLEEAQEALLAWLNNW
LAGDCDDELSQYPSVAFGLSCALAELAGTLPQAANYRTAPLCYGDPDELILKLADMPGEKVAKVKVGLYE
AVRDGMLVNLLLEAIPDLKLRLDANRGWTLEKAQQFAKYVPPDYRHRIAFLEEPCKTPDDSRAFARATGI
AIAWDESLREPDFQFEAEPGVRAIVIKPTLTGSLEKCQELIEQAHALGLRAVISSSIESSLGLTQLARLA
AWLTPDTIPGLDTLDLMQAQLVRPWPGSKLPLLTLDELELLW
>gnl|CDD|235346 PRK05111, PRK05111, acetylornithine deacetylase; Provisional
KMKLPSFIEMYRALIATPSISATDPALDQSNRAVIDLLAGWFEDLGFNVEIQPVPGTRGKFNLLASLGSG
EGGLLLAGHTDTVPFDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILAT
ADEETSMAGARAFAEATAIRPDCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHD
VIGELLQLRDELQERYHNPAFTVPYPTLNLGHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREA
LAPVSERWPGRITVAPLHPPIPGYECPADHQLVRVVEKLLGHKAEVVNYCTEAPFIQQLGCPTLVLGPGS
IEQAHQPDEYLELSFIKPTRELLRQLIHHFCLH
>gnl|CDD|235347 PRK05113, PRK05113, electron transport complex protein RnfB; Provisional
MSAIWIAVAALSLLALVFGAILGFASRRFKVEGDPIVEKIDAILPQSQCGQCGYPGCRPYAEAIANGEKI
NKCPPGGEATMLKLAELLGVEPQPLDGEAQEATPARKVAFIDEDNCIGCTKCIQACPVDAIVGATKAMHT
VISDLCTGCDLCVAPCPTDCIEMIPVAETPDNWKWDLNTIPVRIIPVEQHA
>gnl|CDD|179941 PRK05114, PRK05114, YoaH family protein
MFAGLPSLTHEQQQKAVERIQELMAQGMSSGEAIALVAEELRANHQGERIVARFEDEDE
>gnl|CDD|235348 PRK05122, PRK05122, major facilitator superfamily transporter; Provisional
EPVAEPALSGLRLTLRIVSIVMFTFISYLTIGLPLAVLPGYVHDQLGFSAFLAGLVISLQYLATLLSRPH
AGRYADTLGPKKAVVFGLCGCALSGLLYLLAGLLAAWPVLSLLLLLLGRLLLGIGESLAGTGSILWGIGR
VGALHTGRVISWNGIATYGALAIGAPLGVLLYHWGGLAGLGLLIMLLALLGLLLARPRPAVPPVKGERLP
FRRVLGRVWPYGMGLALASIGFGTIATFITLYYAARGWDGAALALTLFGVAFVGARLLFGNLINRLGGLR
VAIVSLLVEILGLLLLWLAPSPWMALIGAALTGFGFSLVFPALGVEAVKRVPPQNRGAALGAYSVFLDLS
LGITGPLAGLVASWFGYPSIFLAAALAALLGLALTWLLYRRAPRAVPEA
>gnl|CDD|235349 PRK05124, cysN, sulfate adenylyltransferase subunit 1; Provisional
MNTAIAQQIANEGGVEAYLHAQQHKSLLRFLTCGSVDDGKSTLIGRLLHDTKQIYEDQLASLHNDSKRHG
TQGEKLDLALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDA
RKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNLDIRFVPLSALEG
DNVVSQSESMPWYSGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPNLDFRGYAGTLASGVVKVGDRVKV
LPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDEIDISRGDLLVAADEALQAVQHASADVVWMAEQPLQ
PGQSYDIKIAGKKTRARVDAIRYQVDINTLTQREAENLPLNGIGLVELTFDEPLVLDPYQQNRVTGGFIF
IDRLTNVTVGAGMVREPLAQATAAPSEFSAFELELNALVRRHFPHWGARDLLGG
>gnl|CDD|235352 PRK05151, PRK05151, electron transport complex protein RsxA; Provisional
MTEYLLLFVSTVLVNNFVLVKFLGLCPFMGVSKKLETAIGMGLATTFVLTLASICAWLVNTYILIPLDLI
YLRTLAFILVIAVVVQFTEMVVRKTSPTLYRLLGIFLPLITTNCAVLGVALLNINLGHNFLQSALYGFGA
AVGFSLVLVLFAAIRERLAVADVPAPFRGAAIALITAGLMSLAFMGFTGLVKL
>gnl|CDD|235354 PRK05159, aspC, aspartyl-tRNA synthetase; Provisional
MMKRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEELFETIKKLKRESV
VSVTGTVKANPKAPGGVEVIPEEIEVLNKAEEPLPLDISGKVLAELDTRLDNRFLDLRRPRVRAIFKIRS
EVLRAFREFLYENGFTEIFTPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGP
VFRAEEHNTSRHLNEYTSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPETPIP
RITYDEAIEILKSKGNEISWGDDLDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISK
SFDLLFRGLEITSGGQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLE
NIREAVLFPRDRHRLTP
>gnl|CDD|179950 PRK05166, PRK05166, histidinol-phosphate transaminase
ECMAPPSSLARAEVRPLPPYNAGLTIEEVRARYGVPRIAKLGSNENPLGPSPAVRRAFADIAELLRLYPD
PQGRALREAIAARTGVPADRIILGNGSEDLIAVICRAVLRPGDRVVTLYPSFPLHEDYPTMMGARVERVT
VTPDLGFDLDALCAAVARAPRMLMFSNPSNPVGSWLTADQLARVLDATPPETLIVVDEAYAEYAAGDDYP
SALTLLKARGLPWIVLRTFSKAYGLAGLRVGYGLVSDPELVGLLDRVRTPFNVNGAAQAAALAALDDEEH
LAKGVALALAERERLKKELAEMGYRIAPSRANFLFFDARRPASAVAEALLRQGVIVKPWKQPGFETFIRV
SIGSPEENDHFVAALDKVLEA
>gnl|CDD|235356 PRK05170, PRK05170, YcgN family cysteine cluster protein
MLDPPFWQTKTLDEMSDAEWESLCDGCGKCCLHKLEDEDTGEIYYTNVACRLLDIKTCQCSDYENRFEFV
PDCVKLTPENLPEFEWLPPTCAYRLLAEGKDLPSWHPLITGSKEAVHKAGISVRGRVVSESEVDDWEDHI
VNWPLWA
>gnl|CDD|179953 PRK05174, PRK05174, bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase
MMTKQSSYTKEDLLACGRGELFGPGNAQLPAPPMLMMDRITEISETGGEFGKGYIVAELDINPDLWFFGC
HFIGDPVMPGCLGLDAMWQLVGFYLGWLGGPGKGRALGVGEVKFTGQVLPTAKKVTYEIDIKRVINRKLV
MGIADGRVLVDGEEIYTAKDLKVGLFKDTSAF
>gnl|CDD|235358 PRK05179, rpsM, 30S ribosomal protein S13; Validated
MARIAGVDIPRNKRVVIALTYIYGIGRTRAKEILAAAGIDPDTRVKDLTDEELDKIREEIDKNYKVEGDL
RREVSMNIKRLMDIGCYRGLRHRRGLPVRGQRTKTNARTRKGPRKTIAGKKK
>gnl|CDD|235359 PRK05182, PRK05182, DNA-directed RNA polymerase subunit alpha; Provisional
TEFLKPQKIEVEEESEDDNYGKFVLEPLERGFGTTLGNALRRVLLSSLPGAAVTSVKIDGVLHEFSTIPG
VREDVTEIILNLKGLRLKLHGDEPVTLTLSKKGPGEVTAGDIETDGDVEIVNPDLVIATLNEGAKLEMEL
TVERGRGYVPAEENKEDAPIGRIPVDAIFSPVKKVNYTVENTRVGQRTDYDKLILEVETDGSITPEEALA
LAAKILVEQLSVFVDLEEAEEAEEEVEEEEPEFDPILLRPIEELELSVRSYNCLKRAGINTIGDLVQRTE
EELLKTRNLGKKSLEEIKEKLAELGLSLGM
>gnl|CDD|235360 PRK05183, hscA, chaperone protein HscA; Provisional
MALLQISEPGQSAAPHQRRLAVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEA
RANAAQDPKNTISSVKRFMGRSLADIQQRYPHLPYQFVASENGMPLIRTAQGLKSPVEVSAEILKALRQR
AEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGG
GTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQAGLSPRLDPEDQRLLLDAARAAKEALSD
ADSVEVSVALWQGEITREQFNALIAPLVKRTLLACRRALRDAGVEADEVKEVVMVGGSTRVPLVREAVGE
FFGRTPLTSIDPDKVVAIGAAIQADILAGNKPDSDMLLLDVIPLSLGLETMGGLVEKIIPRNTTIPVARA
QEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLSVTAMEKST
GVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLSAAERA
AIDAAMAALREVAQGDDADAIEAAIKALDKATQEFAARRMDRSIRRALAGHSVDEI
>gnl|CDD|235361 PRK05184, PRK05184, pyrroloquinoline quinone biosynthesis protein PqqB; Provisional
MRIIVLGSAAGGGFPQWNCNCPNCRGARAGTIRAKPRTQSSIAVSADGEDWVLLNASPDIRQQIQATPAL
QPARGLRDTPIAAVVLTDGQIDHTTGLLTLREGQPFPVYATPAVLEDLSTGFPIFNVLDHYGGVQRRPIA
LDGPFAVPGLPGLRFTAFPVPSKAPPYSPHRSDPEPGDNIGLRIEDRATGKRLFYAPGLAEVTDALRARL
AGADCVLFDGTLWTDDEMIRAGVGTKTGRRMGHLPQSGPGGMIAALARLPIARKILIHINNTNPILDEDS
PERAELEAAGIEVAHDGMEIEL
>gnl|CDD|179959 PRK05185, rplT, 50S ribosomal protein L20; Provisional
ARVKRGVVARARRKKILKLAKGYRGARSRLYRVAKQAVMKALQYAYRDRRQKKRDFRKLWIARINAAARQ
NGLSYSRFINGLKKAGIEIDRKVLADLAVNDPAAFAALVEKAKA
>gnl|CDD|235363 PRK05198, PRK05198, 2-dehydro-3-deoxyphosphooctonate aldolase; Provisional
GDIEVGNDLPFFLIAGPCVIESRDLALRIAEHLKEITDKLGIPYVFKASFDKANRSSIHSFRGPGLEEGL
KILQEVKETFGVPVLTDVHEPEQAAPVAEVVDVLQIPAFLCRQTDLLVAAAKTGKVVNIKKGQFLAPWDM
KNVVDKVREAGNDKIILCERGTSFGYNNLVVDMRGLPIMRETGAPVIFDATHSVQLPGGQGGSSGGQREF
VPVLARAAVAVGVAGLFIETHPDPDNALSDGPNMLPLDKLEPLLEQLKAIDDLV
>gnl|CDD|235364 PRK05201, hslU, ATP-dependent protease ATPase subunit HslU
MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRL
AKLANAPFIKVEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAK
NNWGEEEEKEEISATRQKFRKKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKK
KKKRKLKVKEARKILIEEEAAKLIDMEEIKQEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRD
LLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSDLIPELQGRFPIRVELDALTEEDFVRILTEPKAS
LIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHTVMEKLLEDISFEAPDMSGETVTI
DAAYVDEKLGDLVKDEDLSRYIL
>gnl|CDD|235365 PRK05205, PRK05205, bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR
MMKKEILDAEALRRALTRIAHEIIERNKGLDNLVLVGIKTRGVWLAERLAERLEQLEGVDVPVGELDITL
YRDDLTKKGLHPQVKPTDIPFDIEGKRVILVDDVLYTGRTIRAALDALFDYGRPARVQLAVLVDRGHREL
PIRADYVGKNIPTSRDERVVVRLAEVDGRDRVVLER
>gnl|CDD|235366 PRK05218, PRK05218, heat shock protein 90; Provisional
MAMETGEFQAEVKQLLHLMIHSLYSNKEIFLRELISNASDAIDKLRFEALTDPALYEGDGDLKIRISFDK
EARTLTISDNGIGMTREEVIENLGTIAKSGTKEFLEKLKGDQKKDSQLIGQFGVGFYSAFMVADKVTVIT
RSAGPAAEAVRWESDGEGEYTIEEIEKEERGTEITLHLKEDEDEFLDEWRIRSIIKKYSDFIPVPIKLEK
EEEETINSASALWTRSKSEITDEEYKEFYKHLAHDFDDPLFWIHNNVEGPFEYTGLLYIPKKAPFDLFNR
DRKGGLKLYVKRVFIMDDAEELLPEYLRFVKGVIDSEDLPLNVSREILQEDRVVKKIRKAITKKVLDELE
KLAKNDREKYEKFWKEFGPVLKEGLYEDFANREKLAKLLRFASTHEGKYVSLAEYVERMKEGQKKIYYIT
GDSREAAKNSPHLELFKKKGIEVLLLTDPIDEFWISYLEEFDGKPFKSVARGDLDLGKEDEEEKEEKEEA
EEEFKPLLERLKEALGDKVKDVRLSHRLTDSPACLVADEGDMSTQMEKLLKAAGQEVPESKPILEINPNH
PLVKKLADEADEAKFKDLAELLYDQALLAEGGSLEDPAAFVKRLNELLLKLLA
>gnl|CDD|235367 PRK05222, PRK05222, 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
MIKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVL
DTAVLLGAIPERFGNLGGSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFDPDTQFKLTSNKLLD
EFEEAKALGINTKPVLLGPVTFLWLSKSKGEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVL
DLPQEWLEAFKRAYEALAAAKPRPKLLLATYFGSLNDALDLLASLPVDGLHLDLVRGPEQLAALLKYFPA
DKVLSAGVIDGRNIWRADLEAALALLEPLAAKVDRLWVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQ
KLEELALLARALNGGRGAVAEALAANRAAIAARRTSPRVHNPAVRARLAALTEADFQRQSPYAERAAAQR
ARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRLQEELGLDVLVHGEFERN
DMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGMLTGPVTI
LNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRLA
TSGVKDETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFEDFGYPNEIGPGVYDIHSPRV
PSVEEIEELLRKALEVIPAERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAELAA
>gnl|CDD|235368 PRK05225, PRK05225, ketol-acid reductoisomerase; Validated
ANYFNTLNLRQQLAQLGKCRFMDRDEFADGASYLKGKKIVIVGCGAQGLNQGLNMRDSGLDISYALRKEA
IAEKRASWRKATENGFKVGTYEELIPQADLVINLTPDKQHSDVVRAVQPLMKQGAALGYSHGFNIVEVGE
QIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFV
AEVKSDLMGEQTILCGMLQAGSLLCFDKLVAEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPA
KIRAFELSEQLKEIMAPLFQKHMDDIISGEFSSTMMADWANDDKKLLTWREETGKTAFENAPQYEGKISE
QEYFDKGVLMVAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGN
YLFSHAAVPLLKDFMATLQPGDLGKGLPSNAVDNAQLRDVNEAIRNHPIEQVGKKLRGYMTDMKRIA
>gnl|CDD|235369 PRK05231, PRK05231, homoserine kinase; Provisional
MAVYTDVSDDELAAFLAPYDLGELLSLKGIAEGIENSNFFLTTTQGEYVLTLFERLTAEDLPFFLGLMQH
LAARGVPVPAPVARRDGAALGELAGKPAAIVTFLEGKWPRAPTAAHCAEVGEMLARMHLAGRDFPLERPN
LRGLAWWRELAPRLLPFLADEQAALLEAELAAQLAFLASAAWPALPRGVIHADLFRDNVLFEGDRLSGFI
DFYFACNDKLLYDVAITLNDWCFEADGSLDATKARALLAAYQSVRPLTAAERAALPVMLRGAALRFWLSR
LYDWLLPRAGALVKPKDPLEFERKLRFRRAVVSALPYGL
>gnl|CDD|179969 PRK05234, mgsA, methylglyoxal synthase; Validated
MPARKRIALIAHDHKKDDLVAWVKAHKDLLEQHELYATGTTGGLIQEATGLDVTRLLSGPLGGDQQIGAL
IAEGKIDMLIFFRDPLTAQPHDPDVKALLRLADVWNIPVATNRATADFLISSLLFDDEVEILIPDYQRYL
AE
>gnl|CDD|235370 PRK05244, PRK05244, Der GTPase-activating protein YihI
KKKKSSPKRSKGMAKSKKKTREELDAEARERKRKKKHKGLKSGSRHNEGNTQSKGKGQAQKKDPRIGSKK
PIPLGVEEKVKPKKKKPKSKKPKLSPEQELEKLENDERLNALLDRLEAGETLSAEDQKWVDEKLDRIDEL
MEKLGISDDDDEEESEEEESDDDLLRLFEGGNIKDFK
>gnl|CDD|235371 PRK05246, PRK05246, glutathione synthetase; Provisional
MMKVAFQMDPIESINIKKDSTFAMMLEAQRRGHELFYYEPDDLSLRGGEVVARARPLTVRDDKGDWYELG
EEQRLPLADFDVILMRKDPPFDMEYIYATYLLERAERPGTLVVNKPQSLRDANEKLFTLWFPELMPPTLV
TRDKAEIRAFRAEHGDIILKPLDGMGGAGIFRVKADDPNLGSILETLTEHGREPVMAQRYLPEIKEGDKR
ILLVDGEPVGYALARIPAGGETRGNLAAGGRGEATPLTERDREICAAIGPELKERGLIFVGIDVIGDYLT
EINVTSPTGIREIERLTGVDIAGMLWDAIEAKLAAK
>gnl|CDD|235372 PRK05248, PRK05248, hypothetical protein; Provisional
MDYEFLRDLTGEVKARFSMGHEAIGRWFNEEVGKNLAKLDEVLAAAAAVKGSEREWQLAGHEYTLWLDGE
EVMVRANQLDFEEEDELEEGMSYYDEESLAFCGLEDFEQVLQSWRAFVQQK
>gnl|CDD|235373 PRK05249, PRK05249, Si-specific NAD(P)(+) transhydrogenase
MHMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKALREAVLRLIGFNQNPL
YSSYRVKLRITFADLLARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADK
IVIATGSRPYRPPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRL
LSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGVIVHLKSGKKIKADCLLYANGRTGNTDGLNLE
NAGLEADSRGQLKVNENYQTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAVGEATAHLIEDIPTGIYT
IPEISSVGKTEQELTAAKVPYEVGRARFKELARAQIAGDNVGMLKILFHRETLEILGVHCFGERATEIIH
IGQAIMEQKGTIEYFVNTTFNYPTMAEAYRVAALDGLNRLF
>gnl|CDD|235375 PRK05253, PRK05253, sulfate adenylyltransferase subunit CysD
MDQYRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFP
EMIEFRDRRAKELGLELIVHSNPEGIARGINPFRHGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEE
KSRAKERIFSFRDEFGQWDPKNQRPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYF
AHERPVVERDGMLIMVDDRMPLRPGEVVEERMVRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERG
GRAIDDDQEASMEKRKREGYF
>gnl|CDD|235376 PRK05254, PRK05254, uracil-DNA glycosylase; Provisional
PMKMLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYH
GPGQAHGLSFSVPPGVPIPPSLRNIFKELEDDLGFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAG
KGWETFTDAVIKALNERREPVVFILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANA
LLKQHGKTPIDWQL
>gnl|CDD|235377 PRK05255, PRK05255, ribosome-associated protein
DVPMRDPEEEDDEIIWVSKSQIKRDAEALQDLGEELVELSKDQLAKLPLDEDLRDAILEAQRITSHEARR
RQLQYIGKLMRNEDVEPIRAALDKLKNKHNQETARFHKLERWRDRLLAEGDDALTEFLEEYPDADRQQLR
QLIRNAKKEKAQNKPPKSFRELFQYLRELIE
>gnl|CDD|235378 PRK05256, PRK05256, chromosome partition protein MukE
MSSTNIEDVMPVKLAQAIANPLFPALDSQLRSGRHIGLDELDNHAFLMDFQEELEEFYRRYNVELIRAPE
GFFYLRPRSTTLIPRSVLSELDMLVGKILCYLYLSPERLAHEGIFTQQELYDELLTLADEAKLLKLVNNR
STGSDLDKQKLQEKVRTSLNRLRRLGMVWFMGHDSSKFRITESVFRFGADVRSGDDPREAQLRLIRDGEA
MPIENHLQQESSLNDETEEEQPDEEEEE
>gnl|CDD|179979 PRK05257, PRK05257, malate:quinone oxidoreductase; Validated
SEESKTDVVLIGGGIMSATLGTLLKELEPEWSITMFERLDGVALESSNGWNNAGTGHSALCELNYTPEKA
DGSIDISKAVKINEQFQISRQFWAYLVEKGVLPDPRSFINPVPHMSFVWGEDNVAFLKKRYEALKANPLF
AGMEFSEDPAQIKEWAPLMMEGRDPSQKVAATRIEIGTDVNFGALTRQLVGYLQKQGNFELQLGHEVRDI
KRNDDGSWTVTVKDLKTGEKRTVRAKFVFIGAGGGALPLLQKSGIPEAKGYGGFPVSGQFLVCENPEVVA
QHHAKVYGKASVGAPPMSVPHLDTRVIDGKRSLLFGPFAGFSTKFLKNGSLLDLFSSVRPSNLLPMLAVG
LDNFDLTKYLISQVMLSDEDRFEALREFYPNAKPEDWELIVAGQRVQIIKKDPKKGGVLQFGTEVVSSAD
GSIAALLGASPGASTAVPIMLEVLEKCFPDRMASPEWQPKLKEMIPSYGQKLNDNPALLEEIRAYTSEVL
GLDY
>gnl|CDD|179980 PRK05260, PRK05260, chromosome partition protein MukF
MSEFSQTVPELVAWARKNDFSLSLPTERLAFLLAIATLNGERLDGEMSEGELVDAFRHVSDAFEQTSETI
TVRANNAINDLVRQRLLNRFTSEQAEGNAIYRLTPLGIGITDYYIRQREFSTLRLSMQLSIVAGELKRAA
DAAEEGGDEFHWRRNVFAPLKYSVAEIFDSIDLTQRLMDEQQQQVKDDIAQLLNKDWRAAISSCELLLSE
TSGTLRELQDTLEAAGDKLQANLLRIQDATMGRDDLDFVDRLVFDLQSKLDRIISWGQQAIDLWIGYDRH
VHKFIRTAIDMDKNRVFSQRLRQSVQTYFDHPWALTYANADRLLDLRDEELALRDEEVTGELPAELEYEE
FNEIREQLAALIEEALAVYKEQQGPLDLGLVLREYLAQYPRARHFDVARIVVDQAVRLGVAEADFTGLPA
KWQPINDYGAKVQAHVIDKY
>gnl|CDD|235379 PRK05261, PRK05261, phosphoketolase
TAPLSSEELELLDAYWRAANYLSVGQIYLRDNPLLREPLKPEHVKPRLLGHWGTTPGLNFIYAHLNRLIR
KYDLNMIYITGPGHGGPAMVANAYLEGTYSEIYPEITQDEEGMARLFKQFSFPGGIPSHAAPETPGSIHE
GGELGYSLSHAYGAAFDNPDLIVACVVGDGEAETGPLATSWHSNKFLNPATDGAVLPILHLNGYKIANPT
ILARISDEELEALFRGYGYEPYFVEGDDPADMHQEMAAALDTAIEEIRAIQKEAREGGDTTRPRWPMIVL
RTPKGWTGPKEVDGKPIEGSWRAHQVPLANVRDNPEHLDLLEDWLRSYRPEELFDEDGRLKPELAALAPK
GDRRMGANPHANGGLLLRDLRLPDFRDYAVPVGKPGAVMAEATRVLGKYLRDVIKLNPDNFRIFGPDETA
SNRLQAVFEVTDRQWMAEILPYDEHLAPDGRVMEVLSEHLCEGWLEGYLLTGRHGFFSSYEAFIHIVDSM
FNQHAKWLKVAREIPWRKPIPSLNYLLTSHVWRQDHNGFSHQDPGFIDHVANKKPDVIRVYLPPDANTLL
AVADHCLRSRNYINVIVAGKQPRPQWLSMDEARKHCTKGLGIWDWASNDDGEEPDVVLACAGDVPTLETL
AAADLLREHFPDLKIRVVNVVDLMKLQPPSEHPHGLSDREFDALFTTDKPVIFAFHGYPWLIHRLTYRRT
NHHNFHVRGYKEEGTTTTPFDMVVLNELDRFHLAIDAIDRVPILGTKAAALIQRMRDKLIEHRAYIREHG
EDMPEIRDWKWPGLK
>gnl|CDD|179982 PRK05264, PRK05264, met regulon transcriptional regulator MetJ
MAEWNGEYISPYAEHGKKSEQVKKITVSIPLKVLKILTDERTRRQVNNLRHATNSELLCEAFLHAFTGQP
LPDDEDLRKERSDEIPEAAKEIMREMGIDPETWEY
>gnl|CDD|235380 PRK05265, PRK05265, pyridoxine 5'-phosphate synthase; Provisional
MMIRLGVNIDHIATLRNARGTNYPDPVRAALIAEQAGADGITVHLREDRRHIRDRDVRLLRETLKTELNL
EMAATEEMLDIALEVKPHQVTLVPEKREELTTEGGLDVAGQFDKLKPAIARLKDAGIRVSLFIDPDPEQI
EAAAEVGADRIELHTGPYADAKTEAEAAELERIAKAAKLAASLGLGVNAGHGLNYHNVKPIAAIPGIEEL
NIGHAIIARALFVGLEEAVREMKRLMDEA
>gnl|CDD|235381 PRK05269, PRK05269, transaldolase B; Provisional
MTNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQI
DDAIDKLAVNFGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGI
RAAEQLEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRILDWYKKNTGKKEYAPAEDPGVVSVTKIY
NYYKKHGYKTVVMGASFRNTGQILELAGCDRLTISPALLEELAASEGELERKLSPPGEAKARPVPLTEAE
FRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIAAKLA
>gnl|CDD|235382 PRK05270, PRK05270, UDP-glucose--hexose-1-phosphate uridylyltransferase
MTISQLIEKLIDYAIQNGLIEELDRIYLRNRLLALLGEDSYEEVDEDEDLESPIDLLDQLVDYAVENGLI
EDTQTERDILDAQLMDLLTPRPSEVNRRFWEKYQKSPEAATDYFYQLSKANNYIKTDAIAKNISWKVPTK
YGDLEITINLSKPEKDPKAIAAAKKAKASSYPKCLLCMENEGYAGRLNHPARSNHRIIRLTLGGESWGFQ
YSPYAYFNEHCIVLSEKHRPMKISRKTFERLLDFVEQFPHYFIGSNADLPIVGGSILSHDHYQGGRHTFP
MAKAPIEEEFTLAGYPDVKAGIVKWPMSVIRLTSKNKDELIDAADKILEAWRGYSDESVDILAYTDGTPH
NTITPIARRRGGKYELDLVLRNNRTSEEHPDGIFHPHPEVHHIKKENIGLIEVMGLAILPGRLKEELEEV
EKYLLGEANEVAAKHQEWAEQLKAKYGITTKENVEAIVQEEVGSVFARVLEDAGVFKRTEEGQAAFDRFI
ESL
>gnl|CDD|235384 PRK05274, PRK05274, 2-keto-3-deoxygluconate permease; Provisional
MQMKIKRTIEKIPGGMMLVPLLLGALINTFAPGALYFGSFTNALFKTGAVPILAVFLFCMGASINLRATG
TVLKKGGTLLLTKFAVAALVGVIAGKFIGEEGIRLGGFAGLSTLAIIAAMDNTNGGLYAALMGQYGTKED
AGAFVLMSLEDGPFMTMLALGAAGLASFPPPALVGAVLPLLVGFILGNLDPELRQFLGKAVPVLIPFFAF
ALGNGIDLGTIITAGLSGILLGVAVVAVTGIPLYLADRLIGGGNGVAGAAAGSTAGNAVATPAAVAAADP
SFAPFAPAATAQVAAAVIVTAILAPILTAWWSKRVGKRAAETETPE
>gnl|CDD|235385 PRK05277, PRK05277, H(+)/Cl(-) exchange transporter ClcA
LFMAAVVGTLTGLVGVAFELAVDWVQNQRLGLLASVADNGLLLWIVAFLISAVLAMIGYFLVRRFAPEAG
GSGIPEIEGALEGLRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMVLDIFRLRSDEARH
TLLAAGAAAGLAAAFNAPLAGILFVIEEMRPQFRYSLISIKAVFIGVIMATIVFRLFNGEQAVIEVGKFS
APPLNTLWLFLLLGIIFGIFGVLFNKLLLRTQDLFDRLHGGNKKRWVLMGGAVGGLCGLLGLLAPAAVGG
GFNLIPIALAGNFSIGMLLFIFVARFITTLLCFGSGAPGGIFAPMLALGTLLGLAFGMVAAALFPQYHIE
PGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLILPLIITCLGATLLAQFLGGKPIYSALLERTLAK
QEAEQAARSKAAPASENT
>gnl|CDD|235386 PRK05279, PRK05279, N-acetylglutamate synthase; Validated
MMKERSTEFVDWFRHSAPYINAHRGKTFVIMLGGEAIAHGNFSNIVHDIALLHSLGIRLVLVHGARPQIE
EQLAARGIEPRYHKGLRVTDAAALECVKQAAGELRLDIEARLSMGLPNTPMAGAHIRVVSGNFVTARPLG
VDDGVDYQHTGEVRRIDAEAIRRQLDSGAIVLLSPLGYSPTGESFNLTMEEVATQVAIALKADKLIFFTE
SQGVLDEDGELIRELSPNEAQALLEALEDGDYNSGTARFLRAAVKACRGGVRRSHLISYAEDGALLQELF
TRDGIGTMIVMESLEQLRRATIDDVGGILELIRPLEEQGILVRRSREQLEREIDKFTVIERDGLIIGCAA
LYPFPEEKMGEMACLAVHPDYRGSGRGERLLKRIEQRARQLGLKRLFVLTTRTAHWFLERGFVPVDVDDL
PEAKRQLYNYQRRSKVLVKDL
>gnl|CDD|179990 PRK05282, PRK05282, dipeptidase PepE
MELLLLSNSTLPGTGYLEHALPLIAELLAGRRKAVFIPYAGVTQSWDDYTAKVAEALAPLGIEVTGIHRV
ADPVAAIENAEAIFVGGGNTFQLLKQLYERGLLAPIREAVKNGTPYIGWSAGANVAGPTIRTTNDMPIVD
PPSFDALGLFPFQINPHYTNALPEGHNGETREQRIREFLVVNPELPVVGLPEGSWLRVSGGHATLGGPNP
AYVFKAGEEAVELEAGSDFSFLL
>gnl|CDD|235388 PRK05286, PRK05286, quinone-dependent dihydroorotate dehydrogenase
MYYPLARPLLFKLDPETAHELTIRALKRASRTPLLSLLRQRLTYTDPRLPVTVMGLTFPNPVGLAAGFDK
NGEAIDALGALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPL
GINIGKNKDTPLEDAVDDYLICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELHG
YVPLLVKIAPDLSDEELDDIADLALEHGIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIR
RLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQIYSGLIYEGPGLVKEIVRGLARLLRRDG
>gnl|CDD|235389 PRK05287, PRK05287, cell division protein ZapD
MMTMILYEYPLNEKIRTYLRLEFLFQQLTFNLAQDDPADHHVAFRTLFELLDVLERGDLKSDLLKELERQ
RQKLQKWRGNPGVDQEALEALLQELEQASAALNAAPRIGQSLREDRFLSSIRQRLSIPGGCCSFDLPALH
AWLHLPQEQRQQDLQQWLAPLAPLRDALTLVLRLLRESGQFRKQTALNGFYQQNLEGRDAQLLRLRLDLE
LGLYPEISGHKYRFAIRFMPLDSEPGQVDEDIEFELACCS
>gnl|CDD|235390 PRK05289, PRK05289, acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase
MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQ
DLKYKGEPTRLVIGDNNTIREFVTINRGTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAG
HVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIH
ALRRAYKLLYRSGLTLEEALEELAEEYPDSPEVKEILDFIESSKRGIIRPRG
>gnl|CDD|235391 PRK05290, PRK05290, hybrid cluster protein; Provisional
MFCYQCEQTARGNGCTAQGVCGKTAETADLQDLLIYALKGLSAYALKARELGIIDHEVDRFVPEALFTTL
TNVNFDDERIVGYIKEAIALREALKAKLAADGNAPEDLPDAALWLPADDLEELLAQAAEVGVLADATENE
DIRSLRELLLYGLKGMAAYAEHARVLGQTDEEIYAFYHKALAALGDDPLDVDELLALVLECGKMNVKVMA
LLDKANTETYGHPEPTKVNIGVRKGPGILVSGHDLKDLEELLEQTEGTGINVYTHGEMLPAHGYPELKKY
PHLVGNYGSAWQNQQKEFASFPGPILMTTNCIIPPKGSYKDRIFTTGIVGWPGVKHIEGDGKKDFSPVIE
KALELPGFPPDEIEHEITVGFAHNAVLAVADKVIDAVKSGAIRHFFLMGGCDGAKPGRNYYTEFAEKLPK
DTVILTLGCGKYRFNKLDLGDIGGIPRLLDAGQCNDAYSAIVIALALAEAFGCDVNDLPLSLVLSWYEQK
AVAVLLTLLSLGVKNIRLGPTLPAFLSPNVLKVLVEKFGIRPITTVEEDLKAILGA
>gnl|CDD|235392 PRK05291, trmE, tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE
MMMNDTIAAIATPPGRGGIGIIRISGPDALEIAQKLFGKKLPKPRTAHYGHIRDPGEVIDEVLVLYFPAP
NSFTGEDVVEIQCHGGPAVLNLILELLLALGARLAEPGEFTKRAFLNGKLDLTQAEAIADLIDAKTEAAA
RLALRQLQGALSKLINELREELLELLALVEAAIDFPEEDIEFLSDEKILEKLEELIAELEALLASARQGE
ILREGLKVVIAGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIEEHINLDGIPLRLIDTAGIRETDDEV
EKIGIERSREAIEEADLVLLVLDASEPLTEEDDEILEELKDKPVIVVLNKADLTGEIDLEEENGKPVIRI
SAKTGEGIDELREAIKELAFGGFGGNQEGVFLTNARHLEALERALEHLERALEGLESGLPLELLAEDLRL
ALEALGEITGEVTSEDLLDRIFSSFCIGK
>gnl|CDD|179997 PRK05293, glgC, glucose-1-phosphate adenylyltransferase; Provisional
KKEMLAMILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHIGI
GSPWDLDRINGGVTILPPYSESEGGKWYKGTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYH
KEKEADVTIAVIEVPWEEASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLKEYLIEDEKN
PNSSHDFGKNVIPLYLEEGEKLYAYPFKGYWKDVGTIESLWEANMELLRPENPLNLFDRNWRIYSVNPNL
PPQYIAENAKVKNSLVVEGCVVYGTVEHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAV
IGDGVIIGGGKEVITVIGENEVIGVGTVIG
>gnl|CDD|235393 PRK05294, carB, carbamoyl-phosphate synthase large subunit
MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPIT
PEFVEKIIEKERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIG
LPVPRSGIAHSMEEALEVAEEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESL
LGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETG
GCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLAVGYTLDEIKNDITGKTPASFEPS
LDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTGLDEDLFEEESLEE
LREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLREAKR
LGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVL
GSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKP
KGVIVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVA
EEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLI
GGIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPR
ASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTG
EVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFLSVRDRDKEEVVELAKRLLELGFKILATSGTAKFLREAG
IPVELVNKVHEGRPHIVDLIKNGEIDLVINTPTGRQAIRDGFSIRRAALEYKVPYITTLAGARAAVKAIE
ALKFGELEVRSLQEYH
>gnl|CDD|235394 PRK05297, PRK05297, phosphoribosylformylglycinamidine synthase; Provisional
MLILRGSPALSAFRLQKLLARLQAAVLPVTSIYAEYVHFADLSAPLSAEEQAKLERLLTYGPAEHEPAGR
LFLVTPRPGTISPWSSKATDIAHNCGLAGIRRIERGIAYYVEAALSAEQRAALAALLHDRMTESVFADLD
DAEALFSHHEPKPLTSVDVLGGGRAALEAANVELGLALAEDEIDYLVEAFTKLGRNPTDVELMMFAQANS
EHCRHKIFNADWTIDGEEQPKSLFKMIKNTHETNPDGVLSAYKDNAAVMEGSKVGRFFPDPDTGRYGYHQ
EPAHILMKVETHNHPTAISPFPGAATGSGGEIRDEGATGRGSKPKAGLTGFSVSNLRIPGFEQPWEEDYG
KPERIASALDIMIEGPLGGAAFNNEFGRPNLLGYFRTFEQKVNSHNEEVRGYHKPIMLAGGIGNIRADHV
QKGEIPVGAKLIVLGGPAMRIGLGGGAASSMASGQSSEDLDFASVQRGNPEMERRCQEVIDRCWQLGDDN
PILSIHDVGAGGLSNAFPELVNDGGRGGRFDLRKIPNDEPGMSPLEIWCNESQERYVLAIAPEDLELFEA
ICERERCPFAVVGEATEERHLTLEDSHFDNKPVDLPLDVLLGKPPKMHRDVKTVKAKGPALDYSGIDLAE
AVERVLRLPTVASKSFLITIGDRSVTGLVARDQMVGPWQVPVADCAVTAASYDGYAGEAMAMGERTPVAL
LDAAASARMAVGEALTNIAAAPIGDLKRIKLSANWMAAAGHPGEDARLYDAVKAVGMELCPALGITIPVG
KDSLSMKTKWQEGGEDKEVTSPLSLIISAFAPVEDVRKTLTPQLRTDKDTALLLIDLGRGKNRLGGSALA
QVYNQLGDKAPDVDDAEDLKGFFNAIQALVAEGLLLAYHDRSDGGLLTTLAEMAFAGHCGLDIDLDALGD
DALAALFNEELGAVIQVRAADRDAVEAILAEHGLSDCVHVIGKPNAGDRIVITRNGKTVFSESRTELRRW
WSETSYQMQRLRDNPECADQEFDAILDQADPGLNVKLTFDPNEDIAAPFIATGARPKVAILREQGVNSHV
EMAAAFDRAGFDAIDVHMSDLLAGRVTLEDFKGLVACGGFSYGDVLGAGEGWAKSILFNPRLRDQFEAFF
ARPDTFALGVCNGCQMMSNLKEIIPGAEHWPRFVRNRSEQFEARFSLVEVQESPSIFLQGMAGSRLPIAV
AHGEGRAEFPDAHLAALEAKGLVALRYVDNHGQVTETYPANPNGSPNGITGLTTADGRVTIMMPHPERVF
RTVQNSWHPEEWGEDSPWMRMFRNARKWVG
>gnl|CDD|235395 PRK05298, PRK05298, excinuclease ABC subunit UvrB
MMKPFKLVSPYKPAGDQPQAIEELVEGIEAGEKHQTLLGVTGSGKTFTMANVIARLQRPTLVLAHNKTLA
AQLYSEFKEFFPENAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINEEIERLRHSATKSLLERRDVIVVA
SVSCIYGLGSPEEYLKMVLSLRVGQEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFPAYYEER
AIRIEFFGDEIERISEFDPLTGEVLGELDRVTIYPASHYVTPRERLERAIESIKEELEERLKELEKEGKL
LEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPYTLLDYFPDDFLLFIDESHVTVPQIGGM
YNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEAKVPQTIYVSATPGDYELEKSGGVVVEQIIRPTGLLD
PEIEVRPTKGQVDDLLSEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTLERVEIIR
DLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDS
MQKAIDETERRREIQIAYNEEHGITPKTIKKKIRDILDSVYKKDKLSKKELEKLIKELEKQMKEAAKNLE
FEEAARLRDEIKELKEELLGLS
>gnl|CDD|235396 PRK05299, rpsB, 30S ribosomal protein S2; Provisional
MAVVSMKQLLEAGVHFGHQTRRWNPKMKPYIFGERNGIHIIDLQKTVPMLDEAYNFVRDVAANGGKILFV
GTKKQAQEAIAEEAERCGMPYVNHRWLGGMLTNFKTIRKSIKRLKELEKMEEDGTFEKLTKKEALMLTRE
LEKLEKSLGGIKDMGGLPDALFVVDPNKEHIAVKEARKLGIPVVAIVDTNCDPDGVDYPIPGNDDAIRSI
KLYTSKIADAILEGRQGRLAEAAEEEEEEAEEEEEEEEEEEAEEAEAE
>gnl|CDD|235398 PRK05302, PRK05302, 30S ribosomal protein S7; Validated
MPRRRRAPKREVLPDPKYGSVLVTKFINKLMLDGKKSVAEKIVYGALDIIEEKTGKDPLEVFEKALENVK
PVVEVKSRRVGGATYQVPVEVRPERRQALAMRWLVEAARKRGEKTMAERLANELLDAANNRGAAVKKRED
THRMAEANKAFAHYRW
>gnl|CDD|235399 PRK05303, flgI, flagellar basal body P-ring protein FlgI
MKMLKLLLALLLLLLLLLAPAAAERIKDLASVQGVRDNQLIGYGLVVGLDGTGDQTTQTPFTTQSLANML
EQLGVNVPPGTNPKLKNVAAVMVTATLPPFARPGQRIDVTVSSIGDAKSLRGGTLLMTPLKGADGQVYAV
AQGNLVVGGFGASGDGSSVTVNVPTVGRIPNGAIVEREVPSDFGQGNSLTLNLRNPDFTTAQRIADAINR
LFGPGVATALDARTVQVRAPADPSQRVRFLARIENLEVEPDAPAKVVINERTGTIVMGQDVRVSPVAVSH
GNLTVTITEQPQVSQPNPFSGGQTVVTPQTQIDVEEEGGRLFVVPEGATLADLVRALNALGATPRDLIAI
LQALKAAGALHAELEVI
>gnl|CDD|235400 PRK05305, PRK05305, phosphatidylserine decarboxylase family protein
PIHREGYPFIAAAALVLLILGLLWWPLAWIGLLLTLFCLYFFRDPERVIPTDDGLVVSPADGKVVVIEEV
VPPYGDEPRLRISIFMSVFNVHVNRAPVSGTVTKVEYRPGKFLNAFLDKASEENERNAVVIETADGGEIG
VVQIAGLIARRIVCYVKEGDEVERGERFGLIRFGSRVDVYLPLGTEPLVSVGQKVVAGETVLARLP
>gnl|CDD|180007 PRK05309, PRK05309, 30S ribosomal protein S11; Validated
AKKKKTVKKKVKKNIPSGVAHIHATFNNTIVTITDRQGNVISWASAGGLGFKGSRKSTPYAAQVAAEDAA
KKAKEHGMKTVEVFVKGPGSGRESAIRALQAAGLEVTSIKDVTPIPHNGCRPPKRRRV
>gnl|CDD|235402 PRK05312, pdxA, 4-hydroxythreonine-4-phosphate dehydrogenase PdxA
MMMRPLALSLGDPAGIGPEIALKAWLRRRELGLPPFFLIGDPAVLAARARLLGLDVPVAEVTDPEEAAAV
FADALPVLPLPFPAPVVPGQPDPANAAGVIAAIERAVGLVLSGEAAAVVTAPIAKKVLYDAGFAFPGHTE
FLAELAGVATGKPVQPVMMLAGPQLRVVPVTIHIPLRDVPAALTPELIVATARITAADLRRRFGIASPRL
AVAGLNPHAGEGGALGREDIDIIAPAIEQLRAEGIDARGPLPADTMFHAAARATYDAAICMYHDQALIPI
KTLDFDGGVNVTLGLPFIRTSPDHGTAFDIAGKGIARPDSLIAALRLAAQMAANRA
>gnl|CDD|180009 PRK05313, PRK05313, hypothetical protein; Provisional
MMDPQEILETIEMIEEENLDIRTVTMGISLLDCIDPDLDRAAEKIYDKITTKAKNLVEVAEEIEREYGIP
IVNKRISVTPISLIAAATDAEDYVEIAKALDRAAKEVGVDFIGGFSALVQKGMTKGDRALIESIPEALAS
TERVCSSVNVGSTKAGINMDAVKLMGEIIKETAELTKDRDGIGCAKLVVFANAPEDNPFMAGAFHGVGEP
DAVINVGVSGPGVVKAALEKVKGADFDELAETIKKTAFKITRMGELVGREAAERLGVPFGIVDLSLAPTP
AVGDSVAEILEEMGLERVGAPGTTAALALLNDAVKKGGAMASSRVGGLSGAFIPVSEDAGMIEAVEAGAL
SLEKLEAMTAVCSVGLDMIAIPGDTPAETISAIIADEAAIGVINNKTTAVRIIPVPGKKVGDMVEFGGLL
GRAPVMPVNKFSSEDFIRRGGRIPAPIHSLKN
>gnl|CDD|235403 PRK05318, PRK05318, deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
MTSSVWQERRLGEDKQRRNDHRSPYQRDRARILHSAAFRRLQAKTQVLGVGENDFYRTRLTHSLEVAQIG
TGIVAQLKKEKQPELKPLLPSDSLIESLCLAHDIGHPPFGHGGEVALNYMMRDHGGFEGNGQTFRILTKL
EPYTEHFGMNLTRRTLLGILKYPALYSELVAQYPPPDVANHRQLKASDWKPPKGIFDDDQDIFDWVLEPL
SENDRALFQSLRPEPDSPKEHLKTRYKSLDCSIMELADDIAYGVHDLEDAIVLGLVTRSQWQEDVAPQLA
QCGDPWLEEEIETIGEKLFSGEHHLRKDAIGTLVNYFITSIRIKENEEFEEPLLRYNAALEPEFAAALEV
LKQFVYKYVIRKPEVQRLEYKGQQIVMELFEALSSDPERLLPRNTQERWRKAEDEENSMRVICDYISGMT
DEYAYRLYQQLF
>gnl|CDD|235405 PRK05320, PRK05320, rhodanese superfamily protein; Provisional
MQIVNIAAYKFVSLDDPETLRPLVLARCEALGLKGTILLAPEGINLFLAGTREAIDAFYAWLRADARFAD
LQVKESLSDSQPFRRMLVKLKREIITMKRPAIRPELGRAPSVDAATLKRWLDQGHDDAGRPVVMLDTRNA
FEVDVGTFDGALDYRIDKFTEFPEALAAHRADLAGKTVVSFCTGGIRCEKAAIHMQEVGIDNVYQLEGGI
LKYFEEVGGAHYDGDCFVFDYRTALDPQLAPLVDVTCFACRAVVTPE
>gnl|CDD|235406 PRK05321, PRK05321, nicotinate phosphoribosyltransferase; Provisional
HTWKADPIIRSLLDTDFYKLTMQQAVLHHYPDAQVEYEFICRNDEVDLAEYIDEIREQLDHLCTLRLTDD
ELDYLRGLPFFKPDFLDWLRLFRLNPYEVTVSIDDGQLDIRIEGPWLETILWEVPLLAIISELYFRARSP
EVLYAQAKRRLWEKIELLKALPDLSGFKIADFGTRRRFSFEWQEEVVEALKEGLPGAFVGTSNVHLAMKL
GLTPIGTMAHEWFMAHQALGPRLRDSQYAALEDWVREYRGDLGIALTDTIGMDAFLRDFDLYFAKLFDGL
RHDSGDPIEWGEKAIAHYEKLGIDPRTKTLVFSDGLDFDKALELYRHFKGRIKLSFGIGTNLTNDFPGVK
PLNIVIKLVECNGRPVAKLSDSPGKTMCDDPEFLRYLRQVFGLPLVVKAS
>gnl|CDD|235407 PRK05322, PRK05322, galactokinase; Provisional
MMKEELKKKFAEVFGEEAEDVFFSPGRINLIGEHTDYNGGHVFPAAITLGTYGAARKRDDKKVRLYSANF
EDLGIIEFDLDDLSFDKEDDWANYPKGVLKFLQEAGYKIDHGFDILIYGNIPNGAGLSSSASIELLTGVI
LKDLFNLDLDRLELVKLGQKTENEFIGVNSGIMDQFAIGMGKKDHAILLDCNTLEYEYVPLDLGDYVIVI
MNTNKRRELADSKYNERRAECEKALEELQKKLDIKSLGELTEEEFDEYSYLIKDETLLKRARHAVTENQR
TLKAVKALKAGDLEKFGRLMNASHVSLRDDYEVTGLELDTLVEAAWKQEGVLGARMTGAGFGGCAIAIVK
KDKVEAFKENVGKAYEEKIGYAASFYVAEIGDGAREL
>gnl|CDD|235408 PRK05324, PRK05324, succinylglutamate desuccinylase; Provisional
MLAMDDFLALTLAGHPPAVTEFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQL
VRDLLAGELPLRARLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSDEARRAAELEQAVEDFFAAG
AERVRWHYDLHTAIRGSKHEQFAVLPQRGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALA
CTLELGKVLPFGQNDLSRFAATDQALRALISGEELPERSADPPRLYRVVRQITKHSDDFELHFADDVENF
TAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIGLRAGLMLVPTTLD
>gnl|CDD|235409 PRK05325, PRK05325, hypothetical protein; Provisional
KSLVDRQRFLRRVKEQIKKALPDAISERSIIDSDGGEVVSIPIRDIDEPKFRYGRGGKREGVGPGNGEFV
VGDRIGRPQGGGGGGGQGGGDGEGEDYFEFEISLEELLDLLFEDLELPNLKKKGLKEIEEEKTRRAGYRR
TGPPSNLDKKRTLREALKRRIALGRPKRRELRELEEELEALEALEEIERLRALRAKIDRVPFIDPFDLRY
RNWEKVPKPESQAVMFCLMDVSGSMDEAEKDLAKRFFFLLYLFLRRKYENVEVVFIRHHTEAKEVDEEEF
FYSRESGGTIVSSAYKLALEIIEERYPPAEWNIYAFQASDGDNWSSDNPRCVELLREELLPVCNYFAYIE
VTPRAYRHQTLWREYERLQDTFPNFAMQRIRDKEDIYPVFRELFKKEAAEA
>gnl|CDD|235410 PRK05326, PRK05326, potassium/proton antiporter
MDTINSLLLIGALLLLLSILASRLSSRLGIPSLLLFLAIGMLAGEDGLGGIQFDNYPLAYLVGNLALAVI
LFDGGLRTRWSSFRPALGPALSLATLGVLITAGLTGLFAHWLLGLDWLEGLLLGAIVGSTDAAAVFSLLR
GKGLNLKERVASTLEIESGSNDPMAVFLTITLIELITGGETGLSWGFLLLFLQQFGLGALIGLLGGWLLV
QLLNRIALPAEGLYPILVLAGALLIFALTAALGGSGFLAVYLAGLVLGNRPIRHRHSILRFFDGLAWLAQ
IGMFLVLGLLVTPSRLLDIALPALLLALFLILVARPLAVFLSLLPFRFNLREKLFISWVGLRGAVPIVLA
TFPMMAGLPNAQLIFNVVFFVVLVSLLLQGTTLPWAARKLGVVVPPEARPVSRVELDPLEESDAELLEYR
VPAGSWLVGKALRDLRLPRGALIALIIRDGKLLVPTGSTRLKAGDVLLVLGPERDLPALERLFSQSPPGK
LDQRFFGDFILEGDAKLADLALIYGLELDQQTLGELIKQRLGGAPVVGDQVELGGIILTVAEGRVTKVGL
RL
>gnl|CDD|235411 PRK05327, rpsD, 30S ribosomal protein S4; Validated
MARYTGPKCKLSRRLGVDLFKSGKRCLKRKYPPGQHGQRRRKPKLSDYGLQLREKQKLRRIYGVLEKQFR
RYFKEAARRKGNTGENLLQLLESRLDNVVYRLGFAPTRRQARQLVSHGHILVNGKKVNIPSYRVKPGDVI
EVREKSKKLPRIKEALELAERRGVPDWLEVDAEKLEGTFKRLPEREEIPVPINEQLIVELYSK
>gnl|CDD|235412 PRK05329, PRK05329, glycerol-3-phosphate dehydrogenase subunit GlpB
MKFDVLVIGGGLAGLTAALAAAEAGKRVALVAKGQGALHFSSGSIDLLGYLPDGQPVSDPFEALAALAEQ
APEHPYSLVGADAVREALAQFQALLEAAGLPLVGSVERNHLRPTPLGTLRPTWLSPPSVPAGVALLDAKR
ILVVGIEGLRDFQPHLAAANLHAQFQGLEVRTAELELPGLDRDNPREFRAVNIARLLDDPENREALADAL
KPLAGDAEAVLLPAVLGLDDDAAVLAELEEALGCPVFELPTLPPSVPGLRLQNALRRAFERLGGRIMPGD
EVLGAEFEGGRVTAVWTRNHGDIPLRARHFVLATGSFFSGGLVAERDGIREPIFGLDVLQPADRADWYQR
DFFAPHPFLQFGVATDATLRPLDSQGGPVIENLYAAGAVLGGYDPIREGCGSGVALATALHAAEQIAEEA
GG
>gnl|CDD|235413 PRK05330, PRK05330, oxygen-dependent coproporphyrinogen oxidase
TMMEPDKARVKAWLLGLQDRICAALEALDGEARFVEDSWQRPEGGGGRSRVLENGRVFEKAGVNFSHVHG
EFLPPSATAHRPELAGRSFEATGVSLVAHPRNPYVPTVHMNVRFFIATKPGPVWWFGGGFDLTPYYPFEE
DAVHFHRTAKDACDPFGPEYYPRFKKWCDEYFYLKHRNEPRGVGGIFFDDLNSPGFERDFAFTQAVGDAF
LDAYLPIVERRKDTPYGEREREFQLYRRGRYVEFNLVYDRGTLFGLQTGGRTESILMSLPPLVRWEYDYQ
PEPGSPEARLSDFLKPRDWL
>gnl|CDD|235415 PRK05333, PRK05333, NAD-dependent protein deacetylase
APDADPAALDALQDFVERHPRLFVLTGAGISTDSGIPDYRDRNGQWKRSPPITYQAFMGSDAARRRYWAR
SMVGWPVFGRAQPNAAHHALARLGAAGRIERLVTQNVDGLHQRAGSRDVIELHGRLDGVRCMGCGARHPR
AEIQHVLEAANPEWLALEAAPAPDGDADLEWAAFDHFRVPACPACGGILKPDVVFFGENVPRERVAAARA
ALDAADAVLVVGSSLMVYSGYRFCVWAAQQGKPIAALNLGRTRADPLLTLKVEASCAQALAALVARLGLA
GRDAH
>gnl|CDD|235416 PRK05335, PRK05335, tRNA (uracil-5-)-methyltransferase Gid; Reviewed
MMKPVNVIGAGLAGSEAAWQLAKRGVPVELYEMRPVKKTPAHHTDGFAELVCSNSFRSDSLTNAVGLLKE
EMRRLGSLIMEAADAHRVPAGGALAVDREGFSEYVTEALENHPLITVIREEVTEIPEDITIIATGPLTSD
ALAEAIKALTGEDYLYFFDAAAPIVDKDSIDMDKVYLASRYDKGEADYLNCPMTKEEYEAFYEALIAAEK
AELKDFEKEKYFEGCMPIEVMAERGRETLRFGPMKPVGLTDPRTGKRPYAVVQLRQDNAAGTLYNIVGFQ
TKLKWGEQKRVFRMIPGLENAEFVRYGVMHRNTFINSPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAA
SGLLAGINAARLALGKEPVIPPPTTALGALLNYITGANPKHFQPMNANFGLFPPLGKRIRGEDKKERKEA
YAERALADLKEWLKEL
>gnl|CDD|235417 PRK05337, PRK05337, beta-hexosaminidase; Provisional
MGPLMLDVAGTELTAEERERLQHPLVGGVILFARNFEDPAQLRELTAAIRAAVRPPLLIAVDQEGGRVQR
FREGFTRLPAMQSFGALWDRDPLEALKLAEEAGWLMAAELRACGIDLSFAPVLDLDGISAVIGDRAFHRD
PQVVAALASAFIDGMHAAGMAATGKHFPGHGAVEADSHVETPVDERPLEEIRAEDMAPFRALIAAGLDAV
MPAHVIYPQVDPRPAGFSRYWLQDILRQELGFDGVIFSDDLSMEGAAVAGDYAERAQAALDAGCDMVLVC
NNRDGAVSVLDNLSPPISAERLTRLYGRGAFSWQELMASPRWKAAQAALAQLHERWQ
>gnl|CDD|235418 PRK05338, rplS, 50S ribosomal protein L19; Provisional
MNLIKEIEAEQLRKDIPEFRPGDTVRVHVKVVEGNKERIQAFEGVVIARRGRGLNETFTVRKISYGVGVE
RTFPLHSPRIDSIEVVRRGKVRRAKLYYLRELRGKAARIKERRDAK
>gnl|CDD|235419 PRK05339, PRK05339, pyruvate, phosphate dikinase/phosphoenolpyruvate synthase regulator
MMMKRHVFLVSDSTGETAETVGRAALSQFPNVEFEEHRYPFVRTEEKADEVLEEINAERPIVFYTLVDPE
LREILEERCAEFGIPCIDILGPLIAPLEQELGLKPTPEPGRTHGLDEEYFKRIEAIEFALAHDDGQDPRG
LDEADVILVGVSRTSKTPTSLYLANKGIKAANYPLVPEVPLPEELFPIDPKKIFGLTIDPERLIEIRKER
LPNLGLSRYASLEQCREELAEAERLFRREGIPVIDVTNKSIEETAAKILEILGLRRRMY
>gnl|CDD|235420 PRK05340, PRK05340, UDP-2,3-diacylglucosamine hydrolase; Provisional
MPTLFISDLHLSPERPAITAAFLRFLRGEARQADALYILGDLFEAWIGDDDPSPFAREIAAALKALSDSG
VPCYFMHGNRDFLLGKRFAKAAGMTLLPDPSVIDLYGQRVLLLHGDTLCTDDKAYQRFRRKVRNPWLQWL
FLALPLSIRLRIAAKMRAKSKAANQSKSLEIMDVNPEAVAALMEKHGVDTLIHGHTHRPAIHQLQAGGQP
ATRIVLGDWHEQGSVLKVDADGVELIPFPFD
>gnl|CDD|235422 PRK05342, clpX, ATP-dependent Clp protease ATP-binding subunit ClpX
ARGGDSKKLLYCSFCGKSQHEVRKLIAGPGVYICDECIELCNEIIREELKEEAVELKELPTPKEIKAHLD
QYVIGQERAKKVLSVAVYNHYKRLRHGDKKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD
ATTLTEAGYVGEDVENILLKLLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKI
LEGTVASVPPQGGRKHPQQEFIQVDTTNILFICGGAFDGLEKIIKQRLGKKGIGFGAEVKSKKEKRTEGE
LLKQVEPEDLIKFGLIPEFIGRLPVVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEAL
EAIAKKAIERKTGARGLRSILEEILLDVMFELPSREDVEKVVITKEVVEGKAKPLLIYREKS
>gnl|CDD|235423 PRK05346, PRK05346, Na(+)-translocating NADH-quinone reductase subunit C; Provisional
MAFNKDSNGKTLIVVVVLCLVCSVIVAGAAVGLKPRQEENKLLDKQKNILAAAGLVTKKDVLELYAKRIE
PRLVDLATGELVEGDPATFDERKAAKDPATSIALTPEQDIAGIKRRANYAEVYLVKDENGKLTQVILPIY
GKGLWSTMYGFVALEPDGNTVKGLTFYEHGETPGLGGEIENPQWQAQWVGKKLFDEQGKPAIKVVKGGAS
AKDEHGVDGLSGATLTSNGVQNSFKFWLGEEGYGPFLKKLRAGGLN
>gnl|CDD|235424 PRK05347, PRK05347, glutaminyl-tRNA synthetase; Provisional
MMMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDD
TNPEKEDQEYVDSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLT
EPGKNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCI
YPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLV
EEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMAVLD
PLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNAYV
IKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVPNPAAGKD
FLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAKI
>gnl|CDD|235425 PRK05349, PRK05349, Na(+)-translocating NADH-quinone reductase subunit B; Provisional
MGLKNFLDKIEPHFEKGGKYEKFYPLYEAVDTFLYTPGTVTKGATHVRDAIDLKRIMITVWLALFPAMFF
GMYNVGYQAQLALAAGAIADGWHYALFNALGGGTADAGWWSNFLYGALYFLPIYLVSFIVGGFWEVLFAV
VRGHEVNEGFFVTSILFALILPPTIPLWQVALGISFGVVIAKEVFGGTGRNFLNPALAGRAFLFFAYPAQ
MSGDAVWVAVDGFSGATALSQAAAGGLDALVNTVTGQPITWMDAFLGFIPGSIGETSTLAILIGGAILLF
TRIASWRIVAGVMIGMIATSLLFNLIGSDTNPMFAMPWYWHLVLGGFAFGMVFMATDPVSASFTNKGKWI
YGALIGFMTVLIRVVNPAYPEGMMLAILFANLFAPLFDYFVVQANIKRRLARGGK
>gnl|CDD|180033 PRK05350, PRK05350, acyl carrier protein; Provisional
MMTREEILERLRAILVELFEIDPEDITPEANLYEDLDLDSIDAVDLVVHLQKLTGKKIKPEEFKSVRTVQ
DVVDAVERLLKE
>gnl|CDD|235426 PRK05352, PRK05352, Na(+)-translocating NADH-quinone reductase subunit A; Provisional
MMIKIKKGLDLPIAGAPEQVIEDGPAPKTVALLGEDYVGLRPKMKVKEGDKVKKGQPLFEDKKNPGVKFT
SPASGTVVAINRGERRVLQSVVIEVEGDEQVTFEKYDAKDLASLSREQVKENLLESGLWTALRTRPFSKV
PAPDSTPRAIFVTAMDTNPLAADPEVIIAEQEEAFQAGLTVLSRLTDGKVHVCKAPGASLPGENLKNVEV
HTFSGPHPAGLVGTHIHFLDPVSAGKTVWTIGYQDVIAIGKLFLTGELYTERVVALAGPAVKKPRLVRTR
LGASLSELTAGELKAGDNRVISGSVLTGRTAKGPHAYLGRYHNQVSVLPEGRERELFGWLRPGFNKFSVT
RTYLSHLFKKKLFNFTTNTNGSERAMVPIGNYERVMPLDILPTQLLRALIVGDTDEAQALGALELDEEDL
ALCTFVCPGKYEYGPILRDGLDRIEKEG
>gnl|CDD|235427 PRK05354, PRK05354, biosynthetic arginine decarboxylase
MQEVAMSDWSIEDSRELYNIDHWGAGYFDINDKGHVSVRPDGDPGASIDLAELVKELRERGLRLPLLLRF
PDILQDRVRSLNAAFKKAIEEYGYQGDYRGVYPIKVNQQRRVVEEIVASGKPYNLGLEAGSKPELMAVLA
LAGDPGALIVCNGYKDREYIRLALIGRKLGHKVFIVIEKLSELELILEEAKELGVKPRLGVRARLASQGS
GKWQSSGGEKSKFGLSATEVLEAVERLREAGLLDCLQLLHFHLGSQIANIRDIKTAVREAARFYVELRKL
GAPIQYLDVGGGLGVDYDGTRSQSDSSVNYSLQEYANDVVYTLKEICEEHGVPHPTIISESGRALTAHHA
VLVFNVLGVESQEYEEPPAPAEDAPPLLQNLWETYQEISERNLQEIYHDAQQDLEEALTLFALGYLSLQE
RAWAEQLYWAICRKIQKLLDPKNRHPPELDELQERLADKYYVNFSLFQSLPDAWAIDQLFPIMPLHRLDE
EPTRRAVLADITCDSDGKIDQFIDGQGIKTTLPLHELDPGEPYYLGFFLVGAYQEILGDMHNLFGDTNAV
HVRVDEDGGYEIEHVIEGDTVADVLEYVQYDPKELLERLREKAVKEGKLSPEERQQLLEELEAGLRGYTY
LEDE
>gnl|CDD|235428 PRK05355, PRK05355, 3-phosphoserine/phosphohydroxythreonine transaminase
MMRVYNFSAGPAMLPEEVLEQAQQELLDWNGSGMSVMEISHRSKEFEAVAEEAEADLRELLNIPDNYKVL
FLQGGASLQFAMVPMNLLGGGKKADYVDTGSWSKKAIKEAKKYGEVNVAASSEDDGFTYIPPLDEWQLSD
DAAYVHYTSNETIDGTEFHELPDTGDVPLVADMSSDILSRPIDVSKFGLIYAGAQKNIGPAGLTIVIVRE
DLLGRALPSIPSMLDYKTHADNDSMYNTPPTFAIYLAGLVFKWLKEQGGVAAMEKRNQEKAALLYDAIDS
SDFYRNPVAPEDRSRMNVPFTLADEELDKKFLAEAKAAGLVGLKGHRSVGGMRASIYNAMPLEGVQALVD
FMKEFERRHG
>gnl|CDD|235429 PRK05359, PRK05359, oligoribonuclease; Provisional
NEDNLIWIDLEMTGLDPERDRIIEIATIVTDADLNILAEGPVIAIHQSDEALAAMDEWNTRTHTRSGLID
RVRASTVSEAEAEAQTLEFLKQWVPAGKSPLCGNSIGQDRRFLARYMPELEAYFHYRNLDVSTLKELARR
WKPEILNGFKKQGTHRALADIRESIAELKYYREHFFKLAPG
>gnl|CDD|235430 PRK05362, PRK05362, phosphopentomutase; Provisional
MKRVFLIVLDSVGIGAAPDAAKFGDEGADTLGHIAEARKGGLKLPNLAKLGLGNIATGTPIAGVPANAEP
IGYYGKAQEVSSGKDTPTGHWEIMGVPVLFPFGYFPNGFPQELIDEIEERAGRPGILGNKHASGTEIIDE
LGEEHMKTGKPIVYTSADSVFQIAAHEEVFGLEELYRICEIAREILLDRPYNVGRVIARPFVGEPGNFTR
TGNRHDYALKPPAPTVLDKLKEAGGEVIAVGKIADIFAGQGITEKVKTKSNMDGMDATIEEMKEAGDNGL
VFTNLVDFDSLYGHRRDVAGYAAALEEFDARLPELLAALKEDDLLIITADHGNDPTWPGTDHTREYVPLL
VYGPKFKGGSLGHRETFADIGATIADNFGVEPMEYGKSFLDELK
>gnl|CDD|235431 PRK05363, PRK05363, protein-methionine-sulfoxide reductase catalytic subunit MsrP
IKIKKPWKLPESEVTPESVYLNRRRFLKLTPEEDVTTYNNFYEFGTDKADPARNAGSLKTDPWTVKIDGE
VEKPGTLDIDDLLKLFPLEERIYRLRCVEAWSMVIPWIGFPLAKLLKRVEPTSNAKYVAFETLYDPEQMP
GQRSRFLDWPYVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLVVPWKYGFKSIKSIVRIRLTEEQP
PTTWNLLAPNEYGFYANVNPNVDHPRWSQATERRIGEGGLFAERRPTLMFNGYGEQVASLYAGMDLRKNF
>gnl|CDD|180040 PRK05365, PRK05365, malonic semialdehyde reductase; Provisional
SEALDDAALDQLFTEARTHNGWLDEPVSDEQLRELYDLVKWGPTSANCSPARFVFVRSAEAKERLRPALS
EGNLAKTLAAPVTAIVAYDTEFHEHLPKLFPHADARSWFAGNPALAEETAFRNSSLQGAYLILAARALGL
DAGPMSGFDAAAVDAEFFAGTTWKSNFLVNIGYGDPAKLFPRLPRLSFDEACRIL
>gnl|CDD|235433 PRK05368, PRK05368, homoserine O-succinyltransferase; Provisional
MPIKIPDDLPAVEILRSENIFVMTESRAAHQDIRPLKILILNLMPKKIETETQFLRLLGNTPLQVDIHLL
RIDSHESKNTPAEHLENFYCTFEDIKDEKFDGLIITGAPVEQLPFEDVDYWDELKEILDWAKTHVTSTLF
ICWAAQAALYHLYGIPKYTLPEKLSGVFEHRVLDPHHPLLRGFDDSFLVPHSRYTEVREEDIRAATGLEI
LAESEEAGVYLFASKDKREVFVTGHPEYDADTLAQEYFRDLGAGLNPPVPENYFPDDDPTLPPLARWRSH
ANLLFSNWLNYYVYQETPYDLR
>gnl|CDD|235434 PRK05370, PRK05370, argininosuccinate synthase; Validated
MSTILKHLPVGQRVGIAFSGGLDTSAALLWMRQKGAVPYAYTANLGQPDEDDYDAIPRRAMEYGAENARL
IDCRAQLVAEGIAAIQCGAFHISTGGVTYFNTTPLGRAVTGTMLVAAMKEDGVNIWGDGSTYKGNDIERF
YRYGLLTNPELKIYKPWLDQDFIDELGGRAEMSEFLIAHGFDYKMSVEKAYSTDSNMLGATHEAKDLEHL
NSGIKIVNPIMGVAFWDEDVEIKAEEVTVRFEQGRPVALNGKTFSDPVELMLEANRIGGRHGLGMSDQIE
NRIIEAKSRGIYEAPGMALLHIAYERLVTGIHNEDTIEQYRINGRRLGRLLYQGRWFDPQALMLRESLQR
WVASAITGEVTLELRRGNDYSILNTVSPNLTYKPERLSMEKVESAAFSPDDRIGQLTMRNLDITDTREKL
FIYAKTGLLSSGEASGLPQLENLENKD
>gnl|CDD|235435 PRK05371, PRK05371, x-prolyl-dipeptidyl aminopeptidase; Provisional
MKYNQFSYIPTDFETALAELKRLGFDLDLDASFKANLETFLRRSFFTYADTDYPLSNLIATPDTDLLTFF
QSPRELTAEVFYLVALQLLGFDPGVDFTLNDALAFMKKIGLPIVTTDLIKALYQLLNTRTKNGQTLIDSL
VSQGLLPGDNKPHFFNGKSLPVFDTSQLIREVVYVETPVDTDQDGKLDLVKVTIVRPKETASGLKVPVIM
TASPYYQGTNDVANDKKLHNVDVELYAKPPRAQFTPLKTQPRKLPVGPAEESFTHINSYSLNDYFLPRGF
AVVYVSGIGTRGSDGCPTTGDYQEIESMKAVIDWLNGRATAYTDRTRGKEVKADWSNGKVAMTGKSYLGT
LPNAVATTGVEGLETIIPEAAISSWYDYYRENGLVRAPGGYQGEDLDVLAELTYSRNLLAGDYLRHNEAC
EKLLAELTAAQDRKTGDYNDFWDDRNYLKDADKIKASVLVVHGLNDWNVKPKQVYQWWDALPENGVPKKL
FLHQGGHVYPNNWQSIDFRDTMNAWFTHKLLGIDNGVENELPAVIWQDNTTPQTWHKEADWPAPEATPVT
LLAGGGGQGGGLILNHYGGETFERYTDDARAFKLDLAAGKSGAARLIFITPPLTKDLRISGTPKLTLRVK
SSTNKGNLSAQLVDYGPKKRLTDTPAILGRRSLDNGYNFGREDLREFPFRETPYRIITRGWANLQNRKSL
LTVEPITPGKWYDVTFDLQPTDYVLPAGHQLGLVLYSTDFEHTIRPNPGTELTLDLSQSSLTLPVVG
>gnl|CDD|180045 PRK05377, PRK05377, fructose-1,6-bisphosphate aldolase; Reviewed
MMNQEQLEKMKNGKGFIAALDQSGGSTPKALKLYGVEEDAYSNEEEMFDLVHEMRTRIITSPAFTGDKIL
GAILFEQTMDREIEGKPTADYLWEKKGVVPFLKVDKGLAEEANGVQLMKPIPNLDDLLDRAVEKGIFGTK
MRSVIKEANEQGIAAVVAQQFEVAKQILAAGLVPIIEPEVDINSPDKAEAEAILKAEILKQLDALPEDQQ
VMLKLTIPTEANLYKELIDHPRVLRVVALSGGYSRDEANELLARNHGLIASFSRALTEGLSAQQSDEEFD
ATLGDAIDSIYDASVA
>gnl|CDD|235436 PRK05379, PRK05379, bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase
PMNRRYDYLVFIGRFQPFHNGHLAVIREALSRAKKVIVLIGSADLARSIKNPFSFEERAQMIRAALAGID
LARVTIRPLRDSLYNDSLWLAEVQAAVAEHAGADARIGLIGHEKDASSYYLRSFPQWELVDVPNTEDLSA
TEIRDAYFEGRISSFYGWAVPAPVYAFLEAFRQTPAYAQLVAEADFIEQYRKAWAAAPYPPTFVTVDAVV
VQSGHVLLVRRRAEPGKGLWALPGGFLEQDETLLDACLRELREETGLKLPEPVLRGSIRDQQVFDHPGRS
LRGRTITHAFLFEFPAGELPRVKGGDDADKARWVPLAELLAMRDRMFEDHFQIITHFLGR
>gnl|CDD|235437 PRK05380, pyrG, CTP synthetase; Validated
MTKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDL
DLGHYERFIDTNLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEI
GGTVGDIESLPFLEAIRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCR
SERPLPEEEKRKIALFCNVPEEAVISAPDVDSIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVE
RLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVKVNIKWIDSEDLEEENVAELLKGVDGILVP
GGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLEDANSTEFDPDTPHPVIDLMPEQK
DVSDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQLEKAGLVFSGTSPDGRLVEI
VELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKRK
>gnl|CDD|235438 PRK05382, PRK05382, chorismate synthase; Validated
KLFRVTTFGESHGPALGAVIDGCPAGLPLTEEDIQKELDRRRPGYSRGTTMRIEPDEVEILSGVFEGKTT
GTPIALLIRNTDQRSKDYSEIKTRPRPGHADYTYFLKYGFRDYRGGGRSSARETAARVAAGAVAKKLLKE
LGIEVRGHVVQIGGIEADLDWEEVEERADANPVRCPDPEAEEEMEELIDEAKKEGDSLGGVVEVVAEGVP
AGLGEPVFDKLDADLAHALMSINAVKGVEIGDGFAAARLRGSEVNDEIYYTGIGRLTNHAGGILGGISNG
EPIVVRVAFKPTPSIRKPQRTVDIRTGEPTELATKGRHDPCVVPRAVPVAEAMVALVLADHLLRKRDQLG
EVKRNVPRY
>gnl|CDD|235441 PRK05388, argJ, bifunctional glutamate N-acetyltransferase/amino-acid acetyltransferase ArgJ
GVTAPKGFRAAGVAAGIKKSGRKDLALIVSDGPASAAGVFTTNKFKAAPVLVCREHLADGRLRAVVVNSG
NANACTGEQGLQDARATAEAVAELLGIPAEEVLVASTGVIGEPLPMDKILAGLPAAVAALSEDGWEDAAE
AIMTTDTFPKQAAREVEIDGKTVTIGGIAKGAGMIAPNMATMLAFITTDAAISPEVLQALLREAVDKSFN
RITVDGDTSTNDTVLLLANGASGNPEIGDTPDLAAFEEALTEVCQDLAKQIVRDGEGATKLIEVTVTGAA
SEEDARKIAKAIANSPLVKTAIFGEDPNWGRILAAVGYSGADFDPDRLDIYLGGVLVAKNGGPAPFYREE
DASAYMKQEDEITIRVDLGLGDGSATAWTCDLSYDYVKINADYRT
>gnl|CDD|235443 PRK05395, PRK05395, type II 3-dehydroquinate dehydratase
MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEARDGADG
IIINPGAYTHTSVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALA
ERLSAS
>gnl|CDD|180054 PRK05396, tdh, L-threonine 3-dehydrogenase; Validated
MKALVKLKAEPGLWLTDVPVPEPGPNDVLIKVKKTAICGTDVHIYNWDEWAQKTIPVPMVVGHEFVGEVV
EVGSEVTGFKVGDRVSGEGHIVCGHCRNCRAGRRHLCRNTKGVGVNRPGAFAEYLVIPAFNVWKIPDDIP
DDLAAIFDPFGNAVHTALSFDLVGEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELARKMGAT
RAVNVAKEDLRDVMAELGMTEGFDVGLEMSGAPSAFRQMLDNMNHGGRIAMLGIPPGDMAIDWNKVIFKG
LTIKGIYGREMFETWYKMSALLQSGLDLSPIITHRFPIDDFQKGFEAMRSGQSGKVILDWD
>gnl|CDD|180055 PRK05398, PRK05398, formyl-coenzyme A transferase; Provisional
MTKPLEGIKVLDFTHVQSGPSCTQLLAWFGADVIKVERPGVGDVTRNQLRDIPDVDSLYFTMLNSNKRSI
TLDTKTPEGKEVLEKLIREADVLVENFGPGALDRMGFTWERIQEINPRLIVASIKGFGPGSPYEDVKAYE
NVAQCAGGAASTTGFWDGPPTVSGAALGDSNTGMHLAIGILAALLQREKTGRGQRVTVSMQDAVLNLCRV
KLRDQQRLDHLGYLEEYPQYPNGTFGDAVPRAGNASGGGQPGWILKCKGWETDPNAYIYFIIQPQGWEPI
CKAIGKPEWITDPAYATPEARQPHLFDIFAEIEKWTMTKTKFEAVDILNAFDIPCGPVLSMKEIAEDPSL
RASGTIVEVDHPLRGKYLTVGSPIKLSDSPPDVKRSPLLGEHTDEVLAELGYSDDQIAALKQNGAI
>gnl|CDD|235444 PRK05399, PRK05399, DNA mismatch repair protein MutS; Provisional
SMMDMSKLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAKKASRLLDITLTKRGKSAGEPIPMAGVP
YHAAEGYLAKLVKKGYKVAICEQVEDPATAKGPVKREVVRIVTPGTVTDEALLDEKQNNYLAAIAQDGGG
YGLAYLDLSTGEFRVTELDEEELLAELARLNPAEILVPEDFSEDELLLLRRGLRRRPPWEFDLDTAEKRL
LEQFGVASLDGFGVDLPLAIRAAGALLQYLKETQKRSLPHLRSPKRYEESDYLILDAATRRNLELTENLR
GGRKNSLLSVLDRTVTAMGGRLLRRWLHRPLRDREAIEARLDAVEELLEDPLLREDLRELLKGVYDLERL
LSRIALGRANPRDLAALRDSLEALPELKELLAELDSPLLAELAEQLDPLEELADLLERAIVEEPPLLIRD
GGVIADGYDAELDELRALSDNGKDWLAELEARERERTGISSLKVGYNKVFGYYIEVTKANLDKVPEDYIR
RQTLKNAERYITPELKELEDKILSAEEKALALEYELFEELREEVAEHIERLQKLAKALAELDVLASLAEV
AEENNYVRPEFTDDPGIDIEEGRHPVVEQVLGGEPFVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALI
VLLAQIGSFVPAESARIGIVDRIFTRIGASDDLASGRSTFMVEMTETANILNNATERSLVLLDEIGRGTS
TYDGLSIAWAVAEYLHDKIGAKTLFATHYHELTELEEKLPGVKNVHVAVKEHGGDIVFLHKVVPGAADKS
YGIHVAKLAGLPASVIKRAREILAQLESASEKAKAASAEEDQLSLFAEPEESPLLEALKALDPDNLTPRE
ALNLLYELKKLLKK
>gnl|CDD|235445 PRK05402, PRK05402, 1,4-alpha-glucan branching protein GlgB
IDPDDINALVAGRHHDPFSVLGPHPTGAGLVVRALLPGAEEVWVILPGGGRKLAELERLHPRGLFAGVLP
RKGPFDYRLRVTWGGGEQLIDDPYRFGPLLGELDLYLFGEGTHLRLYETLGAHPVTVDGVSGVRFAVWAP
NARRVSVVGDFNGWDGRRHPMRLRGESGVWELFIPGLGEGELYKFEILTADGELLLKADPYAFAAEVRPA
TASIVADLSQYQWNDAAWMEKRAKRNPLDAPISIYEVHLGSWRRHEDGGRFLSYRELADQLIPYVKEMGF
THVELLPIAEHPFDGSWGYQPTGYYAPTSRFGTPDDFRYFVDACHQAGIGVILDWVPAHFPKDAHGLARF
DGTALYEHADPREGEHPDWGTLIFNYGRNEVRNFLVANALYWLEEFHIDGLRVDAVASMLYLDYSRKEGE
WIPNIYGGRENLEAIDFLRELNAVVHEEFPGALTIAEESTAWPGVTRPTEEGGLGFGYKWNMGWMHDTLD
YMERDPIYRKYHHNELTFSLLYAYSENFVLPLSHDEVVHGKGSLLGKMPGDDWQKFANLRAYYGYMWAHP
GKKLLFMGGEFGQGREWNHDASLDWHLLDFPWHRGVQRLVRDLNHLYRAEPALHELDFDPEGFEWIDADD
AENSVLSFLRRGKDDGEPLLVVCNFTPVPRHDYRLGVPQAGRWREVLNTDAEHYGGSNVGNGGGVHAEEV
PWHGRPHSLSLTLPPLATLILKPEAE
>gnl|CDD|235446 PRK05406, PRK05406, 5-oxoprolinase subunit PxpA
MMKIDLNCDLGESFGAWKMGDDEALLPLVTSANIACGFHAGDPAVMRRTVRLAKENGVAIGAHPGYPDLE
GFGRRNMDLSPEELYALVLYQIGALQAIARAAGGRVSHVKPHGALYNMAAKDPALADAVAEAVAAVDPSL
ILVGLAGSELIRAAEEAGLRTASEVFADRAYTADGTLVPRSQPGAVIHDEEEAAAQVLQMVQEGRVTAID
GEWIPVEADTICVHGDGPGAVAFARRIRAALEAAGI
>gnl|CDD|180059 PRK05408, PRK05408, oxidative damage protection protein; Provisional
MARTVFCVKLGKEAEGLDFPPYPGELGKRIYENISKEAWQEWLKHQTMLINEKRLNMMDPEARKFLEEQM
EKFLFGEGAVKPEGYVPPSK
>gnl|CDD|235447 PRK05409, PRK05409, hypothetical protein; Provisional
MATPLPLGAGLGLRPEHYDEILALKPDVDFFEVHPENYMGAGGPPLAQLDAIRERYPLSLHGVSLSLGGA
APLDKDHLKRLKALADRYQPPLVSEHLAWSSDGGHLYDLLPLPYTEEALDHVAERIRQVQDILGRPLLLE
NPSSYLAFPDSEMSEWEFLNELAERTGCGLLLDVNNVYVNAVNHGFDPLAYLDALPLERVAYIHLAGHDS
EGGDLLIDTHGAPVIDPVWDLYEYAIARHGPVPTLLERDFNIPPFAELLAELDKARAILARAAARAAASA
A
>gnl|CDD|180061 PRK05412, PRK05412, putative nucleotide-binding protein; Reviewed
MPSFDIVSEVDLQEVDNAVDQANKEISTRFDFKGSKASIELKEEEITLTAESDFQLKQVKDILRSKLIKR
GIDLKALDYGKVEKASGKTVKQEVKLKQGIDQELAKKIVKLIKDSKLKVQAQIQGDQVRVTGKKRDDLQA
VIALLRKADLGQPLQFNNFRD
>gnl|CDD|235448 PRK05414, PRK05414, urocanate hydratase; Provisional
IYGYRFRPEREIRAPRGTELTAKGWLQEAALRMLMNNLDPEVAERPEELVVYGGIGRAARNWECYDAIVK
TLKELEDDETLLVQSGKPVGVFKTHPDAPRVLIANSNLVPHWANWEHFNELEAKGLTMYGQMTAGSWIYI
GSQGIVQGTYETFAEAARQHFGGDLAGRLVLTAGLGGMGGAQPLAATMAGAVCLAVEVDESRIDKRLRTG
YLDEKADDLDEALALAEEAKAAGEPLSIGLLGNAADVLPELVRRGIRPDLVTDQTSAHDPLNGYLPVGWT
LEEAAELRAEDPEEFVKAAKASMARHVEAMLAFQARGAYVFDYGNNIRQMAFDAGVENAFDFPGFVPAYI
RPLFCEGKGPFRWVALSGDPEDIYKTDAAVKELFPDDEHLHRWIDMARERILFQGLPARICWLGYGERAR
LGLAFNEMVRNGELKAPIVIGRDHLDSGSVASPNRETEAMKDGSDAVADWPLLNALLNTASGATWVSLHH
GGGVGMGYSIHAGFVIVADGTEEAAERLERVLTNDPATGVMRHADAGYEIAIETAKEKGITLPMLA
>gnl|CDD|235450 PRK05416, PRK05416, RNase adapter RapZ
MTAAPMRLVIVTGLSGAGKSVALRALEDLGYYCVDNLPPSLLPKLVELLAQSGGIRKVAVVIDVRSRPFF
DDLPEALDELRERGIDVRVLFLDASDEVLIRRYSETRRRHPLSGDGSLLEGIELERELLAPLRERADLVI
DTSELSVHQLRERIRERFGGRERGLTVTVESFGFKYGIPLDADLVFDVRFLPNPHYDPELRPLTGLDKPV
ADYVLAQPEVEEFLDKIRDLLEFWLPGYEREGKSYLTIAIGCTGGQHRSVAIAERLAERLSKGYNVQVRH
RDLERRKE
>gnl|CDD|235451 PRK05417, PRK05417, glutathione-dependent formaldehyde-activating enzyme; Provisional
MMSVAIHPSVDNGVRPGAEGFAGGTLVCKCTSNPVEVRVKAQTAHNHACGCTKCWKPEGALFSVVAVVPR
DNVTVTANGDKLKVVDESATIQRHACKECGVHMYGRIENKDHPFYGLDFVHTELSQEQGWSAPGFAAFVS
SIIESGTDPEQMDGIRARLKELGLEPYDCLSPALMDAIATHVAKKKGVLAA
>gnl|CDD|235452 PRK05419, PRK05419, protein-methionine-sulfoxide reductase heme-binding subunit MsrQ
MRLTPRQLAWLKVLLHLAGLLPLAWLVYLGATGGLGADPVKDIEHFTGLWALVFLLATLAVTPLRRLTGQ
PLLIRTRRLLGLWAFFYATLHLLSYLLLDLGLDWSLLGKEIVKRPYITVGMAAFLILLPLALTSTRASQR
RLGKRWQKLHRLVYLIAILAPLHYLWSVKSDSPEPLIYAAIVAVLLALRLKKLRRRWRRLRARAG
>gnl|CDD|235453 PRK05420, PRK05420, aquaporin Z; Provisional
MFKKLAAEFFGTFWLVFGGCGSAVLAAAFPELGIGFLGVALAFGLTVLTMAYAVGHISGGHFNPAVSVGL
WAGGRFPAKELVPYIIAQVVGGIAAAAVLYLIASGKAGFDLAGSGFASNGYGEHSPGGYSLLAALVCEVV
LTAFFLLVILGATDKRAPAGFAPIAIGLALTLIHLISIPVTNTSVNPARSTGVALFVGGWALEQLWLFWV
APIVGAIIGGLIYRLLLEKDD
>gnl|CDD|235454 PRK05421, PRK05421, endonuclease/exonuclease/phosphatase family protein
MRKKTYAMRYVAGQPAERILPPGSFASIGQALPPGEPLSTEERLRLLVWNIYKQQRAGWLSVLKNLGKDA
DLVLLQEAQTTPELVQFATANYLAADQAPAFVLPQHPSGVMTLSKAHPVYCCPLREREPWLRLPKSALIT
EYPLPNGRTLLVVNIHAINFSLGVDVYSKQLEPIGDQIAHHSGPVILAGDFNTWSRKRMNALKRFARELG
LKEVRFTDDQRRRAFGRPLDFVFYRGLNVSKASVLVTRASDHNPLLVEFSLKK
>gnl|CDD|235455 PRK05422, smpB, SsrA-binding protein SmpB
PGSKVIAQNKKARHDYFIEETFEAGIVLTGTEVKSLRAGKANLKDSYVLIKNGEAWLFNAHISPYEQGNH
FNHDPRRTRKLLLHKKEIDKLIGKVERKGYTLVPLKLYFKNGRAKVEIGLAKGKKLHDKRETIKERDWKR
EKARAMKA
>gnl|CDD|180070 PRK05423, PRK05423, DUF496 family protein
METTKPSFQDVLEFVRLFRRKNKLQREIQDNEKKIRDNQKRVLLLDNLSDYIKPGMSIEEIQGIIANMKS
DYEDRVDDYIIKNAELSKERREISKKLKAMGEMK
>gnl|CDD|235458 PRK05427, PRK05427, putative manganese-dependent inorganic pyrophosphatase; Provisional
MMKILVFGHKNPDTDSICSAIAYAYLKKALGLDAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEVQV
ILVDHNEFQQSPDDIDEATVVGVVDHHRLGNFETSNPLYYRIEPVGCTATILYKMFKENGVEIPKEIAGL
MLSAILSDTLLFKSPTTTEQDKAAAEELAEIAGVDIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNG
KKVGIGQVETVDLSEVLDRKAELEAAMKAVKAEEGYDLFLLLITDILNEGSELLVVGDDKDVVEKAFNVK
LEDNTAFLDGVVSRKKQVVPQLTEAFAA
>gnl|CDD|235459 PRK05428, PRK05428, HPr kinase/phosphorylase; Provisional
MKSVTVKDLIEDLKLEVVAGEEGLDREITTSDISRPGLELAGYFNYYHPERVQVLGKTEISYLNQLSEEE
RKERLKKLFSLEPPCIIVTRGLEPPPELLEAAKEAGIPLLRTPLSTTRLISKLTNYLDRKLAPRTSVHGV
LVDIYGIGVLITGESGIGKSETALELIKRGHRLVADDAVDIKRIGPDTLEGRCPELLQHLLEIRGLGIID
VRTLFGATAVRDKKRIQLVVELEEWDEDKEYDRLGLDEETEEILGVKIPKITIPVRPGRNLAVIIEAAAR
NYRLKLMGYDAAEEFIERLRKLIEENES
>gnl|CDD|235461 PRK05431, PRK05431, seryl-tRNA synthetase; Provisional
MLDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEA
LIAEVKELKEEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHW
ELGEKLGILDFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQL
PKFEEDLYKIEDDDLYLIPTAEVPLTNLHRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQF
DKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVVLLCTGDLGFSAAKTYDLEVWLPSQNTYREIS
SCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLVAILENYQQADGSVTIPEVLRPYMGGLE
VIPPK
>gnl|CDD|235463 PRK05434, PRK05434, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
MMMKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNI
GAGRIVYQDLTRINKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEE
GVKKVYVHAFLDGRDTPPKSALGYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGE
GPFTAESAVEALEASYARGETDEFVKPTVIGGEPVAGIEDGDAVIFFNFRADRARQITRAFTDPDFDGFD
RVPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVLAKAGLTQLRIAETEKYAHVTFFFNGGREEPFPG
EDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFANPDMVGHTGNLEAAVKAVEAVDEC
LGRVVDAVLKVGGTLLITADHGNAEQMIDPETGQPHTAHTTNPVPFILVGGKALRLEGGKLADIAPTILD
LLGLEQPAEMTGKSLIE
>gnl|CDD|235464 PRK05435, rpmA, 50S ribosomal protein L27; Validated
MAHKKGGGSTRNGRDSESKRLGVKRFGGQFVKAGNIIVRQRGTKFHPGVNVGRGKDHTLFALVDGVVKFE
RKGRNRKYVSVV
>gnl|CDD|235467 PRK05441, murQ, N-acetylmuramic acid-6-phosphate etherase; Reviewed
MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGA
GTSGRLGVLDASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAA
SGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMIST
GVMIRLGKVYGNLMVDVKATNEKLVDRAVRIVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEA
KALLARHGGFLRKALAELG
>gnl|CDD|235468 PRK05442, PRK05442, malate dehydrogenase; Provisional
MKAPVRVAVTGAAGQIGYSLLFRIASGDMLGKDQPVILQLLEIPPALKALEGVVMELDDCAFPLLAGVVI
TDDPNVAFKDADVALLVGARPRGPGMERKDLLEANGAIFTAQGKALNEVAARDVKVLVVGNPANTNALIA
MKNAPDLPAENFTAMTRLDHNRALSQLAAKAGVPVADIKKMTVWGNHSATQYPDFRHATIDGKPAAEVIN
DQAWLEDTFIPTVQKRGAAIIEARGASSAASAANAAIDHVRDWVLGTPEGDWVSMGVPSDGSYGIPEGLI
FGFPVTCENGEYEIVQGLEIDDFSREKIDATLAELEEERDAVKHLL
>gnl|CDD|235469 PRK05443, PRK05443, polyphosphate kinase; Provisional
AAPEAPPTEDLSDPERYINRELSWLAFNERVLEEAADPRNPLLERLRFLSIFSSNLDEFFMVRVAGLKRQ
IRAGVEQRSPDGLTPREQLDAISERAHRLVEEQYRLYNEELLPALAKEGIRILRYDELSEAQREWLREYF
REEIFPVLTPLAIDPAHPFPFISNLSLNLAVELEGDAIKFALVKVPRVLPRFVRLPGGEHRFVLLEDIIR
AFLDELFPGYEVLGCYQFRVTRNADLEVDEEEAEDLLEALEKELKRRRFGEVVRLEVEADMPEELLEFLL
EELGLSEDDVYRVDGPLNLTDLMQLPDVDRPDLKFPPFTPRRPPRLDHGGDIFAAIREKDILLHHPYESF
DPVVEFLRQAAADPDVLAIKQTLYRTSKDSPIVDALIEAAENGKQVTVLVELKARFDEEANIRWARRLEE
AGVHVVYGVVGLKTHAKLALVVRREGGGLRRYVHLGTGNYNPKTARLYTDLSLLTADPEIGEDVTRLFNY
LTGYSRPVKLRKLLVSPFTLRERLLELIDREIANARAGKPARIIAKMNSLVDPQIIDALYEASQAGVKID
LIVRGICCLRPGVPGLSENIRVRSIVGRFLEHSRIYYFGNGGDEEVYISSADWMPRNLDRRVEVLFPILD
PRLKQRLLEILEIQLADNVKAWELQPDGSYRRVPPARGEEPFNAQEYLLENAELSGRGAAL
>gnl|CDD|235470 PRK05444, PRK05444, 1-deoxy-D-xylulose-5-phosphate synthase; Provisional
IPKYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRI
IWDVGHQAYPHKILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGGED
RKVVAVIGDGALTGGMAFEALNNAGDLKSDLIVILNDNEMSISPNVGALSNYLARLRSSTLFEELGFNYI
GPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGEQPKSSKPGKPS
YTKVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVA
IYSTFLQRAYDQVIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQM
LYTALAYDDGPIAIRYPRGNGVGVELPELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLASATV
VDARFVKPLDEELLLELAAKHDLVVTVEEGAIMGGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREE
LLAELGLDAEGIARRILELL
>gnl|CDD|180087 PRK05445, PRK05445, YfbU family protein
MEMTNAQRLILSNQYKIMTMLDPENAERYRRLQTIIERGYGLQMRELDREFGELTEETCRTVIDIMEMYH
ALQVSWKNLKDKQGIDERRLTFLGFDAATEARYLGYVRFLVNVEGRYPHFDKGTHGFNSQTPMWDKYQRM
LTVWRACPRQYHLSANEILQILNA
>gnl|CDD|235471 PRK05446, PRK05446, bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB
MQKILFIDRDGTLIEEPPTDFQVDSLDKLAFEPGVIPALLKLQKAGYKLVMVTNQDGLGTDSFPQEDFDP
PHNLMMQIFESQGIKFDEVLICPHFPEDNCSCRKPKTGLVEEYLAEGAIDLANSYVIGDRETDVQLAENM
GIKGIRYARETLNWDAIAEQLTKRDRYAHVVRNTKETDIDVEVWLDREGKSKINTGIGFFDHMLDQIATH
GGFRLEIKVKGDLHIDDHHTVEDTALALGEALKQALGDKRGIGRFGFVLPMDECLARCALDISGRPYLVF
KAEFKRERVGDMSTEMVEHFFRSLSDAMGCTLHLKTKGKNDHHKVESLFKAFGRALRQAIRVEGNTLPSS
KGVL
>gnl|CDD|235472 PRK05447, PRK05447, 1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
MKRITILGSTGSIGTQTLDVIRRNPDRFRVVALSAGKNVELLAEQAREFRPKYVVVADEEAAKELKEALA
AAGIEVLAGEEGLCELAALPEADVVVAAIVGAAGLLPTLAAIRAGKRIALANKESLVCAGELVMDAAKKS
GAQILPVDSEHSAIFQCLPGEKQEGVEKIILTASGGPFRDWPLEELANVTPEQALKHPNWSMGRKITIDS
ATMMNKGLEVIEAHWLFGLPYEQIEVVIHPQSIIHSMVEYVDGSVLAQLGPPDMRLPIAYALAYPERVPS
GVKPLDLTKLGTLTFEPPDFERFPCLKLAYEALKAGGTAPAVLNAANEVAVAAFLAGKIGFLDIADLIEK
VLERHNPEPPSLEDVLEADAEARERARELIARLAA
>gnl|CDD|180090 PRK05449, PRK05449, aspartate alpha-decarboxylase; Provisional
MLRTMLKSKIHRATVTEADLNYEGSITIDEDLLDAAGILENEKVQIVNVNNGARFETYVIAGERGSGVIC
LNGAAARLVQVGDLVIIAAYAQMDEEEAKTHKPKVVFVDEDNRIKETAKYIPVQVA
>gnl|CDD|235473 PRK05450, PRK05450, 3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSP
DHPSGTDRIAEAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPN
VVKVVLDADGRALYFSRAPIPYGRDAFADSAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLR
ALENGYRIHVVVVEEAPSIGVDTPEDLERVRALLA
>gnl|CDD|235475 PRK05452, PRK05452, anaerobic nitric oxide reductase flavorubredoxin; Provisional
MSIHVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLA
DIDYIVINHAEEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIF
VETPMLHWPDSMMTYLTGDAVLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKI
TEILGFNLPVDMIATSHGVVWRDNPTQIVELYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAEVD
PRVAVKIFNVARSDKNEILTNVFRSKGVLVGSSTMNNVMMPKIAGLLEEITGLRFRNKRASAFGSHGWSG
GAVDRLSTRLQDAGFEMSLSLKAKWRPDQDALELCREHGREIARQWALAPLPQSTVNTVVKEETSATTTA
DLGPRMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFDELASEAK
>gnl|CDD|235476 PRK05454, PRK05454, glucans biosynthesis glucosyltransferase MdoH
DEGRTALKAMPPEAPLAMPPQPWTKEEEGPERRWRTVGTLRRLILLGLTLAQTAVATWEMKAVLPYGGWT
LLEPALLVLFALLFAWISLGFWTALMGFLQLLRGRDKYSISASAAGDPPPPPEARTAILMPIYNEDPARV
FAGLRAMYESLAATGHGAHFDFFILSDTRDPDIAAAEEAAWLELRAELGGEGRIFYRRRRRNVGRKAGNI
ADFCRRWGGAYDYMVVLDADSLMSGDTLVRLVRLMEANPRAGLIQTLPVAVGADTLFARLQQFATRVYGP
LFAAGLAWWQGGEGNYWGHNAIIRVKAFAEHCGLPPLPGRGPFGGHILSHDFVEAALMRRAGWGVWLAPD
LPGSYEELPPNLLDELKRDRRWCQGNLQHLRLLLAKGLHPVSRLHFLTGIMSYLSAPLWLLFLLLGTALA
LQAALTEPEYFQPRQLFPVWPQWDPELAIALFAATMVLLFLPKLLGLLLVLLDPKRRRAFGGALRLLLSV
LLETLFSALLAPIRMLFHTRFVVSILLGRDVGWNSQRRDDGSTPWGEAFRRHGWHTLLGLVLAAGAAWLS
PSLLLWLAPILLGLILAIPLSVLTSRASLGLALRRRGLFDPVLLQ
>gnl|CDD|235477 PRK05456, PRK05456, ATP-dependent protease subunit HslV
GTTILAVRRNGKVAIAGDGQVTLGNTVMKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEHQG
NLLRAAVELAKDWRTDRYLRRLEAMLIVADKEHSLIISGNGDVIEPEDGIIAIGSGGNYALAAARALLEN
TDLSAEEIAEKALKIAADICIYTNHNITIEEL
>gnl|CDD|235478 PRK05457, PRK05457, protease HtpX
MKRIALFLLTNLAVMLVLGIVLSLLGVQSYLNLGGLLVFAAVFGFGGSFISLLMSKWMAKRSTGAEVIEQ
PRNETERWLVETVARQARQAGIGMPEVAIYHSPEINAFATGASKNNSLVAVSTGLLQNMSRDEVEAVLAH
EISHIANGDMVTMTLIQGVVNTFVIFLSRIIAQIVDRFVSGNEEGNGIGYFIVSIVLEIVFGILASIIVM
WFSRHREFRADAGGAKLAGREKMIAALQRLKTSYEPQLPGSMAAFGINGKSGLSELFMSHPPLEKRIAAL
RSGR
>gnl|CDD|235479 PRK05458, PRK05458, guanosine 5'-monophosphate oxidoreductase; Provisional
MMKVFDYEDIQLIPNKCIVNSRSECDTSVTLGPRTFKLPVVPANMQTIIDEKIAEWLAENGYFYIMHRFD
PEARIPFIKDMHEQGLIASISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPE
TFVIAGNVGTPEAVRELENAGADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGI
RTHGDIAKSIRFGATMVMIGSLFAGHEESPGKTVEIDGKLYKEYFGSASEFQKGEYKNVEGKKILVPHKG
SLKDTLTEMEQDLQSSISYAGGRDLDAIRKVDYVIVKNSIFNGDKI
>gnl|CDD|180098 PRK05461, apaG, CO2+/MG2+ efflux protein ApaG; Reviewed
MYSAVTYGIEVSVQPRYLEEQSDPEEGRYVFAYTITIENLGRVPVQLLSRHWLITDANGRVQEVRGEGVV
GEQPVLAPGESFEYTSGAVLETPSGTMQGHYQMVDEDGERFEVPIPPFRLAVPRTLH
>gnl|CDD|235480 PRK05462, PRK05462, adenosylmethionine decarboxylase
KPMKKLKLHGFNNLTKSLSFNIYDICYAKTEEERDGYIAYIDEQYNAERLTEILTEVCSIIGANILNIAR
QDYEPQGASVTILISEEPVDPKLIDKSEHPGPLPETVVAHLDKSHITVHTYPESHPEGGICTFRADIDVS
TCGVISPLKALNYLIHSFESDIVTIDYRVRGFTRDINGKKHFIDHEINSIQNFISEDTKSLYDMIDVNVY
QENIFHTKMLLKEFDLDNYLFNTKPEDLSPEERQEITALLRKEMREIYYGRNIPAV
>gnl|CDD|180100 PRK05463, PRK05463, putative hydro-lyase
AELAAMTPAEARQAIRAGELTGPTAGLAPGYAQANLVILPKDWAYDFLLFCQRNPKPCPLLDVTEPGSPE
LPLLGPDADIRTDVPRYRVYRDGELVEEVTDITDLWRDDLVTFLIGCSFSFEHALLEAGIPVRHIEEGRN
VPMYRTNIPCRPAGRFSGPMVVSMRPIPAADAIRAVQITSRFPAVHGAPVHIGDPAAIGIADLARPDFGD
AVEIEPGEIPVFWACGVTPQAVVMAAKPPFAITHAPGHMLITDLPDSELAVL
>gnl|CDD|235482 PRK05465, PRK05465, ethanolamine ammonia-lyase subunit EutC
AKAWILVPNPVDADPWLELRRFTPARIGLGRAGTSLPTQALLRFQADHAQARDAVHLPVDEEALAAQLAN
LLEVRSAASDRDEYLTRPDLGRRLSDESREALKAQCGKNPDVQIVVADGLSALAVEANAEPLLPALLAGL
KAAGWSVGPPVFVRQGRVALGDEIGELLGAKVVVVLIGERPGLSSPDSLGAYLTYAPRVGTTDADRNCIS
NIHPGGLPYAEAAAKIAYLIKEALRLKASGVDLKDESDALLLAAAATAAL
>gnl|CDD|235483 PRK05467, PRK05467, Fe(II)-dependent oxygenase superfamily protein; Provisional
MLLHIPDVLSPEEVAQIRELLDAAEWVDGRVTAGAQAAQVKNNQQLPEDSPLARELGNLILDALTRNPLF
FSAALPRKIHPPLFNRYEGGMSYGFHVDNAVRSLPGTGGRVRTDLSATLFLSDPDDYDGGELVIEDTYGE
HRVKLPAGDLVLYPSTSLHRVTPVTRGVRVASFFWIQSLVRDDSQRELLFDLDTAIQSLLARHGDSPELD
LLTGVYHNLLRRWAEV
>gnl|CDD|235484 PRK05469, PRK05469, tripeptide aminopeptidase PepT
MDKLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDENGYVMATLPANVDKDV
PTIGFIAHMDTAPDFSGKNVKPQIIENYDGGDIALGDGNEVLSPAEFPELKNYIGQTLITTDGTTLLGAD
DKAGIAEIMTALEYLIAHPEIKHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFN
AASAKITIHGVNVHPGTAKGKMVNALLLAADFHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYII
RDFDREGFEARKALMQEIAKKVNAKYGEGRVELEIKDQYYNMREKIEPHPHIVDLAKQAMEDLGIEPIIK
PIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVIVEIAELTAERA
>gnl|CDD|180105 PRK05470, PRK05470, fumarate reductase subunit FrdD
INQNPKRSDEPVFWGLFGAGGMWSAIIAPVLILLVGILLPLGLFPGDALSYERVLAFAQSFIGKLFLLLM
IVLPLWCGLHRIHHGMHDLKIHVPAGKWVFYGLAAILTVVALIGVLTI
>gnl|CDD|235485 PRK05471, PRK05471, CDP-diacylglycerol pyrophosphatase; Provisional
MRKAGLLFLVLLVIAVLAAGLGYWKLRGADRDALWKIVSEQCLPNQQQNQNPAPCAEVDPQAGYVLLKDR
NGPLQYLLMPTYRISGIESPLLLEPSTPNYFALAWQARDFMSKKYGKPIPDSAVSLAINSRYGRTQDQLH
IHISCLRPDVRAQLDNNLAAISSRWLPLPGGLRGHEYLARRVTESELVQRSPFRMLAEEVPGAREHMGRY
GLAVARQSDGSFVLLATERDLLTLNRASAEELQDHSCAILRG
>gnl|CDD|235486 PRK05472, PRK05472, redox-sensing transcriptional repressor Rex; Provisional
MMKQKKIPEATIKRLPLYYRYLKELKEEGVERVSSKELAEALGVDSAQIRKDLSYFGEFGKRGVGYNVEE
LLEFIEKILGLDRTWNVALVGAGNLGRALLNYNGFEKRGFKIVAAFDVDPEKIGTKIGGIPVYHIDELEE
VVKENDIEIGILTVPAEAAQEVADRLVEAGIKGILNFAPVRLSVPEDVIVRNVDLTVELQTLSYFLNNYE
LKE
>gnl|CDD|180108 PRK05473, IreB-like, IreB family regulatory phosphoprotein. IreB (EF1202) was characterized in Enterococcus faecalis as a small protein, well-conserved in the Firmicutes. It belongs to a system that includes the Ser/Thr protein kinase IreK, and phosphatase IreP, undergoes phosphorylation on threonine residues, and is involved in regulating cephalosporin resistance. This family was previously named DUF965 by Pfam model pfam06135
MSSFDKTMRFDFDDEKKKDVREILTTVYDALEEKGYNPINQIVGYLLSGDPAYIPRHNDARNLIRKLERD
EILEELVKSYLKGNGK
>gnl|CDD|235487 PRK05474, PRK05474, xylose isomerase; Provisional
EYFPDIDKIRYEGPESDNPLAFRHYNPDEVVLGKTMEEHLRFAVAYWHTFCWPGADPFGGGTFQRPWDQP
GDALDLAKAKADAAFEFFTKLGVPYYCFHDVDVAPEGASLKEYNANLDEIVDYLKEKQAETGVKLLWGTA
NLFSNPRYMAGAATNPDPDVFAYAAAQVKTALDATKRLGGENYVFWGGREGYETLLNTDLKREREQLARF
LQMVVDYKHKIGFKGTFLIEPKPQEPTKHQYDYDAATVYGFLKQYGLEKEFKLNIEANHATLAGHTFEHE
LAVARALGILGSIDANRGDYQLGWDTDQFPNNVYETTLAMYEILKAGGFTTGGLNFDAKVRRQSTDPEDL
FYAHIGGMDTFARGLKVAAKMIEDGVLEKLVAERYASWDSGLGQDILAGKLSLEDLAAYALAHGLNPQHQ
SGRQELLENLVNRYIFD
>gnl|CDD|235488 PRK05476, PRK05476, S-adenosyl-L-homocysteine hydrolase; Provisional
TTATGTDYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKA
LGAEVRWASCNPFSTQDDVAAALAAAGIPVFAWKGETLEEYWECIERALDGHGPNMILDDGGDLTLLVHT
ERPELLANIKGVTEETTTGVHRLYAMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLI
AGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVDPICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDV
ITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKPQVDEYTLPDGKRIILLAEGRLVNLGAAT
GHPSEVMDMSFANQALAQIELFTNRGKLEPGVYVLPKELDEEVARLKLKALGVKLDELTEEQAEYIGVWV
EGPFK
>gnl|CDD|235489 PRK05477, gatB, Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB
AMMNFEVVIGLEVHVQLNTKSKIFSGCSTDFGAEPNTNVCPVCLGLPGALPVLNKEAVEYAIKAGLALNC
EIAKRSRFDRKNYFYPDLPKGYQISQYDEPIAENGYLEIELGEKRIGIERIHLEEDAGKSVHDQGAGYSL
VDYNRAGVPLIEIVSEPDMRSPEEARAYLKKLRSILRYLGISDGNMEEGSLRCDANVSVRPKGQEEFGTR
VEIKNLNSFRFVEKAIEYEIERQIEILESGGEVVQETRLFDEDKGETRSMRSKEEAHDYRYFPEPDLPPL
EISDEWIEEIRAELPELPDAKRARFVEEYGLSEYDARVLTSDKELADYFEAVVAAGADAKLAANWLMGEL
LGLLNEEGIEIEESPITPEQLAELIKLIDDGTISGKIAKEVFEEMLETGGDPDEIVEEKGLKQISDEGAL
EAIVDEVLAANPKAVEDYKAGKEKALGFLVGQVMKATKGKANPKLVNELLKEKL
>gnl|CDD|235490 PRK05478, PRK05478, 3-isopropylmalate dehydratase large subunit
MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDR
DLPIADPVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGAL
AFGIGTSEVEHVLATQTLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRA
LSMEGRMTICNMSIEAGARAGLVAPDETTFEYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLD
AADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAERALAYMGLKPGTPITDIKIDKVFIGSCTNS
RIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAMNPDKLPP
GERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL
>gnl|CDD|235491 PRK05479, PRK05479, ketol-acid reductoisomerase; Provisional
MMKVYYDKDADLSLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLREGSKSWKKAEADGFEVLTVAEA
AKWADVIMILLPDEVQAEVYEEEIEPNLKEGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRRE
YEEGGGVPCLIAVHQDASGNAKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTELIKAG
FETLVEAGYQPEMAYFECLHELKLIVDLIYEGGIANMRYSISNTAEYGDYVSGPRVITEETKKEMKEVLK
DIQSGEFAKEWILENKAGRPTFKALRREEAEHPIEKVGAKLRAMMPWIKK
>gnl|CDD|235492 PRK05480, PRK05480, uridine/cytidine kinase; Provisional
MMMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDL
LIEHLKALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRL
IRRLKRDVNERGRSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN
>gnl|CDD|235493 PRK05481, PRK05481, lipoyl synthase; Provisional
AEKVARKPDWLRVKLPTGEEYTEIKKLLRELGLHTVCEEASCPNIGECWSRGTATFMILGDICTRRCPFC
DVATGRPLPLDPDEPERVAEAVARMGLKYVVITSVDRDDLPDGGAQHFAETIRAIRELNPGTTIEVLIPD
FRGRMDALLTVLDARPDVFNHNLETVPRLYKRVRPGADYERSLELLKRAKELHPGIPTKSGLMVGLGETD
EEVLEVMDDLRAAGVDILTIGQYLQPSRKHLPVERYVTPEEFDEYKEIALELGFLHVASGPLVRSSYHAD
EQAAGAEVA
>gnl|CDD|180119 PRK05500, PRK05500, bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase
MNFFDKLTQAIAQNQSLLVVGLDPNPEMMPGRYSSQSLIQQLWTWLKFIIEETADLVCAYKPTLGFYQAL
GSPGLELLLEVLAAIPPDIPIILDAKHGDLNTSTIFAKTIFEQWQVDAVTLSPYAGQDHVAPFLVYPDKG
VFILCHTSNPGAIALQEYPTPENPFYLQVVKEAKTWGTPEQLGLEVGTTNPEVLAKIRQIAPERLILLRS
IWAEKGNLNQILTAGLNSNGDGLLIPVPQDLLGAANLKEQVKSLREEINQIRQQIVQESSSCDLWTPDVC
LLNQHPHQDLILQLYDIGCLLFGEYVQASGATFSYYIDLRKIISNPQLFHQVLSAYAEILKNLTFDRIAG
IPYGSLPTATGLALHLHHPMIFPRKEVKAHGTRRLIEGNFHPGETVVVVDDILITGKSVMEGAEKLKSAG
LNVRDIVVFIDHEQGVKDKLQSHGYQAYSVLTISEITETLYQAGRINEEQYQALTEH
>gnl|CDD|180120 PRK05506, PRK05506, bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
MSHQSDLIAEDILAYLAQHERKSLLRFITCGSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGTQG
DEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKG
VLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLHDVTFIPISALKGDNVV
TRSARMPWYEGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPNLDFRGFAGTVASGVVRPGDEVVVLPSG
KTSRVKRIVTPDGDLDEAFAGQAVTLTLADEIDISRGDMLARADNRPEVADQFDATVVWMAEEPLLPGRP
YLLKHGTRTVPASVAAIKYRVDVNTLERLAAKTLELNEIGRCNLSTDAPIAFDPYARNRTTGSFILIDRL
TNATVGAGMIDFALRRATNVHWQASDVSREARAARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRH
TYLLDGDNVRHGLNRDLGFSDADRVENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEGEFV
EVFVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDSPYEAPENPELRLDTTGRSPEELAEQVLELLRRRG
AI
>gnl|CDD|180121 PRK05508, PRK05508, methionine-R-sulfoxide reductase
YNELTPEEEAVILRKGTEPPFSGEYNDFFEKGTYVCKQCGAPLYRSEDKFKSGCGWPSFDDEIKGAVKRI
PDADGRRTEIVCANCGGHLGHVFEGEGFTPKNTRHCVNSISLKFVPDKG
>gnl|CDD|235496 PRK05518, rpl6p, 50S ribosomal protein L6P; Reviewed
MVAAYIREEIEIPEGVTVEIEGLVVTVKGPKGELTRDFWYPGVTISVEDGKVVIETEFARKKTKAMVGTF
ASHIKNMIKGVTEGFEYKLKIVYSHFPMQVKVQGNEVVIENFLGEKSPRRAKILGGVKVKVKGEDVIVEG
IDKEDVGQTAANIEQATKIKGFDRRVFQDGIYIVEKEVKG
>gnl|CDD|235497 PRK05528, PRK05528, peptide-methionine (S)-S-oxide reductase
METVYFAGGCLWGVQAFFKTLPGVIHTEAGRANGRTSTLDGPYDGYAECVKTHFDPRMVSITDLMGYLFE
IIDPYSVNKQGNDVGEKYRTGIYSEVDDHLIEARQFIERREDADKIAVEVLPLTNYVKSAEEHQDRLEKF
PEDYCHIPKDLLNKYK
>gnl|CDD|135428 PRK05529, PRK05529, cell division protein FtsQ; Provisional
MTVNDEAYQNLRYARKERKDYERVRRFTTRIRRRFILLACAVGAVLTLLLFVMLSAYSPLLALRSIEVAG
NMRVKPQDIVAALRDQFGKPLPLVDPETVRKKLAAFPLIRSYSVESKPPGTIVVRVVERVPLAFIQRGDG
FHVVDAAGVSIKVTQARPLGMPLIDVPKDGNQEQLFAAAAWVLAALPADLKKQVDLISAETPDDVNLTLR
NSGKTVFWGSFENSKLKAKVLEALLKIPGHYSSYDVSAPEAPAVG
>gnl|CDD|180124 PRK05537, PRK05537, bifunctional sulfate adenylyltransferase/adenylylsulfate kinase
LILPNGGPLPNLYVSPESREKLKAEALSLPSLDLSPRQICDLELLMNGGFSPLKGFMGRADYECVLENMR
LADGTLWPIPITLDVSEKFAAGLEIGERIALRDQEGVLLAILTVSDIWEPDKEREAEAVFGTTDPAHPGV
NYLHRWAGKFYLGGPLTGIQLPVHYDFVQLRLTPAELRARFRKLGWRRVVAFQTRNPLHRAHEELTKRAA
REVGANLLIHPVVGMTKPGDIDHFTRVRCYEALLDKYPPATTLLSLLPLAMRMAGPREALWHAIIRRNYG
CTHFIVGRDHAGPGKDSRGKPFYGPYDAQELFAKYADEIGITMVPFKEMVYVQDKAQYVPVDEVPQGATV
LTISGTELRRRLREGLEIPEWFSFPEVVAELRRTYPPRHKQGFTVFFTGLSGAGKSTIAKALMVKLMEMR
GRPVTLLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAICAPIAPYRATRREVREMIEAY
GGFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTNVTPDECAHKILLYL
EEKGYLRG
>gnl|CDD|235498 PRK05541, PRK05541, adenylylsulfate kinase; Provisional
MQMKPNGYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHYGYDKQSRIEMALKRAKL
AKFLADQGMIVIVTTISMFDEIYAYNRKHLPNYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDI
PFDEPKADLVIDNSCRTSLDEKVDLILNKLKLRLIQ
>gnl|CDD|235499 PRK05550, PRK05550, bifunctional methionine sulfoxide reductase B/A protein; Provisional
MDKMKSLTPFEYRVIEDKGTERPFSGEYYDHDEKGVYLCRRCGAPLFRSEDKFNSGCGWPSFDDEIPGAV
KRLPDADGRRTEIVCANCGAHLGHVFEGEGLTPKNTRHCVNSASLDFVPAEEGAYDTEEAIFAGGCFWGV
EYYFKKLPGVLSVESGYTGGDTKNPTYEQVCSGTTGHAEAVRVEFDPAKISYETLLKVFFEIHDPTQLNR
QGPDIGTQYRSAIFYHDDEQKQIAEKLIAELTKKGYPVVTEVEAAGPFYPAEDYHQDYYEKHGKQPYCHI
VVK
>gnl|CDD|235500 PRK05557, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Validated
MSLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESV
ERAVDEAKAEFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINI
SSVVGLMGNPGQANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPL
GRLGQPEEIASAVAFLASDEAAYITGQTLHVNGGMVMG
>gnl|CDD|235501 PRK05559, PRK05559, DNA topoisomerase IV subunit B; Reviewed
AAMMTNNYNADSIEVLEGLEPVRKRPGMYIGSTDTRGLHHLVQEVIDNSVDEALAGHGKRIEVTLHADGS
VSVRDNGRGIPVGIHPEEGKSGVEVILTKLHAGGKFSNKAYKFSGGLHGVGVSVVNALSSRLEVEVKRDG
KVYRQRFEGGDPVGPLEVVGTAGKRKTGTRVRFWPDPKIFDSPKFSPERLKERLRSKAFLLPGLTITLND
ERERQTFHYENGLKDYLAELNEGKETLPEEFVGSFEGEAEGEAVEWALQWTDEGGENIESYVNLIPTPQG
GTHENGFREGLLKAVREFAEKRNLLPKGKKLEGEDVREGLAAVLSVKIPEPQFEGQTKEKLGSREARRFV
SGVVKDAFDLWLNQNPELAEKLAEKAIKAAQARLRAAKKVKRKKKTSGPALPGKLADCTSQDPERTELFL
VEGDSAGGSAKQARDREFQAILPLRGKILNTWEASLDDVLANEEIHDIIVAIGIGPGDSFDLEDLRYGKI
IIMTDADVDGAHIATLLLTFFYRHFPPLVEAGHVYIALPPLYRVDKGKKKIYALDEEEKEELLKKLGKKG
GKPEIQRFKGLGEMNPDQLWETTMDPETRRLVRVTIDDAEETEKLVDMLMGKKAEPRREWIEENGDFAEE
E
>gnl|CDD|235502 PRK05560, PRK05560, DNA gyrase subunit A; Validated
EGDRIIPVNIEDEMKRSYLDYAMSVIVGRALPDVRDGLKPVHRRILYAMNELGNTPDKPYKKSARIVGDV
MGKYHPHGDSAVYDALVRMAQDFSMRYPLVDGQGNFGSIDGDPAAAMRYTEARMSKIAHELLADIDKETV
DFVPNYDGSEQEPTVLPARFPNLLVNGSSGIAVGMATNIPPHNLGEVIDACLALIDNPDITIEELMEIIP
GPDFPTGGIILGRSGIREAYRTGRGSIVMRAKAEIEEIKGREAIIVTEIPYQVNKARLIEKIAELVKEKK
IEGISDLRDESDRDGMRIVIELKRDAVPEVVLNNLYKHTQLQTSFGINMLALVDGQPKLLNLKEILEAFL
EHRKEVITRRTRFELRKAEERAHILEGLLIALDNIDEVIALIRASPTPAEAKEGLMERFGLSEIQAQAIL
DMRLQRLTGLERDKIEDEYKELLALIADLKDILASPERLLEIIKEELLEIKEKFGDPRRTEIIEGEGDID
DEDLIPEEDVVVTLTHGGYIKRTPLDEYRAQRRGGKGVSGAKTKEDDFVEHLFVASTHDTLLFFTNRGRV
YRLKVYEIPEASRTARGRPIVNLLPLEPGEKITAILPVREFDDDKYLFFATKNGTVKKTSLSEFSNIRSN
GIIAINLDEGDELIGVRLTDGDDDILLATKNGKAIRFPESDVRPMGRTARGVRGIKLREGDEVVSMDVVR
EDSQEILTVTENGYGKRTPVSEYRLQGRGGKGVITIKITEKNGKLVGALPVDDDDEIMLITDSGKLIRTR
VSEISITGRNTQGVRLIRLDEGDKVVSVARVAEEE
>gnl|CDD|235503 PRK05561, PRK05561, DNA topoisomerase 4 subunit A
PPDMSMLEGIEDLPLEEFLEERYLRYAMYVIMDRALPDVRDGLKPVQRRILYAMSELGLTPDAKFKKSAR
VVGDVLGKYHPHGDSSIYDAMVRMAQDFSYRYPLVDGQGNFGSIDGDPAAAMRYTEARLSPIAELLLEEI
DEGTVDFVPNFDGTLKEPTVLPARFPNLLLNGATGIAVGMATDIPPHNLREVIDAAIHLIDNPDATLEEL
MEFVPGPDFPTGGEIITGRDGIRKAYETGRGSIRVRARWEIEDLAGGRWQIVITELPYQVSKAKLIEQIA
ELMNAKKLPGIADVRDESDRENPVRIVIEPKSNRVDPEALMNHLFATTDLESSYRVNMNAIGLDGRPRVK
GLKEILSEWLDHRREVVTRRSQFRLDKVEKRLHILEGLLIAFLNIDEVIRIIRESDEPKANLMARFDLSE
IQAEAILELRLRRLAKLEEIEIRKEQDELRKEIAELEAILASERKLRKLIKKELKADAKKFGDPRRTPIE
EAEEAIAIDEEALIPDEPVTVVLSKKGWVRRAKGHSIDASGLSFKEGDSLLFAFEARTTDKLLLFTSTGR
VYSLPVHELPSARGDGEPLTGLVDLAPGEEIVHVLAFDPDQKLLLASSAGYGFVVTLEDLVARTRAGKAV
INLKDGDEVLPPVPVEDDDHLAAITSNGRLLVFPLSELPELGKGKGVKLINLPKDDDGLVDLRVLNPEDG
LVLLTAGKRKLKLKPSELEKYRGKRARRGRLLPRGLKRVPRF
>gnl|CDD|235504 PRK05562, PRK05562, NAD(P)-dependent oxidoreductase
MLKDNKEDIYNEENKYMFISLLSNKIKVLIIGGGKAAFIKGKTFLKKGCYVYILSKKFSKEFLDLKKYGN
LKLIKGNYDKEFIKDKHLIVIATDDEKLNNKIRKHCDRLYKLYIDCSDYKKGLCIIPYQRSTKNFVFALN
TKGGSPKTSVFIGEKVKNFLKKYDDFIEYVTKIRNKAKKNELKDEIIEFICSDDFYFFYKKGKANLILSM
FYGEEDFEFLNSG
>gnl|CDD|235505 PRK05563, PRK05563, DNA polymerase III subunits gamma and tau; Validated
MMYQALYRKWRPQTFEDVVGQEHITKTLKNAIKQGKISHAYLFSGPRGTGKTSAAKIFAKAVNCLNPPDG
EPCNECEICKAITNGSLMDVIEIDAASNNGVDEIRDIRDKVKYAPSEAKYKVYIIDEVHMLSTGAFNALL
KTLEEPPAHVIFILATTEPHKIPATILSRCQRFDFKRISVEDIVERLKYILDKEGIEYEDEALRLIARAA
EGGMRDALSILDQAISFGDGKVTYEDALEVTGSVSQEALDDLVDAIVEGDVAKALKILEELLDEGKDPNR
FIEDLIYYLRDLLLVKTSPELEILDESTENDELFKELSEKLDIERLYRMIDILNDAQQQIKWTNQPRIYL
EVALVKLCEQAAASPEYDTELEVLLQRVEQLEQELKQLKAQPVGVAPEQKEKKKEKKKNKKKKYKVPRGK
IYKVLKEATRQDLELLKNVWGEILESLKAQRKSLRALLVNSEPVAASEDTVVLAFEYEIHFEKAMLDKEL
NDTIENILSKLLGKSVEIVAVPEDEWQKIREEFLQKHKNEEEEEEEEEELPLIPEAKELFGEDLVEIID
>gnl|CDD|180132 PRK05564, PRK05564, DNA polymerase III subunit delta'; Validated
MSFHTIIGHENIKNRIKNSIIKNRFSHAHIIVGEDGIGKSLLAKEIALKILGKSQQREYVDIIEFKPINK
KSIGVDDIRNIIEEVNKKPYEGDKKVIIIYNSEKMTEQAQNAFLKTIEEPPKGVFIILLCENLEQILDTI
KSRCQIYKLNRLSKEEIEKFISYKYNDIKEEEKKSAIAFSDGIPGKVEKFIEDDSLKNIRNMSLEILKDI
KKSNINILLKYENFLIKYKENWEEILTCILSYIRDSLLYKETGNEELIINIDKIEDIKHISEKFSYKKLN
KMIEIINDTRDNLSSNVNPTLVFDSMLIKMQEV
>gnl|CDD|235506 PRK05565, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
MKLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDV
ENLVEQIVEKFGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNI
SSIWGLIGASCEVLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPL
GRLGKPEEIAKVVLFLASDDASYITGQIITVDGGWTC
>gnl|CDD|235508 PRK05568, PRK05568, flavodoxin; Provisional
MKKINIIYWSGTGNTEAMANLIAEGAKENGAEVKLLNVSEASVDDVKGADVVALGSPAMGDEVLEEGEME
PFVESISSLVKGKKLVLFGSYGWGDGEWMRDWVERMEGYGANLVNEGLIVNNTPEGEGIEKCKALGEALA
KA
>gnl|CDD|135442 PRK05569, PRK05569, flavodoxin; Provisional
MKKVSIIYWSCGGNVEVLANTIADGAKEAGAEVTIKHVADAKVEDVLEADAVAFGSPSMDNNNIEQEEMA
PFLDQFKLTPNENKKCILFGSYGWDNGEFMKLWKDRMKDYGFNVIGDLAVNESPNKEELNSAKELGKKLA
K
>gnl|CDD|235509 PRK05571, PRK05571, ribose-5-phosphate isomerase B; Provisional
MKIAIGSDHAGFELKEEIIEHLEELGHEVIDLGPDSYDASVDYPDYAKKVAEAVVAGEADRGILICGTGI
GMSIAANKVKGIRAALCHDTYSAHLAREHNNANVLALGARVIGPELAKDIVDAFLATEFEGGRHQRRIDK
IDEYEAQK
>gnl|CDD|180137 PRK05572, PRK05572, RNA polymerase sporulation sigma factor, SigF/SigG family
MDIEVKNKKKKPQLKDEENKELIKKSQDGDQEARDTLVEKNLRLVWSVVQRFLNRGYEPDDLFQIGCIGL
LKAVDKFDLSYDVKFSTYAVPMIIGEIQRFLRDDGTVKVSRSLKETANKIRKDKDELSKELGREPTIEEL
AEYLGVTPEEVVLAQEASRSPQSIHETVHENDGDPITLLDQIADQSEEDWFDKIALKEAIRELDERERLI
VYLRYFKDKTQSEVAKRLGISQVQVSRLEKKILKQMKEKLDE
>gnl|CDD|235510 PRK05573, rplU, 50S ribosomal protein L21; Validated
MYAIIKTGGKQYKVEEGDVIKVEKLDAEVGDTVEFDEVLLVGGGEEVKIGAPYVEGAKVTAEVVEHGRGK
KVIVFKYKRRKNYRKKQGHRQPYTKVKITSINA
>gnl|CDD|180140 PRK05575, cbiC, precorrin-8X methylmutase; Validated
MDYIKKPMGIEKRSFEIIGEEMGEHNFSEEELKIVKRVIHTTADFEYKDLIYIREGAIEAAKEILKKGTK
IYTDTNMALSGINKKALKKLNSTVQCYVSREEVAKIAKERGITRSMAAVEKAAEEGVEFFVFGNAPTALY
KLKELIKEGKANPKFIIAVPVGFVGAAESKEELEKLDIPYITVRGRKGGSTVAAAIVNALMYML
>gnl|CDD|235512 PRK05576, PRK05576, cobalt-factor II C(20)-methyltransferase
MGKLYGIGLGPGDPELLTVKAARILEEADVVYAPASRKGGGSLALNIVRPYLKEETEIVELHFPMSKDEE
EKEAVWKENAEEIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSFTAIASRAGVP
LAMGDESLAIIPATREALIEQALTDFDSVVLMKVYKNFALIEELLEEGYLDALYVRRAYMEGEQILRRLE
EILDDLDYFSTIIANRQWE
>gnl|CDD|180142 PRK05578, PRK05578, cytidine deaminase; Validated
MDWKELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRL
VAIACVGETGEPLSPCGRCRQVLAEFGGPDLLVTLVAKDGPTGEMTLGELLPYAFTPDDLG
>gnl|CDD|235513 PRK05579, PRK05579, bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
MRMLAGKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAA
EAAMGHIELAKWADLVLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLA
TLRSRGVEIIGPASGRLACGDVGPGRMAEPEEIVAAAERALSPKDLAGKRVLITAGPTREPIDPVRYITN
RSSGKMGYALARAAARRGADVTLVSGPVNLPTPAGVKRIDVESAQEMLDAVLAALPQADIFIMAAAVADY
RPATVAEGKIKKGEGELTLELVPNPDILAEVAALKDKRPFVVGFAAETGDVLEYARAKLKRKGLDLIVAN
DVSAGGGFGSDDNEVTLIWSDGGEVKLPLMSKLELARRLLDEIAERLLE
>gnl|CDD|235514 PRK05580, PRK05580, primosome assembly protein PriA; Validated
MMKIARVLLPVPLPRPFDYLIPEGLEVQPGDRVRVPFGNRKLIGVVVGVEEGSEVPADKLKPILEVLDLE
PLLPPELLRLLDWAADYYLSPLGEVLRLALLAELALAASSAVLKGLVKKGLIELEEVEVLRLRPPPDPAF
EPPTLNPEQAAAVEAIRAAAGFSPFLLDGVTGSGKTEVYLQAIAEVLAQGKQALVLVPEIALTPQMLARF
RARFGAPVAVLHSGLSDGERLDEWRKAKRGEAKVVIGARSALFLPFKNLGLIIVDEEHDSSYKQQEGPRY
HARDLAVVRAKLENIPVVLGSATPSLESLANAQQGRYRLLRLTKRAGGARLPEVEIIDMRELLRGENGSF
LSPPLLEAIKQRLERGEQVLLFLNRRGYAPFLLCRDCGWVAECPHCDASLTLHRFQRRLRCHHCGYQEPI
PKACPECGSTDLVPVGPGTERLEEELAELFPEARILRIDRDTTRRKGALEQLLAQFARGEADILIGTQML
AKGHDFPNVTLVGVLDADLGLFSPDFRASERTFQLLTQVAGRAGRAEKPGEVLIQTYHPEHPVIQALLAQ
DYDAFAEQELEERRAAGYPPFGRLALLRASAKDEEKAEKFAQQLAALLPNLLPLLDVEVLGPAPAPIAKI
AGRYRYQLLLKSPSRADLQKLLRAWLALLQKLPQARKVRWSIDVDPQSF
>gnl|CDD|235515 PRK05581, PRK05581, ribulose-phosphate 3-epimerase; Validated
MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMV
ENPDRYVPDFAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSV
NPGFGGQKFIPEVLEKIRELRKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEA
IDSLRAELAA
>gnl|CDD|235517 PRK05583, PRK05583, ribosomal protein L7Ae family protein; Provisional
MMNKFLNFLGLTKKAGKLLEGYNKCEEAIKKKKVYLIIISNDISENSKNKFKNYCNKYNIPYIEGYSKEE
LGNAIGRDEIKILGVKDKNMAKKLLKLWNESQEH
>gnl|CDD|180148 PRK05584, PRK05584, 5'-methylthioadenosine/adenosylhomocysteine nucleosidase
MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDA
VINTGVAGGLAPGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKELNLNV
HRGLIASGDQFIAGAEKVAAIRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEF
LAVAAKYSANILKRMLEKLA
>gnl|CDD|235518 PRK05585, yajC, preprotein translocase subunit YajC; Validated
FFISNAYAQAAAPAGSGLSSLLPLVVFFAIFYFLIIRPQQKRQKEHKKMLSSLAKGDEVVTNGGIIGKVT
KVSEDFVIIELNDDTEIKIQKSAIAAVLPKGTLKSL
>gnl|CDD|180150 PRK05586, PRK05586, acetyl-CoA carboxylase biotin carboxylase subunit
MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISAT
VLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIEN
EEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIE
FQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDK
DGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQEDIKINGHSIECRINAEDPKNGFMP
CPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEGVNTNID
FQFIILEDEEFIKGTYDTSFIEKKLVD
>gnl|CDD|235519 PRK05588, PRK05588, histidinol phosphate phosphatase
MFDTHIHTEFSTDSKMKIEEAIKKAKENNLGIIITEHMDLNLPDKNKFCFDVDSYFNKYSKYRNNKLLLG
IELGMEKDLIEENKELINKYEFDYVIGSIHLVDKLDLYLDEFYKDKSKEEAYHIYFENMLKCLEKYDFID
SLGHIDYISRYAKYEDKEIYYDEFKEIIDEILKVLIEKEKVLEINTRRLDDKRSVENLVKIYKRFYELGG
KYITLGSDAHNIEDIGNNFKFALEIAEYCNLKPVYFKNRKPEYDK
>gnl|CDD|235520 PRK05589, PRK05589, peptide chain release factor 2; Provisional
MQEPNFWNDIKEAQEITSEEKYLKDKLDKYNHLRNRIEDIEVLCEMMSEEDDEMKKEIISEVKNIKEEID
RFKIETLLSGEYDRNNAILTLHSGVGGTDAQDWTEMLLRMYTRWAEKKGYKVEIIDLLEGDEAGIKSVTL
KITGEFAYGYLKAEKGIHRLVRISPFNANGKRQTSFASVEVLPELTDDQDIEIRSEDLKIDTYRAGGAGG
QHVNKTESAVRITHIPTGIVVQCQNERSQHSNKETAMKMLKSKLVELKERAHKEKIEDLTGELKDMGWGS
QIRSYVFHPYNLVKDHRTGVETSNVDSVMDGDIDNFITQYLKGNF
>gnl|CDD|235521 PRK05590, PRK05590, hypothetical protein; Provisional
MSLYKEWTDMVVDYVKTKGEAAFWKEYGSVEKNIYTQILANHKEVVEGTVKELAEKFGTSVVFFMGFLDG
INDSLKEPLDLEKLEEDTEVSLDIDFEKLYYNMLDAKADWLYNLPQWEAIFSEEKRKEIHKEWKKSKTVV
NENKVGRNDPCPCGSGKKYKKCCGKN
>gnl|CDD|235525 PRK05595, PRK05595, replicative DNA helicase; Provisional
MDAPIRSLPQSIEAEQSVLGAMIIDKTSIAEAAEVLKSEDFYRDSHKVIFSAIIELYQKDIAVDMLTLTE
NLKSTDKLEAAGGVTYITELSNSIVSTANIQSYIKIVKDKSTLRRLIKSSTEIIENSYNNQDDVEKVIDS
AEKKIFDISEKRTTSDFEPLSNVLERGFEQIENLFNNKGETTGVASGFRELDAKTSGFQKGDMILIAARP
SMGKTTFALNIAEYAALREGKSVAIFSLEMSKEQLAYKLLCSEANVDMLRLRTGNLEDKDWENIARASGP
LAAAKIFIDDTAGVSVMEMRSKCRRLKIEHGIDMILIDYLQLMSGGKGSESRQQEVSEISRSIKALAKEM
ECPVIALSQLSRAPEQRADHRPMLSDLRESGSIEQDADVVMFLYRDEYYNKETEDKNVAECIIAKQRNGP
TGTVKLAWLGQYSKFGNLDVIHQE
>gnl|CDD|235526 PRK05597, PRK05597, molybdopterin biosynthesis protein MoeB; Validated
VKNLDIARYRRQIMLGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHR
QVIHSTAGVGQPKAESAREAMLALNPDVKVTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAA
RLGIPHVWASILGFDAQLSVFHAGHGPIYEDLFPTPPPPGSVPSCSQAGVLGPVVGVVGSAMAMEALKLI
TGVGTPLIGKLGYYDSLDGTWEYIPVVGNPAVLERVRGSTPVHGISGGFGEVLDVPRVSALPDGVTLIDV
REPSEFAAYSIPGAHNVPLSAIREGANPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIE
GWLDS
>gnl|CDD|235527 PRK05599, PRK05599, SDR family oxidoreductase
MSILILGGTSDIAGEIATLLCHGEDVVLAARRPEAAQGLASDLRQRGATSVHVLSFDAQDLDTHRELVKQ
TQELAGEISLAVVAFGILGDQERAETDEAHAVEIATVDYTAQVSMLTVLADELRAQTAPAAIVAFSSIAG
WRARRANYVYGSTKAGLDAFCQGLADSLHGSHVRLIIARPGFVIGSMTTGMKPAPMSVYPRDVAAAVVSA
ITSSKRSTTLWIPGRLRVLAWIMRLVPRPIWRKMPR
>gnl|CDD|235528 PRK05600, PRK05600, thiamine biosynthesis protein ThiF; Validated
MALSEHTLSPFMQLPTSELRRTARQLALPGFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITL
IDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAENAVELLNGVDLVLDGSD
SFATKFLVADAAEITGTPLVWGTVLRFHGELAVFNSGPDHRGVGLRDLFPEQPSGDSIPDCATAGVLGAT
TAVIGALMATEAIKFLTGIGDVQPGTVLSYDALTATTRSFRVGADPARPLVTRLRPSYEAARTDTTSLID
ATLNGSATLLDVREPHEVLLKDLPEGGASLKLPLSAITDDADILHALSPIDGDNVVVYCASGIRSADFIE
KYSHLGHELTLHNLPGGVNA
>gnl|CDD|235529 PRK05601, PRK05601, DNA polymerase III subunit epsilon; Validated
MNQSGPDRAPSGNSGGTNADTMSTTSPSEDHAARQEAARQEAIEAAPFVAVSIQTSGIHPSTSRLITIDA
VTLTADGEEVEHFHAVLNPGEDPGPFHLHGLSAEEFAQGKRFSQILKPLDRLIDGRTLILHNAPRTWGFI
VSEAKRAMNAAARANRNRNRGNRRGGRGRRRQRVGHIPKPVVIVDTLATARRQGVALDDIRIRGVAHTLG
LDAPAAEASVERAQVPHRQLCREETLLVARLYFALRASGPLSSIDPEDLRADKFGLQRSIIRVDAQEAPR
TLENPGTYEPGKGLVAGMEVVVAPEITMDPDIIIQAIVRAGLAYSEKLTRQTSVVVCNQTRDLDGKAMHA
QRKGIPLLSDVAFLAAVERVKEGKKVE
>gnl|CDD|235530 PRK05602, PRK05602, RNA polymerase sigma factor; Reviewed
RMDADPDEELLARVAAGDPAAFRVLVARKLPRLLALATRMLGDPAEAEDVAQETFLRIWKQAPSWRPGEA
RFDTWLHRVVLNLCYDRLRRRREVPVEDAPDVPDPAPGPDAGLEARQRARRVEQALAALPERQREAIVLQ
YYQGLSNIEAAAVMDISVDALESLLARGRRALRAQLADLPGSEDDR
>gnl|CDD|235531 PRK05605, PRK05605, long-chain-fatty-acid--CoA ligase; Validated
IAPSQEMSAFADKPWLQSYAPWTPHDLDYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRA
AAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVA
PTVERLRRTTPLETIVSVNMIAAMPLLQRLALRLPIPALRKARAALTGPAPGTVPWETLVDAAIGGDGSD
VSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGPERVLAALPMFHAYGLTLC
LTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPV
STVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDPDETMPDGEEGEL
LVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREH
PGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR
REVREELLEKLGA
>gnl|CDD|235532 PRK05610, rpsQ, 30S ribosomal protein S17; Reviewed
EERMPRKTLQGRVVSDKMDKTIVVLVERRVKHPLYGKIVKRSKKYHAHDENNEAKIGDVVRIMETRPLSK
TKRWRLVEIVEKAV
>gnl|CDD|180163 PRK05611, rpmD, 50S ribosomal protein L30; Reviewed
MKTLKITLVKSLIGRKPKQRATLRGLGLRKINSTVELEDTPAIRGMINKVSHLVKVEEV
>gnl|CDD|168128 PRK05613, PRK05613, O-acetylhomoserine/O-acetylserine sulfhydrylase
MPKYDNSNADQWGFETRSIHAGQSVDSDTSARNLPIYQTTSYVFDSAEHAKQRFALEDLGPIYSRLTNPT
VEALENRIASLEGGVHAVAFASGQAAETAAILNLAGAGDHIVTSPRLYGGTETLFLVTLNRLGIEVTFVE
NPDDPESWQAAVQPNTKAFFGETFANPQADVLDIPAVAEVAHRNQVPLIVDNTIATAALVRPLELGADVV
VASLTKFYTGNGSGLGGVLIDGGKFDWTVERDGKPVFPYFVTPDPAYHGLKYADLGAPAFGLKARAGLLR
DTGATLSPFNAWVTAQGLDTLSLRLERHNENAIKVAEFLNNHEKVAKVNFAGLKDSPWYATKEKLGLKYT
GSVLSFDIKGGKDEAWAFIDALKLHSNLANIGDVRSLVVHPATTTHSQSDEAGLARAGITQATVRLSVGI
EDIDDIIADLEGGFAAI
>gnl|CDD|180164 PRK05614, gltA, citrate synthase
MADKKATLTLNGGEASVELPILKGTLGPDVIDIRKLYGSTGYFTYDPGFTSTASCESKITYIDGDKGILL
YRGYPIEQLAEKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGV
VGALSAFYHDSLDINDPEHREIAAIRLIAKMPTLAAMAYKYSIGQPFVYPRNDLSYAENFLRMMFATPCE
EYEVNPVLVRALDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEE
IGSVDNIPEFIARAKDKNDGFRLMGFGHRVYKNYDPRAKIMRETCHEVLKELGLNDPLLEVAMELEEIAL
NDEYFIERKLYPNVDFYSGIILKALGIPTSMFTVIFALARTVGWIAHWNEMHSDPEQKIGRPRQLYTGY
>gnl|CDD|235533 PRK05617, PRK05617, 3-hydroxyisobutyryl-CoA hydrolase; Provisional
TEDEVLAEVEGGVGVITLNRPKALNALSLEMIRAIDAALDAWEDDDAVAAVVIEGAGERGFCAGGDIRAL
YEAARAGDPLAADRFFREEYRLNALIARYPKPYIALMDGIVMGGGVGISAHGSHRIVTERTKMAMPETGI
GFFPDVGGTYFLSRAPGALGTYLALTGARISAADALYAGLADHFVPSADLPALLDALISLRWDSGADVVD
AALAAFATPAPASELAAQRAWIDECFAGDTVEDIIAALEADGGEFAAKTADTLRSRSPTSLKVTLEQLRR
ARGLTLEECLRRELRLALAMLRSPDFVEGVRAVLIDKDRNPKWSPATLEDVTPEDVEAFFAP
>gnl|CDD|235534 PRK05618, PRK05618, 50S ribosomal protein L25/general stress protein Ctc; Reviewed
METITLEAEVREEFGKGAARRLRRAGKVPAVIYGKGKEPVSISVDEKELIKALKKGAFLSTLLDLEVGGK
KQKVLVKDVQRHPVKDFILHVDFLRVDAGEKVKVEVPVHFVGEAKGVGVKLGGVLNQVLHELEVECLPED
IPEFIEVDVSGLEIGDSIHVSDLKLPEGVKLLDDPDEVVATVVAPRGEEEEEEEEAA
>gnl|CDD|180167 PRK05620, PRK05620, long-chain fatty-acid--CoA ligase
MLSTMQDVPLSLTRILEYGSTVHGDTTVTTWGGAEQEQTTFAAIGARAAALAHALHDELGITGDQRVGSM
MYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKECPCVRAVVF
IGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQS
LSLRTTDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVP
TLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSG
EARWAYRVSQGRFPASLEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEGGGAASTFRGEDVE
DANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDK
WGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLADGDF
EIIKLKGPGESGESDS
>gnl|CDD|235535 PRK05621, PRK05621, F0F1 ATP synthase subunit gamma; Validated
MASLKEIRRRIKSVKNTQKITKAMEMVAASKLRKAQERAEASRPYAEKIRKVISHLASASEYDHPLLVER
EVKRVGYIVVTSDRGLCGGYNSNIIKKVLELIKELEAQGKEVKLIVIGRKGVDFFKRRGINVVAEYTGLG
DQPTFEEAIGIAKKLLDAYDNGEFDELYIVYNKFVNTLSQEPTVEQLLPLEKEEEEEETSWDYEYEPDAE
EILDALLPRYVESQIYQALLENKASEQAARMTAMKNATDNAGDLIKKLTLVYNRARQAAITQEITEIVGG
AEAL
>gnl|CDD|180169 PRK05625, PRK05625, 5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated
MRPYVIVNAAMSADGKLATKTRYSRISGPEDFDRVHELRAEVDAVMVGIGTVLADDPSLTVHRYAAGKPE
NPIRVVVDSSARTPPDARILDGPAKTIVAVSEAAPSEKVEELEKKGAEVIVAGGERVDLPDLLEDLYERG
IKRLMVEGGGTLIWSMFKEGLVDEVRVTVGPKIIGGKDAPTLADGEGFIEEEDPLKLELAKVCRCDEGVV
LTYKVKK
>gnl|CDD|180170 PRK05626, rpsO, 30S ribosomal protein S15; Reviewed
MSLTKEKKAEIIKEYGRHEGDTGSPEVQVALLTERINHLTEHLKEHKKDHHSRRGLLKMVGQRRKLLDYL
KKKDVERYRALIERLGLRR
>gnl|CDD|235536 PRK05627, PRK05627, bifunctional riboflavin kinase/FAD synthetase
QLIRGLHNIPQPPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLT
PLRDKAELLAELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEA
GKEFGFEVTIVPEVKEDGERVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLP
LPDRVLPADGVYAVRVKVDGKPYPGVANIGTRPTVDGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQ
KFDSLDELKAQIAKDIETARAFLAL
>gnl|CDD|180173 PRK05629, PRK05629, hypothetical protein; Validated
PGSVQPPVHLVLGDDEFLAERARLNIVHDIRSSMADSLQVTTLKASEVSQGELLDALSPSLFGEDRVIVL
TNMEQAGKEPTDLALSAAVDPSPGIYLIIMHSGGGRTKSMVPKLEKIAVVHEAAKLKPRERPGWVTQEFK
NHGVRPTPDVVHALLEGVGSDLRELASAISQLVEDTQGNVTVEKVRAYYVGVAEVSGFDIADLACAGQVS
KAVASTRRALQLGVSPVALAAALSMKVGQIARLYSTRGRIDSFELAKELGMPPFVVEKTAKVARNWSGDA
VSEAVILMADLDAAVKGQGGDPEFAIESAVRRVAELAR
>gnl|CDD|235537 PRK05632, PRK05632, phosphate acetyltransferase; Reviewed
MSRSIYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIAQPPLTMSEVEALLASGQLDELLEEIVARY
HALAKDCDVVLVEGLDPTRKHPFEFSLNAEIAKNLGAEVVLVSSGGNDTPEELAERIELAASSFGGAKNA
NILGVIINKLNAPVDEQGRTRPDLSEIFDDSSKANVDPSKLFASSPLPLLGVVPWSPDLIAPRVIDIAKH
LGATVLNEGDILTRRVKSVTVCARSIPNMLEHLKPGSLVVTPGDRSDVILAALLAAMNGPPIAGLLLTGG
YEPDPRIAKLCEGAFETGLPVLSVDTNTYQTALRLQSFNGEVPVDDHERIETVLELVASHVDTDELLERL
TATSERSRRLSPPAFRYQLTERARAAKKRIVLPEGDEPRTLKAAAICLERGIADCVLLGNPEEIRRVAAA
QGVDLPAGIEIIDPSEVRERYVAPLVELRKHKGMTEEVAREQLEDNVYFGTMMLALGEVDGLVSGAVHTT
ANTIRPALQLIKTAPGSSLVSSVFFMLLPDQVLVYGDCAVNPDPTAEQLAEIAIQSADSAAAFGIEPRVA
MLSYSTGTSGSGADVEKVREATRLARERRPDLLIDGPLQYDAAVDPSVARSKAPNSPVAGRATVFIFPDL
NTGNTTYKAVQRSAGAVSIGPMLQGLRKPVNDLSRGALVDDIVNTIAITAIQAQ
>gnl|CDD|235538 PRK05634, PRK05634, nucleosidase; Provisional
MSMTRVLVVSATKEEAVYVPAGLPLLITGIGKVAAAVALTRALARRGVLPPRVVNIGTAGALRDGLSGVF
EPSHVINHDFSSDLIRALTGHPVANRLELPTGDGAVLATGDAFISDTATRDRLAQRADLVDMEGYAVAAV
AAEFGVPCRLVKHVSDSADESALGSWPEAVDASARELGEWLAEHV
>gnl|CDD|180177 PRK05636, PRK05636, replicative DNA helicase; Provisional
MSDMHGASFDDDYVPPPEPSDADDAHVDVPAPAFEDFSPAQAFGQGTRGGDRRGFKRREESREYRDFRQP
PYDNEAEQGVLGAMLLSPDTVIDIVEVLTPEDFYRPAHQLIFQAIIDLFSDNKEIDPVIVAGRLDRTNDL
ERVGGAPYLHTLIQSVPTAANARYYAEIVSEKAVLRRLVDAGTRVVQLGYEGDEGAEIDSVIDRAQQEVF
AVSQKNQSEDYAVLADILDPTMDELEMLSSQGGIATGIPTGFKDLDDLTNGLRGGQMIIVAARPGVGKST
LALDFMRSASIKHNKASVIFSLEMSKSEIVMRLLSAEAEVRLSDMRGGKMDEDAWEKLVQRLGKIAQAPI
FIDDSANLTMMEIRSKARRLKQKHDLKLIVVDYLQLMSSGKRVESRQQEVSEFSRQLKLLAKELDVPLIA
ISQLNRGPESRTDKRPQLADLRESGSLEQDADMVMLLYRPDSQDKDDERAGEADIILAKHRGGPIDTVQV
AHQLHYSRFVDMARG
>gnl|CDD|180178 PRK05637, PRK05637, anthranilate synthase component II; Provisional
MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRT
LGQIPLLGICLGFQALLEHHGGKVEPCGPVHGTTDNMILTDAGVQSPVFAGLATDVEPDHPEIPGRKVPI
ARYHSLGCVVAPDGMESLGTCSSEIGPVIMAAETTDGKAIGLQFHPESVLSPTGPIILSRCVEQLLAN
>gnl|CDD|235539 PRK05638, PRK05638, threonine synthase; Validated
KMKCPKCGREYNSYIPPFCICGELLEIIYDYSSVDVRKWKNRDPGVWRYKELLPQVKKIISLGEGGTPLI
RARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFV
VVPRKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEI
NPTHVIVPTGSGSYLYSIYKGFKELLEIGVIEEIPKLIAVQTERCNPIASEILGNKTKCNETKALGLYVK
NPVMKEYVSEAIKESGGTAVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEGYIEKGDKVVLV
VTGSGLKGYGEGGREKFTIGGTKLEILKILSEREMYGYEIWKALGKPLKYQAVYQHIKELEELGLIEEAY
RKGRRVYYKLTEKGRRLLENLE
>gnl|CDD|168145 PRK05639, PRK05639, acetyl ornithine aminotransferase family protein
MEYPKIVVKPPGPKAKELIEREKRVLSPGIGVKLFPLVPKRGFGALIEDVDGNVFIDFLAGAAAASTGYS
HPKLVKAVQEQVALIQHSMIGYTHSERAIRVAEKLAEISPIENPKVLFGLSGSDAVDMAIKVSKFSTRRP
WILAFIGAYHGQTLGATSVAAFQSSQKRGFSPLMPNVVWIPYPNPYRNPWGINGYEEPDELINRFLDYLE
NYVFSHVVPPDEVAALFAEPIQGDAGIVVPPENFFKELKKLLDEHGILLVMDEVQTGIGRTGKWFASEWF
EVKPDLIIFGKGVASGMGLSGVIGRKELMDLTSGSALLTPAANPVISAAAEATLEIIEEENLLKNALKVG
EFIKKRLLEMKESFEVIGDVRGKGLMIGVEIVKENGKPDPELTGKICWRAFELGLILPSYGMFGNVIRIT
PPLVITKEIAEKGLEIMERAIKDALAGKVERKVVTWH
>gnl|CDD|101884 PRK05640, PRK05640, putative monovalent cation/H+ antiporter subunit B; Reviewed
MLGIILGIIAVTLALIVVLHRDFLASLISYSLASLLFALLAMLFRAPDVALSLIVVGGIVIGLFIFAYEE
TREEIKIDLPLGLAVIPLALALLRTRITVNSLSYEAYLKAWNIGNLVSEILAGWRLYDSVGEALILFSAA
LGFSLLVRGVK
>gnl|CDD|235540 PRK05641, PRK05641, putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
MMKVKVIVDGVEYEVEVEELGPGKFRVSFEGKTYEVEAKGLGIDLSAVQEQVPTPAPAPAPAVPSAPTPV
APAAPAPAPASAGENVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEG
DTVDTGQPLIELG
>gnl|CDD|235541 PRK05643, PRK05643, DNA polymerase III subunit beta; Validated
MKFTISRNALLKALQLVQGAVERRNTIPILSNVLIEAEGGKLSLTATDLEISIETTIPAEVEVEEGSITV
PAKKLLDIVRKLPDGAEITLELEENNRLTIKSGKSRFNLPTLPAEDFPNLPEIEEEVSFTLPQKTLKRLI
EKTQFAMSTQETRYYLNGVLLEIEGNELRAVATDGHRLAVRKLELEEGSLGDFSVIIPRKTLLELQKLLD
DEEPVEIFISDNQILFEFGNTIFTSKLIDGKFPDYRRVIPKEFDKKLTVDRKELLQALERASILSNEKSR
GVKLSLSEGQLKISANNPEQGEAEEELEVEYSGEELEIGFNVKYLLDVLKALDSEEVRLSFNDANSPFLI
RPPDDDSFLYVIMPMRL
>gnl|CDD|235542 PRK05644, gyrB, DNA gyrase subunit B; Validated
KEEKAQEYDASQIQVLEGLEAVRKRPGMYIGSTGERGLHHLVYEIVDNSIDEALAGYCDHIEVTINEDGS
ITVTDNGRGIPVDIHPKTGKPAVEVVLTVLHAGGKFGGGGYKVSGGLHGVGVSVVNALSTWLEVEVKRDG
KIYYQEYERGVPVTPLEVIGETDETGTTVTFKPDPEIFETTEFDYDTLATRLRELAFLNKGLKITLTDER
EGEEKEETFHYEGGIKEYVEYLNRNKEPLHEEPIYFEGEKDGIEVEVAMQYNDGYSENILSFANNINTHE
GGTHEEGFKTALTRVINDYARKNKLLKEKDDNLTGEDVREGLTAVISVKHPEPQFEGQTKTKLGNSEVRG
IVDSVVSEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKSALESSSLPGKLADCSSKDPEE
SELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIGDDFDISKL
RYHKIIIMTDADVDGAHIRTLLLTFFYRYMRPLIEAGYVYIAQPPLYKIKKGGKEYAYSDEELDEILAEL
KLKGNPKYGIQRYKGLGEMNPEQLWETTMDPETRTLLQVTIEDAAEADEIFSILMGDDVEPRREFIEENA
KYVRNLDI
>gnl|CDD|135493 PRK05645, PRK05645, lysophospholipid acyltransferase
MEKFKGALMVGALRLFALLPWRAVQGVGAGIGWLMWKLPNRSREVVRINLSKCFPELSPAELEKLVGQSL
MDIGKTLTESACAWIWPPQKSLELVREVEGLEVLEQALASGKGVVGITSHLGNWEVLNHFYCSQCKPIIF
YRPPKLKAVDELLRKQRVQLGNRVAPSTKEGILSVIKEVRKGGQVGIPADPEPAESAGIFVPFLGTQALT
SKFVPNMLAGGKAVGVFLHALRLPDGSGYKVILEAAPEDMYSTDVEVSAAAMSKVVERYVRAYPSQYMWS
MKRFKKRPAGEARWY
>gnl|CDD|235543 PRK05646, PRK05646, lipid A biosynthesis lauroyl acyltransferase; Provisional
MDRPRFRAAFLHPRFWPLWLGLGLLWLVVQLPYRVLLWLGRALGALMYRLAGSRRRIAARNLELCFPEKS
AAERERLLKENFASTGIAFFEMAMSWWWPKARLARLAHIEGLEHLQQAQQEGQGVILMALHFTTLEIGAA
LLGQQHTIDGMYREHKNPVFDFIQRRGRERHNLDSTAIEREDVRGMLKLLRAGRAIWYAPDQDYGAKQSI
FVPLFGIPAATVTATTKFARLGRARVIPFTQKRLADGSGYRLVIHPPLEDFPGESEEADCLRINQWVERV
VRECPEQYLWAHRRFKSRPEGEPKLYPKRR
>gnl|CDD|235545 PRK05650, PRK05650, SDR family oxidoreductase
NRVMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQA
CEEKWGGIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGL
MQGPAMSSYNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNLLDSFRGPNPAMKAQVGKLLEKSPI
TAADIADYIYQQVAKGEFLILPHEQGRRAWQLKRQAPQALYDEMTLMATKMRAKSQRKAN
>gnl|CDD|235546 PRK05653, fabG, 3-oxoacyl-ACP reductase FabG
MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVR
ALIEAAVEAFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNIS
SVSGVTGNPGQTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLG
RLGQPEEVANAVAFLASDAASYITGQVIPVNGGMYM
>gnl|CDD|168156 PRK05656, PRK05656, acetyl-CoA C-acetyltransferase
MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAA
IKAGLPHSVPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLV
DSMITDGLWDAFNDYHMGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGE
PLAFATDEQPRAGTTAESLAKLKPAFKKDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYA
NAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHP
IGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIERD
>gnl|CDD|235548 PRK05657, PRK05657, RNA polymerase sigma factor RpoS; Validated
MTLKVHDLNEDADFDENGVEVFDEKALVEEEPSDNDLAEEELLSQGATQRVLDATQLYLNEIGYSPLLTA
EEEVYFARRALRGDFAARQRMIESNLRLVVKIAKRYLNRGLALLDLIEEGNLGLIRAVEKFDPERGFRFS
TYATWWIRQTIERAIMNQTRTIRLPVHVVKELNVYLRAARELEHKLDHEPSAEEIAELLDKPVDDVSRML
ALNERITSLDTPLGGDPEKSLLDILADEQENGPEDTTQDDDMKQSIVKWLFELNDKQREVLARRFGLLGY
EAATLEDVAREIGLTRERVRQIQVEALRRLREILQTQGLSIEALF
>gnl|CDD|235549 PRK05658, PRK05658, RNA polymerase sigma factor RpoD; Validated
GDSPMLDNPQSQLKKLIKRGKERGYLTYAELNDHLPEDIVDSEQIEDIIAMLNDMGIQVVEEAPDADDLL
LAENEADAQTDEDAEEEAAAALSSVESEIGRTDDPVRMYLREMGTVELLTREGEIEIAKRIEAGENIMIA
ALCESPLTIDAILEWYDRLENGERRLRELIDGFVDPNAEEDPAHVGSELEELDDDEDEEEEEDENDDSLA
ADESELPEKVLEKFKALAKQYKKLRKAQEKKVEGRLAQHKKYAKLREKLKEELKSLRLTSKQIDELVEQL
RDINKRVRGQERELLRLVERLKMPRKDFLKLFQGNELDITWLEKEIASGKPWSEFLVRVYDEIKKLQQEL
EAIEEETGLTIEELKEINRQISKGEAKARRAKKEMVEANLRLVISIAKKYTNRGLQFLDLIQEGNIGLMK
AVDKFEYRRGYKFSTYATWWIRQAITRSIADQARTIRIPVHMIETINKLNRISRQMLQEIGREPTPEELA
ERLGMPEDKVRKVLKIAKEPISLETPIGDDEDSHLGDFIEDKNAELPIDAAIQESLREATTDVLASLTPR
EAKVLRMRFGIDMNTDHTLEEVGKQFDVTRERIRQIEAKALRKLRHPSRSRKLRSFLDN
>gnl|CDD|168162 PRK05665, PRK05665, amidotransferase; Provisional
MSLRICILETDVLRPELVAQYQGYGRMFEQLFARQPIAAEFVVYNVVQGDYPADDEKFDAYLVTGSKADS
FGTDPWIQTLKTYLLKLYERGDKLLGVCFGHQLLALLLGGKAERASQGWGVGIHRYQLAAHAPWMSPAVT
ELTLLISHQDQVTALPEGATVIASSDFCPFAAYHIGDQVLCFQGHPEFVHDYSRALLDLRQEHLGEEVYS
KGVASLAHDHQGTTVAEWMMRFVAQKPTAA
>gnl|CDD|235552 PRK05670, PRK05670, anthranilate synthase component II; Provisional
MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFA
GKVPILGVCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDC
LEVTAWTDDGEIMGVRHKELPIYGVQFHPESILTEHGHKLLENFLELAR
>gnl|CDD|168165 PRK05671, PRK05671, aspartate-semialdehyde dehydrogenase; Reviewed
MSQPLDIAVVGATGTVGEALVQILEERDFPVGTLHLLASSESAGHSVPFAGKNLRVREVDSFDFSQVQLA
FFAAGAAVSRSFAEKARAAGCSVIDLSGALPSAQAPNVVPEVNAERLASLAAPFLVSSPSASAVALAVAL
APLKGLLDIQRVQVTACLAVSSLGREGVSELARQTAELLNARPLEPRFFDRQVAFNLLAQVGAPDAQGHT
ALERRLVAELRQLLGLPELKISVTCIQVPVFFGDSLSVALQSAAPVDLAAVNAALEAAPGIELVEAGDYP
TPVGDAVGQDVVYVGRVRAGVDDPCQLNLWLTSDNVRKGAALNAVQVAELLIKHYL
>gnl|CDD|235553 PRK05672, dnaE2, error-prone DNA polymerase; Validated
MLPPYAELHCHSNFSFLDGASHPEELVERAARLGLRALAITDECGLAGVVRAAEAAKELGLRLVIGAELS
LGPDPDPGGPHLLVLARDREGYGRLSRLITRARLRAGKGEYRLDLDDLAEPAGGHWAILTGCRKGFVILA
LPYGGDAAALAALAALLDAFFADRVWLELTLHGRPDDDRRNARLAALAARAGVPLVATGDVHMHHRSRRR
LQDAMTAIRARRSLAEAGGWLAPNGERHLRSGAEMARLFPDYPEALAETVELAERCAFDLDLLAYEYPDE
PVPAGHTPASWLRQLTEAGAARRYGPGIPPKARAQIEHELALIAELGYEGYFLTVHDIVRFARSQGILCQ
GRGSAANSAVCYALGITEVDPVQSGLLFERFLSPERDEPPDIDVDFEHDRREEVIQYVYRRYGRDRAAQV
ANVITYRPRSAVRDVAKALGLSPGQVDAWAKQVSRWSGSADDLQRLRQAGLDPESPIPRRVVELAAQLIG
FPRHLSQHSGGFVICDRPLARLVPVENAAMEGRSVIQWDKDDCAAVGLVKVDVLALGMLSALHRAFDLIA
EHRGRRLTLASIPLDDPAVYDMLCRADSVGVFQVESRAQMAMLPRLRPRTFYDLVVEVAIVRPGPIQGGM
VHPYLRRRNGQEPVTYPHPELEKVLERTLGVPLFQEQVMQIAIDAAGFTPGEADQLRRAMAAWRRKGRLE
RLRERLYDGMLARGYTGEFADRIFEQIKGFGEYGFPESHAASFAKLVYASSWLKCHHPAAFCAALLNSQP
MGFYSPQQLVQDARRHGVEVLPVDVNASGWDATLEPLPDGGPAVRLGLRLVRGLGEEAAERIVAARARGP
FTSVEDLARRAGLDRRQLEALADAGALRSLGGDRRQALWAAGAAATERLDLLPGAPASEAAPALPGMSEG
ELVAADYWTTGLSLDSHPLALLRPRLDARGVVSAAELLDVEDGRRVRVAGVVTHRQRPGTASGVTFLTLE
DETGMVNVVVWPGLWERQRREALGARLLLVRGRVQNAEGVRHLVADRLEDLSPLLGGLRTRSRDFH
>gnl|CDD|235554 PRK05673, dnaE, DNA polymerase III subunit alpha; Validated
RFVHLHVHSEYSLLDGAAKIKPLVKKAAELGMPAVALTDHGNLFGAVEFYKAAKGAGIKPIIGCEAYVAP
EKKDDVSGGGAYTHLTLLAKNETGYRNLFKLSSRAYLEGQYGYKPRIDREWLAEHSEGLIALSGCPSGEV
GTALLAGQYDEAEEAAAEYQEIFGDRFYLELMRHGLPIERRVEHALLELAKELGLPLVATNDVHYLTPED
AEAHEALLCIAEGKTLDDPDRFRFYSPEQYLKSAEEMRELFADLPEALDNTVEIAERCNVEVRLGKPFLP
RFPTPDGETEEDYLRKEAKEGLEERLAFLFPDEERPEYVERLEYELDVIIQMGFPGYFLIVADFIQWAKD
NGIPVGPGRGSGAGSLVAYALGITDLDPLRFGLLFERFLNPERVSMPDFDIDFCQDRRDEVIRYVAEKYG
RDAVAQIITFGTMKAKAVIRDVGRVLGMPYGFVDRITKLIPPDPGITLAKAYEEEPELRELYESDPEVKR
LIDMARKLEGLTRNAGVHAAGVVISPTPLTDFVPLYRDPDSGMPVTQFDMKDVEAAGLVKFDFLGLRTLT
IIDDALKLIKKRRGIDVDLEAIPLDDPKTYELLQRGETLGVFQLESRGMRDLLKRLKPDCFEDIIALVAL
YRPGPMESGMIPNFIDRKHGREEIEYPHPELEPILKETYGIIVYQEQVMQIAQVLAGYSLGGADLLRRAM
GKKKPEEMAKQREIFVEGAKKNGIDEEAADAIFDLLEKFAGYGFNKSHAAAYALVSYQTAYLKAHYPAEF
MAALLTSDMDNTDKVAVYLDECRRMGIKVLPPDVNESLYDFTVVDGDIRYGLGAIKGVGEGAVEAIVEAR
EEGGPFKDLFDFCARVDLKKVNKRVLESLIKAGAFDSLGPNRAALLASLEDAVDAADQHKKAEASGQFDL
FGGLGEEPEDVEVSVPDVEEWDKKEKLAGERETLGLYLSGHPLDGYEDELRRLRDTRLADLEPTEGGSVV
TVAGLVVSVRRRVTKRGNKMAIVTLEDLSGRIEVMLFSEALEKYRDLLEEDRIVVVKGQVSFDDGGLRLT
AREVMDLEEARAKYARPLRISLPDRQLTPQLLERLKQVLEPHRGTSPVHLYLQDPDAEAELRLGDRWRVT
PSDALLGDLKALLGV
>gnl|CDD|168168 PRK05674, PRK05674, gamma-carboxygeranoyl-CoA hydratase; Validated
MSDFQTIELIRDPRGFATLWLSRADKNNAFNAQMIRELILALDQVQSDASLRFLLLRGRGRHFSAGADLA
WMQQSADLDYNTNLDDARELAELMYNLYRLKIPTLAVVQGAAFGGALGLISCCDMAIGADDAQFCLSEVR
IGLAPAVISPFVVKAIGERAARRYALTAERFDGRRARELGLLAESYPAAELEAQVEAWIANLLLNSPQAL
RASKDLLREVGDGELSPALRRYCENAIARIRVSAEGQEGLRAFLEKRTPAWQTDA
>gnl|CDD|168170 PRK05677, PRK05677, long-chain-fatty-acid--CoA ligase; Validated
MIENFWKDKYPAGIAAEINPDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHT
DLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVL
PKTGVKHVIVTEVADMLPPLKRLLINAVVKHVKKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVA
VLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHN
ILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVT
GCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQ
RPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVP
DEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAG
LK
>gnl|CDD|180194 PRK05678, PRK05678, succinyl-CoA synthetase subunit alpha; Validated
MSILINKDTKVIVQGITGKQGTFHTEQMLAYGTNIVGGVTPGKGGTTVLGLPVFNTVAEAVEATGANASV
IYVPPPFAADAILEAIDAGIDLIVCITEGIPVLDMLEVKAYLERKKTRLIGPNCPGIITPGECKIGIMPG
HIHKKGRVGVVSRSGTLTYEAVAQLTDLGFGQSTCVGIGGDPINGTNFIDVLEAFEEDPETEAIVMIGEI
GGSAEEEAAEYIKANVTKPVVGYIAGVTAPPGKRMGHAGAIISGGKGTAEEKKEALEAAGVKVARTPSEI
GELLKEVLKGL
>gnl|CDD|235555 PRK05679, PRK05679, pyridoxal 5'-phosphate synthase
RADLPAEPLALFERWLAEAVKAELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQL
AANPKAALLFPWKSLERQVRVEGRVEKVSAEESDAYFASRPRGSQIGAWASKQSRPISSRAALEAKFAEV
KAKFAQGEVPRPPHWGGYRVVPESIEFWQGRPSRLHDRILYRRDDGGWKIERLAP
>gnl|CDD|235556 PRK05681, flgC, flagellar basal body rod protein FlgC; Reviewed
MSLFSSFNIAGSGLSAQSQRLNVISSNIANADSTAAPDGDPYRRKQVVFAAELDPGQGTGGVKVAKIVED
QSPFKLVYDPGHPAADAKGYVKYPNVNVVVEMVDMISASRSYEANVEVLNAAKSMMQKTLTIGQS
>gnl|CDD|235557 PRK05682, flgE, flagellar hook protein FlgE; Validated
MSFNTAVSGLNAASNRLDVIGNNIANANTTGFKSSRAEFADLYANSAGTNPTQVGSGVKVAGVAQQFSQG
SITSTGNSLDLAISGNGFFVVSNGGNGFYTRAGAFKLDKNGYLVNAAGYYLQGYPADADGGTPPTVGAGL
VPLNIPTTALAPKATTSGTFQGNLPSTAAFDPTDPDTYNHSTSLTVYDSLGNSHTLDVYFVKTGDNTWEV
YVYDDGKPVSTTATGTGTTTLTFDSNGALTTTTSPTTFNITGGATNGADGGQTITLDLSGSTQYASGFTV
SATTQDGYAPGTLTGYSIDDDGTVTAVYSNGQTKPLGQIALANFANPDGLTKVGGNVWSATAASGVALIG
TAGSGGFGTIQSGALESSNVDLSTELVNMIVAQRNYQANAKTIKTQDQLLQTLVNLR
>gnl|CDD|235558 PRK05683, flgK, flagellar hook-associated protein FlgK; Validated
MSLISIGLSGLGASQTALAVTGNNIANVDTAGYSRQQTVQTTKASQQSGAGYIGTGTTLADVRRIYNSFL
DTQLRTATSLNSDASAYLGQISQLDKLLSDSTTGISPALQRFFTALQTAAANPTDTAARQLLLTQAQGLS
KRFNSLSSQLNQQNSNINSQLSAMTDQVNNLTTSIASYNKQIAQASASGATPNDLLDARDEAVRQLNELV
GVTVVERDGNYDVYIGSGQPLVVGNTANTLSVVPGPSDPSRYNVQLNRGSSTQDVTSVVSGGEIGGLLRY
RSDVLDPAMNELGRLALVVADQINSQLGQGIDLNGNFGSSLFGDINSADAISQRSLAKNGNSAGSGNLNV
TIKDTSKLTTSDYEVTFTSATNYTVRRLSDGTDMGSFDLSDNPAPVIDGFSLSLNGGTLAAGDSFKVTPT
RNAASDIETVLTDPKKLAFAAPLTAEAGSGNSGTGSITQPTLTSKLDIYDPAQTADLQNAIKNSTPVKLV
FGADSSGPQSYTLVDAKGNAIGSGTIVPGQSNTLTLAVPMPDASGNPINDATFTFEMTISGSPQAGDSFT
VSFNGAGSSDNRNALALLGLQTKSTVGVGSGGKGTSLTDAYGKLVERVGTLASQARADATATAAVLKQAK
DSRDSLSGVSLDEEAANLIKFQQYYTASSQIIKAAQETFSTLINAL
>gnl|CDD|235559 PRK05684, flgJ, flagellar assembly peptidoglycan hydrolase FlgJ
MSDSLSDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYT
SMYDQQIAQQLSAGGGLGLADMMVKQLSPEQSPAPEESAGAVPMKFDLETVQSYQNQALAQLVRKAIPQP
PLASDKPLFGSSDDFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADG
SWKGPVTEITTTEYENGVAVKVKAAFRVYDSYLESFNDYVSLLTNNPRYAAVTQAASPEQFARALQDAGY
ATDPNYARKLVSVIQQMKSMGEKVSKAYSHDL
>gnl|CDD|235561 PRK05686, fliG, flagellar motor switch protein G; Validated
DAEKAKADLDELTGPEKAAILLLALGEEAAAKVLKHLTEEEVQKLSAAMANLRNVSPEQVEAVLEEFEDE
FEAGAYILMGGIDYARSLLEKALGEEKADSILERILESLGTSGFDFLRKMDPQQLANFIRNEHPQTIALI
LSYLKPDQAAEILSLLPEELRADVMMRIATLEGVSPEALKEVEEVLEKKLSSMANADRTKMGGVKTVAEI
LNNLDRQTEKTILESLEEEDPELAEKIKDLMFVFEDLVDLDDRSIQRLLREVDNDVLALALKGASEELRE
KFLSNMSKRAAEMLREDLEALGPVRLSDVEEAQKKIVQIARRLAEAGEIVLGGGDDEIV
>gnl|CDD|235562 PRK05687, fliH, flagellar assembly protein FliH
KMSPSDLIRADDLLAWQRWQLPDFDPPPEPPPPEPAAPPPEPPEPEEVPEEEAAPLTEEELEAIRQQAHE
EGFAAGKAEGRAEGYEAGYQEGLAQGLEQGLAEGQAQAAPQAAQLQALAAQFQEPLALLDSVIESRLVQL
ALELARQVIGQELKTDPSAILAAIRELLQALPMFSGKPQLRVNPDDLELVEQLLGAELSLHGWRLLADPS
LHRGGCRISAEEGDVDASLETRWQEVCRLLAPGSLW
>gnl|CDD|168181 PRK05688, fliI, flagellar protein export ATPase FliI
MRLERTSFAKRLEGYAEAISLPAQPVVEGRLLRMVGLTLEAEGLRAAVGSRCLVINDDSYHPVQVEAEVM
GFSGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTI
NPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGREVK
EFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALA
IGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRL
AEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPH
LVQFLRQGLRENVSLAQSREQLAAIFAPAAG
>gnl|CDD|235563 PRK05689, fliJ, flagella biosynthesis chaperone FliJ
MSRASALATLLDLAEKAEEQAALQLGQARQELQQAEQQLKMLEDYRLEYRQQLNDRGSAGMTSSWWINYQ
QFLQQLEKAITQQRQQLTQWTQKVDNARKYWQEKKQRLEALETLQERYQTEARLAENKREQKQMDEFAQR
AAMRKPE
>gnl|CDD|180204 PRK05690, PRK05690, molybdopterin biosynthesis protein MoeB; Provisional
MMAELSDEEMLRYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLS
NLQRQVLHDDATIGQPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLN
RACFAAKKPLVSGAAIRMEGQVTVFTYQDDEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAI
KLLTGYGEPLSGRLLLYDAMTMQFREMKLKRDPGC
>gnl|CDD|235564 PRK05691, PRK05691, peptide synthase; Validated
[encoded data, 4396 characters]
>gnl|CDD|180206 PRK05692, PRK05692, hydroxymethylglutaryl-CoA lyase; Provisional
LPKRVKIVEVGPRDGLQNEKRFIPTADKIALIDRLSAAGLSYIEVASFVSPKWVPQMADAAEVMAGIQRR
PGVTYAALTPNLKGLEAALAAGADEVAVFASASEAFSQKNINCSIAESLERFEPVAEAAKQAGVRVRGYV
SCVLGCPYEGEVPPEAVADVAERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAEFPAERLAGHFHDTY
GQALANIYASLEEGITVFDASVGGLGGCPYAPGASGNVATEDVLYMLHGLGIETGIDLDKLVRAGQFIQS
KLGRPLP
>gnl|CDD|168186 PRK05693, PRK05693, SDR family oxidoreductase
MPVVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEH
GGLDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFA
GAYCASKAAVHALSDALRLELAPFGVQVMEVQPGAIASQFASNASREAEQLLAEQSPWWPLREHIQARAR
ASQDNPTPAAEFARQLLAAVQQSPRPRLVRLGNGSRALPLLARLLPRGLLDRVLRKRFGLLRPL
>gnl|CDD|180207 PRK05696, fliL, flagellar basal body-associated protein FliL; Reviewed
MAEEEALELEDEAPKSKKKLIIIIVIGVLLALGGGGAAWFFMGSSDKAAAAAAEAAAEAAAAVKGPALYV
PMPRPFVFNVPGNGRDRLVQIKVQLMVRGSDDEELAKKHIPLIESALLMTFSSATVDQLSTPAGKEELRQ
KALASVQETLQKVTGKPVVEKVLFTGFVMQ
>gnl|CDD|235565 PRK05697, PRK05697, flagellar basal body-associated protein FliL-like protein; Validated
MKRLIAKLLILLSLALSLPAAAEAEEAPEAPKYAYYGLEPDIVTNYISDGKKLGYVKIDVELMVKDPDDL
AAVEHHDPLIRNALVELLGQQTEDKVKSLTGREEIRQECLKQVNELLEQETGKPLVVDLLFTKYIYQ
>gnl|CDD|168189 PRK05698, fliN, flagellar motor switch protein FliN
MADENDITSPEDQALADEWAAALEEAGDAGQDDIDALLGADAGAEPSGPRAPMEEFGSSPKPNEPVSLEG
PNLDVILDIPVSISMEVGSTDINIRNLLQLNQGSVIELDRLAGEPLDVLVNGTLIAHGEVVVVNEKFGIR
LTDVISPSERIKKLR
>gnl|CDD|235566 PRK05699, fliP, flagellar biosynthesis protein FliP; Reviewed
AMRRLLALALLLLALASAAAAAPLPGLNLLPGANGGQEYSLSLQLLLLLTVLSLAPAILLMMTSFTRIII
VLSLLRQALGTQQTPPNQVLIGLALFLTFFIMSPVFDKIYDDAIQPYLDEKITLEEALERAAAPLREFML
KQTREKDLALFAKLAGEPPKTPEDVPLSVLVPAFVLSELKTAFQIGFLIFLPFLIIDLVVASVLMSMGMM
MLPPVIISLPFKLLLFVLVDGWNLLVGSLVQSFGG
>gnl|CDD|235567 PRK05700, fliQ, flagellar type III secretion system protein FliQ
MTPESVMDLFREAMKVALMLAAPLLLVALVVGLVVSIFQAATQINEQTLSFIPKILAVLLTLIIAGPWML
NTLLDYTRTLFSNIPTLIG
>gnl|CDD|235568 PRK05701, fliR, flagellar type III secretion system protein FliR
LLEWVAAFFLPFVRIGALLMTMPGFSERSIPARVKLGLALALTFAVAPLLPVPDVPLFSLDLLLLVIQEI
LIGLALGLVAQILFAALQFAGQIIDMQMGLSFASVVDPTSGQQSPLLGQFLTLLALLLFLALDGHHLLIR
ALVDSFETLPIGGFLLNGNAFLLLAKALSAMFLIGLQLALPIIVLLLLVNLALGLINRTAPQLNIFVIGF
PLKITVGLLLLALILPALMPVFENLFSEAFQL
>gnl|CDD|235569 PRK05702, flhB, flagellar type III secretion system protein FlhB
MAEDDDDEKTEEPTPKKLEKAREKGQVPRSRELNTAASLLAGLVVLWFFGPSLARRLSGMLRALFSFDRE
IIFDPNDVLSLFLLLLLEALLALLPILLLLVLAALLAPVLQGGLLFSPKALKPKFSKLNPLKGLKRMFSA
QGLVELLKSLLKVLLVGGVAYFVLWSNLDELLSLAAEPLEAALGHALDLVLKLLLLVVLALLVIAAIDVP
FQRWQYLKKLKMTKQEVKDEHKQSEGDPEVKGRIRQLQREMARRRMMAAVPKADVVITNPTHYAVALKYD
RGKMAAPVVVAKGVDEVALKIREIAREHNVPIVENPPLARALYATVEIGQEIPEELYKAVAEVLAYVYQL
KRWRKGGGQ
>gnl|CDD|235570 PRK05703, flhF, flagellar biosynthesis protein FlhF
MKIKKFTAKDMREALKQIKEELGADAVILSNKKVRKGGFLGKKLVEVTAAVDEDETPKKNPVLREEKRKP
AKSILSLQALLEKRPSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKAAAESKVVQKELDELRDELK
ELKNLLEDQLSGLRQVERIPPEFAELYKRLKRSGLSPEIAEKLLKLLLEHMPPRERTAWRYLLELLANMI
PVRVEDILKQGGVVALVGPTGVGKTTTLAKLAARYALLYGKKKVALITLDTYRIGAVEQLKTYAKIMGIP
VEVVYDPKELAKALEQLRDCDVILIDTAGRSQRDKRLIEELKALIEFSGEPIDVYLVLSATTKYEDLKDI
YKHFSRLPLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVPDDIKVANPEELVRLLLGGFNKSE
PSEE
>gnl|CDD|235571 PRK05704, PRK05704, 2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase
MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVG
QVLGRIDEGAAAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGG
RVTKEDVLAALAAAAAAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEV
DMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRG
LVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGM
HKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLLDL
>gnl|CDD|180215 PRK05707, PRK05707, DNA polymerase III subunit delta'; Validated
MAEIYPWQQSLWQQLAGRGRHPHAYLLHGPAGIGKRALAERLAAALLCEAPQGGGACGSCKGCQLLRAGS
HPDNFVLEPEEADKTIKVDQVRELVSFVVQTAQLGGRKVVLIEPAEAMNRNAANALLKSLEEPSGDTVLL
LISHQPSRLLPTIKSRCQQQACPLPSNEESLQWLQQALPESDERERIELLTLAGGSPLRALQLHEQGVRE
QRARVLDGVKKLLKQQQSASQLAESWLKVPLLLLFDWFCDWAHDILRYQLTQDEEGLGLADMRKVLQYLA
QKSPQAKVLALQDWLLEQRQKVLGKANLNRQLLLEALLVQWAGLPGAG
>gnl|CDD|235572 PRK05708, PRK05708, putative 2-dehydropantoate 2-reductase
MSMTWHILGAGSLGSLWACRLARAGLPVRLILRDRQRLAAYQQAGGLTLVEQGQASLYAIPAETADAAEP
IHRLLLACKAYDAEPAVASLAHRLAPGAELLLLQNGLGSQDAVAARVPHARCIFASSTEGAFRDGDWRVV
FAGHGFTWLGDPRNPTAPAWLDDLREAGIPHEWTVDILTRLWRKLALNCAINPLTVLHDCRNGGLLEHAQ
EVAALCAELSELLRRCGQPAAAANLHEEVQRVIQATAANYSSMYQDVRAGRRTEISYLLGYACRAADRHG
LPLPRLQHLQQRLVAHLRARGLPTD
>gnl|CDD|235573 PRK05710, PRK05710, tRNA glutamyl-Q(34) synthetase GluQRS
MTMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLH
WDGPVLYQSQRHDAYRAALDRLRAQGLVYPCFCSRKEIAAAAPAPPDGGGIYPGTCRDLLHGPRNPPAWR
LRVPDAVIAFDDRLQGRQHQDLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQI
YLQQLLGLPTPRYLHLPLVLNADGQKLSKQNGAPALDAAGPLPVLAAALRFLGQPPPAADASVEELLAQA
VAHWDLTRLPRQAEINPAF
>gnl|CDD|235574 PRK05711, PRK05711, DNA polymerase III subunit epsilon; Provisional
TAIMRQIVLDTETTGLNQREGHRIIEIGAVELINRRLTGRNFHVYIKPDRLVDPEALAVHGITDEFLADK
PTFAEVADEFLDFIRGAELIIHNAPFDIGFMDYEFALLGRDIPKTNTFCKVTDTLAMARRMFPGKRNSLD
ALCKRYGIDNSHRTLHGALLDAEILAEVYLAMTGGQTSLGFAMEGETQQQQGEETIQRIVRQRSRLPVVR
ATDEELAAHEARLDLLDKKGGSCLWRKYAE
>gnl|CDD|235575 PRK05713, PRK05713, iron-sulfur-binding ferredoxin reductase
MPELRVGERRWSVPAGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEKREQGWRL
ACQCRVVGDLRVEVFDPQRDGLPARVVALDWLGGDVLRLRLEPERPLRYRAGQHLVLWTAGGVARPYSLA
SLPGEDPFLEFHIDCSRPGAFCDAARQLQVGDLLRLGELRGGALHYDPDWQERPLWLLAAGTGLAPLWGI
LREALRQGHQGPIRLLHLARDSAGHYLAEPLAALAGRHPQLSVELVTAAQLPAALAELRLVSRQTMALLC
GSPASVERFARRLYLAGLPRNQLLADVFLPHA
>gnl|CDD|168201 PRK05714, PRK05714, 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
MRADLLIVGAGMVGSALALALQGSGLEVLLLDGGPLSVKPFDPQAPFEPRVSALSAASQRILERLGAWDG
IAARRASPYSEMQVWDGSGTGQIHFSAASVHAEVLGHIVENRVVQDALLERLHDSDIGLLANARLEQMRR
SGDDWLLTLADGRQLRAPLVVAADGANSAVRRLAGCATREWDYLHHAIVTSVRCSEPHRATAWQRFTDDG
PLAFLPLERDGDEHWCSIVWSTTPEEAERLMALDDDAFCAALERAFEGRLGEVLSADPRLCVPLRQRHAK
RYVEPGLALIGDAAHTIHPLAGQGVNLGFLDAAVLAEVLLHAAERGERLADVRVLSRFERRRMPHNLALM
AAMEGFERLFQADPLPLRWLRNTGLKLVDQMPEAKALFVRQALGLSGDLPELARA
>gnl|CDD|180218 PRK05715, PRK05715, NADH-quinone oxidoreductase subunit NuoK
MIPLQHYLILAAILFCIGLVGLLLRRNAIVVLMSIELMLNAVNLNFVAFSSYLGDLDGQVFAFFVITVAA
AEAAIGLAILLQLYRNRGTIDVDDLNELKG
>gnl|CDD|235576 PRK05716, PRK05716, methionine aminopeptidase; Validated
MAITIKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRDQGAIPAPLGYHGFPKSICT
SVNEVVCHGIPSDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKP
GARLGDIGHAIQKYAEAEGFSVVREYCGHGIGRKFHEEPQIPHYGAPGDGPVLKEGMVFTIEPMINAGKR
EVKTLKDGWTVVTKDGSLSAQYEHTVAVTEDGPEILTLRPEE
>gnl|CDD|168204 PRK05717, PRK05717, SDR family oxidoreductase
MSEPNPGHNGRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAQ
VAAGVAEVLGQFGRLDALVCNAAIADPHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIV
NLASTRARQSEPDTEAYAASKGGLLALTHALAISLGPEIRVNAVSPGWIDARDPSQRRAEPLSEADHAQH
PAGRVGTVEDVAAMVAWLLSRQAGFVTGQEFVVDGGMTRKMIYLD
>gnl|CDD|235577 PRK05718, PRK05718, keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
MKNWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIG
AGTVLNPEQLAQAIEAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEAS
GGVKMLKALAGPFPDVRFCPTGGISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVAL
AK
>gnl|CDD|235578 PRK05720, mtnA, methylthioribose-1-phosphate isomerase; Reviewed
LQPRPVAWKDGAVRILDQRKLPHEVEYVELTTAEEVADAIRDMVVRGAPAIGIAAAYGMALAAREDASDD
GEEFLKKLEEAAAYLAASRPTAVNLFWALDRMREVLAPLPGAERKAALEEEAIEIHEEDVEINRAIGEHG
LTLIRKGQGILTHCNAGWLATAGYGTALAPIYAAKEKGIDIHVYADETRPRLQGARLTAWELYQAGIDVT
VITDNMAAHLMQTGKIDAVIVGADRIAANGDVANKIGTYQLAIAAKYHGVPFYVAAPSSTIDLTLADGKE
IPIEERDPEEVTEVGGVRIAPEGVKVYNPAFDVTPAELITGIITEKGIVAPPDTANLAALFPEK
>gnl|CDD|235579 PRK05722, PRK05722, glucose-6-phosphate 1-dehydrogenase; Validated
MRLPRTAEPCDLVIFGATGDLARRKLLPALYNLYKAGLLPEDFRIIGVARRDWSDEDFREVVREALKEFA
RTPFDEEVWERFLSRLYYVSGDVTDPESYERLKELLEELDEERGTGGNRVFYLATPPSLFGTICENLAAA
GLNEGGGWRRVVIEKPFGHDLASARELNDQVGEVFKEEQIYRIDHYLGKETVQNLLALRFANALFEPLWN
RNYIDHVQITVAETVGVEGRGGYYDKSGALRDMVQNHLLQLLALVAMEPPASLDADSIRDEKVKVLRALR
PITPEDVKENTVRGQYTAGWIGGKPVPGYREEEGVNPDSTTETFVALKLEIDNWRWAGVPFYLRTGKRLP
KKVTEIVIVFKPPPHNLFEESAEELGPNKLVIRIQPDEGISLRFNAKVPGEGMELRPVKLDFSYSEAFGE
ASPEAYERLLLDVMLGDQTLFVRRDEVEAAWKWVDPILEAWEADGGPPPPYPAGTWGPEAADALLARDGR
SWREP
>gnl|CDD|168208 PRK05723, PRK05723, flavodoxin; Provisional
MKVAILSGSVYGTAEEVARHAESLLKAAGFEAWHNPRASLQDLQAFAPEALLAVTSTTGMGELPDNLMPL
YSAIRDQLPAAWRGLPGAVIALGDSSYGDTFCGGGEQMRELFAELGVREVQPMLRLDASETVTPETDAEP
WLAEFAAALKG
>gnl|CDD|235580 PRK05724, PRK05724, acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
MMLNYLDFEKPIAELEAKIEELRAVAEDSDVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRP
YTLDYIELLFTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKA
LRLMKMAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGV
GDRVLMLEYSTYSVISPEGCASILWKDASKAPEAAEAMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAA
AALKEALLEALAELKGLSPEELLERRYEKFMSIGRFLES
>gnl|CDD|235581 PRK05728, PRK05728, DNA polymerase III subunit chi; Validated
MTRADFYHLTLSALEALLCELAEKALRAGWRVLVQCEDEEQAEALDEALWTFRDESFLPHGLAGEGPAAG
QPVLLTWPGKRNANHRDLLINLDGAVPAFAAAFERVVDFVGYDEAAKQAARERWKAYRAAGYALTYWQQG
ED
>gnl|CDD|235582 PRK05729, valS, valyl-tRNA synthetase; Reviewed
MMMELPKTYDPKEVEAKWYQKWEEKGYFKPDDNSKKPFSIVIPPPNVTGSLHMGHALNNTLQDILIRYKR
MQGYNTLWLPGTDHAGIATQMVVERQLAAEGKSRHDLGREKFLEKVWEWKEESGGTITNQLRRLGASCDW
SRERFTMDEGLSKAVREVFVRLYEKGLIYRGKRLVNWDPKLQTALSDLEVEYKEVKGKLWHIRYPLADGS
DYLVVATTRPETMLGDTAVAVNPEDERYKHLIGKTVILPLVGREIPIIADEYVDPEFGTGAVKITPAHDP
NDFEVGKRHNLPMINIMDEDGTINENPGEYQGLDRFEARKAIVADLEELGLLVKIEPHTHSVGHSDRSGV
VIEPYLSDQWFVKMKPLAKPALEAVENGEIKFVPERWEKTYFHWMENIQDWCISRQLWWGHRIPAWYDED
GEVYVGREEPEAREKALLTQDEDVLDTWFSSALWPFSTLGWPEKTEDLKRFYPTSVLVTGFDIIFFWVAR
MIMMGLHFTGQVPFKDVYIHGLVRDEQGRKMSKSKGNVIDPLDLIDKYGADALRFTLAALASPGRDIRFD
EERVEGYRNFANKLWNASRFVLMNLEGADVGELPDPEELSLADRWILSRLNRTVAEVTEALDKYRFDEAA
RALYEFIWNEFCDWYLELAKPVLQEAAKRATRATLAYVLEQILRLLHPFMPFITEELWQKLAPLGIEESI
MLAPWPEADEAIDEAAEAEFEWLKELITAIRNIRAEMNIPPSKKLPLLLKGADAEDRARLEANEAYIKRL
ARLESLEILADDEEAPEGAASAVVGGAELFLPLEGLIDVEAELARLEKELAKLEKEIERVEKKLSNEGFV
AKAPEEVVEKEREKLAEYEEKLAKLKERLARLKA
>gnl|CDD|235583 PRK05731, PRK05731, thiamine monophosphate kinase; Provisional
MAMGEFDLIARLFARRPSSRELGIGDDAALLGPPPGQRLVVSTDMLVEGVHFRPDWSSPEDLGYKALAVN
LSDLAAMGARPAAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTTRGPDLSISVTAIGDVPG
GRALRRSGAKPGDLVAVTGTLGDSAAGLALLLNGLRVPDADAAALISRHLRPQPRVGLGQALAGLASAAI
DISDGLAADLGHIAEASGVGADIDLDALPISPALREAAEGEDALRWALSGGEDYELLFTFPPENRGALLA
AAGHLGVGVTIIGRVTEGEGVVVDGEPVTLDLKGYDHF
>gnl|CDD|235584 PRK05732, PRK05732, 2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
MSRMDVIIVGGGMAGATLALALSRLSHGGLPVALIEAFAPESDAHPGFDARAIALAAGTCQQLARLGVWQ
ALADCATPITHIHVSDRGHAGFVRLDAEDYGVPALGYVVELHDVGQRLFALLDKAPGVTLHCPARVANVE
RTQGSVRVTLDDGETLTGRLLVAADGSHSALREALGIDWQQHPYEQVAVIANVTTSEAHQGRAFERFTEH
GPLALLPMSDGRCSLVWCHPLEDAEEVLSWSDAQFLAELQQAFGWRLGRITHAGKRSAYPLALVTAAQQI
SHRLALVGNAAQTLHPIAGQGFNLGLRDVMSLAETLTQALARGEDIGDYAVLQRYQQRRQQDREATIGFT
DGLVRLFANRWAPLVVGRNLGLMAMDLLPPARDWLARRTLGWVAR
>gnl|CDD|235585 PRK05733, PRK05733, single-stranded DNA-binding protein; Provisional
MARGVNKVILVGTCGQDPEVRYLPNGNAVTNLSLATSEQWTDKQSGQKVERTEWHRVSLFGKVAEIAGEY
LRKGSQVYIEGKLQTREWEKDGIKRYTTEIVVDMQGTMQLLGGRPQGDDQGGQGGGNYNQSAPRQQAQRP
QQAAQQQSRPAPQQPAPQPAADFDSFDDDIPF
>gnl|CDD|235586 PRK05738, rplW, 50S ribosomal protein L23; Reviewed
YDVIKRPVITEKSTLLMEKQNKYVFEVAPDATKPEIKAAVEKLFGVKVESVNTLNVKGKTKRFGRRIGKR
SDWKKAIVTLAEGQKIDFFGGA
>gnl|CDD|235587 PRK05740, secE, preprotein translocase subunit SecE; Reviewed
NYYLREQSLPVRALAVVVLIAAAGGVALLTAKGKAFFAFAKESRTEVRKVVWPTRQETLQTTLIVIAVVI
VMALILWGLDSILVWLISFITG
>gnl|CDD|180232 PRK05748, PRK05748, replicative DNA helicase; Provisional
MSEVAALRVPPQSIEAEQAVLGAIFLDPDALITVSEYLSPDDFYRHAHRLIFRAMLKLSDRGEPIDVVTV
TEILDDQGDLEEVGGLSYLAELANSVPTAANIEYYAKIVAEKAMLRRLIRTATEIANDAYEPEDDADEIL
DEAEKKIFEVSERRNKSGFKNIKDVLVKAYDRIEMLHNQTGDITGIPTGFTDLDKMTSGLQPNDLIIVAA
RPSVGKTAFALNIAQNVATKTDKNVAIFSLEMGAESLVMRMLCAEGNIDAQRLRTGQLTDDDWPKLTIAM
GSLSDAPIYIDDTPGIKVTEIRARCRRLAQEHGGLGLILIDYLQLIQGSGRSGENRQQEVSEISRSLKAL
AKELKVPVIALSQLSRGVEQRQDKRPVMSDIRESGSIEQDADIVAFLYRDDYYDEETENKNTIEIIIAKQ
RNGPVGTVELAFQKEYNKFVNLARREED
>gnl|CDD|235589 PRK05749, PRK05749, 3-deoxy-D-manno-octulosonic-acid transferase; Reviewed
MLRLLYTALLYLALPLILLRLLLRSRKAPKYRKRWGERFGFRKPNPPPKGPLIWFHAVSVGETRAAIPLI
RALRKRYPDLPILVTTMTPTGSERAQALFGDDVEHRYLPYDLPGAVRRFLRFWRPKLVIIMETELWPNLI
AELKRRGIPLVLANARLSERSFKRYQKFKRFYRLLFKNIDLVLAQSEEDAERFLALGAKNEVTVTGNLKF
DIEVPPELAARAATLRRQLAPNRPVWIAASTHEGEEELVLDAHRALLKQFPNLLLILVPRHPERFKEVEE
LLKKAGLSYVRRSQGEPPSADTDVLLGDTMGELGLLYAIADIAFVGGSLVKRGGHNPLEPAAFGVPVISG
PHTFNFKEIFERLLQAGAAIQVEDAEDLAKAVTYLLTDPDARQAYGEAGVAFLKQNQGALQRTLQLLEPY
LPPLK
>gnl|CDD|180234 PRK05751, PRK05751, preprotein translocase subunit SecB; Validated
MSEQNNTGAQPQFQIQRIYTKDLSFENPNAPAIFQEEWQPEVNLNLDTNANKLAEDVYEVVLTVTVTAKL
GEKTAFLCEVQQAGIFTIRNIPEEQLAPLLGIECPNILFPYAREIIADLVRRGGFPPLNLAPINFDALYE
QRLQQAQQAAAEAQEA
>gnl|CDD|235590 PRK05752, PRK05752, uroporphyrinogen-III synthase; Validated
MSGWRLLLTRPAEECAALAASLAEAGIFSSSLPLLAIEPLPETPEQRALLLELDRYCAVIVVSKPAARLG
LELLDRYWPQPPQQPWFSVGAATAAILQDYGLDVSYPEQGDDSEALLALPALRQALAVPDPRVLIMRGEG
GRELLAERLREQGASVDYLELYRRCLPDYPAGTLLQRVEAERLNGLVVSSGQGFEHLQQLAGADWPELAR
LPLFVPSPRVAEQARAAGAQTVVDCRGASAAALLAALRRQAAPAS
>gnl|CDD|180236 PRK05753, PRK05753, nucleoside diphosphate kinase regulator; Provisional
MMTKPTIIINELDAERLDRLLEQPAFAGPPIAEALNAELDRAQVVPPAEMPADVVTMNSRVRFRDLSSGE
ERVRTLVYPADADDSEGQLSVLAPVGAALLGLSVGQSIDWPLPGGKETHLEVLEVEYQPEAAGEYHR
>gnl|CDD|235591 PRK05755, PRK05755, DNA polymerase I; Provisional
MKTLLLIDGSSLLFRAFYALLPTLRNSDGLPTGAVYGFLNMLLKLLKEEKPTHVAVAFDAKGKTFRHELY
PEYKANRPPMPEDLREQIPLIRELLRALGIPLLELEGYEADDVIGTLAKQAEAAGYEVLIVTGDKDLLQL
VDDNVTLLDTMGVSKNEELDPEEVVEKYGVTPEQIIDYLALMGDSSDNIPGVPGIGEKTAAKLLQEYGSL
EGLYENLDEIKGKKKEKLRENKEQAFLSRKLATIKTDVPLEVDLEDLELQPPDREKLIALFKELEFKSLL
RRAAAAEAAPLDEEDYETILDEEELEAWLAKLKAAGLFAFDTETTSLDPMQAELVGLSFAVEPGEAAYIP
LDQLDREVLAALKPLLEDPAIKKVGQNLKYDLHVLARYGIELRGIAFDTMLASYLLDPGRRHGLDSLAER
YLGHKTISFEEVAGKQLTFAQVDLEEAAEYAAEDADVTLRLHEVLKPKLLEEPGLLELYEEIELPLVPVL
ARMERNGIKVDREYLKELSAELAQRLAELEQEIYELAGEEFNINSPKQLGEILFEKLGLPVGKKTKTGYS
TDAEVLEKLADDHPIPDKILEYRQLSKLKSTYTDALPKLINPDTGRIHTSFNQTVTATGRLSSSDPNLQN
IPIRTEEGRRIRKAFVAPEGYKLLSADYSQIELRILAHLSGDEGLIEAFAEGEDIHTATASEVFGVPLEE
VTSEQRRRAKAINFGIIYGMSAFGLAQQLGISRKEAKEYIDRYFERYPGVKEYMERTVEQAREKGYVETL
FGRRRYLPDINSRNGNRRAFAERAAINAPIQGSAADIIKLAMIRVDKALKEEGLKSRMLLQVHDELVFEV
PEDELEEVKKLVKEVMENAVELSVPLVVDVGVGDNWDEAH
>gnl|CDD|235592 PRK05756, PRK05756, pyridoxal kinase PdxY
MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIG
WLGECDAVLSGYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAAD
IITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPL
VDFMRQPVGVGDLTSALFLARLLQGGSLEEALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMF
QARRLA
>gnl|CDD|235593 PRK05758, PRK05758, F0F1 ATP synthase subunit delta; Validated
MSELSTVARPYAKALFEVALEKGSLDAWSEELTFLAEVAENEDLAALLSSPLVSAEQKKKLLAAVFKSLS
EYVQNFLKVLAENGRLALLPEILEQFEALRAEHENIVDAEVTSAFPLSEEQLDKLKAALEKRLGRKVKLN
EKVDPSLIGGVIIKVGDRVIDGSVRGKLERLKDALKS
>gnl|CDD|180240 PRK05759, PRK05759, F0F1 ATP synthase subunit B; Validated
MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARA
EAAEIIEQAKKRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGREL
DAAAQSDLIDKLIAEL
>gnl|CDD|180241 PRK05760, PRK05760, F0F1 ATP synthase subunit I; Validated
RPGRLPAKRLLLIQLVVVLVAALVLWVAVGPVWGYSALIGGLIAVLANAYFAHCAFRFSGARAAKAIVRS
FYAGEAGKIIITAVLFALAFAGVQPLLPPLKFGTYLLVLGVNWFAPLLFINNKK
>gnl|CDD|235594 PRK05761, PRK05761, DNA-directed DNA polymerase I
YEWETSEGAKATERKDYSPYLLSVDYDGKLGKAVVKLYDPETGKIYKWYDRTGHKPYFLTDLDPDEIDKI
PKILRHPSFDHLEIVEKYDGLRDKKVKVTKIVVKDPLAVRRLRLSVRDIPRAWEADIKYEFRYIYDNGLI
PGMPYDVKNGLESVEPEILVEEIKKAFKDERKLAEDWLPIFEAPIPKIKRIAIDIEVYTPAKGRIPDDSE
KELLAELFDIILEYPPVVTFNGDNFDLPYLYNRALKLGIPKEEIPIEPGRAGIHIDLYKFFQNKAVRSYA
FYGKYRHREARLDAVGRALLGISKVELETNISELDLEELAEYNFRDAEITLKLTFFNNELVLKLILLLSR
ISKLPIEELSRATISTWISNLEYWEHRKRGWLIPWKEDILRLDHEVYKKAIIKGKKYRGGLVFQPPPGIF
FNVYVLDFASLYPSIIVKWNLSPETVRIPECKCHYDDEVPELGHSVCDDRPGLTSVLVGLLRDFRVKIYK
KKAKDPNLDEERRAWYDVVQRALKVFLNASYGVFGAENFKLYRIEVAESITALGREILLSTKKKAEELGL
KVLYGDTDSLFVWGPTKESLEELIKEIEERTGIDLEVDKTYDWVAFSGLKKNYFGVLKDGKVKIKGIVAK
KRNTPEFVKELQREVLEVLKSIRSPEDVEKVKDEIEDVLKRYYEKLRAKDYPLDELAIRVRLSKPLDEYT
KNTPQHVKAALQLRDYGVEVSPGDIISYVKVDDKRGVKPVQLAKLSEIDVEKYIELLRSALEQILSALGV
SWDDIRGTTRLDSFLSF
>gnl|CDD|235595 PRK05762, PRK05762, DNA polymerase II; Reviewed
MMLQQGFILTRHYRDTPGGPEVELWLATDEGPRVVLLDPQFRPYFIPAEQDERAESLLAGEIGVRLSPLA
LKDFHRRPVLGLYCRQHRQLTRLPKRLREGGVDVYEADIRFPERYLMERFITPCVWFSGEVEQYTTDGVL
RNARLKPAPDYRPPLKVVSLDIETSNKGELYSIGLEGCGQRPVIMLGPPNGEALDFLEYVADEKALLEKF
NAWFAEHDPDVIIGWNVVQFDLRLLQERAERYGIPLRLGRDGSELEWREHPFRSGYGFASVPGRLVLDGI
DALKSATWVFDSFSLEYVSQRLLGEGKAIDDPYDRMDEIDRRFAEDKPALARYNLKDCELVTRIFEKTKL
LPFLLERATVTGLPLDRVGGSVAAFEHLYLPRAHRAGYVAPNLGERPGEASPGGYVMDSKPGLYDSVLVL
DFKSLYPSIIRTFNIDPDGLVEGLAQPPEESVAGFLGARFSREKHFLPEIVERLWEGRDEAKREMNKPLS
QAIKIIMNAFYGVLGSSGCRFFDPRLASSITMRGHEIMKQTRELIEAQGYQVIYGDTDSTFVWLGGAHDE
EDAAKIGRALVQEINQWWQEHLQQEFGLESALELEFEKHYRRFFMPTIRGAEEGSKKRYAGLIQEGDGDG
RIVFKGLETVRTDWTPLAKEFQQELYERIFRGEPYVDYVREVIDKLRAGELDEKLVYRKRLRRPLDEYQR
NVPPHVRAARLADEMGYKVGRPLQYQNGGKIGYVITVNGPEPLEYRKSPIDYDYYIEKQLQPVADRILPF
FGDDFATLKTGQLGLF
>gnl|CDD|235596 PRK05764, PRK05764, aspartate aminotransferase; Provisional
MMKLSKRVSRVTPSATLAVTAKAKELKAQGRDVISLGAGEPDFDTPEHIKEAAIEALDDGKTKYTPAAGI
PELREAIAAKLKRDNGLDYDPSQVIVTTGAKQALYNAFMALLDPGDEVIIPAPYWVSYPEMVKLAGGVPV
FVPTGEENGFKLTVEQLEAAITPKTKALILNSPSNPTGAVYSPEELEAIADVAVEHDIWVLSDEIYEKLV
YDGAEFTSIASLSPELRDRTITVNGFSKAYAMTGWRLGYAAGPKELIKAMSKLQSHSTSNPTSIAQYAAV
AALNGPQDEVEEMRQAFEERRDLMVDGLNEIPGLECPKPEGAFYVFPNVSKLLGKSITDSLEFAEALLEE
AGVAVVPGIAFGAPGYVRLSYATSLEDLEEGLERIERFLESLK
>gnl|CDD|235597 PRK05765, PRK05765, precorrin-3B C17-methyltransferase; Provisional
MGKLYIVGIGPGSKEQRTIKAQEAIEKSNVIIGYNTYLRLISDLLDGKEVIGARMKEEIFRANTAIEKAL
EGNIVALVSSGDPQVYGMAGLVFELISRRKLDVDVEVIPGVTAALAAAARLGSPLSLDFVVISLSDLLIP
REEILHRVTKAAEADFVIVFYNPINENLLIEVMDIVSKHRKPNTPVGLVKSAYRNNENVVITTLSSWKEH
MDEIGMTTTMIIGNSLTYSWKNYMITPRGYERKYEL
>gnl|CDD|235598 PRK05766, rps14P, 30S ribosomal protein S14P; Reviewed
KYKPPKKRKYGKGARECQRCGRKQGLIRKYGLYLCRQCFREVAPKLGFKKYS
>gnl|CDD|180247 PRK05767, rpl44e, 50S ribosomal protein L44e; Validated
MKMPKKIRTYCPYCKTHTEHEVEKVKKGKRSELKWGQRQYRRKTIGYGGKFSPVPGGAKPTKKVDLRYRC
TECGKAHTREGFRAKKFELVEV
>gnl|CDD|235599 PRK05769, PRK05769, acetyl ornithine aminotransferase family protein
DMPRRPRIVVELPGPKAREIIERDEKYLAQSTRRWYPLVIERGEGVWVEDVDGNVYLDFNAGIAVTNVGH
AHPKVVKAVKEQAEKFLHYSLTDFYYEPAVELAERLVEIAPGGFEKKVFFTNSGTESNEAAIKIARYHTG
RKYIIAFLGAFHGRTYGSLSLTASKPVQRKGFFPLMPGVIHVPYPNPYRNPWGIENPEECGNAVLDFIED
YLFKKLVPPEEVAAIIVEPIQGEGGYVVPPKNFFKELRKLADKYGILLIDDEVQTGMGRTGKMFAIEHFG
VEPDIITLAKAIAGGLPLGAVIGRAELMFLPPGSHANTFGGNPVAAAAALATLEELEEGLLENAQKLGEY
LRKELKELKEKYEFIGDVRGLGLMIGVELVKDRKEPDPKLRDKVLYEAFKRGLLLLGAGKSAIRIIPPLI
ITEEEADIGLEILEEAIKELL
>gnl|CDD|235600 PRK05771, PRK05771, V-type ATP synthase subunit I; Validated
LAPVRMKKVLIVTLKSYKDEVLEALHELGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLN
PLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNFDLDLSLLL
GFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLGFERLELEEE
GTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFLKTDKTFAIEG
WVPEDRVKKLKELIDKATGGSAYVEFVEPDEEEEEVPTKLKNPKFIKPFESLTEMYSLPKYNEIDPTPFL
AIFFPLFFGMMLGDAGYGLLLLLIGLLLSFKLKKKSEGLKRLLKILIYLGISTIIWGLLTGSFFGFSLPI
FLPGGYLELPEGYPSLSTENDVMTILIISLLIGVIHLFLGLLLGFINNVRKGDYKDAFLAQLGWLLILLG
ILLIVLGGFGLVVGLGPLGLIGKYLIIGGVVLIILGEGIDGKSLGGALGGLGLYEITGYLGDVLSYARLM
ALGLAGAGIAMAFNLMAGLLPPSIGVIGIIVGIIIFIFGHLLNIALSILGAFVHGLRLHYVEFFGKFYEG
GGKKFNPFKAIRKYTE
>gnl|CDD|168237 PRK05772, PRK05772, S-methyl-5-thioribose-1-phosphate isomerase
MKLTVKEVKELFKPKLLPIIWKDNTLTLLDQSLLPFETVYVDLKTVEEVALAIRNMQVRGAPAIGITAGY
GMVLALIENNVKTLDDAIRELTRAKTILDSARPTAVNLVWATSRMLNKAKNTVESGNAKSVNELIELLKV
EAKKIFEEEYDAEIQMGLYGLEKLNDGDTVLTQCNAGGLATGTGLGTALAPVKLAKALGMSVSVIAPETR
PWLQGSRLTVYELMEEGIKVTLITDTAVGLVMYKDMVNNVMVGADRILRDGHVFNKIGTFKEAVIAHELG
IPFYALAPTSTFDLKSDVNDVKIEERDPNEVRTIRGVPITPEDVNVYNPVFDVTPPKYITGIITEKGIIY
PPFHKNIRKILER
>gnl|CDD|235601 PRK05773, PRK05773, 3,4-dihydroxy-2-butanone 4-phosphate synthase; Validated
MDFEEARKALESGIPVLIYDFDGREEEVDMVFYAGAVTWKSIYTLRKNAGGLICYATSNSEGKTLGLNFL
AEILKRHELYRKLVKKPSYGDEPAFSLWVNHVKTKTGISDYDRALTIRELHKVVELAKTNPEEAREEFYE
NFYSPGHVPILIGRGIRERRGHTELSIALAQAAGLEPSAVIAEMLDEKLSLSKEKAKKIAKNLGFPLVEG
KEIFKEVVI
>gnl|CDD|235602 PRK05776, PRK05776, DNA topoisomerase I; Provisional
GYILVIAEKPKAARKIAEALSEKPIRCRIYGVPYWIVKRDGKKIVVAPAAGHLFGLHTKSKGFPVFDYEW
KPLYEIDKGSKYTKKYYELLSSLSKYADEFINACDYDIEGSVIGYLIIKYLGDPKKAKRMKFSALTKSDI
RRAFRNLETLDYEMINAGIARHELDWLWGINVSRALMSSVRDASGKRVILSAGRVQSPTLKYVVEREIER
NLFVPLPYFSVSIIIEKNGYEFTLKYENKKFETKEEAKEILEEIKKTGYLKVTKVEVKIEILEPPPPFNL
GDLQVEAARIYGFSPYKTQSIAEDLYLDGLISYPRTNSQKLPPTLNIRNILKGLSRSPQYRPLVNLLLKE
TKGVLKPVQGPKDDPAHPAIYPTGEPPKNLSKDEFKLYDLIVRRFLASFAAPAVLSNTIVTLRVPGFPLV
FSASGQRIEERGWLKYYPFHKFDEEELPLLKKGERVKIVDVKVRKSYTKPPSRYSKASLLKWMESVGIGT
EATRARIIETLFKRGYLTSNGKYIEVTPLGFGVAEVLEKYFPDIVSVELTRDFEEKLEMIRTGKATREEV
IEEAKETLNKLLEEFKKNKDEIGEELAKALGLIKPVGKCKICGREAYKDGLCKYHYEAKKRLVKAYEEWK
ERTGYDHKEYLEKISKLKSTGKWVKDVITYMLNMNDKSWK
>gnl|CDD|235603 PRK05777, PRK05777, NADH-quinone oxidoreductase subunit NuoN
MTITSLNLILLLPELILLGAAVVLLLIDAFVRRHSRRATLAVLALLLALVALLFVLGAAGGGTAFGGMLV
VDGFALFLKGLILLASLLALLLARPYLEDRGRGEFYLLVLFALLGMMVMVSANDLLTLFLGLELLSLPLY
ALAALRRDRRRSLEAAIKYFVLGALASGFLLYGMSLLYGATGSLSFAGIAKALADGSGNSLLLLFGLVFL
LVGLAFKLSAVPFHMWTPDVYEGAPTPVTAFLATAPKIAAFAVLLRLLVVAFGGLSEDWQQVLAIIAIAS
MLVGNLAALSQTNIKRLLAYSSIAHAGYLLVGLAAGTAEGYSAVLFYLLAYLFMTLGAFGVISLLRRKGG
EAESISDFAGLSKRSPLLAAVMTIFMLSLAGIPPTAGFWGKFYVFEAAVEAGLWWLAVIGVLNSAIGAFY
YLRVIKLMYFDEPPRDAPVNWPLSAGGAVLSVSALLVLVLGIFPQPLLDLAAQAIP
>gnl|CDD|235604 PRK05778, PRK05778, 2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
LMKNALGLTYLRYDGLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHT
LHGRAIAFATGAKLANPDLEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTP
EGSKTKTAPYGNIEPPIDPCALALAAGATFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGR
NTSTKSPAYMREYYKKRVYKLKLEEDYDPTDRDKAAEKMLEEELGGKIPIGVFYKNERPTFEERLEKLIE
PLLELPPAALRPGKEALDTIN
>gnl|CDD|235605 PRK05782, PRK05782, bifunctional sirohydrochlorin cobalt chelatase/precorrin-8X methylmutase; Validated
MDRQSNTAIILIGHGSRRETFNSDMEGMANYLKEKLGVPIYLTYNEFAEPNWRSLLNEIIKEGYRRVIIA
LAFLGRGNHVFRDIMGELGVQRLNSWEVSKISGKEVEFYVTEPLSDSPLVGLALYYRLARALDALPTLEY
TEDPEEIEERSMNYILENLGLDVKDWREKRVIARAVYASGNLELAKYVKISNDLLDAGIEAIRAESEIVA
DVKMVSAGIRWKKVTCMIDAERTKELAKELGITRAAAAMRLSLGQGGKVVVIGNAPTALIETLKLVKEGV
DIPFIVATPPGFTNAKEVKEALIESGIPSVVLRGTYGGSGIAVAIINELIKMAME
>gnl|CDD|235606 PRK05783, PRK05783, hypothetical protein; Provisional
MKYYVELIIINKDSVRDPEGETIQRYVIERYTGNIIEVRAGKYLVFKIEANSPEEAKELALKIAREGRLY
NPIVHKIVVRVRRE
>gnl|CDD|235607 PRK05785, PRK05785, hypothetical protein; Provisional
NMGLGATWEELQEAYNKIPKAYDRANRFISFNQDVRWRAELVKTILKYCGRPKKVLDVAAGKGELSYHFK
KVFKYYVVALDYAENMLKMNLVADDKVVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIAEFTRVSRKQ
VGFIAMGKPDNVIKRKYLSFYLRYIMPYIACLAGAKCRDYKYIYYIYERLPTNSFHREIFEKYADIKVYE
ERGLGLVYFVVGSSRG
>gnl|CDD|235608 PRK05786, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
MRLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGNIHYVVGDVSSTESARN
VIEKAAKVLNAIDGLVVTVGGYVEDTVEEFSGLEEMLTNHIKIPLYAVNASLRFLKEGSSIVLVSSMSGI
YKASPDQLSYAVAKAGLAKAVEILASELLGRGIRVNGIAPTTISGDFEPERNWKKLRKLGDDMAPPEDFA
KVIIWLLTDEADWVDGVVIPVDGGARLK
>gnl|CDD|235609 PRK05787, PRK05787, cobalt-precorrin-7 (C(5))-methyltransferase
MIYIVGIGPGDPEYLTLKALEAIRKADVVVGSKRVLELFPELIDGEAFVLTAGLRDLLEWLELAAKGKNV
VVLSTGDPLFSGLGKLLKVRRAVAEDVEVIPGISSVQYAAARLGIDMNDVVFTTSHGRGPNFEELEDLLK
NGRKVIMLPDPRFGPKEIAAELLERGKLERRIVVGENLSYPDERIHKLTLSEIEPLEFSDMSVVVILDER
>gnl|CDD|235610 PRK05788, PRK05788, cobalt-precorrin 5A hydrolase
VSTMKIAIICATERGRDLAERLKAKLKADCYTSEKLEYEGFADAFEEAFGCYDALIFIMATGIAVRVIAP
LLKDKWSDPAVVVVDEKGKFVISLLSGHHGGANELARDLAKILGAVPVITTATDVNGKAAVDTIAKQLNA
KIVNRESTKKVNAALVNGEKVGLWGDELDPVIRVSLRNDVPELPKVTVKLRPKNVVLGIGCRKGVSAEEI
AEAVERALEALNIDPRAVKAIASITLKKDEPGLLQLAEELGVPFITFSKEELNEVEHKFPGSSFVKKTVG
VGGVAEPSALLASNGKLILEKLKYNGVTIAIGKLH
>gnl|CDD|180261 PRK05790, PRK05790, putative acyltransferase; Provisional
MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAA
LKAGLPVEVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELV
DTMIHDGLTDAFNGYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGD
PVVVDTDEHPRPDTTAESLAKLRPAFDKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYA
VAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHP
IGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP
>gnl|CDD|235611 PRK05793, PRK05793, amidophosphoribosyltransferase; Provisional
NMMMDLEGDKFKEECGVFGVFSKNNIDVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVF
SKEKLKGLKGNSAIGHVRYSTTGASDLDNAQPLVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTS
IDSEVILNLIARSAKKGLEKALVDAIQAIKGSYALVILTEDKLIGVRDPHGIRPLCLGKLGDDYILSSES
CALDTIGAEFIRDVEPGEIVIIDEDGIKSIKFAEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAGRQ
LYKEYPVDADIVIGVPDSGIPAAIGYAEASGIPYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVN
VEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFRVSSPPVKYPCYFGIDTPYRKELIGANMSVEEIR
EMIGADSLGYLSIEGLLESLNGDKGFCLGCFNGVYPVSAPKEGPKYLLE
>gnl|CDD|235612 PRK05800, cobU, adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase; Validated
GMLILVTGGARSGKSRFAERLAAQSGLQVLYIATAQPFDDEMAARIAHHRQRRPAHWQTVEEPLDLAELL
RADAAPGRCVLVDCLTTWVTNLLFEEGEEAIAAEIDALLAALQQLPAKIILVTNEVGMGIVPEYRLGRHF
RDIAGRLNQQLAAAADEVYLVVAGLPLKLK
>gnl|CDD|235613 PRK05802, PRK05802, sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein
MYERLDCIDAGSEYCPCHLAETGECIVCSQLQGKKFCDCKNWKGVCIYQEFIWNGNKAKEGRKTYECKII
KKENIEDNLIILTLKVPHKLARDLVYPGSFVFLRNKNSSSFFDVPISIMEADTEENIIKVAIEIRGVKTK
KIAKLNKGDEILLRGPYWNGILGLKNIKSTKNGKSLVIARGIGQAPGVPVIKKLYSNGNKIIVIIDKGPF
KNNFIKEYLELYNIEIIELNLLDDGELSEEGKDILKEIIKKEDINLIHCGGSDILHYKIIEYLDKLNEKI
KLSCSNNAKMCCGEGICGACTVRYGGHKVKRLCKVQVDPR
>gnl|CDD|180266 PRK05803, PRK05803, RNA polymerase sporulation sigma factor SigK
MMFLFAALLYIVKEILFLVSYVKNNSFPQPLSEEEERKYLELMKEGDEEARNILIERNLRLVAHIVKKFE
NTGEDVDDLISIGTIGLIKAIESFDAGKGTKLATYAARCIENEILMHLRNLKKTKKEVSLQDPIGVDKEG
NEISLIDILGSEEDDVIEQVELKMEVEKLYKKIDILDEREKEVIEMRYGLGNGKEKTQREIAKALGISRS
YVSRIEKRALKKLFKELYRAEKE
>gnl|CDD|180267 PRK05805, PRK05805, phosphate butyryltransferase; Validated
MIKSFDEILSKAKEQPPKTISVAVAQDEPVLEAVKEAKELGIANAILVGDKEKIKEIAKEIDMDLEDFEI
IDEKDNRKAALKAVELVSSGKADMVMKGLVDTANFLRAVLNKEIGLRTGKTMSHVAVFEVPKYDRLLFLT
DAAFNIAPDLKEKIDIINNAVTVAHAIGIENPKVAPICAVEVVNPKMPATLDAALLSKMSDRGQIKGCIV
DGPLALDNALSEEAAKHKGIDGPVAGNADILLVPNIEAGNVMYKTLTYFADCKNGGLLVGTSAPVVLTSR
ADSHETKLNSIALAALVAAKL
>gnl|CDD|235614 PRK05807, PRK05807, RNA-binding protein S1
MTLKAGSILEGTVVNITNFGAFVEVEGKTGLVHISEVADTYVKDIREHLKEQDKVKVKVISIDDNGKISL
SIKQAMKQKKSVKPAEIDWQKEKNKNNNGNFEDRLSKFLKDSEERFQDLKKHQDSKGRGYKKSNGY
>gnl|CDD|180269 PRK05808, PRK05808, 3-hydroxybutyryl-CoA dehydrogenase; Validated
MGIQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAALAR
ITGTTDLDDLKDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMH
FFNPVPVMKLVEIIRGLATSDATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVAT
AEDIDEGMKLGCNHPIGPLALADLIGLDTCLAIMEVLYEGFGDSKYRPCPLLRKMVAAGWLGRKTGRGFY
DY
>gnl|CDD|180270 PRK05809, PRK05809, short-chain-enoyl-CoA hydratase
MELKNVILEKEGHIAVVTINRPKALNALNSETLKELDTVLDDIENDDNVYAVILTGAGEKAFVAGADISE
MKDLNEEEGRKFGLLGNKVFRKLENLDKPVIAAINGFALGGGCELSMACDIRIASEKAKFGQPEVGLGIT
PGFGGTQRLARIVGPGKAKELIYTGDMINAEEALRIGLVNKVVEPEKLMEEAKALANKIAANAPIAVKLC
KDAINRGMQVDIDTAVAIEAEDFGECFSTEDQTEGMTAFVEKREKNFKNK
>gnl|CDD|235615 PRK05812, secD, preprotein translocase subunit SecD; Reviewed
WKYLLILLVLLIGLLYALPNLRGALAPATPEWLPALGAKPMKLGLDLRGGVHFLLEVDMDDALKKRLESL
ADDLRSLLREKKIRYGGVEITFRDAEDRDKAIALLRKLSSLTEAELKEITEEALEQAIEIIRNRVNELGV
AEPVIQRQGADRIVVELPGVQDTARAKEILGKTATLEFRLVPVILTGDDITDASASFDQQGQPVVNITLD
SEGAKKFADITKANIGKRMAIVLDGEVISAPVIQSAITGGSAQITGNFTAEEARDLALLLRAGALPAPLE
IVEERTIGPSLGADSIRAGLIAGLIGLALVLLFMILYYRLFGLIANIALVANLVLILAVLSLLGATLTLP
GIAGIVLTIGMAVDANVLIFERIREELREGRSLRSAIEAGFKRAFSTILDSNITTLIAAIILYALGTGPV
KGFAVTLGIGILTSMFTAITVTRALVNLLYGRRKRLKKLSIG
>gnl|CDD|235616 PRK05813, PRK05813, single-stranded DNA-binding protein; Provisional
MMDNLMENNKVYLEGKVVSELEFSHEMYGEGFYNFKLEVPRLSDSKDILPVTVSERLLAGMDLKVGTLVI
VEGQLRSYNKFIDGKNRLILTVFARNIEYCDERSDIKNPNEIFLDGYICKEPVYRTTPFGREIADLLLAV
NRPYNKSDYIPCIAWGRNARFCKTLEVGDNIRVWGRVQSREYQKKLSEGEVVTKVAYEVSISKMEKVEKE
EANNKEKHQ
>gnl|CDD|235617 PRK05815, PRK05815, F0F1 ATP synthase subunit A; Validated
IEHHLIIGFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGK
KFAPLAFTLFLFILLMNLLGLIPYLLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPHP
LLLPIEIISEFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYI
FMMLTIVYISMAVEEEH
>gnl|CDD|235618 PRK05818, PRK05818, DNA polymerase III subunit delta'; Validated
SLMKNKTHPLLLIERKGSFLKPFLYEYLTSIVCTKANGFCKTCESCLKILNGKYNDFYLIFDQKNPIKKE
DALSIINKLNRPSVESNGKKIYIIYGIEKLNKQSANSLLKLIEEPPKNTYGIFTTRNENNILNTILSRCV
QYVVLSKEKKVPFKVESNDRYFQYILLSFYSVDEQLQAYNNGSFSKLKNIIETLINKKNKLIQIHKAWIL
FKTFSYYEIAQLLNLLIPTVDPEKKSKLYNLLSNLKYNLPKTALFANIISW
>gnl|CDD|180275 PRK05819, deoD, DeoD-type purine-nucleoside phosphorylase
MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSIS
IYANELITDYGVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDA
AKEKGITVHVGNVFSADLFYNPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGE
ATTAEERQTTFNDMIEIALESAILG
>gnl|CDD|180276 PRK05820, deoA, thymidine phosphorylase; Reviewed
MFLAQEIIRKKRDGGALSDEEIDWFIDGYTDGTVSDGQIAALAMAIFFNGMTRPERVALTLAMRDSGEVL
DWSSLNLNGPIVDKHSTGGVGDKISLMLAPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYRAFPSND
RFREILKDVGVAIIGQTSDLAPADKRLYALRDVTATVESIPLITASILSKKLAEGLDALVLDVKVGSGAF
MKTYEEARELARSMVEVANGAGVRTTALLTDMNQPLASSAGNALEVREAVEFLTGGYRPPRLVEVTMALA
AEMLVLAGLAKDEAEARADLAAVLDSGKAAERFGRMVAAQGGPPDFVENYDKYLPTAPHTKPVYADRSGV
LSAMDTRALGMAVVRLGGGRRRKGDPIDYSVGLTLHARLGDRVDAGEPLATLHADDEERFQEAAAALKAA
IRIGDEAPEATPLIYRRITA
>gnl|CDD|235619 PRK05826, PRK05826, pyruvate kinase; Provisional
RMLRRTKIVATLGPASDSPENLEKLIEAGVNVVRLNFSHGSHEEHGKRAALVREIAAKLGRPVAILLDLK
GPKIRVGKFKEGKITLKTGDKFTLDTDQKEEGDKERVGVDYKGLPKDVKPGDILLLDDGKLQLKVVEVDG
DEVETEVKNGGPLSNNKGINIPGGGLSLPALTEKDKADIKFAAEQGVDYIAVSFVRSAEDVEEARRLLRE
AGCPHAKIIAKIERAEAVDNIDEIIEASDGIMVARGDLGVEIPDEEVPGLQKKIIRKAREAGKPVITATQ
MLESMIENPRPTRAEVSDVANAVLDGTDAVMLSGETAAGKYPVEAVEAMARICKGAEKEFSINLSKHRLD
RQFDRIDEAIAMSAMYAANHLKGVKAIVALTESGRTARLISRFRPGAPIFAVTRDEKTQRRLALYRGVYP
VLFDSAADTDDAAEEALRLLLEKGLVESGDLVVVTSGDPMGTAGG
>gnl|CDD|180278 PRK05828, PRK05828, acyl carrier protein; Validated
MQEMEILLKIKEIAKKKNFAVTLDESNINKPYRELKIDSLDMFSIIVSLESEFNIEFSDEKLMKLKNLAD
LILEVKELKKQKGV
>gnl|CDD|180279 PRK05834, PRK05834, hypothetical protein; Provisional
MVDSNLIDELKSISLSMFRKNFFGLYHGSISAKIEANQFIINKQNAIFDELDENSLIVLYDKKDYRWKEA
SIDSPIHASIYKNISEAKFIAYAMPPYTTAYSLRHNKILPRDYFGYRSLGEISIYDPKDFDDWYERADTE
ILRYLQEKNKNFVVIKGYGVYAYARDIYELAKKIAILENSCKILRLSDLMDRLS
>gnl|CDD|180280 PRK05835, PRK05835, class II fructose-1,6-bisphosphate aldolase
MLVKGNEILLKAHKEGYGVGAFNFVNFEMLNAIFEAGNEENSPLFIQASEGAIKYMGIDMAVGMVKIMCE
RYPHIPVALHLDHGTTFESCEKAVKAGFTSVMIDASHHAFEENLELTSKVVKMAHNAGVSVEAELGRLMG
IEDNISVDEKDAVLVNPKEAEQFVKESQVDYLAPAIGTSHGAFKFKGEPKLDFERLQEVKRLTNIPLVLH
GASAIPDDVRKSYLDAGGDLKGSKGVPFEFLQESVKGGINKVNTDTDLRIAFIAEVRKVANEDKSQFDLR
KFFSPAQLALKNVVKERMKLLGSANKI
>gnl|CDD|180281 PRK05839, PRK05839, succinyldiaminopimelate transaminase
MTFEPYPFEKLRELLKEITPNKEYKGLDLTIGEPQFETPKFIQDALKNNAHLLNKYPKSAGEESLREAQR
GFFKRRFKIELKENELIPTFGTREVLFNFPQFVLFDKQNPTIAYPNPFYQIYEGAAIASRAKVLLMPLTK
ENDFTPSLNEKELQEVDLVILNSPNNPTGRTLSLEELIEWVKLALKHDFILINDECYSEIYENTPPPSLL
EASILVGNESFKNVLVINSISKRSSAPGLRSGFIAGDASILKKYKAYRTYLGCASPLPLQKAAAVAWLDD
EHAEFFRNIYAKNLKLAREILGITIPPATFYVWLPVDNDEEFTKKLYQNEGIKVLPGSFLGRNGIGKGYV
RIALVYDTPKLEKALEIIKTYLEN
>gnl|CDD|235620 PRK05841, flgE, flagellar hook protein FlgE; Validated
MNDTLLNAYSGIKTHQFGLDSLSNNIANVNTLGYRSNIPEFKTLFSSHLDALNAKSVVANDRNYGVTGSS
NAISNKDGEYKPSDGEFHMAYQGKGWFVVGPNKNGSMTINKDGFSKKQDNYFTRDGSFARDADGYLVNPE
GYYVYGIDLGKIKDGTLNSTARDEADIEKLHGNTLSPLQIPQDLTYQPVLTTKVGISVNLNPKDHLKGVQ
DFFLNDKGEFIKERFLNQDINALANDDNEPIDAITNRKLNITIQKEDGKKEDFVFTYGDAEKGENQFKTL
GDLKKLLKEKTGLDLNLIRSEKGAKSPPLLLEIANPSQTPITFSLSGGIADKLGLNANGMELKKGISRDS
VAIKIPSYSTEVEIYDKAGDKYLLQSEYYMTNSGDPTSSPRKNQTWEVKSYIVDPKNKTPINTDPTWEIV
GFDATHKMKAAPMTLDFKGNKLTYSLDKSEDHDSSNLSYQDSKLLEASQDGKPRGILRDVRIDENGVISL
AFSNGVVEPMGRIGIAAFTNDQGLRKVGGNLFEMQEGTINGENRPLSGNPILGWDEEGKLKFGKVRHKYL
ETSNVDAGNALTNLILMQRGYSMNARAFGTGDDLIKEAISLKK
>gnl|CDD|235621 PRK05842, flgD, flagellar hook assembly protein FlgD
MAIDLAEVTGAKAAQERKKEQPTIANGLDKNAFMKLFLEQLKNQDPTAPMETDKIITQTAQLTQVEMQEE
NKKTMQEVASAMKSNKETNESLKDFQGALKDTMENLNKGMDDSLKANNALREVSALNSVSMIGKIAETDV
SGANFDGNNKLSFSLFFDEKIDASKGVPAIQILNENNELVKTIPLKDYNGQKGYINFEWDGLNEKGEKVP
KGNYKIKAEYNLDSHSKQYLQTRIGRGEVESVIFDKGKPMLRMGEMILPIDSAIEFYKPDQKPLEQKPLE
QKLSDQKPLDQKPQT
>gnl|CDD|180284 PRK05844, PRK05844, pyruvate flavodoxin oxidoreductase subunit gamma; Validated
MLEIRWHSRAGQGAVTGAKGLADVIAKTGKEVQAFAFYGSAKRGAAMTAYNRIDDEPILNHEKFMQPDYV
LVIDPGLVFIENIFANEKEDTKYIITTHLSKEELIEKKPELKGKKVFLVDCIKISMETIGRPIPNTPMLG
ALMKVSGMLEIDAFKEAFKKVLGKKLPQKVIDANMLAIQRAYEEVQ
>gnl|CDD|235622 PRK05846, PRK05846, NADH:ubiquinone oxidoreductase subunit M; Reviewed
MNWPLLSLLIFLPLIGGLLVLLTERFGARLARWIALIGTLLTLLLSLVLWIGFDSSNAGFQFVEKHPWIP
RFGISYHLGVDGISLLLVVLTALLTPLAVLASWEEIKKRVKFYMAALLWLEGGVIGVFAALDLLLFYVFF
EAMLIPMYFLIGVWGGKNRIYAATKFFLYTLLGSLLMLVAIIYLVVVYYNATGTFDIADLLNLPLPPGVQ
YWLFLAFFIAFAVKMPMFPLHTWLPDAHVQAPTAGSVLLAGILLKMGAYGLLRFSLPLFPDASHEFAPII
ITLGVIAIIYGALVALAQTDIKKLIAYSSISHMGFVTLGIFAGNQLGIQGAIFQMISHGLSSAALFLLVG
VLYDRLHTRDIADYGGLAKVMPVLAAFFLFFAMASLGLPGTSGFVGEFLILLGSFQVNPVIAFIATTGLI
LAAVYSLWLYQRVMFGPVKNEVAKLKDLNGRELLILLPLVALLLLLGVYPKPLLDVIHPSVENLLQWVAP
SVATTRP
>gnl|CDD|235623 PRK05849, PRK05849, hypothetical protein; Provisional
TRMAELFFQTKAETLANLQPILKKAKILPLLLFSVREWLSNKDKVLEEIQNSFPADKLIVRSSSRSEDSS
SSSNAGAFLSILNVNADSKDQLLKAIEKVIASYGTSKDDEILVQPMLEDIVLSGVAMSRDPESGAPYYVI
NYDESGSTDSVTSGSGGSATTVYHYRDALVFKPPRLKKLIELIRELEALFGCDFLDIEFAIDEKEELYIL
QVRPITVPEKWNAEFLSLVAQALERIYKKFESLQEPRPRLLGDRTIFGVMPDWNPAEIIGLRPKPLAFSL
YRELITDNIWAYQRDNYGYRDLRSHPLMHSFAGIPYIDVRLSFNSFIPAGLDEKIAEKLVNAYLDKLAKN
PELHDKIEFEIVFSCYDFTLDKKLEELLPGGFSENEIKRIEFSLLKLTNRIISPKSGLFRKDLEKIEKLE
ERYKELLNSNLDPLDKIYWLLEDCKRYGTLPFAGIARAAFVATQLLKSLVEIGALSQEELDAFLNSLNTV
SKELSKDLNSLGELSKDEFLKRYGHLRPGTYDILSPRYDEDPELYFDWTKDESTVDSDKEFELSPEELKA
LNKLLHEHGLNIDAEEFLDFLKEAIEGRELVKFEFTRNLSDALELIALLGAYYGISREDLSHLDIKDLLN
LYSSLLSINPKELFLEEIKRNKQEYELTRSLKLPPLICSADDVYSFEIHESKPNFITQKRVEATVADLDN
DNDDDLEGKIVCIENADPGYDWLFTKGIAGLITCYGGANSHMAIRAAELGLPAVIGVGEELFEKWLKAKR
ILLDCASQRIEIL
>gnl|CDD|235624 PRK05850, PRK05850, acyl-CoA synthetase; Validated
SSVPSLLRERASLQPDDAAFTFIDYEQDPAGVAETLTWSQLYRRTLNVAEELRRHGSTGDRAVILAPQGL
EYIVAFLGALQAGLIAVPLSVPQGGAHDERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSAPPVIE
VDLLDLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYFGDTGGVPPPDTTV
VSWLPFYHDMGLVLGVCAPILGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVRKTSDD
DMAGLDLGGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEATVYVATREPGQPPESVRFD
YEKLSAGHAKRCETGGGTPLVSYGSPRSPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETER
TFGATLVDPSPGTPEGPWLRTGDLGFISEGELFIVGRIKDLLIVDGRNHYPDDIEATIQEITGGRVAAIS
VPDDGTEKLVAIIELKKRGDSDEEAMDRLRTVKREVTSAISKSHGLSVADLVLVAPGSIPITTSGKIRRA
ACVEQYRQDEFTRLDATP
>gnl|CDD|180289 PRK05851, PRK05851, long-chain-fatty acid--ACP ligase MbtM
MNELAAALSDAMTASGRDLVVLDRESGLWRRHPWPEVHGRAENVAARLLDRDRPGAVGLVGEPTVELVAA
IQGAWLAGAAVSILPGPVRGADDGRWADATLTRFAGIGVRTVLSHGSHLERLRAVDSSVTVHDLATAAHT
NRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLA
FLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATLTAAPNFAYNLIGKYARRVSDVDLGALRVALNG
GEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAESTCAVTVPVPGIGLRVDEVTTDDGSGARRHAVLGNP
IPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAPIDPDDWFPTGDLGYLVDGGLVVCGRAKEL
ITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEFRGPDEAGARSEVVQRVASECGV
VPSDVVFVAPGSLPRTSSGKLRRLAVKRSLEAADG
>gnl|CDD|235625 PRK05852, PRK05852, fatty acid--CoA ligase family protein
MRFMGGAAPMASDFGPRIADLVEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDR
VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLT
VNVGGDSGPSGGTLSVHLDAATEPTPATSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIIT
GYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQI
LLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQTENP
VVSTGLVGRSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSA
AGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEEL
VQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQFGHSV
>gnl|CDD|235626 PRK05853, PRK05853, hypothetical protein; Validated
VVGHIVNDPQRRKVGDQEVIKFRVASNSRRRTADGGWEPGNSLFITVNCWGRLVTGVGAALGKGAPVIVV
GHVYTSEYEDRDGNRRSSLEMRATSVGPDLSRCIVRIEKPRYTGPSAGEAPAATGTGAADAADAPASAAD
SVSDVVDDDAATGHNPLPLSA
>gnl|CDD|235627 PRK05854, PRK05854, SDR family oxidoreductase
MRKPLDITVPDLSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVPDAKLSLR
ALDLSSLASVAALGEQLRAEGRPIHLLINNAGVMTPPERQTTADGFELQFGTNHLGHFALTAHLLPLLRA
GRARVTSQSSIAARRGAINWDDLNWERSYAGMRAYSQSKIAVGLFALELDRRSRAAGWGITSNLAHPGVA
PTNLLAARPEVGRDKDTLMVRLIRSLSARGFLVGTVESAILPALYAATSPDAEGGAFYGPRGPGELGGGP
VEQALYPPLRRNAEAARLWEVSEQLTGVSFPAS
>gnl|CDD|235628 PRK05855, PRK05855, SDR family oxidoreductase
SQPRRTVVSSDGVRLAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKR
TAAYTLARLADDFAAVIDAVSPDRPVHLLAHDWGSIQGWEAVTRPRAAGRIASFTSVSGPSLDHVGFWLR
SGLRRPTPRRLARALGQLLRSWYIYLFHLPVLPELLWRLGLGRAWPRLLRRVEGTPVDPIPTQTTLSDGA
HGVKLYRANMIRSLSRPRERYTDVPVQLIVPTGDPYVRPALYDDLSRWVPRLWRREIKAGHWLPMSHPQV
LAAAVAEFVDAVEGGPPARALLRARVGRPRGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEA
AAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPDIVVNNAGIGMAGGFLDTSAEDWDRVL
DVNLWGVIHGCRLFGRQMVERGTGGHIVNVASAAAYAPSRSLPAYATSKAAVLMLSECLRAELAAAGIGV
TAICPGFVDTNIVATTRFAGADAEDEARRRGRADKLYQRRGYGPEKVAKAIVDAVKRNKAVVPVTPEAHA
GYGVSRFAPWLLRSLARLDVAS
>gnl|CDD|180293 PRK05857, PRK05857, fatty acid--CoA ligase
MGGKKFQAMPQLPSTVLDRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVL
VISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVI
AVDIAAVTRESEHSLDAASLAGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEGLNWVT
WVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKS
ANATVPSLRLVGYGGSRAIAADVRFIEATGVRTAQVYGLSETGCTALCLPTDDGSIVKIEAGAVGRPYPG
VDVYLAATDGIGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYI
KGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIA
ARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARVVVRG
>gnl|CDD|235629 PRK05858, PRK05858, acetolactate synthase
PAQTGHAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGV
AVLTAGPGVTNGMSAMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGR
LVDQALQAAVTPHRGPVFVDFPMDHAFSMADDDGRPGALTELPAGPTPDPDALARAAGLLAEAQRPVIMA
GTDVWWGHAEAALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVLVVGVPMDFRLGFG
VFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAILSALAGAGGDRTDHQGWIEELRTAETAARARDAAE
LADDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAAR
LARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEKHPMEALYGYDVAADLRPGTRYD
EVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTDPSVAYPRRSNLA
>gnl|CDD|180295 PRK05862, PRK05862, enoyl-CoA hydratase; Provisional
MAYETILVETRGRVGLITLNRPKALNALNDALMDELGAALAAFDADEGIGAIVITGSEKAFAAGADIKEM
ADLSFMDVYKGDYITNWEKVARIRKPVIAAVAGYALGGGCELAMMCDIIIAADTAKFGQPEIKLGVLPGM
GGSQRLTRAVGKAKAMDLCLTGRMMDAAEAERAGLVSRVVPADKLLDEALAAATTIASFSLPAVMMAKEA
VNRAYETTLAEGLLFERRLFHSLFATEDQKEGMAAFVEKRKPVFKHR
>gnl|CDD|168278 PRK05864, PRK05864, enoyl-CoA hydratase; Provisional
VAGYRSTMSLVLVDHPRPEIALITLNRPERMNSMAFDVMVPLKEALAEVSYDNSVRVVVLTGAGRGFSSG
ADHKSAGVVPHVEGLTRPTYALRSMELLDDVILALRRLHQPVIAAVNGPAIGGGLCLALAADIRVASSSA
YFRAAGINNGLTASELGLSYLLPRAIGSSRAFEIMLTGRDVDAEEAERIGLVSRQVPDEQLLDTCYAIAA
RMAGFSRPGIELTKRTLWSGLDAASLEAHMQAEGLGQLFVRLLTANFEEAVAARAEKRPPVFTDDK
>gnl|CDD|235630 PRK05865, PRK05865, sugar epimerase family protein
MRIAVTGASGVLGRGLTARLLSQGHEVVGIARHRPDSWPSSADFIAADIRDATAVESAMTGADVVAHCAW
VRGRNDHINIDGTANVLKAMAETGTGRIVFTSSGHQPRVEQMLADCGLEWVAVRCALIFGRNVDNWVQRL
FALPVLPAGYADRVVQVVHSDDAQRLLVRALLDTVIDSGPVNLAAPGELTFRRIAAALGRPMVPIGSPVL
RRVTSFAELELLHSAPLMDVTLLRDRWGFQPAWNAEECLEDFTLAVRGRIGLGKRTFSLPWRLANIQDLP
AVDSPADDGVAPRLAGPEGANGEFDTPIDPRFPTYLATNLSEALPGPFSPSSASVTVRGLRAGGVGIAER
LRPSGVIQREIAMRTVAVFAHRLYGAITSAHFMAATVPFAKPATIVSNSGFFGPSMASLPIFGAQRPPSE
SSRARRWLRTLRNIGVFGVNLVGLSAGSPRDTDAYVADVDRLERLAFDNLATHDDRRLLSLILLARDHVV
HGWVLASGSFMLCAAFNVLLRGLCGRDTAPAAGPELVSARSVEAVQRLVAAARRDPVVIRLLAEPGERLD
KLAVEAPEFHSAVLAELTLIGHRGPAEVEMAATSYADNPELLVRMVAKTLRAVPAPQPPTPVIPLRAKPV
ALLAARQLRDREVRRDRMVRAIWVLRALLREYGRRLTEAGVFDTPDDVFYLLVDEIDALPADVSGLVARR
RAEQRRLAGIVPPTVFSGSWEPSPSSAAALAAGDTLRGVGVCGGRVRGRVRIVRPETIDDLQPGEILVAE
VTDVGYTAAFCYAAAVVTELGGPMSHAAVVAREFGFPCVVDAQGATRFLPPGALVEVDGATGEIHVVELA
SEDGPALPGSDLSR
>gnl|CDD|235631 PRK05866, PRK05866, SDR family oxidoreductase
MSKRPLRRLTDQLTLAGMRPPISPQLLINRPPRQPVDLTGKRILLTGASSGIGEAAAEQFARRGATVVAV
ARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDILINNAGRSIRRPLAESLDRW
HDVERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATWGVLSEASPLFSVYNASKAALSAVSRVIETEW
GDRGVHSTTLYYPLVATPMIAPTKAYDGLPALTADEAAEWMVTAARTRPVRIAPRVAVAARALDSVAPRA
VNALMQRQGEQPN
>gnl|CDD|135631 PRK05867, PRK05867, SDR family oxidoreductase
VLDLFDLHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQH
QQVTSMLDQVTAELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGGV
IINTASMSGHIINVPQQVSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTEYQPLWE
PKIPLGRLGRPEELAGLYLYLASEASSYMTGSDIVIDGGYTCP
>gnl|CDD|180297 PRK05868, PRK05868, FAD-binding protein
MKTVVVSGASVAGTAAAYWLGRHGYSVTMVERHPGLRPGGQAIDVRGPALDVLERMGLLAAAQEHKTRIR
GASFVDRDGNELFRDTESTPTGGPVNSPDIELLRDDLVELLYGATQPSVEYLFDDSISTLQDDGDSVRVT
FERAAAREFDLVIGADGLHSNVRRLVFGPEEQFVKRLGTHAAIFTVPNFLELDYWQTWHYGDSTMAGVYS
ARNNTEARAALAFMDTELRIDYRDTEAQFAELQRRMAEDGWVRAQLLHYMRSAPDFYFDEMSQILMDRWS
RGRVALVGDAGYCCSPLSGQGTSVALLGAYILAGELKAAGDDYQLGFANYHAEFHGFVERNQWLVSDNIP
GGAPIPQEEFERIVHSITIKDY
>gnl|CDD|235632 PRK05869, PRK05869, enoyl-CoA hydratase; Validated
MNEFVNVVVSDGSQDAGLATLLLSRPPTNALTRQVYREIVAAANELGRRDDVAAVILYGGHEIFSAGDDM
PELRTLSAQEADTAARVRQQAVDAVAAIPKPTVAAITGYALGAGLTLALAADWRVSGDNVKFGATEILAG
LAPSGDGMARLTRAAGPSRAKELVFSGRFFDAEEALALGLIDEMVAPDDVYDAAAAWARRFLDGPPHALA
AAKAGISDVYEL
>gnl|CDD|180298 PRK05870, PRK05870, enoyl-CoA hydratase; Provisional
MMDPVLLDVDDGVALITVNDPDRRNAVTAEMSAQLRAAVAAAEADPDVHALVVTGAGKAFCAGADLTALG
AAPGRPAEDGLRRIYDGFLAVASCPLPTIAAVNGAAVGAGLNLALAADVRIAGPKALFDARFQKLGLHPG
GGATWMLQRAVGPQVARAALLFGMRFDAEAAVRHGLALMVADDPVAAALELAAGPAAAPRELVLATKASM
RATASLAQHAAAVEFELGPQAASVQSPEFAARLAAAQRR
>gnl|CDD|235633 PRK05872, PRK05872, short chain dehydrogenase; Provisional
GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLTVVADVTDLA
AMQAAAEEAVERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQ
VSSLAAFAAAPGMAAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRDADADLPAFRELRAR
LPWPLRRTTSVEKCAAAFVDGIERRARRVYAPRWVRLMQWLRPVLVTRLGQREVRRFVPRLLPRMDAEVA
ALGRADSARTASLENR
>gnl|CDD|102036 PRK05874, PRK05874, L-fuculose-phosphate aldolase; Validated
MNFVDDPESAVLAAAKDMLRRGLVEGTAGNISARRSDGNVVITPSSVDYAEMLLHDLVLVDAGGAVLHAK
DGRSPSTELNLHLACYRAFDDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRCTEYAASGTPE
VGRNAVRALEGRAAALIANHGLVAVGPRPDQVLRVTALVERTAQIVWGARALGGPVPIPEDVCRNFTGVY
GYLRANP
>gnl|CDD|180300 PRK05875, PRK05875, short chain dehydrogenase; Provisional
MQLSFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALKGAGAVRYEPADVTDE
DQVARAVDAATAWHGRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGS
FVGISSIAASNTHRWFGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESPELSADY
RACTPLPRVGEVEDVANLAMFLLSDAASWITGQVINVDGGHMLRRGPDFSSMLEPVFGADGLRGVV
>gnl|CDD|135637 PRK05876, PRK05876, short chain dehydrogenase; Provisional
MDGFPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEV
THLADEAFRLLGHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGHVVF
TASFAGLVPNAGLGAYGVAKYGVVGLAETLAREVTADGIGVSVLCPMVVETNLVANSERIRGAACAQSST
TGSPGPLPLQDDNLGVDDIAQLTADAILANRLYVLPHAASRASIRRRFERIDRTFDEQAAEGWRH
>gnl|CDD|235634 PRK05877, PRK05877, aminodeoxychorismate synthase component I; Provisional
VLRALGAATARLGLPPPAALTGDWFGSRAVIAPSVSIRPVAPDDVFAVPPGTAGAAAPGAVGGGWFGYLS
YPDAGADGRPPRIPEAAGGWTDHVLRRDRDGQWWYESLSGAPDPDWLASALATTRARPAPPCRIDWTPPD
RAAHRDGVLACLEAIAAGEVYQACVCTQFTGTVTGSPLDFFADGVARTAPARAAYLAGDWGAVASLSPEL
FLRRRGSVVTSSPIKGTLPLDADPSALRASAKDVAENIMIVDLVRNDLGRVARTGTVTVPELLVVRPAPG
VWHLVSTVSAQVPDELPMSDLLDATFPPASVTGTPKLRARELISQWEPVRRGIYCGTVGLASPVAGCELN
VAIRTVEFDADGNAVLGVGGGITADSDPDAEWQECLHKAAPIVGLPAAATSAPAR
>gnl|CDD|235635 PRK05878, PRK05878, pyruvate phosphate dikinase; Provisional
PAGTLENAVVLLDGGANQPRELLGGKGHGIDMMRRLGLPVPPAFCITTEVCVRYLADPGSTIDAIWDDVL
DRMRWLEAETGRTFGRGPRPLLVSVRSGAAQSMPGMMDTILNLGINDAVEQALAAEGGDPDFAADTRRRF
TEMYRRIVGSGSPPPDDPYEQLRAAIEAVFASWNSPRAVAYRRHHGLDDDGGTAVVVQAMVFGNLDANSG
TGVLFSRNPITGANEPFGEWLPGGQGEDVVSGLVDVAPITALRDEQPAVYDELMAAARTLERLGRDVQDI
EFTVESGKLWLLQTRSAKRSAQAAVRLALQLHDEGLIDDAEALRRVTPTHVETLLRPSLQPEARLAAPLL
AKGLPACPGVVSGTAYTDVDEALDAADRGEPVILVRDHTRPDDVHGMLAAQGIVTEVGGATSHAAVVSRE
LGRVAVVGCGAGVAAALAGKEITVDGYEGEVRQGVLALSAWSESDTPELRELADIAQRISPLRAHASGDY
PRLDDDSDDAVRAALAAGHADVVSDTPLIVMLTALRLQGA
>gnl|CDD|180303 PRK05880, PRK05880, F0F1 ATP synthase subunit C; Validated
MDPTIAAGALIGGGLIMAGGAIGAGIGDGVAGNALISGVARQPEAQGRLFTPFFITVGLVEAAYFINLAF
MALFVFATPVK
>gnl|CDD|180304 PRK05883, PRK05883, acyl carrier protein; Validated
PGVASFAMTSSPSTVSATLLSILRDDLNVDLTRVTPDARLVDDVGLDSVAFAVGMVAIEERLGVALSEED
LLSCDTVGDLEAAIAAKVRDE
>gnl|CDD|135642 PRK05884, PRK05884, SDR family oxidoreductase
VEVLVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKELDVDAIVCDNTDPASLEEARGLFPHHL
DTIVNVPAPSWDAGDPRTYSLADTANAWRNALDATVLSAVLTVQSVGDHLRSGGSIISVVPENPPAGSAE
AAIKAALSNWTAGQAAVFGTRGITINAVACGRSVQPGYDGLSRTPPPVAAEIARLALFLTTPAARHITGQ
TLHVSHGALAHFG
>gnl|CDD|235636 PRK05886, yajC, preprotein translocase subunit YajC; Validated
MESLVLFLPFLLIMGGFMYFASRRQRKAMQATIDLHESLQPGDRVHTTSGLQATIVGITDDTVDLEIAPG
VVTTWMKLAVRDRILPDDEDDEELNADLDKDVDDVAGER
>gnl|CDD|235637 PRK05888, PRK05888, NADH-quinone oxidoreductase subunit NuoI
IKQYLKSMLLKELLKGLGVTLKYFFKKKVTIQYPEEKLPLSPRFRGRHALRRDPNGEERCIACKLCAAIC
PADAITIEAAEREDGRRRTTRYDINFGRCIFCGFCEEACPTDAIVETPDFELATETREELIYDKEKLLAN
GDRVEREIAPGKAADANYRGEAEA
>gnl|CDD|180306 PRK05889, PRK05889, biotin/lipoyl-binding carrier protein
MAEDVRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI
S
>gnl|CDD|180307 PRK05892, PRK05892, nucleoside diphosphate kinase regulator; Provisional
MKVKSKGLAPAARDHLEAELARLRARRDRLAVEVNDRGMIGDHGDQAEAIQRADELARLDDRINELDRRL
RTGPTPWSGSETLPGGTEVTLRFPDGEVETMHVISVVEETPVGREAETLTADSPLGQALAGHQAGDTVTY
STPQGPAQVELLAVKLPS
>gnl|CDD|235638 PRK05896, PRK05896, DNA polymerase III subunits gamma and tau; Validated
MSEITFYRKYRPHNFKQIIGQELIKKILVNAILNNKLTHAYIFSGPRGIGKTSIAKIFAKAINCLNPKDG
DCCNSCSVCESINTNQSVDIVELDAASNNGVDEIRNIIDNINYLPTTFKYKVYIIDEAHMLSTSAWNALL
KTLEEPPKHVVFIFATTEFQKIPLTIISRCQRYNFKKLNNSELQELLKSIAKKEKIKIEDNAIDKIADLA
DGSLRDGLSILDQLSTFKNSEIDIEDINKTFGLVDNNKKINLIELIQKNDIEELRNLINELESKGINFEA
FCRDLINLLIDLLVYQKTKNINLLKKLSKEQLKTLNLEKQKLLSIEFNTNFLLNNFVSLINRLKASVNQV
FEFEIYLYKIINANPDKLENKKIEISIKPEKKTINNSQIITTKKINIVEESNKNSVHFDTLYKTKIFYHK
KKINQNNKEQDIKKEELLEKEFVKKSEKIPKNDELLDNLELAKQKFFNKDIELSKNMLQKFNKFKNEESA
ENSFIDIIKQADLVLWVSPNALILGVEDLGLIELINKVNESFEFIKTIFKKFNKNKLVIAISKKQATKIT
NIKNQKLKTNIINDVDIDDLKMLIKKEKTRKQEVDALLSEIEDEE
>gnl|CDD|135648 PRK05898, dnaE, DNA polymerase III subunit alpha
MFINLNTHSHYSLLSSTLSIDDIIKFALDNNQPYVCLTDLNNLYGCIEFYDKAKAHNLIPIIGLEIEYQS
TNATLVLYAKNYNGYLNLIKISSFIMTNKEFEIQDYLDDLFIVCKKGTFVFKSPNFYQTHNQNAPNAIAF
NSVFYANKNDKIVFNAMLAIKNDLKIDELKNCQDFDNNHFLNDNEAQSLFSPIQLDNLNKVLNELKVEIH
DLPINIIKYDKQNSIISSEILKQLCISGLNKRLNANDGQVKKIYVKRLKYELDIINEKQFDDYFLIVYDF
INFAKSNGIIIGPGRGSAAGSLIAYLLHITDIDPIKYNLIFERFLNPTRKSMPDIDTDIMDERRDEVVEY
LFEKYGNDHVAHIITFQRIKAKMAIRDVGRILGIDLKVIDKICKNIKPDYEEDLDLAIKKNTILKEMYVL
HKELFDLAKKIINAPRQIGTHAAGVVLSNSLLTNIIPIQLGINDRPLSQYSMEYLERFGLIKMDLLGLKN
LTIIDNVLKLIKENQNKKIDLFNINLNDKNVFEDLAKGRTNGIFQLESPGMKKVLKKVKPQNIEDISIVS
ALFRPGPQQNIKTFVERRFKREEFSYWNEATKKILEPTHGIIVYQEQVINLVKTIANFDIATADNFRRAI
SKKDEKILIQLKKDFIEGALKNNYKQPLVNQIFEYIFSFADYGFNHSHSLAYSYISYWMAYLKHYYPLEF
LSILLSHTSASKDKLLSYLNEAKEFNISIKKPDINYSSNSFVLDTQKQIIRFGFNTIKGFGDELLKKIKS
ALQNKTFSDFISYIDALKKNNVSLSNIEILINVGTFDSFKLSRLFLLNNLPEIFEKTSLNGHFFELNLVG
LEYAKDMSVKERFLKKEIQYLGIDLNSLNYANYKNEIDYNELKYTIKDIKEIELKNTNYETNIFAQVYEI
KQSKTKNGNLSFYLETLINNKKKTITIFQHSKYLIDEIDIGGIYVRGVKLLNHLNFIDNVK
>gnl|CDD|235639 PRK05899, PRK05899, transketolase; Reviewed
SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGH
GSMLLYSLLHLAGYDLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAAL
FNRPGLDIVDHYTYVLCGDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFE
AYGWHVIEVDGHDVEAIDAAIEEAKASTKPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELG
WDYRKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPEDYSGRYIHYGVREFAMAAIANGLAL
HGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRP
ADANETAAAWKYALERKDGPSALVLTRQNLPVLERTAQEEGVAKGGYVLRDDPDVILIATGSEVHLALEA
ADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVGLDGKVLGIDTFGA
SAPADELFKEFGFTVENIVAAAKELL
>gnl|CDD|235640 PRK05901, PRK05901, RNA polymerase sigma factor; Provisional
MTTASTKAELAAEEEAKKKLKKLAAKSKSKGFITKEEIKEALESKKKTPEQIDQVLIFLSGMVKDTDDAT
ESDIPKKKTKTAAKAAAAKAPAKKKLKDELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDD
DLDDDDIDDDDDDEDDDEDDDDDDVDDEDEEKKEAKELEKLSDDDDFVWDEDDSEALRQARKDAKLTATA
DPVKAYLKQIGKVKLLNAEEEVELAKRIEAGLYAEELLAEGEKLDPELRRDLQWIGRDGKRAKNHLLEAN
LRLVVSLAKRYTNRGLSFLDLIQEGNLGLIKAVEKFDYTKGYKFSTYATWWIRQAITRAMADQARTIRIP
VHMVETINKLGRIERELLQELGREPTPEELAKEMGFTPEKVREIQKYNREPISLDKTIGKEGDSQFGDFI
EDSEAVSPVDAVSFTLLQDQLQEVLETLSEREAGVIRMRFGLTDGQPKTLDEIGQVYGVTRERIRQIESK
TLRKLRHPSRSQVLRDFLD
>gnl|CDD|235641 PRK05904, PRK05904, coproporphyrinogen III oxidase; Provisional
IFNKKTKHLYIHIPFCQYICTFCDFKRILKTPQTKKIFKDFLKNIKMHIKNFKIKQFKTIYLGGGTPNCL
NDQLLDILLSTIKPYVDNNCEFTIECNPELITQSQINLLKKNKVNRISLGVQSMNNNILKQLNRTHTIQD
SKEAINLLHKNGIYNISCDFLYCLPILKLKDLDEVFNFILKHKINHISFYSLEIKEGSILKKYHYTIDED
KEAEQLNYIKAKFNKLNYKRYEVSNWTNNFKYISKHNLAYWRTKDWAAIGWGAHGFENNIEYFFDGSIQN
WILIKKVLTDHELYQQILIMGLRLKDGLDLNKEINKEAYLYFKNKLKHISINKNNHLRADNIDLLNLSII
DIF
>gnl|CDD|235642 PRK05905, PRK05905, 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase
MKYKSYAKINLGLSIYKKCKKVTKHKLESIFILVENVYDDIEIEKIEKNIDDIHYFDETNEILVYSRLIL
VKTLEWLRDKYNIKNHFKIKIKKRIPIGSGLGSGSSNAAVLMKWILEFEGINEINYKDVVNKLGSDIPFF
LSGYKTAYISDYGSQVEDLIGQFKLTYKVIFMNVNVSTKKVFEKFDDNQHVIKNNFKTIIKNLKENIVVN
IHNDLQEPCFELYPNLLYKYNELLNDGFYTILSGAGSSFIVIKKINEN
>gnl|CDD|168292 PRK05906, PRK05906, lipid A biosynthesis lauroyl acyltransferase; Provisional
MFKRLRTGKKTIVDHLVYYLGLGVITILRLLPRSSLRLFGKGLGTLLFYFISDYRKTALTNLALAFPEKS
FAERYQIARQSVQHVIITFLELLAVEKLAGHIDELIAIATSEDAPEGFFPEEVSSQQELEHTFSRLDEQE
GAILFCGHQANWELPFLYITKRYPGLAFAKPIKNRRLNKKIFSLRESFKGKIVPPKNGINQALRALHQGE
VVGIVGDQALLSSSYSYPLFGSQAFTTTSPALLAYKTGKPVIAVAIYRKPNGYLVVPSKKFYANKSLPIK
ESTEQLMDRLMRFLEKGIACKPEQWMWLHKRWKRKLRHKFKKKYAYSHILVIVKGTSLQALQRFLIELAE
FYSGASLSLALINAADETVLANSFPPYSLQFFSSEEELLALPNSFPAIFDLFGLSRKLRKHFKRTGSRKI
YTRNELEKSLLHPQSLIQSFHKLLRRVDTRSKKG
>gnl|CDD|235643 PRK05907, PRK05907, hypothetical protein; Provisional
SIHITSFKDFSQYYEEKRPAVIVIGSSSEEDKDIFIELLVSGRKSEFDGQGLLQQELLSWTEHFGLFASQ
ETIGIYQAEKMSSSTQEFLIRYARNPNPHLTLFLFTTKQECFSSLSKKLSSALCLSLFGEWFADRDKRIA
QLLIQRAKELGISCSLGLASLFVSKFPQTGLFEILSEFQKLLCQMGKKESLEASDIQSFVVKKEAASLWK
LRDALLRRDRVEGHSLLRSLLSDMGEDPLGIIAFLRSQCLYGLRSIEEQSKERKHRIFVAYGKERLLQAL
NLLFYAESLIKNNVQDPILAVETLVIRMTNL
>gnl|CDD|168293 PRK05910, PRK05910, type III secretion system protein; Validated
VVNNKRGSSWKMVAIPLCILFTLIFPLPQWLLDFGLCINFALSLSIVFWVFSLRSSASARLFPSLFLYLC
LLRLGLNLASTRWILSSGWASPLIFSLGNFFSLGSLPAALTACLLLFLVNFLVITKGSERIAEVRARFSL
EALPGKQMSLDADLVSGRASYSRVSKQKNSLLEESDFFSAMEGVFRFVKGDAIMSCILLGVNILAATFLG
RATGYAVGDLWLTVLGDALVSQVPALLTSCAAATLISKVGEKESLLQHLLDYYEQSRQHFRFIALLLCSL
ACIPGAPKAPILGFSVLLFLAYKNPSSGETLLFQKERFEFVELALPDEGVGNPANLYRAAREEIFQELGV
VFPEEIVVRHVESSPRLIFSGQEVYLRELSCPAILPSLRNLAPEAISERFVKRLVEEFQEVAGISIEEII
PKKISENSLVFLLRALVRERVSLHLFPKILEAIAVYGSQGKSSEELVEKVRKYLGKQIGRSLWNRQDTLE
VITIDSHVEQFIRDSYSKSNPDMNEKVVAQVKSLLERSGEGNFRAIVTGCETRFELKKMVDPYFPDLLVL
SHSELPEEIPISLLGAVSDEVLLS
>gnl|CDD|235644 PRK05911, PRK05911, RNA polymerase sigma factor sigma-28; Reviewed
MKTQKTQNIAETWQLYWSTQEIEYRDVLIEFYLPLVKNVAHRLISGMPSHVKTEDLYASGVEGLVRAVER
FDPEKSRRFEGYALFLIKAAIIDDLRKQDWVPRSVHQKANKLADAMDSLRQSLGKEPTDGELCEYLNISQ
QELSGWFSSARPALILSLNEEFPCQSDDEAGLALEERIADERAETGYDVVDKKEFSSILAEAILALEEKE
RKVMALYYYEELVLKEIGKILGVSESRVSQIHSKALLKLRATLSAFL
>gnl|CDD|102059 PRK05917, PRK05917, DNA polymerase III subunit delta'; Validated
MESAAWEALIQRVRDQKVPSAIILHGQDLSNLSARAYELASLILKETSPEAAYKISQKIHPDIHEFSPQG
KGRLHSIETPRAIKKQIWIHPYESPYKIYIIHEADRMTLDAISAFLKVLEDPPQHGVIILTSAKPQRLPP
TIRSRSLSIHIPMEEKTLVSKEDIAYLIGYAQGKESVTEVGQIVKGSADTDKQVLRDKTKAMLEVLLQLF
RDRFLLALKVPASALAYPDLLKEILTLPVLPLEKVLSIIERAVQALDNSSSAPSCLEWVALQLWSLKNRQ
QMLIRNRRGS
>gnl|CDD|180312 PRK05920, PRK05920, aromatic acid decarboxylase; Validated
SKMKRIVLAITGASGAIYGVRLLECLLAADYEVHLVISKAAQKVLATETGLKLPAVPDLAEAFLREQLGA
AAGQLRVHGKDDWGAPIASGSFRTDGMVIAPCSMGTLAAIAHGLSDNLIERAADVVLKERRKLILVPRET
PLSLIHLENMLKLAEAGAIILPAIPAFYHKPQTIDDLVDFVVARILDLLGIDLDLIKRWGGPKQ
>gnl|CDD|102061 PRK05922, PRK05922, type III secretion system ATPase; Validated
MTHLQEEKLLIHQWQPYRECGLLSRVSGNLLEAQGLSACLGELCQISLSKSPPILAEVIGFHNRTTLLMS
LSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEI
FPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGREVREYIEQHKEGLA
AQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYA
ASVFHHVSEFTERAGNNDKGSITALYAILHYPNHPDIFTDYLKSLLDGHFFLTPQGKALASPPIDILTSL
SRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDAHLDRAVKLLPSIKQFLSQPLSSYCAL
HNTLKQLEALLKHE
>gnl|CDD|235646 PRK05925, PRK05925, aspartate kinase; Provisional
MAPLVYKFGGTSLGTAESIRRVCDIICKEKPSFVVVSAVAGVTDLLEEFCRLSKGKREALTEKIREKHEE
IAKELGIEFSLSPWWERLEHFEDVEEISSEDQARILAIGEDISASLICAYCCTYVLPLEFLEARQVILTD
DQYLRAVPDLALMQTAWHELALQEDAIYIMQGFIGANSSGKTTVLGRGGSDFSASLIAELCKAREVRIYT
DVNGIYTMDPKIIKDAQLIPELSFEEMQNLASFGAKVLHPPMLKPCVRAGIPIFVTSTFDVTKGGTWIYA
SDKEVSYEPRIKALSLKQNQALWSVDYNSLGLVRLEDVLGILRSLGIVPGLVMAQNLGVYFTIDDDDISE
EYPQHLTDALSAFGTVSCEGPLALITMIGAKLASWKVVRTFTEKLRGYQTPVFCWCQSDMALNLVVNEEL
AVAVTELLHNDYVKQKFSVV
>gnl|CDD|168296 PRK05926, PRK05926, hypothetical protein; Provisional
MTTLPARILPKSSWLKTLFDDYLSGARLSEEDALQLLLLTDAEDQRALWSFADLIRANRVGDTVYYSSTL
YLYPTNFCQFNCTFCSFYAKPGDPKGWFYTPDQLVQSIKENPSPITETHIVAGCFPSCNLAYYEELFSKI
KQNFPDLHIKALTAIEYAYLSKLDNLPVKEVLQTLKIAGLDSIPGGGAEILVDEIRETLAPGRLSSQGFL
EIHKTAHSLGIPSNATMLCYHRETPEDIVTHMSKLRALQDKTSGFKNFILLKFASENNALGKRLRKMGSR
HSIPPASIIAVARLFLDNFPNIKALWNYLGIEVALHLLSCGANDLSSTHQGEKVFQMASSQEPIKMDIEG
MAHLITQQGRIPCLTNSKTV
>gnl|CDD|135660 PRK05927, PRK05927, dehypoxanthine futalosine cyclase
MNLPARISFQEGLELFLYSPLEELQEHADSLRKQRYPQNTVTYVLDANPNYTNICKIDCTFCAFYRKPHS
SDAYLLSFDEFRSLMQRYVSAGVKTVLLQGGVHPQLGIDYLEELVRITVKEFPSLHPHFFSAVEIAHAAQ
VSGISTEQALERLWDAGQRTIPGGGAEILSERVRKIISPKKMGPDGWIQFHKLAHRLGFRSTATMMFGHV
ESPEDILLHLQTLRDAQDENPGFYSFIPWSYKPGNTALGRRVPHQASPELYYRILAVARIFLDNFDHIAA
SWFGEGKEEGAKGLHYGADDFGGTILDESVHKCTGWDLQSSEEEICAMILSEGFIPVERNTFYRPISLAR
>gnl|CDD|235647 PRK05928, hemD, uroporphyrinogen-III synthase; Reviewed
MMKILVTRPSPKAEELVELLRELGFVALHFPLIEIEPGRQLPQLAAQLAALGADWVIFTSKNAVEFLLSA
LKKKKLKWPKNKKYAAIGEKTALALKKLGGKVVFVPEDGESSELLLELPELLLKGKRVLYLRGNGGREVL
GDTLEERGAEVDECEVYERVPPKLDGAELLARLQSGEVDAVIFTSPSTVRAFFSLAPELGRREWLLSCKA
VVIGERTAEALRELGIKVIIVPDSADNEALLRALKELLK
>gnl|CDD|235648 PRK05932, PRK05932, RNA polymerase factor sigma-54; Reviewed
MKQSLQLRQSQKLAMTPQLQQAIRLLQLSTLELQQELEQALEENPLLELEDDTADLEQKEIPEELPLDTS
WDEIYTAGSPSGSGGDYIDDELPVYQGETTESLQDHLLEQIELTPFSETDRAIATYIIDALDDEGYLTED
LEEIAESLGVELDEVEAVLKRIQSFDPAGVGARDLQECLLLQLEQLDDTPRLDEAMEIISDHLDLLARRD
FRTLAKKLGVKEEDLQEALDLIRSLDPKPGAGFGTEEPEYVVPDVFVRKINGGWLVELNPDSLPRLRINQ
EYAALVSRSARDEDKQFLREKLQEAKWLIKSLEQRKETLLKVARCIVEQQRDFFEHGEEALKPLVLKDIA
EELGMHESTISRATTNKYMATPRGIFELKYFFSSAVSTDGGGEASSTAIRALIKKLIAAENPKKPLSDSK
IAELLKEQGIDVARRTVAKYREALNIPSSSQRKRL
>gnl|CDD|180315 PRK05933, PRK05933, type III secretion system protein; Validated
MAVAAEPSASWLKSRNEFLSSLQKTEEGVSFPVFPKELCQQKLKEKFRLEDVELSIESRGSLSAAAAVQE
FGEHLLLQPFLAQPFESGEFYFVTSEEDLQALMVAVFNDSSLASYFYEKDKLLGFHYYFVAEICKLLQEL
PWIPSLSVKVTGDAAFSARALQGSYQVVDVSCRLDGKCVRFRLLVPETTAQSCQKFLSEKDQAFDMHKID
LQTPITLSVEVGYCQLTQEEWHQVVPGSFILLDSCLYDPDTEESGALLTIQRHQFFGGRFLDKQSGEFKI
TSYPNLQPEDPPEEPSEGGPAAPLPGATKLVAEVARYSLSVGEFLKLGPGSILQFDGVHPTLGVDIILNG
AKVGRGEIIALGDVLGIRVLEV
>gnl|CDD|168300 PRK05934, PRK05934, type III secretion system protein; Validated
MFFQFLKKKIASLGISPLGYLLAAILIGFAILFGKPSSPSPTPTQVSTEKTPGNWLKLSQLGNPKLIESL
AKKEQLEKDLTMFHPVAQATVALSLETEDDPMSPAEISVILSLPKAETLSPSLLHSITDYLTSSVPGLTK
EHITLSDNLGNLYSPLFEQSNSLLTTSLERYLGKIFPKEHFALNYLPVADEPTLQLTVNEDYLATLPKEA
REKLLSHMQEILKSAFPEMHPIVIEIVPFLKTAHKTSRLSKILLGITILLLSLGILALASFYLAFHAYER
VSQEKEKIKQGINIPKLIEIMQKESPEKIALILSYLDPKKAEELLNKLPEDMKHQVLKLKT
>gnl|CDD|235649 PRK05935, PRK05935, biotin--protein ligase; Provisional
MKVIYYEIAETPSTNTTAKEGMHLWDPYALTVISTREQTAGKGKFGKSWHSSDQDLLASFCFFITVLNID
VSLLFRLGTEAVMRLGEDLGITEAVIKWPNDVLVHGEKLCGVLCETIPVKGGLGVILGIGVNGNTTKDEL
LGIDQPATSLQELLGHPIDLEEQRERLIKHIKHVLIQTLPKLLARESNHG
>gnl|CDD|102071 PRK05937, PRK05937, 8-amino-7-oxononanoate synthase; Provisional
MKESLSIDFVTNDFLGFSRSDTLVHEVEKRYRLYCRQFPHAQLGYGGSRAILGPSSLLDDLEHKIAHFHG
APEAFIVPSGYMANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQR
SFGRIFIFVCSVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLVTY
SKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPPHLLISIQVAYDFLSQEGELARKQLFRLKEYFAQK
FSSAAPGCVQPIFLPGISEQELYSKLVETGIRVGVVCFPTGPFLRVNLHAFNTEDEVDILVSVLATYLEK
YQKNVVIGHESTMQRTLCDN
>gnl|CDD|235650 PRK05939, PRK05939, cystathionine gamma-synthase family protein
RLAGIEHGAVHKPIHTSVTYGYEDARDLIDVFQGKKPGFTYARQGTPTTAALEAKITKMEGGVGTVCFAT
GMAAIAAVFLTLLRAGDHLVSSQFLFGNTNSLFGTLRGLGVEVTMVDATDVQNVAAAIRPNTRMVFVETI
ANPGTQVADLAGIGALCRERGLLYVVDNTMTSPWLFRPKDVGASLVINSLSKYIAGHGNALGGAVTDTGL
FDWSAYPNIFPAYRKGDPQQWGLTQIRKKGLRDMGATLSSEAAHRIAIGAETLALRVDRSCSNALALAQF
LEAHPKVARVYYPGLASHPQHARATELFRHYGGLLSFELADGIDCFDFLNRLKLVIKATHLGDTRTLVIP
VAPTIYYEMGAERRASMGIADSLIRVSVGIEDEADLIADFEQALDAT
>gnl|CDD|235651 PRK05940, PRK05940, anthranilate synthase component I
MTDILQPWHWRSLPLNGRTGSEIFERLFGQQGIATLLESPYPTPADYPPLSRYSICAGSPRKPRLWTPKL
GEILPFLRQLLARSLDPSALPEHLPFTGGWLGWLGYDLAWEIERLPHLNPDPLPFPVAYWYEPESFAILD
HQEQILWLAASDPSQLDRLEQQLEQPTPEPDLPLDLRTPPSSLIFYTTQQEYEAAVRQAKKYIQAGDIFQ
ANLSLRFQTTTSADSWQIYRRLQQINPSPFASYWRTPWGDVVSCSPERLVQLQGNQAQTRPIAGTRPRGK
TPAEDQQLAEELLSNIKERAEHIMLVDLERNDLGRVCQWGSVEVDELLTIERYSHVIHLVSNVVGTLQPN
RDAIDLIRALFPGGTITGCPKVRCMEIIEELEPVRRNLFYGSCGYLDQRGNLDLNILIRTLLYTPLSRGL
STIWGQVGAGIVADSDPEKEWLESLQKAKAQLAALNLVRSQNS
>gnl|CDD|180317 PRK05942, PRK05942, aspartate aminotransferase; Provisional
MSLDWITPADRLQALPPYVFARLDELKARAREQGLDLIDLGMGNPDGAAPQPVIEAAIAALADPQNHGYP
PFEGTASFRQAITDWYHRRYGVELDPDSEALPLLGSKEGLTHLALAYVNPGDVVLVPSPAYPAHFRGPLI
AGAQIYPIILKPENDWLIDLSSIPEEVAQQAKILYFNYPSNPTTATAPREFFEEIVAFARKYEIMLVHDL
CYAELAFDGYQPTSLLEIPGAKDIGVEFHTLSKTYNMAGWRVGFVVGNRHIIQGLRTLKTNLDYGIFSAL
QKAAETALQLPDSYLQQVQERYRTRRDFLIQGLGELGWNIPPTKATMYLWVPCPVGMGSTDFALNVLQKT
GVVVTPGNAFGEGGEGYVRISLIADCDRLGEALDRLKQAGIRYQ
>gnl|CDD|180318 PRK05943, PRK05943, 50S ribosomal protein L25; Reviewed
MFTINAEVRPEQGKGASRRLRRAGKFPAIIYGGNEAPVSIVLDHKDVINLQAKAEFYKEVITLVIDGKEV
KVKVQAVQRHPFKPKLEHIDFVRA
>gnl|CDD|180319 PRK05945, sdhA, succinate dehydrogenase/fumarate reductase flavoprotein subunit
MLEHDVVIVGGGLAGCRAALEIKRLDPSLDVAVVAKTHPIRSHSVAAQGGIAASLKNVDPEDSWEAHAFD
TVKGSDYLADQDAVAILTQEAPDVIIDLEHLGVLFSRLPDGRIAQRAFGGHSHNRTCYAADKTGHAILHE
LVNNLRRYGVTIYDEWYVMRLILEDNQAKGVVMYHIADGRLEVVRAKAVMFATGGYGRVFNTTSNDYAST
GDGLAMTAIAGLPLEDMEFVQFHPTGLYPVGVLISEAVRGEGAYLINSEGDRFMADYAPSRMELAPRDIT
SRAITLEIRAGRGINPDGSAGGPFVYLDLRHMGKEKIMSRVPFCWEEAHRLVGVDAVTEPMPVRPTVHYC
MGGIPVNTDGRVRRSADGLVEGFFAAGECACVSVHGANRLGSNSLLECVVYGRRTGAAIAEYVQGRKLPE
VDEQRYLKEAKQRIQALLDQSGTYRINQLRQQFQDCMTDHCGVFRTEEIMQEGLEKIQQLKQQYEQIYLD
DKGKCWNTELIEALELRSLMVVGEIILTSALNRQESRGAHSREDYPQRDDQNFLKHTLAYYSPAGIDIQY
MPVVITMFEPQERKY
>gnl|CDD|180320 PRK05948, PRK05948, precorrin-2 C(20)-methyltransferase
MTLGTLYGISVGPGDPELITLKGLRLLQSAPVVAFPAGLAGQPGLAEQIIAPWLSPQQIKLPLYFPYVQD
EEQLEQAWQAAADQVWHYLEQGEDVAFACEGDVSFYSTFTYLAQTLQELYPQVAIQTIPGVCSPLAAAAA
LGIPLTLGSQRLAILPALYHLEELEQALTWADVVVLMKVSSVYPQVWQWLKARNLLEQASLVERATTPEQ
VIYRNLEDYPDLRLPYFSLLIIQKRPRN
>gnl|CDD|180321 PRK05949, PRK05949, RNA polymerase sigma factor; Validated
MPTANTNTKTKQPTFSADMVRTYLHEIGRVPLLTHEQEIVYGKQVQQMMSLLEAKEALAKKLGREPSLPE
WAEAVNLSETELKQTLKQGKRAKQKMIEANLRLVVAIAKKYQKRNMEFLDLIQEGTLGLERGVEKFDPTR
GYKFSTYAYWWIRQAITRAIAQQARTIRLPIHITEKLNKIKKTQRELSQKLGRSATPAEIAKELELEPSQ
IREYLSMARQPISLDVRVGDNQDTELSELLEDEGPSPDQYITQELLRQDLNNLLAELTPQQREVLTLRFG
LEDGKELSLAKVGERLNLSRERVRQLEHQALAHLRRRRANVKEYLAS
>gnl|CDD|235652 PRK05950, sdhB, succinate dehydrogenase iron-sulfur subunit; Reviewed
TFKIYRYNPDVDANPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGL
ACITPISDLKKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDTPPPARERLQSPEDREKLDGL
YECILCACCSTSCPSFWWNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVC
PKGLNPTKAIGEIKRMLLERRV
>gnl|CDD|180323 PRK05951, ubiA, prenyltransferase; Reviewed
LQNAKLFFIFTRPWSFVMTAIVAFFSIAYGYYLFRSFDPLLGALMLLGYFLLHASLNVFNDYKDYVLDCD
HHETTGYRQHPIQAGIMTLGHLRVLGIALGAIALQLGWSLVLDRGIGAVTLALLGVFLWTCYMGPPFFLK
YRWLGEHLVFYAWSHMLVMGLIYVWLGNLSSPNLLAGVPLGLLMALVLLSNNLRDIEDDERKGIPTLAVI
FGRRGAALYIFALLSPYVILQILLIAILTPLISLWALLSLLVAYALCLWQLRKFPPDPDEATVQLFMLFG
YLYILATLLSALGFAA
>gnl|CDD|235653 PRK05952, PRK05952, beta-ketoacyl-ACP synthase
MMKVVVTGIGLVSALGDLEQSWQRLLQGKSGIKLHQPFPELPPLPLGLIGNQPSSLEDLTKTVVTAALKD
AGLTPPLTDCGVVIGSSRGCQGQWEKLARQMYQGDDSPDEELDLENWLDTLPHQAAIAAARQIGTQGPVL
APMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTGAYPFDRQREGLVLGE
GGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAH
GTATRLNDQREANLIQALFPHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLN
FVRQAQQSPLQNVLCLSFGFGGQNAAIALGK
>gnl|CDD|180325 PRK05953, PRK05953, Precorrin-8X methylmutase
MEWHVTDAQSLAIIDQEIGKHVLSPAEYEIVRRVIYATADFEYLSLIRFSERALQAGAAALAARTTIVVD
VPMVQVGIAPTLQNTFANPVYCSTETITRPQKEKTRTAWGIETLARRYPEAIFVIGQSQTALTALVELVE
AEEIRPALVIATPAGFIDADDAKERLQDSLVPHITIDGRKGGAVVAVAIIDGLVDLAWQAYGQDREGN
>gnl|CDD|180326 PRK05954, PRK05954, precorrin-8X methylmutase; Provisional
MTMLNHPILEQSFAIIDQEIGPHNFSPLEYAIARRVIHSTADFEFINLLRFSPNAIAAGLAALRQKTPII
TDVTMVKQGIQTLVNKTFQNPIITAIDQVSIPLPGKTRTETGLLKCAQQYPEAIYVIGNAPTALLALCQQ
IRAGRVKPSLVIGVPVGFVSVVEAKQALAQLDVPQIRVEGRKGGSPVAAAIVNALLILAWRDE
>gnl|CDD|235654 PRK05957, PRK05957, pyridoxal phosphate-dependent aminotransferase
MTQFTSRMDAVQSPIIPVVGQLIRENPGTISLGQGVVSYPPPPEAIEALNNFLANPENHKYQAVQGIPPL
LEAITQKLQQDNGIELNNEQAIVVTAGSNMAFMNAILAITDPGDEIILNTPYYFNHEMAITMAGCQPILV
PTDDNYQLQPEAIEQAITPKTRAIVTISPNNPTGVVYPEALLRAVNQICAEHGIYHISDEAYEYFTYDGV
KHFSPGSIPGSGNHTISLYSLSKAYGFASWRIGYMVIPIHLLEAIKKIQDTILICPPVVSQYAALGALQV
GKSYCQQHLPEIAQVRQILLKSLGQLQDRCTLHPANGAFYCFLKVNTDLNDFELVKQLIREYRVAVIPGT
TFGMKNGCYLRIAYGALQKATAKEGIERLVQGLKTIVQQ
>gnl|CDD|235655 PRK05958, PRK05958, 8-amino-7-oxononanoate synthase; Reviewed
MSWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYG
AGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGA
RLSRARVRRYPHNDVDALEALLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTG
VLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAAR
AALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQPLIVGDNERALALAAALQEQGFWVGAIR
PPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL
>gnl|CDD|168315 PRK05962, PRK05962, amidase; Validated
LEATLARLAARAGEEHVFSKLYAERARAEADAADARRRAGRSLGPLDGRIVSIKDLFDVAGEPTLAGSVI
RRDAPPAGADALIVQRLRNAGAVIIGKTHMTEFAFTPVGLNPHYGEPGNAIDPARIPGGSSSGAAVSVAE
GTSEIAIGSDTGGSVRIPAALNGLVGFKPTARRIPLEGAFPLSPSLDSIGPLARTVADCAAADAVMAGEK
PIPLEVLPVAGLRIGLPKGYLLADMEPDVAAAFEASLAALEKAGARIADLAIDDLIARLAEATRIGSIAG
IEASHIHADWLADLDANVDIRVKRPLSRRIKVPLEAYHRLMRTRAALARAMDERLAGFDMFALPATPIVA
PTIASVSEDEEEYDRVENLLLRNTQVANQFDLCSITLPMPGMALPAGLMLTARNGSDRRLLAAAASVEKL
LEHD
>gnl|CDD|180328 PRK05963, PRK05963, beta-ketoacyl-ACP synthase III
VCSSRIAGFGHAVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSDAGIE
RSDIALTLLATSTPDHLLPPSAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRAQGKPVLVVAAN
ILSRRINMAERASAVLFADAAGAVVLAPSAKANSGVLGSQLISDGSHYDLIKIPAGGSARPFAPERDASE
FLMTMQDGRAVFTEAVRMMSGASQNVLASAAMTPQDIDRFFPHQANARIVDKVCETIGIPRAKAASTLET
YGNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGMTGGAVVMRV
>gnl|CDD|235656 PRK05964, PRK05964, adenosylmethionine--8-amino-7-oxononanoate transaminase; Provisional
PEQLMALDLSHVWHPYTQMKLHPPPIPIVRAEGAYLYLADGRELIDAISSWWVATHGHNHPYIDQAIREQ
LDRLDHVIFAGFTHEPAERLAQRLVALTPGGLDHVFFSDSGSVAVEVALKMALQYWRNRGEPGRSRFLSL
RGGYHGDTIGTMSVGDRGGMHALYTPLLFEQVTAPFPPDGYEQATLDALEALLEKHAGEIAAFIVEPLVQ
GAGGMLFYDPRYLAELRRICDRHGVLLIFDEIATGFGRTGTLFACEQAGVSPDIMCLSKGLTGGYLPLAA
TLCTAEIFEAFYSDDRAKAFMHSPSYTANPLACAAANASLDLFEDEPVLERVAALSAGLAEGLEPFRDLP
GVADVRVLGAIGAVELDRPVLERDGPALRAFALERGVLLRPLGNTIYLMPPYIITAEELDRITDAIVEVA
DEL
>gnl|CDD|180330 PRK05965, PRK05965, hypothetical protein; Provisional
MNSNSLIELDRAHLIHPVASYRGHEARGVTVLASAKGATLTDASGHQLLDAFAGLWCVNVGYGQESIVEA
AAEQMRELPYATGYFHFGSEPAIRLAAKLAERAPGSLNHVYFTLGGSDAVDSAVRFIRHYWNATGRPSKK
QFISLERGYHGSSSVGAGLTALPAFHRGFDLPLPWQHKIPSPYPYRNPVGDDPQAIIAASVAALRAKVAE
LGADNVAAFFCEPIQGSGGVIVPPKGWLKAMREACRELGILFVADEVITGFGRTGPLFACEAEGVVPDLM
TVAKGLTSGYVPMGAVLMSDHVYQGIADGAGAAAPVGHGYTYSAHPVSAAVGLEVLRLYHEGGLLANGQK
AGPRFAAGLDALRAHPLVGDVRGRGLLGALELVADKATKTPFDAALDPADRIFDRAYANGLVFRAFGDGV
LGFAPALCCTEGEFDLIFERTRKTLDDVLADPDVRAALK
>gnl|CDD|235657 PRK05967, PRK05967, cystathionine beta-lyase; Provisional
MAKKQLKTEKAGINTRLAHDGNDPGDYHGFVNPPVVHASTVLFPDAETMATRGQKYTYGTRGTPTTDALC
KAIDALEGSAGTILVPSGLAAVTVPFLGFLSPGDHALIVDSVYYPTRHFCDTMLKRLGVEVEYYDPEIGA
GIAKLMRPNTKVVHTEAPGSNTFEMQDIPAIAEAAHRHGAIVMMDNTWATPLYFRPLDFGVDISIHAATK
YPSGHSDILLGTVSANEKCWPQLLEAHGTLGLCAGPDDTYQILRGLRTMGIRLEHHRKSALEIARWLEGR
PDVARVLHPALPSFPGHEIWKRDFSGASGIFSFVLAAGPEKGKAKAHAFLDALEIFGLGYSWGGYESLAL
HVKLGDRTVAKAPYAGPVIRLQIGLEDVPDLKADLERGFAAASAV
>gnl|CDD|168320 PRK05968, PRK05968, hypothetical protein; Provisional
MNDGLDPFDLAALITAHDEGNAFDAVVPPIFQTSLFTFDSYDEMEDVYAGEKVRPIYSRGDNPTVRAFEE
MLAKLEGAEDARGFASGMAAISSTVLSFVEPGDRIVAVRHVYPDAFRLFETILKRMGVEVDYVDGRDEEA
VAKALPGAKLLYLESPTSWVFELQDVAALAALAKRHGVVTMIDNSWASPVFQRPITLGVDLVIHSASKYL
GGHSDTVAGVVAGSKEHIARINAEAYPYLGAKLSPFEAWLLLRGLRTLPLRMKAHEASALEIARRLKAHP
VVERVCHPALANHPPAGLSGTSGLFSFIFREGIDVRAFADALKLFRLGVSWGGHESLVVPAEVVLQQKAQ
PNSAARFGVSPRSVRLHVGLEGTEALWADLEQALAAASR
>gnl|CDD|235658 PRK05972, ligD, ATP-dependent DNA ligase; Reviewed
MAAKPLSEYRRKRDFSKTPEPSGEARRAPSKALRFVIQKHDATRLHYDFRLELDGVLKSWAVPKGPSLDP
ADKRLAVHVEDHPLDYGDFEGTIPKGQYGAGTVIVWDRGYWEPEGDPEEGYAKGKLKFTLHGEKLHGSWV
LVRMRLDRSGKRENWLLIKHRDEFARPGDEYDVLEALPDSVASGRTMAAIAAGKGRAPKPFMTPKGNAGL
AAAARAAAAAAAKKAKKKALPDFLAPQLATLVDRPPSGDGWIYEIKFDGYRILARIEGGEVRLFTRNGLD
WTAKLPALAKAAAALGLPDAWLDGEIVVLDEDGVPDFQALQNAFDEGRTEDLVYFAFDLPFLGGEDLREL
PLEERRARLRALLEAARSDRIRFSEHFDAGGDAVLASACRLGLEGVIGKRADSPYVSGRSEDWIKLKCRA
RQEFVIGGYTDPKGSRSGFGSLLLGVHDDDHLRYAGRVGTGFGAATLKTLLPRLKALATDKSPFAGKPAP
RKARGVHWVKPELVAEVEFAGWTRDGIVRQAVFKGLREDKPAREVVAERPAPPATAEPAAPAAAAAAAAT
AAAAAKAEVAGVRISHPDRVIDPDSGVTKLDLARYYEAVADWMLPHLKGRPVSLVRAPDGIGGELFFQKH
AMPGASPGIELLDVAPDHKPLLQIDRVEGLVAAAQMGAVELHTWNATPDRIEVPDRLVFDLDPGPGVPWK
AVVEAARLMRTRLDELGLESFLKTSGGKGLHVVVPLARRLDWDEVKAFAQAVCQHMARDLPERFLAKMGK
KNRVGKIFLDYLRNGRGATTVAALSPRARPGAPVSMPLTWEELKALLDPKQWTIRTVPARLAKLSDPWAD
YADARQSLTAAMKRLGRKPP
>gnl|CDD|168322 PRK05973, PRK05973, replicative DNA helicase; Provisional
MRLSAPIYHLKRKAKLLSRAQNIPLHEALDRIAAEEGFSSWSLLAAKAAATTPAEELFSQLKPGDLVLLG
ARPGHGKTLLGLELAVEAMKSGRTGVFFTLEYTEQDVRDRLRALGADRAQFADLFEFDTSDAICADYIIA
RLASAPRGTLVVIDYLQLLDQRREKPDLSVQVRALKSFARERGLIIVFISQIDRSFDPSAKPLPDIRDVR
LPNPLDLSLFDKACFLNNGEIQIQAVA
>gnl|CDD|235659 PRK05974, PRK05974, phosphoribosylformylglycinamidine synthase subunit PurS; Reviewed
YKVKVTVTLKEGVLDPQGQAIKGALGSLGYDGVEDVRQGKYFELELEGESEEKAEADLKEMCEKLLANPV
IEDYRIEIEE
>gnl|CDD|168324 PRK05975, PRK05975, 3-carboxy-cis,cis-muconate cycloisomerase; Provisional
MSISVFDHPFLSGLFGDDEIAALFSAEADIAAMLAFEAALAEAEAEHGIIPAEAAERIAAACETFEPDLA
ALRHATARDGVVVPALVRQLRAAVGEEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDA
LEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRDRLEALRADVFPLQFGGAAGTLEKLGGKAAA
VRARLAKRLGLEDAPQWHSQRDFIADFAHLLSLVTGSLGKFGQDIALMAQAGDEISLSGGGGSSAMPHKQ
NPVAAETLVTLARFNATQVSGLHQALVHEQERSGAAWTLEWMILPQMVAATGAALRLALELAGNIRRLGK
A
>gnl|CDD|180334 PRK05978, PRK05978, hypothetical protein; Provisional
ANSMQNTAPFVGRNGGAPLEKRPVGRAMWRGFRGRCPACGEGKLFRAFLKPVDHCAACGEDFTHHRADDL
PAYLVIVIVGHIVVGGFMGTETTFNLPVWLHLAIWLPITLIASLALLQPIKGAVIGLQWALRMHGFGGEN
DSPEDDAA
>gnl|CDD|180335 PRK05980, PRK05980, crotonase/enoyl-CoA hydratase family protein
MTDTVLIEIRDGIALLTLNRPEKLNALNYALIDRLLARLDAIEVDESVRAVILTGAGDRAFSAGADIHEF
SASVAAGADVALRDFVRRGQAMTARLEAFPKPVIAAVNGLAFGGGCEITEAVHLAIASERALFAKPEIRL
GMPPTFGGTQRLPRLAGRKRALELLLTGDAFSAERALEIGLVNAVVPHEELLPAARALARRIIRHSPVAV
AAILTAVTRGLNLSIAEGLLIESEQFARMAGSADLREGLAAWIERRRPAY
>gnl|CDD|235661 PRK05981, PRK05981, enoyl-CoA hydratase/isomerase
MQFKKVTLDFDGGVAILTLDHPEVMNAVSIDMLGGLAEALDAIEDGKAEVRCLVLTGAGRGFCTGANLQG
RGSGGRESDSGGDAGAALETAYHPFLRRLRNLPCPIVTAVNGPAAGVGMSFALMGDLILCARSAYFLQAF
RRIGLVPDGGSTWLLPRLVGKARAMELSLLGEKLPAETALQWGLVNRVVDDAELMAEAMKLAHELANGPT
VALGLIRKLYWDSPENDFEEQLNLEREAQRIAGKTEDFKEGVGAFLQKRPAQFKGR
>gnl|CDD|180337 PRK05985, PRK05985, cytosine deaminase; Provisional
MTDLLFRNVRPAGGAAVDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGDPWY
PNEPGPSLRERIANERRRRAASGHPAAERALALARAAAAAGTTAMRSHVDVDPDAGLRHLEAVLAARETL
RGLIDIQIVAFPQSGVLSRPGTAELLDAALRAGADVVGGLDPAGIDGDPEGQLDIVFGLAERHGVGIDIH
LHEPGELGAFQLERIAARTRALGMQGRVAVSHAFCLGDLPEREVDRLAERLAEAGVAIMTNAPGSVPVPP
VAALRAAGVTVFGGNDGIRDTWWPYGNGDMLERAMLIGYRSGFRTDDELAAALDCVTHGGARALGLEDYG
LAVGARADFVLVDAETVAEAVVAVPVRRLVVRGGRIVARDG
>gnl|CDD|235662 PRK05986, PRK05986, cob(I)yrinic acid a,c-diamide adenosyltransferase
QQRQQRVKAPVDARIAAAQEEKGLLIVHTGNGKGKSTAAFGMALRAVGHGKKVGVVQFIKGAWSTGERNL
LEFGGGVEFHVMGTGFTWETQDRERDIAAAREGWEEAKRMLADESYDLVVLDELTYALKYGYLDVEEVLE
ALNARPGMQHVVITGRGAPRELIEAADLVTEMRPVKHPFDAGVKAQKGIEW
>gnl|CDD|180339 PRK05988, PRK05988, formate dehydrogenase subunit gamma; Validated
MPDEPWDAARIAAIIAEHKHLEGALLPILHAIQDEFGYVPEDAVPVIAEALNLSRAEVHGVITFYHDFRT
HPPGRHVLKLCRAEACQAMGGDALAAHAKARLGIDFHQTTADGAVTLEPVYCLGLCACSPAAMLDGEVHG
RLDPQRLDALLAEARR
>gnl|CDD|235663 PRK05989, cobN, cobaltochelatase subunit CobN; Reviewed
MHLLLTQPGGFVDGDGAVDLGQTPADIVLLSAADTDLALLAAAVRRLPDDFPSLRLANLLRLQQPASVDL
YVEDVLRHADVVVVRLLGGRRYWPYGLEALVALAARRGAPLIVLPGDDAPDPELPALSTVPAELAARLWR
YLAEGGPANLRNLLRYLADTALGTGDEPEPPVPLPAAGIYHPGKAFASLEDYLAWWAPRKAPTVAILFYR
AHLQAGNTAPIDALIAALEARGLNPLPVFVSSLKDAESPEVLEDLFNADALVDAVLNATGFALAAAAWDV
EVLAALDVPVLQVICSGGNREAWEASSQGLSPRDIAMQVALPEFDGRIIPRAISFKELDEDGVVEYVPDP
ERIDFVAGLARRWARLRRKPNADKRVALILANYPTKDGRIGNAVGLDTPASAVRLLRALRAAGYDVGDLP
ADGDALIHALLLAGGTNDFWLTGEQLRGAAQSLPLADYRAWFATLPEEVRDEVTERWGPPPGDPYVREGD
GRFVIPGLRFGNVFVGIQPPRGYGGDPVAIYHDPDLPPPHHYLAFYLWLREGFGADAVVHVGKHGNLEWL
PGKSVGLSADCYPDAALGDLPHLYPFIVNDPGEGTQAKRRAQAVIIDHLTPPMTRAELYGDLADLEQLID
EYYEAAALDPRRLPALREQILELVRAANLDRDLGLSEAPDEDDFDDFLLHLDGYLCELKEAQIRDGLHIF
GEAPEGEQRVDLVLAILRAPQGDGEGARPGLRRALALDLGLDACDLAEPWTGPRPAALLALDDAPWRTAG
DTVERLEVLAAELVEALEPAGWDPTAAVLEFAATELVPRLAATPDEIEQLLRGLDGRFVPPGPSGAPTRG
RPDVLPTGRNFYSVDPRAVPTRAAWELGQKLAEQLLERYLQEHGEYPRSVGLSVWGTSTMRTGGDDIAQA
LALLGVRPVWDEASRRVTGLEIIPLAELGRPRIDVTLRISGFFRDAFPNVIALFDDAVRAVAALDEPDED
NPVRAHVRAELARLGARGLDEAEARRRATLRIFGSKPGAYGAGLQQLIDSRNWRDDADLAEAYLNWGGYA
YGRGVDGEAARDLFEERLRRVQAVVQNQDSREHDLLDSDDYFQYHGGMTAAVRHLSGAAPAAYIGDHSRP
DAPRIRTLKEEIARVVRSRVVNPKWIAGMKRHGYKGAFEMAATVDYLFGWDATTGVVDDWMYEAVADTYV
LDEENREFFEEHNPWALREIAERLLEAARRGLWQAPDPETLELLEELYLEIEGD
>gnl|CDD|180341 PRK05990, PRK05990, precorrin-2 C(20)-methyltransferase; Reviewed
AKGRLIGLGVGPGDPELLTLKALRLLQAAPVVAYFVAKGKKGNAFGIVEAHLSPGQTLLPLVYPVTTEIL
PPPLCYETVIADFYDTSAEAVAAHLDAGRDVAVICEGDPFFYGSYMYLHDRLAPRYETEVIPGVCSMLGC
WSVLGAPLVYRNQSLSVLSGVLPEEELRRRLADADAAVIMKLGRNLDKVRRVLAALGLLDRALYVERATM
ANQRIVPLAEVDPMASPYFSLILVPGEKWQG
>gnl|CDD|180342 PRK05991, PRK05991, precorrin-3B C17-methyltransferase; Provisional
MSGRLFVIGTGPGNPEQMTPEALAAVEAATDFFGYGPYLDRLPLRADQLRHASDNREELDRAGAALAMAA
AGANVCVVSGGDPGVFAMAAAVCEAIENGPAAWRAVDLTIVPGVTAMLAVAARIGAPLGHDFCAISLSDN
LKPWELIEKRLRLAAEAGFVIALYNPISRARPWQLGEAFDLLREHLPATVPVIFGRAAGRPDERIAVAPL
AEADASMADMATCVIIGSAETRIVARPGKPDLVYTPRSAA
>gnl|CDD|180343 PRK05993, PRK05993, SDR family oxidoreductase
MDMKRSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEAEGLEAFQLDYAEPESIAALVAQVL
ELSGGRLDALFNNGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLV
PMKYRGAYNASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRFRANALAAFKRWIDIENSVHRAAYQQ
QMARLEGGGSKSRFKLGPEAVYAVLLHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLRKAA
>gnl|CDD|180344 PRK05994, PRK05994, O-acetylhomoserine aminocarboxypropyltransferase; Validated
MTDRSPGFATLAVHAGAQPDPTTGARATPIYQTTSFVFNDADHAASLFGLQAFGNIYTRITNPTNAVLEE
RVAALEGGTAALAVASGHAAQFLVFHTLLQPGDEFIAARKLYGGSINQFGHAFKSFGWQVRWADADDPAS
FERAITPRTKAIFIESIANPGGTVTDIAAIAEVAHRAGLPLIVDNTLASPYLIRPIEHGADIVVHSLTKF
LGGHGNSMGGIIVDGGTFDWSKSGKYPMLSEPRPEYHGLVLHETFGNFAFAIAARVLGLRDLGPAISPFN
AFLILTGIETLPLRMQRHSDNALAVAEWLKGHPKVSWVNYAGLPDDPYHALAQKYSPKGAGAVFTFGLKG
GYEAGVKLVSSLKLFSHLANIGDTRSLVIHPASTTHRQLTDEQKVAAGAGPDVVRLSIGIEDVDDIIADL
EQALAKA
>gnl|CDD|235664 PRK05995, PRK05995, enoyl-CoA hydratase; Provisional
MMYETLEIEQRGQVATVTLNRPDVRNAFNETVIAELTAAFRALDADDSVRAVVLAGAGKAFCAGADLNWM
KKMAGYSDDENRADARRLADMLRAIYRCPKPVIARVHGDAYAGGMGLVAACDIAVAADHAVFCLSEVRLG
LIPATISPYVIRAMGERAARRYFLTAERFDAAEALRLGLVHEVVPAEALDAKVDELLAALVANSPQAVRA
GKRLVRDVAGRPIDAALIADTASRIALIRATEEAREGVAAFLEKRKPAWRGR
>gnl|CDD|235665 PRK05996, motB, MotB family protein
MEMEIHHEGKNEIIIVRRGGDDDHEGHHGGVWKIAYADFMTAMMAFFLVMWLINAANEETKAAVASYFNP
IKLTDRKPSEKGLKDPVDGAEGEQKPGKSKFEEDQRVEGSSAVTGDDTTRTSGDQTNYSEADLFRNPYAV
LAEIAQEVGQQANVSAKGDGGAAQSGPATGADGGEAYRDPFDPDFWSKQVEVTTAGDLLPPGQAREQAQG
AKSATAAPATVPQAAPLPQAQPKKAATEEELIADAKKAATGEPAANAAKAAKPEPMPDDQQKEAEQLQAA
IAQAIGGVAGKLAEGVTVTPVEGGLLISLTDQVDYGMFAIGSAVPRAELVLAMEKIGQLLAERPGAVIIR
GHTDARPFKSATYDNWRLSTARAQSAYYMLVRGGLDEKRIEQVEGFADRRPKLPNDPNAAANRRIEILIQ
SKQ
>gnl|CDD|235666 PRK06002, fliI, flagellar protein export ATPase FliI
MTPDNALARLAALVERYAAPEPLVRIGGTVSEVTASHYRVRGLSRFVRLGDFVAIRADGGTHLGEVVRVD
PDGVTVKPFEPRIEIGLGDAVFRKGPLRIRPDPSWKGRVINALGEPIDGLGPLAPGTRPMSIDATAPPAM
TRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFL
EDTLADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEP
PVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQG
RYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGGYRAGSDPDLDQAVDLVPRIYEA
LRQSPGDPPSDDAFADLAAALKGAAQAQNA
>gnl|CDD|168340 PRK06003, flgB, flagellar basal body rod protein FlgB; Reviewed
MSPIYLFDLASRQAQWLSVRQATVAGNIANANTPGYRARDVQPFADVLDKTGLTMAATSPGHLGASATGI
DVTEARPDDSWEVTHSGNSVSLEQEMMKAGEIKRQYSLNTAIVKSFHRMMLMTVKG
>gnl|CDD|235667 PRK06004, flgB, flagellar basal body rod protein FlgB; Reviewed
MLRTRMQWHQERQKVLAENVANADTPGFRPRDLVEPKFDASGQAQAAGASTGGLGMMRTSASHMAPAGAS
PSFDARRGAGFETRPAGNAVNLEDEMLKVSDNQMDYAAAASLYQKSLGLLKTAIGKR
>gnl|CDD|180347 PRK06005, flgA, flagellar basal body P-ring formation protein FlgA
MARMRAISALARLALAGAFLLAAMAGAAAADRIAFVVPSTTIYPGETISDSMLLEVQFVTNPPAAAQYVL
SIDQVVGKVAKRTLLPGRPIPVSALREPSLVTRGSPVKLVFSAGGLTITAAGTPLQSGAAGDLIRVRNVD
SGVIVSGTVLADGTIQVGAK
>gnl|CDD|235669 PRK06008, flgL, flagellar hook-associated family protein
MKTSFISTLALQNALRLTIAKLQAELSKAQTEATTGRYADVGLSLGSKTARSVSLRREYDRLASLTDSNS
LVTQRLTATQTALGQIIEAAQSFLNDLLAANSSAQTAATVAQSARSALSSLTSTLNTSVNGEYLFAGINT
DVKPLTDYGAPGSAAKTAVDTAFQTYFGFAPGDPAVSNITAAQMQDFLDGTFAPLFSDANWSANWSSASD
TNMTSRISPTETAETSTSANAEGFRKLAMAYVMVSELGDIGLSSEAQDTVTDKAITYTGQAISGLTTEQS
QLGLAQSRVTKANTRLDAQIKLLNGQILDLEGVDPYEASTRVNALQTQLETSYSLTSQLQQLSLVNYL
>gnl|CDD|235670 PRK06009, flgD, flagellar hook assembly protein FlgD
MAVDATTSATSSSTTSSTSTASNSTSAANKASVNYDSFLQLLIAQMKNQDPTDPMDATQYVSQLATFSQV
EQSIQTNSKLDTLLASSSLTQAEGLIGRTVTSADGSITGVVKSVTVYSDGVIATLEDGKKVLLGPGVTIS
>gnl|CDD|235671 PRK06010, fliQ, flagellar biosynthesis protein FliQ; Reviewed
MNEADALDIVRDAIWTVLVASGPAVLAAMVVGVAIALFQALTQIQEMTLTFVPKIVAIFVTLLLTLPFMG
AQISAFTLLIYSRIAGGF
>gnl|CDD|235672 PRK06012, flhA, flagellar type III secretion system protein FlhA
ANLAAMLRLPGNLKLLKWRDLAVAILVLAILAMMILPLPPFLLDLLLTFNIALSVLILLVALFIQRPLDF
SAFPTLLLITTLLRLALNVASTRLILLEGHEGTDAAGKVIEAFGHFVVGGNFVVGIVVFIILVIINFVVI
TKGAGRIAEVAARFTLDAMPGKQMAIDADLNAGLIDEEEAKKRRKELQQEADFYGAMDGASKFVKGDAIA
GILITVINIIGGLIIGVVQHGMSFGEAAETYTLLTIGDGLVSQIPALLISTAAGIIVTRVSSDGDVGEQI
VGQLFANPKALYIAAGVLFLLGLVPGMPHLPFLLLAGLLGFLAYRLRKREKKAAELAAEEAEEEEAAEPE
EESWDDVLPVDPLELEVGYGLIPLVDENQGGELLDRIRSIRKKIAQELGFLVPPVRIRDNLQLPPNEYRI
KIKGVEVGSGELRPGRLLAMNPGGVDGELPGIPTKEPAFGLPAVWIDEALREQAQLLGYTVVDPSTVVAT
HLTEVIKNHAAELLGRQEVQQLLDRLAKEYPKLVEELVPKVLSLGTLQKVLQNLLKERVSIRDLRTILET
LADYAPITKDPDELTEHVRQRLGRQIVQQYKGEDGELPVITLDPELEQLLLQSLQGTGGGSYLALEPGLA
ERLLQSLQEALERQEMKGEPPVLLVSPALRPYLRRLLERFLPQLPVLSYNEIPDNIEIRIVGTVGIN
>gnl|CDD|168348 PRK06015, PRK06015, 2-dehydro-3-deoxy-phosphogluconate aldolase
LKLQPVIPVLLIDDVEHAVPLARALAAGGLPAIEITLRTPAALDAIRAVAAEVEEAIVGAGTILNAKQFE
DAAKAGSRFIVSPGTTQELLAAANDSDVPLLPGAATPSEVMALREEGYTVLKFFPAEQAGGAAFLKALSS
PLAGTFFCPTGGISLKNARDYLSLPNVVCVGGSWVAPKELVAAGDWAGITKLAAEAAALKA
>gnl|CDD|235673 PRK06018, PRK06018, putative acyl-CoA synthetase; Provisional
MLGLMQDWPLLCHRIIDHAARIHGNREVVTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATI
AWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLPSVERYVV
LTDAAHMPQTTLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMAN
NGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPGAKLDGASVYELLDTEKVTFTAGVPTVWL
MLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSPLGTLAALKPPFSKLPGDA
RLDVLQKQGYPPFGVEMKITDDAGKELPWDGKTFGRLKVRGPAVAAAYYRVDGEILDDDGFFDTGDVATI
DAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATRE
EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFKDYKLPTAAA
>gnl|CDD|235674 PRK06019, PRK06019, phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
GMKTIGIIGGGQLGRMLALAAAPLGYKVIVLDPDPDSPAAQVADEVIVADYDDVAALRELAEQCDVITYE
FENVPAEALDALAARVPVPPGPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVL
KTRRGGYDGKGQWVIRSAEDLEAAWALLGSVPCILEEFVPFEREVSVIVARGRDGEVVFYPLVENVHRNG
ILRTSIAPARISAELQAQAEEIASRIAEELDYVGVLAVEFFVTGDGELLVNEIAPRPHNSGHWTIEACST
SQFEQHLRAILGLPLGTTRLLSPAVMVNLLGDDWLEPRWDALLALPGAHLHLYGKAEARPGRKMGHVTVL
GDDVEALLAKLEALAPDWAEIW
>gnl|CDD|168351 PRK06023, PRK06023, crotonase/enoyl-CoA hydratase family protein
MTDHILVERPGAHPGVQVIRFNRPEKKNAITRAMYATMAKALKAADADDAIRAHVFLGTEGCFSAGNDMQ
DFLAAAMGGTSFGSEILDFLIALAEAEKPIVSGVDGLAIGIGTTIHLHCDLTFASPRSLFRTPFVDLALV
PEAGSSLLAPRLMGHQRAFALLALGEGFSAEAAQEAGLIWKIVDEEAVEAETLKAAEELAAKPPQALQIA
RDLMRGPREDILARIDEEAKHFAARLKSAEARAAFEAFMRR
>gnl|CDD|235675 PRK06025, PRK06025, acetyl-CoA C-acetyltransferase
MAEAYIIDAVRTPRGIGKVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLG
RMAALDAGYDIKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAGKPPL
GMGSGNLRLRALHPQSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDGSV
ALDHEEFPRPQTTAEGLAALKPAFTAIADYPLDDKGTTYRGLINQKYPDLEIKHVHHAGNSSGVVDGAAA
LLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEK
FIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKRGLVTMCAAGGMAPAIIIERV
>gnl|CDD|180353 PRK06026, PRK06026, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated
MTFELKTVAGKRVLFVMAADAEYGPHLRARFTPLMTGVGPVEAAVNLTAALARLKAAGDLPDLVVSLGSA
GSAKLEQTEVYQVSSVSYRDMDASPLGFEKGVTPFLDLPATVELPLRIPGIPEASLSTGGNIVSGAAYDA
IDADMVDMETYAVLRACQAFGVPLIGLRGISDGAAELKHVGDWTEYLHVIDEKLAGAVDRLERALEDGLL
WL
>gnl|CDD|235676 PRK06027, purU, formyltetrahydrofolate deformylase; Reviewed
MMMMQRYVLTLSCPDRPGIVAAVSNFLYEHGGNIVDADQFVDPETGRFFMRVEFEGDGLIFNLETLRADF
AALAEEFEMDWRLLDSAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSLVERFGIPF
HHVPVTKETKAEAEARLLELIDEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQA
YERGVKLIGATAHYVTADLDEGPIIEQDVIRVDHRDTAEDLVRAGRDVEKQVLARAVRWHLEDRVLVYGN
KTVVFR
>gnl|CDD|235677 PRK06029, PRK06029, UbiX family flavin prenyltransferase
MKRLIVGISGASGAIYGVRLLQVLRDVGEIETHLVISQAARQTLAHETDFSLRDVQALADVVHDVRDIGA
SIASGSFGTDGMVIAPCSMKTLAKIAHGYSDNLITRAADVMLKERRRLVLCVRETPLHLGHLRNMTKLAE
MGAIIMPPVPAFYHRPQTLEDMVDQTVGRVLDLFGIEHDLYPRWQ
>gnl|CDD|180356 PRK06030, PRK06030, hypothetical protein; Provisional
LNPQALERLWHIAPDKRRERLIELCEAVIDLLALAFGVSGAEIASPLRGRREVSRIRQIAMYVAHVSLGW
PMNEVALAFGRDRTTVGHACHTVEDLRDDAAFDARVSVLERIVNSAFTAWRMAA
>gnl|CDD|235678 PRK06031, PRK06031, phosphoribosyltransferase; Provisional
MTEADFMAPHDFWQEIHPPGTFAGDGPFRSSYPATLPDGRQLLLPIRGLPDGDRALASLIVNQASFEVLD
ALAEHLAEKARAFDPDVVAGLPTLGLTLAAAVARKLGHTRYVPLGTSRKFWYRDELSVPLSSITTPDQGK
RLYIDPRMLPLLEGRRVALIDDVISSGASIVAGLRLLAACGIEPAGIGAAMLQSERWRESLAAAGPQWPA
RVVGVFATPILERTAAGWWQAPA
>gnl|CDD|235679 PRK06032, fliH, flagellar assembly protein H; Validated
MAAPRKFLFDTDFDAPGKARERARAAAEFAQAVAEAEAAAYAQGFAAGQREAAAQSERRLADALERIAQA
AAGLLAALAAVEHEMETEAADLALAVARKIAGAALAAEPLAEITAAVRDCLRHLVATPHLVVRVNDALVE
AARERLERLARESGFEGRLVVLADPDMAPGDCRLEWADGGVVRDRAAIEARIEEAVGRY
>gnl|CDD|180359 PRK06033, PRK06033, flagellar motor switch protein FliN
VSTLDAVSVELMVVLGRSSMPIHQVLRMGRGAVIPLDATEADEVWILANNHPIARGEVLIDRNRIAVEVT
RAADMLDRMAGRR
>gnl|CDD|235680 PRK06034, PRK06034, hypothetical protein; Provisional
GSTAPPAPPSLAELRWEIDAIDEELHQLLMERGDIIDRLIAVKRTQEVGSAFRPGREADMMRRLVSRHRG
ILPLDTVESIWRVIIATFTYVQAPFSVHADGSGGEAAMRDSARFHFGFTVPYVPHFSAQAVVEAVARSKG
DLGLVSLTSSDTPWWGRLEAEGAPKIIARLPFVERADHPAALPVFVVSRPADDAAVTEVETWSVRVSGWV
ADAARALAALAEVVAVPDVAADGAALLVSLPGFVQLDTIADALRLAGASVRSTALVGSHAARYDVPPSG
>gnl|CDD|180361 PRK06035, PRK06035, 3-hydroxyacyl-CoA dehydrogenase; Validated
MDIKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGPYGLRNLVEKGKMSEDEAKAI
MARIRTSTSYESLSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFI
GMHWFNPAPVMKLIEVVRAALTSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIG
IATIKDIDEMCKLAFGFPMGPFELMDIIGIDTVYHIAEYLYEETGDPQFIPPNSLKQMVLNGYVGDKKVK
YGSKGGWFDYY
>gnl|CDD|180362 PRK06036, PRK06036, S-methyl-5-thioribose-1-phosphate isomerase
MRTIDWNDESNSVKLIDQTLLPEEYKVIECKTLESLCEAIKSLRVRGAPALGAAGGYGIALAARLSKAKD
VDELLKDLKVAAETLKSTRPTAVNLSWGVDRVLKAALDAEDVEEIRDIALREAERIAEEDVARNKLIGKH
GAKLLEDGDTVLTHCNAGRLACVDWGTALGVIRSAVEQGKEIKVIACETRPLNQGSRLTTWELMQDNIPV
TLITDSMAGIVMRQGMVDKVIVGADRITRDAVFNKIGTYTHSVLAKEHEIPFYVAAPLSTFDFEGWEGSV
KIEERDPDELRYCGKTQIAPKDVPVYNPAFDATPMENVTAIITEKGVFYPPFLLDEVLV
>gnl|CDD|180363 PRK06038, PRK06038, N-ethylammeline chlorohydrolase; Provisional
MADIIIKNAYVLTMDAGDLKKGSVVIEDGTITEVSESTPGDADTVIDAKGSVVMPGLVNTHTHAAMTLFR
GYADDLPLAEWLNDHIWPAEAKLTAEDVYAGSLLACLEMIKSGTTSFADMYFYMDEVAKAVEESGLRAAL
SYGMIDLGDDEKGEAELKEGKRFVKEWHGAADGRIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHV
LETEAELNQMKEQYGMCSVNYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIA
PVPKLLERGVNVSLGTDGCASNNNLDMFEEMKTAALLHKVNTMDPTALPARQVLEMATVNGAKALGINTG
MLKEGYLADIIIVDMNKPHLTPVRDVPSHLVYSASGSDVDTTIVDGRILMEDYKVLCMDEQDVMEDAKKA
AEELVSRVNA
>gnl|CDD|235682 PRK06041, PRK06041, archaellar assembly protein FlaJ
MMEMKVSILPRLGLPPKDYLLKILLPAVVFSILLIILAILYFSLLLLLLPILLLGSAVGYPYIKLDSKKK
KINNDLHFFITYMAVLSTTDIDRDEIFRILSEKEEYGALAKEFRKIYVLVDKWNYSLAEACRFVAKRTPS
ELFADFLDRLAYSIDSGEPLKEFLKQEQDTVMEDYKTFYERALYSLDVWKDLYVSLLLSVTFVAVFAIIS
PILTGTDPTTTLSLSLFLFLFIEVGGVYVIKKRVPKDPLWHTLEIKTKEQKKIRKLLIISVPLSAILVLL
LLLLGFIIGPILIDKIPLPILIALPLTPLAIPGYVARKEEKKIKRRDENFPSFIRSLGSSVSAKGGTTTE
ALKYLDKKDFGPLTPDINALYKRLNLRIDSKKAWRYFIGETGSYLIQKFSEMFVDAVELGGDPKVIGEII
SSNFLEIVLLRKKRYQSASSFVGLLYGLHAAMAFALFISLGIAKIMSDLISSLNIPAETVIGIIHVTPPS
GIPLLEYLLVIILIILSLLSALAIKIVDGGHKYNSLFHFVIMLWISGLVMYVTPPLVGSLLSF
>gnl|CDD|180366 PRK06043, PRK06043, fumarate hydratase; Provisional
MEYHLKTPLKKEDIEKLNVGDIVYISGEILTARDEAHARILEMKEKGKELPFSLEGAVIYHCGPLMKKTD
EGWKVVSAGPTTSARMSKMTPKLLEKVEVRAIIGKGGMKNVADALKGKCVYLAYTGGCAALAAESIKRVK
AVHWLDLGMPEAVWVLEVEEFGPLIVGIDAKGNDLYSEVREKAEKNFEKIIK
>gnl|CDD|180368 PRK06048, PRK06048, acetolactate synthase large subunit
MTGSTEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGK
VGVCVATSGPGATNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKD
LPRIIKEAFHIASTGRPGPVLIDLPKDVTTAEIDFDYPDKVELRGYKPTYKGNPQQIKRAAELIMKAERP
IIYAGGGVISSNASEELVELAETIPAPVTTTLMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAV
GARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPIVGDAKQVLKSLIKYVQYCDRKEWLDKINQ
WKKEYPLKYKEREDVIKPQYVIEQIYELCPDAIIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGF
PAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRQWQELFYDKRYSHTC
IKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSPMVPAGAAINEILDLE
E
>gnl|CDD|235683 PRK06049, rpl30p, 50S ribosomal protein L30P; Reviewed
EMYAVIRIRGRVNVPRDIADTLKMLRLHRVNHCVLVPETPSYKGMLQKVKDYVTWGEIDADTLAELLRKR
GRLEGNKKLTDEYVKENTGYDSIEELAEALVEGEIKLKDLPGLKPVFRLHPPRGGFGGIKRPFKEGGELG
YRGEKINELLRRMR
>gnl|CDD|235684 PRK06052, PRK06052, methionine synthase
MQEIIFDDIGSFPLPEGVTREWVENAFETREEDEKLFSVVRSAFQMKIDAGVQVPTYPQFRDMIEQFLDI
IRDEKCCEEPYVVKEECAKILELEAIEEVAKEYKEETGETLEVRVCVTGPTELYLQEFGGTIYTDILLIL
AKSVERFVENAIKSAKNFKIKTISIDEPSLGINPEIQFSDDEIISALTVASTYARKQGADVEIHLHSPLY
YELICETPGINVIGVESAATPSYLDLIDKKVLEDTDTFLRVGVARTDIFSLIAILNEKYGTNAWKDKEYL
QEIVTELETPEVIKKRLEKAYSIFGDRIKYVGPDCGLGSWPSQELAFRLLENVAKAINEFRAEK
>gnl|CDD|180371 PRK06057, PRK06057, short chain dehydrogenase; Provisional
LSQRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLFVPTDVTDEDAVNALF
DTAAETYGSVDIAFNNAGISPPEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTAS
FVAVMGSATSQISYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELFAKDPERAARRLVHV
PMGRFAEPEEIAAAVAFLASDDASFITASTFLVDGGISGAYVTPL
>gnl|CDD|235685 PRK06058, PRK06058, 4-aminobutyrate--2-oxoglutarate transaminase
MYRLPQSRRLVTEIPGPKSQALAERRAAAVAAGVGSTLPVYVARAGGGIVEDVDGNRLIDLGSGIAVTSV
GNSAPRVVEAVREQVARFTHTCFMVTPYEGYVAVAEQLNRLTPGDHEKRSALFNSGAEAVENAVKIARSY
TGRQAVVVFDHAYHGRTNLTMALTAKSMPYKSGFGPFAPEVYRAPMSYPYRDPKGLATDGEEAAARAITV
IEKQVGADNLAAVIIEPIQGEGGFIVPAEGFLPALLEWCRENGVVFIADEVQTGFARTGAWFACEHEGIV
PDLITTAKGIAGGLPLSAVTGRAEIMDAPHPGGLGGTYGGNPVACAAALAAIETIEEDDLVARARQIEAL
MTDRLRALAAEDDRIGDVRGRGAMIAIELVKPGTTEPDAELTKALAAAAHAAGVIVLTCGTYGNVIRLLP
PLVIGDELLREGLDVLEAALADL
>gnl|CDD|180373 PRK06059, PRK06059, lipid-transfer protein; Provisional
SMPEPVYILGAGMHPWGKWGRDFVEYGVVAARAALADAGLDWRDVQLVVGADTIRNGYPGFVAGATFAQA
LGWNGAPVSSSYAACASGSQALQSARAQILAGLCDVALVVGADTTPKGFFAPVGGERPDDPDWLRFHLIG
ATNPVYFALLARRRMDLYGATVEDFAQVKVKNARHGLLNPNARYRKEVTVEDVLASPVVSDPLRLLDICA
TSDGAAALIVASKSFARRHLGSVAGVPSVRAISTVTPRYPQHLPELPDIATDSTAAVPAPERVFKDQILD
AAYAEAGIGPEDLSLAEVYDLSTALELDWYEHLGLCPKGEAEALLRSGATTLGGRIPVNPSGGLACFGEA
IPAQAIAQVCELTWQLRGQAGGRQVEGARVGITANQGLFGHGSSVIVAR
>gnl|CDD|180374 PRK06060, PRK06060, p-hydroxybenzoic acid--AMP ligase FadD22
MRNGNLAGLLAEQASEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQ
LLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAARVAPGGYE
PMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPL
ATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERL
MEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIA
KGYWNRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVA
VRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQS
PTKPIWELSLTEPGSGVRAQRDDLSASNMTIAGGNDGGATLRERLVALRQERQRLVVDAVCAEAAKMLGE
PDPWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEAELAGGHGRLKSAG
PVNSGATGLWAIEEQLNKVEELVAVIADGEKQRVADRLRALLGTIAGSEAGLGKLIQAASTPDEIFQLID
SELGK
>gnl|CDD|235686 PRK06061, PRK06061, amidase; Provisional
ASGSDAGAISGSGNDRLPGLTDQAYQLASGAVTSVELVRRSLRRIEASQPTLNAFRVVRAEAALAEAAEA
DRRRAAGDRLPLLGVPIAVKDDVDVAGVPTAFGTAGEVPPATADSEVVRRLRAAGAVIVGKTNTCELGQW
PFTSGPAFGHTRNPWSRDHTPGGSSGGSAAAVAAGLVTAAIGSDGAGSVRIPAAWTHLVGIKPQRGRIST
WPLPEAFNGLTVNGPLARTVADAALLLDAASGNHPGDRHRPPPVTVSDAVGRAPGPLRIALSTRFPFTGF
PAKLHPEIRAAVRRVAEQLALLGHTVVPADPDYGLRLGLNFLPRSTAGLRDWAERLGDPVLLDPRTVSNA
RMGRLLSQAILRLARAAEAAAQRRVGSIFDIVDVVLAPTTAQPPPRVGAFDRLGGWATDRAMIAACPYTW
PWNVLGWPSINVPAGFTSDGLPIGAQLMGPANSEPLLISLAAQLEAVSGWAERQPPVWWTSSP
>gnl|CDD|235687 PRK06062, PRK06062, hypothetical protein; Provisional
PNGLGSDEATAEGARAYALDRAHVFHSWSAQGKINPMVIAGAEGSYVWDYEGRRYLDFSSQLVNTNIGHQ
HPKVVAAIQEQAARLCTVAPAHANDARSEAARLIAERAPGDLSKVFFTNGGADANEHAVRMARLHTGRPK
VLSAYRSYHGGTGSAINLTGDPRRWPNDTGRAGVVHFFGPFLYRSEFHATTEEEECERALAHLERVIELE
GPSTIAAILLESVPGTAGILVPPPGYLAGVRELCDRHGIVLIADEVMAGFGRTGKWFAIEHFGVVPDLIT
FAKGVNSGYVPLGGVAISEAIAATFADRPYPGGLTYSGHPLACAAAVATINAMEEEGIVENAARIGAEVL
GPGLRELAERHPSVGEVRGLGVFWALELVADRETREPLAPYGASSAAMAAVKAACKERGLLPFVNGNRIH
VVPPCTVTEDEVREGLAILDAALAVADAATA
>gnl|CDD|180377 PRK06063, PRK06063, DEDDh family exonuclease
MMSHTWGRPASHYPRGWAVVDVETSGFRPGQARIISLAVLGLDADGNVEQSVVTLLNPGVDPGPTHVHGL
TAEMLEGQPQFADIAGEVAELLRGRTLVAHNVAFDYSFLAAEAERAGAELPVDQVMCTVELARRLGLGLP
NLRLETLAAHWGVPQQRPHDALDDARVLAGILRPSLERARERDVWLPLHPVTRRRWPNGRVTHDELRPLK
ALAARMPCPYLNPGRYVAGRPLVQGMRVALSAEVSRTHEELVERILHAGLAYSDSVDRDTSLVVCNDPAP
EQGKGYHARQLGVPVLDEAAFLELLRAVVGGAS
>gnl|CDD|235688 PRK06064, PRK06064, thiolase domain-containing protein
MRDVAIIGVGQTKFGELWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLFVSQEHIAALIADY
AGLAPIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAGDYEWEEFFG
ATFPGLYALIARRYMHKYGTTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSP
ITDGAAAVILASEEKAKEYTDTPVWIKASGQASDTIALHDRKDFTTLDAAVVAAEKAYKMAGIEPKDIDV
AEVHDCFTIAEILAYEDLGFAKKGEGGKLAREGQTYIGGDIPVNPSGGLKAKGHPVGATGVSQAVEIVWQ
LRGEAEKGRQQVIGAGYGLTHNVGGTGHTAVVHILSRKR
>gnl|CDD|180379 PRK06065, PRK06065, thiolase domain-containing protein
MKVNIHLNKRVAVIGAGLTLFRRRLLETPQELAWEAASKALDEAGLELKDIDCVVIGSAPDAFDGVHMKG
EYLSHGSGGIRKPVSRVYVGGATGVMTAIAGWYHVASGLCQKVLAVAEEKMSPARPHPQAVFRYIWDPIL
EKPLNPNLIWIFAMEMHRYMATYGIKKEEIALVSVKNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQL
LDVSPVSDGAAAIVLASEDLARRYTDTPVWVEGVGWTLDNTEWPNRDLAYPRYVEFAARMAYKMAGIERP
RKEIDVAEPYDPFDYKELHHLEGLQLAKRGEAPKLLKEGVFDIDGDIPSSPSGGLLGVGNPIAAAGLMKV
ISIYWQLKGTAGKMQVKKPVHTGVAQAWGDLMQAGTVIVLRN
>gnl|CDD|180380 PRK06066, PRK06066, thiolase domain-containing protein
TFLNRVAIVGIGWYGFRPTTPEVSFREMMFEAASRAYKDAGNINPRRDVDSFISCQEDFWEGIAIADEFA
PDQIGGAMRPTMTVAGDGLQGLAHAVMHINSGLANVVVVEAHSKPSDILTFSDVVKFAMDPIYVRPIGPP
NPHFIAGLDAVKFMSRKGITREDLALVVEKNKKAGLSNPRASYASNISLEDVLSSEYVVYPLTELDIAPF
VDGAIVVVLASEEVAKKLTDDPVWIKGIGWSTESSNLETAELGKANYMRIAADMAYKMAGIESPRKEVDA
AEVDDRYSYKELQHIEALRLSEEPEKDSLLREGNFDPQGELPVNPSGGHLAKGVPLEASGLSLLLDAVEY
LRGEAGARQGKAERAVVASWRGIPTLTGSVVVVER
>gnl|CDD|180381 PRK06067, PRK06067, flagellar accessory protein FlaH; Validated
EGKKEIISTGNEELDRKLGGGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTENTSKSYLK
QMESVKIDISDFFLWGYLRIFPLNTEGFEWNSTLANKLLELIIEFIKSKREDVIIIDSLTIFATYAEEDD
ILNFLTEAKNLVDLGKTILITLHPYAFSEELLSRIRSICDVYLKLRAEQIGGRYVKVLEVVKLRGARKTT
GNIISFDVDPAFGIKIIPLSLAKA
>gnl|CDD|235689 PRK06069, sdhA, succinate dehydrogenase/fumarate reductase flavoprotein subunit
MEVLKYDVVIVGSGLAGLRAAVAAAERSGGKLSVAVVSKTQPMRSHSVSAEGGTAAVLYPEKGDSFDLHA
YDTVKGSDFLADQDAVEVFVREAPEEIRFLDHWGVPWSRRPDGRISQRPFGGMSFPRTTFAADKTGFYIM
HTLYSRALRFDNIHFYDEHFVTSLIVENGVFKGVTAIDLKRGEFKVFQAKAGIIATGGAGRLYGFTTYAH
SVTGDGLAIAYRAGIPLKDMEFVQFHPTGLVPSGILITEAARGEGGYLINKEGERFMKRYAPQKMELAPR
DVVSRAIMTEIMEGRGFKHESGLCYVGLDLRHLGEEKINERLPLIREIAKKYAGIDPVTEPIPVRPAAHY
TMGGIHTDVYGRVLTADGEWVRGLWAAGEAAAVSVHGANRLGSNSTAECLVWGRIAGEQAAEYALKRPAP
SSPVEKLAEKEEKRIFDKLLKKEGGEPSYEIRRELNDIMDKNFGIFRDESGLAEALKKIKKLRERYKNVR
IEDKSRIYNTDLKDALELDGMLDLAEVVAIGALLRTESRGAHYRLDYPKRDDENWLKHTLAYYTGGGPKV
TYTPVTITKWKPEERKY
>gnl|CDD|168377 PRK06072, PRK06072, enoyl-CoA hydratase; Provisional
MIKVESREGYAIVTMSRPDKLNALNLEMRNEFISKLKQINADPKIRVVIVTGEGRAFCVGADLSEFAPDF
AIDLRETFYPIIREIRFSDKIYISAINGVTAGACIGIALSTDFKFASRDVKFVTAFQRLGLASDTGVAYF
LLKLTGQRFYEILVLGGEFTAEEAERWGLLKISEDPLSDAEEMANRISNGPFQSYIAAKRMINLVLYNDL
EEFLEYESAIQGYLGKTEDFKEGISSFKEKREPKFKGI
>gnl|CDD|235690 PRK06073, PRK06073, NADH dehydrogenase subunit A; Validated
MSFMQAALAFGLVIVLGLAAGVGTYKLLKLILPSKPTPLKVSRYEAGNPPTGPAKLWLPMQYYGYLLLFL
TLEPIVVLLLLIAFAPYYTFRDLLLLIVVALVLMYPVLYYAYKQANRIELWRVR
>gnl|CDD|235691 PRK06074, PRK06074, NADH dehydrogenase subunit C; Provisional
SEKLEELVAKLLEKLPDAIGKVTVAFGELTLKVPAEKILEVLTFLRDDPELRFEQLIDLTGVDYPERGKR
FEVVYHLLSYKHNVRLRVKVRAPEDPVVPSVVDIWPSANWYEREAYDLYGIVFEGHPDLRRILTDYGFEG
HPLRKDFPLTGYVEVRYDDEQKRVVYEPVTLSPWEGTPYVLPGDEKAGT
>gnl|CDD|180385 PRK06075, PRK06075, NADH-quinone oxidoreductase subunit D
EAEIRNYTLNFGPQHPAAHGVLRLILELDGEVVVRADPHIGYLHRGTEKLAEYRTYLQAIPYFDRLDYVS
PMNNEHAYCLAVEKLLGIEVPERAQYIRVLFLELNRILSHLLWLGTHALDLGAMTVFLWGFREREKLLDL
YEAVTGARMHHAYIRPGGVRRDLPDGLLEDIRDFLDYFPKRLDDYETLLTDNRIWKQRLVGVGVVSKERA
LALGFTGPMLRASGVAWDLRKSQPYEVYDELDFDVPVGKNGDCYDRYLVRVEEMRQSLRIIEQCLDRLRP
PPGPVMVDDPKIAPPARLEMKTSMEALIHHFKLVTEGFRVPAGEVYAAVESPKGEFGVYLVSDGGNKPYR
VKIRAPSFAHLQALDEMCRGHMLADVVAIIGSLDIVFGEVDR
>gnl|CDD|235692 PRK06076, PRK06076, NADH-quinone oxidoreductase subunit NuoH
MSLFGPDLLLLILLKAVVILVVVLLCVAFLIWFERKVLARMQLRYGPNRVGPFGLLQLVADGIKLLFKED
IIPAGADKVLFLLAPVIAFIPAFLAWAVIPFGPELVIADLNVGILYILAISSLGVYGVILAGWASNNKYA
LLGALRAAAQMISYEVPLGLSLLAVVLLAGSLNLSDIVEAQFLSWNIIPQPPAFVVFFIAAVAETNRHPF
DLPEAESELVAGYHTEYSGMKFGLFFLGEYINMILVSALITTLFLGGWLPPFPLGGGIPGAIWFVLKVAF
FVFLFIWLRATLPRYRYDQLMRLGWKVLLPLSLVNLLLTAAV
>gnl|CDD|235693 PRK06077, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
MYSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENGGEGIGVLADVSTREG
CETLAKATIDRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMREGGAIVNIA
SVAGIRPAYGLSIYGAMKAAVINLTKYLALELAPKIRVNAIAPGFVKTKLGESLFKVLGMSEKEFAEKFT
LMGKILDPEEVAEFVAAILKIESITGQVFVLDSGESLKGGIK
>gnl|CDD|180387 PRK06078, PRK06078, pyrimidine-nucleoside phosphorylase; Reviewed
MRMVDLIQKKRDGKELTTEEINFFIEGYTNGTIPDYQMSALAMAIYFKDMTDRERADLTMAMVNSGDTID
LSAIEGIKVDKHSTGGVGDTTTLVLAPLVAAFGVPVAKMSGRGLGHTGGTIDKLESIKGFHVEISQEDFI
KLVNENKVAVIGQSGNLTPADKKLYALRDVTATVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKT
VEDAEELAHAMVRIGNNVGRNTMAVISDMSQPLGRAIGNALEVLEAIDTLQGKGPKDLTELVLTLGSQMV
VLAGKAKTLEEAREHLIEVMNNGKALEKFKEFLSAQGGDASVVDDPEKLPQAKYQIEVPAKESGYISELV
ADEIGLAAMLLGAGRATKEDEIDLAVGIVLRKKVGDSVKKGESLATIYANRENVEDVKAKFYKNIKISKE
HVVAPELIHIIITE
>gnl|CDD|235694 PRK06079, PRK06079, enoyl-[acyl-carrier-protein] reductase FabI
MSGILSGKKIVVMGVANKRSIAWGCAQAIKDQGATVIYTYQNDRMKKSLQKLVDEEDLLVECDVASDESI
ERAFATIKERVGKIDGIVHAIAYAKKEELGGNVTDTSRDGYALAQDISAYSLIAVAKYARPLLNPGASIV
TLTYFGSERAIPNYNVMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKTLAVTGIKGHKDLLKESDS
RTVDGVGVTIEEVGNTAAFLLSDLSTGVTGDIIYVDKGVHLI
>gnl|CDD|235695 PRK06080, PRK06080, 1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated
STFKAWLELARPKTLPAAFAPVLVGTALAYWLGSFHPLLALLALLAALLLQIATNLANDYGDYVKGTDTE
DRVGPLRAIGRGGISPKQVKRAAIAFFGLAALLGLYLVAVSGWWLLLLGLLCIAAAILYTGGPKPYGYTG
LGELFVGVFFGLVIVLGTYYLQAGTVDSAVFLPALPCGLLIGAVLLANNIRDIETDRENGKNTLAVRLGD
KNARRLHAALLALAYLCIVLLALLGLASPWGLLFLLSLPLAVKAARPVLRKQKPETLIPALKATGKTNLL
FGLLFAIGLLLSQ
>gnl|CDD|180390 PRK06082, PRK06082, aspartate aminotransferase family protein
MTQNIKPTHFRSEGDINTTPARQDWNASMNDERTQALLKRDSEVFLHQAMSTPCLDVLASAEGIYIEDVD
GKKYMDFHGNNVHQLGYGHPHVIEKVKEQMAKLPFSPRRFTNETAIECAEKLTEIAGGELNRVLFAPGGT
SAIGMALKLARHITGNFKVVSLWDSFHGASLDAISVGGEACFRQGMGPLMAGVERIPPAVSYRGAFPDAD
GSDVHYADYLEYVIEKEGGIGAFIAEAVRNTDVQVPSKAYWKRVREICDKHNVLLIIDEIPNGMGRTGEW
FTHQAYGIEPDILCIGKGLGGGLVPIAAMITKDKYNTAAQISLGHYTHEKSPLGCAAALATIEVIEQEGL
LEKVKADSQFMRERLLEMKAKYPLIGDVRGIGLLWGVELVTDRHTKERAYDEAEAVLYRCLNNGLSFKVS
QGNVIQLSPPLIITREELTQALAILEEAIAKICQDFNYS
>gnl|CDD|180392 PRK06084, PRK06084, bifunctional O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
MKLETLAIHAGYSPDPTTKAVAVPIYQTTSYAFDDTQHGADLFDLKVPGNIYTRIMNPTNDVLEQRVAAL
EGGVGALAVASGMAAITYAIQTIAEAGDNIVSVAKLYGGTYNLLAHTLPRIGIETRFAAHDDIAALEALI
DERTKAVFCESIGNPAGNIIDIQALADAAHRHGVPLIVDNTVATPVLCRPFEHGADIVVHSLTKYIGGHG
TSIGGIVVDSGKFPWAEHKERFALLNTPDPSYHGVTYTEAFGPAAFIGRCRVVPLRNMGAALSPFNAFLI
LQGLETLALRMERHTENALKVARYLQQHPQVAWVKYAGLPDHPEHELARRYMGGKPASILSFGIKGGQAA
GARFIDALKLVVRLVNIGDAKSLACHPASTTHRQLNDEELEKAGVSRDMVRLSIGIEHIDDIIADLAQAL
DASKG
>gnl|CDD|180393 PRK06087, PRK06087, medium-chain fatty-acid--CoA ligase
KVTLTFNEQRRAAYRQQGYWGDASLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASRLANWLLAKG
IEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLI
LPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHN
NILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCM
LGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPL
SRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRM
DEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTL
EEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRLTQDVCEEIE
>gnl|CDD|180394 PRK06090, PRK06090, DNA polymerase III subunit delta'; Validated
MNNDYPWLVPVWQNWKAGLDAGRIPGALLLQSDEGLGVESLVELFSRALLCQNYQSEACGFCHSCELMQS
GNHPDLHVIKPEKEGKSITVEQIRQCNRLAQESSQLNGYRLFVIEPADAMNESASNALLKTLEEPAPNCL
FLLVTHNQKRLLPTIVSRCQQWVVTPPSTAQAMQWLKGQGITVPAYALKLNMGSPLKTLAMMKEGGLEKY
HKLERQLVDALSGPVSDQLKCASLIAADPLTHLSWLWLLLTDAQKVHFGVQNEYYLPGSAALGPFTYSGL
YVSTAKLERLKEQLQQFSGLNTELLIMNWLIESREELCL
>gnl|CDD|180395 PRK06091, PRK06091, membrane protein FdrA; Validated
MIHAFIKKGCFQDSVSLMIISRKLSESENVDDVSVMMGTPANKALLDTTGFWHDDFNNATPNDICVAIRT
EAADAGIAQAIMQQLEEALKQLAQGSGSSQSLTQVRRWDSACQKLPDANLALISVAGEYAAELAEQALDR
NLNVMMFSDNVTLEDEIRLKTRAREKGLLVMGPDCGTAMIAGTPLAFANVMPEGNIGVIGASGTGIQELC
SQIALAGEGITHAIGLGGRDLSAEVGGISALTALEMLSADEKSEVIAFVSKPPAEAVRLKIINAMKATGK
PVVALFLGYTPAVARDENVWFASTLDEAARLACLLSRVTAQRNAILPVSQGFICGLYTGGTLAAEAAGLL
AGHLGVEADDEHHHGMMLDADGHQIIDLGDDFYTVGRPHPMIDPTLRNQLIADLGAKPQVRVLLLDVVIG
FGATADPAGSLVSAIQKACAARADGQPLYAIATVTGTERDPQCRSQQIATLEDAGIAVVDSLPEATLLAA
ALIRPLLSATQQHTPSLLENVAVINIGLRSFALDLQSAGKPVVHYQWAPVAGGNKKLARLLERLQ
>gnl|CDD|235696 PRK06092, PRK06092, 4-amino-4-deoxychorismate lyase; Reviewed
MFWINGQPQESLSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIPLDDWAQLEQEMKQL
AAELENGVLKVIISRGSGGRGYSPAGCAAPTRILSVSPYPAHYSRWREQGITLALCPTRLGRNPLLAGIK
HLNRLEQVLIRAELEQTEADEALVLDSEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLA
QSGYPVVEVDASLEELLQADEVFICNSLMPVWPVRAIGETSYSSGTLTRYLQPLCERL
>gnl|CDD|180397 PRK06096, PRK06096, molybdenum transport protein ModD; Provisional
MIFLSDAQLDALLLEDIQGGDLTTRALGIGHQPGYIEFFHRQGGCVSGISVACKMLTTLGLTIDDAVSDG
SQANAGQRLISAQGNAAALHQGWKAVQNVLEWSCGVSDYLAQMLALLRERYPDGNIACTRKAIPGTRLLA
TQAVLAAGGLIHRAGCAETILLFANHRHFLHDPQDWSGAINQLRRHAPEKKIVVEADTPKEAIAALRAQP
DVLQLDKFSPQQATEIAQIAPSLAPHCTLSLAGGINLNTLKNYADCGIRLFITSAPYYAAPADIKVSLQP
AASI
>gnl|CDD|235697 PRK06099, PRK06099, F0F1 ATP synthase subunit I; Validated
MSAVLNQAKKHYKKALKIEFFLLLVLFLLLLIWQGQSAVSFLLGFLSAFLPFCLFVYWIFFRKQKNSSKL
TAFYRGEAIKFILTIVLIVIAFKLLPVLHFIAFFVGFFIALVLNNLIPFILNKRTN
>gnl|CDD|180398 PRK06100, PRK06100, DNA polymerase III subunit psi; Provisional
MSINEKQYLQEMGISQWELIHPERLAGYQPPTQDLDSDCKLLLVAPQCPQNETALLFERILKSMQLELSQ
ARHIEPEQLSQLGYHSLEWVWFAGCDPLSLPAAKQLQSPLLSDIDGNNQHRRALWQQICSYQ
>gnl|CDD|180399 PRK06101, PRK06101, SDR family oxidoreductase
MTAVLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHTQSANIFTLAFDVTDHPGTKAALSQLPF
IPELWIFNAGDCEYMDDGKVDATLMARVFNVNVLGVANCIEGIQPHLSCGHRVVIVGSIASELALPRAEA
YGASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDKNTFAMPMIITVEQASQEIRAQLARGKSHI
YFPARFTWLIRLLGLLPYAWQGRLVRRLLK
>gnl|CDD|235698 PRK06102, PRK06102, amidase
KSTGAKSAAQLAVLIQSGALDPVQVAEQALDAIASYADQAVFISLTEERAMREAEASSARWRAGRSLGLL
DGIPIAWKDLFDVAGSVTTAGSVVLANAAPASRDAAVVALLARAGMVSIGRTNMSEFAFSGLGLNPHYGT
PVNPRSTDVPRIPGGSSSGSAVAVAAGLVPVAMGTDTGGSVRIPAAFNGLVGYKATRGRYSMDGVFPLAK
SLDSLGPLCRSVRDAVWIDAAMRGLTAPDVVRRPLAGLRLVVPETVVFDDAEPGVRAAFEAAVERLQAAG
ALVERQAFPAFQEILDLIARHGWLVTAEAFALHQERLDGPDAARMDPRVVKRTRLGRKITASDYIALLEA
RERLIAQVTRELGGALLATPTVAHVAPPLAPLEADDDLFFATNLKTLRNTMPGNFLDMCGVSLPCGTGAA
GMPVGLLLSAPAGRDERLLRAALAVEAVIRGD
>gnl|CDD|180401 PRK06105, PRK06105, aminotransferase; Provisional
MTMLPNSLEARDIAYHLHPYTNARRHEEEGPLVIERGEGIYVYDDAGKRYIEGMAGLWSVALGFSEQRLV
EAAARQMKKLPFYHTFSHKSHGPVIDLAEKLVAMAPVPMSKVFFTNSGSEANDTVVKLVWYYNNALGRPE
KKKIISRQRGYHGVTIASASLTGLPNNHRSFDLPLDRILHTGCPHYYRFGLPGESEEAFATRLANELEAL
ILAEGPDTIAAFIGEPVMGAGGVIVPPKTYWEKIQAVLRKYDILLVADEVICGFGRTGNMFGCETFGIKP
DILVMSKQLSSSYQPLSAVLMNEKVYDPIADESGKIGTFGHGFTASGHPVAAAVALENLAIIEERDLVGN
AAERGARLQARLRALADHPLVGEVRGVGLIAAVELVADKATKTPFEPPGKVGARANAAAHEHGVISRAMG
DTLAFCPPLIITAAQVDEMVDRFGRALDDVAAWVAAGGPA
>gnl|CDD|180403 PRK06107, PRK06107, aspartate transaminase
MSTFVPAARVSRIKPSPSTAAAARARELRAAGRSIVDLTVGEPDFDTPDHIKQAAVAAIERGETKYTLVN
GTPALRKAIIAKLERRNGLHYADNEITVGGGAKQAIFLALMATLEAGDEVIIPAPYWVSYPDMVLANDGT
PVIVACPEEQGFKLTPEALEAAITPRTRWLILNAPSNPTGAVYSRAELRALADVLLRHPHVLVLTDDIYD
HIRFDDEPTPHLLAAAPELRDRVLVTNGVSKTYAMTGWRIGYAAGPADLIAAINKLQSQSSSCPSSISQA
AAAAALNGDQSFVTESVAVYKQRRDYALALLNAIPGLSCLVPDGAFYLYVNCAGLIGKTTPEGKVLETDQ
DVVLYLLDSAGVAVVQGTAYGLSPYFRLSIATSLETLEEACARIERAVAALR
>gnl|CDD|180404 PRK06108, PRK06108, pyridoxal phosphate-dependent aminotransferase
ARPAARALPESGIREVANAGRGREGVLPLWFGESDLPTPDFIRDAAAAALADGETFYTHNLGIPELREAL
ARYVSRLHGVATPPERIAVTSSGVQALMLAAQALVGPGDEVVAVTPLWPNLVAAPKILGARVVCVPLDFG
GGGWTLDLDRLLAAITPRTRALFINSPNNPTGWTASRDDLRAILAHCRRHGLWIVADEVYERLYYAPGGR
APSFLDIAEPDDRIIFVNSFSKNWAMTGWRLGWLVAPPALGQVLEKLIEYNTSCVAQFVQRAAVAALDEG
EDFVAELVARLRRSRDHLVDALRALPGVEVAKPDGAMYAFFRIPGVTDSLALAKRLVDEAGLGLAPGTAF
GPGGEGFLRWCFARDPARLDEAVERLRRFLAR
>gnl|CDD|235699 PRK06110, PRK06110, threonine dehydratase
MMFTLAELEAAAAVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRV
RGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAER
GLHMVPSFHPDLVRGVATYALELFRAVPDLDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAY
ALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNVAEGAGA
AALAAALQERERLAGKRVGLVLSGGNIDRAVFARVLAGAAAE
>gnl|CDD|180406 PRK06111, PRK06111, acetyl-CoA carboxylase biotin carboxylase subunit; Validated
MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIA
KKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLED
AEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIE
IQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDE
QKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSFTQDDIKRSGHAIEVRIYAEDPKTFFPS
PGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEGIKTNIPL
LLQVLEDPVFKAGGYTTGFLTKQLVKKSTK
>gnl|CDD|235700 PRK06112, PRK06112, acetolactate synthase catalytic subunit; Validated
LSKPLSAPGFTLNGTVAHAIARALKRHGVEQIFGQSLPSALFLAAEAIGIRQIAYRTENAGGAMADGYAR
VSGKVAVVTAQNGPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVT
VAERIDDYVDQAFTAATSGRPGPVVLLLPADLLTAAAAAPAAPRSNSLGHFPLDRTVPAPQRLAEAASLL
AQAQRPVVVAGGGVHISGASAALAALQSLAGLPVATTNMGKGAVDETHPLSLGVVGSLMGPRSPGRHLRD
LVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEEVGRNYEALRLVGDARLTLAALTDALRGRD
LAARAGRRAALEPAIAAGREAHREDSAPVALSDASPIRPERIMAELQAVLTGDTIVVADASYSSIWVANF
LTARRAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLN
NGILGFQKHAETVKFGTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITD
PSAFPPISFFEPMDRAAG
>gnl|CDD|135765 PRK06113, PRK06113, 7-alpha-hydroxysteroid dehydrogenase; Validated
MFNSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDIT
SEQELSALADFALSKLGKVDILVNNAGGGGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGV
ILTITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQKML
QHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVSGGGVQELN
>gnl|CDD|180408 PRK06114, PRK06114, SDR family oxidoreductase
PQLFDLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEHIEAAGRRAIQIAADVTSK
ADLRAAVARTEAELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSI
VNIASMSGIIVNRGLLQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTRPEMVHQTKLF
EEQTPMQRMAKVDEMVGPAVFLLSDAASFCTGVDLLVDGGFVCW
>gnl|CDD|235701 PRK06116, PRK06116, glutathione reductase; Validated
MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGY
GFDVTENKFDWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATG
GRPSIPDIPGAEYGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDI
RETLVEEMEKKGIRLHTNAVPKAVEKNADGSLTLTLEDGETLTVDCLIWAIGREPNTDGLGLENAGVKLN
EKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGRRLSERLFNNKPDEKLDYSNIPTVVFSHPPIG
TVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFA
VAIKMGATKADFDNTVAIHPTAAEEFVTMR
>gnl|CDD|180411 PRK06123, PRK06123, SDR family oxidoreductase
MRKVMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRL
FEAVDRELGRLDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRGGAIVN
VSSMAARLGSPGEYIDYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEPGRVDRVKAG
IPMGRGGTAEEVARAILWLLSDEASYTTGTFIDVSGGR
>gnl|CDD|235702 PRK06124, PRK06124, SDR family oxidoreductase
MSILQRFSLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIA
DEEAVAAAFARIDAEHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYG
RIIAITSIAGQVARAGDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAADPAVGPW
LAQRTPLGRWGRPEEIAGAAVFLASPAASYVNGHVLAVDGGYSVHF
>gnl|CDD|235703 PRK06125, PRK06125, short chain dehydrogenase; Provisional
MDLHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVHALDLSSPE
AREQLAAEAGDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIG
AAGENPDADYICGSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTLLKGRARAELGDESRWQ
ELLAGLPLGRPATPEEVADLVAFLASPRSGYTSGTVVTVDGGISARGSA
>gnl|CDD|235704 PRK06126, PRK06126, hypothetical protein; Provisional
AMENTSETPVLIVGGGPVGLALALDLGRRGVDSILVERKDGTAFNPKANTTSARSMEHFRRLGIADEVRS
AGLPVDYPTDIAYFTRLTGYELARFRLPSAREAITPVGGPDGSWPSPELPHRIPQKYLEPILLEHAAAQP
GVTLRYGHRLTDFEQDADGVTATVEDLDGGESLTIRADYLVGCDGARSAVRRSLGISYEGTSGLQRDLSI
YIRAPGLAALVGHDPAWMYWLFNPDRRGVLVAIDGRDEWLFHQLRGGEDEFTIDDVDARAFVRRGVGEDI
DYEVLSVVPWTGRRLVADSYRRGRVFLAGDAAHLFTPTGGYGMNTGIGDAVNLAWKLAAVLNGWAGPALL
DSYEAERRPIAARNTDYARRNADALGSFPVPPEIEDDGPAGDAARRKVGDALSEHARQEFNSPGITLGYR
YDGSPIIVPDGTPPPPDDPGVYVPSACPGGRAPHAWLSDGRSLYDLFGPGFTLLRFGDAAVDVAPLEAAA
AALGVPLAVVDLPGPEAAALYEADLVLVRPDQHVAWRGDAAPDDAAALLDQVLGH
>gnl|CDD|235705 PRK06127, PRK06127, enoyl-CoA hydratase; Provisional
STMSSISSPTGKLLAEKTGGLGRITFNNPARHNAMSLDMWEALPQALAAAEDDDAIRVVVLTGAGEKAFV
SGADISQFEESRSDAEAVAAYEQAVEAAQAALADYAKPTIACIRGYCIGGGMGIALACDIRIAAEDSRFG
IPAARLGLGYGYDGVKNLVDLVGPSAAKDLFYTARRFDAAEALRIGLVHRVTAADDLETALADYAATIAG
NAPLTLRAAKRAIAELLKDEPERDMAACQALVAACFDSEDYREGRAAFMEKRKPVFKGR
>gnl|CDD|180413 PRK06128, PRK06128, SDR family oxidoreductase
MSSAKNQYAMQNPLTQYPQPPFPEQTQEAPGTIHEMQPKPDHGEQSYKGFGRLQGRKALITGADSGIGRA
TAIAFAREGADIALNYLPEEEQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKELGGLDILVN
IAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGASIINTGSIQSYQPSPTLLDYASTKA
AIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSGGQPPEKIPDFGSETPMKRPGQPVEMAPLYVLLAS
QESSYVTGEVFGVTGGLLLS
>gnl|CDD|235706 PRK06129, PRK06129, 3-hydroxyacyl-CoA dehydrogenase; Validated
PMGSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGEAPDAVLARI
RVTDSLADAVADADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAH
PINPPYLIPVVEVVPAPWTAPATLARAEALYRAAGQSPVRLRREIDGFVLNRLQGALLREAFRLVADGVA
SVDDIDAVIRDGLGLRWSFMGPFETIDLNAPGGVADYAQRYGPMYRRMAAERGQPVPWDGELVARVEAER
RAALPLDQLAARQAWRDRRLMALAAHRR
>gnl|CDD|235707 PRK06130, PRK06130, 3-hydroxybutyryl-CoA dehydrogenase; Validated
MNPIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPLGIASAGMGRIRME
AGLAAAVSGADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFT
PADVIPLVEVVRGDKTSPQTVATTMALLRSIGKRPVLVKKDIPGFIANRIQHALAREAISLLEKGVASAE
DIDEVVKWSLGIRLALTGPLEQRDMNGLDVHLAVASYLYQDLENRTTPSPLLEEKVEAGELGAKSGQGFY
AWPPERREEVLADKSAALVEVRAWLESREPV
>gnl|CDD|235708 PRK06131, PRK06131, dihydroxy-acid dehydratase; Validated
TPGLLRSLAWFGDDDFRAFYHRSFMKNQGYPDELFDGRPIIGICNTWSDLNPCNAHFRQLAERVKRGVLE
AGGFPVEFPVISLGESFLRPTAMLYRNLAAMDVEEMIRGYPIDGVVLLGGCDKTTPALLMGAASVDLPAI
VLSGGPMLNGKHKGERLGSGTDVWKYWEELRAGEIDLEEFLEAEAGMARSAGTCNTMGTASTMACMAEAL
GMSLPGNAAIPAVDARRIRMAELTGRRIVEMVHEDLKPSDILTREAFENAIRVNAAIGGSTNAVIHLIAI
AGRAGVELDLDDWDRIGRDVPVLVNLQPSGEYLMEDFYYAGGLPAVLRELGELLHLDALTVNGKTLGENL
AGAPVYNDDVIRPLDNPLKPEGGIAVLRGNLAPDGAVIKPSAASPELLKHEGRAVVFEGYEDYKARIDDP
DLDVDEDTVLVLRNAGPKGYPGMPEVGNMPIPKKLLRQGVKDMVRISDARMSGTAYGTVVLHVAPEAAAG
GPLALVRTGDRIRLDVPARRLDLLVSDEELARRRAAWPPPPPRAERGYQELYRDHVLQADEGCDFDFLVG
YRGAPVPRDSH
>gnl|CDD|235709 PRK06132, PRK06132, hypothetical protein; Provisional
GAMRMRRLLALGLLAAALLVDAAPAPPAPPPPASSPAKAAPKSLKPGEFLWKPEAKPQGPLVIVVSLDEQ
RLYVYDNGILIAVSTVSTGKRGHETPTGVFSILQKDKDHRSNIYSNAPMPYMQRLTWSGIALHAGNLPGY
PASHGCVRLPSAFAKKLYGWTRMGTTVIISDGEVAPVEVAHPLLLAPKAAPAPAPASDAAANGRPAAPAP
APAEAAWADADAPTGPISILVSRADQRLYVRRNFQPIFEAPVTIAAPEAPLGTHVFTLGALDDGGGTARW
SVVSLPLSKTRRKRLGITVGEAAPATPDSPAEALDRITIPPDFRRRIAALLTPGSTLVITDQGIGGETGS
GTDFIVITR
>gnl|CDD|235710 PRK06133, PRK06133, glutamate carboxypeptidase; Reviewed
RLLRLALLALLAAAAAAGAAAAAPDAELLAAAQQEQPAYLDTLKELVSIESGSGDAEGLKQVAALLAERL
KALGAKVERAPTPPSAGDMVVATFKGTGKRRIMLIAHMDTVYLPGMLAKQPFRIDGDRAYGPGIADDKGG
VAVILHALKILQQLGFKDYGTLTVLFNPDEETGSPGSRELIAELAAQHDVVFSCEPGRAKDALTLATSGI
ATALLEVKGKASHAGAAPELGRNALYELAHQLLQLRDLGDPAKGTTLNWTVAKAGTNRNVIPASASAQAD
VRYLDPAEFDRLEADLQEKVKNKLVPDTEVTLRFERGRPPLEANAASRALAEHAQGIYGELGRRLEPIDM
GTGGGTDAAFAAGSGKAAVLEGFGLVGFGAHSNDEYIELNSIVPRLYLLTRMIMELSRDK
>gnl|CDD|180419 PRK06134, PRK06134, putative FAD-binding dehydrogenase; Reviewed
TPSAAAYPPDLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGTTAWSGGWMWIPRNPLARRAG
IVEDIEQPRTYLRHELGARYDAARIDAFLEAGPHMVAFFERHTALRFADGNAIPDYHGDTPGAATGGRSL
IAAPFDGRELGALLERLRKPLRETSFMGMPIMAGADLAAFLNPTRSFRAFLHVARRFARHLIDLARHGRG
MHLVNGNALVARLLKSAEDLGVRIWESAPARELLREDGRVAGAVVETPGGLQEIRARKGVVLAAGGFPHD
PARRAALFPRAPTGHEHLSLPPPGNSGDGLRLGESAGGVVATDLASPVAWAPVSLVPHADGSVGHFPHII
ERGKPGLIGVLANGKRFVNEADSYHDYVAAMFAATPPGQPVRSWLICDHRFLRRYGLGHIRPAPLPLGPY
VRSGYLKRGASLEELARACGIDPDGLEATVARYNRHARNGQDPDFGRGSTPYNRKQGDPAHGGPNPCVAP
IEHGPFYAVKVLPGCLGTFAGLKTDADARVLDQAGQPIPGLYAAGNDMASVMGGFYPSGGITLGPALTFG
YIAGRHIAGASGYEAEQSAGA
>gnl|CDD|235711 PRK06136, PRK06136, uroporphyrinogen-III C-methyltransferase
MMGKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEIN
RLLVDYARKGKVVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSV
TFVTGHEAAGKLEPEVNWSALADGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVR
GTLGTIAEGAAAEDIQSPAIIVIGEVVALRAKLAWFEAQ
>gnl|CDD|235712 PRK06138, PRK06138, SDR family oxidoreductase
MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGGRAFARQGDVGSAEAVEA
LVDFVAARWGRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTAS
QLALAGGRGRAAYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFARHADPEALREALRA
RHPMNRFGTAEEVAQAALFLASDESSFATGTTLVVDGGWLAA
>gnl|CDD|235713 PRK06139, PRK06139, SDR family oxidoreductase
MMGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQ
VKALATQAASFGGRIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFIN
MISLGGFAAQPYAAAYSASKFGLRGFSEALRGELADHPDIHVCDVYPAFMDTPGFRHGANYTGRRLTPPP
PVYDPRRVAKAVVRLADRPRATTTVGAAARLARLAHFLAPGLTARLMGRLTRRYLARAPRAARSSGNLFA
PPSGAGGIDGGWRSRPRVRARAVAAPLLIGAAAAALIAGAVLARSRRRRR
>gnl|CDD|180421 PRK06141, PRK06141, ornithine cyclodeaminase family protein
MLVIDAEQTRQALPFPALIEALRDAFARGCVMPVRHVHSLEVPGEAQATLLLMPAWNEGRYIGVKAVTVF
PGNPARGLPGLHSTYLLFDGRTGEPLALVDGTELTARRTAAASALAASYLARKDASRLLVVGTGRLASLL
ALAHASVRPIKQVRVWGRDPAKAEALAAELRAQGFDAEVVTDLEAAVRQADIISCATLSTEPLVRGEWLK
PGTHLDLVGNFTPDMRECDDEAIRRASVYVDTRAGALAEAGDLLIPIAEGVFSPDDIRGELAELCRGQHK
GRTSDDEITLFKSVGTALEDLAAAILVYEALNGR
>gnl|CDD|235714 PRK06142, PRK06142, crotonase/enoyl-CoA hydratase family protein
MMTTYESFTVELADHVAQVTLNRPGKGNAMNPAFWSELPEIFRWLDADPEVRAVVLSGSGKHFSYGIDLP
AMAGVFGQLGKDGLARPRTDLRREILRLQAAINAVADCRKPVIAAVQGWCIGGGVDLISACDMRYASADA
KFSVREVDLGMVADVGSLQRLPRIIGDGHLRELALTGRDIDAAEAEKIGLVNRVYDDADALLAAAHATAR
EIAAKSPLAVRGTKEVLDYMRDHRVADGLRYVATWNAAMLPSKDLTEAIAAHMEKRPPEFTG
>gnl|CDD|180423 PRK06143, PRK06143, enoyl-CoA hydratase; Provisional
MIMLNAHAGVTRDDRGVATLTIRNAGSLNILGTPVILALTQALRWLAADPDVRVLVLRGAGEKAFIGGAD
IKEMATLDQASAEAFISRLRDLCDAVRHFPVPVIARIPGWCLGGGLELAAACDLRIAAHDAQFGMPEVRV
GIPSVIHAALLPRLIGWARTRWLLLTGETIDAAQALAWGLVDRVVPLAELDAAVERLAASLAGCGPQALR
QQKRLLREWEDMPLDVAIDDSVAEFGAAFLTGEPQRHMAAFLNRKR
>gnl|CDD|180424 PRK06144, PRK06144, enoyl-CoA hydratase; Provisional
MAMTTSTDELLLEVRGGIARITFNRPAARNAMTWAMYEGLAEICEAIAADPSIRAVVLRGAGDKAFVAGT
DIAQFRAFSTAEDAVAYERRIDRVLGALEQLRVPTIAAIAGACVGGGAAIAAACDLRIATPSARFGFPIA
RTLGNCLSMSNLARLVALLGAARVKDMLFTARLLEAEEALAAGLVNEVVEDAALDARADALAELLAAHAP
LTLRATKEALRRLRREGLPDGDDLIRMCYMSEDFREGVEAFLEKRPPKWKGR
>gnl|CDD|102207 PRK06145, PRK06145, acyl-CoA synthetase; Validated
MFNLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAF
AASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQGGLEI
PPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGI
AVLWVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESR
IRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICM
RGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPE
VAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRV
LRDELNG
>gnl|CDD|235715 PRK06147, PRK06147, 3-oxoacyl-(acyl carrier protein) synthase; Validated
MMRALAIVGSGMVTAVGLDAPSSCAAIRARLDNFQETRFIDPPGGEWLIGAPVPLPPPWRGPERLAEMAA
PAIAEALEGLPALDASEAPLLLCVAEEERPGRPPDLEERLLRELEARLGLRLEPGSAVIARGRVSGAVAL
AQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQNSNGFIPGEAAAAVLLGRPAGGEAPGLP
LLGLGLGREPAPVGESEDLPLRGDGLTQAIRAALAEAGCGLEDMDYRIADLNGEQYRFKEAALAEMRLFR
VRKEFFDLWHPAECIGEIGAAIGPALLGVALAASRKGYGPGPNVLCHLSDDDGARAALVLEYRRGPAR
>gnl|CDD|180426 PRK06148, PRK06148, hypothetical protein; Provisional
MTDLSHPAPEFTTKDAEALLAQHFGISATATPLDGERDLNFRLTTDDGADYILKIVNPSEPRVESDFQTA
ALDHLAAVAPDLPVPRLIPSLSGASLASAQDPDGEPRLLRLLSWLPGTPLAEAAPRTEALLDNLGRALGR
LDRALQGFMHPGALRDLDWDLRHAGRARDRLHFIDDPEDRALVERFLARFERNVAPRLAALPAQVIHNDA
NDYNILVDADDGERISGLIDFGDAVHAPRICEVAIAAAYAILDHPDPIGAAAALVAGYHAVYPLQAQELD
LLFDLIRMRLAVSVTNSASRREQTPDNPYLAISEAPAWRLLERLDAMNPRLATARLRKACGFDAVEGAGR
VRAWLDANRGAFAPLVGPDLATLPKASVPVGDAAHPDSAGQRPAEAAAWWDEFCARTGAQLGIGPYGEPR
LVYTDEAFTSRFIEGERRTVHLGVDLFAPAGTPVYAPLAGTVRSVEIEAVPLGYGGLVALEHETPGGDPF
YTLYGHLAHEAVSRLKPGDRLAAGELFGAMGDAHENGGWAPHLHFQLSTDTSLSATEWPGVGEPDYLDVW
AALFPDPAALLGLPDEAVAQSGRDKAEILRERKEHLLPNLSISYSDPIKFVRGWGVWLIDNRGRAYLDCF
NNVCHVGHAHPRVVAAAARQAARLNTNTRYLHDAIVAYAERLTATLPDGLTVAFFVNSGSEANSLALRLA
RAHTGQRDAIVLDHAYHGTTTELIDLSPYKFNRKGGKGRPDHVEVAEVPDSYRGPERWPDAEHGRRFAES
VAEQIAAMAAKGRGPAFFIAESIPSVAGQIFLPEGYLREVYAMVRAAGGVCIADEVQVGFGRVGSHWWAF
ETQGVVPDIVTMGKPIGNGHPMGAVVTTREIADSFDNGMEYFNTFGGNPVSCAIGLAVLDIIEDEDLQRN
ALEIGNYLLAGLRELQDRFDIIGDVRGMGLFLGIELVTDRKTKAPATAIARYVKNGARERGILIGTEGPH
DNVLKIRPPLIFSRADADHLLEVLDDVLAAALK
>gnl|CDD|235716 PRK06149, PRK06149, aminotransferase
MTDEALIDRSSLPAPDVSEAQAERILAEHYGLSGTLTELGSQQDRNFRVDSDGGRFVLKICHAAYAAVEL
EAQHAALRHLAEREPALRVPVVIPALDGEELLTLDVRGQGLRVRLLDYLPGQPLTRLGHLAPASVAGLGA
LCARVARALADFDHPGLDRTLQWDLRHAGPVVAHLLSHITDPAQRARIAEATRDAARRLQPLAPALPLQA
VHLDITDDNVVGSRDADGRWQPDGVIDFGDLVRTWRVADLAVTCASLLHHAGGDPFSILPAVRAYHAVRP
LSEAELKALWPLVVARAAVLVASSEQQLAVDPDNAYVRDNLAHEWEIFDVATSVPFALMEAAILAALGFD
PPPPDLSGWAPLLPGLDPASVALVDLSVLSPHFSAGNWEQPGIDWRLLASAAAAGGVAATRYGEYRLSRT
PLLSAREPATFALGVDLCLPAGTAVAAPFAGTVVRDGQGHLTLRGDALELHLDGVEPAVEDGAAVRAGDP
LGSVAGEGPLRVQLCPVAGLVPPLFARPSQAAAWLALCPSPAPLLGLPCDAPPPDAAALLARRDASFARV
QKHYYADPPQIERGWRHHLFDMAGRSYLDMVNNVTVLGHGHPRLAAAAARQWSLLNTNSRFHYAAVAEFS
ERLAALAPDGLDTVFLVNSGSEANDLAIRLAWAASGRRDVVSVLEAYHGWTVATDAVSTSIADNPQALET
RPDWVHPVESPNTYRGRFRGADSAADYVRDVVAQLEELDASGRGLAGFICEPVYGNAGGIALPPGYLQQV
YAAVRARGGVCIADEVQVGYGRLGHYFWGFEQQGVVPDIITMAKGMGNGHPLGAVITRREIAEALEAEGY
FFSSTGGSPVSCRIGMAVLDVLREEKLQENARRVGDHLKARLEALADRHPLIGAVHGMGLYLGVELVRDR
QTLEPATEETAAICDRLLELGVIMQPTGDHLNILKIKPPLCLDRESADFFVDMLDRVLTEGW
>gnl|CDD|180428 PRK06151, PRK06151, N-ethylammeline chlorohydrolase; Provisional
MRTLIKARWVLGFDDGDHRLLRDGEVVFEGDRILFVGHRFDGEVDRVIDAGNALVGPGFIDLDALSDLDT
TILGLDNGPGWAKGRVWSRDYVEAGRREMYTPEELAFQKRYAFAQLLRNGITTAMPIASLFYRQWAETYA
EFAAAAEAAGRLGLRVYLGPAYRSGGSVLEADGSLEVVFDEARGLAGLEEAIAFIKRVDGAHNGLVRGML
APDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLHGTTPLEWLADVGLLGPRLLIPHATY
ISGSPRLNYSGGDDLALLAEHGVSIVHCPLVSARHGSALNSFDRYREAGINLALGTDTFPPDMVMNMRVG
LILGRVVEGDLDAASAADLFDAATLGGARALGRDDLGRLAPGAKADIVVFDLDGLHMGPVFDPIRTLVTG
GSGRDVRAVFVDGRVVMEDGRLPGVDLAALRAQAQQQFDKLVADYPERDWRRPPVQEIFPPSFPIAEA
>gnl|CDD|235717 PRK06153, PRK06153, hypothetical protein; Provisional
MSQKLISLNPDLKRLRDEGYEVEVRGGHLLVHDVPYVNASREVRLGTLVSTLTLAGDVTTRPDDHVIHFD
GEFPCNADGTPITQIIHSSTAADLGAGLTVQHSFSNKPGGGGYADYYHKMTTYATIISGPARVLDPTASA
RTFRVIEDAEEDSVFNYPDTASSRAGIGALSAKLEGQRIAIIGLGGTGSYILDLVAKTPVREIHLFDGDD
FLQHNAFRSPGAASIEELREAPKKVDYFKSRYSNMRRGIVPHPEYIDEDNVDELDGFTFVFVCVDKGSSR
KLIVDYLEALGIPFIDVGMGLELSNGSLGGILRVTLSTPDKRDHVDGRLPFSDDDDNDVYSSNIQIAELN
ALNAALAVIKWKKLFGFYRDLEDEHHSTYTTDGNMLTNEDGKE
>gnl|CDD|235718 PRK06154, PRK06154, thiamine pyrophosphate-requiring protein
MADGTHALPNAHLPAEAKTMKVAEAVAEILKEEGVELLFGFPVNELFDAAAAAGIRPVIARTERVAVHMA
DGYARATSGERVGVFAVQYGPGAENAFGGVAQAYGDSVPVLFLPTGYPRGSTDVAPNFESLRNYRHITKW
CEQVTLPDEVPELMRRAFTRLRNGRPGPVVLELPVDVLAEELDELPLDHRPSRRSRPGADPVEVVEAAAL
LLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTLNGKSAFPEDHPLALGSGGRARPATVAHFLRE
ADVLFGIGCSLTRSYYGLPMPEGKTIIHSTLDDADLNKDYPIDHGLVGDAALVLKQMIEELRRRVGPDRG
RAQQVAAEIEAVRAAWLAKWMPKLTSDSTPINPYRVVWELQHAVDIKTVIITHDAGSPRDQLSPFYVASR
PGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNNFSMGG
YDKVMPVSTTKYRATDISGDYAAIARALGGYGERVEDPEMLVPALLRALRKVKEGTPALLEVITSEETAL
SRPWP
>gnl|CDD|235719 PRK06155, PRK06155, crotonobetaine/carnitine-CoA ligase; Provisional
GEPLGAGLAARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKR
GDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDL
PLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGR
NSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVS
ILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQRPGSMGRLAP
GFEARVVDEHDQELPDGEPGELLLRADEPFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVD
RIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRL
AYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTADTWDREAAGVQLPRSGT
>gnl|CDD|235720 PRK06156, PRK06156, dipeptidase
MSRSLKKLLAALLLLASLSAATQAAAATLTKPQLDALLYARLKYGAAAIESLRELVAFPTVRVEGVPQHE
NPEFIGFKKLLKSLARDFGLDYRNVDNRVLEIGLGGSGSDKVGILTHADVVPANPELWVLDGTRLDPFKV
TLVGDRLYGRGTEDDKGAIVTALYAMKAIKDSGLPLARRIELLVYTTEETDGDPLKYYLERYTPPDYNIT
LDAEYPVVTAEKGWGTIMATFPKRAADGKGAEIVAMTGGAFANQIPQTAVATLSGGDPAALAAALQAAAA
AQVKRHGGGFSIDFKRDGKDVTITVTGKSAHSSTPESGVNPVTRLALFLQSLDGDLPHNHAADAARYIND
LVGLDYLGEKFGVAYKDDFMGPLTLSPTVVGQDDKGTEVTVNLRRPVGKTPELLKGEIADALAAWQAKHQ
VALDIDYYWGEPMVRDPKGPWLKTLLDVFGHFTGLDAKPVAIAGSTNAKLFPNAVSFGPAMPGVKYTGHT
ENEFKTVEQFMLDLQMYTEMLIRIGNLPKM
>gnl|CDD|180433 PRK06157, PRK06157, acetyl-CoA acetyltransferase; Validated
MATGIKDKVAILGMGCTKFGERWDAGAEDLMVEAFLEALADAGIEPKDIDAAWFGTHYDEIGSGKSGTPL
SRALRLPNIPVTRVENFCATGSEAFRGAVYAVASGAYDIALALGVEKLKDTGYGGLPVANPGTLADMTMP
NVTAPGNFAQLASAYAAKYGVSREDLKRAMAHVSVKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGL
FDCCGVSDGAAAAIVTTPEIARALGKKDPVYVKALQLAVSNGWELQYNGWDGSYFPTTRIAARKAYREAG
ITDPREELSMAEVHDCFSITELVTMEDLGLSERGQAWRDVLDGFFDADGGLPCQIDGGLKCFGHPIGASG
LRMLYEMYLQLLGRAGERQLKNPRLALTHNLGGAPGQNVCSVSIVGRE
>gnl|CDD|180434 PRK06158, PRK06158, thiolase; Provisional
MMERFLRGRTAIVGAATAGLGEAPGLSAMELLAQAAHRALADAGLTMADVDGLFTASPDDALWGLSVAEY
LGIRPRFVDGTMIGGSSFLAHLLPAALALEAGLCDVALICYGSNQRSAGGKLRSMLDPQPYEAPYKPVNP
VSAYALAAARHMHQYGTTREQLAEVAVAARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTD
GAGAVVMVRADRARDLPRPPVYVLGAAAATWHRQISSMPDLTVTAAAESGPRAFAMAGLTPADIDVVELY
DAFTINTILFLEDLGFCAKGEGGAFVEGGRIAPGGRLPVNTNGGGLSCVHPGMYGLFLLIEAVRQLRGEA
GERQVAGAEVALAHGNGGVLSSQATAILGTAATL
>gnl|CDD|180435 PRK06161, PRK06161, putative monovalent cation/H+ antiporter subunit F; Reviewed
MLAWAILIAQVALALAMLLALWRLLRGPRAQDRILALDTLYINAILLLLVFGIRLGSTIYFEAALLIALL
GFVSTVALAKFLLRGEVIE
>gnl|CDD|235721 PRK06163, PRK06163, hypothetical protein; Provisional
SNSAVTRSNAKVMNRFDLTCRLVAKLKDEEAVIGGIGNTNFDLWAAGQRPQNFYMLGSMGLAFPIALGVA
LAQPKRRVIALEGDGSLLMQLGALGTIAALAPKNLTIIVMDNGVYQITGGQPTLTSQTVDVVAIARGAGL
ENSHWAADEAHFEALVDQALSGPGPSFIAVRIDDKPGVGTTERDPAQIRERFMQGLGVREPI
>gnl|CDD|235722 PRK06164, PRK06164, acyl-CoA synthetase; Validated
TPHDAAPRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNC
IEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIDFAAILAAVPPDALPPLRAI
AVVDDAADATPAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHA
RAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEML
RRILDTAGERADFPSARLFGFASFAPALGELAALARARGVPLTGLYGSSEVQALVALQPATDPVSVRIEG
GGRPASPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDG
QFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAFVIPTDGASPDEAGLMAA
CREALAGFKVPARVQVVEAFPVTESANGAKIQKHRLREMAQARLAAERAA
>gnl|CDD|180437 PRK06169, PRK06169, putative amidase; Provisional
PTDLADLTAVELLAAYRRGELSPVEATQAVLDRIDRRDPAVNAFCLVDAEGALAAARASEERWRRGEPCG
LLDGVPVSIKDIFLTRGWPTLRGSRAIDADGPWDVDAPAVARLREAGAVLLGKTTTPEFGWKGVTDSPLY
GITRNPWDTRLTAGGSSGGAAAAVALGMGPLSVGTDGGGSVRIPASFCGTFGFKPTFGRVPLYPASPFGT
LAHVGPMTRTVADAALLLDVIARPDARDWSALPPPTTSFLDALDRDVRGLRIAYSPTLGYVDVDPEVAAL
VAQAVQRLAALGARVEEVDPGFSDPVEAFHVLWFAGAARLLRALPPGQRALLDPGLRRIAERGATYSASD
YLDATAVRAALGARMGAFHERYDLLLTPTLPIPAFEAGHDVPPGSGLTDWTQWTPFTYPFNLTQQPAASV
PCGFTAAGLPVGLQIVGPRHSDDLVLRVARAYEQALPWPHGAPAAT
>gnl|CDD|235723 PRK06170, PRK06170, amidase; Provisional
MSAKAADEWSFLPATELAAALAAGEVSSVELTDLAIARIERHDGKINAIVVRDFDRARAAARAADAARAR
GERGPLLGIPVTVKESFNVAGLPTTWGFPDLRDYVPAEDAVAVARLKAAGAVILGKTNVPLGLQDWQSYN
EIYGTTNNPWDLARTPGGSSGGSAAALAAGFGALSIGSDIGGSLRVPAHYCGVYAHKPTLGLVPLRGHIP
PPAPALPGQADLAVAGPMARSARDLALLLDVMAGPDPLDGGVAYRLALPPARHGRLKDFRVLVLDEHPLL
PTDAAVRAAIERLAAALADAGARVVRHSPLLPDLAESARLYMRLLFAASAARFPPDAYADAQARAAGLSA
DDRSLAAERLRGAVLSHRDWLFADAAREELRAAWRRFFAEFDVVLCPVTPTPAFPHDHAPDPLERRIDID
GVSYPYWDQLVWAGLATLPGLPATAIPIGLSATGLPVGVQIVGPALEDRTPLRLAELLEEEFGGFRPPPL
>gnl|CDD|180439 PRK06171, PRK06171, sorbitol-6-phosphate 2-dehydrogenase; Provisional
MQDWLNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQHENYQFVPTDVSSAEEVNHTVAE
IIEKFGRIDGLVNNAGINIPRLLVDEKDPAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVI
VNMSSEAGLEGSEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEATGLRTPEYEEALAYTRG
ITVEQLRAGYTKTSTIPLGRSGKLSEVADLVCYLLSDRASYITGVTTNIAGGKTRG
>gnl|CDD|180440 PRK06172, PRK06172, SDR family oxidoreductase
MSMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAE
VKALVEQTIAAYGRLDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIV
NTASVAGLGAAPKMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEADPRKAEFAA
AMHPVGRIGKVEEVASAVLYLCSDGASFTTGHALMVDGGATAQ
>gnl|CDD|180442 PRK06175, PRK06175, L-aspartate oxidase; Provisional
MNLYADVLIVGSGVAGLYSALNLRKDLKILMVSKGKLNECNTYLAQGGISVARNKDDITSFVEDTLKAGQ
YENNLEAVKILANESIENINKLIDMGLNFDKDEKELSYTKEGAHSVNRIVHFKDNTGKKVEKILLKKVKK
RKNITIIENCYLVDIIENDNTCIGAICLKDNKQINIYSKVTILATGGIGGLFKNSTNQRIITGDGIAIAI
RNNIKIKDLDYIQIHPTAFYEETIEGKKFLISESVRGEGGKLLNSKGERFVDELLPRDVVTKAILEEMKK
TGSNYVYLDITFLDKDFLKNRFPTIYEECLKRGIDITKDAIPVSPAQHYFMGGIKVDLNSKTSMKNLYAF
GEVSCTGVHGANRLASNSLLEGLVFSKRGAEKINSEIDNIKLNITKVYTLKHDVEYYSLLNKKIIIKEIE
KLRGDLKDELVSC
>gnl|CDD|180443 PRK06176, PRK06176, cystathionine gamma-synthase
MRMQTKLIHGGISEDTTTGAVSVPIYQTSTYRQDAIGRPKGYEYSRSGNPTRFALEELIADLEGGVKGFA
FASGLAGIHAVFSLFQSGDHVLLGDDVYGGTFRLFDKVLVKNGLSCTIIDTSDLSQIKKAIKPNTKALYL
ETPSNPLLKITDLAQCASVAKDHGLLTIVDNTFATPYYQNPLLLGADIVVHSGTKYLGGHSDVVAGLVTT
NNEALAQEIAFFQNAIGGVLGPQDSWLLQRGIKTLGLRMEAHQKNALCVAEFLEKHPKVEKVYYPGLPTH
PNHELAKKQMRGFSGMLSFTLKNDSEAVAFVESLKLFILGESLGGVESLVGIPAFMTHACIPKEQREAAG
IRDGLVRLSVGIEHEQDLLEDLEQAFAKIG
>gnl|CDD|235724 PRK06178, PRK06178, acyl-CoA synthetase; Validated
MAEEAYLAELRALQQAAWPAGIPREPEYPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDR
FAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQL
APVVEQVRAETSLRHVIVTSLADVLPAEPTLPLPDSLRAPRLAAAGAIDLLPALRACTAPVPLPPPALDA
LAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATL
VLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVVSFVKKLNPDYRQRWRAL
TGSVLAEAAWGMTETHTCDTFTAGFQDDDFDLLSQPVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVR
TPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAV
LGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPEIRIVDALPMTATGKVRKQDLQ
ALAEELK
>gnl|CDD|235725 PRK06179, PRK06179, short chain dehydrogenase; Provisional
MSNSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPGVELLELDVTDDASVQAAVDEVIAR
AGRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAP
YMALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNFDANAPEPDSPLAEYDRERAVVSKAVAKA
VKKADAPEVVADTVVKAALGPWPKMRYTAGGQASLLSKLRRFMPAGAVDKSLRKTFGLPA
>gnl|CDD|180446 PRK06180, PRK06180, short chain dehydrogenase; Provisional
MSSMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVA
DAEATFGPIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGG
LITMPGIGYYCGSKFALEGISESLAKEVAPFGIHVTAVEPGSFRTDWAGRSMVRTPRSIADYDALFGPIR
QAREAKSGKQPGDPAKAAQAILAAVESDEPPLHLLLGSDALRLVRAKLAALDAEIDAWEAVTVSTDF
>gnl|CDD|235726 PRK06181, PRK06181, SDR family oxidoreductase
GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIE
AAVARFGGIDILVNNAGITMWSRFDELTDLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAG
LTGVPTRSGYAASKHALHGFFDSLRIELADDGVAVTVVCPGFVATDIRKRALDGDGKPLGKSPMQESKIM
SAEECAEAILPAIARRKRLLVMSLRGRLGRWLKLIAPGLVDKIARKAIASGRR
>gnl|CDD|180448 PRK06182, PRK06182, short chain dehydrogenase; Validated
MQKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLASLGVHPLSLDVTDEASIKAAVDTIIA
EEGRIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYT
PLGAWYHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWGDIAADHLLKTSGNGAYAEQAQAVAAS
MRSTYGSGRLSDPSVIADAISKAVTARRPKTRYAVGFGAKPLIFLRRILPDRAFDRLIMSATR
>gnl|CDD|235727 PRK06183, mhpA, bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase
MAAQHPDAHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERWPTLYDLPRAVGIDDEALRVLQAIGLADE
VLPHTTPNHGMRFLDAKGRCLAEIARPSTGEFGWPRRNAFHQPLLEAVLRAGLARFPHVRVRFGHEVTAL
TQDDDGVTVTLTDADGQRETVRARYVVGCDGANSFVRRTLGVPFEDLTFPERWLVVDVLIANDPLGGPHT
YQYCDPARPYTSVRLPHGRRRWEFMLLPGETEEQLASPENVWRLLAPWGPTPDDAELIRHAVYTFHARVA
DRWRSGRVLLAGDAAHLMPPFAGQGMNSGIRDAANLAWKLAAVLRGRAGDALLDTYEQERRPHARAMIDL
AVRLGRVICPTDRLAAALRDAVLPVGTLFPQPRVELGGGDRGLLDDVLGPGFAVLGWGCDPLAGLSDEQR
ARWRALGARFVQVVPAVQAHTAQDDHDSDVDGALRAWLARHGASAVLLRPDRYVAAAADAQTLGALLAAL
AALLHLTRAA
>gnl|CDD|235728 PRK06184, PRK06184, hypothetical protein; Provisional
YTTTDVLIVGAGPTGLTLAIELARRGVSFRLIEKAPEPFPGSRGKGIQPRTQEVFDDLGVLDRVVAAGGL
YPPMRIYRDDGSVAESDMFAHLEPTPDEPYPLPLMVPQWRTERILRERLAELGHRVEFGCELVGFEQDAD
GVTARVAGPAGEETVRARYLVGADGGRSFVRKALGIGFPGETLGIDRMLVADVSLTGLDRDAWHQWPDGD
MGMIALCPLPGTDLFQIQAPLPPGGEPDLSADGLTALLAERTGRTDIRLHSVTWASAFRMNARLADRYRV
GRVFLAGDAAHVHPPAGGQGLNTSVQDAYNLGWKLAAVLAGAPEALLDTYEEERRPVAAAVLGLSTELLD
AIKRGDMRRGRDVQQLDLGYRGSSLAVDGPERTGGLRAGDRAPDAPLLGAAGQPTRLFDLFRGPHWTLLA
FGAGAAAILARRGLRIHRVGDAAEGGDLVDDAGHFRDAYGLTGGTLVLVRPDGYVGLIAAGDDAAALEAY
LARVGLGRKDEY
>gnl|CDD|235729 PRK06185, PRK06185, FAD-dependent oxidoreductase
MAEVETTDCCIVGGGPAGMMLGLLLARAGVDVTVLEKHADFLRDFRGDTVHPSTLELMDELGLLERFLEL
PHQKVRTLRFEIGGRTVTLADFSRLPTPYPYIAMMPQWDFLDFLAEEASAYPNFTLRMGAEVTGLIEEGG
RVTGVRARTPDGPGEIRADLVVGADGRHSRVRALAGLEVREFGAPMDVLWFRLPREPDDPESLMGRFGPG
QGLIMIDRGDYWQCGYVIPKGGYAALRAAGLEAFRERVAELAPELADRVAELKSWDDVKLLDVRVDRLRR
WHRPGLLCIGDAAHAMSPVGGVGINLAIQDAVAAANILAEPLRRGRVSDRDLAAVQRRREFPTRVTQALQ
RRIQRRLLAPALAGRGPLGPPLLLRLLNRLPWLRRLPARLVGLGVRPEHVPTFARRA
>gnl|CDD|180452 PRK06186, PRK06186, hypothetical protein; Validated
TLRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEITDPEDLAGFDGIWCVPGSPYRNDDG
ALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIAPLSCSLVEKTGDIRLR
PGSLIARAYGTLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDGDVRAVELPGHPFFVATLFQPERAA
LAGRPPPLVRAFLRAARAA
>gnl|CDD|235730 PRK06187, PRK06187, long-chain-fatty-acid--CoA ligase; Validated
MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYL
EAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAP
LAPEVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDV
YLVIVPMFHVHAWGLPYLALMAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDF
SSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLPGQWTKRRSAGRPLPGVEA
RIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDV
IISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKL
PKRIAFVDELPRTSVGKILKRVLREQYAEGK
>gnl|CDD|235731 PRK06188, PRK06188, acyl-CoA synthetase; Validated
QATMADLLHSGATYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSL
NRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPAPFVERALALLARVPSLKHVLTL
GPVPDGVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADP
RFLMCTPLSHAGGAFFLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDL
SSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPKRLTSCGRPTPGLRV
ALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIV
TGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPK
QVDFVDSLPLTALGKPDKKALRARYWEGRGRAVG
>gnl|CDD|235732 PRK06189, PRK06189, allantoinase; Provisional
MMYDLIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAREIIDADGLYVFPGMIDVHVHFNEPGRTH
WEGFATGSAALAAGGCTTYFDMPLNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNLEHLRELAE
AGVIGFKAFMSNSGTDEFRSSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLE
SRPVVAELEAVQRALLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGA
VAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHSPCPPELKEGDDFFLVWGGISGGQSTLLVMLTEGYIE
RGIPLETIARLLATNPAKRFGLPQKGRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRV
VATYLRGQCVYQDGEVFPPPRGQLLRPSVVK
>gnl|CDD|235733 PRK06190, PRK06190, enoyl-CoA hydratase; Provisional
MTEPILLVETHDRVRTLTLNRPEARNALSAALRRALFAALAEADADDDVDVVVLTGADPAFCAGLDLKEL
GGDGSAYGAQDALPNPSPAWPAMRKPVIGAINGAAVTGGLELALACDILIASERARFADTHARVGILPGW
GLSVRLPQKVGIGRARRMSLTGDFLDAADALRAGLVTEVVPHDELLPRARRLAASIAGNNPAAVRALKAS
YDDGAAAQTGDALALEAEAARAHNRSVSPDGIAARREAVMARGRAQVR
>gnl|CDD|235734 PRK06193, PRK06193, hypothetical protein; Provisional
MARRAMALLGALLLILLGAGSGEEAASDEADDKTLLESLQKGGYVIYFRHAATDRSQADQDTSDMDDCST
QRNLSEEGREQARAIGEAFRALAIPVGKVISSPYCRAWETAQLAFGRHEKEIRLNFLNSEPVPAERNALL
KAGLRPLLTTPPDPGTNTVLVGHDDNLEAATGIYPEPEGEAAVFEPLGGEGFKLLGNLPPEDWARL
>gnl|CDD|180458 PRK06194, PRK06194, hypothetical protein; Provisional
MKDFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQV
EALADAALERFGAVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEKDPAYE
GHIVNTASMAGLLAPPAMGIYNVSKHAVVSLTETLYQDLSLVTDQVGASVLCPYFVPTGIWQSERNRPAD
LANTAPPTRSQLIAQAMSQKAVGSGKVTAEEVAQLVFDAIRAGRFYIYSHPQALASVRTRMEDIVQQRNP
SDPFADK
>gnl|CDD|235735 PRK06195, PRK06195, DNA polymerase III subunit epsilon; Validated
MNFVAIDFETANEKRNSPCSIGIVVVKDGEIVEKVHYLIKPKEMRFMPINIGIHGIRPHMVEDELEFDKI
WEKIKHYFNNNLVIAHNASFDISVLRKTLELYNIPMPSFEYICTMKLAKNFYSNIDNARLNTVNNFLGYE
FKHHDALADAMACSNILLNISKELNSKDINEISKLLGVTLGYVNENGYKPSSRKGRILKRSNRQAPRKKK
KIIESFGFTAFKEEVVVFTGGLASMTRDEAMILVRRLGGTVGSSVTKKTTYLVTNTKDIEDLNREEMSNK
LKKAIDLKKKGQNIKFLNEEEFLQKCKEK
>gnl|CDD|235736 PRK06196, PRK06196, oxidoreductase; Provisional
RQHPIGSGFGAASTAEEVLAGHDLSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGI
DGVEVVMLDLADLESVRAFAERFLDSGRRIDILINNAGVMACPETRVGDGWEAQFATNHLGHFALVNLLW
PALAAGAGARVVALSSAGHRRSPIRWDDPHFTRGYDKWLAYGQSKTANALFAVHLDKLGKDQGVRAFSVH
PGGILTPLQRHLPREEQVALGWVDEHGNPIDPGFKTPAQGAATQVWAATSPQLAGMGGLYCEDCDIAEPT
PKDAPWSGVRPHAIDPEAAARLWALSAALTGVDAF
>gnl|CDD|235737 PRK06197, PRK06197, short chain dehydrogenase; Provisional
MKMTKWTAADIPDQSGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAATPGADVT
LQELDLTSLASVRAAADALRAAYPRIDLLINNAGVMYTPKQTTADGFELQFGTNHLGHFALTGLLLDRLL
PVPGSRVVTVSSGGHRIRAAIHFDDLQWERRYNRVAAYGQSKLANLLFTYELQRRLAAAGATTIAVAAHP
GVSNTELARNLPRALRPVATVLAPLLAQSPEMGALPTLRAATDPAVRGGQYYGPDGFGEQRGYPKVVASS
AQSHDEDLQRRLWAVSEELTGVSFPV
>gnl|CDD|180462 PRK06198, PRK06198, short chain dehydrogenase; Provisional
MGRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVED
CRRVVAAADEAFGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAEGTIV
NIGSMSAHGGQPFLAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATEGEDRIQREFHGAPDDWL
EKAAATQPFGRLLDPDEVARAVAFLLSDESGLMTGSVIDFDQSVWGAYDG
>gnl|CDD|235738 PRK06199, PRK06199, ornithine cyclodeaminase; Validated
MTTSTKIDFIYLSEQDMIRAGVTDMAACVDTMEEMFGLLYQGDYRMAGANNDSHGAMITFPENSPFPTMP
KPTPDRRFMAMPAYLGGRFRTAGVKWYGSNIANREKGLPRSILMFVLNDADTGAPLAIMSANLLSAYRTG
AVPGVGARHLARKDSKVVGLLGPGVMGKTILAAFMAVCPGIDTIKIKGRGQKSLDSFATWVAETYPQITN
VEVVDSIEEVVRGSDIVTYCNSGETGDPSTYPYVKREWVKPGAFLLMPAACRIDEGMEQGDVRKVVDNTG
LYEAWFEEVPKPAHNLIPVIGVRFMDMIAEGKLTLDQLEDIGDIVAGKAPGRQNDEEIIIMSVGGMPVED
VAWGTVVYRNALEKGIGVKLNLWDTPVLR
>gnl|CDD|235739 PRK06200, PRK06200, 2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
MGWLHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRA
VDQTVDAFGKLDCFVGNAGIWDYNTSLVDIPAETLDTAFDEIFNVNVKGYLLGAKAALPALKASGGSMIF
TLSNSSFYPGGGGPLYTASKHAVVGLVRQLAYELAPKIRVNGVAPGGTVTDLRGPASLGQGETSISDSPG
LADMIAAITPLQFAPQPEDHTGPYVLLASRRNSRALTGVVINADGGLGIRGIR
>gnl|CDD|180465 PRK06201, PRK06201, hypothetical protein; Validated
MAIGFRVLPSWPRVDAALVEAFRELPVANISDSMNRMTAGGAGLRPMHRGGRLAGTALTVRTRPGDNLMI
HRALDLARPGDVIVVDGGGDLTNALVGEIMLAIAARRGVAGVVIDGAVRDVAALREMGFPVFARGVTHRG
PYKDGPGEINVPVAIGGMVIEPGDLIVGDDDGLVAVPPADAEALLEAARAKHAAEAKQLEAIRAGRYDRS
WVDRALARAGC
>gnl|CDD|180466 PRK06202, PRK06202, hypothetical protein; Provisional
MPWGDLSRRRDRQPEVMDDPGCDPARLDRTYAGFRRVNRIVAGWRGLYRRLLRPALSADRPLTLLDIGCG
GGDLAIDLARWARRDGLRLEVTAIDPDPRAVAFARANPRRPGVTFRQAVSDELVAEGERFDVVTSNHFLH
HLDDAEVVRLLADSAALARRLVLHNDLIRSRLAYALFWAGTRLLSRSSFVHTDGLLSVRRSYTPAELAAL
APQGWRVERQWPFRYLLVWDPH
>gnl|CDD|235740 PRK06203, aroB, 3-dehydroquinate synthase; Reviewed
MRVIRQSFAVTFEYPVYFTRDLFSPENPLLAEVLAADGEGKPKKVLVVIDSGVLRAHPDLLEQITAYFAA
HADVLELVAEPLVVPGGEAAKNDPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRL
IRIPTTVLAQNDSGVGVKNGINAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDA
AFFDWLEAHAAALAARDPEAMEELIYRCAELHLEHIAGGGDPFEFGSSRPLDFGHWSAHKLEQLTNYALR
HGEAVAIGIALDSLYSYLLGLLSEAEAQRILALLRALGFPLYHPALATRDSKGRELLKGLEEFREHLGGR
LTITLLTGIGRGIEVHEIDLDLLRQAIARLAERAKASTA
>gnl|CDD|235741 PRK06205, PRK06205, acetyl-CoA C-acetyltransferase
MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAA
LDAGLPVTVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLH
DRLARGRETAGGRRFPVPGGMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQ
RKGDPTVVDRDEHPRADTTLESLAKLRPIMGKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPL
ARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADDEERLNV
NGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAAVFERVN
>gnl|CDD|235742 PRK06207, PRK06207, pyridoxal phosphate-dependent aminotransferase
MMSIEAKFARLGTDNAPGQEVRQSAAGLEALLRGEPLPGRPVDFSHGDVDAHEPTPGAFELFSAGVERGG
VQAYTEYRGDADIRELLAARLAAFTGAPVDAADELIITPGTQGALFLAVAATVARGDKVAIVQPDYFANR
KLVEFFEGEMVPVQLDYLSADKRAGLDLDQLEEAFKAGVRVFLFSNPNNPAGVVYSAEEIAQIAALARRY
GATVIVDQLYSRLLYDGTSYTHLRALPIDPENVITIMGPSKTESLSGYRLGVAFGSPAIIDRMEKLQAIV
SLRAAGYSQAVLRTWFSEPDGWMKDRIARHQAIRDDLLRVLRGVEGVFVRAPQAGSYLFPRLPRLAVSLH
DFVKILRLQAGVIVTPGTEFSPHTADSIRLNFSQDHAAAVAAAERIAQLIERYRA
>gnl|CDD|235743 PRK06208, PRK06208, class II aldolase/adducin family protein
MSAVLSRAADTAAALSIPQPPREGLWFPRPPPFATVAEERLHRKQRLAAAFRLFARFGFDEGLAGHITAR
DPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVEGDRPLNRAAFAIHSAIHEARPDVVAAAHTHSTYG
KAWSTLGRPLDPITQDACAFYEDHALFDDFTGVVVDTSEGRRIAAALGTHKAVILQNHGLLTVGPSVDAA
AWWFIALERACQTQLLAEAAGPPQPIDHETARHTRSQVGSEYGGWFNFQPLYQRIVAEEPDLLD
>gnl|CDD|180471 PRK06209, PRK06209, glutamate-1-semialdehyde 2,1-aminomutase; Provisional
SQLLQSRLHALIPGGAHTYAKGDDQYPELAPGFIQRGSGAHVWDVDGNEYIEYGMGLRAVGLGHAYPPVV
EAVREALQDGCNFTRPSAIELDAAESFLELIDGADMVKFCKNGSDATSAAVRLARAYTGRDLVARCADHP
FFSTDDWFIGTTPMSAGIPASVSALTVTFRYNDIASLEALFEDHPGRIACVILEPATADEPQDGFLHEVR
RLCHENGALFILDEMITGFRWHMRGAQKLYGIVPDLSCFGKALGNGFAVSALAGKREYMELGGLEHTDRE
RVFLLSTTHGAETHALAAAIATMAIYRDEDVIERLHEQGAKLAAGVNEAAAEHGLQDHVRVSGRPCCLTY
STLDGNGQPSQAFRTLFLQETIRRGVLMPSLVVSYAHGDADIERTIDAVHGALGVYRKALEDGVEGYLVG
RPVKPVFRRFN
>gnl|CDD|180472 PRK06210, PRK06210, enoyl-CoA hydratase; Provisional
DMAYDAVLYEVADSGVAVITLNRPDRLNAWTPVMEAEVYAAMDRAEADPAVRVIVLTGAGRGFCAGADMG
ELQTIDPSDGRRDTDVRPFVGNRRPDYQTRYHFLTALRKPVIAAINGACAGIGLTHALMCDVRFAADGAK
FTTAFARRGLIAEHGISWILPRLVGHANALDLLLSARTFYAEEALRLGLVNRVVPPDELMERTLAYAEDL
ARNVSPASMAVIKRQLYEDAFQTLAEATARANREMHESLQRPDFIEGVASFLEKRPPRFPGL
>gnl|CDD|235744 PRK06213, PRK06213, crotonase/enoyl-CoA hydratase family protein
MSELVSYTLEDGVATITLDDGKVNALSPAMIDALNAALDQAEDDRAVVVITGQPGIFSGGFDLKVMTSGA
QAAIALLTAGSTLARRLLSHPKPVIVACTGHAIAKGAFLLLSADYRIGVHGPFKIGLNEVAIGMTMPHAA
IELARDRLTPSAFQRAVINAEMFDPEEAVAAGFLDEVVPPEQLLARAQAAARELAGLNMGAHAATKLKVR
AAALEAIRAAIEGDAAEFG
>gnl|CDD|235745 PRK06214, PRK06214, sulfite reductase subunit alpha
LISLIPESAPFSEEQRAWLNGFFAGLLGPDVEGATALSPGEAPALLAAPPAAADDDDAPWHDPSLPIDER
MALAEGRPLPRKLMAAMAQQDCGQCGYNCQDYAEAIASGEEKRLNLCAPGGKETARMLKKLAEEFGAAPA
AAAPAAAAADAAPAAAALGPLGTSRDNPVEATFLSRRRLNKPGSEKETWHVEIDLAGSGLDYEVGDSLGL
FPANDPALVDAVIAALGAPPEFPIGGKTLREALLEDVSLGPAPDGLFELLSYITGGAARKKARALAAGED
PDGDAATLDVLAALEKFPGIRPDPEAFVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRYEIGSRLRLG
VASTFLGERLAPGTRVRVYVQKAHGFALPADPNTPIIMVGPGTGIAPFRAFLHERAATKAPGRNWLFFGH
QRSATDFFYEDELNGLKAAGVLTRLSLAWSRDGEEKTYVQDRMRENGAELWKWLEEGAHFYVCGDAKRMA
KDVERALVDIVAQFGGRSPDEAVAFVAELKKAGRYQADVY
>gnl|CDD|235746 PRK06215, PRK06215, hypothetical protein; Provisional
SPTGYRTRMRRSIRLLVAALALAATVALATGPAQAATWSSSDQWGTWSNGGYTLYNDVWGSGAGPQTIWA
NSYSNWGVWANHPNTGGIKSYPHVAKNIGKPLSSLGTLSSSFNVTVPSSGAYETAYDIWDSSNAYEIMLW
VNYTGAVGPIGSKQTNVSVGGHTWNVYKGSNGSNKVFSFLRTSNTNSGTVDILAVLKWIKTKGWFGDVTV
GEVQFGFEITSSSGGLNFTTNNYSVTSS
>gnl|CDD|168472 PRK06217, PRK06217, hypothetical protein; Validated
MMRIHITGASGSGTTTLGAALAERLDIPHLDTDDYFWLPTDPPFTTKRPPEERLRLLLEDLRPREGWVLS
GSALGWGDPLEPLFDLVVFLTIPPELRLERLRLREFQRYGNRILPGGDMHKASLEFLEWAASYDTAGPEG
RSLAAHEQWLADQSCPVLRLDGDLTVEDLLDEVLDHLASAPGA
>gnl|CDD|235747 PRK06222, PRK06222, sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein
MYKILEKEELAPNVFLMEIEAPRVAKKAKPGQFVIVRIDEKGERIPLTIADYDREKGTITIVFQAVGKST
RKLAELKEGDSILDVVGPLGKPSEIEKFGTVVCVGGGVGIAPVYPIAKALKEAGNKVITIIGARNKDLLI
LEDEMKAVSDELYVTTDDGSYGRKGFVTDVLKELLESGKKVDRVVAIGPVIMMKFVAELTKPYGIKTIVS
LNPIMVDGTGMCGACRVTVGGETKFACVDGPEFDGHLVDFDELMRRLAMYKEEEKLALEKYEEKLGHKGG
G
>gnl|CDD|180477 PRK06223, PRK06223, malate dehydrogenase; Reviewed
ARKKISIIGAGNVGATLAHLLALKELGDVVLFDIVEGVPQGKALDIAEAAPVEGFDTKITGTNDYEDIAG
SDVVVITAGVPRKPGMSRDDLLGINAKIMKDVAEGIKKYAPDAIVIVVTNPVDAMTYVALKESGFPKNRV
IGMAGVLDSARFRTFIAEELNVSVKDVTAFVLGGHGDSMVPLVRYSTVGGIPLEDLLSKEKLDEIVERTR
KGGAEIVGLLKTGSAYYAPAASIAEMVEAILKDKKRVLPCSAYLEGEYGVKDVYVGVPVKLGKNGVEKII
ELELDDEEKAAFDKSVEAVKKLIEALK
>gnl|CDD|235748 PRK06224, PRK06224, citryl-CoA lyase
MMKGKTKWWRTSISDVTPEEIYVRGYDLEDLIGKLSFTDMIFLLLRGRLPTPNEARLLDAVLVALVDHGL
TPSAAAARMTASGGESLQGAVAAGLLALGSVHGGAGEQAAELLQEIAAAADAGADLDAAARAIVAEYRAA
GKRVPGFGHPLHKPVDPRAPRLLALAREAGVAGRHCRLAEALEAALAAAKGKPLPLNVDGAIAAILADLG
FPPALARGLFVISRAAGLVAHVWEELQQPIGFRIWDPAEEAVEYTGPPPRELE
>gnl|CDD|235749 PRK06225, PRK06225, pyridoxal phosphate-dependent aminotransferase
KKYAKAAKVPPSGFKTSNEFFDYVFKDKEMIWMGQNTNHLGPHEEVREAMIRCIEEGEYCKYPPPEGFPE
LRELILKDLGLDDDEALITAGATESLYLVMRAFLSPGDNAVTPDPGYLIIDNFASRFGAEVIEVPIYSEE
CNYKLTPELVKENMDENTRLIYLIDPLNPLGSSYTEEEIKEFAEIARDNDAFLLHDCTYRDFAREHTLAA
EYAPEHTVTSYSFSKIFGMAGLRIGAVVATPDLIEVVKSIVINDLGTNVIAQEAAIAGLKVKDEWIDRIR
RTTFKNQKLIKEAVDEIEGVFLPVYPSHGNMMVIDISEAGIDPEDLVEYLLERKIFVRQGTYTSKRFGDR
YIRVSFSIPREQVEVFCEEFPDVVETLRTS
>gnl|CDD|235750 PRK06228, PRK06228, F0F1 ATP synthase subunit epsilon; Validated
ASMNLKILLPFEVFAEKKGVTRIVAETREGSFGLLPHRLDCVAALVPGILVYETEAEGEVYVAVDEGILV
KTGPDVLVSVRNAIGGTDLGELREAVEQEFLTLDERERSVRSALAKLESGFIRRFMELKHD
>gnl|CDD|180481 PRK06231, PRK06231, F0F1 ATP synthase subunit B; Validated
MKLWKTRVFKLLLLSFSFLIISLFLVSCTENVEELKSKSIINELFPNFWVFIAHLIAFSILLLLGIFLFW
KPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEIIDQANYEALQLKSELEKEANR
QANLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFIRELEANEK
>gnl|CDD|180482 PRK06233, PRK06233, vitamin B12 independent methionine synthase
ETTQTKAPFRFDIVGSFLRPERLKEAREQFAIGEISQDQLLKIQHAEIKRLVKEQVELGLKAVTDGEFNR
SWWHLDFLWGLNGVGKYEYEDSYKFHGAKTRTDNAELAGKVAFNPDHPFFAAFKYLKSIVPEGVLPKQTI
PSPSLLFRDNRSDNWPKFYDSWDDYLDDLAQAYHDTIQHFYDLGARYIQLDDTTWAYLISKLNDTENDPK
EHQKYVKLAEDAVYVINKALADLPEDLTVTTHICRGNFKSTYLFSGGYEPVAKYLGQLNYDGFFLEYDND
RSGSFEPLKQIWNNRDNVRIVLGLITSKFPELEDEDEIIARIDEATEYVPLSNLALSTQCGFASTEEGNI
LTEADQWAKLALVKKIADKVWK
>gnl|CDD|168478 PRK06234, PRK06234, methionine gamma-lyase; Provisional
MENIKKMGFATKAIHGGHIGDKQFGSLATPIYQTSTFIFDSAEQGGRRFAGEESGYIYSRLGNPTSTEVE
NKLALLEGGEAAVVAASGMGAISSSLWSALKAGDHVVASDTLYGCTFALLNHGLTRYGVEVTFVDTSNLE
EVRNALKANTKVVYLETPANPTLKVTDIKAISNIAHENNKECLVFVDNTFCTPYIQRPLQLGADVVVHSA
TKYLNGHGDVIAGFVVGKEEFINQVKLFGIKDMTGSVIGPFEAFLIIRGMKTLQIRMEKHCKNAMKVAKF
LESHPAVEKVYYPGLESFEYYELAKKQMSLPGAMISFELKGGVEEGKVVMNNVKLATLAVSLGDAETLIQ
HPASMTHSPYTAEERKEAGISDGLVRLSVGLEDVDDIIADLKQALDLIVK
>gnl|CDD|235751 PRK06241, PRK06241, phosphoenolpyruvate synthase; Validated
MSSYVLDFQEIDKTQLPLVGGKGANLGELSRAGIPVPEGFCVTTEAYKKFLEQNEEFDALLDQLSALKLE
DREQIGEISAKIREVIEAIEIPEDIVEAIAAALSKFGEDHAYAVRSSATAEDLPTASFAGQQDTYLNVIG
KDAILQHIRKCWASLFTERAVIYRIQNGFDHRKVYMSVVVQKMVFPEASGIMFTADPVTGNRKVLSIDAS
FGLGEALVSGLVSADTYKVREGKIIDKTIATKKLAIYALKEGGTETKEIEPEQQKSQTLTDEQILELARL
GRKIEAHFGCPQDIEWCLADGTFYILQSRPITTLYPIPEVTDPLTHVYISVGHQQMMTDAMKPLGLSFFQ
LTTMDSPAPMGEAGGRLFYDITNLLASPAGRKLLINMLGVSDPLMKDALTTLIKRKDFIKLLPKGKAALK
SISKFLPIIQIYFENDPAIVEELIARSEASIAELKQDIQTKSGDELFDFILEDIQQLKDILFDPQSYAFV
MAGMNASSWLNEKMEKWLGEKNAADTLSQSVPNNITSEMGLALLDVADVIRPYPEVIAYLEHAKDDTFLD
ELVQLDGGEEFRDAIEAFLEKYGMRCPGEIDITKPRWREDPSTLVPMILNNIKNFEPGASKRKFEQGRQE
ALEKEEELLSRLQQLPDGEQKAKETKRMISRLRNFIGYREYPKYGRIRRYGIYKQALLKEAEQLVQAGVL
AEPEDIFYLTFEELREVVRTNKLDYELIAKRKEEYELYEKLTPPRVMTSDGEIITGKYKRENLPAGALIG
LPVSSGVVEGRARVILNPEDADLEKGDILVTAFTDPGWTPLFVSIKGLVTEVGGLMTHGAVIAREYGIPA
VVGVENATKLIKDGQRIRVDGTEGYVEILEE
>gnl|CDD|180484 PRK06242, PRK06242, flavodoxin; Provisional
MKALIVYASVHHGNTEKIAKAIAEVLDAEVIDPGDVNPEDLSEYDLIGFGSGIYFGKFHKSLLKLIEKLP
PVSGKKAFIFSTSGLPFLKYHKALKKKLKEKGFEIVGEFSCKGFDTFGPFKLIGGINKGHPNEKDLENAK
EFAENLKKKL
>gnl|CDD|180485 PRK06245, cofG, FO synthase subunit 1; Reviewed
DVNMSKIVTYSRNVFIPLTYECRNRCGYCTFRRDPGQPSLLSPEEVKEILRRGADAGCTEALFTFGEVPD
ESYERIKEQLAEMGYSSILEYLYDLCELALEEGLLPHTNAGILTREEMEKLKEVNASMGLMLEQTSPRLL
NTVHRGSPGKDPELRLETIENAGKLKIPFTTGILIGIGETWEDRAESLEAIAELHERYGHIQEVIIQNFS
PKPGIPMENHPEPSLEEMLRVVALARLILPPDISIQVPPNLNRDTGLLLLDAGADDLGGISPVTKDYVNP
EYPWPDIEELREILEEAGWPLKERLPVYPKYIKEGWLSERLQELIEALSDAGGYRR
>gnl|CDD|180486 PRK06246, PRK06246, fumarate hydratase; Provisional
MREIHVEDIIEAVAELCIEANYYLPDDVKEALKKAYEKEESPIGKEILKAILENAEIAKEEQVPLCQDTG
MAVVFVEIGQDVHIEGGDLEDAINEGVRKGYEEGYLRKSVVADPLTRKNTGDNTPAVIHTEIVPGDKLKI
TVAPKGGGSENMSALKMLKPADGLEGIKKFVLETVKEAGGNPCPPIIVGVGIGGTFDKAAKLAKKALLRP
IGERNPDPEIAALEEELLEEINKLGIGPMGLGGKTTALDVKIETYPCHIASLPVAVNIQCHAARHAEVVL
>gnl|CDD|180487 PRK06247, PRK06247, pyruvate kinase; Provisional
MKRNRRVKILATLGPASSSEDMIRKLVEAGADVFRLNFSHGDHDDHRELYKRIREVEDETGRPIGILADL
QGPKLRLGRFADGKVQLANGQTFRLDVDDAPGDHDRVSLPHPEIAAALKPGDRLLVDDGKVRLVVEACDG
DDVVCRVVEGGPVSDRKGVSLPGTVLSVSALTEKDRADLEFALELGVDWVALSFVQRPEDVEEVRKIIGG
RVPVMAKIEKPQAIDRLEAIVEASDAIMVARGDLGVEVPLEQVPLIQKRIIRAARRAGKPVVVATQMLES
MIENPVPTRAEVSDVATAVLDGADAVMLSAETASGKYPVEAVRTMARIIRQVERDPTYPPLIHAQRPQPE
ATKRDAISYAARDIAERLDLAALVAYTSSGDTALRAARERPPLPILALTPNPETARRLALTWGVHCVVVD
DARDTDDMVRRADRIALAEGFYKRGDRVVIVAGVPPGTPGSTNMLRIAYIGEDDVS
>gnl|CDD|180488 PRK06249, PRK06249, putative 2-dehydropantoate 2-reductase
MDSETPRIGIIGTGAIGGFYGAMLARAGFDVHFLLRSDYEAVRENGLQVDSVHGDFHLPPVQAYRSAEDM
PPCDWVLVGLKTTANALLAPLIPQVAAPDAKVLLLQNGLGVEEQLREILPAEHLLGGLCFICSNRVGPGV
IHHLAYGRVNLGYHSGPAADDGITARVEEGAALFRAAGIDSQAMPDLAQARWQKLVWNIPYNGLSVLLNA
STDPLMADPDSRALIRALMAEVIQGAAACGHTLPEGYADHMLAVTERMPDYRPSMYHDFEEGRPLELEAI
YANPLAAARAAGCAMPRVEMLYQALEFLDRRNR
>gnl|CDD|235752 PRK06251, PRK06251, V-type ATP synthase subunit K; Validated
MKRASLILSVLLPILISSVIAGAQAPSDTAQGFAGINIGAGLAVGLAAIGAGIAVGMAAAAGIGVLTERR
DMFGTVLIFVAIGEGIAVYGILFAVLMLFGKF
>gnl|CDD|235753 PRK06252, PRK06252, methylcobalamin:coenzyme M methyltransferase; Validated
SELTPKERLLNALKGKEVDRVPVICVTQTGTVELMDITGAYWPEAHSDPEKMADLAIAGYEVAGFEAVRV
PFCMTVEAEAMGCEVDMGTKDRQPSVTKYPIKKDVEYRKLPDDLLEEGRIPTVLEAIKILKEKVGEEVPI
IAGLTGPISLASSLMGPKNFLKWLIKKPELAHEFLDFVTDFCIEYAKAQLEAGADVICIADPSASPELLG
PKMFEEFVLPYLNKIIDEVKGLPTILHICGDLTSILEEMADCGFDGISIDEKVDVKTAKENVGDRAALIG
NVSTSFTLLNGTPEKVKAEAKKCLEDGVDILAPGCGIAPKTPLENIKAMVEARKEYYAE
>gnl|CDD|235756 PRK06259, PRK06259, succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
MKMITITVKRFDPEKDEPHFESYEVPVKEGMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEP
VLACKTEVEDGMIIEPLDFPVIKDLIVDREPYYKKLKSLRNYLQRKNEKITYPEDIEDIKKLRGCIECLS
CVSTCPARKVSDYPGPTFMRQLARFAFDPRDEGDREKEAFDEGLYNCTTCGKCVEVCPKEIDIPGKAIEK
LRALAFKKGLGLPAHLEVRENVLKTGRSVPKEKPSFLEEVSDIYPYGNEKLRVAFFTGCLVDYRLQEVGK
DAIRVLNAHGISVIIPKNQVCCGSPLIRTGQTDVAEELKKKNLEIFNKLDVDTVVTICAGCGSTLKNDYK
EKEFNVMDITEVLVEVGLEKYKPLDITVTYHDPCHLRRGQGIYEEPRKILRSIPGLEFVEMEIPDQCCGA
GGGVRSGKPEIAEALGKRKAEMIRETGADYVITVCPFCEYHIRDSLKKYSEDIPVMNIVSLLDKVY
>gnl|CDD|235758 PRK06263, sdhA, succinate dehydrogenase flavoprotein subunit; Reviewed
MEDEIMITDVLIIGSGGAGARAAIEAERGKNVVIVSKGLFGKSGCTVMAEGGYNAVLNPEDSFEKHFEDT
MKGGAYLNDPKLVEILVKEAPKRLKDLEKFGALFDRTEDGEIAQRPFGGQSFNRTCYAGDRTGHEMMMGL
MEYLIKERIKILEEVMAIKLIVDENREVIGAIFLDLRNGEIFPIYAKATILATGGAGQLYPITSNPIQKT
GDGFAIAYRAGAELIDMEMVQFHPTGMVYPYSGRGILVTEAVRGEGGILYNKNGERFMKRYDPERMELST
RDVVARAIYTEIQEGRGTNHGGVYLDVTHLPDEVIEEKLETMLEQFLDVGVDIRKEPMEVAPTAHHFMGG
IRINEDCETNIPGLFACGEVAGGVHGANRLGGNALADTQVFGAIAGKSAAKNAENNEFKKVNRSVEEDIA
RIKSEIKFLNGSINPYDLIDELKKTMWDYVSIVRNEKGLKKALEEINELKEKLKDLKVNGIVDFNKALEL
ENMILVAELVIKSALLRKESRGAHYREDYPETNDEWFGNIILNKNKIKFEKRE
>gnl|CDD|235759 PRK06264, cbiC, cobalt-precorrin-8 methylmutase
MGASTKDGLDIANKSREIVKNKIKEVLGDKIKLYSEEEMGIIERVVHATADPEYAKLVVFSNDPIEEGLD
AIKDKKPIIVDINMVKAGIRYNNVYCFISEPEVFELAKKEQITRAVASMRLAKELIDGGIVVIGNAPTAL
FEVIRLVKEEGIKPKLVVGVPVGFVKAAESKEALRNTNIPSISTIGPKGGTPVAVSIINGIIALSKNERA
>gnl|CDD|235760 PRK06265, PRK06265, cobalt transporter CbiM
MHIPDGVLPLPVLAGGWVIAAAGVALGLRRLDEERIPLVALLAAAFFVASLIHVPIGPTSVHLVLNGLAG
IVLGWAAFPAILVALLLQALLFGFGGLTVLGVNTLNMALPAVLAGYLFRKLLRRTPPPRGLAAFLAGALA
VFLAALLCALELALSGGFPFVPAAKLLGLAHLPLMVIEGIITAFAVSFLARVRPELLKS
>gnl|CDD|235761 PRK06266, PRK06266, transcription initiation factor E subunit alpha; Validated
IYTMLNNPLVQKVLFEIMEGDEEGFEVLKALIKKGEVTDEEIAEQTGIKLNTVRKILYKLYDARLADYKR
EKDEETNWYTYTWKPELEKLPEIIKKKKMEELKKLKEQLEEEENNMFFFCPNCHIRFTFDEAMEYGFRCP
QCGEMLEEYDNSELIKELKEQIKELEEELKLNPLFSKY
>gnl|CDD|235762 PRK06267, PRK06267, hypothetical protein; Provisional
MNSEEILENSIKAFKLTEKHHGNIVSLERALFLGWYCNLKGPCKFCYMSTQKDKIKDPLKARRRVESILA
EAILMKRIGWKLEFISGGYGYTTEEINDIAEMIAYIQGCKQYLNVGIIDFLNINLNEIEGVVGAVETVNP
KLHREICPGKPLDKIKEMLLKAKDLGLKTGITIILGLGETEDDIEKLLNLIEELDLDRITFYSLNPQKGT
IFENKPSVTTLEYMNWVSSVRLNFPKIKIITGTWVDKLTNIGPLIMSGSNVITKFPLFSMYGTKEGKRVE
NEIRWTGRELYGTFTDLDVLKGKKKLEKTPYVDEKINISSKNLERVENLRPEIDKKIERYVKKTLKNLKK
>gnl|CDD|235763 PRK06270, PRK06270, homoserine dehydrogenase; Provisional
MEMKIALIGFGGVGQGVAELLAEKREYLKKRYGLDLKVVAIADSSGSAIDPDGLDLELALKVKEETGKLA
DYPEGGGEISGLEVIRSVDADVVVEATPTNIETGEPALSHCRKALERGKHVVTSNKGPLALAYKELKELA
KKNGVRFRYEATVGGAMPIINLAKETLAGNDIKSIKGILNGTTNYILTRMEEEGLSYEQALAEAQELGYA
EADPTYDVEGIDAALKVVILANSILGADLTIKDVEVEGITKITPEAIELAAKEGYRIKLIGEVSREKDLS
VSPRLVPLDHPLAVSGTLNAATFETDLAGDVTVVGRGAGSIETASAILSDLIAIHDRYGKA
>gnl|CDD|180501 PRK06271, PRK06271, V-type ATP synthase subunit K; Validated
GAIGAGLAVGIAGLGSGIGAGITGASGAGVVAEDPNKFGTAIVFQALPQTQGLYGFLVAILILFVFKTAP
EWAMLAAGLAVGLAGLSAIGQGIAASAGLGAVAEDDSIFGKAMVFSVLPETQAIYGLLVAILLLVGVFAS
PGVETIAALGAGLAVGFAGLSGIGQGITAAGAIGATARDPDAMGKGLVLAVMPETFAIFGLLIAILIMLG
IMF
>gnl|CDD|235764 PRK06273, PRK06273, ferredoxin; Provisional
LKNLAKIFLSGIYENLERIIFGSDRYTDKEMRNAILTGTVELPKKVFEELCIGCGGCANVCPTKAIEMIP
VEPVKITEGYVKTKIPKIDYEKCVYCLYCHDFCPVFALFNEISPIHPRDVGEDIEVDVSKLLEKPVEISE
EQLSKISQILSINLSKIVKKEKKAN
>gnl|CDD|235765 PRK06274, PRK06274, indolepyruvate oxidoreductase subunit beta
MNFNLIIAGVGGQGVLLASRILANAAMNEGFHVRTAETLGMSQREGSVISHLRFGDEISSPLIPEGQADL
LLALEPAEVARNLHFLKKGGKIIVNAYAIHPATTVGSEKYDPEKEIKFAKEKICDVICIDFTKLADEIGN
PRSLNVIMLGAAFGAGLLPLSKESVLETIEAELPEKLREINLAAFELGIELISLISE
>gnl|CDD|235766 PRK06276, PRK06276, acetolactate synthase large subunit
MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVAT
SGPGATNLVTGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRA
AFEIAKTGRPGPVHIDLPKDVQEGELDLEKYPIPAKIDLPGYKPTTFGHPLQIKKAAELIAEAERPVILA
GGGVIISGASEELIELSELVKIPVCTTLMGKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRF
SDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPIVGDAKNVLRDLLAELMKKEIKNKSEWLERVKKL
KKESIPRMDFDDKPIKPQRVIKELMEVLREIDPSKNTIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGT
MGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGMVYQWQNLYYGKR
QSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEALPMVPPGGNLTNI
LGPYRVEPTVKAQCFSEIKKILNPKV
>gnl|CDD|235767 PRK06277, PRK06277, energy conserving hydrogenase EhbF
MNLLPLMVVFPMICAIIFNLLHGKDKLIKYLTFIVAILLPILPFLASYGYYYFGGHGLVNGYHSGITYLF
NPAKQIIIFVLSLIASLVLITGLGEKKSSGLYVFLMLMGLASVSAIVLADDIFNLYVFFEIAAIVQVGLV
IASGTEEAYKAALKYMILGNVAGSILLLGIGFLLASTGTLNITDIHNALLVNPTSPVIYGGLLLLIFGLL
YGSGLPPFHTIKSDIYAKAKPFGSALLQTFSKFVLVALMLVIFKLFGGLSYFPSAQGVLIALSVLAMVFG
VVMALLQTDYKRLLAYHAISQGGYVAAGLALGTPLGIVAGIFHAINHVIYKSALFLGAGIVSYRTKTSNL
RKLGGLLPVMPVVAFMVLCAKLAISGVPPFNGFQSKLMLAQAAMQANMPELAIIMIIVSIGTFVSMMKAF
YLIYLKPKPEELEYKNKKVPKYAVFSLAVLTILCIILGLFPDLVTNYLYPFANEIGRN
>gnl|CDD|180505 PRK06278, PRK06278, cobyrinic acid a,c-diamide synthase; Validated
MEIGLLDIKGSLPCFENFGNLPTKIIDENNIKEIKDLDGLIIPGGSLVESGSLTDELKKEILNFDGYIIG
ICSGFQILSEKIDIGRKSPVPIIKEGLGLLDVEFSPLICTDRVEFKIEDDSLFTKKNERGTGFHCHTYGN
IEINGDTKILTYSKIQKLNYKMVGEKEILSGVFKGKVFGTMVHNFLDNPFVVENFLKYLKIKEDEKEEIF
KKNKILKEKLKSRSGISTNNKKEERNKPKGIILLATGSESGKTFLTTSIAGKLRGKVFVAKIGPDVRDIV
PSLYLLREKMTKYNSIKIGDRGWSDVEEFLEFVKNSDYDYYIIEGVMGAFTGALNKKNPYSGAEIAKALG
FPVYIVSSCSKSGIEGAFVESMAYYSLLKKMGVKVEGIILNKVYNMEIFEKVKKIAENSNINLIGVGKLK
VEKRGLIPEVEIDYEEFCKAAMEVDENIDIPKIEINAKNPDFRGYTNFEEILDKWS
>gnl|CDD|180506 PRK06279, PRK06279, putative monovalent cation/H+ antiporter subunit E; Reviewed
MRLLYGIGYLIVLIKAIIEAWIDVVKRSLNGKIDPEVIEIETEINRPVGQVLLANSITLTPGTLTIDLDS
EERILKVASISPRSRDDIIPFEPYIKKMFD
>gnl|CDD|235768 PRK06280, PRK06280, hypothetical protein; Provisional
MIDYIIMILALLSAIGALIQKDLIKCAILTGFGGLGLAYLYQLLLAPDVALTEAILGGAILPAFFAFTVR
RTQRIDE
>gnl|CDD|180508 PRK06281, PRK06281, putative monovalent cation/H+ antiporter subunit B; Reviewed
MSTILKIIALPIAIFIMCLGIMTILGGHITPGGGFQGGAMIAAGFILCIVVYGLEKSPFNFSHEFMSIME
SFGALGYVGLGLCGLFFSGSFLYNLGTDLYGLVPQAVSAIFNYPDPTNAGIIPYLNIVVGLKVFVGLSAI
VIAFMEFKKEEEEE
>gnl|CDD|180509 PRK06285, PRK06285, chorismate mutase; Provisional
DSESAEKRLNEIRKRIDEIDEQIIDLIAERTSLAKEIAELKKSLGMPIFDPEREDYIHEKIRKLCEEHNI
DENIGLKIMKILMEHSKELQKEYLER
>gnl|CDD|235769 PRK06286, PRK06286, putative monovalent cation/H+ antiporter subunit G; Reviewed
MMQFVGIIQDILLIIASIGILIASIRLWRVEKDRKNVVYARIHILGVIDIACILILLALGQPLLALTYLI
LAPFLAHAIANAHYNDELKEQ
>gnl|CDD|180511 PRK06287, PRK06287, cobalt transport protein CbiN; Validated
MMDNKKFLIAGLIVALLIAILAPFLASGDPDGLESAAEKIINEKTLEPNLEEAGLEEEGTVAPSPMPDYS
IPGMGKIGEIIAMVIGTLLVLALAYGVGKIFKKKSSE
>gnl|CDD|235770 PRK06288, PRK06288, RNA polymerase sigma factor WhiG; Reviewed
MAKKMSGKIPKYAQQDETELWREYKKTGDPKIREYLILKYSPLVKYVAGRIAVGMPQNVEFDDLVSYGVF
GLIDAIEKFDPEREIKFKTYAVTRIRGAIFDELRSIDWIPRSVRQKARQIERAIAMLEARLGRTPSDEEI
ADELGISLEEYNSLLSKLSGTSVVSLNDLWFGGDEGDEVSLMDTLESPAALNPDEIAEREEIKRVIVEAI
KTLPEREKKVLILYYYEDLTLKEIGKVLGVTESRISQLHTKAVLQLRAKLAEIKKGIL
>gnl|CDD|235771 PRK06289, PRK06289, acetyl-CoA acetyltransferase; Provisional
MSDDVWVLGGYQSDFARNWTKEGRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFFGELFAGQGHLGAM
PATVHPALWGVPASRHEAACASGSVATLAAMADLRAGRYDVALVVGVELMKTVPGDVAAEHLGAAAWTGH
EGQDARFPWPSMFARVADEYDRRYGLDEEHLRAIAEINFANARRNPNAQTRGWAFPDEATNDDDATNPVV
EGRLRRQDCSQVTDGGAGVVLASDAYLRDYADARPIPRIKGWGHRTAPLGLEQKLDRSAGDPYVLPHVRQ
AVLDAYRRAGVGLDDLDGFEVHDCFTPSEYLAIDHIGLTGPGESWKAIENGEIAIGGRLPINPSGGLIGG
GHPVGASGVRMLLDAAKQVTGTAGDYQVEGAKTFGTLNIGGSTTTTVSFVVGT
>gnl|CDD|235772 PRK06290, PRK06290, LL-diaminopimelate aminotransferase
MESYIQNLFAERIGGKNFGKETVIYKFEKIKRAKRAAKEKHPDMELIDMGVGEPDEMADESVVEVLCEEA
KKPENRGYADNGIQEFKEAAARYMEKVFGVKDIDPVTEVIHSIGSKPALAMLPSCFINPGDVTLMTVPGY
PVTGTHTKYYGGEVYNLPLLEENNFLPDLDSIPKDIKEKAKLLYLNYPNNPTGAVATKEFYEEVVDFAKE
NNIIVVQDAAYAALTFDGKPLSFLSVPGAKEVGVEIHSLSKAYNMTGWRLAFVVGNELIVKAFATVKDNN
DSGQFIAIQKAGIYALDHPEITEKIREKYSRRLDKLVKILNEVGFKAEMPGGTFYLYVKAPKGTKSGIKF
ENAEEFSQYLIKEKLISTVPWDDAGHFLRFSVTFEAKDEEEEDRILEEIKRRLSDVEFEF
>gnl|CDD|235773 PRK06291, PRK06291, aspartate kinase; Provisional
MRLVMKFGGTSVGDGERIRHVAKLVKRYRSEGNEVVVVVSAMTGVTDALLEIAEQALDVRDIAKVKDFIA
DLRERHYKAIEEAIKDPDIREEVSKTIDSRIEELEKALVGVSYLGELTPRSRDYILSFGERLSAPILSGA
LRDLGIKSVALTGGEAGIITDSNFGNARPLPKTYERVKERLEPLLKEGVIPVVTGFIGETEEGIITTLGR
GGSDYSAAIIGAALDADEIWIWTDVDGVMTTDPRIVPEARVIPKISYIEAMELSYFGAKVLHPRTIEPAM
EKGIPVRVKNTFNPEFPGTLITSDSESSKRVVKAVTLIKNVALINISGAGMVGVPGTAARIFSALAEEGV
NVIMISQGSSESNISLVVDEADLEKALKALRREFGEGLVRDVTFDKDVCVVAVVGAGMAGTPGVAGRIFS
ALGESGINIKMISQGSSEVNISFVVDEEDGERAVKVLHDEFILGE
>gnl|CDD|235774 PRK06292, PRK06292, dihydrolipoamide dehydrogenase; Validated
MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGI
HADGPKIDFKKVMARVRRERDRFVGGVVEGLEKKPKIDKIKGTARFVDPNTVEVNGERIEAKNIVIATGS
RVPPIPGVWLILGDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDP
EVSKQAQKILSKEFKIKLGAKVTSVEKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGI
ELDERGRPVVDEHTQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQ
IASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDGFVKVYADKKTGRLLGAHIIGPDAEHLIHLLA
WAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFSKLIHG
>gnl|CDD|180517 PRK06293, PRK06293, single-stranded DNA-binding protein; Provisional
MMFGYIVGRLGADPEERMTSKGKRVVVLRLGVKSRVGSKDETVWCRCNIWGNRYDKMLPYLKKGSGVIVA
GEMSPESYVDKDGSPQSSLVVSVDTIKFSPFGRNEGSRQPSAGEDEGQQRGYDNVSIGFEGESLDTESAL
DKDMYAGYGQDQQYASEDVPF
>gnl|CDD|180519 PRK06298, PRK06298, type III secretion system protein; Validated
MGEKTEKATPKRLRDARKKGQVAKSQDFPSAITFIVSMFLTFSLSSFFAKHLGSFLVSIFKTAPTNHDPV
VTVYYLKNCLILILTASLPLLGAVAFVGVLVGFLIVGPTFSTEVFKPDIKKFNPIDNLKQKFKVKTLIEL
LKSILKISGAALILYIVLKNRVPLIIETAGVPPLVTAQIFKEILYKAVTSIGIFFLVVAVLDLVYQRHNF
AKELKMEKFEVKQEFKDTEGNPEIKGRRRQIAQEIAYEDTSSQVKHASAVVSNPKDIAVAIGYMPEKYKA
PWIIAMGINLRAKRIIAEAEKYGVPIMRNVPLAHQLLDEGKELKFIPESTYEAIGEILLYITSLNAQNPN
NKNINQ
>gnl|CDD|235775 PRK06299, rpsA, 30S ribosomal protein S1; Reviewed
KEQDAQNQNDMEESFAELFEESLKESETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEQGEL
EVKVGDEVEVYVERIEDGFGETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLNGVEAF
LPGSQVDVRPVRDTDPLEGKELEFKVIKLDKKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVK
NITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVGDEVKVKVLKFDKEKKRVSLGLKQLGEDPWEAI
EKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHPSKVVSVGQEVEVMVLEIDEEKR
RISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISWDKKGEEAVELYK
KGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLIRA
SELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEKEAIAEYNSASDSKTTLGDLLKA
ALKGK
>gnl|CDD|235776 PRK06300, PRK06300, enoyl-(acyl carrier protein) reductase; Provisional
MLKIDLTGKIAFIAGIGDDQGYGWGIAKALAEAGATILVGTWVPIYKIFSQSLELGKFDASRKLSNGSLL
TFAKIYPMDASFDTPEDVPEEIRENKRYKDLSGYTISEVAEQVKKDFGHIDILVHSLANSPEISKPLLET
SRKGYLAALSTSSYSFVSLLSHFGPIMNPGGSTISLTYLASMRAVPGYGGGMSSAKAALESDTKVLAWEA
GRRWGIRVNTISAGPLASRAGKAIGFIERMVDYYQDWAPLPEPMEAEQVGAAAAFLVSPLASAITGETLY
VDHGANVMGIGPEMFPKDS
>gnl|CDD|180523 PRK06305, PRK06305, DNA polymerase III subunits gamma and tau; Validated
MTSYQVSSRKYRPQTFSEILGQDAVVAVLKNALRFNRAAHAYLFSGIRGTGKTTLARIFAKALNCQNPTE
DQEPCNQCASCKEISSGTSLDVLEIDGASHRGIEDIRQINETVLFTPSKSRYKIYIIDEVHMLTKEAFNS
LLKTLEEPPQHVKFFLATTEIHKIPGTILSRCQKMHLKRIPEETIIDKLALIAKQEGIETSREALLPIAR
AAQGSLRDAESLYDYVVGLFPKSLDPDSVAKALGLLSQDSLYTLDEAITTQNYAQALEPVTDAMNSGVAP
AHFLHDLTLFFRNILLKQYNKQLSSVATKYSSEQLLEIIDFLGESAKHIQLTIFEKTFLETVIIHLIRIY
QRPTLSQLVSQIKSPAFTQLRLESCPPQIKSSNSQQTVSSPQPQPVAKLEQGSLLTAASPQTKKETIHQE
VPSPSLSKSAAIDTLLQFAVVEFSGILTKEP
>gnl|CDD|180524 PRK06309, PRK06309, DNA polymerase III subunit epsilon; Validated
MPALIFYDTETTGTQIDKDRIIEIAAYNGVTSESFQTLVNPEIPIPAEASKIHGITTDEVADAPKFPEAY
QKFIEFCGTDNILVAHNNDAFDFPLLRKECRRHGLEPPTLRTIDSLKWAQKYRPDLPKHNLQYLRQVYGF
EENQAHRALDDVITLHRVFSALVGDLSPQQVYDLLNESCHPRIFKMPFGKYKGKPLSEVPKSYIAWLEKQ
GALDKPENKEIKAAIELLQQLK
>gnl|CDD|180525 PRK06310, PRK06310, DNA polymerase III subunit epsilon; Validated
MSLLKDTEFVCLDCETTGLDVKKDRIIEFAAIRFTFDEVIDSVEFLINPERVVSAESQRIHHISDAMLRD
KPKIAEVFPQIKGFFKEGDYIVGHSVGFDLQVLSQESERIGETFLSKHYYIIDTLRLAKEYGDSPNNSLE
ALAVHFNVPYDGNHRAMKDVEINIKVFKHLCKRFRTLEQLKQILSKPIKMKYMPLGKHKGRLFSEIPLEY
LQWASKMDFDQDLLFSIRSEIKHRKKGTGFSQANNPFLGL
>gnl|CDD|235778 PRK06319, PRK06319, DNA topoisomerase I/SWI domain fusion protein; Validated
MKKSLIIVESPAKIKTLQKLLGEGFIFASSLGHIVDLPAKEFGIDIENDFEPDYQILPDKEEVINKICKL
AKKCDVVYLSPDPDREGEAIAWHIANQLPKNTKIQRISFNAITKGAVTEALKHPREIDMALVNAQQARRL
LDRIVGYKISPILSRKLQRRSGVSAGRVQSVALKLVVDREKAIEAFVPVEYWNIRVHLKDPKTQKTFWAH
LYSVDGKKWEKEIPEGKTEDEVLLINSKEKADHIVELLESATYTVTRVESKEKRRNAYPPFITSTLQQEA
SRHFRFSSSRTMNIAQTLYEGVDLDSEGATGLITYMRTDSVRTDPEALKQVRKYIEGTFGKEFLPSSPNV
YTTKKMAQDAHEAIRPTDITLTPEKLRSKLTEDQYKLYSLIWKRFVASQMIPAIYDTLAIRITTNKGIDL
RATGSLLKFKGFLAVYEEKRDDEGDEEENIHLPKLHEQDVLTKEELSAEQAFTKPLPRFTEASLVKELEK
SGIGRPSTYATIMNKIQSREYTLKENQRLRPTELGKIISQFLETNFPRIMDIGFTALMEDELELIADNKK
PWKLLLQEFWELFLPVVVTAEKEAFIPRIVTEIDCPKCHKGKLVKIWAKNRYFYGCSEYPECDYKTSEEE
LTFNKEDYAEDTPWDSPCPLCGGEMKVRHGRFGTFLGCENYPECRGIINIHKKGEEGIEPEETVPCPAIG
CTGHIVKRRSRFNKMFYSCSEYPACSVIGNSIDAVITKYAGTPKTPYEKKTKAKKKSASTKGKAAKTVKK
KSKAKSKKTTKKRAGPLYTPSPALAAMIGAEPVGRGEATKKVWDYIKEHGLQSPENKKLIIPDSKLQGVI
GPDPIDMFQLSKKLSQHLIK
>gnl|CDD|180528 PRK06321, PRK06321, replicative DNA helicase; Provisional
MATQTKKPQPTQLLSPPNSKESEMIVLGCMLTSVNYLNLAANQLQEDDFYFLEHKIIFRVLQDAFKSDKP
IDVHLAGEELKRRNQLNVIGGPSYLITLAEFAGTSAYIEEYAEIIRSKSILRKMIQTAKEIEKKALEEPK
DVATALDEAQNLLFKISQTTNLAQYVLVADKLKGLTSSKDKPFLLQLQERQEAFQQSAQGDSSPMISGIP
THFIDLDKMINGFSPSNLMILAARPAMGKTALALNIAENFCFQNRLPVGIFSLEMTVDQLIHRIICSRSE
VESKKISVGDLSGRDFQRIVSVVNEMQEHTLLIDDQPGLKITDLRARARRMKESYDIQFLIIDYLQLLSG
SGNLRNSESRQTEISEISRMLKNLARELNIPILCLSQLSRKVEDRANHRPMMSDLRESGSIEQDSDLVMF
LLRREYYDPNDKPGTAELIVAKNRHGSIGSVPLVFEKEFARFRNYAACEFPG
>gnl|CDD|235779 PRK06327, PRK06327, dihydrolipoamide dehydrogenase; Validated
MSKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNPKGKPALGGTCLNVGCIPSKALLASSEEFENA
GHHFADHGIHVDGVKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKTDAGYEIKVTGED
ETVITAKHVIIATGSEPRHLPGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVT
ILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVSVAYTDADGEAQTLEVDKLIVSI
GRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVYAIGDVVRGPMLAHKAEEEGVAVAERIAGQKGH
IDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRALAMGEPDGFVKIIADAKTDEILGV
HVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVDKRPLHF
>gnl|CDD|180530 PRK06328, PRK06328, HrpE/YscL family type III secretion apparatus protein
MKFFSLIYKDQEVAPNKKVLSPEAFSALLDAQELLEKTKEDSEAYTQETHEECEKLREEAKNQGFKEGSK
AWSKQLAFLEEETQKLREQVKEALVPLAIASVKKIIGKELELHPETIVSIIANSLKELTQHKRIIIHVNP
KDLAIVEKSRPELKKIVEYADSLIISPKADVTPGGCIIETEAGIINAQLDVQLAALEKAFSTILKHKNPA
DQSTTDQPQQKKE
>gnl|CDD|235780 PRK06330, PRK06330, transcript cleavage factor/unknown domain fusion protein; Validated
MDYLEKLQVLIENRQPSKFFSLWEEYCFNDVVRGDELVQLLEKIKSSSLAPLFGKIAETVLPLWEQIPEG
EEKDKVLQLVLDLQTTNSKNLLDIALEYVNKKYGGSPNFKEALRVVGLRDGRTFQGSLSRFDLLMHLAKG
NFVFHQGGWGVGEIMGVSFLQQKVLIEFEGVMGAKDISFETAFKSLVPLSKDHFLARRFGDPDGFEAFAK
KNPVEVIECLLKDLGPKTAKEIKDELVDLVIPEADWSRWWQSAKAKIKKDTRIETPDSLKDPYVLRPKGL
SHESQLERSLSGSTDVDKKIQTIYTFVRDLHSELKNEENRKSLIKKLQDLDLEELNSALLLQRALLLSEF
LGEKSSELDCENIASLSEDQIEDIVNNIEIVALQKSFLALIRKCSPVWVPVFMKLLLSTTQPMLRDQVFK
VLNADKESRENLLKKLLALIEQPMLYPELFVWFFLKLGSHEDGLFPPDDKEIERQFLESALILMHKVAST
PQKDLGKKLYSFLVGQRYLVVRQMIEGASLEYLKEFLLLSSKCPQFSSSDLGVLRSLAEVVQPSLKKGTS
EVEEEILWTTSESFTRMKNKLQSLVGKEMVENAKEIEDARALGDLRENSEYKFALEKRARLQEEIRVLSE
EINRARILTKDDVFTDKVGVGCKVVLEDDQGDKVCYTILGPWDADPDNKILSLKSKLAQEMLGKKVGDSV
QFQGKKYKISRIQSIWDE
>gnl|CDD|235781 PRK06333, PRK06333, beta-ketoacyl-ACP synthase
MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDLAEDAEAGFDPDRY
LDPKDQRKMDRFILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLS
PFTIPSFLTNMAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLA
GFAAARALSTRFNDAPEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHM
TAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFGHVSGLAVSSTKSATGH
LLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGLDVVANKARPMDMDYALSNGFGFGGVNASILFR
RWEP
>gnl|CDD|180533 PRK06334, PRK06334, long chain fatty acid--[acyl-carrier-protein] ligase; Validated
MHDNRNTARSKRGKLRSGKTVLESFLKLCSEMTTATVCWDEQLGKLSYNQVRKAVIALATKVSKYPDQHI
GIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHLAQTHGEDAEYPF
SLIYMEEVRKELSFWEKCRIGIYMSIPFEWLMRWFGVSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLA
NQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLGST
PVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVITINTVNSPK
HESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGETWYVTGDLGYV
DRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAADHAGPLVVCGLPGEKVRLCLFTTFPTSIS
EVNDILKNSKTSSILKISYHHQVESIPMLGTGKPDYCSLNALAKSLFGE
>gnl|CDD|235782 PRK06341, PRK06341, single-stranded DNA-binding protein; Provisional
MAGSVNKVILIGNLGADPEIRRTQDGRPIANLRIATSETWRDRNSGERKEKTEWHRVVIFNEGLCKVAEQ
YLKKGAKVYIEGQLQTRKWTDQSGVERYSTEVVLQGFNSTLTMLDGRGEGGGGGGGGDDGGGGDFGSSGP
SRGGPRPASSGGGGNFSRDMDDDIPF
>gnl|CDD|180535 PRK06342, PRK06342, transcription elongation factor GreA
MSVAFTKEESAETAAETLLPDRPISPHPNLVTEAGLKALEDQLAQARAAYEAAQAIEDVNERRRQMARPL
RDLRYLAARRRTAQLMPDPASTDVVAFGSTVTFSRDDGRVQTYRIVGEDEADPKAGSISYVSPVARALMG
KAVGDVVSVGGQELEIIAIA
>gnl|CDD|180536 PRK06347, PRK06347, 1,4-beta-N-acetylmuramoylhydrolase
MQKTRKERILEALQEEKKNKKSKKFKTGATIAGVTAIATSITVPGIEVIVSADETAPADEASKSAEANTT
KEAPATATPENTTEPTVEPKQTETKEQTKTPEEKQPAAKQVEKAPAEPATVSNPDNATSSSTPATYNLLQ
KSALRSGATVQSFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNYNLFGIKGAYNGQSY
TKQTLEDDGKGNYYTITAKFRKYPSYHQSLEDYAQVIRKGPSWNPNYYSKVWKSNTTSYKDATKALTGTY
ATDTAYATKLNDLISRYNLTQYDSGKTTGGNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKV
TVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSKPSTGTSTSKPSTGTSTNAKVYTVVKGDSLWRIA
NNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSKPSTNTNTSKPSTNTNTNAKVYTVAKGDSL
WRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNTAKPSTNKPSNSTVKTYTVKKGDSLWA
ISRQYKTTVDNIKAWNKLTSNMIHVGQKLTIK
>gnl|CDD|180537 PRK06348, PRK06348, pyridoxal phosphate-dependent aminotransferase
MKNKFLAKKYQQMEVNIMAEIATLAKKFPDIIDLSLGDPDLITDESIINAAFEDAKKGHTRYTDSGGDVE
LIEEIIKYYSKNYDLSFKRNEIMATVGACHGMYLALQSILDPGDEVIIHEPYFTPYKDQIEMVGGKPIIL
ETYEEDGFQINVKKLEALITSKTKAIILNSPNNPTGAVFSKETLEEIAKIAIEYDLFIISDEVYDGFSFY
EDFVPMATLAGMPERTITFGSFSKDFAMTGWRIGYVIAPDYIIETAKIINEGICFSAPTISQRAAIYALK
HRDTIVPLIKEEFQKRLEYAYKRIESIPNLSLHPPKGSIYAFINIKKTGLSSVEFCEKLLKEAHVLVIPG
KAFGESGEGYIRLACTVGIEVLEEAFNRIEKMTF
>gnl|CDD|235783 PRK06349, PRK06349, homoserine dehydrogenase; Provisional
MKPLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGVDLPGILLTTDPEELVND
PDIDIVVELMGGIEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIK
ALREGLAANRITRVMGIVNGTTNYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILA
SLAFGTRVDFDDVYVEGISKITAEDIAYAKELGYRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGV
MNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARNLVRVPHLGFQPSALADLPIAPMEEIESKYY
LRLLVADKPGVLAKIAAIFAENGISIESILQKGAGGEGAEIVIVTHETSEAALRAALAAIEALDVVLGIP
SVIRVE
>gnl|CDD|235784 PRK06354, PRK06354, pyruvate kinase; Provisional
MSLRDLMRRTKIVATIGPASESPEKLRQLIEAGATTARLNFSHGDHEEHGARIKNIREASKKLGKTVGIL
QDLQGPKIRLGRFEDGPIELKTGDEFILTSREVLGTQEKFSVTYDGLADEVPVGSRILLDDGLIELEVEE
VDKADGELHCKVLVGGVLSNKKGVNFPGVSLSLPAITEKDREDLIFGLEQGVDWIALSFVRNPSDVLEIR
ELIEEHNGKHIPIIAKIEKQEAIDNIDAILELCDGLMVARGDLGVEIPAEEVPLLQKRLIKKANRLGKPV
ITATQMLDSMQRNPRPTRAEASDVANAILDGTDAVMLSNETAAGDYPVEAVQTMATIAVRIEKDLPYRDI
LSKRPEFTTTITNAISQAVSHIALQLDAAAIVTLTKSGATARNVSKYRPKTPILAVTPNESVARRLQLVW
GVTPLLVLDAPSTDETFDAAINVAQESGLLKQGDLVVITAGTLVGESGSTDLMKVHVVGAVVAKGQGIGR
KSVSGKARVAKTAAEVAKVNEGDILVTPSTDADMIPAIEKAAAIITEEGGLTSHAAVVGLRLGIPVIVGV
KNATSLIKDGQIITVDAARGVVYSGHASVL
>gnl|CDD|180541 PRK06357, PRK06357, hypothetical protein; Provisional
MLFQKEREDLAKVVKTMFDRKETNAAGGNISVRMTAEKNKEYIIMTPTLMSEAKLCDLSPYQILVVDLNT
GEVIEGVGRVTREINMHEAAYVANPKIKCVYHSHAKESMFWATLGLEMPNLTEATQKLGKIPTLPFAPAT
SPELAEIVRKHLIELGDKAVPSAFLLNSHGIVITDTSLHKAYDILETIEWNAYIAYQATVFDKLGLLKLY
HDRELN
>gnl|CDD|180543 PRK06361, PRK06361, histidinol phosphate phosphatase domain-containing protein
THTIFSDGELIPSELVRRARVLGYRAIAITDHADASNLEEILEKLVRAAEELELYWDIEVIPGVELTHVP
PKLIPKLAKKARDLGAEIVVVHGETIVEPVEEGTNLAAIECEDVDILAHPGLITEEEAELAAENGVFLEI
TARKGHSLTNGHVARIAREAGAPLVINTDTHAPSDLITYEFARKVALGAGLTEKELEEALENNPKLLLKR
LG
>gnl|CDD|235785 PRK06365, PRK06365, thiolase domain-containing protein
MITFSDRQLKMKKKSRDVYMVAAGVTKFDKASPYMDFRERVKKAFDYAMNDAGLTLADIDGSVASYFSDH
FQRQLLAGIMVQDYLGLVPKPSKRIEGGGATGGLAFQAGYEEIASGRMDCVAVYGFETMSHVNTWKGNEF
IALASDTNFDYPLGGFYTGYYAMMAVRHMYEFGTTVEQLAKVSVKNHGNAIHNPFAQSPMKITVEDVRKS
PMVSYPLTRLDVCAMSDGAACAILASEDKAFEITDKPVLIKAIGTGSDTLRLADRPFGEVPLLPNESPDD
YKDLRYPGVHSFRAGRMAAKEAYEMAGITDPLNDLDLIELHDAYTSSEIQTYEDLGLCKYGEGGQFIESG
KPELPGKLPVNPSGGLLAAGHAVGATGIMQAVFMFWQLQGRIKKHFHDDYLQVKNAKRGLIHSHAGTGTY
VTVTILEAPK
>gnl|CDD|102340 PRK06366, PRK06366, acetyl-CoA C-acetyltransferase
MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAA
YHAGLPFGVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRWGPKHLLHKN
YKIDDAMLVDGLIDAFYFEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFNDLD
RDEGIRKTTMEDLAKLPPAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDP
LDFVEAPIPATRKLLEKQNKSIDYYDLVEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGS
RIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLEMVE
>gnl|CDD|235786 PRK06369, nac, nascent polypeptide-associated complex protein; Reviewed
GMGGMNPRKMKQMMKQMGIDVEELDVEEVIIRLKDKEIVFENPQVTVMDAQGQKTYQIVGEPEEVEKEAE
KEVEIPEEDIELVAEQTGVSEEEARKALEEANGDLAEAILKLSSE
>gnl|CDD|235787 PRK06370, PRK06370, FAD-containing oxidoreductase
TPAQRYDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEY
GVSVGGPVSVDFKAVMARKRRIRARSRHGSEQWLRGLEGVDVFRGHARFESPNTVRVGGETLRAKRIFIN
TGARAAIPPIPGLDEVGYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPRE
DEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEA
AGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHTAYNDARIVAANLLDGGRRKVSDRIVPYATYT
DPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQGFMKVVVDADTDRILGATILGVHGDEMIH
EILDAMYAGAPYTTLSRAIHIHPTVSELIPTLAQALRRTRLTP
>gnl|CDD|180547 PRK06371, PRK06371, S-methyl-5-thioribose-1-phosphate isomerase
MKVKIDGETKTLKAVWYEDGEVKLIDQRKLPDKIEIFEAKNSDDVAYAIKNMVVRGAPAIGVTAAYGLAM
ASKNGENMDEAVEKIRSTRPTAYDLFKAIRYMNSNEFDMNAARRYAMEIIGRSKKIGEYGNELIKNGARI
LTHCNAGALAVVDWGTALAPIRIAHRNGKNIFVFVDETRPRLQGARLTAWELAQEGIDHAIIADNAAGYF
MRKKEIDLVIVGADRIASNGDFANKIGTYEKAVLAKVNGIPFYVAAPGSTFDFSIKSGDEIPIEERDENE
VLEINGCRIGPQESHARNPAFDVTPNEYVTGFITEYGIFKPNELWKLKS
>gnl|CDD|235788 PRK06372, PRK06372, translation initiation factor IF-2B subunit delta; Provisional
MDVKDLLSDNASGSADVAFKIISFFSHNDIDENIIKDLKNYFFGMGLVRNVCDSIISGPNLRPKNLKLGI
EKHEKMAIEHAKPLFNDSVIGTISSSQVLKAFISSSEKIKSVYILESRPMLEGIDMAKLLVKSGIDVVLL
TDASMCEAVLNVDAVIVGSDSVLYDGGLIHKNGTFPLALCARYLKKPFYSLTISMKIERNFLYSTYPNFK
NHPCSEWNIDIPCINRYFDKTPPDLIDYYINENGFVKPSDVNI
>gnl|CDD|180548 PRK06380, PRK06380, metal-dependent hydrolase; Provisional
MSILIKNAWIVTQNEKREILQGNVYIEGNKIVYVGDVNEEADYIIDATGKVVMPGLINTHAHVGMTASKG
LFDDVDLEEFLMKTFKYDSKRTREGIYNSAKLGMYEMINSGITAFVDLYYSEDIIAKAAEELGIRAFLSW
AVLDEEITTQKGDPLNNAENFIREHRNEELVTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETR
KEVYDHVKRTGERPVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTGGSPPIP
EMLDNGINVTIGTDSNGSNNSLDMFEAMKFSALSVKNERWDASIIKAQEILDFATINAAKALELNAGSIE
VGKLADLVILDARAPNMIPTRKNNIVSNIVYSLNPLNVDHVIVNGKILKENGRLNGFNPDEFIDAEFI
>gnl|CDD|235789 PRK06381, PRK06381, threonine synthase; Validated
MEEELSSSEEKPPGGTPLLRARKLEEELGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGT
CGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANP
GSVNSVVDIEAYSAIAYEIYEALGDVPDAVAVPVGNGTTLAGIYHGFRRLYDRGKTSRMPRMIGVSTSGG
NQIVESFKRGSSEVVDLEVDEIRETAVNEPLVSYRSFDGDNALEAIYDSHGYAFGFSDDEMVKYAELLRR
MEGLNALPASASALAALVKYLKKNGVNDNVVAVITGRRQ
>gnl|CDD|235790 PRK06386, PRK06386, replication factor A; Reviewed
MLSKISDINAARQNVDLKVKVLSLNKRTIKNDRGETIYYYGIIGDETGTVPFTAWEFPDAVKSGDVIEIK
YCYSKEYNGKIRIYFDSRSEVMLKPDENIEVKRTYKLVKIRDLSLVTPYVSVIGKITGITKKEYDSDGTS
KIVYQGYIEDDTARVRISSFGKPLEDNRFVRIENARVSQYNGYIEISVGNKSVIKEVESDINLESRNIFI
FEIKSPVGGITIMGFIVSVGQGSRIFTKCSVCNKIIEDGVCKDHPDAPVYLDIFGYFTISDGTGFVTCYA
NKDSFLPYININENEFARKASSMNPNMLIKKNLLGKCFSVTGDLRKKDDEIDMNVISAKSITADEIKIIE
VEIEEEFQ
>gnl|CDD|235791 PRK06389, PRK06389, argininosuccinate lyase; Provisional
MKIWSGGAGEELENDFYDNIVKDDIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINALIDIYKN
GIEIDLDLEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDKIIEIEKILYEIIKVIPGFN
LKGRLPGYTHFRQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELL
GMEKNIKNPVYSSSLYIKTIENISYLISSLAVDLSRICQDIIIYYENGIITIPDEFTTGSSLMPNKRNPD
YLELFQGIAAESISVLSFIAQSELNKTTGYHRDFQIVKDSTISFINNFERILLGLPDLLYNIKFEITNEK
NIKNSVYATYNAWLAFKNGMDWKSAYAYIGNKIREGEVLDEYQPEDLTDYIDVNELKRINHNIKIIIEPR
EKLIEYAENLIKNI
>gnl|CDD|102354 PRK06392, PRK06392, homoserine dehydrogenase; Provisional
IRISIIGLGNVGLNVLRIIKSRNDDRRNNNGISVVSVSDSKLSYYNERGLDIGKIISYKEKGRLEEIDYE
KIKFDEIFEIKPDVIVDVTPASKDGIREKNLYINAFEHGIDVVTANKSGLANHWHDIMDSASKNRRIIRY
EATVAGGVPLFSLRDYSTLPSRIKNFRGIVSSTINYVIRQEANGRGFLDVVKIAQKMGIAETNYSDDLMG
LDAARKSVILANHLFGKDYTLRDVTYDGIENIDRSSMDNERLVTEVAMINGGPHAESRIRSLSRNDFLGM
IGPLSLGYQMETDINGTINVSDNYDGPYETAGAVVNDVMLLSKYKI
>gnl|CDD|102355 PRK06393, rpoE, DNA-directed RNA polymerase subunit E''; Validated
MKVQYRACKKCKRLTPEKTCPVHGDEKTTTEWFGFLIITEPEGSAIAKRAGITEPGMYAIKVRQ
>gnl|CDD|235793 PRK06394, rpl13p, 50S ribosomal protein L13P; Reviewed
FEAMVVIDAEGQILGRLASYVAKRLLEGEEVVIVNAEKAVITGNRERVIEKYKQRRERGSHYNPYRNGPK
YPRRPDRIFKRTIRGMLPYKKPRGREALKRLKVYVGVPKELEGKEFEVIDEADLSRLSTIKYVTLGEVSK
ELGAKF
>gnl|CDD|135898 PRK06397, PRK06397, V-type ATP synthase subunit H; Validated
MELMRMDDLEEIKIIKEKEESIDKEIANIKNEQENEIKEAKSKYEEKAKKTEEESLNMYNAALMEARKEA
EKKAVEIINKAKQEASLIKLKISEDELRKFVINRVIEYLEE
>gnl|CDD|235794 PRK06398, PRK06398, aldose dehydrogenase; Validated
DLGLKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDVDYFKVDVSNKEQVIKGIDYVISKY
GRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRN
AAAYVTSKHAVLGLTRSIAVDYAPTIRCVAVCPGSIRTPLLEWAAELEVGKDPEHVERKIREWGEMHPMK
RVGKPEEVAYVVAFLASDLASFITGECVTVDGGLRALIPLSTPKIGTK
>gnl|CDD|235795 PRK06402, rpl12p, 50S ribosomal protein L12P; Reviewed
MEYIYAALLLHSAGKEINEDNLKKVLEAAGVEVDEARVKALVAALEDVNIEEAIKKAAAAPVAAAAAAAA
AAAAAAAEEKKEEEEEEEEKEESEEEAAAGLGALFG
>gnl|CDD|102361 PRK06404, PRK06404, anthranilate synthase component I; Reviewed
MLYDNIEEFRDRKNFAYFASFPDRITGYEYLFVSDDYNTDPEGIFDGELRPLIVTYDFVNACFNNKVEKS
GWPYFYSMDPETSYKRNIERKSFKTVKLKGNYNDISLSLKIKELIELIRAGEVLQVVISREFEANIDFKE
KLSEFINNDRSRYVFYYRFGKYRVVGSSPENVFTVNGNIINVDPIAGTYDDKILSNELLNSEKDKLEHRM
LLDLARNDLSKFADIGTLNVDKVMKIEEFSSVKHLVSQVTAKFSNASYRDILASMFPAGTVSGSPKERAI
EIINKYEETPRGPYGGAIGIISKGYTDMALVIRTAYSHGNGFRVRAGAGIVKDSDPEDEVNEIYSKARSV
M
>gnl|CDD|235796 PRK06406, PRK06406, vitamin B12-dependent ribonucleotide reductase
EKMVKEVIKRDGTVVPFDKKKIAMAIYKAMLSVKNGSMEDAEELTDKVVERLKKYERPTVEQIQDIVEKV
LMTKKINGKDFTDVAKSYILYREKRRKIREEKELIGVKDDLKLTLNAIKVLEARYLLKDEDGKIIETPRQ
MFRRVARHIAIVEALYDDEVYDKTGKQKENAEVIGKLSVTQEDMLKRAFRYLKEEGIMKGDFEEFLDFLK
TKWDSIEEYINKFEEVMSNLKFVPNSPTLMNAGTKLGQLSACFVLPVPDSIEGIFNALKYTAMIHKSGGG
TGFSFSRLRPKDDIVASTKGVASGPLSFMRIFDVTTDVIKQGGKRRGANMGILSYHHPDIMEFITSKDSE
NKVLSNFNISVAVTDEFFDKLDNDDYYPLRNPRNGKEVKRIKARQVWDLIITQAWKTGDPGVIFLDEINR
KNPVKNLGEIESTNPCGEQPLLPYESCNLGSINLSKFVENGKIDWDRLRETVHIATRFLDNVIDANKFPV
PQIKEMTRMTRKIGLGVMGFADMLIKLGIPYNSEEALEIAEKVMKFINEESHRASQKLAEERGVFPAWYG
SEWEKKGIKMRNSTTTTIAPTGTISIIAGCSSSIEPLFAIAFVRHVLNGQELLEVNPLFEEITRKRGLYS
EELMRKVAETGNLQNIDVPEDIKRIFVTAHEIDPQWHVLMQATFQRYCDSGVSKTINLRYDATPEDIAKA
YRLAKDLHCKGITVYRDKSKTVQVLYAGTKTTKKEEKEEVKEIELVTKMPDKYLKLDSTFDPACPTGKCD
K
>gnl|CDD|180556 PRK06407, PRK06407, ornithine cyclodeaminase; Provisional
MYYISEDDVLRNLNMKECIGALREAFEEYGAGRANSSTRVRTFSPGHVLNTMPAYMEKYHIAGLKTYIAG
RNGARFVVLLFDVNNPELVAIFEANRLGQIRTGAVTAYATSILHKNVENFTIIGSGFQAETQLEGMASVY
NPKRIRVYSRNFDHARAFAERFSKEFGVDIRPVDNAEAALRDADTITSITNSDTPIFNRKYLGDEYHVNL
AGSNYPNRREAEHSVLNDADIVVTEHMEQSLRESSEISEYVKKGGKPVELKDFAKNNGSYSGLRRTVFKS
MGIGLEDIAAGYLVLKNMGIL
>gnl|CDD|235797 PRK06411, PRK06411, NADH-quinone oxidoreductase subunit NuoB
PLQKDEIVTMGLEEELNKGVVLTTLDDLVNWARKNSLWPLTFGLACCAIEMMAAGTSRYDLDRFGMVFRA
SPRQADLMIVAGTLTNKMAPALRRLYDQMPEPKWVISMGSCANSGGMYHYSYSVVQGVDRIVPVDVYVPG
CPPRPEALLYGILKLQKKIRQSERERKRGERIAVTNLRTPTIA
>gnl|CDD|235798 PRK06416, PRK06416, dihydrolipoamide dehydrogenase; Reviewed
FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFG
IKAENVGIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQTYTAKNIIL
ATGSRPRELPGIEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPG
EDKEISKLAERALKKRGIKIKTGAKAKKVEQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLE
ELGVKTDRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAHKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTH
PEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDGFVKLIFDKKDGEVLGAHMVGARASELIQE
AQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLHA
>gnl|CDD|180559 PRK06418, PRK06418, transcription elongation factor NusA-like protein; Validated
MKIPICEVCVKTGLLCPRCQSLLDSGEVTELDVEVSKVLLKLEEDKELKDVEYKKAYEVDDLVILLVTSG
PRIPIGKGGKIAKALSRKLGKKVRVVEKTNDIKKLAVQLLSPARVLGVNTVWLPDGTVQYVIRVSRRDRR
RLPAKPELLESILSKITGTEVKIRVI
>gnl|CDD|102368 PRK06423, PRK06423, phosphoribosylformylglycinamidine synthase; Provisional
MKFKVEVTYKPGVEDPEALTILKNLNILGYNGIKGVSISKVYYFDADSYNEVDEIAGKILTNPVIHSYKI
ERD
>gnl|CDD|102370 PRK06425, PRK06425, histidinol-phosphate aminotransferase; Validated
MRGHGGDVYEASSKYGRIIDFSANINDFMDIGDISIYPEISYTDIEDQIKIYTQGLKIKVLIGPGLTHFI
YRLLSYINVGNIIIVEPNFNEYKGYAFTHGIRISALPFNLINNNPEILNNYNFDLIFIVSPDNPLGNLIS
RDSLLTISEICRKKGALLFIDEAFIDFVPNRAEEDVLLNRSYGNVIIGRSLTKILGIPSLRIGYIATDDY
NMKISRKITEPWSVCDPAIDFIRSIDLDYVAKHSLDIMENERSYLINNLEAMGFRAAGDPSANFITFMIP
DAHDFYSYLLKNGILVRLLDDYECLGEQYIRIAIRRRSFNIKLVNALRNFLN
>gnl|CDD|180561 PRK06427, PRK06427, bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
MMKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFS
DIRIDAVKIGMLASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPN
LPEAEALTGLPIADTEDEMKAAARALHALGCKAVLIKGGHLLDGEESVDWLFDGEGEERFSAPRIPTKNT
HGTGCTLSAAIAAELAKGASLLDAVQTAKDYVTRAIRHALEIGQGHGPVNHFAYLW
>gnl|CDD|102372 PRK06432, PRK06432, NADH dehydrogenase subunit A; Validated
MLDGYIPLLIIIVVIPLALIFGFKILPALGANRYGDNRISLKTEDILKKAAYEDTPPGSDQSYLEPYESG
EVAREIWGGPSINQYYIVVLLFVVFDVDMLLLFPWAFDFKRLGLIPFIETLIFLAMPLFAVYYAFKMGYM
RWLK
>gnl|CDD|180562 PRK06433, PRK06433, NADH dehydrogenase subunit J; Provisional
MMYETIAFALFALVTVAFSLGVVLSRDVWHSALYLGVALFSVAVLYVMLNAEFLAAVQVLVYVGAVLILI
TFAVMLTKGEEGEESRGA
>gnl|CDD|102374 PRK06434, PRK06434, cystathionine gamma-lyase; Validated
AEKRMLNGFNTRAVQSGELRDPRFGNVTTPIFETSTFVYPNSEKEAYMDSTRGMPYIYTRWGNPTVQAFE
EKYAVLENAEHALSFSSGMGAITSAILSLIKKGKRILSISDLYGQTFYFFNKVLKTLGIHVDYIDTDRLN
SLDFDPSNYDLIYAESITNPTLKVPDIKNVSSFCHENDVIVDATFASPYNQNPLDLGADVVIHSATKYIS
GHSDVVMGVAGTNNKSIFNNLVERRKTLGSNPDPIQAYLALRGLKTLGLRMEKHNKNGMELARFLRDSKK
ISNVYYPDTEIGKKVLRGFGGMLSFELRSMEDVHKFIRNLEIPMVAASLGGVESLITLPVETSHSSLSPE
ERERLGISDNLVRFSIGIEDIDDLIKDIENALSK
>gnl|CDD|235800 PRK06436, PRK06436, 2-hydroxyacid dehydrogenase
MNVYVNFPMSKKLLEICRDILDLDDVHWYPDYYDAEAILIKGRYVPGKKTKMIQSLSAGVDHIDVSGIPE
NVVLCSNAGAYSISVAEHAFALLLAWAKNICENNYNMKNGNFKQSPTKLLYNKSLGILGYGGIGRRVALL
AKAFGMNIYAYTRSYVNDGISSIYMEPEDIMKKSDFVLISLPLTDETRGMINSKMLSLFRKGLAIINVAR
ADVVDKNDMLNFLRNHNDKYYLSDVWWNEPIITETNPDNVILSPHVAGGMSGEIMQPAVALAFENIKNFF
EGKPKNIVRKEEYIVRSERFLGI
>gnl|CDD|135906 PRK06437, PRK06437, hypothetical protein; Provisional
MIAMIRVKGHINKTIEIDHELTVNDIIKDLGLDEEEYVVIVNGSPVLEDHNVKKEDDVLILEVFSGG
>gnl|CDD|102377 PRK06438, PRK06438, hypothetical protein; Provisional
SVKKLVYGIYPRTEELRLEYNRWERGLIPDSEINEKINEEKYIFYDKVKDIGIDEYTDPLFNWYDIFRPI
SLSVNGVSLGPLTRYLETNTFYRIPEISGVKDFNRELDKFQKIDENPPLPLYHLKKGISIFLPSPYSFYK
MSKTLEKIDYNDFYKKLVNIYSRILDIFSIKNVVLLDVFYYKNDNYSYLSDLAKKYNVILITSGNVSKLN
FNGLGHKFESIVRDDEVDYIINKCSYPGIKIFSGDNTKMEDLKARKEISGYDNVLLTHSDYMDFLPREIA
DIKVELLGKAGD
>gnl|CDD|102378 PRK06439, PRK06439, NADH dehydrogenase subunit J; Provisional
MNKYLALIAIILFFIAFAVPVAFMRGTFIPVSQNISRIGTELFNTYIVPFELLSVIIVGAVIGVMYVAWG
EE
>gnl|CDD|235801 PRK06443, PRK06443, chorismate mutase; Validated
MVHFIDMEDLRSEILENTMDIIELIEKRRELARMIGIIKMRNGLSIRDSERENYVKNNLKSDNPLLNMIF
EATIHYQKNISLNINIEVSGDYDSLILSLGLILSRPGIEIYIEDNPDSIEEGCSKAGGHVVIGLPDKDDH
IVDINSGFPVKMEENRMTIFPDLIKTEVRLNSKRVLV
>gnl|CDD|102381 PRK06444, PRK06444, prephenate dehydrogenase; Provisional
MMEIIIGKNGRLGRVLCSILDDNGLGVYIKKADHAFLSVPIDAALNYIESYDNNFVEISSVKWPFKKYSG
KIVSIHPLFGPMSYNDGVHRTVIFINDISRDNYLNEINEMFRGYHFVEMTADEHDLLMSEIMVKPYIISM
ILKDIKSDIKTGSFDKLLEVSEIKEKENWEVFNDTIIYNPYTNVINDLIERLNKVID
>gnl|CDD|180563 PRK06445, PRK06445, acetyl-CoA C-acetyltransferase
LEDVYLVDFARTAFSRFRPKDPQKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWL
YGGRHPIFLARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPHIEPNP
KLLTDPKYIEYDLTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEG
KKKVVDVDQSVRPDTSLEKLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSF
GFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGH
PLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLERV
>gnl|CDD|235802 PRK06446, PRK06446, hypothetical protein; Provisional
MDEELYTLIEFLKKPSISATGEGIEETANYLKDTMEKLGIKANIERTKGHPVVYGEINVGAKKTLLIYNH
YDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKHKLNVNVKFLYEGEEEIGS
PNLEDFIEKNKNKLKADSVIMEGAGLDPKGRPQIVLGVKGLLYVELVLRTGTKDLHSSNAPIVRNPAWDL
VKLLSTLVDGEGRVLIPGFYDDVRELTEEERELLKKYDIDVEELRKALGFKELKYSDREKIAEALLTEPT
CNIDGFYSGYTGKGSKTIVPSRAFAKLDFRLVPNQDPYKIFELLKKHLQKVGFNGEIIVHGFEYPVRTSV
NSKVVKAMIESAKRVYGTEPVVIPNSAGTQPMGLFVYKLGIRDIVSAIGVGGYYSNAHAPNENIRIDDYY
KAIKHTEEFLKLYSTL
>gnl|CDD|180565 PRK06450, PRK06450, threonine synthase; Validated
MVKEVCMKCGKERESIYEIRCKKCGGPFEILIDFEFDKNLERKNFPYIKHFISLGEGRTPLIKKGNIWFK
LDFLNPTGSYKDRGSVTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIE
SYGAEVVRVRGSREDVAKAAENSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWKIPNYVFIPVSAGTLLL
GVYSGFKHLLDSGVISEMPKIVAVQTEQVSPLCAKFKGISYTPPDKVTSIADALVSTRPFLLDYMVKALS
EYGECIVVSDNEIVEAWKELAKKGLLVEYSSATVYAAYKKYSVNDSVLVLTGSGLKVL
>gnl|CDD|235803 PRK06451, PRK06451, NADP-dependent isocitrate dehydrogenase
MQKIPEDGEVIKFENGKWIVPKKPIILYVEGDGIGPEITHAAMKVINKAVEKAYGSDREIKWVEVLAGDK
AEKLTGNRFPKESEELIEKYRVLLKGPLETPIGKGWKSINVAIRLMLDLYANIRPVKYIPGIESPLKNPE
KIDLIIFRENTDDLYRGIEYPYDSEEAKKIRDFLRKELGVEVEDDTGIGIKLISKFKTQRIARMAIKYAI
DHKRKKVTIMHKGNVMKYTEGAFREWAYEVALKEFRDYVVTEEEVTKNYNGVPPSGKVIINDRIADNMFQ
QIIIRPDEYDIILAPNVNGDYISDAAGALVGNIGMLGGANIGDTGGMFEAIHGTAPKYAGKNVANPTGII
KGGELMLRFMGWDKAADLIDKAIMESIKQKKVTQDLARFMGVRALSTTEYTDELISIIDMLS
>gnl|CDD|180567 PRK06452, sdhA, succinate dehydrogenase flavoprotein subunit; Reviewed
MEKIEYDAVVIGGGLAGLMSAHEIASAGFKVAVISKVFPTRSHSAAAEGGIAAYIPGNSDPNDNPDYMTY
DTVKGGDYLVDQDAAELLSNKSGEIVMLLERWGALFNRQPDGRVAVRYFGGQTYPRTRFVGDKTGMALLH
TLFERTSGLNVDFYNEWFSLDLVTDNKKVVGIVAMQMKTLTPFFFKTKAVVLATGGMGMLYRHTTNSYIN
TGDGFGIALRAGAALKDPEFVQFHPTALYPSDVLISEAARGEGGILKNVKGERFMTKYAPKKLDLAPRDI
VSRAIITEIREGRGFPGGYVGLDLTHLGEEYIKERLALAVEAAKSFAGVDAFTEPIPVRPAQHYYMGGID
VDIDGRNPDIVGLFSAGEAACVSVHGANRLGSNSLLDTLVFGQVTGRTVVQFLKSNPGNPTSNYEKEAEK
VVDDAYKFVKSESGVHFGQILEKLRDTMWDYVGIYRDEGGLLNAMSEINKLRGMISNMYVTDKSKVYNTE
FFNALELRNMLDLALVIAKSALERKESRGAHYRTDYPDRDDNNWLKHTIAYLRGNTVEVTFKPVKITRWK
PEPRVY
>gnl|CDD|235804 PRK06455, PRK06455, riboflavin synthase; Provisional
MMKIGIADTTFARVDMGSAAIDELRKLDPSAKIIRYTVPGIKDLPVAAKKLIEEEGCDIVMALGMPGPTE
KDKYCAHEASIGLIMAQLMTNKHIIEVFVHEDEAKDEKELKELAEDRAREHAENLVKLLFKPEKLTKYAG
KGLRQGYPDAGPIRK
>gnl|CDD|180569 PRK06456, PRK06456, acetolactate synthase large subunit
MPTGARILVDSLKREGVKVIFGIPGLSNMQIYDAFVEDLANGELRHVLMRHEQAAAHAADGYARASGVPG
VCTATSGPGTTNLVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIP
QWIKNAFYIATTGRPGPVVIDIPRDIFYEKMEEIKWPEKPLVKGYRDFPTRIDRLALKKAAEILINAERP
IILVGTGVVWSNATPEVLELAELLHIPIVSTFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVV
GARFSDRTFTSYDEMVETRKKFIMVNIDPTDGEKAIKVDVGIYGNAKIILRELIKAITELGQKRDRSAWL
KRVKEYKEYYSQFYYTEENGKLKPWKIMKTIRQALPRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGM
GTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGLVRQVQDLFFG
KRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELALPTLPPGGRL
KQVILRDPRKSS
>gnl|CDD|180570 PRK06457, PRK06457, pyruvate dehydrogenase; Provisional
MPSVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMG
TSGPGSIHLLNGLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIR
RAIREAISKRGVAHINLPVDILRKSSEYKGSKNTEVGKVKYSIDFSRAKELIKESEKPVLLIGGGTRGLG
KEINRFAEKIGAPIIYTLNGKGILPDLDPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLNKSA
KVIQVDIDNSNIGKRLDVDLSYPIPVAEFLNIDIEEKSDKFYEELKGKKEDWLDSISKQENSLDKPMKPQ
RVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAVENKRQVIS
FVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVMGYPEWGVDLYNPDFTKIAESIGFKGF
RLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPMPPKLTFKQAGEYVLSIFREKLEGI
>gnl|CDD|235805 PRK06458, PRK06458, hydrogenase 4 subunit F; Validated
MSYSILFALLLLIPLLASLLLFALRKRRLVATLNVLGITLTLILALWLVFTVPDAGEIFAAGLWFFIDDL
NVFFLALIGVVGFLTSLYSIGYMRHEVEHGELSPVTLRLYYGMYQLFLFTMLLALTSNNLGLMWVAIEAT
TLSSALLVGIYRTRASLEAAWKYIIICSVGVAFALFGTILVYANAATVMGDGEMAILWTELLKHASLLDP
TLMKLAFVFLLIGFGTKVGLFPMHAWLPDAHSEAPSPVSALLSGVLLNVALYAVLRYYILIDAAIGSDFP
GRLLLIFGLLSVLVAAFFLLRQRDIKRLFAYSSIEHMGLIAFALGIGGPLGIFAALLHMLNHSLTKSAIF
FASGNVLQKYGTRDINVIRGLLKVSPLTGWGLMLGALAIAGMPPFGVFISEFLILTAGLARGPLLIAILL
LLLLTLAFAALVRRVAGMVFGEPPEAVNRGDLGWLTTSPMFVHLVLVLVLGLYIPQPLVRWLQQAATIVL
>gnl|CDD|235806 PRK06459, PRK06459, hydrogenase 4 subunit B; Validated
TLLYILPVFLISILLSIFNKKASYILTMISSIILLITSIYEYNGVLSFFSIISTIVWILASLYSIEYDHY
GKWLSSLYILTILGMAIVLTSDNYLLFLAGWEIMTIPSYVAIALTKKNKRPAFVFMAFGELSTVLILAGF
AWAFIISGTTNFSYLPSPVPLILASFGFIIKMGMMPFLVSEWLPIAHGNAPSNFSAILSATMTLMGVYGI
LKMTILTQTIPIGYFGLTILAIGAFSILFGALYAYVSENVKGLLAFSTIENNGAILVALGLYMVTKQLIT
SIEHFSLITVILYSFAHSVAKTGLFLSSGLQEKQSITYSKKIRNRWIELGLTLLASSLSGLLPNIGGVAS
WLLLESLFMFAYVLHNVISILFIVTGAIIAMGEGLATALLIKYITYTSLFRNTKEQLSKIKKYPILLSAL
IVLILGFTLPYLISPFKTSTTILGMLTNSLILSQYYNTTFGGISPLYIILLIVAFSLISYLAFGKPKIRK
AEPWNNGVNEKEEYTSFAMANNIRLMLKKILRTEEEKFLPTYGLDVFWEYMLSLANSYRRFSKIFAKTLM
NSSISWYMIYIILTLIVVIIVVVMG
>gnl|CDD|235807 PRK06460, PRK06460, hypothetical protein; Provisional
MKDATRTVREDIDEATGAITTPIYQTTAYHYPEGEKYRYSREANPTVLELTKKIVELENAEMGVAFSSGM
GAISTTALALLKPGNSVLVHRDMFGRSYRFFTDYLKNWGVNVDASNPGSDNIIEKAKSKRYDVVFVENIT
NPLLRVVDITELSKVCKENGSILIVDATFSTPINQKPLELGADIVVHSASKFLAGHNDVIAGLAAGYGKL
LNVIDQMRRTLGTSLDPHAAYLTLRGIKTLKIRMDVINRNAEQIAEFLEGHPKVVKVYYPGLKSHVDYEI
ARRVLKGFGGVLSFEVNGGQESALKVMKSLKLIIPAQTLGGVNSVISHPATMSHRTLSLEERKIVGITDS
LLRLSVGIEDVNDLIEDLDRALSTLY
>gnl|CDD|180574 PRK06461, PRK06461, single-stranded DNA-binding protein; Reviewed
MEMITKIKDLKPGMERVNVTVRVLEVGEPKVIQTKGGPRTISEAVVGDETGRVKLTLWGEQAGSLKEGEV
VEIENAWTTLYRGKVQLNVGKYGSISESDDEEVPEAEEIPEETPEAPGGGGGFRGGGRR
>gnl|CDD|235808 PRK06462, PRK06462, asparagine synthetase A; Reviewed
KDLERYPKEYEEFLRMSWKHISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLGSD
LPVKQISIDFYGVEYYLADSMILHKQLALRMLGKIFYLSPNFRLEPVDKDTGRHLYEFTQLDIEIEGADL
DEVMDLIEDLIKYLVKELLEEHEDELEFFGRDLPHLKRPFKRITHKEAVEILNEEGCRGIDLEELGSEGE
KSLSEHFEEPFWIIDIPKGSREFYDREDPERPGVLRNYDLLLPEGYGEAVSGGEREYEYEEIVERIREHG
VDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPRVPGIVAL
>gnl|CDD|180576 PRK06463, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
YSMRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREKGVFTIKCDVGNRDQVKKSK
EVVEKEFGRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNA
GIGTAAEGTTFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQEEAEKLRELFRNKT
VLKTTGKPEDIANIVLFLASDDARYITGQVIVADGGRIDNLTHSL
>gnl|CDD|235809 PRK06464, PRK06464, phosphoenolpyruvate synthase; Validated
MKMMKYVLWFEELGMEDVPLVGGKNASLGEMISNLSGAGVPVPPGFATTAEAYRYFLEQTGLNEKIYELL
DGLDVDDVDALAKAGAQIRQLIIDTPFPPDLEQEIREAYAKLSAGYGEASVAVRSSATAEDLPDASFAGQ
QETFLNVRGIDDVLEAVKECFASLFTDRAISYRVHQGFDHFKVALSAGVQKMVRSDLAASGVMFTLDTES
GFRDVVFITASWGLGEMVVQGAVNPDEFYVHKPTLKAGKPAIVRRTLGSKKIKMVYDDGGEHGVKTVDVP
EEERNRFSLTDEEVLELAKQAVIIEKHYGRPMDIEWAKDGDDGKLYIVQARPETVKSRKEANVLERYKLK
GQGKVLVEGRAIGPGIGSGKVRVILDISEMDKVQPGDVLVTDMTDPDWEPVMKRASAIVTNRGGRTCHAA
IIARELGIPAVVGTGNATEVLKDGQEVTVSCAEGDTGYVYEGLLEFEVEEVSLEEMPETPTKIMMNVGNP
ERAFDFAALPNDGVGLARLEFIINNMIGVHPLALLEFDQQDADLKAEIEELTAGYASPEEFYVDKLAEGI
ATVAAAFYPKPVIVRLSDFKSNEYANLIGGERYEPEEENPMLGFRGASRYLSESFREAFALECEAIKRVR
EEMGLTNVEVMIPFVRTVEEAEKVIELLAENGLKRGENGLKVIMMCEIPSNALLAEEFLEYFDGFSIGSN
DLTQLTLGLDRDSGLVAHLFDERNPAVKKLISMAIKAAKKAGKYVGICGQAPSDHPDFAEWLVEEGIDSI
SLNPDAVVDTWLAVAEVEKKIILEA
>gnl|CDD|180578 PRK06466, PRK06466, acetolactate synthase 3 large subunit
MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGV
VLVTSGPGATNAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPE
IIKKAFYIAQSGRPGPVVVDIPKDMTNPAEKFEYEYPKKVKLRSYSPAVRGHSGQIRKAVEMLLAAKRPV
IYSGGGVVLGNASALLTELAHLLNLPVTNTLMGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVG
ARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPIVGPVESVLTEMLAILKEIGEKPDKEALAAW
WKQIDEWRGRHGLFPYDKGDGGIIKPQQVVETLYEVTNGDAYVTSDVGQHQMFAAQYYKFNKPNRWINSG
GLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALGMVRQWQDMQ
YEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAMKDRLVFIDIYVDRSEHVYPMQIAD
GSMRDMWLSKTERT
>gnl|CDD|235810 PRK06473, PRK06473, NADH-quinone oxidoreductase subunit M
MLSALIWIPLLGAILIGFWPSGINGKLARSVALVIASVLLLLSLVLAFQFDPGNPNQQFTEFIPWIDSLG
LSYHLGVDGLSLPLLVLNSLLTLIAIYSSDESIQRPRFYYSLLLLLNAGVSGAFLAQDLLLFFLFYELEL
IPLYLLIAIWGGQRRGYAATKFLLYTAISGILILVSFLGLVWLSGASSFDYEPLRSHTLPLSTQLLLLAP
ILVGFGIKIPLVPFHTWLPDAHVEASTPVSVLLAGVLLKLGTYGLLRFGVGLFPEAWVYLAPWLATWAVV
SVLYGASCAIAQKDMKKMVAYSSIGHMGYILLAAAAATPLSILAAVFQMISHGLISALLFLLVGVVYKKT
GSRDVDVLRGLLNPERGLPITGSLMILGVMASAGIPGMVGFIAEFLVFRGSFPIFPVQTLLCMIGTGLTA
VYFLLLVNRVFFGRLTAELSNLPRVLWSERLPALVLAVLIVVLGIQPSWLVRWTEPTATALLTGQSTVAA
VSPNKAIETS
>gnl|CDD|235811 PRK06474, PRK06474, hypothetical protein; Provisional
MSNKAEILMHPVRMKICQVLMRNKEGLTPLELVKILKDVPQATLYRHLQTMVDSGILHVVKEKKVRSVSE
KYYAINEEDAKIEGSEWTGLSDDEKLNYISYYQLSLLQQYQSYLKSLEEQNSKEDKATFSVVELKLDEEE
FEEFQSELNELMIKYYNSQPKSDEIETRTVAITIIPET
>gnl|CDD|180582 PRK06475, PRK06475, FAD-binding protein
TRGSPLIAGAGVAGLSAALELAARGWAVTIIEKAQELSEVGAGLQLAPNAMRHLERLGVADRLSGTGVTP
KALYLMDGRKARPLLAMQLGDLARKRWHHPYIVCHRADLQSALLDACRNNPGIEIKLGAEMTSQRQTGNS
ITATIIRTNSVETVSAAYLIACDGVWSMLRAKAGFSKARFSGHIAWRTTLAADALPASFLSAMPEHKAVS
AWLGNKAHFIAYPVKGGKFFNFVAITGGENPGEVWSKTGDKAHLKSIYADWNKPVLQILAAIDEWTYWPL
FEMADAQFVGPDRTIFLGDASHAVTPFAAQGAAMAIEDAAALAEALDSDDQSAGLKRFDSVRKERIAAVA
KRGQLNRFAYHATGIFALGRNMLFAIRSPESFLKDLDWLYGYDAANAVRN
>gnl|CDD|235812 PRK06476, PRK06476, pyrroline-5-carboxylate reductase; Reviewed
MKIGFIGTGAITEAMVTGLLTSPADVSEIIVSPRNAQIAARLAERFPKVRIAKDNQAVVDRSDVVFLAVR
PQIAEEVLRALRFRPGQTVISVIAATDRAALLEWIGHDVKLVRAIPLPFVAERKGVTAIYPPDPFVAALF
DALGTAVECDSEEEYDLLAAASALMATYFGILETATGWLEEQGLKRQKARAYLAPLFASLAQDAVRSTKT
DFSALSREFSTKGGLNEQVLNDFSRQGGYAALTDALDRVLRRINGRAS
>gnl|CDD|180584 PRK06481, PRK06481, flavocytochrome c
MKKKLWTTLGMLLLLALILVGCGSNTTSKSDSSSSKESEKTEVTSGASKTSYTDPSELKDKYDIVIVGAG
GAGMSAAIEAKDAGMNPVILEKMPVAGGNTMKASSGMNASETKFQKAQGIADSNDKFYEETLKGGGGTND
KALLRYFVDNSASAIDWLDSMGIKLDNLTITGGMSEKRTHRPHDGSAVGGYLVDGLLKNVQERKIPLFVN
ADVTKITEKDGKVTGVKVKINGKETKTISSKAVVVTTGGFGANKDMIAKYRPDLKGYVTTNQEGSTGDGI
KMIEKLGGTTVDMDQIQIHPTVQQSKSYLIGEAVRGEGAILVNQKGKRFGNELDTRDKVSAAINKLPEKY
AYVVFDSGVKDRVKAIAQYEEKGFVEEGKTIDELAKKINVPAETLTKTLDTWNKAVKNKKDEAFGRTTGM
DNDLSTGPYYAIKIAPGIHYTMGGVKINTNTEVLKKDGSPITGLYAAGEVTGGLHGENRIGGNSVADIII
FGRQAGTQSAEFAKAQ
>gnl|CDD|235813 PRK06482, PRK06482, SDR family oxidoreductase
MSKTWFITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDRLWVLQLDVTDSAAVRAVVDRA
FAALGRIDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQI
AYPGFSLYHATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPARTNFGAGLDRGAPLDAYDDTPVGDLRRAL
ADGSFAIPGDPQKMVQAMIASADQTPAPRRLTLGSDAYASIRAALSERLAALEAQKAVALSTDVDA
>gnl|CDD|180586 PRK06483, PRK06483, dihydromonapterin reductase; Provisional
MPAPILITGAGQRIGLALAWHLLAQGQPVIVSYRTHYPAIDGLRQAGAQCIQADFSTNAGIMAFIDELKQ
HTDGLRAIIHNASDWLAEKPGAPLADVLARMMQIHVNAPYLLNLALEDLLRGHGHAASDIIHITDYVVEK
GSDKHIAYAASKAALDNMTLSFAAKLAPEVKVNSIAPALILFNEGDDAAYRQKALAKSLLKIEPGEEEII
DLVDYLLTSCYVTGRSLPVDGGRHLK
>gnl|CDD|168574 PRK06484, PRK06484, short chain dehydrogenase; Validated
SKAQSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGF
EQLHREFGRIDVLVNNAGVTDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAAIVNVA
SGAGLVALPKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAELERAGKLDPSAVRSRI
PLGRLGRPEEIAEAVFFLASDQASYITGSTLVVDGGWTVYGGSGPASTAQAPSPLAESPRVVAITGGARG
IGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDVLVNN
AGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQGGVIVNLGSIASLLALPPRNAYCASKAA
VTMLSRSLACEWAPAGIRVNTVAPGYIETPAVLALKASGRADFDSIRRRIPLGRLGDPEEVAEAIAFLAS
PAASYVNGATLTVDGGWTAFGDAGDASDPL
>gnl|CDD|235814 PRK06486, PRK06486, aldolase
MAHSLTTDSAPPAGNRPLLDSDAVAQARVDLAACFRAAARHGLEEGICNHFSAVLPGHDDLFLVNPYGYA
FSEITASDLLICDFDGNVLAGRGEPEATAFFIHARIHRAIPRAKAAFHTHMPYATALSLTEGRPLTTLGQ
TALKFYGRTAVDEDYNGLALDAAEGDRIARAMGDADIVFLKNHGVMVCGPRIAEAWDDLYYLERACEVQV
LAMSTGRPLVPVDPAIAAAVARQMREGDRESARLHLEALRRTLDREEPAYRT
>gnl|CDD|180588 PRK06487, PRK06487, 2-hydroxyacid dehydrogenase
MRAVFLDHDSLDLGDLDLSPLEQAFDELQLHDATTPEQVAERLRGAQVAISNKVALDAAALAAAPQLKLI
LVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLALLLALATRLPDYQQAVAAGRWQQSSQFCLLD
FPIVELEGKTLGLLGHGELGGAVARLAEAFGMRVLIGQLPGRPARPDRLPLDELLPQVDALTLHCPLTEH
TRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGAATDVLSVEPPVNGNPLLAPDIPRLI
VTPHSAWGSREARQRIVGQLAENARAFFAGKPLRVVS
>gnl|CDD|235815 PRK06489, PRK06489, hypothetical protein; Provisional
VNRLLLTLLAALLLPLSVSAAAAAAYPAPQEGDWVARDFTFHSGETLPELRLHYTTLGTPHRNADGEIDN
AVLVLHGTGGSGKSFLSPTFAGELFGPGQPLDASKYFIILPDGIGHGKSSKPSDGLRAAFPRYDYDDMVE
AQYRLVTEGLGVKHLRLILGTSMGGMHAWMWGEKYPDFMDALMPMASQPTEMSGRNWMWRRMLIESIRND
PAWNNGNYTTQPPSLKRANPMFAIATSGGTLAYQAQAPTRAAADKLVDERLAAPVTADANDFLYQWDSSR
DYNPSPDLEKIKAPVLAINSADDERNPPETGVMEAALKRVKHGRLVLIPASPETRGHGTTGSAKFWKAYL
AEFLAQVPKR
>gnl|CDD|180590 PRK06490, PRK06490, glutamine amidotransferase; Provisional
PKQARDKRPVLIVLHQERSTPGRVGQLLQERGYPLDIRRPRLGDPLPDTLEDHAGAVIFGGPMSANDPDD
FIRREIDWISVPLKENKPFLGICLGAQMLARHLGARVAPHPDGRVEIGYYPLRPTEAGRALMHWPEMVYH
WHREGFDLPAGAELLATGDDFPNQAFRYGDNAWGLQFHPEVTRAMMHRWVVRGAHRLTLPGAQPRRAHLE
GRLLHDAALRAWLEAFLDHWFAGGPAAAA
>gnl|CDD|180591 PRK06494, PRK06494, enoyl-CoA hydratase; Provisional
MALPFSTVERKGHVTIVTLNRPEVMNALHLDAHFELEEVFDDFAADPEQWVAIVTGAGDKAFSAGNDLKE
QAAGGKRGWPESGFGGLTSRFDLDKPIIAAVNGVAMGGGFELALACDLIVAAENATFALPEPRVGLAALA
GGLHRLPRQIGLKRAMGMILTGRRVTAREGLELGFVNEVVPAGELLAAAERWADDILACSPLSIRASKQA
VYRGLEVSLEEAITAQRDYPAVEARRASQDYIEGPKAFAEKRPPRWKGR
>gnl|CDD|168580 PRK06495, PRK06495, enoyl-CoA hydratase/isomerase family protein
MMMSQLKLEVSDHVAVVTLDNPPVNALSRELRDELIAVFDEISERPDVRVVVLTGAGKVFCAGADLKGRP
DVIKGPGDLRAHNRRTRECFHAIRECAKPVIAAVNGPALGAGLGLVASCDIIVASENAVFGLPEIDVGLA
GGGKHAMRLFGHSLTRRMMLTGYRVPAAELYRRGVIEACLPPEELMPEAMEIAREIASKSPLATRLAKDA
LNTIENMSLRDGYRYEQDITAKLAKTEDAKEAQRAFLEKRPPVFKGR
>gnl|CDD|180592 PRK06498, PRK06498, isocitrate lyase; Provisional
MSTYQSDIDAVAALKEKQGSTWNAINPESAARMRLQNRFKTGLDIAKYTAKIMRADMAAYDADSSKYTQS
LGCWHGFIAQQKMISIKKHFGTTKRRYLYLSGWMVAALRSEFGPLPDQSMHEKTSVPALIEELYTFLRQA
DARELNDLFRELDAAREAGDKAKEAAIQAKIDNFETHVVPIIADIDAGFGNEEATYLLAKKMIEAGACCI
QIENQVSDEKQCGHQDGKVTVPHEDFLAKIRAVRYAFLELGVDDGVIVARTDSLGAGLTQQIAVSQEPGD
LGDQYNSFLDCEEIDAADLGNGDVVIKRDGKLLRPKRLPSGLFQFREGTGEDRCVLDCITSLQNGADLLW
IETEKPHVAQIAGMVNRIREVVPNAKLVYNNSPSFNWTLNFRQQVYDAWKAEGKDVSAYDRAKLMSAEYD
DTELAAEADEKIRTFQADAAREAGIFHHLITLPTYHTAALSTDNLAKGYFGDQGMLGYVAGVQRKEIRQG
IACVKHQNMAGSDIGDDHKEYFAGEAALKAGGKDNTMNQFA
>gnl|CDD|235816 PRK06500, PRK06500, SDR family oxidoreductase
MSRLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKAL
AQALAEAFGRLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLNGSINA
HIGMPNSSVYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGLPEATLDAVAAQIQALVP
LGRFGTPEEIAKAVLYLASDESAFIVGSEIIVDGGMSNL
>gnl|CDD|235817 PRK06501, PRK06501, beta-ketoacyl-ACP synthase
MTAYRDHLGRPIVAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTVDFLPESPFG
ASALSEALARLAAEEALAQAGIGKGDFPGPLFLAAPPVELEWPARFALAAAVGDNDAPSYDRLLRAARGG
RFDALHERFQFGSIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEA
LIRFSLLSALSTQNDPPEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFH
RTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMI
GHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARDARVTAVLSNSFGFGGQNASLVL
TAEPA
>gnl|CDD|180595 PRK06504, PRK06504, acetyl-CoA C-acetyltransferase
MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNA
VLASKLPESVPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLPAKNGLGHYK
SPGMEERYPGIQFSQFTGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGE
MHTVDEGIRFDATLEGIAGVKLIAEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIG
GDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGA
SGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVERL
>gnl|CDD|180596 PRK06505, PRK06505, enoyl-[acyl-carrier-protein] reductase FabI
MEGLMQGKRGLIMGVANDHSIAWGIAKQLAAQGAELAFTYQGEALGKRVKPLAESLGSDFVLPCDVEDIA
SVDAVFEALEKKWGKLDFVVHAIGFSDKNELKGRYADTTRENFSRTMVISCFSFTEIAKRAAKLMPDGGS
MLTLTYGGSTRVMPNYNVMGVAKAALEASVRYLAADYGPQGIRVNAISAGPVRTLAGAGIGDARAIFSYQ
QRNSPLRRTVTIDEVGGSALYLLSDLSSGVTGEIHFVDSGYNIVSMPTLEELKSSDEERGE
>gnl|CDD|180597 PRK06508, PRK06508, acyl carrier protein; Provisional
MSSTFDKVADIIAETSDIPRDTITPESHTIDDLGIDSLDFLDIVFAIDKAFGIKLPLEQWTQEVNEGKVP
TEEYFVLKNLCAKIDELVAAKAA
>gnl|CDD|180598 PRK06512, PRK06512, thiamine phosphate synthase
MTKQKMKPIESRCRIVLVAPPIADGAELAKLLRAALQGGDVASVILPQYGLDEATFQKQAEKLVPVIQEA
GAAALIAGDSRIAGRVKADGLHIEGNLAALAEAIEKHAPKMIVGFGNLRDRHGAMEIGELRPDYLFFGKL
GADNKPEAHPRNLSLAEWWAEMIEIPCIVQAGSDLASAVEVAETGAEFVALERAVFDAHDPPLAVAQANA
LLDEKAPRFED
>gnl|CDD|235818 PRK06518, PRK06518, hypothetical protein; Provisional
QQAAKQEPVLDLQKSLASNNVVIFHGRAQVTSGVTFKLIADGWRKEITRDIRLYGVDTCAPRQKARLGDQ
EWPCGAVATAWLVTKTLNKWLSCRQARMENGVHYAQCFVDGVDIAALGLAEGMAVLSKDDHEDPGPAQYA
SLEEKARKAYRGLWSSTFQMPWDWRRDHGSYNPFDNL
>gnl|CDD|235819 PRK06519, PRK06519, beta-ketoacyl-ACP synthase
MRMQPNDVVITGIGLVSSLGEGLDAHWNALSAGRPQPNVDTETFAPYPVHPLPEIDWSQQIPKRGDQRQM
ETWQRLGTYAAGLALDDAGIKGNEELLSTMDMIVAAGGGERDIAVDTAILNEARKRNDRGVLLNERLMTE
LRPTLFLAQLSNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDM
LLLYELGGLLLKGGWAPVWSRGGEDGGGFILGSGGAFLVLESREHAEARGARPYARISGVESDRARRAPG
DLEASLERLLKPAGGLAAPTAVISGATGAHPATAEEKAALEAALAGPVRGIGTLFGHTMEAQFPLGLALA
ALSVSKGALFPPFDASGEKPMSGAAREAVVTTVGHWRGEGMALVEAAA
>gnl|CDD|180601 PRK06520, PRK06520, 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
MQRTKAPFRADVVGSFLRPAAIKQARQQFAAGEIDAAALRKIEDMEIRKVVEKQRACGLKVVTDGEFRRA
WWHFDFFDGLQGVERYEAEQGIQFNGVQTKARGVRVTGKLDFPDDHPMLEDFRFLKSISGDATPKMTIPS
PSVLHFRGGRKAIDATVYPDLDDYFDDLAKTWRDAIKAFYDAGCRYLQLDDTVWAYLCSDDQRQQIRERG
DDPDELARIYARVLNKALAGKPADLTIGLHVCRGNFRSTWISEGGYEPVAETLFGGVNVDAFFLEYDNER
AGGFEPLRFIPPGHQQVVLGLITTKNGELENADDVKARLAEAAKFVPLEQLCLSPQCGFASTEEGNSLSE
EQQWAKLRLVVEIANEVW
>gnl|CDD|235820 PRK06521, PRK06521, hydrogenase 4 subunit B; Validated
QMLALQLLLLSLLLYLALGLAGLLLLRRPRLAIRLSGPTGLLGGLLGLASGLTALFAGPTLAAVLPLGLP
FLPFHLRLDALSAFFLLVISLLGAAASLYSLGYFREYEGKGPGAMGFFYNLFLASMVLVLLADDAFSFLV
AWETMSLSSWFLVIANHREAEIRRAGFLYLLMAHAGALAILLAFGLLARESGSYDFAAMRAAHLSPFWAS
LVFLLALFGFGAKAGLVPLHVWLPRAHPAAPSHVSALMSGVMLKVAIYGILRVVFDLLGAPGWWWGVLVL
ALGAISAVLGVLYALAEHDLKRLLAYSTIENIGIIFVGLGLAMVFIAYGMPLLAALALTAALYHLLNHAL
FKSLLFLGAGAVLHATGTRDMEKLGGLIRRMPWTAWAFLIGCLAISALPPLNGFVSEWLLLQSLLSSPGL
PQWGLKLAVPIAAAMLALTAALAAMCFVKFYGITFLGRPRSEKAEEAHEVPRWMRAAMLLLAALCVLLGL
LPGWVAPVIDPVAQALVGTPLVTVASGLLLVPVSSSRASYSPLLFLLLLLALALLPLYWLLVRRFRAGRR
RRGPAWACGYPWETAMAQYSAEGFAQPIRRVFAPLFRLRRQLPPPGDLAPARYRARVTDPFWERLYLPIA
RAVQRLAKRVQRLQSGRIRLYLLYVFATLVVLLLVVA
>gnl|CDD|235821 PRK06522, PRK06522, 2-dehydropantoate 2-reductase; Reviewed
MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRLEDGEITVPVLAADDPAELGPQDLV
ILAVKAYQLPAALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRHTGG
GRLKIGEPDGESAAAEALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYR
ALIRALMEEVAAVAEAEGVHLSVEEVREYVRQVIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKH
GIPTPLNDALYGLLKAKESERGLY
>gnl|CDD|180604 PRK06523, PRK06523, short chain dehydrogenase; Provisional
MSFFLELAGKRALVTGGTKGIGAATVARLLEAGARVVTTARSRPDDLPEGVEFVAADLTTAEGCAAVARA
VLERLGGVDILVHVLGGSSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQ
RRLPLPESTTAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALAERLAEAAGTDYEGAKQ
IIMDSLGGIPLGRPAEPEEVAELIAFLASDRAASITGTEYVIDGGTVPTV
>gnl|CDD|180605 PRK06524, PRK06524, biotin carboxylase-like protein; Validated
MIVPAREPEPQPRRVLNGLSDIRAFFHNNTVPLYFISPTPFNLLGIDRWIRNFFYLTYYDSFDGEHPRVF
VPRRRDRRDFDGMEDVCNYLLRHPETLEFIKRRGPGGKACFVMFDEETEALARQAGLEVMHPPAELRHRL
DSKIVTTRLANEAGVPSVPHVLGRVDSYDELSALAHGAGLGDDLVVQTPYGDSGSTTFFVRGQRDWDKYA
GGIVGQPEIKVMKRIRNVEVCIEACVTRHGTVIGPAMTSLVGYPELTPYRGGWCGNDIWPGALPPAQTRK
AREMVRKLGDVLSREGYRGYFEVDLLHDLDADELYLGEVNPRLSGASPMTNLTTEAYADMPLFLFHLLEY
MDVDYELDIEEINSRWERGYGEDEWGQLIMKETSPDVELFTATPRTGIWRMDDDGRVSFARQGNDWATLL
DESEAFYLRVAAPGDYRYEGADLGVLVTRGRLQTDDYRLTERARRWIDGIKAQFASTPLTPAAPIVSRLV
ARA
>gnl|CDD|180606 PRK06525, PRK06525, hydrogenase 4 subunit D; Validated
ENLALLTLLLPFIGALVVFFLPGRRAAELGVLFAALTTLCMLSLAYAFYQAGKVAVTLTLVNLGDVALFG
LVIDPVSVLIGFVVVLLGLLVTLYSTGYMSPGNREHPVHEGTGRYYAFLLLFIGAMAGLVYSSTLLGLLL
FFEITGLCSWALISYYQSPKALRSALKALLITHIGSLGLYLAAATLFLQTGTFALSALSGLHGSLKYLVF
LGILFAAWGKSAQLPFYSWLPDAMEAPTPASAYLHAASMVKVGVYIFARAIQSMGPIPHVIGYVGAVMAI
VTLLYGFLMYLPQQDMKRLLAYSTITQLGYMFFGLSLAILGSRLALEGSIAYIFNHAFAKSLFFLVAGAL
SYSCGTRLLPRLRGVLKKLPLVGVGFCVAALAITGVPPFNGFFSKFPIFAAGFELSVEYWILLPAMVLLL
IESVASFAWFLRWFGRVVFGEPSEAVADAAPLPGSMKLVLIVLIVMSLVSPVIAAPWLQ
>gnl|CDD|180607 PRK06526, PRK06526, transposase; Provisional
VASELAYLTRALKAPTLAGAVERLAERARAESWSHEEFLAACLQREVAARESHGGEGRIRAARFPARKSL
EEFDFDHQRSLKRDTIAHLGTLDFVTGKENVVFLGPPGTGKTHLAIGLGIRACQAGHRVLFATAAQWVAR
LAAAHHAGRLQAELVKLGRYPLLIVDEVGYIPFEPEAANLFFQLVSSRYERASLIVTSNKPFGRWGEVFG
DDVVAAAMIDRLVHHAEVISLKGDSYRLKDRDLGRVPAATKTND
>gnl|CDD|180608 PRK06529, PRK06529, amidase; Provisional
MTYKDATAMAQAVQQGQVTPLELVTQAIYKAKKLNPTLNAIVSERYEEALEEAKQRDFSGKPFAGVPIFL
KDLGQELKGQLSTSGSRLFKNYQATKTDLYVKRLEDLGFIILGRSNTPEFGFKNISDSSLHGPVNLPFDN
SRNAGGSSGGAAALVSSGIVALAAASDGGGSIRIPASFNGLIGLKPSRGRIPVGPGSYRGWQGASVHFAL
TKSVRDTRRLLYYLQMYQMESPFPLATLSKESLFQSLQRPLKIAFYQRSPDGSPVSLDAAKALKQAVTFL
REQGHEVVELEEFPLDMTEVMRSYYIMNSVETAAMFDDIEDALGRPMTKDDMETMTWAIYQSGQDIPAKR
YSQVLQKWDTYSATMASFHETYDLLLTFTTNTPAPKHGQLDPDSKLMANLAQAEIFSSEEQQNLVETMFE
KSLAITPYTALANLTGQPAISLPTYETKEGLPMGVQLIAAKGREDLLLGIAEQFEAAGLLKI
>gnl|CDD|235822 PRK06531, yajC, preprotein translocase subunit YajC; Validated
MGIPTIIMFVVMLGLIFFMQRQQKKQAQERQNQLNAIQKGDEVVTIGGLYGTVDEVDTEAKTIVLDVDGV
YLTFELAAIKRVVPKAETEETSVVNEPAVELKDTASTESAIES
>gnl|CDD|180610 PRK06539, PRK06539, ribonucleoside-diphosphate reductase subunit alpha
MSITVVKRDGSKEPYDANKVNAAIEDAARGLDDAITWVTQLASELEITLFDGITTQQLDEAVIQVALQNV
KDDPAFDTVAARLLLKKIYKRVLGDYDSPEELQDLHANHFRRTIEKGVAEGLLDSRLGGLFDLERLAAAL
DPTRDELLKYIGVVTLNNRYGIRARNGDALEVPQYFWMRIAMGLSLNEDDPTSSALAFYEKMSKLEYLAA
GSTLVNAGTPYPQLSNCFVMEMQDDIEHIAKTTRDVMWLTKGTGGIGLSVSKLRAQGSPIRSNNTTSTGP
IPFMHTIDSVLRAVSRGGKKFGALCFYMENWHMDFPEFLDLRQNSGDPYRRTRTANTAVWISDEFMKRVQ
NDEDWYLFDPLETPDLNELYGKAFSKRYAQYVEQAEAGRIRMFKRITAREQFRAILMSLQTTSHPWLTWK
DTINNRALNNNTGTIHLSNLCTEICLPQDRDNVSVCNLASINLSRHLADGELDWAQLEESTRLAVRQLDN
LIDITASSVKEADFSNQQNRAIGLGVMGFTDMVERLGYSYESEEAYDLIDRIMEHISYAAIDESADLAAE
RGAYPNFEGSRWSRGMVPVDSIALLEADRGVPVDVNRTTRLDWDALRAKVRGGMRNATLMAIAPTASIGL
VAGTTPGLDPQFSQIFSRSTSSGKFLEVNRNLVADLKELGLWETVREEILRSQGDIQEIAAIPDEIKALY
RTSFQLSPYAFLEVAARAQKWVDQAISRNMYLESRDIGDMMDIYTAAWEMGVKTTYYLHMKPRHTAEQST
VKVNKSAERRGGPRRGFAGFGAGVPPAVSADLIPGASCPVDAQAPQQCESCR
>gnl|CDD|235823 PRK06541, PRK06541, aspartate aminotransferase family protein
MMGVDVNSDTDLQALAKRHLWMHFTRHGAYIDAPVPVIVRGEGCYIWDDRGKRYLDGLAGLFVVQVGHGR
AELAEAAAKQAGTLAFFPLWSYAHPPAIELAERLAALAPGDLNRVFFTTGGSEAVESAWKLAKQYFKLTG
KPGKHKVISRAIAYHGTTQGALAITGLPAFKAPFEPLVPGGFRVPNTNFYRAPELGDDPEAFGRWAADRI
EEAIEFEGPDTVAAVFLEPVQNAGGCFPPPPGYFERVREICDRYDVLLVSDEVICAFGRLGEMFGCERFG
YVPDIITCAKGITSGYSPLGAMIASDRLFEPFLDGPTMFLHGYTFGGHPVSAAVALANLDIFEREGLLDH
VRDNEPAFRATLEKLLDLPIVGDVRGDGYFYGIELVKDKATKETFTDDESERLLRGFLSPALFEAGLYCR
ADDRGDPVVQLAPPLISGQEEFDEIEQILRSVLTEAWARL
>gnl|CDD|235824 PRK06545, PRK06545, prephenate dehydrogenase; Validated
RTVLIVGLGLIGGSLALAIKAAGPDVFIIGYDPSAAQLARALGFGVIDELAADLQRAAAEADLIVLAVPV
DATAALLAELADLELKPGVIVTDVGSVKGAILAEAEALLGDLIRFVGGHPMAGSHKSGVAAARADLFENA
PWVLTPDDHTDPDAVAELKDLLSGTGAKFVVLDAEEHDRAVALVSHLPHILASSLAARLAGEHPLALRLA
AGGFRDITRIASSDPGMWRDILESNAEALLDALDEWIEDLDRARDALESGDAEAIAELFDAGKAGRDRLP
GKHGGAIPSFYDLYVDVPDEPGVIARVTAILGEEGISIENLRILEAREDIHGVLQISFKNEEDRERAKAL
LEEFWTYTV
>gnl|CDD|180614 PRK06546, PRK06546, pyruvate dehydrogenase; Provisional
MAKTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVC
AGSCGPGNLHLINGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRV
LHSAIQHAVAGGGVSVVTLPGDIADEPAPEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGA
GVRGAHAEVLALAEKIKAPVGHSLRGKEWIQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFPYDQ
FLPDVRTAQVDIDPEHLGRRTRVDLAVHGDVAETIRALLPLVKEKTDRRFLDRMLKKHARKLEKVVGAYT
RKVEKHTPIHPEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGA
QLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMLVDGLPDFGTDHPPVDYA
AIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTDPNALSIPPTITGEQVKGFALAASKTVLNGG
VGEMVDMARSNLRNIPRP
>gnl|CDD|235825 PRK06547, PRK06547, hypothetical protein; Provisional
MLVALIAARLCGGGMITVLIDGRSGSGKTTLAGALAARTGFQLVHLDDLYPGWHGLAAASEHVAEAVLDE
GRPGRWRWDWANNRPGDWVSVEPGRRLIIEGVGSLTAANVALASLLGEVLTVWLDGPEALRKERALARDP
DYAPHWEMWAAQEERHFARYDPRDVADWLGSD
>gnl|CDD|75628 PRK06548, PRK06548, ribonuclease H; Provisional
MTNNEIIAATDGSSLANPGPSGWAWYVDENTWDSGGWDIATNNIAELTAVRELLIATRHTDRPILILSDS
KYVINSLTKWVYSWKMRKWRKADGKPVLNQEIIQEIDSLMENRNIRMSWVNAHTGHPLNEAADSLARQAA
NNFSTRSAHIPGPGWTERSAK
>gnl|CDD|235826 PRK06549, PRK06549, acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
MLRKFKITIDGKEYLVEMEEIGAPAQAAAPAQPASTPVPVPTEASPQVEAQAPQPAAAAGADAMPSPMPG
TILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITIG
>gnl|CDD|180617 PRK06550, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
QEFMTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKPDLSGNFHFLQLDLSDDLEPLFDWVPSVDI
LCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAY
TASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAADFEPGGLADWVARETPIKRWAEPEEVAELT
LFLASGKADYMQGTIVPIDGGWTLK
>gnl|CDD|180618 PRK06552, PRK06552, keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
MKKSEILTKLKANGVVAVVRGESKEEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVELYKDDPEVLI
GAGTVLDAVTARLAILAGAQFIVSPSFNRETAKICNLYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGST
LGPSFIKAIKGPLPQVNVMVTGGVNLDNVKDWFAAGADAVGIGGELNKLASQGDFDLITEKAKKYMSSLR
KAK
>gnl|CDD|235827 PRK06553, PRK06553, lipid A biosynthesis lauroyl acyltransferase; Provisional
MMFLLKRLKLRLRRALKRFAGWLVAQLVFGLLGLLRLFPADKAINFFGRLARLIGPLLPRHRVALDNLRA
AFPEKSEAEIEAIALGMWDNLGRLGAEYAFLDAIFDYDPEAPEPGRVEVRGIEIFERLRDDGKPALIFTA
HLGNWELLAIAAAAFGLDVTVLFRPPNNPYAARKVLEARRTTMGGLVPSGAGAAFALAGVLERGGHVGML
VDQKFTRGVEVTFFGRPVKTNPLLAKLARQYDCPVHGARCIRLPGGRFRLELTERVELPRDADGQIDVQA
TMQALTDVVEGWVREYPGQWLWLHRRWR
>gnl|CDD|180620 PRK06555, PRK06555, pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Validated
MAVKKVALLTAGGLAPCLSSAVGGLIERYTEIAPEVEIIAYRSGYQGLLLGDSIEITPAVRANAGLLHRY
GGSPIGNSRVKLTNVADCVKRGLVKEGENPLKVAAERLAADGVDILHTIGGDDTNTTAADLAAYLAENGY
DLTVVGLPKTIDNDVVPIRQSLGAWTAAEQGARFFDNVINEHSANPRMLIIHEVMGRNCGWLTAATARAY
REWLDRQEYVPGFGLSAERWDIHAVYLPEMAFDLEAEAERLKAVMDEVGNVNIFLSEGAGLDAIVAEMEA
AGEEVKRDAFGHVKLDTINPGAWFAKQFAELLGAEKVMVQKSGYFARSAPANAEDLRLIKSMVDLAVECA
LRGVSGVIGHDEEQGGKLRAIEFPRIKGGKAFDTSTPWFTELLDEIGQPYGPA
>gnl|CDD|235828 PRK06556, PRK06556, vitamin B12-dependent ribonucleotide reductase; Validated
RRASARARKKARKGLKIERVFTTPGVHPYDEVTWERRDVVITNWRDGKVNFEQRDVEFPKFWSVNATNIV
ASKYFRGAVGTPERENSLKQLIDRVVKTYTDAGREHGYFATEEDAEIFEHELTWLLLHQKFSFNSPVWFN
VGTESPQQVSACFILSVDDSMESILNWYKEEGMLFKGGSGTGTNLSRIRSSKELLSGGGTASGPVSFMRG
ADASAGTIKSGGATRRAAKMVILDVDHPDIEEFIETKAKEEDKIRALRDAGYDMDLGGEAYSSVQYQNAN
NSVRVSDEFMRAVENDGEFGLRARTDGEVIETVDAKELFRKIAEAAWECADPGIQYDDTINDWHTCPESG
RINASNPCSEYMFLDNSSCNLASLNLMKFLRDDGTFDVESFRHAVELVITAMEISICFADFPTEKIARNT
RAFRQLGLGYANLGALLMATGLPYDSDGGRALAAAITSLMTGEAYRRSAELAGVVGPFEGYARNAEPHLR
VMRKHAAANDAIRPLGEVDAALLEAAKEAWDDALELGEKNGYRNAQASVLAPTGTIGFMMDCDTTGIEPD
FALVKYKKLVGGGSMKIVNQTVPRALKKLGYSEEQIEAIVEYIAEHGHIEGAPGLKPEHYAVFDCAMKPA
SGERSISPMGHVRMMAAVQPFLSGAISKTVNMPEDATVEDIEEVYLEGWKLGLKALAIYRDNCKVGQPLN
TSKKEKEDKEAEAAAEAELLAKVKELQKYRPVRRRLPKERPSITHSFSVGGAEGYMTVGSYPDGGLGEVF
IKMAKQGSTLAGLMDAFSTAISIGLQYGVPLEVYVSKFSNMRFEPAGMTDDPDIRIAKSIMDYIFRRLAL
DFLPFEERAELGIFTAEERAAQLETGSYAPASDADLIAEAAASAAPAAPSAAPKEANSEAAPAPKEAHSS
TELLELQLGEAADAPLCPTCGTKMVRNGSCYVCEGCGSTSGCS
>gnl|CDD|235829 PRK06557, PRK06557, L-ribulose-5-phosphate 4-epimerase; Validated
GPEVRAMVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDLDGN
VVEGDLKPSSDTASHLYVYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVGPFALIG
DEAIGKGIVETLKGGRSPAVLMQNHGVFTIGKDAEDAVKAAVMVEEVARTVHIARQLGEPIPIPQEEIDR
LYDRYQNVYGQ
>gnl|CDD|235830 PRK06558, PRK06558, V-type ATP synthase subunit K; Validated
MEHLANFFTQNGGAFFAALGAALAVGLSGIGSAKGVGKAGEAAAGLLTEEPEKFGKALILQLLPGTQGLY
GFVIGFLIWQKITPELSLAQGLAYFAACLPIAIVGLFSAISQGKVAAAGIQILAKRPEEFTKGIILAAMV
ETYAILAFVVSFLLLNGVK
>gnl|CDD|180625 PRK06563, PRK06563, crotonase/enoyl-CoA hydratase family protein
VSRERRGHVLLIGLDRPAKRNAFDSAMLDDLALALGEYEADDELRVAVLFAHGEHFTAGLDLADVAPKLA
AGGFPFPEGGIDPWGTVGRRLSKPLVVAVQGYCLTLGIELMLAADIVVAADNTRFAQLEVQRGILPFGGA
TLRFPQAAGWGNAMRYLLTGDEFDAQEALRLGLVQEVVPPGEQLERAIELAERIARAAPLGVQATLASAR
AAVREGEAAAAAQLPPELRPLFTSEDAKEGVQAFLERRPARFKGR
>gnl|CDD|180626 PRK06565, PRK06565, amidase; Validated
MIEVTEVSIAELRAALESGRTTAVELVKAYLARIDAYDGPATGTALNAVVVRNPDALKEAEASDARRARG
ETLGPLDGIPYTAKDSYLVKGLTAASGSPAFKDLVAQRDAFTIERLRAAGAICLGKTNMPPMANGGMQRG
VYGRAESPYNAAYLTAPFASGSSNGAGTATAASFSAFGLAEETWSSGRGPASNNGLCAYTPSRGVISVRG
NWPLTPTMDVVVPYARTMADLLEVLDVIVADDPDTRGDLWRLQPWVPIPKASEVRPASYLALAAGADALK
GKRFGVPRMYINADPDAGTSENPGIGGPTGQRIHTRPSVIDLWEAARRALEAAGAEVIEVDFPLVSNCEG
DRPGAPTVFNRGLVSPEFLHDELWELSGWAFDDFLRANGDPKLNRLADVDGPQIFPHDPGTLPNREGDLA
AGMDEYVNMAKRGLKSWDQIPTLPDGLRGLEKTRKLDLEDWMDGLGLDAVLFPTVADVGPADADVNPASA
DIAWSNGVWVANGNLAIRHLGVPTVTVPMGVMADIGMPVGLTFAGRAYDDNALLRFAAAFEATGSRRMVP
PRTPPL
>gnl|CDD|235832 PRK06567, PRK06567, putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Validated
MKLGFNLDFNELDLTGLKKLDQIFLDYLFKADKSLHKDLMLFRSTPLSIIPQDYSEFLLKISPHLDDFLA
ELFCISKEITISRLKHKDFDIIYECKRKFVQRVAVKKYPPEKIKDIDFEDVYLKLTDLIGTNFTSREFAK
QIIIWQQAEESFAEELDIAARYAAYRVYLCESIKSHPQDDILFNLPQKLDKENLIDDKKILKYQKNERVD
FDYTDSFLNLDEALNHSHYCIYCHKQDKDSCSKGLLQPQNRHCEERSDVAISGDLTRLPRSLQSLAMTDL
KQGCPLKQKISEMNYVKAQGFNLSALAIIVIDNPMVAATGHRICNDCSKACIYQKQDPVNIPLIESNILE
ETLKLPYGLEIYLLLTRWNPLNIYAPLPKEPTNYNILVTGLGPAGFSLSYYLLRSGHNVTAIDGLKITLL
PFDVHKPIKFWHEYKNLLSERMPRGFGGVAEYGITVRWDKNNLDILRLILERNNNFKYYDGVALDFNITK
EQAFDLGFDHIAFCIGAGQPKVLDIENFEAKGVKTASDFLMTLQSGGAFLKNSNTNMVIRMPIAVIGGGL
TSLDAATESLYYYKKQVEEFAKDYIEKDLTEEDKEIAEEFIAHAKLFKEAKNNEELRKVFNKLGGATVYY
RGRLQDSPAYKLNHEELIYALALGVDFKENMQPLRINVDKYGHVESVEFENRNRHCEQSKTAWQSHEFGL
TRLPRQCYAFPRNDIKTKTVIMAIGIENNTQFDEDKYSYFGDCNPKYSGSVVKALASSKEGYDAINKKLI
NNNPSFKGSYKDFCTQLDYLLTSRVNKINILDDKTFELIIHSPLAAKNFKFGQFFRLQNYSEDAAKLIEP
VALSPIDIDVEKGLISFIVFEVGKSTSLCKTLSENEKVVLMGPTGSPLEIPQNKKIVIVDFEVGNIGLLK
VLKENNNEVIFVTYPDIKIRKLVSVDIVIINASPEIIEELQSLKNEIFGENTEIIVSVNSSMQCMMKGIC
GQCIQKVKGEQKYIFACSQQNQNAEIVDFKSLKTRLRQNSLQEKMRKL
>gnl|CDD|168615 PRK06568, PRK06568, F0F1 ATP synthase subunit B; Validated
MNFLDESFWLAVSFVIFVYLIYRPAKKAILNSLDAKILEVQEKVLKAEKLKEDAALLFEQTNAQIKKLET
LRSQMIEESNEVTKKIIQEKTKEIEEFLEHKKSDAIQLIQNQKSTASKELQDEFCDEVIKLVSEYFQSVK
LSESNIAKNLMDKS
>gnl|CDD|180627 PRK06569, PRK06569, F0F1 ATP synthase subunit B'; Validated
MPQFDIATYYSQIFWLIVTFGLLYIFVYKFITPKAEEIFNNRQTNIQDNITQADTLTIEVEKLNKYYNEE
IDKTNTEIDRLKKEKIDSLESEFLIKKKNLEQDLKNSINQNIEDINLAAKQFRTNKSEAIIKLAVNIIEK
IAGTKADMNLLQNIK
>gnl|CDD|180628 PRK06580, PRK06580, putative monovalent cation/H+ antiporter subunit E; Reviewed
MLMLTKIKFILYFPWLLLEIWKSAFSVIKIIWQRKIGIEPVFEWVDAEGLEEIGEIIYGNSITLTPGTVT
LDINNNMLLVHALNKSSITDLQRGIMIKKIKQI
>gnl|CDD|235833 PRK06581, PRK06581, DNA polymerase III subunit delta'; Validated
IIERLEFNLKHNKLYNSWLIEAENIEQALKDLEKFIYIKLFKNSIPLENNPDYHFIARETSATSNAKNIS
IEQIRKLQDFLSKTSAISGYKVAIIYSAELMNLNAANSCLKILEDAPKNSYIFLITSRAASIISTIRSRC
FKINVRSSILHAYNELYSQFIQPIADNKTLDFINRFTTKDRELWLDFIDNLLLLMNRILKKSANFNIELL
DLENKIFNKLSNRNPSYLLQKFTDIKKLIYNTIDYDLDLKTSYILVVNEFSSN
>gnl|CDD|180630 PRK06582, PRK06582, coproporphyrinogen III oxidase; Provisional
KIQNMRVMANDLSIYIHWPFCLSKCPYCDFNSHVASTIDHNQWLKSYEKEIEYFKDIIQNKYIKSIFFGG
GTPSLMNPVIVEGIINKISNLAIIDNQTEITLETNPTSFETEKFKAFKLAGINRVSIGVQSLKEDDLKKL
GRTHDCMQAIKTIEAANTIFPRVSFDLIYARSGQTLKDWQEELKQAMQLATSHISLYQLTIEKGTPFYKL
FKEGNLILPHSDAAAEMYEWTNHYLESKKYFRYEISNYAKIGQECLHNLTYWNYNSYLGIGPGAHSRIIE
SSSSVSAIMMWHKPEKWLDAVKTKNVGIQTNTKLTHQEIIEEILMMGLRLSKGINISTLEQKLNTKLENI
LDMNNLKHYQALDLIRLDENIYLTDKGLMLHSYIVPRLII
>gnl|CDD|235834 PRK06585, holA, DNA polymerase III subunit delta; Reviewed
MMKIKAHEVDRFLARPDPKIRAVLLYGPDRGLVRERARRLAKSVVPDLDDPFAVVRLDGDDLDADPARLE
DEANAISLFGGRRLIWVRAGSKNLAAALKALLESPPGDAFIVIEAGDLKKGSSLRKLFETAAYAAAIPCY
ADDERDLARLIDDELAEAGLRITPDARALLVALLGGDRLASRNEIEKLALYAHGKGEITLDDVRAVVGDA
SALSLDDAADAALAGDLAAFERALDRALAEGTAPVLILRAALRHFQRLHIVRLKVENGKSAEQAIASLRP
PVFFKRKPDFEKALRRWSLERLLRALERLQAAELDCRRNPALADAIARRVLLSIAVRARRRGR
>gnl|CDD|168619 PRK06588, PRK06588, putative monovalent cation/H+ antiporter subunit D; Reviewed
FIQNTKFTFPLTNFELMFDFHPQNQLIALAFLIVTAILNLYTISQNRKLECLIGSLYCLSSIICVFAADF
ISMIISLEFMTIFACIIIFCDQLKIKPARQYFLTHLFSSGLILIGMTLLIQTTSNTAFTSLTESVNNFEL
PAIFILAGCLINASAIFVNGWVVNCYPIASSSGIVYLISFTTKVTLIIILKLFSGLEILKFFGISMIIYG
LVFSLIEKNLKRLICYLTVSQLGFILAAISINSPNIAYLITSFIFIHILYNGLFALYFAYIEDEYDIKNY
QDLQNTQINFILLIGFVISILIYTSILPISSSYIKDEIANILNENNVMLFSKIATCTVLFGLLMESSTSL
LRRFMSQESRKNIKNKSFIIYLDSCFRRNDIRTITYLSFCIITLCICLFYPIQISHTANFKLVILAISLL
LALIFRKIPRISTENINLDLYQYIEKFIYFSIDKYKETADNNEDAAEYLNFKVIWDNILSKISAWHNQQT
AIFIVLFLLISLILTL
>gnl|CDD|235835 PRK06589, PRK06589, putative monovalent cation/H+ antiporter subunit D; Reviewed
SMILQFTTPNNLLLSTLLVGALNLTSPFATKKDSFIRNFLLITISIFFFGNILLIDLLFLKGIRAQFELM
DFGNYSIGLHLEPLGLIFLLLIGFLWICALLYTPKYLAINNIDSSSRFLFFFNLTILIGVLIALSSDLFT
MFVCYELLTISTAFLIGHTRNNISLSGGYKYLKILMISALLLFLPAVILIYTKTGNLDFVSGGLFSKNQS
IILLLMFIYGIAKTAIFPVHSWLPAAMVAHYPVSALLHAVIVVKTGLFCIYKILLYIFGLSYLQRIFAEF
NWLIFIPIVSIFYSSLKALKTDNIKKILAYSTISQLSLALLSAFILTPKALGAAILHLVSHSFAKICLFY
SMGSIYSLKKEDQVDKLHGTSKSFPLISFIISISSLSLIGIPIFSGFISKFLILLAASEQNQPWLSIIVM
LVVIASSILSALYLLKILSSIYKPSLSENSFITKSLPYLMQISVITCCCALTLFYFIQILIREFLAYIT
>gnl|CDD|235836 PRK06590, PRK06590, NADH:ubiquinone oxidoreductase subunit L; Reviewed
MMNLLWLIVLLPLIGALILGLFGRRIGEKWAHLVGTGLVGLSALLSLVVFFDFLLGGGRAFSQTLWTWIS
VGDFDVDFGLRVDGLSATMLVVVTGVSFLVHIYSIGYMAHDEGYRRFFAYLNLFTFSMLMLVLSDNLLQL
FFGWEGVGLCSYLLIGFWYKKPSAGAAAMKAFIVNRVGDVGLALGIFLLFAEFGSLNYDEVFAAAPQFFG
LGWSALTLICLLLFIGAMGKSAQFPLHTWLPDAMEGPTPVSALIHAATMVTAGVYLVARMSPLFELSPEA
LLFVAIVGAVTALFAAFIGLVQTDIKRVLAYSTMSQLGYMFLALGVGAYAAAIFHLMTHAFFKALLFLGA
GSVIHAMHHEQDIRKMGGLRKKMPVTYATFLIGTLALIGIPPFAGFFSKDEILEAAFANGHINLFVAGLV
GAFLTAFYSFRLIFLVFHGKEKEKIHHPHESPAVMTLPLIVLAVLSVFAGALIVPPFLGVLPLTTELAHG
EAEHHLPVWVALLPLVVALAGIALAWLLYLKKPTLPTSIAAPGRFLYTLLRNKYYFDELYEKVFVKPGLA
LARLLWKDGDDGIIDGLVPNSARLVGGGSRVLRRLQTGYLRHYAASMLIGAVVLLALLLLVGGG
>gnl|CDD|235837 PRK06591, PRK06591, putative monovalent cation/H+ antiporter subunit D; Reviewed
MILANHFPIIQILFPLFGALLIISFRFIEFARIITRICILSSLLVSIYGYSIIQNTELSYTMGGWTSKIG
IEYRLNSLNQAIIVYLNLVLLFFLVFCHKITNQTILKYINNNRKSLFYGILLFAHTGYLGMIATNDFFNL
YVFIEISALSSYVLIASGNNPKSLIGAFDYLIMGSIGATLILIAIGFLLSITGSLNMTDIAAYLQEHTNS
RIITIAIGFFLIGAILKTAFFPMHFWMMRAYNNTASVILVYLAGISTIIGIYIIYKFTYIIIGYETIKTA
ITNFIRPIALATLIIAPYFAYQAKNFKNIIIYSCFTQIGYVFLLYVTENGIIILPSLLLADSINKIALFL
IDAYNESYKREPNKVLIIIAIICSCGLPISPLFFIKVNILELLLTQNLLLDFIIILLSSVGSLFYHYKMV
LLLFPTKQESHS
>gnl|CDD|235838 PRK06596, PRK06596, RNA polymerase factor sigma-32; Reviewed
MTKALQLLALSPEGNLDAYIQAVNKIPMLTAEEEYMLAKRLREHGDLEAAKQLVLSHLRFVVHIARGYRG
YGLPQADLIQEGNIGLMKAVKRFDPEVGVRLVSFAVHWIKAEIHEYILRNWRIVKVATTKAQRKLFFNLR
KAKKRLGWLNPEEVEMVAEELGVSEEEVREMESRLSGQDASLDAPIDDDDEESGAPQDYLEDKSSDPADV
LEEDNWEDQRRALLADALEGLDERSRDIIEARWLDDDKSTLQELAAEYGVSAERVRQIEKNAMKKLKAAI
EAAA
>gnl|CDD|235839 PRK06598, PRK06598, aspartate-semialdehyde dehydrogenase; Reviewed
MKKVGFVGWRGMVGSVLMQRMVEENDFDLIEPVFFSTSQAGGAAPSFGGKEGTLQDAFDIDALKKLDIII
TCQGGDYTNEVYPKLRAAGWQGYWIDAASTLRMKDDAIIILDPVNRDVIDDALANGVKTFVGGNCTVSLM
LMALGGLFKNDLVEWVSVMTYQAASGAGARNMRELLTQMGALHGAVADELADPASAILDIDRKVTELMRS
GDLPTDNFGVPLAGSLIPWIDKDLGNGQSREEWKGQAETNKILGLTKNPIPVDGLCVRVGAMRCHSQALT
IKLKKDVPLAEIEEILAAHNPWVKVVPNDREATMRELTPAAVTGTLTIPVGRLRKLNMGPEYLSAFTVGD
QLLWGAAEPLRRMLRILLK
>gnl|CDD|235840 PRK06599, PRK06599, DNA topoisomerase I; Validated
MAKKLVIVESPAKAKTIKKYLGKDYKVLASFGHVRDLPKKKGGVDPDNDFAPKYEIIEGKEKVVDALKKA
AKKADAVYLATDPDREGEAIAWHIAEVLKEAKLKDKNVKRVVFNEITKKAVQEAIENPRDIDMDLVDAQQ
ARRALDYLVGFKLSPLLWKKVRRGLSAGRVQSVALRLICEREDEIEAFIPQEYWTIEADLATSNGEPFTA
KLVEVNGKKLEKFSITNEEQAKALVKALEGQAYTVDKIEKKERKRNPPPPFITSTLQQEASRKLGFSAKK
TMRIAQKLYEGIDLGEGTVGLITYMRTDSVRLSNEALDEARKYITKKYGKEYLPAKPRVYKKKSKNAQEA
HEAIRPTSINRTPESLKPYLTPDQFKLYELIWKRTVASQMAPAILDQTSVDIASENGKYVFRATGSVILF
PGFLKVYGESKDDEEEDDEKLLPPLKEGEKLKLDELLPEQHFTEPPPRYSEASLVKKLEEYGIGRPSTYA
SIISTLQDREYVELEKKRFIPTDLGRIVNDFLVEHFPKYVDYDFTAGLEDELDEIAEGKKDWKPVLREFW
EPFISNLEKVEEDVRTEKVTQEETDETCPKCGGGPLVLKLGKNGKFLGCSGYPECKYTKNITRDEDEPIE
EEEIVEEEKCPKCGGPLVLKKGRYGKFLACSGYPECKHIKPLEKP
>gnl|CDD|180638 PRK06602, PRK06602, NADH:ubiquinone oxidoreductase subunit A; Validated
MTEVLAHYLPFLIFLIVAIGLGILLLVAGKLLGPRAPDREKNSPYESGFEAFGDARMKFDVRFYLVAILF
VIFDLEAAFLFPWAVSFREIGWLGFVEAMIFILVLLVGLVYLWRKGALDWE
>gnl|CDD|168626 PRK06603, PRK06603, enoyl-[acyl-carrier-protein] reductase FabI
MTTGLLQGKKGLITGIANNMSISWAIAQLAKKHGAELWFTYQSEVLEKRVKPLAEEIGCNFVSELDVTNP
KSISNLFDDIKEKWGSFDFLLHGMAFADKNELKGRYVDTSLENFHNSLHISCYSLLELSRSAEALMHDGG
SIVTLTYYGAEKVIPNYNVMGVAKAALEASVKYLANDMGENNIRVNAISAGPIKTLASSAIGDFSTMLKS
HAATAPLKRNTTQEDVGGAAVYLFSELSKGVTGEIHYVDCGYNIMGSNKL
>gnl|CDD|235841 PRK06606, PRK06606, branched-chain amino acid transaminase
SMADRAGYIWFNGELVPWEDAKVHVLTHALHYGTGVFEGIRAYDTPKGPAIFRLREHTKRLFNSAKILRM
EIPYSVDELMEAQREVVRKNNLKSAYIRPLVFVGDEGLGVRPHGLPTDVAIAAWPWGAYLGEEALEKGIR
VKVSSWTRHAPNSIPTRAKASGNYLNSILAKTEARRNGYDEALLLDVEGYVSEGSGENIFIVRDGVLYTP
PLTSSILEGITRDTVITLAKDLGIEVIERRITRDELYIADEVFFTGTAAEVTPIREVDGRQIGNGKRGPI
TEKLQSAYFDIVRGRTEKYAHWLTPV
>gnl|CDD|235842 PRK06608, PRK06608, serine/threonine dehydratase
NLLLQNPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGK
LPDKIVAYSTGNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKAKEDEEQ
GFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNAN
DAYLSLKNNKIYRLNYSPNTIADGLKTLSVSARTFEYLKKLDDFYLVEEYEIYYWTAWLTHLLKVICEPS
SAINMVAVVNWLKTQSKPQKLLVILSGGNIDPILYNELWKEDYLTIPPKILCSDLISA
>gnl|CDD|168629 PRK06617, PRK06617, 2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
MSNTVILGCGLSGMLTALSFAQKGIKTTIFESKSVKSPEFFKDIRTTALTPHSKNFLFSIDIWEELEKFV
AEMQDIYVVDNKASEILDLRNDADAVLGYVVKNSDFKKILLSKITNNPLITLIDNNQYQEVISHNDYSII
KFDDKQIKCNLLIICDGANSKVRSHYFANEIEKPYQTALTFNIKHEKPHENCAMEHFLPLGPFALLPLKD
QYASSVIWSTSSDQAALIVNLPVEEVRFLTQRNAGNSLGKITIDSEISSFPLKARIANRYFHNRIVLIAD
TAHTVHPLAGQGLNQGIKDIEILSMIVSNNGTLQEYQKLRQEDNFIMYKLTDELNNIFSNYSKNLRCLRQ
IGFKVINNFKPIKNLITSYAMGKR
>gnl|CDD|168630 PRK06620, PRK06620, hypothetical protein; Validated
QQYIFRFTTSSKYHPDEFIVSSSNDQAYNIIKNWQCGFGVNPYKFTLLIKGPSSSGKTYLTKIWQNLSNA
YIIKDIFFNEEILEKYNAFIIEDIENWQEPALLHIFNIINEKQKYLLLTSSDKSRNFTLPDLSSRIKSVL
SILLNSPDDELIKILIFKHFSISSVTISRQIIDFLLVNLPREYSKIIEILENINYFALISKRKITISLVK
EVLN
>gnl|CDD|102471 PRK06628, PRK06628, lipid A biosynthesis lauroyl acyltransferase; Provisional
MKKFLKKLRYLIEYFIVVIFLKVIGIFGVDKAADICSFIARKVGILFAVNKIARRNIKAVFGDMCDVEKI
IDQTWDNFGRFIGEFTYVNKMDEAELERRIEIIGIENIKKLEGQPFLLFSGHFANWDISLKILHKFYPKV
AVIYRKANNPYVNKLVNESRAGDKLRLIPKGPEGSRALVRAIKESESIVMLVDQKMNDGIEVPFLGHPAM
TASAIAKIALQYKYPIIPCQIIRTKGSYFKVIVHPQLKFEQTGDNKADCYNIMLNINQMLGEWVKQNPAQ
WFWFHNRWKK
>gnl|CDD|168631 PRK06630, PRK06630, hypothetical protein; Provisional
MSWIDKFFITFFHKKVGEDEFLNQYYESRNIDYLGRPRRFVIYKNVNEPTKIPPSWHAWLHHLVNEIPKN
IQLFPWQKNNKIVKKLPKTSNLKYNRWQP
>gnl|CDD|168632 PRK06633, PRK06633, acetyl-CoA C-acetyltransferase
MTKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQT
LIHAGIPKEVPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAKFGDIKMV
DLMQYDGLTDVFSGVFMGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTT
SLFDHDETVRPDTSLEILSKLRPAFDKNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYAS
AGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPI
GASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEAV
>gnl|CDD|235843 PRK06635, PRK06635, aspartate kinase; Reviewed
MALIVQKFGGTSVGDVERIKRVAERVKAEVEAGHQVVVVVSAMGGTTDELLDLAKEVSPLPDPRELDMLL
STGEQVSVALLAMALQSLGVKARSFTGWQAGIITDSAHGKARITDIDPSRIREALDEGDVVVVAGFQGVD
EDGEITTLGRGGSDTTAVALAAALKADECEIYTDVDGVYTTDPRIVPKARKLDKISYEEMLELASLGAKV
LHPRSVEYAKKYNVPLRVRSSFSDNPGTLITGEEEEIMEQPVVTGIAFDKDEAKVTVVGVPDKPGIAAQI
FGALAEANINVDMIVQNVSEDGKTDITFTVPRDDLEKALELLEEVKDEIGAESVTYDDDIAKVSVVGVGM
RSHPGVAAKMFEALAEEGINIQMISTSEIKISVLIDEKYLELAVRALHEAFGLD
>gnl|CDD|235844 PRK06638, PRK06638, NADH-quinone oxidoreductase subunit J
MTGEAIAFYILALLAVLAALGVVTSRNPVHSALFLILTFLSIAGLYFLLGAEFLGVVQIIVYVGAVMVLF
LFVVMMLDVDFSEREQLREWLPGGVLIGLVILLGLLLLLIVGAIIAASGVNAQGIAAGEGNTKAIGILLF
TDYLLPFELASVLLLVAMVGAIVLARRERARVKRQDVPAQLPDGREDALSVVKVEEGK
>gnl|CDD|135984 PRK06642, PRK06642, single-stranded DNA-binding protein; Provisional
MAGSLNKVILIGNVGRDPEIRTTGEGKKIINLSLATTETWKDRITSERKERTEWHRVVIFSEGLVSVVER
YVTKGSKLYIEGSLQTRKWNDNSGQEKYTTEVVLQNFNSQLILLDSKNSNNHNQDSGHSEYKHPETKNHS
FDHSDLDDEIPF
>gnl|CDD|180643 PRK06645, PRK06645, DNA polymerase III subunits gamma and tau; Validated
DINSSNQYIPFARKYRPSNFAELQGQEVLVKVLSYTILNDRLAGGYLLTGIRGVGKTTSARIIAKAVNCS
ALITENTTIKTCEQCTNCISFNNHNHPDIIEIDAASKTSVDDIRRIIESAEYKPLQGKHKIFIIDEVHML
SKGAFNALLKTLEEPPPHIIFIFATTEVQKIPATIISRCQRYDLRRLSFEEIFKLLEYITKQENLKTDIE
ALRIIAYKSEGSARDAVSILDQAASMSAKSDNIISPQVINQMLGLVDSSVIIEFVEYIIHRETEKAINLI
NKLYGSSVNLEIFIESVSDFIAYLNKVKMLPNYSLPIYESFNDRTKSILDKISLPHLSILWQIYNKGVGE
IKISYNQLTETEMLVIKSIYSTSLPLLTDFDGNNQNLNQSINPEIKKKFEIVDFLEYLYKNNEIDIYYFL
LNHTELKNLSDNRLEFVSLEVTSKIKKQIEDLLAAFTNEKFEIIIIKEQNKQTLKNQLIGKIEASNDFGL
IKKHFPNVKISDILLKS
>gnl|CDD|102480 PRK06646, PRK06646, DNA polymerase III subunit chi; Provisional
MQQFSIYQTSDELLLKSILLLIEKCYYSDLKSVILTADADQQEMLNKNLWTYSRKQFIPHGSKLDPQPEK
QPIYITDELQNPNNASVLVIISPTDIGKILQAKEYIRVFKRIIIITDLPEDLKELTVKINKFTGQENKID
CFTQNPRGAWNKVV
>gnl|CDD|235845 PRK06647, PRK06647, DNA polymerase III subunits gamma and tau; Validated
MSYRGTATKRRPRDFNSLEGQDFVVETLKHSIESNKIANAYIFSGPRGVGKTSSARAFARCLNCVNGPTP
MPCGECSSCKSIDNDNSLDVIEIDGASNTSVQDVRQIKEEIMFPPASSRYRVYIIDEVHMLSNSAFNALL
KTIEEPPPYIVFIFATTEVHKLPATIKSRCQHFNFRLLSLEKIYNMLKKVCLEDQIKYEDEALKWIAYKS
TGSVRDAYTLFDQVVSFSDSDITLEQIRSKMGLTGDEFLEKLASSILNEDAKELLCVLDSVFLSGVSVEQ
FLLDCIEFFRELLFLKHGIKNEAFIGIKAERLPEKLREFDLSQIERAISVLLETYRDLQFSVNPRYELEI
NFSKILRLKDYVPNHELIKQIQDLESKLLEHAAPDSCNFDVGSDNESTDDLSPIPIDPPLKAELPEIRSL
EPDESTKEDEPLKTKIDSDMLSTESWDDEIDEIFIEVRDNFDRSNDNEEIKESFIYVVSKYVQTLVYSGE
VLIDGEVLYYKIFSGFEYNQLQAYKNEIRDEFLKEFPALSLIFQKQFKDLEDDFDAKVRTVKNIFGASEV
KEK
>gnl|CDD|180645 PRK06649, PRK06649, V-type ATP synthase subunit K; Validated
MDIGLIGAAAALGISAIGSALGMGAAGMAAIGAWKRCYMQGKPAPFLLIVFVGAPLTQTIYGYILMNTLL
GVMSQTNPWLLLGAGIGGGLAIAASAFAQGKAAAGACDALAETGKGFANYLLVLGLIETVALFVMVFLMI
FKF
>gnl|CDD|235846 PRK06654, fliL, flagellar basal body-associated protein FliL; Reviewed
MAEKDDIGDENIDVGDAPDGRKVGLLPDVIIKILQWVAIGLFAVIFIVTVVYFVSKMVVSQSGAPNAFPV
FSNEYLEKRPMLQWYESIGEIRGNTADTPPKTFVVKLALGYAENNKNILNELGRRKVRLKDIIREYFSQK
TGQELKNESQIKAEIKARINSILRNGEIKDIAFTQIDIFDM
>gnl|CDD|235847 PRK06655, flgD, flagellar hook assembly protein FlgD
MSIANTVGSSSTSGLSTTSSSSSSKKGAADLQDDFLTLLVAQLKNQDPLNPMDNSQMTSQLAQFSTVSGI
EKLNTTLGSLSSQMTSSQALQASSLVGRGVLVPGDTVLVGTGGTTPFGVELPSAADNVTVTITDSAGQVV
RTIDLGAQSAGVVSFTWDGTDTDGNALPDGNYTIKASASVGGKQLVAQTLTYANVQSVSLGANGGGLDLN
LAGTGVTLSDVRQIL
>gnl|CDD|168637 PRK06661, PRK06661, hypothetical protein; Provisional
MDIKYNLAAAYRIMAYLSLDDHTYTHLSARPKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILEGEEYQ
YNKTGYFIHGSIYKTRPDISAIFHYHTPASIAVSALKCGLLPISQWALHFYDRISYHNYNSLALDADKQS
SRLVNDLKQNYVMLLRNHGAITCGKTIHEAMFYTYHLEQACKTQCLLNSTKKQELIIPSVEICKKTVKDL
LSFEEDLGKRDWAAWLRLIKM
>gnl|CDD|180648 PRK06663, PRK06663, flagellar hook-associated protein 3
IMRVSHPMQYNNLKSSLRRQESKMTKLQNQLSTGQRIQKLRDDPTAATHSIRYKSRLFKLDRYQKNIDDG
KDRLRYAEGYLQSITNILQRARELAVQGANGTYQADDKKKIAKEIDELLEDLVDIANARGADGYSIFSGT
KIDTEPFEVIRGNIKGLQGDAGSNQIIGVEYNGDIGEQNREIENGIYIPVNYPGNKVFWGTNQSIISSVD
ASGYVVKEDQKIYIDGVEIHLSAGDTIDDIIAKINDSSAPVKASLDPVLNSISLKTTTPHQIWLEDEEGG
TVLQDLGLITNATKEPPYNYSNSAEVSGRSIFDSLIQLRDALLNNDQELIGGRALGEIDEALDNLLTTLA
DLGAKENRLDRSYARISKEKLDMTEALSKNEDIDVTEAITNLNMLELAHQASLGVSGKIMQPTLLDFLR
>gnl|CDD|235848 PRK06664, fliD, flagellar hook-associated protein FliD; Validated
MSDFTIPGVNSGYNTNEIVKSLMKLERIPIDRSEQKLESLKQQKDAWQDINRKITDLRSKARALYSFNNP
FAEKSANSSNEGVLTGDASRGAKNGNHKLEIKQIASSDQFLSDNFPKDIQIPEGTYTFLVGKKEISVKFS
GGDIRDLVSAINNRGKGFLSASIVKSDGDGNSLTLTSLKTGKENKLKFEDEALGLAKQIGLVGELKTNFP
PNEQPIVYGQSSSTNKLFFTENGIVLEPLSEQSIDIPETIEIKKRSKIEFEVSYEDASEEEIENKIVFNP
GEATFEGAKVENEDSQVDLESDLKLPKEKKYIQMNMLKIESKEGHSLKLPPINASDNFEKVELPLGELSD
LKALNIENNANNKAIVIRNIEIFDPKARGGALPVNAKSEAKDAKIKFDGVEVERDKNEITDLIPGVTLNL
HKASEDPVTLKIEPDYEKIKNLIIEFVAAYNEVLAEINIVTSNEKSSIIEELTYLSDEEKEEAYKNLGLL
RGEFTLLRLKSRLKTIISSSYPTSDDNAFRMLNQIGISTNSVGSSGGLIQDGYLELDEKKLDEVLKENPD
SVRELFAFDSNGDAVMDNGVAKMLLEYLSPYTQAGGIIYNKVKGLDERIADNNKKIEEYEKKLESKERKL
KGKYLTMDQTVKKMKEQSNYLKNFNKSGRNR
>gnl|CDD|180650 PRK06665, flgK, flagellar hook-associated protein FlgK; Validated
MDSTFSGIEIGKRSLFAHKQALQTTGHNISNASTKGYSRQRVTMKTFDPLYAPSLNRAEKPGQIGQGVEI
QSIERIRDELLDSRIIEESGRLGYWKTKDKYLSQLEQVYNEPEDQSLRTRLDDFWDSWQDLSNYPEGLAE
RQVVLERAQSLGERIHDRYRSLERIRDMANDEIEITVEEINNILRNIADLNEQIVKSQAMGDNPNDLLDR
RDLLVDKLSSLIDVSIERSDPDEFMIHIGGRHLVQGNIANELDLEANPPNEGYWDILWSANGDPALLRTG
KLGALIELRDTDIRDEINELDTLAINIVDLVNEIHRSGFGLNGKTGRDFFTQEYKLTNTRGNYDSNGDGQ
FDSTHIFRVNGTNSIDPDEKIGISGTLRFQASNKNGTVEIPYNATDTVNDVIKRINNSNAQVTAYLNHNN
KLVLKATKADDDENPDFVIRHIEDSGDFLVGYTGILNASGPEGAYDYQRIDTINKLQGNGADYTVSPLKH
PASWIKVNDIIRNDPSNIAAGIGDPTNPNGIGDGRAALAIASLRNSPVMVGKSKTFDDFFANTISNIGIK
GETAEIEKESQNQIMKELEDLRQSVSGVNLDEELANMIEFQHGYNASARFISVSNELLDTIINRMGV
>gnl|CDD|235849 PRK06666, fliM, flagellar motor switch protein FliM; Validated
MMDDILSQEEIDALLSGVSDGEVDDEELKEEGDEKKVRPYDFKRQERFSRERLRSLEIINERFARLLRIG
LSNLLRRSVEISVGSVDQQPYGEFIRSLPVPTSLNLVHMKPLRGTALIEFDPSLVFIMVDNLFGGDGRFH
TKVGREFTETEQRIIDRILKLAFENLKEAWSSVVPIEPEYVRSEVNPQFANIVSPNEIVVVVSFHIEIGG
GGGMMNICIPYSMIEPIREKLSSPYWMSDSRDKDKRWRKELEQQVQQAEVELVAELGEIKLTLSEILNLK
VGDVIPLEKPADDPLIVYVDGKPKFLCQYGKSNGRKALQIEELIERELNEKNEELEK
>gnl|CDD|180652 PRK06667, motB, flagellar motor protein MotB; Validated
MAMRKKKCPKCIQGAPEYMLTYGDMVTLLLCFFVMLFTTNDVDENVLQIISASFTGTGFFKGGQTLSKGK
LSELGNSIMSLPSTEKGKQLSQAKKNASSLFKPEIQSNKVAVTEDERGLVISLASDAFFYPGSAEVKLEE
NRETLQKIASFIGFLDLAGRNFRIEGHTDNVDVNPEGPWKSNWELSGARAVNMLEYILNYGDQSESWFQV
SGFAGSRPLATEDTPEGRAYNRRIDIVILTDASLSRSKGIKQ
>gnl|CDD|235850 PRK06669, fliH, flagellar assembly protein H; Validated
MPKVIFKRSNVINKEKLKTHEIQKYRFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFE
IVEAAEEEAKEELLKKTDEASSIIEKLQMQIEREQEEWEEELERLIEEAKAEGYEEGYEKGREEGLEEVR
ELIEQLNKIIEKLIKKREEILESSEEEIVELALDIAKKVIKEISENSKEIALALVKELLKEVKDATDITI
RVNPEDYEYVKEQKDELISLLDNEEHLKIYEDDAISKGGCVIETDFGNIDARIDTQLKQLKEKLLENLKI
G
>gnl|CDD|180654 PRK06672, PRK06672, hypothetical protein; Validated
MKINWTEVKEKIRPQISKPSYETWFTNTTVYLEDDILTIYCPNEFARDWLESHYKELVFNTLREMFNTTF
EIQFDLCNGEPSNLKDVQKEKLSSWDEVKKALRPKIAEKTFMTWIRNTNATIKDNKVIIFCEDAFHRDLL
EGEYKNIISSTVQKITDEEYQIWFEIGSSATSKAQVHHVKNNQRTSGQEESKTIWNKIKDKMQLKISRPS
YETWVKETTARINEDSLIIYFENEFQQEWVKKSYKDLISQIAKELTGNTYEIQFELKSNTTSNNEKSTIK
DITSELGEQFKVSNNSLKYNDVDESNKRIRALEEKIMNLEKVIGTLVEKLDAVELKTQLEK
>gnl|CDD|235851 PRK06676, rpsA, 30S ribosomal protein S1; Reviewed
MMEEFEESLNSVKEVEVGDVVTGEVLKVEDKQVFVNIEGYKVEGVIPISELSNDHIEDINDVVKVGDELE
VYVLKVEDGEGNLLLSKRRLEAEKAWDKLEEKFEEGEVVEVKVTEVVKGGLVVDVEGVRGFIPASLISTR
FVEDFSDFKGKTLEVKIIELDPEKNRVILSRRAVVEEERAAKKEELLSSLKEGDVVEGTVARLTDFGAFV
DIGGVDGLVHISELSHERVEKPSEVVSVGQEVEVKVLSIDWETERISLSLKDTLPGPWEGVEEKLPEGDV
IEGTVKRLTDFGAFVEVLPGVEGLVHISQISHKHIATPSEVLEEGQEVKVKVLEVNEEEKRISLSIKALE
EAPAEEEDRREEYRQYELPEEETGFSLGDLIGDKLKKLKL
>gnl|CDD|180656 PRK06680, PRK06680, D-amino acid aminotransferase; Reviewed
MKRIAYVNGRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAE
LVEVLRELIRRNRVREGLVYLQVTRGVARRDHVFPAADVKPSVVVFAKSVDFARPAAAAETGIKVITVPD
NRWKRCDIKSVGLLPNVLAKQAAKEAGAQEAWMVDDGFVTEGASSNAWIVTKDGKLVTRPADNFILPGIT
RHTLIDLAKELGLEVEERPFTLQEAYAAREAFITAASSFVFPVVQIDGKQIGNGKPGPIAKRLREAYEEF
ARLTAV
>gnl|CDD|136002 PRK06683, PRK06683, hypothetical protein; Provisional
MSYQKVSNAENVVVGHKRTLEAIKNGIVKEVVIAEDADMRLTHVIIRTALQHNIPITKVESVRKLGKVAG
IQVGASAIGIIS
>gnl|CDD|180657 PRK06687, PRK06687, TRZ/ATZ family protein
MKVFQHVNIVTCDQDFHVYLDGILAVKDSQIVYVGQDKPAFLEQAEQIIDYQGAWIMPGLVNCHTHSAMT
GLRGIRDDSNLHEWLNDYIWPAESEFTPDMTTNAVKEALTEMLQSGTTTFNDMYNPNGVDIQQIYQVVKT
SKMRCYFSPTLFSSETETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNI
PLHVHVAETKEESGIILKRYGKRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLK
LASGIAPIIQLQKAGVAVGIATDSVASNNNLDMFEEGRTAALLQKMKSGDASQFPIETALKVLTIEGAKA
LGMENQIGSLEVGKQADFLVIQPQGKIHLQPQENMLSHLVYAVKSSDVDDVYIAGEQVVKQGQVLTVEL
>gnl|CDD|235852 PRK06688, PRK06688, enoyl-CoA hydratase; Provisional
MTMVTDLLVELEDGVLTITINRPDKKNALTAAMYQALADALEAAATDPAVRVVVLTGAGRAFSAGGDIKD
FPKAPPKPPDELAPVNRFLRAIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFAKLGLCP
DAGGSALLPRLIGRARAAEMLLLGEPLSAEEALRIGLVNRVVPAAELDAEADAQAAKLAAGPASALRYTK
RAINAATLTELEEALAREAAGFGRLLRTPDFREGATAFIEKRKPDFTGF
>gnl|CDD|180659 PRK06690, PRK06690, acetyl-CoA C-acyltransferase
NRAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFLSKGMEREIDDVILGNVVGPGGNVARLSALEAGLG
LHIPGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSPETIGDPDMGVAAEYV
AERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFNGLLDESIKKEMNYERIIKRTKPAFLHNGTVT
AGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDY
FEINEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGG
IGLALLFEKVE
>gnl|CDD|180660 PRK06696, PRK06696, uridine kinase; Validated
MSRKQLIKELAEHILTLNLTRPLRVAIDGITASGKTTFADELAEEIKKRGRPVIRASIDDFHNPRVIRYR
RGRESAEGYYEDAYDYTALRRLLLDPLGPNGDRQYRTASHDLKTDIPVHNPPLLAAPNAVLIVDGTFLLR
PELRDLWDYKIFLDTDFEVSRRRGAKRDTEAFGSYEEAEKMYLARYHPAQKLYIAEANPKERADVVIDNS
DPANPRLLFRERM
>gnl|CDD|136007 PRK06698, PRK06698, bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
MNRIGIIGAMQIEIDLLLEKLIMQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVD
AIINTGVAGGLHPDVKVGDIVISTNVTHHDVSKTQMKNLFPFQEEFIASKELVELARKACNSSSLHMEIH
EGRIVSGECFVEDSKLKAKLIDEYAPHCTEMEGAAIGHVAYINEVPFLVIRCISDSADDEAQISYDDFAK
TAANYCSEIIVEMLKTISSKTYSSKGENEMLQALIFDMDGTLFQTDKILELSLDDTFDHLRSLQLWDTVT
PIDKYREIMGVPLPKVWEALLPDHSLEIREQTDAYFLERLIENIKSGKGALYPNVKEIFTYIKENNCSIY
IASNGLTEYLRAIVSYYDLDQWVTETFSIEQINSLNKSDLVKSILNKYDIKEAAVVGDRLSDINAAKDNG
LIAIGCNFDFAQEDELAQADIVIDDLLELKGILSTVQRL
>gnl|CDD|235853 PRK06701, PRK06701, short chain dehydrogenase; Provisional
QAGPRQKPFPPMPAQHQNKQPGIESLMNPLPQFEAPNYKGSGKLKGKVALITGGDSGIGRAVAVLFAKEG
ADIAIVYLDEHEDANETKQRVEKEGVKCLLIPGDVSDEAFCKDAVEETVRELGRLDILVNNAAFQYPQQS
LEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQGSAIINTGSITGYEGNETLIDYSATKGAIHAFTRSLA
QSLVQKGIRVNAVAPGPIWTPLIPSDFDEEKVSQFGSNTPMQRPGQPEELAPAYVFLASPDSSYITGQML
HVNGGVIVNG
>gnl|CDD|102505 PRK06702, PRK06702, bifunctional O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
MGESWGKGTICVQGGYTPKNGEPRVLPLYQSTTYKYDTSDDLAALFNLEAEGYIYTRIGNPTLAAFEQKL
AELEGGVGAVATASGQAAIMLAVLNICSSGDHLLCSSTVYGGTFNLFGVSLRKLGIDVTFFNPNLTADEI
VALANDKTKLVYAESLGNPAMNVLNFKEFSDAAKELEVPFIVDNTLATPYLCQAFEHGANIIVHSTTKYI
DGHASSLGGIVIDGGNFDWTNGKYPELVEPDPSYHGVSYVQNFGAAAYIVKARVQLLRDYGNCMSPFNAY
ISNIGLETLHLRMERHSENALAVAKWLADHERIEWVNYPGLDSNENYSLAQKYLKKGASGVLTFGIKGGL
EAAKEFIANVKLATLVTHVADARTCVIHPASTTHRQLSAEDQRLAGVTSDLIRLSVGIEDVSDIIADLEA
ALVGGKQHADHN
>gnl|CDD|235854 PRK06703, PRK06703, flavodoxin; Provisional
MAKILIAYASMSGNTEDIADLIKVSLDAFDHEVVLQEMDGMDAEELLAYDGIILGSYTWGDGDLPYEAED
FHEDLENIDLSGKKVAVFGSGDTAYPLFCEAVTIFEERLVERGAELVQEGLKIELAPETDEDVEKCSNFA
IAFAEKFAQMN
>gnl|CDD|180663 PRK06704, PRK06704, RNA polymerase subunit sigma-70
MCTKVTHILKNHIDMNHSNINFLIEQYGELKRYCTFLTKNKWDGEDLAQETVCKVLQKYSNKDICMTLVY
KIARNRWLDQIKSKSVHEKIRDQITFEEPHEKIADLHEMVGKVLSSLNVQQSAILLLKDVFQYSIADIAK
VCSVSEGAVKASLFRSRNRLKTVSEEGIEIVEFTDDMEVVVTSIREERPELLTKLLPTIDFTKLPSKQPV
LLFNVKQPSSYSCMLCVA
>gnl|CDD|180664 PRK06705, PRK06705, argininosuccinate lyase; Provisional
MKQSKEEFIKSEGADFPGKTYVDCVLQHVFNFQRNYLLKDMFQVHKAHIVMLTEENLMKKEEAKFILHAL
KKVEEIPEEQLLYTEQHEDLFFLVEHLISQEAKSDFVSNMHIGRSRNDMGVTMYRMSLRRYVLRLMEHHL
LLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAAALSTT
SFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPY
VQISSIMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPYLYKGIEKAIRVFCIM
NAVIRTMKVEEDTLKRRSYKHAITITDFADVLTKNYGIPFRHAHHAASVIANMSLEQKKELHELCFKDVN
IYLQEKFKIQLLEKEWEEIISPEAFIQKRNVYGGPSKKEMERMINNRKELFRKEEEVFEKEKQRILQAEN
DLNMLASNIIES
>gnl|CDD|235855 PRK06707, PRK06707, amidase; Provisional
MKKWVKVTLSIAGGIVLLACAGGYYVYKNYFPKEPERIVYDKERVLQPIHNQLKGINIENVKIKEKEVVN
ATVDELQKMIDDGKLSYEELTSIYLFRIQEHDQNGITLNSVTEINPNAMEEARKLDQERSRNKKSNLYGI
PVVVKDNVQTAKVMPTSAGTYVLKDWIADQDATIVKQLKEEGAFVLGKANMSEWANYLSFTMPSGYSGKK
GQNLNPYGPIKFDTSGSSSGSATVVAADFAPLAVGTETTGSIVAPAAQQSVVGLRPSLGMVSRTGIIPLA
ETLDTAGPMARTVKDAATLFNAMIGYDEKDVMTEKVKDKERIDYTKDLSIDGLKGKKIGLLFSVDQQDEN
RKAVAEKIRKDLQDAGAILTDYIQLNNGGVDNLQTLEYEFKHNVNDYFSQQKNVPVKSLEEIIAFNKKDS
KRRIKYGQTLIEASEKSAITKDEFEKVVQTSQENAKKELDRYLVEKGLDALVMINNEEVLLSAVAGYPEL
AVPAGYDNNGEPVGAVFVGKQFGEKELFNIGYAYEQQSKNRKPPKL
>gnl|CDD|180666 PRK06710, PRK06710, long-chain-fatty-acid--CoA ligase; Validated
MKVEKPWLKSYPEEIPSTISYDIQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLG
VEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQS
ATKIEHVIVTRIADFLPFPKNLLYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLAL
LQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL
IPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGK
LVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNK
PEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDP
YRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNEDE
QTG
>gnl|CDD|168652 PRK06714, PRK06714, S-adenosylhomocysteine nucleosidase; Validated
MKRIAIVAAWEPELTYLHQSYPSERIEKRAAWEFHFHTINDLEIISVITGVGKVSCASCVQLLISEFQPD
ELFMTGICGSLSNKVKNGHIVVALNAIQHDVTAAGSGEDVFNLYNGRTAPIETTKSLVRRIKKIRSYDPI
HFGTFLSGDQRIRSSEMRYLLHTVYGALAVDQEVAAFAYVCQINKKPFLCLKAASDQANDKTKEEQKIFK
MLACERACEHLIAFLRVYEINVVNHR
>gnl|CDD|180667 PRK06718, PRK06718, NAD(P)-binding protein
NMPLMIDLSNKRVVIVGGGKVAGRRAITLLKYGAHIVVISPELTENLVKLVEEGKIRWKQKEFEPSDIVD
AFLVIAATNDPRVNEQVKEDLPENALFNVITDAESGNVVFPSALHRGKLTISVSTDGASPKLAKKIRDEL
EALYDESYESYIDFLYECRQKIKELQIEKREKQILLQEVLSSEYLNEDKQELFLRWLESRVH
>gnl|CDD|180668 PRK06719, PRK06719, precorrin-2 dehydrogenase; Validated
MYNMYPLMFNLHNKVVVIIGGGKIAYRKASGLKDTGAFVTVVSPEICKEMKELPYITWKQKTFSNDDIKD
AHLIYAATNQHAVNMMVKQAAHDFQWVNVVSDGTESSFHTPGVIRNDEYVVTISTSGKDPSFTKRLKQEL
TSILPKLIKKISRTHKL
>gnl|CDD|180669 PRK06720, PRK06720, hypothetical protein; Provisional
MTVRLIEGVMKMKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEITNLGGEALFV
SYDMEKQGDWQRVISITLNAFSRIDMLFQNAGLYKIDSIFSRQQENDSNVLCINDVWIEIKQLTSSFMKQ
QEEVVLSDLPIFGIIGTKGQSFHTVEALV
>gnl|CDD|180670 PRK06722, PRK06722, exonuclease; Provisional
MENATHFIVFDIERNFRPYKSEDPSEIVDIGAVKIEASTMKVIGEFSELVKPGARLTRHTTKLTGITKKD
LIGVEKFPQIIEKFIQFIGEDSIFVTWGKEDYRFLSHDCTLHSVECPCMEKERRIDLQKFVFQAYEELFE
HTPSLQSAVEQLGLIWEGKQHRALADAENTANILLKAYSERDITKRYKRHGELELVKNGKLTEKAKKKMR
KWVFKEMRKNTERPFVWSTFESSDTWESITERYYISESTIELLKKHFRTAVRKAERQIRYLAEMEKVVEE
N
>gnl|CDD|180671 PRK06724, PRK06724, hypothetical protein; Provisional
MNTLRAGIHHIEFWVANLEESISFYDMLFSIIGWRKLNEVAYSTGESEIYFKEVDEEIVRTLGPRHICYQ
AINRKVVDEVAEFLSSTKIKIIRGPMEMNHYSEGYYTIDFYDPNGFIIEVAYTPNVEM
>gnl|CDD|180672 PRK06725, PRK06725, acetolactate synthase large subunit
MKQYTTYEKLQCEEVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEG
YARASGKVGVVFATSGPGATNLVTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNY
QVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDVQNEKVTSFYNEVVEIPGYKPEPRPDSMKLREVAKA
ISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLFLGMLGMHGTYAANMAVTE
CDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVVGDVKKALHMLLHMSIHTQTDE
WLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRTFLTSGG
LGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQEMFY
ENRLSESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFPMVPPNKGN
NEMIMKRWEE
>gnl|CDD|136022 PRK06728, PRK06728, aspartate-semialdehyde dehydrogenase; Provisional
MSEKGYHVAVVGATGAVGQKIIELLEKETKFNIAEVTLLSSKRSAGKTVQFKGREIIIQEAKINSFEGVD
IAFFSAGGEVSRQFVNQAVSSGAIVIDNTSEYRMAHDVPLVVPEVNAHTLKEHKGIIAVPNCSALQMVTA
LQPIRKVFGLERIIVSTYQAVSGSGIHAIQELKEQAKSILAGEEVESTILPAKKDKKHYPIAFNVLPQVD
IFTDNDFTFEEVKMIQETKKILEDPNLKMAATCVRVPVISGHSESVYIELEKEATVAEIKEVLFDAPGVI
LQDNPSEQLYPMPLYAEGKIDTFVGRIRKDPDTPNGFHLWIVSDNLLKGAAWNSVQIAETMVEEGII
>gnl|CDD|75717 PRK06731, flhF, flagellar biosynthesis regulator FlhF; Validated
MVVKKEKQESVPFIIQKVIRMLEQNDVEQYFIHAYAEKLKVKFENATMITEEVIEYILEDMSSHFNTENV
FEKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVRDEA
AMTRALTYFKEEARVDYILIDTAGKNYRASETVEEMIETMGQVEPDYICLTLSASMKSKDMIEIITNFKD
IHIDGIVFTKFDETASSGELLKIPAVSSAPIVLMTDGQDVKKNIHIATAEHLAKQMLQTS
>gnl|CDD|235856 PRK06732, PRK06732, phosphopantothenate--cysteine ligase; Validated
MKILITSGGTTEPIDSVRGITNHSTGQLGKIIAETFLAAGHEVTLVTTKTAVKPEPHPNLSIIEIENVDD
LLETLEPLVKDHDVLIHSMAVSDYTPVYMTDLEEVSASDNLNEFLTKQNTEAKISSASDYQVLFLKKTPK
VISYVKKWNPNITLVGFKLLVNVSKEELIKVARASLIKNQADYILANDLTDISADQHKALLVSKNEVYTA
QTKEEIADLLLERIEKYDS
>gnl|CDD|180674 PRK06733, PRK06733, hypothetical protein; Provisional
MANVVEPTLTEDLVQLLRKERIVTLATTDFEKQVPNVSAISWVYAVSKTSIRFAVDQRSRIVENIRHNPG
VVLTIIANESVYSISGAAEILTDRMEGVPLKLALIEVNVEEVRDVMFYGAKIATEPTYEKTYDLRAAAKL
DNQVLVALKEL
>gnl|CDD|180675 PRK06737, PRK06737, ACT domain-containing protein
MSHTFSLVIHNDPSVLLRISGIFARRGYYISSLNLNERDTSGVSEMKLTAVCTENEATLLVSQLKKLINV
LQVNKL
>gnl|CDD|180676 PRK06739, PRK06739, pyruvate kinase; Validated
MTIDRICTIGPASNNKETLAQLINNGMKIVRLNLSHGTHESHKDIIRLVKSLDDSIKILGDVQGPKIRLG
EIKGEQITLQAGDSFILHTQPVTGSSTEASVDYEGIANDVKVGSRILMNDGEVELIVEKVSTDKIETKVK
TGGNISSHKGVNLPGAIVRLPAITEKDKKDIQFLLEEDVDFIACSFVRKPSHIKEIRDFIQQYKETSPNL
IAKIETMEAIENFQDICKEADGIMIARGDLGVELPYQFIPLLQKMMIQECNRTNTYVITATQMLQSMVDH
SIPTRAEVTDVFQAVLDGTNAVMLSAESASGEHPIESVSTLRLVSEFAEHVKKDGPFVMKDVLELLHKSL
DE
>gnl|CDD|180677 PRK06740, PRK06740, histidinol phosphate phosphatase domain-containing protein
MKVDYHIHLEEGPYSIGWLAKINEALQHYEPLKEAKHSMEWLVKTQERLQRRVKEGPYTTKWIDLYLEEA
LRKGIKEVGIVDHLYRFYEAREYYEKYVDISDSRLGRLQKEWLDQVRVASLDDFTKAIEEAKERWSKRGV
TLKLGIEADYFIGGEQELQSLLALGDFDYVIGSVHFLNGWGFDNPDTKEYFEEHDLYALYDTFFKTVECA
IRSELFDIIAHLDNIKVFNYRLDENEQLSYYKEIARALVETNTATEINAGLYYRYPVREMCPSPLFLQVL
AKHEVPITLSSDAHYPNDLGKYVEENVKTLRNHGVTSLATFTKRVRTMRLL
>gnl|CDD|102525 PRK06742, PRK06742, flagellar motor protein MotS; Reviewed
MIKRPQKGSPRWMTTFTDLTMLLLTFFVLLVATSKQDAVKLSKMLEKFSDTEQVDAKVMENTIPDISHEK
NDEKMISKKRMDELYKKLKAYVDNNGISQVNVYREDTGVSVVIVDNLIFDTGDANVKPEAKEIISQLVGF
FQSVPNPIVVEGHTDSRPIHNDKFPSNWELSSARAANMIHHLIEVYNVDDKRLAAVGYADTKPVVPNDSP
QNWEKNRRVVIYIKE
>gnl|CDD|136027 PRK06743, PRK06743, flagellar motor protein MotP; Reviewed
VGIIVGFAIVIAAIMLGGGGIKAFKNFLDVSSILIVIGGTTATIVVAYRFGEIKKYTKSIFTVLHRREED
LEQLTDLFVDFSKKSKKHGLLSLEVDGEQVDNPFIQKGIRLMLSGYDEDELKEVLMKDVETEVYELRKGA
ALLDKIGDFAPAWGMIGTLIGLIIMLQNLQDTSQIGTGMAVAMLTTLYGSVLANMIAIPLAEKVYRGIED
LYTEKKFVIEAISELYRGQIPSKLKLKLDTYVYETKIKKVKRAA
>gnl|CDD|75726 PRK06746, PRK06746, peptide chain release factor 2; Provisional
MMGAGFWDDQQGAQAVINEANALKDMVGKFRQLDETFENLEITHELLKEEYDEDLHEELESEVKGLIQEM
NEYELQLLLSDPYDKNNAILELHPGAGGTESQDWGSMLLRMYTRWAEKRGFKVETVDYLPGDEAGIKSVT
LLIKGHNAYGYLKAEKGVHRLVRISPFDSSGRRHTSFVSCEVVPEFNDEVEIEVRTEDLKIDTYRASGAG
GQHVNTTDSAVRITHTPTNTVVTCQSERSQIKNREHAMKMLKAKLYQKKLEEQQAELDEIRGEQKEIGWG
SQIRSYVFHPYSLVKDHRTNTEVGNVQAVMDGEIDPFIDAYLRSRI
>gnl|CDD|180678 PRK06748, PRK06748, hypothetical protein; Validated
KTVIEGVYSPCYGKVEKLFVRESSYVYEWEKLALIETIDKQKVEIKVGISGYIESLEVVEGQAIADQKLL
ITVRDDLLITGSD
>gnl|CDD|168658 PRK06749, PRK06749, replicative DNA helicase; Provisional
MSIQNVEAEKTVLGSLLLDGELIKECRLTEQYFSMPVHKSIFQLMRKMEDEGQPIDLVTFTSRVDPNFLK
GIGGMEYFIGLMDGVPTTSNFSYYEGLVRGAWKMYQAGVLGHKMGERLIAEKSEKIIGETITALCELEEK
DCVCEFDLKDALVDLYEELHQDAKEITGIETGYTSLNKMTCGLQEGDFVVLGARPSMGKTAFALNVGLHA
AKSGAAVGLFSLEMSSKQLLKRMASCVGEVSGGRLKNPKHRFAMEDWEKVSKAFAEIGELPLEIYDNAGV
TVQDIWMQTRKLKRKHGDKKILIIVDYLQLITGDPKHKGNRFQEISEISRKLKLLARELNVCVVALSQLS
RSVESRQDKRPLLSDLRETGQIEQDADVIMLMYREDYYDKETMQKEMTEIHVAKHRNGPVGSFKLRFLKE
FGRFVEGG
>gnl|CDD|168659 PRK06751, PRK06751, single-stranded DNA-binding protein; Provisional
MMNRVILVGRLTKDPDLRYTPNGVAVATFTLAVNRAFANQQGEREADFINCVIWRKQAENVANYLKKGSL
AGVDGRLQTRNYEGQDGKRVYVTEVLAESVQFLEPRNGGGEQRGSFNQQPSGAGFGNQSSNPFGQSSNSG
NQGNQGNSGFTKNDDPFSNVGQPIDISDDDLPF
>gnl|CDD|168660 PRK06752, PRK06752, single-stranded DNA-binding protein; Validated
MMNRVVLIGRLTKEPELYYTKQGVAYARVCVAVNRGFRNSLGEQQVDFINCVVWRKSAENVTEYCTKGSL
VGITGRIHTRNYEDDQGKRIYITEVVIESITFLERRREGASQ
>gnl|CDD|168661 PRK06753, PRK06753, hypothetical protein; Provisional
MKIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESVKEVGAGIGIGDNVIKKLGNHDLAKGIKNAGQILST
MNLLDDKGTLLNKVKLKSNTLNVTLHRQTLIDIIKSYVKEDAIFTGKEVTKIENETDKVTIHFADGESEA
FDLCIGADGIHSKVRQSVNADSKVRYQGYTCFRGLIDDIDLKLPDCAKEYWGTKGRFGIVPLLNNQAYWF
ITINAKERDPKYSSFGKPHLQAYFNHYPNEVREILDKQSETGILHHDIYDLKPLKSFVYGRIVLLGDAAH
ATTPNMGQGAGQAMEDAIVLANCLNAYDFEKALQRYDKIRVKHTAKVIKRSRKIGKIAQIESKLLVALRN
RVMKRMPNALAAGQTKFLYKSKE
>gnl|CDD|180679 PRK06754, mtnB, methylthioribulose 1-phosphate dehydratase
MKQLQRRWNELAEIKKELAARDWFPATSGNLSIKVSDDPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVE
ETELKPSAETLLHTHIYNNTNAGCVLHVHTVDNNVISELYGDDGAVTFQGQEIIKALGIWEENAEIHIPI
IENHADIPTLAEEFAKHIQGDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLLSIQGGVSK
>gnl|CDD|102532 PRK06755, PRK06755, hypothetical protein; Validated
MLFFLKKWNELKDVKSELALRDWFYGTKISLSLCTSKEPLTFLVNVEGRDKGLFSEEDFIVVNCMCEPVF
ENEEKPAAESFMHADIYKKSSAECILQVQTVDSHLISELYGEEGEVTFDKRSVERVFGKEGITEMTIPIV
EDEKKFADLLENNVPNFIEGGGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLLMIKGAKSSVI
>gnl|CDD|168663 PRK06756, PRK06756, flavodoxin; Provisional
MSKLVMIFASMSGNTEEMADHIAGVIRETENEIEVIDIMDSPEASILEQYDGIILGAYTWGDGDLPDDFL
DFYDAMDSIDLTGKKAAVFGSCDSAYPKYGVAVDILIEKLQERGAAVVLEGLKVELTPEDEDVEKCLQFG
AEFVKHLS
>gnl|CDD|136035 PRK06758, PRK06758, hypothetical protein; Provisional
MNQYIRYTIAVLFAIIGGTICFWTNTQLGENIIFNGIETLVSASILGGYIFFLFNPEENAQKTMLLTMIG
IVGGCISYSMTNYTLPLQLSSAFFHGLWTWFIAFCLADVFNLLQDNEEENGRQIESNS
>gnl|CDD|235857 PRK06759, PRK06759, RNA polymerase factor sigma-70; Validated
MKPATFTEAVVLYEGLIVNQIKKLGIYQDYEEYYQCGLIGLWHAYERYDEKKGSFPAYAVVTVRGYILER
LKKEFAVQEKCVCVGEYEDHFHFEDVEMKVKDFMSVLDEKEKYIIFERFFVGKTMGEIALETEMTYYQVR
WIYRQALEKMRNSV
>gnl|CDD|180681 PRK06760, PRK06760, hypothetical protein; Provisional
MKKTLTIFMLTILLLISFSACSKKENSFPANGVLIIGDENNISPIINRYQEITKENEVFSVKKGEVGNGQ
VLILNESTAQALIKEKVFRKRDNGSNYWPIDTLPKFPKEGSLLFANEDEKTIKSIKIEGKEIPVTYDSDA
WIGNTRNYPTQWYVIVAKNSVYKEIKANETKMHLLHFKKSIGDEKPKMSTDNTLVNENVKVKKLIKGLEG
EVSFQFVTIGEKS
>gnl|CDD|180682 PRK06761, PRK06761, hypothetical protein; Provisional
MMTKLIIIEGLPGFGKSTTAKMLNDILSQNGIEVELYLEGNLDHPADYDGVACFTKEEFDRLLSNYPDFK
EVLLKNVLKKGDYYLLPYRKIKNEFGDQFSDELFNDISKNDIYELPFDKNTELITDRWNDFAEIALEENK
VYIFECCFIQNPVTILMIKYGAQKEKITNYVMKLAKIIENLNPMLFYLEQDDVEFSFRKALKERNPEWST
GIVDYYTNQGYGKEHNLSGVEGRIKVLEARKNLELEILDMLKMKKEKINNTKEEIDSYRSMLKDKLTIQM
VK
>gnl|CDD|235858 PRK06762, PRK06762, hypothetical protein; Provisional
MTTLIIIRGNSGSGKTTIAKQLQERLGRGTLLVSQDVVRRDMLRVKDGPGNLSIDLIEQLVRYGLGHCEF
VILEGILNSDRYGPMLKELIHLFRGNAYTYYFDLSFEETLRRHSTRPKSHEFGEDDMRRWWNPHDTLGVI
GETIFTDNLSLKDIFDAILTDIGLRK
>gnl|CDD|136040 PRK06763, PRK06763, F0F1 ATP synthase subunit alpha; Validated
MNMKKVILAGALGIAALSGTNLPGLEITKASAASIESNFSTIEGRVVEVDNGVIVIKSKQYEEPVSVYID
SLSNVKVGDEVKATGSMMRNFTEYMVATAVENTTNKLGMHMKEDGSPDYVIGEVSKVYTMEDDGDGATKY
VVVEYPSLNGKKLIIDVFLTKGQVFHVGDKVKVDMKYVGWGGSSINWNTTDHIEKVNEVKSNVENNDDVW
IWS
>gnl|CDD|102540 PRK06764, PRK06764, hypothetical protein; Provisional
MKKIKKFAGVALAGTIGLSGLLFLEPSVSAAESQQVKEENFNAIDVSMNINELYVLSGRSIDVLSGDKEA
IQLNKYTIRFSKPGKYVIRVNGCIYNDVYTFIVNE
>gnl|CDD|235859 PRK06765, PRK06765, homoserine O-acetyltransferase; Provisional
MRLALLISGSVPALALMQIVEKEKFTLKEFTTEGGRTIPDVQMGYETYGTLNRAKSNVILITHYFSATSH
AAGKYTADDEESGYWDGLIGPGKAIDTNKYFVISTDTLCNVQVKDPNVITTGPASINPKTGKPYGMDFPV
VTILDFVRVQKELIKSLGIARLHAVMGPSMGGMQAQEWAVHYPHMVERMIGVIGNPQNDAWTSVNVLQNW
AEAIRLDPNWKGGKYYGEEQPMKGLTLALRMMTMNAFDEHFYETTFPRNASIEVDPYEKVSTLTSFEKEI
NKATYRRAELVDANHWLYLAKAVQLFDAGHGFSSLEEALSNIEANVLMIPCKQDLLQPPRYNYKMVDILQ
KQGKYAEVYEIESINGHMAGVFDIHLFEKKIYEFLNRKV
>gnl|CDD|180685 PRK06767, PRK06767, methionine gamma-lyase; Provisional
MKKKHMETALIHHGYTSEEHKGSLTPPLFQTSTFTFETAQQGEASFAGVDPSYIYSRLGNPTVKLFEERM
AVLEGGEEALAFGSGMAAISATLIGFLKAGDHIICSNGLYGCTYGFLEVLEEKFMITHSFCDMETEADIE
NKIRPNTKLIFVETPINPTMKLIDLKQVIRVAKRNGLLVIVDNTFCSPYLQRPLELGCDAVVHSATKYIG
GHGDVVAGVTICKTRALAEKIRPMRKDIGGIMAPFDAWLLLRGLKTLAVRMDRHCDNAEKIVSFLKNHDA
VEGVWYPEGELASRQMKRGGGVISFSIKGGKEETQAFINDLHFITIAVSLGDTETLIQHPATMTHAAIPA
ELRQEMGIYDNLIRLSVGLESWEDIVSDLEQALKKI
>gnl|CDD|180686 PRK06769, PRK06769, HAD-IIIA family hydrolase
MTNIQAIFIDRDGTIGGDTTIHYPGSFTLFPFTKASLQKLKANHIKIFSFTNQPGIADGIATIADFVQEL
KGFGFDDIYLCPHKHGDGCECRKPSTGMLLQAAEKHGLDLTQCAVIGDRWTDIVAAAKVNATTILVRTGA
GYDALHTYRDKWAHIEPNYIAENFEDAVNWILN
>gnl|CDD|180687 PRK06770, PRK06770, hypothetical protein; Provisional
MKKLFKWIGIIAGMAVLGIGVTYGMLYYAENPVKNAQTAQPAAKKEKVLADENVSLPNSGFNKTFKSTEE
EIITAMHKMTHQKVKADEKWGFIEMTQENIEKLKDIINSSNFVQKEELLAILERWEKGDFSKIVEDHNYL
WKLQGGNTGKATGVMSPEEEKEYILEMFKKEYSGSLLIAG
>gnl|CDD|180688 PRK06771, PRK06771, hypothetical protein; Provisional
MEFWMIIPIAIFGFIYIVEKLTKIEKKTDARLKRMEDRLQLITKEMGIVDREPPVNKELRQLMEEGQTVT
AVKRVREAFGFSLLEAKQYVDKL
>gnl|CDD|102546 PRK06772, PRK06772, salicylate synthase
MKISEFLHLALPEEQWLPTISGVLRQFAEEECYVYERQPCWYLGKGCQARLHINADGTQATFIDDAGEQK
WAVDSIADCARRFMAHPQVKGRRVYGQVGFNFAAHARGIAFNAGEWPLLTLTVPREELIFEKGNVTVYAD
SADGCRRLCEWVKEAGTTTQNAPLAVDTALNGEAYKQQVARAVAEIRRGEYVKVIVSRAIPLPSRIDMPA
TLLYGRQANTPVRSFMFRQEGREALGFSPELVMSVTGNKVVTEPLAGTRDRMGNPEHNKAKEAELLHDSK
EVLEHILSVKEAIAELEAVCQPGSVVVEDLMSVRQRGSVQHLGSGVSGQLAENKDAWDAFTVLFPSITAS
GIPKNAALNAIMQIEKTPRELYSGAILLLDDTRFDAALVLRSVFQDSQRCWIQAGAGIIAQSTPERELTE
TREKLASIAPYLMV
>gnl|CDD|180689 PRK06774, PRK06774, aminodeoxychorismate synthase component II
MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFA
DKLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGC
FELTAWSERGGEMDEIMGIRHRTLPLEGVQFHPESILSEQGHQLLDNFLKN
>gnl|CDD|180690 PRK06777, PRK06777, 4-aminobutyrate--2-oxoglutarate transaminase
MKNSELNQRRLEATPRGVGVMCDFYAERAENATLWDVEGREYIDFAAGIAVLNTGHRHPKVVAAVRQQLD
QFTHTAYQIVPYASYVTLAERINALAPIDGPAKTAFFTTGAEAVENAVKIARAYTGRPGVIAFGGAFHGR
TLLTMALTGKVAPYKVGFGPFPGSIFHALYPNELHGVSVEEALSSVERLFKADIAPDQVAAILLEPIQGE
GGFNVAPPEFMSALRTLCDEHGILLIADEVQTGFARTGKLFAMEYYDVKPDLITMAKSLGGGMPISAVVG
RAEVMDAPAPGGLGGTYAGNPLAVAAALAVLDVIAEEKLCQRALILGAHLVEVLEKAKASCPAIVDIRAR
GSMVAVEFNDPQTGKPSPEFTRQYQRQALEEGLLLLSCGVHGNVIRFLYPLTIPDAQFSKALNILTRLLA
S
>gnl|CDD|235860 PRK06778, PRK06778, hypothetical protein; Validated
GATTIIKRANRKKHHVRHSGAWKVAFADFTLAMMALFMVLWIVNSVSKSERESIIAALHGQSIFNGGGLS
PLNKISPSHPPKPATVAVPEETEKKARDVNEKTALLKKKSATELGELATSINTIARDAHMEANLEMEIVP
QGLRVLIKDDQNRNMFERGSAQIMPFFKTLLVELAPVFDSLDNKIIITGHTDAMAYKNNIYNNWNLSGDR
ALSARRVLEEAGMPEDKVMQVSAMADQMLLDAKNPQSAGNRRIEIMVLTKSASDTLYQYFGQHGDKVVQP
LVQKLDKQQ
>gnl|CDD|235861 PRK06782, PRK06782, flagellar motor switch protein; Reviewed
MPEQHTKGDTSTIVLEKEEEHLTPQECDILGEIANISFGSASTVLSTLLNQQVSISAPRIEIVDLYDTSD
VEVPHVVLNVHFTKGLDMENLLVLKQDVALSIADLMMMGTGEVEDGKELGELELSAVQEAMNQMMGFSAT
SMSEMFQDTIDISPPTIKVIKLSEELEKIDGNQTIVKVSFDLKIGDLVNSKLVQIISVEHAKEMINKLLS
GGVEEAEIVEEEIHLTQEEKDVLGEVANISIGSASTVLSTLLNQPVSISTPNVEAINVRHYDGVEVPFVI
LNVDFVEGLKNENVFVFTKDVALIMADLMMMGTGEVDEEKELTELELSAIKEIMNQMMGHAATAMSEMFQ
EKIDISPPTVKFVTLKEEMLGESIEVDELVQITFNLEVGDLLQTKMYQILPISEAKEMVRLLLYPMVKEE
EEIATEEIEPEKVVEPVVQPIEFKEVKQMEPVYMDTSILQDVPMNVKVVFGSTKKTIQDILSLQENEVVV
LDEDIDEPIRIYVNGVLVAYGELVNVDGFFGVKVTKSL
>gnl|CDD|180693 PRK06788, PRK06788, flagellar motor switch protein; Validated
MKHEVSPVSLMELEDFAGKRNEASKAHIDTVSDISIELGVKLGKASITLGDVKQLKVGDVLEVEKNLGHK
VDVYLSNMKVGIGEAIVMDEKFGIIISEIEADKKQAALMKAQSQMQDKE
>gnl|CDD|180694 PRK06789, PRK06789, flagellar motor switch protein; Validated
MKLQDDIPLTIYFEIGNTKKKIEDLLHITKGTLYRLENSTKNTVRLMLENEEIGTGKILTKNGKMYVEIV
ELKR
>gnl|CDD|180695 PRK06792, flgD, flagellar basal body rod modification protein; Validated
MPTVGLNTTSTNHIPLQAGAQTKNASVTGAQSTAQQANGVSASTQKTPGIMDKDDFLKLFLASFQHQDPF
NAMDMNQMMNQTAQLSLMEQVQNMTKAVDKLQSTMYSTALDGGMKFLGKYVRGVSNDGKQVTGQVETVRL
AENNDVQLIVDNQVVSLRFVERVSDKPITETNPEDEKKDDIEKNEEVKPD
>gnl|CDD|180696 PRK06793, fliI, flagellar protein export ATPase FliI
RLLMNENQKWNTFIETPFYTKVGKVHSVQEQFFVAKGPKAKIGDVCFVGEHNVLCEVIAIEKENNMLLPF
EQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVF
ETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGM
RKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPIGGKTLL
MESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSV
SRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQENAENAYIFECKNKVEGINTFLKQGRSDSFQ
FDDIVEAMHHIV
>gnl|CDD|180697 PRK06797, flgB, flagellar basal body rod protein FlgB; Reviewed
MPDLVSDVGHYMNYLVTKRNTVSSNIANANTPGYKAQDVTFAEQMNKSSALYKSNAADLKSNPDLYQTNE
MHLPTVNTKNTYAKIQTKSMQTNKDGNSVDVTTEMLDLMKANQLYGISINAINTQYAINQAARGR
>gnl|CDD|180698 PRK06798, fliD, flagellar hook-associated protein 2
MAGTATGIGGRQQIWNLGNNMIDTSNFVELELQALEMKKTPYTNQKQSLTSEKLLYASLKKEFSSFLQTF
KDLTTFKGNEKKVTLSQEGYITVQADASAIAGTYNITVENLAQRHQITSKPVPDIDAKIGVDETIKINGK
EIKVTKDMTYKDLINKINSGNYGVSAYTLGNKIFFTSTTEGEEGSIKFTDGDSGFLEAIGLVQSSGVAAN
DITAAENAEYTINGIKGTSATNKIETIPGVTINLKKETTEPIKLTIQDSNVKDAANLIKKMVDEYNKAVS
TVDLFAGKGGALQGSAIMFSINRAMNNVFTFSQDGNYLFSFGIQVDKEGTMKVDEEALKKALKENPDAAK
QFFFGINGLGKEMEKSLDKIFGDEGIIGERSKSIDNRVSKLDLKITDIDTQNKQKQDNIVDKYQKLESTL
AALDSQLKTIKAMTKQKSDD
>gnl|CDD|180699 PRK06799, flgK, flagellar hook-associated protein FlgK; Validated
MRLSDYNTPLSGMLAAQMGLQTTQQNLSNIHTPGYVRQMVNYGSVGASGGLLPEQQIGYGVQTLGVDRIT
DEVKTKQYNDQLSQLSYYNYMNSALSRVESMVGTTGKNSLSSLMDGFFNAFREVAKNPEQANYYDTLISE
TGKFTSQLNRLAKGLDELEAQTTEDIEAHVNEFNRLAKSLAEANKKIGQAGTQVPNQLLDERDRILTEMS
KYANIEVSYESMNPNIASVRMNGVLTVNGQDTYPLQLNKTKEPMEFEIYGSEIPLPSGAIISAIDTKAKI
KSYKKNLEELMSSLKKAVNTVMGKSFFVGDSAKKWKLNPEFAKDVSKMKISAETANKLAAITDDKYKEGL
SYKQALDQFIVGVASDKSAVNAYQKIHTDLLEGIQQEKMSLEGVNMEEEMVNLMAFQKYFVANSKAITTM
NEVFDSLFSII
>gnl|CDD|180700 PRK06800, fliH, flagellar assembly protein H; Validated
MSLFKNRIPKNSVSFSEETYELQFPKPIEVEVEEEIQKDHEELLAQQKSLHKELNQLRQEQQKLERERQQ
LLADREQFQEHVQQQMKEIEAARQQFQKEQQETAYEWTELLWDQSFQLAEKIVNQAVDTRLLDVLPILTG
IVQTLPTSFEKLNITVHPETFERIQEEKENTKEYWLLQLVEWKYDFSLQFGEFVLEEEKEFFEFKFAPIF
AKLRQKWEEEKLFEEQNV
>gnl|CDD|180701 PRK06801, PRK06801, ketose 1,6-bisphosphate aldolase
MALISLANGLAHARKHGYALGAFNVLDSHFLRALFAAAKQERSPFIINIAEVHFKYISLESLVEAVKFEA
ARHDIPVVLNLDHGLHFEAVVRALRLGFSSVMFDGSTLEYEENVRQTREVVKMCHAVGVSVEAELGAVGG
DEGGALYGEADSAKFTDPQLARDFVDRTGIDALAVAIGNAHGKYKGEPKLDFARLAAIHQQTGLPLVLHG
GSGISDADFRRAIELGIHKINFYTGMSQAALAAVEQRMTHRHAIYDEFAELLLGIEEAISDTVAQQMRIF
GSAGQA
>gnl|CDD|180702 PRK06802, flgC, flagellar basal body rod protein FlgC; Reviewed
MSFNDIYRIAGSAMTAQTIRLNTVASNLANAESPAASAATAYKARSPVFAAVYSARTLADPRGVQGAQVQ
VLDVVQVGGSVKRYEPNNPLANPQGYVFYPDVNVVEEMADMMSASRSFETNVEVLNSVKSMQQSLLKLGE
R
>gnl|CDD|235862 PRK06803, flgE, flagellar basal body protein FlaE
MSFNIALSGLNATTQQLNTISNNIANSSTKGFKGSRTEFSSIYNGGQPGGVEVSSVSQNFSKDGSLTYTG
RGLDLAISGGGFFVLKESDGDTAYTRAGMFRSDVDGYLTDPQGMKLQGYPVDAAGNLQTGNVSDLQVQTA
SLPAKATDQLDFVANLDASVTPIDPSVSPFDPTDEKSYNSSTTSTVYDSLGNEHAVTQYFVKTATNEWAV
HYTVDGGDVTPPLGHTLQFDDTGALIPGKGSTINLHGTFNPAGASDYDIDIDYTGSTQYAADFNNSRNKS
NGYTSGELNGVRIEDNGMVYATYTNGQRQLQGQVVLANFANPNGLVTVSNTAWSASNKSGAPILGTPGTG
TLGSLTSGALEGSNVDITAELVGLMTAQRNYQANAKVISTNDTMQQALFNAI
>gnl|CDD|235863 PRK06804, flgA, flagellar basal body P-ring formation protein FlgA
MYYSQGWKPNFRLTETISIKGKHTLSSLLICGALLCANTISAAENNTRKQVYTQVLHAATQDIAQTAKNK
NWQGYQVKMNIFIPAEISRYKPCQKALQVALPTAETQHLSRLRYEVSCPDGQGWEVVVTVKPDIYLPVWV
AKQTLERGRKVQADDIELKKKNISGVQGGYITDPDEAIGLTIKRRIRQLQAVIPSQLEQPVLVERGQHVL
MIAAQDGIEAQTLGIAQKNGRKGELIKVKNLSSGRVVTATVDGSGRVRMLG
>gnl|CDD|180705 PRK06806, PRK06806, class II aldolase
MPLVQMKELLKKANQENYGVGAFSVANMEMVMGAIKAAEELNSPIILQIAEVRLNHSPLHLIGPLMVAAA
KQAKVPVAVHFDHGMTFEKIKEALEIGFTSVMFDGSHLPLEENIQKTKEIVELAKQYGATVEAEIGRVGG
SEDGSEDIEMLLTSTTEAKRFAEETDVDALAVAIGNAHGMYNGDPNLRFDRLQEINDVVHIPLVLHGGSG
ISPEDFKKCIQHGIRKINVATATFNSVITAVNNLVLNTPYSDYFTYHQDVIKAAYENVKKHMQIFGSENK
A
>gnl|CDD|235864 PRK06807, PRK06807, 3'-5' exonuclease
MGNISLPLDYVVIDFETTGFNPYNDKIIQVAAVKYRNHELVDQFVSYVNPERPIPDRITSLTGITNYRVS
DAPTIEEVLPLFLAFLHTNVIVAHNASFDMRFLKSNVNMLGLPEPKNKVIDTVFLAKKYMKHAPNHKLET
LKRMLGIRLSSHNAFDDCITCAAVYQKCASIEEEAKRKSNKEVLDETAVYEAVKEILVKNKRDIEWIRCM
NVGSYLDIKAFYPVMRLKVKGRKKYVLTDILEDDVKEICTSLKCEPALKSEVGNTRIMLNSLEDVLKLES
YILEQYDFVLQALHDYKNNEMNADEKLKEYLNI
>gnl|CDD|180707 PRK06811, PRK06811, RNA polymerase factor sigma-70; Validated
MKINEDNFIKELKKKNEKALEFIVDTYGNLVKKIVHKVLGTVNYSQLIEECVNDIFLSIWNNIDKFDEEK
GSFKKWIAAISKYKAIDYKRKLTKNNEIDSIDEFILISEESIENEIILKENKEEILKLINDLEKLDREIF
IRRYLLGEKIEEIAKKLGLTRSAIDNRLSRGRKKLQKNKLNISLGGEVI
>gnl|CDD|168683 PRK06813, PRK06813, homoserine dehydrogenase; Validated
MKIKVVLSGYGTVGREFIKLLNEKYLYINETYGIDLVVSGVLGRNVAIHNEDGLSIHHLLRYGGGSCAIE
KYIEHHPEERATDNISGTVLVESTVTNLKDGNPGKQYIKQAIEKKMDIVAISKGALVTNWREINEAAKIA
NVRIRYSGATAAALPTLDIGQFSLAGCHIEKIEGILNGTTNYILTKMNEEDITFEEALKEAQSKGIAETN
PILDVSGSDSACKLLLLTNSLMGTENKLTDIHIKGIEHVTKQQIRNAKEQNKIIKLIASAYKDNEGNVNL
NVEPYKIEKNHPLANVNGTEKGITFFTDTMGQVTTIGGASNPRGAAAAALKDIINLYRKDLSRINR
>gnl|CDD|235865 PRK06814, PRK06814, acyl-[ACP]--phospholipid O-acyltransferase
DTMKLYLMKSRRFAPLFWTQFFGAFNDNFLKNALVILILYGLSGALGAYNNALVTLAGAVFILPFFIFSA
LAGQLADKYDKAKLAKILKFAEIGIAALAIYGFHLNSVPLLFAALFLMGIHSALFGPIKYSILPDHLNKD
ELLGANALVEAGTFIAILLGTIIGGLATISGNFVILVALLMGIAVLGWLASLFIPKTGNAAPDLKIDRNI
IRSTITLLKYAKADKRIWLAILGISWFWLVGAVVLSQLPLLAKETLGGDENVATLFLAVFSVGVAVGSFL
ASKLSEGRITLLYVPIGALLMGLFGLDLAFASSSVPAEPAQLKSILVFLSKRHGWRILIDLFGLAAAGGL
YIVPLFAALQAWANPAHRARVIAANNVLNAAFMVAGTIILALLQALGFSIPWIILFIALANLIVAILILR
LLPTNLLRDIFSILFRAFYRVEVKGLENLQKAGKKAVIAANHVSFLDGPLLAAYLPEEPTFAIDTDIAKA
WWVKPFLKLAKALPVDPTNPMATRTLIKEVQKGEKLVIFPEGRITVTGSLMKIYDGPGMIADKAGAMVVP
VRIDGLQFTHFSRLKNQVRRKWFPKVTVTILPPVKLAVDPELKGRERRSAAGAALYDIMSDMMFETSDYD
RTLFEALIEAAKIHGFKKLAVEDPVNGPLTYRKLLTGAFVLGRKLKKNTPPGENVGVMLPNANGAAVTFF
ALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSRAFIEKARLGPLIEALEFGIRIIYLEDVRAQIGL
ADKIKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNA
LPVFHSFGLTGGLVLPLLSGVKVFLYPSPLHYRIIPELIYDTNATILFGTDTFLNGYARYAHPYDFRSLR
YVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGIDE
GGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE
LAAELWPDALHAAVSIPDARKGERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGK
IDYVAVTKLAEEAAAKPEAA
>gnl|CDD|180709 PRK06815, PRK06815, threonine/serine dehydratase
NTLFDAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQG
VITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGK
VYISPYNDPQVIAGQGTIGMELVEQQPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLY
TSLEAGEIVEVAEQPTLSDGTAGGVEPGAITFPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAG
VALAAALKLAPRYQGKKVAVVLCGKNIVLEKYLEAVS
>gnl|CDD|235866 PRK06816, PRK06816, StlD/DarB family beta-ketosynthase
MNVYITSTGAFLPGEPVSNDEMEAYLGLINGKPSRARRIILRNNGIKTRHYALDPEGRPTHSNAQMAAEA
IRDLLDDAGFSLGDIELLACGTSQPDQLMPGHASMVHGELGAPPIEVVSSAGVCAAGMMALKYAYLSVKA
GESRNAVATASELASRWFRASRFEAEEEKLAELEENPEIAFEKDFLRWMLSDGAGAVLLENKPRPDGLSL
RIDWIDLRSYAGELPVCMYAGAEKNEDGSLKGWSDYPPEEAEAASALSLKQDVRLLNENIVVYTIKPLLE
LVDKRNLDPDDIDYFLPHYSSEYFREKIVELLAKAGFMIPEEKWFTNLATVGNTGSASIYIMLDELLNSG
RLKPGQKILCFVPESGRFSTAFMLLTVV
>gnl|CDD|235867 PRK06819, PRK06819, FliC/FljB family flagellin
MAAVINTNSLSLLTQNNLNKSQSSLGTAIERLSSGLRINSAKDDAAGQAIANRFTSNIKGLTQAARNAND
GISIAQTTEGALNEINNNLQRVRELTVQAQNGSNSSSDLDSIQDEISQRLAEIDRVSDQTQFNGVKVLAE
DTTMSIQVGANDGETIDINLQKIDSKSLGLGSFSVSGVSGALTSLTFTDTALDTSVTGVTTTTALDFSDI
STFAKGATVHGIGDVGTDGAYADGYVIRTTDGKQYKGEVDATNGKVTFADDANGDPITDATKLEAAAQFS
PAGKATASPLETLDDALKQVDGLRSSLGAVQNRFESTVTNLNNTVTNLSSARSRIEDADYATEVSNMSRA
QILQQAGTSVLAQANQVPQTVLSLLR
>gnl|CDD|180712 PRK06820, PRK06820, EscN/YscN/HrcN family type III secretion system ATPase
MKLPDIARLTPRLQQQLTRPSAPPEGLRYRGPIVEIGPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQ
EMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWRELDCPPPSPLTR
QPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAADVMVLALIGERGREVREFLEQ
VLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPP
AAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYP
AIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGEYQAGEDLQADEALQRYPAICAFLQQ
DHSETAHLETTLEHLAQVVG
>gnl|CDD|136070 PRK06823, PRK06823, ornithine cyclodeaminase family protein
MKILNKQKILAKFDADRATLLLKEGFIAFSQGRVQMPPVQHLLFDQANGDCCIKSGYLQGDDQFVVKVST
GFYDNPAQGLPSNQGLMLAFSAKTGEPQALLLDEGWLTALRTALAGRIVARLLAPQHVSAIGIVGTGIQA
RMQLMYLKNVTDCRQLWVWGRSETALEEYRQYAQALGFAVNTTLDAAEVAHAANLIVTTTPSREPLLQAE
DIQPGTHITAVGADSPGKQELDAELVARADKILVDSIAQCTDFGEVSHAFKAGLLAHHNLTELGLALAQG
IPFRENDQQITLADLTGVAIQDVQIAKGILGDLKG
>gnl|CDD|168689 PRK06824, PRK06824, translation initiation factor Sui1; Validated
SSLSALGGLVYSTEHGRHCPDCGQPVAACICKQAAAPAGDGIVRVRRETKGRGGKTVTVITGVPLAEDAL
KELAKELKRRCGTGGTLKDGVIEIQGDHVELLLAELLKRGFKAKKAGG
>gnl|CDD|235868 PRK06826, dnaE, DNA polymerase III DnaE; Reviewed
MKMSFVHLHVHTEYSLLDGSARIKDLIKRAKELGMDSIAITDHGVMYGVVDFYKAAKKQGIKPIIGCEVY
VAPRSRFDKEPDIDNETYHLVLLAKNETGYKNLMKIVSKAFTEGFYYKPRVDHELLKEHSEGLIALSACL
AGEVPRYILKGNYEKAKEAALFYKDIFGKENFYLELQDHGIPEQRKVNEELIKLSKELGIPLVATNDVHY
IRKEDAKAHDVLLCIQTGKTVDDENRMRFPSDEFYLKSPEEMYELFSYVPEALENTVKIAERCNVEFEFG
KSKLPKFPLPEGYDPYEYLRELCYEGLKKRYPNPSEELIERLEYELSVIKQMGYVDYFLIVWDFIRFARE
NGIMVGPGRGSAAGSLVAYTLGITKIDPIKYNLLFERFLNPERVSMPDIDIDFCYERRQEVIDYVVEKYG
KDRVAQIITFGTMAARAAIRDVGRALNYPYAEVDRIAKMIPTELGITIDKALELNPELKEAYENDERVRE
LIDTARALEGLPRHASTHAAGVVISSEPLVEYVPLQKNDGSIVTQFTMTTLEELGLLKMDFLGLRTLTVI
RDAVDLIKKNRGIEIDLDKIDYDDKKVYKMIGEGKTVGVFQLESAGMRSFMKELKPDSLEDIIAGISLYR
PGPMDSIPRYIKNKNNPEKIEYLHPKLEPILKVTYGCIVYQEQVMQIVRDLAGYSMGRSDLVRRAMSKKK
HDVMEEERKNFIYGIVDEGGPGCIRNGIDEETANKIFDSMMDFASYAFNKSHAAAYAVVAYQTAYLKRYY
PVEFMAALLNSVMGNSDKVAFYIEECRRLGIEVLPPDINESYSKFTVEGDKIRFGLAAVKNVGENAIDSI
VEEREKKGKFKSLVDFCERVDTSQINKRAVESLIKAGAFDSLGVYRSQLLAVYEKILDSISKQRKKNIEG
QISLFDLIGEEEESSLEIKYPDIKEFDKKELLAMEKEMLGLYISGHPLEEYEETLKKQTSATISDIISDE
EEDGESKLKDGDKVIIGGIITEVKRKTTRNNEMMAFLTLEDLYGTVEVIVFPKVYEKYRSLLNEDNIVLI
KGRVSLREDEEPKLICEEIEPLVINSEKKLYLRVEDKKDIKLKLKELKEILKQYPGNTPVYLYTEKERKK
FKLDRELWVNLSPELINELKELLGEENVKVV
>gnl|CDD|180714 PRK06827, PRK06827, phosphoribosylpyrophosphate synthetase; Provisional
METLPVGSLGIIALPSCRELADKVDEHLVRIRERKENENIESLAFKGYSRESYLIPAKFIRFSNGEAKGE
ILESVRGKDIYILQDVGNYSVTYNMFGEKNHMSPDDHFQDLKRTIDAIRGKARRITVIMPFLYESRQHKR
KGRESLDCALALQELEELGVDNIITFDAHDPRIENAIPLMGFENLYPSYQIIKALLKNEKDLEIDKDHLM
VISPDTGAMDRAKYYASVLGVDLGLFYKRRDYSRVVNGRNPIVAHEFLGRDVEGKDVLIVDDMIASGGSM
IDAAKELKSRGAKKIIVAATFGFFTNGLEKFDKAYEEGYFDRIIGTNLVYHPEELLSKPWYIEVDMSKLI
ARIIDALNHDVSLSKLLDPTDIIQKLLKKYNS
>gnl|CDD|180715 PRK06828, PRK06828, amidase; Provisional
MEMQFNTLLQKELTIHDIQTAMEDGKLTSKELVMYYLHRIAKYDQDGPKINSILEINPDAIFIAEALDHE
RKIKGVRGPLHGIPVLLKDNIETNDSMHTSAGTIALEQHISSEDAFLVTKLREAGAVILGKANMTELANF
MSFEMWAGYSARGGQTINPYGTGEDDMFVGGSSTGSAIAVAANFTVVSVGTETDGSILSPAVQNSVVGIK
PTVGLISRRGIIPFTYSQDTAGPFARTVTDAAILLGSLTGVDEKDVVTHKSEGIAEHDYTKYLDANGLNG
AKIGVYNNAPKEYYESGEYDEKLFKETIEVLRSEGATVVEDIDIPSFHREWSWGVLLYELKHSLDNYLSK
LPSTIPVHSISELMEFNENIAERALKYGQTKLERRKDFPNTLRNPEYLNARLEDIYFSQEQGIDFALEKY
NLDAILFPSYIGSTICAKAGYPSIAIPAGYMEGGRPFGITLASTAFSEGTLIKLAYAFEQATKHRKIPGL
S
>gnl|CDD|235869 PRK06830, PRK06830, ATP-dependent 6-phosphofructokinase
FMMKVTELDFAIETLGECKIPSPLIYSLAAGDTTHFVSDSDRVLFDVSLSLIKEEDAPGTEPPSFEKAGP
REKIYFDPSKVKAAIVTCGGLCPGLNDVIRAIVLELHHHYGVRRILGIRYGYQGLIPRYGHDPVELTPEV
VADIHEFGGTILGSSRGPQDPEEIVDTLERMNINILFVIGGDGTLRGASAIAEEIERRGLKISVIGIPKT
IDNDINFIQKSFGFETAVEKATEAIRCAHVEANGAPNGIGLVKLMGRHSGFIAAYAALASKDVNFVLIPE
VPFDLEGPNGLLAALEKRLAERGHAVIVVAEGAGQELFDDTGETDASGNPKLGDIGLFLKDRIKEYFKAR
GIPINLKYIDPSYIIRSVPANANDSVYCGFLGQNAVHAAMAGKTGMVVGRWNNRFVHLPIDLAVSKRKKV
NPEGDLWRSVLESTGQPRSMGNK
>gnl|CDD|180717 PRK06833, PRK06833, L-fuculose-phosphate aldolase
MLLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVEGE
RKPSSELDMHLIFYRNREDINAIVHTHSPYATTLACLGWELPAVHYLIAVAGPNVRCAEYATFGTKELAE
NAFEAMEDRRAVLLANHGLLAGANNLKNAFNIAEEIEFCAEIYYQTKSIGEPKLLPEDEMENMAEKFKTY
GQRK
>gnl|CDD|235870 PRK06834, PRK06834, hypothetical protein; Provisional
MTEHAVVIAGGGPTGLMLAGELALAGVDVAIVERRPNQELVGSRAGGLHARTLEVLDQRGIADRFLAQGQ
VAQVTGFAATRLDISDFPTRHNYGLALWQNHIERILAEWVGELGVPIYRGREVTGFAQDDTGVDVELSDG
RTLRAQYLVGCDGGRSLVRKAAGIDFPGWDPTTSYLIAEVEMTEEPEWGVHRDALGIHAFGRLEDEGPVR
VMVTEKQVGATGEPTLDDLREALIAVYGTDYGIHSPTWISRFTDMARQAASYRDGRVLLAGDAAHVHSPV
GGQGLNTGVQDAVNLGWKLAQVVKGTSPESLLDTYHAERHPVAARVLRNTMAQVALLRPDDRTEALRDIV
AELLGMDEPRKRIAAMMSGLDIHYDLGEGHPLLGRRMPDLDLVTADGPRRVFTLLHNARPVLLNLGAPGA
FDIAPWSDRVRLVDAKYAGPWELPVLGAVAAPAAVLIRPDGYVAWVGEGTDDGLADALTTWFGPPAAR
>gnl|CDD|235871 PRK06835, PRK06835, DNA replication protein DnaC; Validated
MIKGYISEILKEYEKRRDKEELELKNRKEEVYKKIPEIAEIDDEIAKLGIKLSRAILKNPDKKEETLKEL
KEKITDLRVKKAELLVSNGYPPDYLEMKYTCPKCKDTGFINGKKCSCYKQKLINLYYKQSNLKEILKEEN
FSNFNLNYYSDEKDDDEPLSPRKNMEKILEKCKNFIENFDKNNENLLFYGNTGTGKTFLSNCIAKELLDR
GKSVIYRTADELIEILREIRFNNDKELEEVYDLLINCDLLIIDDLGTEKITEFSKSELFNLINKRLLRQK
KMIISTNLSLEELLKTYSERISSRLLGNFTLLKFYGEDIRIKKNLQKKN
>gnl|CDD|180720 PRK06836, PRK06836, pyridoxal phosphate-dependent aminotransferase
MISEKIKGLLEKSSWIRKMFEEGARLKAEYGADNVFDFSLGNPSVPPPAAVKEALRELAEEEDPGLHGYM
PNAGYPEVREAIAESLNRRFGTPLTADHIVMTCGAAGALNVALKAILNPGDEVIVFAPYFVEYRFYVDNH
GGKLVVVPTDTDTFQPDLDALEAAITPKTKAVIINSPNNPTGVVYSEETLKALAALLEEKSKEYGRPIYL
ISDEPYREIVYDGAEVPYIFKYYDNSIVVYSFSKSLSLPGERIGYIAVNPEMEDADDLVAALVFANRILG
FVNAPALMQRVVAKCLDATVDVSIYKRNRDLLYDGLTELGFECVKPQGAFYLFPKSPEEDDVAFCEKAKK
HNLLLVPGSGFGCPGYFRLSYCVDTETIERSLPAFEKLAKEYKG
>gnl|CDD|180721 PRK06837, PRK06837, ArgE/DapE family deacylase
MMLTPDLTQRILAAVDAGFDAQVAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDRWSIDPDDLKSH
PGAGPVEIDYSGAPNVVGTYRPAGKTGRSLILQGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMK
AGLAAMLFALDALRAAGLAPAARVHFQSVIEEESTGNGALSTLQRGYRADACLIPEPTGEKLVRAQVGVI
WFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRELEAEWNARKASDPHFEDVPHPINFNVGIIKGGDWA
SSVPAWCDLDCRIAIYPGVTAADAQAEIEACLAAAARDDRFLSNNPPEVVWSGFLAEGYVLEPGSEAEAA
LARAHAAVFGGPLRSFVTTAYTDTRFYGLYYGIPALCYGPSGEGIHGFDERVDLESVRKVTKTIALFVAE
WCGVEPA
>gnl|CDD|168698 PRK06839, PRK06839, o-succinylbenzoate--CoA ligase
MQGIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLL
FAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKI
DNFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAF
PTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEEL
MREFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRG
PNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVY
EVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLV
NQLKSR
>gnl|CDD|235872 PRK06840, PRK06840, 3-oxoacyl-ACP synthase
MEMNVGIVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEKPVPGPEDHTSDMAIAAAKPALKQAGV
DPAAIDVVIYIGSEHKDYPVWSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAKDLLYSDPSIENVLL
VGGYRNSDLVDYDNPRTRFMFNFAAGGSAALLKKDAGKNRILGSAIITDGSFSEDVRVPAGGTKQPASPE
TVENRQHYLDVIDPESMKERLDEVSIPNFLKVIREALRKSGYTPKDIDYLAILHMKRSAHIALLEGLGLT
EEQAIYLDEYGHLGQLDQILSLHLALEQGKLKDGDLVVLVSAGTGYTWAATVIRWGPVK
>gnl|CDD|180723 PRK06841, PRK06841, short chain dehydrogenase; Provisional
MTDTKQFDLAFDLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDV
SDSQSVEAAVAAVISAFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGG
GKIVNLASQAGVVALERHVAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGKKAWAGEKGER
AKKLIPAGRFAYPEEIAAAALFLASDAAAMITGENLVIDGGYTIQ
>gnl|CDD|180724 PRK06842, PRK06842, Fe-S-containing hydro-lyase
MEKKITTPLTEEKVKDLKAGDSVLISGYIYTARDAAHKRLIELLDKGEELPIDIKDQIIYYVGPSPAKPG
KVIGSAGPTTSYRMDAYAPRLLDIGLKGMIGKGARSDEVIESIKKNKAVYFGAIGGAAALIAKSIKKSEV
IAYEDLGAEAIRKLEVKDFPVVVIIDSEGNNLYEIGQKEYLDSLK
>gnl|CDD|180725 PRK06843, PRK06843, inosine 5-monophosphate dehydrogenase; Validated
MPNKITKEALTFDDVSLIPRKSSVLPSEVSLKTQLTKNISLNIPFLSSAMDTVTESQMAIAIAKEGGIGI
IHKNMSIEAQRKEIEKVKTYKFQKTINTNGDTNEQKPEIFTAKQHLEKSDAYKNAEHKEDFPNACKDLNN
KLRVGAAVSIDIDTIERVEELVKAHVDILVIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALD
LISVGADCLKVGIGPGSICTTRIVAGVGVPQITAICDVYEVCKNTNICIIADGGIRFSGDVVKAIAAGAD
SVMIGNLFAGTKESPSEEIIYNGKKFKSYVGMGSISAMKRGSKSRYFQLENNEPKKLVPEGIEGMVPYSG
KLKDILTQLKGGLMSGMGYLGAATISDLKINSKFVKISHSSLKESHPHDVFNIT
>gnl|CDD|235873 PRK06846, PRK06846, putative deaminase; Validated
ITDPHYWLTNVRLETGFDYENGVIVQTETALCTLEIQDGKIVAIRPNKQVPDATLPTYDANGLLMLPAFR
EMHIHLDKTYYGGPWKACRPAKTIQDRIELEQKELPELLPTTQERAEKLIELLQSKGATHIRSHCNIDPV
IGLKNLENLQAALERYKDGFTYEIVAFPQHGLLRSNSEPLMREAMKMGAHLVGGVDPASVDGAIEKSLDT
MFQIAVDFNKGVDIHLHDTGPLGVATIKYLVETTEEAQWKGKVTISHAFALGDLNEEEVEELAERLAAQG
ISITSTVPIGRLHMPIPLLHDKGVKVSLGTDSVIDHWSPFGTGDMLEKANLLAELYRWSDERSLSRSLAL
ATGGVLPLNDEGERVWPKVGDEASFVLVDASCSAEAVARQSPRTAVFHKGQLVAGSLAGV
>gnl|CDD|235874 PRK06847, PRK06847, hypothetical protein; Provisional
MAAVKKVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVYGAGITLQGNALRALRELGVLDECLEAGF
GFDGVDLFDPDGTLLAELPTPRLAGDDLPGGGGIMRPALARILADAARAAGADVRLGTTVTAIEQDDDGV
TVTFSDGTTGRYDLVVGADGLYSKVRSLVFPDEPEPEYTGQGVWRAVLPRPAEVDRSLMYLGPTTKAGVV
PLSEDLMYLFVTEPRPDNPRIEPDTLAALLRELLAPFGGPVLQELREQITDDAQVVYRPLETLLVPAPWH
RGRVVLIGDAAHATTPHLAQGAGMAIEDAIVLAEELARHDSLEAALQAYYARRWERCRMVVEASARIGRI
EIEGGDKAEHAGLMRESMELLAQPI
>gnl|CDD|235875 PRK06848, PRK06848, cytidine deaminase
MPLNSEDYELIKAAEKVIEKRYRNDWHHVGAALRTKTGRIYAAVHLEAYVGRITVCAEAIAIGKAISEGD
HEIDTIVAVRHPKPHEDDREIWVVSPCGACRELISDYGKNTNVIVPYNDELVKVNIMELLPNKYTREVE
>gnl|CDD|235876 PRK06849, PRK06849, hypothetical protein; Provisional
MNTKKTVLITGARAPAALELARLFHNAGHTVILADSLKYPLSRFSRAVDGFYTIPSPRWDPDAYIQALLS
IVQRENIDLLIPTCEEVFYLSHAKEELSAYCEVLHFDFELLLLLHNKWEFAEQARSLGLSVPKTYLITDP
EAIRNFMFKTPHTPYVLKPIYSRFVRRVDLLPKEAALKELPISKDNPWVMQEFIQGKEYCSYSIVRSGEL
RAHSCYKPEYCAGSGAQIAFQPINHPRIEEFVTHFVKELNYTGQISFDFIETENGDAYPIECNPRTTSGL
HLFDPEVAPAYLNDKVNNAIIPLPNSEPTIWLAMLLWRLPGLRSKQKRKRWLKDLCSGPDAIYQHNDPLP
FLYQFHSLIELLLLSNLRRRKGWAASTFDIEWNGELVEL
>gnl|CDD|235877 PRK06850, PRK06850, hypothetical protein; Provisional
MSPLRQATELVEYEDGEPIEELIEEIQELYCADNRPWVIGYSGGKDSTAVLQLVWNALAGLPPEKRTKPV
YVISSDTLVENPVVVDWVNKSLERINEAAKKQGLPITPHKLTPKINDTFWVNLIGKGYPAPRRKFRWCTE
RLKIDPSNDFIKDKVSEFGEVIVVLGVRKAESAARAQVMAKHEIEGSRLSRHTTLPNAFVYTPIEDWSND
DVWKYLLQWENPWGGSNRDLFTLYRGASADGECPLVVDTSTPSCGNSRFGCWVCTVVTKDKSMEAMIQNG
EEKWMQPLLDFRNELAIPENDREYRDFRRRNGKVQLFERKDGGDISIEPIPGPYTLKYREEWLRKLLEAQ
RDVRANAPPGRDIELITLEELHEIRRIWLEEKHEWEDSLPRIYEEVTGEDLPWPGDDQSLFGSDEADLLE
ELCQEDGLHLELVRKLLDLERQYRGLSRRSGIYDKLEKILKQDWRSLEEIAQNAALLRKLKDAIHQGDIE
KIEQELQELQKQIQKSW
>gnl|CDD|235878 PRK06851, PRK06851, hypothetical protein; Provisional
MTGNVKHYFAGGNTARGFYSLYDSIIDGANRIFILKGGPGTGKSTLMKKIGEEFLEKGYDVEFLHCSSDN
DSLDGVIIPELKIAILDGTAPHVVDPKAPGAVEEIINLGDAWDEDKLRKHKEEILKINEEISRCFQRAYE
YLNEALAIHDEWEKIYIENMDFAKANELTDELIQELFKGAPGKISKGKVRHLFLGAITPKGAVDFVPSLT
EGVKNRYFLKGRPGTGKSTMLKKIAKAAEERGFDVEVYHCGFDPDSLDMVIIPELNFAIFDSTAPHEYFP
SREGDEIIDMYDELIDPGTDEKYAEEIKKAKERYKAKLNEATSFLAKAKALHDKLEEIYIPAMDFSKVDA
IKEEILERILRYAAEVV
>gnl|CDD|180731 PRK06852, PRK06852, aldolase; Validated
TRDDVKVPLDVPEEMREEYIENYLEITKGTGRLMLFAGDQKIEHLNDDFYGEGIAKDDADPEHLFRIASK
AKIGVFATQLGLIARYGMDYPDVPYLVKLNSKTNLVKTSQRDPLSRQLLDVEQVVEFKENSGLNILGVGY
TIYLGSEYESEMLSEAAQIIYEAHKHGLIAVLWIYPRGKAVKDEKDPHLIAGAAGVAACLGADFVKVNYP
KKEGANPAELFKEAVLAAGRTKVVCAGGSSTDPEEFLKQLYEQIHISGASGNATGRNIHQKPLDEAVRMC
NAIYAITVEDKSVEEALKIYNGEK
>gnl|CDD|180732 PRK06853, PRK06853, indolepyruvate oxidoreductase subunit beta; Reviewed
MMKTNILIVGVGGQGILLASKILGEAALAAGYDVKVSEVHGMSQRGGSVVSHVRFGDEVYSPLIPEGKAD
LLLAFEPLEALRYLPYLKKGGKVVVNTQPIVPVPVSLGLAKYPEDEEILEELKKLGIKVYVIDAEKIAKE
AGNIKAANVVLLGALAKFLPIDEETLEEAIKERVPPKFVEVNLKAFEAGREAAEKLA
>gnl|CDD|235879 PRK06854, PRK06854, adenylyl-sulfate reductase subunit alpha
AMANPEVVEVDTDILIIGGGMAGCGAAFEAKEWAPDLKVLIVEKANIKRSGAVAQGLSAINAYIGEGETP
EDYVRYVRKDLMGIVREDLVYDIARHVDSVVHLFEEWGLPIWKDENGKYVRRGRWQIMINGESYKPIVAE
AAKKALGDNVLNRVFITDLLVDDNRIAGAVGFSVRENKFYVFKAKAVIVATGGAAGIYRPRSPGEGRGRM
WYPPFNTGSGYAMGIRAGAEMTTFENRFIPLRFKDGYGPVGAWFLLFKAKAVNALGEEYEAKNAAELKKY
VPYADYKPIPTCLRNYATVEENKAGRGPIYMDTEEALQDKHLESELWEDFLDMTPGQALLWAAQNIEPEE
ENSEIMGTEPYIVGSHSGASGYWVSGPEDWVPEEYKWGYNRMTTVEGLFAAGDVVGGSPHKFSSGSFAEG
RIAAKAAVRYILDNKDEKPEIDDDQIEELKKEIYAPLERYEEFKDYSTDPDVNPNYISPEQLEERLQKIM
DEYAGGISTNYTTNEKLLEIALELLEMLEEDSEKLAARDLHELMRCWELKHRLLVAEAHIRHLLFRKETR
WPGYYERADYPGKDDENWKCFVNSRYDPGTGEWTIRKLPYYQIIPEHK
>gnl|CDD|180734 PRK06855, PRK06855, pyridoxal phosphate-dependent aminotransferase
MRNDIVHSGAGELTYEIRNIVAVAKKLEKLGVKITWENIGDPIAKGEKIPDWMKEIVAELVMDDKSYGYC
PTKGVLETREFLAELNNKRGGAQITPDDIIFFNGLGDAIAKIYGLLRREARVIGPSPAYSTHSSAEAAHA
GYPPVTYRLDPENNWYPDLDDLENKVKYNPSIAGILLINPDNPTGAVYPKEILREIVDIAREYDLFIICD
EIYNNIVYNGKKTVPLSEVIGDVPGIALKGISKELPWPGSRCGWIEVYNADKDEVFKKYINSILNAKMIE
VCSTTLPQMAIPRIMSHPEYKNYLKERNKRYEKRSNIAYEKLKDVPGLKVNRTNGAFYMTVVFEDGVLNN
KQSLPIENPEVKEYVEGLVKGPVSPDKRFVYYLLASTGICVVPLSSFCTELNGFRVTLLERDEEKFEWIY
QTLAEKIEEYLAS
>gnl|CDD|180735 PRK06856, PRK06856, DNA polymerase III subunit psi; Validated
MSRRDWLLQQLGITQWVLRRPGVLQGEIAISLPEHIRLVIVAEELPALTDPLLQDVLRSLTLSPDQVLCL
TPEQVAMLPQGHRCNSWLLGTDEPLSLAGAQWQSPALTELKANPTAKRALWQQICTYE
>gnl|CDD|235880 PRK06860, PRK06860, lipid A biosynthesis lauroyl acyltransferase; Provisional
MKMTNLPKFSRALLHPRYWLTWLGIGLLWLIVLLPYPVLYKLGRGLGKLALRFMKRRAKIARRNLELCFP
EMSEQEREAIVVKNFESVGMALIETGMAWFWPDWRIKRWTEVEGLEHIREVQAQGRGVLLVGVHFLTLEL
GARIFGMHNPGIGVYRPNDNPLYDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGERIWYAPDHDYGPRSS
VFVPFFAVEQAATTTGTWMLARMSKAAVIPFVPRRKPDGKGYELIILPPEDSPPLDDAEATAAWMNKVVE
KCILMAPEQYMWLHRRFKTRPEGVPSRYD
>gnl|CDD|136097 PRK06863, PRK06863, single-stranded DNA-binding protein; Provisional
MAGINKVIIVGHLGNDPEIRTMPNGEAVANISVATSESWTDKNTGERREVTEWHRIVFYRRQAEVAGEYL
RKGSQVYVEGRLKTRKWQDQNGQDRYTTEIQGDVLQMLGGRNQRNAGGYGNSGPAPQQSYQAGQTNNGNS
QQASRPAPQQAAPQAEPPMDGFDDDIPF
>gnl|CDD|180738 PRK06871, PRK06871, DNA polymerase III subunit delta'; Validated
MALYPWLQPTYQQITQAFQQGLGHHALLFKADSGLGTEQLIRALAQWLMCQTPQGDQPCGQCHSCHLFQA
GNHPDFHILEPIDNKDIGVDQVREINEKVSQHAQQGGNKVVYIQGAERLTEAAANALLKTLEEPRPNTYF
LLQADLSAALLPTIYSRCQTWLIHPPEEQQALDWLQAQSSAEISEILTALRINYGRPLLALTFLEQGLLE
QRKTFLRQFWLFYRRRSPLELLPLFDKELVLQQLDWLLAFLSDALKAKLDIASGWICQDLQRGILQFSQQ
QSAQGLLKAHQIIQKVRSDLLQINAVNQELILLDGLTRLVTEVFE
>gnl|CDD|180739 PRK06876, PRK06876, F0F1 ATP synthase subunit C; Validated
MELIMGLTAIAAAIAIGLAALGAAIGIGLLGGKFLEGAARQPELIPMLQTKMFIGAGLVDAIPIIGVGIA
LLFLFANP
>gnl|CDD|168717 PRK06882, PRK06882, acetolactate synthase 3 large subunit
MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGC
VLVTSGPGATNAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPS
TIKKAFYIASTGRPGPVVIDIPKDMVNPANKFTYEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPV
LFVGGGVITAECSEQLTQFAQKLNLPVTSSLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIG
VRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPIVGSAKNVLEEFLSLLEEENLAKSQTDLTAW
WQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQMFAALHYPFDKPRRWINSGGA
GTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGMVKQWQDLIYS
GRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKLVFVDVNVDETEHVYPMQIRGGA
MNEMILSKPEETDA
>gnl|CDD|180740 PRK06886, PRK06886, hypothetical protein; Validated
MKQLIRSLKTIIRDEVIKKGGWVNAHAHADRAFTMTPEKIAIYHYANLQQKWDLVDEVKRNSTVEDYYAR
FSQAIELMISQGVTAFGTFVDIDPICEDRAIIAAHKAREVYKHDIILKFANQTLKGVIEPTAKKWFDIGS
EMVDMIGGLPYRDELDYGRGLEAMDILLDTAKSLGKMVHVHVDQFNTPKEKETEQLCDKTIEHGMQGRVV
AIHGISIGAHSKEYRYRLYQKMREADMMVIACPMAWIDSNRKEDLMPFHNALTPADEMIPEGITVALGTD
NICDYMVPLCEGDMWQELSLLAAGCRFYDLDEMVNIASINGRKVLGLEE
>gnl|CDD|235882 PRK06895, PRK06895, anthranilate synthase component II
ATKLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENFSHILISPGPDVPRAYPQLFAMLERYH
QHKSILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSPLFDGLPEEFNIGLYHSWAVSEENFPT
PLEITAVCDENVVMAMQHKTLPIYGVQFHPESYISEFGEQILRNWLAISP
>gnl|CDD|235883 PRK06901, PRK06901, oxidoreductase
MATLNIAIAAEFELSEKLLEALEQSDLEIEQISIVEIEPFGEEQGIRFNNKAVEQIAPEEVEWADFNYVF
FAGKMAQAEHLAQAAEAGCIVIDLYGICAALANVPVVVPSVNDEQLAELRQRNIVSLPDPQVSQLALALA
PFLQEQPLSQIFVTSLLPASYTDAETVKKLAGQTARLLNGIPLDEEEQRLAFDVFPANAQNLELQLQKIF
PQLENVTFHSIQVPVFYGLAQMVTALSEYELDIESQLAEWQQNNLLRYHEEKLITPVLNGENENGEESVK
LHISQLSAVENGVQFWSVADEQRFNLAFLAVKLLELIYQQGY
>gnl|CDD|136106 PRK06904, PRK06904, replicative DNA helicase; Validated
KATTGSQQSARIKDKKTAQVLIPPHSIEAEQAVLGGIMLDNRHWDSVAERVIADDFYTFEHRIIFQEMEL
LFRQNTPIDLLTLDQALKTKGKSDEVGGFAYLAELSNNTPSAANILAYADIVREKAILRELISVGNNIAK
NAYSPKGQDIKDILDEAERDVFSIAEKRTTANEGPQNVINLLENTIDKIENLAATPTNNGVTGVTTGFTD
LDKKTAGLQPSDLIIVAARPSMGKTTFAMNLCENAAMASEKPVLVFSLEMPAEQIMMRMLASLSRVDQTK
IRTGQNLDQQDWAKISSTVGMFKQKPNLYIDDSSGLTPTELRSRARRVYRENGGLSLIMVDYLQLMRAPG
FEDNRTLEIAEISRSLKALAKELKVPVVALSQLNRTLENRGDKRPVNSDLRESGSIEQDADLIMFIYRDE
VYNETTEDNKGVAEIIIGKQRNGPIGRVRLAFQGQYSRFDNLANIPQYYDKY
>gnl|CDD|180742 PRK06911, rpsN, 30S ribosomal protein S14; Reviewed
MAKKSMLMRESKRAKLVEKYRQRRNELKQLIKSSDDFQVIMESQAKLAKLPVNSNPVRYVTRCKQCGRPH
AVYRKFNLCRICLRQQLMVGNIPGGRKSSW
>gnl|CDD|180744 PRK06914, PRK06914, SDR family oxidoreductase
MNKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNLQQNIKVQQLDVTDQNSIH
NFQLVLKEIGRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISS
ISGRVGFPGLSPYVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNTNIWEVGKQLAENQSETTSPYKE
YMKKIQKHINSGSDTFGNPIDVANLIVEIAESKRPKLRYPIGKGVKLMILAKKILPWRLWEYLVLKSLKK
>gnl|CDD|180745 PRK06915, PRK06915, peptidase
MEQLKKQICDYIESHEEEAVKLLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIWEPSFKKLKDHPYF
VSPRTSFSDSPNIVATLKGSGGGKSMILNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNV
ALLLAMEALIESGIELKGDVIFQSVIEEESGGAGTLAAILRGYKADGAIIPEPTNMKFFPKQQGSMWFRL
HVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEEKRNDRITDPLYKGIPIPIPINIGKIEGGSWPSSVPD
SVILEGRCGIAPNETIEAAKEEFENWIAELNDVDEWFVEHPVEVEWFGARWVPGELEENHPLMTTLEHNF
VEIEGNKPIIEASPWGTDGGLLTQIAGVPTIVFGPGETKVAHYPNEYIEVDKMIAAAKIIALTLLDWCEV
KK
>gnl|CDD|235884 PRK06917, PRK06917, aspartate aminotransferase family protein
MRSYLIKPLLGQPYPVISHGKGVYLYDQNGNKYFDGSSGAVTAGIGHGVKEIADAIKEQAEEVSFVYRSQ
FTSEPAEKLAKKLSDLSPGDLNWSFFVNSGSEANETAMKIAIQHFQERGIQGKHKILSRWMSYHGITMGA
LSMSGHPLRRQRFVSLLEDYPTISAPYCYRCPVQKVYPTCQLACATELETAIERIGAEHIAAFIAEPIIG
AAGAAVVPPKGYYKVIKEICDHYDILFIADEVMTGLGRTGAMFAMEHWGVEPDIMTLGKGLGAGYTPIAA
TVVSDRVMEPILRGSRSIMSGHTLSANPLSAATALAVLEYMEKHNLPEKAAEKGEYLIKGLQKVQQQSTI
IGDVRGKGLLIGVEFVADKKTKQPFSKSQAVASELISVAAKNGLLLYPAVAGQDGKEGDAVIIAPPMTIT
YSELDELLSIFAKSVEEMMQKGGHSIA
>gnl|CDD|235885 PRK06918, PRK06918, 4-aminobutyrate aminotransferase; Reviewed
NTKKFAKVNEQIPGPKAASLLERRQNIVPKGVSNGIPTFAQSANGALVTDVDGNQYIDFAGAIGTINVGH
SHPKVKEALHKQVDQYIHTGFNVMMYEPYIELAEKLAALAPGSFDKKVLFLNSGAEAVENAVKIARKYTK
RQGIISFSRGFHGRTLMTMTMTSKVKPYKFGFGPFAPEVYKAPFPYEYRRPEGLTEEQYDDFMIEEFKNF
FISEVAPETIAAVVMEPVQGEGGFIVPSKKFVQEVRNICSEHGILFVADEIQTGFARTGKYFAIEHFDVV
PDLITVSKSLGAGVPISGVIGRKEIMDESAPGELGGTYAGSPLGCAAALAVLDIIEKENLNDRAIELGKV
VMNRFEEMKNKYNCIGDVRGLGAMCAFELVQDRKTKEPDKTLTANICKEANKRGLLLLSAGTYGNVIRVL
MPLVITDEQLEEGLTIIEESLQACYEKANTA
>gnl|CDD|180749 PRK06920, dnaE, DNA polymerase III subunit alpha
MKFVHLQCQTVFSLLKSACKIDELVVRAKELGYSSLAITDENVMYGVIPFYKACKKHGIHPIIGLTASIF
SEEEEKSYPLVLLAENEIGYQNLLKISSSIMTKSKEGIPKKWLAHYAKGLIAISPGKDGEIEQLLLEDKE
SQAEEVARAYQNMFGNFYMSLQHHAIQDELLLQEKLPEFSNRVNIPVVATNDVRYINQSDALVHECLLSV
ESGTKMTDPDRPRLKTDQYYLKSSDEMEALFSHVPEAIYNTVEIAERCRVEIPFHVNQLPKFPVPSNETA
DMYLRRVCEEGLQKRYGTPKEVHINRLNHELNVISRMGFSDYFLIVWDFMKYAHENHILTGPGRGSAAGS
LVSYVLEITDIDPIEYDLLFERFLNPERVTLPDIDIDFPDTRRDEMIRYVKDKYGQLRVAQIVTFGTLAA
KAAIRDIARVMGLPPRDIDIFSKLIPSKLGITLKDAYEESQSLREFIQGNLLHERVFEIAKRVEGLPRHT
SIHAAGVIMSQEPLTGSVAIQEGHNDVYVTQYPADALEELGLLKMDFLGLRNLTLLENIIKFIEQKTGKE
IDIRNLPLQDEKTFQLLGRGDTTGVFQLESSGMRNVLRGLKPNEFEDIVAVNSLYRPGPMEQIPTFIESK
HGKRKIEYLHPDLKPILERTYGVIVYQEQIMQIASKLAGFSLGEADLLRRAVSKKNRDILDQERKHFVQG
CLQNGYDETSAEKIYDLIVRFANYGFNRSHAVAYSMIGYQLAYLKANYTLEFMTALLSSAIGNEDKIVQY
IRETKRKGFHVLPPSLQRSGYNFQIEGNAIRYSLLSIRNIGMATVTALYEEREKKMFEDLFEFCLRMPSK
FVTERNLEAFVWSGCFDDFGVSRTNLWKSLKGALEYANLARDLGDAVPKSKYVQGEELSFIEQLNKEKEV
LGFYLSSYPTAQYVKLAKELEIPSLAQAMRHKKKVQRAIVYITSVKVIRTKKGQKMAFITFCDQNDEMEA
VVFPETYIHFSDKLQEGAIVLVDGTIELRNHKLQWIVNGLYPLEEMDAYEEKKDASVYVKLPSQYEKKLL
NQVTKILFDYSGFAKVLIYYEKEHKMVQLSRSLSIHPSEECLGALREIVGEENVVVK
>gnl|CDD|180750 PRK06921, PRK06921, hypothetical protein; Provisional
MTKRTIEEKAAELLMRERPSTTTKPEESDAERYDCPKCKDRGIIIYRRNTAEVWRQCECVEQRKIERLLK
ASEITEAFRKLTFKNFKTEGKPQAIKDAYECAVEYVKDFEKIQESRKNSIALLGQPGSGKTHLLTAAANE
LMRKKGVPVLYFPFVEGFGDLKDDFDLLEAKLNRMKKVEVLFIDDLFKPVNGKPRATEWQIEQMYSVLNY
RYLNHKPILISSELTIDELLDIDEALGSRIVEMCKDYLVIIKGDSFELNHRLEGER
>gnl|CDD|180751 PRK06922, PRK06922, class I SAM-dependent methyltransferase
RLKSIEVLNTYIEGDSVAIPTWLKHLIEAEEIHQNYENVQVLGALKTDAVLYYVHRTLQVLDGLSLDEEA
YRIIEKVLTYSELAKVGSLKQREQWKKKGINLLVHNEGSADIFSDIQFIERVETNLNSTEYLFIQDLIRT
HGLIGQYIRGEARLDSHVPLINTYKEEYGDVRLKEILYYLNQCIIEGVSKALWSEVKNDVKITIDGLFDG
YMEPFTSRIHRLTPKHKESAFEKDIIMGSEKSDVQTFLSDKDLWYVEPSMHALSFEDIWTVFVMLKNEIG
TRKVQHIHFEKLMQQLHYDFKGEKKDNVYRKRVIEKYLREYRENEKPNTTHVSFQVKVDEDMKTAYVSFR
FSAVGEALITFCVEAEKIDMMHARANVLLFDFFGLRKDAYDRFHNEEVYLEHMNSSADDKRIILDYIKGD
TIVDVGAGGGVMLDMIEEETEDKRIYGIDISENVIDTLKKKKQNEGRSWNVIKGDAINLSSSFEKESVDT
IVYSSILHELFSYIEYEGKKFNHEVIKKGLQSAYEVLKPGGRIIIRDGIMTEDKRLMRVIRFKDAGGMKF
LEQYVQEFKGRIIQYEVLADNTVKMPVNDAMEFLYTYTWGEDSFVHEVQEQFGIFTPNDYKDFVKGIFGD
KVNIVQAMNYLQDGYTNHLSEKIEFTDESGNAVALPDSTFFMVLEKR
>gnl|CDD|235886 PRK06923, PRK06923, isochorismate synthase DhbC; Validated
MNEFTAVKELSEKLLEDYKTESSFFFASPTRTILAEGEFTTVKHHEIESFPERVQAVLRNAKQAGNPNPI
VVGALPFDRRKEVQLIVPEYSRISERLQLDTTNHLEINRNLTFEMTPVPDPEVYMNGVKQGIAKIQDGDL
KKIVLSRSLDVKSSEKIDKQKLLRELAEHNKHGYTFAVNLPKDENENSKTLIGASPELLVSRHGMQVISN
PLAGSRPRSDDPVEDKRRAEELLSSPKDLHEHAVVVEAVAAALRPYCHTLHVPEKPSVIHTEAMWHLSTE
VKGELKDPNTSSLELAIALHPTPAVCGTPTEEAREAIQQIEPFDREFFTGMLGWSDLNGDGEWIVTIRCA
EVEENTLRLYAGAGVVAESKPEDELAETSAKFQTMLKAMGLNDSSLNEK
>gnl|CDD|180753 PRK06924, PRK06924, (S)-benzoin forming benzil reductase
MRYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEI
LSSIQEDNVSSIHLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVDKRVINIS
SGAAKNPYFGWSAYCSSKAGLDMFTQTVATEQEEEEYPVKIVAFSPGVMDTNMQAQIRSSSKEDFTNLDR
FITLKEEGKLLSPEYVAKALRNLLETEDFPNGEVIDIDEYL
>gnl|CDD|235887 PRK06925, PRK06925, flagellar motor protein MotB
MERRKRQQSKGSPKWMVTFSDLITLILVFFILLFSMSQIDAQKFKAAVESFQQRGSLGFLPSAIEFENPA
ESSEDEEKQEDQLDELLKKVNEYIEENELKSVITAKRDERGVVLVLQEAVLFETGEADILKQAEPFLHKI
GVLLSTIPNDIKVEGHTDSRPISTYRYPSNWELSAARASSVIRYFTSKEKLDSSRFIAVGYADTKPVVPN
TTEENMQENRRVEIVISDPT
>gnl|CDD|180755 PRK06926, PRK06926, flagellar motor protein MotP; Reviewed
MKKFDYLTPVGIFLGITIVVLGVISNSGLSGFLSFIDLTSILIVTGGLCAALFISFSPKDLKLAPRVLKQ
AFQSQEDDVEELVQTFVSLSEKARREGLLSLEAELEEVKDPFIKKGLLLAIDGWEPETIRDIMMAEIAAM
EERHRKGRRIFEKAGEYAPAWGMIGTLVGLVLMLKNLNDPSTLGPNMAIALLTTLYGTLLANLVFLPIAA
KLEEKTEEEVFVKQVIIEGVIGVQSGQNPRILEEKLSVFSSKEDWTKEEEDRKKKEEVHEA
>gnl|CDD|235888 PRK06928, PRK06928, pyrroline-5-carboxylate reductase; Reviewed
MEKIGFIGYGSMADMIATKLLETEVATPEEIILYSSSKNEHFNQLYDKYPTVELADNEAEIFTKCDHSFI
CVPPLAVLPLLKDCAPVLTPDRHVVSIAAGVSLDDLLEITPGLQVSRLIPSLTSAVGVGTSLVAHAETVN
EANKSRLEETLSHFSHVMTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRNSSLSDEEAFQFLNFALA
GTGKLLVEEDYTFSGTIERVATKGGITAEGAEVIQAQLPQFFDELLDRTQKKYASSKKEIQAQKRDL
>gnl|CDD|180757 PRK06930, PRK06930, positive control sigma-like factor; Validated
MQDLLKEYKRTLKQLRKMYKDAQEEIDEQLKDKKIIRSMISDLEYVIEWMEKGRQPGNRRGIDRRAAYQR
EVICDPLLIQRYFRSMEDLEWDIEEPESVISEWDKIRIEDALSVLTEREKEVYLMHRGYGLSYSEIADYL
NIKKSTVQSMIERAEKKIARQINESLFCMA
>gnl|CDD|235889 PRK06931, PRK06931, diaminobutyrate--2-oxoglutarate transaminase
MTDKVRIDLLGAQATNATNETYLARQAEFESNVRSYPRKLPLAIAKAQGVWVTDVEGNQYLDCLAGAGTL
ALGHNHPDVLQSIQDVLTSGLPLHTLDLTTPLKDAFSEYLLSLLPGQGKEYCLQFTGPSGADAVEAAIKL
AKTYTGRSNVISFSGGYHGMTHGALAVTGNLSPKNAVNGLMPGVQFMPYPHEYRCPLGIGGEAGVKALTY
YFENFIEDVESGVRKPAAVILEAIQGEGGVNPAPVEWLQKIREVTQKHGILLIVDEVQAGFARTGKMFAF
EHAGIEPDIIVMSKAVGGGLPLAVLGIKKEFDAWQPGGHTGTFRGNQLAMATGLTTLKILKEENLAQNAA
ERGEWLKAQLAELQKRYPCIGNVRGRGLMIGIEIVDERQPADAMGSYPADGELAAAIQKACFENGLLLER
GGRNGNVVRLLPPLLITQAECEEFIDRFEQALLAAVKAV
>gnl|CDD|235890 PRK06932, PRK06932, 2-hydroxyacid dehydrogenase
MMKIVFLDSTAIPKHINIPRPSFPHEWIEYDHTSAEQTIERAKDADIVITSKVLFTRETLAQLPKLKLIA
ITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHVLGMIFALKHSLMGWYRDQLSDRWATCKQFCYFDY
PITDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLYAEHKGASVCREGYTPFEEVLKQADIVTLHCPLTET
TQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEPPEKDNPLIQAAKRLPN
LLITPHIAWASDSAVTTLVNKVAQNIEEFVQQGK
>gnl|CDD|235891 PRK06933, PRK06933, YscQ/HrcQ family type III secretion apparatus protein
MSLLTLPKASLSELSLRQRLSHYQQHFLWEEGKLSLTVSQPPSSLDCILQLQWKGQTFTLYCFGADLANW
LAPDLQGAAFFSLPKELQLALLERQTVFLPKLVCNDLATASLSVTQPLLSLRLSRDNASLSLWLTSPEAL
LALLPPRPSSERLPIPLLLSLQWGKVYLTLDEFDSLELGDVLLAPEGSGPNSPVLAYVEGRPWAYCQLQS
NKLELIGMHTESNDLNPEPLLTDLNQLPVQVSFEVGRQTLDLHTLTSLQPGSLIDLTTPVDGEVRLLANG
RLLGHGRLVEIQGRLGVRVERLFGVTQS
>gnl|CDD|180760 PRK06934, PRK06934, flavodoxin; Provisional
MNKLRFTSLTKHLILFLAVAVSSLSLIAEAADRNARRVLIVYFSQPEDVKLEGVDGVSGASILQKNGEVL
GSTQYVAQIIQEETGGDLFRIETVKPYPRQHDPLLKYAEQEVKEGGRPEMREKIQNLADYDQIFIGYPIW
WYKMPMVMYSFFEQHDFSGKTLIPFTTHGGSRFSDSLREIKRLQPNAQLVTQGLAISRNDVTDDDTPKEI
INWLNTLPNMP
>gnl|CDD|180761 PRK06935, PRK06935, 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD
MELDKFSMDFFSLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDETRRLIEKEGRKVTFVQV
DLTKPESAEKVVKEALEEFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQ
GSGKIINIASMLSFQGGKFVPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIRADKNR
NDEILKRIPAGRWGEPDDLMGAAVFLASRASDYVNGHILAVDGGWLVR
>gnl|CDD|180762 PRK06936, PRK06936, EscN/YscN/HrcN family type III secretion system ATPase
MLSLDYIPHHLRHAIVGSRLIQIRGRVTQVTGTILKAVVPGVRIGELCYLRNPDNSLSLQAEVIGFAQHQ
ALLTPLGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRR
LIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGREVREFIESD
LGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPT
RRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPA
IDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEYQKGQDKEADQAIERIGAIRGFLRQG
THELSHFNETLNLLETLTQ
>gnl|CDD|180763 PRK06937, PRK06937, HrpE/YscL family type III secretion apparatus protein
MLPFVRLNASNLSLAPGLRVLRAEDYQSLLSAEELVEAARQRAEEIEAEAQEVYEQQKQLGYQAGLDEAR
TEQAELILETVLQCQEFYRGVEQQMSEVVLEAVRKILNDYDDVERTLQVVREALALVSNQKQVVVRVNPD
QAAAVREQIAKVLKDFPEVGYLEVVADARLDQGGCILETEVGIIDASLDGQLEALEQAFHSTIG
>gnl|CDD|235892 PRK06938, PRK06938, diaminobutyrate--2-oxoglutarate aminotransferase; Provisional
TSLIESSPLRAPAAAMETLYEFSNSPLLERQSRRESNARSYPRRIPLALKRARGIYVEDVEGRQFIDCLA
GAGTLALGHNHPVVIEAIQQVLADELPLHTLDLTTPVKDQFVQDLFASLPEAFAREAKIQFCGPTGTDAV
EAALKLVKTATGRSTVLSFQGGYHGMSQGALSLMGNLGPKKPLGALLPGVQFLPYPYDYRCPFGLGGEAG
VRANLHYLENLLDDPESGVVLPAAVILEVVQGEGGVIPAPIEWLRGLRRITEEAGIPLIVDEIQSGFGRT
GKMFAFEHAGIIPDVVVLSKAIGGSLPLAVVVYREWLDTWQPGAHAGTFRGNQMAMAAGSATLRYIKEHR
LAEHAAAMGERLREHLRQLQRDYPQLGDVRGRGLMLGVEIVDPQGEPDALGHPPANGELASLIQRECLRR
GLILELGGRHGSVVRFLPPLIITAEQIDEVAEIFAEAVAAAVAK
>gnl|CDD|235893 PRK06939, PRK06939, 2-amino-3-ketobutyrate coenzyme A ligase; Provisional
MSGAFYAQLREELEEIKAEGLYKEERVITSPQGADITVADGKEVINFCANNYLGLANHPELIAAAKAALD
SHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASII
DGVRLCKAKRYRYANNDMADLEAQLKEAKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVD
DSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPA
IVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEEGV
YVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI
>gnl|CDD|180766 PRK06940, PRK06940, short chain dehydrogenase; Provisional
MKEVVVVIGAGGIGQAIARRVGAGKKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAAT
AQTLGPVTGLVHTAGVSPSQASPEAILKVDLYGTALVLEEFGKVIAPGGAGVVIASQSGHRLPALTAEQE
RALATTPTEELLSLPFLQPDAIEDSLHAYQIAKRANALRVMAEAVKWGERGARINSISPGIISTPLAQDE
LNGPRGDGYRNMFAKSPAGRPGTPDEIAALAEFLMGPRGSFITGSDFLVDGGATASYRYGPLKPE
>gnl|CDD|235895 PRK06945, flgK, flagellar hook-associated protein FlgK; Validated
SSSLLNIGLSGLNAAQWGLTTTGHNISNAATPGYSRQRVVQAEAGGQYTGSGYLGQGVNVVTVKRQYSQY
LSAQLNNAQAASSSLSTYYSQISQLNNYLADPTAGLSPAITSFFTGLQNVANNPSDPSARQTMLSNAQTL
ASQFNAAGQQLDQLRQSVNTQLTSSVTQINSYTKQIAQLNDQIAKAESSQGQPPNDLLDQRDQLVSELSK
LVGVTVVQQDDGGYNVFVGNGQPLVVGNQSYQLTTVPSPSDPSRLTVAGYKPPGTTQELPDSSLTGGTLG
GLLAFRSQTLDPAQNQLGRLAASLAAQFNAQNALGIDLNGNLGGDLFSVAGPTVYANANNTGSATLTASI
TNASALTTSDYTLSYDGTNYTLTRLSDGSVVGTATSLPTPPPTTIDGLSLSLSGTMNAGDSFLVQPTRNA
ANGFSVATTDGSAIAAASPVRASAGSTNTGTGAISQGSVSSGYPLPSGTTTLTYDAATGTLSGFPAGTTV
TVAGTPPTSVTITPATTPVPYTSGAGISLVFNGVSVTLSGTPADGDTFTIGPNTGGTNDGRNALALAKLQ
NAKTLDGGTATYTGAYAQLVNQVGNKASQLKVSSAAQTALLGQITAAQQSVSGVNLDEEAANLLRYQQAY
QANAKVIQTASTLFDTLLGIF
>gnl|CDD|180770 PRK06946, PRK06946, lipid A biosynthesis lauroyl acyltransferase; Provisional
LGRLGTALAIGLLKLLAFLPYGLTARFGDGLGWLLYRIPSRRRRIVHTNLKLCFPDWSDARREELARRHF
RHVIRSYVERSVQWFGSEKKLEKLVQVDSAIDLTDPDGPPTIFLGLHFVGIEAGSIWLNYSLRRRVGSLY
TPMSNPLLDAIAKAARGRFGAEMVSRADSARQVLRWLRDGKPVMLGADMDFGLRDSTFVPFFGVPACTLT
AVSRLARTGGAQVVPFITEVLPDYKGYRLRVFKPWENYPTGDDDLDARRMNAFLEEQIRLMPEQYYWVHK
RFKTRPPGEPSVY
>gnl|CDD|180771 PRK06947, PRK06947, SDR family oxidoreductase
MRKVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAM
FDAVQSAFGRLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRGGAIVN
VSSIASRLGSPNEYVDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASGGQPGRAARLGAQ
TPLGRAGEADEVAETIVWLLSDAASYVTGALLDVGGGR
>gnl|CDD|180772 PRK06948, PRK06948, ribonucleotide reductase-like protein; Provisional
DSFVRMIGDMDEQPICDAVFADRYALPGETSRAQVFARVARALALAEPPDTRAGAARRFYRNLLNGAIGA
GRIMANAGAAPDQTMVNCFVHPIRAPAALTAVHPNLDRALDDARLTLLMGGGIGYDFSAIPPADARPDAD
HPDSPGVCAALDRFDRICAALPFRDGRRGAQMAVLRCDHPDLLAFVAAKRGRARWTTFNLSVAVTDAFMQ
AVAQDLPWALRHRAPPRRAAGGALRGADGAWTYATVPARHLWREIVSAARDSAEPGLLFVDTIDAANPLR
EHERIDATNPCGEQPLPPYGSCVLGPIDLSRFVRHPFGVGGEPRFDFAALATAVRIQVRMLDNALDLTRW
PLAAHAREARQKRRIGVGVTGLADALTMMRLRYDSPAAREMARYIASDLRHHAYAASAALAAERGAYPLC
DPAAHLDALRAGPPLPHAVCHAIARHGLRNSHLLSFAPVGSVSLAFGDNCSPGIEPARAWIEHRPVRAGA
GGARGMRAENHAYRLFRSLRGERAALPDYFVTAADVAPADHLAMRAALQPYVDAGISKTVTLPNHYSLAE
VDALLFQAWRAGLKGITIFRPDPALDAVPSDDDAV
>gnl|CDD|180773 PRK06949, PRK06949, SDR family oxidoreductase
MGRSINLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDY
QSIKAAVAHAETEAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAG
NTKPGGRIINIASVAGLRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWET
EQGQKLVSMLPRKRVGKPEDLDGLLLLLAADESQFINGAIISADDGFG
>gnl|CDD|180774 PRK06953, PRK06953, SDR family oxidoreductase
MKTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGAEALALDVADPASVAGLAWKLDGEA
LDAAVYVAGVYGPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIGDATG
TTGWLYRASKAALNDALRAASLQARHATCIALHPGWVRTDMGGAQAALDPAQSVAGMRRVIAQATRRDNG
RFFQYDGVELSW
>gnl|CDD|180775 PRK06954, PRK06954, acetyl-CoA C-acetyltransferase
MTAVDQDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAP
ARQAALGAGLPLSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMG
HGQVLDHMFLDGLEDAYDKGRLMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTV
AGKKGDTVIDRDEQPFKANPEKIPTLKPAFSKTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARV
VGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGLPHEKVNVNGGACA
LGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIELI
>gnl|CDD|235896 PRK06955, PRK06955, biotin--[acetyl-CoA-carboxylase] ligase
MNAATPSSTPASGDWRIDRDRLDAHLAAAARAWPLEIVEETGSTNADLMARLKALPRSADALPAPIVRVA
YEQTAGRGRQGRPWFAQPGNALLFSVACVLPRPVAALAGLSLAVGVALAEALAALPAALGQRIALKWPND
LLIAGRKLAGILIETVWATPDATAVVIGIGLNVRRADAVAAEVDALRAREAALARGLPPVALAAACAGAN
LTDTLAAALNALAPALQAFGADGLAPFAARWHALHAYAGREVVLLEDGAELARGVAHGIDETGQLLLDTP
AGRQAIAAGDVSLREADAAR
>gnl|CDD|180777 PRK06958, PRK06958, single-stranded DNA-binding protein; Provisional
MASVNKVILVGNLGADPEVRYLPSGDAVANIRLATTDRYKDKASGEFKEATEWHRVAFFGRLAEIVGEYL
KKGSSVYIEGRIRTRKWQGQDGQDRYSTEIVADQMQMLGGRGGSGGGGGGGDEGGYGGGGGGGGGGYGGE
SRSGGGGGRASGGGGGGAGGGASRPSAPAGGGFDEMDDDIPF
>gnl|CDD|235898 PRK06964, PRK06964, DNA polymerase III subunit delta'; Validated
MLYPWQTDDWNRLQALRARLPHALLLHGQAGIGKLDFAQHLAQGLLCETPQPDGEPCGTCAACNWFAQGN
HPDYRIVRPEALAAEAPGAADEAKEADADEGGKKTKAPSKEIKIEQVRALLDFCGVGTHRGGARVVVLYP
AEALNVAAANALLKTLEEPPPGTVFLLVSARIDRLLPTILSRCRQFPMTVPAPEAAAAWLAAQGVADADA
LLAEAGGAPLAALALASDENRPLRDWTLGQLAAGAACDAFACAETLQKLPVPAVLGWLQRWLYDLLAQRL
AGAPRYFPAQRAALARCAAAVDANALARFAKAVTRQRAVENHPLAARLVFEELFLGYRELFA
>gnl|CDD|180780 PRK06965, PRK06965, acetolactate synthase 3 catalytic subunit; Validated
MNMPSAEFSTAESLSPPAADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQA
AVHAADGYARATGKVGVALVTSGPGVTNAVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITR
PIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPKDVSKTPCEYEYPKSVEMRSYNPVTKGHSGQ
IRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMGLGAYPASDKKFLGMLGMHGTYE
ANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPRKIIHIDIDPSSISKRVKVDIPIVGDVKEVLKELIEQ
LQTAEHGPDADALAQWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQMWAAQ
FYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLN
NRYLGMVRQWQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRLKDRTVFLDFQ
TDPTENVWPMVQAGKGITEMLLGSEDL
>gnl|CDD|180781 PRK06973, PRK06973, nicotinate-nucleotide adenylyltransferase
RAAAPQGPTPNAEPAPPLARPRRIGILGGTFDPIHDGHLALARRFADVLDLTELVLIPAGQPWQKADVSA
AEHRLAMTRAAAASLVLPGVTVRVATDEIEHAGPTYTVDTLARWRERIGPDASLALLIGADQLVRLDTWR
DWRRLFDYAHLCAATRPGFDLGAASPAVAAEIAARQADADVLQATPAGHLLIDTTLAFDLSATDIRAHLR
ACIARRAQVPDASAEHVPAAVWAYILQHRLYHR
>gnl|CDD|235899 PRK06975, PRK06975, bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
ARAFTVVVTRPDGQSAALAAQLAAAGLDVLDFPLLDIAPVADDAPLRAALARLSDYALVVFVSPNAVDRA
LARLDAIWPHALPVAVVGPGSVAALARHGIAAPAHRVIAPDAPADGGEARYDSEALFAEIDAAFGALAGK
RVLIVRGDGGREWLAERLREAGAEVELVEAYRRVVPEPSIGAWERVHALLSGAPHAWLLTSSEAVRNLDE
LARAHLNPAEIDALKHAPLVAPHARIAEQARALGFDRITLTGAGDERIVRAFLTWADAAAQPATAAPAPS
RMTDTNDSKSVTSQPAAAAAAPAPPPNPPATPPEPPARRGRGSAALWFVVVVLACAAAVGGYALNRKVDR
LDQELVQRQQANDAQTAELRVKTEQAQASVHQLDSQFAQLDGKLADAQSAQQALEQQYQDLSRNRDDWMI
AEVEQMLSSASQQLQLTGNVQLALIALQNADARLATSDSPQAVAVRKAIAQDIERLKAAPSADLTGLAIK
LDDAIAKIDALPLSGEALPPHATMAAAPAAAAAAAAAAAAAGEPRWKAWWRRFSAGVGEQLKQLVQVRRI
DNADAMLLSPDQGYFLRENLKLRLLNARLSLLSRNDAAFKSDLHAAQAALARYFDTASKDTQTVQDLLKQ
VDAASLTVAVPNLNTSLAAVQQFKKR
>gnl|CDD|235901 PRK06986, fliA, flagellar biosynthesis sigma factor; Validated
AYTAEGKMDQDELVEQYAPLVKRIALRLKARLPASVDLDDLIQAGMIGLLEAARRYDGEQGASFETYAGQ
RIRGAMLDELRSLDWVPRSVRRNAREVAQAIRQLEQELGREPTDTEVAEKLGLSLEEYREMLLDTNISQL
FSIDELRGEHGDSILVTEDHQDEDPLQQLEDEELREALVEAIESLPEREQLVLSLYYQEELNLKEIGAVL
GVSESRVSQIHSQAIKRLRARLGEWT
>gnl|CDD|235902 PRK06988, PRK06988, formyltransferase
MKPRAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDNPTENIWFGSVAAVAAEHGIPVITPADPNDPELR
AAVAAAAPDFIFSFYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAK
PDAGAIVDQTAVPILPDDTAAQVFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLAQGSYFGGRKPEDGRI
DWSKPAAQVYNLIRAVAPPYPGAFTDLGGTRFVVARARLAAPGAAAARDLPPGLHVSDNALFGVCGDGRA
VSILELRRQQDGGETVVTPAQFAQFIHSSRHS
>gnl|CDD|235903 PRK06991, PRK06991, electron transport complex subunit RsxB
MTDSKTLADRIEDLLPQTQCTKCGYDGCRPYAEAIAAGEANYNRCPPGGAEGIARLAALLGKPVIPLDPA
NGVERPRAVAVIDEQLCIGCTLCMQACPVDAIVGAPKQMHTVLADLCTGCDLCVPPCPVDCIDMVPVTGE
RTGWDAWSQAQADAARARHDARQARLRREREAAEARAAARAAASAAAAAAEASAAAAPAADDAEAKKRAI
IAAALERARKKKEELAAQGAGPKNTEGVSAAVQAQIDAAEARRKRLAEQRDAPDDANADG
>gnl|CDD|235904 PRK06995, flhF, flagellar biosynthesis protein FlhF
MNIKKFFGKTSRDALRLVREALGADAVILSNRAVDGGVEIVALADSDLAALAPPAAAAPAAAQPPPAAAP
AAVSRPAAPAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRLARAAAAAP
RPRVPADAAAAVADAVKARIERIVNDTVMQELRSLRGMLEEQLASLAWGERQRRDPVRAALLKHLLAAGF
SAQLVRMLVDNLPEGDDAEAALDWVQSALAKNLPVLDSEDALLDRGGVFALMGPTGVGKTTTTAKLAARC
VMRHGASKVALLTTDSYRIGGHEQLRIYGKILGVPVHAVKDAADLRLALSELRNKHIVLIDTIGMSQRDR
MVSEQIAMLHGAGAPVKRLLLLNATSHGDTLNEVVQAYRGPGLAGCILTKLDEAASLGGALDVVIRYKLP
LHYVSNGQRVPEDLHLANKKFLLHRAFCAPRDASPFVPQDDELPLLLAALTARSGAELHEVRFG
>gnl|CDD|235905 PRK06996, PRK06996, UbiH/UbiF/VisC/COQ6 family ubiquinone biosynthesis hydroxylase
MTTAASMAAPDFDIAIVGAGPVGLALAGWLARRSATRALSIALIDAREPAASANDPRAIALSHGSRVLLE
TLGAWPADATPIEHIHVSQRGHFGRTLIDRDDHDVPALGYVVRYGSLVAALARAVRGTPVRWLTSTTAHA
PAQDADGVTLALGTPQGARTLRARIAVQAEGGLFHDQKADAGDSARRRDYGQTAIVGTVTVSAPRPGWAW
ERFTHEGPLALLPLGGPRQADYALVWCCAPDEAARRAALPDDAFLAELGAAFGTRMGRFTRIAGRHAFPL
GLNAARTLVNGRIAAVGNAAQTLHPVAGQGLNLGLRDAHTLADALSDHGATPLALATFAARRALDRRVTI
GATDLLPRLFTVDSRPLAHLRGAALTALEFVPPLKHALARQMMFGQRR
>gnl|CDD|180789 PRK06997, PRK06997, enoyl-[acyl-carrier-protein] reductase FabI
MGFLAGKRILITGLLSNRSIAYGIAKACKREGAELAFTYVGDRFKDRITEFAAEFGSDLVFPCDVASDEQ
IDALFASLGQHWDGLDGLVHSIGFAPREAIAGDFLDGLSRENFRIAHDISAYSFPALAKAALPMLSDDAS
LLTLSYLGAERVVPNYNTMGLAKASLEASVRYLAVSLGPKGIRANGISAGPIKTLAASGIKDFGKILDFV
ESNAPLRRNVTIEEVGNVAAFLLSDLASGVTGEITHVDSGFNAVVGGMAG
>gnl|CDD|235906 PRK07003, PRK07003, DNA polymerase III subunit gamma/tau
MTYQVLARKWRPKDFASLVGQEHVVRALTHALDGGRLHHAYLFTGTRGVGKTTLSRIFAKALNCETGVTS
QPCGVCRACREIDEGRFVDYVEMDAASNRGVDEMAALLERAVYAPVDARFKVYMIDEVHMLTNHAFNAML
KTLEEPPPHVKFILATTDPQKIPVTVLSRCLQFNLKQMPAGHIVSHLERILGEERIAFEPQALRLLARAA
QGSMRDALSLTDQAIAYSANEVTETAVSGMLGALDQTYMVRLLDALAAGDGPEILAVADEMALRSLSFST
ALQDLASLLHRIAWAQFAPASVLDEWPEAADLRRFAELLSPEQVQLFYQIATVGRGELGLAPDEYAGFTM
TLLRMLAFEPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAA
TRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAF
EPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAAAALDVLRNAG
MRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPRARAATGDAPPNGAARAEQAAESRGAPPPWE
DIPPDDYVPLSADEGFGGPDDGFVPVFDSGPDDVRVAPKPADAPAPPVDTRPLPPAIPLDAIGFDGEWPA
LAARLPLKGVAYQLAFNSELTAADGGTLKLAVPVPQYADAAQVAKLKAALADALGKPVEVAVEVGPARRT
AAALDAAERAKRQREAEQEIHADPFVQQLLREFGASIVEGSIRPVAAEAGAPDGASPTLH
>gnl|CDD|235907 PRK07004, PRK07004, replicative DNA helicase; Provisional
MNAPADPQLESLKVPPHSIEAEQSVLGGLLLDNAAWDRIADFLSQSDFYRYDHRIIFEHIGRLIAATRPA
DVITVYEALTTSGKAEEVGGLAYLNALAQNTPSAANIRRYAEIVRDRAVLRRLVSVADEISADAFNPQGK
EVRQLLDEAESKVFSIAEEGARGTQGFLEIGPLLTQVVERIDTLYHTANPSDVTGTPTGFVDLDRMTSGM
HGGELIIVAGRPSMGKTAFSMNIGEYVAVEYGLPVAVFSMEMPGTQLAMRMLGSVGRLDQHRMRTGRLTD
EDWPKLTHAVQKMSEAQLFIDETGGLNPMELRSRARRLARQCGKLGLIIIDYLQLMSGSSQGENRATEIS
EISRSLKSLAKELDVPVIALSQLNRGLEQRPNKRPVMSDLRESGAIEQDADVILFIYRDEVYNPDSPDKG
TAEIIIGKQRNGPIGPVRLTFLGQYTKFDNFAGAQNFYGE
>gnl|CDD|180792 PRK07006, PRK07006, isocitrate dehydrogenase; Reviewed
PAEGEKITVNNGKLNVPNNPIIPFIEGDGIGPDITPAMLKVVDAAVEKAYKGERKISWMEIYAGEKATKV
YGEDVWLPEETLDLIREYRVAIKGPLTTPVGGGIRSLNVALRQELDLYVCLRPVRYFKGVPSPVKRPEDT
DMVIFRENSEDIYAGIEWKAGSAEAKKVIKFLQEEMGVKKIRFPETSGIGIKPVSEEGTERLVRAAIEYA
IDNDRKSVTLVHKGNIMKFTEGAFKDWGYQLAEEEFGDELIDGGPWDKIKNPETGKEIIVKDSIADAFLQ
QILLRPAEYDVIATMNLNGDYISDALAAQVGGIGIAPGANINDGHAIFEATHGTAPKYAGLDKVNPGSVI
LSAEMMLRHMGWTEAADLIIKSMEKTIASKTVTYDFARLMEGATEVKCSEFGDALIKNM
>gnl|CDD|235908 PRK07008, PRK07008, long-chain-fatty-acid--CoA ligase; Validated
LLGQMMDMPLLISSLIAHAARHAGDTEIVSRRVEGDIHRYTYRDCERRAKQLAQALAALGVEPGDRVGTL
AWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLTFLPLVDALAPQCPNVKGWVA
MTDAAHLPAGSTPLLCYETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRSTVLHAYGAAL
PDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPGPDLDGKSLYELIEAERVTFSAGVPTVWLG
LLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKLKWKHSQLPLDE
QRKLLEKQGRVIYGVDMKIVGDDGRELPWDGKAFGDLQVRGPWVIDRYFRGDASPLVDGWFPTGDVATID
ADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREE
LLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRDYVLPTA
>gnl|CDD|180794 PRK07018, flgA, flagellar basal body P-ring formation protein FlgA
MMLTLKRLLAIIALLFSALSAAAAATQQSPEAISEQAEQFLEQQLEAGLPGKVSVTVATLDPRLRLPACD
QLEASLPSNARLWGNVTVGVRCGGPYPWTVYVPVRVQVTGPYVVAARPLARGEKLSASDVTLREGDLDTL
PPGVFTDPDQLVGAVSKRRIAPGQPIRLNMLRQAWVVCKGQTVSIIARGDGFSVKTEGEALNDGAVGQQI
RVRNMASGQVVSGIVTGDGEVEVNL
>gnl|CDD|235909 PRK07021, fliL, flagellar basal body-associated protein FliL; Reviewed
AMSDSAIPPAKSGKKRKLWLIILILLLLAAAAGAGYSWWLSKEQATAAAKAAPAPPPAPVFFPLETFTVN
LQPDDDADRVLYVGLTLRLPDEATRERLKDYLPEVRSRLLLLLSRKHAAELATEEGKQKLAAEIKQTLSQ
PLVPGQPPQVVTDVLFTAFILQ
>gnl|CDD|180796 PRK07023, PRK07023, SDR family oxidoreductase
AVRAIVTGHSRGLGAALAEQLLQPGIAVLGVARSRHPSLAAAAGERLAEVELDLSDAAAAAAWLAGDLLA
AFVDGASRVLLINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAA
RNAYAGWSVYCATKAALDHHARAVALDANRALRIVSLAPGVVDTGMQATIRATDEERFPMRERFRELKAS
GALSTPEDAARRLIAYLLSDDFGSTPTADIRNL
>gnl|CDD|235910 PRK07024, PRK07024, SDR family oxidoreductase
MPLKVFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARVSVYAADVRDADALAAAAA
DFIAAHGLPDVVIANAGISVGTLTEEREDLAVFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVA
GVRGLPGAGAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMTAHNPYPMPFLMDADRFAARAA
RAIARGRRFRVIPWQMGVVAKLLRVLPRWLYDRLFAGAPRKPRAGAG
>gnl|CDD|235911 PRK07027, PRK07027, cobalamin biosynthesis protein CbiG; Provisional
MMRVALGIGCRRGVPAEQIEAAIRAALAQRPLASADVRVVATLDLKADEAGLLALCARHGWPLRAFSAAQ
LAASEGALSGPSDAVRARVGVDGVAEPCALLAAPRGRLILPKTALDGVTVALAGPL
>gnl|CDD|235912 PRK07028, PRK07028, bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
MERPILQVALDLLELDRAVEIAKEAVAGGADWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTG
AIEVEMAAKAGADIVCILGLADDSTIEDAVRAARKYGVRLMADLINVPDPVKRAVELEELGVDYINVHVG
IDQQMLGKDPLELLKEVSEEVSIPIAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAI
DSGKPVKIDKFKKSLDEEIREIFMQVSTPNISDAMHRKGAMKGIKPLVRGTKMVGKAVTVQTFAGDWAKP
VEAIDVAKPGDVIVIYNSSKDIAPWGELATLSCLNKGIAGVVIDGAVRDVDEIRKLGFPVFARAIVPNAG
EPKGFGEINAEIVCGGQTVRPGDWIIGDENGVVVVPKERAYEIARRALEVKKTEDRIREEIRRGRTLSEV
IELKKWEKKK
>gnl|CDD|180800 PRK07030, PRK07030, adenosylmethionine--8-amino-7-oxononanoate transaminase; Provisional
MGLNDQWMQRDLKVLWHPCTQMKDHEQLPLIPIRRGEGVWLEDFEGKRYLDAVSSWWVNVFGHANPRINQ
RIKDQVDQLEHVILAGFSHEPVIELSERLVKITPPGLSRCFYADNGSSAIEVALKMSFHYWRNRGKPRKK
RFVTLTNSYHGETLAAMSVGDVALFTETYKPLLLDTIKVPSPDCYLRPEGMSWEEHSRRMFAHMEQTLAE
HHDEIAAVIVEPLIQGAGGMRMYHPVYLKLLREACDRYGVHLIHDEIAVGFGRTGTMFACEQAGIRPDFL
CLSKALTGGYLPLAAVLTTDTVYQAFYDDYPTLRAFLHSHSYTGNPLACAAALATLDIFEQDNVIENNRA
LARRMAEATAHLADHPHVAEVRQTGMILAIEMVQDKASKTPYPWQERRGLKVYQHALERGALLRPLGSVV
YFLPPYVITPEQIDFLAEVASEGIDIATRDSVSVAVSDFPDFRDPG
>gnl|CDD|180801 PRK07033, PRK07033, DotU family type VI secretion system protein
NTSSDPFSAGSGGFVPPNPGDRTPAAAPAAGAPFQPRPGRGAASGLNPLVAAANPLLNLIPQIRSTVHHP
DPASLREQLLDEIRQFEERAQQAGVPYEVIIGARYCLCTALDEAAALTPWGGSGVWSSHSLLVTFHNETW
GGEKFFQLLARLSQNPRQHLDLLELLYFCLALGFEGRYRVLDNGRSQLEALRQRLAQMIRSVRGEYAPAL
SPHWRDVPVARVLLRPTVPLWVCVALALLLALLLFIGLRWRLADRSDPVFAAIYALRLPVVQIARPAPQP
PPAPRLAKFLEPEIRAGLVAVRDEADRSVVTLRGDGLFASASTSVRDRYQPVLARVADALNQVKGNVLVT
GYSDNVPIRTARFPSNWELSQARAQAVRALLAARLGQPERVTAEGRGDSDPVAPNDSAENRARNRRVEIT
LLVAPGS
>gnl|CDD|168775 PRK07034, PRK07034, hypothetical protein; Provisional
MNEFERQIRAAISAARNGAKHAEQSLTTPMWQAKSTVASLGGIVPRSGSSSTSQAENYKEGLADQAASGN
NMARTSAPPVTLYQQQPNANDSYPNGNNNNPNGDNNNPNGSNNNIARVQRMPHGISRGLYERPGMLLGAW
DNAYIAAAMPLLLLVENIRSWPTRNAAEVRPPIVRELQYFQQHLQKKNYPQEDINHLSYLLCTYIDGIFN
GLQTPDSYNQSLLVEFHRDAWGGEDCFEHLRVYMNSPKQYREVLEFYDLIMCLGFDGKYQMIEHGAVLLM
DLRSRLHTQLYGQDATQSLAIAQAVKGSPRRQYIKALKIFTYGFALCLCAYGVTAWYLHQQSQQIRSNIL
TWVLPEPRKINIMETLPNPLSNILNEGWLEVRKDPRGWLLIFTSDGAFRTGEATLSEEFINKKNIERLGL
ALAPWPGDIEVIGHTDNKPFRSTSGNNNLKLSAARASVVADKLRESTQINETHQREISAIGRGESDPLAD
NATEEGRKRNRRVDILWKIGQRDADKAMKQFLENPTPEVQGTNTQQ
>gnl|CDD|180802 PRK07035, PRK07035, SDR family oxidoreductase
TNLFDLTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEME
QIDALFAHIRERHGRLDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSI
VNVASVNGVSPGDFQGIYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNDAILKQAL
AHIPLRRHAEPSEMAGAVLYLASDASSYTTGECLNVDGGYLS
>gnl|CDD|235913 PRK07036, PRK07036, aminotransferase
MAYRADALLALAQADKRHLLHPWHDFSSLGKEGSLVIVEAEGIYVTDADGRRYLDGIGGMWCVNVGYGRE
EMADAIADQARRLPYYTPFGDMTNAPAAELAAKLAELAPGDLNHVFLTTGGSTAVDSALRFVHYYFNVRG
RPAKKHIITRGDAYHGSTYLTASLTGKAADRTEFDYASDLVHHLSSPNPYRRPAGMSEAAFCDFLVDEFE
DKILSLGADNIAAFIAEPILGSGGVIVPPPGYHARMREICRRYDILYISDEVVTGFGRLGHFFASEAVFG
IQPDIITFAKGLTSGYQPLGAVIISERLLDVISGPNAKGNVFTHGFTYSGHPVACAAALKNIEIMEREGL
CEHVREVGPYFEERLASLRELPLVGDVRGDHLMACVECVADKGSKALLPEDIAIGQRIDRHCQERGLLVR
PLEHLCVLSPPLIITRAQIDEIVAILRAAIEETADELAAHGLWRGE
>gnl|CDD|180803 PRK07037, PRK07037, extracytoplasmic-function sigma-70 factor; Validated
LDVFVDNRSMLVKIAARIVGCRSRAEDVVQDAFVKLVEAPNQDAVKQPVAYLFRIVRNLAIDHYRRQALE
NKYHGDEEDGLDVPSPEASPEAALINRDTLRHVADALSELPARTRYAFEMYRLHGETQKDIARELGVSPT
LVNFMIRDALVHCRKCLDACHRG
>gnl|CDD|235914 PRK07041, PRK07041, SDR family oxidoreductase
LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAPVRTAALDITDEAAVDAFFAEAGPF
DHVVITAADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAARIAPGGSLTFVSGFAAVRPSASGVLQGAI
NAALEALARGLALELAPVRVNTVSPGLVDTPLWSKLAGDAREAMFAAAAERLPARRVGQPEDVANAILFL
AANGFTTGSTVLVDGGHAIV
>gnl|CDD|235915 PRK07042, PRK07042, amidase; Provisional
MTALHDLSAVELLAGYRARSLSPVEVTEAVLAHIARWEPHLNALYAFDPEAARAAARASTARWAKGEPLG
PLDGVPVTIKENIATRGVPVPLGTAATDLPPAAADAPPAARLREAGAVILAKTTMPDYGMLSSGLSSFHG
LTRNPWDLDQNPGGSSAGAGAAAAAGYGPLHLGTDIGGSVRLPAGWCGIVGLKPSLGRIPIDPPYTGRCA
GPMTRTVDDAALLMSVLSRPDARDGTSLPPQDIDWSDLDIDVRGLRIGLMLDAGCGLAVDPEVRAAVEAA
ARRFEAAGAIVEPVPPFLTRAMLDGLDRFWRARLWSDLAALPPERRAKVLPYIRRWAEGGADLSGVEAVR
GFNQTFAMRAAAARLFAEFDYVLSPVAPVPAFPAEWASPTNDPARPFEHIAFTVPWNMSEQPAASINCGF
TRDGLPIGLQIVGPRFDDLGVLRLAKAFEGWRGPQRPWPEPPRA
>gnl|CDD|235916 PRK07044, PRK07044, aldolase II superfamily protein; Provisional
AQPAAVPARVSPAEWQARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLV
KIDLDGNVVDDSPYPVNPAGFTIHSAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFYGRLA
YHDYEGIALDLDEGERLVADLGDKPAMLLRNHGLLTVGRTVAEAFLLMYTLERACEIQVAAQAGGGELVL
PPPEVAERTARQSLFDPGAGAGELAWPALLRKLDRIDPGYRD
>gnl|CDD|136171 PRK07045, PRK07045, putative monooxygenase; Reviewed
MKNNPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAG
GLRRDAMRLYHDKELIASLDYRSASALGYFILIPCEQLRRLLLAKLDGLPNVRLRFETSIERIERDADGT
VTSVTLSDGERVAPTVLVGADGARSMIRDDVLRMPAERVPYATPMAFGTIALTDSVRECNRLYVDSNQGL
AYFYPIGDQATRLVVSFPADEMQGYLADTTRTKLLARLNEFVGDESADAMAAIGAGTAFPLIPLGRMNLD
RYHKRNVVLLGDAAHSIHPITGQGMNLAIEDAGELGACLDLHLSGQIALADALERFERIRRPVNEAVISY
GHALATTYHDRAALVANFRSQLQTSGRDAAWLGAAVEV
>gnl|CDD|235917 PRK07046, PRK07046, aminotransferase; Validated
MMTTHGIDLARAAALLARERARFLEAHPRSRALAARAAQHLLGGVPMHWMNDWPTPFPLFVAEARGARFT
DVDGHRYDDFCLGDTGAMFGHSPAPVARALAEQARRGLTTMLPSEDAAWVGEELARRFGLPYWQVATTAT
DANRFVLRWARAVTGRPKILVFNGCYHGTVDDVFVDLVDGRPVQRPGLLGQVHDLTATTRVVEFNDLAAL
EAALADGDVAAVLAEPAMTNIGMVLPEPGFHEALRELTRRYGTLLVIDETHTISSGPGGYTRAHGLEPDF
LVVGKPIAGGVPCAVYGFSAELAERAQAAKASAPPGHSGIGTTLSANALAMAAMRATLAEVMTEAAYAHM
LALAARLAAGLRAVIARHGLPWHVTRVGARVEFQFAPTPPRNGAEAAAALDPELEAALHLYLLNRGVLIT
PFHNMMLVCPATTAADVDRLVAAFDACLGELLA
>gnl|CDD|235918 PRK07048, PRK07048, threo-3-hydroxy-L-aspartate ammonia-lyase
SDLLLPTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQ
RRAGVVTFSSGNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAE
ERGLTLIPPYDHPHVIAGQGTAAKELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAG
NDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEP
TGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARFAALLSG
>gnl|CDD|180809 PRK07049, PRK07049, cystathionine gamma-synthase family protein
MTAPHPSKTHIGNRELHPETQMLNYGYDPELSEGAVKPPVFLTSTFVFRSAEDGRDFFDYVSGRKEPPAG
EGAGLVYSRFNHPNSEIVEDRLAVYEGAESAALFSSGMSAIATTLLAFVRPGDVILHSQPLYGGTETLLA
KTFRNFGVGAVGFADGLSEAAIGAAAEAAAAKGRVSLILIETPANPTNSLVDVAAVRRVADAIEARQGHR
PIIACDNTLLGPVFQKPLEHGADLSVYSLTKYVGGHSDLVAGAVLGRKALIRQVRALRSAIGTQLDPHSC
WMLGRSLETLVLRMERANRNARAVAEFLRDHPKVEKLHYLPFLDPDSAYGAVYKRQCTGAGSTFSFDIKG
GQAAAFRFLNALQIFKLAVSLGGTESLASHPASMTHSGVPADVRERIGVLESTIRLSIGIEHPDDLIADL
AQALDAA
>gnl|CDD|180810 PRK07050, PRK07050, cystathionine beta-lyase; Provisional
MTASTPKRALQTRIVQPDDQIPPGFRSFVTPVARASTVVFPDLATMRALDWRQDVQWRYGLHATPTSLAL
AQRLAEIEGGRHALLQPSGLAAISLVYFGLVKAGDDVLIPDNAYGPNRDHGEWLARDFGITVRFYDPLIG
AGIADLIQPNTRLIWLEAPGSVTMEVPDVPAITAAARARGVVTAIDNTYSAGLAFKPFEHGVDISVQALT
KYQSGGSDVLMGATITADAELHAKLKLARMRLGIGVSADDCSLVLRGLPSLQVRLAAHDRSALEVAEWLK
ARPEIATVLHPALPDCPGHAFWMRDFTGAGGLFSVVFDERYSPAQVDAFVEALELFAIGWSWGGACSLAM
PYDVASMRTAKWPHRGTLVRLYIGLEDEADLIADLEQALEAALA
>gnl|CDD|180811 PRK07051, PRK07051, biotin carboxyl carrier domain-containing protein
MAQHEIVSPLPGTFYRRPSPDAPPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVE
AGQVLARIEE
>gnl|CDD|235919 PRK07053, PRK07053, glutamine amidotransferase; Provisional
MMKTAVAIRHVAFEDLGSFEQVLGARGYRVRYVDVGVDDLETLDALEPDLLVVLGGPIGVYDDELYPFLA
PEIALLRQRLAAGLPTLGICLGAQLIARALGARVYPGGQKEIGWAPLTLTDAGRASPLRHLGAGTPVLHW
HGDTFDLPEGATLLASTPACRHQAFAWGNHVLALQFHPEAREDRFEAWLIGHAGELAAAGIDPRTLRADT
AQHGPALEAAARRMFGEWLDRVGL
>gnl|CDD|235920 PRK07054, PRK07054, isochorismate synthase
MSACLSALRDTFARAARQAAATGRPVLAAASFPLRPLDPFDLFAAWDDGATPWCFWEAGDLPVALFGWGC
ALELNAHGDQRFARLEARWRALVADAVVAGPQPPRLVGGFRFDPRGPRSAHWQAFADASLTLAKLLVVRE
GEAYWAVCQHLVAAHDDPAALAGACCARIERLARPAPAADDDAPRLLRASALQAREWQHEVRRAVDAIRG
GAFGKVVLARDVLQQYARPVAIGPLLRRLRLRDPHAHLFAFRRGNACFLGATPERLVRVAAGDLHTHALA
GTIARGADPAEDARLGAALMASAKDRLEHALVVDAIRAALAPLSRALDIPDQPSLHRLPRLQHLSTPIRA
TLAPDATLLQVVAALHPTPAVGGHPRAAALDYIRAHEGFDRGWYAAPIGWLDAHGNGDFAVALRSALITG
GACRLFAGCGIVADSEPASEYRETCLKLSGMREALRARDAAAAGRTEAPLQSGVA
>gnl|CDD|235921 PRK07056, PRK07056, amidase; Provisional
TFTMLPTLAALAADLAAGRTTSRALVEAALARIADPAGEGARVFTHVDADAARAAADAADALRAAGAAPS
PLAGIPVSVKDLFDVAGQVTRAGSRVLADAPPAAADAPAVARLRRAGAVLIGRTNMTEFAFSGLGLNPHY
GTPRNPWRRDVGDGRIPGGSSSGAAVSVADGMAAAALGTDTGGSIRIPAALCGLTGFKPTARRVPLQGAV
PLSTTLDSIGPLARSVACCALVDAVLAGEEPVVPAARPLEGLRLAVPTTVVLDGLDATVAAAFERALKRL
SAAGAIIEEIAFPELAELAEINAKGGFSAAESYAWHRPLLARHRDQYDPRVAARILRGEPMSAADYIDLL
AARAAWIARAAARLARFDALVMPTVPIVPPRIADLEADDAAFFRTNALLLRNPSLINFLDGCALSLPCHA
PGEAPVGLMLAGAPGRDDRLLAIALAVEAVLRGI
>gnl|CDD|235922 PRK07058, PRK07058, acetate/propionate family kinase
MSKPLLLTFNAGSSTVKIGLFEVDGNEARRIGKGDIDFRRAPLRFHLRNGGETLDIPLKASVTDDLHTVL
DETFDWLAAHFDVSELVAVGHRVVHGGDRFAGAVLIDDATLDAIEALVPLAPLHQPQSLRLIRAIRHLRP
HLPQTASFDTAFHRTQPDLVRRFAIPRALHDEGIKRYGFHGLSYKFVAGELRRRAPELARGKVVAAHLGS
GASLCALDAGKSRDTSMGFSTLDGIPMATRCGALDPGVVLHLLKQEGMSLDEVEDLLYHRSGLLGVSGIS
GDTRDLLASDAPEAREALDLFALRIAGEIARLAATLGGLDAVVFTAGIGEHQPAIRAAVCERLAWLGVEL
DPAANAANAFTISSRTSRVAAFVIPTDEEQVIADEAFSVLRAMPAT
>gnl|CDD|235923 PRK07059, PRK07059, Long-chain-fatty-acid--CoA ligase; Validated
MEKIWLKSYPPGVPAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGL
AKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAK
TAVKHVVVASMGDLLGFKGHIVNFVVRRVKKMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQ
YTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPDQLNFVCALPLYHIFALTVCGLLGMRTGGR
NILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEM
TGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGY
WNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVG
VPDEHSGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDGKA
>gnl|CDD|180817 PRK07060, PRK07060, short chain dehydrogenase; Provisional
MNMAFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRLDVGDDAAIRA
ALAAAGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRGGSIVNVSSQAA
LVGLPDHLAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAWSDPQKSGPMLAAIPLGRF
AEVDDVAAPILFLLSDAASMVSGVSLPVDGGYTAR
>gnl|CDD|180818 PRK07062, PRK07062, SDR family oxidoreductase
MMQIQLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFPGARLLAARCDVLD
EADVAAFAAAVEARFGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAAS
IVCVNSLLALQPEPHMVATSAARAGLLNLVKSLATELAPKGVRVNSILLGLVESGQWRRRYEARADPGQS
WEAWTAALARKKGIPLGRLGRPDEAARALFFLASPLSSYTTGSHIDVSGGFARHV
>gnl|CDD|235924 PRK07063, PRK07063, SDR family oxidoreductase
MMNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVAGARVLAVPADVTDA
ASVAAAVAAAEEAFGPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSI
VNIASTHAFKIIPGCFPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAQPDPAAAR
AETLALQPMKRIGRPEEVAMTAVFLASDEAPFINATCITIDGGRSVLYHD
>gnl|CDD|180820 PRK07064, PRK07064, thiamine pyrophosphate-binding protein
EKVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVA
LTSTGTGAGNAAGALVEALTAGTPLLHITGQIETPYLDQDLGYIHEAPDQLTMLRAVSKAAFRVRSAETA
LATIREAVRVALTAPTGPVSVEIPIDIQAAEIELPDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLWL
GGGARHAGAEVKRLVDLGFGVVTSTQGRGVVPEDHPASLGAFNNSAAVEALYKTCDLLLVVGSRLRGNET
LKYSLALPRPLIRVDADAAADGRGYPNDLFVHGDAARVLARLADRLEGRLSVDPAFAADLRAAREAAVAD
LRKGLGPYAKLVDALRAALPRDGNWVRDVTISNSTWGNRLLPIFEPRANVHALGGGIGQGLAMAIGAALA
GPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYGVIRNIQDAQYGGRRYYVELHTPDFALL
AASLGLPHWRVTSADDFEAVLREALAKEGPVLVEVDMLSIGPFAAAFAGPPVKK
>gnl|CDD|168796 PRK07066, PRK07066, L-carnitine dehydrogenase
MAVITDIKTFAAIGSGVIGSGWVARALAHGLDVVAWDPAPGAEAALRANVANAWPALERQGLAPGASPAR
LRFVATIEACVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVG
HPFNPVYLLPLVEVLGGERTAPEAVDAAMGIYRALGMRPLHVRKEVPGFIADRLLEALWREALHLVNEGV
ATTGEIDDAIRFGAGIRWSFMGTFLTYTLAGGDAGMRHFMQQFGPALELPWTKLVAPELTDALIDRVVEG
TAEQQGPRSIKALERYRDECITEVLEAIAAVKARHGMRFED
>gnl|CDD|235925 PRK07067, PRK07067, L-iditol 2-dehydrogenase
MMRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRI
VAAAVERFGGIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGGKIINMAS
QAGRRGEALVSHYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQVDALFARYENRPPGEKK
RLVGEAVPLGRMGVPDDLTGMALFLASADADYIVAQTYNVDGGNWMS
>gnl|CDD|180822 PRK07069, PRK07069, short chain dehydrogenase; Validated
RAFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFAAEINAAHGEGVAFAAVQDVTDEAQWQALL
AQAADAMGGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVA
AFKAEPDYTAYNASKAAVASLTKSIALDCARRGLDVRCNSIHPTFIRTGIVDPIFQRLGEEEATRKLARG
VPLGRLGEPDDVAHAVLYLASDESRFVTGAELVIDGGICAM
>gnl|CDD|180823 PRK07074, PRK07074, SDR family oxidoreductase
TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARFVPVACDLTDAASLAAALAN
AAAERGPVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGM
AALGHPAYSAAKAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAWEARVAANPQVFEELKKWYPLQDFA
TPDDVANAVLFLASPAARAITGVCLPVDGGLTAGNREMARTLTLESH
>gnl|CDD|136191 PRK07075, PRK07075, isochorismate lyase
MKTPEACTGLDDIREAIDRLDRDIIAALGRRMQYVKAASRFKPSEASIPAPERVAAMLPERRRWAEQAGL
DADFVEKLFAQLIHWYIAQQIKHWRQQRGLA
>gnl|CDD|235926 PRK07077, PRK07077, phosphorylase
MAAAQGRDPRPVLAVTGMAFEARIAAGPGVEVVCAARADRLERALLAAFDARGCAGIVSFGVAGGLDPDL
APGDLVVATAVDAPFGRVDTDARWSARLAAALELTPVARRVVRGGLAGVEAPVVGAAAKAALHRATGALA
VDMESHIAAAFAAARGLPFAACRVIVDPAWRTLPAAATAGLRDDGSTDILPILRGLARQPSQLGALLQVA
IDARAARRSLRQARHALGRAGALRIGLV
>gnl|CDD|235927 PRK07078, PRK07078, hypothetical protein; Validated
MLDFNDINEPALANLDAERDEIRAALLARLESVLTTLFPAGKKRGGKFVIGDILGSPGDSLEVVLDGEKA
GLWTDRATGDGGDVFALIAAQLGLDVHTDFPRVLDMAAELLGRARATPVRKRKKSPPVDDLGPATAKWDY
LDAAGKLIAVVYRYDPPGRRKEFRPWDAKRRKMAPPEPRPLYNQPGLLSAEQVVLVEGEKCAQALIDAGV
VATTAMHGANAPVDKTDWSPLAGKAVLIWPDRDKPGWEYADRAAQAILSAGASSCAVLLPPEDLPEGWDA
ADAIAEGFDVAGFLAHGERLPVLDSVDDPAPVDLSDESVWATEDALALAFTRRYKDDWRYCALWGKWLVW
TGSRWRTEDTLLATHLIRGVCREAALKADSPKVAAKLASAATVGGVERLARSDRRHAATSEEWDADPWLL
NTPGGVVDLRTGRLRPHRREDRMTKITTATPAGDCPTWRRFLAEVTGGDAELQAYLQRMAGYALTGSTSE
HALFFLYGTGANGKSVFVNTLATILGDYAANAPMDTFMETRGDRHPTDLAGLRGARFVSAIETEQGRRWA
ESKVKNLTGGDKISARFMRQDFFEFFPQFKLLIAGNHKPAIRNVDEAMKRRLHLIPFTVTVPPERRDKRL
QQKLLAERDGILAWAVEGCLDWQRNGLDPPQSVVEATEEYFEAEDALGQWIEERCERGANAKELTAELFN
DWKEWAERAGEFVGSQKRFSDLLATRGFEKWRLTGGLRGFRGIGLKPKPYGAYTPYRDD
>gnl|CDD|235928 PRK07079, PRK07079, hypothetical protein; Provisional
MTREAAIARAAAYFDSGAFFADLARRVAYRTESQNPDRAPALRAYLTDEIAPALAALGFTCRIVDNPVAG
GGPFLIAERIEDDALPTVLIYGHGDVVRGYDEQWREGLSPWTLTEEGDRWYGRGTADNKGQHTINLAALE
QVLAARGGRLGFNVKLLIEMGEEIGSPGLAEVCRQHREALAADVLIASDGPRLSAERPTLFLGSRGAVNF
RLRVNLRDGAHHSGNWGGLLRNPGTVLAHAIASLVDARGRIQVPGLRPPPLPAAVRAALADITVGGGPGD
PAIDPDWGEPGLTPAERVFGWNTLEVLAFKTGNPDAPVNAIPGSARAVCQLRFVVGTDWENLAPHLRAHL
DAHGFPMVEVTVERGSPATRLDPDDPWVRWALASIARTTGKKPALLPNLGGSLPNDVFADILGLPTLWVP
HSYPACSQHAPNEHLLASVAREGLQIMAGLFWDLGEQGPALLAARRAHA
>gnl|CDD|235929 PRK07080, PRK07080, amino acid--[acyl-carrier-protein] ligase
PAMAAAMTADAPELDAGRNDFRDELFDAGLLIPTGVDGLYGRSGLFEDVVEALDALITRLGADQGAEVLR
FPPVMSRAEFERSGYLKSFPQLAGTVHSFCGNEAEHRRLLACLDRGEDWTESQKPTDVVLTPAACYPVYP
VLARRGALPADGRLVDVASYCFRHEPSLDPARMQLFRMREYVRIGTPEQIVAFRQSWIERGTAMADALGL
PVEIDLANDPFFGRGGKIVAASQREQNLKFELLIPIYSDAPPTACMSFNYHMDHFGLTWGIRTADGAVAH
TGCVGFGLERLALALFRHHGLDPAAWPAAVRDVLWGT
>gnl|CDD|180828 PRK07081, PRK07081, acyl carrier protein; Provisional
MKNTIRTILKKVAKLEVPIDSIADDADLYEAGLSSLATVQLMLAIEDAFDIEIPDEMLNRKLFASIDALA
GAVTQLQDAEKSA
>gnl|CDD|180829 PRK07084, PRK07084, class II fructose-1,6-bisphosphate aldolase
MVSYKELGLVNTREMFAKAVKGGYAIPAYNFNNMEQLQAIIQACVETKSPVILQVSKGARKYANATLLRY
MAQGAVEYAKELGCPIPIVLHLDHGDSFELCKDCIDSGFSSVMIDGSHLPYEENVALTKKVVEYAHQFDV
TVEGELGVLAGVEDEVSAEHHTYTQPEEVEDFVKKTGVDSLAISIGTSHGAYKFKPGQCPPPLRFDILEE
IEKRIPGFPIVLHGSSSVPQEYVKTINEYGGKLKDAIGIPEEQLRKAAKSAVCKINIDSDGRLAMTAAIR
KVFDEKPEEFDPRKYLGPARDELKKLYKHKIINVLGSNGKA
>gnl|CDD|235930 PRK07085, PRK07085, diphosphate--fructose-6-phosphate 1-phosphotransferase; Provisional
MNKSYLQLARLKYRPKLPKLLQNDPGLIKIVDGEFTESVADQDELAELFPNTYGLPYVTFVKGSESSSKP
LKVGVILSGGQAPGGHNVIAGLFDGLKKLNPDSKLFGFIGGPLGLLNGKYIEITEEVIDEYRNTGGFDMI
GSGRTKIETEEQKEACLETVKKLKLDGLVIIGGDDSNTNAAILAEYFAKHGCKTQVIGVPKTIDGDLKNE
FIETSFGFDTATKTYSEMIGNISRDALSAKKYWHFIKLMGRSASHIALECALQTHPNICLISEEVAEKKM
SLQDIVHYIASVIADRAAKGKNYGVILIPEGLIEFIPEMKSLIKELNSLLAENESEFKGLDTEAQREYII
SKLSPESAKLFKSLPEDIARQLLLDRDPHGNVQVSKIETEKLLIEMVKKELEKLKPEGKYKGPFSAISHF
FGYEGRSAFPSNFDADYCYALGYTAALLILNGKTGYMSTIKNLTSPYTEWIAGAVPLTMMMNMERRHGKE
KPVIKKALVDLDGPPFKYFAKYRDIWALEDSYRFPGPLQYFGPEELCDQRTLTLLLELNKNSWQK
>gnl|CDD|180831 PRK07088, PRK07088, ribonucleoside-diphosphate reductase subunit alpha
MNIKIKKRDGQYEPLQVEKTKKMVKLACEGLYGCDPLELELDSRIQFRDGMTTKEIQKSLIQTAIEKVIQ
NSKDNNGNNTKKTNPNWQYVAARLYVFDLYKEARINRHYNSFGYGDYYELVKKLVEEKLYGEYLLQNYSK
EEIKELEKYIKPERDFLFNYEGLKLLADRYLVKGFNREILELPQERFMGIAMHLAIPEGKEKRVYYAKKF
YDLLSELKATVATPTLSNAGTPFYQLSSCFISVVDDNLWSIYDVNQKFAQVSKHGGALGIYTGKIRALNS
EIRGFKNASGGVIPWIKLYNDTAIAVDQLGKRKGGAAITLDIWHKDIPEFLDLKTNNGDDRRKAHDIFPG
VSYPDLFMKRLEKRENWSLFDPHEIKKVKGYSLEDYYDEEDRKEFTKKYLECEEDTNIPRRTVPVLDIMK
KIMKSAVETGTPFIFFRDTVNKANPNKHKGMIYSSNLCHEIAQNMSESELLEEEIIDENGYYEVVQKIKA
GDMVTCNLNSIVLGNVDDEELEEVIPTQIRMLDNVISLNYYPVPEAEITSDKYRAIGLGTSGYHHMLANN
KIRWESDEHIKFADKIYEEIAYYAIKASMELAKEKGSYPAFKGSEWETGKYFERRGYNSERWKKLKEEIK
KYGMRNGYITAVAPTGSTSNIANTTAGIDPVFKRFFMEEKKGSFTPKTAPDLNEENFWYYKEAHTIDQQW
SIKACGVRQRHIDQAQSFNLYITPEYKAKQILNLYIEAWKQGVKTIYYVRNKSLEMDECTSCSS
>gnl|CDD|180832 PRK07090, PRK07090, class II aldolase/adducin domain protein; Provisional
MAKTLSLSKDELVARAQRQMDNELKDSGWTLRQKLALTCRILFDAGHDSGLAGQITARAEAPGTYYTQRL
GLGFDEITASNLLLVDEDLNVLDGEGMPNPANRFHSWIYRARPDVNCIIHTHPPHVAALSMLEVPLVVSH
MDTCPLYDDCAFLKDWPGVPVGNEEGEIISAALGDKRAILLSHHGQLVAGKSIEEACVLALLIERAARLQ
LLAMAAGPIKPIPPELAREAHDWISTPKRSAATFAYYARRALRRHPDCLD
>gnl|CDD|235931 PRK07092, PRK07092, benzoylformate decarboxylase; Reviewed
MPKATAPAAAMTTVRDATIDLLRRFGITTVFGNPGSTELPFLRDFPDDFRYVLGLQEAVVVGMADGYAQA
TGNAAFVNLHSAAGVGNAMGNLFTAFKNHTPLVITAGQQARSILPFEPFLAAVQAAELPKPYVKWSIEPA
RAEDVPAAIARAYHIAMQPPRGPVFVSIPYDDWDQPAEPLPARTVSSAVRPDPAALARLGDALDAARRPA
LVVGPAVDRAGAWDDAVRLAERHRAPVWVAPMSGRCSFPEDHPLFAGFLPASREKISALLDGHDLVLVIG
APVFTYHVEGPGPHLPEGAELVQLTDDPGEAAWAPMGDAIVGDIRLALRDLLALLPPSARPAPPARPMPP
PAPAPGEPLSVAFVLQTLAALRPADAIVVEEAPSTRPAMQEHLPMRRQGSFYTMASGGLGYGLPAAVGVA
LAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGALRWFAPVFGVRDVPGLDLPGLDFV
ALARGYGCEAVRVSDAAELADALARALAADGPVLVEVEVA
>gnl|CDD|235932 PRK07093, PRK07093, para-aminobenzoate synthase component I; Validated
YTMQEFIQRANELGKQKTPFFFLIDFEQQKPIIEPLEELAESGILFDFNGKTNVPSQVRPHKPFELQKEP
ISFEEYQQGFELVQEEIQAGNSYLLNLTYPTPIETNLSLEEIFQASKAKYKLLFKDQFVCFSPEPFVRIE
DNKISTYPMKGTIDASLPNAEEKLLNDEKEFAEHATIVDLLRNDLSMVAKNVRVTRFRYIDKIKTNKGEI
LQTSSEISGTLPENWQENIGDILAKLLPAGSITGAPKEKTVEIIEQAEGYERGFYTGVFGYFDGESLDSA
VMIRFIEQENDGLYFKSGGGITIDSDLKDEYNELIQKVYVPIY
>gnl|CDD|235933 PRK07097, PRK07097, gluconate 5-dehydrogenase; Provisional
MSENLFSLKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTD
EDGVQAMVSQIEKEVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGK
IINICSMMSELGRETVSAYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLRELQADGSRH
PFDQFIIAKTPAARWGDPEDLAGPAVFLASDASNFVNGHILYVDGGILAYIGKQP
>gnl|CDD|235934 PRK07101, PRK07101, hypothetical protein; Provisional
MMFPLFETIAIEDGEIQNLSYHQQRYERTLAEFYGKEAPFDLAEIIQPPTELQEGLVRCRIDYNAEIYQV
QYFPYQRRPIRSFQPVYCDDIDYSLKYTDRSALNELFAQKGECDEIIIIKNGLVTDTSIGNLAFFDGKQW
FTPKKPLLKGTQRARLLDEGKIKEKDITVEDLLQYEEIRLINAMNGF
>gnl|CDD|180838 PRK07102, PRK07102, SDR family oxidoreductase
MKKILIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVAVSTHELDILDTASHAAFL
DSLPALPDIVLIAVGTLGDQAACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDR
GRASNYVYGSAKAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPMTAGLKLPGPLTAQPEEVAKDIFRAI
EKGKDVIYTPWFWRLIMLIIRSIPEPIFKRLSL
>gnl|CDD|180839 PRK07103, PRK07103, polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPDDAGAGLASAFIGAELDSLALPERLD
AKLLRRASLSAQAALAAAREAWRDAALGPVDPDRIGLVVGGSNLQQREQALVHETYRDRPAFLRPSYGLS
FMDTDLVGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLG
AMGSDRFADEPEAACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSL
EGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPLGDETELAALFASGLAHAWINATKSLTGHGLSAAGIVE
LIATLLQMRAGFLHPSRNLDEPIDERFRWVGSTAESARIRYALSLSFGFGGINTALVLER
>gnl|CDD|180840 PRK07105, PRK07105, pyridoxamine kinase; Validated
KNPVKRVAAIHDLSGFGRVALTASIPIMSSMGLQVCPLPTALLSSHTGGFQNPSIIDLTDGMQAFLTHWK
SLNLKFDAIYSGYLGSPRQIQIVSDFIKYFKKKDLLVVVDPVMGDNGKLYQGFDQEMVEEMRKLIQKADV
ITPNLTEACLLLDKPYLEKSYSEEEIKQLLRKLADLGPKIVIITSVPFEDGKIGVAYYDRATDRFWKVFC
KYIPAHYPGTGDIFTSVITGSLLQGDSLPIALDRAVQFIEKGIRATLGLKYDLREGILLEKVLGYLIAPF
QELL
>gnl|CDD|180841 PRK07106, PRK07106, phosphoribosylaminoimidazolecarboxamide formyltransferase
MNELELKYGCNPNQKPARIFMKEGELPIEVLNGRPGYINFLDALNSWQLVKELKEATGLPAAASFKHVSP
AGAAVGLPLSDTLKKIYFVDDMELSPLACAYARARGADRMSSYGDFAALSDVCDVETAKLLKREVSDGII
APGYTPEALEILKAKKKGNYNIIKIDPNYEPAPIETKDVFGITFEQGRNELKIDEDLLKNIVTENKELPD
EAKRDLIIALITLKYTQSNSVCYAKDGQAIGIGAGQQSRIHCTRLAGNKADIWYLRQHPKVLNLPFKEGI
RRPDRDNAIDVYLSDDYMDVLADGVWQQFFTEKPEPLTREEKRAWLATLTGVALGSDAFFPFGDNIERAA
KSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFHH
>gnl|CDD|180842 PRK07107, PRK07107, IMP dehydrogenase
MAFYFEEPSRTFSEYLLVPGLSSKECVPANVSLKTPLVKFKKGEESAITLNIPLVSAIMQSVSDDNMAIA
LAREGGLSFIFGSQSIESEAAMVRRVKNYKAGFVVSDSNLTPDNTLADVLDLKEKTGHSTVAVTEDGTAH
GKLLGIVTSRDYRISRMSLDTKVKDFMTPFEKLVTANEGTTLKEANDIIWDHKLNTLPIVDKNGNLVYLV
FRKDYDSHKENPLELLDSSKRYVVGAGINTRDYAERVPALVEAGADVLCIDSSEGYSEWQKRTLDWIREK
YGDSVKVGAGNVVDREGFRYLAEAGADFVKVGIGGGSICITREQKGIGRGQATALIEVAKARDEYFEETG
VYIPICSDGGIVYDYHMTLALAMGADFIMLGRYFARFDESPTNKVNINGNYMKEYWGEGSNRARNWQRYD
LGGDKKLSFEEGVDSYVPYAGSLKDNVAITLSKVRSTMCNCGALSIPELQQKAKITLVSSTSIVEGGAHD
VILKDKSNNLIK
>gnl|CDD|180843 PRK07108, PRK07108, acetyl-CoA C-acyltransferase
MTEAVIVSTARTPLAKSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANIARQ
IALRAGLPVTVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRHMLREGWLVEH
KPEIYWSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKATGRLFTK
EVTVSADEGIRPDTTLEGVSKIRSALPGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAV
AGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPY
GVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFEVL
>gnl|CDD|235935 PRK07109, PRK07109, short chain dehydrogenase; Provisional
MMLKPIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAE
AVQAAADRAEEELGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAII
QVGSALAYRSIPLQSAYCAAKHAIRGFTDSLRCELLHDGSPVSVTMVQPPAVNTPQFDWARSRLPVEPQP
VPPIYQPEVVADAILYAAEHPRRELWVGGPAKAAILGNRLAPGLLDRYLARTGYRGQQTDRPADPDRPDN
LYEPVPGDHGAHGRFGDRARRSSYQLWAQRPLVAAALALLAAALLAAALARRRR
>gnl|CDD|235936 PRK07110, PRK07110, polyketide biosynthesis enoyl-CoA hydratase; Validated
MMMKVVELREVEEGIAQVTMQDRVNKNAFSDELCDQLHEAFDTIAQDPRYKVVILTGYPNYFATGGTQEG
LLSLQTGKGTFTEANLYSLALNCPIPVIAAMQGHAIGGGLVLGLYADIVVLSRESVYTANFMKYGFTPGM
GATAILPEKLGLALGQEMLLTARYYRGAELKKRGVPFPVLPRAEVLEKALELARSLAEKPRHSLVLLKDH
LVADRRRRLPEVIEQEVAMHEKTFHQPEVKRRIESLYGG
>gnl|CDD|235937 PRK07111, PRK07111, anaerobic ribonucleoside triphosphate reductase; Provisional
MMLYIVKRDGREVPFDEEKITNAIFKAAEAVGGELDESEAIELTQKVIKYLEEKYKEEVTVEDIQDLVEK
VLIENGHAETAKAYILYRAERTRIREIKSDLMKAIEEIGNDTDRENANVSGNTPSGKMLRIASESNKDYY
NLYLLPKELAKAHENGDIHIHDLDFYNLTTTCLQIDLKKLLERGFNTGHGYIREPKRIESAAALACIILQ
SNQNDMHGGQSIPNFDNDMAPFVEKTFRRHRKEILEKLLELGVGEEVDEKESLNEEEELLLLLLALDFNI
AKKAQEKADELAEKETRKRTYQAMEGFIHNLNTMHSRAGAQVPFSSINYGTDTSPEGRMVCENLLLATEK
GLGKGETPIFPIQIFRVKEGVNYNEEDPNYDLFKLACRVAAKRLFPNFSFLDAPFNKEYYDKGRPPTEVA
TMGCRTRVMSNVNGEEGTKGRGNLSFTTINLPRLAIEAKKDIDKFFELLDERLELAIEQLLHRYEVQKTL
KVKDFPFLMGQGLWKGSENLGPDDSIEPVLKQGTLGIGFIGLAETLVALTGKHHGESEEAQELGLKIVSH
MRDFCDEYKEEYKLNYSLLATPAEGLSGRFIKMDRKKFGEIKGVTDKEYYTNSFHVPVYYPISIFEKIEI
EAPYHKLTNGGHISYVELDGDPSKNVEAFEIIVKAMKNTNIGYGSINHPVDRCPVCGYLGVIEDKCPKCG
STNIQRIRRITGYLGTLDRFNSAKKAERRDRVKHG
>gnl|CDD|235938 PRK07112, PRK07112, enoyl-CoA hydratase/isomerase
MDYQTIRVRQQGDVCFLQLHRPEAQNTINDRLIAECMDVLDRCEHAATIVVLEGLPEVFCFGADFSAIAE
KPDAGRADLIDAEPLYDLWHRLATGPYVTIAHVRGKVNAGGIGFVAASDIVIADETAPFSLSELLFGLIP
ACVLPFLIRRIGTQKAHYMTLMTQPVTAQQAFSWGLVDAYGANSDTLLRKHLLRLRCLNKAAVARYKSYA
STLDDTVAAARPAALAANIEMFADPENLRKIARYVETGKFPWEAD
>gnl|CDD|235939 PRK07114, PRK07114, bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase
AKFDRIAVLTAMKATGMVPVFYHADVEVAKKVIKACYDGGARVFEFTNRGDFAHEVFAELVKYAAKELPG
MILGVGSIVDAATAALYIQLGANFIVTPLFNPDIAKVCNRRKVPYSPGCGSLSEIGYAEELGCEIVKLFP
GSVYGPGFVKAIKGPMPWTKIMPTGGVEPTEENLKKWFGAGVTCVGMGSKLIPKEALAAKDYAGIEQKVR
EALAIIKEVRKK
>gnl|CDD|235940 PRK07115, PRK07115, AMP nucleosidase; Provisional
MKTKEEIVQNWLPRYTGSPLEEFGPYILLTNFSYYVEVFAELFGVPVSGSMFSMAHATAEGITIINFGMG
SPNAATIMDLLSALNPKAVLFLGKCGGLKSKYQVGDYFLPIAAIRGEGTSDDYFPPEVPALPNFVLQKAV
SSIIRDKGLDYWTGTVYTTNRRFWEHDKEFKEYLYETRAQAIDMETATLFAAGFANNIPTGALLLISDLP
LRPEGVKTKESDNKVTKTYTEEHIEIGIEALKSLRKKGKGVKHLRFGE
>gnl|CDD|180850 PRK07116, PRK07116, flavodoxin; Provisional
ANNKTLVAYFSATGTTKKVAEKLAEVTGADLFEIKPEQPYTAADLDWNDKKSRSSVEMADKSSRPAIAKK
IENIAEYDVIFLGFPIWWYVAPRIINTFLESYDFSGKTVIPFATSGGSGIGNAEKELKKSYPDANWKEGR
LLNGGASKEEIKEWINKLDL
>gnl|CDD|180851 PRK07117, PRK07117, acyl carrier protein; Validated
MDKQRIFDILVRHIREVLPDLDQHQFQPEDSLVDLGANSMDRAEIVIMTLESLSLKIPLVEFAGAKNIGE
LADLLYAKL
>gnl|CDD|235941 PRK07118, PRK07118, Fe-S cluster domain-containing protein
MNMILFAVLSLGALGLVFGILLAFASKKFAVEEDPRVEAVREVLPGANCGGCGYPGCDGYAEAVVNGDAP
PNLCPVGGAEVAEKVAEILGKEAAESEPKVAVVRCQGTCDKAKERYEYQGIKDCAAAALLFGGPKGCSYG
CLGLGSCVAACPFDAIHIENGLPVVDEDKCTGCGACVKACPRNVIELIPKSARVFVACNSKDKGKAVKKV
CEVGCIGCGKCVKACPAGAITMENNLAVIDQEKCTSCGKCVEKCPTKAIRILNKPPKVKEPKKAAAEAAA
>gnl|CDD|235942 PRK07119, PRK07119, 2-ketoisovalerate ferredoxin reductase; Validated
MMEKVLMKGNEAIAEAAIRAGCRCYFGYPITPQSEIPEYMSRRLPEVGGVFVQAESEVAAINMVYGAAAT
GKRVMTSSSSPGISLKQEGISYLAGAELPCVIVNIMRGGPGLGNIQPSQGDYFQAVKGGGHGDYRLIVLA
PSSVQEMVDLTMLAFDLADKYRNPVMVLGDGVLGQMMEPVEFPPRKKRPLPPKDWAVTGTKGRRKNIITS
LFLDPEELEKHNLRLQEKYAKIEENEVRYEEYNTEDAELVLVAYGTSARIAKSAVDMAREEGIKVGLFRP
ITLWPFPEKALEELADKGKGFLSVEMSMGQMVEDVRLAVNGKKPVEFYGRMGGMVPTPEEILEKIKEILG
GA
>gnl|CDD|180854 PRK07121, PRK07121, FAD-binding protein
MSTDIPRPVSAEDVTSWDDEADVVVVGFGAAGACAAIEAAAAGARVLVLERAAGAGGATALSGGVIYLGG
GTAVQKAAGFEDSPENMYAYLRVAVGPGVDEEKLRRYCEGSVEHFDWLEGLGVPFERSFFPEKTSYPPND
EGLYYSGNEKAWPFAEIAKPAPRGHRVQGPGDSGGGAMLMDPLAKRAAALGVQIRYDTRATRLIVDDDGR
VVGVEARRYGETVAIRARKGVVLAAGGFAMNREMVARYAPAYAGGLPLGTTGDDGSGIRLGQSAGGATAH
MDQVFAWRFIYPPSALLRGILVNARGQRFVNEDTYGARIGQFILEQPGGTAYLIVDEALFEEARAQLRPQ
IDGRTPGAWKAETVEELARKLGIPPGGLQATVDAYNRAAAGGEDPPFHKQPEWLRPLDTGPFAAIDLSLG
KAPTPGFTLGGLRVDEDTGEVLRADGAPIPGLYAAGRCASGIASNGYVSGLSLADCSFFGRRAGRHAAAR
AG
>gnl|CDD|168831 PRK07122, PRK07122, RNA polymerase sigma factor SigF; Reviewed
MTARAAGGSRPRASTDEYADVPEMFRELAGLPAGSPEFQRQRDRIVTRCLPLADHIARRFDGRGEPRDDL
VQVARVGLVNAVNRFDVETGSDFVSFAVPTIMGEVRRHFRDNSWSVKVPRRLKELHLRLGRATAELSQRL
GRAPTASELAAELGMDREEVVEGLVAGSAYNTLSIDSGGGSGDDDARAIADTLGDVDAGLDQIENREALR
PLLAALPERERTVLVLRFFESMTQTQIAERVGISQMHVSRLLAKTLARLRDQLE
>gnl|CDD|180855 PRK07132, PRK07132, DNA polymerase III subunit delta'; Validated
MNNWIKFLDNSATQNKISHSFLLKSNYNEDIDEKILYFLNKFNNLQITNLNEQELPANIILFDIFDKDLS
KSEFLSAINKLYFSSFVQSQKKILIIKNIEKTSNSLLNALLKTIEEPPKDTYFLLTTKNINKVLPTIVSR
CQVFNVKEPDQQKILAKLLSKNKEKEYNWFYAYIFSNFEQAEKYINKESENLLKKFEEALNKSLKEKYEL
ILFLNKKLTKENALFLLKLLKFFFKSIFANKKKKNPKNIKVAFSKKKKFKIEFFELITIIDEFLNSLETN
ENFNLQKQAFLVKIYEIYE
>gnl|CDD|235943 PRK07133, PRK07133, DNA polymerase III subunits gamma and tau; Validated
MRMKYKALYRKYRPKTFDDIVGQDHIVQTLKNIIKSNKISHAYLFSGPRGTGKTSVAKIFANALNCSHKT
DLLEPCQECIENVNNSLDIIEMDAASNNGVDEIRELIENVKNLPTQSKYKIYIIDEVHMLSKSAFNALLK
TLEEPPKHVIFILATTEVHKIPLTILSRVQRFNFRRISEDEIVSRLEFILEKENISYEKNALKLIAKLSS
GSLRDALSIAEQVSIFGNNKITLKNVEELFGLVSNENLINLLNLLYSKDIKEVLNILNQIKEQGIDPELL
LISLINLVKEFIIFNKTKDNSLLEYYSEEDLEKLKIDDDFAYKFIEILFDLLKDLKISDNPNDTLEILII
KLLALSELEEEDENEIKFKKIEENSIDNLDIKEKKIENENDIEGKSDTKNLEEGFETKDNKNKNSSFINK
TENILTNSPLKDELLEKTTEIINIENPQEFEFGQIGNDIISTEIAQLDENQNLIDTGEFDLENNFSNSFN
PENGNKIDENINETFDTSTISANLSENKTNFAQSFNNKDTNLINSEIPIDLIKDTITINNSQKNVKKNGN
KDYLSVEEVINLIMLAIKFHSQNQVEYKKLVQNWNKNLPLFEYDVEFMEIAHFLKDLKILASSDNFILFS
SKRDEIDELIIKLNKNNYKVNFQNFLEKIFGGPKHIFAISKKLINEAKIYWKAINNTKKSVVIKPLEKPK
KYEKTSVSKENLEKEIFGDKFTKKK
>gnl|CDD|235944 PRK07135, dnaE, DNA polymerase III DnaE; Validated
MKLINLHTNTEYSFLSSTIKLDSLIKYAKENNLKTLVLTDHNNMFGVPKFYKLCKKNNIKPIIGLDLEVE
NFRFILLAKNYSGYKLLNELSSKKSKNKEIELNDLDSDNIIIIDHPKNGFYAKNKEQLELKNYYINSNDP
KIENAVYVQERKLLFAEDNEYLKILNKIGNNKEENSNFKFFDFEKWFEDIDEKILKRTNYLVENINIEFP
KKEFNLPDFDNNLGLESDLFLKKILKESVINKKAELKYYPNVKERINYEYSVIKKLKFSNYFLIIWDFIK
WARKNKISIGPGRGSASGSLVSYLLNITSVNPLKYDLLFERFLNPDRITMPDIDIDIQDDRRDEVIDYIF
EKYGYEHCATISTFQTLGAKSAIRDVGRMLGIPESDVNAISKLIPNNQSLEEAYDKNKSFFRELISKGDP
IYKKLYKIAKKLEGLPRQSGTHAAGIIISNKPITNYVPTFESKDNYNQVQYSMEFLEDFGLLKIDLLGLK
NLTIIKNIEEKINKELLFDHLINFNDLPIIDKKTNNLLSNGKTEGIFQLESPGMKSTIKKVGIDSFEDIV
AIISLYRPGPIQYIPIYAKNKKNPKNIEKIHPEYDEIVAPTYGIIIYQEQIMQIAQKVAGFSFAQADLLR
RAISKKDETKLDKIKDKFIEGGIKNGYSKKVLEKIYSLIEKFADYGFNKSHAVAYATLAYKMAYYKANYP
LVFYSALISNSNGSQENIKKYVKEAKNNGIKVYSPDINFSTENAVFDNGKIFLPLIMIKGLGSVAIKKII
DERNKNGKYKNFFDFILRLKFIGISKSIIEKLIKANTLRSFGNQDTLLNNLELAKNYAETILSKVAKNLY
DDYKNFGLDLEFILEEIERDLEEESKNEIEYLGMSFNAFDTNKLEKNQIRLKDLRINTEYRLAIEVKNVK
RLRKANKEYKKVILSDDSVEITIFVNDNDYLLFETLKKGDIYEFLISKSKNNKFYIINNKKKE
>gnl|CDD|235945 PRK07139, PRK07139, amidase; Provisional
MIKNKGNFQKALEELKNDKNNAVSYVFDEKNNKDGPLANCVFTIKDNFATSEGPTHASSKSLENFKPSYN
ATVVQKLINAGAKPVAKVHCDELGLGGTGLFSAFGLIKNPLDSSKLVGGSSSGSAATFNKNISFAIGSDT
GDSVRLPASFIGKVGFKPSYGAISRYGLFAYASSLDTVAYFTHNVNDAIILSKVLFGKDENDLTSVDVKI
NNVKKTKPKKVAYLDCFKELEEYVAKKYKKLINILKSENIEVEKIKIDEKLLKAIKPVYKIISYSEASSN
LANLNGIAFGNREKGSSWEEIMINTRSEGFGKMVQKRLILGSYFLEEENQEKYFLKAKKVRRVIKNYYES
IHNKFDIVIYPAYADIAPDIDENENKSDNYMDYILTISNLVGNPSLSIPLGKYNNLPFNLAIDSKIYDDE
KLLSYSLYIEELIKGINEE
>gnl|CDD|235946 PRK07143, PRK07143, hypothetical protein; Provisional
MMKVYTFPLKNFKFEKPTFVLGGFESFHLGHLELFKKAKESNDEIVIVIFKNPENLPKNTNKKFSDLNSR
LQTLANLGFKNIILLDFNEELQNLSGNDFIEKLTKNQVSFFVVGKDFRFGKNASWNADDLKEYFPNVHIV
EILKINQQKISTSLLKEFIEFGDIELLNSLLLYNYSISITINKNFEFTYPQNIIKLHAGIYLAYVVINNF
KYHGILKINFNNKNKIKFFDFDLIINKYQEIFIEIVKEIRIISSNEDNNILNDDIEIAKKFFLNNKKNN
>gnl|CDD|235947 PRK07152, nadD, nicotinate-nucleotide adenylyltransferase
MKIAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYINPFKKKQKASNGEHRLNMLKLALKNLPKME
VSDFEIKRQNVSYTIDTIKYFKKKYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIVVFKRKKNINKKN
LKKYNVLLLKNKNLNISSTKIRKGNLLGKLDPKVNDYINENFLYLEDILKSFLDEYRYKHCLRVAQLAAE
LAKKNNLDPKKAYYAGLYHDITKEWDEEKHRKFLKKYLKDVKNLPWYVLHQYVGALWLKHVYGIDDEEIL
NAIRNHTSLAEEMSTLDKIVYVADKIEPGRKYIGIQKLRKLAFKDLDEAFKEVLKYQYELIK
>gnl|CDD|235948 PRK07157, PRK07157, acetate kinase; Provisional
MKAKILVINAGSSSIKWQLFDKENLNLIASGLAERIGLENGLIKIKFGKKKYEKEVDMPNHKVAVAVLIE
IWEENKLIEDLEEIELIGFRVVHGGDYFNGPTKLDDKEISKIEKVAKYAPLHNPGALQTIKAFKKVLPKA
KLSASFDTAFHTSIPKINYTYPINYEIAKKYGIKKYGFHGISHKFITNKVEKILNKDKVNFVNLHIGNGA
SLCAIKNSKSIDTSMGLTPLAGVMMGTRSGDIDPSIHEFVAKEANMSISEFTDLLNKKSGLLGVSGISSD
LRDVIKAAESGNKRAKFALDLYAQKIVDYLANYINKIGKKIDAIVFTAGVGENSAFVRELVINKINIPNI
KLDKEKNLKKIGEYGPIELISTPDSDIPVYVIRTNEELLIAKNAIKLYEN
>gnl|CDD|235949 PRK07159, PRK07159, F0F1 ATP synthase subunit C; Validated
VNSIVNFVGQILQNTQTVSQKVAADSSGLKAAYIGAGLAMIGVIGVGLGQGYAFGKAVEAIARNPEAQKQ
VFKLLFIGSAISETSSIYALLVAFILIFVG
>gnl|CDD|235950 PRK07164, PRK07164, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional
NNEKIIAIIYADNNEFVNLENFEFILLKNIESFQKKIAIFRYKNYNILYINTGIGLINAALATQKLIEKY
QIEIIINYGAVGSNINIDLGQVVYPEKFYLLDAITPWYPPGQTPGEKEFYENNKINKNFNKIHLGSSNSF
IFDLDKLKIIKDFIFVSFFDMEAFALAQVCFKNKVKFYCIKYVSDFIENNSDIEIVNNNIKKGSKKALEF
IFELLENI
>gnl|CDD|235951 PRK07165, PRK07165, ATP F0F1 synthase subunit alpha
MNPKIKSIFDYIVEVKGEYDYQQNQFFTLKNNPNVKAFVISATEDKAYLLINNEKGKIKINDELIELNNT
NKVKTSKEYFGKIIDIDGNIIYPEAQNPLSKKFLPNTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPI
GKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPST
SPYEQYLAPYVAMAHAENISYNDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERA
GKFKNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKT
ITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKMFNQKGFSLYSYRFVLLISKLISWGL
LKDVKDEQKALDFIDYLIENDPDAKKIFNKIKNNEDVDDELMKNYFAFLLNQYSDYVNLNWKIENEHSFL
KLSEEFLEKVAKKLGDK
>gnl|CDD|180864 PRK07168, PRK07168, uroporphyrin-III C-methyltransferase
MNGYVYLVGAGPGDEGLITKKAIECLKRADIVLYDRLLNPFFLSYTKQTCELMYCGKMPKNHIMRQEMIN
AHLLQFAKEGKIVVRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNSV
TLLTGHAKGPLTDHGKYNSSHNSDTIAYYMGIKNLPTICENLRQAGKKEDTPVAVIEWGTTGKQRVVTGT
LSTIVSIVKNENISNPSMTIVGDVVSLRNQIAWKERKPLHGKKVLFTSATNKTSVMKQKLQEAGAEIYQI
PTFKKEEYTLTLEQINEIFNVNRLVFCSAESVEILMQSCSKYKKDIRSLQAELQHMNVATQEKLMQYGLL
SKEAKFSSDTTVYLGRNINRIAFIQEKIGAGSYMMTHKYTIDHRFDEVHSRMLSEFLWDSIVFEGRASID
TFLAEVKRLGFIDIVTLPFSYTDVPTLHYANKVGFHNIDHQLQETLMQKDMVRQ
>gnl|CDD|180865 PRK07178, PRK07178, acetyl-CoA carboxylase biotin carboxylase subunit
MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPLAGYLNPRRLVNLAV
ETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADL
DEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEV
QILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDAD
GEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLSYKQEDIQHRGFALQFRINAEDPKNDFLPS
FGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALDRGRRALDDMRVQGVKTTIPY
YQEILRNPEFRSGQFNTSFVESHPELTNYSIKRKPEELAAAIAAAIAAHAGL
>gnl|CDD|180866 PRK07179, PRK07179, quorum-sensing autoinducer synthase
QTIDNETQYINMKEKHKNPPLPDFIEERLDKYIEERVNKNWNGKHLVLGKTPGPDAIILQSNDYLNLSGH
PDIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTP
VYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPGIIVVDSVYSTTGTIAPLADIVDIAEEF
GCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFS
STLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIRSESQIIALETGSERNTEVLRDAL
EERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWFWKST
>gnl|CDD|75964 PRK07182, flgB, flagellar basal body rod protein FlgB; Reviewed
MGIHFQKALGVHPMAMQLRLTRAELLSANLANVNTPNFQAKDIDFAAEMQRAKRGNGVMAAPDRSSAQML
STQMSSAQMSSPQMMSSPQIMSSPQIKYRLPYQPSLDGNTVALNVEQAEFSKNALDYQTSLSFLNMKLTG
LKQAIEGK
>gnl|CDD|235953 PRK07188, PRK07188, nicotinate phosphoribosyltransferase; Provisional
RLTNKTFKFDERIGEGWYSAVYFLKTREIIEKFNPNNIVTMQFFQRRENAVLCGTDEVIALLKTFAKDPS
KLKIRYLKDGDIINPFETVLEIEGPYENFGFLEGIIDGILARRTSVATNAYNVVQAANEKPVIFMGDRAD
HYLQQAGDGYAAYIGGISAFSTHAQNEWWGKSGFGTMPHALIQMFNGDVVEACKAYHKTFPEDELIALVD
YNNDVITDSLKVAREFGDKLKGVRVDTSKNMIDKYFIRHPEVLGTFDPRGVNPELIKALRKALDENGGKH
VKIIVSSGFDAKKIREFEAQNVPVDIYGVGSSLLKINIGFTGDAVELNGKKEAKAGRKYRPNPRLERVKL
EK
>gnl|CDD|235954 PRK07189, PRK07189, malonate decarboxylase subunit beta; Reviewed
TDPAALLADRSFIEASARERAAALLDAGSFRELLGPFERVMSPHLPLQGIPPQFDDGVVVGKGTLDGRPV
VVAAQEGRFMGGSVGEVHGAKLAGALELAAEDNRNGIPTAVLLLFETGGVRLQEANAGLAAIAEIMRAIV
DLRAAVPVIGLIGGRVGCFGGMGIAAALCSYLIVSEEGRLGLSGPEVIEQEAGVEEFDSRDRALVWRTTG
GKHRYLSGLADALVDDDVAAFRAAALALLARGPFPAAHRSAEQARLLARLARFDTCRDALDVWRALGIAD
PEAVPDLDAAAFAALAARLSE
>gnl|CDD|235955 PRK07190, PRK07190, FAD-binding protein
MSTQVTDVVIIGAGPVGLMCAYLGQLCGLNTVIVDKSDGPLEVGRADALNARTLQLLELVDLFDELYPLG
KPCNTSSVWANGKFISRQSSWWEELEGCLHKHFLMLGQSYVEKLLDDKLKEAGAAVKRNTSVVNIELNQA
GCLTTLSNGERIQSRYVIGADGSRSFVRNHFNVPFEIIRPQIIWAVIDGVIDTDFPKVPEIIVFQAETSD
VAWIPREGEIDRFYVRMDTKDFTLEQAIAKINHAMQPHRLGFKEIVWFSQFSVKESVAEHFFIQDRIFLA
GDACHIHSVNGGQGLNTGLADAFNLIWKLNMVIHHGASPELLQSYEAERKPVAQGVIETSGELVRSTKYS
ANGTHAQDYVKIVEKRAGYITGMGIRYGEEGLCGSRLFDFEIFQGSEKTRLYSLLDYRKFTLFIFGDCEV
ELNVPEFVKVIHIYPQQEQANFWTRNSPYAGQAILVRPDSYIEWSVPLDQVESLFALAQLTEFNLSH
>gnl|CDD|180871 PRK07191, flgK, flagellar hook-associated protein FlgK; Validated
MNFIRTAFSGMQAAQAHLNATSMNIANMHTPGYSRQGVEQSAIGADGQGGVNAGNGVNVDGIRRLSQQYV
VMQEWQANSQQGYYDAGEQYFNALELVVGNKSTSLATGLNNFFSALSAATQLPDSPPMRQQVIESANAMA
LRFNNVNNFIVQQKKSIGQQRDATVKQINSLTRSIADYNQKILKNRSDGNNISDLLDQRDLQIKKLSGLI
EVRVVQQEDGTYRVSVKNGQPLVNGAVAAELAVDTSSVGTQKLTLHFSGATQGMNMSCGGQLGGLNDYEL
TTLKPLQDSTQEMAKTVADKFNDQLTKGFDMNGAPGKPLFTFNPSDPNGMLQLSAIKPEELALSGDPKPP
GDNSNLFELLEIRSQKTDLPGMGNVSLGDAATALVGYIAITSNQNHSELENAENVRNQAERYWESFSGVN
NDEEAMNLMEYQRAYQSNMKVIATGDKLFSDLLALV
>gnl|CDD|235956 PRK07192, flgL, flagellar hook-associated protein FlgL; Reviewed
MRISTNTLYSTMLRSIQQLQAGLGKLQQQMSTGKRILTPSDDPIASARLLELSREQSNNSQYADNIANLS
NSLNNQEGHLSGVNDQLQSIRSLLVAAGNGSLSDEDRSAMATELRSMLDSLLGLANAKDSEGNYLFSGTA
SNTQPITFDAAGGTYTYNGNSDQRQVQVGEGVQMPVNVTGQSVFQGGGLDVFNTLDKLIDLLETPALPAA
DAALTAAVDEALGAIDDALDNVLTVRTELGSRQNELDLLDGNHEDRKLQYQKILSDLQDLDYAEALSDLS
NQMAALEAAQKTFVKINSLSLFNLI
>gnl|CDD|235958 PRK07194, fliG, flagellar motor switch protein G; Reviewed
SSDNKGMSNLEQAAILLLSMGEEAAAMVMQQLSREEVQRLSQKMARLSGIKVDQARQVLQRFFDDYREQS
GINGASRSYLQRTLNKALGGDIAKSLINSIYGDEIRHRMQRLQWVDPQQLARLIANEHLQMQAVFLAFLP
PESAAAVLKYLPEDRQDDILYRIAQLDDVDRDVVDELDELIERCLAVLSEQSHTKVIGVKQAADIINRFP
GDRQQLMEMLKEHDEEVVNEIEDNMYDFFILSRQSEETLQRLMDEVPMELWAVALKGTEPALRQAILRVM
PKRQAQALEAQIERLGPVPLSRVEQARKEIMALVRELAEAGEIELQLFEEQVVE
>gnl|CDD|180875 PRK07196, fliI, flagellar protein export ATPase FliI
ALDHALKSIENIHLARVAGRLVRVTGLLLESVGCRLAIGQRCRIESVDETFIEAQVVGFDRDITYLMPFK
HPGGVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLD
VGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMA
KSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPS
AFSIIPRLAESAGNSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQS
ISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQEVGHPAL
FSASVEQLTGMFPS
>gnl|CDD|235959 PRK07198, PRK07198, GTP cyclohydrolase II
AMTKSKSSGHIRLTSHPAGGGKAALPIHWGAATAAERGPVIGTLTNPAHRNVIGTHSGSYSVYRALAVAA
GALDREHRPDLTNTAPTDAIGPHPQWGDPGKIVSLDPWGHLVAEVFADEIAAGYDIRPTIAVTKAHINLP
EIHDAIAAGRLKPDGKILLANGDVVVTKAAIEPVWYLPGVAERFGVSETDLRRTLFEQTGGMFPELVTRP
DLEVFLPPIGGQTVYIFGDVTDLADPETELTCRVHDECNGSDVFGSDICTCRPYLTHGIEECIRGAQRGG
VGLIVYNRKEGRALGEVTKFLVYNARKRQVGGDTAATYFARTECVAGVQDMRFQELMPDVLHWLGIRRIH
RLVSMSNMKYDAITGSGIEVGERVPIPDELIPADARVEIDAKKAAGYFTPGPVPDANELAKVKGRGLD
>gnl|CDD|235960 PRK07199, PRK07199, ribose-phosphate diphosphokinase
MQPLLLALPGNEAAAGRLAAALGVEVGRIELHRFPDGESYVRLDSPVAGRTVVLVCSLDRPDEKLLPLLF
AAEAARELGARRVGLVAPYLAYMRQDIAFHPGEAISQRHFARLLSGSFDRLVTVDPHLHRYPSLSEVYPI
PAVVLSAAPAIAAWIRAHVPRPLLIGPDEESEQWVAAVAERAGAPHAVLRKTRHGDRDVEISLPDAAPWA
GRTPVLVDDIVSTGRTLIEAARQLRAAGAASPDCVVVHALFAGDAYSALAAAGIARVVSTDTVPHPSNAI
SLAPLLAEALRREFDDPLPLA
>gnl|CDD|235961 PRK07200, PRK07200, aspartate/ornithine carbamoyltransferase family protein; Validated
MKTVNELIKDLNSLTSHMHEKDFLLTWEKTPDELKAVLDVADALRALREENISTKVFNSGLGISVFRDNS
TRTRFSYASACNLLGLEVQDLDEGKSQIAHGETVRETANMISFMADVIGIRDDMYIGKGNAYMREVGAAV
DDGYKQGVLPQRPTLVNLQCDIDHPTQSMADLLHLIEHFGGLENLKGKKIAMTWAYSPSYGKPLSVPQGI
IGLMTRFGMDVTLAHPEGYDLMPEVVEVAKKNAKASGGSFRQVNSMEEAFKDADIVYPKSWAPYKVMEER
TELYRAGDHEGIKALEKELLAQNAQHKDWHCTEEMMKLTKDGKALYMHCLPADISGVSCKEGEVTESVFD
RYRIALYKEASWKPYIIAAMIFLRKYKNPGALLEQLLKEAQPRVK
>gnl|CDD|235962 PRK07201, PRK07201, SDR family oxidoreductase
MRYFVTGGTGFIGRRLVSRLLDRRREATVHVLVRRQSLSRLEALAAYWGADRVVPLVGDLTEPGLGLSEA
DIAELGDIDHVVHLAAIYDLTADEEAQRAANVDGTRNVVELAERLQAATFHHVSSIAVAGDYEGVFREDD
FDEGQGLPTPYHRTKFEAEKLVREECGLPWRVYRPAVVVGDSRTGEMDKIDGPYYFFKVLAKLAKLPSWL
PMVGPDGGRTNIVPVDYVADALDHLMHKDGRDGQTFHLTDPKPQRVGDIYNAFARAAGAPPDARLFGFLP
GFVAAPLLAALGPVRRLRNAVATQLGIPPEVLDFVNYPTTFDSRETRAALKGSGIEVPRLASYAPRLWDY
WERHLDPDRARRRDLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGG
TAHAYTCDLTDSAAVDHTVKDILAEHGHVDYLVNNAGRSIRRSVENSTDRFHDYERTMAVNYFGAVRLIL
GLLPHMRERRFGHVVNVSSIGVQTNAPRFSAYVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPMI
APTKRYNNVPTISPEEAADMVVRAIVEKPKRIDTPLGTFAEVGHALAPRLARRILHQLYLMFPDSAAAKG
ISPRRSARARVSREQRALARLMPGIHW
>gnl|CDD|235963 PRK07203, PRK07203, putative aminohydrolase SsnA
MLLIGNGTAITRDPAKPVIEDGAIAIEGNVIVEIGTTDELKAKYPDAEFIDAKGKLIMPGLINSHNHIYS
GLARGMMANIPPPPDFISILKNLWWRLDRALTLEDVYYSALICSLEAIKNGVTTVFDHHASPNYIGGSLF
TIADAAKKVGLRAMLCYETSDRDGEKELQEGVEENIRFIKHIDEAKDDMVEAMFGLHASFTLSDATLEKC
REAVKETGRGYHIHVAEGIYDVSDSHKKYGKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFV
VHNPESNMGNAVGYNPVLEMIKNGILLGLGTDGYTSDMFESYKVANFKHKHAGGDPNVGWPESPAMLFEN
NNKIAERYFGAKFGILEEGAKADLIIVDYNPPTPLNEDNINGHILFGMNGGSVDTTIVNGKVVMEDRKFL
NFDEESIYARARKAAAKLWKRM
>gnl|CDD|235964 PRK07204, PRK07204, beta-ketoacyl-ACP synthase III
MKRYISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHFVDGETSSYMGAEAAKKAVEDAKLT
LDDIDCIICASGTIQQAIPCTASLIQEQLGLQHSGIPCFDINSTCLSFITALDTISYAIECGRYKRVLII
SSEISSVGLNWGQNESCILFGDGAAAVVITKGDHSSRILASHMETYSSGAHLSEIRGGGTMIHPREYSEE
RKEDFLFDMNGRAIFKLSSKYLMKFIDKLLMDAGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTI
FEDHGNMIAASIPVALFEAIKQKKVQRGNKILLLGTSAGLSIGGILLEY
>gnl|CDD|235965 PRK07205, PRK07205, hypothetical protein; Provisional
MKSYITEKVQDACVAAIKTLVSYPSVLNEGENGTPFGQAIQDVLEATLDLCQGLGFKTYLDPKGYYGYAE
IGQGEELLAILCHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNK
RIRFIFGTDEETLWRCMNRYNEVEEQATMGFAPDSSFPLTYAEKGLLQAKLVGPGSDQLELEVGQAFNVV
PAKASYQGPKLEAVKKELDKLGFEYVVKENEVTVLGKSVHAKDAPQGINAVIRLAKALVVLEPHPALDFL
ANVIGEDATGLNIFGDIEDEPSGKLSFNIAGLTITKEKSEIRIDIRIPVLADKEKLVQQLSQKAQEYGLT
YEEFDYLAPLYVPLDSELVSTLMSVYQEKTGDDSPAQSSGGATFARTMPNCVAFGALFPGAPQTEHQANE
HIVLEDLYRAMDIYAEAIYRLTTD
>gnl|CDD|180883 PRK07206, PRK07206, hypothetical protein; Provisional
MMKKVVIVDPFSSGKFLAPAFKKRGIEPIAVTSSCLLDPYYYASFDTSDFIEVIINGDIDDLVEFLRKLG
PEAIIAGAESGVELADRLAEILTPQYSNDPALSSARRNKAEMINALAEAGLPAARQINTADWEEAEAWLR
ENGLIDRPVVIKPLESAGSDGVFICPAKGDWKHAFNAILGKANKLGLVNETVLVQEYLIGTEYVVNFVSL
DGNHLVTEIVRYHKTSLNSGSTVYDYDEFLDYSEPEYQELVDYTKQALDALGIKNGPAHAEVMLTADGPR
LIEIGARLDGGLHPDVARLATGDSQLDATVESLADPDVFRETLREGYRLKAHVFNVFLISPAAGVFSNVE
FLEEIQKLPSFKKSHIYVKEGDYVPQTVDLFSQPGTVYLVHKDKEQLWQDYEKIRKMESKGVYLLP
>gnl|CDD|235966 PRK07207, PRK07207, ribonucleoside-diphosphate reductase subunit alpha
DTATTQEESAASRPLAAASQGALAAAAPGQLADYKVIRRNGSVVPFEPSKIAVAMTKAFLAVEGGQAAAS
ARVRETVEQLTEQVVRALVRRRPSGGTFHIEDIQDQVELALMRSGEHKVARAYVLYREKRAQERAAEAEA
AAAEAHPGLNVTLDDGVRRPLDMARLRALIEEACEGLEAVDAEPILAETLKNLYDGVPMDEVYKALILAA
RTLIEKEPNYSYVTARLLLDTLRREALGFLGVPEEVTQAEMATRYAEYFPAFIKKGIEAELLDPKLAQFD
LERLGAALDPERDLQFTYLGLQTLYDRYFLHVDGTRIELPQAFFMRVAMGLALNEIDREARAIEFYNLLS
SFDFMSSTPTLFNSGTLRPQLSSCYLTTVPDDLDGIYEAIKDNALLSKFAGGLGNDWTPVRALGSHIKGT
NGKSQGVVPFLKVVNDTAVAVNQGGKRKGAVCAYLETWHLDIEEFLELRKNTGDDRRRTHDMNTANWIPD
LFMKRVMEDGEWTLFSPSEVPDLHDLFGKAFEEAYTAYEAKAARGEIKLFKKIPAVDLWRKMLSMLFETG
HPWITFKDPCNLRSPQQHVGVVHSSNLCTEITLNTSDDEIAVCNLGSVNLVAHIKDGAKLDHEKLKRTVS
TAMRMLDNVIDINYYAVPKARNSNLRHRPVGLGIMGFQDALYLLRIPYASDEAVEFADRSMEAVSYYAIW
ASTELAEERGRYSSYEGSLWSRGILPIDSLKLLAEARGGYLEVDRSSTLDWDALRARIKKHGMRNSNCMA
IAPTATISNIIGVSQSIEPTYQNLYVKSNLSGEFTVVNPYLVRDLKARGLWDEVMVNDLKYFDGSLQRID
RIPADLKALYATAFEVDPRWLVEAASRRQKWIDQAQSLNLYMAGASGKKLDETYKLAWLRGLKTTYYLRT
LGATHVEKSTVNTGALNAVSSGGGGAGGAAAAAAAPPAADPKACSIDDPDCEACQ
>gnl|CDD|235967 PRK07208, PRK07208, hypothetical protein; Provisional
MTNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTYKGNRFDIGGHRFFSKSPEVMDL
WNEILPDDDFLLRPRLSRIYYRGKFFDYPLKAFDALKNLGLWRTAKCGASYLKARLRPRKEEDSFEDWVI
NRFGRRLYSTFFKGYTEKVWGVPCDEISADWAAQRIKGLSLGKAIRNALRRSLGLKRRNKEVETSLIEEF
RYPKLGPGQLWETAAEKLEALGGKVVLNAKVVGLHHDGDGRIAVVVVNDTDGTEETVTADQVISSMPLRE
LVAALDPPPPPEVRAAAAGLRYRDFITVGLLVKELNLFPDNWIYIHDPDVKVGRLQNFNNWSPYLVPDGR
DTWLGLEYFCFEGDDLWNMSDEDLIALAIQELARLGLIRPADVEDGFVVRVPKAYPVYDGTYERNVEIIR
DLLDHFPNLHLVGRNGMHRYNNQDHSMLTAMLAVENIIAGETKHDIWQVNTEAEYHEEK
>gnl|CDD|235968 PRK07209, PRK07209, ribonucleotide-diphosphate reductase subunit beta; Validated
MLSWDDEVKAVMPALDALAVATGLEELEGGAARVNVDDKRIINCRADVNQLVPFKYKWAWEKYLAGCANH
WMPQEVNMSRDIALWKSPNGLTEDERRIVKRNLGFFSTADSLVANNIVLAIYRHITNPECRQYLLRQAFE
EAIHTHAYQYIVESLGLDEGEIFNMYHEVPSIRAKDEFLIPFTRSLTDPNFKTGTPENDQKLLRNLIAFY
CIMEGIFFYVGFTQILSLGRQNKMTGIAEQYQYILRDESMHLNFGIDLINQIKLENPHLWTAEFQAEIRE
LIKEAVELEYRYARDTMPRGVLGLNASMFKDYLRFIANRRLQQIGLKPQYPGTENPFPWMSEMIDLKKEK
NFFETRVIEYQTGGALSWD
>gnl|CDD|180887 PRK07211, PRK07211, single-stranded DNA binding protein
MGAIEDVYEDLDTDVSEEEFREAVEEKVEQMGGLADEETAAMLIAHELRDEEVNGIADIEPGMDEVKFLA
KVLSIGDLRTFERDGEDEDGRVINVEVADETGSVRVAFWDEQAVAAEEELEVGQVLRIKGRPKDGYNGLE
VSVDKVEPDPDAEIDVQIGDTYTVEDLSLGLSDVTLVGVVLDTDSVRTFDRDDGSEGRVSNLTVGDETGR
VRVTLWDDRADLAEELDAGESVEIVDGYVRERDGSLELHVGDRGAVEEVDEDVEYVPDTTPIESLEIDET
VDIAGVVRSADPKRTFDRDDGSEGQVRNVRIQDDTGDIRVALWGEKADLDIGPGDEVVAADVEIQDGWQD
DLEASAGWQSTVVVLDDGADAATGTSGDAAAGGGGESAGLSAFAGDGSDADTASSAGSAGASATTGGSEA
ADAAADGDGEEVEFTGTVVQAGDPVVLDDGEETMSVETDADVRLGEEVTVRGSLRDGRIDAEDVF
>gnl|CDD|235969 PRK07213, PRK07213, chlorohydrolase; Provisional
MLVYLNGNFLYGEDFEPKKGNLVIEDGIIKGFTNEVHEGNVIDAKGLVIPPLINAHTHIGDSSIKDIGIG
KSLDELVKPPNGLKHKFLNSCSDKELVEGMKEGLYDMYNNGIKAFCDFREGGIKGINLLKKASSDLPIKP
IILGRPTEADENELKKEIREILKNSDGIGLSGANEYSDEELKFICKECKREKKIFSIHAAEHKGSVEYSL
EKYGMTEIERLINLGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLEKGILLG
IGTDNFMANSPSIFREMEFIYKLYHIEPKEILKMATINGAKILGLINVGLIEEGFKADFTFIKPTNIKFS
KNPYASIITRCESGDIVNKILKGKL
>gnl|CDD|235970 PRK07217, PRK07217, replication factor A; Reviewed
MSDLRQHAEEIHEQFSDLGVDVSVEDVEERLDTLVTEFKVPEDEARRSVTNYYLKEAGIDRDELSGGGGS
ELVNIADIDEPEQWVDVTAKVVQLWEPSSDSIAQVGLLGDETGTIKFTKWAKSDLPELEEGKSYLLKNVV
TDEYQGRFSVKLNRTTSIEELDEDIEVGDDEVEVEGALVDIQSGSGLIKRCPEEDCTRVLQNGRCSEHGK
VEGEFDLRIKGVLDDGEEVQEVIFNREATEELTGITLEEAKQMAMDALDTGVVLDELKEKLLGRYYRVTG
PTLGRYLLADSVEPLTGPVDAEELLIKARSI
>gnl|CDD|180890 PRK07218, PRK07218, Single-stranded DNA binding protein
DMKLDPHAEELASDLGVDKEEVKEELENLVAYSVPIDEAKQSIRRKYGGGGSGGTPSSKDIKELSTDDKN
VTVTGRVLTIGERSIRYQGDDHVIYEGILADETGTISYTAWKDFGLSPGDTVTIGNAGVREWDGRPELNI
GESTTVSLLDDSSLPPYSIGGDKKLIDLGPGDRGVNVEARVLELEHREIDGRDGETTILSGVLADETGRL
PFTDWDPLPEIEIGASIRIEDAYVREFRGVPSVNVSEFTTVEALDREVSVSKDPPRLKIREAVERGGIFD
VELVGNIISVRDGSGLIERCPECGRVIQKGQCRSHGAVEGEDDLRIKAILDDGTGSVTVILDRELTEIVY
GGTLEDAEELAREAMDKDVVAEDIRERLVGREYRVRGNLSVDEYGANLVAESFWVPDDDPAKRAVALLAE
VGP
>gnl|CDD|235971 PRK07219, PRK07219, DNA topoisomerase I; Validated
TELIIAEKNNAARRIADILSGGKAKKKRVNGVPYYEFERKGEKWIVIGLSGHIVTVDFPEEYGDWRDVDP
AELIDADPVKKITKQNYINALKKLAKDADEIIIATDYDREGELIGKEAYHILREVCQVPVKRARFSSLTK
KEIRKAFENPDEIDFNLADAGEARQIIDLYWGAALTRFLSLSVRQLGRWDFLSVGRVQTPTLAFIVDRER
EIRAFDPEDYWKIEALLDKEAQYFYRDLIGGHEAEKFWDEEEAEEIYEKLKGAKEATVSSVKKRERTISP
PAPFNTTEFLREASKIFGISPKRAMEIAEKLYTAGYISYPRTDNTVYPDDLDPKELLKKLSKKKEYGPYA
ESILEQENIKPTEGKKETTDHPPIHPVDVPKREELSDDEWKVYELIVRRFLATLADPAEWEYLKVELDVN
GEIFKASGSRLVEEGWHEVYPYEKFDEKELPDLEEGEKLKVNKIEIEAKETQPPKRYTQSSLIKEMEKRG
LGTKATRHDIIEKLYKRGYVIEGDPPRPTDLGIAVIEALEKYAPEIVSEEMTAQLEADMQAIEDGKKKKE
DVTEESREMLKEILSELKEKRKEIGDHLAGSLKAENRSLKTIGKCPECGGDLIIIRTDKGSRFVGCSGYP
DCRNTFPLPSTGRIKVLDEVCEKCGLPVIKILRGKQTFVVGCPDCEAEKEEEDPDEVIGPCPKCGGELAI
KQLKYGSFLGCTNYPKCKYTLPLPRRGKITVTDEKCPECGLPLLRVKGGFGDELGCCNNPKCNYTEKQKK
EKESKSELEALKGVGAKTAEKLKDAGVETVTDLTAADPDAVAAKVDGVSADR
>gnl|CDD|180892 PRK07220, PRK07220, DNA topoisomerase I; Validated
MHLIITEKNIAARRIAQILAPKKPKKTRVSGVDVYRYEDNGDDTVVVGLSGHIVNIDFPKEYNNWQKVDA
RDLIDAEIITTPTQKKIVTALKKLGKEADRVTIATDYDREGELIGVEALNIIKKVNPDIKFDRVRYSAIT
KKEIERAFSNPVEVDFNLADAGHSRQVIDLVWGAALTRYISLAAGRLGKMFLSVGRVQSPTLALIVDREK
EREAFVPTPYWEIYATLENNGETFVAQHSTRRFWEKEEADRVFEKLGKTAEVTEVEKGTKTDKPPTPFNT
TEFISAANSIGFSAANAMRIAESLYTNGYISYPRTDNTVYPESLDLREQIEIFAEGPFGEYAQKLLEKGE
LVPTRGKKETTDHPPIYPASLAKKSELKEDEWKVYELVVRRFFATFAGPAEWETMKLRFDIGGEEFRANG
SRLTEPGWRWYYPYNAPEDRLLPELSEGEELKVKKKEMLDKETQPPGRYGQGRLIKLMEDLGLGTKATRH
EIISKLYSRAYIHGNPIQPTNTAFAVVDALEKYAPTITKPDMTSRLEEDMDKIAEGKIKEDAVLEESREM
LEQVFDELDKNREKIRESLREGLREDKIIGKCPLCGSDLMVRRSKRGSRFIGCEGYPECTFSLPLPKSGQ
IIVTDKVCEAHGLNHIRIINGGKRPWDLGCPQCNFIEWQKKQKEEKAQQPKKEKPKSIKDIKGIGKKTAE
KLEEAGITTVEALAEADPVELSKTTKISVKKIKSWQESVN
>gnl|CDD|235972 PRK07225, PRK07225, DNA-directed RNA polymerase subunit B'; Validated
MMRKAKVYVNGKLIGTHDDPEELVEEIREARRSGEISEEVNVSYKEETNEVIINTDAGRARRPLIVVENG
EPLLTEEHIEKLKNGELTFDDLVKQGVIEYLDAEEEENAYIAVYEEDLTEEHTHLEIDPSLILGIGAGMI
PYPEHNASPRITMGAGMIKQSLGLPAANYKLRPDTRGHLLHYPQVPLVKTQTQEIIGFDERPAGQNFVVA
VMSYEGYNIEDALIMNKASIERGLGRSHFFRTYEGEERRYPGGQEDRFEIPDKDVRGYRGEEAYRHLDED
GLVNPETEVKEGDVLIGKTSPPRFLEEPDDFGISPEKRRETSVTMRSGEEGIVDTVILTETEEGSRLVKV
RVRDLRIPELGDKFASRHGQKGVIGLIVPQEDMPFTESGVVPDLIINPHAIPSRMTVGHVLEMIGGKVGS
LEGRRVDGTAFSGEDEEDLREALEKLGFEHTGKEVMYDGITGEKIEAEIFVGVIYYQKLHHMVANKLHAR
SRGPVQVLTRQPTEGRAREGGLRFGEMERDVLIGHGAAMLLKERLLDESDKVEIYVCAKCGMIAIYDKKR
NRKYCPICGEETDIYPVEMSYAFKLLLDELKSLGIAPRLELEDKV
>gnl|CDD|235973 PRK07226, PRK07226, fructose-bisphosphate aldolase; Provisional
MMNIGKRIRLERIFNRRTGRTVIVPMDHGVSHGPIDGLVDIRDTVNKVAEGGADAVLMHKGLARHGHRGY
GRDVGLIVHLSASTSLSPDPNDKVLVGTVEEAIKLGADAVSVHVNVGSETEAEMLEDLGEVAEECEEWGM
PLLAMMYPRGPGIKNEYDPEVVAHAARVAAELGADIVKTNYTGDPESFREVVEGCPVPVVIAGGPKTDTD
REFLEMVRDAMEAGAAGVAVGRNVFQHEDPEAITRAISAVVHEGASVEEALKILGLV
>gnl|CDD|180895 PRK07228, PRK07228, 5'-deoxyadenosine deaminase
MTILIKNAGIVTMNAKREIVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLCQTLF
RGIADDLELLDWLKDRIWPLEAAHDAESMYYSALLGIGELIESGTTTIVDMESVHHTDSAFEAAGESGIR
AVLGKVMMDYGDDVPEGLQEDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGVRDLADE
YGVRIHTHASENRGEIETVEEETGMRNIHYLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSS
NLKLASGIAPVPDLLERGINVALGADGAPCNNTLDPFTEMRQAALIQKVDRLGPTAMPARTVFEMATLGG
AKAAGFEDEIGSLEEGKKADLAILDLDGLHATPSHGVDVLSHLVYAAHGSDVETTMVDGKIVMEDGELTT
IDADAVRREANRSIKRLLKRAGLKK
>gnl|CDD|235974 PRK07229, PRK07229, aconitate hydratase; Validated
MGLTLTEKILYAHLVEGELEPGEEIAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVQYVDHNLLQA
DFENADDHRFLQSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDV
ALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATI
TNMGAELGATTSIFPSDERTREFLKAQGREDDWVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVP
VSEVAGIKVDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGA
RILENACGPCIGMGQAPATGNVSLRTFNRNFPGRSGTKDAQVYLASPETAAASALTGVITDPRTLALENG
EYPKLEEPEGFAVDDAGIIAPAEDGSDVEVVRGPNIKPLPLLEPLPDLLEGKVLLKVGDNITTDHIMPAG
AKWLPYRSNIPNISEFVFEGVDNTFPERAKEQGGGIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFA
RIHKANLINFGILPLTFADPADYDKIEEGDVLEIEDLREFLPGGPLTVVNVTKDEEIEVRHTLSERQIEI
LLAGGALNLIKKKLAA
>gnl|CDD|235975 PRK07231, FabG-like, SDR family oxidoreductase
MRLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGGRAIAVAADVSDEADVEA
AVAAALERFGSVDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVA
STAGLRPRPGLGWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGEPTPENRAKFLAT
IPLGRLGTPEDIANAALFLASDEASWITGVTLVVDGGRCVG
>gnl|CDD|235976 PRK07232, PRK07232, bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
EQLKQAALDYHRFPRPGKIEVTPTKPLATQRDLSLAYSPGVAAPCLEIAKDPADAYKYTARGNLVAVISN
GTAVLGLGNIGALASKPVMEGKGVLFKKFAGIDVFDIEVDEEDPDKFIEAVAALEPTFGGINLEDIKAPE
CFYIEEKLRERMDIPVFHDDQHGTAIISAAALLNALELVGKKIEDVKIVVSGAGAAAIACLNLLVALGAK
KENIIVCDSKGVIYKGRTEGMDEWKAAYAVDTDARTLAEAIEGADVFLGLSAAGVLTPEMVKSMADNPII
FALANPDPEITPEEAKAVRPDAIIATGRSDYPNQVNNVLCFPYIFRGALDVGATTINEEMKLAAVRAIAE
LAREEVSDEVAAAYGGQKLSFGPEYIIPKPFDPRLIVKIAPAVAKAAMDSGVATRPIADMDAYREKLEAF
VYKTGLVMKPIFAKAKKDPKRVVFAEGEEERVLRAAQEVVDEGLAKPILIGRPEVIEARIKKLGLDLKAG
VDFEIVNPEDDPRYEEYWQYYYELLQRKGVTPEDARRLVRRDRTVIGAMMVARGDADAMICGLTGRYHEH
LRPVRQVIGLRPGVHTAAAMNALLLKGGNLFIADTYVNEDPTAEELAEIALMAAEEVRRFGIEPRVALLS
HSNFGSSDSPSARKMREAVELLRERAPDLEVDGEMHGDAALNEEIRKDLYPFSRLKGPANVLVMPNLEAA
NISYNLLKELGGGVTIGPILLGMAKPVHILTPSATVRRIVNMTALAVVDAQT
>gnl|CDD|235977 PRK07233, PRK07233, hypothetical protein; Provisional
KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGLPIERFYHHIFKSDEALLELLDELG
LEDKLRWRETKTGYYVDGKLYPLGTPLELLRFPHLSLIDKFRLGLLTLLARRIKDWRALDKVPAEEWLRR
WSGEGVYEVFWEPLLESKFGDYADDVSAAWLWSRIKRRGNRRYSLFGEKLGYLEGGFATLIDALAEAIEA
RGGEIRLGTPVTSVVIDGGGVTGVEVDGEEEDFDAVISTAPPPILARLVPDLPADVLARLRRIDYQGVVC
MVLKLRRPLTDYYWLNINDPGAPFGGVIEHTNLVPPERYGGEHLVYLPKYLPGDHPLWQMSDEELLDRFL
SYLRKMFPDFDRDDVRAVRISRAPYAQPIYEPGYLDKIPPYDTPIEGLYLAGMSQIYPEDRSINGSVRAG
RRVAREILEDRRNA
>gnl|CDD|235978 PRK07234, PRK07234, putative monovalent cation/H+ antiporter subunit D; Reviewed
MTSLTPVWIALPFLLGFAIYLLPKLDRNLALGMAIVSAVYALGLVASMVPLELTLLDNFGVTLRADALSG
YFILTNALVTLAVIFYCWESAKTRFFYAQLLILHGSVNAAFVCADLISLYVALEVLSIATFLLVAYPRTD
RAIWVGLRYLFYSNVAMLFYLIGAVLVYQANGTFAFSGLATADPEAFALIALGLLVKGGIFVSGLWLPLT
HSEAEPPVSALLSGVVVKAGVFPLVRCALDVPGLDLIVRIFGVGTALLGVLFALLEKDLKRMLAFSTISQ
LGFILAAPLVGGLYALAHGLVKSTLFLCAGALPSRNFTELISQMLGIGKWIPLTMASFSIAGFPLLAGFV
SKVLTLKNLLPWQAIALNLAAVGTAASFWKFIFLPFSADDEDKKPLPGFWNAIALLLGGLFLANGVYTEA
YTLGNILKALLTIGLGWLPYFLVFRRLILKLPRVLEQFEHLVGVMSLVLV
>gnl|CDD|235979 PRK07235, PRK07235, amidase; Provisional
MAIKRPTLEQLREIAAQFGLDLTDEELASYLSLMQASLDAYDRIDELPDEIPPVKYPRTPGYRPEAEENP
YGAWYVKTSIKGAAEGKLAGKTVALKDNVAVAGVPMMNGSSTLEGFVPSFDATVVTRLLDAGATIVGKAT
CEDLCFSGGSHTSDPGPVHNPRDPGYSAGGSSSGSAALVAAGEVDMAIGGDQGGSIRIPSAWCGIYGMKP
THGLVPYTGAFPIERTIDHLGPMTATVRDNALLLEVIAGRDGLDPRQPAQPPVDDYTAALDRGVKGLKIG
ILREGFGLPNSEPEVDEAVRAAAKRLEDLGATVEEVSIPLHRLALAIWNPIATEGATAQMMLGNGYGFNW
KGLYDTGLLDAFGAGWRERADDLSETVKLVMLLGQYGLERYHGRYYAKARNLARRLRAAYDEALRKYDLL
VMPTTPMVATPLPAPDASREEYVSRALEMIANTAPFDVTGHPAMSVPCGLVDGLPVGLMLVGRHFDEATI
LRAAAAFEASGD
>gnl|CDD|235980 PRK07236, PRK07236, hypothetical protein; Provisional
MTHMSGPRAVVIGGSLGGLFAALLLRRAGWDVDVFERSPTELDGRGAGIVLQPELLRALAEAGVALPADI
GVPSRERIYLDRDGRVVQRRPMPQTQTSWNVLYRALRAAFPAERYHLGETLVGFEQDGDRVTARFADGRR
ETADLLVGADGGRSTVRAQLLPDVRPTYAGYVAWRGLVDEAALPPEARAALRDRFTFQLGPGSHILGYPV
PGEDGSTEPGKRRYNWVWYRNAPAGEELDELLTDRDGTRRPFSVPPGALRDDVLAELRDDAAELLAPVFA
ELVEATAQPFVQAIFDLEVPRMAFGRVALLGDAAFVARPHTAAGVAKAAADAVALAEALAAAAGDIDAAL
AAWEAERLAVGAAIVARGRRLGARLQAQGRDPPERA
>gnl|CDD|180903 PRK07238, PRK07238, bifunctional RNase H/acid phosphatase; Provisional
MKVVVEADGGSRGNPGPAGYGAVVWDADRGEVLAERAEAIGRATNNVAEYRGLIAGLEAAAELGATEVEV
RMDSKLVVEQMSGRWKVKHPDMKPLAAQARELASQFGRVTYTWIPRARNAHADRLANEAMDAAAGGEPWG
PSAAAADADPAKSAAPPAPTAPGWTGARGTPTRLLLLRHGQTELSVQRRYSGRGNPELTEVGRRQAAAAA
RYLAARGGIDAVVSSPLQRARDTAAAAAKALGLDVTVDDDLIETDFGAWEGLTFAEAAERDPELHRAWLA
DTSVAPPGGESFDAVARRVRRARDRLIAEYPGATVLVVSHVTPIKTLLRLALDAGPGVLYRLHLDLASLS
IAEFYPDGPASVRLVNDTSHLR
>gnl|CDD|235981 PRK07239, PRK07239, bifunctional uroporphyrinogen-III synthetase/response regulator domain protein; Validated
MAQADSAPLAGFTVGVTAARRAEELAALLERRGARVVHAPALRIVPLADDDELRAATRALIAAPPDIVVA
TTGIGFRGWVEAADGWGLADELLEALSSARLLARGPKATGAIRAAGLREEWSPASESSAEVLEYLLEEGV
AGKRIAVQLHGATDEWEPLPEFLEALRAAGAEVVPVPVYRWVPPPDPGPLDRLVDAIASRGLDAVTFTSA
PAVAALLERAREMGLLDQLLAALRTDVLAACVGPVTAAPLVRAGVPTSAPERMRLGALARHITEELPLRR
ARTLRAAGHVLEIRGHAVVVDGEVKPLSPAPMALLRALAARPGRVVSREDLLAALPGGGTDEHAVETAVA
RLRTALGDPKLVQTVVKRGYRLAVDPRDDDV
>gnl|CDD|180905 PRK07246, PRK07246, bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
MTQKKLRKYAVVDLEATGAGPNASIIQVGIVIIEGGEIIDSYTTDVNPHEPLDEHIKHLTGITDQQLAQA
PDFSQVARHIYDLIEDCIFVAHNVKFDANLLAEALFLEGYELRTPRVDTVELAQVFFPTLEKYSLSHLSR
ELNIDLADAHTAIADARATAELFLKLLQKIESLPKECLERLLEYADSLLFESYLVIEEALANAKPYSSPD
YIKVQGIVLKKTAASLKPRKLSQDFSINIALLGLEERPKQESFAKLVGEDFHDGPASFIEAQTGIGKTYG
YLLPLLAQSDQRQIIVSVPTKILQDQIMAEEVKAIQEVFHIDCHSLKGPQNYLKLDAFYDSLQQNDDNRL
VNRYKMQLLVWLTETETGDLDEIKQKQRYAAYFDQLKHDGNLSQSSLFYDYDFWKRSYEKAKTARLLITN
HAYFLTRVQDDKDFARNKVLVFDEAQKLMLQLEQLSRHQLNITSFLQTIQKALSGPLPLLQKRLLESISF
ELLQLSEQFYQGKERQLIHDSLSRLHQYFSELEVAGFQELQAFFATAEGDYWLESEKQSEKRVTYLNSAS
KAFTHFSQLLPETCKTYFVSATLQISPRVSLADLLGFEEYLFHKIEKDKKQDQLVVVDQDMPLVTETSDE
VYAEEIAKRLEELKQLQQPILVLFNSKKHLLAVSDLLDQWQVSHLAQEKNGTAYNIKKRFDRGEQQILLG
LGSFWEGVDFVQADRMIEVITRLPFDNPEDPFVKKMNQYLLQEGKNPFYDYFLPMTILRLKQAIGRTMRR
EDQKSAVLILDRRILTKSYGKQILASLAEEFLISQQNFSDVLVEIDRFLI
>gnl|CDD|180906 PRK07247, PRK07247, 3'-5' exonuclease
MKRLETYIAFDLEFNTVNGVSHIIQVSAVKYDDHKEVDSFDSYVYTDVPLQSFINGLTGITADKIADAPK
VEEVLAAFKEFVGELPLIGYNAQKSDLPILAENGLDLSDQYQVDLYDEAFERRSSDLNGIANLKLQTVAD
FLGIKGRGHNSLEDARMTARVYESFLESDQNKEYLEQQEEVTSDNPFAALGGLFD
>gnl|CDD|168880 PRK07248, PRK07248, chorismate mutase
MDLEEIRQEIDQIDDQLVALLEKRMALVEQVVAYKKATGKPVLDTKREQVILDKVSSLVENKAYQETIVA
TFKDIMKRSRDYQTQNI
>gnl|CDD|180907 PRK07251, PRK07251, FAD-containing oxidoreductase
MLTYDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMYGGTCINIGCIPTKTLLVAAEKNLSFEQVMAT
KNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQAGDEKIELTAETIVINTGAVSNVLPIPGLAD
SKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEE
DGITFLLNAHTTEVKNDGDQVLVVTEDETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQ
TSVPGVFAVGDVNGGPQFTYISLDDFRIVFGYLTGDGSYTLEDRGNVPTTMFITPPLSQVGLTEKEAKEA
GLPYAVKELLVAAMPRAHVNNDLRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKK
QIFTHPTMAENLNDLFNI
>gnl|CDD|180908 PRK07252, PRK07252, S1 RNA-binding domain-containing protein
MKIGDKLKGTITGIKPYGAFVALENGTTGLIHISEIKTGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASL
SLRTLEEEKQHFPHRHRFSNSRHKIGFKPLEEQLPIWIEEALQYLKKKKK
>gnl|CDD|235982 PRK07259, PRK07259, dihydroorotate dehydrogenase
RLSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIG
LQNPGVDAFIEEELPWLEEFDTPIIANVAGSTEEEYAEVAEKLSKAPNVDAIELNISCPNVKHGGMAFGT
DPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINTLKGMAIDIKTRKPILANVT
GGLSGPAIKPIALRMVYQVYQAVDIPIIGMGGISSAEDAIEFIMAGASAVQVGTANFYDPYAFPKIIEGL
EAYLDKYGIKSIEEIVGIAHK
>gnl|CDD|180910 PRK07260, PRK07260, enoyl-CoA hydratase; Provisional
FEHIIYEVEDDLATLTLNRPEVSNGFNIPMCQEILEALRLAEEDPSVRFLLINANGKVFSVGGDLVEMKR
AVDEDDVQSLVKIAELVNEISFAIKQLPKPVIMCVDGAVAGAAANMAVAADFCIASTKTKFIQAFVGVGL
APDAGGLFLLTRAIGLNRATHLAMTGEALTAEKALEYGFVYRVAESEKLEKTCEQLLKKLRRGSSNSYAA
IKSLVWESFFKGWEDYAKLELALQESLAFKEDFKEGVRAFSERRR
>gnl|CDD|180911 PRK07261, PRK07261, DNA topology modulation protein
MKIAIIGYSGSGKSTLARKLSQHYNCPVLHLDTLHFQPNWQERDDDDMIADISNFLLKHDWIIDGNYSWC
LYEERMQEADQIIFLNFSRFNCLYRAFKRYLKYRGKTRESMAENCPEKFDWEFIKWILLDGRSKKQKENY
QSVCQKYSHKTIVLKNQKELDQYLKKIRKSY
>gnl|CDD|235983 PRK07269, PRK07269, cystathionine gamma-synthase; Reviewed
MSKDLHINTILAQAGIKSDEATGALVTPLHFSTTYQHPEFGQSTGFDYTRTKNPTRAKLEETLAAIESAD
YALATSSGMSAIVLAFSVFPVGSKVVAVRDLYGGSFRWFNQQEKEGRFHFTYANTEEELIAAIEEDTDIV
YIETPTNPLMVEFDIEKVAKLAHAKGAKVIVDNTFYSPIYQRPIELGADIVLHSATKYLSGHNDVLAGVV
VTNDLELYEKLFYNLNTTGAVLSPFDSYLLMRGLKTLSLRMERSTANAQEVVAFLKKSPAVKEVLYTGKG
GMISFKVADETRIPHILNSLKVFTFAESLGGVESLITYPTTQTHADIPAEVRHSYGLTDDLLRLSIGIED
ARDLIADLKQALEG
>gnl|CDD|180914 PRK07274, PRK07274, single-stranded DNA-binding protein; Provisional
MYNKVILIGRLTATPELVKTANDKSVARVTLAVNRRFKNQNGEREADFINVVLWGKLAETLASYASKGSL
ISIDGELRTRKYEKDGQTHYVTEVLCQSFQLLESRAQRAMRENNVGNDLADLVLEEEELPF
>gnl|CDD|180915 PRK07275, PRK07275, single-stranded DNA-binding protein; Provisional
MINNVVLVGRMTRDAELRYTPSNVAVATFTLAVNRTFKSQNGEREADFINCVIWRQQAENLANWAKKGAL
IGVTGRIQTRNYENQQGQRVYVTEVVADNFQMLESRATREGGSGGSYNGGFNNAPSANSYSAPAQQTPNF
GRDESPFGNSNPMDISDDDLPF
>gnl|CDD|180916 PRK07276, PRK07276, DNA polymerase III subunit delta'; Validated
MDLKQKQPKVFQRFQTILEQDRLNHAYLFSGDFASFEMALFLAQSLFCEQKEGVLPCGHCRSCRLIEQGE
FSDVTVIEPQGQVIKTDTIRELVKNFSQSGYEGKQQVFIIKDADKMHVNAANSLLKVIEEPQSEIYIFLL
TNDENKVLPTIKSRTQIFHFPKNEAYLIQLLEQKGLLKTQAELLAKLAQSTSEAEKLAQNKKFLELIDQA
ERFVTILLKDKDEAYLQVARLVQLADEKEEQDQVLTLLTLLLAQERMQVNVRTQLEAVYQARKMWQSNVS
FQNALEYMVL
>gnl|CDD|180917 PRK07279, dnaE, DNA polymerase III DnaE; Reviewed
MFAQLDTKTVYSFMDSLIDLEKYVERAKELGYQTIGIMDKDNLYGAYHFIEGAQKNGLQPILGLELNIFV
EEQEVTLRLIAKNTQGYKNLLKISTAKMSGKKQFSDLSQYLEGIAVIVPYFDWSETLELPFDYYIGVDQE
TPGSDFKRPILPLRTVRYFESADRETLQMLHAIRDNLSLREVPLVSSDQELISCQSLETLFQERFPQALD
NLEKLVSGISYDFDTDLKLPRFNRDRPAVEELRELAELGLKEKGLWSSPYQERLDKELSVIHDMGFDDYF
LIVWDLLRFGRSQGYYMGMGRGSAAGSLVAYALDITGIDPVKHNLLFERFLNKERYSMPDIDIDLPDIYR
SEFLRYVRNRYGSDHSAQIVTFSTFGAKQAIRDVFKRFGVPEYELSNLTKKISFRDSLASVYEKNISFRQ
IINSKLEYQKAFEIAKRIEGNPRQTSIHAAGVVMSDDDLTNHIPLKYGDDMMITQYDAHAVEANGLLKMD
FLGLRNLTFVQKMQEKVAKDYGIHIDIEAIDLEDKETLALFAAGDTKGIFQFEQPGAINLLKRIKPVCFE
DIVATTSLNRPGASDYTDNFVKRRHGQEKVDLIDPVIAPILEPTYGIMLYQEQVMQIAQVFAGFSLGKAD
LLRRAMSKKNASEMQKMEEDFLQGALELGHSEEKARELFDRMEKFAGYGFNRSHAFAYSALAFQLAYFKA
HYPAVFYDIMLNYSSSDYITDALEFGFEVAKLSINTIPYHDKIENKKIYLGLKNIKGLPRDLAYWIIENR
PFSSIEDFLTRLPENYQKKEFLEPLIKIGLFDSFEKNRQKIINNLDNLFVFVNELGSLFADSSYSWVEAE
DYSETEKYSLEQELLGVGVSKHPLQAIAEKSSRPFTPISQLVKNSEATILVQIQSIRVIRTKTKGQQMAF
LSVTDTKKKLDVTLFPETYRQYKDELKEGKFYYLKGKIQERDGRLQMVLQQIQEASSERFWILLENHEHD
QEISEILGAFPGSIPVIIHYQEEKETIQSTHIFVAKSEELEEKLSEFVLKTVYR
>gnl|CDD|180918 PRK07281, PRK07281, methionyl aminopeptidase
MITLKSAREIEAMDRAGDFLASIHIGLRDLIKPGVDMWEVEEYVRRRCKEENVLPLQIGVDGAMMDYPYA
TCCGLNDEVAHAFPRHYILKEGDLLKVDMVLSEPLDKSIVDVSKLNFDNVEQMKKYTESYRGGLADSCWA
YAVGTPSDEVKNLMDVTKEAMYRGIEQAVVGNRIGDIGAAIQEYAESRGYGVVRDLVGHGVGPTMHEEPM
VPNYGTAGRGLRLREGMVLTIEPMINTGTWEIDTDMKTGWAHKTLDGGLSCQYEHQFVITKDGPVILTSQ
GEERTY
>gnl|CDD|180919 PRK07282, PRK07282, acetolactate synthase large subunit
MEKISLESPKSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKS
TGKLGVAVVTSGPGATNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRE
TADIPRIITEAVHIATTGRPGPVVIDLPKDVSALETDFIYDPEVNLPSYQPTLEPNDMQIKKILKQLSKA
KKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFM
INIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDAKKALQMLLAEPTVHNNTEKWIE
KVTKDKNRVRSYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTM
GFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQESFYEGRT
SESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLEVITEDVPMLIEVDISRKEHVLPMVPAGKSNHEML
GVKFHA
>gnl|CDD|180920 PRK07283, PRK07283, YlxQ-related RNA-binding protein
NNKQKISNLLGLAQRAGRIISGEELVVKAIQSGQAKLVFLANDAGPNLTKKVTDKSNYYQVEVSTVFSTL
ELSAAVGKPRKVLAVTDAGFSKKMRSLM
>gnl|CDD|180922 PRK07308, PRK07308, flavodoxin; Validated
MALAKIVYASMTGNTEEIADIVADKLRELGHDVDVDECTTVDASDFEDADIAIVATYTYGDGELPDEIVD
FYEDLADLDLSGKIYGVVGSGDTFYDYFCKSVDDFEAQFALTGATKGAESVKVDLAAEDEDIERLEAFAE
ELAAKV
>gnl|CDD|235985 PRK07309, PRK07309, pyridoxal phosphate-dependent aminotransferase
MDLTKRFNKQLDKIEVSLIRQFDQSISDIPGILKLTLGEPDFTTPDHVKEAAKRAIDANQSHYTGMAGLL
ELRQAAADFVKEKYNLDYAPENEILVTIGATEALSASLTAILEPGDKVLLPAPAYPGYEPIVNLVGAEIV
EIDTTENDFVLTPEMLEKAILEQGDKLKAVILNYPANPTGVTYSREQIKALADVLKKYDIFVISDEVYSE
LTYTGEPHVSIAEYLPDQTILINGLSKSHAMTGWRIGLIFAPAEFTAQLIKSHQYLVTAATTMAQFAAVE
ALTNGKDDALPMKKEYIKRRDYIIEKMTDLGFKIIKPDGAFYIFAKIPAGYNQDSFKFLQDFARKKAVAF
IPGAAFGPYGEGYVRLSYAASMETIKEAMKRLKEYMEEHAG
>gnl|CDD|235986 PRK07313, PRK07313, phosphopantothenoylcysteine decarboxylase; Validated
MKNILLAVSGSIAAYKAADLTSQLTKRGYQVTVLMTKAATKFITPLTLQVLSKNPVHLDVMDEHDPKLMN
HIELAKRADLFLVAPATANTIAKLAHGIADDLVTSVALALPATTPKLIAPAMNTKMYENPATQRNLKTLK
EDGVQEIEPKEGLLACGDEGYGALADIETILETIENTLKEKT
>gnl|CDD|235987 PRK07314, PRK07314, beta-ketoacyl-ACP synthase II
KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMD
RFIQYGIAAAKQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINM
AAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTR
NDDPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAAR
AMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAI
FSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGGTNASLVFKRYE
>gnl|CDD|180926 PRK07315, PRK07315, fructose-bisphosphate aldolase; Provisional
MAIVSAEKFVQAARDNGYAVGGFNTNNLEWTQAILRAAEAKKAPVLIQTSMGAAKYMGGYKVCKNLIENL
VESMGITVPVAIHLDHGHYEDALECIEVGYTSIMFDGSHLPVEENLKLAKEVVEKAHAKGISVEAEVGTI
GGEEDGIIGKGELAPIEDAKAMVETGIDFLAAGIGNIHGPYPENWEGLDLDHLEKLTEAVPGFPIVLHGG
SGIPDDQIQEAIKLGVAKVNVNTECQIAFANATRKFARDYEANEAEYDKKKLFDPRKFLAPGVKAIQASV
EERIDVFGSANKA
>gnl|CDD|235988 PRK07318, PRK07318, dipeptidase PepV; Reviewed
MTIDWKKEVEKRKDDLIEDLQELLRINSVRDDSKAKEGAPFGPGPVKALEKFLEIAERDGFKTKNVDNYA
GHIEYGEGEEVLGILGHLDVVPAGDGWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIKELGLPL
SKKVRFIVGTDEESGWKCMDYYFEHEEAPDFGFSPDAEFPIINGEKGITTFDLVHFEGENEGDYVLVSFK
SGLRENMVPDSAEAVITGDDLDDLIAAFEAFLAENGLKGELEEEGGKLVLTVIGKSAHGSTPEKGVNAAT
YLAKFLNQLNLDGDAKAFLDFAAEYLHEDTRGEKLGIAYEDDVMGDLTMNVGVFSFDEEKGGTLGLNFRY
PVGTDFEKIKAKLEKLIGVTGVELSEHEHQKPHYVPKDDPLVKTLLKVYEKQTGLKGEEQVIGGGTYARL
LKRGVAFGAMFPGSEDTMHQANEYIEIDDLIKAAAIYAEAIYELAK
>gnl|CDD|180928 PRK07322, PRK07322, adenine phosphoribosyltransferase; Provisional
METYPLTVGGVTRELPLIRVGPDLAIALFVILGDTELTEAAAEALAKRLPTEVDVLVTPETKGIPLAHAL
SRRLGKPYVVARKSRKPYMQDPIIQEVVSITTGKPQLLVLDGADAEKLKGKRVAIVDDVVSTGGTLTALE
RLVERAGGQVVAKAAIFAEGDASNRLDVIYLAHLPLFP
>gnl|CDD|235989 PRK07324, PRK07324, transaminase; Validated
MKIPRFGVEEWLNVYEKSATYDIAESCIDSLTLEELLALAGKNPEAFYQELGQKKLTYGWIEGSPEFKEA
VASLYQNVKPENILQTNGATGANFLVLYALVEPGDHVISVYPTYQQLYDIPESLGAEVDYWQLKEENGWL
PDLDELRRLVRPNTKLICINNANNPTGALMDRAYLEEIVEIARSVDAYVLSDEVYRPLDEDGSTPSIADL
YEKGISTNSMSKTYSLPGIRVGWIAANEEVIDILRKYRDYTMICAGVFDDMLASLALEHRDAILERNRKI
VRTNLAILDEWVAKEPRVSYVKPKAVSTSFVKLDVDMPSEDFCLKLLKETGVLLVPGNRFDLEGHVRIGY
CCDTETLKKGLKKLSEFLREFDS
>gnl|CDD|235990 PRK07326, PRK07326, SDR family oxidoreductase
MMSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNVLGLAADVRDEADVQ
RAVDAIVAAFGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISS
LAGTNFFAGGAAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTPSEKDAWKIQPEDIAQ
LVLDLLKMPPRTLPSKIEVRPSRPPSK
>gnl|CDD|235991 PRK07327, PRK07327, enoyl-CoA hydratase/isomerase family protein
MTMLARYADYPALRFDRPPPGVLEIVLNGPGALNAADARMHRELADIWRDVDRDPDVRVVLIRGEGKAFS
AGGDLALVEEMADDFEVRARVWREARDLVYNVINCDKPIVSAIHGPAVGAGLVAALLADISIAAKDARII
DGHTRLGVAAGDHAAIVWPLLCGMAKAKYYLLLCEPVSGEEAERIGLVSLAVDDDELLPKALEVAERLAA
GSQTAIRWTKYALNNWLRMAGPTFDTSLALEFMGFSGPDVREGLASLREKRAPDFPGD
>gnl|CDD|235992 PRK07328, PRK07328, histidinol-phosphatase; Provisional
KMLVDYHMHTPLCGHAVGTPEEYVQAARRAGLKEIGFTDHLPMYFLPPEWRDPGLAMRLEELPFYVSEVE
RLRARFPDLYVRLGIEADYHPGTEEFLERLLEAYPFDYVIGSVHYLGAWGFDNPDFVAEYEERDLDELYR
RYFALVEQAARSGLFDIIGHPDLIKKFGHRPREDLTELYEEALDVIAAAGLALEVNTAGLRKPVGEIYPS
PALLRACRERGIPVVLGSDAHRPEEVGFGFAEALALLKEVGYTETVVFRARKRRAYPLG
>gnl|CDD|180933 PRK07329, PRK07329, hypothetical protein; Provisional
IRDQHLHTHFSFDSDAKFEDYLTHFDGEIVTTEHLDLSNPYDTGQDDVPDYAKYSAEIAELNEKYGNRIK
KGIEIGYFAPREDDILDFLANKDFDLKLLSVHHNGVYDYLDDEVADMDKKELLQEYFEKMEEAIGRVHDA
DVLAHFDYGLRLFDLTVEELKAFEPQLTRIFAKMIDNDLAFELNTKSMYLYGNEGLYRYAIELYKQLGGK
LFSIGSDAHKLEHYRYNFDDAQKLLKEHGIKEIALI
>gnl|CDD|235993 PRK07331, PRK07331, cobalt transporter CbiM
MHIPDNYLSPSTCAVMGAAMIPIWGKAVKKVKVEISKKKMPLLGIAAAFSFLIMMFNVPLPGGTTGHAVG
GTLIAILLGPWAACLAVTVALAIQALLFGDGGILAFGANCFNMAFIMPFVGYYIYKFIKKWTKSKKGEYI
GAFIGGYIGINVAALFAAIEFGLQPLLFKDASGLPLYSPYPLSVTIPAMLLPHLLVAGILEGIFTALVFS
FIKRVSPGILYEGKKKKLRPLYGLLLALIILTPLGLLAAGTAWGEWGPEELKQRLGFVPKGMENGFSFNA
LFPDYSIAGLPEVLGYILSAVVGVLIFLIIFKIISSLKKNKV
>gnl|CDD|180935 PRK07333, PRK07333, ubiquinone biosynthesis hydroxylase
QCDVVIAGGGYVGLALAVALKQAAPHLPVTVVDAAPAGAWSRDPRASAIAAAARRMLEALGVWDEIAPEA
QPITDMVITDSRTSDPVRPVFLTFEGEVEPGEPFAHMVENRVLINALRKRAEALGIDLREATSVTDFETR
DEGVTVTLSDGSVLEARLLVAADGARSKLRELAGIKTVGWDYGQSGIVCTVEHERPHGGRAEEHFLPAGP
FAILPLKGNRSSLVWTERTADAERLVALDDLVFEAELEQRFGHRLGELKVLGKRRAFPLGLTLARSFVAP
RFALVGDAAHGIHPIAGQGLNLGLKDVAALAEVVVEAARLGLDIGSLDVLERYQRWRRFDTVRMGVTTDV
LNRLFSNDSTLLRSVRDIGLGLVDRLPKLKSFFIRQAAGLTGDTPRLLKGEAL
>gnl|CDD|235994 PRK07334, PRK07334, threonine dehydratase; Provisional
AGLMVTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEER
ARGVIAMSAGNHAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEE
EGLTFVHPYDDPAVIAGQGTVALEMLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYP
SMYAAIKGVALPCGGSTIAEGIAVKQPGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGA
AGLAALLAYPERFRGRKVGLVLSGGNIDTRLLANVLLRGLVRAGRLARLRVDIRDRPGALARVTALIGEA
GANIIEVSHQRLFTDLPAKGAELELVIETRDAAHLQEVIAALRAAGFEARLVE
>gnl|CDD|180937 PRK07337, PRK07337, pyridoxal phosphate-dependent aminotransferase
MRLAARVDAIEPFYVMELAKEAQALERAGRDIIHMGIGEPDFTAPEPVVEAAARALRRGVTQYTSALGLA
PLREAIAAWYARRFGLDVAPERIVVTAGASAALLLACLALVERGDEVLMPDPSYPCNRHFVAAAEGRPVL
VPSGPAERFQLTAADVEAAWGERTRGVLLASPSNPTGTSIAPDELRRIVEAVRARGGFTIVDEIYQGLSY
DAAPVSALSLGDDVITINSFSKYFNMTGWRLGWLVVPEALVGTFEKLAQNLFICASALAQHAALACFEPD
TLAIYERRRAEFKRRRDFIVPALESLGFKVPVMPDGAFYVYADCRGVAHPAAGDSAALTQAMLHDAGVVL
VPGRDFGPHAPRDYIRLSYATSMSRLEEAVARLGKLFG
>gnl|CDD|235995 PRK07338, PRK07338, hydrolase
MVSEERAVLDLIDDRQAPMLEQLIAWAAINSGSRNLDGLARMAELLADAFAALPGEIELIPLPPVEVIDA
DGRTLEQAHGPALHVSVRPEAPRQVLLTGHMDTVFPADHPFQTLSWLDDGTLNGPGVADMKGGIVVMLAA
LLAFERSPLADKLGYDVLINPDEEIGSPASAPLLAELARGKHAALTYEPALPDGTLAGARKGSGNFTIVV
TGRAAHAGRAFDEGRNAIVAAAELALALHALNGQRDGVTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPE
DAAWAEAELKKLIAQVNQRHGVSLHLHGGFGRPPKPIDAAQQRLFEAVQACGAALGLTIDWKDSGGVCDG
NNLAAAGLPVVDTLGVRGGNIHSEDEFVILDSLVERAQLSALILMRLAQGEI
>gnl|CDD|235996 PRK07340, PRK07340, delta(1)-pyrroline-2-carboxylate reductase family protein
TMPVLDAAETAALLPYPALADALAAALLDYAAGRIQSPERLVVPLQGGGVLLSMPASAADLAITKLVTVC
PGNAARGLPTIQGEVVVADAATGERLFLLDGPTVTGRRTAAVSLLAARTLAPAPPGDLLLIGTGVQARAH
LEAFAAGLPVRRVWVRGRTAASAAAFCAHARALGPTAEPLDGEAIPEAVDLVVTATTSRTPVYPEAARAG
RLVVAVGAFTPDMAELAPRTVRGSRLYVDDPAGARHEAGDLIQAGVDWSRVRPLADALRGAWPARGGPVL
FKSVGCAAWDLAACRLARRALSRR
>gnl|CDD|235997 PRK07342, PRK07342, peptide chain release factor 2; Provisional
NKAEDPSLWNDAQEAQKLMRERQQLDDSINGINHLEQTLNDNIELIAMGEEEGDKSIVEDAEKTIRDLKD
EIDRRQIDALLSGEADANDTYLEVHAGAGGTESQDWASMLLRMYTRWAERQGRKVEVLEVHDGEEAGIKS
ATILVKGHNAYGWLKTESGVHRLVRISPYDSNARRHTSFASIWVYPVIDDNIEVDVNESDVRIDTYRSSG
AGGQHVNTTDSAVRITHIPTGIVVQCQQERSQHKNRAKAWSMLRARLYEEELKKREEATNAAAASKTDIG
WGHQIRSYVLQPYQLVKDLRTGVESTNPQDVLDGDLNEFMEAALAHRISGGADMIEDID
>gnl|CDD|180941 PRK07352, PRK07352, F0F1 ATP synthase subunit B; Validated
MMTLLLLATEAEGGFGLNLNLLETNLINLAIVIGLLYYFGRGFLGKILEERREAILQALKEAEERLRQAA
QALAEAQQKLAQAQQEAERIRADAKARAEAIRAEIEKQAIEDMARLKQTAAADLSAEQERVIAQLRREAA
ELAIAKAESQLPGRLDEDAQQRLIDRSIANLGGN
>gnl|CDD|235999 PRK07353, PRK07353, F0F1 ATP synthase subunit B'; Validated
LFDFDATLPLMAVQFVLLTFILNALFYKPVGKVVEEREDYIRTNRAEAKERLAEAEKLEAQYEQQLASAR
KQAQAVIAEAEAEADKLAAEALAEAQAEAQASKEKARREIEQQKQAALAQLEQQVDALSRQILEKLLAAK
>gnl|CDD|180942 PRK07354, PRK07354, F0F1 ATP synthase subunit C; Validated
MDSITSAASVVAAALAVGLAAIGPGIGQGNAAGGAVEGIARQPEAEGKIRGTLLLSLAFMESLTIYGLVV
ALVLLFANPFA
>gnl|CDD|236000 PRK07360, PRK07360, FO synthase subunit 2; Reviewed
PMTDQIFEDILERARKGKDLSKEDALELLETTEPRRIFEILELADRLRKEQVGDTVTYVVNRNINFTNIC
EGHCGFCAFRRDEGDHGAFWLTIAEILEKAAEAVKRGATEVCIQGGLHPAADSLEFYLEILEAIKEEFPD
IHLHAFSPMEVYFAAREDGLSYEEVLKALKDAGLDSMPGTAAEILVDEVRRIICPEKIKTAEWIEIVKTA
HKLGLPTTSTMMYGHVETPEHRIDHLLILREIQQETGGITEFVPLPFVHENAPLYERGRVKGGAPGLEDL
LLYAVSRIFLGNWIKNIQASWVKLGLKLAQVALNCGANDLGGTLMEEHITKMAGASGGTYMSVEELQWMI
KSIGRIPKQRDTLYEIIEVID
>gnl|CDD|180944 PRK07362, PRK07362, NADP-dependent isocitrate dehydrogenase
MAMYEKLTPPSTGSKITFKNGKPVVPDNPIIPFIRGDGTGVDIWPATQKVLDAAVAKAYGGERKINWFKV
YAGDEACDLYGTYQYLPEDTLEAIREYGVAIKGPLTTPIGGGIRSLNVALRQIFDLYSCVRPCRYYAGTP
SPHKNPEKLDVIVYRENTEDIYMGIEWEAGDEIGDKLIKHLNEEVIPASPELGKRQIPLGSGIGIKPVSK
TGSQRHIRRAIEHALRLPGDKRHVTLVHKGNIMKYTEGAFRDWGYELATTEFRDECVTERESWILSNKEK
NPNISIEDNARMIEPGYDSLTPEKKAAICAEVKEVLDSIWSSHGNGKWKEKVLVDDRIADSIFQQIQTRP
QEYSILATLNLNGDYISDAAAAIVGGLGMAPGANIGDNAAIFEATHGTAPKHAGLDRINPGSVILSGVMM
LEYLGWQEAADLITKGLSAAIANKQVTYDLARLMEPPVDPLSCSEFAEAIISHF
>gnl|CDD|180945 PRK07363, PRK07363, NADH-quinone oxidoreductase subunit M
MLSVLLWLPILGAIIIGFFPGNLPSARLRQITLVFAVLVLAWSLFLLTQFDLSDPGMQFQEYLPWNEPLG
LSYSLGVDGLSLPLLVLNSLLTWIAIYSIGENTERPRLYYSLILLINGGIAGALLAQNLLLFFLFYELEL
IPFYLLIAIWGGEKRGYASIKFLIYTAVSGLLVLAAFLGIVWLSGSTSFDYDAISTQNLSLNTQLILLTG
LLLGFGIKIPLVPLHTWLPDAYTEASPAVAILLGGVLAKLGTYGLLRFGLQLFPQTWSLVAPGLAIIGTI
SVIYGALSAIAQKDIKRMVAYSSIGHMGYILVAAAAGTQLSLLGAVAQMISHGLILALLFHLVGIVERKV
GTRDLDVLNGLMNPIRGLPLTSALLVLAGMASAGIPGLVGFVAEFIVFQGSFSTFPIPTLLCIVASGLTA
VYFVILLNRTCFGRLDNKLAYYPKVLWSEKIPALILTALILFLGVQPNWLVRWSEPTTTAMVAAIPPTEQ
TVISQVALKKS
>gnl|CDD|236001 PRK07364, PRK07364, FAD-dependent hydroxylase
MTLTAATSPTLPSTRSLTYDVAIVGGGIVGLTLAAALKDSGLRIALIEAQPAEAAAAKGQAYALSLLSAR
IFEGIGVWEKILPQIGKFRQIRLSDADYPGVVKFQPTDLGTEALGYVGEHQVLLEALQEFLQSCPNITWL
CPAEVVSVEYQQDAATVTLEIEGKQQTLQSKLVVAADGARSPIRQAAGIKTKGWKYWQSCVTATVKHEAP
HNDIAYERFWPSGPFAILPLPGNRCQIVWTAPHAQAKALLALPEAEFLAELQQRYGDQLGKLELLGDRFL
FPVQLMQSDRYVQHRLALVGDAAHCCHPVGGQGLNLGIRDAAALAQVLQTAHQRGEDIGSLAVLKRYERW
RKRENWLILGFTDLLDRLFSNQWWPLVVVRRLGLWLLRHVPPLKRLALRLMTGLKGRTPQLAKRE
>gnl|CDD|180947 PRK07366, PRK07366, LL-diaminopimelate aminotransferase
MQFAQRLQPLQSNVFADMDRAKAQARAAGKELIDLSLGSSDLPAPAHALEAIAQSLHDPSTHGYLLFHGT
LDFREAAAQWYEQRFGLAVDPETEVLPLIGSQEGTAHLPLAVLNPGDFALLLDPGYPSHAGGVYLAGGQI
YPMPLRAENDFLPVFADIPTEVLAQARLMVLSYPHNPTTAIAPLSFFQEAVAFCQQHDLVLVHDFPYVDL
VFDGEVEPPSILQADPEKSVSIEFFTLSKSYNMGGFRIGFAIGNAQLIQALRQVKAVVDFNQYRGILNGA
IAALTGPQATVQQTVQIFRQRRDAFINALHQIGWPVPLPEATMYVWAKLPEPWQGNSVEFCTQLVAQTGV
AASPGSGFGKSGEGYVRFALVHDPDILEEAVERIAAFL
>gnl|CDD|236002 PRK07369, PRK07369, dihydroorotase; Provisional
MSNELLQQVRVLDPVSNTDRIADVLIEDGKIQAIEPHIDPIPPDTQIIDASGLILGPGLVDLYSHSGEPG
FEERETLASLAAAAAAGGFTRVAILPDTFPPLDNPATLARLQQQAQQIPPVQLHFWGALTLGGQGKQLTE
LAELAAAGVVGFTDGQPLENLALLRRLLEYLKPLGKPVALWPCDRSLAGNGVMREGLLALRLGLPGDPAS
AETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEALASYDPNLRLD
PPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVAFAEAPPGAIGLELALPLLWQNLVETGELSAL
QLWQALSTNPARCLGQEPPSLAPGQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRVLQTWV
>gnl|CDD|180949 PRK07370, PRK07370, enoyl-[acyl-carrier-protein] reductase FabI
MLDLTGKKALVTGIANNRSIAWGIAQQLHAAGAELGITYLPDEKGRFEKKVRELTEPLNPSLFLPCDVQD
DAQIEETFETIKQKWGKLDILVHCLAFAGKEELIGDFSATSREGFARALEISAYSLAPLCKAAKPLMSEG
GSIVTLTYLGGVRAIPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTLASSAVGGILDMIH
HVEEKAPLRRTVTQTEVGNTAAFLLSDLASGITGQTIYVDAGYCIMGM
>gnl|CDD|236003 PRK07373, PRK07373, DNA polymerase III subunit alpha; Reviewed
MVKIISRRSLGVQPVYDIGVAQDHNFLLANGLIASNCFNKSHSTAYAYVTYQTAYLKANYPVEYMAALLT
ANSGNQDKVQKYRENCQKMGIEVEPPDINRSGKDFTPVGEKILFGLSAVRNLGEGAIESILKAREEGGEF
KSLADFCDRVDLRVVNRRALETLIYCGAFDKIEPNRQQLINDLELVIDWAQKRAKEKASGQGNLFDLLGG
NTSNSSAANNAFEQAPSAPPVADFSLQEKLKLEKELLGFYVSEHPLKSIRRPARLLSPINLSELEEQKEK
TKVSAVVMLNEVKKIVTKKGDPMAFLQLEDLSGQSEAVVFPKSYERISELLQVDARLIIWGKVDRRDDQV
QLIVEDAEPIEEVRMVMVELSPQQAGNIVSQHRLKEILQEQAGDKNKAKVPVIAIIQSGGNRQLVRLGQQ
YWVQDEHSAVQALQNAGFNAYAEPLLSQA
>gnl|CDD|168927 PRK07374, dnaE, DNA polymerase III subunit alpha; Validated
MAFVPLHNHSDYSLLDGASQLPKMVERAKELGMPAIALTDHGVMYGAIELLKLCKGKGIKPIIGNEMYVI
NGSIDDPQPKKEKRYHLVVLAKNATGYKNLVKLTTISHLNGMRGRGIFSRPCIDKELLKQYSEGLIVSTA
CLGGEIPQAILRGRPDVARDVAAWYKEVFGDDFYLEIQDHGSIEDRIVNVELVRIAKELGIKLIATNDAH
YLSKNDVEAHDALLCVLTGKLISDEKRLRYTGTEYIKSEEEMLRLFRDHLDPEVIQEAIANTVEVAEKVE
EYDILGTYRMPRFPIPEGHTAVSYLTEVTEQGLLKRLKLNSLDEIDENYKERLSYELKIIEQMGFPTYFL
VVWDYIRFAREQGIPVGPGRGSAAGSLVAYALGITNIDPVKNGLLFERFLNPERKSMPDIDTDFCIERRG
EVIDYVTRRYGEDKVAQIITFNRMTSKAVLKDVARVLDIPYGEADRLAKLIPVVRGKPAKLKAMIGKESP
SPEFREKYEKDPRVKKWVDMAMRIEGTNKTFGVHAAGVVIASDPLDELVPLQRNNDGQVITQYFMEDIES
LGLLKMDFLGLKNLTMIEKTLELVEQSTGERIDPDNLPLDDEKTFELLARGDLEGIFQLESSGMRQVVRD
LKPSSLEDISSILALYRPGPLDAGLIPKFINRKHGREAIDFAHPLLEPILTETYGIMVYQEQIMKIAQDL
AGYSLGQADLLRRAMGKKKVSEMQKHRGIFVEGASKRGVDEKVADELFDQMVLFAEYCFNKSHSTAYGAV
TYQTAYLKAHYPVAYMAALLTVNAGSSDKVQRYISNCNSMGIEVMPPDINRSGIDFTPKGNRILFGLSAV
KNLGDGAIRNIIAARDSDGPFKSLADLCDRLPSNVLNRRSLESLIHCGALDAFSPNANRAQLIADLDLVL
DWASSRARDRASGQGNLFDLLAGSEEEASNDLSSAPKAAPVPDYPPTEKLKLEKELLGFYLSDHPLKQLT
EPAKLLAPISLSSLEEQPDKAKVSAIAMIPEMKQVTTRKGDRMAILQLEDLTGSCEAVVFPKSYERLSDH
LMTDTRLLVWAKVDRRDDRVQLIIDDCREIDDLRLLLVELDPDQASDIRVQHKLRECLQKHRPERDELGV
KIPVVAAVRNGNSVRYVRLGHQFCVKDAQAAVKALQQKSFQARSSSLLVV
>gnl|CDD|236004 PRK07375, PRK07375, Na+/H+ antiporter subunit C
MQLMIYALAIALLVIGLYGLIFKRNLLKKIIGLDVFQTGVNLFYIAIGYRSGGGVPILSPSGFTTYADPL
PQALVLTAIVIGFATTAVMLALIVKLYKDYGTLSESEIEKED
>gnl|CDD|236005 PRK07376, PRK07376, NADH-quinone oxidoreductase subunit L
MESAYQYAWLIPVLPLLGAVLVGLGLISFNQTTNRLRQPVAVLLISLVGAAAVLSYALLWSQIQGHEPYE
RLFEWASAGDFHLPMGYVIDPLGAVMLVLVTTVALLVMIYSDGYMAHDPGYVRFFAYLSLFSSSMLGLVI
SPNLVQIYVFWELVGMCSYLLVGFWYDRKGAADAAQKAFVVNRVGDFGLLLGILGLFWATGSFDFDGIAD
RLSELVSSGAVSGWLALLLCILVFLGPMAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGVFLVARM
YPVFEQFPAVMTVIAWTGAITAFLGASIALTQNDIKKGLAYSTISQLGYMVMAMGCGAYSAGLFHLMTHA
YFKAMLFLGSGSVIHGMEEVVGHDPVLAQDMRLMGGLRKYMPITAITFLIGCLAISGIPPFAGFWSKDEI
LGAAFEANPALWFVGFLTAGMTAFYMFRMYFLTFEGEFRGNDKELQKELLAAADAPGHHEGHHEEHGEHH
HHSGSPHESPWTMTLPLVVLAVPSVLIGLLGTPWNNRFEAFLHAPGEALEAAAHFEWGEFLILAGASVGI
ALIGITLASLMYLLKKIDPAAIAERFPPLYQFSLNKWYLDDIYEKLFVKGSRRLARQVLEVDYKVVDGVV
NLTGLVTLGSGEGLKYFENGRAQFYALIVFGAVLGLVIVFGVT
>gnl|CDD|236006 PRK07377, PRK07377, hypothetical protein; Provisional
NDSYLYVITALLPLTALLLVLQVNPYHALVIRGILGAIAALVYALLGAADVALTEALVGTMLAITLYAVA
VRSSLVMRLGVLEIETETSSVFDQLIDQLRTILDKYHLRLELVVYPDLQALEQALRDKEVHAICLESGSP
HAEEDEAYQLVTRVQRLYEILKPELTSSLTTLTYINLPNTEEKH
>gnl|CDD|236008 PRK07390, PRK07390, NAD(P)H-quinone oxidoreductase subunit F; Validated
MLQFLLQTSWLIPLYGLIGALLSLPWSPGIIRRTGPRPAAYLNLLMTLLAFVHSLLALRAIWNQPPQQLS
FPWLQVADLDLSLSLEISPVTLGALELITGLSLLAQIYALGYLEKDWGLARFFALLGFFEAAMSGLALSD
SLFFSYVLLEILTLSTYLLVGFWYAQPLVVTAARDAFLTKRVGDLLLLMGVVALSPLAGTLNFSDLAAWA
ATANLDPLTATLLGLALIAGPTGKCAQFPLHLWLDEAMEGPNPASILRNSVVVATGAWVLIKLQPVLALS
PVALTVLIVIGTVTAIGASLVAIAQIDIKRALSYSTSAYLGLVFIAVGLQQPDIALLLLLTHAIAKALLF
MSVGSIILTTITQDLTELGGLWSRMPATTLAFLVGSAGLVALLPLGGFWALLRLADGLWAVSPWLVGVLL
LVNALTAFNLTRVFRLVFLGKPQQKTRRSPEVLWPMALPMVILAGFTLHLPLLLQQWGLLPSWEALNLWA
APLLVASGLLGVLLGAWIYLNKAWSRPIQLPLRFLQDLLAYDFYTDRLYRLTIVFVVALISRLTAWFDRY
VVDGLVNLVGLATLFSGQGLKYSVSGQSQFYVLTILLGVALLGALLLWSLLLL
>gnl|CDD|168934 PRK07394, PRK07394, hypothetical protein; Provisional
MSERFRELLKKVGSGEHTSKDLTREEAADALKLMLLGEATPAQIGAFLIAHRIKRPTPEELAGMLDTYDE
LGPKLQSPSNQRPPIVFGMPYDGRSRTAPIYPLTALILAAAGQPVVLHGGDRMPTKYGVPLVELWQGLGV
DLTGLSLEQVQEGFEQTGLAFIYQPDHFPLAESLIPYRDEIGKRPPLATLELIWTPHQGDHHLVSGFVHP
PTEARAWEALELRGETNFTTVKGLEGSCDLPISRTAIIGRVQNGHFERLILHPRDYGCGGKDVPWESTEE
WLEQAQAALNGEPGPLTQALIWNGGFYLWRAGISSSLEEGIEKAEELLNSGKALQKLQQLIA
>gnl|CDD|236010 PRK07395, PRK07395, L-aspartate oxidase; Provisional
LSSTILPSQFDVLVVGSGAAGLYAALCLPSHLRVGLITKDTLKTSASDWAQGGIAAAIAPDDSPKLHYED
TLKAGAGLCDPEAVRFLVEQAPEAIASLVEMGVAFDRHGQHLALTLEAAHSRPRVLHAADTTGRAIVTTL
TEQVLQRPNIEIISQALALSLWLEPETGRCQGISLLYQGQITWLRAGAVILATGGGGQVFAQTTNPAVST
GDGVALAWRAGAQLRDLEFFQFHPTALTKPGAPRFLISEAVRGEGAHLVDAQGRRFAFDYHPAGELAPRD
VVSRAIFSHLQKTATDPATAHVWLDLRPIPAERIRRRFPNIIRVCQKWGIDVFQEPIPVAPAAHYWMGGV
VTDLNNQTSIPGLYAVGETASTGVHGANRLASNSLLECLVFAAQLAQLELPIEPPASPDLPPISFIIDAS
QWKNEQEQIQRIRQELPELVWQSAGICREADTLERAIAQVEQWQQQLAALPLSQFLANLPPGQTVSFNGP
DAEQQLRLWAETRNLLDIAYLILKSALFRTESRGGHYRLDYPQTDPAWQVHTLVQGERWWQSP
>gnl|CDD|180958 PRK07396, PRK07396, dihydroxynaphthoic acid synthetase; Validated
YAPVEWQDCKEYEDILYKSADGIAKITINRPEVRNAFRPKTVKEMIDAFADARDDDNIGVIILTGAGDKA
FCSGGDQKVRGYGGYVDDDGVPRLNVLDLQRLIRTCPKPVIAMVAGYAIGGGHVLHLVCDLTIAADNAIF
GQTGPKVGSFDGGYGASYLARIVGQKKAREIWFLCRQYDAQEALDMGLVNTVVPLADLEKETVRWCREML
QNSPMALRCLKAALNADCDGQAGLQELAGNATMLFYMTEEAQEGRNAFNEKRQPDFSKFPRFP
>gnl|CDD|236011 PRK07399, PRK07399, DNA polymerase III subunit delta'; Validated
NLFANLIGQPLAIELLTAAIKQNRIAPAYLFAGPEGVGRKLAALCFIEGLLSQGSPSKNIRRRLEEGNHP
DLLWVEPTYQHQGKLITASEAEEAGLKRKAPPQIRLEQIREIKRFLSRPPLEAPRKVVVIEDAETMNEAA
ANALLKTLEEPGNGTLILIAPSPESLLPTIVSRCQIIPFYRLSDEQLEQVLKRLGDEEILNINFPELLAL
AQGSPGAAIANIEQLQSIPPELLQKLEQPPKSPLEALELAKDISEELDIEQQLWLIDYLQQHYWQKTKNR
QLLKQLEKLRKQLLSYVQPRLAWEVTLLELSQLD
>gnl|CDD|180960 PRK07400, PRK07400, 30S ribosomal protein S1; Reviewed
SRTQNTDADDIGFTHEDFAALLDKYDYHFKPGDIVNGTVFSLEPRGALIDIGAKTAAFMPIQEMSINRVE
GPEEVLQPNETREFFILSDENEDGQLTLSIRRIEYMRAWERVRQLQKEDATVRSEVFATNRGGALVRIEG
LRGFIPGSHISTRKPKEELVGEELPLKFLEVDEERNRLVLSHRRALVERKMNRLEVGEVVVGTVRGIKPY
GAFIDIGGVSGLLHISEISHEHIETPHSVFNVNDEMKVMIIDLDAERGRISLSTKQLEPEPGDMLKDPQK
VFDKAEEMAAKYRQMLLAQAEGGEEPEEEMEEEVAAEE
>gnl|CDD|180961 PRK07402, PRK07402, precorrin-6Y C5,15-methyltransferase subunit CbiT
MLWPYVTPGIPDELFERLPGIPLTKREVRLLLISQLRLEPDSVLWDIGAGTGTIPVEAGLLCPKGRVIAI
ERDEEVVNLIRRNCDRFGVKNVEVIEGSAPECLAQLAPAPDRVCIEGGRPIKEILQAVWQYLKPGGRLVA
TASSLEGLYAISEGLAQLQARNIEVVQAAVNRLETRGFSQVFAAVDPIFILSGEKL
>gnl|CDD|180962 PRK07403, PRK07403, type I glyceraldehyde-3-phosphate dehydrogenase
MIRVAINGFGRIGRNFLRCWLGRENSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNG
KTIKCVSDRNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIGTYVVGVNHHE
YDHEDHNIISNASCTTNCLAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPT
STGAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDL
PLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEWGYSQRVVDLAELVARKWK
>gnl|CDD|180963 PRK07405, PRK07405, RNA polymerase sigma factor SigD; Validated
KTAKTSTDLVRTYLREIGRVPLLTHEEEILYGKQVQRLVALQEIREELAEELGREPTDAEWAKAAKLSEE
ELRSAIAEGEAAKRKMVEANLRLVVSVAKKYLKRNVDLLDLIQEGTIGMQRGVEKFDPTKGYRFSTYAYW
WIRQAITRAIAEKSRTIRLPIHITEKLNKIKKAQRQLSQQLGRAATIGELAEELELTPKQVREYLERARQ
PLSLDLRVGDNQDTELGELLEDTGASPEDFATQSSLQLDLERLMEDLTPQQKEVIALRFGLEDGQPLTLA
KIGERLNISRERVRQIEREALSKLRKRKANIQEYLAS
>gnl|CDD|236012 PRK07406, PRK07406, RNA polymerase sigma factor RpoD; Validated
TPELEDELLLLEEDRQPAATDDLDSDEDEESSSENADELSEKEAKAKALARIKIGPKKVYTEDSIRVYLQ
EIGRIRLLRPDEEIELARKIADLLELEELREQFESELGREPSDKEWAELVDMPLPKFRRRLMLGRRAKEK
MVQSNLRLVVSIAKKYMNRGLSFQDLIQEGSLGLIRAAEKFDHEKGYKFSTYATWWIRQAITRAIADQSR
TIRLPVHLYETISRIKKTTKVLSQEFGRKPTEEEIAESMEMTIEKLRFIAKSAQLPISLETPIGKEEDSR
LGDFIEADGETPEDDVAKNLLREDLEGVLATLSPRERDVLRLRYGLDDGRMKTLEEIGQIFNVTRERIRQ
IEAKALRKLRHPNRNSVLKEYIR
>gnl|CDD|180965 PRK07408, PRK07408, RNA polymerase sigma factor SigF; Reviewed
TTSTESLKSETMELLRAYQQNPSIALRNQLVELNLGLVRKEAHRWSNQCSEPYEDLVQVGSLGLIRAIER
FDPSKGHAFSSFAIPYIRGEIQHYLRDKSPTVRIPRRWQELQRQAKKVRQELRQELGRQPTDQEIAQALD
ISLEEWQEIKLALQNRTPLSLDAPVNQDEDGSTSLGDLLPDPRYRSFQLAQEDRIRLQQALAQLEERTRE
VLEFVFLHDLTQKEAAERLGISPVTVSRRVKKGLDQLKKLLQPEDD
>gnl|CDD|180967 PRK07411, PRK07411, molybdopterin-synthase adenylyltransferase MoeB
MLNPNLDEIQLSKDEYERYSRHLILPEVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDF
DVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPYDVVVDGTDNFP
TRYLVNDACVLLNKPNVYGSIFRFEGQATVFNYEGGPNYRDLYPEPPPPGMVPSCAEGGVLGILPGIIGV
IQATETIKIILGAGNTLSGRLLLYNALDMKFRELKLRPNPERPVIEKLIDYEQFCGIPQAKAAEAAQKAE
IPEMTVTELKALLDSGADDFVLIDVRNPNEYEIARIPGSVLVPLPDIENGPGVEKVKELLNGHRLIAHCK
MGGRSAKALGILKEAGIEGTNVKGGITAWSREVDPSVPQY
>gnl|CDD|180968 PRK07413, PRK07413, cob(I)yrinic acid a,c-diamide adenosyltransferase
MRRRGIGIVTAQDSSERSKGQLHVYDGEGKGKSQAALGVVLRTIGLGICEKRQTRVLLLRFLKGPGRAYD
EDAAIEALQRGFPHLIDQVRTGRAEFFGADEITKFDRQEAQRGWDIAKGAIASGLYSVVVLDELNPVLDL
GLLPVDEVVNTLKSRPEGLEIIITGRAAPQSLLDIADLHSEMRPHRRPTASELGVPFNSSGGIEIYTGEG
KGKSTSALGKALQAIGRGISQDKSHRVLILQWLKGGSGYTEDAAIAALRESYPHLVDHLRSGRDAIVWRG
QQQPIDYVEAERAWEIARAAIASGLYKTIILDELNPTVDLELLPVEPIVQTLLRKPRDTEVIITGRCKNQ
PAYFDLASVHSEMVCHKHYAEQGVDLKRGVDY
>gnl|CDD|168945 PRK07414, PRK07414, P-loop NTPase family protein
MVAQLEVSSANSSLPLPYTIEGLVQVFTSSQRNFFTSVMAQALRIAGQGTPVLIVQFLKGGIQQGPDRPI
QLGQNLDWVRCDLPRCLDTPHLDESEKKALQELWQYTQAVVDEGRYSLVVLDELSLAIQFGLIPETEVLE
FLEKRPSHVDVILTGPEMPESLLAIADQITELRRSHRP
>gnl|CDD|180969 PRK07415, PRK07415, NAD(P)H-quinone oxidoreductase subunit H; Validated
MAQLETRTEPMVLNFGPHHPSMHGVLRLIVTLDGEDVVDCEPVIGYLHRGMEKIAENRTNVMYVPYVSRW
DYAAGMFNEAITVNAPEKLANIPVPKRASYIRVIMLELNRIANHLLWLGPFLADVGAQTPFFYIFREREM
IYDLWEAATGQRLINNNYFRIGGVAADLPYGWLEKCLDFCDYFGPKIDEYEKLITNNPIFRRRIEGLGTI
SREEAINWGLSGPMLRASGVKWDLRKVDHYECYDDFDWDVAWETEGDCLARYRVRIEEMRESVKIIRQAC
KGIPGGPYENLEAKRMAEGKKSEWNGFDYQYVAKKVAPTFKIPNGELYVRLESGKGELGIFIQGNNDVTP
WRWKIRAADFNNLQILPHLLKGAKVADIMAILGSIDVIMGSVDR
>gnl|CDD|180970 PRK07417, PRK07417, prephenate/arogenate dehydrogenase
MKIGIVGLGLIGGSLGLDLRSLGHTVYGVSRRESTCERAIERGLVDEASTDLSLLKDCDLVILALPIGLL
LPPSEQLIPALPPEAIVTDVGSVKAPIVEAWEKLHPRFVGSHPMAGTAESGVEAGQRGLFKNRPWVLTPT
ENTDLNALAIVEELAVSLGSKIYTADPEEHDRAVALISHLPVMVSAALIQTCGTEKDPSVLKLAQNLASS
GFADTSRVGGGNPELGVMMAEYNRAALLRSLASYRQSLDQLEELIEQENWSALEQKLEQTQELRPNFLN
>gnl|CDD|236014 PRK07418, PRK07418, acetolactate synthase large subunit
LTSSPPKIGDSTTVTPQRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAEAEGWLKHILVRHEQ
GAAHAADGYARATGKVGVCFGTSGPGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGIT
LPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIPKDVGQEEFDYVPVEPGSVKPPGYRPTVKGN
PRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVTTTLMGKGAFDEHHPLSVGMLGMHG
TAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRPDVPIVGDVRKVLVKLL
ERSLEPTTPPRTQAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLAPDAYYTTDVGQHQMWAAQFL
RNGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGW
QGMVRQWQESFYGERYSASNMEPGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRR
DENCYPMVPPGKSNAQMVGLPEHPELALAAELIYCSNCGAKNPSTHRFCPECGTKL
>gnl|CDD|236015 PRK07419, PRK07419, 2-carboxy-1,4-naphthoquinone phytyltransferase
VMTTTSMSPSRRKLWLAAIKPPMYSVAIMPILVGTAWALGETGVFRLDQFITFLLAAILILAWENLSNDV
FDADTGIDKNKFHSVVNLTGNKSLVFWLANLFLLLGLLGILAIALQSDWTVLGLVLLCCFLGYLYQGPPF
RLGYQGLGEPLCFLAFGPLAVAAALYSQTPSWSLIPLAASIILGLATSLILFCSHFHQVEDDLAAGKRSP
IVRLGTKRGAQLLPWIVGLIYALELLPVLLGFWPWTTLLSLLSLPFAIKLIRLVRENHDQPEKVSNSKFI
AVRFHFWSGLLLSLGLILAYLLPK
>gnl|CDD|236016 PRK07424, PRK07424, bifunctional sterol desaturase/short chain dehydrogenase; Validated
MVNAWLQAAGLILGSILWVEIVRDSYHALAHQWNPLYRLHNWHHRVFRPDLSVVSEEIYRKAHWYNDVPE
ALVMLLFGTLPVLLLQQWNVPYGWLAWLGVLYTLTFLFGAIARGLGLPNADELTDLTHLPGPFETLPSQW
FVNRPYHWRHHFDNQNAYYCGTFTLVDKLMGTALSLKGKTVAVTGASGTLGQALLKELHQQGAKVVALTS
NSDKITLEINGEDLPVKTLHWQVGQEAALAELLEKVDILIINHGINVHGERTPEAINKSYEVNTFSAWRL
MELFFTTVKTNRDKATKEVWVNTSEAEVNPAFSPLYELSKRALGDLVTLRRLDAPCVVRKLILGPFKSNL
NPIGVMSADWVAKQILKLAKRDFRNIIVTINPLTYLLFPIKEFSVSLYFKLFSRSS
>gnl|CDD|180975 PRK07429, PRK07429, phosphoribulokinase; Provisional
MTSMPDRPVLLGVAGDSGCGKTTFLRGLADLLGEELVTVICTDDYHSYDRKQRKELGITALDPRANNLDI
MYEHLKALKTGQPILKPIYNHETGTFDPPEYIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIA
WKIKRDMAKRGHTYEQVLAEIEAREPDFEAYIRPQRQWADVVIQFLPTQLIDNDEENKVLRVRLVLRPGI
PHPDPAYLFDEGKLTCSYPGIALRYGPDRYMGKPVDVLEVDGHATLEQFDNLEEMIYIEPHLSNTSTKYY
GELTGLLLGHTDYPGSSNGLALFQLLIGYKMRAAYERLTAKEAKLAV
>gnl|CDD|236018 PRK07431, PRK07431, aspartate kinase; Provisional
MALIVQKFGGTSVGSVERIQAVAQRIARTKEAGNDVVVVVSAMGKTTDELVKLAKEISSNPPRREMDMLL
STGEQVSIALLSMALHELGQPAISLTGAQVGIVTESEHGRARILEIKTDRIQRHLDAGKVVVVAGFQGIS
LSSNLEITTLGRGGSDTSAVALAAALGADACEIYTDVPGVLTTDPRLVPEAQLMDEISCDEMLELASLGA
SVLHPRAVEIARNYGVPLVVRSSWSDAPGTLVTSPPPRPRSLGGLELGKPVDGVELDEDQAKVALLRVPD
RPGIAAQLFEELAAQGVNVDLIIQSIHEGNSNDIAFTVAENELKKAEAVAEAIAPALGGAEVLVETNVAK
LSISGAGMMGRPGIAAKMFDTLAEAGINIRMISTSEVKVSCVIDAEDGDKALRAVCEAFELEDSQIEINP
TASGQDEPEVRGVALDRNQAQLAIRNVPDRPGMAASIFGALAEANISVDMIVQSQRCRSDGTRDISFTVP
KEDREAAQKVLRELAKQLPGAEVEDGPAIAKVSIVGAGMPGTPGVAARMFRALADAGINIEMIATSEIRT
SCVVAEDDGVKALQAVHQAFGLAGEEK
>gnl|CDD|180977 PRK07432, PRK07432, S-methyl-5'-thioadenosine phosphorylase
MTQAKIGIIGGSGLYKMEALKDVEEVQLETPFGSPSDALIVGTLDGTRVAFLARHGRNHTLLPTELPFRA
NIYAMKQLGVEYLISASAVGSLKEEAKPLDMVVPDQFIDRTKNRISTFFGEGIVAHIGFGDPICPALAGV
LADAIASLNLPDVTLHRGGTYVCMEGPAFSTKAESNLYRSWGATVIGMTNLPEAKLAREAEIAYATLALV
TDYDCWHPDHDSVTVEMVIGNLHKNAVNAQKVIQETVRRLSANPPVSAAHSALKYAILTPLDKVPAATKE
KLALLLQKYL
>gnl|CDD|236019 PRK07445, PRK07445, O-succinylbenzoic acid--CoA ligase; Reviewed
MEQPLELLKQLSNQDWLIGYNSQRFYQLAQQLYLQLQQLATPRTPPKILLAESDPLQFLAAFLAAVAAGC
PVFLANPHWGQQEWQQVLNLVQPDQIWGLDQLKLSHPPPLPSQGILPNLETGWIMIPTGGSSGQIRFAIH
TWETLTASVQGFQRYFQLQQVNSFCVLPLYHVSGLMQFMRSFLTGGKLVILPYKRLKSGQELPPNPSDFF
LSLVPTQLQRLLQLRPQWLAQFRTILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQIATLKPDDFLA
GNNSSGQVLPHAQITIPANQTGNITIQAQSLALGYYPQILDSQGIFETDDLGYLDAQGYLHILGRNSQKI
ITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPK
HWIPVPQLPRNPQGKINRQQLQQIAVQRLGLP
>gnl|CDD|236021 PRK07451, PRK07451, translation initiation factor
SSSAKSSSSKRIVYQEFGNVDNSAALERGVPDLPPQQQNLRVQATRSGRKGKTVTVITGFQHKPETLAKL
LKQLKTQCGSGGTVKDNTIEIQGDHRQKILEILIKLGYKAKISGG
>gnl|CDD|180984 PRK07454, PRK07454, SDR family oxidoreductase
MSLNSMPRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAI
APGIAELLEQFGCPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINV
SSIAARNAFPQWGAYCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPLWDTETVQADFDRSAMLSP
EQVAQTILHLAQLPPSAVIEDLTLMPSAGAF
>gnl|CDD|180985 PRK07455, PRK07455, bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase
MQQDWLAQLQQHRAIAVIRAPDLELGLQMAEAVAAGGMRLIEITWNSDQPAELISQLREKLPECIIGTGT
ILTLEDLEEAIAAGAQFCFTPHVDPELIEAAVAQDIPIIPGALTPTEIVTAWQAGASCVKVFPVQAVGGA
DYIKSLQGPLGHIPLIPTGGVTLENAQAFIQAGAIAVGLSGQLFPKE
>gnl|CDD|180986 PRK07459, PRK07459, single-stranded DNA-binding protein; Provisional
MSLNSVTLVGRAGRDPEVRYFESGSVVCNLTLAVNRRSRDDEPDWFNLEIWGKTAQVAADYVKKGSLIGI
TGSLKFDRWTDRNTGEDRSKPVIRVDRLELLGSKRDSEGNANPSNSSEIPF
>gnl|CDD|180987 PRK07468, PRK07468, crotonase/enoyl-CoA hydratase family protein
MMFETIRIAVDARGVATLTLNRPEKHNALSARMIAELTTAARRLAADAAVRVVVLTGAGKSFCAGGDLGW
MRAQMTADRATRIEEARRLAMMLKALNDLPKPLIGRIQGQAFGGGVGLISVCDVAIAVSGARFGLTETRL
GLIPATISPYVVARMGEANARRVFMSARLFDAEEAVRLGLLSRVVPAERLDAAVEAEVTPYLSCAPGAVA
AAKALVRALGAPIDEAVIDATIEALADTWETEEAREGIAAFFDKRAPAWRGG
>gnl|CDD|180988 PRK07470, PRK07470, acyl-CoA synthetase; Validated
PMSRRVMNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQM
FESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAG
LDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMAFVITNHLADLMPGTTEQDASL
VVAPLSHGAGIHQLCQVARGAATVLLPSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHS
SLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLPPALHDAEDGPDARIGTCGFERTGME
VQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMY
ISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLP
KRFFFWDALPKSGYGKITKKMVREELEERGLLDLERAP
>gnl|CDD|236022 PRK07471, PRK07471, DNA polymerase III subunit delta'; Validated
MSLPEADREEGAPHPRETTALFGHAAAEAALLDAYRSGRLHHAWLIGGPQGIGKATLAYRMARFLLATPP
PGGDGAVPPPTSLAIDPDHPVARRIAAGAHGGLLTLERSWNEKGKRLRTVITVDEVRELISFFGLTAAEG
GWRVVIVDTADEMNANAANALLKVLEEPPARSLFLLVSHAPARLLPTIRSRCRKLRLRPLAPEDVIDALA
AAGPDLPDDPRAALAALAEGSVGRALRLAGGDGLALYRRLTALLDTLPRLDRRALHALADAAAGRDRAAR
FALFLDLLDRWLARLARAGARGAPPPEAVPGEAALLARLAPDARLRRWAEVWEKIGRRARRTEAVNLDRK
ALVLDVFGLLAEAAR
>gnl|CDD|168961 PRK07473, PRK07473, M20/M25/M40 family metallo-hydrolase
MNPANLPFDSEAMLAGLRPWVECESPTWDAAAVNRMLDLAARDMAIMGATIERIPGRQGFGDCVRARFPH
PRQGEPGILIAGHMDTVHPVGTLEKLPWRREGNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITV
LFTPDEEVGTPSTRDLIEAEAARNKYVLVPEPGRPDNGVVTGRYAIARFNLEATGRPSHAGATLSEGRSA
IREMARQILAIDAMTTEDCTFSVGIVHGGQWVNCVATTCTGEALSMAKRQADLDRGVARMLALSGTEDDV
TFTVTRGVTRPVWEPDAGTMALYEKARAIAGQLGLSLPHGSAGGGSDGNFTGAMGIPTLDGLGVRGADYH
TLNEHIEVDSLAERGRLMAGLLATLE
>gnl|CDD|236023 PRK07474, PRK07474, sulfur oxidation protein SoxY; Provisional
MVFMPMALSRRQALALGGGALAAAVLPPRAAPARAAAVDAAIRKFTGGAPPREGKVKLDVPEIAENGNTV
PVTVSVDSPMTAADYVKAIHVFADGNPQPGVATFHFGPAAGRAEASTRIRLAQTQNVIAIAEMSDGSLWS
AKATVKVTIGGCGG
>gnl|CDD|236024 PRK07475, PRK07475, hypothetical protein; Provisional
MKAKARGGQTIYGASIGILMLDTRFPRIPGDVGNAATWPFPVRYKVVRGATPERVVEGDDPSLLDAFVAA
ARELEAEGVRAITTSCGFLALFQRELAAALGVPVATSSLLQVPLIQALLPAGQKVGILTADASSLTPAHL
LAVGVPPDTSSLPIAGLEEGGEFRRNILENRGELDNEAAEQEVVAAARALLERHPDIGAIVLECTNMPPY
AAAIQRATGLPVFDIVTLINWLHSGLAPRPYYGFL
>gnl|CDD|236025 PRK07476, eutB, threonine dehydratase; Provisional
VSLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGV
VTASTGNHGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLT
MVPPFDDPRIIAGQGTIGLEILEALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHA
SLAAGRPVQVEEVPTLADSLGGGIGLDNRYTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGA
VGIAALLAGKIAARDGPIVVVVSGANIDMELHRRIINGEVAD
>gnl|CDD|180993 PRK07478, PRK07478, short chain dehydrogenase; Provisional
MMRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYA
KALVALAVERFGGLDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIF
TSTFVGHTAGFPGMAAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTPEALAFVAG
LHALKRMAQPEEIAQAALFLASDAASFVTGTALLVDGGVSITRT
>gnl|CDD|180994 PRK07480, PRK07480, putative aminotransferase; Validated
APNNRTTAELQALDAAHHLHPFSDMKALNEKGSRVITRAEGVYLWDSEGNKILDGMAGLWCVNVGYGRKE
LADAAARQMRELPYYNTFFKTTHPPAIELAAKLAEVAPPGFNHVFFTNSGSEANDTVLRMVRHYWALKGK
PQKKVIISRKNGYHGSTVAGASLGGMKYMHEQGDLPIPGIVHIDQPYWFGEGGDMTPEEFGLAAARQLEA
KILELGADNVAAFIGEPIQGAGGVIIPPATYWPEIQRICRKYDILLVADEVICGFGRTGEWFGSQHFGIK
PDLMTIAKGLTSGYIPMGAVGVGDRVAEVLIEEGGEFNHGFTYSGHPVAAAVALANLRILRDEGIVERVR
DDTGPYLQKRLRELADHPLVGEVRGVGLVGAIELVKDKATRERFEAGGGVGTICRDHCFANGLIMRAVGD
RMIISPPLVITHAEIDELVEKARKALDATAAELGAR
>gnl|CDD|168967 PRK07481, PRK07481, hypothetical protein; Provisional
FLMSNNARRFWHPMAHPAEMKARPPIIIVRGDGVYVYDIDGKKLLDGVGGLWNVNVGHNREEVKEAIVRQ
LDELEYYSTFDGTTHPRAIELSYELIDMFAPEGMRRVFFSSGGSDSVETALKLARQYWKVRGQPERTKFI
SLKQGYHGTHFGGASVNGNTVFRRNYEPLLPGCFHVETPWLYRNPFTEQDPEELARICARLLEREIAFQG
PDTIAAFIAEPVQGAGGVIVPPANFWPLVREVCDRHGILLIADEVVTGFGRTGSWFGSRGWGVKPDIMCL
AKGITSGYVPLGATMVNARIADAFEANADFGGAIMHGYTYSGHPVACAAALATLDIVVREDLPANAAKRG
AYLLEGLQPLKERFELVGDVRGKGLMLALDLVADKATREPIDPSKGYANAVADVARENGVLVRPSGTKII
LSPPLVIQREDVDRIVDALDAGLSAVPFQ
>gnl|CDD|236026 PRK07482, PRK07482, hypothetical protein; Provisional
MMQKIDELLAWDRDHFFHPSTHLGDHARGELPGRIVEGGEGIRITDAQGRRYIDAFAGLYCVNVGYGRTE
VAEAIAEQAKELAYYHTYVGHGTEASITLSKRIIDRAPAGMSKVYYGLSGSDANETQIKLVWYYNNVLGR
PEKKKIISRWRGYHGSGVVTGSLTGLSLFHQHFDLPIARVLHTEAPHYYRRADAGMSEEQFSAYCADELE
ELILAEGPDTIAAFIAEPVLGTGGIVPPPAGYWPAIQAVLKKYDILLIADEVVTGFGRLGSMFGSDHYGI
EPDLITVAKGLTSAYAPLSGSIVGEKVWDVLEQGSDEHGAIGHGWTYSGHPICAAAALANLDILERENLV
GNAAEVGAYFRARLRAAFGDHPLVGEVRGVGMLAAVEFVADRDDRTPFDPALKIGPQVSAAALERGVIAR
AMPHGDILGFAPPLVLTRAEADEIVAIAKDAVDEVLGRLLA
>gnl|CDD|236027 PRK07483, PRK07483, aspartate aminotransferase family protein
MTHVFHRSPRATLPVAVAGEGIYLIDATGKRYLDASGGAAVSCLGHSHPRVIAAIHAQIDRLAYAHTSFF
TTEPAEALADRLVAAAPAGLEHVYFVSGGSEAVEAALKLARQYFVEIGQPQRRHFIARRQSYHGNTLGAL
AIGGNAWRREPFAPLLIEAHHVSPCYAYREQRAGESDEAYGQRLADELEAKILELGPDTVAAFVAETVVG
ATAGAVPPVPGYFKRIREVCDRYGVLLILDEVMCGMGRTGTLFACEEDGVAPDLVTIAKGLGAGYQPIGA
VLASDRIYDAIADGSGFFQHGHTYLGHATACAAALAVQRVIAEDGLLANVRARGEQLRARLRERLGQHPH
VGDIRGRGLFVGVELVADRATKAPFDPALKLHARIKREAMARGLMVYPMGGTIDGVRGDHVLLAPPFIIT
AAQIDEIVERLGDAIDAALAAAG
>gnl|CDD|236028 PRK07486, PRK07486, amidase; Provisional
PASPPPDPIVRLSAHALSRAIRRRQVSCVEVMRAYLAHIERVNPAVNAIVALRDRDALLAEAAEKDAALA
RGEYRGWLHGMPQAPKDLAPTKGIRTTLGSPIFADQVPQEDAIVVERMRAAGAIFIGKTNTPEFGLGSHT
YNPVYGATRNPYDPSRSAGGSSGGAAAALALRMLPVADGSDMMGSLRNPAAFNNVYGFRPSQGRVPHGPG
GDVFVQQLGTEGPMGRTVEDVALLLAVQAGYDPRDPLSLAEDPARFAQPLEADLRGKRIAWLGDWGGYLP
MEAGVLELCEAALATLRELGCDVEAALPAFPPERLWRAWLTLRHFLVGGSLLALYRDPARRALLKPEAIW
EIEGGLALTAAQVYEASVIRSAWYQALLRLFERYDFLALPTAQVFPFDAEWRWPRAIAGRAMDTYHRWME
VVVPATLAGLPAISVPVGFNAAGLPMGMQIIGPPRADLAVLQLAHAYEQATDWVQRRPPALLAA
>gnl|CDD|236029 PRK07487, PRK07487, amidase; Provisional
MMQELWRLSAAELAAAVRSRDVSAREAAEAALARLDAVNPAINAVVDHRPEEALAQADAVDAARARGDDP
GPLAGVPVTVKVNVDQAGFATTNGVRLQKDLIAPADSPVVDNLRKAGAVIIGRTNTPAFSYRWFTDNPLH
GRTLNPWDPSLTPGGSSGGAAAAVAAGIGAIAHGTDIGGSIRYPAYACGVHGLRPTLGRVPAYNASSPER
PIGAQLMSVQGPLARTVADLRLALAAMAAPDPRDPWWVPAPLEGPPRPKRVALCVRPDGLDVDPEVEAAL
RDAARRLEDAGWTVEEVDDTPPLREAAELQERLWLGDGYEALLAAAEAEGDPGALAALRGQRAKARPLDL
AGYMNALARRATLTRQWQLFFEDYPLLLMPVSAELPFPDDLDRQGAEGFRRVWEAQLPQIALPFMGLPGL
SVPTGLVGGVPVGVQLVAGRFREDLCLAAGEAIEARGGPPTPIDPVRMG
>gnl|CDD|236030 PRK07488, PRK07488, indoleacetamide hydrolase
TSHRDPDVASLSLTEAAAALRSGRLSCLELVEALLARAAALAPLNAFTTVDAEGALAAARRIDAQRAAGA
ALLLAGVPIVIKDNINTAGMPTTAGTPALLGFVPATDAPVVQRLLDAGAVPLGKANMHELAFGITSNNGA
FGAVRNPYDPARIAGGSSGGTAAAVAARLAPAGLGTDTGGSVRIPAALCGVVGLRPTVGRYSGDGVVPIS
HTRDTVGPIARSVADLALLDAVITGDAALPAPVALAGLRLGVPAAPFWDGLDPDVAAVAEAALAKLAAAG
VTFVELDLPGLHELNEAVGFPIALYEALADLRAYLRENGAGVSFEELVARIASPDVRAIFRDLLDPPQIS
EDAYRAALDVGRPRLQAWYRQAFARHGLDAILFPTTPLTAPPIGDDDTVILNGAAVPTFARVIRNTDPAS
NAGLPGLSLPAGLTPHGLPVGLELDGPAGSDRRLLAIGRALERVLGRLPAPD
>gnl|CDD|236031 PRK07490, PRK07490, hypothetical protein; Provisional
MTMALSDEEQIRVDLAAAFRWIARLGMHEAVANHFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLDADD
PSTAERPDVPDATAWAIHGQIHRRLPHARCVMHVHSVYATALACLADPTLPPIDQNTARFFNRVAVDTLY
GGMALEEEGERLAGLLGDKRRLLMGNHGVLVTGDTVAEAFDDLYYFERACQTYITALSTGQPLRVLSDAV
AEKTARDWEDYPGFSRQHFAELKALLDEEDPSYAD
>gnl|CDD|181001 PRK07494, PRK07494, UbiH/UbiF family hydroxylase
SLMEKEHTDIAVIGGGPAGLAAAIALARAGASVALVAPEPPYADLRTTALLGPSIRFLERLGLWARLAPH
AAPLQSMRIVDATGRLIRAPEVRFRAAEIGEDAFGYNIPNWLLNRALEARVAELPNITRFGDEAESVRPR
EDEVTVTLADGTTLSARLVVGADGRNSPVREAAGIGVRTWSYPQKALVLNFTHSRPHQNVSTEFHTEGGP
FTQVPLPGRRSSLVWVVRPAEAERLLALSDAALSAAIEERMQSMLGKLTLEPGRQAWPLSGQVAHRFAAG
RTALVGEAAHVFPPIGAQGLNLGLRDVATLVEIVEDRPEDPGSAAVLAAYDRARRPDILSRTASVDLLNR
SLLSDFLPVQDLRAAGLHLLYSFGPLRRLFMREGLGPG
>gnl|CDD|236032 PRK07495, PRK07495, 4-aminobutyrate--2-oxoglutarate transaminase
MTNTSLTDRRNAAISRGVGMTTQIYADRAENAEIWDKEGRRYIDFAAGIAVVNTGHRHPRVIAAVKAQLD
RFTHTCHQVVPYENYVRLAERLNALVPGDFAKKTIFVTTGAEAVENAVKIARAATGRSAVIAFGGGFHGR
TFMGMSLTGKVVPYKVGFGAMMPDVYHVPFPVELHGVSVEQSLAALDKLFKADVDPQRVAAIIIEPVQGE
GGFYPAPAAFMKALRELCDQHGILLIADEVQTGFARTGKLFAMEHHEVAADLTTMAKGLAGGFPLAAVTG
RAEIMDAPGPGGLGGTYGGNPLGIAAAHAVLDVIEEEDLCERANQLGNRLKQRLASLRETVPEIADIRGP
GFMNAVEFNDADSGLPSAEFANRVRLKALEKGLILLTCGVHGNVIRFLAPITIQDDVFAEALDILEASIL
EASAA
>gnl|CDD|236033 PRK07500, rpoH2, RNA polymerase factor sigma-32; Reviewed
MAADASADRSMIRSAMKAPYLEREEEHALAYRWKDHRDEDALHRIISAHMRLVISMAGKFRRFGLPMNDL
IQEGYVGLLEAAARFEPDREVRFSTYATWWIRASIQDYILRNWSIVRGGTSSAQKALFFNLRRLRARLAQ
ADEELTKQEIHREIATALGVSLSDVEMMDARLSGPDASLNAPQSEEDEGRSERMDFLVDDSPLPDEQVES
SIDGERRRRWLTQALQTLNERELRIIRERRLREDGATLEALGEELGISKERVRQIEARALEKLRRALLSQ
SPEVAYFAA
>gnl|CDD|236034 PRK07502, PRK07502, prephenate/arogenate dehydrogenase family protein
MSAPLFDRVALIGIGLIGSSLARAIRRLGLAGEIVGADRSAETRARARELGLGDRVTTSAAEAVKGADLV
ILCVPVGASGAVAAEIAPHLKPGAIVTDVGSVKASVIAAMAPHLPEGVHFIPGHPLAGTEHSGPDAGFAE
LFENRWCILTPPEGTDPAAVARLTAFWRALGARVEEMDPEHHDLVLAITSHLPHLIAYTIVGTADDLERV
TESEVIKYSASGFRDFTRIAASDPTMWRDVFLHNKDAVLEMLGRFTEDLAALQRAIRWGDGDALFDLFTR
TRAIRRGIIEAGQDVAAPDFGRQAAKL
>gnl|CDD|181005 PRK07503, PRK07503, methionine gamma-lyase; Provisional
MRDSHNNTGFSTRAIHHGYDPLDHGGALVPPVYLTATFAFPTAEYGAECFAGEEEGHFYSRISNPTLALL
EQRMASLEGGEAAVALASGMGAITATLWTLLRPGDEVIVDQTLYGCTFAFLHHGLGEFGVTVRHVDLTDP
AALKAAISDKTRMVYFETPANPNMRLVDIAAVAEIAHGAGAKVVVDNTYCTPYLQRPLELGADLVVHSAT
KYLGGHGDITAGLVVGGKALADRIRLEGLKDMTGAVMSPFDAFLLMRGLKTLALRMDRHCASAQAVAEWL
ARHPAVELVHYPGLPSFAQHALAQRQMALPGGMIAFELKGGIAAGRRFMNALQLFARAVSLGDAESLAQH
PASMTHSTYTPEERAEHGISEGLVRLSVGLEDVADILADLAQALDACAVAAAA
>gnl|CDD|168979 PRK07504, PRK07504, O-succinylhomoserine sulfhydrylase; Reviewed
MTTEMARKWRPATRLVHSGTLRSQFGETSEALFLTQGFVYDTAEAAEARFKGEDPGFIYSRYSNPTVDMF
EKRMCALEGAEDARATASGMAAVTAAILCQVKAGDHVVAARALFGSCRYVVETLLPRYGIESTLVDGLDL
DNWEKAVRPNTKVFFLESPTNPTLEVIDIAAVAKIANQAGAKLVVDNVFATPLFQKPLELGAHIVVYSAT
KHIDGQGRCLGGVVLSDKAWIEEHLQDYFRHTGPSLSPFNAWTLLKGLETLPVRVRQQTESAAAIADFLA
GHPKVARVIYPGRADHPQADIIAKQMTGGSTLVAFELKGGKEAAFRFLNALKIVRISNNLGDAKSLITHP
ATTTHKNLSPEARAELGISEGFLRLSAGLEDTDDLIEDLAAALKKVRA
>gnl|CDD|181006 PRK07505, PRK07505, hypothetical protein; Provisional
MQHKYRNNKKRINRAEKFWDAAYDEGLNGLTVGEREGILITLADGHTFVNFVSCSYLGLDTHPAIIEGAV
DALKRTGSLHLSSSRTRVRSQILKDLEEALSELFGASVLTFTSCSAAHLGILPLLASGHLTGGVPPHMVF
DKNAHASLNILKGICADETEVETIDHNDLDALEDICKTNKTVAYVADGVYSMGGIAPVKELLRLQEKYGL
FLYIDDAHGLSIYGKNGEGYVRSELDYRLNERTIIAASLGKAFGASGGVIMLGDAEQIELILRYAGPLAF
SQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTEQSGSFLPIRLIYIGDEDTAIKAAKQ
LLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILDEGLA
>gnl|CDD|236035 PRK07508, PRK07508, aminodeoxychorismate synthase component I
PLILFRDDPAGRAVLFADPSEIIRARTPDEFAPALAAMERARAAGKWLAGYLSYEAGYLLEPKLAPLMPE
GRETPLLCFGVFDAPSPEAPAPARPSENAARLRDPVARWDFADYAQRFERLHRHIRAGDCYQANLTFPLD
ARWGGDPLALFWALAARQPVGYGALVDLGGPVILSRSPELFFRVDGEGWIETHPMKGTAPRGATPAEDAR
LRAALLNDEKNQAENRMIVDLLRNDISRISEVGSLDVPELFDIETYPTVHQMVSRVRARLLPGLGLADIF
AALFPCGSITGAPKIRAMEILRELEPGPRDLYCGAIGWIAPDGRMRFNVAIRTLSLFPGGRAVFNVGGGI
VFDSTAEAEYEECLLKARFAVGDTPIPR
>gnl|CDD|181008 PRK07509, PRK07509, crotonase/enoyl-CoA hydratase family protein
MMDRVSVTIEDGIADVRLNRPDKMNALDFAMFEELIATIKRLKKDRGIRAVILSGEGGAFCAGLDVKSVA
SSPGNAVKLLFKRLPGNANLAQRVSLGWRRLPVPVIAALEGVCFGGGLQIALGADIRIAAPDTKLSIMEA
KWGLVPDMAGTVSLRGLVRKDVARELTYTARVFSAEEALELGLVTHVSDDPLAAALALAREIAQRSPDAI
AAAKRLINRSWTASVRALLARESVEQIRLLLGKNQKIAVKAQMKKRAPKFLD
>gnl|CDD|181009 PRK07511, PRK07511, enoyl-CoA hydratase; Provisional
MSAELLSRREGSTLVLTLSNPGARNALHPDMYAAGIEALNTAERDPSIRAVVLTGAGGFFCAGGNLNRLL
ENRAKPPSVQAASIDGLHDWIRAIRAFPKPVIAAVEGAAAGAGFSLALACDLLVAARDAKFVMAYVKVGL
TPDGGGSWFLARALPRQLATELLLEGKPISAERLHALGVVNRLAEPGQALAEALALADQLAAGSPNALAR
IKSLIADAPEATLAAQLEAERDHFVASLHHADALEGIAAFLEKRAPDYKR
>gnl|CDD|236036 PRK07512, PRK07512, L-aspartate oxidase; Provisional
MMEDLRILTGRPVIVGGGLAGLMAALKLAPRPVVVLSPAPLGEGASSAWAQGGIAAALGPDDSPALHAAD
TLAAGAGLCDPAVAALITAEAPAAIEDLLRLGVPFDRDADGRLALGLEAAHSRRRIVHVGGDGAGAAIMR
ALIAAVRATPSITVLEGAEARRLLVDDGAVAGVLAATAGGPVVLPARAVVLATGGIGGLYAVTTNPAGAF
GQGLALAARAGAVIADPEFVQFHPTAIDIGRDPAPLATEALRGEGAILINEDGERFMADIHPGAELAPRD
VVARAVFAEIAAGRGAFLDARAALGAHFATRFPTVYAACRSAGIDPARQPIPVAPAAHYHMGGIAVDADG
RSSLPGLWAAGEVASTGLHGANRLASNSLLEAVVFAARAAEDIAGTPAAAAAPLSAAAAPALDPADLALL
RPIMSRHVGVLRDADGLRRAIAALLPLEAGAGPAADPATVALLIAVAALAREESRGAHFRTDFPLTAPAA
RRTRLTLADALEIARSLAEEAAA
>gnl|CDD|181011 PRK07514, PRK07514, malonyl-CoA synthase; Validated
MNNNLFDALRAAFADRDAPFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALY
LATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVETLDADGTGSLLEA
AAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTH
GLFVATNVALLAGASMIFLPKFDPDAVLALMPRATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAP
LLAETHREFQERTGHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGM
IEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEID
ELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKV
QKNLLREQYADLFA
>gnl|CDD|236037 PRK07515, PRK07515, 3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
HNVVISGTGLYTPPESISNEELVASFNAYVERFNAENAAAIAAGEVEALQPSSSEFIEKASGIKSRYVMD
KEGILDPDRMRPRIPERSNDELSIQAEMGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQ
ALGIEGFAFDMNVACSSATFGIQTAANAIRSGSARRVLVVNPEICSGHLNFRDRDSHFIFGDVATAVIVE
RADTATSAGGFEILGTRLFTQFSNNIRNNFGFLNRADPEGIGARDKLFVQEGRKVFKEVCPMVAEHIVEH
LAENGLTPADVKRFWLHQANINMNQLIGKKVLGRDATPEEAPVILDEYANTSSAGSIIAFHKHSDDLAAG
DLGVICSFGAGYSIGSVIVRKR
>gnl|CDD|181013 PRK07516, PRK07516, thiolase domain-containing protein
MMTASIVGWAHTPFGKLDAETLESLIVRVAREALAHAGIAAGDVDGIFLGHFNAGFSPQDFPASLVLQAD
PALRFKPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPTAEVGDILLGASYLKEEGDTP
GGFAGVFGRIAQAYFQRYGDQSDALAMIAAKNHANGVANPYAQMRKDLGFEFCRTVSEKNPLVAGPLRRT
DCSLVSDGAAALVLADAETARALQRAVRFRARAHVNDFLPLSRRDPLAFEGPRRAWQRALAQAGVTLDDL
SFVETHDCFTIAELIEYEAMGLAPPGQGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATGVSMHVLAA
MQLTGEAGGMQIPGAKLAGVFNMGGAAVANYVSILERVK
>gnl|CDD|236038 PRK07521, flgK, flagellar hook-associated protein FlgK; Validated
MSLSSALNTAQSGLTATSRQTSVVSRNIANAGTPGYSRREASLVSGPAGGQVVGISRAQDPALLAQRLLA
TSAAAAQDTLADGLERLASTVGDNDYEGSPSARLSDFQAALQTAASSPDNTTLAQAAVDAAQDLANSLND
ASDAVQSARADADAEIADSVDTLNDLLAQFEDANNAVVSGTATGRDASDALDQRDKLLKQISQIVGVTTV
TRDNNDMALYTDGGVTLFETTPRTVTFTPTATYTAGTTGNAVYIDGVPLTGGSGVMPLAGGSLAALLQLR
DEIAPTYQAQLDEIARGLITRFAESDPTGAAGDPGLFTDSGAPADPAAGEAGLAGRISVNAAVDPSQGGD
PWLLRDGGINGAAYLGANTTGAAGFSTRLNALVDALSAPRTFDSAAGLSGSSSLMDLAASSLSWLEQQRS
SASSEASYASALLSRADEALSNATGVDTDDEMALLLDLEQSYAASAKVISTVDEMLDSLLDAV
>gnl|CDD|236039 PRK07522, PRK07522, acetylornithine deacetylase; Provisional
MASMSSLDILERLVAFDTVSRDSNLALIEWVRDYLAAHGVESELIPDPEGDKANLFATIGPADRGGIVLS
GHTDVVPVDGQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGC
LGVPSMIARLPERGVKPAGCIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAH
LRDLADRLAAPGPFDALFDPPYSTLQTGTIQGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEA
ELLPEMRAVHPEAAIEFEPLSAYPGLDTAEDAAAARLVRALTGDNDLRKVAYGTEAGLFQRAGIPTVVCG
PGSIEQAHKPDEFVELAQLAACEAFLRRLLASLAA
>gnl|CDD|236040 PRK07523, PRK07523, gluconate 5-dehydrogenase; Provisional
MSLNLFDLTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTD
HDAVRAAIDAFEAEIGPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGK
IINIASVQSALARPGIAPYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALVADPEFSAWL
EKRTPAGRWGKVEELVGACVFLASDASSFVNGHVLYVDGGITASL
>gnl|CDD|236041 PRK07524, PRK07524, 5-guanidino-2-oxopentanoate decarboxylase
MTTCGEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFI
ITGPGMTNIATAMGQAYADSIPMLVISSVNRRASLGKGRGKLHELPDQRAMVAGVAAFSHTLMSAEDLPE
VLARAFAVFDSARPRPVHIEIPLDVLAAPADHLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGG
GALAAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGASQSLPAVRALIAEADVVLAVGTELGETDYD
VYFDGGFPLPGELIRIDIDPDQLARNYPPALALVGDARAALEALLARLPGQAAAADWGAARVAALRQALR
AEWDPLTAAQVALLDTILAALPDAIFVGDSTQPVYAGNLYFDADAPRRWFNASTGYGTLGYGLPAAIGAA
LGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIA
LARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQACWFAAV
>gnl|CDD|236042 PRK07525, PRK07525, sulfoacetaldehyde acetyltransferase; Validated
MGKMKMTPSEAFVETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMG
MVIGQNGPGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMA
EVLNRVFDKAKRESGPAQINIPRDYFYGVIDVEIPQPVRLERGAGGEQSLAEAAELLSEAKFPVILSGAG
VVLSDAIEECKALAERLDAPVACGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLNPF
GTLPQYGIDYWPKDAKIIQVDINPDRIGLTKKVSVGICGDAKAVARELLARLAERLAGDAGREERKALIA
AEKSAWEQELSSWDHEDDDPGTDWNEEARARKPDYMHPRQALREIQKALPEDAIVSTDIGNNCSIANSYL
RFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNY
QWGAEKKNQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAIDAQNEGKTTVIEIM
CNQELGEPFRRDALKKPVRVLGKYKDDM
>gnl|CDD|236043 PRK07529, PRK07529, AMP-binding domain protein; Validated
MPAFATLADIEAIEAVPLAARDLPASTYELLSRAAARHPDAPALSFLLDADPLDRPETWTYAELLADVTR
TANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANPINPLLEPEQIAELLRAAGAKVLVTLGPFP
GTDIWQKVAEVLAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHARILDFDAELARQPGDRLFSGRPI
GPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARG
AHVVLATPQGYRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVF
RRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVVILDDAGRYLRDCAVDEVGVL
CIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRH
PAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAERAAVPKHVRILDALPKTAVGKIF
KPALRRDAIRRVLRAALRDAGVEAEVVDVVEDGRRGLVAQVALRGAEDREAVAAVLGRYAFPWEISTADP
HA
>gnl|CDD|181018 PRK07530, PRK07530, 3-hydroxybutyryl-CoA dehydrogenase; Validated
MMAIKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLARQVAKGKISEEARAAALA
RISTATDLEDLADCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGI
HFMNPVPVMKLVELIRGIATDEATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIYTLYEGVG
SVEAIDTAMKLGANHPMGPLELADFIGLDTCLSIMQVLHDGLADSKYRPCPLLVKYVEAGWLGRKTGRGF
YDYRGEVPVPTR
>gnl|CDD|236044 PRK07531, PRK07531, carnitine 3-dehydrogenase
MTMIMKAACIGGGVIGGGWAARFLLAGIDVAVFDPHPEAERIIGEVLANAERAYAMLTDAPLPPEGRLTF
CASLAEAVAGADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPY
NPVYLLPLVELVGGGKTSPETIRRAKEILREIGMKPVHIAKEIDAFVGDRLLEALWREALWLVKDGIATT
EEIDDVIRYSFGLRWAQMGLFETYRIAGGEAGMRHFLAQFGPCLKWPWTKLMDVPDLDDALVDKIAGQSD
AQSGGLSIRELERIRDENLVGIMQALKAGDGGKGWGAGKLLADFEARLWAAGGSPADSADLSQPLRLVET
KVPPAWVDYNGHMTEHRYLQVFGDTTDALLRLIGVDAAYVAAGHSYYTVETHIRHLGEAKAGQALHVETQ
LLSGDEKRLHLFHTLYDAGGELIATAEHMLLHVDLKAGKAVPAPAAVLAALKPIAEAHAELPLPEGAGRH
VGQRR
>gnl|CDD|181020 PRK07533, PRK07533, enoyl-[acyl-carrier-protein] reductase FabI
PMQPLLPLAGKRGLVVGIANEQSIAWGCARAFRALGAELAVTYLNDKARPYVEPLAEELDAPIFLPLDVR
EPGQLEAVFARIAEEWGRLDFLLHSIAFAPKEDLHGRVVDCSREGFALAMDVSCHSFIRMARLAEPLMTN
GGSLLTMSYYGAEKVVENYNLMGPVKAALESSVRYLAAELGPKGIRVHAISPGPLKTRAASGIDDFDALL
EDAAERAPLRRLVDIDDVGAVAAFLASDAARRLTGNTLYIDGGYHIVG
>gnl|CDD|236045 PRK07534, PRK07534, betaine--homocysteine S-methyltransferase
MTNALSDLLAERGVLLADGATGTNLFNMGLESGEAPELWNEDHPDNITALHQGFVDAGSDIILTNSFGGT
AARLKLHDAQDRVHELNRAAAEIAREVADKAGRKVIVAGSVGPTGEIMEPMGALTHALAVEAFHEQAEGL
KAGGADVLWVETISAPEEIRAAAEAAKLAGMPWCGTMSFDTAGRTMMGLTPADLADLVEKLGEPPLAFGA
NCGVGASDLLRTVLGFTAQGPERPIIAKGNAGIPKYVDGHIHYDGTPELMAEYAVLARDAGARIIGGCCG
TMPEHLAAMRAALDARPRGPRPSLETIVERLGPFSSASDGTDDAGPARERRGRRRR
>gnl|CDD|181022 PRK07535, PRK07535, methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated
MIIIGERINGTRKSIAEAIEAKDAAFIQKLALKQAEAGADYLDVNAGTAVEEEPETMEWLVETVQEVVDV
PLCIDSPNPAAIEAGLKVAKGPPLINSVSAEGEKLEVVLPLVKKYNAPVVALTMDDTGIPKDAEDRLAVA
KELVEKADEYGIPPEDIYIDPLVLPLSAAQDAGPEVLETIRRIKELYPKVHTTCGLSNISFGLPNRKLIN
RAFLVMAMGAGMDSAILDPLDRDLMGAIAAAEALLGQDPYCRNYLKAFRKG
>gnl|CDD|236046 PRK07538, PRK07538, hypothetical protein; Provisional
MKVLIAGGGIGGLTLALTLHQRGIEVVVFEAAPELRPLGVGINLLPHAVRELAELGLLDALDAIGIRTRE
LAYFNRHGQRIWSEPRGLAAGYDWPQYSIHRGELQMLLLDAVRERLGPDAVRTGHRVVGFEQDADVTVVF
LGDRAGGDLVSVRGDVLIGADGIHSAVRAQLYPDEGPPRWNGVMMWRGVTEAPPFLTGRSMVMAGHLDGK
LVVYPISEPVDADGRQLINWVAEVRVDDAGAPRREDWNRPGDLEDFLPHFADWRFDWLDVPALIRAAEAI
YEYPMVDRDPLPRWTRGRVTLLGDAAHPMYPVGSNGASQAILDARALADALAAHGDPEAALAAYEAERRP
ATAQIVLANRLNGPEGVLQLVEERAPGGFADIDDVISSAELEAIAARYKAAAGFAPEQLNAAP
>gnl|CDD|181024 PRK07539, PRK07539, NADH-quinone oxidoreductase subunit NuoE
MLSAEELAAIEREIAKYPRPRSAVIPALKIVQEQRGWVPDEAIEAVADYLGMPAIDVEEVATFYSMIFRQ
PVGRHVIQVCTSTPCWLRGGEAILAALKKKLGIKPGETTADGRFTLLEVECLGACDNAPVVMINDDTYED
LTPEKIDELLDELK
>gnl|CDD|181025 PRK07544, PRK07544, branched-chain amino acid aminotransferase; Validated
VIPFDDRDGFIWMDGELVPWRDAKVHVLTHGLHYASSVFEGERAYGGKIFKLREHSERLRRSAELLDFEI
PYSVAEIDAAKKETLAANGLTDAYVRPVAWRGSEMMGVSAQQNKIHLAIAAWEWPSYFDPEAKMKGIRLD
IAKWRRPDPETAPSAAKAAGLYMICTISKHAAEAKGYADALMLDYRGYVAEATGANIFFVKDGVIHTPTP
DCFLDGITRQTVIELAKRRGIEVVERHIMPEELAGFSECFLTGTAAEVTPVSEIGEYRFTPGAITRDLMD
DYEALVRPRAAA
>gnl|CDD|169002 PRK07546, PRK07546, hypothetical protein; Provisional
MPDFELIETLRWEPGAGFPRLDRHLARLERSARALGFPCDPAAVRAKLAEAVAGAQGPLRLRLTLARDGR
LTVETAPLPPLPPDTVWRVAIARTRLDSADPLLRYKTTRRAAYDAARAELPPAEADEVILLNERGEVCEG
TITNVFLDRGGGMLTTPPLSCGLLPGVLRAELLDAGRAREAVLTVDDLKSARAIWVGNSLRGLIRAELI
>gnl|CDD|181026 PRK07550, PRK07550, aminotransferase
PLNPLIAALFPPPIPEVRAWLAGYDGADGPLIDLSQAVPGYPPPPELLRALAEAAADPAAHLYGPVEGLP
ELREAYAAHYSRLYGAAISPEQVHITSGCNQAFWAAMVTLAGAGDEVILPLPWYFNHKMWLDMLGIRPVY
LPCDEGPGLLPDPAAAEALITPRTRAIALVTPNNPTGVVYPPELLHELYDLARRHGIALILDETYRDFDS
GGGAPHDLFADPDWDDTLVHLYSFSKSYALTGHRVGAVVASPARIAEIEKFMDTVAICAPRIGQIAVAWG
LPNLADWRAGNRAEIARRRDAFRAVFARLPGWELLASGAYFAYVRHPFPDRPSREVARRLAKEAGILCLP
GTMFGPGQEGYLRLAFANADVAGIGELVERLRAFAP
>gnl|CDD|181027 PRK07558, PRK07558, F0F1 ATP synthase subunit C; Validated
MDAEALKFIGAGLACIGMAGAALGVGNIFGNYLSGALRNPSAADSQFGYLLIGAALAEALGIFSFLIALL
LLFA
>gnl|CDD|181028 PRK07559, PRK07559, 2'-deoxycytidine 5'-triphosphate deaminase; Provisional
STTPARAAGILPDQAIAALIASGAITSERPLDDDQIQPASLDLRLGAKAYRVRASFLPGPGRTVADRLDR
LKLHEIDLTDGAVLETGCVYIVPLLESLALPADLSASANPKSSTGRLDVFTRVITDGAQEFDKIPAGYHG
PLYAEISPRTFPILVRTGSRLSQIRFRRGEARLSDAELAALHAAEPLVDGEDPSGGGIALSVDLSGGEDG
LVGYRAKRHTGVIDVDRIGAHDVLDFWEPLYARGDGELILDPGEFYILASREAVHVPPDYAAEMVPFDPL
VGEFRVHYAGFFDPGFGHAEAGGTGSRAVLEVRSHEVPFILEHGQIVGRLVYERMLERPDALYGAGLGSN
YQGQGLKLSKHFRAW
>gnl|CDD|236047 PRK07560, PRK07560, elongation factor EF-2; Reviewed
GRRKKMVEKILELMKNPEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLALDFDEEEQARGIT
IKAANVSMVHEYEGKEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERV
KPVLFINKVDRLIKELKLTPQEMQQRLLKIIKDVNKLIKGMAPEEFKEKWKVDVEDGTVAFGSALYNWAI
SVPMMQKTGIKFKDIIDYYEKGKQKELAEKAPLHEVVLDMVVKHLPNPIEAQKYRIPKIWKGDLNSEVGK
AMLNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNRVQQVGIYMGPEREEVEE
IPAGNIAAVTGLKDARAGETVVSVEDMTPFESLKHISEPVVTVAIEAKNPKDLPKLIEVLRQLAKEDPTL
VVKINEETGEHLLSGMGELHLEVITYRIKRDYGIEVVTSEPIVVYRETVRGKSQVVEGKSPNKHNRFYIS
VEPLEEEVIEAIKEGEISEDMDKKEAKILREKLIEAGMDKDEAKRVWAIYNGNVFIDMTKGIQYLNEVME
LIIEGFREAMKEGPLAAEPVRGVKVRLHDAKLHEDAIHRGPAQVIPAVRNAIFAAMLTAKPTLLEPIQKV
DINVPQDYMGAVTREIQGRRGKILDMEQEGDMAIIEAEAPVAEMFGFAGEIRSATEGRALWSTEFAGFEP
VPDSLQLDIVRQIRERKGLKPELPKPEDFLS
>gnl|CDD|236048 PRK07561, PRK07561, DNA topoisomerase I subunit omega; Validated
GKSLVIVESPAKAKTINKYLGSDYVVKASVGHIRDLPTSASSVPAKEKGALWARMGVDPDHDFEALYEVL
PGKEKVVSELKKAAKDADELYLATDPDREGEAIAWHLLEVLGGDDVPVKRVVFNEITKNAIQEAFENPRE
LDINLVNAQQARRFLDRLVGYMVSPLLWKKIARGLSAGRVQSVAVRLIVEREREIEAFVPEEYWDIHADL
TTPRGDAFEARLTHLDGKKFAPVDLLNEAQAEAAVAALEGARYSVASVEDKPTTRKPSAPFTTSTLQQEA
SRKLGFSVKKTMRIAQRLYEAGYITYMRTDSTNLSQEAINAARGYIGDNYGKKYLPEKPRQYSSKAKNAQ
EAHEAIRPSDVFRTPDQLKGLEGDAQRLYELIWKRFVASQMAPARYDSTTVTIAAGDAELRATGRVLRFD
GFLKVYVEGRDDALDDEDRRLPALKVGDALTLEKLDPTQHFTKPPARYSEASLVKELEKLGIGRPSTYAS
IISTIQDRGYVRLENRRFYPEKMGRIVTDRLEEFFPRLVDYDFTARMEEELDDIANGEADWKPVLDDFYK
DFSQQLEKAEELREEGGMRPNQMVITDRDCPTCGRGMGIRTGKTGVFLGCSGYALKERCKTTRNLTPEEE
TLNVLEGEDAETRALGADPECGTAMVLRSGRFGPYVQEGEGDKPRRLSLPKGNNPECVGLEIALGLLSLP
RPVGEHPECGSEIQAKIGRFGPYVKCGGTYASLKNTRKVLTIGLNRAVELLAEPKRPKEDPVPLPELGCP
KSGAPFVLRDGRYGPYVKHGKANATLPKGRETRAPTVEEALELLAEKPEKLRYLADAPAKDPAGKKAAVK
FSRKTKQQYVASEKDGKAT
>gnl|CDD|236049 PRK07562, PRK07562, vitamin B12-dependent ribonucleotide reductase
MKIERRFTKAGQSPYADIEFRKATSEIRNPDGSVVFRLENIEVPAQWSQVAADILAQKYFRKAGVPARLK
KVEENGVPSFLWRSVPDEEALAALPEEERFGSETSAKQVFDRLAGCWTYWGWKGGYFDSEEDARAFYDEL
RYMLATQMVAPNSPQWFNTGLHWAYGIDGPGQGHFYVDPKTGKLTKSKSAYEHPQPHACFIQSVEDDLVN
EGGIMDLWVREARLFKYGSGTGSNFSNLRGEGEKLSGGGKSSGLMSFLKIGDRAAGAIKSGGTTRRAAKM
VIVDIDHPDIEEFIDWKVKEEQKVAALVTGSKIVSKHLKAIMKACVNCEGDGDDCFDPAKNPALKREIKA
AKKALVPENYIKRVIQFARQGYTDIDFPTYDTDWDSEAYLTVSGQNSNNSVRVTDEFLRAVENDGDWNLT
ARTDGKVAKTLKARDLWEKIGYAAWASADPGLQFNTTINDWHTCPASGPIRASNPCSEYMFLDDTACNLA
SLNLLTFRDEDTKRFDVEAYEHACRLWTVVLEISVLMAQFPSKEIAELSYEFRTLGLGYANIGGLLMTMG
IPYDSDEGRAICGALSAIMTGVAYATSAEMAKELGPFPGYEKNADHMLRVIRNHRRAAHGESEGYEGLSV
NPVPLDHANCPDQDLVAHAKAAWDKALELGEKHGYRNAQVTVIAPTGTIGLVMDCDTTGIEPDFALVKFK
KLAGGGYFKIINRAVPEALRTLGYSESQIAEIEAYAVGHGTLNQAPGINHSTLKAKGFTDEKIEKVEAAL
KSAFDIKFAFNKWTLGEDFCKDTLGIPAEQLNDPSFDLLEHLGFSKKDIEAANDHVCGAMTLEGAPFLKA
EHLPVFDCANPCGKIGKRYLSVESHIRMMAAAQPFISGAISKTINMPNEATVEDCKNAYMLSWKLALKAN
ALYRDGSKLSQPLNSSLIEDDDDDDALEALIEAPAAARAVQVAEKIVERVVERIIREREKLPDRRKGYTQ
KAVVGGHKVYLRTGEYDDGRLGEIFIDMHKEGAAFRSLMNNFAIAVSLGLQYGVPLEEYVDAFTFTRFEP
AGMVQGNDAIKNATSILDYVFRELAVSYLGRNDLAHVDPSDFGFDALGKGIQEGKAPVGEVATNVVSTGL
TRGRKPTLVVVTGGGAAAGAAVAAAPAASAATFSDKAAAAAAAAAAAAAAEAKKVEAERRAEAKMQGYTG
EACSECGNFTLVRNGTCLKCDTCGSTTGCS
>gnl|CDD|236050 PRK07564, PRK07564, phosphoglucomutase; Validated
IHPRAGQPAQPSDLINVPRLVSAYYTLKPDPTNPFQDVKFGTSGHRGSSLQPSFNENHILAIFQAICEYR
GKQGITGPLFVGGDTHALSEPAIQSALEVLAANGVGVVIVGRGGYTPTPAVSHAILKYNGRGGGLADGIV
ITPSHNPPEDGGIKYNPPNGGPADTDVTDAIEARANELLAYGLKGVKRIPLDRALASMTVEVIDPVADYV
EDLENVFDFDAIRKAGLRLGVDPLGGATGPYWKAIAERYGLDLTVVNAPVDPTFNFMPLDDDGKIRMDCS
SPYAMAGLLALKDAFDLAFANDPDGDRHGIVTPGGLMNPNHYLAVAIAYLFHHRPGWRAGAGVGKTLVSS
AMIDRVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESAGASFLRRDGSVWTTDKDGLIAVLLAAEIL
AVTGKSPSEIYRELWARFGRPYYSRHDAPATPEQKAALRKLSPELVGATELAGDPIDASLTEAPGNGAAI
GGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIQKEAQEIVADLIAA
>gnl|CDD|236051 PRK07565, PRK07565, dihydroorotate dehydrogenase-like protein
MDLSTTYLGLTLRNPLVASASPLSESVDNVKRLEDAGAGAVVLKSLFEEQIRHEAAELDRHLTHGTESFA
EALDYFPEPAKFYVGPEEYLELIRRAKEAVDIPVIASLNGSSAGGWVDYARQIEQAGADALELNIYYLPT
DPDISGAEVEQRYLDILRAVKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNRFYQPDIDLETL
EVVPGLVLSTPAELRLPLRWIAILSGRVGADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIG
TILRGLEDWMERHGYESLQQFRGSMSQKNVPDPAAFERAQYMKALSSYSPEAGP
>gnl|CDD|236052 PRK07566, PRK07566, chlorophyll synthase ChlG
ISEALENTSKPRQLLGPKGASPTTSIWKARLQLMKPITWFPPMWAFLCGAVSSGAFGWTLENVLKLLAGM
LLAGPLLCGTSQTLNDYFDREVDAINEPYRPIPSGAISLRWVLYLIAVLTVLGLAVAYLLGPWVFLAALL
GLFLAWIYSAPPLRLKQNGWLGNYAVGLSYEGLPWWAGAAAFGAGLPSWPIVILALLYSLGAHGIMTLND
FKSVEGDRQLGLRSLPVVFGEKNAARIACVVIDLFQLAVIALLLAWGQPLYAAIVGLLLIPQITLQDRLL
RDPLERDVWYNASAQPFYVLGMLVTALAIRHLGL
>gnl|CDD|181035 PRK07567, PRK07567, glutamine amidotransferase; Provisional
MKPFLLLSPRPEDEAADAEYAAFLRYTGLDPAELRRIRLDREPLPDLDLDDYSGVIVGGSPFNVSDPAES
KSPWQRRVEAELSGLLDEVVARDFPFLGACYGVGTLGHHQGGVVDRTYGEPVGAVTVSLTDAGRADPLLA
GLPDTFTAFVGHKEAVSALPPGAVLLATSPTCPVQMFRVGENVYATQFHPELDADGLKTRIDFYRDHGYF
APEEADSLIARARSVDVTAPNRILRNFVERYR
>gnl|CDD|181036 PRK07568, PRK07568, pyridoxal phosphate-dependent aminotransferase
MKISKRVLNMPASPIRKLVPYADEAKKRGIKVYHLNIGQPDIKTPEVFFEAIKNYDEEVLAYSHSQGIPE
LREAFAKYYKKWGIDVEPDEILITNGGSEAILFAMMAICDPGDEILVPEPFYANYNGFATSAGVKIVPVT
TKIEEGFHLPSKEEIEKLITPKTKAILISNPGNPTGVVYTKEELEMLAEIAKKHDLFLISDEVYREFVYD
GLKYTSALSLEGLEDRVIIIDSVSKRYSACGARIGCLISKNKELIAAAMKLCQARLSPPTLEQIGAAALL
DTPESYFDEVREEYKKRRDILYEELNKIPGVVCEKPKGAFYIIAKLPVDDAEDFAKWLLTDFNYNGETVM
VAPASGFYATPGLGKNEIRIAYVLNEEDLKRAMEILKEALEKYNKRK
>gnl|CDD|181037 PRK07569, PRK07569, bidirectional hydrogenase complex protein HoxU; Validated
MSVKTLTIDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEIEGSNKLLPACVTPVAE
GMVVQTNTPRLQEYRRMIVELLFAEGNHVCAVCVANGNCELQDLAIEVGMDHVRFPYLFPRRPVDISHPR
FGIDHNRCVLCTRCVRVCDEIEGAHTWDVAGRGAKSRVITDLNQPWGTSETCTSCGKCVQACPTGAIFRK
GSTVGEMEKDRDKLEFLVTAREKR
>gnl|CDD|181038 PRK07570, PRK07570, succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
MKLTLKIWRQKGPDDKGKFETYEVDDISPDMSFLEMLDVLNEQLIEKGEEPVAFDHDCREGICGMCGLVI
NGRPHGPDRGTTTCQLHMRSFKDGDTITIEPWRAAAFPVIKDLVVDRSALDRIIQAGGYVSVNTGGAPDA
NAIPVPKEDADRAFDAAACIGCGACVAACPNGSAMLFTGAKVSHLALLPQGQPERARRVRAMVAQMDEEG
FGNCTNTGECEAVCPKGISLENIARMNREYLRASFRGRDD
>gnl|CDD|236053 PRK07571, PRK07571, bidirectional hydrogenase complex protein HoxE; Reviewed
TTTDNPTTPPSATHPSGDKRFKVLEATMKRNQYRQDALIEVLHKAQELFGYLERDLLLYVARQLKLPLSR
VYGVATFYHLFSLKPSGEHTCVVCTGTACYVKGSAAILEDLENELGIKAGETTADGKLSLLTARCLGACG
IAPAVVFDGKVAGKQTPESVLEKVQGWLQ
>gnl|CDD|181039 PRK07572, PRK07572, cytosine deaminase; Validated
MFDLIVRNANLPDGRTGIDIGIAGGRIAAVEPGLQAEAAEEIDAAGRLVSPPFVDPHFHMDATLSYGLPR
VNASGTLLEGIALWGELKPLLTQEALVERALRYCDWAVARGLLAIRSHVDVCDPRLLAVEALLEVRERVA
PYLDLQLVAFPQDGVLRSPGAVDNLERALDMGVDVVGGIPHFERTMADGAESVRLLCEIAAERGLRVDMH
CDESDDPLSRHIETLAAETQRLGLQGRVAGSHLTSMHSMDNYYVSKLIPLMAEAGVNAIANPLINITLQG
RHDTYPKRRGMTRVPELMAAGINVAFGHDCVMDPWYSLGSGDMLEVAHMGLHVAQMTGQDAMRACFDAVT
VNPARIMGLEGYGLEPGCNADLVLLQARDPIEAIRLRAARLAVIRRGKVIARTPPRVARLSLPGRPATVD
FRLDRP
>gnl|CDD|236054 PRK07573, sdhA, fumarate reductase/succinate dehydrogenase flavoprotein subunit
GMMILDAKIPEGPIEEKWDRYKFHLKLVNPANKRKFDVIVVGTGLAGASAAATLGELGYNVKVFCYQDSP
RRAHSIAAQGGINAAKNYQNDGDSVYRLFYDTVKGGDFRAREANVYRLAEVSVNIIDQCVAQGVPFAREY
GGLLANRSFGGAQVSRTFYARGQTGQQLLLGAYQALSRQIAAGTVKMYTRTEMLDLVVVDGRARGIVARN
LVTGEIERHTADAVVLATGGYGNVFYLSTNAMGSNATAIWRAHKKGAYFANPCFTQIHPTCIPVSGDYQS
KLTLMSESLRNDGRIWVPKKKGDKRKPNDIPEEERDYYLERRYPAFGNLVPRDVASRAAKERCDAGRGVG
PTGLGVYLDFADAIKRLGKDVIRERYGNLFDMYERITGENPYETPMRIYPAVHYTMGGLWVDYNLMSTIP
GLFVIGEANFSDHGANRLGASALMQGLADGYFVLPYTIGNYLADTIGTPKVSTDHPEFKEAEAEVQDRID
RLLNIKGKRTVDSFHRELGKIMWDYCGMARNEEGLKKALEKIRALREEFWKNVRVPGSADELNQELEKAG
RVADFLELGELMCRDALHREESCGGHFREEHQTEDGEALRDDENFAYVAAWEYKGDGKEPVLHKEPLEFE
NVKLAQRSYK
>gnl|CDD|181041 PRK07574, PRK07574, NAD-dependent formate dehydrogenase
MAKKLCVLYPDPVDGYPPSYARDSIPVITSYPDGQTLPTPKAIDFTPGELLGSVSGELGLRKFLEERGHE
LVVTSDKDGPDSDFEKELPDADVVISQPFWPAYLTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITV
AEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGGWNIADCVSRSYDLEGMTVGIVGAGRIGLAVLRR
LKPFDVKLHYTDRHRLPEEVEQELGLTYHVSFDSLVSVCDVVTIHCPLHPETEHLFDADVLSRMKRGSYL
VNTARGKIVDRDAVVRALESGHLAGYAGDVWFPQPAPADHPWRTMPRNGMTPHISGTTLSAQARYAAGTR
EILECFFEGRPIRDEYLIVDGGRLAGTGAHSYTAG
>gnl|CDD|236055 PRK07575, PRK07575, dihydroorotase; Provisional
MMMSLLIRNARILLPSGELLLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGL
EHKEDLFTASRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPELLTAN
PTCGIKIFMGSSHGPLLVDEEAALERIFAEGTRLIAVHAEDQARIRARRAEFAGISDPADHSQIQDEEAA
LLATRLALKLSKKYQRRLHILHLSTAIEAELLRQDKPSWVTAEVTPQHLLLNTDAYERIGTLAQMNPPLR
SPEDNEALWQALRDGVIDFIATDHAPHTLEEKAQPYPNSPSGMPGVETSLPLMLTAAMRGKCTVAQVVRW
MSTAVARAYGIPNKGRIAPGYDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVF
DRGQVNTEVRGQALTFDE
>gnl|CDD|236056 PRK07576, PRK07576, short chain dehydrogenase; Provisional
MTTMFDFAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDY
AAVEAAFAQIADEFGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASII
QISAPQAFVPMPMQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIAGTEGMARLAPSPELQAAVA
QSVPLKRNGTKQDIANAALFLASDMASYITGVVLPVDGGWSLGGASIAMAELGQ
>gnl|CDD|181044 PRK07577, PRK07577, SDR family oxidoreductase
MSSRTVLVTGATKGIGLALSLRLANLGHQVIGIARSAIDDFPGELFACDLADIEQTAATLAQINEIHPVD
AIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRAIFGALDRTSYS
AAKSALVGCTRTWALELAEYGITVNAVAPGPIETELFRQTRPVGSEEEKRVLASIPMRRLGTPEEVAAAI
AFLLSDDAGFITGQVLGVDGGGSL
>gnl|CDD|236057 PRK07578, PRK07578, short chain dehydrogenase; Provisional
MKILVIGASGTIGRAVVAELSKRHEVITAGRSSGDVQVDITDPASIRALFEKVGKVDAVVSAAGKVHFAP
LAEMTDEDFNVGLQSKLMGQVNLVLIGQHYLNDGGSFTLTSGILSDEPIPGGASAATVNGALEGFVKAAA
LELPRGIRINVVSPTVLTESLEKYGPFFPGFEPVPAARVALAYVRSVEGAQTGEVYKVG
>gnl|CDD|236058 PRK07579, PRK07579, dTDP-4-amino-4,6-dideoxyglucose formyltransferase
MKTILVLTDNVHAHALAVDLIARKNDMDVDYFCSFKSQTSFAKEIYQSPIKQLDVAERVAEIVERYDLVL
SFHCKQRFPAKLVNGVRCINIHPGFNPYNRGWFPQVFSIINGLKIGATIHEMDEQLDHGPIIAQREVEIE
SWDSSGSVYARVMDIERELVLEHFDAIRDGSYTAKKPATEGNLNSKKDFKQLREIDLDERGTFRHFINRL
RALTHDDYKNAYFVDESGRKVFVRLVLEPEKPAEA
>gnl|CDD|236059 PRK07580, PRK07580, Mg-protoporphyrin IX methyl transferase; Validated
MMMFNYLEHKSEVRTYFNRTGFDRWARIYSDAPVSKVRATVRAGHQRMRDTVLSWLPADGDLTGLRILDA
GCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGDLESLLGRFDTVVCLDVLIHY
PQEDAARMLAHLASLTRGSLIFTFAPYTPLLALLHWIGGLFPGPSRTTRIYPHREKGIRRALAAAGFKVV
RTERISSGFYFSRLLEAVRR
>gnl|CDD|236060 PRK07581, PRK07581, hypothetical protein; Validated
QEFMGDYETFDLGDVELQSGATLPDARLAYKTYGTLNAAKDNAILYPTWYSGTHQDNEWLIGPGRALDPE
KYFIIIPNMFGNGLSSSPSNTPAPFNAARFPHVTIYDNVRAQHRLLTEKFGIERLALVVGWSMGAQQTYH
WAVRYPDMVERAAPIAGTAKTTPHNFVFLEGLKAALTADPAFNGGWYAEPPERGLRAHARVYAGWGFSQA
FYRQELWRAMGYASLEDFLVGFWEGNFLPRDPNNLLAMLWTWQRGDISRNPAYGGDLAAALGSITAKTFV
MPISTDLYFPPEDCEAEAALIPNAELRPIESIWGHLAGFGQNPADIAFIDAALKELLAS
>gnl|CDD|236061 PRK07582, PRK07582, cystathionine gamma-lyase; Validated
AYGDGTRSVHAGGPEAVPGEPVLPGPVFAAPYHLSPGEPTGPDTYGRASNPTWRALEAALGELEGAEALV
FPSGMAAITAVLRALLRPGDTVVVPADGYYQVRALAREYLAPLGVTVREAPTAGMAEAALAGADLVLAET
PSNPGLDVCDLAALAAAAHAAGALLVVDNTTATPLGQRPLELGADLVVASDTKALTGHSDLLLGYVAGRD
PELMAAVERWRLLAGAIPGPFEAWLAHRSLGTLGLRFARQCANALAVAELLAGHPAVRGVRYPGLPGDPA
HEVAARQMRRFGGLVSFELADAAAAERFVAASRLVVAATSFGGVHTSADRRARWGDAVPEGFVRLSCGIE
DTDDLVADLERALDAL
>gnl|CDD|236062 PRK07583, PRK07583, cytosine deaminase
MSSFFSLPESGRYWLKNARVPAALLEGGVPPGDTLEGLVLVDIEIADGKIAAILPAGGAPDELPAVDLKG
RMVWPCFVDMHTHLDKGHIWPRSPNPDGTFPGALDAVTADREAHWSAEDLYRRMEFGLRCAYAHGTSAIR
THLDSFAPQAAISWEVFAELREAWAGRIALQAVSLVPLDAYLTDAGERLADLVAEAGGLLGGVTYMNPDL
DAQLDRLFRLARERGLDLDLHVDETGDPASRTLKAVAEAALRNGFEGKVTCGHCCSLAVQPEEQAQATIA
LVAEAGIAIVSLPMCNLYLQDRQPGRTPRWRGVTLVHELKAAGIPVAVASDNCRDPFYAYGDHDMLEVFR
EAVRILHLDHPYDDWPAAVTTTPADIMGLPDLGRIAVGAPADLVLFKARSFSELLSRPQSDRIVLRAGKP
IDTTLPDYRELDDLMGAP
>gnl|CDD|236063 PRK07586, PRK07586, acetolactate synthase large subunit
MNGAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLFEGVATGAADGYARMAGKPAATLL
HLGPGLANGLANLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAA
AAVAAARGAPGQVATLILPADVAWSEGGPPAPPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALR
ERGLAAAARIAAATGARLLAETFPARMERGAGRPAVERLPYFAEQALAQLAGVRHLVLVGAKAPVAFFAY
PGKPSRLVPEGCEVHTLAGPGEDAAAALEALADALGAKPAAPPLAAPARPPLPTGALTPEAIAQVIAALL
PENAIVVDESITSGRGFFPATAGAAPHDWLTLTGGAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQ
ALWTQARENLDVTTVIFANRAYAILRGELARVGAGNPGPRALDMLDLDDPDLDWVALAEGMGVPARRVTT
AEEFADALAAALAEPGPHLIEAVV
>gnl|CDD|169028 PRK07588, PRK07588, FAD-binding domain
MKVAISGAGIAGPTLAYWLRRYGHEPTLIERAPELRTGGYMVDFWGVGYEVAKRMGITDQLREAGYQIEH
VRSVDPTGRRKADLNVDSFRRMVGDDFTSLPRGDLAAAIYTAIDGQVETIFDDSIATIDEHRDGVRVTFE
RGTPRDFDLVIGADGLHSHVRRLVFGPERDFEHYLGCKVAACVVDGYRPRDERTYVLYNEVGRQVARVAL
RGDRTLFLFIFRAEHDNPPLTPAEEKQLLRDQFGDVGWETPDILAALDDVEDLYFDVVSQIRMDRWSRGR
VALVGDAAACPSLLGGEGSGLAITEAYVLAGELARAGGDHRRAFDAYEKRLRPFIAGKQAAAAKFLSVFA
PKTRFGLYVRNIAMKIMNLPPVADFVGAGSFRDDFELPEYE
>gnl|CDD|236064 PRK07589, PRK07589, ornithine cyclodeaminase; Validated
MVRFVSVDDMARLVRRVGVETFLRELADYLEADFRRWQEFDKSPRVASHSPDGVIELMPTSDGELYSFKY
VNGHPKNTRRGLQTVMAFGVLADVDTGYPLLLSEMTLLTALRTAATSALAAKYLARPDSRTMALIGNGAQ
SEFQALAFKALLGIEEIRLYDIDPAATAKLARNLAGPGLRIVACRSVAEAVEGADIITTVTADKTNATIL
TDDMVEPGMHINAVGGDCPGKTELHPDILRRARVFVEYEPQTRIEGEIQQLPADFPVTELWRVLTGEAPG
RESADQITLFDSVGFALEDFSALRYVRDLAEDTGLGEQLDLVPDPDDPKDLFGLLRRAAAAAAAAA
>gnl|CDD|136438 PRK07594, PRK07594, EscN/YscN/HrcN family type III secretion system ATPase
MKNELMQRLRLKYPPPDGYCRWGRIQDVSATLLNAWLPGVFMGELCCIKPGEELAEVVGINGSKALLSPF
TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPDVCWKDYDAMPPPAMVRQPITQPLM
TGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNVLVLIGERGREVREFIDFTLSEETRK
RCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPG
VFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATL
SRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQRGVDTDTDKAIDTYPDICTFLRQSKDEVCGP
ELLIEKLHQILTE
>gnl|CDD|236066 PRK07597, secE, preprotein translocase subunit SecE; Reviewed
LPKMSKMKKLKKFFKDVKAELKKVTWPTRKELVRSTIVVLVFVAFFALFFYLVDLLFSKLISLL
>gnl|CDD|236067 PRK07598, PRK07598, RNA polymerase sigma factor SigC; Validated
MPATSFYADAAYEPQKSRQALDPDILEDDPDDSLDDVQELEIAAADEAVETAARNRRSTDLVRLYLQEIG
RVRLLGRDEEVSEAQKVQRYMKLIVLANAAKEGDEVIKPYLRLIEVRERLTSELGHRPSLERWAKTADIS
LADLKPTLAEGKRRWAEIAKLTVEELEQIQKQGLRAKEHMIKANLRLVVSVAKKYQNRGLELLDLVQEGT
LGLERAVEKFDPTKGYRFSTYAYWWIRQGITRAIATQSRTIRLPVHITEKLNKIKKAQRKISQEKGRTPT
IEDIAQELEMTPTQVREVLLRVPRSVSLETKVGKDKDTELGDLLETDDISPEEMLMRESLQRDLQHLLAD
LTSRERDVIRMRFGLADGHTYSLAEIGRALDLSRERVRQIESKALQKLRQPKRRNRIRDYLELLS
>gnl|CDD|181057 PRK07608, PRK07608, UbiH/UbiF family hydroxylase
AYHMKFDVVVVGGGLVGASLALALAQSGLRVALLAPRAPPRPADDAWDSRVYAISPSSQAFLERLGVWQA
LDAARLAPVYDMRVFGDAHARLHFSAYQAGVPQLAWIVESSLIERALWAALRFQPNLTWFPARAQGLEVD
PDAATLTLADGQVLRADLVVGADGAHSWVRSQAGIKAERRPYRQTGVVANFKAERPHRGTAYQWFRDDGI
LALLPLPDGHVSMVWSARTAHADELLALSPEALAARVERASGGRLGRLECVTPAAGFPLRLQRVDRLVAP
RVALVGDAAHLIHPLAGQGMNLGLRDVAALADVLAGREPFRDLGDLRLLRRYERARREDILALQVATDGL
QRLFALPGPLARWLRNAGMALVGALPLVKRWLVRHALG
>gnl|CDD|181058 PRK07609, PRK07609, CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
MSFQVTLQPSGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGPHQASALSGEERA
AGEALTCCAKPLSDLVLEAREVPALGDIPVKKLPCRVASLERVAGDVMRLKLRLPATERLQYLAGQYIEF
ILKDGKRRSYSIANAPHSGGPLELHIRHMPGGVFTDHVFGALKERDILRIEGPLGTFFLREDSDKPIVLL
ASGTGFAPIKSIVEHLRAKGIQRPVTLYWGARRPEDLYLSALAEQWAEELPNFRYVPVVSDALDDDAWTG
RTGFVHQAVLEDFPDLSGHQVYACGSPVMVYAARDDFVAAGLPAEEFFADAFTYAADLA
>gnl|CDD|181059 PRK07627, PRK07627, dihydroorotase; Provisional
MKIHIKGGRLIDPAAGTDRQADLYVAAGKIAAIGQAPAGFNADKTIDASGLIVCPGLVDLSARLREPGYE
YKATLESEMAAAVAGGVTSLVCPPDTDPVLDEPGLVEMLKFRARNLNQAHVYPLGALTVGLKGEVLTEMV
ELTEAGCVGFSQANVPVVDTQVLLRALQYASTFGFTVWLRPLDAFLGRGGVAASGAVASRLGLSGVPVAA
ETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDP
PLRSQRDREAIRAALADGTIDAICSDHTPVDDDEKLLPFAEATPGATGLELLLPLTLKWADEAKVPLARA
LARITSAPARVLGLPAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQV
AFERR
>gnl|CDD|236068 PRK07630, PRK07630, CobD/CbiB family protein; Provisional
MTFFSVLLALIIEQLRPLSPRNPVYALFRAHAESLEHGFNAGKARHGVLAWLLVVLPWVLAVALVYYLLY
KVSPVLAFLWNVAVLYLTLGFRQFSHYFTDIHLALRNDDLPRARELLGEWTGLDTVDMPVSEIVRHTIEH
ALVASHRHVFGVFFWFVLPPGPAGAVLYRLAEYLARSWGVPSDDRTAAFGLFAQRAFFVIDWVPARLTAL
GFAIVGNFEDAIYAWRNQARQWPDENDGILLAAGAGALGVRLGGPLAEPSSVDALAVGDRPPLGVGDEAD
PRTLQSAVGLVWRALVLWMLLLLLLSIAVWVG
>gnl|CDD|236070 PRK07636, ligB, ATP-dependent DNA ligase; Reviewed
MFISPMLLESAKEPFNSENYITEPKFDGIRLIASKNNGLIRLYTRHNNEVTAKFPELLNLDIPDGTVLDG
ELIVLGSTGAPDFEAVMERFQSKKSTKIHPVVFCVFDVLYINGVSLTALPLSERKEILASLLLPHPNVKI
IEGIEGHGTAYFELVEERELEGIVIKKANSPYEINKRSDNWLKVINYQYTDVLITGYRKEEFGLLLSYLD
GRSAGIMEFMPYDARKKFYKRAKRLVVGEDKKFVYIEPIIGCRVKHRFKTKNGMLRIPSFVEWRI
>gnl|CDD|236071 PRK07638, PRK07638, acyl-CoA synthetase; Validated
MGITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIAILLENRIEFLQLFAGA
AMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRVIEIDEWKRMIEKYLPTYAPIEN
VQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQ
TVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYA
KLYEFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIG
GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDS
YWGEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEKIYE
>gnl|CDD|181065 PRK07639, PRK07639, petrobactin biosynthesis protein AsbD
MRREALKNAVLKIMEEKLELKNVTHLEETMRLNEDLYIDSVMMLQLIVYIEMDVKLCVPEDEVDPKAFLT
VGSLLDFMEELQPLQD
>gnl|CDD|181066 PRK07649, PRK07649, aminodeoxychorismate/anthranilate synthase component II
MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFA
GKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDC
LEVTSWTEEGEIMAIRHKTLPIEGVQFHPESIMTSHGKELLQNFIRKYSPSVTSC
>gnl|CDD|181067 PRK07650, PRK07650, 4-amino-4-deoxychorismate lyase; Provisional
LIYVNGQYVEEEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDEVLL
ILKNLLEKNGLENAYVRFNVSAGIGEIGLQTEMYEEPTVIVYMKPLAPPGLPAEKEGVVLKQRRNTPEGA
FRLKSHHYLNNILGKREIGNDPNKEGIFLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVI
KVLEELGIEVKEGFYTKEELLSADEVFVTNSIQEIVPLTRIEERDFPGKVGMVTKRLQNLYEMQREKLWS
RNE
>gnl|CDD|236072 PRK07656, PRK07656, long-chain-fatty-acid--CoA ligase; Validated
DNEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVI
AALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPH
TEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRY
LAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDL
SSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASGVTTFNRLDDDRKTVAGTIGTAIAGVENKI
VNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIV
GGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRS
IEFLDELPKNATGKVLKRALREK
>gnl|CDD|181069 PRK07657, PRK07657, enoyl-CoA hydratase; Provisional
MLQNISVDYVTPHVVKITLNRPRAANALSLALLEELQNILTQINEEANVRVVILTGAGEKAFCAGADLKE
RAGMNEEQVRHAVSLIRTTMEMVEQLPQPVIAAINGIALGGGLELALACDFRIAAESASLGLTETTLAII
PGAGGTQRLPRLIGVGRAKELIYTGRRISAQEAKEIGLVEFVVPAHLLEEKAIEIAEKIASNGPIAVRQA
KEAISNGIQVDLHTGLQIEKQAYEGTIPTKDRLEGLQAFKEKRKPMYKGE
>gnl|CDD|181070 PRK07658, PRK07658, enoyl-CoA hydratase; Provisional
MKFLSVRVEDHVAVITLNHPPANALSSQVLHELSELLDQVEKDDNVRVVVIHGEGRFFSAGADIKEFTSV
TEAEQATELAQLGQVTFERVEKFSKPVIAAIHGAALGGGLELAMSCHIRFATESAKLGLPELNLGLIPGF
AGTQRLPRYVGKAKALEMMLTSEPITGAEALKWGLVNGVFPEETLLDDAKKLAKKIAGKSPATTRAVLEL
LQTTKSSSYYEGVKREAKIFGEVFTSEDAKEGVQAFLEKRKPSFSGK
>gnl|CDD|236073 PRK07659, PRK07659, enoyl-CoA hydratase; Provisional
VTSKMESVVVKYEGRVATIMLNRPEALNALDEPMLKELLQALKEVAESSAHIVVLRGNGRGFSAGGDIKM
MLSSNDESKFDGVMNTISEIVVTLYTMPKLTISAIHGPAAGLGLSIALTADYVIADISAKLAMNFIGIGL
IPDGGGHFFLQKRVGENKAKQIIWEGKKLSATEALDLGLIDEVIGGDFQTAAKQKISEWLQKPLKAMIET
KQIYCELNRSQLEQVLQLEKRAQYAMRQTADHKEGIRAFLEKRLPVFKGE
>gnl|CDD|181072 PRK07661, PRK07661, acetyl-CoA C-acetyltransferase
MREAVIVAGARTPVGKAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARN
IGALAGLPYTVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHVVRPNPRLVEAA
PEYYMGMGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTVGENNKLQEETI
TFSQDEGVRADTTLEILGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVA
GVPPEVMGIGPIAAIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLG
CTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFELL
>gnl|CDD|236074 PRK07666, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
MAQSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEE
VTAAIEQLKNELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIIN
ISSTAGQKGAAVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGLTDGNPDKVMQP
EDLAEFIVAQLKLNKRTFIKSAGLWSTNP
>gnl|CDD|169051 PRK07667, PRK07667, uridine kinase; Provisional
MSTNELINIMKKHKENRFILGIDGLSRSGKTTFVANLKENMKQEGIPFHIFHIDDYIVERNKRYHTGFEE
WYEYYYLQWDIEWLRQKFFRKLQNETKLTLPFYHDETDTCEMKKVQIPIVGVIVIEGVFLQRKEWRDFFH
YMVYLDCPRETRFLRESEETQKNLSKFKNRYWKAEDYYLETESPKDRADLVIK
>gnl|CDD|181074 PRK07668, PRK07668, hypothetical protein; Validated
MLSKEGRKFLDDTRVYLIAKGIKEEDIESFLEDAELHLIEGEKDGKTVEDIFGDSPKEYANELVKEMEVD
RKENIKLILFIIIGILSFWIIANILFGNPNHPLTYSLIQLIGYPISLILTIIGLIFLLRMASFKSKLTEK
WFLIIYLVILIPMLLIVAIMFLNKWYGTPMLQFTQMQSYILAGLIFLITVIINIYFLGWFGLLYLIIPLS
IMFLFKYFNSEDVVPMIFQIIILYGSLYVLMFIEIKREKNKREE
>gnl|CDD|181075 PRK07670, PRK07670, FliA/WhiG family RNA polymerase sigma factor
MQSLTYEEQKLWDRWKEERDPDAADELIRRYMPLVHYHVQRISVGLPKSVSKDDLKSLGMLGLYDALEKF
DPSRDLKFDTYASFRIRGAIIDGLRKEDWLPRSMREKTKKVEAAIEKLEQRYMRNVTPKEVAAELGMTEE
EVEATMNEGFFANLLSIDEKTHDQDDGENVSVTIRDDKTPTPEEKLLKEELIEELAEKIKQLSEKEQLVI
SLFYKEELTLTEIGQVLNLSTSRISQIHSKALFKLKKLLEK
>gnl|CDD|181076 PRK07671, PRK07671, bifunctional cystathionine gamma-lyase/homocysteine desulfhydrase
MRAKTKLIHGGIIGDPSTGAVSVPIYQVSTYKQEAVGKHQGYEYSRTGNPTRAALEELIAVLEGGHAGFA
FGSGMAAITAVMMLFSSGDHVILTDDVYGGTYRVMTKVLNRFGIEHTFVDTSNLEEVEEAIRPNTKAIYV
ETPTNPLLKITDIKKISTIAKEKGLLTIVDNTFMTPYWQSPISLGADIVLHSATKYLGGHSDVVAGLVVV
NSPELAEDLHFVQNSTGGILGPQDSWLLLRGLKTLGIRMEEHETNSRAIAEFLNNHPAVNKVYYPGLPSH
PNHELAKEQANGFGGMISFDVGSEETANKVLERLQYFTLAESLGAVESLISIPSQMTHASIPADRRKELG
ITDGLIRISVGIEDGEDLIEDLAQALA
>gnl|CDD|181077 PRK07677, PRK07677, short chain dehydrogenase; Provisional
EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVE
QIDEKFGRIDALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGIKGNIINMVATY
AWDAGPGVIHSAAAKAGVLAMTRTLAVEWGRKYGIRVNAIAPGPIERTGGADKLWESEEAAKRTIQSVPL
GRLGTPEEIAGLAYFLLSDEAAYINGTCITMDGGQWLNQYPF
>gnl|CDD|181078 PRK07678, PRK07678, aminotransferase; Validated
MMKTKQTDELLAKDEQYVWHGMKPYNPNATMVVAKAEGAWVTDIQGNRYLDGMSGLWCVNVGYGRKELAE
AAYEQLKTLSYFPLTQSHEPAIKLAEKLNEWLGGEYVIFFSNSGSEANETAFKIARQYHAQKGEPHRYKF
ISRYRAYHGNSMGALAATGQAQRKYKYEPLAPGFLHVPPPDCYRMPGIESEDIYDLECVKEIDRVMTWEL
SETIAAVIMEPIITGGGVLMPPQDYMKAVKEICQKHGALLISDEVICGFGRTGKAFGFMNYGVKPDIITM
AKGITSAYLPLSATAVKKEIYEAFKGKGEYEHFRHVNTFGGNPAACALALKNLEIMENENLIERSAQLGE
LLLEQLKEELGEHPLVGDIRGKGLLVGIELVNDKETKEPADNDKVASVVAACKEKGLIIGKNGDTVAGYN
NVLTLSPPLVISSEEIAFIVGTLKTALERIK
>gnl|CDD|181079 PRK07679, PRK07679, pyrroline-5-carboxylate reductase; Reviewed
MSIQNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRLQELHQKYGVKGTHNKKELLTDANILF
LAMKPKDVAEALIPFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVPIIRAMPNTSAAILKSATAISPSKH
ATAEHIQTAKALFETIGLVSVVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTM
IGAAEMLKASEKHPSILRKEITSPGGTTEAGIEVLQEHRFQQALISCITQATQRSHNLGKTLEQLTKEK
>gnl|CDD|181080 PRK07680, PRK07680, late competence protein ComER; Validated
MNIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERYPGIHVAKTIEEVISQSDLIFICV
KPLDIYPLLQKLAPHLTDEHCLVSITSPISVEQLETLVPCQVARIIPSITNRALSGASLFTFGSRCSEED
QQKLERLFSNISTPLVIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEETNISKEEATTLASEMLIGMG
KLLEKGLYTLPTLQEKVCVKGGITGEGIKVLEEEVGDMFHRLFQRTHEKFDEDLEKVDQQFNK
>gnl|CDD|181081 PRK07681, PRK07681, LL-diaminopimelate aminotransferase
MTYTLATRMKAFQSSIFSELGAYKKEKIAAGHKMIDLSIGNPDMPPADFVREEMVHTANQKESYGYTLSG
IQEFHEAVTEYYNNTHNVILNADKEVLLLMGSQDGLVHLPMVYANPGDIILVPDPGYTAYETGIQMAGAT
SYYMPLKKENDFLPDLELIPEEIADKAKMMILNFPGNPVPAMAHEDFFKEVIAFAKKHNIIVVHDFAYAE
FYFDGNKPISFLSVPGAKEVGVEINSLSKSYSLAGSRIGYMIGNEEIVRALTQFKSNTDYGVFLPIQKAA
CAALRNGAAFCEKNRGIYQERRDTLVDGFRTFGWNVDKPAGSMFVWAEIPKGWTSLSFAYALMDRANVVV
TPGHAFGPHGEGFVRIALVQDEEVLQQAVENIRNSGIFALEKVDELVKN
>gnl|CDD|181082 PRK07682, PRK07682, aminotransferase
VESLQPSGIRKFFDLAANMEGVISLGVGEPDFVTPWNVREASIRSLEQGYTSYTANAGLLELRQEIAKYL
KKRFAVSYDPNDEIIVTVGASQALDVAMRAIINPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENEF
KVQPAQIEAAITAKTKAILLCSPNNPTGAVLNKSELEEIAVIVEKHDLIVLSDEIYAELTYDEAYTSFAS
IKGMRERTILISGFSKGFAMTGWRLGFIAAPVYFSEAMLKIHQYSMMCAPTMAQFAALEALRAGNDDVIR
MRDSYRKRRNFFVTSFNEIGLTCHVPGGAFYAFPSISSTGLSSEEFAEQLLLEEKVAVVPGSVFGESGEG
FIRCSYATSLEQLQEAMKRMKRFVENKK
>gnl|CDD|236075 PRK07683, PRK07683, aminotransferase A; Validated
MEHLINPRVKDIQISGIRQFSNMVQNYDNLISLTIGQPDFPTPSHVKEAAKRAITENYTSYTHNAGLLEL
RKAACNFVKDKYDLHYSPESEIIVTIGASEAIDIAFRTILEPGTEVILPAPIYPGYEPIIRLCGAKPVFI
DTRSTGFRLTAEALENAITEKTRCVVLPYPSNPTGVTLSKEELQDIADVLKDKNIFVLSDEIYSELVYEQ
PHTSIAHFPEMREKTIVINGLSKSHSMTGWRIGFLFAPSYLAKHILKVHQYNVTCASSISQYAALEALTA
GKDDAKMMRHQYKKRRDYVYNRLISMGLDVEKPTGAFYLFPSIGHFTMSSFDFALDLVEEAGLAVVPGSA
FSEYGEGYVRLSYAYSIETLKEGLDRLEAFLQQKAKS
>gnl|CDD|181084 PRK07688, PRK07688, thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
MNERYSRQELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLY
TESDVKNNLPKAVAAKKRLEEINSDVRVEAIVQDVTAEELEELVTGVDLIIDATDNFETRFIVNDAAQKY
GIPWIYGACVGSYGLSYTIIPGKTPCLRCLLQSIPLGGATCDTAGIISPAVQIVASYQVTEALKLLVGDY
EALRDGLVSFDVWKNEYSCMNVQKLKKDNCPSCGEKALYPYLNYENTTKTAVLCGRNTVQIRPPHKEEYD
LEELAELLRDRGLDVNVNPYLLSFSLEEKRLVLFKDGRVLVHGTKDISEAKTIYHRYIG
>gnl|CDD|181085 PRK07691, PRK07691, putative monovalent cation/H+ antiporter subunit D; Reviewed
IMNNLVILPILIPVITAILLIFLGKRPIIQRYVALIGSLLTLVAAIILVANVYKHGIQTLELGNWKAPFG
IVFVADMFAALLVLTSSIITFLVILYSFQTIGIERERYYYYPSVLFMLAGVNGAFLTGDIFNLFVFFEVM
LMASYVLIVIGGTKIQLRESIKYVLINVVSSAFFVVAVAILYSVVGTLNMADISVKIAELSAGQTGLITV
VAILFLFVFATKAGLFPLYFWLPGSYYAPPIAIAALFGALLTKVGVYAIARTFTLFFSHDTSFTHYLILI
LALLTIIFGVIGAVAYFDIKKIIIYNIMIAVGVILVGVAMMTESGMIGAIYYLIHDMIVKAALFLLIGIM
IKITGTTDLKKMGGLIKRYPVLGWMFFIAALSLAGIPPLSGFYGKFFIVEGTFEAGFYVSGIIVLLSSLL
VLYSVIKIFLKGFWGEPKGYDLNNKVPVKKLLLPAVVLVAITILYGLGAEPLYPYVKQAAETLYDPSTYI
EAVLKE
>gnl|CDD|181086 PRK07695, PRK07695, thiazole tautomerase TenI
KNELHVISNGHQSFEELVAVAMQIHSEVDYIHIREREKSAKELYEGVESLLKKGVPASKLIINDRVDIAL
LLNIHRVQLGYRSFSVRSVREKFPYLHVGYSVHSLEEAIQAEKNGADYVVYGHVFPTDCKKGVPARGLEE
LSDIARALSIPVIAIGGITPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAESIKKWA
>gnl|CDD|181087 PRK07701, flgL, flagellar hook-associated protein FlgL; Validated
MRVTQNMLANNFLRNINSNLEKLDKYQEQLSTGKKITRPSDDPVVAMKSLRYRTDLAEVEQYQKNASDAK
SWLENTESALDQATDILQRARELAVQAANGTNTQTDRQAIAQEIEQLKEQLIQIANTQYNGRYIFNGTKT
DTPPVTDDGDNIENSTDSGDIEFEIAKGNTINVNVPGDKAFGGQSGGGSNLFEMLDNLENALDSGDTQGV
SNLLSDIDQHIDNVLAVRAELGARSNRLELIENRLSDQEVNATKLLSDNEDVDLAEVITDLKTQENVYRA
ALAVGARIIQPSLVDFLR
>gnl|CDD|181088 PRK07708, PRK07708, hypothetical protein; Validated
MKYRIHWTYKTKKGLQTELTSDWMNIEEALQLAEDFEKTGRVKELEFYDEMDTEWSLKELKKLSKEVEEE
PHEILVYFDGGFDKETKLAGLGIVIYYKQGNKRYRIRRNAYIEGIYDNNEAEYAALYYAMQELEELGVKH
EPVTFRGDSQVVLNQLAGEWPCYDEHLNHWLDRIEQKLKQLKLTPVYEPISRKQNKEADQLATQALEGTV
IESHKELTE
>gnl|CDD|169068 PRK07709, PRK07709, fructose-bisphosphate aldolase; Provisional
MPLVSMKEMLNKALEGKYAVGQFNMNNLEWTQAILAAAEEEKSPVILGVSEGAARHMTGFKTVVAMVKAL
IEEMNITVPVAIHLDHGSSFEKCKEAIDAGFTSVMIDASHHPFEENVETTKKVVEYAHARNVSVEAELGT
VGGQEDDVIAEGVIYADPAECKHLVEATGIDCLAPALGSVHGPYKGEPNLGFAEMEQVRDFTGVPLVLHG
GTGIPTADIEKAISLGTSKINVNTENQIEFTKAVREVLNKDQEVYDPRKFIGPGRDAIKATVIGKIREFG
SNGKA
>gnl|CDD|236076 PRK07710, PRK07710, acetolactate synthase large subunit
TNVMRTMSSKTEEKLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAE
GYARISGKPGVVIATSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHN
YQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKDMVVEEGEFCYDVQMDLPGYQPNYEPNLLQIRKLVQ
AVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTLLGLGGFPADHPLFLGMAGMHGTYTANMALY
ECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIVADAKQALQVLLQQEGKKENH
HEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFKTPDKWVTS
GGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRQWQEE
FYNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMPMVAPG
KGLHEMVGVKK
>gnl|CDD|236077 PRK07714, PRK07714, YlxQ family RNA-binding protein
MSMSDWKSFLGLANRARKVISGEELVLKEVRSGKAKLVLLSEDASVNTTKKITDKCTYYNVPMRKVENRQ
QLGHAIGKDERVVVAVLDEGFAKKLRSMLD
>gnl|CDD|181090 PRK07718, fliL, flagellar basal body-associated protein FliL; Reviewed
MKNKLIKIMLIILIVIALIGTAALVLVMGFSEAKKQSGEPTIDEIVESSVDTPEITTNLKSGNFIRIQFK
IETDSKKAKEELEKRDFQVKNIIIEELADMNAEDFKGKKGLEALKEQLKEKINNLMQEGKVEKVYITSFI
LQ
>gnl|CDD|181091 PRK07720, fliJ, flagellar biosynthesis chaperone FliJ
MAYTFRLQKVLELKENEKEKALGEYEEAVSRFEQVAEKLYELLKQKEDLEQAKEEKLQSGLSIQEIRHYQ
QFVTNLERTIDHYQLLVMQAREQMNRKQQDLTEKNIEVKKYEKMKEKKQEMFALEEKAAEMKEMDEISIQ
QFARQG
>gnl|CDD|181092 PRK07721, fliI, flagellar protein export ATPase FliI
MKTQQLIDCIETLDPYKRYGKVSRVIGLMIESKGPESSIGDVCYIHTKGGGDKAIKAEVVGFKDEHVLLM
PYTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIRE
PMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSADLNVIALIGERGREVREFIERDLGPE
GLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGY
TPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVL
KSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREIDEAIQFYPQIISFLKQGTDEK
ATFEESIQALLSLFGKGE
>gnl|CDD|236078 PRK07726, PRK07726, DNA topoisomerase 3
MRLFIAEKPSVGRDIADVLKPHKKGDGYIEGNGYIVTWAIGHLLELAEPEAYDERYKRWRLEDLPIIPEK
WKLVVKKKTAKQFNVVKKLLKQATEIVIATDADREGELIAREILDYCGVRKPIKRLWISSLTDKAIKRAF
ANLKPGKETIPLYYSALARSRADWLVGINMTRAYTLLGRKAGYNGVLSVGRVQTPTLALVVRRDEEIENF
VPKPYWEVEAHLTPGERFTAKWQPSEPYQDEEGRLLDRPLAEQVVARIQGQPAKVTEVETKRKKEYAPLL
YDLSELQIDANKRFGLSAKETLDIAQSLYETHKLITYPRTDSRYLPEDMVATLPEVLNAISKVDPYLLLA
PPVLDPSIRSRAWNDKKVTAHHAIIPTEQPPNLSKLSEDERKVYDLIARRYLAQFLPPAEYDKTTIELEI
AGGTFIAKGKQVVEAGWKALLGKKEEDEEKEQPLPVLAKGDELKVEKGEVKEGQTQPPKRFTEGTLLSAM
ENIARFVQDKELKKTLKETDGLGTEATRAGIIEKLFKRGYLEKKGKYIHATDKGKQLIDALPEELTSPDM
TAKWEQALDQISEGQLSYQDFMQPLKQWLKQLVEQAKQSSEKYKFDNLTGPKCPDCGKPMLKVKGKNGKM
LVCQDRECGKRKNVSKKTNARCPNCKKK
>gnl|CDD|236079 PRK07729, PRK07729, glyceraldehyde-3-phosphate dehydrogenase; Validated
MKTKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGK
KIRLLNNRDPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLD
IEKHTIISNASCTTNCLAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTT
GAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPL
VSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGYSCRVVDLVTLVADELAKQENVQHI
>gnl|CDD|236080 PRK07734, motB, flagellar motor protein MotB; Reviewed
KKNRKKKKKKHEEHIDESWLIPYADLLTLLLALFIVLFAMSSIDAAKFKQMAVAFNSEFAGGTGVKDFLS
DQKPEDEKELSASSLEAEQAKKKEEAEAKKKKEMEELKAVQKKIDQYIKEKQLSSSLQTKLTEEGLLITI
LDNILFDSGKADVRLEDLPLAKEISNLLVSNPPRNITISGHTDNVPIANAQFASNWELSVMRAVNFMQVL
LENKELDPEKFSAKGYGEYKPIASNDTAEGRAKNRRVEVLILPLTEKNK
>gnl|CDD|236081 PRK07735, PRK07735, NADH-quinone oxidoreductase subunit C
MDPEKDLEDLKKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAK
AAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAA
ALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAA
AKAKAAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTKGAEGKKEEEPKQEEPSVNQPYLNK
YVEVIKEKLGEDVLEDSYINKLSKDVPTLVVEPEKYYEVAELLRFHEQLAFDYLSELHGTDFVTHMEVYV
HLYSYGKRQSVAVKVKLDREAPQVESVTPLWKGANWPEREAYDLLGIVFKGHPNLSRILLPDDWVGHPLR
KDYEPYDVEV
>gnl|CDD|236082 PRK07737, fliD, flagellar hook-associated protein 2
MVMRITGLASGMDIDDIVSKLMKTERAPLDKLTQKKQTLEWQRDSYREMNTLLKDLDDYIFNNITRQSTY
LKKTVTSSNESVVTATASSSAANGSTTMQVTQLATAATWKSSAKTSFYTGADQTLTFNVTNPGETTAKTV
EISVKQTDTLDDVISKLNSSDLGVSAFKDKIWNGTEYVETIAITSKATGAGASIQAADGATASFFSQQLG
FTNLDADNELTAKTEGQNAQVTINGLQTERTSNTFTINGVTYTLKNTTAGTVTLSVATDVDGIFNKIKDF
VDKYNELIDKINAKLKEERYRDYPPLTDEQKEAMTEKQIELWEEKAKSGLLRGDSILSSALSKMRMDFYT
KVEGIDGGFSQLAQIGITTSSNYLDGGKLEIDETKLRQKIKENPDAVYQLFNSGGSSSNYNEKGIARRLR
DTLKETIKSIEQKAGNTTMTNQQFAIGKDLNQIETQIDRFQDRLKQIEDRYYKKFSAMEKAIQKANEQSM
YLMNALGGGAQ
>gnl|CDD|236083 PRK07738, PRK07738, flagellar protein FlaG; Provisional
MTIERLSSSEPSYEAYRTEQVNSQVEKSEVPEQETGQQSEYEVSKEDLEEVVDGMNELLEPSQTSLKFEL
HEKLNEYYVQVVDERTNEVIREIPPKKLLDMYAAMMEFVGLLVDKKI
>gnl|CDD|236084 PRK07739, flgK, flagellar hook-associated protein FlgK; Validated
MMSTFMGLETARRGLFAQQAALYVTGHNIANANTPGYTRQRVNLAATPPYPTPGMNRPKIPGQMGTGVEA
GSVERIRDQFLDIQYRRENNKLGYWETKADALSQMEDIMNEPSDTGLNKVLDQFWNSLQELSKNPENLGA
RSVVRQRAQALAETFNYLSQSLTDIQNDLKSEIDVTVKEINSLASQISDLNKQIAKVEPNGYLPNDLYDQ
RDLLLDELSKIVNITVEYNKSGGNALEDAEGTFRIDILGGNGKGTLVDGKDSTVNELSVNKDDVTGLVTD
LSLGGTTVSWDDTGQPVNPSSGKLKGLLEMYGYMSGNGEEKGLYPEMLNDLDKLAYTFATAFNEVHKQGY
GLNGSTGIDFFDGTGDSTKGAAKTIKVSDDILADLNNIAAASDDGELGDGSNALNLANLKDFKLNSGLDT
TTFDDFYQSLIGNLGVDAQEANRMAENQEVLVDQVDNRRQSVSGVSLDEEMTNMIKFQHAYNAAARMITA
IDEMLDKIINGMGIVGR
>gnl|CDD|236085 PRK07740, PRK07740, hypothetical protein; Provisional
MERMNPMQRLWRQLSLGLPRSASAAMLGSDNALQQEAWIRSIQKEAKRDDVLDIPLTDLPFVVFDLETTG
FSPQQGDEILSIGAVKTKGGEVETDTFYSLVKPKRPIPEHILELTGITAEDVAFAPPLAEVLHRFYAFIG
AGVLVAHHAGHDKAFLRHALWRTYRQPFTHRLIDTMFLTKLLAHERDFPTLDDALAYYGIPIPRRHHALG
DALMTAKLWAILLVEAQQRGITTLHDLYAALSRC
>gnl|CDD|236086 PRK07742, PRK07742, phosphate butyryltransferase; Validated
MKLEHLIDQAAGQPKKTVAVAVAEDEEVIEAVAKAIELQLARFRLYGNQEKIMGMLQEHGLQTSEHIEII
HAQSSAEAAELAVKAVRNGEADVLMKGNVPTANILKAVLNKEWGLRKGSVLSHVAVFEVPNYDRLIFVTD
AAMNIAPDLEQKAAIIQNAVEVARAIGIDLPKVAPLAAVEVVNPAMQATIDAAALTQMNRRGQIKNCVVD
GPLALDNAVSQIAAEHKGIVSDVAGKADILLVPTIEAGNVLYKSLVYFADAKVGAMIAGAKAPIVLTSRA
DSAETKLYSLALAVCTASK
>gnl|CDD|236087 PRK07748, PRK07748, 3'-5' exonuclease KapD
MDEQQFLFLDFEFTMPQHKKKPKGFFPEIIEVGLVSVVGCEVEDTFSSYVKPKTFPSLTERCKSFLGITQ
EDVDKGISFEELVEKLAEYDKRCKPTIVTWGNMDMKVLKHNCEKAGVPFPFKGQCRDLSLEYKKFFGERN
QTGLWKAIEEYGKEGTGKHHCALDDAMTTYNIFKLVEKDKEYLVKPEPPTIGERVDFSKVLKKVSTQ
>gnl|CDD|169084 PRK07756, PRK07756, NADH-quinone oxidoreductase subunit A
MASVYENSYMIVLIFLLLGILLPVVALTLGRMLRPNKPSAAKATTYESGIEPFHDANIRFHARYYIFALL
FVIFDVETLFLYPWAVAYDKLGLFALIEMLIFVVMLLVGLAYAWKKKVLQWL
>gnl|CDD|236088 PRK07757, PRK07757, N-acetyltransferase
MMEIRKARLSDVKAIHALINVYAKKGLMLPRSLDELYENIRDFYVAEEEGEIVGCCALHILWEDLAEIRS
LAVSEDYRGQGIGRMLVEACLEEARELGVKRVFALTYQPEFFEKLGFREVDKEALPQKVWADCIKCPKFP
NCDEIAMIKELG
>gnl|CDD|181104 PRK07758, PRK07758, hypothetical protein; Provisional
MATEKTLRTCEKGHEYYKSSDCPTCPTCEKERKPKEGFLSLLSAPARRALEHHGIHTVEELSKYSEKEIL
KLHGMGPASLPKLRKALEESGLSFK
>gnl|CDD|236090 PRK07764, PRK07764, DNA polymerase III subunits gamma and tau; Validated
MALALYRRYRPATFAEVIGQEHVTEPLSTALDSGRINHAYLFSGPRGCGKTSSARILARSLNCVEGPTST
PCGECDSCVALAPGGPGSLDVTEIDAASHGGVDDARELRERAFFAPAESRYKIFIIDEAHMVTPQGFNAL
LKIVEEPPEHLKFIFATTEPDKVIGTIRSRTHHYPFRLVPPEVMRGYLERICAQEGVPVEPGVLPLVIRA
GGGSVRDSLSVLDQLLAGAGPEGVTYERAVALLGVTDSALIDEAVDALAAGDGAALFGTVDRVIEAGHDP
RRFAEDLLERLRDLIVLQAVPDAAERGLVDAPADQLDRMRAQAQRLGPAELTRAADVVNDGLTEMRGATS
PRLLLELLCARMLLPSASDDERGLLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAA
AAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAP
AAAPAAPAAPAAPAGADDAATLRERWPEILAAVPKRSRKTWAILLPEATVLGVRGDTLVLGFSTGGLARR
FASPGNAEVLVTALAEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPA
GAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQ
PAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAP
AAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAMELLEEELGAKKIEEFAAD
>gnl|CDD|181107 PRK07765, PRK07765, aminodeoxychorismate/anthranilate synthase component II
MRILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQFDGVLLSPGPGTPERAGASIDMVR
ACAAAGTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPET
LPAELEVTARTDSGVIMAVRHRELPIHGVQFHPESVLTEGGHRMLANWLTVCGWAPDEALVRRLENEVAA
AVAP
>gnl|CDD|236091 PRK07768, PRK07768, long-chain-fatty-acid--CoA ligase; Validated
MSRFTEKMYANARTSPRGMVTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPT
AQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRVIGMIGAKAVVVGEPFLAAAPVLEEKGIRVLTVADLLA
ADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGMV
GFLTVPMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRRQAKPGAFDLSSLRF
ALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGMAEATLAVSFSPCGAGLVVDEVDADLLAALRRAVP
ATKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYLTMDGFIPAQDADGWLDTGD
LGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGHSREGFAVAVESNAF
EDPAEVRRIRHQVAHEVVAEVGVRPRNVVVLGPGSIPKTPSGKLRRANAAELVTP
>gnl|CDD|181109 PRK07769, PRK07769, long-chain-fatty-acid--CoA ligase; Validated
MNMAFHNPFDVNGKIRFPPNTNLVRHVERWAKVRGDKLAYRFLDFSTERDGVARDLTWSQFGARNRAVGA
RLQQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGRLHAVLDDCTPSAILTTTDSA
EGVRKFFRARPAKERPRVIAVDAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVL
QVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRRPGRWIRELARKPGGTGGTFS
AAPNFAFEHAAARGLPKDGEPPLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEAT
LFVSTTPMDEEPTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGE
IWLHGNNIGTGYWGKPEETAATFQNILKSRLSESHAEGAPDDALWVRTGDYGVYFDGELYITGRVKDLVI
IDGRNHYPQDLEYTAQEATKALRTGYVAAFSVPANQLPQVVFDDSHAGLKFDPEDTSEQLVIVAERAPGA
HKLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSLRSGYGQPAFPDAS
D
>gnl|CDD|236092 PRK07772, PRK07772, single-stranded DNA-binding protein; Provisional
MAGDTTITVVGNLTADPELRFTPSGAAVANFTVASTPRTFDRQTNEWKDGEALFLRCSIWRQAAENVAES
LTKGMRVIVTGRLKQRSYETREGEKRTVVELEVDEIGPSLRYATAKVTRASRGGGGGGGGGGFGGGGGGS
GGGGGGGGGGGAPGGGGAQASAPADDPWSSAPASGGFGGGDDEPPF
>gnl|CDD|236093 PRK07773, PRK07773, replicative DNA helicase; Validated
MAVVDDLAPGMDSSPPSEDYGRQPPQDLAAEQSVLGGMLLSKEAIARVLERLRPGAFYRPAHQNIYDAIL
DLYGRGEPADLVTVAAELDRRGLLERIGGAPYLHTLISTVPTAANADYYARIVAEKALLRRLIEAGTRIV
QYGYAEGADVAEVVDRAQAEIYDVTDRRLSEDFVALEDLLQPTFDEIDAIASSGGLARGVPTGFTELDAM
TNGLHPGQLIIVAARPSMGKTTFGLDFARNCAIRHRLAVAIFSLEMSKEQLVMRLLSAEAKIKLSDMRSG
RMSDDDWTRLARAMGEISEAPIFIDDTPNLTVMEIRAKARRLRQEANLGLIVVDYLQLMTSGKKYENRQQ
EVSEISRHLKLLAKELEVPVVALSQLSRGVEQRTDKRPMLSDLRESGCLTGDTLILRADTGAEVPIGELV
GERPFAVWALDERTLRLVAAPVSNVFPTGRKPVFRLRTRSGREIRATANHPFLTFEGWKRLDELKVGDRL
ALPRRVPSPDTQRMTEAELALLGHLIGDGCTLPRHPIQYTSVDANLAAVVVSLAHSVFGDYIAPRIPSER
RWYQVYLPARQRLTRGKRNPIAAWLDGLGLFGLRSHEKFVPEAVFRQPNDQVALFLRHLWSTDGSVRLRD
GKNPQPRVYYASSSRRLADDVQQLLLRLGINARLTHVPQLGKGRDQYHVHISGAKDLVRFLRHVGAVGAE
KVAALEMLRQYLKGPVRNPNRDSIPKKVWAQLVRNRLSAKGMTHRQLHAPLGMAYCGSTLWKHNLSRERA
HRVAARIESRAIHELARSDVYWDTVVSITSIGEEEVFDLTVPGTHNFVANGIIVHNSIEQDADVVILLYR
PDYYDRDDPRGGEAEFIVAKHRNGPTGTVTLAFQLHLSRFANLARS
>gnl|CDD|236094 PRK07774, PRK07774, SDR family oxidoreductase
MGRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSA
KAMADATVSAFGGIDYLVNNAAIYGGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAI
VNQSSTAAWLYSNFYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPKEFVADMVKGIP
LSRMGTPEDLVGMCLFLLSDEASWITGQIFNVDGGQIIRS
>gnl|CDD|181113 PRK07775, PRK07775, SDR family oxidoreductase
MPRFEPHPDRRPALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTD
PDSVKSFVAQAEEALGEIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGD
LIFVGSDVALRQRPHMGAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMGWSLPAEVIGPMLE
DWAKWGQARHDYFLRASDLARAITFVAETPRGAHVVNMEVQPEAPLRAPADRQKLALGEEGMPG
>gnl|CDD|236095 PRK07777, PRK07777, putative succinyldiaminopimelate transaminase DapC
MTVSRLRPFGTTIFAEMSALAVRTGAVNLGQGFPDEDGPPEMLEAAQEAIAGGVNQYPPGPGIPELRAAI
AAQRRRRYGLEYDPDTEVLVTVGATEAIAAAVLGLVEPGDEVLLIEPYYDSYAAVIAMAGAHRVPVPLVP
DGRGFALDLDALRAAVTPRTRALIVNSPHNPTGTVLTAAELAAIAELAVEHDLLVITDEVYEHLVFDGAR
HLPLATLPGMRERTVTISSAAKTFNVTGWKIGWACGPAPLIAAVRAAKQYLTYVGGAPFQPAVAHALDHE
DAWVAALRDSLQAKRDRLAAGLAEAGFEVHDSAGTYFLCADPRPLGYDDGTEFCRALPERVGVAAIPMSV
FYDPADAWNHLVRFAFCKRDDTLDEAIRRLRALRGRG
>gnl|CDD|181115 PRK07785, PRK07785, NADH dehydrogenase subunit C; Provisional
EGSPSSPNPADGTPGPASPTPEVIDVRRGMFGVSGTGDTSGYGGLVRPVTLPGSSPRPYGGYFDEVADRL
EEALPEFADAIERVVVDRGELTLHVRREHLVEVAQTLRDDPALRFELCLGVSGVHYPHDTGRELHAVYHL
TSITHNRRIRLEVAVPDADPHIPSLVSVYPTNDWHERETYDFFGIVFDGHPALTRIEMPDDWVGHPQRKD
YPLGGIPVEYKGATIPPPDQRRSYS
>gnl|CDD|169098 PRK07786, PRK07786, long-chain-fatty-acid--CoA ligase; Validated
TRALTLAQEQPYLARRQNWVNQLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRV
LILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLST
VVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTN
GADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVC
AEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCMLLGEDAIRKLGSVGKV
IPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDR
KKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRL
ARYKHPKALEIVDALPRNPAGKVLKTELRERYGACVNVERRSASAGFTERRE
>gnl|CDD|236096 PRK07787, PRK07787, acyl-CoA synthetase; Validated
LASLNPAAVAAAADIADAVRIGGRVLSRSDLAGAATAVAERVAGARRVAVLATPTLATVLAVVGALIAGV
PVVPVPPDSGVAERRHILADSGAQAWLGPAPDDPAGLPHVPVRLHARSWHRYPEPDPDAPALIVYTSGTT
GPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYA
QALSEGGTLYFGVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLI
TLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGETVGELQVRGPTLFDGYLNRPDATAAAFTADG
WFRTGDVAVVDPDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV
VGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG
>gnl|CDD|236097 PRK07788, PRK07788, acyl-CoA synthetase; Validated
MKLMKSVSGYLTRGSAEAHYLRVMIRSGAVDLERPDNGLRLAADIRRYGPFAGLVAHAARRAPDRAALID
ERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAE
VAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKPPKPGG
IVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLRR
RFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPV
LYNLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGR
DKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQ
RLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD
>gnl|CDD|236098 PRK07789, PRK07789, acetolactate synthase 1 catalytic subunit; Validated
PSPPTPAAAASAAPPPAAPAARPRIVAPERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKV
RHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVTPIADANMDSVPVVAITGQVGRGLIGTDAF
QEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPKDALQAQTTFSWPPRMDLPGY
RPVTKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTTLMARGAFPDSHPQHL
GMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHADVPIVGDVK
EVIAELIAALRAEHAAGGKPDLTAWWAYLDGWRETYPLGYDEPSDGSLAPQYVIERLGEIAGPDAIYVAG
VGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIE
GIPIKVALINNGNLGMVRQWQTLFYEERYSNTDLHTHSHRIPDFVKLAEAYGCVGLRCEREEDVDAVIEK
ARAINDRPVVIDFVVGKDAMVWPMVAAGTSNDEIQYARGIRPLFDDEEEAAE
>gnl|CDD|236099 PRK07791, PRK07791, short chain dehydrogenase; Provisional
MGLLDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIGVGLDGSASGGSAAQAVVDEIVAAGGEAVANG
DDIADWDGAANLVDAAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRA
ESKAGRAVDARIINTSSGAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPAARTRMTETV
FAEMMAKPEEGEFDAMAPENVSPLVVWLGSAESRDVTGKVFEVEGGKISVAEGWRHGPTVDKGARWDPAE
LGPVVA
>gnl|CDD|181120 PRK07792, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
SPRTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVLDEIRAAGAKAVAVAGD
ISQRATADELVATAVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRAKAK
AAGGPVYGRIVNTSSEAGLVGPVGQANYGAAKAGITALTLSAARALGRYGVRANAICPRARTAMTADVFG
DAPDVEAGGIDPLSPEHVVPLVQFLASPAAAEVNGQVFIVYGPMVTLVAAPVVERRFDADGDAWDPGELS
ATLRDYFADRDPEESFSATALLRQRR
>gnl|CDD|236100 PRK07798, PRK07798, acyl-CoA synthetase; Validated
MAWNIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAM
LGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLP
GAVDYEDALAAGSPERDFGERSPDDLYLLYTGGTTGMPKGVMWRQEDIFRVLLGGRDFATGEPIEDEEEL
AKRAAAGPGMRRFPAPPLMHGAGQWAAFAALFSGQTVVLLPDVRFDADEVWRTIEREKVNVITIVGDAMA
RPLLDALEARGPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLTDSIGSSETGFGGSGTVAKGAVHTG
GPRFTIGPRTVVLDEDGNPVEPGSGEIGWIARRGHIPLGYYKDPEKTAETFPTIDGVRYAIPGDRARVEA
DGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAEL
RAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYRWAKEQAAER
>gnl|CDD|181122 PRK07799, PRK07799, crotonase/enoyl-CoA hydratase family protein
MEGGPHALVEQRGHTLIVTMNRPEARNALSTEMLRIMVDAWDRVDNDPDIRSCILTGAGGAFCAGMDLKA
ATKKPPGDSFKDGSYDPSRIDALLKGRRLTKPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKW
SLFPMGGSAVRLVRQIPYTVACDLLLTGRHITAAEAKEIGLIGHVVPDGQALDKALELAELINANGPLAV
QAILRTIRETEGMHENEAFKIDTKIGIPVFLSEDAKEGPRAFAEKRAPNFQGR
>gnl|CDD|181123 PRK07801, PRK07801, acetyl-CoA C-acetyltransferase
MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTS
WLAAGLPEEVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGEQLGFTSPF
AESKGWLHRYGDQEVSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGGVTVDEG
PRETSLEKMAGLKPLVEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLT
APIPATRYALEKTGLSIDDIDVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTT
LLHELERTGGRYGLQTMCEGGGTANVTIIERL
>gnl|CDD|236101 PRK07803, sdhA, succinate dehydrogenase flavoprotein subunit; Reviewed
MTEVERHSYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSLFGKAHTVMAEGGCAAAMGNVNPKDNWQVH
FRDTMRGGKFLNNWRMAELHAKEAPDRVWELETYGALFDRTKDGRISQRNFGGHTYPRLAHVGDRTGLEL
IRTLQQKIVSLQQEDHAELGDYEARIKVFAECTITELLKDGGRIAGAFGYWRESGRFVLFEAPAVVLATG
GIGKSFKVTSNSWEYTGDGHALALRAGATLINMEFVQFHPTGMVWPPSVKGILVTEGVRGDGGVLKNSEG
KRFMFDYIPDVFKGQYAETEEEADRWYKDNDNNRRPPELLPRDEVARAINSEVKAGRGSPHGGVYLDIAS
RLPAEEIKRRLPSMYHQFKELADVDITKEPMEVGPTCHYVMGGVEVDPDTGAATVPGLFAAGECAGGMHG
SNRLGGNSLSDLLVFGRRAGLGAADYVRGLGSRPAVSEEAVDAAAREALAPFERPAGAENPYTLHAELQQ
TMNDLVGIIRKEDEIEQALEKLAELKERAANVSVEGHRQYNPGWHLALDLRNMLLVSECVARAALERTES
RGGHTRDDHPGMDPEWRRINLVCRADPVGGHVTVTRQPQPPMRPDLLALFEISELEKYYTDEELAE
>gnl|CDD|236102 PRK07804, PRK07804, L-aspartate oxidase; Provisional
ALPRRLAAPAPGWRDAADVVVVGSGVAGLTAALAARRAGRRVLVVTKAALDDGSTRWAQGGIAAVLDPGD
SPEAHVADTLVAGAGLCDPDAVRSLVAEGPRAVRELVALGARFDESPDGRWALTREGGHSRRRIVHAGGD
ATGAEVQRALDAAVRADPLDIREHALALDLLTDGTGAVAGVTLHVLGEGSPDGVGAVHAPAVVLATGGLG
QLYAATTNPAGSTGDGVALALRAGAAVSDLEFVQFHPTVLFLGPAAGGQRPLISEAVRGEGAILVDAQGN
RFMAGVHPLADLAPRDVVAKAIDRRMKATGDDHVYLDARGIEGFARRFPTITASCRAAGIDPVRQPIPVA
PAAHYSCGGVVTDVYGRTSVPGLYAAGEVACTGVHGANRLASNSLLEGLVVGERAGAAAAAHAAAAGRPR
ATPAVGPEPGLLPALDRAELQRAMTRGAGVLRSAAGLARAADRLAAGAPARVVPGRADWEDTNLTLVARA
LVAAALARTESRGCHWREDFPDTDDEWARSIVVRLADDGNLVVVQALVAVC
>gnl|CDD|181126 PRK07806, PRK07806, SDR family oxidoreductase
MGDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKVVAEIEAAGGRASAVGADLTDEES
VAALMDTAREEFGGLDALVLNASGGMESGMDEDYAMRLNRDAQRNLARAALPLMPAGSRVVFVTSHQAHF
IPTVKTMPEYEPVARSKRAGEDALRALRPELAEKGIGFVVVSGDMIEGTVTATLLNRLNPGAIEARREAA
GKLYTVSEFAAEVARAVTAPVPSGHIEYVGGADYFLTA
>gnl|CDD|181127 PRK07807, PRK07807, GuaB1 family IMP dehydrogenase-related protein
MRFLNGHRPAYDLTYDDVFLVPSRSDVGSRFDVDLSTADGTGTTIPLVVANMTAVAGRRMAETVARRGGL
VVLPQDIPIDVVAEVVAWVKSRDLVFDTPVTLSPDDTVGDALALLPKRAHGAVVVVDEEGRPVGVVTEAD
CAGVDRFTQVRDVMSTDLVTLPAGTDPREAFDLLEAARVKLAPVVDADGRLVGVLTRTGALRATIYTPAV
DAAGRLRVAAAVGINGDVAAKARALLEAGVDVLVVDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAE
GTRDLVEAGADIVKVGVGPGAMCTTRMMTGVGRPQFSAVLECAAAARELGAHVWADGGVRHPRDVALALA
AGASNVMIGSWFAGTYESPGDLMRDRDGRPYKESFGMASARAVAARTAGDSAFDRARKALFEEGISTSRM
YLDPGRPGVEDLLDHITSGVRSSCTYAGARTLAEFHERAVVGVQSAAGYAEGRPLPTSW
>gnl|CDD|236103 PRK07810, PRK07810, O-succinylhomoserine sulfhydrylase; Provisional
DSSVRTPKALPDGVSQATIGVRGGLLRSGFEETAEALYLTSGYVYESAAAAEAAFTGELDRFVYSRYGNP
TVSMFEERLRLIEGAEACFATASGMSAVFTALGALLGAGDRLVAARSLFGSCFVVCNEILPRWGVETVFV
DGEDLSQWEEALSVPTQAVFFETPSNPMQSLVDIAAVSELAHAAGAKVVLDNVFATPLLQRGLPLGADVV
VYSGTKHIDGQGRVLGGAILGDREYIDGPVQKLMRHTGPALSAFNAWVLLKGLETLALRVRHSNASALRI
AEFLEGHPAVRWVRYPFLPSHPQYDLAKRQMSGGGTVVTFELDAPEDAAKKRAFEVLDKLRVIDISNNLG
DAKSLITHPATTTHRAMGPEGRAAIGLGDGVVRLSVGLEDTDDLIADLDRALG
>gnl|CDD|236104 PRK07811, PRK07811, cystathionine gamma-synthase; Provisional
SEDMSDHHANQGFATRAIHAGYEPDPATGAVNPPIYASSTFAQDGVGGLRGGYEYARTGNPTRTALEEQL
AALEGGAYGRAFSSGMAATDCLLRAVLRPGDHIVIPNDAYGGTFRLIDKVFTRWGVEYTPVDLSDLDAVR
AAITPRTKLIWVETPTNPLLSITDIAALAELAHDAGAKVVVDNTFASPYLQQPLALGADVVVHSTTKYIG
GHSDVVGGALVTNDEELDEAFAFLQNGAGAVPGPFDAYLTLRGLKTLAVRMDRHSENAEAVAEFLAGHPE
VSTVLYPGLPSHPGHEVAARQMRGFGGMVSVRLAGGEEAARDFCARTKVFTLAESLGGVESLIEHPSAMT
HASTAGSQLEVPDDLVRLSVGIEDVADLLADLEQALGQ
>gnl|CDD|236105 PRK07812, PRK07812, O-acetylhomoserine aminocarboxypropyltransferase; Validated
STSTDADPTANWSFETKQIHAGQTPDPATNARALPIYQTTSYTFDDTDHAAALFGLAEPGNIYTRIMNPT
QDVVEQRIAALEGGVAALLLASGQAAETFAILNLAGAGDHIVSSPRLYGGTYNLFHYTLPKLGIEVSFVE
DPDDLDAWRAAVRPNTKAFFAETISNPQIDVLDIPGVAEVAHEAGVPLIVDNTIATPYLIRPLEHGADIV
VHSATKYLGGHGTAIAGVIVDGGTFDWTQGRFPGFTTPDPSYHGVVFAELGPPAYALKARVQLLRDLGSA
ISPFNAFLIAQGLETLSLRIERHVANAQRVAEFLEARDEVASVNYAGLPSSPWYERAKRLAPKGTGAVLS
FELAGGVEAGKAFVNALTLHSHVANIGDVRSLVIHPASTTHSQLTPEEQLATGVTPGLVRLAVGIEGIDD
ILADLEAGFAAAKAFS
>gnl|CDD|181131 PRK07814, PRK07814, SDR family oxidoreductase
MILDRFRLDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAH
PEATAGLAGQAVEAFGRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSGGG
SVINISSTMGRLAGRGFAAYGTAKAALAHYTRLAALDLCPRIRVNAIAPGSILTSALEVVAANDELRAPM
EKATPLRRLGDPEDIAAAAVYLASPAGSYLTGKTLEVDGGLTFPNLDLPIPDL
>gnl|CDD|181133 PRK07819, PRK07819, 3-hydroxybutyryl-CoA dehydrogenase; Validated
MSDAIQRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLERAVSRGKLTERERDAAL
ARLRFTTDLGDFADRQLVIEAVVEDEAVKTEIFAELDKVVTDPDAVLASNTSSIPIMKLAAATKRPGRVL
GLHFFNPVPVLPLVELVPTLVTSEATVARAEEFASDVLGKQVVRAQDRSGFVVNALLVPYLLSAIRMVES
GFATAEDIDKAMVLGCAHPMGPLRLSDLVGLDTVKAIADSMYEEFKEPLYAPPPLLLRMVEAGLLGKKSG
RGFYTY
>gnl|CDD|236107 PRK07823, PRK07823, S-methyl-5'-thioadenosine phosphorylase
MHNNGAMLGVIGGSGFYSFFGSDAREVNVDTPYGPPSAPITIGEVGGRRVAFLPRHGRDHEFSPHTVPYR
ANMWALRALGVRRVFAPCAVGSLRPELGPGTVVVPDQLVDRTSGRAQTYFDSGGVHVSFADPYCPTLRAA
ALGLPGVVDGGTMVVVQGPRFSTRAESRWFAAQGWSLVNMTGYPEAVLARELELCYAAIALVTDLDAGVE
AGEGVKAVDVFAEFGRNIERLKRLVRDAIAAVPAERTCTHCRAHAGVTLPFELP
>gnl|CDD|236108 PRK07824, PRK07824, o-succinylbenzoate--CoA ligase
ALAGRAPALLPVPAQDERRAALLRDALRVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHDR
LGGPGQWLLALPAHHIAGLQVLVRSVIAGSEPVELDVSAGFDPTALPRAVAELGGGRRYTSLVPMQLAKA
LDDPAATAALAELDAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSGGCVYDGVPLDGVRVRVEDGRI
ALGGPTLAKGYRNPVDPDPFAEPGWFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPA
VADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRA
LVRRFAGE
>gnl|CDD|181136 PRK07825, PRK07825, short chain dehydrogenase; Provisional
DDLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGLVVGGPLDVTDPASFAAFLD
AVEADLGPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAG
KIPVPGMATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELIAGTGGAKGFKNVEPEDVAAAIV
GTVAKPRPEVRVPRALGPLAQAQRLLPRRVREALNRLLGGDRVFLDVDTAARAAYERRARGEA
>gnl|CDD|236109 PRK07827, PRK07827, enoyl-CoA hydratase family protein
DTPVDTLVRYAVDGGVATLTLDSPHNRNALSARLVAQLHDGLRAAAADPAVRAVVLTHTGGTFCAGADLS
EAGGGGGDPYDAAVARAREMTALLRAIVELPKPVIAAIDGHVRAGGFGLVGACDIVVAGPESTFALTEAR
IGVAPAIISLTLLPRLSPRAAARYYLTGEKFGAAEAARIGLVTAAADDVDAAVAALLADLRRGSPQGLAE
SKALTTAAVLAGFDRDAEELTEESARLFVSDEAREGMTAFLQKRPPRWAL
>gnl|CDD|236110 PRK07831, PRK07831, SDR family oxidoreductase
NLSTAPKYVPGHGLLAGKVVLVTAAAGTGIGSATARRALEEGARVVISDIHERRLGETADELAAELGLGR
VEAVVCDVTSEAQVDALIDAAVERLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAAL
RYMRARGHGGVIVNNASVLGWRAQHGQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFLAK
VTSAELLDELAAREAFGRAAEPWEVANVIAFLASDYSSYLTGEVVSVSSQHA
>gnl|CDD|181139 PRK07832, PRK07832, SDR family oxidoreductase
KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRALDISDYDAVAAFAA
DIHAAHGSMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGRGGHLVNVSSAA
GLVALPWHAAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEIAGVDREDPRVQKWVDR
FRGHAVTPEKAAEKILAGVEKNRYLVYTSPDIRALYWFKRKAWWPYSLVMRQVNVFFTRALR
>gnl|CDD|236111 PRK07843, PRK07843, 3-oxosteroid 1-dehydrogenase
MAMTVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGSTARSGGGVWIPNNEVLKRAGVPDTP
EAARTYLHSIVGDVVPPERIDAYLDRGPEMLSFVLAHSPLKLCWVPGYSDYYPEAPGGRPGGRSIEPKPF
DARKLGADLAGLEPPYGKVPLNMVVMQQDYVWLNLLKRHPRGVLRALKVGARTLWAKATGKNLLGMGQAL
AAGLRIGLQRAGVPVLLNTPLTDLYVEDGRVTGVHAAESGEPQLIRARRGVILASGGFEHNEQMRAKYQR
APIGTEWTVGAKANTGDGILAGEKLGAALDLMDDAWWGPTIPLPGGPWFALSERNLPGSIIVNMSGKRFM
NESAPYVEAVHHMYGGEYGQGPGPGENIPAWLVFDQRYRDRYLFAGLQPRQPIPSRWLESGVIVKADTLA
ELAAKIGVPADALTATVQRFNGFARSGVDEDFHRGESAYDRYYGDPTNKPNPNLGELSHAPFYAAKMVPG
DLGTKGGLRTDVRGRVLRDDGSVIEGLYAAGNVSAPVMGHTYAGPGATIGPAMTFGYLAALDIAAQA
>gnl|CDD|236112 PRK07845, PRK07845, flavoprotein disulfide reductase; Reviewed
MTRIVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRF
IDDGEARVDLPAVNARVKALAAAQSADIRARLEREGVRVIAGRGRLIDPGLGPHRVKVTTADGGEETLDA
DVVLIATGASPRILPTAEPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRD
RVLPGEDADAAEVLEEVFARRGMTVLKRSRAESVERTGDGVVVTLTDGRTVEGSHALMAVGSVPNTAGLG
LEEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTGVLPLASVAAMQGRIAMYHALGEAVSPLRLKTVASN
VFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAKMSGLRDGFVKLFCRPGTGVVIGGVVVAPRASE
LILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEAARRLMAHDDLD
>gnl|CDD|181142 PRK07846, PRK07846, mycothione reductase; Reviewed
HYDLIIIGTGSGNSILDERFADKRIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVDAEL
DGVRWPDIVSRVFGRIDPIAAGGEEYRGRDTPNIDVYRGHARFIGPKTLRTGDGEEITADQVVIAAGSRP
VIPPVIADSGVRYHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDIS
ERFTELASKRWDVRLGRNVVGVSQDGSGVTLRLDDGSTVEADVLLVATGRVPNGDLLDAAAAGVDVDEDG
RVVVDEYQRTSAEGVFALGDVSSPYQLKHVANHEARVVQHNLLHPDDLIASDHRFVPAAVFTHPQIASVG
LTENEARAAGLDITVKVQNYGDVAYGWAMEDTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSF
GLDAREMARGQYWIHPALPEVVENALLGLDL
>gnl|CDD|236114 PRK07849, PRK07849, aminodeoxychorismate lyase
MSMPPPVVVTLDPYGGSERVHDPSAPLLHADDLAAVRGDGVFETLLVRDGRPCNLEAHLERLARSAALLD
LPEPDLDRWRRAVELAIEEWRAPEDEAALRLVYSRGRESGGAPTAWVTVSPVPERVARARREGVSVITLD
RGYPSDAAERAPWLLAGAKTLSYAVNMAALRYAARRGADDVIFTSTDGYVLEGPTSTVVIATDDRLLTPP
PWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAADGVWLVSSVRLAARVHTLDGRPLPRDPLADEL
TELVDAAIVSDR
>gnl|CDD|181145 PRK07850, PRK07850, steroid 3-ketoacyl-CoA thiolase
MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTA
WLHAGLPYHVGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGRGLPRPDSW
DIDMPNQFEAAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEEGQPTGETRLV
TRDQGLRDTTMEGLAGLKPVLEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEP
YYHLDGPVQATAKVLEKAGMKIGDIDLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGA
RLITTALHELERTDKSTALITMCAGGALSTGTIIERI
>gnl|CDD|181146 PRK07851, PRK07851, acetyl-CoA C-acetyltransferase
MPEAVIVSTARSPIGRAFKGSLKDMRPDDLAAQMVRAALDKVPALDPTDIDDLMLGCGLPGGEQGFNMAR
VVAVLLGYDFLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSLPDTKNPLFA
EAQARTAARAEGGAEAWHDPREDGLLPDVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGF
FEREITPVTLPDGTVVSTDDGPRAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKAREL
GLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKL
NVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGGGQGMAMVLERLS
>gnl|CDD|236115 PRK07854, PRK07854, enoyl-CoA hydratase; Provisional
MIGVTRDGQVLTIELQRPERRNALNAELCEELREAVRKAVDESARAIVLTGQGTVFCAGADLSGDVYADD
FPDALIEMLHAIDAAPVPVIAAINGPAIGAGLQLAMACDLRVVAPEAYFQFPVAKYGIALDNWTIRRLSS
LVGGGRARAMLLGAEKLTAEQALATGMANRIGTLADAQAWAAEIAGLAPLALQHAKRVLNDDGAIEEAWP
AHKELFDKAWASQDAIEAQVARIEKRPPKFQGA
>gnl|CDD|181147 PRK07855, PRK07855, lipid-transfer protein; Provisional
MLSGKAAIVGIGATEFSKNSGRSELRLACEAVLAALDDAGLAPSDVDGLVTFTMDTNPEIAVARALGIGE
LKFFSRIHYGGGAACATVQQAAMAVATGVADVVVCYRAFNERSGMRFGQGQTGLAENPTSTGVDYGWSYP
HGLLTPAAWVAMLARRYMHEYGATSEDFGRVAVADRKHAATNPKAWFYGRPITLEDHQNSRWIAEPLRLL
DCCQESDGAVALVVTSAERARDLKQRPAVIKAAAQGSGADQYMMTSYYRDDITGLPEMGLVARQLWAQSG
LGPADIDTAILYDHFTPFVLMQLEELGFCGRGEAKDFIADGALELGGRLPINTHGGQLGEAYIHGMNGIA
EAVRQLRGTSVNQVPGVENVLVTAGTGVPTSGLILG
>gnl|CDD|236116 PRK07856, PRK07856, SDR family oxidoreductase
NLDLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGRPAEFHAADVRDPDQVAALVDAIV
ERHGRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGGGSIVNIGSVSGRR
PSPGTAAYGAAKAGLLNLTRSLAVEWAPKVRVNAVVVGLVRTEQSELHYGDAEGIAAVAATVPLGRLATP
ADIAWACLFLASDLASYVSGANLEVHGGGERPAFLAAASANK
>gnl|CDD|236117 PRK07857, PRK07857, chorismate mutase
MRPEPPHHENAELEARMPTGTDDPLSDAEIDELREEIDRLDAEILALVKRRTEVSQAIGKARMASGGTRL
VHSREMKVIERYREELGPEGKDLAMLLLRLGRGRLG
>gnl|CDD|236118 PRK07860, PRK07860, NADH dehydrogenase subunit G; Validated
PPDLVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVT
DGMVVKTQLTSPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFPKPIN
ISTQVLLDRERCVLCARCTRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGA
AYRFRARPFDLVSTPSVCEHCASGCAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTYATQPDRIT
TPLVRDEDGELEPASWSEALAVAARGLAAARGRVGVLVGGRLTVEDAYAYAKFARVALGTNDIDFRARPH
SAEEADFLAARVAGRGLGVTYADLEKAPAVLLVGFEPEEESPIVFLRLRKAARKHGLKVYSIAPFATRGL
EKMGGTLLRTAPGGEAAALDALATGAPDVAELLRTPGAVILVGERLATVPGALSAAARLADATGARLAWV
PRRAGERGALEAGALPTLLPGGRPVADPAARAEVAAAWGVDELPAAPGRDTAGILAAAAAGELGALLVGG
VEPADLPDPAAALAALDAAGFVVSLELRHSAVTERADVVLPVAPVAEKAGTFLNWEGRLRPFEAALRTTG
ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGAWDGARAAAPAVPAAAPPQPGAGEAVLATWRMLLD
DGRLQDGEPHLAGTARPPVARLSAATAAEIGVADGDAVTVSTERGSITLPLAITDMPDRVVWLPLNSPGS
TVRRTLGATAGAVVRIAAGGTATEAGA
>gnl|CDD|236120 PRK07867, PRK07867, acyl-CoA synthetase; Validated
TSSAPTVAELLLPLAEDDDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLL
LGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWADELAAHR
DAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMA
GWAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPG
DIARFARRFGCVVVDGFGSTEGGVAITRTPDTPPGALGPLPPGVAIVDPDTGTECPPAEDADGRLLNADE
AIGELVNTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIE
RILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQPDLGPKQWPSYVRVCAELPR
TATFKVLKRQLSAEGVDCADPVWWIRRLTPSDYAALADE
>gnl|CDD|236121 PRK07868, PRK07868, acyl-CoA synthetase; Validated
VDLNFSAVTRPVERLVATAQNGLEVLRLGGLETGSVPSPFQIVESVPMYRLRRYFPPDNRPGQPPVGPPV
LMVHPMMMSADMWDVTRDDGAVGILHRAGLDPWVIDFGSPDKVEGGMERNLADHVVALSEAIDTVKDVTG
RDVHLVGYSQGGMFCYQAAAYRRSKDIASIVTFGSPVDTLAALPMGIPAGLAAAAADFMADHVFNRLDIP
GWMARTGFQMLDPVKTAKARVDFLRQLHDREALLPREQQRRFLESEGWIAWSGPAISELLKQFIAHNRMM
TGGFAINGQMVTLADITCPVLAFVGEVDDIGQPASVRGIRRAAPNAEVYESLIRAGHFGLVVGSRAAQQT
WPTVADWVKWLEGDGDKPENIHLMADQPAEHTDSGVSLSSRVAHGVGEVAEAALALARGAADAAVAANRS
VRTLAVETARTLPRLARLGQINDHTRISLGRIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLI
AVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPDTDLAAAVRLGGVTEIITDPTNLEAARQLPG
RVLVLGGGESRDLDLPDDADVIDMEKIDPDAVELPGWYRPNPGLARDLAFIAFSTAGGELVAKQITNYRW
ALSAFGTASAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSY
TWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSGAKIGS
KGRPLPGAGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLARARGPIDPTASVKRGVFAPADTWIST
EYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQLAVAAVTLRPGA
AITAADLTEALASLPVGLGPDIVHVVPEIPLSATYRPTVSALRAAGIPKPGRQAWYFDPETNRYRRLTPA
VRAELTGGHRRGAA
>gnl|CDD|181154 PRK07869, PRK07869, amidase; Provisional
MTRVHAFGDDALGDLDAVGLAEAIRAGRVSAAEVVEAAIARAEAVNPALNALAYAAFDRARDRAARPGSQ
GGFFSGVPTFIKDNVDVAGLPTMHGSDAWTPRPAKADSDFARQFLATGLISLGKTQLPEFGFSASTEHPR
LGPVRNPWNTDYSAGASSGGSAALVAAGVVPIAHANDGGGSIRIPAACCGLVGLKPSRGRLPLDPELRRL
PVNIVANGVLTRTVRDTAAFYREAERYYRNPKLPPIGDVTGPGKQRLRIAVVTDSVTGREADPEVREAVL
ATARLLEELGHRVEPVDLPVPASFVDDFLLYWGFLAFALVRGGRRTFGPSFDRTRLDNLTLGLARHARRN
LHRLPLAIARLRRLRRVYARFFGTYDVVLTPTLAHTTPEIGYLDPTQDFDTVLDRLISYVAFTPLQNATG
EPAISLPLGQSSDGLPVGMMFSADVGDEATLLELAYELEEAQPWPRIQ
>gnl|CDD|169138 PRK07874, PRK07874, ATP synthase F0 subunit C
MNEIILAQEATETTFTGLGAVGYGLAAIGPGIGVGIVVGKALEGMARQPEMAGQLRTTMFLGIAFVEALA
LIGLVAGFLF
>gnl|CDD|236122 PRK07877, PRK07877, Rv1355c family protein
MNKSGEDGTAYRAVVLDEDDPADRLVLARLRADPGIEFVDRIDEQLAELRRLRPPPDPELLAEPGRWVYY
PWRRTVVHLLGPREFRAVRLDRNRNKITAEEQERLGRLRIGVVGLSVGHAIAHTLAAEGLCGELRLADFD
TLELSNLNRVPAGVFDLGVNKAVVAARRIAELDPYLPVEVFTDGLTEDNVDAFLDGLDVVVEECDSLDVK
VLLREAARARRIPVLMATSDRGLLDVERFDLEPDRPILHGLLGDIDAAKLAGLSTKDKVPHVLRILDAEA
LSARMAASLVEVDQTLSTWPQLASDVVLGAAAVAEAVRRIGLGEPLESGRVRVDLDELLDRLDDPPPPPS
GAGWEAESAPPAPPADRAAEALPQDALEIVAAAAIRAPSGGNVQPWHIEADQDRLTIRLAPEHTSAMDVG
YRGSAVAVGAALFNARVAAAAHGLLGPVEFFPGDEGSPLRATLRFGRGDDPELAALYQPMLLRETNRHHG
TPAPIDDATVEALTAAAAAEGARLHLLTDRDDIDAAAEILAAADRIRYLTPRLHEEMISELRWPGDDAPD
TGIDVRTLELDPADLAGLDILRRPDVMARLARWDGGSALGDDTRDRVSSSSALAVVTVPGATLTDYARGG
SAMEAVWIAAQQLGLAVQPVSPVFLYARNRGELEGLSPEFADELGRLQKRFRELVGIGADEAEVLLFRLS
HAPPPSVRSRRRPLREVLEISR
>gnl|CDD|181156 PRK07878, PRK07878, molybdopterin biosynthesis-like protein MoeZ; Validated
MSTSLPPLVEPAAELTRDEVARYSRHLIIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLG
IVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPSNAVELFSQYDLILDGT
DNFATRYLVNDAAVLAGKPYVWGSIYRFEGQASVFWEDAPDGLGLNYRDLYPEPPPPGMVPSCAEGGVLG
VLCASIGSIMGTEAIKLITGIGEPLLGRLMVYDALEMTYRTIKIRKDPSTPKITELIDYEAFCGVVSDEA
QQAAAGSTITPRELKEWLDSGKKIALIDVREPVEWDIVHIPGAQLIPKSEILSGEALAKLPQDRTIVLYC
KTGVRSAEALAALKKAGFSDAVHLQGGVVAWAKQVDPSLPMY
>gnl|CDD|236123 PRK07883, PRK07883, DEDD exonuclease domain-containing protein
VQLSFDDLGTPLRDVTFVVVDLETTGGSPAGDAITEIGAVKVRGGEVLGEFATLVNPGRPIPPFITVLTG
ITTAMVAGAPPIEEVLPAFLEFARGAVLVAHNAPFDIGFLRAAAARCGYPWPGPPVLCTVRLARRVLPRD
EAPNVRLSTLARLFGATTTPTHRALDDARATVDVLHGLIERLGNLGVHTLEELLTYLPRVTPAQRRKRHL
ADGLPHAPGVYLFRGPSGEVLYVGTAVNLRRRVRSYFTAAETRGRMREMVALAERVDHVECAHALEAEVR
ELRLIAAHKPPYNRRSKFPERRWWVRLTDEAFPRLSVVRAVEDDGAAYLGPFRSRRAAEEAAEALARAFP
LRQCTDRLSRRARHGPACALAELGRCPAPCDGRESAAEYAEAVARARAALTGDDDAVLAALRARIDRLAA
AERFEEAARLRDRLAALLRALARAQRLAALAAVPELVAARPDGEGGWELAVVRHGRLAAAGVAPRGVPPM
PVVDALVATAETVLPGPGPLPGASVEETELLLRWLEQPGVRLVRVDGGWASPARGAGRWAAWLARAR
>gnl|CDD|236124 PRK07889, PRK07889, enoyl-[acyl-carrier-protein] reductase FabI
MMGLLEGKRILVTGVITDSSIAFHVARVAQEQGAEVVLTGFGRALRLTERIAKRLPEPAPVLELDVTNEE
HLASLADRVREHVDGLDGVVHSIGFAPQSALGGNFLDAPWEDVATALHVSAYSLKSLAKALLPLMNEGGS
IVGLDFDATVAWPAYDWMGVAKAALESTNRYLARDLGPRGIRVNLVAAGPIRTLAAKAIPGFELLEEGWD
ERAPLGWDVKDPTPVARAVVALLSDWFPATTGEIVHVDGGAHAMGA
>gnl|CDD|181159 PRK07890, PRK07890, short chain dehydrogenase; Provisional
MLLKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCA
NLVALALERFGRVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMIN
SMVLRHSQPKYGAYKMAKGALLAASQSLATELGPQGIRVNSVAPGYIWGDPLKGYFRHQAGKYGVTVEQI
YAETAANSDLKRLPTDDEVASAVLFLASDLARAITGQTLDVNCGEYHH
>gnl|CDD|236126 PRK07899, rpsA, 30S ribosomal protein S1; Reviewed
MPSPTVTTPQVAVNDIGSAEDFLAAIDKTIKYFNDGDIVEGTVVKVDRDEVLLDIGYKTEGVIPSRELSI
KHDVDPNEVVEVGDEVEALVLQKEDKEGRLILSKKRAQYERAWGTIEKIKEKDGVVTGTVIEVVKGGLIL
DIGLRGFLPASLVEMRRVRDLQPYIGQEIEAKIIELDKNRNNVVLSRRAWLEQTQSEVRSEFLNQLQKGQ
VRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVEVGQEVTVEVLDVDMDRERVSLSLKATQ
EDPWQQFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELAERHVEVPEQVVQVGDEVFVKVID
IDLERRRISLSLKQANEGVTPESEDFDPALYGMAAEYDEQGNYIYPEGFDPETNEWLEGFEKQREEWEAQ
YAEAERRWEAHTAQVEKAAAAEAAAAAASSESSSSASSSSSEAEAGGTLASDEQLAALREKLAGNA
>gnl|CDD|181162 PRK07904, PRK07904, decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase
MLDAVGNPQTILLLGGTSEIGLAICERYLKNAPARVVLAALPDDPRRDAAVAQMKAAGASSVEVIDFDAL
DTDSHPKVIDAAFAGGDVDVAIVAFGLLGDAEELWQNQRKAVQIAEINYTAAVSVGVLLGEKMRAQGFGQ
IIAMSSVAGERVRRSNFVYGSTKAGLDGFYLGLGEALREYGVRVLVVRPGQVRTRMSAHAKEAPLTVDKE
DVAKLAVTAVAKGKELVWAPPAFRYVMMVLRHIPRPIFRKLPI
>gnl|CDD|181163 PRK07906, PRK07906, hypothetical protein; Provisional
VVDLCSELIRIDTTNTGDGTGKGEREAAEYVAEKLAEVGLEPTYLESAPGRANVVARLPGADPSRPALLV
HGHLDVVPAEAADWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEE
AGGTYGAHWLVDNHPELFEGVTEAISEVGGFSLTVPGRDRLYLIETAEKGLAWMRLTARGRAGHGSMVND
DNAVTRLAEAVARIGRHRWPLVLTPTVRAFLDGVAELTGLEFDPDDPDALLAKLGPAARMVGATLRNTAN
PTMLKAGYKVNVIPGTAEAVVDGRFLPGREEEFLATVDELLGPDVEREWVHRDPALETPFDGPLVDAMNA
ALLAEDPGARVVPYMLSGGTDAKAFSRLGIRCYGFAPLRLPPDLDFAALFHGVDERVPVDALRFGVRVLD
RFLRTC
>gnl|CDD|236127 PRK07907, PRK07907, hypothetical protein; Provisional
MTILTADDLRARVAELLPRVRADLEELVRIPSVAADPFRREEVARSAEWVADLLREAGFDDVRVVSADGA
PAVIGTRPAPPGAPTVLLYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRALG
GDLPVGVTVFVEGEEEMGSPSLERLLAEHPDLLAADVIVIADSGNWSVGVPALTTSLRGNADVVVTVRTL
EHAVHSGQFGGAAPDALTALVRLLATLHDEDGNVAVDGLDATEPWLGVDYDEERFRADAGVLDGVELIGT
GSVADRLWAKPAITVIGIDAPPVAGASNALPPSARARLSLRVAPGQDAAEAQDALVAHLEAHAPWGAHVT
VERGDAGQPFAADASGPAYDAARAAMREAWGKDPVDMGMGGSIPFIAELQEAFPQAEILVTGVEDPKTRA
HSPNESVHLGELERAAVAEALLLARLAAA
>gnl|CDD|236128 PRK07908, PRK07908, threonine-phosphate decarboxylase
VASSDTSPLAALRHHGDQDAGPGLLDFAVNVRHDTPPEWLRERLAARLGDLAAYPSTEDERRARAAVAAR
HGRTPDEVLLLAGAAEGFALLARLRPRRAAVVHPSFTEPEAALRAAGIPVHRVVLDPPFRLDPAAVPDDA
DLVVIGNPTNPTSVLHPAEQLLALRRPGRILVVDEAFADAVPGEPESLAGDDLPGVLVLRSLTKTWSLAG
LRVGYALGAPDVLARLTRGRAHWPVGTLQLEAIAACCAPRAVAEAAADAARLAADRAEMVAGLRAVGARV
VDPAAAPFVLVRVPDAELLRKRLRERGIAVRRGDTFPGLDPDYLRLAVRPRAEVPVLVQALAEILKAGG
>gnl|CDD|236129 PRK07910, PRK07910, beta-ketoacyl-ACP synthase
MMTELTTGKGFPNVVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEEFDLPVRIGGHLLEEFDH
QLTRVELRRMSYLQRMSTVLGRRVWENAGSPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPL
AVQMYMPNGPAAAVGLERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGF
AQMRIVMSTNNDDPAGACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVA
PDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNALGGHRPAVYAPKSALGHSVG
AVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSFGFGGHNVALAFGRY
>gnl|CDD|169151 PRK07912, PRK07912, salicylate synthase
SELSVATGAVSTASSSIPMPAGVDPADLAAELAAVVTESVGEDYLLYERDGQWVLAAGVQAMVELDSDEL
RVIRDGVTRRQQWSGRPGAALGEAVDRLLLETDQAFGWVAFEFGVYRYGLQQRLAPGTPLARVFSPRTRI
VVTEKGIRLFGAGIRHREAIDRLLATGVREVPQSRSVDVSDDPSGYRDRVAVAVAEIAAGRYHKVILSRC
VEVPFAVDFPATYRLGRRHNTPVRSFLLRLGGIRALGYSPELVTAVRADGVVITEPLAGTRAFGRGAAID
RLARDDLESNSKEIVEHAISVRSSLAEITEIAEPGSAAVIDFMTVRERGSVQHLGSTVRGRLDASSDRMD
ALEALFPAVTASGIPKAAGVDAIFRLDEAPRGLYSGAVVMLSADGGLDAALTLRAAYQVGGRTWLRAGAG
IIEESEPEREFEETCEKLSTLAPYLVARQ
>gnl|CDD|236130 PRK07914, PRK07914, hypothetical protein; Reviewed
MTEPAPLHLVLGDEELLVERAVAAVLRSARQRAGTADVPVSRMRAGDVSTYELAELLSPSLFAEERVVVL
EAAAEAGKDAAALILSAAADLPPGTVLVVVHSGGGRAKALANQLRKLGAEVHPCARITKAAERADFVRKE
FRSLRVKVDDDTVTALLDAVGSDLRELASACSQLVADTGGAVDAAAVRRYHSGKAEVKGFDIADKAVAGD
VAGAAEALRWAMMRGEPHVVLADALAEAVHTIARVGPLSGDPYRLAGELGMPPWRVQKAQKQARRWSRDT
VATAMRVVAALNADVKGAAADADYALESAVRRVAELVADR
>gnl|CDD|236131 PRK07920, PRK07920, lipid A biosynthesis lauroyl acyltransferase; Provisional
DLGYAAGWRLVRALPEPVARRLFDAGADVAWRRRGGGVRQLRRNLARVVPDAPAAVLDALVRAAMRSYAR
YWREAFRLPSMSRERLAARVRVSIEGLEHLDAALAAGRGVVLALPHSGNWDMAGAWLVQHHGPFTTVAER
LKPESLYERFVAYRESLGFEVLPLTGGERPPFEVLAERLRAGGVVCLLADRDLTRSGVEVDFFGERTRMP
AGPAALALETGAALLPVHLWFEGDGWGFRVHPPLDVPSAEDVAAMTQALADAFAANIAAHPEDWHMLQPL
WLADLDPARRARLRAALE
>gnl|CDD|181169 PRK07921, PRK07921, RNA polymerase sigma factor SigB; Reviewed
HMADATARATTSRVDSDLDAQSPAADLVRVYLNGIGKTALLTAADEVELAKRIEAGLYAEHLLETRKRLS
EARKRDLAAVVRDGEAARRHLLEANLRLVVSLAKRYTGRGMPLLDLIQEGNLGLIRAMEKFDYTKGFKFS
TYATWWIRQAITRGMADQSRTIRLPVHLVEQVNKLARIKRELHQQLGREATDEELAEESGIPEEKIADLL
EHSRDPVSLDMPVGSDEEAPLGDFIEDSEATSAENAVIAGLLHTDIRSVLATLDEREQQVIRLRFGLDDG
QPRTLDQIGKLFGLSRERVRQIEREVMSKLRNGERADRLRSYAS
>gnl|CDD|236132 PRK07922, PRK07922, amino-acid N-acetyltransferase
TAAGAITVRRARTSDVPAIKRLVDPYAQGRILLEKNLVTLYEAVQEFWVAEHLDGEVVGCGALHVMWEDL
AEIRTVAVDPAARGRGVGHAIVERLLDVARELGLSRVFVLTFEVEFFARHGFVEIDGTPVTPEVYAELLR
SYDEGVAEFLDLSRVKPNTLGNTRMLLHL
>gnl|CDD|181171 PRK07928, PRK07928, NADH dehydrogenase subunit A; Validated
MNVYIPILVLGALAAAFAVVSVVVASLVGPKRYNRAKLEAYECGIEPTPQPAGGGRFPVKYYLTAMLFIV
FDIEIVFLYPWAVSFDALGVFGLVEMALFMLTVFVAYAYVWRRGGLEWD
>gnl|CDD|236133 PRK07933, PRK07933, dTMP kinase
MLIAIEGVDGAGKRTLTEALRAALEARGRSVATLAFPRYGRSVHADLAAEALHGRHGDLADSVYAMATLF
ALDRAGARDELAGLLAAHDVVILDRYVASNAAYSAARLHQDADGEAVAWVAELEFGRLGLPVPDLQVLLD
VPVELAAERARRRAAQDADRARDAYERDDGLQQRTGAVYAELAAQGWGGPWLVVDPDVDPAALAARLAAA
LLP
>gnl|CDD|181173 PRK07937, PRK07937, lipid-transfer protein; Provisional
MRDVAVVGFAQAPHVRRTDGTTNGVEMLMPCFAELYAELGITKSDIGFWCSGSSDYLAGRAFSFISAIDS
IGAVPPINESHVEMDAAWALYEAWVKLLTGEVDTALVYGFGKSSAGTLRRVLALQLDPYTVAPLWPDSVS
MAGLQARAGLDAGKWTEEQMAEVAARSRADARRNPSAEPSISVDELLARPYFADPLRRHDIAPITDGAAA
VVLAAGDRARELRERPAWITGIEHRIESPSLGARDLTRSPSTALAAEAATGGDAGGVDVAELHAPFTHQE
LILREALGLGDKTKVNPSGGALAANPMFAAGLERIGEAARHIWDGSARRALAHATSGPALQQNLVAVLEG
RG
>gnl|CDD|181174 PRK07938, PRK07938, enoyl-CoA hydratase family protein
MPITSTTPEPGIAEVTVDYPPVNALPSAGWFALADAITAAGADPDTRVVVLRAEGRGFNAGVDIKELQAT
PGFTALIDANRGCFAAFRAVYECAVPVIAAVHGFCLGGGIGLVGNADVIVASDDATFGLPEVDRGALGAA
THLQRLVPQHLMRALFFTAATITAAELHHFGSVEEVVPRDQLDEAALEVARKIAAKDTRVIRAAKEALNG
IDPQDVERSYRWEQGFTFELNLAGVSDEHRDAFVEKRKA
>gnl|CDD|236134 PRK07940, PRK07940, DNA polymerase III subunit delta'; Validated
MSVWDDLVGQEAVVAELRAAARAARADVAAAGSGMTHAWLFTGPPGSGRSVAARAFAAALQCTDPDEPGC
GECRACRTVLAGTHPDVRVVAPEGLSIGVDEVRELVTIAARRPSTGRWRIVVIEDADRLTERAANALLKA
VEEPPPRTVWLLCAPSPEDVLPTIRSRCRHVALRTPSVEAVAEVLVRRDGVDPETARRAARASQGHIGRA
RRLATDEEARARRAEVLNLALRLARVSDAVAAAEELVKAAEAEAKALTAERDEAETEELRTALGAGGTGK
GPAKALRGAAGALKDLEKRQKRRATRASRDALDRALVDLAGLYRDVLVVQLGAEVGLINPDMADRLAELA
ARSTPEGLLRRIDAVLACRERLAGNVKPLLAVEAMVAALRQALR
>gnl|CDD|181176 PRK07942, PRK07942, DNA polymerase III subunit epsilon; Provisional
MSWHPGPLAAFDLETTGVDPETARIVTAALVVVDADGEVVESREWLADPGVEIPEEASAVHGITTEYARA
HGRPAAEVLAEIADALREAWARGVPVVVFNAPYDLTVLDRELRRHGLPSLVPGPVIDPYVIDKAVDRYRK
GKRTLTALCEHYGVRLDNAHEATADALAAARVAWALARRFPELAALSPAELHELQAVWYAEQAASFQAYL
RRKGRPAAVVDGAWPLRPLPDA
>gnl|CDD|236135 PRK07945, PRK07945, PHP domain-containing protein
MDPVAALRRIAFLLERARADTYRVRAFRRAADVVEALDAAERARRARAGSLTSLPGIGPKTAKVIAQALA
GRVPDYLAELRADAEPLGGGALRAALRGDLHTHSDWSDGGSPIEEMARTAAALGHEYCALTDHSPRLTVA
NGLSAERLRKQLDVVAELNEELAPFRILTGIEVDILDDGSLDQEPELLDRLDVVVASVHSKLRMDAAAMT
RRMLAAVANPHTDVLGHCTGRLVTGNRGTRPESKFDAEAVFAACREHGTAVEINSRPERRDPPTRLLRLA
LDAGCLFSIDTDAHAPGQLDWLGYGCERAEEAGVPADRIVNTWPADRLLAWTGSR
>gnl|CDD|236136 PRK07946, PRK07946, putative monovalent cation/H+ antiporter subunit C; Reviewed
MTANLGLLVAIGVLTSAGVYLLLERSLTRMLLGLLLIGNGVNLLILTAGGPAGNPPILGRTSEYGETMAD
PLAQAMILTAIVITMGITAFVLALAYRSYRLTTADEVEDDPEDTRVALRRRGLASAAPDHDRSDDPETGR
QTAEGDAFGPEEFERPLEEAKDL
>gnl|CDD|181179 PRK07948, PRK07948, putative monovalent cation/H+ antiporter subunit F; Reviewed
MTVVLTIAAVFLSLAAILTTYRILAGPNSLDRLVALDTLVAVTMCALATWAAWTLDTTVTNAMTALALIG
FIGSVSVARFRVPDGA
>gnl|CDD|181180 PRK07952, PRK07952, DNA replication protein DnaC; Validated
MKNVGDLMQRLQKMMPAHIKPAFKTGEELLAWQKEQGRIRSAALERENRAMKMQRTFNRSGIRPLHQNCS
FENYRVECEGQMNALSKARQYVEEFDGNIASFIFSGKPGTGKNHLAAAICNELLLRGKSVLIITVADIMS
AMKDTFSNSETSEEQLLNDLSNVDLLVIDEIGVQTESRYEKVIINQIVDRRSSSKRPTGMLTNSNMEEMT
KLLGERVMDRMRLGNSLWVIFNWDSYRSRVTGKE
>gnl|CDD|236137 PRK07956, ligA, NAD-dependent DNA ligase LigA; Validated
TMEEAKKRIEELREELNHHAYAYYVLDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDG
FEKVRHLVPMLSLDNAFSEEELRAFDKRVRKRLPDPPLTYLCELKIDGLAVSLLYENGVLVRAATRGDGT
TGEDITANVRTIRSIPLRLHGNEPERLEVRGEVFMPKADFEALNEERREEGEKPFANPRNAAAGSLRQLD
PKITAKRPLSFFAYGVGEVEGGELPDSQSEALEFLKAWGFPVNPYRKLCTSIEEVLAFYEEIEEERHDLP
YDIDGVVIKVDDLALQEELGFTAKAPRWAIAYKFPAEEATTKLLDIEVQVGRTGAVTPVARLEPVEVAGV
TVSRATLHNADEIERKDIRIGDTVVVRRAGDVIPEVVGVVLEKRPGDEREIVMPTHCPVCGSELVRVEGE
AVLRCTNGLSCPAQLKERLIHFVSRNAMDIDGLGEKIIEQLFEKGLIHDPADLFKLTAEDLLGLEGFGEK
SAQNLLDAIEKSKETSLARFLYALGIRHVGEKAAKALARHFGSLEALRAASEEELAAVEGVGEVVAQSIV
EFFAVEENRELIDELLEAGVNMEYKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTD
LVVAGEAAGSKLAKAQELGIEVLDEEEFLRLLGEG
>gnl|CDD|181182 PRK07960, fliI, flagellum-specific ATP synthase FliI
MTTRLTRWLTTLDNFEAKMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGSETHEVESEVV
GFNGQRLFLMPLEEVEGILPGARVYARNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETG
ALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIG
ERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMA
QREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGH
IVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQRNRDLVSVGAYAKGSDPMLDK
AIALWPQLEAFLQQGIFERADWEDSLQALERIFPT
>gnl|CDD|181183 PRK07963, fliN, flagellar motor switch protein FliN; Validated
MSDMNNPSDDNNGAMDDLWAEALNEQKATSSKSAADAVFQQLGGGDVSGTLQDIDLIMDIPVKLTVELGR
TRMTIKELLRLTQGSVVALDGLAGEPLDILINGYLIAQGEVVVVADKYGVRITDIITPSERMRRLSR
>gnl|CDD|181184 PRK07967, PRK07967, beta-ketoacyl-ACP synthase I
MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVKLDPTGLIDRKVMRFMGD
ASAYAYLAMEQAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMAST
VSACLATPFKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKY
NDTPEKASRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCM
QMALATVDTPIDYINTHGTSTPVGDVKELGAIREVFGDKSPAISATKSLTGHSLGAAGVQEAIYSLLMME
HGFIAPSANIEELDPQAAGMPIVTETTDNAELTTVMSNSFGFGGTNATLVFRRYKG
>gnl|CDD|181185 PRK07979, PRK07979, acetolactate synthase 3 large subunit
MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGV
VLVTSGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQ
VLKKAFWLAASGRPGPVVVDLPKDILNPANKLPYVWPESVSMRSYNPTTQGHKGQIKRALQTLVAAKKPV
VYVGGGAINAACHQQLKELVEKLNLPVVSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVG
VRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGDARQVLEQMLELLSQESAHQPLDEIRDW
WQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGL
GTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQWQDMIYS
GRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALEQVRNNRLVFVDVTVDGSEHVYPMQIRG
GGMDEMWLSKTERT
>gnl|CDD|181186 PRK07983, PRK07983, exodeoxyribonuclease X; Provisional
MLRVIDTETCGLQGGIVEIASVDVIDGKIVNPMSHLVRPDRPISPQAMAIHRITEAMVADKPWIEDVIPH
YYGSEWYVAHNASFDRRVLPEMPGEWICTMKLARRLWPGIKYSNMALYKSRKLNVQTPPGLHHHRALYDC
YITAALLIDIMNTSGWTAEEMADITGRPSLLTTFTFGKYRGKAVSDVAERDPGYLRWLFNNLDDMSPELR
LTLKHYLEN
>gnl|CDD|181187 PRK07984, PRK07984, enoyl-ACP reductase FabI
MGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVLPCDVAEDAS
IDAMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSA
LLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHC
EAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMNELELK
>gnl|CDD|181188 PRK07985, PRK07985, SDR family oxidoreductase
MSHLKDPTTQYYTGEYPKQKQPTPGIQAKMTPVPDCGEKTYVGSGRLKDRKALVTGGDSGIGRAAAIAYA
REGADVAISYLPVEEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKALGGLDIMALVAGKQV
AIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKGASIITTSSIQAYQPSPHLLDYAATKAAILNYS
RGLAKQVAEKGIRVNIVAPGPIWTALQISGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQESSYV
TAEVHGVCGGEHLG
>gnl|CDD|181189 PRK07986, PRK07986, adenosylmethionine--8-amino-7-oxononanoate transaminase; Validated
MTTDDLAFDQRHIWHPYTSMTSPLPVYPVVSAEGCELILADGRRLVDGMSSWWAAIHGYNHPQLNAAMKS
QIDAMSHVMFGGITHPPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAMKMALQYWQAKGEPRQRFLTL
RHGYHGDTFGAMSVCDPDNSMHSLYKGYLPENLFAPAPQSRFDGEWDERDIAPFARLMAAHRHEIAAVIL
EPIVQGAGGMRIYHPEWLKRVRKLCDREGILLIADEIATGFGRTGKLFACEHAGIAPDILCLGKALTGGT
MTLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAVANASLSLLESGDWQQQVAAIEAQLREELAPL
RDAPMVADVRVLGAIGVVETTRPVNMAALQRFFVEQGVWIRPFGKLIYLMPPYIILPEQLQRLTAAVNRA
VQDETFFC
>gnl|CDD|181190 PRK07993, PRK07993, DNA polymerase III subunit delta'; Validated
MKWYPWLRPDYEQLVGSYQAGRGHHALLIQALPGMGDDALIYALSRWLMCQQPQGHKSCGHCRGCQLMQA
GTHPDYYTLTPEKGKSSLGVDAVREVTEKLYEHARLGGAKVVWLPDAALLTDAAANALLKTLEEPPENTW
FFLACREPARLLATLRSRCRLHYLAPPPEQYALTWLSREVTMSQDALLAALRLSAGAPGAALALLQPERW
QQREALCQALAYALPSGDWLSLLPALNHEQAPARLHWLATLLMDALKRQHGAAYVTNQDQPPLVAQLANH
LSPARLQAILGDVCHCREQLLSVTGVNRELLLTDLLLRIEHYLQPGTVLPVPHL
>gnl|CDD|236138 PRK07994, PRK07994, DNA polymerase III subunits gamma and tau; Validated
MSYQVLARKWRPQTFAEVVGQEHVLTALANALDLGRLHHAYLFSGTRGVGKTTIARLLAKGLNCETGITA
TPCGECDNCREIEQGRFVDLIEIDAASRTKVEDTRELLDNVQYAPARGRFKVYLIDEVHMLSRHSFNALL
KTLEEPPEHVKFLLATTDPQKLPVTILSRCLQFHLKALDVEQIRQQLEHILQAEQIPFEPRALQLLARAA
DGSMRDALSLTDQAIASGNGQVTTDDVSAMLGTLDDDQALSLLEALVEGDGERVMALINQLAERGPDWEG
LLVELLELLHRIAMAQLLPAALDNDMADIELRLRELARTLPPEDVQLYYQTLLIGRKDLPLAPDRRMGVE
MTLLRMLAFHPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTS
QLLAARQQLQRAQGATKAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVK
KEPVATPKALKKALEHEKTPELAAKLAAEAIERDPWAALVSQLGLPGLVEQLALNAWKEEHDNGEVCLHL
RPSQRHLNSPRAQQRLAEALSELLGRTVELTIEEDDNPAVETPLEWRQRIYEEKLAQAEESIIADPNIQT
LRQFFDAELDEDSIRPI
>gnl|CDD|181192 PRK07998, gatY, class II aldolase
MPLVNGRILLDRIQEKHVLAGAFNTTNLETTISILNAIERSGLPNFIQIAPTNAQLSGYDYIYEIVKRHA
DKMDVPVSLHLDHGKTFEDVKQAVRAGFTSVMIDGAALPFEENIAFTKEAVDFAKSYGVPVEAELGAILG
KEDDHVSEADCKTEPEKVKDFVERTGCDMLAVSIGNVHGLEDIPRIDIPLLKRIAEVSPVPLVIHGGSGI
PPEILRSFVNYKVAKVNIASDLRKAFITTVGKAYVNNHNEANLARVMAKAKQAVEEDVYSKIKMMNSNHR
LVR
>gnl|CDD|169179 PRK08005, PRK08005, ribulose-phosphate 3 epimerase family protein
MILHPSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSP
QRWLPWLAAIRPGWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPD
GRGQQFIAAMCEKVSQSREHFPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTLSQFTAL
>gnl|CDD|181193 PRK08006, PRK08006, replicative DNA helicase DnaB
MAGNKPFNKQQAEPRERDPQVAGLKVPPHSIEAEQSVLGGLMLDNERWDDVAERVVADDFYTRPHRHIFT
EMARLQESGSPIDLITLAESLERQGQLDSVGGFAYLAELSKNTPSAANISAYADIVRERAVVREMISVAN
EIADAGYDPQGRTSEDLLDLAESRVFQIAESRANKDEGPKNIADILDATVARIEQLFQQPHDGVTGVNTG
YDDLNKKTAGLQPSDLIIVAARPSMGKTTFAMNLCENAAMLQDKPVLIFSLEMPGEQIMMRMLASLSRVD
QTRIRTGQLDDEDWARISGTMGILLEKRNMYIDDSSGLTPTEVRSRARRIFREHGGLSLIMIDYLQLMRV
PSLSDNRTLEIAEISRSLKALAKELQVPVVALSQLNRSLEQRADKRPVNSDLRESGSIEQDADLIMFIYR
DEVYHENSDLKGIAEIIIGKQRNGPIGTVRLTFNGQWSRFDNYAGPQYDDE
>gnl|CDD|181194 PRK08007, PRK08007, aminodeoxychorismate synthase component 2
MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYA
GRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPAC
FEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFLHR
>gnl|CDD|181195 PRK08008, caiC, putative crotonobetaine/carnitine-CoA ligase; Validated
MDIVGGQHLRQMWDDLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLD
NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLT
RVALPADDGVSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCA
LRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQP
PSANDRQHCLREVMFYLNLSDQEKDAFEERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRPGFCYE
AEIRDDHNRPLPAGEIGEICIKGVPGKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRR
CNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAK
FKVPSYLEIRKDLPRNCSGKIIKKNLK
>gnl|CDD|181196 PRK08010, PRK08010, pyridine nucleotide-disulfide oxidoreductase; Provisional
MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMYGGTCINIGCIPTKTLVHDAQQHTDFVRAIQR
KNEVVNFLRNKNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEGNLEIHGEKIFINTGAQTVVPPIPGIT
TTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILR
DQGVDIILNAHVERISHHENQVQVHSEHAQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYL
HTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARE
SGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILR
DQIFTHPSMSESLNDLFSLVK
>gnl|CDD|236139 PRK08013, PRK08013, oxidoreductase; Provisional
MQSVDVVIAGGGMVGLAVACGLQGSGLRVAVLEQRVPEPLAADAPPALRVSAINAASEKLLTRLGVWQDI
LARRASCYHGMEVWDKDSFGRIAFDDQSMGYSHLGHIIENSVIHYALWQKAQQSSDITLLAPAELQQVAW
GENEAFLTLKDGSMLTARLVVGADGANSWLRNKADIPLTFWDYQHHALVATIRTEEPHDAVARQVFHGDG
ILAFLPLSDPHLCSIVWSLSPEEAQRMQQAPEEEFNRALAIAFDNRLGLCELESERQVFPLTGRYARQFA
AHRLALVGDAAHTIHPLAGQGVNLGFMDAAELIAELRRLHRQGKDIGQHLYLRRYERSRKHSAALMLAGM
QGFRDLFAGNNPAKKLLRDIGLKLADTLPGVKPQLIRQAMGLNDLPEWLR
>gnl|CDD|181198 PRK08017, PRK08017, SDR family oxidoreductase
MQKSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMNSLGFTGILLDLDDPESVERAADEVIAL
TDNRLYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLIST
PGRGAYAASKYALEAWSDALRMELRHSGIKVSLIEPGPIRTRFTDNVNQTQSDKPVENPGIAARFTLGPE
AVVPKLRHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKILRG
>gnl|CDD|181199 PRK08020, ubiF, 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
MTNQPTDIAIVGGGMVGAALALGLAQHGFSVAVLEHAAPAPFDADSQPDVRISAISAASVALLKGLGVWD
AVQAMRSHPYRRLETWEWETAHVVFDAAELKLPELGYMVENRVLQLALWQALEAHPNVTLRCPASLQALQ
RDDDGWELTLADGEEIQAKLVIGADGANSQVRQMAGIGVHGWQYRQSCMLISVKCENPPGDSTWQQFTPS
GPRAFLPLFDNWASLVWYDSPARIRQLQAMSMAQLQQEIAAHFPARLGAVTPVAAGAFPLTRRHALQYVQ
PGLALVGDAAHTINPLAGQGVNLGYRDVDALLDVLVNARSYGEAWASEAVLKRYQRRRMADNLLMQSGMD
LFYAGFSNNLPPLRFARNLGLMAAQRAGVLKRQALKYALGL
>gnl|CDD|181200 PRK08025, PRK08025, kdo(2)-lipid IV(A) palmitoleoyltransferase
MFPQQKFSREFLHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQM
SAEEREKMIAENFRSLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGG
RVMGLCQPMMATYRPHNNKLMEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGPKGSSF
APFFAVENVATTNGTYVLSRLSGAAMLTVTMVRKADYSGYRLFITPEMEGYPTDENQAAAYMNKIIEKEI
MRAPEQYLWIHRRFKTRPVGESSLY
>gnl|CDD|236140 PRK08026, PRK08026, FliC/FljB family flagellin
MAQVINTNSLSLITQNNINKNQSALSSSIERLSSGLRINSAKDDAAGQAIANRFTSNIKGLTQAARNAND
GISVAQTTEGALSEINNNLQRVRELTVQAATGTNSQSDLDSIQDEIKSRLDEIDRVSGQTQFNGVNVLAK
DGSMKIQVGANDGETITIDLKKIDSDTLGLDGFNVNGKGTVANTAATVSDLTAAGATLDTTGLYDVKTKN
AALTTADALAKLGDGDKVTATATGGDYTYNAKSGKYQAADLAATLTPDVGGTAGASYTIKDGTYEVNVDS
DGKITLGGSALYIDATGNLTTNNAGAATKATLDALKKTASEGAATAKAALAAAGVTVADGVTAKTVKMSY
TDKNGKVIDGGYAVKTGDDYYAADYDEITGAISATTTYYTAKDGTTKTAANKLGGADGKTEVVTIDGKTY
VASDGKQTTLAEAAATTTENPLAALDAAIASIDKFRSSLGAVQNRLDSAVTNLNNTTTNLSEAQSRIQDA
DYATEVSNMSKAQIIQQAGNSVLAKANQVPQQVLSLLQG
>gnl|CDD|181202 PRK08027, flgL, flagellar hook-filament junction protein FlgL
MRLSTQMMYQQNMRGITNSQAEWMKYGEQMSTGKRVVNPSDDPIAASQAVVLSQAQAQNSQYTLARTFAT
QKVSLEESVLSQVTTAIQNAQEKIVYAGNGTLSDDDRASLATDLQGLRDQLLNLANTTDGNGRYIFAGYK
TDKAPFDEATGGYVGGTESITQQVDAARSMVIGHTGDQIFDSITSNAVPEPDGSASETNLFAMLDSAIAA
LKTPVAGSDADKETAAAALDKTNRGLKNSLNNVLTVRAELGTQLNELESLDSLGSDRALGQKQQMSDLVD
VDWNSAISSYVMQQAALQASYKAFTDMQGMSLFQLNR
>gnl|CDD|236141 PRK08032, fliD, flagellar capping protein; Reviewed
MASISSLGVGSGLDLDSLLDSLTAAEKKRLTPITNQQSSYTAKLTAYGTLKSALEKFQTANTALNKADLF
SSTKVSSSTTAFSATTDSGASAGKYTISVTQLAQAQSLTTATVSSTKEALGTSDSTRTITITQPGRKEPL
EIDLTAGQTSLSGIRDAINKAEGGVSASIIKVGDGEYRLVLTSKDTGTDNAMTISVEGDSKLNDFLNYDS
STGSGNMTQSVAAQNAKLTVNGIAIERQSNTITDAPEGITLNLKKVTTGNQTLTITKDTTKAKEAIKDWV
DAYNSLQDTFSSLTKYTAVDAGADQSSSNGALLGDSTLRTIQTQLKSQLANSQSSSDFKTLAQIGITQDP
SDGKLEIDDDKLTKALKEDPAGVKALFVGDGKKTGITTQIATNLKSWLSTTGIIKTATDGVNKTLKKLTK
QYNAVSDSIDATIARYKAQFTQLDKLMTSLNSTSSYLTQQFE
>gnl|CDD|181204 PRK08035, PRK08035, YscQ/HrcQ family type III secretion apparatus protein
MLRIANEERPWVETLPTQGATIGEVTLSMQEYPVQGEGVYFTLHYHGELCGLWLSEQCWQRWCEGLIGTA
NPSLIAPELLYGIAEWGLTPLLQAFDATLCQNESPTSCSSLPKQLAVTIKWEVEEQEFHGVLFTWPTAFL
RNTLGEWSAERQQIYPALPWVVGLVAGWCHLTLIQLEQIEPGMGLRLHCAGELRLGFCWLWLPGGIQAYI
LLTEGNTMTIDELNQDIDTLLASGSPMSKSPGTSSVELEQLPQQVVMEIGRLSLPIGQLRQLAVGDVLPV
GGCFYPEVTIRLNGRIIGQGELLACDNELMVRITRWYLQKNTA
>gnl|CDD|181205 PRK08040, PRK08040, putative semialdehyde dehydrogenase; Provisional
MSEGWNIALLGATGAVGEALLELLAERQFPVGELYALASEESAGETLRFGGKSVTVQDAAEFDWSQAQLA
FFVAGREASAAYAEEATNAGCLVIDSSGLFALEPDVPLVVPEVNPFVLADYRNRNIIAVADSLTSQLLTA
IKPLIDQAGLSRLHVTNLLSASAHGKAAVDALAGQSAKLLNGIPIEEGFFGRQLAFNMLPLLPDSEGSVR
EERRLVDQVRKILQDEGLPISVSCVQSPVFYGHAQMVHFEALRPLAAEEARDALEQGEDIVLSEENDYPT
QVGDASGNPHLSIGCVRNDYGMPEQLQFWSVADNVRFGGALMAVKTAEKLVQEYLY
>gnl|CDD|181206 PRK08042, PRK08042, formate hydrogenlyase subunit 3; Reviewed
AAAVLAFLFSFQKALSGWIAGIGGAVGSLYTAAAGFTVLTGAVGVSGALSLVSYDVQISPLNAIWLITLG
LCGLFVSLFNIDWHRHAQVKANGLLINLLMAAAVCAVIASNLGMFVVMAEIMALCAVFLTGNSKEGKLWF
ALGRLGTLLLAIACWLLWQRYGTLDLRLLDMRMQQLPLGSDIWLLGVIGFGLLAGIIPLHGWVPQAHANA
SAPAAALFSTVVMKIGLLGILTLSLLGGNAPLWWGVALLVLGMITAFVGGLYALMEHNIQRLLAYHTLEN
IGIILLGLGAGVTGIALEQPALIALGLVGGLYHLLNHSLFKSVLFLGAGSVWFRTGHRDIEKLGGIGKKM
PVISIAMLVGLMAMAALPPLNGFAGEWVIYQSFFKLSNSGAFVARLLGPLLAVGLAITGALAVMCMAKVY
GVTFLGAPRTKEAENATCAPLLMSVSVVALAICCVIGGVAAPWLLPMLSAAVPLPLEPANTTVSQPMITL
LLIACPLLPFIIMAIFKGDRLPSRSRGAAWVCGYDHEKSMVITAHGFAMPVKEAFAPVLKLRKWLNPVSL
VPGWQCAGSALLFRRLALVELAVLVVIVVSRGA
>gnl|CDD|181207 PRK08043, PRK08043, bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase
MLFSFFRNLFRVLYRVRVTGDTQALKGERVLITPNHVSFLDGILLALFLPVRPVFAVYTSISQQWYMRWL
KPYIDFVPLDPTKPMAIKHLVRLVEQGRPVVIFPEGRITVTGSLMKIYDGAGFVAAKSGATVIPVRIEGA
ELTHFSRLKGLVKRRLFPQITLHILPPTQLPMPDAPRARDRRKLAGEMLHQIMMEARMAVRPRETLYEAL
LSAQYRYGAGKPCIEDVNFTPDSYRKLLKKTLFVGRILEKYSVEGERIGLMLPNATISAAVIFGASLRRR
IPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKDDVTTADKLWIFA
HLLMPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFG
LTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFARLRYVVAGAEK
LQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEQGGRLQLKG
PNIMNGYLRVEKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE
QLALGVSPDKQHATAIKSDASKGEALVLFTTDSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSG
KPDFVTLKSMVDEPEQHD
>gnl|CDD|169193 PRK08044, PRK08044, allantoinase AllB
MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHW
EGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEV
GVVGFKCFVATCGDRGIDNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHD
YVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEE
IGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAV
QKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGA
RITKTILRGDVIYDIEQGFPVAPKGQFIL
>gnl|CDD|169194 PRK08045, PRK08045, cystathionine gamma-synthase; Provisional
MTRKQATIAVRSGLNDDEQYGCVVPPIHLSSTYNFTGFNEPRAHDYSRRGNPTRDVVQRALAELEGGAGA
VLTNTGMSAIHLVTTVFLKPGDLLVAPHDCYGGSYRLFDSLAKRGCYRVLFVDQGDEQALRAALAEKPKL
VLVESPSNPLLRVVDIAKICHLAREAGAVSVVDNTFLSPALQNPLALGADLVLHSCTKYLNGHSDVVAGV
VIAKDPDVVTELAWWANNIGVTGGAFDSYLLLRGLRTLVPRMELAQRNAQAIVKYLQTQPLVKKLYHPSL
PENQGHEIAARQQKGFGAMLSFELDGDEQTLRRFLGGLSLFTLAESLGGVESLISHAATMTHAGMAPEAR
AAAGISETLLRISTGIEDGEDLIADLENGFRAANKG
>gnl|CDD|181208 PRK08049, PRK08049, F0F1 ATP synthase subunit I; Validated
MSVSLYSGKVARKLLLLQLLTFVASGALFSLKDPFWGVSALAGGLAAWLPNVLFMIFAWRHQAHTPAKGR
VAWSFAFGEALKVLATIALLVVALGVFKAVFLPLGLTWLSVLVVQILAPAVINN
>gnl|CDD|236142 PRK08051, fre, FMN reductase; Validated
TTLSCKVTSVEAITDTVYRVRLVPEAPFSFRAGQYLMVVMGEKDKRPFSIASTPREKGFIELHIGASELN
LYAMAVMERILKDGEIEVDIPHGDAWLREESERPLLLIAGGTGFSYARSILLTALAQGPNRPITLYWGGR
EEDHLYDLDELEALALKHPNLHFVPVVEQPEEGWQGKTGTVLTAVMQDFGSLAEYDIYIAGRFEMAKIAR
ELFCRERGAREEHLFGDAFAFI
>gnl|CDD|236143 PRK08055, PRK08055, chorismate mutase; Provisional
IRHITIFLCSLLMCSSAFALAVTAVSLGALATLINERLSYMKDVAGYKAEHHLPIEDLTQEQKVLAEAEE
EAASNGLDPESIKPFIVAQMDAAKAIQYRYRADWLSQPEPSWPPQDLSDVRQRIRQLDTQILIQIAQRLK
VCGPFSHGDMAWFRSTINQPNLSEADKSAIFAALSQVRLKR
>gnl|CDD|236144 PRK08057, PRK08057, cobalt-precorrin-6x reductase; Reviewed
MMPRILLLGGTSEARALARALAAAGVDIVLSLAGRTGGPADLPGPVRVGGFGGAEGLAAYLREEGIDLVI
DATHPYAAQISANAAAACRALGIPYLRLERPSWLPQPGDRWIEVDDIEEAAEALAPFRRVLLTTGRQPLA
HFAAILPEHRLLVRVLPPPEVLLGLPRAEIIALRGPFSLELERALLRQHRIDVVVTKNSGGAGTEAKLEA
ARELGIPVVMIARPALPYADREFEDVAELVAWLRHLLA
>gnl|CDD|181214 PRK08058, PRK08058, DNA polymerase III subunit delta'; Validated
MMTWEQLTALQPVVVKMLQNSIAKNRLSHAYLFEGAKGTGKKATALWLAKSLFCLERNGVEPCGTCTNCK
RIDSGNHPDVHLVAPDGQSIKKDQIRYLKEEFSKSGVESNKKVYIIEHADKMTASAANSLLKFLEEPSGG
TTAILLTENKHQILPTILSRCQVVEFRPLPPESLIQRLQEEGISESLATLLAGLTNSVEEALALSEDDWF
AQARALVIKLYEALHEKDLQSFVFVQEKWMPLFKEKDQQQLGLDLLLLIYRDLLYLQLGEEDRLVFREQK
EMLQQLALSYSQQQIVAALELILEAKRRLNSNVNFQLVMEQLVLRLQEG
>gnl|CDD|181215 PRK08059, PRK08059, general stress protein 13; Validated
MMSQYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVDEEKG
KISLSIRATEEAPEAKRKKGKILIPNPSEQGFNTLRDKLEEWIEQSNKTDLIK
>gnl|CDD|181216 PRK08061, rpsN, type Z 30S ribosomal protein S14
MAKKSLIAKAKRKPKFKVRAYTRCERCGRPHSVYRKFGLCRICFRELAYKGQIPGVKKASW
>gnl|CDD|236145 PRK08063, PRK08063, enoyl-[acyl-carrier-protein] reductase FabL
VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIEALGRKALAVKANVGDVEKIK
EMFAQIDEEFGRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLS
SLGSIRYLENYTTVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPNREELLEDARAKTP
AGRMVEPEDVANAVLFLCSPEADMIRGQTIIVDGGRSLLV
>gnl|CDD|236146 PRK08064, PRK08064, cystathionine beta-lyase MetC
MAMSYSIDTLLLHNQYKHDKQTGAVNVPIYHASTFHQFDFDTFGKYDYSRSGNPTREALEDIIAELEGGT
KGFAFASGMAAISTAFLLLSKGDHVLISEDVYGGTYRMITEVLSRFGIEHTFVDMTNLEEVAQNIKPNTK
LFYVETPSNPLLKVTDIRGVVKLAKAIGCLTFVDNTFLTPLLQKPLDLGADVVLHSATKFLAGHSDVLAG
LAVVKDEELAQKLYFLQNSFGAVLGVQDCWLVLRGLKTLHVRLEHSSETANKIALYLQEHPKVQNVYYPG
LQTHLGFDIQQSQATSAGAVLSFTLQSEEAVRQFVSHVKLPVFAVSLGAVESILSYPAKMSHAAMPKEER
DERGITDGLLRLSVGLENVDDLIADFEQALSYVEEPVNAK
>gnl|CDD|181219 PRK08068, PRK08068, transaminase; Reviewed
MEFEPSELLKQLPKQFFASLVAKVNKKVAEGHDVINLGQGNPDQPTPEHIVEALQEAAENPANHKYSPFR
GYPFLKEAAADFYKREYGVTLDPETEVAILFGGKAGLVELPQCLMNPGDTILVPDPGYPDYLSGVALARA
QFETMPLIAENNFLPDYTKIPEEVAEKAKLMYLNYPNNPTGAVATKAFFEETVAFAKKHNIGVVHDFAYG
AIGFDGQKPVSFLQTPGAKDVGIELYTLSKTFNMAGWRVAFAVGNESVIEAINLLQDHLFVSLFGAIQDA
AIEALLSDQSCVAELVARYESRRNAFISACREIGWEVDAPKGSFFAWMPVPKGYTSEQFADLLLEKAHVA
VAPGNGFGEHGEGYVRVGLLTDEERLREAVERIGKLNLF
>gnl|CDD|236147 PRK08071, PRK08071, L-aspartate oxidase; Provisional
MPSADVIIIGSGIAALTVAKELCHEYNVIIITKKTKRNSNSHLAQGGIAAAVATYDSPNDHFEDTLVAGC
HHNNERAVRYLVEEGPKEIQELIENGMPFDGDETGPLHLGKEGAHRKRRILHAGGDATGKNLLEHLLQEL
VPHVTVVEQEMVIDLIIENGRCIGVLTKDSEGKLKRYYADYVVLASGGCGGLYAFTSNDKTITGDGLAMA
YRAGAELVDLEFIQFHPTMLYANGRCVGLVSEAVRGEGAVLINEDGRRFMMGIHPLADLAPRDVVARAIH
EELLSGEKVYLNISSIQNFEERFPTISALCEKNGVDIETKRIPVVPGAHFLMGGVKTNLDGETSIPGLYA
IGEVACTGVHGANRLASNSLLEGLVFGKRAAEHILTKATKPRLNPFAEKEKKFIVLNHLPTKEEIQEKMM
KYVGIVRTEQSLSEAKRWLEKYGVRNMILDHDALTNEEIELSHMLTVAKLIVVSALQRTESRGGHYRSDY
PHRNWRGKEIVRTKRKLQIV
>gnl|CDD|181222 PRK08073, flgL, flagellar hook-associated protein 3
MRVSTFQNANWAKNQLMDLNVQQQYHRNQVTSGKKNLSMSEDPLAASKSFAIQHSLANIEQMQKDVADSK
NVLNQTENTLSGMSKSLTRVDQLVLQALNGTNDEKELKAIGAEIDQILKQVVYLANTKEQGRYVFGGDSA
EKKPFTEDGTYQGGTEDVNWRLNDGYEVKAFRNGEALLTPVINTLKKMVDAMQTGDQKALQPLLEENKKN
LDIIINRTTEVGGTMNTVETFKTILSEQNLALQENRKEIEDVDLAVAISDLAYINATYEATLKAVSTMSK
TSILDYM
>gnl|CDD|236148 PRK08074, PRK08074, bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
MSKRFVVVDLETTGNSPKKGDKIIQIAAVVVEDGEILERFSSFVNPERPIPPFITELTGISEEMVKQAPL
FEDVAPEIVELLEGAYFVAHNVHFDLNFLNEELERAGYTEIHCPKLDTVELARILLPTAESYKLRDLSEE
LGLEHDQPHRADSDAEVTAELFLQLLNKLERLPLVTLQQLRRLSDHLKSDIAELLDENILKKMMHGKPLD
EEFDEYRGIALRKREVEKNLEETCRSDFDAFLEKTEEKLSLAMPKYEKREGQQEMMKEVYTALRDSEHAL
IEAGTGTGKSLAYLLPAAYFAKKKEEPVVISTYTIQLQQQLLEKDIPLLQKIFPFPVEAALLKGRSHYLC
LRKFEQALQEEDDNYDVALTKAQLLVWLTETETGDLDELNLPSGGKLLWNRIASDGESDGGKQSPWFSRC
FYQRAKNRAKFADLVITNHALLLTDLTSEEPLLPSYEHIIIDEAHHFEEAASRHLGEQFSYMSFQLLLSR
LGTLEEDGLLSKLAKLFKKSDQASRSSFRDLDESLKELKFEADELFQMLRSFVLKRKKQEQNGRLIYRYN
TESEKGKLWDAITELANRLCYDLRDLLTLLEAQKKELQEKMESESAFLTGEYAHLIDLLEKMAQLLQLLF
EEDPDYVTWIEIDAKGAINATRLYAQPVEVAERLADEFFAKKKSVILTSATLTVNGSFDYIIERLGLEDF
YPRTLQIPSPFSYEEQAKLMIPTDMPPIKDVPIEEYIEEVAAYIAKIAKATKGRMLVLFTSYEMLKKTYY
NLKNEEELEGYVLLAQGVSSGSRARLTKQFQQFDKAILLGTSSFWEGIDIPGDELSCLVIVRLPFAPPDQ
PVMEAKSEWAKEQGENPFQELSLPQAVLRFKQGFGRLIRTETDRGTVFVLDRRLTTTSYGKYFLESLPTV
PVYEGTLEELLEEVEEFL
>gnl|CDD|181224 PRK08084, PRK08084, DnaA inactivator Hda
VSLNTPAQLSLPLYLPDDETFASFYPGDNDSLLAALQNALRQEHSGYIYLWSREGAGRSHLLHAACAELS
QRGRAVGYVPLDKRAWFVPEVLEGMEQLSLVCIDNIECIAGDELWEMAIFDLYNRILESGRTRLLITGDR
PPRQLNLGLPDLASRLDWGQIYKLQPLSDEEKLQALQLRARLRGFELPEDVGRFLLKRLDREMRTLFMTL
DQLDRASITAQRKLTIPFVKEILKL
>gnl|CDD|181225 PRK08085, PRK08085, gluconate 5-dehydrogenase; Provisional
MNDLFSLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHK
QEVEAAIEHIEKDIGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKI
INICSMQSELGRDTITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEDEAFTAWLC
KRTPAARWGDPQELIGAAVFLSSKASDFVNGHLLFVDGGMLVAV
>gnl|CDD|181226 PRK08087, PRK08087, L-fuculose-phosphate aldolase
MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEGKLP
SSEWRFHMAAYQTRPDANAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHV
ALALKNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQLYLKTLAITDPVPVLSDEEIAVVLEKFKTYG
LRIEE
>gnl|CDD|236149 PRK08088, PRK08088, 4-aminobutyrate--2-oxoglutarate transaminase
MNTNKSLMQRRSAAVPRGVGQIHPIFADRAENCRVWDVEGREYLDFAGGIAVLNTGHLHPKVVAAVEAQL
KKLSHTCFQVLAYEPYLELCEKMNQKVPGDFAKKTLLVTTGSEAVENAVKIARAATKRSGVIAFTGAYHG
RTHYTLALTGKVNPYSAGMGLMPGHVYRALYPCPLHGVSEDDAIASIERIFKNDAAPEDIAAIIIEPVQG
EGGFYAASPAFMQRLRALCDEHGIMLIADEVQTGAGRTGTLFAMEQMGVAADLTTFAKSIAGGFPLAGVT
GRAEVMDAIAPGGLGGTYAGNPIACAAALAVLKVFEQENLLQKANALGEKLKDGLLAIAEKHPEIGDVRG
LGAMIAIELFEDGDHSKPNAKLTAQIVARARDKGLILLSCGPYYNVLRILVPLTIEDAQIRQGLEIIAQC
FDEAK
>gnl|CDD|169215 PRK08091, PRK08091, ribulose-phosphate 3-epimerase; Validated
MSKLSLIQQLKQQPISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIKQFPTHCF
KDVHLMVRDQFEVAKACVAAGADIVTLQVEQTHDLALTIEWLAKQKTTVLIGLCLCPETPISLLEPYLDQ
IDLIQILTLDPRTGTKAPSDLILDRVIQVENRLGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSAL
FSQGELKTTLKEWKSSLM
>gnl|CDD|236150 PRK08097, ligB, NAD-dependent DNA ligase LigB
MKLWMALLISLLLWSSSAWAVCPDWSPARAQEEIAALQQQLAQWDDAYWRQGKSEVDDEVYDQLRARLTQ
WQRCFGGPEPRDVPLPPLNGKVLHPVAHTGVKKLADKQALARWMAGRSDLWVQPKVDGVAVTLVYRDGKL
VQAISRGNGLKGEDWTAKARLIPAIPQQLPGALANLVLQGELFLRREGHIQQQMGGINARAKVAGLMMRK
DPSPTLNQIGVFVWAWPDGPASMPERLAQLATAGFPLTQRYTHPVKNAEEVARWRERWYRAPLPFVTDGV
VVRQAKEPPGRYWQPGQGEWAVAWKYPPVQQVAEVRAVQFAVGRTGKITVVLELEPVMLDDKRVSRVNIG
SVRRWQQWDIAPGDQVLVSLAGQGIPRLDKVVWRGAERTKPTPPDADRFHSLSCFRASPGCQEQFLARLV
WLSGKQGLGLDGIGEGTWRALHQTGLFEHLFSWLALTPEQLANTPGIGKARAEQLWHQFNLARQQPFSRW
LKALGIPLPQAALNALDDRSWQQLLSRSEQQWQQLPGIGEGRARQLIAFLQHPEVKALADWLAAQGITGF
EP
>gnl|CDD|236151 PRK08099, PRK08099, multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR
QQGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGLEFPRQMKKIGVVFGKFYPLHTGHIY
LIQRACSQVDELHIIICYDDERDRKLFEDSAMSQQPTVSDRLRWLLQTFKYQKNIKIHAFNEEGMEPYPH
GWDVWSNGIKAFMAEKGIQPDVIYTSEEQDAPQYEEHLGIETVLVDPKRTFMNISGTQIRENPFRYWEYI
PTEVRPFFVRTVAILGGESSGKSTLVNKLANIFNTTSAWEYGREYVFSHLGGDEMALQYSDYDKIALGHA
QYIDFAVKYANKVAFIDTDFVTTQAFCKKYEGREHPFVQALIDEYRFDLTILLENNTPWVADGLRSLGSS
VDRKRFQNLLKEMLKENNIEYVHVESPDYDKRYLRCVELVDQMLGEQRI
>gnl|CDD|181230 PRK08105, PRK08105, flavodoxin; Provisional
MAKVGIFVGTVYGNALLVAEEAEAILTAQGHEVTLFEDPELSDWQPYQDELVLVVTSTTGQGDLPDSIVP
LFQALKDTAGYQPNLRYGVIALGDSSYDNFCGAGKQFDALLQEQGAKRVGERLEIDACETPEPEVEANPW
VEQWGTLLS
>gnl|CDD|181231 PRK08114, PRK08114, cystathionine beta-lyase; Provisional
MTDKKLDTQLVNAGRSKKYTQGSVNSVIQRASSLVFDSVEAKKHATRNRANGELFYGRRGTLTHFSLQEA
MCELEGGAGCALYPCGAAAVANAILAFVEQGDHVLMTGTAYEPTQDFCSKILSKLGVTTTWFDPLIGADI
AKLIQPNTKVVFLESPGSITMEVHDVPAIVAAVRSVNPDAVIMIDNTWAAGVLFKALDFGIDISIQAGTK
YLVGHSDAMIGTAVANARCWEQLRENSYLMGQMVDADTAYMTSRGLRTLGVRLRQHEESSLKVAEWLAEH
PEVARVNHPALPGCKGHEFWKRDFTGSSGLFSFVLKKKLTDEQLANYLDNFSLFSMAYSWGGFESLILAN
QPEEIAAIRPAGEVDFTGTLIRLHIGLEDVDDLIADLAAGFARIV
>gnl|CDD|236152 PRK08115, PRK08115, vitamin B12-dependent ribonucleotide reductase
MMTTMMEKMKINIEKLNKDIEHFPQVHPITPDMHITHKGVSRLVMLDRYSFKDTEKKTLAEGDFVVLTVK
ADPKFPARGLGFIVELDWEAKKAKILVEEEFRGVLDDPEEAETGIVTRSLDTIEKPLEIFYEQIAKRNAT
GLAAVEKTEEKRKESFEKFYQELVNMNFVPAGRVLYGAGSKTDVTYFNCYVMPFVKDSREGISEHRKQVM
EIMSRGGGVGTNGSTLRPRNTLARGVNGKSSGSVSWLDDIAKLTHLVEQGGSRRGAQMIMLADWHPDILE
FIISKMQNPRILRYLLENTEDEQIKRLVKEKLKFTPLSEVEEAMYQAIVNYKNIEGQGGFDTKVIKEAEN
KLRTGGTYTVNNPEFLTGANISVCLTKEFMEAVENDEEYELRFPDVENYTEEEMEIYNEEWHEVGDVREW
EKMGYPVRTYRKIKAKELWNLINICATYSAEPGIFFIDNANEMTNAKAYGQKVVATNPCGEQPLAPYSVC
NLAAINLANMADKETKTVDYEKLKRTVEVGVRMQDNVIDATPYFLEENKKQALGERRVGLGVMGLHDLLI
YCETVYGSEEGNQLVDQIFETIATTAYRTSIELAKEKGSFPFLVGQTEEETAKLREAFINTGYMKKMPED
IREDILKYGIRNSHLLTVAPTGSTGTMVGVSTGLEPYFSFSYYRSGRLGKFIEVKADIVQEYLDKHPEAD
ENHLPEWFISAMELKPEAHADVQCIIQRWVDSSLSKTVNAPKGYTVEQVQKVYERLYRGGAKGGTVYVDG
SRDAQVLTLKAEENDLDEQLLLLPEELEEEETKKPVVLVDTIQDVRSTDVTIGSEVGNTCPVCREGTVEE
IGGCNTCTNCGAQLKCGL
>gnl|CDD|236153 PRK08116, PRK08116, hypothetical protein; Validated
MTRSVDTEADSEEDGGEYCEVCGKRIEKVVELLGKNRIVPIMCECEREAEEAKEREEENREKQRRIERLK
SNSLLDEKFRNSTFENFLFDKGSEKAYKIARKYVKKFEEMKKENVGLLLWGSVGTGKTYLAACIANELIE
KGVPVIFVNFPQLLNRIKSTYKSSGKEDENEIIRSLVNADLLILDDLGAERDTEWAREKVYNIIDSRYRK
GLPTIVTTNLSLEELKNQYGKRIYDRILEMCTPVENEGKSYRKEIAKEKLQRLKELLK
>gnl|CDD|181234 PRK08117, PRK08117, aspartate aminotransferase family protein
MQTTWSDLVERYPQLLAPALAKDHPNLPVVKGEGCYYYGVDGKEYLDFTSGIAVANVGHRHPKVVQAIKE
QADKLMHGPSGVIYYESILKLAEELAEITPGGLDCFFFSNSGAEAIEGALKLAKHVTKRPYIISFTGCFH
GRTLGALSVTTSKSKYRKYYQPLLGSVYQAPYPYCDRCPKGEDPEVCFLECLRDLESLFKHQVTPEEVAA
VIIEPVLGEGGYIVPPKSFLKKLREICDRHGILLIFDEVQTGFGRTGEWFAAQTFGVVPDIMTIAKGIAS
GLPLSAVVASKELMEQWPLGSHGTTFGGNPVACAAALATLEVIKEEKLLDNANEMGAYALERLEVLKEKH
PVIGDVRGIGLMIGIEIVDPDGEPDGDAVEKILDKCLEKGLLFYLCGNAGNVLRMIPPLTVTKEEIDEGL
DILDEALTEYEAK
>gnl|CDD|181235 PRK08118, PRK08118, DNA topology modulation protein
MKKIILIGSGGSGKSTLARQLGEKLNIPVHHLDALFWKPNWEGVPKEEQITVQNELVKEDEWIIDGNYGG
TMDIRLNAADTIIFLDIPRTICLYRAFKRRVQYRGKTRPDMGAGCEEKFDLQFFKWIWEYPKTKRPSILK
RLNQLSEEKDIVILKSRNEVRLFLEKI
>gnl|CDD|236154 PRK08119, PRK08119, flagellar motor switch protein; Validated
MMNDFLSQEEIDALLNGGDSDSEEASEESPEEEELTDLEKDALGEIGNISMGSAATALSTLLNQKVNITT
PVVSVTTLEELKKEFPIPYVAVEVKYTEGLSGENLLVIKQDDAAIIADLMMGGDGTVEEPELSEIELSAV
QEAMNQMIGSAATSMSTMFNRKVDISPPKSKILDFAEEPLTEEIPEDEPIVKVSFRLKIGELIDSEIMQL
LPVDFAKELVAILLGEEEEEEEEVEEEEAQASPAAEPATAQAAPAPKQEQQQAPPQRQEPEKEAQPVNVQ
PAQFQSFDPPPLATTEPRNLDLILDVPLQVTVELGRTKKSIKDILELGTGSIIELDKLAGEPVDILVNGK
LIAKGEVVVIDENFGVRITDIVSQSERIKSLK
>gnl|CDD|236155 PRK08123, PRK08123, histidinol-phosphatase HisJ
MMKRDGHTHTPFCPHGSKDDLEAYIERAIELGFTEITFTEHAPLPPGFIDPTPRQDSAMAIEQLERYLKE
LNELKKKYAGQIDIRIGLEVDYIEGYEEETRAFLNEYGPLLDDSILSVHFLKGDGEYYCIDYSPETFAEF
VDLLGSIEAVYEAYYETVLQSIEADLGPYKPKRIGHITLVRKFQKLFPPDFDEKNKELIEDILALIKKRG
YELDFNTAGLRKPYCGEPYPPGEIITLAKKLGIPLVYGSDAHSAADVGRGYDTIEQKILK
>gnl|CDD|181238 PRK08124, PRK08124, flagellar motor protein MotA; Validated
MDITTIIGLILGLIAVVVGMVVKGASLAVLLNPAAILIIIVGTIAAVMIAFPMSELKKVPKLFKVLFKEK
KDPSKEELIEQFVEWASESRREGLLALEAQLDEIDDPFLKRGLKMVIDGQSPEFIRDVLEEEIEAMEERH
AAGAAIFTQAGTYAPTLGVLGAVIGLIAALGNLSDIEKLGHAISAAFVATLLGIFTGYVLWHPFANKLKR
KSKEEIELKYIIIEGVLAIQEGNAPRVIEEKLLGYLSPKERKKLEEGAEKNAE
>gnl|CDD|236156 PRK08125, PRK08125, bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA
MKAVVFAYHDIGCVGIEALLAAGYEIAAVFTHTDNPGENHFFGSVARLAAELGIPVYAPEDVNHPLWVER
IRELAPDVIFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRAD
AGAIVAQQRVAIAPDDTALTLHHKLCHAARQLLEQTLPAIKHGNIPEIPQDESQATYFGRRTPADGLIDW
HKPASTLHNLVRAVTDPWPGAFSYVGEQKFTVWSSRVLPDASGAQPGTVLSVAPLRIACGEGALEIVTGQ
AGDGLYMQGSQLAQELGLVAGARLNSKPACSAKRRTRVLILGVNGFIGNHLTERLLRDDNYEVYGLDIGS
DAISRFLGHPRFHFVEGDISIHSEWIEYHIKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLKIIRYC
VKYNKRIIFPSTSEVYGMCTDKYFDEDTSNLIVGPINKQRWIYSVSKQLLDRVIWAYGEKEGLRFTLFRP
FNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLVDGGKQKRCFTDIRDGIEALFRIIENKDNRCDG
QIINIGNPDNEASIRELAEMLLASFEKHPLRDHFPPFAGFRVVESSSYYGKGYQDVEHRKPSIRNARRLL
DWEPKIDMQETIDETLDFFLRTVDLTEKAS
>gnl|CDD|236157 PRK08126, PRK08126, hypothetical protein; Provisional
MTDGTLDPPAFDFLSFLSTTAEHKDSEYETAVAASGATELPAIVPAGEDSALRLAEIRAAANPLLEAARP
LLRALADMPATLDSAAVEQLRTLLVREVRLFQKLCEQANLRRDHMLGVRYCLCTALDEAANRTTWGRGGV
WASRGLLTTFHGERDGGEKVFLLIGRLATDPQEHVDLLEVIYRILSLGFEGRYSVEADGRRKLEQIRQRL
YTEITGRRDPVPPALSPHWQGAEPGRLRSFRDVPVWATAAVLSLILLGLFGWYKYRLLTRSADVQQRIAA
IGRMTPPPAPHRLRLKILLKNEIARGTLSVDEDARHSSVVFRGDAMFVPGQATVNPAMGPLIAKIAREIA
RVGGKVTVTGHTDNQPIRSAQFASNLVLSEKRAAQVAQMLQSAGVPASRLEAVGKGDAQPVADNRTPQGR
AQNRRVEITVAE
>gnl|CDD|181241 PRK08130, PRK08130, putative aldolase; Validated
MTEQALREEIVRLGRSLFQRGYTVGSAGNISARLDDGGWLVTPTGSCLGRLDPARLSKVDADGNWLSGDK
PSKEVPLHRAIYRNNPECGAVVHLHSTHLTALSCLGGLDPTNVLPPFTPYYVMRVGHVPLIPYYRPGDPA
IAEALAGLAARYRAVLLANHGPVVWGSSLEAAVNATEELEETAKLILLLGGRPPRYLTDEEIAELRSTFG
ARW
>gnl|CDD|181242 PRK08131, PRK08131, 3-oxoadipyl-CoA thiolase
MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNA
LLLAGLPVTVPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDAKVF
DTTIGARFPNPKIVAQYGNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVP
QGRKLPPKLVAEDEHPRPSSTVEALTKLKPLFEGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMAR
ILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLGVDFDDPRVNPNGG
AIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIERVS
>gnl|CDD|236158 PRK08132, PRK08132, FAD-dependent oxidoreductase; Provisional
IDYQTPKFPYRPHADQDADDPARHPVVVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLSTGSRAICFAKR
SLEIFDRLGCGERMVDKGVSWNVGKVFLRDEEVYRFDLLPEPGHRRPAFINLQQYYVEGYLVERAQALPN
IDLRWKNKVTGLEQHDDGVTLTVETPDGPYTLEADWVIACDGARSPLREMLGLEFEGRTFEDRFLIADVK
MKADFPTERWFWFDPPFHPGQSVLLHRQPDNVWRIDFQLGWDADPEAEKKPENVIPRVRALLGEDVPFEL
EWVSVYTFQCRRMDRFRHGRVLFAGDAAHQVSPFGARGANSGIQDADNLAWKLALVLRGRAPDSLLDSYA
SEREFAADENIRNSTRSTDFITPKSPVSRLFRDAVLRLARDHPFARRLVNSGRLSVPAVYADSPLNTPDG
DAFAGGPVPGAPAPDAPVRADGEPGWLLDLLGGGFTLLLFGDDAAAAALLQALAAAALPVRVVAVVPAGA
AQAAAGVLEDADGLAAERYDARPGTVYLIRPDQHVAARWRTPDAAAVRAALARALGR
>gnl|CDD|181244 PRK08133, PRK08133, O-succinylhomoserine sulfhydrylase; Validated
DDDSLGFDTLAVRAGQLRSPFGEHSEALFLTSSFVFESAAEAAARFAGEEPGNIYSRFTNPTVTMFQERL
AALEGAEACVATASGMAAILAVVMALLQAGDHVVSSRSLFGSTVSLFEKIFARFGIETTFVDLTDLDAWR
AAVRPNTKLFFLETPSNPLTELADIAALAEIAHAAGALLVVDNCFCTPALQQPLKLGADVVIHSATKYLD
GQGRVLGGAVVGSKELMEEVFGFLRTAGPTLSPFNAWVFLKGLETLSLRMEAHSANALALAEWLEAHPGV
ERVFYPGLPSHPQHELAKRQQKGGGAIVSFEVKGGREAAWRVIDATRLISITANLGDTKTTITHPATTTH
GRLSPEARAAAGITEGLIRVAVGLEDVADIKADLARGLAA
>gnl|CDD|236159 PRK08134, PRK08134, O-acetylhomoserine aminocarboxypropyltransferase; Validated
MPGMSPPGFDTLALHAGAAPDPATGARAVPIHLTTSFVFRDSDHAAALFNLERAGHVYSRISNPTVAVLE
ERVAALEGGVGAIATASGQAALHLAIATLMGAGSHIVASSALYGGSHNLLHYTLRRFGIETTFVKPGDID
GWRAAIRPNTRLLFGETLGNPGLEVLDIPTVAAIAHEAGVPLLVDSTFTTPYLLRPFEHGADLVYHSATK
FLGGHGTAIGGVLVDGGRFDWEASGKFPELTEPYAGFHGMVFAEESTVAAFLLRARREGLRDFGACLSPM
NAWQLLQGIETLPLRMERHVANTRKVVAFLASHPAVARVAHPELESHPDHALAKRLLPRGAGSVFSFDLK
GGRAAGRKFIESLKLFSHLANVGDARSLVIHPASTTHFRMDAAALAAAGIGEGTIRLSIGLEDADDLIDD
LKRALKAAEKAGA
>gnl|CDD|236160 PRK08136, PRK08136, glycosyl transferase family protein; Provisional
MDYAKIIKEIGRGKNGARDLDRDTARALYGAMLDGRVPDLELGAILIALRIKGESEAEMLGFLDAMQAHT
IPLTPPAGRPMPVVIPSYNGARKQANLTPLLALLLAREGVPVLVHGVSEDPTRVTSAEIFEALGIPPTLH
ADQAQAKLAEGQPAFIPVGVLCPPLARLLALRWRMGVRNSAHTLAKLATPFAEGAALRLSSYTHPEYRDR
LAEFFSDIGARALLMRGTEGEVYANPRRCPQIDWIHDGGCRVLVERQSGSADEPPELPAAKDAATTAAWI
ERVLAGEVPVPESIARQVACCLVAAGEAATIEDGLAR
>gnl|CDD|236161 PRK08137, PRK08137, amidase; Provisional
QTALEERAGALQAAMPAGAAPASQLTRAYLQRIARIDRDGPRLNAVIELNPDAEADAAALDAERKAGKVR
GPLHGIPVLLKDNIDAADPMPTTAGSLALAGNRPTRDAFLVARLRDAGAVILGKANLSEWANFRSTRSSS
GWSARGGLTRNPYALDRSPCGSSSGSGAAVAAGLAAVAIGTETDGSITCPAAINGLVGLKPTVGLVSRDG
IVPISHSQDTAGPMTRTVADAAAVLTAIAGGDPADPATASAPAPAVDYVAALDADALRGARLGVARNYLG
YHPEVDAQFERALAELKAAGAVVIDVVDLDDGDWGEAEKVVLLHEFKAGLNAYLRSTAPHAPVRTLADLI
AFNRAQHAREMPYFGQELFEQAQAAPGLDDPAYLDALADAKRLAGPEGIDAALKEHRLDALVAPTTGPAW
LIDLINGDSFGGSSSTPAAVAGYPHLTVPMGQVQGLPVGLSFIGAAWSEARLLELGYAYEQATHARREPR
FVETANP
>gnl|CDD|236162 PRK08138, PRK08138, enoyl-CoA hydratase; Provisional
MMSTATDVVLLERPADGVALLRLNRPEARNALNMEVRQQLAEHFTELSEDPDIRAIVLTGGEKVFAAGAD
IKEFATAGAIEMYLRHTERYWEAIAQCPKPVIAAVNGYALGGGCELAMHADIIVAGESASFGQPEIKVGL
MPGAGGTQRLVRAVGKFKAMRMALTGCMVPAPEALAIGLVSEVVEDEQTLPRALELAREIARMPPLALAQ
IKEVVLAGADAPLDAALALERKAFQLLFDSEDQKEGMDAFLEKRKPAYKGK
>gnl|CDD|181249 PRK08139, PRK08139, enoyl-CoA hydratase; Validated
MMAPAAATEAPLLLREDRDGVATLTLNRPQAFNALSEAMLAALQAALDAIAADPSVRVVVLAAAGKAFCA
GHDLKEMRAARGLAYFRALFARCSRVMQAIVALPQPVIARVHGIATAAGCQLVASCDLAVAADTARFAVP
GVNIGLFCSTPMVALSRNVPRKQAMEMLLTGEFIDAATAREWGLVNRVVPADALDAAVARLAAVIAAKSP
AAVRIGKEAFYRQAEMPLADAYAYAGDVMAENMMAEDAEEGIDAFLEKRPPEWRGR
>gnl|CDD|236163 PRK08140, PRK08140, enoyl-CoA hydratase; Provisional
MMYETILLAIEAGVATLTLNRPDKLNSFTREMHRELREALDQVEDDGARALLLTGAGRGFCAGQDLADRD
VTPGGAMPDLGESIETFYNPLVRRLRALPLPVIAAVNGVAAGAGANLALACDIVLAARSASFIQAFVKIG
LVPDSGGTWFLPRLVGMARALGLALLGEKLSAEQAEQWGLIWRVVDDAALADEAQQLAAHLATQPTRGLA
LIKQAMNASATNTLDAQLDLERDLQREAGRSADYAEGVSAFLEKRAPRFTGR
>gnl|CDD|236164 PRK08142, PRK08142, thiolase domain-containing protein
MSIKGKAYIVGAYEHPTRKAPDKSVAQLHAEVAKGALADAGLSLADVDGYFCAGDAPGLGPASMVDYLGL
KLRHVDSTETGGSSYLAHVGHAAQAIAAGKCSVALITLAGRPRSEGSSGTEPRNWGADAPDAPFEAPYGP
TTHNLYAMCAMRHMHEYGTTSEQLAWIKVAASHHAQHNPHAMLRDVVTVEDVLNSPMIADPLHRLDCCVV
TDGGGALVVVRPEIARSLKRPLVKVLGAGEAIKGQMGGKVDLTYSGAAWSGPAAFAEAGVTPADIKYASI
YDSFTITVLMQLEDLGFCKKGEGGKFVADGNLISGVGKLPFNTDGGGLCNNHPANRGGMTKVIEAVRQLR
GEAHPAVQVPNCDLALAHGTGGLLGSRHGSATLILERE
>gnl|CDD|236165 PRK08147, flgK, flagellar hook-associated protein FlgK; Validated
MSSLINTAMSGLNAAQAALNTVSNNISNYNVAGYTRQTTILAQAGSTLTAGGWIGNGVYVSGVQREYDAF
ITNQLRAAQTQSSGLTTRYEQMSKIDNLLSDSTNSLSTTMQDFFTSLQTLVSNAEDPAARQALIGKAEGL
VNQFKTTDQYLRDQDKGVNTAIGSSVDQINNYAKQIASLNDQITRLTGVGAGASPNDLLDQRDQLVSELN
QIVGVEVSVQDGGTYNITMANGYSLVQGSTAYQLAAVPSSADPTRTTVAYVDGTAGNIEIPEKLLTTGSL
GGLLTFRSQDLDQTRNQLGQLALAFADAFNTQHKAGFDANGDAGEDFFSIGKPAVLSNSKNTGTASLTAE
YTDASAVKATDYKISFDGTNWQVTRLSDNTTFTVTPDANGKTLEFDGLKVTVTGTPAANDSFTLKPVSDA
IVNMDVLITDESKIAMASEADGGDSDNRNGQALLDLQNKKLVGGKKSFNDAYASLVSDVGNQTATLKTSS
TTQANVVTQLTNQQQSVSGVNLDEEYGNLQRFQQYYLANAQVLQTASTLFDALLNIR
>gnl|CDD|236166 PRK08149, PRK08149, FliI/YscN family ATPase
LRLLQRLAHPLRIQGPIIEAELPDVAIGEICEIRAGWHSNEVIARAQVVGFQRERTILSLIGNAQGLSRQ
VVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVGPISEERVIDVAPPSYAERRPIREPLITGVR
AIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVL
VYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDS
LPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVF
GQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGEYRRGENADNDRAMDKRPALEAFLKQDVAEKSSFSDTL
ERLNEFAA
>gnl|CDD|181254 PRK08150, PRK08150, crotonase/enoyl-CoA hydratase family protein
PSLVSYELDGGVATIGLNRPAKRNALNDGLIAALRAAFARLPEGVRAVVLHGEGDHFCAGLDLSELRERD
AGEGMHHSRRWHRVFDKIQYGRVPVIAALHGAVVGGGLELASAAHIRVADESTYFALPEGQRGIFVGGGG
SVRVPRLIGVARMTDMMLTGRVYDAQEGERLGLAQYLVPAGEALDKAMELARRIAQNAPLTNFAVLNALP
RIADMSADDGLFVESLMAAVAQSAPEAKERLRAFLEKKAAKVKPP
>gnl|CDD|181255 PRK08153, PRK08153, pyridoxal phosphate-dependent aminotransferase
MAFPRLTPLVESLPSTVPFVGPETLERQRGRPFRARIGANESGFGPSPSVIAAMREAAAEIWKYGDPENH
DLRHALAAHHGVAPENIMVGEGIDGLLGLIVRLYVEPGDPVVTSLGAYPTFNYHVAGFGGRLVTVPYRDD
REDLDALLDAARRENAPLVYLANPDNPMGSWHPAADIVAFIEALPETTLLVLDEAYCETAPAGAAPPIDT
DDPNVIRMRTFSKAYGLAGARVGYAIGAPGTIKAFDKVRNHFGMNRIAQAAALAALKDQAYLAEVVGKIA
AARDRIAAIARANGLTPLPSATNFVAIDCGRDGAFARAVLDGLIARDIFVRMPGVAPLDRCIRVSCGPDE
ELDLFAEALPEALEAARKG
>gnl|CDD|236167 PRK08154, PRK08154, anaerobic benzoate catabolism transcriptional regulator; Reviewed
SADADAGPTADATAMTGAAAEEAPFLAALGERVRTLRARRGMSRKVLAQASGVSERYLAQLESGQGNVSI
LLLRRVARALGCSLADLLGDVDTSSPDWLLIRELLEQASPAQLARVRDALSGMLGAGRRAARRRRIALIG
LRGAGKSTLGRMLAARLGVPFVELNREIEREAGLSVSEIFALYGQEGYRRLERRALERLIAEHEEMVLAT
GGGIVSEPATFDLLLSHCYTVWLKASPEEHMARVRAQGDLRPMADNREAMEDLRRILASREPLYARADAV
VDTSGLTVAQSLARLRELVRPALGLPATR
>gnl|CDD|181257 PRK08155, PRK08155, acetolactate synthase large subunit
MASSGTTSTRKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGM
ARTTGKPAVCMACSGPGATNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYL
VRDIEELPQVISDAFRIAQSGRPGPVWIDIPKDVQTAVIELEALPAPAEKDAAPAFDEESIRDAAAMINA
AKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADL
LIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDDVLAQLLPLVEAQPRAEWHQ
LVADLQREFPCPIPKADDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGT
MGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVHQQQSLFYGQR
VFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYPMVPPGAANTE
MIGE
>gnl|CDD|236168 PRK08156, PRK08156, EscU/YscU/HrcU family type III secretion system export apparatus switch protein
MANKTEKPTKKKLRDSAKKGQSFKSKDLITAVVLLGGIAYLVSFGSFSEFMSIYKRILADNFDINIGDYF
LAVMIIFLKILIPFLLLCLLAGALPTLLQTRFVLATEAIKLNFSALNPVKGLKKIFSLRTVKEFVKALLY
LIVFALTAYVFWKNYKKEIFSQLNGNIVGLIVIWRELLVKLVLTFLACALIVLILDFIAEYFLHMKDMKM
DKQEVKREYKEQEGNPEIKSKRREAHQEILSEQVKSDIRNSRLIVANPTHIAIGIYFNPELAPIPFISVR
ETNQRALAVRAYAEKVGVPVVRDIKLARRLYKTHRRYSFVSLEDLDEVLRLLIWLEQVENAGMGVPQPQE
NEVRSAEPGAD
>gnl|CDD|181259 PRK08158, PRK08158, YscQ/HrcQ family type III secretion apparatus protein
MSLRVRQIDRREWLLAQTATEWQRHGQDVTLEYPTRQGMWLRLADAEGSWSGWIQPGDWLEHVSPELAGA
AVSAGAEHLVVEWLAATERPLELPVPHLSCRRLCVGNPVPGSALPEGPLLRIMTDRGGLWFENAPELPAV
GGGRPKMLRWPLRFVIGSSDTQRSLLGRIGIGDVLLISTSRAEVYCYAKKIGHFNRVEEGIIVETLDIQH
IEEENNTTETAETLPGLNQLPVKLEFVLYRKNVTLAELEELCQQQLLSLPTNAELNVEIRANGALLGNGE
LVQMDDTLGVEIHEWLSGSGNVE
>gnl|CDD|181260 PRK08159, PRK08159, enoyl-[acyl-carrier-protein] reductase FabI
MAQASGLMAGKRGLILGVANNRSIAWGIAKACRAAGAELAFTYQGDALKKRVEPLAAELGAFVAGHCDVT
DEASIDAVFETLEKKWGKLDFVVHAIGFSDKDELTGRYVDTSRDNFTMTMDISVYSFTAVAQRAEKLMTD
GGSILTLTYYGAEKVMPHYNVMGVAKAALEASVKYLAVDLGPKNIRVNAISAGPIKTLAASGIGDFRYIL
KWNEYNAPLRRTVTIEEVGDSALYLLSDLSRGVTGEVHHVDSGYHVVGMKAVDAPDISVVKD
>gnl|CDD|236169 PRK08162, PRK08162, acyl-CoA synthetase; Validated
MNIYEQGLDRNAANYVPLTPLSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDT
VAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPK
PLVIDVDDPEYPGGRFIGALDYEAFLASGDPDFAWTLPADEWDAIALNYTSGTTGNPKGVVYHHRGAYLN
ALSNILAWGMPKHPVYLWTLPMFHCNGWCFPWTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIV
LSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFDLTHVYGLTETYGPATVCAWQPEWDALPL
DERAQLKARQGVRYPLQEGVTVLDPDTMQPVPADGETIGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHT
GDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDG
ASATEEEIIAHCREHLAGFKVPKAVVFGELPKTSTGKIQKFVLREQAKSLKAIDL
>gnl|CDD|181262 PRK08163, PRK08163, 3-hydroxybenzoate 6-monooxygenase
MTKVTPVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIGEIGAGIQLGPNAFSALDALGVGEAARQRAV
FTDHLTMMDAVDAEEVVRIPTGQAFRARFGNPYAVIHRADIHLSLLEAVLDHPLVEFRTSTHVVGIEQDG
DGVTVFDQQGNRWTGDALIGCDGVKSVVRQSLVGDAPRVTGHVVYRAVIDVDDMPEDLRINAPVLWAGPH
CHLVHYPLRGGEQYNLVVTFHSREQEEWGVKDGSKEEVLSYFEGIHPRPRQMLDKPTSWKRWATADREPV
AKWSTGRVTLLGDAAHPMTQYMAQGACMALEDAVTLGKALEGCDGDAEAAFALYESVRIPRTARVVLSAR
EMGRIYHAKGVERQVRNLLWKGRTQEQFYDALEWLYGWKEDNCLEP
>gnl|CDD|236171 PRK08168, PRK08168, NADH-quinone oxidoreductase subunit L
VLLSVCALLPAVLMSLAAGGLLLSRWLTRALWRIAQAASLAGLFLALLGLVLFATGAAWPAAAWLEVSGL
GLVMAALVQLLGWVIGRFSHRYLQGEPGQRRYVRALAGVLAAVHLLVLSDHLLVLIAAWAAISLALHRLL
CFYPDRPFARLAAHKKFIADRLAELLLLAAAALAYLEVGSLSLSALWAHLAAQGASPSLQAAALLLVLAV
ILKTAQLPVHGWLIQVMEAPTPVSALLHAGVVNLGGFVLIRFAPLLEQAPPARWLLVLVGLATAVLAGLV
MLTRISIKVRLAWSTVAQMGFMLLECGLGLYELALLHLVAHSLYKAHAFLSASEAVRDTRLRRLQGPQSA
AGVVSLLLAPLLSAALVLLLQSLLPLGAWPWWWSAVLALAWAPLLWQPCASGASTLSGLGLGLLLVAGLT
ALAFLAHLLPLGLADAPGPALGLAALAGMAALYLLQALLQRRPQHRLSRWLRRWSYAGFYLDEWYTRLAL
RLWPTRWPPRAARPALRAAPTTSARD
>gnl|CDD|181265 PRK08170, PRK08170, acetyl-CoA C-acetyltransferase
MARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVV
ALRLGCGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWLAGWYAA
KSIGQKLAALGKLRPSYLAPVIGLLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQ
AEGRLKEVVPLFDRDGKFYDHDDGVRPDSSMEKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEA
VKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWADE
EYCREQLGLDGALGELDRERLNVDGGAIALGHPVGASGARIVLHLLHALKRRGTKRGIAAICIGGGQGGA
MLLERV
>gnl|CDD|181266 PRK08172, PRK08172, acyl carrier protein
MNMDIEARVKKVITSCIAVDVDSINGQTHLVEDLYADSLDLIDIVFGLSEEFDISCNENDLPDMTTFADI
CRVVKKSLESRV
>gnl|CDD|236172 PRK08173, PRK08173, DNA topoisomerase III; Validated
MSKALIIAEKPSVANDIARALGGFTKHDEYFESDEYVLSSAVGHLLEIAAPEEYEVKRGKWSFAHLPVIP
PHFDLNPIAKTESRLKVLTKLIKRKDVTRLINACDAGREGELIFRLIAQHAKAKKPVKRLWLQSMTPQAI
RDGFANLRSDEDMQPLADAARCRSEADWLVGINGTRAMTAFNSKGGGFFLTTVGRVQTPTLSIVVEREEK
IRRFVPRDYWEVRAEFVAAAGFYEGRWFDPKFKKDEFDPEKRASRLWSEAAAEAIVAACRGKPGTVTEES
KPSTQLSPLLFDLTSLQREANGRFGFSAKNTLGLAQALYEKHKVLTYPRTDSRALPEDYLGTVKQTLEML
KESNNYLPHAKQILDKGWVKPNKRIFDNSKISDHFAIIPTLQAPKSLSEPEQKLYDLVVKRFLAVFFPAA
EFLVTTRITEVAGHHFKTEGKVLVNPGWLAVYGKEAQGADANLVPVQKGEKVKTDKIEAVALTTKPPARY
NEATLLSAMEGAGKLVEDDELREAMAEKGLGTPATRAAIIEGLLGEKYLVREGRELIPTAKAFQLMTLLR
GLGVEELTSPELTGEWEYKLSQIERGKLSRDAFMQEIAQMTQQIVKRAKEYDSDTIPGDYATLQTPCPNC
GGVVKENYRRFACTKCDFSISKIPGGRQFEIAEVEELLRKKEIGPLSGFRSKMGRPFSAILKLSDETKNY
KLEFDFGQDQGGEDGEPVDFSAQEPVGACPKCGGRVFEHGMSYVCEKSVGPPKTCDFRSGKVILQQEISR
EQMAKLLADGKTDLLPGFKSSRTGRNFKAYLVKQPDGKIGFEFEPREPKAAAAKKTAAKATAAAATKAEK
AAAKKAPAKKTAAKKTAARKTG
>gnl|CDD|181268 PRK08175, PRK08175, aminotransferase; Validated
RRFTRIDRLPPYVFNITAELKMAARRRGEDIIDFSMGNPDGPTPPHIVEKLCEVAQRPDTHGYSTSRGIP
RLRRAISRWYQDRYDVDIDPESEAIVTIGSKEGLAHLMLATLDHGDTVLVPNPSYPIHIYGAVIAGAQVR
SVPLVEGVDFFNELERAIRESYPKPKMMILGFPSNPTAQCVELEFFEKVVALAKRYDVLVVHDLAYADIV
YDGWKAPSIMQVPGAKDVAVEFFTLSKSYNMAGWRIGFMVGNPELVSALARIKSYHDYGTFTPLQVAAIA
ALEGDQQCVRDIAEQYKRRRDVLVKGLHEAGWMVEMPKASMYVWAKIPEPYAAMGSLEFAKKLLNEAKVC
VSPGIGFGDYGDTHVRFALIENRDRIRQAIRGIKAMFRADGLLPA
>gnl|CDD|181269 PRK08176, pdxK, pyridoxine/pyridoxal/pyridoxamine kinase
MSSLLLFNDKSRALQADIVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPD
EWFSGYLRALQERDALRQLRAVTTGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSGIYVKPD
LPEAYRQHLLPLAQGLTPNIFELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVITSAAGNEENQEMQVVV
VTADSVNVISHPRVDTDLKGTGDLFCAELVSGLLKGKALTDAAHRAGLRVLEVMRYTQQAGSDELILPPL
A
>gnl|CDD|236173 PRK08177, PRK08177, SDR family oxidoreductase
KRTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEKLDMNDPASLDQLLQRLQGQ
RFDLLFVNAGISGPAHQSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPD
GGEMPLYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDMGGDNAPLDVETSVKGLVEQIEAASGK
GGHRFIDYQGETLPW
>gnl|CDD|236174 PRK08178, PRK08178, acetolactate synthase 1 small subunit
MQNTTHDNVILELTVRNHPGVMSHVCGLFARRAFNVEGILCLPIQDGDKSRIWLLVNDDQRLEQMISQIE
KLEDVLKVRRNQSDPTMFNKIAVFFQ
>gnl|CDD|236175 PRK08180, PRK08180, feruloyl-CoA synthase; Reviewed
ATPARYRPVAFAPPAVEVERRADGTIYLRSAEPLGDYPRRLTDRLVHWAQEAPDRVFLAERGADGGWRRL
TYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSLVSQDFGKLRH
VLELLTPGLVFADDGAAFARALAAVVPADVEVVAVRGAVPGRAATPFAALLATPPTAAVDAAHAAVGPDT
IAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVLVDWLPWNHTFGGNHNLGIVLYNGGT
LYIDDGKPTPGGFDETLRNLREISPTVYFNVPKGWEMLVPALERDAALRRRFFSRLKLLFYAGAALSQDV
WDRLDRVAEATCGERIRMMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPVGGKLEVRVKGPN
VTPGYWRAPELTAEAFDEEGYYRSGDAVRFVDPADPERGLMFDGRIAEDFKLSSGTWVSVGPLRARAVSA
GAPLVQDVVITGHDRDEIGLLVFPNLDACRRLAGLLADASLAEVLAHPAVRAAFRERLARLNAQATGSST
RVARALLLDEPPSLDAGEITDKGYINQRAVLARRAALVEALYADEPDDPVIIAA
>gnl|CDD|136670 PRK08181, PRK08181, transposase; Validated
MSTTNVIDEARLGLLLNELRLPTIKTLWPQFAEQADKEGWPAARFLAAIAEHELAERARRRIERHLAEAH
LPPGKTLDSFDFEAVPMVSKAQVMAIAAGDSWLAKGANLLLFGPPGGGKSHLAAAIGLALIENGWRVLFT
RTTDLVQKLQVARRELQLESAIAKLDKFDLLILDDLAYVTKDQAETSVLFELISARYERRSILITANQPF
GEWNRVFPDPAMTLAAVDRLVHHATIFEMNVESYRRRTALERKRGPGRPPTRATIKTAS
>gnl|CDD|169261 PRK08182, PRK08182, single-stranded DNA-binding protein; Provisional
MSTHFVGEGNIGSAPEYREFPNGNDEPRRLLRLNVYFDNPVPTKDGEYEDRGGFWAPVELWHRDAEHWAR
LYQKGMRVLVEGRMERDEWTDNEDNERVTFKVEARRVGILPYRIESVTLSPKPAATEPEAEPKPQAAQES
TAPKEPKR
>gnl|CDD|236176 PRK08183, PRK08183, NADH:ubiquinone oxidoreductase subunit NDUFA12
KSFLLQIFTWWNGQTLGTRFFTWRKGERVGEDEFGNVYYRTKGGKPSDGRERRWVIYNGYAEASRIPPEW
HGWLHHTVDVPPTKEPYPPREWEKPHQPNLTGTPLAYRPKGSILRGGERPRATGDYDAWTPGN
>gnl|CDD|181275 PRK08185, PRK08185, hypothetical protein; Provisional
MKELLKVAKEHQFAVGAFNVADSCFLRAVVEEAEANNAPAIIAIHPNELDFLGDNFFAYVRERAKRSPVP
FVIHLDHGATIEDVMRAIRCGFTSVMIDGSLLPYEENVALTKEVVELAHKVGVSVEGELGTIGNTGTSIE
GGVSEIIYTDPEQAEDFVSRTGVDTLAVAIGTAHGIYPKDKKPELQMDLLKEINERVDIPLVLHGGSANP
DAEIAESVQLGVGKINISSDMKYAFFKKVREILSDNPSLYEPNQIYPSAIEAAKEVVRHKMDLFNSTGKA
DLY
>gnl|CDD|236177 PRK08186, PRK08186, allophanate hydrolase; Provisional
MPLPTDLTLASLRAAYRAGTLTPRAVVAALYARIAAVDDPEVWIHLRPEADLLAQAAALEARDPAALPLY
GVPFAVKDNIDVAGLPTTAACPAFAYTPERDATVVARLRAAGAIVIGKTNLDQFATGLVGTRSPYGAVRN
AFDPEYVSGGSSSGSAVAVALGLVSFALGTDTAGSGRVPAAFNNIVGLKPTLGLLSTRGVVPACRTLDCV
SVFALTVDDADAVLAVMAGFDPADPYSRANPADAPAALPAGPRVGVPRAAQLEFFGDAEAEAAFAAALAR
LEALGAELVEIDFSPFLEAARLLYEGPWVAERYAAVGEFLEAHPDAVDPVVRGIIAGAAAFSAADAFRAL
YRLAELRRAAEAVLAGIDALLVPTAPTHPTIAEVAADPIGLNSRLGTYTNFVNLLDLCALAVPAGFRADG
LPFGVTLIAPAFADQALADLAARLQAALALPLGGGPAPPAPPPPLPAGPDRVRLAVVGAHLSGMPLNHQL
TSRGARLLEATTTAPDYRLYALAGTPPPKPGLVRVAEGGAAIAVEVWELPPAAFGSFVAAIPAPLGIGTV
ELADGRWVKGFLCEPAALAGARDITEFGGWRAYLASLAAA
>gnl|CDD|236178 PRK08187, PRK08187, pyruvate kinase; Validated
SDDDLSEPAALLEALLALRADVVEEAQARLAGWASRIERPEFLPSAANLAHYLALRRHDLRPLQRALMPL
GLSSLGRLESRVLPTLDAVIAALAALCGEPGPPPRPSPEQFFAGERLLAAHTEELFGPRPAARRTRIMVT
LPSEAADDPDFVLRLAERGMDCARINCAHDDPAAWQAMIGHLRQAERATGRRCKILMDLAGPKIRTGAVA
GPLGKTRLYTGDRLALVAQGPPRRIDEEHFQVTCTLPEILARLAVGARVWIDDGKLGARVERVGPGGALL
EVTHARPKGLKLKPEKGLNFPDTALDLPALTEKDRADLDFVARHADLVGYSFVQSPGDVEALQAALAARR
PDDWRKLGLVLKIETPRAVANLPELIVQAAGRQPFGVMIARGDLAVEIGFERLAEMQEEILWLCEAAHVP
VIWATQVLEGLVKKGLPSRAEMTDAAMAARAECVMLNKGPYLVEAVTFLDDLLARMDGHQHKKTPQLRAL
RSW
>gnl|CDD|236180 PRK08190, PRK08190, bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
MDLELIENRTFDEIAIGDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALI
SAVLGTRLPGPGTIYLGQSLRFRRPVRIGDTLTVTVTVREKDPEKRIVVLDCRCTNQDGEVVITGTAEVI
APTEKVRRPRVVLPEVRLHRHDRYERLLAAARGLPPLRTAVVHPCDAESLRGALEAAEAGLIEPVLVGPE
AKIRAAAEEAGLDLSGVRIVDVPHSHAAAARAVALARAGEVEALMKGSLHTDELLSAVVARDSGLRTERR
ISHVFAMDVPTYPRPLLITDAAINIAPTLEDKRDIVQNAIDLAHALGVEEPKVAILSAVETVNPKMPSTL
DAAALCKMADRGQITGGIVDGPLAFDNAISAEAARTKGIVSPVAGQADILVVPDLEAGNMLAKQLTYLAG
ADAAGIVLGARVPIILTSRADSLRARLASCALALLVAHARRAGPAA
>gnl|CDD|169269 PRK08192, PRK08192, aspartate carbamoyltransferase; Provisional
MQFQGSHILSVNQLDRDAIQRIFNVADRMEPYALREKRTRVLEGAILGNLFFEPSTRTRVSFGCAFNLLG
GHVRETTGMASSSLSKGESLYDTARVLSTYSDVIAMRHPDAGSVKEFAEGSRVPVINGGDGSNEHPTQAL
LDLFTIQKELAHAGRGIDGMHIAMVGDLKFGRTVHSLSRLLCMYKNVSFTLVSPKELAMPDYVISDIENA
GHKITITDQLEGNLDKADILYLTRIQEERFPSQEEANKYRGKFRLNQSIYTQHCKSNTVIMHPLPRDSRA
QANELDNDLNSHPNLAIFRQADNGLLIRMALFALTLGVDDQLEKYECPVNWYSRKADR
>gnl|CDD|236181 PRK08193, araD, L-ribulose-5-phosphate 4-epimerase AraD
MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKL
KPSSDTPTHLVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEY
EWETGKVIVETFEKRGIDPAAVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQ
QTLLDKHYLRKHGKNAYYGQK
>gnl|CDD|181281 PRK08194, PRK08194, tartrate dehydrogenase; Provisional
MKQFKIAVIPGDGVGKEVVPAAVRVLKAVAEVHGGLKFEFTEFPWSCEYYLEHGEMMPEDGLEQLKQFDA
IFLGAVGNPKLVPDHISLWGLLIKIRREFEQVINIRPAKQLRGIKSPLANPKDFDLLVVRENSEGEYSEV
GGRIHRGEDEIAIQNAVFTRKGTERAMRYAFELAAKRRKHVTSATKSNGIVHSMPFWDEVFQEVGKDYPE
IETDSQHIDALAAFFVTRPEEFDVIVASNLFGDILTDIGAAIMGSIGIAPAANINVNGKYPSMFEPVHGS
APDIAGKGIANPIGQIWTAKLMLDHFGEEELGSHLLDVIEDVTEDGIKTPDIGGRATTDEVTDEIISRLK
KL
>gnl|CDD|181282 PRK08195, PRK08195, 4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
GKKIYISDVTLRDGMHAVRHQYTLEQVRAIARALDAAGVPVIEVTHGDGLGGSSFNYGFGAHTDEEYIEA
AAEVVKQAKIAALLLPGIGTVDDLKMAYDAGVRVVRVATHCTEADVSEQHIGLARELGMDTVGFLMMSHM
APPEKLAEQAKLMESYGAQCVYVVDSAGALLPEDVRDRVRALRAALKPDTQVGFHGHNNLGLGVANSLAA
VEAGATRIDGSLAGLGAGAGNTPLEVLVAVLDRMGWETGVDLYKLMDAAEDLVRPLMDRPVRVDREALTL
GYAGVYSSFLLHAERAAERYGVDARDILVELGRRKMVGGQEDMIVDVALDLARERAA
>gnl|CDD|181283 PRK08197, PRK08197, threonine synthase; Validated
PFSYVSHLECSKCGETYDADQVHNLCKCGKPLLVRYDLEAVKQAVTREALAGRPANLWRYHELLPVRDPE
HIVSLGEGMTPLLPLPRLGKALGIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNAGA
AWAAYAARAGIRATIFMPADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYR
IEGKKTMGLELAEQLGWRLPDVILYPTGGGVGLIGIWKAFDELEALGWIGGKRPRLVAVQAEGCAPIVKA
WEEGKEESEFWEDAHTVAFGIRVPKALGDFLVLDAVRETGGCAIAVSDDAILAAQRELAREEGLFACPEG
AATFAAARQLRESGWLKGDERVVLFNTGSGLKYPDTVPVVVPVL
>gnl|CDD|181285 PRK08199, PRK08199, thiamine pyrophosphate protein; Validated
MTSTPRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTG
RPGICFVTRGPGATNASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAA
RIPELVSRAFHVATSGRPGPVVLALPEDVLSETAEVPDAPPYRRVAAAPGAADLARLAELLARAERPLVI
LGGSGWTEAAVADLRAFAERWGLPVACAFRRQDLFDNRHPNYAGDLGLGINPALAARIREADLVLAVGTR
LGEVTTQGYTLLDIPVPRQTLVHVHPDAEELGRVYRPDLAIVADPAAFAAALAALEPPASPAWAEWTAAA
HADYLAWSAPLPGPGAVQLGEVMAWLRERLPADAIITNGAGNYATWLHRFFRFRRYRTQLAPTSGSMGYG
LPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTIRMHQEREYPGRVSGT
DLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRIDPEAITPTATLSQIREQALA
>gnl|CDD|169276 PRK08201, PRK08201, dipeptidase
MMQQVEAYLRERREAHLEELKEFLRIPSISALSEHKEDVRKAAEWLAGALEKAGLEHVEIMETAGHPIVY
ADWLHAPGKPTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEG
TLPVNVKFCIEGEEEIGSPNLDSFVEEEKDKLAADVVLISDTTLLGPGKPAICYGLRGLAALEIDVRGAK
GDLHSGLYGGAVPNALHALVQLLASLHDEHGTVAVEGFYDGVRPLTPEEREEFAALGFDEEKLKRELGVD
ELFGEEGYTALERTWARPTLELNGVYGGFQGEGTKTVIPAEAHAKITCRLVPDQDPQEILDLIEAHLQAH
TPAGVRVTIRRFDKGPAFVAPIDHPAIQAAARAYEAVYGTEAAFTRMGGSIPVVETFSSQLHIPIVLMGF
GLPSENFHAPNEHFHLENFDKGLRTLVEYWHQLAEG
>gnl|CDD|236183 PRK08202, PRK08202, purine nucleoside phosphorylase; Provisional
DLLEKIEEAAAFIREKTGAFKPEIGLILGSGLGALADEIENAVVIPYADIPGFPVSTVEGHAGELVLGRL
GGKPVLAMQGRFHYYEGYSMEAVTFPVRVMKALGVETLIVTNAAGGLNPDFGPGDLMLISDHINLTGRNP
LIGPNDDEFGPRFPDMSDAYDPELRALAKKVAKELGIPLQEGVYVGVSGPSYETPAEIRMLRTLGADAVG
MSTVPEVIVARHCGLKVLGISCITNLAAGISDEPLSHEEVLEVAERAAPKFGRLVKAILARL
>gnl|CDD|236184 PRK08203, PRK08203, hydroxydechloroatrazine ethylaminohydrolase; Reviewed
TTLWIKNPLAIVTMDAARREIADGGLVVEGGRIVEVGPGGALPQPADEVFDARGHVVTPGLVNTHHHFYQ
TLTRALPAAQDAELFPWLTTLYPVWARLTPEMVRVATQTALAELLLSGCTTSSDHHYLFPNGLRDALDDQ
IEAAREIGMRFHATRGSMSLGESDGGLPPDSVVEDEDAILADSQRLIDRYHDPGPGAMLRIALAPCSPFS
VSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERFGMRPVDYLEDLGWLGPDVWLAHCVHLDDAEIA
RLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDGSASNDGSNLIGEARQALLLQRLRYGPDA
MTAREALEWATLGGARVLGRDDIGSLAPGKLADLALFDLDELRFAGAHDPVAALVLCGPPRADRVMVGGR
WVVRDGQLTTLDLAALIARHRAAARRLAAGA
>gnl|CDD|181288 PRK08204, PRK08204, hypothetical protein; Provisional
MKRTLIRGGTVLTMDPAIGDLPRGDILIEGDRIAAVAPSIEAPDAEVVDARGMIVMPGLVDTHRHTWQSV
LRGIGADWTLQTYFREIHGNLGPMFRPEDVYIANLLGALEALDAGVTTLLDWSHINNSPEHADAAIRGLA
EAGIRAVFAHGSPGPSPYWPFDSVPHPREDIRRVKKRYFSSDDGLLTLGLAIRGPEFSSWEVARADFRLA
RELGLPISMHQGFGPWGATPRGVEQLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSVTPEIEMMMG
HGYPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRFALQAERARDNAVHLREGGMPPPRLTLTARQVLEW
ATIEGARALGLEDRIGSLTPGKQADLVLIDATDLNLAPVHDPVGAVVQSAHPGNVDSVMVAGRAVKRNGK
LLGVDLERLRRLAAASRDRLLSRRARKAS
>gnl|CDD|236186 PRK08206, PRK08206, diaminopropionate ammonia-lyase; Provisional
MSMFLLKNNIADNKPYDGADLPLLSQEEAKKARAFHQSFPGYAPTPLVALPDLAAELGVGSILVKDESYR
FGLNAFKALGGAYAVARLLAEKLGLDISELSFEELTSGEVREKLGDITFATATDGNHGRGVAWAAQQLGQ
KAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENGWVVVQDTAWEGYEEIPTWIMQGY
GTMADEAVEQLKEMGVPPTHVFLQAGVGSLAGAVLGYFAEVYGEQRPHFVVVEPDQADCLYQSAVDGKPV
AVTGDMDTIMAGLACGEPNPLAWEILRNCADAFISCPDEVAALGMRILANPLGGDPPIVSGESGAVGLGA
LAALMTDPDYQELREKLGLDEDSRVLLISTEGDTDPDRYREIVWEGKYA
>gnl|CDD|236187 PRK08207, PRK08207, coproporphyrinogen III oxidase; Provisional
IKIKLNDERFRYDLQDILNLFFEESEIGFEEEEDADLIIEIDIEENEKVSVKLTDVITGYVFEETFAKDF
SAFLDEKERLKRVVKRVLLSLLKKLTGKELPWGILTGIRPTKILHKLLDEGLSKEEIHKELKEEYLISEE
KAKLLLEIAKRELSFLLYRDKNEVSIYIGIPFCPTRCLYCSFPSYPIKGYKGLVEPYLEALHYEIEEIGK
YLKEKGLKITTIYFGGGTPTSLTAEELERLLEEIYENFPDVKNVKEFTVEAGRPDTITEEKLEVLKKYGV
DRISINPQTMNDETLKAIGRHHTVEDIIEKFHLAREMGFDNINMDLIIGLPGEGLEEVKHTLEEIEKLNP
ESLTVHTLAIKRASRLTENKEKYKVADREEIEKMMEEAEEWAKELGYVPYYLYRQKNMLGNLENVGYAKP
GKESIYNIQIMEEKQTIIGLGAGAVSKFVFPDENRIERFANPKDPKEYIERIDEMIERKIKILEELYG
>gnl|CDD|181292 PRK08208, PRK08208, coproporphyrinogen III oxidase family protein
NNNDPYRSYMYSYPHKTAYRPLEPRPSLSEVWEREYEDALSLYIHIPFCEMRCGFCNLFTRTGADAEFID
SYLDALIRQAEQVAEALAPARFASFAVGGGTPTLLNAAELEKLFDSVERVLGVDLGNIPKSVETSPATTT
AEKLALLAARGVNRLSIGVQSFHDSELHALHRPQKRADVHQALEWIRAAGFPILNIDLIYGIPGQTHASW
MESLDQALVYRPEELFLYPLYVRPLTGLGRRARAWDDQRLSLYRLARDLLLEAGYTQTSMRMFRRNDAPD
KGAPAYSCQTDGMLGLGCGARSYTGNLHYSSPYAVNQQTIRSIIDDYIATPDFTVAEHGYLLSEDEMKRR
FIIKSLLQAQGLDLADYRQRFGSDPLRDFPELELLIDRGWLEQNGGRLRLTEEGLALSDAIGPVFISPEV
RALMAEYEQR
>gnl|CDD|236188 PRK08210, PRK08210, aspartate kinase I; Reviewed
MKIIVQKFGGTSVSTEERRKMAVNKIKKALKEGYKVVVVVSAMGRKGDPYATDTLLSLVGEEFSEISKRE
QDLLMSCGEIISSVVFSNMLNENGIKAVALTGGQAGIITDDNFTNAKIIEVNPDRILEALEEGDVVVVAG
FQGVTENGDITTLGRGGSDTTAAALGVALKAEYVDIYTDVDGIMTADPRIVEDARLLDVVSYNEVFQMAY
QGAKVIHPRAVEIAMQANIPLRIRSTYSDSPGTLITSLGDAKGGIDVEERLITGIAHVSNVTQIKVKAKE
NAYDLQQEVFKALAEAGISVDFINIFPTEVVFTVSDEDSEKAKEILENLGLKPSVRENCAKVSIVGAGMA
GVPGVMAKIVTALSEEGIEILQSADSHTTIWVLVKEEDMEKAVNALHDAFELS
>gnl|CDD|181295 PRK08213, PRK08213, gluconate 5-dehydrogenase; Provisional
MMTVLELFDLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADV
ADEADIERLAEETLERFGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPRG
YGRIINVASVAGLGGNPPEVMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTLER
LGEDLLAHTPLGRLGDDEDLKGAALLLASDASKHITGQILAVDGGVSAV
>gnl|CDD|181296 PRK08215, PRK08215, RNA polymerase sporulation sigma factor SigG
MTRNKVEICGVNTSKLPVLKNEEMRELFERMQNGDKEAREKLINGNLRLVLSVIQRFNNRGENVDDLFQV
GCIGLMKAIDNFDLSQNVKFSTYAVPMIIGEIRRYLRDNNPIRVSRSLRDIAYKALQVREKLINENSKEP
TVEEIAKELEVPREEVVFALDAIQDPVSLFEPIYHDGGDPIYVMDQISDEKNKDENWLEEIALKEAMKKL
NDREKLILNLRFFQGKTQMEVAEEIGISQAQVSRLEKAALKHMRKYIQ
>gnl|CDD|181297 PRK08217, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
MDLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVE
ATFAQIAEDFGQLNGLINNAGILRDGLLVKAKDGKVTSKMSLEQFQSVIDVNLTGVFLCGREAAAKMIES
GSKGVIINISSIARAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKPEALE
RLEKMIPVGRLGEPEEIAHTVRFIIENDYVTGRVLEIDGGLRL
>gnl|CDD|181298 PRK08219, PRK08219, SDR family oxidoreductase
MERPTALITGASRGIGAAIARELAPTHTLLLGGRPAERLDELAAELPGATPFPVDLTDPEAIAAAVEQLG
RLDVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWG
SYAASKFALRALADALREEEPGNVRVTSVHPGRTDTDMQRGLVAQEGGEYDPERYLRPETVAKAVRFAVD
APPDAHITEVVVRPRPR
>gnl|CDD|236190 PRK08220, PRK08220, 2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
MNAMDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYPFATFVLDVSDAAAVAQVCQRL
LAETGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHV
PRIGMAAYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQRTLWVDEDGEQQVIAGFPEQFKLG
IPLGKIARPQEIANAVLFLASDLASHITLQDIVVDGGATLGA
>gnl|CDD|181301 PRK08222, PRK08222, hydrogenase 4 subunit H; Validated
MLKLLKTIMRAGTATVKYPFAPLEVSPGFRGKPDLMPSQCIACGACTCACPANALTIQTDDQQNSRTWQL
YLGRCIYCGRCEEVCPTRAIQLTNNFELTVTNKADLYTRATFHLQRCSRCERPFAPQKTVALAAELLAQQ
QNAPQNREMLRAQASVCPECKQRATLINDDTDVPLVAKEQL
>gnl|CDD|181302 PRK08223, PRK08223, hypothetical protein; Validated
MAPFDYDEAFCRNLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQ
AGAMMSTLGRPKAEVLAEMVRDINPELEIRAFPEGIGKENADAFLDGVDVYVDGLDFFEFDARRLVFAAC
QQRGIPALTAAPLGMGTALLVFDPGGMSFDDYFDLSDGMNEVEKAVRFLAGLAPSMLHRGYLADPSRVDL
ENRTGPSTGLACQLCAGVVATEVLKILLGRGRVYAAPWFHQFDAYRSRYVRTWRPGGNRHPLQRLKRRLL
RRRLNRR
>gnl|CDD|236191 PRK08224, ligC, ATP-dependent DNA ligase; Reviewed
MDLPVMPPVEPMLAKSVDAIPPGDGWSYEPKWDGFRCLVFRDGDEVELGSRNGKPLTRYFPELVAALRAE
LPERCVLDGEIVVARDGGLDFEALQQRIHPAASRVRKLAEETPASFVAFDLLALGDRDLTGRPFAERRAA
LEAAAAGSGPVHLTPATTDPATARRWFEEFEGAGLDGVIAKPLDGPYQPGKRAMFKVKHERTADCVVAGY
RYHKSGPVVGSLLLGLYDDDGQLHHVGVTSAFPMARRRELTAELEPLRTPFGDHPWNWAAFTGRAPGGPS
RWSAGKDLSWVPLRPERVVEVRYDHMEGGRFRHTAQFLRWRPDRDPRSCTYEQLEEPVRYDLADVLPGAR
>gnl|CDD|181304 PRK08225, PRK08225, acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
MTKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE
>gnl|CDD|181305 PRK08226, PRK08226, SDR family oxidoreductase UcpA
MGKLTGKTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGRGHRCTAVVADVRDPASVA
AAIKRAKEKEGRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMS
SVTGDMVADPGETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIARQSNPEDPESVLT
EMAKAIPLRRLADPLEVGELAAFLASDESSYLTGTQNVIDGGSTLPETVSVGI
>gnl|CDD|181306 PRK08227, PRK08227, 3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase
GAGALDWGMKNRLSRIFNPKTGRTVMLAFDHGYFQGPTTGLERIDINIAPLFPYADVLMCTRGILRSVVP
PATNKPVVLRASGGNSILKELSNEAVAVDMEDAVRLNACAVAAQVFIGSEYEHQSIKNIIQLVDAGLRYG
MPVMAVTAVGKDMVRDARYFSLATRIAAEMGAQIIKTYYVEEGFERITAGCPVPIVIAGGKKLPERDALE
MCYQAIDEGASGVDMGRNIFQSEHPVAMIKAVHAVVHENETAKEAYELYLSEKN
>gnl|CDD|236192 PRK08228, PRK08228, L(+)-tartrate dehydratase subunit beta; Validated
MMKKILTTPIKDEDLQDIKVGDVIYLTGTLVTCRDVAHRRLIELGRELPVDLNGGAIFHAGPIVRPKKND
DKFEMVSVGPTTSMRMEKFEKEFIEQTGVKLIVGKGGMGPGTEEGCQEFKALHCVFPAGCAVLAATQVEE
IEDAQWRDLGMPETLWVCRVKEFGPLIVSIDTHGNNLFEENKKLFNERKEPIVEEICEHVHFIK
>gnl|CDD|236193 PRK08229, PRK08229, 2-dehydropantoate 2-reductase; Provisional
MMARICVLGAGSIGCYLGGRLAAAGADVTLIGRARIGDELRAHGLTLTDYRGRDVRVPPSAIAFSTDPAA
LATADLVLVTVKSAATADAAAALAGHARPGAVVVSFQNGVRNADVLRAALPGATVLAGMVPFNVISRGPG
AFHQGTSGALAIEASPALRPFAAAFARAGLPLVTHEDMRAVQWAKLLLNLNNAVNALSGLPLKEELAQRS
YRRCLALAQREALRVLKAAGIRPARLTPLPPAWIPRLLRLPDPLFRRLAGRMLAIDPLARSSMSDDLAAG
RATEIDWINGEIVRLAGRLGAPAPVNARLCALVHEAERAGARPAWSGEALLAELRIAAPAG
>gnl|CDD|181309 PRK08230, PRK08230, tartrate dehydratase subunit alpha; Validated
MNKSQAVNKLTDIMAKFTAYISKRLPDDVTAKLKELKDAETSPLAKIIYDTMFENQQLAIDLNRPSCQDT
GVIQFFVKVGARFPLLGELESILKEAVEEATVKAPLRHNAVETFDEYNTGKNTGSGVPWVFWEIVPDSDD
AEIEVYMAGGGCTLPGRAKVLMPGEGYEGVVKFVFDVITSYGVNACPPLLVGVGIATSVETAAVLSKKAI
LRPIGSRNPNPRAAELEKRLEEGLNRIGLGPQGLTGNSSVMGVNIESAARHPSTIGVAVSTGCWAHRRGT
IVFDADLNYEILSHTGVAL
>gnl|CDD|181310 PRK08233, PRK08233, hypothetical protein; Provisional
KKTKIITIAAVSGGGKTTLTERLTHKLKNSKALYFDRYDFDNCPEDICKWIDKGANYSEWVLTPLIKDIQ
ELIAKSNVDYIIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDTGNEIHNDLKHYLNYAR
PLYLEALHTVKPNADIVLDGALSVEEIINQIEEELYRREVIV
>gnl|CDD|181311 PRK08235, PRK08235, acetyl-CoA C-acetyltransferase
MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAA
RAAGIPWEVQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVI
DLMVADGLTCAFSGVHMGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGD
PIVVAKDEAPRKDTTIEKLAKLKPVFDKTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHT
AIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHP
IGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIEVH
>gnl|CDD|236194 PRK08236, PRK08236, hypothetical protein; Provisional
MKRVLVVTAVPAERDAVLRGLGNDSRFDVLAAGVGPAAAAASTARALAAAAAPYDLVVSAGIAGGFPGKA
EVGSLVVADEIIAADLGAETPDGFLPVDELGFGTTTIQVDPALVRQLTEALLAAALGATAGPVLTVSTVT
GTAETAAALAARHPDAVAEAMEGFGVAEAAAAAGLPVLELRAISNPVGPRDRAAWRIKEALAALTAASSV
LA
>gnl|CDD|236195 PRK08238, PRK08238, UbiA family prenyltransferase
MDDRAQSSRDLPLVVDLDGTLIRTDLLHESIFALLRRNPLALLRLPLWLLRGKAALKRRLARRVDLDVAT
LPYNEEVLDYLRAERAAGRKLVLATASDERLAQAVAAHLGLFDGVFASDGTTNLKGAAKAAALVEAFGER
GFDYAGNSAADLPVWAAARRAIVVGASPGVARAARALGPVERVFPPRPARLRTWLKALRVHQWAKNLLVF
VPLLAAHQFGDLQALLAALLAFLAFSLCASAVYILNDLLDLEADRAHPRKRRRPFASGALPIPFGLAAAP
LLLLAGLALALALGPAFLLVLLAYLALTLAYSLRLKRKVLVDVLTLAALYTLRIIAGAAAIGVALSFWLL
AFSMFFFLSLALVKRYTELRRALQRGKPKIAGRGYRPSDLPLVLSLGVASGYAAVLVLALYINSDAVRAL
YRHPQLLWLACPILLYWISRVWLLAHRGEMHDDPVVFALKDRVSLVVGALCALIFLAAI
>gnl|CDD|236196 PRK08241, PRK08241, RNA polymerase subunit sigma-70
DPATAAAALLARAAAGDRDAFAALVEPHRRELLAHCYRMLGSVHDAEDAVQETLLRAWRGYDRFEGRSSL
RTWLYRIATNVCLDALEGRARRPLPTDLGAPAADPVDELVERPEVPWLEPYPDALLDPAAADPAARVVAR
ESVRLAFVAALQHLPPRQRAVLILRDVLGWSAAEVAELLDTSVAAVNSALQRARATLAERGPSAADTLRE
PDDPEERALLARYVAAFEAYDVDALVALLTEDATWSMPPFPLWYRGRDAIAAFLAGQCPGAGCGGSRLVP
TRANGQPAFAQYMRDPDGGGHRPWALHVLELRGGRIAHVTSFLDTTLFPRFGLPATLPA
>gnl|CDD|236197 PRK08242, PRK08242, acetyl-CoA C-acetyltransferase
MTEAYIYDAVRTPRGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIAR
TAVLAAGLPETVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAMDPSTN
FPTYFVPQGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNGLTILDHDEHMRP
GTTMESLAKLKPSFAMMGEMGGFDAVALQKYPEVERINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLK
PRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVN
GGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATIIERV
>gnl|CDD|236198 PRK08243, PRK08243, 4-hydroxybenzoate 3-monooxygenase; Validated
MRTQVAIIGAGPAGLLLGQLLHLAGIDSVVLERRSREYVEGRIRAGVLEQGTVDLLREAGVGERMDREGL
VHDGIELRFDGRRHRIDLTELTGGRAVTVYGQTEVTRDLMAARLAAGGPIRFEASDVALHDFDSDRPYVT
YEKDGEEHRLDCDFIAGCDGFHGVSRASIPAGALRTFERVYPFGWLGILAEAPPVSDELIYANHERGFAL
CSMRSPTRSRYYLQCPLDDKVEDWSDERFWDELRRRLPPEDAERLVTGPSIEKSIAPLRSFVAEPMQYGR
LFLAGDAAHIVPPTGAKGLNLAASDVRYLARALVEFYREGDTALLDAYSATALRRVWKAERFSWWMTSML
HRFPDDDPFDQRIQLAELDYLTSSRAAATTLAENYVGLPFED
>gnl|CDD|236199 PRK08244, PRK08244, monooxygenase
MKYEVIIIGGGPVGLMLASELALAGVKTCVIERLKETVPYSKALTLHPRTLEILDMRGLLERFLEKGRKL
PSGHFAGLDTRLDFSALDTSSNYTLFLPQAETEKVLEEHARSLGVEIFRGAEVLAVRQDGDGVEVVVRGP
DGLRTLTSSYVVGADGAGSIVRKQAGIAFPGTDATFTAMLGDVVLKDPPPSSVLSLCTREGGVMIVPLSG
GIYRVLIIDPERPQVPKDEPVTLEELKTSLIRICGTDFGLNDPVWMSRFGNATRQAERYRSGRIFLAGDA
AHIHFPAGGQGLNVGLQDAMNLGWKLAAAIKGWAPDWLLDSYHAERHPVGTALLRNTEVQTKLFDFTRPG
LALRSMLSDLLGFPEVNRYLAGQISALDVHYEPDAEMPPHPLNGKRLPDLELTLSDGESERLYSLLHKGT
FLLLSFGSEPQDWSRYPHVRVVRASLAEGRADWNDVHTALIRPDGHVAWAVDASDPNAEEAIAAGISRWC
GVI
>gnl|CDD|236200 PRK08245, PRK08245, hypothetical protein; Validated
MDITRLSPATREALKRVSTATLTTALFKRGLRNQFIRGVRPLRPGGPRMVGPAFTLRFVPAREDLNTPES
FADPESPQRAAIETCPPGCVLVVDARGDARAGSFGDILCTRLKKRGVAGLVTDGGVRDSPGIAALGLPVW
CAGPSAPTNLTGLTAVDINVPIGCGGVAVFPGDIIVADDDGVVVIPAALADEVAAEAVEQERWEDFIREE
VAAGASLPGLYPPNAETKAEYEAWRKKRGR
>gnl|CDD|181319 PRK08246, PRK08246, serine/threonine dehydratase
AHAMITRSDVRAAAQRIAPHIRRTPVLEADGAGFGPAPVWLKLEHLQHTGSFKARGAFNRLLAAPVPAAG
VVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGA
LLCHAYDQPEVLAGAGTLGLEIEEQAPGVDTVLVAVGGGGLIAGIAAWFEGRARVVAVEPEGAPTLHAAL
AAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALA
ALLSGAYVPAPGERVAVVLCGANTDPATLA
>gnl|CDD|181320 PRK08247, PRK08247, methionine biosynthesis PLP-dependent protein
QMSTIETKLAQIGNRSDERTGTVNPPVYFSTAYRHEGIGESTGFDYSRTGNPTRGVLEQAIADLEGGDQG
FACSSGMAAIQLVMSLFRSGDELIVSSDLYGGTYRLFEEHWKKWNVRFVYVNTASLKAIEQAITPNTKAI
FIETPTNPLMQETDIAAIAKIAKKHGLLLIVDNTFYTPVLQRPLEEGADIVIHSATKYLGGHNDVLAGLV
VAKGQELCERLAYYQNAAGAVLSPFDSWLLIRGMKTLALRMRQHEENAKAIAAFLNEQPGVTDVLYPGRG
GMLSFRLQDEEWVNPFLKSLKLITFAESLGGVESFITYPATQTHADIPEEIRIANGVCNRLLRFSVGIEN
VEDLIADLKQAFKQVK
>gnl|CDD|236201 PRK08248, PRK08248, homocysteine synthase
MSEERTFRLETLAIHAGQEIDPTTGSRAVPIYQTTSYGFRDSEHAANLFSLKEFGNIYTRIMNPTTDVFE
KRIAALEGGIGALAVSSGQAAITYSILNIASAGDEIVSSSSLYGGTYNLFAHTLPKLGITVKFVDPSDPE
NFEAAITDKTKALFAETIGNPKGDVLDIEAVAAIAHEHGIPLIVDNTFASPYLLRPIEHGADIVVHSATK
FIGGHGTSIGGVIVDSGKFDWKGSGKFPGLTEPDPSYHGLVYTDAVGEAAYITKARVQLLRDLGAALSPF
NSFLLLQGLETLHLRMERHSENALAVAKFLEEHEAVEWVSYPGLPSHPSYELAKKYLPKGQGAILTFGIK
GGVEAGKKLIDSVKLFSHLANVGDSKSLIIHPASTTHQQLSEEEQLAAGVTPGLVRLSVGTEAIDDILDD
LRQAIRQSQTV
>gnl|CDD|236202 PRK08249, PRK08249, cystathionine gamma-synthase family protein
KMDFNNAGVGTKAVWAGEKEYLPYGATQVPVVLSVAYGYDDIDEWYDVALGKKPGHIYSRNTNPTVQAFE
EKVRILEGAEAATAFSTGMAAISNTLYTFLKPGDRVVSIKDTYGGTNKIFTEFLPRMGVDVTLCETGDHE
QIEAEIAKGCDLLYLETPTNPTLKIVDIERLAAAAKKVGALVVVDNTFATPINQNPLALGADLVIHSATK
FLSGHADALGGVVCGSKELMEQVYHYREINGATMDPMSAYLILRGMKTLKLRVRQQQESAMALAKYLQTH
PKVEAVYYPGLETHPNHEIAKAQMRGFGGILSFVLKGGMDTVKRLLPKLRYAHRAANLGAVETIYGPART
TSHVENTLEERAALGIPEGLVRISVGIEDTEDLIADLEQAFAHLESEL
>gnl|CDD|181323 PRK08250, PRK08250, glutamine amidotransferase; Provisional
MRVHFIIHESFEAPGAYLKWAENRGYDISYSRVYAGEALPENADGFDLLIVMGGPQSPRTTREECPYFDS
KAEQRLINQAIKAGKAVIGVCLGAQLIGEALGAKYEHSPEKEIGYFPITLTEAGLKDPLLSHFGSTLTVG
HWHNDMPGLTDQAKVLATSEGCPRQIVQYSNLVYGFQCHMEFTVEAVELLIAHSQQELSQAQGKRFVQSP
EELRAWDYSEMNQKLFRFLDKLTLA
>gnl|CDD|181324 PRK08251, PRK08251, SDR family oxidoreductase
TRQKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYPGIKVAVAALDVNDHDQVFE
VFAEFRDELGGLDRVIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISS
VSAVRGLPGVKAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAKAKSTPFMVDTETGVKA
LVKAIEKEPGRAAVPWWPWAPLGALMRVLPLRLVRKFA
>gnl|CDD|181325 PRK08252, PRK08252, crotonase/enoyl-CoA hydratase family protein
MSDEVLVERRGRVLIITINRPEARNAVNAAVAQGLAAALDELDADPDLSVGILTGAGGTFCAGMDLKAFA
RGERPSIPGRGFGGLTERPPRKPLIAAVEGYALAGGFELALACDLIVAARDAKFGLPEVKRGLVAAGGGL
LRLPRRIPYHIAMELALTGDMLTAERAHELGLVNRLTEPGQALDAALELAERIAANGPLAVAASKRIVVE
SGDWSEDEMFARQRELIAPVFTSADAKEGATAFAEKRAPVWTGK
>gnl|CDD|236203 PRK08255, PRK08255, bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase
MRIVCIGGGPAGLYFALLMKLLDPAHEVTVVERNRPYDTFGWGVVFSDATLGNLRAADPVSAAAIGDAFN
HWDDIDVHFKGRRIRSGGHGFAGIGRKRLLNILQARCEELGVKLVFETEVPDDQALAADADLVIASDGLN
SRIRTRYADTFQPDIDTRRCRFVWLGTHKVFDAFTFAFEETEHGWFQAHAYRFDDDTSTFIVETPEEVWR
AAGLDEMSQEESIAFCEKLFADYLDGHPLMSNASHLRGSAWINFPRVVCERWVHWNRRVPVVLMGDAAHT
AHFSIGSGTKLALEDAIELARCLHEHPGDLPAALAAYEEERRVEVLRIQNAARNSTEWFENVERYAGLEP
EQFAYSLLTRSQRISHENLRLRDAAWLEGYERWFARRAGAPVARPPPPMFTPFRLRGLTLKNRVVVSPMA
MYSAVDGVPGDFHLVHLGARALGGAGLVMTEMTCVSPEGRITPGCPGLYNDEQEAAWKRIVDFVHANSDA
KIGIQLGHSGRKGSTRLGWEGIDEPLEEGNWPLISASPLPYLPGSQVPREMTRADMDRVRDDFVAAARRA
AEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDW
VEGGNTPDDAVEIARAFKAAGADLIDVSSGQVSKDEKPVYGRMYQTPFADRIRNEAGIATIAVGAISEAD
HVNSIIAAGRADLCALARPHLADPAWTLHEAAEIGYRDVAWPKQYLAGKRQLERNLERAAAPALQ
>gnl|CDD|181327 PRK08256, PRK08256, lipid-transfer protein; Provisional
NKVFVAGVGMTPFEKPGASWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYGDSTSGQRALYEVGMTG
IPIVNVNNNCSTGSTALFLARQAVRSGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFD
PAPPALRMFGGAGREHMEKYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQC
CPPTCGAAAAIVCSEEFARKHGLDRAVEIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIG
PEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFIDDGDNTYGGRWVVNPSGGLLSKGHPLGATGLAQC
AELTWQLRGTAGARQVEGARLALQHNLGLGGACVVTLYQRA
>gnl|CDD|236204 PRK08257, PRK08257, acetyl-CoA acetyltransferase; Validated
VDPRTPVIVGVGQVTERPDDPAYGLEPVDLMAAAARAAAADAGADAVLEAIDSVAVVNQLSWRYRDPPGL
LAERLGADPARTVYSPVGGNSPQRLVNEAALRIAAGEADVALVAGAEAQSTATKLRKAGEKLDWTPQDEG
PLADRGGDPRPMASPAELRHGLDRPVYVYPLFENALRAALGRSPEEHRAEMGELWAPFSAVAAKNPHAWI
PRERSAEEIVTPTPDNRMIAWPYTKLMNANDMVDQGAAVLLTSVAKARRLGVPEDRWVYLHGGADAHDPY
DILERPDLHRSPAIRAAGRRALALAGLGIDDIDAFDLYSCFPSAVQVAARELGLDLDDPRPLTVTGGLPF
FGGPGNNYVTHAIAEMVERLRANPGRRGLVTANGGYLTKHSVGVYSTEPPAGWRLEDSASVQAEVDAEPT
PEVVVEASGRATVETYTVVYGRDGEPEKGIVIGRTPDGARTLAVTEDPALLAALVDRDPVGAKVAVRADG
DGNLATRA
>gnl|CDD|181329 PRK08258, PRK08258, enoyl-CoA hydratase family protein
MSPFRGSKRPLAGYEARHFLWEVDDGVATITLNRPERKNPLTFESYAELRDLFRELVYADDVKAVVLTGA
GGNFCSGGDVHEIIGPLTKMDMPELLAFTRMTGDLVKAMRACPQPIIAAVDGVCAGAGAILAMASDLRLG
TPSAKTAFLFTRVGLAGADMGACALLPRIIGQGRASELLYTGRSMSAEEGERWGFFNRLVEPEELLAEAQ
ALARRLAAGPTFAHGMTKTMLHQEWDMGLEEAIEAEAQAQAICMQTEDFRRAYEAFVAKRKPVFEGD
>gnl|CDD|236205 PRK08259, PRK08259, crotonase/enoyl-CoA hydratase family protein
MSMSVRVERNGPVTTVILNRPEVRNAVDGPTAAALADAFRAFDADDAASVAVLWGAGGTFCAGADLKAVG
TGRGNRLHPSGDGPMGPSRMRLSKPVIAAVSGYAVAGGLELALWCDLRVAEEDAVFGVFCRRWGVPLIDG
GTVRLPRLIGHSRAMDLILTGRPVDADEALAIGLANRVVPKGQARAAAEELAAELAAFPQTCLRADRLSA
LEQWGLPEEAALANEFAHGLAVLAAEALEGAARFAAGAGRHGAF
>gnl|CDD|236206 PRK08260, PRK08260, enoyl-CoA hydratase; Provisional
MTYETIRYDVADGIATITLNRPDKLNAFTVTMARELIEAFDAADADDAVRAVIVTGAGRAFCAGADLSAG
GNTFDLDAPRTPVEADEEDRADPSDDGVRDGGGRVTLRIFDSLKPVIAAVNGPAVGVGATMTLAMDIRLA
STAARFGFVFGRRGIVPEAASSWFLPRLVGLQTALEWVYSGRVFDAQEALDGGLVRSVHPPDELLPAARA
LAREIADNTSPVSVALTRQMMWRMAGADHPMEAHRVDSRAIYSRGRSGDGKEGVSSFLEKRPAVFPGKVS
HDMPDFFPWWDEPEFK
>gnl|CDD|236207 PRK08261, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
SDRYLQFVNSGLGKFLAKKLGLPQPVPLRRYRPGQPLLDGPVLVGGAGRLAEALAALLAGLGYDVVANND
GGLTWAAGWGDRFGALVFDATGITDPADLKALYEFFHPVLRSLAPCGRVVVLGRPPEAAADPAAAAAQRA
LEGFTRSLGKELRRGATAQLVYVAPGAEAGLESTLRFFLSPRSAYVSGQVVRVGAADAAPPADWDRPLAG
KVALVTGAARGIGAAIAEVLARDGAHVVCLDVPAAGEALAAVANRVGGTALALDITAPDAPARIAEHLAE
RHGGLDIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGN
RGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMTAAIPFATREAGRRMNSLQQGGLPVDV
AETIAWLASPASGGVTGNVVRVCGQSLLGA
>gnl|CDD|236208 PRK08262, PRK08262, M20 family peptidase
LRRILLGLLALLLLLAAVLAVRTFRFKSRQIDVPAVAPVAVDEDAAAERLSEAIRFRTISNRDRAEDDAA
AFDALHAHLEESYPAVHAALEREVVGGHSLLYTWKGSDPSLKPIVLMAHQDVVPVAPGTEGDWTHPPFSG
VIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVGGLGARAIAELLKERGVRLA
FVLDEGGAITEGVLPGVKKPVALIGVAEKGYATLELTARATGGHSSMPPRQTAIGRLARALTRLEDNPLP
MRLRGPVAEMFDTLAPEMSFAQRVVLANLWLFEPLLLRVLAKSPETAAMLRTTTAPTMLKGSPKDNVLPQ
RATATVNFRILPGDSVESVLAHVRRAVADDRVEIEVLGGNSEPSPVSSTDSAAYKLLAATIREVFPDVVV
APYLVVGATDSRHYSGISDNVYRFSPLRLSPEDLARFHGTNERISVANYARMIRFYYRLIENAAGL
>gnl|CDD|181334 PRK08263, PRK08263, short chain dehydrogenase; Provisional
MMEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVET
AVEHFGRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGI
SAFPMSGIYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWAGTSAKRATPLDAYDTLREELAEQ
WSERSVDGDPEAAAEALLKLVDAENPPLRLFLGSGVLDLAKADYERRLATWEEWEAVSRAAQGAI
>gnl|CDD|181335 PRK08264, PRK08264, SDR family oxidoreductase
MMDIKGKVVLVTGANRGIGRAFVEQLLARGAAKVYAAARDPESVTDLGPRVVPLQLDVTDPASVAAAAEA
ASDVTILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNF
PNLGTYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGLDAPKASPADVARQILDALEAGDE
EVLPDEMARQVKAALSADPKNYEEQLAG
>gnl|CDD|236209 PRK08265, PRK08265, short chain dehydrogenase; Provisional
MIGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERA
VATVVARFGRVDILVNLACTYLDDGLASSRADWLAALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISA
KFAQTGRWLYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDELSGGDRAKADRVAAPFHLLG
RVGDPEEVAQVVAFLCSDAASFVTGADYAVDGGYSALGPEQGVPAIPRLAE
>gnl|CDD|181337 PRK08266, PRK08266, hypothetical protein; Provisional
MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIRVIHTRHEQAAGYMAFGYARSTGRPG
VCSVVPGPGVLNAGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHLHEMPDQLATLRSFTKWAERIEHPS
EAPALVAEAFQQMLSGRPRPVALEMPWDVFGQRAPVAAAPPLRPAPPPAPDPDAIAAAAALIAAAKNPMI
FVGGGAAGAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLGLNFAAAYELWPQTDVVIGIGSRLELPTFR
WPWRPDGLKVIRIDIDPTEMRRLKPDVAIVADAKAGTAALLDALSKAGSKRPSRRAELRELKAAARQRIQ
AVQPQASYLRAIREALPDDGIFVDELSQVGFASWFAFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPD
RPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFGGRVVASDLVNPDFVKLAES
FGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVPRGSEASPWPFIHPAPPA
>gnl|CDD|236210 PRK08267, PRK08267, SDR family oxidoreductase
MKSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNAWTGALDVTDRAAWDAALADF
AAATGGRLDVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAI
YGQPGLAVYSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAGSTKRLGVRLTPED
VAEAVWAAVQHPTRLHWPVGKQAKLLAFLARLSPGFVRRLINKSLARPRK
>gnl|CDD|236211 PRK08268, PRK08268, 3-hydroxy-acyl-CoA dehydrogenase; Validated
MMALPSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADA
ALARLRPVEALADLADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERV
AGLHFFNPVPLMKLVEVVSGLATDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEE
GVADPATIDAILREAAGFRMGPFELMDLIGLDVNHAVMESVYRQFYQEPRFRPSLIQQELVAAGRLGRKS
GQGFYRYADGAKQPPAEAAPPAALPPVWVSADVEGDLAALARLLERLGATIETGEGPSADGLVLLAPTGG
DTTTAAAREGLDAARVVLIDLLLDYAAAKRRTLMAAPATSPAARDAAHALFQQDGKAVSVIRDSPGFVAQ
RTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWGDRLGAARILRVLENLQALYGDPRYRPSP
WLRRRAALGLSLRSEEA
>gnl|CDD|181340 PRK08269, PRK08269, 3-hydroxybutyryl-CoA dehydrogenase; Validated
MGQGIALAFAFAGHDVTLIDFKPRDAAGWRALDAEARAEIERTLAALVALGRIDAAQADAVLARIAVVAR
DGAADALADADLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLN
PAYLMPLVEVSPSDATDPAVVDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAED
IDKAIRTGFGLRFAVLGLLEFIDWGGCDILYYASRYLAGEIGPDRFAPPAIVVRNMEEGRDGLRTGAGFY
DYAGVDVPAYRRQRLGEFARLLDHLGLAPAFDGA
>gnl|CDD|236212 PRK08270, PRK08270, ribonucleoside triphosphate reductase
MPTKIIKRDGRIVPFDAEKITEAIAKAFKATGEFDPSEAERLALRVIEKLEDEDIPSVEEIQDIVEKVLI
EAGYFKTAKAYILYREQHARLRNDKKTLLDVEDTVDEYLDREDWRVNENSNMGYSLQGLILNISGKVTAN
YWLNKVYPPEIGEAHRNGDLHIHDLDMLSGYCAGWSLRDLLLEGFNGVPGKVESKPPKHFRSALGQIVNF
LGTLQNEWAGAQAFSSFDTYLAPFVRKDGLSYKEVKQAIQEFVFNLNVPSRWGFQTPFTNLTFDLTVPED
LKDQPVIIGGEEMDFTYGDFQKEMDMINRAFIEVMLEGDANGRVFTFPIPTYNITKDFDWDSENADLLFE
MTAKYGLPYFQNFINSDLKPEDVRSMCCRLQLDLRELRKRGGGLFGSAELTGSIGVVTINLPRLGYLSKD
EEEFFARLDELMDLAKDSLEIKRKVIERLTDKGLYPYTKRYLGTLRNHFSTIGLNGMNEACLNFLGKDIT
TEEGRAFALRVLDHMRERLVEFQEETGNLYNLEATPAEGTTYRLAKEDKKRYPDIITAGTDEEPYYTNST
QLPVGYTDDPFEALELQDELQTKYTGGTVFHLYLGEAISDAEACKKLVKKALENYRLPYITITPTFSICP
KHGYLSGEHEFCPKCGEETEVYSRVV
>gnl|CDD|181342 PRK08271, PRK08271, anaerobic ribonucleoside triphosphate reductase; Provisional
MKVQVSFEPGFEELYSKLKSKYGYEMLRLEGIQIQLKVGFISEYFFAKNAADGSKIDANANVRHKNIATY
EAELMKDFFKLINRYLVWNKIKELFGKELADEYLRQIENHEIYVHDETSLKPYCFSYTMYPILEDGLTKI
GGESKAPKHLSSFCGSFINFVFAVSSQFAGAVATVEFLVYFDYFARKDYGDDYLPTHRKEIENHLQIVVY
SLNQPAAARGYQSVFWNISYYDRNYFKAMFGGFVYPDGSTPNWEDIIALQKFFMEWFNKEREKAMLTFPV
VTAALLTDDGKCKDEDFADFIAKENSKGNSFFIYISDSADSLASCCRLRNEISDNGFSYSLGAGGVNTGS
INVITINLPRIAQEARDRDDFLEILRERVDKIHKYQLAYREIMEERIAAGMLPLYDAGFISLDKQFLTIG
INGMVEAAEFMGLTVGYNEEYKDFVQEVLKVIYEANEKASKEYGFTFNTEFVPAENLGVKLAKWDREDGY
GVPRQCYNSYSYVVEDANTDALDKFKLHGKELDKYLSGGSALHLNLDERLSEEGYRKLLNIAAKTGCNYF
AFNVKITICNDCHHIDKRTGKRCPICGSENIDYYTRVIGYLKRVSAFSKVRQKEYPRRHYHRS
>gnl|CDD|236213 PRK08272, PRK08272, crotonase/enoyl-CoA hydratase family protein
IRPVDLDNLKTMTYEVTGRIARITLNRPEKGNAITADTPLELRAAVERADLDPGVHVILVSGAGKGFCAG
YDLSAYAEGSSSGGGGGAYPGKRQAVNHLPDDPWDPMIDYQMMSRFVRGFMSLWHAHKPTVAKVHGYCVA
GGTDIALHCDQVIAADDAKIGYPPTRVWGVPATGMWAYRLGPQRAKRLLFTGDCITGAQAAEWGLAVEAV
PPEELDERTERLVERIAAVPVNQLAMVKLAVNSALLQQGVATSQMLATVFDGIARHTPEGHAFKADAAEH
GFKEAVRERDEPFGDGGRRLSR
>gnl|CDD|181344 PRK08273, PRK08273, thiamine pyrophosphate protein; Provisional
MSQTVADFILERLREWGVRRVFGYPGDGINGLLGALGRADDKPEFVQARHEEMAAFMAVAHAKFTGEVGV
CLATSGPGAIHLLNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVAGAFVQMVTVPEQLR
HLVDRAVRTALAERTVTAVILPNDVQELEYEPPPHAHGTVHSGVGYTRPRVVPYDEDLRRAAEVLNAGRK
VAILVGAGALGATDEVIAVAERLGAGVAKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVG
SSFPYSEFLPKEGQARGVQIDIDGRMLGLRYPMEVNLVGDAAETLRALLPLLERKKDRSWRERIEKWVAR
WWETLEARAMVPADPVNPQRVFWELSPRLPDNAILTADSGSCANWYARDLRMRRGMMASLSGTLATMGPA
VPYAIAAKFAHPDRPVIALVGDGAMQMNGMAELITVAKYWRQWSDPRLIVLVLNNRDLNQVTWEQRVMEG
DPKFEASQDLPDVPYARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVKTDPNVPPLPPHITLEQ
AKAFASALLKGDPDAGGVIVQTAKQVLQEVLPGKGER
>gnl|CDD|236214 PRK08274, PRK08274, FAD-dependent tricarballylate dehydrogenase TcuA
MASMVDVLVIGGGNAALCAALAAREAGASVLLLEAAPREWRGGNSRHTRNLRCMHDAPQDVLVGAYPEEE
FWQDLLRVTGGRTDEALARLLIRESSDCRDWMRKHGVRFQPPLSGALHVARTNAFFWGGGKALVNALYRS
AERLGVEIRYDAPVTALELDDGRFVGARAGSAAGGAERIRAKAVVLAAGGFESNREWLREAWGQPADNFL
VRGTPYNQGDLLKALLDAGADRIGDPSQCHAVAIDARAPLYDGGICTRIDCVPLGIVVNRDGERFYDEGE
DFWPKRYAIWGRLVAQQPGQIAYQIFDAKAIGRFMPPVFPPIQADTLEELAEKLGLDPAAFLRTVAAFNA
AVRPGPFDPTVLDDCGTEGLTPPKSHWARPIDTPPFYAYPVRPGITFTYLGLKVDEDARVRFADGRPSPN
LFAAGEMMAGNVLGKGYPAGVGLTIGAVFGRIAGEEAARHAQHEAA
>gnl|CDD|181346 PRK08275, PRK08275, putative oxidoreductase; Provisional
DAMNTQEVETDILVIGGGTAGPMAAIKAKERNPALRVLLLEKANVKRSGAISMGMDGLNNAVIPGHATPE
QYTKEITIANDGIVDQKAVYAYAEHSFETIQQLDRWGVKFEKDETGDYAVKKVHHMGSYVLPMPEGHDIK
KVLYRQLKRARVLITNRIMATRLLTDADGRVAGALGFDCRTGEFLVIRAKAVILCCGAAGRLGLPASGYL
FGTYENPTNAGDGYAMAYHAGAELANLECFQINPLIKDYNGPACAYVTGPLGGYTANAKGERFIECDYWS
GQMMWEFYQELQSGNGPVFLKLDHLAEETIQTIETILHTNERPSRGRFHEGRGTDYRQQMVEMHISEIGF
CSGHSASGVWVNEKAETTVPGLYAAGDMASVPHNYMLGAFTYGWFAGENAAEYVAGRDLPEVDAAQVEAE
RARVLAPLHREDGLPPAQVEYKLRRLVNDYLQPPKVTRKMEIGLQRFAEIREDLERIKARDPHELMRALE
VSSIRDCAEMAARASLFRTESRWGLYHYRVDFPERNDAEWFCHTHLRKDEDGRMVSFKRPVEPY
>gnl|CDD|236215 PRK08276, PRK08276, long-chain-fatty-acid--CoA ligase; Validated
PAVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHL
TAAEIAYIVDDSGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADET
AGADMLYSSGTTGRPKGIKRPLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALA
LGGTVVVMEKFDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVKR
AMIDWWGPIIHEYYASSEGGGVTVITSEDWLAHPGSVGKAVLGEVRILDEDGNELPPGEIGTVYFEMDGY
PFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADV
AVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL
RDRYWEGRQRAI
>gnl|CDD|236216 PRK08277, PRK08277, D-mannonate oxidoreductase; Provisional
MMPNLFSLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLD
KESLEQARQQILEDFGPCDILINGAGGNHPKATTDNEFHELIEPTKTFFDLDEEGFEFVFDLNLLGTLLP
TQVFAKDMVGRKGGNIINISSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE
QNRALLFNEDGSLTERANKILAHTPMGRFGKPEELLGTLLWLADEKASSFVTGVVLPVDGGFSAYSGV
>gnl|CDD|181349 PRK08278, PRK08278, SDR family oxidoreductase
MMSLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEPHPKLPGTIHTAAEEIEAAGGQALPLVGD
VRDEDQVAAAVAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSE
NPHILTLSPPLNLDPKWFAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWPRTTIATAAVRNLLGGD
EAMRRSRTPEIMADAAYEILSRPAREFTGNFLIDEEVLREAGVTDFSRYAVDPGAPLMPDLFV
>gnl|CDD|236217 PRK08279, PRK08279, long-chain-acyl-CoA synthetase; Validated
TITLMDLAARLPRRLPDLPGILRGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNA
RANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIV
GEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTAKDTAFYIYTSGT
TGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRF
WDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEG
NVGFINVFNFDGTVGRVPLWLAHPYAIVKYDVDTGEPVRDADGRCIKVKPGEVGLLIGRITDRGPFDGYT
DPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEA
VVYGVEVPGTDGRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK
EGFDPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAGKFRL
>gnl|CDD|181352 PRK08285, cobH, precorrin-8X methylmutase; Reviewed
MLDYIRDGAEIYRQSFATIRAEADLSRFPADLEKVAVRMIHACGMVDVADDLAFSPGAVAAARAALAAGA
PILCDARMVAEGITRARLPADNEVICTLRDPRVPELAAELGNTRSAAALELWRPRLAGSVVAIGNAPTAL
FRLLEMLDAGAPRPAAILGFPVGFVGAAESKDALAADSRGVPYLIVRGRRGGSAMAAAAVNALASERE
>gnl|CDD|181353 PRK08286, cbiC, cobalt-precorrin-8 methylmutase
MNYIQQPQKIEEKSFEIIQEIIDETRPDYRFASPLEEAIIKRVIHTTADFDWLDILWFSPDALEKIIDAL
RNPCTIYTDTTMALSGINKRLLDTLGCEYRCYISDPRVVELAKEQGITRSMAAVDIAAAEEGPKLFVFGN
APTALFRLLEMVEHGQLQVDAVVGVPVGFVGAAESKEALTESDLPAIAALGRKGGSNVAAAIVNAILYHL
REAQ
>gnl|CDD|181354 PRK08287, PRK08287, decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase
MKDELFLRGEKVPMTKEEVRALALSKLELHRAKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRL
IKENRQRFGCGNIDIIPGEAPIELPGKADAIFIGGSGGNLTAIIDWSLAHLHPGGRLVLTFILLENLHSA
LAHLEKCGVSELDCVQLQVSSLTPLGAGHYFKPNNPTFIISCQKEEN
>gnl|CDD|236219 PRK08289, PRK08289, glyceraldehyde-3-phosphate dehydrogenase; Reviewed
MTMSPEKHLQDWQEREELAEAMIPLIGKLYRNKNVVVSLYGRSLINRSVIDILKAHRFARRIVGKELSVR
ETFPILEALSKLDLGPARVDIGKLAVKYKAEGDGSDVEAFVAEELADAVGGADDIEPRDVVLYGFGRIGR
LLARLLIEKTGGGNGLRLRAIVVRKGSEGDLEKRASLLRRDSVHGPFNGTITVDEENNAIIANGNYIQVI
YANSPEEVDYTAYGINNALVVDNTGKWRDEEGLSQHLKSKGVAKVLLTAPGKGDIKNIVHGVNHSDITDE
DKIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRSAPLNMVITETGAA
KAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSLHSPLQNQIDYTDSTEVV
SSDFVGSRHAGVVDSQATIVNGNRAVLYVWYDNEFGYSCQVVRVMEQMAGVRYPTYP
>gnl|CDD|236220 PRK08290, PRK08290, enoyl-CoA hydratase; Provisional
MEYEYVRYEVAGRIARITLNRPEARNAQNRQMLYELDAAFRRAEADDAVRVIVLAGAGKHFSAGHDLGSG
TPGRDRDPGPDQHPTLWWDGATKPGVEQRYAREWEVYLGMCRRWRDLPKPTIAQVQGACIAGGLMLAWVC
DLIVASDDAFFSDPVVRMGIPGVEYFAHPWELGPRKAKELLFTGDRLTADEAHRLGMVNRVVPRDELEAE
TLELARRIAAMPPFGLRLTKRAVNQTLDAQGFRAALDAVFDLHQLGHAHNAEVGGDRLGGADARGMADAR
KAAAAKPA
>gnl|CDD|236221 PRK08291, PRK08291, cyclodeaminase
MSPMTILTEAELRALVPLDLDAIDCVEAAFAALATGAVAMPPILRLDIPEHRGEVDVKTAYIPGLDSFAI
KVSPGFFDNPKLGLPSLNGLMVVLSARTGLVEALLLDNGYLTDVRTAAAGAVAARHLAREDASRAAVIGA
GEQARLQLEALTLVRPIREVRVWARDAAKAEAYAADLRAELGIPVTVARDVHEAVAGADIIVTTTPSEEP
ILKAEWLHPGLHVTAMGSDAEHKNEIAPAVFAAADLYVCDRLSQTRRLGELHHAIAAGLVAADAVFPELG
QVIAGRRPGRTSDDDITICDLTGTGVQDTAIATLALARARAAGAGTIFEN
>gnl|CDD|236222 PRK08292, PRK08292, AMP nucleosidase; Provisional
PPMPAKESFLDPAAAVDRLEALYERSTAALRDAFAAYIRGGELPDERARAYGLFVYPELRVTTDGSTPVP
DSTRAYGRVAHPGVYSTTVTRPDLFRDYLREQLRLLMQNYGVPIEVGPSQQPIPYPYVIDEGSHLELDRS
MSAGLADHFPTPDLAQIGDEIADGTYEPHPGEPLPLALFDAQRVDFSLARLRHYTGTPPEHFQPFVLFTN
YQRYVDEFVRWGREQLADPDSPYTALVEPGGVVITAETEAPEAAISDLAWRLPQMPAYHLIRADGQGITL
VNIGVGPSNAKTITDHLAVLRPHAWLMIGHCGGLRNSQRIGDYVLAHAYLRDDHVLDAVLPPWIPIPAIA
EVQVALEDAVAEVTGLPGEELKRRMRTGTVVTTDDRNWELRYSASALRFNQSRAVALDMESATIAANGYR
FRVPYGTLLCVSDKPLHGEIKLPGQANAFYEGAVSQHLQIGIRAIELLRAEGDRLHSRKLRSFDEPPFR
>gnl|CDD|181359 PRK08293, PRK08293, 3-hydroxyacyl-CoA dehydrogenase
MDIKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEATKEAPAEAALN
RITLTTDLAEAVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLA
LHFANEIWKNNTAEIMGHPGTDPEVFDTVVAFAKAIGMVPIVLKKEQPGYILNSLLVPFLSAALALWAKG
VADPETIDKTWMIATGAPMGPFGILDIVGLDTAYNITSNWAEATDDENAKKAAALLKEYIDKGKLGVATG
EGFYNYP
>gnl|CDD|236223 PRK08294, PRK08294, phenol 2-monooxygenase; Provisional
MQFHLNGYVPGDPRIQPAAGRGINRPADLPDEVDVLIVGCGPAGLTLAAQLSAFPDITTRIVERKPGRLE
LGQADGIACRTMEMFQAFGFAERILKEAYWINETAFWKPDPADPSTIVRTGRVQDTEDGLSEFPHVIVNQ
ARVHDYFLDVMRNSPTRLEPDYGREFVDLEVDEEGEYPVTVTLRRTDGEHEGEEETVRAKYVVGCDGARS
RVRKAIGRELRGDSANHAWGVMDVLAVTDFPDIRLKCAIQSASEGSILLIPREGGYLVRLYVDLGEVPPD
ERVAVRNTTVEEVIAKAQRILHPYTLDVKEVAWWSVYEVGQRLTDRFDDVPAEEAGTRLPRVFIAGDACH
THSAKAGQGMNVSMQDGFNLGWKLAAVLSGRSPPELLHTYSAERQAIAQELIDFDREWSTMMAAPPKEGG
GVDPAELQDYFVKHGRFTAGTATHYAPSLLTGEATHQDLATGFPIGKRFHSAPVIRLADAKPVHLGHAAT
ADGRWRIYAFADAADPAGPGSALDALCEFLAESPDSPLRRFTPSGADIDAVIDVRAIFQQPHRELDLEDV
PALLLPRKGRFGLTDYEKVFCADLSGADIFDLRGIDRDRGAVVVVRPDQYVANVLPLDAHAELAAFFAGF
LLAR
>gnl|CDD|181361 PRK08295, PRK08295, RNA polymerase sporulation sigma factor SigH
LRMKDYDELEDEELVELARSGDKEALEYLIEKYKNFVRAKARSYFLIGADREDIVQEGMIGLYKAIRDYD
KDKLSSFKSFAELCITRQIITAIKTANRQKHIPLNSYVSLDKPIYDEESDRTLLDVISEAKVTDPEELII
SKEELEDIEEKIEELLSELEKEVLELYLDGKSYQEIAEELNRHVKSIDNALQRVKRKLEKYLENREIT
>gnl|CDD|181362 PRK08296, PRK08296, hypothetical protein; Provisional
ANKRFPKPFEVPTPAGAEGWEEMYPYYLVFQEERREKEEERFWFYDSMHWPEPMYPFDTITGEAAYLALG
QYNARIFSIPPANGIDFRVLNGYVYISPVPVTDPEEIGERVPLFQERAGFYYQNWDPLYAKWKEKVLAII
KELEALEFPPLPDVEPEEVVFEGRGEAGSYDLLESYDRLIDLLFRAWQYHFEFLNLGYAAYLTFYDFCKQ
LFPDIPDQHITEMVAGIDVIMFRPDDELKRLARLAVELGIADIFASGDSPQEIEAALARSPGGREWLAEW
EEAKDPWFYFSTGTGFYHHDKSWIDDLEIPLGYIKDYIGRLRRGETIERPTEALRAERDRIVEEYRDLLD
GDERKAFDELLGLARTVYPYVENHNFYVEHWFMSVFWRKVRELGKLLVKHGFLEEVDDIFYLNRTEVLQA
LFDLVTAWAVGGPPRGPAYWPEEIARRKAIMEKLRSWSPPPALGVPPEVITEPFTIMLWGITTERVQDWL
GLEDGAEGELKGFAASPGVVEGPARVIRSADELSEVQEGEILVCPVTSPSWAPIFAKIKATVTDIGGVMS
HAAIVCREYGLPAVVGTGNATKRIKTGQRLRVDGTKGVVTILD
>gnl|CDD|236225 PRK08298, PRK08298, cytidine deaminase; Validated
MNIEQALYDVAKQLIEQRYPNGWGGAAAMRVEDGTILTSVAPEVINASTELCMETGAICEAHKLQKRVTH
SICVARENEHSELKVLSPCGVCQERLFYWGPDVMCAVTNADDPTDIIFKPLKELQPYHWTEAYHDE
>gnl|CDD|236226 PRK08299, PRK08299, NADP-dependent isocitrate dehydrogenase
MAKIKVKNPVVELDGDEMTRIIWKFIKDKLILPYLDIDLEYYDLGIENRDATDDQVTIDAANAIKKYGVG
VKCATITPDEARVKEFNLKKMWKSPNGTIRNILGGTVFREPIICKNVPRLVPGWTKPIVIGRHAYGDQYR
ATDFKVPGKGKLTLVFTGEDGEPIEHEVHDFPGAGVAMGMYNLDESIRDFARASFNYGLDRKYPVYLSTK
NTILKAYDGRFKDIFQEVYEAEFKEKFEAAGITYEHRLIDDMVASALKWEGGYVWACKNYDGDVQSDTVA
QGFGSLGLMTSVLMTPDGKTVEAEAAHGTVTRHYRQHQKGEETSTNPIASIFAWTRGLAHRGKLDGNPEL
VKFADTLEKVCIETVESGFMTKDLALLVGPDQKWLTTEEFLDAIDENLEKAL
>gnl|CDD|236227 PRK08300, PRK08300, acetaldehyde dehydrogenase; Validated
MMSKLKVAIIGSGNIGTDLMIKILRSEHLEPGAMVGIDPESDGLARARRLGVATSAEGIDGLLAMPEFDD
IDIVFDATSAGAHVRHAAKLREAGIRAIDLTPAAIGPYCVPAVNLDEHLDAPNVNMVTCGGQATIPIVAA
VSRVAPVHYAEIVASIASKSAGPGTRANIDEFTETTSRAIEKVGGAARGKAIIILNPAEPPLIMRDTVYC
LVDEDADQDAIEASVHAMVAEVQAYVPGYRLKQEPQFDRTFDGLRVTVFLEVEGAGDYLPAYAGNLDIMT
AAALAVAERIAQHLLAGAAAAA
>gnl|CDD|236228 PRK08301, PRK08301, RNA polymerase sporulation sigma factor SigE
LRLRLLWYKLLLKLGLKTDEIYYIGGSEALPPPLSKEEEEYLLNKLPKGDEAVRSLLIERNLRLVVYIAR
KFENTGINIEDLISIGTIGLIKAVNTFNPEKKIKLATYASRCIENEILMYLRRNNKVKAEVSFDEPLNID
WDGNELLLSDVLGTDNDIIYKDIEDEVDRKLLKKALKKLSDREKQIMELRFGLNGGEEKTQKEVADMLGI
SQSYISRLEKRIIKRLKKEINKMV
>gnl|CDD|236229 PRK08303, PRK08303, short chain dehydrogenase; Provisional
PMMKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTRARRSEYDRPETIEETAELVTAAGGRGI
AVQVDHLVPEQVRALVERIDREQGRLDILVNDIWGGEKLFEWGKPVWEHSLDKGLRMLRLAIDTHLITSH
FALPLLIRRPGGLVVEITDGTAEYNATHYRLSVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPGWLRS
EMMLDAFGVTEENWRDALAKEPHFAISETPRYVGRAVAALAADPDVARWNGQSLSSGQLARVYGFTDLDG
SRPDAWRYLVEVQDAGKPADVTGYR
>gnl|CDD|236230 PRK08304, PRK08304, stage V sporulation protein AD; Validated
AMKKIGKQTWVFENPPYIISTGTIVGPKEGEGPLGKYFDKILDDDYCGEKSWEKAERKMMEDAIQQALQK
ANLKKSDIDYLLAGDLLNQIISANFAARELGIPFLGLYGACSTMMESLALGSMLIDGGFADRVLAATSSH
FATAERQFRFPTEYGGQRPPTAQWTVTGAGAVLLSREGSGPRITHATIGKVVDLGIKDPNDMGAAMAPAA
ADTIQQHFKDTGRSPEDYDLIVTGDLGRVGREILKELLKEEGYDIGDNYNDCGLMIYDSEQQDVFAGGSG
CACSAVVTYGYLLKELQKGKLKRVLVVATGALLSPTSSQQGESIPGIAHAVVIERVK
>gnl|CDD|181370 PRK08305, spoVFB, dipicolinate synthase subunit B; Reviewed
MSLKGKRIGFGLTGSHCTYDEVMPEIEKLVDEGAEVTPIVSYTVQTTDTRFGKAEEWIKKIEEITGNKVI
NTIVEAEPLGPKKLLDCMVIAPCTGNTMAKLANAITDSPVLMAAKATLRNQRPVVLAISTNDALGLNAKN
LGRLLNTKNIYFVPFGQDDPVKKPNSLVARMDLLIDTVEEALEGKQLQPVLIEYFR
>gnl|CDD|181371 PRK08306, PRK08306, dipicolinate synthase subunit DpsA
TGKHIAVIGGDARQLELIRKLVELGAKVSLVGFDQLDHGFTGATKSSSLEEALSDVDVIILPVPGTNDEG
NVDTVFSNEKLVLTEELLELTPEHCTIFSGIANPYLKELAKETNRKLVELFERDDVAILNSIPTAEGAIM
MAIEHTPITIHGSNVLVLGFGRTGMTLARTLKALGANVTVGARKSAHLARITEMGLSPFHLSELAEEVGK
IDIIFNTIPALVLTKEVLSKMPPEALIIDLASKPGGTDFEYAEKRGIKALLAPGLPGKVAPKTAGQILAN
VLSQLLAEDLIARKEN
>gnl|CDD|181372 PRK08307, PRK08307, stage III sporulation protein SpoAB; Provisional
MKLLGAVLIIAASTWIGFLYAKRYKERPRQLRELKAALQSLEAEIMYGHTPLPEALENIAKQSPKPISTL
FQRFSERLESGEGETAYEAWEKALEENWKNTALKKEDIEILLQFGKTLGQSDREGQQKHIRLALEHLERE
EEEAEEEQKKNEKMYKYLGFLAGLLIVILLI
>gnl|CDD|236231 PRK08308, PRK08308, acyl-CoA synthetase; Validated
MLIVNDEEYSKSDFDLRLQRYEEMEQFQEAAGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEA
AIRMAKRAGCHGLLYGESDFTKLEAVNYLAEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCE
QDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNPKFALNILRNTPQHILYAVPLMLHILGRLLPG
TFQFHAVMTSGTPLPEAWFYKLRERTTYMMQQYGCSEAGCVSICPDMKSHLDLGNPLPHVSVSAGSDENA
PEEIVVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDP
VAGERVKAKVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA
>gnl|CDD|236232 PRK08309, PRK08309, short chain dehydrogenase; Provisional
MHALVIGGTGMLKRVSLWLCEKGFHVSVIARREVKLENVKRESTTPESITPLPLDYHDDDALKLAIKSTI
EKNGPFDLAVAWIHSSAKDALSVVCRELDGSSETYRLFHVLGSAASDPRIPSEKIGPARCSYRRVILGFV
LEDTYSRWLTHEEISDGVIKAIESDADEHVVGTVEPW
>gnl|CDD|181375 PRK08310, PRK08310, amidase; Provisional
MLNHDPFNAFIAKPDKPLPHAASGPLAGLRFAVKDVFDVAGYVTGCGNPDWLAESPVATRTAPAVEKLLA
AGARFVGKTQTDELAFSLNGQNAHYGTPVNPAAPDRVPGGSSSGSAAAVAGGLADFALGTDTGGSVRAPA
SFCGLYGLRPTHGRISLEGVMPLAPSFDTVGWFARDIALLERVGEVLLGDDAQEFPLTQRLLIPVDLFAL
LDPAVRAALEAALARLRPHLGPAKPASVPPLSLDEWYEAFRVLQAAEAWETHGAWISSGNPQLGPGVADR
FAAGAEVTADQVEAARARRAAFARELAALLGPDAVLLLPTVPGAAPLRGAPFEALEAYRERALRLLCIAG
LAGLPQISLPLASVDGAPFGLSLIGPRGSDRSLLALAQTIAAARS
>gnl|CDD|236233 PRK08311, PRK08311, RNA polymerase sigma factor SigI
RKKSLEDILEKIKNGDEELREELIEEYKPFIAKVVSSVCGRYIDWENDDELSIGLIAFNEAIDSYDEEKG
KSFLSFAELVIKRRLIDYFRKESKHNLVLSNSDEEDEEENDIEIELSLEEYQEEEENEERREEIEEFKKE
LKEFGITFEDLVKESPKHRDTRENAIKIAKTIAENEELLEKLKRKKKLPLKELEKRVKVSRKTLERNRKY
IIAVAIILAGDYPYLKEYIRGEEEGEE
>gnl|CDD|236234 PRK08312, PRK08312, indolepyruvate oxidoreductase subunit beta family protein
MSASMSTRRPIKIAILAMGGQGGGVLADWIVDLAEHAGWFAQSTSVPGVAQRTGATIYYVELFPGALAPL
AGRAPVLALMPTPGDVDVVIAAELMEAGRAVQRGFVTPDRTTLIASTHRVYAIAEKMAPGDGRADSAALL
DAARAAAKRFIAFDMEALAEAAGSVISASLFGALAGSGALPFAREQFEAVIRASGKGVKASLRAFAAGFA
AAQQGGAAPPPPAAAAPTAPRPRPPALAARALLARVEAEFPAAARAMLLEGLRRLVDYQDAAYAAEYLDR
LAALAAADGGGARDFALTREAARHLALWMSYDDTIRVADLKTRASRFERVRDEVGAKPGQIVQVTEFMHP
RLEEICGTLPAGLGRWLEASPRLRAWLDRRTRRGRRVRTSSLRGFLLLYLLAGLRRLRRRSLRHAEEQAH
IERWLAAALAAAREDPALAVEILQCQRLVKGYSDTHARGLSKFDRLMAALDALAGRPDAADWLARLREAA
LADEAGRALDAALATIASFA
>gnl|CDD|181378 PRK08313, PRK08313, thiolase domain-containing protein
MKRLAAVLGTGQTKYVAKRQDVSMAGLVREAIDRALADAGLTWDDIDAVVVGKAPDFFEGVMMPELFLAD
ALGATGKPLIRVHTAGSVGGSTAVVAASLVQSGVYRRVLAVAWEKQSESNAMWALSIPVPFTKPVGAGAG
GYFAPHVRAYIRRSGAPEHIGAMVAVKDRLNGAKNPYAHLHQPDITLEKVMASQMLWDPIRFDETCPSSD
GACAVVIGDEEAADAAAGRPVAWIHGTAMRTEPLAFAGRDQVNPQAGRDAAAALWKAAGITDPRDEIDVA
EIYVPFSWFEPMWLENLGFAPEGEGWKLTEAGETAIGGRLPVNPSGGVLSSNPIGASGMIRFAEAALQVM
GKAGEHQVDGARKALGHAYGGGSQFFSMWVVGSEKP
>gnl|CDD|236235 PRK08314, PRK08314, long-chain-fatty-acid--CoA ligase; Validated
LPKSLTLPETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQN
SPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYS
DYLPAEPEIAVPAWLRAEPPLQALAPGGVVAWKEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMH
THRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWDREAAARLIERYRV
THWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNP
PDRPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEIDGKRFFRT
GDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPE
ARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAAK
>gnl|CDD|236236 PRK08315, PRK08315, AMP-binding domain protein; Validated
GLSYVRGPTDVPLLEQTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDR
VGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFKDSDYVAMLYELAPE
LATCEPGQLQSARLPELRRVIFLGDEKHPGMLNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGT
TGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGATMVYPGEGFDPLA
TLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVTIAYGM
TETSPVSTQTRTDDPLEKRVTTVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTA
EAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGE
EVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEELGLQAAK
>gnl|CDD|181381 PRK08316, PRK08316, acyl-CoA synthetase; Validated
LMERSTRARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHN
SDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVL
GGREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMS
ADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDF
DTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEIAPLATVLGPEEHLRRPGSAGRPVLNV
ETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDM
IKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKV
PKRVIFVDELPRNPSGKILKRELRERYAGAFTD
>gnl|CDD|181382 PRK08317, PRK08317, hypothetical protein; Provisional
LPDFRRYRARTFELLAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLGPN
VEFVRGDADGLPFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTDWDTLVWHSGDRALM
RKILNFWSDHFADPWLGRRLPGLFREAGLTDIEVEPYTLIETDLKEADKGFGLIRAARRAVEAGGISADE
ADAWLADLAQLARAGEFFFSVTGFLVVGRKP
>gnl|CDD|236237 PRK08318, PRK08318, NAD-dependent dihydropyrimidine dehydrogenase subunit PreA
MADLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKTLGPPIVNVSSPRFGALVKEDRRFI
GFNNIELITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGM
SERGMGSAVGQVPELVEMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVD
LDRMIPMPIVNGKSSHGGYCGPAVKPIALNMVAEIARDPETRGLPISGIGGIETWRDAAEFILLGAGTVQ
VCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVGLAVPNVTDWEDLDLNYIVYARIDQDKCIGCGRC
YIACEDTSHQAIEWDEDGTRTPEVIEEECVGCNLCAHVCPVEGCITMGEVKFGKPYANWTTHPNNPARAA
>gnl|CDD|181384 PRK08319, PRK08319, energy-coupling factor ABC transporter permease
MHIMEGFLPPKWAAFWWLLSLPFVVYGLRRLRKIVKEDPEQKPLLALAGAFIFVLSALKIPSVTGSCSHP
TGTGLGAILFGPAVTAVLGAIVLLFQALLLAHGGLTTLGANVFSMAIVGPFVGYLVYKLLRKAGLNLAVA
VFLAAFLADLATYVVTSVQLALAFPDPVGGFMASFAKFAGIFAVTQIPLAIAEGLLTVLIFNYLTKYRPD
LLVKLGVLSEEEVA
>gnl|CDD|236238 PRK08320, PRK08320, branched-chain amino acid aminotransferase; Reviewed
MEQLIYLNGEFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEIPLSKEE
MTEIVLETLRKNNLRDAYIRLVVSRGVGDLGLDPRKCPKPTVVCIAEPIGLYPGELYEKGLKVITVSTRR
NRPDALSPQVKSLNYLNNILAKIEANLAGVDEAIMLNDEGYVAEGTGDNIFIVKNGKLITPPTYAGALEG
ITRNAVIEIAKELGIPVREELFTLHDLYTADEVFLTGTAAEVIPVVKVDGRVIGDGKPGPITKKLLEEFR
ELTKKDGT
>gnl|CDD|181386 PRK08321, PRK08321, 1,4-dihydroxy-2-naphthoyl-CoA synthase
MTAMVSDIFDPDLWRPVPGFDFTDITYHRAVDQGTVRIAFDRPEVRNAFRPHTVDELYRALDHARMSPDV
GCVLLTGNGPSPKDGGWAFCSGGDQRIRGRDGYQYAEGDEADTVDPARAGRLHILEVQRLIRFMPKVVIA
VVPGWAAGGGHSLHVVCDLTLASREHARFKQTDADVGSFDGGYGSAYLARQVGQKFAREIFFLGRTYSAE
EAHDMGAVNAVVPHAELETEALEWAREINGKSPTAMRMLKYAFNLTDDGLVGQQLFAGEATRLAYMTDEA
QEGRDAFLEKRDPDWSDFPWYY
>gnl|CDD|236239 PRK08322, PRK08322, acetolactate synthase large subunit
MKAADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLST
LGPGATNLVTGVAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVRE
AFRLAEEERPGAVHLELPEDIAAEETDGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRK
TASKALTEFVDKTGIPFFTTQMGKGVIPETHPLSLGTAGLSQGDYVHCAIEHADLIINVGHDVIEKPPFF
MNPNGDKKVIHINFLPAEVDPVYFPQVEVVGDIANSLWQLKERLADQPHWDFPRFLKIREAIEAHLEEGA
DDDRFPMKPQRIVADLRKVMPDDDIVILDNGAYKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKL
VHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQENMGFEDFGLDFGNPDFVKY
AESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVDYSENDRVLNQELGELSCQL
>gnl|CDD|236240 PRK08323, PRK08323, phenylhydantoinase; Validated
MSTLIKNGTVVTADDTYKADVLIEDGKIAAIGANLGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDD
FETGTRAAACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEE
GITSFKLFMAYKGALMLDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPP
EVEGEATNRAIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGA
KYVMSPPLRDKEHQDALWRGLQDGDLQVVATDHCPFCFEQKKQLGRGDFTKIPNGTPGVEDRMPLLFSEG
VMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDPNATKTISASTLHSNVDYNPYEGFEV
TGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQAVV
>gnl|CDD|236241 PRK08324, PRK08324, bifunctional aldolase/short-chain dehydrogenase
MKNLWDDAEAAALDELALLVYRSRLLGADPRLVNHGGGNTSVKTTETDLTGEPVEVLWVKGSGGDLATIT
AAGFAALRLDPLRALKELGVLSDDEMVAYLRHCLFDPNAPAPSIETLLHAFLPFKHVDHTHPDAIIAIAN
APDGEELTREIFGDRVGWVPYVRPGFDLALAIAEAVRANPGAEGVVLGKHGLFTWGDTAKEAYERTIEII
TRAEEYIEARGAGFGGAVYEALPAPERRAIAAALAPVLRGAVSTEERGILHFRDSDAVLEFVNSADLPRL
AQLGTSTPDHFIRTKIRPLVLDAPPAADLEALKARLEEAVAAYRADYAAYFERNKAADSPAMLDPNPRVV
LIPGLGMFSFGKDKKTARVAADIYENAINVMRGAEAVGRYEPLSEQEAFDIEYWSLEQAKLQRMPKPKPL
AGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRALGVACDVTDEAAVQAAFE
EAALAFGGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGGSIVFIASKN
AVNPGPNFGAYGAAKAAELHLVRQLALELGPDGIRVNGVNPDAVVRGSGIWTGEWIEARAAAYGLSEEEL
EEFYRARNLLKREVTPEDVAEAVVFLASGLLSKTTGAIITVDGGNAAAFLR
>gnl|CDD|236242 PRK08326, PRK08326, R2-like ligand-binding oxidase
MEMTEEGMVHTDFKSLRSGGLNWNSFPMKLFAKGNAKFWNPADIDFSRDAEDWEKLSDEERDYATRLCAQ
FIAGEEAVTLDIQPLISAMAAEGRLEDEMYLTQFAFEEAKHTEAFRRWFDAVGVTEDLSVYTDDNPSYRQ
IFYEELPAALNRLSTDPSPENQVRASVTYNHVVEGVLAETGYYAWRKICVTRGILPGLQELVRRIGDDER
RHIAWGTYTCRRLVAADDSNWDVFEERMNELLPLALGLIDEIFALYGDQIPFELSNDEFVDYAADRGQRR
LGAIERARGRPVEEIDVDYSPEQLEDTFAEE
>gnl|CDD|236243 PRK08327, PRK08327, thiamine pyrophosphate-requiring protein
SMALTMYTAAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGRPLPEFVICPHEIVAISMAHGYA
LVTGKPQAVMVHVDVGTANALGGVHNAARSRIPVLVFAGRSPYTEEGELGSRNTRIHWTQEMRDQGGLVR
EYVKWDYEIRRGDQIGEVVARAIQIAMSEPKGPVYLTLPREVLAEEVPEVKADAGRQMAPAPPAPDPEDI
ARAAEMLAAAERPVIITWRAGRTAEGFASLRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDPRADLAEA
DLVLVVDSDVPWIPKKIRPDADARVIQIDVDPLKSRIPLWGFPCDLCIQADTSTALDQLEERLKSLASAE
RRRARRRRAAVRELRIRQEAAKRAEIERLKDRGPITPAYLSYCLGEVADEYDAIVTEYPFVPRQARLNKP
GSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEAAHWVAERYGLPVLVVVFNNGGWL
AVKEAVLEVYPEGYAARKGTFPGTDFDPRPDFAKIAEAFGGYGERVEDPEELKGALRRALAAVRKGRRSA
VLDVIVDRV
>gnl|CDD|169382 PRK08328, PRK08328, hypothetical protein; Provisional
MLSERELERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQ
ILHWEEDLGKNPKPLSAKWKLERFNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFETRYLLDDYAH
KKGIPLVHGAVEGTYGQVTTIVPGKTKRLREIFPKVKKKKGKFPILGATAGVIGSIQAMEVIKLITGYGE
PLLNKLLIVDLANNVFEVVEL
>gnl|CDD|236244 PRK08329, PRK08329, threonine synthase; Validated
MLRCTKCGRTYEEKFKLRCDCGGTLLVEREYGSFDSPREYLDMRRYIDYLPVDEEFLPHLTPPITPTVKR
SIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASK
EKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFV
PVGSGTLFLGIWKGFKELHEMGEISKMPKLVAVQAEGYESLCKRSKSENKLADGIAIPEPPRKEEMLRAL
EESNGFCISVGEEETRAALHWLRRMGFLVEPTSAVALAAYWKLLEEGLIEGGSKVLLPLSGSGLKNL
>gnl|CDD|169384 PRK08330, PRK08330, biotin--protein ligase; Provisional
IGRNIIYFDEVDSTNEYAKRIAPDEEEGTVIVADRQTAGHGRKGRAWASPEGGLWMSVILKPKVSPEHLP
KLVFLGALAVVDTLREFGIEGKIKWPNDVLVNYKKIAGVLVEGKGDFVVLGIGLNVNNEIPDELRETATS
MKEVLGREVPLIEVFKRLVENLDRWYKLFLEGPGEILEEVKGRSMILGKRVKIIGDGEILVEGIAEDIDE
FGALILRLDDGTVKKVLYGDVSLRFL
>gnl|CDD|181392 PRK08332, PRK08332, vitamin B12-dependent ribonucleotide reductase
MPVEKVMKRDGRIVPFDESRIRWAVQRAMWEVGVRDEKKLDEVVKRIVQRINELYDGKIPHIENIQDIVE
LELMRAGLFEVAKAYILYRKKKAEIREEKKRILNKKELDEIDKRFSINALRVLASRYLKKDENGNIIESP
RELFERVAILAVIPDLLYDERVFDKNGNYSQDLKRVEYYLENFEEFDGKYSIGKYKLNKYHFERMVNLYR
ELAEKGKMKVSIDEFLKMLERGEFDKYEKEIEEYFRLMTNQIFMPNTPALINSGRPLGMLSACFVVPIED
DMESIMKAAHDVAMIQKAGGGCIDGNAKIIFENEGEEHLTTMAEMYERYKHLGEFYDEEYNRWGIDVSEV
PIYVKSFDPETKRVVKGKVKVIWKYELGEDVPKYEIKTNKGTKILTSPWHPFFVLTPDFKIVEKRADELK
EGDILIGGMPDGEDYEFIFDYWLAGFIAGDGSIDKYRSHVKGHEYVYDRLRIYDYTTETLGIINDHLEKT
FGKRYSLQRDRNIHYIDIKAKGITSHYIELLRGITNGIPPPILKEGKNAVLSFITGLFDAEGHVNSKPGI
ELGMVNKKLIEDVTHYLNSLGIKARMREKPRKDGIDYVMHVEEYSSLLRFYELIGKNLQNSEKREKLEEL
LSKHNGGSFGLTLNFNAFKEWASKYGVEFKTNGSQTLAIIKNEKVSLGQWHRRGRVSKAVLVKMLRKLYE
TTKSEEVKRMLHLIEGLEVVKEITVTNEPKTFYDLTVERYQNYLAGENGMIFVHNTGLNFSKLRPEGDIV
GTTTGAASGPVSFMHLIDAVSDVIKQGGVRRGANMGILEIWHPDIEKFIHAKEKNIGTNVLSNFNISVGI
WEDFWEALKEGKKYPLINPRTGEVVKEIDPKSLFEELAYMAWAKADPGVIFFDVINRRNVLKEAKGGPIR
ATNPCVVGDTRILTPEGYIKAEELFSLAKERGKKEAVAVEGIAEEGEPYAYSVEILLPGEEEVKYETVHG
KALAIADPVAVPAYVWKVGKKKVARVRTKEGYEITATLDHKLMTPEGWKEVGDLKPGDKILLPRFEVEED
FGSESIGEDLAFVLGWFIGDGYLNVNDKRAWFYFNAEKEEEIAWKIREILAKHFGIKAEPHRYGNQIKLG
VRGEAYRWLESIVKTNEKRVPEIVYRLKPREIAAFLRGLFSADGYVDNDMAIRLTSKSRELLRDVQDLLL
LFGILSKIYERPYKSEFKYTTKDGEERTYRAEGYYELVIANYSRKLFAEKIGFEGYKMEKLSLQKTKIDE
PIVTVESVEVLGEEIVYDFTVPEHHSYISNGFMSHNCGEEPLYEYESCNLASINLAKFVKYDENGKPYFD
WDEYAYVIQKVAKYLDNAIDVNKFPLPEIDYNTKLTRRIGVGMMGLADALFKLGIPYNSEEGFKFMRKVT
EYLTFYAYKYSVEAAKKRGTFPLYEKTEYPKGELPVEGFYHPEIWNLPWDKLVEEIKKYGVRNAMVTTCP
PTGSVSMIADTSSGIEPIFALVYKKSVTVGEFYYVDPVFEAELKKRGLYSEELLKKISDNYGSVQGLEEI
PEDMQRVFVTALDIHWLDHILAQANIQMWLTDSASKTINMINEATVEDVKAAYLIAHFLGCKGVTVYRDG
SLSVQVYSVEGEKKKRYKPKPSEYAKKVLLEIVEKEPWIKNFINVDEILNGKREKELTFSLSHVSAVKPK
VEHSEHAQRPDGIPEEKIRELLGVVYCPVCYEKEGKLVELRMESGCATCPVCGWSKCVIS
>gnl|CDD|181393 PRK08333, PRK08333, aldolase
MRNVKAQLVKYSKLAHERGLTAAFGGNLSIRVGNLVFIKATGSVMDELTREQVAVIDLNGNQLSSVRPSS
EYRLHLAVYRNRPDVRAIAHLHPPYSIVASTLLEEELPIITPEAELYLKKIPILPFRPAGSVELAEQVAE
AMKEYDAVIMERHGIVTVGRSLREAFYKAELVEESAKLWYLKFK
>gnl|CDD|169386 PRK08334, PRK08334, S-methyl-5-thioribose-1-phosphate isomerase
MEIRYKPEELTKLPRSVEYEEGKVYMIDQRLLPREFKVIELRTVEEVAEAIKTMTVRGAPAIGAAAAFGL
ALYAETSKAKTKDEFMDGFYKAYETLKNTRPTAVNLFWALNRIKKLVEEHLEDPLDEIKRLIVEEAQKIA
DEDVEANLRMGHYGAEVLPEGNVLTHCNAGSLATVHLGTVGAVLRVMHKDGTLKLLWVDETRPVLQGARL
SAWEYHYDGIPLKLISDNMAGFVMQQGKVDAIIVGADRIVANGDFANKIGTYTLAVLAKEHGIPFFTVAP
LSTIDMSLKSGKEIPIEERSPEEVLTCGGCRIAPDVDVYNPAFDVTPHKYLTGIITDRGVVWPPFERNLK
KLFEEE
>gnl|CDD|169387 PRK08335, PRK08335, translation initiation factor IF-2B subunit alpha; Validated
MLPPEVREILEEMKAERIRGASWLAKKGAEAYLLLAEELDGEELENALKELREEIPEVNPTMASLYNLAR
FIPITNNPELVKSRAEEFLRLMEEAKREIGNIGSELIDDGDVIITHSFSSAVLEILKTAKRKGKRFKVIL
TESAPDYEGLALANELEFLGIEFEVITDAQLGLFAKEATLALVGADNVTRDGYVVNKAGTYLLALACHDN
GVPFYVAAETFKFHPELKSEEVELVERPYARQGHRVRNVLFDVTPWKYVRGIITELGILVPPREI
>gnl|CDD|181394 PRK08338, PRK08338, 2-oxoacid:ferredoxin oxidoreductase subunit gamma
MQIRFAGIGGQGVVLAGVILGEAAAIEGLNVLQTQDYSSASRGGHSIADVIISKEPIYDVMVTKADVLVA
LHQLGYETAKSSLKEDGLLIIDTDLVKPDRDYIGAPFTRIAEETTGLALTVNMVALGYLVAKTGVVKKES
VEEAIRRRVPKGTEEINIKAFRKGYEEGLK
>gnl|CDD|169389 PRK08339, PRK08339, short chain dehydrogenase; Provisional
MLKIDLSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYIVADLTKR
EDLERTVKELKNIGEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRII
YSTSVAIKEPIPNIALSNVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDRAKREGKSV
EEALQEYAKPIPLGRLGEPEEIGYLVAFLASDLGSYINGAMIPVDGGRLNSVF
>gnl|CDD|169390 PRK08340, PRK08340, SDR family oxidoreductase
MNVLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGEVYAVKADLSDKDDLKNLVKEA
WELLGGIDALVWNAGNVRCEPCMLHEAGYSDWLEAALLHLVAPGYLTTLLIQAWLEKKMKGVLVYLSSVS
VKEPMPPLVLADVTRAGLVQLAKGVSRTYGGKGIRAYTVLLGSFDTPGARENLARIAEERGVSFEETWER
EVLERTPLKRTGRWEELGSLIAFLLSENAEYMLGSTIVFDGAMTRGVNL
>gnl|CDD|236245 PRK08343, secD, preprotein translocase subunit SecD; Reviewed
MSKLKKLLKDWRVLLLIVLVLASIVAIFPPGGGPGGFTNLQYGLDLSGGSWIQLKLEGPVTQETMDLVVE
ILESRLNALGLKDIKVYPVGDQYIVVEVPGVDADTAKEIIEKQGVFEARIQTPGNNNETVLTGDDIESVG
SPSQDPSGGAWGVPFTLSEDGAEKFAEVAKGKGATDDPSGHPLDMYLDGELIYAAPLSPDLASGLASGPV
VITVGSTGTTEEAKEEAKELYIHLRSGALPVKLDIEGSGSVSPSLGEQFKKGSLIAGLLALLAVALVVFL
RYREPRIALPMVITSLSEVIIILGFAALIGWQLDLASIAGIIAVIGTGVDDLIIITDEVLHEGKVPSRKV
FLSRIKRAFFIIFAAAATTIAAMSPLAVMGLGDLKGFAITTILGVLIGVLITRPAYGDIIKELLKKD
>gnl|CDD|236246 PRK08344, PRK08344, V-type ATP synthase subunit K; Validated
VYVALGAALAAGLAGAASSFGVGIAGSAAAGAVAEDEKNFRNALILAGLPMTQTIYGLITLFLILMYAGI
LGGGFKFAEPDTINLGKALALLGAGLLVGLAELLSAIPQGIICASGIGALPRTPGKTFTQTIILAAYAEL
MGIFGLVFAILGLSLIG
>gnl|CDD|236247 PRK08345, PRK08345, cytochrome-c3 hydrogenase subunit gamma; Provisional
NPYALHDAKILEVYDLTEREKLFLLRFEDPELAESFTFKPGQFVQVTIPGVGEVPISICSSPTRKGFFEL
CIRRAGRVTTVIHRLKEGDIVGVRGPYGNGFPVDEMEGMDLLLIAGGLGMAPLRSVLLYAMDNRWKYGNI
TLIYGAKYYEDLLFYDELIKDLAEAENVKIIQSVTRDPEWPGCHGLPQGFIERVCKGVVTDLFREANTDP
KNTYAAICGPPVMYKFVFKELINRGYRPERIYVTLERRMRCGIGKCGHCIVGTSTSIKYVCKDGPVFTYF
DILSTRGLI
>gnl|CDD|181399 PRK08348, PRK08348, NADH-plastoquinone oxidoreductase subunit; Provisional
RLPLLPTVLRNLFKKPATNLFPATEPVPVPEDFRGKILYDVDKCVGCRMCVTVCPAGVFVYLPEIRKVAL
WTGRCVFCGQCVDVCPTGALQMSDDFLLASYDRFDEKFIPLKPEKVEEIK
>gnl|CDD|169396 PRK08349, PRK08349, hypothetical protein; Validated
MKAVALLSSGIDSPVAIYLMLRRGVEVYPVHFRQDEKKEEKVRELVERLQELHGGKLKDPVVVDAFEEQG
PVFEKLRELKKEKWTCIFCKYTMYRKAERIAHEIGASAIITGDSLGQVASQTLDNLMVISTATDLPVLRP
LIGLDKEEIVKIAKEIGTFEISIEPEPPCPFVPKYPVVRASLGEFEKILEEVYVLGPE
>gnl|CDD|169397 PRK08350, PRK08350, hypothetical protein; Provisional
MTVIENIIGRVAVLRGGKYSVEVDVITDSGFGRFAAPIDENPSLYIAEAHRAVSEVDEIIGPELIGFDAS
EQELIDSYLWEIDGTEDFSHIGANTALAVSVAVAKAAANSKNMPLYSYIGGTFTTELPVPILEFAEDENF
EYYVLVRDLMEITDVVDAVNKILENSKEVSLEGLSKASEKAGDELGLEVALGIAQKREMETEKVLNLVED
NNIAYIKPIGDEELFLELIAGTHGVFIDGEYLFRTRNILDRRYYNALSIKPINLGTLTDLYNLVNDVKSE
RITPILAEAKYESADEALPHLAVGLRCPAMLIHKDSVEKINELNRIAEDLGERGRIITFEE
>gnl|CDD|181400 PRK08351, PRK08351, DNA-directed RNA polymerase subunit E''; Validated
MTEKACRHCHYITTEDRCPVCGSRDLSDEWFDLVIIIDVENSRIAKKLGAKVPGKYAIRVR
>gnl|CDD|169399 PRK08354, PRK08354, putative aminotransferase; Provisional
YHGGIREEGLIDFSASVNPYPPEWLDEMFERAKEISGRYTYYEWLEEEFSKLFGEPIVITAGITEALYLI
GILALRDRKVIIPRHTYGEYERVARFFAARIIKGPNDPEKLEELVERNSVVFFCNPNNPDGKFYNFKELK
PLLDAVEDRNALLILDEAFIDFVKKPESPEGENIIKLRTFTKSYGLPGIRVGYVKGFEEAFRSVRMPWSI
GSTGYAFLEFLIEDDFEHLRKTMPLIWREKERFEKALYVKSDANFFIKDVGDAEKFVEFLKRNGILVRDC
TSFGLPGYIRFSVRDREENEKLIRALREWRL
>gnl|CDD|169400 PRK08356, PRK08356, hypothetical protein; Provisional
MGVEKMIVGVVGKIAAGKTTVAKFFEEKGFCRVSCSDPLIDLLTHNVSDYSWVPEVPFKGEPTRENLIEL
GRYLKEKYGEDILIRLAVDKKRNCKNIAIDGVRSRGEVEAIKRMGGKVIYVEAKPEIRFERLRRRGAEKD
KGIKSFEDFLKFDEWEEKLYHTTKLKDKADFVIVNEGTLEELRKKVEEILRELSK
>gnl|CDD|181401 PRK08360, PRK08360, aspartate aminotransferase family protein
MKPLEIIERYSKVISPANRVTYYPLVPVKAENAKVWDIEGNEYIDFLSDAAVQNVGHNNPRVVKAIKEQT
DKLIHYTPIYGFPVEPLLLAEKLIEIAPGDNPKVSFGLSGSDANDGAIKFARAYTKRRKILSYLRSYYGS
TYGAMSLTGLDFPVRALVGELSDVHYIPYPDCYRCPFGKEPGSCKMECVEYIKEKFEGEVYAEGVAALFA
EPIQGDAGMIVPPEDYFKKLKKILDEHGILLVVDEVQSGLGRTGKWFAIEHFGVEPDIITLGKPLGGGLP
ISATIGRAEIMDSLPPLAHAFTLSGNPVASAAALAVIEEIEEKNLLKRAEKLGNYTKKRLEEMKKKHELI
GDVRGIGLMIGVDLVKDRETKERAYEEAAKVVWRAWELGLIVTFFSGNVLRIQPPLTIEKEVLDEGLDIL
EEAIEDVEEGKVPDEVLEKVKGW
>gnl|CDD|236248 PRK08361, PRK08361, aspartate aminotransferase; Provisional
MRYKKRKYFIAGRINLIQRSKIRELFERASKMENVISLGIGEPDFDTPKNIKEAAKRALDEGWTHYTPNA
GIPELREAIAEYYKKFYGVDVDVDNVIVTAGAYEATYLAFESLLEEGDEVIIPDPAFVCYVEDAKIAEAK
PIRIPLREENEFQPDPDELLELITKRTRMIVINYPNNPTGATLDKEVAKAIADIAEDYNIYILSDEPYEH
FLYEGAKHYPMIKYAPDNTILANSFSKTFAMTGWRLGFVIAPEQVIKDMIKLHAYIIGNVASFVQIAGIE
ALRSKESWKAVEEMRKEYNERRKLVLKRLKEMPHIKVFEPKGAFYVFANIDETGMSSEDFAEWLLEKARV
VVIPGTAFGKAGEGYIRISYATSKEKLIEAMERMEKALEEL
>gnl|CDD|181402 PRK08363, PRK08363, alanine aminotransferase; Validated
MIRASERAMGVEYAIRDVVLPARELEKKGIKVIRLNIGDPVKFDFQPPEHMKEAYCRAIKEGHNYYGPSE
GLPELREAIVKREKRKNGVDITPDDVRVTAAVTEALQLIFGALLDPGDEILIPGPSYPPYTGLVKFYGGV
PVEYRTIEEEGWQPDIDDIRKKITEKTKAIAVINPNNPTGALYEKKTLKEILDIAGEHDLPVISDEIYDL
MTYEGKHVSPGSLTKDVPVIVMNGLSKVYFATGWRLGYIYFVDPEGKLAEVREAIDKLARIRLCPNTPAQ
FAAIAGLTGPMDYLEEYMKKLKERRDYIYKRLNEIPGISTTKPQGAFYIFPRIEEGPWKDDKEFVLDVLH
EAHVLFVHGSGFGEYGAGHFRLVFLPPVEILEEAMDRFEEFMRERLGS
>gnl|CDD|236249 PRK08364, PRK08364, sulfur carrier protein ThiS; Provisional
VMLMIRVKVIGRGIEKEIEWRKGMKVADILRAVGFNTESAIAKVNGKVALEDDPVKDGDYVEVIPVVSGG
>gnl|CDD|169406 PRK08366, vorA, 2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed
PIRKVVSGNYAAAYAALHARVQVVAAYPITPQTSIIEKIAEFIANGEADIQYVPVESEHSAMAACIGASA
AGARAFTATSAQGLALMHEMLHWAAGARLPIVMVDVNRAMAPPWSVWDDQTDSLAQRDTGWMQFYAENNQ
EVYDGVLMAFKVAETVNLPAMVVESAFILSHTYDVVEMIPQELVDEFLPPRKPLYSLADFDNPISVGALA
TPADYYEFRYKIAKAMEEAKKVIKEVGKEFGERFGRDYSQMIETYYTDDADFVFMGMGSLMGTVKEAVDL
LRKEGYKVGYAKVRWFRPFPKEELYEIAESVKGIAVLDRNFSFGQEGILFTEAKGALYNTDARPIMKNYI
VGLGGRDFTVNDVKAIAEDMKKVIEKGKLDKEVDWYHLKR
>gnl|CDD|181403 PRK08367, porA, pyruvate ferredoxin oxidoreductase subunit alpha; Reviewed
MPIRTVMKANEAAAWAAKLAKPKVIAAFPITPSTLVPEKISEFVANGELDAEFIKVESEHSAISACVGAS
AAGVRTFTATASQGLALMHEVLFIAAGMRLPIVMAIGNRALSAPINIWNDWQDTISQRDTGWMQFYAENN
QEALDLILIAFKVAEDERVLLPAMVGFDAFILTHTVEPVEIPDQEVVDEFLGEYEPKHAYLDPARPITQG
ALAFPAHYMEARYTVWEAMENAKKVIDEAFAEFEKKFGRKYQKIEEYRTEDAEIIFVTMGSLAGTLKEFV
DKLREEGYKVGAAKLTVYRPFPVEEIRALAKKAKVLAFLEKNISFGLGGAVFADASAALVNESEKPKILD
FIIGLGGRDVTFKQLDEALEIAEKALKGEEVEEVNWIGLRKEIL
>gnl|CDD|236250 PRK08373, PRK08373, aspartate kinase; Validated
MVEKMIVVKFGGSSVRYDFEEALELVKYLSEENEVVVVVSALKGVTDKLLKLAETFDKEALEEIEEIHEE
FAKRLGIDLEILSPYLKKLFNSRPDLPSEALRDYILSFGERLSAVLFAEALENEGIKGKVVDPWEILEAK
GSFGNAFIDIKKSKRNVKILYELLERGRVPVVPGFIGNLNGFRATLGRGGSDYSAVALGVLLNAKAVLIM
SDVEGIYTADPKLVPSARLIPYLSYDEALIAAKLGMKALHWKAIEPVKGKIPIIFGRTRDWRMGTLVSNE
SSGMPILVHKVGEEHAEILVVGVEEEIGYPVYEEGEFWFKIKVPKEELIEALREIHRRVFE
>gnl|CDD|169409 PRK08374, PRK08374, homoserine dehydrogenase; Provisional
MEVKVSIFGFGNVGRAVAEVLAEKSRVFKERYGVELKVVSITDTSGTIWLPEDIDLREAKEVKENFGKLS
NWGNDYEVYNFSPEEIVEEIDADIVVDVTNDKNAHEWHLEALKEGKSVVTSNKPPIAFHYDELLDLANER
NLPYLFEATVMAGTPIIGLLRENLLGDTVKRIEAVVNATTTFILTRMEQGKTFEEALKEAQTLGIAERDP
SKDIDGIDAGYKATILHWVAFPPITFEEVGIRGIKDVTEGEIERAKAKGRNVRLVATVEEGRISVKPKKL
PENSPLAVEGVENAAVIKTDLLGELVLKGPGAGGKETASGVVTDIIKAALKFPKYR
>gnl|CDD|236251 PRK08375, PRK08375, putative monovalent cation/H+ antiporter subunit D; Reviewed
MISHLLPLLVAVPLLAAALIVLLPKRRRLRWALALLVAALTFALAISLLPQVLDGGVIAYVVGGWPPGIG
IELRADSLSALFLLVTSILAIAALLYAIGYGEHRQTRFYALFLLLLAGLLGALLTADLFNLFVFLEIMSL
SSYALVAMGGDRRALAAARKYLIVGLIGSTFLLIGVGLLYGVTGTLNMADLAGALAENPTVVTAFGFVLL
ALALKAAVFPLHTWLPRAYPAAPPVVTALLSGLVTKVAVYALIRIYFTVFGGDFRFALGLGWLLAVLALL
SMLVGSLAALGQDDVKRVLAYSTVSQMGYILLGLALLTPLALAAGLLHLLHHALMKGALFLAAGAIEVTY
GTRRLSELSGLGRRMPLTAAAFAVASLSLIGVPPTSGFVSKWYLVVGAVEAGQWLVLAVLLASSLLALLY
FLRIWYRAFFGPPPPGSEAPKQEAPLGMLAPSLALALLSLLLGIYAGPLLQLADAAAAGLLGTSAYV
>gnl|CDD|236252 PRK08376, PRK08376, putative monovalent cation/H+ antiporter subunit D; Reviewed
VLGEHLPPLLIIIPLFGAFSMPIVSLLGGKAREIWAVLISFLTLIVALLVFYEVWNNGTIVYVLGAESPT
LTLPFGSGGFPIRIIWEVDLFGAFMALIATIVSFLAVLYSISYMKHDTGLDKYYTLILLLELGMLGMAIT
GDLFNFFVFLEIMSIASYALVAFRNDTWEAIEAGIKYMFVGSLASSMVLLGIALLYGQYGTLNMAYLAVK
MSENPTVVAKIALALFIAGLAMKSGAVPVHMWLPDAYPAAPSSISAMLLVIKQAGLYALARVLFSIYGPA
INLATVGWVIIILGCLTMFVGVAMAVVQKDVKRLLAYHSVSQIGYMLLGLGVGLAALGDPAMASYGEIAL
AGGIYHIVNHALYKALLFLTAGAVIYETGTRNLNELGGLARTMPKTTIAFLIGAAAIVGLPPFNGFASKW
LIYESSALFNPILGVIAMIGSVLTLASFVKVFHTAFFGPPSEKVMNVKEPPKPMLVPMLILAIAIIGMGL
FPWQISDKLMAPAAKALEDQGGYISAVLGGG
>gnl|CDD|181406 PRK08377, PRK08377, NADH dehydrogenase subunit N; Validated
MSQYASLLIALPLISAFFVPVIKGIGKSAVRYYLILITLLQTGIAGWVFMEVYTTGKPIIIMAGGWKPPV
GINLYIGPFAALFVLIIAIVSFIMSIFSLKAVEVEPIDKYAMLFLLLMLGATGMIATGDIFNLFVFMEIT
AITAYALTAYNKTGEAAEASMKYIVLGGIGSSFFLIGVALIYGATGTLNMAHIAQLAGTIDPTVAQVGLA
LLIFGLAVEAELFPLNAWAPDAYQAAPHPITVMFSAFVVKAGLYAMARILYLMQNANGWSSVLKLVIIMA
TLTVFFAELSALRQKNVKRMIAYSSIGQVGMIALALALGTQAGVDAGVFHMINHAIVKALLFLAVGYVGI
TLGGTEIEKFEGLGKRMPLTALALTIGALSTVGIPLFNVFWSKFRIILAGLSAGYTWPVALVLGASVVEA
VYYFRLIHTMWFKGEGERIRENAAIGIILLLLAALIVVIGIYPTPFWEVVQKAGSDIFNVAQYVKNVPLM
GVGA
>gnl|CDD|236253 PRK08378, PRK08378, hypothetical protein; Provisional
MNCDMCIQYIILALMIISAILAVEWRDLLAAAVGMAAVSLFASLEFFMLQAPDVAMAEAAIGAALSTAVV
IFAIKRTERWEREEEEKGWWVRW
>gnl|CDD|169414 PRK08381, PRK08381, putative monovalent cation/H+ antiporter subunit F; Reviewed
MAQENLLVAGFWILLFTALLASYRVIFGPTLADRIVGLNTITTKVVGIIAILSVLWEEYYLLDLAIVLLM
VNAVGGLILAKYMERRG
>gnl|CDD|169415 PRK08382, PRK08382, putative monovalent cation/H+ antiporter subunit E; Reviewed
MSRMPFYLRERLEEVKERVLYEIYEAQKLPPWERFVLTWLILLAFWVIISGDLSPRGLILGALTTLIIAS
YMRDFLTEDIRRSGHLLWKILYFALIYLPQYLIIMAFRLLESNLKVAKHVIFMDINPGIVKIKTDLHSDT
GITILANSITLTPGTLTLDVVKKLGETYLYVHWIDVETLNREKAGEKIKGDIEEWLKKIFW
>gnl|CDD|181407 PRK08383, PRK08383, putative monovalent cation/H+ antiporter subunit E; Reviewed
MSFITAFIWSYVLWLVLTAGSKGLLWSPEELIAGLIFAAIVGYATRNIIGEKATRFLNPIRWLLFIAYAF
GPLFWGMVKANLDVAYRVITGKIRPGIVKVPVDLENDAQYTILSNSITLTPGTLTIEACPEEKALYVHWI
NVPEGLEKPESSEPVSGPFEKWARRLGE
>gnl|CDD|236256 PRK08386, PRK08386, putative monovalent cation/H+ antiporter subunit B; Reviewed
SDMGLIVKTAARAIIPLIGIFGAYIVLHGHLTPGGGFQGGATIAGGGALFLVAFGLDEVKKRFNKTLYSA
LEGLGGLVFLGAAMLGISVAFFYNILWHTGPLFGGFVGYGNPGTLLSAGFLPIMNLAVGLKVFGGLVSAI
FAMALFRRWKS
>gnl|CDD|169420 PRK08387, PRK08387, putative monovalent cation/H+ antiporter subunit B; Reviewed
MSLVVRTTTKLVAPFLVTYAAYLMLYGHLSPGGGFQAGVILAVAVILLITSHGYKKVRKRFRKRTVSLLE
SSSGLFIVGLGIAGLLFGLFFLNFLRPSGGIVMPFNIGVGLKVGAAFVLVFYILIRWVERD
>gnl|CDD|236257 PRK08388, PRK08388, putative monovalent cation/H+ antiporter subunit C; Reviewed
MIAFQFITAFLMIALGIYAFLYKRNLIKLILALDLIDSGIHLLLISLGYRMENGLPPTAPIYTGYETLKS
PMVGPIPQALVLTSIVIGVCVLSLAMALTINAYRHYGTLDVTKLRRLRG
>gnl|CDD|236258 PRK08389, PRK08389, putative monovalent cation/H+ antiporter subunit C; Reviewed
MIEAYYFGAIALVLIGLYGVLVKKNLLKIIIGLDIMETGVNLLLISIGYVSGRSAPILSEGITPSNYVDP
IPQALVLTAIVIGVSTTALALSVAIKLYEKYGTLNVEEIRRLRG
>gnl|CDD|169423 PRK08392, PRK08392, hypothetical protein; Provisional
MDLHTHTVYSDGIGSVRDNIAEAERKGLRLVGISDHIHYFTPSKFNAYINEIRQWGEESEIVVLAGIEAN
ITPNGVDITDDFAKKLDYVIASVHEWFGRPEHHEYIELVKLALMDENVDIIGHFGNSFPYIGYPSEEELK
EILDLAEAYGKAFEISSRYRVPDLEFIRECIKRGIKLTFASDAHRPEDVGNVSWSLKVFKKAGGKKEDLL
FSELL
>gnl|CDD|181411 PRK08393, PRK08393, N-ethylammeline chlorohydrolase; Provisional
MSILIKNGYVIYGENLKVIRADVLIEGNKIVEVKRNINKPADTVIDASGSVVSPGFINAHTHSPMVLLRG
LADDVPLMEWLQNYIWPRERKLKRKDIYWGAYLGLLEMIKSGTTTFVDMYFHMEEVAKATLEVGLRGYLS
YGMVDLGDEEKREKEIKETEKLMEFIEKLNSPRVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLS
ETMDEIKQIREKYGKSPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVMP
LRKLLNAGVNVALGTDGAASNNNLDMLREMKLAALLHKVHNLDPTIADAETVFRMATQNGAKALGLKAGV
IKEGYLADIAVIDFNRPHLRPINNPISHLVYSANGNDVETTIVDGKIVMLDGEVLTLDEEKILDKFLKVI
EKLR
>gnl|CDD|169425 PRK08395, PRK08395, fumarate hydratase; Provisional
VKLKTPLSWEDVLKLKAGDVVYLSGIIYTARDLAHRRFLSEGFPFNPEGAVIYHCGPLVKNKKIVSAGPT
TSARMNKYLDFLFSLGVRGIIGKGGMNAEPFKGRAVYFAFPGGAGSLAAKSIKRVRDVYWEDLGMPDAVW
ELEVEDFPLLVAIDSKGRSLYR
>gnl|CDD|236259 PRK08401, PRK08401, L-aspartate oxidase; Provisional
MMKVGIVGGGLAGLTAAISLAKKGFDVTIIGPGIKKSNSYLAQAGIAFPILEGDSIRAHVLDTIRAGKYI
NDEEVVWNVISKSSEAYDFLTSLGLEFEGNELEGGHSFPRVFTIKNETGKHIIKILYKHARELGVNFIRG
FAEELAIKNGKAYGVFLDGELLKFDATVIATGGFSGLFKFTAGSPLNLGTLIGDAVMKGAPARDLEFVQF
HPTGFIGKRGTYLISEAVRGAGAKLVTGDGERFVNELETRDIVARAIYRKMQEGKGVFLDATGIEDFKRR
FPQIYAFLRKEGIDPSRDLIPVTPIAHYTIGGISVDTFYRTGIKNLYAIGEAASNGFHGANRLASNSLLE
CIVSGLEVARTISRERPKLREVKEPPYHGYELGDVDSIREILWNHAGIVRSEESLREGLKKLEGIEADPR
LKLLAKGVLECALAREESRGAHYREDFPFMRKEFERPSFFDGRCRL
>gnl|CDD|169427 PRK08402, PRK08402, replication factor A; Reviewed
MTVLTKEEIIERIERKTGMSREEIEEKIREIMKEEGISEHAAALLLAEELGVNLEGEEEAPLMHISDLVP
GMRGVNIVGRVLRKYPPREYTKKDGSTGRVASLIIYDDTGRARVVLWDAKVAKYYNKINVGDVIKVIDAQ
VRESLSGLPELHINFRARIILNPDDPRVEEIPPLEEVRSYNYTRKKIGELEGGERFVEVRGTIAKVYRVL
VYDACPECRRKVDYDPATDTWICPEHGEVEPIKITILDFGLDDGTGYIRVTLFGDDAAELLGVEPEEIAE
KLKELIEMGLTPKEAARKLAEEEFYNIIGREIVVRGNVIEDRFLGLILKASSWDEVDYKREIERVRAELE
ELGKM
>gnl|CDD|169428 PRK08404, PRK08404, V-type ATP synthase subunit H; Validated
MEDVIKEIVKAEKEAEERIEKAKEEAKKIIRKAKEEAKKIEEEIIKKAEEEAQKLIEKKKKEGEEEAKKI
LEEGEKEIEELKVKAEENFETAVSEAIKLIRGS
>gnl|CDD|181413 PRK08406, PRK08406, transcription elongation factor NusA-like protein; Validated
MEIKLTTEEIRYIALFESITGATVKDCIIDDDRIIFVVKEGDMGLAIGKGGENVKRLEEKLGKDIELVEY
SDDPEEFIKNIFAPAAVRSVTIKKKNGDKVAYVEVAPEDKGIAIGKNGKNIERAKDLAKRHFDIDDIILT
>gnl|CDD|181414 PRK08410, PRK08410, D-2-hydroxyacid dehydrogenase
MKIVILDAKTLGDKDLSVFEEFGDFQIYPTTSPEEVIERIKDANIIITNKVVIDKEVLSQLPNLKLICIT
ATGTNNVDIEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSESPIFTHISRPL
GEIKGKKWGIIGLGTIGKRVAKIAQAFGAKVVYYSTSGKNKNEEYERVSLEELLKTSDIISIHAPLNEKT
KNLIAYKELKLLKDGAILINVGRGGIVNEKDLAKALDEKDIYAGLDVLEKEPMEKNHPLLSIKNKEKLLI
TPHIAWASKEARKTLIEKVKENIKDFLEGGK
>gnl|CDD|236260 PRK08411, PRK08411, flagellin; Reviewed
MGFRINTNVAALNAKANSDLNAKSLDASLSRLSSGLRINSAADDASGMAIADSLRSQANTLGQAISNGND
ALGILQTADKAMDEQLKILDTIKTKATQAAQDGQSLKTRTMLQADINRLMEELDNIANTTSFNGKQLLSG
NFTNQEFQIGASSNQTVKATIGATQSSKIGVTRFETGARITTSGVVQLTIKNYNGIDDFKFQNVVISTSV
GTGLGALAEEINKNADKTGVRATFDVETTGVAAIKAGTTSDDFAINGVTIGKVEYKDGDGNGALVAAINS
VKDTTGVEASIDENGKLVLTSRDGRGIKIDGDIGGGSGILANMKENYGRLSLVKNDGKDILISGTNLSFA
GMGATDMISQASVSLRESKGQIDANVADAMGFNSYKGGVMIQGFSSVSAFMSSEGSGFSQGSGYSVGSGK
NYSVGLSSGIQISSASAMSTVYVVSAGSGFSSGSNLSQFAAMKTTAANVKDETAGVTTLKGAMAVMDIAE
TAITNLDQIRADIGSVQNQVTSTINNITVTQVNVKAAESQIRDVDFAAESANYSKANILAQSGSYAMAQA
NAVQQNVLRLLQ
>gnl|CDD|236261 PRK08412, flgL, flagellar hook-associated protein FlgL; Validated
MRVTFGSKYNQMNNYQNALQNKLNDVNTQIASGLKIQYGYQDSDVYNQNLKLQYEENTLDQGIDVASSAY
TFTLNTDKALNEFSKTMEAFKTKLIQAANDVHSETSREAIANDLEALKEHMINLANTSIGGEFLFSGSKV
DTKPIDSNGTYHGNDEDLNALVGSGNLVPYNISGQELFLGKDSDKHKLITTNVKLLNQNKLHPDVMDALE
HSSLPEEVYIKPSDTLRDLIGDNDKDPTNDPKEFFYLQGVRPDGSSFKEKFSLSKAYQNKESATKVSDLL
DKIGHAYGNTSQNKVVDVSLNNWGQIEIKDLTPGSSNLDFHLISSDGDFDDLDALRSSGKRVTEYVKSAF
VTDRSLSQIKAVPDMYNPRVLEIPSVFVTKDNVLANKNTKLSDIFGDSVDTLKIGATRLSNTSGTKIPNL
PVYLLLDVKNSTIQDLKDAIKARFGNEVDVEIETNGRLRIIDKSSKESPISLALSALDQKGLEVAGIPTN
NASEYQKTYFNKEGSKLESNVSQIIKNGNEYATGSTKLSEVAGGSLDGQVFNMKLNDVNGSFLEAQINLS
NAGSFLSLPNGIKIPLYDPHDTPAAVQVSKADEVTYRQLMDAMSIALNYSNTDPAIYQQISDNPTSKESK
EAYINLLKQAKGNVSVNLNEQGKLIIQDNMHSNTKMQFMLYDSDANDFSQALHSDKPSLTFNANNALTID
DPSVNFFDQLDNIITAVRKGIYRPDALGDTYSSDMRNIGIQNGITLIDHLSDHVEKMHAKNGAHSNAFEN
IIRRNEVLKTQVQSIRSEVIGTDMAETYNKFSNLTTNYNAVLASTNKINNLSLVNYL
>gnl|CDD|181416 PRK08415, PRK08415, enoyl-[acyl-carrier-protein] reductase FabI
MIMKGKKGLIVGVANNKSIAYGIAKACFEQGAELAFTYLNEALKKRVEPIAQELGSDYVYELDVSKPEHF
KSLAESLKKDLGKIDFIVHSVAFAPKEALEGSFLETSKEAFNIAMEISVYSLIELTRALLPLLNDGASVL
TLSYLGGVKYVPHYNVMGVAKAALESSVRYLAVDLGKKGIRVNAISAGPIKTLAASGIGDFRMILKWNEI
NAPLKKNVSIEEVGNSGMYLLSDLSSGVTGEIHYVDAGYNIMGMGAVEKEEDGKTVLAWDLQKE
>gnl|CDD|181417 PRK08416, PRK08416, enoyl-ACP reductase
NMSNEMKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEEANKIAEDLEQKYGIKAKAYPLNILE
PETYKELFKKIDEDFDRVDFFISNAIISGRAVVGGYTKFMRLKPKGLNNIYTATVNAFVVGAQEAAKRME
KVGGGSIISLSSTGNLVYIENYAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTNYE
EVKAKTEELSPLNRMGQPEDLAGACLFLCSEKASWLTGQTIVVDGGTTFK
>gnl|CDD|236262 PRK08417, PRK08417, metal-dependent hydrolase
IRIKDGKITEIGSDLKGEEILDAKGKTLLPALVDLNVSLKNDSLSSKNLKSLENECLKGGVGSIVLYPDS
TPAIDNEIALELINSAQRELPMQIFPSIRALDEDGKLSNIATLLKKGAKALELSSDLDANLLKVIAQYAK
MLDVPIFCRCEDSSFDDSGVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLE
LLDKFKSEGEKLLKEVSIHHLILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKS
NSKKDLAFDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGLNSGEIEVGKEADLVLF
DPNESTIIDDNFSLYSGDELYGKIEAVIIKGKLYLE
>gnl|CDD|181419 PRK08418, PRK08418, metal-dependent hydrolase
MKIIGASYIFTCDENFEILEDGAVVFDDKILEIGDYENLKKKYPNAKIQFFKNSVLLPAFINPHTHLEFS
ANKTTLDYGDFIPWLGSVINHREDLLEKCKGALIQQAINEMLKSGVGTIGAISSFGIDLEICAKSPLRVV
FFNEILGSNASAVDELYQDFLARFEESKKFKSKKFIPAIAIHSPYSVHPILAKKALQLAKKENLLVSTHF
LESKAEREWLEESKGWFKKFFEKFLKEPKPLYTPKEFLELFKGLRTLFTHCVYASEEELEKIKSKNASIT
HCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISLSLLDELRAALLTHANMPLLELAKILLLSATR
YGAKALGLNNGEIKEGKDADLSVFELPEECTKKEQLPLQFILHAKEVKKLFIGGKEVK
>gnl|CDD|181420 PRK08419, PRK08419, lipid A biosynthesis lauroyl acyltransferase; Reviewed
LSDRIYLSLFYILKFFLAKMPHCIFLRLAKALAFIMRYLDKKRRKIAKANLDFCFGESKSQEEKKRIIKK
CYENFAFFGLDFIRNQNTTKEEILNKVTFINEENLLDALKKKRPIIVTTAHYGYWELFSLALAAYYGAVS
IVGRLLKSAPINEMISKRREQFGIELIDKKGAMKELLKALKQGRALGILVDQNVVPKEGVEVKFFNKRVT
HTTIASILARRYNALIIPVFIFNDDYSHFTITFFPPIRSKITDDAEADILEATQAQASACEEMIRKKPDE
YFWFHRRFKSFYPEIYKR
>gnl|CDD|236263 PRK08425, flgE, flagellar hook protein FlgE; Validated
MMRSLWSGVSGLQAHQIAMDVEGNNIANVNTTGFKYSRASFVDMLSQTKLIATAPKGGLGGQNDMQIGLG
VGVSSTTKIFSQGSIQNTDKNTDLAIQGDGFFIVSPDGGTTRNYTRDGDFKFDAQGNFVNNGGYVVQGWV
SDTDTGTIDSTGPIQNIRIDPGMVMPARASTEVSIKANLNSGRHIGTQSAPIYALDSVHGWNDKTGDTAK
TNDDGINPFYDSSKNLAQVAEDMGVLFNADGDALNLREGQGIWVSYADAKMTKDIVPSAENLDITLNGVK
ISFTNDSAVSGTSSLVAAKNAINAQKSKTGVEAYLDGNQLRLENTNSLGTTEKMKNIVITVNGTGTFANF
VDGDKDITAFKYSYTSSPSPIVPMYNNSDIRQFRTTEDLRALLQRDARIVVDPDGDGNYQDSNASVKVTV
NQYGMFEISNPDNKNTIKKNLNLFVTGYSSKNDNVTNNVLFTNIMKGLNGASLIEGGASASSSKLTHATH
AASIDIYDSLGSKHTLRIEFYKSSTTQDGGAEWNMIIIVPEPAEINGGSEGRPNNFEGGRLRFNNDGSLA
GMNPPTLQFDPNNGAAAPQRINLSFGTSGSFDGLTSVDKISETYAIEQDGYTAGDLMDIRFDSDGTILGA
FTNGRTFALAQVALANFANNAGLQAEGGNVFSQTANSGQAVIGAAGTGGRGSISGSKLEMSNVDLSRSLT
QLIVIQRGFQANSKTITTSDQMLNTLLQLKQ
>gnl|CDD|236264 PRK08432, PRK08432, flagellar motor switch protein FliY; Validated
MNDFIKIFINEVVSTIEGLTGKAPEVGLEKEFSVSTENLIKPPYARAIISASGDENGKIELLAPVVLVTA
LSDLMLGGEGISKEEMDDDDLDAAKEIASNIFGAISTSLGAQKLLPKLNFTIENVEFVDENPDLSDYAKL
FLFSFKIEDIKSQIILLMDEAFENIFEKKPKEEGEETTDSASEEIKTHKASLSNEEIKNINMILDVKLPV
RVRIGQKKMLLKDVLSMDIGSVVELNQLANDPLEILVDDKVIAKGEVVIVDGNFGIQITEIGTKKERLEQ
LKH
>gnl|CDD|181423 PRK08433, PRK08433, flagellar motor switch protein FliN
EKEKEKANKERELELSTYLEELICDYENLLDIEVDFSAELGTTQISLLEILKFEKGSVIDLEKPAGESVE
LYINGRIIGKGEVMVYEKNLAIRINEILDSNAVVYYLKKES
>gnl|CDD|236265 PRK08439, PRK08439, 3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
MKRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKAD
RFIQLGLKAAREAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNM
LGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTR
NDDPKKASRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLRAM
KAALEMAGNPKIDYINAHGTSTPYNDKNETAALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIM
AMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGGTNGVVIFKKV
>gnl|CDD|181425 PRK08441, oorC, 2-oxoglutarate-acceptor oxidoreductase subunit OorC; Reviewed
MRAQLRFTGVGGQGVLLAGEILAEAKIKAGGYGVKASTYTSQVRGGPTKVDIILDDKEILYPYANEGEID
FMLSTAQISYNQFKSGVKEGGIIVVEPNLVKPTEEDKKKWQIYEIPIITIAKDEVGNVITQSVVALAIAV
EMTKCVDEDIVKDTMLSKVPAKVAEANKKAFELGKKYALEALK
>gnl|CDD|181426 PRK08444, PRK08444, aminofutalosine synthase MqnE
MDLIEKLENNERLNQEEAVKLYDLDLFTLGKYADKKRTKLHGKKVYFNVNRHINPTNICADVCKFCAFSA
HRKNPNPYTMSHEEILEIVKNSVKRGIKEVHIVSAHNPNYGYEWYLEIFKKIKEAYPNLHVKAMTAAEVD
FLSRKFGKSYEEVLEDMLEYGVDSMPGGGAEIFDEEVRKKICKGKVSSERWLEIHKYWHKKGKMSNATML
FGHIENREHRIDHMLRLRDLQDKTGGFNAFIPLVYQRENNYLKVEKFPSSQEILKTIAISRILLDNIPHI
KAYWATLTLNLALVAQEFGANDLDGTIEKESIQSAAGAKSANGLSLEDFIFLIKDSGFIPVERDSLYNEL
KKY
>gnl|CDD|181427 PRK08445, PRK08445, dehypoxanthine futalosine cyclase
MKRLSKEEALDLIKNAPLKELGEMALERKQELHPEKITTFIVDRNINYTNICWVDCKFCAFYRHLKEDDA
YILSFEEIDKKIEELLAIGGTQILFQGGVHPKLKIEWYENLVSHIAQKYPTITIHGFSAVEIDYIAKISK
ISIKEVLERLQAKGLSSIPGAGAEILSDRVRDIIAPKKLDSDRWLEVHRQAHLIGMKSTATMMFGTVEND
EEIIEHWERIRDLQDETGGFRAFILWSFQPDNTPLKEEIPEIKKQSSNRYLRLLAVSRLFLDNFKNIQSS
WVTQGSYIGQLALLFGANDLGSTMMEENVVKAAGASFRMNQAEMIELIKDIGEIPAKRNTAYEILERF
>gnl|CDD|236266 PRK08447, PRK08447, ribonucleoside-diphosphate reductase subunit alpha
MITVVKRNGRIEPLDISKIQKYTSDAVEGLEGVSQSELEVDAKIQFRDGITTEEIQQTLIKTAVDKIDID
RPNWTFVAARLFLYDLYHKVSGFTGYNHLKEYFEKGEKEGRILLGLKEKYDLDDLNAYIKPERDLQFNYL
GIKTLYDRYLIKDRNNNPIELPQHMFMAIAMFLAQNELDPQKWAKKFYDVISKFEVMLATPTLSNARTTR
HQLSSCYIGSTPDNIEGIFDSYKEMALLSKYGGGIGWDWSKVRAMGSYIDGHKNAAGGIIPFLKITNDIA
IAVDQLGTRKGAIAVYLEPWHMDISDFIDLRKNSGEERRRAHDLFPALWINDLFMKRVEEDAMWTLFDPY
ECKDLTELYGEEFEKRYLEYEKDEKIIKEYINAKELWKKILTNYFETGLPFLCFKDNANRANPNAHAGII
RSSNLCTEIFQNTAPNHYKIKIEFEDGSIEFFEEEELVTVDSGITKKAKKITSLDSLKGKKIYIVEKEKK
DGKTAVCNLASINLSKINTKEDIERVVPIAIRMLDNVIDLNFYPNRKVKATNLKSRAIGLGVMGEAQMLA
EHKIAWGSKEHLEKIDEIMEQISYNAIDASSNLALEKGVYPDFEGSNWSKGIFPIDKANEEAKKLVERGG
LFDSACDWEGLREKVKKDGMRNGYLMAIAPTSSISILVGTTQTIEPVYKRKWFEENLSGLIPVVVPNLSP
ETWQYYTPAYDLDQKDLIKAAAVRQKWIDQGQSLNIFLSLDKASGKYLNEIYTLAWKLGLKSTYYLRSES
PESEEVSVADRSIECEGCQ
>gnl|CDD|236267 PRK08451, PRK08451, DNA polymerase III subunits gamma and tau; Validated
MQALALKYRPKHFDELIGQESVSKTLSLALDNNRLAHAYLFSGLRGSGKTSSARIFARALVCEQGPSSTP
CDTCIQCQSALENRHIDIIEMDAASNRGIDDIRELIEQTKYKPSMARFKIFIIDEVHMLTKEAFNALLKT
LEEPPSYVKFILATTDPLKLPATILSRTQHFRFKQIPQNSIISHLKTILEKEGVSYEPEALEILARSGNG
SLRDTLTLLDQAIIYCKNAITESKVADMLGLLDPSKLEDFFQAILNQDKEKLFELLKELEDYEAEMVLDE
MMLFLKEKFLSKDSEFSILLYERFFRILSSAKSLLKEGADDGFVLLLMLFKMKEALKLKEIDDAIEELEQ
EKTTAIIPLNTPAPIIPNTEKEEAKDRIFKNLFEQLLDKIYDRNYELGECFEKNIRFIDFDSNTLTWESN
AQGEDKELLRKGFKIIKEIVDEVFGKGAKIKIQKALKSAENPLQSLKEFKPSNEKKKIDTESTAEMLEEE
AKKDDEEVQETQLKEATELQEFMINNEDLIEEAKELFGIKSIELL
>gnl|CDD|236268 PRK08452, PRK08452, flagellar protein FlaG; Provisional
MVNEISGQGGQAPTSHTSINQTTSKEIERSNIQTTIDQSKKTIDGGNNEQLKKKLEELTEKLNEEMKRLD
TNIRFGYNDKIKGLVVSVKEANGGKVIREIPSKEAIELMEYMRDVIGIIFDKKG
>gnl|CDD|181432 PRK08453, fliD, flagellar filament capping protein FliD
MAIGSLSSLGLGSKVLNYDVIDKLKDADEKALIAPLDKKMEQNVEKQKALVEIKTLLSALKSPVKTLSDY
STYLSRKSNVTGDALSASVGAGVPIQDIKVDVQNLAQGDINELGAKFSSRDDVFSQVDTTLKFYTQGKDY
AIDIKAGMTLGDVAQSITDATNGEVMGIVMKTGGNDPYQLMINSKNTGEDNRIYFGSTLQSTLTNKNALS
LVDGSGKGDLSLNLKDADGNMHTVPIMLELPESASIKQKNAAIQKAIEQALENDPNFKDLIANGDINIGT
LHGGKSLIINDRRGGNIEVKGSKAKELGFLQTTTQESDLLKSSRTIKEGKLEGVISIGGIKLDLSALTKE
GNTSEENADAIAQAINAKAGLYAFKNAEGKLVINSKTGMVTIKGEDALGKKSLKDLGLKAGTVQSYEASQ
ETLFMSKNLQKASDAKFTYNGVSITRPTNEVNDVISGVNITLEQTTEPNKPAIISVSRDNQAIIDSLKEF
VKAYNELIPKLDEDTRYDADTKIAGIFNGVGDIRSIRSSLNNVFSYSVHTDNGVESLMKYGLSLDEKGVM
TLDEAKLSSALNSDPKATQDFFYGSDSKDMGGREIHQEGIFSKFNQVIANLIDGGNAKLKIYEDSLTRDA
KSLTKDKENAQELLKTRYDIMAERFAAYDSQISKANQKFNSVQ
>gnl|CDD|181433 PRK08455, fliL, flagellar basal body-associated protein FliL; Reviewed
MAEEQENEAQQKKKKSKALLIIIIGVVVLLLLIVGVIAMLLMGSKEEEKENAQKPTQEVQANPPANSAQE
AKEGSNIQDFLNIGPLYPLDPFTVNLLSQSGRRYLKTSISLELSNEKLKPELDKKDPVIRDIIIRILSSK
TVEEVSTNKGKERLKDEIVGKLNEFLIDGFIKNVFFTDFVVQ
>gnl|CDD|181434 PRK08456, PRK08456, flagellar motor protein MotA; Validated
MDLSTILGMVLAVASISVGDILEGGNPLHVIHLSSFIIVVPTALFAAMTATHKKYVKAAYKELKIVFKNP
GVNLNERIKQLVELATLARKDGVLALEGRVAQIEDEFLKNGLSMLVDGKDLEEIKESMEIQIEEMEEYYH
GAAHYWITAGETCPTMGLVGAVMGLMLALQKLDNPAEMAAGIAGAFTATVTGIMGSYALFGPWGHKLKAK
SKDIIKEKTVILEGILGIAEGANPRDLEEKLLNYLSPGEPKKSQFEK
>gnl|CDD|181435 PRK08457, motB, flagellar motor protein MotB; Reviewed
MAKKKKPTECPAGEKWAVPYADFLSLLLALFIALYAISAVNKAKVEALKTEFIKIFDYTAKPEVKQPVKV
IPPDSGDAEEEMDELKSLKASQNTQQETIERRKGEGGALDQIDNGIALKLPSKLLFENGSAEIINADMMD
YLKRIAKIITKLPKQVKINVRGYTDNSPLNKSRYKDHYELAAARAYNVMKVLIQYGINPNRLSFSSYGSN
NPIAPNDSLENRLKNNRVEIFFKVDANDTSTQKSILDEIFNIHKQQE
>gnl|CDD|236269 PRK08462, PRK08462, acetyl-CoA carboxylase biotin carboxylase subunit
KKEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIIS
AAEIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGAL
KSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRH
IEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLL
DSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKLKGHAIECRITAEDPKKFYP
SPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEGIKTTIP
FHLEMMENADFINNKYDTKYLEEHF
>gnl|CDD|169452 PRK08463, PRK08463, acetyl-CoA carboxylase subunit A; Validated
MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPIKGYLDVKRIVEIAK
ACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSES
MEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIE
FQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDD
YNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDLEQSDIKPRGFAIEARITAENVWKNFIP
SPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLAVNKLERALKEFVIDGIRTTIP
FLIAITKTREFRRGYFDTSYIETHMQELLEKTEDRHQENKEEVIAAIAAALKKIRESR
>gnl|CDD|236270 PRK08471, flgK, flagellar hook-associated protein FlgK; Validated
MMGIFSSLNTGYTGLQAAQVMVDTTGNNISNASSEFYTRQRVVQSAQAALNTGGGNVGTGTDIETIVRIH
DEFVYSRYKKASTELEYTDYEFSTLQEASQYFPDLDDTGILKDLQDYFNAWNDFASNPKDSAQKQALAQK
TETLTNNIKDTRERLDTLQKKVNEELKVTVDEINSLGKQIAEINKQIKEVEAGKTLKHANELRDKRDELE
LTLSKLVGANVFKSSIKSDSRLDTTSADFGESYNLNIGGFNIVDGSNFHPLVLDEDENKGGFNQIYYESD
DFKRIDITDKISGGKVGALLDLRGRNYDGGSGGTLDGKIQDYIDNLDTFAKTLIESTNNIYAQSATESIE
SDPLSLKSDEALVDTNYNIQNGSFDLVVYDTDGKEVARKTINIDVITTMNDIVQQINANTDDNNDNNANN
DVDDYFTASFNNDTKTGDGLFQIQPKNASQGYTVSIEDKGTNFPGALGLNRFFDGDDASNISLNSSYKKD
PTTIRAWLAPVDGNNDVANKMQQLQYDKVNFYNNKGTIKNMTIEEYYRFLTTKIASDTEKNNRINDTNKA
LLNSVKKEYQSISGVSTDEELVNLIKFQSSYGAAAKIITTIDQMLDTLLGIKQ
>gnl|CDD|181439 PRK08472, fliI, flagellar protein export ATPase FliI
MPLESLKNKLQKFNLSPRFGSITKISPTIIEADGLNPSVGDIVKIESSDNGKECLGMVVVIEKEQFGISP
FSFIEGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEV
FSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPEFIEKNLGGDL
ENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPP
SVLSLLPQLMERAGKEEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILN
SASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAYQKGNDKELDEAISKKEFMEQFLKQNPNELF
PFEQTFEQLEEILR
>gnl|CDD|236271 PRK08474, PRK08474, F0F1 ATP synthase subunit delta; Validated
MEELIAKRYAKALLSSLSSDELNDIYSNLKILSSAFADEKFKEIISSPEISKEQKIEFLLSFVDNANAKF
QNFIKLLAENKRLELIPAIAKELERQIALKENEYVGVVYSNEKLSEETLKKLEEKLSKKFNAKIKLKQKK
SDYDGIKVEVDDLGVEVSFSKDRLKNQLIEYILKAI
>gnl|CDD|236272 PRK08475, PRK08475, F0F1 ATP synthase subunit B; Validated
KFFFLLLLGFYAFAASLGATEQYDIIERTINFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEIQEKLK
ESKEKKEDALKKLEEAKEKAELIVETAKKEAYILTQKIEKQTKDDIENLIKSFEELMEFEVRKMEREVVE
EVLNELFESKKVSLNQQEYVNILLKKV
>gnl|CDD|181442 PRK08476, PRK08476, F0F1 ATP synthase subunit B'; Validated
MMLDVNPYLMLATFVVFLLLIVILNSWLYKPLLKFMDNRNASIKNDLEKVKTNSSDVSEIEHEIETILKN
AREEANKIRQKAIAKAKEEAEKKIEAKKAELESKYEAFAKQLANQKQELKEQLLSQMPEFKEALNAKLSK
I
>gnl|CDD|236273 PRK08477, PRK08477, biotin--[acetyl-CoA-carboxylase] ligase
MEIRVFESLDSTQTYLIEKIKNGELKAPFAIVAKEQTAGIGSRGNSWEGKKGNLFFSFALKESDLPKDLP
LQSSSIYFGFLLKEVLKELGSKVWLKWPNDLYLDDKKIGGVITNKIKNFIVCGIGLNLKFSPKNFACLDI
EISDDLLLEGFLQKIEKKILWKQIFSKYKLEFEKSKSFSFHIDGKLVSLKDAELLEDGSILINGKKVYSL
R
>gnl|CDD|181444 PRK08482, PRK08482, F0F1 ATP synthase subunit C; Validated
MKKLALLFLALAGVAFAADGGMGGMDMIKSYSVLAAGIGLGIAALGGAIGMGNTAAATIAGTARNPGLGG
KLMTTMFIALAMIEAQVIYALVIALIALYANPFLS
>gnl|CDD|236274 PRK08485, PRK08485, DNA polymerase III subunit delta'; Validated
MMMISKIIITSDFEESKEELINEFGKKNLRFFIKEEFKIEDAKEVIAEAYIAESEEKIIVIAAPSYGIEA
QNALLKILEEPPKNICFIIVAKSKNLLLPTIRSRLIIEKRKQKKPVKPLDLDLKKLDLKDIYEFLKELEK
ENKLSKEELKELIESLLKECVKYKIPLNEEELEYFDKAIKLADLNAKSSYVLLPLLLSLLEKKKTP
>gnl|CDD|236275 PRK08486, PRK08486, single-stranded DNA-binding protein; Provisional
MFNKVILVGNLTRDVELRYLPSGSAIATIGLATSRRFKKQDGEKGEEVCFIDIRLFGRTAEIANQYLSKG
SKVLIEGRLTFESWMDQNGQKRSKHTITAESMQMLDSKSDNPQANAMQDNSFHENFNNNYPGNYNNPSQD
PYMNQAQSYNQNAYAKENQQAQPPKYENSVPEIDIDEEEIPF
>gnl|CDD|236276 PRK08487, PRK08487, DNA polymerase III subunit delta; Validated
MYKKELDTLLKQNKLPNAFLLYGEDEFQIELYAKKISEKFKPENELKTLYFDEYDFEQAKDFLSQSSLFG
GKNLLIIKLDKKIPKKELKLLIELCEKNSDNYFIIELYGADSKTKDIEKLFQKKDEAVFVRFFKPNAREA
LELLQERAKELGLDIDQNALNHLYFIHNEDLALAANELEKLAILNEPITLKDIQELVFGLGSVSFEDFFE
KLLNKKDIKDDLEKLLEEGFNEIALLNSLERFFYQLFLFFAYIKINGKPDAKEILGYKPPKQIAENLAKQ
AIKIKEAQYKEIFELLLEWELELKTGQKIDKNLFLLSTLIKIQKILNP
>gnl|CDD|181448 PRK08489, PRK08489, NAD(P)H-quinone oxidoreductase subunit 3
MSHEDLSHPYFGVFVLLVLTFVAFFLTTRLARFISRKLAQKNTEKLKLAIYECGPEPVKQPNRISSHFYI
MALLFILFDVEIVFMFPWAVDFKLLGLFGLIEMLLFIVLLTIGFIYAWKKGALEWQSIK
>gnl|CDD|181449 PRK08491, PRK08491, NADH-quinone oxidoreductase subunit C
MRKYSPKKNVQKKSYYTDRFYVAPPTPKSYVEGSVFEKDLNHLSYKVEILESYIELDQAVIWIKKDDNFK
VLKILKHLGYECLSEMSAIDFLAKKGGFEVFYQLLSMSKRKRVRVKCFLKEKEALQSVSFLFKSANWSER
EMYDMFGIVINNHPYLKRILMPDDWVGHPLLKSYPLKGDEFAQWYEVDKIFGKEYREVVGPEQRDSARVD
EKDTFNFARIGHEVPKGEELKEKEEKQEYQEEGGVAFVKKLKKKASKILKKRR
>gnl|CDD|236277 PRK08493, PRK08493, NADH-quinone oxidoreductase subunit G
MITITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEADGKRVYSCNTKAKEGMNI
LTNTPNLMDERNAIMQTYDVNHPLECGVCDKSGECELQNFTHEMGVNHQPYAIKDTHKPHKHWGKINYDP
SLCIVCERCVTVCKDKIGESALKTVPRGLDAPDKSFKESMPKDAYAVWSKKQKSLIGPVGGETLDCSFCG
ECIAVCPVGALSSSDFQYTSNAWELKKIPATCPHCSDCCLIYYDVKHSSILNQESKIYRVSNDFYFNPLC
GAGRFAFDFQNEADKDEKAFKEAVEAFKEAKAIKFNSFITNEEALILQRLKKKFGLKLINEEALKFQQFL
KVFSEVSGKSYSANLEDIKTSDFVVVAGSALKTDNPLLRYAINNALKMNKASGLYFHPIKDNVIANLSKN
FFCITHEVGAEEIILYFLLKKFLEEEAILKSLEEFKQSIVKEAALSILEEIREKVLEQAEQGCENQEEVK
KEVPKKVKKIPEVDTYLLLEELGINEETYEKLEALLAKKNNFTLVVGEDLYAHKNAKNLAKLLGLIQKYT
AFKVILIPPSTNTLGVALICDLSEEIEGGKTVGYNEKGDFTISSLEKGDLALPALNQQEGTFTNIDKRVV
PTNAALPFEGYDLNDIANALGFDEEYTIDYTKKLPTEKGFKAIEFDDLENYYTNDGSNHRGYELETSSFE
KSAKEETIECEPIKPLKEKIGINIYLANPITQFNNFTNKAENLNEKAGLYVSEAFLKKLNLKDGDNVTLK
KEEEELTGSVYLDESLKGGAYLPSFDLKLNTSSFFREYRFASVDIKEQV
>gnl|CDD|236278 PRK08506, PRK08506, replicative DNA helicase; Provisional
MDELYDLDIERAVLSSILFSPDKFEEIASVLEPKDFYLPAHQDIFEAMLKLHNEDEPIDEEFIRKKLPKD
KKIDEEILLEILATNPIDNIEAYVEEIKEKSIKRELLSLANTIPEQAVEEDQKSSDILDEVERELYSITN
GSNSEDFKDSKEVIESTMEHIKKQKRLGNKDIIGLDTGFVELNKMTKGFNKGDLIIIAARPSMGKTTLCL
NMALKALNQDKGVAFFSLEMPAEQLMLRMLSAKTSIPLQNLRTGDLDDDEWERLSDACDELSKKKLFVYD
SGYVNIHQVRAQLRKLKSQHPEIGLAVIDYLQLMSGSGNFKDRHLQISEISRGLKLLARELDIPIIALSQ
LNRSLESRADKRPMLSDLRESGAIEQDADIILFVYRDDVYKEREEKEKEKKAKKEGKEERRIHFQNKSIE
EAEIIIGKNRNGPTGTVKLRFQKEFTRFVDKPIESHYEEGEETKADIEIPTT
>gnl|CDD|181452 PRK08507, PRK08507, prephenate dehydrogenase; Validated
MKIGIIGLGLMGGSLGLALKEKGLISKVYGYDHNELHLKKALELGLVDEIVSFEELKKCDVIFLAIPVDA
IIEILPKLLDIKENTTIIDLGSTKAKIIESVPKHIRKNFIAAHPMAGTENSGPKAAIKGLYEGKVVVLCD
VEKSGEKHQERAKEIFSGLGMRIVYMDAKEHDLHAAYISHLPHIISFALANTVLKEEDERNIFDLAGGGF
RSMSRLAKSSPAMWSDIFKQNKENVLEAIDEFIKELEQFKQLIENEDWEELEEWMEQANKLREIL
>gnl|CDD|236279 PRK08508, PRK08508, biotin synthase; Provisional
MKEIFLCAISNISSGNCKEDCKYCTQSAHYKADIKRYKRKDIEQIVQEAKMAKANGALGFCLVTSGRGLD
DKKLEYVAEAAKAVKKEVPGLHLIACNGTASVEQLKELKKAGIFSYNHNLETSKEFFPKICTTHTWEERF
QTCENAKEAGLGLCSGGIFGLGESWEDRISFLKSLASLSPHSTPINFFIPNPALPLKAPTLSADEALEIV
RLAKEALPNARLMVAGGREVVFGERQYEIFEAGANAIVIGDYLTTKGEAPKKDIEKLKSLGFEIATSCH
>gnl|CDD|236280 PRK08515, flgA, flagellar basal body P-ring formation protein FlgA
MKIIFLFLIILNNLFGINISSLKTEIKEAYLKEYKNNKIEIKSINLEPTSSLPEDFSQYEFLRIELNAFN
SLKGFGRASFKTPNNPNKKLFFRYSIIANLEVLKSIRAIKKDDNLTANNTKKKRIPFGKLPKNPLLEDDI
DNLSAKSFIPPGTILTADKFKALILVRKNDIINGVLKEGGVSIEISLKALQDGNLGDIIQAKNKSNKILK
AKVLSKNKAEIL
>gnl|CDD|236281 PRK08517, PRK08517, 3'-5' exonuclease
MLKQDIQALIAKLKKQSLSYGMLEKSLSRLLKDIDIDLELLKALGLPLVENKENLITLKTRFTPIKDQVF
CFVDIETNGSKPKKHQIIEIGAVKVKNGEIIDRFESFVKAKEVPEYITELTGITYEDLENAPSLKEVLEE
FRLFLGDSVFVAHNVNFDYNFISRSLEEIGLGPLLNRKLCTIDLAKRTIESPRYGLSFLKELLGIEIEVH
HRAYADALAAYEIFKICLLNLPSYIKTTEDLIDFSKTAKTLKKKKPR
>gnl|CDD|181458 PRK08527, PRK08527, acetolactate synthase large subunit
KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVA
IVTSGPGFTNAVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRI
LKEAFYIARSGRPGPVHIDIPKDVTATLGEFEYPKEISLKTYKPTYKGNSRQIKKAAEAIKEAKKPLFYL
GGGAILSNASEEIRELVKKTGIPAVETLMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARF
DDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIVGDLKNVLKEMLEELKEENPTTYKEWREILKRY
NELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWVAQFYPFNYPRQLATSGGLGTMGYGL
PAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQWQTFFYEERYSETD
LSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLPMVPAGGALYNMILPK
KKD
>gnl|CDD|181459 PRK08533, PRK08533, flagellar accessory protein FlaH; Reviewed
MELAKIELSRDELHKRLGGGIPAGSLILIEGDESTGKSILSQRLAYGFLQNGYSVSYVSTQLTTTEFIKQ
MMSLGYDINKKLISGKLLYIPVYPLLSGNSEKRKFLKKLMNTRRFYEKDVIIIDSLSSLISNDASEVAVN
DLMAFFKRISSLNKVIILTANPKELDESVLTILRTAATMLIRLEVKVFGGDLKNSAKIVKYNMAKGSFQK
SIPFRVEPKIGLAVEIASVA
>gnl|CDD|181460 PRK08534, PRK08534, pyruvate ferredoxin oxidoreductase subunit gamma; Reviewed
MIEIRFHGRGGQGAVTAAEILAKAAFEDGKFSQAFPFFGVERRGAPVMAFTRIDDKPIRLRSQIYEPDYV
IVQDPTLLDSVDVTSGLKKDGIIIINTTKDPEDLKYDTKAKVYTIDATKIALDVLGVPIVNTTMLGAFAG
ATGEVSLESLKKAILERFPGKLGEKNAEAVEKAYNLMKEEY
>gnl|CDD|236282 PRK08535, PRK08535, ribose 1,5-bisphosphate isomerase
MEVMPEVLETAEKIKTMEIRGAGRIARAAAEALKDQAEKSDAESPEEFKAEMRAAANILISTRPTAVSLP
NAVRYVMRYYSGETVEEARESVIERAEEFIESSENAVEKIGEIGAKRIRDGDVIMTHCNSSAALSVIKTA
HEQGKDIEVIATETRPRNQGHITAKELAEYGIPVTLIVDSAVRYFMKDVDKVVVGADAITANGAVINKIG
TSQIALAAHEARVPFMVAAETYKFSPKTLLGELVEIEERDPTEVLPEEILAKLPGVKVRNPAFDVTPPEY
IDAIITEIGAIPPEMAYTIIKEYLGWALEE
>gnl|CDD|181462 PRK08537, PRK08537, 2-oxoacid:ferredoxin oxidoreductase subunit gamma
MRKEIRISGFGGQGIILAGVILGRAAALYDGKYAVQTQSYGPEARGGASKSEVVISDEEIDYPKVISPDI
LVAMSQEAYDKYLDDLKEGGTVIVDPDLVPIREIEYEKKVKVYKVPFTEIAEEEIGLSIVANIVMLGALT
KLTGIVSKEAIEKAILDSVPKGTEEKNLMAFEKGYEL
>gnl|CDD|236284 PRK08541, PRK08541, flagellin; Validated
MKKGAVGIGTLIVFIAMVLVAAVAAAVLINTSGYLQQKASATGRETTQQVASGIQVLKVIGYANAPSNGN
ITKLAIYVTPNAGSEGIDLSNTKITLSDGGKKAVLVYDSGSLSATGGTNNIFNLTVWSNLNGGTSFGIIV
LQDADGSLSNSYPTINKGDIVALLVNVSAVFGDGIPPRTKVSGEVIPEFGAPGVIDFTTPSTYTQNVIEL
Q
>gnl|CDD|236285 PRK08554, PRK08554, peptidase; Reviewed
MDVLELLSSLVSFETVNDPSKGIKPSKECPKFIKDTLESWGIESELIEKDGYYAVYGEIGEGKPKLLFMA
HFDVVPVNPEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLNGKVIFAFTGDEEIGGA
MAMHIAEKLREEGKLPKYMINADGIGMKPIIRRRKGFGVTIRVPSEKVKVKGKLREQTFEIRTPVVETRH
AAYFLPGVDTHPLIAASHFLRESNVLAVSLEGKFLKGNVVPGEVTLTYLEPGEGEEVEVDLGLTRLLKAI
VPLVRAPIKAEKYSDYGVSITPNVYSFAEGKHVLKLDIRAMSYSKEDIERTLKEVLEFNLPEAEVEIRTN
EKAGYLFTPPDEEIVKVALRVLKELGEDAEPVEGPGASDSRYFTPYGVKAIDFGPKGGNIHGPNEYVEID
SLKKMPEVYKRIALRLLG
>gnl|CDD|181465 PRK08557, PRK08557, hypothetical protein; Provisional
MFKEDTKFASPYEIKILNKLTNKNFQYDDAIILEKLSGLDYRKRVYISEDQIGILEFDLLDLDWKFHPSP
SYYLIEEPKIKLKPTKRRLKGKYIKEELIENPEELNEILENDYVGVEIGNFLGVGVKKEDRIKIKDLSLK
KELDFEKIEDYLEKNKERIEKLEENSLSILKDYIEKYKNKGYAINASFSGGKDSSVSTLLAKEVIPDLEV
IFIDTGLEYPETINYVKDFAKKYDLNLDTLDGDNFWENLEKEGIPTKDNRWCNSACKLMPLKEYLKKKYG
NKKVLTIDGSRKYESFTRANLDYERKSGFIDFQTNVFPILDWNSLDIWSYIYLNDILYNPLYDKGFERIG
CYLCPSALNSEFLRVKELYPELFNRWVKYLKKYGYDEDEILRGFWRWKELPPKMKELKKNMGVDIEK
>gnl|CDD|181466 PRK08558, PRK08558, adenine phosphoribosyltransferase; Provisional
MNRAEKVRLQLRAVRVLRSLKKTYTYEELSSITGLPESVLNRYVNGHVLPSVERAREIVEKLGPYYNLEE
EVKARIKVDDEGYVDNSSVVFDPSFLRLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGADLVYA
KKSKETGVEKFYEEYQRLASGIEVTLYLPASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVF
FLIAVGEVGIDRAREETDAPVDALYTLE
>gnl|CDD|181467 PRK08559, nusG, transcription antitermination protein NusG; Validated
MKPEMSMIFAVKTTAGQERNVALMLAMRAKKENLPIYAILAPPELKGYVLVEAESKGAVEEAIRGIPHVR
GVVPGEISFEEVEHFLKPKPIVEGIKEGDIVELIAGPFKGEKARVVRVDESKEEVTVELLEAAVPIPVTV
RGDQVRVVKKEEE
>gnl|CDD|236286 PRK08560, PRK08560, tyrosyl-tRNA synthetase; Validated
IEERLELITRNTEEVVTEEELRELLESKEEPKAYIGFEPSGKIHLGHLLTMNKLADLQKAGFKVTVLLAD
WHAYLNDKGDLEEIRKVAEYNKKVFEALGLDPDKTEFVLGSEFQLDKEYWLLVLKLAKNTTLARARRSMT
IMGRRMEEPDVSKLVYPLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDG
GGIKMSKSKPGSAIFVHDSPEEIRRKIKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLE
YESYEELERDYAEGKLHPMDLKNAVAEYLIEILEPVREYLEEGPELLEL
>gnl|CDD|236287 PRK08561, rps15p, 30S ribosomal protein S15P; Reviewed
MARMHTRRRGKSGSTRPARTEPPEWVDYSPEEIEELVVELAKQGYSPSMIGIILRDQYGIPDVKLITGKK
ITEILEENGLAPEIPEDLRNLIKKAVNLRKHLEENPKDLHNKRGLQLIESKIRRLVKYYKRTGVLPADWR
YSPETAELLVS
>gnl|CDD|236288 PRK08562, rpl32e, 50S ribosomal protein L32e; Validated
SERKRLLKLRLKLKRKKPEFKRQDWHRYKRLGDKWRRPRGLDSKMRLKLKGKPAIVEVGYRSPKAVRGLH
PSGYEEVLVHNVKELEKLDPETQAARIASTVGKRKRLEILKKARELGIKVLNPGK
>gnl|CDD|236289 PRK08563, PRK08563, DNA-directed RNA polymerase subunit E'; Provisional
MYKLVKLEDVVRIPPEMFGEDLEEAALEVLREKYEGRIDKELGIIVAVLDVKVIGEGKIVPGDGATYHEV
EFDALVFKPELQEVVEGEVVEVVEFGAFVRIGPVDGLLHISQIMDDYISYDPKNGRLIGKESKRVLKVGD
VVRARIVAVSLKERRPRGSKIGLTMRQPGLGKLEWIEEEKKKAKKEA
>gnl|CDD|236290 PRK08564, PRK08564, S-methyl-5'-thioadenosine phosphorylase
MIEPNEKASIGIIGGSGLYDPGIFENSKEVKVYTPYGEPSDNIIIGEIEGVEVAFLPRHGRGHRIPPHKI
NYRANIWALKELGVEWVIAVSAVGSLREDYKPGDFVIPDQFIDMTKKREYTFYDGPVVAHVSMADPFCPE
LRKIIIETAKELGIRTHEKGTYICIEGPRFSTRAESRMWREVFKADIIGMTLVPEVNLACELGMCYATIA
MVTDYDVWAEKPVTAEEVTRVMAENTEKAKKLLYEAIPRIPEERKCSCCDSLKTALV
>gnl|CDD|236291 PRK08565, PRK08565, DNA-directed RNA polymerase subunit B; Provisional
RWTVVEAYFKEKGLVRQHLDSYNDFIERGLQEIVDEFGEIKTEIPGLKIVLGKIRVGEPEIKEADGSERP
ITPMEARLRNLTYAAPLYLTMIPVENGIEYEPEEVKIGDLPIMVKSKICPLSGLSPDELIEIGEDPKDPG
GYFIINGSERVIVSQEDLAPNRVLVDKGEAGSSITHTAKVISSRAGYRAQVTVERRKDGTIYVSFPAVPG
KIPFVILMRALGLETDRDIVYAVSLDPEIQQELLPSLEQASSIAATVEDALDYIGKRVAIGQPREYRIER
AEQILDKYLLPHLGTSPEDRIKKAYFLGQMASKLLELYLGRREPDDKDHYANKRLRLAGDLLAELFRVAF
KQLVKDLKYQLEKSYARGRKLDLRAIVRPDIITERIRHALATGNWVGGRTGVSQLLDRTNYLSTLSHLRR
VVSPLSRGQPHFEARDLHGTQWGRICPFETPEGPNCGLVKNLALMAQISVGVDEEEVEEILYELGVVPVE
EAREEEYISWSRVYLNGRLIGYHPDGEELAEKIRELRRSGKISDEVNVAYIETGEINEVYVNCDSGRVRR
PLIVVENGKPKLTREHVEKLKKGELTFDDLVKMGVIEYLDAEEEENAYVALDPEDLTPEHTHLEIWPPAI
LGITASIIPYPEHNQSPRNTYQAAMAKQSLGLYAANFRIRTDTRGHLLHYPQRPLVQTRALEIIGYNDRP
AGQNAVVAVLSYTGYNIEDAIIMNKASIERGLARSTFFRTYETEERKYPGGQEDKIEIPEPNVRGYRGEE
YYRKLDEDGIVSPEVEVKGGDVLIGKTSPPRFLEELEELSLGLQERRDTSVTVRHGEKGIVDTVLITESP
EGNKLVKVRVRDLRIPELGDKFASRHGQKGVIGMLVPQEDMPFTEDGIVPDLIINPHAIPSRMTVGQLLE
SIAGKVAALEGRFVDATPFYGEPEEELRKELLKLGYKPDGTEVMYDGRTGEKIKAPIFIGVVYYQKLHHM
VADKIHARARGPVQILTRQPTEGRAREGGLRFGEMERDCLIGHGAAMLLKERLLDSSDKTTIYVCELCGH
IAWYDRRKNKYVCPIHGDKGNISPVEVSYAFKLLLQELMSMGISPRLKLGDKV
>gnl|CDD|236292 PRK08566, PRK08566, DNA-directed RNA polymerase subunit A'; Validated
SMMMIPKRIGSIKFGLLSPEEIRKMSVTKIITADTYDDDGYPIDGGLMDPRLGVIDPGLRCKTCGGRAGE
CPGHFGHIELARPVIHVGFAKLIYKLLRATCRECGRLKLTEEEIEEYLEKLERLKEWGSLADDLIKEVKK
EAAKRMVCPHCGEKQYKIKFEKPTTFYEERKEGLVKLTPSDIRERLEKIPDEDLELLGINPEVARPEWMV
LTVLPVPPVTVRPSITLETGQRSEDDLTHKLVDIIRINQRLKENIEAGAPQLIIEDLWELLQYHVTTYFD
NEIPGIPPARHRSGRPLKTLAQRLKGKEGRFRGNLSGKRVNFSARTVISPDPNLSINEVGVPEAIAKELT
VPERVTEWNIEELREYVLNGPEKHPGANYVIRPDGRRIKLTDKNKEELAEKLEPGWIVERHLIDGDIVLF
NRQPSLHRMSIMAHRVRVLPGKTFRLNLAVCPPYNADFDGDEMNLHVPQTEEARAEARILMLVQEHILSP
RYGGPIIGGIQDHISGAYLLTRKSTLFTKEEALDLLRAAGIDELPEPEPAIENGKPYWTGKQIFSLFLPK
DLNLEFKAKICSGCDECKKEDCEHDAYVVIKNGKLLEGVIDKKAIGAEQGSILDRIVKEYGPERARRFLD
SVTRLAIRFIMLRGFTTGIDDEDIPEEAKEEIDEIIEEAEKRVEELIEAYENGELEPLPGRTLEETLEMK
IMQVLGKARDEAGEIAEKYLGLDNPAVIMARTGARGSMLNLTQMAACVGQQSVRGERIRRGYRDRTLPHF
KPGDLGAEARGFVRSSYKSGLTPTEFFFHAMGGREGLVDTAVRTSQSGYMQRRLINALQDLKVEYDGTVR
DTRGNIVQFKYGEDGVDPMKSDHGKPVDVDRIIERVLGKEVE
>gnl|CDD|236293 PRK08568, PRK08568, preprotein translocase subunit SecY; Reviewed
MGFLDKLEPILERLPAVKRPKGHVPFKEKLKWTAIVLILYFILTNIPLYGISQSSQDLFELLRIIFAGSF
GTLLQLGIGPIVTAGIILQLLVGSKLINLDLSDPEDRALFQGLQKLLAIVMIALEAAPFVLAGAFGPATG
LASTPLLALLIFLQLFLGGILIILLDELVSKWGIGSGISLFILAGVSQTIFVGLFNWLTGGQGLPVGFIP
ALFSAITSGNLTLALLLTTRGLLLLGLITTIVIFLIVVYLESMRVEIPLSHGRVRGARGRYPLKFIYVSV
LPVILVRALQANIQLFGQLLQRLGIPILGTYDSSGASPISGLAYYLSPPHSPYDWIQDPLRAIIYALFMI
VLSILFAIFWVETTGLDPKTQARQLQNSGMQIPGFRRNPKVIEKVLERYIPPVTVIGGAIVGLLAVLADL
LGALGGGTGLLLTVSIVYQLYEEIAREQLMEMYPLLRRFLGE
>gnl|CDD|236294 PRK08569, rpl18p, 50S ribosomal protein L18P; Reviewed
MATGPRYKVPFRRRREGKTDYRKRLKLLLSGKPRLVVRKTNKHVIAQIVKYDPKGDRTLASAHSRELAKY
GWKGDTGNTPAAYLTGLLAGKKALKAGVEEAVLDIGLHRPTKGSRVFAALKGAIDAGLEIPHGEEVLPDE
DRIRGEHIAEYAESLKEENYKKQFSKYLERGLDPEDLPEHFEEVKEKILEEYE
>gnl|CDD|236295 PRK08570, rpl19e, 50S ribosomal protein L19e; Reviewed
MMDLSAQKRLAADILGVGVSRVWIDPEALEDVAEAITREDIRELIKEGVIKAKPKKGISRGRARERHEKR
KKGRRRGPGSRKGKKGARTPKKERWINRIRALRRYLRELRDEGKIDRKTYRKLYRKAKGGEFRSVSHLKT
YIEEHGLLKE
>gnl|CDD|181478 PRK08571, rpl14p, 50S ribosomal protein L14P; Reviewed
MKGIRSKVTRGLPVGARLVCADNTGAKEVEIISVKGYKGVKRRLPKAGVGDMVVVSVKKGTPEMRKQVLR
AVVVRQRKEYRRPDGTRVKFEDNAAVIVTPEGTPKGTEIKGPVAREAAERWPKIASIASIIV
>gnl|CDD|236296 PRK08572, rps17p, 30S ribosomal protein S17P; Reviewed
RNIGLDVKPPEEECDDPNCPFHGTLPVRGQVLEGTVVSDKMHKTVVVEREYLHYVPKYERYEKRRSRIHA
HNPPCIDAKVGDKVKIAECRPLSKTKSFVVVEKKERAE
>gnl|CDD|236297 PRK08573, PRK08573, bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase
LIPVALTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDM
GIDAAKTGMLSNREIIEAVAKTVSKYGFPLVVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPE
AEKLTGMKIRSVEDARKAAKYIVEELGAEAVVVKGGHLEGEEAVDVLYHNGTFREFRAPRVESGCTHGTG
CSFSAAIAAGLAKGLDPEEAIKTAKKFITMAIKYGVKIGKGHCPVNPMAWIEIPAERWRAYEELEEALEE
IEENAAVFAKLIPEVGMNIGYAIDPRYARTINDVAAVKGRIVRYMGRVKPVGPVEFGASDHLARAILTAM
KKDPEIRSAMNIKYSEELVEKAKSLGYTVAYIDRREEPEEVKAREGASIPWIIEEAYKQTGRRPDIIYDL
GDWGKEPMIRILGRTPVEVVEKLLRLIR
>gnl|CDD|236298 PRK08574, PRK08574, cystathionine gamma-synthase family protein
MRRGTDAVRGYRGSDPYGSLQPPIYLTALFRQEGEAYPSDRGFDLKYSREENPTLRPLEEALAKLEGGVD
ALAFNSGMAAISTLFFSLLKAGDRVVLPMEAYGTTLRLLKSLEKFGVKVVLAYPSTEDIIEAIKEGRTKL
VFIETMTNPTLKVIDVPEVAKAAKELGAILVVDNTFATPLLYRPLRHGADFVVHSLTKYIAGHNDVVGGV
AVAWSGEFLEELWEWRRRLGTIMQPFEAYLVLRGLKTLEVRFERQCRNAMAIAEFLSEHPKVAEVYYPGL
PSDPYHGVAKRLFGKDLYGGVVSFRVKGGRDAVLKFLRSLKLIKPSPSLGGVESLATYPVKSAASPIPEE
DRKALGITEDLVRLSVGLEDVEDLIEDLDQALGSI
>gnl|CDD|236299 PRK08575, PRK08575, 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
MKIKKALVGSYPRPVKLAKVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFRWDDIFDP
TISFISGVEKGGLQRFYDNNFYYRQPVIKEKINLKEENPYLQWLESAREIKEEVSLESKLKAVLPGPLTY
AVLSDNEYYKNLIELMEDYASVVNSLIKELSSVVDAVEIHEPSIFAKGIKRDTLEKLPEVYKTMAKNVNI
EKHLMTYFEINNLKRLDILFSLPVTYFGIDVIENLKKLGRVYTYLKGRKVYLGILNARNTKMEKISTIRR
IVNKVKRKGVSDIIVGNNTLFDFIPEVVAVKKLKLLGKLEKLEGGE
>gnl|CDD|236300 PRK08576, PRK08576, hypothetical protein; Provisional
MFNIIVRSRKDAKAVKAINERFYGGWNLEVSSLGGARKFEEVEDNLEEALEDDYFPILLLGREEKDLAEE
LIKELPPNSYVRVVPRKRVRNMRVEELYWNLEEAKARFRLGVSWSGSAYVLSPENGEGIEIHPDYDIFLA
IGEGFRKNMKKLLGVDIGENALVLRKLGGEHEVYSGPRKVAELEISKKIGKPTEVLWRIPYPEEVSLEKL
IEANREVLEAFEKASIKFLRKFEEWTVIVPWSGGKDSTAALLLAKKAFGDVTAVYVDTGYEMPLTDEYVE
KVAEKLGVDLIRAGVDVPMPIEKYGMPTHSNRWCTKLKVEALEEAIRELEDGLLVVGDRDGESARRRLRP
PVVERKTNFGKILVVMPIKFWSGAMVQLYILMNGLELNPLYYKGFYRLGCYICPSLRSWEIELLKRLPVL
PLILKKRPLYKFLVRKRK
>gnl|CDD|236301 PRK08577, PRK08577, hypothetical protein; Provisional
MRLYELVKVDSKGRITIPLEIREALGIREGMYVLLIADTDKKEIHLEPIALPGKKLVEIELVVEDRPGVL
AKITGLLAEHGVDILATECEELKRGELAECVIIVDLSKSDIDLEELEEELKKLEEVKEVEIRQIEA
>gnl|CDD|236302 PRK08578, PRK08578, preprotein translocase subunit SecF; Reviewed
MEVPEVDYMKYSNRQLIAIPLAVLLLSLLLLGGTFATTGSPVKLGIDFTGGTEITIQTNDASPDELESAL
SGEPGVDVRKGSGNGYIITFGSGDDTDVDKLADAVKEFFNVDSISELNYSEKQIGPTFGSQFQEQALKAV
GFAFIGMAVVVFLIFRTPVPSLAVILSAFSDIIIALALMNLFGIELSLATVAALLMLIGYSVDSDILLTT
RVLKRRGTFDESIKRAMRTGITMTLTTIAAMAVLYIVSTIPQAEVLANIAAVLIFGLLADLMNTWLLNAG
ILRWYKTEGKKR
>gnl|CDD|236303 PRK08579, PRK08579, anaerobic ribonucleoside triphosphate reductase; Provisional
MVQLMEMKKRDIIEEYAAWNSLDVNENANRYPGPTGFFAYVLEEALKESLVSLLPEPGLEAHFSGDIYIH
KLPYSLYIPYCTGHSISRLLEKGLKTPTIISRPARHFDTFVDHVANYLITMQHYFTGAQAFSSVEWYAGP
FIRKDGLDYRKIKQNIQRLVYNLNYPSRVGMQTPFTNFTVTLDAPKKMLEGDYAVYDGKKVGPLGEYEEE
AKLFLLALTEVLREGDALGQPFTFPIPTLMTTAKMLWDDPEVFEAVFTTAAKRGSFYWLNTRVVDPDASY
AMCCRINIDKNELMYAFGVGGKSRRDLEDAEEEYLEKLEKQRFGGLWAMPDITGSVNVTTVNLPRIALEA
RGDDDKFWELYEERLELVRITLDWFRERYVKLLKTYPEMYSMIKEYLEEFPSSHFNTIGIIGLPEAAAIY
LGEPKLWTEGSRRDWLEAAELMKKMVEFAVEKAREWMKETGTPWNVEEVPGESAAAKLAIKDLKLFPELR
EYLSDPENPIYSTSIAPYYGPLELWDRIEIEEKVQQEFTGGVMMHIFLGEEPDPEALAKLTKRIMNTKLV
YWSYTPAITVCNKCGRSTTGLYTRCPRCGSEDVEVWSRIIGYYRPLKNWNPYRKKEFWLRKHYSR
>gnl|CDD|236304 PRK08581, PRK08581, amidase domain-containing protein
MKKNKILIYLLSTTLVLPTLTSPTAYADDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSN
QDNNDKKFSTIDSSTSDSNNIIDFIYKNLPQTNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPR
NSEKSTNDSNKNSDSSIKNDTDTQSSKQDKADNQKAPSSNNTKPSTSNKQPNSPKPTQPNQSNSQPASDD
TANQKSSSKDNQSMSDSALDSILDQYSEDAKKTQKDYASQSKKDKTETSNTKNPQLPTQDELKHKSKPAQ
SFENDVNQSNTRSTSLFETGPSLSNNDDSGSFNVVDSKDTRQFIKSIAKDAHRIGQDNDIYASVMIAQAI
LESDSGQSALAKSPNHNLFGIKGAYEGNSVSFNTLEADGNQLYSINAGFRKYPSTKESLEDYADLIKNGI
DGNSTIYKPTWKSEAKSYKDATSHLSKTYATDPNYAKKLNSIIKHYNLTQFDDEKMPDLDKYESSIKDYD
DSSSEFKPFREYSGSSPYPHGQCTWYVYNRMKQFGTSISGDLGDAHNWNNRAQARGYQVSHTPKRHAAVV
FEAGQAGADQHYGHVAFVEKVNSDGSIVISESNVKGLGIISYRTIDAAAAEELSYITGK
>gnl|CDD|236305 PRK08582, PRK08582, RNA-binding protein S1
MSIEVGSKLQGKVTGITNFGAFVELPEGKTGLVHISEVADNYVKDINDHLKVGDEVEVKVLNVEDDGKIG
LSIKKAKDRPKRQHDRPRHEDNRGGGNDVAPKEDFEQKMSRFLKDSEDRLTSIKRNTESKRGGRGARRG
>gnl|CDD|236306 PRK08583, PRK08583, RNA polymerase sigma factor SigB; Validated
MKESSQPTKLTKEEVNKWIAEYQENQDEEAQEKLVKHYKNLVESLAYKYSKGQSHHEDLVQVGMVGLLGA
IRRYDPSFGRSFEAFAVPTIIGEIKRYLRDKTWSVHVPRRIKELGPKIKKAVDELTTELQRSPKISEIAD
RLGVSEEEVLEAMEMGKSYQALSVDHSIEADSDGSTVTLLDIVGQQEDGYELTEQRMILEKILPVLSDRE
KSIIQCTFIENLSQKETGERLGISQMHVSRLQRQAIKKLREAAFLDT
>gnl|CDD|181490 PRK08588, PRK08588, succinyl-diaminopimelate desuccinylase; Reviewed
EEEKIQILADIVKINSVNDNEIEVANYLQDLFAKHGIESKIVKVNDGRANLVAEIGSGSPVLALSGHMDV
VAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGELG
AKQLTEKGYADDLDALIIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEY
FDSIKKHNPYLGGLTHVVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNQNGAAQL
SLDIYSNHRPVASDKDSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKPDFPVIIFGPGNNLTAH
QVDEYVEKDMYLKFIDIYKEIIIQYLK
>gnl|CDD|181491 PRK08589, PRK08589, SDR family oxidoreductase
MKRLENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVK
DFASEIKEQFGRVDVLFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTS
SFSGQAADLYRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTGTSEDEAGKTFREN
QKWMTPLGRLGKPEEVAKLVVFLASDDSSFITGETIRIDGGVMAYTWPGEMLSDDSWKRTLE
>gnl|CDD|236307 PRK08591, PRK08591, acetyl-CoA carboxylase biotin carboxylase subunit; Validated
MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA
EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDD
EEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIE
IQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEK
NGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSIKQEDIVFRGHAIECRINAEDPAKNFMP
SPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIARMKRALSEFVIDGIKTTIP
LHLRLLNDPNFQAGDYNIHYLEKKLALQEEK
>gnl|CDD|181493 PRK08593, PRK08593, aspartate aminotransferase family protein
MSKAHQLIQEDEHYFAKSGRIKYYPLVIDHGYGATLTDVDGKTYIDLLASASSQNVGHAPPRVVEAIKAQ
ADKFIHYTPAYMYHEPLVRLAKKLCELAPGDFEKRVTFGLSGSDANDGIIKFARAYTGRPYIISFTNAYH
GSTYGSLSMSGISLNMRRKYGPLLPGFVHIPFPDKYRGMYEEPDANFVEEYLAPLKEMFEKYLPADEVAC
IVIETIQGDGGLLEPVPGYFEALYKFCREHGILFAVDDIQQGLGRTGKWSSISHFNITPDLMSFGKSLAG
GMPMSAIVGRKEIMESLEAPAHLFTTGANPVSCAAALATIDMIEDESLLQRSAEKGEYARKRFDQWVSKY
NFVGDVRGYGLSIGIDIVSDKKLKTRDNEAALKICNYCFEHGVVIIAVAGNVLRFQPPLVITYEQLDTAL
NTIEQAFTALEAGKLDQPDISGQGW
>gnl|CDD|236308 PRK08594, PRK08594, enoyl-[acyl-carrier-protein] reductase FabI
MMLSLEGKTYVVMGVANKRSIAWGIARSLHNAGAKLVFTYAGERLEKEVRELADTLEGQESLLLPCDVTS
DEEITACFETIKEEVGVIHGVAHCIAFANKEDLRGEFLETSRDGFLLAQNISAYSLTAVAREAKKLMTEG
GSIVTLTYLGGERVVQNYNVMGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRTLSAKGVGGFNSILK
EIEERAPLRRTTTQEEVGDTAAFLFSDLSRGVTGENIHVDSGYHIIG
>gnl|CDD|181495 PRK08596, PRK08596, acetylornithine deacetylase; Validated
VSQLLEQIELRKDELLELLKTLVRFETPAPPARNTNEAQEFIAEFLRKLGFSVDKWDVYPNDPNVVGVKK
GTESDAYKSLIINGHMDVAEVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIEL
PGDLIFQSVIGEEVGEAGTLQCCERGYDADFAVVVDTSDLHMQGQGGVITGWITVKSPQTFHDGTRRQMI
HAGGGLFGASAIEKMMKIIQSLQELERHWAVMKSYPGFPPGTNTINPAVIEGGRHAAFIADECRLWITVH
FYPNETYEQVIKEIEEYIGKVAAADPWLRENPPQFKWGGESMIEDRGEIFPSLEIDSEHPAVKTLSSAHE
SVLSKNAILDMSTTVTDGGWFAEFGIPAVIYGPGTLEEAHSVNEKVEIEQLIEYTKVITAFIYEWCHTKK
E
>gnl|CDD|181497 PRK08600, PRK08600, putative monovalent cation/H+ antiporter subunit C; Reviewed
MEILMIIVIGILTAIAVYLILSKSLLRIIIGTTLLSHGANLLLLTMGGLKKGAVPILGEGVTSYVDPLPQ
ALILTAIVISFGVTAFFLVLAYRTYKELGTDNVEQMRGVPEDD
>gnl|CDD|236310 PRK08601, PRK08601, NADH dehydrogenase subunit 5; Validated
MLIMLSSQTLLTLFFIALIIALLSGLLFLNPRMPLRYVRIHIGILALPSLVALLGLIGANGDVVVGPWHL
DTLAWLMAFFVLTLGFIIQRFSVRYLLGDRSYRKYFALFTFTTGFASLAWLSGDLRLMALCWGATLLGLT
LLIGLNKGWKVAREAAKISGMLFLISWLALALAIVWLFIATGEWQLTSVLSNENLAQLGTWEKTGINLLL
ILAVMIPAAQWPFQRWLIESAVAPTPVSAIMHAGLVNAGGIMLTRFSPLFHDDIAQILLLIFASISVLIG
TGISLVQVDYKRQLVGSTMAQMGFMLVQCALGAYSAAIIHLILHGLFKATLFLQSGSAVPRFNIVKQANE
KKSYLWIVVGRVLGLLIAIAFWLSSPGEGYQLLSALILGWSLYVSWNQLVAFGEGRMGRIAGLIVLAGVA
LIYFIVHNSFYKWLHTIMYQSVQPPASAVIIVIAILLFGSLLSIWVARRRSSTLFAVLYLWLVRLGEARP
KSVESHPNYLKHYLSKGGN
>gnl|CDD|181499 PRK08605, PRK08605, D-lactate dehydrogenase; Validated
MTKIKIMSVRDEDAPYIKAWAEKHHVEVDLTKEALTDDNVEEVEGFDGLSLSQQIPLSEAIYKLLNELGI
KQIAQRSAGFDTYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRHFNQIQTKVREHDFRWEPPIL
SRSIKDLKVAVIGTGRIGLAVAKIFAKGYGSDVVAYDPFPNAKAATYVDYKDTIEEAVEGADIVTLHMPA
TKYNHYLFNADLFKHFKKGAVFVNCARGSLVDTKALLDALDNGLIKGAALDTYEFERPLFPSDQRGQTIN
DPLLESLINREDVILTPHIAFYTDAAVKNLIVDALDATLEVLQTGTTRLRVN
>gnl|CDD|236311 PRK08609, PRK08609, DNA polymerase/3'-5' exonuclease PolX
MNKKDVIKLLETIATYMELKGENPFKISAFRKAAQALELDERSLSEIDDFTKLKGIGKGTAEVIQEYRET
GESSVLQELKKEVPEGLLPLLKLPGLGGKKIAKLYKELGVVDKESLKEACENGKVQALAGFGKKTEEKIL
EAVKELGKRPERLPIAQVLPIAQEIEEYLATIDEIIRFSRAGSLRRARETVKDLDFIIATDEPEAVREQL
LQLPNIVEVIAAGDTKVSVELEYEYTISVDFRLVEPEAFATTLHHFTGSKDHNVRMRQLAKERGEKISEY
GVEQADTGEVKTFESEEAFFAHFGLPFIPPEVREDGSEFERYKDLSNLITLSDIQGDLHMHTTWSDGAFS
IEEMVEACIAKGYEYMAITDHSQYLKVANGLTEERLLEQAEEIKALNEKYPEIDILSGIEMDILPDGSLD
YDDEVLAELDYVIAAIHSSFSQSEEEIMKRLENACRNPYVRLIAHPTGRLIGRRDGYDVNIDQLIELAKE
TNTALELNANPNRLDLSAEHLKKAQEAGVKLAINTDAHHTEMLDDMKYGVATARKGWIQKDRVINTWSRE
EFKDFIKRNK
>gnl|CDD|181501 PRK08610, PRK08610, fructose-bisphosphate aldolase; Reviewed
MPLVSMKEMLIDAKENGYAVGQYNLNNLEFTQAILEASQEENAPVILGVSEGAARYMSGFYTVVKMVEGL
MHDLNITIPVAIHLDHGSSFEKCKEAIDAGFTSVMIDASHSPFEENVATTKKVVEYAHEKGVSVEAELGT
VGGQEDDVVADGIIYADPKECQELVEKTGIDALAPALGSVHGPYKGEPKLGFKEMEEIGLSTGLPLVLHG
GTGIPTKDIQKAIPFGTAKINVNTENQIASAKAVRDVLNNDKEVYDPRKYLGPAREAIKETVKGKIKEFG
TSNRAK
>gnl|CDD|181502 PRK08611, PRK08611, pyruvate oxidase; Provisional
MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIG
VCLSIGGPGAIHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLP
EIVNQAIRTAYEKKGVAVLTIPDDLPAQKIKDTTNKTVDTFRPTVPSPKPKDIKKAAKLINKAKKPVILA
GLGAKHAKEELLAFAEKAKIPIIHTLPAKGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPY
VDYLPKKAKAIQIDTDPANIGKRYPVNVGLVGDAKKALHQLTENIKHVEDRRFLEACQENMAKWWKWMEE
DENNASTPIKPERVMAAIQKIADDDAVLSVDVGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAA
KIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGELEYAIDLSDMDYA
KFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNAAPLPGKIVNDEALGYSKWAIKSLFEDK
KLDQMPPLKKALKRFL
>gnl|CDD|236312 PRK08617, PRK08617, acetolactate synthase AlsS
TDKKKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGV
VLVTSGPGVSNLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSE
VLANAFRAAESGRPGAAFVSLPQDVVDAPVTSKAIAPLSKPKLGPASPEDINYLAELIKNAKLPVLLLGM
RASSPEVTAAIRRLLERTNLPVVETFQAAGVISRELEDHFFGRVGLFRNQPGDELLKKADLVITIGYDPI
EYEPRNWNSEGDATIIHIDVLPAEIDNYYQPERELIGDIAATLDLLAEKLDGLSLSPQSLEILEELRAQL
EELAERPARLEEGAVHPLRIIRALQDIVTDDTTVTVDVGSHYIWMARYFRSYEPRHLLFSNGMQTLGVAL
PWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQEEMKYGRSSGVDF
GPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVDYSDNIKLMEQLLPDQL
>gnl|CDD|236313 PRK08618, PRK08618, ornithine cyclodeaminase family protein
MLVLSAEDQKKLFNMNEAIEADKEALKAYSEGKTITPLRTNLPFPNENNTSLIMPGYAEGLEALGLKIVS
VVPENKKKGKPTIPGTVILSDFETGEVLAILDGTYLTQIRTGALSGVATKYLAREDAKTLCLIGTGGQAK
GQLEAVLAVRDIERVRVYSRTFEKAYAFAQEIQSKFNTEIYVVNSADEAIEEADIIVTVTNAKTPVFSEK
LKKGVHINAVGSFMPDMQELPSEAIARANKVVVESKEAALEETGDLIVPLKEGLISKDDIHGELGQIISG
EIAGRESDEEITVFKSVGLAVVDIVVAKYIYEKAVENGVGKEIEF
>gnl|CDD|181505 PRK08621, PRK08621, galactose-6-phosphate isomerase subunit LacA; Reviewed
MAIIIGADKAGFELKEVVKDYLEDNKYEVVDVTEEGAEDFVDSTLAVAKEVNKSEDNLGIVIDAYGAGSF
MVATKIKGMVAAEVSDERSAYMTRGHNNARMITMGSEIVGDGLAKNIIKGFVEGKYDGGRHQIRVDMLNK
MC
>gnl|CDD|181506 PRK08622, PRK08622, galactose-6-phosphate isomerase subunit LacB; Reviewed
MKIAIGCDHIVTDEKMAVSDYLKSKGHEVIDVGTYDFTRTHYPIFGKKVGEAVASGEADLGVCICGTGVG
ISNAVNKVPGIRSALVRDMTSALYAKEELNANVIGFGGKITGELLMCDIIDAFINAEYKPTEENKKLIEK
IDHLEKPNADQANPHFFDEFLEKWDRGEYHD
>gnl|CDD|236314 PRK08624, PRK08624, hypothetical protein; Provisional
MMDKDELKESLTPEDIIKILEEVGCENVRGKDGNTIAETACHNDGGGSTKLYYYIENDNFHCYTRCGDIF
DVFELLCKRLKMEGKALSFSKAIRKITKILGLSYFYEPKQQGIKPSFLKILDWVWTGKKEKKEKIQPQLK
SFNENILNQFVKIPNRKWLDEGISEKTQKYWEIKFYLDVISQRIIIPHRDESGELIGIRGRLLDKELVDK
NKYFPIYVNDTGYNHPKGKILYGLWQNKKYIKEKKKVIIVESEKSVLFSDKFYGEGNFVVAICGSNISEV
QAEKLLRLGVEEVTIALDKEYMDVTEEEVYEYIKKLMKPVKTFAPYVNIYILKDEAGLLKYKDSPPDDNK
DTLEELMSVYRKEVPVIEWKNNG
>gnl|CDD|181507 PRK08626, PRK08626, fumarate reductase flavoprotein subunit; Provisional
MKIIYTDALVIGAGLAGLRVAIAAAQRGLDTIVLSLVPAKRSHSAAAQGGMQASLGNAVKGEGDNEDVHF
ADTVKGSDWGCDQEVARMFVHTAPKAVRELAAWGVPWTRVTAGPRTVVINGEKVTITEKEEAHGLINARD
FGGTKKWRTCYTADGTGHTMLYAVDNEAIKLGVPVHDRKEAIALIHDGKRCYGAVVRCLITGELRAYVAK
ATLIATGGYGRIYKVTTNAVICEGIGAAIALETGVAPLGNMEAVQFHPTAIVPSGILVTEGCRGDGGLLR
DKDGYRFMPDYEPEKKELASRDVVSRRMTEHIRKGKGVKSPYGPHLWLDIRILGRKHIETNLREVQEICE
NFLGIDPAKDWIPVRPTQHYSMGGIRTNPTGESYGLKGLFSAGEAACWDMHGFNRLGGNSLAETVVAGMI
VGKYVADFCLGNELEIDTALVEKFVKKQQDRIDELIAGEGKENVFEIKNEMQEIMMEKVGIFRNGPELEK
AVKELQELLERSKNIGLKSKKRGANPELEEALRVPRMLKLALCVAYGALARTESRGAHAREDYPKRNDRD
WLNRTLASWPEGEALEPTLEYEPLDVMKMELPPGFRGYGAGNIIEHPDTEKRQAEIDKILAELGEGKDRY
EIQHALMPFELPEKYKAKNERLGDTLE
>gnl|CDD|181508 PRK08628, PRK08628, SDR family oxidoreductase
MDLNLKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEFAEELRALQPRAEFVQVDLTDDAQC
RDAVEQTVAKFGRIDGLVNNAGVNDGVGLEAGREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISS
KTALTGQGGTSGYAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTPLYENWIATFDDPEAKLAAITA
KIPLGHRMTTAEEIADTAVFLLSERSSHTTGQWLFVDGGYVHLDRALT
>gnl|CDD|181509 PRK08629, PRK08629, coproporphyrinogen III oxidase family protein
MIQTLNGYQANITVPNLALSYMERVMQKSVDKNLRLDTLSADMMPAPVEGKKYMLYAHVPFCHTLCPYCS
FHRFYFKEDKARAYFISLRKEMEMVKELGYDFESMYVGGGTTTILEDELAKTLELAKKLFSIKEVSCESD
PNHLDPPKLKQLKGLIDRLSIGVQSFNDDILKMVDRYEKFGSGQETFEKIMKAKGLFPIINVDLIFNFPG
QTDEVLQHDLDIAKRLDPRQITTYPLMKSHQTRKSVKGSLGASQKDNERQYYQIINELFGQYNQLSAWAF
SKKNDEGFDEYVIDYDEYLGVGSGSFSFLDGTLYVNTFSLRDYQERIAAGQMGVIAQKNFSKKEVMQYRF
LLGMFSGRLSIKYFRETFGVNLDKALFKEMLLLKLIGAIKNDPGDLIVTDFGKYLGVVMMKEFYTGMDNV
RAQFRDPLKLCDM
>gnl|CDD|236315 PRK08633, PRK08633, 2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
MMKNLLKIIGFLPLLLTQFLNAFNDLGHKILIQNTLIKAYDGSEQVILTAIVNALFLLPFLLLSSPAGFL
ADKFSKNRVIRIVKLFEVGLTLLIVLAYYLGWFWLAFAVTFLLGAQSAIYSPAKYGIIPELVGKENLSRA
NGLLEAFTIVAILAGTALFSFLFESVNGNTPSEILGRIAPAGLVLLAVAVLGLIFAYRLPKVPAAAPEVF
DKKKYLFPKLLWRNLKLLRSDRVLWLAIIGLSYFWFISQLAQANFPAYAKEVLGLDNTFQVQYLLAASAI
GIGIGSLLAGRLSGRHIELGLVPLGALGLALSLFLLPTAPSLASVLVLFFLFGFSAGLFIVPLNALIQFR
APEKELGKVLAANNFLQNVGMLLFLALTTLFSGLGLSPAGLFYLIALVTLIGTLYTLLLLPDSLLRFLLL
LLMHTRYRLRVEGRENIPAKGGALLLGNHVSWIDWALLQAASPRPIRFVMERSIYEKWYLKWFFKLFGVI
PISSGGSKESLEFIRKALDDGEVVCIFPEGAITRNGQLNEFKRGFELIVKGTDVPIIPFYIRGLWGSIFS
RASGKFLWRWPTRIPYPVTVAFGKPMPAHSTAHEVKQAVFELSFDSWKSRKEALPPLAEAWIDTAKRNWS
RLAVADSTGGELSYGKALTGALALARLLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVNLNYTAS
EAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKVIYLEDLKAKISKVDKLTALLAARLLPARL
LKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTV
TLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKL
KPEVADAFEEKFGIRILEGYGATETSPVASVNLPDVLAADFKRQTGSKEGSVGMPLPGVAVRIVDPETFE
ELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGE
MVPLGAVEEELAKALGGEEVVFAVTAVPDEKKGEKLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFK
VEALPLLGSGKLDLKGLKELALALLG
>gnl|CDD|236316 PRK08636, PRK08636, LL-diaminopimelate aminotransferase
MFDEIEFNKIKRLPKYVFAEVNELKMAARRAGEDIIDFSMGNPDGPTPQHIIDKLCESAQKPKTHGYSVS
KGIYKLRLAICNWYKRKYNVDLDPETEVVATMGSKEGYVHLVQAITNPGDVAIVPDPAYPIHSQAFILAG
GNVHKMPLEYNEDFELDEDQFFENLEKALRESSPKPKYVVVNFPHNPTTATVEKSFYERLVALAKKERFY
IISDIAYADITFDGYKTPSILEVEGAKDVAVESYTLSKSYNMAGWRVGFVVGNKKLVGALKKIKSWLDYG
MFTPIQVAATIALDGDQSCVEEIRETYRKRRDVLIESFANAGWELQKPRASMFVWAKIPEPARHLGSLEF
SKQLLTEAKVAVSPGIGFGEYGDEYVRIALIENENRIRQAARNIKKFLKELEG
>gnl|CDD|181512 PRK08637, PRK08637, hypothetical protein; Provisional
EKATKYNATIGMATEKGGPMYLSSLQDLLNDLTPDEIFPYAPPQGIPELRDLWQEKMLRENPSLSGKKMS
LPIVTNALTHGLSLVADLFVDQGDTVLLPDHNWGNYKLTFNTRRGAEIVTYPIFDEDGGFDTDALKEALQ
AAYNKGKVIVILNFPNNPTGYTPTEKEATAIVEAIKELADAGTKVVAVVDDAYFGLFYEDSYKESLFAAL
ANLHSNILAVKLDGATKEEFVWGFRVGFITFGTKAGSSQTVKEALEKKVKGLIRSNISNGPHPSQSAVLR
ALNSPEFDKEKQEKFQILKERYEKTKEVLYDGKYDDAWQAYPFNSGYFMCLKLKGVDAEELRVHLLEKYG
IGTIALNETDLRIAFSCVEEEDIPELFDSIYKAIKDLR
>gnl|CDD|236317 PRK08638, PRK08638, bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB
MHITYDLPVAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLT
DAEKRKGVVACSAGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEE
IVEEEGRTFIPPYDDPKVIAGQGTIGLEILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQS
ENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVV
TEGAGALATAALLSGKLDQYIQNKKVVAIISGGNVDLSRVSQITGHVVAADAS
>gnl|CDD|236318 PRK08639, PRK08639, threonine dehydratase; Validated
MTVKMTVSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDE
ELAAGVVCASAGNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEFVEIVLVGDTFDDSAAAAQ
EYAEETGATFIPPFDDPDVIAGQGTVAVEILEQLEKEGSPDYVFVPVGGGGLISGVTTYLKERSPKTKII
GVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLTFEILKDVVDDVVLVPEGAVCTTILELYNK
EGIVAEPAGALSIAALELYKDEIKGKTVVCVISGGNNDIERMPEIKERSLIYEGLKHYFIVNFPQRPGAL
REFLDDVLGPNDDITRFEYLKKNNRETGPVLVGIELKDAEDYDGLIERMEAFGPSYIDINPNEPLYNLLI
>gnl|CDD|181515 PRK08640, sdhB, succinate dehydrogenase iron-sulfur subunit; Reviewed
MSEKTVRLIIKRQDGPDSKPYWEEFEIPYRPNMNVISALMEIRRNPVNAKGEKTTPVVWDMNCLEEVCGA
CSMVINGKPRQACTALIDQLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIPIDGTYDLGPGPRM
PEEKRQWAYELSKCMTCGCCLEACPNVNEKSDFIGPAAISQVRLFNAHPTGEMHKEERLRALMGDGGIAD
CGNAQNCVRVCPKGIPLTTSIAAMNRETTKQSFKSFFGS
>gnl|CDD|236319 PRK08641, sdhA, succinate dehydrogenase flavoprotein subunit; Reviewed
MAKGKVIVVGGGLAGLMATIKAAEAGVHVDLFSLVPVKRSHSVCAQGGINGAVNTKGEGDSPWIHFDDTV
YGGDFLANQPPVKAMCEAAPGIIHLLDRMGVMFNRTPEGLLDFRRFGGTLHHRTAFAGATTGQQLLYALD
EQVRRYEVAGLVTKYEGWEFLGAVLDDEGVCRGIVAQDLFTMEIESFPADAVIMATGGPGIIFGKSTNST
INTGSAASRVYQQGAYYANGEFIQIHPTAIPGDDKLRLMSESARGEGGRVWTYKDGKPWYFLEEKYPAYG
NLVPRDIATREIFDVCVEQKLGINGENMVYLDLSHKDPKELDIKLGGILEIYEKFTGDDPRKVPMKIFPA
VHYSMGGLWVDYDQMTNIPGLFAAGECDYSYHGANRLGANSLLSAIYGGMVAGPNAVEYIKGLGKSADDV
SSSVFEQALKQEQEKFDNILSMDGTENAYVLHKELGEWMTDNVTVVRENDKLLETDEKIQELMERYKRIS
VNDTSRWSNQGASFTRQLWNMLELARVITIGALNRNESRGAHYKPEFPERNDENWLKTTMATYTPEGEEP
EFSYEDVDTSLIPPRKRDYTSKKKGAKKL
>gnl|CDD|181517 PRK08642, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
MQISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEALADELGDRAIALQADVTDREQVQAM
FATATEHFGKPITTVVNNALADFSFDGDARKKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGR
IINIGTNLFQNPVVPYHDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASAATPDEVFDLIA
ATTPLRKVTTPQEFADAVLFFASPWARAVTGQNLVVDGGLVMN
>gnl|CDD|181518 PRK08643, PRK08643, (S)-acetoin forming diacetyl reductase
MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAV
RQVVDTFGDLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHGGKIINATSQ
AGVVGNPELAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFDIAHQVGENAGKPDEWGME
QFAKDITLGRLSEPEDVANCVSFLAGPDSDYITGQTIIVDGGMVFH
>gnl|CDD|236320 PRK08644, PRK08644, sulfur carrier protein ThiS adenylyltransferase ThiF
RGEIPSMEEFEAMLASRHTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNR
QQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDEDNIEELFKDCDIVVEAFDNAETKAMLVETVLE
HPGKKLVAASGMAGYGDSNSIKTRRIGKNFYIVGDFVTEAKPGNPLMAPRVNIAAAHQANLVLRLILGEE
VA
>gnl|CDD|236321 PRK08645, PRK08645, bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; Reviewed
MMKLLERLKERVLIADGAMGTLLYSRGVPLDRCFEELNLSHPELILRIHREYIEAGADVIQTNTFGANRI
KLKRYGLEDKVKEINRAAVRLAREAAGDDVYVAGTIGPIGGRGPLGDISLEEIRREFREQIDALLEEGVD
GLLLETFYDLEELLLALEAAREKTDLPIIAQVAFHEDGVTQNGTSLEEALKELVAAGADVVGLNCGLGPY
HMLEALERIPIPENAPLSAYPNAGLPEYVDGRYVYSANPEYFAEYALEFVEQGVRLIGGCCGTTPEHIRA
MARALKGLKPVTEKEVKPRPKVVVTEEPLKAKSSLLDKLKKGKTVIVELDPPKGLDTDKFLEGAKALKEA
GVDAITLADNPLARVRISNIALASLIKRELGIEPLVHITCRDRNLIGLQSHLLGLHALGIRNVLAITGDP
AKVGDFPGATSVYDLNSFGLIKLIKQLNEGISYSGKPLGKKTNFSIGGAFNPNVRNLDKEVKRLEKKIEA
GADYFITQPVYDEELIEELLEATKHLGVPIFIGIMPLVSYRNAEFLHNEVPGITLPEEIRERMRAVEDKE
EAREEGVAIARELIDAAREYFNGIYLITPFLRYEMALELIKYIKSKQEVKEG
>gnl|CDD|236323 PRK08651, PRK08651, succinyl-diaminopimelate desuccinylase; Reviewed
VEAMMFDIVEFLKDLIKIPTVNPPGENYEEIAEFLRDTLEELGFSTEIIEVPNEYVKKHDGPRPNLIARR
GSGNPHLHFNGHYDVVPPGEGWSVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAGDGNIELA
IVPDEETGGTGTGYLVEEGKVTPDYVIVGEPSGLDNICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEA
AAKIAERLKSSLSTIKSKYEYDDERGAKPTVTLGGPTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRD
ELEALLDEVAPELGIEVEFEITPFSEAFVTDPDSELVKALREAIREVLGVEPKKTISLGGTDARFFGAKG
IPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVLKRLAKGS
>gnl|CDD|236324 PRK08652, PRK08652, acetylornithine deacetylase; Provisional
TERAKELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIESDGEVINIVVNSKAELFVEVHYDTVPVR
AEFFVDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSDEEEGGRGSALFAERYRPKMAIV
LEPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPHIGIQEII
GGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEYTEIWDGFELDEDEEIVQLLEKAMK
EVGLEPEFTVMRSWTDAINFRYNGTKTVVWGPGELDLCHTKFERIDVREVEKAKEFLKALNEILLES
>gnl|CDD|236325 PRK08654, PRK08654, acetyl-CoA carboxylase biotin carboxylase subunit
MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVA
KKAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIED
IEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIE
IQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSN
GNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSFKQEDITIRGHAIECRINAEDPLNDFAPS
PGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIARMRRALYEYVIVGVKTNIPF
HKAVMENENFVRGNLHTHFIEEETTILEEMKRYALEEEEREKTLSEKFFPGNKKVAAIAAAVNAYISSAK
KDNEEIKKK
>gnl|CDD|236326 PRK08655, PRK08655, prephenate dehydrogenase; Provisional
MKISIIGGTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKELGVEYANDNIDAAKDADIVIISVPINV
TEDVIKEVAPHVKEGSLLMDVTSVKERPVEAMEEYAPEGVEILPTHPMFGPRTPSLKGQVVILTPTEKRS
NPWFDKVKNFLEKEGARVIVTSPEEHDRIMSVVQGLTHFAYISIASTLKRLGVDIKESRKFASPIYELMI
DIIGRILGQNPYLYASIQMNNPQIPEIHETFIKECEELSELVKNGDREEFVERMKEAAKHFGDTERALGR
SDKAIYALNQEFEKLLKSIGKEIGLKHIYSGKIHVGILKKVTPDYVTLKKNNKEIKLKISNIRLLSEKEL
REWKKKNLEKYVRDISVLFPKGADPEVILDLLDNLKHVFDIEIIDVYSGKQIEEGYLSVTFRITVFGKED
LENVEEILEGIGGKIRY
>gnl|CDD|181526 PRK08659, PRK08659, 2-oxoacid:acceptor oxidoreductase subunit alpha
MTKVDFLQGNEACAEGAIAAGCRFFAGYPITPSTEIAEVMARELPKVGGVFIQMEDEIASMAAVIGASWA
GAKAMTATSGPGFSLMQENIGYAAMTETPCVIVNVQRGGPSTGQPTKPAQGDMMQARWGTHGDHPIIALS
PSSVQECFDLTIRAFNLAEKYRTPVIVLADEVVGHMREKVVLPEPDEIEIIERKLPKVPPEAYKPFDDPE
GGVPPMPAFGDGYRFHVTGLTHDERGFPTTDPETHEKLVRRLVRKIEKNRDDIVLYEEYMLEDAEVVVVA
YGSVARSARRAVKEAREEGIKVGLFRLITVWPFPEEAIRELAKKVKAIVVPEMNLGQMSLEVERVVNGRA
KVEGINKIGGELITPEEILEKIKEVA
>gnl|CDD|181527 PRK08660, PRK08660, aldolase
MWQEFARIGKKLFAHGLVSSHFGNISVRTGDGLLITRTGSMLDEITEGDVIEVGIDDDGSVDPLASSETP
VHRAIYRRTSAKAIVHAHPPYAVALSLLEDEIVPLDSEGLYFLGTIPVVGGDIGSGELAENVARALSEHK
GVVVRGHGTFAIGKTLEEAYIYTSQLEHSCKVLYLVRTAKK
>gnl|CDD|236328 PRK08662, PRK08662, nicotinate phosphoribosyltransferase; Reviewed
MMRFYIASEEEIKSGKTTDIYFERTVEILEHAGKNPKVVAEVTASSLPKGEWGVFAGLEEVLELLEGKPV
DVYALPEGTLFDPKEPVMRIEGPYLEFGIYETALLGILAHASGIATAAARCKEAAGDKPVLSFGARHVHP
AIAPMMDRAAYIGGCDGVSGVLGAELLGIEPSGTMPHALILIFGDQVEAWKAFDEVVPPDVPRIALVDTF
KDEREEALRAAEALGDRLDGVRLDTPSSRRGNFRKIVREVRWTLDIRGYEHVKIFVSGGLDPERIRELRD
VVDGFGVGTYISFAPPVDFSMDIVEVEGKPIAKRGKLPGIKQVPRLKEIREYVLEQLEELGLS
>gnl|CDD|236329 PRK08664, PRK08664, aspartate-semialdehyde dehydrogenase; Reviewed
MMKLKVGILGATGMVGQRFVQLLANHPWFEVTALAASERSAGKTYGEAVRWQLDGPIPEEVADMEVVSTD
PEAVDDVDIVFSALPSDVAGEVEEEFAKAGKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVQRKRRGW
DGFIVTNPNCSTIGLVLALKPLMDFGIERVHVTTMQAISGAGYPGVPSMDIVDNVIPYIGGEEEKIEKET
LKILGKFEGGKIVPADFPISATCHRVPVIDGHTEAVFVKFKEDVDPEEIREALESFKGLPQELGLPSAPK
KPIILFEEPDRPQPRLDRDAGDGMAVSVGRLREDGIFDIKFVVLGHNTVRGAAGASVLNAELLKKKGYL
>gnl|CDD|236330 PRK08665, PRK08665, vitamin B12-dependent ribonucleotide reductase
MKMPADLPDMKLTDNALTVLEKRYLKKDEDGKPIETPEDMFRRVARTIAAAELIYDSKADVEALADRFYD
LMTSLEFLPNSPTLMNAGRELGQLSACFVLPVGDSIEEIFDAVKHAALIHKSGGGTGFSFSRLRPKNDRV
GSTGGVASGPVSFMRVFDAATEAIKQGGTRRGANMGILRVDHPDIMEFITCKEDNGELTNFNISVAITEA
FMEAVEADEEYDLINPRTGEVVGRLNAREVFDLIVEMAWENGEPGIVFIDRINRDNPTPHLGEIESTNPC
GEQPLLPYESCNLGSINLSKMVKNGDVDWEKLREVVHLAVRFLDNVIDANKYPLPQIEEMTKGNRKIGLG
VMGWADMLIQLGIPYDSEEAVELAEKVMKFIQDEAHAASRELAEERGPFPNYEGSIYDKDGLGPMRNATV
TTIAPTGTISIIAGCSSGIEPLFALSFTRNVMDGERLVEVNPVFEAAAKEEGFYSEELMEKIAEKGSIQD
IDEVPEDVRRVFVTAHDISPEWHVRMQAAFQKHTDNAVSKTVNFPNEATIEDVREVYRLAYELGCKGVTI
YRDGSRDEQVLSTGKKEKKEEEPAAAVEPKKLEPRPRPKVTKGFTEKVQTGCGPLYVTVNEDEGGPFEVF
TTLGKAGGCAAAQSEAIGRLVSLALRSGVDVREIVKQLKGIRCPSPAGQGGNKVLSCPDAIAKVLEKHYL
GGGKDVGAGNGTGSAGIEAPAPERGACPECGSILEHEEGCVVCHSCGYSKCG
>gnl|CDD|169548 PRK08666, PRK08666, 5'-methylthioadenosine phosphorylase; Validated
MVRIAIIGGSGVYDPKILENIREETVETPYGEVKVKIGTYAGEEVAFLARHGEGHSVPPHKINYRANIWA
LKELGVERILATSAVGSLNPNMKPGDFVILDQFLDFTKNRHYTFYDGGESGVVHVDFTDPYCPELRKALI
TAARELGLTYHPGGTYVCTEGPRFETAAEIRMFRILGGDLVGMTQVPEAVLARELEMCYATVAIVTNYAA
GISPTKLTHSEVVELMAQNSENIKKLIMKAIELIPKERRCPCKDALKGATG
>gnl|CDD|236331 PRK08667, PRK08667, hydrogenase membrane subunit; Validated
MLAGLFLGAILLLLAAAVIPLVFRHKRKRVWQSVLWLVIAIALLLFAGSLQLFTGNPLDIPLWGIAPGLD
ITFHIDRLAAFFIILIGLVSLCVAIYSLGYNEHMSSNERANLLSALTALFILSMLGVVASANTFSFLFFW
EIMALSSFFLVMNDYQEEETQRAGIFYFVMTQLSTVFLMLGIIVLFIQTGSFELSPLGASAGILSLVFLL
LFLGFGIKAGIIPFHKWLPYAHPASPSNVSALMSGVMLKVAVYGLVRFLMDVLSPELWWGVLILLAGSIS
ALLGVIYALKEHDLKGLLAYSSIENIGIILMGIGLYVIFGVYGLDTLALLALGGALFHSLNHALFKSLLF
LTAGSVVHATGTRNIEKMGGLVKLMPYTSALFLVGAVSIAALPPFNGFASELLLYESFFQSFSVADPLIK
ILLFSVLAIFALTSALAAACFVKAFGITFLAMPRSQEARSAKEVSKPMLIGPAVLAVACLVLGLFSVQIF
SLAGYSFDLPDLLLVGLLLVIFGVLVFGMVRLFSPRKSRISETWACGYPRPTPRMEYTASGFSEPLVQIF
RLIYRTRIYNEREYEDNQQAIFKQGKSEIHLLKFFEEYLYLPPARLIGRISRYVSRLQNGDLDSYVLYVF
LTVLVVILALGWLA
>gnl|CDD|236332 PRK08668, PRK08668, NADH dehydrogenase subunit M; Validated
MELTLLLLTPLIGSVLAYLLKKINEKIGVIGNALPLLFLIKLYFTLKVGTGEKLTLFFGGFKLTFTLTHL
SWFFAMISLLVIFSVAFFMVSEKTKNDAYFNMFALMSLAGVLGVFLANDLLTLYIFWEIMTFSSFMMVPM
GKKESRKASLKYFVLSAIGAYAMLYAIFLIYAKTGTFDFADISQGLINDTSTGFALIVFLFLLAFGVAKA
GIFPLHVWAPDAYSEAPQSFSAVLSGQLSKLGAYGFLLVLYVLPGTKLFSEFGTYRGVPLFNYILAWLGN
ISIIVGTLMAILQEDIKKLIAYSSVANGGYILVGLGLGTSLGFAGGLFHVFNHALFKGLFFLIFAAVIYR
TGTTKISEMGGLIEKMPFTFAMYLVAIISLAGIPPMSGFASKWLIFEALISKGMPITAFMAFFGSIGSFL
YVFRPLAGVFLGQLPSDHKDVKEAPLPMLIPMAILVLLNVVFGVAPGLVLQEINKIFGELGIGPIDYEGW
EIKTGFGSWNALTVFILFVVGFIIAAIIYFLGAKARKVDLTDTYTSGEFVYNEDLYHYARNFYAPLERAY
AFWPSFEKLYEMIAKFFEDFGEWIRSYFYNGNPQAYAFYLAIVLLILAWW
>gnl|CDD|181535 PRK08673, PRK08673, 3-deoxy-7-phosphoheptulonate synthase; Reviewed
IIVMKPGATEEEIDEVIEEVESAGLKTHVSPGVERTVIGLIGDKGKVDAAKFEALPGVEEVVPVLKPYKL
ASREFKPEPTVVKVGDVEIGGGKPVVIAGPCSVESEEQILEIARAVKEAGAQILRGGAFKPRTSPYSFQG
LGEEGLKLLAEAREETGLPIVTEVMDPRDVELVAEYVDILQIGARNMQNFDLLKEVGKTNKPVLLKRGMS
ATIEEWLMAAEYILAEGNPNVILCERGIRTFETATRNTLDLSAVPVIKKLTHLPVIVDPSHATGKRDLVE
PLALAAVAAGADGLIVEVHPDPEKALSDGPQSLTPEEFEELMKKLRAIAEALGRE
>gnl|CDD|181536 PRK08674, PRK08674, bifunctional phosphoglucose/phosphomannose isomerase; Validated
PMGMLEEYLNWPEQFEEALEIAISLDLEEDLEKIDNIVISGMGGSGIGGDLLRILLFDELKVPVFVNRDY
TLPAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKIIAITSGGKLKEMAKEHGLPVIIVPGGYQPRAA
LGYLFTPLLKILEKLGLIPDKSAEVLETKIVLSELAEGLKEKVPTLKNLAKRLAGKLYGRIPVIYGSGLT
LAVAYRWKTQINENAKYPAFYNEIPELNHNEIVGYERPQSLLKYFFVVVLRDSEHPRIKKRVEITIDILT
EAVINVIEIYPEGNSPLARIFSLIYLGDFASLYLAELRGVDPTPVPIIDYLKRRLAE
>gnl|CDD|181537 PRK08676, PRK08676, hydrogenase membrane subunit; Validated
IIVYYLLVALLFLRLGLLSRSHRLLNALALGHGLWHLGLSLWVLLVLPLPGYFMESRYLFIDHLGIFVVL
IASVVFILAALYARGYVDHLLSNGELDPENLKVFYLGFNLLLSVITFAFFSDNLALFWIFAELTTVFSAM
LIAILSARENIDAALKYIFIASTAMIFAFIGLIFLFSLTRQALGTGTLNWTELAAHASLLSPSVLGASFL
FIFIGFLAKSGLVPFHTWLPAAYAKAPSVVSALLSGTVLNIGIYGILRLSALLRQSGAAEQFSNVLIGLG
IFSIAVAAFSMLSQRNLKKLIAFSSIEHMGLMLLGIGIGTPLALFWMLFHMLAHSLVKSGLFFSAGILHR
QYRSDRFDRIFDVFRLQPVAAWGVILGSAAIIGMPPFPLFLSKFFILLQLGGISVWLVLAVLLLLLLAAS
SFAIFLLKAFTRVSEGNADRPVFRTPLSMKLPIVIILALVLALGVYFPPGLADFLDQIVKELGFV
>gnl|CDD|169553 PRK08690, PRK08690, enoyl-[acyl-carrier-protein] reductase FabI
MGFLQGKKILITGMISERSIAYGIAKACREQGAELAFTYVVDKLEERVRKMAAELDSELVFRCDVASDDE
INQVFADLGKHWDGLDGLVHSIGFAPKEALSGDFLDSISREAFNTAHEISAYSLPALAKAARPMMRGRNS
AIVALSYLGAVRAIPNYNVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGIADFGKLLGH
VAAHNPLRRNVTIEEVGNTAAFLLSDLSSGITGEITYVDGGYSINALSTEG
>gnl|CDD|236333 PRK08691, PRK08691, DNA polymerase III subunits gamma and tau; Validated
MAYQVLARKWRPKTFADLVGQEHVVKALQNALDEGRLHHAYLLTGTRGVGKTTIARILAKSLNCENAQHG
EPCGVCQSCTQIDAGRYVDLLEIDAASNTGIDNIREVLENAQYAPTAGKYKVYIIDEVHMLSKSAFNAML
KTLEEPPEHVKFILATTDPHKVPVTVLSRCLQFVLRNMTAQQVADHLAHVLDSEKIAYEPPALQLLGRAA
AGSMRDALSLLDQAIALGSGKVAENDVRQMIGAVDKQYLYELLTGIINQDGAALLAKAQEMAACAVGFDN
ALGELAILLQQLALIQAVPSALAHDDPDSDILHRLAQTISGEQIQLYYQIAVHGKRDLSLAPDEYAGFMM
TLLRMLAFAPLAAASCDANAVIENTELQSPSAQTAEKETAAKKPQPRPEAETAQTPVQTASAAAMPSEGK
TAGPVSNQENNDVPPWEDAPDEAQTAAGTAQTSAKSIQTASEAETPPENQVSKNKAADNETDAPLSEVPS
ENPIQATPNDEAVETETFAHEAPAEPFYGYGFPDNDCPPEDGAEIPPPDWEHAAPADTAGGGADEEAEAG
GIGGNNTPSAPPPEFSTENWAAIVRHFARKLGAAQMPAQHSAWTEYHPDTGLMVLAMTAEARATADKKRL
DKIRDTLAQAYGLQLTLQTQDWRDEAGRETPAMQDKRVQAEDRQKAQALLEADPAAQKILQAFGAQWQPE
SLELAANRP
>gnl|CDD|181538 PRK08699, PRK08699, DNA polymerase III subunit delta'; Validated
MIYPWHQEQWRQIAEHWERRPNAWLFAGKKGIGKTAFARFAAQALLCETPAPGHKPCGECMSCHLFGQGS
HPDFYEITPLSDEPENGRKLLQIKIDAVREIIDNVYLTSVRGGLRVILIHPAESMNLQAANSLLKVLEEP
PPQVVFLLVSHAADKVLPTIKSRCRKMVLPAPSHEEALAYLRERGVAEPEERLAFHSGAPLFDEEPELRA
LRIKLLDILAEPRLLKILDYAALFDKEKLPLAVFVGWMQKWLVDLGLCLQHMKPVYYPAYEDRLLQTASG
FRPRNVFAAEDMLKQLAPYGFHTLNVKMQIEHLLINYLELKKENG
>gnl|CDD|169556 PRK08703, PRK08703, SDR family oxidoreductase
MATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPEPFAIRFDLMSAEE
KEFEQFAATIAEATQGKLDGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDA
SVIFVGESHGETPKAYWGGFGASKAALNYLCKVAADEWERFGNLRANVLVPGPINSPQRIKSHPGEAKSE
RKSYGDVLPAFVWWASAESKGRSGEIVYL
>gnl|CDD|169557 PRK08706, PRK08706, lipid A biosynthesis lauroyl acyltransferase; Provisional
MKFIFFVLYVLQFLPFALLHKLADLTGLLAYLLVKPRRRIGEINLAKCFPEWDEEKRKTVLKQHFKHMAK
LMLEYGLYWYAPAGRLKSLVRYRNKHYLDDALAAGEKVIILYPHFTAFEMAVYALNQDVPLISMYSHQKN
KILDEQILKGRNRYHNVFLIGRTEGLRALVKQFRKSSAPFLYLPDQDFGRNDSVFVDFFGIQTATITGLS
RIAALANAKVIPAIPVREADNTVTLHFYPAWDSFPSEDAQADAQRMNRFIEERVREHPEQYFWLHKRFKT
RPEGSPDFY
>gnl|CDD|236334 PRK08719, PRK08719, ribonuclease H; Reviewed
MRASYSIYIDGAAPNNQHGCVRGGIGLVVYDEAGEIVDEQSITVNRYTDNAELELLALIEALEYARDGDV
IYSDSDYCVRGFNEWLDTWKQKGWRKSDKKPVANRDLWQQVDELRARKYVEVEKVTAHSGIEGNEAADML
AQAAAEL
>gnl|CDD|181539 PRK08722, PRK08722, beta-ketoacyl-ACP synthase II
MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARK
MDLFIQYGIAAGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIV
NMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALS
TRNDEPQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGG
ALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRALGEAGSKQVLVSSTKSMTGHLLGAAGSV
EAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVESMEYAICNSFGFGGTNGSLIFKKM
>gnl|CDD|236335 PRK08724, fliD, flagellar filament capping protein FliD
MSLGPMGMSGGMDINSMVSKIVDAERVPKQQRIDNERTDIDTSISAYGRLRESLDTMKNLMTNFRQEKAF
AVRTVDTSDEDVVSATATTDAIAGKYAIDVLQLAQSHKVASDVLDEDAKFGPGKLQISLGDKSFTLDVVG
NSKLVDIVRGINGAKSNPGVRASIINDVEGPRLILASNVSGKDNQIKISVDAEYGNPLKRFEYKTLEDRV
RALEKARAAAQQVIAPLTPEEQKVAPELSDEEGNAIPPADQEVAEEIQDAAQIAQQQEATAALAALEEPI
SAGGATAAAAGQAAIDAAEAKAYLRPEDRIPGWTETASGTLLDSYPEPEEELDEAAIAKAPDVPGWSNTA
SGTLTDSYVTPKEAQAEIEQKLAQEKAQLDAAVEKGELTPEQAKQIARAKLEPEERERLEKIDKAQAALK
QAQSAFDLYSGMTEVQSAQDSMVVLDGVAQLSSNNNVIEDAIEGVDLTLKGKTDKNKPPAEIGVEYDRQS
VRNDIEQFVAAYNQFYQTSKALSGVDPATGQKGPLAGDSTVRSADSRLKSVFSSSIEQAPENLKSLTEFG
ITTTRQGTLEINYDMLDRQLNNNFNKLEEFFGGNTGFAKRVEDAIQSMTGVTGSIRTREKSLREQNYRLN
DDQVALDRRMESLEKRTHAKFAAMQDATGKMQGQLGGMMNALG
>gnl|CDD|181542 PRK08733, PRK08733, LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase
MSESANVAVRPSLRNPKHWPMYLGLAVMVLAARLPWTLQRALGRGVGWVAMRLAGTRRRAAEVNLKLCFP
EQDDAWRARLLRDSFDALGVGLFEFARAWWGSIDVIRPGVQIEGLEHLQQLQQQGRGVLLVSGHFMTLEM
CGRLLCDHVPLAGMYRRHRNPVFEWAVKRGRLRYATHMFANEDLRATIKHLKRGGFLWYAPDQDMRGKDT
VFVPFFGHPASTITATHQLARLTGCAVVPYFHRREGGRYVLKIAPPLADFPSDDVIADTTRVNAAIEDMV
REAPDQYLWIHRRFKRQPGGRSDFYR
>gnl|CDD|181543 PRK08734, PRK08734, lauroyl acyltransferase
MNPDVKARLLYRTAALVGRLPWPLLKRLADLLAWSWRKLNARESRVTRRNLELAYPELSPQQRAQLHAQI
LRSTARQALEVLRTWTHPPAENLARLRQRHGQELYDAALASGRGVIVAAPHFGNWELLNQWLSERGPIAI
VYRPPESEAVDGFLQLVRGGDNVRQVRAEGPAVRQLFKVLKDGGAVGILPDQQPKMGDGVFAPFFGIPAL
TMTLVNRLAERTGATVLYGWCERIGPDLEFALHVQPADPAVADPDPLRAATALNAGIERIARRDPAQYQW
TYKRYTLRPPGSGEHNPYATERHPH
>gnl|CDD|181544 PRK08737, PRK08737, acetylornithine deacetylase; Provisional
MTDLLESTLDHLQALVSFDTRNPPRAITTGGIFDYLRAQLPGFQVEVIDHGAGAVSLYAVRGTPKYLFNV
HLDTVPDSPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANAGDGDAAFLFSSDEEANDPRCVAAF
LARGIPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKQDPSASALHQAMRWGGQALDHVESLA
HARFGGLTGLRFNIGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFAGFAEPAAATFEETFRGPS
LPSGDIARAEERRLAARDVADALDLPIGNAVDFWTEASLFSAAGYTALVYGPGDIAQAHTADEFVTLDQL
QRYAESVHRIINDS
>gnl|CDD|181546 PRK08751, PRK08751, long-chain fatty acid--CoA ligase
MSQARPWLQSYPAGVAAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGE
LQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQV
IADTPVKQVITTGLGDMLGFPKAALVNFVVKYVKKLVPEYRINGAIRFREALALGRKHSMPTLQIEPDDI
AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEGCEVVITALPLYHIFALTANGLVFMKIG
GCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWK
QVTGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMK
GYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAA
VGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAKA
>gnl|CDD|181547 PRK08760, PRK08760, replicative DNA helicase; Provisional
MSARPGFRSNRNRDRDDDDYDRPEPRLDQLRVPPHSVEAEQAVLGGLMLAPDALDRVNDQLTENDFYRRD
HRLIYRAIRELSEKDRPFDAVTLGEWFESQGKLEQVGDGAYLIELASTTPSAANIAAYAEIVRDKAVLRQ
LIEVGTTIVNDGFQPEGRESIELLASAEKAVFKIAEAGARGRTDFVAMPGALKDAFEELRNRFENGGNIT
GLPTGYNDFDAMTAGLQPTDLIILAARPAMGKTTFALNIAEYAAIKSKKGVAVFSMEMSASQLAMRLISS
NGRINAQRLRTGALEDEDWARVTGAIKMLKETKIFIDDTPGVSPEVLRSKCRRLKREHDLGLIVIDYLQL
MSVPGNSENRATEISEISRSLKGLAKELNVPVIALSQLNRSLETRTDKRPVMADLRESGAIEQDADMIVF
IYRDDYYNKENSPDKGLAEIIIGKHRGGPTGSCKLKFFGEYTRFDNLAHDSVGSFE
>gnl|CDD|236337 PRK08762, PRK08762, molybdopterin-synthase adenylyltransferase MoeB
SIREISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRS
AHAAATLRELGYTRVASVAGGFSAWKDAGLPLERPRLLTDEQDERYSRHLRLPEVGEEGQRRLLEARVLL
IGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQVEAV
QERVTSDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDAGRQRGQAPCY
RCLFPEPPPPELAPSCAEAGVLGVLPGVIGLLQATEAIKLLLGIGDPLTGRLLTFDALAMRFRELRLPPD
PHCPVCAPGRPFPGYIDYAAFCAGAA
>gnl|CDD|181549 PRK08763, PRK08763, single-stranded DNA-binding protein; Provisional
MARGINKVILVGNLGNDPDIKYTQSGMTITRISLATTSVRKDREGNTQERTEWHRVKFFGKLGEIAGEYL
RKGSQCYIEGSIRYDKFTGQDGQERYVTEIVADEMQMLGGRGEGGGGGGGGIRPQRQPAPRQNNGQDYAP
RRQQPAPQQSAPPMDDFADDDIPF
>gnl|CDD|181550 PRK08764, PRK08764, Rnf electron transport complex subunit RnfB
PSPAPTLVERLDRLLPQTQCGQCGFDGCRPYAQAMARGEATIDRCPPGGDAGARALAQVLGVPARPYDRS
RGTHKLPQVAWIVEADCIGCTKCIQACPVDAIVGGAKHMHTVIAPLCTGCELCVPACPVDCIELH
>gnl|CDD|181551 PRK08769, PRK08769, DNA polymerase III subunit delta'; Validated
MTSAFSPWQQRAYDQTVAALDAGRLGHGLLICGPEGLGKRAVALALAEHVLASGPDPAAAQRTRQLIAAG
THPDLQLVSFIPNRTGDKLRTEIVIEQVREISQKLALTPQYGIAQVVIVDPADAINRAACNALLKTLEEP
SPGRYLWLISAQPARLPATIRSRCQRLEFKLPPAHEALAWLLAQGVSERAAQEALDAARGHPGLAAQWLR
EDGLALRRAVAQDLEQIASGRAGAVDVAQRWTNDGQADQRLRHAADLALAQASAGLTDPSRLHKLATWFD
AANRTRDLLRTTVRADLAVTELLLAWREGERQPRSRGTR
>gnl|CDD|181552 PRK08773, PRK08773, UbiH/UbiF family hydroxylase
MSRRSRRDAVIVGGGVVGAACALALADAGLSVALVEGREPPRWQADQPDLRVYAFAADNAALLDRLGVWP
AVRAARAQPYRRMRVWDAGGGGELGFDADTLGREQLGWIVENDLLVDRLWAALHAAGVQLHCPARVVALE
QDADRVRLRLDDGRRLEAALAIAADGAASTLRELAGLPVSRHDYAQRGVVAFVDTEHPHQATAWQRFLPT
GPLALLPFADGRSSIVWTLPDAEAERVLALDEAAFSRELTQAFAARLGEVRVASPRTAFPLRRQLVQQYV
SGRVLTLGDAAHVVHPLAGQGVNLGLRDVAALQQLVRQAHARRADWAAPHRLQRWARTRRSDNTVAAYGF
DAINRVFSNDEMHLTLLRGSVLGLAGKLPPLVDALWKRASGV
>gnl|CDD|181553 PRK08775, PRK08775, homoserine O-succinyltransferase
MSLVNTASPSTTLCVDTPTPDDDGPPAVRGEVAIPLSMRHAGLEDLRLRYELIGPAGAPVVFVAGGISAH
RHVAATATFPEKGWWEGLVGSGRALDPARFRLLAFDFIGADGSLDVPIDTADQADAIALLLDALGIARLH
AFVGYSYGALVGLQFASRHPARVRTLVVVSGAHRAHPYAAAWRALQRRAVALGQLQCAEKHGLALARQLA
MLSYRTPEEFEERFDAPPEVINGRVRVAAEDYLDAAGAQYVARTPVNAYLRLSESIDLHRVDPEAIRVPT
VVVAVEGDRLVPLADLVELAEGLGPRGSLRVLRSPYGHDAFLKETDRIDAILTTALRSTGETA
>gnl|CDD|181554 PRK08776, PRK08776, O-succinylhomoserine (thiol)-lyase
MSFRDPTDAPCSAATAAVRAGIDRDTAYGAVTPPIVLSSNFSFDGFGNKRQYDYTRSGNPTRDLLGEALA
ELEGGAGGVITATGMGAINLVLNALLQPGDTLVVPHDAYGGSWRLFNALAKKGHFALITADLTDPRSLAD
ALAQSPKLVLIETPSNPLLRITDLRFVIEAAHKVGALTVVDNTFLSPALQKPLEFGADLVLHSTTKYING
HSDVVGGAVVARDAELHQQLVWWANALGLTGSPFDAFLTLRGLRTLDARLRVHQENADAIAALLDGHAAV
NQVYYPGLASHPGHALAARQQKGFGAMLSFELEGGEAAVRAFVDGLRYFTLAESLGGVESLIAHPASMTH
AAMTAEARAAAGISDGLLRLSVGIESAEDLLIDLRAGLARAEAVLTAAARKKVDA
>gnl|CDD|181555 PRK08780, PRK08780, DNA topoisomerase I; Provisional
MSKHLVIVESPAKAKTINKYLGKDFTVLASYGHVRDLVPKEGAVDPENGFAMRYDLIDKNEKHVEAIAKA
AKSADDLYLATDPDREGEAISWHLAEILKERGLLKDKPMQRVVFTEITPRAIKEAMAKPRDIASDLVDAQ
QARRALDYLVGFNLSPLLWRKIQRGLSAGRVQSPALRMIVEREEEIEAFIAREYWSIEADCAHPSQPFNA
KLIKLDGQKFEQFTITDGDTAEAARLRIQQAAQGTLHVTDVESKERKRNPAPPFTTSTLQQEASRKLGFT
TRRTMQVAQKLYEGVDLGDEGSVGLITYMRTDSVNLSQDALAEIRDVIARDYGTASLPDQPNTYKTKSKN
AQEAHEAVRPTSALRTPAQVARFLSDDQRRLYELIWKRAVACQMIPATLNTVSVDLAAGSEHVFRATGST
VVVPGFLAVYEEGKDDKSAEDEDEGRKLPPMKEGDNVPLERIRAEQHFTEPPPRYTEASLVKALEEYGIG
RPSTYASIISTLQFRKYVEMEGRRFRPTDVGRAVNKFLTGHFTRYVDYDFTARLEDDLDAVSRGEKEWIP
LMEKFWGPFKELVEEKKDSVDRTEAGQVRELGTDPKSGKPVSVRIGRFGPMVQIGTKDDEEKPRFASLRP
GQSIDSITLEEALELFKLPRALGETDEGEDVSVGIGRFGPFVKRGSKYASLKKEDDPYTIDLARALFLIE
EKEEIARNRVIKDFEGSGIQVLNGRYGPYITDGKLNGKIPKDREPASLTLEEVQQLLADAPVRKGFRAKK
AALKKAKVSA
>gnl|CDD|136970 PRK08787, PRK08787, peptide chain release factor 2; Provisional
MLEKTVIGIADVLSGLADAGELLDLAESEQDEDTALAVIADLDKYQAHVEKLEFQRMFSGQMDGANAFVD
IQAGAGGTEAQDWAEILLRMYLRWAESRGWKTELMEVSGGEVAGIKSATVRIEGEYAYGWLKTEIGVHRL
VRKSPFDSDNRRHTSFTSVFVSPEVDDNIEIDINPADLRTDVYRSSGAGGQHVNKTESAVRITHIPTNTV
VACQTGRSQHQNRDNAMKMLAAKLYELEVQKRNAEKDALEATKSDIGWGSQIRNYVLDQSRIKDLRTGIE
RSDTQKVLDGDLDEFVEASLKAGLAAGSKRLDA
>gnl|CDD|236338 PRK08788, PRK08788, enoyl-CoA hydratase; Validated
NMSAVRPFPEAGELSQLRVYYEEERNVMWMYMRAQPRPCFNLELLDDIMNLQRAIRQRLDDSGLPVDFWV
LASDVPGVFNLGGDLALFAELIRAGDRDALLAYARACVDGVHAFHRGFGAGAISIALVQGDALGGGFEAA
LSHHTIIAERGAKMGFPEILFNLFPGMGAYSFLARRVGPKLAEELILSGKLYTAEELHDMGLVDVLVEDG
QGEAAVRTFIRKSKRKLNGWRAMLRARRRVNPLSLEELMDITEIWVDAALQLEEKDLRTMERLVRAQNRR
VGDLAAA
>gnl|CDD|181557 PRK08808, PRK08808, type II secretion system protein J
MMRRRAAGFTLIEVLLATVLLVGGLALAFATLRSASAVSQRGEAIAQRSERMRAVEEFLRRRLAGALPIA
MGIDTQSQQPILFVGEPQRMRFAADVPDYLGRGGPYLHDLSVVGDGDQRQLLIALTMLQSGKTIEESPPL
PPELLADGLQQVHFRYRGIDPSTGQLSPWLPQWEWHDRLPLLVRIQIRSDGAAWPPLVVALPQSGSGGAG
Q
>gnl|CDD|181558 PRK08811, PRK08811, uroporphyrinogen-III synthase; Validated
MALSHHHTMTGAATADAAWTLISLRPSGEHAPLRRAVARHGGRLLALSPWRLQRLDTAQARDALRQALAA
PIVVFTSPAAVRAAHRLLPLQRPARAHWLSVGEGTARALQACGIDEVVRPTRMDSEGLLALPLAQAPLQA
VGLITAPGGRGLLAPTLQQRGARILRADVYQRVPLRLRASTLAALSRAAPRSVLALSSAEALTLILQQLP
DALRRALQQRPVVASSDRLLDAAHAAGFIHVMRAAGPLPAQLAAAAAAIMTPPRPC
>gnl|CDD|236339 PRK08813, PRK08813, threonine dehydratase; Provisional
MDMPDSGRPTVQEPDVGDVAVSVADVLAAQARLRRYLSPTPLHYAERFGVWLKLENLQRTGSYKVRGALN
ALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEA
YAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAAHAPDVVIVPIGGGGLASGVALALKSQGVRVVGA
QVEGVDSMARAIRGDLREIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHV
IAEGAGALALAAGRRVSGKRKCAVVSGGNIDATVLATLLSEVRPRPPRKPRRRNTERLRNERSAPAPPN
>gnl|CDD|236340 PRK08815, PRK08815, GTP cyclohydrolase II RibA
MSPTVSPSAQPFGDPAAIRCERAAAELRAGRPVLLTDAQGQRRAVIALDSSTAQSAAAFARAAQGRHYLF
LTATRAQVLGLEAPQGARVALPDVDYDRLAALAYLRDGRVPAPWAPGDALDAGAVEIARLALLLPAMVAV
PLPVHDEAAFAGCQALALADLDAGCATSAAAGYELVTRTPVPLRGLGMTEFVVFRGGVAQRDQVAIVVGQ
PDLSSAVPVRVHSSCLTGDLFGSLKCDCGDQLRHGLAKLKELGGGVLLYLDQEGRGNGIAAKMRAYGYQH
AGLDTIDADAQLGFGPDERRYGSAVAMLRGLGITRVRLLTNNPTKAERLRAAGIEVEDRIRVTGRITAEN
ERYLRTKADRAGHALDVDALILAAQ
>gnl|CDD|181561 PRK08818, PRK08818, prephenate dehydrogenase; Provisional
MIAQPVVGIVGSAGAYGRWLARFLRTRMQLEVIGHDPADPGSLDPATLLQRADVLIFSAPIRHTAALIEE
YVALAGGRAAGQLWLDVTSIKQAPVAAMLASQAEVVGLHPMTAPPKSPTLKGRVMVVCEARLQHWSPWVQ
SLCSALQAECVYATPEHHDRVMALVQAMVHATHLAQAGVLRDYAPLLGELRALMPYRSASFELDTAVIAR
ILSLNPSIYEDIQFGNPYVGEMLDRLLAQLQELRALVAQGDDAARARFRAQFLHANAQALQEDALAAGNY
TYERVGYLLADLTEPLTLSVYLPEDRPGSLRTLLHVFEQHGVNLSSIHSSRTPAGELHFRIGFEPGSDRA
ALARAAAEIDASGIGRVLER
>gnl|CDD|181562 PRK08840, PRK08840, replicative DNA helicase; Provisional
MADNRNRKIPDAQVDAIKVPPHSLEAEQSVIGGLLLDNERWDTVAEKVVASDFYSRPHRLIFEGVKSILE
AGKPLDLITLSEHLERREQLEDVGGFAYLADLAKNTPSAANINAYADIVAERALVRNLIGVANEIADAGY
DPQGRTSEDLLDMAESKVFAIAEARTSENEGPQNVDSILEKTLERIELLYKTPQDGVTGVDTGFTDLNKK
TAGLQGSDLIIVAARPSMGKTTFAMNLCENAAMDQDKPVLIFSLEMPAEQLMMRMLASLSRVDQTKIRTG
QLDDEDWARISSTMGILMEKKNMYIDDSSGLTPTEVRSRARRIAREHGGLSMIMVDYLQLMRVPALSDNR
TLEIAEISRSLKALAKELNVPVVALSQLNRSLEQRADKRPVNSDLRESGSIEQDADLIMFIYRDEVYNPD
SPLKGTAEIIIGKQRNGPIGSVRLTFQGQYSRFDNYAGPAFDDE
>gnl|CDD|181563 PRK08841, PRK08841, aspartate kinase; Validated
MPLIVQKFGGTSVGSIERIQTVAEHIIKAKNDGNQVVVVVSAMAGETNRLLGLAKQVDSVPTARELDVLL
SAGEQVSMALLAMTLNKLGYAARSLTGAQANIVTDNQHNDATIKHIDTSTITELLEQDQIVIVAGFQGRN
ENGDITTLGRGGSDTTAVALAGALNADECQIFTDVDGVYTCDPRVVKNARKLDVIDFPSMEAMARKGAKV
LHLPSVQHAWKHSVPLRVLSSFEVGEGTLIKGEAGTQAVCGIALQRDLALIEVESESLPSLTKQCQMLGI
EVWNVIEEADRAQIVIKQDACAKLKLVFDDKIRNSESVSLLTLVGLEANGMVEHACNLLAQNGIDVRQCS
TEPQSSMLVLDPANVDRAANILHKTYVTSEQPQDNPLKQAFL
>gnl|CDD|181564 PRK08849, PRK08849, 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
MNKYDIAVVGGGMVGAATALGFAKQGRSVAVIEGGEPKAFEPSQPMDIRVSAISQTSVDLLESLGAWSSI
VAMRVCPYKRLETWEHPECRTRFHSDELNLDQLGYIVENRLIQLGLWQQFAQYPNLTLMCPEKLADLEFS
AEGNRVTLESGAEIEAKWVIGADGANSQVRQLAGIGITAWDYRQHCMLINVETEQPQQDITWQQFTPSGP
RSFLPLCGNQGSLVWYDSPKRIKQLSAMNPEQLRSEILRHFPAELGEIKVLQHGSFPLTRRHAQQYVKNN
CVLLGDAAHTINPLAGQGVNLGFKDVDVLLAETEKQGVLNDASFARYERRRRPDNLLMQTGMDLFYKTFS
NSLTPLKFVRNAALKLAENSGPLKTQVLKYALGM
>gnl|CDD|236341 PRK08850, PRK08850, 2-octaprenyl-6-methoxyphenol hydroxylase; Validated
MMQSVDVAIIGGGMVGLALAAALKESDLRIAVIEGQLPEEALNELPDVRVSALSRSSEHILRNLGAWQGI
EARRAAPYIAMEVWEQDSFARIEFDAESMAQPDLGHIVENRVIQLALLEQVQKQDNVTLLMPARCQSIAV
GESEAWLTLDNGQALTAKLVVGADGANSWLRRQMDIPLTHWDYGHSALVANVRTVDPHNSVARQIFTPQG
PLAFLPMSEPNMSSIVWSTEPLRAEALLAMSDEQFNKALTAEFDNRLGLCEVVGERQAFPLKMRYARDFV
RERVALVGDAAHTIHPLAGQGVNLGLLDAASLAQEILALWQQGRDIGLKRNLRGYERWRKAEAAKMIAAM
QGFRDLFSGSNPAKKLVRGIGMSLAGQLPGAKDEIMKRALGLKGELPELAKQVWL
>gnl|CDD|181566 PRK08857, PRK08857, aminodeoxychorismate/anthranilate synthase component II
MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFA
GKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPEC
FELTAWTELEDGSMDEIMGFQHKTLPIEAVQFHPESIKTEQGHQLLANFLART
>gnl|CDD|181567 PRK08861, PRK08861, O-succinylhomoserine (thiol)-lyase
MSTRKPATIAVRTGIESDSQYHAVVPPIYLSTNYGFPAFGEVPKYDYTRSGNPNRGLLEQTLSELESGKG
AVVTNCGTSALNLWVSALLGPDDLIVAPHDCYGGTYRLFNTRANKGDFKVQFVDQSDAAALDAALAKKPK
LILLETPSNPLVRVVDIAELCQKAKAVGALVAVDNTFLTPVLQKPLELGADFVIHSTTKYINGHSDVIGG
VLITKTKEHAEELAWWGNCIGATGTPFDSYMTLRGIRTLGARMRVHEESAQQILAYLQTQSLVGTIYHPS
LPEHPGHEIAKKQQSGFGSMLSFEFAGSFEQLKVFVKALALFSLAESLGGVESLICHPASMTHRAMGEEA
LAEAGVSQQLLRLSVGLEDAQDLIADLDQAFAKAAEAN
>gnl|CDD|236342 PRK08862, PRK08862, SDR family oxidoreductase
MDIKSSIILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTDNVYSFQLKDFSQESIR
HLFDAIEQQFNRAPDVLVNNWTSSPLPSLFDEQPSESFIQQLSSLASTLFTYGQVAAERMRKRNKKGVIV
NVISHDDHQDLTGVESSNALVSGFTHSWAKELTPFNIRVGGVVPSIFSANGELDAVHWAEIQDELIRNTE
YIVANEYFSGRVVEAEV
>gnl|CDD|236343 PRK08868, PRK08868, flagellar protein FlaG; Provisional
MEISSYASNIQPYGSNSGTKFASENGNGTSSVLVSDKTRSVSSEKVEKTEQELSVEAAVAMAEQRQELNR
EELEKMVEQMNEFVKSINKGLSFRVDEESGRDVVTIYEASTGDIIRQIPDEEMLEVLRRLAEQAHNSGLL
VEKV
>gnl|CDD|236344 PRK08869, PRK08869, polar flagellin E
AVNVNTNVSAMTAQRNLNGATSALSQSMERLSSGKRINSAKDDAAGLQISNRLTTQIRGLDVAVRNANDG
ISIAQTAEGAMNETTNILQRMRDLSLQSANGSNSASDRQALQEEVTALNDELNRIAETTSFGGTKLLNGS
FGTKSFQIGANSGEAVSLDLKSMRSDAKIMGGVSYDAEGGADKDWTVGAGNTDLNVSFDDKGGETQAITI
NAKAGDDIEELATYINGQTDGVGASVSEDGKLQLFAAGQKVSGGVSFSGGLAAELGLGNATAVTVDDLDI
STVGGAQQAVAVIDAALKYVDSHRADLGAFQNRFTHAINNLQNISENLSASNSRIKDTDFAKETTELTKA
QILQQAGTSILAQAKQAPQSALSLLQ
>gnl|CDD|236345 PRK08870, flgL, flagellar hook-associated protein FlgL; Reviewed
MRISTAQMYQQSVNSMLDQQSQLSQLQQQLSSGKKLLTPSDDPVAAAQAVNLSQQSALLDQYTKNINLAR
NRLQQEESTLGSVEDLLQRARELVVQAGNGSLSDSDRQAIATELQGLRDQLLNLANSKDGSGNYLFAGTQ
SGTQPFAFDASGNVVYSGDQGQRQVQVADSVQVATNDPGDEVFMSVPNGGGDYVPNANASNTGTGLLGSA
SITDPSDPVNGDTYTITFTDNGAGGTNTYVTDSSTGTVVTAQAYDAGQPINFNGVEVQISGAPAAGDSFT
LTPAPQASIFDTLDDAIAALESPVSTPAADAALQNALAQALRNLDNALNNVLTARASVGARLNELDSAEA
VHEDNKLQNTSALSDLEDLDYASAISEFELQQAALQAAQQAFSKVQSLSLFNYI
>gnl|CDD|181572 PRK08871, flgK, flagellar hook-associated protein FlgK; Validated
MASDLLNVGTQSVLTAQRQLNTTGHNISNVNTEGYSRQSVIQGTNDPRQFGGSTYGMGVHVENVRRSWDQ
FAVNELNLSTTNLANKTDTEANLDMLSSMLSSVASKKIPENLNEWFDAVKTLADSPNDLGARKVVLEKAK
LISQTLNDFHETVRQQKDVTNKKLDLGVERINQIALEIRDIHRLMMRTPGPHNDLMDQHEKLVKELSQYT
KVTVTPRKNAEGFNVHIGNGHTLVSGTEASQLKMIDGYPDPHQRRLAMVEGKGLKAIKADDIGGKLGALL
DMRDEHIPYLMDELGRLATGFSSEVNTLQSQGLDLRGNVGGNLFTDVNSEVIARSRVVTAPNSKADVAVF
IDDISQLKGGEYALRYDGSQYTVTKPSGEQQSLDPDGNPSAFYLDGMRVEVRNPPQAGERILLRPTRNGA
AQIKLETNDAKKIAAQSYEASTTFAQGKAKFKILQAGDLREFEVIVSPTGDQFAVTDTKGNILLQPQPYP
PKGPVTVGGTTFELTEGALANDKFTANLVPSEGDNGNLRKMQNLQTDKVMDDGESTIIDLYHNLNTEVGL
KKATATRLADVARLEKEAAQSRVASISGVNLDEEAANMMKFQQAYMASSRIMQAANDTFNTILQLR
>gnl|CDD|181573 PRK08878, PRK08878, cobalamin biosynthesis family protein
MEEKFSQFYANGALLVMWGALLFHLILPIPHAAHPVTLWHKFAELLASKVNTPHSYQQSLLSGALAWGLM
IFPCLILLIALKPLVWQPPLFELALLLLALDWRNNEKLAKQLIQALAKEDKAQARELLKPYVNRDTETLS
LLGLGKAGAETIIMGYGRNVIGVLFWYGIAGGIGAFMYRLTAELARAWSPSRDQFRPFGIPAVRILAILD
FIPLRLFALLILLGKNAGHTFQGLLQQSKSWPLPGPAWLLCAIGNKLQLSLGGPAIYQGKKAERAKIGGR
IAPSAIHLAQIQRLLAWRIFVWIALQSLLLGLIYQGL
>gnl|CDD|181574 PRK08881, rpsN, 30S ribosomal protein S14; Reviewed
MAKKSMIAREKKRKKLVAKYAAKRAELKAIISDPNLSDEERYEARLKLQKLPRNSSPTRLRNRCELTGRP
RGYYRKFGLSRIKLRELAHRGEIPGVVKASW
>gnl|CDD|181576 PRK08887, PRK08887, nicotinate-nicotinamide nucleotide adenylyltransferase
MKKIAVFGSAFNPPSLGHKSVIESLSHFDLVLLVPSIAHAWGKTMLDYETRCQLVDAFIQDLGLSNVQRS
DIEQELYAPDESVTTYALLTRLQELYPEADLTFVIGPDNFLKFAKFYKADEITQRWTVMACPEKVPIRST
DIRNALQNGKDISHLTTPGVARLLKEHQLYTEPS
>gnl|CDD|236347 PRK08903, PRK08903, DnaA regulatory inactivator Hda; Validated
MMRQLTLDLGPPPPPTFDNFVAGENAELVARLRELAAGPVADRFFYLWGEAGSGRSHLLQALVADASYGG
RNARYLDAASPLLAFDFDPEAELYAVDDVERLDDAQQIALFNLFNRVRAHGQGALLVAGPAAPLALPLRE
DLRTRLGWGLVYELKPLSDADKIAALKAAAAERGLQLADEVPDYLLTHFRRDMPSLMALLDALDRYSLEQ
KRPVTLPLLREMLAQPE
>gnl|CDD|236348 PRK08905, PRK08905, lysophospholipid acyltransferase family protein
LLTFLFRLLSRLPLSWLHALGGWLGRLAYRLPGRYRRRLRANLRQAGGDPDPAMVKAAAAETGRMILELP
YVWFRKPEEIETMVKDDHGWEHVEAALAEGRGILFLTPHLGCFEVTARYIAQRFPLTAMFRPPRKAALRP
LMEAGRARGNMRTAPATPQGVRMLVKALRRGEAVGILPDQVPSGGEGVWAPFFGRPAYTMTLVARLAEVT
GVPVIFVAGERLPRGRGYRLHLRPVQEPLPGDKAADAAVINAEIERLIRRFPTQYLWGYNRYKRPRGAPA
PPAAAVDEA
>gnl|CDD|181580 PRK08912, PRK08912, aminotransferase
MKMGNPVFADLPTTIFEVMSQLAREHGAINLGQGFPDDPGPEDVRRAAADALLDGSNQYPPMMGLPELRQ
AVAAHYARFQGLDLDPETEVMVTSGATEALAAALLALVEPGDEVVLFQPLYDAYLPLIRRAGGVPRLVRL
EPPHWRLPRAALAAAFSPRTKAVLLNNPLNPAGKVFPREELALLAEFCQRHDAVAICDEVWEHVVFDGRR
HIPLMTLPGMRERTVKIGSAGKIFSLTGWKVGFVCAAPPLLRVLAKAHQFLTFTTPPNLQAAVAYGLGKP
DDYFEGMRADLARSRDRLAAGLRRIGFPVLPSQGTYFLTVDLAPLGLAEDDVAFCRRLVEEAGVAAIPVS
AFYEEDPVTSVVRFCFAKRDATLDEAVERLAAARRRR
>gnl|CDD|236349 PRK08913, flgL, flagellin
MIMRVATFANSSQLIAAALRTQQTMASLQIQESSGLKSESFAGLGADAQQAVNLQVSVTRAQSYIDAATL
AQSKVQVMYSAVGQIADLAQQLRSSLSAASTGTSTDATSAAASAQQALTQLATLLNTQYGGQYVFAGADT
TTAPVDLSSFAAGADSASSADTSYYQGDDTLTSVRVSATQGVSYGVTADNSAFEQLMRALMLVANSSSLS
SSTLSQALDLASTAVDDLGDVQSRLGNAASRLTAASSRQTEYKSFAETLLSDLTGVDVAAVTAQLSTYQT
QLTASYSAISKMKSLNLASYL
>gnl|CDD|236350 PRK08916, PRK08916, flagellar motor switch protein FliN
MADNDLQVPLPDLNGADAPPEDDVGYNEEEQADRTAADLEAVFDVPVQVSAVLGRSKMDVGQLLKLGPGS
VLELDRKVGEAIDIYVNNRLVARGEVVLVEDRLGVTMTEIIKAERA
>gnl|CDD|236351 PRK08927, fliI, flagellar protein export ATPase FliI
MMAALAAAIGDIDTLVIYGRVVAVRGLLVEVAGPIHALSVGARIVVETRGGRPVPCEVVGFRGDRALLMP
FGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPYPLRAPPPPAHSRARVGE
PLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQEFLQDDLGPE
GLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGY
TPTVFAELPRLLERAGPGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAIN
VLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGAYRAGSDPEVDEAIRLNPALEAFLRQGKD
EATSLAEGYARLAQILGGPETE
>gnl|CDD|181584 PRK08931, PRK08931, S-methyl-5'-thioadenosine phosphorylase
MTKAVLGIIGGSGVYDIDGLEDARWERVESPWGEPSDALLFGRLGGVPMVFLPRHGRGHRLSPSDINYRA
NIDALKRAGVTDIVSLSACGSFREELPPGTFVIVDQFIDRTFAREKSFFGTGCVAHVSMAHPVCPRLGDR
LAAAARAEGITVHRGGTYLCMEGPQFSTLAESKLYRSWGCDVIGMTNMPEAKLAREAEICYATVAMVTDY
DCWHPDHDAVTVDAVIAVLLANADKARALVARLAPDLGAEREPCPAGCDRALDHAIITAPEARDPALLAK
LDAVAGRVL
>gnl|CDD|181585 PRK08936, PRK08936, glucose-1-dehydrogenase; Provisional
MYSDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVAEEIKKAGGEAIAVKGDVTVES
DVVNLIQTAVKEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIKGNI
INMSSVHEQIPWPLFVHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKFADPKQRADVE
SMIPMGYIGKPEEIAAVAAWLASSEASYVTGITLFADGGMTLYPSFQAGRG
>gnl|CDD|236352 PRK08937, PRK08937, adenylosuccinate lyase; Provisional
IALAEAQAELGVIPKEDIAEIVLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIG
SERITGLARVLRSYLVTALENVPLWHERDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIER
NLDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAWKNQKDLRELLEADERFTKQLTKEELDELFD
PEAFVG
>gnl|CDD|236353 PRK08939, PRK08939, primosomal protein DnaI; Reviewed
MESIGKTLKKLMKRQDFRKRYEKLKQEVLADPDVQAFLQEHQEELTQEMIDRSLSKLYEYIDQRKKCDRG
CPNYAKGYQPKLVMNGGYIDVSYLPTPEKIEADEEKAIKKRIQSIYMPKDLLQASLADIDLDDRDRLDAL
MAALDFLEAYPPGEKVKGLYLYGDFGVGKSYLLAAIANELAKKGVSSTLLHFPEFIRELKNSISDGSVKE
KIDAVKEAPVLMLDDIGAEQMSSWVRDEVLGVILQYRMQEELPTFFTSNFDFDELEHHLAYTQRGEDETW
KAARIMERIRYLAKEVHLEGKNRRNN
>gnl|CDD|236354 PRK08942, PRK08942, D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase
KSMKAIFLDRDGVINVDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNAL
HEKMDWSLADRGGRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAG
VTPVLVRTGKGVTTLAEGAAPGTWVLDSLADLPQALKKQQK
>gnl|CDD|236355 PRK08943, PRK08943, lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
MEMKKDNKEYIPRFQKSFLHPRYWGTWLGIGALAGLALMPPRLRDPLAAKLGRLVGKLAKKARRRARINL
SLCFPEKSEAEREAIIDEMFATAPQAMLMMAELALRSPKHLQRRVEWHGLEILEEARANGENVIFLVPHG
WAIDIPAMLLASQGQPMAAMFHNQRNPLFDWLWNRVRRRFGGRLHAREDGIKPFISSVRQGYWGYYLPDE
DHGPEHSVFVDFFATYKATLPGIGRLAKVCRARVVPLFPVYNGKTHRLDIEIRPPMDDLLSADDETIARR
MNEEVEQFVGPHPEQYMWILKLLKTRKPGEDLYP
>gnl|CDD|236356 PRK08944, motB, flagellar motor protein MotB; Reviewed
MMAEKKCKCPPPGAPAWLATFADLMSLLMCFFVLLLSFSEMDVLKFKQIAGSMKFAFGVQNKIEVKDIPK
GTSIIAQEFRPGRPEPTPIEVIMQQTIDMTQQTLEFQAGESDSAGGTQQQRGKQRGGEASAEVKAEKAAA
QEQIEDLVKKLAQQLEKEIEDGAIEIESLGQQIIIRIREKGSFPSGSAFLQPKFKPVVRKIGELLKDVPG
IITVSGHTDNVPISSELYRSNWDLSSARAVAVAHELLKVKGFDPQRLKVVGMADTQPLVPNDTAENRARN
RRVEIIIEQGKAKESDEIPVKD
>gnl|CDD|236357 PRK08945, PRK08945, putative oxoacyl-(acyl carrier protein) reductase; Provisional
MHYQPKPDLLKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIPLD
LLTATPQNYQQLADTIEEQFGRLDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLL
KSPAASLVFTSSSVGRQGRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAMRASAFPGE
DPQKLKTPEDIMPLYLYLMGDDSRRKNGQSFDAQPGR
>gnl|CDD|181592 PRK08947, fadA, 3-ketoacyl-CoA thiolase; Reviewed
MEDVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALDPAEIDDIIWGCVQQTLEQGFNIAR
NAALLAGIPHSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHGVDFHPGLSKNV
AKAAGMMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVI
RPETTVEALAALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIM
GYGPVPATQKALKRAGLSISDIDVFELNEAFAAQSLPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGA
RISTTLLNLMERKDAQFGLATMCIGLGQGIATVFERV
>gnl|CDD|181593 PRK08951, PRK08951, malate synthase; Provisional
MNMSTINSTQIQQNLNPFIAEAVFAVETVNAAQQEEKQAKAKQFLDRLFPLANGSHQDVSSYVVYYQHLL
AFFADGSHSGLRQPKQFVAFNGHKSEPSAILLKDSGSHVELTFDRHGGTGSRDLANIEDIQLETCTTFSQ
EPTENRSTAMRHWISLLKGDESGRPAADQEDKEFTAKDGSDYQLKSCFSL
>gnl|CDD|169599 PRK08955, PRK08955, glyceraldehyde-3-phosphate dehydrogenase; Validated
MTIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVING
KRIRTTQNKAIADTDWSGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLNIVMGVNDHLFD
PAIHPIVTAASCTTNCLAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTT
GSATAITEIFPELKGKLNGHAVRVPLANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPL
VSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYANRTAELARKVGLAD
>gnl|CDD|181595 PRK08960, PRK08960, pyridoxal phosphate-dependent aminotransferase
MAQGYSRRSRDIEPFHVMALLARANELEAAGHDVIHLEIGEPDFTTAEPIVAAGQAALAAGHTRYTAARG
LPALREAIAGFYAQRYGVDVDPERILVTPGGSGALLLASSLLVDPGKHWLLADPGYPCNRHFLRLVEGAA
QLVPVGPDSRYQLTPALVERHWNADTVGALVASPANPTGTLLSRDELAALSQALRARGGHLVVDEIYHGL
TYGVDAASVLEVDDDAFVLNSFSKYFGMTGWRLGWLVAPPAAVPELEKLAQNLYISASTPAQHAALACFE
PETLAILEARRAEFARRRDFLLPALRELGFGIAVEPQGAFYLYADISAFGGDAFAFCRHFLETEHVAFTP
GLDFGRHQAGQHVRFAYTQSLPRLQEAVERIARGLRS
>gnl|CDD|236358 PRK08961, PRK08961, bifunctional aspartate kinase/diaminopimelate decarboxylase
SASPSTDRWVVLKFGGTSVSRRHRWDTIAKIVRKRLAEGGRVLVVVSALSGVSNELEAIIAAAGAGDSAS
RVAAIRQRHRELLAELGVDAEAVLAERLAALQRLLDGIRALTRASLRWQAEVLGQGELLSTTLGAAYLEA
SGLDMGWLDAREWLTALPQPNQSEWSQYLSVSCQWQSDPALRERFAAQPAQVLITQGFIARNADGGTALL
GRGGSDTSAAYFAAKLGASRVEIWTDVPGMFSANPKEVPDARLLTRLDYDEAQEIATTGAKVLHPRSIKP
CRDAGIPMAILDTERPDLSGTSIDGDAEPVPGVKAISRKNGIVLVSMETIGMWQQVGFLADVFTLFKKHG
LSVDLISSSETNVTVSLDPSENLVNTDVLAALSADLSQICRVKIIVPCAAVSLVGRGMRSLLHKLGPAWA
TFGAERVHLISQASNDLNLTFVIDESDADGLLPRLHAELIESGAMPVVFGPRWREIFGSVRPRPTPWWHA
ERARLLTLSDAGSPCYVYHLPTVRARARALAALAAVDQRFYAIKANPHPAILRTLEEEGFGFECVSIGEL
RRVFELFPELSPERVLFTPNFAPRAEYEAAFALGVTVTLDNVEPLRNWPELFRGREVWLRIDPGHGDGHH
EKVRTGGKESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRRMADELASFARRFPDVRTI
DLGGGLGIPESAGDEPFDLDALDAGLAEVKAQHPGYQLWIEPGRYLVAEAGVLLARVTQVKEKDGVRRVG
LETGMNSLIRPALYGAYHEIVNLSRLDEPAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAY
GYSMSSTYNLREPAREVVLDA
>gnl|CDD|181597 PRK08963, fadI, 3-ketoacyl-CoA thiolase; Reviewed
TRQGDRIAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAR
EIVLGTGMNVHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLARALVDLN
KARTLGQRLKLFSRLRLRDLLPVPPAVAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWA
EGKLDDEVMTAHVPPYKQPLEEDNNIRGDSTLEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSES
RAKALGLTPLGYLRSYAFAAIDVWQDMLLGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLANLQMFA
SERFAREKLGRSQAIGEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRRRGGGLGLTTACAAGGLG
AAMVLEVE
>gnl|CDD|181598 PRK08965, PRK08965, putative monovalent cation/H+ antiporter subunit E; Reviewed
MMRRLLPQPLLSLWLALVWLLLNGSFSLGNLLLGLLLGLLIPLLLALLVPLEGRLRRPLALLRLLLVVLY
DLVVSNIQVAWLILRPGPRPRPGFVAVPLRLRSDLALTLLANIITLTPGTVVVEISRDRRTLYVHVLDLD
DPEALIREIKQRYERLLMEIFE
>gnl|CDD|181599 PRK08972, fliI, flagellar protein export ATPase FliI
QNRQHQLLNRLKQYKVKVPPFRAVASGKLVRVVGLTLEATGCRAPVGSLCSIETMAGELEAEVVGFDGDL
LYLMPIEELRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRR
PITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTADVIVVGLVGERGREVKEFIEEI
LGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPA
TKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHY
PAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQNRDLISIGAYKQGSDPRIDNAIRLQPAMNAFLQ
QTMKEAVPYDMSVNMLKQLAAQCK
>gnl|CDD|236359 PRK08974, PRK08974, long-chain-fatty-acid--CoA ligase FadD
MEKVWLNRYPADVPAEINPDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLG
LKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVF
KTPVKHVILTRMGDQLSTAKGTLVNFVVKYIKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDLAF
LQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNL
LITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTG
QYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQ
RPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPS
EVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDNK
>gnl|CDD|181601 PRK08978, PRK08978, acetolactate synthase 2 catalytic subunit; Reviewed
MNGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIAT
SGPGATNLITGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAE
AFEIASSGRPGPVLVDIPKDIQLAEGELEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMA
GAVPALREFLAATGMPAVATLKGLGAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGK
LNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDLNALLPALQQPLNIDAWRQHCAQLRAEHAWRYDHPGE
AIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDD
TVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQWQQLFFDERYSETDLSDNPDFVMLASA
FGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDELENVWPLVPPGASNSEMLEKLS
>gnl|CDD|181602 PRK08979, PRK08979, acetolactate synthase 3 large subunit
MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGV
VLVTSGPGATNTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPE
IIKKAFYIASTGRPGPVVIDLPKDCLNPAILHPYEYPESIKMRSYNPTTSGHKGQIKRGLQALLAAKKPV
LYVGGGAIISGADKQILQLAEKLNLPVVSTLMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIG
VRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPIVGSADKVLDSMLALLDESGETNDEAAIASW
WNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQMFAALYYPFDKPRRWINSGGL
GTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGMVKQWQDMIYQ
GRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAMKDRLVFVDINVDETEHVYPMQIRGGA
MNEMWLSKTERT
>gnl|CDD|236360 PRK08983, fliN, flagellar motor switch protein FliN
SSDEDTADDWAAAMAEQALEEALAAELDELVDDSAPITEDEARKLDTILDIPVTISMEVGRSFISIRNLL
QLNQGSVVELDRVAGEPLDVMVNGTLIAHGEVVVVNDKFGIRLTDVISQTERIKKLK
>gnl|CDD|181604 PRK08990, PRK08990, flagellar motor protein PomA; Reviewed
MDLATLIGLIGAFAFVIMAMVLGGGIGMFVDVPSILIVFGGSLFVVLMKFNLGQFFGAVKIAGKAFMFKI
DKPEDLIEQIVEMADAARKGGFLALEEAEISNSFMQKGVDLLVDGHDGDVVRAALEKDIALTEERHETGI
GIFRAFGDVAPAMGMIGTLIGLVAMLSNMDDPKSIGPAMAVALLTTLYGAVLANMVAIPIADKLSLRMGE
EMLNRNLIMDAVLAIQDGQNPRVIEGFLKNYLAEKKRKIDTTDG
>gnl|CDD|181605 PRK08993, PRK08993, 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD
MILDAFSLEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEPTETIEQVTALGRRFLSLTADLRKID
GIPALLERAVAEFGHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGGKI
INIASMLSFQGGIRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSAEIL
DRIPAGRWGLPSDLMGPVVFLASSASDYINGYTIAVDGGWLAR
>gnl|CDD|181606 PRK08997, PRK08997, isocitrate dehydrogenase; Provisional
MKQTITVIPGDGIGPSIIDATLKILDKLGCDFEYEFADAGLTALEKHGELLPQRTLDLIEKNKIALKGPL
TTPVGEGFTSINVTLRKKFDLYANVRPVLSFPGTKARYDNIDIITVRENTEGMYSGEGQTVSEDGETAEA
TSIITRKGAERIVRFAYELARKEGRKKVTAVHKANIMKSTSGLFLKVAREVALRYPDIEFEEMIVDATCM
QLVMNPEQFDVIVTTNLFGDILSDLCAGLVGGLGMAPGANIGRDAAIFEAVHGSAPDIAGKNLANPTSVI
LAAIQMLEYLGMPDKAERIRKAIVAVIEAGDRTTRDLGGTHGTTDFTQAVIDRL
>gnl|CDD|236361 PRK08999, PRK08999, Nudix family hydrolase
SMKRIHVAAGVIRDADGRILLARRPEGKHQGGLWEFPGGKVEPGETVEQALARELQEELGIEVTAARPLI
TVRHDYPDKRVRLDVRRVTAWQGEPHGREGQPLAWVAPDELAVYPFPPANQPIVRALRLPDTYLITPEGE
DGDAAFLARLERALAAGIRLIQLRAPQLPPAAYRALARAALGLCRRAGAQLLLNGDPELAEDLGADGVHL
TSAQLAALAARPLPAGRWVAASCHDAEELARAQRLGVDFAVLSPVQPTASHPGAAPLGWEGFAALIAGVP
LPVYALGGLGPGDLEEAREHGAQGIAGIRGLW
>gnl|CDD|181608 PRK09004, PRK09004, FMN-binding protein MioC; Provisional
MADITLISGSTLGGAEYVADHLAEKLEEAGFSTETLHGPLLDDLSASGLWLIVTSTHGAGDLPDNLQPFF
EELQEQKPDLSQVRFAAIGIGSSEYDTFCGAIDKLEQLLKAKGAKQIGETLKIDVLQHPIPEDPAEEWLK
SWINLL
>gnl|CDD|181609 PRK09009, PRK09009, SDR family oxidoreductase
MNILIVGGSGGIGKAMVKQLLERYPDATVHATYRHHKPDFQHDNVQWHALDVTDEAEIKQLSEQFTQLDW
LINCVGMLHTQDKGPEKSLQALDADFFLQNITLNTLPSLLLAKHFTPKLKQSESAKFAVISAKVGSISDN
RLGGWYSYRASKAALNMFLKTLSIEWQRSLKHGVVLALHPGTTDTALSKPFQQNVPKGKLFTPEYVAQCL
LGIIANATPAQSGSFLAYDGETLPW
>gnl|CDD|236362 PRK09010, PRK09010, single-stranded DNA-binding protein; Provisional
MASRGVNKVILVGNLGQDPEVRYMPNGGAVANITLATSESWRDKQTGEMKEQTEWHRVVLFGKLAEVAGE
YLRKGSQVYIEGQLRTRKWTDQSGQDRYTTEVVVNVGGTMQMLGGRQGGGAPAGGNIGGQQQGGWGQPQQ
PQGGNQFSGGAQSRPQQSAPAAPSNEPPMDFDDDIPF
>gnl|CDD|181611 PRK09014, rfaH, transcription/translation regulatory transformer protein RfaH
MKSWYLLYCKRGQLQRAQEHLERQGVECLYPMITLEKIVRGKRTEVSEPLFPNYLFVEFDPEVIHTTTIR
STRGVSHFVRFGAQPAIVPSDVIYQLSVYKPEKIVDPETPKPGDKVIITEGAFEGLQAIYTEPDGEARSI
LLLNLLNKQVKHSVDNTQFRKI
>gnl|CDD|181613 PRK09019, PRK09019, stress response translation initiation inhibitor YciH
MSDSNSRLVYSTDTGRIDEEKAKPERPKGDGIVRIQRQTSGRKGKGVCLITGLDLDDAELKKLAAELKKK
CGCGGAVKDGVIEIQGDKRDLLKSLLEAKGMKVKLAGG
>gnl|CDD|181614 PRK09027, PRK09027, cytidine deaminase; Provisional
MQPRFQTALAQLPDALQSALAPILADQDFPAMLTAEQVSQLKSASGLDDDALALALLPLAAACAVTPISH
FNVGAIARGVSGNFYFGANMEFAGAALQQTVHAEQSAISHAWLRGEKAIADITVNYTPCGHCRQFMNELN
SASDLRIHLPGRQAHTLHDYLPDAFGPKDLNITTLLMDPQDHGLALDTGDPLIQAALDAANRSHAPYSQS
YSGVALETKDGRIYTGRYAENAAFNPSLPPLQGALNLLNLSGEDFSDIQRAVLVEKADAKLSQWDATQAT
LKALGCHELERVLLA
>gnl|CDD|181615 PRK09028, PRK09028, cystathionine beta-lyase; Provisional
MSEKKATKIVSAGRDKKWTKGVINPPVFRASTVVFDTVAEMRHAAKNRANGEMFYGRRGTPTHFAFQAAI
VELEGGAGTALYPSGAAAISNALLSFLKAGDHLLMVDSCYEPTRDLCDKILKGFGIETTYYDPMIGEGIR
ELIRPNTKVLFLESPGSITMEVQDVPTLSRIAHEHDIVVMLDNTWASPINSRPFEMGVDISIQAATKYIV
GHSDVMLGTATANEKHWDQLREHSYLMGQCTSPDDVYLAMRGLRTLGVRLAQHEKNALKVANWLATRPEV
DHVRHPAFETCPGHEFFKRDFSGSNGLFSFVLKQGDPKAVTALVEGMQHFKMGFSWGGFESLILGVFGIN
KLRTATNWDFSKPLIRLHIGLEDVDDLIADLEAGFERYNAVLAA
>gnl|CDD|236363 PRK09029, PRK09029, O-succinylbenzoic acid--CoA ligase; Provisional
MMIFSDWPWRHWAQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAY
LALLQCGARVLPLNPQLPQPLLEELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATM
TLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQGIVWRWLYAGATLVVRDKQ
PLEQALAGCTHASLVPTQLWRLLDNRSEPLSLKAVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMASTV
CAKRADGLAGVGSPLPGREVKLVDGEIWLRGASLALGYWRQGQLVPLVNDEGWFATRDRGEWQNGELTIL
GRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVNLAEWLQDKLA
RFQQPVAYYLLPPELKNGGIKISRQALKEWVAQQLGNN
>gnl|CDD|236364 PRK09034, PRK09034, aspartate kinase; Reviewed
MKVVKFGGSSLASAEQFKKVLNIVKSDPERKIVVVSAPGKRFKEDTKVTDLLILYAEAVLAGEDYEDIFE
AIIARYAEIAKELGLDADILEKIEEILEHLANLASRNPDRLLDAFKARGEDLNAKLIAAYLNYEGIPARY
VDPKEAGIIVTDEPGNAQVLPESYDNLKKLRDRDEKLVIPGFFGVTKDGQIVTFSRGGSDITGAILARGV
KADLYENFTDVDGIYAANPRIVKNPKSIKEITYREMRELSYAGFSVFHDEALIPAYRGGIPINIKNTNNP
EDPGTLIVPDRDNKNKNPITGIAGDKGFTSIYISKYLMNREVGFGRKVLQILEDHGISYEHMPSGIDDLS
IIIRERQLTPKKEDEILAEIKQELNPDELEIEHDLAIIMVVGEGMRQTVGVAAKITKALAEANINIQMIN
QGSSEISIMFGVKNEDAEKAVKAIYNAFFKEVLV
>gnl|CDD|181618 PRK09038, PRK09038, flagellar motor protein MotD; Reviewed
MMRRRKHHEEHENHERWLVSYADFITLLFAFFVVMYAISSVNEGKYKVLSEALTGAFNGPSRSMKPIPIG
KEQPKTTQPARPLVIDSEQPDARAQDQLKTIADDLRKALGPLIESGQVTVRRNELWIEIEINSSLLFGSG
DAMLSDQAFAILEKVAEVLKPAPNPIHVEGFTDNVPIATAQFPSNWELSAARAASVVRLLADDGVAPSRL
AAVGYGEFQPVADNDTAEGRARNRRVVLVILRNLDVRRSLTPVGSANATPDAALRRAGTQAAPATAKTDS
G
>gnl|CDD|181619 PRK09039, PRK09039, peptidoglycan -binding protein
MALARRRRRRRGVDYWPGFVDALSTLLLVIMFLLTVFVVAQFFLSREISGKDSALDRLNSQIAELADLLS
LERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVE
LLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRVQELNRYRSEFFGRLREILGDR
EGIRIVGDRFVFQSEVLFPTGSAELNPEGQAEIAKLAAALIELAKEIPPEINWVLRVDGHTDNVPLSGTG
RFRDNWELSSARAISVVKFLIALGVPADRLAAAGFGEFQPLDPGDTPEARARNRRIELKLTER
>gnl|CDD|181620 PRK09040, PRK09040, hypothetical protein; Provisional
SDEIDGGVEQTAPVWAVFGDLMSVLLGAFVLILVGVIGVQLELSSKLEAEVKQRQAEAQRRKTLEQALAG
PLAAGRVTLVNGRIGISGSVLFALNSDQLQPEGRELLKSLAGPLAAYLRARDEILMVSGFTDDQPVRAGN
RRFADNWELSAQRALTVTRALIDAGVPASSVFAAAFGSEQPVASNADDEGRAKNRRVEIAPVPRPSASAG
AARG
>gnl|CDD|236365 PRK09041, motB, motility protein MotB
MKKENHPPIVVKRVKKKGHGHHGGSWKIAYADFMTAMMAFFLVMWLLSSSTPEQLIGIAEYFRTPLKVAL
TGGDRSSDSTSPIPGGGDDITQQDGEVNKQPNIAELAQGEKERREQERLEKLKQELDQAIESNPKLRQFK
PQLLIDLTQEGLRIQIVDSQNRPMFATGSAEVEPYMRDILREIAPVLNDVPNRISLSGHTDATPYANGEK
GYSNWELSADRANASRRELVAGGMDEGKVLRVVGLASTMLLDKKDPLNPVNRRISIVVLNKKAEEAILHE
NAESVALSAQNEPVSALEAPAAAPAASVPAAPAAEPR
>gnl|CDD|236366 PRK09045, PRK09045, TRZ/ATZ family hydrolase
PMPMEPVDLLIEARWIVPVEPAGVVLEDHAVAIRDGRIVAILPRAEARARYAAAETVELPDHVLIPGLIN
AHTHAAMSLLRGLADDLPLMTWLQDHIWPAEGAWVSEEFVRDGTLLAIAEMLRGGTTCFNDMYFFPEAAA
EAAHQAGMRAQIGMPVLDFPTAWASDADEYLAKGLELHDQWRHHPLISTAFAPHAPYTVSDENLERIRTL
AEQLDLPIHIHLHETAQEIADSLKQHGQRPLARLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHC
PESNLKLASGFCPVAKLLQAGVNVALGTDGAASNNDLDLFGEMRTAALLAKAVAGDATALPAHTALRMAT
LNGARALGLDDEIGSLEPGKQADLVAVDLSGLETQPVYDPVSQLVYAAGREQVSHVWVAGKQLLDDRELT
TLDEAELLARARQWREKIAAKRA
>gnl|CDD|236367 PRK09047, PRK09047, RNA polymerase factor sigma-70; Validated
VRDDDAALDIVQDAMIKLAEKYGDRPAAEWPPLFQRILQNRIHDWFRRQKVRNTWVSLFSSFSDDDDDDD
FDPLETLDSADEGAESPADKLERAQVLQLIEEAIQKLPARQREAFLLRYWEDMDVAETAAAMGCSEGSVK
THCSRATHALAKALEAKGITL
>gnl|CDD|181624 PRK09050, PRK09050, beta-ketoadipyl CoA thiolase; Validated
MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNPGVDWEAVDDVIYGCANQAGEDNRNVARM
SALLAGLPVSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSRQAEI
FDTTIGWRFVNPLMKAQYGVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTI
PQKKGDPVVVDRDEHPRPETTLEALAKLKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRA
RILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLADDDARVNPNG
GAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIERV
>gnl|CDD|181625 PRK09051, PRK09051, beta-ketothiolase BktB
MMREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRV
AAINAGVPQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAK
LVDMMVGALHDPFGTIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKG
EVVFDTDEHVRADTTLEDLAKLKPVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGY
AHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGH
PVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFERL
>gnl|CDD|181626 PRK09052, PRK09052, acetyl-CoA C-acyltransferase
MSKQLQDAYIVAATRTPVGKAPRGMFKNTRPDDLLAHVLRSAVAQVPGLDPKLIEDAIVGCAMPEAEQGL
NVARIGALLAGLPNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKPSMSPA
IFARDENVGIAYGMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFPDLAT
GEVDVKTRTVDLDEGPRADTSLEGLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLA
RFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGA
IALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGIFERL
>gnl|CDD|181627 PRK09053, PRK09053, 3-carboxy-cis,cis-muconate cycloisomerase; Provisional
LEASARLTDLYFGSPAMRAIFSDRATVQRMLDFEAALARAEAACGVIPAAAVAPIEAACDAERLDLDALA
QAAALAGNLAIPLVKQLTAQVAARDAEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALAT
LAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGGAAGTLASLGEQALP
VAQALAAELQLALPALPWHTQRDRIAEFASALGLLAGTLGKIARDVSLLMQTEVGEVFEPAAAGKGGSST
MPHKRNPVGCAAVLTAATRAPGLVATLFAAMPQEHERALGGWHAEWDTLPELACLAAGALAQMAQIVEGL
EVDAARMRANLDLTHGLILAEAVMLALADRIGRLDAHHLVEQASKRAVAEGRHLRDVLAEDPQVSAHLSP
AALDRLLDPAHYLGQAHAWVDRVLAEHASRHA
>gnl|CDD|181631 PRK09059, PRK09059, dihydroorotase; Validated
MMRPILLANARIIDPSRGLDEIGTVLIEDGVIVAAGKGAGNQGAPEGAEIVDCAGKAVAPGLVDARVFVG
EPGAEHRETIASASRAAAAGGVTSIIMMPDTDPVIDDVALVEFVKRTARDTAIVNIHPAAAITKGLAGEE
MTEFGLLRAAGAVAFTDGRRSVANTQVMRRALTYARDFDAVIVHETRDPDLGGNGVMNEGLFASWLGLSG
IPREAEVIPLERDLRLAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVSINHLSLNENDIGEYRTF
FKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQDVDTKRLPFSEAAAGAIGLETLLAAALRLYHNGEV
PLLRLIEALSTRPAEIFGLPAGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTI
VAGKTVYEL
>gnl|CDD|181632 PRK09060, PRK09060, dihydroorotase; Validated
MTQTFDLILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAGEVIDCRGLHVLPGVIDSQVHFREPGL
EHKEDLETGSRAAVLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELE
RLPGCAGIKVFMGSSTGDLLVEDDEGLRRILRNGRRRAAFHSEDEYRLRERKGLRVEGDPSSHPVWRDEE
AALLATRRLVRLARETGRRIHVLHVSTAEEIDFLADHKDVATVEVTPHHLTLAAPECYERLGTLAQMNPP
IRDARHRDGLWRGVRQGVVDVLGSDHAPHTLEEKAKPYPASPSGMTGVQTLVPIMLDHVNAGRLSLERFV
DLTSAGPARIFGIAGKGRIAVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQR
VMWDGELVGPPTGEPVRFLETLPR
>gnl|CDD|236369 PRK09061, PRK09061, D-glutamate deacylase; Validated
SAKVAVLSLLLMPASMAPYDLVIRNGRVVDPETGLDAVRDVGIKGGKIAAVGTAAIEGDRTIDATGLVVA
PGFIDLHAHGQSVAAYRMQAFDGVTTALELEAGVLPVARWYAEQAGEGRPLNYGASVGWTPARIAVLTGP
QAEGTIADFGKALGDPRWQERAATPAELAEILELLEQGLDEGALGIGIGAGYAPGTGHKEYLELARLAAR
AGVPTYTHVRYLSNVDPRSSVDAYQELIAAAAETGAHMHICHVNSTSLRDIDRCLALVEKAQAQGLDVTT
EAYPYGAGSTVVGAAFFDPGWLERMGLGYGSLQWVETGERLLTREELAKLRANDPGGLVLIHFLDEDNPR
DRALLDRSVLFPGAAIASDAMPWTWSDGTVYEGDAWPLPEDAVSHPRSAGTFARFLREYVRERKALSLLE
AIRKCTLMPAQILEDSVPAMRRKGRLQAGADADIVVFDPETITDRATFEDPNRPSEGVRHVLVNGVPVVS
NGELVRDARPGRPVRRPVK
>gnl|CDD|181635 PRK09065, PRK09065, glutamine amidotransferase; Provisional
VKPLLIIQTGTPPPSIRARYGDFPHWIRVALGLAEQPVVVVRVFAGEPLPAPDDFAGVIITGSWAMVTDR
LDWSERTADWLRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVELHPAAADDPLFAGLPA
QFPAHLTHLQSVLRLPPGAVVLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRARADCLRREGLD
ARTLLREVSEAPWARKLLRRFVRLARR
>gnl|CDD|236371 PRK09070, PRK09070, aminodeoxychorismate synthase component I
MTLTRPLPADIDLLALHRLAPERYPALLESSASGTAQGRWDVLLLAQGKCLRLDPDGVTRQLLEGDFLDA
LDAAWQAERVPHDGESSLPFRGGWAVLLDYELAGQVEPILKLPMRTDGLPLALALRAPAAVLRDRHSGRC
VLVAEPGREHLLDQIEADLAACAALPPLPVWLAPQAVEEDPPERFTDGVERVLDYIRAGDVFQVNLSRAW
QAQFANAVDPAALYARLRAANPAPFSGLFVAAGRAIVSSSPERLVSVQGGVVQTRPIAGTRPRFAGDDDA
ALIRELVGHPKERAEHVMLIDLERNDLGRICAPGSVEVDELMTVESYAHVHHIVSNVRGRLRDGVTPGEV
IRAVFPGGTITGCPKVRCMQIIAELEQTPRGAYTGSFGYLNRDGDMDLNILIRTAEVQGNQVRFRTGAGI
VVDSDPERELDETRAKARGLLRALEQA
>gnl|CDD|181637 PRK09071, PRK09071, glycosyl transferase family protein
EHPFAEYIRILGKGKRGRRSLTREEARQAMGMILDGEVEDDQLGAFLMLLRVKEETAEELAGFVEAIRER
LQAPPLAVDLDWPSYAGKRRHLPWYLLAAKLLAQNGYRVLLHGGGGHTAGRLYTEQLLEALGIPIARSWQ
EAEQALEEHNIAYLPLEDFAPQLQRMIDLRNTLGLRSPINTLARLLNPLNAKASLQGIFHPGYQQLHREA
ARLLGDQNALVFKGEGGESERNPDVSTTLYGSRNGEAWDEEWPALSEERHVKPEELDPEQLLAVWRGEEE
DEYGENAVIATMALALWRGLNQSREEAFEKAAQLWATRDKSIA
>gnl|CDD|236372 PRK09072, PRK09072, SDR family oxidoreductase
MDLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRHRWVVADLTSEAGREA
VLARAREMGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGST
FGSIGYPGYASYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAMNSEAVQALNRALGNAMDDPED
VAAAVLQAIEKERAERWLGWPEKLFVRLNGLLPSLVDRALRKQLPVIHRFARR
>gnl|CDD|236373 PRK09076, PRK09076, enoyl-CoA hydratase; Provisional
MMIELDLEIDGHVAILTLNNPPANTWTADSLQALKQLVLELNADKDVYALVITGDGEKFFSAGADLNLFA
DGDKAVAREMARRFGEAFEALSAFRGVSIAAINGYAMGGGLECALACDIRIAEEQAQMALPEASVGLLPC
AGGTQNLPWLVGEGWAKRMILCGERVDAATALRIGLVEEVVEKGEAREAALALAQKVANQSPSAVAACKT
LIQAARNGPRAAALALERELFVDLFDTEDQREGVNAFLEKRAPQWKND
>gnl|CDD|236374 PRK09077, PRK09077, L-aspartate oxidase; Provisional
MNTSPEHQCDVLIIGSGAAGLSLALRLAEHRRVAVLSKGPLSEGSTFYAQGGIAAVLDETDSIESHVEDT
LIAGAGLCDEDAVRFIAENAREAVQWLIDQGVPFTTDEQANGEEGYHLTREGGHSHRRILHAADATGKAV
QTTLVERARNHPNITVLERHNAIDLITSDKLGLPGRRVVGAYVLNRNKERVETIRAKFVVLATGGASKVY
LYTTNPDIASGDGIAMAWRAGCRVANMEFNQFHPTCLYHPQARSFLITEALRGEGAYLKLPDGTRFMPDF
DERAELAPRDIVARAIDHEMKRLGADCVYLDISHKPADFIRQHFPTIYERCLELGIDITKEPIPVVPAAH
YTCGGVMVDLHGRTDLDGLYAIGEVSYTGLHGANRMASNSLLECLVYGRSAAEDILSRLPKAPMPPTLPA
WDESRVTDSDEEVVIQHNWHELRLFMWDYVGIVRTTKRLERALHRIRLLQQEIDEYYANFRVSNNLLELR
NLVQVAELIVRCAMERKESRGLHYTLDYPELLPEAGPTILSPPNRA
>gnl|CDD|181642 PRK09082, PRK09082, methionine aminotransferase; Validated
MTNNPLIPQSKLPNVGTTIFTVMSALAAEHGAINLSQGFPDFDGPPYLVEALAYAMAAGHNQYPPMTGVA
ALREAIAAKTARLYGRQYDADSEITVTAGATEALFAAILALVRPGDEVIVFDPSYDSYAPAIELAGGRAV
RVALQPPDFRVDWQRFAAAISPRTRLIILNTPHNPSGTVWSAADMRALWQLIAGTDIYVLSDEVYEHIVF
DGAGHASVLRHPELRERAFVVSSFGKTYHVTGWKVGYCVAPAALSAEFRKVHQYNTFTVNTPAQLALADY
LRAEPEHYLELPAFYQAKRDRFRAALANSRFKLLPCEGTYFQLVDYSAISDLDDVEFCQWLTREHGVAAI
PLSVFYADPFPHRLVRLCFAKQEETLDAAAERLCQL
>gnl|CDD|236376 PRK09084, PRK09084, aspartate kinase III; Validated
LVVAKFGGTSVADFDAMNRSADIVLSNPNTRLVVLSASAGVTNLLVALAEGAEPGDERLALLDEIRQIQY
AILDRLGDPNVVREEIERLLENITVLAEAASLATSPALTDELVSHGELMSTLLFVELLRERGVQAEWFDV
RKVMRTDDRFGRAEPDVAALAELAQEQLLPLLAEGVVVTQGFIGSDEKGRTTTLGRGGSDYSAALLAEAL
NASRVEIWTDVPGIYTTDPRIVPAAKRIDEISFEEAAEMATFGAKVLHPATLLPAVRSNIPVFVGSSKDP
EAGGTWICNDTENPPLFRAIALRRNQTLLTLHSLNMLHARGFLAEVFGILARHKISVDLITTSEVSVSLT
LDTTGSTSTGDTLLTQALLTELSQLCRVEVEEGLALVALIGNNLSKACGVAKRVFGVLEPFNIRMICYGA
SSHNLCFLVPESDAEQVVQALHQNLFEG
>gnl|CDD|169652 PRK09087, PRK09087, hypothetical protein; Validated
MRDAPEQLPLNFSHDPAYGRDDLLVTESNRAAVSLVDHWPNWPSPVVVLAGPVGSGKTHLASIWREKSDA
LLIHPNEIGSDAANAAAEGPVLIEDIDAGGFDETGLFHLINSVRQAGTSLLMTSRLWPSSWNVKLPDLKS
RLKAATVVEIGEPDDALLSQVIFKLFADRQLYVDPHVVYYLVSRMERSLFAAQTIVDRLDRLALERKSRI
TRALAAEVLNEMGQAG
>gnl|CDD|181644 PRK09088, PRK09088, acyl-CoA synthetase; Validated
IAFHARLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARV
GAIYVPLNWRLSASELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADALEPADTPSIPPERVSLI
LFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNG
FEPKRTLGRLGDPALGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDDGIPMV
DGFGMSEAGTVFGMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRP
QATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADA
QWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGRK
>gnl|CDD|236377 PRK09094, PRK09094, putative monovalent cation/H+ antiporter subunit C; Reviewed
MELVLALAIGVLTASGVWLLLRPRTFQVILGLSLLSYAVNLFIFAMGRLRVGAPPVLQPGVPVDLANYTD
PLPQALVLTAIVIGFAMTALFLVVALASRGLTGTDHVDGREPEE
>gnl|CDD|181646 PRK09098, PRK09098, HrpE/YscL family type III secretion apparatus protein
MAIWLRSTPAALGLSCDVIPREAFATVLALDAALAAVHAERDAVLAAARARAERIVAEARAQAEAILEAA
RREADRSARRGYAAGLRQALAEWHARGADHAFAERRAARRMRERLAEIVAAAVEQIVLGEDRAALFARAA
QTLERVVDGASYLTVRVHPADLDAARAAFGAAAAAGGRNVPVEVVGDPRLAPGACVCEWDFGVFDASLDT
QLRALRRALARALAAPQEDAGRA
>gnl|CDD|169656 PRK09099, PRK09099, type III secretion system ATPase; Provisional
ALAELSRLADALERELAALPAVRRTGKVVEVIGTLLRVSGLDVTLGELCELRQRDGTLLQRAEVVGFSRD
VALLSPFGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSR
RMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCDVNVIALIGERGREVREFIEL
ILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPP
ARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYP
AIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVGEYRAGSDPVADEAIAKIDAIRDFLSQ
RTDEYSDPDATLAALAELSGD
>gnl|CDD|181647 PRK09101, nrdB, ribonucleotide-diphosphate reductase subunit beta; Reviewed
MAYTTFSQTKNDQLKEPMFFGQSVNVARYDQQKYEIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHE
KHIFISNLKYQTLLDSIQGRSPNVALLPLVSIPELETWIETWSFSETIHSRSYTHIIRNIVNDPSVVFDD
IVTNEEILKRAKDISSYYDDLIEMTSYYHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFY
VSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLMRSGKDDPEMAEIAEECKQECYDLFVQA
AEQEKEWADYLFKDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINAWLVSDNVQVAPQ
EVEVSSYLVGQIDSEVDTDDLSDFEL
>gnl|CDD|236378 PRK09102, PRK09102, ribonucleoside-diphosphate reductase subunit alpha
EKMQNKLVFQINIDRSRDAWLTEFGKATLRDRYLLEGESYQDLFARIAEAYADIDPEHAQRFYDYMSRGW
FMPATPVLSNGGTDRGLPISCFLNYVEDSLEGIVNTWNENVWLAKRGGGIGSYWGNVRSIGEPIRNNGKS
SGIIPFIKVMDSLTLAISQGSLRRGSFAVYLDIEHPEIEEFLDIRKPTGDPNRKALNLHHGVCVTDEFME
AVEDGDEWDLISPKDKSVIRTVKARDLWAKILETRIETGEPYLLFIDNVNRALPEVYKDLGLKVKASNLC
SEITLPTGIDHLGEDRTAVCCLSSLNLEYYDEWKDTDAFIEDLMRFLDNVLQDFIDKAPDEMERAKYSAM
RERSVGLGVMGFHSYLQSKMIPFESVMAKQWNKKIFKHIREQADKASKELAKEKGECPDAAGYGVMRRFS
TKMAIAPTASISIILGNTSPGIEPIAANYYTHKTLKGSFTVKNKYLEKLLEEKGKDTDEVWSSILTNEGS
VQHLDFLSEEEKDVFKTAFEIDQRWIIELAADRQKYIDQAQSLNLFLPANVPKRDLNKLHFEAWKKGVKS
LYYQRSKSVQRADKVSHDVLKKRLVEKSAFNRDYDECLACQ
>gnl|CDD|181649 PRK09103, PRK09103, ribonucleoside-diphosphate reductase subunit alpha
SLLVTKRDGRTERINLDKIHRVITWAAEGLHNVSVSQVELRSHIQFYDGIKTSDIHETIIKAAADLISRD
APDYQYLAARLAIFHLRKKAYGQFEPPALYDHVVKMVEMGKYDKHLLEDYTEEEFDQMDTFIDHWRDMNF
SYAAVKQLEGKYLVQNRVTGEIYESAQFLYILVAACLFSNYPKETRLDYVKRFYDAVSTFKISLPTPIMS
GVRTPTRQFSSCVLIECGDSLDSINATSSAIVKYVSQRAGIGINAGRIRALGSPIRGGEAFHTGCIPFYK
HFQTAVKSCSQGGVRGGAATLFYPIWHLEVESLLVLKNNRGVEENRVRHMDYGVQINKLMYQRLIKGGDI
TLFSPSDVPGLYDAFFADQDEFERLYTKYEQDDSIRKKRVKAVELFSLMMQERASTGRIYIQNVDHCNTH
SPFDPKVAPVRQSNLCLEIALPTKPLNDVNDENGEIALCTLSAFNLGAINSLDELEELADLAVRALDALL
DYQDYPIPAAKRGAMGRRTLGIGVINFAYYLAKNGVRYSDGSANNLTHKTFEAIQYYLLKASNELAKEQG
ACPWFNETTYAQGILPIDTYKKDLDAICNEPLHYDWETLREEIKTHGLRNSTLSALMPSETSSQISNATN
GIEPPRGYVSIKASKDGILKQVVPDYERLKDAYELLWEMPNNDGYLQLVGIMQKFVDQSISANTNYDPSR
FPSGKVPMKQLLKDLLTAYKFGVKTLYYHNTRDGAEDAQDDLQPSIQDDGCEGGACKI
>gnl|CDD|236379 PRK09104, PRK09104, hypothetical protein; Validated
SMADLDPVLDHIDANLDASLERLFALLRIPSISTDPAYAADCRKAADWLVADLASLGFEASVRDTPGHPM
VVAHHEGPTGDAPHVLFYGHYDVQPVDPLDLWESPPFEPRIKETPDGRKVIVARGASDDKGQLMTFVEAC
RAWKAVTGSLPVRVTILFEGEEESGSPSLVPFLEANAEELKADVALVCDTGMWDRETPAITTSLRGLVGE
EVTITAADRDLHSGLFGGAAANPIRVLTRILAGLHDETGRVTLPGFYDGVEELPPEILAQWKALGFTAEA
FLGPVGLSIPAGEKGRSVLEQIWSRPTCEINGIWGGYTGEGFKTVIPAEASAKVSFRLVGGQDPAKIREA
FRAYVRARLPADCSVEFHDHGGSPAIALPYDSPALAAAKAALSDEWGKPAVLIGSGGSIPIVGDFKRILG
MDSLLVGFGLDDDRIHSPNEKYDLESFHKGIRSWARILAALAEA
>gnl|CDD|181651 PRK09105, PRK09105, pyridoxal phosphate-dependent aminotransferase
MMLALSRRSFLRLAALGAAAAALGLLAAAAAAAKRAAAPPAAEGAVFLNANECPLGPSPAARDAAARSAA
LSGRYDLELEDDLRTLFAAQEGLPADHVMAYAGSSEPLNYAVLAFTSPTAGLVTADPTYEAGWRAADAQG
APVAKVPLRADGAHDVKAMLAADPNAGLIYICNPNNPTGTVTPRADIEWLLANKPAGSVLLVDEAYIHFS
DAPSVVDLVAQRKDLIVLRTFSKLYGMAGMRLGLAAARPDLLAKLARFGHNPLPVPAAAAGLASLRDPKL
VPQRRAENAAVREDTIAWLKKKGYKCTPSQANCFMVDVKRPAKAVADAMAKQGVFIGRSWPIWPNWVRVT
VGSEEEMAAFRSAFAKVMRG
>gnl|CDD|236380 PRK09107, PRK09107, acetolactate synthase 3 catalytic subunit; Validated
SAQKSHMPRQMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYAR
STGKPGVVLVTSGPGATNAVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVK
DVNDLARVIHEAFHVATSGRPGPVVVDIPKDVQFATGTYTPPQKAPVHVSYQPKVKGDAEAITEAVELLA
NAKRPVIYSGGGVINSGPEASRLLRELVELTGFPITSTLMGLGAYPASGKNWLGMLGMHGTYEANMAMHD
CDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRVDVPIIGDVGHVLEDMLRLWKARGKKP
DKEALADWWGQIARWRARNSLAYTPSDDVIMPQYAIQRLYELTKGRDTYITTEVGQHQMWAAQFFGFEEP
NRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYMGMV
RQWQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCF
PMIPSGKAHNEMLLPDEATDEAVANAIDAKGRALV
>gnl|CDD|181654 PRK09109, motC, flagellar motor protein; Reviewed
MDVLSLIGLILAFVAIIGGQVLEGGHLGSLLNGPAFLIVIGGTLGAVLLQTPLAVFKRAFKILRWVFFPP
RSDLEGGIDRIVEWSNTARKEGLLGLEDVADREPDPFARKGLQLLVDGAEPESIRSVLEVEIDTQEHRDL
QAAKVFESMGGYAPTIGIIGAVMGLIHVMENLADPSQLGSGIAVAFVATIYGVASANLLFLPVANKLKSI
IHRQSRYREMLVEGLVAIAEGENPRSIELKLQGYLH
>gnl|CDD|181655 PRK09110, PRK09110, flagellar motor stator protein MotA
MLIIIGYIVVLGSVFGGYLLAGGHLGALIQPAELLIIGGAALGAFIVGNPGKAIKATLKALPKLFKGPKY
KKADYMDLLALLYELLRKARQEGMMALEAHIENPEESPIFAKYPKILKDHHLVDFICDYLRLMISGNMNP
HEIEALMDEEIETHHHEAEVPAHALQKVADALPAFGIVAAVLGVVKTMGSIDQPPAVLGALIGAALVGTF
LGILLAYGFVGPLAARLEQVVEEDTKMYQCIKVTLLASLNGYAPQIAVEFGRKTLPSTERPSFAELEEHV
RGV
>gnl|CDD|236382 PRK09111, PRK09111, DNA polymerase III subunits gamma and tau; Validated
APDAAAAATPYRVLARKYRPQTFDDLIGQEAMVRTLTNAFETGRIAQAFMLTGVRGVGKTTTARILARAL
NYEGPDGDGGPTIDLCGVGEHCQAIMEGRHVDVLEMDAASHTGVDDIREIIESVRYRPVSARYKVYIIDE
VHMLSTAAFNALLKTLEEPPPHVKFIFATTEIRKVPVTVLSRCQRFDLRRIEADVLAAHLSRIAAKEGVE
VEDEALALIARAAEGSVRDGLSLLDQAIAHGAGEVTAEAVRDMLGLADRARVIDLFEALMRGDVAAALAE
FRAQYDAGADPVVVLTDLAEFTHLVTRLKIVPDAAEDPSLSEAERTRGAEFAKKLSMRVLSRLWQMLLKG
IEEVQGAPRPLAAAEMVLIRLAYAADLPTPDEALRRLQEGPPSPGGGGGGPPGGGGAPGAPAAAAAPGAA
AAAPAAGGPAAALAAVPDAAAAAAAPPAPAAAPQPAVRLNSFEDIVALAEEKRDIKLKAAVERDVRLVRF
EPGRLEFALAPGAPRDLAQRLARKLEEWTGRRWVVSVSREGGQPTLAEQEAAAREEREAAAEADPLVAAV
LAAFPGAKIVDVRDLAPEAAEEEPAAEAEDPDALPDDD
>gnl|CDD|169667 PRK09112, PRK09112, DNA polymerase III subunit delta'; Validated
MEELMIPEQHDDLDGVPSPSENTRLFGHEEAEAFLAQAYREGKLHHALLFEGPEGIGKATLAFHLANHIL
SHPDPAEAPETLADPDPASPVWRQIAQGAHPNLLHITRPFDEKTGKFKTAITVDEIRRVGHFLSQTSGDG
NWRIVIIDPADDMNRNAANAILKTLEEPPARALFILISHSSGRLLPTIRSRCQPISLKPLDDDELKKALS
HLGSSQGSDGEITEALLQRSKGSVRKALLLLNYGGLEIIATIDQLLAGSGPDARKAHKLADALSGRESEV
QFDFFRDHLLDRIMAEARRAAEAGDLALAERLARLWSEIIEEIVEAEAYNLDRKQTVISLLEKLHRAFRT
G
>gnl|CDD|181657 PRK09116, PRK09116, beta-ketoacyl-ACP synthase
MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYDGLNTRLAAPIDDFELPAHYTRKKIRSM
GRVSLMATRASELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMP
HTTAVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATST
RNDAPELTPRPFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIA
MELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATAAVFGARMPISSLKSYFGHTLGACGALEAWMSIE
MMNEGWFAPTLNLTQVDPACGALDYIMGEAREIDTEYVMSNNFAFGGINTSLIFK
>gnl|CDD|236383 PRK09120, PRK09120, p-hydroxycinnamoyl CoA hydratase/lyase; Validated
MSYENRWDTVKVEVEDGIAWVTLNRPEKRNAMSPTLNREMIDVLDALEFDDDAGVLVLTGAGDAWSAGMD
LKEYFRETDAQPEILQERIRREAYGWWRRLRWYQKPTIAMVNGWCFGGGFSPLVACDLAIAADEAQFGLS
EINWGIPPGGGVSKAMADTVGHRDALYYIMTGETFTGRKAAEMGLVNESVPLAQLRARTRELAAKLLEKN
PVVLRAAKDGFKRVRELTWDQAEDYLYAKLEQANSLDPEGGREEGLKQFLDDKSYKPGLGAYKRS
>gnl|CDD|181659 PRK09121, PRK09121, methionine synthase
TLLPTSTAGSLPKPSWLAEPETLWSPWKLQGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTT
FIEHLSGVDFEKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLY
DDHYKSREKLAWEFAKILNQEAKELEAAGVDIIQFDEPAFNVFFDEVNDWGVAALERAIEGLKCETAVHI
CYGYGIKANTDWKKTLGSEWRQYEEAFPKLQKSNIDIISLECHNSRVPMDLLELIRGKKVMVGAIDVASD
TIETPEEVADTLRKALQFVDADKLYPCTNCGMAPLSRDVARGKLNALSAGAEIVRRELA
>gnl|CDD|181661 PRK09124, PRK09124, ubiquinone-dependent pyruvate dehydrogenase
MKQTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVC
AGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRV
LAIAMRKAILNRGVAVVVLPGDVALKPAPERATPHWYHAPQPVVTPAEEELRKLAALLNGSSNITLLCGS
GCAGAHDELVALAETLKAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYRQ
FYPTDAKIIQIDINPGSLGRRSPVDLGLVGDVKATLAALLPLLEEKTDRKFLDKALEHYRKARKGLDDLA
VPSDGGKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGA
QAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEMKAGGYLTDGTDLHNPDFA
AIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMPPQIKLEQAKGFSLYMLRAIISGR
GDEVIELAKTNWLR
>gnl|CDD|181662 PRK09125, PRK09125, DNA ligase; Provisional
FLLLLLLLALALLLALLLLASSANAAAPDLQLATVYDKGQDISGYLVSEKLDGVRAYWDGKQLLTRQGNP
IAAPAWFTAGFPPFPLDGELWAGRGQFEAISSIVRDKTPDDAAWRKVRFMVFDLPDAPGDFEERLAVLKK
LLAKLPSPYIKIIEQIRVRSEAALQQFLDQIVAAGGEGLMLHRPDAPYEAGRSDDLLKLKPYYDAEATVI
GHLPGKGKFAGMLGALLVETPDGREFKIGSGFSDAERENPPKIGSIITYKYRGLTKNGLPRFASFLRVRE
DE
>gnl|CDD|236385 PRK09126, PRK09126, FAD-dependent hydroxylase
MMHSDIVVVGAGPAGLSFARSLAGSGLKVTLIERQPLAALADPAFDGREIALTHASREILQRLGAWDRIP
EDEISPLRDAKVLNGRSPFALTFDARGRGADALGYLVPNHLIRRAAYEAVSQQDGIELLTGTRVTAVRTD
DDGAQVTLANGRRLTARLLVAADSRFSATRRQLGIGADMHDFGRTMLVCRMRHELPHHHTAWEWFGYGQT
LALLPLNGHLSSLVLTLPPDQIEALLALDPEAFAAEVTARFKGRLGAMRLVSSRHAYPLVAVYAHRFVAK
RFALIGDAAVGMHPVTAHGFNLGLKGQDILARLILAAARRGQDIGAASLLERYERKHRLATRPLYHATNA
IAALYTDDRPPARLLRRAVLRAANRFPPLKQAIAKQLTGRKK
>gnl|CDD|236388 PRK09133, PRK09133, hypothetical protein; Provisional
RKTTARALALALALLAAAAATGAAAAAAPAAPTADQQAARDLYKELIEINTTASTGSTTPAAEAMAARLK
AAGFADADIEVTGPYPRKGNLVARLRGTDPKKPILLLAHMDVVEAKREDWTRDPFKLVEENGYFYGRGTS
DDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEGTPMNGVAWLAENHRDLIDAEFALNEGGGGTLDE
DGKPVLLTVQAGEKTYADFRLEVTNPGGHSSRPTKDNAIYRLAAALSRLAAYRFPVMLNDVTRAYFKQSA
AIETGPLAAAMRAFAANPADEAAIALLSADPSYNAMLRTTCVATMLEGGHAENALPQRATANVNCRIFPG
DTIEAVRATLKQVVADPAIKITRIGDPSPSPASPLRPDIMKAVEKLTAAMWPGVPVIPSMSTGATDGRYL
RAAGIPTYGVSGLFGDPDDTFAHGLNERIPVASFYEGRDFLYELVKDLAGGA
>gnl|CDD|236389 PRK09134, PRK09134, SDR family oxidoreductase
SPPMSMAAPRAALVTGAARRIGRAIALDLAAHGFDVAVHYNRSRDEAEALAAEIRALGRRAVALQADLAD
EAEVRALVARASAALGPITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGL
VVNMIDQRVWNLNPDFLSYTLSKAALWTATRTLAQALAPRIRVNAIGPGPTLPSGRQSPEDFARQHAATP
LGRGSTPEEIAAAVRYLLDAPSVTGQMIAVDGGQHLAWLTPDVAGITE
>gnl|CDD|181668 PRK09135, PRK09135, pteridine reductase; Provisional
MMTDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADALAAELNALRPGSAAALQADLLDPD
ALPELVAACVAAFGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRGAIVN
ITDIHAERPLKGYPVYCAAKAALEMLTRSLALELAPEVRVNAVAPGAILWPEDGNSFDEEARQAILARTP
LKRIGTPEDIAEAVRFLLADASFITGQILAVDGGRSLTL
>gnl|CDD|236390 PRK09136, PRK09136, S-methyl-5'-thioinosine phosphorylase
MLAIIGGTGLTQLAGLDIVQRQVVRTPYGAPSGPLTFGTLAGREVVFLARHGHGHTIPPHKVNYRANIWA
LKQAGATRVLAVNTVGGIHADMGPGTLVVPDQIIDYTWGRKSTFFEGDGEEVTHIDFTHPYSPMLRQRLL
AAARAAGVSLVDGGVYAATQGPRLETAAEIARLERDGCDLVGMTGMPEAALARELGLPYACLALVANWAA
GRGDSAEITMAEIEAALDAAMGRVRELLERLVRGD
>gnl|CDD|181670 PRK09140, PRK09140, 2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
MRLMQPFTKLPLIAILRGITPDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDRALIGAGTV
LSPEQVDRLADAGGRLIVTPNTDPEVIRRAVALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGPAG
IKALRAVLPPDVPVFAVGGVTPENLAPYLAAGAAGFGLGSALYRPGQSAEEVAERARAFVAAYREA
>gnl|CDD|236391 PRK09145, PRK09145, 3'-5' exonuclease
MMNWLRRLWWRRRLKDPRYAFLFEPPPPDEWVALDCETTGLDPRRAEIVSIAAVKIRGNRILTSERLELL
VRPPQSLSAESIKIHRLRHQDLEDGLSEEEALRQLLAFIGNRPLVGYYLEFDVAMLNRYVRPLLGIPLPN
PLIEVSALYYDKKERHLPDAYIDLRFDAILKHLDLPVLGRHDALNDAIMAALIFLRLRKGDA
>gnl|CDD|236392 PRK09146, PRK09146, DNA polymerase III subunit epsilon; Validated
MMKSKMSQPALDWPAKFAQKAEQAKDPRLKRFYAAGLVSPDTPLSEVPFVALDFETTGLDAEQDAIVSIG
LVPFTLQRIRCRQARHWVVKPRRPLEEESVVIHGITHSELQDAPDLERILDELLEALAGKVVVVHYRRIE
RDFLDQALRNRIGEGIEFPVIDTMEIEARIQRKQAGGLWNRLKGKKPESIRLADSRLRYGLPAYSPHHAL
TDAIATAELLQAQIAHHFSPDTPISKLWL
>gnl|CDD|236393 PRK09147, PRK09147, succinyldiaminopimelate transaminase; Provisional
MNPRLDRLQPYPFEKLRALFAGVTPPADLPPISLSIGEPKHPTPAFIKDALAANLDGLASYPTTAGLPAL
REAIAAWLERRYGLPALDPATQVLPVNGSREALFAFAQTVIDRDGPGPLVVCPNPFYQIYEGAALLAGAE
PYFLNCDPANNFAPDFDAVPAEVWARTQLLFVCSPGNPTGAVLPLDDWKKLFALSDRYGFVIASDECYSE
IYFDEAAPPLGLLEAAAELGRDDFKRLVVFHSLSKRSNVPGLRSGFVAGDAALLKKFLLYRTYHGCAMPP
AVQAASIAAWNDEAHVRENRALYREKFDAVTPILAPVLDVQLPDAGFYLWAKVPGDDTEFARRLYADYNV
TVLPGSYLAREAHGVNPGAGRVRIALVAPLAECVEAAERIVDFCRS
>gnl|CDD|181674 PRK09148, PRK09148, LL-diaminopimelate aminotransferase
MEEFHRIRRLPPYVFEQVNRLKAAARAAGADIIDLGMGNPDLPTPQHIVDKLCETAQDPRTHRYSASKGI
PGLRRAQAAYYARRFGVKLNPDTQVVATLGSKEGFANMAQAITAPGDVILCPNPSYPIHAFGFIMAGGVI
RSVPAEPDEEFFPALERAVRHSIPKPIALIVNYPSNPTAYVADLDFYKDVVAFAKKHDIIILSDLAYSEI
YFDGNPPPSVLQVPGAKDVTVEFTSMSKTFSMAGWRMGFAVGNERLIAALTRVKSYLDYGAFTPIQVAAT
AALNGPQDCIAEMRELYKKRRDVLVESFGRAGWDIPPPAASMFAWAPIPEAFRHLGSLEFSKLLVEKADV
AVAPGVGFGEHGDGYVRIALVENEQRIRQAARNIKRFLSSADETLHNVVPLAAAR
>gnl|CDD|181675 PRK09162, PRK09162, hypoxanthine-guanine phosphoribosyltransferase; Provisional
MSLEEIRQVLAEADCLVSAAEVEAAIDRMADEITADLADENPLVLCVMGGGLVFTGQLLPRLDFPLEFDY
LHATRYRNETTGGELVWKVKPRESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDR
KAKPLKADFVGLEVPDRYVFGYGMDYKGYWRNLPGIYAVKG
>gnl|CDD|181676 PRK09165, PRK09165, replicative DNA helicase; Provisional
MADNLVLDLAPDAAEPEIRELPHNIEAEQALLGAILINNRALDRVSDFLKPEHFFEPLHQRIYEAIAKII
RKGKLATPVTLKTFLENDEALGELGGVQYLAKLATEAVTIINARDYGRIIYDLALRRELINIGEDVVNNA
YDAPVDVAPQEQIEDAEQKLYELAETGRYEGGFQSFGTAITEAVDMANAAFKRDGHLSGISTGLRDLDSK
LGGLHPSDLIILAGRPSMGKTALATNIAFNAAKAYRREAQPDGSKKAVNGGVVGFFSLEMSAEQLATRIL
SEQSEISSSKIRRGKISEEDFEKLVDASQELQKLPLYIDDTPALSISQLRARARRLKRQHGLDLLVVDYL
QLIRGSSKRSSDNRVQEISEITQGLKALAKELNIPVIALSQLSRQVEQRDDKRPQLSDLRESGSIEQDAD
VVMFVYREEYYLKRKEPREGTPKHEEWQEKMEKVHNKAEVIIAKQRHGPTGTVKLAFESEFTRFGDLADR
SQLPEEY
>gnl|CDD|236394 PRK09169, PRK09169, hypothetical protein; Validated
RGPAHAPHKRRRDAAAPADPRPRRRPRLGDAPAPRTARADSGATPRGRPRAGADREPTSEQLRDYERWLD
RAAAGQLDAQREQQCARLWFLVQQARARKVDPDFCLDLARDNVLAQRNGYGLAQLAHLGNKLSKYPDRPA
CMAAIAWIAGQLLDALREALDAISFALLLNALSKWPDNTDCQTAAEQLADRLASDSRLLQAMDAQEVANA
LNALSKWPDSPRCRNAAERLAERLADEPGLLQSLRAQEVALLLNALSKWPDDEACRQAAEALAARLAREP
GLRLALDPQGVANALNALSKWPDTEACRQAAEALAERLAQERGLLQAMNAQAVANALNALSKWPDEEACR
AAAEALAARLARDAGLRRALNAQELANALNALSKWPDEEACRAAAEALAARLARDAGLRAALNAQGVANA
LNALSKWPGAEACRQAALALAARLAADARLRNALSAQELANALNALSKWPDEAACRRAAEALAARLAGDA
ELRQALDAQGLANALNALSKWPDSDACRAAAEALADRLAQDPALLQAMDAQGLANTLNALSKWPEEPDCR
AAAEALAARLARRPDLRSALNAQGLANLLNALSKWPDEDACRAAAEALAGRLARDAGLLDAFNAQDLANL
LNGLSKWPDEDDCRQAAEALAARLLRDAGLPRAFDAQGLANALNALSKWPDEAACRAAALALAERLAREA
GLRQAFDAQGVANALNALSKWPEEEACRAAAEALAGRLAADADLRQAMNPQGLANSLNALSKWPQEPACQ
QAALLLAERLGSAGLPFRTFTMAGLAQLANAMARLILKLEDQDDEEDLALARARLRELAAHLDLRPERLE
QADARDIAVLFKALASARLKDGLRLLARPGLNRLATLHRATGFREDNLETLGNLCAGLLPLARSPELKAH
RADALRLLERLQPIVARKIELYLRAHLAAAAPAALRIERGGEAFGTRRPALTFYQLLKAYAVVARQWKRR
YVEGDRQRVRQRREALKAWVKETLERTRGAIEADLDEMSWNLIAQIEAGDDVLDALDLRLQKDLDKITAA
HPPTRFDVAAVRREMRTLPGVPRPPASGAGATTLQVVDMQGRELRGNRDEAEKPYSFFTRLTGGALPLVE
VQLPGKLSAFMLARTFQYQGEPWRMDLFGGSRLTPGRTRVFELLLAGAAKRYGRLPAIRYADTAPGSALM
QLIRKLAPQREDWYRMQRALLEMVPRDHVVEGPLRLGLLPDRVPGPAHPFKLRGPDGEPIALCPNDGCGF
IKESLAMRIPAVRQAMEAWQAVRAGRATEAQQQLAFPEQRMSSLPPQALQHYPRDEAVLEEAREALRRRL
QSLAALWATDPADGPRRLDTLKLYELLTGGGIEGVQGRAVPSADDKLHLPTEKSQVFDRTGGPVLLGKPP
YDKENLLPVPAERVGTAAQGDATARFLDTCFAIQYSYTGFDDSGSESGDDAPMLHSKGMLIVVPDAMWPA
DHNDADLVCSTEDLKVHSSWTQGRDRDRLPARMDSTGSLRVKDIFAPGRLGALPIPELRKRDMDTDGDDV
FVYAGYPKLAAHIRRFMEDRERRRGKLRSFKPPKTATPAFDEQGRYQAGRAAEILSAQRGQELVGRASTL
QFRFLAQPDALREAMAERAMFGTYEGTERELRRGLRRLLEGEAEAPQALQELRERARLGIARAHHPVARE
AAELLHAQLEALAAAPANTPSPAAPPPALSAALAQRFPPLAEAYAQAGTPRARLAALVDHYPVARLPHPD
EQFPEGQPGYVPGAPEETLRNLLTLGVKVGTDAPKSDTGTDLFLKIAERLERALRSFPDRIRSVPYTKST
ARELRDGRFDAEAALARLEDNPTLAAGVMEMALEELQQHGLLDGPPAPGARARAVTEEDIRQLARTLHAR
ARQAEARITPMLRAAIEGIGGQLRGLAHRLKSEGSLFEKLRGLMAKKHLTPEEAAALVNDALRYSVVLPP
QTFVAGYRRILGALDEQGHTRTRVTNHFKKRGPAFKGINVTLDATGEGVRLEIQFHTPQTFDLKERFHDL
YKQAQALQLQGASSEQQRALLAPARDAFRAVPTPPGCEEIDDWEAEPPSTARPRAPAAAAPAAGAPRSPA
LAELVERLGAQARRIEREVGPLLQALLQKLAGGLRVDKPHSVRKIAKKIGKKIARIQALRGLSPEQAAAR
VRDALRWEVVLPAEGFGAAVEQARQALGAKGLRVMRINNGFAAPDTTYAGLNVNLRTAAGLDFEIQFHTA
DSLRTKNKTHKLYEKLQDLEVAPARERDPAKRLALQQANARLLQGLRDAAATVPRPEGIETIASFDRYRD
APASGT
>gnl|CDD|169691 PRK09173, PRK09173, F0F1 ATP synthase subunit B; Validated
MDATFWAFVGLVLFLALVVYLKVPGMIARSLDARADRIKNELAEARRLREEAQQLLAEYQRKRKEAEKEA
ADIVAAAEREAEALTAEAKRKTEEYVARRNKLAEQKIAQAETDAINAVRSSAVDLAIAAAEKLLAEKVDA
KAASELFKDALAQVKTRLN
>gnl|CDD|169692 PRK09174, PRK09174, F0F1 ATP synthase subunit B
MFVTPAYAQEATQPGTTAHEAPAAGAVHTETGVAHEAEHGSGVFPPFDSTHYASQLLWLAITFGLFYLFM
SRVILPRIGGIIETRRDRIAQDLDQAARLKQEADAAVAAYEQELAQARAKAHSIAQAAREAAKAKAEAER
AAIEASLEKKLKEAEARIAAIKAKAMADVGSIAEETAAAIVEQLIGGTADKASVAAAVKAARAS
>gnl|CDD|236395 PRK09177, PRK09177, xanthine-guanine phosphoribosyltransferase; Validated
MSLMSKKFPVSWDQLHRDARALAWRLLPAGQWKGIIAVTRGGLVPAAILARELGIRLVDTVCISSYDHDN
QGELKVLKRAEGDGEGFLVVDDLVDTGGTARAVREMYPKAHFATVYAKPAGRPLVDTYVTDVPQDTWIEF
PWDMGLTFVPPLADGK
>gnl|CDD|236396 PRK09181, PRK09181, aspartate kinase; Validated
MMMHTVEKIGGTSMSAFDAVLDNIILRPRKGEDLYNRIFVVSAYGGVTDALLEHKKTGEPGVYALFAKAN
DEAWREALEAVEQRMLAINAELFADGLDLARADKFIRERIEEARACLIDLQRLCAYGHFSLDEHLLTVRE
MLASIGEAHSAFNTALLLQNRGVNARFVDLTGWDDDDPLTLDERIKKAFKDIDVTKELPIVTGYAKCKEG
LMRTFDRGYSEMTFSRIAVLTGADEAIIHKEYHLSSADPKLVGEDKVVPIGRTNYDVADQLANLGMEAIH
PKAAKGLRQAGIPLRIKNTFEPEHPGTLITKDYVSEQPRVEIIAGSDKVFALEVFDQDMVGEDGYDLEIL
EILTRHKVSYISKATNANTITHYLWGSLKTLKRVIAELEKRYPNAEVTVRKVAIVSAIGSNIAVPGVLAK
AVQALAEAGINVLALHQSMRQVNMQFVVDEDDYEKAICALHEALVENHNHGAAIA
>gnl|CDD|236397 PRK09182, PRK09182, DNA polymerase III subunit epsilon; Validated
TDLEEMAKALEASGRYRVLRRLVPRPIYPAPRGEFVRLGVILDTETTGLDPRKDEIIEIGMVAFEYDDDG
RIGDVLDTFGGLQQPSRPIPPEITRLTGITDEMVAGQTIDPAAVDALIAPADLIIAHNAGFDRPFLERFS
PVFATKPWACSVSEIDWSARGFEGTKLGYLAGQAGFFHEGHRAVDDCQALLELLARPLPETGQPPLAELL
EASRRSRVRIWAENSPFEMKDHLKARGYRWSDGSDGRPKSWWIEVGEDDLEAELAFLRTEIYRWREADPP
IQRLTAFDRFSDRG
>gnl|CDD|181681 PRK09183, PRK09183, transposase/IS protein; Provisional
MMELQHQRLMALCGQLQLESLISAAPALAQQAVDQEWSYMDFLEHLLHEEKLARHQRKQAMYTRMAAFPA
VKTFEEYDFTFATGAPQKQLQSLRSLSFIERNENIVLLGPSGVGKTHLAIALGYEAVRAGIKVRFTTAAD
LLLQLSTAQRQGRYKTTLQRGVMAPRLLIIDEIGYLPFSQEEANLFFQVIAKRYEKGSMILTSNLPFGQW
DQTFAGDAALTSAMLDRLLHHSHVVQIKGESYRLKQKRKAGVIAEANPE
>gnl|CDD|181682 PRK09184, PRK09184, acyl carrier protein; Provisional
MSSMTALERELAELIVEELNLEDVQPESIDADAPLYGEGLGLDSIDILEIALVISKRYGFQLRSDNPDNQ
RIFASLRALAAYVAAHRTK
>gnl|CDD|236398 PRK09185, PRK09185, beta-ketoacyl-ACP synthase
MTPVYISAFGATSALGRGLDAILAALRAGRASGMRPCDFWLVDLPTWVGEVVGVELPALPAALAAFDCRN
NRLALLALQQIEPAVEAAIARYGADRIGVVLGTSTSGILEGELAYRRRDPAHGALPADYHYAQQELGSLA
DFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNGFNSLESLSPQPCR
PFSANRDGINIGEAAAFFLLEREDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADI
GYINLHGTATPLNDAMESRAVAAVFGDGVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQ
PDPALPPLYLVENAQALAIRYVLSNSFAFGGNNCSLIFGRAD
>gnl|CDD|236399 PRK09186, PRK09186, flagellin modification protein A; Provisional
MLKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSLVELDITDQESL
EEFLSKSAEKYGKIDGAVNCAYPRNKDYGKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNL
VNISSIYGVVAPKFEIYEGTSMTSPVEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGILDNQPEAFL
NAYKKCCNGKGMLDPDDICGTLVFLLSDQSKYITGQNIIVDDGFSL
>gnl|CDD|236400 PRK09188, PRK09188, serine/threonine protein kinase; Provisional
NPNIDVPLPGDQIPALSARFVETAVLKRDVFSTVERGYFAGDPGTARAVRRRVSEVPWWSKPLARHLAAR
EIRALKTVRGIGVVPQLLATGKDGLVRGWTEGVPLHLARPHGDPAWFRSAHRALRDLHRAGITHNDLAKP
QNWLMGPDGEAAVIDFQLASVFRRRGALYRIAAYEDLRHLLKHKRTYAPDALTPRERKILARKSLPSRIW
LATGKKVYNFITRGLFSWSDGEGTGDRIDNEAPAIQAALKSDPAVSDVAIALFSLPAKGVGLYAFVEAEL
PADEKSLRARLAGAKPPKPPEHIQPVAALPRDADGTVRDDILRLIAMNQIDELDDLLREPEIRGLVEAIA
AHRLNLTDRRVTQAE
>gnl|CDD|169701 PRK09189, PRK09189, uroporphyrinogen-III synthase; Validated
MRVLVTRPEPAAERTAARLRAMGHEPVLLPLSRPVHDVAAAFTALSEPHGAIAVTSAEAVRHLAALGERL
LPHLALPLFAVGEATAEAARELGFRHVIEGGGDGVRLAETVAAALAPTARLLYLAGRPRAPVFEDRLAAA
GIPFRVAECYDMLPVMYSPATLSAILGGAPFDAVLLYSRVAARRFFALMRLSIAPPADEKTRFLCLSARV
AAALPASLRAQALIAAMPDEKSLLSLLSKL
>gnl|CDD|236401 PRK09190, PRK09190, RNA-binding protein
DPADLDGGPRDRRGNERRCIVTREVGPPDELIRFVVGPDGQVVPDLKRKLPGRGCWVSADRAAVEKAVAK
KLFARAAKADVKVPPDLADLVEALLARRALDALGLARKAGQVVSGFEKVDAALRSGEAAALIHASDGAAD
GKRKLDQARRALVHETGREIPVIGLFTAAELGLAFGRENVIHAALLAGGAAERVVKRAQRLAGYRGGDPG
RAAGGAAETA
>gnl|CDD|236402 PRK09191, PRK09191, two-component response regulator; Provisional
MSLSQRIAPHLPYLRRYARALTGSQSSGDAYVAATLEALLADPSIFPEASSPRVGLYRLFHRLWSSAGAN
DPEPGSPFEARAERRLAGLTPLPRQAFLLTALEGFSVEEAAEILGVDPAEAEALLDDARAEIARQVATRV
LIIEDEPIIAMDLEQLVESLGHRVTGIARTRAEAVALAKKTRPGLILADIQLADGSSGIDAVNDILKTFD
VPVIFITAFPERLLTGERPEPAFLITKPFQPDTVKAAISQALFFQETERLA
>gnl|CDD|236403 PRK09192, PRK09192, fatty acyl-AMP ligase
DVTMSPTPTTSSLPRRYADFPTLVEALDYAALGEAGMNFYDRRGQLEEALPYQTLRARAEAGARRLLALG
LKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYIAQLRGMLASAQPAAIITPDELLP
WVNEATHGNPLLHVLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISH
DGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLQWLDLISRNRGTISYSPPFG
YELCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEATLAVSFSP
LGSGIVVEEVDRDRLEYQGKAVAPGAETRRVRTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPS
LMSGYFRDEESQDVLAADGWLDTGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGD
AAAFSIAQENGEKIVLLVQCRISDEERRGQLIHALAALVRSEFGVEAAVELVPPHSLPRTSSGKLSRAKA
KKRYLSGAFASLDVAASLA
>gnl|CDD|236404 PRK09193, PRK09193, indolepyruvate ferredoxin oxidoreductase; Validated
PLPASLRMALADVTLDDKYTLERGRVFLTGTQALVRLPLLQRERDRAAGLNTAGFVSGYRGSPLGGLDQE
LWRAKKHLAAHDIVFQPGLNEDLAATAVWGSQQVNLFPGAKYDGVFGMWYGKGPGVDRSGDVFRHANAAG
TSPHGGVLALAGDDHAAKSSTLPHQSEHAFKAAGMPVLFPANVQEILDYGLHGWAMSRYSGLWVGMKTVT
DVVESSASVDVDPDRVQIVLPEDFEMPPGGLNIRWPDPPLEQEARLLDYKLYAALAYARANKLDRVVIDS
PNARLGIVAAGKAYLDVRQALRDLGLDEETAARLGIRLYKVGMVWPLEPQGVRAFAEGLDEILVVEEKRQ
IIEYQLKEELYNWPDDVRPRVIGKFDPQGNWLLPAHGELSPAIIAKAIARRLLKLELPGDVRARIAARLA
VLEAKEAALALPRVTAARTPYFCSGCPHNTSTRVPEGSRALAGIGCHYMATWMDRNTSTFTQMGGEGVPW
IGQAPFTDEKHVFQNLGDGTYFHSGLLAIRAAVAAGVNITYKILYNDAVAMTGGQPVDGGLSVPQITRQL
AAEGVKRIVVVTDEPEKYDGVARLAPGVTVHHRDELDAVQRELREIPGVTVLIYDQTCAAEKRRRRKRGT
LPDPAKRVFINEAVCEGCGDCSVKSNCLSVEPVETEFGRKRRIDQSSCNKDFSCLKGFCPSFVTVEGGKL
RKPAAAAADAAALPPLPEPALPALDGPYNILVTGVGGTGVVTIGALLGMAAHLEGKGVSVLDMTGLAQKG
GAVVSHVRIAARPEDIHATRIAAGEADLVIGCDLVVAAGPEALSRMRPGRTRAVVNTHETPTADFVRNPD
WRFPGAALEAALRAAVGGDRVDFIDATRLATALLGDSIYTNMFLLGYAWQKGLLPLSAAAIERAIELNGV
AVEMNLAAFRWGRRAAHDPAAVAALAAAAPPAPAPPSLDELIARRVAFLTAYQNAAYAARYRALVERVRA
AERALGPGSEALTEAVARNLFKLMAYKDEYEVARLYTDPAFLAKLAAQFEGDYKLTFHLAPPLLAKKDPR
GRPRKRAFGPWMMPAFRLLAKLKGLRGTALDPFGYTEERRTERALIAEYEALVDELLARLTADNLALAVE
LASLPDEIRGYGHVKEANVAAARARWAELLAQLRAPEAAQARAAA
>gnl|CDD|236405 PRK09194, PRK09194, prolyl-tRNA synthetase; Provisional
MRTSQLFLPTLKETPADAEVISHQLLLRAGYIRKLASGIYTYLPLGLRVLRKIENIVREEMNKIGAQEVL
MPALQPAELWQESGRWEEYGPELLRLKDRHGRDFVLGPTHEEVITDLVRNEIKSYKQLPLNLYQIQTKFR
DEIRPRFGLMRGREFIMKDAYSFHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEF
MVLADSGEDTIVYSDESDYAANIEKAEALPPPRAAAEEALEKVDTPNAKTIEELAEFLNVPAEKTVKTLL
VKADGELVAVLVRGDHELNEVKLENLLGAAPLELATEEEIRAALGAVPGFLGPVGLPKDVPIIADRSVAD
MSNFVVGANEDDYHYVGVNWGRDFPVPEVADLRNVVEGDPSPDGGGTLKIARGIEVGHIFQLGTKYSEAM
NATVLDENGKAQPLIMGCYGIGVSRLVAAAIEQNHDEKGIIWPKAIAPFDVHIVPVNMKDEEVKELAEKL
YAELQAAGIEVLLDDRKERPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFL
KALKK
>gnl|CDD|181690 PRK09195, gatY, tagatose-bisphosphate aldolase; Reviewed
MYLVSTKQMLNNAQRGGYAVPAFNIHNLETMQVVVETAAELHSPVIIAGTPGTFSYAGTEYLLAIVSAAA
KQYHHPLALHLDHHEKFDDIAQKVRSGVRSVMIDGSHLPFAQNISLVKEVVDFCHRFDVSVEAELGRLGG
QEDDLQVDEADALYTDPAQAREFVEATGIDSLAVAIGTAHGMYKGEPKLDFDRLENIRQWVNIPLVLHGA
SGLPTKDIQQTIKLGICKVNVATELKIAFSQALKNYLTEHPEANDPRHYLQPAKSAMKDVVSKVIADCGC
EGKA
>gnl|CDD|181691 PRK09196, PRK09196, fructose-bisphosphate aldolase class II
MALISLRQLLDHAAEHGYGVPAFNVNNLEQVQAIMEAADETDSPVILQASAGARKYAGEPFLRHLILAAV
EEYPHIPVVMHQDHGNSPATCQRAIQLGFTSVMMDGSLKADGKTPASYEYNVDVTRKVVEMAHACGVSVE
GELGCLGSLETGMGGEEDGHGAEGKLSHDQLLTDPEEAADFVKKTQVDALAIAIGTSHGAYKFTRKPTGD
VLAIDRIKEIHARLPNTHLVMHGSSSVPQELLDIINEYGGDMPETYGVPVEEIQEGIKHGVRKVNIDTDL
RLAMTGAIRRFLAENPSEFDPRKYLKPAMEAMKKICKARYEAFGTAGQASKIKPISLEEMAKRYASG
>gnl|CDD|236406 PRK09197, PRK09197, fructose-bisphosphate aldolase; Provisional
PGVATGEDYQEMFDRAKENGFALPAVNVVGTDSINAVLEGAAEAKSPVIIQFSNGGAAFIAGKGVKDDGQ
GAAVLGAIAGAKHVHEVAEHYGVPVILHTDHCAKKLLPWIDGLLDAGEKHFAAGGKPLFSSHMIDLSEEP
LEENIEICSKYLERMAKAGMTLEIELGVTGGEEDGVDNSHEDNSKLYTQPEDVLYAYEALGKISGRFTIA
ASFGNVHGVYKPGNVKLRPEILKDSQEYVSKKFGLPAKPFDFVFHGGSGSTLEEIREAVSYGVVKMNIDT
DTQWAFWRGVLDYYFKNYDYLQGQVGNPEGEDKPNKKYYDPRVWLRAAEASMAARLEEAFEDLNSIGVLL
>gnl|CDD|236407 PRK09198, PRK09198, putative nicotinate phosphoribosyltransferase; Provisional
MMMLLNPILNTDSYKASHRLQYPPGTTYLYSYLESRSGGRYDKVVFFGLQYFLKEYLIQPITEAFIDEAK
ALLVAHGLPFNRAGWRRIVDKYGGYLPLRIKAVPEGSVVPVHNVLMTIENTDPEFFWLPNYLETLLLRNV
WYPSTVATISWEYKQLIRQYLEKTADDLDFLPFQLHDFGARGMSSLESAALGGAAHLVSFLGTDTIPALL
YAERYYNADMAGFSIPATEHSVMTSWGREGELEAYRNMIEQFYPGGIVSIVSDSYDLWNAITEPWGGELK
DEILARGGTLVIRPDSGDPVTIICGTLELLDEIFGGTVNSKGYKVLNPHVGVIQGDGITLDSIEAILEAL
KAKGFAAENIVFGMGGALLQYVNRDTQGFAMKASAIEVNGEWRDIFKDPITDQGKKSKKGRLKLIKDNGE
YRTVDLDEAGDENDDLLQTVFENGKLLVEYSLAEIRARLHAAR
>gnl|CDD|236408 PRK09200, PRK09200, preprotein translocase subunit SecA; Reviewed
MKKKLLGDIDKRRLKKYRKIVKQINKLEGKMSSLSDEELRQKTIEFKERLASGKTLDDILPEAFAVVREA
AKRVLGMRPYDVQLIGALVLHEGNIAEMQTGEGKTLTATMPLYLNALEGKGVHLITVNDYLAKRDAEEMG
QVYEFLGLTVGLNFSDIDDASEKKAIYEADIIYTTNSELGFDYLRDNLADSKEDKVQRPLNYAIIDEIDS
ILLDEAQTPLIISGKPRVQSNLYHIAAKFVKTLEEDVDYEFDEEKKEVWLTDQGIEKAESYFGIDNLYSL
EHQVLYRHIILALRAHVLFKRDVDYIVYDGEIVLVDRFTGRVLPGRKLQDGLHQAIEAKEGVEITEENRT
MASITIQNLFRMFPKLSGMTGTAKTEEKEFFEVYNMEVVQIPTNRPIIRIDYPDKVFVTLDEKYKAVIEE
VKERHETGRPVLIGTGSIEQSETFSKLLDEAGIPHNLLNAKNAAKEAQIIAEAGQKGAVTVATNMAGRGT
DIKLGEGVHELGGLAVIGTERMESRRVDLQLRGRSGRQGDPGSSQFFISLEDDLLKRFAPEELEKLKKKL
KTDAQRLTGLLFNRKVHKIVVKAQRISEGAGYSAREYALELDDVINIQRDVVYKERNRLLEEDDRDLIDI
VILMIDVYLEAVAEEYLLEKSLLEEWIYENLSFQLNEILSNTNFPDKKEVVQFLLEEAEKQLKEKRNKLP
SATLYNQFLRKVALKAIDQNWVEQVDALQQLKEGIGLRQYGQRNPIREYQKEALESFEYMYENIKKDMVR
NLLLSLLVFDKEGEIVIHFP
>gnl|CDD|236409 PRK09201, PRK09201, AtzE family amidohydrolase
MMNLSSLSAAEIAAAVRAGELSARAVAQATLARIARANPQLNAFTAVTAERALAEAARIDAARAAGEPLG
PLAGVPFAVKNLFDVAGLTTLAGSKINRDRPPATRDATAVRRLEAAGAVLVGALNMDEYAYGFTTENSHY
GATRNPHDLTRIAGGSSGGSAAAVAAGLVPFTLGSDTNGSIRVPASLCGIFGLKPTYGRLSRAGSFPFVA
SLDHIGPFARSVADLALVYDVLQGPDPQDPFQADRPAEPTAPLLDRGAEGLRIAVLGGYFAQWADPEARA
AVDRVAKALGATREVELPEAARARAAAFIITASEGGNLHLPALRTRPQDFDPASRDRLLAGAMLPAAWYV
QAQRFRRWFRQAVLELFEHVDVLIAPATPCSAPLIGQETMRIDGVELPVRANLGILTQPISFIGLPVVAV
PLRTPGGLPIGVQLIAAPWREDLALRAAAALEQQGVAAAPVPTVF
>gnl|CDD|236410 PRK09202, nusA, transcription elongation factor NusA; Validated
MNKELLEAIEAVAREKGIDREVVIEALEEALATAYKKKYGPEANIRVEIDRKTGDIEVFRRWEVVEEVED
PTKEISLEEARKIDPDAEVGDYIEEEIESVDFGRIAAQTAKQVIVQKIREAERERVYEEYKDRVGEIITG
VVKRVERGNIIVDLGRAEAILPRKEQIPRENFRPGDRVRAYVYEVRKEARGPQIILSRTHPEFLKKLFEQ
EVPEIADGLIEIKAIARDPGSRAKIAVKSNDPRIDPVGACVGMRGSRIQAISNELGGEKIDIILWSDDPA
QFIINALSPAEVSSVVVDEDEHSADVVVPDDQLSLAIGKNGQNVRLASKLTGWKIDIMTEEEASEKRQAE
FDAILDLFMEALDIDEEIAQLLVEEGFSSLEELAYVPVEELLEIEGFDEETVEELRERAKEALETEALAQ
EEKLADDLLSLEGLDRELAFKLAEKGIKTLEDLAEQAVDELIDIEGDEEK
>gnl|CDD|181699 PRK09206, PRK09206, pyruvate kinase PykF
MKKTKIVCTIGPKTESEEMLTKLLDAGMNVMRLNFSHGDYAEHGQRIKNLRNVMSKTGKKAAILLDTKGP
EIRTMKLEGGNDVSLKAGQTFTFTTDKSVVGNKERVAVTYEGFTADLSVGNTVLVDDGLIGMEVTAITGN
EVICKVLNNGDLGENKGVNLPGVSIALPALAEKDKQDLIFGCEQGVDFVAASFIRKRSDVLEIREHLKAH
GGENIQIISKIENQEGLNNFDEILEASDGIMVARGDLGVEIPVEEVIFAQKMMIEKCNRARKVVITATQM
LDSMIKNPRPTRAEAGDVANAILDGTDAVMLSGESAKGKYPLEAVSIMATICERTDRVMNSRLESNNDNR
KLRITEAVCRGAVETAEKLDAPLIVVATQGGKSARSVRKYFPDATILALTTNEKTARQLVLSKGVVPQLV
KEIASTDDFYRLGKELALQSGLAQKGDVVVMVSGALVPSGTTNTASVHVL
>gnl|CDD|181700 PRK09209, PRK09209, ribonucleoside-diphosphate reductase subunit alpha
MKEELQVTTWIVKEAGNRKLPFDKERLDRYIDQIHAEFPQLDVEDYKRRVFNFVERKESVTADDLVDYLI
REAEARVDLEEPEWTFFAARLYLNRLYKRASRNRFYDASEKYGSFVGLQESLAERGIYSNDLLKRYSKEE
LIEAGKMIDPERDKLFTYIGLYLLADRYLATDSDRNVYELPQERWLTIALYLMQNEPRERRMQLVKEAYW
ALSNLYMTVATPTLANAGKVGGQLSSCFIDTVDDSLQGIYDSNTDVARVSKHGGGVGAYLGKVRSRGSDI
RGFKGVSSGVIPWIKQLNNTAVSVDQLGQRKGAIAVYLDVWHKDIESFLDLRLNNGDERLRAHDVFTGVC
IPDLFMEAVERRGDWYLFDPHEVKKVMGWYLEDFYDEKKGDGSFREKYEECVADERLSRKTVKAIDIMKR
IMVSQLETGNPFMFYRDEVNRMNPNKHEGMIYSSNLCTEIMQNMSPTVMIQEIISGGQIVITKQPGDFVV
CNLSSINLGRAVTADVLERLIPIQVRMLDNVIDLNQLPVPQATITNQKYRAIGLGTFGWHHLLALKGIAW
ESEEAVQYADELYERINYLTIQASMELAKEKGAYPVFKGSDWQTGEYFERRGYNSPQWDELAAQVAENGV
RNAYLMAVAPNMSTAQIAGSTASIDPIYSAFYYEEKKDYRRPVTAPDLSLDTWPYYEKGAYKVDQFWSIR
QNAARQRHVDQSISFNFYVPSTIRASELLDLHMTAWKEGLKTTYYVRSTDIDIEECEWCSS
>gnl|CDD|236413 PRK09210, PRK09210, RNA polymerase sigma factor RpoD; Validated
KKTKKKETTTLEQVVKELIEKGKKRGTLTYDEIAEKLIPFELDSDQIDDLYERLEDAGISIVDEEGNPSS
AQVVEEEEEEELDNDLSVPPGVKINDPVRMYLKEIGRVPLLTAEEEIELAKRIEEGDEEAKQRLAEANLR
LVVSIAKRYVGRGMLFLDLIQEGNMGLMKAVEKFDYRKGFKFSTYATWWIRQAITRAIADQARTIRIPVH
MVETINKLIRVQRQLLQELGREPTPEEIAEEMDMPPEKVREILKIAQEPVSLETPIGEEDDSHLGDFIED
QDATSPADHAAYELLKEQLEDVLDTLTDREENVLRLRFGLDDGRTRTLEEVGKVFGVTRERIRQIEAKAL
RKLRHPSRSKQLKDFLE
>gnl|CDD|169719 PRK09212, PRK09212, pyruvate dehydrogenase subunit beta; Validated
MAQLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGA
AFAGLRPIVEFMTFNFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHI
PGLKVVAPYFAADCKGLLKTAIRDPNPVIFLENEILYGHSHEVPEEEESIPIGKAAILREGSDVTIVTFS
IQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEA
FDYLDAPVERVTGKDVPLPYAANLEKLALPSEEDIIEAVKKVCYRSI
>gnl|CDD|181704 PRK09218, PRK09218, peptide deformylase; Validated
MIKPIVKDQLFLSQKSQPATKEDLQLAQDLQDTLLANRDECVGMAANMIGVQKRIIIFSLGFVPVVMFNP
VIVSKSGPYETEEGCLSLTGERPTKRYEEITVKYLDRNWREQTQTFTGFTAQIIQHELDHCEGILI
>gnl|CDD|181705 PRK09219, PRK09219, xanthine phosphoribosyltransferase; Validated
MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAAL
ALGVPVVFAKKKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDII
EQAGAKVAGIGIVIEKSFQDGRKLLEEKGYRVESLARIASLENGKVTFV
>gnl|CDD|236415 PRK09220, PRK09220, methylthioribulose 1-phosphate dehydratase
MTLEELLQQLIAAGRWIGARGWVPATSGNMSVRLDEQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGR
KPSAETLLHTQLYRLFPEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQKAFAGQTTHETAVVVPIFDN
DQDIARLAARVAPYLDAQPLRYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRLLEAK
>gnl|CDD|181707 PRK09221, PRK09221, beta alanine--pyruvate transaminase; Provisional
MPDMAAAARTDPNDLDAHWMPFTANRQFKAAPRLLVSAEGMYYTDADGRKILDGTAGLWCCNAGHGRPEI
VEAVARQAATLDYAPAFQMGHPLAFELAERLAELAPGGLDHVFFTNSGSESVDTALKIALAYHRARGQGT
RTRLIGRERGYHGVGFGGISVGGIVNNRKMFGGLLPGVDHLPHTLDLPENAFSKGQPEHGAELADDLERL
VALHDASTIAAVIVEPMAGSAGVLVPPKGYLQRLREICDKHGILLIFDEVITGFGRLGAAFAAERFGVTP
DIITFAKGLTNGAIPMGAVIASDEIYDAFMQGPEYAIEFFHGYTYSAHPVACAAGLATLDIYREEDLFER
AAELAPYFEDAVHSLKGLPHVIDIRNIGLVAGIELAPRPGAPGARGYEAFMKCFEKGLLVRYTGDTIALS
PPLIIEKAQIDELVDALGDALRAVA
>gnl|CDD|236416 PRK09222, PRK09222, NADP-dependent isocitrate dehydrogenase
MAEKTPITVAYGDGIGPEIMEAVLKILEAAGAPLEIETIEIGEKVYKKGWTSGISPSAWESIRRTKVLLK
APITTPQGGGYKSLNVTLRKTLGLYANVRPCVSYHPFVETKHPNLDVVIIRENEEDLYAGIEHRQTPDVY
QCLKLISRPGSEKIIRYAFEYARANGRKKVTCLTKDNIMKLTDGLFHKVFDEIAKEYPDIEAEHYIVDIG
AARLATNPENFDVIVTPNLYGDILSDIAAEISGSVGLAGSANIGEEYAMFEAVHGSAPDIAGKNIANPSG
LLNAAVMMLVHIGQFDIAELIENAWLKTLEDGIHTADIYNEGVSKKKVGTKEFAEAVIENLGQKPEKLKP
ASYPLAKKPASPIDYYPRTKEKKELVGVDVFVDWDGSDANELAAKLEKLALGNLKLKMISNRGLKVWPDG
TPETFCSDHWRCRFMAKDGTEIKHADILELLLRLSEAGIDFIKTEKLYLFDGVPGFSLAQGE
>gnl|CDD|236417 PRK09224, PRK09224, threonine ammonia-lyase IlvA
MGADYLRKILTARVYDVAQETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARG
VITASAGNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGL
TFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACL
KAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCQEYVDDVITVDTDEICAAIKDVFEDTRSIAEPAGA
LALAGLKKYVAQHGIEGETLVAILSGANMNFDRLRYVAERAELGEQREALLAVTIPEEPGSFLKFCELLG
GRNVTEFNYRYADAKEAHIFVGVQLSRGQEERAEIIAQLRAHGYPVVDLSDDELAKLHVRYMVGGRPPKP
LDERLYRFEFPERPGALLKFLSTLGTHWNISLFHYRNHGADYGRVLAGFQVPDADEPEFEAFLDELGYPY
WDETDNPAYRLFLA
>gnl|CDD|236419 PRK09228, PRK09228, guanine deaminase; Provisional
MTTKAYRGRLLHFTADPAEVDDEDALRYIEDGLLLVEDGRIVAAGPYAELRAQLPADAEVTDYRGKLILP
GFIDTHIHYPQTDMIASYGEQLLDWLNTYTFPEERRFADPAYAREVAEFFLDELLRNGTTTALVFGTVHP
QSVDALFEAAEARNMRMIAGKVLMDRNAPDGLRDTAESGYDDSKALIERWHGKGRLLYAITPRFAPTSTP
EQLEAAGALAREHPDVWIQTHLSENLDEIAWVKELFPEARDYLDVYERYGLLGPRAVFAHCIHLEDRERR
RLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEAYKVQQLQGYRLSP
FQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLDPAATPLLALRTARAESLEELLFALMTLGDDRAVA
ETYVAGRPVYRRL
>gnl|CDD|236420 PRK09229, PRK09229, N-formimino-L-glutamate deiminase; Validated
SMTTLFAERALLPDGWARNVRLTVDADGRIAAVEPGAAPAGAERLAGPVLPGMPNLHSHAFQRAMAGLTE
VRGPPQDSFWSWRELMYRFALRLTPDQLEAIARQLYVEMLEAGYTSVGEFHYLHHDPDGTPYADPAEMAL
RIVAAARAAGIGLTLLPVLYAHSGFGGQPPNPGQRRFINDPDGFLRLLEALRRALAALPGARLGLAPHSL
RAVTPDQLAAVLALAAPDGPVHIHIAEQTKEVDDCLAWSGARPVEWLLDHAPVDARWCLVHATHLTDAET
ARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGIGSDSHVSIDLVEELRLLEYGQRLRDRRRNVL
AAAAQPSVGRRLFDAALAGGAQALGRAIGGLAVGARADLVVLDLDHPALAGREGDALLDRWVFAGGDAAV
RDVWVAGRWVVRDGRHRLREAIAAAFRAALAALLAA
>gnl|CDD|181713 PRK09230, PRK09230, cytosine deaminase; Provisional
SNNALMTIKNARLPGKEGLWQITIEDGKISAIEPQSEASLEAGEVLDAEGGLAIPPFIEPHIHLDTTQTA
GEPNWNQSGTLFEGIERWAERKALLTHEDVKQRAWQTLKWQIANGIQHVRTHVDVSDPTLTALKAMLEVK
EEVAPWVDLQIVAFPQEGILSYPNGEALLEEALRLGADVVGAIPHFEFTREYGVESLHKAFALAQKYDRL
IDVHCDEIDDEQSRFVETVAALAHREGMGARVTASHTTAMHSYNGAYTSRLFRLLKMSGINFVANPLVNI
HLQGRFDTYPKRRGITRVKEMLEAGINVCFGHDDVFDPWYPLGTANMLQVLHMGLHVCQLMGYGQINDGL
NLITTHSARTLNLQDYGIEVGNPANLIILPAENGFDAVRRQVPVRYSIRHGKVIAETQPAQTTIYLEQPE
AVDFKR
>gnl|CDD|236421 PRK09231, PRK09231, fumarate reductase flavoprotein subunit; Validated
QTFQADLAIIGAGGAGLRAAIAAAEANPNLKIALISKVYPMRSHTVAAEGGSAAVAQDHDSFDYHFHDTV
AGGDWLCEQDVVEYFVHHCPTEMTQLEQWGCPWSRKPDGSVNVRRFGGMKIERTWFAADKTGFHMLHTLF
QTSLKYPQIQRFDEHFVLDILVDDGHVRGLVAMNMMEGTLVQIRANAVVMATGGAGRVYRYNTNGGIVTG
DGMGMAYRHGVPLRDMEFVQYHPTGLPGSGILMTEGCRGEGGILVNKDGYRYLQDYGLGPETPLGEPKNK
YMELGPRDKVSQAFWHEWRKGNTISTPRGDVVYLDLRHLGEKKLHERLPFICELAKAYVGVDPVKEPIPV
RPTAHYTMGGIETDQNCETRIKGLFAVGECSSVGLHGANRLGSNSLAELVVFGRVAGEQAAERAATAGPG
NEAALDAQAADVEQRLKALVNQEGGENWAKIRDEMGLSMEEGCGIYRTPELMQKTIDKLAELKERFKRVR
ITDTSSVFNTDLLYTIELGYGLDVAECMAHSALARKESRGAHQRLDEGCTERDDVNFLKHTLAFYNADGT
PRIEYSDVKITKSPPAKRVYGA
>gnl|CDD|236422 PRK09234, fbiC, FO synthase; Reviewed
VVPPQSPTPTASAMRRALRRARDGVTLDVDEAAVLLTARGDDLADLCASAARVRDAGLGAAGRPGVVTYS
RKVFIPLTRLCRDRCHYCTFATVPGKLEAAYLSPDEVLDIARAGAAAGCKEALFTLGDRPEDRWPEAREW
LDERGYDSTLDYVRAMAIRVLEETGLLPHLNPGVMSWSELARLKPVAPSMGMMLETTSRRLFEEKGGPHY
GSPDKDPAVRLRVLEDAGRLSVPFTTGILIGIGETLAERAESLFAIRKLHREYGHIQEVIVQNFRAKPDT
AMAGVPDAGLEELLATIAVARLVLGPKMRIQAPPNLVSGDECAALLGAGIDDWGGVSPLTPDHVNPERPW
PQLDELAAVTAEAGFTLVERLTAYPEYVRAGEPWIDPRLRGHVAALADPETGLAREDAWPVGRPWQEPDE
GWSSGRTDLHTAIDTEGRTTDRRSDFDSAYGDWESIREQVHEGRAPERIDTDVLAALRAAERDPAGLTDD
EALALFTADGPALEAVCRLADDLRRDVVGDDVTYVVNRNINFTNICYTGCRFCAFAQRKTDADAYTLSLD
EVADRAWEAWVAGATEVCMQGGIHPELPGTGYADLVRAVKARVPSMHVHAFSPMEIVNGAARLGLSIREW
LTALREAGLDTIPGTAAEILDDEVRWVLTKGKLPTAEWIEVVTTAHEVGLRSSSTMMYGHVDTPRHWVAH
LRVLRDIQDRTGGFTEFVPLPFVHQNAPLYLAGAARPGPTHRENRAVHALARIMLHGRIDNIQTSWVKLG
VEGTRAMLRGGANDLGGTLMEETISRMAGSEHGSAKTVAELEAIAEGAGRPARQRTTLYGPVAAERLAAA
RAS
>gnl|CDD|181716 PRK09236, PRK09236, dihydroorotase; Reviewed
MKRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREPGLTH
KGDIASESRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNLDEIKRLDPK
RVCGVKVFMGASTGNMLVDNPETLERIFRDAPTLIATHCEDTPTIKANLAKYKEKYGDDIPAEMHPLIRS
AEACYKSSSLAVSLAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGNLIK
CNPAIKTASDREALRQALADDRIDVIATDHAPHTWEEKQGPYFQAPSGLPLVQHALPALLELVHEGKLSL
EKVVEKTSHAPAILFDIKERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFV
NGQLVYHNGQLVESCRGQRLEFDR
>gnl|CDD|236423 PRK09237, PRK09237, amidohydrolase/deacetylase family metallohydrolase
LLLRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVHVYPGSTPYG
DEPDEVGVRSGVTTVVDAGSAGADNFDDFRKLTIEASKTRVLAFLNISRIGLLAQDELADLEDIDADAVA
EAVKRNPDFIVGIKARMSSSVVGDNGIEPLELAKAIAAEANLPLMVHIGNPPPSLEEILELLRPGDILTH
CFNGKPNRILDEDGELRPSVLEALERGVRLDVGHGTASFSFKVAEAAIAAGILPDTISTDIYCRNRINGP
VYSLATVMSKFLALGMPLEEVIAAVTKNAADALRLPELGRLQVGSDADLTLFTLKDGPFTLTDSEGDSLI
GERLLTPLATVRGGKVVLTEQGSAEHAFDA
>gnl|CDD|236424 PRK09238, PRK09238, bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
MLEAYRKHVAERAALGIPPLPLDAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAA
IAKGEAKSPLISPEKAVELLGTMLGGYNVEPLIDLLDDAELAPEAAEALKHTLLVFDAFHDVAEKAKAGN
AYAKEVLESWADAEWFTSRPELPEKITVTVFKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPGPI
KQIEELKKKGHPVAYVGDVVGTGSSRKSATNSVLWHMGEDIPYVPNKRAGGVVLGGKIAPIFFNTMEDSG
ALPIELDVSKLNMGDVIDIYPYKGKIRNETGEVIATFKLKTDVLLDEVRAGGRIPLIIGRGLTTKAREAL
GLPPSDVFRKPKQPADSGKGFTLAQKMVGRACGVPGVRPGTYCEPKMTTVGSQDTTGPMTRDELKDLACL
GFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFIMNRGGVSLRPGDGVIHSWLNRMLLPDTVGTGGDSHTR
FPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVHAIPYYAIKQGLLTVEKKGKK
NIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLSKEPIIEYLRSNIVLLKWMIAEGYGDARTL
ERRIAAMEEWLANPELLEADADAEYAAVIEIDLAEIKEPILACPNDPDDVRLLSEVAGTKIDEVFIGSCM
TNIGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQARVAD
GATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGRIPTVEEYQEYVAEIDATADDIYRYLNF
>gnl|CDD|181719 PRK09239, PRK09239, chorismate mutase; Provisional
MSDEQARAPAELAALRQSIDNIDAALIHMLAERFKCTQAVGVLKAEHGLPPADPAREAYQIERLRQLAKD
ANLDPDFAEKFLNFIIKEVIRHHERIAAEHGDPG
>gnl|CDD|181721 PRK09242, PRK09242, SDR family oxidoreductase
TQHRWRLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFPEREVHGLAADVS
DDEDRRAILDWVEDHWDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASS
AIVNIGSVSGLTHVRSGAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYEQ
VIERTPMRRVGEPEEVAAAVAFLCMPAASYITGQCIAVDGGFLRYGF
>gnl|CDD|236426 PRK09243, PRK09243, nicotinate phosphoribosyltransferase; Validated
MLMYNDDSLALLTDLYELTMAQAYLRDGIHNRRAVFELFFRKLPFGRGYAVFAGLERLLEYLENLRFTEE
DIEYLRSLGIFDEDFLDYLRNFRFTGDVRAVPEGELVFPNEPLLRVEGPLAEAQLLETLLLNIINFQTLI
ATKAARIVSAAGGRPLLEFGSRRAQGPDAAVWAARAAYIGGFDATSNVLAGKRYGIPVSGTMAHSFVQAF
DDEYEAFRAYAETYPDNTVLLVDTYDTLKSGVPNAIKVAKELGDGIELGGVRIDSGDLAYLSKKVRKMLD
EAGFTDTKIVASNDLDEYTIASLKLQGAPIDGFGVGTKLVTGSDAPALGGVYKLVAIEGEGGMIPKIKLS
NSPEKVTTPGRKQVYRIYDKGGKAEADVITLADEEEEEPLKMFHPVHTYKSKTVKNFDAEPLLVPVMENG
KRVYELPSLEEIRAYAAAQLASLPEEYKRLLNPHAYPVDLSQAL
>gnl|CDD|181723 PRK09245, PRK09245, crotonase/enoyl-CoA hydratase family protein
MTDFLLVERDGHIVTLTMNRPETRNALSDNDAVDALVAACAAINADRSVRAVILTGAGTAFSSGGNVKDM
RARVGAFGGSPADIRQGYRHGIQRIPLALYNLEVPVIAAVNGPAIGAGCDLACMCDIRIASETARFAESF
VKLGLIPGDGGAWLLPRIIGMARAAEMAFTGDAIDAATALEWGLVSRVVPADQLLPAARALAERIAANPP
HALRLTKRLLREGQHASLDTLLELSAAYQALAHHTADHREAVDAFLEKRPPVFTGR
>gnl|CDD|236428 PRK09247, PRK09247, ATP-dependent DNA ligase; Validated
MKAFAELLDRLDLTTSTNAKLALLADYFRSAPDPDRAWALALLTGGLPRRLVKTRLLRELAAERADLPPW
LFEESYDYVGDLAETIALLLPAPSDEASDLPLAPWLEEVLLPLRGLGREELRAALADLWDRLDEDGRFAL
NKLITGGFRVGVSARLVTRALAELGGVDEARIAQRLMGLWPPYADLFAWLIGPEEDPLPADPGQPYPFFL
AHPLEDEDLTLGDPADWQAEWKWDGIRVQLVRRGGEVRLWSRGEELITERFPELAEAAEALPDGTVLDGE
LLVWRPEDGRPQPFADLQQRIGRKTVGKKLLADYPAFLRAYDLLEDGGEDLRALPLAERRARLEALIARL
PDPRLDLSPLVPFSDWDELAALRAAARERGVEGLMLKRRDSPYLVGRKKGPWWKWKRDPLTIDAVLMYAQ
RGHGRRASLYTDYTFGVWDGPEGGRQLVPFAKAYSGLTDEEIKQLDRWVRKNTVERFGPVRSVRPELVFE
IAFEGIQRSKRHKSGIAVRFPRILRWRWDKPAREADTLETLQALLDAES
>gnl|CDD|236429 PRK09248, PRK09248, putative hydrolase; Validated
MKYPVDTHTHTIASGHAYSTLHENAAEAKQKGLKLFAITDHGPDMPGAPHYWHFGNLRVLPRKVDGVGIL
RGIEANIKNYDGEIDLPGDMLKKLDIVIAGFHEPVFAPGDKETNTQALINAIKNGRVDIIGHPGNPKYPI
DIEAVVKAAKEHNVALEINNSSFGHSRKGSEDNCRAIAALCKKAGVWVALGSDAHIAFDIGNFEEALKIL
DEVGFPEERILNVSPRRLLDFLESRGKAPIPEFADL
>gnl|CDD|236431 PRK09250, PRK09250, class I fructose-bisphosphate aldolase
MTDIAMLLGKDADSLLSHRCKIPKDQLHLPGPDFVDRVMIYSDRNPGVLRNLQRLLNHGRLAGTGYLSIL
PVDQGFEHSAGASFAPNPLYFDPENIVKLAIEAGCNAVASTLGVLEAVARKYAHKIPFILKLNHNELLSY
PNTYDQALTASVEDALRLGAVAVGATIYFGSEESRRQIEEISEAFEEAHELGLATVLWSYLRNSAFKKDG
DYHTAADLTGQANHLAATIGADIIKQKLPTNNGGYKAINFGKTDDRVYSKLTSDHPIDLVRYQVANCYMG
RRGLINSGGASKGEDDLLDAVRTAVINKRAGGMGLIIGRKAFQRPMAEGVKLLNAIQDVYLDKKITIA
>gnl|CDD|181730 PRK09256, PRK09256, aminoacyl-tRNA hydrolase
MLRITRRLVIPENELEWRFIRASGPGGQNVNKVSTAVELRFDIAASSLPEFYKERLLALAGHRITKDGVI
VIKAQEFRSQERNREDALERLVALIREALKPPKKRRATKPTRGSKERRLESKKQRGEVKALRGKVRDD
>gnl|CDD|181731 PRK09257, PRK09257, aromatic amino acid transaminase
MFEHLEAAPADPILGLMEAFRADPRPDKVNLGVGVYKDEQGRTPVLRAVKKAEARLLETETTKNYLPIEG
LAAYRQAVQELLFGADSPALAAGRVATVQTPGGTGALRVGADFLKRAFPDAKVWVSDPTWPNHRAIFEAA
GLEVKTYPYYDAATKGLDFDAMLADLSQAPAGDVVLLHGCCHNPTGADLTPEQWDELAELLKERGLIPFL
DIAYQGFGDGLEEDAYGLRAFAAAGLELLVASSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKATIR
TNYSNPPAHGAAIVATILNDPELRAEWEAELEEMRERIKAMRQLLVEALKAKGPSRDFDFIARQRGMFSY
SGLTPEQVDRLREEFGVYAVGSGRINVAGLNESNIDYVAEAIAAVL
>gnl|CDD|181732 PRK09258, PRK09258, 3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
MKYSNVAILSLAYELAPVVVTSSEIEERLAPLYERLRLPPGQLEALTGIRERRWWPEGTQLSDGAIAAGR
KALAEAGIDPSDIGLLINTSVCRDYLEPATACRVHHNLGLPKSCANFDVSNACLGFLNGMLDAANMIELG
QIDYALVVSGESAREIVEATIDRLLAPETTREDFAQSFATLTLGSGAAAAVLTRGSLHPRGHRLLGGVTR
AATEHHELCQGGRDGMRTDAVGLLKEGVELAVDTWEAFLAQLGWAVEQVDRVICHQVGAAHTRAILKALG
IDPEKVFTTFPTLGNMGPASLPITLAMAAEEGFLKPGDRVALLGIGSGLNCSMLEVKW
>gnl|CDD|236433 PRK09259, PRK09259, putative oxalyl-CoA decarboxylase; Validated
TAMSDQLQLTDGFHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLT
QKPGVCLTVSAPGFLNGLTALANATTNCFPMIMISGSSEREIVDLQQGDYEELDQLNAAKPFCKAAFRVN
RAEDIGIGVARAIRTAVSGRPGGVYLDLPAKVLAQTMDADEALTSLVKVVDPAPAQLPAPEAVDRALDLL
KKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSLALANADVVLLVG
ARLNWLLSHGKGKTWGADKKFIQIDIEPQEIDSNRPIAAPVVGDIGSVMQALLAGLKQNTFKAPAEWLDA
LAERKEKNAAKMAEKLSTDTQPMNFYNALGAIRDVLKENPDIYLVNEGANTLDLARNIIDMYKPRHRLDC
GTWGVMGIGMGYAIAAAVETGKPVVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNNGGIYRGDDVNLSG
AGDPSPTVLVHHARYDKMMEAFGGVGYNVTTPDELRHALTEAIASGKPTLINVVIDPAAGTESGHITNLN
PKSVAGKKK
>gnl|CDD|236434 PRK09260, PRK09260, 3-hydroxyacyl-CoA dehydrogenase
IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQGVARGKLTEAARQAALARLS
YSLDLKAAVADADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHF
FNPVHKMKLVELIRGLETSDETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATA
EDIDKAIRLGLNFPMGPLELGDLVGLDTRLNNLKYLHETLGEKYRPAPLLEKYVKAGRLGRKTGRGVYDY
TNRENVPG
>gnl|CDD|236435 PRK09261, PRK09261, phospho-2-dehydro-3-deoxyheptonate aldolase; Validated
MMYQTDDLRIKEIKPLIPPAELKEELPLTEEAAETVARSRKEIHNILHGKDDRLLVVVGPCSIHDPKAAL
EYARRLAKLREELKDKLEIVMRVYFEKPRTTVGWKGLINDPDLDGSFDINDGLRIARKLLLDINELGLPA
ATEFLDPITPQYIADLISWGAIGARTTESQVHRELASGLSCPVGFKNGTDGNIKVAIDAIIAASAPHHFL
GITKDGRSAIVSTTGNPDCHVILRGGNKGPNYDAESVAEAKERLEKAGLPPRIMIDCSHANSGKDHKRQP
EVARDVAAQIAAGNKAIIGVMIESHLVEGNQDLPPKLVYGQSITDACIGWEDTEALLRELAEAVRARRR
>gnl|CDD|181735 PRK09262, PRK09262, hypothetical protein; Provisional
MLGVVVRNIERADAAVVDRLAEFGVATVHEAQGRVGLLKPYMRPIYQGARIAGTAVTVLVQPGDNWMMHV
AVEQCQPGDVLVVAPTSPCTDGFFGDLLATSLQARGVRGLVIDAGVRDVRTLTEMGFPVWSRAISAQGTV
KATLGSVNVPVVCAGALVNPGDVVVADDDGVVVVPRAQAAAVADAAEAREANEESKRERLAAGELGLDIY
KMRERLAKKGLRYVD
>gnl|CDD|236436 PRK09263, PRK09263, anaerobic ribonucleoside triphosphate reductase; Provisional
MMPKVIKRDGRKVPFDSEKIKNAIEKAAKAVEVDDEDYCATVAAEIASRVEGRDEVDIEEIQDAVENQLM
AGPYKALARAYIEYRHDRDIAREKATDLNEEIRGLIEQSNEAVLNENANKDSKVFSTQRDLLAGIVSKHY
ALRHLLPRDVVNAHEKGDIHYHDLDYSPFFPMFNCCLIDLKGMLTNGFKIGNAEIESPKSIQTATAVTAQ
IIAQVASSQYGGCTINRIDEVLAPYAEKSYEKHLKDAEEWVIEEKAEAYARARTEKEIYDAMQSLEYEIN
TLHTSNGQTPFVTLGFGLGTSWESRLIQKAILRNRIAGLGKERKTAIFPKLVFAIKDGLNLKPGDPNYDI
KQLALECATKRMYPDILNYDKIVELTGSFKTPMGCRSFLQGWKDENGEEVHDGRNNLGVVTLNLPRIALE
AKGDEDKFWEILDERLELAKKALMTRIERLKGAKPRVAPILYMYGAFGVRLKADDDVDELFKNGRATISL
GYIGLYETINALYGGSWEVNPEAKAFALAIVKRMKDACDQWKKETGYGFSLYSTPSESLTDRFCRLDTEK
FGVIPGITDKGYYTNSFHYDVRKKVNPFEKLDFEKPYPPLASGGFIHYCEYPNLQHNLKALEAVWDYSYD
RVGYLGTNTPIDECYECGFTGEFECTEKGFTCPKCGNHDPKTVSVTRRTCGYLGNPDARPFNHGRQEEIK
RRVKHMSGGQI
>gnl|CDD|236437 PRK09264, PRK09264, diaminobutyrate--2-oxoglutarate transaminase
SMDMDIFERLESEVRSYCRSFPVVFDKAKGSWLYDEDGKEYIDFFAGAGALNYGHNNPVLKQALIDYLQR
DGITHGLDMHTTAKREFLETFEETILKPRGLDYKVQFTGPTGTNAVEAALKLARKVTGRTNIVAFTNGFH
GMTLGSLAVTGNSHKRQGAGVPLNNVTRMPYDGYFGGDVDTLAYLEKLLEDSSSGVDLPAAVIVETVQGE
GGINVASAEWLQRLAKLCRKHDILLIVDDIQAGCGRTGTFFSFERAGITPDIVTLSKSISGYGLPMALVL
IKPELDVWKPGEHNGTFRGNNLAFVTATAALEEYWSDDAFEKEVKAKGELVRERLEEIAAKYPGLGAEVR
GRGMMQGIDFGDGELAGKIAAEAFENGLIIETSGPEDEVVKLLPPLTIDEEELEEGLDILEEAVAEVLAE
EESKA
>gnl|CDD|181738 PRK09265, PRK09265, aminotransferase AlaT; Validated
MKPIEKSSKLENVCYDIRGPVLKEAKRLEEEGHKILKLNIGNPAPFGFEAPDEILRDVIRNLPTAQGYSD
SKGLFSARKAIMQYYQQKGIPDVDVDDIYIGNGVSELIVMAMQALLNNGDEVLVPAPDYPLWTAAVSLSG
GKPVHYLCDEEAGWFPDLDDIRSKITPRTKAIVIINPNNPTGAVYSKELLEEIVEIARQHNLIIFADEIY
DKILYDGAVHISIASLAPDLLCVTFNGLSKAYRVAGFRVGWMVLSGPKKHAKGYIEGLDMLASMRLCANV
PAQHAIQTALGGYQSINELILPGGRLYEQRDRAWELLNAIPGVSCVKPKGALYAFPKLDPKVYPIHDDEQ
FVLDLLLQEKVLLVQGTGFNWPEPDHFRIVTLPRVDDLEEAIGRIGRFLSGYRQ
>gnl|CDD|236438 PRK09266, PRK09266, hypothetical protein; Provisional
TMPLIELNGRPATAEDLAALALANYGHFTSMQVRDGRVRGLDLHLQRLRRASRELFGAALDDDRVRAQLR
AALAAGPADASVRVTVFAPDFDFRNPLADVAPDVLVATSPPADGPAGPLRLQSVPYERELPHIKHVGTFG
QLHLRRLAQRAGFDDALFVDPDGRVSEGATWNLGFWDGGAVVWPQAPALPGVTMALLQRGLERLGIPQRT
RPVTLADLGRFAGAFACNAWRGQRAVSAIDDVALPDSHALLELLRRAYEAEPWQAI
>gnl|CDD|236439 PRK09267, PRK09267, flavodoxin FldA; Validated
MAKIGIFFGSDTGNTEDIAKMIQKKLGKDVADVVDIAKASKEDFEAYDLLILGIPTWGYGELQCDWDDFL
PELEEIDFSGKKVALFGLGDQEDYAEYFCDAMGTLYDIVEPRGATIVGHWPTDGYTFEASKAVDDGKFVG
LALDEDNQSELTDERIEAWVKQIKPEFGL
>gnl|CDD|236440 PRK09268, PRK09268, acetyl-CoA C-acetyltransferase
MTMPTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNL
TRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLRKILLE
LNRAKTTGDRLKALGKLRPKHLAPEIPRNGEPRTGLSMGEHAAITAKEWGISREAQDELAAASHQNLAAA
YDRGFFDDLITPFLGLTRDNNLRPDSSLEKLAKLKPVFGKGGRATMTAGNSTPLTDGASVVLLASEEWAA
EHGLPVLAYLVDAETAAVDFVHGKEGLLMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWE
DEEYCRERLGLDAPLGSIDRSKLNVNGSSLAAGHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQG
VTAILER
>gnl|CDD|236441 PRK09269, PRK09269, chorismate mutase; Provisional
MKQLLRASLAAAALLALLLLLGPPAAAAGDDSALTPLVDLAAQRLALADPVALSKWDSGKPIEDPPREAQ
VLANVEAQAPAHGVDPDYVRRFFRDQIEANKLVQYALLARWRLAGAAPPGPRPDLASIRPRLDRLQQELL
DALADVAPLRSAPDCPARLARAVANVARLRRLDSLHRQALDRATGDYCHAGGA
>gnl|CDD|236442 PRK09270, PRK09270, nucleoside triphosphate hydrolase domain-containing protein; Reviewed
LKVQAQYRDEEIEAVHKPLLRRLAALQAEPQRRTIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQVPM
DGFHLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDDEVYWPVFDRSLEDPVADAIVVPPTARLV
IVEGNYLLLDEEPWRRLAGLFDFTIFLDAPAEVLRERLVARKLAGGLSPEAAEAFVLRNDGPNARLVLET
SRPADLVLEMTATGEYRLV
>gnl|CDD|181744 PRK09271, PRK09271, flavodoxin; Provisional
MRILLAYASLSGNTREVAREIEERCEEAGHEVDWVETDVQTLAEYPLDPEDYDLYLLGTWTDNAGRTPPE
MKRFIAELAETIGKPPNVAVFGTGETQWGEEYYCGAVHRMARFFGSSYPRLKIEQMPHGERDAAAIDNWT
DKVLALCKNDPDADHYRHVA
>gnl|CDD|181745 PRK09272, PRK09272, hypothetical protein; Provisional
MFLIVKYLISALIIVAITEIAKRSPTLGGLIAALPLVSLLSLIWLYVEGQDDEKLSNFAWGVFWGVPPTL
PMFLIVPLLLKRGFGFWLSLLAGIGVTAVLFLLQALLLK
>gnl|CDD|181746 PRK09273, PRK09273, hypothetical protein; Provisional
MKIALINENSQAAKNAIIYEALKKVADPKGHEVFNYGMYDEEDHQLTYVQNGIMASILLNSKAVDFVVTG
CGTGQGAMLALNSFPGVVCGYCIDPTDAYLFAQINNGNALSLPFAKGFGWGAELNLRYIFEKLFTGERGE
GYPKERAEPQQRNAGILNEVKAATYKDLLDILKAIDQDLLKTAISGERFQEYFFENCQDKEIAAYVKSVL
A
>gnl|CDD|236443 PRK09274, PRK09274, peptide synthase; Provisional
MMASMANIARHLPRAAQERPDQLAVAVPGGRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAV
LMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKAHLARRLFGWGKPSVRRL
VTVGGRLLWGGTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDY
GIEPGEIDLPTFPLFALFGPALGMTSVIPDMDPTRPATVDPAKLFAAIERYGVTNLFGSPALLERLGRYG
EANGIKLPSLRRVISAGAPVPIAVIERFRAMLPPDAEILTPYGATEALPISSIESREILFATRAATDNGA
GICVGRPVDGVEVRIIAISDAPIPEWDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDV
WHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPGAQRPVLCVEL
EPGVACSKSALYQELRALAAAHPHTAGIERFLIHPSFPVDIRHNAKIFREKLAVWAAKQLKG
>gnl|CDD|236444 PRK09275, PRK09275, bifunctional aspartate transaminase/aspartate 4-decarboxylase
EDEKKLEKLSPFELKDELIKLAKSKSARLMLNAGRGNPNWLATTPREAFFRLGQFAVEESRRSWSYPGGL
GGMPQKEGIEERFEAFLEEHKDVPGIDFLRDAVSYVRDQLGFDADEFVYELVDGIIGDNYPVPDRMLKHT
EKIVKDYLRQEMCGGRPPKGEFDLFAVEGGTAAMCYIFDSLKENGLLKAGDKIALMTPIFTPYLEIPELP
RYDLEVVHINADEENEWQYPDSELEKLRDPSIKALFLVNPSNPPSVAMSDESLEKIADIVNEKRPDLMII
TDDVYGTFVDDFRSLFAVLPYNTILVYSFSKYFGATGWRLGVIALHEDNVFDKLIAKLPEEKKKELDKRY
SSLTTDPEKLKFIDRLVADSRQVALNHTAGLSTPQQVQMALFSLFALLDEEDAYKKAMKDIIRRRYKALY
EGLGLPEPEDPNNAAYYTLIDLEEWAEKNYGKEFADYLKKNYSPVDLLFRLAEETGVVLLPGGGFGGPEW
SVRVSLANLNEEDYAKIGKAIRKLLDEYYEEYKKSKK
>gnl|CDD|181749 PRK09276, PRK09276, LL-diaminopimelate aminotransferase; Provisional
MMKLADRIKNLPPYLFAEIDKKKAEKIARGVDVISLGIGDPDLPTPDHIIEAMCKAVEDPENHQYPSYEG
MLEFRKAVADWYKRRFGVELDPETEVISLIGSKEGIAHIPLAFVNPGDVVLVPDPGYPVYKIGTIFAGGE
PYFMPLKEENGFLPDLDAIPEDVAKKAKLMFINYPNNPTGAVADLEFFEEVVDFAKKYDIIVCHDAAYSE
IAYDGYKPPSFLEVPGAKDVGIEFHSLSKTYNMTGWRIGFAVGNADLIAGLGKVKSNVDSGVFQAIQEAG
IAALNGPQEVVEELRKIYQERRDILVEGLRKLGLEVEPPKATFYVWAPVPKGYTSAEFATLLLDKAGVVV
TPGNGFGEYGEGYFRIALTVPDERIEEAVERIKKL
>gnl|CDD|236445 PRK09277, PRK09277, aconitate hydratase AcnA
MSSTDSFKARKTLEVGGKSYDYYSLRALEAKGLGDISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEW
LPKAKPDREIPFRPARVVMQDFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTP
DAFEKNVELEFERNEERYQFLKWGQKAFDNFRVVPPGTGICHQVNLEYLAPVVWTREDGELVAYPDTLVG
TDSHTTMINGLGVLGWGVGGIEAEAAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGV
VGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEEQVALVEAYAKAQGLW
RDPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSAELGVQGFGLDEAEEGEDYELPDG
AVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLEKAGLLPYLEALGFN
LVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVVAYALAGTVD
IDLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWD
PDSTYIRNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFN
SYGSRRGNHEVMMRGTFANIRIRNEMVPGVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGT
GSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLEDLKPG
ATVTVVITRADGEVVEFPVLCRIDTAVEVDYYRNGGILQYVLRDLLAS
>gnl|CDD|236448 PRK09281, PRK09281, F0F1 ATP synthase subunit alpha; Validated
MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDN
VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRK
SVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVR
KLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRP
PGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFN
AGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGQRLVELL
KQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKDLSDEIEAKLK
AAIEEFKKTFAA
>gnl|CDD|236449 PRK09282, PRK09282, pyruvate carboxylase subunit B; Validated
MKKVKITDTTLRDAHQSLLATRMRTEDMLPIAEKLDKVGFWSLEVWGGATFDVCIRYLNEDPWERLRKLK
KALPNTPLQMLLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQ
GTISYTTSPVHTIEKYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEVDLPVQLHSHCTSGL
APMTYLKAVEAGVDIIDTAISPLAFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQF
ESEFTIVDTRVLIHQVPGGMISNLVSQLKEQNALDKLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVL
NVLTGERYKVITKEVKDYVKGLYGRPPAPINEELRKKIIGDEEPITCRPADLLEPELEKARKEAEELGKS
EKEDVLTYALFPQIAKKFLEEREAGELKPEPEPKEAAAAGAEGIPTEFKVEVDGEKYEVKIEGVKAEGKR
PFYLRVDGMPEEVVVEPLKEIVVGGRPRASAPGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMEN
EIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP
>gnl|CDD|236450 PRK09283, PRK09283, porphobilinogen synthase
MMFPFTRPRRLRKTAALRRLVRETRLTPNDLIYPLFVVEGENEREEIPSMPGVYRLSIDLLVKEAEEAVE
LGIPAVALFGVPELKDEDGSEAYNPDGLVQRAIRAIKKAFPELGVITDVCLDEYTSHGHCGILEDGYVDN
DETLELLAKQALSQAEAGADIVAPSDMMDGRVGAIREALDEAGFTDVPIMSYSAKYASAFYGPFRDAAGS
APQFGDRKTYQMDPANRREALREVALDIEEGADMVMVKPALPYLDIIRRVKDEFNLPVAAYQVSGEYAMI
KAAAQNGWIDEERVVLESLLSIKRAGADGILTYFAKDAARWLR
>gnl|CDD|236451 PRK09284, PRK09284, thiamine biosynthesis protein ThiC; Provisional
REQRASAQAFIDTLVTGPFPGSRKIYVEGSRPDIRVPMREIHLSDTPTGGGEPNPPVPVYDTSGPYTDPD
AKIDLRKGLPKLREPWIEERGDTEELEGRSVKSSDYRLADAGLDHLRFGLLRRPRRAKAGKNVTQMHYAR
QGIITPEMEYVAIRENMGREEVLRRQHPGESFGAAIPEEITPEFVRDEVAAGRAIIPANINHPESEPMII
GRNFLVKINANIGNSAVTSSIEEEVEKMVWATRWGADTVMDLSTGKNIHETREWILRNSPVPIGTVPIYQ
ALEKVNGVAEDLTWEIFRDTLIEQAEQGVDYFTIHAGVLLRYVPLTAKRVTGIVSRGGSIMAKWCLAHHK
ENFLYTHFEEICEIMAAYDVSFSLGDGLRPGSIADANDEAQFAELETLGELTKIAWEHDVQVMIEGPGHV
PMHLIKENMDKQLEHCHEAPFYTLGPLTTDIAPGYDHITSAIGAAMIGWFGTAMLCYVTPKEHLGLPNKD
DVKEGVITYKIAAHAADLAKGHPGAQIRDNALSKARFEFRWEDQFNLSLDPDTARAFHDETLPAESAKVA
HFCSMCGPKFCSMKISQEVRDYAAEEAGMAEKSEEFRASGGELYLPV
>gnl|CDD|236452 PRK09285, PRK09285, adenylosuccinate lyase; Provisional
MELSALTALSPLDGRYASKTAALRPIFSEFGLIRYRVQVEVEWLIALAAHPGIPEVPPFSAEANAFLRAI
VENFSEEDAARIKEIERTTNHDVKAVEYFLKEKLAGLPELEAVSEFIHFACTSEDINNLSHALMLKEARE
EVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAVEILGKINGA
VGNYNAHLAAYPEVDWHAFSREFVESLGLTWNPYTTQIEPHDYIAELFDAVARFNTILIDLDRDVWGYIS
LGYFKQKTKAGEIGSSTMPHKVNPIDFENSEGNLGLANALLEHLAAKLPISRWQRDLTDSTVLRNLGVAF
GYSLIAYDSLLKGLGKLEVNEARLAEDLDANWEVLAEPIQTVMRRYGIENPYEKLKELTRGKRITAEALR
EFIDGLDLPEEAKARLKALTPANYIGLAAELADEIK
>gnl|CDD|236453 PRK09287, PRK09287, NADP-dependent phosphogluconate dehydrogenase
MGKNLALNIASHGYTVAVYNRTPEKTDEFLAEEGKGKKIVPAYTLEEFVASLEKPRKILLMVKAGAPVDA
VIEQLLPLLEKGDIIIDGGNSNYKDTIRREKELAEKGIHFIGMGVSGGEEGALHGPSIMPGGQKEAYELV
APILEKIAAKVEDGEPCVTYIGPDGAGHYVKMVHNGIEYGDMQLIAEAYDLLKDGLGLSAEEIADVFAEW
NKGELNSYLIEITADILRQKDEETGKPLVDVILDKAGQKGTGKWTSQSALDLGVPLTLITEAVFARYLSS
LKDQRVAASKVLSGPAAKFEGDKAEFIEDVRQALYASKIVSYAQGFALLRAASEEYGWDLDLGEIARIWR
GGCIIRAQFLQKITDAYEANPDLANLLLDPYFKDILEEYQDALRRVVALAVQAGIPVPAFSSALSYYDSY
RTARLPANLIQAQRDYFGAHTYERTDKEGFFHTEWSEDG
>gnl|CDD|236454 PRK09288, purT, formate-dependent phosphoribosylglycinamide formyltransferase
MTRLGTPLSPSATRVMLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSHVIDMLDGDALRAV
IEREKPDYIVPEIEAIATDALVELEKEGFNVVPTARATRLTMNREGIRRLAAEELGLPTSPYRFADSLEE
LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSPEDIEKAWEYAQEGGRGGAGRVIVEEFIDFDYEITLLTVR
AVDGGTHFCAPIGHRQEDGDYRESWQPQPMSPAALEEAQEIAKKVTDALGGRGLFGVELFVKGDEVYFSE
VSPRPHDTGMVTLISQNLSEFELHARAILGLPIPDIRLYSPAASAVILAEGESANPSFDGLAEALAVPGT
DVRLFGKPEIRGGRRMGVALATGEDVEEAREKAKEAASKVKVVGG
>gnl|CDD|236455 PRK09289, PRK09289, riboflavin synthase
MFTGIVEEVGTVESIEPKGDGLRLTIEAGKLLSDLKLGDSIAVNGVCLTVTEIDGDSFTVDVSPETLRRT
NLGDLKVGDRVNLERALRLGDRLGGHIVSGHVDGTGEIVSIEKEGNSVEFRFKAPAELAKYIVEKGSIAV
DGVSLTVNEVDGDRFSVNLIPHTLENTTLGEKKVGDRVNLEIDLLAKYVERLTE
>gnl|CDD|236456 PRK09290, PRK09290, allantoate amidohydrolase; Reviewed
MLRIDAERLWARLDELAKIGATPDGGVTRLALSPEDLQARDLFAEWMEAAGLTVRVDAVGNLFGRLEGRD
PDAPAVLTGSHLDTVPNGGRFDGPLGVLAGLEAVRTLNERGIRPRRPIEVVAFTNEEGSRFGPAMLGSRV
FTGALTPEDALALRDADGVSFAEALAAIGYDGDEAVGAARARRDIKAFVELHIEQGPVLEAEGLPIGVVT
GIVGQRRYRVTFTGEANHAGTTPMALRRDALLAAAEIILAVERIAAAHGPDLVATVGRLEVKPNSVNVIP
GEVTFTLDIRHPDDAVLDALVAELRAAAEAIAARRGVEVEIELISRRPPVPFDPGLVAALEEAAERLGLS
YRRLPSGAGHDAQILAAVVPTAMIFVPSVGGISHNPAEFTSPEDCAAGANVLLHALLELAEEG
>gnl|CDD|181762 PRK09291, PRK09291, SDR family oxidoreductase
MSKTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRGLALRVEKLDLTDAIDRAQAA
EWDVDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGP
FTGAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTGFNDTMAETPKRWYDPARNFTDPEDLAFPL
EQFDPQEMIDAMVEVIPADTGLFRNLLPAAIEDMVKDEQAHAWTRRQ
>gnl|CDD|236457 PRK09292, PRK09292, Na(+)-translocating NADH-quinone reductase subunit D; Validated
MADSKSLKKVLLGPLFDNNPIALQVLGICSALAVTTKLETALVMTLAVTFVTAFSNFFISLIRNHIPNSV
RIIVQMTIIASLVIVVDQVLKAYAYDISKQLSVFVGLIITNCIVMGRAEAFAMKNPPIPSFLDGIGNGLG
YGAILLIVAFFRELFGSGTLFGFTVLPTVQNGGWYQPNGLMLLPPSAFFLIGLLIWVIRTWKPEQVEKK
>gnl|CDD|236458 PRK09293, PRK09293, class 1 fructose-bisphosphatase
SMKTLGEFLVEQQREFPHATGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFA
NEILIEALKARGHVAGLASEEEDEIVPIPENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPVGTPTE
EDFLQPGNNQVAAGYVLYGPSTMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHW
EPGVKKYIELLAGKDGPRGRPYNMRYIGSMVADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLV
EQAGGAASDGKQRILDIEPESLHQRVPLFLGSKEEVERVEEYHAEAP
>gnl|CDD|181765 PRK09294, PRK09294, phthiocerol/phthiodiolone dimycocerosyl transferase
MFPGSVIRKLAPSEEVFARYEAFTGYTAHLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGWELVAD
DLLHPGIVVVDGDAARPLPELQLDQGVSLLALDVVPDDGGARVTLYIHHSIADAHHSASLLDELWSRYTD
VVTTGDPGPIRPQPAPQSLEAVLAQRGIRRQALSGAERFMPAMYAYELPPTPTAAVLAKPGLPQAVPVTR
CRLSKAQTSSLAAFGRRHRLTVNALVSAAILLAEWQLRRTPHVPLPYVYPVDLRFRLTPPVAATEGTNLL
GAATYLAEIGPDTDIVDLARAIAATLRADLADGVIQQSFLHFGTAFEGTPPGLPPVVFITNLGVAPPMRT
PPGLELEDIHSQFYCAISVPIGGYSCGVFAGRLLIEHHGHIAAPGKSLEAIRELLCTVPSEYGWIM
>gnl|CDD|181766 PRK09295, PRK09295, cysteine desulfurase SufS
MTFSVEKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKME
NVRKQAALFINARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAE
LRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPV
DVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQEMPPWEGGGSMIATVSLTEGTTWAKAPWRFEAGTPN
TGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESVPDLTLYGPQNRLGVIAFNLGKHHAYDVGSF
LDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQRIHRLLG
>gnl|CDD|181767 PRK09296, PRK09296, cysteine desulfuration protein SufE
MALLPDKEKLLRNFSRCANWEEKYLYIIELGQRLPPLTDEDRSPQNLIQGCQSQVWIVMRQNAQGIIELQ
GDSDAAIVKGLIAVVFILYQQMTPQDIVNFDVRPWFEKLALTQHLTPSRSQGLEAMIRAIRAKAAALS
>gnl|CDD|236460 PRK09300, PRK09300, tRNA splicing endonuclease; Reviewed
MKGELEGGVVFVGKDARSRLYDSRGYGRPKGDGLELAPVEAAYLLFRGKIEIVDGLGFRDLFARASLRPN
FELRYLVYKDLRERGYYVQPGDADFRVYPRGSGPGDGESKYRVRVVSERDPLPFSDLIERKQLVLAVVDE
ESEITYYEVKRIDPKGRMEEDPPDKVSGTLLGDRVVVWDPPGELYERGFYGKPLDGRRLQLSLVEAAYLL
ERGVLSVEILDADEFVERAREVEGEFDRKLAVYRDLRERGFVPKTGFKFGSDFRVYEGVESVEKLPHSEY
LVRVIPDDHEFSPRDLSRAVRLAHSVRKKMVFALIDDGGIRYLSIERLKP
>gnl|CDD|181770 PRK09301, PRK09301, circadian clock protein KaiB; Provisional
MSPRKTYILKLYVAGNTPNSVRALKTLKNILETEFKGVYALKVIDVLKNPQLAEEDKILATPTLAKILPP
PVRKIIGDLSDREKVLIGLDLLYEELSEEELES
>gnl|CDD|236461 PRK09302, PRK09302, circadian clock protein KaiC; Reviewed
MNQPSASPGIEKLPTGIEGFDDITHGGLPKGRPTLVSGTAGTGKTLFALQFLVNGIKRFDEPGVFVTFEE
SPEDIIRNVASFGWDLQKLIDEGKLFILDASPDPSEQEEAGEYDLEALFIRIEYAIDKIGAKRVVLDSIE
ALFSGFSNEAVVRRELRRLFAWLKQKGVTAVITGERGDEYGPLTRYGVEEFVSDCVIILRNRLEGEKRTR
TLRILKYRGTTHGKNEYPFTITEDGISVLPLTAMRLTQRSSNERISSGVPDLDEMLGGGFFRGSIILVSG
ATGTGKTLLASKFAEAACRRGERCLLFAFEESRAQLIRNARSWGIDLEKMEEKGLLKIICARPESYGLED
HLIIIKREIEEFKPSRVAIDPLSALARGGSLNEFRQFVIRLTDYLKSEEITGLFTNLTPDFMGSHSITES
HISSLTDTWILLQYVEINGEMNRALYVLKMRGSWHSNQIREFVITDKGIHIKDPFRGFEGILSGSPRRAQ
EAEERRELSRRFEEVERKQ
>gnl|CDD|236462 PRK09303, PRK09303, histidine kinase
MMQMSLSPQNSRQPLQLLLFADRRPLSREDIQRIIAYLESLDCGFPISLQIIDPGEQPELLELFRLVATP
ALIKISPEPRQVLAGSNIFQQLKNWWPRWQQEGATYSGLGENLQPSEIDSGRYSQELLQLSDELFVLRQE
NETLLEQLKFKDRVLAMLAHDLRTPLTAASLALETLELGQIDEDTELKPALIEQLQDQARRQLEEIERLI
TDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPSVYADQERIRQVLLNL
LDNAIKYTPEGGTITLSMLHRTTQKVQVSICDTGPGIPEEEQERIFEDRVRLPRDEGTEGYGIGLSVCRR
IVRVHYGQIWVDSEPGQGSCFHFTLPVYRG
>gnl|CDD|236463 PRK09304, PRK09304, arginine exporter ArgO
MLSYYFQGFALGAAMILPLGPQNAFVMNQGIRRQYHLMIALLCALSDLVLICAGIFGGSALLMQSPWLLA
LVTWGGVAFLLWYGFGAFKTAMSSNIELASAEVMKQGRWKIIATMLAVTWLNPHVYLDTFVVLGSLGGQL
DVEPKRWFALGTISASFLWFFGLALLAAWLAPRLRTAKAQRIINLFVGCVMWFIALQLARQGIAHAQ
>gnl|CDD|137204 PRK09310, aroDE, bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
MLCATISGPSFLEAKQQILRSLKLVDCIELRVDLLLSLSDLELKKLIELAPIPILTWKKHESCSQAAWID
KMQSLAKLNPNYLDIDKDFPKEALIRIRKLHPKIKIILSYHTSEHEDIIQLYNEMLASAADYYKIAVSSS
SSTDLLNIIHQKRSLPENTTVLCMGGMGRPSRILSPLLQNAFNYAAGIGAPPVAPGQLSLEHLLFYNYAN
LSAQSPIYGLIGDPVDRSISHLSHNPLFSQLSLNCPYIKLPLTPQELPKFFSTIRDLPFLGLSVTMPLKT
AVLDFLDKLDPSVKLCGSCNTLVFRNGKIEGYNTDGEGLFSLLKQKNIPLNNQHVAIVGAGGAAKAIATT
LARAGAELLIFNRTKAHAEALASRCQGKAFPLESLPELHRIDIIINCLPPSVTIPKAFPPCVVDINTLPK
HSPYTQYARSQGSSIIYGYEMFAEQALLQFRLWFPTLLFKHLEKTFRRRVANLASLF
>gnl|CDD|181774 PRK09311, PRK09311, bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II
MTMFDSIEEAIADIAAGKAVIVVDDEDRENEGDLIFAAEKATPELVAFMVRHTSGYVCVPLTEEDADRLD
LPPMVAHNQDSHGTAFTVSVDAANGVTTGISAADRATTIRLLADPASKPADFTRPGHVFPLRAKPGGVLR
RAGHTEAAVDLARLAGLQPAGVICEIVNEDGTMARVPELRVFADEHDLALITIADLIAYRRRHEKLVERE
VEARLPTRFGEFRAIGYTSILDGKEHVALVKGDIGDGEDVLVRVHSECLTGDVFGSRRCDCGPQLDAALA
QIAEEGRGVVLYMRGQEGRGIGLLHKLRAYQLQDEGYDTVDANLKLGFPADARDYGIGAQILVDLGVRSM
RLLTNNPRKIAGLQGYGLHVTERVPLPVRANEENERYLRTKRDRMGHDLDLL
>gnl|CDD|181775 PRK09314, PRK09314, bifunctional 3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II
MPIKRVEEAIEDIKNGKMLIMVDDEDRENEGDLVYAAIFSTPEKVNFMATHARGLICVSLTKELAKKLEL
PPMVSKNTSNHETAFTVSIDAKEATTGISAFERDMTIKLLADDTSKPSDFVRPGHIFPLIAKDGGVLVRT
GHTEGSVDLCKLAGLKPVAVICEIMKEDGTMARRDDLEDFAKKHNLKMIYVSDLVEYRLKNESLIKEEEK
EESEFAGFKAEKYTFLDHLQNEHIAFKFGEIKLTPNVKFHKIGSDFELLTSDKFSELLKAIEYLKKNGGV
LIFLNTESKENNQVKDYGIGAQILKYLGIKDIKLLSSSEDKEYVGLSGFGLNIVETIEL
>gnl|CDD|236464 PRK09318, PRK09318, bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II
MEELREAFLEGKPVILIDRNRENEADFVYPAQIITEEVVNFFLSYGKGLLCLTADEEDLLKRGFFKLPSN
GGETNFFIPVDYGTGTGISASERALTCRKLAEGLYVHEFRYPGHVTLLGGIGFNRRRGHTEASLELSELL
GFKRYAVIVEILDEKGDSHDLDYVLKLAEKFSLPVLEIDDVWKEFVRRKQLIKVKAEAKLPTDYGEFEIV
SFENHLDGKEHVAIVKEPLGEVPLVRIHSECVTGDTLSSLRCDCGSQLANFLRMISKEGGILIYLRQEGR
GIGLSNKIKAYELQDKGLDTVEANRALGFKEDERDYAAAFQILKALGIEKVRLLTNNPRKTKALEKYGIE
VVETVPLYGEVTKYNRFYLKTKVEKLGHKLELREVNV
>gnl|CDD|236465 PRK09319, PRK09319, bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase RibB/GTP cyclohydrolase II RibA
FKIEFDSIDDALAAIRNGECVVVVDDENRENEGDLICAAQFATPEMINFMATEARGLICLAMTGERLDEL
DLPLMVDRNTDSNQTAFTVSIDAGPELGVSTGISAEDRARTIQVAINPDTKPEDLRRPGHIFPLRAKEGG
VLKRAGHTEAAVDLARLAGLYPAGVICEIQNPDGSMARLPELKEYAKQHGLKLISIADLISYRLQNERFV
YREAVAKLPSQFGQFQAYGYRNELDGSEHVALVKGDPANFKDEPVLVRMHSECLTGDAFGSLRCDCRMQL
EAALKMIENEGEGVVVYLRQEGRGIGLINKLKAYSLQDGGLDTVEANERLGFPADLRNYGVGAQILNDLG
IKRLRLITNNPRKIAGLGGYGLEVVDRVPLLIEANDYNAEYLATKAEKLGHLLLQTYLVTIAIAWDGEPY
SVTERYELLEKLRHLARSHGLLLQEEARPRALALFDRPSLVWHLGFDQNKVASADWYKQSNHPYIKAIEL
LLDELAQWPNTKRLGFLISSGDDPALHLQVQLDRQELSLAELPSSLYSPLETQTIYSFTFSIVWS
>gnl|CDD|236466 PRK09325, PRK09325, coenzyme F420-reducing hydrogenase subunit beta; Validated
DPFGKYKEVVSARSTDKEILKKAQDGGIVTALLIYALEEGIIDGVIVAGDGEEPWKPVPKVATTPEEILE
AAGTKYTISPNVSVLKEAVREYGLDKVGIVGTPCQIQAVRKAQLYPVGMRHVPDKIALIVGIFCMENFPY
EGLKTIVEDHCGVKMEDVKKMDIGKGKFWVYTKRGDVKTIPLKETHKYEQPGCHVCTDYTAELADISTGS
VGSPDGWSTVFVRTKKGEEIFNKAVEAGLLETKPIEEVKPGLELLEKLAKEKKEKNKKEIEHRKELGLPV
PY
>gnl|CDD|181779 PRK09326, PRK09326, F420H2 dehydrogenase subunit F; Provisional
MPPKIAEVIEYDVCTACGACEAVCPIGAITVDKKAEIRDPNDLELYEKGAAPNVCEGCLTCSRICPVVDG
YIEDELANVRKFFGARSNIGGQDGGVTSAILKSLLKQGEIDCAVGITRNEKWETELVLLTSAEDVERTRG
TKYTYDSVLSALREPFEKYDRIAVIGVPCQAHGARLIRENVNDKIVLIIGLLCMESFHHDVMLDKIIPEI
MGVKIEDVVKMDFTKGKFWAYTKDGEVHSVPIKDVAKYARNPCHHCCDYTSVFADISVGSVGAPDGWNSV
LIRTDIGEKYFKMVRDELEIMEDPKPGMELVKKLINMKHKNNAEHYLEVCEKFSFETGGIR
>gnl|CDD|236467 PRK09328, PRK09328, N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
MMTIAEALREATARLASPRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYIL
GEAEFWGLDFKVSPGVLIPRPETEELVEWALEALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDI
SPEALAVARRNAKHGLGARVEFLQGDWFEPLPGGRFDLIVSNPPYIPEADIHLLQPEVRDHEPHLALFGG
EDGLDFYRRIIEQAPRYLKPGGWLLLEIGYDQGEAVRALLAAAGFADVETRKDLAGRDRVVLGRR
>gnl|CDD|236469 PRK09331, PRK09331, Sep-tRNA:Cys-tRNA synthetase; Provisional
MDINLDKYGNIELRRLEEEFINLDPIQRGGILTPEARKALIEYGDGYSVCDYCPGRLDQIKKPPIADFHE
DLAEFLGMDEARVTHGAREGKFAVMHSLCKKGDYVVLDGLAHYTSYVAAERAGLNVREVPKTGYPEYKIT
PEAYAEKIEEVKEETGKPPALALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLG
ADFIVGSGHKSMAASAPSGVLATTEEYADKVFRTSRKFGVKEVELLGCTLRGAPLVTLMASFPHVVERVK
RWDEEVKKARWFVDELEKIEGFKQLGEKPRNHDLMKFETPSFDEIAKKHKRRGFFLYEELKKRGIHGIKP
GATKEFKLSTYGLTWEQVEYVADAFKEIAEKYGLEVN
>gnl|CDD|236470 PRK09333, PRK09333, 30S ribosomal protein S19e; Provisional
MVTVYDVPADLLIERLAEYLKNVDEIKPPEWAAFVKTGVHKERPPEQEDWWYVRAASILRKVYIDGPVGV
ERLRTAYGGRKNRGVRPEHFVKGSGSIIRKILQQLEKAGLVEKTKKGRVITPKGRSLLDNLAAEVKKELA
EERPELEKYL
>gnl|CDD|181784 PRK09334, PRK09334, 30S ribosomal protein S25e; Provisional
QQKKKKKKEGSKTEKEIKSTIITLDEELLKRVAKEVKKEKIVTPYTLASKYGIKISVAKKVLRELEKRGV
LVLYSKNRRTPIYVPA
>gnl|CDD|181785 PRK09335, PRK09335, 30S ribosomal protein S26e; Provisional
MPKKRENRGRRKGDKGHVGYVQCDNCGRRVPRDKAVCVTKMYSPVDPQLAKELEKKGAIIARYPVTKCYC
VNCAVHLGIIKIRPEEERKKKAPLR
>gnl|CDD|181786 PRK09336, PRK09336, 30S ribosomal protein S30e; Provisional
MPSHGSLTKAGKVRSQTPKIPPKPKKNEVPRVRNRREYERRVLKARQQAA
>gnl|CDD|181787 PRK09343, PRK09343, prefoldin subunit beta; Provisional
MAENIPPEVQAQLAQLQQLQQQLERLLQQKSQIDLELREINKALEELEKLPDDTPIYKIVGNLLVKVDKT
KVEKELKERKELLELRSRTLEKQEKKLREKLKELQAKINEMLSKYYPQGGQ
>gnl|CDD|236471 PRK09344, PRK09344, phosphoenolpyruvate carboxykinase
MATVPQDLEAYGITNLSNVHYNLSYAELYEEALRRGEGVLTDTGALAVDTGKFTGRSPKDKFIVRDPSTE
DTIWWGDDNKPISPEKFDALKQKVLAYLSGKDLFVVDGFAGADPEYRLPVRVITELAWHALFVRNLFIRP
SEEELASFEPDFTIINAPKFKADPERDGTNSETFIAINFTERIVLIGGTDYAGEMKKSIFSVMNYLLPLK
GVLPMHCSANVGEEGDVALFFGLSGTGKTTLSADPNRKLIGDDEHGWDDGGVFNFEGGCYAKTINLSEEA
EPEIYDAIRFGAVLENVVVDEDGTVDFDDGSLTENTRAAYPIEHIPNAVKPSRAGHPKNIIFLTADAFGV
LPPVSKLTPEQAMYHFLSGYTAKVAGTERGVTEPQPTFSTCFGAPFLPLHPTVYAELLGERIKAHGAKVY
LVNTGWTGGPYGTGKRISIKYTRAIINAILDGSLDNAETTTDPIFGLAVPTSVPGVDSEILDPRNTWADK
AAYDEKAKKLARLFRENFEKFEDTVGEEIVAAGPKL
>gnl|CDD|236472 PRK09347, folE, GTP cyclohydrolase I; Provisional
NEPDKEKIEEAVREILEALGEDPDREGLLDTPKRVAKMYEELFSGYANDPKEVLNKTFEEEMGYDEMVLV
KDITFYSMCEHHLLPFIGKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGV
AVVIEAEHMCMTMRGVRKPGSKTVTSALRGLFKTDPATRAEFLSLIRH
>gnl|CDD|236473 PRK09348, glyQ, glycyl-tRNA synthetase subunit alpha; Validated
SKKMTFQDIILTLQDYWADQGCVILQPYDMEVGAGTFHPATFLRALGPEPWNAAYVQPSRRPTDGRYGEN
PNRLQHYYQFQVILKPSPDNIQELYLGSLEALGIDPLEHDIRFVEDNWESPTLGAWGLGWEVWLDGMEVT
QFTYFQQVGGIECKPVTGEITYGLERLAMYLQGVDNVYDLVWNDGVTYGDVFLQNEVEQSKYNFEHADVE
MLFKLFDDYEKEAKRLLEKGLPLPAYDYVLKASHTFNLLDARGAISVTERQRYILRIRNLARAVAEAYLE
SRE
>gnl|CDD|236474 PRK09350, PRK09350, elongation factor P--(R)-beta-lysine ligase
SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPGASQGKTLWLMTSPEYHM
KRLLAAGSGPIFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQ
AFLRYLGIDPLSADKTQLREVAAKLGLSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAA
LAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGL
PDCSGVALGVDRLIMLALGAESISEV
>gnl|CDD|236475 PRK09352, PRK09352, beta-ketoacyl-ACP synthase 3
MMYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGID
PEDIDLIIVATTTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGA
EKLSRIVDWTDRSTCVLFGDGAGAVVLGASEEPGILSTHLGSDGSYGDLLYLPGGGSRGPASPGYLRMEG
REVFKFAVRELAKVAREALEAAGLTPEDIDWLVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAAS
IPLALDEAVRDGRIKRGDLVLLEGFGGGLTWGAALVRWP
>gnl|CDD|236476 PRK09354, recA, recombinase A; Provisional
MAMDEEKQKALEAALKQIEKQFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPES
SGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVD
LIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETT
TGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTKVKVVKNKVAPPFKQAEFDIMYGEGISREGELIDLGV
ELGIIEKSGAWYSYNGEKIGQGRENAKQYLKENPELADEIEKKIREKLGLSAAAAEEEEEEDEEEEEEE
>gnl|CDD|236477 PRK09355, PRK09355, hydroxyethylthiazole kinase; Validated
QIAEALEKVREKNPLVHNITNDVVMNFTANGLLALGASPAMAHAPEEAEEMAKIAGALVINIGTLTEERI
EAMLAAGKIANEAGKPVVLDPVGVGATSYRTEFALELLAEVKPAVIRGNASEIAALAGEAAETKGVDSTD
GSADAVEIAKAAAKKYGTVVVVTGEVDYITDGERVVSVHNGHPLMTKVTGTGCLLSAVVAAFAAVEKDYL
EAAAAACAVYGIAGELAAERSEKGPGSFQPAFLDALYQLTEEDIAERAKVEEV
>gnl|CDD|236479 PRK09357, pyrC, dihydroorotase; Validated
MMILIKNGRVIDPKGLDEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHLREPGQEDK
ETIETGSRAAAAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGAITKGLAGEELTEFGAL
KEAGVVAFSDDGIPVQDARLMRRALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPAVAEE
VMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPL
RTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLL
EKMTINPARILGLPAGPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIV
YQD
>gnl|CDD|236480 PRK09358, PRK09358, adenosine deaminase; Provisional
MNLLMIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPWVRAAYDFRDLQSFLDKYDAGV
AVLQTEEDLRRLAFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLIL
CFMRHFGEEAAARELEALAARYRDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPES
IWEALDELGAERIGHGVRAIEDPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTIN
TDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFLSEEEKAALLAEVDAWLAA
>gnl|CDD|236481 PRK09360, lamB, maltoporin LamB
MMITLRKLPLAVAVAAGLLSTQAMAVDFHGYARSGIGWTGSGGEQQCFQTTGAQSKYRLGNECETYAELK
LGQELWKEGDKSFYFDSMVAYSVNQQNDWESTDPALREFNVQAKNLIEWLPGATLWAGKRFYQRHDVHMI
DFYYWDISGPGAGIENIDLGFGKLSLAWTRNTENGGSYSFASNNIYDYTNDTANDVFDVRLAGIETNPGG
SLELGVDYGRANLTDGYKLADGASKDGVMFTAEHTQSLLGGFNKFVVQYATDSMTSQGKGHSQGSSINNN
GHMLRVIDHGAISLGDKWEMMYVLMYQDIDWDNNNGTTWYSVGVRPMYKWTPIMSTLLEAGYDNVKSQRT
GDKNNQYKITLAQQWQAGDSIWSRPAIRVFATYAKWDEKTDENGNSFSRGDDDEWTFGAQMEAWW
>gnl|CDD|236482 PRK09361, radB, DNA repair and recombination protein RadB; Provisional
MDERLPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTEGLSPERFKQI
AGEDFEELLSNIIIFEPSSFEEQSEAIRKAEKLAKENVGLIVLDSATSLYRLELEDEEDNSKLNRELGRQ
LTHLLKLARKHDLAVVITNQVYSDIDSDGLRPLGGHTLEHWSKTILRLEKFRNGKRRATLEKHRSRPEGE
SAEFRITDRGIEIID
>gnl|CDD|181800 PRK09362, PRK09362, phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed
MEKKELLYEGKAKIVYSTDDPDLLIVEFKDDATAFNGEKKEQIDGKGVLNNQISSFIFKKLEEAGIPTHF
IEKLSDREQLVKKVEIIPLEVVVRNVAAGSLVKRLGIEEGTVLPPPIVEFYYKNDALGDPMINEDHILAL
GWATPEELAEIKELALKINDVLKGLFAGAGIRLVDFKLEFGRDKDGEIVLADEISPDTCRLWDKETNEKL
DKDRFRRDLGGVIEAYEEVLKRLGELLE
>gnl|CDD|236483 PRK09364, moaC, cyclic pyranopterin monophosphate synthase MoaC
MSQLTHINEQGRAKMVDVSDKAETVRTAVAEGSVRMSPETLALIRDGTAKKGDVLATARIAGIMAAKRTS
DLIPLCHPLMLTGVDVDFEWDPELPGVRITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIG
DVRLLEKSGGKSGDFKREA
>gnl|CDD|236484 PRK09367, PRK09367, histidine ammonia-lyase; Provisional
MMTITLTPGTLTLEDLRAVAREGAKVELDPSARAAIAASRAVVERIVAEGRPVYGINTGFGKLASVRIAP
EDLEQLQRNLVLSHAAGVGEPLPEEVVRLMMLLRLNSLARGHSGVRPEVIEALLALLNAGVTPVIPEKGS
VGASGDLAPLAHMALVLLGEGEAFYKGERLPAAEALAKAGLEPVTLAAKEGLALINGTQASTALALLGLF
DAEDLLAAADVAGALSVEALLGSDAPFDARIHALRGHPGQIDVAANLRALLEGSSIITSSHDCERVQDPY
SLRCQPQVHGACLDQLRYAAEVLEIEANAVTDNPLVFPDGDVISGGNFHGEPVAFAADFLAIAVAEIGSI
SERRIARLVDPALSGLPPFLVPDPGLNSGFMIAQVTAAALVSENKTLAHPASVDSIPTSANQEDHVSMGT
HAARKLREMAENLRRVLAIELLAAAQGLDFRAPLKTSPALEAAYALLREKVPFLDEDRYFAPDIEAAAEL
VASGALAAAA
>gnl|CDD|236485 PRK09368, PRK09368, gas vesicle structural protein GvpA
MTVASQPAGGGPGSGGLYDVLDLILDRGLVIDAFVRVSLVGIEILTIDARVVVASVDTYLRFAEACNRLD
LESREQSSGLPGLVGEVTESGARGKSKGALTGAAETASEALGQGRGSDEEEERRRERPRPRKAPRRRRRE
>gnl|CDD|236486 PRK09369, PRK09369, UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNG
TVTIDASNINNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEI
EHGYVEAKADGRLKGAHIVLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGA
GTDTITIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGED
GIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAEGTSVITETIFENRFMHVPELIRMGADIEVDG
HTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRGYERIEEKLRALGADIERV
>gnl|CDD|181805 PRK09371, PRK09371, gas vesicle structural protein GvpA
EKTPDSSSLAEVIDRILDKGIVVDAWVRVSLVGIELLAIEARVVVASVETYLKYAEAIGLTAQAAAPA
>gnl|CDD|236487 PRK09372, PRK09372, ribonuclease E inhibitor RraA
MEYDTSDLCDIYPDDVRVVEPLFSSFGGRSSFGGPITTVKCFEDNGLVKELLEEPGEGRVLVVDGGGSLR
RALVGDNLAELAVDNGWEGIVVYGCVRDVDELAELDIGIQALAAIPVKSDKEGIGERDVPVNFGGVTFFP
GDYLYADNDGIIVSPEPLD
>gnl|CDD|236489 PRK09375, PRK09375, quinolinate synthase NadA
PAAYPFPPLPPPLSTMEKADLKERIKRLKKERNAVILAHYYQRPEIQDLADFTGDSLELARFAAETDADT
IVFCGVHFMAETAKILSPEKTVLLPDLEAGCSLADMCPAEEFRAFKEAHPDATVVTYVNTSAAVKARADI
VCTSSNAVKIVEALPQGKKILFLPDQHLGRYVAKQTGADIILWPGHCIVHEEFTAEDLERLRAEYPDAKV
LVHPECPPEVVALADFVGSTSQIIKAAKASPAKKFIVGTEIGIVHRLQKANPDKEFIPARSCAHCPTMKM
ITLEKLLEALEEERNEITVDEEIAEKARLALERMLELSA
>gnl|CDD|236490 PRK09376, rho, transcription termination factor Rho; Provisional
MNLSELKNKSLSELLELAEELGIENASRLRKQELIFAILKAQAEKGGDIFGEGVLEILPDGFGFLRSPDA
NYLPGPDDIYVSPSQIRRFNLRTGDTVEGKIRPPKEGERYFALLKVETVNGEDPEKARNRPLFENLTPLY
PNERLRLETGNPEDLSTRIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIANSITTNHPEVHLIVLLIDER
PEEVTDMQRSVKGEVVASTFDEPAERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSG
KVLSGGVDANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLAEK
RIFPAIDINRSGTRKEELLLSPEELQKVWILRKILSPMDEVEAMEFLLDKLKKTKTNEEFFDSMNR
>gnl|CDD|181811 PRK09379, PRK09379, LytR family transcriptional regulator
MKKKILFWILGIIGVLIIGGGIYAYNVYSSVSNTLDEVHEPLKRDSEKRDEKVKISKKDPISILLMGVDE
RGGDKGRSDSLIVMTLNPKTNSMKMVSIPRDTYTEIVGKGKKDKINHAYAFGGVDMSVATVENFLDVPVD
YYIEVNMEGFKDIVDAVGGVTVNNDLEFTYDGHHFAKGNIHLNGDEALAYTRMRKEDPRGDFGRQMRQRQ
VIQGVIKKGASFSSLTNYGDVLKAIEKNVKTNLTQDQMFDIQKNYKDCRKNSEQIQIPGDGHKAADGIWY
YYVPDAAKQDLTNKLKEHLELTK
>gnl|CDD|181812 PRK09381, trxA, thioredoxin TrxA
MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPK
YGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLA
>gnl|CDD|236492 PRK09382, ispDF, bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional
TLMSDISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPE
IKFVTLVTGGATRQESVRNALEALDSEYVLIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLKRA
NETVDREGLKLIQTPQLSRTKTLKAAADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADL
LLSPSRDIRTGNGFDVHAFEEGDPVTLCGVKIPHDFGLKGHSDADVALHALTDALLGAIGAGDIGEHFPD
SDPQWKGAASKILLEHAADFVREAGGEIINADVTIIAEAPKIGPHKQAMRENLAEILGIPKDRVSVKATT
TEKLGFVGRGEGIAAIATATVKYPDWTK
>gnl|CDD|236493 PRK09389, PRK09389, (R)-citramalate synthase; Provisional
MMVRILDTTLRDGEQTPGVSLTPEEKLEIARKLDELGVDVIEAGSAITSEGEREAIKAVTDEGLNAEICS
FARAVKVDIDAALECDVDSVHLVVPTSDLHIEYKLKKTREEVLETAVEAVEYAKDHGLIVELSGEDASRA
DLDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSELVKGPVSIHCHNDFGLAVANTLAALAA
GADQVHVTINGIGERAGNASLEEVVMALKHLYDVETGIKLEELYELSRLVSRLTGIPVPPNKAIVGENAF
AHESGIHVDGLLKDTETYEPITPETVGRERRIVLGKHAGRAALKAALKEMGIEVSDDQLNEIVSRVKELG
DRGKRVTDADLLAIAEDVLGIERERKVKLDELTVVSGNKVTPTASVKLNVDGEEIVEAGTGVGPVDAAIN
AVRKALSGVADIELEEYHVDAITGGTDALVEVEVKLSRGDRVVTVRGADADIIMASVEAMMDGINRLL
>gnl|CDD|181815 PRK09390, fixJ, response regulator FixJ; Provisional
SDKGVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLK
ARGSPLPVIVMTGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAPEAAKSEAVAADIRARIA
SLSERERQVMDGLVAGLSNKVIARDLDISPRTVEVYRANVMTKMQAGSLSELVRMALRAGRG
>gnl|CDD|236494 PRK09391, fixK, transcriptional regulator FixK; Provisional
MLLQIKRQTFESNTSPPAPVARPANPFAAISGHAGLVASEFSYKKGEEIYGEGEPADYVYQVESGAVRTY
RLLSDGRRQIGAFHLPGDVFGLESGSTHRFTAEAIVDTTVRLIKRRSLEQAAATDVDVARALLSLTAGGL
RHAQDHMLLLGRKTAMERVAAFLLEMDERLGGAGMMALPMSRRDIADYLGLTIETVSRALSQLQDRGLIG
LSGARQIELRNRQALRNLDA
>gnl|CDD|181817 PRK09392, ftrB, transcriptional activator FtrB; Provisional
MRREDLIRLRNLPLFADMADATFERLMRGAFLQRFPPGTMLITEGEPADFLFVVLDGLVELSASSQDRET
TLAILRPVSTFILAAVVLDAPYLMSARTLTRSRVLMIPAELVREAMSEDPGFMRAVVFELAGCYRGLVKS
LKNQKLRSSAERLANYLLKQSLRQGGADVVTLPYEKRVLASYLGMTPENLSRAFAALASHGVHVDGSAVT
ITDPAGLARFAKPSPLIDNPEPTRPA
>gnl|CDD|181818 PRK09393, ftrA, transcriptional activator FtrA; Provisional
NTSMMTMHNHLVVALAYDGLCTFEFGCAVEIFGLPRPELGVDWYRFAVAAVEPGPLRAAGGITVVADGGL
ELLDRADTIVIPGWRGPDAPVPEPLLEALRAAHARGARLCSICSGVFVLAAAGLLDGRRATTHWRYAERL
QARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPPHRDGGQAQFVPR
PVASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLE
SSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRFGR
>gnl|CDD|236495 PRK09395, actP, cation/acetate symporter ActP
MMKRLLTALAALLPAAAAAADAISGEVEKQPTNWQAIIMFLIFVVFTLGITYWAAKRTRSASDFYTAGGG
ITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSIGFLVGWPIILFLIAERLRNLGKYTFADVASY
RLKQGPIRTLSACGSLVVVALYLIAQMVGAGKLIQLLFGLNYHVAVVLVGVLMMVYVLFGGMLATTWVQI
IKAVLLLSGATFMAFMVMKHVGFSFENLFSEAVAVHPKGLAIMGPGGLVKDPISALSLGLALMFGTAGLP
HILMRFFTVSDAKEARKSVFYATGFIGYFYILTFIIGFGAIVLVGTNPEFKDAAGALIGGNNMAAVHLAN
AVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVIKKGKATERDELRVSKITTLVLGVVAII
LGILFEKQNIAFMVGLAFAIAASANFPVLLLSMYWKGLTTRGAVIGGWLGLISAVVLMILSPTVWVDILG
HEKAIFPYEYPALFSMPLAFVGIWFFSITDNSARAKREREAFRAQFVRSQTGIGASGASAH
>gnl|CDD|236496 PRK09398, sspN, acid-soluble spore protein N; Provisional
MGNPKKNSKQFAPNHLGTQPRKAGGNKGKKMQDQSGKQPQVIQTKGE
>gnl|CDD|181821 PRK09399, sspP, small acid-soluble spore protein P
MTNKNTSKDMRKNAPKGENPGQPEPLSGSKKVKNRNHSRQKHHAHHDM
>gnl|CDD|236497 PRK09400, secE, preprotein translocase subunit SecE; Reviewed
MSSNKLQENVKNFLEDYKRVLKVARKPTREEFLLVAKVTGLGILLIGLIGFIIYLIMTLLP
>gnl|CDD|236499 PRK09404, sucA, 2-oxoglutarate dehydrogenase E1 component; Reviewed
MNSAMKAWLDSSFLFGANAAYIEELYEQYLKDPDSVDEEWRAFFDGLPGVAPDVAHSAVRESFRRLAKPA
RVSSAVSDPQVKVLQLINAYRFRGHLAANLDPLGLWKRPDVPELDPAFYGLTEADLDRTFNTGSLALGKE
TATLREIIEALKKTYCGSIGVEYMHISDPEERRWLQQRIESGRPSFSAEEKKAILERLTAAEGFERFLHT
KFVGQKRFSLEGGESLIPMLDEIIRRAGKLGVKEIVIGMAHRGRLNVLVNVLGKPPRDLFAEFEGKHGPD
EVLGSGDVKYHLGFSSDRETDGGEVHLSLAFNPSHLEIVNPVVEGSVRARQDRRGDGQDRKKVLPILIHG
DAAFAGQGVVAETLNLSQLRGYRTGGTIHIVINNQIGFTTSPPDDRSTPYCTDVAKMVQAPIFHVNGDDP
EAVVFATRLALEYRQKFKKDVVIDLVCYRRHGHNEGDEPSFTQPLMYKKIKKHPTTRELYADKLVAEGVI
TEEEADEMVNEYRDALDAGFEVVKEWRPADWLAGDWSPYLGHEWDDPVDTGVPLERLKELAEKLTTVPEG
FKVHPKVKKILEDRREMAEGEKPIDWGMAEALAFASLLDEGYPVRLSGQDSGRGTFSHRHAVLHDQKTGE
TYIPLNHLSEGQASFEVYDSPLSEEAVLGFEYGYSTAEPNTLVIWEAQFGDFANGAQVVIDQFISSGEQK
WGRLSGLVMLLPHGYEGQGPEHSSARLERFLQLCAEDNMQVCNPTTPAQYFHLLRRQALRPFRKPLVVMT
PKSLLRHPLAVSSLEELAEGSFQPVIGDIDELDPKKVKRVVLCSGKVYYDLLEARRKRGIDDVAIVRIEQ
LYPFPHEELAAELAKYPNAKEVVWCQEEPKNQGAWYFIQHHLEEVLPEGQKLRYAGRPASASPAVGYMSL
HKKQQEALVEDALG
>gnl|CDD|236500 PRK09405, aceE, pyruvate dehydrogenase subunit E1; Reviewed
IRDGSESQLNDIDPIETQEWLEALDSVIREEGPERAHYLLEQLLERAREKGVSLPASATTPYINTIPVEE
EPEYPGDLELERRIRSYIRWNAAAMVLRANKKDLGLGGHISSFASSATLYEVGFNHFFRAPNEPHGGDLV
FFQGHASPGIYARAFLEGRLTEEQLDNFRQEVDGKGLSSYPHPWLMPDFWQFPTVSMGLGPIMAIYQARF
LKYLENRGLKDTSDQKVWAFLGDGEMDEPESLGAISLAAREKLDNLIFVINCNLQRLDGPVRGNGKIIQE
LEGIFRGAGWNVIKVIWGSRWDPLLAKDTSGKLVQLMNETVDGDYQTYKAKDGAYVREHFFGKYPETKAL
VADMSDDDIWALNRGGHDPRKVYAAYKAAVEHKGQPTVILAKTIKGYGMGEAGEGKNIAHQVKKLDLDDL
KHFRDRFNIPISDEQLEKLPYYKPGEDSPEIKYLHERRKALGGYLPARRPKFEPLEVPALSAFEALLKGS
GEREISTTMAFVRILNILLKDKEIGKRIVPIIPDEARTFGMEGLFRQIGIYNPHGQLYTPVDRDQLMYYK
ESKDGQILQEGINEAGAMASWIAAATSYSTHGEPMIPFYIYYSMFGFQRIGDLAWAAGDQRARGFLLGGT
AGRTTLNGEGLQHEDGHSHILASTIPNCVSYDPAFAYEVAVIVQDGLRRMYGEQENVFYYITVMNENYHQ
PAMPEGAEEGILKGMYKLETAEGKKGKPKVQLLGSGTILREVLEAAEILAEDYGVAADVWSVTSFNELAR
DGQDVERWNMLHPTEEPRVPYVTQVLKGAEGPVVAATDYMKLFAEQIRAFVPGDYVVLGTDGFGRSDTRE
ALRRFFEVDAEYVVVAALKALADEGEIDASVVAEAIKKYGIDPDKANPRTA
>gnl|CDD|181826 PRK09406, gabD1, succinic semialdehyde dehydrogenase; Reviewed
MPIATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMT
LEMGKTLASAKAEALKCAKGFRYYAEHAEALLADEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQV
VRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGS
EPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDA
FAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVIT
DITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMT
VSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG
>gnl|CDD|236501 PRK09407, gabD2, succinic semialdehyde dehydrogenase; Reviewed
ATTTALPMPAPSALTFERLRRLTARVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAW
AATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPKLLAPRRRAG
ALPVLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLP
RDLWQVVTGPGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAA
AGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHV
DDAVAKGATVLAGGKARPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYG
LNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIAT
QRVLPLAPPPGMPYEKYAKLMLTGLRLMKKLRGR
>gnl|CDD|181828 PRK09408, ompX, outer membrane protein OmpX
MKKIACLSALACVLAVTAGTAVAATSTVTGGYAQSDAQGVANKMGGFNLKYRYEQDNSPLGVIGSFTYTE
KSRTADSGDYNKGQYYGITAGPAYRINDWASIYGVVGVGYGKFQTTEYPTYKHDTSDYGFSYGAGLQFNP
MENVALDFSYEQSRIRSVDVGTWIAGVGYRF
>gnl|CDD|181829 PRK09409, PRK09409, IS2 transposase TnpB; Reviewed
MDSARALIARGWGVSLVSRCLRVSRAQLHVILRRTDDWMDGRRSRHTDDTDVLLRIHHVIGELPTYGYRR
VWALLRRQAELDGMPAINAKRVYRIMRQNALLLERKPAVPPSKRAHTGRVAVKESNQRWCSDGFEFCCDN
GERLRVTFALDCCDREALHWAVTTGGFNSETVQDVMLGAVERRFGNDLPSSPVEWLTDNGSCYRANETRQ
FARMLGLEPKNTAVRSPESNGIAESFVKTIKRDYISIMPKPDGLTAAKNLAEAFEHYNEWHPHSALGYRS
PREYLRQRACNGLSDNRCLEI
>gnl|CDD|236502 PRK09410, ulaA, PTS system ascorbate-specific transporter subunit IIC; Reviewed
MNIFLFFINNILTQPAILVGLIALIGLILQKKPASDVIKGTLKTIIGFLILGAGAGILVSSLKPFGTMFQ
EAFGIQGVVPNNEAIVAAAQKKFGSATALIMLLGFLINILLARFTPFKYIFLTGHHMFQMACLIAVILSV
AGLSGWGLIIFGGLLLGLYWAISPAITQKYTRKVTGNDGFAIGHFQSLGYWLAGKVGKLFGKKEKSTEDI
KLPKSLSFLRDSTVSTAITMTIFFLIAALFAGIEYVEEMAGGQNFIVYILMQGLTFAAGVFIILQGVRMF
LAELVPAFQGISEKLVPGAKPALDCPAVFPYAPNAVLIGFLSSFIGGLIGMGILGAFGSVVIIPGFIPHF
FCGATAGVFGNATGGWRGAIIGAFVNGLLITFLPALLLPVLGSLGMANTTFGDWDFGAPGILLGFLAKLF
GIIGIIIVIALALLVLAGRALRKKEDAEKQLA
>gnl|CDD|181831 PRK09411, PRK09411, carbamate kinase; Reviewed
MKTLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARSYRLAIVHGNGPQVGLLALQNLAWKEVEP
YPLDVLVAESQGMIGYMLAQSLSAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAY
GWQMKRDGKYLRRVVASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTEDGAGSEAVIDKDLAAALLA
EQINADGLVILTDADAVYENWGTPQQRAIRHATPDELAPFAKADGAMGPKVTAVSGYVRSRGKPAWIGAL
SRIEETLAGEAGTCISL
>gnl|CDD|236503 PRK09412, PRK09412, anaerobic C4-dicarboxylate transporter; Reviewed
MFWLELIIVLLAIFLGARLGGIGIGFAGGLGVLILTFIFGLKPGSIPIDVILIIMAVIAAIAAMQAAGGL
DYLVKLAEKILRKNPKYITFLAPIVTYLFTFLAGTGHIAFSTLPVIAEVAKEQGIRPSRPLSIAVVASQI
AITASPISAAVVAMSSVLEPLGVSYLTLLMVVIPSTLLAVMVAAFVTNKMGKELKDDPEYQKRLAEGLVK
LRGEKEIEIKPGAKLSVILFLLGVVAVVLYAIFPSLRPGFIEGPPLGMTEAIQIFMLSAAALIVLLCKID
TDEILSSSVFKSGMSACICILGVAWLGDTFVNAHIDEIKETAGSLIQSYPWLLAVALFFASALLYSQAAT
AKALMPLALALGVPPLTAIASFAAVSGLFVLPTYPTLLAAVEMDDTGTTRIGKYVFNHSFMIPGLLGIAV
SVAFGFLLGSIVL
>gnl|CDD|181833 PRK09413, PRK09413, IS2 repressor TnpA; Reviewed
MIDVLGPEKRRRRTTQEKIAIVQQSFEPGMTVSLVARQHGVAASQLFLWRKQYQEGSLTAVAAGEQVVPA
SELAAAMKQIKELQRLLGKKTMENELLKEAVEYGRAKKWIAHAPLLPGDGE
>gnl|CDD|181834 PRK09414, PRK09414, NADP-specific glutamate dehydrogenase
MSADEYLESVLEQVKKRNPGQPEFHQAVREVLESLWPVLEKNPEYAEAGILERLVEPERVIIFRVPWVDD
KGQVQVNRGFRVQFNSAIGPYKGGLRFHPSVNLSILKFLGFEQIFKNALTGLPIGGGKGGSDFDPKGKSD
AEIMRFCQSFMTELYRHIGPDTDVPAGDIGVGGREIGYLFGQYKRLTNRFEGVLTGKGLSFGGSLIRTEA
TGYGLVYFAEEMLKARGDSFEGKRVVVSGSGNVAIYAIEKAQQLGAKVVTCSDSSGYVYDEEGIDLEKLK
EIKEVRRGRISEYAEEFGAEYLEGGSPWSVPCDIALPCATQNELDEEDAKTLIANGVKAVAEGANMPSTP
EAIEVFLEAGVLFAPGKAANAGGVATSGLEMSQNASRLSWTFEEVDARLHDIMKNIHHACVETAEEYGKP
GNYVAGANIAGFVKVADAMLAQGVI
>gnl|CDD|181835 PRK09415, PRK09415, RNA polymerase factor sigma C; Reviewed
MEELTIEAFEIEDKEDLIDEIMNEYGQEVLQLVYSYVKNKEVAEDLTQEIFVKCYKSLHTYKGKSSLKTW
LYRIAINHCKDYLKSWHNKKVIVTEDIFTYMESQKESVEEEVIQNAEDERLASAVMSLPIKYREVIYLFY
YEELSIKEIAEVTGVNENTVKTRLKKAKELLKKGLEEEV
>gnl|CDD|181836 PRK09416, lstR, PadR family transcriptional regulator
MEDRLKGLKKSMDNTTFKHLSFSEQHQKAVREKIKQSSEKEEDILLAILQLLMNEKTGYELLQLLRQRGI
LTFEGNEGSLYTLLHRLEQNRFIQSSWDHEGAKYYQLTDKGNKMLRKAEKNATKARFILKGLVQE
>gnl|CDD|181837 PRK09417, mogA, molybdenum cofactor biosynthesis protein MogA; Provisional
MDTLKIGLVSISDRASSGVYEDKGIPALEEWLASALTSPFEIETRLIPDEQDLIEQTLIELVDEMGCDLV
LTTGGTGPARRDVTPEATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIK
ETLEGLKDADGNVVVPGIFAAVPYCIDLIGGPYIETNPEVVKAFRPKSARRDV
>gnl|CDD|236504 PRK09418, PRK09418, bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
MKKSKKMLAGATLAIGVIAPQVLPATAHADEKTGESTVNLRILETSDIHVNLMNYDYYQTKTDNKVGLVQ
TATLVNKAREEAKNSVLFDDGDALQGTPLGDYVANKINDPKKPVDPSYTHPLYRLMNLMKYDVISLGNHE
FNYGLDYLNKVISKTEFPVINSNVYKDDKDNNEENDQNYFKPYHVFEKEVEDESGQKQKVKIGVMGFVPP
QVMNWDKANLEGKVKAKDIVETAKKMVPKMKAEGADVIVALAHSGVDKSGYNVGMENASYYLTEVPGVDA
VLMGHSHTEVKDVFNGVPVVMPGVFGSNLGIIDMQLKKVNGKWEVQKEQSKPQLRPIADSKGNPLVQSDQ
NLVNEIKDDHQATIDYVNTAVGKTTAPINSYFSLVQDDPSVQLVTNAQKWYVEKLFAENGQYSKYKGIPV
LSAGAPFKAGGRNGATYYTDIPAGTLAIKNVADLYVYPNTLYAVKVNGAQVKEWLEMSAGQFNQIDPKKT
EEQPLVNIGYPTYNFDILDGLKYEIDVTQPAKYDKDGKVVNANTNRIINMTYEGKPVADNQEFIVATNNY
RGSSQTFPGVSKGEVVYQSQDETRQIIVKYMQETPVIDPAADKNWAFKPIVADKLNTTFDSSPNAQKYIK
KDGNISYVGPSENEFAKYAIDITKKNDDDKETGGENPTTPPTGEGDNGENPTTPPTGEGNNGENPTTPPT
GEGNNGGNPTTPSTDEGNNAGSGQTTTDNQNSKETTTVSENKEERDLPKTGTSVASTIGAGLAFIGAGFL
LLFRRKKANR
>gnl|CDD|236505 PRK09419, PRK09419, multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase
LKKFSRKKITAILVTSAMIFSLILPLTTTKAEENEAHPLVNIQILATTDLHGNFMDYDYASDKETTGFGL
AQTATLIKKARKENPNTLLVDNGDLIQGNPLGEYAVKDNILFKNKTHPMIKAMNALGYDAGTLGNHEFNY
GLDFLDGTIKGANFPVLNANVKYKNGKNVYTPYKIKEKTVTDENGKKQGVKVGYIGFVPPQIMTWDKKNL
KGKVEVKNIVEEANKTIPEMKKGGADVIVALAHSGIESEYQSSGAEDSVYDLAEKTKGIDAIVAGHQHGL
FPGADYKGVPQFDNAKGTINGIPVVMPKSWGKYLGKIDLTLEKDGGKWKVVDKKSSLESISGKVVSRDET
VVDALKDTHEATIAYVRAPVGKTEDDIKSIFASVKDDPSIQIVTDAQKYYAEKYMKGTEYKNLPILSAGA
PFKAGRNGVDYYTNIKEGDLAIKDIGDLYLYDNTLYIVKLNGSQVKDWMEMSAGQFNQIKPNDGDLQALL
NENFRSYNFDVIDGVTYQIDVTKPAKYNENGNVINADGSRIVNLKYDGKPVEDSQEFLVVTNNYRASGGG
GFPHLKEDEIVYDSADENRQLLMDYIIEQKTINPNADNNWSIAPIKGTNWVTFESSLAVKPFNEGKINIP
YSRDGRTPGVGAYKLNFVDEAEPEKKDNWELTILHTNDFHGHLDGAAKRVTKIKEVKEENPNTILVDAGD
VYQGSLYSNLLKGLPVLKMMKEMGYDASTFGNHEFDWGPDVLPDWLKGGGDPKNRHQFEKPDFPFVASNI
YVKKTGKLVSWAKPYILVEVNGKKVGFIGLTTPETAYKTSPGNVKNLEFKDPAEAAKKWVKELKEKEKVD
AIIALTHLGSNQDRTTGEITGLELAKKVKGVDAIISAHTHTLVDKVVNGTPVVQAYKYGRALGRVDVKFD
KKGVVVVKTSRIDLSKIDDDLPEDPEMKEILDKYEKELAPIKNEKVGYTSVDLDGQPEHVRTGVSNLGNF
IADGMKKIVGADIAITNGGGVRAPIDKGDITVGDLYTVMPFGNTLYTMDLTGADIKKALEHGISPVEFGG
GAFPQVAGLKYTFTLSAEPGNRITDVRLEDGSKLDKDKTYTVATNNFMGAGGDGYSFSAASNGVDTGLVD
REIFTEYLKKLGNPVSPKIEGRIQEVFLPTKQKDGSWTLKEDQ
>gnl|CDD|236506 PRK09420, cpdB, bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
MMMIKLSATLLATLLAASANAATVDLRIMETTDLHSNMMDFDYYKDKPTEKFGLVRTASLIKAARAEAKN
SVLVDNGDLIQGSPLGDYMAAKGLKAGDVHPVYKAMNTLDYDVGNLGNHEFNYGLDYLKKALAGAKFPYV
NANVIDAKTGKPLFTPYLIKEKEVKDKDGKEHTIKIGYIGFVPPQIMVWDKANLEGKVTVRDITETARKY
VPEMKEKGADIVVAIPHSGISADPYKAMAENSVYYLSEVPGIDAIMFGHSHAVFPGKDFADIPGADIAKG
TLNGVPAVMPGRWGDHLGVVDLVLENDSGKWQVTDAKAEARPIYDKANKKSLAAEDPKLVAALKADHQAT
RAFVSQPIGKAADNMYSYLALVQDDPTVQIVNNAQKAYVEHFIQGDPDLADLPVLSAAAPFKAGGRKNDP
ASYVEVEKGQLTFRNAADLYLYPNTLVVVKATGAEVKEWLECSAGQFNQIDPNSTKPQSLINWDGFRTYN
FDVIDGVNYQIDVTQPARYDGECKLINPNANRIKNLTFNGKPIDPKATFLVATNNYRAYGGKFAGTGDDH
IAFASPDENRSVLAAYISAESKRAGEVNPSADNNWRFAPIKSDKKLDIRFETSPSDKAAAFIKEKAQYPM
KKVGTDDIGFAVYQIDLSK
>gnl|CDD|181841 PRK09421, modB, molybdate ABC transporter permease subunit
MILSDPEWQAVLLSLKVSSVAVLFSLPFGILVAWLLARCRFPGKSLLDSLLHLPLVLPPVVTGYLLLISM
GRRGFIGQWLYEWFGISFAFSWRGAALAAAVMAFPLMVRAIRLSLEAVDRKLEQAARTLGASPWRVFFTI
TLPLTLPGIIAGTVLAFARSLGEFGATITFVSNIPGETQTIPSAMYTLIQTPGGESAAARLCIISIAIAL
ASLLLSEWLARRSRKRLGA
>gnl|CDD|181842 PRK09422, PRK09422, ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
MKAAVVNKDHTGDVVVEKTLRPLKHGEALVKMEYCGVCHTDLHVANGDFGDKTGRILGHEGIGIVKEVGP
GVTSLKVGDRVSIAWFFEGCGHCEYCTTGRETLCRSVKNAGYTVDGGMAEQCIVTADYAVKVPEGLDPAQ
ASSITCAGVTTYKAIKVSGIKPGQWIAIYGAGGLGNLALQYAKNVFNAKVIAVDINDDKLALAKEVGADL
TINSKRVEDVAKIIQEKTGGAHAAVVTAVAKAAFNQAVDAVRAGGRVVAVGLPPESMDLSIPRLVLDGIE
VVGSLVGTRQDLEEAFQFGAEGKVVPKVQLRPLEDINDIFDEMEQGKIQGRMVIDFTH
>gnl|CDD|181843 PRK09423, gldA, glycerol dehydrogenase; Provisional
MDRIFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGECSD
NEIDRLVAIAEENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERY
LFLPKNPDLVLVDTAIIAKAPARFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETL
LEDGLKAKLAVEAKVVTPALENVIEANTLLSGLGFESGGLAAAHAIHNGLTALEDTHHLTHGEKVAFGTL
TQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSDEELRKVAEAACAEGETIHNMPFKVTPEDVAA
AILAADAYGQRYKQEW
>gnl|CDD|236507 PRK09424, pntA, Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIIL
KVNAPSDDEIALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYR
AVIEAAHEFGRFFTGQITAAGKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAE
FLELDFEEEGGSGDGYAKVMSEEFIKAEMALFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSV
IVDLAAENGGNCELTVPGEVVVTDNGVTIIGYTDLPSRLPTQSSQLYGTNLVNLLKLLCPEKDGNIVVDF
DDVVIRGVTVVRDGEITWPPPPIQVSAAPAAAAAAPAAKEEEKKPASPWRKYALMALAAALFGWLASVAP
AEFLSHFTVFVLACVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALLQIGSGSGLVTFLAFIAVLIAS
INIFGGFTVTQRMLKMFRK
>gnl|CDD|181845 PRK09425, prpD, bifunctional 2-methylcitrate dehydratase/aconitate hydratase
MSAVISNVRPDPDQVLVDIADYVLNYEIDSAEAYDTARYCLMDTLGCGLLALRYPECTKLLGPIVPGTVV
PNGARVPGTSFQLDPVQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKAVAEGKEPLT
MRDVLTAMIKAHEIQGVLALENSFNRVGLDHVLLVKVASTAVVAKLLGGTREEILNALSLAWVDGQSLRT
YRHAPNTGSRKSWAAGDATSRAVRLALIALTGEMGYPSALTAPTWGFYDVLFKGKPFRFQRPYGSYVMEN
VLFKISFPAEFHAQTAVEAAVTLHPQVKARLDDIERITIRTHESAIRIIDKKGPLNNPADRDHCLQYMVA
VPLLFGRLTAEDYEDAVAADPRIDALREKMVVVEDPQFTRDYLDPEKRSIANAVQVFFKDGSSTEEVEVE
YPIGHRRRRAEGIPLLVEKFKANLATRFPAKQQQRILDLCLDQERLEAMPVNEFVDLFVI
>gnl|CDD|236508 PRK09426, PRK09426, methylmalonyl-CoA mutase; Reviewed
MSTIPDFADLALKAAASAPGKTPDSLVWQTPEGIDVKPLYTAADLEGLEHLDTLPGFAPFLRGPYATMYA
GRPWTIRQYAGFSTAEESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVVGDVGKAGVAIDSVEDMK
ILFDGIPLDKMSVSMTMNGAVLPILAFYIVAAEEQGVPPEKLSGTIQNDILKEFMVRNTYIYPPEPSMRI
IADIFAYTSQNMPKFNSISISGYHMQEAGATADLELAYTLADGREYVRAGLAAGLDIDDFAPRLSFFWAI
GMNFFMEIAKLRAARLLWAKIVKQFGPKNPKSLALRTHCQTSGWSLTEQDPYNNVVRTTIEAMAATLGGT
QSLHTNALDEAIALPTDFSARIARNTQLILQEETGITRVVDPWAGSYYVESLTHELAEKAWAHIEEVEAL
GGMAKAIEAGIPKLRIEEAAARTQARIDSGKQVIVGVNKYRLDKEDPIDVLEVDNTAVRAEQIARLERLR
AERDEAAVEAALAALTRAARSGEGNLLALAVDAARARATVGEISDALEKVFGRHRAEIRTISGVYGSEYG
DDPEFAAARALVEAFAEAEGRRPRILVAKMGQDGHDRGAKVIATAFADLGFDVDIGPLFQTPEEAARQAV
ENDVHVVGVSSLAAGHKTLVPALIEALKKLGREDIMVVVGGVIPPQDYDFLYEAGVAAIFGPGTVIADAA
IDLLELLSARLGYA
>gnl|CDD|236509 PRK09427, PRK09427, bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase TrpF
TMMPTVLAKIVADKAIWVAARKQQQPLASFQNEIQPSDRSFYDALKGPKTAFILECKKASPSKGLIRDDF
DPAEIARVYKHYASAISVLTDEKYFQGSFDFLPIVRAIVTQPILCKDFIIDPYQIYLARYYGADAILLML
SVLDDEQYRQLAAVAHSLNMGVLTEVSNEEELERAIALGAKVIGINNRNLRDLSIDLNRTRELAPLIPAD
VIVISESGIYTHAQVRELSPFANGFLIGSSLMAEDDLELAVRKLILGENKVCGLTRPQDAKAAYDAGAVY
GGLIFVEKSPRYVSLEQAQEIIAAAPLRYVGVFRNADIEDIVDIAKQLSLAAVQLHGDEDQAYIDALREA
LPKTCQIWKAISVGDTLPARDLQHVDRYLLDNGQGGTGQTFDWSLLPGQSLDNVLLAGGLNPDNCQQAAQ
LGCAGLDFNSGVESAPGIKDAQKLASVFQTLRAY
>gnl|CDD|236510 PRK09428, pssA, CDP-diacylglycerol--serine O-phosphatidyltransferase
MLSKFKRNKHQQHLAQLPKIPQSPDDVETLYSPADFRETLLEKIASAKKRIYIVALYLEDDEAGREILDA
LYQAKQQNPELDIKVLVDWHRAQRGLIGAAASNTNADWYCEMAQEYPGVDIPVYGVPVNTREALGVLHLK
GFIIDDTVLYSGASLNNVYLHQHDKYRYDRYHLIRNAELADSMVNFIQQNLLNSPAVNRLDQPNRPKTKE
IKNDIRQFRQRLRDAAYQFQGQANNDELSVTPLVGLGKKNLLNKTIFHLMASAEQKLTICTPYFNLPAIL
VRNIIRLLRRGKKVEIIVGDKTANDFYIPPDEPFKIIGALPYLYEINLRRFAKRLQYYIDNGQLNVRLWK
DGDNSYHLKGIWVDDRWMLLTGNNLNPRAWRLDLENALLIHDPKQELAEQREKELELIRTHTTRVKHYSQ
LESIADYPVKVRKLIRRLRRIRIDRLIKRIL
>gnl|CDD|236511 PRK09429, mepA, penicillin-insensitive murein endopeptidase; Reviewed
MLKTLLALLALLASSASAAATPWGKITQPVAGAAQSIGSYANGCLAGAVALPLDGPGYQVMRLSRNRYWG
HPDLIAFIERLSAQAAQAGLGTLLIGDMSQPRGGPFLSGHASHQTGLDADIWLPLPKRRLSRAERERPSA
LDLVSRDGLRVDPNLWTPQHASLIKLAAQDPRVTRIFVNPAIKKQLCRTAGGDRSWLRKVRPWWGHDYHF
HVRLRCPAGSPECEDQAPPPPGDGCGAELASWSDAPFEPPKPTTKPKPKPPPPLPPACQAVLDAP
>gnl|CDD|236512 PRK09430, djlA, co-chaperone DjlA
MQYWGKILGFAFGFLFGGFFGALLGLLIGHMFDKARSRKGGGWFANQRERQALFFNTTFAVMGHLAKAKG
RVTEADIRIASQLMDRMNLHGEARRAAQQAFREGKEPDFPLREKLRQFRSVCGGRFDLLRMFLEIQIQAA
FADGSLHPNERQVLYVIAEELGFSRFQFDQLLRMMQAGFRFQQQQGGGGYQQAQRGPTLEDAYKVLGVSE
SDDDQEIKRAYRKLMSEHHPDKLVAKGLPPEMMEMAKEKAQEIQAAYELIKKQKGFK
>gnl|CDD|236513 PRK09431, asnB, asparagine synthetase B; Provisional
MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTH
VLAVNGEIYNHQELRAELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDP
IGIIPLYYGYDEHGNLYFASEMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKN
ELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAIAKKYAARRIEDDERSEAWWPQLHSFAVGLEGSPD
LKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYDVTTIRASTPMYLMARKIKAMGIKMVLSGEG
ADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPED
KMCGNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVSDQQLATARFRFPYNTP
TTKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKNMDDPSGRAVSGVHQSAY
>gnl|CDD|181852 PRK09432, metF, methylenetetrahydrofolate reductase
MSFFHANQRDALNQSLAELQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRT
HSIIKGIKKRTGLEAAPHLTCIDATPDELRTIAKDYWNNGIRHIVALRGDLPPGSGKPEMYASDLVTLLK
SVADFDISVAAYPEVHPEAKSAQADLINLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIVPG
ILPVSNFKQLKKFADMTNVRIPAWMAKMFDGLDDDAETRKLVGASIAMDMVKILSREGVKDFHFYTLNRA
ELTYAICHTLGVRPGL
>gnl|CDD|181853 PRK09433, thiP, thiamine transporter membrane protein; Reviewed
GWLIPGVLAAALLVALALLALLALWLHAPGGDWDAVWQDSYLWHVLRFSFWQAFLSALLSVLPAIPLARA
LYRRRFPGRGLLLRLCAMTLVLPVLVAVFGLLSVYGRSGWLAQLLQALGLEWPFSIYGLQGILLAHVFFN
LPLATRLLLQALESIPAEQRQLAAQLGMRGWQFFRLVEWPYLRRQLPPVAALIFMLCFTSFATVLTLGGG
PKATTIELAIYQALSFDFDLARAALLALLQMVLCLGLVLLSQRLSKAIAVGATLLRGWRDPQDSLWSRLW
DGLLIVLALLLLLPPLLAVVVSGLNASLLRVLAQPALWQALWTSLRIALAAALLAVVLTMMLLWSSRELR
LRQRKLAAQALELSGMLILAMPGIVLATGLFLLLRNTTDLPASALGIVILTNALMALPYALRVLEPPMRD
IAARYGRLCQSLGIRGWSRLRLIELRALRRPLAQAFAFACALSLGDFGVIALFGSQDFRTLPFLLYQQLG
SYRSQDAAVTALLLLLLCLLLFTLIERLPGRHAKT
>gnl|CDD|236514 PRK09434, PRK09434, aminoimidazole riboside kinase; Provisional
MMNKVWVLGDAVVDLIPEGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVD
TTYLRLDPAHRTSTVVVDLDDQGERSFTFMVRPSADLFLQPQDLPPFRQGEWLHLCSIALSAEPSRSTTF
EAMRRIKAAGGFVSFDPNLREDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYALADR
YPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAGLWTDEAELAEIIAQA
QACGALATTAKGAMTALPNRQELE
>gnl|CDD|236515 PRK09435, PRK09435, methylmalonyl Co-A mutase-associated GTPase MeaB
AMMRRELDVDELVEGVLAGDRAALARAITLVESTRPDHRALAQELLDALLPHTGNALRIGITGVPGVGKS
TFIEALGMHLIEQGHKVAVLAVDPSSTRTGGSILGDKTRMERLSRHPNAFIRPSPSSGTLGGVARKTRET
MLLCEAAGYDVILVETVGVGQSETAVAGMVDFFLLLQLPGAGDELQGIKKGIMELADLIVINKADGDNKT
AARRAAAEYRSALRLLRPKDPGWQPPVLTCSALEGEGIDEIWQAIEDHRAALTASGEFAARRREQQVDWM
WEMVEEGLLDRLFADPAVRARLPELEAAVAAGTLTPALAARQLLEAFGLQYF
>gnl|CDD|181856 PRK09436, thrA, bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
MRVLKFGGTSVANAERFLRVADIIESNARQEQVAVVLSAPAKVTNHLVAMIEKAAKGDDAYPEILDAERI
FHELLDGLAAALPGFDLAQLKAKVDQEFAQLKDILHGISLLGECPDSVNAAIISRGERLSIAIMAAVLEA
RGHDVTVIDPRELLLADGHYLESTVDIAESTRRIAASFIPADHVILMPGFTAGNEKGELVTLGRNGSDYS
AAILAACLDADCCEIWTDVDGVYTADPRVVPDARLLKSLSYQEAMELSYFGAKVLHPRTIAPIAQFQIPC
LIKNTFNPQAPGTLIGAESDEDSLPVKGISNLNNMAMFNVSGPGMKGMVGMASRVFAALSRAGISVVLIT
QSSSEYSISFCVPQSDAAKAKRALEEEFALELKEGLLEPLEVEENLAIISVVGDGMRTHPGIAAKFFSAL
GRANINIVAIAQGSSERSISVVIDNDDATKALRACHQSFFLSDQVLDVFVIGVGGVGGALLEQIKRQQPW
LKKKNIDLRVCGIANSRKMLLDEHGIDLDNWREELAEAGEPFDLDRLIRLVKEYHLLNPVIVDCTSSQAV
ADQYADFLAAGFHVVTPNKKANTSSYAYYHQLREAARKSRRKFLYETNVGAGLPVIETLQNLLNAGDELL
KFEGILSGSLSFIFGKLDEGMSFSEATRLAKEKGYTEPDPRDDLSGMDVARKLLILAREAGYELELEDIE
VESVLPEEFDASGSVDEFMARLPELDAEFAARVAKARAEGKVLRYVGQIEDGKCRVGIAEVDANHPLYKV
KGGENALAFYTRYYQPIPLVLRGYGAGNEVTAAGVFADLLRTLSWKLGV
>gnl|CDD|181857 PRK09437, bcp, thioredoxin-dependent thiol peroxidase; Reviewed
MNPLKAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGI
STDKPEKLSRFAEKELLNFTLLSDEDHQVAEQFGVWGEKKFMGKTYDGIHRISFLIDADGKIEHVFDKFK
TSNHHDVVLDYLKE
>gnl|CDD|236516 PRK09438, nudB, dihydroneopterin triphosphate pyrophosphatase; Provisional
MMPYKRPVSVLVVIYTPDLGVLMLQRADDPDFWQSVTGSLEEGETPAQTAIREVKEETGIDVLAEQLTLI
DCQRSIEYEIFPHWRHRYAPGVTRNTEHWFCLALPHERPVVLTEHLAYQWLDAREAAALTKSWSNAEAIE
QLVIRLAL
>gnl|CDD|181859 PRK09439, PRK09439, PTS system glucose-specific transporter subunit; Provisional
MGFFDKLKSLVSDDKKDTGTIEIIAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTGNKMVAPVDGTIGK
IFETNHAFSIESDSGVELFVHFGIDTVELKGEGFKRIAEEGQRVKVGDPIIEFDLPLLEEKAKSTLTPVV
ISNMDEIKELIKLSGSVTAGETPVIRVKK
>gnl|CDD|236517 PRK09440, avtA, valine--pyruvate transaminase; Provisional
MQFSKFGEKFTRHSGITQLMDDLNDGLRTPGAIMLGGGNPAHIPEMEDYFRDLLADLLASGKLTEALGNY
DGPQGKDELIEALAALLNERYGWNISPQNIALTNGSQSAFFYLFNLFAGRRADGSLKKILFPLAPEYIGY
ADAGLEEDLFVSYRPNIELLPEGQFKYHVDFEHLHIDEDTGAICVSRPTNPTGNVLTDEELEKLDALARQ
HNIPLLIDNAYGPPFPGIIFSEATPLWNPNIILCMSLSKLGLPGVRCGIVIADEEIIEALSNMNGIISLA
PGRLGPAIAAEMIESGDLLRLSETVIRPFYRQKVQLAIALLRRYLPDEPCLIHKPEGAIFLWLWFKDLPI
TTEELYQRLKARGVLVVPGHYFFPGLDEDWPHAHQCIRMNYVQDDEEIEKGIAILAEEVEKAYAES
>gnl|CDD|236518 PRK09441, PRK09441, cytoplasmic alpha-amylase; Reviewed
MRNGTMMQYFEWYLPNDGKLWNRLAERAPELAEAGITAVWLPPAYKGTSGGYDVGYGVYDLFDLGEFDQK
GTVRTKYGTKEELLNAIDALHENGIKVYADVVLNHKAGADEKETFRVVEVDPDDRTQIISEPYEIEGWTR
FTFPGRGGKYSDFKWHWYHFSGTDYDENPDESGIFKIVGDGKGWDDQVDDENGNFDYLMGADIDFRHPEV
REELKYWAKWYMETTGFDGFRLDAVKHIDAWFIKEWIEHVREVAGKDLFIVGEYWSHDVDKLQDYLEQVE
GKTDLFDVPLHYNFHEASKQGRDYDMRNIFDGTLVEADPFHAVTFVDNHDTQPGQALESPVEPWFKPLAY
ALILLREEGYPCVFYGDYYGASGYYIDMPFKEKLDKLLLARKNFAYGEQTDYFDHPNCIGWTRSGDEENP
GLAVVISNGDAGEKTMEVGENYAGKTWRDYTGNRQETVTIDEDGWGTFPVNGGSVSVWV
>gnl|CDD|236520 PRK09444, pntB, Re/Si-specific NAD(P)(+) transhydrogenase subunit beta
MSGGLVTAAYIVAAILFIFSLAGLSKHETSRQGNNFGIAGMAIALIATIFGPDTGNVGWIIIAMVIGGAI
GIRLAKKVEMTEMPELVAILHSFVGLAAVLVGFNSYLDHDAGMAPVLVNIHLTEVFLGIFIGAVTFTGSI
VAFGKLRGKISSKPLMLPHRHKLNLAALVVSFLLLIVFVRTDSVGLQVFALLLMTLIALAFGWHLVASIG
GADMPVVVSMLNSYSGWAAAAAGFMLSNDLLIVTGALVGSSGAILSYIMCKAMNRSFISVIAGGFGTDGS
STGDDEEVGEHRETTAEEVAEMLKNSHSVIITPGYGMAVAQAQYPVAEITEKLRARGINVRFGIHPVAGR
LPGHMNVLLAEAKVPYDIVLEMDEINDDFADTDTVLVIGANDTVNPAAQEDPNSPIAGMPVLEVWKAQNV
IVFKRSMNTGYAGVQNPLFFKENTQMLFGDAKASVDAILKAL
>gnl|CDD|236521 PRK09448, PRK09448, DNA starvation/stationary phase protection protein Dps; Provisional
VKTKASNLLYTRNDVPDSEKKATIELLNQQLAQFIDLSLITKQAHWNMKGANFIAVHEMLDGFRTALEDH
LDTMAERAVQLGGVALGTTQVVASKTPLKSYPLDIHNVQDHLKALADRYAIVANDVRKAIDEAGDEDTAD
IFTAASRDLDKFLWFIEAHIEE
>gnl|CDD|181865 PRK09449, PRK09449, dUMP phosphatase; Provisional
MKYDWILFDADETLFHFDAFAGLQRMFSRYGVDFTAEDFQDYQAVNKPLWVDYQNGAITALQLQHTRFES
WAEKLNVTPGELNSAFLNAMAEICTPLPGAVELLNALRGKVKMGIITNGFTELQQVRLERTGLRDYFDLL
VISEQVGVAKPDVAIFDYALEQMGNPDRSRVLMVGDNLHSDILGGINAGIDTCWLNAHGREQPEGIAPTY
QVSSLSELEQLLCK
>gnl|CDD|236522 PRK09450, cyaA, class I adenylate cyclase
MRKYLETLKQRLDALNQLRLARALAALSPAFQQVLSLLPLLLHVNHPLLPGYVSGNTPAGICNFTPDETQ
LAYLQRLELSFGYSVQDPPKGELPITGLYTMGSTGSIGQSESSDLDIWVCHRPWLDAEERQLLQRKCSLL
EQWAASLGVEVNFFLMDEERFRHNESGSALGGEDCGSTQHILLLDEFYRTAIRLAGKRPLWWLVPVEEEE
HYDDYVMTLYSKGFLNPNEWLDLGGLSSLPAEEYFGASLWQLYKGIDSPYKSVLKLLLLEAYSSEYPNTQ
LLSLDFKQRLLAGEIDSDGLDPYCLMLERVTRYLTAINDPTRLELVRRCFYLKVGEKLSRERACVGWRRE
LLSQLVSEWGWDEERLALLDNRANWKIGQVREFHNELVDALMQSYRNLIRFARRNNLSSSISPQDIGILT
RKLYAAFERLPGKVTLLNPQISPDLSEPDLTFIEVPPGRANRSGWYLYNQAPDPDSIIGHQPLEYNRYLN
KLVAWAYFNGLLTSSTRLHLKGNGSDLDLAKLQELVADLRQHFPLRLPAPTPQALLQPCEIRHLLIIVNL
EVDPTAHLRGQVVHFDFRNLDVFSFGGEQENLVGSVDLIYRNSWNEVRTLHFEGEQALLDALKTILGKMH
QDAAPPPSVEVFCYSQHLRGLIRTRVQQLVSECIELRLGSTRQEPGKALRVAGQTWGLFFERLGVSVQKL
ENAVEFYGALSENKLHGLPVQLDTNFLKLPAVVDGFASEGIIQFFFEDNEDGFNVYILDESNRLEHYHHC
EGSKEELVRDVSRFYSSSHDRFTYGSSFINFNLPQFYQLVRVDGRLQVIPFRSQLEEALN
>gnl|CDD|181867 PRK09451, glmU, bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU
MLNSAMSVVILAAGKGTRMYSDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLADEP
LNWVLQAEQLGTGHAMQQAAPFFADDEDILMLYGDVPLISVETLQRLRDAKPQGGIGLLTVKLDNPTGYG
RITRENGKVVGIVEQKDATDEQRQIQEINTGILVANGADLKRWLAKLTNNNAQGEYYITDIIALAHQEGR
EIVAVHPQRLSEVEGVNNRLQLARLERVYQAEQAEKLLLAGVMLRDPARFDLRGTLTHGRDVEIDTNVII
EGNVTLGNRVKIGAGCVLKNCVIGDDCEISPYSVVEDANLGAACTIGPFARLRPGAELAEGAHVGNFVEM
KKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGAT
IGAGTTVTRDVAENELVISRVPQRHIQGWQRPVKKK
>gnl|CDD|236523 PRK09452, potA, spermidine/putrescine ABC transporter ATP-binding protein PotA
SKKLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGR
IMLDGQDITHVPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQR
KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALT
MSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDATVIERLDEQRVRANVEGRECNIYVNFA
VEPGQKLHVLLRPEDLRVEEINDDEHAEGLIGYVRERNYKGMTLDSVVELENGKMVMVSEFFNEDDPDFD
HSLGQKVAVTWVEGWEVVLADEEHK
>gnl|CDD|181869 PRK09453, PRK09453, phosphodiesterase; Provisional
MKLMFASDTHGSLPATEKALELFAQSGADWLVHLGDVLYHGPRNPLPEGYAPKKVAELLNAYADKIIAVR
GNCDSEVDQMLLHFPIMAPYQQVLLEGKRLFLTHGHLYGPENLPALHDGDVLVYGHTHIPVAEKQGGIIL
FNPGSVSLPKGGYPASYGILDDNVLSVIDLEGGEVIAQVAIN
>gnl|CDD|236524 PRK09454, ugpQ, cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
MMSNWPYPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAG
ELTWQDLAQLDAGSWFSAAFAGEPLPTLSQVAARCRAHGMAANIEIKPTTGREAETGRVVALAARALWAG
AAVPPLLSSFSEDALEAARQAAPELPRGLLLDEWPDDWLELTRRLGCVSLHLNHKLLDEARVAALKAAGL
RILVYTVNDPARARELLRWGVDCICTDRIDLIGPDFTAQ
>gnl|CDD|236525 PRK09455, rseB, anti-sigma E factor; Provisional
MKQLWFAVSLLTGSLLFSANASAQPLSSGALLQQMNEASQSLNYELSFINITKQGIESLRYRHARLDNKP
LAQLLQMDGPRREIIQRGNEISYFEPGLEPFTLNGDHIVDSLPSLIYADFKRLSKYYDFISVGRTRIADR
LCQVIRIVPKDGTRYSYIVWIDEESKLPLRVDLLDRDGETLEQFRVISFTVNDDISSLMQGLAKANLPPL
LSLPAGEKAKFNWQPGWLPQGFKEVSRSRRTLPTMDNPIESRLYSDGLFSFSVNVSNADKDSSSEQLLRQ
GRRTVYSEVRGNKEITVVGELPPATAKRIAQSIKFGAAQ
>gnl|CDD|181872 PRK09456, PRK09456, ?-D-glucose-1-phosphatase; Provisional
MLYIFDLGNVIVDIDFNRVLGVWSDLSRVPLATLKKRFTMGEAFHQHERGEISDEAFAEALCHEMALSLS
YEQFAHGWQAVFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEVRAAADHIYLSQDLGMR
KPEARIYQHVLQAEGFSAADAVFFDDNADNIEAANALGITSILVTDKQTIPDYFAKVLC
>gnl|CDD|181873 PRK09457, astD, succinylglutamic semialdehyde dehydrogenase; Reviewed
MTLWINGDWIAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAA
LLEENKEELAEVIARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKRSEMADGAAVLRHRPHGVVAV
FGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAH
PDIDGLLFTGSANTGYLLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCA
RRLLVPQGAQGDAFLARLVAVAKRLTVGRWDAEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQ
LQAGTGLLTPGIIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLL
EIRAGIVNWNKPLTGASSAAPFGGVGASGNHRPSAYYAADYCAYPMASLESDSLTLPATLSPGLDFS
>gnl|CDD|236526 PRK09458, pspB, envelope stress response membrane protein PspB
MSALFLAIPLTIFVLFVAPIWLWLHYRSKRQGSQGLSQEEQQRLAQLTEKAERMRERIQALEAILDAEHP
NWRNR
>gnl|CDD|181876 PRK09461, ansA, cytoplasmic asparaginase I; Provisional
MQKKSIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMPEFHRPEMPDFTIHEYTPLIDSSDMTPEDWQH
IADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAA
NYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGELIVHPITPQ
PIGVVTIYPGISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNM
GGYATGNALAHAGVISGADMTVEAALTKLHYLLSQELSTEEIRQAMQQNLRGELT
>gnl|CDD|236527 PRK09462, fur, ferric uptake regulator; Provisional
MTDNNTALKKAGLKVTLPRLKILEVLQEPDNHHVSAEDLYKRLIDMGEEIGLATVYRVLNQFDDAGIVTR
HNFEGGKSVFELTQQHHHDHLICLDCGKVIEFSDDSIEARQREIAAKHGIKLTNHSLYLYGHCAEGDCRE
DEHAHEGK
>gnl|CDD|236528 PRK09463, fadE, acyl-CoA dehydrogenase; Reviewed
LWSLWLLVPLAIILLPLNLPPLRRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKK
LLNYPKPTLTAEEQAFLDGPVEELCRMVNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAY
AHSRVLQKLASRSGTLAVTVMVPNSLGPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGS
IPDTGVVCKGEWQGEEVLGMRLTWNKRYITLAPIATVLGLAFKLYDPDGLLGDKEDLGITCALIPTDTPG
VEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPKMAGQGWRMLMECLSVGRGISLPSNSTGGAKLAAL
ATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLGEKPSVLSAIAKYHLTERGRQ
VINDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCHPYVLKEMEAAQNND
KQALKAFDKALFGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVSMLVLG
GSLKRRERLSARLGDILSQLYLASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVV
AGLLRVLVFPLGRRYRAPSDKLDHQVAKLLQTPSATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPI
EKKICKALKKGKLPFLRLDELADEALAAGVISEEEAALLREAEEARLRVINVDDFDPEELAAKPVKLPEK
VQKVEAA
>gnl|CDD|181879 PRK09464, pdhR, pyruvate dehydrogenase complex transcriptional repressor PdhR
MAYSKIRQPKLSDVIEQQLEFLILEGTLRPGEKLPPERELAKQFDVSRPSLREAIQRLEAKGLLLRRQGG
GTFVQSSLWQSFSDPLVELLSDHPESQFDLLETRHALEGIAAYYAALRGTDEDFERIRECHHAIELAQQS
GDLDAEANAVMQYQIAVTEAAHNVVLLHLLRCMEPMLEQNVRQNFELLYRRREMLPKVSSHRARIFEAIV
AGKPEKAREASHRHLAFIEEILLDLSREESRRERSLRRLQQRKN
>gnl|CDD|236529 PRK09465, tolC, outer membrane channel protein; Reviewed
MKKLLPLLIGLSLAGFSSASQAEDLLQVYQQARLSNPELLKAAADRDAAFEKINEARSPLLPQLGLGAGY
TYSNGYRDANGIDSNGTSASLQLTQTIFDMSKWRALTLAEKAAGIADVTYQTAQQTLILRTATAYFNVLR
AIDNLSFTEAEKRAIYRQLDQTTQRFNVGLVAITDVQNAQAQYDTVLANEVLARNNLDNAYEALRQITGN
YYPELAVLNTERFSTPKPQSVNALLKEAEKRNLSLLSARLSQDLAREQIRLAQAGHMPTLDLTASYGISD
TSYSGANGTQYDDSDMGQNKVGLNLSLPLYSGGAVNSQVKQAQYNFVGASEQLESAHRSVVQTVRSSFNN
INASISSINAYEQAVVSAQSSLDATEAGYEVGTRTIVDVLDATTTLYDAKQQLSNARYNYLINQLNLKQA
LGTLNEQDLLALNNGLGKPVSTSPEN
>gnl|CDD|236530 PRK09466, metL, bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional
MSVIAQAGAMGRQLHKFGGSSLADAKCYRRVAGILAEYSQPDDLVVVSAAGKTTNQLISWLKLSQTDRLS
AHQVQQTLRRYQQDLIEGLLPAEQARSLLSRLISDLERLAALLDGGINDAQYAEVVGHGEVWSARLMAAL
LNQQGLPAAWLDARSFLRAERAAQPQVDEGLSYPLLQQLLAQHPGKRLVVTGFISRNEAGETVLLGRNGS
DYSATLIGALAGVERVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSD
IDLQLRCSYQPEQGSTRIERVLASGTGARIVTSLDDVCLIELQVPASHDFKLAQKELDQLLKRAQLRPLA
VGVHPDRQLLQLAYTSEVADSALKLLDDAALPGELKLREGLALVALVGAGVTRNPLHCHRFYQQLKDQPV
EFIWQSEDGLSLVAVLRQGPTESLIQGLHQSLFRAEKRIGLVLFGKGNIGSRWLELFAREQSTLSARTGF
EFVLVGVVDSRRSLLNYDGLDASRALAFFDDEAVEWDEESLFLWLRAHPYDELVVLDVTASEQLALQYPD
FASHGFHVISANKLAGSSPSNFYRQIKDAFAKTGRHWLYNATVGAGLPINHTVRDLRNSGDSILAISGIF
SGTLSWLFLQFDGSVPFSELVDQAWQQGLTEPDPRDDLSGRDVMRKLVILAREAGYEIEPDDVRVESLVP
AHLEDGSLDQFFENGDELDEQMLQRLEAAAEQGKVLRYVARFDANGKARVGVEAVRPDHPLANLLPCDNV
FAIESRWYRDNPLVIRGPGAGREVTAGAIQSDLNRLAQLL
>gnl|CDD|236531 PRK09467, envZ, osmolarity sensor protein; Provisional
MRFSPRSSFARTLLLIVTLLFISQVVSYLVVLNYAILPSLQQFNKVLAYEVRLLFTDQLEDGTQLVVPPA
FRREIYRELGISLYSNEAAEEAGLRWAQHYEFLSEQMSQQLGGPTEVRVEVGKESPIVWIKTPLAPNIWV
RVPLTEIHQGDFSPLFRYTLAIGLLSVAGGWLFIRIQNRPLVALEHAALQVGKGEIPPPLREYGASEVRS
VTRAFNQMAAGIKQLEDDRTLLMAGVSHDLRTPLTRIRLATEMMSEEDGYLAESINKDIEECNAIIEQFI
DYLRTGQEMPMEMADLNALLGEVIAAESGYEREIETALQPGPIEVPMNPIAIKRALANLVVNAARYGNGW
IKVSSGTEGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGDSARGSSGTGLGLAIVKRIVDQHNGKVELGNS
EEGGLSARAWLPLTT
>gnl|CDD|181883 PRK09468, ompR, osmolarity response regulator; Provisional
MMQENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRR
LRSQNNPTPIIMLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLRRQAPELPGAPSQEEEVIA
FGKFKLNLGTRELFRGDEPMPLTTGEFAVLKALVSHPREPLSRDKLMNLARGREYSAMERSIDVQISRLR
RLIEEDPAHPRYIQTVWGLGYVFVPDGAK
>gnl|CDD|181884 PRK09469, glnA, glutamate--ammonia ligase
MSAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNADFFEEGKMFDGSSIGGWKGINESDMVLMP
DASTAVLDPFFEDSTLIIRCDILEPGTMQGYDRDPRSIAKRAEDYLRSTGIADTVLFGPEPEFFLFDDIR
FGSSISGSHVAIDDIEAAWNSGTKYEGGNKGHRPGVKGGYFPVPPVDSSQDIRSAMCLVMEEMGLVVEAH
HHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHAFGKTATFMPKPMFGDNGSGMHCHMSLSKNGV
NLFAGDKYAGLSEQALYYIGGIIKHAKAINALANPTTNSYKRLVPGYEAPVMLAYSARNRSASIRIPVVA
SPKARRIEVRFPDPAANPYLCFAALLMAGLDGIKNKIHPGEAMDKNLYDLPPEEAAEIPQVAGSLEEALN
ALDADREFLTAGGVFTDDAIDAYIALRREEVDRVRMTPHPVEFELYYSV
>gnl|CDD|236532 PRK09470, cpxA, envelope stress sensor histidine kinase CpxA
KRLPMINSLTARIFAIFWLTLALVLMLVLMLPKLDSRQMTELLDSEQRQGLMIEQHIEAELANDPPNDLM
WWRRLFRAIDKWAPPGQRLLLVTSEGRIIGAERSEMQAVRNFIGQSDNADHPQKKKYGRVEIVGPFSVRD
GEDNYQLYLIRPANSPQSDFINLLFDRPLLLLLVTMLVSTPLLLWLAWSLAKPARKLKNAADEVAQGNLR
QHPELETGPQEFRQAGASFNQMVTALERMMTSQQRLLSDISHELRTPLTRLQLATALLRRRQGESKELER
IETEAQRLDSMINDLLVLSRNQQKNHLERETFKANSLWSEVLEDAKFEAEQMGKSLTVSAPPGPWPINGN
PNALASALENIVRNALRYSHTKIEVAFSVDKDGLTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGG
TGLGLAIVENAIQQHRGWVKAEDSPLGGLRLTIWLPLYKRS
>gnl|CDD|181886 PRK09471, oppB, oligopeptide ABC transporter permease OppB
MLKFILRRCLEAIPTLFILITISFFMMRLAPGSPFTGERTLPPEVMANIEAKYHLNDPIMTQYFSYLKQL
AHGDFGPSFKYKDYSVNDLVASSFPVSAKLGAAAFFLAVILGVSAGVIAALKQNTKWDYTVMGFAMTGVV
IPSFVVAPLLVLIFAITLHWLPGGGWNGGALKFMILPMVALSLAYIASIARITRGSMIEVLHSNFIRTAR
AKGLPMRRIILRHALKPALLPVLSYMGPAFVGIITGSMVIETIFGLPGIGQLFVNGALNRDYSLVLSLTI
LVGALTILFNAIVDVLYAVIDPKIRY
>gnl|CDD|181887 PRK09472, ftsA, cell division protein FtsA; Reviewed
MIKATDRKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAEL
MADCQISSVYLALSGKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQ
EGIKNPVGLSGVRMQAKVHLITCHNDMAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVD
IGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSV
GGRPPRSLQRQTLAEVIEPRYTELLNLVNEEILQLQEQLRQQGVKHHLAAGIVLTGGAAQIEGLAACAQR
VFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYGKESHLNGEAEVEKRVTASVGSWIKRLNSWLRKEF
>gnl|CDD|181888 PRK09473, oppD, oligopeptide transporter ATP-binding component; Provisional
TVPLAQQQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG
RIGGSATFNGREILNLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESV
RMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRE
FNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIPG
NPPNLLRLPKGCPFQPRCPHAMEICSSAPPLEEFGPGRLRACFKPVEELL
>gnl|CDD|236533 PRK09474, malE, maltose/maltodextrin ABC transporter substrate-binding protein MalE
MKIKKGLRTLALSALATLMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLE
EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALS
LIYNKDLVPTPPKTWEEIPALDKELKAKGKSAIMWNLQEPYFTWPLIAADGGYAFKFENGGYDVKDVGVN
NAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTFNGKP
SKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLGAVALKSFQEELAKDPRIAATMDNA
QNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKRITK
>gnl|CDD|236534 PRK09476, napG, quinol dehydrogenase periplasmic component; Provisional
MSRSAKPQNGRRRFLRDVVRTAGGLAAVGVALGLQQQQARASGVALRPPGALNENDFLSACIRCGLCVQA
CPYDTLKLATLASGLSAGTPYFVARDIPCEMCEDIPCVKACPSGALDRELVDIDDARMGLAVLVDQENCL
NFQGLRCDVCYRVCPLIDKAITLELERNERTGKHAFFLPTVHSDACTGCGKCEKACVLEKAAIKVLPRSL
AKGKLGHHYRKGWLEKDEGRSSNAGEIKKLDTKKAEDYLNSGEL
>gnl|CDD|236535 PRK09477, napH, quinol dehydrogenase membrane component; Provisional
GWWRAHRFLILRRLSQLSILALFLSGPWFGVWILKGNLSSSLLFDTIPLTDPLATLQSLAAGHLPATVAL
IGALIITVFYALAGGRAFCSWVCPVNLVTDLANWLRRKLGLNQSATLPRNLRYWLLVLVLVGSALTGTLA
WEWINPVSMLHRGLVFGFGSGWWLILAIFLFDLFVVEHGWCGHLCPLGAFYGLIGKKSLIRVKAHDRQKC
TRCMDCFHVCPEPQVLRPPLKGKQSPSQVTSGDCITCGRCIDVCSEDVFNFTIRFKSGAKS
>gnl|CDD|181892 PRK09478, mglC, galactose/methyl galactoside ABC transporter permease MglC
MSALNKKSFLTYLKEGGIYVVLLVLLAIIIIQDPTFLSLLNLSNILTQSSVRIIIALGVAGLIVTQGTDL
SAGRQVGLAAVVAATLLQSMDNANKVFPELATMPIALVILIVCAIGAVIGLINGLIIAYLNVTPFIATLG
TMIIVYGINSLYYDFVGASPISGFDSGFSTFAQGFVALGSFRLSYITFYALIAVAFVWVLWNKTRFGKNI
FAIGGNPEAAKVSGVNVPLNLLMIYALSGVFYAFGGMLEAGRIGSATNNLGFMYELDAIAACVVGGVSFS
GGVGTVIGVVTGVIIFTVINYGLTYIGVNPYWQYIIKGAIIIFAVALDSLKYARKK
>gnl|CDD|236536 PRK09479, glpX, fructose 1,6-bisphosphatase II; Reviewed
EAMDRNLALELVRVTEAAALAAARWMGRGDKNAADGAAVDAMRKMLNTVPIDGTVVIGEGERDEAPMLYI
GEKVGTGGGPEVDIAVDPLEGTTLTAKGQPNALAVLAVAERGSLLHAPDMYMEKLAVGPEAKGVVDLDAP
VAENLRAVAKALGKDVSDLTVVVLDRPRHEELIAEIREAGARVKLISDGDVAGAIATAFPDTGVDILMGI
GGAPEGVLAAAALKCLGGEMQGRLLPRNEEERARAKKMGITDLDKVLTLDDLVRGDDVIFAATGVTDGDL
LKGVRFKGGGATTHSLVMRSKSGTVRFIESIHRLDKKDP
>gnl|CDD|181894 PRK09480, slmA, division inhibitor protein; Provisional
MAMKRPKKGERREQILQALAQMLESPPGERITTAKLAARVGVSEAALYRHFPSKARMFEGLIEFIEESLF
SRINQILKDEKDTLARARLILLLLLGFAERNPGMTRVLTGDALMFEDERLQGRINQLFDRIEAQLRQILR
EAKLREGLGFDLDEAALASLLLAFVEGRLSRFVRSGFKRKPTEHFDAQWRLILA
>gnl|CDD|236537 PRK09481, sspA, stringent starvation protein A; Provisional
MAVAANKRSVMTLFSGPTDIYSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNPYQSVPTLVDRELTLY
ESRIIMEYLDERFPHPPLMPVYPVARGESRLMMHRIEKDWYSLMNKIVNGSASEADAARKQLREELLAIA
PVFGEKPYFMSEEFSLVDCYLAPLLWRLPVLGIELSGPGAKELKGYMTRVFERDSFLASLTEAEREMRLG
R
>gnl|CDD|181896 PRK09482, PRK09482, flap endonuclease-like protein; Provisional
MMNHLLIIDALNLIRRIHAVQPSPNDINACVETCQHALDKLIRHSQPTHAVAVFDGDARSSGWRHQLLPD
YKAGRKPMPEALQQGLPAIRAAFEELGIDSWHADGNEADDLIATLAVKVAQAGHQATIVSTDKGYCQLLS
PTIQIRDYFQKRWLDAPFIEQEFGVEPQQLPDYWGLAGISSSKIPGVAGIGPKSAAELLNQFRSLENIYE
SLDALPEKWRKKLEEHKEMARLCRKLAQLQTDLPLGGNLQQLRLNR
>gnl|CDD|236538 PRK09483, PRK09483, response regulator; Provisional
MINVLLVDDHELVRAGIRRILEDIKGIKVVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKIL
RYTPDVKIIMLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIRSVHSGQRYIASDIAQQMALSQIEP
ATENPFASLSERELQIMLMITKGQKVNEISEQLNLSPKTVNSYRYRMFSKLNISGDVELTHLAIRHGLLN
AETLSSQ
>gnl|CDD|181898 PRK09484, PRK09484, 3-deoxy-manno-octulosonate-8-phosphatase KdsC
ASLATCYGPVSDDVMAKAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAII
TGRKSKLVEDRMTTLGITHLYQGQSNKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADA
HPLLLPRADYVTRIAGGRGAVREVCDLLLLAQGKLDEAKGQSI
>gnl|CDD|181899 PRK09485, mmuM, homocysteine methyltransferase; Provisional
MNPFKELLAQGPVLILDGALATELEARGCDLNDSLWSAKVLLENPELIYQVHLDYFRAGADCAITASYQA
TFQGFAARGLSEAEAEELIRRSVELAKEARDEFWAEKPLVAGSVGPYGAYLADGSEYRGDYGLSEEELQD
FHRPRIEALAEAGADLLACETIPNLDEAEALVELLKEEFPGVPAWLSFTLRDGTHISDGTPLAEAAALLA
ASPQVVAVGVNCTAPELVTAAIAALRAVTDKPLVVYPNSGEVYDAVTKTWHGPADDASLGELAPEWYAAG
ARLIGGCCRTTPEDIAALAAALKT
>gnl|CDD|181900 PRK09487, sdhC, succinate dehydrogenase cytochrome b556 subunit
MIRNVKKQRPVNLDLQTIRFPITAIASILHRVSGVITFVAVGILLWLLGTSLSSPEGFEQAAAIMDSFFV
KFIMWGILTALAYHVVVGIRHLLMDFGYLEETLEAGKRSAKISFVITVVLSLLAGVLVW
>gnl|CDD|181901 PRK09488, sdhD, succinate dehydrogenase membrane anchor subunit
MVSNASALGRNGVHDFILVRATAIVLTLYIIYMVGFFATSGELTYEVWRGFFASAFTKVFTLLALFSILI
HAWIGMWQVLTDYVKPLALRLMLQLVIVVALVVYVIYGFVVVWGV
>gnl|CDD|181902 PRK09489, rsmC, 16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC
MSALTPASEVLLRHSDDFEQRRVLFAGDLQDDLPAQLDAASVRVHTQQFHHWQVLSRQMGDNARFSLVAT
AEDVADCDTLIYYWPKNKQEAQFQLMNLLSLLPVGTDIFVVGENRSGVRSAEKMLADYAPLNKIDSARRC
GLYHGRLEKQPVFDADKFWKEYQVDGLTVKTLPGVFSRDGLDVGSQLLLSTLTPHTKGKVLDVGCGAGVL
SAVLARHSPKIRLTLSDVSAAALESSRATLAANGLEGEVFASNVFSDIKGRFDMIISNPPFHDGIQTSLD
AAQTLIRGAVRHLNSGGELRIVANAFLPYPDLLDETFGSHEVLAQTGRFKVYRAIMTRQAKK
>gnl|CDD|236539 PRK09490, metH, B12-dependent methionine synthase; Provisional
PNDMSSRLAQLRALLAERILVLDGAMGTMIQRYKLEEADYRGERFADWPCDLKGNNDLLVLTQPDVIEAI
HRAYLEAGADIIETNTFNATTIAQADYGMESLVYELNFAAARLAREAADEWTAKTPDKPRFVAGVLGPTN
RTASISPDVNDPGFRNVTFDELVAAYREQTRGLIEGGADLILIETIFDTLNAKAAIFAVEEVFEELGVRL
PVMISGTITDASGRTLSGQTTEAFWNSLRHAKPLSIGLNCALGADELRPYVEELSRIADTYVSAHPNAGL
PNAFGEYDETPEEMAAQIGEFAESGFLNIVGGCCGTTPEHIAAIAEAVAGLPPRKLPEIPVACRLSGLEP
LNIDDDSLFVNVGERTNVTGSAKFARLIKEEDYDEALDVARQQVENGAQIIDINMDEGMLDSEAAMVRFL
NLIASEPDIARVPIMIDSSKWEVIEAGLKCIQGKGIVNSISLKEGEEKFIEHARLVRRYGAAVVVMAFDE
QGQADTRERKIEICKRAYDILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEATRWIKQNLPHAK
ISGGVSNVSFSFRGNNPVREAIHAVFLYHAIKAGMDMGIVNAGQLAIYDDIPPELREAVEDVVLNRRPDA
TERLLEIAEKYRGKGGKKAKAEDLEWRSWPVEKRLEHALVKGITEFIEEDTEEARQQAARPLEVIEGPLM
DGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFIEAKKEGGTDRKSNGKILMATVKGDVHDIGKNI
VGVVLQCNNYEVIDLGVMVPAEKILETAKEENADIIGLSGLITPSLDEMVHVAKEMERQGFTIPLLIGGA
TTSKAHTAVKIAPNYSGPVVYVTDASRAVGVVSSLLSDEQRDAYVAETRAEYEKVREQHARKKPRKPLLT
LEAARANRFKIDWEAYTPPKPKFLGVQVFEDYDLAELREYIDWTPFFQTWELAGKYPAILEDEVVGEEAR
KLFADAQAMLDKIIAEKWLTARGVIGLFPANSVGDDIEVYTDESRTEVLATLHHLRQQTEKRGRPNYCLA
DFVAPKESGKADYIGAFAVTAGLGEDELADRFEAAHDDYNAIMVKALADRLAEAFAEYLHERVRKEFWGY
APDENLSNEELIREKYQGIRPAPGYPACPDHTEKATLFDLLDAEKNTGMKLTESYAMWPGASVSGWYFSH
PESKYFAVGKIGRDQVEDYAARKGMSVEEVERWLAPNLG
>gnl|CDD|181904 PRK09491, rimI, ribosomal-protein-alanine N-acetyltransferase; Provisional
MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIA
VDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADGREDAI
IMALPL
>gnl|CDD|181906 PRK09493, glnQ, glutamine ABC transporter ATP-binding protein GlnQ
MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKV
DERLIRQEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGG
QQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFID
KGRIAEDGDPQVLIKNPPSQRLQEFLQHVS
>gnl|CDD|181907 PRK09494, glnP, glutamine ABC transporter permease protein; Reviewed
MQFDWSAIWPAIPLLLEGAKMTLWISVLGLAGGLVIGLLAGFARAYGGWIANHIALVFIELIRGTPIVVQ
VMFIYFALPMAFNDLRIDPFTAAVVTIMINSGAYIAEITRGAVLSIHKGFREAGLALGLSRRETLRYVIG
PLALRRMLPPLGNQWIISIKDTSLFIVIGVAELTRQGQEIIAGNFRALEIWSAVAVIYLIITLVLSFILR
RLERRMKIL
>gnl|CDD|236540 PRK09495, glnH, glutamine ABC transporter periplasmic protein; Reviewed
MKSVLKVSLAALTLAFAVSSHAADKKLVVATDTAFVPFEFKQGDKYVGFDIDLWAAIAKELKLDYTLKPM
DFSGIIPALQTKNVDLALAGITITDERKKAIDFSDGYYKSGLLVMVKANNNDIKSVKDLDGKVVAVKSGT
GSVDYAKANIKTKDLRQFPNIDNAYLELGTGRADAVLHDTPNILYFIKTAGNGQFKAVGDSLEAQQYGIA
FPKGSELREKVNGALKTLKENGTYAEIYKKWFGTEPK
>gnl|CDD|236541 PRK09496, trkA, Trk system potassium transporter TrkA
MKIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDVRTVVGNGSSPDVLREAGAEDADLLI
AVTDSDETNMVACQIAKSLFGAPTTIARVRNPEYAEYDKLFSKEALGIDLLISPELLVAREIARLIEYPG
ALDVEEFADGRVQLVEVKVYEGSPLVGKPLSDLREHFPDIDVRVVAIFRGGRLIIPRGDTVIEAGDEVYF
IGAREHIRAVMSEFGRLEKPVKRVMIVGGGNIGYYLAKLLEKEGYSVKLIERDPERAEELAEELPNTLVL
HGDGTDQELLEEEGIDEADAFIALTNDDEANILSSLLAKRLGAKKVIALVNRPAYVDLVEGLGIDIAISP
RQATASEILRHVRRGDIVAVHSLRRGAAEAIEAVAHETSKVVGKPLKDLKLPKGVLIGAIVRGGEVIIPT
GDTVIEPGDHVIVFVLDKKFVPDVEKLFQVSPF
>gnl|CDD|181910 PRK09497, potB, spermidine/putrescine ABC transporter membrane protein; Reviewed
MKNTSKFQNVVIVTIVGWLVLFVFLPNLMIIGTSFLTRDDANFVKMVFTLDNYTRLLDPLYAEVLLHSLN
MALIATLACLVLGYPFAWFLAKLPHKVRPLLLFLLIVPFWTNSLIRIYGLKIFLSTKGYLNEFLLWLGVI
DTPIRIMFTESAVIIGLVYILLPFMVLPLYSSIEKLDKPLLEAARDLGANKLQTFIRIIIPLTMPGIIAG
CLLVLLPAMGMFYVSDLLGGAKNLLIGNVIKSQFLNIRDWPFGAATSITLTIVMGLMLLVYYRASKLLNK
KVELE
>gnl|CDD|181911 PRK09498, sifA, type III secretion system effector SifA
MPITIGNGFLKSEILTNSPRNTKEAWWKVLWEKIKDFFFSTGKAKADRCLHEMLFADRAPTRERLTEIFF
ELKELACASQRDRFQVHNPHENDATIILRIMDQNEENELLRITQNTDTFSCEVMGNLYFLMKDRPDILKS
HPQMTAMINRRYSEIVDYPLPSTLCLNPAGAPILSVPLDNIEGYLYSELRKGNLDGWKTQEKATYLAAKI
QSGIEKTTRILHHANISESTQQNAFLETMAMCGLKQLEIPPPHTHIPIEKMVKEVLLADKTFQAFLVTDP
STSQSMLAEIVEAISDQVFHAIFRIDPQAIQKMAEEQLTTLHVRSEQQSGCLCCFL
>gnl|CDD|137339 PRK09499, sifB, type III secretion system effector SifB
MPITIGRGFLKSEMFSQSAISQRSFFTLLWEKIKDFFCDTQRSTADQYIKELCDVASPPDAQRLFDLFCA
LYELSSPSCRGNFHFQHYKDAECQYTNLCIKDGEDIPLCIMIRQDHYYYEIMNRTVLCVDTQSAHLKRYS
DINIKASTYVCEPLCCLFPERLQLSLSGGITFSVDLKNIEETLIAMAEKGNLCDWKEQERKAAISSRINL
GIAQAGVTAIDDAIKNKIAAKVIENTNLKNAAFEPNYAQSSVTQIVYSCLFKNEILMNMLEESSSHGLLC
LNELTEYVALQVHNSLFSEDLSSLVETTKNEAHHQS
>gnl|CDD|236542 PRK09500, potC, spermidine/putrescine ABC transporter membrane protein; Reviewed
MGRLLRGGFMTLVYAYLYIPIIILIVNSFNSSRFGINWKGFTTKWYELLFNNDSLLQAAQHSLTMAVFSA
TFATLIGSLTAVALYRYRFRGKKFVSGMLFVVMMSPDIVMAISLLVLFMLLGIQLGFWSLLFAHITFCLP
FVVVTVYSRLKGFDVRMLEAAKDLGASEFTILRKIILPLALPAVAAGWLLSFTLSLDDVVVSSFVTGPSY
EILPLKIYSMVKVGVSPEVNALATILLVLSLVLVILSQLLARDKTK
>gnl|CDD|181913 PRK09501, potD, spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
MKKWSRHLLAAGALALGMSAAHADDNNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYESNETMYAKLK
TYKDGAYDLVVPSTYYVDKMRKEGMIQKIDKSKLTNFSNLDPDMLNKPFDPNNDYSIPYIWGATAIGVNS
DAIDPKSVTSWADLWKPEYKGSLLLTDDAREVFQMALRKLGYSGNTTDPKEIEAAYNELKKLMPNVAAFN
SDNPANPYMEGEVNLGMIWNGSAFVARQAGTPIDVVWPKEGGIFWMDSLAIPANAKNKEGALKLINFLLR
PDVAKQVAETIGYPTPNLAARKLLSPEVANDKSLYPDAETIKKGEWQNDVGAASSIYEEYYQKLKAGR
>gnl|CDD|181914 PRK09502, iscA, iron-sulfur cluster assembly protein IscA
MSITLSDSAAARVNTFLANRGKGFGLRLGVRTSGCSGMAYVLEFVDEPTPEDIVFEDKGVKVVVDGKSLQ
FLDGTQLDFVKEGLNEGFKFTNPNVKDECGCGESFHV
>gnl|CDD|181915 PRK09504, sufA, iron-sulfur cluster assembly scaffold protein; Provisional
MDMHSGTFNPDDFAWQGLTLTPAAAAHIRELMAKQPGMKGVRLGVKQTGCAGFGYVLDSVSEPDKDDLVF
EHDGAKLFVPLQAMPFIDGTEVDYVREGLNQIFKFHNPKAQNECGCGESFGV
>gnl|CDD|236543 PRK09505, malS, alpha-amylase; Reviewed
MKLSALALTLLPGPAVAASWTSPGFPAFSEQGTGTFVSHAQLTKGTYPLTLNFDQQCWQPAGAIKLNQML
SLQPCSGTPPQWRLFRDGDYTLQIDTRSGTPTLMLSIKNAAESPVANLTRQCPVWDGGPVTVDVSDTFAE
GTVVRDAYSGQIATVKNGKITLTPAAHSGGLLLLERAETEAAAPFDWHNATVYFVLTDRFENGDPSNDHS
YGRHKDGMQEIGTFHGGDLRGLTEKLDYLQQLGVNALWISSPLEQIHGWVGGGTKGDFPHYAYHGYYTLD
WTKLDANMGTEADLRTLVDEAHQRGIRILFDVVMNHTGYATLADMQEFQFGALYLSGDENKKTLGERWSD
WQPAAGQNWHSFNDYINFSDSTAWDKWWGKDWIRTDIGDYDNPGFDDLTMSLAFLPDIKTESTQASGLPV
FYANKPDTRAKAIDGYTPRDYLTHWLSQWVRDYGIDGFRVDTAKHVELPAWQQLKQEASAALAEWKKANP
DKALDDAPFWMTGEAWGHGVMKSDYYRHGFDAMINFDYQEQAAKAVDCLAQMDPTYQQMAEKLQDFNVLS
YLSSHDTRLFFEGGQSYAKQRRAAELLLLAPGAVQIYYGDESARPFGPTGSDPLQGTRSDMNWQEVSGKS
AALLAHWQKLGQFRARHPAIGAGKQTTLSLKQYYAFVREHGDDKVMVVWAGQQ
>gnl|CDD|236544 PRK09506, mrcB, bifunctional glycosyl transferase/transpeptidase; Reviewed
MAGNDREPIGRKGKPSRPVKQKVSRRRYRDDDDYDDYDDYEDEEPMPRKGKGKGRKPRGKRGWLWLLLKL
FIVFAVLIAIYGVYLDQKIRSRIDGKVWQLPAAVYGRMVNLEPGMSYSKNEMVKLLEATQYRQVSKMTRP
GEFTVQANSIEMIRRPFDFPDSKEGQVRARLTFDGDRLATIVNLDNNRQFGFFRLDPRLITMLQSPNGEQ
RLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGGSTLTQQLVKNLFLSNER
SLWRKANEAYMALIMDARYSKDRILELYLNEVYLGQSGDDQIRGFPLASLYYFGRPVEELSLDQQALLVG
MVKGASLYNPWRNPKLALERRNLVLRLLQQQQIIDQELYDMLSARPLGVQPKGGVISPQPAFMQMVRQEL
QAKLGDKVKDLSGVKIFTTLDPVSQDAAEKAVEEGIPALKKQRKLSDLETAMVVVDRFSGEVRAMVGGSE
PQFAGYNRAMQARRSIGSLAKPATYLTALSQPDKYRLNTWIADAPISLRQPNGQVWSPQNDDRRFSGRVM
LVDALTRSMNVPTVNLGMALGLPAVTDTWIKLGVPKDQLNPVPAMLLGALNLTPIEVAQAFQTIASGGNR
APLSALRSVIAEDGKVLYQSFPQAERAVPAQAAYLTLYTMQQVVQRGTGRQLGAKYPNLHLAGKTGTTND
LVDSWFAGIDGKEVTITWVGRDNNQPTKLYGASGAMTIYQRYLENQTPTPLNLTPPEDIVDMGVDYDGNF
VCGSGGMRVLPVWTDDPQSLCQQSEMQQQPSQPQQQPQQQPAEQKDSDGVAGWIKDMFGQ
>gnl|CDD|169931 PRK09507, cspE, cold shock-like protein CspE
MSKIKGNVKWFNESKGFGFITPEDGSKDVFVHFSAIQTNGFKTLAEGQRVEFEITNGAKGPSAANVIAL
>gnl|CDD|181918 PRK09508, leuO, leucine transcriptional activator; Reviewed
MPEVQTDHAETKESSEPQLRMVDLNLLTVFDAVMQEQNITRAAHNLGMSQPAVSNAVARLKVMFNDELFV
RYGRGIQPTARARQLFGPVRQALQLVQNELPGSGFEPESSERVFNLCICSPLDIRLTSQIYNRIEQIAPN
IHVVFKSSLNQNIEHQLRYQETEFVISYEEFDRPEFTSVPLFKDELVLVASKNHPRIKGPITEEQLYNEQ
HAVVSLDRFASFSQPWYDTVDKQASIAYQGTALSSVLNVVSQTHLVAIAPRWLAEEFAESLELQILPLPL
KNNSRTCYLSWHESAGRDKGHQWMEELLVSICKR
>gnl|CDD|181919 PRK09509, fieF, CDF family cation-efflux pump FieF
MNQSYARLVSRAAIAATAMASLLLLIKIFAWWYTGSVSLLAALVDSLVDIAASLTNLLVVRYSLQPADDE
HTFGHGKAESLAALAQSMFISGSALFLFLTGIQHLISPTPMNDPGVGIIVTLVALICTLILVTFQRWVVR
KTQSQAVRADMLHYQSDVMMNGAILLALGLSWYGWHRADALFALGIGIYILYSALRMGYEAVQSLLDRAL
PDEERQEIIDIVTSWPGVSGAHDLRTRQSGPTRFIQLHLEMEDNLPLVQAHMIADQVEQALLRRFPGSDV
IIHQDPCSVVPREGKRSWL
>gnl|CDD|236545 PRK09510, tolA, cell envelope integrity inner membrane protein TolA; Provisional
MSKATEQNDKLKRAIIISVVLHIILFALLIWSSFDENIEASGGGGGGSVIDAVMVDPGAVVEQYNRQQQQ
QKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAK
AAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK
AAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLDSGKNAPKTGGGAK
GNGAQGAGAGNGKKGGASGADIDQYAGQIKSAIQSKFYDASSYAGKTCTLRIKLAPDGTLLDIKKEGGDP
ALCQAALAAAKTAKIPKPPSQEVYEKFKNAPLDFKPQ
>gnl|CDD|181921 PRK09511, nirD, nitrite reductase small subunit NirD
MSQWKDICKIDDILPGTGVCALVGDEQVAIFRPYHDEQVFAISNIDPFFQASVLSRGLIAEHQGELWVAS
PLKKQRFRLSDGLCMEDEQFSVKHYDARVKDGVVQLRA
>gnl|CDD|181922 PRK09512, rbsC, ribose ABC transporter permease protein; Reviewed
TTQTVSGRRYFTKAWLIEQKSLIALLVLIAIVSTLSPNFFTVNNLFNILQQTSVNAIMAVGMTLVILTSG
IDLSVGSLLALTGAVAASIVGIEVNALVAVPAALALGAAIGAVTGVIVAKGKVQAFIATLVMMLLLRGVT
MVYTDGSPINTGFTDNADLFGWFGIGRPLGIPTPVWIMAIVFLAAWYMLHHTRLGRYIYALGGNEAATRL
SGINVNKVKIIVYALCGLLAALAGIIEVARLSSAQPTAGTGYELDAIAAVVLGGTSLAGGKGRIVGTLIG
ALILGFLNNGLNLLGVSSYYQMIVKAVVILLAVLVDNKKQ
>gnl|CDD|181923 PRK09513, fruK, 1-phosphofructokinase; Provisional
MSRRVATITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGF
QQLFSELGIANRFQVVQGRTRINVKLTEKDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVAVSGS
LPRGVSPEAFTDWMTRLRSQCPCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPELKDVIEAAH
ALREQGIAHVVISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATA
VSALAVSQSNVGITDRPQLAAMMARVDLTPFN
>gnl|CDD|181924 PRK09514, zntR, Zn(2+)-responsive transcriptional regulator
MYRIGELAKLAEVTPDTLRFYEKQGLMDPEVRTEGGYRLYTEQDLQRLRFIRRAKQLGFTLEEIRELLSI
RLDPEHHTCQEVKGIVDEKLAEVEAKIAELQHMRRSLQRLNDACCGTAHSAVYCSILEALEQGASGVKSG
>gnl|CDD|169939 PRK09517, PRK09517, multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional
MTDFSLYLVTDPVLGGGPEKVAGIVDSAISGGVSVVQLRDKNAGVEDVRAAAKELKELCDARGVALVVND
RLDVAVELGLHVHIGQGDTPYTQARRLLPAHLELGLTIETLDQLEAVIAQCAETGVALPDVIGIGPVAST
ATKPDAPPALGVDGIAEIAAVAQDHGIASVAIGGVGLRNAAELAATGIDGLCVVSAIMAAANPAAAAREL
RTAFQPTRSPETQTELSQTELQGAFVNSPSAPRVLSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALV
AQNTHGVNTIHTPPLTFLEEQLEAVFSDVTVDAVKLGMLGSADTVDLVASWLGSHEHGPVVLDPVMVATS
GDRLLDADATEALRRLAVHVDVVTPNIPELAVLCGEAPAITMDEAIAQARGFARTHGTIVIVKGGHLTGD
LADNAVVRPDGSVHQVENPRVNTTNSHGTGCSLSAALATLIAAGESVEKALEWATRWLNEALRHADHLAV
GSGNGPVDHGHLARRLTHAAETTPWAHLRAGATAASFTTPSTVKSPAPRIEPAGPFTRALWEASGDIIAE
INDSDFIRMLGDGTLRRPEFDFYIDQDAQYLRQYSRALARLSSIAPDSHAQVEWAQSAAECIVVEAELHR
SYLSGKEAPSAPSPVTMAYTDFLIARTYTEDYVVGVAAVLPCYWLYAEIGLMLAEQNHDEHPYKDWLNTY
SGEEFIAGTRAAIARVEKALENAGPEQRVDAARAFLSASVHEREFFDQATRHGWT
>gnl|CDD|236546 PRK09518, PRK09518, bifunctional cytidylate kinase/GTPase Der; Reviewed
MIIVAIDGPAGVGKSSVSRALAQYLGYAYLDTGAMYRACAWWCLKQGIDLDAELVDEQVVTEAVGEFFTG
LHFDISVDPDSPGVFADGEDISEEIRSPEVSSHVSAVAAIPPVRNVLIAAQRAYIAREASADSFSGGLGI
VAEGRDITTVVAPDAEVRILLTAREEVRQARRSGQDRSETPGVVLEDVAARDEADSKVTSFLSAADGVTT
LDNSDLDFDETLDLLIGLVEDAIEEQEYDQYAANLEGYELDEGDEDLLEGSGFVAGDEKAGPKAVGVVAI
VGRPNVGKSTLVNRILGRREAVVEDTPGVTRDRVSYDAEWAGTDFKLVDTGGWEADVEGIDSAIASQAQI
AVSLADAVVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKIDDQASEYDAAEFWKLGLGEPYPISAMH
GRGVGDLLDEALDSLKVAEKTSGFLTPSGLRRVALVGRPNVGKSSLLNQLTHEERAVVNDLAGTTRDPVD
EIVEIDGEDWLFIDTAGIKRRQHKLTGAEYYSSLRTQAAIERSELALFLFDASQPISEQDLKVMSMAVDA
GRALVLVFNKWDLMDEFRRQRLERLWKTEFDRVTWARRVNLSAKTGWHTNRLAPAMQEALESWDQRIPTG
KLNAFLGKIQAEHPHPLRGGKQPRILFATQASTRPPRFVIFTTGFLEHGYRRFLERSLREEFGFEGSPIQ
ISVNIREKKKRK
>gnl|CDD|77219 PRK09519, recA, intein-containing recombinase RecA
MTQTPDREKALELAVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPES
SGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALD
IVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETT
TGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNKCLAEGTRIFDPVTGTTHRIEDVVDGRKPI
HVVAAAKDGTLHARPVVSWFDQGTRDVIGLRIAGGAIVWATPDHKVLTEYGWRAAGELRKGDRVAQPRRF
DGFGDSAPIPADHARLLGYLIGDGRDGWVGGKTPINFINVQRALIDDVTRIAATLGCAAHPQGRISLAIA
HRPGERNGVADLCQQAGIYGKLAWEKTIPNWFFEPDIAADIVGNLLFGLFESDGWVSREQTGALRVGYTT
TSEQLAHQIHWLLLRFGVGSTVRDYDPTQKRPSIVNGRRIQSKRQVFEVRISGMDNVTAFAESVPMWGPR
GAALIQAIPEATQGRRRGSQATYLAAEMTDAVLNYLDERGVTAQEAAAMIGVASGDPRGGMKQVLGASRL
RRDRVQALADALDDKFLHDMLAEELRYSVIREVLPTRRARTFDLEVEELHTLVAEGVVVHNCSPPFKQAE
FDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEGEQLGQGKENARNFLVENADVADEIEKKIKEKLGI
GAVVTDDPSNDGVLPAPVDF
>gnl|CDD|236547 PRK09521, PRK09521, exosome complex RNA-binding protein Csl4; Provisional
MVKQGDLVLPGDYLAVIEEYLPGEGTYEDNGEVYASVVGKVFIDDINRKISVIPFKKTPPLLKKGDIVYG
RVVDVKEQRALVRIVSIEGSERELATSKLAYIHISQVSDGYVESLTDAFKIGDIVRAKVISYTDPLQLST
KGKDLGVIYAMCSRCRTPLVKKGENELKCPNCGNIETRKLSSYYGKGGI
>gnl|CDD|181927 PRK09522, PRK09522, bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD
MADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPEL
LTRLRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNI
PAGLTINAHFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPTNTLQPILEKLYQA
QTLSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPDYLFADIVGTG
GDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFA
PKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGG
MDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKGDAAHEAAVAA
NVAMLMRLHGHEDLQANAQTVLEVLRSGSAYDRVTALAARG
>gnl|CDD|236548 PRK09525, lacZ, beta-galactosidase
MTMIMDSLAQILARRDWENPGVTQLNRLPAHPPFASWRNSEAARDDRPSQQRQSLNGEWRFSYFPAPEAV
PESWLECDLPDADTIPVPSNWQLHGYDAPIYTNVTYPIPVNPPFVPEENPTGCYSLTFTVDESWLQSGQT
RIIFDGVNSAFHLWCNGRWVGYSQDSRLPAEFDLSPFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGIF
RDVSLLHKPTTQLSDFHITTELDDDFRRAVLEVEAQVNGELRDELRVTVQLWDGETLVASGTAPFGTEII
DERGAYADRVTLRLNVENPKLWSAETPNLYRAVVSLLDADGTLIEAEAYDVGFRKVEIENGLLKLNGKPL
LIRGVNRHEHHPEHGQVMDEETMVQDILLMKQHNFNAVRCSHYPNHPLWYELCDRYGLYVVDEANIETHG
MVPMNRLSDDPRWLPAMSERVTRMVQRDRNHPSIIIWSLGNESGHGANHDALYRWIKSNDPSRPVQYEGG
GADTAATDIICPMYARVDEDQPFPAVPKWSIKKWISLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQY
PRLQGGFIWDWVDQGLTKYDENGNPWWAYGGDFGDTPNDRQFCMNGLVFPDRTPHPALYEAKHAQQFFQF
SLLSTTPLTIEVTSEYLFRHSDNELLHWSVALDGKPLASGEVPLDLAPQGSQRITLPELPQPESAGQLWL
NVEVVQPNATAWSEAGHRSAWQQWRLPEPLSLPLPTASHAAPQLTQDEQDFCIELGNQRWQFNRQSGLLS
QWWVGGKEQLLTPLRDQFTRAPLDNDIGVSEATRIDPNAWVERWKAAGLYQLEARLLQCDADTLADAVLI
TTEHAYQHQGKTLFISRKTYRIDGQGEMTIDVDVEVASDLPPPARIGLTCQLAQVAERVSWLGLGPHENY
PDRLLAACFGRWDLPLSDMHTPYIFPSENGLRCGTRELNYGRHQIRGDFHFNISRYSQQQLMETSHRHLL
QAEEGTWLNIDGFHMGVGGDDSWSPSVHPEFLLSAGRYHYQLTWCQK
>gnl|CDD|181929 PRK09526, lacI, lac repressor; Reviewed
MKSKPVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLAT
TSLALHAPSQIAAAIKSRADQLGYSVVISMVERSGVEACQAAVNELLAQRVSGVIINVPLEDADAEKIVA
DCADVPCLFLDVSPQSPVNSVSFDPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDY
QLQPIAVREGDWSAMSGYQQTLQMLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTED
SSYFIPPLTTIKQDFRLLGKEAVDRLLALSQGQAVKGSQLLPTSLVVRKSTAPPNTQTASPQ
>gnl|CDD|181930 PRK09527, lacA, galactoside O-acetyltransferase; Reviewed
MNMSMTERIKAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVGENAWVEPPVYF
SYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWI
GSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREINDRDKQYYFKDYKVESSV
>gnl|CDD|236549 PRK09528, lacY, galactoside permease; Reviewed
MATMYYLKNPNYWIFSLFFFFFFFIWSSWFSFFPIWLHDINGLSGTDTGIIFSANSLFALLFQPLYGLIS
DKLGLKKHLLWIISGLLVLFGPFFIYVFAPLLQYNILLGAIVGGIYLGFGFLAGAGAIEAYIERVSRRSG
FEYGRARMWGSLGWALCAFIAGILFNINPQINFWLGSGSALILLVLLFFAKPDAPSTAKVANALGANASA
VSLKDALALLKLPKFWFLVLYVIGVACFYDVFDQQFPNFFASFFATPEQGTRVFGYLNSFQVFLEALIMF
FAPFIINRIGAKNALLLAGTIMAVRIIGSGFATGPLEVSILKLLHAFEVPFLLVGVFKYITLNFDVRLSA
TIYLVGFQFAKQLGAVFLSTLAGNLYDSIGFQGTYLILGGIVLLFTLISVFTLSGDRELSLLRRQVPEAA
>gnl|CDD|236550 PRK09529, PRK09529, bifunctional acetyl-CoA decarbonylase/synthase complex subunit alpha/beta; Reviewed
MSKKVAEAAITGAITALSAAEGLLKQALAKYGPDTKVGFPNTAYYLPVIYGLTGIKVETLGDLEPVLNKC
RKLLPPEPYLENALDAGLATLIAAEIIEALRYLKQPEPYTETPWTGFIDDPILRKLGVELVDGTIPGFAV
IVGAAPDSEKAKKIIKELQKKNLLTFLCGEVIEQLIEAGVKLGLDYRLVPLGDDITSAIHAANFAIRAAL
IFGGVEPGDYEELLDYTKERVPAFVNALGELDDEWVAAAAGAINLGFPVITDQDVPEGICVPEWVLSEPD
YDKIVQKALEVRGIKVTVTEIPIPVSFGPAFEGERVRKEDMYVEFGGGRTPAFELVRMADMDEVEDGKIE
VIGPDIDEVEEGSRLPLGIVVEVAGRKMQEDFEPVLERRIHHFLNYIEGVMHIGQRDIAWVRISKDAFEK
GFRLKHIGEILYAKFKQEFPSIVDKVQVTLYTDPEKVLELLEKARAIYKKRDERLKGLTDEDVDTFYSCT
LCQSFAPTHVCVVTPERPGLCGAVSWLDAKAAYEINPTGPNQPIPKGECLDEKLGQWSGVNEFVRKASQG
AVERVNLYSIMEDPMTSCGCFEAIAAILPECNGFMVVNREYSGMTPCGMTFSTLAGTIGGGVQTPGFMGI
SKSYITSRKFIQADGGIARLVWMPKELKEELKDRLNARAKEEGLPDFYDKIADETVGTTEEEILPFLEEK
GHPALTMEPLI
>gnl|CDD|181933 PRK09532, PRK09532, DNA polymerase III subunit alpha; Reviewed
MSFVGLHIHSDYSLLDGASQLPALVDRAIELGMPAIALTDHGVMYGAIELLKVCRNKGIKPIIGNEMYVI
NGDIEKQKRRRKYHQVVLAKNTQGYKNLVKLTTISHLQGVQGKGIFARPCINKELLEQYHEGLIVTSACL
GGEIPQAILSGRPDAARKVAKWYKKLFGDDFYLEIQDHGSQEDRIVNVEIVKIARELGIKIIATNDSHFI
SCYDVEAHDALLCIQTGKLITEDKRLRYSGTEYLKSAEEMRLLFRDHLPDDVIAEAIANTLEVADKIEPY
NILGEPRIPNYPVPSGHTPDTYVEEVAWQGLLERLNCKSRSEVEPVYKERLEYELKMLQQMGFSTYFLVV
WDYIKYARDNNIPVGPGRGSAAGSLVAYCLKITNIDPVHHGLLFERFLNPERKSMPDIDTDFCIERRDEM
IKYVTEKYGEDRVAQIITFNRMTSKAVLKDVARVLDIPYGEADKMAKLIPVSRGKPTKLKVMISDETPEP
EFKEKYDNDPRVRRWLDMAIRIEGTNKTFGVHAAGVVISSEPLDEIVPLQKNNDGAVITQYFMEDLESLG
LLKMDFLGLRNLTTIQKTADLIKENRGVEIDLDQLPLDERKALKILAKGEAKKLPKDVQKTHKLLERGDL
EGIFQLESSGMKQIVRDLKPSNIEDISSILALYRPGPLDAGLIPKFINRKHGREPIDYEHQLLEPILNET
YGVLVYQEQIMKMAQDLAGYSLGEADLLRRAMGKKKISEMQKHREKFIDGAAKNGVSKKVAENLFDQMVK
FAEYCLSYDTEVLTVEYGLLPIGKIVEENIECTVYSVDPNGFVYTQPIAQWHHRGEQEVFEYCLEDGSII
RATKDHKFMTTDGEMLPIDEIFERGLELKQIKLP
>gnl|CDD|236551 PRK09533, PRK09533, bifunctional transaldolase/phosoglucose isomerase; Validated
MNPLKALAQHGQSVWLDFLARGFIAKGELKRLVEEDGLRGVTSNPAIFEKAIGSSDEYDDAIKAALAEGD
RSVIELYETLAIEDIQAAADVLRPVYDATDGADGFVSLEVSPYLALDTEGTIAEARRLWAAVDRPNLMIK
VPATPEGLPAIRQLIAEGINVNVTLLFSQDVYEEVAEAYISGLEARAAKGGDPSHVASVASFFVSRIDSA
VDKRLDEKIAAANDPAEKAALEALKGKVAIANAKLAYQRYKRLFAGPRWEALAAKGAKPQRLLWASTGTK
NKAYSDVLYVEELIGPDTVNTMPPATLDAFRDHGKVRATLEEDVDEARAVLADLAEAGISLDAVTDKLVA
EGVQLFADAFDKLLGAVAEKREALLGGRLDRQTLSLGADLAKAVAAALEAWRADGKIRRLWARDASVWTG
ADEAKWLGWLDIVEDELAHLAEYEAFAEEVRAEGFTDAVVLGMGGSSLGPEVLAETFGQRDGFPKLHVLD
STDPAQVRALEAAVDLARTLFIVSSKSGGTLEPNIFKDYFFARVKEVLGAKAGRHFVAVTDPGSSLEKVA
KEDGFRKIFHGDPDIGGRYSVLSPFGLVPAAAAGIDVRALLDSALAMVRSCGPSVPPADNPGVQLGLALG
VAATQGRDKVTIVASPAIADFGAWAEQLIAESTGKEGKGLIPIDGEPLGDPAVYGNDRVFVYLRLAGEAD
AAQDAALAALEAAGHPVVRIVLDSAEQLGQEFFRWEMATAVAGAVLGINPFDQPDVEASKIKTRELTAAY
EKTGALPAETPAASDGGLALYTDAANAAALREGADGTLESWLKAHLGRVKAGDYVALLAYIERNPAHIAA
LQAIRLAVRDARKVATCLEFGPRFLHSTGQAYKGGPDSGVFLQITADDAADLPVPGQKYSFGVVKAAQAR
GDFDVLTERGRRALRVHLKGDLKSGLKALAAAIRAALA
>gnl|CDD|236552 PRK09534, btuF, corrinoid ABC transporter substrate-binding protein; Reviewed
MHRMRFRSLVIVALAVTMTAAGGALAPAPAAQHADADRACSFPVTETDATGTEITLDERPERVVTLNPSA
AQTMWELGARDRVVGVTQYASYLDGAEERTNVSGGQPFGVNVEAVVGLDPDLVLAPNAVAGDTVTRLREA
GITVFHFPAATSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRPRVLYPLGDGYTA
GGNTFIGALIEAAGGHNVAADATTDGYPQLSEEVIVQQDPDVIVVATASALVAETEPYASTTAGETGNVV
TVNVNHINQPAPRIVESMATMATAFHNTTTNDTLDAQPSATTTATSTAPPTDATDGTAPGFGVAAALAAL
LGAALIARR
>gnl|CDD|236553 PRK09535, btuC, cobalamin ABC transporter permease BtuC
MRVSGRAVAWSAGLTALLVAVVLVSAAIGPVRIPPRTVAMALLNAVAVPVGVAVTTHGVPVLSVGLSLPA
PDLEYASPFSFAVPETAQTIVLQIRLPRILLAATVGFALAAAGTVMQGFFRNPMADPSIIGVSSGAAVGA
VAAIVLPLAVPFGLQAAAFAGALVAAFGVYAIATENGRTPVATLLLAGVAVQTFLGAVISYLLLHSGESL
RRAVYWLMGHLHGSTWSDVEVALPVVVVGFVVLLAYARDLNVLLLGEEDAHTLGIEVERTKRLLLALASV
VTAAAVAVAGVIGFVGLIVPHVMRLLVGPDHRILLPTSALAGASFLVATDTVARSGPAEVPVGIVTAALG
APFFLYLLRTREVHAL
>gnl|CDD|236554 PRK09536, btuD, corrinoid ABC transporter ATPase; Reviewed
MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL
SARAASRRVASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSL
SGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELV
LLADGRVRAAGPPADVLTADTLRAAFDARTAVGTDPATGAPTVTPLPDPDRTEAAADTRVHVVGGGQPAA
RAVSRLVAAGASVSVGPVPEGDTAAETAARVGCEAVTVPPFKPIEDSTRAEATDLIIAADAVVAAGVAAA
ARSGVIGLLAGNAPTLTVTDAAAAPEWADDTVDCTALVDAVRALTDDTADDV
>gnl|CDD|236555 PRK09537, pylS, pyrrolysine--tRNA(Pyl) ligase
MDKKPLDVLISATGVWMSRTGLLHKIKNFEVSRSKIHIEMDCGERLTVRNSRSSRTARALRHHKYRKTCK
RCRVSDEDINRFLTKTFEDKTQVKVKVVSAPTKKKKAMPKSVVRAPKPLENPVPAQAESSGSKPVPSIPV
STPEVKAPAPALTPSQKDRLETLLSPKDKISLNSEKPKFKELESELVSRRKNDLKQMYEEDREDYLGKLE
RDITKFFVDRGFLEIKSPILIPAEYIERMGIDNDTELSKQIFRVDKNFCLRPMLAPGLYNYLRKLDRILP
DPIKIFEIGPCYRKESDGKEHLEEFTMVNFCQMGSGCTRENLENIIDDFLKHLGIDYEIIGDNCMVYGDT
IDIMHGDLELSSAVVGPIPLDREWGIDKPWIGAGFGLERLLKVKHGYKNIKRASRSESYYNGISTNL
>gnl|CDD|236556 PRK09539, PRK09539, tRNA-splicing endonuclease subunit beta; Reviewed
VTIMSEKAETTLEKIYLALSSSKQLPSEIIYLVNWDKVDVFVDLKQRGRKTIDGIDEISLIIKDKENKYT
AMVLIVDENEKVSFKKILDKLHFSKSMNLELYLAIVDKYGDVTYYTLSEIKLSK
>gnl|CDD|137367 PRK09541, emrE, EmrE family multidrug efflux SMR transporter
MNPYIYLGGAILAEVIGTTLMKFSEGFTRLWPSVGTIICYCASFWLLAQTLAYIPTGIAYAIWSGVGIVL
ISLLSWGFFGQRLDLPAIIGMMLICAGVLVINLLSRSAPH
>gnl|CDD|236557 PRK09542, manB, phosphomannomutase/phosphoglucomutase; Reviewed
IKAYDVRGVVGEQIDEDLVRDVGAAFARLMRAEGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIG
LASTDQLYFASGLLDCPGAMFTASHNPAAYNGIKLCRAGAKPVGQDTGLAAIRDDLIAGVPAYDGPPGTV
TERDVLADYAAFLRSLVDLSGIRPLKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPL
DPANLVDLQAFVRETGADIGLAFDGDADRCFVVDERGQPVSPSAVTALVAARELAREPGATIIHNLITSR
AVPELVAERGGTPVRTRVGHSFIKALMAETGAIFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQDRP
LSELMADYQRYAASGEINSTVADAPARMEAVLKAFADRIVSVDHLDGVTVDLGDGSWFNLRASNTEPLLR
LNVEARTEEEVDALVDEVLAIIRAQ
>gnl|CDD|181938 PRK09543, znuB, zinc ABC transporter permease subunit ZnuB
MIELLLPGWLAGIMLACAAGPLGSFVVWRRMSYFGDTLAHASLLGVAFGLLLDVNPFYAVIAVTLLLAGG
LVWLEKRPQLAIDTLLGIMAHSALSLGLVVVSLMSNVRVDLMAYLFGDLLAVTPEDLISIAIGVVIVLAI
LFWQWRNLLSMTISPDLAFVDGVKLQRVKLLLMLVTALTIGVAMKFVGALIITSLLIIPAATARRFARTP
EQMAGVAVLVGMLAVTGGLTFSAFYDTPAGPSVVLCAALLFILSMMKKQAS
>gnl|CDD|181939 PRK09544, znuC, high-affinity zinc transporter ATPase; Reviewed
MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIG
YVPQKLYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ
LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEVVSLH
PEFISMFGPRGAEQLGIYRHHHNHRHDLQGRIVLRRGNDRS
>gnl|CDD|236558 PRK09545, znuA, zinc ABC transporter substrate-binding protein ZnuA
LHKKTLLFAALLAALLGGATQAANAAVVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKR
LQSADLVVWVGPEMEAFLEKPVSKLPENKQVTIAQLPDVKPLLMKGAHDDHHDDDHDHAGHEKSDEDHHH
GEYNMHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFH
DAYGYFEKHYGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGT
LDPLGTNIKLGKDSYSEFLSQLANQYASCLK
>gnl|CDD|181941 PRK09546, zntB, zinc transporter ZntB
IKGSDLNVPDAVYAWQLDGKGGVKPLEDNDVIDEAHPCWLHLDYTHPDSAQWLATTPLLPDNVRDALAGE
STRPRVSRLGEGTLITLRCINGNTDERPDQLVAMRVYITDRLIVSTRHRKVLALDDVVSDLQEGTGPTDC
GGWLVDVCDALTDHASEFIEELHDKIIDLEDNLLDQQIPPRGELALLRKQLIVMRRYMAPQRDVFARLAS
ERLPWMSDDDRRRMQDIADRLGRGLDDLDACIARTAVLADEIASVMAEAMNRRTYTMSLMAMVFLPTTFL
TGLFGVNLGGIPGGGWPFGFSIFCLLLVVLIGGVAWWLKRSKWL
>gnl|CDD|181942 PRK09547, nhaB, sodium/proton antiporter NhaB
MEISLGRAFWKNFLGQSPDWYKLAIIAFLIINPLIFFLVSPFVAGWLLVAEFIFTLAMALKCYPLQPGGL
LAIEAVFIGMTSPEHVYHEIAANLEVLLLLMFMVAGIYFMKQLLLFIFTKLLLSIRSKMLLSLAFCLAAA
FLSAFLDALTVIAVVISVAVGFYGIYHRVASGKGFSEDHDLTDDSHIDELYREDLEQFRAFLRSLMMHAG
VGTALGGVMTMVGEPQNLIIAKQAGWHFGEFFLRMAPVTVPVLICGLLTCLLVEKFRWFGYGAKLPEKVR
QVLQDYDDQERAKRTRQDKAKLIVQALIGVWLIVALALHLAEVGLIGLSVIILATAFTGVTDEHAIGKAF
EEALPFTALLTVFFAVVAVIIDQHLFAPIIQFVLQASEHAQLSLFYIANGLLSSISDNVFVGTVYINEAK
AALESGAISRKQFELLAVAINTGTNLPSVATPNGQAAFLFLLTSALAPLIRLSYGRMVWMALPYTIVLTL
VGLLAVEFTLAPVTEWFYQMGWI
>gnl|CDD|236559 PRK09548, PRK09548, PTS ascorbate-specific subunit IIBC
METLYEIFLNFFSQVIGKAPLLLGLVACIGYLLLKKDTTTIIKGTIKTIVGFMLVQVGAGTLVAGFKPVI
EALSLYHGLTGAVIDPYTSMQATLETMGDNYAWVGYAVLLALFLNILLVVFRRITGIRTIMLTGHIMFQQ
AGLIAVFYHVLGASMWETVIYGAVLMALYWGISSNIMNKPTQQVTGGAGFSIGHQQQVASWIATKIAPKL
GDKEDSVDDLKLPKWLHIFHDSIVATAIVMTVFFGIILLSFGLDNLQIMAGKTHWFIYILETGLKFAVAI
QVIVIGVRMFVAELSESFKGISERVIPNAVLAIDCAAIYAYSPNAVVFGFMWGAIGQFLAVGILIAFNLK
GIDVDAPIIIIPGFIPMFFSNATIGVFANHFGGWKAVMKICFVMGIIEVLGSAWVIQLIANISQGTQFNG
WMGMADWALGFPPILQGLVGSKSAFFFVLLALALVYMIFASKQLRAKEAAAAAGGKTVDQLDGYNLDEEV
INAVQKLISKQDGGKPVRILAVCGQGQGSSMMMKMKIKKYLDKRGIPIIMDSCAVNDYKGKLETIDIIVC
SKHLANEIEFGEGKFVLGVQNMLNPNSFGDELLELIKKNFVL
>gnl|CDD|236560 PRK09549, mtnW, 2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Reviewed
MSGIIATYLIHDDSHDLEKKAEQIALGLTVGSWTDLPHLEQEQLKKHKGNVVHVEELEEHERKGVKRGII
KIAYPLANFSPDLPAILTTTFGKLSLDGEVKLIDLTFSDELKRHFPGPKFGIDGIRNLLGVHDRPLLMSI
FKGVIGRDLDYLKEQLRDQALGGVDLVKDDEILFENALTPFEKRIVAGKEVLQEVYETTGHKTLYAVNLT
GRTFELKEKAKRAAEAGADALLFNVFAYGLDVLQSLAEDPEIPVPIMAHPAVSGAYTPSPLYGISSPLLL
GKLLRYAGADFSLFPSPYGSVALEKEEALAIAKELTEDDDPFKRSFPVPSAGIHPGLVPLLIRDFGKDVV
INAGGGIHGHPNGAQGGGKAFRAAIDAVLQGKPLHEAAEDDENLHSALDIWGNPSVE
>gnl|CDD|236562 PRK09552, mtnX, 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Reviewed
MMSIQIFCDFDGTITNNDNIIAIMKKFAPPEWEELKDDILSQELSIQEGVGQMFQLLPSNLKEEIIQFLL
ETAEIREGFHEFVQFVKENNIPFYVVSGGMDFFVYPLLQGLIPKEQIYCNGSDFSGEYITITWPHPCDEH
CQNHCGCCKPSLIRKLSDTNDFHIVIGDSITDLEAAKQADKVFARDFLITKCEELGIPYTPFETFHDVQT
ELKHLLEVK
>gnl|CDD|181947 PRK09553, tauD, taurine dioxygenase; Reviewed
ERLSITPLGPYIGAQISGIDLTRPLSDNQFEQLYHALLRHQVLFFRDQPITPQQQRDLAARFGDLHIHPV
YPHAEGVPEIIVLDTHNDNPPDNDNWHTDVTFIETPPLGAILAAKQLPSTGGDTLWASGIAAYEALSAPF
RQLLSGLTAEHDFRKSFPEYKYRKTEEEHQRWEEAVAKNPPLLHPVVRTHPVSGRQALFVNEGFTTRIVD
LSEKESEALLGFLFAHITKPEFQVRWRWQPNDVAIWDNRVTQHYANADYLPQRRIMHRATILGDKPF
>gnl|CDD|236563 PRK09554, feoB, Fe(2+) transporter permease subunit FeoB
MKKLTIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPGTYSLTTISSQT
SLDEQIACHYILSGDADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSAR
LGCPVIPLVSTRGRGIEALKLAIDRHQANENVELVHYPQPLLNEADSLAKVMPSDIPLQQRRWLGLQMLE
GDIYSRAYAGEASQHLDAALARLRNEMDDPALHIADARYQCIAAICDAVSNTLTAEPSRLTTALDKIILN
RWLGLPIFLFVMYLMFLLAINIGGALQPLFDVGSVAIFIHGIQWLGYTLHFPDWLTIFLAQGLGGGINTV
LPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVGFGCNVPSVMGARTLDAPRER
LMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYLLGIVMAILTGLMLKYTIMRGEASPFVMELP
VYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIVDNINDSALASVSRVITPVLKP
IGVHEDNWQATVGLFTGAMAKEVVVGTLNTLYTAENIQDEEFNPAEFNLGDELFGAVDETWQSLKDTFSL
SVLANPIEASKGDGEMGTGAMGVMSQKFGSAAAAYSYLIFVLLYVPCISVMGAIARESSRGWMGFSILWG
LNIAYSLATLFYQVASFSQHPTYSLVCILAVILFNIVVLGLLRRARSRVDVELLATRKSVSSCCAATTGD
CH
>gnl|CDD|181949 PRK09555, feoA, ferrous iron transporter A
MQLTPDTAYKITGFSREISPAYRQKLLSLGMLPGSSFNVVRVAPLGDPIHIETRRVSLVLRKKDLALLEL
EAVS
>gnl|CDD|236564 PRK09556, uhpT, hexose-6-phosphate:phosphate antiporter
LAFLNQVRKPTLDLPLEVQRKMWFKPFMQSYLVVFIGYLTMYLIRKNFKAAQNDMISTYGLSTTELGMIG
LGFSITYGVGKTLVGYYADGKNTKQFLPFLLILSAICMLGFGASLGSGSVSLGLMIALWALSGFFQSTGG
PCSYSTITRWTPRRKRGRFLGFWNISHNLGGAGAGGVALWGANYFFDGHVIGMFIFPSIIALIIGFIGLR
YGSDSPEELGWGKAEEIFGEPISEEDKETESTDMTKWQIFVEYVLKNPVIWLLCFANIFLYIVRIGIDNW
SPVYAFQELGFSKEDAINTFTLFEIGALVGSLLWGWLSDLANGRRALVACIALALIIFTLGVYQHATSEY
MYLASLFALGFLVFGPQLLIGVAAVGFVPKKAIGVANGIKGTFAYLFGDSFAKVGLGMIADPTKNGTPIF
GYTLTGWAGTFAALDIAAIGCICLMAIVAVMEERKIRREKKIQQLTI
>gnl|CDD|236565 PRK09557, PRK09557, fructokinase; Reviewed
MRIGIDLGGTKIEVIALDDAGEELFRKRLPTPRDDYQQTIEAIATLVDMAEQATGQRGTVGVGIPGSISP
YTGLVKNANSTWLNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAI
NGRVHIGGNGIAGEWGHNPLPWMDEDELRYRNEVPCYCGKQGCIETFISGTGFATDYRRLSGKALKGSEI
IRLVEEGDPVAELAFRRYEDRLAKSLAHVINILDPDVIVLGGGMSNVDRLYPTLPALLKQYVFGGECETP
VRKALHGDSSGVRGAAWLWPK
>gnl|CDD|236566 PRK09558, ushA, bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
MMKFLKRLVALALLAALALCGSTAQAYEKDKTYKITILHTNDHHGHFWRNEYGEYGLAAQKTLVDQIRKE
VAAEGGSVLLLSGGDINTGVPESDLQDAEPDFRGMNLIGYDAMAVGNHEFDNPLSVLRKQEKWAKFPFLS
ANIYQKSTGERLFKPYAIFDRQGLKIAVIGLTTEDTAKIGNPEYFTDIEFRDPAEEAKKVIPELKQTEKP
DVIIALTHMGHYDDGEHGSNAPGDVEMARSLPAGGLDMIVGGHSQDPVCMAAENKKQVDYVPGTPCKPDQ
QNGTWIVQAHEWGKYVGRADFEFRNGELKLVSYQLIPVNLKKKVKWEDGKSERVLYTEEIAEDPQVLELL
TPFQEKGQAQLDVKIGETNGKLEGDRSKVRFVQTNLGRLIAAAQMERTGADFAVMNGGGIRDSIEAGDIT
YKDVLTVQPFGNTVVYVDMTGKEVMDYLNVVATKPPDSGAYAQFAGVSMVVDCGKVVDVKINGKPLDPAK
TYRMATPSFNAAGGDGYPKLDNHPGYVNTGFVDAEVLKEYIQKNSPIDAADYEPKGEIVYQ
>gnl|CDD|236567 PRK09559, PRK09559, putative global regulator; Reviewed
MAFTPFPPRQPSASARLPLTLISLDDWALATITGADSEKYLQGQVTADVSQLTEDQHLLAAHCDAKGKMW
SNLRLFRRGDGFAWIERRSVRENQLTELKKYAVFSKVTIAPDDERVLLGVAGFQARAALANLFSELPDAE
KPVVQEGATTLLWFEHPAERFLLVTDEATANMLTEKLRGEAQLNNSQQWLALDIEAGFPVIDAANSGQFI
PQATNLQALGGISFKKGCYTGQEMVARAKFRGANKRALWWLAGKASRVPEAGEDLELKMGENWRRTGTVL
AAVQLDDGQVWVQVVMNNDLEADSVFRVRDDAGNTLHIQPLPYSLEE
>gnl|CDD|236568 PRK09560, nhaA, pH-dependent sodium/proton antiporter; Reviewed
MLSVIRRFLKSEAAGGILLMAAAALAMIVANSPLSEGYFSFLHTPVAIQIGAFSIGKSLLHWINDGLMAV
FFLLVGLEIKRELLEGQLSSWQQRILPAIAAVGGMVVPALIYAAFNYNNPETLRGWAIPAATDIAFALGV
LALLGKRVPVSLKVFLLALAIIDDLGAIVIIALFYTSDLSLPALALAAIAIAVLFLLNRLGVTKLTPYLI
VGAILWFAVLKSGVHATLAGVVLAFCIPLKGKKGDEESPLHHLEHALHPWVAFAILPLFAFANAGVSLAG
ISLSSLTSPVPLGIALGLFLGKQVGVFGFSWLAVKLGLAKLPEGANWKQIYGVSVLCGIGFTMSLFIGSL
AFGASEELLTEARLGILLGSLLSAILGYLLLRLTLRKKE
>gnl|CDD|181955 PRK09561, nhaA, sodium/proton antiporter NhaA
MMKHIRRFLSSEASGGILLIIAAALAMLMANSPTSGWYQDFLETPVQLRVGALEINKPLLLWINDGLMAV
FFLLIGLEVKRELLEGSLASRRQAALPVIAAIGGMLVPALIYLLFNYADPVTREGWAIPAATDIAFALGV
LALLGSRVPVALKIFLLALAIIDDLGAIVIIALFYTSDLSMVSLGVAAVAIAVLAVLNLCGVRRTSVYIL
VGVVLWVAVLKSGVHATLAGVIVGFFIPLKEKHGRSPAERLEHGLHPWVAFLILPLFAFANAGVSLQGVT
LDGLTSPLPLGIALGLFIGKPLGIFLFSWLAVKLKLAKLPEGTTFKQIYAVGVLCGIGFTMSIFIASLAF
GGVDPELINYAKLGILIGSLLSAVIGYSWLRKVLPASV
>gnl|CDD|236569 PRK09562, mazG, nucleoside triphosphate pyrophosphohydrolase; Reviewed
SRMETSEAIDRLLEIMARLRDPEGGCPWDKEQTFASLAPYTIEEAYEVVDAIERGDLDDLREELGDLLLQ
VVFHAQMAEEQGAFDFADVVEAISDKLIRRHPHVFGDVEAESSEEVLANWEQIKAEERAESSVLDGIPRG
LPALMRAYKIQKKAARVGFDWESLEPVLDKVEEEIDELKEALAQGDQAKIEEEFGDLLFALVNLARHLGI
DPEAALRKANAKFERRFRAVEQLAAAQGKTLEDASLEEMDALWQEAKRQEKA
>gnl|CDD|181958 PRK09564, PRK09564, coenzyme A disulfide reductase; Reviewed
MKIIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGACGLPYFVGGFFDDPNTMIARTPEEFIKSG
IDVKTEHEVVKVDAKNKTITVKNLKTGSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLAL
KELLKDEEIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHL
NEFVKSLIGEDKVEGVVTDKGEYEADVVIVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAA
GDCATIYNIVSNKNVYVPLATTANKLGRMVGENLAGRHVSFKGTLGSACIKVLDLEAARTGLTEEEAKKL
GIDYKTVFIKDKNHTNYYPGQEDLYVKLIYEADTKVILGGQIIGKKGAVLRIDALAVAIYAKLTTQELGM
MDFCYAPPFARTWDALNVAGNVAK
>gnl|CDD|236571 PRK09565, PRK09565, heme-binding protein
MERREPPQTEEGWYVLHDFRSIDWDAWRDAPERVRDRAIEEGIDYLQAHEAVEDAEEGDSAVFSVLGHKA
DLLILHLRPTLADLDRAERRFEQTALAAFTEQADSYVSVTEASGYTEKSREYFEGEVDDDSGLARYIESR
LHPEIPDAEFVSFYPMSKRRGPEHNWYDLPFDERAEHMSSHGDIGRQYAGKVTQIIAGSIGFDDWEWGVT
LFADDPTDIKELLYEMRFDPSSSKFAEFGRFYVGRRFPPSDLGAFLAGERVPTATPEDAADGGTGGTHDA
EEFGEHGHHGGHPGGEDGEHPHGHEDSGGHHGSGGDNFDHYDRHVATTVRADGGREDSDEEIRGELADAG
VYAGQPHGEDVYALVLYSEADPDELFEEVEGLRENFDHYDTHVKTAVYEAEEDGGRTAVVSLWETEDAAD
TAAGFLADLPGIVARAGEGDGFGTMGMFYTVKPDYREDFVETFDTVGGLLAEMDGHRETDLLVNRDDEND
MFIASQWDSKEDAMAFFRSDAFRETVEWGRDVLADRPRHVFLA
>gnl|CDD|236572 PRK09566, nirA, ferredoxin-nitrite reductase; Reviewed
SMTRPTLEGKKLNKIEKNKAEKDGLAVKDELEKFAQIGWEAMDETDLELRLKWLGMFWRPVTPGKFMLRL
RVPNGILTSEQLRVLASIVQRYGDDGSADITTRQNLQLRGILLEDLPEILNRLKAVGLTSVQSGMDNVRN
ITGSPVAGIDPDELIDTRPLTQKLQDMLTNNGEGNPEFSNLPRKFNIAIAGGRDNSVHAEINDIAFVPAY
KDGVLGFNVLVGGFFSSQRCAYAIPLNAWVKPDEVVRLCRAILEVYRDNGLRANRQKGRLMWLIDEWGIE
KFRAAVEAQFGPPLLTAAPGDEIDWEKRDHIGVHPQKQAGLNYVGLHVPVGRLYAEDMFELARLAEVYGS
GEIRLTVEQNVIIPNIPDENLETFLAEPLLQKFSLEPGPLARGLVSCTGNQYCNFALIETKNRALALAKE
LDAELDLPQPVRIHWTGCPNSCGQPQVADIGLMGTKARKNGKTVEGVDIYMGGKVGKDAKLGECVQKGIP
CEDLKPVLKDLLIEQFGAKPKSE
>gnl|CDD|236573 PRK09567, nirA, NirA family protein
ATMSSEFSAEQKRYLEGFAAGADAARATRGAAGGQTPAAPAAEPTGPDAIHIKAQDRFLAAGKKLCDQEK
WKREENPFDAWDRLKAQAAAGAFPKPADNFRWKYHGLFYVAPAQDSYMCRLRIPNGILTHWQFAGLADLA
DRHGGGYSHVTTRANLQLREIPPEHAVPVLEGLVDLGLTARGSGADNIRNVTGSPTAGIDPQELLDTRPY
AREWHHHILNDRSLYGLPRKFNVAFDGGGRIATLEDTNDIGFQAVRVLEGAGVAPGVYFRLVLGGITGHK
DFARDTGVLLRPEEATAVADAIVRVFIENGDRTNRKKARLKYVLDAWGFDKFLEAVEEKLGRPLTRVPAE
AVAPRPAADRFAHVGVHPQKQPGLNWIGVVLPVGRLTTDQMRGLAKIAARYGDGEIRLTVWQNLLISGVP
DADVAAVEAAIEALGLTTEASSIRAGLVACTGNAGCKFAAADTKGHALAIADYCEPRVALDQPVNIHLTG
CHHSCAQHYIGDIGLIGAKVAVSEGDTVEGYHIVVGGGFGEDAAIGREVFRDVKAEDAPRLVERLLRAYL
AHRQGPDETFQAFTRRHDPEALRSLAEEQPVLA
>gnl|CDD|236574 PRK09568, PRK09568, DNA primase regulatory subunit PriL
MVLDVKKYPFIKSLEDELKKYGGGITLSDLLLNSTTLIDQAKDRIQKIKSGEELPHYVSYNEPVLVFYTT
LLSLAILNDLRLIRKYAHKEAKQFKSLLQNENEENLLEITKLLGLNINKCDLKIKFSLEKKRRIVQLEFS
VNFIDYLKYTKGLREDFKLSKQILYKGYVYLDKNQLTDLLAENIKNKIVEMIRPLNLKEIPEKLKSLIEE
KGGKTPPCIENILGKEELSEEEIRTLITYYINIGKGLDSIIAIMNVTNIEDLYKKYRGDKKTRYIVYSCA
RMKQLGLCVSNCNVKNPLQLYYGSKE
>gnl|CDD|181961 PRK09569, PRK09569, citrate (Si)-synthase
MQLKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPE
TFEALPKAPGSEYPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSV
GILAMQRESKFAKFYNEGKFNKMDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQIPSDPELDYGANF
AHMIGQPKPYKDVARMYFILHSDHESGNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGW
IQQFQEKLGGEEPTKEQVEQALWDTLNAGQVIPGYGHAVLRKTDPRYTAQREFCLKHLPDDPLFKLVAMI
FEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRALGVMANITWDRGLGYAIERPK
SVTTEMLEKWAAEGGRK
>gnl|CDD|236575 PRK09570, rpoH, DNA-directed RNA polymerase subunit H; Reviewed
MKKFDVLDHELVPEHEILSEEEAKKLLKEYGIKPEQLPKIKASDPVVKAIGAKPGDVIKIVRKSPTAGEA
VYYRLVVEG
>gnl|CDD|181963 PRK09573, PRK09573, (S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
MSIKAYFELIRPKNCIGASIGAIIGYLIASNFKIDLKGIILAALVVFLVCAGGNVINDIYDIEIDKINKP
ERPIPSGRISLKEAKIFSITLFIVGLILSIFINIYAFLIALLNSILLYLYAKDLKKTGLIGNLIVAYLTG
LSFIFGGLAVFNVLRIIILFLCAFFSTWSREIVKDIEDIEGDLKENVITLPIKYGIKKSWYIAKILLILA
IVLSPLPYFLGIFGIYYLIVVIICDILFIIAMLILLKNPSIEGASKASKYLKIIMILGLIAFLIGSLPI
>gnl|CDD|236576 PRK09575, vmrA, MATE family efflux transporter
SITIMMNQSIYRTFWRYTIPSIAAMLVNGLYQIVDGIFIGHYVGAEGLAGINMAWPVIGIILGIGLMVGM
GTGSLLSIKRGEGDLEKAKRILTTGLLLLLLLGPIVSVILFLFADDFLRAQGAEGRTLELALQYIQVLIW
GCLFTLGAIALPFLLRNDESPNLATGLMVIGALINIVLDYLFIGWLDWGLTGAAIATALAQLVVTVLGLG
YFFSSRANIRLTLKELRFNWSLAPKIVLLGSSSFFMYLYGSFVVALHNRLFMEYGSALTVGAYAIVGYLM
VLYYLVAEGIAEGMQPPVSYYFGARQYDNIKKLLKLAMKVTVLAGIAWVLLLNLFPETMIALFNSGDSEL
IAETIVGIRLHLFAMFLDGFLVLASAYFMAVNQGGKALFISIGNMLIQLPFLFILPKWLGVDGVWLAMPL
SNIALSLVVAPMLWRDVKKLKKPTQVEAAVAAS
>gnl|CDD|169981 PRK09577, PRK09577, multidrug efflux RND transporter permease subunit
MARFFIDRPVFAWVISLFIMLGGIFAIRALPVAQYPDIAPPVVSIYATYPGASAQVVEESVTALIEREMN
GAPGLLYTSATSSAGQASLSLTFKQGVNADLAAVEVQNRLKTVEARLPEPVRRDGIQVEKAADNIQLIVS
LTSDDGRLTGVELGEYASANVLQALRRVEGVGKVQFWGAEYAMRIWPDPVKLAALGLTASDIASAVRAHN
ARVTIGDIGRSAVPDSAPIAATVFADAPLKTPEDFGAIALRARADGSALYLRDVARIEFGGNDYNYPSYV
NGKTATGMGIKLAPGSNAVATEKRVRATMDELSRYFPPGVKYQIPYETSSFVRVSMNKVVTTLIEAGVLV
FLVMFLFMQNFRATLIPTLVVPVALLGTFGVMLAAGFSINVLTMFGMVLAIGILVDDAIVVVENVERLMV
EEGLSPYDATVKAMKQISGAIVGITVVLTSVFVPMAFFGGAVGNIYRQFALSLAVSIGFSAFLALSLTPA
LCATLLKPVDGDHHEKRGFFGWFNRFVARSTQRYATRVGAILKRPLRWLVVYGALTAAAALLFTRLPTAF
LPDEDQGNFMVMVIRPQGTPLAETMQSVREVESYLRRHEPVAYTFALGGFNLYGEGPNGGMIFVTLKDWK
ERKAARDHVQAIVARINERFAGTPNTTVFAMNSPALPDLGSTSGFDFRLQDRGGLGYAAFVAAREQLLAE
GAKDPALTDLMFAGTQDAPQLKLDIDRAKASALGVSMDEINTTLAVMFGSDYIGDFMHGSQVRRVIVQAD
GRHRLDPDDVKKLRVRNAQGEMVPLAAFATLHWTLGPPQLTRYNGYPSFTINGSAAPGHSSGEAMAAIER
IAATLPAGIGYAWSGQSFEERLSGAQAPMLFALSVLVVFLALAALYESWSIPFAVMLVVPLGVIGAVLGV
TLRGMPNDIYFKVGLIATIGLSAKNAILIVEVAKDLVAQRMSLADAALEAARLRLRPIVMTSLAFGVGVL
PLAFASGAASGAQIAIGTGVLGGVITATVLAVFLVPLFFVVVGRLFDVGPRR
>gnl|CDD|169982 PRK09578, PRK09578, MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit
YEWARRRRLLLAALVALFVLAGCGKGDSDAAAAAPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARV
AGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERD
YTEAVADERQAKAAVASAKAELARAQLQLDYATVTAPIDGRARRALVTEGALVGQDQATPLTTVEQLDPI
YVNFSQPAADVEALRRAVKSGRATGIAQQDVAVTLVRADGSEYPLKGKLLFSDLAVDPTTDTVAMRALFP
NPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVKVVGQNGKVRDVEVEADQMSGRDWIVTRG
LAGGERVIVDNAAQFAPGTAVKAVERAPAAKPAPG
>gnl|CDD|169983 PRK09579, PRK09579, multidrug efflux RND transporter permease subunit
MAFTDPFIRRPVLASVVSLLIVLLGFQAWSKLQIRQYPQMENALITVTTAYPGANAETIQGYITQPLQQS
LASAEGIDYMTSVSRQNFSIISIYARIGADSDRLFTELLAKANEVKNQLPQDAEDPVLSKEAADASALMY
ISFYSEEMSNPQITDYLSRVIQPKLATLPGMAEAEILGNQVFAMRLWLDPVKLAGFGLSAGDVTQAVRRY
NFLSAAGEVKGEYVVTSINASTELKSAEAFAAIPVKTSGDSRVLLGDVARVEMGAENYDSISSFDGIPSV
YIGIKATPSANPLDVIKEVRAIMPELESQLPPNLKVSIAYDATLFIQASIDEVVKTLGEAVLIVIVVVFL
FLGALRSVLIPVVTIPLSMIGVLFFMQMMGYSINLLTLLAMVLAIGLVVDDAIVVVENIHRHIEEGKSPF
DAALEGAREIAMPVVSMTITLAAVYAPIGFLTGLTGALFKEFALTLAGAVIISGIVALTLSPMMCALLLR
HEENPSGLAHRLDRLFERLKQRYQRALHGTLNTRPVVLVFAVIVLALIPVLLKFTQSELAPEEDQGIIFM
MSSSPQPANLDYLNAYTDEFTPIFKSFPEYYSSFQINGFNGVQSGIGGFLLKPWNERERTQMELLPLVQA
KLEEIPGLQIFGFNLPSLPGTGEGLPFQFVINTANDYESLLQVAQRVKQRAQESGKFAFLDIDLAFDKPE
VVVDIDRAKAAQMGVSMQDLGGTLATLLGEGEINRFTIDGRSYKVIAQVERPYRDNPGWLNNYYVKNEQG
QLLPLSTLITLSDRARPRQLNQFQQLNSAIISGFPIVSMGEAIETVQQIAREEAPEGFAFDYAGASRQYV
QEGSALWVTFGLALAIIFLVLAAQFESFRDPLVILVTVPLSICGALIPLFLGVSSMNIYTQVGLVTLIGL
ISKHGILIVEFANQLRHEQGLSRREAIEEAAAIRLRPVLMTTAAMVFGMVPLILATGAGAVSRFDIGLVI
ATGMSIGTLFTLFVLPCIYTLLAKPDAAPGVAQAANA
>gnl|CDD|181965 PRK09580, sufC, cysteine desulfurase ATPase component; Reviewed
MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLEL
SPEDRAGEGIFMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTR
SVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDY
IKPDYVHVLYQGRIVKSGDFTLVKQLEEQGYGWLTEQQ
>gnl|CDD|236577 PRK09581, pleD, response regulator PleD; Reviewed
MTARILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKS
DPATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKPINDVALFARVKSLTRLKMVIDELRLRASTNAEIG
VTALMIMAYANKDEDGRILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFEN
YDPLRLCSQLRSKERTRYVPILLLVDEDDDPRLVKALELGVNDYLMRPIDKNELLARVRTQIRRKRYQDA
LRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVL
REFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKERLNVTVSIGV
AELRPSGDTIEALIKRADKALYEAKNTGRNRVVALAA
>gnl|CDD|181967 PRK09582, chaB, putative cation transport regulator ChaB
MPYKTKSDLPESVKHVLPAHAQDIYKEAFNSAWDQYKDKEDRRDDASREETAHKVAWAAVKHEYAKGDDD
KWHKKS
>gnl|CDD|236578 PRK09583, PRK09583, mycothiol-dependent maleylpyruvate isomerase; Reviewed
MMDDAHDLPLHERLAAVRRATARLLRAVAGLDDASVREPSLLPGWTRGHVLAHLARNADALVNLLEWART
GVETPMYASPEARDADIEAGATRPAAALRADLDHSAARLDVAWDALPADAWSATVGTAQGRTVPAAELVW
MRLREVEIHHVDLGAGYTFADLPEVFVERLLAWIVGRLAGRPDVPALVLLDDGDRPTTVVGDGGDPVVVS
GPLAALLGWLTGRGPGGVLTGAGLPALPPWL
>gnl|CDD|181969 PRK09584, tppB, dipeptide/tripeptide permease DtpA
MSTANQKPTESVSLNAFKQPKAFYLIFSIELWERFGYYGLQGIMAVYLVKQLGMSEADSITLFSSFSALV
YGLVAIGGWLGDKVLGTKRVIMLGAIVLAIGYALVAWSGHDAGIVYMGMATIAVGNGLFKANPSSLLSTC
YEKDDPRLDGAFTMYYMSINIGSFFSMLATPWLAAKYGWSVAFALSVVGMLITVVNFAFCQRWVKQYGSK
PDFEPINYRKLLLTIVGVVALIAIATWLLHNQEIARMALGVVALGIVVIFGKEAFAMKGAARRKMIVAFI
LMLEAIIFFVLYSQMPTSLNFFAIRNVEHSILGIAVEPEQYQALNPFWIMIGSPILAAIYNKMGDRLPMP
HKFAIGMVLCSGAFLVLPLGAKFANDAGIVSVNWLIASYGLQSIGELMISGLGLAMVAQLVPQRLMGFIM
GSWFLTTAGAALIAGYVANLMAVPDNVTDPLMSLEVYGRVFLQIGIATAVIAVLMLLTAPKLNRMTQDDS
ADKAAKAATA
>gnl|CDD|236579 PRK09585, anmK, anhydro-N-acetylmuramic acid kinase; Reviewed
SMRYIGLMSGTSLDGVDAALVEIDGEGTKVELLASATVPYPDELRAALLALLQGGADELERLAELDTALG
RLFAEAVNALLAEAGLSPEDIDAIGSHGQTVRHRPGEGFTLQIGDGALIAELTGITVVADFRRRDVAAGG
QGAPLVPAFHQALFGHPDETRAVLNIGGIANITLLPPGGGPVIGFDTGPGNALIDAWIQRHGGKPYDKDG
AWAASGKVDEALLARLLAHPYFALPPPKSTGRELFNLAWLERQLAGFGLSPEDVQATLTELTAASIARAV
RRLPPGPDELLVCGGGARNPTLMERLAALLPTEVATTDALGIDGDAKEALAFAWLAVRTLRGLPGNLPSV
TGASGPVVLGAIYPA
>gnl|CDD|181971 PRK09586, murP, PTS system N-acetylmuramic acid transporter subunits EIIBC; Reviewed
MAKISSELLNTILTRVGGPGNIASCGNCMTRLRLTLHDSSLVDPAAIKTIEGVKGVILSDDQVQVVLGPG
KAQRAAKAMNELLGEAAAPVQDLAEIAAQNKRQLKAKQTSGVQQFLAKFATIFTPLIPGFIAAGLLLGIA
TLIEQVMHVPADAQGTLPDALNYMKVFSKGLFTFLSILIGYNAQQAFGGTGVNGAIIASLFLLGYNPAAT
TGYYAGFHDFFGLPIDPRGNIIGVLIAAIAGARIERMVRRFMPDDLDMILTSLITLLITGALAFLIIMPL
GGWLFEGMSWLFMHLNSNPFGCAVLAGLFLIAVVFGVHQGFIPVYFALMDSQGFNSLFPILAMAGAGQVG
AALALYWRAQKHSALRTQVKGAIIPGLLGVGEPLIYGVTLPRMKPFVTACLGGAAGGFFIGLIAWLGLPV
GLNSVFGPSGLVALPLMTSAQGILPGMAVYAGGLLVAYVCGFIFTTLFGCKNVDLD
>gnl|CDD|181972 PRK09588, PRK09588, hypothetical protein; Reviewed
MGNYIRPLSDAVFIIASDKSWIESSAIQQLHTTAKLPGMRRVVGMPDLHPGRGYPIGAAFFSVGRFYPAL
VGNDIGCGMALWQTDLLARKYNADKLEKRLSDLDDPLDESWLEENVPLALAQHPWRSSLGTIGGGNHFAE
LQQVDEIYDAELFALLGLDADQLLLLVHSGSRGLGQAILRRHVASFGHNGLPEGSDDALAYLAEHDDALA
FARANRQLIARRILQQLRAEGEPVLDVAHNFVEPCQVGGEDGWLHRKGATPSDQGLVVIPGSRGDYSYLV
KPVASEESLFSLAHGAGRKWMRTECKGRLAAKFTVTQLSRTPLGSRVICRDRQLIFEEAPEAYKSIESVI
QDLVQAGLITPVARLRPVLTYKTSGE
>gnl|CDD|181973 PRK09589, celA, 6-phospho-beta-glucosidase; Reviewed
MSGFKKGFLWGGAVAAHQLEGGWNEGGKGISVADVMTAGAHGVPREITEGVIEGKNYPNHEAIDFYHRYK
EDIALFAEMGFKCFRTSIAWTRIFPQGDELEPNEEGLQFYDDLFDECLKQGIEPVVTLSHFEMPYHLVTE
YGGWRNRKLIDFFVRFAEVVFTRYKDKVKYWMTFNEINNQANFSEDFAPFTNSGILYSPGEDREQIMYQA
AHYELVASALAVKTGHEINPDFQIGCMIAMCPIYPLTCAPNDMMMATKAMHRRYWFTDVHVRGYYPQHIL
NYFARKGFNLDITPEDNAILAEGCVDYIGFSYYMSFATKFHEDNPQLDYVETRDLVSNPYVKASEWGWQI
DPAGLRYSLNWFWDHYQLPLFIVENGFGAIDQREADGTVNDHYRIDYLAAHIREMKKAVVEDGVDLMGYT
PWGCIDLVSAGTGEMKKRYGFIYVDKDNEGKGTLERSRKKSFYWYRDVIANNGENI
>gnl|CDD|181974 PRK09590, celB, PTS cellobiose transporter subunit IIB
MKKALIICAAGMSSSMMAKKTTEYLKEQGKDIEVDAITATEGEKAIAAAEYDLYLVSPQTKMYFKQFEEA
GAKVGKPVVQIPPQAYIPIPMGIEKMAKLILENI
>gnl|CDD|181975 PRK09591, celC, PTS cellobiose transporter subunit IIA
MNQEELQVAAFEIILHSGNARTEVHEAFAAMREGNFDLAEQKLNQSNEELLEAHHAQTKLLQEYASGTEI
KIEIIMVHAQDHLMTTMTLREVAKEMLALYKKVN
>gnl|CDD|181976 PRK09592, celD, PTS cellobiose transporter subunit IIC
MDQQNGLFGFLEKHLMGPMGKLAQFRIVRAIMAAGMASIPFTIVGSMFLVLSVLPQAFSFPILADIFAAS
FDKFSNLYMVANNATMGILSLYFALVFGYEYTKIYAEEEKLNVNPLNGALLSLMAFFMTVPELVFKGGSM
TLVTSLKKDAVIIDGWAMGNGVTRLGTTGIFTAIIMAILTVQLYRFCVKHNWVIKMPEAVPEGVSRSFTA
LIPGFVVAFVVIFINGILVALGTDIFKVIAIPFSFVSNLTNTWIGLMIIYFLIHALWIVGIHGANIVSSF
VTPIVLANMAENAKGAHIPFAGEFNNAFVIIGGSGATLGLCIFIAFAAKSEQLKALGKASIVPAIFNINE
PLIFGLPIVYNPYLAIPFILAPMVSATVAYVAISLHFVKPIIAQVPWPTPVGLGAFIGTADWRAAVLALV
CAIVAFLVWFPFIKHYDNKLLKEEQGKAA
>gnl|CDD|236580 PRK09593, arb, 6-phospho-beta-glucosidase; Reviewed
TEKMPFPKGFLWGGATAANQCEGAYNVDGRGLANVDVVPIGEDRFPIITGEKKMFDFEEGYFYPAKEAID
MYHHYKEDIALFAEMGFKTYRMSIAWTRIFPKGDELEPNEAGLQFYEDIFKECHKYGIEPLVTITHFDCP
MHLIEEYGGWRNRKMVGFYERLCRTLFTRYKGLVKYWLTFNEINMILHAPFMGAGLYFEEGENKEQVKYQ
AAHHELVASAIATKIAHEVDPENKVGCMLAAGQYYPNTCHPEDVWAAMKEDRENYFFIDVQARGEYPNYA
KKRFEREGITIEMTEEDLELLKENTVDFISFSYYSSRVASGDPKVNEKTAGNIFASLKNPYLKASEWGWQ
IDPLGLRITLNTIWDRYQKPMFIVENGLGAVDKPDENGYVEDDYRIDYLAAHIKAMRDAINEDGVELLGY
TTWGCIDLVSAGTGEMKKRYGFIYVDRDNEGKGTLKRSKKKSFDWYKKVIASNGEDLE
>gnl|CDD|181978 PRK09597, PRK09597, lipid A 1-phosphatase LpxE
MKKFLFKQKFCESLPKSFSKTLLALSLGLILLGIFAPFPKVPKQPSVPLAFHFTEHYARFIPTILSVAIP
LIQRDAIGLFQVANASIATTLLTHTTKRALNHVTINDQRLGERPYGGNFNMPSGHSSMVGLAVAFLMRRY
SFKKYWWLLPLIPLTMLARIYLDMHTIGAVLAGLGVGMLCVSLFTSPKKK
>gnl|CDD|236581 PRK09598, PRK09598, phosphoethanolamine--lipid A transferase EptA
MASLFHLKFLKPLSCLQAGLLYSLLNGVLYHFPLFAYVYKESNQVSFIAMLVVLLFCVNGLLFLLLGLLS
RRLMRLSAIVFSLLNSIAFYFINTYKVFLNKSMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYK
IPLKNSSKKAPFAAILALVLIFLASAFANSKNWLWFDKHAKFLGGLILPWSYSVNTFRVSAHKFFAPTIK
PLLPPLFSPNHSKSVVVLVIGESARKHNYALYGYEKPTNPRLSKRLATHELTLFNATSCATYTTASLECI
LDSSFKNTSNAYENLPTYLTRAGIKVFWRSANDGEPNVKVTSYLKNYELIQKCPNCEAPYDESLLYNLPE
LIKASSNENVLLILHLAGSHGPNYDNKYPLNFRVFKPVCSSVELSSCSKESLINAYDNTIFYNDYLLDKI
ISMLKNLKQPALMIYLSDHGESLGEGAFYLHGIPKSIAPKEQYEIPFIVWASDSFKKQHSIIQTQTPINQ
NVIFHSVLGVFDFKNPSAVYRPSLDLFKHKKE
>gnl|CDD|236582 PRK09599, PRK09599, NADP-dependent phosphogluconate dehydrogenase
MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPAPRVVWLMVPAG
EITDATIDELAPLLSPGDIVIDGGNSYYKDDIRRAELLAEKGIHFVDVGTSGGVWGLERGYCLMIGGDKE
AVERLEPIFKALAPRAEDGYLHAGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASRFDLDLAAVAEVW
RRGSVIRSWLLDLTADALAEDPKLDEISGYVEDSGEGRWTVEEAIDLAVPAPVIAAALFMRFRSRQEDSF
ADKVVAALRNGFGGHAVKKKE
>gnl|CDD|236584 PRK09602, PRK09602, translation-associated GTPase; Reviewed
MITIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVAYVRVECPCKELGVKCNPRNGKCIDGTR
FIPVELIDVAGLVPGAHEGRGLGNQFLDDLRQADALIHVVDASGSTDEEGNPVEPGSHDPVEDIKFLEEE
LDMWIYGILEKNWEKFSRKAQAEKFDIEEALAEQLSGLGINEEHVKEALRELGLPEDPSKWTDEDLLELA
RELRKISKPMVIAANKADLPPAEENIERLKEEKYYIVVPTSAEAELALRRAAKAGLIDYIPGDSDFEILG
ELSEKQKKALEYIREVLKKYGGTGVQEAINTAVFDLLDMIVVYPVEDENKLTDKKGNVLPDAFLLPKGST
ARDLAYKIHTDIGEGFLYAIDARTKRRIGEDYELKDGDVIKIVSTA
>gnl|CDD|181983 PRK09603, PRK09603, DNA-directed RNA polymerase subunit beta/beta'
MSKKIPLKNRLRADFTKTPTDLEVPNLLLLQRDSYDSFLYSKDGKESGIEKVFKSIFPIQDEHNRITLEY
AGCEFGKSKYTVREAMERGITYSIPLKIKVRLILWEKDTKSGEKNGIKDIKEQSIFIREIPLMTERTSFI
INGVERVVVNQLHRSPGVIFKEEESSTSLNKLIYTGQIIPDRGSWLYFEYDSKDVLYARINKRRKVPVTI
LFRAMDYQKQDIIKMFYPLVKVRYENDKYLIPFASLDANQRMEFDLKDPQGKIILLAGKKLTSRKIKELK
ENHLEWVEYPMDILLNRHLAEPVMVGKEVLLDMLTQLDKNKLEKIHDLGVQEFVIINDLALGHDASIIHS
FSADSESLKLLKQTEKIDDENALAAIRIHKVMKPGDPVTTEVAKQFVKKLFFDPERYDLTMVGRMKMNHK
LGLHVPDYITTLTHEDIITTVKYLMKIKNNQGKIDDRDHLGNRRIRAVGELLANELHSGLVKMQKTIKDK
LTTMSGAFDSLMPHDLVNSKMITSTIMEFFMGGQLSQFMDQTNPLSEVTHKRRLSALGEGGLVKDRVGFE
ARDVHPTHYGRICPIETPEGQNIGLINTLSTFTRVNDLGFIEAPYKKVVDGKVVGETIYLTAIQEDSHII
APASTPIDEEGNILGDLIETRVEGEIVLNEKSKVTLMDLSSSMLVGVAASLIPFLEHDDANRALMGTNMQ
RQAVPLLRSDAPIVGTGIEKIIARDSWGAIKANRAGVVEKIDSKNIYILGEGKEEAYIDAYSLQKNLRTN
QNTSFNQVPIVKVGDKVEAGQIIADGPSMDRGELALGKNVRVAFMPWNGYNFEDAIVVSERITKDDIFTS
THIYEKEVDARELKHGVEEFTADIPDVKEEALAHLDESGIVKVGTYVSAGMILVGKTSPKGEIKSTPEER
LLRAIFGDKAGHVVNKSLYCPPSLEGTVIDVKVFTKKGYEKDARVLSAYEEEKAKLDMEHFDRLTMLNRE
ELLRVSSLLSQAILEEPFSHNGKDYKEGDQIPKEEIASINRFTLASLVKKYSKEVQNHYEITKNNFLEQK
KVLGEEHEEKLSILEKDDILPNGVIKKVKLYIATKRKLKVGDKMAGRHGNKGIVSNIVPVADMPYTADGE
PVDIVLNPLGVPSRMNIGQILEMHLGLVGKEFGKQIASMLEDKTKDFAKELRAKMLEIANAINEKDPLTI
HALENCSDEELLEYAKDWSKGVKMAIPVFEGISQEKFYKLFELAKIAMDGKMDLYDGRTGEKMRERVNVG
YMYMIKLHHLVDEKVHARSTGPYSLVTHQPVGGKALFGGQRFGEMEVWALEAYGAAHTLKEMLTIKSDDI
RGRENAYRAIAKGEQVGESEIPETFYVLTKELQSLALDINIFGDDVDEDGAPKPIVIKEDDRPKDFSSFQ
LTLASPEKIHSWSYGEVKKPETINYRTLKPERDGLFCMKIFGPTKDYECLCGKYKKPRFKDIGTCEKCGV
AITHSKVRRFRMGHIELATPVAHIWYVNSLPSRIGTLLGVKMKDLERVLYYEAYIVKEPGEAAYDNEGTK
LVMKYDILNEEQYQNISRRYEDRGFVAQMGGEAIKDLLEEIDLITLLQSLKEEVKDTNSDAKKKKLIKRL
KVVESFLNSGNRPEWMMLTVLPVLPPDLRPLVALDGGKFAVSDVNELYRRVINRNQRLKRLMELGAPEII
VRNEKRMLQEAVDVLFDNGRSTNAVKGANKRPLKSLSEIIKGKQGRFRQNLLGKRVDFSGRSVIVVGPNL
KMDECGLPKNMALELFKPHLLSKLEERGYATTLKQAKRMIEQKSNEVWECLQEITEGYPVLLNRAPTLHK
QSIQAFHPKLIDGKAIQLHPLVCSAFNADFDGDQMAVHVPLSQEAIAECKVLMLSSMNILLPASGKAVAI
PSQDMVLGLYYLSLEKSGVKGEHKLFSSVNEIITAIDTKELDIHAKIRVLDQGNIIATSAGRMIIKSILP
DFIPTDLWNRPMKKKDIGVLVDYVHKVGGIGITATFLDNLKTLGFRYATKAGISISMEDIITPKDKQKMV
EKAKVEVKKIQQQYDQGLLTDQERYNKIIDTWTEVNDKMSKEMMTAIAKDKEGFNSIYMMADSGARGSAA
QIRQLSAMRGLMTKPDGSIIETPIISNFKEGLNVLEYFNSTHGARKGLADTALKTANAGYLTRKLIDVSQ
NVKVVSDDCGTHEGIEITDIAVGSELIEPLEERIFGRVLLEDVIDPITNEILLYADTLIDEEGAKKVVEA
GIKSITIRTPVTCKAPKGVCAKCYGLNLGEGKMSYPGEAVGVVAAQSIGEPGTQLTLRTFHVGGTASRSQ
DEREIVASKEGFVRFYNLRTYTNKEGKNIIANRRNASILVVEPKIKAPFDGELRIETVYEEVVVSVKNGD
QEAKFVLRRSDIVKPSELAGVGGKIEGKVYLPYASGHKVHKGGSIADIIQEGWNVPNRIPYASELLVKDN
DPIAQDVYAKEKGIIKYYVLEANHLERTHGIKKGDIVSEKGLFAVIADDNGREAARHYIARGSEILIDDN
SEVSANSVISKPTTNTFKTIATWDPYNTPIIADFKGKVSFVDIIAGVTVAEKEDENTGITSLVVNDYIPS
GYKPSLFLEGANGEEIRYFLEPKTSIAISDGSSVEQAEVLAKIPKATVKSRDITGGLPRVSELFEARKPK
PKDVAILSEVDGIVSFGKPIRNKEHIIVTSKDGRSMDYFVDKGKQILVHADEFVHAGEAMTDGVVSSHDI
LRISGEKELYKYIVSEVQQVYRRQGVSIADKHIEIIVSQMLRQVRILDSGDSKFIEGDLVSKKLFKEENA
RVIALKGEPAIAEPVLLGITRAAIGSDSIISAASFQETTKVLTEASIAMKKDFLEDLKENVVLGRMIPVG
TGMYKNKKIVLRTLEDDPKF
>gnl|CDD|236585 PRK09604, PRK09604, tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD
MLILGIETSCDETSVAVVDDGRGLLSNVVASQIDLHARYGGVVPELASRAHVENIVPLIEEALKEAGLTL
EDIDAIAVTAGPGLVGALLVGVSFAKALALALNKPLIGVNHLEGHLLAPFLEEEPEFPFLALLVSGGHTQ
LVLVKGIGDYELLGETLDDAAGEAFDKVAKLLGLGYPGGPAIDKLAKQGDPDAFKFPRPMDRPGLDFSFS
GLKTAVLNTIEKSEQTKADIAASFQAAVVDVLVIKTKRALKQTGVKTLVVAGGVAANSGLRERLAELAKK
RGIEVFIPPLKLCTDNAAMIAAAGYERLKAGEFSDLDLNARPRWPLDELSAL
>gnl|CDD|236586 PRK09605, PRK09605, bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase
MIVLGIEGTAWKTSAGIVDSDGDVLFNESDPYKPPSGGIHPREAAEHHAEAIPKVIKEALEEAGLKPEDI
DLVAFSQGPGLGPCLRVVATAARALALSLDVPLIGVNHCVAHVEIGRLTTGAEDPVTLYVSGGNTQVLAY
LNGRYRVFGETLDIGVGNALDKFARHVGLPHPGGPKIEKLAKDGKKYIDLPYVVKGMDFSFSGLLTAAKR
AYDAGEPLEDVCYSLQETAFAMLTEVTERALAHTGKDEVLLVGGVAANNRLREMLKEMCEERGADFYVPE
PRFCGDNGAMIAWLGLLMYKAGDTLDIEDTRVNPNFRTDEVEVTWIKEEEVKRRKIPDHLIGKGAEADIK
KGEYLGRDAVIKERVPKGYRHPELDERLRTERTRAEARLLSEARRAGVPTPVIYDVDPEEKTIVMEYIGG
KDLKDVLEGNPELVRKVGEIVAKLHKAGIVHGDLTTSNFIVRDDRLYLIDFGLGKYSDLIEDKAVDLHVL
KQSLESTHYDFEELWEAFLEGYRETEGAEDVLERLKEIEKRGRYL
>gnl|CDD|236587 PRK09606, PRK09606, DNA-directed RNA polymerase subunit B''; Validated
MMEDRRVLSDAYFKEHRLVRHHIDSYNDFVDNGLQKIIDEQGPIETEIEDGVYVELGKIRVGKPVVKEAD
GSEREIYPMEARLRNLTYSAPLYLEMSPVEGGEEEEPEEVYIGELPVMVGSKICNLYGLSEEELIEVGED
PLDPGGYFIVNGSERVLMTLEDLAPNKILVEKDERYGDRIEVAKVFSQRRGYRALVTVERNRDGLLEVSF
PSVPGSIPFVILMRALGLETDEEIVEAVSDDPEIVKFMLENLEEAEVDTQEEALEYIGKRVAPGQTKEYR
IKRAEYVIDRYLLPHLGVEPEVRRAKAHYLGRMAEACFELALGRREEDDKDHYANKRLKLAGDLMEDLFR
VAFNRLARDVKYQLERANMRNRELSIKTAVRSDVLTERLEHAMATGNWVGGRTGVSQLLDRTDYMATLSH
LRRVVSPLSRSQPHFEARDLHPTQWGRICPSETPEGPNCGLVKNFAQMVEISTGEDEEEVKEILKELGVE
PERG
>gnl|CDD|236588 PRK09607, rps11p, 30S ribosomal protein S11P; Reviewed
MSSMRKEKWGIAHIYASFNNTIITITDLTGAETIAKSSGGMVVKADRDESSPYAAMQAAEKAAEDAKEKG
ITGVHIKVRAPGGNGQKSPGPGAQAAIRALARAGLRIGRIEDVTPIPHDGTRPPGGRRGRRV
>gnl|CDD|181988 PRK09609, PRK09609, hypothetical protein; Provisional
IPKWTIKKISFVAILIAISVVFLIIGVRLAPFRALPTFKISFIGLPIKITGFIFGPIVGFFTGLLSDLIS
FLFVPGVYHPYYTLAAMVYGFIPGIVGWFFFKFGKKFFGKESRIKRYDNKIFKQKEQYDFALENPNSEKI
QKIKQKIILLEKKKKKLEKTNEEKSLLNFSWIAALIILVIIILFIYFVVGFLDPDFFIQSFSFIKNKRSL
MILIISGFILMIIFVIWARFFIKPKRFLTIAPIVIFSALLEPINVILLSSADAQSLGLDFDTWLFIHIIT
SPIKIWFNLSIIYFTYKIIAPLVNKKYSYSYV
>gnl|CDD|236589 PRK09612, rpl2p, 50S ribosomal protein L2P; Validated
MGKRIISQRRGRGTPTFRSPSHRYKGPVKYPPLDKDGTLRGKVVDILHDPGRNAPVAKVKFENGEEFLIL
APEGLYVGQEIEIGPSAEIKPGNTLPLGEIPEGTPVCNIESRPGDGGKFARSSGTYALVVGHEGDKVIVQ
LPSGKIKELNPRCRATIGVVAGGGRKEKPFLKAGKKYHKMKAKAKKWPRVRGVAMNAVDHPHGGGNHQHP
GRPSTVSRNAPPGRKVGHIAARRTGRRK
>gnl|CDD|236591 PRK09614, nrdF, ribonucleotide-diphosphate reductase subunit beta; Reviewed
RKIIGGNTYSAINWNKIEDPWDYEAWKRLTANFWLPEEVPLSNDLKDWKKLSDEEKNLYTRVFGGLTLLD
TLQNNNGMPNLMPDITTPEEEAVLANIAFMEAVHAKSYSYIFSTLCSPEEIDEAFEWAEENPYLQKKADI
IQDFYEPLKKKILRKAAVASVFLEGFLFYSGFYYPLYLARQGKMTGTAQIIRLIIRDESLHGYYIGYLFQ
EGLEELPELEQEELKDEIYDLLYELYENEEAYTELLYDIVGLAEDVKKYIRYNANKRLMNLGLEPLFPEE
EEVNPIWLNGLSNNADENHDFFEGKGTSYVKGATEATEDDDWDF
>gnl|CDD|181992 PRK09615, ggt, gamma-glutamyltranspeptidase; Reviewed
MIKPTFLRRVAIAALLSGSCFSAVAAPPAAPPVSYGVEEDVFHPVRAKQGMVASVDATATQVGVDILKQG
GNAVDAAVAVGYALAVTHPQAGNLGGGGFMLLRTKNGNTTAIDFREMAPAKATRDMFLDDQGNPDSKKSL
TSHLASGTPGTVAGFSLALDKYGTMPLNKVVQPAFKLARDGFIVNDALADDLKTYGSEVLPNHENSKAIF
WKEGEPLKKGDKLVQANLAKSLEMIAENGPDAFYKGTIADQIAQEMQKNGGLITKEDLAAYKAVERTPIS
GDYRGYQVYSMPPPSSGGIHIVQILNILENFDMKKYGFGSADAMQIMAEAEKYAYADRSEYLGDPDFVKV
PWQALTNKAYAKSIADQIDINKAKPSSEIRPGKLAPYESNQTTHFSVVDKDGNAVAVTYTLNTTFGTGIV
AGNSGILLNNQMDDFSAKPGVPNVYGLVGGDANAVGPNKRPLSSMSPTIVVKDGKTWLVTGSPGGSRIIT
TVLQMVVNSIDYGMNVAEATNAPRFHHQWLPDELRVEKGFSPDTLKLLEAKGQKVALKEAMGSTQSIMVG
PDGELYGASDPRSVDDLTAGY
>gnl|CDD|236593 PRK09617, PRK09617, type III secretion system protein; Reviewed
MRLIFRFFLCLFILSAPYSFADPDLTTQAVILIFLALSPFLVMLLTSFLKIIIVLSLLRNALGVQQTPPS
QVLNGIALILSIYIMFPTGVAMYNDAQKGIESNAVPRSLFSAEGAETVFVAANKSKEPLRSFLIKNTPKP
QIASFYKISQKTFPPEIRDALTPSDFMIIIPAFIMGQLKNAFEIGVLIYLPFFVIDLVTANVLLAMGMMM
LSPLSISLPLKLLLVVMVDGWTLLLEGLMISFK
>gnl|CDD|236594 PRK09618, flgD, flagellar hook assembly protein FlgD
MTMTGIDSSLWLANSKKAERRTGNQNLGKDDFLKLLITQLQNQDPTNPMEDKEFIAQMAQFSSLEQMTNM
NKSMEKLVSSSDGLTKYSELIGKEVEWEGEDGEIVSGTVTSVKQKDGDYPLVLDNGTWIVADNVTSVGLK
EK
>gnl|CDD|181996 PRK09619, flgD, flagellar hook assembly protein FlgD
MQINESRNSANVGNQSPAPEGGLPGAEQLNNQFMTLLVAQIQNQDPLNPADGTEFVSQLAQLSQVQSTEN
MAKLMKSNTVLMDNMQTLATANLVGQQVMVESHEITLGEDPVAGRLTLKHPAPTLTLHITDILGQEKKID
LGKQPAGPVNFTLDPAALGLQPGQYQLSVVSGSGEELIPVEVAGKVNNVRISPQGGAPQLNITGLGEVPY
YQITQFGA
>gnl|CDD|181997 PRK09620, PRK09620, hypothetical protein; Provisional
MKGKKVLITSGGCLEKWDQVRGHTNMAKGTIGRIIAEELISKGAHVIYLHGYFAEKPNDINNQLELHPFE
GIIDLQDKMKSIITHEKVDAVIMAAAGSDWVVDKICDQEGNVLDMNGKISSDIAPIIHFQKAPKVLKQIK
QWDPETVLVGFKLESDVNEEELFERAKNRMEEAKASVMIANSPHSLYSRGAMHYVIGQDGKGQLCNGKDE
TAKEIVKRLEVLCNHVTAL
>gnl|CDD|236595 PRK09621, PRK09621, ATP synthase subunit C
MIDMSVVGPALAMGLAMIGSAIGCGMAGVASHAVMSRIDEGHGKIIGLSAMPSSQSIYGLILMLLLNDAI
KDGKLSALSGIAIGISVGIALLLSAIMQGKCCASAIQAYARSSEIYGKSFAAIGIVESFALFAFVFALLL
F
>gnl|CDD|181999 PRK09622, porA, 2-oxoacid:ferredoxin oxidoreductase subunit alpha
MAKKIELQEIEVWDGNTAASNALRQAQIDVVAAYPITPSTPIVQNYGSFKANGYVDGEFVMVESEHAAMS
ACVGAAAAGGRVATATSSQGLALMVEVLYQASGMRLPIVLNLVNRALAAPLNVNGDHSDMYLSRDSGWIS
LCTCNPQEAYDFTLMAFKIAEDQKVRLPVIVNQDGFLCSHTAQNVRPLSDEVAYQFVGEYQTKNSMLDFD
KPVTYGAQTEEDWHFEHKAQLHHALMSSSSVIEEVFNDFAKLTGRKYNLVETYQLEDAEVAIVALGTTYE
SAIVAAKEMRKEGIKAGVATIRVLRPFPYERLGQALKNLKALAILDRSSPAGAMGALFNEVTSAVYQTQG
TKHPVVSNYIYGLGGRDMTIAHLCEIFEELNENALAGKLTHPTQQFVGLRGPKLSFF
>gnl|CDD|170016 PRK09623, vorD, 3-methyl-2-oxobutanoate dehydrogenase subunit delta
MNTLFGEKKEEAKKIVLKSVDEYPEAPISLGTTLSNFTGDWRTFMPVVDESKCVKCYICWKFCPEPAIYI
KEDGYVAIDYDYCKGCGICANECPTKAITMVKEEK
>gnl|CDD|170017 PRK09624, porD, pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
MAESPFKADIERVQKEYSEKMTPGAIAYIPGSSVINKTGSWRVFMPEFNRDKCVRCYLCYIYCPEPAIYL
DEEGYPVFDYDYCKGCGICANECPTKAIEMVRETK
>gnl|CDD|236596 PRK09625, porD, pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
MDKMKGWDEFEMGAVLFPFEKNAQSEMEKHNEERHYTEQSSFTTSVAHWRVEKPVHNNEICINCFNCWVY
CPDAAILSRDKKLKGVDYSHCKGCGVCVEVCPTNPKSLLMFEEQIENETALTQWPKKEEKKKS
>gnl|CDD|236597 PRK09626, oorD, 2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
AKMSAPDNTPVWVDESRCKACDICVSVCPAGVLAMRIDPHAVLGKMIKVVHPESCIGCRECELHCPDFAI
YVADRKEFKFAKLSKEAKERAEAVKANKYMKLE
>gnl|CDD|182002 PRK09627, oorA, 2-oxoglutarate synthase subunit alpha
MREIISTGNELVAKAAIECGCRFFGGYPITPSSEIAHEMSVLLPKCGGTFIQMEDEISGISVALGASMSG
VKSMTASSGPGISLKAEQIGLGFIAEIPLVIVNVMRGGPSTGLPTRVAQGDVNQAKNPTHGDFKSIALAP
GSLEEAYTETVRAFNLAERFMTPVFLLLDETVGHMYGKAVIPDLEEVQKMIINRKEFDGDKKDYKPYGVA
QDEPAVLNPFFKGYRYHVTGLHHGPIGFPTEDAKICGKLIDRLFNKIESHQDEIEEYEEYMLDDAEILII
AYGSVSLSAKEAIKRLREEGIKVGLFRPITLWPSPAKKLKEIGDKFEKILVIELNMGQYLEEIERVMQRD
DFHFLGKANGRPISPSEIIAKVKEL
>gnl|CDD|182003 PRK09628, oorB, 2-oxoglutarate ferredoxin oxidoreductase subunit beta
MAFNYDEYLRVDKMPTLWCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTH
GRAVAYATGIKLANPDKHVIVVSGDGDGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKG
MWTVTAQYGNIDPTFDACKLATAAGASFVARESVIDPQKLEKLLVKGFSHKGFSFFDVFSNCHINLGRKN
KMGEAVQMLKWIESRTVSKRKFDALSPEERVGKFPTGILKHDTDRKEYCEAYEEVIEAAQGKQKVDL
>gnl|CDD|104071 PRK09629, PRK09629, bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
MSAFTGLSLVIEPNDLLERLDAPELILVDLTSSARYEAGHIRGARFVDPKRTQLGKPPAPGLLPDTADLE
QLFGELGHNPDAVYVVYDDEGGGWAGRFIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVPPVAGGPVT
LTLHDEPTATREYLQSRLGAADLAIWDARAPTEYSGEKVVAAKGGHIPGAVNFEWTAGMDKARNLRIRQD
MPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKALGYPRVKAYAGSWGEWGNHPDTPVEVPTVAAAPIE
AVEVAQPAAPAQPAPAETVEPVRATEPSKGSQKYSGHSSSGPSMKDRLFIISQYLLPHHLLSRLAGCVAE
CRVRWFKNAFTAWFARRYQVDMSQALVEDLTSYEHFNAFFTRALKADARPLDTTPGAILSPADGAISQLG
PIDHGRIFQAKGHSFSVLELLGGDPKLSAPFMGGEFATVYLSPKDYHRVHMPLAGTLREMVYVPGRIFSV
NQTTAENVPELFARNERVVCLFDTERGPMAVVLVGAMIVASVETVWAGLVTPPKRELKTFSYDEAARAPI
HLEKGAEMGRFKLGSTAIVLFGPNQVKWAEQLTAGSKVQMGQALAVPAQA
>gnl|CDD|170022 PRK09630, PRK09630, DNA topoisomerase IV subunit A; Provisional
MSDVSDLFKTHFMHYASYVILERAIPHILDGLKPVQRRLLWTLFRMDDGKMHKVANIAGRTMALHPHGDA
PIVEALVVLANKGYLIDTQGNFGNPLTGDPHAAARYIEARLSPLAKEVLFNTDLMTFHDSYDGREKEPDI
LPAKLPLLLLHGVDGIAVGMTTKIFPHNFCELLEAQIAILNDQPFTLLPDFPSGGTMDASEYQDGLGSIT
LRASIDIINDKTLLIKEICPSTTTETLIRSIENAAKRGIIKIDSIQDFSTDLPHIEIKLPKGIYAKDLLR
PLFTHTECQVILTSRPTAIYQNKPVETSISEILRLHTETLQGYLKKELLILEDSLSREHYHKTLEYIFIK
HKLYDTVREMLSKRKTSPSSSDLHNAVLEALTPFLDTLPTPVDKQATAQLASLTIKKILCFNENSYTKEL
ACIEKKQAAVQKDLSQLKKYTVKYLKGLLETYGQLGHRKTQIAKFKAKKLSALKQQELF
>gnl|CDD|236598 PRK09631, PRK09631, DNA topoisomerase IV subunit A; Provisional
MMDIKTLFKDNFLQYASYVIKDRAIPDVIDGLKPVQRRILHSLFEMHDGKFHKVANVVGNTMKYHPHGDA
SIYEALVNLANKDLFIDKQGNFGNLFTGDPASAARYIECRLTPLAKEVLYNKEITEYEPSYDGRNNEPLC
LPAKIPVILIQGAEGIAVGMATKILPHNFNEILQAVKSELLGESFALYPDFPTGGIVDVSEYADGNGKVL
VRAKIETKDEKTIVIREIPFGTTTESLIASIEKAARKGKIKISSINDYTAENVEIEIKLPRGVYASEVIE
ALYAYTDCEVSISVNLLVIKDRYPVIYTVTDIIKFHAEHLQKVLKMELELERAKLLEKIFAKTLEQIFIE
ERIYKRIETISSEEDVISIVLSELKPFKEELSRDVTEEDIENLLKIPIRRISLFDIDKNQKEIRILNKEL
KSVEKNLKSIKGYAINFIDKLLAKYSKEYPRKTEISLIKSVDVREIATKNLKVYYDLKTGFVGTSVKDGE
FIGNASYYDKILVIRKDGTYVVKNIPDKTFIDKKNVYVGVVDINNSKEQVFSIIYRDKKDNFYYVKRFKI
DKFILDKVYRFLPEGTEILFLSTFEDFSLNLQFVPKPRQKDIVKMFRIDDFLVKGRSAIGKRISSREVKK
VKFKK
>gnl|CDD|236599 PRK09632, PRK09632, ATP-dependent DNA ligase; Reviewed
AAADRETVEVDGHRVTLTNLDKVLYPATGTTKAEVIDYYAAIAPVMLPHIAGRPVTRKRWPNGVDGEVFF
EKNLASSAPDWLPRATIQHSDGTTTYPLVDSAAGLAWLAQQAALEVHVPQWRFDAEGGELNPGPATRLVF
DLDPGEGVGLAECAEVARAVRDLLADIGLETFPVTSGSKGIHLYAPLDGPVSSEGASVVAKEVARALEQD
HPDLVTSTMTKSLRAGKVFVDWSQNNGSKTTIAPYSLRGREHPTVAAPRTWEELDDPGLRQLEYDEVLAR
VARDGDLLAPLDADLPVDDRLTKYRSMRDASKTPEPVPAAPPVAGDGNTFVIQEHHARRLHYDFRLERDG
VLVSWAVPKNLPTTPSVNHLAVHTEDHPLEYATFEGTIPKGEYGAGEVTIWDSGTYETEKWRDGEVIVTL
HGERIGGRYALIRTGGDNWLAHLMKDQAPGASPKAEEADDLAPMLATAGTVAGLKASQWAFEGKWDGYRL
LAEADHGALRLRSRSGRDVTAEYPELAALAEDLADHHVVLDGEIVALDDSGVPSFGLLQNRGRDTRVEFW
AFDLLYLDGRSLLRKPYRDRRKLLEALAPSGGSLTVPPLLPGDGAEALAYSRELGWEGVVAKRRDSTYQP
GRRSSSWIKDKHWRTQEVVIGGWRPGEGGRSSGIGSLLLGIPDPGGLRYVGRVGTGFTERELASLKETLA
PLHRDTSPFDADLPAADAKGATWVRPELVGEVRYSEWTPDGRLRQPSWRGLRPDKKPGDVVRES
>gnl|CDD|182006 PRK09633, ligD, DNA ligase D
MKPMQPTLTTSIPIGDEWRYEVKYDGFRCLLIIDETGITLISRNGRELTNTFPEIIEFCESNFEHLKEEL
PLTLDGELVCLVNPYRSDFEHVQQRGRLKNTEVIAKSANARPCQLLAFDLLELKGESLTSLPYLERKKQL
DKLMKAAKLPASPDPYAKARIQYIPSTTDFDALWEAVKRYDGEGIVAKKKTSKWLENKRSKDWLKIKNWR
YVHVIVTGYDPSNGYFTGSVYKDGQLTEVGSVKHGMEDEERQTLRAIFKQNGTKTKSGEYTLEPSICVTV
ACITFDGGTLREPSFVSFLFDMDPTECTYQQLQRQLAPLPPKVEITSLDKPIWPKIHKTKADYLLYLQEV
SPFLLPFLRDRALTVIRYPHGSGGESFYQKNKPDYAPDFVQSARDDEIEYIVCNDLSTLLWLGNQLALEF
HIPFQTIDSTRPTEIVFDLDPPSRDEFPLAVEAALELKRLFDQFGLTSFVKTSGNKGLQLYIPLSKNAFT
YEETRLFTEFIAEYLCSQFPELFTTERLKKNRGNRLYLDYVQHAEGKTIIAPYSTRGNELGTVATPLYWD
EVNSDLSPDQFTIPAVIERIKEIGCPFASFRRNPQDEPFKAVLDQLKEKS
>gnl|CDD|182008 PRK09635, sigI, RNA polymerase sigma factor SigI; Provisional
MSQHDPVSAAWRAHRAYLVDLAFRMVGDIGVAEDMVQEAFSRLLRAPVGDIDDERGWLIVVTSRLCLDHI
KSASTRRERPQDIAAWHDGDASVSSVDPADRVTLDDEVRLALLIMLERLGPAERVVFVLHEIFGLPYQQI
ATTIGSQASTCRQLAHRARRKINESRIAASVEPAQHRVVTRAFIEACSNGDLDTLLEVLDPGVAGEIDAR
KGVVVVGADRVGPTILRHWSHPATVLVAQPVCGQPAVLAFVNRALAGVLALSIEAGKITKIHVLVQPSTL
DPLRAELGGG
>gnl|CDD|236600 PRK09636, PRK09636, RNA polymerase sigma factor SigJ; Provisional
MTMADAAAEFEPLRPHLLSVAYRMLGSVADAEDIVQEAWLRWNNADRAQIRDPRAWLTRVVTRLCLDRLR
SARHRRETYVGPWLPEPVVEELDDPLEAVVAAEDLSLALMLALERLSPLERAAFLLHDVFGVPFDEIAST
LGRSPAACRQLASRARKHVRAARPRFPVSDEEGAELVEAFFAALASGDLDALVALLAPDVVLHADGGGKV
PTALRPIYGADKVARFFLGLARRYGPGGSTLVRLALVNGLPGFVTAEADGEPQTTALEVEDGKIVAIYDV
RNPDKLTHLPLKI
>gnl|CDD|236601 PRK09637, PRK09637, RNA polymerase sigma factor SigZ; Provisional
MKLESIWSEYKAQLKAFLHSRVSNEADVDDLLQEVLIKTHSNLHSLKDGSSIKSWLYQIANNTIIDFYRK
KNRSEELPDDLLFEDEEREENAKKELAPCLRPFIDALPEKYAEALRLTELEGLSQKEIAEKLGLSLSGAK
SRVQRGRVKLKELLEGCCDFEIDRQGNLIDYEQKSTECKKC
>gnl|CDD|182010 PRK09638, PRK09638, RNA polymerase sigma factor SigY; Reviewed
MQMDEKELIQKAKKGDDAALTTLFQQHYSFLYKYLLKLTLDPDLAEDLVQETMLKAIENLSSFQGRSKFS
TWLISIASRLYKDHLRKQKREKLRLQRAKEETLRKEKWEAAIKGAEWSEMLDALSKLDPEFRAPVILKHY
YGYTYEEIAKMLNIPEGTVKSRVHHGIKQLRKEWGQ
>gnl|CDD|236602 PRK09639, PRK09639, RNA polymerase sigma factor SigX; Provisional
SDETFEDLFEQYYPDVVQQIFYIVKDRTQAEDLAQEVFLRLYRSDFKGIENEKGWLIKSARNVAYNYLRS
EKRRRARILGEFQWQEVDNEPSPEEIWIRKEEITKVQEVLAKMTERDRTVLLLRFSGYSYKEIAEALGIK
ESSVGTTLARAKKKFRKIYEQMEEEE
>gnl|CDD|236603 PRK09640, PRK09640, RNA polymerase sigma factor SigX; Reviewed
MRYDPRELNDEELVARVHVELFHVTRAYEELMRRYQRTLFNVCARYLGNDRDADDVCQEVMLKVLYGLKN
FEGKSKFKTWLYSITYNECITQYRKERRKRRLMDALSLDPLEEASEEKAPKPEERGGLDRWLVHVNPIDR
EILVLRFVAELEFQEIADIMHMGLSATKMRYKRALDKLREKFAGLAET
>gnl|CDD|182012 PRK09641, PRK09641, RNA polymerase sigma factor SigW; Provisional
MDLLIKRLIKQVKKGDQNAFAELVDLYKDKIYQLCYRMLGNRHEAEDAAQEAFIRAYVNIDSYDINRKFS
TWLYRIATNLTIDRLRKRKPDYYLDAEVAGTEGLTMYSQLAADDALPEEQVVSLELQETIQEAILQLPEK
YRTVIVLKYIEDLSLKEISEILDLPVGTVKTRIHRGREALRKQLRHL
>gnl|CDD|170031 PRK09642, PRK09642, RNA polymerase sigma factor
MQTYRHYIFQVIFSILRHEEDAKDVTQEVFVKIHASLPNYQFRGLKTWMARIATNHAIDYKRKKARENEE
LSLCKETEENIKSSHNIEDLLLTKEQKLLIAQKLRELPENYRDVVLAHYLEEKSYQEIALQEKIEVKTVE
MKLYRARKWIKKHWKEEEFL
>gnl|CDD|236604 PRK09643, PRK09643, RNA polymerase sigma factor SigM; Reviewed
MGYCPAVGFGERSDAELLAAHVAGDRYAFGELFRRHHRRLWAVARRTSGTREDAADALQDAMLSAHRAAG
SFRGDAAVSSWLHRIVVNACLDRLRRAKARPTVPLDDVYPVAQLERDPTARVETALAVQRALMRLPVEQR
AALVAVDMQGYSVADAARMLGVAEGTVKSRCARGRARLAELLGYLRAGGNAS
>gnl|CDD|170033 PRK09644, PRK09644, RNA polymerase sigma factor SigM; Provisional
MEIEEIYKMYINDVYRYLFSLTKSHHAAEDLLQETFYRAYIYLEDYDNQKVKPWLFKVAYHTFIDFVRKE
KKVSFVGTDEIEAIQAESTEEYVVAKNSYEKLIQIIHTLPVIEAQAILLCDVHELTYEEAASVLDLKLNT
YKSHLFRGRKRLKALLKEEKSQNDK
>gnl|CDD|236605 PRK09645, PRK09645, ECF RNA polymerase sigma factor SigL
SGMATAEAALMRALYDEHAAPLWRYALRLTGDRARAEDVVQETLLRAWQHPEVLADTGRSARAWLFTVAR
NLVIDERRSARARPVEGGDDVLGVPEQSAPDEVDRALDRLLVADALAQLSPEHRAVLVRSYYRGWSTAQI
AADLGIPEGTVKSRLHYALRALRLALQERGVTR
>gnl|CDD|182015 PRK09646, PRK09646, ECF RNA polymerase sigma factor SigK
MKAAVPMTGPPAESPDLDALLRRVARGDQDAFAELYDRTSSRVYGLVRRVLRDPGYSEETTQEVYLEVWR
TASRFDPARGSALAWLLTLAHRRAVDRVRSEQAASQREVRYGARNVDPAFDQVAEEVEARLERERVRDCL
DALTDTQRESVTLAYYGGLTYREVAERLAVPLGTVKTRMRDGLIRLRDCLGVSS
>gnl|CDD|236606 PRK09647, PRK09647, RNA polymerase sigma factor SigE; Reviewed
RDDDWVEPSDELTGTAVFDATGDKATMPSWEELVRQHADRVYRLAYRLSGNQHDAEDLTQETFIRVFRSL
QNYQPGTFEGWLHRITTNLFLDMVRRRARIRMEALPEDYDRVPGDEPNPEQIYHDARLDPDLQAALDSLP
PEFRAAVVLCDIEGLSYEEIAATLGVKLGTVRSRIHRGRQQLRAALAAHAPHAECAALLNPAR
>gnl|CDD|236607 PRK09648, PRK09648, RNA polymerase sigma factor ShbA
SAAMTDTGEELDALVAEAVAGDRRALREVLEIIRPLVVRYCRARLGGVERPGLSADDVAQEVCLAVITAL
PRYRDQGRPFLAFVYGIAAHKVADAHRAAGRDKAVPTEEVPERPSDDAGPEERALRSESSNRMRELLDTL
PEKQREILILRVVVGLSAEETAEAVGSTPGAVRVAQHRALARLRAEIEA
>gnl|CDD|137458 PRK09649, PRK09649, RNA polymerase sigma factor SigC; Reviewed
MTATASDDEAVTALALSAAKGNGRALEAFIKATQQDVWRFVAYLSDVGSADDLTQETFLRAIGAIPRFSA
RSSARTWLLAIARHVVADHIRHVRSRPRTTRGARPEHLIDGDRHARGFEDLVEVTTMIADLTTDQREALL
LTQLLGLSYADAAAVCGCPVGTIRSRVARARDALLADAEPDDLTG
>gnl|CDD|182018 PRK09651, PRK09651, RNA polymerase sigma factor FecI; Provisional
SDRATTTASLTFESLYGTHHGWLKSWLTRKLQSAFDADDIAQDTFLRVMVSETLSTIRDPRSFLCTIAKR
VMVDLFRRNALEKAYLEMLALMPEGGAPSPEERESQLETLQLLDSMLDGLNGKTREAFLLSQLDGLTYSE
IAHKLGVSVSSVKKYVAKATEHCLLFRLEYGL
>gnl|CDD|236608 PRK09652, PRK09652, RNA polymerase sigma factor RpoE; Provisional
VERVQRGDRAAFALLVRRYQPRVKRLLSRLTRDPADAEDLVQETFIKAYRALHSFRGGAAFYTWLYRIAR
NTAINYLRKQGRRPPASDVDAEEAEDFDLADALRDISTPENELLSAELEQRVRAAIESLPEELRTAITLR
EIEGLSYEEIAEIMGCPIGTVRSRIFRAREALRAKLQPLLDE
>gnl|CDD|236609 PRK09653, eutD, phosphotransacetylase
MDLFESLKEKAKGKKKKIVLPEGEDERVLKAAKRLQKEGLVEPILLGNPEEIRAKAKELGLDLDGVEIID
PETYPLLEEFAEAFVELRKGKGTEEDAAELLKDPNYFGTMLVKLGKADGMVSGAIHSTADTLRPALQIIK
TKPGVKTVSSVFIMVKGDERYIFADCAVNPNPTAEQLAEIAINSAETAKAFGIDPKVAMLSFSTKGSAKG
PEVDKVQEATEIAKELAPDLKIDGELQFDAAFVPEVAAKKAPGSPVAGKANVFVFPSLEAGNIGYKIAQR
LGGFEAVGPILQGLNKPVNDLSRGCSVEDIYNLALITAAQAQGE
>gnl|CDD|182021 PRK09662, PRK09662, GspL-like protein; Provisional
VIHQQHMRNIAQWLQANGITRATVAPDWMSIPCGFMAGDAQRVICRIDECRGWSAGRALAPVMFRAQLNE
QDLPLSLTVVGIAPEELSAWAGADAERLTVTALPAITTYGEPEGNLLTGPWQPRVSYRKQWARWRVMILP
ILLILVALAVERGVTLWSVSEQVAQSRTQAEKQFLTLFPEQKRIVNLRSQVTMALKKYRPQADDTRLLAE
LSAIASTLKSASLSDIEMRGFTFDQKRQTLHLQLRAANFASFDKLRSALATDYVVQQDALQKEGDAVSGG
VTLRRK
>gnl|CDD|182022 PRK09664, PRK09664, low affinity tryptophan permease TnaB
MTDQAEKKHSAFWGVMVIAGTVIGGGMFALPVDLAGAWFFWGAFILIIAWFSMLHSGLLLLEANLNYPVG
SSFNTITKDLIGNTWNIISGITVAFVLYILTYAYISANGAIISETISMNLGYHANPRIVGICTAIFVASV
LWISSLAASRITSLFLGLKIISFVIVFGSFFFQVDYSILRDATSTTAGTSYFPYIFMALPVCLASFGFHG
NIPSLIICYGKRKDKLIKSVVFGSLLALVIYLFWLYCTMGNIPRESFKAIISSGGNVDSLVKSFLGTKQH
GIIEFCLLVFSNLAVASSFFGVTLGLFDYLADLFKIDNSHGGRFKTVLLTFLPPALLYLIFPNGFIYGIG
GAGLCATIWAVIIPAVLAIKARKKFPNQMFTVWGGNLIPAIVILFGITVILCWFGNVFNVLPKFG
>gnl|CDD|182023 PRK09665, PRK09665, PTS galactitol transporter subunit IIA
MSNLFVRTGISFVDRSEALTHIGNEMLAKGVVHDTYPQALIAREAEFPTGIMLEQHAVAIPHCEAIHAKS
PAIYLIRPDKKVHFQQADDDNDVAVSLVIALIVENPQQQLKLLRCLFGKLQQPDIVETLLTLPETQLKEY
FTKYVLDSDE
>gnl|CDD|236610 PRK09669, PRK09669, putative symporter YagG; Provisional
MNTSQLTTKDKIGYGLGDTACNLVWQTVMLFLAYFYTDVFGLSAAIMGTMFLVVRVLDAVTDPLMGALVD
RTRTRHGQFRPYLLWFAIPFGVVCLLTFYTPDFGATGKIIYACVTYILLSLVYTAINVPYCAMPGAITND
PRERHSLQSWRFALSFIGGLIVSVIALPLVDILGKGDEQKGYFYAMMVMGLLGVVLFFCCFFMTKERYTP
EVDNSSSVWKDLKLLLGNSQWRIMFIFNVVLLTAVVTRGGATLYYVNYVLLRPDLATLFLVTGMIAGLFG
ALLSERLLGKFDRVRAFKWTIVAFVILSALIFFIPPSNVWLIFALNILFNFIQNLTTPLQWSMFSDVVDY
EEKRSGRRLDGLVFSTNLFAIKLGLAIGGAVVGWILAWVDYVGGAAVQSASVLTTINLLFTVIPGVLFAG
MAIILNFYKLNDARVEAIAQELVK
>gnl|CDD|236611 PRK09672, PRK09672, phage exclusion protein Lit; Provisional
MNSALQHLQVEIKALASRVAPENENELEDLSNIHDIKVLVVEDSGGFNFRVGKKTGEITITETSLEYLWL
FSLAAWVLYEEYSQAQLLAEDGEQNLDLETINGLDKSRDLSEYLLNRAETLESIIEELSSVHTNWPENLP
NPEADKEISVEEDQEVANDLFLCALAWILLHEIAHVEFQHSSLESNEDSIQEEKEADSYATNWLLSKSEK
YAPSKKRSVGIAIALLFLQELELENKSCGKGTHPDADQRIFANLSKLEISDESGIWLLQAMLIVTLFRQT
KIDFLPMTCLTFKDVLGDLLAQIKE
>gnl|CDD|182026 PRK09674, PRK09674, enoyl-CoA hydratase-isomerase; Provisional
MSELLVSRQQRVLLLTLNRPEARNALNNALLTQLVNELEAAATDTSIGVCVITGNARFFAAGADLNEMAE
KDLAATLNDPRPQLWQRLQAFNKPLIAAVNGYALGAGCELALLCDIVIAGENARFGLPEITLGIMPGAGG
TQRLIRSVGKSLASQMVLTGESITAQQAQQAGLVSEVFPPELTLERALQLASKIARHSPLALRAAKQALR
QSQEVDLQAGLAQERQLFTLLAATEDRHEGISAFLEKRTPDFKGR
>gnl|CDD|137467 PRK09677, PRK09677, putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
LKLAKRYGLCGFIRLVRDVLLTKVFYRNCRIIRFPFYIRNDGSINFGEGFTSGVGLRLDAFGRGKLFFGD
NVQVNDYVHIACIESITIGRDTLIASKVFITDHNHGSFKHSDDFSSPNLPPDMRTLESSAVVIGQRVWIG
ENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNHETKLWE
>gnl|CDD|137468 PRK09678, PRK09678, DNA-binding transcriptional regulator; Provisional
MFHCPLCQHAAHARTSRYITDTTKERYHQCQNVNCSATFITYESVQRYIVKPGEVHAVRPHPLPSGQQIM
WM
>gnl|CDD|182027 PRK09681, PRK09681, putative type II secretion protein GspC; Provisional
MFWLMLLIISAKMAHSLWRYFSFSAEYTAVSPSANKPPRADAKTFDKNDVQLISQQNWFGKYQPVAAPVK
QPEPAPVAETRLNVVLRGIAFGARPGAVIEEGGKQQVYLQGETLGSHNAVIEEINRDHVMLRYQGKIERL
SLAEEERSTVAVTNKKAVSDEAKQAVAEPAVSAPVEIPAAVRQALAKDPQKIFNYIQLTPVRKEGIVGYA
VKPGADRSLFDASGFKEGDIAIALNQQDFTDPRAMIALMRQLPSMDSIQLTVLRKGARHDISIALR
>gnl|CDD|236612 PRK09685, PRK09685, DNA-binding transcriptional activator FeaR; Provisional
HTNPSADNEFQQWLSQINQVCGRFDGRPLTNRFIGELSTHDAGGLKLSTVTTNAVNLSRTWQEIKHSDDA
HFFTVFQLSGHAIIEQDDRQVQLAAGDITLIDASRPCSIYPQGLSEQISLLLPRELVEQYFPGQKPACAG
RLSASLPMVQLSHRLLQQSMNGPALSETESEALLEALIALLRPALHQRESVQPRRERQFQKVVALIDQSI
QEEILRPEWIAGELGISVRSLYRLFAEQGLVVAQYIRNRRLDRCADDLRPAADDEKITSIAYKWGFSDSS
HFSTAFKQRFGVSPGEYRRKFR
>gnl|CDD|170047 PRK09687, PRK09687, putative lyase; Provisional
MSNSYKKRKASKEYSLYSQCKKLNDDELFRLLDDHNSLKRISSIRVLQLRGGQDVFRLAIELCSSKNPIE
RDIGADILSQLGMAKRCQDNVFNILNNLALEDKSACVRASAINATGHRCKKNPLYSPKIVEQSQITAFDK
STNVRFAVAFALSVINDEAAIPLLINLLKDPNGDVRNWAAFALNSNKYDNPDIREAFVAMLQDKNEEIRI
EAIIGLALRKDKRVLSVLIKELKKGTVGDLIIEAAGELGDKTLLPVLDTLLYKFDDNEIITKAIDKLKRS
>gnl|CDD|182029 PRK09689, PRK09689, prophage protein NinE; Provisional
MATPLIRVMNGHIYRVPNRRKRKPELKPSEIPTLLGYTASLVDKKWLRLAARRNHG
>gnl|CDD|170049 PRK09692, PRK09692, integrase; Provisional
MARQTKPLTDTEIKAAKPKEADYVLYDGDGLELLIKSSGSKIWQFRYYRPLTKTRAKKSFGPYPSVTLAD
ARNYRAESRSLLAKQIDPQEHQQEQLRSSLEAKTNTFQLVAERWWNVKKASVTEDYAEDIWRSLERDVFP
AIGDISVTDIKAHTLVQAVQPVQARGALETVRRLCQRINEVMIYAQNTGLIDAVPSVNIGKAFEKPQKKN
MPSIRPDQLPQLMQTMRTASISLSTRCLFMWQLLTITRPAEAAEARWEEIDIEAQEWKIPAARMKMNRDH
TVPLSDEALAILEMMKPLSGNREFIFPSRIKPNQPMNSQTVNAALKRAGLGGVLVSHGLRSIASTALNEQ
GFPPDVIEAALAHVDKNEVRRAYNRSDYLEQRRPMMQWWADFVMAADSGSMIEGGIKGMKLVG
>gnl|CDD|236613 PRK09693, PRK09693, Cascade antiviral complex protein; Validated
MNLLKDDWIPVRPLGGGKVQKITLQTLLCSDQRWQLSLPRDDMELAALQLLICLTQVLLPPTDDVELKDR
IMNPLTEDEFEEGIAPWIDMFDLNHPEQPFMQTKGVVAKDVTPMTKLLAGLEGGTNAAFVNQPGQGEALC
GGCTAIALFNQAMNAPGFGGGFKSGLRGGGPITTLVAGENLRTTVLLNVLTEDRLQTFFPLWSHTESQPT
WIAPIKSGEVIPASSIGLARGLFWQPAHIELCIPDGIGKCSCCGQESEQRYTGFLKEKFNFTVNGLWPHP
HSPLIVRVKKGEVEEKFCAFTTSAPSWTQLSRYVVGKEIQNEEGNRPAAVVNQARNLAPGRPLRLIVGGY
RNNQASILERRHDLLSFNQGWQKHGSVINEIVTLGLGYKEALRKALNTFAEGFKKKDFKGAGVSVHETAM
RRFYRQSEQIILDTLADVDFKQADELRAGAVDKLHQLCEMLFNQSVAPYAHHPKLIKTLAKARATLYKH
>gnl|CDD|182031 PRK09694, PRK09694, CRISPR-associated helicase/endonuclease Cas3
MESFKYYCRYWGKASKSLTKGNDYHLLPYHCLDVAAVADCWWDQSPVLRSQFSANEMLSKQQVRAWLLFF
VALHDIGKFDIRFQYKAPEIWLKLNPAGPSISGPSTQMCRKYDHGAAGLLWFRQDFRSNQASDDSFFDAA
PHPYEAWFPWMEAVTGHHGYILHSQDQDDSRWEMPASLASYAEQDKQAREEWIQALEALFLTPAGLSLND
IPPPCSPLLAGFCSVSDWLGSWTTTFTFLFNSPILALRQYFQQRQQDAARVLELSGLVANKKPYGGVHAL
LDNGYQPRQLQTLVDALPLQPGLTIIEAPTGSGKTEAALAYAWRLIDQGLADSIIFALPTQATANAMLSR
LEALASKLFPSPNLILAHGNSRFNHLFQSLKSRAATEQGQEEAWVQCCEWLSQSNKRVFLGQIGVCTIDQ
VLISVLPVKHRFIRGFGLGRSVLIVDEVHAYDAYMYGLLEAVLKAQAQAGGSVILLSATLPATLKQKLLD
TYGGHDPVELSSAYPLITWRGVNGAQRFDLSAHPEQLPARFTIQLEPICLADMLPDLTLLQRMIAAANAG
AQVCLICNLVDDAQKLYQRLKELNNTQVDIDLFHARFTLNDRREKEQRVIENFGKNGKRNQGRILVATQV
VEQSLDLDFDWLITQLCPVDLLFQRLGRLHRHHRKYRPAGFEIPVATVLLPDGEGYGRSGYIYGNTRVLW
RTEQLLEEHNAASLFFPDAYREWIESVYDEAEMDEEPEWVISGMDKFEDKECEKRYKARKMLKWAEETPL
SDNDERVLALTRDGEMSLPVLPYVQTEHGKQLLDGQVLEQLDEEQQYEALALNRVNVPHTWKRSFLEVVD
EDGLIWLEGHQDADGWCWQGKNDIVITYTEDEGMTRVI
>gnl|CDD|182032 PRK09695, PRK09695, glycolate permease GlcA
MVTWTQMYMPMGGLGLSALVALIPIIFFFVALAVLRLKGHVAGAITLILSILIAIFAFKMPIDMAFAAAG
YGFIYGLWPIAWIIVAAVFLYKLTVASGQFDIIRSSVISITDDQRLQVLLIGFSFGALLEGAAGFGAPVA
ITGALLVGLGFKPLYAAGLCLIANTAPVAFGALGVPILVAGQVTGIDPFHIGAMAGRQLPFLSVLVPFWL
VAMMDGWKGVKETWPAALVAGGSFAVTQFFTSNYIGPELPDITSALVSIVSLALFLKVWRPKNTETAISM
GQSAGAMVVNKPSSGGPVPSEYSLGQIIRAWSPFLILTVLVTIWTMKPFKALFAPGGAFYSLVINFQIPH
LHQQVLKAAPIVAQPTPMDAVFKFDPLSAGGTAIFIAAIISIFILGVGIKKGIGVFAETLISLKWPILSI
GMVLAFAFVTNYSGMSTTLALVLAGTGVMFPFFSPFLGWLGVFLTGSDTSSNALFGSLQSTTAQQINVSD
TLLVAANTSGGVTGKMISPQSIAVACAATGMVGRESELFRYTVKHSLIFASVIGIITLLQAYVFTGMLVS
>gnl|CDD|182033 PRK09697, PRK09697, putative general secretion pathway protein GspB
MFEFYIAAREQKETGHPGIFSRQKHSTIIYVICLLLICLWFAGMVLVGGYARQLWVLWIVKAEVTVEAET
PAFKQSTQHYFFKKQPLPVVESVEEEDEPGVAVENAPSSSEDEENTVEESDEKAGLRERVKNALNELER
>gnl|CDD|182034 PRK09698, PRK09698, D-allose kinase; Provisional
KQKNVVLGIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAPDLVSGLGEMIDEYLRRFNARCHGIVMGFP
ALVSKDRRTVISTPNLPLTALDLYDLADKLENTLNCPVFFSRDVNLQLLWDVKENNLTQQLVLGAYLGTG
MGFAVWMNGAPWTGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRRWYEQQPRDYPLSDLFVH
AGDHPFIQSLLENLARAIATSINLFDPDAIILGGGVMDMPAFPRETLIAMIQKYLRKPLPYEVVRFIYAS
SSDFNGAQGAAILAHQRFLPQS
>gnl|CDD|182035 PRK09699, PRK09699, D-allose ABC transporter permease
KPFNFALFWDKYGTFFILAIIVAIFGSLSPEYFLTTNNITQIFVQSSVTVLIGMGEFFAILVAGIDLSVG
AILALSGMVTAKLMLAGVDPFLAALIGGVLVGGALGAINGCLVNWTGLHPFIITLGTNAIFRGITLVISD
ANSVYGFSFDFVNFFAASVIGIPVPVIFSLIVALILWFLTTRMRLGRNIYALGGNKNSAFYSGIDVKFHI
LVVFIISGVCAGLAGVVSTARLGAAEPLAGMGFETYAIASAIIGGTSFFGGKGRIFSVVIGGLIIGTINN
GLNILQVQTYYQLVVMGGLIIAAVALDRLISK
>gnl|CDD|182036 PRK09700, PRK09700, D-allose ABC transporter ATP-binding protein AlsA
MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN
KLDHKLAAQLGIGIIYQELSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLD
EKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRR
ICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVR
DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDN
GFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLI
SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI
LTNRDDMSEEEIMAWALPQE
>gnl|CDD|182037 PRK09701, PRK09701, D-allose transporter substrate-binding protein
MNKYLKYFSGTLVGLMLSTSAFAAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQS
QLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNLKKAGGNVEAFVTTDNVAV
GAKGASFIIDKLGAEGGEVAIIEGKAGNASGEARRNGATEAFKKASQIKLVASQPADWDRIKALDVATNV
LQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGL
KLMVDAEKSGKVIPLDKAPEFKLVDSILVTQ
>gnl|CDD|77355 PRK09702, PRK09702, PTS sugar transporter subunit IIB
MFSNHADMMLTQIAIGLCFTLLYFVVFRTLILQFNMCTPGREDAEVKLYSKAEYKASRGQTTAAEPKKEL
DQAAGILQALGGVGNISSINNCATRLRIALHDMSQTLDDEVFKKLGAHGVFRSGDAIQVIIGLHVSQLRE
QLDSLINSHQSAENVAITEAV
>gnl|CDD|236614 PRK09705, cynX, putative cyanate transporter; Provisional
MPSKFPLNFMLLVLVLIGLNMRPLLTSVGPLLPQLRQASGMSFSVAALLTALPVVTMGGLALAGSWLHQH
VSERRSVAISLLLIAVGALMRELYPQSALLLSSALLGGVGIGIIQAVMPSVIKRRFQQRTPLVMGLWSAA
LMGGGGLGAAITPWLVQHSETWYQTLAWWALPAVVALFAWWWQSAREVASSHKTTTTPVRVVFTPRAWTL
GVYFGLINGGYASLIAWLPAFYIEIGASAQYSGSLLALMTLGQAAGALLMPAMARHQDRRKLLMLALVLQ
LVGFCGFIWLPLQLPVLWAMVCGLGLGGAFPLCLLLALDHSVQPAIAGKLVAFMQGIGFIIAGLAPWFSG
VLRSISGNYLMDWAFHALCVVGLMIITLRFAPARFPQLWVKEA
>gnl|CDD|182039 PRK09706, PRK09706, transcriptional repressor DicA; Reviewed
MKNLTLGQRIRYRRKQLKLSQRSLAKAVKVSHVSISQWERDETEPTGKNLFALAKALQCSPTWLLFGDED
KQPTPPVPLNQPVELSEDQKELLELFDALPESEQDAQLSEMRARVENFNKLFEELLKARKRSAKK
>gnl|CDD|236615 PRK09709, PRK09709, exodeoxyribonuclease VIII
MSTKKQVYPLYYLRKNDKARKRLGEKDGFLWASAKKESTAASRGYLAVDDAGKDESDFFKPVRVNFPVVN
DLPPEGEFDTTFCERYELGSEDGMTWELIPGAASAPDNAHYQGNTNVNGEDMTEIEENMLLPISGQELPI
RWLAQHGSEKPVTHVSRDDLQALHIARAEELPAVTALAVSHKTSLLDPLEIRDLHKLVRDTDKVFPNPGN
SNLGLITAFFEAYLNADYTDRGLLTKEWMKGNRVSHITRTASGANAGGGNLTDRGEGFVHDLTSLARDVA
TGVLARSMDLDIYNLHPAHAKRIEEIIAENKPPFSVFRDKFITMPGGLDYSRAIVVASVKEAPIGIEVIP
AHVTEYLNKVLTETDHANPDPEIVDIACGRSSAPMPQRVTEEGKQDDEEKPQPSGTTADEQATAETVEPD
ATEHHQDTQPLDAQSQVNSVDAKYQELRAELHEARKNIPSKNPVDADKLLAASRGEFVEGISDPNDPKWV
KGIQTRDCVYQNQPETEKTSPEMKQPEPVVQQEPEIVCNACGQTGGDNCPDCGAVMGDATYQETFDEESQ
VEAKENDPEEMEGAEHPHNENAGSDPHRDCSDETGEVADPVIVEDIEPGIYYGISNENYHAGPGVSKSQL
DDIADTPALYLWRKNAPVDTTKTKTLDLGTAFHCRVLEPEEFSNRFIVAPEFNRRTNAGKEEEKAFLMEC
ASTGKTVITAEEGRKIELMYQSVMALPLGQWLVESAGHAESSIYWEDPETGILCRCRPDKIIPEFHWIMD
VKTTADIQRFKTAYYDYRYHVQDAFYSDGYEAQFGVQPTFVFLVASTTIECGRYPVEIFMMGEEAKLAGQ
QEYHRNLRTLADCLNTDEWPAIKTLSLPRWAKEYAND
>gnl|CDD|182042 PRK09710, lar, type I toxin-antitoxin system endodeoxyribonuclease toxin RalR
MRYDNVKPCPFCGCPSVTVKAISGYYRAKCNGCESRTGYGGSEKEALERWNKRTTGNNNGGVHV
>gnl|CDD|137485 PRK09713, focB, formate transporter
MRNKLSFDLQLSARKAAIAERIAAHKIARSKVSVFLMAMSAGVFMAIGFTFYLSVIADAPSSQALTHLVG
GLCFTLGFILLAVCGTSLFTSSVMTVMAKSRGVISWRTWLINALLVACGNLAGIACFSLLIWFSGLVMSE
NAMWGVAVLHCAEGKMHHTFTESVSLGIMCNLMVCLALWMSYCGRSLCDKIVAMILPITLFVASGFEHCI
ANLFVIPFAIAIRHFAPTSFWQLAHSSADNFPALTVSHFITANLLPVMLGNIIGGAVLVSMCYRAIYLRQ
ES
>gnl|CDD|182043 PRK09716, PRK09716, YhaC family protein
MFPVSSIGNDISSDLVRRKMNDLPESPTGNNLEALAPGIEKLKQTSIEMVTLLNTLQPGGKCIITGDFQK
ELAYLQNVILYNDSSLRLDFLGYNAQIIQRSDNTCELTINEPLKNQEISTGNINVNCPLKDIYNEIRRLN
VIFSCGTGDIVDLSSLDLRNVDLDYYDFTDKHMANTILNPFKLNSTNFTNANMFQVNFVSSTQNATISWD
YLLKITPVLTSISDMYSEEKIKFVESCLNELGDITEEQLKIMRFAIIKSIPRATLTDKLENELTKEIYKS
SSKINNCLNRIKLPEMIDFSSEKIHDYIDIIIEDYENIKENAYLVIPQINYTMDLNIEDSSSEELLSDNT
LEKDENSPDNGFEVGEYNTYEAYNSENQYFTREDYTYNYDLLNAI
>gnl|CDD|182044 PRK09717, PRK09717, stationary phase growth adaptation protein; Provisional
MKQEVEKWRPFGHPDGDIRDLSFLDAHQAVYVQHHEGKEPLEYRFWVTYSLHCFTKDYEHQTNEEKQSLM
YHAPKESRPFCQHRYNLARTHLKRTILALPESNVIHAGYGSYAVIEVDLDGGDKAFYFVAFRAFREKKKL
RLHVTSAYPISEKQKGKSVKFFTIAYNLLRNKQLPQPSK
>gnl|CDD|182045 PRK09718, PRK09718, SopA family protein
IKHGVVQGNNIVDFDLLRNFNGGPGLNRENFIYISNIFLNIKQRNEKNHSINMFREVSISGDIVSVKFYR
NEKIECACDFLMDKDAQGYIDLSDLDLTSCHFKGDVISKVSFLSSNLQHVTFECKEIGDCNFTTAIVDNV
IFKCRRLHNVIFIKASGEYVDFSKNILDTVDFSQSQLTHSNFRECQIRNSNFDNCYLYASHFTRAEFLSA
KEISFIKSNLTAVMFDHVRISTGNFKDCITEQLELTIDYSDIFGNEDLDGYINNIIKMIDTLPDNAMILK
SVLAVKLVMQLKILNIVNKNFIENMKKIFSHCPYIKDPIIRSYIHPDEDNKFDNFMRQNRFSKVNFDTQQ
MIDFINRFNMNKWLIDKNNNFFIQLIDQALRSTDDTIKANAWHLYKEWIRSDDVSPLFIEIEDNLRTFNT
NELTRNDNIFILFSSVDDGPVMVVSSQRLHDMLNPTKDTNWNSTYIYKSRHEMLPVNLTPETLFGSKSHD
KHALFPIFTASWRANRIKNKGI
>gnl|CDD|182046 PRK09719, PRK09719, hypothetical protein; Provisional
MHRVTYPCLTSRRFQLALIHRRVVDKRTSMHSRTASESTGARIHRPWCARHQVRPAWRCQYDKLHRVPFR
SPELRLDSGPGYTTGSYRY
>gnl|CDD|182047 PRK09720, cybC, cytochrome b562; Provisional
METLNDNLKVVEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDAL
KLANEGKVKEAQAAAEQLKTTRNSYHKKYR
>gnl|CDD|236616 PRK09722, PRK09722, allulose-6-phosphate 3-epimerase; Provisional
MRMKISPSLMCMDLLKFKEQIEFLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTD
PQDYIDQLADAGADFITLHPETINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVD
PGFAGQPFIPEMLDKIAELKALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGTSGLFNLDEDIDE
AWDIMTAQIEAATGEVQPH
>gnl|CDD|236617 PRK09723, PRK09723, fimbrial-like adhesin
MKKFFRYFLFLALCLSCYTASAGTDDNVSYIVGNYYGVGPSDQKWNETGPSGDATVTFRYATSTNNLVFY
KPTQLGPTGVKLYWSQLDTASGGGFLYCNRSGNTSGGPMTIEHAMVDSGKMYNGHKLFKTSVPGLYYTLE
ISNMWSAYTNISSPGIYIGDSSEQYFNWSNPSEDTLYWSCNNANSTNKYWAVGGIVQTLTIEFYTDTNFN
PTGAQQVSLSLSKNYLYSFKAYGAGSGINEHSYFLKIDFDLTNLKLTNPTCFTSALSGTSVTGSTVKMGE
YSAEQIKNGATPVPFDISLQNCVRVRNIETKLVSTKVGTENKQLLGNTLTGNDAAKGVGVLIEGLKNSKS
PQMTLKPNDSTSVYKDYETPDEDDTTGGIYPDQGNGTTQPLHFQATLKQDGNIAIEPGEFKATSTFQVTY
P
>gnl|CDD|182049 PRK09726, PRK09726, type II toxin-antitoxin system antitoxin HipB
MMSFQKIYSPTQLANAMKLVRQQNGWTQSELAKKIGIKQATISNFENNPDNTTLTTFFKILQSLELSMTL
CDAKNASPESTEQQDLEW
>gnl|CDD|137493 PRK09727, PRK09727, his operon leader peptide; Provisional
MTRVQFKHHHHHHHPD
>gnl|CDD|182050 PRK09729, PRK09729, hypothetical protein; Provisional
MNFIRQGLGIALQPELTLKSIAGELCSVPLEPTFYRQISLLAKEKPVEGSPLFLLQTCTEQLVVNGKI
>gnl|CDD|182051 PRK09730, PRK09730, SDR family oxidoreductase
MAIALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMF
TAIDQHDEPLAALVNNAGILFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSGGAIVNV
SSAASRLGAPGEYVDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGRVDRVKSNI
PMQRGGQPEEVAQAIVWLLSDKASYVTGSFIDLAGGK
>gnl|CDD|182052 PRK09731, PRK09731, type II secretion system protein
MLRDKFIHYFQQWRERQLSRGEHWLAQHLAGRSPREKGMLLAAVVFLFSVGYYVLIWQPLSERIEQQETM
LQQLVAMNTRLKSAAPDIIAARKSATTTPAQVSRVISDSASAHSVVIKRIAERGENIQVWIEPVVFNDLL
NWLNALDEKYALRVTQIDVSAAEKPGMVNVQRLEFGRG
>gnl|CDD|170072 PRK09732, PRK09732, hypothetical protein; Provisional
MKTKVILSQQMASAIIAAGQEEAQKNNWSVSIAVADDGGHLLALSRMDDCAPIAAYISQEKARTAALGRR
ETKGYEEMVNNGRTAFVTAPLLTSLEGGVPVVVDGQIIGAVGVSGLTGAQDAQVAKAAAAVLAK
>gnl|CDD|182053 PRK09733, PRK09733, fimbrial-like protein
AFKKSLLVAGVAMILSNNVFADEGHGIVKFKGEVISAPCSIKPGDEDLTVNLGEVADTVLKSDQKSLAEP
FTIHLQDCMLSQGGTTYSKAKVTFTTANTMTGQSDLLKNTKETEIGGATGVGVRILDSQSGEVTLGTPVV
ITFNNTNSYQELNFKARMESPSKDATPGNVYAQADYKIAYE
>gnl|CDD|236618 PRK09736, PRK09736, 5-methylcytosine-specific restriction enzyme subunit McrC; Provisional
MSQGMIPIRNIYYMLSYAFDLLREQDYKDIATEEFDNLPDLLAEILAKGVERRLKRGLGRGYRSRTEVLS
RVRGRIDFSKTIRGRLLQRGKLVCRFDELSEDTLRNRIIKSTLELLIRHDIDKDIKDRLRSLLVYFGGVS
TIDPSRIEWSYLQYGRNNQDYKFLISVCKLVVNGLLPTENSGNKRLMDFERDEKRMSRLYEKFVLGFYRR
ELPSDPSIVVTASYIKWALDSITDGSDELLPIMKTDITLDSKDKRLIIDAKYYSSLTQGRYDKEKLHSNN
LYQIFAYLKNQEGSGDLADTASGLLLYPKVDEDVDEVYVIQGHRIRVATVDLGQPFSSIRSQLLRIVDNY
FA
>gnl|CDD|236619 PRK09737, PRK09737, type I restriction-modification system specificity subunit
MSAGKLPEGWVTTHISEICSVIRGVKPPKGYATKSLTMGDLPFIRTTDITNGAVDLTTLPYCMDAPEDVS
KYQLQDRDIVISSAGSIGFSFLAQNPLPSNVVFASFAIRLKPVNYFSEYFLKHFLESSDYRNQLSLMSAG
NAVQNINAQSLSTLTFPIPPIAEQKIIAEKLDTLLAQVDSTKARLEQIPQILKRFRQAVLGAAVSGKLTE
EWRWPDLPSTWSVHKYSELVDSRLGGMSSKANNFGSATPYLRNINVRWGSFDLEDLQDILISDIERRELK
LKLGDVLFCRGNEPLEVGRCAIWKEPQDIPVIYQKALIRARVKDDIIPEYLVYNLKSPDSRNISLSQLFT
GTTQKHITGKALANYPIRVPPLEEQAEIVRRVEQLFAYADTIEKQVNNALARVNNLTQSILAKAFRGELT
AQWRAENPSLISGENSAAALLEKIKAERAASGGKKASRKKS
>gnl|CDD|182055 PRK09738, PRK09738, small toxic polypeptide; Provisional
MKLPRSPLVWCVLIVCLTLLIFTYLTRKSLCELRYRDGDREVAAFMAYESGK
>gnl|CDD|236620 PRK09739, PRK09739, NAD(P)H oxidoreductase
MQSMRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPEDEPDWKNPDKRYSPEV
HQLYSELLEHDALVFVFPLWWYSFPAMLKGYIDRVWNNGLAYGDGHKLPFNKVRWVALVGGSKESFVKRG
WEKNMSDYLNVGMASYLGIEDSDVTFLYNTLVFDGEELHASHYQSLLSQAREMVDALAK
>gnl|CDD|182057 PRK09741, PRK09741, hypothetical protein; Provisional
PQDGIKLHRSNFTAIGQQLQPYLETGKCFRIIIKPWREKRSLSQNALSHMWYSEISEYLISRGKTFATPA
WVKEALKHTYLGYETVELVDVVTGEITTIQSLRHTSDLDTGEMYVFLCKVEAWAMNIGCHLTIPQSCEYQ
LLRDKQEA
>gnl|CDD|137503 PRK09744, PRK09744, DNA-binding transcriptional regulator DicC; Provisional
MLKIDAIAFFGSKTKLANAAGVRLASVAAWGELVPEGRAMRLQEASGGELQYDPKVYDEYRKAKRAGRLN
NENHS
>gnl|CDD|182058 PRK09750, PRK09750, hypothetical protein; Provisional
MYMYKITATIEKEGGTPTNWTRYSKSKLTKSECEKMLSGKKEAGVSREQKVKLINFNCEKLQSS
>gnl|CDD|137505 PRK09751, PRK09751, putative ATP-dependent helicase Lhr; Provisional
VIAPTGSGKTLAAFLYALDRLFREGGEDTREAHKRKTSRILYISPIKALGTDVQRNLQIPLKGIADERRR
RGETEVNLRVGIRTGDTPAQERSKLTRNPPDILITTPESLYLMLTSRARETLRGVETVIIDEVHAVAGSK
RGAHLALSLERLDALLHTSAQRIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRHPQIRIVVPVANMDDV
SSVASGTGEDSHAGREGSIWPYIETGILDEVLRHRSTIVFTNSRGLAEKLTARLNELYAARLQRSPSIAV
DAAHFESTSGATSNRVQSSDVFIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVI
QVATPLSVASGLQRIGRAGHQVGGVSKGLFFPRTRRDLVDSAVIVECMFAGRLENLTPPHNPLDVLAQQT
VAAAAMDALQVDEWYSRVRRAAPWKDLPRRVFDATLDMLSGRYPSGDFSAFRPKLVWNRETGILTARPGA
QLLAVTSGGTIPDRGMYSVLLPEGEEQAGSRRVGELDEEMVYESRVNDIITLGATSWRIQQITRDQVIVT
PAPGRSARLPFWRGEGNGRPAELGEMIGDFLHLLADGAFFSGTIPPWLAEENTIANIQGLIDEQRNATGI
VPGSRHLVLERCRDEIGDWRIILHSPYGRRVHEPWALAIAGRIHALWGADASVVASDDGIVARIPDTDGK
LPDAAIFLFEPEKLLQIVREAVGSSALFAARFRECAARALLMPGRTPGHRTPLWQQRLRASQLLEIAQGY
PDFPVILETLRECLQDVYDLPALERLMRRLNGGEIQISDVTTTTPSPFATSLLFGYVAEFMYQSDAPLAE
RRASVLSLDSELLRNLLGQVDPGELLDPQVIRQVEEELQRLAPGRRAKGEEGLFDLLRELGPMTVEDLAQ
RHTGSSEEVASYLENLLAVKRIFPAMISGQERLACMDDAARLRDALGVRLPESLPEIYLHRVSYPLRDLF
LRYLRAHALVTAEQLAHEFSLGIAIVEEQLQQLREQGLVMNLQQDIWVSDEVFRRLRLRSLQAAREATRP
VAATTYARLLLERQGVLPATDGSPALFASTSPGVYEGVDGVMRVIEQLAGVGLPASLWESQILPARVRDY
SPEMLDELLATGAVIWSGQKKLGEDDGLVALHLQEYAAESFTPAEADQANRSALQQAIVAVLADGGAWFA
QQISQRIRDKIGESVDLSALQEALWALVWQGVITSDIWAPLRALTRSSSNARTSTRRSHRARRGRPVYAQ
PVSPRVSYNTPNLAGRWSLLQVEPLNDTERMLALAENMLDRYGIISRQAVIAENIPGGFPSMQTLCRSME
DSGRIMRGRFVEGLGGAQFAERLTIDRLRDLATQATQTRHYTPVALSANDPANVWGNLLPWPAHPATLVP
TRRAGALVVVSGGKLLLYLAQGGKKMLVWQEKEELLAPEVFHALTTALRREPRLRFTLTEVNDLPVRQTP
MFTLLREAGFSSSPQGLDWG
>gnl|CDD|182059 PRK09752, PRK09752, AIDA-I family autotransporter YfaL
MRIIFLRKEYLSLLPSMIASLFSANGVAAVIDSCQGYDIKASCQASRQSLSGITQDWSIADGQWLVFSDM
TNNASGGAVFLQQGAEFTLSPENETGMTLFANNTVSGEYNNGGAIFAKENSTLNLTDVIFSGNVAGGYGG
AIYSSGTNDTGAVDLRVTNAMFRNNIANDGKGGAIYTINNDVYLSDVIFDNNQAYTSTSYSDGDGGAIDV
TDNNSDSKHPSGYTIINNTAFTNNTAEGYGGAIYTNSATAPYLIDISVDDSYSQNGGVLVDENNSAAGYG
DGPSSAAGGFMYLGLSEVTFDIADGKTLVIGNTENDGAVDSIAGTGLITKTGSGDLVLNADNNDFTGEMQ
IENGEVTLGRSNSLMNVGDTHCQDDPQDCYGLTIGSIDKYQNQAELNVGSTQQTFVHSLTGFQNGTLNID
AGGNVTVNQGSFAGTIEGAGQLTIAQNGSYVLAGAQSMALTGDIVVDDGAVLSLEGDAADLRALQDDPQS
IVLNGGVLDLSDFSTWQSGTSYNDGLEVSGSSGTVIGSQDVVDLAGGDDLHIGGDGKDGVYVVIDAGDGQ
VSLANNNSYLGTTQIASGTLMVSDNSQLGDTHYNRQVIFTDKQQESVMEITADVDTRSTTTGHGRDIEMR
ADGEVAVDAGVDTQWGALMADSSGQHQDEGSTLTKTGAGTLELTASGTTQSAVRVEEGTLKGDVADIIPY
ASSLWVGDGATFVTGADQDIQSIDATSSGTIDISDGTVLRLTGQDTSVALNASLFNGDGTLVNATDGVTL
TGELNTNLETDSLTYLSDVTVNGNLTNTSGAVSLQNGVAGDTLTVNGDYTGGGTLLLDSELNGDDSVSDQ
LVLNGNTAGNTTVVVNSITGIGEPTSTGIKVVDFAADPTQFQNNAQFSLAGSGYVNMGAYDYTLVEDNND
WYLRSQEVTPPSPPDPDPTPDPDPTPDPDPTPDPEPTPAYQPVLNAKVGGYLNNLRAANQAFMMERRDHA
GGDGQTLNLRVIGGDYHYTAAGQLAQHEDTSTVQLSGDLFSGRWGDDGEWMLGIVGGYSDNQGDSRSNMT
GTRADNQNHGYAVGLTSSWFQHGNQKQGAWLDSWLQYAWFNNDVSEQEDGTDHYHSSGIIASLEAGYQWL
PGRGVVIEPQAQVIYQGVQQDDFTAANHARVSQSQGDDIQTRLGLHSEWRTAVHVIPTLDLNYYHDPHST
EIEEDGSTISDDAVKQRGEIKVGVTGNISQRVSLRGSVAWQKGSDDFAQTAGFLSMTVKW
>gnl|CDD|170080 PRK09754, PRK09754, phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQE
NNVHLHSGVTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREV
LQPERSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIE
HVVDGEKVELTLQSGETLQADVVIYGIGISANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITR
LDNGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWFWSDQYSDNLQFIGDMRGDDWLCRGNPETQKA
IWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIA
>gnl|CDD|182060 PRK09755, PRK09755, ABC transporter substrate-binding protein
MYTRNLLWLVSLVSAAPLYAADVPANTPLAPQQVFRYNNHSDPGTLDPQKVEENTAAQIVLDLFEGLVWM
DGEGQVQPAQAERWEILDGGKRYIFHLRSGLQWSDGQPLTAEDFVLGWQRAVDPKTASPFAGYLAQAHIN
NAAAIVAGKADVTSLGVKATDDRTLEVTLEQPVPWFTTMLAWPTLFPVPHHVIAKHGDSWSKPENMVYNG
AFVLDQWVVNEKITARKNPKYRDAQHTVLQQVEYLALDNSVTGYNRYRAGEVDLTWVPAQQIPAIEKSLP
GELRIIPRLNSEYYNFNLEKPPFNDVRVRRALYLTVDRQLIAQKVLGLRTPATTLTPPEVKGFSATTFDE
LQKPMSERVAMAKALLKQAGYDASHPLRFELFYNKYDLHEKTAIALSSEWKKWLGAQVTLRTMEWKTYLD
ARRAGDFMLSRQSWDATYNDASSFLNTLKSDSEENVGHWKNAQYDALLNQATQITDATKRNALYQQAEVI
INQQAPLIPIYYQPLIKLLKPYVGGFPLHNPQDYVYSKELYIKAH
>gnl|CDD|182061 PRK09756, PRK09756, PTS N-acetylgalactosamine transporter subunit IIB
MSSPNILLTRIDNRLVHGQVGVTWTSTIGANLLVVVDDVVANDDIQQKLMGITAETYGFGIRFFTIEKTI
NVIGKAAPHQKIFLICRTPQTVRKLVEGGIDLKDVNVGNMHFSEGKKQISSKVYVDDQDLADLRFIKQRG
VNVFIQDVPGDQKEQIPD
>gnl|CDD|236621 PRK09757, PRK09757, PTS N-acetylgalactosamine transporter subunit IIC
MHEITLLQGLSLAALVFVLGIDFWLEALFLFRPIIVCTLTGAILGDIQTGLITGGLTELAFAGLTPAGGV
QPPNPIMAGLMTTVIAWSTGVDAKTAIGLGLPFSLLMQYVILFFYSAFSLFMTKADKCAKEADTAAFSRL
NWTTMLIVASAYAVIAFLCTYLAQGAMQALVKAMPAWLTHGFEVAGGILPAVGFGLLLRVMFKAQYIPYL
IAGFLFVCYIQVSNLLPVAVLGAGFAVYEFFNAKSRQQAQPQPVASKNEEEDYSNGI
>gnl|CDD|182063 PRK09759, PRK09759, type I toxin-antitoxin system toxin HokA
MPQKYRLLSLIVICFTLLFFTWMIRDSLCELHIKQGSYELAAFLACNLKE
>gnl|CDD|182064 PRK09762, PRK09762, galactosamine-6-phosphate isomerase; Provisional
QTLQQVENYTALSERASEYLLAVIRSKPDAVICLATGATPLLTYHYLVEKIHQQQVDVSQLTFVKLDEWV
DLPLTMPGTCETFLQQHIVQPLGLREDQLISFRSEEINETECERVTNLIARKGGLDLCVLGLGKNGHLGL
NEPGESLQPACHISQLDARTQQHEMLKTAGRPVTRGITLGLKDILNAREVLLLVTGEGKQDATERFLTAK
VSTAIPASFLWLHSNFICLIDR
>gnl|CDD|182065 PRK09764, PRK09764, GntR family transcriptional regulator
MGHKPLYRQIADRIREQIARGELKPGDALPTESALQTEFGVSRVTVRQALRQLVEQQILESIQGSGTYVK
EERVNYDIFQLTSFDEKLSDRHVDTHSEVLIFEVIPADDFLQQQLQITAQDRVWHVKRVRYRKQKPMALE
ETWMPLALFPDLTWQVMENSKYHFIEEVKKMVIDRSEQEIIPLMPTEEMSRLLNISQTKPILEKVSRGYL
VDGRVFEYSRNAFNTDDYKFTLIAQRKSSR
>gnl|CDD|182066 PRK09765, PRK09765, PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
MNLTTLTHRDLLCLNARFTSREEAIHALAQRLAALGKISSTEQFLEEVYRRESLGPTALGEGLAVPHGKT
AAVKEAAFAVATLSEPLQWEGVDGPEAVDLIFLLAIPPNEAGTTHMQLLTALTTRLADDEIRARIQSATT
PDELLSALDDKGGTQPSASFSNAPTIVCVTACPAGIAHTYMAAEYLEKAGRKLGVNVYVEKQGANGIEGR
LTADQLNSATACIFAAEVAIKESERFNGIPALSVPVAEPIKHAEALIQQALELKRSDETRTVQQDTQPVK
SVKTELKQALLSGISFAVPLIVAGGTVLAVAVLLSQIFGLQDLFNEENSWLWMYRKLGGGLLGTLMVPVL
AAYTAYSLADKPALAPGFAAGLAANMIGSGFLGAVVGGLIAGYLMRWVKNHLRLSSKFNGFLTFYLYPVL
GTLGAGSLMLFVVGEPVAWINNSLTAWLNGLSGSNALLLGAILGFMCSFDLGGPVNKAAYAFCLGAMANG
VYGPYAIFASVKMVSAFTVTASTMLAPRLFKEFEIETGKSTWLLGLAGITEGAIPMAIEDPLRVIGSFVL
GSMVTGAIVGAMNIGLSTPGAGIFSLFLLHDNGAGGVMAAIGWFGAALVGAAISTAILLIWRRHAVKHGN
Y
>gnl|CDD|182067 PRK09767, PRK09767, DUF559 domain-containing protein
MMDKIKSNARDLRRNLTLQERKLWRYLRSRRFGDFKFRRQHPVGSYILDFACCSARVVVELDGGQHDLAV
AYDTRRTSWLESQGWTVLRFWNNEIDCNEEAVLEIILQELNRRSPSP
>gnl|CDD|170086 PRK09772, PRK09772, transcriptional antiterminator BglG; Provisional
MNMQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPL
EVMATCDRIISLAQERLGKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTI
IDKRLGVQLPKDEVGFIAMHLVSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLK
FLSWRILEHASINDSDESLQQAVKQNYPQAWQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKEH
>gnl|CDD|236622 PRK09774, PRK09774, fec operon regulator FecR; Reviewed
MNPLLTDSRRQALRSASHWYAVLSGERVSPQQEARWQQWYEQDQDNQWAWQQVENLRNQMGGVPGDVASR
ALHDTRLTRRHVMKGLLLLLGAGGGWQLWRSETGEGLRADYRTAKGEVSRQRLEDGSLLTLNTQSAVDVR
FDAHQRTVRLWYGEIAITTAKDALQRPFRVLTRQGQLTALGTEFTVRQQDNFTQLAVQQHAVEVLLASAP
AQKRIVNAGESLQFSASEFGAVKPLDDESTSWTQGILSFSDKPLGEVIATLSRYRNGVLRCDPAVAGLRL
SGTFPLKNTDAILNVIAQTLPVKIQSITRYWVNISPLAK
>gnl|CDD|236623 PRK09775, PRK09775, type II toxin-antitoxin system HipA family toxin YjjJ
MMSLLTTLLLQGPLSAAELAARLGVSQATLSRLLAALGDQVVRFGKARATRYALLRPLRGVSRFPLYRVD
EDGQAHKFGQLYPVWPAGFCVVLDADGDWGWFDGLPWYLDDMRPQGFLGRAWARRHAALLGLPEDIRLWT
EDDVLRALLSFGGDVPGNLLIGEGAYQRWLTAPDPTAIPLADKATRYPQLAEDALAGEVVGSSAGGEQPK
FTAYAETPDGNRHVIVKFSAADDNPVSQRWRDLLIAEHLALQVLREAGIPAAATRVIVQAGGQVFLEVER
FDRTGELGRRGMVSLEALDAEFVGSPGPWPAAARRLAAQGLITEEDAQRAELLWAFGRLIANTDMHAGNL
SFVLSDGRPLALAPVYDMLPMAFAPNSGGELRDAAIEIRLDLSVSKEAWRTALPLAEQFWQRVAGDPRIS
EAFRPIAAAMREKLRRLAGRIA
>gnl|CDD|182070 PRK09776, PRK09776, putative diguanylate cyclase; Provisional
VSLGLVSFIFTLFSLELSRFPTTLAPLWFPTAIMMVAFYRHAGRMWPGILLSCSLGNIAANILLFSTSSL
NLTWTTINLVEAVVGAVLLRKLLPWYNPLQNLADWLRLALGSAIVPPLLGGVLVVLLTPGDDPLRAFLIW
VLSEAIGMLALVPLGLLFKPHYLLRHRNPRLLFESLLTLAITLTLSWLALLYLPWPFTFIIVLLMWSAVR
LPRMEAFLIFLTTVMMVSLMMAADPSLLATPRTYLMSHMPWLPFLLILLPANIMTMVMYAFRAERKHISE
SETRFRNAMEYSAIGMALVGTEGQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLLSG
EINSYSMEKRYYRRDGEVVWALLAVSLVRDTDGTPLYFIAQIEDINELKRTEQVNERLMERITLANEAGG
IGIWEWDLKPNIISWDKRMFELYEIPPHIKPTWQVWYACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVV
KDGVRHIRALANRVLNKDGEVERLLGINMDMTEVRQLNEALFQEKERLHITLDSIGEAVVCTDMAMKVTF
MNPVAEKMTGWTQEEALGVPLLTVLHITFGDNGPLMENIYSCLTSRSAAYLEQDVVLHCRSGGSYDVHYS
ITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALV
FIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISA
INDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSEHRAL
SLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVI
HEFFRQAAKAVASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLV
QKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAG
PVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLLNSSYFAIN
>gnl|CDD|182071 PRK09777, fecD, Fe(3+) dicitrate ABC transporter permease subunit FecD
MKIALVIFITLALAGCALLSLRMGVIPLPWRALLTDWQAGDEHYYVLMEYRLPRLLLALFVGAALAVSGV
LVQGIVRNPLASPDILGVNHAASLASVGALLLFPSLPVMWLPLLAFIGGMAGLILLKMLAGTHQPMKLAL
TGVALSALWASLTDYLMLSRPQDINNALLWLTGSLWGRDWSFVKVALPWLILLLPLSLSFCRDLDLLALG
DARATTLGVSVPHTQFWALLLAVALTATGVAACGPISFIGLVVPHLMRSLVGGRHRRLLPVSALTGALLL
LLADLLARIIHPPLELPAGVLTAIIGAPWFFWLLVRMR
>gnl|CDD|170091 PRK09778, PRK09778, type I toxin-antitoxin system antitoxin YafN
MHRILAEKSVNITELRKNPAKYFIDQPVAVLSNNRPAGYLLSASAFEALMDMLAEQEEKKPIKARFRPSA
ARLEEITRRAEKYLNDMTDDDFNDFKE
>gnl|CDD|170092 PRK09781, PRK09781, hypothetical protein; Provisional
MEDVKLYVERVGVDPASGADIRIARRESTSWHKDIVAELINQVLRCGAALIIIAVLTACDDRQVSYFPDY
AAIPEQSGIWTWLPVFFPSSASEIEMTFNLDSNLFYADFSVADGDKRAHFESVLGEESVVHYANFSHKSW
CKTGKTLWNSEARAKPFFITQISVDRYRITNHMPGCTKPGE
>gnl|CDD|236624 PRK09782, PRK09782, bacteriophage N4 receptor, outer membrane subunit; Provisional
NNLNRVIGWSGLLLTSLLSTSALADNIGTSAEELGLSDYRHFVIYPRLDKALKAQKNNDEATAIREFEYI
HQQVPDNIPLTLYLAEAYRHFGHDDRARLLLEDQLKRHPGDARLERSLAAIPVEVKSVTTVEELLAQQKA
CDAVPTLRCRSEVGQNALRLAQLPVARAQLNDATFAASPEGKTLRTDLLQRAIYLKQWSQADTLYNEARQ
QNTLSAAERRQWFDVLLAGQLDDRLLALQSQGIFTDPQSRITYATALAYRGEKARLQHYLIENKPLFTTD
AQEKSWLYLLSKYSANPVQALANYTVQFADNRQYVVGATLPVLLKEGQYDAAQKLLATLPANEMLEERYA
VSVATRNKAEALRLARLLYQQEPANLTRLDQLTWQLMQNGQSREAADLLLQRYPFQGDARLSQTLMARLA
SLLESHPYLATPAKVAILSKPLPLAEQRQWQSQLPGIADNCPAIVRLLGDMSPSYDAAAWNRLAKCYRDT
LPGVALYAWLQAEQRQPDAWQHRAVAYQAYQVEDYATALAAWQKISLHDMSNEDLLAAANTAQAAGNGAA
RDRWLQQAEQRGLGDNALYWWLHAQRYIPGQPELALNDLTRSLNIAPSANAYVARATIYRQRHNVPAAVS
DLRAALELEPNNSNYQAALGYALWDSGDIAQSREMLERAHKGLPDDPALIRQLAYVNQRLDDMAATQHYA
RLVIDDIDNQALITPLTPEQNQQRFNFRRLHEEVGRRWTFSFDSSIGLRSGAMSTANNNVGGAAPGKSYR
SYGQLEAEYRLGRNMLLEGDLLSVYSRVFADTGENGVMMPVKNPMSGTGLRWKPLRDQIFFLAVEQQLPL
NGQNGASDTMLRASASFFNGGKYSDEWHPNGSGWFAQNLYLDAAQYTRQDIQAWTADYRVSWHQKVANGQ
TLEPYAHVQDNGYRDKGTQGAQLGGVGVRWNIWTGETHYNAWPHKVSVGVEYQHTFKAINQRNGERNNAF
LTIGVHW
>gnl|CDD|236625 PRK09783, PRK09783, copper/silver efflux system membrane fusion protein CusB; Provisional
MKKIALIIGSMIAGGIISAAGFTWVAKAEPPAEKTSTAERKVLFWYDPMYPNTRFDKPGKSPFMDMDLVP
KYADEESSASSGGVRIDPTQTQNLGVKTATVTRGPLTFAQTFPANVSYNEYQYAIVQARAAGFIDKVYPL
TVGDKVQKGTPLLDLTIPDWVEAQSEYLLLRETGGTATQTEGILERLRLAGMPEADIRRLIATRKIQTRF
TLKAPIDGVITAFDLRAGMNIAKDNVVAKIQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTI
RKWTLLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQLNTASEPMLLIPSQALIDTGSEQRVITVDADG
RFVPKRVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANISGALERMRSESATHAH
>gnl|CDD|182074 PRK09784, PRK09784, YccE family protein
GSNIHGISCTANNYLKQAWNDIKNEYEKNQTYSITLFENTLVCFMRLYNELRRKVNEEDTPCLECESLEK
EFEEMQNDNDLSLFMRTLRTNDTQIYSGVSGGITYTIQYVRDIDIVRVSLPGRGSESITDFKGYYWYGFM
EYIENINACDDVFSEYCLDDENMSIQPEQINTPGISDLDSGIDLSGISFIQSEINKTYGLKYAPVDGDGY
CLLRAILVLKQHDYSWALGSHKTQKEVYEEFIKIVDKQTIEALVDTAFYNLREDVKTLFGVDLQSDNKIQ
GQGSFMSWSFLFFKKQFIDSCLNNEKCILHLPEFIFNDNKNLLALDTDTSDRIKAVKNFLAVLSDSICSL
FIVNSNVASISLGNESFSTDEDLEYGYLINTGNHYDVYLPPELFAQAYKLNNKEMNAQLDYLNRYAI
>gnl|CDD|182075 PRK09786, PRK09786, endodeoxyribonuclease RUS; Reviewed
MNTYSITLPWPPSNNRYYRHNRGRTHISAEGQAYRDNVARIIKNAMLDIGLAMPVKIRIECHMPDRRRRD
LDNLQKAAFDALTKAGFWLDDAQVVDYRVVKMPVTKGGRLELTITEMGNE
>gnl|CDD|182076 PRK09790, PRK09790, hypothetical protein; Reviewed
MITNYEATVVTTDDIVHEVNLEGKRIGYVIKTENKETPFTVVDIDGPSGNVKTLDEGVKKMCLVHIGKNL
PAEKKAEFLATLIAMKLKGEI
>gnl|CDD|182077 PRK09791, PRK09791, LysR family transcriptional regulator
MAFQVKIHQIRAFVEVARQGSIRGASRMLNMSQPALTKSIQELEEGLAAQLFFRRSKGVTLTDAGESFYQ
HASLILEELRAAQEDIRQRQGQLAGQINIGMGASIARSLMPAVISRFHQQHPQVKVRIMEGQLVSMINEL
RQGELDFTINTYYQGPYDHEFTFEKLLEKQFAVFCRPGHPAIGARSLKQLLDYSWTMPTPHGSYYKQLSE
LLDDQAQTPQVGVVCETFSACISLVAKSDFLSILPEEMGCDPLHGQGLVMLPVSEILPKATYYLIQRRDT
RQTPLTASLITLFRRECGYLQS
>gnl|CDD|182078 PRK09792, PRK09792, 4-aminobutyrate transaminase; Provisional
MSNNEFHQRRLSATPRGVGVMCNFFAQSAENATLKDVEGNEYIDFAAGIAVLNTGHRHPDLVAAVEQQLQ
QFTHTAYQIVPYESYVTLAEKINALAPVSGQAKTAFFTTGAEAVENAVKIARAHTGRPGVIAFSGGFHGR
TYMTMALTGKVAPYKIGFGPFPGSVYHVPYPSDLHGISTQDSLDAIERLFKSDIEAKQVAAIIFEPVQGE
GGFNVAPKELVAAIRRLCDEHGIVMIADEVQSGFARTGKLFAMDHYADKPDLMTMAKSLAGGMPLSGVVG
NANIMDAPAPGGLGGTYAGNPLAVAAAHAVLNIIDKESLCERANQLGQRLKNTLIDAKESVPAIAAVRGL
GSMIAAEFNDPQTGEPSAAIAQKIQQRALAQGLLLLTCGAYGNVIRFLYPLTIPDAQFDAAMKILQDALS
D
>gnl|CDD|182079 PRK09793, PRK09793, methyl-accepting chemotaxis protein IV
MFNRIRISTTLFLILILCGILQIGSNGMSFWAFRDDLQRLNQVEQSNQQRAALAQTRAVMLQASTALNKA
GTLTALSYPADDIKTLMTTARASLTQSTTLFKSFMAMTAGNEHVRALQKETEKSFARWHNDLEHQATWLE
SNQLSDFLTAPVQGSQNAFDVNFEAWQLEINHVLEAASAQSQRNYQISALVFISMIIVAAIYISSALWWT
RKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEI
VAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEI
ATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEES
VNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEA
AVATEQLANQADHLSSRVAVFTLEEHEVARHESAQLQIAPVVS
>gnl|CDD|182080 PRK09795, PRK09795, aminopeptidase; Provisional
MTLLASLRDWLKAQQLDAVLLSSRQNKQPHLGISTGSGYVVISRESAHILVDSRYYADVEARAQGYQLHL
LDATNTLTTIVNQIIADEQLQTLGFEGQQVSWETAHRWQSELNAKLVSATPDVLRQIKTPEEVEKIRLAC
GIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEKASFDTIVASGWRGALPHGKASDKIVAAGEFVT
LDFGALYQGYCSDMTRTLLVNGEGVSAESHPLFNVYQIVLQAQLAAISAIRPGVRCQQVDDAARRVITEA
GYGDYFGHNTGHAIGIEVHEDPRFSPRDTTTLQPGMLLTVEPGIYLPGQGGVRIEDVVLVTPQGAEVLYA
MPKTVLLTGEA
>gnl|CDD|182081 PRK09796, PRK09796, PTS system cellobiose/arbutin/salicin-specific transporter subunits IIBC; Provisional
MAKNYAALARSVIAALGGVDNISAVTHCMTRLRFVIKDDALIDSPTLKTIPGVLGVVRSDNQCQVIIGNT
VSQAFQEVVSLLPGDMQPAQPVGKPKLTLRRIGAGILDALIGTMSPLIPAIIGGSMVKLLAMILEMSGVL
TKGSPTLTILNVIGDGAFFFLPLMVAASAAIKFKTNMSLAIAIAGVLVHPSFIELMAKAAQGEHVEFALI
PVTAVKYTYTVIPALVMTWCLSYIERWVDRITPAVTKNFLKPMLIVLIAAPLAILLIGPIGIWIGSAISA
LVYTIHGYLGWLSVAIMGALWPLLVMTGMHRVFTPTIIQTIAETGKEGMVMPSEIGANLSLGGSSLAVAW
KTKNPELRQTALAAAASAIMAGISEPALYGVAIRLKRPLIASLISGFICGAVAGMAGLASHSMAAPGLFT
SVQFFDPANPMSIVWVFAVMALAVVLSFILTLLLGFEDIPVEEAAAEARKHQ
>gnl|CDD|182082 PRK09798, PRK09798, MazF-MazE toxin-antitoxin system antitoxin MazE
MIHSSVKRWGNSPAVRIPATLMQALNLNIDDEVKIDLVDGKLIIEPVRKEPVFTLAELVNDITPENLHEN
IDWGEPKDKEVW
>gnl|CDD|182084 PRK09800, PRK09800, putative hypoxanthine oxidase; Provisional
MIIHFTLNGAPQELTVNPGENVQKLLFNMGMHSVRNSDDGFGFAGSDAIIFNGNIVNASLLIAAQLEKAD
IRTAESLGKWNELSLVQQAMVDVGVVQSGYNDPAAALIITDLLDRIAAPTREEIDDALSGLFSRDAGWQQ
YYQVIELAVARKNNPQATIDIAPTFRDDLEVIGKHYPKTDAAKMVQAKPCYVEDRVTADACVIKMLRSPH
AHALITHLDVSKAEALPGVVHVITHLNCPDIYYTPGGQSAPEPSPLDRRMFGKKMRHVGDRVAAVVAESE
EIALEALKLIDVEYEVLKPVMSIDEAMAEDAPVVHDEPVVYVAGAPDTLEDDNSHAAQRGEHMIINFPIG
SRPRKNIAASIHGHIGDMDKGFADADVIIERTYNSTQAQQCPTETHICFTRMDGDRLVIHASTQVPWHLR
RQVARLVGMKQHKVHVIKERVGGGFGSKQDILLEEVCAWATCVTGRPVLFRYTREEEFIANTSRHVAKVT
VKLGAKKDGRLTAVKMDFRANTGPYGNHSLTVPCNGPALSLPLYPCDNVDFQVTTYYSNICPNGAYQGYG
APKGNFAITMALAELAEQLQIDQLEIIERNRVHEGQELKILGAIGEGKAPTSVPSAASCALEEILRQGRE
MIQWSSPKPQNGDWHIGRGVAIIMQKSGIPDIDQANCMIKLESDGTFIVHSGGADIGTGLDTVVTKLAAE
VLHCPPQDVHVISGDTDHALFDKGAYASSGTCFSGNAARLAAENLREKILFHGAQMLGEPVADVQLATPG
VVRGKKGEVSFGDIAHKGETGTGFGSLVGTGSYITPDFAFPYGANFAEVAVNTRTGEIRLDKFYALLDCG
TPVNPELALGQIYGATLRAIGHSMSEEIIYDAEGHPLTRDLRSYGAPKIGDIPRDFRAVLVPSDDKVGPF
GAKSISEIGVNGAAPAIATAIHDACGIWLREWHFTPEKILTALEKI
>gnl|CDD|182085 PRK09801, PRK09801, LysR family transcriptional regulator
MLNSWPLAKDLQVLVEIVHSGSFSAAAATLGQTPAFVTKRIQILENTLATTLLNRSARGVALTESGQRCY
EHALEILTQYQRLVDDVTQIKTRPEGMIRIGCSFGFGRSHIAPAITELMRNYPELQVHFELFDRQIDLVQ
DNIDLDIRINDEIPDYYIAHLLTKNKRILCAAPEYLQKYPQPQSLQELSRHDCLVTKERDMTHGIWELGN
GQEKKSVKVSGHLSSNSGEIVLQWALEGKGIMLRSEWDVLPFLESGKLVQVLPEYAQSANIWAVYREPLY
RSMKLRVCVEFLAAWCQQRLGKPDEGYQVM
>gnl|CDD|182086 PRK09802, PRK09802, DeoR family transcriptional regulator
MSNTDASGEKRVTGTSERREQIIQRLRQQGSVQVNDLSALYGVSTVTIRNDLAFLEKQGIAVRAYGGALI
CDSTTPSVEPSVEDKSALNTAMKRSVAKAAVELIQPGHRVILDSGTTTFEIARLMRKHTDVIAMTNGMNV
ANALLEAEGVELLMTGGHLRRQSQSFYGDQAEQSLQNYHFDMLFLGVDAIDLERGVSTHNEDEARLNRRM
CEVAERIIVVTDSSKFNRSSLHKIIDTQRIDMIIVDEGIPADSLEGLRKAGVEVILVGE
>gnl|CDD|182087 PRK09804, PRK09804, C4-dicarboxylate transporter DcuC
MFGIIISVIVLITMGYLILKNYKPQVVLAAAGIFLMMCGVWLGFGGVLDPAKSSGYLIVDIYNEILRMLS
NRIAGLGLSIMAVGGYARYMERIGASRAMVSLLSRPLKLIRSPYIILSATYVIGQIMAQFITSASGLGML
LMVTLFPTLVSLGVSRLSAVAVIATTMSIEWGILETNSIFAAQVAGMKIATYFFHYQLPVASCVIISVAI
SHFFVQRAFDKKDKNINHEQAEQKALDNVPPLYYAILPVMPLILMLGSLFLAHVGLMQSELHLVVVMLLS
LTVTMFVEFFRKHNLRETMDDVQAFFDGMGTQFANVVTLVVAGEIFAKGLTTIGTVDAVIRGAEHSGLGG
IGVMIIMALVIAICAIVMGSGNAPFMSFASLIPNIAAGLHVPAVVMIMPMHFATTLARAVSPITAVVVVT
SGIAGVSPFAVVKRTAIPMAVGFVVNMIATITLFY
>gnl|CDD|77417 PRK09806, PRK09806, tryptophanase leader peptide; Provisional
MNILHICVTSKWFNIDNKIVDHRP
>gnl|CDD|182088 PRK09807, PRK09807, hypothetical protein; Provisional
MVAALFGCQPYLVQRFLAVDNDFAAILKGNGQHAAVDFAVDIAVAIPVVQTLFNGQPQLISQAMKFTVVH
CCILFLSDGGSIAAWGQGFKVCTSAAAFRHDSSVTGIMMSLCSERFVSSLGRSYTTPFPVSGKHYDQVYR
ASILTLTELKKPTNKPHCDSA
>gnl|CDD|137533 PRK09810, PRK09810, lipoprotein antitoxin entericidin A
MMKRLIVLVLLASTLLTGCNTARGFGEDIKHLGNSISRAAS
>gnl|CDD|182089 PRK09812, PRK09812, type II toxin-antitoxin system ChpB family toxin
MVKRSKFERGDIVLVGFDPASGHEQQGAGRPALVLSVAAFNQLGMTLVAPITQGGNFARYAGFAVPLHCE
EGDTQGVVLVNQVRMMDLEARLAKRIGLAADEVVEDALLRLQAVVE
>gnl|CDD|182090 PRK09813, PRK09813, fructoselysine 6-kinase; Provisional
KKLATIGDNCVDIYPQLGKAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVH
TKHGVTAQTQVELHDNDRVFGDYTEGVMADFALSEEDYAWLAQYDIVHAAIWGHAEDAFPQLHAAGKLTA
FDFSDKWDSPLWQTLVPHLDYAFASAPQEDEFLRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAP
EPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGAW
>gnl|CDD|236626 PRK09814, PRK09814, sugar transferase
MKVHITNLYGMSGNSAALKAKNDVTKIAKQLGFEELGIYFYNIKRDSLSERSKRLDGILASLKPGDIVIF
QFPTWNGFEFDRLFVDKLKKKQVKIIILIHDIEPLRFDSNYYLMKEEIDMLNLADVLIVHSKKMKDRLVE
EGLTTDKIIVQGIFDYLNDIELVKTPSFQKKINFAGNLEKSPFLKNWSQGIKLTVFGPNPEDLENSANIS
YKGWFDPEELPNELSKGFGLVWDGDTNDGEYGEYYKYNNPHKLSLYLAAGLPVIVWSKAAIADFIVENGL
GFVVDSLEELPEIIDNITEEEYQEMVENVKKISKLLRNGYFTKKALVDAIKEL
>gnl|CDD|77423 PRK09816, thrL, thr operon leader peptide; Provisional
MKRISTTITTTITITTGNGAG
>gnl|CDD|182092 PRK09818, PRK09818, kinase inhibitor
MKTLIVSSVLAFITFSAQAAAFQVTSNEIKTGEQLTTSHVFSGFGCEGGNTSPSLTWSGAPEGTKSFAVT
VYDPDAPTGSGWWHWTVANIPATVTYLPADAGRRDGTKLPTGAVQGRNDFGYAGFGGACPPKGDKPHHYQ
FKVWALKTDKIPVDSNSSGALVGYMLNANKIATAEITPVYEIK
>gnl|CDD|182093 PRK09819, PRK09819, mannosylglycerate hydrolase
MAKSKVHIVPHMHWDREWYFTTERSRILLVNNMEEILDRLEQDNDYKYYVLDGQTSLLEDYLAVKPEDKE
RVKKLVQAGKLIIGPWYTQTDQLVVSGESIVRNLLYGIRDCREFGEPMKIGYLPDSFGQSGQMPQIYNGF
GITRTLFWRGVSDRHGTDKTEFLWQSDDGSEVLAQQLPLGYAIGKYLPEDEEELKKRLDEYFGVLEKKSS
TKNILLPNGHDQMPLQKNLFEVMDKLNEIYPEREFVISRFENVFEKLEKQRDNLPTLKGEFIDGKYMRVH
RSIFSTRMDIKIANARIENKIVNVLEPLASIAYSLGFEYPHGLLEKIWKEMFKNHAHDSIGCCCSDTVHR
DIVARYKLAEDLADNLLDFYMRKIADNMPQSDADKLTVFNLLPYEREEVINTTVYLPASQFTLRDDRGNP
LPYTIREKRDIDPGLLDRQIVHYGNYDPFMEFDIQINVQILPAMGYRTLYIELNEEGNVIEPKSSAEGII
ENEFYQITLNENGTLTIVDKKSGKTYDRQLIIEENGDDGDEYDYSPPREDWVITSAEAVPSVEISHSAWQ
SRAVIRYRLAVPKNLEERAAGQKTGRMPVKLVVTLSKNSRRIDFDVNLDNQADDHRLRVLFPTEIASKFS
LADQQFGSITRPVNDPAMDVWEQEGWQEAPISIEPMQSFVALHDERHGVAVFTEGVREYEIIGENYDTIA
LTLFRGVGLLGKEDLLYRPGRPSGIKIPTPDSQLLGELSFRFSLTSYEGTFDEAGVAQQAKEYLTPVQCY
NKIPFLNMRLNDEEFTLPESYSLLKMPPDGAVLSAVKKAEDRDGLILRFFNPAESKTCDATVAFSKEVKS
LDETMLDEKITTEENQGSNLSGELKPCQVQTFLVK
>gnl|CDD|182094 PRK09821, PRK09821, putative transporter; Provisional
MSTILLLCIALAGVILLLLLVIKAKVQPFVALLLVSLLVALAAGIPAGEVGKVMIAGMGGVLGSVTIIIG
LGAMLGRMIEHSGGAESLANYFTRKLGDKRTIAALTLAAFILGIPVFFDVGFIILAPIIYGFAKVAKVSP
LKFGLPVAGIMLTVHVALPPHPGPVAAAGLLHADIGWLTIIGIAISIPVGIVGYFAAKIINRRQYALSVE
VLEQMQLAPASEEGATKLSDKINPPGAALITSLIVIPIAIIMLGTVSATLLPPSHPLLGTLQLIGSPMVA
LLIALVLAFWLLALRRGWSLQHTSDVMGSALPTAAVVILVTGAGGVFGKVLVESGVGKALANMLQMIHLP
LIPAAFIISLALRASQGSATVAILTTSGLLSEAVMGLNPIQCVLVTLAACFGGLGLSHVNDSGFWIVTKY
LGLSVADGLKTWTVLTTILGLTGFLITWCVWAVI
>gnl|CDD|182095 PRK09822, PRK09822, lipopolysaccharide core biosynthesis protein; Provisional
MGSVNFITHADVLQLIAKRTAEDCIIFLSGPTSRKTPLSLLRMKDVIAVNGSVQYLLNNNVKPFLYLLTD
VRFLHRRREDFYNFSRNSQFTIVNLDVYEQASVDDQKYIEENCLIIRSFYRREKGGFLKKIKFNILKRVH
KALLISVPLSKRGRLAGFCKDISIGYCSCHTIAYTAIQVAYSLKYGRIICSGLDLTGSCPRFYDESTSPM
PSELSKDLFKILPFFTFMRKNVSDLNIFNLSDDTAIHYDIIPYITASELEDEIYYDKIV
>gnl|CDD|170114 PRK09823, PRK09823, putative inner membrane protein; Provisional
MSVSRRIIHHGLWFALLGPLIGVLFLVLYIFFLPGAKEPLLLLVIIQVLPLFLLLSWTTGAIPALLTGVA
VACLPEKIYQQKIYRCLACGIGGVVITTLYCAVIVHIKGMASSLIYENILSGDSLVVRIIPALLAGVIMG
RIITYLPGLDISCPETNSLS
>gnl|CDD|236627 PRK09824, PRK09824, PTS system beta-glucoside-specific transporter subunits IIABC; Provisional
MEYTELAREIVAGVGGADNIVSLMHCATRLRFKLKDNSKAQAEVLKKNPGVIMVVESGGQFQVVIGNHVA
DVFLAVNSVAGLGEKAQQAPENDKKGNLLNRFIDVISGIFTPLIGVMAATGILKGMLALALTFGWTTEQS
GTYKILFAASDALFFFFPIILGYTAGKKFGGNPFTAMVIGGALVHPLMIAAFEAGQKADALGLDFLGIPV
TLLNYSSSVIPIIFSAWLCSILERRLNAWLPSAIKNFFTPLLCLMVIVPLTFLLIGPLATWLSELLAAGY
QWLYQAVPAFAGAVMGAFWQVFVIFGLHWGLVPLMINNLTVLGHDTMLPLLMPAVMAQVGAALGVFLCTR
DAQKKVVAGSAFLAGLFGITEPAVYGVNLPLKRPFIFGCISGALGAAIIGYAQTKVYSFGLPSIFTFMQT
IPPTGIDFTVWASVIGTVIAIGCAFVGTVMFGFPTAKRQPAQVAPQEKTPEVITPPEQGGICSPMTGEVV
PLEQVADTTFASGLLGKGIAILPSVGEVRSPVAGRVASLFATLHAIGLESDDGVEVLIHVGIDTVKLDGK
FFTAHVNVGDKVNTGDLLIEFDIPAIREAGYDLTTPVLISNSDDYTDVLPHATAQVSAGEPLLSIIR
>gnl|CDD|182097 PRK09825, idnK, gluconokinase
MAGESYILMGVSGSGKSLIGSKIAALFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYS
LYKKNETGFIVCSSLKKQYRDILRKSSPNVHFLWLDGDYETILARMQRRAGHFMPPDLLQSQFDALERPC
ADEHDIARIDVNHDIENVTEQCRQAVQAFRQALSAS
>gnl|CDD|182098 PRK09828, PRK09828, putative fimbrial outer membrane usher protein; Provisional
MTIKSTKNYHPHLTRLATFCALLYSNSAACAELVEYDHTFLMGQGASNIDLSRYSEGNPTLPGTYDVSVY
VNDQPISSQSIPFIDIGKKNAQACITLKNLLQFHIKSPDINNEKAILLARDDELGDCLNLTKIIPQASVR
YDVSDQRLDIDVPQAWVMKNYQGYVDPSLWENGINAAMLSYNLNGYHSESPGRTNDSIYAAFNGGINLGA
WRLRARGNYNWMTDSGSDYDFQNRYLQRDIAALRSQLIIGESYTTGETFDSVSIRGIRLYSDSRMLPPGL
ASYAPIIRGVANSNAKVTITQSGYKIYETTVPPGAFVIDDLSPSGYGSDLIVTIEEADGSKRTFSQPFSS
VVQMLRPGVGRWDISAGQVLDDSLQDEPNLGQASYYYGLNNYLTGYTGIQYTDNNYTAGLLGLGMNTSVG
AFAFDVTHSNAEIPDDKTYQGQSYRLTWNKLFEATSTSFNVAAYRYSTQDYLGLNDALTLIDEVKHPEQD
LEPKSMRNYSRMKNQVTVSINQPLKFEKKDYGSFYLSGSWSDYWASGQSRSNYSVGYSNSASWGSYSVSL
QRSWNEDGEKDDSVYLSFSIPIENLLGTERRSSGFQSIDTQLNSDFKGNNQLNVSSSGNSEDNRISYSVN
TGYSMNKNSKDLSYVGGYASYESPWGTLSGSASASSDNSRQYSLSTDGGFVLHSGGLTFSNDSFSDSDTL
ALVKAPGAKGARINYGNSTIDRWGYGVTSALSPYRENRVALDINTLENDVELKSTSAVAVPRQGAVVLAD
FETDQGRSAIMNITRSDGKNIPFAADVYDEQGNVIGNVGQGGQAFVRGIEDQGELRIRWLEEGKPVSCLA
HYQQPATAEKIGQTIILNGITCQIQ
>gnl|CDD|182099 PRK09831, PRK09831, GNAT family N-acetyltransferase
IQIRNYQPGDFQQLCAIFIRAVTMTASQHYSPQQIAAWAQIDESRWKEKLAKSQVRVAVINAQPVGFITC
IEHYIDMLFVDPEYTRRGVASALLKPLIKSESELTVDASITAKPFFERYGFQTVKQQRVECRGEWFINFY
MRYKPQH
>gnl|CDD|182100 PRK09834, PRK09834, DNA-binding transcriptional regulator
MTEYKTVRGLSRGLMVLRALNRLDGGATVGLLAELTGLHRTTVRRLLETLQEEGYVRRSASDDSFRLTLK
VRQLSEGFRDEQWISALAAPLLGDLLRRVVWPTDLTTLDVDAMVIRETTHRFSPLSFHRAMVGRRLPLLL
TAAGRAYLAFCPEEEREALLELLASRPGDEDQLARDPARLEAMLARTRKRGYGENYGGWDQQPKIASIAV
PVRSGQRVLGCLNLVYIASAMSIEEAAKRYLPALQRAAKQIEAGVESQAILVA
>gnl|CDD|182101 PRK09835, PRK09835, Cu(+)/Ag(+) sensor histidine kinase
MVSKPFQRPFSLATRLTFFISLATIAAFFAFTWIMIHSVKVHFAEQDINDLKQISATLERVLNHPDETQA
RRLMTLEDIVAGYSNVLISLADSHGKTVYHSPGAPDLREFVRDAIPDKDARGGEVFLWSGPTPMMPGHGH
GHMEHSNWRMIALPVGPLVDGKPIYTLLIALSIDFHLHYINDLKNKLIMTASVISLLIVFIVLLAVHKGH
APIRSVSRQIQNITSKDLDVRLDPQTVPIELEQLVLSFNHMIERIEDVFTRQSNFSADIAHEIRTPITNL
ITQTEIALSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLDLADEVGKVFDFFE
AWAEERGVELRFVGDPCQVAGDPLMLRRAISNLLSNALRYTPAGEAITVRCQEVDHQVQLVVENPGTPIA
PEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDARGTRFVISLPRLE
>gnl|CDD|182102 PRK09836, PRK09836, DNA-binding transcriptional activator CusR; Provisional
MKLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSAN
KGMPILLLTALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAAVIIESQFQVADLMVDLVSR
KVTRSGTRITLTSKEFTLLEFFLRHQGEVLPRSLIASQVWDMNFDSDTNAIDVAVKRLRGKIDNDFEPKL
IQTVRGVGYMLEVPDGQ
>gnl|CDD|182103 PRK09837, PRK09837, Cu(I)/Ag(I) efflux RND transporter outer membrane protein
MSPCKLLPFSVALALTGCVSLAPDYQRPAMPVPQQFSLSQNGLVNAADNYQNTGWRTFFVDNQVKTLISE
ALVNNRDLRMATLKVQEARAQYRLTDADRYPQLNGEGSGSWSGNLKGDTATTREYSTGLNLSFDLDFFGR
LKNMSEAERQNYLASEEAQRAVHILLVSNVAQSYFNQQLAYAQLQIAEETLRNYQQSYAFVEKQLLTGSS
NVLALEQARGVIESTRADIAKRQGELAQANNALQLLLGSYGKLPQAQTVNSDSLQSVKLPAGLSSQILLQ
RPDIMEAEHALMAANANIGAARAAFFPSISLTSGLSTSSSDLSSLFNASSGMWNFIPKIEIPIFNAGRNQ
ANLDLAEIRQQQSVVNYEQKIQNAFKEVADALALRQSLNDQISAQQRYLASLQITLQRARALYQHGAVSY
LEVLDAERSLFATRQTLLDLNYARQVNEISLFTALGGGWQE
>gnl|CDD|182104 PRK09838, PRK09838, periplasmic copper-binding protein; Provisional
MKKALKVAMFSLFSVIGFNAQANEHHQHGDMHEAMSAAQPQVISGTGVVKGIDLESKKITIHHEPIPAVN
WPEMTMRFTITPQTKMSEIKTGDKVAFNFVQQGNLSLLQDIKVSQ
>gnl|CDD|182105 PRK09840, PRK09840, catecholate siderophore receptor Fiu; Provisional
MENNRNFPARQFHSLAFFAGLCIGITPVAQALAAEGQTNADDTLVVEASTPSLYAPDQSADPKFSQPLAD
TTQTITVISEQVIKDQGATNLTEALRNVPGVGTFFAGENGNTTTGDAIYMRGFDTSNSIYVDGIRDIGSI
SRDTFNTEQVEVIKGPSGTDYGRSAPTGSINMISKQPRNDSGIDASASIGSAWFRRGTLDVNQVIGDTTA
VRLNVMGEKTHDAGRDKVKNERYGVAPSVAFGLGTANRLYLNYLHVTQNNTPDGGIPTIGLPGYSAPSAG
RAALNHAGKVDTHNFYGTDSDYDDSTTDTATMRFEHDINDNTTLRNTTRWSRVKQDYLLTAIMGGASNIT
TPTPSDVNTWTWSRTANTKDVSNKILTNQTNLTSTFYTGSIGHDVSTGVEFTRETQTNYGVNPVTLPAVN
LYHPDSSIHPGGLTRNGANANGQTDTFAIYAFDTLQLTRDWELNGGIRLDNYHTEYDSATACGGSGRGAI
TCPAGVAKGSPVTTVDTAKSGNLVNWKAGALYKLTENGNVYINYAVSQQPPGGSNFALAQSGSGNSANRT
DFKPQKANTSEIGTKWQVLDKRLLLTAALFRTDIENEVEQNDDGTYSQYGKKRVEGYELSVAGNITPAWQ
VIAGYTQQKATVKNGKDVAQDGSSSLPYTPEHAFTLWSQYQATDDLSVGGGARYIGSMHRGSDGAVGTPA
FTEGYWVADAKLGYRVNRNLDLQLNVYNLFDTDYVASINKSGYRYHPGEPRTFLLTANMHF
>gnl|CDD|182106 PRK09841, PRK09841, tyrosine-protein kinase
MTTKNMNTPPGSTQENEIDLLRLVGELWDHRKFIISVTALFTLIAVAYSLLSTPIYQADTLVQVEQKQGN
AILSGLSDMIPNSSPESAPEIQLLQSRMILGKTIAELNLRDIVEQKYFPIVGRGWARLTKEKPGELAISW
MHIPQLNGQDQQLTLTVGENGHYTLEGEEFTVNGMVGQRLEKDGVALTIADIKAKPGTQFVLSQRTELEA
INALQETFTVSERSKESGMLELTMTGDDPQLITRILNSIANNYLQQNIARQAAQDSQSLEFLQRQLPEVR
SELDQAEEKLNVYRQQRDSVDLNLEAKAVLEQIVNVDNQLNELTFREAEISQLYKKDHPTYRALLEKRQT
LEQERKRLNKRVSAMPSTQQEVLRLSRDVEAGRAVYLQLLNRQQELSISKSSAIGNVRIIDPAVTQPQPV
KPKKALNVVLGFILGLFISVGAVLARAMLRRGVEAPEQLEEHGISVYATIPMSEWLDKRTRLRKKNLFSN
QQRHRTKNIPFLAVDNPADSAVEAVRALRTSLHFAMMETENNILMITGATPDSGKTFVSSTLAAVIAQSD
QKVLFIDADLRRGYSHNLFTVSNEHGLSEYLAGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRM
RQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRSVGTSLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAIL
NGVIKRASTAYSYGYNYYGYSYSEKE
>gnl|CDD|236628 PRK09846, recT, recombination protein RecT
AKADLQKTQGNRAPAAVKNNTLADFINKMKEQFALALPKHMTADRLIRIATTEIRKNPKLAECDTMSFLG
AIMQCAQLGLEPGSALGHAYLLPFGNKNEKSGKKNVQLIIGYRGMIDLARRSGQIASISARVVYENDEFE
FEYGLEEKLVHRPGENGDGPVTHVYAVARLKDGGTQFEVMSRKQIEKVRDRSKAGNNGPWVDHYEEMAKK
TVIRRLFKYLPVSIEIQRAVSMDEKVRLDIDPDDSSVLTGEYSVIDNSAEEESANE
>gnl|CDD|182108 PRK09847, PRK09847, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
MNFHHLAYWQDKALSLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVF
ERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYG
EVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEA
GLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMKRVWLEAGGKSANIVFADC
PDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHA
DSVHSFIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLAND
SQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIW
ISLE
>gnl|CDD|182109 PRK09848, PRK09848, glucuronide transporter; Provisional
MNQQLSWRTIVGYSLGDVANNFAFAMGALFLLSYYTDVAGVGAAAAGTMLLLVRVFDAFADVFAGRVVDS
VNTRWGKFRPFLLFGTAPLMIFSVLVFWVPTDWSHSSKVVYAYLTYMGLGLCYSLVNIPYGSLATAMTQQ
PQSRARLGAARGIAASLTFVCLAFLIGPSIKNSSPEEMVSVYHFWTIVLAIAGMVLYFICFKSTRENVVR
IVAQPSLKISLQTLKRNRPLFMLCIGALCVLISTFAVSASSLFYVRYVLNDTGLFTVLVLVQNLVGTVAS
APLVPGMVARIGKKNTFLIGALLGTCGYLLFFWVSVWSLPVALVALAIASIGQGVTMTVMWALEADTVEY
GEYLTGVRIEGLTYSLFSFTRKCGQAIGGSIPAFILGLSGYIANQVQTPEVIMGIRTSIALVPCGFMLLA
FVIIWFYPLTDKKFKEIVVEIDNRKKVQ
>gnl|CDD|236629 PRK09849, PRK09849, putative oxidoreductase; Provisional
MTMAGGWTGKILRVNLTTGNITTEDSSKYKDYIGGMGIGYKIMYDEVPPGTKPFDEANKLVFATGPLTGS
GAPCSGRTNITSLSTFTKGNLVVDAHMGGHFAAQMKFAGYDAIIIEGKADSPVWLKIKDDKVSIEDADFL
WGKGTRATTEEICRLMGPEACVAAIGQAGENLVPLSGILNSRNHSAGGTGAVMGSKNLKAIGVEGTGGVN
IAGDRQEMKRLNDYMLTELIGANNNHVVPSTPQSWAEYSDPGSRWTARKGLFWGAAEGGPIETGEIPPGN
QNTVGFRTYKSVFDLGPAAEKYTVKMSGCHSCPIRCMTQLKIPRVKEYGVPSTGGNTCVANFVHTTIFPN
GPKDFEDKDEGRVIGNLVGLNLFDDYGLWCNYGQLHRDFTYCYSKGVFKRVLPAEEYAEIRWDQLEAGDP
AFLKDFYYRIAHREGELSHLADGSYAIAERWNLGEEYWGYAKNKLWSKFGYPVHHANEASAQVGSIVNCM
FNRDAMTHSHINFIGSGLPLKLQREIAAELWGSEDAYDETKNYTPINDAKAKFAKWSLLRNCLHDSLTLC
NWVWPMTVSPLKSRNYRGDLALEAKFFSAVTGEEMTEEELDLAAERIFTLHRALTVKLMQTKDMRNEHDL
ICSWVFDKDPDKPPFTEGTIKMDRDDMQAALTMFYKEMGWDPQTGCPTRATLERLGLEDVADDLAAHGLL
PA
>gnl|CDD|182111 PRK09850, PRK09850, pseudouridine kinase; Provisional
MREKDYVVIIGSANIDVAGYSHESLNYADSNPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQ
SLLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINDMNISNAITAEYLAQHREFIQRAKVIVA
DCNISEEALAWILDNAANVPVFVDPVSAWKCVKVRDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAA
WFHQHGLNRLVLSMGGDGVYYSDISGESGWSAPIKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQ
GCSSMALSCEYTNNPDLSIANVISLVENAECLN
>gnl|CDD|182112 PRK09852, PRK09852, cryptic 6-phospho-beta-glucosidase; Provisional
MSVFPEGFLWGGALAANQSEGAFREGGKGLTTVDMIPHGEHRMAVKLGLEKRFQLRDDEFYPSHEAIDFY
HRYKEDIALMAEMGFKVFRTSIAWSRLFPQGDELTPNQQGIAFYRSVFEECKKYGIEPLVTLCHFDVPMH
LVTEYGSWRNRKMVEFFSRYARTCFEAFDGLVKYWLTFNEINIMLHSPFSGAGLVFEEGENQDQVKYQAA
HHELVASALATKIAHEVNPQNQVGCMLAGGNFYPYSCKPEDVWAALEKDRENLFFIDVQARGAYPAYSAR
VFREKGVTIDKAPGDDEILKNTVDFVSFSYYASRCASAEMNANNSSAANVVKSLRNPYLQVSDWGWGIDP
LGLRITMNMMYDRYQKPLFLVENGLGAKDEIAANGEINDDYRISYLREHIRAMGEAIADGIPLMGYTTWG
CIDLVSASTGEMSKRYGFVYVDRDDAGNGTLTRTRKKSFWWYKKVIASNGEDLE
>gnl|CDD|182114 PRK09854, cmtB, PTS mannitol transporter subunit IIA
MRLSDYFPESSISVIHSAKDWQEAIDFSMVSLLDKNYISENYIQAIKDSTINNGPYYILAPGVAMPHARP
ECGALKTGMSLTLLEQGVYFPGNDEPIKLLIGLSAADADSHIGAIQALSELLCEEEILEQLLTASSEKQL
ADIISRG
>gnl|CDD|182115 PRK09855, PRK09855, PTS N-acetylgalactosamine transporter subunit IID
MGSEISKKDITRLGFRSSLLQASFNYERMQAGGFTWAMLPILKKIYKDDKPGLSAAMKDNLEFINTHPNL
VGFLMGLLISMEEKGENRDTIKGLKVALFGPIAGIGDAIFWFTLLPIMAGICSSFASQGNLLGPILFFAV
YLLIFFLRVGWTHVGYSVGVKAIDKVRENSQMIARSATILGITVIGGLIASYVHINVVTSFAIDSTHSVA
LQQDFFDKVFPNILPMAYTLLMYYFLRVKKAHPVLLIGVTFVLSIVCSAFGIL
>gnl|CDD|182116 PRK09856, PRK09856, fructoselysine 3-epimerase; Provisional
MKTGMFTCGHQRLPIEHAFRDASELGYDGIEIWGGRPHAFAPDLKAGGIKQIKALAQTYQMPIIGYTPET
NGYPYNMMLGDEHMRRESLDMIKLAMDMAKEMNAGYTLISAAHAGYLTPPNVIWGRLAENLSELCEYAEN
IGMDLILEPLTPYESNVVCNANDVLHALALVPSPRLFSMVDICAPYVQAEPVMSYFDKLGDKLRHLHIVD
SDGASDTHYIPGEGKMPLRELMRDIIDRGYEGYCTVELVTMYMNEPRLYARQALERFRALLPEDE
>gnl|CDD|182117 PRK09857, PRK09857, recombination-promoting nuclease RpnA
MSKKQSSTPHDALFKLFLRQPETARDFLAFHLPAPIHALCDMKTLKLESSSFIDDDLRESYSDVLWSVKT
EQGPGYIYCLIEHQSTSNKLIAFRMMRYAIAAMQNHLDAGYKTLPMVVPLLFYHGIESPYPYSLCWLDCF
ADPKLARQLYASAFPLIDVTVMPDDEIMQHRRMALLELIQKHIRQRDLMGLVEQMACLLSSGYANDRQIK
GLFNYILQTGDAVRFNDFIDGVAERSPKHKESLMTIAERLRQEGEQSKALHIAKIMLESGVPLADIMRFT
GLSEEELAAASQ
>gnl|CDD|137559 PRK09859, PRK09859, multidrug transporter subunit MdtE
MNRRRKLLIPLLFCGAMLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGG
IIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYD
TARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVTVQRLDPIYV
DLTQSVQDFLRMKEEVASGQIKQVQGSTPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPN
GDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQ
AGDRVIVSGLQRIRPGIKARAISSSQENASTESKQ
>gnl|CDD|182118 PRK09860, PRK09860, putative alcohol dehydrogenase; Provisional
MAASTFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQP
NPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTA
GTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATP
ITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVC
NAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDF
AVLATNALKDACGFTNPIQATHEEIVAIYRAAM
>gnl|CDD|182119 PRK09861, PRK09861, lipoprotein NlpA
MKLTTHHLRAGAALLLAGILLAGCDQSSSDAKHIKVGVINGAEQDVAEVAKKVAKEKYGLDVELVGFSGS
LLPNDATNHGELDANVFQHRPFLEQDNQAHGYKLVAVGNTFVFPMAGYSKKIKTVAQIKEGATVAIPNDP
TNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMELEGAQLPRVLDDPKVDVAIISTTYIQQT
GLSPVHDSVFIEDKNSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAETIFNGGAVPGW
>gnl|CDD|182120 PRK09862, PRK09862, ATP-dependent protease
MSLSIVHTRAALGVNAPPITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLA
PADLPKEGGRYDLPIAIALLAASEQLTANKLDEYELVGELALTGALRGVPGAISSATEAIKSGRKIIVAK
DNEDEVGLINGEGCLIADHLQAVCAFLEGKHALERPKPTDAVSRALQHDLSDVIGQEQGKRGLEITAAGG
HNLLLIGPPGTGKTMLASRINGLLPDLSNEEALESAAILSLVNAESVQKQWRQRPFRSPHHSASLTAMVG
GGAIPGPGEISLAHNGVLFLDELPEFERRTLDALREPIESGQIHLSRTRAKITYPARFQLVAAMNPSPTG
HYQGNHNRCTPEQTLRYLNRLSGPFLDRFDLSLEIPLPPPGILSKTVVPGESSATVKQRVMAARERQFKR
QNKLNAWLDSPEIRQFCKLESEDARWLEETLIHLGLSIRAWQRLLKVARTIADIDQSDIITRQHLQEAVS
YRAIDRLLIHLQKLLT
>gnl|CDD|182121 PRK09863, PRK09863, putative frv operon regulatory protein; Provisional
MLNERELKIVDLLEQQDRSGGELAQQLGVSRRTIVRDIAYINFTLNGKAIGSISGSAKYHLEILNRRSLF
QLLQKSDNEDRLLLLRLLLNTFTPMAQLASALNLSRTWVAERLPRLNQRYERICCIASRPGLGHFIDETE
EKRIDILANLIRKDPQLIPKAGPTRDNLQHLSRTACDNQHRWPLMQGDYLSSLILAIYALRNQLTDEWPQ
YPGDEIKQIVEHSGLFLGDNAVRTLTGLIEKQHQQAQVISADNVQQLLQRVPGIASLNAIDTQLVENIFG
HLLRCLAFPVWIAEHRQSSINNLKAQNPAAFDMALHFITLLREQLDIPLFDSDLIALYFACALERHQNER
VPILLLADQNSIATINQLIIEQKVLNIRVIIVRSLSELEAIREEIEPLLIINNSHYLVDLQDAINFYITF
KNVITAAGIEQLKHLLATAYIRQNPERFLSAPGSFHYSNVRGEKWQHVTRQICAQLVAQHLLTADEAQRI
IAREGAGNQLILNHLSIPHCWTEQERRYRGFAITLAQPIEVNNEVIYLVLIVLAAADAAHELKIFSYLYS
VLCQHPAEVIAGVTGYEAFIELLH
>gnl|CDD|182122 PRK09864, PRK09864, aminopeptidase
MNIELLQQLCEASAVSGDEQEVRDILINTLEPCVNEITFDGLGSFVARKGNKGPKVAVVGHMDEVGFMVT
HIDESGFLRFTTIGGWWNQSMLNHRVTIRTHKGVKIPGVIGSVAPHALTEKQKQQPLSFDEMFIDIGANS
REEVEKRGVEIGDFISPEANFACWGEDKVVGKALDNRIGCAMMAELLQTVNNPEITLYGVGSVEEEVGLR
GAQTSAEHIKPDVVIVLDTAVAGDVPGIDNIKYPLKLGQGPGLMLFDKRYFPNQKLVAALKSCAAHNDLP
LQFSTMKTGATDGGRYNVMGGGRPVVALCLPTRYLHANSGMISKADYDALLTLIRDFLTTLTAEKVNAFS
QFRQVD
>gnl|CDD|182123 PRK09866, PRK09866, clamp-binding protein CrfC
MYTQTLYELSQEAERLLQLSRQQLQLLEKMPLSVPGDDAPQLALPWSQPNIAERHAMLNNELRKISRLEM
VLAIVGTMKAGKSTTINAIVGTEVLPNRNRPMTALPTLIRHTPGQKEPVLHFSHVAPIDCLIQQLQQRLR
DCDIKHLTDVLEIDKDMRALMQRIENGVAFEKYYLGAQPIFHCLKSLNDLVRLAKALDVDFPFSAYAAIE
HIPVIEVEFVHLAGLESYPGQLTLLDTPGPNEAGQPHLQKMLNQQLARASAVLAVLDYTQLKSISDEEVR
EAILAVGQSVPLYVLVNKFDQQDRNSDDADQVRALISGTLMKGCITPQQIFPVSSMWGYLANRARHELAN
NGKLPPPEQQRWVEDFAHAALGRRWRHADLADLEHIRHAADQLWEDSLFAQPIQALLHAAYANASLYALR
SAAHKLLNYAQQAREYLDFRAHGLNVACEQLRQNIHQVEESLQLLQLNQAQVSGEIKHEIELALTSANHF
LRQQQDAVNAQLAALFQDDSEPLSEIRTRCETLLQTAQNTISRDFTLRFAELESTLCRVLTDVIRPIEQQ
VKMELSESGFRPGFHFPVFHGVVPHFNTRQLFSEVISRQEATDEQSTRLGVVRETFSRWLNQPDWGRGNE
KSPTETVDYSVLQRALSAEVDLYCQQMAKVLAEQVDESVTAGMNTFFAEFASCLTELQTRLRESLALRQQ
NESVVRLMQQQLQQTVMTHGWIYTDAQLLRDDIQTLFTAER
>gnl|CDD|182124 PRK09867, PRK09867, hypothetical protein; Provisional
MTRTLKPLILNTGALALTLILIYTGISAHDKLTWLMEVTPVIIVVPLLLATARRYPLTPLLYTLIFFHAI
ILMVGGQYTYAKVPVGFEVQEWLGLSRNPYDKLGHFFQGLVPALVAREILVRGMYVRGRKMVAFLVCCVA
LAISAMYELIEWWAALAMGQGADDFLGTQGDQWDTQSDMFCALLGALTTVIFLARFHCRQLRRFGLITG
>gnl|CDD|182125 PRK09870, PRK09870, tyrosine recombinase; Provisional
MKNKADNKKRNFLTHSEIESLLKAANTGPHAARNYCLTLLCFIHGFRASEICRLRISDIDLKAKCIYIHR
LKKGFSTTHPLLNKEIQALKNWLSIRTSYPHAESEWVFLSRKGNPLSRQQFYHIISTSGGNAGLSLEIHP
HMLRHSCGFALANMGIDTRLIQDYLGHRNIRHTVWYTASNAGRFYGIWDRARGRQRHAVL
>gnl|CDD|182126 PRK09871, PRK09871, tyrosine recombinase; Provisional
MSKRRYLTGKEVQAMMQAVCYGATGARDYCLILLAYRHGMRISELLDLHYQDLDLNEGRINIRRLKNGFS
TVHPLRFDEREAVERWTQERANWKGADRTDAIFISRRGSRLSRQQAYRIIRDAGIEAGTVTQTHPHMLRH
ACGYELAERGADTRLIQDYLGHRNIRHTVRYTASNAARFAGLWERNNLINEKLKREEV
>gnl|CDD|182127 PRK09874, PRK09874, multidrug efflux MFS transporter MdtG
MSPCENDTPINWKRNLTVAWLGCFLTGAAFSLVMPFLPLYVEQLGVTGHSALNMWSGLVFSITFLFSAIA
SPFWGGLADRKGRKIMLLRSALGMGIVMVLMGLAQNIWQFLILRALLGLLGGFVPNANALIATQVPRNKS
GWALGTLSTGGVSGALLGPLAGGLLADSYGLRPVFFITASVLFLCFLVTLFCIRENFQPVSKKEMLHMRE
VVTSLKNPKLVLSLFVTTLIIQVATGSIAPILTLYVRELAGNVSNIAFISGMIASVPGVAALLSAPRLGK
LGDRIGPEKILITALIFSVLLLIPMSFVQTPLQLGILRFLLGAADGALLPAVQTLLVYNSSNQIAGRIFS
YNQSFRDIGNVTGPLMGAAISANYGFRAVFLVTAGVVLFNAVYSWNSLRRRRIPQVSN
>gnl|CDD|182128 PRK09875, PRK09875, phosphotriesterase-related protein
MSFDPTGYTLAHEHLHIDLSGFKNNVDCRLDQYAFICQEMNDLMTRGVRNVIEMTNRYMGRNAQFMLDVM
RETGINVVACTGYYQDAFFPEHVATRSVQELAQEMVDEIEQGIDGTELKAGIIAEIGSSEGKITPLEEKV
FIAAALAHNQTGRPISTHTSFSTMGLEQLALLQAHGVDLSRVTVGHCDLKDNLDNILKMIDLGAYVQFDT
IGKNSYYPDEKRIAMLHALRDRGLLNRVMLSMDITRRSHLKANGGYGYDYLLTTFIPQLRQSGFSQADVD
VMLRENPSQFFQ
>gnl|CDD|182129 PRK09877, PRK09877, 2,3-diketo-L-gulonate TRAP transporter small permease protein YiaM; Provisional
MKRILEGILAINIAVLSCIVFINIILRYGFQTSILSVDELSRYLFVWLTFIGAIVAFMDNAHVQVTFLVE
KLSPANQRRVSLLTHSLILLLCGALAWGATLKTIQDWSDYSPILGLPIGLMYAACLPTSLVIALFELRHL
YQLITRSNSLTSPQQGA
>gnl|CDD|182130 PRK09880, PRK09880, L-idonate 5-dehydrogenase; Provisional
MQVKTQSCVVAGKKDVAVTEQEIEWNNNGTLVQITRGGICGSDLHYYQEGKVGNFVIKAPMVLGHEVIGK
IVHSDSSGLKEGQTVAINPSKPCGHCKYCLSHNENQCTTMRFFGSAMYFPHVDGGFTRYKVVDTAQCIPY
PEKADEKVMAFAEPLAVAIHAAHQAGDLQGKRVFVSGVGPIGCLIVAAVKTLGAAEIVCADVSPRSLSLA
REMGADKLVNPQNDDLDHYKAEKGYFDVSFEVSGHPSSINTCLEVTRAKGVMVQVGMGGAPPEFPMMTLI
VKEISLKGSFRFTEEFNTAVSWLANGVINPLPLLSAEYPFTDLEEALIFAGDKTQAAKVQLVF
>gnl|CDD|182131 PRK09881, PRK09881, D,D-dipeptide ABC transporter permease
MMLSEETSAVRPQKQTRFNGAKLVWMLKGSPLTVTGAVIIVLMLLMMIFSPWLATHDPNAIDLTARLLPP
SAAHWFGTDEVGRDLFSRVLVGSQQSILAGLVVVAIAGMIGSLLGCLSGVLGGRADAIIMRIMDIMLSIP
SLVLTMALAAALGPSLFNAMLAIAIVRIPFYVRLARGQALVVRQYTYVQAAKTFGASRWHLISWHILRNS
LPPLIVQASLDIGSAILMAATLGFIGLGAQQPSAEWGAMVANGRNYVLDQWWYCAFPGAAILLTAVGFNL
FGDGIRDLLDPKAGGK
>gnl|CDD|236631 PRK09885, PRK09885, type II toxin-antitoxin system YafO family toxin
MMRVFKTKLIRLQLTAEELDALTADFISYKRDGVLPDIFGRDALYDDSFTWPLLKFERVAHIHLANVNNP
FPLQLRQFSRTSGYHLVYCQGAFDEQAYLLIAILKPEPHKLARDNNQMHKLGKMAEAFRMRF
>gnl|CDD|77467 PRK09890, PRK09890, cold shock protein CspG; Provisional
MSNKMTGLVKWFNADKGFGFITPDDGSKDVFVHFTAIQSNEFRTLNENQKVEFSIEQGQRGPAAANVVTL
>gnl|CDD|170147 PRK09891, PRK09891, protein YmcE
MRRWISQNNIRLPRGAFFISALFFFNAVCIVSDNLLIIESFGEMAYNISYLTRVPGTNTLLACCCLLRPE
EVNSEY
>gnl|CDD|182133 PRK09894, PRK09894, diguanylate cyclase; Provisional
MIKKTTEIDAILLNLNKAIDAHYQWLVSMFRSVVARDASKPEITDNHSHGLCQFGRWIDHLGPLDNDELP
YVRLLDSAHQHMHNCARELLLAIVEGHWQDAHFDAFQEGLLSFTAALTDYKIYLLTIRSNMDVLTGLPGR
RVLDESFDHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEF
IICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTG
RNRVMFIDEQNVINRV
>gnl|CDD|182134 PRK09897, PRK09897, FAD-NAD(P)-binding protein
MKKIAIVGAGPTGIYTFFSLLQQQTPLSISIFEQADEAGVGMPYSDEENSKMMLANIASIEIPPIYCTYL
EWLQKQEDSHLQRYGVKKETLHDRQFLPRILLGEYFRDQFLRLVDQARQQKFAVAVYESCQVTDLQITNA
GVMLATNQDLPSETFDLAVIATGHVWPDEEEATRTYFPSPWSGLMEAKVDACNVGIMGTSLSGLDAAMAV
AIQHGSFIEDDKQHVVFHRDNASEKLNITLMSRTGILPEADFYCPIPYEPLHIVTDQALNAEIAKGEEGL
LDRVFRLIVEEIKFADPDWSQRIALESLNVDSFAQAWFAERKQRDPFDWAEKNLQEVERNKREKHTVPWR
YVILRLHEAVQEIVPHLNEHDHKRFSKGLARVFIDNYAAIPSESIRRLLALREAGIIHILALGEDYEMEI
NESRTVIKTEDNSYSFDVFIDARGQRPLKVKDIPFPGLREQLQKTGDEIPDVGEDYTLQQPEDIRGRVAF
GALPWLMHDQPFVQGLTACAEIGEAMARAVVKPASRARRRLSFD
>gnl|CDD|182135 PRK09898, PRK09898, ferredoxin-like protein
MNPVDRPLLDIGLTRLEFLRISGKGLAGLTIAPALLSLLGCKQEDIDSGTVGLINTPKGVLVTQRARCTG
CHRCEISCTNFNDGSVGTFFSRIKIHRNYFFGDNGVGSGGGLYGDLNYTADTCRQCKEPQCMNVCPIGAI
TWQQKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLCGECANACPTGALKIIEWKDITV
>gnl|CDD|182136 PRK09902, PRK09902, lipopolysaccharide kinase InaA
MAVSAKYDEFNHWWATEGDWVEEPNYRRNGMSGVQCVERNGKKLYVKRMTHHLFHSVRYPFGRPTIVREV
AVIKELERAGVIVPKIVFGEAVKIEGEWRALLVTEDMAGFISIADWYAQHAVSPYSDEVRQAMLKAVALA
FKKMHSVNRQHGCCYVRHIYVKTEGKAEAGFLDLEKSRRRLRRDKAINHDFRQLEKYLEPIPKADWEQVK
AYYYAM
>gnl|CDD|104216 PRK09903, PRK09903, transporter YfdV
MLTFFIGDLLPIIVIMLLGYFSGRRETFSEDQARAFNKLVLNYALPAALFVSITRANREMIFADTRLTLV
SLVVIVGCFFFSWFGCYKFFKRTHAEAAVCALIAGSPTIGFLGFAVLDPIYGDSVSTGLVVAIISIIVNA
ITIPIGLYLLNPSSGADGKKNSNLSALISAAKEPVVWAPVLATILVLVGVKIPAAWDPTFNLIAKANSGV
AVFAAGLTLAAHKFEFSAEIAYNTFLKLILMPLALLLVGMACHLNSEHLQMMVLAGALPPAFSGIIIASR
FNVYTRTGTASLAVSVLGFVVTAPLWIYVSRLVS
>gnl|CDD|182137 PRK09906, PRK09906, DNA-binding transcriptional regulator HcaR; Provisional
MELRHLRYFVAVAEELNFTKAAEKLHTAQPSLSQQIKDLENCVGVPLLVRDKRKVALTAAGEVFLQDARA
ILEQAEKAKLRARKIVQEDRQLTIGFVPSAEVNLLPKVLPMFRLRHPDTLIELVSLITTQQEEKLRRGEL
DVGFMRHPVYSDEIDYLELLDEPLVVVLPVDHPLAHEKEITAAQLDGVNFISTDPAYSGSLAPIIKAWFA
QHNSQPNIVQVATNILVTMNLVGMGLGCTIIPGYMNNFNTGQVVFRPLAGNVPSIALLMAWKKGEMKPAL
RDFIAIVQERLASVTA
>gnl|CDD|182138 PRK09907, PRK09907, endoribonuclease MazF
MVSRYVPDMGDLIWVDFDPTKGSEQAGHRPAVVLSPFMYNNKTGMCLCVPCTTQSKGYPFEVVLSGQERD
GVALADQVKSIAWRARGATKKGTVAPEELQLIKAKINVLIG
>gnl|CDD|182139 PRK09908, PRK09908, xanthine dehydrogenase iron sulfur-binding subunit XdhC
MNHSETITIECTINGMPFQLHAAPGTPLSELLREQGLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAW
AEGKEIRTLEGEAKGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAKPREKPLTITEIRRGLAGNLC
RCTGYQMIVNTVLDCEKTK
>gnl|CDD|182140 PRK09912, PRK09912, L-glyceraldehyde 3-phosphate reductase; Provisional
MVWLANPERYGQMQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPP
GSAEENFGRLLREDFAAYRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRV
DENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDKSGLLD
TLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQS
MAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNLTFSTEELAQIDQHIADGELNLWQASSDK
>gnl|CDD|182141 PRK09913, PRK09913, PTS fructose transporter subunit IIA
MAALTASCIDLNIQGNGAYSILKQLATIALQNGFITDSHQFLQTLLLREKMHSTGFGSGVAVPHGKSACV
KQPFVLFARKAQAIDWQASDGEDVNCWICLGVPQSGEEDQVKIIGTLCRKIIHQDFIHQLKQGDTDQVLA
LLNQTLSS
>gnl|CDD|182142 PRK09915, PRK09915, MdtP family multidrug efflux transporter outer membrane subunit
MINRQLSRLLLCSILGSTTLISGCALVRKDSAPHQQLKPEQIKLADDIHLASSGWPQAQWWKQLNDPQLD
ALIQRTLSGSHTLAEAKLREEKAQSQADLLDAGSQLQVAALGMLNRQRVSANGFLSPYAMDAPALGMDGP
YYTEATVGLFAGLDLDLWGVHRSAVAAAIGAHNAALAETAAVELSLTTGVAQLYYSMQASYQMLDLLEQT
RDVIDYAVKAHQSKVAHGLEAQVPFHGARAQILAVDKQIAAVKGQITETRESLRALIGAGASDMPEIKPV
ALPRVQTGIPATLSYELLARRPDLQAMRWYVQASLDQVDSARALFYPSFDIKAFFGLDAIHLDTLFKKTS
RQFNFIPGLKLPLFDGGRLNANLEGTRAASNMMIERYNQSVLNAVRDVAVNGTRLQTLNDEREMQAERVE
ATRFTQRAAEAAYQRGLTSRLQATEARLPVLAEEMSLLMLDSRRVIQSIQLMKSLGGGYQAAPVVEKK
>gnl|CDD|182143 PRK09917, PRK09917, threonine/serine exporter
MGVIEFLLALAQDMILAAIPAVGFAMVFNVPVRALRWCALLGAIGHGSRMLMMTSGLNIEWSTFMASMLV
GTIGIQWSRWYLAHPKVFTVAAVIPMFPGISAYTAMISAVKISHLGYSEPLMITLLTNFLKASSIVGALS
IGLSLPGLWLYRKRPRV
>gnl|CDD|236632 PRK09918, PRK09918, putative fimbrial chaperone protein; Provisional
NRFNLFFLFTALVLLSSSSAVHAAGMVPETSVVIVEESDGEGSINVKNTDSNPILLYTTLVDLPEDKSKL
LLVTPPVARVEPGQSQQVRFILKSGSPLNTEHLLRVSFEGVPPKPGGKNKVVMPIRQDLPVLIQPAALPV
VRDPWKLLVWSISGNNLVVSNPSPYVVRLGQQVILLPSGKVVALPKPYILPGESLTVAITNSKATDTKVR
FFPASRYGFVVPSYTAPLTP
>gnl|CDD|236633 PRK09919, PRK09919, anti-adapter protein IraM; Provisional
MKWIVIDTVISPSTGISFSAISSLRNLKLILWYQADIFLPPGSIITPVKSGVLLNDKPYPITIYNITPFN
KALWSLLKSSQECPGNENKITNKCLYNFSCIIKICPYGLKRNIP
>gnl|CDD|182146 PRK09920, PRK09920, acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
MKTKLMTLQDATGFFRDGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRV
KKVIASHIGTNPETGRRMISGEMDVELVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEGKQTLTLDGKT
WLLERPLRADLALIRAHRADTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVI
DHIIVSQES
>gnl|CDD|182147 PRK09921, PRK09921, permease DsdX; Provisional
MHSQIWVVSTLLISIVLIVLTIVKFKFHPFLALLLASFFVGAMMGMGPLEMVNAIESGIGGTLGFLAAVI
GLGTILGKMMEVSGAAERIGLTLQRCRWLSADVIMVLVGLICGITLFVEVGVVLLIPLAFSIAKKTNTSL
LKLAIPLCTALMAVHCVVPPHPAALFVANKLGADIGSVIVYGLLVGLMASLVGGPLFLKFLGNRLPFKPV
PTEFADLEVRDEKTLPSLGATLFTVLLPIGLMLVKTVAELNMAKEGTLYTLLEFIGNPITAMFIAVFVAY
YILGIRQHMGMGTLLTHTENGFGSIANILLIIGAGGAFNAILKSSGLADTLAVILSNMHMHPILLAWLVA
LILHAAVGSATVAMMGATAIVAPMLPLYPDISPEIIAIAIGSGAIGCTIVTDSLFWLVKQYCGATLNETF
KYYTTATFIASVVALAGTFLLSFII
>gnl|CDD|182148 PRK09922, PRK09922, lipopolysaccharide 1,6-galactosyltransferase
MKIAFIGEAVSGFGGMETVISNVINTFEESKINCEMFFFCRNDKMDKAWLKEIKYAQSFSNIKLSFLRRA
KHVYNFSKWLKETQPDIVICIDVISCLYANKARKKSGKQFKIFSWPHFSLDHKKHAECKKITCADYHLAI
SSGIKEQMMARGISAQRISVIYNPVEIKTIIIPPPERDKPAVFLYVGRLKFEGQKNVKELFDGLSQTTGE
WQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQPWEVVQQKIKNVSALLLTSKFEGFPMTLLEAMSY
GIPCISSDCMSGPRDIIKPGLNGELYTPGNIDEFVGKLNKVISGEVKYQHDAIPNSIERFYEVLYFKNLN
NALFSKLQK
>gnl|CDD|137592 PRK09925, PRK09925, leu operon leader peptide; Provisional
MTHIVRFIGLLLLNASSLRGRRVSGIQH
>gnl|CDD|236634 PRK09926, PRK09926, fimbrial chaperone
MFFNTKHTTALCFATCMAFSSSSIADIVISGTRIIYKSDQKDVNVRLENKGNNPLLVQSWLDTGDDNAEP
GSIKVPFTATPPVSRIDPKRGQTIKLMYTASTALPKDRESVFWFNVLEVPPKPDAEKVANQSLLQLAFRT
RIKLFYRPDGLKGNPSEAPLALKWSWAGSEGKASLRVTNPTPYYVSFSSGDLEAGGKRYPVDSKMIAPFS
DESMKVKGLSGKASSGKVHFYAINDFGGAIEGNASL
>gnl|CDD|236635 PRK09928, PRK09928, choline transport protein BetT; Provisional
MVMTDLSHKREKDRINPVVFYTSAGLILLFSLTTILFTDFSNRWINRTLNWVSKTFGWYYLLAATLYIVF
VIFIACSRFGSIKLGPEQSKPEFSLLSWAAMLFAAGIGIDLMFFSVAEPVTQYMQPPEGAGQTIEAARQA
MVWTLFHYGLTGWSMYALMGMALGYFSYRYNLPLTIRSALYPIFGKRINGPIGHSVDIAAVIGTIFGIAT
TLGIGVVQLNYGLSVLFDIPESLAAQAALIALSVIIATISVTSGVNKGIRVLSELNVLLALGLILFVLFM
GDTSFLLNALVLNVGDYVNRFMGMTLNSFAFDRPTEWMNNWTLFFWAWWVAWSPFVGLFLARISRGRTIR
QFVLGTLIIPFTFTLLWLSIFGNSALYEIIHGNAAFAEEAMAHPERGFYSLLAQYPAFTFSASVATITGL
LFYVTSADSGALVLGNFTSKLKDINSDAPNWLRVFWSVAIGLLTLGMLMTNGISALQNTTVIMGLPFSFV
IFFVMAGLYKSLKVEDYRRASANRDTAPRLVGLQDRLNWKQRLSRVMNYPGTRYTRRMLDTVCRPAMEEV
AQELRLRGAYVELNELPPEEDERLGHLDLLVHLGDEQNFVYQIWPQRYSVPGFTYRARSGKSTYYRLETF
LLEGSQGNDLMDYSKEQVINDILDQYERHLNFLHLHREAPGNSVMFPDA
>gnl|CDD|182151 PRK09929, PRK09929, hypothetical protein; Provisional
MKIISKMLLGALAFAVTNVYAAELMTKAEFEKVESQYEKIGTISTSNEMSTADAKEDLIKKADEKGADVL
VLTSGQTDNKIHGTADIYKKK
>gnl|CDD|182152 PRK09932, PRK09932, glycerate 3-kinase
MKIVIAPDSFKESLSAEKCCQAIKAGFSTLFPDANYICLPIADGGEGTVDAMVAATGGNIVTLEVCGPMG
EKVNAFYGLTGDGKTAVIEMAAASGLMLVAPEKRNPLLASSFGTGELIRHALDNGIRHIILGIGGSATVD
GGMGMAQALGVRFLDADGQVLGANGGNLARVASIEMDECDPRLANCHIEVACDVDNPLVGARGAAAVFGP
QKGATPEMVEELEQGLQNYARVLQQQTEINVCQMAGGGAAGGMGIAAAVFLNADIKPGIEIVLNAVNLEQ
AVQGAALVITGEGRIDSQTAGGKAPLGVASVAKQFNVPVIGIAGVLGDGVEVVHQYGIDAVFSILPRLAP
LAEVLASGETNLFNSARNIACAIKIGQGIKN
>gnl|CDD|182153 PRK09934, PRK09934, fimbriae assembly protein
MRRVFFACFCGLLWSPLSWAADPLGEINIELHGNVVDFTCTVNTADSDKTVDLGTWPTKQLLNAGDTTQP
VPFSLKLEGCPPGSASITFTGTPASDTNLLALDDPAMAQTVAIEIRDSDRSRLALGQASPTVEVDANGNA
TLNFYANYIALADGVQPGVAKADATFMINYN
>gnl|CDD|182154 PRK09935, PRK09935, fimbriae biosynthesis transcriptional regulator FimZ
MKPASVIIMDTHPIIRMSIEVLLQKNSELQIVLKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKR
IKQIQSTVKVLFLSSKSECFYAGRAIQAGANGFVSKCNDQNDIFHAVQMILSGYTFFPSETLNYIKSNKC
STNSSTDTVLSNREVTILRYLVSGLSNKEIADQLLLSNKTVSAHKSNIYGKLGLHSIVELIDYAKLHELL
>gnl|CDD|182155 PRK09936, PRK09936, DUF4434 family protein
MRKFIFVLLTLLLVSPFSQAMKGIFYQPQNRDSQVTDTQWQGLWSQLRLQGFDTLVVQWTRYGDADFGGQ
RGWLAKRLAAAQQAGLKLVVGLYADPEFFMHQKQDGAALESYLNRQLGASLQQARLWSAAWGVPVDGWYL
PAELDDLNWRDEARRQPLLTWLNAAQRLIDVSAKPVHISAFFAGNMSPDGYRQWLEQLKATGVNVWVQDG
SGVDKLTAEQRERYLQASLDCQSSAPASGIVYELFRQVSGKGKPFTAEPKPPAEIASLLAKRSSCGKDTL
YFSLRYLPVAHGILEY
>gnl|CDD|77494 PRK09937, PRK09937, cold shock-like protein CspD
MEKGTVKWFNNAKGFGFICPEGGGEDIFAHYSTIQMDGYRTLKAGQSVQFDVHQGPKGNHASVIVPVEVE
AAVA
>gnl|CDD|182156 PRK09939, PRK09939, acid resistance putative oxidoreductase YdeP
MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGA
KAIAWEVTDKQVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQS
YSDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCD
LVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRI
GGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAE
LADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGITEKP
SAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVA
TKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQ
AALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGL
LEDPSSAFNSKLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPD
GKRSSRRMDRLKVVIYPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPSN
>gnl|CDD|182157 PRK09940, PRK09940, transcriptional regulator YdeO; Provisional
MSLVCSVIFIHHAFNANILDKDYAFSDGEILMVDNAVRTHFEPYERHFKEIGFNENTIKKYLQCTNIQTV
TVPVPAKFLRASNVPTGLLNEMIAYLNSEERNHHNFSELLLFSCLSIFAACKGFITLLTNGVLSVSGKVR
NIVNMKLAHPWKLKDICDCLYISESLLKKKLKQEQTTFSQILLDARMQHAKNLIRVEGSVNKIAEQCGYA
STSYFIYAFRKHFGNSPKRVSKEYRCQRHTGMNTGNTMSALAI
>gnl|CDD|182158 PRK09943, PRK09943, HTH-type transcriptional regulator PuuR
MSDEGLAPGKRLSEIRQQQGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEFFSEP
EKPDEPQVVINQDDLIEMGSQGVSMKLVHNGNPNRTLAMIFETYQPGTTTGERIKHQGEEIGTVLEGEIV
LTINGQDYHLVAGQSYAINTGIPHSFSNTSAGICRIISAHTPTTF
>gnl|CDD|137602 PRK09945, PRK09945, hypothetical protein; Provisional
MGSDAKNLMSDGNVQIVKTGEVIGATQLTEGELIVEAGGRAENTVVTGAGWLKVATGGIAKCTQYGNNGT
LSVSDGAIATDIVQSEGGAISLSTLATVNGRHPEGEFSVDQGYACGLLLENGGNLRVLEGHRAEKIILDQ
EGGLLVNGTTSAVVVDEGGELLVYPGGEASNCEINQGGVFMLAGKASDTLLAGGTMNNLGGEDSDTIVEN
GSIYRLGTDGLQLYSSGKTQNLSVNVGGRAEVHAGTLENAVIQGGTVILLSPTSADENFVVEEDRAPVEL
TGSVALLDGASMIIGYGADLQQSTITVQQGGVLILDGSTVKGDSVTFSVGNINLNGGKLWLITGAATHVQ
LKVKRLRGEGAICLQTSAKEISPDFINVKGEVTGDIHVEITDASRQTLCNALKLQPDEDGIGATLQPA
>gnl|CDD|182159 PRK09946, PRK09946, hypothetical protein; Provisional
MIITRADLREWRVGAVMYRWFLRHFPRGGSYADIHHALIEEGYTDWAESLVEYAWKKWLADENFAHQEVS
SMQKLATDPGERPFCSQFARSDDHARIGCCEDNARIATAGYAAQIASMGYSVRIGSVGFNSHIGSSGERA
RVAVTGNSSRISSAGDSSRIANTGMRVRVCTLGERCHVASNGDLVQIASFGANARIANSGDNVHIIASGE
NSTVVSTGVVDSIILGPGGSAALAYHDGERVRFAVAIEGENNIRAGVRYRLNEQHQFVEC
>gnl|CDD|182160 PRK09947, PRK09947, YdhW family putative oxidoreductase system protein
MGEMNHQDELPLAEVSEVDEAKRQWLQGMRHPVDTVTEPEPAEILAEFIRQHSAAGQLVARAVFLSPPYS
VAEEELSVLLEELKENGDYADIACLTGSQDDYYYSTQAMSENYAAMSLQVVEQDICRAIAHAVRFECQTY
PRPYKVAMLMQAPYYFQEAQIEAALAAMDVAPEYADIRQVESSTGVLYLFSERFMTYGKAYGLCEWLEVE
QFQNP
>gnl|CDD|236636 PRK09950, PRK09950, putative transporter; Provisional
MQNNKKKKDKPLISTSLLAVFFIVAALSLFPQQSAAAANTIFQWVTRTFGSPVQLFVLLAMILVLYLATS
KYGNIRLGEGKPEYSTLSWLFMFICAGLGSSTLYWGVMEWAYYYQTPGLNIAPRSPKALEYSVSYSFFHW
GISAWATYALASLIMAYHFHVRKNKGLSLSGIIAAITGVKPQGPWGRLVDLMFLIATVGALTISLVVTAA
TFTRGLSALTGLPNNFTVQAFVILLSGVIFCLSSYIGIDNGLQRLSKMVGWGAFLFALLVLIVGPTEFIT
NNIINSIGLTTQNFLQMSLFTDPMGDGSFTRNWTVFYWLWWISYTPGVAMFVTRVSRGRKIKEVIWGLIL
GSSVGCWFFFGVLESYAIHQFINGVINVPQILNTLGGETAVQQLLSSLPAGKLFLAAYLGIMIIFLASHM
DAVAYTMAATSTRNLREGDDPDRGLRLFWCVVITLIPLSILFTGASLDTMKTTVVLTALPFLVILLIKVY
GFIRWLKQDYADVPAH
>gnl|CDD|182162 PRK09951, PRK09951, hypothetical protein; Provisional
MCGRFAQSQTREDYLAYLAEDIERDIPYDPEPIGRYNVAPGTKVLLLSERDEHLHLDPVFWGYAPGWWDK
PPLINARVETAATSRMFKPLWQHGRAICFADGWFEWKKEGDKKQPYFIYRADGQPIFMAAIGSTPFERGD
EAEGFLIVTAAADQGLVDIHDRRPLVLSPEAAREWMRQEISGKEASEIATSGCVPANQFTWHPVSRAVGN
VKNQGAELIQPV
>gnl|CDD|182163 PRK09952, PRK09952, shikimate transporter; Provisional
MDSTLISTRPDEGTLSLSRARRAALGSFAGAVVDWYDFLLYGITAALVFNREFFPQVSPAMGTLAAFATF
GVGFLFRPLGGVVFGHFGDRLGRKRMLMLTVWMMGIATALIGLLPSFSTIGWWAPVLLVTLRAIQGFAVG
GEWGGAALLAVESAPKNKKAFYSSGVQVGYGVGLLLSTGLVSLISMMTTDEQFLSWGWRIPFLFSIVLVL
IALWVRNGMEESAEFEQQQHEQAAAKKRIPVIEALLRHPGAFLKIIALRLCELLTMYIVTAFALNYSTQN
LGLPRELFLNIGLLVGGLSCLTIPCFAWLADRFGRRRVYITGALIGTLSAFPFFMALEAQSIFWIVFFSI
MLANIAHDMVVCVQQPMFTEMFGASYRYSGAGVGYQVASVVGGGFTPFIAAALVTYFGGSWHSVAIYLLA
GCLISAMTALLMKDNQRA
>gnl|CDD|182165 PRK09954, PRK09954, sugar kinase
MNNREKEILAILRRNPLIQQNEIADILQISRSRVAAHIMDLMRKGRIKGKGYILTEQEYCVVVGAINMDI
RGMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCI
RLHGQSTSTYLAIANRQDETVLAINDTHILQQLTPQLLNGSRDLIRHAGVVLADCNLTAEALEWVFTLAD
EIPVFVDTVSEFKAGKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDE
SVFCSEKDGEQFLLTAPAHTTVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAISRASGSLNNPTL
SADNALSLVPMV
>gnl|CDD|182166 PRK09955, rihB, ribosylpyrimidine nucleosidase
MEKRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGMPQP
IMRQQIVADNIHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAI
LPKIREIVLMGGAYGTGNFTPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGG
PAGELFSDIMNFTLKTQFENYGLAGGPVHDATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGV
LGKPANTKVGITIDTDWFWGLVEECVRGYIKTH
>gnl|CDD|182167 PRK09956, PRK09956, ISNCY family transposase
MTESTTSSPHDAVFKTFMFTPETARDFLEIHLPEPLRKLCNLQTLRLEPTSFIEKSLRAYYSDVLWSVET
SDGDGYIYCVIEHQSSAEKNMAFRLMRYATAAMQRHLDKGYDRVPLVVPLLFYHGETSPYPYSLNWLDEF
DDPQLARQLYTEAFPLVDITIVPDDEIMQHRRIALLELIQKHIRDRDLIGMVDRITTLLVRGFTNDSQLQ
TLFNYLLQCGDTSRFTRFIQEIAERSPLQKERLMTIAERLRQEGHQIGWQEGKLEGLQEGMHEQAIKIAL
RMLEQGFDRDQVLAATQLSEADLAANNH
>gnl|CDD|182168 PRK09958, PRK09958, acid-sensing system DNA-binding response regulator EvgA
MNAIIIDDHPLAIAAIRNLLIKNDIEILAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKR
QYSGIIIIVSAKNDHFYGKHCADAGANGFVSKKEGMNNIIAAIEAAKNGYCYFPFSLNRFVGSLTSDQQK
LDSLSKQEISVMRYILDGKDNNDIAEKMFISNKTVSTYKSRLMEKLECKSLMDLYTFAQRNKIG
>gnl|CDD|182169 PRK09959, PRK09959, acid-sensing system histidine kinase EvgS
MKFLPYIFLLCCGLWSTISFADEDYIEYRGISSNNRVTLDPLRLSNKELRWLASKKNLVIAVHKSQTATL
LHTDSQQRVRGINADYLNLLKRALNIKLTLREYADHQKAMDALEEGEVDIVLSHLVASPPLNDDIAATKP
LIITFPALVTTLHDSMRPLTSSKPVNIARVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGQNDYFI
GSNIITSSMISRYFTHSLNVVKYYNSPRQYNFFLTRKESVILNEVLNRFVDALTNEVRYEVSQNWLDTGN
LAFLNKPLELTEHEKQWIKQHPDLKVLENPYSPPYSMTDENGSVRGVMGDILNIITLQTGLNFSPITVSH
NIHAGTQLNPGGWDIIPGAIYSEDRENNVLFAEAFITTPYVFVMQKAPDSEQTLKKGMKVAIPYYYELHS
QLKEMYPEVEWIKVDNASAAFHKVKEGELDALVATQLNSRYMIDHYYPNELYHFLIPGVPNASLSFAFPR
GEPELKDIINKALNAIPPSEVLRLTEKWIKMPNVTIDTWDLYSEQFYIVTTLSVLLVGSSLLWGFYLLRS
VRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEHYFTADYYKNAMLPLENSDSPFKD
VFSNAHEVTAETKENRTIYTQVFEIDNGIEKRCINHWHTLCNLPASDHAVYICGWQDITETRDLIHALEV
ERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILD
VDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNA
LKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKEL
IKNMQGDLSLESHPGIGTTFTITIPVEISQQVATVEAKAEQPITLPEKLSILIADDHPTNRLLLKRQLNL
LGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANEREKGLS
CGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHLDIEALKNNTANDLQLMQEILMTFQHETHKDLPAA
FHALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLEITPVSDDSKPEILQLLNSVKEHIAELDQEIA
VFCQKND
>gnl|CDD|182170 PRK09961, PRK09961, aminopeptidase
MDLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLNESTGPKVMICAHMDEVGFMV
RSISREGAIDVLPVGNVRMAARQLQPVRITTREECKIPGLLNGDRQGNDVSAMRVDIGARSYDEVMQAGI
RPGDRVTFDTTFQVLPHQRVMGKAFDDRLGCYLLVTLLRELHDAELPAEVWLVASSSEEVGLRGGQTATR
AVSPDVAIVLDTACWAKNFDYGAANHRQIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGIPLQADMFSN
GGTDGGAVHLTGTGVPTVVMGPATRHGHCAASIADCRDILQMIQLLSALIQRLTRETVVQLTDF
>gnl|CDD|170182 PRK09965, PRK09965, 3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
MNRIYACPVADLPEGEALRVDTSPVIALFNVGGEFYAIDDRCSHGNASLSEGYLEDDATVECPLHAASFC
LRTGKALCLPATDPLRTYPVHVEGGDIFIDLPEAQP
>gnl|CDD|182171 PRK09966, PRK09966, diguanylate cyclase DgcN
MDNDNSLNKRPTFKRALRNISMTSIFITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFA
DGPAATETLAALGQQGQFSTAEVRDKQQNILASWHYTRKDPGDTFSNFISHWLFPAPIIQPIRHNGETIG
EVRLTARDSSISHFIWFSLAVLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSE
ERIAEFHRFALDFNSLLDEMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSA
LLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSAL
TQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKHQRAEKLVR
>gnl|CDD|182172 PRK09967, PRK09967, OmpA family protein
MIKHLVAPLIFTSLILTGCQSPQGKFTPEQVAAMQSYGFTESAGDWSLGLSDAILFAKNDYKLLPESQQQ
IQTMAAKLASTGLTHARMDGHTDNYGEDSYNEGLSLKRANVVADAWAMGGQIPRSNLTTQGLGKKYPIAS
NKTAQGRAENRRVAVVITTP
>gnl|CDD|182173 PRK09968, PRK09968, protein-serine/threonine phosphatase
MPSTRYQKINAHHYRHIWVVGDIHGEYQLLQSRLHQLSFCPETDLLISVGDNIDRGPESLNVLRLLNQPW
FISVKGNHEAMALDAFETGDGNMWLASGGDWFFDLNDSEQQEATDLLLKFHHLPHIIEITNDNIKYVIAH
ADYPGDEYDFGKEIAESELLWPVDRVQKSLNGELQQINGADYFIFGHMMFDNIQTFANQIYIDTGSPKSG
RLSFYKIK
>gnl|CDD|236637 PRK09970, PRK09970, xanthine dehydrogenase subunit XdhA; Provisional
MAIGKSIMRVDAIAKVTGRAKYTDDYVMAGMLYAKYVRSPIAHGKVKSIDTEEARSLPGVEAVFTWEDVP
DIPFPTAGHPWSLDPNHRDIADRALLTRHVRHHGDAVAAVVARDELTAEKALKLIKVEYEELPVITDPEA
ALAEGAPPIHNGRGNLLKQSTMSTGNVQQTIKAADYQVQGHYETPIVQHCHMENVTSYAYMEDDGRITIV
SSTQIPHIVRRVVGQALGIPWGKVRVIKPYVGGGFGNKQDVLEEPLAAFLTSKVGGRPVKVSLSREECFL
ATRTRHAFTIDIKMGVNRDGTLKGYSLDVLSNTGAYASHGHSIASAGGNKVAYLYPRCAYKYSSKTVYTN
LPSAGAMRGYGAPQVVFAVESMLDDAATALGIDPVEFRLRNAAREGDANPLSGKRIYSAGLPECLEKGRK
IFEWDKRRAECKNQQGNLRRGVGVACFSYTSGTWPVGLEIAGARLLMNQDGTVQVQSGATEIGQGSDTVF
SQMVAETVGIPVSDVRVISTQDTDVTPFDPGAYASRQSYVAGPAIRKAALELKEKILAHAAVMLHQSAMN
LDIIDGHIVVKRPGEPLMSLEELAMDAYYHPERGGQITAESSIKTTTNPPAFGCTFVDVEVDIALCKVTI
NRILNVHDSGHILNPLLAEGQVHGGMGMGIGWALFEEMIIDEKTGVVRNPNLLDYKLPTMMDLPQLESAF
VEIYEPQSAYGHKSLGEPPIISPAPAIRNAVLMATGVAINTLPMTPQRLFEEFKEAGLI
>gnl|CDD|182175 PRK09971, PRK09971, xanthine dehydrogenase subunit XdhB; Provisional
MFDIAEYHEAATLEEAIELLADNPQAKLIAGGTDVLIQLHHHNDRYRHLVSIHNIAELRGITLAEDGSIR
IGAATTFTQIIEDPIIQKHLPALAEAAVSIGGPQIRNVATIGGNICNGATSADSAPPLFALDAKLEIHSP
NGVRFVPINGFYTGPGKVSLEHDEILVAFIIPPEPYEHAGGAYIKYAMRDAMDIATIGCAVLCRLDNGNF
EDLRLAFGVAAPTPIRCQHAEQTAKGAPLNLETLEAIGELVLQDVAPRSSWRASKEFRLHLIQELTKRVI
KEAVAAAGGKL
>gnl|CDD|170188 PRK09973, PRK09973, lipoprotein YqhH
MKTIFTVGAVVLATCLLSGCVNEQKVNQLASNVQTLNAKIARLEQDMKALRPQIYAAKSEANRANTRLDA
QDYFDCLRCLRMYAE
>gnl|CDD|236638 PRK09974, PRK09974, type II toxin-antitoxin system PrlF family antitoxin
NARMAAVLETESKLTDRGQTTVPAPVRKALKLKKRDSIHYEILPGGQVFICRLGDEEEDPVLGAFLDFLA
ADIQNNPQRIRPFDKSLIQRGKKLVAGVDVDLDAPLSDDDE
>gnl|CDD|182177 PRK09975, PRK09975, DNA-binding transcriptional regulator EnvR; Provisional
MAKKTKAEALKTRQELIETAIAQFALRGVSNTTLNDIADAANVTRGAIYWHFENKTQLFNEMWLQQPPLR
ELIQEHLTAGLEHDPLQQLREKFIAGLQYIAKIPRQQALLQILYHKCEFNDEMLSEGVIREKMGFNPQTL
REVLQRCQQQGCIANNLDLDVVLIILHGAFSGIVKNWLMNPAGYDLYKQAPALVDNVLRMLMPDENITKL
IHQ
>gnl|CDD|182178 PRK09977, PRK09977, MgtC/SapB family protein
MTAEFILRIILAGILGGLIGLERQMRGKGAGLRTHVLIGMGSALFMIVSKYGFADVLSLDHVGLDPSRIA
AQVVTGVGFIGAGNILVRNQNIKGLTTAADIWVTAAIGMVIGSGMYELGIYGSVMTLLVLEVFHQLTFRL
MNKHYHLQLTLVNGNVVSMLDWFKQQKIKTDLVSLQENEDHEVVAIDITLHATTSIEDLYRLLKGIAGVK
GVSIS
>gnl|CDD|137624 PRK09978, PRK09978, DNA-binding transcriptional regulator GadX; Provisional
MQSLHGNCLIAYARHKYILTMVNGEYRYFNGGDLVFADASQIRVDKCVENFVLVSRDTLSLFLPMLKEEA
LNLHAHKKVSSLLVHHCSRDIPVFQEVAQLSQNKNLRYAEMLRKRALIFALLSVFLEDEHFIPLLLNVLQ
PNMRTRVCTVINNNIAHEWTLARIASELLMSPSLLKKKLREEETSYSQLLTECRMQRALQLIVIHGFSIK
RVAVSCGYHSVSYFIYVFRNYYGMTPTEYQERSAQGLPNRDSAASIVAQGNFYGTDRSAEGIRL
>gnl|CDD|77522 PRK09979, PRK09979, rho operon leader peptide rhoL
MRSEQISGSSLNPSCRFSSAYSPVTRQRKDMSR
>gnl|CDD|182179 PRK09980, ompL, porin OmpL
MKKLNTIVLLSSLTSASVFAGAYVENREAYNLASDQGEVMLRVGYNFDMGAGIMLTNTYTFQRDDELKHG
YNEIEGWYPLFKPTDKLTIQPGGLINDKSIGSGGAVYLDVNYKFTPWFNLTVRNRYNHNNYSSTDLNGEL
DNNDSYEIGNYWNFIITDKFSYTFEPHYFYNVNDFNSSNGTKHHWEITNTFRYRINEHWLPYFELRWLDR
NVNPYHREQNQIRIGTKYFF
>gnl|CDD|182180 PRK09981, PRK09981, DUF406 domain-containing protein
MKDVVDKCSTKGCAIDIGTVIDNDNCTSKFSRFFATREEAESFMTKLKELAAAASSADEGASVAYKIKDL
EGQVELDAAFTFSCQAEMIIFELSLRSLA
>gnl|CDD|137627 PRK09982, PRK09982, universal stress protein UspD; Provisional
MAYKHIGVAISGNEEDALLVNKALELARHNDAHLTLIHIDDGLSELYPGIYFPATEDILQLLKNKSDNKL
YKLTKNIQWPKTKLRIERGEMPETLLEIMQKEQCDLLVCGHHHSFINRLMPAYRGMINKMSADLLIVPFI
DK
>gnl|CDD|182181 PRK09983, pflD, putative formate acetyltransferase 2; Provisional
MTNRISRLKTALFANTREISLERALLYTASHRQTEGEPVILRRAKATAYILEHVEISIRDEELIAGNRTV
KPRAGIMSPEMDPYWLLKELDQFPTRPQDRFAISEEDKRIYREELFPYWEKRSMKDFINGQMTDEVKAAT
STQIFSINQTDKGQGHIIIDYPRLLNHGLGELVAQMQQHCQQQPENHFYQAALLLLEASQKHILRYAELA
ETMAANCTDAQRREELLTIAEISRHNAQHKPQTFWQACQLFWYMNIILQYESNASSLSLGRFDQYMLPFY
QASLTQGEDPAFLKELLESLWVKCNDIVLLRSTSSARYFAGFPTGYTALLGGLTENGRSAVNVLSFLCLD
AYQSVQLPQPNLGVRTNALIDTPFLMKTAETIRLGTGIPQIFNDEVVVPAFLNRGVSLEDARDYSVVGCV
ELSIPGRTYGLHDIAMFNLLKVMEICLHENEGNAALTYEGLLEQIRAKISHYITLMVEGSNICDIGHRDW
APVPLLSSFISDCLEKGRDITDGGARYNFSGVQGIGIANLSDSLHALKGMVFDQQRLSFDELLSVLKANF
ATPEGEKVRARLINRFEKYGNDIDEVDNISAELLRHYCKEVEKYQNPRGGYFTPGSYTVSAHVPLGSVVG
ATPDGRFAGEQLADGGLSPMLGQDAQGPTAVLKSVSKLDNTLLSNGTLLNVKFTPATLEGEAGLRKLADF
LRAFTQLKLQHIQFNVVNADTLREAQQRPQDYAGLVVRVAGYSAFFVELSKEIQDDIIRRTAHQL
>gnl|CDD|182182 PRK09984, PRK09984, phosphonate ABC transporter ATP-binding protein
MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRT
VQREGRLARDIRKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRV
GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTL
HQVDYALRYCERIVALRQGHVFYDGSSQQFDNERFDHLYRSINRVEENAKAA
>gnl|CDD|182183 PRK09986, PRK09986, LysR family transcriptional regulator
MERLYRIDLKLLRYFLAVAEELHFGRAAARLNISQPPLSIHIKELEDQLGTPLFIRHSRSVVLTHAGKIL
MEESRRLLDNAEQSLARVEQIGRGEAGRIEIGIVGTALWGRLRPAMRHFLKENPNVEWLLRELSPSMQMA
ALERRELDAGIWRMADLEPNPGFTSRRLHESAFAVAVPEEHPLASRSSVPLKALRNEYFITLPFVHSDWG
KFLQRVCQQAGFSPQIIRQVNEPQTVLAMVSMGIGITLLPDSYAQIPWPGVVFRPLKERIPADLYAVYHP
DQVTPALNKLLAAL
>gnl|CDD|182184 PRK09987, PRK09987, dTDP-4-dehydrorhamnose reductase; Provisional
MNILLFGKTGQVGWELQRALAPLGNLIALDVHSTDYCGDFSNPEGVAETVRKIRPDVIVNAAAHTAVDKA
ESEPEFAQLLNATSVEAIAKAANEVGAWVVHYSTDYVFPGTGDIPWQETDATAPLNVYGETKLAGEKALQ
EHCAKHLIFRTSWVYAGKGNNFAKTMLRLAKEREELSVINDQFGAPTGAELLADCTAHAIRVALNKPEVA
GLYHLVASGTTTWHDYAALVFEEARKAGITLALNKLNAVPTSAYPTPARRPHNSRLNTEKFQQNFALVLP
DWQVGVKRMLTELFTTTAI
>gnl|CDD|182185 PRK09989, PRK09989, HPr family phosphocarrier protein
MPRFAANLSMMFTEVPFIERFAAARKAGFDAVEFLFPYDYSTLQIQKQLEQNHLTLALFNTAPGDINAGE
WGLSALPGREHEARADIDLALEYALALNCEQVHVMAGVVPAGEDAERYRAVFIDNLRYAADRFAPHGKRI
LVEALSPGVKPHYLFSSQYQALAIVEEVARDNVFIQLDTFHAQKVDGNLTHLIRDYAGKYAHVQIAGLPD
RHEPDDGEINYPWLFRLFDEVGYQGWIGCEYKPRGLTEEGLGWFDAWR
>gnl|CDD|182186 PRK09990, PRK09990, DNA-binding transcriptional regulator GlcC; Provisional
MKDERRPIADVVAERIERLIVDGVLKVGQALPSERRLCEKLGFSRSALREGLTVLRGRGIIETAQGRGSF
VARLNRVQDASPLMHLFSSQPRTLYDLLEVRALLEGESARLAALRGTQADFVLITRRYEEMLAAHENNKE
IDPIEHARLDHAFHLAICEASHNPVLVHTLQSLTDLMLSSVFASVNNLYHRPQQKKQIDRQHARLYNAVL
QRLPEQAQRAARDHIRTVRDNLREIEQEEQRLVRATLRLEG
>gnl|CDD|182187 PRK09993, PRK09993, C-lysozyme inhibitor; Provisional
SSGGMMFKALTTVAALVIATSAMAQDDLTISSLAKGETTKAAFNQMVQGHKLPAWVMKGGTYSPAQTVTL
GDETYQVMSACKPHDCGSQRIAVLWSEKSNQMTGVFSTIDEKTSQEKLTWLNVNDALSIDGKTVLFAALT
GSLENHPDGFNFK
>gnl|CDD|182188 PRK09997, PRK09997, hydroxypyruvate isomerase; Provisional
MLRFSANLSMLFGEYDFLARFEKAAQCGFRGVEFMFPYDYDIEELKQVLASNKLEHTLHNLPAGDWAAGE
RGIACIPGREEEFRDGVAAAIRYARALGNKKINCLVGKTPAGFSSEQIHATLVENLRYAANMLMKEDILL
LIEPINHFDIPGFHLTGTRQALKLIDDVGCCNLKIQYDIYHMQRMEGELTNTMTQWADKIGHLQIADNPH
RGEPGTGEINYDYLFKVIENSDYNGWVGCEYKPQTTTEAGLRWMDPYR
>gnl|CDD|182189 PRK10001, PRK10001, serine-type D-Ala-D-Ala carboxypeptidase
MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKI
MTSYVVGQALKADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIAL
ADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEF
TFNKIRQPNRNRLLWSSNLNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTW
GFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQV
VGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKFHQWFGSWFS
>gnl|CDD|236639 PRK10002, PRK10002, porin OmpF
MMKRNILAVIVPALLVAGTANAAEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGE
TQINSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVYDALGYTDMLPEF
GGDTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIV
GAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGFANKTQDVL
LVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGATYYFNKNMSTYVDYIINQIDSDNKLGVGS
DDTVAVGIVYQF
>gnl|CDD|236640 PRK10003, PRK10003, ferric-rhodotorulic acid outer membrane transporter; Provisional
LSTQFNRDNQYQAIAKPSLLAGCIALALLPSAAFAAPATEDTVIVEGSATAPVDDGEQDYSVKTTSAGTK
MQMTQRDIPQSVSIVSQQRMEDQQLQTLGEVMENTLGISKSQADSDRALYYSRGFQIDNYMVDGIPTYFE
SRWNLGDALSDTALFERVEVVRGATGLMTGTGNPSAAINMVRKHATSREFKGDVSAEYGSWNKQRYVADL
QSPLTEDGKVRARIVAGYQNNDSWLDRYNSEKTFFSGIVDADLGDLTTLSAGYEYQRIDVNSPTWGGLPR
WNTDGSSNSYDRARSTAPDWAYNDKEINKVFMTLKQRFADTWQATLNATHSEVEFDSKMMYVDAYVDKAT
GMLVGPYSNYGPGFDYVGGTGWNSGKRKVDALDLFADGSYELFGRQHNLMFGGSYSKQNNRYFSSWANIF
PDEIGSFYNFNGNFPQTDWSPQSLAQDDTTHMKSLYAATRVSLADPLHLILGARYTNWRVDTLTYSMEKN
HTTPYAGLVYDINDNWSTYASYTSIFQPQNDRDSSGKYLAPITGNNYELGLKSDWMNSRLTTTLAIFRIE
QDNVAQSTGTPIPGSNGETAYKAVDGTVSKGVEFELNGAITDNWQLTFGATRYIAEDNEGNAVNPNLPRT
TVKLFTRYRLPVMPELTVGGGVNWQNRVYTDTVTPYGTFRAEQGSYALVDLFTRYQVTKNFSVQGNVNNL
FDKTYDTNVEGSIVYGAPRNFSITATYQF
>gnl|CDD|182192 PRK10005, PRK10005, dihydroxyacetone kinase ADP-binding subunit DhaL
MSLSRTQIVNWLTRCGDIFTEESDYLTGLDREIGDADHGLNMNRGFSKVVEKLPAIADKDIGFILKNTGM
TLLSSVGGASGPLYGTFFIRAAQATQARQSLTLEELYQMFRDGADGVISRGKAEPGDKTMCDVWVPVVES
LRQSSEQNLSVPAALNAAVSIAESAAQSTITMQARKGRASYLGERSIGHQDPGATSVMFMMQALALAAKE
>gnl|CDD|182193 PRK10014, PRK10014, DNA-binding transcriptional repressor MalI; Provisional
MATAKKITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLI
VRDLSAPFYAELTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDLREMA
EEKGIPVVFASRASYLDDVDTVRPDNMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLK
FGLPFHSEWVLECTSSQKQAAEAITALLRHNPTISAVVCYNETIAMGAWFGLLRAGRQSGESGVDRYFEQ
QVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRMMQRITHEETHSRNLIIPPRLIARK
>gnl|CDD|182194 PRK10015, PRK10015, oxidoreductase; Provisional
MSDDKFDAIVVGAGVAGSVAALVMARAGLDVLVIERGDSAGCKNMTGGRLYAHTLEAIIPGFAASAPVER
KVTREKISFLTEESAVTLDFHREQPDVPQHASYTVLRNRLDPWLMEQAEQAGAQFIPGVRVDALVREGNK
VTGVQAGDDILEANVVILADGVNSMLGRSLGMVPASDPHHYAVGVKEVIGLTPEQINDRFNITGEEGAAW
LFAGSPSDGLMGGGFLYTNKDSISLGLVCGLGDIAHAQKSVPQMLEDFKQHPAIRPLISGGKLLEYSAHM
VPEGGLAMVPQLVNDGVMIVGDAAGFCLNLGFTVRGMDLAIASAQAAATTVIAAKERADFSASSLAQYKR
ELEQSCVMRDMQHFRKIPALMENPRLFSQYPRMVADIMNDMFTIDGKPNQPVRKMIMGHAKKIGLINLLK
DGIKGATAL
>gnl|CDD|182195 PRK10016, PRK10016, DNA gyrase inhibitor SbmC
MNYEIKQEQKRTIAGFHLVGPWEQTVKQGFEQLMMWVDSHNIVPKEWVAVYYDNPDEVPAEKLRCDTVVT
VPDDFVLPENSEGVILTEIPGGQYAVAVARVVDDDFAKPWYQFFNSLLQDSAYQMAPKPCFEVYLNDGAE
DGYWDIEMYVPVQKKH
>gnl|CDD|182196 PRK10017, PRK10017, colanic acid biosynthesis protein; Provisional
MKLLILGNHTCGNRGDSAILRGLLDAINILNPHAEVDVMSRYPVSSSWLLNRPVMGDPLFLQMKQHNSAA
GVVGRVKKVLRRRYQHQVLLSRVTDTGKLRNIAIAQGFTDFVRLLSGYDAIIQVGGSFFVDLYGVPQFEH
ALCAFMAKKPLYMIGHSVGPFQDEQFNQLANYVFGHCDALILRESVSLDLMKRSNITTAKVEHGVDTAWL
VDHHTEDFTASYAVQHWLDVAAQQKTVAITLRELAPFDKRLGTTQQAYEKAFAGVVNRIIDEGYQVIALS
TCTGIDSYNKDDRMVALNLRQHVSDPARYHVVMDELNDLEMGKILGACELTVGTRLHSAIISMNFGTPAI
AINYEHKSAGIMQQLGLPEMAIDIRHLLDGSLQAMVADTLGQLPALNARLAEAVSRERQTGMQMVQSVLE
RIGEVK
>gnl|CDD|182197 PRK10018, PRK10018, colanic acid biosynthesis glycosyltransferase WcaA
MKDNPLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCSTSWEQLQQYVTALNDPRITYIHNDIN
SGACAVRNQAIMLAQGEYITGIDDDDEWTPNRLSVFLAHKQQLVTHAFLYANDYVCQGEVYSQPASLPLY
PKSPYSRRLFYKRNIIGNQVFTWAWRFKECLFDTELKAAQDYDIFLRMVVEYGEPWKVEEATQILHINHG
EMQITSSPKKFSGYFHFYRKHKDKFDRASKKYQLFTLYQIRNKRMTWRTLLTLLSVRNGKRLADGIRGR
>gnl|CDD|236641 PRK10019, PRK10019, nickel/cobalt efflux transporter RcnA
MTEFTTLLQQGNAWFFIPSAILLGALHGLEPGHSKTMMAAFIIAIKGTIKQAVMLGLAATISHTAVVWLI
AFGGMYLSRRFTAQSAEPWLQLISAVIIISTAFWMFWRTWRGERNWLENMHHHDHDHDHDHDHEHHHDHG
HHHHHEHGATAEEYQDAHERAHANDIKRRFDGREVTNGQILLFGLTGGLIPCPAAITVLLICIQLKALTL
GATLVLSFSIGLALTLVTVGVGAAISVQQAAKRWSGFNTLARRAPYFSSLLIGLVGVYMGVHGFMGIMR
>gnl|CDD|182199 PRK10022, PRK10022, putative DNA-binding transcriptional regulator; Provisional
TLTEDDVLEQLDAQDNLFSFMKTAHSILLQGIRQFLPSLFVDNDEEIVEYAVKPLLAQSGPLDDIDVALR
LIYALGKMDKWLYADITHFSQFWHYLNEQDETPGFADDMTWDFISNVNSITRNATLYDALKAMKFADFAV
WSEARFSGMVKTALTLAVTTTLKELTP
>gnl|CDD|182200 PRK10026, PRK10026, arsenate reductase (glutaredoxin)
MSNITIYHNPACGTSRNTLEMIRNSGTEPTIIHYLETPPTRDELVKLIADMGISVRALLRKNVEPYEELG
LAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLEILPDAQKGAFTKEDGEKVVDEAGKRL
K
>gnl|CDD|182201 PRK10027, PRK10027, cryptic adenine deaminase; Provisional
MNNSINHKFHHISRAEYQELLAVSRGDAVADYIIDNVSILDLINGGEISGPIVIKGRYIAGVGAEYADAP
ALQRIDARGATAVPGFIDAHLHIESSMMTPVTFETATLPRGLTTVICDPHEIVNVMGEAGFAWFARCAEQ
ARQNQYLQVSSCVPALEGCDVNGASFTLEQMLAWRDHPQVTGLAEMMDYPGVISGQNALLDKLDAFRHLT
LDGHCPGLGGKELNAYIAAGIENCHESYQLEEGRRKLQLGMSLMIREGSAARNLNALAPLINEFNSPQCM
LCTDDRNPWEIAHEGHIDALIRRLIEQHNVPLHVAYRVASWSTARHFGLNHLGLLAPGKQADIVLLSDAR
KVTVQQVLVKGEPIDAQTLQAEESARLAQSAPPYGNTIARQPVSASDFALQFTPGKRYRVIDVIHNELIT
HSRSSVYSENGFDRDDVCFIAVLERYGQRLAPACGLLGGFGLNEGALAATVSHDSHNIVVIGRSAEEMAL
AVNQVIQDGGGLCVVRNGQVQSHLPLPIAGLMSTDTAQSLAEQIDALKAAARECGPLPDEPFIQMAFLSL
PVIPALKLTSQGLFDGEKFAFTTLEVTE
>gnl|CDD|236642 PRK10030, PRK10030, YiiX family permuted papain-like enzyme
MKIRLLILSLLVSVPAFAWQPQTGDIIFQISRSSQSKAIQLATHSDYSHTGMIVKRNKKPYVFEAVGPVK
YTPLKQWIAHGEKGKYVVRRLENGLSVEQQQKLAQTAKRYLGKPYDFYFSWSDDRIYCSELVWKVYQNAL
GMEVGEQQKLKEFDLSNPLVQAKLKERYGKNIPLEETVVSPQAVFDSPQLTTVAKEW
>gnl|CDD|182203 PRK10034, PRK10034, gluconate transporter GntP
MHVLNILWVVFGIGLMLVLNLKFKINSMVALLVAALSVGMLAGMDLMKLLHTMKAGFGNTLGELAIIVVF
GAVIGKLMVDSGAAHQIAHTLLARLGLRYVQLSVIIIGLIFGLAMFYEVAFIMLAPLVIVIAAEAKIPFL
KLAIPAVAAATTAHSLFPPQPGPVALVNAYGADMGMVYIYGVLVTIPSVICAGLILPKFLGNLERPTPSF
LKADQPVDMNNLPSFGTSILVPLIPAIIMISTTIANIWLVKGTPAWEVVNFIGSSPIAMFIAMVVAFVLF
GTARGHDMQWVMNAFESAVKSIAMVILIIGAGGVLKQTIIDTGIGDTIGMLMSHGNISPYIMAWLITVLI
RLATGQGVVSAMTAAGIISAAILDPATGQLVGVNPALLVLATAAGSNTLTHINDASFWLFKGYFDLSVKD
TLKTWGLLELVNSVVGLIIVLIISMVA
>gnl|CDD|182204 PRK10037, PRK10037, cellulose biosynthesis protein BcsQ
MAILGLQGVRGGVGTTSITAALAWSLQMLGENVLVIDACPDNLLRLSFNVDFTHRQGWARALLDGQDWRD
AGLRYTSQLDLLPFGQLSIEEQENPQHWQTRLGDICSALQQLKASGRYQWILLDLPRGASPLTRQLLSLC
DHSLAIVNVDANCHIRLHQQALPAGAHILINDLRIGSQLQDDLYQLWLQSQRRLLPMLIHRDEAMAECLA
AKQPLGEYRSDSLAAEEILTLANWCLLHYSGLKTPVGSAS
>gnl|CDD|170217 PRK10039, PRK10039, hypothetical protein; Provisional
MSVLYIQIRKNQITVRNLESKKEVSGDAPFSTERLLIGQFFPAEKVLQDLVRQVHPRSTWHLFLRAKRTH
IIIHALEMNEGGLSQVEERILIELAVGSTPKGYRQLYIHPQSVPLSDSAVIQIIKQK
>gnl|CDD|182205 PRK10040, PRK10040, hypothetical protein; Provisional
ALILFLGTLVSFYADAGNKPCSGKKGGISHCTGGKFVCNDGSISASKKTCTN
>gnl|CDD|236643 PRK10044, PRK10044, ferrichrome outer membrane transporter; Provisional
MARSKTAQPNHSLRKIAVVVATAVSGMSVYAQAAVEPKEETITVTAAPAPQESAWGPAATIAAKRSATGT
KTDTPIEKTPQSISVVTAEEMALHQPKSVKEALSYTPGVSVGTRGASNTYDHLIIRGFAASGQSQNNYLD
GLKLQGNFYNDAVIDPYMLERAELMRGPVSVLYGKSNPGGLLNMVSKRPTTEPLKEVQFKMGTDNLFQTG
FDFSDALDDDGVYSYRLTGLARSANAQQKGSEEQRYAIAPSFTWRPDDKTNFTFLSYFQNEPETGYYGWL
PKEGTVEPLPNGKRLPTDFNEGAKNNTYSRNEKMVGYSFDHEFNDTFTVRQNLRYAENKTSQRSVYGYGV
CSDKGHYLNRGYVVDDEKLQNFSVDTQLQSKFATGDVDHTLLTGVDFMRMRNDINAWFGYADSVPLLNLY
GPVNTDFDFNANSGPYQILNKQKQTGLYVQDQAEWDKWLVTLGGRYDWADQSSLNRVNGTTDKRDDKQFT
WRGGVNYLFDNGITPYFSYSESFEPSSGTGKDGNIFAPSKGKQYEAGVKYVPKDRPIVVTGAVYQLTKTN
NLTADPENSFFSVQGGEIRARGVELEAKAALSANVNVTGSYTYTDAEYTTDTTYKGNTPAQVPKHMASLW
ADYTFFDGPLSGLTLGTGGRYTGSSYGDPANSFKVGSYTVVDALVKYDLARFGMAGSSVALNVNNLFDRE
YVASCFNTYGCFWGAERQVVATATFRF
>gnl|CDD|182207 PRK10045, PRK10045, ACP phosphodiesterase
MNFLAHLHLAHLADSSLSGNLLADFVRGNPEESFPPDVVAGIYMHRRIDVLTDNLPEVREAREWFRSETR
RVAPITLDVMWDHFLSRHWSQLSPDFPLQEFVCYAREQVMTILPDSPPRFVNLNNYLWSEQWLERYRDMD
FIQNVLNGMASRRPRLDALRDSWYDLDAHYDALETRFWQFYPRMMAQASRKAL
>gnl|CDD|182208 PRK10046, dpiA, two-component response regulator DpiA; Provisional
MTAPLTLLIVEDETPLAEMHAEYIRHIPGFSQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLH
ELVQAHYPGDVVFTTAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQRKHMLESIDSASQKQID
EMFNAYARGEPKDELPTGIDPLTLNAVRKLFKEPGVQHTAETVAQALTISRTTARRYLEYCASRHLIIAE
IVHGKVGRPQRIYHS
>gnl|CDD|236644 PRK10049, pgaA, outer membrane protein PgaA; Provisional
ALSWLRQALKSALSNNQIADWLQIALWAGQDAEVITVYNRYRVHMQLPARGYAAVAVAYRNLKQWQNSLT
LWQKALSLEPQNDDYQRGLILTLADAGQYDEALVKAKQLVSGAPDKANLLALAYVYKRAGRHWDELRAMT
QALPRAPQTQQYPTEYVQALRNNRLSAPALGAIDDANLTPAEKRDLEADAAAELVRLSFMPTRSEKERYA
IADRALAQYDALEALWHDNPDATADYQRARIDRLGALLARDRYKDVISEYQRLKAEGQIIPPWAQRWVAS
AYLKLHQPEKAQSILTELFYHPETIADLSDEELADLFYSLLESENYPGALTVTAHTINNSPPFLRLYGSP
TSIPNDDWLQGQSLLSQVAKYSNDLPQAEMRARELAYNAPGNQGLRIDYASVLQARGWPRAAENELKKAE
VLEPRNINLEVEQAWTALDLQEWRQMDVLTDDVVAREPQDPGVQRLARARDVHHMAELRIAGSTGLDSDG
PDSGKHDVDITTILYSPPLADNWRGFAGFGYADGQFSEGKGIVRDWLAGVEWRSRDIWLEAELSERVFGH
EHKPGARLSGWYDFNDNWRIGGSLERLSHRTPLRALKNGVTANGGQGYVRWYQNERREYGVSWAFSDFSD
GNRRQEYSLSGQERLWSSPYLIVDFLPSLYYSQNSEHDTPYYNPIKDFDVLPALEADHLLYRRYETSWSQ
QFSAGVGAYWQKHYGTGAITQLGYGQRISWNDVIDAGATLRWDKRPYDGDREHNLYVEFDLTFRF
>gnl|CDD|182210 PRK10050, PRK10050, curli production assembly/transport protein CsgF
MRVKHAVVLLMLISPLSWAGTMTFQFRNPNFGGNPNNGAFLLNSAQAQNSYKDPSYNDDFGIETPSALDN
FTQAIQSQILGGLLSNINTGKPGRMVTNDYIVDIANRDGQLQLNVTDRKTGQTSTIQVSGLQNNSTDF
>gnl|CDD|182211 PRK10051, csgA, major curlin subunit CsgA
MKLLKVAAIAAIVVSGSALAGVVPQYGGGGNHGGGGNNSGPNSTLNIYQYGGGNSALALQSDARNSDLTI
TQHGGGNGADVGQGSDDSSIDLTQNGFGNSATLDQWNGKNSDMTVKQFGGGNGAAVDQTASNSSVNVTQV
GFGNNATAHQY
>gnl|CDD|182212 PRK10053, PRK10053, YdeI family stress tolerance OB fold protein
MKLQAIALASFLVMPYALADDQGGLKQDAAPPPPHAIEDGYRGTDDARKMTVEQAKTMHDGATVSLRGNL
IDHKGDDRYVFRDKSGEINVIIPAAVFDGREVQPDQMININGSLDKKSAPPVVRVTHLQK
>gnl|CDD|182213 PRK10054, PRK10054, efflux MFS transporter YdeE
MNLSLRRSTSALLASSLLLTIGRGATLPFMTIYLSRQYSLSVDLIGYAMTIALTIGVVFSLGFGILADKF
DKKRYMLLAITAFASGFIAIPLVNNVTLVVLFFALINCAYSVFSTVLKAWFADNLSSTSKTKIFSLNYTM
LNIGWTVGPPLGTLLVMQSINLPFWLAAICSAFPLVFIQIWVQRSEKAIATETGSVWSPSVLLQDKALLW
FTCSGFLASFVSGAFASCISQYVMVVADSDFAEKVVAVVLPVNAAMVVSLQYSVGRRLNAANIRPLMTAG
TLCFVIGLVGFIFSGNSLLLWGMSAAVFTVGEIIYAPGEYMLIDHIAPPGMKASYFSAQSLGWLGAAINP
LVSGVILTTLPPWSLFVILALAIVAAWLLMLKGMRARPWGQPALC
>gnl|CDD|182214 PRK10057, rpsV, stationary-phase-induced ribosome-associated protein
MKSNRQARHILGLDYKISNQRKVVTEGDKSSVVNNPTGRKRRAE
>gnl|CDD|236645 PRK10060, PRK10060, cyclic di-GMP phosphodiesterase
MKDVRESQTLYNFLGTHSPYWRLTEDSNALELSATEETETNVAVALSPEQAARIREMTVITSSLMLTLTL
DGEPLSVHLVGRKINKREWAGTASAWHDTPSVARDLSHGLSFAEQVVSEANSVIVILDSRGNIQRFNRLC
EEYTGLKEHDVIGQSVFKLFMSRREAAASRRNIRGFFRSGNAYEVERWIKTRKGQRLFLFRNKFVHSGSG
KNEIFLICSGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDNFKKV
NDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGLI
EVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALEND
QLVIHYQPKITWRGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKG
INLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLD
DFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTK
NGVNERQGFLFAKPMPAVAFERWYKRYLKRKLI
>gnl|CDD|182216 PRK10061, PRK10061, DNA damage-inducible protein YebG; Provisional
MAVEVKYVVIREGEEKMSFTSKKEADAYDKMLDTADLLDTWLTNSPVQMEDEQREALSLWLAEQKDVLST
ILKTGKLPSPQVVGAESEEEDASHAA
>gnl|CDD|182217 PRK10062, PRK10062, hypothetical protein; Provisional
MAGSSLLTLLDDIATLLDDISVMGKLAAKKTAGVLGDDLSLNAQQVSGVRANRELPVVWGVAKGSLINKV
ILVPLALIISAFIPWAITPLLMIGGAFLCFEGVEKVLHMLEARKHKEDPAQRQQRLEKLAAQDPLKFEKD
KVKGAIRTDFILSAEIVAITLGIVAEAPLLNQVLVLSGIALVVTVGVYGLVGVIVKIDDLGYWLAEKSSA
LAQALGKGLLIIAPWLMKALSIVGTLAMFLVGGGIVVHGIAPLHHAIEHFAGQQSAVVAMILPTVLNLVL
GFIIGGIVVLGVKAVAKMRGQAH
>gnl|CDD|236646 PRK10064, PRK10064, catecholate siderophore receptor CirA; Provisional
MFRLNPFVRVGLCASAISCAWPVLAVDDDGETMVVTASAVEQNLKDAPASISVITQEDLQRKPVQNLKDV
LKEVPGVQLTNEGDNRKGVSIRGLDSSYTLILIDGKRVNSRNAVFRHNDFDLNWIPVDAIERIEVVRGPM
SSLYGSDALGGVVNIITKKIGQKWHGTVTVDTTIQEHRDRGDTYNGQFFTSGPLIDGVLGMKAYGSLAKR
EKDDPQNSTTTDTGETPRIEGFTSRDGNVEFAWTPNQNHDFTAGYGFDRQDRDSDSLDKNRLERQNYSLS
HNGRWDYGNSELKYYGEKVENKNPGNSSPITSESNSIDGKYTLPLTAINQFLTFGGEWRHDKLSDAVNLT
GGTSSKTSASQYALFVEDEWRIFEPLALTTGVRMDDHETYGDHWSPRAYLVYNATDTVTVKGGWATAFKA
PSLLQLSPDWTSNSCRGACKIVGSPDLKPETSESWELGLYYMGEEGWLEGVESSVTVFRNDVDDRISISR
TSDVNAAPGYQNFVGFETNGRGRRVPVFRYYNVNKARIQGVETELKIPFNDEWKLSLNYTYNDGRDVSNG
ENKPLSDLPFHTANGTLDWKPLALEDWSFYVSGNYTGQKRADSATAKTPGGYTIWNTGAAWQVTKDVKLR
AGVLNLGDKDLSRDDYSYNEDGRRYFMAVDYRF
>gnl|CDD|236647 PRK10069, PRK10069, 3-phenylpropionate/cinnamic acid dioxygenase subunit beta
ATGGAASRRQRAQVSLELHHEISQFLYREARLLDEWRYDDWLALLAEDIHYTMPMRTTVNAQRRDRREGV
QTPPTMAWFDDNKDQLERRVARLETGMAWAEEPPSRLRHLITNVRVEETDIPDEFAVRSNFLLYRSRGER
DEDFLVGRREDVLRREGDGWRLARRRIVLDQAVLLAKNLSVFL
>gnl|CDD|182221 PRK10070, PRK10070, proline/glycine betaine ABC transporter ATP-binding protein ProV
MAIKLEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTM
VRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEE
RREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKL
QAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIA
RRTPNGLIRKTPGFGPRSALKLLQDEDREYGYVIERGNKFVGAVSIDSLKTALTQQQGLDAALIDAPLAV
DAQTPLSELLSHVGQAPCAVPVVDEDQQYVGIISKGMLLRALDREGVNNG
>gnl|CDD|182222 PRK10072, PRK10072, HTH-type transcriptional regulator
MEYKDPMFELLSSLEQIVFKDETQKITLTQKTTSFTEFEQLRKGTGLKIDDFARVLGVSVAMVKEWESRR
VKPSSAELKLMRLIQANPALSKQLME
>gnl|CDD|182223 PRK10073, PRK10073, putative glycosyl transferase; Provisional
MMNSTPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQAN
AGVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADWCFRDTGETWQSIPSDR
LRSTGVLSGPDWLRMALSSRRWTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQ
SLYKYYLHDTSVSRLPRQGNKNLNYQRHYIKITRMLEKLNRRYADKIKIYPAFHQQITKEALRVCHAVRK
EPDILTRQRMIAEIFTSGMYKRIWKNARSVKLGYQLLLWSFRLWQWRD
>gnl|CDD|182224 PRK10076, PRK10076, pyruvate formate lyase II activase; Provisional
LRDADECPSGAFERIGRDITLDALEREVMKDDIFFRTSGGGVTLSGGEVLMQAEFATRFLQRLRLWGVSC
AIETAGDAPASKLLPLAKLCDEVLFDLKIMDATQARDVVKMNLPRVLENLRLLVSEGVNVIPRLPLIPGF
TLSRENMQQALDVLIPLGIKQIHLLPFHQYGEPKYRLLGKTWSMKEVPAPSSADVATMREMAERAGFQVT
VGG
>gnl|CDD|182225 PRK10077, xylE, D-xylose transporter XylE; Provisional
MNTQYNSSYIFSITLVATLGGLLFGYDTAVISGTVESLNTVFVAPQNLSESAANSLLGFCVASALIGCII
GGALGGYCSNRFGRRDSLKIAAVLFFISALGSAWPEFGFTSIGPDNTGYVPEFVIYRIIGGIGVGLASML
SPMYIAEIAPAHIRGKLVSFNQFAIIFGQLVVYFVNYFIARSGDASWLNTDGWRYMFASEAIPALLFLML
LYFVPETPRYLMSRGKQEQAEGILRKIMGNTLATQALQEIKHSLDHGRKTGGKLLMFGVGVIVIGVMLSV
FQQFVGINVVLYYAPEIFKTLGASTDIALLQTIIVGVINLTFTVLAIMTVDKFGRKPLQIIGALGMAIGM
FSLGTAFYTQAPGIVALLSMLFYVAAFAMSWGPVCWVLLSEIFPNAIRGKALAIAVAAQWIANYFVSWTF
PMMDKNSWLVAHFHNGFSYWIYGCMGVLAALFMWKFVPETKGKTLEEMEALWEPETKKT
>gnl|CDD|236648 PRK10078, PRK10078, ribose 1,5-bisphosphokinase; Provisional
MGKLIWLMGPSGSGKDSLLAALRQREQTQLLVAHRYITRPASAGSENHIALSEQEFFTRAGQNLFALSWH
ANGLYYGVGIEIDLWLHAGFDVLVNGSRAHLPQARARYQSALLPVCLQVSPEILRQRLENRGRENASEIN
ARLARAARYQPQDCHTLNNDGSLRQSVDTLLTLLHLSQKEKHHACL
>gnl|CDD|182227 PRK10079, PRK10079, phosphonate metabolism transcriptional regulator PhnF; Provisional
MHLSRHPTSYPTRYQEIAAKLEQELRQHYRCGDYLPAEQQLAARYEVNRHTLRRAIDQLVEKGWVQRRQG
VGVLVLMRPYDYPLNAQARFSQNLLDQGSHPTSEKLLSVLRPASGHVADALGITEGENVIHLRTLRRVNG
VALCLIDHYFADLTWWPTLQRFDSGSLHDFLREQLGIALRRSQTRISARRAQAKESQLLEIPNMSPLLCV
RTLNHRDGESSPAEYSVSLTRADMIEFTMEH
>gnl|CDD|170240 PRK10081, PRK10081, lipoprotein toxin entericidin B
MVKKTIAAIFSVLVLSTVLTACNTTRGVGEDISDGGNAISGAATKAQQ
>gnl|CDD|182228 PRK10082, PRK10082, hypochlorite stress DNA-binding transcriptional regulator HypT
MDDCGAGLHNIETKWLYDFLTLEKCRNFSQAAVSRNVSQPAFSRRIRALEQAIGVELFNRQVTPLQLSEQ
GKIFHSQIRHLLQQLESNLAELRGGSDYAQRKIKIAAAHSLSLGLLPSIISQMPPLFTWAIEAIDVDEAV
DKLREGQSDCIFSFHDEDLLEAPFDHIRLFESQLFPVCASDEHGEALFNLAQPHFPLLNYSRNSYMGRLI
NRTLTRHSELSFSTFFVSSMSELLKQVALDGCGIAWLPEYAIQQEIRSGQLVVLNRDELVIPIQAYAYRM
NTRMNPVAERFWRELRELEIVLS
>gnl|CDD|182229 PRK10083, PRK10083, putative oxidoreductase; Provisional
MKSIVIEKPNSLAIEERPIPQPAAGEVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGE
GVDAARIGERVAVDPVISCGHCYPCSIGKPNVCTSLVVLGVHRDGGFSEYAVVPAKNAHRIPDAIADQYA
VMVEPFTIAANVTGRTGPTEQDVALIYGAGPVGLTIVQVLKGVYNVKAVIVADRIDERLALAKESGADWV
INNAQEPLGEALEEKGIKPTLIIDAACHPSILEEAVTLASPAARIVLMGFSSEPSEIVQQGITGKELSIF
SSRLNANKFPVVIDWLSKGLIDPEKLITHTFDFQHVADAIELFEKDQRHCCKVLLTFAE
>gnl|CDD|236649 PRK10084, PRK10084, dTDP-glucose 4,6 dehydratase; Provisional
MKILVTGGAGFIGSAVVRHIINNTQDSVVNVDKLTYAGNLESLADVSDSERYVFEHADICDRAELDRIFA
QHQPDAVMHLAAESHVDRSITGPAAFIETNIVGTYVLLEAARNYWSALDEDKKNAFRFHHISTDEVYGDL
PHPDEVENSEELPLFTETTAYAPSSPYSASKASSDHLVRAWLRTYGLPTIVTNCSNNYGPYHFPEKLIPL
VILNALEGKPLPIYGKGDQIRDWLYVEDHARALYKVVTEGKAGETYNIGGHNEKKNLDVVLTICDLLDEI
VPKATSYREQITYVADRPGHDRRYAIDASKISRELGWKPQETFESGIRKTVEWYLANTEWVQNVKSGAYQ
SW
>gnl|CDD|182231 PRK10086, PRK10086, DNA-binding transcriptional regulator DsdC
EPLREMRNRLLNGWQLSKLHTFEVAARHQSFALAADELSLTPSAVSHRINQLEEELGIKLFVRSHRKVEL
TEEGKRVFWALKSSLDTLNQEILDIKNQELSGTLTVYSRPSIAQCWLVPRLADFTRRYPSISLTILTGNE
NVNFQRAGIDLAIYFDDAPSAQLTHHFLMDEEILPVCSPEYAERHALTGNPDNLRHCTLLHDRQAWSNDS
GTDEWHSWAQHFGVNLLPPSSGIGFDRSDLAVIAAMNHIGVAMGRKRLVQKRLASGELVAPFGDMEVKCH
QHYYVTTLPGRQWPKIEAFIDWLKEQVKTTS
>gnl|CDD|182232 PRK10089, PRK10089, chaperone CsaA
METITYEDFEKVDIRVGTIVEAEPFPEARKPAYKLWIDFGEEIGVKQSSAQITPHYTPEELIGKQVVAVV
NFPPKQIAGFMSEVLVLGFEDEDGEVVLLTPDRPVPNGVKLV
>gnl|CDD|182233 PRK10090, PRK10090, aldehyde dehydrogenase A; Provisional
LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKR
ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGET
VGQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINS
GQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGARV
ALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLN
VAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYLQSD
>gnl|CDD|182234 PRK10091, PRK10091, MFS transport protein AraJ; Provisional
MKKVILSLALGTFGLGMAEFGIMGVLTELAHDVGISIPAAGHMISYYALGVVVGAPIIALFSSRYSLKHI
LLFLVALCVIGNAMFTLSSSYLMLAIGRLVSGFPHGAFFGVGAIVLSKIIKPGKVTAAVAGMVSGMTVAN
LLGIPLGTYLSQEFSWRYTFLLIAVFNIAVLASIYFWVPDIRDEAKGGLREQFHFLRSPAPWLIFAATMF
GNAGVFAWFSYIKPYMMFISGFSETSMTFIMMLVGLGMVLGNLLSGRLSGRYSPLRIAAVTDFIIVLALL
MLFFFGGMKTASLIFAFICCAGLFALSAPLQILLLQNAKGGELLGAAGGQIAFNLGSAIGAYCGGMMLTL
GLAYNYVALPAALLSFAAMSSLLLYGRYKRQQ
>gnl|CDD|182235 PRK10092, PRK10092, maltose O-acetyltransferase; Provisional
MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVTEAYIEPTFRCDY
GYNIFLGNNFYANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGG
RAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL
>gnl|CDD|182236 PRK10093, PRK10093, primosomal replication protein N''; Provisional
LLLEKLEGQLATLRQRCAPLAQHATLSARFDRHLFQTRSTLLQAYLDEAGDNLAALRHAVEQQQLPQVAW
LAEHLAAQLEAIAREAAAWSLREWDSAPPGLARWQRKRIQHQEFERRLLEMVAERRARLARATDLVEQQT
LHREVEAYEGRLARCRHALEKIENVLARLTR
>gnl|CDD|182237 PRK10094, PRK10094, HTH-type transcriptional activator AllS
MFDPETLRTFIAVAETGSFSKAAERLCKTTATISYRIKLLEENTGVALFFRTTRSVTLTAAGEHLLSQAR
DWLSWLESMPSELQQVNDGVERQVNIVINNLLYNPQAVAQLLAWLNERYPFTQFHISRQIYMGVWDSLLY
EGFSLAIGVTGTEALANTFSLDPLGSVQWRFVMAADHPLANVEEPLTEAQLRRFPAVNIEDSARTLTKRV
AWRLPGQKEIIVPDMETKIAAHLAGVGIGFLPKSLCQSMIDNQQLVSRVIPTMRPPSPLSLAWRKFGSGK
AVEDIVTLFTQRRPEISGFLEIFGNPRS
>gnl|CDD|236650 PRK10095, PRK10095, ribonuclease I; Provisional
MKAFWRNAALLAVSLLPFSSANAVALQAKQYGDFDRYVLALSWQTGFCQSQHDRNRNEPDECRLQKETTN
KADFLTVHGLWPGLPKSVAARGVDERRWMRFGCATRPIPNLPEARASRKCSAPETGLSLETAAKLSEVMP
GAGGRSCLERYEYAKHGACFGFDPDAYFGTMVRLNQEIKESEAGKFLADNYGKTVSRRDFDAAFAKSWGK
ENVKAVKLTCQGNPAYLTEIQISLKADAINAPLSANSFLPQPHPGNCGKQFVIDKAGY
>gnl|CDD|182239 PRK10096, citG, triphosphoribosyl-dephospho-CoA synthase; Provisional
MSMPATSTKTTKLATSLIDEYALLGWRAMLTEVNLSPKPGLVDRINCGAHKDMALEDFHRSALAIQGWLP
RFIEFGACSAEMAPEAVLHGLRPIGMACEGDMFRATAGVNTHKGSIFSLGLLCAAIGRLLQLNQPVTPTT
VCSTAASFCRGLTDRELRTNNSQLTAGQRLYQQLGLTGARGEAEAGYPLVINHALPHYLTLLDQGLDPEL
ALLDTLLLLMAINGDTNVASRGGEGGLRWLQREAQTLLQKGGIRTPADLDYLRQFDRECIERNLSPGGSA
DLLILTWFLAQI
>gnl|CDD|182240 PRK10098, PRK10098, putative dehydrogenase; Provisional
MESGHRFDAQTLHSFVQAVWRQAGSEEREAKLVADHLVAANLAGHDSHGVGMIPSYVRSWSQGHLQLNHH
AKIVKDAGAVLTLDGDRGFGQVVAHEAMALGIERARQHGICAVALRNSHHIGRIGHWAEQCAAAGLVSIH
FVNVVGDPMVAPFHGRDSRFGTNPFCVVFPRKGKPPLLLDFATSAIAFGKTRVAWNKGVPVPPGCLIDVN
GVPTTDPAVMQESPLGALLTFGEHKGYALAAMCEILGGALSGGKTTHQETLQTSDAILNCMLTIIIDPAA
FGAPDCSAEAEAFVEWVKASPHDGDKPILLPGEPERATRAERQAQGIPLDAGTWQQICDAARQVGMPEAT
>gnl|CDD|182241 PRK10100, PRK10100, transcriptional regulator CsgD
MFNEVHSSHGHTLLLITKPSLQATALLQHLKQSLAITGKLHNIQRSLDDISSGSIILLDMMEADKKLIHY
WQDTLSRKNNNIKILLLNTPEDYPYREIENWPHINGVFYAMEDQERVVNGLQGVLRGECYFTQKLASYLI
THSGNYRYNSTESALLTHREKEILNKLRIGASNNEIARSLFISENTVKTHLYNLFKKIAVKNRTQAVSWA
NDNLRR
>gnl|CDD|182242 PRK10101, csgB, curlin minor subunit CsgB; Provisional
MKNKLLFMMLTILGAPGIAAAAGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQVRQGGSKLLAV
VSQEGSSNRAKIDQTGDYNLAYIDQTGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAVVVQR
QSQMAIRVTQR
>gnl|CDD|182243 PRK10102, csgC, curli assembly protein CsgC; Provisional
MNTLLLLAALSSQITFNTTQQGDIYTIIPQVTLTQPCLCRVQILSLREGSSGQSQTQQEKTLSLPANQPI
ALSKLSLNISPDDRVKIVVTVSDGQSLHLSQQWPPSSEKS
>gnl|CDD|236651 PRK10106, PRK10106, multiple antibiotic resistance protein MarB
IAALLLLFSGQGVAEQTTQPVVQNCRDVMVVPSSQEQPPFDLNHMGTGSDKSDELGVPYYNQHAL
>gnl|CDD|182245 PRK10110, PRK10110, PTS maltose transporter subunit IICB
MTAKTAPKVTLWEFFQQLGKTFMLPVALLSFCGIMLGIGSSLSSHDVITLIPFLGNPVLQAIFTWMSKIG
SFAFSFLPVMFCIAIPLGLARENKGVAAFAGFVGYAVMNLAVNFWLTNKGILPTTDAAVLKANNIQSILG
IQSIDTGILGAVIAGIIVWMLHERFHNIRLPDALAFFGGTRFVPIISSLVMGLVGLVIPLVWPIFAMGIS
GLGHMINSAGDFGPMLFGTGERLLLPFGLHHILVALIRFTDAGGTQEVCGQTVSGALTIFQAQLSCPTTH
GFSESATRFLSQGKMPAFLGGLPGAALAMYHCARPENRHKIKGLLISGVIACVVGGTTEPLEFLFLFVAP
VLYVIHALLTGLGFTVMSVLGVTIGNTDGNIIDFVVFGILHGLSTKWYMVPVVAAIWFVVYYVIFRFAIT
RFNLKTPGRDSEVASSIEKAVAGAPGKSGYNVPAILEALGGADNIVSLDNCITRLRLSVKDMSLVDVQAL
KDNRAIGVVQLNQHNLQVVIGPQVQSVKDEMAGLMHTVQA
>gnl|CDD|182246 PRK10113, PRK10113, cell division activator CedA
MMKPLRQQNRQIISYVPRVEPAPPEHAIKMDSFRDVWMLRGKYVAFVLMGESFLRSPAFSVPESAQRWAN
QIRQEGEVTE
>gnl|CDD|182247 PRK10115, PRK10115, protease 2; Provisional
MLPKAARIPHAMTLHGDTRIDNYYWLRDDTRSQPEVLDYLHQENSYGHRVMASQQALQDRILKEIIDRIP
QREVSAPYIKNGYRYRHIYEPGCEYAIYQRQSAFSEEWDEWETLLDANKRAAHSEFYTLGGMAITPDNTI
MALAEDFLSRRQYGIRFRNLETGNWYPELLDNVEPSFVWANDSWTFYYVRKHPVTLLPYQVWRHTIGTPA
SQDELVYEEKDDTFYVSLHKTTSKHYVVIHLASATTSEVLLLDAELADAEPFVFLPRRKDHEYSLDHYQH
RFYLRSNRHGKNFGLYRTRVRDEQQWEELIPPRENIMLEGFTLFTDWLVVEERQRGLTSLRQINRKTREV
IGIAFDDPAYVTWIAYNPEPETSRLRYGYSSMTTPDTLFELDMDTGERRVLKQTEVPGFDAANYRSEHLW
ITARDGVEVPVSLVYHRKHFRKGHNPLLVYGYGSYGASIDADFSFSRLSLLDRGFVYAIVHVRGGGELGQ
QWYEDGKFLKKKNTFNDYLDACDALLKLGYGSPSLCYGMGGSAGGMLMGVAINQRPELFHGVIAQVPFVD
VVTTMLDESIPLTTGEFEEWGNPQDPQYYEYMKSYSPYDNVTAQAYPHLLVTTGLHDSQVQYWEPAKWVA
KLRELKTDDHLLLLCTDMDSGHGGKSGRFKSYEGVAMEYAFLIALAQGTLPATPAD
>gnl|CDD|182248 PRK10116, PRK10116, universal stress protein UspC; Provisional
MSYSNILVAVAVTPESQQLLAKAVSIARPVNGKISLITLASDPEMYNQFAAPMLEDLRSVMQEETQSFLD
KLIQDADYPIEKTFIAYGELSEHILEVCRKHHFDLVICGNHNHSFFSRASCSAKRVIASSEVDVLLVPLT
GD
>gnl|CDD|182249 PRK10117, PRK10117, trehalose-6-phosphate synthase; Provisional
MSRLVVVSNRIAPPDEHKASAGGLAVGILGALKAAGGLWFGWSGETGNEDQPLKKVKKGNITWASFNLSE
QDYDEYYNQFSNAVLWPAFHYRLDLVQFQRPAWEGYLRVNALLADKLLPLLKDDDIIWIHDYHLLPFASE
LRKRGVNNRIGFFLHIPFPTPEIFNALPPHDELLEQLCDYDLLGFQTENDRLAFLDCLSNLTRVTTRSGK
SHTAWGKAFRTEVYPIGIEPDEIAKQAAGPLPPKLAQLKAELKNVQNIFSVERLDYSKGLPERFLAYEAL
LEKYPQHHGKIRYTQIAPTSRGDVQAYQDIRHQLETEAGRINGKYGQLGWTPLYYLNQHFDRKLLMKIFR
YSDVGLVTPLRDGMNLVAKEYVAAQDPANPGVLVLSQFAGAANELTSALIVNPYDRDEVAAALDRALTMP
LAERISRHAEMLDVIVKNDINHWQECFISDLKQIVPRSAESQQRDKVATFPKLA
>gnl|CDD|236652 PRK10118, PRK10118, flagellar hook length control protein FliK
MITLPQLITTDVDTTTGLPGGKATDAAQDFLALLAGALGGETTQGKDAPLTLADLQAAGGKLSKGLLTTK
GEPLVSDKLADLLAQQANLLIPVDETLPVITDEQSLSSPLTPALKTSALAALSKNAQKDEKADDLSDEDL
ASLSALFAMLPGQDNTTPVADAPSTVLPAEKPTLLTKDMPSAPQDETHTLSSDEHEKGLTSAQLTTAQPD
DAPGTPAQPLTPLAAEAQAKAEVISTPSPVTAAASPTITPHQTQPLPTAAAPVLSAPLGSHEWQQSLSQH
ITLFTRQGQQSAELRLHPEDLGQVQISLKLDDNQAQLQMVSPHSHVRAALEAALPVLRTQLAESGIQLGQ
SNISSESFSGQQQSSSQQQQSSRTGNHEPLAGEDDDTLAVPASLQAAARGNGAVDIFA
>gnl|CDD|182251 PRK10119, PRK10119, putative hydrolase; Provisional
MDLQHWQAQFENWLKNHHQHQDAAHDICHFRRVWATAQKLAADDDVDMLVVLTACYFHDIVSLAKNHPQR
HRSSILAAEETRRILREDFPDFPAEKIEAVCHAIEAHSFSAQIAPLTLEAKIVQDADRLEALGAIGLARV
FAVSGALGVALFDAEDPFAQHRPLDDKQYALDHFQTKLLKLPQTMQTERGKQLAQHNADFLVEFMAKLSA
ELKGEYEGLDEKVIDAFSPAG
>gnl|CDD|182252 PRK10122, PRK10122, UTP--glucose-1-phosphate uridylyltransferase GalF
MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTS
YELESLLEQRVKRQLLAEVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASA
DPLRYNLAAMIARFNETGRSQVLAKRMPGDLSEYSVIQTKEPLDREGKVSRIVEFIEKPDQPQTLDSDLM
AVGRYVLSADIWPELERTEPGAWGRIQLTDAIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRN
LKEGAKFRKGIEKLLSE
>gnl|CDD|182253 PRK10123, wcaM, putative colanic acid biosynthesis protein; Provisional
MPFKKLSRRTFLTASSALAFLHTPFARALPARQSVNINDYNPHDWIASFKQAFSEGQTVVVPAGLVCDNI
NTGIFIPPGKTLHILGSLRGNGRGRFVLQDGSQVTGEEGGSMHNITLDVRGSDCTIKGLAMSGFGPVTQI
YIGGKNKRVMRNLTIDNLTVSHANYAILRQGFHNQIIGANITNCKFSDLQGDAIEWNVAINDRDILISDH
VIERINCTNGKINWGIGIGLAGSTYDNNYPEDQAVKNFVVANITGSDCRQLIHVENGKHFVIRNIKAKNI
TPDFSKKAGIDNATVAIYGCDNFVIDNIEMINSAGMLIGYGVIKGKYLSIPQNFKLNNIQLDNTHLAYKL
RGIQISAGNAVSFVALTNIEMKRASLELHNKPQHLFLRNINVMQESSVGPALKMNFDLRKDVRGVFMAKK
ETLLSLANVHAVNEKGQSSVDIDRINHHIVNVEKINFRLPERRE
>gnl|CDD|182254 PRK10124, PRK10124, putative UDP-glucose lipid carrier transferase; Provisional
TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRS
WRGVKASTELALLLQNWTLSLIFSAGLVAFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHG
YNKRMVAVAGDLPAGQMLLESFRNEPWLGFEVVGVYHDPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIA
MSMCDGARVKKLVRQLADTTCSVLLIPDVFTFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVL
ASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVVTQATQNDPRVTK
VGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVKPGITGWAQINGWRGET
DTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY
>gnl|CDD|182256 PRK10126, PRK10126, low molecular weight protein-tyrosine-phosphatase Wzb
MFNNILVVCVGNICRSPTAERLLQRYHPELKVESAGLGALVGKGADPTAISVAAEHQLSLEGHCARQISR
RLCRNYDLILTMEKRHIERLCEMAPEMRGKVMLFGHWDNECEIPDPYRKSREAFEAVYTLLERSARQWAQ
ALNAEQV
>gnl|CDD|182257 PRK10128, PRK10128, 2-keto-3-deoxy-L-rhamnonate aldolase; Provisional
MNALLSNPFKEGLRKGEVQIGLWLSSTTSYMAEIAATSGYDWLLIDGEHAPNTIQDLYHQLQAIAPYASQ
PVIRPVEGSKPLIKQVLDIGAQTLLIPMVDTAEQARQVVSATRYPPYGERGVGASVARAARWGRIENYMA
QANDSLCLLVQVESKTALDNLDEILDVEGIDGVFIGPADLSASLGYPDNAGHPEVQRIIETSIRRIRAAG
KAAGFLAVDPDMAQKCLAWGANFVAVGVDTMLYTDALDQRLAMFKSGKNGPRAKGSY
>gnl|CDD|182258 PRK10130, PRK10130, HTH-type transcriptional regulator EutR
MKKTRTANLHHLYHEPLPENLKLTPKVEVDNVHQRQTTDVYEHALTITAWQQIYDQLHPGKFHGEFTEIL
LDDIQVFREYTGLALRQSCLVWPNSFWFGIPATRGEQGFIGSQCLGSAEIATRPGGTEFELSTPDDYTIL
GVVISEDVITRQANFLHNPERVLHMLRNQSALEVKEQHKAALWGFVQQALATFCENPENLHQPAVRKVLG
DNLLMAMGAMLEEAQPMVTAESISHQSYRRLLSRAREYVLENMSEPVTVLDLCNQLHVSRRTLQNAFHAI
LGIGPNAWLKRIRLNAVRRELISPWSQSTTVKDAAMQWGFWHLGQFATDYQQLFAEKPSLTLHQRMREWG
>gnl|CDD|182259 PRK10132, PRK10132, hypothetical protein; Provisional
MFNRPNRNDVDDGVQDIQNDVNQLADSLESVLKSWGSDAKGEAEAARRKAQALLKETRARMHGRTRVQQA
ARDAVGCADTFVRERPWCSVGTAAAVGIFIGALLSLRK
>gnl|CDD|182260 PRK10133, PRK10133, L-fucose:H+ symporter permease
MGNTSIQTQSYRAVDKDAGQSRSYIIPFALLCSLFFLWAVANNLNDILLPQFQQAFTLTNFQAGLIQSAF
YFGYFIIPIPAGILMKKLSYKAGIITGLFLYALGAALFWPAAEIMNYTLFLVGLFIIAAGLGCLETAANP
FVTVLGPESSGHFRLNLAQTFNSFGAIIAVVFGQSLILSNVPHQSQDVLDKMTPEQLSAYKHSLVLSVQT
PYMIIVAIVLLVALLIMLTKFPALQSDNHSDAKQGSFSASLSRLARIRHWRWAVLAQFCYVGAQTACWSY
LIRYAVEEIPGMTAGFAANYLTGTMVCFFIGRFTGTWLISRFAPHKVLAAYALIAMALCLISAFAGGHVG
LIALTLCSAFMSIQYPTIFSLGIKNLGQDTKYGSSFIVMTIIGGGIVTPVMGFVSDAAGNIPTAELIPAL
CFAVIFIFARFRSQTATN
>gnl|CDD|236653 PRK10137, PRK10137, alpha-glucosidase; Provisional
MKIKTILTPVTCALLISGCSSFSAHAANADNYKNVIDRTGAPQYMRDYDYDDHQRFNPFFDLGAWHGHLL
PDGPNTMGGFPGVALLTEEYINFMASNFDRLTVWQDGKKVDFTLEAYSIPGALVQKLTADDVQVEMTLRF
ATPRTSLLETKITSNKPLDLVWDGELLEKLEAKEGKPLSDKTIAGEYPDYQRKISATRDGLKVTFGKVRA
TWDLLTSGESEYQVHKSLPVQTEINGNRFTSKAHINGSTTLYTTYSHLLTAQEVSKEQMQIRDILARPAF
YLTASQQRWEEYLKKGLTNPDATPEQTRVAVKAMETLNGNWRSPAGAVKFNTVTPSVTARWFSGNQTWPW
DTWKQAYAMAHFNPDVAKENIRAVFSWQIQPDDSVRPQDVGFVPDLIAYNLSPERGGDGGNWNERNTKPS
LAAWSVMEVYNVTQDKAWLAEMYPKLVAYHDWWLRNRDHNGNGVPEYGATRDKAHNTESGEMLFTVKKGD
KEETQSGLNNYARVVEKGQYDSLEIPAQVAASWESGRDDAAVFGFIDKEQLDKYVANGGKRSDWTVKFAE
NRSQDGTLLGYSLLQESVDQASYMYSDNHYLAEMATILGKPEEAKRYRQLAQQLADYINTCMFDETTGFY
YDVRIEDKPLANGCAGKPIVERGKGPEGWSPLFNGAATQANADAVVKVMLDPKEFNTFVPLGTAALTNPA
FGADIYWRGRVWVDQFYFGLKGMERYGYRDDALKLADTFFRHAKGLTADGPIQENYNPLTGAQQGAPNFS
WSAAHLYMLYNDFFRK
>gnl|CDD|182262 PRK10139, PRK10139, serine endoprotease DegQ
MKKQTQLLSALALSVGLTLSASFQAVASIPGQVAGQAPLPSLAPMLEKVLPAVVSVRVEGTASQGQKIPE
EFKKFFGDDLPDQPAQPFEGLGSGVIIDAAKGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDI
ALLQIQNPSKLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIISALGRSGLNLEGLENFIQTDASIN
RGNSGGALLNLNGELIGINTAILAPGGGSVGIGFAIPSNMARTLAQQLIDFGEIKRGLLGIKGTEMSADI
AKAFNLDVQRGAFVSEVLPNSGSAKAGVKAGDIITSLNGKPLNSFAELRSRIATTEPGTKVKLGLLRNGK
PLEVEVTLDTSTSSSASAEMITPALQGATLSDGQLKDGTKGIKIDEVVKGSPAAQAGLQKDDVIIGVNRD
RVNSIAEMRKVLAAKPAIIALQIVRGNESIYLLLR
>gnl|CDD|182263 PRK10140, PRK10140, N-acetyltransferase
MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDV
QQRPRRSHVADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEG
TGKKYALRNGEYVDAYYMARVK
>gnl|CDD|236654 PRK10141, PRK10141, DNA-binding transcriptional repressor ArsR; Provisional
MSFLLPLQLFKILSDETRLGIVLLLRESGELCVCDLCTALDQSQPKISRHLALLRESGLLLDRKQGKWVH
YRLSPHIPAWAAKIIEQAWLCEQEDVQAIVRNLARQNCSGDSKNICS
>gnl|CDD|182266 PRK10146, PRK10146, aminoalkylphosphonate N-acetyltransferase
MPACELRPATQYDTDAVYALICELKQAEFDHQAFRVGFNANLRDPNMRYHLALLDGEVVGMIGLHLQFHL
HHVNWIGEIQELVVMPQARGLNVGSKLLAWAEEEARQAGAEMTELSTNVKRHDAHRFYLREGYEQSHFRF
TKAL
>gnl|CDD|236655 PRK10147, phnH, phosphonate C-P lyase system protein PhnH
AMTLQPGFADPVQDAQHVFRALLKAMARPGTIVTLPPALRGPQPLNPATTAVLLTLCDNDTPLWLAPALD
NDAVRQWLRFHTGAPLVAEPEQARFALLDGAIALPPLFAFALGTLEYPERSATLILQVASLEGGRPLRLR
GPGIEAEERIAAPGLPECFLHERTENPALFPLGIDLILTCGERLLALPRTTHVEVC
>gnl|CDD|236656 PRK10148, PRK10148, VOC family metalloprotein YjdN
MPLSPYLSFAGNCADAIAYYQQTLGAELLYKISFGEMPKSAQDSEEGCPSGMQFPDTAIAHANVRIAGSD
IMMSDAIPSGKAHYSGFTLVLDTQDVEEGKRWFDNLAANGKIEMAWQETFWAHGFGKVTDKFGVPWMINV
VKQQPTQ
>gnl|CDD|236657 PRK10150, PRK10150, beta-D-glucuronidase; Provisional
MLYPVETKTREIKDLSGLWAFKLDRENCGIDQRWWESALPESRAMAVPGSFNDQFADADIRNYVGDVWYQ
REVFIPKGWAGQRIVLRFGSVTHYAKVWVNGQEVMEHKGGYTPFEADITPYVYAGKSVRITVCVNNELNW
QTLPPGNVIEDGNGKKKQKYNFDFFNYAGIHRPVMLYTTPKTHIDDITVVTELAQDLNHASVDWSVETNG
DVDSVSVTLRDADGQVVATGQGTSGTLQVVNPHLWQPGEGYLYTLCVELAKSGTECDTYPLRFGIRSVAV
KGGQFLINGKPFYFKGFGKHEDADIRGKGLDEVLNVHDHNLMKWIGANSFRTSHYPYSEEMLDLADRHGI
VVIDETPAVGLNLSFGAGLEAGNKPKETYSEEAVNGETQQAHLQAIRELIARDKNHPSVVMWSIANEPAS
REQGAREYFAPLAELTRKLDPTRPVTCVNVMFATPDTDTVSDLVDVLCLNRYYGWYVDSGDLETAEKVLE
KELLAWQEKLHKPIIITEYGADTLAGLHSMYDDMWSEEYQCAFLDMYHRVFDRVPAVVGEQVWNFADFAT
SQGILRVGGNKKGIFTRDRQPKSAAFLLKKRWTGIPFGEKPQKG
>gnl|CDD|182270 PRK10151, PRK10151, 50S ribosomal protein L7/L12-serine acetyltransferase
MTEIIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMF
MIFKEDELIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPA
SNQVALRNGFTLEGCLKQAEYLNGAYDDVNLYARIIDSD
>gnl|CDD|236658 PRK10153, PRK10153, DNA-binding transcriptional activator CadC; Provisional
MQQPVFRIGEWLVTPSENKISRQGREVTLEPRLIDLLVFFAQHSGEVLSRDELIDHVWDRAIVTDHVVTQ
SISELRKSLKDGREDNPEYIVTVPKRGYKLVAPVIWYSEEEGEEILASSPPPIPEAVPATAEPSESANAQ
FPAPPLTRAVCQSPAKSKRFTTFWVWRLFLLSLGICVLLVAMSSLTYRQPVVKIRQLLNPRDIDFRFQNG
NSCNNWSSQLSYADGIGQLLMADLNTVSTFVVHDKTNYNINEPSSSGKTLGIAFVNQRHYRAQQCFLSVE
LVDNADGSVMLSKRYFLTNGNQLSVQNDLSNSLSRALNQPWPERMQERLQQGLPHQGAALTLFYQAHHYL
NSGDAKSLNKASDLLEEILKSEPDFTYAQAEKALADIVRHSQQPLDEKQLAALSTELDNIVALPELNVLP
RIYEILAVQALVKGKTDEAYQAINKAIDLEMSWLNYVLLGKVYELKGDNRLAADAYSTAFNLRPGENTLY
WIENLVFQTSVETVVPYLYRFLAPSVV
>gnl|CDD|182272 PRK10154, PRK10154, DUF2541 family protein
MKSVFTISASLAISLMLCCTAQANDHKILGVIAMPRNETNDLALKLPVCRIVKRIQLSADHGDLQLSGAS
VYFKAARSASQSLNIPSEIKEGQTTDWININSDNDNKRCVSKITFSGHTVNSSDMATLKIIGDD
>gnl|CDD|182273 PRK10157, PRK10157, putative oxidoreductase FixC; Provisional
MSEDIFDAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVTGGRLYAHSLEHIIPGFADSAPVER
LITHEKLAFMTEKSAMTMDYCNGDETSPSQRSYSVLRSKFDAWLMEQAEEAGAQLITGIRVDNLVQRDGK
VVGVEADGDVIEAKTVILADGVNSILAEKLGMAKRVKPTDVAVGVKELIELPKSVIEDRFQLQGNQGAAC
LFAGSPTDGLMGGGFLYTNENTLSLGLVCGLHHLHDAKKSVPQMLEDFKQHPAVAPLIAGGKLVEYSAHV
VPEAGINMLPELVGDGVLIAGDAAGMCMNLGFTIRGMDLAIAAGEAAAKTVLSAMKSDDFSKQKLAEYRQ
HLESGPLRDMRMYQKLPAFLDNPRMFSGYPELAVGVARDLFTIDGSAPELMRKKILRHGKKVGFINLIKD
GMKGVTVL
>gnl|CDD|236659 PRK10158, PRK10158, bifunctional tRNA pseudouridine(32) synthase/23S rRNA pseudouridine(746) synthase RluA
MGMENYNPPQEPWLVILYQDEHIMVVNKPSGLLSVPGRLEEHKDSVMTRIQRDYPQAESVHRLDMATSGV
IVVALTKAAERELKRQFREREPKKQYVARVWGHPSPAEGLVDLPLICDWPNRPKQKVCYETGKPAQTEYE
VVEYAADNTARVVLKPITGRSHQLRVHMLALGHPILGDRFYASPEARAMAPRLLLHAEMLTITHPAYGNS
MTFKAPADF
>gnl|CDD|182275 PRK10159, PRK10159, phosphoporin PhoE
MKKSTLALVVMGIVASASVQAAEVYNKDGNKLDVYGKVKAMHYMSDNDSKDGDQSYIRFGFKGETQINDQ
LTGYGRWEAEFAGNKAESDTAQQKTRLAFAGLKYKDLGSFDYGRNLGALYDVEAWTDMFPEFGGDSSAQT
DNFMTKRASGLATYRNTDFFGVIDGLNLTLQYQGKNENRDVKKQNGDGFGTSLTYDFGGSDFAISGAYTN
SDRTNEQNLQSRGTGKRAEAWATGLKYDANNIYLATFYSETRKMTPISGGFANKTQNFEAVAQYQFDFGL
RPSLGYVLSKGKDIEGIGDEDLVNYIDVGATYYFNKNMSAFVDYKINQLDSDNKLNINNDDIVAVGMTYQ
F
>gnl|CDD|182276 PRK10160, PRK10160, taurine ABC transporter permease TauC
MSVLINEKLHSRRLKWRWPLSRQLTLSIGTLAVLLAVWWAVAALQLISPLFLPPPQQVLAKLLTIAGPQG
FMDATLWQHLAASLTRIVLALLAAVVIGIPVGIAMGLSPTVRGILDPLIELYRPVPPLAYLPLMVIWFGI
GETSKILLIYLAIFAPVAMSALAGVKSAQQVRIRAAQSLGASRAQVLWFVILPGALPEILTGLRIGLGVG
WSTLVAAELIAATRGLGFMVQSAGEFLATDVVLAGIAVIAIIAFLLELGLRALQRRLTPWHGEVQ
>gnl|CDD|182277 PRK10161, PRK10161, phosphate response regulator transcription factor PhoB
MARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKR
ESMTRDIPVVMLTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRRISPMAVEEVIEMQGLSLD
PTSHRVMAGEEPLEMGPTEFKLLHFFMTHPERVYSREQLLNHVWGTNVYVEDRTVDVHIRRLRKALEPGG
HDRMVQTVRGTGYRFSTRF
>gnl|CDD|236660 PRK10162, PRK10162, acetyl esterase
ENKLPVLDLISAEMKAVVNTQQPDLPDWPATGDIAEQRQYYTLERRFWNAGAPEMATRAYMVPTPYGQVE
TRLYYPQPDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCC
YFHQHAEDYGINMSRIGFAGDSAGAMLALASALWLRDKQIDCGKVAGVLLWYGLYGLRDSVSRRLLGGVW
DGLTQQDLQMYEEAYLSNDADRESPYYCLFNNDLTRDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCE
FKLYPGTLHAFLHYSRMMDTADDALRDGAQFFTAQLKT
>gnl|CDD|182279 PRK10163, PRK10163, HTH-type transcriptional repressor AllR
MTEVRRRGRPGQAEPVAQKGAQALERGIAILQYLEKSGGSSSVSDISLNLDLPLSTTFRLLKVLQAADFV
YQDSQLGWWHIGLGVFNVGAAYIHNRDVLSVAGPFMRRLMLLSGETVNVAIRNGNEAVLIGQLECKSMVR
MCAPLGSRLPLHASGAGKALLYPLAEEELMSIILQTGLQQFTPTTLVDMPTLLKDLEQARELGYTVDKEE
HVVGLNCIASAIYDDVGSVVAAISISGPSSRLTEDRFVSQGELVRDTARDISTALGLKAHP
>gnl|CDD|182280 PRK10167, PRK10167, hypothetical protein; Provisional
MNQQRFDDSTLIRIFALHELHRLKEHGLTRGALLDYHSRYKLVFLAHSQPEYRKLGPFVADIHQWQSLDD
FYNQYRQRVIVLLSHPANVRDHTNVLMHVQGYFRPHIDSTERQQLAALIDSYRRGEQPLLAPLMRIKHYM
ALYPDAWLSGQRYFELWPRVINLRHSGVL
>gnl|CDD|182281 PRK10170, PRK10170, Ni/Fe-hydrogenase large subunit
MSTQYETQGYTINNAGRRLVVDPITRIEGHMRCEVNINDQNVITNAVSCGTMFRGLEIILQGRDPRDAWA
FVERICGVCTGVHALASVYAIEDAIGIKVPDNANIIRNIMLATLWCHDHLVHFYQLAGMDWIDVLDALKA
DPRKTSELAQSLSSWPKSSPGYFFDVQNRLKKFVEGGQLGIFRNGYWGHPQYKLPPEANLMGFAHYLEAL
DFQREIVKIHAVFGGKNPHPNWIVGGMPCAINIDESGAVGAVNMERLNLVQSIITRTADFINNVMIPDAL
AIGQFNKPWSEIGTGLSDKCVLSYGAFPDIANDFGEKSLLMPGGAVINGDFNNVLPVDLVDPQQVQEFVD
HAWYRYPNDQVGRHPFDGITDPWYNPGDVKGSDTNIQQLNEQERYSWIKAPRWRGNAMEVGPLARTLIAY
HKGDAATVESVDRMMSALNLPLSGIQSTLGRILCRAHEAQWAAGKLQYFFDKLMTNLKNGNLATASTEKW
EPATWPTECRGVGFTEAPRGALGHWAAIRDGKIDLYQCVVPTTWNASPRDPKGQIGAYEAALMNTKMAIP
EQPLEILRTLHSFDPCLACSTHVLGDDGSELISVQVR
>gnl|CDD|182282 PRK10171, PRK10171, Ni/Fe-hydrogenase b-type cytochrome subunit
MQQKSDNVVSHYVFEAPVRIWHWLTVLCMAVLMVTGYFIGKPLPSVSGEATYLFYMGYIRLIHFSAGMIF
TVVLLMRIYWAFVGNRYSRELFIVPVWRKSWWQGVWYEIRWYLFLAKRPSADIGHNPIAQAAMFGYFLMS
VFMIITGFALYSEHSQYAIFAPFRYVVEFFYWTGGNSMDIHSWHRLGMWLIGAFVIGHVYMALREDIMSD
DTVISTMVNGYRSHKFGKISNKERS
>gnl|CDD|182283 PRK10172, PRK10172, AppA family phytase/histidine-type acid phosphatase
MSVLMKAILIPFLSLLIPLTPQSAFAQSEPELKLESVVIVSRHGVRAPTKATQLMQDVTPDAWPQWPVKL
GWLTPRGGELVTLLGHYQRQRLVADGLLAAKGCPQPGQVAAIADVDQRTRKTGEAFLAGLAPDCAITVHT
QADTSKPDPLFNPLKTGVCQLDNANVTDAILSRAGGSIADFTQRYQTAFRELERVLNFAQSPLCLSREKQ
DKSCSLTQALPSELKVSADNVSLSGAVSLASMLTEIFLLQQAQGMPEPAWGRITDSHQWNTLLSLHNAQF
YLLQRTPEVARHRATPLLDLIMTALTPHPPQKQAYGITLPTSVLFIAGHDTNLANLGGALELNWTLPGQP
DNTPPGGELVFERWRRLSDNSQWIQVSLVYQTLQQMRDKTPLSLNTPPGEVKLTLAGCEERNAQGMCSLA
GFTQIVNEARIPACSL
>gnl|CDD|182284 PRK10173, PRK10173, glucose-1-phosphatase/inositol phosphatase; Provisional
MKKSLLAAAVAGAVLLSSAAQAQTVPEGYQLQQVLMMSRHNLRAPLANNGSVLEQSTPNAWPEWDVPGGQ
LTTKGGVLEVYMGHYMREWLAQQGLVKSGECPPPDTVYAYANSLQRTVATAQFFITGAFPGCDIPVHHQE
KMGTMDPTFNPVITDDSAAFREQALAAMEKELSKLQLTPSYQLLEKIVNYKDSPACKEKQQCSLVDGKNT
FSAKYQQEPGVSGPLKVGNSLVDAFTLQYYEGFPMDQVAWGEIKTDQQWKVLSKLKNGYQDSLFTSPEVA
RNVAKPLVKYIDKALVTDRASAPKVTVLVGHDSNIASLLTALDFKPYQLHDQYERTPIGGKIVFQRWHDS
KANRDLMKIEYVYQSAEQLRNADALTLQAPPQRVTLELKGCPIDANGFCPMDKFDSVLNEAAK
>gnl|CDD|182285 PRK10174, PRK10174, hypothetical protein; Provisional
MPTQEAKAHHVGEWASLRNTSPEIAEAIFEVAGYDEKLAEKIWEEGSDEVLVKAFAKTDKDSLFWGEQTI
ERKNV
>gnl|CDD|182286 PRK10175, PRK10175, YceK/YidQ family lipoprotein
MRLIVVSIMVTLLSGCGSIISRTIPGQGHGNQYYPGVQWDVRDSAWRYITILDLPFSLVFDTLLLPIDIH
HGPYE
>gnl|CDD|236661 PRK10177, PRK10177, YchO/YchP family invasin
TMSRFVFRSFSLTLLLLLAGGTANAQSAFTQQAQNPFDQNQDGLPDLGMAPENHDGEKHFAEMAKDFGEA
SMNDNGLDTGEQAKQFAFGKVRDAVSQQVNQHVESWLSPWGNASVDLKVDNEGHFTGSRGSWFVPLQDND
RYLTWSQLGLTQQDDGLVSNVGVGQRWAAGNWLLGYNTFYDNLLDENLQRAGFGAEAWGEYLRLSANYYQ
PFAAWHEQTATQEQRMARGYDITAQMRLPFYQHLNTSVSVEQYFGDRVDLFNSGTGYHNPVALSLGLNYT
PVPLVTVTAQHKQGESGESQNNLGLKLNYRFGVPLKKQLSAGEVAESQSLRGSRYDNPQRNNLPVMEYRQ
RKTLTVFLATPPWDLQPGETVPLKLQIRSRHGIRQLSWQGDTQALSLTPGADANSAEGWTIIMPAWDNGE
GASNRWRLSVVVEDNQGQRVSSNEITLTLVEPFDALSNDELRWEP
>gnl|CDD|236662 PRK10178, PRK10178, D-alanyl-D-alanine dipeptidase; Provisional
MMDTTRLVEITVAFHGVEIDLKYATADNLTGKPIYREARCLLHKDAEAALRKAVSIAQLAGLTLRIYDAY
RPQQAQQVLWDACPDPQYVADLGRGSNHSRGTAIDLTLVDAHGNILDMGTGFDEMHARSHHFHPGVPPAA
QRNRLLLLGIMHAAGFVHIASEWWHYELPGAAAYPLLDDQASGT
>gnl|CDD|182289 PRK10179, PRK10179, formate dehydrogenase-N subunit gamma; Provisional
MSKSKMIVRTKFIDRACHWTVVICFFLVALSGISFFFPTLQWLTQTFGTPQMGRILHPFFGIAIFVALMF
MFVRFVHHNIPDKKDIPWLLNIVEVLKGNEHKVADVGKYNAGQKMMFWSIMSMIFVLLVTGVIIWRPYFA
QYFPMQVVRYSLLIHAAAGIILIHAILIHMYMAFWVKGSIKGMIEGKVSRRWAKKHHPRWYREIEKAEAK
KESEEGI
>gnl|CDD|182290 PRK10183, PRK10183, hypothetical protein; Provisional
KLTPETDANHKTASPQPIRRISSQTLLGPDGKVIIDHDGQEYLLRKTQAGKLLLTK
>gnl|CDD|182291 PRK10187, PRK10187, trehalose-6-phosphate phosphatase; Provisional
MTEPLTVPPELSANYAWFFDLDGTLAEIKPHPDQVVVPDNILQGLQLLATANDGALALISGRSMVELDAL
AKPYRFPLAGVHGAERRDINGKTHIVHLPDAIARDISVQLHTALAQLPGAELEAKGMAFALHYRQAPQHE
DALLALAQRITQIWPQLALQPGKCVVEIKPRGTNKGEAIAAFMQEAPFAGRTPVFVGDDLTDEAGFAVVN
RLGGISVKVGTGATQASWRLAGVPDVWSWLEMITTAQQQKRENNRRDDYESFSRSI
>gnl|CDD|182292 PRK10188, PRK10188, transcriptional regulator SdiA
MQDTDFFSWRRTMLLRFQEMAAAEEVYHELQLQTQQLEYDYYSLCVRHPVPFTRPKVAFYTTYPEAWVSH
YQAENYFAIDPVLKPENFSQGHLMWNDDLFSEAQALWDAARAHGLRRGVTQCLMLPNRALGFLSFSRCSA
REIPILSDELELRLQLLVRESLMALMRLEDEMVMTPEMNFSKREKEILKWTAEGKTSAEIAMILSISENT
VNFHQKNMQKKFNAPNKTQIACYAAATGLI
>gnl|CDD|182293 PRK10189, PRK10189, EmmdR/YeeO family multidrug/toxin efflux MATE transporter
LNISSALRQVVHGTRWYAKRKSYRVLFWREITPLAVPIFIENLCVLLMGVLSTFLVSWLGKEAMAGVGLA
DSFNMVIMAFFAAIDLGTTVVVAFSLGKRDRRRARAAARQSLVIMTLFAVLLAVLIHFFGEQIIDLVAGD
ATPEVKALALTYLELTVWSYPAAAITLIGSGALRGAGNTKIPLLINGGMNILNIIISSILIYGLFSWQGL
GFVGAGLGLTISRYIGAVAIIWVLMIGFNPALRISLKSYFKPLNFAIIWEVMGIGIPASIESVLFNGGKL
LTQMFVAGMGTSVIAGNFIAFSIAALINLPGNALGSASTIITGTRLGKGQIAQAERQLRHVFWLSTLGLT
AIAWLSAPFAGLLASFYTQDPDVKHVVKILIWLNALFMPIWAASWVLPAGLKGARDARYAMWVSMLGMWG
CRVVAGYILGIMLGFGVVGVWMGMFLDWAVRGVLFYWRMVSGRWLWKYPRPEPQKCEK
>gnl|CDD|182294 PRK10190, PRK10190, L,D-transpeptidase; Provisional
MRRVNILCSFALLFASHTSLAVTYPLPPEGSRLVGQSLTVTVPDHNTQPLETFAAQYGQGLSNMLEANPG
ADVFLPKSGSQLTIPQQLILPDTVRKGIVVNVAEMRLYYYPPDSNTVEVFPIGIGQAGRETPRNWVTTVE
RKQEAPTWTPTPNTRREYAKRGESLPAFVPAGPDNPMGLYAIYIGRLYAIHGTNANFGIGLRVSQGCIRL
RNDDIKYLFDNVPVGTRVQIIDQPVKYTTEPDGSRWLEVHEPLSRNRAEFESDRKVPLPVTPSLRAFING
QEVDVNRANAALQRRSGMPVNISSGSRQMF
>gnl|CDD|182295 PRK10191, PRK10191, putative acyl transferase; Provisional
MVLAYRVAHFCSVWRKKNVLNNLWAAPLLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVA
GDDFTIRHGVTIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKA
RVKVIK
>gnl|CDD|182296 PRK10194, PRK10194, ferredoxin-type protein NapF
KIDASRRGILTGRWRKASNGIRPPWSGDESHFLTHCTRCDACINACENNILQRGAGGYPSVNFKNNECSF
CYACAQACPESLFSPRHTRAWDLQFTIGDACLAYQSVECRRCQDSCEPMAIIFRPTLSGIYQPQLNSQLC
NGCGACAASCPVSAITAEYLHAH
>gnl|CDD|182297 PRK10197, PRK10197, GABA permease
MLSIAGVIGASLFVGSSVAIAEAGPAVLLAYLFAGLLVVMIMRMLAEMAVATPDTGSFSTYADKAIGRWA
GYTIGWLYWWFWVLVIPLEANIAAMILHSWVPGIPIWLFSLVITLALTGSNLLSVKNYGEFEFWLALCKV
IAILAFIFLGAVAISGFYPYAEVSGISRLWDSGGFMPNGFGAVLSAMLITMFSFMGAEIVTIAAAESDTP
EKHIVRATNSVIWRISIFYLCSIFVVVALIPWNMPGLKAVGSYRSVLELLNIPHAKLIMDCVILLSVTSC
LNSALYTASRMLYSLSRRGDAPAVMGKINRSKTPYVAVLLSTGAAFLTVVVNYYAPAKVFKFLIDSSGAI
ALLVYLVIAVSQLRMRKILRAEGSEIRLRMWLYPWLTWLVIGFITFVLVVMLFRPAQQLEVISTGLLAIG
IICTVPIMARWKKLVLWQKTPVHNTR
>gnl|CDD|182298 PRK10198, PRK10198, formate hydrogenlyase regulator HycA
MTIWEISEKADYIAQRHRRLQDQWHIYCNSLVQGITLSKARLHHAMSCAPDKDLCFVLFEHFRIYVTLAD
GFNSHTIEYYVETKDGEDKQLIAQAQLDIDGMIDGRVNNRDREQVLEHYLEKIASVYDSLYTAVEDNVPV
NLSQLVKGQSPA
>gnl|CDD|182299 PRK10199, PRK10199, alkaline phosphatase isozyme conversion aminopeptidase; Provisional
MFSALRHRTAALALGVCFILPVQAASPKPGDFANTQARHIATFFPGRMTGSPAEMLSADYLRQQFQQMGY
QSDIRTFNSRYIYTARDNRKNWHNVTGSTVIAAHEGKAPQQIIIMAHLDTYAPQSDADVDANLGGLTLQG
MDDNAAGLGVMLELAERLKNVPTEYGIRFVATSGEEEGKLGAENLLKRMSDTEKKNTLLVINLDNLIVGD
KLYFNSGVNTPEAVRKLTRDRALAIARRHGIAATTNPGLNKNYPKGTGCCNDAEVFDKAGIPVLSVEATN
WNLGNKDGYQQRAKTAAFPAGNSWHDVRLDNQQHIDKALPGRIERRCRDVVRIMLPLVKELAKASK
>gnl|CDD|182300 PRK10200, PRK10200, putative racemase; Provisional
MKTIGLLGGMSWESTIPYYRLINEGIKQRLGGLHSAQLLLHSVDFHEIEECQRRGEWDKTGDILAEAALG
LQRAGAEGIVLCTNTMHKVADAIESRCSLPFLHIADATGRAITGAGMTRVALLGTRYTMEQDFYRGRLTE
QFSINCLIPEADERAKINQIIFEELCLGQFTEASRAYYAQVIARLAEQGAQGVIFGCTEIGLLVPEERSV
LPVFDTAAIHAEDAVAFMLS
>gnl|CDD|182301 PRK10201, PRK10201, G/U mismatch-specific DNA glycosylase
MVEDILAPGLRVVFCGINPGLSSAHTGFPFAHPANRFWKVIHQAGFTDRQLKPEEAQHLLDTRCGVTKLV
DRPTVQANEVSKQELRSGGRKLIEKIEDYQPQALAVLGKQAYEQGFSQRGAQWGKQTLTIGSTQVWVLPN
PSGLNRASLEKLVEAYRELDQALVVRGR
>gnl|CDD|182302 PRK10202, ebgC, beta-galactosidase subunit beta
MRIIDNLEQFRQIYASGKKWQRCVEAIENIDNIQPGVAHSIGDSLTYRVETDSATDALFTGHRRYFEVHY
YLQGQQKIEYAPKETLQVVEYYRDETDREYLKGCGETVEVHEGQIVICDIHEAYRFICNNAVKKVVLKVT
IEDGYFHNK
>gnl|CDD|182303 PRK10203, PRK10203, hypothetical protein; Provisional
MWLLDQWAERHILEAQRKGEFDNLPGSGEPLILDDDSHVPPELRAGYRLLKNAGCLPPELEQRREAIQLL
DLLKGIREDDPQYQEVSRRLSLLELKLRQAGLSTDFLRGDYADKLLNKINDN
>gnl|CDD|182304 PRK10204, PRK10204, hypothetical protein; Provisional
MKKLTDKQKSRLWEQQRNRNFQASRRLEGVEMPLVTLTAEEALARLEELRRHYER
>gnl|CDD|182305 PRK10206, PRK10206, putative oxidoreductase; Provisional
VINCAFIGFGKSTTRYHLPYVLNRKDSWHVAHIFRRHAKPEEQAPIYSHIHFTSDLDEVLNDPDVKLVVV
CTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTAKKAIESG
KLGEIVEVESHFDYYRPVAETKPGLPQDGAFYGLGVHTMDQIISLFGRPDHVAYDIRSLRNKANPDDTFE
AQLFYGDLKAIVKTSHLVKIDYPKFIVHGKKGSFIKYGIDQQETSLKANIMPGEPGFAADDSVGVLEYVN
DEGVTVREEMKPEMGDYGRVYDALYQTLTHGAPNYVKESEVLTNLEILERGFEQASPATVTLAK
>gnl|CDD|182306 PRK10207, PRK10207, dipeptide/tripeptide permease DtpB
MNTTAPMGLLQQPRPFFMIFFVELWERFGYYGVQGILAVFFVKQLGFSQEQAFITFGAFAALVYGLISIG
GYVGDHLLGTKRTIVLGAIVLAIGYFMTGMSLLKPDLIFIALGTIAVGNGLFKANPASLLSKCYPPKDPR
LDGAFTLFYMSINIGSLISLSLAPVIADKFGYSVTYNLCGAGLIIALLVYFACRGMVKDIGSEPDHKPMS
FSKLLLVLLGSVVMIFVCAWLMHNVEVANLVLIVLSIVVTIIFFREAFKLDKTGRNKMFVAFVLMLEAVV
FYILYAQMPTSLNFFAINNVHHEILGFSINPVSFQALNPFWVVVASPILAGIYTHLGSKGKDLSMPMKFT
LGMFLCSLGFLTAAAAGMWFADAQGLTSPWFIVLVYLFQSLGELFISALGLAMIAALVPQHLMGFILGMW
FLTQAAAFLLGGYVATFTAVPDNITDPLETLPVYTNVFGKIGLVTLGVAVVMALMVPWLNRMINTPESH
>gnl|CDD|182307 PRK10208, PRK10208, acid-activated periplasmic chaperone HdeA
TGKSKTNMKKALAVVLGGLLLLPVVSNAADAQKAADNKKPVNSWTCEDFLAVDESFQPTAVGFAEALNNK
DKPEDAVIDVQGIETVTPAIVQACTQDKKASFKDKVKGEWKKIK
>gnl|CDD|182308 PRK10209, PRK10209, HdeD family acid-resistance protein
MLYIDKATLLNFDEEMLKKQRRAIQIIAVLLFIGGLLCLSFPFVSGDALSTVVGILLICSGIALIVGLFA
NRSHNFWPMLSGILLGVAYLVLGYFFIRNPEVGMFSLAAFIAGLFCVGGIIRLMSGYKQRKMKGSWLQIV
IGVLDLVIAWLLLGAGPQVSITLVTTLVGIEMIFSSFSLFSFASLFKKQQ
>gnl|CDD|182309 PRK10213, nepI, purine ribonucleoside efflux pump NepI
MSEFIAENRGADAITRPNWSAVFSVAFCVACLIIVEFLPVSLLTPMAQDLGISEGVAGQSVTVTAFVAMF
ASLFITQTIQATDRRYVVILFAVLLTLSCLLVSFANSFSLLLIGRACLGLALGGFWAMSASLTMRLVPPR
TVPKALSVIFGAVSIALVIAAPLGSFLGELIGWRNVFNAAAVMGVLCIFWIIKSLPSLPGEPSHQKQNTF
RLLQRPGVMAGMIAIFMSFAGQFAFFTYIRPVYMNLAGFGVDGLTLVLLSFGIASFVGTSLSSFILKRSV
KLALAGAPLVLAVSALVLTLWGSDKIVATGVAIIWGLTFALVPVGWSTWITRSLADQAEKAGSIQVAVIQ
LANTCGAAIGGYALDNIGLTSPLMLSGTLMLLTALLVTAKVKMK
>gnl|CDD|182310 PRK10214, PRK10214, ilvB operon leader peptide IvbL
MTTSMLNAKLLPTAPSAAVVVVRVVVVVGNAP
>gnl|CDD|236663 PRK10215, PRK10215, hypothetical protein; Provisional
KLNFKGFFKAAGLLPLAFMLSGCISYGLVSHTAKGESGKYQWQSDTITGLSLAKDSNGTKGWVFVGEHFD
YLLTDGADEVVKMLNDPAINRHKIQVADDAKFVLNAGKKKFTGKISLYYRWNNEEEKALATGYGFICGVQ
HETCTRSLENLKGTIHQKNKNMDYSKVMAFYHPFTVRFYEYKSTRGIPGVSRALLPVTVALDIVTAPLQL
LIVYAVNQ
>gnl|CDD|182312 PRK10216, PRK10216, HTH-type transcriptional regulator YidZ
MKKSLTTLDLNLLLCLQLLMQERSVTKAAKRMNVTPSAVSKSLAKLRAWFDDPLFVNTPLGLSPTPLMVS
MEQNLAEWMQMGNQLLDKPHHQTPRGLKFELAAESPLMMIMLNALSKRIYQRYPQATIKLRNWDYDSLDA
ITRGEVDIGFTGRESHPRSRELLSLLPLAIDFEVLFSDLPCVWLRKDHPALHEEWNLDTFLRYPHISICW
EQSDTWALDDVLQELGRERTIALSLPEFEQSLFMAAQPDHLLLATAPRYCQYYNQLHQLPLVALPLPFDE
SQQKKLEVPFTLLWHKRNSHNPKIVWLRETIKNLYASMA
>gnl|CDD|182313 PRK10217, PRK10217, dTDP-glucose 4,6-dehydratase; Provisional
MRKILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVF
TEHQPDCVMHLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALTEDKKSAFRFHHISTDEVYGD
LHSTDDFFTETTPYAPSSPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALA
GKPLPVYGNGQQIRDWLYVEDHARALYCVATTGKVGETYNIGGHNERKNLDVVETICELLEELAPNKPQG
VAHYRDLITFVADRPGHDLRYAIDASKIARELGWLPQETFESGMRKTVQWYLANESWWKQVQDGSYQGER
LGLKG
>gnl|CDD|104396 PRK10218, PRK10218, translational GTPase TypA
MIEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRI
NIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWV
VDQVFDLFVNLDATDEQLDFPIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQIS
QLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLG
ELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCGKEGKFVTSRQILDRLNKELVHNVALRVEET
EDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPYENVTLDVEEQHQGSVMQALG
ERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRPGEVGQRQNGVLIS
NGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPP
IRMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRAPKDD
>gnl|CDD|182314 PRK10219, PRK10219, superoxide response transcriptional regulator SoxS
MSHQKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTE
RPIFDIAMDLGYVSQQTFSRVFRRQFDRTPSDYRHRL
>gnl|CDD|182315 PRK10220, PRK10220, phnA family protein
MSLPHCPKCNSEYTYEDNGMYICPECAHEWNDAEPAQESDELIVKDANGNLLADGDSVTIVKDLKVKGSS
SMLKIGTKVKNIRLVEGDHNIDCKIDGFGPMKLKSEFVKKN
>gnl|CDD|182316 PRK10222, PRK10222, PTS ascorbate transporter subunit IIB
MIMKMKVDQFLTQSNIDHTVNSCAVGEYKSELSGADIIIASTHIAGEITVTGNKYVVGVRNMLSPADFGP
KLLEVIKEHFPQDVK
>gnl|CDD|236664 PRK10224, PRK10224, pyr operon leader peptide
MVQCVRHFVLPRLKKDAGLPFFFPLITHSQPLNRGAFFCPGVRR
>gnl|CDD|182318 PRK10225, PRK10225, Uxu operon transcriptional regulator
MKSATSAQRPYQEVGAMIRDLIIKTPYNPGERLPPEREIAEMLDVTRTVVREALIMLEIKGLVEVRRGAG
IYVLDSSGSHNTDSPDANVCNDAGPFELLQARQLLESNIAEFAALQATREDIVKMRQALQLEERELASSA
PGSSESGDMQFHLAIAEATHNSMLVELFRQSWQWRENNPMWIQLHSHLDDSLYRKEWLGDHKQILAALIK
KDARAAKLAMWQHLENVKQRLLEFSNVDDIYFDGYLFDSWPLDKVDA
>gnl|CDD|182319 PRK10226, PRK10226, isoaspartyl peptidase; Provisional
MGKAVIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGI
GAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVS
PEIFSTPLRYEQLLAARAEGATVLDHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGD
SPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAALMDYGGLSLAEACERVVMEKLPALGGSGGLIAI
DHEGNVALPFNTEGMYRAWGYAGDTPTTGIYRE
>gnl|CDD|182320 PRK10227, PRK10227, HTH-type transcriptional regulator CueR
MNISDVAKITGLTSKAIRFYEEKGLVTPPMRSENGYRTYTQQHLNELTLLRQARQVGFNLEESGELVNLF
NDPQRHSADVKRRTLEKVAEIERHIEELQSMRDQLLALANACPGDDSADCPIIENLSGCCHHRAG
>gnl|CDD|236665 PRK10229, PRK10229, threonine efflux system; Provisional
MLMLFLTVAMVHIVALMSPGPDFFFVSQTAVSRSRKEAMMGVLGITCGVMVWAGVALLGLHLILEKMAWL
HTIIMVGGGLYLCWMGYQMLRGALKKEDVAAEEPQVELAKSGRSFLKGLLTNLSNPKAIIYFGSVFSLFV
GDNVGAGARWGLFALIIVETLAWFTVVASLFALPQMRRGYQRLAKWIDGFAGALFAGFGIHLIISR
>gnl|CDD|182322 PRK10234, PRK10234, transcriptional regulator GutM
MVSALITVAVIAWCAQLALGGWQISRFNRAFDTLCQQGRVGVGRSSGRFKPRVVVALALDEQQRVVDTLF
MKGLTVFARPQKIPALTGLHLGDLQPDVIFPHDPLSQNALSLALKLKR
>gnl|CDD|182323 PRK10236, PRK10236, acidic protein MsyB
MNVNYLNDSDLDFLQHCSEEQLANFARLLTHNEKGKTRLSSVLMRNELFKSMEGHPEQHRRNWQLIAGEL
QHFGGDSIANKLRGHGKLYRAILLDVSKRLKLKADKEMSTFEIEQQLLEQFLRNTWKKMDEEHKQEFLHA
VDARVNELEELLPLLMKDKLLAKGVSHLLSSQLTRILRTHAAMSVLGHGLLRGAGLGGPVGAALNGVKAV
SGSAYRVTIPAVLQIACLRRMVSATQV
>gnl|CDD|182324 PRK10238, PRK10238, aromatic amino acid transporter AroP
MEGQQHGEQLKRGLKNRHIQLIALGGAIGTGLFLGSASVIQSAGPGIILGYAIAGFIAFLIMRQLGEMVV
EEPVAGSFSHFAYKYWGSFAGFASGWNYWVLYVLVAMAELTAVGKYIQFWYPEIPTWVSAAVFFVVINAI
NLTNVKVFGEMEFWFAIIKVIAVVAMIIFGGWLLFSGNGGPQATVSNLWDQGGFLPHGFTGLVMMMAIIM
FSFGGLELVGITAAEADNPEQSIPKATNQVIYRILIFYIGSLAVLLSLMPWTRVTADTSPFVLIFHELGD
TFVANALNIVVLTAALSVYNSCVYCNSRMLFGLAQQGNAPKALASVDKRGVPVNTILVSALVTALCVLIN
YLAPESAFGLLMALVVSALVINWAMISLAHMKFRRAKQEQGVVTRFPALLYPLGNWICLLFMAAVLVIML
MTPGMAISVYLIPVWLIVLGIGYLFKEKTAKAVKAH
>gnl|CDD|182325 PRK10239, PRK10239, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
MTVAYIAIGSNLASPLEQVNAALKALGDIPESRILAVSSFYRTPPLGPQDQPDYLNAAVALETALAPEEL
LNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPD
GETLREVLHTLAFDKPAKW
>gnl|CDD|182326 PRK10240, PRK10240, (2E,6E)-farnesyl-diphosphate-specific ditrans,polycis-undecaprenyl-diphosphate synthase
MDGNGRWAKKQGKIRAFGHKAGAKSVRRAVSFAANNGIEALTLYAFSSENWNRPAQEVSALMELFVWALD
SEVKSLHRHNVRLRIIGDTSRFNSRLQERIRKSEALTAGNTGLTLNIAANYGGRWDIVQGVRQLAEQVQQ
GNLQPDQIDEEMLNQHICMHELAPVDLVIRTGGEHRISNFLLWQIAYAELYFTDVLWPDFDEQDFEGALN
AFANRERRFGGTEPGDETA
>gnl|CDD|182327 PRK10241, PRK10241, hydroxyacylglutathione hydrolase; Provisional
MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFP
QIVVYGPQETQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEG
TASQMYQSLKKINALPDDTLICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNE
RQINLFLRTEDIDLINVINEETLLQQPEERFAWLRSKKDRF
>gnl|CDD|236666 PRK10244, PRK10244, anti-adapter protein IraP
MKNLIAELLAKLAQKEEESKELTAQVEALELLVTAMLRTMGKNGQQELIEQVEGAINAVSKPDDSVPDSD
TELLLTYVNKLLRHPRQV
>gnl|CDD|182329 PRK10245, adrA, diguanylate cyclase AdrA; Provisional
MNDENFYKKAAAHGEEPPLTPQNEHQRSGLRFARRVRLPRAVGLAGMFLPIASTLVSHPPPGWWWLLLVG
WAFVWPHLAWQIASRAVDPLSREIYNLKTDAVLAGMWVGVMGVNVLPSTAMLMIMCLNLMGAGGPRLFVA
GLVLMVVSCLVTLELTGITVSFNSAPLEWWLSLPVIVIYPLLFAWVSYQTATKLAEHKRRLQVMSTRDGM
TGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVI
GRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMSHYREWLKSADLA
LYKAKNAGRNRTEVAA
>gnl|CDD|182330 PRK10246, PRK10246, exonuclease subunit SbcC; Provisional
MKILSLRLKNLNSLKGEWKIDFTAEPFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLNNVSQSQND
LMTRDTAECLAEVEFEVKGEAYRAFWSQNRARNQPDGNLQAPRVELARCADGKILADKVKDKLELTATLT
GLDYGRFTRSMLLSQGQFAAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGV
ALLTPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQL
AALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNT
WLAEHDRFRQWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQHAE
QRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQEARI
KDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQL
QRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQ
QIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLET
LPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFL
AALLDEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRE
NTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVEDWGYLNSLIGSKEGDKFRKFAQGLTLDNLVWLA
NQQLTRLHGRYLLQRKASEALELEVVDTWQADAVRDTRTLSGGESFLVSLALALALSDLVSHKTRIDSLF
LDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKINGLGYSKLDSAFAVK
>gnl|CDD|182331 PRK10247, PRK10247, putative ABC transporter ATP-binding protein YbbL; Provisional
MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGED
ISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSG
GEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL
QPHAGEMQEARYELA
>gnl|CDD|236667 PRK10249, PRK10249, phenylalanine transporter; Provisional
MKNASTVSEDTASNQEPTLHRGLHNRHIQLIALGGAIGTGLFLGIGPAIQMAGPAVLLGYGVAGIIAFLI
MRQLGEMVVEEPVSGSFAHFAYKYWGPFAGFLSGWNYWVMFVLVGMAELTAAGIYMQYWFPDVPTWIWAA
AFFIIINAVNLVNVRLYGETEFWFALIKVLAIIGMIGFGLWLLFSGHGGEKASIDNLWRYGGFFATGWNG
LILSLAVIMFSFGGLELIGITAAEARDPEKSIPKAVNQVVYRILLFYIGSLVVLLALYPWVEVKSNSSPF
VMIFHNLDSNVVASALNFVILVASLSVYNSGVYSNSRMLFGLSVQGNAPKFLTRVSRRGVPINSLMLSGA
ITSLVVLINYLLPQKAFGLLMALVVATLLLNWIMICLAHLRFRAAMRRQGRETQFKALLYPFGNYLCIAF
LGMILLLMCTMDDMRLSAILLPVWIVFLFVAFKTLRRK
>gnl|CDD|182333 PRK10250, PRK10250, MmcQ/YjbR family DNA-binding protein
MDKQSLHETAKRLALELPFTEHCWPFGPEYDVFKIGGKIFMLSSELRGRPFINLKSDPQKSLLNQQIYPS
IKPGYHMNKKHWISVYPGEDISEALLRDLINDSWNLVVDGLAKRDQKRLRPG
>gnl|CDD|182334 PRK10251, PRK10251, enterobactin synthase subunit EntD
MVDMKTTHTSLPFAGHTLHFVEFDPASFHEQDLLWLPHYAQLQHAGRKRKAEHLAGRIAAVYALREYGYK
CVPAIGELRQPVWPAGVYGSISHCGTTALAVVSRQPIGIDIEEIFSAQTATELTDNIITPAEHERLADCG
LAFPLALTLAFSAKESAFKASEIQTLAGFLDYQIISWNKQQIIIHRENEFFAVHWQIKEKIVITLCQ
>gnl|CDD|236668 PRK10252, entF, enterobactin non-ribosomal peptide synthetase EntF
AEPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNG
EVWQWVDPALTFPLPEIIDLRTQPDPHAAAQALMQADLQQDLRVDSGKPLVFHQLIQLGDNRWYWYQRYH
HLLVDGFSFPAITRRIAAIYCAWLRGEPTPASPFTPFADVVEEYQRYRASEAWQRDAAFWAEQRRQLPPP
ASLSPAPLPGRSASADILRLKLEFTDGAFRQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMR
RLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDEPLFGP
VLNIKVFDYQLDFPGVQAQTHTLATGPVNDLELALFPDEHGGLSIEILANPQRYDEATLIAHAERLKALI
AQFAADPALLCGDVDILLPGEYAQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMR
EQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLI
TTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWM
QNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSML
AAFVASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAA
VRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYR
TGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATGGDARQLVG
YLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTE
TIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEED
ESRRLGFGTILPLREGDGPTLFCFHPASGFAWQFSVLSRYLDPQWSIYGIQSPRPDGPMQTATSLDEVCE
AHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTWPPETQNWREKEANGLDPEVL
AEIDREREAFLAAQQGSLSTELFTTIEGNYADAVRLLTTAHSVPFDGKATLFVAERTLQEGMSPEQAWSP
WIAELDVYRQDCAHVDIISPEAFEKIGPILRATLNE
>gnl|CDD|182336 PRK10253, PRK10253, iron-enterobactin ABC transporter ATP-binding protein
MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH
IQHYASKEVARRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQS
VDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRY
ASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDDPVAGTPLVVPLGRTA
>gnl|CDD|182337 PRK10254, PRK10254, proofreading thioesterase EntH
MIWKRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAG
FLMTRDGQCVVGTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVLG
>gnl|CDD|182338 PRK10255, PRK10255, PTS system N-acetyl glucosamine specific transporter subunits IIABC; Provisional
MNILGFFQRLGRALQLPIAVLPVAALLLRFGQPDLLNVAFIAQAGGAIFDNLALIFAIGVASSWSKDSAG
AAALAGAVGYFVLTKAMVTINPEINMGVLAGIITGLVGGAAYNRWSDIKLPDFLSFFGGKRFVPIATGFF
CLVLAAIFGYVWPPVQHAIHAGGEWIVSAGALGSGIFGFINRLLIPTGLHQVLNTIAWFQIGEFTNAAGT
VFHGDINRFYAGDGTAGMFMSGFFPIMMFGLPGAALAMYFAAPKERRPMVGGMLLSVAVTAFLTGVTEPL
EFLFMFLAPLLYLLHALLTGISLFVATLLGIHAGFSFSAGAIDYALMYNLPAASQNVWMLLVMGVVFFAI
YFVLFSAVIRMFNLKTPGREDKEDEIVTEEANSNTEEGLTQLATNYIAAVGGTDNLKAIDACITRLRLTV
ADSARVNDAMCKRLGASGVVKLNKQTIQVIVGAKAESIGDAMKKVVARGPVAAASAEATPATAAPVAKPQ
AVPNAVSIAELVSPITGDVVALDQVPDEAFASKAVGDGVAVKPTDKIVVSPAAGTIVKIFNTNHAFCLET
EKGAEIVVHMGIDTVALEGKGFKRLVEEGAQVSAGQPILEMDLDYLNANARSMISPVVCSNIDDFSGLII
KAQGHVVAGQTPLYEIKK
>gnl|CDD|182339 PRK10257, PRK10257, putative kinase inhibitor protein; Provisional
MKLISNDLRDGDKLPHRHVFNGMGYDGDNISPHLAWDDVPAGTKSFVVTCYDPDAPTGSGWWHWVVVNLP
ADTRVLPQGFGSGLVALPDGVLQTRTDFGKAGYGGAAPPKGETHRYIFTVHALDVERIDVDEGASGAMVG
FNVHFHSLASASITAMFS
>gnl|CDD|182340 PRK10258, PRK10258, biotin biosynthesis protein BioC; Provisional
MATVNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTAL
DLSPPMLAQARQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTT
LVQGSLPELHQAWQAVDERPHANRFLPPDAIEQALNGWRYQHHIQPITLWFDDALSAMRSLKGIGATHLH
EGRDPRILTRSQLQRLQLAWPQQQGRYPLTYHLFLGVIERD
>gnl|CDD|137782 PRK10259, PRK10259, hypothetical protein; Provisional
MKTINTVVAAMALSTLSFGVFAAEPVTASQAQNMNKIGVVSADGASTLDALEAKLAEKAAAAGASGYSIT
SATNNNKLSGTAVIYK
>gnl|CDD|182341 PRK10260, PRK10260, L,D-transpeptidase; Provisional
MNMKLKTLFAAAFAVVGFCSTASAVTYPLPTDGSRLVGQNQVITIPEGNTQPLEYFAAEYQMGLSNMMEA
NPGVDTFLPKGGTVLNIPQQLILPDTVHEGIVINSAEMRLYYYPKGTNTVIVLPIGIGQLGKDTPINWTT
KVERKKAGPTWTPTAKMHAEYRAAGEPLPAVVPAGPDNPMGLYALYIGRLYAIHGTNANFGIGLRVSHGC
VRLRNEDIKFLFEKVPVGTRVQFIDEPVKATTEPDGSRYIEVHNPLSTTEAQFEGQEIVPITLTKSVQTV
TGQPDVDQVVLDEAIKNRSGMPVRLN
>gnl|CDD|182342 PRK10261, PRK10261, glutathione transporter ATP-binding protein; Provisional
MPHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAG
GLVQCDKMLLRRRSRQVIELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASRE
EAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQL
IKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAAVPQLGAMKG
LDYPRRFPLISLEHPAKQEPPIEQDTVVDGEPILQVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPG
ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTV
GDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA
VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYT
RKLMAAVPVADPSRQRPQRVLLSDDLPSNIHLRGEEVAAVSLQCVGPGHYVAQPQSEYAFMRR
>gnl|CDD|182343 PRK10262, PRK10262, thioredoxin reductase; Provisional
MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMH
EHATKFETEIIFDHINKVDLQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCD
GFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEE
VTGDQMGVTGVRLRDTQNSDNIESLDVAGLFVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIP
GVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADAK
>gnl|CDD|236669 PRK10263, PRK10263, DNA translocase FtsK; Provisional
MSQEYTEDKEVTLTKLSSGRRLLEALLILIVLFAVWLMAALLSFNPSDPSWSQTAWHEPIHNLGGMPGAW
LADTLFFIFGVMAYTIPVIIVGGCWFAWRHQSSDEYIDYFAVSLRIIGVLALILTSCGLAAINADDIWYF
ASGGVIGSLLSTTLQPLLHSSGGTIALLCVWAAGLTLFTGWSWVTIAEKLGGWILNILTFASNRTRRDDT
WVDEDEYEDDEEYEDENHGKQHESRRARILRGALARRKRLAEKFINPMGRQTDAALFSGKRMDDDEEITY
TARGVAADPDDVLFSGNRATQPEYDEYDPLLNGAPITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVD
VPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPY
YAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVV
EPEPVVEETKPARPPLYYFEEVEEKRAREREQLAAWYQPIPEPVKEPEPIKSSLKAPSVAAVPPVEAAAA
VSPLASGVKKATLATGAAATVAAPVFSLANSGGPRPQVKEGIGPQLPRPKRIRVPTRRELASYGIKLPSQ
RAAEEKAREAQRNQYDSGDQYNDDEIDAMQQDELARQFAQTQQQRYGEQYQHDVPVNAEDADAAAEAELA
RQFAQTQQQRYSGEQPAGANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQ
PVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQ
PQDTLLHPLLMRNGDSRPLHKPTTPLPSLDLLTPPPSEVEPVDTFALEQMARLVEARLADFRIKADVVNY
SPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDN
AKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDP
KMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIAEADRMMRPIPD
PYWKPGDSMDAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVI
TGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDW
KARGRPQYVDGITSDSESEGGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQ
MEAQGIVSEQGHNGNREVLAPPPFD
>gnl|CDD|182345 PRK10264, PRK10264, hydrogenase 1 maturation protease; Provisional
MSEQRVVVMGLGNLLWADEGFGVRVAERLYAHYHWPEYVEIVDGGTQGLNLLGYVESASHLLILDAIDYG
LEPGTLRTYAGERIPAYLSAKKMSLHQNSFSEVLALADIRGHLPAHIALVGLQPAMLDDYGGSLSELARE
QLPAAEQAALAQLAAWGIVPQPANESRCLNYDCLSMENYEGVRLRQYRMTLEEQG
>gnl|CDD|182346 PRK10265, PRK10265, chaperone modulator CbpM
MANVTVTFTITEFCLHTGVSEEELNEIVGLGVIEPREIQETTWVFDDHAAIVVQRAVRLRHELALDWPGI
AVALTLLDEIAHLKQENRLLRQRLSRFVAHP
>gnl|CDD|182347 PRK10266, PRK10266, curved DNA-binding protein
MELKDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQLWQ
HRNDPQFNRQFQHGDGQSFNAEDFDDIFSSIFGQHARQSRQRPAARGHDIEIEVAVFLEETLTEHKRTIS
YNLPVYNAFGMIEQEIPKTLNVKIPAGVGNGQRIRLKGQGTPGENGGPNGDLWLVIHIAPHPLFDIVGQD
LEIVVPLAPWEAALGAKVTVPTLKESILLTIPPGSQAGQRLRVKGKGLVSKKQTGDLYAVLKIVMPPKPD
EKTAALWQQLADAQSSFDPRKDWGKA
>gnl|CDD|182348 PRK10270, PRK10270, putative aminodeoxychorismate lyase; Provisional
MKKVLLIILLLLVVLGIAAGVGVWKVRHLADSKLLIKEETIFTLKPGTGRLALGEQLYADKIINRPRVFQ
WLLRIEPDLSHFKAGTYRFTPQMTVREMLKLLESGKEAQFPLRLVEGMRLSDYLKQLREAPYIKHTLSDD
KYATVAQALELENPEWIEGWFWPDTWMYTANTTDVALLKRAHKKMVKAVDSAWEGRADGLPYKDKNQLVT
MASIIEKETAVASERDQVASVFINRLRIGMRLQTDPTVIYGMGERYNGKLSRADLETPTAYNTYTITGLP
PGPIATPGEASLKAAAHPAKTPYLYFVADGKGGHTFNTNLASHNRSVQDYLKVLKEKNAQ
>gnl|CDD|182349 PRK10271, thiK, thiamine kinase; Provisional
MAVDYLPGEVKSYLPDTNELAGLLYHLHQQPRFGWRITLLPLLEQYWQQSDPARRTPFWLRMLKRLRKAG
EPRPLRLAPLHMDVHAGNLVHSASGLRLIDWEYAGDGDIALELAAVWVENTEQHRQLVNDYATRAKIDAA
QLWRQVRRWFPWVLMLKAGWFEYRWRQTGDQQFIRLADDTWRQLLIKQ
>gnl|CDD|182350 PRK10276, PRK10276, translesion error-prone DNA polymerase V autoproteolytic subunit
MLFIKPAELREIVTFPLFSDLVQCGFPSPAADYVEQRIDLNELLIQHPSATYFVKASGDSMIDAGISDGD
LLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTVQLIPMNSAYSPITISSEDTLDVFGVVTHIVKAMR
>gnl|CDD|182351 PRK10278, PRK10278, SirB family protein
MTSFSTLLSVHLISVALSVGLFVLRFWWRYQKHPLAFARWTRIVPPVVDTLLLLSGIGLMAKTHILPFTG
QGQWLTEKLFGVIIYIVLGFIALDYRRMRSQQARFIAFPLALVVLYIIIKLATTKIPLLG
>gnl|CDD|182352 PRK10279, PRK10279, patatin-like phospholipase RssA
MRKIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALEDWVTSFSYWDV
LRLMDLSWQRGGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMP
GLMAPVAHNGYWLVDGAVVNPVPVSLTRALGADIVIAVDLQHDAHLMQQDLLSFNVSEENSENGDSLPWH
ARLKERLGSITTRRAVTAPTAMEIMTTSIQVLENRLKRNRMAGDPPDILIQPVCPQISTLDFHRAHAAIA
AGQLAVEKKMDELLPLVRTN
>gnl|CDD|182353 PRK10280, PRK10280, peptidyl-dipeptidase Dcp
MTTMNPFLVQSTLPYLAPHFDQIADHHYRPAFDEGVRQKRAEIAAIALNPQAPDFNNTILALEQSGELLT
RVTSVFFAMTAAHTNDELQRLDEQFSAELAELANDIYLNGELFARVDAVWQQRESLGLDSESIRLVEVIH
QRFVLAGAKLAQADKAKLKVLNTEAATLTSQFNQRLLAANKSGGLVVNDIHQLAGLSEQEIALAAEAARE
KGLDNRWLIPLLNTTQQPALAELRDRQTRENLFAAGWTRAEKGDANDTRAIIQRLVEIRAQQAKLLGFPH
YAAWKIADQMAKTPEAALNFMREIVPAARQRASDELASIQAVIDKQQGGFSAQAWDWAFYAEQVRREKYA
LDEAQLKPYFELNTVLNEGVFWTANQLFGIKFVERFDIPVYHPDVRVWEIFDHNGVGLALFYGDFFARDS
KSGGAWMGNFVEQSTLNETRPVIYNVCNYQKPAAGQPALLLWDDVITLFHEFGHTLHGLFARQRYATLSG
TNTPRDFVEFPSQINEHWASHPQVFARYARHYQSGEAMPDELQEKMRNASLFNKGYDMSELLSAALLDMR
WHCLEENEAMQDVDDFELRALVAENLDLPAVPPRYRSSYFAHIFGGGYAAGYYAYLWTQMLADDGYQWFV
EQGGLTRENGQRFREAILSRGNSTDLERLYRQWRGHAPQIMPMLQHRGLNI
>gnl|CDD|182354 PRK10281, PRK10281, PhzF family isomerase
MKPQIYHVDAFTSQPFRGNSAGVVLNADGLSEAQMQLIARELNHSETAFLLSSDDSSYDVRVRYFTPTVE
VPICGHATVAAHYVRATVLGLGNCTVWQTTLAGILPVDIEKENDDYRISMTQGTPEFEPPLEGETRAAII
NALGLTEDDILPGLPIQVASTGHSKVMIPLKPEVDLDALSPNLAALTAISKQIGCNGFFPFQIRPGKNEI
LTDGRMFAPAIGIVEDPVTGNANGPMGAYLVHHNLLPHDGKVLRFKGHQGRALGRDGTIEVTVTIRDNQP
EKVTISGQAVILFHAEWAI
>gnl|CDD|182355 PRK10286, PRK10286, methylated-DNA--[protein]-cysteine S-methyltransferase
MLRLLEEKIATPLGPLWVICDEQFRLRAVEWEEYSERMVQLLDIHYRKEGYERISATNPGGLSDKLRDYF
AGNLSIIDTLPTATGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCH
RVIGRNGTMTGYAGGVQRKEWLLRHEGYLLL
>gnl|CDD|182356 PRK10287, PRK10287, thiosulfate:cyanide sulfurtransferase; Provisional
MFKKGLLALALVFSLPVFAAEHWIDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKNDTVKLYCNAG
RQSGQAKEILSEMGYTHAENAGGLKDIAMPKVKG
>gnl|CDD|182357 PRK10290, PRK10290, superoxide dismutase [Cu-Zn] SodC2
MKRFSLAILALVVCTGAQAASEKVEMNLVTSQGVGQSIGSVTITETDKGLEFSPDLKALPPGEHGFHIHA
KGSCQPATKDGKASAAEAAGGHLDPQNTGKHEGPEGAGHLGDLPALVVNNDGKATDPVIAPRLKSLDEVK
DKALMVHVGGDNMSDQPKPLGGGGERYACGVIK
>gnl|CDD|182358 PRK10291, PRK10291, glyoxalase I; Provisional
MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIA
LSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN
>gnl|CDD|182359 PRK10292, PRK10292, fumarate hydratase FumD
MGNRTKEDELYREMCRVVGKVVLEMRDLGQEPKHIVIAGVLRTALANKRIQRSELEKQAMETVINALVK
>gnl|CDD|182360 PRK10293, PRK10293, 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
MIWKRKITLEALNAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAG
YLCTEGEQKVVGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL
>gnl|CDD|182361 PRK10294, PRK10294, 6-phosphofructokinase 2; Provisional
MVRIYTLTLAPSLDSATITPQIYPEGKLRCSAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLV
SLLADENVPVATVEAKDWTRQNLHVHVEASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSL
PPGVKLEKLTQLISAAQKQGIRCIIDSSGDALSAALAIGNIELVKPNQKELSALVNRDLTQPDDVRKAAQ
ELVNSGKAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGV
AAGSAATLNQGTRLCSHDDTQKIYAYLSR
>gnl|CDD|182362 PRK10296, PRK10296, DNA-binding transcriptional regulator ChbR; Provisional
MQPVINAMEIATVREQQLFNGKNFHVFIYNKTESVSGLHQHDYYEFTLVLTGRYYQEINGKRVLLERGDF
VFIPLGSHHQSFYEFGATRILNVGISKRFFEQHYLPLLPYCFVASQVYRTNNAFLTYIETVISSLNFRET
GLDEFVELVTFYVINRLRHYREEQVIDDIPQWLKATVEKMHDKEQFSESALENMVRLSGKSQEYLTRATR
RYYGKTPMQIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTPGSYRKKLTEFN
>gnl|CDD|182363 PRK10297, PRK10297, PTS system N,N'-diacetylchitobiose-specific transporter subunit IIC; Provisional
MSNVIASLEKVLLPFAVKIGKQPHVNAIKNGFIRLMPLTLAGAMFVLINNVFLSFGEGSFFYSLGIRLDA
STIETLNGLKGIGGNVYNGTLGIMSLMAPFFIGMALAEERKVDALAAGLLSVAAFMTVTPYSVGEAYAVG
ANWLGGANIISGIIIGLVVAEMFTFIVRRNWVIKLPDSVPASVSRSFSALIPGFIILSIMGIIAWALNTW
GTNFHQIIMDTISTPLASLGSVVGWAYVIFVPLLWFFGIHGALALTALDSGIMTPWALENIATYQQYGSV
EAALAAGKTFHIWAKPMLDSYIFLGGSGATLGLIIAIFIASRRADYRQVAKLALPSGIFQINEPILFGLP
IIMNPVMFIPFILVQPILAAITLVAYYLGIIPPITNIAPWTMPTGLGAFFNTNGSVAALLVALFNLGIAT
LIYLPFVVVANKAQNAIDKEESEEDIANALKF
>gnl|CDD|182364 PRK10299, PRK10299, PhoP/PhoQ regulator MgrB
MKKFRWVVLVVVVLACLLLWAQVFNMMCDQDVQFFSGICAINKFIPW
>gnl|CDD|182365 PRK10301, PRK10301, CopC domain-containing protein YobA
MASTARSLRYALAILTTSLVTPAVWAHAHLTHQYPAANAQVTAAPQALTLNFSEGIEPGFSGATITGPKQ
ENIKTLPAKRNEQDQKQLIVPLADSLKPGTYTVDWHVVSVDGHKTKGHYTFSVK
>gnl|CDD|182366 PRK10302, PRK10302, hypothetical protein; Provisional
MIYIGLPQWQHPKWVRLGITSLEDYARHFNCVEGNTTLYALPKPEIVLRWRDMTTDDFRFCFKFPATISH
QAALRHCDDLVQEFFTRLAPLADRIGQYWLQLPAAFGPRELPALWQFLDALPAGFTYGVEVRHPEFFAKG
EAEQALNRGLHQRGVNRVILDSRPVHAARPHSEAIRDAQRKKPKVPVHAVVTADNPLVRFIGSDDMAQNL
ELFQVWLQKLPQWHQTTTPYLFIHTPDIAQAPELVQTLWPDLRKALPEIGPAPDWPQQSSLF
>gnl|CDD|182367 PRK10304, PRK10304, non-heme ferritin
MLKPEMIEKLNEQMNLELYSSLLYQQMSAWCSYHTFEGAAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRI
NTVESPFAEYSSLDELFQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQWYVSEQHEEEKLFKSIIDK
LSLAGKSGEGLYFIDKELSTLDTQN
>gnl|CDD|182368 PRK10306, PRK10306, zinc/cadmium-binding protein; Provisional
MAIRLHKLAVALGVLLVSAPAFAHGHHSHGKPLTEVEQKAANGVFDDANVQDRTLSDWDGVWQSVYPYLQ
SGKLDPVFQKKAKKDKTKTFEEIKAYYRKGYATDVEMIGIENGIVEFHRGNEVTSCKYDYDGYKILTYAS
GKKGVRYLFECKDAESKAPKYVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPTYYPYQLSSEEVV
DEMLHH
>gnl|CDD|236670 PRK10307, PRK10307, colanic acid biosynthesis glycosyltransferase WcaI
MKILVYGINYAPELTGIGKYTGEMAEWLAARGHEVRVITAPPYYPQWRVGEGYSAWRYRRESEGGVTVWR
CPLYVPKQPSGLKRLLHLGSFALSSFFPLLAQRRWRPDRVIGVVPTLFCAPGARLLARLSGARTWLHIQD
YEVDAAFGLGLLKGGKVARLATAFERSLLRRFDNVSTISRSMMNKAREKGVAAEKVIFFPNWSEVARFQP
VADADVDALRAQLGLPDGKKIVLYSGNIGEKQGLELVIDAARRLRDRPDLIFVICGQGGGKARLEKMAQC
RGLPNVHFLPLQPYDRLPALLKMADCHLLPQKAGAADLVLPSKLTNMLASGRNVVATAEPGTELGQLVEG
IGVCVEPESVEALVAAIAALARQALLRPKLGTVAREYAERTLDKENVLRQFIADIRGLVAER
>gnl|CDD|236671 PRK10308, PRK10308, 3-methyl-adenine DNA glycosylase II; Provisional
MYTLNWQPPYDWSWMLGFLAARAVSGVETVAEGYYARSLAVGEHRGVVTVIPDIARHTLHINLSAGLEPV
AAECLAKMSRLFDLQCNPQIVNGALGKLGAARPGLRLPGSVDAFEQGVRAILGQLVSVAMAAKLTAKVAQ
LYGERLDDFPEYVCFPTPERLAAADPQALKALGMPLKRAEALIHLANAALEGTLPLTIPGDVEQAMKTLQ
TFPGIGRWTANYFALRGWQAKDVFLPDDYLIKQRFPGMTPAQIRRYAERWKPWRSYALLHIWYTEGWQPD
EDS
>gnl|CDD|182371 PRK10309, PRK10309, galactitol-1-phosphate 5-dehydrogenase
MKSVVNDTDGIVRVAESPIPEIKHQDDVLVKVASSGLCGSDIPRIFKNGAHYYPITLGHEFSGYVEAVGS
GVDDLHPGDAVACVPLLPCFTCPECLRGFYSLCAKYDFIGSRRDGGNAEYIVVKRKNLFALPTDMPIEDG
AFIEPITVGLHAFHLAQGCEGKNVIIIGAGTIGLLAIQCAVALGAKSVTAIDINSEKLALAKSLGAMQTF
NSREMSAPQIQSVLRELRFDQLILETAGVPQTVELAIEIAGPRAQLALVGTLHHDLHLTSATFGKILRKE
LTVIGSWMNYSSPWPGQEWETASRLLTERKLSLEPLIAHRGSFESFAQAVRDLAGNPMPGKVLLQIP
>gnl|CDD|182372 PRK10310, PRK10310, PTS galactitol transporter subunit IIB
MKRKIIVACGGAVATSTMAAEEIKELCQSHNIPVELIQCRVNEIETYMDGVHLICTTARVDRSFGDIPLV
HGMPFVSGVGIEALQNKILTILQG
>gnl|CDD|182373 PRK10314, PRK10314, GNAT family N-acetyltransferase
MIEWQDLHHSELSVSQLYALLQLRCAVFVVEQNCPYQDIDGDDLTGDNRHILGWKNDELVAYARILKSDD
DLEPVVIGRVIVSEALRGEKVGQQLMSKTLESCTRHWPDKPVYLGAQAHLQNFYQSFGFIPVTEVYEEDG
IPHIGMAREVIQA
>gnl|CDD|182374 PRK10316, PRK10316, hypothetical protein; Provisional
MKRLIMATMVTAVLASSTVWAADNAAAQQQTAATQQTQKTTAAAERISEQGLYAMRDVQVARLALFHGDP
EKAKELTNQASALLSDDSTDWAKFAKPDKKAPVNGDQYIVINASVGISEDYVATPEKEAAIKIANEKMAK
GDKKGAMEELRLAGVGVMENQYLMPLKQTRNAVADAQKLLDKGKYYEANLALKGAEDGIIVDSEALFVN
>gnl|CDD|236672 PRK10318, PRK10318, hypothetical protein; Provisional
KKILCLLITLLFTLPAYAKLTAHEEARINAMLEGLAQKKDCTFVRNGDEHTCKEAVSHLRLKLGNTRNRI
DTAEQFIDKVASSSSISGKPYIVKCPGKSDENAQPWLHALIAETDKTVPAQ
>gnl|CDD|182376 PRK10319, PRK10319, N-acetylmuramoyl-L-alanine amidase AmiA
MSTFKPLKTLTSRRQVLKAGLAALTLSGMSQAIAKEEPLKTSNGHSKPKAKKSGGKRVVMLDPGHGGIDT
GAIGRNGSKEKHVVLAIAKNVRSILRNHGIDARLTRSGDTFIPLYDRVEIAHKHGADLFMSIHADGFTNP
KAAGASVFALSNRGASSAMAKYLSERENRADEVAGKKATDKDHLLQQVLFDLVQTDTIKNSLTLGSHILK
KIKPVHKLHSRNTEQAAFVVLKSPSIPSVLVETSFITNPEEERLLGTTAFRQKIATAIAEGIISYFHWFD
NQKAHSK
>gnl|CDD|182377 PRK10323, PRK10323, cysteine/O-acetylserine transporter
MTPTLLSAFWTYTLITAMTPGPNNILALSSATSHGFRQSTRVLAGMSLGFLIVMLLCAGISFSLAVIDPA
AVHLLSWAGAAYIVWLAWKIATSPTKEDGLQAKPISFWASFALQFVNVKIILYGITALSTFVLPQTQALS
WVVGVSVLLAMIGTFGNVCWALAGHLFQRLFRQYGRQLNIVLALLLVYCAVRIFY
>gnl|CDD|182378 PRK10324, PRK10324, ribosome-associated translation inhibitor RaiA
MTMNITSKQMEITPAIRQHVADRLAKLEKWQTHLINPHIILSKEPQGFVADATINTPNGVLVASGKHEDM
YTAINELINKLERQLNKLQHKGEARRAATSVKDANFVEEVEEE
>gnl|CDD|182379 PRK10325, PRK10325, heat shock protein GrpE; Provisional
MSSKEQKTPEGQAPEEIIMDQHEEIEAVEPEASAEQVDPRDEKIANLEAQLAEAQTRERDGILRVKAEME
NLRRRTELDIEKAHKFALEKFINELLPVIDSLDRALEVADKANPDMSAMVEGIELTLKSMLDVVRKFGVE
VIAETNVPLDPNVHQAIAMVESDDVAPGNVLGIMQKGYTLNGRTIRAAMVTVAKAKA
>gnl|CDD|182380 PRK10328, PRK10328, DNA-binding protein StpA
MSVMLQSLNNIRTLRAMAREFSIDVLEEMLEKFRVVTKERREEEEQQQRELAERQEKINTWLELMKADGI
NPEELLGNSSAAAPRAGKKRQPRPAKYRFTDVNGETKTWTGQGRTPKPIAQALAEGKSLDDFLI
>gnl|CDD|182381 PRK10329, PRK10329, glutaredoxin-like protein NrdH
MRITIYTRNDCVQCHATKRAMESRGFDFEMINVDRVPEAAETLRAQGFRQLPVVIAGDLSWSGFRPDMIN
RLHPAPHAASA
>gnl|CDD|182382 PRK10330, PRK10330, electron transport protein HydN
MNRFIIADASKCIGCRTCEVACVVSHQENQDCASLTPETFLPRIHVIKGVNVSTATVCRQCEDAPCANVC
PNGAISRDKGFVHVMQERCIGCKTCVVACPYGAMEVVVRPVIRNSGAGLNVRAEKAEANKCDLCNHREDG
PACMAACPTHALICVDRNKLEQLSAEKRRRAALDSTASLMF
>gnl|CDD|182383 PRK10331, PRK10331, L-fuculokinase; Provisional
QDVILVLDCGATNVRAIAVDRQGKIVARASTPNASDIAAENSDWHQWSLDAILQRFADCCRQINSELTEC
HIRGITVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGAFSFNTLYKLVW
LKENHPQLLEQAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVE
AGEQIGTLQPSAAALLGLPVGIPVISAGHDTQFALFGSGAGQNQPVLSSGTWEILMVRSAQVDTSLLSQY
AGSTCELDSQSGLYNPGMQWLASGVLEWVRKLFWTAETPYQTMIEEARAIPPGADGVKMQCDLLACQNAG
WQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVL
DDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRYFYPQTEPEFIEEV
>gnl|CDD|182384 PRK10332, PRK10332, prepilin-type N-terminal cleavage/methylation domain-containing protein
MSASLKNQRGFSLPEVLLAMVLMVMIVTALSGYQRTLMNSFASRNQYRQLWRHAWQQTQLRAISPPANWQ
VNRMQTSQAGCVSISVTLVSPGGRQGQMTRLHCPNRQ
>gnl|CDD|182385 PRK10333, PRK10333, 5-formyltetrahydrofolate cyclo-ligase family protein; Provisional
MIRQRRRALTPEQQQEMGQQAATRMMTYPPVVMAHTVAVFLSFDGELDTQPLIEQLWRAGKRVYLPVLHP
FSAGNLLFLNYHPQSELVMNRLKIHEPKLDVRDVLPLSRLDVLITPLVAFDEYGQRLGMGGGFYDRTLQN
WQHYKTQPVGYAHDCQLVEKLPVEEWDIPLPAVVTPSKVWEW
>gnl|CDD|182386 PRK10334, PRK10334, small-conductance mechanosensitive channel MscS
MEDLNVVDSINGAGSWLVANQALLLSYAVNIVAALAIIIVGLIIARMISNAVNRLMISRKIDATVADFLS
ALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAAGVLLVMFRPFRAGEYVDLGG
VAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFSREPVRRNEFIIGVAYDSDIDQVKQILTNIIQ
SEDRILKDREMTVRLNELGASSINFVVRVWSNSGDLQNVYWDVLERIKREFDAAGISFPYPQMDVNFKRV
KEDKAA
>gnl|CDD|182387 PRK10336, PRK10336, two-component system response regulator QseB
MRILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKG
QREPVLILTARDALAERVEGLRLGADDYLCKPFALIEVAARLEALMRRTNGQASNELRHGNVMLDPGKRI
ATLAGEPLTLKPKEFALLELLMRNAGRVLPRKLIEEKLYTWDEEVTSNAVEVHVHHLRRKLGSDFIRTVH
GIGYTLGEK
>gnl|CDD|182388 PRK10337, PRK10337, sensor protein QseC; Provisional
MKFTQRLSLRVRLTLIFLILASITWLLSSFVAWKQTTDNVDELFDTQQMLFAKRLSTLDLNELNAPDRMA
QTPKKLKHGHVDDDALAFAIFTRDGKMVLNDGDNGEDIPYSYQREGFADGQLVGDDDLWRFVWLTSPDGK
YRIVVGQEWEYREDMALAIVAGQLIPWLVALPIMLIILMVLLGRELAPLKKLALALRMRDPDSETPLNAT
GVPSEVRPLVEALNQLFARTHAMMVRERRFTSDAAHELRSPLAALKVQTEVAQLSDDDPQARKKALLQLH
AGIDRATRLVDQLLTLSRLDSLDNLQDVAEIPLEDLLQSAVMDIYHTAQQAGIDVRLTLNAHPVIRTGQP
LLLSLLVRNLLDNAIRYSPQGSVVDVTLNARNFTVRDNGPGVTPEALARIGERFYRPPGQEATGSGLGLS
IVRRIAKLHGMNVSFGNAPEGGFEAKVSW
>gnl|CDD|182389 PRK10339, PRK10339, DNA-binding transcriptional repressor EbgR; Provisional
MATLKDIAIEAGVSLATVSRVLNDDPTLNVKEETKHRILEIAEKLEYKTSSARKLQTGAVNQHHILAIYS
YQQELEINDPYYLAIRHGIETQCEKLGIELTNCYEHSGLPDIKNVTGILIVGKPTPALRAAASALTDNIC
FIDFHEPGSGYDAVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKADIREVAFAEYGRLKQVVREED
IWRGGFSSSSGYELAKQMLAREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFP
PLSTVRIHSEMMGSQGVNLLYEKARDGRALPLLVFVPSKLKLRGTTR
>gnl|CDD|236673 PRK10340, ebgA, cryptic beta-D-galactosidase subunit alpha; Reviewed
MNRWENIQLTHENRLAPRAYFFSYDSVAQARTFARETSSLFLLLSGQWNFHFFDHPLYVPEAFTSELMSD
WGHITVPAMWQMEGHGKLQYTDEGFPFPIDVPFVPSDNPTGAYQRTFTLSDGWQGKQTIIKFDGVETYFE
VYVNGQYVGFSKGSRLTAEFDISAMVKTGDNLLCVRVMQWADSTYLEDQDMWWLAGIFRDVYLVGKPLTH
INDFTVRTDFDEDYCDATLSCEVVLENLAASPVVTTLEYTLFDGERVVHSSAIDHLAIEKLTSASFAFTV
EQPQQWSAESPYLYHLVMTLKDANGNVLEVVPQRVGFRDIKVRDGLFWINNRYVKLHGVNRHDNDHRKGR
AVGMDRVEKDIQLMKQHNINSVRTAHYPNDPRFYELCDIYGLFVMAETDVESHGFANVGDISRITDDPQW
EKVYVDRIVRHIHAQKNHPSIIIWSLGNESGYGCNIRAMYHAAKALDDTRLVHYEEDRDAEVVDVISTMY
TRVELMNEFGEYPHPKPRILCEYAHAMGNGPGGLTEYQNVFYKHDCIQGHYVWEWCDHGIQAQDDNGNVW
YKYGGDYGDYPNNYNFCIDGLIYPDQTPGPGLKEYKQVIAPVKIHALDLTRGELKVENKLWFTNLDDYTL
HAEVRAEGETLASGQIKLRDVAPNSEAPLQITLPQLDAREAFLNITVTKDSRTRYSEAGHSIATYQFPLK
ENTAQPVPFAPNNARPLTLEEDRLSCTVRGYNFAITFSKVSGKLTSWQVNGESLLTREPKINFFKPMIDN
HKQEYEGLWQPNHLQIMQEHLRDFAVEQSDGEVLIISRTVIAPPVFDFGMRCTYIYRIAADGQVNVALSG
ERYGDYPHMIPCIGFTMGINGEYDQVAYYGRGPGENYADSQQANLIDIYRSTVDAMFENYPFPQNNGNRQ
HVRWTALTNRHGNGLLVVPQRPINFSAWHYTQENIHAAQHTNELQKSDYITLNLDHQLLGLGSNSWGSEV
LDSYRVWFRDFSYGFTLLPVSGGEATAQSLASYEFGAGFFS
>gnl|CDD|182391 PRK10341, PRK10341, transcriptional regulator TdcA
MSTILLPKTQHLVVFQEVIRSGSIGSAAKELGLTQPAVSKIINDIEDYFGVELIVRKNTGVTLTPAGQVL
LSRSESITREMKNMVNEINGMSSEAVVDVSFGFPSLIGFTFMSDMINKFKEVFPKAQVSMYEAQLSSFLP
AIRDGRLDFAIGTLSNEMKLQDLHVEPLFESEFVLVASKSRTCTGTTTLESLKNEQWVLPQTNMGYYSEL
LTTLQRNGISIENIVKTDSVVTIYNLVLNADFLTVIPCDMTSPFGSNQFITIPIEETLPVAQYAAVWSKN
YRIKKAASVLVELAKEYSSYNGCRRRQLIEVG
>gnl|CDD|182392 PRK10342, PRK10342, glycerate kinase I; Provisional
MKIVIAPDSYKESLSASEVAQAIEKGFREIFPDAQYVSVPVADGGEGTVEAMIAATQGSERHAWVTGPLG
EKVNASWGISGDGKTAFIEMAAASGLELVPAEKRDPLVTTSRGTGELILQALESGATNIIIGIGGSATND
GGAGMVQALGAKLCDANGNEIGFGGGSLNTLNDIDISGLDPRLKDCVIRVACDVTNPLVGDNGASRIFGP
QKGASEAMIVELDNNLSHYADVIKKALHVDVKDVPGAGAAGGMGAALMAFLGAELKSGIEIVTTALNLEE
HIHDCTLVITGEGRIDSQSIHGKVPIGVANVAKKYHKPVIGIAGSLTDDVGVVHQHGIDAVFSVLTSIGT
LDEAFRGAYDNICRASRNIAATLAIGMRNAG
>gnl|CDD|182393 PRK10343, PRK10343, ribosome assembly RNA-binding protein YhbY
MNLSTKQKQHLKGLAHPLKPVVLLGSNGLTEGVLAEIEQALEHHELIKVKIATEDRETKTLIVEAIVRET
GACNVQVIGKTLVLYRPTKERKISLPR
>gnl|CDD|182394 PRK10344, PRK10344, DNA-binding transcriptional regulator SfsB
MESNFIDWHPADIIAGLRKKGTSMAAESRRNGLSSSTLANALSRPWPKGEMIIAKALGTDPWVIWPSRYH
DPQTHEFIDRTQLMRSYTKPKK
>gnl|CDD|182395 PRK10345, PRK10345, PhoP regulatory network protein YrbL
MIRLSEQSPLGTGRHRKCYAHPEDAQRCIKIVYHRGDGGDKEIRRELKYYAHLSRRLIDWSGIPRYYGTV
ETDCGTGYVYDVIADFDGKPSITLTEFAEQCRYEEDVAQLRQLLKKLKRYLLDNRIVTMELKPQNILCQR
ISESEVIPVVCDNIGESTFIPLATWSKWCCRRKQERKWKRFIAQPALAIALQKDLQPRESKTLALTSREA
>gnl|CDD|182396 PRK10347, PRK10347, putative adenosine monophosphate-protein transferase Fic
MSDKFGEGRDPYLYPGLDVMRNRLNIHQAQRLEQAAYEMTALRAATIELGPLVRGLPHLCAIHRQLYQDI
FDWAGQLREVDIYQGDTPFCHFAYIEKEGNALMQDLEEEGYLVGLEKAKFVERLAHYYCEINVLHPFRVG
SGLAQRIFFEQLAIHAGYQLSWQGIEKEAWNQANQSGAMGDLTALQMIFSKVVSEAGESE
>gnl|CDD|182397 PRK10348, PRK10348, ribosome-associated heat shock protein Hsp15; Provisional
MKEKPAVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPSKIVELNATLTLRQGNDERTVIVKA
ITEQRRPASEAALLYEETAESVEKREKMALARKLNALTMPHPDRRPDKKERRDLLRFKHGDSE
>gnl|CDD|137836 PRK10349, PRK10349, pimeloyl-ACP methyl ester esterase BioH
MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQ
QAPDKAIWLGWSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTV
ERFLALQTMGTETARQDARALKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLV
PRKVVPMLDKLWPHSESYIFAKAAHAPFISHPAEFCHLLVALKQRV
>gnl|CDD|182398 PRK10350, PRK10350, DUF2756 family protein
MKRLLLLTALLPFVGFAQPINTLNNPNQPGYQIPSQQRMQTQMQTQQIQQKGMLNQQLKTQTRLQQQHLQ
NQINNNSQRVQQGQPGNNPARQQMLPNTNGGMLNSNRNPDSSLNQQHMLPERRNGDMLNQPSTPQPDIPL
KTIGP
>gnl|CDD|182399 PRK10351, PRK10351, 4'-phosphopantetheinyl transferase AcpT
VSTLSAAPLPPALREQAPQGPRRARWLAGRVLLSHALSPLPEIIYGEQGKPAFAPETPLWFNLSHSGDDI
ALLLSDEGEVGCDIEVIRPRANWRSLANAVFSLGEHAEMDAVHPEQQLEAFWRIWTRKEAIVKQRGGSAW
QIVSVDSTLPSALSVSHCQLENLSLAVCTPTPFTLTADSVQWLDSVN
>gnl|CDD|182400 PRK10352, PRK10352, nickel transporter permease NikB; Provisional
MLRYILRRLLLLIPMLLAASVIIFLMLRLGTGDPALDYLRLSNLPPTPEMLASTRTMLGLDQPLYVQYGT
WLWKALHLDFGISFATQRPVLDDLLNFLPATLELAGAALVLILLTSVPLGIWAARHRDRLPDFAVRFIAF
LGVSMPNFWLAFLLVMAFSVYLQWLPAMGYGGWQHIILPAVSIAFMSLAINARLLRASMLEVAGQRHVTW
ARLRGLSERQVERRHILRNASLPMITAVGMHIGELIGGTMIIENIFAWPGVGRYAVSAIFNRDYPVIQCF
TLMMVVVFVVCNLIVDLLNAALDPRIRRHEGAHA
>gnl|CDD|182401 PRK10353, PRK10353, DNA-3-methyladenine glycosylase I
MERCGWVSQDPLYIAYHDNEWGVPETDSKKLFEMICLEGQQAGLSWITVLKKRENYRACFHQFDPVKVAA
MQEEDVERLVQDAGIIRHRGKIQAIIGNARAYLQMEQNGEPFADFVWSFVNHQPQVTQATTLSEIPTSTP
ASDALSKALKKRGFKFVGTTICYSFMQACGLVNDHVVGCCCHPGNKP
>gnl|CDD|182402 PRK10354, PRK10354, RNA chaperone/antiterminator CspA
MSGKMTGIVKWFNADKGFGFITPDDGSKDVFVHFSAIQNDGYKSLDEGQKVSFTIESGAKGPAAGNVTSL
>gnl|CDD|182403 PRK10355, xylF, D-xylose ABC transporter substrate-binding protein
MKIKNILLTLCASLLLTSVAAHAKEVKIGMAIDDLRLERWQKDRDIFVKKAESLGAKVFVQSANGNEETQ
MSQIENMINRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADIDFYISFDNEKVGELQAKAL
VDKVPQGNYFLMGGSPVDNNAKLFRAGQMKVLKPYIDSGKIKVVGDQWVDGWLPENALKIMENALTANNN
KIDAVVASNDATAGGAIQALSAQGLSGKVAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVE
LGNGEEPKANTTLNNGLKDVPSRLLTPIDVNKNNIDSTVIKDGFHKKSEL
>gnl|CDD|182404 PRK10356, PRK10356, protein bax
MILTPIRRYGAMILMLLTLVFSGEVLAKTHTTTASQKSHLTKASNKQVSSKQEYSRNSAKSSSLPDLRKY
PSGTPRKKAFLRTVMPYITSQNAAITAERNWLISKQYQGQWSPAERARLKDIAKRYKVKWSGNTRKIPWN
TLLERVDIIPTSMVATMAAAESGWGTSKLARNNNNLFGMKCMKGRCTNAPGKVKGYSQFSSVKESVSAYV
TNLNTHPAYSSFRKSRAQLRKADQEVTATAMIHKLKGYSTKGSSYNNYLFAMYQDNQRLIAAHM
>gnl|CDD|182405 PRK10357, PRK10357, putative glutathione S-transferase; Provisional
MKLIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPLGKVPALVTEEGECWFDSPIIAEYI
ELLNVAPAMLPRDPLAALRVRQLEALADGIMDAALVSVREQARPAAQQSEDELLRQREKINRSLDALEGY
LVDGTLKTDTVNLATIAIACAVGYLNFRRVAPGWCVDRPHLVKLVENLFQRESFARTEPPKA
>gnl|CDD|182406 PRK10358, PRK10358, tRNA (uridine(34)/cytosine(34)/5-carboxymethylaminomethyluridine(34)-2'-O)-methyltransferase TrmL
MLNIVLFEPEIPPNTGNIIRLCANTGFRLHIIEPMGFAWDDKRLRRAGLDYHEFTAVTRHHDYAAFLEAE
NPQRLFALTTKGTPAHSAVSYQDGDYLMFGPETRGLPASILDALPAEQKIRIPMMPDSRSMNLSNAVSVV
VYEAWRQLGYPGAVLRD
>gnl|CDD|182407 PRK10359, PRK10359, lipopolysaccharide core heptose(II) kinase RfaY
MITKKKIKGYTVFYKDNDNKYKEIFDDFLSYNIKTIKVFRNIDDTKVSLIDTDYGKYILKVFAPKVKRTE
RFLKSFVKGDYYENLIVQTDRVRSEGLASLNDFYLLAERKTLRYAHTYIMLIEYIEGVELNDMPEISEDV
KAKIKASIESLHQHGMVSGDPHKGNFIVSKNGLRIIDLSGKRCTAQRKAKDRIDLERHYGIKNEIKDLGY
YLLIYKKKLRKFIRKLKGKASR
>gnl|CDD|182408 PRK10360, PRK10360, transcriptional regulator UhpA
MITVALIDDHLIVRSGFAQLLGLEPDLQVVAEFGSGREALAGLPGRGVQVCICDISMPDISGLELLSQLP
KGMATIMLSVHDSPALVEQALNAGARGFLSKRCSPDELIAAVHTVATGGCYLTPDIAIKLASGRQDPLTK
RERQVAEKLAQGMAVKEIAAELGLSPKTVHVHRANLMEKLGVSNDVELARRMFDGW
>gnl|CDD|182409 PRK10361, PRK10361, DNA recombination protein RmuC; Provisional
MDFSIMVYAVIALVGVAIGWLFASYQHAQQKAEQLAEREEMVAELSAAKQQITQSEHWRAECELLNNEVR
SLQSINTSLEADLREVTTRMEAAQQHADDKIRQMINSEQRLSEQFENLANRIFEHSNRRVDEQNRQSLNS
LLSPLREQLDGFRRQVQDSFGKEAQERHTLAHEIRNLQQLNAQMAQEAINLTRALKGDNKTQGNWGEVVL
TRVLEASGLREGYEYETQVSIENDARSRMQPDVIVRLPQGKDVVIDAKMTLVAYERYFNAEDDYTRESAL
QEHIASVRNHIRLLGRKDYQQLPGLRTLDYVLMFIPVEPAFLLALDRQPELITEALKNNIMLVSPTTLLV
ALRTIANLWRYEHQSRNAQQIADRASKLYDKMRLFVDDMSAIGQSLDKAQDNYRQAMKKLSSGRGNVLAQ
AEAFRGLGVEIKREINPDLAEQAVSQDEEYRLRSVPEQPNDEAYQRDDEYNQQSR
>gnl|CDD|182410 PRK10363, cpxP, cell-envelope stress modulator CpxP
MRIVTAAVMASTLAVSSLSHAAEVGTGDNWHPGEELTQRSTQSHMFDGISLTEHQRQQMRDLMQQARHEQ
PPVNVSEMETMHRLVTAENFDENAVRAQAEKMAQEQVARQVEMAKVRNQMYRLLTPEQQAVLNEKHQQRM
EQLRDVTQWQKSSSLKLLSSSNSRSQ
>gnl|CDD|236674 PRK10364, PRK10364, two-component system sensor histidine kinase ZraS
MQRSKDSLAKWLSALLPVVIVGLVGLFSVTVIRDYGRETAAARQTLLEKGSVLIRALESGSRVGMGMRMH
HAQQQALLEEMAGQPGVRWFAVTDEQGTIVAHSNPGMVGKQLYSPQEMQQLHPGDEEAWRRIDSADGEPV
LEIYRQFQPMFAAGMHGMRHMQQYAAANTPQAIFIAFDASNLVSAQAREQRNTLIILFALATVLLASLLA
FFWYRRYLRSRQLLQDEMKRKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMA
KEADRLNRVVSELLELVKPTHLALQAVDLNDLINHSLQLVSQDANSREIQLRFTANDTLPEIQADPDRLT
QVLLNLYLNAIQAIGQHGVISVTASESGAGVKISVTDSGKGIAADQLEAIFTPYFTTKAEGTGLGLAVVH
NIVEQHGGTIQVASQEGKGATFTLWLPVNITRRDPQG
>gnl|CDD|182412 PRK10365, PRK10365, sigma-54-dependent response regulator transcription factor ZraR
MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKE
IKALNPAIPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQFG
MVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESEL
FGHEKGAFTGADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAA
THRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLI
HYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQSQDIQPLVEVEKEVILAALEKTGGN
KTEAARQLGITRKTLLAKLSR
>gnl|CDD|182413 PRK10367, PRK10367, DNA-damage-inducible SOS response protein; Provisional
MAFLTSSDKALWRLALPMIFSNITVPLLGLVDTAVIGHLDSPVYLGGVAVGATATSFLFMLLLFLRMSTT
GLTAQAFGAKNPQALARALVQPLLLALGAGALIALLRTPLIDLALHIVGGSEAVLEQARRFLEIRWLSAP
ASLANLVLLGWLLGVQYARAPVILLVVGNILNIVLDLWLVMGLHMNVQGAALATVIAEYATLLIGLLMVR
KVLKLRGISLEMLKTAWRGNFRRLLALNRDIMLRSLLLQLCFGAITVLGARLGSDIIAVNAVLMTLLTFT
AYALDGFAYAVEAHSGQAYGARDGSQLLDVWRAACRQSGIVALLFSLVYALAGEHIIALLTSLPQIQQLA
DRYLIWQVILPLVGVWCYLLDGMFIGATRAAEMRNSMAVAAAGFALTLLTLPWLGNHGLWLALTVFLALR
GLSLAAIWRRHWRNGTWFAAT
>gnl|CDD|236675 PRK10369, PRK10369, heme lyase subunit NrfE; Provisional
MLFLPEAGFLALLLSLGVNVLTPLTAFAGVRLRWPAMMRLTCIGILAQFALLLLAFGVLTYCFLISDFSV
IYVAQHSHSLLSWGLKLAAVWGGHEGSLLLWVLLLSAWSALFAWHYRQQTDPLFPLTLAVLSLILAALLL
FVVLWSDPFVRIFPPAIEGRDLNPMLQHPGLIFHPPLLYLGYGGLMVAASVALASLLRGEFDAACARICW
RWALPGWSALTAGIILGSWWAYCELGWGGWWFWDPVENASLLPWLSATALLHSLSLTRQRGIFRHWSLLL
AIVTLILSLLGTLIVRSGILVSVHAFALDNVRAVPLFSLFALLSLASLALYGWRARDGGPAVRFSGLSRE
MLILATLLLFSAVLLIVLVGTLYPMIYGLLGWGRLSVGAPYFNRATLPFGLLMLVVIVLATFVSGKRVQL
PALLAHAGVLLFAAGIVVSSVSRQEISLNLQPGQQVTLAGYTFRFERLDLQAKGNYTSEKAIIALFRHQQ
RIGELTPERRFYEARRQQMMEPGIRWNGIHDWYAVMGEKTGADRYAFRLYVQSGVRWIWGGGLLMIAGAL
LSGWRGRKRDE
>gnl|CDD|182415 PRK10370, PRK10370, formate-dependent nitrite reductase complex subunit NrfG; Provisional
MKLRPIPVKMLTTLTILMVFLCVGSYLLSPKWQAVRAEYQRLADPLHQFASQQTPEAQLQALQDKIRANP
QNSEQWALLGEYYLWRNDYDNALLAYRQALQLRGENAELYAALATVLYYQAGQHMTPQTREMIDKALALD
ANEVTALMLLASDAFMQADYAQAIELWQKVLDLNSPRVNRTQLVESINMAKLLQNRQK
>gnl|CDD|182416 PRK10371, PRK10371, transcriptional regulator MelR
MNTDTFMCSSDEKQTRSPLSLYSEYQRLEIEFRPPHIMPTSHWHGQVEVNVPFDGDVEYLINNEKVQINQ
GHITLFWACTPHQLTDPGNCRSMAIFNLPMHLFLSWPLDKDLINHVTHGMVIKSLATQQLSPFEVRRWQQ
ELNSPNEQIRQLAIDEIGLMLKRFSLSGWEPILVNKTSRTHKNSVSRHAQFYVSQMLGFIAENYDQALTI
NDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGK
YVGMSPQQYRKLSQQRRQTFPG
>gnl|CDD|182417 PRK10372, PRK10372, PTS ascorbate transporter subunit IIA
MKLRDSLAENKSIRLQAEAETWQEAVKIGVDLLVAADVVEPRYYQAILDGVEQFGPYFVIAPGLAMPHGR
PEEGVKKTGFALVTLKKPLEFNHEDNDPVDILITMAAVDANTHQEVGIMQIVNLFEDEANFDRLRACRTE
QEVLDLIDRTNAAA
>gnl|CDD|236676 PRK10376, PRK10376, putative oxidoreductase; Provisional
MSTIMSSGTFTLGGRSVNRLGYGAMQLAGPGVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQ
LIREALHPYPDDLTIVTKVGARRGEDGSWLPAFSPAELRRAVHDNLRNLGLDVLDVVNLRLMGDGHGPAE
GSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAEIVCVQNHYNLAHRADDALIDALARDGIAYV
PFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEEVL
AELDGIAREA
>gnl|CDD|182419 PRK10377, PRK10377, PTS glucitol/sorbitol transporter subunit IIA
MTVIYQTTITRIGASATDALSDQMLITFREGAPADIEEYCFIHCHGELKGALQPGLQFELGQHRYPVTAV
GSVAEDNLRELGHVTLRFDGLNEAEFPGTVHVAGPVPDDIAPGSVLKFER
>gnl|CDD|236677 PRK10378, PRK10378, inactive ferrous ion transporter periplasmic protein EfeO; Provisional
MTINFRRNALQLALAALFSSAFMANAADIPQVKVTVNDKQCEPMTLTVNAGKTQFIIQNHSQKALEWEIL
KGVMVVEERENIAPGFSQKMTANLQPGEYDMTCGLLTNPKGKLIVKGEATADAAQSDALLSLVGPIAAYK
AYVTAEVTQLVTDTKAFTDAVKAGDIEKAKALYAPTRQHYERIEPIAELFSDLDGSIDAREDDFEQKAAD
PKFTGFHRLEKALFGDNTTKGMDKYADQLYTDVLDLQKRISELAFPPSKVVGGAAGLIEEVAASKISGEE
DRYSHTDLWDFQANVDGSQKIVDLLRPLLEKANPELLAKVDANFKKVDTILAKYRTKDGFETYDKLTDAD
RNALKGPITALAEDLAQLRGVLGLD
>gnl|CDD|182421 PRK10380, PRK10380, hypothetical protein; Provisional
MPTKPPYPREAYIVTIEKGKPGQTVTWYQLRADHPKPDSLISEHPTAQEAMDAKKRYEDPDKE
>gnl|CDD|182422 PRK10381, PRK10381, LPS O-antigen length regulator; Provisional
MSSLNIKQNSDAHFPDYPLASPSNNEIDLFELISVLWKAKKTIIAITFAFACAGLLISFILPQKWTSTAV
VTPPELVQWQELEKTLTKLRVLDLDVKVDRSSLFNLFIKKFQSRSLLEEYLRSSPYVMDQLKEAKIDELD
LHRAIVALSEKMKAVDNNASKKKDEESLYTSWTLSFTAPTSEEAQDVLSGYINYISTIVVKEVLENIRNK
LEIKTQFEKEKLAMDRIKLKNQLDANIQRLNYSLSIANAAGIKKPVYSNGQAVKDDPDFSIALGADGLER
KLEIEKSVTDVAEINGELRNRQYYVEQLKKLNINDVNFTPFKYQLSPSLPVKKDGPGKALIVILAALIGG
MLACGFVLLRHAMRSRKQDLMLADHLV
>gnl|CDD|182423 PRK10382, PRK10382, alkyl hydroperoxide reductase subunit C; Provisional
MSLINTKIKPFKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYS
VSTDTHFTHKAWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEG
IGRDASDLLRKIKAAQYVASHPGEVCPAKWKEGEATLAPSLDLVGKI
>gnl|CDD|236678 PRK10386, PRK10386, curli production assembly/transport protein CsgE
MKRYLRWIVAAELLFAAGNLHAAVEVEVPGLLTDHTVSSIGHDFYRAFSDKWESDYDGNLTINERPSARW
GSWITITVNQDVIYQTFLFPNKRDFEKTVVFALDQTEEALNRRQIDQALLSTGDLARDEF
>gnl|CDD|236679 PRK10387, PRK10387, glutaredoxin 2; Provisional
MKLYIYDHCPFCVKARMIFGLKNIPVELIVLANDDEATPIRMIGQKQVPILQKDDGSYMPESLDIVHYID
ELDGKPLLTGKRSPAIEEWLRKVFGYLNKLLYPRFAKADLPEFATPSARQYFIDKKEASIGDFDALLAHT
PGLIKEINADLRALDPLIVKPNAVNGELSTDDIHLFPILRNLTLVKGIEWPPRVADYRDNMSKKTQVPLL
>gnl|CDD|182426 PRK10391, PRK10391, transcription modulator YdgT
MTVQDYLLKFRKISSLESLEKLFDHLNYTLTDDQEIINMYRAADHRRAELVSGGRLFDLGQVPKSVWHYV
Q
>gnl|CDD|236680 PRK10396, PRK10396, hypothetical protein; Provisional
MKTGPLNESELEWLDDILTKYGTDHAILDVAELDGLLTAVLSSPREIEPAQWLVAIWGGADYVPRWASEK
EMTRFMDLAFQHMNDTAERLNEYPEQFEPLFGLREVDGQELTIVEEWCFGYMRGVALSDWSTLPDSLKPA
LEAIALHGTEENFELLEKMSPEAFEESVDAIRPAALALHAYWMAHPQEKAVQQPIKAEEKVGRNDPCPCG
SGKKFKQCCLH
>gnl|CDD|182428 PRK10397, PRK10397, lipoprotein; Provisional
MKKLAIAGALMALAGCAEVENYNDVVKTPAPAGLAGYWQTKGPQRALVSPEAIASLIVTKEGDTLDCRQW
QRVIAVPGKLTLRSDDLTNVTVKRELYELERDGNTLEYDGMTLQRVDRPTAECAAALDKAPLPTPLP
>gnl|CDD|236681 PRK10401, PRK10401, HTH-type transcriptional regulator GalS
MITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVS
DAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDQIPG
MVLINRVVPGYAHRCVCLDNVSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPP
ESWIGTGTPDMQGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARY
TDPQLTTVRYPIASMAKLATELALQGAAGNLDPRASHCFMPTLVRRHSVATRQNAAAITNSTNQAM
>gnl|CDD|236682 PRK10402, PRK10402, DNA-binding transcriptional activator YeiL; Provisional
MKESKNSEEISHYMSESAFKDCFSFDVSADTELFHFLAREYIVQEGQQPSYLFYLTRGRAKLYATLANGK
VSLIDFFAAPCFIGEIELIDKDHETKAVQAIEECWCLALPMKDCRPLLLNDALFLRKLCKFLSHKNYRNI
VSLTQNQSFPLENRLAAFILLTQEGDLYHEKHTQAAEYLGVSYRHLLYVLAQFIQDGYLKKSKRGYLIKN
RKQLSGLALELKPENK
>gnl|CDD|182431 PRK10403, PRK10403, nitrate/nitrite response regulator protein NarP
MPEATPFQVLIVDDHPLMRRGVRQLLELDPGFEVVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDT
LNALRRDGVTAQIIILTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIRAGAKGSKVFSERVNQYLRE
REMFGAEEDPFSVLTERELDVLHELAQGLSNKQIASVLNISEQTVKVHIRNLLRKLNVRSRVAATILFLQ
QRGAQ
>gnl|CDD|182432 PRK10404, PRK10404, stress response protein ElaB
MSNQFGDTRIDDDLTLLSETLEEVLRSSGDPADQKYVELKARAEKALDDVKKRVSQASDSYYYRAKQAVY
RADDYVHEKPWQGIGVGAAVGLVLGLLLARR
>gnl|CDD|182433 PRK10406, PRK10406, alpha-ketoglutarate transporter; Provisional
MAESTVTADSKLTSSDTRRRIWAIVGASSGNLVEWFDFYVYSFCSLYFAHIFFPSGNTTTQLLQTAGVFA
AGFLMRPIGGWLFGRIADKHGRKKSMLISVCMMCFGSLVIACLPGYETIGTWAPALLLLARLFQGLSVGG
EYGTSATYMSEVAVEGRKGFYASFQYVTLIGGQLLALLVVVVLQQTLEDAELREWGWRIPFALGAVLAVV
ALWLRRQLDETSQQETRALKEAGSLKGLWRNRRAFIMVLGFTAAGSLCFYTFTTYMQKYLVNTAGMHANV
ASGIMTAALFVFMLIQPLIGALSDKIGRRTSMLCFGSLAALFTVPILSALQNVSSPYAAFGLVMCALLIV
SFYTSISGILKAEMFPAQVRALGVGLSYAVANALFGGSAEYVALSLKSIGMETAFFWYVTLMAVVAFLVS
LMLHRKGKGMRL
>gnl|CDD|182434 PRK10408, PRK10408, L-valine transporter subunit YgaH
MNYEVLLIGLLVGTANYLFRYLPLRLRVGRARPTLKRGKVGILLDSIGIASICALLVVSTAPEVMHDPRK
LLPTLVGFLVLGACFYKTRSIIIATLLGALAYGLAFKVLAI
>gnl|CDD|182435 PRK10409, PRK10409, HypC/HybG/HupF family hydrogenase formation chaperone
MCIGVPGQIRTIDGNQAKVDVCGIQRDVDLTLVGSCDENGQPRVGQWVLVHVGFAMSVINEAEARDTLDA
LQNMFDVEPDVGALLYGEEK
>gnl|CDD|236683 PRK10410, PRK10410, nitrous oxide-stimulated promoter family protein
MLGKKILREKKTIKKMIRLYCKAKHGGEPQKLCPECEELLEYAQKRLDRCPFGEEKPTCKKCPVHCYKPA
KREKMKQVMRFSGPRMLLRHPILAIRHLFD
>gnl|CDD|236684 PRK10411, PRK10411, L-fucose operon activator
MKAARQQAIVDLLLNHTSLTTEALAEQLNVSKETIRRDLNELQTQGKILRNHGRAKYIHRQNQDSGDPFH
IRLKSHYAHKADIAREALAWIEEGMVIALDASSTCWYLARQLPDINIQVFTNSHPICQELGKRERIQLIS
SGGTLERKYGCYVNPSLISQLKSLEIDLFIFSCEGIDSSGALWDSNAINADYKSMLLKRAAQSLLLIDKS
KFNRSGEARIGHLDEVTHIISDERQVATSL
>gnl|CDD|182438 PRK10413, PRK10413, hydrogenase maturation factor HybG
MCIGVPGQVLAVGEDIHQLAQVEVCGIKRDVNIALICEGNPADLLGQWVLVHVGFAMSIIDEDEAKATLD
ALRQMEYDITSA
>gnl|CDD|236685 PRK10414, PRK10414, biopolymer transporter ExbB
MGNNLMQTDLSVWGMYQHADIVVKCVMIGLILASVVTWAIFFSKSVEFFNQKRRLKREQQLLAEARSLDQ
ANDIAADFGSKSLSLHLLNEAQNELELSEGSDDNEGIKERTSFRLERRVAAVGRQMGRGNGYLATIGAIS
PFVGLFGTVWGIMNSFIGIAQTQTTNLAVVAPGIAEALLATAIGLVAAIPAVVIYNVFARQIGGYKAMLG
DVAAQVLLLQSRDLDLEASAAAHPVRVAQKLRVG
>gnl|CDD|182440 PRK10415, PRK10415, tRNA-dihydrouridine synthase B; Provisional
MRIGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQ
IAGSDPKEMADAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDLVKSILTEVVNAVDVPVTLKI
RTGWAPEHRNCVEIAQLAEDCGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVSIPVIANGDITDPLKAR
AVLDYTGADALMIGRAAQGRPWIFREIQHYLDTGELLPPLPLAEVKRLLCAHVRELHDFYGPAKGYRIAR
KHVSWYLQEHAPNDQFRRTFNAIEDASEQLEALEAYFENFA
>gnl|CDD|236686 PRK10416, PRK10416, signal recognition particle-docking protein FtsY; Provisional
FFSWLKKKKKEKKEGWFERLKKGLSKTRENFGEGINGLFAKKKIDEDLLEELEELLIEADVGVETTEEII
EELRERVKRKNLKDPEELKELLKEELAEILEPVEKPLNIEEKKPFVILVVGVNGVGKTTTIGKLAHKYKA
QGKKVLLAAGDTFRAAAIEQLQVWGERVGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHN
KTNLMEELKKIKRVIKKADPDAPHEVLLVLDATTGQNALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFA
IADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGGED
>gnl|CDD|236687 PRK10417, nikC, nickel transporter permease NikC; Provisional
SSRWSVRLALIIIALLALIALTSQWWLPYDPQAIDLPSRLLSPDAQHWLGTDHLGRDIFSRLMAGTRVSL
GSVMACLLLVLALGLVIGGSAGLLGGRVDQATMRVADMFMTFPTSILAFFMVGVLGTGLTNVIIAIALSH
WAWYARMVRSLVISLRQREFVLAARLSGAGHVRVFIDHLLPAVIPQLLVLATLDIGHMMLHVAGLSFLGL
GVTAPTAEWGVMINDARQYIWTQPLLMFWPGLALFISVMAFNLLGDALRDHLDPHLVTEHAH
>gnl|CDD|236688 PRK10418, nikD, nickel transporter ATP-binding protein NikD; Provisional
MPQQIELRNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKP
VAPCALRGRKIATIMQNPRSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFE
MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADD
VAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHLALYGMELAS
>gnl|CDD|236689 PRK10419, nikE, nickel ABC transporter ATP-binding protein NikE
MTLLNVSGLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVS
WRGEPLAKLNRAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDL
DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITH
DLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSPAGRVLQNAVLPAFPVRRRTTEKV
>gnl|CDD|182445 PRK10420, PRK10420, L-lactate permease; Provisional
MNLWQQNYDPAGNIWLSSLIASLPILFFFFALIKLKLKGYVAASWTVAIALAVALLFYKMPVANALASVV
YGFFYGLWPIAWIIIAAVFVYKISVKTGQFDIIRSSILSITPDQRLQMLIVGFCFGAFLEGAAGFGAPVA
ITAALLVGLGFKPLYAAGLCLIVNTAPVAFGAMGIPILVAGQVTGIDSFEIGQMVGRQLPFLTIIVLFWI
MAIMDGWRGVKETWPAVVVAGGSFAIAQYLSSNFIGPELPDIISSLVSLVCLTLFLKRWQPVRIFRFGDL
GASQVDMTLAHTGYTAGQVLRAWSPFLFLTATVTLWSIPPFKALFASGGALYEWVINIPVPYLDKLVARM
PPVVSEATAYAAVYKFDWFSATGTAILFAALLSIVWLKMKPSDAISTFGSTLKELALPIYSIGMVLAFAF
ISNYSGLSSTLALALAHTGHAFTFFSPFLGWLGVFLTGSDTSSNALFAALQATAAQQIGVSDVLLVAANT
TGGVTGKMISPQSIAIACAAVGLVGKESDLFRFTVKHSLIFTCMVGVITTLQAYVLTWMIP
>gnl|CDD|236690 PRK10421, PRK10421, DNA-binding transcriptional repressor LldR; Provisional
RRLSDEVADRVRALIEEKNLEAGMKLPAERQLAMQLGVSRNSLREALAKLVSEGVLLSRRGGGTFIRWRH
ETWSEQNIVQPLKTLMADDPDYSFDILEARHAIEASTAWHAAMRATPGDKEKIQLCFEATLSEDPDLASQ
ADVRFHLAIAEASHNVVLLQTMRGFFDVLQSSVKQSRQRMYLVPPVFSQLTEQHQAVMDAILAGDAEGAR
KAMMAHLSFVHTTIKRFDEDQARQARITRLPGDHNEHSREKNA
>gnl|CDD|182447 PRK10422, PRK10422, lipopolysaccharide core biosynthesis protein; Provisional
MDKPFRRILIIKMRFHGDMLLTTPVISSLKKNYPDAKIDVLLYQDTIPILSENPEINALYGIKNKKAGAS
EKIKNFFSLIKVLRANKYDLIVNLTDQWMVALLVRLLNARVKISQDYHHRQSAFWRKSFTHLVPLQGGHI
VESNLSVLTPLGLSSLVKETTMSYRPESWKRMRRQLDHLGVTQNYVVIQPTARQIFKCWDNDKFSAVIDA
LQARGYEVVLTSGPDKDDLACVNEIAQGCQTPPVTALAGKTTFPELGALIDHAQLFIGVDSAPAHIAAAV
NTPLICLFGATDHIFWRPWSDNMIQFWAGDYQEMPTRDELDRNEKYLSVIPAADVIAAVDKLLPSSTTGT
SL
>gnl|CDD|182448 PRK10423, PRK10423, transcriptional repressor RbsR; Provisional
MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPF
YSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREIMQRYPSVPTV
MMDWAPFDGDSDLIQDNSLLGGDLATQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDG
YEVTGDFEFNGGFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMT
PPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQLTPELMERGSV
>gnl|CDD|170429 PRK10424, PRK10424, ilv operon leader peptide
MTALLRVISLVVISVVVIIIPPCGAALGRGKA
>gnl|CDD|182449 PRK10425, PRK10425, 3'-5' ssDNA/RNA exonuclease TatD
MFDIGVNLTSSQFAKDRDDVVARAFAAGVNGMLITGTNLRESQQAQKLARQYPSCWSTAGVHPHDSSQWQ
AATEEAIIELAAQPEVVAIGECGLDFNRNFSTPEEQERAFVAQLAIAAELNMPVFMHCRDAHERFMALLE
PWLDKLPGAVLHCFTGTREEMQACLARGLYIGITGWVCDERRGLELRELLPLIPAERLLLETDAPYLLPR
DLTPKPASRRNEPAFLPHILQRIAHWRGEDAAWLAATTDANARTLFGL
>gnl|CDD|236691 PRK10426, PRK10426, alpha-glucosidase; Provisional
MDTPRPQLLDFTFEINNDGFTLRFQQRLILRHSKDNPCLWIGSGVADIDMYRGNFSIKDKLTEKIALTDN
RIWLRLAADPDEHIYGCGEQFSYFDLRGKPFPLWTSEQGVGRNKQTYVTWQADCKENAGGDYYWTYFPQP
TFVSSQKYYCHVDNSAYMNFDFSAPEYHELELWEDKATLRFECADTYISLLEKLTALFGRQPELPDWAYD
GVTLGIQGGTEVVQKKLDTMRNAGVKVNGIWAQDWSGIRMTSFGKRLMWNWKWDSERYPQLDSRIKQLNE
EGIQFLGYINPYLASDGDLCEEAAEKGYLAKDADGGDYLVEFGEFYAGVVDLTNPEAYEWFKEVIKKNMI
GLGCSGWMADFGEYLPTDAYLHNGVSAEIMHNAWPALWAKCNYEALEETGKLGEILFFMRAGYTGSQKYS
TLFWAGDQNVDWSLDDGLASVVPAALSLGMSGHGLHHSDIGGYTTLFGMKRTKELLLRWCEFSAFTPVMR
THEGNRPGDNWQFDSDAETIAHFARMTRVFTTLKPYLKELVAEAAKTGLPVMRPLFLHYEDDAATYTLKY
QYLLGRDLLVAPVHEEGRTDWTVYLPEDKWVHLWTGEAFAGGEITVEAPIGKPPVFYRAGSEWASLFASL
RSIAG
>gnl|CDD|182451 PRK10427, PRK10427, PTS fructose-like transporter subunit IIB
MMAYLVAVTACVSGVAHTYMAAERLEKLCQLEKWGVKIETQGALGTENRLTDEDIRRADVVLLITDIELA
GAERFEHCRYVQCSIYAFLREPQRVMSAVRKVLSAPQQTHLILE
>gnl|CDD|182452 PRK10428, PRK10428, hypothetical protein; Provisional
MNKDEAGGNWKQFKGKVKEQWGKLTDDDMTVIEGKRDQLVGKIQERYGYQKDQAEKEVVDWETRNDYRW
>gnl|CDD|182453 PRK10429, PRK10429, melibiose:sodium transporter MelB
MSISMTTKLSYGFGAFGKDFAIGIVYMYLMYYYTDVVGLSVGLVGTLFLVARIWDAINDPIMGWIVNNTR
SRWGKFKPWILIGTLANSVVLFLLFSAHLFEGTAQYVFVCVTYILWGMTYTIMDIPFWSLVPTLTLDKRE
REQLVPYPRFFASLAGFVTAGFTLPFVNYVGGGDRGFGFQMFTLVLIAFFIVSTIITLRNVHEVYSSDNQ
VSAEGSHLTLKDIVALIYKNDQLSCLLGMALAYNIASNIINGFAIYYFTYVIGDADLFPYYLSYAGAANL
VTLILFPRLVKSLSRRILWAGASIFPVLSCGVLLLMGLAAPHNALLIVIAGILLNIGTALFWVLQVIMVA
DTVDYGEYKLGIRCESIAYSVQTMVVKGGSAFAAFFIGVVLGLIGYVPNVEQSAQTLLGMQFIMIGLPTL
FFMITLVLYFRYYRLNGDFLRRIQIHLLDKYRKVPPEPVHAEIPVGAVSDVKA
>gnl|CDD|182454 PRK10430, PRK10430, two-component system response regulator DcuR
MINVLIVDDDAMVAELNRRYVAQIPGFQCCGTASTLEQAKEIIFNSDTPIDLILLDIYMQQENGLDLLPV
LHEAGCKSDVIVISSAADAATIKDSLHYGVVDYLIKPFQASRFEEALTGWRQKKMALEKHQYYDQAELDQ
LIHGSSSNEQDPRRLPKGLTPQTLRTLCQWIDAHQDYEFSTDELANAVNISRVSCRKYLIWLVNCHILFT
SIHYGVTGRPVYRYRLQAEHYSLLKQYCQ
>gnl|CDD|236692 PRK10431, PRK10431, N-acetylmuramoyl-l-alanine amidase II; Provisional
MMYRIRNWLVATLLLLCAQAGAATLSDIQVSNGNQQARITLSFIGDPDYAFSHQSKRTVALDIKQTGVIQ
GLPLLFSGNNLVKAIRSGTPKDAQTLRLVVDLTENGKTEAVKRQNGSNYTVVFTINADVPPPPPPPPVVA
KRVETPAVVAPRVSEPARNPFKTESNRTTGVISSNTVTRPAARATANTGDKVIIAIDAGHGGQDPGAIGP
GGTREKNVTIAIARKLRTLLNDDPMFKGVLTRDGDYFISVMGRSDVARKQNANFLVSIHADAAPNRSATG
ASVWVLSNRRANSEMASWLEQHEKQSELLGGAGDVLANSQSDPYLSQAVLDLQFGHSQRVGYDVATSVLS
QLQRIGELHKRRPEHASLGVLRSPDIPSVLVETGFISNNSEERLLASDDYQQQIAEAIYKGLRNYFLAHP
MQSAPQGATAQTASTVTTPDRTLPN
>gnl|CDD|236693 PRK10433, PRK10433, putative RNA methyltransferase; Provisional
MRLTIILVAPARAENVGAAARAMKTMGFSELRIVDSQAHLEPAARWVAHGSGDILDNAKVFDTLAEALHD
VDFTVATTARSRAKFHYYATPAELVPLLEEKSSWMSHAALVFGREDSGLTNEELALADVLTGVPMAADYP
SLNLGQAVMVYCYQLAGLMQQPAKSDTTADEGQLQALRQRAMRLLTTLGVADDEKLVDWLQQRLGLLEQR
DTAMLHRLLHDIEKKLTK
>gnl|CDD|182457 PRK10434, srlR, DNA-binding transcriptional repressor
MKPRQRQAAILEYLQKQGKTSVEELAQYFDTTGTTIRKDLVILEHAGTVIRTYGGVVLNKEESDPPIDHK
TLINTHKKELIAEAAVSLIHDGDSIILDAGSTVLQMVPLLSRFNNITVMTNSLHIVNALSELDNEQTILM
PGGTFRKKSASFHGQLAENAFEHFTFDKLFIGTDGIDLNAGVTTFNEVYTVSKAMCNAAREIILMADSSK
FGRKSPNVVCSLEKVDKLITDAGIDPAFRQALEEKGIEVIITGESN
>gnl|CDD|182458 PRK10435, cadB, cadaverine/lysine antiporter
MSSAKKIGLFACTGVVAGNMMGSGIALLPANLASIGSIAIWGWIISIIGAMSLAYVYARLATKNPQQGGP
IAYAGEISPAFGFQTGVLYYHANWIGNLAIGITAVSYLSTFFPVLNDPIPAGIACIAIVWVFTFVNMLGG
TWVSRLTTIGLVLVLIPVVGTAIVGWHWFDAATYAANWNTSDTTDGHAIIKSILLCLWAFVGVESAAVST
GMVKNPKRTVPLATMLGTGLAGIIYIAATQVISGMFPASVMAASGAPFAISASTILGNWAAPLVSAFTAF
ACLTSLGSWMMLVGQAGVRAANDGNFPKVYGEVDKNGIPKKGLLLAAVKMTALMILITLMNSSGGKASDL
FGELTGIAVLLTMLPYFYSCVDLIRFEGVNIRNFVSLICSVLGCVFCFIALMGASSFELAGTFIVSLIIL
MFYARKMHERQSHSM
>gnl|CDD|236694 PRK10436, PRK10436, hypothetical protein; Provisional
SNEMNIDQLHALCQRYQAVLLDSDEETLHVAVVDAPSHELLDALRFATGKRIEIECWPRAQMEQHLQRTQ
QTLPVADQEKDTPVAQLINQTLQSALQKRASDIHFEPAQNHYRIRLRIDGVLHPLPDPSPELGAALTARL
KVLGNLDIAERRLPQDGQFTVELAGNAYSFRIATLPCRGGEKVVLRLLQQVQQALDLETLGMTPAQLAQF
RQALQQPQGLILVTGPTGSGKTVTLYSALQTLNTAQINICSVEDPVEIPLAGINQTQIHPKAGLTFQRVL
RALLRQDPDVIMVGEIRDGETAEIAIKAAQTGHLVLSTLHTNSTSETLVRLQQMGIARWMLASALKLVIA
QRLVRKLCPHCRQQASEPIHLPPNIWPGPLPHWQAVGCEHCYHGYYGRTALFEVLPITPVLQQAIASNAS
PEELETHARQQGMTTLFENGLLAVEQGLTTLEELYRVLGMPH
>gnl|CDD|182460 PRK10437, PRK10437, carbonic anhydrase; Provisional
MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLV
IHTDLNCLSVVQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPQE
RRLDTLCELNVMEQVYNLGHSTIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLEQRYRHGIS
NLKLKHANHK
>gnl|CDD|182461 PRK10438, PRK10438, C-N hydrolase family amidase; Provisional
MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTTGFAMEAAASSLPQDDVVAWMTAKA
QQTNALIAGSVALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLV
CYDLRFPVWSRNRNDYDLALYVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRII
NPQGEIIATAEPHQATRIDAELSLEALQEYREKFPAWRDADEFTLR
>gnl|CDD|236695 PRK10439, PRK10439, enterobactin/ferric enterobactin esterase; Provisional
RSVRAASLLSALAAGSEAWWQRKAGVGTPLVERLDDGMVRVTFWWRDPQGDEEHSTIRRVWIYINGVTDH
HQNSQPQSLQRIAGTDVWQWSTELSANWRGSYCFIPTERDDIFSAFAPAPSPDRLELREGWRKLLPQAIA
DPLNPQSWRGGRGHAVSALEMPQAPLQPGWDRPDAPESPAKEIIWKSERLGNSRRVWIYTTGDAAPEERP
LAILLDGQFWAESMPVWPALDSLTHRGQLPPAVYLLIDAIDTTHRSQELPCNADFWLAVQQELLPQVRAI
APFSDDADRTVVAGQSFGGLAALYAGLHWPERFGCVLSQSGSFWWPHRGGQQEGVLLEQLKAGEVSARGL
RIVLEAGRREPMIMRANQALYAQLHPAGHSVFWRQVDGGHDALCWRGGLIQGLIDLWQPLF
>gnl|CDD|182463 PRK10440, PRK10440, iron-enterobactin ABC transporter permease
MIYVSRRLLITCLLLLAACVAAGLWGLRSGAVTLETSQVFAALMGDAPRSMTMVVTEWRLPRVLMALLIG
AALGVSGAIFQSLMRNPLGSPDVMGFNTGAWSGVLVAMVLFGQDLTAIALAAMAGGIVTSLLVWLLAWRN
GIDTFRLIIIGIGVRAMLVAFNTWLLLKASLETALTAGLWNAGSLNGLTWAKTSPSAPIIILMLIAAALL
VRRMRLLEMGDDTACALGVSVERSRLLLMLVAVVLTAAATALAGPISFIALVAPHIARRLSGTARWGLTQ
AALCGALLLLAADLCAQQLFMPYQLPVGVVTVSLGGIYLIVLLIQESRKK
>gnl|CDD|182464 PRK10441, PRK10441, Fe(3+)-siderophore ABC transporter permease
MSGSVAVTRAIAVPGLLLLLIIATALSLLIGAKSLPASVVLEALSGTCQSADCTIVLDARLPRTLAGLLA
GGALGLAGALMQTLTRNPLADPGLLGVNAGASFAIVLGAALFGYSSAQEQLAMAFAGALVASLIVAFTGS
QGGGQLSPVRLTLAGVALAAVLEGLTSGIALLNPDVYDQLRFWQAGSLDIRNLHTLKVVLIPVLIAGATA
LLLSRALNSLSLGSDTATALGSRVARTQLIGLLAITVLCGSATAVVGPIAFIGLMMPHMARWLVGADHRW
SLPVTLLATPALLLFADIIGRLLVPGELRVSVVSAFIGAPVLIFLVRRKTRGGAL
>gnl|CDD|182465 PRK10443, rihA, ribonucleoside hydrolase 1; Provisional
MALPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKP
LMRELIIADNVHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPEL
HSKIARIVIMGGAMGLGNWTPAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGN
PVATIVAELLDFFMEYHKDEKWGFVGAPLHDPCTIAWLLKPELFTTVERWVGVETQGEYTQGMTVVDYYQ
LTGNKPNATVLVDVDRQGFVDLLAERLKFYA
>gnl|CDD|182466 PRK10444, PRK10444, HAD-IIA family hydrolase
IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSA
MATADFLRRQEGKKAYVIGEGALIHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIA
TNPDTHGRGFYPACGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQ
AGLETILVLSGVSTLDDIDSMPFRPSWIYPSVADIDVI
>gnl|CDD|182467 PRK10445, PRK10445, endonuclease VIII; Provisional
MPEGPEIRRAADNLEAAIKGKPLTDVWFAFPQLKPYESQLIGQRVTHIETRGKALLTHFSNGLTLYSHNQ
LYGVWRVVDTGEEPQTTRVLRVRLQTADKTILLYSASDIEMLTPEQLTTHPFLQRVGPDVLDPNLTPEQV
KERLLSPRFRNRQFSGLLLDQAFLAGLGNYLRVEILWQAGLTPQHKAKDLNEAQLDALAHALLDIPRLSY
ATRGQVDENKHHGALFRFKVFHRDGEACERCGGIIEKTTLSSRPFYWCPGCQK
>gnl|CDD|182468 PRK10446, PRK10446, 30S ribosomal protein S6--L-glutamate ligase
MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAIT
FYGTAALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVV
KLVEGTQGIGVVLAETRQAAESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDF
RSNLHRGGAASVASITPQEREIAIKAARTMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAG
KMIRWIERHATTEYCLKTGG
>gnl|CDD|182469 PRK10447, PRK10447, FtsH protease modulator YccA
MDRIVSSSHDRTSLLSTHKVLRNTYFLLSLTLAFSAITATASTVLMLPSPGLILTLVGMYGLMFLTYKTA
NKPTGILSAFAFTGFLGYILGPILNTYLSAGMGDVIALALGGTALVFFCCSAYVLTTRKDMSFLGGMLMA
GIVVVLIGMVANIFLQLPALHLAISAVFILISSGAILFETSNIIHGGETNYIRATVSLYVSLYNIFVSLL
SILGFASRD
>gnl|CDD|182470 PRK10449, PRK10449, heat shock protein HslJ
MKKVVALVALSLLMAGCVSSGKISVTPEQLQHHRFVLESVNGKPVTSDKNPPEISFGEKMHISGSMCNRF
SGEGKLSDGELTVKGLAMTRMMCADPQLNELDNTISEMLKKGAQVDLTANQLTLATAKQTLMYKLADLVN
>gnl|CDD|182471 PRK10452, PRK10452, multidrug/spermidine efflux SMR transporter subunit MdtJ
MIYWILLALAIATEITGTLSMKWASVSEGNGGFILMLVMISLSYIFLSFAVKKIALGVAYALWEGIGILF
ITLFSVLLFDESLSLMKIAGLTTLVAGIVLIKSGTRKARKPEKEVNHAAV
>gnl|CDD|182472 PRK10454, PRK10454, PTS N,N'-diacetylchitobiose transporter subunit IIA
MFDLDNIVDTQTEAEELEEVVMGLIINSGQARSLAYAALKQAKQGDFAAAKAMMDQSRMALNEAHLVQTK
LIEGDQGEGKMKVSLVLVHAQDHLMTSMLARELITELIELHEKLK
>gnl|CDD|182473 PRK10455, PRK10455, periplasmic protein; Reviewed
MRKLTALFVASTLALGAANLAHAADTTTAPPADAKPMMHHKGKFGPHHDMMFKGLNLTDAQKQQIRDIMK
AQRDQMKRPPLEERRAMHDIIASDTFDKAKAEAQITKMEAQRKARMLAHMETQNKIYNVLTPEQKKQFNA
NFEKRLTERPAHEGKMPAAAE
>gnl|CDD|182474 PRK10456, PRK10456, arginine succinyltransferase; Provisional
MMVIRPVERSDLAALMQLAGKTGGGLTSLPANEATLAARIERALKTWQGELPKSEQGYVFVLEDSETGTV
AGICAIEVAVGLNDPWYNYRVGTLVHASKELNVYNALPTLFLSNDHTGSSELCTLFLDPDWRKEGNGYLL
SKSRFMFMAAFRDKFNDKVVAEMRGVIDEHGYSPFWQSLGKRFFSMDFSRADYLCGTGQKAFIAELMPKH
PIYTDFLSEEAQAVIGQVHPQTAPARAVLEKEGFRYRNYIDIFDGGPTLECDIDRVRAIRKSRLVEVAEG
QPAQGDFPACLVANENYHHFRAVLVRTDPATERLILTAAQLDALKCHAGDRVRLVRLCAEEKTA
>gnl|CDD|182475 PRK10457, PRK10457, hypothetical protein; Provisional
MGILSWIIFGLIAGILAKWIMPGKDGGGFFMTIILGIVGAVVGGWISTFFGFGKVDGFNFGSFVVAVIGA
IVVLFIYRKIKS
>gnl|CDD|236696 PRK10458, PRK10458, DNA cytosine methylase; Provisional
MQENISVTEAYSLLTGSADQALLEKLLEIYDVKTLAAQLNGVGENHWSRAILKRWLAGKSAWHRLSEAEF
AHLQTLLPKPPAHHPHYAFRFIDLFAGIGGIRRGFEAIGGQCVFTSEWNKHAVRTYKANWYCDPATHRFN
EDIRDITLSHKEGVSDEEAAEHIRQHIPDHDVLLAGFPCQPFSLAGVSKKNSLGRAHGFECETQGTLFFD
VARIIDAKRPAIFVLENVKNLKSHDKGKTFRIIMQTLDELGYDVADAEDNGPDDPKIIDGKHFLPQHRER
IVLVGFRRDLNLKADFTLRDISECYPAQRPTLAELLDPVVDAKYILTPVLWKYLYRYAKKHQAKGNGFGY
GLVYPNNPQSVTRTLSARYYKDGSEILIDRGWDMALGEKDFDDPENQQHRPRRLTPRECARLMGFEAPGE
AKFRIPVSDTQAYRQFGNSVVVPVFAAVAKLLEPKIKQAVALRQQEA
>gnl|CDD|236697 PRK10459, PRK10459, MOP flippase family protein
MSLREKTISGAKWTAISTVIIIGLQLVQLTVLARILDNHQFGLLTMSLVIIGFADTLSDMGIGASIIQRQ
DISHLQLSTLYWLNVGLGIVVFVLVFLLSPLIADFYHNPELAPLIKTLSLAFVIIPIGQQFRALLQKELE
FNKLAKIEISAVVAGFTFAVVSAFFWPGALAAILGYLVNSSVRTLLFGYFGRKIYRPALHFSLASVKPNL
SFGAWQTAERIINYLNTNIDTILIGRILGAEVLGGYNLAYNVATVPPMKINPIITRVAFPVFAKIQDDTE
KLRVGFLKLLSVLGIINFPLLLGLMVVSNNFVPLVFGEKWNSAIPILQLLCIVGLLRSVGNPIGSLLLAK
GRADLSFKWNVFKTFLFIPAIVIGGQLAGLIGVALGFLLVQIINTILSYFLMIKPVIGLSYRQYILSIWK
PFYLSLPMLIVSYGLGLLLKGHLALGMLLAVQVAAGVLAYLLMIVLSRHALVVEVKRQFCRSEKMKKLLR
VG
>gnl|CDD|182478 PRK10461, PRK10461, thiamine biosynthesis lipoprotein ApbE; Provisional
MEISFTRVALLAAALLLVGCDQAPQPAKTHATEATVLEGKTMGTFWRVSIPGIDAKRSAELQEKIQTQLD
ADDQLLSTYKKDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEKQP
VQIPSQEQIDAAKAKTGLQHLTVINQSHQQYLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVS
VGGALSSRGMNGEGQPWRVAIQKPTDKENAVQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRP
IEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRREGLAVYMITKEGDGFKTWMSPQFKSFLVSEK
>gnl|CDD|182479 PRK10463, PRK10463, hydrogenase nickel incorporation protein HypB; Provisional
MCTTCGCGEGNLYIEGDEHNPHSAFRSAPFAPAARPKMKITGIKAPEFTPSQTEEGDLHYGHGEAGTHAP
GMSQRRMLEVEIDVLDKNNRLAERNRARFAARKQLVLNLVSSPGSGKTTLLTETLMRLKDSVPCAVIEGD
QQTVNDAARIRATGTPAIQVNTGKGCHLDAQMIADAAPRLPLDDNGILFIENVGNLVCPASFDLGEKHKV
AVLSVTEGEDKPLKYPHMFAAASLMLLNKVDLLPYLNFDVEKCIACAREVNPEIEIILISATSGEGMDQW
LNWLETQRCA
>gnl|CDD|182480 PRK10465, PRK10465, hydrogenase-2 assembly chaperone
MTEEIAGFDTNPAAQLQAAFEEIARRSMHDLPFYHPSIPVYVSDFTLFEGQWIGCVLTPWMLSAVILPGP
DQLWPRRKVGEKLGLQLPYGTMTFTVGELDGVSQYLSCSLMSPLDPSLSAEQGVRLADDCARMLLSLPVT
NPDVPDASRRALLFGRRSG
>gnl|CDD|182481 PRK10466, hybD, HyaD/HybD family hydrogenase maturation endopeptidase
MRILVLGVGNILLTDEAIGVRIVEALEQRYILPDYVEILDGGTAGMELLGDMANRDHLIIADAIVSKKNA
PGTIMVLRDEEVPALFTNKISPHQLGLADVLSALRFTGEFPKKLTLVGVIPESLEPHIGLTPTVEAMIEP
ALEQVLAALRESGVEAIPREAIHD
>gnl|CDD|182482 PRK10467, PRK10467, hydrogenase 2 large subunit; Provisional
MSQRITIDPVTRIEGHLRIDCEIENGVVSKAWASGTMWRGMEEIVKNRDPRDAWMIVQRICGVCTTTHAI
SSVRAAESALNIDVPVNAQYIRNIILAAHTTHDHIVHFYQLSALDWVDITSALQADPTKASAMLKGVSTW
HLNSAEEFTKVQNKIKDLVASGQLGIFANGYWGHPAMKLPPEVNLIAVAHYLQALECQRDANRVVALLGG
KTPHIQNLAVGGVANPINLDGLGVLNLERLMYIKSFIDKLSDFVEQVYKVDTAVIAAFYPEWLTRGKGAV
NYLSVPEFPTDSKNGSFLFPGGYIENADLSTYRPITSHSDEYLIKGIQESAKHAWYKDEAPQAPWEGTTI
PAYDGWSDDGKYSWVKSPTFYGKTVEVGPLANMLVKLAAGRESTQNKLNEIVAIYQKLTGNTLEVAQLHS
TLGRIIGRTVHCCELQDILQNQYSALITNIGKGDHTTFVKPNIPATGEFKGVGFLEAPRGMLSHWMVIKD
GIISNYQAVVPSTWNSGPRNFNDDVGPYEQSLVGTPVADPNKPLEVVRTIHSFDPCMACAVHVVDADGNE
VVSVKVL
>gnl|CDD|182483 PRK10468, PRK10468, hydrogenase 2 small subunit; Provisional
MTGDNTLISSHGINRRDFMKLCAALAATMGLSSKAAAEMAESVTNPQRPPVIWIGAQECTGCTESLLRAT
HPTVENLVLETISLEYHEVLSAAFGHQVEENKHNALEKYKGQYVLVVDGSIPLKDNGIYCMVAGEPIVDH
IRKAAEGAAAIIAIGSCSAWGGVAAAGVNPTGAVSLQEVLPGKTVINIPGCPPNPHNFLATVAHIITYGK
PPKLDDKNRPTFAYGRLIHEHCERRPHFDAGRFAKEFGDEGHRQGWCLYHLGCKGPETYGNCSTLQFCDV
GGVWPVAIGHPCYGCNEEGIGFHKGIHQLANVENQTPRSQKPDVNAKEGGNVSAGAIGLLGGVVGLVAGV
SVMAVRELGRQQKKDNADSRG
>gnl|CDD|182484 PRK10470, PRK10470, ribosome hibernation promoting factor
MQLNITGHNVEITEALREFVTAKFAKLEQYFDRINQVYVVLKVEKVTHISDATLHVNGGEIHASAEGQDM
YAAIDGLIDKLARQLTKHKDKLKQH
>gnl|CDD|182485 PRK10472, PRK10472, low affinity gluconate transporter; Provisional
MSTLTLVLTAVGSVLLLLFLVMKARMHAFVALMVVSMGAGLFSGMPLDKIAATMEKGMGGTLGFLAVVVA
LGAMFGKILHETGAVDQIAVKMLKSFGHSRAHYAIGLAGLICALPLFFEVAIVLLISVAFSMARHTGTNL
VKLVIPLFAGVAAAAAFLLPGPAPMLLASQMNADFGWMILIGLCAAIPGMIIAGPLWGNFISRYVELHIP
DDISEPHLGEGKMPSFGFSLSLILLPLVLVGLKTIAARFVPEGSTAYEWFEFIGHPFTAILVACLVAIYG
LAMRQGMPKDKVMEICGHALQPAGIILLVIGAGGVFKQVLVDSGVGPALGEALTGMGLPIAITCFVLAAA
VRIIQGSATVACLTAVGLVMPVIEQLNYSGAQMAALSICIAGGSIVVSHVNDAGFWLFGKFTGATEAQTL
KTWTMMETILGTVGAIVGMIAFQLL
>gnl|CDD|182486 PRK10473, PRK10473, MdtL family multidrug efflux MFS transporter
MSRFLLCSFALVLLYPAGIDMYLVGLPRIAADLNASEAQLHIAFSVYLAGMAAAMLFAGKIADRSGRKPV
AIPGAALFIIASLLCSLAETSSLFLAGRFLQGIGAGCCYVVAFAILRDTLDDRRRAKVLSLLNGITCIIP
VLAPVLGHLIMLKFPWQSLFYTMAAMGILVLLLSLFILKETRPARAPAASSKPRENSESLLNRFFLSRLV
ITTLSVTVILTFVNTSPVLLMEQMGFSRGEYAIIMALTAGVSMTVSFSTPFALGIFKPRTLMLTSQVLFL
AAGITLALSPSHAVSLFGITLICAGFSVGFGVAMSQALGPFSLRAGVASSTLGIAQVCGSSLWIWLAAVL
GISAWNMLIGILIACSIVSLLLILFVAPGRPVAAHEEIPHHA
>gnl|CDD|170468 PRK10474, PRK10474, PTS fructose-like transporter subunit IIB
MAAEALESAAKAKGWEVKVETQGSIGLENELTAEDVASADMVILTKDIGIKFEERFAGKTIVRVNISDAV
KRADAIMSKIEAHLAQTA
>gnl|CDD|236698 PRK10475, PRK10475, 23S rRNA pseudouridine(2604) synthase RluF
MLTDSSTRLNKYISESGICSRREADRYIEQGNVFINGKRATIGDQVKAGDVVKVNGQLIEPREAEDLVLI
ALNKPVGIVSTTEDGERDNIVDFVNHSKRVFPIGRLDKDSQGLIFLTNHGDLVNKILRAGNDHEKEYLVT
VDKPITDEFIRGMGAGVPILGTVTKKCKVKKEAPFVFRITLVQGLNRQIRRMCEHFGYEVTKLERTRIMN
VSLSGIPLGEWRDLTDDELIDLFKLIENSSSEAKPKAKAKPKTAGIKRPVVKMEKTAEKGGRPASNGKRF
TSPGRKKKGR
>gnl|CDD|182488 PRK10476, PRK10476, multidrug transporter subunit MdtN
MESTPKKSPRKKLPALAIVALAIVALVFVIWRTDSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAV
KKGDLLFRIDPRPYELTVAQAQADLALADAQIMTTQRSVDAERSNAASANEQVERARANAKLATRTLERL
EPLLAKGYVSAQQVDQARTAQRDAEVSLNQALLQAQAAAAAVGGVDALVAQRAAREAALAIAELHLEDTT
VRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGK
VDSIGWGVLPDDGGNVPRGLPYVPRSINWVRVAQRFPVRIMLDKPDPELFRIGASAVVELRPGAAC
>gnl|CDD|182489 PRK10477, PRK10477, outer membrane lipoprotein Blc; Provisional
MRLLPVVAAVTAAFLVVACSSPTPPKGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDG
GLNVINKGYNPDRGMWQESEGKAYFTGAPTRAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWI
LSRTPTISDEVKQQMLAVATREGFDVSKLIWVKQPGS
>gnl|CDD|182490 PRK10478, PRK10478, PTS fructose transporter subunit EIIC
MNELVQILKNTRQHLMTGVSHMIPFVVAGGILLAVSVMLYGKGAVPDAVADPNLKKLFDIGVAGLTLMVP
FLAAYIGYSIADRSALAPCAIGAWVGNSFGAGFFGALIAGIIGGIVVHYLKKIPVHKVLRSVMPIFIIPI
VGTLITAGIMMWGLGEPIGALTNSLTQWLQGMQQGSIVMLAVIMGLMLAFDMGGPVNKVAYAFMLICVAQ
GVYTVVAIAAVAICVPPLGMGLATLIGRKNFSAEERETGKAALVMGCVGVTEGAIPFAAADPLRVIPSIM
VGSVCGAVTAALFGAQCYAGWGGLIVLPVVDGKLGYIAAVAVGAVVTAVCVNVLKSLARKNGSSTDEKED
DLDLDFEIN
>gnl|CDD|182491 PRK10481, PRK10481, hypothetical protein; Provisional
MSASLAILTIGQSPRSDVLPLLTEYLDEDEITHAGLLDGLSREEIMAAYAPEAGEDVLVTRLNDGQQVHV
SKQKVERDLQSVIEVLDNQGYDVILLLCTGEFPSLTARNAILLEPSRILPPLVAAIVGGHQVGVIVPVEE
QLAQQAQKWQVLQKPPVFALASPYHGSEEELIDAGKELLDQGADVIVLDCLGYHQRHRDLLQKALDVPVL
LSNVLVARLAAELL
>gnl|CDD|182492 PRK10483, PRK10483, tryptophan permease; Provisional
MATLTTTQTSPSLLGGVVIIGGTIIGAGMFSLPVVMSGAWFFWSMAALIFTWFCMLHSGLMILEANLNYR
IGSSFDTITKDLLGKGWNVVNGISIAFVLYILTYAYISASGSILHHTFAEMSLNVPARAAGFGFALLVAF
VVWLSTKAVSRMTAIVLGAKVITFFLTFGSLLGHVQPATLFNVAESNASYAPYLLMTLPFCLASFGYHGN
VPSLMKYYGKDPKTIVKCLVYGTLMALALYTIWLLATMGNIPRPEFIGIAEKGGNIDVLVQALSGVLNSR
SLDLLLVVFSNFAVASSFLGVTLGLFDYLADLFGFDDSAMGRFKTALLTFLPPVVGGLLFPNGFLYAIGY
AGLAATIWAAIVPALLARASRKRFGSPKFRVWGGKPMIVLILLFGVGNALVHILSSFNLLPVYQ
>gnl|CDD|236699 PRK10484, PRK10484, putative transporter; Provisional
MLTILSFLGFTLLVAVISWWKTRKTDTSSSDGYFLAGRSLTGPVIAGSLLLTNLSTEQLVGLNGQAYASG
MSVMAWEVTAAIALIILALIFLPRYLKSGITTIPDFLEERYDKTTRRIVSILFLIGYVVSFLPIVLYSGA
LALNSLFHVSELLGISYGAAIWLLVWLIGIIGAIYAVFGGLKAVAVSDTINGIGLLIGGLLVPVFGLIAL
GDGSFMQGLEQLTTVHPEKLNSIGGATDPVPFPTLFTGLILVNLFYWCTNQSIVQRALGAKNLAEGQKGA
LLAAFFKLLGPLILVLPGIIAFHLYGDGLPNADMAYPTLVNDVLPVPLVGFFAAVLFGAILSTFNGFLNS
ASTLFSLDIYKPIINPNASEKQLVKVGKKFGFVLAIISMIVAPLIANAPQGLYSYLQQLNGIYNVPILAI
IIVGFFTKRVPALAAKVALGFGIILYIIINFVLKFDIHFLYVLAILFVINVVVMLIIGKIKPRETPFVLK
DAFAVDLTPWKYAKIASIGILLAMIGVYALFSP
>gnl|CDD|182494 PRK10486, PRK10486, (4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione isomerase
MHVTLVEINVKEDKVDEFIEVFRQNHLGSIQEPGNLRFDVLQDPEVPTRFYIYEAYKDEAAVAFHKTTPH
YKTCVEKLEPLMTGPRKKRLFIGLMP
>gnl|CDD|236700 PRK10489, PRK10489, enterobactin transporter EntS
MNKQSWLLDLSLLKTHPAFRAVFIARFISIFGLGLLGVAVPVQIQMMTGSTLQVGLSVTLTGGAMFIGLM
VGGVLADRYDRKKLILLARGTCGLGFIGLALNAFLPEPSLLAIYLLGLWDGFFGSLGVTALLAATPALVG
RENLMQAGAITMLTVRLGSVISPALGGLLIAAGGVAWNYGLAAAGTFITLLPLLRLPALPPPPQPREHPL
RSLLAGFRFLLASPVVGGIALLGGLLTMASAVRVLYPALADEVWQMGAAQIGLLYAAVPLGAALGALTSG
WLAHSARPGLLMLLSTLGSFLAVGLFGLMPMWILAVLCLALFGYLSAISSLLQYTLLQTQTPDEMLGRIN
GLWTAQNVTGDAIGAALLGGLGAMMTPVASASASGFGLLIIGVLLLLVLGELRRFRQTPPEVDASDS
>gnl|CDD|236701 PRK10490, PRK10490, sensor protein KdpD; Provisional
MNNEPLRPDPDRLLEQTAEPHRGKLKIFFGACAGVGKTYAMLQEAQRLRAQGLDVLVGVVETHGRKETAA
LLEGLTVLPPKRIHHRGRHISEFDLDAALARRPALILMDELAHSNAPGSRHPKRWQDVEELLEAGIDVFT
TVNVQHLESLNDVVGGVTGIQVRETVPDPFFDAADEVVLVDLPPDDLRQRLNEGKVYIAGQAERAIEHFF
RKGNLIALRELALRRTADRVDDQMRAWRDHQGEEKVWHTRDAILLCIGHNTGSEKLVRTAARLAARLGSV
WHAVYVETPRLHRLPEKKRRAILSALRLAQELGAETATLSDPAEEKAVLRYAREHNLGKIIIGRRASRRW
WRRESFADRLARLGPDLDLVIVALDEPPARAIAKAPDSRPFKEKWRVQIQGCLVAIALCALITLIAMQWL
PAFDAANLVMLYLLGVVVVALFYGRWPSVVATVINVASFDLFFVAPRGTLAVSDVQYLLTFAVMLTVGLV
IGNLTAGVRYQARVARYREQRTRHLYEMSKALAVGLSPEDIAATSEHFLASTFQARSQLLLPDDNGKLQP
LTHDQGMTPWDDAIARWSFDKGQPAGAGTDTLPGVPYQILPLKSAQKTYGLLAVEPGNLRQLMIPEQQRL
LETFTLLIANALERLTLTASEEQARLASEREQLRNALLAALSHDLRTPLTVLFGQAEILTLDLASEGSPH
ARQASEIRQQVLNTTRLVNNLLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGHPINLSLPEPLT
LIHVDGPLFERVLINLLENAVKYAGAQAEIGIDAHVEGERLQLDVWDNGPGIPPGQEQLIFDKFARGNKE
SAIPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPLETPPELEEFHEDM
>gnl|CDD|236702 PRK10494, PRK10494, envelope biogenesis factor ElyC
MLFTLKKVIGGLLLPLPLLLLIIGAGLALLWFSRFQKTGKIFISIGWLALLLLSLQPVADRLLRPIESRY
PTWNGSQKVDYIVVLGGGYTWNPQWAPSSNLINNSLPRLTEGIRLWRANPGAKLIFTGGAAKTNTVSTAE
VGARVAQSLGVPREDIITLDLPKDTEEEAAAVKQAIGDAPFLLVTSASHLPRAMIFFQQEGLNPLPAPAN
QLAIDSPLNPWERAIPSPVWLMHSERAGYETLGRIWQWLKGSSGEPRQE
>gnl|CDD|182498 PRK10497, PRK10497, phage shock protein PspD
MNTRWQRAGQKVKPGFKLAGKLVLLTALRYGPAGVAGWAVKSVARKPLKMLLAVALEPLLKRAANKVSQR
YKK
>gnl|CDD|182499 PRK10499, PRK10499, PTS sugar transporter subunit IIB
MEKKHIYLFCSAGMSTSLLVSKMRAQAEKYEVPVIIEAFPETLAGEKGQNADVVLLGPQIAYMLPEIQRL
LPNKPVEVIDSLLYGKVDGLGVLKAAVAAIKKAAAN
>gnl|CDD|236703 PRK10502, PRK10502, putative acyl transferase; Provisional
MQDLSGYSVPKGFRGASAWKVQLWWAVQATLFAWSPQPLYRWRAFLLRLFGAKIGKGVVIRPSVRITYPW
KLTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSHDYSDPHFDLNTAPIVIGEGCWLAADVFVA
PGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPRVETE
>gnl|CDD|182501 PRK10503, PRK10503, MdtB/MuxB family multidrug efflux RND transporter permease subunit
MQVLPPSSTGGPSRLFILRPVATTLLMVAILLAGIIGYRALPVSALPEVDYPTIQVVTLYPGASPDVMTS
AVTAPLERQFGQMSGLKQMSSQSSGGASVITLQFQLTLPLDVAEQEVQAAINAATNLLPSDLPNPPVYSK
VNPADPPIMTLAVTSTAMPMTQVEDMVETRVAQKISQVSGVGLVTLSGGQRPAVRVKLNAQAIAALGLTS
ETVRTAITGANVNSAKGSLDGPTRAVTLSANDQMQSAEEYRQLIIAYQNGAPIRLGDVATVEQGAENSWL
GAWANKQQAIVMNVQRQPGANIIATADSIRQMLPQLTESLPKSVKVTVLSDRTTNIRASVDDTQFELMLA
IALVVMIIYLFLRNIPATIIPGVAVPLSLIGTFAVMVFLDFSINNLTLMALTIATGFVVDDAIVVIENIS
RYIEKGEKPLAAALKGAGEIGFTIISLTFSLIAVLIPLLFMGDIVGRLFREFAVTLAVAILISAVVSLTL
TPMMCARMLSQESLRKQNRFSRASERMFDRVIAAYGRGLAKVLNHPWLTLSVALSTLLLTVLLWIFIPKG
FFPVQDNGIIQGTLQAPQSSSFANMAQRQRQVADVILQDPAVQSLTSFVGVDGTNPSLNSARLQINLKPL
DERDDRVQKVIARLQTAVAKVPGVDLYLQPTQDLTIDTQVSRTQYQFTLQATSLDALSTWVPKLMEKLQQ
LPQLSDVSSDWQDKGLVAYVNVDRDSASRLGISMADVDNALYNAFGQRLISTIYTQANQYRVVLEHNTEN
TPGLAALDTIRLTSSDGGVVPLSSIATIEQRFGPLSINHLDQFPSTTISFNVPDGYSLGDAVQAIMDTEK
TLNLPADITTQFQGSTLAFQSALGSTVWLIVAAVVAMYIVLGVLYESFIHPITILSTLPTAGVGALLALM
IAGSELDVIAIIGIILLIGIVKKNAIMMIDFALAAEREQGMSPRDAIYQACLLRFRPILMTTLAALLGAL
PLMLSTGVGAELRRPLGICMVGGLIVSQVLTLFTTPVIYLLFDRLALYTKSRFPRHEEEA
>gnl|CDD|182502 PRK10504, PRK10504, putative transporter; Provisional
MTDLPDSVRWQLWIVAFGFFMQSLDTTIVNTALPSMAQSLGESPLHMHMVIVSYVLTVAVMLPASGWLAD
RVGVRNIFFTAIVLFTLGSLFCALSGTLNELLLARVLQGVGGAMMVPVGRLTVMKIVPREQYMAAMTFVT
LPGQVGPLLGPALGGLLVEYASWHWIFLINIPVGIIGAIATLMLMPNYTMQTRRFDLSGFLLLAVGMATL
TLALDGSKGLGLSPLAIAGLVAVGVVALLLYLLHARNNNRALFSLKLFRTRTFSLGLAGSFAGRIGSGML
PFMTPVFLQIGLGFSPFHAGLMMIPMVLGSMGMKRIVVQVVNRFGYRRVLVATTLGLALVSLLFMLVALL
GWYYLLPFVLFLQGMVNSTRFSSMNTLTLKDLPDNLASSGNSLLSMIMQLSMSIGVTIAGLLLGLFGQQH
VSVDSGATHTVFMYTYLCMALIIALPALIFARVPNDTHQNVAISRRKRSAQ
>gnl|CDD|236704 PRK10506, PRK10506, prepilin peptidase-dependent protein
MKRSMKKQRGYTLIELLVVMTIVSILSAWGLYGWQRWQQRQRLWQTAQQLLDFLLRLQEDANWHNRDHIL
WLIREGQGWCLVSSVAGANTCTGSSPFVFTPPWPDVALASDTTPSLAFYGLRNTAWAGHIRLKNSAGEWR
LVISSRGRIRLCSEGESEGPLC
>gnl|CDD|182504 PRK10507, PRK10507, bifunctional glutathionylspermidine amidase/glutathionylspermidine synthetase; Provisional
MSKGTTSQDAPFGTLLGYAPGGVAIYSSDYSSLDPQEYPDDAAFRSYIDDEYMGHKWQCVEFARRFLFLN
YGVVFTDVGMAYEIFSLRFLREVVNDNILPLQAFPNGSPRAPEAGALLIWDKGGEFKDTGHVAIITQLHG
NKVRIAEQNVIHSPLPQGQQWTRELEMVVENGCYTLKDTFDDTTILGWMIQTDDTEYSLPQPEIAGELLK
ISGARLENKGQFDGKWLDEKDPLQKAYVQANGHVINQDPYHYFTITESAEQELIKATNELHLMYLHATDK
VLKDDNLLALFDIPKILWPRLRLSWQRRRHHMITGRMDFCMDERGLKVYEYNADSASCHTEAGLILERWA
EQGYKGNGHNPAEGLINELAGAWKHSRARPFVHIMQDKDIEENYHAQFMQQALHQAGFETKILRGLDELR
WDAAGQLIDGDGRLVNCVWKTWAWETALDQIREVSDREFAAVPIRTGHPQNEVRLIDVLLRPEVLVFEPL
WTVIPGNKAILPVLWSLFPHHRYLLDTDFTVNDELVKTGYAVKPIAGRCGSNIDLVSHQEEVLDKTSGKF
AEQKNIYQQLWCLPKVDGKYIQVCTFTVGGNYGGTCLRGDPSLVIKKESDIEPLIVVKD
>gnl|CDD|182505 PRK10508, PRK10508, luciferase-like monooxygenase
MTDKTIPFSVLDLAPIPEGSSAREAFSHSLDLARLAEKRGYHRYWLAEHHNMTGIASAATSVLIGYLAAN
TTTLHLGSGGVMLPNHSPLVIAEQFGTLNTLYPGRIDLGLGRAPGSDQRTMMALRRHMSGDIDNFPRDVA
ELVDWFDARDPNPHVRPVPGYGEKIPVWLLGSSLYSAQLAAQLGLPFAFASHFAPDMLFQALHLYRSNFK
PSARLEKPYAMVCINIIAADSNRDAEFLFTSMQQAFVKLRRGETGQLPPPIENMDQFWSPSEQYGVQQAL
SMSLVGDKAKVRHGLQSILRETQADEIMVNGQIFDHQARLHSFELAMDVKEEL
>gnl|CDD|182506 PRK10509, PRK10509, bacterioferritin-associated ferredoxin; Provisional
MYVCLCNGVSDKKIRQAVRQFHPQSFQQLRKFVPVGNQCGKCIRAAREVMQDELMQMPEFKEIA
>gnl|CDD|182507 PRK10510, PRK10510, OmpA family lipoprotein
MKKRVYLIAAVVSGALAVSGCTTNPYTGEREAGKSGIGAGIGSLVGAGIGALSSSKKDRGKGALIGAAAG
AALGGGVGYYMDVQEAKLRDKMRGTGVSVTRSGDNIILNMPNNVTFDSSSATLKPAGANTLTGVAMVLKE
YPKTAVNVVGYTDSTGSHDLNMRLSQQRADSVASALITQGVDASRIRTQGMGPANPIASNSTAEGKAQNR
RVEITLSPL
>gnl|CDD|182508 PRK10512, PRK10512, selenocysteinyl-tRNA-specific translation factor; Provisional
MIIATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYAYWPQPDGRVLGFIDVPGHEKFLSNMLA
GVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVKAVLREYGFAE
AKLFVTAATEGRGIDALREHLLQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLT
GVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAGDAEKEQINRGDWLLADAPPEPFTRVIVELQTHTPLTQ
WQPLHIHHAASHVTGRVSLLEDNLAELVLDTPLWLADNDRLVLRDISARNTLAGARVVMLNPPRRGKRKP
EYLQWLAALARAQDDAEALALHLERGAVNLADFAWARQLNGEGMRALLQQPGYIQAGDSLLSAPVAARWQ
RKLLDTLATYHEQHRDEPGPGRERLRRMALPMEDEALVLLLIEKMRESGDIHSHHGWLHLPDHKAGFSEE
QQALWQKAEPLFGDEPWWVRDLAKETGTDEQAMRLTLRQAAQQGIITAIVKDRYYRNDRIVQFANMIREL
DQECGSTCAADFRDRLGVGRKLAIQILEYFDRIGFTRRRGNDHLLRDALLFPEK
>gnl|CDD|182509 PRK10513, PRK10513, sugar phosphate phosphatase; Provisional
MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNN
GALVQKAADGETVAQTALSYDDYLYLEKLSREVGVHFHALDRNTLYTANRDISYYTVHESFLTGIPLVFR
EVEKMDPNLQFPKVMMIDEPEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGI
KPEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEKYVLN
>gnl|CDD|182510 PRK10514, PRK10514, putative acetyltransferase; Provisional
MISIRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLWVAVDERDQPVGFMLLSGG
HMEALFVDPDVRGCGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYPLLH
LAYVG
>gnl|CDD|170492 PRK10515, PRK10515, hypothetical protein; Provisional
MALPRITQKEMTEREQRELKTLLDRARIAHGRPLTNSETNSIKKEYIDKLMAEREAEAKKARQLKKKQAY
KPDTEATFSWSANTSTRGRR
>gnl|CDD|236705 PRK10517, PRK10517, magnesium-transporting P-type ATPase MgtA
MLKTMLKELFTRLLRHLPSRLVHRDPLPGAQQTVNTAVPPSLSARCLKAAVMPEEELWKTFDTHPEGLNE
AEVESAREQHGENELPAQKPLPWWVHLWVCYRNPFNILLTILGAISYATEDLFAAGVIALMVAISTLLNF
IQEARSTKAADALKAMVSNTATVLRVINDKGENGWLEIPIDQLVPGDIIKLAAGDMIPADLRILQARDLF
VAQASLTGESLPVEKFATTRQPEHSNPLECDTLCFMGTNVVSGTAQAVVIATGANTWFGQLAGRVSEQDS
EPNAFQQGISRVSWLLIRFMLVMAPVVLLINGYTKGDWWEAALFALSVAVGLTPEMLPMIVTSTLARGAV
KLSKQKVIVKRLDAIQNFGAMDILCTDKTGTLTQDKIVLENHTDISGKTSERVLHSAWLNSHYQTGLKNL
LDTAVLEGVDEESARSLASRWQKIDEIPFDFERRRMSVVVAENTEHHQLICKGALEEILNVCSQVRHNGE
IVPLDDIMLRRIKRVTDTLNRQGLRVVAVATKYLPAREGDYQRADESDLILEGYIAFLDPPKETTAPALK
ALKASGVTVKILTGDSELVAAKVCHEVGLDAGEVLIGSDIETLSDDELANLAERTTLFARLTPMHKERIV
TLLKREGHVVGFMGDGINDAPALRAADIGISVDGAVDIAREAADIILLEKSLMVLEEGVIEGRRTFANML
KYIKMTASSNFGNVFSVLVASAFLPFLPMLPLHLLIQNLLYDVSQVAIPFDNVDDEQIQKPQRWNPADLG
RFMVFFGPISSIFDILTFCLMWWVFHANTPETQTLFQSGWFVVGLLSQTLIVHMIRTRRIPFIQSRAAWP
LMIMTLIVMAVGIALPFSPLASYLQLQALPLSYFPWLVAILAGYMTLTQLVKGFYSRRYGWQ
>gnl|CDD|236706 PRK10518, PRK10518, alkaline phosphatase; Provisional
GKMTRMKQATIALALLPLLFTPVAAARTPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSNKPAK
NVILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGV
KTYNGALGVDIHGKDHPTLLELAKAAGKATGNVSTAELQDATPAALVAHVTSRKCYGPEETSEKCPGNAL
ENGGRGSITEQLLNTRADVTLGGGAKTFAETATAGEWKGKTLREQAKARGYQLVEDADSLNAVTEANQDK
PLLGLFADGNMPVRWLGPKATYHGNLDKPPVTCTPNPQRTADVPTLAQMTDKAIDLLKKNEKGFFLQVEG
ASIDKQDHAANPCGQIGETVDLDEAVQKALEFARKDGNTLVIVTADHAHSSQIIAPDAKAPGLTQALNTK
DGAVMVVSYGNSEEDSQEHTGTQLRIAAYGPHAANVVGLTDQTDLFYTMKDALGLK
>gnl|CDD|182513 PRK10519, PRK10519, hypothetical protein; Provisional
TQVKKNVTDIFIDGARKGFTIATTNLLPNVLMAFVIIQALNITGLLDLVGHIFGPVMALFGLPGEAATVL
LAAWMSMGGAVGVAASLFTAGALTGHHVTILLPAIYLMGSQVQYMGRILGVAEVNAKYYPHLIAVCIINA
LLAMLVMRLIV
>gnl|CDD|182514 PRK10520, rhtB, homoserine/homoserine lactone efflux protein; Provisional
MTLEWWLAYLLTSIILSLSPGSGAINTMSTSISHGYRGAVASIAGLQTGLAIHIVLVGVGLGALFSQSLL
AFEVLKWAGAAYLIWLGIQQWRAAGAIDLHTLASTQSRRRLFKRAVFVNLTNPKSIVFLAALFPQFIMPQ
QPQLMQYLVLGVTTVVVDIIVMIGYATLAQRIARWIKGPKQMKALNKIFGSLFMLVGALLASARH
>gnl|CDD|236707 PRK10522, PRK10522, multidrug transporter membrane component/ATP-binding component; Provisional
MELLRLVWRQYRWPFISVMALSLASAALGIGLIAFINQRLIETADTSLLVLPEFLGLLLLLMAVTLGSQL
ALTTLGHHFVYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITIAFVRLPELVQGIILTLGSAA
YLAWLSPKMLLVTAIWMAVTIWGGFVLVARVYKHMATLRETEDKLYNDYQTVLEGRKELTLNRERAEYVF
ENEYEPDAQEYRHHIIRADTFHLSAVNWSNIMMLGAIGLVFYMANSLGWADTNVAATYSLTLLFLRTPLL
SAVGALPTLLSAQVAFNKLNKLALAPYKAEFPRPQAFPDWQTLELRNVTFAYQDNGFSVGPINLTIKRGE
LLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPEGKPA
NPALVEKWLERLKMAHKLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQ
VLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASRDAVARTA
>gnl|CDD|236708 PRK10523, PRK10523, envelope stress response activation lipoprotein NlpE
MMKKAIITALAAAGLFTLMGCNNRAEVDTLSPAQAAELKPMQQSWRGVLPCADCEGIETSLFLEKDGTWV
MNERYLGAREEPSSFASYGTWARTADKLVLTDSKGEKSYYRAKGDALEMLDREGNPIESQLNYTLEPVQS
PLPVTPMTLRGMYFYMADAATFTDCATGKRFPVANNAELERGYLAARGEGGKPVLLEVEGHFTLRPSMET
GQPDKALIPDGNIKFDPNKDCSSK
>gnl|CDD|182517 PRK10524, prpE, propionyl-CoA synthetase; Provisional
MMSYSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLDYSNPPFARWFVGGRTNLCHNAVDRHLAKRPEQL
ALIAVSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVF
GGFASHSLAARIDDAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHKPRHVLLVDRGLAPMARVAGRD
VDYATLRAQHLGARVPVEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFC
ASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLR
KHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGWPILAIARGVEDRPTRLGSPGVPMYGY
NVKLLNEVTGEPCGPNEKGVLVIEGPLPPGCMQTVWGDDDRFVKTYWSLFGRQVYSTFDWGIRDADGYYF
ILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREARLALE
KEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGRDPGDLTTIEDPAALQQIRQALEE
>gnl|CDD|182518 PRK10525, PRK10525, cytochrome o ubiquinol oxidase subunit II; Provisional
MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYR
ASNKDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFF
IYPEQGIATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASY
SGPGFSGMKFKAIATPDRAEFDQWVAKAKQSPNTMNDMAAFEKLAAPSEYNPVEYFSSVKPDLFKDVINK
FMGHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH
>gnl|CDD|182519 PRK10526, PRK10526, acyl-CoA thioesterase II; Provisional
MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDS
QKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSL
AHLLPPVLKDKFICDRPLEIRPVEFHNPLKGHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPV
ALQPHGIGFLEPGMQIATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEG
VMRNHN
>gnl|CDD|182520 PRK10527, PRK10527, DUF454 family protein
MQRIILIIIGWLAVVLGTLGVVLPLLPTTPFILLAAWCFARSSPRFHAWLLYRSWFGSYLRHWQQHRAMP
PGAKPRAILLILLTFAISLWLVQMPWVRILLLVILACLLIFMWRIPVIDEKQEKH
>gnl|CDD|182521 PRK10528, PRK10528, multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
VLLTFRAAAADTLLILGDSLSAGYRMPASAAWPALLNDKWQSKTSVVNASISGDTSQQGLARLPALLKQH
QPRWVLVELGGNDGLRGFPPQQTEQTLRQIIQDVKAANAQPLLMQIRLPANYGRRYNEAFSAIYPKLAKE
FDIPLLPFFMEEVYLKPQWMQDDGIHPNRDAQPFIADWMAKQLQPLVNHDS
>gnl|CDD|182522 PRK10529, PRK10529, DNA-binding transcriptional activator KdpE; Provisional
MTNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQW
SAIPVIVLSARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHSATPAPDPLVKFSDVTVDLAA
RVIHRGEEEVHLTPIEFRLLAVLLNNAGKVLTQRQLLNQVWGPNAVEHSHYLRIYMGHLRQKLEQDPARP
RHFITETGIGYRFMP
>gnl|CDD|182523 PRK10530, PRK10530, pyridoxal phosphate (PLP) phosphatase; Provisional
MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTY
LYDYQAKKVLEADPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYEHPTGHVIRTLNWAQTLPPEQRPTFT
QVDSLAQAARQVNAIWKFALTHEDLPQLQHFAKHVEHELGLECEWSWHDQVDIARKGNSKGKRLTQWVEA
QGWSMKNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYSHVL
>gnl|CDD|236709 PRK10531, PRK10531, putative acyl-CoA thioester hydrolase
MNTFSVSRLALALAFGVTLTACSSTPPDQRPSDQTAPGTASRPILSASEAKNFTAAHYFASLGPIAAPWN
PSPITLPAQPDFVVGPAGTQGVTHTTVQAAVDAAIAKRTNKRQYIAVMPGTYQGTVYVPAAAPPITLYGT
GEKPIDVKIGLALDGEMSPADWRANVNPRGKYMPGKPAWYMYDSCQSKRAATIGTLCSAVFWSQNNGLQL
QNLTIENTLGDSVDAGNHPAVALRTDGDKVQIENVNILGRQDTFFVTNSGVQNRLETDRQPRTYVKNSYI
EGDVDFVFGRGAVVFDNTEFRVVNSRTQQEAYVFAPATLPNIYYGFLAINSRFNASGDGVAQLGRAWDVD
AGLSAYVNGANTNGQVVIRDSAINEGFNTAKPWADAVTSNRPFAGNTGSQRNLNDTNYNRMWEYNNRGVG
SK
>gnl|CDD|182525 PRK10532, PRK10532, threonine and homoserine efflux system; Provisional
MPGSLRKLPVWLPILLLLIAMASIQSGASLAKSLFPLVGAPGVTALRLALGTLILIAIFKPWRLRFAKEQ
RLPLLFYGVSLGGMNYLFYLSIQTVPLGIAVALEFTGPLAVALFSSRRPVDFVWVVLAVLGLWFLLPLGQ
DVSHVDLTGAALALGAGACWAIYILSGQRAGAEHGPATVAIGSLIAALIFVPIGALQAGEALWHWSILPL
GLAVAILSTALPYSLEMIALTRLPTRTFGTLMSMEPALAAVSGMIFLGETLTLIQWLALGAIIAASMGST
LTIRREPKIKEVD
>gnl|CDD|182526 PRK10533, PRK10533, putative lipoprotein; Provisional
MRYSKLALLIPCALLLSACTTVTPAYKDNGSRSGPCVEGGPDSVAQQFYDYRIQHRSNDIAALRPYLSDK
LATLLSDASRDNSHRQLLSGDPFSSRTTLPDSAHVASASTIPNRDARNIPLRVDLKQGDQGWQDEVLMIR
EGQCWVVDDVRYLGGSVHAPAGTLRQSIENR
>gnl|CDD|236710 PRK10534, PRK10534, L-threonine aldolase; Provisional
MIDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAALFLPTGTQANLVALLSHC
ERGEEYIVGQAAHNYLYEAGGAAVLGSIQPQPIDAAADGTLPLDKVAAKIKPDDIHFARTRLLSLENTHN
GKVLPREYLKQAWEFTRERNLALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGN
RDYIKRARRWRKMTGGGMRQAGILAAAGLYALKHNVARLQEDHDNAAWLAEQLREAGADVMRQDTNMLFV
RVGEEQAAALGEYMRERNVLINASPIVRLVTHLDVSREQLAEVVAHWRAFLAR
>gnl|CDD|182528 PRK10535, PRK10535, macrolide ABC transporter ATP-binding protein/permease MacB
MTALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ
DVATLDADALAQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEY
QPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQA
ERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVNTASGWRQFVSGFREALTMAWRAMAANKMRTLLTMLGII
IGIASVVSIVVVGDAAKQMVLADIRAIGTNTIDIYPGKDFGDDDPQYQQALKYDDLIAIQKQPWVASATP
AVSQSLRLRYGNIDVAASANGVSGDYFNVYGMTFSEGNTFNQEQLNGRAQVVVLDSNTRRQLFPHKADVV
GEVILVGNMPATVIGVAEEKQSMFGSSKVLRVWLPYSTMSGRVMGQSWLNSITVRVKEGYDSAEAEQQLT
RLLTLRHGKKDFFTWNMDSVLKTAEKTTRTLQLFLTLVAVISLVVGGIGVMNIMLVSVTERTREIGIRMA
VGARASDVLQQFLIEAVLVCLVGGALGITLSLLIAFTLQLFLPGWEIGFSPLALLSAFLCSTVTGILFGW
LPARNAARLDPVDALARE
>gnl|CDD|182529 PRK10536, PRK10536, phosphate starvation-inducible protein PhoH
MGRQKAVIKARREAKRVLRRDSRSHKQREEESVTSLVQMGGVEAIGMARDSRDTSPILARNEAQAHYLKA
IESKQLIFATGEAGCGKTWISAAKAAEALIHKDVDRIIVTRPVLQADEDLGFLPGDIAEKFAPYFRPVYD
VLVRRLGASFMQYCLRPEIGKVEIAPFAYMRGRTFENAVVILDEAQNVTAAQMKMFLTRLGENVTVIVNG
DITQCDLPRGVKSGLSDALERFEEDEMVGIVRFGKEDCVRSALCQRTLHAYS
>gnl|CDD|236711 PRK10537, PRK10537, voltage-gated potassium channel protein
HWKTLRRTRAKLWVTLDILALLVALNGLLILKPVYGMAALNLFDIWHIKALSALDLSLLANAPQFMLGVF
LVLMAIGLLFRARLAWAISILLLLAALAITLHFYPWLKFLIGYCIVLLVALLIYRRDFDRSSLAAGTLFA
VISITSLLFYSTFGALYLGDGFSPPIESLSTAFYFSIVTMSTVGYGDIVPVSESARLFTISVIILGITVF
ATSISAIFGPVIRGNLKRLVKGRISHMHRKDHFIICGHSPLAINTYLGLRQRGQAVTVIVPLGLEHRLPD
DADLIPGDSSDSAVLKKAGAARARAILALRDNDADNAFVVLAAKEMSSDVKTVAAVNDSKNLEKIKRVHP
DMIFSPQLLGSELLARTLNGEEIDNDMITSMLFNSGHGIFSDN
>gnl|CDD|182531 PRK10538, PRK10538, bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG
MIVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPA
EWRNIDVLVNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWP
YAGGNVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGGTEFSNVRFKGDDGKAEKTYQNTVALTPE
DVSEAVWWVATLPAHVNINTLEMMPVTQSFAGLNVHRQ
>gnl|CDD|182532 PRK10540, PRK10540, osmotically-inducible lipoprotein OsmB
MFVTSKKMAAAVLAITLAMSLSACSNWSKRDRNTAIGAGAGALGGAVLTDGSTLGTLGGAAVGGVIGHQV
GK
>gnl|CDD|182533 PRK10542, PRK10542, glutathionine S-transferase; Provisional
MKLFYKPGACSLASHITLRESGLDFTLVSVDLAKKRLENGDDYLAINPKGQVPALLLDDGTLLTEGVAIM
QYLADSVPDRQLLAPVGSLSRYHTIEWLNYIATELHKGFTPLFRPDTPEEYKPTVRAQLEKKFQYVDEAL
ADEQWICGQRFTIADAYLFTVLRWAYAVKLNLEGLEHIAAYMQRVAERPAVAAALKAEGLK
>gnl|CDD|182534 PRK10543, PRK10543, superoxide dismutase [Fe]
MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSSEGGVFNNAAQ
VWNHTFYWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTS
NAGTPLTTDATPLLTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA
>gnl|CDD|182535 PRK10545, PRK10545, excinuclease Cho
MVRRLTSPRLEFEAAAIYEYPEHLRPFLEDLPKLPGVYLFHGESDTMPLYIGKSVNIRSRVLSHLRTPDE
AAMLRQSRRISWICTAGEIGALLLEARLIKEQQPLFNKRLRRNRQLCSLQLNEGRVDVVYAKEVDFSRAP
NLFGLFANRRAALQALQSIADEQKLCYGLLGLEPLSRGRACFRSALKRCAGACCGKESHEAHALRLRASL
ERLRVVCWPWQGAVALKEQGPEMTQYHIIQNWLWLGAVNSLEEAATLIRTPAGFDHDGYKILCKPLLSGN
YEITEL
>gnl|CDD|182536 PRK10546, PRK10546, pyrimidine (deoxy)nucleoside triphosphate diphosphatase
MKMIDVVAAIIERDGKILLAQRPAHSDQAGLWEFAGGKVEPGESQPQALIRELREELGIEATVGEYVASH
QREVSGRRIHLHAWHVPDFHGELQAHEHQALVWCTPEEALRYPLAPADIPLLEAFMALRAARPAD
>gnl|CDD|236712 PRK10547, PRK10547, chemotaxis protein CheA; Provisional
MDISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENL
LDEARRGEMQLNTDIINLFLETKDIMQEQLDAYKTSQEPDAASFEYICQALRQLALEAKGETPSAVTRLS
VVAIQEKSEPQDESPRSQSGLRIILSRLKAGEVDLLEEELGNLGTLTDVVKGADSLEATLPGSVAEDDIT
AVLCFVIEADQITFETAVAAPQEKAEETTEVVEVSPKISVPPVLKLAAEQAPAGRVEREKTARSSESTSI
RVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFS
RFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLI
LSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLIFAPGFSTAEQVTDVSGRGVG
MDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREEDLHP
LAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNY
RKVPGISAATILGDGSVALIVDVSALQALNREQRMANTAA
>gnl|CDD|182538 PRK10548, PRK10548, flagella biosynthesis regulatory protein FliT
MNNAPHLLSAWQQILTLSQSMLRLATEGQWDELIEQEVAYVQAVEEIAHLTIPPDISTVMQEQLRPMLRQ
ILDNEAELKQLLQQRMDELSSLIGQSTRQKSVNSAYGQLSGFVLLPDEPLF
>gnl|CDD|182539 PRK10549, PRK10549, two-component system sensor histidine kinase BaeS
MKFWRPGITGKLFLAIFATCMLVLITMHWGVRISFERGFIDYIKHGNEQRLQMLSDALGEQYQQHGNWRF
LRNNDRFVFQILRSFEQDNDSKPGPGMPPHGWRTQFWVVDQNNKVLVGPRGPIPPDGTRRPILVNGAEVG
WVIASPVERLTRNTDINFDKQQRRTSWLIVALSTLLAALATFLLARGLLAPVKRLVEGTHKLAAGDFTTR
VTPTSRDELGRLAQDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRGELEAIQDGVRKFTPESVASL
QAEVGTLTKLVDDLHQLSLSDEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQLSLPDSATVFGDP
DRLMQLFNNLLENSLRYTDSGGSLHISAEQRDKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRASG
GSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVELPLERDLQREV
>gnl|CDD|236713 PRK10550, PRK10550, tRNA dihydrouridine(16) synthase DusC
MRVLLAPMEGVLDSLVRELLTEVNDYDLCITEFLRVVDQLLPVKVFHRLCPELHNASRTPSGTLVRIQLL
GQYPQWLAENAARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVPAHLPVTVKV
RLGWDSGERKFEIADAVQQAGATELVVHGRTKEDGYRAEHINWQAIGEIRQRLTIPVIANGEIWDWQSAQ
QCMAITGCDAVMIGRGALNIPNLSRVVKYNEPRMPWPEVVALLQKYTRLEKQGDTGLYHVARIKQWLGYL
RKEYDEATELFQEIRALNNSPDIARAIQAIDI
>gnl|CDD|182541 PRK10551, PRK10551, cyclic di-GMP phosphodiesterase
MFTRAPSSGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQP
LTLDTCQQVNPELTSRAAFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVDMAILPGTPM
MPNKPAIVIWYRNPLLKNSGVFATLNLNLTPYLLYTSRQEDFDGIALIIGNTALSTFSSRLMNVNELPDM
PLRETTIPGYPLTIRLYADSWTANDIWYALLLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVE
YQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVLPVGA
KLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEATKLFAWLHSQGIEIAIDDFGT
GHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVN
FLQGYWISRPLPLEDFVRWLKEPYTPQW
>gnl|CDD|182542 PRK10553, PRK10553, chaperone NapD
MHTNWQVCSLVVQAKSERISDISTQLNAFPGCEVAVSDAPSGQLIVVVEAEDSETLLQTIESVRNVEGVL
AVSLVYHQQDEQGEETP
>gnl|CDD|182543 PRK10554, PRK10554, outer membrane porin protein C; Provisional
LVAGAANAAEIYNKDGNKLDLYGKVDGLHYFSDDKSVDGDQTYMRLGFKGETQVTDQLTGYGQWEYQIQG
NSAENENNSWTRVAFAGLKFQDVGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFMQQRGNGFATYR
NTDFFGLVDGLNFALQYQGKNGSVSGEGMTNNGRGALRQNGDGYGGSLTYDYGEGFSIGAAISSSKRTDD
QNNLAYIGNGDRAETYTGGLKYDANNIYLAAQYTQTYNATRFGSLGFANKAQNFEVVAQYQFDFGLRPSV
AYLQSKGKDLGNINGRNYGDQDILKYVDVGATYYFNKNMSTYVDYKINLLDDNQFTRDAGINTDDIVALG
LVYQF
>gnl|CDD|182544 PRK10555, PRK10555, multidrug efflux RND transporter permease AcrD
MANFFIDRPIFAWVLAILLCLTGTLAIFSLPVEQYPDLAPPNVRITANYPGASAQTLENTVTQVIEQNMT
GLDNLMYMSSQSSGTGQASVTLSFKAGTDPDEAVQQVQNQLQSAMRKLPQAVQNQGVTVRKTGDTNILTI
AFVSTDGSMDKQDIADYVASNIQDPLSRVNGVGDIDAYGSQYSMRIWLDPAKLNSFQMTTKDVTDAIESQ
NAQIAVGQLGGTPSVDKQALNATINAQSLLQTPEQFRDITLRVNQDGSEVTLGDVATVELGAEKYDYLSR
FNGKPASGLGVKLASGANEMATAKLVLNRLDELAQYFPHGLEYKVAYETTSFVKASIEDVVKTLLEAIAL
VFLVMYLFLQNFRATLIPTIAVPVVLMGTFSVLYAFGYSINTLTMFAMVLAIGLLVDDAIVVVENVERIM
SEEGLTPREATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGTTGAIYRQFSITIVSAMVLSVLVAMILTP
ALCATLLKPLKKGEHHGQKGFFGWFNRMFNRNAERYEKGVAKILHRSLRWILIYVLLLGGMVFLFLRLPT
SFLPLEDRGMFTTSVQLPSGSTQQQTLKVVEKVEKYYFTHEKDNVMSVFATVGSGPGGNGQNVARMFIRL
KDWDERDSKTGTSFAIIERATKAFNKIKEARVIASSPPAISGLGSSAGFDMELQDHAGAGHDALMAARNQ
LLALAAKNPELTRVRHNGLDDSPQLQIDIDQRKAQALGVSIDDINDTLQTAWGSSYVNDFMDRGRVKKVY
VQAAAPYRMLPDDINLWYVRNKDGGMVPFSAFATSRWETGSPRLERYNGYSAVEIVGEAAPGVSTGTAMD
IMESLVKQLPNGFGLEWTAMSYQERLSGAQAPALYAISLLVVFLCLAALYESWSVPFSVMLVVPLGVIGA
LLATWMRGLENDVYFQVGLLTVIGLSAKNAILIVEFANEMNQKGHDLFEATLHASRQRLRPILMTSLAFI
FGVLPMATSTGAGSGSQHAVGTGVMGGMISATILAIFFVPLFFVLVRRRFPLKPRPE
>gnl|CDD|182545 PRK10556, PRK10556, hypothetical protein; Provisional
MYLRPDEVARVLEKAGFTVDVVTQKAYGYRRGENYVYVNREARMGRTALVIHPTLKERSSTLAEPASDIK
TCDHYQQFPLYLAGERHEHYGIPHGFSSREALERYLNGMFG
>gnl|CDD|236714 PRK10557, PRK10557, prepilin peptidase-dependent protein
AMPVKQRGFSLLEVLLAMAIGSVLLLGAARFLPALQRQILTLTRQLRLEDEIWQRVFTVEKDLRRAGYCH
GSCQGEGLEIANPGEAQGSCLIVAWDLNSNGRWEGAPHKESEQFGYRLRNGVLETLRGATSCQGKGWEKL
TDPDEITITTFSVERLDTSGFSPVLTLNLRAASKAEPAIVVQATYSVTGFNL
>gnl|CDD|182547 PRK10558, PRK10558, alpha-dehydro-beta-deoxy-D-glucarate aldolase; Provisional
MNNDVFPNKFKAALAAKQVQIGCWSALANPITTEVLGLAGFDWLVLDGEHAPNDVSTFIPQLMALKGSAS
APVVRVPTNEPVIIKRLLDIGFYNFLIPFVETAEEARRAVASTRYPPEGIRGVSVSHRANMFGTVPDYFA
QSNKNITVLVQIESQQGVDNVDAIAATEGVDGIFVGPSDLAAALGHLGNASHPDVQKAIQHIFARAKAHG
KPSGILAPVEADARRYLEWGATFVAVGSDLGVFRSATQALADTFKK
>gnl|CDD|182548 PRK10559, PRK10559, p-hydroxybenzoic acid efflux pump subunit AaeA
MKTLIRKISRTAITLVLVILAFIAIFRAWVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVK
KGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRLGVQAMSREEIDQANNVLQTVLHQLAK
AQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGYR
AEITPLGSNKVLKGTVDSVAAGVTNSSSTRDSKGMATIDSNLEWVRLAQRVPVRIRLDNQQGNLYPAGTT
ATVVITGKQDRDASQDSPFRKLAHRLREFG
>gnl|CDD|182549 PRK10560, hofQ, outer membrane porin HofQ; Provisional
MVDDVPVAQVLQALAEQEKLNLVVSPDVSGTVSLHLTDVPWKQALQTVVKSAGLILRQEGNILSVHSQAW
QNENIARQEAEQARAQANLPLENRSITLQYADAGELAKAGEKLLSAKGSMTVDKRTNRLLLRDNKTALSA
LEQWVAQMDLPVGQVELAAHIVTINEKSLRELGVKWTLADAQQAGGVGQVTTLGSDLSVATATTRVGFNI
GRINGRLLDLELSALEQKQQLDIIASPRLLASHLQPASIKQGSEIPYQVSSGESGATSVEFKEAVLGMEV
TPTVLQKGRIRLKLHISQNVPGQVLQQADGEVLAIDKQEIETQVEVKSGETLALGGIFSRKNKSGQDSVP
LLGDIPWLGQLFRHDGKEDERRELVVFITPRLVSSE
>gnl|CDD|182550 PRK10561, PRK10561, sn-glycerol-3-phosphate ABC transporter permease UgpA
LLVAPQLIITVIFFIWPAGEALWYSLQSVDPFGFSSQFVGLDNFVALFHDSYYLDSFWTTIKFSTLVTVS
GLLVSLFFAALVDYVVRGSRFYQTLMLLPYAVAPAVAAVLWIFLFNPGRGLITHFLAEFGYDWNHAQNSG
QAMFLVVFASVWKQISYNFLFFFAALQSIPRSLVEAAAIDGAGPIRRFFKLALPLIAPVSFFLLVVNLVY
AFFDTFPVIDAATSGGPVQATTTLIYKIYREGFTGLDLSSSAAQSVVLMFLVIVLTVVQFRYVESKVRYQ
>gnl|CDD|236715 PRK10562, PRK10562, putative acetyltransferase; Provisional
MIREYQPSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVYLPAAQTWVWEEDGKLLGFVSVLEGRF
VGALFVAPKAVRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSW
QADQT
>gnl|CDD|182552 PRK10563, PRK10563, 6-phosphogluconate phosphatase; Provisional
MSQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAE
LEPVYRAEVARLFDSELEPIAGANALLESITVPMCVVSNGPVSKMQHSLGKTGMLHYFPDKLFSGYDIQR
WKPDPALMFHAAEAMNVNVENCILVDDSSAGAQSGIAAGMEVFYFCADPHNKPIDHPLVTTFTDLAQLPE
LWKARGWDITR
>gnl|CDD|236716 PRK10564, PRK10564, maltose operon protein MalM
KMKKSLLALCLSAGLLASAPGISLAAVNYVPQNTSAAPAIPSTALQQLTWQPVDQSKTQTTQLATGGQQL
NVAGISGPVAAYSLPANIGELTLTLSSLVNDKSVFAPNVLVLDQNMRPAAFYPSSYFTYQEPGVMSADRL
EGVLKLTPALGQQKIYLLVYTTEKDLAQTTQLLDPAKAYAKGVGNAVPDIPDPVARHTTDGTLKLKVKTE
SSGNVLIGPLFGSSAPAPVTVGNTAAPVAAPAPAPAKKSEPMLNDTESYFNQAIKQAVKKGDVDKALKLL
DEAERLGSTSARSTFISSVKGKG
>gnl|CDD|182554 PRK10565, PRK10565, putative carbohydrate kinase; Provisional
MTDHTMKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHG
NNGGDGYVVARLAQAAGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGT
GLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVG
QLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRS
GAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEWADVVVIGPGLGQQEWGKKALQKVENFRKPM
LWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRYGGVVVLKGAGTVIAA
EPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGMLATDL
FSTLQRIVNPEVIDKNHD
>gnl|CDD|182555 PRK10566, PRK10566, esterase; Provisional
MIEIETRELAGIEVLHAFPAGQRDTPLPTVFFYHGFTSSKLVYSYFAVALAQAGFRVIMPDAPMHGARFS
GDEARRLNHFWQILLQNMQEFPTLRAAIREEGWLLDDRLAVGGASMGGMTALGIMARHPWVKCVASLMGS
GYFTSLARTLFPPLIPETAAQQAEFNNIVAPLAEWEVTHQLEQLADRPLLLWHGLADDVVPAAESLRLQQ
ALRERGLDKNLTCLWEPGVRHRITPEALDAGVAFFRQHL
>gnl|CDD|182556 PRK10568, PRK10568, molecular chaperone OsmY
MTRLKISKTLLAVMLGSALASGSALAEETLTNKAQSTADSAGQKVDSSMNKVGNFMDDSAITAKVKAALV
DHDNIKSTDISVKTHQKVVTLSGFVESQAQAEEAVKVAKGVEGVTSVSDKLHVRDAKEQSVKGYAGDTAT
TSEIKAKLLADDIVPSRKVKVETTDGVVQLSGTVDSQAQSDRAESIAKAVDGVKSVKNDLKVK
>gnl|CDD|182557 PRK10569, PRK10569, NAD(P)H-dependent FMN reductase; Provisional
MRVITLAGSPRFPSRSSALLEYAREWLNGLGVEVYHWNLQNFAPEDLLYARFDSPALKTFTEQLAQADGL
IVATPVYKASFSGALKTLLDLLPERALEHKVVLPLATGGSVAHMLAVDYALKPVLSALKAQEILHGVFAD
DSQVIDYHHQPQFTPNLQTRLDEALETFWQALHRRDVPVPDLVSLRGNAHA
>gnl|CDD|236717 PRK10572, PRK10572, arabinose operon transcriptional regulator AraC
MYHRMMAEAQNNPLLPGYSFNAHLVAGLTPIEAGGYLDFFIDRPLGMKGYILNLTIRGQGVIFNGGRAFV
CRPGDLLLFPPGEIHHYGRHPDSDEWYHQWVYFRPRAYWADWLNWPSIFAGVGRLRIPDEALQPEFSDLF
GQIEQAGQSEGRYSELLAMNLLERLLLRCMEAIPESLHPPMDPRVREACQYISDHLASEFDIESVAQHVC
LSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSE
FRARCEEKNN
>gnl|CDD|182559 PRK10573, PRK10573, protein transport protein HofC
MASKQLWRWQAINGKGELQDGMLWATSRLLLYQALQQQGLQPLSLKRGRRINARYWRGEQSAEFIRQLAT
LLQAGLPLSEGLQLLAEQHPSAQWQALLQDLAHQLEQGEAFSEALLQWPQVFPPLYQALIATGELTGKLD
ECCFQLARQQEAQQQLTKKVKKALRYPLIILAVALLVVLAMLHFVLPEFAAIYRSFNTPLPLLTRGILAL
SDFLIQYGWLLLLLLFLLAIAYKRLRRKKPTWQIREQRLLLRLPLVGSLIRGQKLSQIFTILALTQSAGL
TLLQGLESAAETLRCPYWQQALTQIQQQIAQGIPLWLALKNHPLFPPLCLQLVRVGEESGSLDLMLENLA
HWHQEQTQALADNLAQLLEPLLMIITGGIVGTLVVAMYLPIFQLGDAMS
>gnl|CDD|236718 PRK10574, PRK10574, putative major pilin subunit; Provisional
MDKQRGFTLIELMVVIAIIAILSAIGIPAYQNYLQKAALTDMLQTFVPYKTAVELCALEHGGLDTCDAGS
NGIPSPTTSRYVSAMSVAKGVITLTGQESLNGLSVVMTPTWDNANGVTGWTRNCNIQSDSALQQACEDVF
RFDDAA
>gnl|CDD|182561 PRK10575, PRK10575, Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC
MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILL
DAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPL
AHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINM
AARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPHPAGAAPVSFVY
>gnl|CDD|236719 PRK10576, PRK10576, Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD
LPDISRRRLLTAMALSPLLWQMNTAAAAAIDPNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPA
LPDSVIDVGLRTEPNLELLTQMKPSLILWSAGYGPSPEKLARIAPGRGFAFSDGKKPLAVARKSLVELAQ
RLNLEAAAETHLAQFDDFIASAKPRLAGRGQRPLLLTSLIDPRHALVFGPNSLFQEVLDELGIENAWQGE
TNFWGSTVVGIERLAAYKDADVICFDHGNSKDMQQLMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMH
FVRVLDNALGGK
>gnl|CDD|236720 PRK10577, PRK10577, Fe(3+)-hydroxamate ABC transporter permease FhuB
MPRLMSRRRARLPALLLALLLLLALALTLTQLSAALPLSQWLQALWGPDADDLEQLLLHYSRLPRLAIAL
LVGAALGLAGALLQQVLRNPLASPTTLGVAAGAQLALVLATLFAPALLALASQLAAFAGGLLAAALVFAL
AGGKRLSPLRLVLAGMVVSLYLGALTTLLLLFNEQYLQGLFLWGAGSLAQNDWSGVQRLLPRLLVGLLLL
LLLARPLTLLGLGDDVARSLGLAVSLTRLAALALAVLLSAAVVSAVGPIGFIGLAAPNLARLLGARRLRA
RLPLSPLIGALLLLLTDQLVRLLAGVGGELLPTGAVTALIGAPLLLWLLPRLRSAQSAPAMSAGDRVAAR
RRRVLAWLLALGLLLLLALVVALSFGRDAHGWNWLSGQLLDALLPLRLPRLLAALLAGAMLAVAGTLLQR
LTRNPLASPEVLGISSGAGLGVVLALFLVPGAGFGWLLAAALLGALAALALILLLARRGGFAPERLLLTG
IALSALFTALIQLLLASGDPRAAQLLTWLSGSTYGVTWAQALPLLIVAVLLLALALLLRRWLDLLPLGDD
TARALGLPVTRARLALLLLAALLTAAATATVGPLSFVGLMAPHLARMLGGRRARPQLVLAALLGALLMVL
ADWLGRTLLFPYQIPAGLLAALIGAPYFLWLLRRSRRR
>gnl|CDD|182564 PRK10578, PRK10578, hypothetical protein; Provisional
MLVYWLDIVGTAVFAISGVLLAGKLRMDPFGVLVLGVVTAVGGGTIRDMALDNGPVFWVKDPTDLVVAMV
TSMLTIVLVRQPRRLPKWMLPVLDAVGLAVFVGIGVNKAFNAEAGPLVAVCMGVITGVGGGIIRDVLARE
IPMILRTEIYATACIIGGIVHATAYYTFSVPLETASMMGMVVTLLIRLAAIRWHLKLPTFALDENGR
>gnl|CDD|182565 PRK10579, PRK10579, pyrimidine/purine nucleoside phosphorylase
MLQSNEYFSGKVKSIGFDSSSTGRASVGVMAEGEYTFSTAEPEEMTVISGALNVLLPGATDWQVYEAGEV
FNVPGHSEFHLQVAEPTSYLCRYL
>gnl|CDD|182566 PRK10580, proY, putative proline-specific permease; Provisional
MESKNKLKRGLSTRHIRFMALGSAIGTGLFYGSADAIKMAGPSVLLAYIIGGVAAYIIMRALGEMSVHNP
AASSFSRYAQENLGPLAGYITGWTYCFEILIVAIADVTAFGIYMGVWFPTVPHWIWVLSVVLIICAVNLM
SVKVFGELEFWFSFFKVATIIIMIVAGIGIIIWGIGNGGQPTGIHNLWSNGGFFSNGWLGMVMSLQMVMF
AYGGIEIIGITAGEAKDPEKSIPRAINSVPMRILVFYVGTLFVIMSIYPWNQVGTNGSPFVLTFQHMGIT
FAASILNFVVLTASLSAINSDVFGVGRMLHGMAEQGSAPKIFSKTSRRGIPWVTVLVMTTALLFAVYLNY
IMPENVFLVIASLATFATVWVWIMILLSQIAFRRRLPPEEVKALKFKVPGGVATTIGGLIFLVFIIGLIG
YHPDTRISLYVGFAWIVLLLIGWMFKRRHDRQLAEAQ
>gnl|CDD|182567 PRK10581, PRK10581, (2E,6E)-farnesyl diphosphate synthase
MDFPQQLQACVQQANQALSRFIAPLPFQNTPVVEAMQYGALLGGKRLRPFLVYATGQMFGVSTNTLDAPA
AAVECIHAYSLIHDDLPAMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAFSILSDAPMPEVSDRDRIS
MISELASASGIAGMCGGQALDLEAEGKQVPLDALERIHRHKTGALIRAAVRLGALSAGDKGRRALPVLDR
YAESIGLAFQVQDDILDVVGDTATLGKRQGADQQLGKSTYPALLGLEQARKKARDLIDDARQSLDQLAAQ
SLDTSALEALANYIIQRDK
>gnl|CDD|182568 PRK10582, PRK10582, cytochrome o ubiquinol oxidase subunit IV; Provisional
MSHSTDHGGASHGSVKTYMTGFILSIILTVIPFWMVMTGAASPAVILGTILAMAVVQILVHLVCFLHMNT
KSDEGWNMTAFVFTVLIIAILVVGSIWIMWNLNYNMMMH
>gnl|CDD|182569 PRK10584, PRK10584, putative ABC transporter ATP-binding protein YbbA; Provisional
MPAENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLV
GQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRL
DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA
ARCDRRLRLVNGQLQEEA
>gnl|CDD|182570 PRK10586, PRK10586, putative oxidoreductase; Provisional
MSHNPIRVVVGPANYFSHPGSIDHLHDFFTDEQLSRAVWIYGERAIAAAQPYLPPAFELPGAKHILFRGH
CSESDVAQLAAASGDDRQVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQAL
HFEIFDDANFLVLVEPRIILNAPQEYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNALAIRDVLL
NSSEQALADQQNGQLTQDFCDVVDAIIAGGGMVGGLGERYTRVAAAHAVHNGLTVLPQTEKFLHGTKVAY
GILVQSALLGQDDVLAQLIGAYQRFHLPTTLAELDVDINNQAEIDRVIAHTLRPVESIHYLPVTLTPDTL
RAAFEKVESFKA
>gnl|CDD|236721 PRK10588, PRK10588, hypothetical protein; Provisional
MSKIIDKLYAVMDKRPLRALSLVMALLLAGCMFWDPSRFAAKTSSLEIWHGLLLMWAVCAGVIHGVGFRP
QKVLWQGIFCPLPADIVLIVGLIFFFF
>gnl|CDD|236722 PRK10590, PRK10590, ATP-dependent RNA helicase RhlE; Provisional
MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHA
KGRRPVRALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLE
HQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEV
ARRNTASEQVTQHVHFVDKKRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKS
QGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVC
VDEHKLLRDIEKLLKKEIPRIAIPGYEPDPSIKAEPIQNGRQQRGGGGRGQGGGRGQQQGQPRRGEGGAK
SASAKPAEKPSRRLGDAKPAGEQQRRRRPRKPAAAQ
>gnl|CDD|182573 PRK10591, PRK10591, hypothetical protein; Provisional
MRALGDLPKSVLILEVLGMLLLVVAYLSLNDYLSLPEPLSTPTAAILMIFLGVLLMLPAAVVIIWRVAKG
LAPQLMNRPPQYSRSEREKDND
>gnl|CDD|182574 PRK10592, PRK10592, putrescine transporter subunit: membrane component of ABC superfamily; Provisional
MNNLPVVRSPWRIVILVLGFTFLYAPMLMLVIYSFNSSKLVTVWAGWSTRWYGELFRDDAMMSAVGLSLT
IAACAATAAAILGTIAAVVMVRFGRFRGSNGFAFMITAPLVMPDVITGLSLLLLFVALAHAIGWPADRGM
LTIWLAHVTFCTAYVAVVISSRLRELDRSIEEAAMDLGATPLKVFFVITLPMIMPAIISGWLLAFTLSLD
DLVIASFVSGPGATTLPMLVFSSVRMGVNPEINALATLILGVVGIVGFIAWYLMARAEKQRIRDIQRARR
G
>gnl|CDD|182575 PRK10593, PRK10593, hypothetical protein; Provisional
MEQLRAELSHLLGEKLSRVECISEQPYAALWALYDSQGNPMPLMARSFSTPGVAQQEAWKLSMLARSGTV
RMPTVYGVMTHEQSPGPDVLLLERLRGVSVEAPARTPERWEQLKDQIVEGLLAWHRIDSRGCVGAVDSTQ
ENLWPSWYQQRVEVLWTTLNQFNNTGLTMQDRRILFRTRECLPALFEGFNDNCVLVHGNFTLRSMLKDPR
SDQLLAMLNPGLMLWAPREYELFRLMDNGLAEQLLWRYLQKAPVAESFIWRRWLYVLWDEVAQLVNTGRF
DRRRFDLAAKSLLPWLA
>gnl|CDD|236723 PRK10594, PRK10594, murein L,D-transpeptidase; Provisional
MLLNKMCGRRLSAISLCLAVTFAPLFNAQADEPEVIPGDSPVAVSEQGEALPQAQQPLPEGSAEKSRTQL
ESQLPAGYKPVYLNQLQLLYAARDMQPMWEDRDAVKAFQQQLAEVAIAGFQPQFTKWVELLTDPAVTGMA
RDVVLSDAMLGYLHFIANIPVKGTRWLYSSKPYALATPPLSVINQWQLALDEGQLPAFVASLAPQHPQYA
AMHEALLALLADTRPWPQLTGKATLRPGQWSNDVPALREILQRTGMLDGGPKITLPGDDTPTDAVVSPSA
VTVETAETKPMDKQTTSRSKPAPAVRAAYDNELVEAVKRFQAWQGLGADGVIGPRTRDWLNVTPAQRAGV
LALNIQRLRLLPGELSTGIMVNIPAYSLVYYQNGNQVLSSRVIVGRPDRKTPMMSSALNNVVVNPPWNVP
TTLARKDILPKVRNDPGYLERHGYTVMRGWNSDAEAIDPWMIDWSTISASNFPYRFQQAPGARNSLGRYK
FNMPSSDAIYLHDTPNHNLFQKDIRALSSGCVRVNKASDLANMLLQDAGWNDARISDALKQGDTRYVNIR
QRIPVNLYYLTAWVAADGRPQYRTDIYNYDLTARSGAQILSKAEQLIR
>gnl|CDD|182577 PRK10595, PRK10595, cell division inhibitor SulA
YANRSSSFSSAASNIARTSTENTTAGLISELVYREDQPMMTQLLLLPLLQQLGQQSRWQLWLTPQQKLSR
EWLQASGLPLTKVMQLSQLSPCHTVEAMERALRTGNYSVVLGWLPDELTEEEHARLVDAAQEGNAMGFIM
RPVSASSHATRQLSGLKIHSNLYH
>gnl|CDD|182578 PRK10597, PRK10597, DNA damage-inducible protein I; Provisional
MRIEVTIAKTSPLPAGAIDALAGELSRRIQYAFPDNEGHVSVRYAAANNLSVIGATKEDKDRISEILQET
WESADDWFVSE
>gnl|CDD|182579 PRK10598, PRK10598, lipoprotein; Provisional
MKKFLFAAALLVSGLLVGCNQLTQYTISEQEINQYLAKHNNFEKQIGLPGVADAHIVLTNLTSQIGREEP
NKVTLTGDANLDISSLFGSQKADMKLTLKAQPVFDKEKGAIYLKDMELVDYTVQPEKMQTVMQTLLPYLN
QSLRSYFNQQPAYVLREDKSKAEALAKKLAKGLEVKPGELVIPFTD
>gnl|CDD|182580 PRK10599, PRK10599, sodium-potassium/proton antiporter ChaA
MSNAQEAVKTRHKETSLIFPVLALVVLFLWGSSQSLPVVIAINLLALIGILSSAFSVVRHADVLAHRLGE
PYGSLILSLSVVILEVSLISALMATGDAAPTLMRDTLYSIIMIVTGGLVGFSLLLGGRKFATQYMNLFGI
KQYLIALFPLAIIVLVFPMALPGANFSTGQALLVALISAAMYGVFLLIQTKTHQSLFVYEHEDEGDDDDP
HHGKPSAHSSLWHAIWLIIHLIAVIAVTKMNASPLETLLTSMNAPVAFTGFLVALLILSPEGLGALKAVL
NNQVQRAMNLFFGSVLATISLTVPVVTLIAFLTGNELQFGLGAPEMVVMVASLVLCHISFSTGRTNVLNG
AAHLALFAAYLMTIFA
>gnl|CDD|182581 PRK10600, PRK10600, nitrate/nitrite two-component system sensor histidine kinase NarX
MAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLLKEMEQTAFSPELQRAAERDGQLAQL
QALQDYWRNELKPALQQAQNPEDVAADVAQFVAGLDALVSAFDHTTEMRIETVVLVHRVFAVFMALLLVF
TIIWLRRRLLQPWRQLLSMANAVSHRDFTQRANISGRDEMAMLGTALNNMSAELAESYAVLEQRVQEKTA
GLEQKNQILSFLWQANRRLHSRAPLCERLSPVLNGLQNLTLLRDIELRVYETDDEENHQEFTCQSDMTCD
DKGCQLCPRGVLPVGDRGTTLKWRLSDKHGQYGILLATLPQGRHLSHDQQQLVDTLVEQLTATLALERQQ
ERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRELLSQIRNELNASWRQLRELL
TTFRLQLTEPGLRPALEASCEEFSARFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSNALKHAQASEV
VVTVAQNQNQVKLSVQDNGCGVPENAERSNHYGLIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIPEKTF
TDVQGDTHE
>gnl|CDD|182582 PRK10602, PRK10602, murein tripeptide amidase MpaA
MTVTRPRAERGAFPPGTEHYGRSLLGAPLLWFPAPAASRESGLILAGTHGDETASVVTLSCALRTLTPSL
RRHHVVLAVNPDGCQLGLRANANGVDLNRNFPAANWKEGETVYRWNSAAEERDVVLLTGDKPGSEPETQA
LCQLIHRLQPAWVVSFHDPLACIEDPRHSELGEWLAQAFELPLVTSVGYETPGSFGSWCADLNLHCITAE
LPPISADEASEKYLFAMANLLRWHPKD
>gnl|CDD|236724 PRK10604, PRK10604, sensor protein RstB; Provisional
MRKLFIQFYLLLFVCFLVMTLLVGLVYKFTAERAGRQSLDDLMKSSLYLMRSELREIPPRDWGKTLKEMD
LNLSFDLRIEPLSKYHLDPASQQRLREGEIVALDDQYTFLQRIPRSHYVLAVGPVPYLYYLHQMRLLDIA
LLALIGLSLAFPVFLWMRPHWQDMLKLEAAAQRLGDGHLAERIHFDEGSSLERLGVAFNQMADNINALIA
SKKQLIDGIAHELRTPLVRLRYRLEMSDNLSAAESQALNRDIGQLEALIEELLTYARLDRPQNELHLSEP
DLPAWLSTHLADIQAVTPEKTVRLDTPHQGDYGALDMRLMERVLDNLLNNALRYAHSRVRVSLLLDGNQA
CLIVEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFS
WPVWHNLPQFTSA
>gnl|CDD|182584 PRK10605, PRK10605, N-ethylmaleimide reductase; Provisional
EKLFSPLKVGAITAPNRVFMAPLTRLRSIEPGDIPTPLMAEYYRQRASAGLIISEATQISAQAKGYAGAP
GLHSPEQIAAWKKITAGVHAEGGHIAVQLWHTGRISHASLQPGGQAPVAPSAINAGTRTSLRDENGQAIR
VETSTPRALELEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRAR
LVLEVVDAGIAEWGADRIGIRISPLGTFNNVDNGPNEEADALYLIEQLGKRGIAYLHMSEPDWAGGEPYS
DAFREKVRARFHGVIIGAGAYTAEKAETLIGKGLIDAVAFGRDYIANPDLVARLQRKAELNPQRPESFYG
GGAEGYTDYPTL
>gnl|CDD|182585 PRK10606, btuE, putative glutathione peroxidase; Provisional
MQDSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLG
QEPGSDEEIKTYCRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTAVAPEESGFYARMVSKGRAPLYP
DDILWNFEKFLVGRDGQVIQRFSPDMTPEDPIVMESIKLALAK
>gnl|CDD|170568 PRK10610, PRK10610, chemotaxis protein CheY
MADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLK
TIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM
>gnl|CDD|236725 PRK10611, PRK10611, protein-glutamate O-methyltransferase CheR
MTSSLPCGQTSLLLQMTQRLALSDAHFRRICQLIYQRAGIVLADHKREMVYNRLVRRLRSLGLNDFGQYL
ALLESNQNSAEWQAFINALTTNLTAFFREAHHFPILAEHARRRSGEYRVWSAAASTGEEPYSIAMTLADT
LGTAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTGPHEGLVRVRQELANYVDFQQ
LNLLAKQWAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSENFSQLSREFYLRGQTV
YGLSKDR
>gnl|CDD|182587 PRK10612, PRK10612, chemotaxis protein CheW
MTGMANVTKLAGEPSGQEFLVFTLGDEEYGIDILKVQEIRGYDQVTRIANTPAFIKGVTNLRGVIVPIVD
LRIKFSQVDVDYNDNTVVIVLNLGQRVVGIVVDGVSDVLSLTAEQIRPAPEFAVTLSTEYLTGLGALGER
MLILVNIEKLLNSEEMALLDSAASEVA
>gnl|CDD|182588 PRK10613, PRK10613, DUF2594 family protein
MSTPDFSTAENNQELANEVSCLKAMLTLMLKAMGQADAGRVILKMEKQIAQIEDETQAAVFSNTVKQIKQ
AYRQ
>gnl|CDD|182589 PRK10614, PRK10614, multidrug efflux system subunit MdtC; Provisional
MKFFALFIYRPVATILLSLAITLCGILGFRLLPVAPLPQVDFPVIMVSASLPGASPETMASSVATPLERS
LGRIAGVNEMTSSSSLGSTRIILQFDFDRDINGAARDVQAAINAAQSLLPSGMPSRPTYRKANPSDAPIM
ILTLTSDTYSQGQLYDFASTQLAQTISQIDGVGDVDVGGSSLPAVRVGLNPQALFNQGVSLDDVRQAISN
ANVRRPQGAVEDGTHRWQIQTNDELKTAAEYQPLIIHYNNGAAVRLGDVATVTDSVQDVRNAGMTNAKPA
ILLMIRKLPEANIIQTVDRIRAKLPELRETIPAAIDLQIAQDRSPTIRASLEEVEQTLAISVALVILVVF
LFLRSGRATLIPAVAVPVSLIGTFAAMYLCGFSLNNLSLMALTIATGFVVDDAIVVLENISRHLEAGMKP
LQAALQGVREVGFTVLSMSLSLVAVFLPLLLMGGLPGRLFREFAVTLSVAIGISLLVSLTLTPMMCAWLL
KSSKPREQKRLRGFGRMLVALQQGYGRSLKWVLNHTRWVGVVLLGTIALNVWLYISIPKTFFPEQDTGRL
MGFIQADQSISFQAMRGKLQDFMKIIRDDPAVDNVTGFTGGSRVNSGMMFITLKPLSERSETAQQVIDRL
RVKLAKEPGANLFLMAVQDIRVGGRQSNASYQYTLLSDDLAALREWEPKIRKALAALPELADVNSDQQDK
GAEMALTYDRDTMARLGIDVQAANSLLNNAFGQRQISTIYQPLNQYKVVMEVDPRYTQDISALEKMFVIN
NEGKAIPLSYFAKWQPANAPLSVNHQGLSAASTISFNLPTGKSLSDASAAIERAMTQLGVPSTVRGSFAG
TAQVFQETMNSQLILILAAIATVYIVLGILYESYVHPLTILSTLPSAGVGALLALELFNAPFSLIALIGI
MLLIGIVKKNAIMMVDFALEAQRNGNLTAQEAIFQACLLRFRPIMMTTLAALFGALPLVLSGGDGAELRQ
PLGITIVGGLVMSQLLTLYTTPVVYLFFDRLRLRFSRKPKQTVTE
>gnl|CDD|182590 PRK10617, PRK10617, cytochrome c-type protein NapC; Provisional
MGNSDRKPGLIKRLWKWWRTPSRLALGTLLLIGFVGGIIFWGGFNTGMEKANTEEFCISCHEMRNTVYQE
YMDTVHYNNRSGVRATCPDCHVPHEFVPKMIRKIKASKELYGKIFGVIDTPQKFEAHRLTMAQNEWRRMK
DNNSQECRNCHNFDYMDTTAQKSVAAKMHDQAVKDGQTCIDCHKGIAHKLPDMREVEPGF
>gnl|CDD|236726 PRK10618, PRK10618, phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
ATTRFSLLPGSITRFFLLFIILLLVTMGLMVYNYVNAWLKDKKYAIVDIAHAIQKRIDTYRYVTWQIYDN
IAATTSPSSGEGLQETRLRPDVYYLEKPRRKTDALIFGSHDSSTLEMTQRMSTYLDTLWGAENVPWSMYY
LNGQDNSLILISTLPLKDLSSRFKESYLSNIVESRRAEMLQQANALDERESFSPLRKLRWQNGYYFTLRT
TFNQPGHLATVIAFDLPINDLIPPGMPLDNFRLEPDATATNNDDNEKEGTDSVSISFNGSWIEISAALNS
TPLKLVYQVPLGTLLLDLLQNNLWPLLLNLGLLALSLFGYYTFRHQYGRPTESMSHELRILRALNEEIVS
NLPLGLLVYDFESNRTVISNKIADHLLPHLNLQKITTMAEQHQGVIQATINNELYEIRMFRSQLAPRTQL
FLLRDQDREVLVNKKLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQ
LAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRI
GDRDALRKILLLLLNYAITTTAYGKITLEVDQDESSPDRLTIRILDTGAGVSIKELDNLHFPFLNQTQGD
RYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAADPEVEEEEEKLLDGVTVLLDITSEE
VRKIVTRQLENWGATCITPDERLISQEYDIFLTDNPSNLTASTLLLSDDESGFRQIGPGQLRVNFNISNA
MQEAILQLIEQQLAQEEVTESPLGGDENALNFYQKQLHASDYYALFVDTVPDDVKRLYTEAATSDFASLA
QTAHRLKGVFAMLNLVPGKQLCETLEHLIREKDEPGIENYISDIDSFVKSLLQQ
>gnl|CDD|182592 PRK10619, PRK10619, histidine ABC transporter ATP-binding protein HisP
MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTIN
LVRDKDGQLKVADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVG
IDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH
EMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKGSLK
>gnl|CDD|182593 PRK10621, PRK10621, hypothetical protein; Provisional
FMDLFMVSPLLLGVLFFVAMLAGFIDSIAGGGGLLTIPALLAAGMSPAQALATNKLQACGGSFSASLYFI
RRKVVNLADQKLNIAMTFVGSMSGALLVQYVQADILRQILPILVIGIGLYFLLMPKLGEEDRQRRLYGLP
FALIAGGCVGFYDGFFGPGAGSFYALAFVTLCGFNLAKATAHAKVLNATSNIGGLLLFILGGKVIWATGF
VMLVGQFLGARLGARLVLSKGQKLIRPMIVIVSAVMSAKLLYDSHGQEILHWLGMN
>gnl|CDD|182594 PRK10622, pheA, bifunctional chorismate mutase/prephenate dehydratase; Provisional
MTSENPLLALREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDA
HYITRLFQLIIEDSVLTQQALLQQHLNKTNPHSARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFA
DIFNQVETGQADYAVLPIENTSSGAINDVYDLLQHTSLSIVGEMTLPIDHCVLVSGTTDLSTIETVYSHP
QPFQQCSQFLNRYPHWKIEYTESTAAAMEKVAQANSPHVAALGSEAGGALYGLQVLERNLANQQQNITRF
IVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLVLRNHNLIMTKLESRPIHGNPWEEMFYLDVQANL
RSAEMQKALKELGEITRSLKVLGCYPSENVVPVDPT
>gnl|CDD|182595 PRK10624, PRK10624, L-1,2-propanediol oxidoreductase; Provisional
MANRMILNETAYFGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPN
PTIEVVKEGVEVFKASGADYLIAIGGGSPQDTCKAIGIISNNPEFADVRSLEGVAPTKKPSVPIIAIPTT
AGTAAEVTINYVITDEEKRRKFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAW
ALTDMLHLKAIEIIAGALRGAVAGDKEAGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVAN
AILLPHVMEYNADFTGEKYRDIARAMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIP
ALAQAAFDDVCTGGNPREATLEDIVELYKKAW
>gnl|CDD|236727 PRK10625, tas, putative aldo-keto reductase; Provisional
MQYHRIPHSSLEVSTLGLGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPRPETQGLTETYIG
NWLAKRGSREKLIIASKVSGPSRNNDKGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNC
FGKLGYSWTDSAPAVSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSL
LNRSFEVGLAEVSQYEGVELLAYSCLAFGTLTGKYLNGAKPAGARNTLFSRFTRYSGEQTQKAVAAYVDI
AKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNIESLHLTLSEEVLAEIEAVHQVYTYPAP
>gnl|CDD|182597 PRK10626, PRK10626, hypothetical protein; Provisional
MMRKMLLAALLSLTAMQAQADYQCSVTPQDDVIISPQTVQVVGASGNLVISPDGNVMRNGKQLSLNAAQR
QQAKDYQAALRQDLPWIDEGAKSRLEKARVALDKVIVQELGESSNVRNRLTKLDAQLKQQMNRIIEHRSD
GLTFHHQAIDQVEADGQQLVNQAMGGILQDSINEMGAKAVLKSGGNPLQAVLGSLGGLQQAIQTEWKNQE
KDFQQFGKDVCSRVVTLEDQRKALVGSLK
>gnl|CDD|182598 PRK10628, PRK10628, LigB family dioxygenase; Provisional
MNVLEDNLYTRAWRTLGETLPRPKAIVVVSAHWYTRGTGVTAMETPRTIHDFGGFPQALYDTHYPAPGSP
ALAQRLVELLAPVPVTLDKEAWGFDHGSWGVLIKMYPDADIPMVQLSIDSTKPAAWHFEMGRKLAALRDE
GIMLVASGNVVHNLRTVKWHGDSSPYPWAESFNQFVKANLTWQGPVEQHPLVNYLQHEGGALSNPTPEHY
LPLLYVLGAWDGKEPISIPVDGIEMGSLSMLSVQVG
>gnl|CDD|236728 PRK10629, PRK10629, EnvZ/OmpR regulon moderator MzrA
MINPRMSLRQLAWLGAVLLLLAALLLAWSALRQQESTLAIRAVHQGASLPDGFYVYQHLDANGIHIKSIT
PENDSLLIRFDSPEQSAAAKEVLDRTLPHGYIIAQQDDNSQAMQWLTRLRDNSHRLG
>gnl|CDD|182600 PRK10631, PRK10631, p-hydroxybenzoic acid efflux subunit AaeB; Provisional
IFSIANQRLRFAVKLAFAIVLALFVGFHFQLETPRWAVLTAAIVAAGPAFAAGGEPFSGAIRYRGMLRII
GTFIGCIAALVIIIATIRAPLLMILLCCIWAGFCTWISSLVRVENSYAWGLAGYTALIIVITIQPEPLLT
PQFAVERCSEIVIGIVCAILADLLFSPRSIKQEVDRELDSLLVAQYQLMQLCIKHGDKEEVDKAWGDLVR
RTTALNGMRSNLMMESSRWQRANRRLKALNTLSLTLITQACETYLIQNTRPELITDTFRELFDTPVETPQ
DVHKQLKRLRRVIAWTGERETPVTIYSWVGAATRYLLLKKGVISNTKISATEEEILQGEPVVKVESAERH
HAMINGWRTTLATALGTLFWLWTGWTSGSGAMVMIAVVTSLAMRLPNPRMVAIDFLYGTLAALPLGALYF
MVIIPNTQQSMLLLCISLGVLGFFIGIEVQKRRLGSLGALASTINILVLDNPMTFHFSQFLDSALGQIVG
CFLALIVILLVRDNSRDRTGRVLLNQFVSAAVSAMTTNVARRKENHLPALYQQLFLLLNKFPGDIPKYRL
ALTLIIAHQRLRDAPIPVNEDLSAFHRQLRRTADHVISARSDDKRRRYFGQLLEELDIYQEKLRIWQAPP
QVTEPVKRLTGMLHKYQHALTD
>gnl|CDD|182601 PRK10632, PRK10632, HTH-type transcriptional activator AaeR
MERLKRMSVFAKVVEFGSFTAAARQLQMSVSSISQTVSKLEDELQVKLLNRSTRSIGLTEAGRIYYQGCR
RMLHEVQDVHEQLYAFNNTPIGTLRIGCSSTMAQNVLAGLTAKMLKEYPGLSVNLVTGIPAPDLIADGLD
VVIRVGALQDSSLFSRRLGAMPMVVCAAKSYLAQYGTPEKPADLSSHSWLEYSVRPDNEFELIAPEGIST
RLIPQGRFVTNDPQTLVRWLTAGAGIAYVPLMWVIDEINRGELEILFPRYQSDPRPVYALYTEKDKLPLK
VQVCINYLTDYFVEVAKLFQEMRGRGKEK
>gnl|CDD|182602 PRK10633, PRK10633, hypothetical protein; Provisional
MDTRFVQAHKEARWALGLTLLYLAAWLVAAYLPGNAPGFTGLPHWFEMACLLLPLLFILLCWLMVKFIFR
DIPLEDDDAA
>gnl|CDD|182603 PRK10634, PRK10634, L-threonylcarbamoyladenylate synthase type 1 TsaC
MNNNLQGDAIAAAVDVLNEERVIAYPTEAVFGVGCDPDSETAVMRLLELKQRPVDKGLILIAANYEQLKP
YIDDSMLTDAQRETIFSCWPGPVTFVFPAPATTPRWLTGRFDSLAVRVTDHPLVVALCQAYGKPLVSTSA
NLSGLPPCRTVEEVRAQFGAAFPVVPGETGGRLNPSEIRDALTGELFRQG
>gnl|CDD|182604 PRK10635, PRK10635, bacterioferritin; Provisional
MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPN
LQDLGKLNIGEDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDL
IGKLGLQNYLQSQIKVED
>gnl|CDD|236729 PRK10636, PRK10636, putative ABC transporter ATP-binding protein; Provisional
MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVN
QETPALPQPALEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSN
EQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLD
PIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRI
KMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAG
KSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQ
GDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLL
RSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKENNANSAQARKDQKRREAELRTQTQP
LRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQ
MLLEGQSN
>gnl|CDD|182606 PRK10637, cysG, siroheme synthase CysG
MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLL
DTCWLAIAATDDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLR
EKLESLLPQHLGQVAKYAGQLRGRVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAVTETTEQLFSE
PLDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQE
EINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYA
QSVRLVTGHLKTGGELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMPADMPVALVENGTSVTQRVVS
GTLTQLGELAQQVNSPSLIIVGRVVGLRDKLNWFSNH
>gnl|CDD|182607 PRK10638, PRK10638, glutaredoxin 3; Provisional
MANVEIYTKATCPFCHRAKALLNSKGVSFQEIPIDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLY
ALDARGGLDPLLK
>gnl|CDD|182608 PRK10639, PRK10639, formate dehydrogenase cytochrome b556 subunit
MKRRDTIVRYTAPERINHWIVAFCFILAAVSGLGFFFPSFNWLMNILGTPQLARILHPFVGVVMFASFII
MFFRYWHHNLINRDDIFWAKNIRKIVVNEEVGDTGRYNFGQKCVFWAAIIFLVLLLVSGVIIWRPYFAPA
FSIPVIRFALMLHSFAAVALIVVIMVHIYAALWVKGTITAMVEGWVTSAWAKKHHPRWYREVRKTTEKKA
E
>gnl|CDD|182609 PRK10640, rhaB, rhamnulokinase; Provisional
MLARYERECRSLTLREIHRFNNGLHSQDGFDTWDVDSLESAIRLGLNKVCEEGIRIDSIGIDTWGVDYVL
LDKQGQRVGLPVSYRDSRTDGVMAQAQQQLGKRDIYRRSGIQFLPFNTLYQLRALTEQQPELIAQVAHAL
LIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGAPKAWFGRPTHPGNVIGHWICPQGNEI
PVVAVASHDTASAVIASPLNDSDAAYLSSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIM
GLWLLQRVLQERQITDLPALIAATAALPACRFLINPNDDRFINPPSMCSEIQAACRETAQPVPESDAELA
RCIFDSLALLYADVLHELAQLRGEPFSQLHIVGGGCQNALLNQLCADACGIRVIAGPVEASTLGNIGIQL
MTLDELNNVDDFRQVVSTNFPLTTFTPNPDSEIARHVAQFQSLRQTKELCA
>gnl|CDD|236730 PRK10641, btuB, TonB-dependent vitamin B12 receptor BtuB
MIKKASLLTALSVTAFSGWAQDTSPDTLVVTANRFQQPVSTVLAPTTVVTRDDIDRWQSKSVNDVLRRLP
GVDIAQNGGLGQLSSLFIRGTNSSHVLVLIDGVRLNQAGISGSADLSQIPISLVQRIEYIRGPRSAVYGS
DAIGGVVNIITTRDKPGTTLSAGWGSNGYQNYDGSTQQQLGDNTRVTLAGDYTYTKGFDVVAYGNTGTQA
QPDRDGFMSKTLWGGLEHQFNDQWSGFVRGYGYDNRTDYDAYYSPGSPLIDTRQLYSQSWDAGLRYNGGI
YSSQLIASYSHSKDYNYDPHYGRYDSSATLDDMKQYNVQWGNTVQVGHGNISAGVDWQKQTTTPGTGYVP
DGYDQRNTGIYLTGQQQIGDVTLEGAARSDDNSQFGWHGTWQTSAGWEFIDGYRFIASYGTAFKAPNLGQ
LYGFYGNPNLKPEESKQWEGGFEGLTGPVNWRLSGYRNDIDNLIDYDDHTLKYYNVGKATIKGVEWTGNF
DTGPLTHQVTLDYVDPRNAITDEPLARRAKQQVKYQLDWQLYDFDWGVTYQYLGTRYDKDYSTYPYQTVK
LGGVSLWDLAVSYPVTSHLTVRGKIANLFDKDYETVYGYQTAGREYTLSGSYTF
>gnl|CDD|182611 PRK10642, PRK10642, proline/glycine betaine transporter ProP
ITLRDVTIIDDGKLRKAITAASLGNAMEWFDFGVYGFVAYALGKVFFPGADPSVQMIAALATFSVPFLIR
PLGGLFFGMLGDKYGRQKILAITIVIMSISTFCIGLIPSYATIGIWAPILLLLCKMAQGFSVGGEYTGAS
IFVAEYSPDRKRGFMGSWLDFGSIAGFVLGAGVVVLISTIVGEANFLDWGWRIPFFIALPLGIIGLYLRH
ALEETPAFQQHVDKLEQGDREGLQDGPKVSFKEIATKHWRSLLTCIGLVIATNVTYYMLLTYMPSYLSHN
LHYSEDHGVLIIIAIMIGMLFVQPVMGLLSDRFGRRPFVILGSVALFVLAIPAFILINSNVIGLIFAGLL
MLAVILNCFTGVMASTLPAMFPTHIRYSALAAAFNISVLVAGLTPTLAAWLVESTQNLMMPAYYLMVVAV
IGLITGVTMKETANRPLKGATPAASDIQEAKEILVEHYDNIEQKIDDIDQEIAELQAKRTRLVQQHPRID
>gnl|CDD|182612 PRK10643, PRK10643, two-component system response regulator PmrA
MKILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKK
YTLPVLILTARDTLEDRVAGLDVGADDYLVKPFALEELHARIRALIRRHQGQGENELQVGNLTLNLGRQQ
VWLDGQELILTPKEFALLSRLMLKAGSPVHREILYQDIYNWDDEPSSNTLEVHIHNLRDKVGKDRIRTVR
GFGYMLVANEEN
>gnl|CDD|182613 PRK10644, PRK10644, arginine/agmatine antiporter
MSSDADAHKVGLIPVTLMVAGNIMGSGVFLLPANLASTGGIAIYGWLVTIIGALGLSMVYAKMSSLDPSP
GGSYAYARRCFGPFLGYQTNVLYWLACWIGNIAMVVIGVGYLSYFFPILKDPLVLTITCVVVLWIFVLLN
IVGPKMITRVQAVATVLALIPIVGIAVFGWFWFRGETYMAAWNVSGLGTFGAIQSTLNVTLWSFIGVESA
SVAAGVVKNPKRNVPIATIGGVLIAAVCYVLSSTAIMGMIPNAALRVSASPFGDAARMALGDTAGAIVSF
CAAAGCLGSLGGWTLLAGQTAKAAADDGLFPPIFARVNKAGTPVAGLLIVGVLMTIFQLSSISPNASKEF
GLVSSVSVIFTLVPYLYTCAALLLLGHGHFGKARPAYLAVTLIAFVYCIWAVVGSGAKEVMWSFVTLMVI
TAFYALNYNRLHKNPYPLDAPISKD
>gnl|CDD|182614 PRK10645, PRK10645, divalent cation tolerance protein CutA
MLDEKSSNTDAVVVLCTAPDEATAQDLAAKVLAEKLAACVTLLPGATSLYYWEGKLEQEYEVQMLLKTTV
SHQQALLECLKSHHPYQTPELLVLPVTHGDTDYLSWLNASLR
>gnl|CDD|182615 PRK10646, PRK10646, tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex ATPase subunit type 1 TsaE
MMNRVIPLPDEQATLDLGARVAKACDGATVIYLYGDLGAGKTTFSRGFLQALGHQGNVKSPTYTLVEPYT
LDNLMVYHFDLYRLADPEELEFMGIRDYFANDAICLVEWPQQGAGVLPDPDVEIHLDYQAQGREARVSAV
SSAGELLLARLAG
>gnl|CDD|182616 PRK10647, PRK10647, ferric iron reductase involved in ferric hydroximate transport; Provisional
MAYRSAPLYEDIIWRTHLQPSDAGLADAIRELIAKTREHLLDFIRLDEPAPLNAMTLAQWSSPNAFSSLL
AVYSDHIYRNQPTLKRENKPLYSLWAQWYIGLMVPPLMLALLTQPQALDVSPEHFHVEFHETGRAACFWY
DVHEDKNATPLSPQERMETLISQALIPVVQALEATGEINGKLIWSNTGYLINWYLTEMKQLLGEALYESL
RQALFFEKTLPNGQDNPLWRTVVLRDGLLVRRTCCQRYRLPDVQQCGDCTLK
>gnl|CDD|182617 PRK10649, PRK10649, phosphoethanolamine transferase CptA
MHSTKVQAKPLFSWKALGWALLFFWFFSTLLQAIIYISGYSGTNGFRDALLFSSLWLIPVFLFPRRIRII
AAVIGVVLWAASLAALCYYVIYGQEFSQSVLFVMFETNTNEASEYLSQYFSLKIVLIALAYTAVAVLLWT
RLRPVYIPWPWRYVVSFALLYGLILHPIAMNTFIKHKPFEKTLDKLASRMEPAAPWQFLTGYYQYRQQLN
SLQKLLNENAALPPLANLKDESGNAPRTLVLVIGESTQRGRMSLYGYPRETTPELDALHKTDPGLTVFNN
VVTSRPYTIEILQQALTFADEKNPDLYLTQPSLMNMMKQAGYKTFWITNQQTMTARNTMLTVFSRQTDKQ
YYMNQQRTQNAREYDTNVLKPFSEVLADPAPKKFIIVHLLGTHIKYKYRYPENQGKFDDRTGHVPPGLNA
DELESYNDYDNANLYNDHVVASLIKDFKATDPNGFLVYFSDHGEEVYDTPPHKTQGRNEDNPTRHMYTIP
FLLWTSEKWQAAHPRDFSQDVDRKYSLAELIHTWSDLAGLSYDGYDPTRSLVNPQFKETPRWIGNPYKKN
ALIDYDTLPYGDQVGNQ
>gnl|CDD|182618 PRK10650, PRK10650, multidrug/spermidine efflux SMR transporter subunit MdtI
MQQFEWIHAAWLALAIVLEIVANIFLKFSDGFRRKIYGILSLAAVLAAFSALSQAVKGIDLSVAYALWGG
FGIAATLAAGWILFGQRLNRKGWIGLVLLLAGMVMIKLA
>gnl|CDD|182619 PRK10651, PRK10651, transcriptional regulator NarL; Provisional
MSNQEPATILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLET
LDKLREKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQAAAGEMVLSEALTPVLAA
SLRANRATTERDVNQLTPRERDILKLIAQGLPNKMIARRLDITESTVKVHVKHMLKKMKLKSRVEAAVWV
HQERIF
>gnl|CDD|182620 PRK10653, PRK10653, ribose ABC transporter substrate-binding protein RbsB
MNMKKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAK
ELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSHIASDNVAGGKMAGDF
IAKKLGEGAKVIQLEGIAGTSAARERGEGFKQAVAAHKFNVLASQPADFDRTKGLNVMQNLLTAHPDVQA
VFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGIKAVNRGKLAATIAQQPDQIGAIGVETADKVLKGE
KVEAKIPVDLKLVTK
>gnl|CDD|182621 PRK10654, dcuC, C4-dicarboxylate transporter DcuC; Provisional
MLTFIELLIGVVVIVGVGRYIIKGYSATGVLFVGGLLLLIISALMGHKVLPASVTSTGYSATDIVEYVKI
LLMSRGGDLGMMIMMLCGFAAYMTHIGANDMVVKLASKPLQYINSPYLLMIAAYFVACLMSLAVSSATGL
GVLLMATLFPVMVNVGISRGAAAAICASPAAIILSPTSGDVVLAAEASEMPLIDFAFKTTLPISIAAIIG
MAIAHFFWQRYLDKKENISHEMLDVSEITTTAPAFYAILPFTPIIGVLIFDGKWGPQLHIITILVICMLL
AAVLEFLRSFNTKKVFSGLEVAYRGMADAFAGVVMLLVAAGVFAQGLSTIGFIQSLISLATSFGSAGIIL
MLVLVILTMLAAITTGSGNAPFYAFVELIPKLAHSSGINPAYLTIPMLQASNLGRTISPVSGVVVAVAGM
AKISPFEVVKRTSVPVLVGLLIVIVATEIMVPGTA
>gnl|CDD|182622 PRK10655, potE, putrescine transporter; Provisional
MSAKSNKMGVVQLTILTAVNMMGSGIIMLPTKLAQVGTISILSWLVTAVGSMALAYAFAKCGMFSRKSGG
MGGYAEYAFGKSGNFMANYTYGVSLLIANVAIAISAVGYGTELFGATLSPVQICLATIGVLWLCTVANFG
GARITGQISSVTVWGVIIPVVGLSIIGWFWFSPSLYVAAWNPHHLPFFSAVGSSIAMTLWAFLGLESACA
NSDAVENPERNVPIAVLGGTLGAAVIYIVSTNVIAGIVPNMELANSTAPFGLAFAQMFNPTVGKIVMALM
VMSCCGSLLGWQFTIAQVFKSSADEGYFPKIFSRVTKVDAPVQGMLIIVVIQSLLSLMTISPSLNSQFNV
LVNLAVVTNIIPYILSMAALVIIQKVANVPPSKAKVANFIAFVGALYSFYALYSSGEEAMLYGSIVTFLG
WTLYGLISPRFELKNKHG
>gnl|CDD|236731 PRK10658, PRK10658, putative alpha-glucosidase; Provisional
MKFSDGNWLIRPGLNLIHPVQVYDVEQQDNELVVYAPPRDVRERGDTLDTPLFTIRFSSPQEGVIGVRIE
HFQGALDNGPHFPLNILQDVKVEIEETEDYAELKSGNLSARVSKGEFWSLDFLRNGRRLTGSQLKSNGYV
QDNDGRNYMREQLDLGVGETVYGLGERFTAFVKNGQTVDIWNRDGGTSSEQAYKNIPFYLTNRGYGVFVN
HPQCVSFEVGSEKVSKVQFSVEGEYLEYFVIDGPTPKEVLDRYTALTGRPALPPAWSFGLWLTTSFTTNY
DEATVNSFIDGMAERDLPLHVFHFDCFWMKEFQWCDFEWDPRTFPDPEGMLKRLKAKGLKICVWINPYIA
QKSPLFKEGKEKGYLLKRPDGSVWQWDKWQPGMAIVDFTNPDACKWYADKLKGLLDMGVDCFKTDFGERI
PTDVVWFDGSDPQKMHNYYTYLYNKTVFDVLKETRGEGEAVLFARSATVGGQQFPVHWGGDCYSNYESMA
ESLRGGLSLGLSGFGFWSHDIGGFENTATADVYKRWCAFGLLSSHSRLHGSKSYRVPWAYDEEAVDVVRF
FTKLKCRLMPYLYREAAEAHERGTPMMRAMVLEFPDDPACDYLDRQYMLGDSLLVAPVFSEAGDVEYYLP
EGRWTHLLTGEEVEGGRWHKEQHDFLSLPLLVRPN
>gnl|CDD|182625 PRK10659, PRK10659, acetate uptake transporter
MGNTKLANPAPLGLMGFGMTTILLNLHNAGFFALDGIILAMGIFYGGIAQIFAGLLEYKKGNTFGLTAFT
SYGSFWLTLVAILLMPKMGLADAPNAQFLGVYLGLWGVFTLFMFFGTLKAARALQFVFFSLTVLFALLAI
GNITGNAAIIHFAGWIGLICGASAIYLAMGEVLNEQFGRTVLPIGESH
>gnl|CDD|182626 PRK10660, tilS, tRNA(Ile)-lysidine synthetase; Provisional
DNMLTLTLNRQLLTSRQILVAFSGGLDSTVLLHLLVQWRTENPGVTLRAIHVHHGLSPNADSWVKHCEQV
CQQWQVPLVVERVQLDQRGLGIEAAARQARYQAFARTLLPGEVLVTAQHLDDQCETFLLALKRGSGPAGL
SAMAEVSPFAGTRLIRPLLARSREELEQYAQAHGLRWIEDDSNQDDRYDRNFLRLRVLPLLQQRWPHFAE
ATARSAALCAEQEQLLDELLAEDLAHLQTPDGTLSIDPLLAMSDARRAAILRRWLAGQGAPMPSRDQLQR
IWQEVALAREDAEPCLRLGAFEIRRYQSQLWLIKSVAGQSETILPWQTWLQPLELPAGLGSLQLVAGGDV
RPPRADEAVSVRFKAQGLLHIVGRNHGRKLKKIWQELGVPPWLRDRTPLLFYGETLIAAAGVFVTQEGQA
EEGENGVSLVWQKTLS
>gnl|CDD|236732 PRK10662, PRK10662, beta-lactam binding protein AmpH; Provisional
MKRSLLFSAALCAAALTSAHAAQPAADPLLASDIVDRYAEHIFYGSGATGMALVVIDGNQRVFRSYGETR
PGNNVRPQLDSLIRIASITKLMTSEVLVKLADDGTVKLTDPLSKYAPPGARVPTYNGQPITLLNLATHTS
ALPREQPGGAAHRPVFVWPTREQRWKWLSTAKLKAAPGTQAAYSNLAFDLLADALAKAAGKPYTQLLREK
ITRPLGMKDTTFTPSPDQCARLMVGEKGASPCNNTLAAIGSGGVYSTPGDMMRWMQQFLSSDNYQRSQQA
DRMQTLIYQRAQLTSVIGMDVPGKADALGLGWVYMAPKDGRPGIIQKTGGGGGFITYMAMIPQRNIGVFV
VVTRSPLTRFSNMSDGVNDLVTELSGNK
>gnl|CDD|182628 PRK10663, PRK10663, cytochrome o ubiquinol oxidase subunit III; Provisional
MATDTLTHATAHAHEHGHHDAGATKVFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVL
VETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHHLIVEGMGPDRSGFLSAFF
ALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM
>gnl|CDD|170612 PRK10664, PRK10664, DNA-binding protein HU-beta
MNKSQLIDKIAAGADISKAAAGRALDAIIASVTESLKEGDDVALVGFGTFAVKERAARTGRNPQTGKEIT
IAAAKVPSFRAGKALKDAVN
>gnl|CDD|182629 PRK10665, PRK10665, P-II family nitrogen regulator
MKLVTVIIKPFKLEDVREALSSIGIQGLTVTEVKGFGRQKGHAELYRGAEYSVNFLPKVKIDVAIADDQL
DEVIDIISKAAYTGKIGDGKIFVAELQRVIRIRTGEADEAAL
>gnl|CDD|182630 PRK10666, PRK10666, ammonium transporter AmtB
MKIATIKTGLASLALLPGLAMAAPAVADKADNAFMMICTALVLFMTIPGIALFYGGLIRGKNVLSMLTQV
TVTFALVCILWVVYGYSLAFGEGNAFFGNFNWLMLKNIELTAVMGSIYQYIHVAFQGSFACITVGLIVGA
LAERIRFSAVLIFVVVWLTLSYIPIAHMVWGGGLLASDGALDFAGGTVVHINAAVAGLVGAYLLGKRVGF
GKEAFKPHNLPMVFTGTAILYIGWFGFNAGSAGAANEIAALAFVNTVVATAAAILGWVFGEWALRGKPSL
LGACSGAIAGLVGVTPACGYVGVGGALIIGVVAGLAGLWGVTMLKRWLRVDDPCDVFGVHGVCGIVGCIL
TGIFAASSLGGVGYAEGVTMGHQVLVQLESIAITIVWSGVVAFIGYKLADLTVGLRVPEEQEREGLDVNS
HGENAYNA
>gnl|CDD|182631 PRK10667, PRK10667, Hha toxicity modulator TomB
MDEYSPKRHDIAQLKFLCETLYHECLANLGESNHGWVNDPTSAVNLQLNELIEHIATFALNFKIKYPEDS
KLIEQIDEYLDDTYMLFSSYGINDQDLQKWRKSGNRLFRCFVNETKCNPASL
>gnl|CDD|182632 PRK10668, PRK10668, DNA-binding transcriptional repressor AcrR; Provisional
MARKTKQQAQETRQHILDAALRLFSQQGVSATSLADIAKAAGVTRGAIYWHFKNKSDLFSEIWELSESKI
GELELEYQAKFPDDPLSVLREILIYILEATVTDERRRLLMEIIFHKCEFVGEMAVVQQAQRNLCLESYDR
IEQTLKHCIEAKQLPANLMTRRAAIIMRGYISGLMENWLFAPESFDLKKEARDLVDILLEMLLLSPTLRN
PATNE
>gnl|CDD|182633 PRK10669, PRK10669, putative cation:proton antiport protein; Provisional
MHHATPLITTIVGGLVLAFILGMLANRLRISPLVGYLLAGVLAGPFTPGFVADTKLAPELAELGVILLMF
GVGLHFSLKDLMAVKSIAIPGAIAQIAVATLLGMALSAVLGWSLMTGIVFGLCLSTASTVVLLRALEERQ
LIDSQRGQIAIGWLIVEDLVMVLTLVLLPAVAGMMEQGDVGFATLAVDLGITIGKVIAFIAIMMLVGRRL
VPWILARSAATGSRELFTLSVLALALGIAFGAVELFDVSFALGAFFAGMVLNESELSHRAAHDTLPLRDA
FAVLFFVSVGMLFDPMILIQQPLAVLATLAIIVFGKSLAAFFLVRLFGHSRRTALTIAASLAQIGEFAFI
LAGLGMALNLLPQAGQNLVLAGAILSIMLNPVLFTLLERYLAKTETLEEQTLEEAIEEEKQIPVDICNHA
LLVGYGRVGSLLGEKLLAAGIPLVVIETSRTRVDELRERGIRAVLGNAANEEIMQLAHLDCARWLLLTIP
NGYEAGEIVASAREKRPDIEIIARAHYDDEVAYITERGANQVVMGEREIARTMLELLETPPAGEVVTG
>gnl|CDD|182634 PRK10670, PRK10670, Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK
MTPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMKHLAVAVTPVAGQL
DLKKVAKALGAKKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELA
AGDLAKLLDAKFADIARRD
>gnl|CDD|182635 PRK10671, copA, copper-exporting P-type ATPase CopA
MSQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGTASAEALIETIKQAGYDASVSHPKA
KPLTESSIPSEALTAASEELPAATADDDDSQQLLLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTAL
VMGSASPQDLVQAVEKAGYGAEAIEDDAKRRERQQETAQATMKRFRWQAIVALAVGIPVMVWGMIGDNMM
VTADNRSLWLVIGLITLAVMVFAGGHFYRSAWKSLLNGSATMDTLVALGTGAAWLYSMSVNLWPQWFPME
ARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARVVTDEGEKSVPLADVQPGMLLRLT
TGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVR
QAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVLIIACPCALGLATPMS
IISGVGRAAEFGVLVRDADALQRASTLDTLVFDKTGTLTEGKPQVVAVKTFNGVDEAQALRLAAALEQGS
SHPLARAILDKAGDMTLPQVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQVDTKALEAEITAQASQGA
TPVLLAVDGKAAALLAIRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDG
KAEAIKRLQSQGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRAT
LRNMKQNLLGAFIYNSLGIPIAAGILWPFTGTLLNPVVAGAAMALSSITVVSNANRLLRFKPKE
>gnl|CDD|236733 PRK10672, PRK10672, endolytic peptidoglycan transglycosylase RlpA
MRKQWLGIGIAAGLLAACTSDDGQQQTVSAPQPAVCNGPVVEISGAEPRYEPYNPTANQDYQRNGKSYKI
VQDPSNFSQAGLAAIYDAEAGSNLTASGERFDPNALTAAHPTLPIPSYVRVTNLANGRMIVVRINDRGPY
GPGRVIDLSRAAADRLNTSNNTKVRIDPIIVAPDGSLSGPGTAGTTVAKQSYALPARPDLSGGMGTPSVQ
PAPAPQGDVLPVSNSTLKSEDPTGAPVTSSGFLGAPTTLAPGVLEGSEPTPTAPSSAPATAPAAAAPQAA
ATSSSASGNFVVQVGAVSDQQRAQQWQQSLSQRFGVPGRVTQNGAVYRVQLGPFASRQQASALQQRLQTE
AQQQSFITTAQ
>gnl|CDD|182637 PRK10673, PRK10673, esterase
MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQD
LLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGAT
TRQQAAAIMRQHLNEEGVIQFLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVT
EAYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYLNDK
>gnl|CDD|236734 PRK10674, PRK10674, deoxyribodipyrimidine photolyase; Provisional
MTTHLVWFRNDLRLHDNLALAAACRDPSARVLALFIATPAQWAAHDMAPRQAAFINAQLNALQIALAEKG
IPLLFHEVDDFAASVEWLKQFCQQHQVTHLFYNYQYEVNERQRDAAVERALRNVVCQGFDDSVLLPPGSV
MTGNHEMYKVFTPFKNAFLKRLREGDPECVPAPKVRSSGAIEPLPPIPFNYPQQSFDTALFPVGEKAAIA
QLRQFCQQGAGEYEQQRDFPAVDGTSRLSAYLATGVLSPRQCLHRLLAEQPQALDGGAGSVWLNELIWRE
FYRHLMVAYPSLCKHRPFIAWTDRVQWQSNPAHLQAWQQGKTGYPIVDAAMRQLNSTGWMHNRLRMITAS
FLVKDLLIDWREGERYFMSQLIDGDLAANNGGWQWAASTGTDAAPYFRIFNPTTQGERFDRDGEFIRRWL
PELRDVPGKAIHQPWRWAEKAGVTLDYPQPIVDHKQARLATLAAYEAARKGA
>gnl|CDD|182639 PRK10675, PRK10675, UDP-galactose-4-epimerase; Provisional
MRVLVTGGSGYIGSHTCVQLLQNGHDVVILDNLCNSKRSVLPVIERLGGKHPTFVEGDIRNEALLTEILH
DHAIDTVIHFAGLKAVGESVQKPLEYYDNNVNGTLRLISAMRAANVKNLIFSSSATVYGDQPKIPYVESF
PTGTPQSPYGKSKLMVEQILTDLQKAQPDWSIALLRYFNPVGAHPSGDMGEDPQGIPNNLMPYIAQVAVG
RRDSLAIFGNDYPTEDGTGVRDYIHVMDLADGHVAAMEKLANKPGVHIYNLGAGVGSSVLDVVNAFSKAC
GKPVNYHFAPRREGDLPAYWADASKADRELNWRVTRTLDEMAQDTWHWQSRHPQGYPD
>gnl|CDD|182640 PRK10676, PRK10676, DNA-binding transcriptional regulator ModE; Provisional
MQAEILLTLKLQQRLFADPRRISLLKQIALTGSISQGAKLAGISYKSAWDAINEMNQLSEHILVERATGG
KGGGGAVLTRYGERLIQLYDLLAQIQQKAFDVLDDDALPLDSLLAAISRFSLQTSARNQWFGTITARDHQ
QVQQHVDVLLADGKTRLKVAITAQSAERLGLDEGKEVLVLIKAPWVGITQDPAVAQAADNQLPGTISHIE
RGAEQSEVLMALPDGQTLCATVPNNEAARLSLQQGDAVTAYFNADRVIIATLC
>gnl|CDD|182641 PRK10677, modA, molybdate transporter periplasmic protein; Provisional
MARKWLRLFAGAVLSFAVAGNALADEGKITVFAAASLTNALQDIAAQYKKEKGVDVVSSFASSSTLARQI
EQGAPADLFISADQKWMDYAVDKKAIDTATRYTLLGNSLVVVAPKASEQKDFTIDKKTDWKSLLNGGRLA
VGDPDHVPAGIYAKEALQKLGAWDTLSPKLARAEDVRGALALVERNEAPLGIVYGSDAVASKKVKVVGTF
PEDSHKPVEYPMAIVKGHNNATVKAFYDYLKGPQAAAIFKRYGFTTK
>gnl|CDD|182642 PRK10678, moaE, molybdopterin synthase catalytic subunit MoaE
MAETRIVVGPAPFSVGEEYPWLAERDEDGAVVTFTGKVRNHNLGDSVKALTLEHYPGMTEKALAEIVDEA
RSRWPLGRVTVIHRVGELWPGDEIVFVGVTSAHRSSAFEAGQFIMDYLKTRAPFWKREATPEGDRWVEAR
DSDQQAAKRW
>gnl|CDD|182643 PRK10680, PRK10680, molybdopterin biosynthesis protein MoeA; Provisional
MEFTAGLMSLETALTEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLAS
GQPLPVAGKAFAGQPFHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAEVRSGQNIRRRG
EDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVH
LMLEQLGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKP
GKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNTASGLPPRQRVRTASRLKKTPGRLDFQR
GILQRNADGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEVGEWVEVEPFNALFGGL
>gnl|CDD|182644 PRK10681, PRK10681, DNA-binding transcriptional repressor DeoR; Provisional
METRRDERIGQLLQALKRSDKLHLKDAAALLGVSEMTIRRDLNAHSAPVVLLGGYIVLEPRSASHYLLSD
QKSRLVEEKRRAAQLAATLVEPNQTLFFDCGTTTPWIIEAIDNELPFTAVCYSLNTFLALQEKPHCRAIL
CGGEFHASNAIFKPLDFQQTLDNICPDIAFYSAAGVHVSKGATCFNLEELPVKHWAMAMAQKHVLVVDHS
KFGKVRPARMGDLTRFDTVVSDRCPDDEFVKYAQAQRIKLMY
>gnl|CDD|182645 PRK10682, PRK10682, putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional
MTALNKKWLSGLVAGALMAVSVGTLAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEG
KLMAGSTGFDLVVPSASFLERQLTAGVFQPLDKSKLPNWKNLDPELLKLVAKHDPDNKYAMPYMWATTGI
GYNVDKVKAVLGEDAPVDSWDLVLKPENLEKLKSCGVSFLDAPEEIFATVLNYLGKDPNSTKADDYTGPA
TDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQASNRAKEAKNGVNVSYSIPKEGALAFFDVF
AMPADAKNKDEAYQFLNYLLRPDVIAHISDHVFYANANKAATPLVSAEVRDNPGIYPPADVRAKLFTLKV
QDPKIDRVRTRAWTKVKSGK
>gnl|CDD|182646 PRK10683, PRK10683, putrescine transporter subunit: membrane component of ABC superfamily; Provisional
MSTLEPPARSKPPGGFKLWLARLQMKHGRKLVIALPYLWLILLFLLPFLIVFKISLAEMARAIPPYTDLM
EWADGQLSITLNLGNFLQLTDDPLYFDAYLQSLQVAAISTLCCLLIGYPLAWAVAHSKPSTRNILLLLVI
LPSWTSFLIRVYAWMGILKNNGVLNNFLLWLGVIDQPLTILHTNLAVYIGIVYAYLPFMVLPIYTALTRI
DYSLVEAALDLGARPLKTFFSVIVPLTKGGIIAGSMLVFIPAVGEFVIPELLGGPDSIMIGRVLWQEFFN
NRDWPVASAVAIIMLLLLIVPIMWFHKHQQKSVGEHG
>gnl|CDD|236735 PRK10684, PRK10684, HCP oxidoreductase, NADH-dependent; Provisional
MTMPTPQCPNRMQVHSIVQETPDVWTISLICHDFYPYRAGQYALVSIRNSAETLRAYTLSSTPGVSEFIT
LTVRRIDDGVGSQWLTRDVKRGDYLWLSDAMGEFTCDDKAEDKYLLLAAGCGVTPIMSMRRWLLKNRPQA
DVQVIFNVRTPQDVIFADEWRQLKQRYPQLNLTLVAENNATEGFIAGRLTRELLQQAVPDLASRTVMTCG
PAPYMDWVEQEVKALGVTADRFFKEKFFTPVAEAATSGLTFTKLQPAREFYAPVGTTLLEALESNKVPVV
AACRAGVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYVLACSCHPQGDLVLA
>gnl|CDD|182648 PRK10687, PRK10687, purine nucleoside phosphoramidase; Provisional
MAEETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAA
KIAEQEGIAEDGYRLIMNTNRHGGQEVYHIHMHLLGGRPLGPMLAHKGL
>gnl|CDD|182649 PRK10689, PRK10689, transcription-repair coupling factor; Provisional
MPEQYRYTLPVKAGDQRQLGELTGAACATEVAEIAERHAGPVVLIAPDMQNALRLHDEIQQFTDQMVMNL
ADWETLPYDSFSPHQDIISSRLSTLYQLPTMQRGVLILPVNTLMQRVCPHSFLHGHALVMKKGQRLSRDA
LRAQLEQAGYRHVDQVMEHGEYATRGALLDLFPMGSEEPYRIDFFDDEIDSLRVFDVDSQRTLEEVEAIN
LLPAHEFPTDKAAIELFRSQWRDTFEVKRDAEHIYQQVSKGTLPAGIEYWQPLFFSEPLPPLFSYFPANT
LLVNTGDLETSAERFWADTLARFENRGVDPMRPLLPPESLWLRVDELFSELKNWPRVQLKTEHLPTKAAN
TNLGYQKLPDLAVQAQQKAPLDALRRFLESFDGPVVFSVESEGRREALGELLARIKIAPKRIMRLDEASD
RGRYLMIGAAEHGFIDTVRNLALICESDLLGERVARRRQDSRRTINPDTLIRNLAELHPGQPVVHLEHGV
GRYAGMTTLEAGGIKGEYLMLTYANDAKLYVPVSSLHLISRYAGGAEENAPLHKLGGDAWSRARQKAAEK
VRDVAAELLDIYAQRAAKEGFAFKHDREQYQLFCDSFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDV
GFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQHYDNFRDRFANWPVRIEMLSRFRSAKEQTQILAEAA
EGKIDILIGTHKLLQSDVKWKDLGLLIVDEEHRFGVRHKERIKAMRADVDILTLTATPIPRTLNMAMSGM
RDLSIIATPPARRLAVKTFVREYDSLVVREAILREILRGGQVYYLYNDVENIQKAAERLAELVPEARIAI
GHGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLRGRVGRSHHQA
YAWLLTPHPKAMTTDAQKRLEAIASLEDLGAGFALATHDLEIRGAGELLGEEQSGQMETIGFSLYMELLE
NAVDALKAGREPSLEDLTSQQTEVELRMPSLLPDDFIPDVNTRLSFYKRIASAKNENELEEIKVELIDRF
GLLPDPARNLLDIARLRQQAQKLGIRKLEGNEKGGFIEFAEKNHVDPAWLIGLLQKQPQHYRLDGPTRLK
FIQDLSERKTRIEWVRQFMRELEENAI
>gnl|CDD|182650 PRK10691, PRK10691, fumarylacetoacetate hydrolase family protein
MYQHRNWQGALLDYPVSKVVCVGSNYAKHIKEMGSATPEEPVLFIKPETALCDLRQPLAIPKDFGSVHHE
VELAVLIGATLRQATEEHVRKAIAGYGVALDLTLRDLQGKMKKAGQPWEKAKAFDNSCPISGFIPVAEFT
GDPQNTTLGLSVNGEVRQQGNTADMIHPIVPLIAYMSRFFTLRAGDVVLTGTPEGVGPLQSGDELTVTFN
GHSLTTRVL
>gnl|CDD|182651 PRK10692, PRK10692, stress response protein YchH
MKRKNASLLGNVLMGLGLVVMVVGVGYSILNQLPQLNLPQFFAHGALLSIFVGALLWLAGARVGGREQVA
DRYWWVRHYDKRCRRSDNRRHS
>gnl|CDD|182652 PRK10693, PRK10693, two-component system response regulator RssB
VLAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQD
VLLKPVKDLNRLREMVFACLYPSMFNSRVEEEERLFRDWDALVDNPAAAAKLLKQLQPPVQQVIAHCRVN
YRQLVAADKPGLVLDIAALSDNDLAFYCLDVTRAGDNGVLAALLLRALFNGLLQEQLAHQNQRLPELGAL
LKQVNHLLRQANLPGQFPLLVGYYHRELKNLILVSAGLNATLNTGEHQVQLSNGVPLGTLGNAYLNQLSQ
RCDAWQCQIWGAGGRLRLMLSAE
>gnl|CDD|236736 PRK10694, PRK10694, acyl-CoA thioester hydrolase YciA
MSTTHNVPQGELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAV
GDVVCCYARCVKTGTTSISINIEVWVKKVASEPIGQRYKATEALFTYVAVDPEGKPRALPVGK
>gnl|CDD|182654 PRK10695, PRK10695, YdbH family protein
KYKAVLALLLLLILLPLTLLLTLPLWLPTLAGIWLPVGTRIALPESPRWTRGGLRLPDLRYLVGDCPLAT
VSNLSLSHPSRWRLNADTVTLDSACLSKLPASEESPAAPLTLAQWQSMLPETWLNIDHLILSPWQEWAGK
LRLSLTPSRQTLRYQGEKLKLQAQLKGQQLTVSQLSVAAPEQQPPVSLNGTFTLPLVLDGLPVQGELTGT
LRLPQEPSPLDAELSWQGQSGQLIVTARGNPDPLLDLPWQFTRQQLTISDGRWYWPYGGQPLSGGVNLTL
DNWQQGLDPALISGRLNLLTQGKAGKGNAVLTLGPGKLSMDNSQLPLQLTGEAKQGDLILYATLPAQLSG
SLLDPTLTFQPGALLRSWGRLIDTLTIDEARWPLAGVKVTRRGVDGRLQAILQAHEPYWGDFNLHLDGQA
NDFLPDAGRWQWRYWGSGSLPPLAARWDVAGRGEWHDNLITLNELSTGFDQLQYGGVTVEKPRLTLTKPL
RWQRDAQHPSFRGALQLDAGKTEFTYGGYLPPSTLKLSVDGRDPTNFQLKGDLQAGAIGPIRLNGRWDGE
RLRGQAWWPKQSLTVFQPLLPPDWKMNLRDGTLYAQAAFSAARGQGFEAGGHWVVKNGSAWMPDGEINGV
DFVLPFRLQDGAWQLGTRGPVTLRIAEINNLFTMQNITADLQGTYPYSEAKPLTLSNVSVDVLDGHLSMS
QLRLPQHDPALLRLNNIDLSELLTALKPKQFAMSGKVNGALPLWLNNPQWIVKDGWLANAGPLTLRLDKD
LADAIVKDNMTAGAAIDWLRYMEISRSWAKVNLDNLGELTLQAKITGTNRVDGKKRTVNLNYTHQENIFQ
LWRSLRFGDNLQQWLEQNA
>gnl|CDD|236737 PRK10696, PRK10696, tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional
ESYEFNKLQKRLRRQVGQAIADFNMIEEGDRVMVCLSGGKDSYTLLDILLNLQKRAPINFELVAVNLDQK
QPGFPEHVLPEYLESLGVPYHIEEQDTYSIVKEKIPEGKTTCSLCSRLRRGILYRTARELGATKIALGHH
RDDILETLFLNMFYGGKLKAMPPKLLSDDGKHIVIRPLAYVAEKDIIKFAEAKEFPIIPCNLCGSQENLQ
RQVVKEMLRDWEKEYPGRIETMFRALQNVVPSHLLDRNLFDFKGLTRD
>gnl|CDD|182656 PRK10697, PRK10697, envelope stress response membrane protein PspC
AGINLNKKLYRIPQQGMVKGVCAGIAHYFDVPVKLVRIIVVLSIFFGLFVFTLVAYIILSFALDPMPDNM
AFGEQQPSSSELLDEVDRELAAGEQRLREMERYVTSDTFTLRSRFRQL
>gnl|CDD|182657 PRK10698, PRK10698, phage shock protein PspA; Provisional
MGIFSRFADIVNANINALLEKAEDPQKLVRLMIQEMEDTLVEVRSTSARALAEKKQLTRRIEQAEAQQVE
WQEKAELALRKEKEDLARAALIEKQKLTDLIATLEHEVTLVDETLARMKKEIGELENKLSETRARQQALM
LRHQAASSSRDVRRQLDSGKLDEAMARFESFERRIDQMEAEAESHGFGKQKSLDQQFAELKADDEISEQL
AALKAKMKQDNQ
>gnl|CDD|182658 PRK10699, PRK10699, phosphatidylglycerophosphatase B; Provisional
MYSIAKRTAVGAALLLVMPLAVWISGWQWQPGEQSWWLKGLFWVTETVTQPWGILTHVLLCGWFLWCLRF
RLKAALVLFAILAAAILVGQGVKSWIKERVQEPRPFVVWLEKTHHIPVDEFYTLKRAERGELVKEQLAEQ
SNIPQWLRSHWQKETGFAFPSGHTMFAASWALLAVGLLWPRRRYKTVALLMLWATGVMGSRLLLGMHWPR
DLVVATLISWLLVTVATWLAQRICGPLTPPPEEN
>gnl|CDD|182659 PRK10700, PRK10700, 23S rRNA pseudouridine(2605) synthase RluB
MSEKLQKVLARAGHGSRREIESIIEAGRVSVDGKIATLGDRVEVTPGLKIRIDGHLISVKESAEQICRVL
AYYKPEGELCTRNDPEGRPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREY
AVRVFGQVDDAKLRQLSRGVQLEDGPAAFKTIKFSGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRL
IRVRYGDIPLPKGLPRGGWTELDLAQTNYLRELVELPPETSSKVAVEKDRRRMKANQIRRAVKRHSQVSG
GRRSGGRNN
>gnl|CDD|236738 PRK10701, PRK10701, DNA-binding transcriptional regulator RstA; Provisional
MNKIVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPK
WQGPIVLLTSLDSDMNHILALEMGACDYILKTTPPAVLLARLRLHLRQNEQATQTKGLQETSLTPYKALH
FGTLTIDPVNRQVTLAGEEISLSTADFDLLWELATHAGQIMDRDALLKNLRGVSYDGLDRSVDVAISRLR
KKLLDNAAEPYRIKTVRNKGYLFAPHAWES
>gnl|CDD|182661 PRK10702, PRK10702, endonuclease III; Provisional
MNKAKRLEILTRLRDNNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVE
GVKTYIKTIGLYNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTH
IFRVCNRTQFAPGKNVEQVEEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKVD
I
>gnl|CDD|236739 PRK10703, PRK10703, HTH-type transcriptional repressor PurR
MATIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSE
APYFAEIIEAVEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEEYRHI
PMVVMDWGEAKADFTDAIIDNAFEGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIK
VPEEWIVQGDFEPESGYEAMQQILSQKHRPTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNA
RYFTPALTTIHQPKDRLGETAFNMLLDRIVNKREEPQTIEVHPRLVERRSVADGPFRDYRR
>gnl|CDD|182663 PRK10707, PRK10707, putative NUDIX hydrolase; Provisional
MEYRSLTLDDFLSRFQLQRPQPNRETLNQRQAAVLIPIVRRPQPTLLLTQRSIHLRKHAGQVAFPGGAVD
PTDASLIATALREAQEEVAIPPSAVEVIGVLPPVDSSTGYQVTPVVGIIPPDLPYRANEDEVAAVFEMPL
AEALHLGRYHPLDIYRRGQSHRVWLSWYEQYFVWGMTAGIIRELALQIGV
>gnl|CDD|182664 PRK10708, PRK10708, protein DsrB
MKVNDRVTVKTDGGPRRPGVVLAVEEFSEGTMYLVSLEDYPLGIWFFNEAGHQDGIFVEKAE
>gnl|CDD|182665 PRK10710, PRK10710, DNA-binding transcriptional regulator BaeR; Provisional
MTELPIDENTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGL
TLCREIRRFSDIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRRCKPQRELQQQDAE
SPLIIDESRFQASWRGKMLDLTPAEFRLLKTLSHEPGKVFSREQLLNHLYDDYRVVTDRTIDSHIKNLRR
KLESLDAEQSFIRAVYGVGYRWEADACRLV
>gnl|CDD|182666 PRK10711, PRK10711, hypothetical protein; Provisional
MMSNIWWSLPLTLIVFFAARKLAARFKFPLLNPLLVAMVVIIPFLLLTGIPYEHYFKGSEVLNDLLQPAV
VALAFPLYEQLHQIRARWKSIISICFIGSVVAMVTGTAVALWMGATPEIAASILPKSVTTPIAMAVGGSI
GGIPAISAVCVIFVGILGAVFGHTLLNAMRIRTKAARGLAMGTASHALGTARCAELDYQEGAFSSLALVI
CGIITSLIAPFLFPLILALMG
>gnl|CDD|236740 PRK10712, PRK10712, PTS system fructose-specific transporter subunits IIBC; Provisional
MKTLLIIDANLGQARAYMAKTLLGAAAAKAGLEIIDNPNDAELAIVLGDSIPNDSALNGKKVWLGDIERA
VAHPELFLSEAKGHAKPYTAPVAAAAPVAASGPKRVVAVTACPTGVAHTFMAAEAIETEAKKRGWWVKVE
TRGSVGAGNAITPEEVAAADLVIVAADIEVDLAKFAGKPMYRTSTGLALKKTAQELDKAVAEATPYQPAG
KAQTATTEGKKESAGAYRHLLTGVSYMLPMVVAGGLCIALSFAFGIEAFKEPGTLAAALMQIGGGSAFAL
MVPVLAGYIAFSIADRPGLTPGLIGGMLAVSTGSGFIGGIIAGFLAGYVAKLISTKLKLPQSMEALKPIL
IIPLISSLVVGLAMIYLIGKPVAGILEGLTHWLQTMGTANAVLLGAILGGMMCTDMGGPVNKAAYAFGVG
LLSTQTYAPMAAIMAAGMVPPLAMGLATMVARRKFDKAQQEGGKAALVLGLCFISEGAIPFAARDPMRVL
PCCIVGGALTGAISMAIGAKLMAPHGGLFVLLIPGAITPVLGYLVAIIAGTLVAGLAYAFLKRPETDAVA
KAA
>gnl|CDD|182668 PRK10713, PRK10713, 2Fe-2S ferredoxin-like protein
MARVTLRITGTQLLCQDEHPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEPLAFIQPGEIL
PCCCRAKGDIEIEM
>gnl|CDD|182669 PRK10714, PRK10714, undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
EIHPIKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAI
LLNRNYGQHSAIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASK
MINRLIQRTTGKAMGDYGCMLRAYRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKY
SFMRLINLMYDLVTCLTTTPLRLLSLLGSIIAIGGFSLAVLLVVLRLTFGPQWAAEGVFMLFAVLFTFIG
AQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTSNNEKENE
>gnl|CDD|182670 PRK10715, flk, flagella biosynthesis regulator Flk
MQPISGPPGQPPGGGRNPPSTAGDQPLSPAQRTTLERLITRIMSLTQQKSAEVWAGLRHDLGLKGDAPLL
SRHFPAAEQNLQQRLLQAQDNHATRQLLQQLTELLPQGNNRQAVSDFIRQQFGQTVLSQLSPEQLKQVLT
LLQNGQLSIPQPQQRPATDRPLLPAEHNALNQLVTKLAAATGEQPKKIWQSMLELSGVKSGELIPAKHFP
LLSQWLQARQTLSQQHAPTLESLQAALKQPLDAQEQQLLSDYAQQRFQASPQTPLTPAQVQDLLNQLFQR
RVERIQEALEPRPLQPLINPLIAPLPDTLQPLAARPGLLALVLVIVILLLLWLVL
>gnl|CDD|236741 PRK10716, PRK10716, long-chain fatty acid transporter FadL
MSQKTLFTKSALAVAVALISSQAWAAGFQLNEFSSSGLGRAYSGEGAIADDAGNVSRNPALITMFDRPTF
SAGAVYIDPDVNISGTSPSGRSLDADNIAPTAWVPNLHFVAPINDQWGWGASATSNYGLATEFNDTYAAG
SVGGKTDLETMNLNLSGAYRLNNAFSFGLGFNAVYARAKIERFAGDLGQLVAGQGQALAATAGGIPSNTE
IAHLNGNQWGFGWNAGILYELDKNNRYALTYRSEVKIDFDGDYSSDLPVAFNNIGLPLPTGTGGATQPGS
LTLNLPEMWEVSGYNRVAPQWAIHYSLAYTSWSQFQELKATSSNGDTLFQKHEGFKDAYRIALGTTYYYD
DNWTFRTGIAFDDSPVPAQNRSISIPDQDRFWLSAGTTYAFNKDASVDVGVSYMHGQSVKINEGPYQFES
EGKAWLYGTNFNYAF
>gnl|CDD|182672 PRK10717, PRK10717, cysteine synthase A; Provisional
MKIFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEG
TAGNTGIGLALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAAPYANPNNYVKGAGRLAEELVA
SEPNGAIWANQFDNPANREAHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLAD
PTGSALYSYYKTGELKAEGSSITEGIGQGRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSS
GINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFLREKGLPVPR
>gnl|CDD|236742 PRK10718, PRK10718, RpoE-regulated lipoprotein; Provisional
MKSLRLLLLALPLLLTGCSTLSSFSWSALSPWNWFGSSLEVSEQGVGGITASTPLQEQAIADALDGDYRL
RSGMKTANGNVVRFFQAMKGDQVAMVINGQQGTVSRIDVLDSDIPTAWGVKIGTPFSDLYSKAFGNCQKA
SGDDNRSVECKAPGSQHISYVFSGEWSGPEGLMPSDDTLKNWKVSKIIWRR
>gnl|CDD|236743 PRK10719, eutA, ethanolamine ammonia-lyase reactivating factor EutA
MMTEELLSVGIDIGTTTTQVIFSRLELENRASVFQVPRIEIIDKEIIYRSPIYFTPLLKQGEIDEAAIKE
LIEEEYQKAGIAPESIDSGAVIITGETARKENAREVVMALSGSAGDFVVATAGPDLESIIAGKGAGAQTL
SEERNTRVLNIDIGGGTANYALFDAGKVIDTACLNVGGRLIETDSQGRVTYISPPGQMILDELGLAITDG
RSLTGEQLQQVTRRMAELLVEVIGGALSPLAQALMTTKLLPAGVPPEIITFSGGVGDCIYRHQPADPFRY
GDIGPLLATALHEHPRLREMNVQFPAETVRATVIGAGAHTTELSGSTIWLEGVQLPLKNLPVLIPSDDEQ
EDEEDLVAAIQQALAWFDLDPETDAYALALPGSLPPSYAAIQTLAKALVDGVARFPNKPHPLIVVAEQDM
GKALGQLLRPQLPKQLPLICIDEVKVRNGDYIDIGTPLFGGSVVPVVVKTLVFPS
>gnl|CDD|236744 PRK10720, PRK10720, uracil transporter; Provisional
TRRAIGVSERPPLLQTIPLSLQHLFAMFGATVLVPILFHINPATVLLFNGIGTLLYLFICKGKIPAYLGS
SFAFISPVLLLLPLGYEVALGGFIMCGVLFCLVALIVKKAGTGWLDVLFPPAAMGAIVAVIGLELAGVAA
GMAGLLPAEGQTPDSKTIIISMVTLAVTVLGSVLFRGFLAIIPILIGVLVGYALSFAMGMVDTTPIIEAH
WFALPTFYTPRFEWFAILTILPAALVVIAEHVGHLVVTANIVKKDLLRDPGLHRSMFANGLSTVISGFFG
STPNTTYGENIGVMAITRVYSTWVIGGAAIIAILLSCVGKLAAAIQAIPLPVMGGVSLLLYGVIGASGIR
VLIESKVDYNKAQNLILTSVILIIGVSGAKVNIGAAELKGMALATIVGIGLSLIFKLISKLRPEEEVLDA
EDADITDK
>gnl|CDD|170660 PRK10721, PRK10721, hypothetical protein; Provisional
MGLKWTDSREIGEALYDAYPDLDPKTVRFTDMHQWICELEDFDDDPQASNEKILEAILLVWLDEAE
>gnl|CDD|236745 PRK10722, PRK10722, two-component system QseEF-associated lipoprotein QseG
QLVVLRHIFQRLLLRRLWLSGLPCLLLAGCVQNANKPAASTAAEEKIPEYQLADYRSTECDDIWALQGKA
AENNPLYWLRAMDCADRLMPAQARAQAKRLPDDSWQNAFKQGILLADAKITPAERRQIVERLNAYSLQIP
AQVRPLYQLWRDGQALQLALAEERQRYQKLQQSSDSELDALRQQQQRLQYQLELTTRKLENLTDIERQLS
SRKQAGNFSPDTPEKPATSEESEAPAPSTDEVTPDEP
>gnl|CDD|182677 PRK10723, PRK10723, polyphenol oxidase
MSKLIVPQWPLPKGVAACSSTRIGGVSLPPYDSLNLGAHCGDNPDHVEENRKRLFAAANLPSKPVWLEQV
HGTDVLRLTGEPYASKRADASYSNTPGTVCAVMTADCLPVLFCNRAGTEVAAAHAGWRGLCAGVLEETVA
CFAAKPENILAWLGPAIGPQAFEVGPEVREAFMAKDAKASAAFIPHGDKYLADIYQLARQRLANVGVEQI
FGGDRCTVTENETFFSYRRDGTTGRMASFIWLI
>gnl|CDD|182678 PRK10724, PRK10724, type II toxin-antitoxin system RatA family toxin
MILFVGFLLMEIVMPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQMTAAVDVSKAG
ISKTFTTRNQLTSNQSILMQLVDGPFKKLIGGWKFTPLSQEACRIEFHLDFEFTNKLIELAFGRVFKELA
SNMVQAFTVRAKEVYSAR
>gnl|CDD|182679 PRK10725, PRK10725, fructose-1-phosphate/6-phosphogluconate phosphatase
MYDRYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPHA
LAREKTEAVKSMLLDSVEPLPLIEVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQH
HKPAPDTFLRCAQLMGVQPTQCVVFEDADFGIQAARAAGMDAVDVRLL
>gnl|CDD|236746 PRK10726, PRK10726, DUF3561 family protein
MQNITLTNNDSQTEDEETTWSLPGAVVGFVSWLLALAIPFLIYGSNTLFFFLYTWPFFLALMPVSVLVGI
ALHSLLRGKLLYSILFTLLTVGCLFWLLFSWLLGW
>gnl|CDD|182681 PRK10727, PRK10727, HTH-type transcriptional regulator GalR
MATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVS
DPFFGAMVKAVEQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPDAELASLMKQIPG
MVLINRILPGFENRCIALDDRYGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPAN
DRLVTFGEPDESGGEQAMTELLGRGRNFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRY
VRPRLTTVRYPIVTMATQAAELALALADNRPLPEITNVFSPTLVRRHSVSTPSLEASHHATSD
>gnl|CDD|182682 PRK10729, nudF, ADP-ribose pyrophosphatase NudF; Provisional
VTFTKNDVEIIARETLYRGFFSLDLYRFRHRLFNGEMSGEVRREIFERGHAAVLLPFDPVRDEVVLIEQI
RIAAYDTSETPWLLEMVAGMIEEGESVEDVARREAIEEAGLIVGRTKPVLSYLASPGGTSERSSIMVGEV
DATTASGIHGLADENEDIRVHVVSREQAYQWVEEGKIDNAASVIALQWLQLHHQALKNEWAK
>gnl|CDD|182683 PRK10733, hflB, ATP-dependent zinc metalloprotease FtsH
MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYI
PVNDPKLLDNLLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKAR
MLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAK
VPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLV
EMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIA
RGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAI
IGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGPEHVSTGAS
NDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRA
RQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPAGWEEPGASNNSDDNGTPKAPRPVDEPRT
PNPGNTMSEQLGDK
>gnl|CDD|182684 PRK10734, PRK10734, putative calcium/sodium:proton antiporter; Provisional
MLLATALLIIGLLLLVYGADRLVFAASILCRTFGIPPLIIGMTVVGIGTSLPEIIVSVAASLHGQRDLAV
GTALGSNITNILLILGLAALIRPFTVHSDVLRRELPLMLLVSVLAGSVLYDGQLSRSDGIFLLLLAVLWL
LFIVKIARLAERQGNDSLTREQLAELPREGGLPVAFLWLGIALIIMPMATRMVIDNATVLANYFAISELT
IGLTVIAIGTSLPELATAIAGARKGENDIAVGNIIGSNIFNIVIVLGLPALISPGEINPLAFSRDYWVML
LVSVIFALLCWRRKRRIGRGAGALLLGGFIVWLAMLYWLSPILVE
>gnl|CDD|182685 PRK10735, tldD, protease TldD; Provisional
MSLNLVSEQLLAANGLNHQDLFAILGQLAERRLDYGDLYFQSSYHESWVLEDRIIKDGSYNIDQGVGVRA
ISGEKTGFAYADQISLLALEQSAQAARTIVRDSGDGKVQTLGAVEHSPLYTSLDPLQSMSREEKLDILRR
VDKVARAADKRVQEVTASLTGVYELILVAATDGTLAADVRPLVRLSVSVLVEEDGKRERGASGGGGRFGY
EYFLADLDGEVRADAWAKEAVRMALVNLSAVAAPAGTMPVVLGAGWPGVLLHEAVGHGLEGDFNRRGTSV
FSGQVGELVASELCTVVDDGTMVDRRGSVAIDDEGTPGQYNVLIENGILKGYMQDKLNARLMGVAPTGNG
RRESYAHLPMPRMTNTYMLAGKSTPQEIIESVEYGIYAPNFGGGQVDITSGKFVFSTSEAYLIENGKVTK
PVKGATLIGSGIEAMQQISMVGNDLKLDNGVGVCGKEGQSLPVGVGQPTLKVDNLTVGGTA
>gnl|CDD|236747 PRK10736, PRK10736, DNA-protecting protein DprA
MVDTEIWLRLMSVSSLYGDKMVRIAHRLLAQSQIDAVVLQATGLTLRQAQQFLQLPRKSLESTLRWLEQP
NHHLLTADSEFYPPQLLAIADYPGALFVSGELAALHSPQLAVVGSRAHSWYGERWGRLFCEELAKNGLTI
TSGLARGIDGVAHRAALQAGGKTIAVLGNGLENIYPRRHARLAESIIEQGGALVSEFPLDTPPLAANFPR
RNRIISGLSKGVLVVEAALRSGSLVTARCALEQGRDVFALPGPIGNPGSEGPHWLIKQGAYLVTSPEDIL
ENLQFGLHWLPDAPENSFYSPDQEEVALPFPELLANVGDEVTPVDVVAERAGQPVPEVVTQLLELELAGW
IAAVPGGYVRLRRACHVRRTNVFV
>gnl|CDD|236748 PRK10737, PRK10737, peptidylprolyl isomerase
MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQ
YDENLVQRVPKDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIR
EATEEELAHGHVHGAHDHHHDHDHDGCCGGHGHDHGHEHGGEGCCGGKGNGGCGCH
>gnl|CDD|182688 PRK10738, PRK10738, OsmC family protein
MQARVKWVEGLTFLGESASGHQILMDGNSGDKAPSPMEMVLMAAGGCSAIDVVSILQKGRQDVVDCEVKL
TSERREEAPRLFTHINLHFIVTGKDLKDAAVARAVDLSAEKYCSVALMLEKAVNITHSYEVIAA
>gnl|CDD|170674 PRK10739, PRK10739, YhgN family NAAT transporter
MNEIISATVLLILIMDPLGNLPIFMSVLKHLEPKRRRAIMIRELLIALLVMLVFLFAGEKILAFLNLRTE
TVSISGGIILFLIAIKMIFPSAEGNSSGLPAGEEPFLVPLAIPLVAGPSILATLMLLSHQYPNQMGHLVI
ALLIAWGGTFVILLQSSLFLRLLGEKGVNALERLMGLILVMLSTQMFLDGIRAWMKG
>gnl|CDD|182689 PRK10740, PRK10740, high-affinity branched-chain amino acid ABC transporter permease LivH
MSEQFLYFLQQMFNGVTLGSTYALIAIGYTMVYGIIGMINFAHGEVYMIGSYVSFMIIAALMMMGIDTSW
LLVAAGFVGAIVIASAYGWSIERVAYRPVRNSKRLIALISAIGMSIFLQNYVSLTEGSRDVALPSLFNGQ
WVVGHSENFSASITTMQAVIWIVTFLAMLALTIFIRYSRMGRACRACAEDLKMASLLGINTDRVIALTFV
IGAAMAAVAGVLLGQFYGVINPYIGFMAGMKAFTAAVLGGIGSIPGAMIGGLILGIAEALSSAYLSTEYK
DVVSFALLILVLLVMPTGILGRPEVEKV
>gnl|CDD|236749 PRK10742, PRK10742, 16S rRNA (guanine(1516)-N(2))-methyltransferase RsmJ
MKICLIDETGAGDGALSVLAARWGLEHDEDNLMALVLTPEHLELRKRDEPKLGGIFVDFVGGAMAHRRKF
GGGRGEAVAKAVGIKGDYLPDVVDATAGLGRDAFVLASVGCRVRMLERNPVVAALLDDGLARGYADAEIG
GWLQERLQLIHASSLTALTDITPRPQVVYLDPMFPHKQKSALVKKEMRVFQSLVGPDLDADGLLEPARLL
ATKRVVVKRPDYAPPLAGVATPNAVVTKGHRFDIYAGTPV
>gnl|CDD|182691 PRK10743, PRK10743, heat shock chaperone IbpA
MRNFDLSPLYRSAIGFDRLFNLLENNQSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLL
VVKGAHADEQKERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEIN
>gnl|CDD|182693 PRK10745, trkD, low affinity potassium transporter Kup
MSTDNKQSLPAITLAAIGVVYGDIGTSPLYTLRECLSGQFGFGVERDAVFGFLSLIFWLLILVVSIKYLT
FVMRADNAGEGGILTLMSLAGRNTSARTTSMLVIMGLIGGSFFYGEVVITPAISVMSAIEGLEIVAPQLD
TYIVPLSIIVLTLLFMIQKHGTGMVGKLFAPIMLTWFLTLAVLGLRSIIANPEVLHALNPMWAVHFFLEY
KTVSFFALGAVVLAITGVEALYADMGHFGKFPIRLAWFTVVLPSLVLNYFGQGALLLKNPEAIKNPFFLL
APDWALIPLLILATLATVIASQAVISGVFSLTRQAVRLGYLPPMRIIHTSEMESGQIYIPFVNWLLYVAV
VIVIVSFEHSSNLAAAYGIAVTGTMVLTSILSTTVARKNWHWNKYFVALILIAFLCIDIPLFSANLDKLL
SGGWLPLSLGLVMFIVMTTWKSERFRLLRRMHEHGNSLEAMIASLEKSPPVRVPGTAVYMSRAINVIPFA
LLHNLKHNKVLHERVILLTLRTEDAPYVHNVRRVQIEQLSPTFWRVVASYGWRETPNVEEVFHRCGLEGL
SCRMMETSFFMSHESLILGKRPWYLRLRGKLFLLLQRNALRAPDQFEIPPNRVIELGTQVEI
>gnl|CDD|182694 PRK10746, PRK10746, putative transport protein YifK; Provisional
MADNKPELQRGLEARHIELIALGGTIGVGLFMGAASTLKWAGPSVLLAYIIAGLFVFFIMRSMGEMLFLE
PVTGSFAVYAHRYMSPFFGYLTAWSYWFMWMAVGISEITAIGVYVQFWFPEMAQWIPALIAVALVALANL
AAVRLYGEIEFWFAMIKVTTIIVMIVIGLGVIFFGFGNGGQSIGFSNLTEHGGFFAGGWKGFLTALCIVV
ASYQGVELIGITAGEAKNPQVTLRSAVGKVLWRILIFYVGAIFVIVTIFPWNEIGSNGSPFVLTFAKIGI
TAAAGIINFVVLTAALSGCNSGMYSCGRMLYALAKNRQLPAAMAKVSRHGVPVAGVAVSILILLVGSCLN
YIIPNPQRVFVYVYSASVLPGMVPWFVILISQLRFRRAHKAAIASHPFRSILFPWANYLTMAFLICVLIG
MYFNEDTRMSLFVGIIFLLAVTLIYKVFGLNRHGKAHKLEE
>gnl|CDD|182695 PRK10747, PRK10747, putative protoheme IX biogenesis protein; Provisional
MLKVLLLFVLLIAGIVVGPMIAGHQGYVLIQTDNYNIETSVTGLAIILILAMVVLFAIEWLLRRIFRTGA
RTRGWFVGRKRRRARKQTEQALLKLAEGDYQQVEKLMTRNADHAEQPVVNYLLAAEAAQQRGDEARANQH
LERAAELADNDQLPVEITRVRIQLARNENHAARHGVDKLLEVAPRHPEVLRLAEQAYIRTGAWSSLLDIL
PSMAKAHVGDEEHRAMLEQQAWIGLMDQAMADQGSEGLKRWWKNQSRKTRHQVALQVAMAEHLIECDDHD
TAQQIILDGLKRQYDERLVLLIPRLKTNNPEQLEKVLRQQIKQHGDTPLLWSTLGQLLMKHGEWQEASLA
FRAALKQRPDAYDYAWLADALDRLHKPEEAAAMRRDGLMLTLQNNPPQ
>gnl|CDD|182696 PRK10748, PRK10748, 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB
MRFYRPLGRISALTFDLDDTLYDNRPVILRTEQEALAFVQNYHPALRSFQNEDLQRLRQALREAEPEIYH
DVTRWRWRAIEQAMLDAGLSAEEASAGADAAMINFAKWRSRIDVPQATHDTLKQLAKKWPLVAITNGNAQ
PELFGLGDYFEFVLRAGPHGRSKPFSDMYHLAAEKLNVPIGEILHVGDDLTTDVAGAIRCGMQACWINPE
NGDLMQTWDSRLLPHIEISRLASLTSLI
>gnl|CDD|182697 PRK10749, PRK10749, lysophospholipase L2; Provisional
MFQQQKDWLTRENAFAAFTMGPLLDFWRQREEAEFTGVDDIPIRFVRFRAPHHDRVVVICPGRIESYVKY
AELAYDLFHLGYDVLIIDHRGQGRSGRLLDDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSM
GGAILTLFLQRHPGVFDAIALCAPMFGIVLPLPSWMARRILNWAEGHPRIRDGYAIGTGRWRPLPFAINV
LTHSRERYRRNLRFYADDPELRVGGPTYHWVRESILAGEQVLAGAGDITTPLLLLQAEEERVVDNRMHDR
FCEARTAAGHPCEGGKPLVIKGAYHEILFEKDAMRSVALNAIVDFFNRHN
>gnl|CDD|182698 PRK10750, PRK10750, Trk system potassium transporter TrkH
MHFRAITRIVGLLVILFSGTMIIPGLVALIYRDGAGRAFTQTFFVALAIGSMLWWPNRKEKGELKSREGF
LIVVLFWTVLGSVGALPFIFSESPNLTITDAFFESFSGLTTTGATTLVGLDSLPHAILFYRQMLQWFGGM
GIIVLAVAILPILGVGGMQLYRAEMPGPLKDNKMRPRIAETAKTLWLIYVLLTVACALALWFAGMDAFDA
IGHSFSTIAIGGFSTHDASIGYFDSPTINTIIAIFLLISGCNYGLHFSLLSGRSLKVYWRDPEFRMFIGV
QLTLVVICTLVLWFHNVYSSALMTLNQAFFQVVSMATTAGFTTDSIARWPLFLPVLLLCSAFIGGCAGST
GGGLKVIRILLLFKQGNRELKRLVHPNAVYSIKLGNRALPERILEAVWGFFSAYALVFIVSMLAIIATGV
DDFSAFASVVATLNNLGPGLGVVADNFTSMNPVAKWILIANMLFGRLEVFTLLVLFTPTFWRE
>gnl|CDD|236750 PRK10751, PRK10751, molybdopterin-guanine dinucleotide biosynthesis protein B; Provisional
MNKTMIPLLAIAAWSGTGKTTLLKKLIPALCARGIRPGLIKHTHHDMDVDKPGKDSYELRKAGAAQTLVA
SQQRWALMTETPDQEELDLHYLASRMDASKLDLILVEGFKHEPIAKIALFRDGAGHRPEELVIDEHVIAV
ASDVPLNLDVPLLDINDVEQIADFIVEWLQKQR
>gnl|CDD|182700 PRK10752, PRK10752, sulfate ABC transporter substrate-binding protein
MNKWGVGLTLLLAATSVMAKDIQLLNVSYDPTRELYEQYNKAFSAHWKQQTGDNVVIRQSHGGSGKQATS
VINGIEADVVTLALAYDVDAIAERGRIDKNWIKRLPDNSAPYTSTIVFLVRKGNPKQIHDWNDLIKPGVS
VITPNPKSSGGARWNYLAAWGYALHHNNNDQAKAQDFVKALYKNVEVLDSGARGSTNTFVERGIGDVLIA
WENEALLAANELGKDKFEIVTPSESILAEPTVSVVDKVVDKKGTREVAEAYLKYLYSPEGQEIAAKNYYR
PRDAEVAKKYENAFPKLKLFTIDEVFGGWTKAQKEHFANGGTFDQISKR
>gnl|CDD|138142 PRK10753, PRK10753, DNA-binding protein HU-alpha
MNKTQLIDVIADKAELSKTQAKAALESTLAAITESLKEGDAVQLVGFGTFKVNHRAERTGRNPQTGKEIK
IAAANVPAFVSGKALKDAVK
>gnl|CDD|182701 PRK10754, PRK10754, NADPH:quinone reductase
MAKRIEFHKHGGPEVLQAVEFTPADPAENEVQVENKAIGINYIDTYIRSGLYPPPSLPSGLGTEAAGVVS
KVGSGVKHIKVGDRVVYAQSALGAYSSVHNVPADKAAILPDAISFEQAAASFLKGLTVYYLLRKTYEIKP
DEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGSAQKAQRAKKAGAWQVINYREENIVERVKEITGGKKV
RVVYDSVGKDTWEASLDCLQRRGLMVSFGNASGPVTGVNLGILNQKGSLYVTRPSLQGYITTREELTEAS
NELFSLIASGVIKVDVAEQQKFPLKDAQRAHEILESRATQGSSLLIP
>gnl|CDD|236751 PRK10755, PRK10755, two-component system sensor histidine kinase PmrB
MISLRRRLLLTIGLILLVFQLISVFWLWHESTEQIQLLVQATLSARNNDEHVMKEIREAVASLLVPSLVM
VSLTLLICFQAVRWITRPLAELQKELEARTADNLTPIAIHSSTLEIEAVTSALNQLVSRLTSTLDQERLF
TADVAHELRTPLAGIRLHLELLEKQHHIDVAPLIARLDQMMHTVEQLLQLARAGQSFSSGHYQTVKLLED
VILPSQDELSEMLEQRQQTLLLPESAADITVQGDATLLRLLLRNLVENAHRYSPEGSTITIKLSQEDGGA
VLAVEDEGPGIDESKCGELSKAFVRMDSRYGGIGLGLSIVSRITQLHHGQFFLQNRQERSGTRAWVWLPK
AQNVAN
>gnl|CDD|236752 PRK10756, PRK10756, protein CreA
MKYKHLILSLSLLLLGPLAHAEEIGSVDTVFKMIGPDHKIVVEAFDDPDVKNVTCYVSRAKTGGIKGGLG
LAEDTSDAAISCQQVGPIELSDKIKNGKAQGEVVFKKRTSLVFKKLQVVRFYDAKRNALAYLAYSDKVVD
GSPKNAISAVPVMPWRQ
>gnl|CDD|236753 PRK10757, PRK10757, inositol-1-monophosphatase
MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESG
ELEGEDQDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRL
RGSTARDLDGTILATGFPFKAKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKP
WDFAAGELLVREAGGIVSDFTGGHNYMLTGNIVAGNPRVVKAMLANMRDELSDALKR
>gnl|CDD|182705 PRK10759, PRK10759, YfiM family lipoprotein
MRALIVPLLLLLSGCSHMANDSWSGQDKAQHFIASAALSAAGNEYAQHQGMSDDRSAAFGLMFSVSLGAG
KELYDSRPAGSGWSWKDLAWDVAGASTGYTLWQLAR
>gnl|CDD|236754 PRK10760, PRK10760, murein hydrolase B; Provisional
MFMRRYVALLPLFVLLAACSSKPKPTETATTTGTPSGGFLLEPQHNVMQMGGDFANNPNAQQFIDKMVNK
HGFDRQQLHEILSQAKRLDWVLRLMDRQAPTTRPPSGPNGAWLRYRKKFITPDNVQNGVVFWNQYEDALN
RAWQVYGVPPEIIVGIIGVETRWGRVMGKTRILDALATLSFNYPRRAEYFSGELETFLLMARDEGDDPLN
LRGSFAGAMGYGQFMPSSFKQYAVDFNGDGHINLWDPVDAIGSVANYFKAHGWVKGDQVAVPANGQAPGL
ENGFKTRYSVSQLAAAGLTPQQPLGNHQQASLLRLDVGTGYQYWYGLPNFYTITRYNHSTHYAMAVWQLG
QAVALARVG
>gnl|CDD|236755 PRK10762, PRK10762, D-ribose transporter ATP binding protein; Provisional
MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTF
NGPKSSQEAGIGIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVG
ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDD
VTVFRDGQFIAEREVADLTEDSLIEMMVGRKLEDQYPRLDKAPGEVRLKVDNLSGPGVNDVSFTLRKGEI
LGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKEN
MSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILD
EPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQEKLMAA
AVGKLNRVNQE
>gnl|CDD|182708 PRK10763, PRK10763, phospholipase A; Provisional
MRTIQGWLLALLLLPLAVYAQEATVKEVHDAPAVRGSIIANMLQEHDNPFTLYPYETNYLLYTYTSDLNK
EAISSYDWAENARKDEVKFQLSLAFPLWRGILGDNSVLGASYTQKSWWQLSNSEESSPFRETNYEPQLFL
GWATDYRFAGWTLRDVEMGYNHQSNGRSDPTSRSWNRLYTRLMAQNGNWLVEVKPWYRIGSTDDNPDITK
YMGYYQLKIGYHLGDAVFSAKGQYNWNTGYGGAELGWSYPITKHVRFYTQVYSGYGESLIDYNFRQTRVG
VGVMLNDLF
>gnl|CDD|236756 PRK10764, PRK10764, potassium-tellurite ethidium and proflavin transporter; Provisional
MQSDKVLPLPAGYFGIVLGLIGLGFAWRYAAQLWPLPAWIGEALVALASIIWALLILAYLYKWIRFPESV
LAELRHPVQSSFVSLIPITTMLVAIGLVPYSRPLAVVLFSFGVVGQLAFAAWRTAGLWRGGHPEEATTPG
LYLPTVANNFVSAMALGALGYHDAGLLFLGAGVFSWLSLEPVILQRLRSSGELPTALRPSLGIQLAPAFV
GCSAYLSVNGGEGDTLAKMLFGYGLLQLLFLLRLMPWILSQGFNASFWSFSFGVAALATTGLHLGHGSDN
GFFHTLAVPLFIFANFIIALLLLRTLALLMQGKLLVRTERAVLM
>gnl|CDD|182710 PRK10765, PRK10765, oxygen-insensitive NADPH nitroreductase
MTPTIELILSHRSIRHFTDEPISEAQREAIINAARAASSSSFLQCSSIIRITDKALREALVELTGGQKYV
AQAAEFWVFCADFNRHLQICPDAQLGLAEQLLIGAVDTAIMAQNALLAAESLGLGGVYIGGLRNNIEAVT
ELLKLPQHVLPLFGLCLGWPAQNPDLKPRLPASLLVHENQYQPLDKDLLAQYDEQLAEYYLTRSSNNRQD
TWSDHIRRTLIKESRPFILDYLHKQGWATR
>gnl|CDD|182711 PRK10766, PRK10766, two-component system response regulator TorR
MSYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRS
RSTVGIILVTGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVKNLLWRISLARQAQPHAQEEDNCYRFA
GYCLNVSRRTLERNGEPIKLTKAEYELLVAFVTNPGQVLSRERLLRMLSHRVENPNDRTIDVLIRRLRHK
LNPDLFVTQHG
>gnl|CDD|236757 PRK10767, PRK10767, chaperone protein DnaJ; Provisional
MAKRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYDQYG
HAAFEQGGGGGGFGGGGGFGDIFGDIFGDIFGGGRGGGRQRARRGADLRYNMEITLEEAVRGVTKEIRIP
TLVTCDTCHGSGAKPGTSPKTCPTCHGAGQVRMQQGFFTVQQTCPTCHGRGKIIKDPCKKCHGQGRVEKE
KTLSVKIPAGVDTGDRIRLSGEGEAGERGGPAGDLYVQIHVKEHPIFERDGNDLYCEVPISFTTAALGGE
IEVPTLDGRVKLKIPEGTQTGKLFRLRGKGVKSVRSGARGDLYCQVVVETPVNLTKRQKELLEEFEESFE
SGEKHSPKSKGFFDKVKDFFD
>gnl|CDD|182713 PRK10768, PRK10768, ribonucleoside hydrolase RihC; Provisional
MRLPIILDTDPGIDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNALKLLHFFNSDVPVAQGAAKPL
VRPLRDAASVHGESGMEGYDFPEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVK
PYIKRIVLMGGSAGRGNVTPNAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPELNRT
GKMLHALFSHYRSGSMQTGLRMHDVCAIAYLLRPELFTLKPCFVDVETQGEFTAGATVVDIDGRLGKPAN
AQVALDIDVDGFQKWFAEVLALAN
>gnl|CDD|182714 PRK10769, folA, type 3 dihydrofolate reductase
MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIVISSQPGTDD
RVTWVKSVDEALAAAGDVPEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEGDTHFPDYEPDEWESVFSEF
HDADEQNSHSYCFEILERR
>gnl|CDD|236758 PRK10770, PRK10770, peptidyl-prolyl cis-trans isomerase SurA; Provisional
FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMG
VKISDEQLDQAIANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVD
SLAKQIGNQNDASTELNLSHILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKG
GQMGWGRIQELPGLFAQALSTAKKGDIVGPIRSGVGFHILKVNDLRGESQNISVTEVHARHILLKPSPIM
TDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALMRLNKGQISAP
VHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQRASAYVKILSNSNA
>gnl|CDD|182716 PRK10771, thiQ, thiamine ABC transporter ATP-binding protein ThiQ
MLKLTDITWLYHHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR
RPVSMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVAL
ARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAW
DGPTDELLSGKASASALLGIKS
>gnl|CDD|182717 PRK10772, PRK10772, cell division protein FtsL; Provisional
MIGGSNERHALPGVIGDDLLRNGKLPLCLFIAVIVSAVTVVTTAHHTRLLTAEREQLVLERDALDIEWRN
LILEENALGDHSRVERIATEKLQMQHVDPSQENIVVQK
>gnl|CDD|182718 PRK10773, murF, UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed
MISVTLSQLADILNGELQGADITIDAVTTDTRKVTPGCLFVALKGERFDAHDFADDAKAAGAGALLVSRP
LDIDLPQLVVKDTRLAFGQLAAWVRQQVPARVVALTGSSGKTSVKEMTAAILRQCGNTLYTAGNLNNDIG
VPLTLLRLTPEHDYAVIELGANHQGEIAYTVSLTRPEAALVNNLAAAHLEGFGSLAGVAKAKGEIFSGLP
ENGIAIMNADSNDWLNWQSVIGSKTVWRFSPNAANSVDFTATNIHVTSHGTEFTLHTPTGSVDVLLPLPG
RHNIANALAAAALAMSVGATLDAVKAGLANLKAVPGRLFPIQLAEGQLLLDDSYNANVGSMTAAAQVLAE
MPGYRVMVVGDMAELGAESEACHRQVGEAAKAAGIDKVLSVGKLSHAISEASGVGEHFADKTALIARLKA
LLAEHQVITILVKGSRSAAMEEVVRALQENGTC
>gnl|CDD|182719 PRK10774, PRK10774, cell division protein FtsW; Provisional
PRLPGFSILVWLSTALKGWVMGSREKDTDSLIMYDRTLLWLTFGLAAIGFVMVTSASMPVGQRLANDPFL
FAKRDAVYLILAFGLALITLRLPMEFWQRYSATMLLGSIIMLLIVLVVGSSVNGASRWIALGPLRIQPAE
LTKLSLFCYLANYLVRKVDEVRNNFWGFLKPMGVMLVLAVLLLAQPDLGTVVVLFVTTLAMLFLAGAKLW
QFIAIIGMGISAVVLLILAEPYRIRRVTSFWNPWEDPFGSGYQLTQSLMAFGRGELWGQGLGNSVQKLEY
LPEAHTDFIFSIIGEELGYIGVVLALLMVFFVAFRAMSIGRKALEIDQRFSGFLACSIGIWFSFQALVNV
GAAAGMLPTKGLTLPLISYGGSSLLIMSTAIMLLLRIDYETRLEKAQAFVRGSR
>gnl|CDD|182720 PRK10775, PRK10775, cell division protein FtsQ; Provisional
MSQAALNTRNREEEEVSSRRSNGTRLAGILFLLMVLGTVLWGGWVVLGWMKDAQRLPLSKLVVTGERHYT
TNDDIRQAILALGAPGTFMTQDVNIIQQQIERLPWIKQVSVRKQWPDELKIHLVEYVPIARWNDQHMVDA
EGNSFSVPADRTGKQVLPMLYGPEGSENEVLQGYREMGQVLAKDKFTLKEAAMTARRSWQLTLNNDIRLE
LGRGDTMKRLARFIELYPVLQQQAQTDGKRISYVDLRYDSGAAVGWAPLPIEESNQQQNQAQAEQQ
>gnl|CDD|182721 PRK10776, PRK10776, 8-oxo-dGTP diphosphatase MutT
MKKLQIAVGIIRNPNNEIFITRRAADAHMAGKWEFPGGKIEAGETPEQALIRELQEEVGITVQHATLFEK
LEYEFPDRHITLWFWLVESWEGEPWGKEGQPGRWVSQVALNADEFPPANEPIIAKLKAL
>gnl|CDD|182722 PRK10778, dksA, RNA polymerase-binding protein DksA
MQEGQNRKTSSLSILAIAGVEPYQEKPGEEYMNEAQLAHFKRILEAWRNQLRDEVDRTVTHMQDEAANFP
DPVDRAAQEEEFSLELRNRDRERKLIKKIEKTLKKVEDEDFGYCESCGVEIGIRRLEARPTADLCIDCKT
LAEIREKQMAG
>gnl|CDD|182723 PRK10779, PRK10779, sigma E protease regulator RseP
LSILWNLAAFIVALGVLITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDRQGTEYVIALIPLGGYVK
MLDERVEPVAPELRHHAFNNKTVGQRAAIIAAGPIANFIFAIFAYWLVFIIGVPGVRPVVGEIAPNSIAA
QAQIAPGTELKAVDGIETPDWDAVRLALVSKIGDESTTITVAPFGSDQRRDKTLDLRHWAFEPDKQDPVS
SLGIRPRGPQIEPVLAEVQPNSAASKAGLQAGDRIVKVDGQPLTQWQTFVTLVRDNPGKPLALEIERQGS
PLSLTLTPDSKPGNGKAEGFAGVVPKVIPLPDEYKTVRQYGPFSAIYEATDKTWQLMKLTVSMLGKLITG
DVKLNNLSGPISIAQGAGMSAEYGLVYYLMFLALISVNLGIINLFPLPVLDGGHLLFLAIEKLKGGPVSE
RVQDFSYRIGSILLVLLMGLALFNDFSRL
>gnl|CDD|182724 PRK10780, PRK10780, molecular chaperone Skp
MKKWLLAAGLGLALATSAGAQAADKIAIVNMGSIFQQVPQRTGVSKQLENEFKGRASELQRMETDLQAKM
QKLQRDGSTMKGSDRTKLEKDVMAQRQTFSQKAQAFEQDRRRRSNEERNKILTRIQTAVKSVANKQGYDL
VVDANAVAYNSSDKDITADVLKQVK
>gnl|CDD|182725 PRK10781, rcsF, Rcs stress response system protein RcsF
MRALPICLLALMLTGCSMLSRSPVEPVQSTAPPPKAEPAKPKAPRAAPVRLYTNAEELVGKPFRDLGEVS
GESCQASNQDSPPSIPTARKRMQINASKMKANAVLLHSCEITSGTPGCYRQAVCIGSALNITA
>gnl|CDD|182726 PRK10782, PRK10782, D-methionine ABC transporter permease MetI
MSEAMMWLLVRGVWETLAMTFVSGFFGFVIGLPVGVLLYVTRPGQIIANAKLYRTLSALVNIFRSIPFII
LLVWMIPFTRVIVGTSIGLQAAIVPLTVGAAPFIARMVENALLEIPTGLIEASRAMGATPMQIVRKVLLP
EALPGLVNAATITLITLVGYSAMGGAVGAGGLGQIGYQYGYIGYNATVMNTVLVLLVILVYLIQFAGDRI
VRAVTHK
>gnl|CDD|182727 PRK10783, mltD, membrane-bound lytic murein transglycosylase D; Provisional
MKAKAILLASVLLVGCQSSKNDATVQQHAQSLSSAGQGEAGKYTSQARWMDDGTSIAPDQDLWAFIGDEL
KMGIPENSRIREQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGAN
AAGIWQIIPSTGRNYGLKQTRWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIK
ANKAKGKPTDFWSLSLPRETKIYVPKMLALSDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEM
AGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLRESLASGEIAAVQSTLVADNTPLNSRSYKVRS
GDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNSDSITYRVRKGDSLSSIAKRH
GVNIKDVMRWNSDTAKNLQPGDKLTLFVKNNSTPDS
>gnl|CDD|236759 PRK10785, PRK10785, maltodextrin glucosidase; Provisional
MMLNAWHLPVAPFVKQSKDQLLITLWLTGEDPPQRVMLRCEPDNEEYLLPMEKQRSQPQVTAWRASLPLN
SGQPRRRYSFKLLWHDRQRWFTPQGFSRRPPARLEQFAVDVPDQGPQWVADQVFYQIFPDRFARSLPREA
VQDHVYYHHAAGQEIILRDWDEPVTAQAGGSTFYGGDLDGISEKLPYLKKLGVTALYLNPIFTAPSVHKY
DTEDYRHVDPQLGGDAALLRLRHATQQRGMRLVLDGVFNHTGDSHPWFDRHNRGTGGACHHPDSPWRDWY
SFSDDGRALDWLGYASLPKLDFQSEEVVNEIYRGEDSIVRHWLKAPYNIDGWRLDVVHMLGEGGGARNNL
QHVAGITQAAKEENPEAYVLGEHFGDARQWLQADVEDAAMNYRGFAFPLRAFLANTDIAYHPQQIDAQTC
AAWMDEYRAGLPHQQQLRQFNQLDSHDTARFKTLLGGDKARMPLALVWLFTWPGVPCIYYGDEVGLDGGN
DPFCRKPFPWDEAKQDGALLALYQRMIALRKKSQALRRGGCQVLYAEGNVVVFARVLQQQRVLVAINRGE
ACEVVLPASPLLNVAQWQRKEGHGDLTDGGGVILTLPA
>gnl|CDD|182729 PRK10786, ribD, bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD
MQDEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYV
TLEPCSHHGRTPPCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLK
RMRTGFPYIQLKLGASLDGRTAMASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSE
LDAQTQALYPQENLRQPVRIVIDSQNRVTPEHRIVQQPGETWLARTQEDSREWPETVRTLLLPEHNGHLD
LVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDELIVYIAPKLLGSDARGLCTLPGLEKLADAPQFKF
SEIRHVGPDVCLHLVPA
>gnl|CDD|182730 PRK10787, PRK10787, DNA-binding ATP-dependent protease La; Provisional
MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFT
VGTVASILQMLKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEG
YIKLNKKIPPEVLTSLNSIDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVE
KRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKM
MSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGP
ILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLF
LLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAPLLDRMEVIRL
SGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLL
LDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSL
GEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRAD
VAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLA
LQNEPSGMQVVTAK
>gnl|CDD|182731 PRK10788, PRK10788, periplasmic folding chaperone; Provisional
MMDNLRTAANSVVLKIILALIILSFILTGVGGYLIGGSNNYAAKVNGQEISRAQLEQAFQSERNRLQQQL
GDQFSELAANEGYMKQLRQQVLNRLIDEALLDQYARELGLGISDEQVKQAIFATPAFQTDGKFDNNKYLA
ILNQMGMTADQYAQALRQQLTTQQLINGVAGTDFMLPGETDELAALVAQQRVVREATIDVNALAAKQTVT
DEEIKSYYDQNKNNFMAPEQFKVSYIKLDAATMQQKITVSDADIQAYYDQHQDQFTQPERKRYSIIQTKT
EAEAKAVLDELKKGADFATLAKEKSTDIISARNGGDLGWLEPATTPDELKNAGLKEKGQLSGVIKSSVGF
LIVRLDDIQPAKVKPLSEVRDDIAAKVKQEKALDAYYALQQKVSDAASNDNESLASAEQAAGVKAVQTGW
FSRDNVPAELNFKPVAQAIFNGGLVGENGAPGSNSDVITVDGDRAFVLRISEHKPEAVKPLAQVRDQVTE
LVKRQKAEQQAKVDAEKLLAALKAGKGEEAMKAAGLSFGEPKTLSRTSQDDPLSQAAFALPLPAKDKPSY
GMAQDMQGNVVLIALDEVTPGSMPEEQKKAMVQGITQNNAQIAFEALMSNLRKEAKIKIGDAA
>gnl|CDD|182732 PRK10789, PRK10789, SmdA family multidrug ABC transporter permease/ATP-binding protein
VALLIIIAMLQLIPPKVVGIIVDGVTEQHMTTGQILMWIGTMVLIAVVVYLLRYVWRVLLFGASYQLAVE
LREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTQISWQLT
LLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTG
KKNMRVARIDARFDPTIYIAIGMANLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIV
ERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPT
GSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQE
IEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI
LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALDDAP
EIREEAVDA
>gnl|CDD|182733 PRK10790, PRK10790, SmdB family multidrug efflux ABC transporter permease/ATP-binding protein
MRSFSQLWPTLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVAGLAAA
YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYV
TVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEV
INGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSALILCGLLMLFGFSASGTIE
VGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRPLQSGRIDIDNVSFAY
RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV
QQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARV
LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQ
LLAAQGRYWQMYQLQLAGEELAASVREEESLS
>gnl|CDD|182734 PRK10791, PRK10791, peptidylprolyl isomerase B
MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKN
EANNGLKNTRGTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVEGMDVVDKIKGVA
TGRSGMHQDVPKEDVIIESVTVSE
>gnl|CDD|236760 PRK10792, PRK10792, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDL
PETTSEAELLALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRP
CTPRGIMTLLERYGIDTYGLNAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAV
GKPGFIPGEWIKPGAIVIDVGINRLEDGKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACE
EYHDP
>gnl|CDD|182736 PRK10793, PRK10793, D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
MKTIFSARIMKRLALTTALCTAFISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRD
PASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSG
NDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYA
IYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGRETE
SKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNTSELHA
PLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWFG
>gnl|CDD|182737 PRK10794, PRK10794, rod shape-determining protein RodA
MTDNPNKKTFWDKIHIDPTMLLIILALLVYSALVIWSASGQDIGMMERKIGQIAMGLVVMVVMAQIPPRV
YEGWAPYLYIICIILLVAVDAFGQISKGAQRWLDLGIVRFQPSEIAKIAVPLMVARFINRDVCPPSLKNT
AIALVLIFMPTLLVAAQPDLGTSILVALSGLFVLFLSGLSWRLIGVAVVLVAAFIPILWFFLMHDYQRQR
VMMLLDPESDPLGAGYHIIQSKIAIGSGGLRGKGWLHGTQSQLEFLPERHTDFIFAVLAEELGLVGVLIL
LALYILLIMRGLWIAARAQTTFGRVMAGGLMLILFVYVFVNIGMVSGILPVVGVPLPLVSYGGSALIVLM
AGFGIVMSIHTHRKMLSKSV
>gnl|CDD|236761 PRK10795, PRK10795, penicillin-binding protein 2; Provisional
MKKLQNSFRDYTAESALFVRRALVAFLGILLLTGVLIANLYNLQIVRFTDYQTRSNENRIKLVPIAPSRG
IIYDRNGTPLALNRTIYQLEMMPEKVDNLQQTLDALRSVVDLTDDDIAAFRKERARSRRFTSIPVKTNLT
EVQVARFAVNQYRFPGVEVKGYQRRYYPYGSALTHVIGYVSKINDKDVERLDKEGKLANYAATHDIGKLG
IERYYEDVLHGKTGYEEVEVNNRGRVIRQLHEQPPQAGHDIYLTLDLKLQQYIETLLAGSRAAVVVTDPR
TGGILALVSTPSYDPNLFVDGISSKDYSGLLNDPNRPLINRATQGVYPPASTVKPYVAVSALSAGVITRN
TSLFDPGWWQLPGSEKRYRDWKKWGHGRLNVTKSLEESADTFFYQVAYDMGIDRLSEWMGKFGYGHYTGI
DLAEERSGNMPTREWKQKRFKKPWYQGDTIPVGIGQGYWTATPIQMSKALMTLINDGIVKVPHLLMSTAE
DGKQVPWVQPHEPPVGDIHSGYWEIAKDGMYGVANRPNGTAHKYFASAPYKIAAKSGTAQVFGLKANETY
NAHKIAERLRDHKLMTAFAPYNNPQVAVAIILENGGAGPAVGTIMRQILDHIMLGDNNTDLPAENPAVAA
AEDH
>gnl|CDD|236762 PRK10796, PRK10796, LPS-assembly lipoprotein RlpB; Provisional
MRYLLTLLLGLAVLVTAGCGFHLRGTTQVPSEMKTLILDSGDPYGPLSRAVRNQLRLNNVELLDDTTRKD
VPSLRLGGSSESKDTASVFQDGQTAEYQMVLTVNAQVLIPGHDIYPISVKVFRSFFDNPLMALAKDAEQD
MIVQEMRDQAAEQLVRKLLSVRAADIRKTEEQASTTTDTPATPARVST
>gnl|CDD|236763 PRK10797, PRK10797, glutamate and aspartate transporter subunit; Provisional
MQLRKLATALLLLGLSAGLAQAEDAAPAAGSTLDKIAKNGVIVVGHRESSVPFSYYDNQQKVVGYSQDYS
NAIVEAVKKKLNKPDLQVKLIPITSQNRIPLLQNGTFDFECGSTTNNLERQKQAAFSDTIFVVGTRLLTK
KGGDIKDFADLKGKAVVVTSGTTSEVLLNKLNEEQKMNMRIISAKDHGDSFRTLESGRAVAFMMDDALLA
GERAKAKKPDNWEIVGKPQSQEAYGCMLRKDDPQFKKLMDDTIAQAQTSGEAEKWFDKWFKNPIPPKNLN
MNFELSDEMKALFKEPNDKALN
>gnl|CDD|182741 PRK10799, PRK10799, type 2 GTP cyclohydrolase I
MKNTELEQLINEKLNSAAISDYAPNGLQVEGRETVQKIVTGVTASQALLDEAVRLQADAVIVHHGYFWKG
ESPVIRGMKRNRLKTLLANDINLYGWHLPLDAHPELGNNAQLAALLGITVMGEIEPLVPWGELTMPVPGL
ELASWIEARLGRKPLWCGDTGPEVVQRVAWCTGGGQSFIDSAARFGVDAFITGEVSEQTIHSAREQGLHF
YAAGHHATERGGIRALSEWLNENTDLDVTFIDIPNPA
>gnl|CDD|182742 PRK10800, PRK10800, acyl-CoA thioesterase YbgC; Provisional
TLFRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALLAERVAFVVRKMTVEYYAPARLD
DMLEVQSEITSMRGTSLTFTQRIVNAEGTLLNEAEVLIVCVDPLKMKPRALPKSIVAEFK
>gnl|CDD|182743 PRK10801, PRK10801, Tol-Pal system protein TolQ
MNILDLFLKASLLVKLIMLILIGFSIASWAIIIQRTRILNAAAREAEAFEDKFWSGIELSRLYQESQGRR
DNLSGSEQIFYSGFKEFVRLHRANSHAPEAVVEGASRAMRISMNRELETLETHIPFLGTVGSISPYIGLF
GTVWGIMHAFIALGAVKQATLQMVAPGIAEALIATAIGLFAAIPAVMAYNRLNQRVNKLELNYDNFMEEF
TAILHRQAFTSSESNKG
>gnl|CDD|182744 PRK10802, PRK10802, peptidoglycan-associated lipoprotein Pal
MQLNKVLKGLMLALPVMAIAACSSNKNASNDQSEGMLGAGTGMDANGGNGNMSSEEQARLQMQQLQQNNI
VYFDLDKYDIRSDFAQMLDAHANFLRSNPSYKVTVEGHADERGTPEYNIALGERRANAVKMYLQGKGVSA
DQISIVSYGKEKPAVLGHDEAAYAKNRRAVLVY
>gnl|CDD|182745 PRK10803, PRK10803, tol-pal system protein YbgF; Provisional
MSSNFRHHLLSLSLLVGVAAPWAAFAQAPISSVGSGSVEDRVTQLERISNAHSQLLTQLQQQLSDNQSDI
DSLRGQIQENQYQLNQVVERQKQIYLQIDSLSSGGAAAQSTSGDQSGAAASATPAADAGTANAGAPVQSG
DANTDYNAAIALVQDKSRQDDAIVAFQNFVKKYPDSTYQPNANYWLGQLNYNKGKKDDAAYYFASVVKNY
PKSPKAADAMFKVGVIMQDKGDTAKAKAVYQQVIKKYPGTDGAKQAQKRLNAM
>gnl|CDD|182746 PRK10805, PRK10805, formate transporter; Provisional
MKADNPFDLLLPAAMAKVAEEAGVYKATKHPLKTFYLAITAGVFISIAFVFYITATTGTGTMPFGMAKLV
GGICFSLGLILCVVCGADLFTSTVLIVVAKASGRITWGQLAKNWLNVYFGNLVGALLFVLLMWLSGEYMT
ANGQWGLNVLQTADHKVHHTFIEAVCLGILANLMVCLAVWMSYSGRSLMDKAFIMVLPVAMFVASGFEHS
IANMFMIPMGIVIRDFASPEFWTAVGSAPEQFSHLTVMNFITDNLIPVTIGNIIGGGLLVGLTYWVIYLR
GNDHH
>gnl|CDD|182747 PRK10807, PRK10807, intermembrane transport protein PqiB
MMESNNGEAKIQKIKRWSPVWIFPIVTALIGAWILFYHFSHQGPEVTLITTNAEGIEAGKTTIKSRSVDV
GVVESVTLSDDLTHVEIKARLNSGMEKLLHKDSVFWVVKPQIGREGISGLGTLLSGAYIELQPGSKGSKP
DKYDLLDSPPLAPPDAKGIRIILDSKKAGQLSPGDPVLFRGYRVGSVETSTFDPQKRLMSYQLFINAPYD
RLVTSNVRFWKDSGIAVDLSSQGMRVEMGSLTTLFSGGVSFDVPEGLELGQPVAEKTEFKLFDDQKSIQD
SLYTDHIDYLMFFKDSVRGLQPGAPVEFRGIRLGTVSKVPFFAPGMRQRFNDDYRIPVLIRIEPERLKMQ
LGENFDVEQHLKELLKRGLRASLKTGNLLTGALYVDLDFYPNAKPWTGPREFNGYPIIPTVSGGLAQIQQ
KLMEALDKINNLPLNPMIEQATSTLSESQRTMRELQTTLDSLNKITSSQSMQQLPADMQKTLRELNRSMQ
GFQPGSPAYNKMVADMQRLDQVLRELQPVLKTLNEKSNALVFEAKDKKDPEPKRAKQ
>gnl|CDD|236764 PRK10808, PRK10808, outer membrane protein A; Reviewed
MKKTAIAIAVALAGFATVAQAAPKDNTWYTGGKLGWSQYHDTGYGFINNNGPTHKNQLGAGAFGGYQANP
YLGFEMGYDWLGRMPYKGDVNNGAFKAQGVQLTAKLGYPITDDLDVYTRLGGMVWRADTKSNVPGARGKD
HDTGVSPVFAGGVEYAITKNWATRLEYQWTNNIGDADTVGARPDNGMLSVGVSYRFGQEEAAPVVAPAPA
PAPVVQTKHFTLKSDVLFNFNKATLKPEGQQALDQLYSQLSNLDPKDGSVVVLGYTDRIGSDAYNQGLSE
KRAQSVVDYLVSKGIPADKISARGMGKSNPVTGNTCDNVKPRAALIDCLAPDRRVEIEVKGIKDVVTQPQ
A
>gnl|CDD|182749 PRK10809, PRK10809, 30S ribosomal protein S5 alanine N-acetyltransferase
MFGYRSNVPKVRLTTDRLVVRLVHERDAWRLADYYAENRHFLKPWEPVRDESHCYPSGWQARLGMINEFH
KQGSAFYFALLDPDEKEIIGVANFSNVVRGSFHACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHR
IMANYMPHNKRSGDLLARLGFEKEGYAKDYLLIDGQWRDHVLTALTTPEWTPGR
>gnl|CDD|236765 PRK10810, PRK10810, anti-sigma-28 factor FlgM
MSIDRTSPLKPVSTVQPRETNDAAVQKRRTAKTTAQSTSTSVKLSDAQAKLMQPGSQDINVERVEALKQA
IRNGELKMDTGKIADALIKEAQSDLQSN
>gnl|CDD|236766 PRK10811, rne, ribonuclease E; Reviewed
MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPL
KEIAREYFPANYSAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGIS
RRIEGDDRTELKEALASLELPEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQE
SNVIVRAFRDYLRQDIGEILIDNPKVLELARQHIAALGRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQ
REVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAFNTNLEAADEIARQLRLRDLGGLIVIDFIDM
TPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESSHHVCPRCSGTGTVRDNESLS
LSILRLIEEEALKENTQEVHAIVPVPIASYLLNEKRSAVNAIETRQGGVRCVIVPNDQMQTPHYSVLRVR
KGEETPTLSYMLPKLHEEAMALPSEEEFAERKRPEQPALATFAMPDVPPAPTPAEPAAPVVAAAPKAAAA
TPPAQPGLLSRFFGALKALFSGGEETKPQEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRDNRTRR
EGRENREENRRNRRQAQQQTAETRESQQAEVTEKARTQDEQQQAPRRERQRRRNDEKRQAQQEAKALNVE
EQSVQETEQEERVQQVQPRRKQRQLNQKVRIEQSVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLP
VVAQTAPEQDEENNAENRDNNGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPEMASGK
VWIRYPVVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVV
VVETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPA
APVVAEVAAEVETVTAVEPEVAPAQVPEATVEHNHATAPMTRAPAPEYVPEAPRHSDWQRPTFAFEGKGA
AGGHSATHHASAPATRPQ
>gnl|CDD|236767 PRK10812, PRK10812, putative DNAse; Provisional
MFLVDSHCHLDGLDYQSLHKDVDDVLAKAAARDVKFCLAVATTLPGYRHMRDLVGERDNVVFSCGVHPLN
QDEPYDVEELRRLAAEEGVVAMGETGLDYYYTPETKVRQQESFRHHIQIGRELNKPVIVHTRDARADTLA
ILREEKVTDCGGVLHCFTEDRETAGKLLDLGFYISFSGIVTFRNAEQLRDAARYVPLDRLLVETDSPYLA
PVPHRGKENQPAMVRDVAEYMAVLKGVSVEELAQVTTDNFARLFHIDASRLQSIR
>gnl|CDD|182753 PRK10814, PRK10814, lipoprotein-releasing ABC transporter permease subunit LolC
MYQPVALFIGLRYMRGRAADRFGRFVSWLSTIGITLGVMALVTVLSVMNGFERELQNNILGLMPQAIITS
EHGSLNPQQLPASALKLDGVNRIAPLTTGDVVLQSARSVAVGVMLGIDPAQKDPLTPYLVNVKQTDLQPG
KYNVILGEQLAGQLGVKRGDQIRLMVPSASQFTPMGRIPSQRLFTVIGTFAANSEVDGYQMLVNQQDASR
LMRYPAGNITGWRLWLDEPLKVDSLSQQKLPEGTVWKDWRERKGELFQAVRMEKNMMGLLLSLIVAVAAF
NIITSLGLLVMEKQGEVAILQTQGLTRRQIMMVFMVQGASAGIIGALLGALLGALLASQLNNLMPIIGVL
LDGAALPVAIEPLQVIVIALVAMAIALLSTLYPSWRAAATQPAEALRYE
>gnl|CDD|182754 PRK10815, PRK10815, two-component system sensor histidine kinase PhoQ
KLLRHFFPLSLRVRFLLATAAVVLALSLAYGMVALVGYSVSFDKTTFRLLRGESNLFYTLAKWENNKLSI
ELPENLDLNSPTLVLIYDENGKLLWRQRDVPWLEKMIQPEWLKKNGFHEIETDVNDSSLLLSGDHSAQQQ
LKEVREDDDDAEMTHSVAVNVYPATSRLPKLTIVVVDTIPQELQRSYMVWSWFSYVLLANLLLVIPLLWL
AAWWSLRPIEALAKQVRELEEGEREQLDPNPPRELTSLVRNLNRLLKNERERYTKYRTTLTDLTHSLKTP
LAVLQSTLRSLRSGKQMSVEQAEPIMLEQISRISQQIGYYLHRASMRSEHNLLSRELHSVAPLLDNLTSA
LNKVYQRKGVNITLDISPEITFVGEKNDFMEVMGNVLDNACKYCLEFVEISARQTDEHLHIVVEDDGPGI
PESKRELIFDRGQRADTLRPGQGLGLSVAREITEQYEGKISAGDSPLGGARMEVIFGRQHSTPKD
>gnl|CDD|182755 PRK10816, PRK10816, two-component system response regulator PhoP
MRVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSND
VSLPILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRRNSGLASQVISLPPFQVDLSRRE
LSINDEVIKLTAFEYTIMETLIRNNGKVVSKDSLMLQLYPDAELRESHTIDVLMGRLRKKIQAQYPQEVI
TTVRGQGYRFDLR
>gnl|CDD|182756 PRK10818, PRK10818, septum site-determining protein MinD
MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATL
NQALIKDKRTENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAI
ITTNPEVSSVRDSDRILGILASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGV
IPEDQSVLRASNQGEPVILDIEADAGKAYADTVDRLLGEERPFRFIEEEKKGFLKRLFGG
>gnl|CDD|236768 PRK10819, PRK10819, transport protein TonB; Provisional
MTLMTLDLPRRFPWPTLLSVGLHGAVVAGLLYTSVHQVIELPAPAQPISVTMVAPADLEPPQAVQPPPEP
VVEPEPEPEPIPEPPKEAPVVIPKPEPKPKPKPKPKPKPVKKVEEQPKREVKPVEPRPASPFENTAPARP
TSSTATAAASKPVTSVSSGPRALSRNQPQYPARAQALRIEGQVKVKFDVDEDGRVDNVRILSAEPRNMFE
REVKQAMRKWRYEAGKPGKGLVVNIVFKINGTTEIE
>gnl|CDD|236769 PRK10820, PRK10820, transcriptional regulator TyrR
MRLEVFCEDRLGLTRELLDLLVLRSIDLRGIEIDPIGRIYLNFAELEFESFSSLMAEIRRIAGVTDVRTV
PFMPSEREHRALSALLEALPEPVLSIDMKGKVELANPASCQLFGQSEEKLRNHTAAQLINGFNFLRWLES
EPQDSHNEHVVINGQDFLMEITPVYLQDENDQHVLVGAVVMLRSTARMGRQLQNLAVNDDSAFSQIVAVS
PKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAP
GAYPNALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNL
VELVQKGEFREDLYYRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWP
GNVRQLKNAIYRALTQLEGYELRPQDILLPDYDAAVAVGEDAMEGSLDEITSRFERSVLTRLYRNYPSTR
KLAKRLGVSHTAIANKLREYGLSQKKGEED
>gnl|CDD|182759 PRK10824, PRK10824, Grx4 family monothiol glutaredoxin
MSTTIEKIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALSACGERFAYVDILQNPDIRAELPKYANWPT
FPQLWVDGELVGGCDIVIEMYQRGELQQLIKETAAKYKSEEPDAE
>gnl|CDD|236770 PRK10826, PRK10826, hexitol phosphatase HxpB
MSTPRQILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDISRREELPDTLGLRIDQVVDLWYARQPWNGP
SRQEVVQRIIARVISLIEETRPLLPGVREALALCKAQGLKIGLASASPLHMLEAVLTMFDLRDYFDALAS
AEKLPYSKPHPEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARMRSIVVPAPEQQNDPRWALADVKLE
SLTELTAADLLG
>gnl|CDD|182761 PRK10828, PRK10828, putative oxidoreductase; Provisional
MDALELLLNRRSASRLAEPAPTGEQLQNILRAGMRAPDHGSLQPWRFFVIEGEGRERFSALLEQGAIAAG
SDEKAIEKARNAPFRAPLIITVVAKCEENHKVPRWEQEVSAGCAVMAMQMAAVAQGFNGIWRSGAWTESP
VVREAFGCREQDKIVGFLYLGTPQLKASTTINPPDPTPFVTYF
>gnl|CDD|236771 PRK10829, PRK10829, ribonuclease D; Provisional
MNYQMITTDDALASVCEAARAFPAIALDTEFVRTRTYYPQLGLIQLYDGEQLSLIDPLGITDWSPFKALL
RDPQVTKFLHAGSEDLEVFLNAFGELPQPLIDTQILAAFCGRPLSCGFASMVEEYTGVTLDKSESRTDWL
ARPLSERQCEYAAADVFYLLPIAAKLMAETEAAGWLPAALDECRLLCQRRQEVLAPEEAYRDITNAWQLR
TRQLACLQLLADWRLRKARERDLAVNFVVREEHLWQVARYMPGSLGELDSLGLSGSEIRFHGKTLLALVA
KAQALPEEALPPPVLNLIDMPGYRKAFKAIKALIQEVSETHGLSAELLASRRQINQLLNWHWKLKPQNGL
PELISGWRGELLAEALTEILQEY
>gnl|CDD|182763 PRK10832, PRK10832, CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
MQFNIPTLLTLFRVILIPFFVLVFYLPFTWAPFVCALIFCVAAVTDWFDGFLARRWNQSTRFGAFLDPVA
DKVMVAIAMVLVTEHYHSWWVTLPAATMIAREIIISALREWMAELGKRSSVAVSWIGKVKTTAQMVALAW
LLWRPNIWVEYAGIALFFVAAVLTLWSMLQYLSAARGDLLDQ
>gnl|CDD|236772 PRK10833, PRK10833, putative assembly protein; Provisional
MRRFLTTLMILLVVLVAGLSALVLLVNPNDFRAYMVKQVEARSGYQLQLDGDLRWHVWPQLSILSGRMSL
TAPGASQPVVSADNMRLDVALWPLLSHQLSVKQVMLKGAVIRLTPDSEAQRSEDAPVAPKGNTLPDVSDD
RGWSFDISSLKVADSLLIWQHEDDEQINVRDINLQMEQDAQRQVSVEFSSRVNRDQRDLTLSLNATVDAS
DYPHQLTANIEQLDYQLQGADLPAQGISGQGSLQAQWQESPKRLSLNQLNLTANDSQLSGSASVTLGEKP
EYQLDLQSDKLNLDNLLGLQPLANDENGAQQGQSQPTLPRPVIASRIDSEPAYQGLRDFTADLTLQADNV
RYRGMNFTQVALQATNQQGLLTITTLSGKLGGGDFSLPGTLDATGASPRITFQPRLKNVELGPLLKAFNL
PISLTGKLSLAGDFSGAGIDAAAFRHQWQGQAHVSMDNARLEGLNIQQLIQQAVERSGGDVKAQENYDNY
TRLDRLTADLTLNRGVLTLNDLQGQSSLLALTGSGQLNLPKQQCDVNFNVRVTGGWNGDSKLIDFLQETP
VPLRVYGNWQQLNYQLQVDQLLRKHLQDEAKKRLNDWAERNKDSRNGKDVKKLLDKL
>gnl|CDD|182765 PRK10834, PRK10834, outer membrane permeability protein SanA
MLKRLIYSLLVLIGLLLLTVLGLDRWMSWKTAPYIYDELQDLPYRQVGVVLGTAKYYRTGVINQYYRYRI
QGAINAYNSGKVNYLLLSGDNALQSYNEPMTMRKDLIAAGVDPSDIVLDYAGFRTLDSIVRTRKVFDTND
FIIITQRFHCERALFIALHMGIQAQCYAVPSPKNMLSVRLREFGARLGALADLYILKREPRFLGPLVPIP
AMHQVPEDAQGYPAVTPEQLLELQKKQGK
>gnl|CDD|182766 PRK10835, PRK10835, hypothetical protein; Provisional
LDFVRGVAILGILLLNISAFGLPKAAYLNPAWYGAISPSDAWTWAILDLVAQVKFLTLFALLFGAGLQLL
LPRGKRWIQSRLTLLVLLGFIHGLLFWDGDILLAYGLVGLICWRLIRDAPSVKSLFNTGVVLYLVGLGVL
LLLGLISRSETSRFWTPDAADILYEKYWKLHGGVEAISNRLDLLSNSLLALGAQYGWQLAGMMLLGAALM
RSGWLKGQFSLRHYRRTALLLVPLGLLINLPAVALQWYLDWDYRWCAFLLQMPRELSAPLQALGYAALIY
GFWPQLSRWRLTLAIACVGRMALTNYLLQTLICTTLFYHFGLFMQFDRLQLLAFVPPVWAANILFSVIWL
RYFRQGPVEWLWRQLTLRAAGPA
>gnl|CDD|182767 PRK10836, PRK10836, lysine transporter; Provisional
MVSETKTTEAPGLRRELKARHLTMIAIGGSIGTGLFVASGATISQAGPGGALLSYMLIGLMVYFLMTSLG
ELAAYMPVSGSFATYGQNYVEEGFGFALGWNYWYNWAVTIAVDLVAAQLVMSWWFPDTPGWIWSALFLGV
IFLLNYISVRGFGEAEYWFSLIKVTTVIVFIIVGVLMIIGIFKGAEPAGWSNWTIGDAPFAGGFAAMIGV
AMIVGFSFQGTELIGIAAGESEDPAKNIPRAVRQVFWRILLFYVFAILIISLIIPYTDPSLLRNDVKDIS
VSPFTLVFQHAGLLSAAAVMNAVILTAVLSAGNSGMYASTRMLYTLACDGKAPRIFAKLSRGGVPRNALY
ATTVIAGLCFLTSMFGNQTVYLWLLNTSGMTGFIAWLGIAISHYRFRRGYVLQGHDLNDLPYRSGFFPLG
PIFAFVLCLIITLGQNYEAFLKDTIDWGGVAATYIGIPLFLIIWFGYKLIKGTHFVRYSEMKFPQNDKK
>gnl|CDD|182768 PRK10837, PRK10837, putative DNA-binding transcriptional regulator; Provisional
MHITLRQLEVFAEVLKSGSTTQASVMLALSQSAVSAALTDLEGQLGVQLFDRVGKRLVVNEHGRLLYPRA
LALLEQAVEIEQLFREDNGALRIYASSTIGNYILPAMIARYRRDYPQLPLELSVGNSQDVINAVLDFRVD
IGLIEGPCHSPELISEPWLEDELVVFAAPDSPLARGPVTLEQLAAAPWILRERGSGTREIVDYLLLSHLP
RFELAMELGNSEAIKHAVRHGLGISCLSRRVIADQLQAGTLVEVAVPLPRLMRTLYRIHHRQKHLSNALQ
RFLSYCQEAN
>gnl|CDD|236773 PRK10838, spr, bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase
VKSQPILRYILRGIPAIAVAVLLSACSANNTAKNMHTETRAVGDSDGSSLQASQDEFENMVRNVDVKSRI
MDQYADWKGVRYRLGGSTKKGIDCSAFVQRTFREQFGLELPRSTYEQQEMGKSVSRSKLRTGDLVLFRAG
STGRHVGIYIGNNQFVHASTSSGVIISSMNEPYWKKRYNEARRVLSRSSS
>gnl|CDD|236774 PRK10839, PRK10839, 16S rRNA pseudouridine(516) synthase RsuA
MRLDKFISQQLGVSRAIAGRELRANRVTVDGEIVKNGAFKLLPEHDVAYDGNPLAQQHGPRYFMLNKPQG
YVCSTDDPDHPTVLYFLDEPVAYKLHAAGRLDIDTTGLVLMTDDGQWSHRITSPRHHCEKTYLVTLESPV
ADDTAEQFAKGVQLHNEKDLTKPAVLEVITPTQVRLTISEGRYHQVKRMFAAVGNHVVELHRERIGAITL
DADLAPGEYRPLTEEEIASVGA
>gnl|CDD|182771 PRK10840, PRK10840, transcriptional regulator RcsB; Provisional
MNNMNVIIADDHPIVLFGIRKSLEQIEWVNVVGEFEDSTALINNLPKLDAHVLITDLSMPGDKYGDGITL
IKYIKRHFPSLSIIVLTMNNNPAILSAVLDLDIEGIVLKQGAPTDLPKALAALQKGKKFTPESVSRLLEK
ISAGGYGDKRLSPKESEVLRLFAEGFLVTEIAKKLNRSIKTISSQKKSAMMKLGVENDIALLNYLSSVTL
SPADKD
>gnl|CDD|182772 PRK10841, PRK10841, two-component system sensor histidine kinase RcsC
MLWLLGALLSVFYIVNALHERESEIRQEFNLSSDQAQRYIRHTSDVMRELKYIAENRLSAENGVLSPRGR
ETKTDVPAFEPLFADSDCSAMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSDNLCMANFGLRNM
PVERDTALKALHERINKYRNAPQQDKGSNLYWISPGARPGVGYFYALTPVYLANRLQALLGIEQTIRLEN
FFTPGTLPMGVTLLDENGHPLLSLTGPESKIKADPRWPQERSWFGYTDGFRELVLKKNLPPSSLSIVYSV
PVDKVLERIRMLILNAILLNVLSAIVLFTLARLFERRIFIPAESNALRLEEHEQFNRKIVASAPVGICIL
RTSDGTNILSNELAHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTNLQISFVHSRYRNENVAICVL
VDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNN
SSSLLLKIISDILDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDP
MRLQQVISNLLSNAIKFTDTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQG
TGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPLYGAQYPQKKGVEGLQGKRCWLAVRNASLEQFLE
TLLQRSGIQVQRYEGQEPTPEDVLITDDPVQKKWQGRAVITFCRRHIGIPLEIAPGEWVHSTATPHELPA
LLARIYRIELESDDSANALPSTDKAVSDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNV
LSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVLK
QTLTVYAERVRKSR
>gnl|CDD|182773 PRK10845, PRK10845, colicin V production protein; Provisional
MVWIDYAIIAVIGFSALVSLIRGFVREALSLVTWGCAFFVASHYYTYLSVWFTGFEDELVRNGIAIAVLF
IATLIVGAIVNYVIGQLVEKTGLSGTDRVLGVCFGALRGVLIVAAILFFLDTFTGFSKSEDWSQSQLIPQ
FSFIIRWFFDYLQSSSSFLPRA
>gnl|CDD|182774 PRK10846, PRK10846, bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
MINKQTPQATSPLASWLSYLENLHSKTIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESI
LMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTASFAEIEAARGDISLTYFEYGTLSALWLFKQAQL
DVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDRESIGREKAGIFRAEKPAVVGEPDMPSTIA
DVAQEKGALLQRRGVDWNYSVTDHDWAFSDGDGTLENLPLPNVPLPNAATALAALRASGLEVSEQAIRDG
IASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRLKALPKNGRVLAVIGMLHDKDIAGTLACLKSVVD
DWYCAPLEGPRGATAEQLAEHLGNGKSFDSVAQAWDAAMADAKPEDTVLVCGSFHTVAHVMEVIDA
>gnl|CDD|182775 PRK10847, PRK10847, DedA family protein
MDLIYFLIDFILHIDVHLAELVAQYGVWVYAILFLILFCETGLVVTPFLPGDSLLFVAGALASLPTNDLN
VHMMVALMLIAAIVGDAVNYTIGRLFGEKLFSNPNSKIFRRSYLDKTHQFYEKHGGKTIILARFVPIVRT
FAPFVAGMGHMSYRHFAAYNVIGALLWVLLFTYAGYFFGTLPFVQDNLKLLIVGIIVVSILPGVIEIWRH
KRAAARAAK
>gnl|CDD|182777 PRK10850, PRK10850, phosphocarrier protein Hpr
MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGKSASAKSLFKLQTLGLTQGTVVTISAEGEDE
QKAVEHLVKLMAELE
>gnl|CDD|182778 PRK10851, PRK10851, sulfate/thiosulfate ABC transporter ATP-binding protein CysA
MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH
ARDRKVGFVFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGG
QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVM
SQGNIEQAGTPDQVWREPATRFVLEFMGEVNRLQGTIRGGQFHVGAHRWPLGYTPAYQGPVDLFLRPWEV
DISRRTSLDSPLPVQVLEVSPKGHYWQLVVQPLGWYNEPLTVVMHGDIDAPQRGERLFVGLQNARLYNGD
ERI
>gnl|CDD|236775 PRK10852, PRK10852, thiosulfate ABC transporter substrate-binding protein CysP
MAVNLLKKNSLALAASLLLAGQAQATELLNSSYDVSRELFAALNPPFEQQWAKDNPGDKLTIKQSHAGSS
KQALAILQGLKADVVTYNQVTDVQILHDKGKLIPADWQSRLPNNSSPFYSTMAFLVRKGNPKNIHDWNDL
VRSDVKLIFPNPKTSGNARYTYLAAWGAADKADGGDKAKTEQFMTQFLKNVEVFDTGGRGATTTFAERGL
GDVLISFESEVNNIRKQYEAQGYEVVVPKTNILAEFPVAWVDKNVQANGTEKAAKAYLNYLYSPQAQTII
TDFYYRVNNPEVMDKLKDKFPQTELFRVEDKFGSWPEVMKTHFTSGGELDKLLAAGRK
>gnl|CDD|182780 PRK10853, PRK10853, putative reductase; Provisional
MVTLYGIKNCDTIKKARRWLEAQGIDYRFHDYRVDGLDSELLQGFIDELGWEALLNTRGTTWRKLDETQR
NAITDAASAAALMLEQPAIIKRPLLCAPGKPMLLGFSESSYQQFFHEV
>gnl|CDD|182781 PRK10854, PRK10854, exopolyphosphatase; Provisional
MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLDSDNMLSEEAMERGLNCLS
LFAERLQGFSPANVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKL
VIDIGGGSTELVIGENFEPILVESRRMGCVSFAQLYFPGGVISKENFQRARLAAAQKLETLAWQYRIQGW
NVALGASGTIKAAHEVLVEMGEKDGLITPERLEMLVKEVLKHKNFAALSLPGLSEERKTVFVPGLAILCG
VFDALAIRELRLSDGALREGVLYEMEGRFRHQDIRSRTAKSLANHYNIDREQARRVLETTMQLYEQWREQ
NPKLAHPQLEALLKWAAMLHEVGLNINHSGLHRHSAYILQNTDLPGFNQEQQLMLATLVRYHRKAIKLDD
LPRFTLFKKKQYLPLIQLLRLGVLLNNQRQATTTPPTLRLITDDSHWTLRFPHDWFSQNALVLLDLEKEQ
EYWEDVTGWRLKIEEESTPEIAA
>gnl|CDD|236776 PRK10856, PRK10856, cytoskeleton protein RodZ
MNTEATQDQNEALTTGERLRQAREQLGLTQQAVAERLCLKVSTVRDIEEDKAPADLASTFLRGYIRSYAR
LVHIPEEELLPGLEKQAPLRAAKVAPMQSFSLGKRRKKRDGWLMTFTWLVLFVVIGLTGAWWWQNHKAQQ
EEITTMADQSSAELSQNSGQSVPLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVV
APSQANVDTAATPAPAAPATPDGAAPLPTDQAGVSTPAADPNALVMNFTADCWLEVTDATGKKLFSGMQR
KGGNLNLTGQAPYKLKIGAPAAVQIQYQGKPVDLSRFIRTNQVARLTLNAE
>gnl|CDD|236777 PRK10857, PRK10857, Fe-S cluster assembly transcriptional regulator IscR
MRLTSKGRYAVTAMLDVALNSEAGPVPLADISERQGISLSYLEQLFSRLRKNGLVSSVRGPGGGYLLGKD
ASSIAVGEVISAVDESVDATRCQGKGGCQGGDKCLTHALWRDLSDRLTGFLNNITLGELVNNQEVLDVSG
RQHTHDAPRTAGRTQDAIDVKLRA
>gnl|CDD|182784 PRK10858, PRK10858, nitrogen regulatory protein P-II
MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIV
DTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI
>gnl|CDD|236778 PRK10859, PRK10859, membrane-bound lytic murein transglycosylase MltF
MKRLKINYLFIGLLALLLAAALWPSIPWFSKEENQLEQIQERGELRVGTINSPLTYYIGNDGPTGFEYEL
AKRFADYLGVKLEIKVRDNISQLFDALDKGKADLAAAGLTYTPERLKQFRFGPPYYSVSQQLVYRKGQPR
PRSLGDLKGGTLTVAAGSSHVETLQELKKKYPELSWEESDDKDSEELLEQVAEGKIDYTIADSVEISLNQ
RYHPELAVAFDLTDEQPVAWALPPSGDDSLYAALLDFFNQIKEDGTLARLEEKYFGHVDRFDYVDTRTFL
RAIDNRLPKYQPLFEKYAGELDWRLLAAIAYQESHWNPQATSPTGVRGLMMLTRNTAQSMGVTDRLDPEQ
SIRGGARYLQDLMERLPESIPEPERIWFALAAYNIGYGHMLDARRLTKKQGGNPDSWADVKKRLPLLSQK
KYYSKTRYGYARGHEAVHYVENIRRYYDSLVGYLQEKEKQAAEEAPQLAQDYPAVSPAELGK
>gnl|CDD|182786 PRK10860, PRK10860, tRNA-specific adenosine deaminase; Provisional
TGVFFLSEVEFSHEYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQ
GGLVLQNYRLLDATLYVTLEPCVMCAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEG
VLADECAALLSDFFRMRRQEIKALKKAQRSTD
>gnl|CDD|182787 PRK10861, PRK10861, signal peptidase I
MANMFALILVIATLVTGILWCVDRFKFAPARRARQAAAQAATGDALDKATLAKVAPKPGWLETGASVFPV
LAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPITQTTLIETGHPKRGDIVVFKYPEDP
KLDYIKRVVGLPGDKVTYDPVSKEVTIQPGCSSGQACENALPVTYSNVEPSDFVQTFSRRNGGEATSGFF
QVPLNETKENGIRLSERKETLGDVTHRILTVPGAQDQVGMYYQQPGQPLATWVVPPGQYFMMGDNRDNSA
DSRYWGFVPEANLVGKATAIWMSFEKQEGEWPTGVRLSRIGGIH
>gnl|CDD|182788 PRK10862, PRK10862, SoxR-reducing system protein RseC
MIKEWATVVSWQNGIALLRCEVKAGCSSCASRAGCGSRLLNKLGPQTTHQLVVPSSQPLVPGQKVELGIA
EGSLLRSALLVYMTPLVGLFLGAALFQLLFGSDLAALCGALLGGVGGFLLARGLSRKLAARAAYQPVILQ
VALPPDLLRVETSS
>gnl|CDD|182789 PRK10863, PRK10863, anti-sigma-E factor RseA
MQKEKLSALMDGETLDSELLNALSHDPEMQKTWESYHLIRDTLRGDVGEVLHFDIASRVAAAIENEPVRQ
VPTLIPESQPAPHQWQKMPFWQKVRPWASQLTQMGVAACVSLAVIVGVQHYNGQSETSQQPETPVFNTLP
MMGKASPVSLGVPSEAAAGNGQQQQVQEQRRRINAMLQDYELQRRLHSEQLQFEQAQTQQAAVQVPGTQS
LGTQSQ
>gnl|CDD|236779 PRK10864, PRK10864, putative methyltransferase; Provisional
MNDELKGKSGKVKVMYVRSDDDSDKRTHNPRTGKGGGRPSGKSRADGGRRPARDDRNSQSRDRKWEDSPW
RTVSRAPGDETPEKADHGGISGKSFIDPEVLRRQRAEETRVYGENACQALFQSRPEAIVRAWFIQSVTPR
FKEALRWMAANRKAYHVVDEAELTKASGTEHHGGVCFLIKKRNGTDVQQWLAQAGAQDCVLALEDVGNPH
NLGGIMRSCAHFGVKGVVVQDAALLESGAAIRTAEGGAEHVQPITGDSFVDVLDDFRQAGYTIVTTSSHK
GTPLFKASLPAKMVLVLGQEYDGLSDAARQQGDLSVSIDGTGNVESLNVSVATGVLLAEWWRQNKA
>gnl|CDD|182791 PRK10865, PRK10865, ATP-dependent chaperone ClpB
MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSR
LPQVEGTGGDVQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAI
EQMRGGESVNDQGAEDQRQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGV
GKTAIVEGLAQRIINGEVPEGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDEL
HTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAIL
RGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQIDSKPEELDRLDRRII
QLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELEQAKIAIEQAR
RVGDLARMSELQYGKIPELEKQLAAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMLESEREKLL
RMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMV
RIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLT
DGQGRTVDFRNTVVIMTSNLGSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQH
IASIAQIQLQRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVP
GKVIRLEVNDDRIVAVQ
>gnl|CDD|182792 PRK10866, PRK10866, outer membrane protein assembly factor BamD
MTRMKYLVAAATLSLFLAGCSGSKEEVPDNPPSEIYATAQQKLQDGNWKQAITQLEALDNRYPFGPYSQQ
VQLDLIYAYYKNADLPLAQAAIDRFIRLNPTHPNIDYVLYMRGLTNMALDDSALQGFFGVDRSDRDPQHA
RAAFRDFSKLVRGYPNSQYTTDATKRLVFLKDRLAKYELSVAEYYTKRGAYVAVVNRVEQMLRDYPDTQA
TRDALPLMENAYRQLQLNAQADKVAKIIAANSA
>gnl|CDD|236781 PRK10869, PRK10869, recombination and repair protein; Provisional
MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSL
KDTPAALRWLEDNQLEDGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPE
HQKTLLDAYANETSLLQEMRAAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQI
DEEYKRLANSGQLLTTSQNALQLLADGEEVNILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEA
SDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPEELPQHHQQLLEEQQQLDDQEDDLETLALAV
EKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFDPEHLSADGADRIEFRVTTNP
GQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQLGESTQVMCVT
HLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTLANAKELLAA
>gnl|CDD|182795 PRK10870, PRK10870, transcriptional repressor MprA; Provisional
MDSSFTPIEQMLKFRASRHEDFPYQEILLTRLCMHMQSKLLENRNKMLKAQGINETLFMALITLESQENH
SIQPSELSCALGSSRTNATRIADELEKRGWIERRESDNDRRCLHLQLTEKGHEFLREVLPPQHNCLHQLW
SALSTTEKDQLEQITRKLLSRLDQMEQDGVVLEAMS
>gnl|CDD|236782 PRK10871, nlpD, murein hydrolase activator NlpD
MSAGSPKFTVRRIAALSLVSLWLAGCSNTSNPPAPVSSVGNGRIVYNRQYGNIPKGSYSGSTYTVKKGDT
LFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQVGNASGTPITGGNAITQADAAEQGVVIKPAQNSTVA
VASQPTITYSESSGEQSANKMLPNNKPAATTVTAPVTAPTASTTEPTASSTSTSTPISTWRWPTDGKVIE
NFSASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEV
KAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR
>gnl|CDD|182797 PRK10872, relA, (p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional
MVAVRSAHLNKAGEFDPDKWIASLGITSQQSCERLAETWAYCLQQTQGHPDASLLLWRGVEMVEILSTLS
MDIDTLRAALLFPLADANVVSEDVLRESVGKSIVNLIHGVRDMDAIRQLKATHNDSVSSEQVDNVRRMLL
AMVEDFRCVVIKLAERIAHLREVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPDE
YKRIAKLLHERRIDREHYIEEFVGHLRAEMKAEGVKAEVYGRPKHIYSIWRKMQKKSLAFDELFDVRAVR
IVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQSIHTVVLGPGGKTVEIQIRTRQMHEDAELG
VAAHWKYKEGAAAGGGRSGHEDRIAWLRKLIAWQEEMADSGEMLDEVRSQVFDDRVYVFTPKGDVVDLPA
GSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIITQKQPNPSRDWLNPNLGYVTTSRGRS
KIHAWFRKQDRDKNILAGRQILDDELEHLGISLKEAEKHLLPRYNFNSLDELLAAIGGGDIRLNQMVNFL
QSQFNKPSAEEQDAAALKQLQQKTYTPQNRSKDNGRVVVEGVGNLMHHIARCCQPIPGDEIVGFITQGRG
ISIHRADCEQLAELRSHAPERIVDAVWGESYSSGYSLVVRVTANDRSGLLRDITTILANEKVNVLGVASR
SDTKQQLATIDMTIEIYNLQVLGRVLGKLNQVPDVIDARRLHG
>gnl|CDD|182798 PRK10873, PRK10873, hypothetical protein; Provisional
MTSRFMLIFAAISGFIYVALGAFGAHVLSKTLGAVEMGWIQTGLEYQAFHTLAILGLAVAMQRRISIWFY
WSSVFLALGTVLFSGSLYCLALSHLRLWAYITPVGGVSFLAGWALMLIGALRLKKKAESHE
>gnl|CDD|182799 PRK10874, PRK10874, cysteine desulfurase CsdA
MNVFNPAQFRAQFPALQDAGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAARE
QVAQLLNAPDAKNIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKL
PLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQA
LDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVI
GLSAALEWLADIDINQAESWSRSLATLAEDALAKLPGFRSFRCQDSSLLAFDFAGVHHSDLVTLLAEYGI
ALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDRALELLVD
>gnl|CDD|236783 PRK10875, recD, exodeoxyribonuclease V subunit alpha
MQKLLLQAVEQKLLRPLDVQFALMVAGDEDPALTLAAALLSADAGEGHVCLPLSRLQPEYLFEGRHPELA
QALWEAAGEPQDWQEALLASPAVSDGDQPTPLVLCGDRLYLQRMWQNERTVARFFNEVNHAIEVDEALLR
QTLDALFGPVTDEVDWQKVAAAVALTRRISVISGGPGTGKTTTVAKLLAALIQLADGERCRIRLAAPTGK
AAARLTESLGKALRQLPLTDEQKKRIPEEASTLHRLLGAQPGSQRLRYHAGNPLHLDVLVVDEASMVDLP
MMARLIDALPPHARVIFLGDRDQLASVEAGAVLGDICRFAEAGYSAERAQQLSRLTGCHLPAGTGTEAAS
VRDSLCLLRKSYRFGSDSGIGQLAAAVNRGDKRAAKAVFQQGFSDIEKRPLQSGEDYQAMLEEALAGYGR
YLDLLAARAEPEAILAAFNRYQLLCALREGPFGVAGLNERIEQALQQKRLIRRPSGPHSRWYEGRPVMIA
RNDSALGLFNGDIGIALDRGQGELRVWFQLPDGNIKSVQPSRLPEHETAWAMTVHKSQGSEFDHTALVLP
NQFTPVVTRELVYTAITRARRRLSLYADERVLSAAIATRTERRSGLAARLSSRAR
>gnl|CDD|236784 PRK10876, recB, exonuclease V subunit beta; Provisional
MMSDVAETLDPLRLPLQGERLIEASAGTGKTFTIAALYLRLLLGLGGSAAFPRPLTVEEILVVTFTEAAT
EELRGRIRSNIHELRIACLREETDNPLYQRLLAEIDDKAQAAQWLLLAERQMDEAAIFTIHGFCQRMLNL
NAFESGMLFEQQLIEDESLLRYQACADFWRRHCYPLPREIARVVFQEWKGPEALLKDISRYLQGEAPVIK
APPPDDETLASRHEQIVARIDAVKQQWREAVGELDALIESSGVDRRSYNSKNLPKWLEKISAWAEEETNS
YQLPKELEKFSQRFLLEKTKKGETPQHPLFEAIDQLLAEPLSLRDLVITRALAEIRETVAQEKRRRGELG
FDDLLSRLDSALQSEGGEALAAAIRTRYPVAMIDEFQDTDPQQYRIFRRIYRHQPETALLLIGDPKQAIY
AFRGADIFTYMKARSEVSAHYTLDTNWRSAPGMVNSVNKLFSQTDDPFLFREIPFIPVKAAGKNQALRFV
VKGETQPAMKFWLMEGEGVGVGDYQQTMAQQCAAQIRDWLQAGQRGEALLMNGDDSRPVRASDITVLVRS
RQEAALIRDALTLLAIPSVYLSNRDSVFETLEAQEMLWLLQAVLAPERERTLRSALATSMMGLDALDIDA
LNNDERAWDALVEEFDGYRQIWRKRGVLPMLRALMSARNIAENLLATAGGERRLTDILHIGELLQEASSQ
LDSEHALVRWLAQQILEPDSQASSQQLRLESDKHLVQIVTIHKSKGLEYPLVWLPFITNFRVQDQAFYHD
RHSFEAVLDLNAAEESVALAEEERLAEDLRLLYVALTRSVWHCSLGVAPLVRRRRKKKGETDLHQSALGY
LLQKGEPGDAAGLRACLEALCDDDIALQTAQETDNQPWQPQDASLAELSARTLQRLLQDNWRVTSYSGLQ
QHGHSIAQDLLPRLDVDAAGEGSVVEEPQLTPHTFPRGASPGTFLHSLFEDLDFTQPVDPEWLQEQLELQ
GFEEQWEPVLTQWITAVLQTPLNETGVSLSQLSARDKQVEMQFYLPIDQPLTASQLDALIRQYDPLSAGC
PPLDFMQVRGMLKGFIDLVFRWQGRYYLLDYKSNWLGEDSSAYTQEAMAQAMQAHRYDLQYQLYTLALHR
YLRHRLADYDYQRHFGGVIYLFLRGVDKEHPGQGIFTTRPNAALIDGLDELFAGETLEEAQ
>gnl|CDD|182802 PRK10877, PRK10877, protein disulfide isomerase II DsbC; Provisional
MKKGFLLFTLLAAAFSGFAHADDAAIQQTLAKLGIQSADIQPSPVAGMKTVLTESGVLYITDDGKHIIQG
PMYDVSGTAPVNVTNQLLLKKLNALEKEMIVYKAPQEKHVITVFTDITCGYCHKLHEQMKDYNALGITVR
YLAFPRQGLDSQAEKDMKSIWCAADRNKAFDDAMKGKDVSPASCDVDIADHYALGVQFGVQGTPAIVLSN
GTLVPGYQGPKEMKAFLDEHQK
>gnl|CDD|182803 PRK10878, PRK10878, FAD assembly factor SdhE
MRELDISIMPFFEHEYDSLSDDEKRIFIRLLECDDPDLFNWLMNHGKPADAELERMVRLIQTRNRERGPV
AI
>gnl|CDD|182804 PRK10879, PRK10879, proline aminopeptidase P II; Provisional
MTQQEFQRRRQALLAKMQPGSAALIFAAPEATRSADSEYPYRQNSDFWYFTGFNEPEAVLVLIKSDDTHN
HSVLFNRVRDLTAEIWFGRRLGQDAAPEKLGVDRALPFSEINQQLYQLLNGLDVVYHAQGEYAYADEIVF
SALEKLRKGSRQNLTAPATLTDWRPWVHEMRLFKSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLE
GEIHHEFNRHGARYPSYNTIVGSGENGCILHYTENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVNGKF
TPAQREIYDIVLESLETSLRLYRPGTSIREVTGEVVRIMVSGLVKLGILKGDVDQLIAENAHRPFFMHGL
SHWLGLDVHDVGVYGQDRSRILEPGMVLTVEPGLYIAPDADVPEQYRGIGIRIEDDIVITETGNENLTAS
VVKKPDEIEALMAAARQQ
>gnl|CDD|182805 PRK10880, PRK10880, adenine DNA glycosylase
MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPL
DEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGN
VKRVLARCYAVSGWPGKKEVENRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIA
YANHSWALYPGKKPKQTLPERTGYFLLLQHGDEVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIA
ADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNGLWYNLAQPPSVGLAAPVERLLQQLRTGAPV
>gnl|CDD|236785 PRK10881, PRK10881, Ni/Fe-hydrogenase cytochrome b subunit
MSMSHDPQPLGGKLISKPVMILGPLIVICMLLIVKRFVFGLGSVSNLNGGYPWGIWIAFDVLIGTGFACG
GWALAWLVYVFNRGQYHPLVRPALLASLFGYSLGGLSITIDVGRYWNLPYFFIPGHFNVNSVLFETAVCM
TIYIGVMALEFAPALLERLGWKVSLKRLNKVMFFIIALGALLPTMHQSSLGSLMIIAGYKVHPLWQSYEM
LPLLSLLTAFIMGFSIVIFEGSLVQAGLRGNGPDEKSLFAKLTKTISVLLAIFLVLRFGELIYRGKLSYA
FAGDFYSVMFWIEVALMLFPLVVLRVAKLRRDSRMLFLSALSALLGGALWRLNYSLIAFNPGGGYHYFPS
WEELLISIGFVAIEICAYIVLIRLFPVLPPLKQNDHNRHEASKA
>gnl|CDD|236786 PRK10882, PRK10882, hydrogenase 2 operon protein HybA
MNRRNFLKAASAGALLAGALPSVSHAAAENRPPIPGALGMLYDSTLCVGCQACVTKCQEINFPERNPQGE
QTWDNPDKLSPYTNNIIKVWKSGTGVNKDQEENGYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHY
DKDVCTGCRYCMVACPFNVPKYDYNNPFGAIHKCELCNQKGVERLDKGGLPGCVEVCPTGAVIFGTREEL
LAEAKRRLALKPGSEYHYPRQTLKSGDTYLHTVPKYYPHVYGEKEGGGTQVLVLSGVPFENLGLPKLDDL
STGARSEHIQHTLYKGMILPLAVLAGLTVLVRRNTKNDHHDGGDDHES
>gnl|CDD|182808 PRK10883, PRK10883, FtsI repressor; Provisional
MSLSRRQFIQASGIALCAGALPLRARAAGQQQPLPVPPLLESRRGQPLFLTLQRAHWSFTGGTKASVWGI
NGRYLGPTIRVWKGDDVKLIYSNRLTEPVSMTVSGLQVPGPLMGGPARMMSPNADWAPVLPIRQNAATCW
YHANTPNRMAQHVYNGLAGMWLVEDEVSKSLPIPNHYGVDDFPVIIQDKRLDNFGTPEYNEPGSGGFVGD
TLLVNGVQSPYVEVSRGWVRLRLLNASNARRYQLQMSDGRPLHVIAGDQGFLPAPVSVKQLSLAPGERRE
ILVDMSNGDEVSITAGEAAGIVDRLRGFFEPSSILVSTLVLTLRPTGLLPLVTDNLPMRLLPDEIMEGSP
IRSREISLGDDLPGINGALWDMNRIDVTAQQGTWERWTVRADMPQAFHIEGVMFLIRNVNGAMPFPEDRG
WKDTVWVDGQVELLVYFGQPSWAHFPFLFYSQTLEMADRGSIGQLLVNPAP
>gnl|CDD|182809 PRK10884, PRK10884, SH3 domain-containing protein; Provisional
MPKLRLIGLTLLALSATAVSHAEEKRYVSDELNTYVRSGPGDQYRIVGTLNAGEEVTLLQVNANTNYAQI
RDSKGRTAWIPLKQLSTTPSLRTRVPDLENQVKTLTDKLNNIDNTWNQRTAEMQQKVAQSDSVINGLKEE
NQKLKNQLIVAQKKVDAANLQLDDKQRTIIMQWFMYGGGVAGIGLLLGLLLPHLIPRRKRKDRWMN
>gnl|CDD|182810 PRK10885, cca, multifunctional CCA addition/repair protein
MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRG
YTGFTCYAAPDVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVAR
FAARFAHLGFRIAPETLALMREMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEI
DALFGVPQPAKWHPEIDTGIHTLMVLDQAAKLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKL
VEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLVKLLDRIDAWRKPQRFEQFLLACEADARGRL
GFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAVAAWKEQRCP
>gnl|CDD|182811 PRK10886, PRK10886, DnaA initiator-associating protein DiaA; Provisional
MLERIKVCFTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETE
RPSLPAIALNTDNVVLTAIANDRLHDEVYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIV
ALTGYDGGELAGLLGPQDVEIRIPSHRSARIQEMHMLTVNCLCDLIDNTLFPHQDD
>gnl|CDD|236787 PRK10887, glmM, phosphoglucosamine mutase; Provisional
RKYFGTDGIRGKVGQAPITPDFVLKLGWAAGKVLARQGRPKVLIGKDTRISGYMLESALEAGLAAAGVDV
LLTGPMPTPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDKPLTCVESA
ELGKASRINDAAGRYIEFCKSTFPNELSLRGLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGLNI
NDECGATDPEALQAAVLAEKADLGIAFDGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRRGQLRGGVVGT
LMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGWRLGGENSGHILCLDKTTTGDGIVAALQVLAAMV
RSGMSLADLCSGMKLFPQVLINVRFKPGADDPLESEAVKAALAEVEAELGGRGRVLLRKSGTEPLIRVMV
EGEDEAQVTALAERIADAVKAAA
>gnl|CDD|182813 PRK10888, PRK10888, octaprenyl diphosphate synthase; Provisional
MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIA
ALIEFIHTATLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVN
VIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLI
DDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHHGTPEQAAMIRTAIEQGNGRHLLEPVLEAMNACGS
LEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQRDR
>gnl|CDD|182814 PRK10892, PRK10892, arabinose-5-phosphate isomerase KdsD
HVELQPGFDFQQAGKEVLAIEREGLAELDQYINQDFTLACEKMFWCKGKVVVMGMGKSGHIGRKMAATFA
STGTPSFFVHPGEAAHGDLGMVTPQDVVIAISNSGESSEILALIPVLKRLHVPLICITGRPESSMARAAD
IHLCVKVPKEACPLGLAPTSSTTATLVMGDALAVALLKARGFTAEDFALSHPGGALGRKLLLRVSDIMHT
GDEIPHVSKTASLRDALLEITRKNLGMTVICDDNMKIEGIFTDGDLRRVFDMGIDLRQASIADVMTPGGI
RVRPGILAVDALNLMQSRHITSVLVADGDHLLGVLHMHDLLRAGVV
>gnl|CDD|236788 PRK10893, PRK10893, LPS export ABC transporter periplasmic protein LptC
MSKTRRWVIILLALIALVLIGWNLADKDEDTAPVVVNNNDPTYQSQHTDTVVYNPEGALSYKLVAQHVEY
YSDQAVSWFTQPVLTTFDKNKVPTWSVRADKAKLTNDRMLYLYGHVEVNSLTPDSQLRRITTDNAQINLV
TQDVTSDDLVTLYGTTFNSSGLKMRGNLRSKTAELIEKVKTSYEIQNKQTQP
>gnl|CDD|182816 PRK10894, PRK10894, lipopolysaccharide ABC transporter substrate-binding protein LptA
TNKLSLNLLLASSLLAASIPAFALTGDTDQPIHIDSDQQSLDMQGNVVTFTGNVVVTQGTIKINADKVVV
TRPGGEQGKEVIDGYGNPATFYQMQDNGKPVKGHASKMHYELAKDFVVLTGNAYLEQLDSNIKGDKITYL
VKEQKMQAFSDKGKRVTTVLVPSQLQDKNKGQTPAQKKSN
>gnl|CDD|182817 PRK10895, PRK10895, lipopolysaccharide ABC transporter ATP-binding protein; Provisional
MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL
PLHARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSG
GERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIV
SQGHLIAHGTPTEILQDEHVKRVYLGEDFRL
>gnl|CDD|182818 PRK10896, PRK10896, PTS IIA-like nitrogen regulatory protein PtsN
MNNDTTLQLSSVLNRECTRSRVHCQSKKRALEIISELAAKQLSLPPQVVFEAILTREKMGSTGIGNGIAI
PHGKLEEDTLRAVGVFVQLEQPIAFDAIDNQPVDLLFALLVPADQCKTHLHTLSLVAKRLADKTICRRLR
AAQSDEELYQIITE
>gnl|CDD|182819 PRK10897, PRK10897, PTS phosphocarrier protein NPr
MTVKQTVEIKNKLGMHARPAMKLFELVQGFDAEVLLRNDEGTEAEANSVIALLMLDSAKGRQIEVEATGP
QEEEALAAVIALFNSGFDED
>gnl|CDD|182820 PRK10898, PRK10898, serine endoprotease DegS
MFVKLLRSVAIGLIVAAILLVAMPSLRSLNPLSTPQFDSTDETPASYNQAVRRAAPAVVNVYNRSLNSTS
HNQLEIRTLGSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATNLPVI
PINPKRVPHIGDVVLAIGNPYNLGQTITQGIISATGRIGLSPTGRQNFLQTDASINHGNSGGALVNSLGE
LMGINTLSFDKSNDGETPEGIGFAIPTQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQG
IVVNEVSPDGPAAKAGIQVNDLIISVNNKPAISALETMDQVAEIRPGSVIPVVVMRDDKQLTLQVTIQEY
PAT
>gnl|CDD|236789 PRK10899, PRK10899, AsmA2 domain-containing protein
LAAWMTIKKGDIAGGDVWLKQGGASWLGEDQTHTLSVDNLTAHISRQGNGWQFDIPDTRLTTDGQPWPSG
ALSLLWLPEQDQVGGPDNKDELRIRASNLELERLEPLLPLASKLTPALGERWQALQPSGKINTLALDIPL
QAPEKTRFQASWQDLSWKQWKLLPGAEHFSGTLSGSVENGRLTFALKQSTLPYEDMFRAPLEIAQGSGTL
SWLNNDKGFQLWGRDLDVQAKSLWARGDFRYLQPANDEPWLGILAGIRLDDAGDAWRYFPEPLMGKDLVD
YLSGAIQGGQVDNATLVYGGNPHLFPYKHNEGQFQVLVPLRNATFAFQPDWPALTNLDIDLNFLNDGLWM
KAPQVKLGGVRASNLSAVIPDYSKEKLLIDADIKGPGKAVGDYFDETPLKDSLGATLDELQLGGDVNGRL
HLDIPLDGELVTASGEVTLRNNSLFIKPLDSTLKNLSGKFRFDNGNLQSDPLSANWFGQPLNVDFSTKEG
AKAYQVAVNLNGDWQPAKLPGLPPAVNEALSGSVPWQGKVGIDLPYHGGATYQVDLNGDLKNVSSHLPSP
LDKPAGEALPLNVKADGNLNSFTLSGSAGADNHFNSRWLLGQKLTLDRAIWQTDSKTLPPLPDQSGLELN
LPPLDGEEWLALLSQKGAAESVSSAARFPQRITLRTPELSLGGQQWNNLSLVSQPQANGTKVEAQGREIN
GTLLMRNNAPWLANIKYLYYNPQWAKTRSSSTPTSPLATAERISFRGWPALQLRCAECWLWGQKLGRIDG
DLTPEGDTLTLTNGLIDTGFARLTASGEWVNNPGGERTSLKGKLSGQKIDEAASFFGVTTPIRNSSFNVD
YDLHWRGAPWQPDEATLNGILKTRLGKGEITDLGTGHAGQLLRLLSFDALLRKLRFDFSDTFSEGFYFDS
IRSTAWIKDGVMHTDDLLVDGLEADIAMKGSVDLVRRQINMEAVVAPEISATVGVATAFAVNPIVGAAVF
AASKVLGPLWSKISIIRYHISGPLDQPQINEVLRQPRKEKAQ
>gnl|CDD|236790 PRK10901, PRK10901, 16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB
SMNLRALAAAAILQVVDQGQSLSAALPALQQKVSDKDRALLQELCYGVLRRLPRLEWLIAQLLAKPLKGK
QRIVHALLLVGLYQLLYTRIPAHAAVDETVEAAKALKRPWAKGLVNAVLRRFQREQEELLAELQADPVAR
YNHPSWLIKRLKKAYPEQWQAILAANNQRPPMWLRVNRRHHSRDAYLALLAEAGIEAFPHAVGPDAIRLE
TPVPVHQLPGFAEGWVSVQDAAAQLAATLLAPQNGERVLDACAAPGGKTAHILELAPQAQVVALDIDAQR
LERVRENLQRLGLKATVIVGDARDPAQWWDGQPFDRILLDAPCSATGVIRRHPDIKWLRRPEDIAALAAL
QSEILDALWPLLKPGGTLLYATCSILPEENEQQIKAFLARHPDAELLDTGTPQQPGRQLLPGEEDGDGFF
YALLIKR
>gnl|CDD|236791 PRK10902, PRK10902, FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
MKSLFKVTLLATTMAVALNAPITFAADAAKPAATADSKAAFKNDDQQSAYALGASLGRYMENSLKEQEKL
GIKLDKDQLIAGVQDAFADKSKLSDQEIEQTLQAFEARVKSAAQAKMEKDAADNEAKGKKYREKFAKEKG
VKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIK
KGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLDVKPAPKADAKPEADAKAADSAK
>gnl|CDD|182824 PRK10903, PRK10903, peptidylprolyl isomerase A
MFKSTLAAMAAVFALSALSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTF
HRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHG
QRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSAKVLP
>gnl|CDD|182825 PRK10904, PRK10904, adenine-specific DNA-methyltransferase
MKKNRAFLKWAGGKYPLLDDIKRHLPKGECLIEPFVGAGSVFLNTDFSRYILADINSDLISLYNIVKLRT
DEYVQAARELFTPETNCAEVYYQLREEFNKSQDPFRRAVLFLYLNRHGYNGLCRYNLRGEFNVPFGRYKK
PYFPEAELYHFAEKAQNAFFYCESYADSMARADKGSVVYCDPPYAPLSATANFTAYHTNSFSLEQQAHLA
EIAEGLVERHIPVLISNHDTMLTREWYQRAKLHVVKVRRSISSNGGTRKKVDELLALYKPG
>gnl|CDD|236792 PRK10905, PRK10905, cell division protein DamX; Validated
MMGVGILVLLLLIIGIGSALKAPSTSSSDQTASGEKSIDLAGNATDQANGVQPAPGTTSAEQTAGNTQQD
VSLPPISSTPTQGQTPVATDGQQRVEVQGDLNNALTQPQNQQQLNNVAVNSTLPTEPATVAPVRNGNASR
QTAKTQTAERPATTRPARKQAVIEPKKPQATAKTEPKPVAQTPKRTEPAAPVASTKAPAATSTPAPKETA
TTAPVQTASPAQTTATPAAGGKTAGNVGSLKSAPSSHYTLQLSSSSNYDNLNGWAKKENLKNYVVYETTR
NGQPWYVLVSGVYASKEEAKRAVSTLPADVQAKNPWAKPLHQVQADLK
>gnl|CDD|182827 PRK10906, PRK10906, DeoR/GlpR family transcriptional regulator
MKQTQRHDAIIELVKQQGYVSTEELVEHFSVSPQTIRRDLNDLAEQNKILRHHGGAALPSSSVNTPWHDR
KATQTEEKERIARKVASQIPNGATLFIDIGTTPEAVAHALLNHSNLRIVTNNLNVANTLMAKEDFRIILA
GGELRSRDGGIIGEATLDFISQFRLDFGILGISGIDSDGSLLEFDYHEVRTKRAIIENSRHVMLVVDHSK
FGRNAMVNMGSISMVDAVYTDQLPPASVMQVIEDHHVQLELC
>gnl|CDD|182828 PRK10907, PRK10907, intramembrane serine protease GlpG; Provisional
MLMITSFSNPRLAQAFVDYMATQGVILTIQQHNQSDIWLADESQAERVRAELARFLENPADPRYLAASWQ
SGHTNSGLRYRRFPFLATLRERAGPLTLGVMIACVVVFILMQILGDQTVMLWLAWPFDPSLKFELWRYFT
HALLHFSLLHILFNLLWWWYLGGAVEKRLGSGKLIVITLISALLSGWVQSKFSGPWFGGLSGVVYALMGY
VWLRGERDPQSGIYLPRGLIAFALLWLVAGYFDLFGMSIANAAHVAGLAVGLAMAFWDTRNARKRK
>gnl|CDD|182829 PRK10908, PRK10908, cell division ATP-binding protein FtsE
MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLK
NREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSG
GEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTL
SDGHLHGGVGGE
>gnl|CDD|236793 PRK10909, rsmD, 16S rRNA m(2)G966-methyltransferase; Provisional
MMKKPNHSGSGQIRIIGGQWRGRKLPVPDSPGLRPTTDRVRETLFNWLAPVIVDARCLDCFAGSGALGLE
ALSRYAAGATLLEMDRAVAQQLIKNLATLKAGNARVVNTNALSFLAQPGTPHNVVFVDPPFRKGLLEETI
NLLEDNGWLADEALIYVESEVENGLPTVPANWQLHREKVAGQVAYRLYIREAQGESDAD
>gnl|CDD|182831 PRK10910, PRK10910, DUF1145 family protein
MLINLGRLLMLCVWGFLILNLVHPFPRPLNIFVNVALIFMVLMHGLQLALLKSTQPKDGPQLSGLEQVRI
FLFGVFELLAWQKKQKVKK
>gnl|CDD|182832 PRK10911, PRK10911, oligopeptidase A; Provisional
MTNPLLTPFSLPPFSAIKPEHVVPAVTKALNDCREAVERVVAQGAPYTWENLCQPLAEVDDVLGRIFSPV
SHLNSVKNSPELREAYEQTLPLLSEYSTWVGQHEGLYQAYRDLRDGDHYATLNTAQKKAVDNALRDFELS
GIGLPKEKQQRYGEIAARLSELGNQYSNNVLDATMGWTKLITDEAELAGMPESALAAAKAQAEAKEQEGY
LLTLDIPSYLPVMTYCDNQALREEMYRAYSTRASDQGPNAGKWDNSEVMEEILALRHELAQLLGFENYAD
KSLATKMAENPQQVLDFLTDLAKRARPQGEKELAQLRAFAKAEFGVDELQPWDIAYYSEKQKQHLYSISD
EQLRPYFPENKAVNGLFEVVKRIYGITAKERKDVDVWHPDVRFFELYDENNELRGSFYLDLYARENKRGG
AWMDDCVGQMRKADGSLQKPVAYLTCNFNRPVNGKPALFTHDEVITLFHEFGHGLHHMLTRIETAGVSGI
SGVPWDAVELPSQFMENWCWEPEALAFISGHYETGEPLPKELLDKMLAAKNYQAALFILRQLEFGLFDFR
LHAEFDPDQGAKILETLAEIKKQVAVVPSPSWGRFPHAFSHIFAGGYAAGYYSYLWADVLAADAFSRFEE
EGIFNRETGQSFLDNILSRGGSEEPMELFKRFRGREPQLDAMLEHYGIKG
>gnl|CDD|182833 PRK10913, PRK10913, dipeptide ABC transporter permease DppC
MSQVTENKVISAPVPMTPLQEFWHYFKRNKGAVVGLVYVVIMLFIAIFANWIAPHNPAEQFRDALLAPPV
WQEGGSWAHILGTDDVGRDVLSRLMYGARLSLLVGCLVVVLSLVMGVILGLIAGYFGGLVDNIIMRVVDI
MLALPSLLLALVLVAIFGPSIVNAALALTFVALPHYVRLTRAAVLVEVNRDYVTASRVAGAGAMRQMFIN
ILPNCLAPLIVQASLGFSNAILDMAALGFLGMGAQPPTPEWGTMLSDVLQFAQSAWWVVTFPGLAILLTV
LAFNLMGDGLRDALDPKLKQ
>gnl|CDD|182834 PRK10914, PRK10914, dipeptide ABC transporter permease DppB
MLQFILRRLGLVIPTFIGITLLTFAFVHMIPGDPVMIMAGERGISPERHAQLLAELGLDKPMWQQYLHYI
WGVMHGDLGISLKSRIPVWDEFVPRFKATLELGVCAMIFAVAVGIPVGVLAAVKRGSIFDHTAVGLALTG
YSMPIFWWGMMLIMLVSVHWNLTPVSGRVSDMVFLDDSNPLTGFMLIDTAIWGEDGNFIDAVAHMILPAI
VLGTIPLAVIVRMTRSSMLEVLGEDYIRTARAKGLTRMRVIIVHALRNAMLPVVTVIGLQVGTLLAGAIL
TETIFSWPGLGRWLIDALQRRDYPVVQGGVLLVATMIILVNLLVDLLYGVVNPRIRHKK
>gnl|CDD|182835 PRK10916, PRK10916, ADP-heptose--LPS heptosyltransferase RfaF
MKILVIGPSWVGDMMMSQSLYRTLKARYPQAIIDVMAPAWCRPLLSRMPEVNEAIPMPLGHGALEIGERR
RLGHSLREKRYDRAYVLPNSFKSALVPFFAGIPHRTGWRGEMRYGLLNDLRVLDKEAFPLMVERYVALAY
DKGVMRTAADLPQPLLWPQLQVSEGEKSETCAAFSLSSERPIIGFCPGAEFGPAKRWPHYHYAELAQQLI
DEGYQVVLFGSAKDHEAGNEILAALNTEQQAWCRNLAGETQLEQAVILIAACKAIVTNDSGLMHVAAALN
RPLVALYGPSSPDFTPPLSHKARVIRLITGYHKVRKGDAAEGYHQSLIDITPQRVLEELNALLLQEEA
>gnl|CDD|236794 PRK10917, PRK10917, ATP-dependent DNA helicase RecG; Provisional
PSLLLLLDAPLTSLKGVGPKTAEKLAKLGIHTVQDLLLHLPRRYEDRTRLKPIAELRPGEKVTVEGEVLS
AEVVFGKRRRLTVTVSDGTGNLTLRFFNFNQPYLKKQLKVGKRVAVYGKVKRGKYGLEMVHPEYEVLEEE
SPELEGRLTPVYPLTEGLKQKTLRKLIKQALELLDALPELLPEELLEKYGLLSLAEALRAIHFPPSDEDL
HPARRRLKFEELFALQLSLLLLRAGRRSKKAGPLPYDGELLKKFLASLPFELTGAQKRVVAEILADLASP
KPMNRLLQGDVGSGKTVVAALAALAAIEAGYQAALMAPTEILAEQHYENLKKLLEPLGIRVALLTGSLKG
KERREILEAIASGEADIVIGTHALIQDDVEFHNLGLVIIDEQHRFGVEQRLALREKGENPHVLVMTATPI
PRTLAMTAYGDLDVSVIDELPPGRKPITTVVIPDSRRDEVYERIREEIAKGRQAYVVCPLIEESEKLDLQ
SAEETYEELQEAFPELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVMVIENAER
FGLAQLHQLRGRVGRGAAQSYCVLLYKDPLSETARERLKIMRETNDGFVIAEKDLELRGPGELLGTRQSG
LPEFKVADLVRDEELLEEARKDARELLERDPELAEALLERWLGERERYDKA
>gnl|CDD|182837 PRK10918, PRK10918, phosphate ABC transporter substrate-binding protein PstS
MKVMRTTVATVVAATLSMSAFSAFAAASLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQI
IANTVDFGASDAPLSDEKLAQEGLFQFPTVIGGVVLAVNIPGLKSGELVLDGKTLGDIYLGKIKKWNDEA
IAKLNPGVKLPSQNIAVVRRADGSGTSFVFTSYLAKVNEEWKSKVGAGSTVNWPTGLGGKGNDGIAAFVQ
RLPGAIGYVEYAYAKQNNLAYTKLISADGKPVSPTEESFSNAAKGADWSKSFAQDLTNQKGDDAWPITST
TFILVHKDQKKPEQGAEVLKFFDWAYKNGAKQANDLDYASLPDSVVEQVRAAWKTNIKDSSGKPLY
>gnl|CDD|182838 PRK10919, PRK10919, ATP-dependent DNA helicase Rep; Provisional
MRLNPGQQQAVEFVTGPCLVLAGAGSGKTRVITNKIAHLIRGCGYQARHIAAVTFTNKAAREMKERVAQT
LGRKEARGLMISTFHTLGLDIIKREYAALGMKSNFSLFDDTDQLALLKELTEGLIEDDKVLLQQLISTIS
NWKNDLKTPAQAAAGAKGERDRIFAHCYGLYDAHLKACNVLDFDDLILLPTLLLQRNEEVRERWQNKIRY
LLVDEYQDTNTSQYELVKLLVGSRARFTVVGDDDQSIYSWRGARPQNLVLLSQDFPALQVIKLEQNYRSS
GRILKAANILIANNPHVFEKRLFSELGYGDELKVLSANNEEHEAERVTGELIAHHFVNKTQYKDYAILYR
GNHQSRVFEKFLMQNRIPYKISGGTSFFSRPEIKDLLAYLRVLTNPDDDSAFLRIVNTPKREIGPATLQK
LGEWAMTRNKSLFTASFDMGLSQTLSGRGYESLTRFTHWLAEIQRLAEREPVAAVRDLIHGIDYESWLYE
TSPSPKAAEMRMKNVNQLFSWMTEMLEGSELDEPMTLTQVVTRFTLRDMMERGESEEELDQVQLMTLHAS
KGLEFPYVYLVGMEEGLLPHQSSIDEDNIDEERRLAYVGITRAQKELTFTLCKERRQYGELVRPEPSRFL
LELPQDDLIWEQERKVVSAEERMQKGQSHLANLKAMLAAKRG
>gnl|CDD|236795 PRK10920, PRK10920, putative uroporphyrinogen III C-methyltransferase; Provisional
MTEQEKSSAVVEETREAVETTSQPVATEKKSKNRTGLVLSAVAIAIALAAGAGLYYHGKQQAQNQTATND
ALANQLTALQKAQESQKQELEGILKQQAKALDQANRQQAALAKQLDELQQKVATISGSDAKTWLLAQADF
LVKLAGRKLWSDQDVTTAAALLKSADASLADMNDPSLITVRRAITDDIATLSAVSQVDYDGIILKLNQLS
NQVDNLRLADNDSDGSPMDSDSEELSSSLSEWRQNLSKSWHNFMDNFITIRRRDDTAEPLLAPNQDVYLR
ENIRSRLLVAAQAVPRHQEETYKQSLENVSTWVRAYFDTDDATTKAFLDEVDQLSQQNISMDLPETLQSQ
PILEKLMQTRVRNLLAQPAAGATEAKAPQADAPAAAPQGE
>gnl|CDD|182840 PRK10921, PRK10921, Sec-independent protein translocase subunit TatC
MAVEDTQPLISHLIELRKRLLNCIIAVLVIFLALVYFANDIYHLVSAPLIKQLPQGATMIATDVASPFFT
PIKLTFMVSLILSAPVILYQVWAFIAPALYKHERRLVVPLLVSSSLLFYIGMAFAYFVVFPLAFGFLAKT
APEGVQVSTDIASYLSFVMALFMAFGVSFEVPVAIVLLCWMGVTTPEDLRKKRPYVLVGAFVVGMLLTPP
DVFSQTLLAIPMYCLFEIGVFFSRFYVGKGRRREEENDAEAESEKTEE
>gnl|CDD|236796 PRK10922, PRK10922, 4-hydroxy-3-polyprenylbenzoate decarboxylase
MDAMKYRDLRDFLTLLEQQGELKRITLPVDPHLEITEIADRTLRAGGPALLFENPKGYSMPVLCNLFGTP
KRVAMGMGQEDVSALREVGKLLAFLKEPEPPKGFRDLFDKLPQFKQVLNMPTKRLRGAPCQQKIWSGDDV
DLNRIPIMTCWPEDAAPLITWGLTVTRGPHKERQNLGIYRQQLIGKNKLIMRWLSHRGGALDYQEWCAAH
PGERFPVSVALGADPATILGAVTPVPDTLSEYAFAGLLRGTKTEVVKCLSNDLEVPASAEIVLEGYIEPG
EMAPEGPYGDHTGYYNEVDSFPVFTVTHITQREDAIYHSTYTGRPPDEPAVLGVALNEVFVPILQKQFPE
IVDFYLPPEGCSYRLAVVTIKKQYAGHAKRVMMGVWSFLRQFMYTKFVIVCDDDVNARDWNDVIWAITTR
MDPARDTVLVENTPIDYLDFASPVSGLGSKMGLDATNKWPGETQREWGRPIKKDPDVVARIDAIWDELAI
FNNGKSA
>gnl|CDD|182842 PRK10923, glnG, nitrogen regulation protein NR(I); Provisional
MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIK
QRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNIQVNGPTTDI
IGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELF
GHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAAT
HQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHFLQVAARELGVEAKLLHPETEAALTR
LAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVPESTSQMQPDSWATLLAQWADRALRSGHQN
LLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME
>gnl|CDD|182843 PRK10925, PRK10925, superoxide dismutase [Mn]
MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPADKKT
VLRNNAGGHANHSLFWKGLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDKLA
VVSTANQDSPLMGEAISGASGFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK
>gnl|CDD|182844 PRK10926, PRK10926, ferredoxin-NADP reductase; Provisional
MADWVTGKVTKVQNWTDALFSLTVHAPVDPFTAGQFTKLGLEIDGERVQRAYSYVNAPDNPDLEFYLVTV
PEGKLSPRLAALKPGDEVQVVSEAAGFFVLDEVPDCETLWMLATGTAIGPYLSILQEGKDLERFKNLVLV
HAARYAADLSYLPLMQELEQRYEGKLRIQTVVSRETAPGSLTGRVPALIESGELEAAVGLPMDAETSHVM
LCGNPQMVRDTQQLLKETRQMTKHLRRRPGHMTAEHYW
>gnl|CDD|236797 PRK10927, PRK10927, cell division protein FtsN
MAQRDYVRRSQPAPSRRKKSTSRKKQRNLPAVSPAMVAIAAAVLVTFIGGLYFITHHKKEESETLQSQKV
TGNGLPPKPEERWRYIKELESRQPGVRAPTEPSAGGEVKTPEQLTPEQRQLLEQMQADMRQQPTQLVEVP
WNEQTPEQRQQTLQRQRQAQQLAEQQRLAQQSRTTEQSWQQQTRTSQAAPVQAQPRQSKPASTQQPYQDL
LQTPAHTTAQSKPQQAAPVTRAADAPKPTAEKKDERRWMVQCGSFRGAEQAETVRAQLAFEGFDSKITTN
NGWNRVVIGPVKGKENADSTLNRLKMAGHTNCIRLAAGG
>gnl|CDD|236798 PRK10929, PRK10929, putative mechanosensitive channel protein; Provisional
MRLIITFLMAWLLSWGAYAATAPDEKQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQY
QQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLS
QLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLSANNRQELARLRS
ELAKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQR
MDLIASQQRQAASQTLQVRQALNTLREQSQWLGVSNALGEALRAQVARLPEMPKPQQLDTEMAQLRVQRL
RYEDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQRELLNSLLSGGDTLILELTKLKVANSQLEDAL
KEVNEATHRYLFWVADVSPISLSYPLEIAQDLRRLLSLDTFSQLGKASVMMLTSKETLLPLFGALLLVGF
SISSRRHYHAFLERSSSRVGKVTQDHFSLTLRTVFWSILVASPLPVLWAALGYGLQNAWPYPLAVAIGDG
VTATVPLLWVFMICATFARPNGLFIAHFGWPRERVARAMRYYLLSIGLIVPLIMALITFDNLNDREFSGT
LGRLCFILLCGALSLVTLSLKRAGIPLYLDKEGSGDNIINHALWNLLIGAPLVAALASALGYLATAQALL
ARLETSVAIWFLLLVVYHIIRRWMLIQRRRIAFDRAKQRRAEILAQRARGEEEAHHSSSPEGAIEVEEPV
IDLDAISAQSLRLVRSILTLIALLSVIVLWSEIHSAFGFLENISLWDVTSTVQGVESLQPITLGSVLIAI
LVFIITTQLVRNLPALLELALLQHLDLTPGTGYAITTITKYLLMLIGGLVGFSMIGIEWSKLQWLVAALG
VGLGFGLQEIFANFISGLIILFEKPIRIGDTVTIRDLTGSVTKINTRATTISDWDRKEIIVPNKAFITEQ
FINWSLSDSVTRVVLTIPAPADANSEEVTEILLTAARRCSLVLDNPAPEVFLVDLQQGIQIFELRIYAAE
MGHRMPLRHEIHQLILAGFREHGIDMPFPPFQMRLESLGGKQTGRTLTSAGKSRTAGSL
>gnl|CDD|236799 PRK10930, PRK10930, FtsH protease activity modulator HflK
MAWNQPGNNGQDRDPWGSSKPGGNSGGNGNKGGRDQGPPDLDDIFRKLSKKLGGLGGGKGTGSGGGSSSQ
GPRPQLGGRVVGIAAAAVVIIWAASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPVNVEAV
RELAASGVMLTSDENVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEGRT
VIRSDTQRELEETIRPYDMGITLLDVNFQAARPPEEVKAAFDDAIAARENEQQYIREAEAYTNEVQPRAN
GQAQRILEEARAYKAQTILEAQGEVARFAKLLPEYKAAPEITRERLYIETMEKVLGHTRKVLVNDKGGNL
MVLPLDQMLKGGNAPAAKSDNGASNLLRLPPASSSTTSGASNTSSSSQGDIMDQRRANAQRNDYQRQGE
>gnl|CDD|182848 PRK10931, PRK10931, adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
MLEQICQLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAW
EVRQHWQRYWLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAWKEECGVRK
QIQVRDARPPLVVISRSHADAELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGH
AVAIAAGAHVHDWQGKTLDYTPRESFLNPGFRVSIY
>gnl|CDD|182849 PRK10933, PRK10933, trehalose-6-phosphate hydrolase; Provisional
MTNLPHWWQNGVIYQIYPKSFQDTTGSGTGDLRGVTQRLDYLQKLGVDAIWLTPFYVSPQVDNGYDVANY
TAIDPTYGTLDDFDELVAQAKSRGIRIILDMVFNHTSTQHAWFREALNKESPYRQFYIWRDGEPETPPNN
WRSKFGGSAWRWHAESEQYYLHLFAPEQADLNWENPAVRAELKKVCEFWADRGVDGLRLDVVNLISKDQD
FPDDLDGDGRRFYTDGPRAHEFLQEMNRDVFTPRGLMTVGEMSSTSLEHCQRYAALTGSELSMTFNFHHL
KVDYPNGEKWTLAKPDFVALKTLFRHWQQGMHNVAWNALFWCNHDQPRIVSRFGDEGEYRVPAAKMLAMV
LHGMQGTPYIYQGEEIGMTNPHFTRITDYRDVESLNMFAELRNDGRDADELLAILASKSRDNSRTPMQWD
NGDNAGFTQGEPWIGLCDNYQEINVEAALADEDSVFYTYQKLIALRKQEPVLTWGDYQDLLPNHPSLWCY
RREWQGQTLLVIANLSREPQPWQPGQMRGNWQLLMHNYEEASPQPCAMTLRPFEAVWWLQK
>gnl|CDD|236800 PRK10935, PRK10935, nitrate/nitrite two-component system sensor histidine kinase NarQ
MMVKRSVTSSIARAMLLIILLSSLTTGFALLTLASSLRDAEAINIAGSLRMQSYRLAYDLQSGSPQLNAH
LREFEQSLHSPALKNLNRWYVPEDVKDRYALLIARWLEMKSYLEQGDSRWYQANIANYVDQIDLFVLALQ
HFAERKLILLAAISLLGLILILTLVFFTVRFTRRQVVAPLNQLVTASQQIEKGQFDHIPLDTTLPNELGL
LAKAFNQMSSELHKLYRSLEASVEEKTRKLTQANRSLEVLYQCSQALNASQIDVHCFRHILQIVRDHEGL
DYLELEVGENEHWRISEGQPNPELPWQILPLTMEDTVLGYLHWQASLPCPDEPLMNNVAQMLGRGLYFNQ
AQKQQQQLLLMEERATIARELHDSLAQVLSYLKIQLTLLKRSLDEDNAKAQSIIAEFDQALSDAYRQLRE
LLTTFRLTIQEANLGSALEEMLDQLRNQTDAKITLDCRLPSQALDAQQQVHLLQIIREATLNAIKHANAS
EIAVSCVTNPDGEHTVSIRDDGIGIGELKEPEGHYGLNIMQERAERLGGTLTISQPPGGGTTVSLTFPSQ
QEPES
>gnl|CDD|236801 PRK10936, PRK10936, TMAO reductase system periplasmic protein TorT; Provisional
MRKLLFLLLSLFLLSLTAFAAANLLTWHLAQRTSLQYSPLLKAKKAWKLCALYPHLKDSYWLSVNYGMVE
EAKRLGVDLKVLEAGGYYNLAKQQQQLEQCVAWGADAILLGAVTPDGLNPDLELQAANIPVIALVNGIDS
PQVTTRVGVSWYQMGYQAGRYLAQWHPKGSKPLNVALLPGPEGAGGSKAVEQGFRAAIAGSDVRIVDIAY
GDNDKELQRNLLQELLERHPDIDYIAGSAVAAEAAIGELRGRNLTDKIKLVSFYLSHQVYRGLKRGKVLA
APSDQMVLQGRLAIDQAVRQLEGAPVPGDVGPKILVLTPKNLDSEDLRRSLSPAGFRPVYRVQ
>gnl|CDD|182852 PRK10938, PRK10938, putative molybdenum transport ATP-binding protein ModF; Provisional
MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRL
SFEQLQKLVSDEWQRNNTDMLSPGEDDTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGE
TRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLAD
CTLAETGEREEILQQALVAQLAHSEQLEGVQLPEPDEPSARHALPANEPRIVLNNGVVSYNDRPILHNLS
WQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRGSGETIWDIKKHIGYVSSSLHLDYR
VSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHP
TLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPACITHRLEFVPDGDIYRYVQTKLN
>gnl|CDD|182853 PRK10939, PRK10939, autoinducer-2 (AI-2) kinase; Provisional
SMSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPDVPGSMEFDLEKNWQLACQCIRQALQKAGI
PASDIAAVSATSMREGIVLYDRNGTEIWACANVDARASREVSELKELHNNFEEEVYRCSGQTLALGALPR
LLWLAHHRPDIYRQAHTITMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPP
VKETGTVLGHVTAKAAAETGLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDP
NMNIRINPHVIPGMVQAESISFFTGLTMRWFRDAFCAEEKLLAERLGIDAYSLLEEMASRVPVGSHGIIP
IFSDVMRFKSWYHAAPSFINLSIDPEKCNKATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGS
KGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENHELYQE
AKEKWQAVYADQLGLVDHGLTTSMWKAPGL
>gnl|CDD|182854 PRK10941, PRK10941, tetratricopeptide repeat-containing protein
MRSLADFEFNKAPLCEGMILASQAIRRDFPSQDVYDELERLVSLAREEISQLLPQDEQLEKLIALFYGEW
GFGGASGVYRLSDALWLDKVLKTRQGSAVSLGAILLWIANRLDLPLMPVIFPTQLILRADWLDGEMWLIN
PFNGETLDEHTLEVWLKGNISPSAELFNEDLDEADNIEVIRKLLDTLKAALMEEKQMELALRASEALLQF
DPEDPYEIRDRGLIYAQLDCEHVALSDLSYFVEQCPEDPISEMIRAQIHSIEQKQIVLH
>gnl|CDD|236802 PRK10942, PRK10942, serine endoprotease DegP
KKTTLALSALALSLGLALSPLSATAAETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRQ
FQQFFGDNSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATKIKV
QLSDGRKFDAKVVGKDPRSDIALIQLQNPKNLTAIKMADSDALRVGDYTVAIGNPYGLGETVTSGIVSAL
GRSGLNVENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMV
EYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALR
AQVGTMPVGSKLTLGLLRDGKPVNVNVELQQSSQNQVDSSNIFNGIEGAELSNKGGDKGVVVDNVKPGTP
AAQIGLKKGDVIIGANQQPVKNIAELRKILDSKPSVLALNIQRGDSSIYLLMQ
>gnl|CDD|170841 PRK10943, PRK10943, cold shock-like protein CspC; Provisional
MAKIKGQVKWFNESKGFGFITPADGSKDVFVHFSAIQGNGFKTLAEGQNVEFEIQDGQKGPAAVNVTAI
>gnl|CDD|182856 PRK10945, PRK10945, hemolysin expression modulator Hha
MSEKPLTKTDYLMRLRRCQTIDTLERVIEKNKYELSDDELAVFYSAADHRLAELTMNKLYDKIPSSVWKF
VR
>gnl|CDD|236803 PRK10946, entE, (2,3-dihydroxybenzoyl)adenylate synthase
MSIPFTRWPEEFARRYREKGYWQDLPLTDILTRHAASDAIAVICGERQFSYRELNQASDNLACSLRRQGI
KPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELNAYASQIEPALLIADRQHALFSDDDFLN
TLVAEHSSLRVVLLLNDDGEHSLDDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYS
VRRSVEICGFTPQTRYLCALPAAHNYPMSSPGALGVFLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVP
PAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTRLDDSDER
IFTTQGRPMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSID
PDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQLR
RFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRASA
>gnl|CDD|182858 PRK10947, PRK10947, DNA-binding transcriptional regulator H-NS
MSEALKILNNIRTLRAQARECTLETLEEMLEKLEVVVNERREEESAAAAEVEERTRKLQQYREMLIADGI
DPNELLNSLAAVKSGTKAKRAARPAKYSYVDENGETKTWTGQGRTPAVIKKAMDEQGKSLDDFLI
>gnl|CDD|236804 PRK10948, PRK10948, Fe-S cluster assembly protein SufD
MAGLPNSSNRALQQWHHLFEAKGGERSPQARQHWQQVLRLGLPTRKHEDWKYTPLEGLLNSQFVFSIAAE
ISPAQRDALALTIDAVRLVFVDGRFSPALSDSTEGPYQVSINDDRQGLPAAIQPEVFLHLTESLAQSVTH
IRLPRGQRPAKPLYLLHITQGVAGEELNTAHYRHHLDLAEGAEATVIEHFVSLNEARHFTGARLTMNVAD
NAHLNHIKLAFENPSSYHFAHNDLLLGRDARAFSHSFLLGAAVLRHNTSTQLNGENSTLRLNSLAMPVKN
EVCDTRTWLEHNKGYCNSRQLHKTIVSDKGRAVFNGLIKVAQHAIKTDGQMTNNNLLLGKLAEVDTKPQL
EIYADDVKCSHGATVGRIDDEQLFYLRSRGINQQDAQQMIIYAFAAELTEAIRDEALKQQVLARIGQRLP
GGIV
>gnl|CDD|182860 PRK10949, PRK10949, signal peptide peptidase SppA
MRTLWRIIAGFFKWTWRLLNFVRELVLNLFFIFLILVGVGIWMQVSNGDTPETASRGALLLDISGVIVDK
PSSSNKLSQLGRQLLGASSDRLQENSLFDIVNTIRQAKDDRNITGIVLDLKNFAGADQPSMQYIGKALRE
FRDSGKPVYAVGDSYSQGQYYLASFANKIYLSPQGVVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKS
AVEPFIRDDMSPAAREADSRWIGELWQNYLNTVAANRQITPQQLFPGAQGILEGLTKVGGDTAKYALDNK
LVDALASSAEIEKALTKAFGWSKTDKNYRAISIYDYALKTPADTGGSIAVIFANGAIMDGEETPGNVGGD
TTAAQIRDARLDPKVKAIVLRVNSPGGSVTASEVIRAELAAARAAGKPVVVSMGGMAASGGYWISTPANY
IVASPSTLTGSIGIFGVINTVENSLDSIGVHTDGVSTSPLADVSITKALPPEFQQMMQLSIENGYKRFIT
LVADSRHKTPEQIDKIAQGHVWTGQDAKANGLVDSLGDFDDAVAKAAELAKLKQWHLNWYVDEPTFFDMV
MDQMSGSVRAMLPDAIQAMLPAPLASVASTVKSESDKLAAFNDPQNRYAFCLTCANVR
>gnl|CDD|236805 PRK10952, PRK10952, proline/glycine betaine ABC transporter permease ProW
NMADQNNPWDTTPAADSAAQSADAWGTPAGAPTDGGGADWLNSAPAPAPEHFNILDPFHKTLIPLDSWVT
EGIDWVVTHFRPVFQGIRVPVDYILNGFQQLLLGMPAPVAIIVFALIAWQISGVGMGVATLVSLIAIGAI
GAWSQAMVTLALVLTALLFCIVIGLPLGIWLARSPRAAKIIRPLLDAMQTTPAFVYLVPIVMLFGIGNVP
GVVVTIIFALPPIVRLTILGINQVPADLIEASRSFGASPRQMLFKVQLPLAMPTIMAGVNQTLMLALSMV
VIASMIAVGGLGQMVLRGIGRLDMGLATVGGVGIVILAIILDRLTQAVGRDSRSRGNRRWYTTGPVGLLT
RPFIK
>gnl|CDD|182862 PRK10953, cysJ, NADPH-dependent assimilatory sulfite reductase flavoprotein subunit
MTTQAPPSALLPLNPEQLARLQAATTDLSPTQLAWVSGYFWGVLNQQPGAVAATPAPAAEMPGITLISAS
QTGNARRVAEQLRDDLLAAKLNVNLVNAGDYKFKQIAQEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKA
PKLENTAFAVFGLGDTSYEFFCQAGKDFDSKLAELGAERLLDRVDADVEYQAAASEWRARVVDALKSRAP
AVAAPSQSVATGAVNEIHTSPYSKEAPLTASLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVW
YQNDPALVKELVELLWLKGDEPVTVDGKTLPLAEALQWHFELTVNTANIVENYATLTRSETLLPLVGDKA
ALQHYAATTPIVDMVRFAPAQLDAEQLIGLLRPLTPRLYSIASSQAEVENEVHITVGVVRYDIEGRARAG
GASSFLADRLEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADGAPGKNWLFFGN
PHFTEDFLYQVEWQRYVKEGLLTRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDGAHIYVCGDANRMA
KDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY
>gnl|CDD|182863 PRK10954, PRK10954, thiol:disulfide interchange protein DsbA
MKKIWLALAGMVLAFSASAAQFTDGKQYTTLDKPVAGEPQVLEFFSFYCPHCYQFEEVYHVSDNVKKKLP
EGTKMTKYHVEFLGPLGKELTQAWAVAMALGVEDKVTPPLFEGVQKTQTIQSAADIRDVFIKAGVKGEDY
DAAWNSFVVKSLVAQQEKAAADLQLRGVPAMFVNGKYMVNNQGMDTSSMDVYVQQYADVVKFLLEKK
>gnl|CDD|182864 PRK10955, PRK10955, envelope stress response regulator transcription factor CpxR
MNKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSIDLLLLDVMMPKKNGIDTLKELRQTH
QTPVIMLTARGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRSHWSEQQQNNDNGSPTLEVDALS
LNPGRQEASFDGQTLELTGTEFTLLYLLAQHLGQVVSREHLSQEVLGKRLTPFDRAIDMHISNLRRKLPD
RKDGHPWFKTLRGRGYLMVSAS
>gnl|CDD|236806 PRK10957, PRK10957, iron-enterobactin transporter periplasmic binding protein; Provisional
PLYRLALLLLGLLLSGIAAAQASAAGWPRTVTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDAPVIASGA
TTPNTRVADDQGFFRQWSDVAKERGVEVLYIGEPDAEAVAAQMPDLIVISATGGDSALALYDQLSAIAPT
LVIDYDDKSWQELATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYNGAGHSANLWTPE
SAQGQLLEQLGFTLAELPAGLQASTSQGKRHDIIQLGGENLAAGLNGETLFLFAGDDKDADAFLADPLLA
NLPAVQNKQVYALGTDTFRLDYYSATQLLDRLAALFG
>gnl|CDD|236807 PRK10958, PRK10958, leucine export protein LeuE; Provisional
MFAEFGVTDLWTYLVGAIFIVLLPGPNSLYVLSTAARRGVKAGYRAACGVFIGDAVLMFLAAAGVASLLK
ATPLLFNVVKYLGAAYLLYLGVKMLRAALRRWRRRAASAAPPYGAPFRRALILSLTNPKAILFFVSFFVQ
FVDPNYAHPALSFLILATILQLVSFCYLSFLIFSGARLAAYFRRRKKLAAGGNSLVGLLFVGFAAKLATA
TS
>gnl|CDD|182867 PRK10959, PRK10959, outer membrane protein W; Provisional
MKKLTVAALAVATLLSGSAFAHEAGDFIVRAGTATVRPNEGSDGVLGSLGEFSVSNNTQLGLTFGYMATD
NIGVELLAATPFRHKVGLGGTGDIAEVKHLPPTLMAQYYFGDAQSKLRPYVGAGVNYTTFFDEKFNDTGK
DAGLSDLSLKDSWGVAGQVGLDYLINKNWLLNASVWYMDIDTDVKFKLGGAQQKISTRLDPWVFMFSAGY
RF
>gnl|CDD|236808 PRK10963, PRK10963, hypothetical protein; Provisional
TELDDRAVVDYLLQNPDFFIRNARLVEQMRVPHPVRGTVSLVEWQMARQRNHIHVLEEEMTLLMEQAIAN
EDLFYRLLPLQSRLAAADSLQDMLMRLHRWARDLGLAGAKIRLFPDRWRLGAPSDFTHLALSRQAFEPLR
IQRLGQRQHYLGPLNGPELLLLLPEAKAVGSVAMSLLGSDGDLGVLLFSSRDAQHYQQGQGTQLLQHLAL
MLPELLERWIERV
>gnl|CDD|236809 PRK10964, PRK10964, lipopolysaccharide heptosyltransferase RfaC
MRVLIVKTSSMGDVLHTLPALTDAQQAIPGIQFDWVVEEGFAQIPSWHPAVDRVIPVAIRRWRKAWFSAP
IRAERKAFREALQAEQYDAVIDAQGLVKSAALVTRLAHGVKHGMDWQSAREPLASLFYNRRHHIAKQQHA
VERTRELFAKSLGYSKPQTQGDYAIAQHFLTNLPADAGPYLVFLHATTRDDKHWPEAHWRELIGLLAPSG
LRIKLPWGAEHEEQRAKRLAEGFPYVEVLPKLSLEQVARVLAGAKAVVSVDTGLSHLTAALDRPNITLYG
PTDPGLIGGYGKNQHACRSPGKSMADLSAETVFQKLETLISL
>gnl|CDD|236810 PRK10965, PRK10965, multicopper oxidase; Provisional
MQRRDFLKLSAALGAASALPLWSRAAFAAERPALPIPPLLTPDARGRIQLTIQAGQSSFAGKTATATWGY
NGNLLGPAVRLQRGKAVTVDITNQLPEETTLHWHGLEVPGEVDGGPQGIIAPGGKRTVTFTVDQPAATCW
FHPHQHGKTGRQVAMGLAGLVLIEDDESLKLGLPKQWGVDDIPVILQDKRFSADGQIDYQLDVMTAAVGW
FGDTLLTNGAIYPQHAAPRGWLRLRLLNGCNARSLNLATSDGRPLYVIASDGGLLAEPVKVSELPILMGE
RFEVLVDTSDGKAFDLVTLPVSQMGMALAPFDKPLPVLRIQPLLISASGTLPDSLASLPALPSLEGLTVR
RLQLSMDPRLDMMGMQMLMEKYGDQAMAGMDMDHMMGHMGHGNMDHMNHGAADAGPAFDFHHANKINGKA
FDMNKPMFAAKKGQYERWVISGVGDMMLHPFHIHGTQFRILSENGKPPAAHRAGWKDTVRVEGGRSEVLV
KFDHDAPKEHAYMAHCHLLEHEDTGMMLGFTVS
>gnl|CDD|182871 PRK10966, PRK10966, exonuclease subunit SbcD; Provisional
MRILHTSDWHLGQNFYSKSRAAEHQAFLDWLLEQVQEHQVDAIIVAGDIFDTGSPPSYARELYNRFVVNL
QQTGCQLVVLAGNHDSVATLNESRDLLAFLNTTVIASASDDLGHQVIILPRRDGTPGAVLCAIPFLRPRD
VITSQAGQSGIEKQQALQAAIADHYQQLYQLACELRDELGQPLPIIATGHLTTVGASKSDSVRDIYIGTL
DAFPAQAFPPADYIALGHIHRAQKVGGTEHIRYSGSPIPLSFDELGKSKSVHLVEFDQGKLQSVTPLPVP
VFQPMAVLKGDLASITAQLEQWRDVSQEPPVWLDIEVTTDDYLHDIQRRIQALTESLPVEVLLVRRSREQ
RERSLASEQRETLSELSVEEVFERRLALEELDEPQQQRLTQLFTQVLHELAEEHEAA
>gnl|CDD|182872 PRK10969, PRK10969, DNA polymerase III subunit theta; Reviewed
MGKNLAKLSQEEMDKVNVDLAASGVAFKERYNMPVIAEAVEREQPEHLRSYFRERLIAYRLASVNLSRLP
YEPKV
>gnl|CDD|182873 PRK10971, PRK10971, sulfate/thiosulfate ABC transporter permease CysT
MLAVSSKRVLPGFTLSLGTSLLFVCLILLLPLSALVMQLSQMSWAQYWEVITNPQVVAAYKVTLLSAFVA
SIFNAVFGLLMAWILTRYRFPGRTLLDALMDLPFALPTAVAGLTLASLFSVNGWYGEWLAKFDIKVTYTW
LGIAVAMAFTSIPFVVRTVQPVLEELGPEYEEAAETLGATRWQSFRKVVLPELSPALLAGVALSFTRSLG
EFGAVIFIAGNIAWKTEVTSLMIFVRLQEFDYPAASAIASVILAASLLLLFSINTLQSRFGRRVVGH
>gnl|CDD|182874 PRK10972, PRK10972, cell division protein ZapA
MSAQPVDIQIFGRSLRVNCPPEQRDALNQAAEDLNQRLQDLKERTRVTNTEQLVFIAALNICYELAQEKA
KTRDYAANMEQRIRMLQQTIEQALLEQGRITEKTNQNFE
>gnl|CDD|182875 PRK10973, PRK10973, sn-glycerol-3-phosphate ABC transporter permease UgpE
MIENRRGLDIFSHTMLILGIAVILFPLYVAFVAATLDKQAVFAVPMTLIPGTHLLENIANIWVNGVGNNS
APFGRMLLNSFVMAFSITVGKITVSMLSAFAIVWFRFPLRNLFFWMIFITLMLPVEVRIFPTVEVIANLK
MLDSYAGLTLPLMASATATFLFRQFFMTLPDELVEAARIDGASPMRFFWDIVLPLSKTNLAALFVITFIY
GWNQYLWPLLIITDVSLGTAVAGIKGMIATGEGTTEWNQVMAAMLLTLIPPVVIVLAMQRAFVRGLVDSE
K
>gnl|CDD|182876 PRK10974, PRK10974, sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB
FMKSLRSTALGLALGLALSGNAQAVTEIPFWHSMEGELGKEVDSLAQRFNASQPDYKIVPVYKGNYEQSL
AAGIAAFRSGNAPAILQVYEVGTATMMASKAIKPVYDVFKDAGIPFDESQFVPTVAGYYSDAKTGHLLSQ
PFNSSTPVLYYNKDAFKKAGLDPEQPPKTWQDLAAYAAKLRAAGMKCGYASGWQGWIQLENFSAWHGLPF
ASKNNGFDGTDAVLEFNKPEQVKHIALLEEMNKKGDFTYVGRKDESTEKFYNGDCAITTASSGSLANIRK
YAKFNYGVGMMPYDADVKGAPQNAIIGGASLWVMQGKDKETYKGVAKFLDFLAKPENAAEWHQKTGYLPI
TTAAYDLTREQGFYEKNPGADTATRQMLNKPPLPFTKGLRLGNMPQIRTIVDEELESVWTGKKTPQQALD
SAVERGNQLLRRFEKSTK
>gnl|CDD|182877 PRK10975, PRK10975, dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase
LAAFSLVQAKVAASDTALLDALQQLGFQLVEGEVDFALPVGNASDTTGARVATETDIPALRQLAAQAFAQ
SRFRAPWYAPDDSGRFYAQWIENAVRGTFDHQCLLLRDASGQIQGFVTLRELNDTDARIGLLAVFPGAQG
RGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGANIESTAYWLYR
>gnl|CDD|182878 PRK10976, PRK10976, putative hydrolase; Provisional
MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARV
HDTDGNLIFSHNLDRDIASDLFGVVHDNPDIITNVYRDDEWFMNRHRPEEMRFFKEAVFKYQLYEPGLLE
PDGVSKVFFTCDSHEKLLPLEQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCI
AFGDGMNDAEMLSMAGKGCIMGNAHQRLKDLLPELEVIGSNADDAVPHYLRKLYLS
>gnl|CDD|182880 PRK10982, PRK10982, galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA
LENGISMVHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQM
QMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG
QWIATQPLAGLTMDKIIAMMVGRSLTQRFPDKENKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIA
GLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRSTGIYAYLDIGFNSLIS
NIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR
GIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEILRLASLH
L
>gnl|CDD|182881 PRK10983, PRK10983, AI-2E family transporter YdiK
MVNVRQPRDLAQILLSVLFIAIMIVACFWVVQPFILGFAWAGMVVIATWPLLLKLQKILWGRRSLAVLVM
TLLLVLLFVIPIALLVNSLVDNSGPLIKWASSGDMTLPDLAWLNSIPLIGAKLYSGWHNLLDMGGSALMA
KVRPYIGTTTTWFVGQAAHIGRFMMHCALMLLFSALLYWRGEQVALGIRHFATRLAGKRGDAAVLLAAQA
IRAVALGVVVTALVQAVLGGIGLAISGVPYATLLTVLMILSCLVQLGPLPVLIPAIIWLYWTGDTTWGTV
LLVWSCVVGTLDNVIRPMLIRMGADLPMILILSGVIGGLIAFGMIGLFIGPVVLAVSYRLFSAWVHEVPP
PTDQPEEILEELEEIEKP
>gnl|CDD|182882 PRK10984, PRK10984, sigma factor-binding protein Crl
MTLPSGHPKSRLIKKFTALGPYLREGQCEENRFFFDCLAVCVNVKPAPEKREFWGWWMELEAQEGRFTYS
YQFGLFDKEGNWVAEPIKDKEVVERLEHTLREFHEKLRELLATLELKLEPADDFNDE
>gnl|CDD|182883 PRK10985, PRK10985, putative hydrolase; Provisional
SAEFTPMRGASNPHLQTLLPRLIRRKVLFTPYWQRLELPDGDFVDLAWSEDPAQARHKPRLVLFHGLEGS
FNSPYAHGLLEAAQKRGWLGVVMHFRGCSGEPNRLHRIYHSGETEDARFFLRWLQREFGHVPTAAVGYSL
GGNMLACLLAKEGDDLPLDAAVIVSAPLMLEACSYRMEQGFSRVYQRYLLNLLKANAARKLAAYPGTLPI
NLAQLKSVRRLREFDDLITARIHGFADAIDYYRQCSALPLLNQIRKPTLIIHAKDDPFMTHEVIPKPESL
PPNVEYQLTEHGGHVGFVGGTLLKPQMWLEQRIPDWLTTYLEAK
>gnl|CDD|236811 PRK10987, PRK10987, beta-lactamase regulator AmpE
MTLFSLLLVLIVERLFKLGEHWQLDHRLEAFFRRKKHFSLLRTLLALLLPMLVVFLLLWLLQGLLFGVPT
LLLWILIGLLCIGAGKQRLHYKAYLQAACRGDSQACYHMAEELTLIHGLPADVSERELLRELQQALLWIN
YRYYLAPLFWFIVLGPWGAVLLMGYAFLRAYQEWLARYQTPLPRAQSGIDALLHVLDWLPVRLAGFGYAL
LGHFEKALPAWFASLLDFHTSQYQVLTRLAQFSLAREPHLDCVQTPLAAVSLAKRNFLLLVVVIALLTIY
GALV
>gnl|CDD|182885 PRK10991, fucI, L-fucose isomerase; Provisional
KISLPKIGIRPTIDGRRMGVRESLEEQTMNMAKATAALITENLRHACGEPVECVIADTCIGGVAEAAACE
EKFSSENVGLTITVTPCWCYGSETIDMDPTRPKAIWGFNGTERPGAVYLAAALAAHSQKGIPAFSIYGHD
VQDADDTSIPADVEEKLLRFARAGLAVASMKGKSYLSIGGVSMGIAGSIVDHNFFESYLGMRVEAVDMTE
LRRRIDQKIYDEEELEMALAWAKKNCKEGEDENAEQYQRNAEQKRAVWEESVKMAMIIRDLMQGNPKLAE
LGFVEEALGHNAIAAGFQGQRHWTDQYPNGDFAEAILNSSFDWNGVREPFVVATENDSLNGVAMLFGHLL
TGTAQIFADVRTYWSPEAVERVTGHKLEGLAEHGIIHLINSGSAALDGTGQQRDSEGNPTMKPHWEITEQ
EADACLAATEWCPAIHEYFRGGGFSSRFLTEGGMPFTMTRLNLIKGLGPVLQIAEGWSVELPKDVHDILD
KRTDPTWPTTWFAPRLTGKGAFTDVYSVMANWGANHGVLTYGHVGADLITLASMLRIPVCMHNVEEEKIF
RPSAWAAFGMDKEGQDYRACQNYGPLYK
>gnl|CDD|236812 PRK10992, PRK10992, iron-sulfur cluster repair protein YtfE
MAYRDQPLGELALSIPRATALFREYDLDFCCGGKQTLARAAARKNLDIDVIEARLAALQEQPIEKDWRSA
PLAELIDHIIVRYHDRHREQLPELILLATKVERVHGDKPDCPRGLAKYLTALHEELSSHMMKEEQILFPM
IKQGMGSQAMGPISVMESEHDEAGELLEVIKHLTNNVTPPPEACTTWRALYNGINELIDDLMEHIHLENN
VLFPRALAGE
>gnl|CDD|236813 PRK10993, PRK10993, omptin family outer membrane protease
MKKKLLAIALIAPLAISAFASTATASFDVTPDNVSVSISLGTLSGKSKELVYDEEGGRKLSQLDWKIKNA
AIIKGDINWDLLPRLSLGASGWTTLASGGGHMVDYDWLDSSQPGWTDRSHHPDTDLNYANEFDLNLKGWL
LQNPNYRLGVMAGYQETRFSWTAYGGSYIYSNGGFRDDIGTFPDGERGIGYKQRFKMPYIGLTGSYRYDD
FEFGGLLKYSGWVSASDNDEHYLRNLTFRDKFKNSPYYSASINAGYYVTPNAKLYVEGAYNRYFEGKGDT
QIYDHATGTSSYFKDAAGIENQNYTVTAGLKYRF
>gnl|CDD|236814 PRK10995, PRK10995, MarC family NAAT transporter
MLDLFKAIGLGLVVLLPLANPLTTVALFLGLSGNMTPEERNRQALMASVYVFAIMMVAFYAGQLVMSTFG
ISIPGLRIAGGLIVAFIGFRMLFPQQKAEDSPEAKSKSEELEDEPSANIAFVPLAMPSTAGPGTIAMIIS
SASTIAEGSTFADWVLMVAPPLIFLLVALILWGSLRSSGAIMRLLGKGGIEAISRLMGFLLVCMGVQFII
NGILEIIKTYH
>gnl|CDD|182889 PRK10996, PRK10996, thioredoxin 2; Provisional
MNTVCTSCQAINRLPDERIEDAAKCGRCGHDLFDGEVINATGETLDKLLQDDLPVVIDFWAPWCGPCRNF
APIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNGAVPKAPFDSWLNEAL
>gnl|CDD|236815 PRK10997, yieM, ATPase RavA stimulator ViaA
MLTLDTLNLLLAISESGLIEEMIIALLASPQLAVFFEKFPRLKRALTKDLPRWREALRQRLKDACVPPEL
AEEFALYQQSQLLSTPQFIVQLPDILDKLHRLHSPFAEQARQLVDANKGANSPITSALHTLFLQRWRLSL
VVQTTTLNQQLLEQEREQLLAELQQRMTLSGQLEPVLAENDEAAGRLWDMSAGQLKRGDYQLIVQYGEFL
KQQPELQKLAEQLGRSREAKSVPRNDAPMETFRTMVREPDTVPEQVVGIHQSDDILRLLPPELATLGIPE
LEYEFYRRLVEKRLLTYRLQGESWREKTVERPVVHQDQDEQPRGPFIVCVDTSGSMGGFNEQCAKAFCLA
LMRIALAENRRCYIMLFSTEVVTYELTGPDGLEQAIRFLSQSFRGGTDLAPCLRAIIEKMQGREWFDADA
VVISDFIAQRLPDELVAKVKELQRQHQHRFHAVAMSAHGKPGIMRIFDHIWRFDTGLRSRLLRRWRR
>gnl|CDD|182891 PRK10998, malG, maltose ABC transporter permease MalG
MAMVQPKSQKLRLFATHLLLLGFIALIMFPLLMVIAISLREGNFATGSLIPEQISWEHWKLALGFSVEHA
DGRVTPPPFPVLLWLWNSVKVAGITAIGIVALSTTCAYAFARMRFKGKATLLKGMLIFQMFPAVLSLVAL
YALFDRLGQYIPFIGLNTHGGVIFAYLGGIALHVWTIKGYFETIDSSLEEAAALDGATPWQAFRLVLLPL
SVPILAVVFILSFIAAITEVPVASLLLRDVNSYTLAVGMQQYLNPQNYLWGDFAAAAVLSAIPITVVFLL
AQRWLVGGLTAGGVKG
>gnl|CDD|236816 PRK10999, malF, maltose ABC transporter permease MalF
TAMMDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAILTLILSSLGLYIFANRKAYAWRY
VYPGLAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQSVLLDRTYQAGKTYNFGLYPAGDEWQLALTD
GETGKNYLSEPFSLEAGGEQKLQLKETDALPEGERAPLRVITQNRQALSQITAVLPDGNKLRMSSLRQFS
GTKPLYTLDDDGTTLTNNQSGVKYRPNNDIGFYQSINADGNWGGEKLSPGFTVTIGWKNFTRVFTDEGIQ
KPFIAIFIWTVVFSLLTVVLTVAVGMVLACLVQWEALKGKAVYRVLLILPYAVPSFISILIFKGLFNQSF
GEINMMLSALFGIKPAWFSDPTLAKTMILIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGAGPFQNF
FKITLPLLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDMIGTTTPAGYTDLLVSYTYRIAFEGGGGQDF
GLAAAIATLIFLLVGALAILNLKATKMKFD
>gnl|CDD|182893 PRK11000, PRK11000, maltose/maltodextrin ABC transporter ATP-binding protein MalK
MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV
PPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQ
RVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG
RVAQVGKPLELYHYPANRFVAGFIGSPKMNFLPVKVTATAIEQVQVELPNRQQVWLPVEGRGVQVGANMS
LGIRPEHLLPSDIADVTLEGEVQVVEQLGNETQIHIQIPAIRQNLVYRQNDVVLVEEGATFAIGLPPERC
HLFREDGTACRRLHKEPGV
>gnl|CDD|236817 PRK11001, mtlR, MltR family transcriptional regulator
QAFENRVLERLNAGKTVRGFFIAAVELLTEAVDILVQRVFRKDDYAVKYAVEPLLDGDGPLGDLSVRLKL
LYGLGVISREEYEDIELLIALREELNHDGNEYRFTDDEILGPFGELHCVAALPPPLEFPQPDDADSSLYQ
MQLQRYQQVVRSTLVLSITEIISELSLKSPF
>gnl|CDD|182895 PRK11006, phoR, phosphate regulon sensor histidine kinase PhoR
MLERLSWKRLVLELALFCLPALILGAFFGYLPWFLLASVTGLLIWHFWNLLRLSWWLWVDRSMTPPPGRG
SWEPLFYGLYQMQLRNRKRRRELGNLIKRFRSGAESLPDAVVLTTEEGNIFWCNGLAQQLLGFRWPEDNG
QNILNLLRYPEFTQYLKTRDFSRPLTLVLNNGRHLEIRVMPYTEGQLLMVARDVTQMHQLEGARRNFFAN
VSHELRTPLTVLQGYLEMMQDQPLEGALREKALHTMREQTQRMEGLVKQLLTLSKIEAAPTIDLNEKVDV
PMMLRVLEREAQTLSQGKHTITFEVDNSLKVFGNEDQLRSAISNLVYNAVNHTPEGTHITVRWQRVPQGA
EFSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFV
LPERLIAKNS
>gnl|CDD|182896 PRK11007, PRK11007, PTS system trehalose(maltose)-specific transporter subunits IIBC; Provisional
MMSKINQQDIDRLIELVGGRENIATVSHCITRLRFVLNDPANADPKEIEQLPMVKGCFTNAGQFQVVIGT
EVGDYYKALIATTGQAEVDKEQAKKAARQNMKWHERLISHFAEIFFPLLPALISGGLILGFRNVIGDIPM
SDGQTLAQMYPFWQTIYDFLWLIGEAIFFYLPVGICWSAVKKMGGTPILGIVLGVTLVSPQLMNAYLLGQ
QLPEVWDFGLFSIEKVGYQAQVIPALLAGLALGFIETRLKRIVPDYLYLVVVPVCSLILAVFLAHALIGP
FGRMIGDGVAFAVKALMTGSFAPIGAALFGFLYAPLVITGVHQTTLAIDLQMIQSMGGTPVWPLIALSNI
AQASAVVGIIIISRKHNEREISVPAAISAYLGVTEPAMYGINLKYRFPMLCAMIGSALAGLICGLNGVMA
NGIGVGGLPGILSIQPQYWQVYALAMLVAIVVPIVLTSFIYKRKERLGTLDIV
>gnl|CDD|182898 PRK11010, ampG, muropeptide MFS transporter AmpG
MSSQYLRIFQQPNSAILLILGFASGLPLALTSGTLQAWMTVENIDLKTIGFFSLVGQAYVFKFLWSPLMD
RYTPPFLGRRRGWLLATQLLLLVAIAAMGFLEPGTQLRWLAALAVVIAFCSASQDIVFDAWKTDVLPAEE
RGAGAAISVLGYRLAMLVSGGLALWLADRYLGWQGMYWLMAALLIPCIIATLLAPEPTDTIPVPKTLEQA
VVAPLRDFFGRNNAWLILLLIVLYKLGDAFAMSLTTTFLIRGVGFDAGEVGLVNKTLGLLATIVGALYGG
ILMQRLSLFRALMIFGILQGVSNAGYWLLSITDKNLYSMGAAVFFENLCGGMGTAAFVALLMTLCNKSFS
ATQFALLSALSAVGRVYVGPVAGWFVEAHGWPTFYLFSVAAAVPGLLLLLVCRQTLEYTQKTDNFIPRTE
YPAGYRFALRLLLAGVSLLAVWLLLLTMNALDLTHFSFLPATLLEVGVLVALSGIVLGGLLDYLALRKTH
L
>gnl|CDD|236819 PRK11013, PRK11013, DNA-binding transcriptional regulator LysR; Provisional
MAAVSLRHIEIFHAVMTAGSLTEAARLLHTSQPTVSRELARFEKVIGLKLFERVRGRLHPTVQGLRLFEE
VQRSYYGLDRIVSAAESLREFRQGQLSIACLPVFSQSLLPGLCQPFLARYPDVSLNIVPQESPLLEEWLS
AQRHDLGLTETLHTPAGTERTELLTLDEVCVLPAGHPLAAKKVLTPDDFAGENFISLSRTDSYRQLLDQL
FAEHGVKRRMVVETHSAASVCAMVRAGVGVSIVNPLTALDYAGSGLVVRRFSISVPFTVSLIRPLHRPAS
ALVDAFSEHLQQQAPALVTRLAAILGPAT
>gnl|CDD|236820 PRK11014, PRK11014, HTH-type transcriptional repressor NsrR
MQLTSFTDYGLRALIYMASLPEGRMTSISEVTEVYGVSRNHMVKIINQLSRAGYVTAVRGKNGGIRLGKP
ASTIRIGDVVRELEPLSLVNCSSEFCHITPACRLKQALSKAVQSFLKELDNYTLADLVEENQPLYKLLLV
E
>gnl|CDD|236821 PRK11017, codB, cytosine permease; Provisional
LSPVPQSARKGVLSLTMVMLGFTFFSASMWAGGTLGTGLSFVDFLLAVLIGNLLLGIYTAALGYIGAKTG
LSTHLLARFSFGEKGSWLPSLLLGFTQVGWFGVGVAMFAIPVVKATGLDINLLIVLSGLLMTVTAYFGIS
ALTILSRIAVPAIALLGGYSVWLAVNDVGGLDGLKAIVPAEPLDFSAALTLVVGSFISGGTLTADFVRFG
RSAKIAVLATMVAFFLGNSLMFIFGAAGAAVYGQADISDVMIAQGLLIPAIVMLGLNIWTTNDNALYASG
LGFCNITRLSSRTLTVVNGIIGTVLALWLYNNFVGWLTLLGSAIPPVGGVIIADYFMNRRGRYPDFATAR
LPRVNWAAILAVALGAAAGHFLPGIVPVNAVLGGALSYIVLNPLLNRKTAAASE
>gnl|CDD|236822 PRK11018, PRK11018, putative sulfurtransferase YedF
MMKNIVPDYRLDMVGEPCPYPAVATLEALPQLKKGEILEVVSDCPQSINNIPLDARNHGYTVLDIQQDGP
TIRYLIQK
>gnl|CDD|182903 PRK11019, PRK11019, DksA/TraR family C4-type zinc finger protein
MASGWANDGAVQEQIDATVEDAIARARSELPRGESLTECEECGEPIPEARRKAIPGVRLCVACQQEKDLQ
QAAFSGYNRRGSKDSQLR
>gnl|CDD|182904 PRK11020, PRK11020, YibL family ribosome-associated protein
MVEKNEIKRLSDRLDAIRHKLAAASLRGDAEKYAQFEKEKATLEAEIARLKEVQSQKLSKEAQKLMKLPF
SRAITKKEQADMGKLKKSVRGLVVVHPMTALGREMGLKEMTGFAKKAF
>gnl|CDD|236823 PRK11021, PRK11021, putative transporter; Provisional
LGLWQGIGLLSTSLLGTGVFAVPALAALVAGNNSLWAWPLLILLIFPIAIVFARLGRHFPHAGGPAHFVG
MAFGPRLGRVTGWLFLSVIPVGLPAALQIAAGFGQALFGWSSWQLLLAELLTLALLWLLNLRGASSSANL
QTVIALLIVALVVAIWWAGDIKPADIPFPAPGSIEWSGLFAALGVMFWCFVGIEAFAHLASEFKNPERDF
PRALMIGLLLAGLVYWACTVVVLHFPAYGDKQAAAASLPGIFVQLFGGYALWVICVIGYLACFASVNIYT
QSFARLVWSQAREGRPPSYLARLSARGVPVNALNAVLGCCAVSILLIYALGLNLEALIAYANGIFVLIYL
LCMLAACKLLKGRYRPLAVLGCLLCLLLLVMLGWKMLYALIMLALLWLFLPKRKTHLSRK
>gnl|CDD|182906 PRK11022, dppD, dipeptide transporter ATP-binding subunit; Provisional
MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEF
NGQDLQRISEKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGI
PDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLI
THDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDR
PNGCLLNPRCPYATDRCRAEEPALNMLAGRQSKCHYPLDDAGRPTL
>gnl|CDD|182907 PRK11023, PRK11023, divisome-associated lipoprotein YraP
MKALSPLAVLLSALLLQGCVAAAVVGTAAVATKAATDPRTVGTQVDDGTLELRVNNALSKDEQIKKEARI
NVTAYQGKVLLTGQSPNAELSERAKQIAMGVEGVNEVYNEIRQGQPIGLGTASKDTWITTKVRSQLLTSD
SVKSSNVKVTTENGEVFLLGLVTQREAKAAADIASRVSGVKRVTTAFTYLK
>gnl|CDD|236824 PRK11024, PRK11024, colicin uptake protein TolR; Provisional
ARARGRGRRELKSEINIVPLLDVLLVLLLIFMATAPIITQSVEVDLPDATESQAVSSNDNPPVIVEVSGV
GQYTVVVDKDRMEQLPEEQVVAEAKSRFKANPKTVFLIGGAKDVPYDEIIKALNLLHSAGVKSVGLMTQP
I
>gnl|CDD|182909 PRK11025, PRK11025, 23S rRNA pseudouridine(955/2504/2580) synthase RluC
MKTETPSVKIVTISADEAGQRIDNFLRTQLKGVPKSMIYRILRKGEVRVNKKRIKPEYKLEAGDEVRIPP
VRVAEREEEAVSPKLQKVAALADVILYEDDHILVLNKPSGTAVHGGSGLSFGVIEGLRALRPEARFLELV
HRLDRDTSGVLLVAKKRSALRSLHEQLREKGMQKDYLALVRGQWQSHVKVVQAPLLKNILQSGERIVRVS
QEGKPSETRFKVEERYAFATLVRASPVTGRTHQIRVHTQYAGHPIAFDDRYGDREFDQQLTGTGLNRLFL
HAAALKFTHPGTGEVMRIEAPLDEQLKRCLQKLRNAK
>gnl|CDD|182910 PRK11026, ftsX, putative protein insertion permease FtsX. FtsX is an integral membrane protein encoded in the same operon as signal recognition particle docking protein FtsY and FtsE. It belongs to a family of predicted permeases and may play a role in the insertion of proteins required for potassium transport, cell division, and other activities. FtsE is a hydrophilic nucleotide-binding protein that associates with the inner membrane by means of association with FtsX [Cellular processes, Cell division, Protein fate, Protein and peptide secretion and trafficking]
HIRQFTNGFNEQVRYAWRGALADLKRKPLATLLTVMVIAISLTLPSVCYLVWKNVNQAATQWYPSPQLTV
YLDKTLDDDAANAVVEQLKAEDGVEKVNYLSREEALGEFRNWSGFGGALDMLEENPLPAVAIIIPKLDFQ
SSEKLNTLRDRLAQIKGVDEVRMDDSWFARLAALTGLVGRVAAMIGVLMVAAVFLVIGNSVRLSIFSRRD
TINVMKLIGATDGFILRPFLYGGALLGFSGALLSLILSEILVWRLSSAVTYVADVFGTKFDLNGLSFDEC
LLLLLVCSMIGWVAAWLATVQHLRRFTPE
>gnl|CDD|236825 PRK11027, PRK11027, hypothetical protein; Provisional
MAESFRTTKRFFDDKNYPRGFSRSGDFTIKEAQLLERYGYAMNALDLGKREPVTEEEKQFVAVCRGEREP
VTEFEKVWLKYMKRIRRPKRFHTLSGGKPQVDGVEDYTDSDD
>gnl|CDD|182912 PRK11028, PRK11028, 6-phosphogluconolactonase; Provisional
KQIVYIASPESQQIHVWNLNHEGALTLLQVVDVPGQVQPMVISPDKRHLYVGVRPEFRVLSYRIADDGAL
TFAAESPLPGSPTHISTDHQGRFLFSASYNANCVSVSPLDKDGIPVAPIQIIEGLEGCHSANIDPDNRTL
WVPCLKEDRIRLFTLSDDGHLVAQEPAEVTTVEGAGPRHMVFHPNQQYAYCVNELNSSVDVWQLKDPHGE
IECVQTLDMMPADFSDTRWAADIHITPDGRHLYACDRTASLISVFSVSEDGSVLSFEGHQPTETQPRGFN
IDHSGKYLIAAGQKSHHISVYEIDGETGLLTELGRYAVGQGPMWVSVLAL
>gnl|CDD|182913 PRK11029, PRK11029, protease modulator HflC
MRKSVIAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVLRDDDNKPLVYAPGLHFKIPFIETVKMLDARIQ
TMDNQADRFVTKEKKDLIVDSYIKWRISDFSRYYLATGGGDISQAEVLLKRKFSDRLRSEIGRLDVKDIV
TDSRGRLTLDVRDALNSGSAGTEDEVATPAADDAIASAAERVEAETKGKVPVINPNSMAALGIEVVDVRI
KQINLPTEVSDAIYNRMRAEREAVARRHRSQGQEEAEKLRATADYEVTRTLAEAERQGRIMRGEGDAEAA
KLFADAFSQDPDFYAFIRSLRAYENSFSGNQDVMVLSPDSDFFRYMKTPTSATR
>gnl|CDD|236826 PRK11031, PRK11031, guanosine-5'-triphosphate,3'-diphosphate diphosphatase
MLSSSSLYAAIDLGSNSFHMLVVREVAGSIQTLARIKRKVRLAAGLDSDNALSNEAMERGWQCLRLFAER
LQDIPPSQIRVVATATLRLAVNADEFLAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIG
GASTELVTGTGAQATSLFSLSMGCVTWLERYFKDRNLTQENFDAAEKAAREVLRPVADELREHGWQVCVG
ASGTVQALQEIMMAQGMDERITLAKLQQLKQRAIQCGRLEELEIEGLTLERALVFPSGLAILIAIFEELN
IESMTLAGGALREGLVYGMLHLPVEQDIRSRTLRNIQRRFQIDTEQAQRVAKLADNFLQQVENEWHLEPR
SRELLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATLLLNQTNPVDLSSLHQQNALP
PRVAERLCRLLRLAIIFASRRRDDLLPEVTLQANDELLTLTLPQGWLAQHPLGAEELEQESQWQSYVHWP
LEVEEL
>gnl|CDD|182915 PRK11032, PRK11032, zinc ribbon-containing protein
MNKVAQYYRELVASLTERLRNGERDIDALVESARKRVDAAGELTRDEVDLITRAVRRDLEEFARSYEESK
EEFSDSVFMRVIKESLWQELADITDKTQLEWREVFQDLNHHGVYHSGEVVGLGNLVCEKCHHHLAFYTPE
VLPLCPKCGHDQFQRRPFEP
>gnl|CDD|236827 PRK11033, zntA, zinc/cadmium/mercury/lead-transporting ATPase; Provisional
SAMSTPDNHGKKAPQFSAFKPLTAVQNADDCCCDGACSSSPTLSEDTPLVSGTRYSWKVSGMDCPSCARK
VENAVRQLAGVNQVQVLFATEKLVVDADNDIRAQVESAVQKAGFSLRDEQAAAAAPESRLKSENLPLITL
AVMMAISWGLEQFNHPFGQLAFIATTLVGLYPIARKALRLIRSGSPFAIETLMSVAAIGALFIGATAEAA
MVLLLFLIGERLEGYAASRARRGVSALMALVPETATRLRDGEREEVAIADLRPGDVIEVAAGGRLPADGK
LLSPFASFDESALTGESIPVERATGEKVPAGATSVDRLVTLEVLSEPGASAIDRILHLIEEAEERRAPIE
RFIDRFSRIYTPAIMLVALLVILVPPLLFAAPWQEWIYRGLTLLLIGCPCALVISTPAAITSGLAAAARR
GALIKGGAALEQLGRVTTVAFDKTGTLTEGKPQVTDIHPATGISESELLALAAAVEQGSTHPLAQAIVRE
AQVRGLAIPEAESQRALAGSGIEGQVNGERVLICAPGKLPPLADAFAGQINELESAGKTVVLVLRNDDVL
GLIALQDTLRADARQAISELKALGIKGVMLTGDNPRAAAAIAGELGIDFRAGLLPEDKVKAVTELNQHAP
LAMVGDGINDAPAMKAASIGIAMGSGTDVALETADAALTHNRLRGLAQMIELSRATHANIRQNITIALGL
KAIFLVTTLLGITGLWLAVLADSGATALVTANALRLLRKRS
>gnl|CDD|236828 PRK11034, clpA, ATP-dependent Clp protease ATP-binding subunit; Provisional
MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLP
ASEEERDTQPTLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISH
GTRKDEPSQSSDPGSQPNSEEQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNP
LLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNS
ILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPS
IEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARLMPVSKRKKT
VNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGS
FLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAV
LLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAME
EIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMG
ARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEKNELTYGFQSAQKHKAEAAH
>gnl|CDD|182918 PRK11036, PRK11036, tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM
MQDRNFDDIAEKFSRNIYGTTKGQIRQAILWQDLDRLLAELPPRPLRVLDAGGGEGQTAIKLAELGHQVI
LCDLSAEMIQRAKQAAEAKGVSDNMQFIHCAAQDIAQHLETPVDLILFHAVLEWVADPKSVLQTLWSVLR
PGGALSLMFYNANGLLMHNMVAGNFDYVQAGMPKRKKRTLSPDYPLDPEQVYQWLEEAGWQIMGKTGVRV
FHDYLRNKHQQRDCFEALLELEQRYCRQEPYISLGRYIHVTARKP
>gnl|CDD|182919 PRK11037, PRK11037, hypothetical protein; Provisional
MMKETQPIDRETLLLEANKIIREHEDYLAGMRATDVEQKNGVLVFRGEYFLDEQGLPTAKTTAVFNMFKH
LAHVLSEKYHLVD
>gnl|CDD|182920 PRK11038, PRK11038, hypothetical protein; Provisional
MSLENAPDEVKLAVDLIYLLEENEIPPRTALAALEIVKRDYEKKLKS
>gnl|CDD|182921 PRK11039, PRK11039, DUF1249 family protein
MKRYTPDFPEMMRLCETNFAQLRRLLPRNDEVGETVSYQVANAQYRLTIVESTRYTTLVEIEQTAPAISY
WSLPSMTVRLYHDAMVAEVCSSQQIFRFKARYDYPNKKLHQRDEKHQINQFLADWLRYCLAHGAMAIPVC
>gnl|CDD|182922 PRK11040, PRK11040, peptidase PmbA; Provisional
MKVISQVAAQRKILEEAVSTALELASGKSDGAEVAVSKTTGISVSTRYGEVENVEFNSDGALGITVYHQQ
RKGSASSTDLSPQAIARTVQAALDIARYTSPDPCAGPADKELLAFDAPDLDLFHPAEVDPDEAIELAARA
EQAALQADKRITNTEGGSFNSHYGIKVFGNSHGMLQSYCSSRHSLSSCVIAEENGDMERDYAYTIGRAMD
DLQTPEWVGAECARRTLSRLSPRKLSTMKAPVIFAAEVATGLFGHLVGAISGGSVYRKSTFLLDSLGKQI
LPEWLTIEEHPHLLKGLASTPFDSEGVRTERRDIIKDGVLQTWLLTSYSARKLGLKSTGHAGGIHNWRIA
GQGLSFEQMLKEMGTGLVVTELMGQGVSAVTGDYSRGAAGFWVENGEIQYPVSEITIAGNLKDMWRNIVT
VGNDIETRSNIQCGSVLLPEMKIAGQ
>gnl|CDD|182923 PRK11041, PRK11041, DNA-binding transcriptional regulator CytR; Provisional
PEKVSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLI
GDCAHQNQQEKTFVNLIITKQIDGMLLLGSRLPFDASKEEQRNLPPMVMANEFAPELELPTVHIDNLTAA
FEAVNYLHELGHKRIACIAGPEEMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDL
PQPPTAVFCHSDVMALGALSQAKRMGLRVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLL
EQLQGHHVSSGSRLLDCELIIRGSTAAPP
>gnl|CDD|182924 PRK11043, PRK11043, Bcr/CflA family multidrug efflux MFS transporter
MQPSKGFLVYLAGLSMLGFLATDMYLPAFKAIQADLQTSASAVSASLSLFLAGFALGQLLWGPLSDRYGR
KPVLLAGLSLFALGSLGMLWVESAAQLLVLRFVQAVGVCSAAVIWQALVIDRYPAQKANRVFATIMPLVA
LSPALAPLLGAWLLNHFGWQAIFATLFAITLLLILPTLRLKPSKKARKQSQDALTFKQLLKSKTYLGNVL
IFAACSAAFFAWLTGSPFILEQMGYSPADIGLSYVPQTIAFLVGGYGCRAALQKWGGEQLLPWLLVLFAV
SVIAIWLASLLSHPSLVPLLIPFCVMAAANGAIYPIVVAQALRPFPQATGKAAALQNTLQLGLCFLASLL
VSALISTPLLTTGSVMLSTVVLVALGYMLQRKAEWGDFNHPFTEVAHSESH
>gnl|CDD|236829 PRK11045, pagP, lipid IV(A) palmitoyltransferase PagP
VKKYILILSLVFLLLLAVASACANAPSWWQTFCENVAQTWNEPEHYDLYIPAITWHNRFAYDKEKIDSYN
ERPWGGGFGKSRYDEKGNWHGLYAMAFKDSHNKWEPIAGYGWEKTWRPLADENFRLGLGFTAGVTARDDW
NYIPIPGLLPLASIGYGRLTFQMTYIPGTYNNGNVLFAWMRFQF
>gnl|CDD|236830 PRK11049, PRK11049, D-alanine/D-serine/glycine permease; Provisional
VDQVKVVADDQAPAEQSLRRNLTNRHIQLIAIGGAIGTGLFMGSGKTISLAGPSIIFVYMIIGFMLFFVM
RAMGELLLSNLEYKSFSDFASDLLGPWAGYFTGWTYWFCWVVTGIADVVAITAYAQFWFPDLSDWVASLA
VVLLLLSLNLATVKMFGEMEFWFAMIKIVAIVALIVVGLVMVAMHFQSPTGVEASFAHLWNDGGMFPKGL
SGFFAGFQIAVFAFVGIELVGTTAAETKDPEKSLPRAINSIPIRIIMFYVFALIVIMSVTPWSSVVPDKS
PFVELFVLVGLPAAASVINFVVLTSAASSANSGVFSTSRMLFGLAQEGVAPKAFAKLSKRAVPAKGLTFS
CICLLGGVVLLYVNPSVIGAFTLVTTVSAILFMFVWTIILCSYLVYRKQRPHLHEKSIYKMPLGKLMCWV
CMAFFAFVLVLLTLEDDTRQALIVTPLWFIALGLGYLFIGKKRAAELRK
>gnl|CDD|182927 PRK11050, PRK11050, manganese-binding transcriptional regulator MntR
RAGTPTAKKVTQLVDVEEHVEGFRQVREAHRRELIEDYVELIADLIAEVGEARQVDIAARLGVSQPTVAK
MLKRLARDGLVEMRPYRGVFLTPEGEKLAQESRERHQIVENFLLALGVSPETARRDAEGIEHHVSEETLA
AFRRFLQRHGAK
>gnl|CDD|236831 PRK11052, malQ, 4-alpha-glucanotransferase; Provisional
MESKRLDQAALAAGIAPSYINAHGKPQAISAETKRRLLAAMGYRTATKSAVTPLPPVKVFTQGKPMQLPL
EGSGEYSWQLTTEEGEQLQGRVTGGKALTLPADLPLGYHTLTLTQDDQRWHCRIIVAPKRCYEPQALLQG
KKLWGACVQLYTLRSEHNWGIGDFGDLKQMLEDVAKRGGDFIGLNPIHALYPANPESASPYSPSSRRWLN
VIYIDVNAVEDFQQSEEAQAWWQSAETQQRLQQARAAEWVDYSTVTALKLTALRLAFKQFAQRDKDDEQM
QAFRQFVAEGGESLLWQAAFDALHAHLVKEDEMRWGWPVWPEEYQDVDSPAVQQFCEEHADEVDFYLWLQ
WLADSQFAACWQLSQQLGMPIGLYRDLAVGVAEGGAETWCDRELYCLKASVGAPPDILGPLGQNWGLPPM
DPHVLQARAYQPFIDLLRANMQHCGALRIDHVMSLLRLWWIPYGETADQGAYVHYPVDDLLAILALESQR
HRCMVIGEDLGTVPVEIVGKLRDSGVYSYKVLYFENDEEGGFRAPAAYPEQSMATLTTHDLPTLRGYWQC
DDLTLGKELGLYPDEEVLRGLYQDRERAKQGLLDALHKHGCLPKRAGHKASLMSMTPTLNRGLQRYVADS
NSALLGLQPEDWLDMAKPVNIPGTSDEYPNWRRKLSATLEEIFADEGVNRLLKDLDKRRKAAAKK
>gnl|CDD|182929 PRK11053, PRK11053, oxygen-insensitive NAD(P)H nitroreductase
MDIVSVAKKRYTTKAFDPSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIAKAAAGNYAF
NERKILDASHVVVFCAKTDMDDAYLELVLEQEDADGRFATEEAKAAQDKGRRFFADMHRKELKDLQHWME
KQVYLALGNLLLGAAALGIDATPIEGFDAAILDAEFGLREKGLTSSVVVPLGYHSEEDFNAKLPKSRLPQ
ETIFTEI
>gnl|CDD|182930 PRK11054, helD, DNA helicase IV; Provisional
MELKATSLGKRLAQHPYNRVELLNAGVKVSGDKHEYLIPFNQLLAIHCKRGLVWGELEFVLPDQKVVRLH
GTEWQETQRFYHHLLAHWQQWSEEMSEILAQVLPQQLDLIARLTQQDKWLTRSQVSGLQQQIRQALSALP
LPVERLEAFDNCREAWRKCLAWLQDGEAARLQHNQAWTEAMLEEYADFFSQVESSPLNPSQARAVVNGED
SLLVLAGAGSGKTSVLVARAGWLLARGQAQPEQILLLAFGRQAAEEMDERIRERLGTEDITARTFHALAL
HIIQQGSKKVPVISKLENDSKARHALLIAEWRKQCSEKKAQAKGWRQWLTEELQWDVPEGNFWDDEKLQR
RLASRLERWVSLMRMHGGSQAEMIAQAPEEVRDLFQKRLKLMAPLLKAWKKALKAENAVDFSGLIHQAVN
YLEKGRFISPWKHILVDEFQDISPQRAALLAALRKQNSQTTLFAVGDDWQAIYRFSGADLSLTTAFHERF
GEGDRCHLDTTYRFNSRIGEVANRFIQQNPHQLKKPLNSLTKGDKKAVTLLPEDQLEALLDKLSGYAKPD
ERILLLARYHHLRPALLDKAATRWPKLQIDFMTIHASKGQQADYVIILGLQEGQDGFPAPARESIMEEAL
LPPPEDFPDAEERRLLYVALTRAKHRVWLLFNKGNPSPFVEELKNLDVPVARKP
>gnl|CDD|182931 PRK11055, galM, galactose-1-epimerase; Provisional
ALAPDGQPYRLLTLRNNAGMVVTLMDWGATWLSCRVPLSDGSVREVLLGCASPEDYPDQAAYLGASVGRY
ANRIANSRFTLDGETYQLSPNQGGNQLHGGPEGFDKRRWQIVNQNDRQVTFSLSSPDGDQGFPGNLGATV
TYRLTDDNRVSITYRATVDKPCPVNLTNHAYFNLDGAEEGSDVRNHKLQINADEYLPVDEGGIPNGGLKS
VAGTSFDFRQPKTIAQDFLADDDQQKVKGYDHAFLLQAKGDGKKPAAHLWSPDEKLQMKVYTTAPALQFY
SGNFLAGTPSRGGGPYADYAGLALESQFLPDSPNHPEWPQPDCILKPGEEYRSLTEYQFIAE
>gnl|CDD|236832 PRK11056, PRK11056, YijD family membrane protein
MMEQSRQEKGTLLLALIAGLSINGTFAALFSSIVPFSIFPLIALVLAVYCLHQRYLNRPMPEGLPGLAAA
CFFLGVFLYSAFVRAEYPEIGSNFFPAVLSVILVFWIGRKLRNRKKKVAE
>gnl|CDD|182933 PRK11057, PRK11057, ATP-dependent DNA helicase RecQ; Provisional
MAQAEVLNLESLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLV
VSPLISLMKDQVDQLLANGVAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNP
ALLAVDEAHCISQWGHDFRPEYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDR
PNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQE
AFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRR
CLEEKPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPPKQYDGLEDAQKAL
SCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQHS
ALQLTEAARPVLRGEVSLQLAVPRIVALKPRAMQKSFGGNYDRKLFAKLRKLRKSIADEENIPPYVVFND
ATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAHVDGDD
>gnl|CDD|182934 PRK11058, PRK11058, GTPase HflX; Provisional
MFDRYEAGEQAVLVHIYFSQDKDMEDLQEFESLVSSAGVEALQVITGSRKAPHPKYFVGEGKAVEIAEAV
KATGASVVLFDHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGW
THLERQKGGIGLRGPGETQLETDRRLLRNRIVQILSRLERVEKQREQGRRARIKADVPTVSLVGYTNAGK
STLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLL
LHVVDAADVRVQENIEAVNTVLEEIDAHEIPTLLVMNKIDMLDDFEPRIDRDEENKPIRVWLSAQTGAGI
PLLFQALTERLSGEVAQHTLRLPPQEGRLRSRFYQLQAIEKEWMEEDGSVSLQVRMPIVDWRRLCKQEPA
LIDYIV
>gnl|CDD|236833 PRK11059, PRK11059, regulatory protein CsrD; Provisional
MKPTMRLTTKLSAFVTLLVALAMFVTLLGCTLSFYQLTQEKQQHRVQALATAIDQHLLTQDAASLQRWLP
ELLQAANIVEVDLSQGDKPVYSFQRPASYRPQGSSSLYRELSLPLLKHPGMSLRLKYVDPFGNYFYSLYA
TASLTLAIGFIVLMLFLGVRWLRRQLAGQELLEERARRILNGEREQAVAGSGYEWPRTASRALDHLLSEL
QDAREERSRFDTFIRSNAFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGES
QVEELLFELINLLSTFVMRYPGALLARYSRSDFAVLLPHRSLKEADSLASQLLKAVDALPPPKMLDRDDF
LHIGICAYRSGQSTEQVMEEAEMALRSAQLQGGNGWFVYDKAQLPEKGRGSVRWRTLLEQTLVRGGPRLY
QQPAVTRDGKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEENLSINL
SVDSLLSRAFQRWLRDTLLQCPRSQRKRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVS
TSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQG
DFFAESQPLD
>gnl|CDD|182936 PRK11060, PRK11060, rod shape-determining protein MreD; Provisional
MASYRSRGRWVIWLSFLIALVLQIMPWPDQLIVFRPSWLLLILIYWVLALPHRVNVGTGFVLGLIWDLIL
GSTLGVRALAMSIIAYLVALKFQLFRNLALWQQALVVMLLSLLMDIIVFWAEFLVINVSFRPEVFWSSVV
NGILWPWLFLLMRKVRRQFAVQ
>gnl|CDD|182937 PRK11061, PRK11061, phosphoenolpyruvate--protein phosphotransferase
MLTRLREIVEKVASAPRLNEALDILVTETCLAMDTEVCSVYLADHDRRCYYLMATRGLKKPRGRTVTLAF
DEGIVGLVGRLAEPINLADAQKHPSFKYIPSVKEERFRAFLGVPIIYRRQLLGVLVVQQRELRQFDESEE
SFLVTLATQLAAILSQSQLTALFGQYRQTRIRALPASPGVAIAEGWQDATQPLLEQVYPASTLDPALERE
RLTGALEEAANEFRRYSKRFAAGAQKETAAIFDLYSHLLNDPRLRRELFAEVDKGSVAEWAVKQVIEKFA
EQFAALSDNYLRERAGDLRALGQRLLFHLDDSEQGPNAWPERFILVADELTATLLAELPQDRLAGVVVRD
GAANSHAAILVRALGIPTVMGADIQPSLLHQRLLIVDGYRGELLVDPEPVLLQEYQRLISEEIELSRLAE
DDVNLPAQLKSGERIKVMLNAGLSAEHEEKLGSRVDGVGLYRTEIPFMLQSGFPSEEEQVAQYQGMLQMF
PDKPVTLRTLDIGADKQLPYMPISEENPCLGWRGIRITLDQPEIFLIQVRAMLRANAATGNLSILLPMVT
SIDEVDEARRLIDRAGREVEEMLGYEIPKPRIGIMIEVPSMVFMLPHLASRVDFISVGTNDLTQYLLAVD
RNNTRVASLYDSLHPAMLRALKMIADEAEQHGLPVSLCGEMAGDPMGALLLIGLGYRHLSMNGRSVARVK
YLLRHIDLAEAENLAQRSLEAQLATEVRHQVAAFMERRGLGGLIRGGK
>gnl|CDD|182938 PRK11062, nhaR, transcriptional activator NhaR; Provisional
MSHINYNHLYYFWMVCKEGSVVGAAEALFLTPQTITGQIKALEERLQGKLFKRKGRGLEPTELGELVFRY
ADKMFTLSQEMLDIVNYRKESNLLFDVGVADALSKRLVSRVLLTAVPEDESIHLRCFESTHEMLLEQLSQ
HKLDMILSDCPVDSTQQEGLFSKKLGECGVSFFCTNPLPEKPFPACLEERRLLIPGRRTMLGRKLLNWFN
SQGLNVEILGEFDDAALMKAFGAYHDAIFVAPSLYAQDFYADHSVVEIGRVDNVKEEYHVIFAERMIQHP
AVQRICNTDFSALFSG
>gnl|CDD|182939 PRK11063, metQ, D-methionine ABC transporter substrate-binding protein MetQ
MAFKFKTFAAVGALIGTLALVGCGQDEKDPNHIKVGVIVGAEQQVAEVAQKVAKEKYGLDVELVTFNDYV
LPNEALSKGDIDANAFQHKPYLDQQIKDRGYKLVAVGNTFVYPIAGYSKKIKSLDELQDGSQVAVPNDPT
NLGRSLLLLQKVGLIKLKDGVGLLPTVLDIVENPKNLKIVELEAPQLPRSLDDAQIALAVINTTYASQIG
LTPAKDGIFVEDKDSPYVNLIVAREDNKDAENVKKFVQAYQSDEVYEAANKVFNGGAVKGW
>gnl|CDD|182940 PRK11064, wecC, UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
MSFETISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRAT
TTPEPADAFLIAVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDL
TFPQQAGEQADINIAYCPERVLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEM
CKLTENSFRDVNIAFANELSLICADQGINVWELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQ
QARLIRTAREVNDGKPHWVIDQVKAAVADCLAATDKRASEVKIACFGLAFKPNIDDLRESPAMEIAELIA
QWHSGETLVVEPNIHQLPKKLDGLVTLVSLDEALATADVLVMLVDHSQFKAINGDNVHQQWVVDT
>gnl|CDD|236834 PRK11067, PRK11067, outer membrane protein assembly factor YaeT; Provisional
MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRVGDTVNDEDISNTIRALFATG
NFEDVRVLRDGNTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGEALDRTTLSNIEKGLEDF
YYSVGKYSASVKAVVTPLPRNRVDLKLVFTEGVSAKIQQINIVGNHAFSTDELISRFQLRDEVPWWNVVG
DRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKLSGVQVSGNLAGH
SAEIEKLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQTQPEINDADKTVKLHVNVDAGNRFYVR
KIRFEGNDTSKDAVLRREMRQMEGAWLGSDLVEQGKERLNRLGFFETVDVDTQRVPGSPDQVDVVYKVKE
RNTGSFNFGVGYGTESGVSFQAGVQQDNWLGTGNSVGINGTKNDYQTYAELSVTDPYFTVDGVSLGGRIF
YNDFEADDADLSDYTNKSYGTDVTLGFPINENNSLRAGLGYVHNSLSNMQPQVAMWRYLYSMGENPSSDS
DNSFKTDDFTFNYGWTYNNLDRGYFPTAGNRVNLTGKVTIPGSDNEYYKVTLDTAQYVPLDDDHKWVLLG
RGRLGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYYPGQASNYTQDGAKDLCKSDDAVGGNA
MAVASLELITPTPFISDKYANSVRTSFFWDMGTVWDTNWDNTAYTRAAGYPDYSDPSNIRMSAGIALQWM
SPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW
>gnl|CDD|182942 PRK11068, PRK11068, phosphatidylglycerophosphatase A; Provisional
MDVAKSRLKLSNPWHLLATGFGSGLSPIVPGTMGSLAAIPFWYLLTFLPWQLYSLVVMLGICIGVYLCHQ
TAKDMGVHDHGSIVWDEFIGMWITLMALPVNDWQWVAAGFVIFRILDMWKPWPIRWFDRNVHGGMGIMID
DIVAGVISAGILYFIGHHWPLGIL
>gnl|CDD|236835 PRK11069, recC, exodeoxyribonuclease V subunit gamma
MFTVYHSNQLDVLKALMVFLIEREPLDDPFEPEMILVQSPGMAQWLQMELAQKFGIAANIDFPLPATFIW
DMFTRVLPDIPKESAFNKEAMTWKLMTLLPQLLERPEFTPLRHYLTDDEDKRKLFQLAARIADLFDQYLV
YRPEWLASWEAGQLVEGLGDAQPWQAPLWKALVEYTHQLGQPRWHRANLYQRFIETLESATTCPPGLPKR
VFICGISALPPVYLQALQALGKHIDIHLLFTNPCRYYWGDIQDPAFLAKLLARQRRHSFEDRELPLFRDS
ENAEQLFNSDGEQDVGNPLLASWGKLGRDNLYLLSQLESSQELDAFVDIEPDNLLHNIQADILELEDHAV
IGVNDEEFSRSDHKRPLDPDDRSLSFHVCHSPQREVEVLHDRLLAMLEADPTLTPRDIIVMVADIDSYSP
FIQAVFGNAPAERYLPFAISDRRARQAHPVLQAFISLLSLPDSRFTAEDVLALLEVPALAARFAITEEGL
RYLRQWVEESGIRWGLDDDNVRELELPATGQHTWRFGLTRMLLGYAMESAAGEWQGVLPYDESSGLIAEL
AGHLASLLMQLNIWRRGLAQPRPLEEWLPVCRQLLDDFFLPDAETEAALALIEQQWQAIIEEGLDAQYGD
AVPLSLLRDELAQRLDQERISQRFLAGPVNFCTLMPMRSIPFKVVCLLGMNDGVYPRTLPPLGFDLMSQK
PKRGDRSRRDDDRYLFLEALLSAQQQLYISYIGRSIQDNSERFPSVLVSELLEYIGQSYCLPGDEALNCD
ESAARVKAHLTCLHTRMPFDPQNFQPGEQQSYAREWLPAASQQGKAHPDFVQPLPFEPPEELTLDELQRF
WRHPVRAFFQRRLKVNFRTEESELPDEEPFTLDGLSRYQLNQQLLNALIEQDDAERLFRRQRAAGKLPYG
AFGEIFWETQCQEMQQLADRVRACRQPGQSLEIDLTLNGVQLTGWLPQVQPDGLLRWRPGLLSVADGLQL
WLEHLVYCASGGNGESRLFGRKEGEWRFPPLAAEQAKQYLSQLIEGYREGMSAPLLLLPKSGGAWLKACY
DRENDAILDDEETQQKARKKLLQAWEGNMMVRGEGDDIYIQRLWRQLDDETLEAIIEQAQRYLLPLFRFN
QS
>gnl|CDD|182944 PRK11070, PRK11070, single-stranded-DNA-specific exonuclease RecJ
QQIQLRRREADETADLPADLPPLLRRLYASRGVRSAQELERSVKGLLPWQQLSGIEKAVELLYNALREGT
RIIVVGDFDADGATSTALSVLALRSLGCSNVDYLVPNRFEDGYGLSPEVVDQAHARGAQLIVTVDNGISS
HAGVAHAHALGIPVLVTDHHLPGETLPAADAIINPNLRDCNFPSKSLAGVGVAFYLMLALRAFLRDQGWF
DERGIAIPNLAELLDLVALGTVADVVPLDANNRILVWQGLSRIRAGKCRPGIKALLEVANRDAQKLAASD
LGFALGPRLNAAGRLDDMSVGVALLLCDNIGEARVLANELDALNQTRKEIEQGMQVEALTLCEKLERSSD
TLPYGLAMYHPEWHQGVVGILASRIKERFHRPVIAFAPAGDGTLKGSGRSIQGLHMRDALERLDTLYPGL
ILKFGGHAMAAGLSLEEDKFELFQQRFGELVTEWLDPSLLQGVVWSDGELSPAEMSLEVAELLRDAGPWG
QMFPEPLFDGRFRLLQQRLVGERHLKVMVEPVGGGPLLDGIAFNVDTTLWPDNSVREVELAYKLDINEFR
GNRSLQLIIDHIWPI
>gnl|CDD|182945 PRK11071, PRK11071, esterase YqiA; Provisional
MSTLLYLHGFNSSPRSAKATLLKNWLAQHHPDIEMIVPQLPPYPADAAELLESLVLEHGGDPLGLVGSSL
GGYYATWLSQCFMLPAVVVNPAVRPFELLTDYLGENENPYTGQQYVLESRHIYDLKVMQIDPLESPDLIW
LLQQTGDEVLDYRQAVAYYAACRQTVEEGGNHAFVGFERYFNQIVDFLGL
>gnl|CDD|236836 PRK11072, PRK11072, bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase
MLPLSSPLQQYWQTLVERLPEPLAPESLSAQLKSVLALSDFVARQLQAHPELLEELAAQLPQPLERQAYA
AWLQELLAAVADEDALMRALRQFRRRVMVRIAWRDLLGLADLEEVLGQLSDLAEALIIAARDWLYAALCA
EYGTPCGAQGEPQPLLILGMGKLGGRELNFSSDIDLIFTYPEHGETQGGRRSIDNQQFFTRLGQRLIKAL
DQVTADGFVFRVDMRLRPFGDSGPLVLSFAALEDYYQEQGRDWERYAMIKARVMGDPDDAYAQELRAMLR
PFVFRRYLDFSAIQALRNMKGMIRREVRRRGLADNIKLGAGGIREIEFIVQVFQLIRGGREPSLQQRSLL
EVLDALAELGLLPEEQVAELRDAYLFLRRLEHLLQAINDQQTQTLPDDPLDRARLAWAMGFADWAALLDV
LDAHRANVRRVFNQLIGDDEEETEEEAASEQWRELWQDALDEEDATPLLAELGFDDPAQVLARLAAFRHS
LRKRTLGPRGRERLDALMPRLLEAACAREDADVTLERLLDLLEAISRRTTYLELLSENPGALKRLISLCA
ASPWIAEQLARYPLLLDELLDPRALYQPTDWDAYRDELRQYLLRVPEDDEEQQMEALRQFKQAQVLRIAA
ADIAGVLPVMKVSDHLTYLAEAILDAVVQQAWQQMVKRHGEPPHLEGRERGFAVIGYGKLGGKELGYASD
LDLVFLHDCPEDAMTDGDKSIDGRQFYLRLAQRIIHLFSTRTSSGILYEVDMRLRPSGAAGLLVSSLEAF
ERYQLNEAWTWEHQALVRARFVAGDPQLGAAFEAIRREVLTQPRDLATLRTEVREMREKMRDHLGNKTRD
RFDLKQDRGGIVDIEFIAQYLVLAHAHEHPELTRWSDNVRILELLAELGLMSEEEAEALTDAYRTLRDEQ
HRLALQEQPGRVPADEFAAERAAVRALWQRVLG
>gnl|CDD|182947 PRK11073, glnL, nitrogen regulation protein NR(II)
MATGTLPDAGQILNSLINSILLLDDDLAIHYANPAAQQLLAQSSRKLFGTPLPELLSYFSLNIELMRESL
QAGQGFTDNEVTLVIDGRSHILSLTAQRLPEGMILLEMAPMDNQRRLSQEQLQHAQQVAARDLVRGLAHE
IKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQADRLRNLVDRLLGPQRPGTHVTESIHKVAERVVQLV
SLELPDNVRLIRDYDPSLPELAHDPDQIEQVLLNIVRNALQALGPEGGTITLRTRTAFQLTLHGERYRLA
ARIDIEDNGPGIPPHLQDTLFYPMVSGREGGTGLGLSIARNLIDQHSGKIEFTSWPGHTEFSVYLPIR
>gnl|CDD|182948 PRK11074, PRK11074, putative DNA-binding transcriptional regulator; Provisional
MWSEYSLEVVDAVARTGSFSAAAQELHRVPSAVSYTVRQLEEWLAVPLFERRHRDVELTPAGEWFVKEAR
SVIKKMQETRRQCQQVANGWRGQLSIAVDNIVRPDRTRQLIVDFYRHFDDVELIIRQEVFNGVWDALADG
RVDIAIGATRAIPVGGRFAFRDMGMLSWACVVSSDHPLASMDGPLSDDELRPYPSLCLEDTSRTLPKRIT
WLLDNQRRLVVPDWESAINCLSAGLCVGMVPTHFAKPLINSGKLVELTLENPFPDSPCCLTWQQNDMSPA
LAWLLDYLGDSETLNKEWLR
>gnl|CDD|236837 PRK11081, PRK11081, tRNA guanosine-2'-O-methyltransferase; Provisional
MNPERYARICEMLARRQPDLTVCMEQVHKPHNVSAIIRTADAVGVHEVHAVWPGSRMRTMGSTAAGSNSW
VQVKTHRTIGDAVAHLKGQGMQILATHLSDTAVDFREIDYTRPTCILMGQEKTGISQEALALADQDIIIP
MIGMVQSLNVSVASALILYEAQRQRQNAGMYLRENSMLPEEEQQRLLFEGGYPVLAKVAKRKGLPYPHID
EQGQIVADADWWATMQAAG
>gnl|CDD|236838 PRK11083, PRK11083, DNA-binding response regulator CreB; Provisional
MQQPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLL
AFHPALPVIFLTARSDEVDRLVGLEIGADDYVAKPFSPREVAARVRTILRRVKKFAAPSPVIRIGHFELD
EPAARISYFGTPLTLTRYEFLLLKTLLLSPGRVFSRQQLMDIVWEDAQDSYDRTVDTHIKTLRAKLRAIN
PDLSPINTHRGMGYSLRP
>gnl|CDD|182951 PRK11085, PRK11085, magnesium/cobalt transporter CorA
MLSAFQLENNRLTRLEVEESQPLVDAVWIDLVEPDDDERLRVQSELGQSLATRPELEDIEASARFFEDED
GLHIHSFFFFEDAEDHAGNSTVAFTIRDGRLFTLRERELPAFRLYRMRARSQTLVDGNAYELLLDLFETK
IEQLADEIENIYSDLEKLSRVIMEGHQGDEYDEALSTLAELEDIGWKVRLCLMDTQRALNFLVRKARLPG
GQLEQAREILRDIESLLPHNESLFQKVNFLMQAAMGFINIEQNRIIKIFSVVSVVFLPPTLVASSYGMNF
EFMPELKWSFGYPGAIILMILAGLAPYLYFKRKNWL
>gnl|CDD|236839 PRK11086, PRK11086, sensory histidine kinase DcuS; Provisional
RHSLPYMKKRKRPMKLSTTVTLMVSAVVFSVLLVVHLLYFSQISRMTRDGLAEKALAIARTVADSPIVIQ
GLQGKPDESGIQTYAEAVRKRNDLLFIVVTDMQGIRYSHPNPQKIGKHFIGGDELPALKGKENVSINRGT
LGQALRVFTPVYDENGKQIGVVAVGISLSEVTEQINESRWSIYWSILFGALVGLIGTVILVRVLKRILFG
LEPYEISTLFEQRQAMLQSIKEGVIAVDDRGEVTLINDEAKRLFNYKKGLEDDPLGTDVESWMPVSRLKE
VLRTGTPRRDEEININGRLLLTNTVPVRVNGEIIGAIATFRDKTEVRQLAQRLDGMVNYADALRAQSHEF
MNKLHVILGLLHLKSYDQLEDYILKTANNYQEEIGSLLGKIKSPVIAGFLLGKISRARELGITLIISEDS
QLPDSGDEDQVHELITILGNLIENALEAVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFDK
GYSTKGSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIPWDGERSNR
>gnl|CDD|236840 PRK11087, PRK11087, oxidative stress defense protein; Provisional
LAALLGLSSMALPAQAAELPDFPHIVTSGTASVDAVPDMATLAVEVNVSAKDAATAKKQVDERVAQYLAF
LEKNGIAKKDISSANLRTQPQYDYQKDGKSELKGYRASRQVTVTVRQLDKLNSLLDGALKAGLNEIRSIE
LGVSKPDEYKDKARKAAIKDAIQQAQSLAKGFGEKLGPVYSIRYHVSNYQPPPMVRMKAADAAPVMSAAE
TYQQQTIQFDDQVDVVFELKP
>gnl|CDD|236841 PRK11088, rrmA, 23S rRNA methyltransferase A; Provisional
MSYQCPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKRSKDPGDNKEMMQARRAFLDAGHYQPL
RDAVANLLAERLDEKATALLDIGCGEGYYTHALADALPEITTMQLFGLDISKVAIKYAAKRYPQVTFCVA
SSHRLPFADQSLDAIIRIYAPCKAEELARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEAEQLEG
FELQHSERLAYPMRLTGSEAVALLQMTPFAWKATPEVKQQLAAKGVFSCETDFNIRVYRRSY
>gnl|CDD|182955 PRK11089, PRK11089, PTS system glucose-specific transporter subunits IIBC; Provisional
MFKNAFANLQKVGKSLMLPVSVLPIAGILLGVGSANFSWLPAVVSHVMAEAGGSVFANMPLIFAIGVALG
FTNNDGVSALAAVVAYGIMVKTMAVVAPLVLHLPAEEIAAKHLADTGVLGGIIAGAIAAYMFNRFYRIKL
PEYLGFFAGKRFVPIISGLAAIFTGVVLSFIWPPIGSAIQTFSQWAAYQNPVVAFGIYGFVERSLVPFGL
HHIWNVPFQMQIGEYTNAAGQVFHGDIPRYMAGDPTAGKLSGGFLFKMYGLPAAAIAIWHSAKPENRAKV
GGIMISAALTSFLTGITEPIEFSFMFVAPILYIIHAILAGLAFPICILLGMRDGTSFSHGLIDFIVLSGN
SSKLWLFPIVGIGYAIVYYTIFRVLIKALDLKTPGREDETEDAKATGTSEMAPALVAAFGGKENITNLDA
CITRLRVSVADVSKVDQAGLKKLGAAGVVVAGSGVQAIFGTKSDNLKTEMDEYIRNH
>gnl|CDD|236842 PRK11091, PRK11091, aerobic respiration control sensor protein ArcB; Provisional
MKQIRLLAQYYVDLMVKLGLVRFSLLLALALVVLAMVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAV
YFLSVVVEQLEESRQRLSRLVAKLEEMRERDLELNVQLKDNIAQLNQEIAEREKAEEARQEAFEQLKNEI
KEREETQIELEQQSSLLRSFLDASPDLVYYRNEDGEFSGCNRAMELLTGKSEKQLIGLTPKDVYSPEAAE
KVIETDEKVFRHNVSLTYEQWLDYPDGRKACFELRKVPFYDRVGKRHGLMGFGRDITERKRYQDALEKAS
RDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQ
LDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVT
VRVRYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSKRLAQAMGGDITVT
SEEGKGSCFTLTIHAPAVAEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKE
ALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPL
SVPALTAMIKKFWDTQDDEESTVTTEESSKANEALLDIPMLEQYVELVGPKLITDSLAVFEKMMPGYLSV
LDSNLTARDQKGIVEEAHKIKGAAGSVGLRHLQQLAQQIQSPDLPAWWDNVQDWVEELKNEWRHDVEVLK
AWLAQAEKK
>gnl|CDD|236843 PRK11092, PRK11092, bifunctional GTP diphosphokinase/guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase
MYLFESLNQLIQTYLPEDQIKRLRQAYLVARDAHEGQTRSSGEPYITHPVAVACILAEMRLDYETLMAAL
LHDVIEDTPATYQDMEQLFGKSVAELVEGVSKLDKLKFRDKKEAQAENFRKMIMAMVQDIRVILIKLADR
THNMRTLGSLRPDKRRRIARETLEIYSPLAHRLGIHHIKTELEELGFEALYPNRYRVIKEVVKAARGNRK
EMIQKILSEIEGRLQEAGIPCRVSGREKHLYSIYCKMVLKEQRFHSIMDIYAFRVIVDDSDTCYRVLGQM
HSLYKPRPGRVKDYIAIPKANGYQSLHTSMIGPHGVPVEVQIRTEDMDQMAEMGVAAHWAYKEHGETGTT
AQIRAQRWMQSLLELQQSAGSSFEFIESVKSDLFPDEIYVFTPEGRIVELPAGATPVDFAYAVHTDIGHA
CVGARVDRQPYPLSQPLTSGQTVEIITAPGARPNAAWLNFVVSSKARAKIRQLLKNLKRDDSVSLGRRLL
NHALGGSRKLDEIPQENIQRELDRMKLATLDDLLAEIGLGNAMSVVVAKNLLGDDAELPTATSSHGKLPI
KGADGVLITFAKCCRPIPGDPIIAHVSPGKGLVIHHESCRNIRGYQKEPEKFMAVEWDKETEQEFIAEIK
VEMFNHQGALANLTAAINTTGSNIQSLNTEEKDGRVYSAFIRLTARDRVHLANIMRKIRVMPDVIKVTRN
RN
>gnl|CDD|182958 PRK11096, ansB, L-asparaginase II; Provisional
EFFKKTALAALVMGFSGAAFALPNITILATGGTIAGGGDSATKSNYTAGKVGVENLVNAVPQLKDIANVK
GEQVVNIGSQDMNDEVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVLVGAMRPST
AMSADGPLNLYNAVVTAADKASANRGVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPLGYIHNGKVDY
QRTPARKHTTDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKTVFDTLAT
AAKNGVAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQMFNQY
>gnl|CDD|236844 PRK11097, PRK11097, cellulase
MRVLRAGVVALLLLAALAAAAACSWPAWEQFKKDYISADGRVIDPSDARKITTSEGQSYGLFFALVANDR
AAFDKLLNWTENNLAQGDLTARLPAWLWGKKADGTWGVLDANSASDADLWIAYSLLEAGRLWKEPRYTAL
GTALLKRIAREEVVTVPGLGSMLLPGPVGFADDGSWRLNPSYLPPQLLRRFARFLPGGPWAALAATNARL
LLETAPKGFSPDWVRYQKGKGFQPDPEKGDIGSYDAIRVYLWAGMLADGDPQKARLLARFKPMAALTAKN
GAPPEKVDVATGKAQGNGPVGFSAALLPFLQALGEPANADAQAAQRQRVADNAPGSDAYYDYVLTLFGQG
WDQGRYRFDADGELLPSWGQECASSR
>gnl|CDD|182960 PRK11098, PRK11098, peptide antibiotic transporter SbmA
MFKSFFPKPKLFFLSAFVWALIAVIFWYAGGGDWLARLTGLAAASGQLPIGAARFWSPDFLWFYAYYLVC
VGLFAGFWFIYSPHPWQRWSILGSALIIFVTWFLVQVSVAVNAWYAPFYDLIQTALSSPGKVTIGQFYSE
VGVFLGIALIAVVISVLNNFFVSHYVFRWRTAMNEYYMAHWQKLRHIEGAAQRVQEDTMRFASTLENLGV
SFINAIMTLIAFLPVLVTLSAHVPELPIVGHIPYGLVIAAIVWSLFGTGLLAVVGIKLPGLEFKNQRVEA
AYRKELVYGEDDADRATPPTVRELFSNVRKNYFRLYFHYMYFNIARILYLQVDNVFGLFLLFPSIVAGTI
TLGLMTQITNVFGQVRGSFQYLINSWTTIVELLSIYKRLRSFEAALDGEPLQEVDHTLL
>gnl|CDD|236845 PRK11099, PRK11099, putative inner membrane protein; Provisional
SFKQKYLVKFWAPIPAVIAAGILSAYYFGITGTFWAVTGEFTRWGGHLLQLFGVHVEEWGYFKIIGLEGT
PLTRIDGMMIIGMFLGCLIAALWANNVKLRMPASRIRILQALIGGIIAGFGARLAMGCNLAAFFTGIPQF
SLHAWFFALATAIGSYFGAKFTLLPFFRIPVKLQKVSAASPLTQKPNRARRRFRLGMLVFAGMLGWALLT
AFNQPKLGLAMLFGVGFGLLIERAQICFTSAFRDLWITGRTHMAKAIILGMAVSAIGIFSYIQLGVPPKI
FWAGPNAVIGGLLFGFGIVLAGGCETGWMYRAVEGQVHFWIVGLGNVIGATLLAYYWDDFAPALATPWPK
INLLETFGPLGGLLITYLLLFLALLLVIGWEKRFFRRAKLTIRTAKELV
>gnl|CDD|236846 PRK11100, PRK11100, sensory histidine kinase CreC; Provisional
MRIGLRLFLGYFLIVALAAYFVLRIFVQEVKPGVRQATEETLVDTANLLAELARDDLLSGRLADGRLAQA
FAQLQQRPFRANIWGIRKTRVDYRVYVTDAQGIVLFDSEGRAVGQDYSRWNDVYLTLRGEYGARSTREDP
ADPESSVMYVAAPIRDGGRIIGVLSVGKPNSSMAPFIKRSERRILWAGALLLGIALLIGAGVVWWLNRSI
RRLTRYADAVTEGKPVPLPKLGSSELRELAQALESMRVKLEGKAYVEQYVQTLTHELKSPLAAIRGAAEL
LQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEAREAQAAAKG
ITLRLRPDDARVLGDPFLLRQALGNLLDNAIDFSPEGGTITLSAEVDGEQVALSVEDQGPGIPDYALPRI
FERFYSLPRPANGRKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPRHF
>gnl|CDD|236847 PRK11101, glpA, anaerobic glycerol-3-phosphate dehydrogenase subunit A
TRDSQETDVIIIGGGATGAGIARDCALRGLRCILVERHDIATGATGRNHGLLHSGARYAVTDAESARECI
SENQILKRIARHCVEPTDGLFITLPEDDLAFQATFIRACEEAGIEAEAIDPQQALILEPAVNPALIGAVK
VPDGTVDPFRLTAANMLDAKEHGAQILTYHEVTGLIREGDTVCGVRVRDHLTGETQEIHAPVVVNAAGIW
GQHIAEYADLRIRMFPAKGSLLIMDHRINNHVINRCRKPADADILVPGDTISLIGTTSTRIDYDQIDDNR
VTAEEVDILLREGEKLAPVMAKTRILRAYAGVRPLVASDDDPSGRNVSRGIVLLDHAERDGLDGFITITG
GKLMTYRLMAEWATDAVCRKLGNTRPCTTADTPLPGSQEPAEVTLRKVISLPAPLRGSAVYRHGDRAPAW
LSEGRLDRSLVCECEAVTAGEVRYAVENLNVNNLLDLRRRTRVGMGTCQGELCACRAAGLLQRFNVTTPA
QSIEQLSTFLNERWKGVQPIAWGDALRESEFTRWVYQGLCGLEPLQAQQKEQKDEL
>gnl|CDD|182964 PRK11102, PRK11102, Bcr/CflA family multidrug efflux MFS transporter
MLMPLAIDMYLPALPVIAADFGVSAGSVQMTLSAYILGFAIGQLFYGPMADSFGRKPVILGGTLVFALAA
VACALAQTIDQLIYMRFLHGLAAAAASVVINALMRDMFPKEEFSRMMSFVTLVMTIAPLLAPIIGGWLLV
WFSWHAIFWVLALAAILAAALVFFFIPETLPKERRQPFHLRTTIRNFASLFRHKRVLGYMLASGFSFAGM
FSFLTAGPFVYIELNGVSPQNFGYYFALNIVFLFVMTIINSRFVRRVGALNMLRFGLWIQFIMGIWLVVS
ALLDLGFWALVVGVAAFVGCVSMISSNAMAVILDEFPHMAGTASSLAGTLRFGIGAIVGALLSLAPFTSA
WPMVWSMAFCSILSILFYLYASRPKKK
>gnl|CDD|182965 PRK11103, PRK11103, PTS mannose transporter subunit IID
MVDTTKTTTEKKLTQSDIRGVFLRSNLFQGSWNFERMQALGFCFSMVPAIRRLYPENNEARKQAIKRHLE
FFNTHPYVAAPILGVTLAMEEQRANGAEIDDGAINGIKVGLMGPLAGVGDPIFWGTVRPVFAALGAGIAM
SGSLLGPLLFFILFNLVRLATRYYGVAYGYKKGIDIVKDMGGGFLQKLTEGASILGLFVMGALVNKWTHV
NIPLVVSTITDQDGKTHVTTVQTILDQLMPGLVPLLLTFACMWLLRKKVNALWIIVGFFVIGIAGYWCGL
LG
>gnl|CDD|182966 PRK11104, hemG, menaquinone-dependent protoporphyrinogen IX dehydrogenase
MKTLILYSSRDGQTRKIASYIASELKEGIQCDVVNLHRIEEPDLSDYDRVVIGASIRYGHFHSALYKFVK
KHATQLNQMPSAFFSVNLTARKPEKRTPQTNSYARKFLMNSPWQPDLCAVFAGALRYPRYRWFDRFMIKL
IMKMTGGETDTSKEVEYTDWEQVANFAREFAQLTDKK
>gnl|CDD|182967 PRK11106, PRK11106, queuosine biosynthesis protein QueC; Provisional
MKRAVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGARAHKVLDVTLLNELA
VSSLTRDSIPVPDYEPEADGLPNTFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVK
ALNHAVSLGMAKDIRFETPLMWLNKAETWALADYYGQLDLVRHETLTCYNGIKGDGCGHCAACHLRANGL
NHYLANKPAVMAALKQKTGLA
>gnl|CDD|236848 PRK11107, PRK11107, hybrid sensory histidine kinase BarA; Provisional
MTKYSLRARVMILILAPTLLIGLLLSSFFVVNRYNELQRQLIDAGASIIEPLAIASEYGMTLQNRESVRQ
LISVLHRRHSDIVRSIAVFDENNQLFVTSNYHLDFESMRLPEGLPIPRLLSVERDGDSLILRTPIISESY
SPDESASSDAKNSQNMLGYIAIELDLKSVRLQQYREIFIAFLMLLLGIGLALLFAFRLMRDVTGPIRNMV
NTVDRIRRGQLDSRVEGNMLGELDMLKNGINAMAMSLSAYHEEMQQNIDQATSDLRETLEQMEIQNVELD
LAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILD
FSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNA
IKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQ
KLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIIDGLPTDCLAGKRLLYVEPNSAAAQATLDILSETP
LEVTYSPTLSQLPEAHYDILLLGLPVTFREPLTMLHERLAKAKSMTDFLILALPCHEQVLAEQLKQDGAD
ACLSKPLSHTRLLPALLEPCHHKQPPLLPPTDESRLPLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSG
HQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAK
PIDEAMLKQVLLRYKPGPKFTSRVVAPEPPEPVHFPNATLDWQLALRQAAGKPDLARDMLQMLLDFLPEV
RNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQQLRSGTSVEDLEPELLELLDEMENVA
RAAKKVLSQ
>gnl|CDD|236849 PRK11109, PRK11109, fused PTS fructose transporter subunit IIA/HPr protein
MFQLSVQDIHLGQQAGNKEEAIRQVAAALTQAGNVAEGYVDGMLAREQQTSTFLGNGIAIPHGTTDTRDL
VLKTGVQVFQFPQGVTWGDGQTAYVAIGIAAKSDEHLGLLRQLTHVLSDDSVAEQLKSATTAEELRALLM
GEKQSEQLKFDTSLITLDVPASDLLTLQALNAGRLKEAGAVDATFVAKVINSKPLNLGQGIWLSDSAEGN
LRSAVAVSRAANAFEVDGEPVALLLTVAAADDQPLAVLKRLSDLLLAQKADRLLSADAATLLALLTSEDA
ETDDVLSAEFVIRNEHGLHARPGAMLVNTIKQFNSEITVTNLDGTGKPANGRSLMKVVALGVKKGHRLRF
TAQGEDAEQALKAIGEAIAAGLGEG
>gnl|CDD|236850 PRK11111, PRK11111, YchE family NAAT transporter
IQTLFDFSIYIKFFIGLFALVNPVGILPVFISMTSHQTAAERNKTNLTANLSVAIILLISLFLGDFILNL
FGISIDSFRIAGGILVVTIAMSMISGKLGEDKQNKQEKSETAVRESIGVVPLALPLMAGPGAISSTIVWG
TRYHSWSNLLGFSVAIALFALCCWLLFRMAPWLVRLLGQTGINVITRIMGLLLMALGIEFIVTGIKGLFP
GLLN
>gnl|CDD|182971 PRK11112, PRK11112, tRNA pseudouridine synthase C; Provisional
MLEILYQDEWLVAVNKPAGWLVHRSWLDRHETVFVMQTVRDQIGQHVFTAHRLDRPTSGVLLMALSSEVA
RLLAQQFEQHQIQKTYHAIVRGWLMEEAVLDYPLKEELDKIADKFAREDKAPQPAVTHYRGLATVEMPVA
TGRYPTTRYSLVELEPKTGRKHQLRRHMAHLRHPIIGDTKHGDLRQNRSLAEHFGCSRLMLHASELSLTH
PFTGEPLTITAGLDETWQQLLSQFGWRGLLPENERVEFSAPSGQDGE
>gnl|CDD|182972 PRK11113, PRK11113, D-alanyl-D-alanine carboxypeptidase/endopeptidase; Provisional
MRFSRIIIGLTSLISFSVQAANVDEYITQLPAGANLALMVQKVGASAPAIDYHSQQMALPASTQKVITAL
AALLQLGPDFRFTTTLETKGKVENGVLKGDLIARFGGDPTLTRQDLRNMVATLKKSGVKQIDGNLLIDTS
VFASHDRAPGWPWNDLTQCFSAPPAAAIVDRNCFSVSLYSAPKPGDRAFIRVPSYYPVTVFSQVRTLPRG
SAEAQYCELDVVPGDLNRYTLTGCLPQRSKPLPLAFAVQDGASYAGAILKDELKQAGIELSGKILRQTQP
NKPGTVLASHQSAPLHDLLKIMLKKSDNMIADTLFRTIGHERFNVPGTFRAGSDAVRQILRQQAGIDLGN
TIIADGSGLSRHNLIAPATMMQVLQYIAQHDKELNLISMLPLAGYDGTLQYRGGLHQAGVDGKVSAKTGS
LQGVYNLAGFITTASGQRMAFVQFLSGYAVPPADQRNRRIPLVRFESRLYKDLYQNN
>gnl|CDD|236851 PRK11114, PRK11114, cellulose biosynthesis cyclic di-GMP-binding regulatory protein BcsB
MKRKLTWLCALALGMSAFPAFATAAAPATQPLANAAGQVMPAAPAAAAPVVAQAAPSRDVTLTFAQLGPA
PGPIVLRGVDPQGGIEFGVRSDEVVTKARLNLEYTYSPALLPDLSHLKVYLNGELMGTLPLDKEQLGKKV
LAQLPIDPRFITDFNRLRLEFIGHYTDVCEDPASSSLWADISPSSSLDLTYQKLPLPNDLALLPAPFFDP
RDNRPLTLPFVFAAKPDLATLRAAGIVASWFGSLADYRGARFPVLYNQLPERNAIVFATNDQRPDFLRLP
AVDGPTLAVIDNPADPYVKLLLVTGRDDKDLLQAAKALALGNALLRGQSVVVNDVKPLAPRKPYDAPNWV
PTDRPVTLGELVTYPQQLQVSGLEPDPIRVNLRLPPDLFLWRGDGIPLDLNYRYTAPPVRDDSRLNISLN
DQFVQSLPLNPKGELNRLLRLRLPLLQGLLDGETDVSIPALKLGSRNQLRFDFDYDSPKTGGCITTQPNN
NRAVIDPDSTIDFSGYRHYIAMPNLRAFANSGFPFTRLADLSQTAVVLPENPSEAEISTLLNLLGRIGAQ
TGYPALRVTVTDDGDVIQLADKDLLVIGGLPPQALLDDWRIDLPVQATGESWVKTPLRQIAPDESDRAAD
ADAYLSSSGAMAALIGFESPFNSQRSVVALLADSPRGLALLNDALNDPGKRAQIFGDVAVIRENGVRSLR
VGEVYYVGHLPWYERLWWALSNHPVLLALLAALSVLLLALVLWRLLRRIARRRLGP
>gnl|CDD|182974 PRK11115, PRK11115, phosphate signaling complex protein PhoU
MDNLNLNKHISGQFNAELESIRTQVLTMGGLVEQQLSDAITAMHNQDAELAKRVIEGDHKVNMMEVAIDE
ACVRIIAKRQPTASDLRLVMAIIKTIADLERIGDVADKIARTALEKFSQQHQPLLVSLESLGRHTIQMLH
DVLDAFARMDLDEAVRIYREDKKVDQEYEGIVRQLMTYMMEDPRTIPSVLTVLWCARSIERIGDRCQNIC
EYIIYFVKGKDVRHVGGDELDKLLAG
>gnl|CDD|182975 PRK11118, PRK11118, putative monooxygenase; Provisional
MATLLQVDFPFNGPFGEEMAKALKPLAESINEEPGFIWKIWTENEKTQEAGGIYLFEDEASAEAYLEMHT
ARLKNFGVEEVRAKIFDVNEPLSQINRAPL
>gnl|CDD|236852 PRK11119, proX, proline/glycine betaine ABC transporter substrate-binding protein ProX
MRKTVLLALALATLASTQAFAADLPGKGITVQPAQSTIAEETFQTLLVSRALEKLGYDVNKPKEVDYNVF
YTSIANGDATFTAVNWFPLHDDMYEAAGGDKKFYREGVYVGGAAQGYLIDKKTADKYNITNIAQLKDPKI
AKLFDTNGDGKADLTGCNPGWGCEAVINHQLKAYGLEDTVTHNQGNYAALMADTIARYKEGKPVLYYTWT
PYWVSDVLKPGKDVVWLQVPFSSLPGDQKNADTKLPNGKNYGFPVNTMHIVANKAFAEKNPAAAKLFEIM
KLPLADINAQNLRMHEGESSEADIERHVDGWIKAHQAQFDGWVKEARAAAK
>gnl|CDD|236853 PRK11121, nrdG, anaerobic ribonucleoside-triphosphate reductase-activating protein
MNYHQYYPVDVVNGPGTRCTLFVSGCVHQCPGCYNKSTWRLNSGHPFTKEMEDQIIADLNDTRIKRQGLS
LSGGDPLHPQNVPDILKLVQRVKAECPGKDIWVWTGYKLDELNAAQRQVVDLIDVLVDGKFVQDLADPSL
IWRGSSNQVIHRLR
>gnl|CDD|182978 PRK11122, artM, arginine ABC transporter permease ArtM
MLEYLPELLKGLHTSLTLTVASLLVALVLALIFTIILTLKTPVLVWLVRGYITLFTGTPLLVQIFLIYYG
PGQFPWLQEYPWLWHLLSQPWLCAMLALALNSAAYSTQLFYGAVRAIPEGQWQSCAALGMSKKQTLRILL
PYAFKRALSSYSNEVVLVFKSTSLAYTITLMDVMGYSQLLYGRTYDVMVFGAAGIIYLVVNGLLTLLMRL
IERKALAFERRN
>gnl|CDD|182979 PRK11123, PRK11123, arginine ABC transporter permease ArtQ
MNEFFPLASAAGMTVGLAVCALIVGLALAMLFAVWESAKWRPVAWPGTALVTLLRGLPEILVVLFIYFGS
SQLLLTLSDGFTLNLGFVQIPVQMDIENFEVSPFLCGVIALSLLYAAYASQTLRGALKAVPVGQWESGQA
LGLSKSAIFFRLVMPQMWRHALPGLGNQWLVLLKDTALVSLISVNDLMLQTKSIATRTQEPFTWYIIAAA
IYLVITLISQYILKRIELRATRFERRPS
>gnl|CDD|182980 PRK11124, artP, arginine transporter ATP-binding subunit; Provisional
MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSK
TPSDKAIRELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPL
HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASR
VVYMENGHIVEQGDASCFTQPQTEAFKNYLSH
>gnl|CDD|236854 PRK11125, nrfA, ammonia-forming cytochrome c nitrite reductase
IKINARRKFSLAIAFFFLTSLVAESTAAPAAEVKPSDKVEARNETFAPKYPDQYDSWKATSESSEIVDAL
AEDPRLVILWAGYAFSKDYNKPRGHFYAVTDVRNTLRTGAPKDAEDGPLPMACWSCKSPDVPRLIEEDGE
DGYFHGKWAKGGPEIVNPIGCADCHDTASMEFAKGKPALRLSRPYAERAMEAIGKPFEKASRQDQRSMVC
AQCHVEYYFDGKNKAVKFPWDKGTTVENMEKYYDEIGFSDWTHSLSKTPMLKAQHPDYETWSAGIHGKNG
VTCIDCHMPKVQNADGKVYTDHKIGNPFDNFDQTCANCHTQSKEALQKVVAERKAKVNDLKIKAEDQLVK
AHFEAKAAWDAGATEAEMKPILTDIRHAQWRWDYAIASHGIHMHAPEEALRILGTALDKAADARTKLARL
LAKKGITDPIQIPDISTKEKAQKAIGLDMEKINAEKQDFLKTVVPQWEEEARKNGLLSQE
>gnl|CDD|236855 PRK11126, PRK11126, 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
GLPWLVFLHGLLGSGQDWQPVGEALPDYPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWL
VGYSLGGRIAMYYACQGLAGGLCGLIVEGGNPGLQNAEERQARWQNDRQWAQRFRQEPLEQVLADWYQQP
VFASLNAEQRQQLVAKRSNNNGAAVAAMLEATSLAKQPDLRPALQALTFPFYYLCGERDSKFQALAQQLA
LPLHVIPNAGHNAHRENPAAFAASLAQILRLI
>gnl|CDD|182983 PRK11127, PRK11127, autonomous glycyl radical cofactor GrcA; Provisional
MITGIQITKAANDDLLNSFWLLDSEKGEARCIVAKAGYAEDQVVAVSKLGEIEYREVPVEVKPEVRVEGG
QHLNVNVLRRETLEDAVKHPEKYPQLTIRVSGYAVRFNSLTPEQQRDVIARTFTESL
>gnl|CDD|236856 PRK11128, PRK11128, 3-phenylpropionate MFS transporter
MVLQPTRWLALSYFGYFFAYGVFLPFWSVWLKGQGYTPETIGLLLGAGLVARFLGSLLIAPRVKDPSQLI
PALRLLALLTLLFAVAFWFGAHSFWLLFVAIGLFNLFFSPLVPLTDALANTWQKQIGLDYGKVRLWGSIA
FVIGSALTGKLVSWFGEQAILWILTAGVASMLLGQLLRPTIMPQGESRQQESAGWPAWKALLKEPTVWRF
LLCVSLLQGSHAAYYGFSAIYWQAAGYSASTIGYLWSLGVVAEVLIFAFSNRLFRRWSARDLLLLSAICG
VVRWGLMGSTTALPWLIVIQILHCGTFTVCHLAAMRYIAARPGSEVIRLQALYSALAMGGSIAIMTVLSG
FLYQHLGAGVFWVMALVALPALFIRPKVVASF
>gnl|CDD|182985 PRK11130, moaD, molybdopterin synthase small subunit; Provisional
MIKVLFFAQVRELVGTDALELAADFPTVEALRQHLAQKGDRWALALEDGKLLAAVNQTLVSFDHPLTDGD
EVAFFPPVTGG
>gnl|CDD|182986 PRK11131, PRK11131, ATP-dependent RNA helicase HrpA; Provisional
MKLTLTALQQQLDELMLRDRQRLSRRLHGAKKIKNPDAQQAIFQEIAKEIAQAAQRVLLREAARPEITYP
ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHTQPRRLAARTVANRIAE
ELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLK
ELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYRPIVEEADDTERDQLQAIFDAVDE
LGREGPGDILIFMSGEREIRDTADALNKLNLRHTEILPLYARLSNSEQNRVFQSHSGRRIVLATNVAETS
LTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFT
DPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDEQASAYKLTPLGRQLA
QLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLWNY
LQEQQKALSSNQFRRLCRTDYLNYLRVREWQDIYTQLRQVVKELGIPVNSEPAEYREIHTALLTGLLSHI
GMKDAEKQEYTGARNARFSIFPGSGLFKKPPKWVMVAELVETSRLWGRIAARIEPEWIEPLAQHLIKRSY
SEPHWEKAQGAVMATEKVTLYGLPIVAARKVNYGQIDPALCRELFIRHALVEGDWQTRHAFFRENLKLRA
EVEELEHKSRRRDILVDDETLFEFYDQRIGHDVVSARHFDSWWKKASRETPELLNFEKSMLIKEGAEKVS
KLDYPNFWHQGNLKLRLSYQFEPGADADGVTVHIPLPLLNQVEESGFDWQIPGLRRELVIALIKSLPKPV
RRNFVPAPNYAEAFLGRVTPLELPLLDSLERELRRMTGVTVDREDWQWDQVPDHLKITFRVVDDKNKKLA
EGKDLQELKDALKGKVQETLSAVADDGIEQSGLHIWSFGELPESYEQKRGGYKVKAYPALVDEKDSVAIK
LFDTELEQQQAMWQGLRRLLLLNIPSPIKYLHEKLPNKAKLGLYFNPYGKVLDLIDDCIACGVDKLIDEN
GGPVWTEEGFAALHEKVRAELNDTVVDIAKQVEQILTAVFNINKRLKGRVDMTMALALSDIKAQMGGLVY
RGFVTGNGWKRLGDTLRYLQAIEKRLEKLAVDPHRDRAQMLKVESVQQAWQQWLNKLPPARREDEDVKEI
RWMIEELRVSYFAQQLGTPYPISDKRILQAMEQI
>gnl|CDD|182987 PRK11132, cysE, serine acetyltransferase; Provisional
MSCEELEIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEA
YAADPEMIASAACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAF
QVDIHPAAKIGRGIMLDHATGIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILG
NIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGKPESDKPSMDMDQHFNGINHTFEYGDGI
>gnl|CDD|182988 PRK11133, serB, phosphoserine phosphatase; Provisional
MNNLTWCDLPEDVSLWPGLPLSLSGDEVMPLDYRAGRSGWLLYGRGLDKQRLTDFQRKLGAAMVIVAAWC
VEDYQVVRLAGSLTPRATRLAHELGLDVAPLGKIPHLRTPGLLVMDMDSTAIQIECIDEIAKLAGTGEEV
AEVTERAMRGELDFEASLRQRVATLKGADANILQQVRENLPLMPGLTELVLKLQALGWKVAIASGGFTYF
ADYLRDKLRLDAAVANELEIMDGKLTGNVLGDIVDAQYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMI
KAAGLGIAYHAKPKVNEQAQVTIRHADLMGVLCILSGSLKHK
>gnl|CDD|236857 PRK11138, PRK11138, outer membrane biogenesis protein BamB; Provisional
MQLRKTLLPGLLSVTLLSGCSSFNSEEDVVKMSPLPQVENQFTPTTVWSTSVGDGVGDYYSRLHPAVAYN
KVYAADRAGLVKALDADTGKEIWSVDLSEKDGWFSKNKSALLSGGVTVAGGKVYIGSEKGQVYALNAEDG
EVAWQTKVAGEALSRPVVSDGLVLVHTSNGMLQALNESDGAVKWTVNLDVPSLTLRGESAPATAFGGAIV
GGDNGRVSAVLMEQGQLIWQQRISQPTGATEIDRLVDVDTTPVVVGGVVYALAYNGNLVALDLRSGQIVW
KREYGSVNDFAVDGGRIYLVDQNDRVYALDTRGGVELWSQSDLLHRLLTAPVLYNGYLVVGDSEGYLHWI
NREDGRFVAQQKVDSSGFLSEPVVADDKLLIQARDGTVYAITRP
>gnl|CDD|182990 PRK11139, PRK11139, DNA-binding transcriptional activator GcvA; Provisional
MSRRLPPLNALRAFEAAARHLSFTRAAEELFVTQAAVSHQIKALEDFLGLKLFRRRNRSLLLTEEGQRYF
LDIREIFDQLAEATRKLRARSAKGALTVSLLPSFAIQWLVPRLSSFNEAHPDIDVRLKAVDRLEDFLRDD
VDVAIRYGRGNWPGLRVEKLLDEYLLPVCSPALLNGGKPLKTPEDLARHTLLHDDSREDWRAWFRAAGLD
DLNVQQGPIFSHSSMALQAAIHGQGVALGNRVLAQPEIEAGRLVCPFDTVLPSPNAFYLVCPDSQAELPK
VAAFRQWLLAEAAQEQE
>gnl|CDD|236858 PRK11142, PRK11142, ribokinase; Provisional
TMGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGES
MRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQL
ETPLETVLAAAKIAKQHGTKVILNPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVL
HQKGIETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAA
AIAVTRKGAQPSIPWREEIDAFLQEQ
>gnl|CDD|236859 PRK11143, glpQ, glycerophosphodiester phosphodiesterase; Provisional
LKNLSLALLLAALLAGSAAAAADSAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQL
VVLHDHYLDRVTDVAERFPDRARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKKVQVYPGRFPMGKSDFR
VHTFEEEIEFIQGLNHSTGKNIGIYPEIKAPWFHHQEGKDIAAKVLEVLKKYGYTGKDDKVYLQCFDANE
LKRIKNELEPKMGMDLKLVQLIAYTDWNETQEKQPDGKWVNYNYDWMFKPGAMKEVAKYADGIGPDYHML
VDETSTPGNIKLTGMVKEAHQAKLVVHPYTVRADQLPEYATDVNQLYDILYNQAGVDGVFTDFPDKAVKF
LNKQK
>gnl|CDD|182993 PRK11144, modC, molybdenum ABC transporter ATP-binding protein ModC
MLELNFKQQLGDLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIC
LPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIG
RALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAF
GPLEEVWASSAMRPWLPKEEQSSILKVTVLEHHPHYAMTALALGDQHLWVNKLDAPLGTALRIRIQASDV
SLVLQPPQQSSIRNILRAKVVEIYDDNGQVEVKLEVGGKTLWARITPWARDELALKPGQWLYAQIKSVSI
TQ
>gnl|CDD|182994 PRK11145, pflA, pyruvate formate lyase 1-activating protein
MSVIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEVTVEELMKEVVTYRHFMNAS
GGGVTASGGEAILQAEFVRDWFRACKKEGIHTCLDTNGFVRRYDPVIDELLDVTDLVMLDLKQMNDEIHQ
NLVGVSNHRTLEFARYLAKRNQKTWIRYVVVPGWTDDDDSAHRLGEFIKDMGNIEKIELLPYHELGKHKW
EAMGEEYKLDGVKPPSKETMERVKGILEQYGHKVMY
>gnl|CDD|236860 PRK11146, PRK11146, lipoprotein-releasing ABC transporter permease subunit LolE
MPLSLLIGLRFSRGRRRGGMVSLISVISTIGIALGVAVLIVGLSAMNGFERELNNRILAVVPHGEIEAVN
QPFTNWQEALARVQKVPGIAAAAPYVNFTGLVENGAKLKAVQVKGVDPQQEQRVSALPSFVQNDAWQNFK
AGEQQIILGKGVADALKVKQGDWVTLMIPNSNPDHKLLQPKRVRLQVAGILQLSGQLDHSLALIPLADAQ
QYLDMGDSVTGIALKVTDVFNANKLVRDAGEVTNSYVYIKSWIGTYGYMYRDIQMIRTIMYLAMVLVIGV
ACFNIVSTLVMAVKDKSGDIAILRTLGAKDGLIRAIFVWYGLLAGLKGSLIGVVIGVVVSLNLTPIIKGI
EKLIGHQFLSGDIYFIDFLPSELHWLDVFYVLVTALVLSLLASWYPARRASKLDPARVLSGQ
>gnl|CDD|236861 PRK11147, PRK11147, ABC transporter ATPase component; Reviewed
MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVAR
LQQDPPRNVEGTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRIN
EVLAQLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFIS
HDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTR
NEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIAL
IGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGKQEVMVNGRPRHV
LGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTV
LLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK
KLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEA
LKNGG
>gnl|CDD|182997 PRK11148, PRK11148, cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHS
SEAYQHFAEGIAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELS
EYQLEWLERKLADAPERHTLVLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDL
DWNGRRLLATPSTCVQFKPHCTNFTLDTVAPGWRELELHADGSLETEVHRLADTEFLPDTASEGY
>gnl|CDD|182998 PRK11150, rfaD, ADP-L-glycero-D-mannoheptose-6-epimerase; Provisional
MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFVNLVDLDIADYMDKEDFLAQIMAGDDFGDIE
AIFHEGACSSTTEWDGKYMMDNNYQYSKELLHYCLEREIPFLYASSAATYGGRTDDFIEEREYEKPLNVY
GYSKFLFDEYVRQILPEANSQICGFRYFNVYGPREGHKGSMASVAFHLNNQLNNGENPKLFEGSENFKRD
FVYVGDVAAVNLWFWENGVSGIFNCGTGRAESFQAVADAVLAYHKKGEIEYIPFPDKLKGRYQAFTQADL
TKLRAAGYDKPFKTVAEGVAEYMAWLNR
>gnl|CDD|182999 PRK11151, PRK11151, DNA-binding transcriptional regulator OxyR; Provisional
MNIRDLEYLVALAEHRHFRRAADSCHVSQPTLSGQIRKLEDELGVMLLERTSRKVLFTQAGLLLVDQART
VLREVKVLKEMASQQGETMSGPLHIGLIPTVGPYLLPHIIPMLHQTFPKLEMYLHEAQTHQLLAQLDSGK
LDCAILALVKESEAFIEVPLFDEPMLLAVYEDHPWANRDRVPMSDLAGEKLLMLEDGHCLRDQAMGFCFE
AGADEDTHFRATSLETLRNMVAAGSGITLLPALAVPNERKRDGVCYLPCIKPEPRRTIGLVYRPGSPLRS
RYEQLAEAIRARMDGHFDKVLKQAV
>gnl|CDD|236862 PRK11152, ilvM, acetolactate synthase 2 small subunit
MMQHQLTIKARFRPEVLERVLRVVRHRGFQVCSMNMTQNTDAQNINIELTVASERPIDLLSSQLNKLVDV
AHVEIL
>gnl|CDD|236863 PRK11153, metN, DL-methionine transporter ATP-binding subunit; Provisional
MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLT
ALSEKELRKARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQ
LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDR
VAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQSTLHLDLPEDYLARLQAEPTTGSGPLLRLEFTGESVDA
PLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDPGDIQAAIAYLQEHGVKVEVLGYV
>gnl|CDD|236864 PRK11154, fadJ, fatty acid oxidation complex subunit alpha FadJ
MEMASAFTLNVREDNIAVITIDVPGEKMNTLKAEFAEQVRAILKQLREDKELKGVVFISGKPDNFIAGAD
INMLAACKTAQEAEALARQGQQLFAEIEALPIPVVAAIHGACLGGGLELALACHYRVCTDDPKTVLGLPE
VQLGLLPGSGGTQRLPRLIGVSTALDMILTGKQLRAKQALKLGLVDDVVPHSILLEVAVELAKKGKPARR
PLPVRERLLEGNPLGRALLFKQARKKTLAKTQGNYPAPERILDVVRTGLEKGMSSGYEAEARAFGELAMT
PESAALRSIFFATTEMKKDTGSDAKPRPVNKVGVLGGGLMGGGIAYVTATKAGLPVRIKDINPQGINHAL
KYSWDLLDKKVKRRHLKPSERDKQMALISGTTDYRGFKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTI
FASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMPLVEVIPHAKTSAETIATTVALAKKQGKTPIVVRD
GAGFYVNRILAPYINEAARLLLEGEPIEHIDAALVKFGFPVGPITLLDEVGIDVGTKIIPILEAALGERF
SAPAAFDKLLNDDRKGRKNGRGFYLYGQKGKKSKKQVDESVYPLLGITPQSRLSANEIAERCVMLMLNEA
VRCLDEGIIRSARDGDIGAVFGIGFPPFLGGPFRYMDSLGAGEVVAILERLAAQYGDRFTPCERLVEMAE
RGESFYPT
>gnl|CDD|236865 PRK11160, PRK11160, cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
MRALLPFLKLYKRHWFMLSLGILLAIVTLLASIGLLTLSGWFLSASAVAGLAGLYSFNYMLPAAGVRGAA
IGRTAGRYGERLVSHDATFRVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISP
LVAALVVILVLTIGLSFFDLTLALTLGGILLLLLLLLPLLFYRLGKKPGQDLTHLRAQYRVQLTEWLQGQ
AELTLFGAEDRYRQQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTVVLMLWLAAGGVGGNAQPGALI
ALFVFAALAAFEALMPVAGAFQHLGQVIASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPD
QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVS
QRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARAL
LHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQEL
LAQQGRYYQLKQRL
>gnl|CDD|183004 PRK11161, PRK11161, fumarate/nitrate reduction transcriptional regulator Fnr
IQSGGCAIHCQDCSISQLCIPFTLNEHELDQLDNIIERKKPIQKGQTLFKAGDELKSLYAIRSGTIKSYT
ITEQGDEQITGFHLAGDLVGFDAIGSGQHPSFAQALETSMVCEIPFETLDDLSGKMPKLRQQIMRLMSGE
IKGDQEMILLLSKKNAEERLAAFIYNLSRRFAQRGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQK
SGMLAVKGKYITIENNDALAQLAGH
>gnl|CDD|236866 PRK11162, mltA, murein transglycosylase A; Provisional
MKGRWVKYLLTGTVLALLAGCSSKPTDRGQQYKDGKFTQPLSLVNQPNASGKPINAGDFAEQVNQIRNSS
PRLYGRYSNTYNAVQEWLLAGGDTRELRQFGIQAWQMEGVDNYGNVQFTGYYTPVIQARHTPQGEFQYPI
YRMPPKRGRLPSRAEIYAGALSGKGLELAYSNSLIDNFIMEVQGSGYVDFGDGRPLNFFAYAGKNGHAYR
SIGKVLIDRGEVPKEDMSMQAIREWGEKHSEAEVRELLEQNPSFVFFKPQPFAPVKGASAVPLVAMASVA
SDRSIIPPGTVLLAEVPLLDNNGKFTGKYELRLMVALDVGGAIKGQHFDIYQGIGPEAGHRAGHYNHYGR
VWVLK
>gnl|CDD|236868 PRK11166, PRK11166, chemotaxis regulator CheZ; Provisional
MMQPSIPAADEASAGDIIARIGQLTRMLRDSLRELGLDQAIEEAAEAIPDARDRLDYVAQMTEQAAERVL
NAVEAAQPHQDQLEKEAKALDARWDEWFANPIELADARELVTDTRAFLADVPEHTSFTNAQLLEIMMAQD
FQDLTGQVIKRMMDVIQEIERQLLMVLLENIPEQESRPKRENESLLNGPQINPEKADVVASQDQVDDLLD
SLGF
>gnl|CDD|236869 PRK11168, glpC, anaerobic glycerol-3-phosphate dehydrogenase subunit C
MSDTSFDSCIKCTVCTTACPVARVNPLYPGPKQAGPDGERLRLKDGALYDESLKYCSNCKRCEVACPSGV
KIGDIIQRARAKYVTERGPPLRDRILSHTDLMGSLATPFAPLVNAATGLKPVRWLLEKTLGIDHRRPLPK
YAFGTFRRWYRKQAAQQAQYKKQVAYFHGCYVNYNHPQLGKDLVKVLNAMGYEVLLPKEKCCGLPLIANG
FLDKARKQAEFNVESLREAIEKGIPVIATSSSCTLTLRDEYPELLGVDNAGVRDHIEDATEFLRRLLDQG
KLLPLKPLPLKVAYHTPCHLEKQGWGLYTLELLRLIPGLEVVVLDSQCCGIAGTYGFKKEKYETSQAIGA
PLFRQIEESGADLVVTDCETCKWQIEMSTGLECEHPITLLAEALGL
>gnl|CDD|183009 PRK11169, PRK11169, leucine-responsive transcriptional regulator Lrp
MVDSKKRPGKDLDRIDRNILNELQKDGRISNVELSKRVGLSPTPCLERVRRLERQGFIQGYTALLNPHYL
DASLLVFVEITLNRGAPDVFEQFNAAVQKLEEIQECHLVSGDFDYLLKTRVPDMSAYRKLLGETLLRLPG
VNDTRTYVVMEEVKQTNRLVIKTR
>gnl|CDD|183010 PRK11170, nagA, N-acetylglucosamine-6-phosphate deacetylase; Provisional
MYALTNGRIYTGHEVLDDHAVVIADGLIEAVCPVAELPPGIEQRDLNGAILSPGFIDLQLNGCGGVQFND
TAEAISVETLEIMQKANEKSGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNQALGLHLEGPYLNLVKK
GTHNPEFIRKPDAEMVDFLCENADVITKVTLAPEMVDAEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAG
ITFATHLYNAMPYITGREPGLVGAILDEPDVYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGA
NIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVRNLVEHVGIALDEALRMATLYPARAIGVDKRLG
SIEAGKVANLTAFTRDFKITKTIVNGNEVVTQ
>gnl|CDD|183011 PRK11171, PRK11171, (S)-ureidoglycine aminohydrolase
KMGYYAPVGGLPPQTDLLTTRAVVTEAYAVIPPDDIVTSVLPGWENTRAWVLARPGLGATFSQYLVEVEP
GGGSDQPEPDEGAETFLFVVEGEITLTLEGKTHALSEGGYAYLPPGSDWTLRNAGAEDARFHWIRKRYEP
VEGHEAPEAFVGNESDIEPIPMPGTDGVWATTRLVDPEDLRFDMHVNIVTFEPGASIPFVETHVMEHGLY
VLEGKGVYRLNNDWVEVEAGDFIWMRAYCPQACYAGGPGPFRYLLYKDVNRHPELT
>gnl|CDD|183012 PRK11172, dkgB, 2,5-didehydrogluconate reductase DkgB
MSIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNL
AKDKLIPSLKESLQKLRTDYVDLTLIHWPSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAI
AAVGAENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAW
AMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLVSPEGLAPEWD
>gnl|CDD|183013 PRK11173, PRK11173, two-component response regulator; Provisional
MQTPHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELR
EQANVALMFLTGRDNEVDKILGLEIGADDYITKPFNPRELTIRARNLLSRTMNLGTVSEERRSVESYKFN
GWELDINSRSLISPDGEQYKLPRSEFRAMLHFCENPGKIQSRAELLKKMTGRELKPHDRTVDVTIRRIRK
HFESTPDTPEIIATIHGEGYRFCGDLE
>gnl|CDD|236870 PRK11174, PRK11174, cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
MDKSRQKELTRWLKQQSKPAKRWLNLSILLGFLSGLLLIAQAWLLATILQALIIENIPREALLPPFILLI
LLFVLRALLAWLRERVGFKAGQHIRQQIRQQVLDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDFYARY
LPQMALAVLVPLLILIAVFPINWAAGLILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLR
GLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLSSAVLEFFASISIALVAVYFGFSYLGELNFGH
YGTGVTLFAGFFVLILAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEKELASNDPVTI
EAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPES
WRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQ
AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQ
IVQQGDYAELSQAGGLFATLLAHRQEEI
>gnl|CDD|236871 PRK11175, PRK11175, universal stress protein UspE; Provisional
AKYQNILVVIDPNQDDQPALRRAVYLAQRNGGKITAFLPIYDFSYEMTTLLSPDEREAMRQGVISQRTAW
IREQAKPYLDAGIPIEIKVVWHNRPFEAIIQEVIAGGHDLVVKMTHQHDKLESVIFTPTDWHLLRKCPCP
VLMVKDQDWPEGGKILVAVNVASEEPYHDALNEKLVEEAIDLAEQLNHAEVHLVNAYPVTPINIAIELPE
FDPSVYNDAIRGQHLLAMKALRQKFGIDEEQTHVEEGLPEEVIPDLAEHLDAELVILGTVGRTGLSAAFL
GNTAEHVIDHLNCDLLAIKPDGYVS
>gnl|CDD|183016 PRK11176, PRK11176, lipid A ABC transporter ATP-binding protein/permease MsbA
MHNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVLKWMPLV
VIGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSS
GALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQM
LKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLT
AGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKRVIERAKGDIEFRNVTFT
YPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVA
LVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIA
IARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERG
THAELLAQNGVYAQLHKMQFGQ
>gnl|CDD|183017 PRK11177, PRK11177, phosphoenolpyruvate-protein phosphotransferase PtsI
MISGILASPGIAFGKALLLKEDEIVINRKKISADQVDQEVERFLSGRAKASAQLEAIKTKAGETFGEEKE
AIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHSVIEGQAKALEELDDEYLKERAADVRDIGKRLLKN
ILGLKIIDLSAIQEEVILVAADLTPSETAQLNLKKVLGFITDIGGRTSHTSIMARSLELPAIVGTGNITK
QVKNGDYLILDAVNNQIYVNPTNEVIEELKAVQEQYASEKAELAKLKDLPAITLDGHQVEVCANIGTVRD
VEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFQAYKAVAEAMGSQAVIVRTMDIGGDKELPYMNLPKE
ENPFLGWRAIRIAMDRKEILHDQLRAILRASAFGKLRIMFPMIISVEEVRELKAEIEILKQELRDEGKAF
DESIEIGVMVETPAAAVIARHLAKEVDFFSIGTNDLTQYTLAVDRGNELISHLYNPMSPSVLNLIKQVID
ASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNFEDAKALAEQALAQPTADE
LMTLVNKFIEEKTLC
>gnl|CDD|183018 PRK11178, PRK11178, uridine phosphorylase; Provisional
MSDVFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGP
STSIAVEELAQLGVRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVE
AAKSIGATTHVGVTASSDTFYPGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLR
AGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVVEAARRLL
>gnl|CDD|183019 PRK11179, PRK11179, DNA-binding transcriptional regulator AsnC; Provisional
MMENYQIDNLDRGILEALMENARTPYAELAKQFGVSPGTIHVRVEKMKQAGIITGTRVDVNPKQLGYDVC
CFIGIILKSAKDYPSALAKLESLDEVVEAYYTTGHYSIFIKVMCRSIDALQHVLINKIQTIDEIQSTETL
ISLQNPIMRTIKP
>gnl|CDD|183020 PRK11180, rluD, 23S rRNA pseudouridine(1911/1915/1917) synthase RluD
MAQQVQLTATVSESQLGQRLDQALAELFPDYSRSRIKEWILDQRVLVNGKVINKPKEKVLGGEQVAIDAE
IEEEARFEPQDIPLDIVYEDDDILVINKPRDLVVHPGAGNPDGTVLNALLHYYPPIADVPRAGIVHRLDK
DTTGLMVVAKTVPAQTRLVEALQKREITREYEAVAIGHMTAGGTVDEPISRHPTKRTHMAVHPMGKPAVT
HYRIMEHFRVHTRLRLRLETGRTHQIRVHMAHITHPLVGDQVYGGRPRPPKGASEEFISTLRKFDRQALH
ATMLRLYHPITGIEMEWHAPLPQDMVELIEALRADFEEHKDEVDW
>gnl|CDD|183021 PRK11181, PRK11181, 23S rRNA (guanosine(2251)-2'-O)-methyltransferase RlmB
MSEIIYGIHAVQALLERAPERFIEVFVLKGREDKRLLPLINELEAQGIVIQLANRQTLDEKAEGAVHQGI
IARVKPGRQLQENDLPDLLASLEQPFLLILDGVTDPHNLGACLRSADAAGVHAVIVPKDRSAQLNATAKK
VACGAAETVPLIRVTNLARTMRMLQEKNIWIVGTAGEADHTLYQSKLTGPLALVMGAEGEGMRRLTREHC
DELISIPMAGSVSSLNVSVATGICLFEAVRQRSA
>gnl|CDD|236872 PRK11183, PRK11183, D-lactate dehydrogenase; Provisional
DNKALINELTRIVGSSHVLTDPAKTERYRKGFRSGQGDALAVVFPGTLLELWRVLQACVAADKIIIMQAA
NTGLTGGSTPNGNDYDRDIVIISTLRLDKIQLLNNGKQVLALPGTTLYQLEKALKPLGREPHSVIGSSCI
GASVIGGICNNSGGALVQRGPAYTEMALYAQIDEDGKLELVNHLGIDLGETPEEILTRLEDGRFDDEDVR
HDGRHASDHEYAERVRDVDADTPARFNADPRRLFEASGCAGKLAVFAVRLDTFPAEKNTQVFYIGTNDPA
VLTEIRRHILANFKNLPVAGEYMHRDAFDIAEKYGKDTFLMIDKLGTDKLPKLFALKGRVDAFLEKVPFL
PPHFTDRVMQALSKLFPSHLPKRMKDYRDKYEHHLLLKMSGDGIEEARAYLKEYFKSAEGDFFECTPEEG
KKAFLHRFAAAGAAIRYRAVHRDEVEDILALDIALRRNDRDWFEHLPPEIDDQLVHKLYYGHFFCHVFHQ
DYIVKKGVDVHALKHEMLELLDARGAEYPAEHNVGHLYKAKPALKKFYRELDPTNSFNPGIGKTSKRKNW
QECC
>gnl|CDD|236873 PRK11186, PRK11186, carboxy terminal-processing peptidase
KFFRLTLLAGLLALAGSAFAVEPIIRADQLPVLKQEPQHATASKRVTSRFTRSHYRQFDLDDAFSAKIFD
RYLNLLDYSHNVLLASDIDQFAKYKTQLDDELKSGKLDVAYDLYNLAQKRRFERYQYALSLLDKPMDFTG
NDTIELDRSKAPWPKDEAELNELWDQRVKYDALNLKLTGKTWPEIKETLTKRYNFAIKRLTQTNSEDVFQ
LAMNAFAREIDPHTSYLSPRNAEQFNTEMNLSLEGIGAVLQMDDDYTVINSLVAGGPAAKSKKLSVGDKI
VGVGQDGKPIVDVIGWRLDDVVALIKGPKGSKVRLEILPAGKGTKTRIVTLTRDKIRLEDRAVKMSVKTV
GGEKVGVLDIPGFYVGLTDDVKKQLQKLEKQNVSGIIIDLRGNGGGALTEAVSLSGLFIPSGPVVQVRDN
NGRVRVDSDTDGVVYYKGPLVVLVDRYSASASEIFAAAMQDYGRALIVGEPTFGKGTVQQHRSLNRIYDQ
MLRPLGSVQYTIQKFYRINGGSTQRKGVTPDIIFPTGIEPTETGESFEDNALPWDSIPAATYVKSGDLTA
LVPELLKKHNARIAKDPEFQYINEDIARYKAEKDKNIVSLNYAEREKENDEDDAKRLARLNERFKREGKK
PLKSLDDLPKDYEEPDPYLDETVNIALDLAKLEKAAP
>gnl|CDD|236874 PRK11187, PRK11187, replication initiation negative regulator SeqA
MKTIEVDEELYRYIASHTQHIGESASDILRRLLKLSAESQVPAAPVTKSVPVASPAPAAAKPVKTIKDKV
RAVRELLLSDEYAEQKKAVNRFLLILSTLYRLDPQAFAQATESLHGRTRVYFARDEQTLLKAGNSTKPKH
IPGTPFWVITNTNTGRKRSMLEHVMQSMGFPAELIEKVCGTI
>gnl|CDD|183025 PRK11188, rrmJ, 23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE
MTGKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYAV
TQIGDKGRVIACDILPMDPIVGVDFLQGDFRDELVLKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPRA
MYLVELALDMCRDVLAPGGSFVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRKL
>gnl|CDD|236875 PRK11189, PRK11189, lipoprotein NlpI; Provisional
MKPFLRWCFVATALLLAGCSSSNSSWRKNEVLAVPLQPTLQQEVILARLNQILASRDLTDEERAQLHYER
GVLYDSLGLRALARNDFSQALALRPDMADAYNYLGIYLTQAGNFDAAYEAFDSVLELDPTYNYAYLNRGI
ALYYGGRYELAQDDLLAFYQDDPNDPYRALWLYLAESKLDPKQAKENLKQRYEKLDKEQWGWNIVEFYLG
KISEETLMERLKAGATDNTELAERLCETYFYLAKYYLSLGDLDEAAALFKLALANNVYNFVEHRYALLEL
ALLGQDQDDLAESDQQ
>gnl|CDD|183027 PRK11190, PRK11190, iron-sulfur cluster biogenesis protein NfuA
MITISDAAQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTELKFDGFSAYVDELSA
PFLEDAEIDFVTDQLGSQLTLKAPNAKMRKVADDAPLMERVEYVLQSQINPQLAGHGGRVSLMEITEDGY
AILQFGGGCNGCSMVDVTLKEGIEKQLLNEFPGELKGVRDLTEHQRGEHSYY
>gnl|CDD|236876 PRK11191, PRK11191, ribonuclease E inhibitor RraB
MANEELLEEQREETREIIEELLEDGSDPDALYTIEHHFSADDFDKLEKAAVEAFKLGYEVTDAEELELED
GDVIFCCDAVSEVALNAELIDAQVEQLLALAEKFDVEYDGWGTYFEDPNAEDGDDEDFVDEDDDGVRH
>gnl|CDD|236877 PRK11192, PRK11192, ATP-dependent RNA helicase SrmB; Provisional
TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRK
SGPPRILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKE
ENFDCRAVETLILDEADRMLDMGFAQDIETIAAETRWRKQTLLFSATLEGDAVQDFAERLLNDPVEVEAE
PSRRERKKIHQWYYRADDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMV
QAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVE
AHDHLLLGKIERYIEEPLKARVIDELRPKTKAPSEKKTGKPSKKVLAKRAEKKEKEKEKPKVKKRHRDTK
NIGKRRKPSGTSEE
>gnl|CDD|236878 PRK11193, PRK11193, 23S rRNA accumulation protein YceD
MQKVKLPLTIDPVRAAQKRLDYQGIYPPEQLKRLAESVVSVDSDVEVSLSFGIDNQRLVVLKGKAVVEVT
LECQRCNEPFTHQVEVEFCFSPVRNDEQAEELPEAYEPIEVNEFGEVDLLQLVEDELILALPIVPMHDSE
HCEVSEADMVFGELPEEAEKPNPFAVLASLKR
>gnl|CDD|183031 PRK11194, PRK11194, ribosomal RNA large subunit methyltransferase N; Provisional
MKEKKINLLDLNRQQMREFFAELGEKPFRADQVMKWIYHYGCDDFDEMTNINKVLREKLKEVAEIRAPEV
AEEQRSSDGTIKWAIAVGDQRVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQV
WRAAKIIGAAKVTGQRPITNVVMMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKL
GDMIDVALAISLHAPNDELRDEIVPINKKYNIETFLAAVRRYLEKSNANQGRVTVEYVMLDHVNDGTEHA
HQLAELLKDTPCKINLIPWNPFPGAPYGRSSNSRIDRFSKVLMEYGFTVIVRKTRGDDIDAACGQLAGDV
IDRTKRTLKKRMQGEAISVKAV
>gnl|CDD|236879 PRK11195, PRK11195, lysophospholipid transporter LplT; Provisional
MSKGFYAIMAAQFFSALADNALLFAAIALLKELHYPDWSQPLLQMFFVLAYIVLAPFVGAFADSFPKGRV
MFIANGIKLLGCLLMLFGIHPLLAYGLVGIGAAAYSPAKYGILTELLPGEKLVKANGWMEGSTIAAILLG
TVLGGALADPHAEAALAVCALIYLLAALFNLFIPRLGARRPGQSWNPIALLRDFFHACRVLWRDKLGRFS
LAGTTLFWGAGATLRFLVLAWAPVALGITLNQPAYLQAVVAIGIAVGAGAAARLVTLETVLRVLPAGILM
GLVVLLMALQHSLLPAYPLLILIGALGGFFVVPMNALLQHRGHVLVGAGHSIAVQNFNENLAMLLMLGLY
SLLVKLGVPVVAVIVGFGLLVALAMALLWRWHRRNQRQFDSVL
>gnl|CDD|183033 PRK11197, lldD, L-lactate dehydrogenase; Provisional
MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLS
MPVALAPVGLTGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNA
LERAKAAGCSTLVFTVDMPVPGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAY
LGKPTGLEDYIGWLGNNFDPSISWKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQL
DGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIALGADTVLLGRAFVYALAAAGQAGVANLLDL
IEKEMRVAMTLTGAKSISEITRDSLVQGNAA
>gnl|CDD|236880 PRK11198, PRK11198, LysM domain/BON superfamily protein; Provisional
MGLFSFVKEAGEKLFDAVTAQADNEDAADALKEHISKQGLGDADVNVQVEDGKATVSGDAASQEAKEKIL
LAVGNIQGIASVDDQVKVATPAPESQFYTVKSGDTLSAIAKKVYGNANKYNKIFEANKPMLKSPDKIYPG
QVLRIPE
>gnl|CDD|183035 PRK11199, tyrA, bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
MVAELTALRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLASRRAEAEALGVPPDL
IEDVLRRVMRESYSSENDKGFKTLNPDLRPVVIVGGKGQLGRLFAKMLTLSGYQVRILEQDDWDRAEDIL
ADAGMVIVSVPIHLTEEVIARLPPLPEDCILVDLTSVKNAPLQAMLAAHSGPVLGLHPMFGPDVGSLAKQ
VVVVCDGRQPEAYQWLLEQIQVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAKENVDLEQLLAL
SSPIYRLELAMVGRLFAQDPQLYADIIMSSPENLALIKRYYQRFGEALELLEQGDKQAFIDSFRKVEHWF
GDYAEQFLKESRSLLQQANDNRQR
>gnl|CDD|183036 PRK11200, grxA, glutaredoxin 1; Provisional
MFVVIFGRPGCPYCVRAKELAEKLSEERDDFDYRYVDIHAEGISKADLEKTVGKPVETVPQIFVDQKHIG
GCTDFEAYVKENLGL
>gnl|CDD|236881 PRK11202, PRK11202, HTH-type transcriptional repressor FabR
MMGVRAQQKEKTRRALIDAAFSQLSAERSFSSLSLREVAREAGIAPTSFYRHFRDMDELGLTMVDESGLM
LRQLMRQARQRIAKGGSVIRTSVSTFMEFIGNNPNVFRLLLRERSGTSAAFRAAVAREIQHFIAELADYL
ELENHMPREFAEAQAEAMVTIVFSAGAEALDVDREQRRQLEERLVLQLRMIAKGAYAIIPGNV
>gnl|CDD|183040 PRK11207, PRK11207, tellurite resistance methyltransferase TehB
MTIRDENYFTDKYGLTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLER
IKAAENLDNLHTAVVDLNNLTFDGEYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTAD
YPCTVGFPFAFKEGELRRYYEGWEMVKYNEDVGELHRTDANGNRIKLRFATMLARKK
>gnl|CDD|183041 PRK11212, PRK11212, 7-cyano-7-deazaguanine/7-aminomethyl-7-deazaguanine transporter
MSSFTPAQRRRALFWLSLFHILIITSSNYLVQLPFTIFGFHTTWGAFSFPFIFLATDLTVRIFGAPLARR
IIFAVMLPALLISYVISVLFYQGSWQGFAALAEFNLFVARIALASFMAYVLGQILDVHVFNRLRQSRAWW
VAPTASTLFGNLSDTLAFFFIAFYRSSDPFMAEHWVEIALVDYCFKLLISLLFFLPAYGVLLNMLLKKLA
>gnl|CDD|183042 PRK11228, fecC, iron-dicitrate ABC transporter permease FecC
LWGLPVAALIGLFWLSLFCYSAIPISAADALNALLPGHTPTLPEALVQNLRLPRSLVAVLIGASLALAGA
LLQTLTHNPLASPSLLGINSGAALAMALTSALSPTPFAGYSLAFIAACGGGLSWLLVMTAGGGWRHTHDR
NRLILAGIALSALCMALTRITLLLAEDHAYGIFYWLAGGVSHARWQEVWQLLPFVVTAVPVVLLLANQLN
LLNLSDSSAHTLGVNLTRLRLVVNMLVLLLVGACVSVAGPVAFIGLLVPHLARFWIGYDQRNVLPMSMLL
GATLMLLADLLARALAFPGELPAGAVLALIGAPCFVWLARRRG
>gnl|CDD|183043 PRK11230, PRK11230, glycolate oxidase subunit GlcD; Provisional
MSILYDERLDGALPDVDRTSLLMALREHLPGLEILHTDEELIPYECDGLSAYRTRPLLVVLPKQMEQVQA
LLAVCHRLRVPVVARGAGTGLSGGALPLEKGVLLVMARFNRILDINPVGRRARVQPGVRNLAISQAAAPH
GLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEALTLGSDALDSPGFDLLALF
TGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPGGLEMMDNLSIRAAEDFIH
AGYPVDAEAILLCELDGVESDVQEDCERVNDILLKAGATDVRLAQDEAERVRFWAGRKNAFPAVGRISPD
YYCMDGTIPRRELPGVLEGIARLSQQYGLRVANVFHAGDGNMHPLILFDANEPGELERAEALGGKILELC
VEVGGSITGEHGVGREKINQMCAQFNSDEITLFHAVKAAFDPDGLLNPGKNIPTLHRCAEFGAMHVHHGH
LPFPELERF
>gnl|CDD|183044 PRK11231, fecE, Fe(3+) dicitrate ABC transporter ATP-binding protein FecE
MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLS
SRQLARRLALLPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLS
GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVV
LANGHVMAQGTPEEVMTPGLLRTVFDVEAEIHPEPVSGTPMCVVR
>gnl|CDD|183045 PRK11233, PRK11233, nitrogen assimilation transcriptional regulator; Provisional
MNFRRLKYFVKIVDIGSLTQAAEVLHIAQPALSQQVATLEGELNQQLLIRTKRGVTPTEAGKILYTHARA
ILRQCEQAQLAVHNVGQALSGQVSIGLAPGTAASSLTMPLLQAVRAEFPGIVLYLHENSGATLNEKLMNG
QLDMAVIYEHSPVAGLSSQPLLKEDLFLVGTQDCPGQSVDLAAVAQMNLFLPRDYSAVRLRVDEAFSLRR
LTAKVIGEIESIATLTAAIASGMGVTVLPESAARSLCGAVNGWMARITTPSMSLSLSLNLSARLPLSPQA
QAVKEILLSLVSSPVMEKRELQLVS
>gnl|CDD|236884 PRK11234, nfrB, phage adsorption protein NrfB
VLATWLYGLKVIAITLAVLMFISGLDDLFIDVVYWVRRIKRKLSVYRRYPRMSYRELYKPDEKPLAIMVP
AWNETGVIGNMAELAATTLDYENYHIFVGTYPNDPATQADVDAVCARFPNVHKVVCARPGPTSKADCLNN
VLDAITQFERSANFAFAGFILHDAEDVISPMELRLFNYLVERKDLIQIPVYPFEREWTHFTSGTYIDEFA
ELHGKDVPVREALAGQVPSAGVGTCFSRRAVTALLEDGDGIAFDVQSLTEDYDIGFRLKEKGMREIFVRF
PVVDEAKEREQRKFLQHARTSNMICVREYFPDTFSAAVRQKSRWIIGIVFQGFKTLGWTSSLTLNYFLWR
DRKGAITNFVSFLAMLLMLQLLLLLLYESLWPDAWHFLSIFSGSAWLMTLLWLNFGLMVNRIVQRVIFVT
GYYGLTQGLLSVLRLLWGNLINFMANWRALRQVLQHGDPRRVAWDKTTHDFPSVTGDTRSLRPLGQILLE
NGVITEEQLDTALRNRVRGLRLGQSLLMQGLISAEQLAQALAEQNGVAWESLDPWQIPSSLIAEMPASVA
LHYAVLPLREEGDELIVASEDGISPVSLAALTRKLGRKVRYVIVPRGQVTTGLRHWYARRRGHDPRAMLY
NAVQHQQQAGEIWRQYVPHQFLFAEILTTLGHIPRSAINVLLLRHERSSLPLGKFLVTEGVISQETLDRA
LTIQRELQVSMQSLLLKAGLNTEQVAQ
>gnl|CDD|183047 PRK11235, PRK11235, type II toxin-antitoxin system RelB/DinJ family antitoxin
MATINVRVDDELKARAYAVLEKLGVTPSEALRLLLQYVAENGRLPFKTVLLSDEDAALLETVRERLANPQ
KGIRVTLDDL
>gnl|CDD|183048 PRK11239, PRK11239, hypothetical protein; Provisional
MKYQLTALEARVIGCLLEKQVTTPEQYPLSVNGVVTACNQKTNREPVMNLSESEVQEQLDNLVKRHYLRT
VSGFGNRVTKYEQRFCNSEFGDLKLSAAEVALITTLLLRGAQTPGELRSRAARMYEFSDMAEVESTLEQL
ANREDGPFVVRLAREPGKRESRYMHLFSGEVDDQPAVTDMSNAVDGDLQARVEALEIEVAELKQRLDSLL
AHLGD
>gnl|CDD|183049 PRK11240, PRK11240, penicillin-binding protein 1C; Provisional
RLLTKRGRWLWLAAAPLLLFLALWLADKLWPLPLHEVNPARVVVAEDGTPLWRFADADGIWRYPVTIEDV
SPRYLEALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQVARLLDPHPRTFGGKIRQLW
RALQLEWHLSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYAEAALLAVLPQAPSRLRPDRWP
ERAEAARNKVLERMAEQGVWSAEQVKESREEPVWLAPRQMPQLAPLFARMMLGKSKSDKIVTTLDAGLQR
RLEDLALNWKGRLPPRSSLAMIVVDHTDMAVRGWVGSVDLNDDSRFGHVDMVNAIRSPGSVLKPFVYGLA
LDDGLIHPASLLQDVPRRTGDYRPGNFDSGFHGPVSMSEALVRSLNLPAVQVLEAYGPKRFAAKLRNVGL
PLYLPAGAEPNLSLILGGAGARLEDMVAAYSAFARHGKAAKLRLQPDDPLLERPLMSPGAAWIIRRIMAD
EAQPLPDAALPRVVPLAWKTGTSYGYRDAWAIGVNARYVIGIWTGRPDGTPVVGQFGFASAVPLLNQVNN
LLLSRSSQRGANLPEDPRPASVSRGVICWPGGQSLPEGDSNCRRRLATWLLDGSQPPTLLLPEQEGINGI
RFPIWLDENGLRVAADCPQARQEMIAVWPLPLEPWLPASERRAARLPPASTICPPLGHDAALPLQLTGVR
DGAVIKRLPGAAEATLPLSTSGGAGRRWWFLNGEPLTERGRNVTLHLTDPGRYQLLVMDESGQIAAVNFV
LQ
>gnl|CDD|183050 PRK11241, gabD, NADP-dependent succinate-semialdehyde dehydrogenase I
MQLNDSTLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAK
ERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRL
IVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVT
GSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALAS
KFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEK
GARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYA
RDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL
>gnl|CDD|183051 PRK11242, PRK11242, DNA-binding transcriptional regulator CynR; Provisional
MLLRHIRYFLAVAEHGNFTRAAEALHVSQPTLSQQIRQLEESLGVQLFDRSGRTVRLTDAGEVYLRYARR
ALQDLEAGRRAIHDVADLSRGSLRLAMTPTFTAYLIGPLIDAFHARYPGITLTIREMSQERIEALLADDE
LDVGIAFAPVHSPEIEAQPLFTETLALVVGRHHPLAARRKALTLDELADEPLVLLSAEFATREQIDRYFR
RHGVTPRVAIEANSISAVLEIVRRGRLATLLPAAIAREHDGLCAIPLDPPLPQRTAALLRRKGAYRSAAA
RAFIELALERRAEIGR
>gnl|CDD|183053 PRK11245, folX, dihydroneopterin triphosphate 2'-epimerase
MAPPAAIIRIKNLRLRTFIGIKEEEINNRQDVVINVTIHYPADKARTSDDIDDALNYRTITKNIIQHVEN
NRFSLLEKLTQDVLDIAREHPWVTYAEVEIDKPHALRFADSVSMTLSWQR
>gnl|CDD|236885 PRK11246, PRK11246, YtjB family periplasmic protein
MARAKLKFRLHRTAIVLICLALLVALMQGASWFSQSHQRARNPQLEELARTLARQVALSLAPLMRSDSPD
EKRIQAILDQLTDESRILDASVYDEQGDLIARSGESVNVRDRLALDGKKAGSYFNQQIVEPIAGKNGPLG
FLRLTLDTHTLATEAKQVDNTTNILRLMLLLALAIGIVLTRTLLQGKRTRWQQSPFLLTASKPVPEEEES
EKKEPEAL
>gnl|CDD|183055 PRK11247, ssuB, aliphatic sulfonates transport ATP-binding subunit; Provisional
MMNTARLNQGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL
AGTAPLAEAREDTRLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQ
RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG
KIGLDLTVDLPRPRRRGSARLAELEAEVLQRVMSRGESEPTRLRWAG
>gnl|CDD|183056 PRK11248, tauB, taurine ABC transporter ATP-binding subunit
MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA
ERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIA
RALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV
ERLPLNFARRFVAGESSRSIKSDPQFIAMREYVLSRVFEQREAFS
>gnl|CDD|236886 PRK11249, katE, hydroperoxidase II; Provisional
HNEKNPHQHQSPLHDSSEAKPGMDSLAPEDGSHRPAPEPTPPGAQPTAPGSLKAPDTRNEKLNSLEAFRK
GSEGYALTTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKS
LSDITKAAFLQDPGKITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIK
FPDFVHAVKPEPHNEIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAE
GKATFVRFHWKPVAGKASLVWDEAQKLTGRDPDFHRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDL
LDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPGHIVPGIDFTNDPLLQGRLFSYTDTQISRL
GGPNFHEIPINRPTCPYHNFQRDGMHRMTIDTGPANYEPNSINGNWPRETPPAPKRGGFESYQERVEGNK
VRERSPSFGDYYSQPRLFWLSQTPIEQRHIIDAFSFELGKVVRPYIRERVVDQLAHIDLTLAQAVAENLG
IPLTDEQLNITPPPDVNGLKKDPALSLYAIPDGDIKGRKVAILLNDGVDAADLLAILKALKAKGVHAKLL
YPRMGEVTADDGTVLPIAATFAGAPSLTFDAVIVPGGKANIADLADNGDARYYLLEAYKHLKPIALAGDA
RKLKAALKLPDQGEEGLVEADSADGSFMDELLTAMAAHRVWSREPKADAIPA
>gnl|CDD|183058 PRK11251, PRK11251, osmotically-inducible lipoprotein OsmE
NMAGILSAAAVLTMLAGCTAYDRNPVQFVEPVVKDVKKGMTRQQVAQIAGKPSSEVSMIHARGTCQTYIL
GNRDGKAQTYFVSFDDTGHVDNKGFQTCAEYDTDPQAAK
>gnl|CDD|183059 PRK11253, ldcA, L,D-carboxypeptidase A; Provisional
MSLFHLIAPSGYPIDQAAALRGVQRLTDAGHQVENVEVIARRYQRFAGTDGERLADLNSLADLTTPNTIV
LAVRGGYGASRLLAGIDWQGLAARQQDDPLLIVGHSDFTAIQLALLAQANVITFSGPMLAADFGAETLNA
FTEHHFWLALRNPTFTIEWQGPQGPTCRVEGTLWGGNLAMLISLIGTPWMPQIEGGILFLEDINEHPFRV
ERMLLQLHHAGILARQQAIVLGSFSGARPNDYDAGYDLEAVYAFLRSRLSIPVITGLDFGHEQRTVTLPL
GAHAELVATAEGFQLTLSGYPVLKA
>gnl|CDD|236887 PRK11259, solA, N-methyl-L-tryptophan oxidase
TMRYDVIVIGLGSMGSAAGYYLARRGLRVLGLDRFMPPHQQGSSHGDTRIIRHAYGEGPAYVPLVLRAQE
LWRELERESGEPLFVRTGVLNLGPADSDFLANSIRSARQHGLPHEVLDAAEIRRRFPQFRLPDGYIALFE
PDGGFLRPELAIKAHLRLAREAGAELLFNEPVTAIEADGDGVTVTTADGTYEAKKLVVSAGAWVKDLLPP
LELPLTPVRQVLAWFQADGRYSEPNRFPAFIWEVPDGDQYYGFPAENGPGLKIGKHNGGQEITSPDERDR
FVTVAEDGAELRPFLRNYLPGVGPCLRGAACTYTNTPDEHFIIDTLPGHPNVLVASGCSGHGFKFASVLG
EILADLAQDGTSDFDLSPFSLSRFAA
>gnl|CDD|183061 PRK11260, PRK11260, cystine ABC transporter substrate-binding protein
MKLAHLGRQALMGVMAVALVAGMSVKSFADEGLLNKVKERGTLLVGLEGTYPPFSFQGEDGKLTGFEVEF
AEALAKHLGVKASLKPTKWDGMLASLDSKRIDVVINQVTISDERKKKYDFSTPYTVSGIQALVKKGNEGT
IKTAADLKGKKVGVGLGTNYEQWLRQNVQGVDVRTYDDDPTKYQDLRVGRIDAILVDRLAALDLVKKTND
TLAVAGEAFSRQESGVALRKGNPDLLKAVNQAIAEMQKDGTLKALSEKWFGADVTK
>gnl|CDD|236888 PRK11263, PRK11263, cardiolipin synthase ClsB
KCSWREGNRIQLLENGEQYYPRVFEAIAAAQEEILLETFILFEDKVGKQLHAALLAAAQRGVKVEVLVDG
YGSPDLSDEFVNELTAAGVRFRYFDPRPRLLGMRTNLFRRMHRKIVVIDGRIAFVGGINYSADHLSDYGP
EAKQDYAVEVEGPVVADIHQFELEALPGQSAARRWWRRHHRAEENRQPGEAQALLVWRDNEEHRDDIERH
YLKALRQARREVIIANAYFFPGYRLLRALRNAARRGVRVRLILQGEPDMPIVRVGARLLYNYLLKGGVQI
YEYCRRPLHGKVALMDDHWATVGSSNLDPLSLSLNLEANLIIRDRAFNQTLRDNLNGLIAADCQQVDETM
LPKRTWWRLTKSVLAFHFLRHFPALAGWLPAHTPRLAQVDPPAQPTMETQDRVETENTGVK
>gnl|CDD|183063 PRK11264, PRK11264, putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTA
RSLSQQKGLIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETS
YPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDV
ADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLEKFLLQ
>gnl|CDD|183064 PRK11267, PRK11267, biopolymer transport protein ExbD; Provisional
MAMHLNENLDDNGEMHEINVTPFIDVMLVLLIIFMVAAPLATVDVKVNLPASTSTPQPRPEKPVYLSVKA
DNSMFIGNDPVTDETMITALDALTEGKKDTTIFFRADKTVDYETLMKVMDTLHQAGYLKIGLVGEETAKA
K
>gnl|CDD|183065 PRK11268, pstA, phosphate ABC transporter permease PstA
MATVEMQNTAALAESRRKMQARRRLKNRIALTLSMATMAFGLFWLIWILMSTITLGIDGMSLALFTEMTP
PPNTAGGGLANAIAGSGLLILWATVVGTPLGIMAGIYLAEYGRKSWLAEVIRFINDILLSAPSIVVGLFV
YTIVVAQMEHFSGWAGVIALALLQIPIVIRTTENMLKLVPDSLREAAYALGTPKWKMISAITLKASVSGI
MTGVLLAIARIAGETAPLLFTALSNQFWSTDMMQPIANLPVTIFKFAMSPFAEWQQLAWAGVLLITLCVL
LLNILARVVFAKKKH
>gnl|CDD|183066 PRK11269, PRK11269, glyoxylate carboligase; Provisional
MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATAGNIG
VCIGTSGPAGTDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVP
RVFQQAFHLMRSGRPGPVLIDLPFDVQVAEIEFDPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVA
GGGVINADASDLLVEFAELTGVPVIPTLMGWGAIPDDHPLMAGMVGLQTSHRYGNATLLASDFVLGIGNR
WANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPDLGIVSDAKAALELLVEVAREWKAAGRLPDRSAWVA
DCQERKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRDTCYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGP
LGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIRQAQRAFDMDY
CVQLAFENINSPELNGYGVDHVKVAEGLGCKAIRVFKPEDIAPALEQAKALMAEFRVPVVVEVILERVTN
ISMGTEIDAVNEFEELADNAADAPTAIMLLD
>gnl|CDD|183067 PRK11272, PRK11272, putative DMT superfamily transporter inner membrane protein; Provisional
MRFRQLLPLFGALFALYIIWGSTYLVIRIGVESWPPLMMAGVRFLIAGILLLAFLLLRGHPLPTLRQWLN
AALIGLLLLAVGNGMVTVAEHQNVPSGIAAVVVATVPLFTLCFSRLFGIRTRKLEWLGIAIGLAGIVLLN
SGGNLSGNPWGAILILIASASWAFGSVWSSRLPLPVGMMAGAAEMLAAGVVLLIASLLSGERLTALPTLS
GFLALGYLAVFGSIIAISAYMYLLRNVRPALATSYAYVNPVVAVLLGTGLGGETLSPIEWLALGVIVFAV
VLVTLGKYLFPA
>gnl|CDD|236889 PRK11273, glpT, glycerol-3-phosphate transporter
MLSIFKPAPHKARLPAAEIDPTYRRLRWQIFLGIFFGYAAYYLVRKNFALAMPYLVEQGFSRGDLGFALS
GISIAYGFSKFIMGSVSDRSNPRVFLPAGLILAAAVMLFMGFVPWATSSIAVMFVLLFLCGWFQGMGWPP
CGRTMVHWWSQKERGGIVSVWNCAHNVGGGLPPLLFLLGMAWFNDWHAALYMPAFAAILVALFAFAMMRD
TPQSCGLPPIEEYKNDYPDDYNEKHEQELTAKQIFMQYVLPNKLLWYIAIANVFVYLLRYGILDWSPTYL
KEVKHFALDKSSWAYFLYEYAGIPGTLLCGWMSDKVFRGNRGATGVFFMTLVTIATIVYWLNPAGNPTVD
MACMIVIGFLIYGPVMLIGLHALELAPKKAAGTAAGFTGLFGYLGGSVAASAIVGYTVDFFGWDGGFMVM
IGGSILAVILLIVVMIGEKRHHEELLQKRNGG
>gnl|CDD|236890 PRK11274, glcF, glycolate oxidase subunit GlcF
MQTNLADFIRDTPEGEEAEAILRKCVHCGFCTATCPTYQLLGDELDGPRGRIYLIKQVLEGAEVTEKTQL
HLDRCLTCRNCETTCPSGVQYGRLLDIGRKVVEEKVPRPLGERLLRWGLREVLPRPALFGPLMRLGQAVR
PLLPEALRAKVPARQPAAPWPPPRHARRVLMLEGCVQPAMSPNINAATARVLDRLGISLVVAPEAGCCGA
VRYHLNAQEGGLARMRRNIDAWWPAIEAGAEAIVMTASGCGATVKEYGHLLRDDPAYAEKAARVSALTRD
LSELLPAEPLELLALLGRPDRRVAFHPPCTLQHGQKLRGKVERLLTRLGFELTLVADSHLCCGSAGTYSL
LQPELSYQLRDNKLAALEAGKPEVIVTANIGCQTHLQSGTRTPVRHWIELVDEALAG
>gnl|CDD|183070 PRK11275, pstC, phosphate ABC transporter permease PstC
MAATKPAFNAPGKKGDIIFSALVKLAALITLLLLGGIIVSLIISSWPSIQKFGLSFLWTKEWDAPNDIYG
ALVPIYGTLVTSFIALLIAVPVSFGIALFLTELAPGWLKRPLGIAIELLAAIPSIVYGMWGLFVFAPLFA
TYFQEPVGNVLSNIPIVGALFSGPAFGIGILAAGVILAIMIIPYIAAVMRDVFEQTPVMMKESAYGIGCT
TWEVIWRIVLPFTKNGVIGGVMLGLGRALGETMAVTFIIGNTYQLDSASLYMPGNSITSALANEFAEAES
GLHTAALMELGLILFVITFIVLAASKLMIMRLAKNEGAR
>gnl|CDD|236891 PRK11278, PRK11278, NADH-quinone oxidoreductase subunit NuoF
PMKNIIRTPETHPLTWRLRDDKQPVWLDEYRSKNGYEGARKALTGMSPDEIVNQVKDAGLKGRGGAGFST
GLKWSLMPKDESMNIRYLLCNADEMEPGTYKDRLLMEQLPHLLVEGMLISAFALKAYRGYIFLRGEYIEA
AVNLRRAIAEATEAGLLGKNIMGTGFDFELFVHTGAGRYICGEETALINSLEGRRANPRSKPPFPATSGV
WGKPTCVNNVETLCNVPAILANGVEWYQNISKGKSKDAGTKLMGFSGRVKNPGLWELPFGTTAREILEDY
AGGMRDGLKFKAWQPGGAGTDFLTEAHLDLPMEFESIGKAGSRLGTALAMAVDHEINMVSLVRNLEEFFA
RESCGWCTPCRDGLPWSVKILRALERGEGQPGDIETLEQLCRFLGPGKTFCAHAPGAVEPLQSAIKYFRE
EFEAGIKQPFSNTHLINGIQPNLLKERW
>gnl|CDD|183072 PRK11280, PRK11280, hypothetical protein; Provisional
AGIGIGVAAALGVAAVASLNVFDRGPQYAQVLSATPIKETVKTPRQECRDVTVTHRRPVQDENRIAGSVL
GAVAGGVLGHQFGGGRGKDVATVAGALGGGYAGNQIQGGMQERDTYTTTQQRCKTVYDKSEKMLGYDVTY
KIGDQQGKIRMDRDPGTQIPLDKNGQLVLN
>gnl|CDD|236892 PRK11281, PRK11281, mechanosensitive channel MscK
YKRSRHFVFRAFIAFLFLLLCLSSAFARAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA
LLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNA
QNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDL
QRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLV
AQELEINLQLSQRLLKATEKLNTLTQQNLRVKNWLDRLTQSERNIKEQISVLKGSLLLSRILYQQQQALP
SADLIEGLADRIADLRLEQFEINQQRDALFQPDAYIDKLEAGHKSEVTDEVRDALLQLLDERRELLDQLN
KQLNNQLNLAINLQLNQQQLLSVSDSLQSTLTQQIFWVNSNKPMDLDWLKAFPQALKDQFKSLKITVSFS
NLWDGLFIALLLFLPLLLIAGLIRWRKKWIKARLQKLAADIGTLKRDSQLHTPKAILITLLLALPVTLIF
LAVGLILLTDAFNQSELLWSWSLKLALFWLVFATCYRVLRPNGVAERHFGMPKEQVSHFRRQIVRLSLAL
LPLLFWSVVAELSPLGLADDVIGQAVIIIALALIAFLVWPLCRESWRDKESHTLRLVVRTVLTIAPIALI
VLVVLGYYYTALRLIGRLIETLYLLIIWNLLYQTVLRGLSVAARRLAYRRALAKRQNLVKEGAEGAEPVE
EPTLALEQVNQQSLRLTDLLLFALFFVMFYWVWSDLITVFSYLDSITLWHYTTTTAGGAVVESITLGNLL
FALIILVVTYVLVRNLPGLLEVLVLSRLNLRQGTSYAITTLLTYIIIAVGAVTAFSTLGVSWDKLQWLVA
ALSVGLGFGLQEIFANFVSGLIILFERPVRIGDTVTIGTFSGTVSKIRIRATTITDFDRKEVIVPNKAFV
TERLINWSLSDTVTRVVIKVGVAYGSDLEKVRELLLQAATENPRVMKEPEPQVFFLNFGASTLDHELRLY
VRELGDRSPTVDELNRRIDRLFRENDINIAFNQLDVFLKNQKGDEVVEVKRDLKGDDPTPAVG
>gnl|CDD|236893 PRK11282, glcE, glycolate oxidase FAD binding subunit; Provisional
DDISAALLERVRQAAADGTPLRIRGGGSKDFYGRALAGEVLDTRAHRGIVSYDPTELVITARAGTPLAEL
EAALAEAGQMLPFEPPHFGGGATLGGMVAAGLSGPRRPWAGAVRDFVLGTRLINGRGEHLRFGGQVMKNV
AGYDVSRLMAGSLGTLGVLLEVSLKVLPRPRAELTLRLEMDAAEALRKLNEWGGQPLPISASCWDGGTLY
LRLSGAEGAVKAARERLGGEELDDAEAAFWQQLREQTLPFFDDGRPLWRLSLPSTAPPLDLPGEQLIDWG
GAQRWLKSDADAAAIRAAAAAAGGHATLFRAGDRAGPVFHPLPAPLLRIHRRLKQAFDPAGIFNPGRLYA
EL
>gnl|CDD|183075 PRK11283, gltP, glutamate/aspartate:proton symporter; Provisional
MKNIKFSLAWQILIALVLGILLGAYLHYHSDSRDWLVSNLLSPAGDIFIHLIKMIVVPIVISTLIVGIAG
VGDAKQLGRIGAKTIIYFEVITTVAIILGITLANVFQPGAGIDMSQLATVDISKYQSTTEEVQSHSHGLM
GTILSLIPTNIFASMAKGEMLPIIFFSVLFGLGLSSLPATHREPLVTVFRSVSETMFKVTHMVMRYAPVG
VFALIAVTVANFGFASLWPLAKLVLLVYFAILFFALVVLGIVARLCGLSIWILIRILKDELILAYSTASS
ETVLPRIIEKMEAYGAPKSITSFVVPTGYSFNLDGSTLYQSIAAIFIAQLYGIDLSIWQEIILVLTLMVT
SKGIAGVPGVSFVVLLATLGSVGIPLEGLAFIAGVDRILDMARTALNVVGNALAVLVIAKWEHKFDRKKA
LAYEREVLGKFDKTADQ
>gnl|CDD|183076 PRK11285, araH, L-arabinose transporter permease protein; Provisional
MSSVSTSGSGAAAAAPPKSRFSLWRIWDQYGMLVVFAVLFIACSLFVPNFASFINMKGLGLAISMIGMVA
CTMLFCLASGDFDLSVASVVAFAGVVTAVVINATESLWLGVAAGLLLGAAVGLVNGFVIARLKINALITT
LATMQIVRGLAYIISDGKAVGISDERFFALGYANFFGVPAPIWLTVACFVVFGFLLNKTTFGRNTLAIGG
NEEAARLAGVPVVRTKIIIFVLQGLVSALAGVILASRMTSGQPMTSIGFELIVISACVLGGVSLKGGIAK
ISGVVAGVLILGTVENAMNLLNISPFYQYVVRGLILLAAVLFDRYKQRAKRTV
>gnl|CDD|183077 PRK11288, araG, L-arabinose ABC transporter ATP-binding protein AraG
SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF
ASTTAALAAGVAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY
LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAI
TVFKDGRYVATFDDMAQVDRDQLVQAMVGREIGDIYGYRPRPLGEVRLRLDGLKGPGLREPISFSVRAGE
IVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVAD
NINISARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILL
DEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQATERQALS
LALPRTSAAVA
>gnl|CDD|236894 PRK11289, ampC, beta-lactamase/D-alanine carboxypeptidase; Provisional
KMKMMLLLLLAALLLTASASAFAAAATPQQLKDIVDRTITPLMEEQDIPGMAVAVIYNGKPYYFNYGVAD
KATGQPVTQDTLFELGSVSKTFTATLAGYAQARGELSLSDPASKYLPELKGSPFDGITLLHLATYTAGGL
PLQVPDEVKDDAQLLRYFQAWQPAYAPGTQRLYSNPSIGLFGYLAAKAMGQPFEQLMEQRLFPPLGLTHT
YINVPEAEMADYAQGYNKEGKPVRVNPGVLDAEAYGVKSTAADMLRFVQANLGPQDLDPTLQQAIQLTQT
GYFRVGDMTQGLGWEMYPYPVSLDTLLAGNSNKMALEPQPVTAITPPQPPVRAVWINKTGSTNGFGAYVA
FVPAKRLGIVMLANKNYPNPARVKAAYQILNALA
>gnl|CDD|236895 PRK11295, PRK11295, HNH nuclease family protein
MAIIPKNYARLESGYREKALKLYPWVCGRCSREFVYSNLRELTVHHIDHDHDNNPEDGSNWELLCLYCHD
HEHSKYTEADQYGSTVIAGEDAQKDVGEATYNPFADLKAMMKK
>gnl|CDD|183080 PRK11300, livG, leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE
GLPGHQIARMGVVRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRAESEALDRAATWLER
VGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLI
EHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKAYLGEA
>gnl|CDD|236896 PRK11301, livM, leucine/isoleucine/valine transporter permease subunit; Provisional
MKPMHLKNALFSALMTFVLAGPFMGLQLELDGTKLVVDTASDIRWQWIAIGTAVVFLFQLLRPALQKGLK
SVSGPKFILPAIDGSTVKQKLFLVALLVAAVAWPFFVSRGAVDIATLTLIYVILGLGLNVVVGLAGLLDL
GYVGFYAVGAYTYALLNHYYGLGFWECLPIAGLMAALFGFLLGFPVLRLRGDYLAIVTLGFGEIIRILLL
NNTEITGGPNGISQIPKPTLFGLEFSRTAREGGWDTFHEFFGLKYDPSDRVIFLYLVALLLVVLTLFVIN
RLLRMPLGRAWEALREDEIACRSLGLNPTRIKLSAFTIGAAFAGFAGTFFAARQGFVSPESFTFIESAFI
LAIVVLGGMGSQFGVILAAILLVVLPELMRDFNEYRMLMFGLLMVLMMIWRPQGLLPMTRPHLELKEQA
>gnl|CDD|183082 PRK11302, PRK11302, DNA-binding transcriptional regulator HexR; Provisional
MNMLEKIQSRLEHLSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHL
AQSLANGTPYVNRNVEEDDSVEAYTGKIFESAMASLDHARQSLDPSAINRAVDLLTQAKKISFFGLGASA
AVAHDAQNKFFRFNVPVVYFDDIVMQRMSCMNSSDGDVVVLISHTGRTKSLVELAQLARENGATVIAITS
AGSPLAREATLALTLDVPEDTDIYMPMVSRIAQLTVIDVLATGFTLRRGAKFRDNLKRVKEALKESRFDK
DLLN
>gnl|CDD|236897 PRK11303, PRK11303, catabolite repressor/activator
MKLDEIARLAGVSRTTASYVINGKAKQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPD
LENTSYARIAKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVSTSLPPEHPFYQRLQND
GLPIIALDRALDREHFTSVVSDDQDDAEMLAESLLKFPAESILLLGALPELSVSFEREQGFRQALKDDPR
EVHYLYANSFEREAGAQLFEKWLETHPMPDALFTTSYTLLQGVLDVLLERPGELPSDLAIATFGDNELLD
FLPCPVNAVAQQHRLIAERALELALAALDEPRKPKPGLTRIRRNLKRR
>gnl|CDD|236898 PRK11308, dppF, dipeptide transporter ATP-binding subunit; Provisional
SQQPLLQAIDLKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGG
ELYYQGQDLLKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAK
VGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVF
ISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATPRLNPDDRRERIKLTGELPSPL
NPPPGCAFNARCPRAFGRCRQEQPQLRDYDGRLVACFAVEQDENPQA
>gnl|CDD|183085 PRK11316, PRK11316, bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE
MKVTLPDFERAGVLVVGDVMLDRYWYGPTSRISPEAPVPVVKVNQIEERPGGAANVAMNIASLGAQARLV
GLTGIDEAARALSKLLAAVGVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPQPLLERIEQA
LPSIGALVLSDYAKGALASVQAMIQLARKAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVVGKCKDEA
ELVEKGMKLIADYDLSALLVTRSEQGMTLLQPGKAPLHLPTQAREVYDVTGAGDTVISVLAAALAAGNSL
EEACALANAAAGVVVGKLGTSTVSPIELENALRGRAETGFGVMSEEQLKLAVAQARARGEKIVMTNGCFD
ILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRMAVLAALEAVDWVVPFEEDTPQRL
IAEILPDLLVKGGDYKPEEIAGSKEVWANGGEVKVLNFEDGCSTTNIIKKIRQ
>gnl|CDD|183086 PRK11320, prpB, 2-methylisocitrate lyase; Provisional
SLHSAGARFRAALAAEKPLQIVGTINAYHALLAERAGFKAIYLSGGGVAAASLGLPDLGITTLDDVLIDV
RRITDACDLPLLVDIDTGFGGAFNIARTVKSMIKAGAAAVHIEDQVGAKRCGHRPNKEIVSQEEMVDRIK
AAVDARTDPDFVIMARTDALAVEGLDAAIERAQAYVEAGADMIFPEAMTELEMYRRFADAVKVPILANIT
EFGATPLFTTEELASAGVAMVLYPLSAFRAMNKAAENVYEAIRRDGTQKAVVDTMQTREELYEYLGYHAY
EQKLDALFAQKK
>gnl|CDD|183088 PRK11331, PRK11331, 5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
MESIQPWIEKFIKQAQQQRSQSTKDYPTSYRNLRVKLSFGYGNFTSIPWFAFLGEGQEASNGIYPVILYY
KDFDELVLAYGISDTNEPHAQWQFSSDIPKTIAEYFQATSGVYPKKYGQSYYACSQKVSQGLDYTRFASM
LDNIINDYKLIFNSGKSVIPPMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFV
ARRLAYLLTGEKAPQRVNMVQFHQSYSYEDFIQGYRPNGVGFRRKDGIFYNFCQQAKEQPEKKYVFIIDE
INRANLSKVFGEVMMLMEHDKRGENWSVPLTYSENDEERFYVPENVYIIGLMNTADRSLAVVDYALRRRF
SFIDIEPGFDTPQFRNFLLNKKAEPSFVESLCQKMNELNQEISKEATILGKGFRIGHSYFCCGLEDGTSP
DTQWLKEIVMTDIAPLLEEYFFDDPYKQQIWADKLLGDS
>gnl|CDD|183089 PRK11337, PRK11337, MurR/RpiR family transcriptional regulator
SQSEFDSALPNGIGLGPYIRMKQEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKL
GFSGFRNLRSALEDYFSQSEQVLHSELSFDDAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQA
RQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAHIMLMSAALLQEGDVVLVVSHSGRTSDVIEAVELA
KKNGAKIICITNSYHSPIAKLADYVICSTAQGSPLLGENAAARIAQLNILDAFFVSVAQLNIEQAEINLQ
KTGAAVDFFRPG
>gnl|CDD|183090 PRK11339, abgT, putative aminobenzoyl-glutamate transporter; Provisional
MSMSSIPSSSQSGKLYGWVERIGNKVPHPFLLFIYLIIVLMVTTAILSAFGVSAKNPTDGTPVVVKNLLS
VEGLHWFLPNVIKNFSGFAPLGAILALVLGAGLAERVGLLPALMVKMASHVNARYASYMVLFIAFFSHIS
SDAALVIMPPMGALIFLAVGRHPVAGLLAAIAGVGCGFTANLLIVTTDVLLSGISTEAAAAFNPQMHVSV
IDNWYFMASSVVVLTIVGGLITDKIIEPRLGQWQGNSDEKLQTLTESQRFGLRIAGVVSLLFIAAIALMV
IPENGILRDPINHTVMPSPFIKGIVPLIILFFFVVSLAYGIATRTIRRQADLPHLMIEPMKEMAGFIVMV
FPLAQFVAMFNWSNMGKFIAVGLTDILESSGLSGIPAFVGLALLSSFLCMFIASGSAIWSILAPIFVPMF
MLLGFHPAFAQILFRIADSSVLPLAPVSPFVPLFLGFLQRYKPDAKLGTYYSLVLPYPLIFLVVWLLMLL
AWYLVGLPIGPGIYPRLS
>gnl|CDD|236899 PRK11340, PRK11340, phosphodiesterase YaeI; Provisional
MMISRRRLLQAAAATIATSSGFGYMHYWEPGWFELIRHRLAFFKDNAAPFKILFLADLHYSRFVPLSLIS
DAIALGIEQKPDLILLGGDYVLFDMPLNFSAFSDVLSPLAECAPTFACFGNHDRPVGTEKNHLIGETLKS
AGITVLFNQATVIATPNRQFELVGTGDLWAGQCKPPPASEANLPRLVLAHNPDSKEVMRDEPWDLMLCGH
THGGQLRVPLVGEPFAPVEDKRYVAGLNAFGERQIYTTRGVGSLYGLRLNCRPEVTMLELV
>gnl|CDD|183092 PRK11342, mhpD, 2-keto-4-pentenoate hydratase; Provisional
MTKHTLEQLAADLRRAAEQGEAIAPLRDLIGIDNAEAAYAIQHINVQHDVAQGRRVVGRKVGLTHPKVQQ
QLGVDQPDFGTLFADMCYGDNEIIPFSRVLQPRIEAEIALVLNRDLPATDITFDELYNAIEWVLPALEVV
GSRIRDWSIQFVDTVADNASCGVYVIGGPAQRPAGLDLKNCAMKMTRNNEEVSSGRGSECLGHPLNAAVW
LARKMASLGEPLRAGDIILTGALGPMVAVNAGDRFEAHIEGIGSVAATFSSA
>gnl|CDD|183093 PRK11346, PRK11346, hypothetical protein; Provisional
MKSSTTIITAYFDIGRGDWTANKGFREKLARSVDVYFSYFERLAALENEMIIFTSPDLKERVEAIRNGKP
TTVIVIDIKKKFRYIRSRIEKIQKDESFTNRLEPRQLKNPEYWSPEYVLVCNLKAYFVNKAINMGLVKTP
LVAWIDFGYCRKPNVTRGLKIWDFPFDENKMHLFTIKKGLTVTSQQQVFDFMIGNHVYIIGGAIVGSQHK
WKEFYKLVLESQKITLNNNIVDDDQGIFVMCYYKRPDLFNLNYLGRGKWFDLFRCFRSNTLGAKMQALRI
FLSRK
>gnl|CDD|183094 PRK11347, PRK11347, antitoxin ChpS; Provisional
MRITIKRWGNSAGMVIPNIVMKELNLQPGQSVEAQVSNNQLILTPISRRYSLDELLAQCDMNAAELSEQD
VWGKSTPAGDEIW
>gnl|CDD|183095 PRK11352, PRK11352, formaldehyde-responsive transcriptional repressor FrmR
MPSTPEEKKKVLTRVRRIRGQIDALERSLEGDAECRAILQQIAAVRGAANGLMAEVLESHIRETFDRNDC
YSREVSQSVDDTIELVRAYLK
>gnl|CDD|236900 PRK11354, kil, FtsZ inhibitor protein; Reviewed
MIAHHFGTDEIPRQCVTPGDYVLHEGRTYIASANNIKKRKLYIRTLTTKTCITDCMIKVFLGRDGLPVKA
ESW
>gnl|CDD|183096 PRK11357, frlA, amino acid permease
MGSQELQRKLGFWAVLAIAVGTTVGSGIFVSVGEVAKAAGTPWLTVLAFVIGGLIVIPQMCVYAELSTAY
PENGADYVYLKNAGSRPLAFLSGWASFWANDAPSLSIMALAIVSNLGFLTPIDPLLGKFIAAGLIIAFML
LHLRSVEGGAAFQTLITIAKIIPFTIVIGLGIFWFKAENFAAPTTTAIGATGSFMALLAGISATSWSYTG
MASICYMTGEIKNPGKTMPRALIGSCLLVLVLYTLLALVISGLMPFDKLANSETPISDALTWIPALGSTA
GIFVAITAMIVILGSLSSCVMYQPRLEYAMAKDNLFFKCFGHVHPKYNTPDVSIILQGALGIFFIFVSDL
TSLLGYFTLVMCFKNTLTFGSIIWCRKRDDYKPLWRTPAFGLMTTLAIASSLILVASTFVWAPIPGLICA
VIVIATGLPAYAFWAKRSRQLNALS
>gnl|CDD|183097 PRK11359, PRK11359, cyclic-di-GMP phosphodiesterase; Provisional
MKLTDADNAADGIFFPALEQNMMGAVLINENDEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHP
EYIRHNREGGKARVEGMSRELQLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLII
AVDHLDRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQD
EFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLEGNILAAMCSSPPFHEMGEIICR
NIESVLNESHVSLFALRNGMPIHWASSSHGAEYQNAQSWSATIRQRDGAPAGTLQIKTSSGAETSAFIER
VADISQHLAALALEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDS
LGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFP
LTLSIGISYDVGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLV
YQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIP
ALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFG
TGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHC
RVIQGYFFSRPLPAEEIPGWMSSVLPLKI
>gnl|CDD|236901 PRK11360, PRK11360, two-component system sensor histidine kinase AtoS
IYPRSFRNQLILLVILLVIVPTLLIGYILETEGRSAVLSEKEKKLSAVVNLLDQALGGRFDLYLASQGVA
DLPREEKIRALNAELAPVTENITHAYPGIGAGYYSKELDAIITYGPSALYQENVGVRIKADHPGREVMRT
NTPLVESGGQVRGGILNSMIPIERNGEVIGYIWANELTEDIRRQAWKMDRRIYAVLAAGLVIGLLLIFLL
SRRFSANVDIIKDGLSTLENDLSTRLPPLPGELGEISQAINNLAQALRETRSLNELILESIADGVIAIDR
QGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFASPLLDTLEHGTEHVDLEISFPGRDRTIELSVS
TSLLHNTHGEMIGALVIFSDLTERKRLQRRVARQERLAALGELVAGVAHEIRNPLTAIRGYVQIWRQQTS
DPPSQEYLSVVLREVDRLNKVIDQLLEFSRPRESQWQPVSLNALVEEVLQLFQTAGVQARVDFETELDNE
LPPIWADPELLKQVLLNILINAVQAISARGKIRIRTWQYSDGQVAVSIEDNGCGIDPELLKKIFDPFFTT
KAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQGNQ
>gnl|CDD|183099 PRK11361, PRK11361, acetoacetate metabolism transcriptional regulator AtoC
MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEM
RSHETRTPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSW
QWGHILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLL
ESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIR
IIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLLANHFLQKFSSENQRDIIDIDPMAM
SLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEVKTAPVGERNLKEEIKRVEKR
IIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID
>gnl|CDD|183100 PRK11365, ssuC, aliphatic sulfonate ABC transporter permease SsuC
MATPVKKWLLRVAPWFLPVGIVAVWQLASSVGWLSTRILPSPEGVVTAFWTLSASGELWQHLAISSWRAL
IGFSIGGSLGLILGLISGLSRWGERLLDTSIQMLRNVPHLALIPLVILWFGIDESAKIFLVALGTLFPIY
INTWHGIRNIDRGLVEMARSYGLSGIPLFIHVILPGALPSIMVGVRFALGLMWLTLIVAETISANSGIGY
LAMNAREFLQTDVVVVAIILYALLGKLADVSAQLLERLWLRWNPAYHLKEATV
>gnl|CDD|183101 PRK11366, puuD, gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
MENIMNNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGS
PSNVQPHLYGENGDEPDADPGRDLLSMALINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLE
HREDPELPVEQQYAPSHEVQVEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSV
INHPFALGVQWHPEWNSSEYALSRILFEGFITACQHHIAEKQRL
>gnl|CDD|183102 PRK11367, PRK11367, hypothetical protein; Provisional
MIRKSATGVIVALAVIWGGGTWYTGTQIQPGVEKFIKDFNDAKKKGEHAYDMTLSYKNFDKGFFNSRFQM
QMTFDNGAPDLNIKPGQKVVFDVDVEHGPLPITMLMHGNVIPALAAAKVNLVNNELTQPLFIAAKNKSPV
EATLRFAFGGSFSTTLDVAPAEYGKFSFGEGQFTFNGDGSSLSNLDIEGKVEDIVLQLSPMNKVTAKSFT
IDSLARLEEKKFPVGESESKFNQINIINHGEDVAQIDAFVAKTRLDRVKDKDYINVNLTYELDKLTKGNQ
QLGSGEWSLIAESIDPSAVRQFIIQYNIAMQKQLAAHPELANDEVALQEVNAALFKEYLPLLQKSEPTIK
QPVRWKNALGELNANLDISIADPAKSSSSTNKDIKSLNFDVKLPLNVVTETAKQLNLSEGMDAEKAQKRA
DKQISGMMTLGQMFQLITIDNNTASLQLRYTPGKVVFNGQEMSEEEFMSRAGRFVH
>gnl|CDD|183103 PRK11370, PRK11370, YciI family protein
MLYVIYAQDVPNSLEKRLSVRPAHLARLQLLQDEGRLLTAGPMPAIDSNDPGEAGFTGSTVIAEFESLEA
AQAWADADPYVAAGVYARVIVKPFKKVLP
>gnl|CDD|183104 PRK11371, PRK11371, hypothetical protein; Provisional
MLRIFIPTSNGKISRRRYIFSFILINFIFAFLIIFFNDGEAGFLVIVSTILLHYLVINMNCQRLRDSGFI
YIKTYVFGTLAVYIISIITMIAEDFACSGNGSMIFLICYFSTFSMLMLAPTDSSKQ
>gnl|CDD|236902 PRK11372, PRK11372, C-type lysozyme inhibitor
MSMKKLLIICLPVLLTGCSAYNQFVERMQTDTLEYQCDEKPLTVKLNNPRQEVSFVYDNQLLHLKQGISA
SGARYTDGIYVFWSKGDEATVYKRDRIVLNNCQLQNPKR
>gnl|CDD|183106 PRK11375, PRK11375, putative allantoin permease
MEHQRKLFQQRGYSEDLLPKTQSQRTWKTFNYFTLWMGSVHNVPNYVMVGGFFILGLSTFSIMLAIILSA
FFIAAVMVLNGAAGSKYGVPFAMILRASYGVRGALFPGLLRGGIAAIMWFGLQCYAGSLALLILIGKIWP
GFLTLGGDFTLLGLSLPGLITFLIFWLVNVGIGFGGGKVLNKFTAILNPCIYIVFGGMAIWAISLVGIGP
IFDYIPSGIQKAENSGFLFLVVINAVVAVWAAPAVSASDFTQNAHSFRAQALGQTLGLVVAYILFAVASV
CIIAGASIHYGADTWNVLDIVQRWDSLFASFFAVLVILMTTISTNATGNIIPAGYQIAALAPTKLTYKNG
VLIASIISLLICPWKLMENQDSIYLFLDIIGGMLGPVIGVMMAHYFVVMRGQINLDELYTAPGDYKYYDN
GFNLTAFSVTLVAVILSLGGKFIPFMEPLSRVSWFVGVIVAFVAYALLKKRTTAEKTGEQKTIG
>gnl|CDD|183107 PRK11376, hlyE, hemolysin HlyE
MTEIVADKTVEVVKNAIETADGALDLYNKYLDQVIPWQTFDETIKELSRFKQEYSQAASVLVGDIKTLLM
DSQDKYFEATQTVYEWCGVATQLLAAYILLFDEYNEKKASAQKDILIKVLDDGITKLNEAQKSLLVSSQS
FNNASGKLLALDSQLTNDFSEKSSYFQSQVDKIRKEAYAGAAAGVVAGPFGLIISYSIAAGVVEGKLIPE
LKNKLKSVQNFFTTLSNTVKQANKDIDAAKLKLTTEIAAIGEIKTETETTRFYVDYDDLMLSLLKEAAKK
MINTCNEYQKRHGKKTLFEVPEV
>gnl|CDD|183108 PRK11377, PRK11377, dihydroxyacetone kinase subunit M; Provisional
MVNLVIVSHSARLGEGVGELARQMLMSDGCKLAIAAGIDDPQNPIGTDAVKVMEAIESVADADHVLVMMD
MGSALLSAETALELLDPEIAAKVRLCAAPLVEGTLAATVSAASGADIDKVIFDAMHALEAKREQLGLPSS
DTEISDTCPAYDEEARSLSVVIKNRNGLHVRPASRLVYTLSTFNADMLLEKNGKCVTPESLNQIALLQVR
YNDTLRLIAKGPEAEEALIAFRQLAEDNFGETEEVAPPTLRPVPSPVSGKAFYYQPVLCTVQAKSTLTVE
EEQERLRQAIDFTLLDLMTLTAKAEASGLDDIAAIFSGHHTLLDDPELLAAASERLQHEHCTAEYAWQQV
LKELSQQYQQLDDEYLQARYIDVDDLLHRTLVHLTQTKEELPQFNSPTILLAENIYPSTVLQLDPAVVKG
ICLSAGSPLSHSAIIARELGIGWICQQGEKLYAIQPEETLTLDVKTQRLNRQG
>gnl|CDD|183109 PRK11379, PRK11379, putative outer membrane porin protein; Provisional
VAMAVICLTAASGLTSAYAAQLADDEAGLRIRLKNELRRADKPSAGAGRDIYAWVQGGLLDFNSGYYSDI
IGVEGGAYYVYKLGARADMSTRWYLDGHDSFGFALGAVKIKPSENSLLKLGRFGTDYSYGSLPYRIPLIA
GSSQRTLPTVSEGALGYWALTPNIDLWGMWRSRVFLWTDSTTGIRDEGVYNSQTGKYDKHRARSFLAASW
HDDTSRYSLGASVQKDVSNQIQSILEKTIPLDPNYTLKGELLGFYAQLEGLSRNTSQPNETALVSGQLTW
NAPWGSVFGSGGYLRHAMNGAVVDTDIGYPFSLSLDRNREGMQSWQLGVNYRLTPQFTLTFAPIVTRGYE
SSKRDVRIEGAGILGGMNYRVSEGPLQGMNFFLAADKGREKRDGSALGDRLNYWDVKMSIQYDFMLK
>gnl|CDD|236903 PRK11380, PRK11380, hypothetical protein; Provisional
MKKVLLQNHPGSEKYPVNGWEIFNSNFERMIKENKAMLLCKWGFYLTCVVAVMFVFAAITSNGLNERGYL
LLITAGCSFLYLLIMLGLIVRAGFKKAKKEQLRYYQAKGIEPLSEEKRQALQLIAVYRFYHGQWSETLEF
WPRKPRPGKDTFQYHVLPFDSIDIISKRRESLEDDWGIEDSEGYCALMEHLLSGDHGANTFKANMEEAPE
QMIALLAKLAVFPSDYISDCANHSSGKSPAKLIWAADLSWMISLSRTAFQAGTIEEELAWHYILLASRKA
HELFESEEDFYKNSRMGFLYWSNCCYRRKLTDAELEACYRYDKQFWEHYSKKCRWPIANVPWGASSVKYS
VLR
>gnl|CDD|183111 PRK11382, frlB, fructoselysine 6-phosphate deglycase
MLDIDKSTVDFLVTENMVQEVEKVLSHDVPLVHAIVEEMVKRDIDRIYFVACGSPLNAAQTAKHLADRFS
DLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIKALELGRACGALTAAFTKRADSPITSAAEFS
IDYQADCIWEIHLLLCYSVVLEMITRLAPNAEIGKIKNDLKQLPNALGHLVRTWEEKGRQLGELASQWPM
IYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHTTERAINF
VKQRTDNVIVIDYAEISQGLHPWLAPFLMFVPMEWLCYYLSIYKDHNPDERRYYGGLVEY
>gnl|CDD|105206 PRK11383, PRK11383, YiaB family inner membrane protein
MDNKISTYSPAFSIVSWIALVGGIVTYLLGLWNAEMQLNEKGYYFAVLVLGLFSAASYQKTVRDKYEGIP
TTSIYYMTCLTVFIISVALLMVGLWNATLLLSEKGFYGLAFFLSLFGAVAVQKNIRDAGINPPKETQVTQ
EEYSE
>gnl|CDD|183112 PRK11385, PRK11385, fimbrial chaperone
MTNTWNRLALLIFAVLSLLVAGELQAGVVVGGTRFIFPADRESISILLTNTSQESWLINSKINRPTRWAG
GEASTVPAPLLAAPPLILLKPGTTGTLRLLRTESDILPVDRETLFELSIASVPSGKVENQSVKVAMRSVF
KLFWRPEGLPGDPLEAYQQLRWTRNSQGVQLTNPTPYYINLIQVSVNGKALSNAGVVPPKSQRQTSWCQA
IAPCHVAWRAINDYGGLSAKKEQNLP
>gnl|CDD|236904 PRK11387, PRK11387, S-methylmethionine permease
MPEPTSQQAGQFKRTMKVRHLVMLSLGGVIGTGLFFNTGYIISTTGAAGTLLAYLIGALVVYLVMQCLGE
LSVAMPETGAFHVYAARYLGPATGYTVAWLYWLTWTVALGSSLTAAGFCMQYWFPQVPVWPWCLLFCALI
FGLNVVSTRFFAEGEFWFSLIKVVTILAFIVLGGAAIFGFIPMQDGSPAPGLRNLTAEGWFPHGGLPILM
TMVAVNFAFSGTELIGIAAGETENPAKVIPVAIRTTIARLVIFFVGTVLVLAALIPMQQAGVEKSPFVLV
FEKVGIPYAADIFNFVILTAILSAANSGLYASGRMLWSLSNEGTLPACFARLTKRGIPLTALSVSMLGGL
LALFSSVVAPDTVFVALSAISGFAVVAVWLSICASHFMFRRRHLRDGKALSELAYRAPWYPLTPILGFVL
CLLACVGLAFDPSQRIALWCGIPFVALCYGAYYLTQRLKRNMTQEARHVAE
>gnl|CDD|183114 PRK11388, PRK11388, DNA-binding transcriptional regulator DhaR; Provisional
MSGAFNNDGRGISPLIATSWERCNKLMKRETWNVPHQAQGVTFASIYRRKKALLTLGQAALEDAWEYMAD
RECALLILDETGCILSRNGDPQTLQQLSALGFNDGTYCAEGIIGTNALSLAAISGQPVKTMGDQHFKQAL
HNWAFCATPVFDSKGRLTGTIALACPVEQTSAADLPLTLSIAREVGNLLLTDSLLAESNRHLNQLNALLE
SMDDGVIAWDEQGNLQFLNAQAARLLRLDATASQGRAITELLTLPAVLQQAIKQAHPLKHVEVTFESQGQ
FIDAVITLKPIIEGQGTSFILLLHPVEQMRQLMTSQLGKVSHTFDHMPQDSPQMRRLIHFGRQAAKSSFP
VLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLGSDRTDSENGRLSKFELAHGGTL
FLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQLYYALHAFEI
TIPPLRMRREDIPALVNNKLRSLEKRFSTRLKIDDDALARLVSYRWPGNDFELRSVIENLALSSDNGRIR
LSDLPEHLFTEQATDDVSATRLSTSLSLAELEKEAIINAAQVCGGRIQEMAALLGIGRTTLWRKMKQHGI
DAGQFKRR
>gnl|CDD|138553 PRK11391, etp, phosphotyrosine-protein phosphatase; Provisional
KFNSILVVCTGNICRSPIGERLLRKRLPGVKVKSAGVHGLVKHPADATAADVAANHGVSLEGHAGRKLTA
EMARNYDLILAMESEHIAQVTAIAPEVRGKTMLFGQWLEQKEIPDPYRKSQDAFEHVYGMLERASQEWAK
RLSR
>gnl|CDD|183115 PRK11394, PRK11394, 23S rRNA pseudouridine(2457) synthase RluE
MRQFIISENTMQKTSFRNHQVKRFSSQRSTRRKPENQPTRVILFNKPYDVLPQFTDEAGRKTLKEFIPVQ
GVYAAGRLDRDSEGLLVLTNNGALQARLTQPGKRTGKIYYVQVEGIPTQDALEALRNGVTLNDGPTLPAG
AELVDEPAWLWPRNPPIRERKSIPTSWLKITLYEGRNRQVRRMTAHVGFPTLRLIRYAMGDYSLDNLANG
EWREATD
>gnl|CDD|236905 PRK11396, PRK11396, environmental stress-induced protein Ves
MEYFDMRKMSVNLWRNAAGETREICTFPPAKRDFYWRASIASIAANGEFSLFPGMERIVTLLEGGEMFLE
SADRFNHTLKPLQPFAFAADQVVKAKLTAGQMSMDFNIMTRLDVCKAKVRIAERTFTTFGSRGGVVFVIN
GAWQLGDKLLTTDQGACWFDGRHTLRLLQPQGKLLFSEINWLAGHSPDQVQ
>gnl|CDD|183117 PRK11397, dacD, serine-type D-Ala-D-Ala carboxypeptidase DacD
LKRRLIIAASLFAFNLSSAFAAENIPFSPQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTG
YVVDRAIDSHRITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADY
IAGGQRQFVEMMNNYVEKLHLKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWN
GITQQNRNGLLWDKTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQ
NFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLPKAEIPHIKAKYVLDGKELEAPISAHQRVGE
IELYDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHHKA
>gnl|CDD|105214 PRK11401, PRK11401, enamine/imine deaminase
MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGD
IIKMTVFITDLNDFATINEVYKQFFDEHQATYPTRSCVQVARLPKDVKLEIEAIAVRSA
>gnl|CDD|183118 PRK11402, PRK11402, transcriptional regulator PhoB
ATDRYSHQLLYATVRQRLLDDIAQGVYQAGQQIPTENELCTQYNVSRITIRKAISDLVADGVLIRWQGKG
TFVQSQKVENALLTVSGFTDFGVSQGKATKEKVIEQERVSAAPFCEKLNIPGNSEVFHLCRVMYLDKEPL
FIDSSWIPLSRYPDFDEIYVEGSSTYQLFQERFDTRVVSDKKTIDIFAATRPEAKWLKCELGEPLFRISK
IAFDQNDKPVHVSELFCRANRVTLTIDNKRH
>gnl|CDD|183119 PRK11403, PRK11403, hypothetical protein; Provisional
MKTSKTVAKLLFVVGALVYLVGLWISCPLLSGKGYFLGVLMTATFGNYAYLRAEKLGQLDDFFIHICQLV
ALITIGLLFIGVLNAPINAYEMVIYPIAFFVCLFGQMRLFRSV
>gnl|CDD|183120 PRK11404, PRK11404, PTS fructose-like transporter subunit IIBC
ESSLRIVAITNCPAGIAHTYMVAEALEQKARSLGHTIKVETQGSSGVENRLSSEEIAAADYVILATGRGL
SGDDRARFAGKKVYEIAISQALKNIDQIFSELPTNSQLFAADSGVKLGKQEVQSGSVMSHLMAGVSAALP
FVIGGGILVALANMLVQFGLPYTDMSKGAPSFTWVVESIGYLGFTFMIPIMGAYIASSIADKPAFAPAFL
VCYLANDKALLGTQSGAGFLGAVVLGLAIGYFVFWFRKVRLGKALQPLLGSMLIPFVTLLVFGVLTYYVI
GPVMSDLMGGLLHFLNTIPPSMKFAAAFLVGAMLAFDMGGPINKTAWFFCFSLLEKHIYDWYAIVGVVAL
MPPVAAGLATFIAPKLFTRQEKEAASSAIVVGATVATEPAIPYALAAPLPMITANTLAGGITGVLVIAFG
IKRLAPGLGIFDPLIGLMSPVGSFYLVLAIGLALNISFIIVLKGLWLRRKAKAAQQELVHEH
>gnl|CDD|236906 PRK11408, PRK11408, hypothetical protein; Provisional
LPRGLADWNFGKTFDESGEGPGYLLVADDVIGGFFALNGGGLGEDVGEVYYFAPDTLKWESLELGYSEFL
GWALSGDLEDFYEDLRWEGWQEDVAKLGGDQVFSFYPFLWTKEASDIEARSRKAVPIEEHYQMNFAPKNM
FGSVD
>gnl|CDD|171099 PRK11409, PRK11409, YoeB-YefM toxin-antitoxin system antitoxin YefM
MRTISYSEARQNLSATMMKAVEDHAPILITRQNGEACVLMSLEEYNSLEETAYLLRSPANARRLMDSIDS
LKSGKGTEKDIIE
>gnl|CDD|236907 PRK11410, PRK11410, hypothetical protein; Provisional
MSAERKAKGWRVYGLVGLGAVALLAAGVWALRYAGSGPELSPLVVHNNLQLDLNEPDALIDSDSLSQLPK
DLLTVPLLRDVLTEDFVFYYENHADRLGLEGSLRRIAYEHDLTLKDKLLSSLLDQPAQVALWRDKDGRLS
HFVVVMQRNGLAKLLEPLAFVATSDSQLSKVESIKVGSEGVPVYQLRYGGGRSLLFASKGDRLLVLSSPG
MLFDDDGQDTEATAILGALLSGDKRWQASFGLEEALPAKTPVRQRIVVSARYLAFGYQRFFPSFAGLRFD
MGNDGWHSFLALNDESASASFDFAPVWNAMPAGASACVALPVDWGAAEELLSHIGAESQVAAKLGEALDG
PAGLCWYADSRLYTPLFVAQLDGAAEAALDQLLGKLFGQNIGAHEAKAPEGRLPVSQTQQGEAQIWQREV
SSRYGQYPKAQAAQPDQLSSDRFFRVSLAMQGKTLLFSLDDRLVDNALDTLNKRYPALADVLPTDGIVPL
YINPQSLAKLLRRETLASLPADLEPVFRNAAQTLLMPKLDALAQYPPYALKLAQAEPGAAWQWLPLTWQP
L
>gnl|CDD|183123 PRK11411, fecB, iron-dicitrate transporter substrate-binding subunit; Provisional
MLAFIRLLFAGLLLLSGSSHAFAVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVADDNDAK
RILPEVRAHLKPWQSVGTRSQPSLEAIAALKPDLIIADSSRHAGVYIALQKIAPTLLLKSRNETYQENLQ
SAAIIGEVLGKKREMQARIEQHKERMAQFASQLPKGTRVAFGTSREQQFNLHSPESYTGSVLAALGLNVP
KAPMNGAAMPSISLEQLLALNPDWLLVAHYRQESIVKRWQQDPLWQMLTAAKKQQVASVDSNTWARMRGI
FAAERIAKDTVKIFHHQPLTVVK
>gnl|CDD|183124 PRK11412, PRK11412, uracil/xanthine transporter
MFKFAVSRESLLSGFQWFFFIFCNTVVVPPTLLSAFQLPQSSLLTLTQYAFLATALACFAQAFCGHRRAI
MEGPGGLWWGTILTITLGEASRGTPINDIATSLAVGIALSGVVTILIGFSGLGHRLARLFTPMVMVVFML
LLGAQLTTIFFKGMLGLPFGIADPNGKIQLPPFGLSVAVMCLVLAMIIFLPQRIARYSLLVGTIVGWILW
AFCFPSSHSLSGELHWQWFPLGSGGALEPGIILTAVITGLVNISNTYGAIRGTDVFYPQQGAGNTRYRRS
FVATGFMTLITVPLAVIPFSPFVSSIGLLTQTGDYRRRSFIYGSVMCLLVALIPALTRLFCSIPLPVSSA
VMLVSYLPLLGSALVFSQQITFTARNIYRLALPLFVGIFLMALPPVYLQDLPLTLRPLLSNGLLVGILLA
VLMENLIPWERIE
>gnl|CDD|183125 PRK11413, PRK11413, putative hydratase; Provisional
MIKLSEKGVYLASGNEIIAEEHFTGEIKKEEAKKGTIAWSILSSHNTSGNMDKLKIKFDSLASHDITFVG
IIQTAKASGMERFPLPYVLTNCHNSLCAVGGTINEDDHVFGLSAAQKYGGIFVPPHIAVIHQYMREMMAG
GGKMILGSDSHTRYGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGA
VFKNGYVKNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHGRGQDYCELNPQP
MAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLTDILREVEIESERVAHGKAKLSLLDKIENGRL
KVQQGIIAGCSGGNYENVIAAANALRGQSCGNDTFSLSVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAF
CGPCFGAGDTPANNGLSIRHTTRNFPNREGSKPANGQMSAVALMDARSIAATAANGGYLTSATELDCWDN
VPEYAFDVTPYKNRVYQGFGKGATQQPLIYGPNIKDWPEMGALTDNILLKVCSKILDPVTTTDELIPSGE
TSSYRSNPLGLAEFTLSRRDPGYVGRSKAVAELENQRLAGNVSELTEVFARIKQIAGQEHIDPLQTEIGS
MVYAVKPGDGSAREQAASCQRVLGGLANIAEEYATKRYRSNVINWGMLPFQMAEEPTFEVGDYIYIPGIR
AALDNPGTTFKGYVIHEDAPVTEITLYMESLTAEEREIIKAGCLINYNKNR
>gnl|CDD|183126 PRK11414, PRK11414, GntR family transcriptional regulator
MPGTEKTQHISLTLQVENDLKHQLSIGALKPGARLITKNLAEQLGMSITPVREALLRLVSVNALSVAPAQ
AFTVPEVSKRQLDEINRIRYELELMAVALAVENLTPQDLAELQELLEKLQQAQEKGDMEQIINANRLFRL
AIYHRSNMPILCEMIEQLWVRMGPSLHYLYEAINPAELREHIENYRLLLAALKAKDKEGCRHCLAEIMQQ
NVAILYQQYNR
>gnl|CDD|183127 PRK11415, PRK11415, hypothetical protein; Provisional
MFPEYRDLISRLKNENPRFMSLFDKHNKLDHEIARKEGSDGRGYNAEVVRMKKQKLQLKDEMLKILQQES
VKEV
>gnl|CDD|236908 PRK11423, PRK11423, methylmalonyl-CoA decarboxylase; Provisional
MSMQYVNVVTINKIATITFNNPAKRNALSKVLIDDLMQALSDLNRPEIRVVILRAPSGSKVWSAGHDIHE
LPSGGRDPLSYDDPLRQILRMIQKFPKPVIAMVEGSVWGGAFELIMSCDLIIAASTSTFAMTPANLGVPY
NLSGILNFTNDAGFHIVKEMFFTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISEKAPLAIAVIK
EQLRVLGEAHPMNPDEFERIQGLRRAVYDSEDYQEGMNAFLEKRKPVFVGH
>gnl|CDD|236909 PRK11424, PRK11424, DNA-binding transcriptional activator TdcR; Provisional
MTGITIFYGDNIIRYVVNTKKGLRPYFKQLPDNYQAKFELNLMSKFSNFIINKPFSAINNAARHIFSRYL
LENKHLFYQYFKISNTGIDHLEQLINVNFFSSDRTSFCECNRFP
>gnl|CDD|183129 PRK11425, PRK11425, PTS N-acetylgalactosamine transporter subunit IIB
MPNIVLSRIDERLIHGQVGVQWVGFAGANLVLVANDEVAEDPVQQNLMEMVLAEGIAVRFWTLQKVIDNI
HRAADRQKILLVCKTPADFLTLVKGGVPVNRINVGNMHYANGKQQIAKTVSVDAGDIAAFNDLKAAGVEC
FVQGVPTEPAVDLFKLL
>gnl|CDD|183130 PRK11426, PRK11426, hypothetical protein; Provisional
MGLFDEVVGAFLKGDAGKYQAILSWVEEQGGIQVLLEKLQSGGLGAILSTWLSNQQGNQSVSGEQLESAL
GTNAVSDLGQKLGVDTSTASSLLAEQLPKIIDALSPQGEVSPQANNDLLSAGMELLKGKLFR
>gnl|CDD|183131 PRK11427, PRK11427, multidrug efflux transporter permease subunit MdtO
MSALNSLPLPVVRLLAFFHEELSERRPGRVPQTLQLWVGCLLVILISMTFEIPFLALSLAVLFYGIQSNA
FYTKFVAILFVVATVLEIGSLFLIYKWSYGYPLIRLIIAGPILMGCMFLMRTHRLGLVFFAVAIVAIYGQ
TFPAMLDYPEVVVRLTLWCIVVGLYPTLLMTLIGVLWFPSRAINQMHQALNDRLDDAISHLTDSLAPLPE
TRIEREALALQKLNVFCLADDANWRTQSAWWQSCVATVTYIYSTLNRYDATSFADSQAIIEFRQKLASEI
NKLQHAVAEGQCWQSDWRISESEAMAARECNLENICQTLLQLGQMDPNTPPTPAAKPPSMVADAFTNPDY
MRYALKTLLACLICYTFYSGVDWEGIHTCMLTCVIVANPNVGSSYQKMVLRFGGAFCGAILALLFTLLVM
PWLDNIVELLFVLAPIFLLGAWIATSSERSSYIGTQMVVTFALATLENVFGPVYDLVEIRDRALGILIGT
VVSAVIYTFVWPESEARTLPQKLAGALGMLSKVLRIPRQQEVTALRTYLQIRIGLHAAFNACEEMCQRVA
LERQLDSEERALLIERSQTVIRQGRDILHAWDATWNSAQALDNALQPDRAGQFADALEKYAAGLATALSR
SPQITLEETPASQAILPTLLKQEQHVCQLFARLPDWTAPALTPATTQAQGATQ
>gnl|CDD|183132 PRK11430, PRK11430, putative CoA-transferase; Provisional
MTNNESKGPFEGLLVIDMTHVLNGPFGTQLLCNMGARVIKVEPPGHGDDTRTFGPYVDGQSLYYSFINHG
KESVVLDLKNDHDKSIFINMLKQADVLAENFRPGTMEKLGFSWETLQEINPRLIYASSSGFGHTGPLKDA
PAYDTIIQAMSGIMMETGYPDAPPVRVGTSLADLCGGVYLFSGIVSALYGREKSQRGAHVDIAMFDATLS
FLEHGLMAYIATGKSPQRLGNRHPYMAPFDVFDTQDKPITICCGNDKLFSALCQALELTELVNDPRFSSN
ILRVQNQAILKQYIERTLKTQAAEVWLARIHEVGVPVAPLLSVAEAINLPQTQARNMLIEAGGIMMPGNP
IKISGCADPHVMPGAATLDQHGEQIRQEFSS
>gnl|CDD|171110 PRK11431, PRK11431, quaternary ammonium compound efflux SMR transporter SugE
MSWIILVIAGLLEVVWAVGLKYTHGFSRLTPSIITVTAMIVSMALLAWAMKSLPVGTAYAVWTGIGAVGA
AITGIVLLGESASPARLLSLALIVAGIIGLKLSTH
>gnl|CDD|183133 PRK11432, fbpC, ferric ABC transporter ATP-binding protein
MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV
THRSIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGG
QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVM
NKGKIMQIGSPQELYRQPASRFMASFMGDANIFPATLSGDYVDIYGYRLPRPAAFAFNLPDGECTVGVRP
EAITLSEQGEESQRCTIKHVAYMGPQYEVTVDWHGQELLLQVNATQLQPDLGEHYYLEIHPYGMFLLADA
A
>gnl|CDD|236910 PRK11433, PRK11433, aldehyde oxidoreductase 2Fe-2S subunit; Provisional
RVGMHEPHDLSLTRRDLLKVSAATAATAAAYPHSTLAASVPAATPAPEISPVTLKVNGKTEQLEVDTRTT
LLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFV
KHDGFQCGYCTPGQICSSVAVLKEIKDGIPSHVTVDLTAAPELTADEIRERMSGNICRCGAYSNILEAIE
DVAGEIA
>gnl|CDD|183135 PRK11436, PRK11436, biofilm-dependent modulation protein; Provisional
MFTYYQAENSTAEPALVNAIEQGLRAEHGVVTEDDILMELTKWVEASDNDILSDIYQQTINYVVSGQHPT
L
>gnl|CDD|236911 PRK11439, pphA, protein-serine/threonine phosphatase
MKQPAPVYQRIAGHQWRHIWLVGDIHGCFEQLMRKLRHCRFDPWRDLLISVGDLIDRGPQSLRCLQLLEE
HWVRAVRGNHEQMALDALASQQMSLWLMNGGDWFIALTDNQQKQAKTLLEKCQRLPFILEVHCRTGKHVI
AHADYPADVYEWQKDVDLHQVLWSRSRLGERQKGQGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGG
ELTLVQLQ
>gnl|CDD|183137 PRK11440, PRK11440, putative hydrolase; Provisional
MLELNAKTTALVVIDLQEGILPFAGGPHTADEVVARAARLAAKFRASGSPVVLVRVGWSADYAEALKQPV
DAPSPAKVLPENWWQHPAALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTAR
NAWELGFNLVIAEDACSAASAEQHQNSMNHIFPRIARVRSVEEILNAL
>gnl|CDD|183138 PRK11443, PRK11443, lipoprotein; Provisional
MKKFIAPLLALLLSGCQIDPYTHAPTLTSTDWYDAGMEDAISGSAVKDDDTLAEWFGDPQVDRGLYLKGY
AEGQKKTCQTDFTYARGLSGKSFPASCDNVENASQLHEVWQKGADENASTIRLN
>gnl|CDD|183139 PRK11445, PRK11445, FAD-binding protein
HYDVAIIGLGPAGSALARLLAGKMKVIAIDKKHQCGTEGFSKPCGGLLAPDAQKSFAKDGLTLPKDVIAN
PQIFAVKTIDLANSLTRNYQRSYINIDRHKFDLWLKSLIPASVEVYHNSLCRKIWREDDGYHVIFRADGW
EQHITARYLVGADGANSMVRRHLYPDHQIRKYVAIQQWFAEKHPVPFYSCIFDNEITDCYSWSISKDGYF
IFGGAYPMKDGRERFETLKEKLSAFGFQFGKPVKTEACTVLRPSRWQDFVCGKDNAFLIGEAAGFISPSS
LEGISYALDSARILSEVLNKQPEKLNTAYWRKTRKLRLKLFGKILKSPFMYNPALRKLIMRSGLASIPQL
K
>gnl|CDD|183140 PRK11447, PRK11447, cellulose synthase subunit BcsC; Provisional
MRKFTLSLLTLSLGLALLPLAQAAPTAQQQLLEQVRLGEATHREDLVRQSLYRLELIDPNNPDVIAARFR
LLLRQGDSDGAQKLLDRLSQLAPDSNAYRSSRTTMLLSTPEGRQALQQARLLATTGRTEEALASYDKLFN
GAPPELDLAVEYWRLVAKLPAQRPEAINQLQRLNADYPGNTGLRNTLALLLFSSGRRDEGFAVLEQMAKS
PAGRDAAAQLWYGQIKDMPVSDASVAALQKYLQVFSDGDSVAAARSQLAEQQKQLADPAFRARAQGLAAV
DSGQGGKAIPELQQAVRANPKDSEALGALGQAYSQQGDRARAVAQFEKALALDPHSSNRDKWESLLKVNR
YWLLIQQGDAALKANNLAQAERLYQQARQVDNTDSYAVLGLGDVAMARKDYAAAERYYQQALRMDPGNTN
AVRGLANLYRQQSPEKALAFIASLSASQRRSIDDIERSLQNDRLAQQAEALENQGKWAQAAELQRQRLAL
DPGSVWLTYRLAQDLRQAGQRSQADALMRRLAQQKPNDPEQVYAYGLYLSGSDRDRAALAHLNTLPRAQW
NSNIQELAQRLQSDQVLETANRLRDSGKEAEAEALLRQQPPSTRIDLTLADWAQQRGDYAAARAAYQRVL
TREPGNADARLGLIEVDIAQGDLAAARAQLAKLPATANDSLNTQRRVALAWAALGDTAAAQRTFNRLIPQ
AKSQPPSMESALVLRDAARFEAQTGQPQQALETYKDAMVASGITPTRPQDNDTFTRLTRNDEKDDWLKRG
VRSDAADLYRQQDLNVTLEHDYWGSSGTGGYSDLKAHTTMLQVDAPLSDGRAFFRTDRVNMDAGSFSTNA
DGKYDDNWGTCTLQDCSGNRSQSDSGASVAVGWRNDRWSWDIGTTPMGFNVVDVVGGISYSGDIGPLGYT
LNAHRRPISSSLLAFGGQKDPPSNTGTTWGGVRANGVGLSLSYDKGEANGVWASLSGDQLTGKNVADNWR
VRWMTGYYYKVINENNRRVTVGLNNMIWHYDKDLSGYSLGQGGYYSPQEYLSFAVPVMWRQRTENWSWEL
GGSVSWSHSRTKTMPRYPLMNLIPTDYQEDAADQSNDGSSSQGFGYTARALVERRLTSNWFVGTGVDIQQ
AKDYTPSHALLYVRYSAAGWQGDLDLPPQPLTPYADW
>gnl|CDD|236912 PRK11448, hsdR, type I restriction enzyme EcoKI subunit R; Provisional
MNKSNFEFLKGHDPVLAALACLAERNFYDDPNTTLIKLRQFGEALAKHIAALLGIYEPPCENQHDLLRRL
GKEGFLPDEILDVFHKLRKIGNKAVHEFHGDHREALMGLKLAFRLAVWFHRTYGKDWDFKPGPFVPPEDP
ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAET
SQERKQKRKEITDQAAKRLELSEEETRILIDQQLRKAGWEADSKTLRFSKGARPEKGRNLAIAEWPTGKT
GRADYALFIGLKPVGVVEAKRKNKDVASKLNQAKRYSKGFDVAEEVPEYGGPWQDTSGGRYKVPFVFSTN
GRPYLKQLKTKSGIWFRDVRKPTNHPRALQGWHTPEGLLDLLESDIEAANQWLADEPFDYGLGLRYYQED
AIQAVEKAIVEGQREILLAMATGTGKTRTAIALMYRLLKAKRFRRILFLVDRSALGEQAEDAFKDTKIEG
DQTFASIYDIKGLEDKFPEDETKVHVATVQGMVKRILYSDDPMDKPPVDQYDCIIVDEAHRGYTLDKEMS
EGELQFRDQLDYVSKYRRVLDYFDAVKIGLTATPALHTTEIFGEPVYTYSYREAVIDGYLIDHEPPIRIE
TRLSQEGIHFEKGEEVEVINTQTGEIDLATLEDEVDFEVEDFNRRVITESFNRVVCEELAKYLDPTGEGK
TLIFAATDAHADMVVRLLKEAFKKKYGQVEDDAVIKITGSIDKPDQLIRRFKNERLPNIVVTVDLLTTGI
DVPSICNLVFLRRVRSRILYEQMLGRATRLCPEIGKTHFRIFDAVDIYEALESVTTMKPVVVNPNISLEQ
LVNELTDADGESHAEHVREQLIAKLQRKLRKATDNAERSFEILAQLRRAGVTPEEFASRLKELGPHEAAE
WLNKHPSLIEQLDELKTINGLDDAPIISDHDDEVVSVERGYGDADKPEDYLEAFDAFVRENINQIPALQV
VVNRPRDLTRKELKELRLLLDQQGFSEASLRSAWKETKNEDIAASIIGFIRQAALGDALVPFEERVDHAM
QKIYAERDWTPVQRKWLERIAKQLKEEVVLDRDAFDTGPFKRRGGFKRLNKVFDGNLDQILDKINEYLWD
EAA
>gnl|CDD|171118 PRK11449, PRK11449, metal-dependent hydrolase
MICRFIDTHCHFDFPPFSGDEEASLQRAAQAGVGKIIVPATEAENFARVLALAERYQPLYAALGLHPGML
EKHSDVSLDQLQQALERRPAKVVAVGEIGLDLFGDDPQFERQQWLLDEQLKLAKRYDLPVILHSRRTHDK
LAMHLKRHDLPRTGVVHGFSGSLQQAERFVQLGYKIGVGGTITYPRASKTRDVIAKLPLASLLLETDAPD
MPLNGFQGQPNRPEQAARVFDVLCELRPEPADEIAEVLLNNTYTLFNV
>gnl|CDD|183142 PRK11453, PRK11453, O-acetylserine/cysteine exporter
MSRKDGVLALLVVVVWGLNFVVIKVGLHNMPPLMLAGLRFMLVAFPAIFFVARPKVPLNLLLGYGLTISF
GQFAFLFCAINFGMPAGLASLVLQAQAFFTIVLGAFTFGERLQGKQLAGIALAIFGVLVLIEDSLNGQHV
AMLGFMLTLAAAFSWACGNIFNKKIMSHSTRPAVMSLVVWSALIPIIPFFVASLILDGSATMIHSLVTID
MTTILSLMYLAFVATIVGYGIWGTLLGRYETWRVAPLSLLVPVVGLASAALLLDERLTGLQFLGAVLIMA
GLYINVFGLRWRKAVKVRG
>gnl|CDD|183143 PRK11459, PRK11459, multidrug resistance outer membrane protein MdtQ; Provisional
MNRDSFYPAIACLPLLIMLAGCAPMHETRQALSQQTPAAHVDTALPTALKNGWPDSQWWKAYHDNQLDSL
INNALQNAPDMQVAEQRIQLAEAQAKAVAAQDGPQLDFSADMERQKMSAEGLMGPFALNDPAAGTTGPWY
TNGTFGLTAGWDLDLWGKNRAEVTARIGTVKARAAEREQTRQLLAGSVARLYWEWQTQAALNTVLQQIEK
EQNNIIATDRQLYQNGITSSVEGVETDINASKTRQQLNDVAGKMKIIEARLSALTNTQTKSLKLKPVALP
KVASQLPDELGYSLLARRADLQAAHWYIESSLSTIDAAKAAFYPDINLMAFLQQDALHLSDLFRHSAQQM
GVTAGLTLPIFDSGRLNANLDIAKAQSNLSIASYNKAVVDAVNDVARAASQVETLAEKNQHQQQIERDAL
RVVGLAQARFNAGIIAGSRVSEAKIPALRERANGLLLQGQWLDASIQLTSALGGGYHR
>gnl|CDD|183144 PRK11460, PRK11460, putative hydrolase; Provisional
MKHDHFVVQSPDKPAQQLLLLFHGVGDNPVAMGEIGSWFAPAFPDALVVSVGGPEPSGNGAGRQWFSVQG
ITEDNRQARVAAIMPTFIETVRYWQQQSGVGASATALIGFSQGAIMALEAVKAEPGLAGRVIAFSGRYAS
LPETAPTATTIHLIHGGEDPVIDVAHAVAAQEALISLGGDVTLDIVEDLGHAIDPRLMQFALDRLRYTVP
KRYWDEALSGGKPGDDDVIEMM
>gnl|CDD|183145 PRK11462, PRK11462, putative transporter; Provisional
MKSEVLSVKEKIGYGMGDAASHIIFDNVMLYMMFFYTDIFGIPAGFVGTMFLVARALDAISDPCMGLLAD
RTRSRWGKFRPWVLFGALPFGIVCVLAYSTPDLSMNGKMIYAAITYTLLTLLYTVVNIPYCALGGVITND
PTQRISLQSWRFVLATAGGMLSTVLMMPLVNLIGGDNKPLGFQGGIAVLSVVAFMMLAFCFFTTKERVEA
PPTTTSMREDLRDIWQNDQWRIVGLLTIFNILAVCVRGGAMMYYVTWILGTPEVFVAFLTTYCVGNLIGS
ALAKPLTDWKCKVTIFWWTNALLAVISLAMFFVPMQASITMFVFIFVIGVLHQLVTPIQWVMMSDTVDYG
EWCNGKRLTGISFAGTLFVLKLGLAFGGALIGWMLAYGGYDAAEKAQNSATISIIIALFTIVPAICYLLS
AIIAKRYYSLTTHNLKTVMEQLAQGKRRCQQQFTSQEVQN
>gnl|CDD|236913 PRK11463, fxsA, phage T7 F exclusion suppressor FxsA; Reviewed
MRPFLLLFLLYPLIEIAVFIAVASVIGVGWTLLLVILTSVLGVLLARSQGFKTLLRAQRKLARGELPAAE
LLDGLLLAVAGVLLLLPGFVTDILGLLLLLPPTRALLRPKLMKRLRRKRNFNGGFSAPGGGGDVIDGEYE
RKDDPDDR
>gnl|CDD|183147 PRK11465, PRK11465, putative mechanosensitive channel protein; Provisional
MRWILFILFCLLGAPAHAVSIPGVTTTTSTDSTTEPAPEPDIEQKKAAYAALADVLDNDTSRKELIDQLR
TAAATPPAEPVPKIVPPTLVEEKTVLQNVTEVSRHYGEALSARFGQLYRNITGSPHKPFNPQTFSNALTH
FLMLAVLVFGFYWLIRLCALPLYRKMGQWARQKNRERSNWLQLPAMIIGAFIIDLLLLALTLFVGQLLSD
NLNAGSRTIAFQQSLFLNAFALIEFFKAILRLIFCPNVPELRPFTIQDASARYWNRRLSWLSSLIGYGLI
VAVPIISNQVNVQVGALANVIIMLCMTVWALYLIFRNKKEITQHLLNLAERSLAFFSLFIRAFALVWHWL
ASAYFIVLFFFSLFDPGNSLKFMMGATVRSLAIIGIAAFVSGMFTRWIAKTITLSPHTQRNYPELQKRLN
GWLSAALKTARILTVCVAVMLLLNAWGLFDFWNWLQNGAGEKTVDILIRIALILFFSAVGWTVLASLIEN
RLASDIHGRPLPSARTRTLLTLFRNALAVIISTITIMIVLSEIGVNIAPLLAGAGALGLAISFGSQTLVK
DIITGVFIQFENGMNTGDLVTIGPLTGTVERMSIRSVGVRQDTGAYHIIPWSSITTFANFVRGIGSVVAN
YDVDRHEDADKANQALKDAVAELMENEEIRGLIIGEPNFAGIVGLTNTAFTLRVSFTTLPLKQWTVRFAL
DSQVKKHFDLAGVRAPVQTYQVLPAPGATPAEPLPPGEPTL
>gnl|CDD|236914 PRK11466, PRK11466, hybrid sensory histidine kinase TorS; Provisional
MNLTLTRRLWMGFALMALLTLTSTLVGWYNLRFISQVEKDNTQALIPTMNMARQLSEASAWELFAAQNLT
SADNEKMWQAQGRMLTAQSLKINALLQALREQGFDTTAIEQQEQEISRSLRQQGELVGQRLQLRQQQQQL
SQQIVAAADEIARLAQGQANNAATSAGATQAGIYDLIEQDQRQAAESALDRLIDIDLEYVNQMNELRLSA
LRVQQMVMNLGLEQIQKNAPTLEKQLNNAVKILQRRQIRIEDPGVRAQVATTLTTVSQYSDLLALYQQDS
EISNHLQTLAQNNIAQFAQFSSEVSQLVDTIELRNQHGLAHLEKASARGQYSLLLLGMVSLCALILILWR
VVYRSVTRPLAEQTQALQRLLDGDIDSPFPETAGVRELDTIGRLMDAFRSNVHALNRHREQLAAQVKART
AELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGE
SLLTILNDILDYSAIEAGGKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPR
RIRQVITNLLSNALRFTDEGSIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKRGGTGLGL
TISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITAEM
LNTSGAQVVAVGNAAQALETLQNSEPFAAALVDFDLPDYDGITLARQLAQQYPSLVLIGFSAHVIDETLR
QRTSSLFRGIIPKPVPREVLGQLLAHYLQLQVNNDQPLDVSQLNEDAALMGTEKIHEWLALFKQHALPLL
DEIDIARASQDSEKIKRAAHQLKSSCSSLGMRQASQACAQLEQQPLSAPLPHEEITRSVAALEAWLAKKD
LNAI
>gnl|CDD|183149 PRK11467, PRK11467, secY/secA suppressor protein; Provisional
MTMYATLEEAIDAAREEFLADNPGIDAEDANVQQFNLQKYVLQDGDIMWQVEFFADEGEEGECLPMLSGE
AAQSVFDGDYDEIEIRQEWQEENTLHEWDEGEFQLEPPLDTEEGRAAADEWDER
>gnl|CDD|183150 PRK11468, PRK11468, dihydroxyacetone kinase subunit DhaK; Provisional
MKKLINDVEDVLDEQLAGLAKAHPELTLHQDPVYVTRADAPVAGKVALLSGGGSGHEPMHCGFVGQGMLD
GACPGEIFTSPTPDQMFECAMQVDGGEGVLLIIKNYTGDVLNFETATELLHDSGVKVTTVLIDDDVAVKD
SLYTAGRRGVANTVLIEKLVGAAAERGYSLDQCAELGRKLNNQGHSIGIALGACTVPAAGKPSFTLADNE
MEFGVGIHGEPGIDRRPFSSLDQTVDEMFDTLLENGSYHRTLRFWDRQQGSWQEEEQTKQPLQSGDRVIA
LVNNLGATPLSELYGVYNRLATRCEQAGLTIERNLIGAYCTSLDMQGFSITLLKVDDETLALWDAPVHTP
ALRWGK
>gnl|CDD|183151 PRK11469, PRK11469, manganese efflux pump MntP
MNITATVLLAFGMSMDAFAASIGKGATLHKPKFSEALRTGLIFGAVETLTPLIGWGMGMLASRFVLEWNH
WIAFVLLIFLGGRMIIEGFRGADDEDEEPRRRHGFWLLVTTAIATSLDAMAVGVGLAFLQVNIIATALAI
GCATLIMSTLGMMVGRFIGSIIGKKAEILGGLVLIGIGVQILWTHFHG
>gnl|CDD|183152 PRK11470, PRK11470, YebB family permuted papain-like enzyme
MNINYPAEYEIGDIVFTCIGAALFGQISAASNCWSNHVGIIIGHNGEDFLVAESRVPLSTVTTLSRFIKR
SANQRYAIKRLDAGLTEQQKQRIVEQVPSRLRKLYHTGFKYESSRQFCSKFVFDIYKEALCIPVGEIETF
GELLNSNPDAKLTFWKFWFLGSIPWERKTVTPASLWHHPGLVLIHAEGVETPQPELTEAV
>gnl|CDD|236915 PRK11475, PRK11475, DNA-binding transcriptional activator BglJ; Provisional
MSSIGIESLFRKFPGNPYKLHTFSSQSSFQDAMSRISFSAVIFSLSAMRSERREGLSCLTELAIKFPRMR
RLVIADDDIEARLIGSLSPSPLDGVLSKASTLEILQQELFLSLNGVRQATDRLNNQWYINQSRMLSPTER
EILRFMSRGYSMPQIAEQLERNIKTIRAHKFNVMSKLGVSSDAGLLDAADILLCLRHCEASNVLHPV
>gnl|CDD|183154 PRK11476, PRK11476, carnitine metabolism transcriptional regulator CaiF
MAENRWVIAREISIHFDIEHCKAINTLSYILSEVTEISCEVKMIPNQLEGRGCQCQRLVKVVDIDEQIYA
RLRNNSREKLVGVRKTPRIPAVPPTELNREQKWQMMLSKSMRR
>gnl|CDD|183155 PRK11477, PRK11477, CdaR family transcriptional regulator
MAGWHLDTKMAQDIVARTMRIIDTNINVMDARGRIIGSGDRERIGELHEGALLVLSQGRVVDIDDAVARH
LHGVRQGINLPLRLEGEIVGVIGLTGEPENLRKYGELVCMTAEMMLEQSRLMHLLAQDSRLREELVMNLI
QAEENTPALTEWAQRLGIDLNQPRVAAVVEVDSGQLGVDSAMAELQQLQNALTTPERNNLVAIVSLTEMV
VLKPALNSFGRWDAEDHRKRVEQLISRMKEYGQLRFRVALGNYFTGPGSIARSYRTAKTTMVVGKQRMPE
SRCYFYQDLMLPVLLDSLRGGWQANELARPLARLKAMDNNGLLRRTLAAWFRHNVQPLATSKALFIHRNT
LEYRLNRISELTGLDLGNFDDRLLLYVALQLDEER
>gnl|CDD|183156 PRK11478, PRK11478, VOC family protein
MLGLKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALNGQYVIELFSFPFPPERPSR
PEACGLRHLAFSVDDIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYEQ
>gnl|CDD|183157 PRK11479, PRK11479, YaeF family permuted papain-like enzyme
MDKPKAYCRLLLPWLLLLSACTVDVSQPDKSATAVNAEAKTWAVKFQHQSSFTEQGIKEITAPDLKPGDL
LFSSSLGVTSFGIRVFSTSSVSHVAIYLGENNVAEATGAGVQIVSLKKAIKHSDKLFALRVPDLTPQQAT
KITAFANKIKDSGYNYRGIVEFIPFMVTRQMCSLNPFSEDFRQQCVSGLAKAQLGSVGEGDKKSWFCSEF
VTEAFAKAGHPLTLAQSGWISPADLLHMREGDVSAFKPETQLQYVGHLKPGIYIKAGRFVGLTQ
>gnl|CDD|183158 PRK11480, tauA, taurine transporter substrate binding subunit; Provisional
MAISSRNTLLAALAFIAFQAQAVNVTVAYQTSAEPAKVAQADNTFAKESGATVDWRKFDSGASIVRALAS
GDVQIGNLGSSPLAVAASQQVPIEVFLLASKLGNSEALVVKKTISKPEDLIGKRIAVPFISTTHYSLLAA
LKHWGIKPGQVEIVNLQPPAIIAAWQRGDIDGAYVWAPAVNALEKDGKVLTDSEQVGQWGAPTLDVWVVR
KDFAEKHPEVVKAFAKSAIDAQQPYIANPDAWLKQPENISKLARLSGVPEGDVPGLVKGNTYLTPQQQTA
ELTGPVNKAIIDTAQFLKEQGKVPAVANDYSQYVTSRFVQ
>gnl|CDD|183159 PRK11482, PRK11482, DNA-binding transcriptional regulator
MDDNNQPERCLARQSSEDKPQIFRTLRNIDLNLLTIFEAVYVHKGIVNAAKILNLTPSAISQSIQKLRVI
FPDPLFIRKGQGVTPTAYATHLHEYISQGLESILGALDITGSYDKQRTITIATTPSVGALVMPVIYQAIK
THYPQLLLRNIPISDAENQLSQFQTDLIIDTHSCSNRTIQHHVLFTDNVVLVCRQGHPLLSLEDDEETLD
NAEHTLLLPEGQNFSGLRQRLQEMFPDRQISFSSYNILTIAALIASSDMLGIMPSRFYNLFSRCWPLEKL
PFPSLNEEQIDFSLHYNKLSLRDPVLENVIDVIRNAF
>gnl|CDD|183160 PRK11486, PRK11486, flagellar type III secretion system protein FliO
MNNHATVQSSAPVSGSPLLQVSGALIGIIALILAAAWLVKRLGFAPKRTGVRGLKISASASLGARERVVI
VDVEDARLVLGVTAGQINLLHKLPPAAPTEEAPVIPQADFQSVMKNLLKRSGRS
>gnl|CDD|236916 PRK11492, hyfE, hydrogenase 4 membrane subunit; Provisional
MTGSLIVNNLAGLMILTSLLVISVRSYRLSAGFYALQSLVLVSIFLTLSCLFAAEELLIWSITAFITKVL
LVPLIMTYAARKLGDNIEEEPVFGPAMSILLAALIVLLCAFVVQPVKLPMALGLKPALAVSLGHFLLGLL
CIVSQRNILKQIFGYCLMENGSHLTLALLAYNAPELVEIGIATDAIFAVIIMVLLARKIYRTHGTLDVNK
LTALKG
>gnl|CDD|236917 PRK11493, sseA, 3-mercaptopyruvate sulfurtransferase; Provisional
MSTTWFVAADWLAEHIDDPEIQIIDARMAPPGQEDRDVAAEYRAGHIPGAVFFDIEALSDHTSPLPHMMP
RPETFAVAMRELGVNQDKHLVVYDEGNLFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVEL
PEGEFNAAFNPEAVVRLTDVLLASHEKTAQIVDARPAARFNAEVDEPRPGLRRGHIPGALNVPWTELVRE
GELKTTDELDAIFFGRGVSFDRPIIASCGSGVTAAVVVLALATLDVPNVKLYDGAWSEWGARADLPVEPA
K
>gnl|CDD|236918 PRK11498, bcsA, cellulose synthase catalytic subunit; Provisional
NARLIGRYRDYRRHGASAFSATLGCLWMILAWIFLPLEHPRWQRIRAEHKNLYPHINASRPRPLDPLRYL
IQTLWLLIGRSRKETPKPRRRAFSGLQNIRGRYHQWLEELPERVSHKTQHLDEKKELGHLSAGARRLILG
IIVTFSLILALICITQPFNPLAQFIFLMLLWGVALLVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLN
WDDPVSLVCGLILLFAETYAWIVLVLGYFQVVWPLNRQPVPLPKDMSLWPTVDIFVPTYNEDLNVVKNTI
YASLGIDWPKDKLNIWILDDGGREEFRQFAQEVGVKYIARPTHEHAKAGNINNALKYAKGEFVAIFDCDH
VPTRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDATFFCG
SCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQ
IFRLDNPLTGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHA
SLTNSRIQGKYRHSFWSEIYETVLAWYIAPPTTVALFNPHKGKFNVTAKGGLVEEEYVDWVISRPYIFLV
LLNLVGVAVGIWRYFYGPPNEILTVIVSLVWVFYNLIILGGAVAVSVESKQVRRSHRVEMTMPAAIARED
GHLFSCTVQDFSDGGLGIKINGQAQLLEGQKVNLLLKRGQQEYVFPTQVTRVMGNEVGLQLMPLTTQQHI
DFVQCTFARADTWALWQDSFPEDKPLESLLDILKLGFRGYRHLAEFAPPSVKGIFRVLTSLVSWVVSFIP
RRPERQEAAQPS
>gnl|CDD|236919 PRK11504, tynA, primary-amine oxidase
TVEMATTTAAAVSHPLDPLTAAEIEAAVAILRAEGLLGESTRFVSIELAEPPKAEVLAFDPGDPIDRRAF
VVLYDRATGKTYEAVVSLTAGEVVSWEEIPGVQPPILLEEFEECEEVVRADPRWQAALAKRGITDFDLVM
VDPWSAGYFGEPEERGRRLARGLAFVRADPGDNGYARPIEGLVAVVDLNTMEVLRVEDHGVVPIPAEDGN
YDPEFIPPLRTDLKPLEITQPEGPSFTVDGNEVEWQKWSFRVGFNPREGLVLHQVSYDDGGRERPILYRA
SLSEMVVPYGDPSPTHYWKNAFDAGEYGLGRLANSLELGCDCLGEIRYFDAVLADSDGEPYTIKNAICMH
EEDYGILWKHTDFRTGSAEVRRSRRLVISFFATVGNYDYGFYWYFYQDGTIEFEVKLTGIVFTAAVPPGE
TPPYGTLVAPGLYAPNHQHFFNARLDMDVDGPGNSVYEVNSVPVPMGPDNPHGNAFYTRETLLETESEAA
RDADPSTGRYWKIVNPNKKNRLGEPVAYKLVPGGNPPLLADPGSSIRQRAGFATHHLWVTPYDPDERYAA
GDYPNQSAGGDGLPAYIAADRSIENTDVVLWYTFGITHVPRPEDWPVMPVDYAGFKLKPVGFFDRNPALD
LPPEPPAACHEHGASEH
>gnl|CDD|183165 PRK11505, PRK11505, phosphate starvation-inducible protein PsiF
MKITLLVTLLFGLVFLTTVGAAERTLTPQQQRMTSCNQQATAQALKGDARKTYMSDCLKNSKSAPGEKSL
TPQQQKMRECNNQATQQSLKGDDRNKFMSACLKKAA
>gnl|CDD|183166 PRK11507, PRK11507, ribosome-associated protein YbcJ
MATFSLGKHPHVELCDLLKLEGWSESGAQAKIAIAEGQVKVDGAVETRKRCKIVAGQTVSFAGHSVQVVA
>gnl|CDD|183167 PRK11508, PRK11508, sulfurtransferase TusE
MLIFEGKEIETDTEGYLKESSQWSEPLAVVIAENEGISLSPEHWEVVRFVRDFYLEFNTSPAIRMLVKAM
ANKFGEEKGNSRYLYRLFPKGPAKQATKIAGLPKPVKCI
>gnl|CDD|183168 PRK11509, PRK11509, hydrogenase-1 operon protein HyaE; Provisional
MSNDTPFDALWQRMLARGWTPVSESRLDDWLTQAPDGVVLLSSDPKRTPEVSDNPVMIGELLREFPDYTW
QVAIADLEQSEAIGDRFGVFRFPATLVFTGGNYRGVLNGIHPWAELINLMRGLVEPQQERAS
>gnl|CDD|236920 PRK11511, PRK11511, MDR efflux pump AcrAB transcriptional activator MarA
MSRRNTDAITIHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKL
KESNEPILYLAERYGFESQQTLTRTFKNYFDVPPHKYRMTNMQGESRFLHPLNHYNS
>gnl|CDD|183170 PRK11512, PRK11512, multiple antibiotic resistance transcriptional regulator MarR
MKSTSDLFNEIIPLGRLIHMVNQKKDRLLNEYLSPLDITAAQFKVLCSIRCAACITPVELKKVLSVDLGA
LTRMLDRLVCKGWVERLPNPNDKRGVLVKLTTSGAAICEQCHQLVGQDLHQELTKNLTADEVATLEHLLK
KVLP
>gnl|CDD|236921 PRK11513, PRK11513, cytochrome b561; Provisional
MENKYSRLQIGIHWLVFLLVIVAYCAMEFRGFFPRSDRPLINMIHVSCGISILVLMVVRLLLRLKYPTPP
IVPKPKPMMTGLAHLGHLVIYLLFIALPVIGLVMMYNRGNPWFAFGLTMPYASEANFERVDSLKSWHETL
ANLGYFVIGLHAAAALAHHYFWKDNTLLRMMPRKRS
>gnl|CDD|183172 PRK11517, PRK11517, DNA-binding response regulator HprR
MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAK
QTPVICLTARDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQHHALNSTLEISGLRMDSVSQSVS
RDNISITLTRKEFQLLWLLASRAGEIIPRTVIASEIWGINFDSDTNTVDVAIRRLRAKVDDPFPEKLIAT
IRGMGYSFVAVKK
>gnl|CDD|183173 PRK11519, PRK11519, tyrosine-protein kinase Wzc
MTEKVKQHAAPVTGSDEIDIGRLVGTVIEARWWVIGITAVFALCAVVYTFFATPIYSADALVQIEQNSGN
SLVQDIGSALANKPPASDAEIQLIRSRLVLGKTVDDLDLDIAVSKNTFPIFGAGWDRLMGRQNETVKVTT
FNRPKEMADQVFTLNVLDDKNYQLSSDGGFSARGQVGQMLKKDGVTLMVEAIHARPGTEFTVTKYSTLGM
INNLQNNLTVTENGKDTGVLSLTYTGEDREQIRDILNSITRNYLEQNIERKSEEASKSLAFLAQQLPEVR
SRLDVAENKLNAFRQDKDSVDLPLEAKAVLDSMVNIDAQLNELTFKEAEISKLYTKEHPAYRTLLEKRKA
LEDEKAKLNGRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKQQELKITEASTVGDVRIVDPAITQPGVL
KPKKALIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEHGISVYASIPLSEWQKARDSVKTIKGIKR
YKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLL
IDCDMRKGYTHELLGTNNVNGLSDILIGQGDITTAAKPTSIANFDLIPRGQVPPNPSELLMSERFAELVN
WASKNYDLVLIDTPPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSIFR
RASAYQDYGYYEYEYKSDA
>gnl|CDD|183174 PRK11521, PRK11521, DUF2509 family protein
LVLLLLILGSLLLQGMNQQQRSFAARVSMESQALRRQAIVQSALEWGKMQSWSTQPAVQCRQYAATGARV
CLRLLADNEALLIAGYEGVSLWRTGEVIDGNIVFSPHGWSDFCPLKERALCQLP
>gnl|CDD|183175 PRK11522, PRK11522, putrescine--2-oxoglutarate aminotransferase; Provisional
MNRLPSSASALACSAHALNLIEKRTLDHEEMKALNREVIEYFKEHVNPGFLEYRKSVTAGGDYGAVEWQA
GGLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVQNQLAKQPLHSQELLDPLRAMLAKTLAALTPGK
LKYSFFCNSGTESVEAALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRKPFMPLLPGFRHV
PFGNIEAMRTALSECKKTGDDVAAVILEPIQGEGGVILPPEGYLTAVRKLCDEFGALLILDEVQTGMGRT
GKMFACEHENVQPDILCLAKALGGGVMPIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVL
LEQNLPAQAEQKGDYLLDGFRQLAREYPDLVQEARGKGMLMAIEFVDNEIGYNFASEMFRQRVLVAGTLN
NAKTIRIEPPLTLTIEQCEQVLKAARKALAAMRVSVEEA
>gnl|CDD|183176 PRK11523, PRK11523, transcriptional regulator ExuR
MEITEPRRLYQQLAAELKERIEQGVYLVGDKLPAERFIADEKNVSRTVVREAIIMLEVEGYVEVRKGSGI
HVVSNQPRHQQAADNNMEFANYGPFELLQARQLIESNIAEFAATQVTKQDIMKLMAIQEQARGEDCFRDS
EWDLQFHVQVALATQNSALAAIVEKMWTQRSHNPYWKKLHEHIDDRTVDNWCDDHDQILKALIRKDPHAA
KLAMWQHLENTKQMLFNETSDDFEFNADRYLFAENPVVHLDTA
>gnl|CDD|183177 PRK11524, PRK11524, adenine-specific DNA-methyltransferase
PTRFGNEAKTIIHGDALTELKKIPSESVDLIFADPPYNIGKNFDGLIEAWKEDLFIDWLYEWIDECHRVL
KKQGTMYIMNSTENMPFIDLYCRKLFTIKSRIVWSYDSSGVQAKKYFGSMYEPILMMVKDAKNYTFNGDA
ILVEAKTGAKRALIDYRKNPPQPYNTQKVPGNVWDFPRVRYLMDEYENHPTQKPEALLKRIILASSNPGD
IVLDPFAGSFTTGAVAKASGRKFIGIEINSEYIKMGLRRLDVASHYSAEELAKVKKRKTGNLSKKSRLSE
VDPD
>gnl|CDD|183178 PRK11525, dinD, DNA-damage-inducible protein D; Provisional
MNEHHQPFEEIKHIGEEGVEFWSARELAPLLGYSEWRNFQKVIARAKTACENSGHAVSDHFVEVTKMVEL
GSGAQREVEDIMLSRYACYLIVQNGDPRKPVIAFGQTYFAIQTRRQELADDEAFRQLREDEKRLFLRNEL
KEHNKQLSEAAQEAGVATAIDFAIFQNHGYQGLYGGLDTKAIHQRKGLKKSQKILDHMGSTELAANLFRA
TQTEEKLKRDGVNSKQQANTTHFDVGRKVRQTIQELGGTMPEELPTPEESIKKLERRLKSTEKKLLKNP
>gnl|CDD|236922 PRK11528, PRK11528, hypothetical protein; Provisional
MRKSLLALTLLATLTIPALAQAEYKGGFANISLNYLDWTSRTTEKSSDKSHKDDFGYLELEGGAGFSWGE
LYGFFDLENPYNGRHAKPGDEQRYTFKNTGRIYLGDTGFNLYGHAYGTYGSPNRRNFHDDNTLYGIGYNF
TGDGWWFKPFFAKHYTDQTYYSGDNGYVAGWVAGYNFTLGSEKFSITNWNEYEFDRDAAYAAGNGGKDGI
NGAVALWWNATKHLTTGIQYRYADNKLGEDFLQDAIIYSIKYNF
>gnl|CDD|236923 PRK11530, PRK11530, hypothetical protein; Provisional
MTTRYLRLLLLGSLLLLAGCAQQSEVRQMHNSVSTLNQEMTQLTQQAVAIEQQNRLNANSTSGVYLLPAA
KTPARLESQIGTLRMSLSNITPEANGTRATLRIQGESNDPLPAFSATVEWGQLDGTTGNPLEVNVQSQLI
NAPASLLAPSDVDIPLRLSGITPEQLGFVRIHDIQPVMQPPPA
>gnl|CDD|183181 PRK11534, PRK11534, DNA-binding transcriptional regulator CsiR; Provisional
MTAPMQITALDGYRWLKNDIIRGNFQPDEKLRMSLLTSRYALGVGPLREALSQLVAERLVTVVNQKGYRV
ASMSEQELLDIFDARANMEAMLVSLAIARGGDEWEADVLAKAHLLSKLEACDASEKMLDEWDLRHQAFHT
AIVAGCGSHYLLQMRERLFDLAARYRFIWLRRTVLSVEMLEDKHDQHQTLTAAILARDTARASELMRQHL
LTPIPIIQQAMAGN
>gnl|CDD|183182 PRK11536, PRK11536, 6-N-hydroxylaminopurine resistance protein; Provisional
MRYPVDVYTGKIQAYPGGKPSAIAKIQVDGELMLTELGLEGDEQAEKKIHGGPDRALCHYPREHYLYWAR
EFPEQAELFVAPAFGENLSTDGLTESNVFIGDIFRWGEALIQVTQPRSPCYKLNYHFDISDIAQLMQNSG
KCGWLYRVIAPGKVSADAPLELVSRVSDVSVQEAAAIAWHMPFDDEQYHRLLSAAGLSASWTRTMQKRRL
SGKIEDFSRRLWG
>gnl|CDD|183183 PRK11537, PRK11537, putative GTP-binding protein YjiA; Provisional
MNPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKTLTNGCICCSRS
NELEDALLDLLDNLDKGNIQFDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDAVHADEQMN
QFTIAQSQVGYADRILLTKTDVAGEAEKLRERLARINARAPVYTVVHGDIDLSLLFNTNGFMLEENVVST
KPRFHFIADKQNDISSIVVELDYPVDISEVSRVMENLLLESADKLLRYKGMLWIDGEPNRLLFQGVQRLY
SADWDRPWGDETPHSTLVFIGIQLPEEEIRAAFAGLRK
>gnl|CDD|183184 PRK11538, PRK11538, ribosome silencing factor
MQGKALQDFVIDKIDDLKGQDIIALDVQGKSSITDCMIICTGTSSRHVMSIADHVVQESRAAGLLPLGVE
GENAADWIVVDLGDVIVHVMQEESRRLYELEKLWS
>gnl|CDD|236924 PRK11539, PRK11539, ComEC family competence protein; Provisional
MSITTVAVAIICGILPLLILPQLPGTWILAFLLLLACLLAFIPVKYCRYIALTLLFFLWGILAAKQILWQ
GETLTQATQDAIVEITATDGMTTHYGQVVIRITHLNGKRIFPALGVVLYGEYLPQAVCAGQRWAMKLKVR
AVHGQLNEGGFDSQRYAIAQRQPLTGRFLQAKVIDPNCSLRQQYLASLEQTLQPYPWRAIILALAFGERL
SVPKEIKNLLRDTGTAHLMAISGLHIAFAALLGWGLARGGQFFLPVRWIGWQFPLLGGWLCAAFYAWLAG
MQPPALRTVLALTLWGLLRLSGRQCSGWQVWLWCLALILLSDPLAVLSDSFWLSALAVAALIFWYQWFPL
PEWFLPGWLRAVLRLLHLQLGITLLLMPLQILLFHGISLTSLPANLWAVPLVSFITVPLILLALVLHLLP
PLEQGLWFLADRSLALVFWPLKSLPEGWINIGERWQWLSFSGWLALIIWRFNWWRSYPAMCVAVLLLMCW
PLWQRPREYEWRVDMLDVGHGLAVVIERNGKAILYDTGNAWPTGDSAQQVIIPWLRWHGLTPEGIILSHE
HLDHRGGLASLLHAWPMAWIRSPLNWANHLPCVRGEQWQWQGLTFSVHWPLEQSNDAGNNDSCVIRVDDG
KHSILLTGDLEAQAEQKLLSRYWQQLAATLLQVPHHGSNTSSSLPFIRAVNGKVALASASRYNAWRLPSV
KVKQRYQQQGYQWRDTPHSGQLSVYFSADGWRISGYREQILPRWYHQWFGVPVDN
>gnl|CDD|183186 PRK11543, gutQ, arabinose-5-phosphate isomerase GutQ
MSEALLNAGRQTLMLELQEASRLPERLGDDFVRAANIILHCEGKVVVSGIGKSGHIGKKIAATLASTGTP
AFFVHPAEALHGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDI
SVEREACPMHLAPTSSTVNTLMMGDALAMAVMQARGFNEEDFARSHPAGALGARLLNKVHHLMRRDDAIP
QVALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGGGALTTPVNEAMTRGGTTLQAQS
RAIDAKEILMKRKITAAPVVDENGKLTGAINLQDFYQAGII
>gnl|CDD|236926 PRK11545, gntK, gluconokinase
MGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVS
LIVCSALKKHYRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPGADETDVLV
VDIDQPLEGVVASTIEVIKKGKT
>gnl|CDD|183189 PRK11546, zraP, zinc resistance sensor/chaperone ZraP
MKRNTKIALVLMALSALAMGSGSAFAHHHWGGGHGMWQQNAAPLTTEQQAAWQKIHNDFYAQTSALRQQL
VSKRYEYNALLTANPPDSSKINAVAKEMENLRQSLDELRVKRDIAMAEAGIPRGAGMGYGGCGGGGHMGM
GHW
>gnl|CDD|183190 PRK11548, PRK11548, outer membrane protein assembly factor BamE
MRCKTLTAAAAVLLMLTAGCSTLERVVYRPDINQGNYLTPNDVAKIHVGMTQQQVAYTLGTPMMQDPFGT
NTWFYVFRQQPGHEKVTQQTLTLTFNSSGVLTNIDNKPALTGN
>gnl|CDD|236927 PRK11551, PRK11551, putative 3-hydroxyphenylpropionic transporter MhpT; Provisional
MSTRTSSASSSRLALTIGLCFLVALLEGLDLQSAGVAAPRMAQEFGLDVAQMGWAFSAGILGLLPGALLG
GRLADRIGRKRILIVSVALFGLFSLATAQAWDFPSLLVARLLTGVGLGGALPNLIALTSEAVGPRLRGTA
VSLMYCGVPFGGALASVIGVLAAGDAAWRHIFYVGGVGPLLLVPLLMRWLPESRAFAQAAGAGKQRAPVL
RALFGEGRATATLLLWISYFFTLIVLYFLLNWLPSLLVGQGLSRSQAGLVQIAFNIGGALGSLLIGALMD
RLRPRRVVLLIYAGILASLAALAAAPSFAGMLLAGFAAGLFVVGGQSVLYALAPLFYPTQVRGTGVGAAV
AVGRLGSMAGPLLAGQLLALGRSTVGVIGASIPVILVAALAALLLVSRPSRADPCA
>gnl|CDD|236928 PRK11552, PRK11552, putative DNA-binding transcriptional regulator; Provisional
MMNNPAMTTRGEQAKQQLIAAALAQFGEYGLHATTRDIAAQAGQNIAAITYYFGSKEDLYLAVAQWIADF
IGEQFRPHAEEAERLFAQPAPDRAAIRELILRACLNMIKLLTQDDTVNLSKFISREQLSPTAAYHLIHEQ
VISPLHSHLTRLIAAYTGCDANDTRTILHTHALIGEVLAFRLGRETILLRTGWTQFDEEKAELINQVVTC
HIDLILNGLRQRSLD
>gnl|CDD|236929 PRK11553, PRK11553, alkanesulfonate transporter substrate-binding subunit; Provisional
MRNIIKLALAGLLSVSTLAVAAESSPEALRIGYQKGSIGLVLAKSHQLLEKRFPQTKISWVEFPAGPQML
EALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEPPKPKAEVILVAENSPIKTVADLKGHKVAFQKGSSS
HNLLLRALRKAGLKFTDIQPTYLTPADARAAFQQGNVDAWAIWDPYYSAALLQGGVRVLKDGTDLNQTGS
FYLAARPYAEKNGAFIQQVLATLTEADALTRSQREQSIALLAKTMGLPAAVIASYLDHRPPTTIKPLSAE
VAAAQQQTADLFYENRLVPKKVDIRQRVWQPTQL
>gnl|CDD|183194 PRK11556, PRK11556, MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit
MKGSRKSRWVIVIVVVIAAIAAFWFWQGRSTSSSAAPGAAKQAQQSPAGGRRGMRSGPLAPVQAATATEQ
AVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQAT
LANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQ
VDVGNQISSGDTTGIVVITQTHPIDLVFTLPESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLD
NQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFVWVLNDENKVSKH
LVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQSATTPEEKATSREYAKKGARS
>gnl|CDD|183195 PRK11557, PRK11557, MurR/RpiR family transcriptional regulator
LRIRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEAL
ASQPEPPSVPVHNQIRGDDPLRLVGEKLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASG
LVAQNFAWKLMKIGINAVAERDMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITG
FTPNALQQRASHCLYTIAEEQATRSAAISSTHAQGMLTDLLFMALIQQDLERAPERIRHSEALVKKLV
>gnl|CDD|236930 PRK11558, PRK11558, putative ssRNA endonuclease; Provisional
MSMLVVVTENVPPRLRGRLAVWLLEVRAGVYVGDVSRRIREMIWQQVTQLAEEGNVVMAWATNTESGFEF
QTFGENRRIPVDLDGLRLVSFLPVENQ
>gnl|CDD|183197 PRK11559, garR, tartronate semialdehyde reductase; Provisional
MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSP
HVKEVALGENGIIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGG
DKAIFDKYYDLMKAMAGSVVHTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGG
LAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHS
ALACYYEKLAKVEVTR
>gnl|CDD|183198 PRK11560, PRK11560, kdo(2)-lipid A phosphoethanolamine 7''-transferase
MRYIKSLTQQKLSFLLAVYIGLFLNIAVFYRRFDSYAQDFTVWKGLSAVVELAATVLVTFFLLRLLSLFG
RRFWRVLASLLVLFSAAASYYMTFFNVVIGYGIIASVMTTDIDLSKEVVGLHFILWLVAVSALPLILIWN
NRCRYTLLRQLRTPGQRIRSLAVVVLAGLLVWAPIRLLDIQQKKVERATGVDLPSYGGVVANSYLPSNWL
SALGLYAWAQVDESSDNNSLLNPAKKFTYQAPKGVDDTYVVFIIGETTRWDHMGILGYERNTTPKLAQEK
NLAAFRGYSCDTATKLSLRCMFVREGGAEDNPQRTLKEQNVFAVLKQLGFSSELFAMQSEMWFYNNTMAD
NYAYREQIGAEPRNRGKPVDDMLLVDEMKQSLGRNPDGKHLIILHTKGSHYNYTQRYPRSFARYQPECIG
VDSGCSKAQLINSYDNSVLYVDHFISSVIDQLRDKKAIVFYAADHGESINEREHLHGTPREMAPPEQFRV
PMMVWMSDKYLANPDNAQAFAQLKKQADMKVPRRHVELFDTILGCLGYTSPDGGINENNNWCHIPDAK
>gnl|CDD|183199 PRK11561, PRK11561, isovaleryl CoA dehydrogenase; Provisional
MHWQTHTVFNQPIPLNNSNLFLSDGALCEAVTREGAGWDSDLLASIGQQLGTAESLELGRLANANPPELL
RYDAQGQRLDDVRFHPAWHLLMQGLCANRVHNLAWEEDARSGAFVARAARFMLHAQVEAGTLCPITMTFA
ATPLLLQMLPAPFQDWLTPLLSDRYDSHLLPGGQKRGLLIGMGMTEKQGGSDVLSNTTRAERLADGSYRL
VGHKWFFSVPQSDAHLVLAQAKGGLSCFFVPRFLPDGQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWL
LGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEG
QTALLFRLARAWDRRADAKEALWARLFTPAAKFVICKRGIPFVAEAMEVLGGIGYCEESELPRLYREMPV
NSIWEGSGNIMCLDVLRVLNKQPGVYDLLSEAFVEVKGQDRHFDRAVRQLQQRLRKPAEEQGREITQQLF
LLGCGAQMLRHASPPLAQAWCQMMLDTRGGVRLSEQVQNDLLLRATGG
>gnl|CDD|183200 PRK11562, PRK11562, nitrite transporter NirC; Provisional
MFTDTINKCAANAARIARLSANNPLGFWVSSAMAGAYVGLGIILIFTLGNLLDPSVRPLVMGATFGIALT
LVIIAGSELFTGHTMFLTFGVKAGTISHGQMWAILPQTWLGNLVGSVFVALLYSWGGGSLLPVDTSIVHS
VALAKTTAPAMVLFFKGALCNWLVCLAIWMAIRTEGAAKFIAIWWCLLAFIASGYEHSVANMTLFALSWF
GHHSEAYTLAGIGHNLLWVTLGNTLSGAVFMGLGYWYATPKANRPVAAKFNQTETAAG
>gnl|CDD|236932 PRK11564, PRK11564, stationary phase inducible protein CsiE; Provisional
MMPTLAPPSVLSAPQRRCQILLMLFQPGLTVTLETFSQLNGVDDDTARQDIAETGREIQRYHRLTLTTGA
DGSYRIEGTALDQRLCLLHWLRRGLRLCPSFITQQFTPALKSELKQRGIARNLYDDTNLQALINLCSRRL
NRQFEERDRQFLQLYLQYCLLQHHAGITPQFNPLQQQWLESKAEFQLAQEIGRHWQRRVLQPPPLDEPLF
LALLFSMLRAPDPLRDAHQRDRRLRQAIKRLVNRFRELGGVRFSDEQGLCDQLYTHLAQALERSLFAIGI
DNTLPEEFARLYPRLLRTTRAALAGFEQEYGVHFSDEEVGLVAVIFGAWLMQENDLHEKQILLLTGDNPE
LEAQIEQQLRELTLLPLNIKYLSVKAFQQSGAPRGVALIITPYATPLPLFSPPLIHADLPLTEHQQQQIR
KILESA
>gnl|CDD|183203 PRK11565, dkgA, 2,5-didehydrogluconate reductase DkgA
MANPTVIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREE
LFITTKLWNDDHKRPREALEESLKKLQLDYVDLYLMHWPVPAIDHYVEAWKGMIELQKEGLIKSIGVCNF
QIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGVFDQKVIRDLADKYG
KTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKRLGPDPDQFGG
>gnl|CDD|183204 PRK11566, hdeB, acid-activated periplasmic chaperone HdeB
RKAFIFMAAVTALSLVNAQSATATNTTPKDMTCQEFIDLNPKSMTPVAFWVLNEDTDYKGGDYVDLNETD
TTQVPKVIEYCKKNPQKKLSTIKNQIKNDLPK
>gnl|CDD|183205 PRK11568, PRK11568, IMPACT family protein
MESYLIPAAPVTVVEEIKKSRFITLLAHTDGVEAAKAFVQSVRAEHPDARHHCWAWVAGAPDDSQQLGFS
DDGEPAGTAGKPMLAQLMGSGVGEITAVVVRYYGGILLGTGGLVKAYGGGVQQALRQLTTQRKVPLTEYT
LQCEYAQLAGIEALLGQFDGKIVNSEYQAFVTLRVALPAAKVAEFSAKLADFSRGSLQLLAIEE
>gnl|CDD|183206 PRK11569, PRK11569, glyoxylate bypass operon transcriptional repressor IclR
MVAPIPAKRGRKPAAATAPATGQVQSLTRGLKLLEWIAESNGSVALTELAQQAGLPNSTTHRLLTTMQQQ
GFVRQVGELGHWAIGAHAFIVGSSFLQSRNLLAIVHPILRNLMEDSGETVNLAVLDQSDHQAIIIDQVQC
TALMRMSAPIGGKLPMHASGAGKAFLAQLSEEQVTKLLHRKGLHAYTHATLVSPVHLKEDLAQTRKRGYS
FDDEEHALGLRCVAACIFDEHREPFAAISISGPISRITDDRVTELGAMVIKAAKEVTLAYGGMR
>gnl|CDD|183207 PRK11570, PRK11570, peptidyl-prolyl cis-trans isomerase; Provisional
MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERAD
AVRRERQQAMAAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSS
VARGEPAEFPVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL
>gnl|CDD|183208 PRK11572, PRK11572, copper homeostasis protein CutC; Provisional
MALLEICCYSMECALTAQQAGADRIELCAAPKEGGLTPSLGVLKSVRERVTIPVHPIIRPRGGDFCYSDG
EFAAMLEDIATVRELGFPGLVTGVLDVDGHVDMPRMRKIMAAAGPLAVTFHRAFDMCANPLNALKQLADL
GVARILTSGQQQDAEQGLSLIMELIAASDGPIIMAGAGVRLSNLHKFLDAGVREVHSSAGQWVPSPMRYR
KAGVSMSSDAEADEFSRYCVDGAAVAAMKGIISRHQAK
>gnl|CDD|236933 PRK11573, PRK11573, hypothetical protein; Provisional
MVVISAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALGTIVG
MRLYGDAGVAIATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMR
LMGIKTDIVVSGALSKEELRTIVHESRSQISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKS
ILRQLTHSPHGRIVLYRDSLDDAISMLRVREAYRLMTEKKEFTKENMLRAADEIYFVPEGTPLSTQLVKF
QRNKKKVGLVVDEYGDIQGLVTVEDILEEIVGDFTTSMSPTLAEEVTPQNDGSVIIDGTANVREINKAFN
WHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDIDILDVQDNMIKQVKVTPVKPLRESVAE
>gnl|CDD|183210 PRK11574, PRK11574, protein deglycase YajL
MSASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGNLEITCSRGVKLLADAPLVEVADGDFDVI
VLPGGIKGAECFRDSPLLVETVRQFHRSGRIVAAICAAPATVLVPHDLFPIGNMTGFPTLKDKIPAEQWQ
DKRVVWDARVNLLTSQGPGTAIDFALKIIDLLVGREKAHEVASQLVMAAGIYNYYE
>gnl|CDD|183211 PRK11578, PRK11578, macrolide transporter subunit MacA; Provisional
MKKRKKVKKRYLIALVIVLAGGITLWRILNAPVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSG
QLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQA
VSQQDLDTAATELAVKQAQIGTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQ
APNILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAIFYYARFE
VPNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALGDPVGDNRYKVKLLRNGETREREVTIGARNDTDVEI
VKGLEAGDEVIIGEAKPGAA
>gnl|CDD|183212 PRK11579, PRK11579, putative oxidoreductase; Provisional
MSDKIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVI
PTPNDTHFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEG
VLGEVAYFESHFDRFRPQVRQRWREQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTD
YFHAILSYPQRRVVLHGTMLAAAESARYIVHGSRGSYVKYGLDPQEERLKNGERLPQEDWGYDMRDGVLT
LVEGEERVEETLLTLPGNYPAYYAAIRDALNGDGENPVPASQAIQVMELIELGIESAKHRATLCLA
>gnl|CDD|183213 PRK11582, PRK11582, flagella biosynthesis regulatory protein FliZ
MMVQQLKRRPLSRYLKDFKHSQTHCAHCRKLLDRITLVFRGQIINKIAISRMDTLIDDNGWQKLQQEWVA
LCRFCSDLHCNTQSDYFDIIGFKQYLFEQTEMSHSTVREYVVRLRRLDEHLHEQNIPLDLLQDGFLDERL
APWLPDTSTNNYRIALRKYQQYLAWQQTY
>gnl|CDD|183214 PRK11586, napB, nitrate reductase cytochrome c-type subunit
MKSHDLKKALCQWTAMLALVVSGAVWAANGVDLSQSPEVSGTQEGAIRMPKEQERMPLNYVNQPPMIPHS
VEGYQVTTNTNRCLQCHGVESYRTTGAPRISPTHFMDSDGKVGAEVAPRRYFCLQCHVPQADTAPIVGNT
FTPSKGYGK
>gnl|CDD|183215 PRK11587, PRK11587, putative phosphatase; Provisional
MRCKGFLFDLDGTLVDSLPAVERAWSNWADRHGIAPDEVLNFIHGKQAITSLRHFMAGASEAEIQAEFTR
LEQIEATDTEGITALPGAIALLNHLNKLGIPWAIVTSGSVPVASARHKAAGLPAPEVFVTAERVKRGKPE
PDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVIAVNAPADTPRLDEVDLVLHSLEQLTVTKQPN
GDVIILLK
>gnl|CDD|236934 PRK11588, PRK11588, putative basic amino acid antiporter YfcC
MSAITESKPTRRWAMPDTLVIIFFVAILAALATYVVPVGMFDSQEVQYQVDGQTKTRKVVDPHSFRILTD
EAGEPEYHRVQLFTTGDERPGLMNFPFEGLTSGSKWGTAVGIIMFMLVIGGAFGIVMRTGTIDNGILALI
RKTRGNEILFIPVLFILFSLGGAVFGMGEEAIAFAIIIAPLMVRLGYDSITTVLVTYVATQIGFATSWMN
PFSVAIAQGIAGVPVLSGSGLRIVMWVIFTLIGLIFTMVYASRVKKNPLLSRVHESDRFFREKQADVEQR
PFTFGDWLVLLVLTAVMVWVIWGVVVNAWFIPEIASQFFTMGLVIGLIGVVFRLNGMTVNTMASSFTEGA
RMMLAPALLVGFAKGILLLLGGGEPGDPSVLNTILNSAGGAISGLPDAVSAWFMLLFQSVFNFFVTSGSG
QAALTMPLMAPLADLVGVNRQVAVLAFQLGDGFTNIIYPTSASLMATLGVCRVDFGNWLKFIWRFLLLLF
IMSSVVVIGAQYMGYH
>gnl|CDD|236935 PRK11589, gcvR, glycine cleavage system transcriptional repressor; Provisional
MPQSSQHYLVITALGADRPGIVNTITRHVSSCGCNIEDSRLAMLGEEFTFIMLLSGSWNAITLIESTLPL
KGAELDLLIVMKRTTARPRPAMPATVWVQVEVADSPHLIERFTALFDSHHMNIAELVSRTQPAEGERPAQ
LHIQITAHSPASQDAANIEQAFKALCTELNAQGSINVVNYSQHDEQDGVK
>gnl|CDD|183219 PRK11593, folB, bifunctional dihydroneopterin aldolase/7,8-dihydroneopterin epimerase
MDIVFIEQLSVITTIGVYDWEQTIEQKLVFDIEMAWDNRKAAKSDDVADCLSYADIAETVISHVEGARFA
LVERVAEEVAELLLARFNSPWVRIKLSKPGAVARAANVGVIIERGNNLK
>gnl|CDD|183220 PRK11594, PRK11594, efflux system membrane protein; Provisional
MSLLPVIVVFGLSFPPIFFELLLSLALFWLVRRVLVPTGIYDFVWHPALFNTALYCCLFYLISRLFV
>gnl|CDD|183221 PRK11595, PRK11595, DNA utilization protein GntX; Provisional
MLTVPGLCWLCRMPLALSHWGICSVCSRALRTLKTCCPQCGLPATHPHLPCGRCLQKPPPWQRLVFVSDY
APPLSGLIHQLKFSRRSELASVLARLLLLEWLQARRSTGLQKPDRIISVPLHQRRHWRRGFNQSDLLCRP
LARWLGCDYDSEALTRTRATATQHFLSARLRKRNLKNAFRLELPVQGQHMAIVDDVVTTGSTVAEIAQLL
LRNGAASVQVWCLCRTL
>gnl|CDD|183222 PRK11596, PRK11596, cyclic-di-GMP phosphodiesterase; Provisional
MIRQVIQRISLPEASIESLQERRYWLQCERAYTFQPIYRTSGRLMAIELLTAVTHPSNPSQRLSPERYFA
EITVSHRLDVVKEQLDLLAQWADFFVRHGLLASVNIDGPTLIALRQQPAILRLIERLPWLRFELVEHIRL
PKDSPFASMCEFGPLWLDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCR
GVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETLETLPLAL
>gnl|CDD|183223 PRK11597, PRK11597, heat shock chaperone IbpB; Provisional
MRNYDLSPLLRQWIGFDKLANALQNAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTV
KGTPEQPEKEVKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAISERPAL
NS
>gnl|CDD|183224 PRK11598, PRK11598, putative metal dependent hydrolase; Provisional
LKRLLKRPSLNLLTFLLLAAFYITLCLNIAFYKQVLQLLPLDSLHNVLVFASMPVVAFSVINIVFTLLSF
PWLRRPLACLFILVGAAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACW
IKIRPATPRWRSVLFRLANILVSVLLILLVAALFYKDYASLFRNNKELVKSLTPSNSIVASWSWYSHQRL
ANLPLVRIGEDAHKNPLMQNQKRKNLTILVVGETSRAENFSLGGYPRETNPRLAKDNVIYFPHTTSCGTA
TAVSVPCMFSNMPRKHYDEELAHHQEGLLDIIQRAGINVLWNDNDGGCKGACDRVPHQDVTALNLPGQCI
DGECYDEVLFHGLENYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFTPTCDTNEIQTCTQQQLVNTY
DNTILYVDYIVDKAINLLKQHQDKFNTSLVYLSDHGESLGENGIYLHGLPYAIAPDQQTHVPMLLWLSPD
YQKRYGVDQQCLQKQAQTQDYSQDNLFSTLLGLTGVQTKEYQAADDILQPCRRLS
>gnl|CDD|183225 PRK11602, cysW, sulfate/thiosulfate ABC transporter permease CysW
MAEVTQLKRYDRPPINWGKWFLIGIGMLVSAFILVVPMIYIFVQAFSKGLMPVLQNLADPDMLHAIWLTV
LIALIAVPVNLVFGILLAWLVTRFNFPGRQLLLTLLDIPFAVSPVVAGLVYLLFYGSNGPLGGWLDEHNL
QLMFSWPGMVLVTIFVTCPFVVRELVPVMLSQGSQEDEAAILLGASGWQMFRRVTLPNIRWALLYGVVLT
NARAIGEFGAVSVVSGSIRGETLSLPLQIELLEQDYNTVGSFTAAALLTLMAIITLFLKSMLQWRLENQE
KRA
>gnl|CDD|183226 PRK11607, potG, putrescine ABC transporter ATP-binding subunit PotG
MNDAIPRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ
PTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQ
EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQ
EEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVLKERQEDGLVIDSPGLVHPLK
VDADASVVDNVPVHVALRPEKIMLCEEPPADGCNFAVGEVIHIAYLGDLSIYHVRLKSGQMISAQLQNAH
RYRKGLPTWGDEVRLCWEADSCVVLTV
>gnl|CDD|236936 PRK11608, pspF, phage shock protein operon transcriptional activator; Provisional
MAEYKDNLLGEANSFLEVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNE
NLLDSELFGHEAGAFTGAQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQV
NVRLVCATNADLPAMVAEGKFRADLLDRLAFDVVQLPPLRERQSDIMLMAEHFAIQMCRELGLPLFPGFT
ERARETLLNYRWPGNIRELKNVVERSVYRHGTSEYPLDNIIIDPFKRRPAEEAIAVSETTSLPTLPLDLR
EWQHQQEKELLQRSLQQAKFNQKRAAELLGLTYHQLRALLKKHQIL
>gnl|CDD|183228 PRK11609, PRK11609, bifunctional nicotinamidase/pyrazinamidase
MKRALLLVDLQNDFCAGGALAVPEGDSTIDVANRLIDWCQSRGIPVIASQDWHPANHGSFASNHGAEPGT
QGELDGLPQTWWPDHCVQNSEGAALHPLLNQKAIDAVFHKGENPLIDSYSAFFDNGHRQKTALDDWLREH
GITELIVMGLATDYCVKFTVLDALALGYQVNVITDGCRGVNLQPQDSAHAFMEMSAAGATLYTLADWEET
QG
>gnl|CDD|183229 PRK11611, PRK11611, enhanced serine sensitivity protein SseB; Provisional
LLELAATEPAHRPAFFRTLLEATVWVPGTAAQGEAVVEDSAVDLQHWEKEDGTSVIPFFTSLEALQQAVE
DEQAFVVMPVRTLFEMTLGETLFLNPKLPTGKEFMPREISLLLGEEGNPLSSQEVLEGGESLLLSEVAEP
PAQMIDSLTTLFKTIKPVKRAFLASIKENADAQPNLLIGIEADGDIEEIIQAAGSVATDTLPGDEPIDIC
QVKEGEKGISHFITEHITPFYERRWGSFLRDFKQNR
>gnl|CDD|183230 PRK11613, folP, dihydropteroate synthase; Provisional
MKLFAQGTTLDLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVS
VEEELDRVIPVVEAIAQRFEVWISVDTSKPEVIRESAKAGAHIINDIRSLSEPGALEAAAETGLPVCLMH
MQGNPKTMQEAPKYDDVFAEVNRYFIEQIARCEAAGIAKEKLLLDPGFGFGKNLSHNYQLLARLAEFHHF
NLPLLVGMSRKSMIGQLLNVGPSERLSGSLACAVIAAMQGAQIIRVHDVKETVEAMRVVEATLSAKENKR
YE
>gnl|CDD|183231 PRK11614, livF, high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF
MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT
DWQTAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSG
GEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVL
ENGHVVLEDTGDALLANEAVRSAYLGG
>gnl|CDD|183232 PRK11615, PRK11615, hypothetical protein; Provisional
MRNLVKYVGIGLLVMGLAACDGKDTKAAAQGAVAESNASGQPVSLLDGKLSFTLPADMSDQSGKLGTQAN
NMHVYADATGQKAVIVILGDDTNEDLAVLAKRLEDQQRSRDPQLQVVTNKAIELKGHKLQQLDSIISAKG
QTAYSSVVLGKVDNQLLTMQITLPADNQQQAQTTAENIINTLVIK
>gnl|CDD|183233 PRK11616, PRK11616, hypothetical protein; Provisional
IRNVLLAFMICSGMLLLSGCSSVMSHTGGKEGTYPGTRASATMLGDDETNWGTKSLAALDMPFTAVMDTL
LLPWDYFRKDSSVRSRVEKSEAQNQATNAVIPPARMPDN
>gnl|CDD|236937 PRK11617, PRK11617, deoxyribonuclease V
MMDLAELRAQQIELASSVIREDRLDKDPPRLIAGADVGFEQGGEVTRAAIVVLKYPSLELVEYQVARIAT
TMPYIPGFLSFREYPALLAAWEQLSQKPDLVFVDGHGIAHPRRLGVASHFGLLVDVPTIGVAKKRLCGKF
EPLSEEPGSLQPLMDKGEQLGWVWRSKARCNPLFISTGHRVSLDSALAWVQRCMKGYRLPEPTRWADALA
SRRPAFVRWQANQP
>gnl|CDD|183235 PRK11618, PRK11618, inner membrane ABC transporter permease protein YjfF; Provisional
MIKRNLPLMITIGVFVLGYLFCLVQFPGFASTRVICNLLTDNAFLGIVAVGMTFVILSGGIDLSVGSVIA
FTGVFLAKLIGDYGWSPLLAFPLVLVMGAAFGAFMGALIHYLKLPAFIVTLAGMFLARGVSFLVSEESIP
INHPFYDTLSSLAWKLPGGGRLSAMALIMLAVVAIGIFLAHRTRFGNNVYAIGGNATSANLMGIPVRRTT
IRIYMLSGFLATLAGIVFSLYTSAGYALAAVGVELDAIAAVVIGGTLLTGGVGTVLGTLFGVLIQGLIQT
YITFDGTLSSWWTKIVIGILLFVFIALQRGLTVLAEN
>gnl|CDD|183236 PRK11619, PRK11619, lytic murein transglycosylase; Provisional
MEKAKMGKWRLLAAGVCLLTVSGVARADSLDEQRQRYQQIKQAWDNRQMDVVEQLMPTLKDYPLYPYLEY
RQLTQDLMNQPAVQVTNFIRANPTLPPARSLQSRFVNELARREDWRGLLAFSPEKPKPVEARCNYYYAKW
ATGQQQEAWQGAKELWLTGKSLPNACDKLFSVWQQSGKQDPLAYLERIRLAMKAGNTGLVTYLAKQLPAD
YQTIASALIKLQNDPNTVETFARTTGPTDFTRQMAAVAFASVARQDAENARLMIPSLVRAQKLNEDQRQE
LRDIVAWRLMGNDVTDEQAKWRDDVIMRSQSTSLLERRVRMALGTGDRRGLNTWLARLPMEAKEKDEWRY
WQADLLLEQGRKAEAEEILRQLMQQRGFYPMVAAQRLGEEYPLKIDKAPKPDSALTQGPEMARVRELMYW
NMDNTARSEWANLVASRSKTEQAQLARYAFNQQWWDLSVQATIAGKLWDHLEERFPLAWNDEFRRYTSGK
GIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYSSSSQLLDPETNINIGTSYL
EYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGQ
KPTLLSDAEWQRRY
>gnl|CDD|236938 PRK11621, PRK11621, Tat proofreading chaperone DmsD
MTDFSQQDNISVTARVLGALFYYAPESAEAAPLVAFLRQDDWETEWPLDAASLAPIAALFATGSEETLAQ
AWQRLFIGPWALPAPPWGSVWLDRESVLFGDSTLALRQWMRENGIQFEMKQNEPEDHFGLLLLLAAWLAE
NGRPTELEELLAWHLLPWSYRFLDVFIEQAGHPFYQALAQLARLTLAQWQSQLLIPVAVKPLYR
>gnl|CDD|183238 PRK11622, PRK11622, ABC transporter substrate-binding protein
MMRILGLLLGLLSLLSLAACASDAENKDWQQILEEAKGQTVYFYAWGGSPAINRYLDWVAKELKERYGIT
LKHVKLADIAEAVNRLLAEKQAGRDTGGSVDLVWINGENFRTLKEAGLLYGPFAETLPNWRYVDTSLPVR
EDFGVPTEGLEAPWGGAQLVFIYDSARTPQPPQSPAELLEWAKANPGRFTYPRPPDFTGTAFLKQLLYEL
TGDPAALKQPVDKATFARVTAPLWDYLDELHPYLWREGKTFPASPAELDQLLADGELDLAMTFNPNHAQS
KIANGELPASTRSFVFDDGTIGNTHFVAIPFNANAKAGAKVVANFLLSPEAQLRKADPAVWGDPSVLDPQ
KLPEEQRAAFAALDLGAATLQPELLPPALPEPHASWVEALEQEWQRRYGTH
>gnl|CDD|236939 PRK11623, pcnB, poly(A) polymerase I; Provisional
MTLPRCTIFTRVANFCRKVLSREESEAEQAVARPQMTVIPREQHAISRKDISENALKVLYRLNKAGYEAY
LVGGGVRDLLLGKKPKDFDVTTNATPEQVRKLFRNCRLVGRRFRLAHVMFGPEIIEVATFRGHHEGNESD
RNTSQRGQNGMLLRDNIFGSIEEDAQRRDFTINSLYYSVADFTVRDYVGGMKDLKEGVIRLIGNPETRYR
EDPVRMLRAVRFAAKLDMRISPETAEPIPRLATLLNDIPPARLFEESLKLLQAGYGYETYKLLCEYHLFQ
PLFPTITRYFTENGDSPMERIIEQVLKNTDTRIHNDMRVNPAFLFAAMFWYPLLEHAQKIAQESGLAYYD
AFALAMNDVLDEACRSLAIPKRLTTLTRDIWQLQLRMSRRQGKRAWKLMEHPKFRAAYDLLALRAEVENN
AELQRLAQWWGEFQVSAPPQQKGMLNELDDDPAPRRRTRRPRKRAPRREGTA
>gnl|CDD|183240 PRK11624, cdsA, phosphatidate cytidylyltransferase
MLKYRLITAFILIPVVIAALFLLPPVGFAIVTLVVCMLAAWEWGQLSGFASRSQRVWLAVLCGLLLALML
FLLPEYHHNIHQPLVEISLWASLGWWIVALLLVLFYPGSAAIWRNSKTLRLIFGVLTIVPFFWGMLALRA
WHYDENHYSGAWWLLYVMILVWGADSGAYMFGKLFGKHKLAPKVSPGKTWEGFIGGLATAAVISWLFGMW
APLDVAPVTLLICSIVAALASVLGDLTESMFKREAGIKDSGHLIPGHGGILDRIDSLTAAVPVFACLLLL
VFRTL
>gnl|CDD|183241 PRK11625, PRK11625, Rho-binding antiterminator; Provisional
MNDTYQPINCDDYDNLELACQHHLMLTLELKDGEVLQAKASDLVSRKNVEYLVVEAAGETRELRLDKIAS
FSHPEIGTVVVSES
>gnl|CDD|183242 PRK11627, PRK11627, hypothetical protein; Provisional
MLKKILFPLVALFMLAGCATPSNTLEVSPKITLPQQDPSLMGVTVSINGADQRQDQALAKVNRDGQLVTL
TPSRDLRFLLQEVLEKQMTARGYMIGPNGAVNLQIIVNQLYADVSEGNVRYNIATKADISIIATAQNGNK
QTKNYRASYNVQGAFQASNKKIADAVNSVLSDVIADMAQDTSISEFIKQNAR
>gnl|CDD|183243 PRK11628, PRK11628, transcriptional regulator BolA; Provisional
MMIREQIEEKLRAAFQPVFLEVVDESYRHNVPAGSESHFKVVLVSDRFTGERFLNRHRMIYSTLAEELST
TVHALALHTYTIKEWEGLQDTVFASPPCRGAGSIA
>gnl|CDD|183244 PRK11629, lolD, lipoprotein-releasing ABC transporter ATP-binding protein LolD
MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNG
QPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRAN
HRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAK
RMSRQLEMRDGRLTAELSLMGAE
>gnl|CDD|183245 PRK11630, PRK11630, threonylcarbamoyl-AMP synthase
MSQFFYIHPDNPQQRLINQAVEIVRKGGVIVYPTDSGYALGCKIEDKNAMERICRIRQLPDGHNFTLMCR
DLSELSTYSFVDNVAFRLMKNNTPGNYTFILKGTKEVPRRLLQEKRKTIGLRVPSNPIALALLEALGEPM
LSTSLMLPGSDFTESDPEEIKDRLEKQVDLIIHGGYLGQQPTTVIDLTDDTPVVVREGVGDVKPFL
>gnl|CDD|236940 PRK11633, PRK11633, cell division protein DedD; Provisional
MASKFQNRLVGTIVLVALGVIVLPGLLDGQKKHYQDEFAAIPLVPKPGDRDEPDMMPAATQALPTQPPEG
AAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAPKPEPKPVVE
EKAAPTGKAYVVQLGALKNADKVNEIVAKLRLSGYRVYTVPSTPVQGKITRIYVGPDASKDKLKGSLGEL
KQLSGLSGVVMGYTPN
>gnl|CDD|236941 PRK11634, PRK11634, ATP-dependent RNA helicase DeaD; Provisional
MAEFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDP
ELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHL
KRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRI
QSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMN
QALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVE
NRERRLLRNIERTMKLTIPEVELPNAELLGKRRLEKFAAKVQQQLESSDLDQYRALLAKIQPTAEGEELD
LETLAAALLKMAQGERPLILPPDAPMRPKREFRDRDDRGPRDRNDRGPRGDREDRPRRERRDVGDMQLYR
IEVGRDDGVEVRHIVGAIANEGDISSRYIGNIKLFASHSTIELPKGMPGEVLQHFTRTRILNKPMNMQLL
GDAQPHTGGERRGGGRGFGGERREGGRNFSGERREGGRGDGRRFSGERREGRAPRRDDSTGRRRFGGDA
>gnl|CDD|183248 PRK11636, mrcA, penicillin-binding protein 1a; Provisional
MKFVKYLLILAVCCILLGAGSIYGLYRYIEPQLPDVATLKDVRLQTPMQVYSADGELIAQYGEKRRIPLT
LDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRK
IKEAFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAGLPKAPSTFN
PLYSMDRAVARRNVVLSRMLDEGYITQAQYDQARSEPIVANYHAPEIAFSAPYLSEMVRQEMYNRYGENA
YEDGYRVYTTITRKVQQAAQQAVRNNVLDYDMRHGYRGPANVLWKVGESAWDNKKITDTLKALPTYGPLL
PAVVTSANPQEATAMLADGSSVALPMEGVRWARPYRSDTQQGPTPRKVTDVVQTGQQIWVRQVDDAWWLA
QVPDVNSALVSINPQNGAVMALVGGFDFNQSKFNRATQALRQVGSNIKPFLYTAAMDKGLTLASMLNDVP
ISRWDAGAGSDWRPKNSPPQYAGPIRLRQGLGQSKNVVMVRAMRAMGVDYAAEYLQRFGFPAQNIVHTES
LALGSASFTPMQVARGYAVMANGGFLVDPYFISKIENDQGGVIFEAKPKVACPECDIPVIYGDTQKSNVL
ENDDVENVATSQEQQNSSVPMPQLEQANQALVAQNGAQEYAPHVINTPLAFLIKSALNTNIFGEPGWMGT
GWRAGRDLKRRDIGGKTGTTNSSKDAWFSGYGPGVVTSVWIGFDDHRRDLGRTTASGAIKDQISGYEGGA
KSAQPAWDDYMKAALEGVPEQPLTPPPGIVTVNIDRSTGKLANGGNSREEYFIEGTQPTQQAVHEVGTTI
IDNGETHELF
>gnl|CDD|236942 PRK11637, PRK11637, AmiB activator; Provisional
MRGKAINTMTRAVKPRRFAIRPILYASVLSAGVLLCAFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQR
ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAFRQGEHT
GLQLILSGEESQRGERILAYFGYLNQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKL
EQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAEREAREAARVRDKQKQAKRK
GSTYKPTESERSLMSRTGGLGRPRGQAFWPVRGPTLHRFGEQLQGELRWKGMVIGASEGTEVKAIADGRV
LLADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGAQVRAGQPIALVGSSGGQGRPSLYFEIRRQGQAV
NPQPWLGR
>gnl|CDD|236943 PRK11638, PRK11638, ECA polysaccharide chain length modulation protein
KPAVSAENELDIRGLCRTLWAGKLWIIGMALLFALIALGYSFLARQEWSATAITDRPTVNMLGGYYSQQQ
FLRNLDIRSNSALSADQPSIMDEAYKEFIMQLAAYDTRREFWLQTDYYKQRMEGNAKADAALLDELINNI
QFTPGDDTKAINDSVKLIAETAPDANNLLRQYVAFASQRAASHLNDELKGAWAARTIQMKAQVKRQEAVA
KAIYDREVNSVEQALKIAEQQGISRSQTDVPAEELPDSELFLLGRPMLQARLENLQAVGPAFDLDYDQNR
AMLATLNVGPTLDPRFQTYRYLRTPEEPVKRDSPRRAFLMIMWGAVGALVGAGVALTRRRRK
>gnl|CDD|183251 PRK11639, PRK11639, zinc uptake transcriptional repressor Zur
MEKTTTQELLAQAEKLCAQRNVRLTPQRLEVLRLMSLQPGAISAYDLLDLLREAEPQAKPPTVYRALDFL
LEQGFVHKVESTNSYVLCHLFDQPTHTSAMFICDRCGAVKEECAEGVEDIMHTLAAKMGFALRHNVIEAH
GLCAACVEVEACRHPDQCQHDHSVQVKKK
>gnl|CDD|183252 PRK11640, PRK11640, putative transcriptional regulator; Provisional
MQREDVLGEALKLLEQQGLANTTLEMLAERVDYPLDELQRFWPDREALLYDALRYHSQQIDTWRRQLLLD
ETLSAEQKLLARYQALSECVSNNRYPGCLFIAACSFYPDPDHPIHQLAEQQKQASYDFTHELLTELEIDD
PAMVAKQMELILEGCLSRLLVKRSQADVDTAKRLAEDILRFAQCRKNGALT
>gnl|CDD|236944 PRK11642, PRK11642, ribonuclease R
MSQDPFQEREAEKYANPIPSREFILEHLTKREKPASREELAVELNIEGEEQLEALRRRLRAMERDGQLVF
TRRQCYALPERLDLLKGTVIGHRDGYGFLRVEGRKDDLYLSSEQMKTCIHGDQVLAQPLGADRKGRREAR
IVRVLVPKTSQIVGRYFTDAGVGFVVPDDSRLSFDILIPPEQIMGARMGFVVVVELTQRPTRRTKAVGKI
VEVLGDNMGTGMAVDIALRTHEIPYIWPQAVEQQVAGLKEEVPEEAKAGRVDLRDLPLVTIDGEDARDFD
DAVYCEKKRGGGWRLWVAIADVSYYVRPPTPLDREARNRGTSVYFPSQVVPMLPEVLSNGLCSLNPQVDR
LCMVCEMTISSKGRLTGYKFYEAVMSSHARLTYTKVWHILQGDQDLREQYAPLVKHLEELHNLYKVLDKA
REERGGISFESEEAKFIFNAERRIERIEQTQRNDAHKLIEECMILANISAARFVEKAKEPALFRIHDKPS
TEAITSFRSVLAELGLELPGGNKPEPRDYAELLESVADRPDAEMLQTMLLRSMKQAIYDPENRGHFGLAL
QSYAHFTSPIRRYPDLSLHRAIKYLLAKEQGHKGNTTETGGYHYSMEEMLQLGQHCSMTERRADEATRDV
ADWLKCDFMLDQVGNVFKGVISSVTGFGFFVRLDDLFIDGLVHVSSLDNDYYRFDQVGQRLIGESSGQTY
RLGDRVEVRVEAVNMDERKIDFSLISSERAPRNVGKTAREKAKKGDAGKKGGKRRQVGKKVNFEPDSAFR
GEKKAKPKAAKKDARKAKKPSAKTQKIAAATKAKRAAKKKVAE
>gnl|CDD|236945 PRK11644, PRK11644, signal transduction histidine-protein kinase/phosphatase UhpB
MFSRLITVIACFFIFSAAWFCLWSISLHLVERPELAVLLFPFGLRLGLMLQCPRGYWPVLLGAEWLLIYW
LAQAVGLPHWLLLLIGSLLTLLPVALASRYRHQRDWRTLLLQGAALTAAALLQSLPWLWHGKEGWNALLL
TLTGGLTLAPTCLLFWHYLAQNTWLPLGPSLVSQPVNWRGRHIVWYLLLFVLSIWLQLGLPDELSRFTPF
CLAIPIIALAWRYGWQGALLATLLNAIALIASQTWHDHPVDLLLSLLAQSLTGLLLGAGIQRQRELNQSL
QKELARNRHLAERLLETEESVRRDVARELHDEIGQTITAIRTQAGIIKRLAADNASVKQSAQLIEQLSLG
VYDTVRRLLGRLRPRQLDDLTLEQAIRSLMREMELEDRGIVSHLDWRIDESALSETQRVTLFRVCQEGLN
NIVKHADASAVTLQGWQQDERLMLVIEDDGSGLPPGSGQQGFGLRGMRERVTALGGTLTISCTHGTRLSV
SLPQR
>gnl|CDD|183255 PRK11646, PRK11646, multidrug efflux MFS transporter MdtH
MSRVSQARNLGKYFLLIDNMLVVLGFFVVFPLISIRFVDQLGWAAVMVGIALGLRQFIQQGLGIFGGAIA
DRFGAKPMIVTGMLMRAAGFATMAIAHEPWLLWLSCILSGLGGTLFDPPRTALVIKLIRPHQRGRFFSLL
MMQDSAGAVIGALLGSWLLQYDFRLVCATGAVLFVLAAAFNAWLLPAYKLSTVRTPVREGMTRVLRDKRF
VTYVLTLTGYYMLAVQVMLMLPIMVNDIAGSPSAVKWMYAIEACLSLTLLYPIARWSEKRFRLEHRLMAG
LLIMSLSMFPIGMVSNLQQLFTLICLFYIGSIIAEPARETLSASLADARARGSYMGFSRLGLALGGAIGY
IGGGWLFDLGKALNQPELPWMMLGIIGLITLLALYWQFSQKRIARRMLER
>gnl|CDD|183256 PRK11648, PRK11648, metal-dependent hydrolase
MTAEGHLLFSIACAIFAKKAELTPVLAQGDWWHIIPGAILTCLLPDIDHPKSFLGQRLKWISKPIARAFG
HRGFTHSLLAVFALLALFYLKVPESWPIPADALQAMVLGYLSHILADMLTPAGVPLLWPCRWRFRLPILV
PQKGNQLERFLCMALFVFAVWMPQSLPENSAVRWSSQMINTLQIQFHRLIKHQVE
>gnl|CDD|236946 PRK11649, PRK11649, putative peptidase; Provisional
MQQIARSIALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHPESAPIVKTIELEKSEIRSLLPEASEPI
DQAAQEDEAIPQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMSDISQLAAQDKELRNLKIGQQLS
WTLTADGDLQRLTWEVSRRETRTYDRTGNGFKETSEMQQGEWVNSVLKGTVGGSFVASAKNAGLTSAEIS
AVIKALQWQMDFRKLKKGDEFSVLMSREMLDGKSEQSQLLGVRLRSGGKDYYAIRAEDGKFYDRNGSGLA
KGFLRFPTAKQFRISSNFNPRRLNPVTGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIR
HGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGK
DRREYLAQVKEVVPQLRFD
>gnl|CDD|236947 PRK11650, ugpC, sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC
MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE
LEPADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQR
QRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNG
GVAEQIGTPVEVYEKPASTFVASFIGSPAMNLLDGRVSADGAAFELAGGIALPLGGGYRQYAGRKLTLGI
RPEHIALSSAEGGVPLTVDTVELLGADNLAHGRWGGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDAD
TGRRIE
>gnl|CDD|183259 PRK11652, emrD, multidrug transporter EmrD
MKRQRNVNLLFMLVLLVAVGQMAQTIYVPAIADMARDLNVREGAVQAVMAAYLLTYGLSQLFYGPLSDRV
GRRPVILVGMSIFILGTLVALFAHSLTVLIAASAIQGLGTGVGGVMARTLPRDLYEGTQLRHANSLLNMG
ILVSPLLAPLIGGLLTTLFGWRACYLFLLLLGAGVTFSMARWMPETRPADARRTRVLASYRTLLSNRRFN
CYLLMLIGTLAGIAVFEACSGVLMGAVLGLSSMTVSILFILPIPAAFFGAWFAGRPNKRFSTLMWQSVIC
CLLAGLLMWIPGWFGVMNVWTLLVPAALFFFGAGMLFPLATSGAMEPFPYLAGTAGALLGGLQNIGSGLA
ALLSAMLPQTGQFSLGLLMTLMGLLILLCWLPLATRMSHQGQPV
>gnl|CDD|236948 PRK11653, PRK11653, DUF1190 family protein
MKRTKSINHASFRKNWRSRHLAPVALAVAAVFMLAGCEKSDETVSLYQNADDCSAANPSKSAECTTAYNN
ALKEAERTAPKYATREDCVAEFGEGQCQQAPAQAGMAPEQAAAQQSSGSFWMPLMAGYMMGRLMGGGAGF
AQQPLFTSKNPASPAYGKYVDADGKNYGAATPGRTMTVPKTAMAPKPATTTTITRGGFGESVAKQSSMQR
SSSSSSGTSSRSMGG
>gnl|CDD|236949 PRK11655, ubiC, chorismate pyruvate lyase; Provisional
MSHPALTILRALRWFDEIPALPPQLLDWLMEEDSMTKRFEQQCKRVSVTLIREGFVTQDELGEEAELLPK
ESRYWLREIVLCGDGEPWLAGRTVVPESTLSGPELALQKLGTTPLGRYLFTSSTLTRDFIEIGRDAGLWA
RRSRLRLSGKPLLLTELFLPASPLYTSCG
>gnl|CDD|183262 PRK11657, dsbG, disulfide isomerase/thiol-disulfide oxidase; Provisional
MKRMLKLILLLALLPLSAAAEELPAPVKALEKQGITIIKTFDAPGGLKGYAAKYQDMGVTIYLTPDGKHA
ISGYMYDEKGENLSEALLEKEVYAPMGREMWQRLEQSHWILDGKADAPRIVYVFADPNCPYCKQFWQQAR
PWVDSGKVQLRHILVGIIKPDSPGKAAAILAAKDPAKALQEYEASGGKLGLKPPASIPAAVRKQLADNQK
LMDDLGANATPAIYYMDKDGTLQQVVGLPDPAQLAEIMGPR
>gnl|CDD|183263 PRK11658, PRK11658, UDP-4-amino-4-deoxy-L-arabinose aminotransferase
MSDFLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGI
GPGDEVITPSLTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAI
RAIGERYGIPVIEDAAHAVGTYYKGRHIGARGTAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHG
LGVDAFDRQTQGRAPQAEVLTPGYKYNLADINAAIALVQLAKLEALNARRREIAARYLQALADLPFQPLS
LPAWPHQHAWHLFIIRVDEERCGISRDALMEALKERGIGTGLHFRAAHTQKYYRERFPTLSLPNTEWNSE
RICSLPLFPDMTDADVDRVITALQQIAGQ
>gnl|CDD|183264 PRK11659, PRK11659, cytochrome c nitrite reductase pentaheme subunit; Provisional
LRSLLTAGVLASGLLWSLNGITATPAAQASDDRHEVTLQRDPDAACLQCHKPDKETMHGKHASAINPNNG
KPVTCTNCHGNISPDHREGVKDVMRFNPPMYSVLEQNSVCMSCHLPEKLREAFWPHDVHATKLTCASCHS
LHPQKDTMQTLSDKQRIKLCVDCHSDQRTNPNFNPASVPLLKE
>gnl|CDD|183265 PRK11660, PRK11660, putative transporter; Provisional
MHKAHLFSVRPFSALIDACWKEKYTAARFTRDLIAGITVGIIAIPLAMALAIASGVPPQYGLYTAAVAGI
VIALTGGSRFSVSGPTAAFVVILYPVSQQFGLAGLLVATLMSGIILILMGLARLGRLIEYIPLSVTLGFT
SGIGIVIATLQIKDFFGLQMAHVPEHYLEKVGALFQALPTINWGDALIGIVTLGVLILWPRLKIRLPGHL
PALLAGTAVMGVLNLLGGHVATIGSRFHYVLADGSQGNGIPPLLPQFVLPWNLPGADGQPFTLSWDLIRA
LLPAAFSMAMLGAIESLLCAVVLDGMTGTKHSANSELVGQGLGNIVAPFFGGITATAAIARSAANVRAGA
TSPISAVIHALLVLLALLVLAPLLSYLPLSAMAALLLMVAWNMSEAHKVVDLLRHAPKDDIIVMLLCMSL
TVLFDMVIAISVGIVLASLLFMRRIAEMTRLAPISVQDVPDDVLVLRINGPLFFAAAERLFTELESRTEG
KRIVVLQWDAVPVLDAGGLDAFQRFVKRLPEGCELRICNLQFQPLRTLARAGIQPIPGRLAFYPTLREAL
ADLLRNEA
>gnl|CDD|183266 PRK11663, PRK11663, glucose-6-phosphate receptor/MFS transporter UhpC
PADAPLITDKHEIDARYRYWRRHILITMYLGYALFYFTRKSFNAAMPEMLADLGLSRSDIGLLATLFYIT
YGVSKFVSGIVSDRSNARYFMGIGLIATGIINILFGFSSSLWAFALLWVLNAFFQGWGWPVCAKLLTAWY
SRTERGGWWAIWNTAHNVGGALIPLVVGAIALHYGWRYGMMIAGIIAIVVGLFLCWRLRDKPQAMGLPSV
GEWRHDALELAQQQEGAGLSRKEILTKYVLLNPYIWLLSFSYVLVYVVRAAINDWGNLYMSETLGVDLVT
ANSAVSMFELGGFIGALVAGWGSDKLFNGNRGPMNLIFAAGILLSVGSLWLMPFASYVMQAACFFTIGFF
VFGPQMLIGMAAAECSHKEAAGAATGFVGLFAYLGAALSGYPLAKVLEIWHWTGFFVVISIAAGISALLL
LPFLNAQAPREASE
>gnl|CDD|236950 PRK11664, PRK11664, ATP-dependent RNA helicase HrpB; Provisional
MSSLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLLQHGGINGKIIMLEPRRLAARNVAQRLAE
QLGEKPGETVGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLL
DVQQGLRDDLKLLIMSATLDNDRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQRFDEAVARATAELLRQ
ESGSLLLFLPGVGEIQRVQEQLASRVASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLT
IEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQSEP
EILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPR
LAAMLVAAKEDDEAALATAAKLAAILEEPPRSGSSDLGVALSRKQPHWQQRAQQLLKRLNVRGGEADSSL
IAPLLALAFPDRIARRRGQDGRYQLANGMGAMLDADDALSRHEWLIAPLLLQGSASPDARILLALPLDID
ELVQRCPQLVQQSDTVEWDEAKGTLRAWRRLQIGQLTVKVQPLAKPSEEELHQALLNWIRRKGLSVLNWT
PEAEQLRLRLLCAAKWLPEYDWPAVDDESLLASLETWLLPHMTGVRSLRGLKSLNIAQALRGLLDWPQRQ
RLDSELPTHYTVPTGSRIAIRYHEDNPPALAVRMQEMFGEAQSPTIAQGRVPLVLELLSPAQRPLQITRD
LAAFWQGAYREVQKEMKGRYPKHVWPDDPANTAPTRRTKKYS
>gnl|CDD|236951 PRK11667, PRK11667, hypothetical protein; Provisional
MMKTIKHLLCCAILAAALISTGAHAASLGDSLSSAASQLGGQAGSSQQGGWSLSSLTGLLSGGGQALSAG
SMNNAAGILQYCAKNNYLSATGAESVKDQLLGKLGLGSTEQKSDTNYLSGLQGLLKTGDGQQLNLSNIGT
TPLKEKVKTKACDLVLKQGKSFL
>gnl|CDD|236952 PRK11669, pbpG, D-alanyl-D-alanine endopeptidase; Provisional
MKFRVSLLSLLLLLAGVPFAPQAVAKTAAATTASQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASIT
KLMTAMVVLDAKLPLDEKLKVDISQTPEMKGVYSRVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGG
YKAFIKAMNAKAKALGMTNTRYVEPTGLSIHNVSTARDLTKLLIASKQYPLIGQLSTTREKTATFRKPNY
TLPFRNTNHLVYRDNWNIQLTKTGFTNAAGHCLVMRTVINNRPVALVVLDAFGKYTHFADASRLRTWIET
GKVTPVPAAALSYKKQKAAQMAAAQS
>gnl|CDD|183270 PRK11670, PRK11670, iron-sulfur cluster carrier protein ApbC
MNEQSQAKSPEALRAMVAGTLANFQHPTLKHNLTTLKALHHVALLDDTLHIELVMPFVWNSAFEELKEQC
SAELLRITGAKAIDWKLSHNIATLKRVNNQPGVNGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVG
ILDADIYGPSIPTMLGAEDQRPTSPDGTHMAPIMAHGLATNSIGYLVTDDNAMVWRGPMASKALMQMLQE
TLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSM
HICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPESEFTAIYRQLADRVA
AQLYWQGEVIPGEISFRAV
>gnl|CDD|183271 PRK11671, mltC, membrane-bound lytic murein transglycosylase MltC
MKKYLALALIAPLLISCSSTKKGDTYNEAWVKDTNGFDILMGQFAHNIENIWGFNEVLIAGPKDYVKYTD
QYQTRSHINFDDGTITIETIAGTNPAAHLRQAIIKTLLMGDDPGSIDLYSDVDDIPISKEPFLYGQVLDN
TGQPIRWEGRASNFADYLLQNKLQSRSNGLRIIYSVTINMVPNHLDKRAHKYLPMVRKASRKYGVDESLI
LAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKDVFRMKGKSGQPSRSYLFDPANNIDTGTAYLAILQNV
YLGGITNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAANIINTMSPGDVYQTLTTRHPSAESRRYLYKVN
TAQKSYRRR
>gnl|CDD|183272 PRK11675, PRK11675, LexA regulated protein; Provisional
MAKEQTDRTTLDLFADERRPGRPKTNPLSRDEQLRINKRNQLKRDKVRGLKRVELKLNADLVDALNELAE
ARNISRSELIEEILMKQLAA
>gnl|CDD|236953 PRK11677, PRK11677, DUF1043 family protein
MTWEYALIGLVVGIIIGAVAMRFGNRKLRQQQALQYELEKNKAELEEYRQELVSHFARSAELLDTMAKDY
RQLYQHMAKSSSELLPNLPAQDNPFRNRLAESEASNDQAPVQMQPRDYSEGASGLLRGGNAKRD
>gnl|CDD|236954 PRK11678, PRK11678, putative chaperone; Provisional
MFIGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTREAVSEWLYRHLDVPAYDDERQALLRRA
IRYNREEDIDVTAQSVFFGLAALAQYLEDPEEVYFVKSPKSFLGASGLKPQQVALFEDLVCAMMLHIKQQ
AEAQLQAAITQAVIGRPVNFQGLGGEEANRQAEGILERAAKRAGFKDVEFQFEPVAAGLDFEATLTEEKR
VLVVDIGGGTTDCSMLLMGPSWRGRADRSASLLGHSGQRIGGNDLDIALAFKQLMPLLGMGSETEKGIAL
PSLPFWNAVAINDVPAQSDFYSLANGRLLNDLIRDAREPEKVARLLKVWRQRLSYRLVRSAEEAKIALSD
QAETRASLDFISDGLATEISQQGLEEAISQPLARILELVQLALDQAQVKPDVIYLTGGSARSPLIRAALA
QQLPGIPIVGGDDFGSVTAGLARWAQVVFR
>gnl|CDD|236955 PRK11679, PRK11679, outer membrane protein assembly factor BamC
MAYSVQKSRVAKVAGVSLVMLLAACSSDQRYKRQVSGDESYLEAPPLKELHAPAGMILPLQNGDYDIPVT
NGSGAVGKALDIRPPAQPLALLSGARTQFSGDTATLLLENSPENSKLWPQVVSVLQAKNYPIAKRDDASQ
TLTTDWVTWNRADEDVQYRGRYQISVKPQGYQQALTVKLLDLEQGGKPVTDPANIQRYNTEMLNLISAGL
DKQATDEANAAANRLVGQIDVQSGADDTGLPVLIVRAPYNVVWQRLPAALEKVGMKVTDRTRSQGTVAVT
YKPPSDSFWQELGAKDPELASGDYKLQVGDLDNRSSLQFIDPKGHPLTQSQNDALVAVFQAAFSKT
>gnl|CDD|183276 PRK11688, PRK11688, thioesterase family protein
STVLTQEEALKLVGEIFVYHMPFNRLLGLELERLEPDFVELSFKMQPELVGNIAQSILHGGVIASVLDVA
GGLVCVGGILARHEDISEEELRQRLSRLGTIDLRVDYLRPGRGERFTATSSVLRAGNKVAVARMELHNEQ
GVHIASGTATYLVG
>gnl|CDD|183277 PRK11689, PRK11689, aromatic amino acid efflux DMT transporter YddG
TSQKATLIGLIAILLWSTMVGLIRGVSESLGPVGGAAMIYSVSGLLLLLTVGFPRLRQFPKRYLLAGGLL
FVSYEICLALSLGYANTRRQAIEVGMVNYLWPSLTILFAVLFNGQKANWLLIPGLLLALAGVAWVLGGDN
GLSLAELINNIASNPLSYGLAFIGAFIWAAYCNVTRKYARGKNGITLFFILTALALWIKYFLSPQPAMVF
SLPAIIKLLLAAAAMGFGYAAWNVGILHGNMTLLATASYFTPVLSAALAALLLSTPLSFSFWQGVAMVTA
GSLLCWLATRRKRRT
>gnl|CDD|236956 PRK11697, PRK11697, two-component system response regulator BtsR
MIKVLIVDDEPLAREELRELLQEEGDIEIVGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGMLD
PEHMPYIVFVTAFDEYAIKAFEEHAFDYLLKPIDPARLAKTLARLRQERSPQDVLLPEAQPPLKHIPCTG
HNRIKLLPLEEVEFVSSRLSGVHVVSAEGKGFTELTLKTLEEKTPLLRCHRQYLVNPAAIQEIRLLDNGQ
AEIITRSGHTVPVSRRYLKSLKEALGLQ
>gnl|CDD|236957 PRK11700, PRK11700, VOC family protein
MANWQSIDELQDLLADLPRFEQKIQELADRLGLDLSQLEADHIALRCNQNETAERWRQGFLQCGELLSEN
IINGRPICLFELDQPLQVGHWSIDCVELPYPGEKRYPHEGWEHIELVLPGDPETLDARALALLSDEGLSL
PGIKVKTSSPKGEGERLPNPTLAVTDGGICIKFHPHSIKEIVASEQA
>gnl|CDD|183280 PRK11701, phnK, phosphonate C-P lyase system protein PhnK; Provisional
MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDG
QLRDLYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEI
DAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTH
DLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLLVSSVLQV
>gnl|CDD|183281 PRK11702, PRK11702, hypothetical protein; Provisional
MAKNRSRRLRKKMHIDEFQELGFSVNWRFPEGTSEEQIDATVDAFIDEVIEPNGLAFDGSGYLAWEGLIC
LQKIGKCTEEHRALVKKWLEGRKLTDVEVSELFDIWWD
>gnl|CDD|183282 PRK11705, PRK11705, cyclopropane fatty acyl phospholipid synthase
MSSSCIEEVSVPDDNWYRIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCD
RLDEFFSRVLRAGLDEKLPHHLKDTLRILRARLFNLQSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCG
YWKDADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERC
AGLPVEIRLQDYRDLNGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPW
INKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYDRTLMAWHENFEAAWPELADNYSERFYRMWRYY
LLSCAGAFRARDIQLWQVVFSPRGVEGGYRVPR
>gnl|CDD|183283 PRK11706, PRK11706, TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
MIPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQP
GDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMA
LAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALLINDPALIERAEIIREKGT
NRSQFFRGQVDKYTWVDIGSSYLPSELQAAYLWAQLEAADRINQRRLALWQRYYDALAPLAEAGRIELPS
IPDDCKHNAHMFYIKLRDLEDRSALINFLKEAGIMAVFHYIPLHSSPAGERFGRFHGEDRYTTKESERLL
RLPLFYNLTDVEQRTVIDTILEFFS
>gnl|CDD|236958 PRK11709, PRK11709, putative L-ascorbate 6-phosphate lactonase; Provisional
MSKVKEITRESWILSTFPEWGTWLNEEIEQEVVPPGTFAMWWLGCTGIWLKTEGGTNVCVDLWCGTGKQT
HGNPLMKRGHQMARMAGVRKLQPNLRTQPFVLDPFAIREIDAVLATHDHSDHIDVNVAAAVLQNCADHVK
FIGPQACVDLWIGWGVPKERCIVVKPGDVVKVKDIKIHALDSFDRTALVTLPADGKAAGGVLPDDMDRRA
VNYLFKTPGGNIYHSGDSHYSNYFAKHGNDHQIDVALGSYGENPRGITDKMTSIDILRMAESLNAKVVIP
VHHDIWSNFQADPQEILVLWKMRKDRLQYGFHPFIWQVGGKFTYPQDKDRFEYHYPRGFDDCFTIEPDLP
FKSFL
>gnl|CDD|183285 PRK11712, PRK11712, ribonuclease G; Provisional
MTAELLVNVTPSETRVALIEGGILQEIHIEREAKRGIVGNIYKGRVSRVLPGMQAAFVDIGLDKAAFLHA
SDIVPHTECVAGEEQKQFVVRDISELVRQGQDIMVQVVKDPLGTKGARLTTDITLPSRYLVFMPGASHVG
VSQRIESEEERERLKKIVAPYCDEQGGFIIRTAAEGVGEEELAQDAAFLKRLWTKVMERKKRYQTRYQLY
GELALAQRVLRDFVGAELDRIRVDSRLTYEELKEFTSEYIPEMTDKLEHYSGRQPIFDLYDVENEIQRAL
ERKVELKSGGYLIIDQTEAMTTVDINTGAFVGHRNLEETIFNTNIEATQAIARQLRLRNLGGIIIIDFID
MNNEDHRRRVLHSLEQALSKDRVKTNINGFSQLGLVEMTRKRTRESLEHVLCGECPTCHGRGTVKTVETV
CYEIMREIVRVHHAYDSDRFLVYASPAVAEALKGEESHALAELEIFVGKQVKVQIEPLYNQEQFDVVMM
>gnl|CDD|236959 PRK11713, PRK11713, 16S ribosomal RNA methyltransferase RsmE; Provisional
MPRLFVLLAAGETLILDGEEAHHLVRVLRLKEGDELRLFDGDGGEYLAEITEIGKKEVELEILEKLELEP
EPPLRLTLAQALPKGDRLELILQKATELGVSAIIPLISERSVVKLDGERADKKLERWQKIAIEAAEQSGR
TRIPEVRPPISLKEFLEELLPADLKAGLKLVLHPEAGGKVLLLIGPEGGFSPEEIELLREAGFTPVSLGP
RILRTETAALAALAALQALLGDLG
>gnl|CDD|236960 PRK11715, PRK11715, cell envelope integrity protein CreD
MLKSSLLLKILTIGGLILLLLIPLMMIRGLIRERSDYRDEVVDEIAQSWGGPQTLVGPVLVIPYTELYTV
TEEDKTVERKRSFRHYTKELYFLPESLNVDGNLKVEERKRGIYQAQVYHADLTLKGSFDVPRLSELDLPN
GAETILLGKAFLVLGVSDARGIGNVPKLQVNGQALTFEPGTGLELLGQGVHAPLPELDLAQQNLDFDFAL
NLRGTGSLSVVPLGRNTEVTLTSNWPHPSFVGDFLPAEREISESGFQAQWQVSHLARNYPQVFASGQDGN
LNLPAFGVSLIDPVDQYQKTERAVKYAILFIALTFAAFFLFELLKKLRIHPVQYLLVGLALVLFYLLLLS
LSEHIGFTLAYLIAALACVLLIGFYLSAVLRSWKRGLLFAAALAALYGVLYGLLQSEDYALLLGSLLLFA
VLALVMFLTRRIDWYA
>gnl|CDD|236961 PRK11716, PRK11716, HTH-type transcriptional activator IlvY
MHVSPSTLSRQIQRLEEELGQPLFVRDNRSVTLTEAGEELRPFAQQTLLQWQQLRHTLDQQGPSLSGELS
LFCSVTAAYSHLPPILDRFRAEHPLVEIKLTTGDAADAVEKVQSGEADLAIAAKPETLPASVAFSPIDEI
PLVLIAPALPCPVRQQLSQEKPDWSRIPFILPEHGPARRRIDLWFRRHKIKPNIYATVSGHEAIVSMVAL
GCGVGLLPEVVLENSPVRNRVQILERVPPITPFELGVCVQKKRLEEPLIDAFWQLLENH
>gnl|CDD|236962 PRK11718, PRK11718, sigma D regulator
MLNQLENAQERWGGSNKLIDRWLHERQQLLVAYCKLAGIKPGKESLSLPNEKALDDFCQLLVDYVSAGHF
EIYEQLVHEAEAFGDLALALAAQIYPRLEATTQQALDFNDKYLETAIDDDNLLEFQQDLSDLGEALEERF
ELEDKLIELLHDAHSEPPAAA
>gnl|CDD|236963 PRK11720, PRK11720, UDP-glucose--hexose-1-phosphate uridylyltransferase
MTQFNPVDHPHRRYNPLTGQWVLVSPHRAKRPWQGQQETPAKETLPAYDPDCFLCPGNTRVTGDVNPDYT
GTYVFTNDFAALMPDTPDAPESDDPLFRCQSARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAE
LGKTYPWVQVFENKGAAMGCSNPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGE
RIVVETEHWLAVVPYWAAWPFETLLLPKAHVLRLTDLTDAQRDDLALALKKLTSRYDNLFQCSFPYSMGW
HGAPFNGEENDHWQLHAHFYPPLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRAVSDIHYRES
>gnl|CDD|236964 PRK11727, PRK11727, 23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF
RTKSNKKKMSAQKPGLHPRNRHRGRYDFAALIQSHPELKPFVILNPYGEQSIDFANPLAVKALNKALLAH
FYGVAHWDIPAGYLCPPIPGRADYIHHLADLLAEDNGGVIPRGANVRVLDIGVGANCIYPLIGVHEYGWR
FVGSDIDPQALASAQAIISANPGLNGAIRLRLQKDSKAIFKGIIHKNERFDATLCNPPFHASAAEARAGS
QRKLRNLGLNKDKKKVLNFGGQQAELWCEGGEVAFIKRMIEESKAFAKQVLWFTSLVSKKENLPPLYRAL
KKVGAVEVKTIEMAQGQKQSRFIAWTFLDDEQRRRWVNRRW
>gnl|CDD|183292 PRK11728, PRK11728, L-2-hydroxyglutarate oxidase
AMYDFVIIGGGIVGLSTAMQLQERYPGARIAVLEKESGPARHQTGHNSGVIHAGVYYTPGSLKARFCRRG
NEATKAFCDQHGIPYEECGKLLVATSELELERMEALYERARANGIEVERLDAEELREREPNIRGLGAIFV
PSTGIVDYRAVAEAMAELIQARGGEIRLGAEVTALDEHANGVVVRTTQGEYEARTLINCAGLMSDRLAKM
AGLEPDFRIVPFRGEYYRLAPEKNQLVNHLIYPVPDPAFPFLGVHLTRMIDGSVTVGPNAVLAFKREGYR
KRDFSLRDLLEILTYPGFWKLAQKHWRSGLGEMKNSLSKSGYLRLVQKYCPSLTLSDLQPYPAGVRAQAV
SRDGKLVDDFLFVETPRSLHVCNAPSPAATSSLPIGEHIVSKV
>gnl|CDD|183293 PRK11730, fadB, fatty acid oxidation complex subunit alpha FadB
MIYQGKTLQVDWLEDGIAELVFDAPGSVNKLDRATLASLGEALDALEAQSDLKGLLLTSAKDAFIVGADI
TEFLSLFAAPEEELSQWLHFANSIFNRLEDLPVPTVAAINGYALGGGCECVLATDYRVASPDARIGLPET
KLGIMPGFGGTVRLPRLIGADNALEWIAAGKDVRAEDALKVGAVDAVVAPEKLQEAALALLKQAIAGKLD
WKARRQPKLEPLKLSKIEAMMSFTTAKGMVAQKAGKHYPAPMTAVKTIEAAAGLGRDEALELEAKGFVKL
AKTNVARALVGIFLNDQYVKGKAKKLAKDAKPVKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALD
LGMTEAAKLLNKQVERGKIDGAKMAGVLSSIRPTLDYAGFERVDVVVEAVVENPKVKAAVLAEVEQKVRE
DTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEVIRGEKTSDETIATVVAYASKMGKTPIV
VNDCPGFFVNRVLFPYFAGFSQLLRDGADFRQIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAEGF
PDRMKKDYRDAIDVLFEAKRFGQKNGKGFYRYEEDKKGKPKKEVDPAVYELLAPVVQPKREFSDEEIIAR
MMIPMINEVVRCLEEGIVASPAEADMALVYGLGFPPFRGGAFRYLDTLGVANYVALADKYAHLGPLYQVP
EGLREMAANGESYYP
>gnl|CDD|236965 PRK11742, PRK11742, bifunctional NADH:ubiquinone oxidoreductase subunit C/D; Provisional
VIGELRNRFGPDAFTVQATRTGIPVVWVKREQLLEVLRFLRKLPKPYVMLFDLHGIDERLRTHREGLPAA
DFTVFYHLISIERNRDIMLKVALSENDLHVPTITKIFPNANWYERETWDMFGITFDGHPHLRRILMPPTW
EGHPLRKDYPARATEFDPFELTKAKQDLEMEALRFKPEEWGMKRGTDNEDFMFLNLGPNHPSAHGAFRIV
LQLDGEEIVDCVPDIGYHHRGAEKMGERQSWHSYIPYTDRIDYLGGCMNEMPYVLAVEKLAGITVPDRVN
VIRVMLSELFRINSHLLYIGTFIQDVGAMTPVFFAFTDRQKIYDVIEAITGFRMHPAWFRIGGVAHDLPR
GWDRLLREFLDWMPKRLDEYEKAALRNSILKGRTQGVAAYNAKEALEWGVTGAGLRATGIDFDVRKARPY
SGYENFDFEVPVGGNGDCYDRVMVKVEEMRQSLRIIEQCLDNMPEGPFKADHPLTTPPPKERTLQHIETL
ITHFLQVSWGPVMPANESFQMIEATKGINSYYLTSDGSTMSYRTRIRTPSFAHLQQIPSVIRGSLVSDLI
VYLGSIDFVMSDVDR
>gnl|CDD|236966 PRK11747, dinG, ATP-dependent DNA helicase DinG; Provisional
MLTDALKAQIRQAYKALQEQLPGFIPRAGQRQMIAEVAKTLAGEYLKDGRILVIEAGTGVGKTLSYLLAG
IPIARAEKKKLVISTATVALQEQLVSKDLPLLLKISGLDFKFTLAKGRGRYVCPRKLAALASDEGTQQDL
LLFLDDELTPPDEEEQKLLARLAKALATGKWDGDRDHWPEPIDDSLWQRITTDKHSCLGRNCPYFRECPF
FKARREIDEADVVVANHDLVLADLELGGGVVLPDPENLLYVLDEGHHLPDVARDHFAASAELKGTADWLE
KLLKLLTKLVALIMEPPLALPERLNAHCEELRELLASLNQILNLFLPAGGEEARYRFEMGELPEELLELA
ERLAKLTEKLLGLLEKLLNDLSEAMKTGKIDIVRLERLLLELGRALGRLEALSKLWRLAAKEDQESGAPM
ARWITREERDGQGDYLFHASPIRVGDQLERLLWSRAPGAVLTSATLRSLNSFDRFQEQSGLPEKDGDRFL
ALPSPFDYPNQGKLVIPKMRAEPDNEEAHTAEMAEFLPELLEKHKGSLVLFASRRQMQKVADLLPRDLRL
MLLVQGDQPRQRLLEKHKKRVDEGEGSVLFGLQSFAEGLDLPGDYLTQVIITKIPFAVPDSPVEATLAEW
LKSRGGNPFMEISVPDASFKLIQAVGRLIRSEQDRGRVTILDRRLLTKRYGKRLLDALPPFKREIEE
>gnl|CDD|236967 PRK11749, PRK11749, dihydropyrimidine dehydrogenase subunit A; Provisional
LKFLTTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEG
NLKGAAETILETNPLPAVCGRVCPQERLCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLFKRAPKTG
KKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTN
TEVGRDITLDELRAGYDAVFIGTGAGLPRFLGIPGENLGGVYSAVDFLTRVNQAVADYDLPVGKRVVVIG
GGNTAMDAARTAKRLGAESVTIVYRRGREEMPASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFV
RMELGEPDASGRRRVPIEGSEFTLPADLVIKAIGQTPNPLILSTTPGLELNRWGTIIADDETGRTSLPGV
FAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEGAASA
>gnl|CDD|236968 PRK11750, gltB, glutamate synthase subunit alpha; Provisional
MHMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFR
AVAEEAGWRLAKNYAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRI
EQVFVNAPAGWRERDFERRLFIARRRIEKRLADDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRL
ESAICVFHQRFSTNTLPRWPLAQPFRYLAHNGEINTITGNRQWARARAYKFQTPLIPDLQEAAPFVNETG
SDSSSLDNMLELLLAGGMDLFRAMRLLVPPAWQNNPDMDPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYA
ACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGPGELLVIDTRTGRILHSAEIDNDLK
SRHPYKEWLEKNVRRLVPFEELPDEQVGSRELDDDTLKSYQKQFQYSFEELDQVIRVLAENGQEAVGSMG
DDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGHAHRVIFKSPVL
SYSDFKQLTTLDEEHYRADTLDLNYDPEETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLPIPA
AMAVGAVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQ
VMLNYRKGINKGLYKIMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNL
SKRAWLARKPIDQGGLLKYVHGGEYHAYNPDVVNTLQKAVQSGDYSDYQEYAKLVNERPVATLRDLLALK
PADNPIPLDEVEPAEELFKRFDSAAMSIGALSPEAHEALAIAMNRLGGRSNSGEGGEDPARYGTEKVSKI
KQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQLPGDKVNPLIARLRYSVPGVTLISPPPHHDIYSI
EDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITISGYDGGTGASPLTSVKYAGSPWEL
GLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATGV
ATQDEKLRKNHYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGETAKQQKLDLSPL
LETAEPPAGKALYCTEERNPPFDKGLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRH
GNQGMADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAIIG
NTCLYGATGGKLFAAGRAGERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYV
LDEDGDFVDRVNHELVEILRVEDLEIHREHLRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKPKAAD
VKALLGHRSRSAAEL
>gnl|CDD|183298 PRK11752, PRK11752, putative S-transferase; Provisional
MTDNTYQPPKVWTWDKSNGGAFANINRPVAGATHEKTLPVGKHPLQLYSLGTPNGQKVTIMLEELLALGV
KGAEYDAWLIRIGEGDQFSSGFVEINPNSKIPALLDRSGNPPIRVFESGAILLYLAEKFGAFLPKDLAAR
TETLNWLFWQQGSAPFLGGGFGHFYAYAPEKIEYAINRFTMEAKRQLDVLDKQLAEHEYIAGDEYTIADI
AIWPWYGNLVLGNLYDAAEFLDVGSYKHVQRWAKEIAERPAVKRGRIVNRTWGE
>gnl|CDD|236969 PRK11753, PRK11753, cAMP-activated global transcriptional regulator CRP
MMVLGKPQTDPTLEWFLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGD
FIGELGLFEEGQERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMALSAQMARRLQNTSRKVGDLAFLD
VTGRIAQTLLDLAKQPDAMTHPDGMQIKITRQEIGRIVGCSREMVGRVLKMLEDQGLISAHGKTIVVYGT
R
>gnl|CDD|236970 PRK11756, PRK11756, exonuclease III; Provisional
MKFVSFNINGLRARPHQLEAIIEKHQPDVIGLQETKVHDEMFPLEEVEALGYHVFYHGQKGHYGVALLSK
QTPIAVRKGFPTDDEEAQRRIIMATIPTPNGNLTVINGYFPQGESRDHPTKFPAKRQFYQDLQNYLETEL
SPDNPLLIMGDMNISPTDLDIGIGEENRKRWLRTGKCSFLPEEREWLDRLMDWGLVDTFRQLNPDVNDRF
SWFDYRSKGFDDNRGLRIDLILATQPLAERCVETGIDYDIRGMEKPSDHAPIWATFKL
>gnl|CDD|236971 PRK11760, PRK11760, putative 23S rRNA C2498 ribose 2'-O-ribose methyltransferase; Provisional
MNKLLLYCRPGFEKECAAEITDKAAELGVFGYARVKENSGYVIFECYQPDDADRLARELPFSELIFARQM
FVVGELLKDLPPEDRISPIVAALQGVVPKFGELRVETPDTNEGKELSKFCRKFTVPLRQALRKAGVLTAK
ENPKRPVLHVFFIAPGCCYVGYSYSNNSSPWPMGIPRLKFPADAPSRSTLKLEEAFHVFIPRDEWDERLA
PGMRAVDLGAAPGGWTYQLVRRGMFVTAVDNGPMAQSLMDTGQVEHLRADGFKFRPPRKNVDWLVCDMVE
KPARVAELMAQWLVNGWCREAIFNLKLPMKKRYEEVRQCLELIEEQLDENGINAQIQAKQLYHDREEVTV
HLRRLWA
>gnl|CDD|236972 PRK11761, cysM, cysteine synthase CysM
MAYPTLEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEAT
SGNTGIALAMIAAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEGEGKVL
DQFANPDNPLAHYETTGPEIWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEGSSIPG
IRRWPEEYLPKIFDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIARENPNAVIVAI
ICDRGDRYLSTGVFPA
>gnl|CDD|183303 PRK11762, nudE, adenosine nucleotide hydrolase NudE; Provisional
MMKMRQKPEILNRETVAKSRLFRVESVDLEFSNGVERVYERMRPSGRGAVMIVPILDDDTLLLIREYAAG
TERYELGFPKGLIDPGETPLEAANRELKEEVGFGARQLTFLKELSLAPSYFSSKMNIVLAEDLYPERLEG
DEPEPLEVVRWPLADLDELLARPDFSEARSVAALFLAREWLKQQG
>gnl|CDD|236973 PRK11767, PRK11767, SpoVR family protein; Provisional
KDRTPLSDGPDWTFELLQRYLDEIERVAKEYGLDTYPNQIEVITAEQMMDAYSSVGMPINYRHWSFGKHF
IETEQLYRRGQMGLAYEIVINSNPCIAYLMEENTMTMQALVIAHACYGHNSFFKNNYLFRTWTDASSIID
YLVFAKNYIAECEERYGVDAVERLLDSCHALMNYGVDRYKRPQKISLQEEKARQKEREEYLQSQVNDLWR
TLPKREEEKAVEEARRFPSEPQENLLYFIEKNAPLLEPWQREILRIVRKIAQYFYPQRQTQVMNEGWATF
WHYTILNHLYDEGLVTDGFMLEFLHSHTNVVFQPPYNSPYYSGINPYALGFAMFQDIRRICESPTEEDRE
WFPDIAGSDWLETLHFAMRNFKDESFISQFLSPKLIRDFRLFSVLDDDRENYLEVSAIHDEEGYREIREA
LSRQYNLSNLEPNIQVWNVDLRGDRSLTLRHIPHNRRPLDESRDEVLKHLHRLWGFDVHLEEVDEDGSVE
LLERCPPR
>gnl|CDD|236974 PRK11768, PRK11768, serine/threonine protein kinase
MNDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEE
HAFALELAEAEIPVVAPLAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRP
FEHRPTLDLQEYGIEPRDWLLASDLIPSDLRPAYLAAADQLLAAVEACWARGDVRLLRLHGDCHPGNILW
RDGPHFVDLDDARMGPAVQDLWMLLSGDRAEQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSA
WLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQEPPLQL
>gnl|CDD|236975 PRK11770, PRK11770, YccF domain-containing protein
MRLLLNIIWFVLGGFWTALGWLLAGLVSCITIIGIPFGRACFKIAKLSLWPFGKEAVHVDELTKDIGTGA
GGLLLNIIWFIFFGWWLALGHLASGIALCITIIGIPFGIQNFKLAAIALWPFGKRIVSVETAQAA
>gnl|CDD|236976 PRK11773, uvrD, DNA-dependent helicase II; Provisional
MDVSYLLDSLNDKQREAVAAPLGNMLVLAGAGSGKTRVLVHRIAWLMQVENASPYSIMAVTFTNKAAAEM
RHRIEQLLGTSQGGMWVGTFHGLAHRLLRAHWQDANLPQDFQILDSDDQLRLLKRLIKALNLDEKQWPPR
QAQWYINGQKDEGLRPQHIQSYGDPVEQTWLKIYQAYQEACDRAGLVDFAELLLRAHELWLNKPHILQHY
QERFTHILVDEFQDTNAIQYAWIRLLAGDTGKVMIVGDDDQSIYGWRGAQVENIQRFLNDFPGAETIRLE
QNYRSTANILKAANALIANNNGRLGKELWTDGGDGEPISLYCAFNELDEARFVVERIKTWQDNGGALSDC
AILYRSNAQSRVLEEALLQAGIPYRIYGGMRFFERQEIKDALAYLRLIANRNDDAAFERVVNTPTRGIGD
RTLDVVRQTARDRQLTLWQACRALLQEKVLAGRAASALQRFIELIDALAQETADMPLHEQTDRVIKDSGL
RAMYEQEKGEKGQARIENLEELVTATRQFSYPDEDEDLTPLQAFLSHAALEAGEGQADAHEDAVQLMTLH
SAKGLEFPLVFIVGMEEGLFPSQMSLEEGGRLEEERRLAYVGITRAMQKLTLTYAESRRLYGKEVYHRPS
RFIREIPEECVEEVRLRATVSRPVSHQRMGTPAVEANDSGFKLGQRVRHPKFGEGTIVNFEGSGAHARVQ
VAFQGQGIKWLVAAYAKLEAV
>gnl|CDD|236977 PRK11776, PRK11776, ATP-dependent RNA helicase DbpA; Provisional
MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKR
FRVQALVLCPTRELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRK
GTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVES
THDLPAIEQRFYEVSPDERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRD
RDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEE
MQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEMVTLCIDGGKKDKLRPGDILGALTGDAGLDGAQIGK
INVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRLLK
>gnl|CDD|236978 PRK11778, PRK11778, putative inner membrane peptidase; Provisional
FLSEYGLFLAKTVTVVVAIAAVVALIVSLAQRKKSQKGELEVTNLNEQYKEMKEELKAALLDKKELKAWH
KAQKKKEKQEAKAAKAKSKPRLFVLDFKGDIDASEVESLREEITAILAVAKPGDEVLLRLESPGGVVHGY
GLAASQLQRLRDAGIPLTVAVDKVAASGGYMMACVADKIIAAPFAIVGSIGVVAQIPNFHRLLKKHDIDV
ELHTAGEYKRTLTLFGENTEEGREKFREELEETHQLFKDFVQRYRPQLDIDKVATGEHWYGQQALELGLV
DEIQTSDDYLLELMKEHEVLEVRYQQKKKLAERLGGSAAESADRLLLRWW
>gnl|CDD|236979 PRK11779, sbcB, exonuclease I; Provisional
DKKMQPTFLWHDYETFGANPALDRPAQFAGIRTDADLNIIGEPLVFYCKPADDYLPSPEAVLITGITPQE
ALEKGLPEAEFAARIHAEFSQPGTCILGYNNIRFDDEVTRYIFYRNFYDPYAREWQNGNSRWDLLDVVRA
CYALRPEGINWPENEDGLPSFKLEHLTKANGIEHENAHDAMSDVYATIAMAKLIKQKQPKLFDYLFQLRN
KRKVAALIDVPAMKPLVHVSGMFGAERGCTSWVAPLAWHPTNKNAVIVCDLAGDPSPLLELDADTLRERL
YTRRADLAEGELPVPLKLVHLNKCPVLAPAKTLRPEDAERLGIDRQQCLDNLALLRQNPDLREKVVAVFA
EAEPFAPSDDVDAQLYDGFFSDADRRLMEIIRETEPENLAALDLTFDDPRLEELLFRYRARNFPETLDDE
EQQRWLEHRRQRLTPERLQQYAAELEQLAQEYEDDEEKQALLKALYDYAEELVPTL
>gnl|CDD|236980 PRK11780, PRK11780, isoprenoid biosynthesis glyoxalase ElbB
MKKIAVILSGCGVYDGSEIHEAVLTLLALDRAGAEAVCFAPDIPQLHVINHLTGEEMGETRNVLVESARI
ARGEIKDLAEADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAFHQAGKPIGFICIAPAM
LPKILGAGVKLTIGNDEDTAAAIEKMGGEHVDCPVDDIVVDEENKVVTTPAYMLAQSIAEAASGIEKLVS
RVLELAE
>gnl|CDD|236981 PRK11783, rlmL, bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL
MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDL
DLYLGVQAIDWTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRIN
ARLNKGEATISLDLSGESLHQRGYRQATGEAPLKENLAAAILLRSGWPQEGTPLLDPMCGSGTLLIEAAM
MAADIAPGLHRERWGFSGWLGHDEALWQELLEEAQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAG
VAELITFEVKDVADLKNPLPKGPTGLVISNPPYGERLGEEPALIALYSQLGRRLKQQFGGWNAALFSSSP
ELLSCLGLRADKQYKLKNGALECVLKNYTIAEESTSSDAEGAQDFANRLRKNLKKLKKWAKQEGIECYRL
YDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLGIPPNKVVLKTRERQKGKNQ
YQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGTASVHAALGG
AKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFD
VQRDHVALIKDAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLIT
HA
>gnl|CDD|236982 PRK11784, PRK11784, tRNA 2-selenouridine synthase; Provisional
MRPDAQDFRALFLNDTPLIDVRSPIEFAEGHIPGAINLPLLNDEERAEVGTCYKQQGQFAAIALGHALVA
GNIAAHREEAWADFPRANPRGLLYCWRGGLRSGSVQQWLKEAGIDVPRLEGGYKAYRRFVIDTLEEAPAQ
FPLVVLGGNTGSGKTELLQALANAGAQVLDLEGLANHRGSSFGRLGGPQPSQKDFENLLAEALLKLDPAR
PIVVEDESRRIGRVHLPEALYEAMQQAPIVVVEAPLEERVERLLEDYVLRMHAAGFQAYPEYLAEALQRI
RKRLGGERYQELLALLDAGGHLAWIEELLLEYYDPMYRYQLEKKADRIDFRGDLAEVAEWLRALL
>gnl|CDD|236983 PRK11788, PRK11788, tetratricopeptide repeat protein; Provisional
MLELLFLLLPVAAAYGWYMGRRSARQDQQKESNRLSRDYFKGLNFLLNEQPDKAIDLFIEMLKVDPETVE
LHLALGNLFRRRGEVDRAIRIHQNLLSRPDLTREQRLLALQELGQDYLKAGLLDRAEELFLQLVDEGDFA
EGALQQLLEIYQQEKDWQKAIDVAERLEKLGGDSLRVEIAHFYCELAQQALARGDLDAARALLKKALAAD
PQCVRASILLGDLALAQGDYAAAIEALERVEEQDPEYLSEVLPKLMECYQALGDEAEGLEFLRRALEEYP
GADLLLALAQLLEEQEGPEAAQALLREQLRRHPSLRGFHRLLDYHLAEAEEGRAKESLLLLRDLVGEQLK
RKPRYRCRNCGFTARTLYWHCPSCKAWETIKPIRGLDGE
>gnl|CDD|236984 PRK11789, PRK11789, 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
MMMLDEDGWLVGARRVPSPNFDARPDGEDISLLVIHNISLPPGEFGGPYIDALFTNRLDPDAHPYFAEIA
GLRVSAHFLIRRDGEIVQFVSFDDRAWHAGVSSFQGRERCNDFSIGIELEGTDTLPFTDAQYQALAALTR
ALRAAYPIIAERITGHSDIAPGRKTDPGPAFDWQRFRALLALPTR
>gnl|CDD|236985 PRK11790, PRK11790, phosphoglycerate dehydrogenase
MAKVSLPKDKIKFLLLEGVHQSAVEVLRAAGYTNIEYHKGALDEEELIEAIKDAHFIGIRSRTQLTEEVL
AAAEKLVAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGIPEKNAKAHRGGWN
KSAAGSFEVRGKTLGIVGYGHIGTQLSVLAESLGMRVYFYDIEDKLPLGNARQVGSLEELLAQSDVVSLH
VPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKSNGDPFESP
LRGLDNVILTPHIGGSTQEAQENIGLEVAGKLVKYSDNGSTLSAVNFPEVSLPEHPGGHRLLHIHENRPG
VLAAINQIFAEQGINIAAQYLQTDGEIGYVVIDVDADYAEEALDALKAIPGTIRARLLY
>gnl|CDD|236986 PRK11792, queF, 7-cyano-7-deazaguanine reductase; Provisional
ALEHSPLGKSTEYPDQYDPSLLFPIPRSLNRDELGLTADLLPFHGVDIWTAYELSWLNAKGKPQVAIGEF
EIPADSPNLIESKSFKLYLNSFNQTRFDSWEAVRQTLERDLSACAGAKVSVRLFPLDEFEGQPIAELPGE
CIDDLDIEIDNYEPDPDLLEAAAEEVVEETLVSHLLKSNCLVTGQPDWGSVQIRYRGPKIDREGLLRYLV
SFRQHNEFHEQCVERIFTDIMRFCQPEKLTVYARYTRRGGLDINPFRSNFEFAPPDNGRLARQ
>gnl|CDD|183318 PRK11797, PRK11797, D-ribose pyranase; Provisional
MKKTGLLNSEISSVIARLGHTDTLVICDAGLPIPNGVERIDLALTKGVPSFLDVLDVVLSEMQVEKAILA
EEIKEHNPELHEALLTQLEQLEQHQGNTIEIEYVSHEEFKQLTAESKAVIRTGECTPYANIILESGVTF
>gnl|CDD|236987 PRK11798, PRK11798, ClpXP protease specificity-enhancing factor; Provisional
MMQMTSTRPYLLRALYEWIVDNGLTPHLLVDATYPGVQVPMEYVRDGQIVLNISPRAVGNLQLGNDAISF
NARFGGVPRQIYVPVAAVLAIYARENGQGMMFEPEAAYDEDEHDDDTDPDDEPPPPPRGGRPHLRVVK
>gnl|CDD|236989 PRK11809, putA, trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
MATTTMGVKLDDATRERIKSAAQRIDRTPHWLIKQAIFNYLEKLENGDTLPELPALLSGAANESEEADTP
AEEPHQPFLEFAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKS
AGGRAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAAT
WGLLFTGKLVSTHNEASLSSSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGF
RYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELY
PRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPFVIDYLIDL
ARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLIYPQFATHNAH
TLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLEN
GANTSFVNRIADTSLPLDELVADPVEAVEKLAQQEGQLGLPHPKIPLPRDLYGKGRANSAGLDLANEHRL
ASLSSALLASAHQKWQAAPMLEDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFA
TPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPLG
PVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGA
ALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAF
DSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGR
PVFQAARENSEDWQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQINASGYGLTLGVH
TRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPEDALAVTLA
RQDAEYPVDAQLRAALLAPLTALREWAAEREPELAALCDQYAELAQAGTTRLLPGPTGERNTYTLLPRER
VLCLADTEQDALTQLAAVLAVGSQALWPDDALHRALVAALPAAVQARIQLAKDWQLADQPFDAVLFHGDS
DQLRALCEQVAQRDGPIVSVQGFARGETNILLERLLIERSLSVNTAAAGGNASLMTIG
>gnl|CDD|236990 PRK11814, PRK11814, cysteine desulfurase activator complex subunit SufB; Provisional
MSANTETTDDVKELVNQEYKYGFVTDIETDELPKGLNEDVVRLISAKKNEPEWMLEWRLKAYRHWLTMEE
PHWAKVHYPPIDYQDISYYSAPKCKSKPKSLDEVDPELLETFEKLGIPLREQKRLAGREVAVDAVFDSVS
VATTFKEKLAEAGVIFCSISEAIQEHPELVKKYLGSVVPVNDNFFAALNSAVFSDGSFVYIPKGVRCPME
LSTYFRINAANTGQFERTLIIADEGSYVSYLEGCTAPMRDENQLHAAVVELVALDDAEIKYSTVQNWYPG
DENGKGGIYNFVTKRGLCRGENSKISWTQVETGSAITWKYPSCILRGDNSVGEFYSVALTNGHQQADTGT
KMIHIGKNTKSTIISKGISAGHSQNTYRGLVKIMPKATNARNFTQCDSLLIGDQCGAHTFPYIEVKNNSA
QVEHEATTSKISEDQLFYCRQRGISEEDAVSMIVNGFCKEVFQELPMEFAVEAQKLLAISLEGSVG
>gnl|CDD|236991 PRK11815, PRK11815, tRNA dihydrouridine(20/20a) synthase DusA
MPEKMSKLPSRRFSVAPMMDWTDRHCRYFHRLLSRHALLYTEMVTTGAIIHGDRERLLAFDPEEHPVALQ
LGGSDPADLAEAAKLAEDWGYDEINLNVGCPSDRVQNGRFGACLMAEPELVADCVKAMKDAVSIPVTVKH
RIGIDDQDSYEFLCDFVDTVAEAGCDTFIVHARKAWLKGLSPKENREIPPLDYDRVYRLKRDFPHLTIEI
NGGIKTLEEAKEHLQHVDGVMIGRAAYHNPYLLAEVDRELFGEPAPPLSRSEVLEAMLPYIERHLAQGGR
LNHITRHMLGLFQGLPGARAWRRYLSENAHKPGAGIEVLEEALALVEEAALEA
>gnl|CDD|236992 PRK11819, PRK11819, putative ABC transporter ATP-binding protein; Reviewed
MMAQYIYTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGI
KVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFNEIYAAYAEPDADFDALAAEQGELQEIIDAADAWD
LDSQLEIAMDALRCPPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYP
GTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQS
PKARQAKSKARLARYEELLSEEYQKRNETNEIFIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPG
GIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKVGN
REIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE
FPGCAVVISHDRWFLDRIATHILAFEGDSQVEWFEGNFQEYEEDKKRRLGADAARPHRIKYKKLTR
>gnl|CDD|236995 PRK11824, PRK11824, polynucleotide phosphorylase/polyadenylase; Provisional
MFNKIVKSIEFGGRTLTLETGKLARQANGAVLVRYGDTVVLVTVVASKEPKEGQDFFPLTVDYEEKTYAA
GKIPGGFFKREGRPSEKETLTSRLIDRPIRPLFPKGFRNEVQVVATVLSVDPENDPDILAMIGASAALSI
SGIPFNGPIAAVRVGYIDGEFVLNPTVEELEESDLDLVVAGTKDAVLMVESEAKELSEEVMLEAIEFGHE
AIQELIDAQEELAAEAGPKWEWQPPEVDEELKAAVKELAEAKLKEAYQITDKQEREAALDAIKEEVLEAL
AAEEEEEEDEKEIKEAFKKLEKKIVRRRILEEGIRIDGRKLDEIRPISIEVGVLPRTHGSALFTRGETQA
LVVATLGTLRDEQIIDGLEGEYKKRFMLHYNFPPYSVGETGRVGSPGRREIGHGALAERALEPVLPSEEE
FPYTIRVVSEILESNGSSSMASVCGSSLALMDAGVPIKAPVAGIAMGLIKEGDKYAVLTDILGDEDHLGD
MDFKVAGTRDGITALQMDIKIDGITREILEEALEQAKEGRLHILGKMNEAISEPRAELSPYAPRIETIKI
PPDKIRDVIGPGGKTIREITEETGAKIDIEDDGTVKIAATDGEAAEAAKERIEGITAEPEVGEIYEGKVV
RIVDFGAFVEILPGKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEIDKRGRIRLSRKAVL
>gnl|CDD|183328 PRK11827, PRK11827, protein YcaR
MDHRLLEIIACPVCNGKLWYNQEKQELICKLDNLAFPLRDGIPVLLETEARVLTADESKS
>gnl|CDD|183329 PRK11829, PRK11829, biofilm formation regulator HmsP; Provisional
MAAVAVVALVTICIFIILQLFHFVQQRKDDYANQLESIAYSVRQPLSEAILSVDIPQAKKILNSLLPIGI
LSRAEVILPNQIQVLHANFPTERPIPHWAKRVFSLPVQITVPLYALERVPANPQPLAHLVLRADSFRMYQ
FILSALSAMLSTYLLLALVLSVSIAWCINRLIIHPLRAMAKELEDIGDHGVLHHQLTLPAHHQDDELGVL
VRNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDHFHLLVIGIETLQEVSGAM
SEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLR
PSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFT
LFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVS
LPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDF
GIGYSSLRYLNHLKSLPIHMIKLDKSFVKNLPEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHG
IQCGQGFLFSPPLPRAEFEAQYFSSAHHVS
>gnl|CDD|236996 PRK11830, dapD, 2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
MSQLQKIIEEAWERRAELTPATADTEVREAVEEVIDLLDSGELRVAEKIDDGEWVVNQWVKKAILLSFRL
NDNQVIEGGDFRFYDKVPLKFAGWDEARFKEAGVRVVPGAVVRRGAYIAPNVVLMPSYVNIGAYVDEGTM
VDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLG
QSTKIYDRETGEVHYGRVPAGSVVVPGSLPSKDGGYSLYCAVIVKKVDAKTRSKTSINELLR
>gnl|CDD|236997 PRK11831, PRK11831, phospholipid ABC transporter ATP-binding protein MlaF
EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEN
IPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM
PSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSI
ADHAYIVADKKIVAHGSAQALQANPDPRVRQFLDGIADGPVPFRYPAGDYHADLLGGGS
>gnl|CDD|183332 PRK11832, PRK11832, hydrogen peroxide resistance inhibitor IprA
MLSVVKPLQEFGKLDKCLSRYGTRFEFNNEKQVIFSSDVNNEDTFVILEGVISLRREENVLIGITQAPYI
MGLADGLMKNDIPYKLISEGNCTGYHLPAKQTITLIEQNQLWRDAFYWLAWQNRILELRDVQLIGHNSYE
QIRATLLSMIDWNEELRSRIGVMNYIHQRTRISRSVVAEVLAALRKGGYIEMNKGKLVAINRLPSEY
>gnl|CDD|183333 PRK11835, PRK11835, hypothetical protein; Provisional
MNNLQLSVVHRLPQSYRWSAGFAGSKVEPIPQNGADGDNSLIGLKLLSHDGDNAWSVMQKLSQALSDIQV
PCSVLECEGEPCLFVNRQDESAATCRLKNFGVAIAEPFSAYYPF
>gnl|CDD|183334 PRK11836, PRK11836, deubiquitinase; Provisional
MMVTVVSNYCQLSQTQLSQTFAEKFTVTEELLQSLKKTALSGDEESIELLHNIALGYDKFGKEAEDILYH
IVRNPTNETLSIIRLIKNACLKLYNLAHTATNSPLKSHDSDNLLFKKLFSPSKLMTIIGDEIPLISEKQS
LSKVLLNDENNELSDGTNFWDKNRQLTTDEIACYLQKIAANAKNTQVNYPTGLYVPYSTRTHLEDALNEN
IKSDPSWPKEVQLFPINTGGHWILVSLQKIVNEKNNTQQIKCVIFNSLRALGHDKENSLKRVINSFNSEL
MGEMSNNNIKVHLTEPEIIFLHADLQQYLSQSCGAFVCMAAQEVIEQRESNSDSAPYTLLKNYADRFKKY
SAEEQYEIDFQHRLVNRNCYLDKYGDANINHYYRNLEIKHSQPKNRASGKRVS
>gnl|CDD|183335 PRK11837, PRK11837, undecaprenyl pyrophosphate phosphatase; Provisional
MLENLNLSLFSLINATPDSAPWMISLAIFIAKDLILIVPLLAVVLWLWGPRDQLTAQRQLVIKIAIALAI
SLLVSWTIGHLFPHDRPFVEGIGYNFLHHAADDSFPSDHGTVIFTFALAFLFWHRLWSGSLLMAIAVAIA
WSRVYLGVHWPLDMLGALLVGMIGCLSAQIIWQLFGEKLYQRLQRLYRFCFALPIRKGWVRD
>gnl|CDD|236998 PRK11840, PRK11840, bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
MRIRLNGEPRQVPAGLTIAALLAELGLAPKKVAVERNLEIVPRSEYGQVALEEGDELEIVHFVGGGSDLV
ADDSWTVAGKTFSSRLLVGTGKYKDFEETAAAVEASGAEIVTVAVRRVNVSDPGAPMLTDYIDPKKYTYL
PNTAGCYTAEEAVRTLRLAREAGGWDLVKLEVLGDAKTLYPDMVETLKATEILVKEGFQVMVYCSDDPIA
AKRLEDAGAVAVMPLGAPIGSGLGIQNPYTIRLIVEGATVPVLVDAGVGTASDAAVAMELGCDGVLMNTA
IAEAKNPVLMARAMKLAVEAGRLAYLAGRMPRRRYADPSSPLAGLI
>gnl|CDD|236999 PRK11854, aceF, pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
MAIEIKVPDIGADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGAL
IMIFESADGAADAAPAQAEEKKEAAPAAAPAAAAAKDVHVPDIGSDEVEVTEILVKVGDTVEAEQSLITV
EGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGEAPAAAPAAAEAAAPAAAPAAAAGVKDVN
VPDIGGDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEV
EGAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKG
TGRKGRILKEDVQAYVKDAVKRAEAAPAAAAAGGGGPGLLPWPKVDFSKFGEIEEVELGRIQKISGANLH
RNWVMIPHVTQFDKADITELEAFRKQQNAEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQR
LTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLG
TTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRR
LVL
>gnl|CDD|237000 PRK11855, PRK11855, dihydrolipoamide acetyltransferase; Reviewed
MAIEFKVPDIGEVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGG
LLAVIEAAGAAAAAAAPAAAAAPAAAAAAAPAPAAAAPAAAAAAAGGGVVEVKVPDIGEITEVEVIEWLV
KVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAAAAPAAAAP
AAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAF
VKGAMSAAAAAAAAAAAAGGGGLGLLPWPKVDFSKFGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDE
ADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTP
NGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAIL
GVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL
>gnl|CDD|237001 PRK11856, PRK11856, branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVG
SVIAVIEEEGEAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGV
DLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKRE
IPHFTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAV
ATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEV
AILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLLE
>gnl|CDD|237002 PRK11857, PRK11857, dihydrolipoamide acetyltransferase; Reviewed
KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAA
PPKLEGKREKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAK
AILIALKEFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARE
RKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRW
IDGATIGRFASRVKELLEKPEILGVY
>gnl|CDD|183341 PRK11858, aksA, trans-homoaconitate synthase; Reviewed
KPKDIEIVDTTLRDGEQTPGVVFTNEEKLAIARMLDEIGVDQIEAGFPAVSEDEKEAIKAIAKLGLNASI
LALNRAVKSDIDASIDCGVDAVHIFIATSDIHIKHKLKKTREEVLERMVEAVEYAKDHGLYVSFSAEDAS
RTDLDFLIEFAKAAEEAGADRVRFCDTVGILDPFTMYELVKELVEAVDIPIEVHCHNDFGMATANALAGI
EAGAKQVHTTVNGLGERAGNAALEEVVMALKYLYGIDLGIDTERLYELSRLVSKASGIPVPPNKAIVGEN
AFAHESGIHVDGVLKNPLTYEPFLPEEVGLERRIVLGKHSGRHALKNKLKEYGIELSREELCELLEKVKE
LSERKKRSLTDEELKELVEDVRRSRKAA
>gnl|CDD|237003 PRK11860, PRK11860, bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase
MFSTEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQL
GDTYRITGLGGQFPVKQADLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDI
DYLGNEGFPPLRIGPAPLRLDAPIRVRGDVSSQFLTALLMALPLVARRDITIEVVGELISKPYIEITLNL
LARFGIAVQREGWQRFTIPAGSRYRSPGEIHVEGDASSASYFIAAGAIAGGAPVRIEGVGRDSIQGDIRF
AEAARAMGAQVTSGPNWLEVRRGAWPLKAIDLDCNHIPDAAMTLAVMALYADGTTTLRNIASWRVKETDR
IAAMATELRKLGATVEEGADYIRVTPPAQAADWKAAAIHTYDDHRMAMCFSLAAFNPAGLPVRINDPKCV
AKTFPDYFEALFSVAQADADRVPVICIDGPTASGKGTVAARVAEALGYHYLDSGALYRLTALAALRAGVA
LDDEAAIAALARGLPVRFEGDRIWLGGEDVTDAIRTEAAGMGASRVSALPAVRAALLALQRSFRRLPGLV
ADGRDMGTVIFPDAALKVFLTASAEARAERRYKQLISKGISANIADLLADLEARDARDTQRSVAPLKPAQ
DALLLDNSDLTIEQAVAQVLDWWQERQPFGA
>gnl|CDD|183343 PRK11861, PRK11861, bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
VLLAAPVAQTGPLLARIAPFLDASTIVTDAGSTKSDVVAAARAALGARIGQFVPGHPIAGRESSGVDAAL
ADLYVGRNVVLCALPENAPDALARVEAMWRAARADVRAMSAEQHDRVFAAVSHLPHVLSFALVEQILGES
DAELKFSYAAGGFRDFTRIAASSPEMWRDVCLANRAALLDELDAYTAVLARLRAAIDAGDGAALEAVFAR
SRAARAAWRERGAKPAPAVRSDTSGTGSHMEHLDLGPFSHAQGTVRLPGSKSISNRVLLLAALAEGETTV
TNLLDSDDTRVMLDALTKLGVKLSRDGGTCVVGGTRGAFTAKTADLFLGNAGTAVRPLTAALAVNGGEYR
IHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRPATISVDAPIRVRGDVSSQFLTALLMTLPL
VKAKDGASVVEIDGELISKPYIEITIKLMARFGVTVERDGWQRFTVPAGVRYRSPGTIMVEGDASSASYF
LAAGALGGGPLRVEGVGRASIQGDVGFANALMQMGANVTMGDDWIEVRGIGHDHGRLAPIDMDFNLIPDA
AMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAQLTPNASIDTYD
DHRMAMCFSLVSLGGVPVRINDPKCVGKTFPDYFDRFLALANA
>gnl|CDD|237005 PRK11864, PRK11864, 3-methyl-2-oxobutanoate dehydrogenase subunit beta
MMSRLLTLPKEEYFYPGNAACPGCGAPLGLRYLLKALGEKTVLVIPASCSTVIQGDTPKSPLTVPVLHTA
FAATAAVASGIEEALKARGEKGVIVVGWAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRS
SSTPYGAWTTTTPGGKREHKKPVPDIMAAHKVPYVATASIAYPEDFIRKLKKAKEIRGFKFIHLLAPCPP
GWRFDPDKTIEIARLAVETGVWPLFEYENGKFKLNSPSKTLLDKKKRKPVEEYLKLQGRFKHLTEEEIKG
LQEEIDEMWEEIKKLAKKFG
>gnl|CDD|183346 PRK11865, PRK11865, pyruvate synthase subunit beta
MLGRRMQIPREEYLAPGHRACAGCGAAIAMRLALKALGKNTVIVVATGCLEVITTPYPETAWNVPWIHVA
FENAAAVASGIERAVKALGKKVNVVAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSG
STPFGASTTTSPAGKYSRGEDRPKKNMPLIMAAHGIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQ
PCPTGWGFPPEKTIEIGRLAVETGYWPLFEIENGKFKITYEPLHLDRRTRKPIEEYLKVQGRFKHLTEED
IEILQKYIDEKWKELGLML
>gnl|CDD|183347 PRK11866, PRK11866, 2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
YAVKRPPIWCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATG
VKWANPKLTVIGYGGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDG
NIEEPFNPIALALAAGATFVARGFSGDVKHLKEIIKEAIKHKGFSFIDVLSPCVTFNKLNTYDWFRPRVY
KLEETGHDPTNFEQAYKKALEWGDRIPIGVFYKEEKPTYEEELDEILKNPPLADQPLQPKPEKDLEEFL
>gnl|CDD|237006 PRK11867, PRK11867, 2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
MTDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTI
HGRALAIATGLKLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPV
GFVTKTTPYGSIEPPFNPVELALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVN
TFDWFKERLVKVHDAEGYDPTNALAAMKTLEEGDPIPTGIFYQVERPTYEEAVRAQIEGPLALQDLLMGG
DTWTVL
>gnl|CDD|183349 PRK11869, PRK11869, 2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
MRPEKYDIAWCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAAT
AVKATNPELTVIAEGGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPW
GVFEEPFNPIALAIALDASFVARTFSGDIEETKEILKEAIKHKGLAIVDIFQPCVSFNKVNTYQWYRENT
YYLKDHDPTDRELAFKRALETEKLPLGIFYINEKPTFEELVPAYKGDKTPLWKREPNFEKLKELIESKRS
>gnl|CDD|183350 PRK11872, antC, anthranilate 1,2-dioxygenase electron transfer component AntC
MNHKVALSFADGKTLFFPVGKDELLLDAALRNGINLPLDCREGVCGTCQGRCESGIYSQDYVDEDALSER
DLAQRKMLACQTRVKSDAAFYFDFDSSLCNAGDTLKISGVVTAVELVSETTAILHLDASAHGRQLDFLPG
QYARLQIPGTDDWRSYSFANRPNATNQLQFLIRLLPDGVMSNYLRERCQVGDEILFEAPLGAFYLREVER
PLVFVAGGTGLSAFLGMLDELAEQGCSPPVHLYYGVRHAADLCELQRLAAYAERLPNFRYHPVVSKASAD
WQGKRGYIHEHFDKAQLRDQAFDMYLCGPPPMVEAVKQWLDEQALENYRLYYEKFTQSNT
>gnl|CDD|237007 PRK11873, arsM, arsenite methyltransferase
MMDADDIKEVVREKYGEIAERGGSGCSGCSCCGASANDAADPSTSLGYSEEELAAVPEGANLGLGCGNPT
ALAELKPGETVLDLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARANARKAGYTNVEFRLGEIEAL
PVADNSVDVIISNCVINLSPDKERVFKEAFRVLKPGGRFAISDVVLRGELPEEIRNDAELYAGCVAGALQ
EEEYLAMLAEAGFVDITIQPKREYRIPDAREFLEDWGIAPGRQLDGYIVSATVEATKPAATC
>gnl|CDD|183352 PRK11874, petL, cytochrome b6-f complex subunit PetL; Reviewed
MGIVFFLGYLGVFTGIALGLYFGLRAAKLI
>gnl|CDD|183353 PRK11875, psbT, photosystem II reaction center protein T; Reviewed
MESFAYILILTLALVTLFFAIAFRDPPKIDK
>gnl|CDD|183354 PRK11876, petM, cytochrome b6-f complex subunit PetM; Reviewed
MASEIFGIAALFWVLIPVGLAGGALLLKLQGD
>gnl|CDD|183355 PRK11877, psaI, photosystem I reaction center subunit VIII; Reviewed
MTGDFAASWLPWIFVPLVGWVFPAVFMVLLGRYITATA
>gnl|CDD|183356 PRK11878, psaM, photosystem I reaction center subunit XII; Reviewed
MEPSLTDTQVFVALVVALHAGVLALRLGTSLYRA
>gnl|CDD|237008 PRK11880, PRK11880, pyrroline-5-carboxylate reductase; Reviewed
MMKKIGFIGGGNMASAIIGGLLASGVPAKDIIVSDPSPEKRAALAEEYGVRAATDNQEAAQEADVVVLAV
KPQVMEEVLSELKGQLDKLVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAED
RELVENLLSAFGKVVWVDDEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAA
KLLLESGEHPAELRDNVTSPGGTTIAALRVLEEKGLRAAVIEAVQAAAKRSKELGKE
>gnl|CDD|237009 PRK11883, PRK11883, protoporphyrinogen oxidase; Reviewed
KKVAIIGGGITGLSAAYRLHKKGPDADITLLEASDRLGGKIQTVRKDGFPIELGPESFLARKPSAPALVK
ELGLEDELVANTTGQSYIYVNGKLHPIPPGTVMGIPTSIAPFLFAGLVSPIGKLRAAADLRPPRWKPGQD
QSVGAFFRRRFGDEVVENLIEPLLSGIYAGDIDTLSLRATFPQLAQAEDKYGSLLRGMRKALPKEKKKTK
GVFGTLKGGLQSLIEALEEKLPAGTIHKGTPVTKIDKSGDGYEIVLSNGGEIEADAVIVAVPHPVLPSLF
VAPPAFALFKTIPSTSVATVALAFPESATNLPDGTGFLVARNSDYTITACTWTSKKWPHTTPEGKVLLRL
YVGRPGDEAVVDATDEELVAFVLADLSKVMGITGDPEFTIVQRWKEAMPQYGVGHIERVAELRAGLPHYP
GLYVAGASFEGVGLPDCIAQAKRAAARLLAE
>gnl|CDD|237010 PRK11886, PRK11886, bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA
KTYTVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPER
ISSQLPPGRVTVLPVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQ
GPAQAMGLSLVVGIAIAEALRRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAM
PDFPEELIDQPWSDLQEAGPTIDRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIG
DKEISGIARGIDEQGALLLEDDGVEKPFNGGEISLRSWE
>gnl|CDD|183360 PRK11889, flhF, flagellar biosynthesis protein FlhF
MESTEKKEALMRIKAASKNELYRKLFDQYGTDYYYVVDESVKRNIPFFWKKNYEMLVAFPEDKQEEVNEG
TAQFHEQLMDVVNDPSEQIVKANGIQSVLHNLENVTTPMSYAAMQTGNSEEWARKKEKLLKLFEKGIVVV
KQTEETKVTKKQKAVKKVVPVKKEEVVVKKEKQESVPFIIQKVIRMLEQNDVEQYFIHAYAEKLKVKFEN
ATMITEEEVIEYILEDMRSHFNTENVFEKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHS
RIGTVQQLQDYVKTIGFEVIAVRDEAAMTRALTYFKEEARVDYILIDTAGKNYRASETVEEMIETMGQVE
PDYICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSGELLKIPAVSSAPIVLMTDGQDVKKNI
HIATAEHLAKQMLQTS
>gnl|CDD|183361 PRK11890, PRK11890, phosphate acetyltransferase; Provisional
MDMAHKHEKYERLIARARTLPPLPTAVAHPCDESSLRGAVEAAQLGLITPILVGPRARIEAVAAECGLDL
SGYEIVDAPHSHAAAAKAVELVREGEAEALMKGSLHTDELMSAVVARDTGLRTERRISHVFVMDVPGYPK
PLIITDAAVNIAPTLEDKADIVQNAIDLAHALGFDEPRVAILSAVETVNPKIPSTLDAAALCKMADRGQI
TGAILDGPLAFDNAISPEAARIKGIVSPVAGDADILVVPDLEAGNMLAKQLTFLAGADAAGIVLGARVPI
ILTSRADSVRTRLASCAVAALVAHARRAALGA
>gnl|CDD|183362 PRK11891, PRK11891, aspartate carbamoyltransferase; Provisional
TVPQQAFLRDAMRRLNMTREAFANRIGVSRRALDTWLLPDDSQESRGMPEIVERFVSEIVERAAPGEKYT
QSVDEQPLADQFAFEGKPQLLSVDQFSRDSVEALFRVADVMQPIARRQKISRVLEGAVLGNLFFEASTRT
RVSFGAAFCRLGGSVCDTTGFTFSSMAKGESIYDTSRVMSGYVDALVIRHPEQGSVAEFARATNLPVING
GDGPGEHPSQALLDLYTIQREFSRLGKIVDGAHIALVGDLKYGRTVHSLVKLLALYRGLKFTLVSPPTLE
MPAYIVEQISRNGHVIEQTDDLAAGLRGADVVYATRIQKERFADESFEGYTPDFQINQALVDAVCKPDTL
IMHPLPRDSRPGANDLSTDLNRDPRLAIFRQTDNGIPVRMAIFAVLLGVENLVQHSMRDATWRPPAYLGP
EDAVFHGID
>gnl|CDD|237011 PRK11892, PRK11892, pyruvate dehydrogenase subunit beta; Provisional
MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKV
NTPIAVLLEEGESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMV
TMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAF
AGLKPIVEFMTFNFAMQAIDQIINSAAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPG
LKVVAPYSAADAKGLLKAAIRDPNPVIFLENEILYGQSFDVPKLDDFVLPIGKARIHREGKDVTIVSFSI
GMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVMEQAF
DYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVEAVKAVCYR
>gnl|CDD|237012 PRK11893, PRK11893, methionyl-tRNA synthetase; Reviewed
KKFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELAD
RNSAAFKRLWEALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESELIED
GYRCPPTGAPVEWVEEESYFFRLSKYQDKLLELYEANPDFIQPASRRNEVISFVKSGLKDLSISRTNFDW
GIPVPGDPKHVIYVWFDALTNYLTALGYPDDEELLAELFNKYWPADVHLIGKDILRFHAVYWPAFLMAAG
LPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAVRYFLLREIPFGQDGDFSREAFINRINAD
LANDLGNLAQRTLSMIAKNFDGKVPEPGALTEADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRA
ANKYIDEQAPWSLAKTDPERLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEEDENRDFAALSWG
RLAPGTTLPKPEPIFPRLEEE
>gnl|CDD|183365 PRK11895, ilvH, acetolactate synthase 3 regulatory subunit; Reviewed
MRHTLSVLVENEPGVLSRVAGLFSRRGYNIESLTVGPTEDPGLSRMTIVTSGDEQVIEQITKQLNKLIDV
LKVVDLTEEAHVERELALVKVRASGENRAEILRLADIFRAKIVDVTPESLTIEVTGDSDKIDAFIDLLRP
YGIKEIVRTGVVAIGRGEKIL
>gnl|CDD|237013 PRK11898, PRK11898, prephenate dehydratase; Provisional
MMKIAYLGPEGTFTEAAALKFFPADGEAELVPYDSIPDVLDAVEAGEVDYAVVPIENSIEGSVNPTLDYL
AHGSPLQIVAEIVLPIAQHLLVHPGHAAKIRTVYSHPQALAQCRKWLAEHLPGAELEPANSTAAAAQYVA
EHPDEPIAAIASELAAELYGLEILAEDIQDYPNNRTRFWLLGRKKPPPPLRTGGDKTSLVLTLPNNLPGA
LYKALSEFAWRGINLTRIESRPTKTGLGTYFFFIDVEGHIDDVLVAEALKELEALGEDVKVLGSYPVYWL
SDL
>gnl|CDD|237014 PRK11899, PRK11899, prephenate dehydratase; Provisional
MSKTNRIAFQGEPGANSHLACRDAFPDMEPLPCATFEDAFEAVESGEADLAMIPIENSLAGRVADIHHLL
PESGLHIVGEYFLPIRHQLMALPGATLEEIKTVHSHPHALGQCRKIIRALGLKPVVAADTAGAARLVAER
GDPSMAALASRLAAELYGLDILAENIEDADHNTTRFVVLSREADWAARGDGPIVTTFVFRVRNIPAALYK
ALGGFATNGVNMTKLESYMVGGSFTATQFYADIEGHPEDRNVALALEELRFFSEEVRILGVYPAHPFRG
>gnl|CDD|237015 PRK11901, PRK11901, hypothetical protein; Reviewed
MDEFKPEDELKPDTSDRRPTRSRKSSNGPKLAVSRQHMMIGIGILVLLLLIIAIGSALKSPTEHESQQSS
NNAGAEKNIDLSGSSSLSSGNQSSPSAANNTSDGHDASGVKNTAPPQDISAPPISPTPTQAAPPQTPNGQ
QRIELPGNISDALSQQQGQVNAASQNAQGNTSTLPTAPATVAPSKGAKVPATAETHPTPPQKPATKKPAV
NHHKTATVAVPPATSGKPKSGAASARALSSAPASHYTLQLSSASRSDTLNAYAKKQNLSHYHVYETKRDG
KPWYVLVSGNYASSAEAKRAIATLPAEVQAKKPWVKPVQQVQQDLKK
>gnl|CDD|183369 PRK11902, ampG, muropeptide transporter; Reviewed
IGAMLLLGFASGLPLALTSGTLQAWMTVEGLDIQTIGFFSLVGQAYIFKFLWAPLMDRYTPPLLGRRRGW
LLLTQVGLAASIAAMAFCPPHAALWPLAGLAVLVAFLSASQDIVFDAYSTDVLHPEERGAGAAVKVLGYR
LAMLVSGGLALWLADRVLGWGNTYLLMAGLMLAGALTTLWAPEPEVPARPPRSLGEAVVGPLRDFFSRRG
AWALLLLIVLYKLGDAFAGSLSTTFLIRGAGFSAGEVGIVNKTLGLAATIVGALAGGTLMVRLGLYRSLM
LFGVLQAVSNLGYWVLAVTPKHLWTMALAIGIENLCGGMGTAAFVALLMALCNRSFSATQYALLSALASV
GRVYVGPTSGYLVEAYGWPGFYLMTVVIALPGLALLWLMRGTIGRYEAQAAE
>gnl|CDD|237016 PRK11903, PRK11903, 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase
MTELLANYVAGRWQAGSGAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLA
AIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKDPAFQ
GQHVLVPTRGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGILPAGALS
VVCGSSAGLLDHLQPFDVVSFTGSAETAAVLRSHPAVVQRSVRVNVEADSLNSALLGPDAAPGSEAFDLF
VKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAG
LAALRAQAEVLFDGGGFALVDADPAVAACVGPTLLGASDPDAATAVHDVEVFGPVATLLPYRDAAHALAL
ARRGQGSLVASVYSDDAAFLAAAALELADSHGRVHVISPDVAALHTGHGNVMPQSLHGGPGRAGGGEELG
GLRALAFYHRRSAVQASPAVLDALTQAAAAP
>gnl|CDD|237017 PRK11904, PRK11904, bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA
LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKKKLGGIDAF
LQEYSLSTEEGIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVK
LDKKADGTPSGVLKRLVNRLGEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGE
AALTAADAERYFKAYARAIEAIGRAAGGADLPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARL
AKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGFGLAVQAYQKRALPVLDWLADLARRQGRRIP
VRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARGAIYPQFATHNAHTVAAILEMA
GHRGFEFQRLHGMGEALYDALLDAPGIPCRIYAPVGSHKDLLPYLVRRLLENGANSSFVHRLVDPDVPIE
ELVADPVEKLRSFETLPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQAGPIINGE
GEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIAL
CVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPTGESNELRLHGRGVFVCISPWNFPLAI
FLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFT
GSTETARIINRTLAARDGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQE
DIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFV
APTAFEIDSISQLEREVFGPILHVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNV
YVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVNTTAAGGNASLLS
>gnl|CDD|237018 PRK11905, PRK11905, bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
MFQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKGTGVEA
LLQEYSLSSQEGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLL
STVNDRGLSAALTRLIARLGEPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEA
ARTAADAERYYRDYERAIHAIGKAATGRGVYDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLA
KAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGIGFVVQAYQKRCPFVIDYLIDLARRSGRRLMV
RLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAARDVIYPQFATHNAQTLAAIYELAG
GKGDFEFQCLHGMGEPLYDQVVGKEKLGRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVNRIVDENVP
VEELIADPVEKVAAMGVAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEALNAFAAKTWHAAPLLA
GGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMP
ELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAA
LVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARL
IQRTLAKRSGPPVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLT
MLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEID
SISDLEREVFGPVLHVVRFKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIG
AVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTPIPPAHESVDTDAAARDFLAWLDKEGKAALAAAAR
DARARSALGLEQELPGPTGESNLLSLHPRGRVLCVADTEEALLRQLAAALATGNVAVVAADSGLAAALAD
LPGLVAARIDWTQDWEADDPFAGALLEGDAERARAVRQALAARPGAIVPLIAAEPTDAYDLARLVEERSV
SINTTAAGGNASLMALGE
>gnl|CDD|183373 PRK11906, PRK11906, HilA family transcriptional regulator YgeH
MDLENKFSYHFLEGLTLTEDGILTQGNEQVYIPQKELGVLIVLLESAGHVVLKDMIIESVWKNIIVSDES
LTRCIYSLRCIFEKIGYDRCIETIYRKGYRFSGQVFKTKINEDNTSDYSIAIFPFTTSLNTLDPLILNQE
LVQIISNKKIDGLYTYPMAATNFCNDHISQNSFLSRFKPDYFVTGRINQNNAVNTLYIELIDAKNLFLIA
SNHLPVDELHNTSQFIIDNILQTVHKPERSVRLAKQDQGYKNHYLSDEMLAGKKELYDFTPESIYRAMTI
FDRLQNKSDIQTLKTECYCLLAECHMSLALHGKSELELAAQKALELLDYVSDITTVDGKILAIMGLITGL
SGQAKVSHILFEQAKIHSTDIASLYYYRALVHFHNEKIEEARICIDKSLQLEPRRRKAVVIKECVDMYVP
NPLKNNIKLYYKETESESHRVIIDNILKLKQLTRICMR
>gnl|CDD|237019 PRK11907, PRK11907, bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
MMKHYFSKSAVALTLALLTASNPKLAQAEEIVTTTPATSTEAEQTTPVESDATEEADNTETPVAATTAAE
APSSSETAETSDPTSEATDTTTSEARTVTPAATETSKPVEGQTVDVRILSTTDLHTNLVNYDYYQDKPSQ
TLGLAKTAVLIEEAKKENPNVVLVDNGDTIQGTPLGTYKAIVDPVEEGEQHPMYAALEALGFDAGTLGNH
EFNYGLDYLEKVIATANMPIVNANVLDPTTGDFLYTPYTIVTKTFTDTEGKKVTLNIGITGIVPPQILNW
DKANLEGKVIVRDAVEAVRDIIPTMRAAGADIVLVLSHSGIGDDQYEVGEENVGYQIASLSGVDAVVTGH
SHAEFPSGNGTSFYAKYSGVDDINGKINGTPVTMAGKYGDHLGIIDLNLSYTDGKWTVTSSKAKIRKIDT
KSTVADGRIIDLAKEAHNGTINYVRQQVGETTAPITSYFALVQDDPSVQIVNNAQLWYAKQQLAGTPEAN
LPILSAAAPFKAGTRGDASAYTDIPAGPIAIKNVADLYLYDNVTAILKVTGAQLKEWLEMSAGQFNQIDP
NSKEPQNLVNTDYRTYNFDVIDGVTYKFDITQPNKYDRDGKLVNPTASRVRNLQYNGQPVDANQEFIVVT
NNYRANGTFPGVKEASINRLLNLENRQAIINYIISEKTINPTADNNWTFTDSIKGLDLRFLTADKAKNLV
TDQEDIVYLAASTASEGFGEYKFVYTESKVVTPDEQQSQEGNSQQDIVLEQGIHITLPAVYPPAPAPQHK
LASPHSQASTKTLPKTGSEKTSMLSLLGLTLLGLVGAWTKKKEH
>gnl|CDD|183375 PRK11908, PRK11908, bifunctional UDP-4-keto-pentose/UDP-xylose synthase
MKKVLILGVNGFIGHHLSKRILETTDWEVYGMDMQTDRLGDLVNHPRMHFFEGDITINKEWIEYHVKKCD
VILPLVAIATPATYVKQPLRVFELDFEANLPIVRSAVKYGKHLVFPSTSEVYGMCPDEEFDPEASPLVYG
PINKPRWIYACSKQLMDRVIWAYGMEEGLNFTLFRPFNWIGPGLDSIYTPKEGSSRVVTQFLGHIVRGEP
ISLVDGGSQKRAFTDIDDGIDALMKIIENKDGVASGKIYNIGNPKNNHSVRELANKMLELAAEYPEYAES
AKKVKLVETTSGAYYGKGYQDVQNRVPKIDNTMQELGWAPKTTMDDALRRIFEAYRGHVAEARALVE
>gnl|CDD|183376 PRK11909, PRK11909, cobalt transporter CbiM
MHIPDGYLGPITCAVFYAIMIPIWYVAGKKVNKSLDKKQVPLLAIGAAFSFVIMMFNVPIPGGTTAHAVG
GTLIAILLGPWAAVISISVALVIQALLFGDGGITAIGANCFNMAFVLPFVGYYVYKLLSILKVRRVIASA
IGGYVGINAAALATGIEFGLQPFLFHTANGTPLYCPYGLNVSIPAMLFAHLTVAGIVEAIVTGLVVYYLQ
KADEENLLYKKSYKLRGDNR
>gnl|CDD|183377 PRK11910, PRK11910, amidase; Provisional
MKRRILITIIVVCTVFSIIGGYVFFTSQQTTTSENKSAVSKKKKPTVKKEKPKQSSNNLTLGKNKENFHL
EKGFGNKQLQVERIIDRIFQSSLKNRTEIKVKPKNNPQKKQNIKPVKPIPSKPEKPEDSPSPFYDKARVM
TPINNQLATLDLAVLEAKEPLIIGADVTKLQQLIATKQLSYKELAGIYLNRIKKYDQNGLNLNAITEINP
TIIAEAEQLDKENTTNKSALYGMPVLLKDNIGTKELPTSAGTVALKDWVIGKDATIVENLKANGALILGK
TNMSEWAAGMDEDLPNGYSGKKGQSKNPYSSNLDPSGSSSGSATAATSDFAAIAIGTETNGSIITPASAQ
SAVGYKPSQGLVNNKGIIPLSSRFDTPGPLTRTVNDAYLTTNALTNTTSNPPLSTDALKGKRIGLLADGE
SNEETAVIKKIKLDLQKAGATIIEGIAVGEFEQKDTDYASLLNADFKHDLNQFLQVNHSPMSTLESIIQF
NQTNPTRNMKYGQSELVKSQQSTITKQQADNLASNLIQSSQNELDSVLQKDKLDAVVTIGMGGSVMFLAP
IAGNPELTIPAGYDEESNQPISLTFITARNSDKILLNMGYAYEQQSKNRKSPNLK
>gnl|CDD|138812 PRK11911, flgD, flagellar basal body rod modification protein; Provisional
MDGISSLSGASQDTNNAVTSSVSKTLGKDDFMKLFLTSLQYQDPSSPLDTNEMMSQMAQLSLMEQVANMT
TAVDKLSEQAQNSALQSAVNFIGKDIKGVSLNGEVISGKVESVQQTTNGVMLKLKDNDSLVPMTYVTEIN
>gnl|CDD|237020 PRK11913, phhA, phenylalanine 4-monooxygenase; Reviewed
DAAYRARRDAGMEKAADYTADQPWIDYTAEEHAIWQTLYERQLALLPGRACDEFLEGLEALGLPKDRIPQ
LDEINRVLQAATGWQVVPVPGLIPFDVFFELLANRRFPVATFIRRPEELDYLQEPDIFHDVFGHVPLLTN
PVFADFMQAYGKLGLRASKEGRLEFLARLYWFTVEFGLIRTPGGLRIYGAGILSSPGETLYALESDSPNR
RPFDLERVMRTPYRIDIFQPTYFVIDSFEQLFDIAEPDFMALVARAKQLGLFAPGFVPKGDAVLT
>gnl|CDD|237021 PRK11914, PRK11914, diacylglycerol kinase; Reviewed
GQLRRHEIGKVTVLTNPLSGHGAAPHAAERAIARLHHRGVDVVEIVGTDAHDARHLVAAALAKGTDALVV
VGGDGVISNALQVLAGTDIPLGIIPAGTGNDHAREFGIPTGDPEAAADVIVDGWTETVDLGRIQDDDGIV
KWFGTVAATGFDSLVTDRANRMRWPHGRMRYNLAMLAELSKLRPLPFRLVLDGTEEIVTDLTLAAFGNTR
SYGGGMLICPNADHTDGLLDITMVQSASRTRLLRLFPTVFKGTHVELDEVSTARAKTVHVECPGINAYAD
GDFACPLPAEISAVPGALQILRPRPG
>gnl|CDD|237022 PRK11915, PRK11915, lysophospholipid acyltransferase
MTAREVGRIGLRKLLQRIGIVAESMTPLATDPVEVTQLLDARWYDERLRALADELGRDPDSVRAEAAGYL
REMAASLDERAVQAWRGFSRWLMRAYDVLVDEDQITQLRKLDRKATLAFAFSHRSYLDGMLLPEVILANR
LSPALTFGGANLNFFPMGAWAKRTGAIFIRRQTKDIPVYRFVLRAYAAQLVQNHVNLTWSIEGGRTRTGK
LRPPVFGILRYITDAVDEIDGPEVYLVPTSIVYDQLHEVEAMTTEAYGAVKRPEDLRFLVRLARQQGERL
GRAYLDFGEPLPLRKRLQELRADKSGTGSEIERIALDVEHRINRATPVTPTAVVSLALLGADRSLSISEV
LATVRPLASYIAARNWAVAGAADLTNRSTIRWTLHQMVASGVVSVYDAGTEAVWGIGEDQHLVAAFYRNT
AIHILVDRAIAELALLAAAETTTNGSVSPATVRDEALSLRELLKFEFLFSGRAQFEKDLANEVRLIGSVV
DTSKAAAAADVWRLLESADLLLAHLVLRPFLDAYHIVADRLAAHEDDSFDEEGFLAECLQVGKQWELQRR
IASAESRSMELFKTALRLARHRELVDGADATDIAKRRQQFADEIATATRRVNTIAELARRR
>gnl|CDD|183380 PRK11916, PRK11916, electron transfer flavoprotein subunit alpha
MSQLNSVWVFSDNPERYAELFGGAQQWGQQVYAIVQNTDQAQAVMPYGPKCIYVLEQNDALQRTENYAES
IAALLKDKHPAMLLLAATKRGKALAARLSVQLNAALVNDATAVDIVDGHICAEHRMYGGLAFAQEKINSP
LAIITLAPGVQEPCTSDTSHQCPTETVPYVAPRHEILCRERRAKAASSVDLSKAKRVVGVGRGLAAQDDL
KMVHELAAVLNAEVGCSRPIAEGENWMERERYIGVSGVLLKSDLYLTLGISGQIQHMVGGNGAKVIVAIN
KDKNAPIFNYADYGLVGDIYKVVPALISQLSR
>gnl|CDD|183381 PRK11917, PRK11917, bifunctional adhesin/ABC transporter aspartate/glutamate-binding protein; Reviewed
MVFRKSLLKLAVFALGACVAFSNANAAEGKLESIKSKGQLIVGVKNDVPHYALLDQATGEIKGFEIDVAK
LLAKSILGDDKKIKLVAVNAKTRGPLLDNGSVDAVIATFTITPERKRIYNFSEPYYQDAIGLLVLKEKNY
KSLADMKGANIGVAQAATTKKAIGEAAKKIGIDVKFSEFPDYPSIKAALDAKRVDAFSVDKSILLGYVDD
KSEILPDSFEPQSYGIVTKKDDPAFAKYVDDFVKEHKNEIDALAKKWGL
>gnl|CDD|171344 PRK11920, rirA, iron-responsive transcriptional regulator RirA
MRLTKQTNYAIRMLMYCAANDGKLSRIPEIARAYGVSELFLFKILQPLVEAGLVETVRGRNGGVRLGRPA
ADISLFDVVRVTEDSFSMAECFENDASECPLVDSCGLNSALRKALNAFFAVLSKYSIADLVKARPNIRFL
LGLDEMEAPRIAA
>gnl|CDD|237023 PRK11921, PRK11921, anaerobic nitric oxide reductase flavorubredoxin
FKINDNVTWVGKIDWELRKFHGEEYSTHRGSSYNSYLIKDEKTVLIDTVWQPFAKEFVENLKKEIDLDKI
DYIVANHGEIDHSGALPELMKEIPDTPIYCTKNGAKSLKGHYHQDWNFVVVKTGDRLEIGSNELIFIEAP
MLHWPDSMFTYLTGDNILFSNDAFGQHYASELMYNDLVDQGELYQEAIKYYANILTPFSPLVIKKIEEIL
SLNLPVDMICPSHGVIWRDNPLQIVEKYLEWAANYQENQVTILYDTMWNSTRRMAEAIAEGIKKANKDVT
VKLYNSAKSDKNDIITEVFKSKAILVGSSTINRGILSSTAAILEEIKGLGFKNKKAAAFGSYGWSGESVK
IITERLKKAGFEIVNDGIRELWNPDDEALDRCRSFGENFAESLK
>gnl|CDD|237024 PRK11922, PRK11922, RNA polymerase sigma factor; Provisional
MTTAPASRPPPLSAASDRELVARVLAGDEAAFEALMRRHNRRLYRTARAILRNDAEAEDVVQEAYLRAFR
ALGTFRGDASLSTWLSRIVLNEALGRLRRRRRLVNLAEMVMASTIAGGERTPLADPAEDPERAAARREIR
ALLERAIDALPDAFRAVFVLRVVEELSVEETAQALGLPEETVKTRLHRARRLLRESLAREIGPALLDAFP
FAGARCDRIVAAVLARLAERS
>gnl|CDD|171347 PRK11923, algU, RNA polymerase sigma factor AlgU; Provisional
MLTQEEDQQLVERVQRGDKRAFDLLVLKYQHKILGLIVRFVHDTAEAQDVAQEAFIKAYRALGNFRGDSA
FYTWLYRIAINTAKNHLVSRGRRPPDSDVSSEDAEFYDGDHALKDIESPERALLRDEIEGTVHRTIQQLP
EDLRTALTLREFDGLSYEDIASVMQCPVGTVRSRIFRAREAIDKALQPLLQES
>gnl|CDD|183384 PRK11924, PRK11924, RNA polymerase sigma factor; Provisional
GQLMPVDATGDKEAFSELFRPHAPDLLRYARRQLGDRALAEDAVQEAFLRAWRKADLFNGKGSARTWLLT
IARNVCYDLLRRRRREKAVLSDDALEPEFAETAETPEAALLAKDDLARIDRCLDALPVKQREVFLLRYVE
GLSYREIAEILGVPVGTVKSRLRRARQLLRECLEAQWEA
>gnl|CDD|237025 PRK11929, PRK11929, bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF
MSIGNRLGNVKLEELLQALAWLRGCVAATADLRLDSREVQPGDLFVACRGAASDGRAFIDQALARGAAAV
LVEAEGEDQVAAADALVLPVADLRKALGELAARWYGRPSEQLSLVAVTGTNGKTSCAQLLAQLLTRLGKP
CGSIGTLGARLDGRLIPGSLTTPDAIILHRILARMRAAGADAVAMEASSHGLEQGRLDGLRIAVAGFTNL
TRDHLDYHGTMQDYEEAKAALFSKLPGLGAAVINADDPAAARLLAALPRGLKVGYSPQNAGADVQARDLR
ATAHGQVFTLATPDGSYQLVTRLLGRFNVSNLLLVAAALKKLGLPLAQIARALAAVSPVPGRMERVGPTA
GAQGPLVVVDYAHTPDALAKALTALRPVAQARNGRLVCVFGCGGDRDKGKRPEMGRIAAELADRVVVTSD
NPRSEAPEAIIDQILAGIPAGARVFVISDRAEAIRQAIWMAAPGDVILIAGKGHETYQEIGGRKLFFDDR
EWARRALLARISSTLIKLRAAKGGSNSLQINSLPHAGAVSTDSRSVGRGELFVALRGENFDGHDYLPQAF
AAGACAAVVERQVADVDLPQIVVDDTRAALGRLATAWRARFSLPVVAITGSNGKTTTKEMIAAILAAWQG
EDRVLATEGNFNNEIGVPLTLLRLRAQHRAAVFELGMNHPGEIAYLAAIAAPTVALVTNAQREHQEFMHS
VEAVARAKGEIIAALPEDGVAVVNGDDPYTAIWAKLAGARRVLRFGLQPGADVYAEKIAKDISVGEAGGT
RCQVVTPAGSAEVYLPLIGEHNLRNALAAIACALAAGASLKQIRAGLERFQPVAGRMQRRRLSCGTRIID
DTYNANPDSMRAAIDVLAELPNGPRALVLGDMLELGDNGPAMHREVGKYARQLGIDALITLGEAARDAAA
AFGAGARGVCASVDEIIAALRGALPEGDSVLIKGSRFMRLERVVDALS
>gnl|CDD|237026 PRK11930, PRK11930, putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
MSYTLESISGILGAEGLGDKDAIIDQILTDSRSLSFPENTLFFALKGERNDGHRYIQELYEKGVRNFVVS
EEKHPEESYPDANFLKVKDPLKALQELAAYHRSQFDIPVIGITGSNGKTIVKEWLYQLLSPDYNIVRSPR
SYNSQIGVPLSVWQLNEEHELGIFEAGISQPGEMEALQKIIKPTIGILTNIGGAHQENFRSIKQKIMEKL
KLFKDCDVIIYNGDNELISSCITKSNLTLKLISWSRKDPEAPLYIPFVEKKEDHTVISYTYKGEDFHFEI
PFIDDASIENLIHCIAVLLYLGYSADQIQERMARLEPVAMRLEVKEGINNCTLINDSYNSDLQSLDIALD
FLNRRSQSKKKTLILSDILQSGQSPEELYRKVAQLISKRGIDRLIGIGEEISSEASKFEGTEKEFFKTTE
AFLKSFAFLKFRNELILVKGARKFEFEQITELLEQKVHETVLEINLNAIVHNLNYYRSKLKPETKIMCMV
KAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMNPEPTSFDTIIDYKLEPEIYSFR
LLDAFIKAAQKKGITGYPIHIKIDTGMHRLGFEPEDIPELARRLKKQPALKVRSVFSHLAGSDDPDHDDF
TRQQIELFDEGSEELQEALGYKPIRHILNSAGIERFPDYQYDMVRLGIGLYGVSASGAGQQALRNVSTLK
TTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNGVGYVLVNGQKAPIVGNICMDMCM
IDVTDIDAKEGDEVIIFGEELPVTELADALNTIPYEILTSISPRVKRVYFQE
>gnl|CDD|183387 PRK11933, yebU, rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
MVYLPDAFLTQMREAMPSHLSMDDFIAACQRPLRRSIRVNTLKISVADFLQLMAPYGWTLTPIPWCEEGF
WIERDDEDALPLGNTAEHLSGLFYIQEASSMLPVAALFADDNAPQRVLDMAAAPGSKTTQIAALMNNQGA
IVANEYSASRVKVLHANISRCGVSNVALTHFDGRVFGAALPETFDAILLDAPCSGEGTVRKDPDALKNWS
PESNLEIAATQRELIESAFHALKPGGTLVYSTCTLNREENQAVCLWLKETYPDAVEFEPLGDLFPGAEKA
LTEEGFLHVFPQIYDSEGFFVARLRKTASVPRLPAPKYKVGKFPFTPAKDKEAQEIRQAAASVGLSWPEN
LRLWQRDKEVWLFPAGIEPLIGKVRFSRIGIKLAETHKKGYRWQHEAVIALASPDNANAFELTPQEAEEW
YMGRDIYPQTAPPAGEVIVTYQGQPIGLAKRVGNRLKNSLPRELVRDGKL
>gnl|CDD|237027 PRK12266, glpD, glycerol-3-phosphate dehydrogenase; Reviewed
MTMMETYDLLVIGGGINGAGIARDAAGRGLSVLLCEQDDLASATSSASTKLIHGGLRYLEHYEFRLVREA
LAEREVLLRMAPHIIWPMRFVLPHRPHLRPAWMIRAGLFLYDHLGKRKSLPGSRGLDLGRDPAGSPLKPE
ITRGFEYSDCWVDDARLVVLNARDAAERGAEILTRTRVVSARRENGLWHVTLEDTATGKRYTVRARALVN
AAGPWVKQFLDDGLGLPSPYGIRLVKGSHIVVPRLFDHDQAYILQNPDGRIVFAIPYEDDFTLIGTTDVE
YKGDPAKVAISEEEIDYLCKVVNRYFKKQLTPADVVWTYSGVRPLCDDESDSAQAITRDYTLELDDENGG
APLLSVFGGKITTYRKLAEHALEKLAPYLPQMGPAWTAGAPLPGGDFPGDRFDALAAALRRRYPWLPEAL
ARRLARAYGTRAERLLGGATSLADLGEHFGHGLYEAEVDYLVEHEWARTAEDILWRRTKLGLRLDAEQQA
RLEAWLAARRAAAAAAAA
>gnl|CDD|237028 PRK12267, PRK12267, methionyl-tRNA synthetase; Reviewed
MMKKTFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQE
YVDEISAGFKELWKKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQL
VDGGKCPDCGREVELVKEESYFFRMSKYQDRLLEYYEENPDFIQPESRKNEMINNFIKPGLEDLSISRTS
FDWGIPVPFDPKHVVYVWIDALLNYITALGYGSDDDELFKKFWPADVHLVGKDILRFHAIYWPIMLMALG
LPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDRYGLDALRYYLLREVPFGSDGDFSPEALVERINSD
LANDLGNLLNRTVAMINKYFDGEIPAPGNVTEFDEELIALAEETLKNYEELMEELQFSRALEEVWKLISR
ANKYIDETAPWVLAKDEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKIFEQLGLEEELTSWESLLE
WGGLPAGTKVAKGEPLFPRIDVEEEIAYIKEQMEGSAPKEPEEKEKKPEKPEITIDDFDKVELRVAEVLE
AEKVEKSDKLLKLQVDLGEEEPRQIVSGIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILAAEDDG
KLTLLTVDKEVPNGSKVK
>gnl|CDD|105491 PRK12269, PRK12269, bifunctional cytidylate kinase/ribosomal protein S1; Provisional
MHGGGERERSFVHPRTRCVAVRARTVLQCRPMGTVIIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYR
AFTLAALRRVSELAVQACSPSPDPDAAVGCAAVPHATNLDTSYAPLTAQKKVALFDEAYWVSFARTVALS
YRAGVMYVGEENVESLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCEGRDLTTVVFVDADLK
CYLDASIEARVARRWAQGTSRLSKQELEQRMRARDAHDRARTVGGLRCAPDALYVDTSCLTIEEVCERIA
REAHRRALWGGERSVENQEGKGTPLVPRQLQERYSFEAPEPGSVRMGTVVQVNAGTVFVDIGGKSEGRVP
VEEFEAPPKAGDGVRVYVERVTPYGPELSKTKADRLGLKVKLRDAERDGTPVEGRIVRLTEKKSGFEVDL
GAGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQSKQHRGNDNIVINRRRYLEERARQAREEFFNS
VHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLS
LKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDEV
ECMILGYDIQAGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSW
VKRTRPADHELEVGKEIECMVIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFV
RVPGGVEGLVRKQHLVENRDGDPGEALRKYAVGDRVKAVIVDMNVKDRKVAFSVRDYQRKVQRDELSRYM
SAPRGEDEGSFTLGDLMRQTSGK
>gnl|CDD|237030 PRK12270, kgd, multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit
SSEFGQNEWLVEEMYQQYLADPNSVDPSWREFFADYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAP
APAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVPTA
TSVRAVPAKLLIDNRIVINNHLKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAEVDGKPTLVTPAHVN
LGLAIDLPKKDGSRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVH
SVPRLMKGQGAIIGVGAMEYPAEFQGASEERLAELGISKVMTLTSTYDHRIIQGAESGEFLRTIHQLLLG
EDGFYDEIFESLRIPYEPVRWATDIPADHEDEVDKNARVMELIHAYRVRGHLMADTDPLEYRQRSHPDLD
VLTHGLTLWDLDREFPVGGFGGKERMKLRDILGVLRDSYCRTVGIEYMHIQDPEQRRWLQERVERPHEKP
TREEQKRILSKLNAAEAFETFLQTKYVGQKRFSLEGGESLIPLLDAVLDQAAEHGLDEVVIGMAHRGRLN
VLANIVGKPYSQIFREFEGNLDPRSAQGSGDVKYHLGAEGTFTQMFGDEIKVSLAANPSHLEAVDPVLEG
IVRAKQDRLDKGEEGFTVLPILLHGDAAFAGQGVVAETLNLSQLRGYRTGGTIHIVVNNQVGFTTAPESS
RSSEYATDVAKMIQAPIFHVNGDDPEAVVRVARLAFEYRQRFHKDVVIDLVCYRRRGHNEGDDPSMTQPL
MYDLIDAKRSVRKLYTEALIGRGDITVEEAEQALRDYQGQLERVFNEVREAEKKPPEPPESVESDQGPPA
GVDTAVSAEVLERIGDAHVNLPEGFTVHPKLKPLLEKRREMAREGGIDWAFGELLAFGSLLLEGTPVRLS
GQDSRRGTFSQRHAVLIDRETGEEYTPLQNLSDDQGKFLVYDSLLSEYAAMGFEYGYSVERPDALVLWEA
QFGDFANGAQTIIDEFISSGEAKWGQRSGVVLLLPHGYEGQGPDHSSARIERFLQLCAEGNMTVAQPSTP
ANYFHLLRRQALSGPRRPLVVFTPKSMLRLKAAVSDVEDFTEGKFRPVIDDPTVDDGAKVRRVLLCSGKL
YYDLAARREKDGRDDTAIVRVEQLYPLPRAELREALARYPNATEVVWVQEEPANQGAWPFMALNLPELLP
DGRRLRRVSRPASASPATGSAKVHAVEQQELLDEAFAR
>gnl|CDD|237031 PRK12273, aspA, aspartate ammonia-lyase; Provisional
MMMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGLLDE
EKADAIVAACDEILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMS
QSTNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVAL
AEDRKRLYRAAELLREVNLGATAIGTGLNAPPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVS
GALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGSSIMPGKVNPVIPEVVNQVCFQVIGNDTTVT
MAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERCREYVENSIGIVTALNPYIGY
ENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPGYKGKRYT
>gnl|CDD|237032 PRK12274, PRK12274, serine/threonine protein kinase; Provisional
SHPPAVNEPLKSDTFGRILLVRGGERKFVRRDLSAAPWWLRGVAWWLARREALALRQLDGLPRTPRLLHW
DGRHLDRSYLAGAAMYQRPPRGDLAYFRAARRLLQQLHRCGVAHNDLAKEANWLVQEDGSPAVIDFQLAV
RGNPRARWMRLLAREDLRHLLKHKRMYCPAALTPVERRVLKRTSWIRELWFATGKPVYRFVTRRVLHWED
NEGQGPKP
>gnl|CDD|183395 PRK12275, PRK12275, hypothetical protein; Reviewed
IMDFEDLDVWKRSMKLAIEIYKLTKLFPDEERYGLTSQLRRAAVSIPSNIAEGYGRESKKDFIRFLYIAL
GSLAELETQLYIAKELGYITKEQYESILQEYDEIAKMLNGLIKKLK
>gnl|CDD|237033 PRK12276, PRK12276, putative heme peroxidase; Provisional
MSEAAITLDGWYCLHDFRSIDWAAWKTLSSDEREAAVDEFLAFLEKWEEVEAAKQGSHAIYSIVGQKADL
MLMILRPTMEELNEIENELNKTRLADYLIPAYSYVSVVELSNYLASSDEDPYQNPHVKARLYPELPKSKY
ICFYPMDKRRQGGDNWYMLPMEERQKLMYSHGMIGRKYAGKVKQIITGSVGFDDWEWGVTLFADDPLQFK
KIVYEMRFDEVSARYGEFGSFFVGNILPAEELLQFLHI
>gnl|CDD|183397 PRK12277, PRK12277, 50S ribosomal protein L13e; Provisional
MREEMEPPKAIVKRPNYRFEYGGKRKDKRIGRGFSIGELEAAGLDIKNARKLGIRVDKRRKTVHEENVEA
LKKFLEQLGNQKS
>gnl|CDD|237034 PRK12278, PRK12278, 50S ribosomal protein L21
MFAVIKTGGKQYKVQAGDLLRVEKLAAEAGETVQFGEVLMLGEGDNVTVGAPFVDGAAVQAEVIEQIKGD
KVIHFKKRRRQSSRRTKGHRQLLTLVRITEILASGADASGVKAATGAGKVEVAAEAAPAKAKKEAAPKAA
PAPAAAAAPPAAAAAGADDLTKITGVGPALAKKLNEAGVTTFAQIAALTDADIAKIDEKLSFKGRIEKDG
WIEQAKELAKG
>gnl|CDD|138835 PRK12279, PRK12279, 50S ribosomal protein L22/unknown domain fusion protein; Provisional
MTNKVIQRNIHISHRKASLVIDLVRNKPVHEAIRILSNTPKKFAPIVLKLLNSAISNVQHNSKDMDPSKL
YIYKIVANQGPTMKRTLPRAKGSADQLFKRTTHLEIVLSDDVNEREKELAAIKAKKSKKPLPVEPKAKVE
TKKVAKPSKVEVKPVEKDENVDPELLKREQQVLKVVEKTASQKEEETTETIMISTSPKNAQVLFDDLEKN
VIFYKTTPVNKVLRVLVYVTSPTKKVVGEFDLESVEIGAISSIWRKYGKQSVISKKEYDAYYEGKDKAHA
LVSKKAYKYRNPKDLSEYNMTKGPSGFQYLK
>gnl|CDD|237035 PRK12280, rplW, 50S ribosomal protein L23; Reviewed
MNINEVIKKPILTEKSYSLMSKNVYTFKVDRRANKIEIKKAVEFIFKVKVLKVNIFNVDKKPKRLGRFPG
FTNSYKKAYVTLAEGYSINLFPEESEKEQKEVSKETEEKEAIKAKKEKKEKKEKKVAEKLAKKKSTKTTK
NTTKKATKKTTTKKEEGK
>gnl|CDD|183399 PRK12281, rplX, 50S ribosomal protein L24; Reviewed
KKVKLKVKKGDMVKVIAGDDKGKTGKVLAVLPKKNRVIVEGVKIAKKAIKPSQKNPNGGFIEKEMPIHIS
NVKKVA
>gnl|CDD|183400 PRK12282, PRK12282, tryptophanyl-tRNA synthetase II; Reviewed
TKPIILTGDRPTGKLHLGHYVGSLKNRVALQNEHEQFVLIADQQALTDNAKNPEKIRRNILEVALDYLAV
GIDPAKSTIFIQSQIPELAELTMYYMNLVTVARLERNPTVKTEIAQKGFGRSIPAGFLTYPVSQAADITA
FKATLVPVGDDQLPMIEQTREIVRRFNSLYGTDVLVEPEALLPEAGRLPGLDGKAKMSKSLGNAIYLSDD
ADTIKKKVMSMYTDPNHIRVEDPGKVEGNVVFTYLDAFDPDKAEVAELKAHYQRGGLGDVKCKRYLEEVL
QELLAPIRERRAEFAKDPGYVLEILKAGSEKAREVAAQTLSEVKDAMGLNYFK
>gnl|CDD|183401 PRK12283, PRK12283, tryptophanyl-tRNA synthetase; Reviewed
FPDRVLSGMRPTGRLHLGHYHGVLKNWVKLQHEYECFFFVADWHALTTHYETPEVIEKNVWDMVIDWLAA
GVDPAQATLFIQSKVPEHAELHLLLSMITPLGWLERVPTYKDQQEKLKEKDLSTYGFLGYPLLQSADILI
YRAGLVPVGEDQVPHVEMTREIARRFNHLYGREPGFEEKAEAAIKKLGKKRAKLYHELRNAYQEEGDDEA
LEQARALLQEQQNLSMGDRERLFGYLEGAGKIILPEPQALLTEASKMPGLDGQKMSKSYGNTIGLREDPE
SVTKKIRTMPTDPARVRRTDPGDPEKCPVWQLHQVYSDEETKEWVQKGCRSAGIGCLECKQPVIDAILRE
QQPMRERAQKYEDDPSLVRAIVADGCEKARKVARETMRDVREAMGLSY
>gnl|CDD|237036 PRK12284, PRK12284, tryptophanyl-tRNA synthetase; Reviewed
MTTRVLTGITTTGTPHLGNYAGAIRPAIAASRQPGVESFYFLADYHALIKCDDPARIQRSTLEIAATWLA
AGLDPERVTFYRQSDIPEIPELTWLLTCVAGKGLLNRAHAYKAAVDKNVAAGEDPDAGVTAGLFMYPVLM
AADILMFNAHKVPVGRDQIQHIEMARDIAQRFNHLYGGEFFVLPEAVIEESVATLPGLDGRKMSKSYDNT
IPLFAPREELKKAIFSIVTDSRAPGEPKDTEGSALFQLYQAFATPEETAAFRQALADGIGWGDAKQRLFE
RIDRELAPMRERYEALIARPADIEDILLAGAAKARRIATPFLAELREAVGLRSLSSAAQAAAAAKKKAAK
APRFKQYREDDGSFYFKLLAADGELLLQSRGFASPKDAGQVIARLQQGGAADLLQVADSPQFADAAAVDA
ALEALREALAP
>gnl|CDD|237037 PRK12285, PRK12285, tryptophanyl-tRNA synthetase; Reviewed
EDEFMVTPWEVSGIVDYDKLFEEFGIEPFTEVLPELPEPHPLMRRGIIFGHRDYDKILEAYRNGKPFAVY
TGFMPSGPMHIGHKMVFDELKWHQEFGANVYIPIADDEAYAARGLSWEETREWAYEYILDLIALGFDPDK
TEIYFQSENIKVYDLAFELAKKVNFSELKAIYGFTGETNIGHIFYPATQAADILHPQLEEGPKPTLVPVG
IDQDPHIRLTRDIAERLHGGYGFIKPSSTYHKFMPGLTGGKMSSSKPESAIYLTDDPETVKKKIMKALTG
GRATLEEQRKLGGEPDECVVYELLLYHLEEDDKELKEIYEECRSGELLCGECKKEAAEKIAEFLKEHQEK
REEAREILEKYLYDGKLA
>gnl|CDD|183405 PRK12287, tqsA, pheromone autoinducer 2 transporter; Reviewed
MAKPIITLNGLKIVIMLGMLVIILCGIRFAADIIVPFILALFIAVVLNPLVQHMVRWRVPRVLAVSLLMT
IIVMLMVLLLAYLGSSLNELARTLPQYRNSIMEPLQALEPLLQRVGIDVSVDQLAKYIDPNAAMTLVTNL
LTQLSNAMSSIFLLLLTVVFMLLEVPQLPGKFQQMMARPVEGMAAIQRALDSVSHYLVLKTAISIITGLV
AWAMLAALDVRFAFVWGLLAFALNYIPNIGSVLAAIPPIIQVLVFNGFYDALLVLAGYLLINLVFGNILE
PRIMGRGLGLSTLVVFLSLIFWGWLLGPVGMLLSVPLTIIVKIALEQTAGGQSIAVLLSDLNKE
>gnl|CDD|237039 PRK12288, PRK12288, small ribosomal subunit biogenesis GTPase RsgA
MSKRKLSKGQQRRVEANHQKRLKTSKEKPELDDSLLGEEQEGIVISRFGQHADVEAADGEVHRCNIRRTI
RSLVTGDRVVWRPGKEALEGVSGVVEAVHPRTSVLTRPDYYDGVKPIAANIDQIVIVSAVLPELSLNIID
RYLVACETLGIEPLIVLNKIDLLDDEGRAFVNEQLDIYRNIGYRVLMVSSHTGEGLEELEAALTGRISIF
VGQSGVGKSSLINALLPEAEILVGDVSDNSGLGQHTTTAARLYHFPHGGDLIDSPGVREFGLWHLEPEQV
TQGFVEFRDYLGTCKFRDCKHDDDPGCALREAVEEGKIAETRFENYHRILESMAEVKTRRHFSDTDD
>gnl|CDD|237040 PRK12289, PRK12289, small ribosomal subunit biogenesis GTPase RsgA
AGVTTTSQLLGTVVAVQANFYRVQLDEPQNLNPPSLLLCTRRTRLKKIGQQVMVGDRVIVEEPDWQGQRG
AIAEVLPRKTELDRPPVANADQILLVFALAEPPLDPWQLSRFLVKAESTGLEIVLCLNKADLVSPTEQQQ
WQDRLQQWGYQPLFISVETGIGLEALLEQLRNKITVVAGPSGVGKSSLINRLIPDVELRVGKVSGKLGRG
RHTTRHVELFELPNGGLLADTPGFNQPDLDCSPRELAHYFPEARQRLAQGNCQFNDCLHRDEPNCAVRGD
WERYEHYLEFLEEAIAQQEQLQQSADEESTLKLKIKASGQERYEPKLESKKYRRPSRRQQHQDLQDLYEN
QE
>gnl|CDD|237041 PRK12290, thiE, thiamine phosphate synthase
MVRLLIPSHLIELTGHVQQCLLLAKEQGFAIDHIELGVSPTAQFQLVKSEQTLRIGTDLISDKEGFEECD
FYLDYVSSLAVTPVAMMCQASCTIYIGLHDEKGFTLDIWQHPHAAEARALYPSSNQRLNSKVEQHLAWVL
TLLALDFPIEDALTLARAMLTQGDNVSRETWPTQFELFPTPVLNDRRLDIQVGWSKEGATRAFPTLDKQS
LGLYPVVDDVEWIERLLPLGINTVQLRIKDPQQADLEQQIIRAIALGREYNAQVFINDYWQLAIKHQAYG
VHLGQEDLEEANLAQLTDAGIRLGLSTHGYYELLRIVQIQPSYIALGHIFPTTTKQMPSKPQGLVRLALY
QKLIDTIPYQGQTGFPTVAIGGIDQSNAEQVWQCGVSSLAVVRAITLAEDPQLVIEFFDQVMAENQLLLR
SESCEPLSYKATEVADA
>gnl|CDD|237042 PRK12291, PRK12291, apolipoprotein N-acyltransferase; Reviewed
MFKKLRTNFLIFFIIKGFLIAILFSNFIYLSFFENYISIFLSSLLALLGLYLLLKSPRNSAFASGFFVGI
LWFYWIGLSFRYYDLTYLIPLIIILIGLVYGLLFYLLLFLKNPYLRLLLLFGLSFIHPFGFDWLNPEIFF
VYSYFDVSKLSLALIFLAAIFLYKKYKKKYKIIGVLLLLFALDFKPFKTSDLPLVNIELVNTNIPQDLKW
DKENLKSIINENLKEIDKAIDEKKDLIVLPETAFPLALNNSPILLDKLKELSHKITIITGALRVEDGHIY
NSTYIFSKGNVQIADKVILVPFGEEIPLPKFFKKPINKLFFGGASDFSKASKFSDFTLDGVKFRNAICYE
ATSEELYEGNPKIVIAISNNAWFVPSIEPTLQKLLLKYYARKYGKTIYHSANGSPSYIITPKLLGSIL
>gnl|CDD|237043 PRK12292, hisZ, ATP phosphoribosyltransferase regulatory subunit; Provisional
MMWQLPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDLRTFKLVDQLS
GRTLGLRPDMTAQIARIAATRLANRPGPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEV
ILLLLEALKALGLPNFTLDLGHVGLFRALLEAAGLSEELEEVLRRALANKDYVALEELVLDLSEELRDAL
LALPRLRGGREVLEEARKLLPSLPIKRALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYV
DGVGNPIASGGRYDDLLGRFGRARPATGFSLDLDRLLELQLELPVEARKDLVIAPDSEALAAALAAAQEL
RKKGEIVVLALPGRNFEDAREYARDRQIVEADGEWQVEPLA
>gnl|CDD|183411 PRK12293, hisZ, ATP phosphoribosyltransferase regulatory subunit; Provisional
MILEHEIPQGSKLYFGKSAKLKREIENVASEILYENGFEEIVTPFFSYHQHQSIADEKELIRFSDEKNHQ
ISLRADSTLDVVRIVTKRLGRSTEHKKWFYIQPVFRYPSNEIYQIGAELIGEEDLSEILNIAAEIFEELE
LEPILQISNIKIPKLVAEILGLDIEVFKKGQIEKLLAQNVPWLNKLVRIKTLEDLDEVIELVPDEIKEEL
EKLKELAESIKYENLVIAPLYYAKMRYYDDLFFRFFDGNSTLASGGNYEIDGISSSGFALYTDNLIEILL
K
>gnl|CDD|237044 PRK12294, hisZ, ATP phosphoribosyltransferase regulatory subunit; Provisional
MNNSEQLIALKESETAFLKYFNKADYELVDFSVIEKLDWKQLNHEDLQQMGERSFWQHEHQIYALRNDFT
DQLLRYYSMYPTAATKVAYAGLIIRNNEAAVQVGIENYAPSLANVQQSFKLFIQFIQQQLRDNVHFVVLG
HYQLLDALLDKSLQTPDILSMIEERNLSGLVTYLSTEHPIVQILKENTQQQLNVLEHYIPNDHPALVELK
IWERWLHTQGYKDIHLDITAQPPRSYYTGLFIQCHFAENESRVLTGGYYKGSIEGFGLGLTL
>gnl|CDD|183413 PRK12295, hisZ, ATP phosphoribosyltransferase regulatory subunit; Provisional
MMPLSASAAAAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDIRRRIFVTSDENGEELCLRPDFTIPV
CRRHIATAGGEPARYAYLGEVFRQRRDRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEV
RLGDVGLFAALVDALGLPPGWKRRLLRHFGRPRSLDALLARLAGPRVDPLDEHAGVLAALADEAAARALV
EDLMSIAGISPVGGRSPAEIARRLLEKAALAAAARLPAEALAVLERFLAISGPPDAALAALRALAADAGL
DLDAALDRFEARLAALAARGIDLERLRFSASFGRPLDYYTGFVFEIRAAGNGDPPLAGGGRYDGLLTRLG
AGEPIPAVGFSIWLDRLAALGGA
>gnl|CDD|237045 PRK12296, obgE, GTPase CgtA; Reviewed
MPRFVDRVVLHVKAGDGGNGCASVHREKFKPLGGPDGGNGGRGGSVVLVVDPQVTTLLDFHFRPHRKATN
GKPGMGDNRDGAAGEDLVLPVPDGTVVLDEDGEVLADLVGAGTRFVAAAGGRGGLGNAALASKARKAPGF
ALLGEPGEERDLVLELKSVADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQAGDTRFTV
ADVPGLIPGASEGKGLGLDFLRHIERCAVLVHVVDCATLEPGRDPLSDIDALEAELAAYAPALDGDLGLG
DLAERPRLVVLNKIDVPDARELAEFVRPELEARGWPVFEVSAASREGLRELSFALAELVEEARAAEPEAE
PTRIVIRPKAVDDAGFTVERDGDGEGGFRVRGEKPERWVRQTDFDNDEAVGYLADRLARLGVEDELLKAG
ARPGDAVTIGTGNGVVFDWEPTTPAGAEVLLGGRGTDARLEENDRPTAAERRAAYRERRDARDEARAELE
AERKAGHWTD
>gnl|CDD|237046 PRK12297, obgE, GTPase CgtA; Reviewed
MFIDQAKIYVKAGDGGDGMVSFRREKYVPKGGPDGGDGGKGGSVIFVADEGLRTLLDFRYKRHFKAENGE
NGMGKNMHGRNGEDLIIKVPVGTVVKDAETGEVIADLVEPGQEVVVAKGGRGGRGNAHFATSTNQAPRIA
ENGEPGEERELRLELKLLADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVM
ADIPGLIEGASEGVGLGHQFLRHIERTRVIVHVIDMSGSEGRDPIEDYEKINKELKLYNPRLLERPQIVV
ANKMDLPEAEENLEEFKEKLGPKVFPISALTGQGLDELLYAVAELLEETPEFPLEEEEVEEEVYYKFEEE
EKDFTITRDEDGVFVVSGEKIERLFKMTNFNRDESLRRFARQLRKMGVDDALREAGAKDGDTVRIGDFEF
EFVD
>gnl|CDD|237047 PRK12298, obgE, GTPase CgtA; Reviewed
MKFVDEAKIRVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVYLEADENLNTLIDYRFERHFRAERG
QNGQGRDCTGKRGKDITIKVPVGTRVIDADTGEVIGDLTEHGQRLLVAKGGWHGLGNTRFKSSVNRAPRQ
KTPGTPGEERELKLELKLLADVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERSFV
VADIPGLIEGASEGAGLGIRFLKHLERCRVLLHLIDIAPIDGSDPVENARIIINELEKYSPKLAEKPRWL
VFNKIDLLDEEEAEERAKAIVEALGWEGPVYLISAASGLGVKELCWDLMTFIEENPREEAEEAEAPEKVE
FMWDDYHREQLEEVEEEDDDDWDDDWDEDDDEGVEVIYKR
>gnl|CDD|237048 PRK12299, obgE, GTPase CgtA; Reviewed
KFIDEAKIYVKAGDGGNGCVSFRREKFIPFGGPDGGDGGRGGSVILEADENLNTLIDFRYKRHFKAENGE
NGMGRNRTGKSGKDLVLKVPVGTQIYDADTGELIADLTEHGQRFLVAKGGKGGLGNAHFKSSTNRAPRYA
TPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVI
ADIPGLIEGASEGAGLGHRFLKHIERTRLLLHLVDIEAVDPVEDYKTIRNELEKYSPELADKPRILVLNK
IDLLDEEEEREKRAALELAALGGPVFLISAVTGEGLDELLRALWELLEEARREEE
>gnl|CDD|237049 PRK12300, leuS, leucyl-tRNA synthetase; Reviewed
LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPILGIAERIARGDPETIELYKSLYGIPEEELEK
FKDPEYIVEYFSEEAKEDMKRIGYSIDWRREFTTTDPEYSKFIEWQFRKLKEKGLIVKGSHPVRYCPNDN
NPVGDHDLLDGEEPEIVEYTLIKFEESEDLILPAATLRPETIFGVTNLWVNPDATYVKAEVDGEKWIVSK
EAAEKLSFQDRDVEIIEEIKGSELIGKKVKNPVTGKEVPILPADFVDPDNGTGVVMSVPAHAPYDYVALR
DLKKNKELLDVIEPIPLIEVEGYGEFPAKEVVEKLGIKSQEDPELEEATKEVYRAEFHKGVLKENTGEYA
GKPVREAREKITKDLIEKGIADIMYEFSNRPVYCRCGTECVVKVVKDQWFIDYSDPEWKELAHKALDNME
IIPEEYRKEFENTIDWLKDRACARRRGLGTRLPWDEEWIIESLSDSTIYMAYYTIAHKIREYGIKPEQLT
PEFFDYVFLGKGDPEEVSKKTGIPKEILEEMREEFLYWYPVDWRHSGKDLIPNHLTFFIFNHVAIFPEEK
WPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQDADWREKEVESVRRQLER
FYELAKELIEIGGEEELRFIDKWLLSRLNRIIKETTEAMESFQTRDAVQEAFYELLNDLRWYLRRVGEAN
NKVLREVLEIWIRLLAPFTPHLAEELWHKLGGEGFVSLEKWPEPDESKIDEEAELAEEYVKRLIEDIREI
LKVAKIKPKKVYIYVAPDWKYEVLEIAAENGDVKEAIKELMKDEELRKHGKEVAKLAQKIVKEVLKLDKE
VRKLILKNIDEEEVLEEAKDFLEKELGVEVEIYGADDPGKKKKKKKALPLKPAIYIE
>gnl|CDD|183419 PRK12301, bssS, biofilm formation regulator BssS
MEKNNEVIQTHPLVGWDISTVDSYDALMLRLHYQSPNDQEPEGAEVGQTLWLTTDVARQFISILEAGIAK
IESGDYQVNEYRRH
>gnl|CDD|183420 PRK12302, bssR, biofilm formation regulator BssR
MFVDRLRIDLLNKLINARIDLAAYLQLRKAKGYMSVSESDHLRDNFFELNRELHDKSLRLNLHLDQEEWS
ALRHAEEALATAAVCLMSGHHDCPTFIAVNADKLENCLTTLTLSIQSLQKHAPLEKA
>gnl|CDD|183421 PRK12303, PRK12303, tumor necrosis factor alpha-inducing protein; Reviewed
MLEKSFLKSKQLFLCGLGVLMLQACTCPNTSQRNSFLQDVPYWMLQNRSEYITQGVDSSHIVDGKKTEEI
EKIATKRATIRVAQNIVHKLKEAYLSKSNRIKQKITNEMFIQMTQPIYDSLMNVDRLGIYINPNNEEVFA
LVRARGFDKDALSEGLHKMSLDNQAVSILVAKVEEIFKDSINYGDVKVPIAM
>gnl|CDD|237051 PRK12307, PRK12307, MFS transporter
MIAKFFPWYSEITRPQKNALFSAWLGYVFDGFDFMLIFYIMYLIKADLGLTDMEGAFLATAAFIGRPFGG
ALFGLLADKFGRKPLMMWSIVAYSVGTGLSGLASGVIMLTLSRFIVGMGMAGEYACASTYAVESWPKHLK
SKASAFLVSGFGIGNIIAAYFMPSFAEAYGWRAAFFVGLLPVLLVIYIRARAPESKEWEEAKLSGKGKHS
QSAWSVFSLSMKGLFNRAQFPLTLCVFIVLFSIFGANWPIFGLLPTYLAGEGFDTGVVSNLMTAAAFGTV
LGNIVWGLCADRIGLKKTFSIGLLMSFLFIFPLFRIPQDNYLLLGACLFGLMATNVGVGGLVPKFLYDYF
PLEVRGLGTGLIYNLAATSGTFNSMAATWLGITMGLGAALTFIVAFWTATILLIIGLSIPDRLKARRESF
QSTKEF
>gnl|CDD|183425 PRK12308, PRK12308, argininosuccinate lyase
MALWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVM
EDPEQILLSDAEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMV
NVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDRE
ALAHNLGFRRATRNSLDSVSDRDHVMELMSVASISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLM
PQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQEDKEGLFDALDTWNDCMEMAALCFDGIK
VNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCALEELSLEQLKEFSDVIEDD
VYQILTIESCLEKRCALGGVSPEQVAYAVEQADKRLAARDTSGVKVRPARLTDIDAIEGMVAYWAGLGEN
LPRSRNELVRDIGSFAVAEHHGEVTGCASLYIYDSGLAEIRSLGVEAGWQVQGQGSALVQYLVEKARQMA
IKKVFVLTRVPEFFMKQGFSPTSKSLLPEKVLKDCDQCPRQHACDEVALEVNLK
>gnl|CDD|183426 PRK12309, PRK12309, transaldolase
MMASLLEQLRQMTVVVADTGDIQAIEKFTPRDATTNPSLITAAAQMPQYQSIVDETLRQARKELGSDAPV
EDVVALAFDRLAVAFGLKILKIVPGRVSTEVDARLSYDTEATIAKARKLISLYEDAGISRDRVLIKIAST
WEGIKAAEVLEKEGIHCNLTLLFGFHQAIACAEAGVTLISPFVGRILDWYKKETGRDSYPGAEDPGVQSV
TQIYNYYKKFGYKTEVMGASFRNIGEIIELAGCDLLTISPKLLEQLRSTEAELPRKLDPANAAGMEIEKI
HMDRATFDKMHAEDRMASEKLDEGIKGFSKALETLEKLLAHRLARLEGGEAFTHAAQEIFRLYDLDGDGF
ITREEWLGSDAVFDALDLNHDGKITPEEMRAGLGAALRLAT
>gnl|CDD|183427 PRK12310, PRK12310, hydroxylamine reductase; Provisional
GDMDMFCYQCEQTATGGCTVMGVCGKDETLASLQDTLIFGLKGIAAYRYHARELGYTDPEVDAFLAEALY
STLTNVNFDLQEHIDLALKVGKANLKVMELLDKAHTETFGEPEPVEVTQGTVEGKAILVTGHNLKALEEL
LKQTEGKGINVYTHSEMLPAHGYPELKKYKHLKGNIGKAWYDQRKLFEKFPGAILGTTNCVMPPKGSYAD
RMFTYGIAGLEGVQHIENDDFTPLIEKALELPELEMESDETLVTGFHHTTVLSLAPKIIEAVKEGKIRRF
FVIAGCDAPGKGREYYRELATSLPKDTVILTLSCGKFRFNDLDYGTIEGTEIPRYIDLGQCNDSISAVKI
ALALADAFGCEVNDLPVSIVLSWMEQKAVAILLGLLSLGIKNIYIGPKLPEFLNPGVLEVLQENFNLKLI
SDPEEDLKKMLGK
>gnl|CDD|183428 PRK12311, rpsB, 30S ribosomal protein S2
MRQLLEAGVHFGHQSHRWNPKMAPYIFGTRNNIHIIDLAQTVPLLHRALQAVSDTVAKGGRVLFVGTKRQ
AQDAVADAAKRSAQYFVNSRWLGGTLTNWKTISGSIQRLRKLDEVLSSGEANGYTKKERLTLQRERDKLD
RALGGIKDMGGLPDLLFVIDTNKEDIAIQEAQRLGIPVAAIVDTNCDPDGITYPVPGNDDAGRAIALYCD
LIARAAIDGISRAQGDLGIDIGASEAPLAEELPAAAAPVETFEGLAGPRGAPDDLKKLTGVSPQIEKKLN
DLGIFHFWQLAELDPDDAAKIGEELGLPGRADGWVAQAKALVAAAE
>gnl|CDD|237052 PRK12313, PRK12313, 1,4-alpha-glucan branching protein GlgB
VKDMSMLTDDDLYLFNTGEHFRLYEYLGAHLEEVDGEKGTYFRVWAPNAQAVSVVGDFNDWRGNAHPLVR
RESGVWEGFIPGAKEGQLYKYHISRQDGYQVEKIDPFAFYFEARPGTASIVWDLPEYKWKDGLWLARRKR
WNALDRPISIYEVHLGSWKRNEDGRPLSYRELADELIPYVKEMGYTHVEFMPLMEHPLDGSWGYQLTGYF
APTSRYGTPEDFMYLVDALHQNGIGVILDWVPGHFPKDDDGLAYFDGTPLYEYQDPRRAENPDWGALNFD
LGKNEVRSFLISSALFWLDEYHLDGLRVDAVSNMLYLDYDEEGEWTPNKYGGRENLEAIYFLQKLNEVVY
LEHPDVLMIAEESTAWPKVTGPVEVGGLGFDYKWNMGWMNDTLRYFEEDPIYRKYHHNLLTFSFMYAFSE
NFVLPFSHDEVVHGKKSLMHKMPGDRWQQFANLRLLYTYMITHPGKKLLFMGSEFGQFLEWKHDESLEWH
LLEDPMNAGMQRFTSDLNQLYKDEPALWELDFSPDGFEWIDADDADQSVLSFIRKGKNKGDFLVVVFNFT
PVEREDYRIGVPVAGIYEEILNTDSEEFGGSGKGNNGTVKAQEGPWHGRPQSLTLTLPPLGALVLKPKRR
LKS
>gnl|CDD|183430 PRK12314, PRK12314, gamma-glutamyl kinase; Provisional
MMRRQLENAKRIVIKVGSSTLSYENGKINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKLDKR
PTSLAEKQALAAVGQPELMSLYSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNE
NDAVATDEIDTKFGDNDRLSAIVAKLVKADLLIILSDIDGLYDKNPRINPDAKLRSEVTEITEEILALAG
GAGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNPSDILDFLEGESIGTLFAPKK
>gnl|CDD|237053 PRK12315, PRK12315, 1-deoxy-D-xylulose-5-phosphate synthase; Provisional
MYLEKINSPADLKKLSLDELEQLASEIRTALLEKDSAHGGHVGPNLGVVELTIALHYVFNSPKDKIVWDV
SHQSYPHKMLTGRKEAFLDPDHYDDVTGYTNPEESEHDFFTVGHTSTSIALATGLAKARDLKGEKGNIIA
VIGDGSLSGGLALEGLNNAAELKSNLIIIVNDNQMSIAENHGGLYKNLKELRDTNGQSENNLFKAMGLDY
RYVEDGNDIESLIEAFKEVKDIDHPIVLHIHTLKGKGYQPAEENKEAFHWHMPFDLETGQSKVPASGESY
SSVTLDYLLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFV
NSTFLQRAYDQLSHDLAINNNPAVMIVFGGSISGNDVTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLE
WALTQHEHPVAIRVPEHGVESGPTVDTDYSTLKYEVTKAGEKVAILALGDFYELGEKVAKKLKEELGIDA
TLINPKFITGLDEELLEKLKEDHELVVTLEDGILDGGFGEKIARYYGNSDMKVLNYGAKKEFNDRVPVEE
LYKRNHLTPEQIVEDILSVLK
>gnl|CDD|237054 PRK12316, PRK12316, peptide synthase; Provisional
[encoded data, 5183 characters]
SRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEKFDDLEELLSELEEI
>gnl|CDD|237055 PRK12317, PRK12317, elongation factor 1-alpha; Reviewed
AKEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGV
TIDLAHKKFETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAGGVMPQTREHVFLARTLGIN
QLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPTLLE
ALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELP
QAEPGDNIGFNVRGVGKKDIKRGDVCGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACT
FEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVIEKVKEIPQLGRFAIRDMGQTIAAGMVIDV
KPAKV
>gnl|CDD|183434 PRK12318, PRK12318, methionyl aminopeptidase
MKRNDPCWCGSGKKWKHCHYPTKPERSLENLKQLYASQYDIIIKTPEQIEKIRKACQVTARILDALCEAA
KEGVTTNELDELSRELHKEYNAIPAPLNYGSPPFPKTICTSLNEVICHGIPNDIPLKNGDIMNIDVSCIV
DGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKYGFSVVDQFVGHG
VGIKFHENPYVPHHRNSSKIPLAPGMIFTIEPMINVGKKEGVIDPINHWEARTCDNQPSAQWEHTILITE
TGYEILTLLDK
>gnl|CDD|183435 PRK12319, PRK12319, acetyl-CoA carboxylase subunit alpha; Provisional
MTDVARILKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAGQPVTVVGIQKGKNLQD
NLKRNFGQPHPEGYRKALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPII
AIIIGEGGSGGALALAVADQVWMLENTMYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDK
VIPEHGYFSSEIIDMIKKNLIEELAQLSQKPLEQLLEERYQRFRKY
>gnl|CDD|138873 PRK12320, PRK12320, hypothetical protein; Provisional
MQILVTDATGAVGRSVTRQLIAAGHTVSGIAQHPHDALDPRVDYVCASLRNPVLQELAGEADAVIHLAPV
DTSAPGGVGITGLAHVANAAARAGARLLFVSQAAGRPELYRQAETLVSTGWAPSLVIRIAPPVGRQLDWM
VCRTVATLLRSKVSARPIRVLHLDDLVRFLVLALNTDRNGVVDLATPDTTNVVTAWRLLRSVDPHLRTRR
VRSWEQLIPEVDIAAVQEDWNFEFGWQATEAIVDTGRGLVGRRLHPAGATNGSGQLALPVEAPPRSVPSH
GEPLGSAAPEGLEGEFDDRIDERFPVFSSASLAEALPGPLTPMTLDVQLSGLRAAGRAMGRVLALGGVVA
DEWERRAIAVFGHRPYIGVSANIVAAAQLPGWDAQAVARRALGEQPQVTELLPFGRPQLAGGPLGSVAKV
VVTARSLALLRHLRSDTHHYVAAADAEHLAAGQLASLPDAGLEVRIRLLRDRIHQGWILTVLWVIDTGVT
AATLEHTRAGSAVSGGGMIMESGRIGAEIAPLAAVLRADPPLCALANDGNLASIRALSAPAAAAVDAVIA
RIGHRGLGEAELANLTFADDPALLLKTAAEIAARPAGPAHPATLIQRLAAGTRSARELAHDTTIRFTHEL
RMTLRELGSRRVAADVIDVVDDVFYLTCDELITTPADARLRIKRRRAERERLQAQRPPDVIDHAWVPVE
>gnl|CDD|237056 PRK12321, cobN, cobaltochelatase subunit CobN; Reviewed
MHLLFRESHGLDETETPVDLGQSPADLVVLSFSDSDLGALAAAWAAAGGGLPSLRLANLAALRHPMSVDL
YVEQVLAGAKAVLIRLLGGLDYWRYGLERLAALARARGIALAVLPGDGRPDPRLDALSTLPVSTLRRLDA
YCRAGGPVNAQAALAQLALAAGLYAGPVAPPKALPRGGFYCPGRGVVALPTACAGADAPLALVLFYRSYL
LAADTAPVDALAAALRARGFAAVGLFVPSLKDPEAAAWLRAALAALRPAAIVNATAFSARGDDGASPLDA
ADCPVFQVALATARRAAWAASERGLSPADLAMHVVLPEVDGRLFAGPISFKEEAARDPDLGFSRFAHRPD
PARIAAVADRAAAWVRLARTPRAERRLALVLSDYPGRGGRAAHAVGLDAPASARAILADLAAAGYATGAP
PDAAALAARLTTPRLSWPLADYRAALATLPEELRAALTAAWGAPEADPACRDGAFRFRALRAGHLLVALQ
PDRGRRADRKADYHDPARPPRHAYVAFYLWLREVGVDALIHLGAHGTLEWLPGKAVALSPACWPEALTGA
LPVIYPFIVNDPGEAAQAKRRLGAVTLGHLPPPLAAAGLPPELARLERLVDEYSTADGLDPRRRDRLARA
IRDEARAAGLEADAGLDADTPPAEALTRIDAFLCDLKESQFRDGLHVFGRAPAGAAEPVRASAEAERAAL
LAALDGRRVAPGPAGSPSRGRSDVLPTGRNLFTVDPRAVPTRAAHALGVKAAEELLRRHLQDHGDWPRGL
VMDLWGSATLRTGGEEFAMALALMGVRPVWDHASGRVTGIEVLPLALLDRPRIDVTLRVSGLFRDVFPAL
IALFDQAARAVAAREEADEDNPLAARRGERAARVFGPAPGSYGAGAAELALDGAWEARAELGEAYLAASS
HAYGGAGGGAPARAAFAARVAAADAFVHAQDLAERDLLDGDDYAAHEGGFAAAAASLGAAAALYHLDTTR
PDRPRARTLTEEIARVVRGRAANPRWIAGMMRHGFRGAAEIAATLDALAAFAALTDAVPDHLFDLLHDAT
LGDEDVRAFLARANPAALAAMRDRFAELRRRGLWQSRRNSIAADLAAAAE
>gnl|CDD|183437 PRK12322, PRK12322, NADH-quinone oxidoreductase subunit D
MLRTEEMLLNVGPQHPSTHGVFRLVLKIDGEIIVEATPVIGYLHRGTEKLAESLQYTQIIPYTDRMDYLS
AMTNNYVYCHAVETMMGLEVPERAEYLRVIAMELGRIASHLVWWGTYLLDIGAVSPFLYAFREREMIINL
LNELCGARLTFNYMRIGGVKWDAPDGWIEKVKEFVPYMREQLAGYHDLVTGNEIFLNRVKGVGIYSAEEA
ISYSLSGVNLRCTGVNWDLRKDEPYSIYDRFDFDIPVGSVGDCWDRYVCRMQEIEQSLKIIEQAVEQFPK
EGPVLAKVPKIIKAPKGEAYVRIESPRGEIGCYIASDGKKKPYRLKFRRPSFYNLQILPKLLKGENIANL
IAILGSIDIVLGEVDG
>gnl|CDD|237057 PRK12323, PRK12323, DNA polymerase III subunit gamma/tau
MSYQVLARKWRPRDFTTLVGQEHVVRALTHALEQQRLHHAYLFTGTRGVGKTTLSRILAKSLNCTGADGE
GGITAQPCGQCRACTEIDAGRFVDYIEMDAASNRGVDEMAQLLDKAVYAPTAGRFKVYMIDEVHMLTNHA
FNAMLKTLEEPPEHVKFILATTDPQKIPVTVLSRCLQFNLKQMPPGHIVSHLDAILGEEGIAHEVNALRL
LAQAAQGSMRDALSLTDQAIAYSAGNVSEEAVRGMLGAIDQSYLVRLLDALAAEDGAALLAIADEMAGRS
LSFAGALQDLASLLQKIALAQVVPAAVQDDWPEADDIRRLAGRFDAQEVQLFYQIANLGRSELALAPDEY
AGFTMTLLRMLAFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVA
AAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPA
PADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPV
VAPRPPRASASGLPDMFDGDWPALAARLPVRGLAQQLARQSELAGVEGDTVRLRVPVPALAEAEVVERLQ
AALTEHFGQPVRVVCEVGAVGATAAAVDAEERAERQRAAEDAIAADPFVQALVRDFGGQVVPGSIQPHAA
>gnl|CDD|237058 PRK12324, PRK12324, decaprenyl-phosphate phosphoribosyltransferase
TVVRGPPKNLLAGYLKLLRPKQWIKNLFVFAAPIFAGNLLNPGALLKVLLAFVLFCLASSAVYLVNDIRD
VEADRLHPTKRNRPIASGVVSVSLAYILAVVLLVASLALAYLLSPKLALVLLVYLVLNLAYSFKLKHQPV
LDVFCIASGFVLRAIAGGVAIGVPLSPWLLLCTALLSLFLAAGKRKAELRLLEDTGAKHRKVLEEYSPGF
LDFMWTIVATAVLVTYSLYAFESGASSPWMIVTIPPVLYGIFRYAYLDVDKGLGGEPEEILLKDRPLLLN
ALLWIILVGIALYFG
>gnl|CDD|237059 PRK12325, PRK12325, prolyl-tRNA synthetase; Provisional
MRLSRYFLPTLKENPKEAEIVSHRLMLRAGMIRQQAAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEIL
MPTIQPADLWRESGRYDAYGKEMLRIKDRHDREMLYGPTNEEMITDIFRSYVKSYKDLPLNLYHIQWKFR
DEIRPRFGVMRGREFLMKDAYSFDLDEEGARHSYNRMFVAYLRTFARLGLKAIPMRADTGPIGGDLSHEF
IILAETGESTVFYDKDFLDLLVPGEDIDFDVADLQPIVDEWTSLYAATEEMHDEAAFAAVPEERRLSARG
IEVGHIFYFGTKYSEPMNAKVQGPDGKEVPVHMGSYGIGVSRLVAAIIEASHDDKGIIWPESVAPFKVGI
INLKQGDEACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIVGPKGLAEGKVELKDR
KTGEREELSVEAAINRLTA
>gnl|CDD|183445 PRK12330, PRK12330, methylmalonyl-CoA carboxytransferase subunit 5S
MPRKIGVTELALRDAHQSLMATRMAMEDMVGACEDIDNAGYWSVECWGGATFDACIRFLNEDPWERLRTF
RKLMPNSRLQMLLRGQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHA
QGTICYTVSPIHTVEGFVEQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACGEDTRINLHCHST
TGVTLVSLMKAIEAGVDVVDTAISSMSLGPGHNPTESLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKY
KEFESKTTGVETEIFKSQIPGGMLSNMESQLKQQGAGDRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQ
AVFNVLMGRYKVLTGEFADLMLGYYGETPGERNPEVVEQAKKQAKKEPITCRPADLLEPEWDKLRAEALA
LEGCDGSDEDVLTYALFPQVAPKFFATRAEGPKNVGKDPAQGAAEAAAAAGHAGAITGPITYKVTVGGRS
HKVTVAPAK
>gnl|CDD|183446 PRK12331, PRK12331, oxaloacetate decarboxylase subunit alpha
MTKIKITETVLRDGQQSLIATRMTTEEMLPILEKLDNAGYHSLEMWGGATFDACLRFLNEDPWERLRKIR
KAVKKTKLQMLLRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQ
VAISYTTSPVHTIDYFVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAVTVPLEVHTHATSGI
AEMTYLKAIEAGADIIDTAISPFAGGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYREE
GILNPKVKDVEPKTLIYQVPGGMLSNLLSQLKEQGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQ
ALMNVISGERYKMVPNEIKDYVRGLYGRPPAPIAEEIKKKIIGDEEVITCRPADLIEPQLEKLREEIAEY
AESEEDVLSYALFPQQAKDFLGRREDPF
>gnl|CDD|183447 PRK12332, tsf, elongation factor Ts; Reviewed
MAITAKLVKELREKTGAGMMDCKKALEEANGDMEKAIEWLREKGLAKAAKKAGRVAAEGLVGSYIHTGGR
IGVLVELNCETDFVARTEEFKELAKDIAMQIAAANPEYVSREDVPAEVIEKEKEIYRAQALNEGKPENIV
EKIVEGRIEKFYKEVCLLEQPFIKDPSKTVEDLIKEAIAKIGENIVVRRFARFELGEG
>gnl|CDD|237064 PRK12333, PRK12333, nucleoside triphosphate pyrophosphohydrolase; Reviewed
MERLLEVMRRLRGPDGCPWDREQTHESLRPYLLEEAAEAVDALSEGDPQELAEELGDVLLQVAFHSVIAE
EEGRFTYPDVERGIVEKLIRRHPHVFGDVQVSGPEEVVANWQAIKAAERGGGPRSAAERVPASLGALARA
AELQKKLGREAGSREGVIAALEEGGVAEALWAVVAWARAEGIDPEIALRERTEKACAQLPDEVE
>gnl|CDD|237065 PRK12334, PRK12334, nucleoside triphosphate pyrophosphohydrolase; Reviewed
PVEAIELLRTSVQYTEEMPTAVAWSLPAARPVHAGDPDHPAVPARLAAGARLISAPDDQPGARLLDAVAV
MDRLRSPGPWESEQTHRSLARYLLEETYELLDAIESGDRDELREELGDVLLQVLFHARIAEEAPEDPFDI
DDVAATLVAKLVRRHPHVFADGEAISLEEQLAQWEARKAAEKARTSVLDGVPLGQPALALAAKVLSRARK
AGLPVPLAPAEDSEDELGALLLALVAVAVAAGVDAEAALRAAVRDFRDRIRAAERAAAADGLGGITE
>gnl|CDD|183450 PRK12335, PRK12335, tellurite resistance protein TehB; Provisional
EMQELICYKQMPVWNKDTLPEMFQEKHNTKEGTWAKLTVLKGELKFYELTEDGEELSEHIFDAENQPPFI
EPQAWHRIEAASDDLECQLSFYCKPEDYFHKKYNLTATHSEVLEAVQTVKPGKALDLGCGQGRNSLYLAL
LGFDVTAVDINQQSLENLQEIAEKENLNIRTGLYDINSASIQEEYDFILSTVVLMFLNRERIPAIIKNMQ
EHTNPGGYNLIVCAMDTEDYPCPMPFSFTFKEGELKDYYQDWEIVKYNENVGHLHKTDENGNRIKLRFAT
LLAKKVK
>gnl|CDD|183451 PRK12336, PRK12336, translation initiation factor IF-2 subunit beta; Provisional
MDYESLLDRAMEVLPEPTKSGERFSIPEPKIFIEGKTTILTNFGEIADALNRDPDHLMKFLQRELGTAGK
IEGGRAVFNGKFTEEDIQAAIDAYVDEYVICSECGLPDTRLVKEDRVLMLRCDACGAHRPVKKRKASSET
QREAIEEGKTYEVEITGTGRKGDGVAKKGKYTIFVPGAKKGEVVKVKIKKISGNLAFAERA
>gnl|CDD|183452 PRK12337, PRK12337, 2-phosphoglycerate kinase; Provisional
IGSRRHRWPFSRGLVVEALLNAGAKTEVAAALARTVEEQLRLRRRSEVTPLALQRLLAEEVEDVLGPEVA
ARLARQTPAFVDIVVREGRGRRPFSRGVLARSLEDAGFSPREAYELASAVELRLRQEGVREIGAKELEKR
TARELAERYGEEARLRYRARQQNAGELFVEEAEGAPRVPFSKGILAQSLMAAGLAPDVARRLARETERDL
RRSGDRVVRRDQLRRKVEALLLEEAGEEVARRYRLLRSIRRPPRPLHVLIGGVSGVGKSVLASALAYRLG
ITRIVSTDAVREVLRAMVSKDLLPTLHASTFNAWRALLPPGEGLPAEPTRAEVLRGFRDQVQQVAVGLGA
IQERSAQEGTSLVLEGVHLVPGYLRHPYQAGALVVPMLVTLPDEALHRRRFELRDRETGASRPRERYLRH
FEEIRLIQDHLLRLARQEGVPVLPGEDLDESIDKALEVVLRRVMAALTPEERAAL
>gnl|CDD|237066 PRK12338, PRK12338, hypothetical protein; Provisional
MRKPYVILIGSASGIGKSTIASELARTLNIKHLIETDFIREVVRGIIGKEYAPALHKSSYNAYTALRDKE
NFKNNEELICAGFEEHASFVIPAIEKVIERAVTDSDDIVIEGVHLVPGLIDIEQFEENASIHFFILSADE
EVHKERFVKRAMEIKRGGKQLEYFRENRIIHDHLVEQAREHNVPVIKNDDIDCTVKKMLSYIREVCVTVT
LQHSVDDLDEVIEIIIKRHGGRITDISYPIPGFKDPLKREVNVSDPDEAEKFIKRLNENPKKKEDLKRLY
SLSNNVHSHRICAPDEESLNRIIEELEEEGLLYEEERPG
>gnl|CDD|105560 PRK12339, PRK12339, mevalonate-3-phosphate 5-kinase
MESTIHFIGGIPGVGKTSISGYIARHRAIDIVLSGDYLREFLRPYVDDEPVLAKSVYDAWEFYGSMTDEN
IVKGYLDQARAIMPGINRVIRRALLNGEDLVIESLYFHPPMIDENRTNNIRAFYLYIRDAELHRSRLADR
INYTHKNSPGKRLAEHLPEYRTIMDYSIADARGYNIKVIDTDNYREARNPLLDPISK
>gnl|CDD|183454 PRK12341, PRK12341, acyl-CoA dehydrogenase
MDFSLTEEQELLLASIRELITRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQ
MLVLEEVSKCGAPAFLITNGQCIHSMRRFGSAEQLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTY
TRKNGKVYLNGQKTFITGAKEYPYMLVLARDPQPKDPKKAFTLWWVDSSKPGIKINPLHKIGWHMLSTCE
VYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLI
QEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSR
FWRDVRCERIGGGTDEIMIYIAGRQILKDYQ
>gnl|CDD|183455 PRK12342, PRK12342, electron transfer flavoprotein
MKIITCFKLVPEEQDIVVTPERTLNFDNAEAKISQFDLNAIEAASQLATDGDEIAALTVGGSLLQNSKVR
KDVLSRGPHSLYLVQDAQLEHALPLDTAKALAAAIEKIGFDLLLFGEGSGDLYAQQVGLLLGELLQLPVI
NAVSKIQRQGNKLIVERTLEDDVEVLELSLPAVLCVTSDINVPRIPSMKAILGAGKKPVTQWQASDIGWS
QSAPLAELVGIRVPPQTERKHIILDNDSPEAIAELAEHLKKALN
>gnl|CDD|237067 PRK12343, PRK12343, cyclic pyranopterin monophosphate synthase MoaC
HVDEDGVKMVDVSEKEDVLRIAVAEGFIKLKPETIEAIREGEVEKGNVLATARVAGILAVKKTPELIPMC
HPIPITGVDVDFEVGEDGIEARVTVKTTYKTGVEMEALTGVSVALLTIWDMVKAAEKDEDGQYPETRIEN
IRVVEKIKEED
>gnl|CDD|237068 PRK12344, PRK12344, putative alpha-isopropylmalate/homocitrate synthase family transferase; Provisional
MMMERIELYDTTLRDGAQGEGISFSVEDKLRIARKLDELGVDYIEGGWPGSNPKDTEFFKRAKELKLKHA
KLAAFGSTRRAGVSAEEDPNLQALLDAGTPVVTIFGKSWDLHVTEALRTTLEENLAMIRDSVAYLKAHGR
EVIFDAEHFFDGYKANPEYALATLKAAAEAGADWVVLCDTNGGTLPHEVAEIVAEVRAAPGVPLGIHAHN
DSGCAVANSLAAVEAGARQVQGTINGYGERCGNANLCSIIPNLQLKMGYECLPEEKLKELTEVSRFVSEI
ANLAPDPHQPYVGASAFAHKGGIHVSAVLKDPRTYEHIDPELVGNRRRVLVSELAGRSNILAKAKELGID
LDKDDPRLKRLLERIKELEAEGYQFEAAEASFELLLRRELGEYPPFFELESFRVIVEKRGDGVSEATVKV
RVGGEREHTAAEGNGPVNALDNALRKALEKFYPELAEVELVDYKVRILDGGKGTAAVVRVLIESTDGKRR
WTTVGVSTNIIEASWQALVDSIEYKLLKDKEAAG
>gnl|CDD|183458 PRK12346, PRK12346, transaldolase A; Provisional
MNQLDGIKQFTTVVADSGDIESIRHYHPQDATTNPSLLLKAAGLPQYQHLIDDAIAWGKKQGGTQEQQVV
AACDKLAVNFGAEILKSVPGRVSTEVDARLSFDREKSIEKARHLVDLYQQQGIDKSRILIKLASTWEGIR
AAEELEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRIYDWYQARKPMDPYVVEEDPGVKSVRNIYD
YYKQHRYETIVMGASFRRTEQILALAGCDRLTISPNLLKELQESESPVERKLIPSSQTFPRPAPMSEAEF
RWEHNQDAMAVEKLSEGIRLFAVDQRKLEDLLAAKL
>gnl|CDD|183459 PRK12347, sgbE, L-ribulose-5-phosphate 4-epimerase; Reviewed
MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGS
KKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGE
YEYQTGEVIIETFEERGISPAQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAM
QNELLDKHYLRKHGANAYYGQ
>gnl|CDD|183460 PRK12348, sgaE, L-ribulose-5-phosphate 4-epimerase; Reviewed
MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGEYR
PSSDTATHLELYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYE
LNTGKVIIETLGNAEPLHTPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGINPQLNHIDSYL
MNKHFMRKHGPNAYYGQK
>gnl|CDD|237069 PRK12349, PRK12349, citrate synthase
AEEKFSPGLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKL
KEEYAVPEGVFNILKALPKETHPMDGLRTGVSALAGYDNDIEDRSLEVNKSRAYKLLSKVPNIVANSYHI
LNNEEPIEPLKELSYSANFLYMLTGKKPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALT
GAVASLKGSLHGGANEAVMYMLLEAGTVEKFEELLQKKLYNKEKIMGFGHRVYMKKMDPRALMMKEALKQ
LCDVKGDYTLYEMCEAGEKIMEKEKGLYPNLDYYAAPVYWMLGIPIQLYTPIFFSSRTVGLCAHVIEQHA
NNRLFRPRVNYIGERHVLS
>gnl|CDD|237070 PRK12350, PRK12350, citrate synthase 2; Provisional
FVPGLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVDGRFGPGLPPAEPFPLPVHLG
DARVDVQAALAMLAPVWGFRPLLDIDDLTARLDLARASVMALSAVAQSARGIGQPAVPQREIDHAATILE
RFMGRWRGEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARV
LPMLDAVERTGDARGWVKGALDRGERLMGFGHRVYRAEDPRARVLRATAKRLGAPRYEVAEAVEQAALAE
LRERRPDRPLETNVEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKRTGRLVRPSARYVGPAPR
SPE
>gnl|CDD|183463 PRK12351, PRK12351, methylcitrate synthase; Provisional
MAAFKPKKSVALSGVVAGNTALCTVGKSGNDLHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYK
TKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLGCLLPEKEDHNFSGARDIADRLLASLGSILLYW
YHYSHNGRRIEVETDDDSIGGHFLHLLHGKKPSESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMY
SAITGAIGALRGPKHGGANEVAFEIQQRYDTPDEAEADIRRRVENKEVVIGFGHPVYTISDPRNKVIKEV
AKKLSKEAGDTKLYDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGVPTAMFTPLFVISRTTGWAAHVIE
QRQDNKIIRPSANYTGPEDRKFVPIEKR
>gnl|CDD|183464 PRK12352, PRK12352, putative carbamate kinase; Reviewed
MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHER
EGLPLTPLANCVADTQGGIGYLIQQALNNRLARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQ
RDELQKANPDWRFVEDAGRGYRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGDYQSV
DAVIDKDLSTALLAREIHADILVITTGVEKVCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKII
ASLTFLEQGGKEVIITTPECLPAALRGETGTHIIKT
>gnl|CDD|237071 PRK12353, PRK12353, putative amino acid kinase; Reviewed
MMKKIVVALGGNALGSTPEEATAQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASEKN
KVPAMPLDVCGAMSQGYIGYHLQNALRNELLKRGIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEE
AEKLAKEKGYTFKEDAGRGYRRVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIREGGGLKGVEA
VIDKDFASAKLAELVDADLLIILTAVDKVYINFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAA
ISFVESRPGRKAIITSLEKAKEALEGKAGTVIVK
>gnl|CDD|183466 PRK12354, PRK12354, carbamate kinase; Reviewed
MRIVVALGGNALLRRGEPLTAENQRANIRIAAEQIAKIAREHELVIVHGNGPQVGLLALQNAAYKDVTPY
PLDVLGAETEGMIGYMLEQELGNLLPERPVATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEKG
WTIKPDGDYFRRVVPSPRPKRIVEIRPIRWLLEKGHLVICAGGGGIPVVYDADGKLHGVEAVIDKDLAAA
LLAEQLDADLLLILTDVDAVYLDWGKPTQRAIAQATPDELRELGFAAGSMGPKVEAACEFVRATGKIAGI
GSLEDIQAILAGEAGTRISPETAGIDY
>gnl|CDD|237072 PRK12355, PRK12355, type-F conjugative transfer system mating-pair stabilization protein TraN
MKRLLPLLLALVAGLAAADSNSDYRAGSDFAKQIKGQGTGSIQGFSPQATIPGYTANPPETKYYGGVTAG
GDGGLKSDGTAAWATDETGKAITESFNNGPPDIISPDAPFIQTGRDVANRADSIVGNTGQQCTAQPVSRS
EFTNYTCERDTNVEQTCTRTASITVDASTTTETRTYTYQCSQLPASIVGGQYVVSFTAPVTGTLLSASLP
VQGTVTAGAGFTSSGTCGNGDRRVGNSLFQGGVTFTLTLTMTVPDKTYTPTVVWVESCPFCKADGTLTGE
TCTEPGGTRTRVINGIPVTRDCWAYQDTYQCQSADTGNCATLADNPACTLVSRQCAFYSNGGGCLHEEAT
YSCPEKKTSGTVMVCGGDVFCLDGDCFDTSSTNSNDFGQAVSALAALAEAGKDVDADDVRIFTGKAESCR
KKAAGFSNCCKDSGWGQDIGLAKCSSEEKALGKAKGNKLTVSVGEYCSKKVLGVCLEKKRSYCCFDSKLA
RIVQEQGRNQLGKGFGSAKHPDCSGFTVDELQKIDFSRIDFSEFYEDLMNNQKLPDSGEITQRVQEKI
>gnl|CDD|237073 PRK12356, PRK12356, glutaminase; Reviewed
TGMLPDAEQLQQAVDQAYAQFKSDTGGKNADYIPALANVPSDLFGVAVVTTDGQVYSAGDSDYRFAIESI
SKVFTLALALEDVGPQAVREKIGADPTGLPFNSVIAIELHGGKPLNPLVNAGAIATTSLVPGANSDERWQ
RILDGQQRFAGRELALSDEVYQSEQTTNFHNRAIAWLLYSYGRLYCDPMEACDVYTRQCSTLVTARDLAT
MGATLAAGGVNPLTGKRVVDADNVPYILAEMTMEGLYERSGDWAYTVGLPGKSGVGGGILAVVPGKMGIA
AFSPPLDSAGNSVRGQKAVAYVADKLGLNLFKGAPYTEK
>gnl|CDD|237074 PRK12357, PRK12357, glutaminase; Reviewed
MIKDSSVQVEGQEKVCLDQWVAHYRTYAAEGRSASYIPALGEINVSQLGICIVKPDGTMIKSGDWEVPFT
LQSISKVISFIAACLSRGISYVLERVDVEPTGDAFNSIIRLEIHKPGKPFNPMINAGAITVASLLPGTSV
QEKLESLYVLIEKMIGKRPAINEEVFQSEWETAHRNRALAYYLKETGFLESDVEETLEVYLKQCSIEVTT
EDIALIGLILAHDGYHPIRKEQVIPKEVARLTKALMLTCGMYNASGKFAAFVGLPAKSGVSGGIMTLVPP
KSRKDLPFQDGCGIGIYGPAIDEYGNSLPGIMLLKHIAKEWDLSIF
>gnl|CDD|183470 PRK12358, PRK12358, glucosamine-6-phosphate deaminase
MKIIITKDYEEMSRVAAHHLLGYMSKTKRVNLAITAGSTPKGMYEYLITLVKGKAWYDNVHYYNFDEIPF
RGKEGEGVTITNLRNLFFTPAGIKEENIHKLTIDNYREHDQKLARDGGLDLVVLGLGADGHFCGNLPGTT
HFHDETVEVPIQGEMVDIVAHGELGGDFSLVPDSYVTMGPKSIMAAKNLLLIVNGKGKAQILKKVLQGPV
TEDVPASILQLHPNLTVILDEAAAAELAL
>gnl|CDD|183471 PRK12359, PRK12359, flavodoxin FldB; Provisional
MKIGLFYGSSTCYTEMAAEKIRDIIGEELVDLHNLKDDPPKLMEQYDVLILGIPTWDFGEIQEDWEAVWD
QLDDLNLEGKIVALYGMGDQLGYGEWFLDALGMLHDKLAPKGVKFVGYWPTEGYEFTSSKPLTADGQLFV
GLALDEVNQYDLSDERIQQWCEQILLEMAELL
>gnl|CDD|237075 PRK12360, PRK12360, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Provisional
MKILIAKNAGFCFGVKRAIDTAYDEIEKNDGKKIYTLGPLIHNNQVVSDLEEKGVKTIEESEIDSLKEGD
VVIIRSHGVSKKVYKDLKDKGLEIIDATCPFVKKIQNIVEEYYNKGYSIIIVGDKNHPEVIGINGWCDNS
AYIVNSIEEVENIPFLDKACVVAQTTIIPELWEDILNVIKLKSKELVFFNTICSATKKRQESAKELSKEV
DVMIVIGGKHSSNTQKLVKICEKNCPNTFHIETADELDLEMLKDYKIIGITAGASTPDWIIEEVIKKIKN
L
>gnl|CDD|183473 PRK12361, PRK12361, hypothetical protein; Provisional
MLSRIHIKYYYLAGALLLLYLAVTGPSILLTFLFAWISLSLFLVGSAYWFNLASIFRKRQDGTIPWYIRW
VFIPFLLGTRLYNAWARKRDSVPAIQKIDENLYLGCRLFPADLEKLKSNKITAILDVTAEFDGLDWSLTE
EDIDYLNIPILDHSVPTLAQLNQAINWIHRQVRANKSVVVHCALGRGRSVLVLAAYLLCKDPDLTVEEVL
QQIKQIRKTARLNKRQLRALEKMLEQGKLNIHKRAWLIANPVSGGGKWQEYGEQIQRELKAYFDLTVKLT
TPEISAEALAKQARKAGADIVIACGGDGTVTEVASELVNTDITLGIIPLGTANALSHALFGLGSKLIPVE
QACDNIIQGHTQRIDTARCNDRLMLLLVGIGFEQKMIESADRERKNALGQLAYLDGLWRAVNENETLTLT
VTLDDAEPQTISTHSLVVANAAPFTSLLAQGGGEPNMTDGLLDITWLDSGGEPGEQLLSLAELALSGLGK
EPEANKVHHAHAKKVTISSQKPIKYVIDGELFEDEDLTIEVQPASLKVFVPYQEINE
>gnl|CDD|171438 PRK12363, PRK12363, phosphoglycerol transferase I; Provisional
MHWILLLSLLLLLWLLVASPRLAWLKAGLLSLFLLLLSAWGLVDRLSGDGVNAATLYHLRADMDGAGVSD
FSGYIAVFIGMILLSLSPLFAFRVRRFRRPRGGGALFAGFVFMLVVTIAQSPLYRDGKRLYYQLRPVDFA
TVAPEYQVPQQPLQKRKNIVWIYGESLERTYFDEDVFPGLMPNLTRLATEAVDVRNLASTEGSGWTIAGM
VASMCGVPLTTAQGDENSMDRMGHFLPEARCLGDYLKDQGYTNHYVGGADASFAGKGKFLSSHGFDEVHD
VNYFLHDKGVAPKHFSAWGVHDDVLLDDAYDEFETLSRAGQPFMLTTLTMDTHHPAGHLPSACKGQRYDS
PLGDIGMLHAIKCSDRLIGQLVDRIRNSRYGKNTIIVIASDHLAMPNDLSDVLTKQKRENLLLFLGKDIA
PQQVVTRAGTTLDSGATLLQLLEPGMRTLGFGRSLLADDAPPSASVAASRDSGKDYPRYLAFARSLWTGR
STRMLRINGNGDVVVGVQQVQPPVLLEYDKDTNLKSVYLENTSRQFDRTHSDGTLAYVDRCTAFEDGSAD
GDWCALVVDRQNTMKLYRDPDLTRGIAVDAPLEATQQGPRPRVRQPIMLTQAARKTLAGRYMLELYASRR
PTRAFWVEAVSSERKVVLAQQWVVPDAKGRIRMPVGLEHAVEDLEIRAWLDYTEEVSVDDFALVKDCNVA
DRS
>gnl|CDD|237077 PRK12364, PRK12364, ribonucleoside-diphosphate reductase subunit alpha
MEIIKRNGTTEPYDREKIEVAIRKAFASVGKPISDEIIYSLVAEVERFIKEKYPNGHNVSVEEIQDLVEK
TLMEHGHYAEVKSYILYRAQRTEKRKAREQIIKFFDDDTVLGVLKEIQKDFPSDEYSLDLLAEKFLSFCK
PNMSEGESLAALIKAAVELTTQEAPDWEFIAARLLMLQFSKKLGKSLEKLGIHSFYDKIKYLTEEGLYGS
YILEHYSREEIEEAAGFIDPERDKLFTYSGLDLLLKRYVIRTHSHEPLESPQEMFLGIALHLAMPEKQDR
MGWVKRFYDMLSKLKVTMATPTLSNARKPFHQLSSCFIDTVPDSLDGIYRSIDNFAQVSKFGGGMGLYFG
KVRAVGSNIRGFQGVAGGVIRWIKLANDTAVAVDQLGMRQGAVAVYLDVWHKDIPEFLQLRTNNGDDRMK
AHDVFPAVCYPDLFWKMVRDDINQSWYLFCPHEILTVKGYALEDYYGEEWEKRYLDCVNDARISKRSIPI
KDLVRLILKSAVETGTPFTFNRDTVNRANPNKHKGMIYCSNLCTEIAQNMSAIETVSTEIETEDGDTVVV
TTTRPGDFVVCNLASLSLGNIDLEDEEELEEVVRTVVRALDNVIDLNFYPVPYAQITNKRYRSIGLGVSG
YHHALAKNGIRWESEEHLEFADRVFERINYAAIKASMEIAKEKGAYGYFEGSDWQTGAYFRKRGYTSEEW
QRLAREVAENGMRNAYLLAVAPTSSTSIIAGTTAGVDPVMKRYFLEEKKGALMPRVAPELSDKTFWLYKN
AHLIDQKWSIRAAGVRQRHIDQAQSVNLYITNEFTMRQVLDLYLLAWEEGVKTIYYVRSKSLEVEECESC
SS
>gnl|CDD|171440 PRK12365, PRK12365, ribonucleoside-diphosphate reductase subunit alpha
MVEVQEKQYTIVKRNGMFVPFNQNRIFQALEAAFRDTRSLEDHSPLPEDLESSIRSITHQVVKEVVQKIT
EGQVVTVERIQDMVESQLYVNGLQDVARDYIVYRDDRKAHRKKSWQSLSVIRRDGTVVHFNPMKISAALE
KAFRATDKIEGMTPSSVLEEINALTQNIVEEILECCSQEDRIDIEKIQDIVEQQLMVVGHYDVAKNYILY
REARARVRDNKEEDGSTEKTIAEEAYEVLSKDGSTYTMTKSQLLAHFAWACSRFPETTDAALLADMAFAN
FYSGIKESEVVLACIMAARANIEKEPDYAFVAAELLLDVVYKEALGKSKYDEDLEEAHKDHFKRYILEGD
TYRLNPELKHYDLDALAEALDLSRDLQFSYMGVQNLYDRYFNHHEGRRLETPQIFWMRVSMGLALNEGQD
KTSWAITFYNLLSTFRYTPATPTLFNSGMRHSQLSSCYLSTVQDDLVHIYKVISDNAMLSKWAGGIGNDW
TAVRATGALIKGTNGKSQGVIPFIKVANDTAVAVNQGGKRKGAVCVYLEVWHLDYEDFLELRKNTGDERR
RTHDINTASWIPDLFFKRLQQKGTWTLFSPDDVPGLHEAYGEEFEKLYEEYERKVDTGEIRLYKKVEAED
LWRKMLSMLYETGHPWMTFKDPSNIRSAQDHKGVVRCSNLCTEILLNCSETETAVCNLGSINLVEHIVND
GLDEEKLSETISIAIRILDNVIDINFYPTKEAKEANLAHRAIGLGVMGFQDALYKLNISYASQEAVEFAD
YSSELIAYYAILASSLLAKERGTYSSYKGSKWDRGYLPIDTIELLKEYRGEANLLMDTSSRKDWEPVRSL
IKEYGMRNSQLMAIAPTATISNIIGVTQSIEPTYKHLFVKSNLSGEFTIPNVYLIEKLKKLGIWDADMLD
DLKYFDGSLLEIERIPDHLKKIFLTAFEIEPEWIIECASRRQKWIDMGQSLNLYLAEPDGKKLSNMYLTA
WKKGLKTTYYLRSSAATSVEKSFVDINKRGIQPRWMKNKSASTSIVVERAKKTPVCSLEEGCESCQ
>gnl|CDD|237078 PRK12366, PRK12366, replication factor A; Reviewed
DYMNIKKLKQKILEKISEEELEKKINEKIEENGGFLGEEAALMMVAQELGIDIEYGQEEEEEDFKISDIE
EGQINVEITGRIIEISNIKTFTRKDGSTGKLANITIADNTGTIRLTLWNDNAKLLKGLKEGDVIKIENAR
SRKWNNDVELNSGSETRIDKLEKYDESRYPIIKENYDIPELEPNLSATIEGEVTKAYPIKEFTRKDGSEG
KLKSFILKDDTGSIRVTLWNDLTDIEVNKGDIVRVKGYVKQGYRTGLEISANNIEILEKLEKEEKELEIV
NIEELTEFEDGEEVDVKGRIIAISDKREVERDDRTAEVQDIELADGTGRVRVSFWGEKAKILENLKEGDA
VKIENCKVRTYYDNEGEKRVDLNAGYSSEIIKDESISFEEIEEKIYKIKDILNLEEDDNDITVIARVVED
YPVNEFERSDGSKGKVRNIELADGTGSIRLTLWDDDAEIEIKEGDAIKILHPYVKENGDYLDLSIGRYGR
IEINPEGEIIKSNRKFIADLEEDDTVEIRGTVVDIRKQKIILYLCPNCRKRVEEVDGEYICEFCGEVEPN
ELLMLNFTLDDGTGTINCRFYGKNVEKLLGMSKEELKELNLEALEDLLGEEVVFYGNVSFRNEELRFNVR
RVNNVDV
>gnl|CDD|237079 PRK12367, PRK12367, short chain dehydrogenase; Provisional
MPQADPMAQSTWQGKRIGITGASGALGKALTKAFRAKGAKVIGLTHSKINNSESNDESPNEWIKWECGKE
ESLDKQLASLDVLILNHGINPGGRQDPENINKALEINALSSWRLLELFEDIALNNNSQIPKEIWVNTSEA
EIQPALSPSYEISKRLIGQLVSLKKNLLDKNERKKLIIRKLILGPFRSELNPIGIMSADFVAKQILDQAN
LGLYLIIVTPNPLTYLLMPLTELGRRLYSRILYKY
>gnl|CDD|171443 PRK12369, PRK12369, putative transporter; Reviewed
MFSSFFASKKWALWAYGGLFFILLSLWYQVSLNVAINEWYGDFYDLLQKAKIEPNNHTAGDFWASILSFL
AIAMPYVLIATVVDYFASHYAFRWREAMTFSYLKFWRNKRDNIEGSSQRIQEDTYRFAKIMESLGLSFLR
AIMTLIAFIPILWGLSDGVSLPFLKDIPGSLVWIALLISLGGLVISWFVGIKLPGLEYNNQKVEAAFRKE
LVYAEDDKKNYAKPETLIELFTGLRFNYFRLFLHYGYFNIWLISFSQMMVIVPYLIMAPGLFAGVITLGV
LMQISNAFSQVRSSFSVFIRNWTTITELRSIYKRLKEFEKNIEYKS
>gnl|CDD|237080 PRK12370, PRK12370, HilA/EilA family virulence transcriptional regulator
MMHFNPVPVSNKKFVFDDFILNMDGSLLRSEKKVNIPPKEYAVLVILLEAAGEIVSKNTLLDQVWGDAEV
NEESLTRCIYALRRILSEDKEHRYIETLYGQGYRFNRPVVVVSPPAPQPTTHTLAILPFQMQDQVQSESL
HYSIVKGLSQYAPFGLSVLPVTITKNCRSVKDILELMDQLRPDYYISGQMIPDGNDNIVQIEIVRVKGYH
LLHQESIKLIEHQPASLLQNKIANLLLRCIPGLRWDTKQISELNSIDSTMVYLRGKHELNQYTPYSLQQA
LKLLTQCVNMSPNSIAPYCALAECYLSMAQMGIFDKQNAMIKAKEHAIKATELDHNNPQALGLLGLINTI
HSEYIVGSLLFKQANLLSPISADIKYYYGWNLFMAGQLEEALQTINECLKLDPTRAAAGITKLWITYYHT
GIDDAIRLGDELRSQHLQDNPILLSMQVMFLSLKGKHELARKLTKEISTQEITGLIAVNLLYAEYCQNSE
RALPTIREFLESEQRIDNNPGLLPLVLVAHGEAIAEKMWNKFKNEDNIWFKRWKQDPRLIKLR
>gnl|CDD|237082 PRK12373, PRK12373, NADH-quinone oxidoreductase subunit E
MLRRLHEDQPDSFAFTPENAAWAEKQITKYPEGRQASAVIPLLMRAQEQEGWVTRAAIEKVADMLDMAYI
RVLEVATFYTQFQLQPVGTRAHIQVCGTTPCMLRGSEALMAVCKSKIHAHPHELNADGTLSWEEVECLGA
CVNAPMVQIGKDYYEDLTPERLEEIIDAFAAGKGPVVKPGPQIGRYASEPAGGLTSLTEEAGKARYNASK
ALAEDIGDTVKRIDGTEVPLLAPWQGDAAPVPPSEAARPKSADAETNAALKTPATAPKAAAKNAKAPEAQ
PVSGTAAAEPAPKEAAKAAAAAAKPALEDKPRPLGIARPGGADDLKLISGVGPKIEATLNELGIFTFDQV
AAWKKAERAWVDGYLNFKGRIERDDWVKQAKALAKGGEAEYIKVFGKKPR
>gnl|CDD|183482 PRK12377, PRK12377, putative replication protein; Provisional
MKNIATGGVLERIRRLAPQGVQPPFRTVDEWREWQLAEGRKRSEEINRQNQQLRVEKILNRSGIQPLHRK
CSFANYQVQNDGQRYALSQAKSIADELMTGCTNFVFSGKPGTGKNHLAAAIGNRLLAKGRSVIVVTVPDV
MSRLHESYDNGQSGEKFLQELCKVDLLVLDEIGIQRETKNEQVVLNQIIDRRTASMRSVGMLTNLNHEAM
STLLGERVMDRMTMNGGRWVNFNWESWRPNVSHLRIVK
>gnl|CDD|237084 PRK12378, PRK12378, YebC/PmpR family DNA-binding transcriptional regulator
MGRAWENIKAKKAKKDGAKSKIFAKLGKEIYVAAKQGGPDPESNPALRFVIERAKKANVPKDVIERAIKK
AKGGGGEDYEEVRYEGFGPNGVMVIVECLTDNVNRTVANVRSAFNKNGGNLGTSGSVAFMFDHKGVFVFE
GDDEDELLEALIDADVDVEDVEEEEGTITVYTDPTDFHKVKKALEAAGIEFLVAELEMIPQNPVELSGED
LEQFEKLLDALEDDDDVQNVYHNVE
>gnl|CDD|183484 PRK12379, PRK12379, propionate kinase
MNEFPVVLVINCGSSSIKFSVLDASDCEVLMSGIADGINSENAFLSVNGGEPAPLAHHSYEGALKAIAFE
LEKRNLNDSVALIGHRIAHGGSIFTESVIITDEVIDNIRRVSPLAPLHNYANLSGIEAAQQLFPGVTQVA
VFDTSFHQTLAPEAYLYGLPWEYYEELGVRRYGFHGTSHRYVSQRAHSLLNLDEDDSGLVVAHLGNGASI
CAVRNGQSVDTSMGMTPLEGLMMGTRSGDVDFGAMAWIASQTGQTLGDLERVVNKESGLLGISGLSSDLR
VLEKAWHEGHERAQLAIKTFVHRIARHIAGHAASLHRLDGIIFTGGIGENSSLIRRLVMEHLAVLGLEID
TEMNNQPNSGGERIISSENSRVICAVIPTNEEKMIALDAIHLGKVN
>gnl|CDD|183485 PRK12380, PRK12380, hydrogenase/urease nickel incorporation protein
MHELSLCQSAVEIIQRQAEQHDVKRVTAVWLEIGALSCVEESAVRFSFEIVCHGTVAQGCDLHIVYKPAQ
AWCWDCSQVVEIHQHDAQCPHCHGERLRVDTGDSLIVKSIEVE
>gnl|CDD|183486 PRK12381, PRK12381, bifunctional succinylornithine transaminase/acetylornithine transaminase; Provisional
MSQPITRENFDEWMVPVYAPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQASK
FWHTGNGYTNEPVLRLAKKLIDATFADRVFFCNSGAEANEAALKLARKYAHDRYGSHKSGIVAFKNAFHG
RTLFTVSAGGQPKYSQDFAPLPPDIRHAAYNDLNSASALIDDQTCAVIVEPIQGEGGVIPADKAFLQGLR
ELCDRHNALLIFDEVQTGVGRTGELYAYMHYGVTPDVLTTAKALGGGFPIGAMLTTEKCASVMTVGTHGT
TYGGNPLASAVAGKVLELINTPEMLNGVKQRHDWFVERLNTINARYGLFSEIRGLGLLIGCVLNAEYAGK
AKQISQEAAKAGVMVLIAGPNVVRFAPALNISEEEITTGLDRFARACERFVSRGSS
>gnl|CDD|183487 PRK12382, PRK12382, putative transporter; Provisional
MTAVSQTETRSSANFSLFRIAFAVFLTYMTVGLPLPVIPLFVHHDLGFGNTMVGIAVGIQFLATVLTRGY
AGRLADQYGAKRSALQGMLACGLAGLAYLLAAILPVSAPFKFALLVVGRLILGFGESQLLTGALTWGLGL
VGPKHSGKVMSWNGMAMYGALAAGAPLGLLLHSHFGFAALALTTMVLPLLAWAFNGTVRKVPAHAGERPS
LWSVVGLIWKPGLGLALQGVGFAVIGTFVSLYFASKGWAMAGFTLTAFGGAFVLMRVLFGWMPDRFGGVK
VAIVSLLVETVGLLLLWLAPTAWVALAGAALTGAGCSLIFPALGVEVVKRVPSQVRGTALGGYAAFQDIA
YGVSGPLAGMLATSFGYPSVFLAGAISAVLGIIVTILSFRRG
>gnl|CDD|237085 PRK12383, PRK12383, putative mutase; Provisional
MARFVVLVIDSFGVGAMKDVTLVRPQDAGANTCGHILSQLPHLQLPTLEKLGLINALGYAPGDMQPSPSA
TWGVAELQHEGADTFMGHQEIMGTRPLPPLRMPFSDVIDRVEQALESAGYQVERRGDGLQFLLVNQAVAI
GDNLEADLGQVYNVTANLSVISFDDALKIGRIVREQVQVGRVIVFGGLLTDSQRILDAAESKEGRFIGIN
APKSGVYDNGYQVVHLGYGVDPKVQVPQKLYEAGVPVVLVGKVADIVNNPYGVSWQNLVDTQRVMDITLD
EFNTHPTAFICTNIQETDLAGHAEDVARYAERLEVVDRNLARLLEAMTPDDCLVVMADHGNDPTIGHSHH
TREVVPLLVYQKGLQATQLGVRTTLSDVGATVCEFFGAPPPQNGRSFLSSLRFAGD
>gnl|CDD|183489 PRK12384, PRK12384, sorbitol-6-phosphate dehydrogenase; Provisional
MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGMAYGFGADATSEQSVLA
LSRGVDEIFGRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGIQGRIIQIN
SKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEYGITVHSLMLGNLLKSPMFQSLLPQYAKKLGIKPDE
VEQYYIDKVPLKRGCDYQDVLNMLLFYASPKASYCTGQSINVTGGQVMF
>gnl|CDD|183490 PRK12385, PRK12385, succinate dehydrogenase/fumarate reductase iron-sulfur subunit
MAEMKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMV
NNVPKLACKTFLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQM
AKYHQFSGCINCGLCYAACPQFGLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGY
CSEVCPKHVDPAAAIQQGKVESAKDFLIAMLKPR
>gnl|CDD|237086 PRK12386, PRK12386, fumarate reductase iron-sulfur subunit; Provisional
MGYTAKFRVWRGDASGGELQDYTVEVNEGEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPR
LMCMTRMSTFDEDETVTVTPMRTFPVIRDLVTDVSFNYEKAREIPSFTPPKDLQPGEYRMQQVDVERSQE
FRKCIECFLCQNVCHVVRDHEENKPAFAGPRFLMRIAELEMHPLDTADRRAEAQEEHGLGYCNITKCCTE
VCPEHIKITDNALIPMKERVVDRKYDPLVWLGSKLFRRRKD
>gnl|CDD|183492 PRK12387, PRK12387, formate hydrogenlyase complex iron-sulfur subunit; Provisional
MFKLIKKVIKTGTATSSYPLEPIAVDKNFRGKPEYNPQQCIGCAACVNACPSNALTVETDLATGELAWEF
NLGRCIFCGRCEEVCPTAAIKLSQEFELAVWKKEDLLQQSEFALCNCRVCGRPFAVQKEIDYAIALLKHN
GDSRAENHRESFETCPECKRQKCLVPSDRIELTRHMKEAI
>gnl|CDD|171459 PRK12388, PRK12388, class II fructose-bisphosphatase
MMSLAWPLFRVTEQAALAAWPQTGCGDKNKIDGLAVTAMRQALNDVAFRGRVVIGEGEIDHAPMLWIGEE
VGKGDGPEVDIAVDPIEGTRMVAMGQSNALAVMAFAPRDSLLHAPDMYMKKLVVNRLAAGAIDLSLPLAD
NLRNVARALGKPLDKLRMVTLDKPRLSAAIEEATQLGVKVFALPDGDVAASVLTCWQDNPYDVMYTIGGA
PEGVISACAVKALGGDMQAELIDFCQAKGDYTENRQIAEQERKRCKAMGVDVNRVYSLDELVRGNDILFS
ATGVTGGELVNGIQQTANGVRTQTLLIGGADQTCNIIDSLH
>gnl|CDD|183493 PRK12389, PRK12389, glutamate-1-semialdehyde aminotransferase; Provisional
MNFTKSEALHQEALEHIVGGVNSPSRSYKAVGGGAPVVMERGKGAYFYDVDGNKYIDYLAAYGPIITGHA
HPHITKAITEAAENGVLYGTPTELEIEFAKMLKEAIPSLEKVRFVNSGTEAVMTTIRVARAYTGRTKIIK
FAGCYHGHSDLVLVAAGSGPSTLGTPDSAGVPKSIAQEVITVPFNDIEALKEALDKWGDEVAAVLVEPIV
GNFGIVEPKPGFLEAVNELAHEAGALVIYDEVITAFRFMYGGAQDLLGVEPDLTALGKIIGGGLPIGAYG
GRKDIMEQVAPLGPAYQAGTMAGNPASMAAGIACLEVLQQEGVYEKLDRLGAMLEEGILEAAEKHGITIT
INRLKGALTVYFTDEKVTNYDQAERSDGEAFGKFFKLMLNQGINLAPSKYEAWFLTTAHTEEDIEETLEA
VDRAFAQL
>gnl|CDD|183494 PRK12390, PRK12390, 1-aminocyclopropane-1-carboxylate deaminase; Provisional
MNLQKFPRYPLTFGPTPIHPLKRLSAHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLVPDALAQGADTL
VSIGGVQSNHTRQVAAVAAHLGMKCVLVQENWVNYEDAVYDRVGNILLSRIMGADVRLVPDGFDIGIRKS
WEDALEDVRAAGGKPYAIPAGASDHPLGGLGFVGFAEEVRAQEAELGFKFDYIVVCSVTGSTQAGMVVGF
AADGRARRVIGIDASAKPEQTRAQVLRIARNTAELVELGRDITEDDVVLDERYAGPEYGLPNEGTLEAIR
LCARLEGMLTDPVYEGKSMHGMIDLVRKGEFPEGSKVLYAHLGGVPALNAYSFLFRN
>gnl|CDD|237087 PRK12391, PRK12391, TrpB-like pyridoxal phosphate-dependent enzyme
QTKILLDEDEIPTQWYNILADLPEPLPPPLDPGTGEPVTPEDLAPIFPMELIEQEVSTERYIDIPEEVRE
IYRLWRPTPLIRARRLEKALGTPAKIYYKYEGVSPTGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGS
ALALACALFGLECTVFMVRVSYEQKPYRRSLMETYGAEVIPSPSDLTEAGRKILAEDPDHPGSLGIAISE
AVEDAAKRPDTKYALGSVLNHVLLHQTVIGLEAKKQLELAGEYPDVVIGCVGGGSNFAGLAFPFLGDKLE
GKKDTRFIAVEPAACPTLTKGEYAYDFGDTAGLTPLLKMYTLGHDFVPPPIHAGGLRYHGMAPLVSLLVH
EGLIEARAYPQTEVFEAAVLFARTEGIVPAPESSHAIAAAIDEALKAKEEGEEKVILFNLSGHGLLDLAA
YDAYLAG
>gnl|CDD|171463 PRK12392, PRK12392, bacteriochlorophyll c synthase; Provisional
TAVARLGFVDKIRAHLELLDPVTWISVFPCLAGGVMASGAMQPTLHDYLLLLALFLMYGPLGTGFSQSVN
DYFDLELDRVNEPTRPIPSGRLSEKEALWNSIIVLLLAIGLGVWLGLHIGGERGMVIISSILAGLFVAYI
YSAPPLKLKKNILTSAPAVGFSYGFITFLSANALFSDIRPEVVWLAGLNFFMAIALIIMNDFKSVEGDKE
GGLKSLTVMIGAKNTFLVSFIIIDLVFAVFAWLAWSWGFTVLMYFILVGLVLNIVIQIQLYRDPKGGISF
MQGAVDDGFGNAIGKSDVQEHNAFLRFQVANNILFLINNLIAAGMIGMKYM
>gnl|CDD|237088 PRK12393, PRK12393, amidohydrolase; Provisional
MPSLLIRNAAAIMTGLPGDAARLGGPDIRIRDGRIAAIGALTPLPGERVIDATDCVVYPGWVNTHHHLFQ
SLLKGVPAGINQSLTAWLAAVPYRFRARFDEDLFRLAARIGLVELLRSGCTTVADHHYLYHPGMPFDTGD
ILFDEAEALGMRFVLCRGGATQTRGDHPGLPTALRPETLDQMLADVERLVSRYHDASPDSLRRVVVAPTT
PTFSLPPELLREVARAARGMGLRLHSHLSETVDYVDFCREKYGMTPVQFVAEHDWLGPDVWFAHLVKLDA
EEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDGAASNESADMLSEAHAAWLLHRAEG
GADATTVEDVVHWGTAGGARVLGLDAIGTLAVGQAADLAIYDLDDPRFFGLHDPAIAPVACGGPAPVKAL
LVNGRPVVENGAIPGLDLAELRHDARAAVRRLLQRAA
>gnl|CDD|183497 PRK12394, PRK12394, metallo-dependent hydrolase
MKNDILITNGHIIDPARNINEINNLRIINDIIVDADKYPVASETRIIHADGCIVTPGLIDYHAHVFYDGT
EGGVRPDMYMPPNGVTTVVDAGSAGTANFDAFYRTVICASKVRIKAFLTVSPPGQTWSGYQENYDPDNID
ENKIHALFRQYRNVLQGLKLRVQTEDIAEYGLKPLTETLRIANDLRCPVAVHSTHPVLPMKELVSLLRRG
DIIAHAFHGKGSTILTEEGAVLAEVRQARERGVIFDAANGRSHFDMNVARRAIANGFLPDIISSDLSTIT
KLAWPVYSLPWVLSKYLALGMALEDVINACTHTPAVLMGMAAEIGTLAPGAFADIAIFKLKNRHVEFADI
HGETLTGTHVLVPQMTIKSGEILYRQIDF
>gnl|CDD|183498 PRK12395, PRK12395, maltoporin; Provisional
MKTSLRTLSVALAAALVSPSVLAIEKIDFHGYMRAGVGVSSDGGLAEWQKTMVGRLGNESDTYGEIGLGA
EVYKKEDVSFYLDSMVSMLSDGSNDSETTIGDDAQFGLRQLNLQIKGLIPGDKEAVIWGGKRYYQRHDLH
IIDTKYWNISGSGAGIENYTVGPGAVSVAWVRGDANDVDTRITGDSDVNINYIDVRYAGFKPWAGSWTEV
GIDYAMPNPTKQQKEYGGLYDADNAVMLTGEISQDMFGGYNKLVLQYANKGLAQNMISQGGGWYDMWHKT
DEAKGYRVINTGLIPITDKFSFNHVLTWGSANDITEYTDKTNLISLVGRAQYQFTQYVRAIGEVGGFYQK
DTYHNGSNYKQGGEKYTIALGLAEGPDFLSRPELRVFASYLNDSENGKPFEDGTSNDTWNFGVQVEAWW
>gnl|CDD|183500 PRK12397, PRK12397, acetate/propionate family kinase
MSYKIMAINAGSSSLKFQLLEMPQGDMLCQGLIERIGMADAQVTIKTHSQKWQETVPVADHRDAVTLLLE
KLLGYQIINSLRDIDGVGHRVAHGGEFFKDSTLVTDETLAQIERLAELAPLHNPVNALGIHVFRQLLPDA
PSVAVFDTAFHQTLDEPAYIYPLPWRYYAELGIRRYGFHGTSHKYVSGVLAEKLGVPLSALRVICCHLGN
GSSICAIKNGRSVNTSMGFTPQSGVMMGTRSGDIDPSILPWIAQREGKTPQQLNQLLNNESGLLGVSGVS
SDYRDVEQAANTGNRQAKLALTLFAERIRATIGSYIMQMGGLDALVFTGGIGENSARARSAVCHNLQFLG
LAVDEEKNQRNATFIQTENALVKVAVINTNEELMIAQDVMRIALPATEGLCVPA
>gnl|CDD|237089 PRK12398, PRK12398, pyruvoyl-dependent arginine decarboxylase; Provisional
KLIPKKVFFTSGVGRHEEMLESFELALRDAGIEKFNLVTVSSILPPNCEIVSREEGLKELSPGEIVFCVM
SRNSSNEPGRTIFASVGCAIPEDQSLNGYLSEYHGYGETEEDAGKYAEKLAREMLSTWTNEEPLRTFNIT
RSAEVDEDGNWTTVVAAAVFII
>gnl|CDD|183502 PRK12399, PRK12399, tagatose 1,6-diphosphate aldolase; Reviewed
LTEQKRKSLEKLSNENGIISALAFDQRGALKRMMAQHQTEEPTVAQIEELKVLVSEELTPYASSILLDPE
YGLPASKARDEDAGLLLAYEKTGYDATTTGRLPDCLDDWSAKRIKEEGADAVKFLLYYDVDEPDEINEQK
KAYIERIGSECVAEDIPFFLEILTYDEKIADNGSVEYAKVKPHKVNEAMKVFSKPRFGVDVLKVEVPVNM
KYVEGFAEGEVVYTKEEAAQHFKEQDAATHLPYIYLSAGVSAELFQETLVFAHEAGAKFNGVLCGRATWA
GSVKVYIEQGEAAAREWLRTEGFENIDELNKVLDKTATSWKEKV
>gnl|CDD|171470 PRK12400, PRK12400, D-amino acid aminotransferase; Reviewed
MAYERFVLWNDAVIDTTKQKTYIELEERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPF
SKAELITLLYKLIENNNFHEDGTIYLQVSRGVQARTHTFSYDVPPTIYAYITKKERPALWIEYGVRAISE
PDTRWLRCDIKSLNLLPNILAATKAERKGCKEALFVRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGI
IRQYVLSLAKTLRIPVQEELFSVRDVYQADECFFTGTTIEILPMTHLDGTAIQDGQVGPITKMLQRSFSQ
SLLQSNMSSS
>gnl|CDD|237090 PRK12402, PRK12402, replication factor C small subunit 2; Reviewed
DAPLWTEKYRPALLEDILGQDEVVERLSRAVDSPNLPHLLVQGPPGSGKTAAVRALARELYGDPWENNFT
EFNVADFFDQGKKYLVEDPRFAHFLGTDKRIRSSKIDNFKHVLKEYASYRPLSADYKTILLDNAEALRED
AQQALRRIMEQYSRTCRFIIATRQPSKLIPPIRSRCLPLFFRAPTDDELVDVLESIAEAEGVDYDDDGLE
LIAYYAGGDLRKAILTLQTAALAAGEITMEAAYEALGDVGTDEVIESLLDAAEAGDFTDARKTLDDLLID
EGLSGGEVLEELLRVARSRYRGDNLARLHRLAADADARLTDGANDRIQLEALLAELG
>gnl|CDD|171472 PRK12403, PRK12403, aspartate aminotransferase family protein
MNAPFAPQRDTRDYQAADAAHHIHAFLDQKALNAEGPRVMVRGEGLHLWDNDGKRYLDGMSGLWCTNLGY
GRKDLAAAAARQMEQLPYYNMFFHTTHPAVIELSELLFSLLPGHYSHAIYTNSGSEANEVLIRTVRRYWQ
VLGKPQKKIMIGRWNGYHGSTLAATALGGMKFMHEMGGLIPDVAHIDEPYWYANGGELTPAEFGRRAALQ
LEEKILELGAENVAGFVAEPFQGAGGMIFPPESYWPEIQRICRQYDVLLCADEVIGGFGRTGEWFAHEHF
GFEPDTLSIAKGLTSGYVPMGGLVLSKRIAEALVEQGGVFAHGLTYSGHPVAAAVAIANLKALRDEGVVT
RVKDDTGPYLQRCLREVFGDHPLVGEVQGAGLVAALQFAEDKATRKRFANENDLAWRCRTIGFEEGVIIR
STLGRMIMAPALVAGRAEIDELVDKTRIAVDRTAREVGVL
>gnl|CDD|183504 PRK12404, PRK12404, stage V sporulation protein AD; Provisional
MLQGHQTWVFENKPVIISTGVVGGPFEAKGPLAEDFDLLHEDLWLGQDSYEKAERKLLEEACSRAIEKAK
LRKEDIQFFLAGDLMNQITPTSFAARTLGIPYLGLFGACSTSMEGLALAALIVNSGGAKYVLTGASSHNA
AVEKQFRYPTEYGGQKPPTAQWTVTGAGAAILSKTGDGPRVTSATIGRVVDMGLTDPFNMGGAMAPAAVD
TIEAHLRDRQIDASYYDLIVTGDLGHVGREIAKDLLHKHGVKVPEEQFQDCGLLIYREGQPVIAGASGPG
CSATVTYGHLLNRMKRGELKRILVVATGALLSPLSFQQGETIPCIAHAVSIEMG
>gnl|CDD|237091 PRK12405, PRK12405, electron transport complex RsxE subunit; Provisional
MSEYKEIFKNGLWKNNPALVQLLGLCPLLAVTTTATNALGLGLATTLVLVCSNLTVSLLRKWIPKEIRIP
IFVMIIASFVTVVQLLMNAYAYGLYQSLGIFIPLIVTNCIILGRAEAFASKNGVLLSALDGLGMGLGFTL
ALVVLGAIREILGNGTLFDGADLLLGPWAKVLRIEVFHTDSPFLLAILPPGAFIGLGLLLALKNLIDKRK
KKRKAKAAAEPALPAGETGKV
>gnl|CDD|183506 PRK12406, PRK12406, long-chain-fatty-acid--CoA ligase; Provisional
MYATIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHF
KPEEIAYILEDSGARVLIAHADLLHGLASALPAGVTVLSVPTPPEIAAAYRISPALLTPPAGAIDWEGWL
AQQEPYDGPPVPQPQSMIYTSGTTGHPKGVRRAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAP
NAYGLRAGRLGGVLVLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAA
APCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEI
GEIYSRIAGNPDFTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAV
LHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSG
KIFKRRLRDPYWANAGRKI
>gnl|CDD|183507 PRK12407, flgH, flagellar basal body L-ring protein FlgH
MKRFLILTALLLALCGCESPALLVQKDDAEFAPPANLIQPATVTEGGGLFQPGYNWSLLQDRRAYRVGDI
LTVILDESTQSSKQAKTNFGKKNDVSLGVPEVLGKKLDKLGGSISGKRDFDGSATSAQQNMLRGSITVAV
HQVLPNGVLVIRGEKWLTLNQGDEYMRVTGLVRADDIARDNSVSSQRIANARISYAGRGALSDANSAGWL
TRFFNHPLFPI
>gnl|CDD|237092 PRK12408, PRK12408, glucokinase; Provisional
SSASSPSAAVAVPRPESFVAADVGGTHVRVALVCASPDAAKPVELLDYRTYRCADYPSLAAILADFLAEC
APVRRGVIASAGYALDDGRVITANLPWTLSPEQIRAQLGLQAVHLVNDFEAVAYAAPYMEGNQVLQLSGP
AQAAAGPALVLGPGTGLGAALWIPNGGRPVVLPTEAGQAALAAASELEMQLLQHLLRTRTHVPIEHVLSG
PGLLNLYRALCALRGATPVHASPAAITAAALAGDDALAHEALQVFCGFLGSVVGDMALAYGARGGVYLAG
GILPQIADFLARSDFVERFLNKGPMRPALEQVPVKLVEHGQLGVLGAASWYLQHQR
>gnl|CDD|237093 PRK12409, PRK12409, D-amino acid dehydrogenase small subunit; Provisional
MSHIAVIGAGITGVTTAYALAQRGYQVTVFDRHRYAAMETSFANGGQLSASNAEVWNHWATVLKGLKWML
RKDAPLLLNPKPSWHKYSWLAEFLAHIPNYRANTIETVRLAIAARKHLFDIAEREGIDFDLERRGILHIY
HDKAGFDHAKRVNALLAEGGLERRAVTPEEMRAIEPTLTGEYYGGYYTPSDSTGDIHKFTTGLAAACARL
GVQFRYGQEVTSIKTDGGGVVLTVQPSAEHPSRTLEFDGVVVCAGVGSRALAAMLGDRVNVYPVKGYSIT
VNLDDEASRAAAPWVSLLDDSAKIVTSRLGADRFRVAGTAEFNGYNRDIRADRIRPLVDWVRRNFPDVST
RRVVPWAGLRPMMPNMMPRVGRGRRPGVFYNTGHGHLGWTLSAATADLVAQVVAQKLPAP
>gnl|CDD|183511 PRK12411, PRK12411, cytidine deaminase; Provisional
MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEF
VAIAIVADTKRPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDLHE
>gnl|CDD|183512 PRK12412, PRK12412, bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase
LNKALTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDPHNGWAHNVFPIPASTLKPQLETTIEG
VGVDALKTGMLGSVEIIEMVAETIEKHNFKNVVVDPVMVCKGADEALHPETNDCLRDVLVPKALVVTPNL
FEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSKLGTETAIDVLYDGETFDLLESEKIDTTNTHG
AGCTYSAAITAELAKGKPVKEAVKTAKEFITAAIRYSFKINEYVGPTHHGAYRKFVVS
>gnl|CDD|183513 PRK12413, PRK12413, bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase
MKTNYILAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAMTEKGFEVFPVDKEIFQQQLDSLKDVP
FSAIKIGLLPNVEIAEQALDFIKGHPGIPVVLDPVLVCKETHDVEVSELRQELIQFFPYVTVITPNLVEA
ELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNRLSQKKAIDLFYDGKEFVILESPVLEKNNIGAGCT
FASSIASQLVKGKSPLEAVKNSKDFVYQAIQQSDQYGVVQYYA
>gnl|CDD|183514 PRK12414, PRK12414, putative aminotransferase; Provisional
MQSATAPRSKLPDVGTTIFTVIGQLAAQHDALNLSQGAPNFAPDPALVEGVARAMRDGHNQYAPMAGIAA
LREALAEKTERLYGARYDPASEVTVIASASEGLYAAISALVHPGDEVIYFEPSFDSYAPIVRLQGATPVA
IKLSPEDFRVNWDEVAAAITPRTRMIIVNTPHNPSATVFSAADLARLAQLTRNTDIVILSDEVYEHVVFD
GARHHSMARHRELAERSVIVSSFGKSYHVTGWRVGYCLAPAELMDEIRKVHQFMVFSADTPMQHAFAEAL
AEPASYLGLGAFYQRKRDLLARELAGSRFELLPSEGSFFMLARFRHFSDESDSDFVLRLIRDARVATIPL
SAFYTDGTDTGLIRLSFSKDDATLVEGARRLCSL
>gnl|CDD|183515 PRK12415, PRK12415, fructose-bisphosphatase class II
MERELALEIVRVTEAAALASAQWMGRGKKNEADDAATTAMRDMFDSVNMAGTVVIGEGELDEAPMLYIGE
ELGTGNGPEVDIAVDPLEGTNIVAKGLANAMAVIAIADKGNLLHAPDMYMEKIAVGPKAAGKISLDDPIE
KTIEIVAEANNKKIRDLTVIVQERERHQDIIDRVRAKGARVKLFGDGDVGASIATALPGTGIDLFVGIGG
APEGVISAAALKCLGGEMQARLVPMNEEEEARCREMGLEDPRQLLMLDDLVSGDDAIFSATGVSAGELLD
GVKFLGGDLAETYSIVMRYKTRTVRFIKTHHHLDHKPHLNLD
>gnl|CDD|183516 PRK12416, PRK12416, protoporphyrinogen oxidase; Provisional
MKTVVVIGGGITGLSTMFYLEKLKKDYNIDLNLILVEKEEYLGGKIHSVEEKDFIMESGADSIVARNEHV
MPLVKDLNLEEEMVYNETGISYIYSDNTLHPIPSDTIFGIPMSVESLFSSTLVSTKGKIVALKDFITKNK
EFTKDTSLALFLESFLGKELVERQIAPVLSGVYSGKLNELTMASTLPYLLDYKNKYGSIIKGFEENKKQF
QSAGNKKFVSFKGGLSTIIDRLEEVLTETVVKKGAVTTAVSKQGDRYEISFANHESIQADYVVLAAPHDI
AETLLQSNELNEQFHTFKNSSLISIYLGFDILDEQLPADGTGFIVTENSDLHCDACTWTSRKWKHTSGKQ
KLLVRMFYKSTNPVYETIKNYSEEELVRVALYDIEKSLGIKGEPEVVEVTNWKDLMPKYHLEHNQAVQSL
QEKMMNLYPNIYLAGASYYGVGIGACIGNGKNTANEIIATLNE
>gnl|CDD|237095 PRK12417, secY, preprotein translocase subunit SecY; Reviewed
MKLLKKFEYKIIYKKILFTCFILFIYILGSNISIPFVSYNDMLGGHESFLKIAAANTGGDLRTLNIFSLG
LGPWMTSMIILQLFSYRKRDGLMKQTIEEQHYRERILTLIIAVIQSLAVILSLPSKERISQTNILLNTLI
LVTGTMFLVWLSDLNARYGIGGPMPIVLVSMIKSIPQDVIEYIDASHIVIILLILLVIITLFFLYFIELV
EYRIPYNDIMNHNRFKMYSYLSIKLNPAGGMPIMYSMSLLVFPQYIIILILSIFPNNSGISADMDMLSFG
SPLGVTVYLILQFLLSYFFSFVNINTKQIAKDMLKSGNYIPGVYPGKDTERYLNYIARRFSWFGALFVTV
IAGIPLYFTLFDPHLSTEIYFSGQFMMFVGMSFNIADEIRALLYFDKYKPLLNQ
>gnl|CDD|183518 PRK12418, PRK12418, cysteinyl-tRNA synthetase; Provisional
VRPVAPGGTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGV
DWRDLAEREIALFREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVVDDEEYPDVYFSVDATP
QFGYESGYDRATMLELFAERGGDPDRPGKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNR
LGSGFDIQGGGSDLIFPHHEFSAAHAEAATGERRFARHYVHAGMIGLDGEKMSKSRGNLVFVSRLRAAGV
DPAAIRLALLAGHYRADREWTDAVLAEAEARLARWRAAAALPAGPDAADVVARVRAALADDLDTPGALAA
VDGWATDALEGGGDDAAAPALVATAVDALLGVAL
>gnl|CDD|237096 PRK12419, PRK12419, 6,7-dimethyl-8-ribityllumazine synthase
MNSSPRFATPQRIAFIQARWHADIVDQARKGFVAEIAARGGAASQVDIFDVPGAFEIPLHAQTLAKTGRY
AAIVAAALVVDGGIYRHEFVAQAVIDGLMRVQLDTEVPVFSVVLTPHHFHESEEHHDFFRAHFVVKGAEA
AHACADTLLSRERLRAQV
>gnl|CDD|237097 PRK12420, PRK12420, histidyl-tRNA synthetase; Provisional
MMEMRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGGGDEILKEIYTLTD
QGKRDLALRYDLTIPFAKVVAMNPNIRLPFKRYEIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAE
LMSMAFELFRRLNLEVTIQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKDLLERGISEE
MADTICNTVLSCLQLSIADFKEAFNNPLVAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVY
EIFLKDGSITSSIGSGGRYDNIIGAFRGDDMNYPTVGISFGLDVIYTALSQKETISSTADVFIIPLGTEL
QCLQIAQQLRSTTGLKVELELAGRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKVPLS
SLS
>gnl|CDD|237098 PRK12421, PRK12421, ATP phosphoribosyltransferase regulatory subunit; Provisional
MPISERWLLPDGVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLQTFKLI
DQLSGRLMGVRADITPQVARIDAHLLNREGVARLCYAGSVLHTLPQGLFGSRTPLQLGAELYGHAGIEAD
LEIIRLMLGLLRNAGVPALHLDLGHVGIFRRLAELAGLSPEEEEELFDLLQRKALPELAEVCQNLGVGSD
LRRMFYALARLNGGLEALDRALSVLALQDAAIRQALDELKTLAAHLKNRWPELPVSIDLAELRGYHYHTG
LVFAAYIPGRGQALARGGRYDGIGEAFGRARPATGFSMDLKELLALQFLEEEAGAILAPWGDDPDLLAAI
AELRQQGERVVQLLPGDDGSSEPGCDHRLVLQDGQWQIEAIQ
>gnl|CDD|183521 PRK12422, PRK12422, chromosomal replication initiator protein DnaA
MRAWEEFLLLQEKEIGTETVDKWLRSLKVLCFDACNLYLEAKDSFQVTWFEEHIRHKVKASLVNNNGKPI
RVHVTSLDKSTPFKKEKQIQQEKTAYFTMKYGELDPLMTFANFLVTPENDLPHRILQEFTKVSEQGKGFP
FNPIYLFGPEGSGKTHLMQAAVHALRESGGKILYVRSELFTEHLVSAIRSGEMQRFRQFYRNVDALFIED
IEVFSGKGATQEEFFHTFNSLHTEGKLIVISSTCAPQDLKAMEERLISRFEWGIAIPLHPLTKEGLRSFL
ERKAEALSIRIEETALDFLIEALSSNVKSLLHALTLLAKRVAYKKLSHQLLYVDDIKALLHDVLEAAESV
RLTPSKIIRAVAQYYGVSPESILGRSQSREYVLPRQVAMYLCRQKLSLSYVKIGDVFSRDHSTVISSIRA
ISQKLEEDDRDISMAIQEITKRLSS
>gnl|CDD|171490 PRK12425, PRK12425, class II fumarate hydratase
MSRTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARL
IEQAADEVLDGQHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSND
CFPTAMHIAAAQAVHEQLLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAE
RAIRAALPAVCELAQGGTAVGTGLNAPHGFAEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALK
TLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGKVNPTQCEALSMLACQVMGNDATIGFAAS
QGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLERGLMLVTALNPHIGYDKAA
EIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEAGGHG
>gnl|CDD|183522 PRK12426, PRK12426, elongation factor P; Provisional
MVLSSQLSVGMFISTKDGLYKVVSVSKVTGPKGETFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNL
EYLYLEGDEYLFLDLGNYDKIYIPKEIMKDNFLFLKAGVTVSALVYDGTVFSVELPHFLELMVSKTDFPG
DSLSLSGGAKKALLETGVEVLVPPFVEIGDVIKVDTRTCEYIQRV
>gnl|CDD|183523 PRK12427, PRK12427, FliA/WhiG family RNA polymerase sigma factor
MENREFEACLTLTPQEEGKYLNAYLPLVKKVVRQLAFQADSVIDREDMEQIALMGLLEALRRYGHPDEQF
AAYAVHRIRGAILDELRELDWRPRRLRQKTHKTNDAIREIAKRLGHEPNFEEISAELNLTAEEYQEYLLL
ENAGTLESLDELLALEAHNDILQSRDLEENIIIEDNLKQALSQLDEREQLILHLYYQHEMSLKEIALVLD
LTEARICQLNKKIAQKIKSFF
>gnl|CDD|237099 PRK12428, PRK12428, coniferyl-alcohol dehydrogenase
TARLLRFLGARVIGVDRREPGMTLDGFIQADLGDPASIDAAVAALPGRIDALFNIAGVPGTAPVELVARV
NFLGLRHLTEALLPRMAPGGAIVNVASLAGAEWPQRLELHKALAATASFDEGAAWLAAHPVALATGYQLS
KEALILWTMRQAQPWFGARGIRVNCVAPGPVFTPILGDFRSMLGQERVDSDAKRMGRPATADEQAAVLVF
LCSDAARWINGVNLPVDGGLAATYIAAVLGF
>gnl|CDD|237100 PRK12429, PRK12429, 3-hydroxybutyrate dehydrogenase; Provisional
MLKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINA
GIDYAVETFGGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMAS
VHGLVGSAGKAAYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPLVRKQIPDLAKERGISEEEVL
EDVLLPLVPQKRFTTVEEIADYALFLASFAAKGVTGQAWVVDGGWTAQ
>gnl|CDD|237101 PRK12430, PRK12430, putative bifunctional flagellar biosynthesis protein FliO/FliP; Provisional
MKNNLFFQSISNSLHPIFNDEKFLQIMSSLFEIILLILILSWILKKISLFKINKIISRMKIIERLSLGSN
ESIIIVEIKQLRLVLGVTKKNISHLYTLPSNSKDEVIKKTNDTLLQKNNFNRSLKNFSKTSWKKTMFYRI
IPLVFLLLFCPSAYADIPGLTSHILDDGSQTWSVPVQTLVFLTSLTFLPAFLLMMTSFTRIVIVFGLLRN
ALGTPYAPPNQILLGLALFLTFFIMSPTFDKIYKDAYLPFSQEKINMDDAILKGAMPLKKFMLNQTRTPD
LELFSKLAHISSYKNKNEIPMRILLPSFITSELKTAFQIGFTIFIPFLIIDLVVASVLMALGMMMVPPST
ISLPFKLMLFVLVDGWQLLITSLAHSFNT
>gnl|CDD|183526 PRK12435, PRK12435, ferrochelatase; Provisional
MKKKIGLLVMAYGTPYKEEDIERYYTHIRHGRKPSEEMLQDLKDRYEAIGGISPLAKITDEQAKALEKAL
NEVQDEVEFKLYLGLKHIEPFIEDAVEQMHNDGIEEAISIVLAPHYSTFSVKSYNKRAKEEAEKLGGPTI
TSIESWYDEPKFIQYWADQIKETFAQIPEEEREKAVLIVSAHSLPEKIIAAGDPYPDQLEETADLIAEQA
NVEHYAIGWQSEGNTPDPWLGPDVQDLTRDLYEEHGYKSFIYTPVGFVAEHLEVLYDNDYECKVVTDEIG
AKYYRPEMPNADPLFIDALADVVLKKLKSVV
>gnl|CDD|171497 PRK12436, PRK12436, UDP-N-acetylmuramate dehydrogenase
MNMQEVYEYLSTVLPEGHVKQDEMLKNHTHIKVGGKADVFVAPTNYDEIQEVIKYANKYNIPVTFLGNGS
NVIIKDGGIRGITVSLIHITGVTVTGTTIVAQCGAAIIDVSRIALDHNLTGLEFACGIPGSVGGALYMNA
GAYGGEISFVLTEAVVMTGDGELRTLTKEAFEFGYRKSVFANNHYIILEARFELEEGVYEEIKAKMDDLT
FKRESKQPLEYPSCGSVFKRPPNNFAGKLIQESGLQGKRIGGVEVSLKHAGFMVNVDNGTAQDYIDLIHF
VQKTVEEKFGVKLEREVRIIGEDKE
>gnl|CDD|183527 PRK12437, PRK12437, prolipoprotein diacylglyceryl transferase; Reviewed
LLTIPQLDPVALQLGPIPVHWYGIIIGLGVLLGLWLATREGKRRGITKDTFSDLVLIAVPIAILGARIYY
VLFEWDYYAQNPSQIFNIWQGGLAIHGGLIGAVLTGIIFAKKKKISFWKLADIAAPSIPLGQAIGRWGNF
INQEAHGRPVTRPFLEGLHLPDFIINQMYIDGVYYHPTFLYESLWNFLGFILLLWLRKKPLRRGEVFALY
LIWYSIGRFFIEGLRTDSLMLFGWLRIAQVISIPLIIIGIILIIYRRKKGIADWRYQEN
>gnl|CDD|171499 PRK12438, PRK12438, hypothetical protein; Provisional
MEMGPPGKRPVLPKRARLLVTAGMGMLALLLFGPRLVDIYTDWLWFGEVGFRSVWITVLLTRLALFAAVA
LVVGGIVLAALLLAYRSRPFFVPDEPQRDPVARYRSAVMRRPRLFGWGIAVTLGVVCGLIAQFDWVTVQL
FVHGGTFGIVDPEFGYDIGFYVFDLPFYRSVLNWLFVAVVLAFLASLLTHYLFGGLRLTTGRGMLTQAAR
VQLAVFAGAFVLLKAVAYWLDRYELLSSGRKEPTFTGAGYTDINAVLPAKLILVAIAVLCAVAFFAAIFL
RDLRIPAMAAALLVLSAILVGGLWPLLMEQFSVRPNAADVESPYIERNIEATRQAYGIGGDWVQYRDYPG
IGTKQPRDVPVDVTTIANVRLLDPHILSRTFTQQQQLKNFYGFPEILDIDRYRIDGELQDYIVAARELSP
KSLTGNQTDWINKHTVYTHGNGFVAAPANRVNAAARDAENISDSNSGYPIYAVSDIASLGSGRQVIPVEQ
PRVYYGEVIAQADPDYAIVGGAPGSAPREYDTDTSKYTYTGAGGVSIGNWFNRLAFAAKYAERNILFSRA
IGSESKIIIHRDPKERVQRVAPWLTTDDNPYPAVVNGRIVWIVDAYTTLDTYPYAQRSSLEGPVTSPTGR
VRQRKEVSYVRNSVKATVDAYDGTVTLYQVDRDDPVLRAWMRVFPGTVKPEDQIPDELRAHFRYPEDLFE
VQRSLLAKYHVDEPREFFTTNAFWSVPSDPTNDANATQPPYYVLVGDQQTAQPSFRLTSAMVGYNREFLS
AYISAHSDPANYGKLTVLELPTDTQTQGPQQIQNSMISDTRVASERTLLERSNRIHYGNLLTLPIADGGI
LYVEPLYTERISTSPSSSTFPQLSRVLVSVREPRTEGGVRVGYAPTLAEALDQVFGPGTGRVATAPGGDA
ASAPPPGAGPPAPPQAVPPPRTTQPPAAPPRGPDVPPAAVAELRETLADLRSAQRSGDFTAYGAALDRLE
KAIDAYETPGG
>gnl|CDD|171500 PRK12439, PRK12439, NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
MAAAKREPKVVVLGGGSWGTTVASICARRGPTLQWVRSAETADDINDNHRNSRYLGNDVVLSDTLRATTD
FAEAANCADVVVMGVPSHGFRGVLTELAKELRPWVPVVSLVKGLEQGTNMRMSQIIEEVLPGHPAGILAG
PNIAREVAEGYAAAAVLAMPDQHLATRLSPLFRTRRFRVYTTDDVVGVEMAGALKNVFAIAVGMGYSLGI
GENTRAMVIARALREMTKLGVAMGGNPETFAGLAGMGDLIVTCTSQRSRNRHVGEQLGAGKPIDEIIASM
NQVAEGVKAASVVMEFADEYGLNMPIAREVDAVINHGSTVEQAYRGLIAEVPGHEVHGSGF
>gnl|CDD|183528 PRK12440, PRK12440, acetate/propionate family kinase
MSNSYVLVINSGSSSLKFAVIDSVTGEAVLSGLGECFGLEDARMSWKYQGEKTEIAIEGEDNHHKIAIGR
LVGLTEELGFTQDIVAVGHRIVHGGEKFTSTVRIDEEVTAEIESLSDLAPLHNPAGAIGIRAAMAAFPSL
PQFAVFDTAFHQTMPKKAFTGAIAKELYTDFGIRRYGFHGTSHYFVSREAAKMLNKPIEESSFISVHLGN
GASVCAIKNGQSVDTSMGFTPLSGLMMGTRCGDLDPGIIEFLLKKGWSQEKVFNSLNKKSGFLGVSGLTS
DARGILEAMEEGHEGATLAFEVFTYRVAKYIASYLAALDSLDGIIFTGGIGENSLPIRREILKNLKLLGF
VEDEKGNEDARFGKAGIIAKSELLNAVAMVIPTNEEFVIAQQSVELL
>gnl|CDD|183530 PRK12444, PRK12444, threonyl-tRNA synthetase; Reviewed
MKEQMIEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNE
GVEIARHSAAHILAQAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIER
VEVSREEAAKLFQEMNDRLKLELLEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWR
GDSNNQVLQRIYGVAFSSQKELEEYLHFVEEAAKRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNEL
EAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMYFSEVDNKSFALKPMNCPGHMLMFKNKLHS
YRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEIKSVMAQIDYVYKTFGFEYEV
ELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALNRSHQCGTIQLDFQ
MPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAVHVQYADE
VADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVES
IKEEIKNRK
>gnl|CDD|171504 PRK12445, PRK12445, lysyl-tRNA synthetase; Reviewed
MSEQETRGANEAIDFNDELRNRREKLAALRQQGVAFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSV
AGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHC
TELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPM
MQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMEL
YMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREAIKKYRPETDMADLDNFDA
AKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGG
REIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSH
TIRDVILFPAMRPQK
>gnl|CDD|171505 PRK12446, PRK12446, undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
MKKIVFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNI
KDPFLVMKGVMDAYVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKI
FVTFEEAAKHLPKEKVIYTGSPVREEVLKGNREKGLAFLGFSRKKPVITIMGGSLGAKKINETVREALPE
LLLKYQIVHLCGKGNLDDSLQNKEGYRQFEYVHGELPDILAITDFVISRAGSNAIFEFLTLQKPMLLIPL
SKFASRGDQILNAESFERQGYASVLYEEDVTVNSLIKHVEELSHNNEKYKTALKKYNGKEAIQTIIDHIS
EA
>gnl|CDD|237103 PRK12447, PRK12447, histidinol dehydrogenase; Reviewed
MMIEYLKKAKSLEKRAETDSKVRETVEAILADIEARGDAAVREYSRKFDKWSPGSFRLSAAEIDAAVAKV
PEQVKEDIRFAQDQVRRFAEAQRDSLQDLEVETLPGVILGHRNIPVNSVGCYVPGGRYPLVASAHMSVLT
AKVAGVKRVIACTPPFPGEPPPAIVAAMHLAGADEIYVLGGVQAVAAMAYGTETIKPVDMLVGPGNAYVA
EAKRQLFGRVGIDLFAGPTETLVIADDTADPELVATDLLGQAEHGPNSPAVLITTSRKLAEEVLAEIERL
LAILPTADVASAAWRDYGEVILCDDLEEMVAEADRYASEHVQVMTEDPDWFLENMTNYGALFLGERTNVA
YGDKVIGTNHVLPTSGAARYTGGLWVGKFLKTVTYQRVTDEASAEIGEYCSRLCRLEGFEGHARQADIRV
RRYGGR
>gnl|CDD|237104 PRK12448, PRK12448, dihydroxy-acid dehydratase; Provisional
PKYRSRTTTHGRNMAGARALWRATGMKDEDFGKPIIAVVNSFTQFVPGHVHLKDLGQLVAREIEAAGGVA
KEFNTIAVDDGIAMGHGGMLYSLPSRELIADSVEYMVNAHCADAMVCISNCDKITPGMLMAALRLNIPVV
FVSGGPMEAGKTKLSDKIIKLDLVDAMVAAADPSVSDEDVAQIERSACPTCGSCSGMFTANSMNCLTEAL
GLSLPGNGSLLATHADRKQLFLEAGRRIVELAKRYYEQDDESVLPRSIATKAAFENAMTLDIAMGGSTNT
VLHLLAAAQEAEVDFTMADIDRLSRKVPCLCKVAPNTQKYHMEDVHRAGGIMGILGELDRAGLLHTDVPT
VHGLTLGEALDQWDIMRTQDEAVKEFFRAAPGGIRTTVAFSQDCRWDSLDTDRENGCIRSVEHAYSKDGG
LAVLYGNIAEDGCIVKTAGVDESILKFTGPARVFESQDDAVEAILGGKVKAGDVVVIRYEGPKGGPGMQE
MLYPTSYLKSKGLGKACALITDGRFSGGTSGLSIGHVSPEAASGGAIGLVEDGDIIEIDIPNRSINLLVS
DEELAARRAAQEARGDKAWKPKNRERKVSFALKAYAALATSADKGAVRDKSKLGG
>gnl|CDD|183533 PRK12449, PRK12449, acyl carrier protein; Provisional
MTREEIFERLINLIQKQRSYLSLAITEQTHLKDDLAVDSIELVEFIINVEDEFHIAIPDEDVEDMVSMGD
LLDYLVQRLT
>gnl|CDD|138982 PRK12450, PRK12450, foldase protein PrsA; Reviewed
MKQMNKLITGVVTLATVVTLSACQSSHNNTKLVSMKGDTITVSDFYNETKNTELAQKAMLSLVISRVFET
QYANKVSDKEVEKAYKQTADQYGTSFKTVLAQSGLTPETYKKQIRLTKLVEYAVKEQAKNETISKKDYRQ
AYDAYTPTMTAEIMQFEKEEDAKAALEAVKAEGADFAAIAKEKTIAADKKTTYTFDSGETTLPAEVVRAA
SGLKEGNRSEIITALDPATSKRTYHIIKVTKKATKKADWKAYQKRLKDIIVTGKLKDPDFQNKVIAKALD
KANVKIKDKAFANILAQFAKPNQKQPAQK
>gnl|CDD|171510 PRK12452, PRK12452, cardiolipin synthase
MKKPIVQLLLIFTIVSIVLFLLNTSYISLYTFVGVLWSITIVGISFVIFIENRSPQSTLAWFLVLALLPV
VGVLLYSIFGRSRWRRKKHLHRSEEQRKLFREILEGRRLELSLKVPLSERSVHLTEVVQKFGGGPAADRT
TTKLLTNGDQTFSEILQAIEQAKHHIHIQYYIYKSDEIGTKVRDALIKKAKDGVIVRFLYDGLGSNTLRR
RFLQPMKEAGIEIVEFDPIFSAWLLETVNYRNHRKIVIVDGEIGFTGGLNVGDEYLGRSKKFPVWRDSHL
KVEGKALYKLQAIFLEDWLYASSGLNTYSWDPFMNRQYFPGKEISNAEGAVQIVASGPSSDDKSIRNTLL
AVMGSAKKSIWIATPYFIPDQETLTLLRLSAISGIDVRILYPGKSDSIISDQASQSYFTPLLKAGASIYS
YKDGFMHAKIVLVDDKIATIGTANMDVRSFELNYEIISVLYESETVHDIKRDFEDDFKHSTEIKWNAFQK
RSIKKRILESFMRLISPLL
>gnl|CDD|183535 PRK12454, PRK12454, carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
MKKRIVIALGGNALLQPGEKGTAENQMKNVRKTAKQIADLIEEGYEVVITHGNGPQVGNLLLQMDAAKDV
GIPPFPLDVAGAMTQGWIGYMIQQALRNELAKRGIEKQVATIVTQVIVDKNDPAFQNPTKPVGPFYDEEE
AKKLAKEKGWIVKEDAGRGWRRVVPSPDPLGIVEIEVIKALVENGFIVIASGGGGIPVIEEDGELKGVEA
VIDKDLASELLAEELNADIFIILTDVEKVYLNYGKPDQKPLDKVTVEEAKKYYEEGHFKAGSMGPKILAA
IRFVENGGKRAIIASLEKAVEALEGKTGTRIIP
>gnl|CDD|84141 PRK12456, PRK12456, Na(+)-translocating NADH-quinone reductase subunit E; Provisional
MTESYLTIFIRAVFVENMALNFFLGMCTFLAISKKVETAFGLGLTVTALLAIATPLNNLIYTYILRENAL
IDGVDLSFLDFITFIGVLAALVQILEMVLERFLPSLHHTLGAFLPLLTIHCAIFGATIFMVQREYTFTES
FVYGTGCGLGWMLAIISMAGLREKMKYSNIPKGLQGLGIVFMTAGLMSLGFMSFSGIRL
>gnl|CDD|237105 PRK12457, PRK12457, 3-deoxy-8-phosphooctulonate synthase
MNVAISPGITVGNDLPFVLFGGINVLESLDFTLDVCGEYVEVTRKLGIPFVFKASFDKANRSSIHSYRGV
GLDEGLRIFEEVKARFGVPVITDVHEVEQAAPVAEVADVLQVPAFLARQTDLVVAIAKTGKPVNIKKPQF
MSPTQMKHVVSKCREAGNDRVILCERGSSFGYDNLVVDMLGFRQMKRTTGDLPVIFDVTHSLQCRDPLGA
ASGGRRRQVLDLARAGMAVGLAGLFLEAHPDPDRARCDGPSALPLDQLEPFLSQVKALDDLVKSFPPLDI
R
>gnl|CDD|183536 PRK12458, PRK12458, glutathione synthetase; Provisional
VNPWETEEETDTTLRLAHEAVNRGHEVAYTTPGDLTIRDDEALAFCAVTKKGKKYKKPENFLSFLKKAEF
KKERLPLAGFDVIFLRANPPLDPLARNWADSVGIAFGRLAARDGVLVVNDPDGLRIANNKLYFQSFPEEV
RPTTHISRNKEYIREFLEESPGDKMILKPLQGSGGQGVFLIEKSAQSNLNQILEFYSGDGYVIAQEYLPG
AEEGDVRILLLNGEPLERDGHYAAMRRVPAGGDVRSNVHAGGSVVKHTLTKEELELCEAIRPKLVRDGLF
FVGLDIVGDKLVEVNVFSPGGLTRINKLNKIDFVEDIIEALERKVQRKSAYRGAVDNA
>gnl|CDD|183538 PRK12460, PRK12460, 2-keto-3-deoxygluconate permease; Provisional
MHIKKAIKKIPGGMMVVPLLIGALINTFFPQALEIGGFTTALFKTGAAPLLGAFLLCMGAQISLKAAPQA
LLKGGVLTITKLGVAIVIGLLVGKFFGAEGIFGLSGLAIVAAMSNSNGGLYAALMGEFGDERDVGAISIL
SLNDGPFFTMLALGAAGLANIPIMALVAALLPLVLGMILGNLDPDMRKFLTKGGPLLIPFFAFALGAGIN
LSMLLQAGLAGILLGVLVTIVTGFFNIFADRLVGGTGIAGAAASSTAGNAVATPLAIAAADPSLAPVAAA
ATAQVAASVIVTAILTPLLTSWVAKKEAKKKA
>gnl|CDD|183539 PRK12461, PRK12461, UDP-N-acetylglucosamine acyltransferase; Provisional
MIHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEPQDFT
YKGEESRLEIGDRNVIREGVTIHRGTKGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTV
GDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPYCMMAGHPTNVHGLNAVGLRRRGFSSRAIRALKR
AYKIIYRSGLSVQQAVAELELQQFESPEVEELIDFIKASKRGIVR
>gnl|CDD|183540 PRK12462, PRK12462, phosphoserine aminotransferase; Provisional
MHRNQLNFSGGPGALPDTVLEQVRQAVVELPETGLSVLGMSHRSSWFSSLLAQAEADLRDLLGIPDEYGV
VFLQGGSSLQFSMIPMNFSRPGAAAPEYVTTGYWSRKAIGEASRVAAMRVVWDGAASGYRTLPSLAELDW
DARAPFRHYVSNETVEGLQFPDAAGLPDSPLIADMSSDFMSRPFDVEAYGMVYAHAQKNLGPAGVTVAII
RRALLERVPDTLPPMLDFRTHVEHRSNYNTPPVFAIYVMALVLRWIRDEIGGVHAMRDINARKAAMLYAT
LDALNEVIDCHAHRAARSTMNVAFRFRQPRLDTLFKEQSTEAGFCGLSGHRSIGGIRASLYNAVSEQAVS
RLCAFLKDFAIRHA
>gnl|CDD|171518 PRK12463, PRK12463, chorismate synthase; Reviewed
MRYITAGESHGPQLTVILEGVPAGLTLAAEHINKELLRRQKGHGRGRRMQIETDTVEIVSGVRHGMTLGS
PITLIVKNDDFKHWTKVMGAEPISEKESKEMKRTITKPRPGHADLNGAIKYGHRDIRNVLERSSARETTV
RVAAGAVAKQILKELGVEIAGHVLEIGGVKAKHISNLSIEEIQTITENSPVRCLDKTVEQEMMDAIDNAK
SSGDSIGGIVEVIAEGMPIGVGSYVHYDRKLDAKLAGAIMSINAFKGAEIGVGFEAARQPGSKVHDEILW
DEEQGYTRKTNNAGGLEGGMTTGMPIVVRGVMKPIPTLYKPLASVDIDTKEAFQASIERSDSCAVPAAGV
VAESVVAWELAHALVEQFGKDRMELIQQNITQHNKYAKEF
>gnl|CDD|237107 PRK12464, PRK12464, 1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
ILGSTGSIGTSALDVVSAHPEHFKVVGLTANYNIELLEQQIKRFQPRIVSVADKELADTLRTRLSANTSK
ITYGTDGLIAVATHPGSDLVLSSVVGAAGLLPTIEALKAKKDIALANKETLVAAGHIVTDLAKQNGCRLI
PVDSEHSAIFQCLNGENNKEIDKLIVTASGGAFRDKTREEMATLTAKDALKHPNWLMGAKLTIDSATLMN
KGFEVIEAHWLFDIPYEKIDVLIHKESIIHSLVEFIDGSVLAQLGAPDMRMPIQYAFHYPTRLPSSYEKL
NLLEIGSLHFEKPDLEKFPCLQYAYEAGKIGGTTPAVLNAANEIANALFLKNRIAFFDIEKTIYATLEAH
HNVKDPSLDDILEADAWARRYANQLLIKKSAPG
>gnl|CDD|183542 PRK12465, PRK12465, xylose isomerase; Provisional
MSNTVYIGAKEYFPGIGKIGFEGRDSDNPLAFKVYDANKTIGDKTMAEHLRFAVAYWHSFCGNGADPFGP
GTRAYPWDVGNTALARAEAKSDAAFEFFTKLGVPYYCFHDIDLAPDADDIGEYESNLKHMVGIAKQRQAD
TGIKLLWGTANLFSHPRYMNGASTNPDFNVVARAAVQVKAAIDATVELGGENYVFWGGREGYACLHNTQM
KREQDNMARFLTLARDYGRSIGFKGNFLIEPKPMEPMKHQYDFDSATVIGFLRQHGLDQDFKLNIEANHA
TLSGHSFEHDLQVASDAGLLGSIDANRGNPQNGWDTDQFPTDLYDTVGAMLVVLRQGGLAPGGLNFDAKV
RRESSDPQDLFLAHIGGMDAFARGLEVANALLTSSPLEQWRAERYASFDSGAGADFAAGKSTLADLAAHA
AGNAPTQISGRQEAYENLINQYLTR
>gnl|CDD|183543 PRK12466, PRK12466, 3-isopropylmalate dehydratase large subunit
MMPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRP
GRDRGITDPGGALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALG
ALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAI
RALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVE
IDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPARRAAMERALDYMGLTPGTPLAGIPIDRVFIGSCT
NGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDVL
APGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLLQAG
>gnl|CDD|237108 PRK12467, PRK12467, peptide synthase; Provisional
MDNNVALRIARRFITLPLEKRRLYLEKMQEEGVSFANLPIPQVRSAFERIPLSYAQERQWFLWQLDPDSA
AYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDDLANEQGRARE
SQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGRE
PSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQA
LSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDP
QASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTATGGRDREGAQLPGLT
VEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLL
DAEERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVG
PDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLR
SLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSM
LMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP
RPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANLGLY
ILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRADGVIEYLG
RMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQATRDELKAQL
RQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLKVERVGL
TDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLS
YAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGS
LTLEEPLLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLV
DELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAV
QSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLI
GFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDD
HQAQAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVAD
PERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRAN
RLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSH
LQARLPLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCAT
QEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSML
QQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRD
SVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLYRTGD
LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGLV
DDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSELEQ
RLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTV
SIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQED
GGWSAMHRAPEQERRPLLWQVVVADKEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHLV
VDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELP
CDHPQGGLQRRHAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGR
EDLFDEIDLTRTVGWFTSLYPVKLSPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALP
VPRITFNYLGQFDGSFDAEKQALFVPSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEA
TIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLSQEQLDRLPVAVGDIEDIYPLSPMQQGMLFHT
LYEGGAGDYINQMRVDVEGLDVERFRTAWQAVIDRHEILRSGFLWDGELEEPLQVVYKQARLPFSRLDWR
DRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFG
QPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARALYPAPAEAVAGHGAHYLHLDATQTR
QLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAE
QTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEALFDSILVFENYPISEALKQGAPSGLRFGAVSS
REQTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQV
LHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGV
AVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTLDRL
DLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFD
GAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYVFGG
EAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPV
PVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIR
GFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLL
VLAAMPLGPNGKVDRKALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLAL
QVLSRIRQSLGLKLSLRDLMSAPTIAELAGYSPLGDVPVNLLLDLNRLETGFPALFCRHEGLGTVFDYEP
LAVILEGDRHVLGLTCRHLLDDGWQDTSLQAMAVQYADYILWQQAKGPYGLLGWSLGGTLARLVAELLER
EGESEAFLGLFDNTLPLPDEFVPQAEFLELLRQLGELIGRANRLLRGLEEGGVGPDVLVGIAIQRCFDIA
PLELYTPLLDAGELAHIFDVAMRLKLLSLQLQEVPAAAAPVYCWWAGKKPTVKIRGFRIELGELEARLQQ
RMASVGIEANHFELLRHDCLLQQVVAYLIAQLPIDG
>gnl|CDD|171522 PRK12468, flhB, flagellar biosynthesis protein FlhB; Reviewed
MAEDSDQEKSEEPTASKLEKAREKGQIPRSRELTSMLMLGAGLTILWMSGESMARQLSAMVAQGLHFDHS
MVSNDKQMLRQIGMLLRQTLLAMLPIFAGLVIVALAVPMLLGGVLFSGESIKFDLKRMSPVAGLKRMFSS
QALAELLKAILKATLVGWVTGLFLWHNWPDMMRLIAAPPVAALGDALHLIIFCGLVVVLGLSPMVGFDVF
YQITSHIKKLRMTKQDIRDEFKNQEGDPHVKGRIRQQQRAMARRRMMVDVPKADVIVTNPTHYAVALQYN
ESKMSAPKVLAKGAGAVALRIRELGAEHRIPLLEAPPLARALFRHSEVGQHIPATLYAAVAEVLAWVYQL
KRWKREGGLIPKKPEHLPVPEALDFATESETKSETD
>gnl|CDD|237109 PRK12469, PRK12469, RNA polymerase factor sigma-54; Provisional
MSATLELRMRQHLALTPRLQQSLRLLQLSSLEFQQELREALDTNPFLEDVQDDAEDAAEATEADGEAGAA
DAEAQADDARPPDDEETDPGEVPYTAAPYYRGSSRRGGDGEDLSPGEWVAAEPTLHEHLHDALRLYFLTE
RDREIARTIIDALDDDGYLRQDLSELAEAADPELGLSEQELEVALRLVQSLDPPGVAARDLSECLLLQLD
ALPADTPALEEAKEIARHHLERLARRETAEIQRRIGCDQETLREACALVRRLDPRPGNHFGSARADYVVP
DVIVRQVRGKWVVTINPAVLPRARIHRRYAELFAQSSGERRSPLNQQLQEARWLIRNAQQRFDTIQRVAE
CIVARQRDFFRYGEIALKPLVLRDVAEELGLHESTISRATGNKYMATPRGTFEFKHFFPRKLEAAGGGEC
SAAAVRALIKEMIAAEQAGDPLSDVALAEMLAGRGVLIARRTVAKYREAMKIPPAELRRRD
>gnl|CDD|171524 PRK12470, PRK12470, amidase; Provisional
MDPTDLAFAGAAAQARMLADGELTAPMLLEVYLQRIERLDSHLRAYRVVLFDRARAEAEAAQQRLDAGER
LPLLGVPIAIKDDVDVAGEVTTYGSAGHGPAATSDAEVVRRLRAAGAVIIGKTNVPELMIMPFTESLAFG
ATRNPWDPNRTPGGSSGGSAAAVAAGLAPVALGSDGGGSIRIPSTWCGLFGLKPQRDRISLEPHDGAWQG
LSVNGPIARSVMDAALLLDATTTVPGPEGEFVAAAAREPGRLRIALSTRVPTPLPVRCGKQELAAVHQAG
ALLRDLGHDVVVRDPDYPAATYANYLPRFFRGISDDADAQAHPDRLEARTRAIARLGSFFSDRRMAALRA
AEVVLSARIQSIFDDVDVVVTPGTATGPSRIGAYQRRGAVSTLLLVVQRVPYFQVWNLTGQPAAVVPWDF
DGDGLPMSVQLVGRPYDEATLLALAAQIESARPWAHRRPPVS
>gnl|CDD|237110 PRK12472, PRK12472, hypothetical protein; Provisional
ASSVSAMRRFRTPAIVTLAALAALAALAGDAAAKRARPAAPTEATAPREAGEPIMAIVSIKSQRVTLYDA
DGWILRAPVSTGTTGRETPAGVFAIVEKDKDHHSTMYDDAWMPNMQRITWNGIALHGGPLPGYAASHGCV
RMPYGFAEKLFDKTRIGMRVIVSPNDAAPVDISHPALFVPKAEALAAAPARAETLAREAEDAARAADEAK
TAAAAAAREAAPLKASLRKLERAKARADAELKRADKALAAAKTDEAKARAEERQQKAAQQAAEAATQLDT
AKADAEAKRAAAAATKEAAKAAAAKKAETAKAATDAKLALEPVSIYISRATQKLYVRRNTHKPAPDGGEV
FDASIEVPVTIRDPDRPIGTHVFTAMARNDAGLRWSAVTIDDGDDAKAALDRITIPPEVLDRIAPTALPR
SSIIVSDEPLSVETNYRTEFVAVLSDQPQGGFITRKPTTAVVVVASDDDWDDGGFGFFFQRYPKPQPANP
RRRRGGPVYYRPFQPGWW
>gnl|CDD|183546 PRK12473, PRK12473, hypothetical protein; Provisional
MKKLVGLGLVAAISFGALSGCSLLGMIAEKANGFVLYGDEEQVQQIMDKYKDEVKSKDFYKMKMGTLEGK
KVLVMDKTTAEKMVKKELLKKVDVKDDTKPLDKLPAITDEQGILFAKEEVKNATLDGKKMKYEGNVIIGS
GRKYTDMYAIVDDATYAKIKGDEKTVGVLSFDKDPSKEFPGINRGSGVEESQLVKIKK
>gnl|CDD|139002 PRK12474, PRK12474, hypothetical protein; Provisional
MGQTMNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKPA
VTLLHLGPGLANGLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVD
SDVARAVQAAQSAPGGIATLIMPADVAWNEAAYAAQPLRGIGPAPVAAETVERIAALLRNGKKSALLLRG
SALRGAPLEAAGRIQAKTGVRLYCDTFAPRIERGAGRVPIERIPYFHEQITAFLKDVEQLVLVGAKPPVS
FFAYPGKPSWGAPPGCEIVYLAQPDEDLAQALQDLADAVDAPAEPAARTPLALPALPKGALNSLGVAQLI
AHRTPDQAIYADEALTSGLFFDMSYDRARPHTHLPLTGGSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAA
YTMQALWTMARENLDVTVVIFANRSYAILNGELQRVGAQGAGRNALSMLDLHNPELNWMKIAEGLGVEAS
RATTAEEFSAQYAAAMAQRGPRLIEAMI
>gnl|CDD|183547 PRK12475, PRK12475, thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
MQERYSRQILFSGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLY
TEEDAKQKKPKAIAAKEHLRKINSEVEIVPVVTDVTVEELEELVKEVDLIIDATDNFDTRLLINDLSQKY
NIPWIYGGCVGSYGVTYTIIPGKTPCLRCLMEHVPVGGATCDTAGIIQPAVQIVVAYQVTEALKILVEDF
EALRETFLSFDIWNNQNMSIKVNKQKKDTCPSCGLTRTYPSLTFENQTKTEVLCGRNTVQIRPGVRRRLN
LEEIKKRLQKIGKVDANPYLLSFQLDEYRFVLFTDGRAFIHGTNDIKKAKRLYARYIG
>gnl|CDD|171527 PRK12476, PRK12476, putative fatty-acid--CoA ligase; Provisional
MNDGSRQELRVPSGLLRIEDCLDADGNIALPPGTTLISLIERNIANVGDTVAYRYLDHSHSAAGCAVELT
WTQLGVRLRAVGARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPELPGHAERLDTALRD
AEPTVVLTTTAAAEAVEGFLRNLPRLRRPRVIAIDAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVG
VEITHRAVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVRRPQRWIK
ALSEGSRTGRVVTAAPNFAYEWAAQRGLPAEGDDIDLSNVVLIIGSEPVSIDAVTTFNKAFAPYGLPRTA
FKPSYGIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDT
GAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKLQSRLAEGSHADGAADDGTWLRTGDLGVYLDGE
LYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPA
IDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGVH
>gnl|CDD|183548 PRK12478, PRK12478, crotonase/enoyl-CoA hydratase family protein
TPDFQTLLYTTAGPVATITLNRPEQLNTIVPPMPDEIEAAIGLAERDQDIKVIVLRGAGRAFSGGYDFGG
GFQHWGEAMMTDGRWDPGKDFAMVTARETGPTQKFMAIWRASKPVIAQVHGWCVGGASDYALCADIVIAS
DDAVIGTPYSRMWGAYLTGMWLYRLSLAKVKWHSLTGRPLTGVQAAEAELINEAVPFERLEARVAEVATE
LARIPLSQLQAQKLIVNQAYENMGLASTQTLGGILDGLMRNTPDALEFIRTAETQGVRAAVERRDGPFGD
YSQAPPELRPDPTHVITP
>gnl|CDD|183549 PRK12479, PRK12479, branched-chain-amino-acid transaminase
MGNQYIYMNGEFVEKEKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIPLTVD
EMEEAVLQTLQKNEYADAYIRLIVSRGKGDLGLDPRSCVKPSVIIIAEQLKLFPQEFYDNGLSVVSVASR
RNTPDALDPRIKSMNYLNNVLVKIEAAQAGVLEALMLNQQGYVCEGSGDNVFVVKDGKVLTPPSYLGALE
GITRNSVIELCERLSIPCEERPFTRHDVYVADEVFLTGTAAELIPVVKVDSREIGDGKPGSVTKQLTEEF
KKLTRERGVRVPGLAESLL
>gnl|CDD|183550 PRK12480, PRK12480, D-lactate dehydrogenase; Provisional
MTKIMFFGTRDYEKEMALNWGKKNNVEVTTSKELLSSATVDQLKDYDGVTTMQFGKLENDVYPKLESYGI
KQIAQRTAGFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDIERRVQAHDFTWQAEIM
SKPVKNMTVAIIGTGRIGAATAKIYAGFGATITAYDAYPNKDLDFLTYKDSVKEAIKDADIISLHVPANK
ESYHLFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAIDTYENEAAYFTNDWTNKDIDDK
TLLELIEHERILVTPHIAFFSDEAVQNLVEGGLNAALSVINTGTCETRLN
>gnl|CDD|171531 PRK12481, PRK12481, 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD
MQLFDLNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPETQAQVEALGRKFHFITADLIQQKDI
DSIVSQAVEVMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNGGKIIN
IASMLSFQGGIRVPSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALRADTARNEAILER
IPASRWGTPDDLAGPAIFLSSSASDYVTGYTLAVDGGWLAR
>gnl|CDD|171532 PRK12482, PRK12482, flagellar motor stator protein MotA
MQKLFGLLVVMGCVFGGYLMSGGSLSSIWQPGEIIIILGAGIGAMILGNPKSVLKEMWHQIKGVIRRKEY
GVEFQRQLLLLLYELLEMVQEGGLKRLDQHIEIPEESSLFQKYPLILQQKRLITFISDNFRLMAMGKINQ
HELEGILDQELDAVEEELLQPSRSLQRIAEAMPGFGICAAVLGIIITMQSIDGSIAEIGLKVAAALVGTF
LGVFICYCLMDPLANAMEQEIKKELSLLECVRTVLVAHVAGKPTLLAVDAGRKLLPLDNKPTFATLDSWI
NAMITAG
>gnl|CDD|237111 PRK12483, PRK12483, threonine dehydratase; Reviewed
AAPTEAVSPTTIAPRAALLADYLRKILAARVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIR
GAYNKMARLPAEQLARGVITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGES
FPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYV
RPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHYVDEVVTVSTDELCAA
IKDIYDDTRSITEPAGALAVAGIKKYAEREGIEGQTLVAIDSGANVNFDRLRHVAERAELGEQREAIIAV
TIPEQPGSFKAFCAALGKRQITEFNYRYADAREAHLFVGVQTHPRHDPRAQLLASLRAQGFPVLDLTDDE
LAKLHIRHMVGGRAPLAHDERLFRFEFPERPGALMKFLSRLGPRWNISLFHYRNHGAADGRVLAGLQVPE
DERAALDAALAALGYPYWEETGNPAYRLFLG
>gnl|CDD|237112 PRK12484, PRK12484, nicotinate phosphoribosyltransferase; Provisional
QRNLALLTDLYEVTMANAYLREGMSAPATFSLFYRKLPDGRGFLIAAGLADVVEFLEAFRFDEQDLRYLR
GLNQFSEEFLAWLAGLRFTGDVRAVPEGTVVFPNEPLLEVTAPLIEAQLVETFLLNQINHQSLIASKAAR
CVLAAAGRPVVDFGARRAHGTDAACYVARASYLAGAAGTSNVLAARQYGIPASGTMAHSFVEAFPDEVAA
FRAFARLYPDATTLLVDTYDTLRGVRNAIEVAKELGNRFDPRGVRLDSGDLAELSKATRAILDAAGLEQV
KIVASGGLDEYRIAALLAAGAPIDGFGVGTRLGVAADAPVLDSAYKLVAYEGRGVTKLSSGKVTYPGRKQ
VFRLYEHGTACGDVIGLHTENIPDGREPLLVPVMTNGRRIQHAPTLDGARDWCEAQLAALPPEARRLVDP
VAVSVTLSGELARLRHADTAEAH
>gnl|CDD|171535 PRK12485, PRK12485, bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II
MAFNTIEEIIEDYRQGKMVLLVDDEDRENEGDLLLAAERCDAQAINFMAREARGLICLTLTDEHCQRLGL
EQMVPSNGSVFSTAFTVSIEAATGVTTGISAADRARTVAAAVAPNARPEDLVQPGHIFPLRAREGGVLTR
AGHTEAGCDLARLAGFSPASVIVEVMNDDGTMARRPDLEVFAAKHGIKIGTIADLIHYRLSTEHTIKRIG
ERELPTVHGTFRLVTYEDRIEGGVHMAMVMGDIRREQPTLVRVHVIDPLRDLVGAEYAGPANWTLWAALQ
KVAEEGHGVVVVLANHESSQALLERIPQLTQPPRQYQRSQSRIYSEVGTGAQILQDLGVGKLRHLGPPLK
YAGLTGYDLEVVESIPFPG
>gnl|CDD|237113 PRK12486, dmdA, dimethylsulfoniopropionate demethylase
KMALISPSRRLRRTPFSDGVEAAGVKAYTVYNHMLLPTVFESVEDDYAHLKEHVQVWDVAVERQVEIRGP
DAARLVQMLTPRDLRGMKPGQCYYVPIVDETGGMLNDPVALKLAEDRWWISIADSDLLLWVKGLANGRKL
DVLVVEPDVSPLAVQGPKADALMARVFGEAIRDLRFFRFGYFDFEGTDLVIARSGYSKQGGFEIYVEGSD
LGMPLWDALFEAGKDLNVRAGCPNLIERIEGGLLSYGNDMTRDNTPHECGLGRFCNTQTDIGCIGKDALL
RVAKEGPQKQIRGIKIGGERIPPCDRAWPLLAGDNRVGQVTSAAYSPDFQTNVAIGMVRMTHWDPGTGLE
VETPDGMRPATVREGFWI
>gnl|CDD|183553 PRK12487, PRK12487, putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase
MLDLLPDLFDHYEDKLTLLNLPFKNFGGKRIFWGEIVTVRCFEDNSKVKEVLAQDGKGKVLVVDGGGSCR
RALLGDQIAQSALDNGWEGIVINGCVRDVGALSTMDLGVKALGASPIKTEKRGQGEVNVTLTMGNVIIEP
GDMLYADENGIAVSKEALDFAFL
>gnl|CDD|237114 PRK12488, PRK12488, cation/acetate symporter
MKLLLPLALLLHSGALLASPALDAGQRQPLNWTAIGMFMVFVLFTLGITRWAARRTRSASDFYTAGGGLT
GMQNGLAIAGDMISAASFLGISAMMFMNGYDGLLYALGVLAGWPIILFLIAERLRNLGKYTFADVVSYRL
AQGPVRLTAAFGTLTVVLMYLVAQMVGAGKLIELLFGISYLYAVVIVGALMVLYVTFGGMLATTWVQIIK
AVLLLSGTSFMAFMVLKHFGFSTEAMFASAVAVHAKGQAILAPGGLLSNPIDAISLGLGMMFGTAGLPHI
LMRFFTVSDAREARKSVLYATGFIGYFYLLIIVVGFGAIVMVGTEPSYRDAGGKIIGGGNMVAVHLAQAV
GGNLFLGFISAVAFATILAVVAGLALSGASAVSHDLYACVIRKGQASEAQEMRVSKIATLGIGLLAVVLG
LMFESQNIAFLSGLVLAIAASVNFPVLFLSMFWKGLTTRGAVAGSYAGLVSAVVLVVLGPAVWVNVLHNA
TALFPYSNPALFSMSLAFLSAWVFSVTDRSERAVAERGRYLAQFVRSMTGIGAAGASKH
>gnl|CDD|237115 PRK12489, PRK12489, anaerobic C4-dicarboxylate transporter; Reviewed
MFWIQFLILLICLFLGARYGGIGLGLLGGIGLVILVFVFGLPPGKPPVDVMLIILAVVTASATLQAAGGL
DVMLQIAERLLRRNPKYITILAPFVTYTLTFLCGTGHVVYSILPIIYDVALKNGIRPERPMAAASVASQM
GITASPVSAAVVSLVAMLGNVTGEGRHITLLDILAVTIPATLIGVLAAALWSLRRGKDLDKDPEFQERLK
DPEFREYVYGTTATLLDKKLPKSAKLAVWIFLAAIAVVVLLAAFSELRPSFGGKPLSMVLVIQMVMLLTG
ALILILTKTDPASISNGEVFKSGMIAIVAIFGIAWMSDTFFGAHMPELKEVLGEMVKEYPWTYAIVLFLV
SKFVNSQAATLAAIVPVGLALGLDPALLVASMPACYGYFFLPTYPSDLAAINFDRTGTTRIGKFVINHSF
ILPGLIGVSVSCVFGYILAAIYL
>gnl|CDD|171539 PRK12492, PRK12492, long-chain-fatty-acid--CoA ligase; Provisional
MQPDFWNDKRPAGVPSTIDLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHT
DLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVL
PDTGIEYLIEAKMGDLLPAAKGWLVNTVVDKVKKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLDDIA
VLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMKEGQEVMIAPLPLYHIYAFTANCMCM
MVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATA
ERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGP
QVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVA
NCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD
IA
>gnl|CDD|237117 PRK12493, PRK12493, magnesium chelatase subunit H; Provisional
IRRVAPEDLNGRSLMKFVYVVLEPQYQSALSAAAASLNRENKLALELSGYLIEELRDPENWEEFKRDVAR
ADFFFGSLLFIEDLARPLVEALAPARDRLCPVCVIPSMPALMRLTKLGSFSLAQELGQSKSAIAQFMKKR
KPKGGAGEQDRMLKLLRTLPKVLKYLPGKAQDARTFILSHQYWLGGSPENLENFLLMLIDRYVPGYKGKL
PQLDPVFYPDLGIWHPLAPEMFEDLKEYLNWYNKRRDISDKLAPTVGLLLQRTHLLTGNDAHYVALIQEL
EARGARVIPAYAGGLDFRKPVEAFFYDPGNPDTPLVDLVVSLTGFALVGGPARQDHPKAIEALKKLNRPY
MVALPLVFQTTEEWEESDLGLHPVQVALQVAIPELDGAIEPIVLSGRDGATGKAIPLQDRIEAIAERAIR
WVRLRRKPRAEKKLAITLFSFPPDKGNVGTAAYLDVFGSIYRLLQELKAAGYDVELPESPKELMEAVLED
NRAQYGSPELNVAARLSVEEYERLTPYYERIEENWGPAPGELNSDGQNLLILGKHFGNVFIGVQPSFGYE
RDPMRLLMSKDASPHHGFAAYYTWLEKVWGADAVLHFGTHGALEFMPGKQMGMSASCWPDRLIGSLPNFY
YYAVNNPSEATIAKRRGYATLISYLTPPAENAGLYKGLRELSELIGSYQQLPDSGRGIQIVNTIREKARQ
LNLDKDVDLPETDAAELDEEERDAYVGALYRELMEIESRLIPCGLHVIGKPPTAEEAIDTLVLIASLDRP
EEGIRSLPELIAESLGRDYEELYRRNDRGVLADVELLQKITEITREAVRALVGELTGADGRVSLVSKLNF
FNMSLPRPWLAALYLAGYAGVDPGELKPLFEYLEFCLEQICADNELGSLLKALDGEYILPGPGGDPVRNP
AVLPTGRNIHALDPQSIPTAAAVAAGKRVVDELLERQREEQGAWPETIACVLWGTDNIKTYGEGLAQALA
LVGARPVPDELGRVNKVELIPLEELGRPRIDVVVTCSGIFRDLFINQMALLDQAVKLAAEADEPLEMNFV
RKHALEQAEELGISLREAATRVFSNASGSYGANVNLLVENSTWEEESELQEMFLSRKSFAFNADGEWNES
REVFESALKTVDVTFQNLDSSEIGLTDIDHYYEYLGGKLKSVERLDGKKPSVYIADTTTANAQVRSLEEM
VRLEARTKLLNPKWYEGMLKHGYEGVREIEKRLNNTYGWSATAGAVDNWVYEEVNETFIQDEEMRERLME
LNPHAFRRIVGRLLEANGRGFWETDEETLERLQELYQELEDRIEGVEEER
>gnl|CDD|183557 PRK12494, PRK12494, NAD(P)H-quinone oxidoreductase subunit J
EPETAATTPEAAIVEAGPVSQWLTENGFEHESLGPDHLGVEIIKVEPDFLLPIATALYAYGFNYLQCQGG
YDEGPGKELVSFYHLIKVSDNADKPREVRLKVFLPRDDPRVPSVYWIWKGADWQERETYDMYGINFEGHP
NLKRILMPEDWVGWPLRKDYIQPDFYELQDAY
>gnl|CDD|183558 PRK12495, PRK12495, hypothetical protein; Provisional
MSDFDKEAEREKLREKYEQDEQKREATERMSELLLQGATMTNAHCDECGDPIFRHDGQEFCPTCQQPVTE
DGAAGDDAGDGAEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEASSTSATDEAATDPPATAAARDGP
TPDPTAQPATPDERRSPRQRPPVSGEPPTPSTPDAHVAGTLQAARESLVETLARFARRAAATDDPRRARE
YLEAAREAAEALDALR
>gnl|CDD|237118 PRK12496, PRK12496, hypothetical protein; Provisional
MMIKVLDASAFIHGYNPEDGEHYTTPSVVEEVKDKESRLILESAISAGKLKILEPSPESIEKVEEAAIKT
GDLMRLSNTDIEVLALALELNGTLYTDDYGIQNVAKKLNIKFENIKTKGIKKVIKWRKVCKGCKKKYPED
YPDDVCEICGSPVKRKMVKRRLKK
>gnl|CDD|237119 PRK12497, PRK12497, YraN family protein
MMMKKRQLGAAGEDLAARYLESKGLRILARNFRCRFGEIDLIARDGDTLVFVEVKTRRSDRFGGAAEAVT
PRKQRRLRRAAQLWLARHPSLADLPCRFDVVAIGGPGPEIEHIKNAFDA
>gnl|CDD|183561 PRK12504, PRK12504, DUF4040 domain-containing protein
DMGTIINAALLLFLVATAVATALLRDVLASIVVFAAFSLGMALIYLILDAPDVAITEAAVGAGISTVLLL
LTLALTGRPDVDKVFERINVPAVLIALVLFVALLYAVPDLPAFGDPNAPAHSHVTQYYIENTYRETGIPN
VVTAVLASYRGYDTFGETVVVFTAGVAVLLVLRREVFA
>gnl|CDD|237120 PRK12505, PRK12505, putative monovalent cation/H+ antiporter subunit B; Reviewed
MSDREDTGLRTDYVESTIIMTTVRVVAPFVFTFGLFVMFHGADSPGGGFQGGVIVASVVLMLAFAFGIDA
TREWLDERLVVAIAVGGVLAFAAIGLGTVLLGGAFLEYHLYPIIHHASKYGIELVELGIGAIVASVIIGL
FFLLAAGFGHAEDGGNDES
>gnl|CDD|237121 PRK12507, PRK12507, putative monovalent cation/H+ antiporter subunit B; Reviewed
TALNFDLGNYLLNLILFLLILISIKIIFAKDLLNAVMLTSVFSLLIAVSFLIMDAPDVAMTEAAVGAGLS
TCVYLNALKLTGRLKNIERTKIIPALLIVLLFGVTLIYMGLDLPNYGDDDAPVHQHVAKYYIENTSRDIG
IPNFVTAILASYRGYDTLGETSVIFIAGIAVLLLLSRKSRRKIPRLDEGSSGHSQHYPILKYISKFLIPY
IILFSLYVQFHGEFSPGGGFQAGVIFASAIILYAMLYGLRKASRYFPPNVLILIAALGVAIYAIVGVISL
FNGGNFLDYYSLTNFINDPLLGQHIGILIVEIGVGLTVAAIMYLIYNVFAGR
>gnl|CDD|183563 PRK12508, PRK12508, Na(+)/H(+) antiporter subunit B
MIKNPILRTITKLMIPVIILFGLYVQFHGDYGPGGGFQAGVIVASAIILYSMLFGLSATLKAVPPSFVRL
MAALGVLIYGGTGIASMLLGGNFLSYDVLIFDSVTGQHLGIFLVELGVGLTVCSSMLIIYFAFASREKE
>gnl|CDD|237122 PRK12509, PRK12509, Na+/H+ antiporter subunit B
MYSLILATASRFLLPLLLLFSVFLLLRGHNEPGGGFIGGLVAAAAFALYLIANGIAAARRLLRVDPLRLL
AAGLLVAVLSGLPALFMGLPFLTALWWKLPLPLIGKVGTPLLFDVGVYLLVLGSTLTIVFSLAEEEG
>gnl|CDD|237123 PRK12511, PRK12511, RNA polymerase sigma factor; Provisional
MERKSKRFDVLDQLVPLRRYARSLTRDSAEAEDLVHDALVRALERRASFRSGGNLRTWLMSILHNAFIDE
LRRRRVEARRADELAVLADASLPAAQEHAVRLAQIRDAFFDLPEEQRAALHLVAIEGLSYQEAAAVLGIP
IGTLMSRIGRARAALRAFEEGTGPARGRAHLRVVGGNDAEDN
>gnl|CDD|171551 PRK12512, PRK12512, RNA polymerase sigma factor; Provisional
MMRGREDEWTDLMRSANAGDAAAYRRLLKAVTPVLRAAARRGLARAGQPADQAEDIVQEILLAVHLKRHT
WDPGAPFAPWLFAIARNKLIDALRRRGRRVFVDIDDFAETLPAEPATETLPAGDVGRHLETLPPRQRDVV
QSISVEGASIKETAAKLSMSEGAVRVALHRGLAALAAKFRSEPA
>gnl|CDD|183566 PRK12513, PRK12513, RNA polymerase sigma factor; Provisional
HLSGAMSTAAASDEALMLRYRAGDAAAFEALYARHRTGLYRFLLRLARDRALAEDIFQETWLRVIRARAQ
YQPRARFRTWLYQIARNLLIDHWRRHGARQAPSLDADEQLHALADDGAAPEQQLSLFRDRRRLQAALETL
PDEQREVFLLREHGDLELEEIAELTGVPEETVKSRLRYALQKLRELLAEEVAVA
>gnl|CDD|105710 PRK12514, PRK12514, RNA polymerase sigma factor; Provisional
TQPDDIEKLIVRVSLGDRDAFSSLYDATSAKLFGICLRVLKDRSEAEEALQDVYVKIWTKADRFAVSGLS
PMTWLITIARNHAIDRLRARKAVAVDIDEAHDLADPSPGPEAEVIAGDEGQRIDACLEELEKDRAAAVRR
AYLEGLSYKELAERHDVPLNTMRTWLRRSLLKLRECLSR
>gnl|CDD|183567 PRK12515, PRK12515, RNA polymerase sigma factor; Provisional
IIAAQATTDEMLLARIAQGDRTAMQTLYGRHHVRVYRFGLRLVRDEQTAEDLVSEVFLDVWRQAGQFEGR
SQVSTWLLSIARFKALSALRRRKHEEIDDEAAAAIEDGADTPEVALQKSDTSAALRACLAKLSPAHREII
DLVYYHEKSVEEVGEIVGIPESTVKTRMFYARKKLAELLKAAGVERGWP
>gnl|CDD|183568 PRK12516, PRK12516, RNA polymerase sigma factor; Provisional
TTGPSVEGTPPFKRELLAALPSLRAFAVSLIGRHDRADDLVQDTIMKAWAKQDHFEVGTNMKAWLFTILR
NEFYSQMRKRGREVQDTDGMFTEQLAVHPSQYGTLDLQDFRAALDQLPDDQREAIILVGASGFAYEEAAE
ICGCAVGTIKSRVNRARQRLQEILQIEGEADYGPDADSARATSRAFA
>gnl|CDD|183569 PRK12517, PRK12517, RNA polymerase sigma factor; Provisional
MFANFRKKSSESPVSSDMLSKQRRYEALVKALHADIYRYAYWLCKDKHIAEDLVQETFLRAWRSLDSLKD
EKAAKAWLITILRRENARRFERKQFDLVDIEDDSIEDDASHSSEEEMEQEWLRRQIAKLDPEYREPLLLQ
VIGGFSGEEIAEILDLNKNTVMTRLFRARNQLKEALEKPDVQRGQSNG
>gnl|CDD|237124 PRK12518, PRK12518, RNA polymerase sigma factor; Provisional
LILRCQRGDRQSFRQLYRRYQQKVRSTLYQLCGRELLDDLVQEVFLRVWKGLPKLRNPAYFSTWLYRITW
NVATDARRQFAQRPSRIQDDSLNDQPSRPSDTPDLMQLHYQDLVQQGLQTLSLEHRAVLVLHDLEDLPQK
EIAEILNIPVGTVKSRLFYARRQLRKFLQQQGVLL
>gnl|CDD|237125 PRK12519, PRK12519, RNA polymerase sigma factor; Provisional
PSAGDSAPTSLSSRSDAELFSALKAGQSAALGVLYDRHAGLVYGLALKILGNSQEAEDLTQEIFLSLWRK
SSYDPKRGSLSSYLLTLTRSRAIDRLRSRRSRQRLLERWQQELLGEASEDTPLEQASLAERSQRVQTALA
QLPESQRQVLELAYYEGLSQSEIAKRLGIPLGTVKARARQGLLKLRELLQDLLE
>gnl|CDD|237126 PRK12520, PRK12520, RNA polymerase sigma factor; Provisional
MTIAPAQLEALRPHLLRFARLQLRDPALAEDAVSETLLAVLEHPERFAGQSSLKTYLVGILKHKIIDAIR
SGRREVRLSLDDADEQSDDDLFDALFAADGHYREPPSDWGDPDAALSRREFFEVLQACVDRLPPRTGRVF
MMREWLELETEEICQELQITATNAWVLLYRARMRLRECLDLHWFGNPPAAA
>gnl|CDD|183571 PRK12522, PRK12522, RNA polymerase sigma factor; Provisional
MEEKVEELIDIYKQQIYSLCYKLAKTKEDAEDIFQETWIKVFSSRHQLSYVENYKKWITTICVRTFYDFY
RKKKRWKDRILDLFHKEDGGEIEFADDVNISEEFIQKVEAEMIREVIQLLNEKYKTVLVLYYYEQYSYKE
MSEILNIPIGTVKYRLNYAKKQMREHLEGFVHE
>gnl|CDD|183572 PRK12523, PRK12523, RNA polymerase sigma factor; Reviewed
MSSAQSPHSELVGALYRDHRGWLLAWLRRNVACRQRAEDLSQDTFVRLLGRPELPTPREPRAFLAAVAKG
LMFDHFRRAALEQAYLAELALVPEAEQPSPEEQHLILEDLKAIDRLLGKLSSKARAAFLYNRLDGMGHAE
IAERLGVSVSRVRQYLAQGLRQCYIALYGEPT
>gnl|CDD|183573 PRK12524, PRK12524, RNA polymerase sigma factor; Provisional
MTMPFDALSDVSDEALLVLYANGDPAAARALTLRLAPRALAVATRVLGDRAEAEDVTQEAMLRLWRIAPD
WRQGEARVSTWLYRVVCNLCTDRLRRRRRASVDLDDAPEPADAAPGAEEALIEGDRMRALDAALAALPER
QRQAVVLRHIEGLSNPEIAEVMEIGVEAVESLTARGKRALAALLAGQRAELGYGEG
>gnl|CDD|139037 PRK12525, PRK12525, RNA polymerase sigma factor; Provisional
MGQGSIKNTLIGQMFQQDYDWLCKKLSRQLGCPHSAEDIASETFLQVLALPDPASIREPRALLTTIARRL
MYEGWRRQDLERAYLQSLAEAPEAVQPSPEEQWMVIETLLAIDRLLDGLSGKARAAFLMSQLEGLTYVEI
GERLGVSLSRIHQYMVEAFKCCYQGFQE
>gnl|CDD|237127 PRK12526, PRK12526, RNA polymerase sigma factor; Provisional
RPTEPKKTGNIIKTQTDEQVPTELSQWLILVAISRDKQAFTHLFQFFAPKIKRFGIKQLGNEAQANELVQ
ETMSNVWRKAHLYNGDKGAATTWVYTVMRNAAFDMLRKIKAKKEQNLGDDIWPIEQALAESQSESEEFSD
HLMDKQILSYIEKLPEAQQTVVKGVYFQELSQEQLAQQLNVPLGTVKSRLRLALAKLKVQMGEQHD
>gnl|CDD|171560 PRK12527, PRK12527, RNA polymerase sigma factor; Reviewed
MENYYRELVRFLSARLGNRQAAEDVAHDAYLRVLERSSSAQIEHPRAFLYRTALNLVVDRHRRHRVRQAE
PLEVLDEEERLHSPSPQTRLDLGQRLALLQRALAELPPACRDSFLLRKLEGLSHQQIAEHLGISRSLVEK
HIVNAMKHCRVRMRQWESG
>gnl|CDD|171561 PRK12528, PRK12528, RNA polymerase sigma factor; Provisional
AHSATVEGLYSAHHHWLTGWLRRRLGCPQSAADLAQDTFVKVLVARETAQIIEPRAFLTTIAKRVLCNHY
RRQDLERAYLEALAQLPERVAPSEEERAIILETLVELDQLLDGLPPLVKRAFLLAQVDGLGYGEIATELG
ISLATVKRYLNKAAMRCYFAL
>gnl|CDD|183574 PRK12529, PRK12529, RNA polymerase sigma factor; Provisional
MNAPSSCLSADRDKVATLYRENHAWLRNWLAYRLRSWGRGVADDLAHDIFLRILASRDGGQREAIRQPRA
YLARIANCVLVSWRRRQSLELAWLEALATLPEPLHPSPEQQSVILETLHEIDALLDTLRPRVKQAFLMAT
LDGMKQKDIAQALDIALPTVKKYIHQAYVTCLSLMPDD
>gnl|CDD|237128 PRK12530, PRK12530, RNA polymerase sigma factor; Provisional
KIEQMNHISSLEIEEIRLQMLKFATLQLKDADLAEDVVQEALVSAYKNADSFKGQSALKTWIFAILKNKI
IDLIRYRKRFVNESELIEEDSPNSFFDEKGHWKPEYYEPSEWQEVENTVYKEEFWLIFEACLNHLPAQQA
RVFMMREYLELSSEQICQECDISTSNLHVLLYRARLQLQACLSKNWFDG
>gnl|CDD|105726 PRK12531, PRK12531, RNA polymerase sigma factor; Provisional
MFNPSPHTFGRQEWLECMEKVKSRDKQAFALVFSYYAPKLKQFAMKHVGNEQVAMEMVQETMSTVWQKAH
LFDGQKSALSTWIYTIIRNLCFDLLRKQKGKDLHIHADDIWPSDYYPPDLVDHYSPEQDMLKEQVMKFLD
RLPKAQRDVLQAVYLEELPHQQVAEMFDIPLGTVKSRLRLAVEKLRHSMDAESL
>gnl|CDD|171564 PRK12532, PRK12532, RNA polymerase sigma factor; Provisional
MPLPDLTDAELIESRKLLLHFARLQLPDHPDLAEDLVQETLLSAYSAGDSFQGRALVNSWLFAILKNKII
DALRQIGRQRKVFTLLDDELLDEAFESHFSQNGHWTPEGQPQHWNTPEKSLNNNEFQKILQSCLYNLPEN
TARVFTLKEILGFSSDEIQQMCGISTSNYHTIMHRARESLRQCLQIKWFNQENPK
>gnl|CDD|237129 PRK12533, PRK12533, RNA polymerase sigma factor; Provisional
ADSDRTAGAAMDAAARGERFRQLVLPHLDAAYNLARWLCGNASDADDVVQEACMRALRFFDSFRGDNARP
WLLAIVRHTWYSEWRRRANAHEVAAPDTLDDADSLDDWQPAGEDPLALLLRAEDVRLVNAALAKLPVEYR
EVLVLRELEDMSYREIAAIADVPVGTVMSRLARARRRLAALLGGASAAQAAPGERAAGRPRRAPAAGTAS
EAIDGL
>gnl|CDD|183576 PRK12534, PRK12534, RNA polymerase sigma factor; Provisional
MSAIPGHDDDETGRLLTATAGGDRHAFEALYRQTSPKLFGVCLRMIPQRAEAEEVLQDVFTLIWHKAGQF
DPSRARGLTWLAMIARNKAIDHLRANAPQRRNVALDDAGELRAADASPLERTERASTRRRIDHCLAELEP
PRSELIRTAFFEGITYEELAARTDTPIGTVKSWIRRGLAKLKACLER
>gnl|CDD|237130 PRK12535, PRK12535, RNA polymerase sigma factor; Provisional
TMKSSERDDAHVTDLALAAGRGDRAALTEFIRETQDDVWRLLAHLGGHDIADDLTQETYLRVMSALPRFA
ARSSARTWLLSLARRVWVDNIRHDMARPRKSATEYEDAAATTASNETTGSWSEWIDVRTLIDALPPERRE
ALILTQVLGYTYEEAAKIADVRVGTIRSRVARARADLIAATATGQASAERGKSAQG
>gnl|CDD|237131 PRK12536, PRK12536, RNA polymerase sigma factor; Provisional
LSAAEARLRALLLRGLAGDAAAYRQFLSELAAHLRGFLRRRLPQLPDEVEDLVQEILLAVHNARHTYRAD
QPLTAWVHAIARYKLMDFLRSRARREALHDPLDDESELFATSDDEAAEARRDLGKLLEQLPDRQRLPIVH
VKLEGLSVAETAQLTGLSESAVKVGIHRGLKALAAKIRGER
>gnl|CDD|171568 PRK12537, PRK12537, RNA polymerase sigma factor; Provisional
MSSPEAPFDYEACLLACARGDRRALQALYQQESARLLGVARRIVRDRALAEDIVHDAFIKIWTGAASFDP
ARGSARGWIYSVTRHLALNVLRDTRREVVLDDDAEETAQTLHEIIDDFDLWANSGKIHRCLEQLEPARRN
CILHAYVDGCSHAEIAQRLGAPLGTVKAWIKRSLKALRECMG
>gnl|CDD|139048 PRK12538, PRK12538, RNA polymerase sigma factor; Provisional
MNYALDVLAPAEAAPATTAPSPIVAEAPDAASVSIVPDPPPVADAVFDEDEELLDRLATDDEAAFRLLVE
RHIDRAYAIALRIVGNRADAEDVVQDTMLKVWTHRGRWQHGRAKFSTWLYRVVSNRCIDLRRKPRTENVD
AVPEVADGKPDAVSVIERNELSDLLEAAMQRLPEQQRIAVILSYHENMSNGEIAEVMDTTVAAVESLLKR
GRQQLRDLLRRHERDIRHAFTDC
>gnl|CDD|237132 PRK12539, PRK12539, RNA polymerase sigma factor SigF
MMSQENELKALMLASLDGDAAAHRALLERLSGHLRAYYKGKLARIGRGAEEAEDLVQEALMAIHTRRHTY
DPEQPLTPWVYAIARYKLIDHLRRTRASLADVPIDDADELVAHDDHAAVESTLDLGRLLARLPEKMRLAI
QAVKLEGLSVAEAATRSGMSESAVKVSVHRGLKALAALIGRETQ
>gnl|CDD|183579 PRK12540, PRK12540, RNA polymerase sigma factor; Provisional
MPLTDSLRDDILAAVPSLRAFAISLSGNGDRADDLVQETLLRALANIDSFQPGSNLPAWLFTILRNLFRS
DYRKRRREVEDADGSYAKTLKSQPGQNAHLEFEEFRAALDKLPQDQREALILVGASGFSYEDAAAICGCA
VGTIKSRVNRARSKLSALLYVDGAEDFGPDDTVRAVIGGSGG
>gnl|CDD|183580 PRK12541, PRK12541, RNA polymerase sigma factor; Provisional
MKRKQSLEEIYSEHMQDLFRYLLSLTGDSHFAEDLMQETFYRMLVHIDYYKGEEIRPWLFTIAYNAFIDW
YRKEKKYKTTTIEEFHLPNVPSTEHEYFIKHEIASWLDSLSSLPLERRNVLLLRDYYGFSYKEIAEMTGL
SLAKVKIELHRGRKETKSIKE
>gnl|CDD|183581 PRK12542, PRK12542, RNA polymerase sigma factor; Provisional
MKVTNNDYEKMEELYELYEQKVYYVAYSILNNIQQAEDAVQETFITLYKNLEKLHSLNTQELKRYILRVA
KNKAIDSYRKNKRHETFLEEYERESIEAVDENIEEWEKRKMSEVQIDTLLKELNESNRQVFKYKVFYNLT
YQEISSVMGITEANVRKQFERARKRVQNMIGGIQHDEFKELQRNI
>gnl|CDD|183582 PRK12543, PRK12543, RNA polymerase sigma factor; Provisional
MLSGDQEAFSEIYDVTIQEVYKTVHFLVEDKQDVDDVVNEIYIQLWESLRKYDSNRPFRFWLIGLVIKQI
HSWRRKRWRRFRIFEKAEEQRKPVSIDFSEDVLSKESNQELIELIHKLPYKLRQVIILRYLHDYSQEEIA
QLLQIPIGTVKSRIHAALKKLRQKEQIEEIFLGEVGNVK
>gnl|CDD|183583 PRK12544, PRK12544, RNA polymerase factor sigma-70
SNANSAVAMDSSDLGNLLQDPVFLEDLRKQMIKFATLQLSDLHLAEDAVQEALIGALKNADSFAGRAAFK
TWVFAILKNKIIDLLRQKKRHVSASSLLRDEEEEEDFEELFDESGHWQKDERPQAWGNPEESLEQEQFWR
IFEACLDGLPAKYARVFMMREFIELETNEICHAVDLSVSNLNVLLYRARLRLRECLENKWFLKEDC
>gnl|CDD|183584 PRK12545, PRK12545, RNA polymerase factor sigma-70
MQHMRSAHDDPAYLAQLRHDLLRFARLQLRDADAAEDAVQEALAAAWSQAGRFAGQSAHKTWVFGILRNK
LIDTLRARQRTVNLSALDAELDGEALLDRELFKDNGHWAAHAKPRPWPKPETILQQQQFWTLFETCLDHL
PEQIGRVFMMREFLDFEIDDICTELTLTANHCSVLLYRARTRLRTCLSEKGLTTEDAAGEM
>gnl|CDD|139055 PRK12546, PRK12546, RNA polymerase sigma factor; Provisional
KAPAKHRDPRDELVEHLPALRAFAISLTRNVAVADDLVQDTIVKAWTNFDKFQEGTNLRAWLFTILRNTF
YSDRRKHKREVPDPEGVHAASLAVKPAHDGRLAMSDFRAAFAQLPDEQREALILVGASGFSYEEAAEMCG
VAVGTVKSRANRARARLAELLQLEEGEELEMTDGATLAVMSRNGMTAA
>gnl|CDD|139056 PRK12547, PRK12547, RNA polymerase sigma factor; Provisional
MMKCSKNFKQELLLALPALRAFAVSLSSKHDKAEDLVQDTLMKAWAKQDSFEMGTNLKAWLFTILRNEFY
SQMRKRGREVQDSDGVFTARVAVHPAQYGSLDLQDFKKALNLLSADQREAIILIGASGFSYEDAAAICGC
AVGTIKSRVSRARNRLQELLKVDG
>gnl|CDD|183585 PRK12548, PRK12548, shikimate dehydrogenase
MENRISGTTGLLGLIGSPVGHSGSPAMYNYSFQKAGLDYAYLAFDIPVDKVPDAIKAIKTFNMRGANVTM
PCKSEAAKYMDELSPAARIIGAVNTIVNDDGKLTGHITDGLGFVRNLREHGVDVKGKKLTVIGAGGAATA
IQVQCALDGAKEITIFNIKDDFYERAEQTAEKIKQEVPECIVNVYDLNDTEKLKAEIASSDILVNATLVG
MKPNDGETNIKDTSVFRKDLVVADTVYNPKKTKLLEDAEAAGCKTVGGLGMLLWQGAEAYKLYTGKDMPV
EEVKELYFS
>gnl|CDD|183586 PRK12549, PRK12549, shikimate 5-dehydrogenase; Reviewed
MSRPSFLAGLIGAGIQASLSPAMHEAEGDAQGLRYVYRLIDLDALGLTADALPELLDAAERMGFAGLNIT
HPCKQAVIPHLDELSDDARALGAVNTVVFRDGRRIGHNTDWSGFAESFRRGLPDASLERVVQLGAGGAGA
AVAHALLTLGVERLTIFDVDPARAAALADELNARFPAARATAGSDLAAALAAADGLVHATPTGMAKHPGL
PLPAELLRPGLWVADIVYFPLETELLRAARALGCRTLDGGGMAVFQAVDAFELFTGREPDAERMLAHFAS
LVAR
>gnl|CDD|183587 PRK12550, PRK12550, shikimate 5-dehydrogenase; Reviewed
MTNMINKDTQLCISLAARPSNFGTRFHNYLYEALGLNFLYKAFTTTDLTAAIGGVRALGIRGCAVSMPFK
EAVIPLVDELDPSAQAIESVNTIVNTDGHLKAYNTDYIAIAKLLASYQVPPDLVVALRGSGGMAKAVAAA
LRDAGFTDGTIVARNEKTGKALAELYGYEWRPDLGGIEADILVNVTPIGMAGGPEADKLAFPEAEIDAAS
VVFDVVALPAETPLIRYARARGKTVITGAEVIALQAVEQFVLYTGVRPSDELIAEAAAFARA
>gnl|CDD|139060 PRK12551, PRK12551, ATP-dependent Clp protease proteolytic subunit; Reviewed
MIPIVIEESGRGERAFDIYSRLLRERIIFLGEPVTSDSANRIVAQLLFLEAEDPEKDIYLYINSPGGSVY
DGLGIFDTMQHVKPDVHTVCVGLAASMGAFLLCAGAKGKRSSLQHSRIMIHQPLGGARGQASDIRIQADE
ILFLKERLNTELSERTGQPLERIQEDTDRDFFMSPSEAVEYGLIDLVIDKRPVKAV
>gnl|CDD|183588 PRK12552, PRK12552, ATP-dependent Clp protease proteolytic subunit
SPIMAVQAPYYGDAVMRTPPPDLPSLLLKERIVYLGLPLFSDDDAKRQVGMDVTELIIAQLLYLEFDDPE
KPIYFYINSTGTSWYTGDAIGFETEAFAICDTMRYIKPPVHTICIGQAMGTAAMILSAGTKGQRASLPHA
TIVLHQPRSGARGQATDIQIRAKEVLHNKRTMLEILSRNTGQTVEKLSKDTDRMFYLTPQEAKEYGLIDR
VLESRKDLPKPV
>gnl|CDD|237133 PRK12553, PRK12553, ATP-dependent Clp protease proteolytic subunit; Reviewed
NSMMQPESRYILPSFIERTSYGVKESDPYNKLFEERIIFLGGQVDDASANDVMAQLLVLESIDPDRDITL
YINSPGGSVTAGDAIYDTIQFIRPDVQTVCTGQAASAGAVLLAAGTPGKRFALPNARILIHQPSLGGGIR
GQASDLEIQAREILRMRERLERILAEHTGQSVEKIRKDTDRDKWLTAEEAKDYGLVDQIITSYRDLK
>gnl|CDD|237134 PRK12554, PRK12554, undecaprenyl pyrophosphate phosphatase; Reviewed
MSLFKAIILGLVQGLTEFLPVSSSGHLRIVGALLGWDDPGAAFTAIIQLGTLLAVLLYFRKDIIRIIKNF
FSSLFGRKPKAKSDARFGWYIIIGTIPAGVLGLLFKDRIETVLRDLRIVAIALIVTGVLLWLADNLARNR
GRKSDEDLTWKDAIIIGLAQALALIPGVSRSGATIIAGLLLGLTREAAARFSFLLAIPAVFGAGLLELYK
IFHDPNASTLLGPTAVAFIVAFIVGYISIAWFMNFLKKGSLKYFAIYRIILGVLLLILLGTGVLSP
>gnl|CDD|237135 PRK12555, PRK12555, chemotaxis-specific protein-glutamate methyltransferase CheB
MRIGIVNDSPLAVEALRRALARDPDHEVVWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMA
ERPCPILIVTSLTERNASRVFEAMGAGALDAVDTPTLGIGAGLEEYAAELLAKIDQIGRLLGRRLAPAAA
PAAASAAPFRTTPRLVAIGASAGGPAALAVLLGGLPADFPAAIVIVQHVDAAFAAGMAEWLDGQTALPVR
EAREGERPQPGHVLLAPTNDHLRLTRDGALRYTREPPVNPYRPSVDVFFESVAQHWGGNAIGVLLTGMGR
DGARGLKAMRQAGAHTIAQDEASSAVYGMPKAAAALGAASEVLPLERIAPRLIALFA
>gnl|CDD|183592 PRK12556, PRK12556, tryptophanyl-tRNA synthetase; Provisional
MSEKIMLTGIKPTGYPHLGNYIGAIKPALQMAKNYEGKALYFIADYHALNAVHDPEQFRSYTREVAATWL
SLGLDPEDVIFYRQSDVPEIFELAWILSCLTPKGLMNRAHAYKAKVDQNKEAGLDLDAGVNMGLYTYPIL
MAADILLFQATHVPVGKDQIQHIEIARDIATYFNHTFGDTFTLPEYVIQEEGAILPGLDGRKMSKSYGNV
IPLFAEQEKLRKLIFKIKTDSSLPNEPKDPETSALFTIYKEFATEEEVQSMREKYETGIGWGDVKKELFR
VVDRELAGPREKYAMYMNEPSLLDEALEKGAERAREIAKPNLAEIKKAIGFE
>gnl|CDD|237136 PRK12557, PRK12557, H(2)-dependent methylenetetrahydromethanopterin dehydrogenase-related protein; Provisional
MKVSVYGAGNQKLYLEQLNLPEKFGGEPPYGGSRMAIEFAEAGHDVVLAEPNRSILSEELWKKVEDAGVK
VVSDDAEAAKHGEIHILFTPFGKKTVEIAKNILPHLPENAVICNTCTVSPVVLYYSLEGELRTKRKDVGI
SSMHPAAVPGTPQHGHYVIAGKTTNGTELATEEQIEKCVELAESIGKEPYVVPADVVSAVADMGSLVTAV
ALSGVLDYYSVGTKIIKAPKEMIEKQILMTLQTMASLVETSGVDGLLKALNPELLLRSASSMHLLEKQKD
LDAALEILENLDEDLLKEIEEAEIKPTTLVAAQALVKEIKTLIGGRAAEGAIRRSMRKLFEH
>gnl|CDD|79035 PRK12559, PRK12559, transcriptional regulator Spx; Provisional
MVVLYTTASCASCRKAKAWLEENQIDYTEKNIVSNSMTVDELKSILRLTEEGATEIISTRSKTFQDLNIN
IEELSLNEFYKLIIEHPLMLRRPIMLDEKRLQIGFNDEEIRKFLPRSVRTFLNIELQKLAN
>gnl|CDD|183595 PRK12560, PRK12560, adenine phosphoribosyltransferase; Provisional
MLLKNLYKNARVVNSGKALTTVNEFTDQLPALRPKVLKETAKEIIKYIDKDIDKIVTEEDKGAPLATPVS
LLSGKPLAMARWYPYSLSELNYNVVEIGSEYFEGVVYLNGIEKGDRVAIIDDTLSTGGTVIALIKAIENS
GGIVSDVICVIEKTQNNGRKKLFTQTGINVKSLVKIDVKPHGVDIIE
>gnl|CDD|237137 PRK12561, PRK12561, NAD(P)H-quinone oxidoreductase subunit 4; Provisional
DKEGKTVRWYALGVGLADFALMCYVFWQHYDPSSSSLQLVERYAWLPQIGLEWSLGVDGLSMPLVLLSGL
ITTLSIFASWKVTRKPRLFYFLMLVLYSAQIGVFLAQDLLLFFLMWELELVPVYLLISIWGGQKRLYAAT
KFILYTALASIFILVAGLALALSGDTFTFDLAELGAKSYPLALELLLYAGFLIAFGVKLPIFPLHTWLPD
AHGEASAPVSMILAGVLLKMGGYALIRFNVQMLPDAHVYFAPALAILGVVNIIYGALNAFAQDNVKRRLA
YSSVSHMGFVLLGIAAFTDLGISGAMLQMISHGLIAAALFFLTGVTYERTHTLSIPNMGGLAKVMPKTFA
LFTASSMASLALPGMSGFVSELTVFLGITSSDVYSSTFRTITILLAAVGLILTPIYLLSMLRRVFYGPRS
ELLPALAVVEDAKPRELFIALSLLVPIIGIGFYPKLATQLYDVKTVALAAQLRQALPVIAQQPQLYAKGF
TAPTIAESELLGIS
>gnl|CDD|105755 PRK12562, PRK12562, ornithine carbamoyltransferase subunit F; Provisional
MSGFYKKHFLKLLDFTPAELNSLLQLAAKLKADKKNGKEVARLTGKNIALIFEKDSTRTRCSFEVAAYDQ
GARVTYLGPSGSQIGHKESIKDTARVLGRMYDGIQYRGHGQEVVETLAEYAGVPVWNGLTNEFHPTQLLA
DLLTMQEHLPGKAFNEMTLVYAGDARNNMGNSMLEAAALTGLDLRLVAPQACWPEASLVAECSALAQKHG
GKITLTEDIAAGVKGADFIYTDVWVSMGEPKEKWAERIALLRGYQVNSKMMALTGNPQVKFLHCLPAFHD
DQTTLGKKMAKEFGLHGGMEVTDEVFESPASIVFDQAENRMHTIKAVMVATLAK
>gnl|CDD|237138 PRK12563, PRK12563, sulfate adenylyltransferase subunit CysD
EPSSPGGAAGASTSRMGHLDRLEAESIHILREVVAECSKPVMLYSIGKDSVVMLHLAMKAFRPTRPPFPL
LHVDTTWKFREMIDFRDRRAKELGLDLVVHHNPDGIARGIVPFRHGSALHTDVAKTQGLKQALDHHGFDA
AIGGARRDEEKSRAKERIFSFRSAFHRWDPKAQRPELWSLYNARLRRGESLRVFPLSNWTELDVWQYIAR
EKIPLVPLYFAKRRPVVERDGLLIMVDDERTPLRPGETPQQRKVRFRTLGCYPLTGAVESDADTVEKIIQ
EMAVTRISERQGRMIDQDSAASMEKKKKEGYF
>gnl|CDD|237139 PRK12564, PRK12564, carbamoyl-phosphate synthase small subunit
MMMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDF
ESDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAE
ELLEKARAFPGLLGLDLVKEVSTKEPYPWPGPGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTT
AEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGAN
HPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSA
YLFDEFVELM
>gnl|CDD|237140 PRK12567, PRK12567, putative monovalent cation/H+ antiporter subunit B; Reviewed
MKWVYLLAILLLFIKVLLSPSFALEPGGRDYVESVVEETGVPNAVTGIIVRNRLYDTLGEVTVFFIAALG
VGLLLANEKPKEKIRRFSDVPLRVLARLLAPFILLFGIYLAIHGHLTPGGGFAAGVAGGTAILLLALSSS
PEEMEHIYERWRAKVWEKLAGLVFVLLGLIGLAGGFLPTGELGALFSGGVIPILNILIGLKVGLGLWGII
LNFIRYRG
>gnl|CDD|139075 PRK12568, PRK12568, glycogen branching enzyme; Provisional
MATEGISEAVMSQTLQALADGLPADAFAVLGPHPQADGRRQVRVLAPGAEAMGLIDGRGKLLARMQASPI
DGVFEGILPADGPYRLRIVWPDVVQEIEDPYAFAPTLDESLLLQIAAGDGQALRRALGAQHVQVGEVPGV
RFAVWAPHAQRVAVVGDFNGWDVRRHPMRQRIGGFWELFLPRVEAGARYKYAITAADGRVLLKADPVARQ
TELPPATASVVPSAAAFAWTDAAWMARRDPAAVPAPLSIYEVHAASWRRDGHNQPLDWPTLAEQLIPYVQ
QLGFTHIELLPITEHPFGGSWGYQPLGLYAPTARHGSPDGFAQFVDACHRAGIGVILDWVSAHFPDDAHG
LAQFDGAALYEHADPREGMHRDWNTLIYNYGRPEVTAYLLGSALEWIEHYHLDGLRVDAVASMLYRDYGR
AEGEWVPNAHGGRENLEAVAFLRQLNREIASQFPGVLTIAEESTAWPGVTAPISDGGLGFTHKWNMGWMH
DTLHYMQRDPAERAHHHSQLTFGLVYAFSERFVLPLSHDEVVHGTGGLLGQMPGDDWRRFANLRAYLALM
WAHPGDKLLFMGAEFGQWADWNHDQSLDWHLLDGARHRGMQQLVGDLNAALRRTPALYRGTHRADGFDWS
VADDARNSVLAFIRHDPDGGGVPLLAVSNLTPQPHHDYRVGVPRAGGWREILNTDSAHYGGSNLGNSGRL
ATEPTGMHGHAQSLRLTLPPLATIYLQAEK
>gnl|CDD|237141 PRK12569, PRK12569, hypothetical protein; Provisional
MKMSIDLNSDMGEGFGPWRIGDGVDEALMPLISSANIATGFHAGDPNIMRRTVELAKAHGVGIGAHPGFR
DLVGFGRRHINASPQELVNDVLYQLGALREFARAHGVRLQHVKPHGALYMHAARDEALARLLVEALARLD
PLLILYCMDGSATERAARELGQPVVREFYADRDYDDSGSIVFTRRVGALDPQQVAAKVLRACREGKVRTV
DGKDIDIDFDSICIHSDTPGALALARATRAALEAA
>gnl|CDD|237142 PRK12570, PRK12570, N-acetylmuramic acid-6-phosphate etherase; Reviewed
HLVSEGRNPATMDIDLLSSLDIVTLINQEDKKVPLAVEKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSG
RLGVLDASECPPTFSVSPEMVIGLIAGGPEAMFTAVEGAEDDPELGAQDLKAIGLTADDVVVGIAASGRT
PYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTRLKSGTAQKMVLNMLSTASMI
RLGKSYQNLMVDVKATNEKLVARAVRIVMQATGCSEDEAKELLKESDNDVKLAILMILTGMDVEQARAAL
SHADGFLRKAIEAHEK
>gnl|CDD|183601 PRK12571, PRK12571, 1-deoxy-D-xylulose-5-phosphate synthase; Provisional
TPRPKTPLLDRIKGPADLRALSDAELEQLADELRAEVISAVSETGGHLGSSLGVVELTVALHAVFNTPKD
KLVWDVGHQCYPHKILTGRRDRFRTLRQKGGLSGFTKRSESEYDPFGAAHSSTSISAALGFAKARALGQP
DGDVVAVIGDGSLTAGMAYEALNNAGAADRRLIVILNDNEMSIAPPVGALAAYLSTLRSSDPFARLRAIA
KGVEERLPGPLRDGARRARELVTGMIGGGTLFEELGFTYVGPIDGHDMEALLSVLRAARARADGPVLVHV
VTEKGRGYAPAEADEDKYHAVGKFDVVTGLQKKSAPSAPSYTSVFGEELTKEAAEDSDIVAITAAMPLGT
GLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYSTFLQRGYDQLLHDVALQNLPVRFVLDR
AGLVGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFPRGEGVGVEIPAEG
TILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTDLLVRHHIVVI
VEEQGAMGGFGAHVLHHLADTGLLDGGLKLRTLGLPDRFIDHASREEMYAEAGLTAPDIAAAVTGALARL
SGVPERETAPP
>gnl|CDD|183602 PRK12573, PRK12573, Na(+)/H(+) antiporter subunit B
MKMNDLILRTVAKIVTFIILLFSVFLFLAGHNEPGGGFIGGLITASALVILLLAFDIKTVRRALPFDFKI
LAGIGLLFAIATGLASIFFGVPFLTHLFFYIPLPILGEVELTTAMLFDLGVYLVVVGVTMTIILTIGENE
>gnl|CDD|183603 PRK12574, PRK12574, monovalent cation/H+ antiporter subunit B
MKENDVVLKTVTKIVVFILLTFGFYLFLAGHNNPGGGFIGGLIFSSAFILMFLAFGVEEVLESLPIDFRK
LMIIGLLLSSITAIIPMFFGKPFLRQAETFVILPLLGEIHLSSITLFELGILFVVVGVIVTIMLSLSGDK
S
>gnl|CDD|171592 PRK12575, PRK12575, succinate dehydrogenase/fumarate reductase iron-sulfur subunit
MADTRILHIYRYDPDDDAAPRMQRYEIAPRAEDRMLLDVLGRVKAQDETLSYRRSCREGICGSDAMNING
RNGLACLTNMQALPREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTVPPERERLQTPQEREQL
DGLYECILCACCSTACPSYWWNPDKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCV
DVCPKGLNPARAIGQIRTMLARRAV
>gnl|CDD|237143 PRK12576, PRK12576, succinate dehydrogenase/fumarate reductase iron-sulfur subunit
MTQSPEKEVIFKVKRYDPEKGSWWQEYKVKVDRFTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKI
NGEPRLACKTLVLDVAKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRL
KPEDQKELWKFAQCIWCGLCVSACPVVAIDPEFLGPAAHAKGYRFLADPRDTITEERMKILIDSSWRCTY
CYSCSNVCPRDIEPVTAIKKTRSFTRVYKPKSEVAERGEKHVEAIRESIFKTGKLEEAPVYLKTYGLLQ
>gnl|CDD|183605 PRK12577, PRK12577, succinate dehydrogenase/fumarate reductase iron-sulfur subunit
MEVLFKILRQKQNSAPYVQTYTLEVEPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSAL
ACKENVGSELARLSDSNSGAIPEITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAARQVPEREFLQ
TPEERSKLDQTGNCILCGACYSECNAREVNPEFVGPHALAKAQRMVADSRDTATEQRLELYNQGTAGVWG
CTRCYYCNSVCPMEVAPLDQITKIKQEILARKDAQDSRAIRHRKVLVDLVKEGGWIDERKFGLQVVGNYF
RDLKGLLSLVPLGLRMLARGKFPLSFEPSEGTAQVRSLIESVQKEDSNS
>gnl|CDD|183606 PRK12578, PRK12578, thiolase domain-containing protein
RRVAVIGVGNSKFGRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGL
TGKVPLRVEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKMTEVDTSTSLAIGGRGGNYQWEYHFYGTT
FPTYYALYATRHMAVYGTTEEQMALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPIS
DGSATAIFASEEKVKELKIDSPVWITGIGYANDYAYVARRGEWVGFKATQLAARQAYNMAKVTPNDIEVA
TVHDAFTIAEIMGYEDLGFTEKGKGGKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATGLSMIYEITKQL
RDEAGKLQQPLKKYIGLVHNVGGTGHFAYVMILRR
>gnl|CDD|183607 PRK12579, PRK12579, putative monovalent cation/H+ antiporter subunit B; Reviewed
MTQKRDIAVALSFFFFGAAILYSLFNINVVPGVNYVYLQNYIVPNLVTAVLFDWRAFDTLGECLILVTSV
MVTGMVFGRGLYDNEFLKEVFSAPESEDYITLQRWGGFTSIIKVLAMPMSILLMALGIITILGGHITPGG
GFQGGALIAAAYILSIVAFGSKSPLWFKHHFLEKLEAFGALLFMLLGVLGMFVSGYYLFNFTELNGYPVF
PSPKGLENTGIIPYLNIAVGLKVLAGLSTITFLLSGEKVIIEYIVKEE
>gnl|CDD|79055 PRK12580, PRK12580, omptin family plasminogen activator Pla
MKKSSIVATIITILSGSANAASSQLIPNISPDSFTVAASTGMLSGKSHEMLYDAETGRKISQLDWKIKNV
AILKGDISWDPYSFLTLNARGWTSLASGSGNMDDYDWMNENQSEWTDHSSHPATNVNHANEYDLNVKGWL
LQDENYKAGITAGYQETRFSWTATGGSYSYNNGAYTGNFPKGVRVIGYNQRFSMPYIGLAGQYRINDFEL
NALFKFSDWVRAHDNDEHYMRDLTFREKTSGSRYYGTVINAGYYVTPNAKVFAEFTYSKYDEGKGGTQTI
DKNSGDSVSIGGDAAGISNKNYTVTAGLQYRF
>gnl|CDD|79056 PRK12581, PRK12581, oxaloacetate decarboxylase; Provisional
MIQFGGFSMQQQVAITETVLRDGHQSLMATRLSIEDMLPVLTILDKIGYYSLECWGGATFDACIRFLNED
PWERLRTLKKGLPNTRLQMLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRA
VKKTGKEAQLCIAYTTSPVHTLNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIKAMTNLPLI
VHTHATSGISQMTYLAAVEAGADRIDTALSPFSEGTSQPATESMYLALKEAGYDITLDETLLEQAANHLR
QARQKYLADGILDPSLLFPDPRTLQYQVPGGMLSNMLSQLKQANAESKLEEVLAEVPRVRKDLGYPPLVT
PLSQMVGTQAAMNVILGKPYQMVSKEIKQYLAGDYGKTPAPVNEDLKRSQIGSAPVTTNRPADQLSPEFE
VLKAEVADLAQTDEDVLTYALFPSVAKPFLTTKYQTDDVIKVTAFIKA
>gnl|CDD|237144 PRK12582, PRK12582, acyl-CoA synthetase; Provisional
PPMGSSAAAVLTKPPFRPLNWKPPDISVERRADGSIVIKSRHPLGPYPRSIPHLLAKWAAEAPDRPWLAQ
REPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYS
LMSHDHAKLKHLFDLVKPRVVFAQSGAPFARALAALDLLDVTVVHVTGPGEGIASIAFADLAATPPTAAV
AAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGGN
ANFNGLLWGGGTLYIDDGKPLPGMFEETIRNLREISPTVYGNVPAGYAMLAEAMEKDDALRRSFFKNLRL
MAYGGATLSDDLYERMQALAVRTTGHRIPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPV
GDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVDPDDPEKGLIFDGRVAEDFKLSTGTWV
SVGTLRPDAVAACSPVIHDAVVAGQDRAFIGLLAWPNPAACRQLAGDPDAAPEDVVKHPAVLAILREGLS
AHNAEAGGSSSRIARALLMTEPPSIDAGEITDKGYINQRAVLERRAALVERLYAEPPGPDVIVL
>gnl|CDD|237145 PRK12583, PRK12583, acyl-CoA synthetase; Provisional
MPQPSYYQGGGDKPLLTQTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPG
DRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELL
PGLAEGQPGALACERLPELRGVVSLAPAPPPGFLAWHELQARGETVSREALAERQASLDRDDPINIQYTS
GTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPNEAFDP
LATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAY
GMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEAT
AESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYG
EEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEELALPV
>gnl|CDD|237146 PRK12584, PRK12584, flagellin A; Reviewed
MAFQVNTNINALNAHVQSALTQNALKTSLEKLSSGLRINKAADDASGMTIADSLRSQASSLGQAIANTND
GMGIIQVADKAMDEQLKILDTIKVKATQAAQDGQTTESRKAIQSDIVRLIQGLDNIGNTTTYNGQALLSG
QFTNKEFQVGAYSNQSIKASIGSTTSDKIGQVRIATGALITASGDISLTFKQVDGVNDVTLESVKVSSSA
GTGIGVLAEVINKNSDRTGVKAYASVITTSDVAVQSGSLSNLTLNGIHIGNIADIKKNDSDGRLVAAINA
VTSETGVEAYTDQKGRLNLRSIDGRGIEIKTDSVSNGPSALTMVNGGQDLTKGSTNYGRLSLTRLDARDI
NVVSASDSQHLGFSAIGFGESQVAETTVNLRDVTGNFNANVKSASGANYNAVIASGNQSLGSGVTTLRGA
MVVMDIAESAMKMLDKVRSDLGSVQNQMISTVNNISITQVNVKAAESQIRDVDFAEESANFNKNNILAQS
GSYAMSQANTVQQNILRLLT
>gnl|CDD|183610 PRK12585, PRK12585, putative monovalent cation/H+ antiporter subunit G; Reviewed
MNVIIEIIISIMILIGGLLSILAAIGVIRLPDVYTRTHAAGISNTFGVSLLLFATVGYFFHSGEGFNARV
LLAVLFIFLTTPVASHLINRAAYDTGVPLAIRIRDQLRSVKKDDIKKKKSLIIRQEQIEKARQEREELEE
RMEWERREEKIDEREDQEEQEREREEQTIEEQSDDSEHEIIEQDESETESDDDKTEK
>gnl|CDD|237147 PRK12586, PRK12586, Na+/H+ antiporter subunit G
MEITKEIFSLIAAIMILLGSIIALISAIGIVKFQDVFLRSHAATKSSTLSVLLTLIGVLIYFIVNTGFFS
VRLLLSLVFINLTSPVGMHLIARAAYRNGAYMYRKNDAHTHASILLSSNEQNSTEALQLRAKKREEHRKK
WYQND
>gnl|CDD|183612 PRK12587, PRK12587, putative monovalent cation/H+ antiporter subunit G; Reviewed
MIKIILISLALIFVIIGALISALAAIGLLRLEDVYSRAHAAGKASTLGAMSLLFGTFLYFIATQGYVNMQ
LIVGIIFVLITGPLSSHMIMKAAYNIKTPYTKKTKVDEISEDLKDTKL
>gnl|CDD|183613 PRK12592, PRK12592, putative monovalent cation/H+ antiporter subunit G; Reviewed
MTLQLFTDIVSLVFILSGAFLSFSASIGLIRFRDTMSRVHAITKPQTTGLILTVVGAIIRVLGHEDFDQS
QRGDLGVLVLLVLFALLTSPVTAQRVGRVSRREGLYGAKDTMSRNQAPAERKPKKS
>gnl|CDD|183614 PRK12595, PRK12595, bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
MMNEELEQLRKEIDEINLQLLELLSKRGELVQEIGEEKTKQGTKRYDPVREREMLDMIAENNEGPFEDST
IQHLFKEIFKASLELQEDDNRKALLVSRKKKPEDTIVDVKGEVIGDGNQSFIFGPCSVESYEQVEAVAKA
LKAKGLKLLRGGAFKPRTSPYDFQGLGVEGLKILKQVADEYGLAVISEIVNPADVEVALDYVDVIQIGAR
NMQNFELLKAAGRVNKPVLLKRGLSATIEEFIYAAEYIMSQGNGQIILCERGIRTYEKATRNTLDISAVP
ILKQETHLPVMVDVTHSTGRRDLLLPTAKAALAIGADGVMAEVHPDPAVALSDSAQQMDIPEFDRFLDEL
KPLANKLNAK
>gnl|CDD|105779 PRK12596, PRK12596, putative monovalent cation/H+ antiporter subunit E; Reviewed
MKKILPYPLLFVSLVLFWLLLNSFTRAQFILGLVIAFGACRVMMALEPQKNHIRSPRMMIWLLYAASIDV
LRSNIAVVRLILSPGRQRHPGFVVIPLELQNRTALAVLACMITASPGTAWVDYNAARGILTIHVLDLEDA
ETWRHLIKERYERPLIEIFGAVDIVEGEKSA
>gnl|CDD|237148 PRK12599, PRK12599, putative monovalent cation/H+ antiporter subunit F; Reviewed
MTLLEDAFLIAAVLLVLALILSLYRVILGPTLPDRVVALDTLNTITVGIIAVLAAATGRPLYLDIAIVYA
LLSFLGTVAIAKYLVGRGGVL
>gnl|CDD|183617 PRK12600, PRK12600, Na(+)/H(+) antiporter subunit F1
MFNIILSIALIIVAISMLLMLIRVIKGPTLADRVVALDAIGINLIAIIALFSILLDTKAYLEVILLIGIL
AFIGTAAFSKFIEKGKVIERDRNH
>gnl|CDD|183618 PRK12603, PRK12603, putative monovalent cation/H+ antiporter subunit F; Reviewed
MMLVFSIFVLLACMGAMLIYVATSRTIYDKILAANLFGTYSVVLIVVLGVINDAQSLFIDVSLVYACIGL
VSAIGFMKFFLHNSFG
>gnl|CDD|183619 PRK12604, PRK12604, putative monovalent cation/H+ antiporter subunit F; Reviewed
MIGINIYLALIAIATLLSMYRVFRGPTTVDRLVAVDIMTTITTGLMVLFALYYKRMIFLDVALVYAILAF
VGVIAFARYLEGGL
>gnl|CDD|237149 PRK12606, PRK12606, GTP cyclohydrolase I; Reviewed
CGVHDQPPAEIRRGRRFDPPALEAAVRELLEALGEDPDREGLLDTPQRVAKAMQYLCDGYEQDPAEALGA
LFDSDNDEMVIVRDIELYSLCEHHLLPFIGVAHVAYLPGGKVLGLSKIARIVDMFARRLQIQENLTRQIA
TAVVTVTQARGAAVVIEAEHLCMMMRGVRKQNSRMITSVMLGAFRDSAQTRNEFLRLIGRS
>gnl|CDD|183621 PRK12607, PRK12607, phosphoribosylaminoimidazole-succinocarboxamide synthase; Provisional
AMLPRTLTEFNFPELPNVYRGKVRDNYDLPDGRRVMVATDRISAFDRVLPAIPYKGQVLNQTAAFWFEAT
KDICPNHVLAVPDPNVVVGKRCEPFPVEMVVRGYLAGSTWRLYKAGKREMYGVTLPDGLRENQKLPEPII
TPTTKAEEGGHDEPISPEEILAQGLLTPEDWDELSKYALALFARGQEMAAERGLILVDTKYEFGKDADGR
IVLIDEIHTPDSSRYWYADGYEERFAAGEPQEQLDKEFVRQWLIERCGPYGQEIPEIPDEVIVSVSERYI
ELYEKITGETFVPDSGSPPLARIRKNLAAYLAR
>gnl|CDD|237150 PRK12608, PRK12608, transcription termination factor Rho; Provisional
MATKTLELPTLQKQSTEEVLGVLEILGDGFGFLRSARRNYLPSPDDVFVPPALIRRFNLRTGDVVEGVAR
PRERYRVLVRVDSVNGTDPEKLARRPHFDDLTPLHPRERLRLETGSDDLSMRVVDLVAPIGKGQRGLIVA
PPRAGKTVLLQQIAAAVAANHPEVHLMVLLIDERPEEVTDMRRSVKGEVYASTFDRPPDEHIRVAELVLE
RAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGRTLSGGVDARALQRPKRLFGAARNIEEGGSLTIIAT
ALVDTGSRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKSGTRREELLLDSKELEKVRRLRRALA
SRKPVEAMEALLEKLRETPDNAEFLNSVQP
>gnl|CDD|237151 PRK12612, PRK12612, putative monovalent cation/H+ antiporter subunit F; Reviewed
DLLIISEIFLIIILLVILLALVLIIRTKDILTRLVISDMVFYAMALILLCLGLYNGTSIYYDIALAAGLL
GFLGTIAYARIISGGRR
>gnl|CDD|171609 PRK12613, PRK12613, galactose-6-phosphate isomerase subunit LacA; Provisional
MAIILGADAHGNALKELIKSFLQEEGYDIIDVTDINSDFIDNTLAVAKAVNEAEGRLGIMVDAYGAGPFM
VATKLKGMVAAEVSDERSAYMTRGHNNARMITMGAEIVGPELAKNIAKGFVTGPYDGGRHQIRVDMLNKM
A
>gnl|CDD|171610 PRK12615, PRK12615, galactose-6-phosphate isomerase subunit LacB; Reviewed
MKIAIGCDHIVTNEKMAVSDFLKSKGYDVIDCGTYDHTRTHYPIFGKKVGEAVVNGQADLGVCICGTGVG
INNAVNKVPGIRSALVRDMTTALYAKEELNANVIGFGGKITGELLMCDIIDAFIKAEYKETEENKKLIAK
IAHLESHHANQEDPDFFTEFLEKWDRGEYHD
>gnl|CDD|183624 PRK12616, PRK12616, bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase
MSMHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENSWDHQVFPIDTDTIRAQLSTIV
DGIGVDAMKTGMLPTVDIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITP
NLFEAGQLSGMGEIKTVEQMKEAAKKIHELGAQYVVITGGGKLKHEKAVDVLYDGETAEVLESEMIDTPY
THGAGCTFSAAVTAELAKGSEVKEAIYAAKEFITAAIKESFPLNQYVGPTKHSALRLSGK
>gnl|CDD|183625 PRK12617, flgA, flagellar basal body P-ring formation protein FlgA
MRLLLLVILLAAAPAWAQSYQSVDSIRAAALATVGPDAEAEATLDPGLRMPACPIALQAQPTGTNTVEVA
CPQPAGWRLFVPLKVRRNQDVLVLRRGITAGETISLADISIEKRDAARIVGAVLADPVAAVGKTARRILP
AGSLLSANDLVSQRLVRRGDTVPLVSRNGGLEVRMSGRALSDAGENERVSVENSSSRRVVQGIVEASGTV
VVSR
>gnl|CDD|183626 PRK12618, flgA, flagellar basal body P-ring formation protein FlgA
MMRLVLLLLLLLLAQPAAAETVVAARTIRALTVIGAEDLALKPGDTPGALTDPAQAIGQEARVTLYAGRP
IRAADLGPPAIVDRNQLVPLAYRLGGLEIRTEGRALSRGGVGDEIRVMNLSSRTTVSGRIAADGSVIVGP
N
>gnl|CDD|183627 PRK12619, flgB, flagellar basal body rod protein FlgB; Provisional
MAINLDSYFGIHAKALIARDQRASVLANNIANVNTPNFKARDVDFNEVLTATMAGNSQQLRVTSDQHIST
NADFMTHLKYRMTHHASLDGNTVDKDMETTEFARNALNYQASLSFLNGKIKSMLTALKGE
>gnl|CDD|183628 PRK12620, flgB, flagellar basal body rod protein FlgB; Provisional
MSSPFTSFLGVHGDALTLREQRMKLIASNLSNVDTPGYKAKDLNFEAALKSAQGEQDGGLMQTTDAKHYE
VGGGGLNPFQITRESDQPSLDGNTVDPDAERAAYGRAALEYRASLSFLESKVRSMLTAITGQ
>gnl|CDD|171613 PRK12621, flgB, flagellar basal body rod protein FlgB; Provisional
MKSLFESHINLVGKVMDMQLQRQNVVMSNLANVNTPGYKPRELEFEKELQAALGLDAKGKMTRTEKNHLP
AVFDPEGFEPEWSKAFKPRVVHGEDRVDLDKEMAKMAKNTLQYNALATVIKKNFEGLKTIIMEGQK
>gnl|CDD|183629 PRK12622, flgB, flagellar basal body rod protein FlgB; Provisional
MNIFERSVDLSHRYLDVLSLRQSVIADNIANVDTPNFKRSKVTFESELERAILNEDKNDLSLIRGNDKHL
SGFKELGYLDVKPHRMLDHLSTLNNNGNNVDIDSEMKALVQNQMMYHLFTNIQAHHFKSVNIVIK
>gnl|CDD|183630 PRK12623, flgB, flagellar basal body rod protein FlgB; Provisional
MRIESISSDQLVYDLLKKGLDASSYRGKVISNNIANVNTKGYKRHYVTFEENLKNNLDNLELKTTNEKHI
NDGVEFGQIKEKVDESTSMRTDGNNVDIDNEMVNQAANTLMYNALITQLNNRLATTRYVIN
>gnl|CDD|139107 PRK12624, flgB, flagellar basal body rod protein FlgB; Provisional
MFEKTHFMKTQDLLERGMNNSIQKRKVISDNIANADVPHFKRSEVIFESMIKRAIESEKIEKEKEVPTQI
SDERHIQFFKPLDYREVQPKTNLDYLTTMRADGNNVDVEKEVVEASNSQMQYMLMIERLNQNYRLLKQVM
RMA
>gnl|CDD|183632 PRK12626, flgB, flagellar basal body rod protein FlgB; Provisional
MLDKLDAEFAFGRQALDVRAYRQELLSSNIANADTPGYRARDVDFASTLARALKQTDGGAAASNAAQLPM
AQPAGVTSGMSMASTAPGHMAGNVKLIPTGGPSDDYGRAQYRMPLQPALDGNTVDLDTERVQFADNALHY
EAGMTVMTQQIKTMIAAITSNS
>gnl|CDD|237152 PRK12627, flgB, FlgB family protein
MFEKLEIFRMASAMARHAGERQAVVARNVANADTPGYRARDLADFAESYRAEGTTGMRATRPGHLNGAAA
GAADPVVTDAGGPASPNGNSVSLEEEMLRAVEAKRQHDRALAIYKSSMSLLRTSLGRS
>gnl|CDD|79089 PRK12628, flgC, flagellar basal body rod protein FlgC; Provisional
MSLNAIFDIAASAMTAETVRLTTSAGNMSNANVEAGSPDEVYQAKYPVFKSVQENANQWMGEQIKAGVKL
DGIYESDAEPHRRYDPNSPIADKDGFVYTSNINYVEEMANIISASRSYQMNIELLNTTKQLMQRTLQLGE
>gnl|CDD|183634 PRK12629, flgC, flagellar basal body rod protein FlgC; Provisional
MSNLPIFDVAGSALHAQSVRLSTIASNLANADSVAGSAEATYKPIEPIFQAQQSRQDPSLTSVNVKEITT
TNAPPIRRYEPGHPLADADGYVFSPDVDPVSQMVNMISASRNYQAGVEMLNTAKELALATLTMGR
>gnl|CDD|183635 PRK12630, flgC, flagellar basal body rod protein FlgC; Provisional
MKAFDTMRISASGLSAERLRMDTIASNIANATTTRTADGGPYKRKIAVFQENLNKELNKKNGAYEKKLYG
VKAVGIVEDKSPFRKVYDPSHPDADEEGYVSMPNVNVLNEMADMMASTRSYEANVTAINAEKSMFSKALE
IGK
>gnl|CDD|183636 PRK12631, flgC, flagellar basal body rod protein FlgC; Provisional
MSLFNIFDVAGSGMSAQSVRLNTTASNIANADSVSSSVDKTYRARHPIFEAEMAKAQSQQQASQGVAVKG
IVESDKPLLKEYSPDHPMADADGFIYKPNVNVMEEMADMISASRSYQMNVQVAEAAKSMLQQTLRMGK
>gnl|CDD|183637 PRK12632, flgC, flagellar basal body rod protein FlgC; Provisional
MTDFSKSLSVSASGMRAQALRLRHVSENIANADTPGYRRKTVSFQEARDFDPGSGLVSTGPVRLDRSELP
RIYDPSHPLADETGYYDGSNVDLVVEIADAREAQRSYEANLRMFDQARQMSSSLLDLLRR
>gnl|CDD|183638 PRK12633, flgD, flagellar basal body rod modification protein; Provisional
MTTVNETTSQAGLALAQAGSNSAAQGIQDQFLTLLVTQLRNQDPLNPMENAELTSQLAQISTVEGINNLK
NTMLAISGQIDVSQSMDAVSMIGKGVLMPGDKVSLGTDPNDPAQRGATPFGIDLQGDATKVTVKVLDPSG
AVVRTMELGDLKTGVHTLQWDGNNDGGQPLADGKYSITVSASDADAKPVKAEALTYGQVKSVAYSTNGLR
LDLGLAGQISMLDVRKVIGA
>gnl|CDD|183639 PRK12634, flgD, flagellar basal body rod modification protein; Reviewed
MSTIASDLYKSLGLSTSSKTAKKEEALGQADFLKLMTEQLQHQDPLKPMENSAFLGQLAQFSTVQGIGDL
NTKVSNFSDSMSSDQVLKGAALVGHNVLVPSAQVAIDATGSAKGVVAATSAGFVNFEITDANGAFVKQIS
VPASAAGEVSFAWDGTDANGNRMAAGKYGVTATQTDTAGSKSKLSTYVQAPVDSVTIGSDGLYLNLTGLG
TSPLANVLRVS
>gnl|CDD|183640 PRK12636, flgG, flagellar basal body rod protein FlgG; Provisional
MLRSMYSGISGMKNFQTKLDVIGNNIANVNTYGFKKSRVTFKDMVSQTISGASGPTANRGGVNSKQVGLG
SQLGAIDTIHTQGSLQTTGRPLDLAISGDGFFRVGDGDNTAYTRAGNFYLDNEGNIVNADGLYLLGMNGG
RIQIPTDAQSFSIGADGTVSYVDAGGELQTAGQIGLATFANPDGLEKAGDNLYRETLNSGTPSAVVPGEG
GTGKIVSGALEMSNVDLAEEFTEMIVAQRGFQANTRIITTSDEILQELVNLKR
>gnl|CDD|183641 PRK12637, flgE, flagellar hook protein FlgE; Provisional
MGFGQGLSGLNAASQNLDVIGNNIANSGTVGFKSGAASFADVYASSRVGLGVKVSAINQRFTVGNISTTG
GEYDMAIDGGKGFFRLTDQSGGVFYSRNGEFMVDKNFYIVNAQGFRLTGYPAGGVGAQPVDLQLPQGNIA
PQATSTAGLQTNLNANAKVIDPNDTPAVDGTVELDGTTYRFTNAGGTFAWVAPAPLDGTYNGGDIVIAGG
AVTGDLASQPGYQPYKPLVAGIPFDPTNPLSYTDQVPTTVYDSLGNSHQMIQYFAKRPAVGTESVYEVYY
VLDGQPMQVNGGASQTLNFDTAGNLLNQPPTAQVTFANPGGNAAPADPLAITVSYNGVTQYGSDFAPKVV
QNGYSSGEFMGLSVGKDGSLVAKYTNGETQTIGTLVLANFNNVQGLQPVGNNAWVETSESGQATLGQPGT
NGLATIAGQALEASNVDMSRELVNMIVAQRTYQANAQTIKTQDEVMQVLMNMR
>gnl|CDD|183642 PRK12640, flgF, flagellar basal body rod protein FlgF; Reviewed
MDRALYTAMSGASQNLNQQAVVANNLANASTPGFRADLAQARAVPVFGEGLPTRVFALASTPGADFSPGP
LQTTGRPLDVALQGDGWLAVQAPDGSEAYTRNGSLQVDANGQLRTANGLPVLGDGGPIAVPPGAKITIGA
DGTISALPPGDPPNAVAEVGRLKLVNPPAAQLTRGDDGLFRTTDGAPAPADPTVRVMSGALEGSNVNAVE
EMVSMIALARQFEMQVKMMKTADENAQAANQLLRMS
>gnl|CDD|105809 PRK12641, flgF, flagellar basal-body rod protein FlgF
MENSIYKSMIAANKLLEKQAIIANNLANISTTGFKEKFILAIQNHNVKNLYNSDKKITKEYYNLSPGTLR
YTGRNLDLFIKDNGWLTIKDTNGQEAYTKNGHLKINSKRKLTVQNNEVIGNNGNIIIPKNINLKISSNGV
ITSIKNNHKHIVETKIGSLKLVQLPSQDLIQKENGLFYLKKNNEINKKHTKNIKHSSKIRVQSGMLEESN
VNASKNMIEMISNARQFEMQMKIISMCDQNTEYANQLININN
>gnl|CDD|237153 PRK12642, flgF, flagellar basal-body rod protein FlgF
MQSGLYVALSSQMALEKRLDTIADNVANVNTVGFRATEVKFDTVVSDTASKKVAFVSQGKSYLSTEAGPL
TKTGNPLDFAVKGDAWFSFDTPAGQVYTRDGRFTMTSTGELVSVTGYPVLDAGGAPIQLNPGGGEPTIGA
DGAIYQNGVQVGAIGLFEIDADAGLLRYGNSGVIPDKPPQPVVDRNSVGVVQGYLEGSNVNAMTEMTQLI
SVSRAFESVSSLMRQSESSVSEAIKTLGGSR
>gnl|CDD|139117 PRK12643, flgF, flagellar basal body rod protein FlgF; Reviewed
MDHAIYTAMGAARQSLELQAVTANNLANASTPGFRAQLAAMRAVPIDGPSLATRTMVTTSTPGVDISQGT
MNFSGRPLDVALQQDGYLAVQLPDGSEAYTRNGNIQISANGQMTVQGYPLMGDNGPIDVPPQAAVTIAAD
GTISALNAGDSPNTIAQLGQIKRVQATAGEMMHGDDGLFHLTPETQQARGAQLPNDPLVKPGEREHQWL
>gnl|CDD|237154 PRK12644, PRK12644, putative monovalent cation/H+ antiporter subunit A; Reviewed
MLALLLAHAVAALLAPLLVRRLGRRAFYVLALVPAAAFVWVLAQWPAVLAGGAPTEVVPWIPSLGLDLAF
RLDALAALMSLLVLGVGALVLLYCARYFDDDEPRLGRFAAELVAFAGAMFGLVTSDNLLLLYVFWELTTV
LSFLLIGHYAERAASRRAALQALLVTTAGGLAMLVGIIILGQAAGTYRLSELLADPPTGPAVSVAVVLIL
VGALSKSAIVPFHFWLPGAMAAPTPVSAYLHAAAMVKAGIYLVARLAPGFADVPVWRPTVLVLGLATMLL
GGWRALRQHDLKLILAYGTVSQLGFLTVLVGIGTRDAALAGLAMLLAHALFKAALFLVVGIIDHSTGTRD
IRKLSGLGRRQPVLAVVAALAAASMAGLPPLLGFVAKEAALEAVLHDGALGPAGPVVLAGIVLGSILTVA
YSLRFLWGAFARKPGAFPSVAVTEMHRPSPLFLAPPAVLAVLGLVLGLLPAPLDALLAPYADTVPAAGGE
PYHLALWHGFTLPLLLSAVVLAAGAALFWARSRVERLQARVPALGNADRAYDATLRALDDLSVRLTGSTQ
RGSLPFYLGVILVTLVVVPGAALALGTRWPPDVRLWDSPAQVVVGLVIIAAALLATRARNRLAAVLLVGV
TGYGCAVIFALHGAPDLALTQFLVETITLVVFVLVLRRLPAEFSDRPLRKRRLVRAALAVAVGATVTVLA
VFAMAARVAEPISLLFPDLAYEFGHGKNVVNVLLVDIRAWDTMGEISVLLVAATGVASLVFRNRRFGRAP
RVSDAAGRAAGAAAKSAAATRRTWLRAGRTLAPERRSLVFEVVTRLLFPSMMVLSVYLLFAGHNAPGGGF
AGGLVAGLALVLRYLAGGRYELGEALPVDAGRLLGTGLFLSAGTALVSLLLGAPVLSSAIIEFDLPVLGD
VKLVTALFFDLGVYLIVVGLVLDVLRSLGAEIDRQIEERAQRARARARRLGRRAR
>gnl|CDD|237155 PRK12645, PRK12645, monovalent cation/H+ antiporter subunit A; Reviewed
MSLLHIAILLPFIFALLIPFLYKYFKRIHTGWFVLPVPVVLFIYFLSLIPTTMSGNTVMKTLPWIPSLGI
NFTLYVDGLSLLFALLITGIGSLVVLYSIYYLSKKKEQLGNFYVYLLLFMGAMLGVVLSDNLIVLYLFWE
LTSISSFLLISYWYEREASRYGAQKSMLITVFGGLSMLGGFILLYIMTGSFSIREMIANADEIQNSPLFI
PAMILILLGAFTKSAQFPFYIWLPDAMEAPTPVSAYLHSATMVKAGIYLVARFTPIFAGSQVWFWTVTLV
GLITLFWGSLNAVKQTDLKGILAFSTVSQLGLIMSLLGIGAASLHYQGDDSKIYAAAITAAIFHLINHAT
FKGSLFMIVGIVDHETGTRDIRKLGGLMTIMPITFTIALIGALSMAGLPPFNGFLSKEMFFESMLNATEA
NLFSLDTWGVLFPVIAWVASVFTFVYSIIFIFKTFFGKYKPEQLPKKAHEAPIGMLISPIILASLVVVFG
LFPNILTNSIIEPAVSAILPTLIDGEDFDVHISLWHGFTPELLMTLGIIILGILLFLTFSKWVKLYQRFP
KKLTLNYLYDRSLDGLEKGSYKMTRSYMTGYLRDYLVYIFSALILLLGFVTIFSVAFSFNFKDVAPIRIY
EVVLVAVLLVAAFAILFAKSRLTSIIMLGAVGYTVALFFVFFRAPDLALTQLVIETISVALFLLCFYHLP
KLNRYEEKRSFKLTNALISIGVGLIVTLIALSAYSNRHFESISKYYIENVYDLAGGKNMVNVILVDFRGF
DTLFEISVLGIAGLGVYTMIKLRKKRGEEG
>gnl|CDD|183646 PRK12646, PRK12646, DUF4040 family protein
MSLVYLLIAILVIMAMILLTSKRRALAKYAGYIALVAPIISSIYFLIQIPSVAKLQYLSTSIPWMKTLDI
NLDLRLDGLSLMFSLIISLIGIAVFFYATQYLSSRKDNLPRFYFYLTLFMFSMIGIVLSDNTILMYVFWE
LTSVSSFLLISYWYNNGDSQFGAIQSFMITVFGGLALLVGFIMLYIMTGTNNITEILGQADHIKNHGLFI
PMIFMFLLGAFTKSAQFPFHIWLPRAMAAPTPVSAYLHSATMVKAGIFLLFRFTPLLGLSNMYIYIVTFV
GLITMLFGSITALKQWDLKGILAYSTISQLGMIMAMVGIGGGYAQHQQDAIASIYVFVLFAALFHLMNHA
IFKCALFMGVGIIDHEAGTRDIRILSGMRQLFPKMNLVMTIAALSMAGVPFLNGFLSKEMFLDALTQTGQ
LSQFSLISMIIIVFIGVIASIFTFTYALYMVKEVFWGKYDSKVFTKKNIHEPWLFSLPSLILMVLVPVIF
FVPNIFGKGIIVPALRSVSGGNHQVDQLAPHVSQWHGFNIPLLLTIIIILLGSVLAIKVDWKKVFTGKIR
QISISKSYEMVYRHFEKFSTKRFKRVMQNRLNQYIIMTLGIFMIIIGYGYIRIGLPKVHQLHVSEFGPLE
IILAIVTVTIGISLIFIRQRLTMVILNGVIGFVVTLFFIAMKAPDLALTQLVVETITTILFIVSFSRLPN
VPRSNANKKREIIKIIVSLLMALIVVSLIFITQQTDGLSSISDFYLKAYKLTGGKNIVNAILGDFRALDT
LFEGLVLIITGLGIYTLLNYKDRRGQDERE
>gnl|CDD|237156 PRK12647, PRK12647, putative monovalent cation/H+ antiporter subunit A; Reviewed
AALAAPWLHRLFGRNAGWLLALLPLALFLYFLSFIPEIAAGETVRGGYAWVPSLGVNLSFLLDGLSLTFA
LLITGIGTLIVLYAGGYLKGHPDLGRFYSYILLFMASMLGLVLSDNLITLFVFWELTSITSFLLIGFNHE
REAARRAALQALLVTGGGGLALLAGLILLGNVTGTYSLSELLASGDVIREHPLYLAILLLVLGGAFTKSA
QFPFHFWLPNAMEAPTPVSAYLHSATMVKAGIYLLARLNPVLGGTPLWQTILPLFGGLTMLTGALLAVRQ
TDLKLILAYSTVSALGTLVMLLGLGSELAIKAAVLFLVAHSLYKGALFMVAGIIDHETGTRDITKLGGLR
RAMPITAAAALLAALSMAGLPPLFGFLAKELIYEALLEAPLWSLILTVAAVLGNALMVAVAFLVGIKPFL
GKLVETPKHPHEAPVLMWLGPAVLAVLGLLFGLFPFFFHAALLSPAASAVLGEPVEVKLALWHGFNLPLL
LSLLTLLLGIGLYLLRARLRAAMAALDRAAGIGPDRGYDRFMDGLVRVAEWQTRVLQNGRLRNYLTVTFL
TAAALLGYTLVRYGEFPGDPSFPDVTFHEWALALIIVAGALATVTTRSRLTAIVSLGVQGFAVALIFILF
GAPDLAMTQFLIETLSVILLVLVLYRLPSFLDLSPPGQRLRDAAIALGCGVGMTLLLLAVTQVPFDDELG
DYFAAYSKPIAHGRNVVNVILVDFRALDTLGEIAVLAVAALGVYALLKLRAGRERRAAAND
>gnl|CDD|237157 PRK12648, PRK12648, putative monovalent cation/H+ antiporter subunit A; Reviewed
MSLLLLVLLPFLGALLAALLPRNARNAEAWLAGLVALAALVLLALLYPAVAAGEVIRAEIEWLPALGLNL
SLRLDGLAWLFALLILGIGLLVVLYARYYLSPADPVPRFFSFLLLFMGAMLGIVLSGNLILLVVFWELTS
LSSFLLIGYWHHRADARRGARMALTVTGAGGLALLAGVLLLGHIVGSYDLDVVLAAGDLIRAHPLYPPAL
VLILLGAFTKSAQFPFHFWLPHAMAAPTPVSAYLHSATMVKAGVFLLARLWPVLAGTEEWFWIVGGAGLI
TLLLGAYFALFQHDLKGLLAYSTISHLGLITLLLGLGSPLAAVAAIFHIINHATFKASLFMAAGIIDHET
GTRDMRRLSGLRRLMPITATLAMVAAAAMAGVPLLNGFLSKEMFFAETLDTHLLGSLDWLLPVAATLAGA
FSVAYSLRFIHDVFFGPPPDDLPKTPHEPPRWMRAPVELLVLLCLLVGIFPALTVGPLLAAAARAVLGGA
LPEYSLAIWHGFNLPLLMSLVALVGGVLLYLLLRRLFRLAARLPGPPLLRRLDGKRIFERVLVALSRWAR
RLTRRLGTGRLQRQLALLVLAALVAALLPLLTGGLLTGTRPLTPVDPVFALLWLLGIACALGAAWQAKHR
LAALILLGGAGLVVCLTFVWFSAPDLALTQLLVEVVTTVLLLLGLRWLPKRTPDESARLRRLRDLALAVV
AGLGVAALAYAVMTRPAPDSISDFFLENALPGGGGTNVVNVILVDFRGFDTFGEITVLGIAALTVYALLR
RFRPAPESIDLPGQQRAQDTAAGHPLVPAVLARLLLPLALLVSVYLFLRGHNLPGGGFIAGLVLAIALIL
QYMASGTRWVEARLRILPHRWIGLGLLIAALTGLGSWLFGYPFLTSAFGYVHLPLIGEVELASALLFDLG
VFLLVVGATLLILSALAHQSLRAHRSGAAPAAEEAEAE
>gnl|CDD|183649 PRK12649, PRK12649, putative monovalent cation/H+ antiporter subunit A; Reviewed
MDSFNAIVLAIFLPFILAWTVPVLEKVLKQRIGWFAAAIAFTSFALIAQVAPEVIHGTIITGSISWLPSA
GVEFSIYADGLAVLIGLIASGIGVIIMSYSNGYMSHKEDLPRYYQYLLLFMGSMIGMVFSGNTIQLFIFW
ELTSITSFMLIGYWRHRPESVYGATKSLLITAGGGLFMFAGFLLLHVITGTYDIATILQDSELIENIKGH
PLFLITLILIFIGAAAKSAQGPFYIWLPNAMEAPTPVSAFLHSATMVKAGVYLVARIHPIFSGTEAWFIL
VSGTGMITMVLAGFLAFRQTDIKAILAYSTISQLAYLMTMYGYTTYHEPGLGVAAATFHLLNHATFKACL
FLVAGIVAHEAATRDIRKLGGLRKEMPITFIVASIAALAMAGIPPLNGFLSKEMFYETSVEMGALIGGPF
TIIIPAVAVLGGVFTFAYSIKLIDGIFLGERTHDHLPHHIHEAPYVMLIPAAFLAGLVILFGLVPSIPIH
NIIEPATSGIVLETAHLHVKLWHGFTPALMMTIITFILGLLIYTKYDAIAAWQDRFNAKYPWISVNYYYD
AIVNNAKGNAHKFASFAQPGPIKLYIKATLLLMIALIFIPLYMLGGDLLPAGLNFDIPPYEAVLMLLMIV
AALAAALLPRYLPAVIALSALGYLVSLLFIYLKAPDLALTQILVETLSTIIFLLVIIKIPQKFKEKIPKG
KLLRDILISGVVSFGVLIVLLNATQGIVPPFESLSHYFIEKSVALTGGHNVVNVILVDFRGYDTLGEISV
LCLAALGVYNLIHSRGEKV
>gnl|CDD|237158 PRK12650, PRK12650, DUF4040 family protein
LLAVLALAALAVVLAPPLVRVLDRKAGWPLAAIFVAAAGLLLKELPPILDGDALTWSVTWIPDLLGNGVD
VNLALRADALSLFFALLALVIGAVVFIYSARYLPRKKGNTSFYLLMTAFMAAMLLLVLADDVVVLFVAWE
LVSLASFFLIARSGSGGEAGSIRTLILTFFGGLTLLAAVAIAATQTGTTSLSGILHSDVWAEKPGLTTVV
AVLIAVAAFTKSAQFPFHFWLPEAMAAITPVSAFLHAAAVVKAGIYLLLRFSPVFHDVAVWNWLLIIVGM
ITALMGAVFAVQKTDLKKLTAYSTVSQLGWIVATIGVGTPFALTAAVVHTLAHALFKSSLFMLIGVVDHQ
AGTRDIRRLGSLWRRMPFTFVSVTIAALSMAAVPPLFGFVSKEGMLTAFLEAPGGNAGVVLLLVGAALGA
VFTFAYSARLVLGAFVDGPRDMSHVKEAPVSLWLPAALPGALSLPLGLVPGLLDAPVSAAATAAAGEHAH
THLALWHGVNTPLLISLLVIVLGILGVLFRKPLWEPLESRPLAPFSGLDILDAVRDRIIAFGRFVGRMAD
SMSPRRHLVIPFLLLILLAGFGLIGVDGLPPRVGGIDRWIDLVLLAIIALGVIALVRTRTRLAAVVLVGV
VGVGVTLQMLTLGAPDVALTQLLVEALTVVVMMLVLRRQPRNFHREKTRRRRFAVLVAVLAGLATFLGVW
ALTGRHERSELAEWYLNNGPEITGGDNVVNTILVEFRALDTLGELSVLGMAGVVIAALLLSRPRSPFAPG
THPFRAPLGDSQLNSVPLRMLLRVLIPILILLSFALFWRGHNEPGGGFIAALVAGAGLMLLYLSAPRDKA
IFVRNPPLTLIGAGILVAVVTGLLGYLHGSFLYPIHGHVLGQHWTTSLIFDLGVYLAVLGMVSMAINLLG
GYLRPGTDYAALDYDPRDQPLPATPTVEPEEDGDTDWPEPVNPASDPSPVAN
>gnl|CDD|237159 PRK12651, PRK12651, Na+/H+ antiporter subunit E
MAFQLLLNIILAVLWLFLTGSFSLGNFIIGFILGLFVLFLFRRLLPARFYLRRIYKLIKLVPIFLKELIK
ANIDVAKIVLKPKLNIEPGIVAVPTDLKTDWEITLLANLITLTPGTLTLDVSDDRKKLYIHAIDVKDKEE
EIREIKDSFEKILLEVFE
>gnl|CDD|237160 PRK12652, PRK12652, monovalent cation/H+ antiporter subunit E
IMMAANRLLVPVADSVTVRQTVAYAVESAEEAAETPTVHLVAAASGRAVDPEGQDELAAAEELLERVEVW
ATEDLGDDASSVTIETALLGTDEYLFGPGDYAEVLIAYAEEHGIDRVVLDPEYNPGGTAPMLQPLERELA
RAGITYEEAPVERPTRRGRLVRAATLDKFAALFGASFGFYLLLGDPLYWFDLLTGAVTALIVAVLLAHVT
FSRPPSLRRTPLRVLRFLLYVPYLLWEIVKANVAIAYVILHPSLPIDPTMVRVRAAVRSGLPLTTLANSI
TLTPGTLTVDVDDRHLLVHSLTPSAREDLFDGGLERAVRFVFYGRAAARIPSPAERGDTPDLSVPSATID
SEIADGD
>gnl|CDD|183653 PRK12653, PRK12653, fructose-6-phosphate aldolase; Reviewed
MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLEVVLPQLHEAMGGQGRLFAQVMATTAEGMVN
DARKLRSIIADIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGG
SGIQTVTDLQQLLKMHAPQAKVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVDAAVAKFEQD
WQGAFGRTSI
>gnl|CDD|237161 PRK12654, PRK12654, monovalent cation/H+ antiporter subunit E
MLHALKYAPWLIGQIFVAGFSLIKDAFKGDKNFNPVVVRYPLRVTKDWQITALAASITATPGTLSLGLRE
PRKPGDPRILLVQAVFGSDPVSVLADIADMEERLAPSVKDIDHGVPGQGPYKELRPSDAEYPSREIADTA
QNPVSKEDREF
>gnl|CDD|183656 PRK12656, PRK12656, fructose-6-phosphate aldolase; Reviewed
MEFMLDTLNLEAIKKWHEILPLAGVTSNPSIAKKEGDIDFFERIREVREIIGDEASIHVQVVAQDYEGIL
KDAHEIRRQCGDDVYIKVPVTPAGLAAIKTLKAEGYHITATAIYTVFQGLLAIEAGADYLAPYYNRMENL
NIDSNAVIGQLAEAIDRENSDSKILAASFKNVAQVNKAFALGAQAVTAGPDVFEAAFAMPSIQKAVDDFA
DDWEAIHGRKSI
>gnl|CDD|183657 PRK12657, PRK12657, putative monovalent cation/H+ antiporter subunit F; Reviewed
MIQTITHIMIISALIIFGIALIICLFRLIKGPTTADRVVTFDTTSAVVMSIVGVLSVLMGTVSFLDSIML
IAIISFVSSVSISRFIGGGHVFNGNNKRNL
>gnl|CDD|183658 PRK12658, PRK12658, Na+/H+ antiporter subunit C
MEALFAILVGVFFAAAIYLMLSRHIIRILFGLALLGNAVNLLIFTAGRLTREVPPLIPAGADVLAEGAAN
PLPQALILTAIVIGFGLLAFLLVLAYRAYQDLGTDDTDEMRVAEPVEEPLPPLGY
>gnl|CDD|183659 PRK12659, PRK12659, Na+/H+ antiporter subunit C
MEFLLAIVVGGLYAAGIYMMLRRSIVKLVIGLILLGNAANLLIFTVGRLTRGAPPLVPEGATAPAGPVAD
PLPQALILTAIVIGFGVQAFAIVLIKRAYQVVGTDDLDEMKTTDTLS
>gnl|CDD|183660 PRK12660, PRK12660, putative monovalent cation/H+ antiporter subunit C; Reviewed
MNLILLLVIGFLVFIGTYMILSINLIRIVIGISIYTHAGNLIIMSMGGYGSSRSEPLITGGNQLFVDPLL
QAIVLTAIVIGFGMTAFLLVLVYRTYKVTKEDEIEGLRGEDDAK
>gnl|CDD|237162 PRK12661, PRK12661, putative monovalent cation/H+ antiporter subunit C; Reviewed
MNNFFLSLTIALLFGIGTFLILRRDMIKVIIGLSIISHAVNLLIVSSGVFEGTKVPIITEQGHEGSGSGI
IYNDNLTSGILAPIVTNGPETEFVDPLVQALVLTAIVIGLATTAFILILAYRIYEEYGTTDIRELRRLRG
>gnl|CDD|183662 PRK12662, PRK12662, putative monovalent cation/H+ antiporter subunit D; Reviewed
MKSHLPILQVIIPLLSAVVCALLKNRKLVKIISCIVVAVSFFIALVLFVQVYSGGVIKYSLGGWGPPYGI
ELRVDILSATMLVLVNFIAVMSVLYGIYPNRKEISVNKIPSFYSAFLLCLGGLLGILVSNDVFNIYVFLE
ISSISSYVLVAMGRDKKALVAAFEYLIIGTIGATFYLIGIGFLYAITGTLNMGDMFLIIQDLPTNRAIQI
GVLFIMVGLFIKAALFPFHKWLIQAYSEAPSFISVFFSGTSTKVMIYLIIRIVYDVFKANFVFTTLPFNN
VFMILAALAIVFGSVLAILSKDIKRIFAYSSISHIGYIILAVSLNTYYGLAAAVAYIVNHSIVKSALFMV
SGSISYHFGTTKLEDCLNLWKSMPKITLAFVLLSLSLIGMPPTSGFVAKWYILDAFIKSNAWIGLVVLLV
GSGLSVIYVWKIVEALYFESRMVESKANDKAFKTPNAMVLCIWIMAILSIIVGIYPIPLTLISEKIAFDL
LY
>gnl|CDD|237163 PRK12663, PRK12663, Na+/H+ antiporter subunit D
MMSNLLILPMLLPLLCGLVLVFLRNRDRLQRYLAIGTLTILTLISLALLIYVQRHGPITLDFGGWLPPFG
IQFTGDSLSALMVTTASFVATAIMAYGFGDIEHSGRRYGFPPFILLLMAGVIGSFLTGDLFNLYVWFEVM
LIASFVLITLGQEREQLRGAIKYVVLNLIGSWLFLLGIGLLYGTFGTLNMAHIAMRLNDMGDTATLTTIA
LLFLLAFGMKAALFPFMWLPAAYHTPNTEVAALFAALLTKVGIYALIRVFTLLFPQERELLHPLLATMAA
ITMVIGALGALAYKDIRRIAGYQVISSIGFILLGLALGTPAGINGAIFYLVHDMVVKTALFLIAGSLVRL
TGYRSLQYLGGLYRKEPLFGALFLILIFAIGGLPPFSGFWGKVLLVQGALDNGAYILLALMLITSLITMY
SLFRIFFLAYWGDKDGEEVNFKPIPLYRKLPLSILAVVVIAMGIAAEPLLNLTQDAAEGLLDPQAYIKSV
FPHGKGE
>gnl|CDD|237164 PRK12664, PRK12664, putative monovalent cation/H+ antiporter subunit D; Reviewed
MTMVLYAISLYGFFFGLIFIVLPLLLYDWSEPVYNLDLVLFIVLSFSLALIFLYILPIKNMRFSEMLCYL
LYYISSIAAISSSSLTLVVIGFEFMALSALMIIAAGCPGGNIGAFIHYACVHFFSGVLLLVGASGQAQNG
QYTGYCKLLFMLGLLINCACFPASSWVVDAYPAASNFGIIVLSLFTTKVAALVLLLFFSGEEILLFLGII
TAIYGIIFASLEQNIRRLLCYNVVGQMGLLIIAIGFSGSSGVAIGILILQIVLSVVYQTLLFMVADSVIN
RTRKFNLNRVGGLFKMSLEAMCCIIAILNMGAFPGTAGFVSKSLITHSIDTAGLTLVLYKKLFLICSLLL
FASVGLKFFWYAFISKSKSKPEAEKVYIGSKLSMIILVLICVVLGMFNSYLLFYNLPSFVYTLKSVALQL
GLILGTTLLFICLRKLFLGRINFKMDIDWIYRAFLPYVILLFNNFVLYVRSISASVLQNVLNSKTLLYFN
NGEKVKEVSSYNSLGFAISASLLFLMSIVLVVLCLNY
>gnl|CDD|237165 PRK12665, PRK12665, putative monovalent cation/H+ antiporter subunit D; Reviewed
MPVLAPLPVLLPLLAAALTLVLGRRPRAQRAISLLALSAVLVLSAVLLYLVDRDGTQAVQLGGWDAPIGI
TLVVDRLSALMLVVSSVVLLAVLVYAIGQGIRDGDEEQPVSIFLPTYLILVAGVSNAFLAGDLFNLYVGF
EILLVASYVLLTLGATAARVRAGVTYVMVSMVSSLLFLIGIALVYAATGTLNMADLAVRLDELPSGTRTA
LFAVLLVAFGIKAAVFPLSFWLPDSYPTAPAPVTAVFAGLLTKVGVYAIIRTHTLLFPGGGLDTLLMVVA
LLTMVVGILGAIAQSDIKRLLSFTLVSHIGYMVFGIALSTVAGLSGAIYYVAHHITVQTTLFLVVGLIER
QAGSSSLRRLGGLAKASPLLAVLFFVPALNLGGIPPFSGFIGKVALLEAGAEDGTWLAWALVAGGVVTSL
LTLYAVARVWTKAFWRAREDAPEGHLADARPAPLLDDSDDIEFADRDDVGRMPRGMVGATAALVAVGLAL
TVFAGPLFAISDRAATELLDRSIYITAVLGG
>gnl|CDD|237166 PRK12666, PRK12666, putative monovalent cation/H+ antiporter subunit D; Reviewed
MDWMNHLIILPILLPLLTAALLLLLDERRRRLKRAISLASTLLLLAVAVALLASAAAGGIGVYLLGNWPA
PFGIVLVLDRLSALMLLLTALLALAALLYALAGWDRAGPHFHALFQFQLMGLNGAFLTGDLFNLFVFFEV
LLAASYGLLLHGSGRARVRAGLHYVAINLVASSLFLIGVGLIYGVTGTLNMADLAQRIAQLPAADRALLE
AGAALLLVVFLIKAAMWPLNFWLPPAYAAASAPVAALFAIMTKVGIYAILRLSTLLFGPEAGASAGFGQD
WLLPGGLATLAFGAIGVLAAQRLRRLAAYLVLVSSGTLLAAIGLGNPAATAAALYYLVHSTLAAAALFLL
ADLVERQRGAAADRLAVTPELYDLDEEEEEEVGVAIPATMALLGLLFFICALALAGLPPLSGFLGKFALL
QALLNPPGAGAAWWLWALVLLSGLAALIALTRAGIRLFWASHERPVPRLRVLELAPVAGLLALCVALTVF
AGPVMRYTQATAAQLHDPAAYIRAVLAAGPAPGPPAGA
>gnl|CDD|237167 PRK12667, PRK12667, putative monovalent cation/H+ antiporter subunit D; Reviewed
LAMDIVGLTPILLVLFAFLLPLLSILLKGNRKIQKIYALLVSLITLILSILLFIQVYSSNKPIVYLFGGW
PAPIGIVYEVDLLGALLGLLTALVMFLILIYSYWYLEHESGPEWYYTLLLGLEAGMLGILLTGDAFNLFV
MLEVLSISAYGLVAYYRDRGDAVEAAIKYALIGAVGTTLYFLALAFLYATFGTLNMADLSAKIRGLSFPL
TGGLAGNPPLALGVALALALWAFTIKAAIFPNHFWLPDAHPAAPSPVSAMLSGLVVNVGAYAIIRFLYTI
FGISPSLIDFRAALSPILIILGAVSAIIGALMMVVQKDVKRLLAYSTISHMGYIFMGIGIGTQLGLAAAL
FHIINHAIAKSLLFLASGVFIHAAGTRDIDELAGLGRKMPIASFAFLIGALSLVGIPPLNGFFSKLLLFN
ALLESGFYLPALVLLIASAISLVGYFRAWYSLFFGKPKSGEEVEHKESPSMSVVILVLALAVLILGILAL
FLPEILDSLIEPAANQAMDPQKYIDAALTR
>gnl|CDD|237168 PRK12668, PRK12668, Na(+)/H(+) antiporter subunit D
MMLDFLPPALVFIAGALLVPFLPGRARKALLLLAPVLAVLAVLTVPEGTYLTVTFLGFDLVLGRVDKLSR
VFGLIFGIMAFIGVIYALHVKDPGQHVAALLYVGSALGAVFAGDLLTLFVFWELMAFTSTFLVWARGTKA
AVRAGFRYLLVHVLGGVLLLAGILLHYAETGSFAFGAIAGLGGTAAWLILIGFGVNAAFPPLHAWLPDAY
PEATVTGSVFLSAFTTKTAVYALARAFPGTELLIYIGAAMAVYGVFFALLENDLRRLLSYHIVSQVGYMV
AGIGIGTALAINGAVAHAFNHILYKGLLFMSAGAVLYRTGTEKLTELGGLYRSMPLTALFCLVGALSISA
FPLFSGFVSKSMIISAAGEDHYVWVWLLLLLASAGTFLHFGIKLPYFAFFGGDSGLRVKDAPRNMLVAMG
IAAFLCIAIGVYPQALYALLPYPVDYEPYTASHVLEQLQLLLFTALAFVLLRKPLLPKRGINLDVDWVYR
RAAFYFLRGLVRPLTRLDAAVDRAVVGAGLRLLMTSANPGSAFDLAAIDGVVDGVARRVLGPGGRLSRRL
PTGTTVLWLALLLAVVLVLLF
>gnl|CDD|183669 PRK12670, PRK12670, putative monovalent cation/H+ antiporter subunit G; Reviewed
MLPMLGMITLGLGIFLIVISVIGVIRFPDFYTRLHAAGITDSLGAALILIGLAMQCGFSVFTVKVLLLIC
LLWITSTTASYALARSAYKSKKKDDKDGG
>gnl|CDD|183670 PRK12671, PRK12671, putative monovalent cation/H+ antiporter subunit G; Reviewed
MNMAADIPLWAAILVAFFLVLGAGLTLIGTIGLVRLKSFYERLHAPTLGTSWGAGGILIASILYFSVLQS
RPVLHEVLIGVFVVVTTPVTLMLLSRAALYRDRSEDSSEKPSALESEQPE
>gnl|CDD|183671 PRK12672, PRK12672, putative monovalent cation/H+ antiporter subunit G; Reviewed
MMIEYLIYIFLAIGVTFNLLGSIALHRFPDVYTRLHGATKCTTFGTIFAVLAVVTHALYRLRLTGDPKYL
QMALHSFVALIALLLTNPVGAHAIARAAHLSGYLPKRAVVDAYEEKLR
>gnl|CDD|237169 PRK12674, PRK12674, putative monovalent cation/H+ antiporter subunit G; Reviewed
TILEIIVSVLLLLGAFFALVGAIGLVRLPDVYTRLHAATKATTLGLGLVLLASALYFAGGGNSLKALLII
LFLFLTAPVAAHLLARAAYRTGVPLWDRS
>gnl|CDD|171652 PRK12675, PRK12675, putative monovalent cation/H+ antiporter subunit G; Reviewed
MIELLFLLFGYSIMFFGALGLLRFPDVYTRLHAATKCDTGGAMGIILALALASDASLLIKLKFLVLAFLI
AMINPMVSHAIARGAYKMGIKPKVVVDMYAWDNP
>gnl|CDD|183673 PRK12676, PRK12676, bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase
MSIMEWLEICDDMAKEVEKAIMPLFGTPDAGETVGMGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISE
ELGEIVGNGPEYTVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNG
KPIKVSKTSELNESAVSIYGYRRGKERTVKLGRKVRRVRILGAIALELCYVASGRLDAFVDVRNYLRVTD
IAAGKLICEEAGGIVTDEDGNELKLPLNVTERTNLIAANGEELHKKILELLEG
>gnl|CDD|237171 PRK12678, PRK12678, transcription termination factor Rho; Provisional
GAPSDAAATATTDTAPRARGGGLAGMKLPELRALAKQLGIKGTSGMRKGELIAAIKEARGGGAAAAAATP
AAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRG
AARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRRE
QGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGG
NEREPELREDDVLVPVAGILDVLDNYAFVRTSGYLPGPNDVYVSMNQVRKNGLRKGDAVTGAVRAPREGE
QGNQRQKFNPLVRLDSVNGMSPEEAKKRPEFGKLTPLYPNERLRLETEPKKLTTRVIDLIMPIGKGQRGL
IVSPPKAGKTTILQNIANAITTNNPECHLMVVLVDERPEEVTDMQRSVKGEVIASTFDRPPSDHTTVAEL
AIERAKRLVELGKDVVVLLDSITRLGRAYNLAAPASGRILSGGVDSTALYPPKRFFGAARNIENGGSLTI
IATALVETGSKMDEVIFEEFKGTGNMELKLDRKLADKRIFPAVDVNASGTRKEELLLSPDELAIVHKLRR
VLSGLDSQQAIDLLISRLKKTKSNYEFLMQVSKTTPGAMDDD
>gnl|CDD|183676 PRK12679, cbl, HTH-type transcriptional regulator Cbl
MNFQQLKIIREAARQDYNLTEVANMLFTSQSGVSRHIRELEDELGIEIFIRRGKRLLGMTEPGKALLVIA
ERILNEASNVRRLADLFTNDTSGVLTIATTHTQARYSLPEVIKAFRELFPEVRLELIQGTPQEIATLLQN
GEADIGIASERLSNDPQLVAFPWFRWHHSLLVPHDHPLTQITPLTLESIAKWPLITYRQGITGRSRIDDA
FARKGLLADIVLSAQDSDVIKTYVALGLGIGLVAEQSSGEQEESNLIRLDTRHLFDANTVWLGLKRGQLQ
RNYVWRFLELCNAGLSVEDIKRQVMENSEEEIDYQI
>gnl|CDD|183677 PRK12680, PRK12680, LysR family transcriptional regulator
MTLTQLRYLVAIADAELNITLAAARVHATQPGLSKQLKQLEDELGFLLFVRKGRSLESVTPAGVEVIERA
RAVLSEANNIRTYAANQRRESQGQLTLTTTHTQARFVLPPAVAQIKQAYPQVSVHLQQAAESAALDLLGQ
GDADIAIVSTAGGEPSAGIAVPLYRWRRLVVVPRGHALDTPRRAPDMAALAEHPLISYESSTRPGSSLQR
AFAQLGLEPSIALTALDADLIKTYVRAGLGVGLLAEMAVNANDEDLRAWPAPAPIAECIAWAVLPRDRVL
RDYALELVHVLAPQIDKRDLRRVLDGNQAPNWPLPPTWESLTQTITS
>gnl|CDD|183678 PRK12681, cysB, HTH-type transcriptional regulator CysB
MKLQQLRYIVEVVNHNLNVSATAEGLYTSQPGISKQVRMLEDELGIQIFARSGKHLTQVTPAGEEIIRIA
REILSKVESIKSVAGEHTWPDKGSLYIATTHTQARYALPPVIKGFIERYPRVSLHMHQGSPTQIAEAAAK
GNADFAIATEALHLYDDLIMLPCYHWNRSVVVPPDHPLAKKKKLTIEELAQYPLVTYVFGFTGRSELDTA
FNRAGLTPRIVFTATDADVIKTYVRLGLGVGVIASMAVDPVADPDLVAIDASHLFSHSTTKIGFRRGTFL
RSYMYDFIERFAPHLTRDVVEKAVALRSNEEIEEMFKDIKLPVR
>gnl|CDD|183679 PRK12682, PRK12682, transcriptional regulator CysB-like protein; Reviewed
MNLQQLRFVREAVRRNLNLTEAAKALHTSQPGVSKAIIELEEELGIEIFIRHGKRLKGLTEPGKAVLDVI
ERILREVGNIKRIGDDFSNQDSGTLTIATTHTQARYVLPRVVAAFRKRYPKVNLSLHQGSPDEIARMVIS
GEADIGIATESLADDPDLATLPCYDWQHAVIVPPDHPLAQEERITLEDLAEYPLITYHPGFTGRSRIDRA
FAAAGLQPDIVLEAIDSDVIKTYVRLGLGVGIVAEMAYRPDRDGDLVALPAGHLFGPNTAWVALKRGAYL
RNYVYKFIELCAPHLSRELIKRAVQGDNN
>gnl|CDD|237172 PRK12683, PRK12683, transcriptional regulator CysB-like protein; Reviewed
MNFQQLRIIREAVRQNFNLTEVANALYTSQSGVSKQIKDLEDELGVEIFIRRGKRLTGLTEPGKELLQIV
ERMLLDAENLRRLAEQFADRDSGHLTVATTHTQARYALPKVVRQFKEVFPKVHLALRQGSPQEIAEMLLN
GEADIGIATEALDREPDLVSFPYYSWHHVVVVPKGHPLTGRENLTLEAIAEYPIITYDQGFTGRSRIDQA
FAEAGLVPDIVLTALDADVIKTYVELGMGVGIVAAMAYDPQRDTGLVALDTDHLFEANTTRVGLRRGAYL
RGYAYRFIELFAPHLSEAEIAAALREAVP
>gnl|CDD|237173 PRK12684, PRK12684, CysB family HTH-type transcriptional regulator
MNLHQLRFVREAVRQNFNLTEAAKALYTSQPGVSKAIIELEDELGVEIFTRHGKRLRGLTEPGRIILASV
ERILQEVENLKRVGKEFAAQDQGNLTIATTHTQARYALPAAIKEFKKRYPKVRLSILQGSPTQIAEMVLH
GQADLAIATEAIADYKELVSLPCYQWNHCVVVPPDHPLLERKPLTLEDLAQYPLITYDFAFAGRSKINKA
FALRGLKPDIVLEAIDADVIKTYVELGLGVGIVADMAFDPERDRNLRAIDAGHLFGSSTTRLGLRRGAYL
RGYVYTFIELFAPTLNRKLVEQALKGEAEAYEL
>gnl|CDD|183682 PRK12685, flgB, flagellar basal body rod protein FlgB; Reviewed
MAINLDAALGVHPQTLDFRVERSKVLASNLANAETPGYKARDLDFKAVMSQINAGMVPNQQYEAQYRVPY
QNSADGNTVELGKEQARYSQNAMDYQTSLTFLNMKISGLKSAIEGR
>gnl|CDD|183683 PRK12686, PRK12686, carbamate kinase; Reviewed
MKEKIVIALGGNAILQTEATAEAQQTAVREAAQHLVDLIEAGHDIVITHGNGPQVGNLLLQQAESNSNKV
PAMPLDTCVAMSQGMIGYWLQNALNNELTERGIDKPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAK
QQAEQPGSTFKEDAGRGYRRVVPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIRDDNTLKGVEAVI
DKDFASEKLAEQIDADLLIILTGVENVFINFNKPNQQKLDDITVAEAKQYIAEGQFAPGSMLPKVEAAID
FVESGEGKKAIITSLEQAKEALAGNAGTHITL
>gnl|CDD|105853 PRK12687, PRK12687, flagellin; Reviewed
MSSLLTNTSAMTALQTLRNVSSSLATTQNRISTGYRVATASDNSAYWSIATTMRSDNEALSAVSDALGLG
AATVDTMYTALTSVVGDSKSGLTALKAKLVAAREPGIDRTKIQSEITAIQNDLKNTAGLAVFNGENWLSV
DSSPSSYNATKSVVSSFTRVGGTVAIKTIDVNIAKLALYDTNGSSTTGILDKTVTVGTATASVSSIDIHL
LTDSATDLTKLDGYIGIVDQALGSVTQASADLGATKTRIDSNSNFVKSLRDAIDRGVGQLVDADMNAEST
RLQALQTQQQLGIQALSIANQGSQSILSLFK
>gnl|CDD|171664 PRK12688, PRK12688, flagellin; Reviewed
MSGIVLSASVRQNLLSLQSTADLLATTQSRLSTGKKVNSALDNPTNFFTAQSLDNRASDINNLLDGIGNG
VQILQAANTGITSLQKLIDSAKSIANQALQTVVGYSTKSNVSTTISGATADDLRGTTSYASATASSNVLY
DGAAGGATAATGATTLGGTAGSLAGTGATAGDGTTALTGTITLIATNGTTATGLLGNAQPADGDTLTVNG
KTITFRSGAAPASTAVPSGSGVSGNLVTDGNGNSTVYLGSATVNDLLSAIDLASGVQTVTISSGAATIAV
SASGGAVSAAAAGAVTLKSSTGADLSVTGKADLLKALGLTTATGAGNATVNANRTTSAGSLGALIQDGST
LNVDGKTITFKNAPIPGAASVPSGYGASGNVLTDGNGNSTVYLQGGTINDVLKAIDLATGVQTATIANGT
ATLATAAGQTASSVNASGQLKLSTGLNADLSITGTGNALSALGLAGNTGTATAFTAARTAGAGGISGKTL
TFTSFNGGTAVNVTFGDGTNGTVKTLAQLNTALQANNLTATIDATGKLTISASNDYASSTLGSTLAGGAI
GGTLTSTLTFSTASAPVADTVAQTTRANLVKQYNNILNQIDTTSQDASFNGVNLLNGDTLKLVFNETGKS
TLSIQGVTFNPAGLGLSALTSGTDFIDNAATNKVLANLNTASSTLRSQASALGSNLSIVQVRQDFSKNLI
NVLQTGSSNLTLADTNEEAANSQALSTRQSIAVSALSLANQSQQSVLQLLR
>gnl|CDD|183684 PRK12689, flgF, flagellar basal-body rod protein FlgF
MQNALLVGLSRQMALERQLDVVANNVANVNTNGFKARSSLFQEYLMPGAHEDNFQRPDRRVSYVQDRGTP
LDLSQGPLEQTKNPLDVAIDGDAFLAVQTPQGERYTRDGALEINAQGQLVTSDGYPVLGTGGPITFQPTD
TGIAISPDGTVSVNEGTATTDSIRGKLRLVTFANPQALKKEGANLYAATAPARPADTKARVEQGYIERSN
VNPVLEMTRMMEVNRTYTQVSSMLQQQSDLRKTAIERLADVPA
>gnl|CDD|183685 PRK12690, flgF, flagellar hook-basal body complex protein
MDNAGYTTLTRQSGLMREMQVVANNIANASTTGFRREGLVFSEYVKSLDSGEASLSMARASGRQTDLEQG
GLTQTGGQFDFAIEGEGFFMVETPQGERLTRAGSFTPNAEGELVDPDGNRLLDAGGAPIFIPPDARSVAV
GADGTLSADGQPLGQIGLYQPTDPLGLRREGGTRFRAEGGVEPAEGARLLQGFLEGSNVNPVSEIARMIE
VQRAYELGQSFLDREDERIRTTIRTLGQ
>gnl|CDD|139158 PRK12692, flgG, flagellar basal body rod protein FlgG; Reviewed
MRALAIAATGMSAQQLNLEVIANNIANLNTTGFKGARAEFTDLLYQAERQQGVPNQAGQEAVPEGAMLGL
GVRAAAIRNLHRQGSLAQTGNQLDLAVNGRGYFQVTSPNGEIQYTRAGSFNKNAAGQLVTMEGYAVDPAI
LIPQNTTQVTINESGQVFAKIDGQVAPQNLGQLTLANFANESGLEPLGNGLYRETPASGAPVVGNPGDVG
FGKIQQGYLEGSNVDPVKEITSLITAQRAFEMNSKVIQAADEMAGTVSKGIR
>gnl|CDD|183687 PRK12693, flgG, flagellar basal body rod protein FlgG; Provisional
MIRALWIAKTGLDAQQTNIDVISNNLANVNTTGFKKSRAVFEDLLYQTIRQPGAQSSQNTTLPSGLQVGT
GVRPVATQKIFTQGNLQQTGNSLDVAIEGQGFFQVQLPDGTIAYTRDGSFKLDQDGQLVTSGGYPLQPEI
TIPENATSITIGTDGTVSVTQAGQAAPQVVGQITLTDFINPAGLESIGENLYLETAASGAPIEGTPGLNG
LGTLRQGFLETSNVNVVEELVNMITGQRAYEMNSKAISTADQMLQYVNQLL
>gnl|CDD|237174 PRK12696, flgH, flagellar basal body L-ring protein; Reviewed
MRKRLLATSLAVLLLAGCSAARQQPSPAPPVTPPPAYVEPEEPADNPGSLFSDSEADLLFADSRARRVGD
IVLVKIVENSKAKNKADTTADKKSTNEYGVSAFFGQDSVAINPFNPLMGGGVGTDPLLKTSSTSKFSGTG
ETKRESTVTATIAARVVRVLPGGLMQVEGARETRVNDETQYIVVSGLVRPRDIGPDNSVMSTQLADARIE
YYGKGVLADKQRPGWFTRLMDNVWPF
>gnl|CDD|237175 PRK12697, flgH, flagellar basal body L-ring protein FlgH
LPSPARRARAAACAAAAAALAGCAQIPREPITQQPMTAQPPMPPSMQAPGSIYNPGYAGRPLFEDQRPRN
VGDILTIVIAENINATKSSGANTNRQGNTDFDVPTAGFLGGLFNKANLSAQGANKFAATGGASAANTFNG
TITVTVTNVLPNGNLVVSGEKQMLINQGNEFVRFSGVVNPNTISGANSVYSTQVADARIEYSAKGYINEA
ETMGWLQRFFLNIAPW
>gnl|CDD|183690 PRK12698, flgH, flagellar basal body L-ring protein FlgH
MARYILLALALLLSGCSSTPEKPIADDPYYAPVYPEAPPTKIAATGSIFQDSQANSLYSDIKAHKVGDII
TVVLKESTQAKKSANNEIKKGSDLSLDPIYAGGGNVSIGGVPLDLGYKDSMNTKRESDADQSNSLSGSIS
ANVMQVLPNGNLVIRGEKWISINNGDEFIRLTGIVRSQDITPDNTIDSTRVANARIQYSGTGTFADAQKV
GWLSQFFMSDWWPF
>gnl|CDD|105864 PRK12699, flgH, flagellar basal body L-ring protein; Reviewed
DGQCSMVLSFSARRRGRLLGPVLIVMLALVGGCSLPTPAPKVQQPMSARPPDLPLIPPSQGNGGIYQAAF
DYQGRGRYHPLFEDRRARQIGDTIIVLLNEKTNASKKSGSNAQRNGDISLSVPSFLGLPFKSIFQDLDLE
ASSSNKFDGKGESSSNNNFTGTITVTVVDILPNGNLLVSGEKQIGINQGHEFIRLSGVINPINVINNTVS
SIQVADARIEYRGNGYLDEAQTMGWLSRFFLSISPF
>gnl|CDD|139164 PRK12700, flgH, flagellar basal body L-ring protein; Reviewed
MMLKTVLRLPVCAALLALAAGCAMIPPEPVVTGPLTAPPPPPPQPSARPNGSIYQPSAYGNYPLFEDRRP
RNVGDIVTIVLEEKTNAAKGVATNTSRDGSATLGVAAAPRFMDGVINDKLDTDISGGNTANGTGKSSANN
TFTGTITTTVIGVLPNGNLQIAGEKQIAINRGSEYVRFSGVVDPRSITGSNTVSSTRVADARIEYRSKGV
MDEVQTMGWLQRFFLIASPF
>gnl|CDD|183691 PRK12701, flgH, flagellar basal body L-ring protein; Reviewed
MNRLNIAVSCLATALLFGCEALHPPAPGDNPDYAPTYPVTPDPKELRKVSGAIYSSETALPLFETPRARH
PGDILTVYLIEKTDAQKNATTTQRKNDTTKITNKLFLGRPISLGSGYSMDFDLDNQRQFNGEGRSIQNNK
LAGSISVTVAKVLANGNMVVQGEKWVRINQGNEFVRLSGIVRPQDIKADNTITSDRIANARISYGGTGQI
NNTNAQGWLSRILWGPLFPT
>gnl|CDD|105866 PRK12702, PRK12702, mannosyl-3-phosphoglycerate phosphatase; Reviewed
MRLVLSSLDGSLLDLEFNSYGAARQALAALERRSIPLVLYSLRTRAQLEHLCRQLRLEHPFICEDGSAIY
VPEHYFPAGILDEQWQHRPPYYVCALGLPYPCLRHILQQVRQDSHLDLIGFGDWTASELAAATGIPLEEA
ERAQKREYSEIFSYSGDPARLREAFAQQEANLTQHLLRLHQLHFSDLPQWYLTGWMQPTLAAEPNSLPGE
QAVQLLLDCYQRHLGPIKALGIGCSPPDLAFLRWSEQKVVLPSPIADSLWKEALRLGGPEVQPQWQLAQL
PGPEGWNEVVLMWLEETDHGDE
>gnl|CDD|237176 PRK12703, PRK12703, tRNA 2'-O-methylase; Reviewed
MITVLRINHRPFRDKRITTHVALTARAFGASSILVDERDETLENTIKKVVDNFGGSFEIKTGIEWKSEFK
KFHGIRVHLTMYGRPIEDVIDEIRESGKDVMVLVGSEKVPIEAYEIADYNVSVTNQPISEVSALAIFLDR
YFDGKELEKSFEGKINVVPMERGKLVKIIPDEDQCLDLLKKYGASDLLIRHVKTVYKLAMRIADCINADR
RLVAAGALLHDIGRTKTNGIDHAVAGAEILRKENIDDRVVSIVERHIGAGITSEEAQKLGLPVKDYVPET
IEEMIVAHADNLFAGDKRLNLKQVMDKYRKKGLHDAAERIKKLHEELSSICGRDLDEIT
>gnl|CDD|237177 PRK12704, PRK12704, phosphodiesterase; Provisional
MMLLIIILIALVALVVGAVIGYFVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLR
NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ
LQELERISGLTAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEILAQAIQRCAADHVAETT
VSVVNLPNDEMKGRIIGREGRNIRALETLTGVDLIIDDTPEAVILSGFDPIRREIARLALEKLVQDGRIH
PARIEEMVEKARKEVDEEIREEGEQAVFELGIHGLHPELIKLLGRLKYRTSYGQNVLQHSIEVAHLAGLM
AAELGLDVKLAKRAGLLHDIGKALDHEVEGSHVEIGAELAKKYKESPVVINAIAAHHGDEEPTSIEAVLV
AAADAISAARPGARRETLENYIKRLEKLEEIANSFEGVEKAYAIQAGREIRVIVKPDKVDDLQAVRLARD
IAKKIEEELQYPGQIKVTVIRETRAVEYAK
>gnl|CDD|237178 PRK12705, PRK12705, hypothetical protein; Provisional
FAMSILLVILLLLIGLLLGVLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQ
EARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTP
EQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRIASETASDLSVSVVPIPSDAMK
GRIIGREGRNIRAFEGLTGVDLIIDDTPEAVVISSFNPIRREIARLTLEKLLADGRIHPARIEEYVQKAN
EEFKQKIYEIGEEVLEELGIFDLKPGLVRLLGRLYFRTSYGQNVLSHSLEVAHLAGIIAAEIGLDPALAK
RAGLLHDIGKSIDRESDGNHVEIGAELARKFNEPDEVINAIASHHNKVNPETVYSVLVQIADALSAARPG
ARRESLDEYVQRLEELEQIAESFPGVEKAYAIQAGRELRVIVEPEKVSDAQATLLARDIAKKIENDLTYP
GPIKVTLIRETRAVEYAR
>gnl|CDD|183694 PRK12706, flgI, flagellar basal body P-ring protein; Provisional
MMKKLIMLIILNLSLFAQENQASKNFKNENSFNNQISESVKLKNIAEICPTNSNFLTGIGIVAGLADKGD
SLKQKDILNKILNEIGINEIDLTNIGSKNIALVNVSLQINGNMIKGSKHNVYIASMLDSKDLTNGILLKT
ELKDKEGKILATASGPIITNNKSKGTGYILNGATIHENQNYTHYNIILKKGDYTLINRISKILTSKNIKN
NIKSGNIIEIEVKNIGLLEEIENIEIETMPKVLIDEQNKIILASTNAEIGPLTFSIERDDQNLFNNKNNK
TIKIQIQKMKLNEFISKNSNNLSNKELIQIIKAAKKINKLNGELILEE
>gnl|CDD|139168 PRK12708, flgJ, peptidoglycan hydrolase; Reviewed
MAINNSSPYLPGLNAGDLIPQNLEQGALKLAAQQFEAQFLQTVLKQMRSASDVMADEDDPFNSKNQGMYR
DFYDAELASRLSSQRSMGLAEVMIKQLSSKLKSAPEVVALESQTLTTTAMQPALIVPPIAKDQK
>gnl|CDD|237179 PRK12709, flgJ, flagellar rod assembly protein/muramidase FlgJ; Provisional
MATFPKANDLTQRFALDVQGFDALRAQAKASPQAGAKMVAGQFDAMFTQMMLKSMRDATPSDGLFDSHTS
KMYTSMLDQQLAQQMSSKGIGVADALMKQLLRNAGVAAGAQGDAGAGGMGGLGGNEGGLAAMNALAKAYA
NAANNGALAGTRGYSAGSALTPPLKGNGGSPDADAFVDKLAAPAQAASAATGIPARFIVGQAALESGWGK
REIRGADGSTSYNVFGIKATKGWTGRTVSAVTTEYVNGKPRRVVAKFRAYDSYEHAMTDYANLLKNNPRY
AGVLNASRSVEGFAHGMQKAGYATDPHYAKKLISIMQQIG
>gnl|CDD|139170 PRK12710, flgJ, flagellar rod assembly protein/muramidase FlgJ; Provisional
MTIQSIATSDFQGLNELKVQAKNNAKEALPEVAKQFEGIFLQSMLKSMRMGQHFLDESSPFSGKNEATFQ
EMLDTQYASTIAESKGIGLAALLAKQLENSVGDKANNPVNSSTEVSNTKVTNSEESLSVVDDFVKSVWPT
AKQAASLIGLDPKLLVAQAALETGWGKFVTRDADGSSSNNLFNIKTGSHSEVESIQVKTTEYIADTPIKI
NASFRKYPSIEHSFHDYVSLIKGSERYQMALANAENPEIYVSELNKAGYATDPNYSNKILSIYHGDELNQ
AIQRCESSEQS
>gnl|CDD|237180 PRK12711, flgJ, flagellar assembly peptidoglycan hydrolase FlgJ
MRIAASPIDLNPSTKADPAKIDKVSRQLEGQFAQMLVKSMRDASSGDPMFPGENQMFREMYDQQMAKALT
DGKGLGLSAMISKQLSGDTGGPALNTALNTAKAAKAYSLVAGKRDASLPLPARDGAAAGITTSSVAAAAL
SAGNLSGIGMSQVLDLIAGRTGAGEAGSDDAAALSWPSANDRWSDVAASDAADANAAVNASAASTAAASL
GERTPEGFVAKIWTHAQKAARELGVDPRALVAQAALETGWGRRGIGNGGDSNNLFGIKATGWNGDKVTTG
THEYVNGVKTTETADFRAYGSAEESFADYVRLLKNNSRYQQALQAGTDIKGFARGLQQAGYATDPGYAAK
IAAIANGPTIDRAVAAIGNAAADLSNRYASTAEPAGLGTIRR
>gnl|CDD|139172 PRK12712, flgJ, flagellar rod assembly protein/muramidase FlgJ; Provisional
MTGATLSAQADLSQRFALDTQGFEALKHSARGGADAGTLQAAARQFEAVFTQMVLKSMRDATPQDGLFDN
EQSKLYMSMMDQQLAQQMSSRGIGLADVMVRQLARATGTQMPPGMNAAGGATAGSAADAEMARLLDGRGA
GAADADAGDLPAIGTIVPGQAWNPTAGLRQYQPQAYADQGQGEDRLGRLPDDAPAHVSAFVARMAGPAEA
ASRASGVPARLIVGQAALESGWGRREITHADGSTTFNVFGIKAGANWKGRVAEVTTTEYVDGQPQKVRAR
FRAYGSYDEACADYARLLTSNPRYAGVVSAASADEAAHGLQRAGYATDPAYGHKLVKIMKKVSA
>gnl|CDD|139173 PRK12713, flgJ, flagellar rod assembly protein/muramidase FlgJ; Provisional
MSFVSYTPRPGVQESVFDLGRLADLKRDAVKAPDGQRQQTEVARQFEALFLQMMLKRMREATPKEGLFDS
QQTEMLQGMADEQLALQLASPGIGLAQALLGQMQQGQPPVPAAAAAGGDAAAARALAGTAAPAPLVRDLR
GNYVQPDPAPRREVNALLDVLRSNRARDRAMAAAEGAPSHVVDFVSRMSRAANVAAQQSGVPARLILGQA
ALESGWGRRELRHEDGSTSYNLFGIKAGASWKGKVVNVMTTEYVDGVAQKLVQPFRAYSSYEESFSDYAR
LIGNSPRYEAVTQAGNEIEAARRIQEAGYATDPRYAEKLISIMGQLRTSVARADFSGGL
>gnl|CDD|183697 PRK12714, flgK, flagellar hook-associated protein FlgK; Provisional
MSIMSTGTSALIAFQRALSTVSHNVANINTEGYSRQRVEFATRTPTDMGYAFVGNGAKITDVGRVADQLA
ISRLLDSGGELSRLQQLSSLSNRVDALYSNTATNVAGLWSNFFDSTSALSSNASSTAERQSMLDSGNSLA
TRFKQLNGQMDSLSNEVNSGLTSSVDEVNRLTQQIAKINGTIGSSAQNAAPDLLDQRDALVSKLVGYTGG
TAVIQDGGFMNVFTAGGQALVVGTTASKLTTVADPYQPTKLQVAMQTQGQNVSLSPSSLGGQIGGLLEFR
SSVLEPTQAELGRLAVGMASSFNAGHSQGMDLYGAMGGNFFNIGSPTVAANPSNTGTASLSASFSNLSAV
DGQNVTLSFDGTNWKATRADTGSAVPMTGTGTAADPLVLNGVSMVVGGTPASGDKFLLQPTAGLAGSLSV
AITDPSRIAAATPVKATATLANQGTGKISDVKVTNAQNPALLTPSSIEFIDANQYTIDGAGPFAYTAGQT
ISANGWSFALDGAPKAGDTFGVGPTGAGSSDNGNAKLLAKVDDAKALNGGTVTLNGALSGLTTSVGSAAR
AANYSADAQKVINDQAQASRDSISGVNLDEEAANMLKLQQAYQAAAQMISTADTMFQAILGAVR
>gnl|CDD|183698 PRK12715, flgK, flagellar hook-associated protein FlgK; Provisional
MSILNIAYSGLNAFQRALDVTGNNIANFKTRGYSRQSIQFTPIASNRYAGSYIGAGVSVSSIYRNVDQFA
NAQVRSTLSYRTQYDAFYNQAIQIDKLLSQDGSSISVPLQTFFDSIGQLNSTPDNIATRGVVLKQSQLLA
QQFNSLQTKLEEYERNSTLQVTESVKIINRITKELAEVNGKLLGNNNIPELLDHRDELLKQLSGYTDLSI
FDQGDGTISVGIASGDMLVAGTQQRDLVVGTGKDSIFGTKIFLSSGGNNQVDITDRLTTGMLGGLIDYEK
NVLGQASQLIGQMAIGLAQTFNAQHKLGMDMNSQIGKDFFTDFNSPGQMLKRSTASADNSGTAVLSVNIS
DISQVKLSDYDLIISDTGANELRLIRKSDGTSTTLTWSSSPPAPPAGQVVIDGMTITVNDLSQLANNDHY
TLTPTRGAARDFALEIKDAYEIALASPVKTTASLNNTGQGQIILGPVLNTASVNKQFRIDFISDTQYNLV
NVTDSTTAGPFAFVPNTNNVIQIPDGITPSYSVVLSGIPKSGDQFTTDYNTGGFGDNRNGLILGNIQQNK
IFSNGSETLFDRYGSLLAEVGGRTNQAKTSFESADILHKQALDFQDSKSGVNLDEEGANLLVFQQAYQAA
GKLMEISNQIMNLLFDIMR
>gnl|CDD|171679 PRK12717, flgL, flagellar hook-associated protein 3
MRISTSQFYESSAANYQRNYSNLVKTQEQASSGIRIQTAADDPVGAARLLQLQQQQAMLDQYSGNITTIK
NSLTQEESTLTSINDTLQRARELAVSAGNGGLTDADRKAIASELKQIEAQLLGLMNSKDANGQYLFAGSK
SDTPPYVRNADGTYSYQGDQTQLSLQVGDTLNLAANDTGYSAFEQAVNTSRTQTTLTSPATDDGRVGLSN
GLVTSSVTYNAQFRAGEPYTLTFTSGTQFKITDASGNDVTSEASGGGKFDPGTEGGQTISFRGVDLELNV
NLKAGSGADADAALAGHSFTLQSKPDTFTATRSPGNTSTAQVTGATITDPAAYNSTFPSSGAVLKFTSAT
AYELYAQPVTADSKPISSGTLTGNTATAAGVTFTLSGTPAAGDQFSVQANTHQTQNILDTLSQLRKALST
PTDGDPAARQALRAALASALGNLASAIDQVDTARSSIGARGNALDIQGTTNESLSLANTTTQSSIRDSDP
AEATTRLTLQQTMLEASQLAFVKISQLSLFNQL
>gnl|CDD|79176 PRK12718, flgL, flagellar hook-associated protein FlgL; Provisional
MRLSTALIYQNGLNGVLNQEAAMARLQEQLSSGRRVLTPADDPLAAALAVNVSQTSSMNSNYDANRKQAE
QALGAQTNTLQSVVKNMQEMLKRVVEAGNGTMSDADRQALVIALKGAREELVGLANATDGNGQYLFSGYK
GFTQPYSFDAATGKVTYNGDLGQRGIQVDQSRLMSGGDVGSDIFNSVTSGTLAYIADAGAGNAGTGQYSA
VSFDGPRAGNYVGRDFRIEFTRDAVTDELQYSVLSDPPVVPPEQPLPANMPYSEGSVIDMNGVSIKLSGQ
PEAGDVFTVETPKSWKMGVQGDAANTGSATLTPVSLPDGLTGKNLSVAFLDDGAGGLLYSVTSTPPDPSL
PANVPVKPGDVIDIGGLKVKVDGQPAAGDTYAVTTPKSANVDVFDTLNDLIGALDTPISGDPQAAAALAN
TLATANKKLNLSLDNVLTVQASVGARLNELEALGNTGAQKGLSYVKQLSDLEDVNIYQATSDLLLRQVAL
QAASLALQRIQGNSLFSMGR
>gnl|CDD|183699 PRK12720, PRK12720, EscV/YscV/HrcV family type III secretion system export apparatus protein
GNRAQRWLSMCAGRQDIVLAVMLLVAVFMMILPLPTWMVDILIAINLMFSVILLMIAIYLRDPLEFSVFP
SLLLITTLYRLALTISTSRLVLLQHDAGEIVDAFGKFVVGGNLAVGLIVFTIITIVQFIVITKGSERVAE
VSARFSLDGMPGKQMSIDGDMRAGVIDADEARRLRQHVQKESRLLGAMDGAMKFVKGDAIAGIIVILVNI
IGGIIIGVMQHDMSASEAVNTYAVLSIGDGLCGQIPSLLISITAGIIVTRVPGEKRQNLANELSSQIGRQ
PQALWLAAVVLMLFALIPGFPFITFAFLAALVAAPAILLRRKKSVVSANGVEAGGSEEGPEGDSMVPGAC
PLMLRLAPTLHSADLIRDIDALRWFLFEDLGVPLPEVNIEVDPELTEKTLTVLLYQEPVLSLSLPPQALL
LLIGPDASLVGDSQTLPNGMGQICWLTKDQAEQAQGFGLDVFAGSQRISALLKCVLLRYMGEFIGVQETR
YLMDAMEKRYGELVKELQRQLPVGKIAEILQRLVSERVSIRDLRTIFGTLVEWAPREKDVVMLTEYVRIA
LRRHILRRFNHEGKWLPVLRIGEGIENLIRESIRQTSAGTYSALSSRHSTQILQLIEQALKQSQKLVLVT
SVDVRRFLRKIIERTLFDLPVLSWQELGDEAEIKVVGSIDLIGEE
>gnl|CDD|183700 PRK12721, PRK12721, EscU/YscU/HrcU family type III secretion system export apparatus switch protein
MSEKTEKPTEKKLRDARKKGQVVKSVEITSGVQLAALLLYFLLEGPSLVEAIIGLINSTIQLLNKPFLYA
LTQILGAVLEVLLRFLLVLGAGLIVATVGTGIAQVGPLLASKAIGPKAEKINPVSNAKQIFSLKSVFELC
KSLLKVVILSLIFAYLLHYYAPSFAYLPYCGAACGLPVVSTLIFWLWGGLLACYLVFGILDYSFQRYKIM
KQLKMSKDDVKQEYKDSEGDPEIKQKRRELQSEIQSGSLANNVKKSTAVVRNPTHIAVCLYYHPGETPLP
RVLEKGKDAQALHIVKLAERNGIPVVENIPLARALFKEVECGDYIPETLFEPVAALLRMVMDIDYQHST
>gnl|CDD|237181 PRK12722, PRK12722, flagellar transcriptional regulator FlhC
MSEKSVVQEARDIQLAMELITLGARLQVLESETQLSRERLIKLYKELRGVSPPKGMLPFSTDWFMTWEPN
IHSSLFYNIYQFLLKTGGCSGIEAVIKAYRLYLEQCPQAEEEPLLSLTRAWTLVRFVDSGMLQLSSCNCC
GGHFVTHAHDPVGSFVCGLCQPPSRAGKTRKLSAAAADIAPQLLDEQ
>gnl|CDD|183702 PRK12723, PRK12723, flagellar biosynthesis regulator FlhF; Provisional
MVQYFTERGPTYNEVIETIKKKYGKNARVMTYKTIPHGGILGLFSRDWVEVSGYVRYDIGQQQINVEDEK
RKILQSIKKEENSSIEDVLKEVKSLKNELAHKKEEINHPTILKIEDILRENDFSESYIKDINEFIKKEFS
LSDLDDYDKVRDSVIIYIAKTIKCSGSIIDNLKKRVFILVGPTGVGKTTTIAKLAAIYGINSDDKSLNIK
IITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKEEITQSKDFDLVLVDTIGKSPKDFMKLAEMKELL
NACGRDAEFHLAVSSTTKTSDVKEIFHQFSPFSYKTVIFTKLDETTCVGNLISLIYEMRKEVSYVTDGQI
VPHNISIAEPLTFIKKINGYRISDDAEFIRKLKSKSYY
>gnl|CDD|183703 PRK12724, PRK12724, flagellar biosynthesis regulator FlhF; Provisional
MEFAKIRGKSYQDCLMEMKMKYGSEATVISQTVVTEGGVMGTGLLAKKMIEIQIGIPEKQASREKIERKL
QDLKELLKQKSYTEPERKKTLQTLKPLSERLEEKESAIYEIESFELEEVITEPERPVGLSFEKELFEKNS
FLESETTIVRKEKDSPLQRLGERLVREGMSQSYVEEMASKLEERLSPVDQGRNHNVTERAVTYLEERVSV
DSDLFSGTGKNQRKVVFFVGPTGSGKTTSIAKLAAKYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGM
PFYPVKDIKKFKETLARDGSELILIDTAGYSHRNLEQLERMQSFYSCFGEKDSVENLLVLSSTSSYHHTL
TVLKAYESLNYRRILLTKLDEADFLGSFLELADTYSKSFTYLSVGQEVPFDILNATKNLMAECVVFPEKI
AELRGEVFTVTG
>gnl|CDD|183704 PRK12726, PRK12726, flagellar biosynthesis regulator FlhF; Provisional
MGKHLVEKMEIFKANSKREIHKKIRLVTNEPYKITDERVTKLGIFKKQYEVTAVIMSEVAIADGRMDFQE
TFQKSVVKNRPKTDDLLKKEKLLEMLAAGAELAQSTPLLEERKTQEEELSAMRLELAALNRELAVKMREE
REQNSDFVKFLKGRGISDTYVADFMQAGRKQFKQVETAHLDDITDWFVPYLSGKLAVEDSFDLSNHRIIS
LIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIVATSPAELEEAVQYM
TYVNCVDHILIDTVGRNYLAEESVSEISAYTDVVHPDLTCFTFSSGMKSADVMTILPKLAEIPIDGFIIT
KMDETTRIGDLYTVMQETNLPVLYMTDGQNITENIFRPKSRWLAERFVGTDRRQVLE
>gnl|CDD|237182 PRK12727, PRK12727, flagellar biosynthesis protein FlhF
MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEGIEIVAASNYDEELVQRALETARSDTPATAAAPA
PAPQAPTKPAAPVHAPLKLSANANMSQRQRVASAAEDMIAAMALRQPVSVPRQAPAAAPVRAASIPSPAA
QALAHAAAVRTAPRQEHALSAVPEQLFADFLTTAPVPRAPVQAPVVAAPAPVPAIAAALAAHAAYAQDDD
EQLDDDGFDLDDALPQILPPAALPPIVVAPAAPAALAAVAAAAPAPQNDEELKQLRGELALMRQMIEREM
NRLTDERLRGSPVRAQALELMDDYGFDAGLTRDVAMQIPADTELHRGRGLMLGLLSKRLPVAPVDPLERG
GVIALVGPTGAGKTTTIAKLAQRFAAQHAPRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESLL
DLLERLRDYKLVLIDTAGMGQRDRALAAQLNWLRAARQVTSLLVLPANAHFSDLDEVVRRFAHAKPQGVV
LTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLRLEDLRRAADKPCTPEHNHAVA
>gnl|CDD|237183 PRK12728, fliE, flagellar hook-basal body protein FliE; Provisional
MMINEISPNQKVFDQNGSNKTNKNNPAEAQKSFSDFLKEALNKVNELQVEADNSTEKLVKGEIVDLHDVM
IAAQKASISLQLTVQIRNKVVEAYQEIMRMQL
>gnl|CDD|183707 PRK12729, fliE, flagellar hook-basal body protein FliE; Provisional
MEINSNSSLWRIYNSGYSGNKPHPLSPKGDKVGVFRTEDRHYKDVKQPVSPDYVAESFSEAMKNALTSVN
DLQVEADELTQKMVFDPNSVDAHDVMIASEKARVALTFTKTIADGVVRAYRELTSLR
>gnl|CDD|183708 PRK12735, PRK12735, elongation factor Tu; Reviewed
MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEY
ETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDM
VDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAID
KPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVL
LRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGTIELPEGV
EMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE
>gnl|CDD|237184 PRK12736, PRK12736, elongation factor Tu; Reviewed
MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEY
ETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDL
VDDEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKP
FLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLR
GVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPEGTEM
VMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD
>gnl|CDD|183710 PRK12737, gatY, tagatose-bisphosphate aldolase subunit GatY
MYIISTKNMLKKAQAEGYAVPAFNIHNLETLQVVVETAAELRSPVILAGTPGTFSYAGTDYIVAIAEVAA
RKYNIPLALHLDHHEDLDDIKKKVRAGIRSVMIDGSHLSFEENIAIVKEVVEFCHRYDASVEAELGRLGG
QEDDLVVDEKDAMYTNPDAAAEFVERTGIDSLAVAIGTAHGLYKGEPKLDFERLAEIREKVSIPLVLHGA
SGVPDEDVKKAISLGICKVNVATELKIAFSDAVKKYFYENPKANDPRKYMTPGKAAMKEVVREKIKVCGS
EGKL
>gnl|CDD|183711 PRK12738, kbaY, tagatose-bisphosphate aldolase subunit KbaY
MSIISTKYLLQDAQANGYAVPAFNIHNAETIQAILEVCSEMRSPVILAGTPGTFKHIALEEIYALCSAYS
TTYNMPLALHLDHHESLDDIRRKVHAGVRSAMIDGSHFPFAENVKLVKSVVDFCHSQDCSVEAELGRLGG
VEDDMSVDAESAFLTDPQEAKRFVELTGVDSLAVAIGTAHGLYSKTPKIDFQRLAEIREVVDVPLVLHGA
SDVPDEFVRRTIELGVTKVNVATELKIAFAGAVKAWFAENPQGNDPRYYMRVGMDAMKEVVRNKINVCGS
ANRISA
>gnl|CDD|237186 PRK12740, PRK12740, elongation factor G-like protein EF-G2
VGHSGAGKTTLTEAILFYTGAIHRIGEVEDGTTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGH
VDFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLQEKL
GAPVVPLQLPIGEGDDFTGVVDLLSMKAYRYDEGGPSEEIEIPAELLDRAEEAREELLEALAEFDDELME
KYLEGEELSEEEIKAGLRKATLAGEIVPVFCGSALKNKGVQRLLDAVVDYLPSPLEVPPVDGEDGEEGAE
LAPDPDGPLVALVFKTMDDPFVGKLSLVRVYSGTLKKGDTLYNSGTGKKERVGRLYRMHGKQREEVDEAV
AGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEPVISLAIEPKDKGDEEKLSEALGKLAEEDPTLRVE
RDEETGQTILSGMGELHLDVALERLKREYGVEVETGPPQVPYRETIRKKAEGHGRHKKQSGGHGQFGDVW
LEVEPLPRGEGFEFVDKVVGGAVPRQYIPAVEKGVREALEKGVLAGYPVVDVKVTLTDGSYHSVDSSEMA
FKIAARLAFREALPKAKPVLLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILGMESRGGGDVVRAEVPLAE
MFGYATDLRSLTQGRGSFSMEFSHYEEVPGNVAEKVIA
>gnl|CDD|183714 PRK12742, PRK12742, SDR family oxidoreductase
MGAFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKDAAERLAQETGATAVQTDSADRDAVIDVV
RKSGALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEGGRIIIIGSVNGDRMPV
AGMAAYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDANPANGPMKDMMHSFMAIKRHGRPEEVA
GMVAWLAGPEASFVTGAMHTIDGAFGA
>gnl|CDD|237187 PRK12743, PRK12743, SDR family oxidoreductase
MAQVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQA
LDKLIQRLGRIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQGGRIINITS
VHEHTPLPGASAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVKPDSRPGIPLGR
PGDTHEIASLVAWLCSEGASYTTGQSLIVDGGFMLANPQFNSELRD
>gnl|CDD|183716 PRK12744, PRK12744, SDR family oxidoreductase
MADHSLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAEETVAAVKAAGAKAVAFQADL
TTAAAVEKLFDDAKAAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLNDNGK
IVTLVTSLLGAFTPFYSAYAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFFYPQEGAEAVAYHK
TAAALSPFSKTGLTDIEDIVPFIRFLVTDGWWITGQTILINGGYTTK
>gnl|CDD|237188 PRK12745, PRK12745, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
MRPVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELAATQQELRALGVEVIFFPADVADLSAHEAM
LDAAQAAWGRIDCLVNNAGVGVKVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEELPHR
SIVFVSSVNAIMVSPNRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTAKYDALIA
KGLVPMPRWGEPEDVARAVAALASGDLPYSTGQAIHVDGGLSIPRL
>gnl|CDD|183718 PRK12746, PRK12746, SDR family oxidoreductase
MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAADETIREIESNGGKAFLIEADLNSIDG
VKKLVEQLKNELQIRVGTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAEG
RVINISSAEVRLGFTGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDPEIRNF
ATNSSVFGRIGQVEDIADAVAFLASSDSRWVTGQIIDVSGGFCL
>gnl|CDD|183719 PRK12747, PRK12747, short chain dehydrogenase; Provisional
MLKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVE
ALYSSLDNELQNRTGSTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNSRI
INISSAATRISLPDFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQYAT
TISAFNRLGEVEDIADTAAFLASPDSRWVTGQLIDVSGGSCL
>gnl|CDD|237189 PRK12748, PRK12748, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
LPLMKKIALVTGASRLNGIGAAVCRRLAAKGIDIFFTYWSPYDKTMPWGMHDKEPVLLKEEIESYGVRCE
HMEIDLSQPYAPNRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQ
YDGKAGGRIINLTSGQSLGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGWITEELK
HHLVPKFPQGRVGEPVDAARLIAFLVSEEAKWITGQVIHSEGGFSR
>gnl|CDD|183721 PRK12749, PRK12749, quinate/shikimate dehydrogenase; Reviewed
MDVTAKYELIGLMAYPIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSFPGAIEGLKALKMRGTGVSMPN
KQLACEYVDELTPAAKLVGAINTIVNDDGYLRGYNTDGTGHIRAIKESGFDIKGKTMVLLGAGGASTAIG
AQGAIEGLKEIKLFNRRDEFFDKALAFAQRVNENTDCVVTVTDLADQQAFAEALASADILTNGTKVGMKP
LENESLVNDISLLHPGLLVTECVYNPHMTKLLQQAQQAGCKTIDGYGMLLWQGAEQFTLWTGKDFPLEYV
KQVMGFGA
>gnl|CDD|183722 PRK12750, cpxP, periplasmic repressor CpxP; Reviewed
MKLAKKLVLAAVVLPLTLGTASAFAFGGKGDHKGGDGECGMGMDRGIMRQLDLTDAQKEQLKEMREANRA
EMKAKYSGNREQSHAEMKAHHAKVQALVLADDFDEAAANDLAKQMVEKQVERRVKMLEKRHQMLSILTPE
QKAKFQELQQERMQECQDKMHKRMKKHASN
>gnl|CDD|171704 PRK12751, cpxP, periplasmic stress adaptor protein CpxP; Reviewed
MRKVTTLVMASMFVLGSSAAFAADNTKVTEGYHGDGKMMMNKKGDRGHHNMFDGINLTEQQRQQMRDLMR
QSHQSQPRLDLEDREAMHKLITADKFDEAAVRAQAEKMSQNQIERHVEMAKVRNQMYNLLTPEQKEALNK
KHQERIEKLQQKPAAQPSSAQK
>gnl|CDD|237190 PRK12755, PRK12755, phospho-2-dehydro-3-deoxyheptonate aldolase; Provisional
MQKDAINNVRITAEQPLITPEELKAELPLSEAAQAQVAASRQAIADILHGRDDRLLVVVGPCSIHDPEAA
LEYARRLKALADELSDRLLIVMRVYFEKPRTTVGWKGLINDPHLDGSFDIEEGLRIARKLLLDLVELGLP
LATEALDPISPQYLGDLISWGAIGARTTESQTHREMASGLSMPVGFKNGTDGSLKVAINAIRAAAQPHRF
LGINQEGQVALLETRGNPDGHVILRGGKKGPNYDAASVAACEAQLEKAGLRPRLMIDCSHANSGKDYRRQ
PAVAEDVVAQIAAGNRSIIGVMIESHLEEGNQSSPPLSELKYGVSITDACIGWETTEALLRELAQALRAR
RAA
>gnl|CDD|183726 PRK12756, PRK12756, Trp-sensitive 3-deoxy-7-phosphoheptulonate synthase AroH
MNKTDELRTARIESLITPAELASEYPITPDVADHVTDSRRRIEKILNGEDPRLLVIIGPCSIHDTDAALD
YATRLAALREQYQDRLEIVMRTYFEKPRTVVGWKGLISDPDLDGSYRVNHGLELARKLLLQINELGLPTA
TEFLDMVTGQYIADLISWGAIGARTTESQIHREMASALSCPVGFKNGTDGNTRIAIDAIRAARASHMFLS
PDKDGQMTIYQTSGNPYGHIIMRGGKKPNYHAEDIAAACDTLREFDLPEHLVVDFSHGNCQKQHRRQLDV
AEDICQQIRNGSTAIAGIMAESFLREGTQKIVAGQPLTYGQSITDPCLGWEDTERLLELLAAAVDSRF
>gnl|CDD|237191 PRK12757, PRK12757, cell division protein FtsN; Provisional
MVALAVAVLVTFIGGLYFITHNKKEEAPLLPNHKPRTGNGLPPKPEERWRYIKELENRQIGVPTPTEPSA
GGEVNSPTQLTDEQRQLLEQMQADMRQQPTQLSEVPYNEQTPQVPRSTVQIQQQAQQQQPPATTAQPQPV
TPPRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVEAEKEKEQRWMVQCGSFKGTEQAESVRAQLAFAGI
ESRITTGGGWNRVVLGPYNSKAAADKMLQRLKGAGHSGCIPLAAGG
>gnl|CDD|237192 PRK12758, PRK12758, DNA gyrase/topoisomerase IV subunit A
MSEEIENNQPEEESSEDEALTHVSGMYKNWFLDYASYVILERAVPHIEDGLKPVQRRILHSMKEMDDGRY
NKVANVVGHTMQYHPHGDASIGDALVQLGQKDLLIDTQGNWGNILTGDGAAAPRYIEARLSKFALEVVFN
PKTTEWQLSYDGRKKEPVTLPVKFPLLLAQGAEGIAVGLSTKILPHNFNELIDASIAYLKGKEFKLYPDF
PTGGIIDVSNYNDGERGGRVRVRAKIEKLDKKTLVITEIPYGTTTSSLIDSILKANDKGKIKIKKVEDNT
AADVEILVHLAPGVSPDKTIDALYAFTDCEVSISPNACVIIDNKPHFLGVSDILRRSTDHTVSLLKQELE
IRLSELEEQWHFASLEKIFIEERIYKEIEEAETWEAVIEAIDKGLEPFKKQFIREVTEDDIVRLTEIKIK
RISKFDSDKADELIARLEAEIAEVKHHLAHLTDYAIAYFTNLKKKYGKGRERKTEIRNFDTIEATKVVEA
NQKLYVNREEGFIGTGLKKDEYVADCSDIDDVIVFRRDGKYMVTKVADKTFVGKDIIHVAVFKKNDKRTI
YNMIYRDGKSGPSYIKRFNVTGVTRDKEYDLTQGTPGSKVLYFSANPNGEAEVVTVTLKPNGRIKKLKFD
LDFSEIAIKGRGSKGNILTKYPVKKIELKEKGVSTLGGRKVWFDDDVGRLNYDERGELLGEFKGDDKILV
ILQDGDYYTTNFELTNHYEPNIIVLEKFDPEKPWSAIYYDGEKKNYYVKRFLIENTDKKFNFISEHPGSK
LELLSTDYYPRIEIVFGKGDGKERPNLEIDLEEFIAVKGIKAKGNRLTTYKVKTINELEPLPYEEPEEET
AEEPEEVDPEDVKSEDDIDDEDTGQLGLF
>gnl|CDD|139206 PRK12759, PRK12759, bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
MVEVRIYTKTNCPFCDLAKSWFGANDIPFTQISLDDDVKRAEFYAEVNKNILLVEEHIRTVPQIFVGDVH
IGGYDNLMARAGEVIARVKGSSLTTFSKTYKPFNYPWAVDLTVKHEKAHWIEDEIDLSEDVTDWKNGKIT
KVEKEYITNILRLFTQSDVAVGQNYYDQFIPLFKNNEIRNMLGSFAAREGIHQRAYALLNDTLGLPDSEY
HAFLEYKAMTDKIDFMMDADPTTRRGLGLCLAKTVFNEGVALFASFAMLLNFQRFGKMKGMGKVVEWSIR
DESMHVEGNAALFRIYCQENPYIVDNEFKKEIYLMASKAVELEDRFIELAYELGTIEGLKADEVKQYIRH
ITDRRLNQLGLKEIYNIEKNPLTWLEWILNGADHTNFFENRVTEYEVAGLTGSWDEAYSA
>gnl|CDD|237193 PRK12764, PRK12764, fumarylacetoacetate hydrolase family protein
PTSAPVPTVVAIVVAPLLARPGKVIAVHLNYPSRAAQRGRTPAQPSYFLKPSSSLALSGGTVERPAGTEL
LAFEGEIALVIGRPARRVSPEDAWSHVAAVTAANDLGVYDLRYADKGSNLRSKGGDGFTPIGPALISARG
VDPAQLRVRTWVNGELVQDDTTEDLLFPFAQLVADLSQLLTLEEGDVILTGTPAGSSVAAPGDVVEVEVD
APADGAPSTGRLVTRVVEGTTPFADFGAQPKVDDVQREEAYGSREAAGLAPQAAGPLSPELKAKLASVAT
ATLSAQLRKRGLNNVSIDGLTPTRPGRRMVGRARTLRYVPNREDLFKEHGGGFNAQKRAFDSVNPGEVLV
IEARGEKGTGTLGDILALRAQVRGAAGVVTDGGVRDYAAVAELGLPVFFAGPHPAVLGRRHVPWDVDITV
ACGGATVQPGDVIVGDDDGVVVIPPALAEEVADDAIAQEHEEAFIAERVAEGASVDGLYPMNAEWRAKYE
EWRRGRPADP
>gnl|CDD|237194 PRK12765, PRK12765, flagellar filament capping protein FliD
MAFGSLSSLGFGSDGVLSQDTIDKLKEADQKAQIDPITTKIEENTTKQKDLTAIKTLLSNFKTSVSSLAD
ETSYLKRKVSISDNPPASVTVNSGVNLQSMKINVSQLAQKDVYQSKGFANDSSFVNATLTGETDLTIFSN
GKEYTITVDKSTTYRDLADKINEASGGKIQAKILNVGGKNPYRLVLQSKETGADNAISFYAGKKDAQSDN
DAENIFKSLGWDLDDTSTIDPGKDKKGYGIKDASLHIQTAQNAEFTYNGIKITRSSNTIDDLGVGVTLTL
NKTGSINFDIQQDTEGVTKAVEDLVDAYNNLVTNLNAATSYNSETGTKGTFQGVSEITSIRSSILADLFS
QVVDGTDEDGKSLQDFGLSLNSDGTLSFDSSKFEQKVSEDPDSTQSFFSGSTKYEDISHTGEVVKSGSLN
IQTGDLTINGKGINFKTLTGKTAEENALNLQNAINSAGIEGVKVSVDSKGFRLVLKGSGGEDIEIKGDAT
ALKELGLSDTTINGKSIETKGIFSKLKDTLQEMTGKDGSLTKYDESLTNEIKSLTTSKESTQELIDTKYE
TMANKWLQYDSIIAKLEQQFSTLKNMINAANNSKN
>gnl|CDD|183731 PRK12766, PRK12766, 50S ribosomal protein L32e; Provisional
EPEELEDISGVGPSKAEALREAGFESVEDVRAADQSELAEVDGIGNALAARIKADVGGLEVSEETEAEVE
DEGGEEEEEEDADVETELRPRGLTEKTPELSDEEARLLTQRRREGKPQFNRQDYHKKKRTPTSWRRPRGG
LSKQRRGIKGKGDTVEAGFRTPTAVRGKHPSGFEEVRVHNTDDLEGVDGDTEAVRIASKVGARKRERIEE
VAEEQGIRVLNPTYVEVEVEDD
>gnl|CDD|237195 PRK12767, PRK12767, carbamoyl phosphate synthase-like protein; Provisional
MMNILVTSAGRRVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPKVTDPNYIDRLLDICKKEKI
DLLIPLIDPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKA
ALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPNLIIQEFIEGQEYTVDVLCDLNGEVISIV
PRKRIEVRAGETSKGVTVKDPELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPLSYMA
GANEPDWIIRNLLGGENEPIIGEYKEGLYMRRYDEVVIVEEELLEA
>gnl|CDD|237196 PRK12768, PRK12768, sulfate transporter family protein
ILDAARKALARLLSPPMRSVFWKVLGLTLLLLVVLWFALRRLFSWFAWPWAEQLLPGFPDWAGWLGWVLS
IAAGLGLALGLALLIAPVTALIAGFFLDDVAEIVEREDYPAEPPGTALPLGRALIESLKFLGLVILGNLV
ALPLLFVPGINLIAFFVINGYLLGREFFEFAAMRFRSEAEAKAFRRKHATTVFLAGLVIAAFVAIPIVNL
LTPLFAAAFMVHLHKRLSGRRPELIAPDRR
>gnl|CDD|183733 PRK12769, PRK12769, putative oxidoreductase Fe-S binding subunit; Reviewed
MNRFIMANSQQCLGCHACEIACVMAHNDEQHVLSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPN
GAISHVDDSIQVNQQKCIGCKSCVVACPFGTMQIVLTPVAAGKVKATAHKCDLCAGRENGPACVENCPAD
ALQLVTEQALSGMAKSRRLRTARQEHQPWHASTAAQEMPAMSKVEQMQATPPRGEPDKLAIEARKTGFDE
IYLPFRADQAQREASRCLKCGEHSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLPEITGRVCP
QDRLCEGACTLRDEYGAVTIGNIERYISDQALAKGWRPDLSQVTKSDKRVAIIGAGPAGLACADVLARNG
VAVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGV
GTYRSMKAGLPNEDAPGVYDALPFLIANTKQVMGLEELPEEPFINTAGLNVVVLGGGDTAMDCVRTALRH
GASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRR
PVPIPGSEFVMPADAVIMAFGFNPHGMPWLESHGVTVDKWGRIIADVESQYRYQTSNPKIFAGGDAVRGA
DLVVTAMAEGRHAAQGIIDWLGVK
>gnl|CDD|237197 PRK12770, PRK12770, putative glutamate synthase subunit beta; Provisional
MDGMKFAFMCKEKPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIER
VREGVKELEEAGVVFHTRTKVCCGEPLHEEEGDEFVERIVSLEELVKKYDAVLIATGTWKSRKLGIPGED
LPGVYSALEYLFRIRAAKLGYLPWEKVPPVEGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEA
PAGKYEIERLIARGVEFLELVTPVRIIGEGRVEGVELAKMRLGEPDESGRPRPVPIPGSEFVLEADTVVF
AIGEIPTPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQSIHEWLD
LK
>gnl|CDD|237198 PRK12771, PRK12771, putative glutamate synthase (NADPH) small subunit; Provisional
MMITDNSDCAIGYEAAFDALTLPDGFSDEIATGPWRHKCPVYVDQTPPCNAACPAGEDIRGWLALVRGGD
YEYAWRRLTKDNPFPAVMGRVCYHPCESGCNRGQVDDAVGINAVERFLGDYAIANGWKFPAPAPDTGKRV
AVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLGVEVRLGVRV
GEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLRAVGEGEPPFLGKRVVVIGGGNTAM
DAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENGATGLRVITVEKME
LDEDGRPSPVTGEEETLEADLVVLAIGQDIDSAGLESVPGVEVGRGVVQVDPNFMMTGRPGVFAGGDMVP
GPRTVTTAIGHGKKAARNIDAFLGGEPYEHRPKREIVKFDKLNLWYFTDAPRAQRPELDADERVGDFDEV
LGGLTEEEARQEAARCLSCGNCFECDNCYGACPQDAIIKLGPGRRYHFDYDKCTGCHICADVCPCGAIEM
GPGE
>gnl|CDD|237199 PRK12772, PRK12772, fused FliR family export protein/FlhB family type III secretion system protein
MINTAYFTALILIFLRIFSFFIMVPIFFPKGTPNIVKVSLALIIAYMLVPGIDYSSVNTINNSTLLIFYC
INEILTGLILGFITNLCFVCVRIAGSMMDLQVGFSMMTMFDPTSNSNTTLIERLLYWFSTVIFFIIDGHH
MLIRALVESFNVIKIGKFFLNQESIMHVINVFIQYFYIGIKIAIPIVLIILITDLTLGLISRTVPQLNIM
ILGLPIKILVGLTAFVIALPLFLKVISSAFSNLPDAIRGFYKAIPLLLIFASDDKTEEATPKKKSDARKK
GQIAKSKELALAITLLACTLVLSALGGYVANTLKETMIYFLNNYLNMNLNYNSLNSLAIITLLRVAKIFL
PVALPIMVFGVAANLLQTGFLFTKEPLKPDLKKLNPINGFKRMFSMRSVMELLKDLTIITIVGIVGYKFL
QDNYLDILNLGNLYLPYIITELKSLVISIFFRITLIMIIIAVADYVYQKYQYNKDLRMTKQEVKEEYKQD
EGDPQIKAKIKQKQREMAMQRMMQEVPKATVVVTNPTHIAVALKYEEGKDEAPKVVAKGADYVALKIKEI
AKENDVPIIENKPLARLIYKKVEIDQEIPQDMYQAVAEILAIVYKLKKK
>gnl|CDD|183737 PRK12773, flhB, flagellar biosynthesis protein FlhB; Reviewed
MKKAIWSRTKKLVVVFVQNPKRFFIRIFYKNLSRVPWVCESGKDSFVKSVLDVFYRFMLFGKRFGKFIFW
KQYYDIVSDFSKKCESSHNLHEIKNLMGVPTIYTRSKILWEFPQFTQDRKSCKSSYNLQNVVKSESNSDH
FSNRNTVSLQNRQEGLVIKDVVHPTSFIFSFLHHFDRWGQKSTSHSLWMFRTIERFFSIIKKLFFKKKFS
KSFIVGIFLFYKKIVKKFLGYSEPIDSKLTEFLNSNLFCYFLQFGFINLTIEIVRRIFRFKIFPPNICLS
TEAADFKIDLQLFAAEDEGRTEPGSERRRREEREKGNVPKSPELPAAVVLLAGVILVYLMGEYFFMRTYY
ILRKYIHGVGLRTDMSSESVTELLKNASTDLFTLLWPLLGITLVGAIIGNVAQVGFIFTPRALSFNFSRI
RPNFKKVLPTRQTLFNLGKSLAKVGLIAWVSYIIISKDFFPILLSGEMGLEQAVALVMNSSFKIFLIVGI
ILLAISIVDYLYQRYEYEESLKMTPSEAKREAKESDGDRSLQARRRQLARDMMNKRKMLAKVPEADVVIT
NPTHFAVALEYKPGIHKAPIVIAKGVDDFALLIIRIARENGVPTVEDRLQARGLYEEVELGAEVPQQFYR
AIATILSRLESFRRAV
>gnl|CDD|183738 PRK12775, PRK12775, putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
MYSIVRREAFSDTTFLWEVEAPDVAASAEPGHFVMLRLYEGAERIPLTVADFDRKKGTITMVVQALGKTT
REMMTKFKAGDTFEDFVGPLGLPQHIDKAGHVVLVGGGLGVAPVYPQLRAFKEAGARTTGIIGFRNKDLV
FWEDKFGKYCDDLIVCTDDGSYGKPGFVTAALKEVCEKDKPDLVVAIGPLPMMNACVETTRPFGVKTMVS
LNAIMVDGTGMCGSCRVTVGGEVKFACVDGPDFDGHKVDFKELHARQKRFKSQEDRANEDYAHVCNLEKQ
LFEEGKRNYKKLKTLVPHQTPMPERDAVERARNFKEVNLGYSLEDALQEAERCIQCAKPTCIAGCPVQID
IPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPQETQCEAQCIIAKKHESVGIGRLERFVGDNARAKP
VKPPRFSKKLGKVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRL
VDIGVKIETNKVIGKTFTVPQLMNDKGFDAVFLGVGAGAPTFLGIPGEFAGQVYSANEFLTRVNLMGGDK
FPFLDTPISLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEEGIDFFFLH
SPVEIYVDAEGSVRGMKVEEMELGEPDEKGRRKPMPTGEFKDLECDTVIYALGTKANPIITQSTPGLALN
KWGNIAADDGKLESTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAARSIATYLRLGKKWPITAEEAAAF
QPGKLLPAIELHTHAGAVAAGAETGVATCPKCHRPLEGDEEYVCCATSELQWRCDDCGKVSEGFAFPYGM
CPACGGKLQALDRRKVEDAAALEAIRTAFEIELGGMAFYARAAKETSDPVLKELFLKFAGMEQEHMATLA
RRYHAAAPSPTEGFKIERAAIMAGVKGRPDDPGNLFRIAIEFERRAVKFFKERVAETPDGSVERQLYKEL
AAEEREHVALLTTEFERWKQGKPGLL
>gnl|CDD|237200 PRK12778, PRK12778, bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase
MNKIVEKEIFSEKVFLLEIEAPLIAKSRKPGQFVIVRVGEKGERIPLTIADADPEKGTITLVIQEVGLST
TKLCELNEGDYITDVVGPLGNPSEIENYGTVVCAGGGVGVAPMLPIVKALKAAGNRVITILGGRSKELII
LEDEMRESSDEVIIMTDDGSYGRKGLVTDGLEEVIKRETKVDKVFAIGPAIMMKFVCLLTKKYGIPTIVS
LNTIMVDGTGMCGACRVTVGGKTKFACVDGPEFDGHLVDFDEMLKRMGAYKTIEGEELLKLEERTAAWRA
ELRKSMKPKERTAIERVPMPELDPEYRAHNRFEEVNLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIP
RFIKNIERGNFLEAAKILKETSALPAVCGRVCPQEKQCESKCIHGKMGEEAVAIGYLERFVADYERESGN
ISVPEVAEKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIEN
LKKLGVKFETDVIVGKTITIEELEEEGFKGIFIASGAGLPNFMNIPGENSNGVMSSNEYLTRVNLMDAAS
PDSDTPIKFGKKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMPARLEEVKHAKEEGIEFLTLHN
PIEYLADEKGWVKQVVLQKMELGEPDASGRRRPVAIPGSTFTVDVDLVIVSVGVSPNPLVPSSIPGLELN
RKGTIVVDEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSSK
>gnl|CDD|183740 PRK12779, PRK12779, putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
MSSVTGTVSNEVLRYEQARSTLESSRSELEELQQSEAVGVFQKQLALLQKRLLNDPASLRNMFIADGTQA
IVWEFQQPELGEAFTTTLWELLLRGDDMSIILQRFIWALPLKFKRKFIKAIDVHLSERYPMFEGLSEGWP
GENFIPPYIRPAEERAVDFDLVNQGYLGYQSLGYSVREVELFVWLEVMRDKQCDDKPCELGVLVQGKAEP
KGGCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCTHTKRPIEIGQLEWYLP
QHEKLVNPNANERFAGRISPWAAAVKPPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIP
EFRLPNQLIDDVVEKIKLLGGRFVKNFVVGKTATLEDLKAAGFWKIFVGTGAGLPTFMNVPGEHLLGVMS
ANEFLTRVNLMRGLDDDYETPLPEVKGKEVFVIGGGNTAMDAARTAKRLGGNVTIVYRRTKSEMPARVEE
LHHALEEGINLAVLRAPREFIGDDHTHFVTHALLDVNELGEPDKSGRRSPKPTGEIERVPVDLVIMALGN
TANPIMKDAEPGLKTNKWGTIEVEKGSQRTSIKGVYSGGDAARGGSTAIRAAGDGQAAAKEIVGEIPFTP
AEIKDRVERAARYTELGQIPQTIVGKVQLAGGIVEFTVRAPMVARSAQAGQFVRVLPWEKGELIPLTLAD
WDAEKGTIDLVVQGMGTSSLEINRMAIGDAFSGIAGPLGRASELHRYEGNQTVVFCAGGVGLPPVYPIMR
AHLRLGNHVTLISGFRAKEFLFWTGDDERVGKLKAEFGDQLDVIYTTNDGSFGVKGFVTGPLEEMLKANQ
QGKGRTIAEVIAIGPPLMMRAVSDLTKPYGVKTVASLNSIMVDATGMCGACMVPVTIDGKMVRKHACIDG
PEIDAHIIDWDKFLPRFNQFKAQELESKKKHGFA
>gnl|CDD|183741 PRK12780, fliR, flagellar biosynthesis protein FliR; Reviewed
MSLPLGDSVLGVFLIFCRIGGCLMVVPGYSSPRVPVQVRLFIALSVSLAVTPLLLPLFRPFLEGAAPAET
LLWIGSETLTGLLIGLLGRVFFFALETMATAVATMIGLGSIPGTPVEDTEAIPALVSLIVLTATALFFAT
DLHWELFRGLVASYDRIPPGEGFGGQTALVQLVDQLSEAFTLALRIASPFIIYSVIVNLAVGLVNKLTPT
IPVYFISTPFVLFGGLLLLYLLSSEFLTQFSLGYAAWLRKG
>gnl|CDD|139219 PRK12781, fliQ, flagellar biosynthetic protein FliQ
MNERDALELVRAAIWTIIVASGPAVGAAMLVGIAIALLQALTQIQEVTLTFVPKIVVILIVMAVTGSFVG
AQIYAFTEMVYGRIESGF
>gnl|CDD|139220 PRK12782, flgC, flagellar basal body rod protein FlgC; Reviewed
MIDPLLASSRIASSGLEAQSTRLRVVSENLANAQSTGRTPGADPYARKTVTFRAELDRAAGAASVRVKEI
GVDTAPFRVEYDPGNPAADENGYVKLPNVNMLIEMADMREANRSYEANLQVIKQARAMVAMTIDLLRS
>gnl|CDD|171720 PRK12783, fliP, flagellar biosynthesis protein FliP; Reviewed
MKRARAILVLALAAGLTASAALAQGAGGVTGVPGLDALLPPGNGAASGRIIQLVALLTVLSLAPGLLVMV
TSFTRFAVALSFLRSGLGLQSTPANLFLVSLALFMTFYVMAPTFDRAWNEGVKPLQENRISEEEAFGKIV
DPFREFMTQHVRPKDLQTFTDLASRSFPKAEAGEKIDLRILIPAFMISELRRGFEIGFLIVLPFLVIDMI
VATIVMSMGMMMLPPTVISLPFKVLFFVLIDGWNLLVSGLVRSFF
>gnl|CDD|183742 PRK12784, PRK12784, hypothetical protein; Provisional
MKTRMEEICSSYEGKVEEIFVNESSYVYEWEKLMMIRKNNGELEKVAVGISGNIRLVNVVVGQQIHTDTL
LVRLEDDLLITGCE
>gnl|CDD|183743 PRK12785, fliL, flagellar basal body-associated protein FliL; Reviewed
MAKKPKKAPAAEGGEGAAPPKKKKKLIIIAAAAVLLLGGGGGGFFFFFSHGHGEHHAEAAEPKKPPVFVD
VPDMLVNLAGDPGERVQYLKLKVVLEVKDEKVVEQIKPLMPRVTDAFQTYLRELRPSDLNGSAGLFRLKE
ELLRRVNVALAPAQVNAVLFKEVVIQ
>gnl|CDD|237201 PRK12786, flgA, flagellar basal body P-ring formation protein FlgA
RMIRALLLAAALLAAAGPAALAAAAAAAPVLRAAVTVTGDVVRLGDLFDNAGDAADIAIYRAPAPGTTGA
LPTAQLIAAARAHGVDWVDTSGIREVTVTRAARTVDAEEIEEQVAQALERRNGLGEAADLSVTFDRDFQP
LTLPASDSGAVTPVDVRFDPRSGRFDATFEIAPAGGAAPVRLRVTGTAYETVEAPVLARAVGRGEVIKSS
DVVWERRPKARVSGDDIASREDLVGMQARRALRAGQPLRGADLAKPDLVQRGQLVTLIYQTPGIYLTARG
KALEDGAEGDVVRVLNLQSKRTVTGTVTGRGQVSVDPAAAALAAAAATANTPATAASE
>gnl|CDD|183745 PRK12787, fliX, flagellar assembly regulator FliX; Reviewed
MKIYGPNGTTAAGGSRSARRTGSSGFSLPDESASGAGEARAVSAPKAVAGVDALLALQGVEDPTERRRRS
VRRGETALDVLDELKIGLLSGTLDAATLARLRRAVRELRAASGDPGLDAVLDEIELRVEVELAKLGQR
>gnl|CDD|237202 PRK12788, flgH, flagellar basal body L-ring protein FlgH
MRCMRLLVAILACLALAGCANNLADALQAPRMSPIGQGLRADARAIPVEPRMRTPVSRRSLWDERTDLYR
DPRASRTGDLLTVTISMNDKATLDNKTDRSRDSQTKFGLDYLAEFLPWSDKGKLTANVSSQTSTKGTGKI
DRTEEVKFSVAAIVVDVLPNGNLLISGSQEVRVNYEMRVLNVGGIVRPLDITRNNTIAYEKVAEARISYG
GRGRLMEVQQPAWGHQVYDQVVPF
>gnl|CDD|183746 PRK12789, flgI, flagellar basal body P-ring protein FlgI
MIRRLLLAVLLGLLAGPVAAAGTRIKDIATLKGVRDNQLVGYGLVTGLQGTGDTLRNAQFTEQSLQSMLD
RMGINVRDARLRTRNVAAVMVTADLPPFTGPGSRIDVTVSSLGDATSLRGGTLLMTSLTGGDGLVYAVAQ
GPLAVSGFSVQGQAESLTQGVPTAGRIPNGALIEREVPGTFRDLPELVLELKNPDFKTATQISDAINAYS
LGRYGRRIASERDQRTVVLMRPRQMAQTRFIAEIGDLTIEPDTPARVVVDQRTGTVVIGRNVQISTVAVT
HGNLTVRVTEAPEVSQPAPFSNGQTVVVPRTEIDANEEGGKLAILRGSDLQTLVRGLNQIGLKPSDIIAI
LQAIKTAGALQAELVVQ
>gnl|CDD|237203 PRK12790, PRK12790, flagellar rod assembly protein FlgJ
SLMSRVPTSYASAAPTYNGRPDIELAEALEKVSPQAQAKAKATATDFEAMFLNSMFSQMTSGLKGEGPFG
DTVGTGVWRSMLTEQYSKSFAKAGGVGISDDVFRTLILQQANRSA
>gnl|CDD|237204 PRK12791, flbT, flagellar biosynthesis repressor FlbT; Reviewed
MPLRVELKPFERIVIGQSVITNSDTRARFLIDGDAPILREKDILTAETADTPAKRVYLCVQLMYLSNDIP
AYHGTYLGLIRELIEAVPSAWPIIEAINNHILNGDLYKALKELRKLIAREEKLLARAEATP
>gnl|CDD|237205 PRK12792, flhA, flagellar biosynthesis protein FlhA; Reviewed
AMALSEALPLERRSRRDFGFAVGIVAILAVLFLPVPAVLIDIGLAFSIALSVLILMVALWIQRPLEFSAF
PTVLLIATLLRLALNIATTRLILSNGQEGVDAAGHVIAGFSQFVMSGDFVIGLVVFAILITVNFLVITKG
ATRIAEVGARFTLDAIPGKQMAIDADLSAGLIDDKEAQRRRRELEEESAFFGSMDGASKFVRGDAIASLI
IIAVNIFGGIIIGVTRHGMPLGQAADVFTKLSVGDGLVSQIPALIVSLAAGLLVSKGGTRGSAEQAVLGQ
LGAYPRALSVAALLMFVLAIVPGLPFLPFALLGGVMAFVAYTIPRRRAARAAAEAAKVKREEESAQAEAK
DSVKEQLRTAEIELCLGKQLAAQLQGAHAELAHRVAKMRRKFAKQYGFVVPEIKLTDSLSLPPKTYQIKI
HGTVVATQELRPGELLVVVGDGPRPDVPGEEVREPAFGMKALWVPDAFANEVRRDGFEPVDNASVLLTHL
SEVIRNNLPQLLSYKDMRALLDRLDPEYKRLIDDICPSQISYSGLQAVLKLLLAERVSIRNLHLILEAVA
EIAPHARRAEQIAEHVRMRIAQQICGDLSDNGVLKVLRLGNRWDLAFHQSLKRDAKGEVVEFDIDPRLVE
QFGTEASEAIRERMDQGHQFVLVTAPEARPYVRMIIERLFPTLPVLSHLEIARGVEIKSLGTIS
>gnl|CDD|237206 PRK12793, flaF, flagellar biosynthesis regulator FlaF
MYQFSYAEVMEDSVASARERERQAFDRSIDLLEAARAKGAYSREAIEALYFTRRLWTVLIEDLGSPENAL
PEELRADLISIGLWVLKEADRIRQGESNNFAGLIEINTSIRDGLK
>gnl|CDD|237207 PRK12794, flaF, flagellar biosynthesis regulatory protein FlaF; Reviewed
MSMAAQAYARAAQPTRTPRETEYQLLAKATRQLKDAQTNGPDRFAALAEALHFNRKLWSIFASDVADPDN
PLPIELRARIFNLSLFVQKHSSKVLRKPEKLTPLIDINRNIAAGLSGRAGAA
>gnl|CDD|237208 PRK12795, fliM, flagellar motor switch protein FliM; Reviewed
MDDGDDDALAADWEAALASEDPEGAAGAATNELTGDMAAEWAAMVEDGGRDNGSERVLNQDEIDSLLGFS
LGEDSADDRSGIRAIIDSALVSYERLPMLEIVFDRLVRLLTTSLRNFTSDNVEVSLDNITSVRFGDYLNS
IPLPALLAVFKAEEWDNYGLLTVDSSLIYSIVDVLLGGRRGTAAMRIEGRPYTTIERNLVERLVEVVLAD
LETAFRPLSPVTFTIDRLETNPRFAAIARPANAAILVRLRIDMEDRGGRIELLLPYATLEPIRDLLLQMF
MGEKFGRDSIWEGHLATEIWQTDVEVDAVLDEQTLPLKRVLNLKVGDTLMLDARPDALVTLRCGDVPLTE
GRMGRVGDRVAVRVEKPLRKPRTTLAAFEASMEQRKDM
>gnl|CDD|237209 PRK12796, spaP, EscR/YscR/HrcR family type III secretion system export apparatus protein
MNNDISLIALLSFFTLLPFIIASGTCFIKFSIVFVMVRNALGLQQVPSNMTLNGIALLLSMFVMMPVIQD
IYVYFQNEPVDFNNIASVVKFVDEGLGGYRDYLIKYSDPELVRFFERAQKKRSYGDEAEANDHDKDEISL
FSLLPAYALSEIKSAFKIGFYLYLPFVVVDLVVSSVLLALGMMMMSPVTISVPIKLILFVAMDGWTLLSK
GLILQYMDLMT
>gnl|CDD|237210 PRK12797, PRK12797, type III secretion system protein YscR; Provisional
MEQLPDPLQLIILLALLSLLPLIAVMGTSFLKISVVLSLLRNALGVQQVPPNMALYGLALILTLFVMAPV
GLAIQDRLQQPPLSLQDPDSVLQLLDAALAPLRDFLKKHTDERERTFFVRSAQRIWPEEAADSLKKDDLL
ILIPAFTLSELTRAFEIGFLLYLPFIVIDLIISNILLAMGMMMVSPTTISLPFKLLLFVLVDGWSRLLHG
LVL
>gnl|CDD|237211 PRK12798, PRK12798, chemotaxis protein; Reviewed
ALRALLALALALALAGPAAGTAAAAAQTGDVLEPYKLVRSLQLLQDSVAAGDHSAHEMQRFLLGTIDERL
RAADPEVWDDPRNVDAALIYLLSGGNPATLRKLLARDKLGNFDQRLADGALAYLSGRGREARKLLAGVAP
EYLPAELGAYLALVQGNLMVATDPATALKLLDQARLLAPGTLVEEAALRRSLFIAAQLGDADKFEALARN
YLRRFRHSPYASQFAQRFVDLVVRLDDEIRDARLVEILSFMDPERQRELYLRIARAALIDGKTELARFAS
ERALKLADPDSADAARARLYRGAALVASDDAESALEELSQIDRDKLSERDRALLEAARSVARQVRRAPAT
SPAKRSADAASEPPSAVAPAPQAPAQLPLSVPVEVDSNSARTRSDPDLQKFVARARSKLDEIDALLKKEG
R
>gnl|CDD|183756 PRK12799, motB, flagellar motor protein MotB; Reviewed
MKHQNHPVILVKKRKTKHGAAHYGGSWKIAYADFMTAMMAFFLVMWLLAVSSPQELTQIAEYFRTPLKVA
LTSGDKSSSSTSPIPGGGDDPTQQVGEVRKQINSEESRQEIHRLNKLREKLDQLIESDPRLKALRPHLLI
NMMDEGLRIQIIDSQNRPMFKMGSAQVEPYMRDILRAIAPILNDIPNKLSLSGHTDDLPYARGERGYSNW
ELSADRANASRRELLAGGLDEGKILRVVGMASTMRLKEQASDDPVNRRISILVLNKQSQHDIEHENLDNR
ALDIEKATGLKQIDTHGTVPVAAVTPSSAVTQSSAITPSSAAIPSPAVIPSSVTTQSATTTQASAVALSS
AGVLPSDVTLPGTVALPAAEPVNMQPQPMSTTETQQSSTGNITSTANGPTTSLPAAPASNIPVSPTSRDA
Q
>gnl|CDD|139237 PRK12802, PRK12802, flagellin; Provisional
MALTVNTNITSLTVQKNLSRASDALSTSMTRLSSGLKINSAKDDAAGLQIATRQTSQIRGQTQAIKNAND
GISIAQTAEGALQESTNILQRMRELAVQSRNDSNDSTDRAALNKEFTTMLDEITRIATSTTLNGKNLLDG
SAGTMTFQVGANTGQSNQITFGLSASFDATGLGVGSGTLITGADSAAAETNAQAAITAIDAALQTINTTR
ADLGAAQNRLQSTISNLQNINENASAARGRVQDTDFAAETAQLTKQQTLQQASTSVLAQANQLPSAVLKL
LQ
>gnl|CDD|183758 PRK12803, PRK12803, flagellin; Provisional
MIINHNTSAINASRNNSINAANLSKTQEKLSSGHRINRASDDAAGMGVAGKINAQIRGLSQASRNTSKAI
NFIQTTEGNLNEVEKVLVRMKELAVQSGNGTYSDADRGSIQIEIEQLTDEINRIADQAQYNQMHMLSNKS
AAQNVRTAEELGMQPAKINTPASLSGSQASWTLRVHVGANQDEAIAVNIYAANVANLFSGEGAQQAAPVQ
EGAQQEGAQAAPAPAAAPAQGGVNSPVNVTTTVDANMSLAKIENAIRMISDQRANLGAFQNRLESIKAST
EYAIENLKASYAQIKDATMTDEVVASTTNSILTQSAMAMIAQANQVPQYVLSLLR
>gnl|CDD|183759 PRK12804, PRK12804, flagellin; Provisional
MRINHNIAALNTLNRLSANNGASQKNMEKLSSGLKINRAGDDAAGLAISEKMRGQIRGLEMASKNAQDGI
SLIQTAEGALTETHSILQRVRELVVQAGNTGTQDGTDLGAIQDEIKALVDEIDGISDRTEFNGKKLLDGT
FKPAAPAAGTKSLTFQIGANAAQQLSVNIEAMSADALGVKDTDGTLVTGKSVSDIDVTKFANAAAAADGG
FDDQLKIVDGAIKQVSDQRSKLGAVQNRLEHTINNLGASGENLTAAESRIRDVDMAKEMSEFTKNNILSQ
ASQAMLAQANQQPQNVLQLLR
>gnl|CDD|183760 PRK12805, PRK12805, FliC/FljB family flagellin
MKVNTNIISLKTQEYLRKNNEGMTQAQERLASGKRINSSLDDAAGLAVVTRMNVKSTGLDAASKNSSMGI
DLLQTADSALSSMSSILQRMRQLAVQSSNGSFSDEDRKQYTAEFGSLIKELDHVADTTNYNNIKLLDQTA
TGAATQVSIQASDKANDLINIDLFNAKGLSAGTITLGSGSTVAGYSALSVADADSSQEATEAIDELINNI
SNGRALLGAGMSRLSYNVSNVNNQSIATKASASSIEDADMAAEMSEMTKYKILTQTSISMLSQANQTPQM
LTQLINS
>gnl|CDD|183761 PRK12806, PRK12806, flagellin; Provisional
MAQVINTNVASLTAQRNLGVSGNMMQTSIQRLSSGLRINSAKDDAAGLAISQRMTAQIRGMNQAVRNAND
GISLAQVAEGAMQETTNILQRMRELSVQAANSTNNSSDRASIQSEISQLKSELERIAQNTEFNGQRILDG
SFSGASFQVGANSNQTINFSIGSIKASSIGGIATATGTEVAGAAATDITIAIGGGAATSINSSANFTGAL
NGQDATSAYAKAAAINDAGIGGLSVTASTSGTQAVGAIGGTAGDTYNLTINGVAIYTNLDVATALTNSDL
RDAINGVSNQTGVVASLNGGNMTLTAADGRNITVTESGTGFTAGTDGLTVTGGAFDGALRGTLSISAVDT
IAIGGTVANIGLSANISKDTVGIDSLDVSTASGAQTAIKRIDAALNSVNSNRANMGALQNRFESTIANLQ
NVSDNLSAARSRIQDADYAAEMASLTKNQILQQAGTAMLAQANSLPQSVLSLLGR
>gnl|CDD|171737 PRK12807, PRK12807, flagellin; Provisional
MRINTNINSMRTQEYMRQNQDKMNVSMNRLSSGKRINSAADDAAGLAIATRMRARQSGLEKASQNTQDGM
SLIRTAESAMNSVSNILTRMRDIAVQSSNGTNTAENQSALQKEFAELQEQIDYIAKNTEFNDKNLLAGTG
AVTIGSTSISGAEISIETLDSSATNQQITIKLANTTAEKLGIDATTSNISISGAASALAAISALNTALNT
VAGNRATLGATLNRLDRNVENLNNQATNMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQ
MVSKLLQ
>gnl|CDD|237212 PRK12808, PRK12808, flagellin; Provisional
MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGM
SLIRTADSAMNSVSNILLRMRDIANQSANGTNTDKNQAALQKEFAELQKQITYIADNTQFNDKNLLNSNS
SINIQTLDSSDGDKQIGIDLKSATLEALGINDLSIGANTDIEAVSTKIAALDKNTIAKATVEAKAAFDKA
KDDTKAEDSNILDAAADGFKDGKADDAAKDVEAIKTALSAFTGAATLEEAEAAKTAFEVAQKDLVDTYTK
KAALTKDAVADLDTAKTTSTRSKAAKDLVAAYDKAKSGAKPNDVAKAYLEAKMAYEKDNNAIDGKSKLEA
ADDALEKDAIKTDASKVLVPKLEAAKKATTNSKADSLDAVKAIDEALKTVADNRATLGATLNRLDFNVNN
LKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ
>gnl|CDD|183762 PRK12809, PRK12809, putative oxidoreductase Fe-S binding subunit; Reviewed
MNKFIAAEAAECIGCHACEIACAVAHNQENWPLSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPV
NALTFQSDSVQLDEQKCIGCKRCAIACPFGVVEMVDTIAQKCDLCNQRSSGTQACIEVCPTQALRLMDDK
GLQQIKVARQRKTAAGKASSDAQPSRSAALLPVNSRKGADKISASERKTHFGEIYCGLDPQQATYESDRC
VYCAEKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDRLCEGACTLKDHSGA
VSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLT
FGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPG
VIQALPFLTAHTRQLMGLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMP
GSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLI
MAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDM
LTLFDTKAS
>gnl|CDD|237213 PRK12810, gltD, glutamate synthase subunit beta; Reviewed
MGKPTGFLEYDRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDL
VYRGRWEEAAERLHQTNNFPEFTGRVCPAPCEGACTLNINFGPVTIKNIERYIIDKAFEEGWVKPDPPVK
RTGKKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEF
RTNVEVGKDITAEELLAEYDAVFLGTGAYKPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGDETEPFISAK
GKHVVVIGGGDTGMDCVGTAIRQGAKSVTQRDIMPMPPSRRNKNNPWPYWPMKLEVSNAHEEGVEREFNV
QTKEFEGENGKVTGVKVVRTELGEGDFEPVEGSEFVLPADLVLLAMGFTGPEAGLLAQFGVELDERGRVA
APDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLMGSTALP
>gnl|CDD|139245 PRK12812, flgD, flagellar basal body rod modification protein; Reviewed
MISSSDWNLNTTATTSTTTKSASTSGATRTDSSSSTGSNPNSQLDKDAFLKLLLIELQHQDPTDPMDSDK
MLTQTSQLAALEMQENTNTTMQKLVEQMQSSMSTSALSALGKMATVSDNAVKLTGADELIALKLYFPEDS
DEGTLEIYDSNNKLVEKIDFKEISQGLFTMEWDGRDNDGVYAGDGEYTIKAVYNNKNGEKITANYGTYPV
EAVKFVDGVAYAKMAGEYVPMDKIQEITEYKLGSSSSTGGSGSSGDSSG
>gnl|CDD|237214 PRK12813, flgD, flagellar basal body rod modification protein; Reviewed
MDIVTGTVTSPGTTTGSSRGSASAASALTSDFETFLRMLTTQLQNQDPLNPMDSSDYAAQLATFSGVEQQ
VKTNDLLTGLGASLGVMGLSQLAGWIGREARAEAPVWFDGTPVTISPNPAADADKAELVVRDAAGAEVAR
ETVPVGAGPVEWAGEDADGNPLPNGAYSFVVESYSGGELLDTEPAEVYSRIVEAQGGSGGTVLVLEGGIE
VPASSVTALRDAS
>gnl|CDD|139246 PRK12814, PRK12814, putative NADPH-dependent glutamate synthase small subunit; Provisional
MNTISLTINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEIKGKNRFVPACSTAVSE
GMVIETENAELHAMRRQSLERLIEQHCGDCLGPCELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLP
GILGRICPAPCEEACRRHGVDEPVSICALKRYAADRDMESAERYIPERAPKSGKKVAIIGAGPAGLTAAY
YLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVIDADIAPLRAMGAEFRFNTVFGRDITLEELQKEFD
AVLLAVGAQKASKMGIPGEELPGVISGIDFLRNVALGTALHPGKKVVVIGGGNTAIDAARTALRLGAESV
TILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERSEGGLELTAIKMQQGEPDESGRRRPVPVEGS
EFTLQADTVISAIGQQVDPPIAEAAGIGTSRNGTVKVDPETLQTSVAGVFAGGDCVTGADIAINAVEQGK
RAAHAIDLFLNGKPVTAPVQPFNSSYGPRDKAPEAFYDRAQPAPRVALPELPLEERTGGFEEVVTGYSPE
QAREEALRCLRCRCNAVDDCRLRDLATRYLPDTPCKEEEHEGFSITRNGDIRFEREKCVDCGICVRTLEE
YGAEGNTDIEVLAESCPTGALS
>gnl|CDD|237215 PRK12815, carB, carbamoyl phosphate synthase large subunit; Reviewed
MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLT
VEFVKRIIAREKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELG
EPVPESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESI
AGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGG
CNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAVGYTLNELKNPVTGLTYASFEPAL
DYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGLSLPIELSGKSDEE
LLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLDLSADLLRKVKE
KGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAEPSSEKKKVLI
LGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAEN
IKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAF
AKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENASQLYPILIDQFIDGKEYEVDAISDGEDVTIPG
IIEHIEQAGVHSGDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRAS
RTVPFVSKATGVPLAKLATKVLLGKSLAELGYPNGLWPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTG
EVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLARRFAQLGFKLLATEGTANWLAEEG
ITTGVVEKVQEGSPSLLERIKQHRIVLVVNTSLSDSASEDAIKIRDEALSTHIPVFTELETAQAFLQVLE
SLALTTQPIQELQEKHKQ
>gnl|CDD|183766 PRK12816, flgG, flagellar basal body rod protein FlgG; Reviewed
MMRSLWTAASGMNAQQFNIDTIANNLANVNTTGFKKIRAEFEDLIYQTQRRAGTPATEDTVTPLGVQVGH
GVKVAATQRLFEQGSLQATGNKLDVAIEGEGFFKILMPDGTYAYTRDGSFKIDANGQLVTSNGYRLLPEI
IFPENYILNSITISEEGIVSVKVGEDNDPIELGQIELYRFVNPAGLSAIGKNLFKETIASGQEIPGIPGS
EGFGRVLQGFLEMSNVSIVEEMVTMIVAQRAYEINSKAIQTSDNMLGTANNLKR
>gnl|CDD|183767 PRK12817, flgG, flagellar basal body rod protein FlgG; Reviewed
MLRAFWNSKSGMNAQQEKLDSISNNLANVNTTGYKREDVSFSDLVYETLDRKGYPTNDKPEIITGTGVKA
TNWIRDNQQGNLLTTGNKTDLAIDGEGFFRVIMADGTYAYTRAGNFNIDSNGMLVDDNGNRLEIQLEAGV
GINNRNTGFDSNNFTVDEDGGISVKNVDGQNKKVGKINIYNAVGNDAFISIGDNLYVPSDGVQVFLNNDV
DILQGYLENSNVDLGKEMTDMIITQRAFQLSSKGIKTADEMWGIINNMRK
>gnl|CDD|183768 PRK12818, flgG, flagellar basal body rod protein FlgG; Reviewed
MIRGLYTAVSGMITLEAKQDVITNNLANVNTVGYKSDNLAFKSFEDVLIENYDKKVGNKNVKNIIGGLSM
GSKIDEVNTLFTQGIIKSTDKPTDFAIQGRGFFTVERNAGNNYYTRDGHFHVDTQGYLVNDSGYYVLGRN
NATGAREPINVGNGKFSTDADGNISLDGNASYKFNVADFNDYNSLKKIGDNLYTGNNPQNINGAIVRQNS
LEKSNVNVTNEMVNMMTTMRSFETNQKIVQSIDETLGKAVNEVGSV
>gnl|CDD|183769 PRK12819, flgG, flagellar basal-body rod protein FlgG
MNGLYIGSMGMMNYMQRINVHSNNVANAQTTGFKAENMTSKVFDVQDTYRRGDGAVTNIGSVDYAVVPAA
THVNLVQGNIQMTNSDTDFFLDDGPAGTSSFFVTSKNGETFLTRDGSFTLNSDRYLQTASGAFVMGENNE
RIRIPEGAKVAVQADGTLYDAVTQNNIARLQTKTVSAEQNDRLVQRENKSFTLAEGNIANLPNGQGIVKN
GMLENSNVDMTKEMADLMTDQRMIQASQRVMTSFDKIYEKEANEILR
>gnl|CDD|105955 PRK12820, PRK12820, bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
MAENDRSFCGHLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRA
EFCVALQGEVQKRLEETENPHIETGDIEVFVRELSILAASEALPFAISDKAMTAGAGSAGADAVNEDLRL
QYRYLDIRRPAMQDHLAKRHRIIKCARDFLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYALPQ
SPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASFIDEEFIFELIEELTARMFAIGGIA
LPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTRYGIFKQILQRGGRIKGINIKGQSEKLSKN
VLQNEYAKEIAPSFGAKGMTWMRAEAGGLDSNIVQFFSADEKEALKRRFHAEDGDVIIMIADASCAIVLS
ALGQLRLHLADRLGLIPEGVFHPLWITDFPLFEATDDGGVTSSHHPFTAPDREDFDPGDIEELLDLRSRA
YDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGFFLRAFDFAAPPHGGIALGLDRVVSMIL
QTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLAELGLLDLGDADQLPGDAEKEDLIDHLSWVSRIGFAE
AERAAIESALADAEELAAQLEDIACDEEPLFSPAPAANRMGEGLEARECSFAATGEILKNAPAVKGDYFK
VAGILD
>gnl|CDD|237216 PRK12821, PRK12821, aspartyl/glutamyl-tRNA amidotransferase subunit C-like protein; Provisional
MGEIKTESFTSDISTSGFIYFAVVFGLILVYLLFKNLLFLFFFKRYPKNTPKIGVINITTIAMIIAVAVS
IVLVLMALAGGLAAALFRGYPGFRVTLELILVKISGLLFGPIIGIFSAATIDFLTVIFSGGVFNYGYVLG
AILTGMIAGILREVLISTKYLKNRNLSDFAYLVLSVGMVIASFLLTQFFVISVTTNLPEIRINGGFDLSF
NAVSQTFKISLVVYTWIILYFGIGIIIFMWVLYLVWKLKQPHNAYSLSGFFHRRYKHANHQFTLFVLTKE
NWFYLILNVITLAGTSLLMINIAFIPIFDTQTTGQTYAFWLLIRLLFAPAIFLLDIIVIYPILLLLTPIM
LKGFKTELSETQTKGIKKSFSDLQSPLFPKHWTSKKQQLNKDELKKLARLVMFDLDDAELEKLQVEFKDI
TSSFKQVEKIDTTNVKPMYAPFSNSPTPLRKDKDVVQKHQKILLKNCKETLGGFVKV
>gnl|CDD|237217 PRK12822, PRK12822, phospho-2-dehydro-3-deoxyheptonate aldolase; Provisional
MAVLKSVMRGTLCGSLPSVAEILKEIPCSEETETWISQQRQDIRNILLGKDPRLLVIIGPCSIHDPQAAL
EYAKRLAVLQHQYLDQLYIVMRTYFEKPRTRKGWKGLIFDPDLDGSNDIEKGLRLARQLLLSINTLGLAT
ATEFLDTTSFPYIADLICWGAIGARTTESQVHRQLASALPCPVGFKNGTDGNIRIAIDAILAARSPHLVT
VPGLTGCISTLLSDGNPHGHIILRGGREPNYGLSDVTKASKLLHDEGLNHRLIIDCSHGNSQKVAKNQIS
VARELCDQLKEGEGAIAGVMVESFLQGGSQKADSAPLEYGQSVTDECLSWQDTEQLLNTLAEAVETRRQE
RFSAQP
>gnl|CDD|183772 PRK12823, benD, 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
MMNQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSELVHEVAAELRAAGGEALALTADLETYAG
AQAAMAAAVEAFGRIDVLINNVGGTIWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIV
NVSSIATRGINRVPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEAPPRRVPRNAAPQSEQEKAWY
QQIVDQTLDSSLMKRYGTIDEQVAAILFLASDEASYITGTVLPVGGGDLG
>gnl|CDD|183773 PRK12824, PRK12824, 3-oxoacyl-ACP reductase
MKKIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEA
LAEIEEEEGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSV
NGLKGQFGQTNYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQMGPEVLQSIVNQIPMKRL
GTPEEIAAAVAFLVSEAAGFITGETISINGGLYMH
>gnl|CDD|237218 PRK12825, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
MGSLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAA
LEAAVAAAVERFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVN
ISSVAGLPGWPGRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDAETP
LGRSGTPEDIARAVAFLCSDASDYITGQVIEVTGGVDVI
>gnl|CDD|183775 PRK12826, PRK12826, SDR family oxidoreductase
TRDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAAL
KAAVAAGVEDFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLT
SSVAGPRVGYPGLAHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQWAEAIAAAI
PLGRLGEPEDIAAAVLFLASDEARYITGQTLPVDGGATLPE
>gnl|CDD|237219 PRK12827, PRK12827, short chain dehydrogenase; Provisional
MASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGIEAAGGKALGLAFDVRD
FAATRAALDAGVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARRGG
RIVNIASVAGVRGNRGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAAPTEHLLNP
VPVQRLGEPDEVAALVAFLVSDAASYVTGQVIPVDGGFC
>gnl|CDD|237220 PRK12828, PRK12828, short chain dehydrogenase; Provisional
MEHSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGGIDLVDPQAAR
RAVDEVNRQFGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIG
AGAALKAGPGMGAYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRADMPDADFSRWVTPEQI
AAVIAFLLSDEAQAITGASIPVDGGVALP
>gnl|CDD|183778 PRK12829, PRK12829, short chain dehydrogenase; Provisional
SAIDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGAKVTATVADVADP
AQVERVFDTAVERFGGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGG
VIIALSSVAGRLGYPGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQLG
IGLDEMEQEYLEKISLGRMVEPEDIAATALFLASPAARYITGQAISVDGNVEYL
>gnl|CDD|183779 PRK12830, PRK12830, UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDT
LEIDPTGIQSMPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNE
GGAIYLKADELKGAHIYLDVVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGT
DVIRIEGVDELHGCRHTVIPDRIEAGTYMILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSI
FVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGRSVVTDTIYEKRFKHVDELKRMGANIKVEGRS
AIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGYSNIIEKLKALGADIWREED
>gnl|CDD|183780 PRK12831, PRK12831, putative oxidoreductase; Provisional
MMKDRKKRVPVREQDPEVRATNFEEVCLGYNEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEG
DFEEAAKIIAKYNALPAVCGRVCPQESQCEGKCVLGIKGEPVAIGKLERFVADWARENGIDLSETEEKKG
KKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVLVYGIPEFRLPKETVVKKEIENIKKLGVKIET
NVVVGKTVTIDELLEEEGFDAVFIGSGAGLPKFMGIPGENLNGVFSANEFLTRVNLMKAYKPEYDTPIKV
GKKVAVVGGGNVAMDAARTALRLGAEVHIVYRRSEEELPARVEEVHHAKEEGVIFDLLTNPVEILGDENG
WVKGMKCIKMELGEPDASGRRRPVEIEGSEFVLEVDTVIMSLGTSPNPLISSTTKGLKINKRGCIVADEE
TGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSKKW
>gnl|CDD|183781 PRK12833, PRK12833, acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
MPSRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAIL
AAARQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGV
VASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARAR
HIEVQILGDGERVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLF
DDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRFAQGDIALRGAALECRINAEDPLRD
FFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAALARAARALRELRIDGMKT
TAPLHRALLADADVRAGRFHTNFLEAWLAEWRAALDAAASAAVGEAA
>gnl|CDD|183782 PRK12834, PRK12834, putative FAD-binding dehydrogenase; Reviewed
MAMDADVIVVGAGLAGLVAAAELADAGKRVLLLDQENEANLGGQAFWSLGGLFLVDSPEQRRLGIKDSLE
LALQDWLGSAGFDRPEDHWPRQWAEAYVDFAAGEKRSWLHSLGLRFFPVVGWAERGGGDAGGHGNSVPRF
HITWGTGPGVVEPFERRVREAAARGLVRFRFRHRVDELVVTDGAVTGVRGTVLEPSDAERGEASSREVVG
EFELRAQAVIVTSGGIGGNHELVRRNWPERLGTPPKDMVSGVPAHVDGRMLGIAEAAGARVINRDRMWHY
TEGIRNWDPIWPNHGIRILPGPSSLWFDATGNRLPAPLFPGFDTLGTLKHILKTGYDYSWFILTQKIIEK
EFALSGSEQNPDLTGKDWKLLLRRRGKGAPGPVEAFKDHGEDFVVADDLEELVAGMNALTGEPLLDYAHL
RRQIEARDREVANPFSKDAQITAIRNARRYLGDRLIRVAKPHRLLDPAAGPLIAVRLHILTRKTLGGLET
DLDSRVLGADGTPLPGLYAAGEAAGFGGGGVHGYNALEGTFLGGCIFSGRAAGRAAARA
>gnl|CDD|237221 PRK12835, PRK12835, 3-ketosteroid-delta-1-dehydrogenase; Reviewed
MSVDEQNFDREVDVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGSTALSGGGIWVPGAPAQRREGY
VPDPEDVRRYLKQITGGLVSAARLRAYVDAAPQMMEFLENLSPWLEFVWKPGYADYYPELPGGSPLGSTI
NVPPIDLRKLGEDEQHLLPPLALAPKGIWFTPKDLRLFYMVRQTWAGKAVLLKLIWRMVRARVFGRRMAA
IGQSLVARLRLALKDAGVPLWLDSPMTELITDPDGAVVGAVVEREGRTLRIGARRGVILATGGFDHDMDW
RKEYLPELERKDWSFGNPANTGDGIRAGEKVGAATDLLDEAWWFPAICWPDGRMQFMLNERMMPAQFIVN
GAGKRFINEAAPYMDFVHAMIAGQRSGVGHIPCWLVTDIRSFSRYVFGGHLPIPKIPFAPVPTGRKFPQA
WLESGVVKKADTWDELAAKIGVPAENLRATAERFNGLARKGHDDDFNRGDSAYDNYYGDPTLPNPNLDPL
GKPPYYAFRIELGDLGTSGGLRTDEHARVLREDDSVIPGLYAVGNTSASVMGRSYAGAGATIGPAMTFGY
VAARHAAAVVAAAAADTTTHSHAG
>gnl|CDD|237222 PRK12837, PRK12837, FAD-binding protein
MSAWDEEVDVLVAGSGGGVAGAYTAAREGLSVALVEATDKFGGTTAYSGGGGMWFPCNPVLRRAGTDDTI
EDALEYYHAVVGDRTPRDLQETYVRGGAPLIEYLEQDEHFEFAELPWPDYFGKAPKARADGQRHIVPKPL
PAAALGELREQIRGPLDTERLGAPPPDYLVGGRALIGRFLAALARFPNARLRLNTPLVELVVEDGRVVGA
VVERGGERRRVRARRGVLLAAGGFEQNDDMRARYGVPGSARDTMGGPGNTGLAHQAAIAVGADTDLMDQA
WWSPGLTHPDGRSAFALWFTGGIFVDQHGERFVNESAPYDRLGRAVIAEMDSGGMTLPFWMIYDDREGEV
PPVKATNVSMVETAQYVAAGLWRTADTLEELAAKIGVPADALTATVARFNGFAAAGVDEDFGRGDEAYDR
AFSGGASPLVPIDTPPFHAAAFGVSDLGTKGGLRTDTAARVLDTDGRPIPGLYAAGNTMAAVSGTTYPGG
GNPIGASMLFSHLAALDMAGRGP
>gnl|CDD|183784 PRK12838, PRK12838, carbamoyl phosphate synthase small subunit; Reviewed
MKAYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYES
KQPQVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDDAHAFD
QIKALVLPKNVVAQVSTKEPYTYGNGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPD
GIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRV
WMTSQNHGYVVDEDSLDGTPLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMM
EKAR
>gnl|CDD|237223 PRK12839, PRK12839, FAD-dependent oxidoreductase
MTPSMTHTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGATAWSGGWMWTPGNSLARADGVVED
KEEPRTYLEHRLGENYDADKVDALLDGAPEMVDFFEKKTALQFVPGAKIADIYGDLPGAGTGHRSVGPKP
VNLRKLGPDVAALLRHQLYETSFLGMGIMAGPDLQAFLHATQDPKGFVHAARRVIVHMWDLATHRRGMQL
VNGTALTGRLLRSADDLGVDLRVSTSATSLTTDKNGRVTGVRVQGPDGAVTVEATRGVVLATGGFPNDVD
RRKELFPRTPTGREHWTLAPAETTGDGISLAESVGARLDRDLASPAAWCPVSLVPYRNGKVGTFPHIMDR
GKPGSIGVLATGKRFVNEANGYYDYTLAMVKAAPEGEPVCSWLIADSRFVRKYPLGMAKPLPVPLTPYLR
SGYLTRGRTIEELAEKCGIDPAGLEATVAEFNENARDGEDPEFGRGTTPFNRGSGDPDNGPNPSLAPLEK
GPFYAVKVVPGSFGTFAGLVADGKSRVLRDDDTPIDGLYAAGNDQASVMGGHYPSGGINLGPAMTFGYIA
GRELAGSTGVER
>gnl|CDD|237224 PRK12842, PRK12842, putative succinate dehydrogenase; Reviewed
EECMTNELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGTTAFSGGVLWIPGNPHAREAGVAD
SREAARTYLKHETGAFFDAAAVEAFLDNGPEMVEFFERETEVKFVPTLYPDYHPDAPGGVDIGRSILAAP
YDIRGLGKDMARLRPPLKTITFIGMMFNSSNADLKHFFNATRSLTSFIYVAKRLATHLKDLALYRRGTQV
TSGNALAARLAKSALDLGIPILTGTPARELLTEGGRVVGARVIDAGGERRITARRGVVLACGGFSHDLAR
IARAYPHLARGGEHLSPVPAGNTGDGIRLAEAVGGAVDIRFPDAAAWMPVSKVPLGGGRTGVFPHLLDRY
KPGVIGVLRNGKRFTNESNSYHDVGAAMIRACEGQKETAMWLICDRATLRKYGLGYAKPAPMPVGPLLRN
GYLIKGDTLAELAGKAGIDAAGLEATVRRYNEGAVKGIDPAFGRGSTSFNRYLGDPDHKPNPCVAPIGSG
PFYAVKVIMGDLGTFDGLRTDVTGEVLDADGTPIAGLYAVGNDRASIMGGNYPGAGITLGPIMTFGYITG
RHLAGVAGGRKLES
>gnl|CDD|237225 PRK12843, PRK12843, FAD-dependent oxidoreductase
MSPVVSELSPERWDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTATSAGTTWIPGTRHG
LAVGPDDSLEAARTYLDALVGDRSPEELRDAFLASGPRAIAFLEANSEVKFRAYASHPDYESDLPGATLR
GRALEPLPFDGRKLGADFALIRPPIPEFTVLGGMMVDRTDVGHLLALTKSWRAFRHAVRLLARYARDRIS
YARGTRLVMGNALIGRLLYSLRARGVRILTQTDVESLETDHGRVIGATVVQGGVRRRIRARGGVVLATGG
FNRHPQLRRELLPAAVARYSPGAPGHTGAAIDLALDAGARYGRGLLSNAFWAPVSVRRRADGSTAVFPHF
YLDRGKPGTIAVNQQGRRFVNESTSYHLFGTAMFAAGKTSPGIPAYLITDAEFLRKYGLGMVRPGGRGLA
PFLRDGYLTVASTLDELAPKLGIDPAALAATVQRHNQYARTGIDPDFGRGATAYQRMNGDAMIGPNPNLG
PIETAPFYAVRLYPGDIGAATGLVTDASARVLNADGQPISGLYACGNDMASIMGGTYPGPGITLGPAIVF
AYLAARHAAKRTLARRAA
>gnl|CDD|183787 PRK12844, PRK12844, 3-ketosteroid-delta-1-dehydrogenase; Reviewed
ATWDETYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGSTAMSGGVLWLPNNPLMKAAGVPDSHE
DALAYLDAVVGDQGPASSPERREAYLRAGPAMVSFLEHQGMRFARCEGWSDYYPDLPGGEARGRSLEAKP
FDARKLGPWFDRLNPPMATPPGTVVMTDEYKWLQLIKRTPRGMRTAARVGARTLAARIRGQKLLTNGAAL
IGRMLEAALAAGVPLWTNTPLTELIVEDGRVVGVVVVRDGREVLIRARRGVLLASGGFGHNAEMRKRYQP
QPNSGDWTNANPGDTGEVIEAAMRLGAALDLMDEAWWVPGAPLPNGGPRPYMHNSERSKPGSIIVDRAGR
RFVNEAGSYMEVGRAMYAQDAVPAWMIMDSRYRKRYLFGTIPPGPTPQEWLDSGYMKRADTIEELAGKTG
IDPAGLAATVERFNGFAATGTDPDFHRGESAYDRYYGDPTNKPNPSLGPLDKPPFYAVRMVPGDVGTSGG
LLTDEHARVLREDGSVIPGLYATGNCTASVMGRTYPGAGASIGNSFVFGYIAALHAAGARSADPPPT
>gnl|CDD|237226 PRK12845, PRK12845, 3-ketosteroid-delta-1-dehydrogenase; Reviewed
AHSATIPAGTPVRDTTVDLLVVGSGTGMAAALAAHELGLSVLIVEKSSYVGGSTARSGGAFWLPASPVLD
EAGAGDTLERARTYLDSVVGGSAPAERSAAFLDNGSATVDMLRRTTPMRFFWARGYSDYHPEQPGGSAAG
RTCECRPFDTAVLGEYRPRLRPGVMEVSIPMPVTGADYRWLNLMARVPRKALPRIAKRLAQGVGGLALGR
RYAAGGQALAAGLFAGVLRAGIPIWTETSLVRLTDDGGRVTGAVVDHRGREVTVTARRGVVLAAGGFDHD
MEMRWKFQSESLGEHASLGAEGNTGDAIRIAQDLGAAIGLMDQAWWFPAVAPLPGGAPAVMLAERSLPGS
LIVDQTGRRFVNEATDYMSFGQRVLERERAGDPVESMWIVFDQQYRNSYVFAAELFPRMPIPQAWYDAGI
AHRADSLADLARKIGVPVDTFVATMRRFNEMAAAGVDSDFGRGRSAYDRYYGDPTVTPNPNLRPLDKGPF
YAVKMVLSDLGTCGGLRADERARVLREDGSVIDGLYAIGNTAANAFGATYPGAGATIGQGLVYGYIAAQD
AAAR
>gnl|CDD|237227 PRK12846, PRK12846, peptide deformylase; Reviewed
MAVRPILKMPDPRLRRPAEPVTAFDTEELQALIDDMFETMRAADGVGLAAPQIGVSLRVVVIDLGDDRVP
PTVLINPEITELSPEEEVGWEGCLSVPGLRGEVERPARVRVRAQDRDGKPIEIEAEGFLARVLQHEIDHL
DGILYTDRLSRLKRERALKKVEKYD
>gnl|CDD|237230 PRK12849, groEL, chaperonin GroEL; Reviewed
MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGA
QLVKEVASKTNDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGS
EEIAQVATISANGDEEIGELIAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERM
EAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGF
GDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAKRVTITKDNTTIVDGAGDKEAIEARVAQIRR
QIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALNATRAAVEEGIVPGGGVALLR
AAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAATGEYGDLIAA
GIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDPPGGMGGMGGMGHM
>gnl|CDD|237231 PRK12850, groEL, chaperonin GroEL; Reviewed
MAAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMG
AQMVKEVASKTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTS
SKEIAQVATISANGDESIGEMIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEK
MRAELEDPYILLHEKKISNLQDLLPILEAVVQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPG
FGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAKRVLITKENTTIIDGAGDKKNIEARVKQIR
AQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALHATRAAVEEGIVPGGGVALL
RARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQTGEYGDMVE
AGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAAAAGPGPGMGGMGY
>gnl|CDD|171770 PRK12851, groEL, chaperonin GroEL; Reviewed
MAAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMG
AQMVREVASKTNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTT
NAEIAQVATISANGDAEIGRLVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADK
MEAELEDPYILIHEKKISNLQDLLPVLEAVVQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPG
FGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAKKVVVEKENTTIIDGAGSKTEIEGRVAQIR
AQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALHATRAAVEEGIVPGGGVALL
RAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAATNEYGDLYA
QGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPAPPGGGMDF
>gnl|CDD|237232 PRK12852, groEL, chaperonin GroEL; Reviewed
MAAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMG
AQMVREVASKTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVAS
SAEIAQVGTISANGDAAIGKMIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEK
MTVELDDAYILLHEKKLSGLQAMLPVLEAVVQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPG
FGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAKKVVIDKENTTIVNGAGKKADIEARVGQIK
AQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQEGIVPGGGVALL
RAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSETFGFDAQTEEYVDMV
AKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAAPAMPAGGGMGGMGF
>gnl|CDD|237233 PRK12853, PRK12853, glucose-6-phosphate dehydrogenase
ADTAPAPPCTLVIFGATGDLARRKLLPALYRLARAGLLPEDLRIIGVGRDDWSDEQWRARVRESLRAFGA
DGFDDAVWDRLAARLSYVQGDVTDPADYARLAEALGPGGNPVFYLAVPPSLFAPVVENLGAAGLLPEGRR
VVLEKPFGHDLASARALNATLAKVFDEDQIYRIDHFLGKETVQNLLALRFANALLEPLWNRNHIDHVQIT
VAETLGVEGRGGFYDATGALRDMVQNHLLQLLALVAMEPPASFDADAVRDEKAKVLRAIRPLDPDDVHTV
RGQYTAGTVGGEPVPGYREEPGVDPDSRTETFVALKLEIDNWRWAGVPFYLRTGKRLAERRTEIVITFKP
VPHALFRGTGVEPPNRLVIRLQPDEGISLELNVKRPGPGMRLRPVELDADYADDERPLEAYERLLLDVLR
GDPTLFVRADEVEAAWRIVDPVLDAWAADPVPPHEYPAGSWGPAAADALLARDGRGWREPAA
>gnl|CDD|237234 PRK12854, PRK12854, glucose-6-phosphate 1-dehydrogenase; Provisional
RTAQGTGPAPPTVFVLFGATGDLAKRKLLPGLFHLARAGLLPPDWRIVGTGRGDVSAEAFREHARDALDE
FGARKLDDGEWARFAKRLRYVPGGFLSAGPGALAAAVAAARAELGGDARLVHYLAVPPSAFLDVTRALGE
AGLAEGSRVVMEKPFGTDLASAEALNAAVHEVFDESQIFRIDHFLGKEAAQNILAFRFANGLFEPIWNRE
FIDHVQIDVPETLGVDTRAAFYDATGAYRDMVVTHLFQVLAFVAMEPPTALEPDAISEEKNKVFRSMRPL
DPAEVVRGQYSGYRDEPGVAPDSTTETFVALKVWIDNWRWAGVPFYLRTGKRMAEGQRIISIAFREPPYS
MFPAGSVGAQGPDHLTFDLADNSKVSLSFYGKRPGPGMRLDKLSLQFSLKDTGPKGDVLEAYERLILDAL
RGDHTLFTTADGIESLWEVSQPLLEDPPPVKPYAPGSWGPNAIHQLAAPDAWRLPFEREWRELG
>gnl|CDD|171774 PRK12855, PRK12855, hypothetical protein; Provisional
MIVTTTSTIQGKEIIEYVDIVNGEAIMGANIVRDLFASVRDVVGGRSGAYESKLKEARDIAMEEMKTLAR
QKNANAIVGIDVDYEVVREGMLMVAVSGTAVRI
>gnl|CDD|105987 PRK12856, PRK12856, hypothetical protein; Provisional
MIVTTTSGIQGKEIIEYIDIVNGEAIMGANIVRDLFASVRDVVGGRAGSYESKLKEARDIAMDEMKELAK
QKGANAIVGVDVDYEVVRDGMLMVAVSGTAVRI
>gnl|CDD|237235 PRK12857, PRK12857, class II fructose-1,6-bisphosphate aldolase
MMLVTVAELLKKAEKGGYAVGAFNCNNMEIVQAIVAAAEAEKSPVIIQASQGAIKYAGIEYISAMVRTAA
EKASVPVALHLDHGTDFEQVMKCIRNGFTSVMIDGSKLPLEENIALTKKVVEIAHAVGVSVEAELGKIGG
TEDDITVDEREAAMTDPEEARRFVEETGVDALAIAIGTAHGPYKGEPKLDFDRLAKIKELVNIPIVLHGS
SGVPDEAIRKAISLGVRKVNIDTNIREAFVARLREVLEKNPDEIDPRKILGPAREAAKEVIREKIRLFGS
AGKA
>gnl|CDD|237236 PRK12858, PRK12858, tagatose 1,6-diphosphate aldolase; Reviewed
KLTAGKLRGLKALADERGVIAAAAMDQRGSLKKMLAKARGDEASYTDLVDFKLAVSEALTPYASAILLDP
EYGLPAAKVRDPNCGLLLSYEKTGYDATAPGRLPDLLDNWSVRRIKEAGADAVKLLLYYRPDEDDAINDR
KHAFVERVGAECRANDIPFFLEPLTYDGKGSDKKAEEFAKVKPEKVIKTMEEFSKPRYGVDVLKVEVPVD
MKFVEGFDGFEEAYTQEEAFKLFREQSDATDLPFIFLSAGVSPELFRRTLEFACEAGADFSGVLCGRATW
QDGIEPYAAEGEEARRAWLNTEGVANITRLNEVLERTATPWKDKYGGKDGIEVNDLPARY
>gnl|CDD|183797 PRK12859, PRK12859, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
MNQLKNKVAVVTGVSRLDGIGAAICKELAEAGADIFFTYWTAYDKEMPWGVDQDEQIQLQEELLKNGVKV
SSMELDLTQNDAPKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFAR
GFDKKSGGRIINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMTEEI
KQGLLPMFPFGRIGEPKDAARLIKFLASEEAEWITGQIIHSEGGFK
>gnl|CDD|237237 PRK12860, PRK12860, flagellar transcriptional regulator FlhC
MLRKSLLQDAQEIRLAIELIGLGARLQVLESETTLSRDRLIRLYKEVRGVSPPKGMLPFSTDWFMTWLAN
IHASLFYNAYRFLKNEARCSGLDALTKGYRLYLEHCCATGTEPVLDLTRAWTLVRFFDAGMLQLARCCRC
GGKFVTHAHDLRHNFVCGLCQPPSRAGKTKKAAPAAADALAAAARAQAA
>gnl|CDD|183798 PRK12861, PRK12861, malic enzyme; Reviewed
MKQTETQRQAALDYHEFPTPGKISVVASKPLVTQRDLALAYTPGVASACEEIAADPLNAFRFTSRGNLVG
VITNGTAVLGLGNIGALASKPVMEGKAVLFKKFAGIDVFDIEINETDPDKLVDIIAGLEPTFGGINLEDI
KAPECFTVERKLRERMKIPVFHDDQHGTAITVSAAFINGLKVVGKSIKEVKVVTSGAGAAALACLDLLVD
LGLPVENIWVTDIEGVVYRGRTTLMDPDKERFAQETDARTLAEVIGGADVFLGLSAGGVLKAEMLKAMAA
RPLILALANPTPEIFPELAHATRDDVVIATGRSDYPNQVNNVLCFPYIFRGALDVGATTITREMEIAAVH
AIAGLAEEEQNDVVAAAYGAYDVSFGPQYLIPKPFDPRLIVRIAPAVAKAAMEGGVATRPIADLDAYVEQ
LQQFVYHSGAFMKPLFAAARQLVRDGGKARIVFTEGEDERVLRAVQVIVDEKLARPILVGRPEVLLARIE
RFGLRLRLGQDVEVTNPEYDERFPQYWTTYWELRCRDGISKEMARVEMRRRLTLIGAMMVRLGDADGMIC
GTVGEYHNHLRFVDEVIGRKPGASTYAAMNILLLDQRTVALVDTHVNDNPDAEQIAEFTIAAARQMEWLN
LTPKVALLSRSNFGSGSAASGVKMRRALEIVREQAPDLEADGEMHGDCALDEGLRARLLPMSPLKGAANL
LVCPNVDAGNIAYNLLKTEAGSNVAVGPFLLGVNAPVNILTSSATVRRIVNMAALTVIEANRNV
>gnl|CDD|183799 PRK12862, PRK12862, malic enzyme; Reviewed
TSSDASAKAELREAALDYHRFPTPGKIEIAPTKPLANQRDLALAYSPGVAAPCLEIAADPANAARYTSRG
NLVAVVSNGTAVLGLGNIGPLASKPVMEGKAVLFKKFAGIDVFDIELDESDPDKLVEIVAALEPTFGGIN
LEDIKAPECFYIERELRERMKIPVFHDDQHGTAIIVAAALLNGLKLVGKDIEDVKLVASGAGAAALACLD
LLVSLGVKRENIWVTDIKGVVYEGRTELMDPWKARYAQKTDARTLAEVIEGADVFLGLSAAGVLKPEMVK
KMAPRPLIFALANPTPEILPEEARAVRPDAIIATGRSDYPNQVNNVLCFPYIFRGALDVGATTINEEMKI
AAVRAIAELAREEQSDVVAAAYGGEDLSFGPDYLIPKPFDPRLILKIAPAVAQAAMDSGVATRPIEDMDA
YREQLNQFVYHSGLIMKPVFAAAKAAPKRVVFAEGEDERVLRAAQVVVDEGLAKPILIGRPAVIEARIER
AGLRLRPGVDFEIVNPEDDPRYRDYWDTYHALMGRKGVTPEMARREVRRRTTLIGAMMVKRGEADAMICG
TEGRYERHLEFVLQVIGKRPGVRVYAAMSLLILPGRTLFLADTHVNEDPTAEELAEITILAAEEVRRFGI
EPKVALLSHSNFGSSDSPSARKMREALEILRERAPDLEVDGEMHGDAALDEELRDRIFPDSRLEGEANLL
VFPNLDAANIAYNLLKTAAGNGLAVGPILLGAAKPVHILTPSATVRRIVNMTALAVADANAYR
>gnl|CDD|183800 PRK12863, PRK12863, YciI-like protein; Reviewed
MLFAILCTDKPGHLEVRLATRPAHLAYLETLEGRLLAAGPLLDDDGKPMVGSLVVVEAESRAAAEAFAAA
DPFAKAGLYESVDIKPFNKAFGNG
>gnl|CDD|183801 PRK12864, PRK12864, YciI-like protein; Reviewed
MAKFVLWGTYCEDALEKRAPFREAHLDRLAKLKEQGILITLGPTKDLTYVFGIFEAEDEETVRQLIEADP
YWQNGIWTEYEVYPWIQAF
>gnl|CDD|171782 PRK12865, PRK12865, YciI-like protein; Reviewed
MLFALLCKDKPGHLNVRMDTRPTHLEYLNKLNAEGTLKIAGPFLDDDGKPCGSLVIVKAETKEAAKALAD
ADPYAKAGLFESVEVKAYNWVFNNPEA
>gnl|CDD|237238 PRK12866, PRK12866, YciI-like protein; Reviewed
MHYLLTYDLVDDYLERREAYRAEHLALAQAATERGELLLAGALADPADGAVLVFEGDSPAAAEAFARADP
YVRNGLVKSWRVRPWTVVVGKEAAPPV
>gnl|CDD|106000 PRK12871, ubiA, prenyltransferase; Reviewed
MKETLKAYIDLTRAHFLPAWPLLFCSGLVLAFANYGGFSWELTIKAALIGLFGFEAGFVLNDYVDRKRDR
LDVENTLTRYWRPFKERPIPSGKLSSKNAFALFILLAAVTSALILTLPYPNSLYVFVIMLYSYGIEAFYQ
VKKRNQKYPVAQLLGRTDFTLFPAAGYLCYGQPDMTALLYMVFFYPWTMAHLGLNDFIDLENDRARGMKS
IAVLYGMKGTMYWVTGFTALHFLAAIFFLRELGPIALYGFLAGFVLLAGANLYLWKEKSQDAGMKILPLY
HASLVIYAVSIILDFIY
>gnl|CDD|237241 PRK12872, ubiA, prenyltransferase; Reviewed
RKLLFAFLKLFRYGNLLIAALGQSLVYMASLLLGLPISWLLLLITFLIAAAVYIINYLTDLEEDIINKPE
RVVFSETKAYGLFLLLNVLGLYLGAYLLAVIGGPKFALIFIIPLILGILYSVFFKRRLKRIPLFKNLVVS
LLWALSPLILGVYYYQLTIFSLLLLYAVFIFLKSFIREIVFDIKDIEGDRKSGLKTLPIVLGKERTLKFL
LILNLLFLILLILGVYTGLLPLLLLVLLLLLAYVLYYIIKLFAADDKKDLLYLSLLDKEHMLLGLISMLL
GLLVL
>gnl|CDD|171787 PRK12873, ubiA, 4-hydroxybenzoate polyprenyltransferase
KSRSIKLSPWFELLRWNKPTGRLILLIPAGWSLWLTPSAPPSLLLLLLIILGGLAVSGAGCIANDLWDRR
IDRKVERTKNRPLARGKISLKTAYSLLIVLLLLSLFVVLSLPQPSRNLCLSLAFLALPPILIYPSAKRWF
AYPQAILALCWGFAVLIPWAAAEGSLNGGWPLLFCWLATLLWTFGFDTVYAMADRRDDAKIGLNSSALSL
GSNALKTVQICYFLTSIFLALAAFIAQVGFIFWPFWLIASIGMQRDILKLFPEKQSIKTIGNHFSNQVIL
GSLLLLGLILARGG
>gnl|CDD|237242 PRK12874, ubiA, 4-hydroxybenzoate polyprenyltransferase
MKKFTKKLKDISELVVFKHSIFSLPFIFIAMIVASKQKNDTGWFGFKLLILGILAAVSARNFAMAFNRLV
DRDIDKDNPRTANRPSVDGRISVKSMVLFIVLNALIFIGVSYFINPLAFKLSFPFLIVLGGYSYFKRFSS
LAHLVLGLSLGLAPIAGVVAVLGEIPLWSVFLALGVMFWVAGFDLLYSLQDMEFDKKRGLHSIPSKFGEK
ATLFISRLFHLLAVLFWLLFVWCAHLGLFAYLGVIVSALILLYEHYLVRKDFKKIDKAFFTLNGYLGIVF
FIFIVLDVLFK
>gnl|CDD|237243 PRK12875, ubiA, prenyltransferase; Reviewed
MNSLGDRLRYLLVLSRPRFWLYLAGPVVVGVAYAADSVADLFSPAAVALFAYFLFPANVFLYGVNDVFDA
DTDELNPKKDREREVRYRGDRRVLVAVALSGALALAFLLVLPPAAWPALLAFLVLSVEYSAPPLRFKTTP
VLDSLSNGLYILPGVAAYALVSGSLPPLLAVAGGWLWAMGMHTFSAIPDIEPDRAAGIRTTATVLGERRT
YAYCAACWLLAAAAFAAVDLRLGALLLVYPALVLAILRAGIAVDRAYWWFPAINTVVGMLLTLGGLWRLV
YG
>gnl|CDD|237244 PRK12876, ubiA, prenyltransferase; Reviewed
MMRIKYFQQLINCKYALFSALFLSASTVFALSLPEISFSLFSLGGIKTISLGGSAFFCARTVGIIVNQII
DCAIDKKNPRTSSRVLPAKLLSINFSMLLLTLCSFLFLSLCWLLNPLCFSLAVLSTLLMIIYPYTKRVTF
LCHWILGLVYYLAILMNFFAIIETPLSFSLFCMASLWGISFGMIIAANDIIYAIQDLEFDRKEGLFSIPA
RFGEKKAIRIASANLIASAIAYLLIGYFVSNKKIFYLCSLVPLTVILKTIKHYSLIDKKKSTLEQKFFLG
NIYLALSFFVNMIGLFLLRG
>gnl|CDD|237245 PRK12879, PRK12879, 3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
MMSYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHVEEYTSDLAIKAAERALARAGL
DAEDIDLIIVATTTPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIG
AERLSKVTDYTDRTTCILFGDGAGAVVLEATENEPGFIDYVLGTDGDGGDILYRTGLGTTMDRDALSGDG
YIVQNGREVFKWAVRTMPKGARQVLEKAGLTKDDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYG
NTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAALLVKWG
>gnl|CDD|171793 PRK12880, PRK12880, beta-ketoacyl-ACP synthase III
MKTRFDKAKISGICVSVPEHKICIDDELESVFSNDIKTLKRMKKVIGLNTRYICDENTCVSDLGKHAANT
LLQGLNIDKNSLDALIVVTQSPDFFMPSTACYLHQLLNLSSKTIAFDLGQACAGYLYGLFVAHSLIQSGL
GKILLICGDTLSKFIHPKNMNLAPIFGDGVSATLIEKTDFNEAFFELGSDGKYFDKLIIPKGAMRIPKAD
IFNDDSLMQTEEFRQLENLYMDGANIFNMALECEPKSFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKE
ELKLNDDKVPNFIMEKYANLSACSLPALLCELDTPKEFKASLSAFGAGLSWGSAVLNFKDLYTKDILIYT
KEK
>gnl|CDD|237246 PRK12881, acnA, aconitate hydratase AcnA
MAHNLHKTLKEFDVGGKTYKFYSLPALGKELGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWL
PERKSDDEIPFVPARVVMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKD
ALDLNMKIEFQRNAERYQFLKWGMQAFDNFRVVPPGTGIMHQVNLEYLARVVHTKEDDGDTVAYPDTLVG
TDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGV
VGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRLTGRTEAQIALVEAYAKAQGLW
GDPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPVAENGFAKKAQTSNGVDLPD
GAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEKLGF
GIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLVVAYALAGTV
RRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDW
DPKSTYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADF
NSYGSRRGNHEVMMRGTFANVRIKNLMIPGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYG
TGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEGLPGEIK
PRQDVTLVIHRADGSTERVPVLCRIDTPIEVDYYKAGGILPYVLRQLLA
>gnl|CDD|183811 PRK12882, ubiA, prenyltransferase; Reviewed
GMTVRGYLELTRPVNAVVAGVAAFIGAFIAGGILSSPSLTGLAFAAVFLATGAGNAINDYFDREIDRINR
PDRPIPSGAVSPRGALAFSILLFAAGVALAFLLPPLCLAIALFNSLLLVLYAETLKGTPGLGNASVAYLT
GSTFLFGGAAVGTEGLLALLVLFALAALATLAREIIKDVEDIEGDRAEGARTLPILIGVRKALYVAAAFL
LVAVAASPLPYLLSTFGLWYLVLVAPADLVMLAAAYRSLKKTDPTASQKLLKYGMFLALAAFIVGR
>gnl|CDD|171796 PRK12883, ubiA, prenyltransferase UbiA-like protein; Reviewed
MELKAFIEITRPHNCILAGIVGILGSLVALGGIPPIKTLILIFLVVYLGCSGGNTINDYFDYEIDKINRP
NRPLPRGAMSRKAALYYSLLLFAVGLALAYLINIEAFLFALGAYVLMFLYAWKLKPLPFIGNVVVALLTG
ATPIYGAIAVGRIGLAGYLAICAFLVNVAREIMKDIEDIEGDKAKGAKTLPIIIGKKRAAYIGAIFGVLT
VIASFLPVKAGIGLGYLPIIIVDAIILYAAYLVLRNPDRETAHKGQKLLKIAIFLAVISFLLGALTK
>gnl|CDD|183812 PRK12884, ubiA, prenyltransferase; Reviewed
RTKMKAYLELLRPEHGLMAGIAVVLGAIIALGGLPLDEALLGFLTAFFASGSANALNDYFDYEVDRINRP
DRPIPSGRISRREALLLAILLFILGLIAAYLISPLAFLVVILVSVLGILYNWKLKEYGLIGNLYVAFLTG
MTFIFGGIAVGELNEAVILLAAMAFLMTLGREIMKDIEDVEGDRLRGARTLAILYGEKIAGRIAAALFIL
AVLLSPLPYLFGIFNILYLAPVLVADLIFLYSAYSLLRSQDRETIRKVRKITLTAMLLALVAFALGAIT
>gnl|CDD|237247 PRK12886, ubiA, prenyltransferase; Reviewed
MMTLLTKLKVFLEMIKFSHTLFALPFAGIGAVLAALGLPGASQLDWILMAMVGARTAAMGFNRLIDAEID
ARNPRTAGRAIPAGLISKGSAILFIVLSSLLMLFAAWFLNPLCLYLSPPALFFLLLYSYCKRFTALAHVV
LGFCLALAPLGAWIAIRGTIELPAILLGLAVLFWVAGFDILYALQDLEFDRKEGLHSIPAKLGVNGSLWI
ARVFHLLMIGFLFALGISAGLGPWFLAGLAVTGILLLYEHWLLRGGDLTRLDAAFFNMNGYISVTLFAAT
LFDRLFYFGGL
>gnl|CDD|183813 PRK12887, ubiA, tocopherol phytyltransferase; Reviewed
LPKNPLQPMTSWLYALWKFSRPHTIIGTSLSVLGLYLIAIAASSNTIALANLGLLLGAWIACLCGNVYIV
GLNQLTDIEIDRINKPHLPLAAGEFSRRQGQRIVIITGILALILAALLGPWLLITVGISLLIGTAYSLPP
IRLKRFPLLAALCIFTVRGVIVNLGLFLHFQWLLGGSVLIPPTVWLLTLFVLVFTFAIAIFKDIPDMEGD
RQYQITTFTLRLGKQAVFKLSCWVLTACYLGMIAVGLLSLPTVNPAFLIVSHLILLALLWWRSQRVDLQD
KQAIAQFYQFIWKLFFLEYLLFPIACLL
>gnl|CDD|183814 PRK12888, ubiA, 4-hydroxybenzoate octaprenyltransferase
RVRAFLRLVAIEHSVFALPFAYIAALTAMFASDGSVHWADLLLVTVAMVGARTFAMAANRIIDREIDARN
PRTAGRELVTGAVSVRTAWTGALVALAVFLGAAALLNPLCLALAPLAVAPLVVYPYAKRFTNFPHAILGL
AQAVGPVGAWIAVTGTWSWPAVLLGLAVGLWIGGFDLIYACQDAEVDRRIGVRSVPARFGVRAALWASRV
AHVVTFALFVWFGLAVGFGALWWIGLAITAGAFAYEHAIVSPTDLSRVNRAFFTANGFVGIALFGFALLD
LLVR
>gnl|CDD|237248 PRK12890, PRK12890, allantoate amidohydrolase; Reviewed
TTPPPINGERLLARLEELAAIGRDGPGWTRLALSDEERAARALLAAWMRAAGLEVRRDAAGNLFGRLPGR
DPDLPPLMTGSHLDTVPNGGRYDGILGVLAGLEVVAALREAGIRPPHPLEVIAFTNEEGVRFGPSMIGSR
ALAGTLDVEAVLATRDDDGTTLAEALRRIGGDPDALPGALRPPGAVAAFLELHIEQGPVLEAEGLPIGVV
TAIQGIRRQAVTVEGEANHAGTTPMDLRRDALVAAAELVTAMERRARALLHDLVATVGRLDVEPNAINVV
PGRVVFTLDLRSPDDAVLEAAEAALLAELEAIAAARGVRIELERLSRSEPVPCDPALVDAVEAAAARLGY
PSRRMPSGAGHDAAAIARIGPSAMIFVPCRGGISHNPEEAMDPEDLAAGARVLLDAVLRLDRQL
>gnl|CDD|237249 PRK12891, PRK12891, allantoate amidohydrolase; Reviewed
SARAPRVDGERLWASLERMAQIGATPKGGVCRLALTDGDREARDLFVAWARDAGCTVRVDAMGNLFARRA
GRDPDAAPVMTGSHADSQPTGGRYDGIYGVLGGLEVVRALNDAGIETERPVDVVIWTNEEGSRFAPSMVG
SGVFFGVYPLEYLLSRRDDTGRTLGEHLARIGYAGAEPVGGYPVHAAYELHIEQGAILERAGKTIGVVTA
GQGQRWYEVTLTGVDAHAGTTPMAFRRDALVGAARMIAFLDALGRRDAPDARATVGMIDARPNSRNTVPG
ECFFTVEFRHPDDAVLDRLDAALRAELARIADETGLRADIEQIFGYAPAPFAPGCIDAVRDAARALGLSH
MDIVSGAGHDACFAARGAPTGMIFVPCVDGLSHNEAEAITPEWFAAGADVLLRAVLQSAQEAGA
>gnl|CDD|183817 PRK12892, PRK12892, allantoate amidohydrolase; Reviewed
SLAMLRIDGQRVLDDLMELAAIGAAKTGVHRPTYSDAHVAARRRLAAWCEAAGLAVRIDGIGNVFGRLPG
PGPGPALLVGSHLDSQNLGGRYDGALGVVAGLEAARALNEHGIATRHPLDVVAWCDEEGSRFTPGFLGSR
AYAGRLDPADALAARCRSDGVPLRDALAAAGLAGRPRPAADRARPKGYLEAHIEQGPVLEQAGLPVGVVT
GIVGIWQYRITVTGEAGHAGTTPMALRRDAGLAAAEMIAAIDEHFPRVCGPAVVTVGRVALDPGSPSIIP
GRVEFSFDARHPSPPVLQRLVALLEALCREIARRRGCRVSVDRIAEYAPAPCDAALVDALRAAAEAAGGP
YLEMPSGAGHDAQNMARIAPSAMLFVPSKGGISHNPAEDTSPADLAQGARVLADTLRRLARG
>gnl|CDD|237250 PRK12893, PRK12893, Zn-dependent hydrolase
MGRNLRINGERLWDSLMALARIGATPGGGVTRLALTDEDREARDLLAQWMEEAGLTVSVDAIGNLFGRRA
GTDPDAPPVLIGSHLDTQPTGGRFDGALGVLAALEVVRTLNDAGIRTRRPIEVVSWTNEEGARFAPAMLG
SGVFTGALPLDDALARRDADGITLGEALARIGYRGTARVGRRAVDAYLELHIEQGPVLEAEGLPIGVVTG
IQGIRWLEVTVEGQAAHAGTTPMAMRRDALVAAARIILAVERIAAALAPDGVATVGRLRVEPNSRNVIPG
KVVFTVDIRHPDDARLDAMEAALRAACAKIAAARGVQVTVETVWDFPPVPFDPALVALVEAAAEALGLSH
MRMVSGAGHDAMFLARVAPAAMIFVPCRGGISHNEAEDTEPADLAAGANVLLHAVLELAGRA
>gnl|CDD|237251 PRK12895, ubiA, prenyltransferase; Reviewed
MNFRDIVDYIKLEHTVFDLPFILAGYVIAAGHYIHPIKILLILIAAVSARTSAMSINRIEGLRYDMINPR
KKDWALVSGRIKMREAIAFTIIFIAIFEICTFLLNRLVFILSPIVIFLFIIDPFLKRYTAWRHIYMGSII
GLGVLAGYLAVIPAFPYNLLIYIIFISSSLWIAGFDIIYVIPDIEYDKINGLKTIMNTYGIKNGLYISDI
FHISSLILFWISGIYIRTLWYLAALIIIYTLVIYQHLIIDPRNPINKRMSFFNANSFIGFVFLIGIILSL
RFPIRM
>gnl|CDD|237252 PRK12896, PRK12896, methionine aminopeptidase; Reviewed
PAQEGRGMEIKSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEEHGAIPSPEGYYGFP
GSTCISVNEEVAHGIPGPRVIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGI
KQVKAGRPLNDIGRAIEDFAKKNGYSVVRDLTGHGVGRSLHEEPSVILTYTDPLPNRLLRPGMTLAVEPF
LNLGAKDAETLDDGWTVVTPDKSLSAQFEHTVVVTRDGPEILTDR
>gnl|CDD|171806 PRK12897, PRK12897, type I methionyl aminopeptidase
MITIKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYLEKHGATSEQKGYNGYPYAICAS
VNDEMCHAFPADVPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIG
NRVGDIGYAIESYVANEGFSVARDFTGHGIGKEIHEEPAIFHFGKQGQGPELQEGMVITIEPIVNVGMRY
SKVDLNGWTARTMDGKLSAQYEHTIAITKDGPIILTKL
>gnl|CDD|237253 PRK12898, secA, preprotein translocase subunit SecA; Reviewed
LPPPRYYRERKDLQASRLDRWLERVLGRLAGRVRGRAARRQRLLADRVLAAAEALAGLSEEALRARSLAL
RARLRARDGFRDALLAEAFALVREASGRVLGQRHFDVQLMGGLALLSGRLAEMQTGEGKTLTATLPAGTA
ALAGLPVHVITVNDYLAERDAELMRPLYEALGLTVGCVVEDQSPDERRAAYGADITYCTNKELVFDYLRD
RLALGQRASDARLALESLHGRSSRSTQLLLRGLHFAIVDEADSVLIDEARTPLIISAPAKEADEAEVYRQ
ALELAAQLKEGEDYTIDAAEKRIELTEAGRARIAELAESLPPAWRGAVRREELVRQALSALHLFRRDEHY
IVRDGKVVIVDEFTGRVMPDRSWEDGLHQMIEAKEGCELTDPRETLARITYQRFFRRYLRLAGMTGTARE
VAGELWSVYGLPVVRIPTNRPSQRRHLPDEVFLTAAAKWAAVAARVRELHAQGRPVLVGTRSVAASERLS
ALLREAGLPHQVLNAKQDAEEAAIVARAGQRGRITVATNMAGRGTDIKLEPGVAARGGLHVILTERHDSA
RIDRQLAGRCGRQGDPGSYEAILSLEDDLLQSFLGSRGLAIRRMELLGPRGGRALGALLLRRAQRRAERL
HARARRALLHADEQLDKLLAFAGRGE
>gnl|CDD|237256 PRK12901, secA, preprotein translocase subunit SecA; Reviewed
MNEFLKKLFGDKSERDLKEIQPIVEKIKAEYPELEALSNDELRAKTDEFKQYIKEAVADIDAKIEELKAE
AIESLDIDEREDIYAQIDKLEKEAYEILEKVLDEILPEAFAIVKETARRFAENEEIEVTATDFDRELAAT
KDFVTIEGDKAIWKNHWDAGGNEITWDMVHYDVQLIGGVVLHQGKIAEMATGEGKTLVATLPVYLNALTG
NGVHVVTVNDYLAKRDSEWMGPLYEFHGLSVDCIDKHQPNSEARRKAYNADITYGTNNEFGFDYLRDNMA
HSPEDLVQRKHNYAIVDEVDSVLIDDARTPLIISGPVPKGDDQEFEELKPRVERLVEAQRKLATQFLAEA
KKLIAEGDKKEGGLALLRAYRGLPKNKALIKFLSEEGIKALLQKTENFYMQDNNREMPEVDEELYFVIDE
KNNSVELTDKGIDYITGNDEDPDFFVLPDIGTELAEIENEGGLDEEEEAEKKEELFQDYSVKSERVHTLN
QLLKAYTLFEKDDEYVVMDGKVKIVDEQTGRIMEGRRYSDGLHQAIEAKENVKIEAATQTFATITLQNYF
RMYHKLAGMTGTAETEAGEFWDIYKLDVVVIPTNRPIARKDKEDLVYKTKREKYNAVIEEITELSEAGRP
VLVGTTSVEISELLSRMLKMRKIPHNVLNAKLHQKEAEIVAEAGQPGTVTIATNMAGRGTDIKLSPEVKA
AGGLAIIGTERHESRRVDRQLRGRAGRQGDPGSSQFYVSLEDNLMRLFGSERIAKVMDRMGLKEGEVIQH
SMISKSIERAQKKVEENNFGIRKRLLEYDDVMNSQREVIYKRRRHALMGERLGMDIANMIYDVCEAIVEN
NKVANDYKGFKFELIRTLAMESPITEEEFNKLKKDELTDKLYDAALENYQRKMERIAEIAFPVIKQVYEE
QGNMYERIVVPFTDGKRTLNVVTNLKEAYETEGKEIVKDFEKNITLHIIDEAWKEHLREMDELKQSVQNA
SYEQKDPLLIYKFESFELFKNMVDKVNREVISFLFKGEIPVQEAPEIREAAPERRLDPKYRTQKEEIQDS
DQRAAASRDTGAQVKETPVRVEKKIGRNDPVPCQNVDGGSGKKYKFKHAENLINSGKWVLVE
>gnl|CDD|237258 PRK12903, secA, preprotein translocase subunit SecA; Reviewed
MKFLKLFFFKSTEMRIAEKILKQINDLEPYYRNLTDEELANKTNEFKDRLKNGETLEDIRVEAFAVAREA
TKRVLGKRPYDVQIIGGIILDLGSVAEMKTGEGKTITSIAPVYLNALTGKGVIVSTVNEYLAERDAEEMG
KVFNFLGLSVGINKANMDPNLKREAYACDITYSVHSELGFDYLRDNMVSSKEEKVQRGLNFCLIDEVDSI
LIDEAKTPLIISGGQSNDSNLYLAADQFVRTLKEDDYKIDEETKAISLTEKGIKKANKFFKLKNLYDIEN
SELVHRIQNALRAHKVMKEDVEYIVRDGKIELVDQFTGRIMEGRSYSEGLQQAIQAKEMVEIEPETKTLA
TITYQNFFRLFKKLSGMTGTAKTEEQEFIDIYNMRVNVVPTNKPVIRKDEPDSIFGTKHAKWKAVVKEVK
RVHKKGQPILIGTAQVEDSETLHELLLEANIPHTVLNAKQNAREAEIIAKAGQKGAITIATNMAGRGTDI
KLSKEVLELGGLYVLGTDKAESRRIDNQLRGRSGRQGDVGESRFFISLDDQLFRRFSNFDKIKEAFKKLG
DDEIKSKFFSKALLNAQKKIEGFNFDTRKNVLDYDDVIRQQRDLIYAQRDLILIADDLSHVIEKMISRAV
EQILKNSFIILKNNTINYKELVEFLNDNLLRITHFKFSEKDFENYHKEELAQYLIEALNEIYFKKRQVIL
DKIALNTFFESERYIILSALDKYWQNHIDTMDKLRSGVNLVQYSQKNPYQVYTEEGTKKFNILLQEIAYD
VIVSLFNNPNAEKILIITEILSDGINNSDINDRPQELIDQIIESEEERLKALRIQREEMLMRPEELELIN
EEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEFKNDPKKLNKLIIAKDVLIKLVISSDEIKQDEKT
TKKKKKDLEKTDEEA
>gnl|CDD|237259 PRK12904, PRK12904, preprotein translocase subunit SecA; Reviewed
MLGLLKKIFGSRNDRELKRLRKIVDKINALEPEMEKLSDEELKAKTAEFKERLAKGETLDDLLPEAFAVV
REASKRVLGMRHFDVQLIGGMVLHEGKIAEMKTGEGKTLVATLPAYLNALTGKGVHVVTVNDYLAKRDAE
WMGPLYEFLGLSVGVILSGMSPEERREAYAADITYGTNNEFGFDYLRDNMVFSLEERVQRGLNYAIVDEV
DSILIDEARTPLIISGPAEDSSELYKRANKIVPTLEKEGDYTVDEKSRTVGLTEEGIEKAEKLLGIENLY
DPENIALVHHLNQALRAHELFKRDVDYIVKDGEVVIVDEFTGRLMPGRRYSDGLHQAIEAKEGVKIQNEN
QTLASITFQNYFRMYEKLAGMTGTADTEAEEFREIYNLDVVVIPTNRPMIRIDHPDLIYKTEKEKFDAVV
EDIKERHKKGQPVLVGTVSIEKSELLSKLLKKAGIPHNVLNAKNHEREAEIIAQAGRPGAVTIATNMAGR
GTDIKLGGNPEMLAAALLEEETEEQIAKIKAEWQEEHEEVLEAGGLHVIGTERHESRRIDNQLRGRSGRQ
GDPGSSRFYLSLEDDLMRIFGSDRVKGMMDRLGMKEGEAIEHKMVTRAIENAQKKVEGRNFDIRKQLLEY
DDVMNDQRKVIYAQRNEILEGEDLSETILDMREDVIEDLVDAYIPPGSYEEDWDLEGLEEALKTDFGLEL
PIEEWLEEGLDEEELRERILEAAEEAYEEKEEELGEEQMREFERVVMLQVLDTKWREHLAAMDHLRQGIG
LRGYAQKDPLQEYKREGFELFEEMLDSIKEEVVRTLMKVQIDPCPCGSGKKYKHCHGRLA
>gnl|CDD|237260 PRK12906, secA, preprotein translocase subunit SecA; Reviewed
MANILKKWFDNDKRELKRLEKIADKVNALEDEYEKLSDEQLQAKTPEFRDRIKDGESLDDLLPEAFAVAR
EGAKRVLGLRPFDVQIIGGIVLHEGNIAEMKTGEGKTLTATLPVYLNALTGKGVHVVTVNEYLSSRDATE
MGELYRWLGLTVGLNLNSMSPDEKRAAYNCDITYSTNSELGFDYLRDNMVVYKEQMVQRPLNYAIVDEVD
SILIDEARTPLIISGQAEKATDLYIRADRFVKTLIKDEAEDGDDDEDTGDYKIDEKTKTISLTEQGIRKA
EKLFGLDNLYDSENTALAHHIDQALRANYIMLKDIDYVVQDGEVLIVDEFTGRVMEGRRYSDGLHQAIEA
KEGVKIQEENQTLATITYQNFFRMYKKLSGMTGTAKTEEEEFREIYNMEVITIPTNRPVIRKDSPDLLYP
TLDSKFNAVVKEIKERHAKGQPVLVGTVAIESSERLSHLLDEAGIPHAVLNAKNHAKEAEIIMNAGQRGA
VTIATNMAGRGTDIKLGPGVKELGGLAVIGTERHESRRIDNQLRGRSGRQGDPGSSRFYLSLEDDLMRRF
GSDRVKAFLDRLGMNDDDQVIESRMITRQVESAQKRVEGNNYDTRKQLLQYDDVMREQREVIYKQRMQVI
NEDKDLKEVLMPMIKRTVDRQVQMYTQGDKKDWDLDALRDFIVSAMPDEETFDFEDLKGKSPEELKKRLL
DIVEDNYAEKEKQLGDPTQMLEFEKVVILRVVDSHWTDHIDAMDQLRQSIGLRGYGQLNPLVEYQEEGYR
MFEEMISNIDYDVTRLFMKAQIRQNI
>gnl|CDD|171815 PRK12911, PRK12911, bifunctional preprotein translocase subunit SecD/SecF; Reviewed
MKQNFKRNLSIIICVFALALYYVLPTCLYYSRPLNKKIDGREARKIIERFTKQVSDARNDLIPRVSKILS
TLKLRGHIKQHPSIPGVVNVHFKLAEDAALFIDNVVHGEPSVPIKSARLYVVGYSEFTGETVVQVSGSLV
TSLTEKDFSFVSYEDEDETVSQELENLATNLFIESERPCSCGYPSIWDTAPIEKVIQVARNLCSGLRLLP
SRKTQAFLSRFFSSERDFTAFLSRLESLSQDEEVKEARQELLDAVYELLHSRACRWNSISPKIVGNVLDC
SELSPFFSSMELTAKERKLLFHLDADVLAKRQQLSGEQRLDFDSLLAVEKQHLATRLNRSVEETEFGFAF
RLRDKDASGKIVLQGHRVCQGIVEHLTALVLNRPAAESCDLITENFPVYCREPRESDAFGCFIFSPERSC
RHFSKGSVYIVLKGLRSIVAKYEQGGAEEAALFQKDLQNLYNCFIHTDAVSWSLGEDRVLEIKEPLQRFI
DVWGEEFVQSFEGKASLEVRDVRDRLATVNRIEKTRQAELVRWHEQYRQAQCSMDPQVRLRAAIPHKNLF
LENLKLNIRKYSRGEHVLRFGIDFVGGKQIRLAFKDHQGKQLTDKEGILKVSDELYARLNKLGVSEVEMR
REGDHIHLSVPGSAGISSAEILGTSKMSFHVVNEQFSSYSALRYEVQRFLDYLWFTARSQDKTSPEAINR
LASALFNGDEGSAPASVREAVTKLKEEGLAFSKSGLEGGSASLDTTYSMIAIEKDSEEKANPLMIVFRNY
ALDGASLKNIRPEFAVGEGYVLNFSVKDTATFSDARELSPTESFHAWTSAYCQEGVSGTKNGQFSGGRGW
RMAVVLDGYVVSDPVLNVPLKDHASVSGKFSHREVHRLATDLKSGAMSFVPEVLSEEVISPELGKSQRTQ
GIISVCLGLAVLIVLMSVYYRFGGVIASGAVLLNLLLIWAALQYLDAPLTLSGLAGIVLAMGMAVDANVL
VFERIREEYLLSRSLSESVEAGYKKAFSAIFDSNLTTILASALLLMLDTGPIKGFALTLIIGIFSSMFTA
LFMTKFFFMIWMNKTQETQLHMMNKFIGIKHDFLKECKRLWVVSGSVLVLGCVALGFGAWNSVLGMDFKG
GYALTLDPSDVCEYDVEQMRSKLRKKFQQIGLSSRDFRIRTFDSSEKIKIYFSQNALDRVEAIEGAGSEQ
SDHHLALVLGVLSDTGSDTSSEVFDATQNFWFKVSGQLSNKMRTQAVIALFGALGIILLYVSLRFEWRYA
FSAICALIHDLLATCAVLVALHFFLQKIQIDLQAIGALMTVLGYSLNNTLIIFDRIREDRQEKLFTPMPI
LINDALQKTLGRTVMTTATTLSVLLILLFVGGGSIFNFAFIMTIGILLGTLSSLYIAPPLLLFMVRKEER
NSL
>gnl|CDD|183829 PRK12921, PRK12921, oxidoreductase
MRIAVVGAGAVGGTFGGRLLEAGRDVTFLVRPKRAKALRERGLVIRSDHGDAVVPGPVITDPEELTGPFD
LVILAVKAYQLDAAIPDLKPLVGEDTVIIPLQNGIGQLEQLEPYFGRERVLGGVVFISAQLNGDGVVVQR
ADHRLTFGEIPGQRSERTRAVRDALAGARLEVVLSENIRQDIWRKLLFNAVMNGMTALGRATVGGILSRP
GGRDLARALLRECLAVARAEGAPLRDDVVEEIVKIFAGAPGDMKTSMLRDMEKGRPLEIDHLQGVLLRRA
RAHGIPTPILDTVYALLKAYEAGPG
>gnl|CDD|237261 PRK12928, PRK12928, lipoyl synthase; Provisional
RSRDKSARIPVERLPEWLRAPIGKASELETVQRLVKQRRLHTICEEARCPNRGECYAQGTATFLIMGSIC
TRRCAFCQVDKGRPMPLDPDEPERVAEAVAALGLRYVVLTSVARDDLPDGGAAHFVATIAAIRARNPGTG
IEVLTPDFWGGQRERLATVLAAKPDVFNHNLETVPRLQKAVRRGADYQRSLDLLARAKELAPDIPTKSGL
MLGLGETEDEVIETLRDLRAVGCDRLTIGQYLRPSLAHLPVQRYWTPEEFEALGQIARELGFSHVRSGPL
VRSSYHAGEQ
>gnl|CDD|183831 PRK12933, secD, protein translocase subunit SecD
MKKQKNKKLLNHYSAWKYVVLIVTIIILLLSAIPTWYGEDAAVQVSAKAGLLLNVVELRQLLQAQGINVK
RIDQKEGKTLIVLDDDSQQSQAKTLLSSMVKEPKELTLSLASAAPKWLQNMGFSPIKLGLDLRGGVQFLL
DVDVDPVYQEQRDALVDSVRQFLREQRIRGVSVRLDDSDQLAVTTPDNDARSAVRQFIQQNYPGWQVTNS
DDRGLQLKLSQQEKTKFRNLTVQQNLQIMRSRIEELGITEALVQRQGEHRIRIELPGVQDPAAAKNVIGA
TASLAFYEVKESGSVNAKVLKDKNGRPVYVARRPVLGGEHIVDARASLGEMGMAEVNISLDRAGGKKMSD
FSRDNIGKPMATSYSEYSRDEQGKTKQSEEVISVATIQSQLGDRFRITGAGSYQEAQQLALLLRAGSLTA
PVTIVEERTIGPSLGAENIENGFAALALGMGITLLFMALWYRRLGWVANVALIANMVCLFGLLALIPGAV
LTLPGIAGLVLTVGMAVDTNVLIFERIKDKLKEGRSFAQAIDTGFDSAFSTIFDANFTTMITAVVLYSIG
NGPIQGFALTLGLGLLTSMFTGIFASRALINLVYGRDARRDVRV
>gnl|CDD|183832 PRK12935, PRK12935, acetoacetyl-CoA reductase; Provisional
MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVED
ANRLVEEAVNHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIIS
ISSIIGQAGGFGQTNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQKIVAKIP
KKRFGQADEIAKGVVYLCRDGAYITGQQLNINGGLYM
>gnl|CDD|171820 PRK12936, PRK12936, 3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
MFDLSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKAL
GQKAEADLEGVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSV
VGVTGNPGQANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQKEAIMGAIPMKRM
GTGAEVASAVAYLASSEAAYVTGQTIHVNGGMAMI
>gnl|CDD|171821 PRK12937, PRK12937, short chain dehydrogenase; Provisional
MTLSNKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEIEAAGGRAIAVQADVADAAAV
TRLFDAAETAFGRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQGGRIINLST
SVIALPLPGYGPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATELFFNGKSAEQIDQLAGLAPLE
RLGTPEEIAAAVAFLAGPDGAWVNGQVLRVNGGFA
>gnl|CDD|171822 PRK12938, PRK12938, 3-ketoacyl-ACP reductase
MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKA
AFDKVKAEVGEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISS
VNGQKGQFGQTNYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEKIVATIPVRR
LGSPDEIGSIVAWLASEESGFSTGADFSLNGGLHMG
>gnl|CDD|183833 PRK12939, PRK12939, short chain dehydrogenase; Provisional
MASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPAS
VQRFFDAAAAALGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVN
LASDTALWGAPKLGAYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPADERHAYYLKGR
ALERLQVPDDVAGAVLFLLSDAARFVTGQLLPVNGGFVMN
>gnl|CDD|171824 PRK12996, ulaA, PTS ascorbate transporter subunit IIC
MFILETLNFVVDILKVPSVLVGLIALIGLVAQKKAFSDVVKGTIKTILGFIVLGGGATVLVGSLNPLGGM
FEHAFNIQGIIPNNEAIVSIALEKYGASTALIMAFGMVANIVVARFTRLKYIFLTGHHTFYMACMIGVIL
TVAGFEGVGLVFTGSLILGLVMAFFPALAQRYMRRITGTDDIAFGHFGTLGYVLSGWIGSLCGKGSRSTE
EMNLPKNLSFLRDSSISISLTMMIIYLIMAVSAGREYVEATFSGGQNYLVYAIIMAITFAAGVFIILQGV
RLILAEIVPAFTGFSEKLVPNARPALDCPVVYPYAPNAVLIGFLFSFLGGLVGLFLLGQMKLVLILPGVV
PHFFTGATAGVFGNATGGRRGAMIGAFANGLLITFLPVLLLPVLGAIGFANTTFSDADFGVIGILLGNLA
RYLSPMAITGLVVALFALLVAYNVLAKNKKATAEVQENSGAKE
>gnl|CDD|237262 PRK12997, PRK12997, PTS sugar transporter subunit IIC
MEFLMTVLNFFIQNILGTPAILVGLIVLIGYILLKKSFSDVITGTIKTTVGFLILNVGAGGLVTTLRPFL
AAFSKAFGLKGVVIDPYAGLAAAQTALGSEFPYVSLILLIGFIVNILLAALRRFTKFKYIFLTGHIMVQQ
AATVLLLVLLLIPGFRNVFGVQLIIIGGIILGVYWAVSPALAQPFMRKITGNDGFAIGHQQMFGYWFSGK
IAGKFGKKEKSTENLKLPKWLSIFRDTVVAIAIVMLVFFGIILLAAGPDIMANVDLIAKGTGGQNWFMYI
IIQALTFSVGVFILLQGVRMFVGELVPAFKGISDKLIPGAKPAVDVPAVFPFAPNAVLIGFIFGTIGGLI
GMGILIVFKSPIVIIPGFVPLFFDGATAGVFGNARGGWRGAIIGSFLSGILITFLPALAVPLLGLAKYGG
WHGNTDWDTDWPAFGLLLKYIGLGGYLLLAIPQLQFAKAKDKEKYY
>gnl|CDD|237263 PRK12999, PRK12999, pyruvate carboxylase; Reviewed
EMKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEI
IRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEG
PIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENP
RHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEF
LVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATLHDLEIGIPSQEDIRLRGYAIQCRIT
TEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDSLLVKLTAWGRTFEQAVARMRRALRE
FRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTVNGFPGVKKKP
PVFPDPRLPKVDLSAPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLLRI
APATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVR
AFVREAAAAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKEL
EKAGAHILAIKDMAGLLKPAAAYELVSALKEEVDLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASM
SGLTSQPSLNSIVAALEGTERDTGLDLDAIRKLSPYWEAVRPYYAPFESGLKSPTTEVYLHEMPGGQYSN
LKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVTPSSKVVGDMALFMVQNGLTPEDVYEPGEDLDFPDS
VVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDFEAERAELEEKLGREVTDRDVLSYLLY
PKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEPDEDGMRTVYFELNGQ
PREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPV
DGTVKRVLVKAGDQVEAGDLLVELEP
>gnl|CDD|183836 PRK13004, PRK13004, YgeY family selenium metabolism-linked hydrolase
IPFKLILMLAEKYKADMTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFDKVEIDPMGNVLGYIGHGKK
LIAFDAHIDTVGIGDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTG
TVQEEDCDGLCWRYIIEEDKIKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKM
APILNELEELNPNLKEDPFLGKGTLTVSDIFSTSPSRCAVPDSCAISIDRRLTVGETWESVLAEIRALPA
VKKANAKVSMYNYDRPSYTGLVYPTECYFPTWLYPEDHEFVKAAVEAYKGLFGKAPEVDKWTFSTNGVSI
AGRAGIPTIGFGPGKEPLAHAPNEYTWKEQLVKAAAMYAAIPKSLLKKK
>gnl|CDD|237265 PRK13009, PRK13009, succinyl-diaminopimelate desuccinylase; Reviewed
MSDVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDFGDVKNLWARRGTEGPHLCFAGHTDVV
PPGDLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAING
TVKVLEWLKARGEKIDYCIVGEPTSTERLGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPA
LAELAATEWDEGNEFFPPTSLQITNIDAGTGATNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGL
DYTLEWTLSGEPFLTPPGKLVDAVVAAIEAVTGITPELSTSGGTSDARFIADYGAQVVEFGPVNATIHKV
NECVSVADLEKLTRIYERILERLLA
>gnl|CDD|139334 PRK13010, purU, formyltetrahydrofolate deformylase; Reviewed
MDAKPRSPSYVLTLACPSAPGIVAAVSGFLAEKGCYIVELTQFDDDESGRFFMRVSFHAQSAEAASVDTF
RQEFQPVAEKFDMQWAIHPDGQRPKVVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDLQPLAVQH
DIPFHHLPVTPDTKAQQEAQILDLIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARP
YHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSYSPEDLVAKGRDVECLTLARAVKAFIEHRVF
INGDRTVVF
>gnl|CDD|237266 PRK13011, PRK13011, formyltetrahydrofolate deformylase; Reviewed
MSRRPDTFVLTLSCPSAAGIVAAVTGFLAEHGCYITELHSFDDRLSGRFFMRVEFHSEEGLDEDALRAGF
APIAARFGMQWELHDPAARPKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPLAAWHGIPF
HHFPITPDTKPQQEAQVLDVVEESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQA
YERGVKLIGATAHYVTDDLDEGPIIEQDVERVDHAYSPEDLVAKGRDVECLTLARAVKAHIERRVFLNGN
RTVVFP
>gnl|CDD|237267 PRK13012, PRK13012, 2-oxoacid dehydrogenase subunit E1; Provisional
TDLSDGIAILLAAAAQLPDIDPQETAEWLEALDAVVAHAGPERARYLLDRLLERAAARGIALPGLLTTPY
VNTIPVDQQPPYPGDLALEERLAAIIRWNALAMVVRANRAYGELGGHIASYASAADLFEVGFNHFFRGRD
DAGGGDLVYFQPHSAPGIYARAFLEGRLSEEQLDHFRQEIGGPGLSSYPHPWLMPDFWQFPTGSMGIGPI
NAIYQARFMRYLQHRGLKDTSGRKVWGFFGDGEMDEPESIAALSLAAREGLDNLVFVINCNLQRLDGPVR
GNGRIIQELEALFRGAGWNVIKVLWGSDWDALFARDTTGALVRRFAETVDGQFQTFKANDGAYNREHFFG
QDPELAALVAHLSDEDIDRLKRGGHDPRKVYAAYAAAVRHKGQPTVILAKTKKGYGMGEAGEGRMTTHQQ
KKLDVEALKAFRDRFRLPLSDEQLEQLPFYKPAEDSPEMRYLHARRAALGGYLPRRRTAAPPLPVPPLSA
FAQFALGAGGKEMSTTMAFVRMLGNLLKDKALGPRIVPIVADEARTFGMANLFRQVGIYSPLGQLYEPED
AGSLLYYREAKDGQILEEGITEAGAISSWIAAATSYSVHGLPMLPFYIYYSMFGFQRVGDLIWAAADQRA
RGFLLGATAGRTTLGGEGLQHQDGHSHLLASTIPNCRAYDPAFAYELAVIVDDGMRRMLEEQEDVFYYLT
VMNENYAQPALPEGAEEGILKGMYRLAAAAEAPRVQLLGSGAILREVLAAARLLADDWGVDADVWSVTSF
TELRRDGLAAERANLLGPAEEARVPYVTQCLAGTRGPVVAATDYVRAVPEQIRAFVPARYVTLGTDGFGR
SDTRAALRRFFEVDRHSIVLAALKALADDGEVERTVVAEAIERYGIDDDKTPPWEV
>gnl|CDD|237268 PRK13013, PRK13013, acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein
ADDRLFAAIEARRDDLVALTQDLIRIPTLNPPGRAYREICEFLAARLAPRGFEVELIRAEGAPGDSETYP
RWNLVARRQGARDGDCVHFNSHHDVVEVGHGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLA
VYPDFAGSIEISGTADEESGGFGGVAYLAEQGRFSPDRVQHVIIPEPLNKDRICLGHRGVWWAEVETRGR
IAHGSMPFLGDSAIRHMGAVLAEIEERLFPLLATRRTAMPVVPEGARQSTLNINSIHGGEPEQDPDYTGL
PAPCVADRCRIVIDRRFLIEEDLDEVKAEITALLERLKRARPGFAYEIRDLFEVLPTMTDRDAPVVRSVA
AAIERVLGRQADYVVSPGTYDQKHIDRIGKLKNCIAYGPGILDLAHQPDEWVGIADMVDSAKVMALVLAD
LLAGTAG
>gnl|CDD|237269 PRK13014, PRK13014, methionine sulfoxide reductase A; Provisional
VDAAADGMETATFAGGCFWGVEGVFQHVPGVVSVVSGYSGGHVDNPTYEQVCTGTTGHAEAVQITYDPKQ
VSYENLLQIFFSTHDPTQLNRQGPDRGEQYRSAIFYHDEEQKKVAEAYIAQLDEAGIFKKPIVTPIKPYK
NFYPAEDYHQDYLKKNPTHPYIVYNDLPKGSGLKAFFESHYGNQPA
>gnl|CDD|237270 PRK13015, PRK13015, 3-dehydroquinate dehydratase; Reviewed
KGKILVLNGPNLNLLGTREPAIYGHETLADVEALCRAAAEALGLEVEFRQSNHEGELIDWIHEARGDVAG
IVINPGAYTHTSVAIRDALAALELPVIEVHISNVHAREAFRHHSYVSAIADGVICGLGTEGYRLALRRLA
TLLQAG
>gnl|CDD|237271 PRK13016, PRK13016, dihydroxy-acid dehydratase; Provisional
MKRKTPEELRSARWFGPDDLRSFGHRSRMMQMGYAPEDFDGKPVIAILNTWSDANPCHGHFRERVEDVKR
GVLQAGGFPLELPALSLSENFVKPTTMLYRNLLAMETEELIRSHPVDGAVLMGGCDKTTPGLVMGAISMG
LPMIYLPAGPMLRGNYRGKVLGSGSDAWKYWDERRAGNITQAEWLEIEGGIARSYGTCMTMGTASTMTAI
AEALGLTLPGASSIPAADANHQRMAALCGRRIVEMVWEDLTPSQILTKAAFENAITVAMATGCSTNAVIH
LIAMARRAGVPLSLDDLDRCGRTVPVIANIRPSGKTYLMEDFFYAGGLRALMKQLGDKLHLDALTVTGKT
LGDNLEGAKVYNDDVIRPLDNPVYAEGSLAVLRGNLAPDGAVIKPAACDPKFLVHRGPALVFDSYPEMKA
AIDDENLDVTPDHVMVLRNAGPQGGPGMPEWGMLPIPKKLLKQGVRDMVRISDARMSGTSYGACVLHVAP
EAYVGGPLALVRTGDIIELDVPARRLHLLVSDEELARRRAAWQPPERRYERGYGWMFSQHVEQADKGCDF
DFLETGFGRAVGEPDIY
>gnl|CDD|237272 PRK13017, PRK13017, dihydroxy-acid dehydratase; Provisional
MMMPKKPPRRLRSQEWFDNPDHPDMTALYLERYMNYGLTREELQSGKPIIGIAQTGSDLSPCNRHHLELA
ERVKEGIRDAGGIPMEFPVHPIQETGKRPTAALDRNLAYLGLVEILYGYPLDGVVLTTGCDKTTPACLMA
AATVDLPAIVLSGGPMLDGWHEGERVGSGTVIWKARELLAAGEIDYEEFMELVASSAPSVGHCNTMGTAS
TMNALAEALGMSLPGCAAIPAPYRERGQMAYATGKRIVEMVWEDLKPSDILTREAFENAIVVNSAIGGST
NAPIHLIAIARHAGVELSLDDWQRVGEDVPLLVNLQPAGKYLGEDFHRAGGVPAVLAELLRAGLLHGDAL
TVSGRTIGENIAGAPAPDRDVIRPYDAPLKERAGFLVLRGNLFDSAIMKTSVISEEFRERYLSEPGDENA
FEGRAVVFDGPEDYHARIDDPALDIDEHCILVIRGAGPVGYPGSAEVVNMQPPAALLKRGIRSLPCIGDG
RQSGTSGSPSILNASPEAAVGGGLALLRTGDRIRIDLNKRRVDVLVSDEELARRRAALKPPVPPSQTPWQ
ELYRKHVGQLSTGACLEPATLYQRVAATRGVPRHNH
>gnl|CDD|237273 PRK13018, PRK13018, cell division protein FtsZ; Provisional
MQDLVKEALIDSEQEKEEKKASDDDFGNPKIVVVGCGGAGNNTINRLYEIGIEGAETIAINTDAQHLAMI
KADKKILIGKSLTRGLGAGGDPEVGRKAAEESRDEIKEVLKGADLVFVTAGMGGGTGTGAAPVVAEIAKE
QGALVVGVVTKPFKFEGRARMQKAEEGIERLREAADTVIVIDNNRLLDIVPNLPIADAFSVADEVIAETV
KGITETITKPSLINLDFADVKSVMKGGGVAMMGVGEAKGQNRAMEAVRAALANPLLDVDYRGAKGALVHI
TGGPDLTLKEANEAASRITEELDPEANIIWGARIDPDMEGKVRVMVIMTGVKSAQILGPGTQPQAIISRR
SGERSRGKDELGIDSIVAHQAGLSFPSR
>gnl|CDD|183845 PRK13019, clpS, ATP-dependent Clp protease adapter ClpS
MSDPATKPKTKTKPKLERYPLYKVIVLNDDFNTFEHVVNCLLKAIPGMSEDRAWRLMITAHKEGSAVVWV
GPLEQAELYHQQLTDAGLTMAPEE
>gnl|CDD|183846 PRK13020, PRK13020, riboflavin synthase subunit alpha; Provisional
MFTGIVQATAEVVAIHKKDGLNTLEIAFPPELLEGLEIGASVAVNGVCLTVTKIEGDRVFFDVMEETLRL
TNLADLRVGDRVNIERSAKFGAEIGGHILSGHVDTTATVVEISDTEENYDIRFRVPPEWMKYIFAKGFIG
VNGCSLTVGEVDESEFEVHLIPETLRATNLGAKKVGDLVNIEIDSQTQVIVDTVERVLAERLAELN
>gnl|CDD|237274 PRK13021, secF, preprotein translocase subunit SecF; Reviewed
MKNINLTKWRYISSAISIVLMLLSLTIIGVKGFNWGLDFTGGVVTEVQLDRKITSSELQPLLNAAYQQEV
SVISASEPGRWVLRYAPADTAQSNVDIQQALAPLGTEVQVLNSSIVGPQVGQELAEQGGLALLVAMLCIL
GYLSYRFEWRLASGALFALVHDVIFVLAFFALTQMEFNLTVLAAVLAILGYSLNDSIIIADRIRELLIAK
PKLAIQEINNQAIVATFSRTMVTSGTTLMTVGALWIMGGGPLEGFSIAMFIGILTGTFSSISVGTSLPEL
LGLSPEHYKVQVISDTP
>gnl|CDD|171842 PRK13023, PRK13023, protein translocase subunit SecDF
MLYFSRWKSALIWLAVLVSLIIASPNFFSRETLANLPDFLPKKQVSLGLDLSGGSRLILQVQNAGKTDLE
TTANIMRQRLEELGYGNPVVEGEGRNQIRVEVPGLYDAQLLKDILTIRGNLSFRAMDDTMSPDDAIRGTP
PADSEIVYSFDDPPVGYLLKKTPILTGHDITDAKASISADDGQPVITLTLDDNGRRRLADLTAQGNENSF
AIVVDNQVVSAPTVSGPLDTSELQIEGAFDLQAANNMAVVLRSGALPQAVTVLEERTIASALGEDYASAA
VLAALLAALVVGLFMVLSYGILGVIALVALVVNIIILTAVLSLIGASISLASIAGLVLTIGLAVDAHILI
YERVREDRRKGYSVVQAMESGFYRALSTIVDANLTTLIAALVLFLLGSGTVHGFALTVAIGIGTTLFTTL
TFTRLLIAQWVRTAKPKEVPKRRLKLVPTVTHIPFMRLQFVTLGISVLACAIVVALFVNIGFNYGIDFRG
GSMVELQARNGDANLEDINERLAELNIDSARVLPAKSPRSALVIIGSQEVGDDAEQTVAVKLRGEFEQDY
SFQRVDVVGPTVSEQLSRAGVLAVILSLIGIFIYVWFRFRWQLALGAVLSTLHDVVILSGMFIVFRMEFN
LWSVAAILTIIGYSLNDTVVIYDRVRENLRRYKSAPLPAIIDASINQTLSRTLLTSFVTFLAHVPLYAFG
GSEIRMFALALSVGIIVASYSSIFIAAPLLVQFGLKPRETDAGDAVDAELAQSLNLES
>gnl|CDD|237276 PRK13024, PRK13024, bifunctional preprotein translocase subunit SecD/SecF; Reviewed
MRNKRWVIFFLTLLLLIGIYYASPKFVTKNINLGLDLQGGFEVLLEVSPADKGKKADREALDSTVEVLRN
RIDGLGVSEPNIQREGNNRIRVELPGVQDPERARELLGSTAKLTFRDVTDPPPPGVGGPVVGPDEGKDTA
VLNPVLLSGDDLTDAGAKFDQDQTNRPSVSLKLKSEGAKKWAKVTEKNSKKGPPNNRIAIVLDPKVISAP
TVNQPINGGSVQISGNFTVEEAKDLANLLNAGALPAPLKIIESRSVGPTLGQDAIDAGIIAGIIGFALIF
LFMLVYYGLPGLIANIALLLYIFLTLGALSSLGAVLTLPGIAGLVLGIGMAVDANVLIFERIKEELRKGK
SLKKAFKKGFKNAFSTILDSNITTLIAAAILFFFGTGPVKGFATTLIIGILASLFTAVFLTRLLLELLVK
RGDKKPFLFGVKKKKIHNINEGVTIFDRIDFVKKRKWFLIFSIVLVIAGIIIFFIFGLNLGIDFTGGTRY
EIRTDQPVDLEQVRADLKELGLGEVNIVTFGSDNNQVLVRTYGILSDDEEADTEIVAKLKNALKNDKGGT
IPSSETVGPTVGKELARNAIIAVLIALIGILLYILIRFEWTFSLGAILALLHDVLIVIGFFSLFRLEVDL
TFIAAILTIIGYSINDTVVVFDRIRENLRLYKKKDLREIVNKSINQTLSRTINTSLTTLLVLLALLIFGG
SSLRNFSLALLVGLIVGTYSSIFIAAPLWLDLEKRRLKKKKKRKKVKKWEVEKIE
>gnl|CDD|237277 PRK13026, PRK13026, acyl-CoA dehydrogenase; Reviewed
MMTLIILLLIAIVLVFAVKPLRRQFITRPVFKFFKKVLPPLSDTEREAMEAGDVWWEGELFSGKPDWQKL
HSYPKPTLTAEEQAFIDNEVETLLTMLDDWDIVQNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYA
NSTIVSKIATRSVSAAVTVMVPNSLGPGELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAI
PDTGIVCRGEFEGEEVLGLRLTWDKRYITLAPVATVLGLAFKLRDPDGLLGDKKELGITCALIPTDHPGV
EIGRRHNPLGMAFMNGTTRGKDVFIPLDWIIGGPDYAGRGWRMLVECLSAGRGISLPALGTASGHMATRT
TGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKPSVVTAIAKYHMTELARDV
VNDAMDIHAGKGIQLGPKNYLGHAYMAVPIAITVEGANILTRNLMIFGQGATRCHPYVLAEMEAAAMEDE
HEGLEAFDSLLFKHIGYAARNAFRALFSALTGSRFISAPVSGETAQYYKDMSRLSAALALLADLSMLILG
GDLKRKEMLSARLGDVLSQLYLASATLKRFEDNGRQQDDLPAVHYAMQDCLHLAAKALDEFLRNFPNRPV
AWLLRALIFPLGNHFRAPSDKLARQLAELMMTPGPARDRLTALCYIFEGDKDGVARVEQAFLAQYAVKPL
YKKLKKAQREGKLPRKVPLLELFAKALEKGVITADEAEKLLAADKLRLDAIQVDDFTPDFMEKKTLQSRK
EKLK
>gnl|CDD|183850 PRK13027, PRK13027, C4-dicarboxylate transporter DctA; Reviewed
MKKFLRSLFGQVVIALVLGVALGAFFPHFAESLKPLGDGFIKLIKMLIGPIVFCVVVSGIAGAGDLKKVG
RVGLKAVIYFEVMTTIALVIGLVLAYLTGPGVGMNIDLRSLDAASLAGYAKNAQSLKGTAGFLLKLIPTT
AVDAFAKGDILQVLLFSVLFGSALSLLGERAKRVNRLIDELSHVLFRIMGFIIKLAPLGVLGAIAFTTGK
YGVGSLKQLGMLVAVFYLTCFVFVVVVLGAVMRLAGFSVFKLIRYLREELLIVLGTASSDAVLPQVMRKL
EHMGIKDSTVGLVIPTGYSFNLDGFSIYLTLAAVFIAQATNTPLSMHDLITILLVSLVTSKGAHGIPGSA
IVILAATLSAIPAIPVLGLVLILPVDWFMGIARALTNLIGNCVATVVVAVWENDIDRARAQAVLNGELRY
V
>gnl|CDD|183851 PRK13028, PRK13028, tryptophan synthase subunit beta; Provisional
MTSYLKSMPDADGFFGEYGGQFVPPELKPALDELEAAYEEIKKDPDFIAELRYLLKHYVGRPTPLYHAKR
LSEELGGAQIYLKREDLNHTGAHKINNCLGQALLAKRMGKKRLIAETGAGQHGVATATAAALFGLECEIY
MGEVDIERQHPNVFRMKLLGAEVVPVTRGGRTLKEAVDSAFEDYLKDPDNTHYAIGSVVGPHPFPMMVRD
FQSVIGEEAREQFLEMTGRLPDAVVACVGGGSNAIGLFSAFLDDESVRLVGVEPAGRGLDLGEHAATLTL
GKPGVIHGFKSYVLQDEDGEPAPVHSIAAGLDYPGVGPEHAYLKDIGRVEYVTATDEEALDAFFLLSRTE
GIIPALESSHAVAYAIKLAPELSKDETILVNLSGRGDKDIDYVAEMLGLGET
>gnl|CDD|237278 PRK13029, PRK13029, indolepyruvate ferredoxin oxidoreductase family protein
MNAPLPDAARMALRAVSLDDKYTLERGRIYISGTQALVRLPLLQRARDRRAGLNTAGFISGYRGSPLGAL
DQALWKAKKHLAAADVVFQPGVNEELAATAVWGSQQLELDPGAKRDGVFGMWYGKGPGVDRSGDALRHAN
LAGTSPLGGVLVLAGDDHGAKSSSVAHQSDHTFIAWGIPVLYPASVQDYLDYGLHGWAMSRYSGLWVGMK
CVTEVVESTASVDLDPDRVDIVLPDDFVLPPGGLHIRWPDDPLAQEERMLEFKWYAALAYVRANRLNRLV
IDGPNPRLGIIAAGKAYLDVRQALRDLGLDDATCAALGIRLLKVGCVWPLDPQSVREFAQGLEEVLVVEE
KRAVIEYQLKEELYNWREDVRPAIFGKFDHRDGAGGEWSVPAGRWLLPAHAELSPALIAKAIARRLAALG
LPADVAARMDARVADIEAKERAAAQPRLLTERKPWFCSGCPHNTSTRVPEGSRALAGIGCHYMAMWMDRS
TEGFSQMGGEGVAWIGQMPFSRRRHVFQNLGDGTYFHSGLLAIRQAIAAGVNITYKILYNDAVAMTGGQP
VDGVLTVPQIARQVHAEGVRRIVVVTDEPGKYRGVARLPAGVTVHHRDELDAVQRELREVPGVSVLIYDQ
TCATEKRRRRKRGTYPDPARRVFINELVCEGCGDCSVQSNCLAVQPVETEFGRKRKINQSSCNKDFSCVK
GFCPSFVTVEGAQLKKPSDAALGRAALAAVAALPLPTLALLDRPYGILVTGIGGTGVVTIGGVLGMAAHL
EGKGVSVLDMAGLAQKGGAVLSHIQIAATPAALHATRIDTGEADLVIACDLVVAASGEALAAMRPGRTRA
AANSHETPTAAFVRNPDWSFPVDQTVALLRDSIGADQCAFFDANALALALLGDSIYANPLLLGFAWQKGW
VPLSLDALERAIELNGVAVDSNRAAFEWGRLAAHDGAAAARADGGEAAARQAIVFQRPESLDDLIESRAA
FLTDYQNAAYAARYRARVDRVRAAEAVVGGGSARLTEAVARNLFKLMAYKDEYEVARLYTDPAFLDQLAA
EFEGEPRLSFHLAPPLFARRDERGHLVKVRYGPWMLPAFRVLARLKGLRGTAFDVFGYTEERRAERALIA
EYRALLDELCPSLTAGRLDIALELARLPEDIRGYGHVKARNVAAAAKRRERLLARYRQPSTGRPLA
>gnl|CDD|237279 PRK13030, PRK13030, indolepyruvate ferredoxin oxidoreductase family protein
ALSDYRLDDRYTATRGRIFLTGTQALVRLLLMQRRRDRARGLNTAGFVSGYRGSPLGGVDQALWKAKKLL
DASDIRFLPGINEELAATAVLGTQQVEADPERTVDGVFAMWYGKGPGVDRAGDALKHGNAYGSSPHGGVL
VVAGDDHGCVSSSMPHQSDFALIAWHMPVLNPANVQEYLDFGLYGWALSRYSGAWVGFKAISETVESGST
VDLDPDRTRWPAPEDFTPPAGGLHNRWPDLPSLAIEARLAAKLPAVRAFARANSIDRWVAPSPDARVGIV
TCGKAHLDLMEALRRLGLDDADLRAAGIRIYKVGLSWPLEPTRLREFADGLEEILVIEEKRPVIEQQIKD
YLYNRPGGARPRVVGKHDEDGAPLLSELGELRPSLIAPVLAARLARHKPALDRRARVVDLVAPQILSNEA
DAVVRTPYFCSGCPHNTSTKVPEGSIAQAGIGCHFMASWMDRDTTGLTQMGGEGVDWIGHAPFTETKHVF
QNLGDGTYFHSGSLAIRQAVAAGANITYKILYNDAVAMTGGQPVDGSISVPQIARQVEAEGVSRIVVVSD
EPEKYRGHHLPAGVTVHHRDELDAVQRELRETPGVTVLIYDQTCAAEKRRRRKRGEFPDPDRRLFINEAV
CEGCGDCGVQSNCLSVEPVETPFGRKRRIDQSSCNKDFSCVNGFCPSFVTVEGATLRKAAGAAFDAAALA
ARVDALPLPATPADAAPYDLLVTGVGGTGVVTVGALLAMAAHLEGKSASVLDFTGLAQKGGAVLSHVRIA
ASPEWLHQVRIDTQQADLLLACDMVVGASPDALQTVRHGRTRAVVNTHEIPTADFVRNPDANLPADALLD
KMRHAAGDERLASLDAQALAEKLLGDAIGANILMLGYAWQLGLVPLSLAALMRAIELNGVAVEMNLLAFR
WGRLAAADPAALAAAWAAAHPVAAPAAPETLDRLVARREAELTAYQDAAYAARYRALVARVRAAEQALAG
DEALTEAVARTLYKLMAYKDEYEVARLYTDPAFRAALEAQFEGDYRLKFHLAPPLLAKADPRTGRPRKRR
FGPWMWPAFRLLARLKGLRGTWLDPFGRTAERRMERALIDDYEATLERLLAALTAGNLDAAAALAELPDE
VRGYGHVKLANLARVKAEEAELLARLGIDAATSAAVRHA
>gnl|CDD|106068 PRK13031, PRK13031, preprotein translocase subunit SecB; Provisional
MDQQAQPQFQIQKVYVKDLSFSIPNSDKIWTTNWKPELHTDLKVEATKLPEENTYETVLTLEVKVENDGM
VAFEAEVKQAGIFTVANMQEAQIEHAKKAFCPNILYHYAREAISDLVISGGFPQLCLSAVNFDAMYQDSL
KESADSKQH
>gnl|CDD|171848 PRK13032, PRK13032, chemotaxis-inhibiting protein CHIPS; Reviewed
MKKKLATTVLALSFLTAGISTHHHSAKAFTFEPFPTNEEIESNKKMLEKEKAYKESFKNSGLPTTLGKLD
ERLRNYLKKGTKNSAQFEKMVILTENKGYYTVYLNTPLAEDRKNVELLGKMYKTYFFKKGESKSSYVING
PGKTNEYAY
>gnl|CDD|171849 PRK13033, PRK13033, formyl peptide receptor-like 1 inhibitory protein; Reviewed
MKKNITKTIIASTVIAAGLLTQTNDAKAFFSYEWKGLEIAKNLADQAKKDDERIDKLMKESDKNLTPYKA
ETVNDLYLIVKKLSQGDVKKAVVRIKDGGPRDYYTFDLTRPLEENRKNIKVVKNGEIDSITWY
>gnl|CDD|237280 PRK13034, PRK13034, serine hydroxymethyltransferase; Reviewed
LMFFFSDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCE
FVDEVEALAIERAKQLFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKW
YNAVQYGVDRLTGLIDYDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLV
AAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTNDEEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEAL
QPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVP
GDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVRKEVKALCSRFPIY
>gnl|CDD|171851 PRK13035, PRK13035, superantigen-like protein 5; Reviewed
MKMAAIAKASLALGILATGTITSLHQTVNASEHEAKYENVTKDIFDLRDYYSGASKELKNVTGYRYSKGG
KHYLIFDKNRKFTRVQIFGKDIERFKARKNPGLDIFVVKEAENRNGTVFSYGGVTKKNQDAYYDYINAPR
FQIKRDEGDGIATYGRVHYIYKEEISLKELDFKLRQYLIQNFDLYKKFPKDSKIKVIMKDGGYYTFELNK
KLQTNRMSDVIDGRNIEKIEANIR
>gnl|CDD|171852 PRK13036, PRK13036, superantigen-like protein; Reviewed
MKLKNIAKASLALGILTTGMITTTAQPVKASTLEVRSQATQDLSEYYKGRGFELTNVSGYKEGNKVTFID
NSQLIDVTLTGNEKLTFKDDEDVSNVDVFVVREGSDKSAITTSIGGITKTNGTQYKDTVQNVNLSISKST
GQHTTSVTSEYYSINKEEISLKELDFKLRKHLIDKHDLYKTEPKDSKIRITMKNGGYYTFELNKKLQPHR
MGDTIDSRNIEKIEVNL
>gnl|CDD|106074 PRK13037, PRK13037, superantigen-like protein; Reviewed
MKFKAIAKASLALGMLATGVITSNVQSVQAKTEVKQQSESELKHYYNKPVLERKNVTGYKYTEKGKDYID
VIVDNQYSQISLVGSDKDKFKDGDNSNIDVFILREGDSRQATNYSIGGVTKTNSQPYIDYIHTPILEIKK
GKEEPQSSLYQIYKEDISLKELDYRLRERAIKQHGLYSNGLKQGQITITMKDGKSHTIDLSQKLEKERMG
ESIDGRQIQKILVEMK
>gnl|CDD|171853 PRK13038, PRK13038, superantigen-like protein; Reviewed
MKFTALAKATLALGILTTGTLTTEVHSGHAKQNQKSVNKHDKEALYRYYTGKTMEMKNISALKHGKNNLR
FKFRGIKIQVLLPGNDKSKFQQRSYEGLDVFFVQEKRDKHDIFYTVGGVIQNNKTSGVVSAPILNISKEK
GEDAFVKGYPYYIKKEKITLKELDYKLRKHLIEKYGLYKTISKDGRVKISLKDGSFYNLDLRSKLKFKYM
GEVIESKQIKDIEVNLK
>gnl|CDD|171854 PRK13039, PRK13039, superantigen-like protein; Reviewed
MKFTAIAKAIFVLGILTTSVMITENQSVNAKGKYEKMNRLYDTNKLHQYYSGPSYELTNVSGQSQGYYDS
NVLLFNQQNQKFQVFLLGKDENKYKEKTHGLDVFAVPELVDLDGRIFSVSGVTKKNVKSIFESLRTPNLL
VKKIDDKDGFSIDEFFFIQKEEVSLKELDFKIRKLLIKKYKLYEGSADKGRIVINMKDENKYEIDLSDKL
DFERMADVINSEQIKNIEVNLK
>gnl|CDD|106077 PRK13040, PRK13040, superantigen-like protein; Reviewed
MKLKTLAKATLVLGLLATGVITTESQTVKAAESTQGQHNYKSLKYYYSKPSIELKNLDGLYRQKVTDKGV
YVWKDRKDYFVGLLGKDIEKYPQGEHDKQDAFLVIEEETVNGRQYSIGGLSKTNSKEFSKEVDVKVTRKI
DESSEKSKDSKFKITKEEISLKELDFKLRKKLMEEEKLYGAVNNRKGKIVVKMEDDKFYTFELTKKLQPH
RMGDTIDGTKIKEINVELEYK
>gnl|CDD|106078 PRK13041, PRK13041, superantigen-like protein; Reviewed
MKMKNIAKISLLLGILATGVNTTTEKPVHAEKKPIVISENSKKLKAYYTQPSIEYKNVTGYISFIQPSIK
FMNIIDGNSVNNLALIGKDKQHYHTGVHRNLNIFYVNEDKRFEGAKYSIGGITSANDKAVDLIAEARVIK
ADHIGEYDYDFFPFKIDKEAMSLKEIDFKLRKYLIDNYGLYGEMSTGKITVKKKYYGKYTFELDKKLQED
RMSDVINVTDIDRIEIKVRKA
>gnl|CDD|183854 PRK13042, PRK13042, superantigen-like protein; Reviewed
MKITTIAKTSLALGLLTTGVITTTTQAANATTPSSTKVEAPQSTPPSTKVEAPQSKPNATTPPSTKVEAP
QQTPNATTPSSTKVETPQSPTTKQVPTEINPKFKDLRAYYTKPSLEFKNEIGIILKKWTTIRFMNVVPDY
FIYKIALVGKDDKKYGEGVHRNVDVFVVLEENKYNLEKYSVGGITKSNSKKVDHKAGVRITKEDNKGTIS
HDVSEFKITKEQISLKELDFKLRKQLIEKHNLYGNVGSGKIVIKMKNGGKYTFELHKKLQENRMADVIDG
TNIDNIEVNIK
>gnl|CDD|171855 PRK13043, PRK13043, superantigen-like protein; Reviewed
MKKNIMNKLVLSTALLLLGTTSTQLPKTPISFSSEAKAYNISENETNINELIKYYTQPHFSLSGKWLWQK
PNGSIHATLQTWVWYSHIQVFGSESWGNINQLRNKYVDIFGTKDEDTVEGYWTYDETFTGGVTPAATSSD
KPYRLFLKYSDKQQTIIGGHEFYKGNKPVLTLKELDFRIRQTLIKNKKLYNGEFNKGQIKITADGNNYTI
DLSKKLKLTDTNRYVKNPKNAQIEVILEKSN
>gnl|CDD|237281 PRK13054, PRK13054, lipid kinase; Reviewed
MTFPKSLLILNGKSAGNEELREAVGLLREEGHTLHVRVTWEKGDAARYVEEALALGVATVIAGGGDGTIN
EVATALAQLEGDARPALGILPLGTANDFATAAGIPLEPDKALKLAIEGRAQPIDLARVNDRTYFINMATG
GFGTRVTTETPEKLKAALGGVAYLIHGLMRMDTLKPDRCEIRGPDFHWQGDALVIGIGNGRQAGGGQQLC
PEALINDGLLDLRILPAPQELLPTLLSTLTGGSEDNPNIIRARLPWLEIQAPHELTFNLDGEPLSGRHFR
IEVLPAALRCRLPPDCPLLR
>gnl|CDD|237282 PRK13055, PRK13055, putative lipid kinase; Reviewed
MQKRARLIYNPTSGQEIMKKNVADILDILEQAGYETSAFQTTPEPNSAKNEAKRAAEAGFDLIIAAGGDG
TINEVVNGIAPLEKRPKMAIIPAGTTNDYARALKIPRDNPVEAAKVILKNQTIKMDIGRANEDKYFINIA
AGGSLTELTYSVPSQLKSMFGYLAYLAKGAELLPRVSPVPVRITYDEGVFEGKISMFFLALTNSVGGFEQ
IVPDAKLDDGKFTLIIVKTANLFELLHLMALILNGGKHIDDPRVIYIKTSKLTIEPLGDDRLMVNLDGEY
GGDAPMTFENLKQHIEFFANTDEISDDALTDELEIEEIAKKFAEEVEDLEQEDE
>gnl|CDD|183857 PRK13057, PRK13057, lipid kinase
LLLVNRHARSGRAALAAARAALEAAGLELVEPPAEDPDDLSEVIEAYADGVDLVIVGGGDGTLNAAAPAL
VETGLPLGILPLGTANDLARTLGIPLDLEAAARVIATGQVRRIDLGWVNGHYFFNVASLGLSAELARRLT
KELKRRWGTLGYAIAALRVLRRSRPFTAEIEHDGRTERVKTLQVAVGNGRYYGGGMTVAHDATIDDGRLD
LYSLEVAHWWRLLALLPALRRGRHGEWPDVRAFRTTELELRTRKPRPINTDGELTTYTPAHFRVLPKALR
VLAPPPA
>gnl|CDD|183858 PRK13059, PRK13059, putative lipid kinase; Reviewed
MKKVKFIYNPYSGENAIISELDKVIRIHQEKGYLVVPYRISLEYDLKNAFKDIDESYKYILIAGGDGTVD
NVVNAMKKLNIDLPIGILPVGTANDFAKFLGMPTDIGEACEQILKSKPKKVDLGKINDKYFINVASTGLF
TDVSQKTDVNLKNTIGKLAYYLKGLEELPNFRKLKVKVTSEEVNFDGDMYLMLVFNGQTAGNFNLAYKAE
VDDGLLDVIIIKACPIIDLIPLFIKVLKGEHLEDVNGLIYFKTDKLEIESNEEIVTDIDGERGPDFPLNI
ECIKGGLKVLGILDE
>gnl|CDD|183861 PRK13105, ubiA, prenyltransferase; Reviewed
IRQLLLSSRPISWINTAYPFAAAYLLAGGEIDWLFVVGTVFFLIPYNLAMYGINDVFDYESDLRNPRKGG
VEGAVLDRAMHRTTLWASVVTTVPFLVVLLAVGSWASGLVLAVSVFAVVAYSAPGLRFKERPFLDSLTSS
THFVSPALYGLVLAGAPFTAALWAVLAAFFLWGMASHAFGAVQDVVADREAGIASIATVLGARRTVRLAV
GLYAAAAVLMLALPWPGWLAAVLALPYVVNTARFWSVTDADCERANRGWRRFLWLNYVSGFLVTMLLIAI
AL
>gnl|CDD|237283 PRK13106, ubiA, prenyltransferase; Reviewed
MSWDPGGLNNTRSKFYIILRFLRIEQTFFSLPMAYLGAFVAIKGIPPISTLILIFLALFFLRTAGMTNDN
LADLEIDAKNPRTKNRPLVTGAIKISEAKALITAGLILFFASAYLVNRWALLLSPIVALIAMSYPYMKRY
TAFANYHLASIQGLAVFSGAVAVLGLYANSLIQVLLRVPWLFVIGTILWAAGFDLYNHIPDAEFDREMGL
HSFAVVLGKWALTFAGLNQLFSVVLDLLGDLYYGLGPIAIAATILHGLIMAYAYYLASKKGDFGRAFYYN
IYSSIVLGLGIIIDVLLGIP
>gnl|CDD|237284 PRK13108, PRK13108, prolipoprotein diacylglyceryl transferase; Reviewed
MRMLPSYIPSPPRGVWYLGPLPVRAYAVCVITGIIVALLIGDRRLTARGGERGMTYDIALWAVPFGLIGG
RLYHLATDWRTYFGDGGAGLAAALRIWDGGLGIWGAVTLGVMGAWIGCRRCGIPLPVLLDAVAPGVVLAQ
AIGRLGNYFNQELYGRETTMPWGLEIFYRRDPSGFDVPNSLDGVSTGQVAFVVQPTFLYELIWNVLVFVA
LIYIDRRFIIGHGRLFGFYVAFYCAGRFCVELLRDDPATLIAGIRINSFTSTFVFIGAVVYIILAPKGRE
APGALRGSEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVV
QVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKA
APIPDPAKPDELAVAGPGDDPAEPDGIRRQDDFSSRRRRW
>gnl|CDD|183864 PRK13109, flhB, flagellar biosynthesis protein FlhB; Reviewed
MSDDTDKESKTEEATERKVRDAIEKGDIPVSREAPVFASMLGLLIALAFFARGQAAQLTGDLAPLLDDPR
GFSLETGADAMLLLSRVALAAGRFLLPILLILAVCGLAASLLQNLPRFVLDRIQPKWSRISPMKGWTRIF
GTSGQVEFLKSLFKFLSVSVVVLLLLRSERAKAVNAMFVDPSQLPELILTVAIRLVSAVAIATIVLVALD
LVWARFHWRRSLRMTKQEIKDEHKQAEGDPSVKARLRSLAQDRARNRMLANVPRATLVIANPTHFAIALR
YERSENPAPLVVAKGQDLIALKIREIAEENGIPVIEDKPLARSLYDAVQVDQVIPAEFYRPVAQILYFLF
SRARKAAA
>gnl|CDD|237285 PRK13111, trpA, tryptophan synthase subunit alpha; Provisional
ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAG
VTLADVFELVREIREKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKK
HGLDLIFLVAPTTTDERLKKIASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGIS
TPEQAAAIAAVADGVIVGSALVKIIEENPEALEALAAFVKELKAALRS
>gnl|CDD|237286 PRK13125, trpA, tryptophan synthase subunit alpha; Provisional
IMRPGLVVYLTAGYPNVESFKEFIIGLVELVDILELGIPPKYPKYDGPVIRKSHRKVKGLDIWPLLEEVR
KDVSVPIILMTYLEDYVDSLDNFLNMARDVGADGVLFPDLLIDYPDDLEKYVEIIKNKGLKPVFFTSPKF
PDLLIHRLSKLSPLFIYYGLRPATGVPLPVSVERNIKRVRNLVGNKYLVVGFGLDSPEDARDALSAGADG
VVVGTAFIEELEKNGVESALNLLKKIRGALDEYK
>gnl|CDD|171868 PRK13128, PRK13128, D-aminopeptidase; Reviewed
MPNIDLPTLEAFVHAIPQNYKGPGGAVAVVKDGEVVLRHAWGFADLARRKAMTPETRMPICSVSKQFTCA
VLLDCIGEPEMLDAALAAYLDQFEDPRPAVRDLCNNQSGLRDYWALTVLCGAAPEGIFLPDQAQNLLRRL
KTTHFAPGTHYSYCNGNFRILADLIEQHTGRSLADLLAERIFAPAGMKTAELIPDTALFDECTGYEGDTV
RGFLPAINRIHWLGDAGICASLDDMIAWEQFIDRTRDDENGLYRRLSVPQTFADGAPAPYGFGLKFEETG
GKRLTGHGGALRGWRCQRWHCADERLSTIVMFNFEGNASDAALKMMNAALGIPPAKPVRAQANPGWFGSW
LNPETGLVLSLEDAGGGRMKARFGTGPEIMDISGENEAQSSMTTLRRDGDMIHLARKDENLTLAMHRLKG
EARQDIAGRYRSDELEADLLIVSEGGAIYGAFEGFLGKSDMYPLYAAGPDVWLLPVQRSMDAPSPGEWKL
VFHRDAAGRITGVTVGCWLARGVEYKRV
>gnl|CDD|237287 PRK13130, PRK13130, RNA-protein complex protein Nop10
MKSKIRKCPKCGVYTLKEICPVCGGKTKNPHPPRFSPEDKYGKYRRALKKRRKLNC
>gnl|CDD|237288 PRK13141, hisH, imidazole glycerol phosphate synthase subunit HisH; Provisional
MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVA
SGKPLLGICLGMQLLFESSEEFGETEGLGLLPGRVRRFPPEEGLKVPHMGWNQLELKKESPLLKGIPDGA
YVYFVHSYYADPCDEEYVAATTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEEC
>gnl|CDD|171871 PRK13142, hisH, imidazole glycerol phosphate synthase subunit HisH; Provisional
MIVIVDYGLGNISNVKRAIEHLGYEVVVSNTSKIIDQAETIILPGVGHFKDAMSEIKRLNLNAILAKNTD
KKMIGICLGMQLMYEHSDEGDASGLGFIPGNISRIQTEYPVPHLGWNNLVSKHPMLNQDVYFVHSYQAPM
SENVIAYAQYGADIPAIVQFNNYIGIQFHPEKSGTYGLQILRQAIQGGFIND
>gnl|CDD|237289 PRK13143, hisH, imidazole glycerol phosphate synthase subunit HisH; Provisional
MMIVIIDYGVGNLRSVSKALERAGAEVVITSDPEEILDADGIVLPGVGAFGAAMENLSPLRDVILEAARS
GKPFLGICLGMQLLFESSEEGGGVRGLGLFPGRVVRFPAGVKVPHMGWNTVKVVKDCPLFEGIDGEYVYF
VHSYYAYPDDEDYVVATTDYGIEFPAAVCNDNVFGTQFHPEKSGETGLKILENFVELIKR
>gnl|CDD|183870 PRK13145, araD, L-ribulose-5-phosphate 4-epimerase; Provisional
KNLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEGD
LNPSSDLPTHVELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGA
YEKETGSVIIEEFEKRGLDPMAVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQINPRVEPA
PQYIMDKHYLRKHGPNAYYGQKGD
>gnl|CDD|237290 PRK13146, hisH, imidazole glycerol phosphate synthase subunit HisH; Provisional
MMTVAIIDYGSGNLRSAAKALERAGAGADVVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLGEAVI
EAVLAAGRPFLGICVGMQLLFERGLEHGDTPGLGLIPGEVVRFQPDGPALKVPHMGWNTVDQTRDHPLFA
GIPDGARFYFVHSYYAQPANPADVVAWTDYGGPFTAAVARDNLFATQFHPEKSQDAGLALLRNFLAWLP
>gnl|CDD|183872 PRK13149, PRK13149, H/ACA RNA-protein complex component Gar1; Reviewed
MKRLGKVLHYAPKGKLIIRLDKQPPIGSVVYDKKLKKIGKVVDVFGPVKEPYVLVKPDKKDPPELVGEKL
YVR
>gnl|CDD|139376 PRK13150, PRK13150, cytochrome c maturation protein CcmE
MNLRRKNRLWVVCAVLAGLGLTTALVLYALRANIDLFYTPGEILYGKRETQQLPAVGQRLRVGGMVMPGS
VRRDPDSLKVNFSLYDAEGSVTVSYEGILPDLFREGQGVVVQGTLEKGNHVLAHEVLAKHDENYTPPEVE
KAMQENHRRPQRADKDTSS
>gnl|CDD|171876 PRK13152, hisH, imidazole glycerol phosphate synthase subunit HisH; Provisional
MIALIDYKAGNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEQVL
VQKKPILGICLGMQLFLERGYEGGVCEGLGFIEGEVVKFEEDLNLKIPHMGWNELEILKQSPLYQGIPEK
SDFYFVHSFYVKCKDEFVSAKAQYGHKFVASLQKDNIFATQFHPEKSQNLGLKLLENFARL
>gnl|CDD|183873 PRK13159, PRK13159, cytochrome c-type biogenesis protein CcmE; Reviewed
MNATRKQRLWLVIGVLTAAALAVTLIVLALQRNMSYLFTPSQVRAGAAAGYQQFRLGGMVKAGSIQRAAD
SLKVSFTVIDKNAATQVEYTGILPDLFRDNQSVIANGRMQGGRFVANEVLAKHDETYMPKELKDAMAEGH
LGKPIPAAAAPLTGP
>gnl|CDD|183874 PRK13165, PRK13165, cytochrome c maturation protein CcmE
MNPRRKKRLWLACAVLAGLALTIGLVLYALRSNIDLFYTPGEILYGKRETQQKPEVGQRLRVGGMVMPGS
VQRDPNSLKVSFTLYDAGGSVTVTYEGILPDLFREGQGIVAQGVLEEGNHIEAKEVLAKHDENYTPPEVE
EAMKKNHRRPAYSYKDKAST
>gnl|CDD|237291 PRK13168, rumA, 23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD
AQFYSPKRRVTTRQIITVTIESLDHDGRGVARHNGKTVFIEGALPGERVEVQVTEDKKQYARAKVVRILK
PSPERVTPRCPHFGVCGGCQLQHLSIDAQIASKQRALEDLLKHLAGVEPEEVLPPIAGPPWGYRRRARLS
VRYVPKKGQLLVGFREKNSSDIVDIDQCPVLVPPLSALLPPLRALLSSLSAKRRLGHVELAQGDNGTALV
LRHLEPLSEADRAKLRAFAEQHGLQLYLQPKGPDLVHLLGPADAQLSYYLPEFGLRLAFSPRDFIQVNAQ
VNQKMVARALEWLDPQPGDRVLDLFCGLGNFTLPLARQAAEVVGVEGVEAMVERARENARRNGLDNVTFY
HANLEEDFTDQPWALGGFDKVLLDPPRAGAAEVMQALAKLGPKRIVYVSCNPATLARDAGVLVEAGYRLK
RAGMLDMFPHTGHVESMALFERG
>gnl|CDD|183876 PRK13169, PRK13169, DNA replication initiation control protein YabA
MDKKEIFDALDDLEQNLGVLLKELGALKKQLAELLEENTALRLENDKLRERLEELEAEEPAKEKKKKEGE
GKDNLARLYQEGFHICNLHYGSRRENGEDCLFCLELLNKK
>gnl|CDD|183877 PRK13170, hisH, imidazole glycerol phosphate synthase subunit HisH; Provisional
MNVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKACT
QPVLGICLGMQLLGERSEESGGVDCLGIIDGPVKKMTDFGLPLPHMGWNQVTPQAGHPLFQGIEDGSYFY
FVHSYAMPVNEYTIAQCNYGEPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLEM
>gnl|CDD|183878 PRK13181, hisH, imidazole glycerol phosphate synthase subunit HisH; Provisional
MIAIIDYGAGNLRSVANALKRLGVEAVVSSDPEEIAGADKVILPGVGAFGQAMRSLRESGLDEALKEHVE
KKQPVLGICLGMQLLFESSEEGNVKGLGLIPGDVKRFRSEPLKVPQMGWNSVKPLKESPLFKGIEEGSYF
YFVHSYYVPCEDPEDVLATTEYGVPFCSAVAKDNIYAVQFHPEKSGKAGLKLLKNFAEL
>gnl|CDD|237292 PRK13182, racA, chromosome-anchoring protein RacA
MKTPFVAKKLGVSPKTVQRWVKQLNLPCEKNEYGHYIFTEEDLQLLEYVKSQIEEGQNMQDTQKPSSNDV
EETQVNTIVQNISSVDFEQLEAQLNTITRRLDELERQLQQKADDVVSYQLLQHRREMEEMLERLQKLEAR
LKKLEPIYITPDTEPTYEREKKPKRRKMIFSIFGF
>gnl|CDD|171884 PRK13183, psbN, photosystem II reaction center protein PsbN
MEAMSPALSLAITILAILLALTGFGIYTAFGPPSKELDDPFDDHED
>gnl|CDD|183880 PRK13184, pknD, serine/threonine-protein kinase PknD
MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSI
CSDGDPVYYTMPYIEGYTLKSLLKSVWQKESLSKELAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLK
PDNILLGLFGEVVILDWGAAIFKKLEEEDLLDIDVDERNICYSSMTIPGKIVGTPDYMAPERLLGVPASE
STDIYALGVILYQMLTLSFPYRRKKGRKISYRDVILSPIEVAPYREIPPFLSQIAMKALAVDPAERYSSV
QELKQDLEPHLQGSPEWTVKATLMTKKKSCWKFYEPILLSKYFPMLESSPAQWYSLMISKIESSSETRLE
YTVTKKGLHEGFGILLPPSEEAERGDFYCGYGLWLHIKNNELSVSLVKNGLEIQKKSQEIISQQETFAIA
IEKSNHRISLFVDQTLWIIHIDYLPSRGGRIGIIIQDLQDIMSNIAIFESSGALRVSCLAVPDAFLAEKL
YDQALIFYRRIRESFPGRKEGYEAQFRLGITLLEKASEQGDPRDFTQALSEFSYLHGGVGAPLEYLGKAL
VYQRLGEYNEEIKSLLLALKRYSQHPEISRLRDHLVYRLHESLYKHRREALVFMLLALWIAPEKISSREE
EKFLEILYHKQQATLFCQLDKTPLQFRSSKMELFLSFWSGFTPFLPELFQRAWDLRDYRALADIFYVACD
LGNWEFFSQFSDILAEVSDEITFTESIVEQKVEELMFFLKGLEALSNKEDYEKAFKHLDNTDPTLILYAF
DLFAIQALLDEEGESIIQLLQLIYDYVSEEERHDHLLVYEIQAHLWNRDLKKAYKLLNRYPLDLLLDEYS
EAFVLYGCYLALTEDREAAKAHFSGCREDALFPRSLDGDIFDYLGKISDNLSWWEKKQLLRQKFLYFHCL
GDSEERDKYRQAYLSLENEFFL
>gnl|CDD|237293 PRK13185, chlL, protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
MALVLAVYGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTFTLTGKLVPTVIDILEEVDFHSEEL
RPEDFVYEGYNGVDCVEAGGPPAGTGCGGYVVGETVKLLKEHHLLDDYDVILFDVLGDVVCGGFAAPLQY
ADYALIVTANDFDSIFAANRIAAAIQAKAKNYKVRLAGVIANRSAGTDLIDKFNEAVGLKVLAHVPDLDA
IRRSRLKGKTLFEMEETDPGLEEVQNEYLRLAEQLLAGPEPLVPKPLKDREIFELLGFDY
>gnl|CDD|237295 PRK13187, PRK13187, UDP-3-O-acyl N-acetylglycosamine deacetylase
MSAPTGWATSQGTLARPLTIDGHGLHTGRRVGVRILPARPEDGVTGIVFRRVEQGRTLATLPVDPALRRA
QPLCTMLRNADGVGVRTVEHLLASLLACEIDHAIVELDAEEVPILDGSATPWVDAIRACGRVALDAPKRF
IRVLRTVVVTDGEGEQRREMRIEPAPRYELSVRNDLRGFGEMHWDGALTPAAFATEIAPSRSYGRVKWAV
PAILAGYLRGVPILRGARPSCTASIVGKRVLGGMRLPDEFVRHRVLDLVGDLALAGAPLLARVSALRPSH
EMNFRLVDALLAEPGAWQWAEFSE
>gnl|CDD|237296 PRK13188, PRK13188, bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; Reviewed
MMIKQRTIKKEVSLQGVGLHTGKEVTITFKPAPENHGYKFKRTDLEGQPIIDADVDNVVDTERGTTLEKN
GVKVHTVEHVLAALYGLGIDNCLIELDGPEPPIMDGSSKPFVEAIEEAGIVEQDAPRNYYVIKETIEYHD
EETGSEIIALPLDDFRITVMVDFDSKVLGSQHATLFDLSEFKKEIAPARTFVFLHEVEALLEQGLIKGGD
LDNAIVIVDKEMSQEELDKLAKKFGKDHISVKENGILNNRPLRFPNEPARHKLLDVIGDLALIGKPIKGR
IIAARPGHAINVEFAKKLKKYIKRNKIAQAPVYDPNKEPILDINRIMKILPHRYPFLLVDKIIELGDTKI
VGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNTVPDPENYSTYFMKIDKVKFRQKVVPGD
TLIFKVELLSPIRRGICQMQGKAYVNGKLVCEAELMAQIVKKKE
>gnl|CDD|237297 PRK13189, PRK13189, peroxiredoxin; Provisional
EEYEEIRMPLIGDKFPEFEVKTTHGPIKLPDDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNT
ELIGLSIDQVFSHIKWVEWIKEKLGVEIEFPIIADDRGEIAKKLGMISPGKGTNTVRAVFIIDPKGIIRA
ILYYPQEVGRNMDEILRLVKALQTSDEKGVATPANWPPNDLIKDKVIVPPASSVEEAKKRLEAKEKGEYE
CYDWWFCYKKLE
>gnl|CDD|106159 PRK13190, PRK13190, putative peroxiredoxin; Provisional
PVKLGQKAPDFTVNTTKGPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVD
SIYSHIAWLRDIEERFGIKIPFPVIADIDKELAREYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETG
RNIDEIIRITKALQVNWKRKVATPANWQPGQEGIVPAPSTLDEAEMRIKEPGAKTWYLKFKK
>gnl|CDD|183885 PRK13191, PRK13191, putative peroxiredoxin; Provisional
MSEGRIPLIGEKFPEMEVITTHGKIKLPDDYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTEL
IGLSVDSNISHIEWVMWIEKNLKVEVPFPIIADPMGNVAKRLGMIHAESSTATVRAVFIVDDKGTVRLIL
YYPMEIGRNIDEILRAIRALQLVDKAGVVTPANWPNNELIGDKVINPAPRTIKDAKMRLGQPFDWWFTYK
EVKTT
>gnl|CDD|183886 PRK13192, PRK13192, bifunctional urease subunit gamma/beta; Reviewed
MRLTPTELDRLLLFTAAELARKRRARGLKLNYPEAVALIADEVLEAARDGRSVAELIDLGRTILTTDDVL
PGVADMVPEVQVEATFPDGTKLVTVHDPIRPAEGDLADALYPGEILPGDGEIELNAGRPAVTLDVTNTGD
RPIQVGSHFHFFEVNRALRFDRAAAYGMRLDIPAGTAVRFEPGETKEVRLVPIGGARVVIGFNGLTNG
>gnl|CDD|237298 PRK13193, PRK13193, pyroglutamyl-peptidase I
MTVLLFGFEPFLEYKENPSQLIVEALNGSTILKEEVKGVILPVEYEKIEDLIVTKIREMKPILTLGIGVA
PGRAKITPEKIAINYKYSREGDNAGKKYKGEKIDPLGQDGIFTNIPVEDLVDLLNENGIPAELSLSAGSY
LCNNAMYIIIREARKYNSLGGFIHVPLHESYAARIQRPIPSMSLDTMIRGIRLSMEFILTNKKENLTFS
>gnl|CDD|183887 PRK13194, PRK13194, pyrrolidone-carboxylate peptidase; Provisional
MKVLVTGFEPFGGDKKNPTMDIVKALDGKKIGDAKVFGRVLPVSFKRAREELEKVLDEIKPDITINLGLA
PGRTHISVERVAVNAIDARIPDNDGEKPEDEPIVEGAPAAYFATLPTREIVEELKKNGIPAVLSYSAGTY
LCNYVMYLTLHHSATKGYPKMAGFIHVPYTPDQVIEKIGKGKNTPSMCLEMEIEAVKIAIRVALEELL
>gnl|CDD|171894 PRK13195, PRK13195, pyrrolidone-carboxylate peptidase; Provisional
MSKVLVTGFGPYGVTPVNPAQLTAEELDGRTIAGATVISRIVPNTFFESIAAAQQAIAEIEPALVIMLGE
YPGRSMITVERLAQNVNDCGRYGLADCAGRVLVGEPTDPAGPVAYHATVPVRAMVLAMRKAGVPADVSDA
AGTFVCNHLMYGVLHHLAQKGLPVRAGWIHLPCLPSVAALDHNLGVPSMSVQTAVAGVTAGIEAAIRQSA
DIREPIPSRLQI
>gnl|CDD|171895 PRK13196, PRK13196, pyroglutamyl-peptidase I
MPTLLLTGFEPFHTHPVNPSAQAAQALNGEQAGALRVHSALLPVEPRAAMAALSRLLDELQPSAVLLTGL
AAGRPQVTLERVAVNVMDFSIPDNAGQTYRDTPVCTEPDAPAAYLSTLPLRAILAAWHDAGIPGHISNTA
GLYVCNFVLYHALHQLHLRGRAEVPCGFLHVPANAQVALAVAGDRPPLPYLPQEEITRAVRVAAETMAGQ
N
>gnl|CDD|237299 PRK13197, PRK13197, pyrrolidone-carboxylate peptidase; Provisional
MMKILVTGFDPFGGEKINPSWEAVKQLPGKEIGGAEIIKRQLPTVFGKSAEVLKEAIEEVQPDAVICIGQ
AGGRTDITPERVAINIDDARIPDNEGNQPIDEPIVEDGPAAYFSTLPIKAMVKAIREAGIPASVSNTAGT
FVCNHVMYGLLHLLDKKYPNIRAGFIHIPYLPEQAVNKPGTPSMSLEDIVRGLELAIEAIVENEDDIKEV
GGATH
>gnl|CDD|171897 PRK13198, ureB, urease subunit beta; Reviewed
MRVKPELIIAEDSSMSAKKSTKDSKEQNTPLGGLVLAETPITFNENKPVTKVKVRNTGDRPIQVGSHFHF
FEVNRALEFDRAAAYGKRLNISSTTAIRFEPGDETEVPLIPFGGKQTLYGFNNLVDGWTGEGVVPNSERP
DKLAAIRLAAERGFKSSK
>gnl|CDD|237302 PRK13201, ureB, urease subunit beta; Reviewed
MIPGEIITKSTEVEINNHHPETVIEVENTGDRPIQVGSHFHFYEANAALDFEREMAYGKHLDIPAGAAVR
FEPGDKKEVQLVEYAGKRKIFGFRGMVNGPIDESRVYRPTDENDAYAGVFGDNGAENVNKKGGKRS
>gnl|CDD|106171 PRK13202, ureB, urease subunit beta; Reviewed
MIPGEIFYGSGDIEMNAAALSRLQMRIINAGDRPVQVGSHVHLPQANRALSFDRATAHGYRLDIPAATAV
RFEPGIPQIVGLVPLGGRREVPGLTLNPPGRLDR
>gnl|CDD|237303 PRK13203, ureB, urease subunit beta; Reviewed
MIPGEYITADGEIELNAGRETVTLTVANTGDRPIQVGSHYHFFEVNPALSFDREAARGMRLNIPAGTAVR
FEPGQTREVELVPLAGARRVYGFRGKVMGKLD
>gnl|CDD|171902 PRK13204, ureB, urease subunit beta; Reviewed
MAKEPTEAAHPQPEQTKTNHKAHRPVGGYVLAKDPIEINQGRPRTTLTVRNTGDRPIQIGSHFHFFEVNR
YLEFDRSKAFGLRLDIPANTAVRFEPGDEKEVTLVPFAGKRFIFGFNNLVDGWSGDGPTPDYQPNREIAA
ERAEKLGFKSCKSGGKDAK
>gnl|CDD|106174 PRK13205, ureB, urease subunit beta; Reviewed
MIPGEYILSSESLTGNVGREAKTIEIINTGDRPVQIGSHFHFAEVNPSISFDRSEGYGFRLDIPSGTAVR
LEPGDARTVNLVAIGGDRIVAGFRDLVDGPLEDLKVNVWEGREDGWRRSSAAGDAPQELPQVEAAERGRK
LDDATDVDTNVGTEEGFEEGRN
>gnl|CDD|237304 PRK13206, ureC, urease subunit alpha; Reviewed
MTRLSRERYAALYGPTTGDRIRLADTDLLIEVTEDRSGGPGLAGDEAVFGGGKVIRESMGQGRATRAEGA
PDTVITGAVILDHWGIVKADVGIRDGRIVAIGKAGNPDIMDGVHPDLVIGPSTEIIAGNGRILTAGAIDC
HVHFICPQIVDEALAAGITTLIGGGTGPAEGSKATTVTPGAWHLARMLEALDGWPVNVALLGKGNTVSAE
ALWEQLRGGAGGFKLHEDWGSTPAAIDACLRVADAAGVQVALHSDTLNEAGFVEDTLAAIAGRSIHAYHT
EGAGGGHAPDIITVASHPNVLPSSTNPTRPHTVNTLDEHLDMLMVCHHLNPAVPEDLAFAESRIRPSTIA
AEDVLHDMGAISMIGSDSQAMGRIGEVVLRTWQTAHVMKRRRGALPGDGRADNNRARRYVAKYTICPAVA
HGIDHEIGSVEVGKLADLVLWEPAFFGVRPHAVLKGGAIAWAAMGDANASIPTPQPVLPRPMFGAAPAAA
AATSVHFVAPQAIEDGLADRLGLRRRLVPVADTRAVGKADMPLNDALPDIEVDPDTFTVRIDGEVWEPQP
AAELPMAQRYFLF
>gnl|CDD|237305 PRK13207, ureC, urease subunit alpha; Reviewed
MAKISRRAYAEMYGPTTGDRVRLADTELWIEVEKDFTTYGEEVKFGGGKVIRDGMGQSQRARADGAVDTV
ITNALILDHWGIVKADIGIKDGRIVAIGKAGNPDIQDGVDIIIGPGTEVIAGEGLIVTAGGIDTHIHFIC
PQQIEEALASGVTTMIGGGTGPATGTNATTCTPGPWHIHRMLQAADAFPMNIGFLGKGNASLPEALEEQI
EAGAIGLKLHEDWGATPAAIDNCLSVADEYDVQVAIHTDTLNESGFVEDTIAAFKGRTIHTFHTEGAGGG
HAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDMLMVCHHLDPSIPEDVAFAESRIRRETIAAEDILH
DLGAISMISSDSQAMGRVGEVIIRTWQTAHKMKVQRGPLPGDSGRNDNFRVKRYIAKYTINPAIAHGISH
EVGSVEVGKLADLVLWKPAFFGVKPELVLKGGMIAWAPMGDPNASIPTPQPVHYRPMFGAYGGALAATSV
TFVSQAALDAGIPEKLGLKKRLVPVKNTRGITKADMKLNDATPKIEVDPETYEVRADGELLTCEPATVLP
LAQRYFLF
>gnl|CDD|237306 PRK13208, valS, valyl-tRNA synthetase; Reviewed
KMMPELPKKYDPEELEEKWQKIWEEEGTYKFDPDERKPVYSIDTPPPTVSGSLHIGHVFSYTHTDFIARY
QRMRGYNVFFPQGWDDNGLPTERKVEKYYGIRKDDISREEFIELCRELTDEDEKKFRELWRRLGLSVDWS
LEYQTISPEYRRISQKSFLDLYKKGLIYRAEAPVLWCPRCETAIAQAEVEYREREGKLNYIKFPVEDGEE
IEIATTRPELLPACVAVVVHPDDERYKHLVGKTAIVPLFGVEVPILADPLVDPDFGTGAVMICTFGDKTD
VTWWRELNLPTRIIIDEDGRMTEAAGKLAGLTIEEARKKIVEDLKSGGLLGKQEPIKHNVKFCERCDTPL
EILVTRQWFIKVLDLKEELLERGKEINWYPEHMRVRLENWIEGLNWDWCISRQRYFGTPIPVWYCKDCGH
PILPDEEDLPVDPTKDEPPGYKCPQCGSPGFEGETDVMDTWATSSITPLIVTGWERDEDLFEKVFPMDLR
PQGHDIIRTWLFYTILRAYLLTGKLPWKNIMISGMVLDPDGKKMSKSKGNVVTPEELLEKYGADAVRYWA
ASARLGSDTPFDEKQVKIGRRLLTKLWNASRFVLHFSADPEPDKAEVLEPLDRWILAKLAKVVEKATEAL
ENYDFAKALEEIESFFWHVFCDDYLELVKSRAYGEDEEEEQKSARYTLYTVLDTLLRLLAPFLPFITEEV
WSWLYGGSVHRASWPEPDEELIDEEDEELGELAKEILSAVRKYKSEAGLSLNAPLKKVEVYGPADLELLE
AAEEDLKAAGNIEELELVEGDPELEVEIIA
>gnl|CDD|237307 PRK13209, PRK13209, L-ribulose-5-phosphate 3-epimerase
MKMLSKQIPLGIYEKALPAGECWLEKLAIAKTAGFDFVEMSVDESDERLARLDWSREQRLALVNALVETG
FRVNSMCLSAHRRFPLGSEDDAVRAQALEIMRKAIQLAQDLGIRVIQLAGYDVYYEQANNETRRRFIDGL
KESVELASRASVTLAFEIMDTPFMNSISKALGYAHYLNSPWFQLYPDIGNLSAWDNDVQMELQAGIGHIV
AFHVKDTKPGVFKNVPFGEGVVDFERCFKTLKQSGYCGPYLIEMWSETAEDPAAEVAKARDFVKARMAEA
GMV
>gnl|CDD|237308 PRK13210, PRK13210, L-ribulose-5-phosphate 3-epimerase
RKHPLGIYEKALPKHLSWEERLVFAKELGFDFVEMSVDESDERLARLDWSKEERLSLVKAIYETGVRIPS
MCLSGHRRFPFGSRDPATRERALEIMKKAIRLAQDLGIRTIQLAGYDVYYEEKSEETRQRFIEGLAWAVE
QAAAAQVMLAVEIMDTPFMNSISKWKKWDKEIDSPWLTVYPDVGNLSAWGNDVWSELKLGIDHIAAIHLK
DTYAVTETSKGQFRDVPFGEGCVDFVGIFKTLKELNYRGPFLIEMWTEKAEEPRAEIKQARRFLEPLMEE
AGLA
>gnl|CDD|237309 PRK13211, PRK13211, N-acetylglucosamine-binding protein GbpA
MKMKLNKLALAAALLLVSGSALAHGYVSSPESRAYLCKLGAGEKNTNCGAVQYEPQSVEGPSGFPESGPP
DGKIASAGNAQFSPLDEQTADRWVKRPIKAGPNTFEWTFTANHVTRNWRYYITKQDWNPNQPLTRDSFDL
TPFCVVDGGMVQPPKRVSHECNVPERTGYQVILAVWEVGDTANSFYNVIDVNFDGGGGVVPEWSKVGQIN
PSMDLKAGDKVMTRVFDANGENPALQTELTIDSATQGKKNNWSHALASKINQEQQQLRAGQLNADGQIEP
VYGKNPIYLKAGSGLERVEIGYDIEAPAPDYELEVSGLAKEYKIGDGAATLDFTVTATGDMNVEATVYNH
DGEALGSKSQTVNDGSQSVSLDLSKLKAGHHMLVVKAKPKDGELIKQQTLDFMLEAKDPPPSGDYDFVFP
EGLKSYTAGTKVLQPKDGKVYQCKPFPYSGYCVQWSASATQFEPGVGSHWGMAWIELG
>gnl|CDD|106181 PRK13213, araD, L-ribulose-5-phosphate 4-epimerase; Reviewed
MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLATGKVVEGD
KKPSSDTDTHLVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGD
YEHETGKVIVETFAEQGLRAADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGVGDM
QQTLLDKHYLRKHGAAAYYGQ
>gnl|CDD|183900 PRK13216, PRK13216, photosystem I reaction center subunit X-like protein; Reviewed
MSSILLAAQATVPKTGTTWNWTGTPIIIGSCLLVLLIAGRSIRYPHVGPKMPLPFPSLFNNPSVATFLAA
MSFGHIIGVAAVLGLTNLGVI
>gnl|CDD|237310 PRK13222, PRK13222, N-acetylmuramic acid 6-phosphate phosphatase MupP
MKFMDIRAVAFDLDGTLVDSAPDLAAAVNAALAALGLPPAGEERVRTWVGNGADVLVERALTWAGREPDE
ELLEKLRELFDRHYAENVAGGSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVI
GGDSLPNKKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVTYGYNYGEPIALSEPDVV
IDHFAELLPLLGLALS
>gnl|CDD|171912 PRK13223, PRK13223, phosphoglycolate phosphatase; Provisional
MSGFEQLFPGRLPRLVMFDLDGTLVDSVPDLAAAVDRMLLELGRPPAGLEAVRHWVGNGAPVLVRRALAG
SIDHDGVDDELAEQALALFMEAYADSHELTVVYPGVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKI
GRYFRWIIGGDTLPQKKPDPAALLFVMKMAGVPPSQSLFVGDSRSDVLAAKAAGVQCVALSYGYNHGRPI
AEESPALVIDDLRALLPGCADPAAEITLPDLQPSQSRESIVVVTRKLWMKVIKALARWRWRA
>gnl|CDD|106187 PRK13225, PRK13225, phosphoglycolate phosphatase; Provisional
MWKRSWKAFIARLSAIDPCGKAVEKLRGFSTGGIKGGSFLHRLKGFSTRNPQVFPQSYPQTLQAIIFDFD
GTLVDSLPTVVAIANAHAPDFGYDPIDERDYAQLRQWSSRTIVRRAGLSPWQQARLLQRVQRQLGDCLPA
LQLFPGVADLLAQLRSRSLCLGILSSNSRQNIEAFLQRQGLRSLFSVVQAGTPILSKRRALSQLVAREGW
QPAAVMYVGDETRDVEAARQVGLIAVAVTWGFNDRQSLVAACPDWLLETPSDLLQAVTQLMRQ
>gnl|CDD|237311 PRK13226, PRK13226, phosphoglycolate phosphatase; Provisional
QLLTEVAAVRFPRAVLFDLDGTLLDSAPDMLATVNAMLAARGRAPITLAQLRPVVSKGARAMLAVAFPEL
DAAARDALIPEFLQRYEALIGTQSQLFDGVEGMLQRLECAGCVWGIVTNKPEYLARLILPQLGWEQRCAV
LIGGDTLAERKPHPLPLLVAAERIGVAPTDCVYVGDDERDILAARAAGMPSVAALWGYRLHDDDPLAWQA
DVLVEQPQLLWNPATWPQT
>gnl|CDD|183903 PRK13230, PRK13230, nitrogenase reductase-like protein; Reviewed
MRKFCFYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKIPTVLDVLREKGIDNLGLE
DIIYEGFNGIYCVESGGPEPGYGCAGRGVITAIDLLKKLGVFEELGPDVVIYDILGDVVCGGFAMPLQKG
LADDVYIVTTCDPMAIYAANNICKGIKRFAKRGKSALGGIIYNGRSVIDAPDIVEEFAKKIGTNVIGKIP
MSNIITEAEIYGKTVIEYAPDSEISNIFRELAEAIYENNTGTIPNPLEEEEIDQIGEKIKELIKKQKIV
>gnl|CDD|183904 PRK13231, PRK13231, nitrogenase reductase-like protein; Reviewed
VMKKIAIYGKGGIGKSTTVSNMAAAYSNDHRVLVIGCDPKADTTRTLCGKRIPTVLDTLKDNRKPELEDI
IHEGFNGILCVESGGPEPGVGCAGRGVIVAMNLLENLGVFDEDIDVVIYDVLGDVVCGGFSVPLREDYAD
EVYIVTSGEYMSLYAANNIARGIKKLKGKLGGIICNCRGIDNEVEIVSEFASRIGSRIIGVIPRSNLVQE
SELDAKTVVETFPESEQASVYRKLANNIMNNTEFSTPEPMDDEEFEEFFKSFRD
>gnl|CDD|183905 PRK13233, nifH, nitrogenase iron protein
MTRKIAIYGKGGIGKSTTTQNTAAAMAYFHDKKVFIHGCDPKADSTRLILGGKPQTTMMDTLRELGEEKV
TPDKVIKTGFKDIRCVESGGPEPGVGCAGRGVITAIDLMEENGAYTDDLDFVFFDVLGDVVCGGFAMPIR
DGKAQEVYIVASGEMMAIYAANNICKGLVKYAEQSGVRLGGIICNSRNVDGELELLEEFTDAIGTQMIHF
VPRDNIVQKAEFNKKTVVEFDPDCNQAKEYKELARKIIENKDFVIPKPLTMDELEEMVVKYGLMD
>gnl|CDD|237314 PRK13238, tnaA, tryptophanase
MENMKHLPEPFRIKMVEPIRLTTREERERALAEAGYNPFLLKSEDVFIDLLTDSGTGAMSDRQWAAMMRG
DEAYAGSRSYYRLEDAVKDIFGYPYTIPTHQGRAAEQILFPVLIKKGDVVPSNYHFDTTRAHIELNGATA
VDLVIDEALDTGSRHPFKGNFDLEKLEALIEEVGAENVPFIVMTITNNSAGGQPVSMANLRAVYEIAKKY
GIPVVIDAARFAENAYFIKQREPGYKDKSIKEIAREMFSYADGLTMSAKKDAMVNIGGLLCFRDEDLFTE
CRTLCILYEGFPTYGGLAGRDMEALAVGLYEGMDEDYLAYRIGQVEYLGEGLEEAGVPIQTPAGGHAVFV
DAGKFLPHIPAEQFPAQALACELYLEAGIRGVEIGSLLLGRDPKTGEQLPAPAELLRLAIPRRVYTQSHM
DYVAEALKAVKENRESIKGLRFTYEPPVLRHFTARLKPVS
>gnl|CDD|183911 PRK13239, PRK13239, alkylmercury lyase MerB
MKLITEILERLASTEEPGGTATLLVPLLRLLAKGRPVSVTTLAAALGWPVEEVEAVLEAMPDTEYDEDGR
IIGYGLTLRPTPHRFEVDGRQLYTWCALDTLIFPALIGRTARVESHCPATGAPVRLTVTPSGVTAVEPAT
AVVSLVLPDEAADVRSSFCCHVHFFASPEAAEPWLSEHPGATIVSVAEAFQLGQELNTHLLQTAES
>gnl|CDD|183912 PRK13240, pbsY, photosystem II protein Y; Reviewed
IDLRLLIVLAPILAAAGWAVFNIGKAAREQFQRFLNRKAK
>gnl|CDD|183913 PRK13241, ureA, urease subunit gamma; Provisional
MHLTPREKDKLLIFTAALLAERRKARGLKLNYPEAVALISDALLEGARDGKTVAELMSYGRTVLTRDDVM
EGVPEMIPDVQVEATFPDGTKLVTVHDPIR
>gnl|CDD|139420 PRK13242, ureA, urease subunit gamma; Provisional
MHLTPREFDKLVIHMLSDVALKRKNKGLKLNHPEAVAVLSAYVLDGAREGKTVEEVMDGARSVLKADDVM
DGVPDLLPLIQVEAVFSDGSRLVSLHNPIT
>gnl|CDD|183914 PRK13243, PRK13243, glyoxylate reductase; Reviewed
MKPKVFITREIPENGIEMLEEHFEVEVWEDEREIPREVLLEKVRDVDALVTMLSERIDCEVFEAAPRLRI
VANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGVAWHP
LMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEAEKELGAEYRPLEELLRESDFVSL
HVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFEEEPYYNEELFSL
KNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTLVNREVVKVRKPGF
>gnl|CDD|183915 PRK13244, PRK13244, protease inhibitor
MRLTARWAAALTLTAAAVLGPLAGAAAAAPEAAASSLYAPSALVLTVGHGEAAATAAPERAVTLTCAPTA
SGTHPAAAAACAELRAVGGDFEELTAVPPEAMCTRDYDPVVVTATGVWQGKRVAYERTFANECVKKSQTG
AVFDF
>gnl|CDD|183916 PRK13245, hetR, heterocyst differentiation control protein; Reviewed
MSNDIDLIKRLGPSAMDQIMLYLAFSAMRTSGHRHGAFLDAAATAAKCAIYMTYLEQGQNLRMTGHLHHL
EPKRVKIIVEEVRQALTEGKLLKMLGSQEPRYLIQLPYVWLEQYPWHPGRSRLPGTSLTSEEKRQIEAKL
PSNLPDAQLVSSFEFLELIEFLHKRSQEDLPPEHRMPLSEALAEHIKRRLLYSGTVTRIDSPWGMPFYAL
TRPFYAPADDQERTYIMVEDTARYFRMMKDWAERRHNVMRILEELDIPPERMEQAMEELDEIIRHWADKY
HQDGGIPMVLQMVFGPKDD
>gnl|CDD|106208 PRK13246, PRK13246, 15,16-dihydrobiliverdin:ferredoxin oxidoreductase
MFDSLVDFLKTNIDELNGHELQISKEFKEHHNKDSKYIIKNWLFSSPEYRKWRITRLDGGKKLQVFNTVA
YPNFKSELPILGADILWFGTSQKLLAILDYQPLIQEKKYLEKYCSSLGFIKKKYSAFDNNKMKNIYDSKK
YFSPWVIICRGNKLNLDRDLNNIFHSFVNNYLNINKSNPVNQFLNLEEIKINQIKYDKYSFEKDPADKLF
KSFFGEKWTKKFINKFLFTLNNEIIH
>gnl|CDD|237315 PRK13247, PRK13247, 15,16-dihydrobiliverdin:ferredoxin oxidoreductase
MFDPFLEELHKEIFSRGGQSLPVPAGLEECVSEKGNAVIRSWLWQVPGFRRWRVTRLDAGDSLQVLNSVA
YPDYNYDLPLMGIDLLWFGKKQKLVAVLDFQPLVQDKDYLDRYFEGLKSLKERFPDLNSEETMRFYDPNQ
YFSPWLLFCKGGAETATNSLPKAFSAFLKAYWQLHDNAKKITSTIEIQEVVQLQIDYDIYSAERDPAHGL
FSSYFGKEWSERFLHEFLFPASVPLAVS
>gnl|CDD|139425 PRK13248, PRK13248, phycoerythrobilin:ferredoxin oxidoreductase; Provisional
MLIQDTIFYRPDWRWHNFLKYLTNNLSKYNCLEKKIPSEYSYKDSTYGSKKSKKNVNLSTWGVTHKKRIQ
FARAVCINSPNYSVLNFLIIPNTIYNVPFFGVDFVSLPNSHLLVLDFQPSLKIQNQYNNELLEKLIKLKN
HCHSSLPLAEKMSADVARFFSPGVIWSKLPKEERSDFLIENQLYTSFKEYLDLYLEILFESKEVNIGLQK
ELINGQNNYLNYRRDNDPARPMLSSLFGKEFTESLINEVLFTT
>gnl|CDD|139426 PRK13249, PRK13249, phycoerythrobilin:ferredoxin oxidoreductase; Provisional
MKILRNSSLDPVSIPGWRWQPFLDDAIKALSPFQPEPYPVAEDFLQRESQTGSKSKPVKVTTATWACKTE
KIRQVRAACVEAGEAASVLNFVINPSNRFDLPFFGADLVTLPNGHLLALDLQPALKTDEIHTQHVWERLM
PIFEHWQSKLPSGGPIPEEAQPYFSPGFLWTRLPLGEEGDNLISEVIRPAFDEYLNLYLDLVEEAKPVSK
ERAFKLLEGQKRYTSYRAEKDPARGMLTRFHGSEWTESYIHNVLFDL
>gnl|CDD|139427 PRK13250, PRK13250, phycoerythrobilin:ferredoxin oxidoreductase; Provisional
MTLYQPFLDYAITLLTERLELQPYPIPAGFERKEAMTGKGKKQEEVVTTSYAFQSPKLRQIRAAHVQGGS
ALQVLNFVIFPHLNYDLPFFGADLVTLPGGHLIALDMQPLFRDDPAYQAKYTEPILPLFNAHQAHLPWGG
DFPEEAKPFFSPAFLWTRPQETEVVETRVFEAFKDYLQAYLDFVEQAEAVTDSEQLAEILQAQLRYLRYR
AEKDPARGMFTRFYGEEWTEEYIHGFLFDLERKLSAVH
>gnl|CDD|183917 PRK13251, PRK13251, trp RNA-binding attenuation protein MtrB
MEMYINGDYVVIKALENGVNVIGLTRGKDTKFHHTEKLDKGEVMIAQFTEHTSAIKIRGKAEIQTKHGEI
ESEEK
>gnl|CDD|183918 PRK13252, PRK13252, betaine aldehyde dehydrogenase; Provisional
MSRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSR
ILRRAVDILRERNDELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRR
EPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR
VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSS
GQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLL
CGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTA
DLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMGPFQSPF
>gnl|CDD|237316 PRK13253, PRK13253, citrate lyase subunit gamma; Provisional
MKIKKTAVAGTLESSDVMIRIAPADTQGIDIQLESSVEKQFGDQIRAVILETLAKLGVENAQVKVDDKGA
LDCVIRARLEAAVLRAAGIEAL
>gnl|CDD|237317 PRK13254, PRK13254, cytochrome c maturation protein CcmE
MMKRKRRRLLIILGALAALGLAVALVLYALRQNIVFFYTPSEVAEGEAPAGRRFRLGGLVEKGSVQRGDG
LTVRFVVTDGNATVPVVYTGILPDLFREGQGVVAEGRLQDGGVFVADEVLAKHDENYMPKEVADALKKAG
VWKDGPGQ
>gnl|CDD|183921 PRK13255, PRK13255, thiopurine S-methyltransferase; Reviewed
MDPDFWHEKWAENQIGFHQEEVNPLLQKYWPALALPAGSRVLVPLCGKSLDMLWLAEQGHEVLGVELSEL
AVEQFFAENGLTPQTRQSGEFEHYQAGEITIYCGDFFALTAADLADVDAVYDRAALIALPEEMRERYVQQ
LAALLPAGCRGLLVTLDYPQEELAGPPFSVSDEEVEALYAGCFEIELLERQDVLEDNPKFVKKGVSRLNE
AVYLLERK
>gnl|CDD|237318 PRK13256, PRK13256, thiopurine S-methyltransferase; Reviewed
MNKLETNNNQYWLDRWQNDDVGFCQESPNEFLVKHFSKLNINDSSVCLIPMCGCSIDMLFFLSKGVKVIG
IELSEKAVLSFFSQNTINYEVIHGNDYKLYKGDDIEIYVADIFNLPKIANNLPVFDIWYDRGAYIALPND
LRTNYAKMMLEVCSNNTQILLLVMEHDKKSQTPPYSVTQAELIKNFSAKIKFELIDSKQRDNIPDYRKAE
GMTEQYYTTYLRKKQY
>gnl|CDD|237321 PRK13259, PRK13259, septation regulator SpoVG
MEVTDVRLRKVNTEGRMKAIVSITFDNEFVVHDIRVIEGNNGLFIAMPSKRTPDGEFRDIAHPINSDTRE
KIQDAILKEYERVGEEEEEEEGAS
>gnl|CDD|183926 PRK13260, PRK13260, 2,3-diketo-L-gulonate reductase; Provisional
MKVTFEELKAAFKRVLLSRGVDEETADACAEMFARTTESGVYSHGVNRFPRFIQQLENGDIIPDAQPQRV
TSLGAIEQWDAQRAIGNLTAKKMMDRAIELARDHGIGLVALRNANHWMRGGSYGWQAAEKGYIGICWTNS
IAVMPPWGAKECRIGTNPLIVAIPSTPITMVDMSMSMFSYGMLEVNRLAGRQLPVDGGFDDEGNLTKDPG
VIEKNRRILPMGYWKGSGLSIVLDMIATLLSGGASVAEVTEDNSDEYGVSQIFIAIEVDKLIDGATRDAK
LQRIMDYVTTAERADENQAIRLPGHEFTTLLAENRRNGIPVDDSVWAKIQAL
>gnl|CDD|237322 PRK13261, ureE, urease accessory protein UreE; Provisional
MMIITQILGNISDLPLAAGAVETVTLEADERVKRRLRVTTDHGEEIGLRLPRGTVLRDGDVLFLDDGRVI
VVRAAPEDVLVVRPRDPLELARAAYHLGNRHVPLQIEGDELLVPYDHVLEDMLEGLGLTVTEVEAPFEPE
RGAYGGAFRHHGHSHDHSH
>gnl|CDD|183928 PRK13262, ureE, urease accessory protein UreE; Provisional
MILIEHILGNVKKDPVWREKLKDATFDLLILDQREAQKSRCRKSSTQGLDLGISLDRNVVLADGDVLAWD
EETNVAVVVQINLRDVMVIDLSELKSRSPDELIKTCFELGHALGNQHWKAVTKHNEVYVPLTVATTMMDS
VMRTHGFQHLPFRFVKGAEILPLLTNSEARLLFGGAEDTDTHVHVASPLDEPHGSGLHIHGIHSHEEGHS
HGDHDHDHSHSHGDHDHDHKH
>gnl|CDD|237323 PRK13263, ureE, urease accessory protein UreE; Provisional
MLTIDKRIAPNVGLAAVLVKRAPTLTLAFDARCKSRLAATLDTGREVAVVLPRGTVLRDGDVLVAEDGAL
VRVAAAPEAVLRVRAGDPLTLMRAAYHLGNRHTPVEVGADYLKLEYDPVLADMLRRLGVTVERASAPFEP
EAGAYGGGHRHGHDATFAEDYALAQQVFHEHHGHSHSHSDHDHDHDHDHDHVHGPGCGHGHHHHHR
>gnl|CDD|183930 PRK13264, PRK13264, 3-hydroxyanthranilate 3,4-dioxygenase; Provisional
MKILKPFNLHKWIEEHRHLLKPPVGNKQIWQDSDFIVMVVGGPNARTDFHYDPGEEFFYQLEGDMYLKVQ
EDGKRRDVPIREGEMFLLPPHVPHSPQREAGSIGLVIERKRPEGELDGFQWYCDECNHKVHEVEVQLTDI
ETDLPPVFAAFYASEELRTCDNCGTVHPGKARPAACE
>gnl|CDD|183931 PRK13265, PRK13265, glycine/sarcosine/betaine reductase complex protein A; Reviewed
MSLLEGKKVIIIGDRDGIPGPAIEECVKTTGAEVVFSSTECFVUTAAGAMDLENQKRVKDLAEKFGAENV
VVILGAAEAEAAGLAAETVTNGDPTFAGPLAGVQLGLRVYHVVEPEIKEEVDPAVYEEQISMMEMVLDVD
EIIEEVKKIREEYC
>gnl|CDD|237325 PRK13267, PRK13267, archaemetzincin-like protein; Reviewed
MMKILIVPIGYVPASVIREASNNLRSVYLDCDVTVDSRQSLPISAYDWERGQYRAEKFLPLLSRIGRFNG
DKNIGITDCDLYYRGLNFVFGLAYPNLRGAVISTYRLRPEFYGNKPDSELFEERVRKEVTHELGHTLGLE
HCDNPRCVMNFSNSVRDVDIKEPNFCGSCQRKLERNLKY
>gnl|CDD|183934 PRK13270, treF, alpha,alpha-trehalase TreF
MLNQKIQNPNPDELMIEVDLCYELDPYELKLDEMIEAEPEPEMIEGLPASDALTPADRYLELFEHVQSSK
IFPDSKTFPDCAPKMDPLDILIRYRKVRRHRDFDLRKFVENHFWLPEVYSSEYVSDPQNSLKEHIDQLWP
VLTREPQDHIPWSSLLALPQSYIVPGGRFSETYYWDSYFTMLGLAESGREDLLKCMADNFAWMIENYGHI
PNGNRTYYLSRSQPPVFALMVELFEEDGVRGARRYLDHLKMEYAFWMDGAESLIPNQAYRHVVRMPDGSL
LNRYWDDRDTPRDESWLEDVETAKHSGRPPNEVYRDLRAGAASGWDYSSRWLRDTGRLASIRTTQFIPID
LNAFLYKLESAIANISALKGEKETEALFRQKASARRDAVNRYLWDDENGIYRDYDWRREQLALFSAAAIV
PLYVGMANHEQADRLANAVRSRLLTPGGILASEYETGEQWDKPNGWAPLQWMAIQGFKMYGDDLLGDEIA
RSWLKTVNQFYQEHHKLIEKYHIAGGVPREGGGGEYPLQDGFGWTNGVVRRLIGLYGEP
>gnl|CDD|237326 PRK13271, treA, alpha,alpha-trehalase TreA
MKSPAPRRPVLLQQAMALAPAGILLCFAALSVQAEETSVTPQPPDILLGPLFNDVQNAKLFPDQKTFADA
VPNSDPLMILADYRMQQNQSGFDLRHFVNVNFTLPKEGEKYVPPEGQSLREHIDGLWPVLTRSTENTEKW
DSLLPLPEPYVVPGGRFREVYYWDSYFTMLGLAESGHWDKVADMVANFAHEIDTWGHIPNGNRSYYLSRS
QPPFFALMVELLAQHEGDAALKQYLPQMQKEYAYWMEGVENLQPGQQEKRVVKLQDGTLLNRYWDDRDTP
RPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLNTIRTTSIVPVDLNALMFKMEK
ILARASKAAGDNAMANQYETLANARQKAIEKYLWNDKEGWYADYDLKSHKVRNQLTAAALFPLYVNAAAK
DRANKVAAATKTHLLQPGGLNTTSVKSGQQWDAPNGWAPLQWVATEGLQNYGQKEVAMDVTWRFLTNVQH
TYDREKKLVEKYDVSSTGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPKEKPCDNVPATRPASKSATPPP
KTKEATPTP
>gnl|CDD|183936 PRK13272, treA, alpha,alpha-trehalase TreA
SPAAPPCCTSLLGLSLSLLLAPCSLTAAPLDGPVVNAPAPTPPTPDLAYPELFQAVQEGELFDDQKHFVD
ALPLRDPALINADYLAQHEHPGFDLRKFVDANFEESPPVQTDAIRQDTALREHIDALWPKLVRSQEQVPA
HSSLLALPHPYVVPGGRFREVYYWDSYFTMLGLVKSGQTTLSRQMLDNFAYLIDTYGHIPNGNRTYYLSR
SQPPFFSYMVELQAGVEGDAAYQRYLPQLQKEYAYWMQGSDDLQPGQAARHVVRLADGSLLNRYWDERDT
PRPEAWLHDTRTAAEAKDRPAAEVYRDLRAGAESGWDYSSRWLADGKTLASIRTTAIVPVDLNSLLYHLE
RTLAQACASSGLAACSQDYAALAQQRKQAIDAHLWNPAGYYADYDWQTRTLSEQVTAAALYPLFAGLASD
DRAKRTADSVRAQLLRPGGLATTALKTGQQWDEPNGWAPLQWVAVDGLRRYGEDALARTIGERFLAQVQA
LFAREHKLVEKYGLDGNAAGGGGGEYALQDGFGWTNGVTLMLLNLYPPGGAK
>gnl|CDD|237327 PRK13273, mdoD, glucan biosynthesis protein D; Provisional
FDFATLKARARALAAKPYVPPPRPLPDVLAKLSYDAYQSIRFRPEHALWAGEPLPFDVQFFHLGMLFRRP
VRIFVVEDGQAREIPYDPALFDYGKDGVDTKLLPGDLGFAGFRLHYPPDPLARRDFVSFLGASYFRAVGK
GQQYGLSARGLAIDTALPGGEEFPDFTAFWLERPKPGATTVTVYALLDSPSVTGAYRFTIRPGEGTVMDV
EATLFPRKDIERLGIAPLTSMFLFGENDRRMADDWRPEVHDSDGLAIWTGNGEWIWRPLNNPPRLQFSAF
SDENPKGFGLLQRDRDFDHYQDDGVFYEKRPSLWVEPRGDWGKGAVQLVEIPTDDETNDNIVAFWVPEAP
PKAGQELRFAYRLYWGADPPVPSPLARVVATRTGMGGFPGQPRPKGARRFVVDFAGGALKAAAPKLKIEP
VITASRGEILQVSILYVPPIDGWRAQFDLVPTSDSTEPVELRLFLRTGGQPLSETW
>gnl|CDD|237328 PRK13274, mdoG, glucan biosynthesis protein G; Provisional
PAAPARMLRRRLLAAAAAALLLAAASAWAFSFDDVAKLARALAAKPYEAPKSNLPAALADLDYDDYRQIR
FRPDKALWRDEKTPFKLQFFHRGFYFDDPVKINEVTDGSVRPIPYDPDLFDFGDVKHDKDLPKDLGFAGF
RVHYPLNRPDKKDEIAVFLGASYFRAVGKGQVYGLSARGLAIDTALPSGEEFPRFREFWIERPKPDDKSL
VIYALLDSPSVTGAYRFVIRPGEDTVVDVQATLFPRDDVEKLGIAPLTSMFLFGPNQPSPADDFRPEVHD
SDGLLIHTGNGEWLWRPLNNPKRLQVSSFADENPKGFGLLQRDRAFSDYEDLEARYELRPSAWVEPKGDW
GKGAVELVEIPTDDETNDNIVAFWVPEQPPEAGQELRFAYRLTWGRDEPKLHAPDLAWVRQTRRSTGDVK
QSNLIRQPDGTRAFVVDFTGPALKKLPEDAPVVAQVSIASNGEIVESVVRRNPETGGWRLTFRVKPKDAK
PVELRAALRNGDQTLSETWSYRWPPN
>gnl|CDD|183939 PRK13275, mtrF, tetrahydromethanopterin S-methyltransferase subunit F; Provisional
GVPMSNKPNMSAIDNVVEDIRYKAQLIARNQKLESGVIATGIIGFAIGFLLALLLVVVPPLLYGLVG
>gnl|CDD|183940 PRK13276, PRK13276, iron-sulfur cluster repair di-iron protein ScdA
MINKNDIVADVVTDYPKAADIFRSVGIDFCCGGQVSIEAASLEKKNVDLNELLQRLNDVEQTNTPGSLNP
KFLNVSSLIQYIQSAYHEPLREEFKNLTPYVTKLSKVHGPNHPYLVELKETYDTFKNGMLEHMQKEDDVD
FPKLIKYEQGEVVDDINTVIDDLVSDHIATGQLLVKMSELTSSYEPPIEACGTWRLVYQRLKALEVLTHE
HVHLENHVLFKKVS
>gnl|CDD|183941 PRK13277, PRK13277, 5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase-like protein; Provisional
IDRKEIKEILEGYDLDKVKIGVLASHSALDVFDGAKDEGFRTIAVCQKGRERTYREFKGIVDEVIVLDKF
KDILSEKVQDELREENAIFVPNRSFAVYVGYDAIENEFKVPIFGNRYLLRWEERTGEKNYYWLLEKAGIP
YPKLFKDPEEIDRPVIVKLPEAKRRLERGFFTASSYEDFYEKSEELIKAGVIDREDLKNARIEEYVIGAH
FNFNYFYSPIRDRLELLGIDRRIQSNLDGFVRLPAPQQLKLNEEPRYIEVGHEPATIRESLLEKVFEIGE
KFVEATKELYPPGIIGPFTLQTIVTPDLDFVVYDVAPRIGGGTNVYMGVGSPYSKLYFGKPMSTGRRIAM
EIKRAIELGRLEKIVT
>gnl|CDD|237329 PRK13278, purP, formate--phosphoribosylaminoimidazolecarboxamide ligase
MINKEEILEILKKYDLDNITIATIGSHSSLQILKGAKKEGFRTIAICKKKREVFYKRFPVADEFIIVDDF
SDILNEAVQEKLREMNAILIPHGSFVAYLGLENVEKFKVPMFGNREILRWEADRDKERKLLEEAGIRIPR
KYESPEDIDRPVIVKLPGAKGGRGYFIAKSPEEFKEKIDKLIERGLITEVEEAIIQEYVVGVPYYFHYFY
SPIKNRLELLGIDRRYESNIDGLVRIPAKDQLELGIDPTYVVVGNIPVVLRESLLPQVFEYGERFVETSK
ELVPPGMIGPFCLESVVTDNLEIVVFEISARIVAGTNLYMNGSPYSYLYWDEPMSMGRRIAREIKLALEK
DRLEKILT
>gnl|CDD|237330 PRK13279, arnT, lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase
KMKSIRYLILLALFFALYYLLPLNTRLLWQPDETRYAEISREMLASGDWIVPHFLGLRYFEKPIAGYWIN
SIGQWLFGDNNFGVRFGSVFSTLLSALLVYWLALRLWRDRRTALLAALIYLSLFLVYGIGTYAVLDPMIT
LWLTAAMCSFWLALQAQTRRGKIGGYLLLGLACGMGFMTKGFLALAVPVISVLPWVIWQKRWKELLIYGP
LAVLSAVLVSLPWALAIAQREPDFWHYFFWVEHIQRFAEDDAQHKAPFWYYLPVLIAGSLPWLGLLPGAL
KQGWRERKKHPGTFYLLLWVVMPLLFFSIAKGKLPTYILPCFAPLAILMAHYAVDCAKNGNPRALRINGW
INLAFGLLGLIALLVVSPWGPLKHPVYQPNETYKVFLAWIAFLGWAFFGWLSLRNPLKRWALAALCPLGL
ALLVGAAIPDRVIDSKQPQFFIEMHQEELQSSRYILSDSVGVAAGLAWELKRSDIILYDQKGELKYGLSY
PDAKGRFVSLDDFPAWLAQHRQEGIVSLVLRLDRDEDLPELALPPADKVYRQGRLVLLQYRQ
>gnl|CDD|237331 PRK13280, PRK13280, N-glycosylase/DNA lyase; Provisional
MVNEERVRELGEILRELGIEGALEIEERVDPQYKAVENLVESLGEDLFAKLVIANALVSYQLSGKGEEWW
WEFSKYFSEKGVEDIVEAYIEFLKNSKGNRRLLEQKIKRIEKVEPFLESLTLLDLPLYYEDLEELLEQLA
KILGAKKESKTVVFAVKMFGYACRAAFGEFRPYPMEIPIPVDYRIAKLTKCSGLVEGPPEEAMRRYKLTQ
EEPIEFWNKVARESGIPPLHIDSILWLVLGALRDGKFRLKKAEEKVEILKELIALLQER
>gnl|CDD|237332 PRK13281, PRK13281, N-succinylarginine dihydrolase
MNAYEVNFDGLVGPTHNYAGLSFGNVASTSNAGQVSNPRAAAKQGLLKMKALADLGFPQGVLPPQERPDL
PLLRRLGFSGSDAQVLEKAAKQAPELLSAASSASSMWTANAATVSPSADTADGRVHFTPANLNNKLHRSI
EAPTTERLLRAIFADEAHFAVHPALPQVALFGDEGAANHNRLCGEYGEPGVELFVYGREAGNRAPPKRYP
ARQTLEASEAVARLHQLDPDRVVFAQQNPDVIDQGVFHNDVIAVGNRNVLFCHEQAFLDQEAVLAELRAK
LDGEFMAIEVPAAEVSVADAVKSYLFNSQLLTLPDGSMALVLPQECRENPAVWAYLNELVAGDGPIKEVK
VFDLRQSMRNGGGPACLRLRVVLNEAELAAVNPAVLMNDALFDRLNAWVDRHYRDRLTPADLADPQLLRE
SRTALDELTQILDLGSVYPFQR
>gnl|CDD|183946 PRK13282, PRK13282, flagellar assembly protein FliW; Provisional
MIFDVKSPILGFETIKKMELEKIDEVFVRLKSADGNSFSFTLINPFALREYEFEIPTYYKELLELEEASN
LLIANIMVIQTPIEESTVNFLAPVVFNLDNNTMGQVVLDSVKYPHYGQAEKISNYIKK
>gnl|CDD|183947 PRK13283, PRK13283, flagellar assembly protein FliW; Provisional
MNYFLKAPILGFEHINEVRLEKIDSLFSKIMGQTNSPALEIVLVNPYCLREYSFVIPKYIELLLDLDSHS
KVEVYCVVVLQKNLEDSMVNFLAPLVFNSKNGFAAQVALSMMDYPDFSFRDPLKSFVVKERERA
>gnl|CDD|237333 PRK13284, PRK13284, flagellar assembly protein FliW; Provisional
MKIESPLFGSVEVDPEKVITFPAGLPGFEDCKRFKLFHEEGPPEPTVFWLQSLDDPDVAFSITDPERLGV
RYEIELSDEEVALLQLERPEDAAVLVIVYRDEAEHPALGGLRANLRAPLVINPISRRGLQKVITGLKPDI
LLRNR
>gnl|CDD|237334 PRK13285, PRK13285, flagellar assembly protein FliW; Provisional
MKIITKRFGEIEIDEEDIITFPEGIPGFEDLKKFILLPLEEDSPFLWLQSVEDPDLAFVVIDPFNFFPDY
EFDLDEEELELLGIESEEDVLVLVIVTIPEDPEKITANLQAPIIINKKKRKGKQVILDNEKYSTKHPLFE
EAARESSE
>gnl|CDD|237335 PRK13286, amiE, aliphatic amidase
MRHGDISSSNDTVGVAVVNYKMPRLHTKAEVLENARKIADMIVGMKQGLPGMDLVIFPEYSTHGIMYDRQ
EMYETASTIPGEETAIFAEACRKAKVWGVFSLTGERHEEHPRKAPYNTLILINDKGEIVQKYRKIMPWCP
IEGWYPGDCTYVSEGPKGLKISLIICDDGNYPEIWRDCAMKGAELIVRCQGYMYPAKEQQVLVAKAMAWA
NNCYVAVANAAGFDGVYSYFGHSAIIGFDGRTLGECGEEEMGIQYAQLSVSQIRDARRNDQSQNHLFKLL
HRGYTGVINSGDGDKGVAECPFDFYRTWVTDPEKARENVEAITRSTVGTAECPVEGLPTEGKEEP
>gnl|CDD|183950 PRK13287, amiF, formamidase; Provisional
MGSLGSLNKPIEGVLVALIQYPVPVVESRADIDKQIEQIIKTVHKTKAGYPGLDLIVFPEYSTQGLNTKK
WTTEEFLCTVDGPEVDAFAQACKENKVWGVFSIMERNPDGNEPYNTAIIIDDQGEIILKYRKLHPWVPVE
PWEPGDLGIPVCDGPGGSKLAVCICHDGMFPEMAREAAYKGANVMIRISGYSTQVREQWILTNRSNAWQN
LMYTASVNLAGYDGVFYYFGEGQVCNFDGTTLVQGHRNPWEIVTAEVRPDLADEARLGWGLENNIYNLGH
RGYVAVPGGAKDCPYTYMKDLAAGKYKLPWEDEIKVKDGTIYGYPTPKRRFGK
>gnl|CDD|237336 PRK13288, PRK13288, pyrophosphatase PpaX; Provisional
MKINTVLFDLDGTLINTNELIISSFLHTLKTYYPNQYKREDVLPFIGPSLHDTFSKIDESKVEEMITTYR
EFNHEHHDELVTEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPD
PEPVLKALELLGAKPEEALMVGDNHHDILAGKNAGTKTAGVAWTIKGREYLEQYKPDFMLDKMSDLLAIV
GDMN
>gnl|CDD|237337 PRK13289, PRK13289, NO-inducible flavohemoprotein
MLSAQTIAIVKATVPLLEEHGEALTAHFYDRMFSHNPELKNIFNQSNQRNGDQPEALANAVLAYARNIDN
LEALLPAVERIAQKHVSLQIKPEHYPIVGEHLLAAIREVLGDAATDEVLDAWGEAYGVLADVFIGREAEI
YEEAASKPGGWRGWRDFRVVKKVPESEVITSFYLEPVDGGPVADFKPGQYLGVRLDPEGEEYQEIRQYSL
SDAPNGKYYRISVKREAGGKVSNYLHDHVNVGDVLELAAPAGDFFLDVASDTPVVLISGGVGITPMLSML
ETLAAQQPKRPVHFIHAARNGGVHAFRDEVEALAARHPNLKAHTWYREPTEQDRAGEDFDSEGLMDLEWL
EAWLPDPDADFYFCGPVPFMQFVAKQLLELGVPEERIHYEFFGPAKVLE
>gnl|CDD|183953 PRK13290, ectC, L-ectoine synthase; Reviewed
MIVRTLDEIEGTERDVKAGNWTSRRLLLKDDGMGFSFHETTIYAGTETHLHYKNHLEAVYCIEGEGEVED
LATGEVHPIRPGTMYALDKHDRHYLRAGEDMRLVCVFNPPLTGREVHDENGVYPL
>gnl|CDD|183954 PRK13291, PRK13291, putative metal-dependent hydrolase
MMDLRYPIGQFQYPEEITEEQIQEWIAEIEALPNELRAAVSGLSDEQLDTPYREGGWTVRQVVHHVADSH
MNAYIRFKLALTEDNPTIKPYDEEKWAELPDSKLPIEVSLVLLEGLHKRWVALLESLTEEDLERTFNHPD
GGETTLDEAIGLYAWHGRHHTAHITSLRKRKGW
>gnl|CDD|183955 PRK13292, PRK13292, NADH-quinone oxidoreductase subunit B/C/D
ETIPENILLASLDDLINWGRANSLWPMFFGLSCCFVEMMTSFTSRYDISRFGAEVLRGTPREADLMVIAG
TVFKKMAPSILRLYEQMAEPKWVISMGSCANSGGMYDVYSVVQGVNQILPVDVYIPGCPPRPEAFLQGLM
LLQEKIRREERPARPVLHLQGGSQGTTRPILVDGATKSRDTRGPGMEGIAIRGTAVQHPRFAGSRSDEMW
RPPAPKHPYPDFGLAGELEGAFGDDVRLDEGATDMLTYRCPPELVPEVLRHLKKRASSPFRRLEDLAAVD
ESCRRDREKFPDFTVNYHLLSFDTPGHVRIKTELRGRTPELPSATGVFPAANWYEREAFDMFGIRFAGHP
NLRRILMPPDWEGHPLRKEHPFRATEMPPYTRDDARRLQPLPAGDFFDRVDEETLILNLGPQHPGTHGII
RFVLKLDGEEIVDMDSDIGYHHRGAEKIGERQHWNQFIPYTDRIDYLAGVQNNLAYVNSVETLCGIEVPD
RAIYIRVMLSELFRIANHLVWLGTFAADVGAMTPVFYTFTDREKIFDIVEMITGGRMHPAWFRIGGVAED
LPEGWKEAVEAFLRWFPGRLKEYEDLLTGNPIFKARLKGVGVITRDEAVEWGISGPNLRACGLAWDLRKK
MPYGGYDRFDFEVPTAEGGDCYARYLVRMEEMRQSLRIVRQAAAGMPGGRWISDDYRYVLPQKRDTLKDI
ESLIHHFVNVTRGPAPPKGECYAAIEAPKGENGYFVVSDGLNIAYRMRIRTPSFPHIQALPLLSRGWLVA
DFLAIIGSIDFVLADLDR
>gnl|CDD|183956 PRK13293, PRK13293, F420-0--gamma-glutamyl ligase; Reviewed
MKMELIGVEGIPLIKPGDDLAELIAERYDLEDGDIIVIASTIVSKAEGRVIDLDDITPSERAIEIAKKLG
KDPRFVQAVLDESREIVVEAPFILTETKHGHVCANAGIDESNVPDGDLLLLPENPDESAERIREGLEELT
GKKVGVIITDTNGRPFRKGQRGVAIGVAGIPALWDWRGEKDLFGRELETTEVAVADELAAAANLVMGEGD
EGIPVVIIRGFNVPFGDGTGSKELFRPKEEDVFRQ
>gnl|CDD|183957 PRK13294, PRK13294, F420-0--gamma-glutamyl ligase; Provisional
MPGPDHGAAAGIEILPVPGLPEFRPGDDLAAAIAAAAPWLRDGDVLVVTSKIVSKAEGRLVRAPEDPEER
DALRRKLIDAEAVRVVARKGRTLITENRLGLVQAAAGVDASNVPRGELALLPVDPDASAAALRAGLRERL
GVDVAVVVTDTMGRAWRNGQTDAAIGAAGLAVLHDYAGAVDAYGNELVVTEVAVADEIAAAADLVKGKLT
GVPVAVVRGLGLLDDGSTARDLVRPGEEDLFRLGTAEALELGRREAVLLRRSVREFSDDPVDPEAVRRAV
AAALTAPAPHHTRPVRFVWLRSAAVRTRLLDAMRDAWRADLRADGLSEESIARRVRRGDILYDAPELVVP
FLVPDGAHSYPDARRTAAERTMFTVAVGAAVQNLLVALAVEGLGSCWIGSTIFAADVVRAVLDLPADWEP
LGAVAIGHPAEPPGPRPPRDPGDFLVER
>gnl|CDD|171961 PRK13295, PRK13295, cyclohexanecarboxylate-CoA ligase; Reviewed
MEFDAVLLPPRRAASIAAGHWHDRTINDDLDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAV
GLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGF
DHAAMARRLRPELPALRHVVVVGGDGADSFEALLITPAWEQEPDAPAILARLRPGPDDVTQLIYTSGTTG
EPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAE
LIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENG
AVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDADGW
FDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVP
RPGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGEDA
>gnl|CDD|106256 PRK13296, PRK13296, CCA tRNA nucleotidyltransferase
MKFYLVGGAVRDMLLGITPKDKDWVVVGATEDEMLANGFIKIAANFPVFIHPQTKQEYALARSEKKTASG
YHGFEVNFSKYITLEDDLKRRDLTINSIAIDQNNKVIDPFNGQADLQNRILRHTSIAFIEDPLRVVRLAR
FKAQLSNFNFSIAQEMLALIKELVKTGELNHLTRERLHIEFVKALNNPKIFFTTLKELEALKIIFPNISC
ILPLIPNKSFFENPIYKGSNINEKITLCLLKIPQQQLDDIRKELLLTNKHYKLLKASIAISKILEDRSIT
AEEIFQLIKNANIIRDKNLFAESLNLYKKYLKICDTITPHRNYQLLQTTINTIKNASIDSLTIKTIPKDK
LRNTLKQLKL
>gnl|CDD|139469 PRK13297, PRK13297, tRNA CCA-pyrophosphorylase; Provisional
MSRADDPGVAGLQVYIVGGAVRDALLGLPAGDRDWVVVGATPEDMARRGFIPVGGDFPVFLHPRTKEEYA
LARTERKSGRGYKGFTFYTGADVTLEQDLQRRDLTVNAIARTPQGELVDPLDGVADVRARVLRHVGEAFA
EDPVRILRLGRFAARFGDFSIAPETMQLCRRMVEAGEADALVPERVWKEVSRGLMAQAPSRMLDVLARAG
ALARVMPELHDDAAVRAEIDRAAAAGLPLAGRYALLCRHTPERDALGRRLRAPVECMDQARLLPLAVDAL
AASATPAAQLDLIERCDALRKPERFDALLQAAAIVAPVDLSAWRARVQAVRAIDAGAIARQCAGDPARIK
PALRQARLQALGGA
>gnl|CDD|237338 PRK13298, PRK13298, tRNA CCA-pyrophosphorylase; Provisional
MKIYLVGGAVRDSLLNLPVKDKDWVVVGGTPKILLSINFQQVGKDFPVFLHPETHEEYALARTERKSGVG
YTGFITDTSSDVTLEEDLIRRDLTINAIAQDENGNYIDPFQGKKDIQLRLLRHVSESFIEDPLRVLRVAR
FAALLVHLGFKIAKETMILMCIMVKKHELLYLTPERIWNETEKALKTDNPHVYFQVLYECNALKFLFPEI
DFLYEKPYFLNSFFKKFNLGNYILMGLSKISKLTKDIDIRFSYLCQFLGSMIPINQIKRNYKKIFFDKYA
ASLIKNLCKRFKIPSYIRNIAVLNTGFYFFLYNIHYQSSKNIITLFSKIDAWRKPDRIKKLIFLSNFNLL
RNKKSINFLIKQGNFLKKAFSVTKKISIKDILKKGFKGYEIKQELYRLRIHKLKFWRNKIIKHKFYL
>gnl|CDD|237339 PRK13299, PRK13299, tRNA CCA-pyrophosphorylase; Provisional
MMPSEFQKALPILEKIKEAGFEAYFVGGSVRDYLLGRPIHDVDIATSAYPEEVKAIFPRTVDVGIEHGTV
LVLENGEEYEVTTFRTESEYVDYRRPSEVTFVRSLEEDLKRRDFTINAIAMDENGEIIDLFDGLEDLKNR
LIRAVGNAEERFQEDALRMMRAVRFASQLGFDLETETFEAMKTQAPLLEKISVERIFVEFEKLLLGPFWR
KGLKLLIETGLYNYLPGLKGKEENLLKLTQLLWFSFETSEQAWAALLISLKIENIKSFLKAWKLSNKFIK
DVVKLLALYALRSERSWEKLDLYQYGKEIALLAEDLRQAQGLSVDEEAIQELYQALPIHDKKELAVNGGD
LLKHFGKKPGPWLGETLRKIEEAIVTGELENEKEAILEWLKEHL
>gnl|CDD|237340 PRK13300, PRK13300, CCA tRNA nucleotidyltransferase
EVLEEVLERIKPTEEEREKLKKVAEELIERLEEAIKELGLDAEVELVGSTARGTWLSGDRDIDIFVLFPK
DTSREELEEKGLEIGKEVAKELLGDYEERYAEHPYVTGEIDGFEVDIVPCYKVESGEEIISAVDRTPFHT
KYVKERLKGKLEDEVRLLKQFLKGIGVYGSELKTRGFSGYLCELLIIHYGSFENVLKAASKWKPPVKIDL
EKHGKEYKFDDPLVVIDPVDPNRNVAAALSLENLATFILAAREFLKNPSLEFFFPSDLSPEEILEELERR
GTTVLALEFPRPDIVEDILYPQLERSLRSIVKLLEREGFEVLRSGAWADEDRAYLLLELEVAELPNVKLH
IGPPVWVREHAENFIEKYEDSVYGPFIEGDRLYVERERKYTTAEELLESDALLKVSLGKNVLESLKEGDI
VLLVDILNGEFEIELAKFLSPKPPWLR
>gnl|CDD|106261 PRK13301, PRK13301, putative L-aspartate dehydrogenase; Provisional
MTHRIAFIGLGAIASDVAAGLLADAAQPCQLAALTRNAADLPPALAGRVALLDGLPGLLAWRPDLVVEAA
GQQAIAEHAEGCLTAGLDMIICSAGALADDALRARLIAAAEAGGARIRVPAGAIAGLDYLQAVAGRDDAE
VVYESRKPVAAWRAELPGMGIDPDTLAESRTLFSGPAREAALRFPKNLNVAATLALAGIGMTRTRVEVVV
DPRARGNQHRIQVRSPLGEMQIELVNAPSPANPKTSWLVAQSVLATIRRHLARFTIG
>gnl|CDD|237341 PRK13302, PRK13302, aspartate dehydrogenase
MSSRPELRVAIAGLGAIGKAIAQALDRGLPGLTLSAVAVRDPQRHADFIWGLRRPPPVVPLDQLATHADI
VVEAAPASVLRAIVEPVLAAGKKAIVLSVGALLRNEDLIDLARQNGGQIIVPTGALLGLDAVTAAAEGTI
HSVKMITRKPPDGLKGAPFLVTNNIDIDGLTEPLLLFEGSAREAAKGFPANLNVAVALSLAGIGPDRTTL
EIWADPGVTRNVHRIEVDADSARFSMTIENIPSENPKTGRITAQSVIALLRKQSAPLRVGT
>gnl|CDD|237342 PRK13303, PRK13303, aspartate dehydrogenase
MMKVAMIGFGAIGAAVLELLEHDPDLRVDWVIVPEHSIDAVRRALGEAVRVVSSVDALPQRPDLVVECAG
HAALKEHVVPILKAGIDCAVISVGALADEALRERLEQAAEAGGARLHLLSGAIGGIDALAAAKEGGLDEV
TYTGRKPPKSWRGTPAEQLCDLDALTEPTVIFEGSAREAARLFPKNANVAATVALAGLGLDRTRVELIAD
PAVTRNVHEIEARGAFGEFEFEMSGKPLPDNPKTSALTALSAIRALRNRAAAIVI
>gnl|CDD|237343 PRK13304, PRK13304, aspartate dehydrogenase
MLKIGIVGCGAIASLITKAILSGRINAELYAFYDRNLEKAENLASKTGAKACLSIDELVEDVDLVVECAS
VNAVEEVVPKSLENGKDVIIMSVGALADKELFLKLYKLAKENNCKIYLPSGAIVGLDGIKAASLGEIKSV
TLTTRKPPKGLEGALKELGIDLEEIKEPKVLFEGKAFEAVKKFPANINVAATLSLASIYPAKVKIIADPN
LDRNVHEITVKGSFGTFKTRVENVPCPDNPKTSALAAYSAIRLLKDLSEPIQVGT
>gnl|CDD|183962 PRK13305, sgbH, 3-keto-L-gulonate-6-phosphate decarboxylase UlaD
MSRPLLQLALDHTSLEAAQRDVTLLKDHVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGE
TLAQQAFGAGANWMTIICAAPLATVEKGHAVAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRD
AQASGQQWGEADLARMKALSDIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAADFHAQ
IDAIWGGK
>gnl|CDD|237344 PRK13306, ulaD, 3-dehydro-L-gulonate-6-phosphate decarboxylase
MSKPLLQIALDNQDLESAIEDAKKVAEEVDIIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGK
ILAKMAFEAGADWVTVICAAHIPTIKAALKVAKEFNGEIQIELYGNWTWEQAQQWRDAGISQVIYHRSRD
AQLAGVAWGEKDLNKVKKLSDMGFKVSVTGGLVVEDLKLFKGIPVKTFIAGRAIRGAADPAAAARAFKDE
IAKYWG
>gnl|CDD|183964 PRK13307, PRK13307, bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase
MYLIGEALIGEGNELAHIDLIIGDKEGPVGQAFANGLTQLSAGHTPLLAVIRPNLITKPATLIVPKVTVK
NMEQAELIFGPAQAAVAKAVADAVEEGIIPKDKAEDLVIVASVFIHPTAKDYNKIYQYNYGATKLAIKRA
LEGFPDVDKVLYEKDRALHPIMGFKVTRLWDPPYLQVALDLPDLEEVERVLSQLPKSDHIIIEAGTPLIK
KFGLEVISKIREVRPDAFIVADLKTLDTGNLEARMAADATADAVVISGLAPISTIEKAIHEAQKTGIYSI
LDMLNVEDPVKLLESLKVKPDVVELHRGIDEEGTEHAWGNIKEIKKAGGKILVAVAGGVRVENVEEALKA
GADILVVGRAITKSKDVRRAAEDFLNKLKPDIDQFRLMTDF
>gnl|CDD|183965 PRK13308, ureC, urease subunit alpha; Reviewed
MATIDRRAYAELYGPTTGDRVRLADTSLLAEVEHDHTVYGDECLFGGGKTLRDGMGMAPGVTSADGALDF
VLCNVTVIDPVLGIVKGDIGIRDGRIVGIGKAGNPDIMDGVDPRLVVGPGTDVRPAEGLIATPGAIDVHV
HFDSAQLVDHALASGITTMLGGGLGPTVGIDSGGPFNTGRMLQAAEAWPVNFGFLGRGNSSKPAALIEQV
EAGACGLKIHEDWGAMPAAIDTCLEVADEYDFQVQLHTDTLNESGFVEDTLAAIGGRTIHMYHTEGAGGG
HAPDIIRVVGEPHCLPSSTNPTNPYTVNTFDEHLDMTMVCHHLNPDVPEDVAFAESRIRAQTIAAEDVLH
DIGAISMLGSDSQGMGRIAEVIARTWQLASKMKDQRGPLPEDRGTFADNARIKRYIAKYTINPAITFGID
DHIGSLEPGKLADIVLWRPAFFGIKPELVIKGGFPAWAAMGDANGSLMTCEPMLQRPQWGAFGRAKQALS
VCFVSPLAIEAGLGERLGLRKRLLPVRGTRTLTKADMLHNDACPDIRVDPQTFEVFVDGELVTCEPATEL
PLAQRYMLR
>gnl|CDD|183966 PRK13309, ureC, urease subunit alpha; Reviewed
MPQISRQEYAGLFGPTTGDKIRLGDTNLFIEIEKDLRGYGDESVYGGGKSLRDGMGANNNLTRDNGVLDL
VITNVTIVDARLGVIKADVGIRDGKIVGIGKSGNPSTMDGVTQGMVVGVSTDAISGEHLILTAAGIDTHI
HLISPQQAYHALSNGVTTFFGGGIGPTDGTNGTTVTPGPWNIRQMLRSIEGLPVNVGILGKGNSYGRGPL
LEQAIAGVAGYKVHEDWGATAAALRHALRVADEVDIQVAVHTDSLNECGYVEDTIDAFEGRTIHTFHTEG
AGGGHAPDIIKVASQTNVLPSSTNPTLPYGVNSQAELFDMIMVCHNLNPNVPADVAFAESRVRPETIAAE
NVLHDMGVISMFSSDSQAMGRVGENWLRAIQTADAMKAARGKLPEDAAGNDNFRVLRYVAKITINPAITQ
GVSHVIGSVEVGKMADLVLWEPRFFGAKPKMVIKGGMINWAAMGDPNASLPTPQPVFYRPMFGAMGKTLQ
DTCVTFVSQAALDDGVKEKAGLDRQVIAVKNCRTISKRDLVRNSQTPNIEVDPETFAVKVDGVHATVKPI
ATASLNQRYFFS
>gnl|CDD|183967 PRK13310, PRK13310, N-acetyl-D-glucosamine kinase; Provisional
MYYGFDIGGTKIELGVFNEKLELQWEERVPTPRDSYDAFLDAVCELVAEADQRFGCKGSVGIGIPGMPET
EDGTLYAANVPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVF
NGKPISGRSYITGEFGHMRLPVDALTLLGWDAPLRRCGCGQKGCIENYLSGRGFEWLYQHYYGEPLQAPE
IIALYYQGDEQAVAHVERYLDLLAICLGNILTIVDPHLVVLGGGLSNFDAIYEQLPKRLPRHLLPVARVP
RIEKARHGDAGGVRGAAFLHLTD
>gnl|CDD|106271 PRK13311, PRK13311, N-acetyl-D-glucosamine kinase; Provisional
MYYGFDMGGTKIELGVFDENLQRIWHKRVPTPREDYPQLLQILRDLTEEADTYCGVQGSVGIGIPGLPNA
DDGTVFTANVPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIV
NGSIVSGRNHITGEFGHFRLPVDALDILGADIPRVPCGCGHRGCIENYISGRGFEWMYSHFYQHTLPATD
IIAHYAAGEPKAVAHVERFMDVLAVCLGNLLTMLGSPFGRGGWGVV
>gnl|CDD|139480 PRK13312, PRK13312, staphylobilin-forming heme oxygenase IsdG
MKFMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKS
DVFKAAHKHVRSKNEDESSPIINNKVITYDIGYSYMK
>gnl|CDD|183968 PRK13313, PRK13313, staphylobilin-forming heme oxygenase IsdI
MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSD
VFKEAHKNVRLKSDDDGQQSPILSNKVFKYDIGYHYQK
>gnl|CDD|183969 PRK13314, PRK13314, heme oxygenase
MIIVTNTAKITKGNGHKLIDRFNKVGKVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSP
AFKAAHSHQGGMPDYILDNKISYYDVKVVRMPMAAAQ
>gnl|CDD|237345 PRK13315, PRK13315, heme oxygenase
MIVVTNRITVKKGFAAKMAPRFTKGGPLEELEGFHKVEVWLIDNDDEYDEMYVNMWWETEEDFEAWRNSD
AFKEAHKRPSKTESDDSPIIGSEIVKSEVLSSLERLS
>gnl|CDD|183970 PRK13316, PRK13316, heme oxygenase IsdG
MIIVTNTIKVEKGAAEHVIRQFTGANGDGHPTKDIAEVEGFLGFELWHSKPEDKDYEEVVVTSKWESEEA
QRNWVKSDSFKKAHGRTKDTREQREDRKGIVGNAIARFEVVHVQNPVIVEK
>gnl|CDD|237346 PRK13317, PRK13317, pantothenate kinase; Provisional
MEMKIGIDAGGTLTKIVYLEEKKQRTFKTEYSAEGKKVIDWLINLQDIEKICLTGGKAGYLQQLLNYGYP
IAEFVEFEATGLGVRYLLKEEGHDLNDYIFTNIGTGTSIHYVDGNSQRRVGGTGIGGGTIQGLSKLLTNI
SDYEQLIELAKHGDRNNIDLKVGDIYKGPLPPIPGDLTASNFGKVLHHLDSEFTSSDILAGVIGLVGEVI
TTLSIQAAREKNIENIVYIGSTLTNNPLLQEIIESYTKLRNCTPIFLENGGYSGAIGALLLATNKKS
>gnl|CDD|237347 PRK13318, PRK13318, type III pantothenate kinase
MLLAIDVGNTNTVFGLYEGGKLVAHWRISTDSRRTADEYGVWLKQLLGLSGLDPEDITGIIISSVVPSVM
HSLERMCRKYFNIEPLVVVGPGVKTGINIKVDNPKEVGADRIVNAVAAYELYGGPLIVVDFGTATTFDVV
SAKGEYLGGVIAPGINISADALFQRAAKLPRVEITKPDSVIGKNTVEAMQSGIYYGYVGLVEGIVKRIKE
ELGKDPKVIATGGLAPLFAEESDTIDIVDPDLTLKGLRLIYERNKELQ
>gnl|CDD|237348 PRK13320, PRK13320, type III pantothenate kinase
VSMNLVIDIGNTTTKLAVFEGDELLEVFVVSTEGVEESLEKLLAKYPAIRDAIVSSVVPLAEEAFSALLK
LLFAVLELDSETPLPFRNDYDTPETLGADRLALCAGARYLFPGKNVLAIDAGTAITYDVLDSEGVYLGGL
ISPGLEMRFKALHEFTARLPLVTIEGPIPLIGRSTEECIRSGVVWGCVAEIEGLIEAYKSKLPELLVILT
GGDAPFLASRLKNTIFADEHAVLKGLNRILEYNK
>gnl|CDD|237349 PRK13321, PRK13321, type III pantothenate kinase
MLLLIDVGNTNIKLGVFDGDRLLRSFRLPTDKSRTSDELGILLLSLFRHAGLDPEDIRAVVISSVVPPLN
YSLESACKRYFGIKPLFVGPGIKTGLKIRYDNPREVGADRIVNAVAARRLYPDRNLIVVDFGTATTFDCV
SGKGEYLGGAICPGILISMEALSQKTAKLPRVEIAKPPSAIGKSTVSSIQSGLYYGYAGLVEGIVARIKA
ELGGPPRVIATGGFASLIAKESRCFDHVDPDLLLEGLRILYQMNRA
>gnl|CDD|237350 PRK13322, PRK13322, pantothenate kinase; Reviewed
MILELDCGNSRLKWRVIDNGGQIIEHGAHLDSPAELLLGLANLASLAPTRCRIVSVLSEEETARLVAILE
KRLGIPVVFAKVAAELAGVRNGYEDPEQLGIDRWLALLGAFHLAKNACLVIDCGTAVTIDLVDADGQHLG
GYICPGLYLMRDALRTHTRRIRYDDGTADSLSPGRNTVDAVERGCLLMLRGFIESQLEQARELWGPDFEI
FLTGGDAPLLADHLPQARVVPDLVFVGLAQYCPLSP
>gnl|CDD|106284 PRK13324, PRK13324, type III pantothenate kinase
MLLVMDMGNSHIHIGVFDGDRIVSQIRYATSSVDSTSDQMGVFLRQALRENSVDLGKIDGCGISSVVPHL
NYSLGSAVIKYFNIKPFFISMDTTDLDMSAVEAHQVGADRIASCISAIADHPNKDLLIIDLGTATTFDLV
TKDKKYLSGSIMPGVKLSLNALCQGASQLSSVTIVKPEVAIGYDTKTNIRSGLYYGHLGALKELKRRSVE
EFGSPVYTIATGGFAGLFKEEDIFNEISPDLILRGIRIAFLENNKKGV
>gnl|CDD|183976 PRK13325, PRK13325, bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase
MTVLKPSHWRVLAELADGLPQHVSQLARMADMKPQQLNGFWQQMPAHIRGLLRQHDGYWRLVRPLAVFDA
EGLRELGERSGFQTALKHECASSNDEILELARIAPDKAHKTICVTHLQSKGRGRQGRKWSHRLGECLMFS
FGWVFDRPQYELGSLSPVAAVACRRALSRLGLKTQIKWPNDLVVGRDKLGGILIETVRTGGKTVAVVGIG
INFVLPKEVENAASVQSLFQTASRRGNADAAVLLETLLAELDAVLLQYARDGFAPFVAEYQAANRDHGKA
VLLLRDGETVFEGTVKGVDGQGVLHLETAEGKQTVVSGEISLRSDDRPVSVPKRRDSERFLLLDGGNSRL
KWAWVENGTFATVGSAPYRDLSPLGAEWAEKADGNVRIVGCAVCGEFKKAQVQEQLARKIEWLPSSAQAL
GIRNHYRHPEEHGSDRWFNALGSRRFSRNACVVVSCGTAVTVDALTDDGHYLGGTIMPGFHLMKESLAVR
TANLNRHAGKRYPFPTTTGNAVASGMMDAVCGSVMMMHGRLKEKTGAGKPVDVIITGGGAAKVAEALPPA
FLAENTVRVADNLVIHGLLNLIAAEGGESEHT
>gnl|CDD|237351 PRK13326, PRK13326, type III pantothenate kinase
SKKVLSSQLIIDIGNTSISFALYKDNKMQIFCKLKTKLDLSFDELYSFLKEKFDFKVNQVFVSSVVPVID
KVLINVIFSLYKVKPLFIGFDLNYDLSFNPYNSNKFLLGSDVFANLVGAIEYYNINDALVVDLGTACTIF
AVSRQDGILGGLINGGPFTNLNALLDNAYLLKDFNLSVPKNLLGLSTSDSVNSGVIYQYKYLIEGVYHDL
KRNYDREFNLIITGGNSNLILPLISVDFIFNLYLTLEGIRILGNAFKFKFVN
>gnl|CDD|183977 PRK13327, PRK13327, type III pantothenate kinase
MSDWLFDLGNSRFKYAPLHGGRAGDVQAWAHGAEAMDAAALAALPSGRVAYVASVAAPALTQRVLACLQE
RFEQVRVVRTAAACAGVRIAYADPSRFGVDRFLALLGARGDAPVLVVGVGTALTIDLLGADGLHHGGRIA
ASPTTMREALHARAVQLPASGGDYVEFANDTDDALTSGCDGAAVALIERSLQHAHRSLGQPVRLLVHGGG
APPLLPLLPDAEFRPALVLDGLATWATAAAAP
>gnl|CDD|237352 PRK13328, PRK13328, type III pantothenate kinase
AMILLIDAGNSRIKWAWADAGRPWVHSGAFAHGLDAALAPDWSALPAPRGAWISNVAGPAVAARLDALLA
ARWPGLPVTWVRSRAAQCGVRNGYREPAQLGSDRWAGLIGARAAFPGEHLLIATFGTATTLDALRADGRF
AGGLILPGLALMMRALARHTAQLPTLDVDAASAAAGAVAPFADDTPDAISAGCLAAQAGLIERAWRDLAA
RWQAPVRLVLSGGAADAVAPALTVPHTRHDNLVLLGLALIAAAAA
>gnl|CDD|183979 PRK13329, PRK13329, pantothenate kinase; Reviewed
MTFLAIDVGNTRLKWGLYDAAQPGAALLAHGAEFLAEIDRLAEGAWAGLPAPARVLGCNVAGDAVARRVA
EQLELWDVAPRWVVASAAECGVRNGYDHPARLGADRWVALIGARHGPARPCLVVMVGTAVTVDALDADGE
FLGGLILPGHGLMLRALESGTAGLHVPTGEVREFPTNTSDALTSGGTQAIAGAVERMFRHLAQHCGAEPE
CLLTGGAAWKLAPSLTVPFELVDNLVLDGLLVIAARRAA
>gnl|CDD|237353 PRK13331, PRK13331, pantothenate kinase; Reviewed
MMFHTSNEWLALMIGNSRLHWGYFSGETLVKTWDTPHLDESIIQLLLPGQTLLIVAPNPLVIASVVPQQT
ELWQTYPNVRLITLDDIPLNNLYPTLGIDRALALWGAGQTYGFPCLVIDAGTALTFTGVDSDRTLVGGAI
LPGLGLQLRSLADKTAALPQVELPPPLPPRWATNTQEAIQSGVIYTILAGLRDFIEDWLSLFPDGKIVLT
GGDGELLHNYLQDLDPELAQRLRVDPNLIFWGIAAIRQGDA
>gnl|CDD|183981 PRK13333, PRK13333, type III pantothenate kinase
MLLCDIGNTNAHFYQNGKIFSLSIEEFKRFKIDQEIYYISVNEELEKKLLKCYPNAINLEPYFELDTIYQ
GLGIDRIAACYAIEDGVVVDAGSAITVDIMSNGIHLGGFILPGIAAYKKAYKKISPRLKQPFNAQISLDA
LPQNTRDAISYGVIKSIILLIEKLAKNKKIYFTGGDGKFLSKFFPNAIYDERLVFRGMKKIIKENG
>gnl|CDD|139494 PRK13335, PRK13335, superantigen-like protein; Reviewed
MKMRTIAKTSLALGLLTTGAITVTTQSVKAEKIQSTKVDKVPTLKAERLAMINITAGANSATTQAANTRQ
ERTPKLEKAPNTNEEKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTESTTPKTKVTTPPSTNT
PQPMQSTKSDTPQSPTIKQAQTDMTPKYEDLRAYYTKPSFEFEKQFGFLLKPWTTVRFMNVIPNRFIYKI
ALVGKDEKKYKDGPYDNIDVFIVLEDNKYQLKKYSVGGITKTNSKKVDHKAELSITKKDNQGMISRDVSE
YMITKEEISLKELDFKLRKQLIEKHNLYGNMGSGTIVIKMKNGGKYTFELHKKLQEHRMADVIDGTNIDK
IEVNIK
>gnl|CDD|183982 PRK13337, PRK13337, putative lipid kinase; Reviewed
MKRARIIYNPTSGRELFKKNLPDVLQKLEQAGYETSAHATTGPGDATLAAERAVERKFDLVIAAGGDGTL
NEVVNGIAEKENRPKLGIIPVGTTNDFARALHVPRDIEKAADVIIEGHTVPVDIGKANNRYFINIAGGGR
LTELTYEVPSKLKTMLGQLAYYLKGIEMLPSLKATDVRIEYDGKLFQGEIMLFLLGLTNSVGGFEKLAPD
ASLDDGYFDLIIVKKANLAELIHIATLALRGEHIKHPKVIYTKANRIKVSSFDKMQLNLDGEYGGKLPAE
FENLYRHIEVFVPKDQENAELINN
>gnl|CDD|183983 PRK13339, PRK13339, malate:quinone oxidoreductase; Reviewed
MAKSESKDVVLVGAGILSTTFGVLLKELDPDWNIEVVERLDSPAIESSNEWNNAGTGHAALCELNYTVQQ
PDGSIDIEKAKEINEQFEISKQFWGHLVKSGTIGNPREFINPLPHISFVRGKNNVKFLKKRYEALKQHPM
FDNIEYTEDIEVMAKWMPLMMPGREANEIMAASKIDEGTDVNFGALTRKLAKHLESHPNAQVKYNHEVVD
LERLSDGGWEVTVKDRNTGEKREQVADYVFIGAGGGAIPLLQKSGIPESKHLGGFPISGQFLRCTNPEVV
KQHQAKVYSKEPVGTPPMTVPHLDTRYIDGKRSLLFGPYAGFGPKFLKHGSNLDLFKSVKPYNITTMLAV
AVKNMPLIKYSIDQVMQTKEGRMNHLRTFYPEARAEDWRLYTAGKRVQVIKDTPEHGKGFIQFGTEVVNS
QDHSVIALLGESPGASTSVSVALEVLERNFPEYAKEWAPKLKEMIPSYGKSLIEDAKLMRKIRKQTSKDL
ELGYYEN
>gnl|CDD|183984 PRK13340, PRK13340, alanine racemase; Reviewed
FRKLLLLPLITLLLCSQPASAAPLLLSDNSANAEQIQPRNAWLEISPGAFRHNIKTLRSLLANKSKVCAV
MKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLRVRSASPAEIEQALRYDLEELIGD
DEQAKLLAAIAKKNGKPIDIHLALNSGGMSRNGLDMSTARGKWEALRIATLPSLGIVGIMTHFPNEDEDE
VRWKLAQFKEQTAWLIGEAGLKREKITLHVANSYATLNVPEAHLDMVRPGGILYGDRHPANTEYKRIMTF
KSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAPVVGRVSMNTLM
VDVTDIPNVKPGDEVVLFGKQGNAEITVDEVEEASGTIFPELYTAWGRTNPRIYVP
>gnl|CDD|237354 PRK13341, PRK13341, AAA family ATPase
QDLFAFHGEQMSQSEAPLADRLRPRTLEEFVGQDHILGEGRLLRRAIKADRVGSLILYGPPGVGKTTLAR
IIANHTRAHFSSLNAVLAGVKDLRAEVDRAKERLERHGKRTILFIDEVHRFNKAQQDALLPWVENGTITL
IGATTENPYFEVNKALVSRSRLFRLKSLSDEDLHQLLKRALQDKERGYGDRKVDLEPEAEKHLVDVANGD
ARSLLNALELAVESTPPDEDGLIDITLAIAEESIQQRAVLYDKEGDAHFDTISAFIKSLRGSDPDAALYW
LARMVEAGEDPRFIFRRMLIAASEDVGLADPQALVVVEACAAAFERVGLPEGLYPLAQAALYLATAPKSN
SVLGFFDALKKVREEQVQDVPNHLRDANRDGKAFGDGVGYRYPHAFRDHWVAQQYLPEALQGEVFWQPSR
QGWEGERRERLARRRAAQLAAASEAEVEQPLLLSSGPDDPALERWLQRQLGQEGERLAILRDRLWSDITW
QRHDRVLNLANRSLLWALGPLRAVPEGGVTVLCSSQEDSDRLVAQLELLDPLERPVLLDGSLEALKTLPA
NLQFEWIGGRLPTGDAVVTKELWQQLTEKLTPAGKLKLLYSIPAVGPAWALLSEDELLYKALYSALLEAE
ELWLKLQWDQSLLQQSLEMPGWSTGIEQWPEELALGIDSKLIKRWLAQGPDYRQALATNLEEERICNLDE
ELTRILGEQLSQWLRHQLFIGRRSK
>gnl|CDD|237355 PRK13342, PRK13342, recombination factor protein RarA; Reviewed
PLAERMRPKTLDEVVGQEHLLGPGKPLRRMIEAGRLSSMILWGPPGTGKTTLARIIAGATDAPFEALSAV
TSGVKDLREVIEEARQRRSAGRRTILFIDEIHRFNKAQQDALLPHVEDGTITLIGATTENPSFEVNPALL
SRAQVFELKPLSEEDIEQLLKRALEDKERGLVELDDEALDALARLANGDARRALNLLELAALGVDSITLE
LLEEALQKRAARYDKDGDEHYDLISALHKSIRGSDPDAALYYLARMLEAGEDPLFIARRLVIIASEDIGL
ADPNALQVAVAAADAVERIGMPEGRIALAQAVIYLALAPKSNAAYTAINAALADVREGGSLPVPLHLRNA
PTKLMKELGYGKGYKYPHDYPNGYVGQQYLPDELKGKRYYEPTERGFEKKIKERLEKLKDKNR
>gnl|CDD|183987 PRK13343, PRK13343, F0F1 ATP synthase subunit alpha; Provisional
MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEEL
VGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERD
FVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIE
TLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRP
PGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFA
AGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAGTQKQITRGRRLRELL
KQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRELDEAWLAALE
EILREAGERFAA
>gnl|CDD|183988 PRK13344, spxA, transcriptional regulator Spx; Reviewed
MIKIYTISSCTSCKKAKTWLNAHQLSYKEQNLGKEPLTKEEILAILTKTENGIESIVSSKNRYAKALDCD
IEELSVNEVIDLIQENPRILKSPILIDDKRLQVGYKEDDIRAFLPRSIRNVENAEARLRAAL
>gnl|CDD|106303 PRK13345, PRK13345, superantigen-like protein; Reviewed
MKLTALAKATLALGILTTGVFTAESKAVHAKVELDETQRKYYINMLHQYYSEESFEPTNISVKSEDYYGS
NVLNFKQRNKAFKVFLLGDDKNKYKEKTHGLDVFAVPELIDIKGGIYSVGGITKKNVRSVFGFVSNPSLQ
VKKVDAKHGFSINELFFIQKEEVSLKELDFKIRKMLVEKYRLYKGASDKGRIVINMKDEKKYVIDLSEKL
SFDRMFDVMDSKQIKNIEVNLN
>gnl|CDD|106304 PRK13346, PRK13346, superantigen-like protein 7; Reviewed
MKLKTLAKATLALGLLTTGVITSEGQAVQAKEKQERVQHLYDIKDLHRYYSSESFEFSNISGKVENYNGS
NVVRFNQENQNHQLFLLGKDKDKYKEGLEGQNVFVVKELIDPNGRLSTVGGVTKKNNKSSETNTHLFVNK
VYGGNLDASIDSFLINKEEVSLKELDFKIRQQLVENYGLYKGTTKYGKITINLKDEKKEEIDLGDKLQFE
RMGDVLNSKDIQNIAVTINQI
>gnl|CDD|237356 PRK13347, PRK13347, coproporphyrinogen III oxidase; Provisional
ADVMHDEALLRYFDAAVPRYTSYPTAPEFSPAFGEDTYREWLRQIGPEEPVSLYLHVPFCRSLCWFCGCN
TIITQRDAPVEAYVAALIREIRLVAASLPQRRRVSQLHWGGGTPTILNPDQFERLMAALRDAFDFAPEAE
IAVEIDPRTVTAEMLQALAALGFNRASFGVQDFDPQVQKAINRIQPEEMVARAVELLRAAGFESINFDLI
YGLPHQTVESFRETLDKVIALSPDRIAVFGYAHVPSRRKNQRLIDEAALPDAEERLRQARAVADRLLAAG
YVPIGLDHFALPDDELAIAQREGRLHRNFQGYTTDRCETLIGFGASAISRFPGGYVQNISSLKAYYRAID
AGRLPIERGYALSDDDRLRRAIIETLMCNFPVDLAAIAARHGFFARYFLDELARLEPLAADGLVTIDGGG
IRVTPEGRPLIRAVAAAFDAYLGRSAAGFSKAI
>gnl|CDD|237357 PRK13348, PRK13348, HTH-type transcriptional regulator ArgP
MLDYKQLEALAAVVETGSFERAARRLHVTPSAVSQRIKALEESLGQPLLVRGRPCRPTPAGQRLLRHLRQ
VALLEADLLSTLPAERGSPPTLAIAVNADSLATWFLPALAAVLAGERILLELIVDDQDHTFALLERGEVV
GCVSTQPKPMRGCLAEPLGTMRYRCVASPAFAARYFAQGLTRHSALKAPAVAFNRKDTLQDSFLEQLFGL
PVGAYPRHYVPSTHAHLAAIRHGLGYGMVPELLIGPLLAAGRLVDLAPGHPVDVALYWHHWEVESPTMEA
LSQRVVEAARRLLA
>gnl|CDD|106307 PRK13349, PRK13349, superantigen-like protein; Reviewed
MNNNITKKIILSTTLLLLGTASTQFPNTPINSSSEAKAYYINQNETNVNELTKYYSQKYLTFSNSTLWQK
DNGTIHATLLQFSWYSHIQVYGPESWGNINQLRNKSVDIFGIKDQETIDSFALSQETFTGGVTPAATSND
KHYKLNVTYKDKAETFTGGFPVYEGNKPVLTLKELDFRIRQTLIKSKKLYNNSYNKGQIKITGADNNYTI
DLSKRLPSTDANRYVKKPQNAKIEVILEKSN
>gnl|CDD|171995 PRK13350, PRK13350, superantigen-like protein; Reviewed
MSKNITKNIILTTTLLLLGTVLPQNQKPVFSFYSEAKAYSIGQDETNINELIKYYTQPHFSFSNKWLYQY
DNGNIYVELKRYSWSAHISLWGAESWGNINQLKDRYVDVFGLKDKDTDQLWWSYRETFTGGVTPAAKPSD
KTYNLFVQYKDKLQTIIGAHKIYQGNKPVLTLKEIDFRAREALIKNKILYNENRNKGKLKITGGGNNYTI
DLSKRLHSDLANVYVKNPNKITVDVLFD
>gnl|CDD|237358 PRK13351, PRK13351, elongation factor G-like protein
AEMPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDGTTVTDWMPQEQERGITIESAATSCDW
DNHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGA
DLFKVLEDIEERFGKRPLPLQLPIGSEDGFEGVVDLITEPELHFSEGDGGSTVEEGPIPEELLEEVEEAR
EKLIEALAEFDDELLELYLEGEELSAEQLRAPLREGTRSGHLVPVLFGSALKNIGIEPLLDAVVDYLPSP
LEVPPPRGSKDNGKPVKVDPDPEKPLLALVFKVQYDPYAGKLTYLRVYSGTLRAGSQLYNGTGGKREKVG
RLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSADPVLLELLTFPEPVVSLAVEPERRGDEQKL
AEALEKLVWEDPSLRVEEDEETGQTILSGMGELHLEVALERLRREFKLEVNTGKPQVAYRETIRKMAEGV
YRHKKQFGGKGQFGEVHLRVEPLERGAGFIFVSKVVGGAIPEELIPAVEKGIREALASGPLAGYPVTDLR
VTVLDGKYHPVDSSESAFKAAARKAFLEAFRKANPVLLEPIMELEITVPTEHVGDVLGDLSQRRGRIEGT
EPRGDGEVLVKAEAPLAELFGYATRLRSMTKGRGSFTMEFSHFDPVPPAVQKKVGSK
>gnl|CDD|237359 PRK13352, PRK13352, phosphomethylpyrimidine synthase ThiC
MTQMEAARKGIITEEMEYVAKKEGVDPEFIREGVAEGRIVIPANINHKNLKPVGIGKGLRTKVNANIGTS
SDISDIEEELEKAKVAVKYGADTIMDLSTGGDLDEIRRAIIEASPVPVGTVPIYQAAVEAARKYGSVVDM
TEDDLFDVIEKQAKDGVDFMTIHCGVTRETLERLKKSGRIMGIVSRGGSFLAAWMLHNNKENPLYEHFDY
LLEILKEYDVTLSLGDGLRPGCIADATDRAQIQELITLGELVKRAREAGVQVMVEGPGHVPLDQIEANVK
LQKRLCHGAPFYVLGPLVTDIAPGYDHITSAIGGAIAAAAGADFLCYVTPAEHLGLPNVEDVREGVIASK
IAAHAADIAKGRPGARERDDEMSKARKNLDWEKQFELALDPEKAREYRDERLKDEEACSMCGKFCAMKIV
NEALEGEKSNC
>gnl|CDD|183992 PRK13353, PRK13353, aspartate ammonia-lyase; Provisional
TNKNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRI
AEAIVQACDEILAGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQS
TNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKR
DRKRIQQAREHLYEVNLGGTAVGTGLNADPEYIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGA
LKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMPGKVNPVMPEVVNQIAFQVIGNDVTITLA
AEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYVEKSVGIATALNPHIGYEA
AARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPGIAGATLLKKN
>gnl|CDD|237360 PRK13354, PRK13354, tyrosyl-tRNA synthetase; Provisional
MKMNILEQLKWRGAINQETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVI
LIGGFTGKIGDPSGKSKERKLLTDEQVQHNAKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLRDYGK
HFTVNRMLERDDVKSRLEREQGISFTEFFYPLLQAYDFVHLNRKEDVDLQIGGTDQWGNILMGRDLQRKL
EGEEQFGLTMPLLEGADGTKMGKSAGGAIWLDPEKTSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDE
LEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPLKDIPTFEVSAETKNLVDLLV
DLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPEDAFDGKFVILRRGKKKFFLVKLK
>gnl|CDD|237361 PRK13355, PRK13355, bifunctional HTH-domain containing protein/aminotransferase; Provisional
KTTFAERLKQAMKARGLKQEDLVHAAEARGVKLGKSHISQYVSGKTGPRRDVLPFLAAILGVSEDWLLGG
ESPADQESDASAVVESAPNSHLADPSAPTTPISQTSSEISIGNRRTFKKSHKLDNVLYDVRGPVVDEANR
MEAAGTHILKLNIGNPAPFGFRTPDEVVYDMAQQLTDTEGYSDSKGLFSARKAIMQYAQLKGLPNVDVDD
IYTGNGVSELINLSMSALLDDGDEVLIPSPDYPLWTACVNLAGGTAVHYRCDEQSEWYPDIDDIRSKITS
RTKAIVIINPNNPTGALYPREVLQQIVDIAREHQLIIFSDEIYDRLVMDGLEHTSIASLAPDLFCVTFSG
LSKSHMIAGYRIGWMILSGNKRIAKDYIEGLNMLANMRLCSNVPAQSIVQTALGGHQSVKDYLVPGGRVY
EQRELVYNALNAIPGISAVKPKAAFYIFPKIDVKKFNIHDDEQFALDLLHDKKVLIVQGTGFNWDKPDHF
RVVYLPRLEDLEDAMDRLADFFSYYRQ
>gnl|CDD|237362 PRK13356, PRK13356, branched-chain amino acid aminotransferase
MAPGSNTWTFFDGEWHEGNVPIMGPADHAAWLGSTVFDGARAFEGVTPDLDLHCARVNRSAEALGLKPTV
SAEEIEALAREGLKRFDPDTALYIRPMYWAEDGFASGVAPDPESTRFALCLEEAPMPEPTGFSLTLSPFR
RPTLEMAPTDAKAGCLYPNNARALREARSRGFDNALVLDMLGNVAETATSNVFMVKDGVVFTPVPNGTFL
NGITRQRVIALLREDGVTVVETTLTYEDFLEADEVFSTGNYSKVVPVTRFDDRSLQPGPVTRRARELYWD
WAHGGR
>gnl|CDD|237363 PRK13357, PRK13357, branched-chain amino acid aminotransferase; Provisional
FTVTLKPNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDGKWHDARLVPYGPLELDPAATVLHYGQEIFE
GLKAYRHKDGSIVLFRPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVPPYGEGASLYLRPF
MIATEPFLGVKPAEEYIFCVIASPVGAYFKGGVKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAE
AKEKGCDQVLYLDAVEHTYIEEVGGMNFFFITKDGTVTPPLSGSILPGITRDSLLQLAEDLGLTVEERPV
SIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEFVIGDGEVGPVTQKLYDELTGIQFGDVEDPHG
WIVKVD
>gnl|CDD|183997 PRK13358, PRK13358, protocatechuate 4,5-dioxygenase subunit beta; Provisional
MGKIVGAFATSHVLMSSKGGEEQAKRVVEGMREIGRRLRELRPDVLVVIGSDHLFNFNTGCQPPFLVGTG
DSDTPYGDMDIPRELVPGHRAFAQAIALHRAADGFDLAQAEELRPDHGVMIPLLFMDPGRRIPVVPVYVN
INTDPFPSAKRCAALGEVIRQAVEKDRPADERVAVIGTGGLSHWLGVPEHGEVNEDFDRMVMDALVSGDL
EALVALGNEEILEQGGNGGLEIRNWIMAAAAVPGRRGEKIYYEAMPQWVTGMGGVQFHV
>gnl|CDD|183999 PRK13360, PRK13360, omega amino acid--pyruvate transaminase; Provisional
MTENVSQTPNDLSAFWMPFTANRQFKKAPRLLVAAKGMYYTTHDGRRVLDGTAGLWCVNAGHGRPEIVEA
VRAQAGELDYAPAFQMGHPKAFELANRIAEIAPGGLNHVFFTNSGSESVDTALKIALAYHRARGEGSRTR
LIGRERGYHGVGFGGISVGGIVPNRKAFGALLPGVDHLPHTLDLARNAFSKGQPEHGAELADELERLVTL
HDASTIAAVIVEPVAGSTGVLIPPKGYLQRLREICDKHGILLIFDEVITGFGRLGAPFAAQYFGVTPDLL
TCAKGLTNGAIPMGAVFVSSEIHDAFMQGPEAGIEFFHGYTYSGHPLACAAALATLDLYEREGLLTRAAR
LAPYWEDALHSLRDAPHVIDIRNLGLVGAVELAPRDGKPGKRAYEVFLKCFEKGLMIRYTGDILALSPPL
IIEEAQIDELFDILAQALKETI
>gnl|CDD|184002 PRK13363, PRK13363, protocatechuate 4,5-dioxygenase subunit beta; Provisional
MAEIVLGMGTSHGPMLVTPPEDWLHRLPRDRNRKYHHYRGRPWTYDALVAERAPENLEEQITPEERTERH
AACEAAIERMRDAIEAARIDVAVIVGNDQMELFTTDNNPAFAIYYGETIRNNPASREKLPSLPPGVKAAM
PGYMPDAETTYPVVPELARHMIRRLVDDGFDITALDRLPDGEGEGHAFGFVHRQLMKDNVLPTVPVLVNT
FYPPNQPTPRRCIALGRSLRRAIRSWPEDARVAVIASGGLSHFVIDEELDRLIIDAIRAKDFAALASLDE
AILQSGTSEIKNWIAVAGALDDAGLDMTWVDYVPCYRTEAGTGTGMGFAAWRTDD
>gnl|CDD|184003 PRK13364, PRK13364, protocatechuate 4,5-dioxygenase subunit beta; Provisional
MAKIIGGITTSHVPAIGGAIAKGLQQDPYWKPFFDGFPPVREWLEKVKPDVAVVFYNDHGLNFFLDKMPT
FAVGAAPEYSNADEGWGIPTLAPFKGDTELSWHIIESLVEEEFDITTCQEMLVDHAFTLPLELFWPGRDY
PVKVVPVCINTVQHPLPSARRCYKLGQAIGRAIASWPSDERVVVIGTGGLSHQLDGERAGFINKDFDLQC
MDSLVSDPEWLTQYSNHELVELAGTQGVELLNWLAMRGALGGKVREVHRNYHIPISNTAAGLMLLETV
>gnl|CDD|184004 PRK13365, PRK13365, protocatechuate 4,5-dioxygenase subunit beta; Provisional
MASIIGGIGTSHVPTIGVAYDKGKQQDPAWKPLFDGYEPVAAWLAEQKADVLVFFYNDHCTTFFFDLYPT
FALGVGERFPVADEGAGLRPLPPIRGDVQLQAHIAECLVNDEFDLTVFQDKPIDHGCAAPLPLLWPHVPD
WPGTVVPIAINVLQYPLPTARRCYRLGQALRRAIESYPEDLRVVVVGTGGLSHQIHGERSGFNNTEWDME
FLDRFQHAPETLTDLTHTDYVRLGGAESVEQIMWLAMRGALGGPIRKLHQNYYLMTTTAMTVVLYEPGE
>gnl|CDD|184005 PRK13366, PRK13366, protocatechuate 4,5-dioxygenase subunit beta; Provisional
MARITASVYTSHVPAIGAAIDLGKTGEPYWQPVFKGYEFSKQWEKEEKPDVIFLVYNDHATAFSLDIIPT
FAIGTAAEYQPADEGWGPRPVPKVIGHPDLAAHIAQSVIQDDFDLTIVNKMDVDHGLTVPLSLMCGQPDA
WPCPVIPFAVNVVQYPVPSGRRCFALGQAIRRAVESYDEDLNVQIWGTGGMSHQLQGPRAGLINREWDNA
FLDRLIADPDGLSKMPHIDYVREAGSEGIELVMWLIARGAMSDVAGGPKPKVAHRFYHVPASNTAVGHLI
LENA
>gnl|CDD|184006 PRK13367, PRK13367, gallate dioxygenase
MARIIGGIAVSHTPTIGFAVDHNKQQDPAWAPIFESFAPLRRWLEEKKPDVLLYIFNDHVTSFFFDHYSA
FALGIDEQYAVADEGGGPRDLPPVRGHAALSRHIGASLMADEFDMSFFQDKPLDHGLFSPLSALLPHDDG
WPVQVVPLQVGVLQFPIPSARRCYKLGQALRRAIESYPEDLKVAIVATGGLSHQVHGERCGFNNPEWDAQ
FLDLLVNDPERLTEMTLAEYATLGGMEGAEVIMWLIMRGALSANVECLHRDYYLPSMTGIATLILENQAR
APPVDVVERHRQHIAHQLAGVEKLPGTYPFTLERSLKAYRINRFLHRLIEPAWRERFLADPEALYDEAGL
SEEERDLIRRRDWRGLIHYGVSFFLLEKLGAVVGVSNLHIYAAMRGQTLEAFQKTRNQQVLYSVAGKAAA
>gnl|CDD|184007 PRK13368, PRK13368, 3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
MKVVVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGGKVVMTS
DDHLSGTDRLAEVMLKIEADIYINVQGDEPMIRPRDIDTLIQPMLDDPSINVATLCAPISTEEEFESPNV
VKVVVDKNGDALYFSRSPIPSRRDGESARYLKHVGIYAFRRDVLQQFSQLPETPLEQIESLEQLRALEHG
EKIRMVEVAATSIGVDTPEDLERVRAIM
>gnl|CDD|237365 PRK13369, PRK13369, glycerol-3-phosphate dehydrogenase; Provisional
MAEPETYDLFVIGGGINGAGIARDAAGRGLKVLLCEKDDLAQGTSSRSGKLVHGGLRYLEYYEFRLVREA
LIEREVLLAAAPHIIWPMRFVLPHSPEDRPAWLVRLGLFLYDHLGGRKRLPGTRTLDLRRDPEGAPLKPE
YTKGFEYSDCWVDDARLVVLNALDAAERGATILTRTRCVSARREGGLWRVETRDADGETRTVRARALVNA
AGPWVTDVIHRVAGSNSSRNVRLVKGSHIVVPKFWDGAQAYLFQNPDKRVIFANPYEGDFTLIGTTDIAY
EGDPEDVAADEEEIDYLLDAANRYFKEKLRREDVVHSFSGVRPLFDDGAGNPSAVTRDYVFDLDAETGGA
PLLSVFGGKITTFRKLAEHALERLKPFFPQMGGDWTAGAPLPGGDIANADFDTFADDLRDRYPWLPRPLA
HRYARLYGTRAKDVLGGARSLEDLGRHFGGGLTEAEVRYLVAREWARTAEDILWRRTKLGLHLSAAERAA
LAAWFANANAAA
>gnl|CDD|237366 PRK13370, mhpB, 3-carboxyethylcatechol 2,3-dioxygenase
MTAALVCLSHSPLVGYVDPAQEVLAEVNAVIAAAREFVAAFDPELVVLFAPDHYNGFFYDVMPPFCIGVS
ATAVGDYGTAAGPLPVPSDLAEALAEAVLDSGIDVAVSYRMQVDHGFAQPLEFLLGGLDAYPVIPVFINS
VAAPLPPFRRVRLLGEAVGRFLATLDKRVLFLGSGGLSHDPPVPELATADPEVRERLIAGRNPTPEERAA
RQQRVIAAARIFAAGQSALHPLNPEWDRAFLDLLESGDLAALDAWTNEEITREAGKSAHEIRTWVAAFAA
LSAFGPYRAEGRYYRPIPEWIAGFAVLSARPEN
>gnl|CDD|237367 PRK13371, PRK13371, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Provisional
RKGFGHAEEVAGALETAYQSSLIQSIRENGYVLQFGDVTIKLARAFGFCWGVERAVAMAYETRRHFPDER
IWITNEIIHNPSVNQHLREMGVRFIPVEKGVKDFSVVTPGDVVILPAFGATVQEMQLLNEKGCHIVDTTC
PWVSKVWNTVEKHKKKDFTSIIHGKYKHEETRATSSFAGTYLVVLDLEEAQYVADYILGGGDREEFLERF
AKAYSPGFDPDRDLERVGVANQTTMLKSETEEIGKLFERTMLRKYGPANLNEHFLSFNTICDATQERQDA
MFSLVEEPLDLMVVIGGYNSSNTTHLQEIAIERGIPSYHIDSPERILSGNSIEHKPLGKELVVTENWLPE
GPVTVGITSGASTPDKVVEDVIEKIFALKEDARPVEE
>gnl|CDD|106330 PRK13372, pcmA, protocatechuate 4,5-dioxygenase subunit alpha/beta
MSLDKPYKDVPGTIIFDADQARKGYNLNQFCMSLMKADNRARFKADEGAYLDEWALNEAQKQAVLAIDLN
QCIAEGGNIYFLAKIGATDGKSFQQMAGSMTGLSEAAYRDMMIGGGRPAEGLRLKDEDGATPPEPAEKAE
PTGAQDAKAQISAALFSSHVPAIGAAIDLGKTEEDYWKKLFAGYDLSREWAKEHLPDVIILVYNDHATAF
DLEIIPTFAIGTAAEFPPADEGWGPRPVPDVIGHPELAAHIAQSVIQDDFDLTIVNEMDVDHGLTVPLSL
MCGDPEAWPCPVIPFAVNVVQYPVPSGRRCYELGQAIRRAIDKWDADPLNVQIWGTGGMSHQLQGPRAGL
INEEFDNAFLDHLIADPEAAAEIPHIDYVDEAGSEGIELVDWLIARGAMDDQAGGASPDAAADGATGRPP
KVNHRFYHVPASNTAVGHLILENP
>gnl|CDD|106331 PRK13373, PRK13373, putative dioxygenase; Provisional
MAKIVAGIGMSHAPGALGWPDAPSASVRRRLLQAADRLGRSLDAARPDVIIAFLDDHFENHFRSLMPTVG
IGVADSHPGPATQWLEALRLTRQERFGGAPEIAERLLRSLVADGYDVARMGEIEYGNNLMVPWKLMAPRS
APAIIPVFTNVFSPPVMPYRRAYAFGAALRNAAEALDADLRVAFMATGGMSHWPPFWNDSSPEADAFLAR
MKAFQTHGKSVLEKDPHLLRDLAAYEIEMAERNQWPLNSPHPLVNEAWDRQMLDALARGDVEFLCGLQYE
DVKRDGGHGGQEIINWIELMGAMKGAPATLLEYEAVTEWICGMAYMDYGVAQAWPVNPLIKEQE
>gnl|CDD|237368 PRK13374, PRK13374, DeoD-type purine-nucleoside phosphorylase
MSTPHINAQPGDFAETVLMPGDPLRAKYIAETYLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSM
VIYVHELIATFGVKNIIRVGSCGATQDDVKLMDVIIAQGASTDSKTNRIRFSGHDFAAIADYQLLEKAVE
TAREKGVPVKVGNVFSSDLFYDPDEDAIEAMERFGILGVDMEVAGLYGLAAYLGAEALAILTVSDHIITG
EETTAEERQLSFNDMIEVALETA
>gnl|CDD|172015 PRK13375, pimE, mannosyltransferase; Provisional
AAAASARRVTRPPARLTRAAPLLLVLSVAARLAWTYLAPNGANFVDLHVYVGGAAALDHPGTLYDYVYAD
QTPDFPLPFTYPPFAALVFYPLHLLPFGVVAFLWQLATIAALYGVVRISQRLLGGGAGGHRVAMLWTAVG
IWLEPVRSTFDYGQINVFLMLAVLYAVYSSRWWLSGLLVGLAAGVKLTPAITGLYFLGARRWAAAAFSAV
VFLATVGVSYLVVGDQARYYFTDLLGDADRVGPIGTSFNQSWRGAISRILGHDAGFGPLVLAAIAVTAVL
ALLAWRALGRSDRLGSLLVVQLFGLLLSPISWTHHWVWVVPLMIWLLHGPWRERPGARVLGWGWLALTVI
GVPWLLSFAQPSIWEISRPWYLAWAGLVYVVATLATLAWIAVTGRRSRRPVPPPDRMAN
>gnl|CDD|237369 PRK13376, pyrB, bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase regulatory subunit; Provisional
MKRDFLGRTLAVIEDLSVEEQLFLYEKTRELKQRWYEGEDVSEFRIKKRDVGIYIVFVEPSTRTKESFIN
AAKFHKNVKVNIFDSEHSSFNKQESYTDTFNMLTGYSDYSIFIVRTRLEGVCRLLEEKVSEFASRNGIEV
PAFINAGDGKHEHPTQELLDEFTFLEQNNFDNSFIHIALVGDLLHGRTVHSKVNGLKIFKNVKVDLIAPE
ELAMPEHYVEKMKKNGFEVRIFSSIEEYLSQKDVAKIWYFTRLQLERMGEDILEKEHILRKAVTFRKEFL
DKLPEGVKFYHPLPRHKVYPTIPTFLDTLPLNGWETQAINGYWVRIVLLSMLGGALEADFDTSKKKEEPE
EDFIIPAPIVHGTKGVQKEGKRGIKPIENGTVIDHIAKGKTPEEIYETIVKIRKILKLYDVDSADGIFRS
ADGNFKGYISLPDRYLSKKEIKKLSAISPNTTVNIIKNSRVVEKYRIKLPPRIYGFEELRCKNENCITNP
AHGENVSASFVRNEKGRFVCEYCETPHTFEEIWSI
>gnl|CDD|184013 PRK13377, PRK13377, protocatechuate 4,5-dioxygenase subunit alpha; Provisional
MALDKPYLDIPGTTIFDADMSRKGYHLNQFCMSLMKAENRERFKADERAYLDEWPMTEEQKQAVLARDLN
RCIALGGNIYFLAKIGATDGKSFQQMAGSMTGMTEEEYRQMMLGGGRSPEGNRYIGEKG
>gnl|CDD|139527 PRK13378, PRK13378, protocatechuate 4,5-dioxygenase subunit alpha; Provisional
MAATSAKREIPGTTIFDGEQARKGYALNKMCFSFNDAANRAAFLADEAAYCRKYGLNEEQKEAIRNRDVL
QLLAAGGNAYYLAKFAGIFGLDMQDIGAQQTGMTKEEFKAKLLAAGR
>gnl|CDD|184014 PRK13379, PRK13379, protocatechuate 4,5-dioxygenase subunit alpha; Provisional
MNPQVQGMEQLGGTYVFDLRTSNRALRLNRFFWHMIRAPWRDRFLQDAEALMQEAGLTEQEKELIRARDW
LGLVQYGANFFVIEKFARVVRMTNLQVYAIMRGETFEEFMQTRRVPDAR
>gnl|CDD|237370 PRK13380, PRK13380, glycine cleavage system protein H; Provisional
MVVENGCEIPSELRYTIKNHEWLRLEGDGTVTVGITDYAQTMAGDVVFVRLKELGKKVEKGKPVATLESG
KWAGPVPAPLTGEVVEVNEALEDSPELVNEDPYGEGWFFRFKPANPEELKQLLDGDAADRLLKENIDAEK
ITCK
>gnl|CDD|237371 PRK13381, PRK13381, peptidase T; Provisional
MQLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDIVIDEHAIVTAKLPGNTPGAPR
IGFIAHLDTVDVGLSPDIHPQILRFDGGDLCLNAEQGIWLRTAEHPELLNYQGEDIIFSDGTSVLGADNK
AAIAVVMTLLENLTENEVEHGDIVVAFVPDEEIGLRGAKALDLARFPVDFAYTIDCCELGEVVYENFNAA
SAEITITGVTAHPMSAKGVLVNPILMANDFISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRD
FDLDGFEARKQFIEEVVAKINAKYPTARVSLTLTDQYSNISNSIKDDRRAVDLAFDAMKELGIEPKVIPM
RGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEVTITICLLAAK
>gnl|CDD|172019 PRK13382, PRK13382, bile acid CoA ligase
AGIKDRLRDTLGLIATLRRAGLIAPMRPDRYLRIVAAMRREGMGPTSGFAIAAQRCPDRPGLIDELGTLT
WRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREG
VDTVIYDEEFSATVDRALADCPQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVILLTSGTTGT
PKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIVTRRRFDPEATLDLI
DRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAG
MIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGSTKDFHDGFMAS
GDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG
ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR
>gnl|CDD|139531 PRK13383, PRK13383, acyl-CoA synthetase; Provisional
VAPTAARALVRSGLLNPPSPRAVLRLLREASRGGTNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRAT
ESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADN
EFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGRIVLLTSGTTGKPKGVPRAPQLRSAVGVWVTILD
RTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILE
LPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPADLRDAPETVGKP
VAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDD
MIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFE
QPRDINIVSSIPRNPTGKVLRKELPG
>gnl|CDD|172020 PRK13384, PRK13384, porphobilinogen synthase
MSNTFPLRRLRRLRRSEAMRDLVRETEVSLSDLIYPIFIEEHITDAVPISTLPGISRLPESALADEIERL
YALGIRYVMPFGISHHKDAKGSDTWDDNGLLARMVRTIKAAVPEMMVIPDICFCEYTDHGHCGVLHNDEV
DNDATVENLVKQSVTAAKAGADMLAPSAMMDGQVKAIRQGLDAAGFEHVAILAHSAKFASSFYGPFRAAV
DCELSGDRKSYQLDYANGRQALLEALLDEAEGADILMVKPGTPYLDVLSRLRQETHLPLAAYQVGGEYAM
IKFAALAGALDERAVVTETLGGLKRAGADLIVSYYAKQYAQW
>gnl|CDD|184017 PRK13385, PRK13385, 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
MNYELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNV
ADQRVEVVKGGTERQESVAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVK
RVKDKQVIETVDRNELWQGQTPQAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKL
TTPEDMPLAKAILQGDIADD
>gnl|CDD|237372 PRK13386, fliH, flagellar assembly protein H; Provisional
MNIKNTWRLGAVKYRRHRFPPLRKVRQVAPSAATLDPADYQQQLMAGFQEGIQQGFDQGLEEGEEEGRQE
GHAAGFAQGRQKGRIEGRQSIRQQFNDAAKPLGALRQQLERYLAEYEQQQRDELLDLVEKVTRQVIRCEL
TLQPQQILALVEETLAALPDDPEQLKVHLNPEEFGRLKDLAPEKVQAWGLVADPSLSAGECRIVTDTSEA
DAGCEHRLDACMDAVKEHLLTEPEHE
>gnl|CDD|237373 PRK13387, PRK13387, 1,4-dihydroxy-2-naphthoate octaprenyltransferase; Provisional
MSAKLFLKLVEIHTKIASFFPVILGTLFSLYVAKIFDWLLFLAFMVAMLAFDIATTAINNYMDFKKALDT
ADYVGIGNGIGQHGLKPRNVLTVILLMYVVAAILGVYLCMNTSWLLLVIGLICFAIGILYTGGPLPLSRM
PLGEIFSGLTMGFGIFLLAVYINTNTITIESLLFQGEMFTIQGNLIAIIAIGVISLPIIFTIANIMLANN
LRDLDEDIKNHRYTLVYYIGREKGVVLFAILFYASYLAIAVIVLMGYISPWALLSFLTLRKPISNLQSFQ
KEAKDPKYFVIAIRNTVLTNTTFGFLLSASLLIQYLF
>gnl|CDD|237374 PRK13388, PRK13388, acyl-CoA synthetase; Provisional
MRDTIAQLLRDRAGDDTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLHVGVLLGNTPEMLFWLA
AAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGLDLPGVRVLDVDTPAYAELVAAAGA
LTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGW
APAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDI
AEFSRRFGCQVEDGYGSSEGAVIVVREPGTPPGSIGRGAPGVAIYNPETLTECAVARFDAHGALLNADEA
IGELVNTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIER
ILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQPDLGTKAWPRYVRIAADLPST
ATNKVLKRELIAQGWATGDPVTLWVRRGGPAYRLMSEPAKAALAAEFATH
>gnl|CDD|184021 PRK13389, PRK13389, UTP--glucose-1-phosphate uridylyltransferase GalU
MAAINTKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIEN
HFDTSFELEAMLEKRVKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIL
DEYESDLSQDNLAEMIRRFDETGHSQIMVEPVADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPS
NLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYG
IRHNTLGTEFKAWLEEEMGIKK
>gnl|CDD|139538 PRK13390, PRK13390, acyl-CoA synthetase; Provisional
MYPGTHAQIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAAL
RSGLYITAINHHLTAPEADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGA
GPRLTEQPCGAVMLYSSGTTGFPKGIQPDLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPL
RWCSMVHALGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAA
PCPVDVKHAMIDWLGPIVYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLGDLHICDDDGNELPAGRIGT
VYFERDRLPFRYLNDPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENA
LTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRT
PTGKLVKGLLR
>gnl|CDD|184022 PRK13391, PRK13391, acyl-CoA synthetase; Provisional
MYPGIHAQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAE
RSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLDGDGELEGFVGYAE
AVAGLPATPIADESLGTDMLYSSGTTGRPKGIKRPLPEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPLY
HSAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVA
IHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFGDLHILDDDGAELPP
GEPGTIWFEGGRPFEYLNDPAKTAEARHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEA
ENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDEL
PRLPTGKLYKRLLRDRYWGNK
>gnl|CDD|184023 PRK13392, PRK13392, 5-aminolevulinate synthase; Provisional
MMNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPDGPRRVTIWCSNDYLGMGQHPDVIGAMV
DALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDAL
NHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNAL
TYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTAL
PPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMS
EHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRLELPRWREAAQAA
>gnl|CDD|184025 PRK13394, PRK13394, 3-hydroxybutyrate dehydrogenase; Provisional
MMSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDA
VNAGIDKVAERFGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVI
YMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIPEQAKELGISE
EEVVKKVMLGKTVDGVFTTVEDVAQTVLFLSSFPSAALTGQSFVVSHGWFMQ
>gnl|CDD|237375 PRK13395, PRK13395, ureidoglycolate lyase
MKTLRAERLTREAFAPFGDVIELDGARHFPINGGTTERFHDLATIDVTGDGGRPLVSLFRAQPRALPVAI
TMMERHPLGSQAFIPLAAVSRYAVVVAPAGEFRPDEMRAFLAEGWQGVNYAKGVWHHPLLALDAVSDFVV
VDRGGPQPNCDEIPLDTPWRLEFEDATASAE
>gnl|CDD|237376 PRK13396, PRK13396, 3-deoxy-7-phosphoheptulonate synthase; Provisional
MIIVMKVGTPEAEIERISQELTSWGLTPEKIVGKHKVVIGLVGDTAELDPLQIQELSPWIEQVLRVEKPF
KRASREYRHGEASEVVVPTPNGPVPFGENHPVVVVAGPCSVENEEMIVETAKRVKAAGAKFLRGGAYKPR
TSPYAFQGHGESALELLAAAREATGLGIITEVMDAADLEKIAEVADVIQVGARNMQNFSLLKKVGAQDKP
VLLKRGMAATIDEWLMAAEYILAAGNPNVILCERGIRTFDRQYTRNTLDLSVIPVLRSLTHLPIMIDPSH
GTGKSEYVPSMAMAAIAAGTDSLMIEVHPNPAKALSDGPQSLTPDRFDRLMQELAVIGKTVGRWPQPAAA
LV
>gnl|CDD|184029 PRK13399, PRK13399, fructose-bisphosphate aldolase class II
MALITLRQLLDHAAENGYGVPAFNVNNMEQILAIMEAAEATDSPVILQASRGARKYAGDAMLRHMVLAAA
EMYPDIPICLHQDHGNSPATCQSAIRSGFTSVMMDGSLLADGKTPASYDYNVDVTRRVTEMAHAVGVSVE
GELGCLGSLETGEAGEEDGVGAEGKLSHDQMLTDPDQAVDFVQRTGVDALAIAIGTSHGAYKFTRKPDGD
ILAIDRIEEIHARLPNTHLVMHGSSSVPQELQEIINAYGGKMKETYGVPVEEIQRGIKHGVRKVNIDTDI
RLAMTGAIRKVLAEHPSEFDPRKALKPAMKAMTALCKQRFEAFGTAGQASKIKVLPLDEMAKRYAKG
>gnl|CDD|106361 PRK13403, PRK13403, ketol-acid reductoisomerase; Provisional
MKTYYEKDANVELLQGKTVAVIGYGSQGHAQAQNLRDSGVEVVVGVRPGKSFEVAKADGFEVMSVSEAVR
TAQVVQMLLPDEQQAHVYKAEVEENLREGQMLLFSHGFNIHFGQINPPSYVDVAMVAPKSPGHLVRRVFQ
EGNGVPALVAVHQDATGTALHVALAYAKGVGCTRAGVIETTFQEETETDLFGEQAVLCGGVTALVKAGFE
TLTEGGYRPEIAYFECLHELKLIVDLMYEGGLTNMRHSISDTAEFGDYVTGSRIVTDETKKEMKRVLTEI
QQGEFAKKWILENQAGRPTYNAMKKAEQNHQLEKVGEELREMMSWIHAPKELVKK
>gnl|CDD|184033 PRK13404, PRK13404, dihydropyrimidinase; Provisional
MMAFDLVIRGGTVVTATDTFQADIGIRGGRIAALGEGLGPGAREIDATGRLVLPGGVDSHCHIDQPSGDG
IMMADDFYTGTVSAAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVLTEE
LPALIAQGYTSFKVFMTYDDLKLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYH
AISRPMLAEREATHRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDRP
GMEGAKYICSPPPRDKANQEAIWNGLADGTFEVFSSDHAPFRFDDTDGKLAAGANPSFKAIANGIPGIET
RLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGADADIAIWDPDREVTITNADLHHAAD
YTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLARSLPDRARPNGRLEPEL
>gnl|CDD|237377 PRK13405, bchH, magnesium chelatase subunit H; Provisional
MPKRTSAADGTPVRVVIVTLDSHLAGAAARARPRLQRDFPGLTLSVHAAAEWGEDPAALEACRADIATGD
IVIATMLFMDEHIRAVLPALQARRDACDAMVGCMSAGEVVKLTRMGKFDMSGPASGPLALLKKLRGKKKE
GGSSGEGQMAMLRRLPKILRFIPGTAQDVRAYFLTLQYWLAGSDENVANMVRFLVDRYAAGPRAALRGIA
KAAAPIEYPEVGLYHPRMPGRITEDLDDLPRPAGAKGTVGLLLMRSYVLAGNTAHYDGVIEALEARGLRV
VPAFASGLDGRPAIEAYFMKDGRPTVDAVVSLTGFSLVGGPAYNDSAAAEEILARLDVPYLAAHPLEFQT
LEQWAASDRGLGPVEATMMVAIPELDGATGPMVFGGRSDGVACTGCDRGCKFSGNDAARDMAVCPERAEM
LAARVARLVALRRSERAERKVAVVLFNFPPNAGATGTAAYLSVFESLFNTLRAMKAEGYTVEVPESVDAL
REAILGGNAARYGTPANVHARVPADDHVRREPWLAEIEAQWGPAPGRHQSDGRSIFVLGAQFGNVFVGVQ
PAFGYEGDPMRLLFEKGFAPTHAFSAFYRWLREDFGADAVLHFGTHGALEFMPGKQAGLSAACWPDRLIG
DLPNVYLYAANNPSEGTLAKRRSAATLISYLTPPLAAAGLYRGLLDLKASLERWRGLPPDATEERAELAA
LIQAQAAAVDLAPAEPAWEEEAGARIAKLWAALLELEYTLIPHGLHVVGEPPSEEERVDLLLAMAEASHG
KRAEIDRLLAEDHELPALLRALDGRFIRPVPGGDLLRTPAILPTGRNLHGFDPFRIPSAFALQDGARQAA
RLLERHAAEGNPLPESVALVLWGTDNLKSEGGPIAQALALMGARPRFDSYGRLAGAELIPLEELGRPRID
VVMTLSGIFRDLLPLQTKLLAEAAFLAASADEPLEQNFVRKHALAYQAEHGCDMETASLRVFSNAEGAYG
SNVNHLVDSGRWEDEDELADTYTRRKSFAYGRSGKPVQQAALLQSVLADVDLAYQNLDSVELGVTTVDHY
FDTLGGISRAVKRAKGGEAPVYIGDQTRGEGTVRTLSEQVALETRTRMLNPKWYEGLLKHGYEGVRQIEA
HVTNTMGWSATTGQVAPWVYQRLTETFVLDEEMRERLAALNPTASAKVANRLIEAHERNYWTPDPETLAA
LRRAGEELEDRLEGVGVAA
>gnl|CDD|237378 PRK13406, bchD, magnesium chelatase subunit D; Provisional
MSPAAADWADAALAAALLAVDPAGLGGVVLRARAGPVRDRWLAALRALLPAGTPLRRLPPGIADDRLLGG
LDLAATLRAGRPVAQRGLLAEADGGVLVLAMAERLEPGTAARLAAALDTGEVRLERDGLALRLPARFGLV
ALDEGAEEDERAPAALADRLAFHLDLDGLALRDAREIPIDADDIAAARARLPAVGPPPEAIAALCAAAAA
LGIASLRAPLLALRAARAAAALAGRTAVEEEDLALAARLVLAPRATRLPAPPQPPEEEPPPPPPPPEDDD
DPPEDEEEQDDAEDRALEEIVLEAVRAALPPDLLARLAAGGARARARSAGGAGAAQKGNRRGRPLGSRPG
EPRGGARLDLIETLRAAAPWQPLRRRQAGTARRLLVRPDDFRIRRFKQRSETTTIFVVDASGSAALHRLA
EAKGAVELLLAEAYVRRDQVALVAFRGRGAELLLPPTRSLVRAKRSLAGLPGGGGTPLAAGLDAAAALAL
QVRRKGMTPTVVLLTDGRANIARDGTAGRAQAEEDALAAARALRAAGLPALVIDTSPRPQPQARALAEAM
GARYLPLPRADAGRLSQAVRAATG
>gnl|CDD|184037 PRK13409, PRK13409, ribosome biogenesis/translation initiation ATPase RLI
MMRIAVVDYDRCQPKKCNYECIKYCPVVRTGEETIEIDEDDGKPVISEELCIGCGICVKKCPFDAISIVN
LPEELEEEPVHRYGVNGFKLYGLPIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVL
KRFRGTELQNYFKKLYNGEIKVVHKPQYVDLIPKVFKGKVRELLKKVDERGKLDEVVERLGLENILDRDI
SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYLADN
VHIAYGEPGAYGVVSKPKGVRVGINEYLKGYLPEENMRIRPEPIEFEERPPRDESERETLVEYPDLTKKL
GDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYIKPDYDGTVEDL
LRSITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL
AVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGEPGKHGHASGPMDMREGMNRFLKELGITFRR
DEETGRPRVNKPGSYLDREQKERGEYYYAD
>gnl|CDD|184038 PRK13410, PRK13410, molecular chaperone DnaK; Provisional
MGRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDGELLVGQLARRQLVLNPQNTFYNLK
RFIGRRYDELDPESKRVPYTIRRNEQGNVRIKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVI
TVPAYFNDSQRQATRDAGRIAGLEVERILNEPTAAALAYGLDRSSSQTVLVFDLGGGTFDVSLLEVGNGV
FEVKATSGDTQLGGNDFDKRIVDWLAEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPF
ITATEDGPKHIETRLDRKQFESLCGDLLDRLLRPVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRT
LIPREPNQNVNPDEVVAVGAAIQAGILAGELKDLLLLDVTPLSLGLETIGGVMKKLIPRNTTIPVRRSDV
FSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGILQVSATDRTTGR
EQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDAALEFGPYFAERQ
RRAVESAMRDVQDSLEQDDDRELDLAVADLQEALYGLNREVRAEYKEEDEGPLQGIKNTFGSLKDELFSD
DYWDDDPWDNPMRRRDRGGRRSRNRRDDDPWDDDDDWL
>gnl|CDD|184039 PRK13411, PRK13411, molecular chaperone DnaK; Provisional
MGKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGDRLVGQLAKRQAVTNAENTVYSIK
RFIGRRWDDTEEERSRVPYTCVKGRDDTVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITV
PAYFTDAQRQATKDAGTIAGLEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVF
EVKATAGNNHLGGDDFDNCIVDWLVENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFI
TADETGPKHLEMELTRAKFEELTKDLVEATIEPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKF
FGGKQPDRSVNPDEAVALGAAIQAGVLGGEVKDLLLLDVTPLSLGIETLGEVFTKIIERNTTIPTSKSQV
FSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGILKVSAQDQGTGR
EQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEELKQRA
EQKVEQLEAALTDPNISLEELKQQLEEFQQALLAIGAEVYQQGGSQTTDTVEPTSDTLITATMNSSNETT
LIDEFNFDFDDEETVASDYEAID
>gnl|CDD|237379 PRK13412, fkp, bifunctional fucokinase/L-fucose-1-P-guanylyltransferase; Provisional
GNDTASTLSGVSAKARRLYAARIANMKKLLSLPPNLVDSFHSLEQVDRTEWFCTSDPVGQKLGSGGGTTW
LLEACFRNGSPGGDFTEWLGKEKRILLHAGGQSRRLPGYAPSGKILTPVPVFRWERGQRLSQNLLSLQLP
LYERIMSKAPEGLHTLIASGDVYIRSEQPLQDIPEADVVCYGLWVDPSLATNHGVFVSSRKSPERLDFML
QKPSLEELGGLSKTHLFLMDIGIWLLSDRAVELLMKRSGKEDGGKLKYYDLYSDFGLALGTHPRIGDDEL
NALSVAILPLPGGEFYHYGTSRELISSTLAVQNLVTDQRRIMHRKVKPHPAMFVQNAVLSGKLTAENATL
WIENSHVGEGWKLASRSIITGVPENSWNLDLPEGVCIDVVPVGDRGFVARPYGLDDVFKGALADGKTTWF
GRPFLEWMEARGLSWPDLKGRTDDLQAAHLFPVVTSVEELGAVLRWMLSEPSLEEGKEIWLRSEKLSADE
ISAYANLARLYAQREAFRKANWRALAANHEKSVFYQLDLADAAEDFVRLLLDMPEILPEDAPLMLRIHNR
MFRARILKLSGARYREEEQAAFRLLRDGLLDGAYPRKQTPKLEVYSDQIVWGRSPVRIDLAGGWTDTPPY
CLYSGGNVVNLAIELNGQPPLQVYVKPCSEPHIVLRSIDLGAMEVVRTNEELRDYKKVGSPFSIPKAALC
LAGFAPRFSAESYASLEEQLKAFGSGIEITLLAAIPAGSGLGTSSILAATVLGAISDFCGLAWDKNEICN
RTLVLEQLLTTGGGWQDQYGGVLPGVKLLQTGAGFAQSPLVRWLPDSLFTQPEYRDCHLLYYTGITRTAK
GILAEIVRSMFLNSTAHLQLLHEMKAHALDMYEAIQRGEFEEFGRLVGKTWEQNKALDSGTNPAAVEAII
ELIKDYTLGYKLPGAGGGGYLYMVAKDPGAAERIRKILTENAPNPRARFVDMSLSDKGLQVSRS
>gnl|CDD|184041 PRK13413, mpi, master DNA invertase Mpi family serine-type recombinase
MIYAYIRVSTDKQTVENQRFEITNFAEKNNLTIDKWIEETISGTKSYKDRKLGKLLKKMRKGDILIVSEL
SRLGRNLMEIMSILNICMEKEVIVYTIKEGYELGDDINSKVLAFAFGLSAEIERNLISQRTKEALARKKA
EGVTLGRPKGSTPKKYKLTGKEEKIKKLLDKGTSKSEIARKLGVSRTTLARFLKTRGLRI
>gnl|CDD|139556 PRK13414, PRK13414, flagellar biosynthesis protein FliZ; Provisional
MNNKFLFLVFLIFFNFFLFAQSNEQLNSVSSDLENEVNLPIFEEDKANLNNKDIQPISLFNISDLVTIVL
FFLIFFFIIFLFKKMILNSKKSKNEQNSNLIRELAFYEIDNKNSIRIINILGNVYVFLVSSNSSILLKEI
KSEEELENLKFRLSKIKSSAKKDSFKSIFKKILRKNKKEEIPFDGNEYAKLENDIETSLKSKQDRLKKF
>gnl|CDD|184042 PRK13415, PRK13415, flagella biosynthesis protein FliZ; Provisional
MKKRIIRIAAICLFAALALHPAPAFAAQSPTVNECLQHPDKCGKETPTGQQTQETAEAAASSVSAFDFVK
LIGATLFVIFLIYALVKWLNKRNRLLKPKGYIEHLGGTSVGQNRSVQLIKVGNRVLVVGVGESIQLLKEI
EDEKEIEEILAQHEERLESKAEWSRWGQKLRDQWKGKSKQKQTTLPSFSALLKEELKELKEKRSEGLKRL
KKKGTAHDE
>gnl|CDD|237380 PRK13417, PRK13417, F0F1 ATP synthase subunit A; Provisional
NQTSFMTKKFIFFALLVVLLPIQIFASGQSSGEVFDLNEVIVHHLMDAAEFPFNIGGVKVFEGEPDFDSS
NHDIFTDHETGKRFHYVGGFDMHITKRVTMMWIVAFFLFLIFIPAANIIAKNPLKVQSRFANTVEVFVNF
LRKDIVDESMHGHGHSYYHYIFTLFFFILFCNLMGLVPSVGELTVVASDYGGLVALGVMDHTPHALPTFA
KVWSGITVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIVSPMAKTFA
LTVRLLANMTAGHVIILALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFVGLSMH
RH
>gnl|CDD|237381 PRK13419, PRK13419, F0F1 ATP synthase subunit A; Provisional
KTFARLVALLVPLLLNQNDAAFASAEAAAEAHHASAAAAAAAPAGEHGAAVHAEAAAHAEQAEGGHEEKA
GDVIMHHILDSYVFEFEPFGEVHLPKLVVGGFDISITKHVVMMWIASAILLVVFLAAGRKYKKMTKSQAP
KGLANAMEALVEFIRLDVAKSNIGHGYEKFLPYLLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFT
FFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAGHIVILSLIFIS
FILKSYIVAVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALFIGLATAHEGHDEEHAEAHGH
>gnl|CDD|237382 PRK13420, PRK13420, F0F1 ATP synthase subunit A; Provisional
EGFLAHVLFHIGPLPITESVLTTWGIMIVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVLPRH
ARLVLPFVGTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEGLREYLKHYLSPSP
FLLPFHLISEITRTLALAVRLFGNIMSLELAALLVLLVAGFLVPVPILMLHIIEALVQAYIFGMLALIYI
AGGIQAHELKSQGESL
>gnl|CDD|237383 PRK13421, PRK13421, F0F1 ATP synthase subunit A; Provisional
MTASPLSTVPLFSLGPVPISAPVVVTWAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTM
QTDPAPYRALIGTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFAE
PTWVMIPLNLVEQLTRTFSLIVRLFGNVMSGVFVIGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAM
VFIGAAVSDDEAS
>gnl|CDD|184046 PRK13422, PRK13422, F0F1 ATP synthase subunit gamma; Provisional
MSNAREIRSKVQSVKNTQKITGAMELVAASKMRGAIVKMNNVRPYVESANTIIKNVTAASIDYPNPYLFD
RDVKRVGYIVTSTDRGLCGGLNINLFKHVLKEIKNNIEDRVGVDVCVIGSKAENFFAKLKDVNIVATAHY
NDKDKEGSIRAIGGAVKVMLDKFTAGEIDRLYMSSNQFVSTIKQRPRLQTLLPIQDIFSAEEIKANKEKA
TKGHWDYIYERDIEEVLNALCIRYIEAQVRGAILENAACEQAARMMAMKNATDNASDIIDQLKLDYNKVR
QAMITQELAEICSGAAAV
>gnl|CDD|237384 PRK13423, PRK13423, F0F1 ATP synthase subunit gamma; Provisional
MASLKDIKKRIVSVKNTRQITKAMKMVSAAKLRRAQENVVAARPYAAKLGEVLGSLAARAGEDAHPLLVP
REVKKALLVVVTSDRGLCGGFNSNLCKAAERFLKENKDEFEEISLTTVGRKGREFLKNRGLIIRKNYGGV
VANLTYETAALLAQELIEGYLAGEYDEVYLVYNEFKSVMSQDITVQQLLPIDPPEAADDEYLPEYIYEPS
RDALLAELLPKHVEVQIYRALLESVASEHGARMTAMDSATKNATEMIGKLTLQYNRARQAAITTELMEIV
SGAEALKG
>gnl|CDD|172047 PRK13424, PRK13424, F0F1 ATP synthase subunit gamma; Provisional
MPSLKDVKVKIAGVKKTKQITKAMNMVASAKLRGAQQRIERFRPYAEKFYDMLGDLASRADSSAHPLLEV
REEIKTCGIVLITSDRGLCGSFNANLINAALKLAKQKTAEGKTVKFYCVGKKGRDAIRKTDFEIVTAYAD
QMTSFDFQLANSIGLEVIDGYLTGELDEVVLVYGEFVSMARQLPITLQILPIAPEEAEEEEAGASSEYIY
EPSVEGLLAELLPRFIKVQIYRGLLDTSASEHAARMTAMDNATRNCDDMIGSLTLLYNKTRQASITRELM
DIVGGAEALKG
>gnl|CDD|139564 PRK13425, PRK13425, F0F1 ATP synthase subunit gamma; Provisional
MPTLKDIRVRIKGVKSTQQVTKAMKMVAAAKLRRAQERAIMARPYAAKLKEMLGSLSAKVDTSLNPLLSP
RSEVNKVLVILITSDRGLCGAFNTNIIKLAQKVIHEDYAALHAKGGVSMICAGTRGFDFFRKRGYNIVKG
YPGVFQNLDFSVAKEIAETASGMYLRGEVDKVVVVYNEFKSVLAPNLKSEVLLPITPEKPGAEGGSDYIY
EPSPAAIIDELVPKHLNTQVWRMMLESNAAEQAARMTAMDSATENAKELLRTLNISYNRARQAAITKELS
EIVAGADALQG
>gnl|CDD|237385 PRK13426, PRK13426, F0F1 ATP synthase subunit gamma; Provisional
MASLKEIKTRIASVQSTRKITSAMKMVASAKLHKAQGAIENMLPYQRKLNHILTNFLSADLDVESPFTVE
RPVKRVAIVVFSSNTSLCGGFNANIIKLLLQTIGEYRTLGQDNILIYPVGKKIEEAVKKLGFKVQGDYQT
LADKPSYEEAAALAMRLMELFLEGEIDKVELIYHHFKSMGVQVLTRETYLPIDLSQEKNAEHAGGVANDY
IIEPSADTVLNDLIPKLLSLKIYTALLDSNASEHAARMVAMQIATDNANELLQELTLQYNKSRQQAITNE
LLDIVGGSMAN
>gnl|CDD|172049 PRK13427, PRK13427, F0F1 ATP synthase subunit gamma; Provisional
MATPREIKKRINSVKNTRKITRTMEMVSTAKSKKATDRVNAAHPYANKIKELVSSLASLEGVVHSPYLRR
PEKIRTVALLIITANRGLCGGFNSNLNRMAKARIAELKKKGVNVELHIVGKKGISFFKFAGEKAEKTYTH
IDDKSGYKEAEELANLFMERFANESVDAVEIASTVYYSAASQKPETTRVLPLEPPTAAAEGSVQDDVVYE
PSPEAILESLLPLVVKTAFLKAILEANASEQIARRIAMKSATDAASEMIKLLTRGYNRVRQAKITQEISE
IVGGADALN
>gnl|CDD|184048 PRK13428, PRK13428, F0F1 ATP synthase subunit delta; Provisional
MSTFIGQLIGFAVIVFLVWRFVVPPVRRLMAARQDTVRQQLAESATAADRLAEADQAHTKAVEDAKAEAA
RVVEEAREDAERIAEQLRAQADAEAERIKVQGARQVQLLRAQLTRQLRLELGHESVRQAGELVRNHVADP
AQQSATVDRFLDELDAMAPSTADVDYPLLAKMRSASRRALASLVDRFDSVAADLDNQALTTLADELVSVA
KLLDREPVLTKHLTEPAEDAAPKIRLVERLFSGKVGAPTLEVLRTAVSQRWSANSDLIDALEHVARLALL
ERAERAGQVDEVEDQLFRFSRILDAQPRLAILLSDYTVPADGRVALLRKVLGGASTVNPVTVALLSQTVE
LLRGQPAEEAVLFLAELAVARRGEVVAQVSAAAELSDAQRTRLTEVLSRIYGRPVSVQLHIDPELLGGLS
IAVGDEVIDGTLSSRLAAAEAQLPD
>gnl|CDD|237386 PRK13429, PRK13429, F0F1 ATP synthase subunit delta; Provisional
MLLNAIARRYAKALFQLAKEKGQLDSVYEELKQLAELLEDSPELRDALSNPVLSAEEKKAVLEKLLGKLK
VSPEVLNFLKLLADRRRLGILPEIAARYLELADEQKGIVRATVTSAVPLSEAQQEAIRQKLEKMTGKKVE
LDTAVDPSLIGGVVVKIGDKVLDASVRTQLRRLKETLKKGE
>gnl|CDD|237387 PRK13430, PRK13430, F0F1 ATP synthase subunit delta; Provisional
MRAASREALASARSRLDELLASADAAAAQIGNELFAVVAVLDRERSLRRALTDPARPPEAKVELVKRLFG
GKVSPATLEVVSDAVRQRWSRPRDLADALEELGVRALLASAEAQGALDDVEDELFRLGRILASNPELRLA
LSDRAAPAEAKRELLARLLYGKVTPVTERLAEQAVGRPRGRSIEEGLDELSNLAAARRGRSVATVTTAVP
LSDEQKQRLAAALSRIYGRPVHLNSEVDPSVLGGMRVQVGDEVIDGSVAGRLERLRRRLAG
>gnl|CDD|184051 PRK13431, PRK13431, F0F1 ATP synthase subunit delta; Provisional
MQDLKVISKHYAKALKNHTKGDLALLEEIVVGLKNVAEAIKLHKLNQVLAHVSLKVKKEVVFEILEKITS
IKACSVLKPVMEVVLKNNRLDMLELITEELSFDSKRTLEATLLVPEKLENNELEAVQQKLQARFNAPVEI
AQDTWSKKGVSLSVSSLDLEIGFSKEDILKKIEKQVIQSI
>gnl|CDD|139571 PRK13434, PRK13434, F0F1 ATP synthase subunit delta; Provisional
MNDSGVSKVYASALLGAANSPEEVEQELGDLVQLLFKDEKIRNFFLSPTVSPEEKEQTLAKNLRGKISDI
TLNFLGVLLNKGRFIYLPEIQKDFTVELDKKKGRVRAQIVSYPSLEPAQVDKLGSILSEKFKSEFILEVS
EDKNLLGGFVVQFNDLKIEKSIASQLGEIKKAMLEKKLPVGAFY
>gnl|CDD|184052 PRK13435, PRK13435, response regulator; Provisional
MFLRQLKVLIVEDEALIALELEKLVEEAGHEVVGIAMSSEQAIALGRRRQPDVALVDVHLADGPTGVEVA
RRLSADGGVEVVFMTGNPERVPHDFAGALGVIAKPYSPRGVARALSYLSARRVGDRASGPTPMGVFLAPA
TLTNS
>gnl|CDD|184053 PRK13436, PRK13436, F0F1 ATP synthase subunit delta; Provisional
MYLKNKNIYNYAEALFDIANEENNVEKYINEVFKIIEILKNNKDLIKLLTSYFIDKEEKFKIIDKIFSAK
IDIYLVNFLKILAKNNLFIYIKQILKKFVKLSNEKLNITYGEIYTTEPLSEVQISRFESKLSKKLNKKVH
LVNKIDPKLIAGIKIKVDNKVFENSIKSKLKELKKQVLK
>gnl|CDD|184054 PRK13441, PRK13441, F0F1 ATP synthase subunit delta; Provisional
MRYSAIASKYARALLNVAIELEKEEEYGEFLDLVCQIYESAKEFFDNPIVKPEKKVSLIKEIMKEFGQEM
DEFFENFLNLVFENKRQKLLPQIRALFEYEKILSEQKVPVNLTTAHELSDEELKLLRKFVRKYVLRDPVF
EETIDESLIAGAVVEFEGKRLDVTVQGRLKKIAREVLKRG
>gnl|CDD|184055 PRK13442, atpC, F0F1 ATP synthase subunit epsilon; Provisional
MAGATLHVNIVAADRPVWSGEATMVVARTTEGDIGILPGHEPLLGVLESGTVTVVTPGGERISAAVDGGF
ISFDSNKLTVLAERAELVA
>gnl|CDD|237388 PRK13443, atpC, F0F1 ATP synthase subunit epsilon; Provisional
MAGTLQFDLVSPERRLASFQATAVQIPGADGDMTAMEGHAPTITTLRPGILRAHGPSGTQEYAVTGGFAE
INATSISVLAEKAIPVEELTGAVLDEFIAEARELASVALPENEPGDVDDAAKTLADMLALGAHSGL
>gnl|CDD|139576 PRK13444, atpC, F0F1 ATP synthase subunit epsilon; Provisional
MMAKKLTVSVISPEKILYKGEVDSLIVPGSEGFFGILPNHAPLVATLGIGLLEIRKGEKLKRISVEGGFC
EVKDNQISILTDHGALKEDIDHEHEKKLLAEAEKLPPSDSKNLLLQKTKTRILVASR
>gnl|CDD|184056 PRK13446, atpC, F0F1 ATP synthase subunit epsilon; Provisional
MAKKLKLEIVTPEKKVLSEEVDEVGAPGVLGEFGVLPGHAPFLTALKIGELTYKKGGKTHYVAVNGGFAE
VSNNKVTVLAETAERAEEIDVERARAALERAEQRLKKLTPEDDSARAEAALERALIRLQVAGKATR
>gnl|CDD|184057 PRK13447, PRK13447, F0F1 ATP synthase subunit epsilon; Provisional
LRLTIATPLAVVVDELDIVSLRAEDASGGFGILPGHADFLTVLRASVVRWRRADGATHYCAVRGGVLRVT
GGARVEIACREAVLGEDLARLEAVVRAVRAAQLDAARRARVEQTRLHAQAVRQLLRYLRPERGADG
>gnl|CDD|139579 PRK13448, atpC, F0F1 ATP synthase subunit epsilon; Provisional
MATFHFDLVSPEKLAFSGEVDQVDIPGVEGDFGVLAGHAPVVAVIRPGILTVTAGGNQQKIVVLGGLAEV
SEKGLTVLADVATSVADLDLAQFAATIAEMEAQLAGKVGDELDRAIERLDHFKSIQHQLNTTAMH
>gnl|CDD|184058 PRK13449, atpC, ATP synthase F1 subunit epsilon
MAKLHFELVTPERLLRSGEVDMVVVPGTEGDFGVLAGHAPFMTTLREGEVTVYSSDGAAPEVFHVQGGFA
EVNEKGLTILAEHAVEAA
>gnl|CDD|184059 PRK13450, atpC, F0F1 ATP synthase subunit epsilon; Provisional
ANNIKLTILTPEKNFYIGEVKEVITEGLDGDIAILPNHVPLITYLKPTITKIIDENGEKKKIFTSSGVLK
VENNEVYILCDASEWPEEIDIKRAENAKKRAEERLRKKDEIDVKRAELALFRAIARIKLKEL
>gnl|CDD|172059 PRK13451, atpC, F0F1 ATP synthase subunit epsilon; Provisional
MKVKIVTPYGIVYDRESDFVSFRTVEGEMGILPRRAPIIAKLSVCDVKIKSGDDEYEYKVADGFLHCDGK
NVIIITEEAGREEEISPHRYLGARERVERVR
>gnl|CDD|106409 PRK13452, atpC, F0F1 ATP synthase subunit epsilon; Provisional
MTKKYLKVDVVSPLGSVFKGEADMVSLRGSAGEMGIAYGHTELLSTLPAGVVNVRKDQHTDVLYVSGGIV
EVTPTRVTIMVDDMERAENLNQAEAEKARARAKEVLKNPDASKLDIEAANKRLKEADARLKALNSSNGLY
YSKDD
>gnl|CDD|184060 PRK13453, PRK13453, F0F1 ATP synthase subunit B; Provisional
MTETANLFVLGAAGGVEWGTVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQK
LEEENKQKLKETQEEVQKILEDAKVQARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSE
LSVLIASKVLRKEISEQDQKALVDKYLKEAGDK
>gnl|CDD|184061 PRK13454, PRK13454, F0F1 ATP synthase subunit B'; Provisional
AMTTEVHAAAAAAGHAASAPGMPQLDFSTFPNQIFWLLVTLVAIYFVLTRVALPRIGAVLAERQGTITND
LAAAEELKQKAVEAEKAYNKALADARAEAQRIVAETRAEIQAELDVAIAKADAEIAAKAAESEKRIAEIR
AGALESVEEVAKDTAEALVAALGGKADAAAVDAAVAQRMKG
>gnl|CDD|184062 PRK13455, PRK13455, F0F1 ATP synthase subunit B; Provisional
MKLLSALAALAASPALAAGGPFFSLSNTDFVVTLAFLLFIGILVYFKVPGMIGGMLDKRAEGIRSELEEA
RALREEAQTLLASYERKQREVQEQADRIVAAAKDEAQAAAEQAKADLEASIARRLAAAEDQIASAEAAAV
KAVRDRAVSVAVAAAADVIAKQMTAADANALIDEAIKEVEARLH
>gnl|CDD|237389 PRK13456, PRK13456, DNA protection protein DPS; Provisional
QEMAVVGREVVEKSGVDVDKLVELLVKNAAAEFTTYYYYTILRAHLIGLEGEGLKEIAEDARLEDRNHFE
ALVPRIYELGGKLPRDIREFHDISACPDAYLPENPTDPKEILKVLLEAERCAIRTYTEICDMTAGKDPRT
YDLALAILQEEIEHEAWFSELLGGGPSGHFRRSYPGESPFVSKFLR
>gnl|CDD|139585 PRK13460, PRK13460, F0F1 ATP synthase subunit B; Provisional
MVLLAAKGLSLLDVNPGLVVWTLVTFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALL
KDYEARLNSAKDEANAIVAEAKSDALKLKNKLLEETNNEVKAQKDQAVKEIELAKGKALSQLQNQIVEMT
ITIASKVLEKQLKKEDYKAFIETELAKLGKLSA
>gnl|CDD|184064 PRK13461, PRK13461, F0F1 ATP synthase subunit B; Provisional
MEINIPTIIATIINFIILLLILKHFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAK
EEGKKIVEEYKSKAENVYEEIVKEAHEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEES
IDESEHRRLIKDFISKVGI
>gnl|CDD|139587 PRK13462, PRK13462, acid phosphatase; Provisional
MGVRNHRLLLLRHGETEWSKSGRHTGRTELELTETGRTQAELAGQALGELELDDPLVISSPRRRALDTAK
LAGLTVDEVSGLLAEWDYGSYEGLTTPQIRESEPDWLVWTHGCPGGESVAQVNERADRAVALALEHMESR
DVVFVSHGHFSRAVITRWVELPLAEGSRFAMPTASIAICGFEHGVRQLSALGLTGHPQPIAAG
>gnl|CDD|172065 PRK13463, PRK13463, phosphoserine phosphatase 1
MKTTVYVTRHGETEWNVAKRMQGRKNSALTENGILQAKQLGERMKDLSIHAIYSSPSERTLHTAELIKGE
RDIPIIADEHFYEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGENFEAVHKRVIEGMQLLLEK
HKGESILIVSHAAAAKLLVGHFAGIEIENVWDDPFMHSASLSIIEFEDGKGEVKQFADISHFQ
>gnl|CDD|184065 PRK13464, PRK13464, F0F1 ATP synthase subunit B
MDMSLQVLGNLNGLTAVAVALLISLPALGTAIGFGVLGGKYLEGVARQPELGGMLLGRMFIVAAFVDAFA
AISIAIGFLVLYANPLAIPGLAEAAQKVIGA
>gnl|CDD|172066 PRK13466, PRK13466, F0F1 ATP synthase subunit C; Provisional
MSLGALALGLACLGVSIGEGLLVASYLSSTARQPEMQSKLMAGVFLGVAFIEGTFFVTLAMTFVLK
>gnl|CDD|237390 PRK13467, PRK13467, F0F1 ATP synthase subunit C; Provisional
MNLTILALALACMGVSLGEGFLMANLFKSAARQPEMIGQLRSLMILGVAFIEGTFFVTLVMSFILK
>gnl|CDD|184067 PRK13468, PRK13468, F0F1 ATP synthase subunit C; Provisional
SLTLIAVVSIIAAGLAVSIGAIGPALAEGRAVAAALDAIAQQPDAAGTISRTLFVGLAMIESMAIYCFVV
AMILLFANPFWN
>gnl|CDD|184068 PRK13469, PRK13469, F0F1 ATP synthase subunit C; Provisional
IDGKAFVMGMSAIGAGIAALAGIGAGIGIGIATGKAVEAVGRQPEASGKIMSTMLLGAALAEATAIYGLV
IAIILLFVN
>gnl|CDD|184069 PRK13471, PRK13471, F0F1 ATP synthase subunit C; Provisional
MENLKDLAQALILLGKYIGAGLCMGIGAIGPGIGEGNIGAHAMDAMARQPEMVGTITTRMLLADAVAETT
GIYSLLIAFLILLVL
>gnl|CDD|237391 PRK13473, PRK13473, aminobutyraldehyde dehydrogenase
MQTKLLINGELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKL
ADAIEENADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVG
VVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDA
LVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDC
TAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGG
EAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHR
VSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKHT
>gnl|CDD|237392 PRK13474, PRK13474, cytochrome b6-f complex iron-sulfur subunit; Provisional
MQQSGSSDVPSMGRRQFMNLLTFGTVTGVALGALYPVVKYFIPPSAGGAGGGTTAKDELGNDIPASQFLA
THPAGDRSLVQGLKGDPTYLVVEEDGTIASYGINAVCTHLGCVVPWNSGENKFQCPCHGSQYDATGKVVR
GPAPLSLALVHVTVEDDKVLFSPWTETDFRTGEKPWWV
>gnl|CDD|184072 PRK13475, PRK13475, ribulose-bisphosphate carboxylase
MDQSNRYADLSLKEEDLIAGGRHILCAYKMKPKAGHGYLEAAAHFAAESSTGTNVEVSTTDDFTRGVDAL
VYEIDEARELMKIAYPVELFDRNIIDGRAMIVSFLTLTIGNNQGMGDVEYAKMHDFYVPPRYLELFDGPS
TDISDLWRVLGRPVKDGGYIAGTIIKPKLGLRPEPFAEACYDFWLGGDFIKNDEPQGNQVFAPLKKTVPL
VADAMKRAQDETGEAKLFSANITADDHYEMIARGEYILETFGENADHVAFLVDGYVAGPGAVTTARRQYP
DQYLHYHRAGHGAVTSPSSKRGYTAFVLSKMARLQGASGIHTGTMGYGKMEGEADDRVIAYMIERDSAQG
PFYHQEWYGMKPTTPIISGGMNALRLPGFFDNLGHGNVINTAGGGAFGHIDGPAAGAKSLRQAYDCWKAG
ADPIEYAKEHKEFARAFESFPGD
>gnl|CDD|237393 PRK13477, PRK13477, bifunctional pantoate--beta-alanine ligase/(d)CMP kinase
MRILRTVAGLRAWLRQQRSETIGFVPTMGALHQGHLSLIRRARQENDVVLVSIFVNPLQFGPNEDLERYP
RTLEADRELCESAGVDAIFAPSPEELYPGGAKSITQVQPPSELTSHLCGASRPGHFDGVATVVTRLLNLV
QPKRAYFGEKDWQQLAIIRRLVADLNLPVTIVGCPTVREADGLALSSRNQYLSAEERQQAAALYRALQAA
KKAFQAGKRINLNLLAAVQEELLSEPGLEVEYLELVDPQTLQPLEQIENIGLLAIAVRCGSTRLIDNVFL
MKRQPIIAIDGPAGAGKSTVTRAVAKKLGLLYLDTGAMYRAVTWLVLQEGIDPQDEEALAELLSDLKIEL
KPSSGSPQRVWINGEDVTEAIRSPEVTSSVSAIAAQPAVRQALVKQQQRIGEKGGLVAEGRDIGTHVFPD
AELKIFLTASVEERARRRALDLQAQGFPVIDLEQLEAQIAERDRLDSTREIAPLRKADDAIELITDGLSI
EEVVDKIIDLYRDRIPEEVWPT
>gnl|CDD|184075 PRK13478, PRK13478, phosphonoacetaldehyde hydrolase; Provisional
MMKIQAVIFDWAGTTVDFGSFAPTQAFVEAFAQFGVEITLEEARGPMGLGKWDHIRALLKMPRVAARWQA
VFGRLPTEADVDALYAAFEPLQIAKLADYATPIPGVLEVIAALRARGIKIGSTTGYTREMMDVVVPLAAA
QGYRPDHVVTTDDVPAGRPYPWMALKNAIELGVYDVAACVKVDDTVPGIEEGLNAGMWTVGVILSGNELG
LSEEEYQALSAAELAARRERARARLRAAGAHYVIDTIADLPAVIADIEARLARGERP
>gnl|CDD|184076 PRK13479, PRK13479, 2-aminoethylphosphonate--pyruvate transaminase; Provisional
MTENDPLLLTPGPLTTSRTVREAMLRDWGSWDDDFNALTASVRAKLVAIATGEEGYTCVPLQGSGTFSVE
AAIGSLVPRDGKVLVPDNGAYGARIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRITHVALVHC
ETTTGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPIDIAELGIDALISSANKCIEGVPGFGFVIARRSE
LEACKGNSRSLSLDLYDQWAYMEKTGQWRFTPPTHVVAAFYQALLELEEEGGVPARGARYANNQRTLVAG
MRALGFEPLLDAEIQSPIIVTFHAPADPAYDFKEFYERLKEQGFVIYPGKLTQVDTFRIGCIGDVDAADI
RRLVAAIAEALYWMGIAM
>gnl|CDD|237394 PRK13480, PRK13480, 3'-5' exoribonuclease YhaM; Provisional
MMKGIEELEVGEQVDHFLLIKSATKGVASNGKPFLTLILQDKSGDIEAKLWDVSPEDEATYVPETIVHVK
GDIINYRGRKQLKVNQIRLATEEDGVKISDFVEKAPLSKEEMQEEITQYIFEMENPNIQRITRHLLKKYQ
EEFLDYPAATKNHHEFVSGLAYHVVSMLRLAKSICDLYPSLNKDLLYAGIILHDLGKVIELSGPVSTTYT
LEGNLLGHISIMVNEIAKAADELQIDGEEVLILQHMVLSHHGKAEWGSPKPPLVKEAEILHYIDNIDAKM
NMMDRALKKTKPGEFTERVFALDNRSFYKPTFLD
>gnl|CDD|184078 PRK13481, PRK13481, glycosyltransferase; Provisional
KKKSKRILLKILLTILIIIALFIGIMYFLSTRDNVDELRKIENKSSFVSADNMPEYVKGAFISMEDERFY
KHHGFDLKGTTRALFSTISDRDVQGGSTITQQVVKNYFYDNERSFTRKVKELFVAHRVEKQYSKNEILSF
YLNNIYFGDNQYTLEGAANHYFGTTVNKNSTTMSHITVLQSAILASKVNAPSVYNINDMSENFTQRVSTN
LEKMKQQNYINETQYQQAMSQL
>gnl|CDD|237395 PRK13482, PRK13482, DNA integrity scanning protein DisA; Provisional
REEELREILKLVAPGTPLREGLERILRARTGALIVLGDDEEVESIVDGGFKLDVEFSPTRLYELAKMDGA
IVLSSDGSRILRANVQLVPDPSIPTSETGTRHRTAERVAKQTGVPVIAVSQRRNIITLYVGGLRYVLEDI
GVILSRANQALQTLEKYKARLDEVLTNLSALEFEDLVTLRDVVTVLQRLEMVRRISEEIEGYVVELGTEG
RLISLQLEELLAGVEEERELLIRDYSQEKDEDPEEILEELQELSSEELLDLSAIARLLGYPGGSEALDTP
VSPRGYRLLSKIPRLPSAVIENLVEHFGSLQGLLAASIEDLDEVEGIGEVRARAIREGLSRLAEQSILDR
YV
>gnl|CDD|184080 PRK13483, PRK13483, ligand-gated channel protein
MKKYLAQVISALCLLPAVFVTHALAQAAPDKTMETVVVTASGYEQQIRDAPASISVITREDLENRFYRDL
TDALLDVPGVVVTGGGDRTDISLRGMGSQYTLILVDGKRQSSRETRPNSDGPGVEQAWTPPLAAIERIEV
IRGPMSSLYGSDAIGGVINIITRKVPNEWQGEVRLDTTLQENSDSGNVYQANFFVNGPLIKDLLGLQLYG
QYTQREEDDIEGGYRDKDARSLTAKLALTPNEDHDIMLEVGTSNQERDSTVGKTVAPLAPGESCGRRGCP
ESSTTEYERSTVSLSHTGRWDFGTSDTYIQHEEFDNKSREMKIKNTDFQSSLVAPLGQEHTLTFGAAYNH
QDLTDETSNQISDLTDISRTQWAVFSEDEWRIADDFALTGGLRLDHDENFGGHVSPRVYGVWNLAPSWTV
KGGVSTGFRAPSLRQTTPDWGQVSRGGNIYGNPDLKPETSLNKELGLYYDLGSGLTASLTVFYNEFKDKI
TRVACPATQCTDGPNQFGADPTTYVNIDEAVTQGVEASLSYPITSTLSLSGNYTYTDSEQKSGAYKGSPL
NQLPKHLFQASLNWEPTDRLNSWARVNYRGEESQPTTGPSSSSFIAPSYTFLDLGANYQLTDNLKLSAGI
YNLFDKEINYEEYGYVEDGRRYWLGMTYSF
>gnl|CDD|139605 PRK13484, PRK13484, IreA family TonB-dependent siderophore receptor
MKNKYIIAPGIAVMCSAVISSGYASSDKKEDTLVVTASGFTQQLRNAPASVSVITSEQLQKKPVSDLVDA
VKDVEGISITGGNEKPDISIRGLSGDYTLILVDGRRQSGRESRPNGSGGFEAGFIPPVEAIERIEVIRGP
MSSLYGSDAIGGVINIITKPVNNQTWDGVLGLGGIIQEHGKFGNSTTNDFYLSGPLIKDKLGLQLYGGMN
YRKEDSISQGTPAKDNKNITATLQFTPTESQKFVFEYGKNNQVHTLTPGESLDAWTMRGNLKQPNSKRET
HNSRSHWVAAWNAQGEILHPEIAVYQEKVIREVKSGKKDKYNHWDLNYESRKPEITNTIIDAKVTAFLPE
NVLTIGGQFQHAELRDDSATGKKTTETQSVSIKQKAVFIENEYAATDSLALTGGLRLDNHEIYGSYWNPR
LYAVYNLTDNLTLKGGIAKAFRAPSIREVSPGFGTLTQGGASIMYGNRDLKPETSVTEEIGIIYSNDSGF
SASATLFNTDFKNKLTSYDIGTKDPVTGLNTFIYDNVGEANIRGVELATQIPVYDKWHVSANYTFTDSRR
KSDDESLNGKSLKGEPLERTPRHAANAKLEWDYTQDITFYSSLNYTGKQIWAAQRNGAKVPRVRNGFTSM
DIGLNYQILPDTLINFAVLNVTDRKSEDIDTIDGNWQVDEGRRYWANVRVSF
>gnl|CDD|139606 PRK13486, PRK13486, TonB-dependent receptor
MRITTLASVVIPCLGFSASSIAAAEDVMIVSASGYEKKLTNAAASVSVISQEELQSSQYHDLAEALRSVE
GVDVESGTGKTGGLEISIRGMPASYTLILIDGVRQGGSSDVTPNGFSAMNTGFMPPLAAIERIEVIRGPM
STLYGSDAMGGVVNIITRKNADKWLSSVNAGLNLQESNKWGNSSQFNFWSSGPLVDDSVSLQVRGSTQQR
QGSSVTSLSDTAATRIPYPTESQNYNLGARLDWKASEQDVLWFDMDTTRQRYDNRDGQLGSLTGGYDRTL
RYERNKISAGYDHTFTFGTWKSYLNWNETENKGRELVRSVLKRDKWGLAGQPRELKESNLILNSLLLTPL
GESHLVTVGGEFQSSSMKDGVVLASTGETFRQKSWSVFAEDEWHLTDALALTAGSRYEHHEQFGGHFSPR
AYLVWDVADAWTLKGGVTTGYKAPRMGQLHKGISGVSGQGKTNLLGNPDLKPEESVSYEAGVYYDNPAGL
NANVTGFMTDFSNKIVSYSINDNTNSYVNSGKARLHGVEFAGTLPLWSEDVTLSLNYTWTRSEQRDGDNK
GAPLSYTPEHMVNAKLNWQITEEVASWLGARYRGKTPRFTQNYSSLSAVQKKVYDEKGEYLKAWTVVDAG
LSWKMTDALTLNAAVNNLLNKDYSDVSLYSAGKSTLYAGDYFQTGSSTTGYVIPERNYWMSLNYQF
>gnl|CDD|237396 PRK13487, PRK13487, chemoreceptor glutamine deamidase CheD; Provisional
KPSIRYPGEASNRYFDRHFQCDAAKILPGEYFVTDDDTAIVTVLGSCVSACLRDPVLGIGGMNHFMLPDG
GDSDGPLSASARYGSYAMELLINDLLKLGARRENLEAKVFGGGNVLRGFTSMNVGERNAEFVRDYLQTER
IPIVAEDLLDIYPRKVYFFPTTGKVLVKKLKHAHNDTLVARESAYRARLSKAPVGGDVELF
>gnl|CDD|237397 PRK13488, PRK13488, chemoreceptor glutamine deamidase CheD; Provisional
PMVIKVGIGEYAVGKSPEVIETSGLGSCVGIILYDRGKKIGGLAHVMLPESSGAGDRNPGKYADTAIPLL
IEEMVKLGARKSKLEAKLAGGAAMFDFSSNNLNIGERNIESAKETLKKLGIRIVAEDVGGDYGRTVKFDL
KTGKVIVRKANGGKVIL
>gnl|CDD|237398 PRK13489, PRK13489, chemoreceptor glutamine deamidase CheD; Provisional
MSGLPIATNRYFDNHFHRPGVKLLPNEFYTTREDMVLVTVLGSCVAACLHDPVAGIGGMNHFMLPDDGAD
AGAAASESMRYGAYAMEVLINELIKAGGRRERFEAKVFGGAAVLAGMTTINIGDRNADFVRRYLALERIR
ITAEDLQGVHPRKVAFMPRTGRAMVKKLRLQVPGVAEREAALAREAHGERAARARARVELFAAPAPSAPA
PARPRIELFGRRATQNATRKQEA
>gnl|CDD|184084 PRK13490, PRK13490, chemoreceptor glutamine deamidase CheD; Provisional
MDIKEIKVGIADLNVAKSPDKIITVGLGSCIGIALYDGIKCIGGLSHIMLPDSTQFSNVTNPMKFADLAI
PILIEKMEKLGANKRNLKAKIAGGASMFNFSDKSMVMDIGNRNGKAVKKKLKELSIPILAEDIGGNKGRT
MIFDTSDGKVYIKTVGLGIKEI
>gnl|CDD|184085 PRK13491, PRK13491, chemoreceptor glutamine deamidase CheD; Provisional
MTRCDDSPSASQISITHVTQGSCVASDSPNEVYATILGSCICTCMCDPVAGVGGMNHFLLPSADVEDAQH
LRYGSHAMELLINALLKLGAARQRIEAKIFGGAMMTPQLGAIGQANAAFARRYLRDEGIRCTAHSLGGNR
ARRIRFWPKTGRVQQMFLGSEDVVPNEQPQFRLQGGAGDVTFFDRHNNAEMPDPIKEPR
>gnl|CDD|184086 PRK13493, PRK13493, chemoreceptor glutamine deamidase CheD; Provisional
MLVVAVRFSIQEEAKGQYYRFNHPSDHRHWVKVMPGGVYATSDQEIIHTGLGSCVSACAWDIEMKVGGMN
HFLLPFNNQFESQHWHPQALLSDSSRYGCYAMEVLINRLLSMGAERERLKFKLFGGAHLMGYQSLVGEKN
VEFVLEYAKREKLNVVAQDLGGAQPRKLLFDPQTGQAWVKRIGFSSAHAIKQDEELYQHSIDKQIPSDDV
ELF
>gnl|CDD|184087 PRK13494, PRK13494, chemoreceptor glutamine deamidase CheD; Provisional
MLNHFNFKLKRDVTIIVPGEAFVSNDRVISTILGSCVAVVLYDESRNLIGMNHYVLVKSDLVISPLQRGR
YGVYAIPMLIDAMLENGASKSNLKAKLFGGTNFMAKGTIKVGLENSEFAVNTLNKYGIPILAKDFDQSKS
RKIFVFPENFKVIVEYPDGAKVF
>gnl|CDD|184088 PRK13495, PRK13495, chemoreceptor glutamine deamidase CheD; Provisional
KMKKVIGIGEYAVMKNPGVIVTLGLGSCVGVCMRDPVAKVGAMAHVMLPDSGGKETDKPGKYADTAIKTL
VEELKKMGAKVERLEAKIAGGASMFESSGMNIGARNVEAVKKHLKDFGIKLVAEDTGGNRARSIEYNIET
GKLLVRKVGGGEQVEIKEI
>gnl|CDD|237399 PRK13497, PRK13497, chemoreceptor glutamine deamidase CheD; Provisional
MITEAAARRVHIIQGEYKVVNDPNVVLSTILGSCVAACLRDPVAGVGGMNHFLLPGSATSPTSGGDATRY
GVHLMELLINGLLKQGARRDRLEAKIFGGAKTIATFSNVGEQNAAFAMQFLRDEGIPVVGSSTGGEHGRK
LEYWPVSGRARQYPLTGAETQRTVALEQRPAAAPKPVETSIEFF
>gnl|CDD|237400 PRK13498, PRK13498, chemoreceptor glutamine deamidase CheD; Provisional
MNTPVGTKEIVLQPGEVVFATRPTRLRTLLGSCVAITFWHPQQHIGGMCHFMLPGRIRKHQPLDGRYADE
AMELLIRHALANGTPPEDYQVKLFGGGNMFPELQQDLHTLNVADKNIHAALALAEQNGLHLKAQDLGSTG
HRSIIFDLWNGNVWVRHQPMEHREKDA
>gnl|CDD|237401 PRK13499, PRK13499, L-rhamnose/proton symporter RhaT
MSNAIILGIIWHLIGGASSGSFYAPFKKVKKWSWETMWSVGGIFSWLILPWLIAALLLPDFWAYYSSFSG
STLLPVFLFGALWGIGGITYGLTMRYLGMSLGIGIAIGITLIVGTLMPPIINGNFDVLLATNGGRMTLLG
VLVALIGVAIVGRAGQLKERKMGIKKAEEFNLKKGLILAVMSGIFSACFSFAMDAGKPMHEAAAALGVDP
LYAALPSYVVIMGGGAITNLGFCFIRLAKNKDLSLKADFSLAKPLLITNVLLSALAGVMWYLQFFFYAMG
HSKLGAQYDFVSWMLHMSFYVLCGNLWGLVLKEWKGASRRPVRVLSLGCVVIILAANIVGLGNAL
>gnl|CDD|184091 PRK13500, PRK13500, HTH-type transcriptional activator RhaR
MVFCNNANLLNVFVRHIANNQLRSLAEVATVAHQLKLLKDDFFASDQQAVAVADRYPQDVFAEHTHDFCE
LVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKHSYASVNDLVLQNIIYCPERLKLNLDWQGAIPGFSAS
AGQPHWRLGSVGMAQARQVIGQLEHESSQHVPFANEMAELLFGQLVMLLNRHRYTSDSLPPTSSETLLDK
LITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTE
CGFEDSNYFSVVFTRETGMTPSQWRHLNSQKD
>gnl|CDD|184092 PRK13501, PRK13501, HTH-type transcriptional activator RhaR
MRAPLLLESRDYLLSEQMPVAVTNRYPQETFVEHTHQFCEIVIVWRGNGLHVLNDHPYRITCGDVFYIQA
ADHHSYESVHDLVLDNIIYCPERLHLNAQWHKLLPPLGPEQNQGYWRLTTQGMAQARPIIQQLAQESRKT
DSWSIQLTEVLLLQLAIVLKRHRYRAEQAHLLPDGEQLDLIMSALQQSLGAYFDMADFCHKNQLVERSLK
QLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQRFIR
SPVLPAKNEP
>gnl|CDD|184093 PRK13502, PRK13502, HTH-type transcriptional activator RhaR
MANQLILLKKDFFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRA
EDKHSYTSVNDLVLQNIIYCPERLKLNVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGR
DPLANEMAELLFGQLVMTLKRHRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLR
QQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQ
SD
>gnl|CDD|184094 PRK13503, PRK13503, HTH-type transcriptional activator RhaS
MTVLHSVDFFPSGNAPVAIEPRLPQAAFPEHHHDFHEIVIVEHGTGIHVFNGQPYTLSGGTVCFVRDHDR
HLYEHTDNLCLTNVLYRSPDAFRFLAGLNQLLPQEQDGQYPSHWRVNQSVLQQVRQLVAQMEQQEESNDL
EAIASREILFMQLLVLLRKSSLQENGENSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQ
QTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIRQGRDGFLQ
>gnl|CDD|237402 PRK13504, PRK13504, NADPH-dependent assimilatory sulfite reductase hemoprotein subunit
HPGPLAVEGKLSDVERIKLESNYLRGTIAEELNDGLTGGFSEDDFQLLKFHGSYQQDDRDIRAERAEQKL
EPAYQFMLRCRLPGGVITPQQWLALDKLADEYGNGTLRLTTRQTFQFHGILKKNLKPVIQTINSVLLDTL
AACGDVNRNVMCTPNPYESRLHAEAYEWAKKISDHLLPRTRAYAEIWLDGEKVATFSGTEEEPIYGKTYL
PRKFKIAVAVPPDNDVDVYANDLGFVAIAENGKLVGFNVLVGGGMGMTHGDKETYPRLADELGYVPPEDV
LDVAEAVVTTQRDYGNRTDRKNARLKYTLERVGLDWFKAEVERRAGKKLEPARPYEFTGRGDRLGWVEGI
DGKWHLTLFIENGRIKDYPGRPLKTGLREIAKIHKGDFRLTANQNLIIANVPPSDKAKIEALLREYGLID
GVEESPLRRNSMACVALPTCGLAMAEAERYLPSFIDRIEALLAKHGLSDEHIVIRMTGCPNGCARPYLAE
IGLVGKAPGRYNLYLGGSFNGTRLPKMYRENITEEEILATLDPLLGRWAKEREPGEGFGDFVIRAGIIRE
VLDGARDFH
>gnl|CDD|237403 PRK13505, PRK13505, formate--tetrahydrofolate ligase; Provisional
TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGE
GKSTVTVGLGDALNKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNL
LAALIDNHIHQGNELGIDPRRITWKRVLDMNDRALRNIVVGLGGPANGVPREDGFDITVASEIMAILCLA
TDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFVHGGPFANIAHGC
NSVLATKTALKLADYVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVAKDDLKEEN
VEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGVEVALSEVWAKGGEGGVEL
AEKVVELIEEGESNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKT
QYSFSDDPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDVDEDGNIVGLF
>gnl|CDD|237404 PRK13506, PRK13506, formate--tetrahydrofolate ligase; Provisional
MLSDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEG
KTVTTIGLTQGLNALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLA
AAAIDARLFHEQRLGYDAFEAQSGLPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPEREDGFDI
TAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCL
IHAGPFANIAHGNSSIIADRIALKLADYVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKA
NSGLYDLRPGQALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLL
TGAFGCEISEAFAQGGEGATALAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAK
QQLAQLTALGYDHLPVCMAKTPLSISHDPALKGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLK
PGYLNIDIDADGEIVGLS
>gnl|CDD|184098 PRK13507, PRK13507, formate--tetrahydrofolate ligase; Provisional
MALDPTKMKDWEIAEEAEKFMKPVEELAEELGLTKEELLPYGHYIAKVDFRKVLDRLKDRPDGKYIDVTA
ITPTPLGEGKSTTTMGLVQGLGKRGKKVSGAIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDIN
AIMNAHNLAMVALTARMQHERNYTDEQLARRGLKRLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGY
MMQSGFGIAVSSEVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQ
TIEGQPVFVHAGPFANIAIGQSSIIADRVGLKLADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIV
ATIRALKMHGGGPKVVPGKPLPEEYTKENVGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIA
IVRRLAEQAGARVAVSRHWEKGGEGALELADAVIDACNEPNDFKFLYPLEMPLRERIETIAREVYGADGV
SYTPEAEAKLKRLESDPETADFGTCMVKTHLSLSHDPALKGVPKGWTLPIRDILTYGGAGFVVPVAGDIS
LMPGTGSDPAFRRIDVDTQTGKVKGLF
>gnl|CDD|237405 PRK13508, PRK13508, tagatose-6-phosphate kinase; Provisional
MILTVTLNPSIDISYPLDELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQFIAEH
LDDQIKHAFYKIKGETRNCIAILHEGQQTEILEKGPEISVQEADGFLHHFKQLLESVEVVAISGSLPAGL
PVDYYAQLIELANQAGKPVVLDCSGAALQAVLESPYKPTVIKPNIEELSQLLGKEVSEDLDELKEVLQQP
LFEGIEWIIVSLGADGAFAKHNDTFYKVDIPKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLKKANVLG
MLNAQEKQTGHVNMANYDELYNQIEVKEV
>gnl|CDD|184100 PRK13509, PRK13509, HTH-type transcriptional regulator UlaR
MTEAQRHQILLELLAQLGFVTVEKVIERLGISPATARRDINKLDESGKLKKVRNGAEAITQQRPRWTPMN
IHQAQNHDEKVRIAKAASQLCNPGESVVINCGSTAFLLGRELCGKPVQIITNYLPLANYLIDQEHDSVII
MGGQYNKSQSITLSPQGSENSLYAGHWMFTSGKGLTADGLYKTDMLTAMAEQKMLSVVGKLVVLVDSSKI
GERAGMLFSRADQIDMLITGKNADPEVLQQLEAQGVSILLV
>gnl|CDD|184101 PRK13510, PRK13510, sulfurtransferase complex subunit TusB
MLHTLSRSPWLTDFAALLRLLKEGDDLLLLQDGVTAALKGNRFLESLRNAPIKLYALKEDLIARGLTGQI
SDSIILISYTDFVRLTVKHSQQMAW
>gnl|CDD|184102 PRK13511, PRK13511, 6-phospho-beta-galactosidase; Provisional
MTKTLPKDFIFGGATAAYQAEGATKTDGKGPVAWDKYLEENYWFTPDPASDFYHRYPEDLKLAEEFGVNG
IRISIAWSRIFPDGYGEVNPKGVEYYHRLFAECHKRHVEPFVTLHHFDTPEALHSNGDWLNRENIDHFVR
YAEFCFEEFPEVKYWTTFNEIGPIGDGQYLVGKFPPGIKYDLAKVFQSHHNMMVAHARAVKLFKDKGYKG
EIGVVHALPTKYPIDPDNPEDVRAAELEDIIHNKFILDATYLGYYSEETMEGVNHILEANGGSLDIRDED
FEILKAAKDLNDFLGINYYMSDWMRAYDGETEIIHNGTGEKGSSKYQLKGVGERVKPPDVPTTDWDWIIY
PQGLYDQLMRIKKDYPNYKKIYITENGLGYKDEFVDGKTVDDDKRIDYVKQHLEVISDAISDGANVKGYF
IWSLMDVFSWSNGYEKRYGLFYVDFETQERYPKKSAYWYKKLAETKVIK
>gnl|CDD|184103 PRK13512, PRK13512, coenzyme A disulfide reductase; Provisional
MPKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKYALAYTPEKFYDR
KQITVKTYHEVIAINDERQTVTVLNRKTNEQFEESYDKLILSPGASANSLGFESDITFTLRNLEDTDAID
QFIKANQVDKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNE
EIDAINGNEVTFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIIT
SHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDTIEFKGFLGNNIVKFFDYTFASVGVKPNELKQFDYKM
VEVTQGAHANYYPGNSPLHLRVYYDTSNRKILRAAAVGKEGADKRIDVLSMAMMNQLTVDELTEFEVAYA
PPYSHPKDLINMIGYKAK
>gnl|CDD|184104 PRK13513, PRK13513, ligand-gated channel protein
VNQRFRKTHKAALVIAAAISSQAYAAEKTNTATPTDTMVVTASGFQQRIQDAPASISVVTREQLENKAYR
DVTDALKDVPGVVVTGGGSTSDISIRGMAAKYTLILVDGKRVDTRSTRPNSDGSGIEQGWLPPLAAIERI
EVVRGPMSSLYGSDAMGGVINIITRKVQKEWHGSLRADATLQEDSKSGDIFQTNAYASGPLIDGLLGLKV
SGLLSHRSEDKIIDGYNEQRMRNGTATFSLTPDDNNEFDFEIGRYVQDRNSTPGRTLALNGTNSDTQYDR
NNYAITHNGYYDFGNSTSYIQRDETRNPSRQMKSVDTIFNTQTSFLLDDHTLSLGGQYRYEELYDKGNQL
PSASDLNKLTRWSWALFAEDEWQMTNDFALTGGIRMDQDQNYGTHWTPRLYGVWHLADQWTLKGGVSTGY
RSPDLRQATDNWGQLTGGGGLPALILGNSDLKPEKSISQEIGILWDNQENLNASVTLFNTDFKDKITEVR
NCDTTNTDGQCVFNGINYDFISDRINVDKANMRGVEATFNWDINQAWSLATNYTFTQSEQKSGAFAGQPL
NQMPKHMANATLNWQTTEDFATWIRINYRGKTSEYLNRTSMGSGTPSYTFVDLGASYQLTKELRLMGGVY
NLLDKRVDIDVNDKVLDGRRYMVGASYDF
>gnl|CDD|237406 PRK13515, PRK13515, carboxylate-amine ligase; Provisional
MMAPEFTLGIEEEYLLVDPETRDLRSYPDALVEACRDTLGEQVKPEMHQSQVEVGTPVCATIAEAREELG
RLRQRVAQLAAQFGLRIIAAGTHPFADWRRQEITPKERYAQLVEDLQDVARRNLICGLHVHVGIPDREDR
IDLMNQVRYFLPHLLALSTSSPFWGGRDTGLKSYRSAVFDEFPRTGLPPAFPSWAEYQRYVALLVKTGCI
DDAKKIWWDLRPSPRFPTLELRICDVCTRLDDALALAALFQALVRKLYRLRRQNLTFRVYRRALIEENKW
RAQRYGLDGKLIDFGKQEEVPARELLEELLEFVDDVADALGSRREVEYARTILEEGTSADRQLRVYAETG
GALRAVVDWLIEETLEGLPAP
>gnl|CDD|237407 PRK13516, PRK13516, gamma-glutamyl:cysteine ligase; Provisional
MPLEDFHVSEPFTLGVELELQLVNPHDYDLTQDSSDLLRAVKNQPTAGEIKPEITESMIEIATGVCRDID
QALGQLSAMRDVLVQAADKLNIGICGGGTHPFQQWQRQRICDNPRFQYLSELYGYLAKQFTVFGQHVHIG
CPSGDDALYLLHGLSRYVPHFIALSASSPYVQGVDTGFASARLNSVSAFPLSGRAPFVLNWQEFEAYFRK
MSYTGVIDSMKDFYWDIRPKPEFGTVEVRVMDTPLTLERAAAIAAYIQALARWLLTERPFKPQEDDYLVY
TFNRFQACRFGLEGVLVDPATGERRPLAEDILRTLDRIAPHAEALGASSALEALRRQVKSGLNDAQWLRE
FYADGGSLIELVRQQCERWAGDS
>gnl|CDD|237408 PRK13517, PRK13517, glutamate--cysteine ligase
MRIDFAGSPRPTLGVEWELLLVDPETGELSPRAAEVLAAAGEDDEGPHLQKELLRNTVEVVTGVCDTVAE
ARADLRRTRALARRAAERRGARLAAAGTHPFSDWSEQPVTDKPRYAELIERTQWWARQQLICGVHVHVGV
PSREKVVPVINRLRPWLPHLLALSANSPFWRGEDTGYASNRAMLFQQLPTAGPPPQFGSWAEYEAYVADL
LKTGVILDEGMVYWDIRPSPKLGTVEVRVADVCLTLRELVALAALVRCLVVTADRRLDAGEPLPTLPPWH
VQENKWRAARYGLDAEIIDDADGRERPVTDDLRDLLERLEPVARELGCAEELAGVAEILRRGAGYQRQRR
VAERHGDLRAVVDALVAETREGR
>gnl|CDD|184108 PRK13518, PRK13518, glutamate--cysteine ligase
METGSAEAFTRMGTLGIEEEFFVVDEYGRPTSGTDELVYEHEPPEILAGRLDHELFKFVIETQTPLIEDP
SEAGAALREVRDALVDHAAAHGYRIAAAGLHPAAKWRELEHAEKPRYRSQLDRIQYPQHRNTTAGLHVHV
GVDDADKAVWIANELRWHLPILLALSANSPYWNGFDTGLASARAKIFEGLPNTGMPTAFEDFEAFQRFER
RMVETGSIEDRGELWYDVRPHTGHGTVEVRTPDAQADPDVVLAFVEYVHALVTDLAERYEDGESGTTLRR
ELLDENKWRAMRHGHDASFIDRDGEGTVDLGELVDRECDRLGVDGIRDLYDAESGAQRQRRLLEEEGVDA
LCESLLL
>gnl|CDD|184110 PRK13523, PRK13523, NADPH dehydrogenase NamA; Provisional
SKLFSPYTIKDVTLKNRIVMSPMCMYSSENKDGKVTNFHLIHYGTRAAGQVGLVIVEATAVLPEGRISDK
DLGIWDDEHIEGLHKLVTFIHDHGAKAAIQLAHAGRKAELEGDIVAPSAIPFDEKSKTPVEMTKEQIKET
VLAFKQAAVRAKEAGFDVIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKEVWDGPL
FVRISASDYHPGGLTVQDYVQYAKWMKEQGVDLIDVSSGAVVPARIDVYPGYQVPFAEHIREHANIATGA
VGLITSGAQAEEILQNNRADLIFIGRELLRNPYFPRIAAKELGFEIEAPKQYERAWG
>gnl|CDD|237410 PRK13524, PRK13524, FepA family TonB-dependent siderophore receptor
MNKKIHSLALLVNLGIYGVAQAAEAEDAKTDDTPASHEDTIVVTAAEQNLQAPGVSTITAEDIRKRPPAN
DVSEIIRTMPGVNLTGNSTSGQRGNNRQIDIRGMGPENTLILIDGKPVSSRNSVRYGWRGERDTRGDTNW
VPPEMIERIEVLRGPAAARYGNGAAGGVVNIITKKPTGEWHGSWNTYFNAPEHKAEGATKRTNFSLSGPL
GDELSFRLYGNLNKTQADAWDINQGHQSARTGSYAGTLPAGREGVINKDINGLLRWDFAPLQSLELEAGY
SRQGNLYAGDTQNTNSDALVKSLYGKETNRMYRQNYALTHRGGWDNGVSTSNYAQYEHTRNSRLPEGLAG
GTEGIFNEKATQFSTIDLDDVMLHSEVNLPFDLLVNQTLTLGTEWNQQRMKDPSSNTQALTSGGAIPGVS
ATGRSPYSKAEIFSLFAEDNMELTDSTMLTPGLRFDHHSIVGNNWSPSLNLSQGLGDDFTLKMGIARAYK
APNLYQTNPNYILYSKGQGCYASAGNGCYLQGNDDLKAETSVNKEIGLEFKRDGWLAGLTWFRNDYRNKI
EAGYVPVGTNSVGKTDIYQWENVPKAVVEGLEGTLNVPVSETVNWTNNLTYMLQSKNKTTGDPLSIIPEY
TLNSTLSWQATEDLSLQSTFTWYGKQKPKKYNYKGQPVTGSATKEVSPYSIVGLSATYDVTKNVSLTGGV
DNLFDKRLWREGNAQTTGDLIAGAGAYTYNEPGRTYYMSLNTHF
>gnl|CDD|237411 PRK13525, PRK13525, pyridoxal 5'-phosphate synthase glutaminase subunit PdxT
MMKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREFIA
SGLPVFGTCAGMILLAKEIEGYEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGEPFPAVFIRAPYIE
EVGPGVEVLATVGGRIVAVRQGNILATSFHPELTDDTRVHRYFLEMVKE
>gnl|CDD|184113 PRK13526, PRK13526, glutamine amidotransferase subunit PdxT; Provisional
MTQKVGVLAIQGGYQKHADMFKSLGVEVKLVKFNNDFDSIDRLVIPGGESTTLLNLLNKHQIFDKLYNFC
SSKPVFGTCAGSIILSKGEGYLNLLDLEVQRNAYGRQVDSFVADISFNDKNITGVFIRAPKFIVVGNQVD
ILSKYQNSPVLLRQANILVSSFHPELTQDPTVHEYFLAM
>gnl|CDD|237412 PRK13527, PRK13527, glutamine amidotransferase subunit PdxT; Provisional
MKIGVLALQGDVEEHIDALKRALDELGIDGEVVEVRRPGDLPDCDALIIPGGESTTIGRLMKREGILDEI
KEKIEEGLPILGTCAGLILLAKEVGDDRVTKTEQPLLGLMDVTVKRNAFGRQRDSFEAEIDLSGLDGPFH
AVFIRAPAITKVGGDVEVLAKLDDRIVAVEQGNVLATAFHPELTDDTRIHEYFLKKVKGK
>gnl|CDD|237413 PRK13528, PRK13528, outer membrane receptor FepA; Provisional
MGMRVNKILWLLTVLLVGLNSPVSAAESSDDDNGETMVVEATAEQELKQQPGVSIITAEDIKKRPPVNDL
SDIIRKMPGVNLTGNSASGTRGNNRQIDIRGMGPENTLILIDGVPVTSRNSVRYSWRGERDTRGDTNWVP
PEMVERIEVIRGPAAARYGSGAAGGVVNIITKRPTNDWHGSLSLYTNQPESSKEGATRRANFSLSGPLAG
DALTMRLYGNLNKTDADSWDINSSAGTKNAAGREGVRNKDINGVLSWKMTPQQILDFEAGYSRQGNIYAG
DTQNSNSSAVTESLAKSGKETNRLYRQNYGLTHNGIWDWGQSRLGFYYEKTNNTRMNEGLAGGGEGRITA
DQTFTTSRLESYRTSGELNVPLNWLFEQTLTVGAEWNRDELNDPSSTSLTVKDGDIGGISGSAADRSSKN
KSEISALYVEDNIEPVPGTNLIPGLRFDYHSEFGSNWSPSLNLSQELGDYFKVKAGIARAFKAPNLYQSS
EGYLLYSRGNGCPKDITSGGCYLVGNKNLDPEISVNKEIGLEFTVDDYHASVTYFRNDYQNKIVAGDDVI
GRTASGAYILQWQNGGKAVVEGLEGNLLVPLMKDRLNWNTNATYMITSEQKDTGNPLSVIPKYTINSTLD
WQITQALSANVNWTLYGKQKPRTHAESRSEETGGLSGKELGAYSLVGVNVNYDINKNLRLNVGVSNLFDK
QIYREGEGANTYNEPGRAYYAGVTASF
>gnl|CDD|237414 PRK13529, PRK13529, oxaloacetate-decarboxylating malate dehydrogenase
MKRDEKKKRPLYTPLRGPALLNNPLLNKGTAFTEEEREEFGLEGLLPPAVETLEEQAERAYRQYQSKPTD
LEKHIYLRNLQDRNETLFYRLLSDHLEEMMPIIYTPTVGEACERFSHIYRRPRGLFISYDDRDRIEDILQ
NAPNRDIKLIVVTDGERILGIGDQGIGGMGIPIGKLSLYTACGGIDPARTLPVVLDVGTNNEQLLNDPLY
LGWRHPRIRGEEYDEFVDEFVQAVKRRFPNALLQFEDFAQKNARRILERYRDEICTFNDDIQGTGAVTLA
GLLAALKITGEPLSDQRIVFLGAGSAGCGIADQIVAAMVREGLSEEEARKRFFMVDRQGLLTDDMPDLLD
FQKPYARKREELADWDTEGDVISLLEVVRNVKPTVLIGVSGQPGAFTEEIVKEMAAHCERPIIFPLSNPT
SRAEATPEDLIAWTDGRALVATGSPFAPVEYNGKTYPIGQCNNAYIFPGLGLGVIASGARRVTDGMLMAA
AHALADCVPLAKPGEGALLPPVEDIREVSRAIAIAVAKAAIEEGLARETSDEDLEQAIEDNMWQPEYRPY
RRT
>gnl|CDD|237415 PRK13530, PRK13530, arsenate reductase (thioredoxin)
MNKKTIYFLCTGNSCRSQMAEGWGKQYLGDKWNVYSAGIEAHGVNPNAIKAMKEVGIDISNQTSDIIDND
ILNNADLVVTLCSHADDVCPSTPPHVKRVHWGFDDPAGKEWSEFQRVRDEIGERIKRFAETGE
>gnl|CDD|184118 PRK13531, PRK13531, regulatory ATPase RavA; Provisional
MAHPHLLAERISRLSSALEKGLYERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLKFAFQNARAFE
YLMTRFSTPEEVFGPLSIQALKDEGRYQRLTSGYLPEAEIVFLDEIWKAGPAILNTLLTAINERRFRNGA
HEEKIPMRLLVTASNELPEADSSLEALYDRMLIRLWLDKVQDKANFRSMLTSQQDENDNPVPASLQITDE
EYQQWQKEIGKITLPDHVFELIFQLRQQLDALPNAPYVSDRRWKKAIRLLQASAFFSGRDAIAPIDLILL
KDCLWHDAQSLNLLQQQLEQLMTEHAWQQQGMLTRLGAIVQRRLQLQQQQSDKTALTVIKQGGMFSRKPH
YQLPVNLTASTLTLLLQKPLKLHDMEVNHITFERSALEQWLQKGGEIRGKLNGIGFAQKLNLEVDSAQHL
VVRDVSLQGSTLALPGSSAEGLPGEIKQQLEELESDWRQQHTLFSEQQPCLFIPSDWLARIEASLQQVGE
QIRQAQQC
>gnl|CDD|237416 PRK13532, PRK13532, nitrate reductase catalytic subunit NapA
MKLSRRDFMKANAAAAAAAAAGLSLPAVANAVVGSAQTAIKWDKAPCRFCGTGCGVLVGTKDGRVVATQG
DPDAPVNRGLNCIKGYFLSKIMYGKDRLTQPLLRMKDGKYDKEGEFTPVSWDQAFDVMAEKFKKALKEKG
PTAVGMFGSGQWTIWEGYAASKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAF
VLWGSNMAEMHPILWSRVTDRRLSNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQNN
AVNWDFVNKHTNFRKGATDIGYGLRPTHPLEKAAKNPGTAGKSEPISFEEFKKFVAPYTLEKTAKMSGVP
KEQLEQLAKLYADPNRKVVSFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGTAR
EVGTFSHRLPADMVVTNPKHREIAEKIWKLPEGTIPPKPGYHAVAQDRMLKDGKLNAYWVMCNNNMQAGP
NINEERLPGWRNPDNFIVVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSD
LWQLVEFSKRFKTEEVWPEELLAKKPEYRGKTLYDVLFANGQVDKFPLSELAEGYLNDEAKHFGFYVQKG
LFEEYASFGRGHGHDLAPFDTYHKVRGLRWPVVDGKETLWRYREGYDPYVKAGEGFKFYGKPDGKAVIFA
LPYEPPAESPDEEYDLWLSTGRVLEHWHTGSMTRRVPELYRAFPEAVCFMHPEDAKARGLRRGDEVKVVS
RRGEVKSRVETRGRNKPPRGLVFVPFFDAAQLINKLTLDATDPLSKQTDFKKCAVKIEKV
>gnl|CDD|184122 PRK13535, PRK13535, erythrose 4-phosphate dehydrogenase; Provisional
TIRVAINGFGRIGRNVLRALYESGRRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVG
DDAIRLLHERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNHD
QLRAEHRIVSNASCTTNCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPV
DTKLAAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTEL
PLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGFANRMLDTTLAMAAAG
>gnl|CDD|237419 PRK13536, PRK13536, nodulation factor ABC transporter ATP-binding protein NodI
LLTRAVAEEAPRRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECF
GLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFGR
YFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL
IWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIEIYGGDPHELS
SLVKPYARRIEVSGETLFCYAPDPEQVRVQLRGRAGLRLLQRPPNLEDVFLRLTGREMEK
>gnl|CDD|237420 PRK13537, PRK13537, nodulation factor ABC transporter ATP-binding protein NodI
GPMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEP
VPSRARHARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELS
GGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCV
IEEGRKIAEGAPHALIESEIGCDVIEIYGPDPVALRDELAPLAERTEISGETLFCYVRDPEPLHARLKGR
AGLRYLHRPANLEDVFLRLTGREMQD
>gnl|CDD|184125 PRK13538, PRK13538, cytochrome c biogenesis heme-transporting ATPase CcmA
MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD
EYHQDLLYLGHQPGIKTELTALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVAL
ARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRLGQ
>gnl|CDD|237421 PRK13539, PRK13539, cytochrome c biogenesis protein CcmA; Provisional
MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD
VAEACHYLGHRNAMKPALTVAENLEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALAR
LLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIPLGLPGARELDLGPFAAEDPA
>gnl|CDD|184127 PRK13540, PRK13540, cytochrome c biogenesis protein CcmA; Provisional
MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLC
TYQKQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLR
LWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKADYEEYHL
>gnl|CDD|184128 PRK13541, PRK13541, cytochrome c biogenesis protein CcmA; Provisional
MLSLHQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP
YCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIAC
QSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLESSIKSAQILQLD
>gnl|CDD|184129 PRK13543, PRK13543, heme ABC exporter ATP-binding protein CcmA
MIEPLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI
DGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSA
GQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTL
EAAA
>gnl|CDD|184130 PRK13545, tagH, teichoic acids export protein ATP-binding subunit; Provisional
MNYKVKFEHVTKKYKMYNKPFDKLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLI
AGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQP
VKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFC
TKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQMSVEERKDFREEQISQFQHGLLQEDQTGRERKRKKGK
KTSRKFKKKRVLITGVCIALLTGIISTGYYYKNLLPFNSENKYAEKVASKENVTESKQMVKKEKGAAKYI
VNSNGISIREEADASSKRLAVANFGDIFTISDSNKNEKKDVEWIQITLSNGEIGWISTKFIEPFKSNNNI
IEDAKLADVTALLKRVYGGNMVSAPTYFGKTLNELETTYPQPLNPLPSMTGKTIVKDGNIQFGISQDKVV
EVVFQDISMSIAKLHELLGKESLSNDAEKNYFYETKSYYIAARSDQTHKEIQSISIVKK
>gnl|CDD|184131 PRK13546, PRK13546, teichoic acids export ABC transporter ATP-binding subunit TagH
MNVSVNIKNVTKEYRIYRTNKERMKDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNII
GGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQP
VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFC
TKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKSKAEQKEFRNKLDESRFVIK
>gnl|CDD|184132 PRK13547, hmuV, heme ABC transporter ATP-binding protein
MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNG
EPLAAIDAPRLARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVG
RDVTTLSGGELARVQFARVLAQLWPPHDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLA
IVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCYGFAVRLVDAGDGVPPVIVPA
>gnl|CDD|237422 PRK13548, hmuV, hemin importer ATP-binding subunit; Provisional
AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWS
PAELARRRAVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQ
QRVQLARVLAQLWEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADR
IVLLHQGRLVADGTPAEVLTPETLRRVYGADVLVQPHPETGAPLVLPR
>gnl|CDD|184134 PRK13549, PRK13549, xylose transporter ATP-binding subunit; Provisional
MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEE
LQASNIRDTERAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATP
VGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAIS
DTICVIRDGRHIGTRPAAGMTEDDIITMMVGRELTALYPREPHTIGEVILEVRNLTAWDPVNPHIKRVDD
VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRD
GIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCL
LLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINH
NLTQEQVMEAALRSEH
>gnl|CDD|184135 PRK13551, PRK13551, agmatine deiminase; Provisional
LNSTPKQDGFRMPAEWEPHDAVWMIWPERPDNWRLGGKPAQAAFAKVAEAIARFEPVTMGVSAAQYANAR
ARLPDNVRVVEMSSDDAWVRDTGPTFVINDKGEVRGVDWGFNAWGGLVGGLYFPWDKDDQVAQKVLEIEG
RDRYRAKPFVLEGGSIHVDGEGTLLTTEECLLNPNRNPHLTKEQIEQLLRDYLGVEKVIWLPDGIYNDET
DGHVDNVCCFVRPGEVALAWTDDENDPQYARSKAALEVLENTTDAKGRKLKVHKLPIPGPLYATEEESAG
VDAVEGTVPREAGERLAASYVNFLIANGGIIFPLFDDPNDALALEILQQMFPDRKVVGVPAREILLGGGN
IHCITQQIPAAK
>gnl|CDD|184136 PRK13552, frdB, fumarate reductase iron-sulfur subunit; Provisional
MGRTLTFNIFRYNPQDPGSKPHMVTYQLEETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVIN
GRPTLACRTLTSDYPDGVITLMPLPVFKLIGDLSVNTGKWFREMSERVESWIHTDKEFDIHRLEERMEPE
EADEIYELDRCIECGCCVAACGTKQMREDFVGAVGLNRIARFELDPRDERTDEDFYELIGNDDGVFGCMS
LLGCEDNCPKDLPLQQQIAYLRRKMAATG
>gnl|CDD|237423 PRK13553, PRK13553, fumarate reductase cytochrome b subunit
MEELIEGYLGKSIEGKKSRIPAKLDFLQSATGLFLGLFMWAHMFFVSTILISDDAMYKVAKFFEGSFFFK
AGEPALVSFVAAGVILIFVVHAFLAMRKFPINYRQYQIFRTHKHLMKHGDTSLWFIQAFTGFAMFFLASV
HLYVMLTNPDKIGPYGSSDRVVSQNMWLLYIVLLFAVELHGSIGLYRLAVKWGWFEGKNPKESRKKLKKV
KWALSVFFLVLGLLTLAAYIKIGYENADNGIETYAPTIQADGKFYEET
>gnl|CDD|237424 PRK13554, PRK13554, fumarate reductase cytochrome b-556 subunit; Provisional
MTSKTRVHTAVNTGPFGHPWSAKADKLQSATGIMLGCFLLLHMHFESSILLGKEAFYHVVQFLEGGMFSS
TGHGFPIVTKVFSVFMLLVVIVHAAVALRRFPAQLGQWRALRSHMGSIKHKDTHAWFWQLITGFILFFLV
PVHLFTMILNPEIGPHLSAERVYHDNAWLLYALLLPAVVIHAMIGLYRVAVKWGLTTNRSGLRKVAKVLI
IYLLCLGTLSLVSYIFIGSELTLPVQPFVPQ
>gnl|CDD|184139 PRK13555, PRK13555, FMN-dependent NADH-azoreductase
MSKVLFVKANDRPAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYKRSQGMELT
AEEEKAVATVDQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLAGGKKVVV
LGARGSDYSSEQMAPMEMAVNYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAAKF
>gnl|CDD|184140 PRK13556, PRK13556, FMN-dependent NADH-azoreductase
MSKVLFVKANNRPAEQAVSVKLYEAFLASYKEAHPNDTVVELDLYKEELPYVGVDMINGTFKAGKGFELT
EEEAKAVAVADKYLNQFLEADKVVFAFPLWNFTIPAVLHTYIDYLNRAGKTFKYTPEGPVGLIGDKKVAL
LNARGGVYSEGPAAEVEMAVKYVASMMGFFGVTNMETVVIEGHNQFPDKAEEIITAGLEEAAKVAAKF
>gnl|CDD|237425 PRK13557, PRK13557, histidine kinase; Provisional
MSSPPEPRPHGRAPSVDESAAGDVSDHRSDIFFAAVETTRMPMIVTDPNQPDNPIVFANRAFLEMTGYAA
EEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAGDLVYFFGS
QLDVSRRRDAEDALRQAQKMEALGQLTGGIAHDFNNLLQVMSGYLDVIQAALSHPDADRGRMARSVENIR
AAAERAATLTQQLLAFARKQRLEGRVLNLNGLVSGMGELAERTLGDAVTIETDLAPDLWNCRIDPTQAEV
ALLNVLINARDAMPEGGRVTIRTRNVEIEDEDLAMYHGLPPGRYVSIAVTDTGSGMPPEILARVMDPFFT
TKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAENPEQEPKARAIDRGGTETILI
VDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVDLLFTDLIMPGGMNGVMLAREARRRQPKI
KVLLTTGYAEASIERTDAGGSEFDILNKPYRRAELARRVRMVLDGPTGVG
>gnl|CDD|237426 PRK13558, PRK13558, bacterio-opsin activator; Provisional
EAAVAPTRGVLFVGDDPEAGPVDCDLDEDGRLDVTQIRDFVAARDRVEAGEIDCVVADHEPDGFDGLALL
EAVRQTTAVPPVVVVPTAGDEAVARRAVDADAAAYVPAVSDDATAAIAERIESAVPEHSRDTEARMPISD
LTVESDRRLKERALDEAPVGITIADATLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVA
ELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEAELALQRERRKLQ
RLLERVEGLVNDVTSALVRATDREEIEAAVCDRVGAGGEYDGAWIGEYDPTSGTITVAEAAGGCDGADGD
VLDLAAAGPAAAALQSVVAETEAVESTDVDGVSGTVDGSAVAAVPLVYRETTYGVLVVYTAEPDEIDDRE
RVVLEALGRAVGAAINALESRRTLTTDEVLELEVELSDPDLFLVELAAATDCRLEYRGSIADDDGGVLVL
FTVPGDDATALVDAAADYDAVQDVRVLVSTDDECLVEFTLSGDSLVRLLSERGGRVQDMHADRDRLELTV
EVPTEAAGRAVVETLRDRYAGAELVSYTERDDPGETPDEFRASLENDLTDRQLTALQKAYVSGYFEWPRR
VEGEELAESMGISRSTFHQHLRAAERKLVGAFFDE
>gnl|CDD|237427 PRK13559, PRK13559, hypothetical protein; Provisional
DTPHTREPLHGDLPAASSKAFSADRKELAAIHDPRDFRGASGRLFEQAMEQTRMAMCITDPHQPDLPIVL
ANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPV
YGEDGRLLYFFGSQWDVTDIRAVRALEAHERRLAREVDHRSKNVFAVVDSIVRLTGRADDPSLYAAAIQE
RVQALARAHETLLDERGWETVEVEELIRAQVAPYAPRATRVAFEGPGIRLGAASVQPLGLVLHELAVNAI
KHGALSADQGRISISWKPSPEGAGFRIDWQEQGGPTPPKLAKRGFGTVIIGAMVESQLNGQLEKTWSDDG
LLARIEIPSRQ
>gnl|CDD|106506 PRK13560, PRK13560, hypothetical protein; Provisional
MQSIIDRLTEALRKAREGDCTLLLEVADGGDAIDALGHDVEELQELLRGHAYDARAIAEAEAQDCREQCE
RNLKANIPGGMFLFALDGDGTFSFPSLLDANGELAAIAKHDLMADKGLLAMLIGGDDGDFFFANPFRSAE
TIAMALQSDDWQEEEGHFRCGDGRFIDCCLRFERHAHADDQVDGFAEDITERKRAEERIDEALHFLQQLL
DNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQPADDYQEADAAKFDADGSQIIEAE
FQNKDGRTRPVDVIFNHAEFDDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIEAAPIAAIGLDA
DGNICFVNNNAAERMLGWSAAEVMGKPLPGMDPELNEEFWCGDFQEWYPDGRPMAFDACPMAKTIKGGKI
FDGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLLANLIVENSPLVLFRWK
AEEGWPVELVSKNITQFGYEPDEFISGKRMFAAIIHPADLEQVAAEVAEFAAQGVDRFEQEYRILGKGGA
VCWIDDQSAAERDEEGQISHFEGIVIDISERKHAEEKIKAALTEKEVLLKEIHHRVKNNLQIISSLLDLQ
AEKLHDEEAKCAFAESQDRICAMALAHEKLYQSEDLADIDFLDYIESLTAHLKNSFAIDFGRIDCKIDAD
DGCLDIDKAIPCGLIISELLSNALKHAFPDGAAGNIKVEIREQGDGMVNLCVADDGIGLPAGFDFRAAET
LGLQLVCALVKQLDGEIALDSRGGARFNIRFPMSPAG
>gnl|CDD|184143 PRK13561, PRK13561, putative diguanylate cyclase; Provisional
MAMVAAVVLVFVFIFCTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKADIPEAEAILASIKPAGV
VSRADVVLPNQFQALRKSFIPERPVPVMVTRLFELPVQISLPVYSLERPANPQPLAYLVLQADSFRMYKF
VMSALSTLVTIYLLLSLILTVAISWCINRLIVHPLRNIARELNDIPPQELVGHQLALPRLHQDDEIGMLV
RSYNLNQQLLQRQYEEQSRNATRFPVSDLPNKALLMALLEQVVARKQTTALMIITCETLRDTAGVLKEAQ
REILLLTLVEKLKSVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCS
IGIAMFYGDLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQP
QVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSV
NLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYA
GLRQLQHMKSLPIDVLKIDKMFVDGLPEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQ
GFLFARALPIEIFEERYLEEK
>gnl|CDD|184144 PRK13562, PRK13562, ACT domain-containing protein
MTRILKLQVADQVSTLNRITSAFVRLQYNIDTLHVTHSEQPGISNMEIQVDIQDDTSLHILIKKLKQQIN
VLTVECYDLVDNEA
>gnl|CDD|237428 PRK13564, PRK13564, anthranilate synthase component 1
MQTQKPTLELLTCKAPYREDPTALFHQLCGDRPATLLLESAEIDSKDNLKSLLLVDSALRITCLGNTVTI
QALTDNGAALLPLLDEALPAGVENEQDPNGLVLTFPPVSPLLDEDARLKSLSVFDALRLLQKLVNTPKEE
REALFLGGLFAYDLVAGFEPLPQLPAGNNCPDYCFYLAETLLVIDHQKKSARLQASLFTPDEEEKQRLAA
RLAQLKQQLTQPAPPLPVTSVPDMEVSVNISDEEFCAVVRKLKEHIRAGDIFQVVPSRRFSLPCPSPLAA
YRVLKKSNPSPYMFYMQDEDFTLFGASPESALKYDASSRQVEIYPIAGTRPRGRRADGSIDRDLDSRIEL
ELRTDHKELAEHLMLVDLARNDLARICQPGSRYVADLLKVDRYSHVMHLVSRVVGELRHDLDALHAYRAC
MNMGTLTGAPKVRAMQLIREVEGQRRGSYGGAVGYLTGHGDLDTCIVIRSAFVENGIATVQAGAGVVLDS
DPQSEADETRNKAQAVLRAIATAHHAQETF
>gnl|CDD|237429 PRK13566, PRK13566, anthranilate synthase component I
TVFADPETSSYTTAGGIAVTRSRRETAYGGALDSLIDLLDERRGAVFSSGYEYPGRYTRWDTGFVDPPLE
ITARGRTFTIEALNARGRVLLPFLADTLKALSEVVVLQSTANRIDGTIKEPDAVFTEEERSRQPSVFTVL
RALIALFASEEDPHLGLYGAFGYDLAFQFEPIEQKLPRPDDQRDLVLYLPDEILVVDHYAARAWVDRYEF
AVGGVSTEGLPRETAPSPYKPTTARPGFADHAPGEYAALVEKAKESFRRGDLFEVVPGQTFYEPCERSPS
EIFRRLKEINPSPYGFFINLGDGEYLVGASPEMFVRVEGRRVETCPISGTIKRGADAIGDAEQIRKLLNS
KKDESELTMCTDVDRNDKSRVCEPGSVKVIGRRQIEMYSRLIHTVDHVEGRLRPGFDALDAFLTHAWAVT
VTGAPKLWAMQFIEDHERSPRRWYGGAVGMVGFDGDMNTGLTLRTIRIKDGVAEVRVGATLLFDSDPEAE
EAETELKASALLQALRGAKPKNLSAEEPDAAAVGEGKRVLLVDHEDSFVHTLANYFRQTGAEVTTVRYGF
AEEMLDRVNPDLVVLSPGPGRPSDFDCKATIDAALARNLPIFGVCLGLQAIVEAFGGELGQLAYPMHGKP
SRIRVRGPGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAIEHKTLPVAAVQFHPESIM
TLGGDVGLRIIENVVRLLAG
>gnl|CDD|184148 PRK13567, PRK13567, anthranilate synthase component I; Provisional
MDIFYKKIKANVTPEVLAQLHSKKIILESTNQQQTKGRYSVVIFDIYGTLTLDNDVLSVSTLKESYQITE
RPYHYLTTKINEDYHNIQDEQLKSLPFISGYVGTCSFDLVRHEFPKLQSIQLEDHKQHDVRLYMVEQVYV
FDHYKDELYIIATNQFSNSTKSDLENRVNKSIEDLTKIQPFMPTQDFDFKTKEIQSNISEERFIEMIQYF
KEKITEGDMFQVVPSRIYKYAHHASQHLNQLSFQLYQNLKRQNPSPYMYYLNIDQPYIVGSSPESFVSVK
DQIVTTNPIAGTIQRGETTQIDNENMKQLLNDPKECSEHRMLVDLGRNDIHRVSKIGTSKITKLMVIEKY
EHVMHIVSEVTGKINQNLSPMTVIANLLPTGTVSGAPKLRAIERIYEQYPHKRGVYSGGVGYINCNHNLD
FALAIRTMMIDEQYINVEAGCGVVYDSIPEKELNETKLKAKSLLEVTP
>gnl|CDD|237430 PRK13568, hofQ, DNA uptake porin HofQ
VLQALADYQQLNLVTAPGVGGNLSLRLIEVPWEQALAIILRMGKLSAEREGNVLMVFPEQEIQERQQKTK
QQAAPQEQMLPLANLTLTLQYADAEEVADSLQSQRGGLLSPRGSVTADKRTNTLLIRDTPAALAQLKNWL
IELDLPLQQVQLAAHIVTISSESLQELGVRWGMGEGKQGNTALRINDFNVNLPLPNPAASAGFHLARLGG
RLLDLELSALEQENQVDIIASPRLFTSHQQTASIKQGTEIPYTVSSGKSGSTSIEFKEAVLGMEVTPKIL
RNGRITLKLKISQNMPGRTIKRGEGEMLAIDKQEIQTQVTVKDGETIVLGGIFQQQKRQSVNKVPLLGDI
PLLGALFRQDTQQQSRRELVIFITPKLISAD
>gnl|CDD|184152 PRK13571, PRK13571, anthranilate synthase component I; Provisional
MADGAATTSREDFRALAAEHRVVPVTRKVLADSETPVGAYRKLAANRPGTFLLESAENGRSWSRWSFIGV
GSPAALTVRDGEAVWLGTPPAGAPTGGDPLAALRATLELLATPRLPGLPPLTGGMVGFLGYDAVRRLERL
PELAVDDLGLPEMLLLLATDLAAVDHHEGTITLIANAVNWNGTDERVDAAYDDAVARLDVMTAALAQPLP
STVATFSRPVPEFRAQRTVEEFGAAVEKLVEEIRAGEAFQVVPSQRFEMDTTADPLDVYRVLRVTNPSPY
MYLLRVPNSDGGTDFSIVGSSPEALVTVTDGRATTHPIAGTRWRGATPEEDALLEKELLADPKERAEHLM
LVDLGRNDLGRVCRPGTVRVVDFSHIERYSHVMHLVSTVTGELAEGRTALDAVTACFPAGTLSGAPKVRA
MELIEELEPTRRGLYGGVVGYLDFAGDADTAIAIRTALMRDGTAYVQAGGGVVADSDPDYEDNEARNKAA
AVLRAIAAAETLRAPG
>gnl|CDD|237432 PRK13572, PRK13572, anthranilate synthase component I; Provisional
MLMKKLDYVNPLKLYSVLRDEGYPFILESAEKGQRKARYTYISANPEFMVRIGNKTKVDGETISKESNPF
KALKENFKITQSGDRFTGGFVGYIAYDAVHNYIGGKIEEPSVFGYYDHVFVYDHVTRKFYFHSLNNNPEE
LFNAEKIVEKAKRFEIEEEDGGSEVLGCDADREEFVEMVEKAKEYIYSGDVFQVVLSREYRLKTDLSPFQ
LYRNLREINPSPYMFLLEFDKDVVGASPETMASVENNILKINPIAGTAPRGKTEEEDKKLAEALLSDEKE
RAEHVMLVDLARNDVRKVSKSGSVRLERFFDVVKYSHVQHIESEVVGELKEDSTMFDAIEAAFPAGTLTG
APKFRAMEIIDELEKSRRKVYGGAVGYFSNSGNADLAIAIRMAEIDKVCRVRAGAGIVADSVPEKEFYET
ERKMAAVLKALGVVN
>gnl|CDD|184155 PRK13574, PRK13574, anthranilate synthase component I; Provisional
MEVHPINEFASPFEVFKCIERDFKVAGLLESIGGPQYKARYSVIAWGTNGYLKIHDDPVNILNSYLKDLK
LVDIPGLFKGGMIGYISYDAVRFWEKIRDLKPAAEDWPYAEFFIPDNIIIYDHNEGKVYVNGDLSSVGGC
GDMGEFKISFYDESLNKNNYEKIVSESLEYIRSGYIFQVVLSRFYRYLFSGDPLRIYYNLRRINPSPYMF
YLKFDERYLIGSSPELLFRVQDNIVETYPIAGTRPRGSDQEEDLKLELELMNSEKDKAEHLMLVDLARND
LGKVCVPGTVRVPELMYVEKYSHVQHIVSKVIGTLKKKYNALDVLKATFPAGTVSGAPKPMAMNIIETLE
EYKRGPYAGAVGFISADGNAEFAIAIRTAFLNKDLLRIQAGAGIVYDSNPESEYFETEHKLRALKTAIGV
>gnl|CDD|237433 PRK13576, PRK13576, type I 3-dehydroquinate dehydratase
MRPLIVASLPIKKIEDLKLIGNFLDADLIELRLDYLKDREVSVIEFLDKYKDKLIVTLRDKAEGGINELD
DELKISLLKELYDKQFLYDVEASFLQKYNVPYDNKIVSIHYFDYLPTSEEVKEIVSKFYEKAFSVKIAVL
GLKGYKEVLLPLLEYENVTVMPMSVNPLERIAFSLLGSKLIYSYAIEPTAQGQLHYKKVKQILNYLNNII
TSSSVT
>gnl|CDD|184158 PRK13577, PRK13577, diaminopimelate epimerase; Provisional
MKFYKYHALGNDYLVIDPRDAPFDPSADAIRRICHRHFGVGSDGILFGPLPSEGADFGLRIFNPDGSEAE
KSGNGLRIFSRYLWDQGLVDDEPFTIETKGGIVECQVLDAGRTIQVEMGKVSFGSTDIPVAGEDREVLNE
KLDVDGRRLTYCAATIGNPHCVVLLDEISEELARELGPLIETHPRFPNRTNVQFLKVLDRNTIQIEIWER
GAGYTLASGSSSCAAAAVAHRLGLCDSSITVHMPGGQIDIEIKDDFHVSMTGPVTKVAEGSLSPECLAQL
V
>gnl|CDD|237434 PRK13578, PRK13578, ornithine decarboxylase; Provisional
MKSLKIAASRELPSCFSTHREVVALDQTDFTDVAAVVLSVADSRSGILALIKRTGFGIPVFVATEEEEEV
PAEVLPRISGVFELCESNNEFYGRQLETAASKYEENLLPPFFDTLTDYVEMGNSTFDCPGHQGGQFFRKH
PAGRQFYDFFGENLFRADMCNADVKLGDLLIHEGAAKDAQKHAAKVFNADKTYFVLNGTSASNKVVTNAL
LTPGDLVLFDRNNHKSNHHGALIQAGATPVYLETARNPFGFIGGIDAHCFDEEYLREQIREVAPERADEA
RPFRLAVIQLGTYDGTIYNARQVVDKIGHLCDYILFDSAWVGYEQFIPMMADCSPLLLELNENDPGIFVT
QSVHKQQAGFSQTSQIHKKDNHIKGQARYCPHKRLNNAFMLHASTSPFYPLFAALDVNAKMHEGESGRRL
WMECVKLGIEARKLILARCKLIRPFIPPVVDGKPWQDYPTEQIASDLRFFSFEPGEKWHGFEGYAEDQYF
VDPCKLLLTTPGIDAETGEYEDFGIPATILANYLRENGIVPEKCDLNSILFLLTPAEDMAKLQQLVAMLA
RFEKHIEDDAPLAEVLPSVYKKNPERYRGYTLRQLCQEMHDLYVSHDVKQLQKEMFRKASFPRVVMNPQD
ANIAYIRGEVELVRLSEAEGRIAAEGALPYPPGVLCVVPGEIWGGAVQRYFLALEEGINLLPGFAPELQG
VYLETDADGRKRAYGYVLKP
>gnl|CDD|237435 PRK13579, gcvT, glycine cleavage system aminomethyltransferase GcvT
MMMDDTSPLKTLPLHALHLAAGARMVPFAGYDMPVQYPAGVLKEHLHTRAHAGLFDVSHMGQIEVSGKDA
AAALERLVPVDILALKEGRQRYTFFTNEQGGILDDLMVTNLGDHLFLVVNAACKDADIAHLREHLSDECE
VNPLDDRALLALQGPEAEAVLADLGPPVAALRFMDGFEPRLHGVDCFVSRSGYTGEDGFEISVPADAAEA
LAEALLADPRVEPIGLGARDSLRLEAGLCLYGHDIDTTTTPVEAALEWAIQKARREAGGFPGAKAILAAL
AKGASRRRVGLKPEGRAPVREGAPLFDDAGTEIGTVTSGGFGPSVGGPVAMGYVPASLAAPGTAVFAEVR
GKRLPVTVHALPFVPHRYKR
>gnl|CDD|184161 PRK13580, PRK13580, glycine hydroxymethyltransferase
SLLDKALLNASGKDQQNLASTAYLAALDVILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMG
NLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAYVQPHSGADANLVAFWAILAHKVESPA
LEKLGAKTVNDLTEEDWEALRAELGNQRLLGMSLDSGGHLTHGFRPNISGKMFHQRSYGVDPDTGLLDYD
EIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFTGDEDPVPHADIV
TTTTHKTLRGPRGGLVLAKKEYADAVDKGCPLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNARA
LAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTP
ALTTLGMGSDEMDEVAELIVKVLSNTTPGTTAEGAPSKAKYELDEGVAQEVRARVAELLARFPLYPEIDL
ETL
>gnl|CDD|237437 PRK13582, thrH, bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH
MEIVCLDLEGVLVPEIWIAFAEKTGIPELRATTRDIPDYDVLMKQRLDILDEHGLGLADIQEVIATLDPL
PGAVEFLDWLRERFQVVILSDTFYEFAGPLMRQLGWPTLFCHSLEVDEDGMITGYDLRQPDGKRQAVKAL
KSLGYRVIAAGDSYNDTTMLGEADAGILFRPPANVIAEFPQFPAVHTYDELLAAIDKASARALSL
>gnl|CDD|184165 PRK13585, PRK13585, 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
MSFEVIPAVDMKGGKCVQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEK
IIEAVGVPVQLGGGIRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAKDGEVVI
KGWTEKTGYTPVEAAKRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLRA
LKEAGAAGVVVGSALYKGKFTLEEAIEAVKG
>gnl|CDD|237439 PRK13586, PRK13586, 1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase
MSKIIPSIDISLGKAVKRIRGVKGTGLILGNPIEIASKLYNEGYTRIHVVDLDAAEGVGNNEMYIKEISK
IGFDWIQVGGGIRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVSIDYDNTKRVLIRG
WKEKSMEVIDGIKKVNELELLGIIFTYISNEGTTKGIDYNVKDYARLIRGLKEYAGGVSSDADLEYLKNV
GFDYIIVGMAFYLGKLRGINVV
>gnl|CDD|172156 PRK13587, PRK13587, 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
MIELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQFECVNRIHIVDLIGAKAQHAREFDYIKS
LRRLTTKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVN
GWEEDTELNLFSFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRL
ASLNVHAAIIGKAAHQASFWEGLS
>gnl|CDD|237440 PRK13588, PRK13588, flagellin B; Provisional
MSFRINTNIAALNAHAVGVQNNRDLSSSLEKLSSGLRINKAADDASGMAIADSLRSQSANLGQAIRNAND
AIGMVQTADKAMDEQIKILDTIKTKAVQAAQDGQTLESRRALQSDIQRLLEELDNIANTTSFNGQQMLSG
SFSNKEFQIGAYSNTTVKASIGATSSDKIGHVRMETSSFSGEGMLASAAAQNLTEVGLNFKQVDGVNDYK
IETVRISTSAGTGIGALSEIINRFSDTLGVRASYNVMATGGTPVQSGTVRELTINGVEIGTVNDVHKNDA
DGRLINAINSVKDRTGVEASLDIQGRINLTSIDGRAISVHAASASGQVFGGGNFAGISGTQHAVVGRLTL
TRTDARDIIVSGVNFSHVGFHSAQGVAEYTVNLRAVRGIFDANVASAAGANANGAQAETNSQGIGAGVTS
LKGAMIVMDMAESARTQLDKIRSDMGSVQMQLVSTINNISVTQVNVKAAESQIRDVDFAEESANFSKYNI
LAQSGSFAMAQANAVQQNVLRLLQ
>gnl|CDD|172158 PRK13589, PRK13589, flagellin A
MGFRINTNIGALNAHANSVVNSRELDKSLSRLSSGLRINSAADDASGMAIADSLRSQAATLGQAINNGND
AIGILQTADKAMDEQLKILDTIKTKATQAAQDGQSLKTRTMLQADINRLMEELDNIANTTSFNGKQLLSG
NFTNQEFQIGASSNQTIKATIGATQSSKIGVTRFETGGRSFTSGEVQLTIKNYNGIDDFKFQKVVISTSV
GTGLGALAEEINKSADKTGVRATFTVETTGVAAIKAGTTSQDFAINGVTIGQVAYKDGDGNGALVSAINS
VKDTTGVEASKDANGQLVLTSRDGRGIKIDGNIGGGAGILANMKENYGRLSLVKNDGKDILISGTNLSAI
GMGATDMISQASVSLRESKGRIDANIADAMGFNSYKGGGKFVVTGGFSSVSAFMSSEGSGFSRGSGYSVG
SGKNYSVGLSQGIQIISSASAMSTVYNVSAGSGFSSGSGLSQFATMKTTAAGVKDETAGVTTLKGAMAVM
DIAETAITNLDQIRADIGSVQNQLQVTINNITVTQVNVKAAESTIRDVDFAAESANFSKYNILAQSGSYA
MSQANAVQQNVLKLLQ
>gnl|CDD|184168 PRK13590, PRK13590, putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional
MALTLEQLNAASAAEATALLDGLYEHSPWIAERALAQRPFRSLAQLKHALVQVVREAGRDAQLGLIRAHP
ELAGKAMVAGSLTAESTHEQGKAGLTHCTPEEFARIQQLNADYNARFGFPFILAVRGPRGLGLSRQEIIA
TFARRLDNHPDFELAEALRNIHRIAEIRLNDKFGAEPVLGNDVWDWAERLAAHSDPGYAEKGQLTVTYLT
DAHRACAQQISHWMRDCGFDEVHIDAVGNVVGRYKGSTPQAKRLLTGSHYDTVRNGGKYDGRLGIFVPMA
CVRELHRQGRRLPFGLEVVGFAEEEGQRYKATFLGSGALIGDFDPAWLDQKDADGITMREAMQHAGLCID
DIPKLRRDPARYLGFVEVHIEQGPVLNELDLPLGIVTSINGSVRYVGEMIGMASHAGTTPMDRRRDAAAA
VAELALYVEQRAAQDGDSVGTVGMLEVPGGSINVVPGRCRFSLDIRAPTDAQRDAMVADVLAELEAICER
RGLRYTLEETMRAAAAPSAPAWQQRWEAAVAALGLPLFRMPSGAGHDAMKLHEIMPQAMLFVRGENAGIS
HNPLESSTADDMQLAVQAFQHLLDQLAAEQP
>gnl|CDD|184169 PRK13591, ubiA, prenyltransferase; Provisional
MGFNVFSGSFERIFKRRRKNSNMYKFLNATFELLNSSTLVAFSGALRIHIAFLLLGLQSSILTCIAGGLI
IYSVYTLDRALDSEEDAVNRSELIGSNKKIGLLVSLLAFLLGTYILAMDGMLLLAFLPFITGYLYSKGIK
IGKFALKLKGGLGVKNIVVGITWGGFIAGIAGSYCGSLIPVGLIFLFFGVKLFINSCVYDFKDVKGDTLA
GIKTLPVSLGEQKTRNLLLGIHLFSHLVLGIALIFGVIAFEPIILLYSFVCGLICIQVYSSPFENEPSFR
KLERTVLVDGESTSIVGLRTIRGCLIA
>gnl|CDD|139690 PRK13592, ubiA, prenyltransferase; Provisional
MIKRLNVYLKEMYPLLPRLILSLTLFFEIYMITLLSNHISSFRIGIQEFVGVFTVFGFWMILRIADDFKD
YETDRRLFPHRALPSGRVKKKDLAIALSFIVAVSVLLNVLFMNNVGWFLFLYIYGTLMSFWFFKRDKIQN
SLPLALVTHNPVMMILNLYTISFVCYKYNLPLLSLPTVLLAFTMYFPSLIWEVCRKIRAPKDETEYVTYS
KLFGYKKATRFIEVVTLLDILTNFALLWNISHVGVVVLVLNVIWMTVQFEQFIKSPTRFNIRERVERYTY
ITETTMVLSVAVYLLMGVL
>gnl|CDD|172161 PRK13595, ubiA, prenyltransferase; Provisional
MRIAPLGILLPLRRLLLISRPALWVNTVGTLVTGVWLTGHLYTLDPGVLPLLLYLTLPFNLLIYGLNDLA
DRETDAASPRKGGWQGARLSPGEVRPLLRAVLLLNAPFLLYLALLLPPAATLLLLLYAALFVGYSLPPLR
FKARPFLDGLSNAAYALPLALPALALGAPVPWPPLLALMAWSVGKHAFDAAQDIPADRAAGTRTVATTLG
VRGTALYALAWFLLAGALLWPVSRLTALALWLICGGMALALWRRPTPETAHRLYPLSIVTPWIVGTVAGV
LLVAALVRGGYP
>gnl|CDD|237441 PRK13596, PRK13596, NADH-quinone oxidoreductase subunit NuoF
MLKDKDRIFTNLYGLQDWSLKGAKKRGDWDGTKAILDKGRDWIIEEMKASGLRGRGGAGFPTGLKWSFMP
KESDGRPHYLVVNADESEPGTCKDRDILRHDPHKLIEGCLIASFAMGAHAAYIYIRGEFIREREALQAAI
DEAYEAGLIGKNACGSGWDFDIYVHHGAGAYICGEETALLESLEGKKGQPRLKPPFPANVGLYGCPTTVN
NVESIAVVPTILRRGAAWFASIGRPNNTGTKLFCISGHVNKPCNVEEAMGIPFRELIEKHAGGVRGGWDN
LLAVIPGGSSVPLIPAEQCEDAIMDFDSLRAVGSGLGTAAVIVMDKSTDIIKAIARLSYFYKHESCGQCT
PCREGTGWMWRVMERMVKGRAQKREIDMLLDVTKQIEGHTICALGDAAAWPIQGLIRHFRPEIEERIDQY
TANAHSDPLEAAE
>gnl|CDD|184171 PRK13598, hisB, imidazoleglycerol-phosphate dehydratase; Provisional
MSRNANITRETKETKIEVFLDIDRKGEIKVSTPVPFFNHMLITLLTYMNSTATVSATDKLPYDDHHIVED
VAITLGLAIKEALGDKRGIKRFSHQIIPMDEALVLVSLDISGRGMAFVNLNLKRSEIGGLATENIPHFFQ
SFAYNSGVTLHISQLSGYNTHHIIEASFKGLGLALYEATRIVDNEIRSTKGVL
>gnl|CDD|106544 PRK13599, PRK13599, peroxiredoxin
MKLLGEKFPSMEVVTTQGVKRLPEDYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSV
DQVFSHIKWVEWIKDNTNIAIPFPVIADDLGKVSNQLGMIHPGKGTNTVRAVFIVDDKGTIRLIMYYPQE
VGRNVDEILRALKALQTADQYGVALPEKWPNNYLIKDHVIVPPSTDEASANERKEKIKSKEIEAFDWWFV
HKPLK
>gnl|CDD|184172 PRK13600, PRK13600, putative ribosomal protein L7Ae-like; Provisional
MSKEKVARFNKQHFVVGLKETLKALKKDQVTSLIIAEDVEVYLMTRVLSQINQKNIPVSFFKSKHALGKH
VGINVNATIVALIK
>gnl|CDD|184173 PRK13601, PRK13601, putative L7Ae-like ribosomal protein; Provisional
AGQDCPSKRVVGAKQTLKAITNCNVLQVYIAKDAEEHVTKKIKELCEEKSIKIVYIDTMKELGVMCGIDV
GAAAAADIIGEK
>gnl|CDD|184174 PRK13602, PRK13602, 50S ribosomal protein L7ae-like protein
MSYEKVSQAKSIVIGTKQTVKALKRGSVKEVVVAEDADPRLTEKVEALANEKGVPVSKVDSMKKLGKACG
IEVGAAAVAIIK
>gnl|CDD|172166 PRK13603, PRK13603, fumarate reductase subunit C; Provisional
MSAYRQPVERYWWARRRSYLRFMLREISCIFVAWFVLYLVLVLRAVGAGGNSYQRFLDFSANPVVVVLNV
VALSFLLLHAVTWFGSAPRAMVIQVRGRRVPARAVLAGHYAAWLVVSVIVAWMVLS
>gnl|CDD|184175 PRK13604, luxD, acyl transferase; Provisional
MKNESSFKTIDHVICLENGQSIRVWETLPKENSPKKNNTILIASGFARRMDHFAGLAEYLSSNGFHVIRY
DSLHHVGLSSGTIDEFTMSIGKNSLLTVVDWLNTRGINNLGLIAASLSARIAYEVINEIDLSFLITAVGV
VNLRDTLERALGYDYLSLPIDELPEDLDFEGHNLGSEVFVTDCFKHGWDTLDSTINKMKGLDIPFIAFTA
NNDSWVKQSEVIDLLDSIRSEQCKLYSLIGSSHDLGENLVVLRNFYQSVTKAAIALDNGSLDLDVDIIEP
SFEDLTSATVKERRLKNEIENEALELA
>gnl|CDD|237442 PRK13605, PRK13605, endoribonuclease SymE; Provisional
MTDTHSIAQPFEAEVSPTNNRQLTVSYASRYPDYSRIPAITLKGQWLEAAGFATGTAVDVRVMEGCIVLT
AQPPAAEESELMQSLRQVCKLSARKQKQVQEFIGVIAGKQKVA
>gnl|CDD|237444 PRK13607, PRK13607, proline dipeptidase; Provisional
MESLASLYKEHIATLQQRTRDALAREGLDALLIHSGELHRVFLDDHDYPFKVNPQFKAWVPVTQVPNCWL
LVDGVNKPKLWFYQPVDYWHNVEPLPESFWTEEVDIKALTKADGIASLLPADRGNVAYIGEVPERALALG
FEASNINPKGVLDYLHYHRAYKTDYELACMREAQKIAVAGHRAAKEAFRAGMSEFDINLAYLTATGQRDN
DVPYGNIVALNEHAAVLHYTKLDHQAPAEMRSFLIDAGAEYNGYAADITRTYAAKEDNDFAALIKDVNKE
QLALIATMKPGVSYVDLHIQMHQRIAKLLRKFQIVTGLSEEAMVEQGITSPFFPHGLGHPLGLQVHDVAG
FMQDDRGTHLAAPEKHPYLRCTRVLEPGMVLTIEPGLYFIDSLLAPLREGPFSKHFNWQKIDALKPFGGI
RIEDNVVVHENGVENMTRDLKLA
>gnl|CDD|184179 PRK13608, PRK13608, diacylglycerol glucosyltransferase; Provisional
MVTQNKKILIITGSFGNGHMQVTQSIVNQLNDMNLDHLSVIEHDLFMEAHPILTSICKKWYINSFKYFRN
MYKGFYYSRPDKLDKCFYKYYGLNKLINLLIKEKPDLILLTFPTPVMSVLTEQFNINIPVATVMTDYRLH
KNWITPYSTRYYVATKETKQDFIDVGIDPSTVKVTGIPIDNKFETPIDQKQWLIDNNLDPDKQTILMSAG
AFGVSKGFDTMITDILAKSANAQVVMICGKSKELKRSLTAKFKSNENVLILGYTKHMNEWMASSQLMITK
PGGITISEGLARCIPMIFLNPAPGQELENALYFEEKGFGKIADTPEEAIKIVASLTNGNEQLTNMISTME
QDKIKYATQTICRDLLDLIGHSSQPQEIYGKVPLYARFFVK
>gnl|CDD|237445 PRK13609, PRK13609, diacylglycerol glucosyltransferase; Provisional
MIKNPKVLILTAHYGNGHVQVAKTLEQTFRQKGIKDVIVCDLFGESHPVITEITKYLYLKSYTIGKELYR
LFYYGVEKIYDKKIFSWYANFGRKRLKLLLQAEKPDIVINTFPIIAVPELKKQTGISIPTYNVLTDFCLH
KIWVHREVDRYFVATDHVKKVLVDIGVPPEQVVETGIPIRSSFELKINPDIIYNKYQLCPNKKILLIMAG
AHGVLGNVKELCQSLMSVPDLQVVVVCGKNEALKQSLEDLQETNPDALKVFGYVENIDELFRVTSCMITK
PGGITLSEAAALGVPVILYKPVPGQEKENAMYFERKGAAVVIRDDEEVFAKTEALLQDDMKLLQMKEAMK
SLYLPEPADHIVDDILAENHVEPNLAQSFT
>gnl|CDD|139699 PRK13610, PRK13610, photosystem II reaction center protein Psb28; Provisional
MTKINENVAIQFVKGENEKDQPEIRLFRNLDGKKGKAVYKFYKPKTITLTNYKSVQRMFLIDSEGVLSTK
KIDLSISEDHVKEVKSTYNWNSEEAFERFMRFASRYANSLSKN
>gnl|CDD|106556 PRK13611, PRK13611, photosystem II reaction center protein Psb28; Provisional
MASIEFSPGIPEVPTQVRLLKSKTGKRGSAIFRFEDLKSDTQNILGMRMIDEEGELTTRNIKAKFLNGEF
KALEVIYDMETEAEWDRFLRFMERFSAANQMGMA
>gnl|CDD|237446 PRK13612, PRK13612, photosystem II reaction center protein Psb28; Provisional
NKMAAIQFSRGVDEPVVPDIRLTRSRDGRTGQATFYFEQPQALAPETTGEITGMYMIDEEGEIVTREVKA
KFVNGKPSALEATYIWKSEQEWDRFMRFMERYAKENGLGFSKS
>gnl|CDD|237447 PRK13613, PRK13613, lipoprotein LpqB; Provisional
DRTPGGRGRAMRAAAAAGCGVVLLAGCASVPTSGDVRGVESTPRQDPQVRVFPAPPREGAAPAEIVQGFL
EALTSFDPDYETARKYLTGDAAKSWRPGGSVTVLAGAPTVSADREGDREGDDATVTLTGTRVATIDEDGQ
YVPASGGYYTDVHLTLQDKTGQWRIDRLPDGLVLSQSDVERNYRSVNLYYFASDGPVLVPDPVYLPVSVQ
DLATQLVRALLAGPTTWLAPVVRSSFPTGTALRKVPDDQNVLTVPLNHKADRAGPARCFGMAAQLLWTLQ
DLPEIQVFTLRIDGEEVELPGSEGEQLCALSEDEANSVASHGGTESPDYYYFIDGQLWLLRISGTSNGTD
PEPVPGALGSGRVPLRRVAVSRDESRAAGISADGDSVYVGSLTPGASIGVHSWGVTADGRLTSPSWDGRG
DLWVVDRDPADPRLLWLLQGDGEPVEVRTPELDGHRVVAVRVARDGVRVALIVEKDGRRSLQIGRIVRDA
KAVVSVEEFRSLAPELEDVTDMSWAGDSQLVVLGREEGGVQQARYVQVDGSTPPASAPAAVTGVESITAS
EDERLPLVAGTSEDGIVRLSSGLQWQTVVKEGTAPVYPG
>gnl|CDD|237448 PRK13614, PRK13614, lipoprotein LpqB; Provisional
GAPRRTRCASAALLVLLVVTLSACAQIPRSGPVGKVISTDGSAGQLNAPVFFPAAPRPGASPETVIEGFY
AAGSGYEDDYAVARQYLTQAAATTWKPDQRTLVFRDNPRVVKTGNENEYNYELDVAYSVDADGIATQFPE
GTKETIPVTLTQVDGEWRISKIPDGIAIPEQTFKVIFGAYPLYFYDPSFTYAVPDVRWFIKKKTVSTAMV
SALLSGPAPYLKGAVASAFPSGIKLARESVPVVSGTATVDLSAKELDEASAEDRQRMQQQLQLTLRAQPD
VVNVELRANQDLVDVEDNSGSVLPPVRDKSVPNRQIGVSDGELVRYENGQISPLPDIQSVAGLGPASPAE
SPVSQTVAFLNGSRTTLYTVSPGQPARALTSGSTLTRPSFSPQDWVWTAGPGGNGRIVAYRPTGVAEGAQ
APTVTLTADWLAGRTVKELRVSREGVRALVISEQNGKSRVQVAGIVRNEDGTPRELTAPITLAADSDADT
GAWVGDSTVVVTKASATSNVVPELLSVDAGQPQQLAPWTGLTSITVGNGPEEVYGQSDGGIFQRLGNGWS
LQLKDPTDPSFAG
>gnl|CDD|184183 PRK13615, PRK13615, lipoprotein LpqB; Provisional
MVAAALVASLVVLLAACASIPDSGPVSEGDPATVTDESGVSYQPDGPQAGDGPDDVIAGFVDAATSSADQ
YGVARQFLSSDFASRWDPFASVVVWEGQARTSEEVDGTYSYSVTTIATVDGQGHYREVGSDQETRLSFQL
VQERGEWRIAKAPDGIALRSTYFREIFSAHALYFFDPTFSFLVPDLRFFVTRASQSVSTRIVKSLLQGPS
PWLSQPAVVTAFPEGTQLASSAVTTAGGTPQVDLSTEARAADGVTQQRMKLQLRQSLSNIPSVLDVQMLV
DGTPLQVADLGGRGPVKDPQAESRPLVLAQGQFGYLGGGTVTPLGTLGTRVTALQADAATLSADGRQAAV
RNASGVWSVGDGDRDAVLLDTRPGLVAPSLDAQGYVWSTPASDPRGLVAWGPDGVGHPVAVSWTATGRVV
SLEVARDGARVLVQLETGAGPQLLVASIVRDGGVPTSLTTTPLELLASPGTPLDATWVDELDVATLTLAP
DGERQVELHQVGGPSKDMGSAADGVSITGANDESGLRVLTSAGALLTPRGSTWQQTATGVSFVATKR
>gnl|CDD|237449 PRK13616, PRK13616, MtrAB system accessory protein LpqB
SRISRRLKLLAALLAVAALLAGCATLPSSSAPQAIGTVERPAPSNEVPKPTPGMDPDLLLRDFLKASADP
ANRHLAARQFLTESASNAWDDAGSALVIDRIDFNESTRSADRVTYTIRANIVGSLSDGGVFEPANGSLET
PIELVKVDGEWRIDRLPDGVVLDRQQFQNTYRRKTLYFADPTGRTLVPDPRWVAVSQDQLATELVSLLIA
GPRPELAPAVRNLLPPGASLRGPVTRADGGKSGVGVGYGGARVDFTGLSTLDPDSRQLLAAQVVWTLARA
DVRGPYVLNADGAPLDDRFAEGWTTSDVAETDPGAADGAAAGLHALVDGSLVSVDGQGVTPVPGAFGQMG
NITSAALSRSGRQVAAVVTLGRGAPDPASSLWVGPLGGVAVQVLEGHSLTRPSWSLDADAVWVVVDGNTV
VRVIRDPATGQLARTPVDASAVASRVPGPISELQLSRDGVRAAMIIGGKVYLAVVEQTEDGQYALTNPRE
VGPGLGDTAVSLDWRTGDSLVVGRSDPEHPVWYVNLDGSNSDALPSRNLSAPVVAVAASPSTVYVTDARA
VLQLPNSDSGDQYWREVPGLMGPRAAPVLPG
>gnl|CDD|139707 PRK13620, psbV, cytochrome c-550; Provisional
MVNIEDGFGCLWLLQIILPCSQTASTSSSHWAGESCPFRELVRSSSPSMVFKTLRRTLWLTLAALLAVFQ
FNLGAAQAAELTAETRTVKLNPQGDNVTLSLKQVAEGKQLFAYACGQCHVGGITKTDPNVGLDPEALALA
TPPRDSVESLVDYLHNPTTYDGEREISELHPSTKSTDIFPKMRNLTEDDLVAISGHILLQPKIVGTKWGG
GKIYY
>gnl|CDD|237450 PRK13621, psbV, cytochrome c-550; Provisional
RRAMRLRSPSILWLLGGLLILQWAGDTSPAAARVDPYVKRYLKVTEPVELPLDAAGETQTFSPEQLTDGK
QLFDSNCLNCHVGGATLPNPNVSLSLKDLRGATPPRDNIAALVAYQRDPMSYDGSEESYGCRQVPEDWMT
DEELQNLAAFILRAAQKAPGWGTEAVEDGQ
>gnl|CDD|184186 PRK13623, PRK13623, iron-sulfur cluster insertion protein ErpA; Provisional
MMSDDVPLPLVFTDAAAAKVKELIEEEGNPDLKLRVYITGGGCSGFQYGFTFDEQVNEDDTTIEKQGVTL
VVDPMSLQYLVGAEVDYTEGLEGSRFVIKNPNAKTTCGCGSSFSI
>gnl|CDD|184187 PRK13625, PRK13625, bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
MKYDIIGDIHGCYQEFQALTEKLGYNWSSGLPVHPDQRKLAFVGDLTDRGPHSLRMIEIVWELVEKKAAY
YVPGNHCNKLYRFFLGRNVTIAHGLETTVAEYEALPSHKQNMIKEKFITLYEQAPLYHILDEGRLVVAHA
GIRQDYIGRQDKKVQTFVLYGDITGEKHPDGSPVRRDWAKEYKGTAWIVYGHTPVKEPRFVNHTVNIDTG
CVFGGRLTALRYPEMETVSVPSSLPFVPEKFRPIS
>gnl|CDD|184188 PRK13626, PRK13626, HTH-type transcriptional regulator SgrR
MPSARLQQQFIRLWQCCEGKSQETTLNELAELLNCSRRHMRTLLNTMQQRGWLTWQAEAGRGKRSRLTFL
YTGLALQQQRAEDLLEQDRIDQLVQLVGDKAAVRQMLLSHLGRSFRQGRHILRVLYYRPLRNLLPGSALR
RSETHIARQIFSSLTRINEENGELEADIAHHWQQISPLHWRFYLRPAIHFHHGRELEMEDVIASLKRLNT
LPLYSHIAKIVSPTPWTLDIHLSQPDRWLPWLLGSVPAMILPQEWETLPNFASHPIGTGPYAVIRNTTNQ
LKIQAFDDYFGYRALIDEVNIWVLPEISEEPVGGLMLQGDQTGEKELESRLEEGCYYLLFDSRSPRGANP
QVRRWLSYVLSPINLLYHADEQYQRLWFPAYGLLPRWHHARLTIPSEKPAGLESLTLTFYQDHSEHRVIA
GIMQQLLASHGVTLEIQEIDYDQWHQGEAESDIWLNSANFTLPLEFSLFAHLYEVPLLQHCIPIDWQADA
ARWRNGELNLANWCQQLVASKALHPLFHHWLILQGQRSMRGVRMNTLGWFDFKSAWFAPPDP
>gnl|CDD|184189 PRK13627, PRK13627, carnitine operon protein CaiE; Provisional
MSYYAFEGLIPVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMHGYCDT
DTIVGENGHIGHGAILHGCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKRQLLMGTPARA
VRSVSDDELHWKRLNTKEYQDLVGRCHASLHETQPLRQMEENRPRLQGTTDVTPKR
>gnl|CDD|184190 PRK13628, PRK13628, serine/threonine transporter SstT; Provisional
MQQMSGLLRRLARGSLVKQILIGLVLGILLALLSPPAAEAVGLLGTLFVGALKAVAPILVFVLVMASIAN
HKKGQKTNIRPILVLYLLGTFLAALVAVVASFLFPSTLVLVASAADISPPQGIVEVLKTLLLSLVDNPIN
ALLNANYIGILAWAIGLGLALRHASDTTKNVVNDLSEAVSQIVKWVIRFAPIGIFGLVASTLAETGFSAL
AGYAQLLAVLVGCMLFVALVVNPLIVFWKIRRNPYPLVFTCLRESGVTAFFTRSSAANIPVNMALCEKLG
LDEDTYSVSIPLGATINMAGAAITITVLTLAAVHTLGIPVDLPTALLLSVVAAISACGASGVAGGSLLLI
PLACSLFGISNDIAMQVVAVGFIIGVLQDSAETALNSSTDVLFTAAACQAED
>gnl|CDD|184191 PRK13629, PRK13629, threonine/serine transporter TdcC; Provisional
MSTSDSIVSSQTKQSSWRKSDTTWTLGLFGTAIGAGVLFFPIRAGFGGLIPILLMLVLAYPIAFYCHRAL
ARLCLSGSNPSGNITETVEEHFGKTGGVVITFLYFFAICPLLWIYGVTITNTFMTFWENQLGFAPLNRGF
VALFLLLLMAFVIWFGKDLMVKVMSYLVWPFIASLVLISLSLIPYWNSAVIDQVDLGSLSLTGHDGILVT
VWLGISIMVFSFNFSPIVSSFVVSKREEYEKDFGRDFTERKCSQIISRASMLMVAVVMFFAFSCLFTLSP
QNMAEAKAQNIPVLSYLANHFASMTGTKSTFAITLEYAASIIALVAIFKSFFGHYLGTLEGLNGLILKFG
YKGDKTKVSLGKLNTISMIFIMGSTWVVAYANPNILDLIEAMGAPIIASLLCLLPMYAIRKAPSLAKYRG
RLDNVFVTVIGLLTILNIVYKLF
>gnl|CDD|237451 PRK13631, cbiO, cobalt transporter ATP-binding subunit; Provisional
LMDYFMKKKLKVPNPLSDDIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVT
HFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKNFKELRRRVSMVFQFPEYQLFKDTIEKDIMF
GPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK
GEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIINSTSIQVPRV
IQVINDLIKKDPKYKKLYQKQPRTIEQLADAINEFIKGGK
>gnl|CDD|237452 PRK13632, cbiO, cobalt transporter ATP-binding subunit; Provisional
IKNKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG
ITISKENLKEIRKKIGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEP
QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILAD
KVIVFSEGKLIAQGKPKEILNNKEILEKAKIDSPFIYKLSKKLKGIDPTYNEEELIEQICK
>gnl|CDD|237453 PRK13633, PRK13633, energy-coupling factor transporter ATPase
MNEMIKCKNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD
GLDTSDEENLWDIRNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRH
APHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE
ADRIIVMDSGKVVMEGTPKEIFKEVEMMKKIGLDVPQVTELAYELKKEGVDIPSDILTIDEMVNELCQLK
>gnl|CDD|237454 PRK13634, cbiO, cobalt transporter ATP-binding subunit; Provisional
MDITFQKVEHRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERV
ITAGKKNKKLKPLRKKVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLA
RSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAA
RYADQIVVMHKGTVFLQGTPREIFADPDELEAIGLDLPETVKFKRALEEKFGISFPKPCLTLEELAHEVV
QLLRKGGHES
>gnl|CDD|184195 PRK13635, cbiO, energy-coupling factor ABC transporter ATP-binding protein
MKEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV
LSEETVWDVRRQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHR
LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRV
IVMNKGEILEEGTPEEIFKSGHMLQEIGLDVPFSVKLKELLKRNGILLPNTYLTMESLVDELWTLHSKK
>gnl|CDD|184196 PRK13636, cbiO, cobalt transporter ATP-binding subunit; Provisional
MEDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI
DYSRKGLMKLRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTH
CLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCD
NVFVMKEGRVILQGNPKEVFAEKEMLRKVNLRLPRIGHLMEILKEKDGFVFDELDLTISQARKTLNSWKN
KIF
>gnl|CDD|237455 PRK13637, cbiO, energy-coupling factor transporter ATPase
MSIKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVD
ITDKKVKLSDIRKKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDK
SPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAK
LADRIIVMNKGKCELQGTPREVFKEVETLESIGLAVPQVTYLVRKLRKKGFNIPDDIFTIEEAKEEILKY
LRGEKNI
>gnl|CDD|184198 PRK13638, cbiO, energy-coupling factor ABC transporter ATP-binding protein
MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKR
GLLALRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHG
QKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLR
QGQILTHGAPGEVFACTEAMEQAGLTQPWLVKLHTQLGLPLCKTETEFFHRMQKCAFREAS
>gnl|CDD|184199 PRK13639, cbiO, cobalt transporter ATP-binding subunit; Provisional
ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK
KSLLEVRKTVGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSG
GQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVM
SDGKIIKEGTPKEVFSDIETIRKANLRLPRVAHLIEILNKEDNLPIKMGYTIGEARRNIKELLKG
>gnl|CDD|184200 PRK13640, cbiO, energy-coupling factor transporter ATPase
MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVD
GITLTAKTVWDIREKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSE
PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMA
DQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGLDIPFVYKLKNKLKEKGISVPQEINTEEKLVQYLCQLNS
KM
>gnl|CDD|237456 PRK13641, cbiO, energy-coupling factor transporter ATPase
MSIKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYH
ITPETGNKNLKKLRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLIS
KSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAE
YADDVLVLEHGKLIKHASPKEIFSDKEWLKKHYLDEPATSRFASKLEKGGFKFSEMPLTIDELVDGIKNN
LKGGFHE
>gnl|CDD|184202 PRK13642, cbiO, energy-coupling factor transporter ATPase
MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL
LTAENVWNLRRKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPAR
LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRI
LVMKAGEIIKEAAPSELFATSEDMVEIGLDVPFSSNLMKDLRKNGFDLPEKYLSEDELVELLADKLR
>gnl|CDD|184203 PRK13643, cbiO, energy-coupling factor transporter ATPase
MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVV
SSTSKQKEIKPVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEK
SPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADY
ADYVYLLEKGHIISCGTPSDVFQEVDFLKAHELGVPKATHFADQLQKTGAVTFEKLPITRAELVTLLTSL
SVNSGGEN
>gnl|CDD|106587 PRK13644, cbiO, energy-coupling factor transporter ATPase
MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS
KLQGIRKLVGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGG
QGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDR
GKIVLEGEPENVLSDVSLQTLGLTPPSLIELAENLKMHGVVIPWENTSSPSSFAEEICRLFLKT
>gnl|CDD|184204 PRK13645, cbiO, energy-coupling factor transporter ATPase
FDFSKDIILDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV
GDYAIPANLKKIKEVKRLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP
EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHN
MDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEIDPPKLYQLMYKLKNKGIDLLNKNIRTIEEF
AKELAKVLK
>gnl|CDD|184205 PRK13646, cbiO, energy-coupling factor transporter ATPase
MTIRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDIT
ITHKTKDKYIRPVRKRIGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMS
QSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVA
RYADEVIVMKEGSIVSQTSPKELFKDKKKLADWHIGLPEIVQLQYDFEQKYQTKLKDIALTEEEFVSLYK
EWQHEK
>gnl|CDD|237457 PRK13647, cbiO, cobalt transporter ATP-binding subunit; Provisional
MDNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN
AENEKWVRSKVGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLS
YGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIV
LKEGRVLAEGDKSLLTDEDIVEQAGLRLPLVAQIFEDLPELGQSKLPLTVKEAVQIIRKLLTKG
>gnl|CDD|184207 PRK13648, cbiO, cobalt transporter ATP-binding subunit; Provisional
MEDKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN
QAITDDNFEKLRKHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEP
NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEAD
HVIVMNKGTVYKEGTPTEIFDHAEELTRIGLDLPFPIKINQMLGHQTSFLTYEGLVDQL
>gnl|CDD|184208 PRK13649, cbiO, energy-coupling factor transporter ATPase
MGINLQNVSYTYQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTL
ITSTSKNKDIKQIRKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFE
KNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVAN
YADFVYVLEKGKLVLSGKPKDIFQDVDFLEEKQLGVPKITKFAQRLADRGISFSSLPITIEEFREVLKHG
>gnl|CDD|184209 PRK13650, cbiO, energy-coupling factor transporter ATPase
MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL
LTEENVWDIRHKIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPAR
LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRV
LVMKNGQVESTSTPRELFSRGNDLLQLGLDIPFTTSLVQSLRQNGYDLPEGYLTEKELEEQLWELISKM
>gnl|CDD|184210 PRK13651, PRK13651, cobalt transporter ATP-binding subunit; Provisional
MQIKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKD
EKNKKKTKEKEKVLEKLVIQKTRFKKIKKIKEIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEE
AKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDN
LNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNKFLIENNMEPPKLLNFVNKLEKKG
IDVPKVTSIEELASEINMYLEKKNK
>gnl|CDD|172200 PRK13652, cbiO, cobalt transporter ATP-binding subunit; Provisional
MHLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK
ENIREVRKFVGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSG
GEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYV
MDKGRIVAYGTVEEIFLQPDLLARVHLDLPSLPKLIRSLQAQGIAIDMAYTYQEAEDAFLKAFGKRA
>gnl|CDD|237458 PRK13654, PRK13654, magnesium-protoporphyrin IX monomethyl ester cyclase; Provisional
PEPATVPSELRPGTKAALKETILTPRFYTTDFDAMAKLDLSPNREELDAILEEMRADYNRHHFVRDEEFD
QDWDHLDPETRKEFIDFLERSCTAEFSGFLLYKELSRRLKDRNPLLAELFQLMARDEARHAGFLNKAMKD
FGLSLDLGFLTKKKKYTFFPPKFIFYATYLSEKIGYWRYITIYRHLEKHPEHRFHPIFKFFENWCQDENR
HGDFFALLMRAQPKLLKGWVNRLWIRFFLLAVFATMYLRDHERPDFYEALGLDAREYDQEVIRKTNETSA
RVFPVVLDVDDPRFYARLERCVENNEKLRAIKASGGPKPLKKLRKLPLFASAAWQFLRLYLLKPIDKEAL
PGTVR
>gnl|CDD|237459 PRK13655, PRK13655, phosphoenolpyruvate carboxylase; Provisional
RKIPRTMSTQHPDNAVVPFFAKSPVISGEDEVDEAYYAFSHLGCDEVMWDYEGKETDYHVVRKLLSKYPD
FFKGHILGKDVFLTPRVPNPKVEKAERKLLAETLESIANSYDLALSFYTQPIFEVILPMTTSAEELIEVQ
RYYEKVVAGVKVKEWIGEFEPKEIEVIPLFEDADALLNADEILEEYLKAKKPHGKYLRVFLARSDPAMNY
GHIASVLSVKYALSRLYELEEELGVEIYPILGVGSLPFRGHLSPENLENVLEEYPGVYTFTVQSAFRYDY
PYEEVKKAIEEINEKLIAPPRILSEEDKEELLEIIEKYSERYQSQIEKLADTINRVAKLIPKRRDRKLHI
GLFGYSRSVGGVSLPRAISFTGALYSIGLPPELIGAGRLLELAKEDDLDILLENYPNLKKDLEFAARFFN
PEVAEKLIDEETIAEIKEDIDEAKEILGLELGPDPEYERLHLLSSLFLLALKEEELQRVKSLILEMAKIR
GFLG
>gnl|CDD|237460 PRK13656, PRK13656, enoyl-[acyl-carrier-protein] reductase FabV
MIIKPKIRGFICTTAHPVGCEANVKEQIEYVKAQGPIANGPKKVLVIGASSGYGLASRIAAAFGAGADTL
GVFFEKPGTEKKTGTAGWYNSAAFDKFAKAAGLYAKSINGDAFSDEIKQKVIELIKQDLGQVDLVVYSLA
SPRRTDPKTGEVYRSVLKPIGEPYTGKTLDTDKDVIIEVTVEPATEEEIADTVKVMGGEDWELWIDALDE
AGVLAEGAKTVAYSYIGPELTHPIYWDGTIGKAKKDLDRTALALNEKLAAKGGDAYVSVLKAVVTQASSA
IPVMPLYISLLFKVMKEKGTHEGCIEQIYRLFSERLYRDGAIPEVDEEGRLRLDDWELRPDVQAAVRELW
PQVTTENLYELTDYAGYKAEFLKLFGFGVDGVDYDADVDPDVKIPLLI
>gnl|CDD|184214 PRK13657, PRK13657, glucan ABC transporter ATP-binding protein/ permease
MSLFRLYARVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAISGKGDIFPLLAAWAGFGLFNI
IAGVLVARHADRLAHRRRLAVLTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLAT
LVALVVLLPLALFMNWRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQS
YNRIEAETQALRDIADNLLAAQMPVLSWWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVG
FATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQG
VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGL
FNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP
PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARG
GRFAALLRAQGMLQEDERRKQPAAEGAN
>gnl|CDD|184215 PRK13658, PRK13658, hypothetical protein; Provisional
MSEFDAQRVAERIDTVLDILVAGDYHSAIHNLEILKAELLRQVAESTSPPDIPKAPWEI
>gnl|CDD|184216 PRK13659, PRK13659, DUF1283 family protein
LLLPLLLQALALSTSAHAETSKLVIESGDSALSKEQARQSKEQWNDTRSLRQKVNKRVEKEFDKADRAFD
NRDKCEQSANINAYWEPNTLRCLDRRTGRPITP
>gnl|CDD|237461 PRK13660, PRK13660, hypothetical protein; Provisional
MKRLLVTGYKSFELGIFKDKDPKIKYIKKAIKRKLIALLEEGLEWVIISGQLGVELWAAEVVLELKEEYP
DLKLAVITPFEEHGENWNEANQEKLANILKQADFVKSISKRPYESPAQFRQYNQFMLEHTDGALLVYDEE
NEGSPKYFYEAAKKKQEKEDYPLDLITFDDLQEIAEEWSENQ
>gnl|CDD|184218 PRK13661, PRK13661, ECF-type riboflavin transporter substrate-binding protein
MKNLSIKTVVAIGIGAALFVILGRFIFIPTGFPNTNIELAYAFLALFAVLFGPVVGFLVGFIGHALKDFI
AYGGPWWTWVLASGIIGLIIGLFKKRLRLENGVFSKKDIVYFNIVQIIANVIAWGLIAPIGDIIIYSEPA
NKVFAQGIVAAIANIISIAIIGTLLLKAYAKSRTKKGSLKKE
>gnl|CDD|184219 PRK13662, PRK13662, hypothetical protein; Provisional
MKLPKEGDFIQIQSYKHDGSLHRTWRDTMVLKTTENAVIGGNDHTLVTESDGRRWVTREPAICYFHKKYW
FNVIAMIREDGVYYYCNLASPFVLDEEALKYIDYDLDIKVFPDGEYRLLDEDEYEQHSKQMNYPPDIDRI
LKENVKILVDWINQKKGPFSPDFVDIWYERYLEYRNR
>gnl|CDD|184220 PRK13663, PRK13663, hypothetical protein; Provisional
MKIGFDNEKYLELQSDHILERINQFDGKLYLEFGGKLFDDYHASRVLPGFEPDNKIKLLQELKDQVEIVI
AINANDIERNKIRGDLGITYDQDVLRLIDDFRELGLYVGSVVITQYDGQPAADAFRNRLERLGIKVYRHY
PIKGYPTDVDHIVSDEGYGKNDYIETTRPLVVVTAPGPGSGKLATCLSQLYHDQKRGIKAGYAKFETFPV
WNLPLKHPVNLAYEAATADLDDVNMIDPFHLEAYGKTAVNYNRDIEVFPVLKRILEKILGKSPYKSPTDM
GVNMVGFCIVDDEACREASKQEIIRRYYQTLVDFKKGGVDEEAVKKIELLMNDAGITPEDRKVVVAAREK
AEETGEPALAIELPDGTIVTGKTSELLGATAAVLLNALKHLAGIDDEIHLISPEIIEPIQNLKTNHLGSR
NPRLHTDEVLIALSISAATNPTAQRAMEQLGNLKGCEAHSTVILSDVDENVFRKLGINVTSDPKYQSKKL
YRK
>gnl|CDD|184221 PRK13664, PRK13664, hypothetical protein; Provisional
MDWLAKYWWILVLVFLVGVLLNVIKDLKRVDHKKFLANKPELPPHRDFNDKWDDEDDWPKKD
>gnl|CDD|237462 PRK13665, PRK13665, hypothetical protein; Provisional
MMTLIGLIIIAVLIIIFLIVFFSFVPVGLWISALAAGVRVGIFTLVGMRLRRVPPSRIVNPLIKAHKAGL
DLTTNQLEAHYLAGGNVDRVVDALIAAQRANIDLDFERAAAIDLAGRDVLEAVQMSVNPKVIETPFIAAV
AKDGIEVKAKARVTVRANIDRLVGGAGEETIIARVGEGIVSTIGSSESHKEVLENPDSISKTVLSKGLDA
GTAFEILSIDIADVDVGKNIGAKLQTDQAEADKRIAQAKAEERRAMAVALEQEMKAKVQEMRAKVVEAEA
EVPLAMAEALRSGNLGVMDYYNMKNIQADTDMRESI
>gnl|CDD|184223 PRK13666, PRK13666, hypothetical protein; Provisional
ASEKVIDHREKALALLKADAEKILKLIKVQMDNLTMPQCPLYEEVLDTQMFGLSREVDFAVRLGLIDEEE
GKQLLSRLERELSALHEAFTNK
>gnl|CDD|184224 PRK13667, PRK13667, hypothetical protein; Provisional
MIYKVFYQETKDEVPVRETTQTLYLEADSEVEVRGRLKDRTAYNIEFIQLLSGAHLEYEKENGDFKLTEF
>gnl|CDD|237463 PRK13668, PRK13668, hypothetical protein; Provisional
MTSFKMRDKLKKRLSHPDWDFSFDREKETLRIERKDNKKGVTISLPPIVAKWEEKKEKAIDEIVYYVEEA
LAAMADKVKLEGNEANIYPVIRSTSFPKKTKEGVPLIYDEHTAETRIYYALDLGKTYRLIDERMLEKLGL
TEEQIREMALFNLRSLPTPVKQDEVAGNTFYFLNTNDGYDASRILNESFLQEMREKIEGEMLVAVPHQDV
LIIADIRNETGYDVLAQMTMDFFAKGLVPITSLSFVYENGELEPIFILAKNRKKFNK
>gnl|CDD|184226 PRK13669, PRK13669, hypothetical protein; Provisional
MNPIVEFCVSNLASGSQAAFEKLEKDPNLDVLEYGCLGYCGICSEGLFALVNGEVVEGETPEELVENIYA
HLEENPMF
>gnl|CDD|237464 PRK13670, PRK13670, nucleotidyltransferase
MKVTGIIVEYNPFHNGHLYHLNQAKKLTNADVTIAVMSGNFVQRGEPAIVDKWTRAKMALENGVDLVVEL
PFLYSVQSADFFAEGAVSILDALGVDSLVFGSESGDIEDFQKIAKILNEEPEEFKKLLKELLKKGLSYPQ
ARSEALEEFLGEINFDLSTPNNILGLEYAKAIAKLGSNIKLHTIKREGAGYHDEELDGEFASATAIRKAL
LEKDLDELKKFVPKATLELLKRYIGPFVSWEDYFPFLKYQLITLSHEDLRQIYQVSEGLENRIKKAIKKA
SSFDEFVELVKTKRYTYTRIQRLLTYILLNATKEDVEKTSLPPYIRVLGFTEKGQQYLKKIKKKSSLPII
TKISKKPWLELDIKATNIYQLINPSQIQEQDFGRPPIR
>gnl|CDD|184228 PRK13671, PRK13671, nucleotidyltransferase
MAIGIIAEYNPFHNGHIYQINYIKNKFPNEKIIVILSGKYTQRGEIAVASFEKRKKIALKYGVDKVIKLP
FEYATQAAHIFAKGAIKKLNKEKIDKLIFGSESNDIELMYKIANTIKENEEEYNQLLKKNLKQGYSFPKA
SSLALKELTGSEIVMPNDILGFEYIKQIVNNNYPIQPYCIKRTVGFHSENPEDNYASATYLRKMIFENKD
ISKYSPMKFKKPPKSIENLYKEFQKIVRNTSKEKLAKIWLVSEGIENLFKKNINAPNYDSFVNKCNSKRY
TSSRIKRIMLYVLLKIKK
>gnl|CDD|184229 PRK13672, PRK13672, hypothetical protein; Provisional
MRKSFYHYLMTQRNPKSNDPKAILANNAFDDLSFPKQSDDFDELSRYLELNASYLFSMSIFDEAWEEYLE
H
>gnl|CDD|237465 PRK13673, PRK13673, hypothetical protein; Provisional
MLHLHITSWVLAIILFFVAYSLYSGGSKKAKILHMILRLFYILIIITGFWLLIRSFGSNHMLYILKMLLG
IIVIGLMEMSLAKRKKGKPTGGFWWIFIIVLVLTILLGLILPLGFGVF
>gnl|CDD|237466 PRK13674, PRK13674, GTP cyclohydrolase I FolE2
TKPMMKATMPDVQSTPDTRLIPIDWVGIKNIRLPVRVDTRDGGTQTTVARVDLTVSLPADFKGIHMSRLY
ELLEEHAEQELSPASLEQLLRDMLESLESRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVF
RLELKVEVPVSSLCPCSKAISRYTAHSQRSVATVKVRLAADAQLWIEDLIDLAEAAASTPLQTLLKRPDE
KAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAVAVIEKDKRGAA
>gnl|CDD|184232 PRK13675, PRK13675, GTP cyclohydrolase; Provisional
MMQLPDVQASEPDIKIGLTRVGVTNVKKLVKIKRKGKRPIVLIPTFEVFVDLPSDRKGIHMSRNVEVIDE
VLEEAVEEEVYEIEDLCGDIAKRLLEKHEYATRAEVRMRSEYMMRRETPVSKKKSQEVVDIIAGAIATRD
GNVRKEIGAEVVGMTACPCAQEMMKERARKKLAELGVDEETIEKFLDNVPMATHNQRGRGTLTIEVPGDE
DVSLEDIIDIIESSMSSPIYELLKRPDENAVVYEAHKNPKFVEDCVREMAKKVVEEFPHLPDDAVVTVRQ
INEESIHRHNAFAERVATMGELRKELNA
>gnl|CDD|237467 PRK13676, PRK13676, YlbF/YmcA family competence regulator
MMVNIYDLANELERALRELPEYKALKEAKEAVKADEEAKKLFDEFRALQLEIQQKQMTGQEITEEEQQKA
QELGQKIQQNELLSKLMEAEQRLSVYINDINKIIFKPLEELYKD
>gnl|CDD|184234 PRK13677, PRK13677, DUF3461 family protein
MYDNLKSLGITNPEDIDRYSLRQEANNDILKIYFRKDKGEFFAKSVKFKYPRQRKTVVADGGGQGYKEVQ
EISPNLRYVIDELDQICQRDREEVDLKRKILDDLRHLESVVANKISEIEADLEKL
>gnl|CDD|184235 PRK13678, PRK13678, hypothetical protein; Provisional
HNHNNEEEELITLVDEEGNEVLFEILFTFDSEEFGKSYVLLSPAGEEEDEDDEIEIQAFSFTEDEDGDEG
DLQPIETDEEWDMIEEVLNTFLDEE
>gnl|CDD|184236 PRK13679, PRK13679, hypothetical protein; Provisional
MKYGIVLFPSKKIQDFANSYRKRYDPHYALIPPHITLKEPFEISDEQLDSIVEELRAIASETKPFTLHVT
KVSSFAPTNNVIYFKVEKTEELEELHERLHSGDFYGEAEYAFVPHITIGQGLSDDEHEDVLGQLKMADVD
HEETIDRFHLLYQLENGSWTVYETFRLG
>gnl|CDD|184237 PRK13680, PRK13680, hypothetical protein; Provisional
KKRGALLGLLLLSACGSVFAANAETSRSVKFPKCEGLDAAGIAASVKRDYLQNRIARWADDQKQLGQADP
VAWVNVQDITGKDDKWQVPLTVRGKSADIHYQVVVDCKAGTAEYQER
>gnl|CDD|184238 PRK13681, PRK13681, protein YohO
MRIAKIGVIALFLLMAIGGIGGVMLAGYTFILRAG
>gnl|CDD|184239 PRK13682, PRK13682, hypothetical protein; Provisional
MLKWAIIFLVIALIAAVLGFGGIAGAAAGIAKILFFIFLVLFVVSLLLGRK
>gnl|CDD|184240 PRK13683, PRK13683, hypothetical protein; Provisional
MYTIELSLKYSPMPISVQRKEAEDAEALYQQIRQAMRSGNPRLLELTCEKVEDKKIAVLSSEISAVQIYE
KSGAAGGGKRPGFSADA
>gnl|CDD|237468 PRK13684, PRK13684, photosynthesis system II assembly factor Ycf48
MKRLLKSLKNLLLLLALLLVLSGCSTTRVPMLSSSPWQVIDLPTEANLLDIAFTDPNHGWLVGSNRTLLE
TNDGGETWEERSLDLPEENFRLISISFKGDEGWIVGQPSLLLHTTDGGKNWTRIPLSEKLPGSPYLITAL
GPGTAEMATNVGAIYRTTDGGKNWEALVEDAAGVVRNLRRSPDGKYVAVSSRGNFYSTWEPGQTAWTPHQ
RNSSRRLQSMGFQPDGNLWMLARGGQIRFNDPDDLESWSKPIIPEITNGYGYLDLAYRTPGEIWAGGGNG
TLLVSKDGGKTWEKDPVGEEVPSNFYKIVFLDPEKGFVLGQRGVLLRYVGSAEA
>gnl|CDD|184242 PRK13685, PRK13685, hypothetical protein; Provisional
MSLSGFAHPWFFLFLLVVAALVALYVVVQRARRRRMLRFANMELLESVAPKRPSRWRHVPAALLVLSLVL
LTVAMAGPTHDVRIPRNRAVVMLVIDVSQSMRATDVEPNRLAAAQEAAKQFADELTPGINLGLIAFAGTA
TVLVSPTTNREATKNAIDKLQLADRTATGEAIFTALQAIATVGAVIGGGDTPPPARIVLMSDGKETVPTN
PDNPRGAYTAARTAKDQGVPISTISFGTPYGSVEINGQRQPVPVDDESLKKIAQLSGGEFYTAASLEELR
AVYATLQQQIGYETIKGDASVGWLRLGALVLALAALAALLINRRLP
>gnl|CDD|237469 PRK13686, PRK13686, photosystem II reaction center protein Ycf12
MGFIMEFLANINLEVIFQLTFVALIVIAGPVVIFLLAFRGGDL
>gnl|CDD|184244 PRK13687, PRK13687, hypothetical protein; Provisional
MNISRQEQRTLHVLAQGGRIEHERDDSGRITAVECYTREGWLLADCTLAVFKKLKRKRLIKSVNGQPYRI
TRRGLNNVRAQLDNR
>gnl|CDD|237470 PRK13688, PRK13688, N-acetyltransferase
MPEVKRLLINYKTLEEFKKFREFGNQELSMLEELQANIIENDSESPFYGIYYGDSLVARMSLYKKGGVEE
PYFEDTQDYLELWKLEVLPKYQNRGYGEMLVDFAKSFQLPIKTIARNKSKDFWLKLGFTPVEYKNDEGED
PLVWHPETNLEAVTNE
>gnl|CDD|237471 PRK13689, PRK13689, hypothetical protein; Provisional
MAQQSKYSDEQVEQLLAELLAVLEKHKAPTDLSLMVLGNMVTNLLNTSVAPAQRQAIAESFARALQSSVK
EDKAH
>gnl|CDD|139768 PRK13691, PRK13691, (3R)-hydroxyacyl-ACP dehydratase subunit HadC; Provisional
MALKTDIRGMVWRYPDYFVVGREQIRQFARAVKCDHPAFFSEDAAAELGYDALVAPLTFVTIFAKYVQLD
FFRHVDVGMETMQIVQVDQRFVFHKPVLAGDKLWARMDIHSVDERFGADIVVTRNVCTNDDGELVMEAYT
TLMGQQGDNSASLKWDKESGQVIRTA
>gnl|CDD|237473 PRK13692, PRK13692, (3R)-hydroxyacyl-ACP dehydratase subunit HadA; Provisional
MALSADIVGMHYRYPDHYEVEREKIREYAVAVQNDDAAYFEEDAAAELGYKGLLAPLTFICVFGYKAQSA
FFKHANIAVADAQIVQVDQVLKFEKPIVAGDKLYCDVYVDSVREAHGTQIIVTKNIVTNEEGDVVQETYT
TLAGRAGEDGEEGFSDGTA
>gnl|CDD|184249 PRK13693, PRK13693, (3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
MALREFSSVKVGDQLPEKTYPLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYV
TSWVGDPGAVTEYNVRFTAVVPVPNDGKGAELVFNGRVKSVDPESKSVTIALTATTGGKKIFGRAIASAK
LA
>gnl|CDD|237474 PRK13694, PRK13694, hypothetical protein; Provisional
SDMSDAEVVAKEQLRAFIERIERLEEEKKTISDDIKDVYAEAKGNGFDVKALKTIIRLRKKDDDERAEEE
AILDLYMDALGMI
>gnl|CDD|237475 PRK13695, PRK13695, NTPase
MKIGITGPPGVGKTTLVLKIAELLKEEGYKVGGFYTEEVREGGKRIGFKIIDLDTGEEGILARVGFPSRP
RVGKYVVNLEDLERIGIPALERALEEADVIIIDEIGKMELKSPKFVKAVEEVLDSEKPVIATLHRRSVHP
FVQEIKSRPGGRVYELTPENRDSLPFEILNRLKG
>gnl|CDD|237476 PRK13696, PRK13696, hypothetical protein; Provisional
MMMKTITISDDVYEKLLEIKGDKSFSEVIRELIEKKKGNLDKLMKAFGILSEEEAEELKKEL
>gnl|CDD|184253 PRK13697, PRK13697, cytochrome c6; Provisional
MKKILSLVLLGLLLLTFAFSSPALAADAANGEQVFSANCASCHAGGKNLVNAGKTLKKADLEKYGMYSLE
AITAQVTNGKNAMPAFKDRLSPDQIEDVAAYVLEQAEKGWK
>gnl|CDD|184254 PRK13698, PRK13698, ParB/RepB/Spo0J family plasmid partition protein
MKRAPVIPKHTSDTQPAEDTSEPSPAAPMVDSLIARVGGMARGNAITLPVCGRDVKFTLEVIRGDSVEKT
SRVWSGNERDQELLTEDSLDDLIPSFLLTGQQTPAFGRRVSGVIEIADGSRRRKAAILTESDYRVLVGEL
DDEQMAALSRLGNDYRPTSAYERGLRYASRLQNEFAGNISALADAENISRKIITRCINTAKLPKSVVALF
AHPGELSARSGEALQKAFTDKEELLKQQTSNLHEQKKAGVIFETEEVITLLTSVLKTSSASRTSLSSRHQ
FAPGATALYKGDKVVFNLDRSRVPTECIEKIEAILKELEKPAS
>gnl|CDD|184255 PRK13699, PRK13699, putative methylase; Provisional
MSRFILGNCIDVMARFPDNAVDFILTDPPYLVGFRDRQGRTIAGDKTDEWLQPACNEMYRVLKKDALMVS
FYGWNRVDRFMAAWKNAGFSVVGHLVFTKNYTSKAAYVGYRHECAYILAKGRPALPQNPLPDVLGWKYSG
NRHHPTEKPVTSLQPLIESFTHPNAIVLDPFAGSGSTCVAALQSGRRYIGIELLEQYHRAGQQRLAAVQR
AMQQGAANDDWFMPEAA
>gnl|CDD|184256 PRK13700, PRK13700, conjugal transfer protein TraD; Provisional
MSFNAKDMTQGGQIASMRIRMFSQIANIILYCLFIFFWILVGLVLWVKISWQTFVNGCIYWWCTTLEGMR
DLIKSQPVYEIQYYGKTFRMNAAQVLHDKYMIWCGEQLWSAFVLAAVVALVICLITFFVVSWILGRQGKQ
QSENEVTGGRQLTDNPKDVARMLKKDGKDSDIRIGDLPIIRDSEIQNFCLHGTVGAGKSEVIRRLANYAR
QRGDMVVIYDRSGEFVKSYYDPSIDKILNPLDARCAAWDLWKECLTQPDFDNTANTLIPMGTKEDPFWQG
SGRTIFAEAAYLMRNDPNRSYSKLVDTLLSIKIEKLRTYLRNSPAANLVEEKIEKTAISIRAVLTNYVKA
IRYLQGIEHNGEPFTIRDWMRGVREDQKNGWLFISSNADTHASLKPVISMWLSIAIRGLLAMGENRNRRV
WFFCDELPTLHKLPDLVEILPEARKFGGCYVFGIQSYAQLEDIYGEKAAATLFDVMNTRAFFRSPSHKIA
EFAAGEIGEKEHLKASEQYSYGADPVRDGVSTGKDMERQTLVSYSDIQSLPDLTCYVTLPGPYPAVKLSL
KYQARPKVAPEFIPRDINPEMENRLSAVLAAREAEGRQMASLFEPDVPEVASGEDVTQAEQPQQPQQPQQ
PQQPQQPQQPVSPVINDKKSDAGVNVPAGGIEQELKMKPEEEMEQQLPPGISESGEVVDMAAYEAWQQEN
HPDIQQQMQRREEVNINVHRERGEDVEPGDDF
>gnl|CDD|237477 PRK13701, psiB, conjugation system SOS inhibitor PsiB
MKTELTLNVLQTMSAQEYEDIRAAGSDERRELTHAVMRELDAPDGWTMNGEYGSEFGGFFPVQVRFTPAH
ERFHLALCSPGDVSPVWVLVLVNAGGEPFAVVQVQDRFAPEAISHSLALAASLDAQGYSVNDIIHILMAE
GGQA
>gnl|CDD|184258 PRK13702, PRK13702, replication regulatory protein RepA
MSQTENAVTSSSGAKRAYRKGNPLSAAEKQRASVARKRATHKEIKVFIQNPLKDKLMELCEEEGLTQAEM
IERLIERELARRAML
>gnl|CDD|184259 PRK13703, PRK13703, conjugal pilus assembly protein TraF; Provisional
MMNKALLPLLLCCFLFPASGKDAGWQWYNEKKNPKEKENKPVPAAPRQEPDIMEKLAVLQTATKRALYEA
ILYPGVENFVKYFRLQNYWTQQAGLFSMSAKKAMLAHPELDYNLQYSHYNGTVRNQLAADQAQQRQAIAK
LAEHYGLMFFYRGQDPIDGQLAQVINDFRDTYGLSVIPVSVDGVINPLLPDSRTDQGQAQRLGVKYFPAL
MLVDPKSGSVRPLSYGFITQDDLAKRFLNVSTDFKPNF
>gnl|CDD|184260 PRK13704, PRK13704, plasmid SOS inhibition protein A; Provisional
MSARSRALVPLSPEQQAAMQAIAEVEKRRHQGRTLAEYPYAKAFFRCLNGSRRISLSDLRFFMPSLNTPE
ERHGNRLQWLEAIDVLIESQGEVCPLPLSGDVAARLFPSVRFRVRERRRHRSAIAFQRYSRQQAREAEQK
WRAYQNLVAQAEIELAFHSPETVGSWYARWSDRVAEHDLETLFWQWWERFPSLSGMERWRWQDEPLWQVI
AEADYAAREAPEAVREMERWMVPNKLREAA
>gnl|CDD|184261 PRK13705, PRK13705, plasmid-partitioning protein SopA; Provisional
MDLMETLNQCINAGHEMTKAIAIAQFNDDSPEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDM
EMRGRVEQRVGYTIEQINHMRDVFGTRLRRAEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLL
VEGNDPQGTASMYHGWVPDLHIHAEDTLLPFYLGEKDDATYAIKPTCWPGLDIIPSCLALHRIETELMGK
FDEGKLPTDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDM
LRDLLKNVDLKGFEPDVRILLTKYSNSNGSQSPWMEEQIRDAWGSMVLKNVVRETDEVGKGQIRMRTVFE
QAIDQRSSTGAWRNALSIWEPVCNEIFDRLIKPRWEIR
>gnl|CDD|184262 PRK13706, PRK13706, conjugal transfer pilus acetylase TraX
MTTDNTNTTRNDSLAARTDTWLQSLLVWSPGQRDIIKTVALVLMVLDHINRILHLDQEWMFLAGRGAFPL
FALVWGLNLSRHAHIRQPAINRLWGWGIIAQFAYYLAGFPWYEGNILFAFAVAAQVLTWCETRSGWRTAA
AILLMALWGPLSGTSYGIAGLLMLAVSHRLYRAEDRAERLALVACLLAVIPALNLATSDAAAVAGLVMTV
LTVGLVSCAGKSLPRFWPGDFFPVFYACHLAVLGVLAL
>gnl|CDD|184263 PRK13707, PRK13707, type IV conjugative transfer system protein TraL
MSGDELDKYRFPETLTNQSRWFGLPLDELIPAAICIGWGITTSKYLFGIIAAVLVWFGIRKLKKGRGSSW
LRDLIYWYLPTALLRGIFHNVPDSCFRQWIK
>gnl|CDD|184264 PRK13708, PRK13708, type II toxin-antitoxin system toxin CcdB
MQFKVYTYKRESRYRLFVDVQSDIIDTPGRRMVIPLASARLLSDKVSRELYPVVHIGDESYRLMTTDMAS
VPVSVIGEEVADLSHRENDIKNAINLMFWGI
>gnl|CDD|237478 PRK13709, PRK13709, conjugal transfer nickase/helicase TraI; Provisional
MSIAQVKSAGSAGNYYTDKDNYYVLGSMGERWAGEGAEQLGLQGSVDKDVFTRLLEGRLPDGADLSRMQD
GSNKHRPGYDLTFSAPKSVSMMAMLGGDKRLIEAHNQAVDFAVRQVEALASTRVMTDGQSETVLTGNLVM
ALFNHDTSRDQDPQLHTHAVVANVTQHNGKWKTLSSDKVGKTGFIENVYANQIAFGKIYREALKEDVEAL
GYETEVVGKHGMWEMKGVPVEAFSSRSQEIREAVGEDASLKSRDVAALDTRKSKQHVDPEVRMAEWMQTL
KETGFDIRAYREAADQRAEIRTQAPGPASQDGPDIQQAVTQAIAGLSDRKVQFTYTDLLARTVGILPPEN
GVIERARAGIDEAISREQLIPLDREKGLFTSGIHVLDELSVRALSRDIMKQNRVTVHPEKSVPRTAGYSD
AVSVLAQDRPSLAIVSGQGGAAGQRERVAELVMMAREQGREVQILAADRRSQMNLKQDERLSGELITGRR
QLQEGMAFTPGSTLIVDQAEKLSLKETLTLLDGAARHNVQVLILDSGQRTGTGSALMVLKDAGVNTYRWQ
GGEQRPATVISEPDKNVRYARLAGDFAASVKAGEESVAQVSGVREQAILTGLIRSALKTQGVLGRPEVTI
TALSPVWLDSKSRYLRDMYRPGMVMEQWNPETRSHDRYVIDRVTAQSHSLTLRDAQGETQVVKISSLDSS
WSLFRPEKMPVADGERLRVLGKIPGLRLKGGDRLQVTSVSEDGLTVVVPGRAEPATLPVDDSPFTALKLE
HGWVETPGHSVSDSATVFASVTQRAMDNATLNGLARSGRDVRLYSSLDETRTAEKLARHPSFTVVSEQIK
ARAGETDLETAISLQKAGLHTPAQQAIHLALPVLESKNLAFSMVDLLTEAKSFAAEGTSFTELGGEINAQ
IKRGDLLYVDVAKGYGTGLLVSRASYEAEKSILRHILEGKEAVTPLMERVPGELMEGLTSGQRAATRMIL
ESTDRFTVVQGYAGVGKTTQFRAVMSAVNTLPESERPRVVGLGPTHRAVGEMRSAGVDAQTLASFLHDTQ
LQQRSGETPDFSNTLFLLDESSMVGNTDMARAYALIAAGGGRAVSSGDTDQLQAIAPGQPFRLMQTRSAA
DVAIMKEIVRQTPELREAVYSLINRDVERALSGIESVKPSQVPRQEGAWAPESSVTEFSHPQEAKLAEAQ
QKAMLAFPDVPMTLYEAIVRDYTGRTPEAREQTLIITHLNEDRRVLNSMIHDAREKAGELGKEQVTVPVL
DTANIRDGELRRLSTWEAHRGALALVDNVYHRIAGIDKDDGLITLRDAEGNTRLISPREAVAEGVTLYTP
DTIRVGTGDRMRFTKSDRERGYVANSVWTVTAVSGDSVTLSDGQQTRVIRPGQERAEQHIDLAYAITAHG
AQGASETYAIALEGTEGGRKQMAGFESAYVALSRMKQHVQVYTDNRQGWTDAINNAVQKGTAHDVLEPKP
DREVMNAERLFSTARELRDTAAGRAVLRQAGLAGGDSPARFIAPGRKYPQPHVALPAFDRNGKSAGIWLN
PLTTDDGNGLRGFSGEGRVKGSEDAQFVALQGSRNGESLLADNMQDGVRIARDNPDSGVVVRIAGEGRPW
NPGAITGGRVWGDIPDNSVQPGAGNGEPVTAEVLAQRQAEEAIRRETERRADEIVRKMAENKPDLPDGKT
EQAVRDIAGQERDRAAISEREAALPESVLREPQREREAVREVARENLLRERLQQMERDMVRDLQKEK
>gnl|CDD|184266 PRK13710, PRK13710, type II toxin-antitoxin system antitoxin CcdA
MKQRITVTVDSDSYQLLKAADVNISGLVNTAMQNEARRLRAERWKAENREGMAEVARFIEMNGSFADENR
NW
>gnl|CDD|184267 PRK13711, PRK13711, P-type conjugative transfer protein TrbJ
MPPVLWRGWIPFCRCTERKKVRNKQVVLLIAGISGIATGIIVSLNIPFIRQGLFYPASPVEIVVSLCLTF
SVSVVFFVGAIVGWISVSEIYYSRMTGLNESSEISEETYNERK
>gnl|CDD|184268 PRK13712, PRK13712, conjugal transfer protein TrbA; Provisional
MSEDYLKMFTGVVLLIFVIIAGYFFSERNDRKMFLLSSLVFLVINIACLYVLTASLWFLCGAIMNQGAAM
VVSMVISSLPNVTSFDSFRRIFICIMLSSVWSGVMWFFIRGLMTG
>gnl|CDD|184269 PRK13713, PRK13713, relaxosome protein TraM
ISNEVYEKINAIVEERRQEGAREKDVSFSSVASMLLELGLRVYEAQMERKESGFNQTEFNKLLLECVVKT
QSTVAKILGIESLSPHVSGNPKFEYANMVEDIREKVSEEMERFFPEND
>gnl|CDD|184270 PRK13715, PRK13715, conjugal transfer protein TraR; Provisional
MSDEADEAYSVTEQLTMTGINRIRQKINAHGIPVYLCEACGNPIPEARRKIFPGVTLCVECQAYQERQRK
HYA
>gnl|CDD|106657 PRK13716, PRK13716, RepA leader peptide Tap
MPGKVQDFFLCSLLLRIVSAGWCD
>gnl|CDD|184271 PRK13717, PRK13717, type-F conjugative transfer system protein TrbI
MTTTQKTTDVTAPRRSHWWWTVPGCLAMVLLNAAVSYGIVRLNAPVTAAFNMKQTVDAFFDSASQKQLSE
AQSKALSARFNTALEASLQAWQQKHHAVILVSPAVVQGAPDITREIQQDIARRMRAEP
>gnl|CDD|172260 PRK13718, PRK13718, conjugal transfer protein TrbE; Provisional
MKVIFTSNRIIDFLIRLTITAIVISPVIYWSWDTVKETTADDMLAAVFVILYSGVLLFILYFFFSALTKL
QKHDERKSDERNED
>gnl|CDD|237479 PRK13719, PRK13719, conjugal transfer transcriptional regulator TraJ; Provisional
MYPMDRRERATIRQIDLPESLTAFIDDYSYPACIRNESGKFIFYNTLFLKEFLGQLQSKEWWFSLPIDTA
TLLSRAELDAMSEPSGMNIIEDVFINNKLWDVIIESFIYGGVVFFLWRFFCAASNVISSIIRGLSTNLEA
KNKVTKYQNDVFILYSFGFSHEYIAQLLNITVGSSKNKISEILKFFGISSRDELLIILHTSEMIFYLYKK
VFEIINR
>gnl|CDD|172262 PRK13720, PRK13720, modulator of post-segregation killing protein; Provisional
MSSQHQDSLLPRFAQGEEGHETTTKRPCLVCVDRVSHTVDIHLSDTKIAVRDSLQRRIQGGGGFHGLRIR
>gnl|CDD|237480 PRK13721, PRK13721, conjugal transfer ATP-binding protein TraC; Provisional
VLGEMSFPQFSRLLPYRDYDQESGLFMNDTTMGFMLEAIPLNGANESIVEALDHMLRTKLPRGIPLCIHL
MSSKLVGDRIEYGLREFSWSGEQAERFNAITRAYYMRAALTQFPLPEGMNLPLTLRHYRVFISYCSPSKK
KSRADILEMENLVKIIRASLQGASITTQTVDAQAFISIVREMINHRPDSLYPKRRQLDPYSDLNYQCVED
SFDLKVRADYLTLGLRENGRNSTARILNFHLAKNPEIAFLWQMADNYSNLLNPELSISCPFILTLTLEVE
DQVKTQSEANLKYMDLEKKSKTSYAKWFPSVEKEAKEWGELRQRLGSNQSSLVSYFLNITAFCPDNNETA
LEVEQDILNSFRKNGFELISPRFNHMRNFLTCLPFMAGEGLFKDLKEAGVVQRAESFNVANLMPLVADNP
LTPAGLLAPTYRNQLAFIDIFFRGMNNTNYNMAVCGTSGAGKTGLIQPLIRSVLDSGGFAVVFDMGDGYK
SLCENMGGVYLDGETLRFNPFANITDIDQSAERIRDQLSVMASPNGNLDEVHEGLLLQAVRASWLAKKNR
ARIDDVVDFLKNARDSEQYADSPTIRSRLDEMIVLLDQYTANGTYGEYFNSDEPSLRDDARMVVLELGGL
EDRPSLLVAVMFSLIIYIENRMYRTPRNLKKLNVIDEGWRLLDFKNHKVGEFIEKGYRTARRHTGAYITI
TQNIVDFDSDKASSAARAAWGNSSYKIILKQSAKEFAKYNQLYPDQFSPLERDMIGGFGAAKDQWFSSFL
LQVENHSSWHRLFVDPLSRAMYSSDGPDFEFVQQKRKEGLSIHEAVWQLAWKKFGPEMASLEAWLEEHEK
YRSV
>gnl|CDD|184274 PRK13722, PRK13722, lytic transglycosylase; Provisional
MKKWMLAICLMFINEICHATDCFDLAGRDYKIDPDLLRAISWKESRYRVNAIGINPVTGYGSGLMQVDSQ
HFNELARYGIKPEHLTTDPCMNIYTGAYYLAIAFKKWGVSWEAVGAYNAGFRKTERQNQRRLAYASEVYR
IYTGIKSSKGIRIPATKKSLPEINSVQNN
>gnl|CDD|237481 PRK13723, PRK13723, conjugal transfer pilus assembly protein TraH; Provisional
IKPLLVLCAALLTVTPAASADVNSDMNQFFNKLGFASNTTQPGVWQGQAAGYATGGSLYARTQVKNVQLI
SMTLPDINAGCGGIDAYLGSFSFINGEQLQRFVKQIMSNAAGYFFDLALQTTVPEIKTAKDFLQKMASDI
NSMNLSSCQAAQGIVGGLFPRTQVSQQKVCQDIAGESNIFADWAASRQGCTVGGQSDSVRDKASDKDKER
VLKNINIMWDALSKNRMFDGNKELKEFVMTLTGTLIFGENGEITPLPARTTDRDIIRAMMEGGTAKIYHC
NDSDKCLKVVADTNVTISRDNALKSQITKLLTSIQNKAVSDTPLTDKEKGFISSTTIPVFKYLVDPQMLG
VSNSLIYQLTDYIGYDILLQYIQELIQQARAMLATGNYPEAVMDHLRENLNQAQRQIAAFQSQVQVQQDA
LLVVDRQMSYMRQQLSARMLSRYQNNYHFGG
>gnl|CDD|237482 PRK13724, PRK13724, conjugal transfer protein TrbD; Provisional
MNMRNINVITARSVPDKSVSDDFMHAVLSNCTTRIVLPAPKEFSSESLPHNFNMAAVGVMKKGMS
>gnl|CDD|184277 PRK13725, PRK13725, tRNA(fMet)-specific endonuclease VapC
MLKFMLDTNICIFTIKNKPEHVRERFNLNTGRMCISSVTLMELIYGAEKSQMPERNLAVIEGFVSRLEVL
DYDTAAATHTGQIRAELARQGRPVGPFDQMIAGHARSRGLIVVTNNTREFERVPGIRIEDWS
>gnl|CDD|184278 PRK13726, PRK13726, type IV conjugative transfer system protein TraE
MEHGARLSTSRVMAIAFIFLSVLIVLSLSVNVIQGVNNYRLQNEQRTAVTPMAFNAPFAVSQNSADASYL
QQMALSFIALRLNVSPETVDASHQALLQYIRPGAQNQMKVILAEEAKRIKNDNVNSAFYQTSVRVWPQYG
RVDIRGVLKTWIGDSKPFTEIKHYILILKRENGVTWLDNFGETDDEKK
>gnl|CDD|237483 PRK13727, PRK13727, conjugal transfer pilin chaperone TraQ; Provisional
ISKRRFSLPRLDITGMWVFSLGVWFHIVARLVYSKPWMAFFLAELIAAILVLFGAYRVLDAWIARVSREE
REALEARQQA
>gnl|CDD|237484 PRK13728, PRK13728, conjugal transfer protein TrbB; Provisional
MSLTKLLLVLLLLMATAVQASTRDEIERLWNPKGMAAQPAQPAADTSARTEKPAPRWFRLSNGRQVNLAD
WKVVLFMQGHCPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFFPNIPVATPTT
FLVNVNTLEALPLLQGATDAAGFMARMDTVLQMYGGKKGAK
>gnl|CDD|184281 PRK13729, PRK13729, conjugal transfer pilus assembly protein TraB; Provisional
MANINTIVKRKQYLWLGIVVVGAAAAIGGALYLSDVDMSGNGEAVAEQEPVPDMTGVVDTTFDDKVRQHA
TTEMQVTAAQMQKQYEEIRRELDVLNKQRGDDQRRIEKLGQDNAALAEQVKALGANPVTATGEPVPQMPA
SPPGPEGEPQPGNTPVSFPPQGSVAVPPPTAFYPGNGVTPPPQVTYQSVPVPNRIQRKTFTYNEGKKGPS
LPYIPSGSFAKAMLIEGADANASVTGNESTVPMQLRITGLVEMPNSKTYDATGCFVGLEAWGDVSSERAI
VRTRNISCLKNGKTIDMPIKGHVSFRGKNGIKGEVVMRNGKILGWAWGAGFVDGIGQGMERASQPAVGLG
ATAAYGAGDVLKMGIGGGASKAAQTLSDYYIKRAEQYHPVIPIGAGNEVTVVFQDGFQLKTIEEMALEKA
QSRAEEDNAESPVPAPPSAESHLNGFNTDQMLKQLGNLNPGQFMSGSQGGGNDGK
>gnl|CDD|184282 PRK13730, PRK13730, conjugal transfer pilus assembly protein TrbC; Provisional
MNRKIKALFALLMGLHGAVHASENVNTPENRQFLKQQENLSRQLREKPDHQLKAWAEKQVLENPLQRSDN
HFLDELVRKQQASQDGKPRQGALYFVSFSIPEEGLKRMLGETRHYGIPATLRGMVNNDLKTTAEAVLSLV
KDGATDGVQIDPTLFSQYGIRSVPALVVFCSQGYDIIRGNLRVGQALEKVAATGDCRQVAHDLLAGKGDS
GK
>gnl|CDD|184283 PRK13731, PRK13731, complement resistance protein TraT
MKTKKLMMVALVSSTLALSGCGAMSTAIKKRNLEVKTQMSETIWLEPASERTVFLQIKNTSDKDMSGLQG
KIADAVKAKGYQVVTSPDKAYYWIQANVLKADKMDLRESQGWLNRGYEGAAVGAALGAGITGYNSNSAGA
TLGVGLAAGLVGMAADAMVEDVNYTMITDVQIAERTKATVTTDNVAALRQGTSGAKIQTSTETGNQHKYQ
TRVVSNANKVNLKFEEAKPVLEDQLAKSIANIL
>gnl|CDD|184284 PRK13732, PRK13732, single-stranded DNA-binding protein; Provisional
MAVRGINKVILVGRLGKDPEVRYIPNGGAVANLQVATSESWRDKQTGEMREQTEWHRVVLFGKLAEVAGE
YLRKGAQVYIEGQLRTRSWEDNGITRYVTEILVKTTGTMQMLGRAPQQNAQPQPGPQQNGQPQSADATKK
GGAKTKGRGRKAAQPEPQPQPPEGEDYGFSDDIPF
>gnl|CDD|184285 PRK13733, PRK13733, conjugal transfer protein TraV; Provisional
MKQISLLIPLLGTLLLSGCAGTNSEFECNATTSDTCMTMEQANEKAKKLEQSSDAKPAAASLPRLAEGNF
RTMPVQTVTATTPSGSRPAVTATPEQKLLAPRPLFTAAREVKTVVPVSSVTPVTPPRPLRTGEQTARLWI
APYIDNQDVYHQPSSVFFVIKPSAWGKPRIN
>gnl|CDD|237485 PRK13734, PRK13734, conjugal transfer pilin subunit TraA; Provisional
MNAVLSVQGASAPVKKKSFFSKFTRLNMLRLARAVIPVAVLMMFFPQLAMAGAGGQDLMASGNTTVKATF
GKDSSVVKWVVLAEVLVGAVMYMMTKNVKFLAGFAIISVFIAVGMSVVGL
>gnl|CDD|184287 PRK13735, PRK13735, conjugal transfer mating pair stabilization protein TraG; Provisional
MNEVYVIAGGEWLRNNLNAIAAFMGTRTWDSIEKIALTLSVLAVAVMWVQRHNVMDLLGWVAVFVLISLL
VNVRTSVQIIDNSDPAKVYRVDNVPVGLAMPASLTTRIGHAMVQSYEMIFAQPDSVTYSKTGMLFGANLV
AKSTDFLSQNPEIANLFQDYVQNCVMGDIYLNHKYTLEELMNSADPYTLIFSRPSPLRGVYDKNNNFLTC
KDASVTLKDKLNLDTQTGGKTWHYYVQQLFGGRPDPDLLFSQMIGDSYSYFYGSSQSASQIMRQNVTMNA
LREGITSYAARSGDTASLVNLATTSSMEKQRLAHASIGHVAMRTLPMMQTILMGIAIGIFPLLVLAAVFN
KLTLSVLKGYVFALMWLQSWPLLYAILNSAMTFYAKQNGAPVVLSELSQIQLKYSDLASTAGYLSMMIPP
LSWGMVKGLGAGFSSVYSHFASSAISPTASAASSVVDGNYSYNNMQTENVNGFSWDTNSTTSFGQMTYQT
GSGATATQTRDGNMVMDASGAMSRLPVGINATRQIASAQQEMAREASNQAESALHGFSSSIASAWNQLSQ
FGSNRGSSDSVTGGADSTMSAQDSMMASRMRSAVESYAKAHNISNEQATQELASRSTRGSAGGYGDAHAE
WGVGPKILGKGGKLGLGVKGGGRAGIDWSDSDGHSASSSSRSSHDARHDIDAQATKDFREASDYFTSRKV
SESGSHTDNNADSRVDQLSAALNSAKQSYDQYTTNMTRSHEYAEMASRTESMSGQMSENLSQQFAQYVMK
HAPQDAEAILTNTSSPEIAERRRAMAWSFVQEQVQPGVDNAWRESRGDIGKGMESVPSGGGSQDIIADHQ
GHQAIIEQRTQDSGIRNDVKHQVDNMVTEYEGNIGDTQNSIRGEENTVKGQYSELQNHHKTEALSQNNKY
NEEKSAQERMPGADSPEELMKRAKEYQDKHKG
>gnl|CDD|237486 PRK13736, PRK13736, conjugal transfer protein TraK; Provisional
MRKNNTAIIFAALFFSCSVMAASGTLAPTVVPMVNGGQASIALSNTSPNLFTVPGDRITAVSSLDGALTN
NEQTASGGVVLATVNKKPFTFILETERGLNLSIQAVPRAGAGRTIQLVSDLRGTGEEAKAWEESQPYESL
LVALSQAVRGGKLPAGYYQVPVTKETLQAPAGLSLTADRVWTGNHLKVVRYRVENPTLSARNLRESDFWQ
PGTRAVMFSQPARQLLAGGRMDVYVIRDGEGNDGQ
>gnl|CDD|237487 PRK13737, PRK13737, conjugal transfer pilus assembly protein TraU; Provisional
MKRSLWLLMLFLLAGHVPAASADSACEGRFVNPITDICWSCIFPLSLGSIKVSQGKVPDTANPSMPIQIC
PAPPPLFRRIGLAIGYWEPMALTDVTRSPGCMVNLGGSLPAFGKTGQGTAKKDDKQVNGAFYHVHWYKYP
LTYWLNIITSLGCLEGGDLDIAYLSEIDPTWTDSSLTTILNPEAVIFANPIAQGACAADAIASAFNMPLD
VLFWCAGSQGSMYPFNGWVSNESSPLQSSLLVSERMAFKLHRQGMIMETIGKNNAVCNEYPSPILPKERW
RYQMVNMYPDSGQCHPFGRSVMRWETGKNPPNTKKNFGYLMWRKRNCVFL
>gnl|CDD|184290 PRK13738, PRK13738, conjugal transfer pilus assembly protein TraW; Provisional
RCRGLIALLIWGQSVAAADLGTWGDLWPVKEPDMLTVIMQRLQALEQSGEMGRKMDAFKERVIRNSLRPP
AVPGIGRAEKYRSRLFDPSVRLAADIRDNEGRVFARQGEVVNPLQYVPFNQTLYFINGDDPAQVAWMKRQ
TPPTLESKIILVQGSIPEMSKALDSRIYFDQNGVLCQRFGIDQVPARVSAVPGGRFLKVEFIPAEEGRK
>gnl|CDD|237488 PRK13739, PRK13739, conjugal transfer protein TraP; Provisional
MANNMSSRQACHALLYVVARVLRWLFWCVKYAVIWPLATMALMVLFVLWKDNTTPGKLLVQEINFVRQTA
PAGQFPVRECRDPFSSSDSPGPSELQDICHYRAADAADYARETDRSLMQLVTALWATLALMYTSLAVITG
KYPVRPGKMKCIRVVTADEHLKEVYTEDASLPGKIRKCPVYFPDDRTNRNNGDKNEHA
>gnl|CDD|184292 PRK13740, PRK13740, conjugal transfer relaxosome protein TraY
MKRRNTRPAPGRKVSLKLDEDTNNKLIEAKERSGRSKTNEVQIRLRDHLKRFPDFYNSEIFREVAEETES
>gnl|CDD|172283 PRK13741, PRK13741, conjugal transfer protein TraS
MITHKDIKTETEKLKDVLSVGEVNIPSLWQVIKPGLIVMLWMLLWPTFLRFLADKVDIRDAGFDVLASGV
LGFIIFVAITNGRMLYLSIPDEFRKESKVIRFIYSKAKFYILVYLIIIFLIVSFGHSILYGFLSIALFII
FSFIYQVDIGRYQLSAIISVIGLFKKEKKLS
>gnl|CDD|184293 PRK13742, PRK13742, replication initiation protein RepE
MAETAVINHKKRKNSPRIVQSNDLTEAAYSLSRDQKRMLYLFVDQIRKSDGTLQEHDGICEIHVAKYAEI
FGLTSAEASKDIRQALKSFAGKEVVFYRPEEDAGDEKGYESFPWFIKRAHSPSRGLYSVHINPYLIPFFI
GLQNRFTQFRLSETKEITNPYAMRLYESLCQYRKPDGSGIVSLKIDWIIERYQLPQSYQRMPDFRRRFLQ
PCVNEINSRTPMRLSYIEKKKGRQTTHIVFSFRDI
>gnl|CDD|184294 PRK13743, PRK13743, conjugal transfer protein TrbF; Provisional
MNHYKYQRPLSMKEKKNDAELKIRQTKRDYDYERRVSDIYFDLFIVFLTAGIVLWVIMHSIFDACIDSWK
ADPELNNFRYMWNILMYVIPYTLWALAAGFLVAGVRNPLCELINGGIRIFRLKRRMRRENTLREGGNDAS
H
>gnl|CDD|139817 PRK13744, PRK13744, conjugal transfer protein TrbG; Provisional
MNKLVSDGSVKKINYPVLYESGITPPLCEVSAPEPDAGGKRIVAYVYKSSRSTVFENPDIVKTCTVRDLK
KDFVNCDEKGEGQ
>gnl|CDD|237489 PRK13745, PRK13745, anaerobic sulfatase-maturation protein
MKMSTIAPFAKPLYIMLKPVGAVCNLACDYCYYLEKSKLYQENPKHVMSDELLEKFIKEYINSQTMPQVL
FTWHGGETLMRPLSFYKKALELQKKYARGRQIDNCIQTNGTLLTDEWCEFFRENNFLVGVSIDGPQEFHD
EYRKNKMGKPSFVKVMKGINLLKKHGVEWNAMAVVNDFNADYPLDFYHFFKELDCHYIQFAPIVERIVSH
QDGRHLASLAQQEGGELAPFSVTPEQWGNFLCTIFDEWVKEDVGKYYIQLFDSTLANWVGEQPGVCSMAK
HCGHAGVMEFNGDVYSCDHFVFPEYKLGNIYQQTLVEMMYSERQTAFGTMKYKSLPTQCKECEYLFACHG
ECPKNRFCRTANGEPGLNYLCKGYHQFFKHVAPYMDFMKKELMNQRPPANVMDAAKENKLKI
>gnl|CDD|184296 PRK13746, PRK13746, aminoglycoside resistance protein; Provisional
MREAVPAEISTQLSEACAVIERHLEPTLLAIHLYGSAVDGGLKPHSDIDLLVTVAVPLDETTRRALMNDL
LEVSAPPGESEILRALEVTVVVHDDVVPWRYPAKRELQFGEWLRNDILAGIFEPAMIDHDLAILLTKARE
HSVALVGPAAEELFDPVPEQDLFEALRDTLALWNSPPDWAGDERNVVLTLARIWYSASTGKIAPKDVAAD
WALERLPAEYQPVLLEARQAYLGQEEDDLASRADALEAFVRYAKGEIEKVVG
>gnl|CDD|184297 PRK13747, PRK13747, putative mercury resistance protein; Provisional
MNSPERLPSETHKPITGYLWGALAVLTCPCHLPILAAVLAGTTAGAFLGEHWGIAALTLTGLFVLSVTRL
LRAFRGRS
>gnl|CDD|184298 PRK13748, PRK13748, putative mercuric reductase; Provisional
MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVGTSPDALTAAVAGLGYRATLADAP
PTDNRGGLLDKMRGWLGGADKHSGNERPLHVAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVG
CVPSKIMIRAAHIAHLRRESPFDGGIAATVPTIDRSRLLAQQQARVDELRHAKYEGILDGNPAITVLHGE
ARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGLKETPYWTSTEALVSDTIPERLAVIGSSV
VALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAHVDGEFVLTTGHG
ELRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTR
AAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANFDTRGFIKLV
IEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFNKDVKQLSCCA
G
>gnl|CDD|184299 PRK13749, PRK13749, HTH-type transcriptional regulator MerD
MSAYTVSRLALDAGVSVHIVRDYLLRGLLRPVACTTGGYGLFDDAALQRLCFVRAAFEAGIGLDALARLC
RALDAADGDEAAAQLAVLRQLVERRREALADLEVQLATMPTEPAQHAESLP
>gnl|CDD|184300 PRK13750, PRK13750, replication protein; Provisional
MTDLLQTYYRQVKNPNPVFTPREGAGTLPFCEKLMEKAVGFTSRFDFAIHVAHARSLGLRRRMPPVLRRR
AIDALLQGLCFHYDPLANRVQCSITTLAIECGLATESAAGKLSITRATRALTFLAELGLITYQTEYDPLI
GCYIPTDITFTPALFAALDVSEVAVAAARRSRVEWENRQRKKQGLDTLGMDELIAKAWRFVRERFRSYQT
ELKSRGIKRARARRDADRERQDIVTLVKRQLTREIAEGRFTANREAVKREVERRVKERMILSRNRNYSRL
ATASP
>gnl|CDD|184301 PRK13751, PRK13751, putative mercuric transport protein; Provisional
MSEPQNGRGALFAGGLAAILASACCLGPLVLIALGFSGAWIGNLTVLEPYRPIFIGAALVALFFAWRRIY
RPAAACKPGEVCAIPQVRATYKLIFWIVAALVLVALGFPYVMPFFY
>gnl|CDD|184302 PRK13752, PRK13752, mercuric resistance operon transcriptional regulator MerR
MENNLENLTIGVFAKAAGVNVETIRFYQRKGLLPEPDKPYGSIRRYGEADVTRVRFVKSAQRLGFSLDEI
AELLRLEDGTHCEEASSLAEHKLKDVREKMADLARMEAVLSELVCACHARKGNVSCPLIASLQGGAELAG
SAMP
>gnl|CDD|184303 PRK13753, PRK13753, dihydropteroate synthase; Provisional
MVTVFGILNLTEDSFFDESRRLDPAGAVTAAIEMLRVGSDVVDVGPAASHPDARPVSPADEIRRIAPLLD
ALSDQMHRVSIDSFQPETQRYALKRGVGYLNDIQGFPDPALYPDIAEADCRLVVMHSAQRDGIATRTGHL
RPEDALDEIVRFFEARVSALRRSGVAADRLILDPGMGFFLSPAPETSLHVLSNLQKLKSALGLPLLVSVS
RKSFLGATVGLPVKDLGPASLAAELHAIGNGADYVRTHAPGDLRSAITFSETLAKFRSRDARDRGLDHA
>gnl|CDD|184304 PRK13754, PRK13754, fertility inhibition protein FinO
MTEQKRPVLTLKRKTEGETPVRSRKTIINVTTPPKWKVKKQKLAEKAAREAELAAKKAQARQALSIYLNL
PPLDEAVNTLKPWWPGLFDGDTPRLLACGIREVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAG
ACRYDTEGYVTEHISQEEEAYAAERLDKIRRQNRIKAELQAVLDEK
>gnl|CDD|237490 PRK13755, PRK13755, organomercurial transporter MerC
MGLITRIADKTGALGSVVSAMGCAACFPALASLGAAIGLGFLSQYEGLFISTLLPLFAAIALLANALGWF
SHRQWLRSALGMIGPALVLAAVFLLLGNGWSANLLYVGLALMVGVSIWDFVSPAHRRCGPDSCELPAKR
>gnl|CDD|172294 PRK13756, PRK13756, TetR family transcriptional regulator
MARLDKEKVIDSALELLNEVGIEGLTTRKLAQKLGVEQPTLYWHVKNKRALLDALAIEILDRHHTHFLPL
EGESWQDFLRNNAKSFRCALLSYRDGAKVHLGTRPTEKQYETLENQLAFLCQQGFSLENALYALSAVGHF
TLGCVLEDQEHQVAKEERETPTTDSMPPLLRQAIEIMDSDGGEPAFLFGLELIICGLEKQLKCES
>gnl|CDD|172295 PRK13757, PRK13757, type A chloramphenicol O-acetyltransferase
MEKKITGYTTVDISQWHRKEHFEAFQSVAQCTYNQTVQLDITAFLKTVKKNKHKFYPAFIHILARLMNAH
PEFRMAMKDGELVIWDSVHPCYTVFHEQTETFSSLWSEYHDDFRQFLHIYSQDVACYGENLAYFPKGFIE
NMFFVSANPWVSFTSFDLNVANMDNFFAPVFTMGKYYTQGDKVLMPLAIQVHHAVCDGFHVGRMLNELQQ
YCDEWQGGA
>gnl|CDD|172296 PRK13758, PRK13758, anaerobic sulfatase-maturase; Provisional
MPPLSLLIKPASSGCNLKCTYCFYHSLSDNRNVKSYGIMRDEVLESMVKRVLNEAEGHCSFAFQGGEPTL
AGLEFFEELMELQRKHNYKNLKIYNSLQTNGTLIDESWAKFLSENKFLVGLSMDGPKEIHNLNRKDCCGL
DTFSKVERAAELFKKYKVEFNILCVVTSNTARHVNKIYKYFKEKDFKFLQFINCLDPLYEEKGKYNYSLK
PKDYTKFLKNLFDLWYEDFLNGNRVSIRYFDGLLETILLGKSSSCGMNGTCTCQFVVESDGSVYPCDFYV
LDKWRLGNIQDMTMKELFETNKNHEFIKSSFKVHEECKKCKWFPLCKGGCRRCRDSKEDSGLELNYYCQS
YKEFFEYAFPRLINVANNIK
>gnl|CDD|237491 PRK13759, PRK13759, arylsulfatase; Provisional
MVQTKKPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWH
HGRVGYGDVVPWNYKNTLPQEFRDAGYYTQCIGKMHVFPQRNLLGFHNVLLHDGYLHSGRNEDKSQFDFV
SDYLAWLREKAPGKDPDLTDIGWDCNSWVARPWDLEERLHPTNWVGSESIEFLRRRDPTKPFFLKMSFAR
PHSPYDPPKRYFDMYKDADIPDPHIGDWEYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQ
IGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGNRGTVIDQVV
ELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFGQYEGWRPYLHGEHALGYSSDNYLTDGKWKYIWFSQTGE
EQLFDLKKDPHELHNLSPSEKYQPRLREMRKKLVDHLRGREEGFVKDGKLVVGELVKLYLPHYPK
>gnl|CDD|184308 PRK13761, PRK13761, phosphopantothenate/pantothenate synthetase
MIPKSHPRYESLLTREKIVEGVEKGITAKQGLIAHGRGEAFDYLLGEKTTPSALEAERAAAALLLLAKHP
VISVNGNTAALVPEEIVELAEALNAKLEVNLFYRTEERVEKIAEVLREHGAKEVLGTDEDARIPGLDHER
AKVSEDGIYSADVVLVPLEDGDRTEALVKMGKTVIAIDLNPLSRTARTATITIVDNITRAVPNMTEYARE
LKKKDREELEEIVENYDNKKNLSEALKEIRERLTKLAL
>gnl|CDD|237494 PRK13763, PRK13763, putative RNA-processing protein; Provisional
MMMMEYVKIPKDRIGVLIGKKGETKKEIEERTGVKLEIDSETGEVIIEPTDGEDPLAVLKARDIVKAIGR
GFSPEKALRLLDDDYVLEVIDLSDYGDSPNALRRIKGRIIGEGGKTRRIIEELTGVDISVYGKTVAIIGD
PEQVEIAREAIEMLIEGAPHGTVYKFLERKKRELKRRRLE
>gnl|CDD|184311 PRK13764, PRK13764, ATPase; Provisional
MKIVPDTSVVIDGRVSELIEKGEYIGGTIIIPEAVVAELEAQANQGREIGFSGLEELKKLRELAEEGLIE
LEFVGERPTLEQIKLAKGGEIDALIREVAKELGATLVTSDRVQAEVARAKGIDVIYLKPEREPLEIEKFF
DEETMSVHLKEGVPPMAKKGKPGEWKLVKIRDEPLTEEELEEIAREILERAKRDPDGFIEIERRGATVVQ
LGNYRIVIARPPFSDGIEITAVRPVVKLSLEDYNLSEKLKERLEERAEGILIAGAPGAGKSTFAQALAEF
YADMGKIVKTMESPRDLQVPPEITQYSKLEGSMEETADILLLVRPDYTIYDEMRKTEDFKIFADMRLAGV
GMVGVVHATRPIDAIQRFIGRVELGMIPQIVDTVIFIEDGEVSKVYDLEFTVKVPTGMKEEDLARPVIEV
RDFETGELEYEIYTFGEQTVVVPVEEEEEKSPVWRLAEKEIEREIKRYLPGPVEVEVVSDNKAVVYVPEK
DIPKVIGKGGKRIKKIEKKLGIDIDVRPLDEEPGEEAEEGEEVTVEETKKHVILIVGPDYAGKTVDVYAG
GEYLFTATVSRKGEIKVAKNSAIAKELLRAIDEGEDIRVRPV
>gnl|CDD|237496 PRK13766, PRK13766, Hef nuclease; Provisional
MMYIEHPLIKPNTIEARLYQQLLAATALKKNTLVVLPTGLGKTAIALLVIAERLHKKGGKVLILAPTKPL
VEQHAEFFRKFLNIPEEKIVVFTGEVSPEKRAELWEKAKVIVATPQVIENDLIAGRISLEDVSLLIFDEA
HRAVGNYAYVYIAERYHEDAKNPLVLGLTASPGSDEEKIKEVCENLGIEHVEVRTEDDPDVKPYVHKVKI
EWVRVELPEELKEIRDLLNEALKDRLKKLKELGVIVSISPDVSKKELLGLQKKLQQEIANDDSEGYEAIS
ILAEAMKLRHAVELLETQGVEALRRYLERLREEARSSGGSKASKRLVEDPRFRKAVRKAKELDIEHPKLE
KLREIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQASKDGDKGMSQKEQIEILDKFR
AGEFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGRQEEGRVVVLIAKGTRDEAYYWSSR
RKEKKMKEELKNLKGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEEKDKETEEDEP
EGPKIIVDSRELRSNVARHLKRLGAEVELKTLEVGDYVVSDRVAVERKTAEDFVDSIIDRRLFEQVKDLK
RAYERPVLIIEGDLYTIRNIHPNAIRGALASIAVDFGIPILFTRDEEETADLLKVIAKREQEEEKREVSV
HGEKKAMTLKEQQEYIVESLPDVGPVLARNLLEHFGSVEAVMTASEEELMEVEGIGEKTAKRIREVVTSE
YKE
>gnl|CDD|237497 PRK13767, PRK13767, ATP-dependent helicase; Provisional
MIEYATKEYSDEEILDLLRPYVREWFKEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIID
ELFRLGREGELEDKVYCLYVSPLRALNNDIHRNLEEPLTEIREIAKERGEELPEIRVAIRTGDTSSYEKQ
KMLKKPPHILITTPESLAILLNSPKFREKLRTVKWVIVDEIHSLAENKRGVHLSLSLERLEELAGGEFVR
IGLSATIEPLEEVAKFLVGYEDDGEPRDCEIVDARFVKPFDIKVISPVDDLIHTPAEEISEALYETLHEL
IKEHRTTLIFTNTRSGAERVLYNLRKRFPEEYDEDNIGAHHSSLSREVRLEVEEKLKRGELKVVVSSTSL
ELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAGHRLGEVSKGRIIVVDRDDLVECAVLLKKAREGKIDRVH
IPKNPLDVLAQHIVGMAIERPWDIEEAYNIVRRAYPYRDLSDEDFESVLRYLAGDYGGLEEKNVYAKIWL
DEEEGKFGKRGKLARMIYYTNIGTIPDEFKCDVYTEDGKYVGNLEEEFLERLEPGDVFVLGGRTYEFLYS
RGSKVYVDPAEGERPTVPSWFSEMLPLSYDLALEIGKFRREVAEMIEKGGEEAVELLLKEYPIDENAARS
IYGYFLEQYLYTGGSVPTDKRLLIEIYDDEEGRRNYIFHSLYGRRANDALSRAVAYILSKRLNANVRVSV
TDNGFMLSVPLNRKLDIEEVLESLNPENVREILKEALDRTELLKRRFRHNATRSLMILRRYKGREKSAER
QQVNAEMLLKFAKELDDFPVLKETYREILEDYMDIENAEEVLEKIRDGEIEVVIGPVPIPSPFAFNIATL
GASDVVLAEDKRELLKELHERVMEFIREKKGNIELE
>gnl|CDD|237498 PRK13768, PRK13768, GTPase; Provisional
MMYIVFFLGTAGSGKTTLTKALSDWLEEQGYDVAIVNLDPAVEYLPYTPDFDVRDYVTAREIMKKYGLGP
NGALIASVDLLLTKADEIKEEIESLDADYVLVDTPGQMELFAFRESGRKLVERLSGSSKSVVVFLIDAVL
AKTPSDFVSLLLLALSVQLRLGLPQIPVLNKADLLSEEELERILKWLEDPEYLLEELKLEKGLQGLLSLE
LLRALEETGLPVRVIPVSAKTGEGFDELYAAIQEVFCGGEDLT
>gnl|CDD|172307 PRK13769, PRK13769, histidinol dehydrogenase; Provisional
MRRGLPRDVVKSVEKIVDDVAERGLQAALEYSERLDGVAPEAALVEPRPGGDPAVVAAALEAAKSLEALY
SRLKPPEAVDFYGGVLRSVFWKPVRRAALYVPARYVSTLVMLAVPARAAGVEEIYVVTPPRGVTGELLAV
AKELGVKGVLAIGGPHGLAYAVFHMGVDMVAGPGGLYVQAAKYVLSQYVGIDGIEGPTELVVYAEGVPPE
VAVRGALAQLEHGPTSFAYLLSTDAELLKAAEEIYRRERTSSMGPLEVRKVAGVEEAVRFIDEIAPEHLE
VWGRREVAYRVRNVGAVSVNMPSPYLDYVAGISHVLPTGGTARWRGIITPLTFMKPIGVAEAVGELELAE
AARRLAEYEGFQYHREAL
>gnl|CDD|172308 PRK13770, PRK13770, histidinol dehydrogenase; Provisional
MLNAQQFLNQFSLEAPLDESLYPIIRDICQEVKVHGDKALKMYNLTFDHTKTDHLEISHEQIKAAFDTLD
EKTKQALQQSYERIKAYQESIKQTNQQLEESVECYEIYHPLESVGIYVPGGKASYPSTVLMTATLAQVAG
VENIVVVTPPQPNGVSQEVLAACYITQVNQVFQVGGAQSIAALTYGTETIPKVDKIVGPGNQFVAYAKKY
LFGQVGIDQIAGPTEIALIIDETADLDAIVYDVFAQAEHDELARTYVISEDAQVLKDLESRIAKALPNVD
RYDIVSKSIANQHYLIHASNFDEACHVMNTIAPEHASIQTVNPQPYIEKVKYVGALFIGHYSPEVIGDYV
AGPSHVLPTNRTARFTNGLSVNDFLTRNTVIHLSKDTFEQIADSAQHIAHVEALYNHQQSILIRQS
>gnl|CDD|184316 PRK13771, PRK13771, putative alcohol dehydrogenase; Provisional
MKAVILPGFKQGYRIEEVPDPKPGKDEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVG
ENVKGFKPGDRVASLLYAPDGTCEYCRSGEEAYCKNRLGYGEELDGFFAEYAKVKVTSLVKVPPNVSDEG
AVIVPCVTGMVYRGLRRAGVKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSESKAKIVSKYADYV
IVGSKFSEEVKKIGGADIVIETVGTPTLEESLRSLNMGGKIIQIGNVDPSPTYSLRLGYIILKDIEIIGH
ISATKRDVEEALKLVAEGKIKPVIGAEVSLSEIDKALEELKDKSRIGKILVKPS
>gnl|CDD|237499 PRK13773, PRK13773, formimidoylglutamase; Provisional
MTNELPVDIPPPPWTGRTDGDTPEHLRWHQAVRPLDGGAEPGARGCVLLGFASDEGVRRNKGRVGAAAGP
DALRGALGSLALHEPRRVYDAGTVTVPGGDLEAGQERLGDAVSALLDAGHLPVVLGGGHETAFGSYLGVA
GSERRRPGKRLGILNLDAHFDLRAAPVPSSGTPFRQIARAEEAAGRTFQYSVLGISEPNNTRALFDTARE
LGVRYLLDEECQVMDRAAVRVFVADFLADVDVIYLTIDLDVLPAAVAPGVSAPAAYGVPLEVIQAVCDRV
AASGKLALVDVAELNPRFDIDNRTARVAARLIHTIVTAHLPAAT
>gnl|CDD|172313 PRK13775, PRK13775, formimidoylglutamase; Provisional
MLEDYYPSTTSYYHGGIDDDLYTAKWGMVMTFLDLNDSSLTPFEGTHFALIGFKSDKGVYINNGRVGAVE
SPAAIRTQLAKFPWHLGNQVMVYDVGNIDGPNRSLEQLQNSLSKAIKRMCDLNLKPIVLGGGHETAYGHY
LGLRQSLSPSDDLAVINMDAHFDLRPYDQTGPNSGTGFRQMFDDAVADKRLFKYFVLGIQEHNNNLFLFD
FVAKSKGIQFLTGQDIYQMGHQKVCRAIDRFLEGQERVYLTIDMDCFSVGAAPGVSAIQSLGVDPNLAVL
VLQHIAASGKLVGFDVVEVSPPHDIDNHTANLAATFIFYLVQIMAQHS
>gnl|CDD|237501 PRK13777, PRK13777, HTH-type transcriptional regulator Hpr
KSGEKDYSIKEAMLFSQKIAQLSKALWKSVEKDWQQWIKPYDLNINEHHILWIAYHLKGASISEIAKFGV
MHVSTAFNFSKKLEERGYLTFSKKEDDKRNTYIELTEKGEELLLETMEEYDPENNSVFNGALPLRELYGK
FPEFIELMAIVRNIYGDDFIDIFEKSLENIEENFTEEDGKLVKKQ
>gnl|CDD|184320 PRK13778, paaA, phenylacetate-CoA oxygenase subunit PaaA; Provisional
PGAIAAPAAAEDSEKQARFDARIAAGEKIEPKDWMPDAYRKTLIRQISQHAHSEIVGMLPEGNWITRAPS
LKRKAILLAKVQDEAGHGLYLYSAAETLGVSREELIDDLLSGKAKYSSIFNYPTLTWADVGVIGWLVDGA
AIMNQVPLCRCSYGPYARAMVRICKEESFHQRQGEEILLALARGTPAQKQMAQDALNRWWWPALMMFGPP
DDDSPHSAQSMAWKIKRFSNDELRQKFVDATVPQAEVLGLTLPDPDLRWNEERGHYDFGEIDWDEFKEVI
KGNGPCNRERLAARRKAHEDGAWVREAALAHAAK
>gnl|CDD|237502 PRK13779, PRK13779, bifunctional PTS system fructose-specific transporter subunit IIA/HPr protein; Provisional
MLNLSESNIHLNAQAINKQQAIEMAAAALEQAGNVENGYLQGMLARELQTSTFLGNGIAIPHGTLDTRHM
VKNTGVQIFQFPQGIEWGEGNIAYVVIGIAARSDEHLSLLRQLTHVLSDEDTAAKLATLTDVKEFRAILM
GETEPFSVPAANISLDVDTQSLLTLVAINAGKLQEQSAVENRFISEVISNPALPLGKGLWVTDSAVGNQK
NALAFSRAKTIFSHNGKAVQGVITVSAVDDQINPTLARLLDDDVQTTLLNGNSEQIIAALNGIVNTASSS
TAETQSAEGAVIGTFTIRNEHGLHARPSANLVNEVKKFTAKITVENLTRGSAPVSAKSLMKIVALGVTQG
HRLRFVAEGEDAQQAIEALAKAIAEGLGENVSAVPPSEPDTIEVMGDQIHTTAVEEDDNLPANAVEGVFV
IKNEHGLHARPSAVLVNEVKKYNASVAVQNLDRNTQLVSAKSLMKIVALGVVKGHRLRFVATGEEAQQAI
DGIGAAIAAGLGE
>gnl|CDD|237503 PRK13780, PRK13780, phosphocarrier protein HPr; Provisional
MASKDFHITAETGIHARPATLLVQTASKFDSDITLEYNGKSVNLKSIMGVMSLGVGQGADITISAEGADA
ADAIAAIEETMKKEGLAE
>gnl|CDD|172320 PRK13782, PRK13782, HPr family phosphocarrier protein
MVQKRVEVSLKTGLQARPAALFVQEANRFHADIFIEKDGKKVNAKSIMGLMSLAIGTGSMITIITEGSDE
EEALEALAAYVQ
>gnl|CDD|237505 PRK13783, PRK13783, adenylosuccinate synthetase; Provisional
MKRVIVGLQWGDEGKGKVVTYLSRYYDIVVRYSGGANAGHTVNYGDFKVVHHLLPSADFKKNVGAAIGNG
VVLDLEVLVEELEELKEKFPDYSGRIFISELAHVVLPVHKELDEIIESVRKNAIGTTKRGIGPAYADKVM
RVGVRLADLFDEEKLREFLEKILSLYKKLYGIEFDVEKMMEDLLTFYEKIKDLVVSPVEIKRILEEKSVL
FEGTQGVLLDLDVGTYPYVTSSNCSTTGVSAGMGFPVKVDEVIGVFKAYTTRVGEGPFPTELFGEEGEKL
RKAGHEYGATTGRPRRCGWLDLPLLRYAIEVSGVDSLVMTKADVLNGFEKIKVCVRYEIGGKEVRDPSSL
RDLEKAEPVYEEFDGWKSLEDKNFLKFVDFIERETGRKIAYISTGPKIEEIVEV
>gnl|CDD|172322 PRK13784, PRK13784, adenylosuccinate synthetase; Provisional
MSNIVIVGAQWGDEGKGKIADTLAEKADLVVRYQGGNNAGHTLVVNGKKTFLHLIPSGVLHQHTKCVIGH
GVVLDPVALDEEITRLQAKGIAISAENLFVSESCTIITSYHKLLDAVRESNTSEKIGTTGKGIGPAYEDK
VSRKGIKFKHLFDKDLLRSRLAISLAEKETLFRDLYKVEYPTLEQEFDKLFALGQKLKQYAADTFSIIDQ
AIAAGKNVVYEGAQGVLLDVDYGTYPFVTSSNTSVAGVYSGATTAGHGLDHVIGITKAYTTRVGEGPFPT
ELFDDVGKFIQHKGGEIGVTTGRIRRCGWLDLPLLKYSAKCSNLTSIALTKVDVLSDMDTLKVCIGYKYE
GKEIYCAYPGIDLYKVEPILVEMEPFSIDETVTKDNMPAALKTYLKTIENHVGIPISSLAYGPSREQILF
FEDYFKKG
>gnl|CDD|237506 PRK13785, PRK13785, adenylosuccinate synthetase; Provisional
MTVTIVGSQLGDEGKGGVVDLYGDAADVVVRYQGGDNAGHTVVHGGEEYKLSLVPSGAVRGKIGVLGNGC
VVNPETLFDEIDALRERGLDPDVRVAERAHVILPYHRVLDGIEEEAKSDSDLEVGTTGRGIGPTYEDKAG
RRGVRVGDLLDPDVLRDRLEYVVPQKRALAEDVYGLDASETPEAFDVDALFEEYREYGERLAEEDMTVNA
GDFLAERIDDGDNVMLEGAQGTSIDIDHGNYPYVTSSNPTAGGAATGTGLGPTVVGQGEVVGIVKAYLSR
VGSGPLPTELGGVEGDTPDEGGRPDEEELATYIREEGGEYGTVTGRPRRVGWLDMPMLRHAARASGFTGL
AINHIDVLAGLDEVKVGHSYELDGEELLTMPATTERWARCEPNFRSFDGWPEVDWAAVAEEGYDALPENA
RTYLEYVSDELDTPIYAVGVGPGREETVVLENPF
>gnl|CDD|184325 PRK13786, PRK13786, adenylosuccinate synthetase; Provisional
MFTIITGAQFGDEGKGKIVDLLAKDYDIVARFQGGDNAGHTVKVGDEVYKLHLIPSGFLLDARVLIGPGV
VLNPEVLAEEIDMLEKHGVKVDAEKLGIDAKTSIIMPYHIELDGLRESARTEKIGTTKRGIGFAYIDKIA
RDEVRMSDLVDKERLMRRLEELAPQKEKEIKELGGDPSIVRDEALIDKYLELGRQLAPYITDVSYEINKA
LDEGKSVLAEGAQGTHLDVIHGTQKFVTSSSTIAGSACANLGVGPTRVDNVLGIVKAYITRVGEGPLPTE
LKDEAGEHLQDVGGEFGTTTGRPRRCGWFDLPLLKKAIYLNGYTEIALTKLDVLTGLDPIKICVGYELDG
EILDYPPELTSDLARCVPVYEELEGWSTDLTEVKAYEDLPENARNYVERLEELMGVPIKYISVGPGREQT
FKKE
>gnl|CDD|172324 PRK13787, PRK13787, adenylosuccinate synthetase; Provisional
MPASLVVGTQWGDEGKAKVIDFLSKDTDIIVRYQGGANAGHTVVVHGKKYVFHLVPSGVIYDQTICVIGN
GVVLDPLFFIEECDRLQKEGFPVKDKLLLSDACHLLFPYHSQIDSARETTSSQEHKIGTTKKGIGICYAD
KMMRTGLRVGDLLDKSYKRRLKHLVDEKNRELDKLYGMPPVSYNDINDGLKFFLSKVGKNIINTAYYLDT
ELKKGKRVLLEGAQGTGLDVDFGTYPYVTSSNPTTGGALIGTGISFQHLKHVIGITKAYTTRVGEGPFPT
ELLGEAGEVLRQKGGEFGATTGRPRRCGWFDVEMLKHSVRINGITSIALTKIDILSDYDTIPVAVGYKLN
GKTLDCFPSQGLEKVEPLYEEFPGWKDDISGINEFQKLPEKCKNYISALEKWIGVKINLVSTGPDRKDTI
IGD
>gnl|CDD|184326 PRK13788, PRK13788, adenylosuccinate synthetase; Provisional
MPGIAIIGAQWGDEGKGKVVDALAPEADFVVRYQGGANAGHTVVAKGKTFKLNLLPSGVLHPHATSVLGD
GMVIDPFRFAEERENLRAGGLNPKLLISERAHLVLPHHKYVDGRKNFVGTTGRGIGPAYSDRARRVGIRF
GDLLDEAVLRERVERLLEAKPNSTREAGWDTVEKALADLAPMREILLPFIADTGSLLREAIREGKRVLFE
GAQATLLDLNYGTYPYVTSSHPTVGGILVGAGVNHKAINKVYGVAKAFTTRVGHGPFPTEVFGEMAIRLR
GKGGNPWDEFGTTTGRARRVGWLDLVLLKYACEVNGFDGLVLTKLDVLSGLEKVKVCVEYDDDGQPVYKE
LPGWGDLDGVKSREALPKEAQAYLELIEETTGVPVVMFSTSPRREDTYGAVSWV
>gnl|CDD|237508 PRK13791, PRK13791, c-type lysozyme inhibitor
MMKRKLIPFTLFLAALSASTTSIAASQEITKSIYTCNDNQVLEVIYVNTEAGNAYAIISQVDEMIPMRLM
KMASGANYEAINKNYTYKLYTKGKTAELVEGDDKPVLSNCSLA
>gnl|CDD|106733 PRK13792, PRK13792, lysozyme inhibitor; Provisional
MKKALWLLLAAVPVVLVACGGSDDDKQTAQVDYLALPGDAKLDTRSVDYKCENGRKFTVQYLNKGDNSLA
VVPVSDNSTLVFSNVISASGAKYAAGQYIWWTKGEEATLYGDWKGGEPTDGVACKER
>gnl|CDD|184329 PRK13793, PRK13793, nicotinate-nicotinamide nucleotide adenylyltransferase
MYTFDYLVFIGRFQPFHLAHMQTIEIALQQSRYVILALGSAQMERNIKNPFLAIEREQMILSNFSLDEQK
RIRFVHVVDVYNDEKWVKQVKSLVNGVIEPNSKVGLIGHFKDESSYYLRLFPEWVMVELDSLKDSISATP
MREAYYQGKIKTDAFPKGTIQFLEEFQNTPLYLQLQQKFLQADHSNIEETVSSHKE
>gnl|CDD|237509 PRK13794, PRK13794, hypothetical protein; Provisional
MKTYLGKIHLKWCDNCNVPVLGKKCAICGSETREVKVTPPGDARPAFKYDIDLINKILEEQFGIENIPEG
KIVLLNKVPGIERMEEIIVDGAVVGIIRYNEKKHRWKIIPRPEGARRLIPTAKKKFIVVKDDVPKFIRNK
GASVLRPGVAEASEDIEEGDDVIILDENGDVVGVGRARMSYEEIVNMEKGMVVKVRKSEEPKNSNILSEY
GPGEETWKDMVEANKNVLDKYERNSIGFIRNTAEKINKPVTVAYSGGKDSLATLLLALKALGINFPVLFN
DTGLEFPETLENVEDVEKHYGLEIIRTKSEEFWEKLEEYGPPARDNRWCSEVCKLEPLGKLIDEKYEGEC
LSFVGQRKYESFNRSKKPRIWRNPYIKKQILAAPILHWTAMHVWIYLFREKAPYNKLYEQGFDRIGCFMC
PAMELGEIELIKAEYPELWEKWENFLKAWAKKHGLSEEWIKKGLWRWRNKKRENKDSDE
>gnl|CDD|237510 PRK13795, PRK13795, hypothetical protein; Provisional
MSKPVYLGKDHIYWCEKCNVPLLGKKCGICGKEGFKVRLTPPGDVRPAFPYDIEFIRRVLEEEFGCDLIP
EDKLVLLNKIPGEDRADEIIVDGRVIGHLRFDLLELRWRFEPRLEGAKRLLKKRLKKWVIVDKGALEPIK
NGKNVLAPGVVEADLDIKKGDEVVVVTEDGEVVGVGRAKMDGDDMIKRFRGRAVKVRKSGRGSPRLPPGR
ATLEDAIEANRKHLEEKEKEAVNFIRGVAEKYNLPVSVSFSGGKDSLVVLDLAREALKDFKAFFNNTGLE
FPETVENVKEVAEEYGIELIEADAGDAFWRAVEKFGPPARDYRWCCKVCKLGPITRAIKENFPKGCLTFV
GQRKYESFSRAKSPRVWRNPWVPNQIGASPIQDWTALEVWLYIFWRKLPYNPLYERGFDRIGCWLCPSSS
LAEFERLKELHPELYEKWEAFLLKWAKRNGLSEEWVEYGFWRWKRLPPKMLKLAKELGISILPERPEDLS
FEVVSGYSPCKAGGYSAEGSFEVDKGINLERLAEVLKMLGEVVYIEELGMVLTKKGTVKVFASGNIWARS
EDKEAAASLFKDAARLLRRAAECVGCGVCVGACPTGAIRIEEGKRKISVDEEKCIHCGKCTEVCPVVKYK
DKRNGS
>gnl|CDD|106738 PRK13797, PRK13797, allantoicase
MSDAPDLTNLVDLAAARFGGTVVAVNDEFFAFAERMLLAEPPVVRPGVFTERGQWTDGWETRRRRDLPGA
DWAIVRLGAPGIAHAVTVDTTHFTGNAPEAVEIHGATLAGYPSAEDVADDSVHWVELVPRTPIAADAVNV
LPVASSGRLRITHLRLTIHPDGGVARLRVHGTVVPDPRLLDRVTSDLAAAYLGGVVVAASDMHYGDRHNL
NASGDARAMGEGWETRRRRGPGHDWAVVRLATQGTIVRAEVDTRHFRGNAPRAVALWAADAPDLLDPDDL
AAITEWRPLLPRTRVQPNTRHLFDLEVPVQATHVRVDAIPDGGLARLRLTGAPTRSGREALAMRWFDALT
PDAAREELLACCGSEDWASAVAARRPFGTLAALLPAAEQEWWRLPESAWLEAFTAHPRIGERPTQAPAPP
TSARATVVSLDAPRREQAAMDQAAEDVRAAFARGNAAYEERFGFIFLVRAAGRGAEEMLELLRARLAHDP
EQELRIAAGQQAEITALRLRHLITGA
>gnl|CDD|184333 PRK13798, PRK13798, putative OHCU decarboxylase; Provisional
LMHQGMGLAEFNALPERQAVHALFECCHSTAWARRLAAARPFADHDALLAAADEALAGLSEADIDEALAG
HPRIGERPASKASAREQAGVADADEAVMAALAAGNRAYEEKFGFVFLICATGRSADEMLAALQQRLHNDP
ETERKVVREELAKINRLRLERLLGPE
>gnl|CDD|106740 PRK13799, PRK13799, unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional
MAEQLEQLAAADLAAAADLLDGIYEHSPWIAEAAAALGPFPSIAAIKQALAGVLDAADRAAKLDLIRAHP
ELAGKAAEAGELTAESTGEQAKAGLNLCTPEEFAAIQKLNADYGKKFGFPFILAVKGARGAGLAKAEIIA
TFERRLHNHPDDELGEALRNIGRIAEIRINDKFGYTPAIGADVMDWAEDIAAHSDPGYADEGALTCTYLS
DAHRACANQISDWMRDAGFDEVEIDAVGNVVGRYKAADDDAKTLITGSHYDTVRNGGKYDGREGIFLAIA
CVKELHEQGERLPFHFEVIAFAEEEGQRFKATFLGSGALIGDFNMELLDIKDADGISLREAIQHAGHCID
AIPKIARDPADVLGFIEVHIEQGPVLLELDIPLGIVTSIAGSARYICEFIGMASHAGTTPMDMRKDAAAA
AAEIALYIEKRAAQDQHASLVATMGQLNVPSGSTNVIPGRCQFSLDIRAATDEIRDAAVADILAEIAAIA
ARRGIEYKAELAMKAAAAPCAPELMKQLEAATDAAGVPLFELASGAGHDAMKIAEIMDQAMLFTRCGNAG
ISHNPLESMTADDMELSADAFLDFLNNFAEE
>gnl|CDD|237512 PRK13800, PRK13800, fumarate reductase/succinate dehydrogenase flavoprotein subunit
MQIPALTDALRLDCDVLVIGGGTAGTMAALTAAEHGANVLLLEKAHVRHSGALAMGMDGVNNAVIPGKAE
PEDYVAEITRANDGIVNQRTVYQTATRGFAMVQRLERYGVKFEKDEHGEYAVRRVHRSGSYVLPMPEGKD
VKKALYRVLRQRSMRERIRIENRLMPVRVLTEGGRAVGAAALNTRTGEFVTVGAKAVILATGPCGRLGLP
ASGYLYGTYENPTNAGDGYSMAYHAGAELSGIECFQINPLIKDYNGPACAYVANPFGGYQVNAQGERFVD
SDYWSGQMMAEVKREIESARGPIYLKVSHLPEETLSALESILHTTERPTRGTFHANRGHDYRTHDIEMHI
SEIGLCSGHSASGVWVDEHARTTVPGLYAAGDLACVPHNYMIGAFVFGDLAGAHAAGTLAEVPAPGELPA
DQLAEAHELIYRPLRHPDGPPQPQVEYKLRRFVNDYVAPPKTAAKLSIAVETFERMAAEIAGMGARTPHE
LMRCAEVSFIRDCAEMAARSSLTRTESRWGLYHDRADLPERDDASWGYHLNLRKGDDGEMEFLKRPVAPY
FVPVPELDDLPPVDRTVVPVGQPPLHGGRAPAEGVSRAAAPATAPEPPSPRILAVLALDAPSVAELAPYL
ADPDPGVRRTAVAVLTETTPPGFGPALVAALGDGAAAVRRAAAEGLRELVEVLPPAPALRDHLGSPDPVV
RAAALDVLRALRAGDAALFAAALGDPDHRVRIEAVRALVSVDDVESVAGAATDENREVRIAVAKGLATLG
AGGAPAGDAVRALTGDPDPLVRAAALAALAELGCPPDDVAAATAALRASAWQVRQGAARALAGAAADVAV
PALVEALTDPHLDVRKAAVLALTRWPGDPAARDALTTALTDSDADVRAYARRALAHA
>gnl|CDD|184335 PRK13802, PRK13802, bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
MSVLDELVAGALEDQRTRELTVSLEEVKKAAAAAPAPIDATRWLKRADGIPVIAEIKRASPSKGHLSDIP
DPAALAREYEQGGASAISVLTEGRRFLGSLDDFDKVRAAVHIPVLRKDFIVTDYQIWEARAHGADLVLLI
VAALDDAQLKHLLDLAHELGMTVLVETHTREEIERAIAAGAKVIGINARNLKDLKVDVNKYNELAADLPD
DVIKVAESGVFGAVEVEDYARAGADAVLVGEGVATADDHELAVERLVKAGARVKASETTPLSEHQGPYWG
QFGGRYVPEALITALDELERVYTQAKADPEFHKELATLNQRYVGRPSPLTEAPRFAERVKEKTGLDARVF
LKREDLNHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQAL
NVARMRMLGAEVVEVTLGDRILKDAINEALRDWVTNVKDTHYLLGTVAGPHPFPAMVRDFQKIIGEEAKQ
QLQDWYGIDHPDAICACVGGGSNAIGVMNAFLDDERVNLYGYEAGGNGPESGKHAIRFAPGTGELGMFQG
AKSYLLENDEGQTLDTYSISAGLDYASVGPEHAWLKDIGRVNYSWATDEEAMNAFKDLCETEGIIPAIES
SHAVAGAYKAAADLKAKGYEHPVMIVNISGRGDKDMNTAGKWFGYLTDEQAAALEANGATGNNAA
>gnl|CDD|237513 PRK13803, PRK13803, bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
KQPKIKICGIKDSALISKAVDMLPDFIGFIFYEKSPRFVGNKFLAPNLEKAIRKAGGRPVGVFVNESAKA
MLKFSKKNGIDFVQLHGAESKAEPAYCQRIYKKSIKKIGSFLIDDAFGFEVLDEYRDHVKYFLFDNKTKI
YGGSGKSFDWEKFYNYNFKFPFFLSGGLSPTNFDRIINLTHPQILGIDVSSGFEDSPGNKKLTLLKSFIT
NVKKKYLSDPAGRYGTFGGAYVPETLMANLQELQESYTKIIKSNEFQKTFKRLLQNYAGRPTPLTEAKRL
SDIYGARIYLKREDLNHTGSHKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFMG
EEDIKRQALNVERMKLLGANVIPVLSGSKTLKDAVNEAIRDWVASVPDTHYLIGSAVGPHPYPEMVAYFQ
SVIGEEAKEQLKEQTGKLPDAIIACVGGGSNAIGIFYHFLDDPSVKLIGVEAGGKGVNTGEHAATIKKGR
KGVLHGSMTYLMQDENGQILEPHSISAGLDYPGIGPMHANLFETGRAIYTSVTDEEALDAFKLLAKLEGI
IPALESSHALAYLKEGRKKFKKKDIVIVNLSGRGDKDIPTLKEYFENLPQ
>gnl|CDD|237515 PRK13805, PRK13805, bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
MTKEEMAVTNVAELDALVEKAKKAQEEFATFTQEQVDKIVRAAALAALDARIPLAKMAVEETGRGVVEDK
VIKNHFASEYIYNSYKDEKTVGVIEEDDEFGIIEIAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPII
FSFHPRAQKSSIAAAKIVLDAAVAAGAPKDIIQWIEEPSVELTNALMNHPGIALILATGGPGMVKAAYSS
GKPALGVGAGNVPAYIDKTADIKRAVNDILLSKTFDNGMICASEQAVIVDDEIYDEVKEEFASHGAYFLN
KKELKKLEKFIFGKENGALNADIVGQSAYKIAEMAGFKVPEDTKILIAEVKGVGESEPLSHEKLSPVLAM
YKAKDFEDAVEKAEKLVEFGGLGHTAVIYTNDDELIKEFGLRMKACRILVNTPSSQGGIGDLYNKLAPSL
TLGCGSWGGNSVSENVGAKHLLNIKTVAKRRENMQWFKVPKKIYFERGSLPYLLDELDGKKRAFIVTDRF
MVELGYVDKVTDVLKKRENGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIMWL
FYEHPETDFEDLAQKFMDIRKRIYKFPKLGKKAKLVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYEL
TPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGAKDP
EAREKMHNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATDPPKQAAFPQYEY
PRADERYAEIARHLGLPGSTTEEKVESLIKAIEELKAELGIPMSIKEAGVDEADFLAKLDELAELAFDDQ
CTGANPRYPLISELKEILLDAY
>gnl|CDD|237516 PRK13806, rpsA, 30S ribosomal protein S1; Provisional
MTGEKFDTPELDESESFAELLEAYEGERKTELRVGDKITGTVIAITEDSVFVDTGSKVDGVVDRAELLDA
DGELTVAVGDEVELYVVSVNGQEIRLSKALSGQGGAAMLEEAYENGVPVEGKVTGTCKGGFNVEVLGRRA
FCPVSQIDLRYVEDPESYVGQTFQFLITRVEENGRNIVVSRRALLEREQKEALEAFMETVKEGDVVEGTV
TRLAPFGAFVELAPGVEGMVHISELSWSRVQKADEAVSVGDTVRVKVLGIERAKKGKGLRISLSIKQAGG
DPWDTVGDRLKAGDKVTGKVVRLAPFGAFVEILPGIEGLVHVSEMSWTRRVNKPEDVVAPGDAVAVKIKD
IDPAKRRISLSLRDAEGDPWADVAERFAPGTTVTGTVEKRAQFGLFVNLAPGVTGLLPASVISRAGKPAT
YEKLKPGDSVTLVVEEIDTAKRKISLAPAGAAGSGADDDDWKQFAPKKSAPASGGLGSLGQALQEAMKKK
K
>gnl|CDD|237517 PRK13807, PRK13807, maltose phosphorylase; Provisional
MKRIFEVDPWKIITHGFDPEDKRLQESLTSLGNGYMGMRGNFEETYSGDTLQGTYIAGVWFPDKTRVGWW
KNGYPEYFGKVINAPNFIGIDIRIDGEELDLAKCEVSDFELELDMKEGVLTRSFTVLKNGKEVRVEAERF
LSIAQKELAVIKYSVTSLNGEAKITFDSYLDGDVKNEDSNYDEKFWQVLEKGADATRAFIVTKTKPNPFG
VPQFTVAAKMSNRTNGKVVPGVETKEKYVENSFTADVKAGETVTLEKRVIVVTSRDYEESELLKAAEDLL
NKAAEKGFEELLAAHTAAWAKRWEKSDVVIEGDDAAQQGIRFNIFQLFSTYYGEDARLNIGPKGFTGEKY
GGATYWDTEAYCVPFYLATADPEVTRNLLKYRYNQLPGAKENAKKQGLKGALYPMVTFNGIECHNEWEIT
FEEIHRNGAIAYAIYNYTNYTGDESYLKEEGLEVLVEIARFWADRVHFSKRKNKYMIHGVTGPNEYENNV
NNNWYTNYIAAWTLEYTLENLDKVKKEAPARLNVTEEELAKWQDIVDKMYLPYDEELGIFVQHDGFLDKD
LRPVSDLPPDQRPINQNWSWDRILRSPFIKQADVLQGIYFFEDRFTKEEKRRNFDFYEPLTVHESSLSPC
VHSILAAELGKEDKAVELYLRTARLDLDNYNNDTEDGLHITSMAGSWLAIVQGFAGMRVRDGQLSFAPFL
PKEWTSYSFKINFRGRLLKVKVDKQEVTIELLSGEPLTIEVYGKKVELKKGVTVTV
>gnl|CDD|172341 PRK13808, PRK13808, adenylate kinase; Provisional
MRLILLGPPGAGKGTQAQRLVQQYGIVQLSTGDMLRAAVAAGTPVGLKAKDIMASGGLVPDEVVVGIISD
RIEQPDAANGFILDGFPRTVPQAEALDALLKDKQLKLDAVVELRVNEGALLARVETRVAEMRARGEEVRA
DDTPEVLAKRLASYRAQTEPLVHYYSEKRKLLTVDGMMTIDEVTREIGRVLAAVGAANAKKAAKTPAAKS
GAKKASAKAKSAAKKVSKKKAAKTAVSAKKAAKTAAKAAKKAKKTAKKALKKAAKAVKKAAKKAAKAAAK
AAKGAAKATKGKAKAKKKAGKKAAAGSKAKATAKAPKRGAKGKKAKKVTKKRA
>gnl|CDD|184340 PRK13809, PRK13809, orotate phosphoribosyltransferase; Provisional
MMNYEDAKLRDQAVAILYQIGAIKFGKFILASGEETPIYVDMRLVISSPEVLQTIATLIWRLRPSFNSSL
LCGVPYTALTLATSISLKYNIPMVLRRKELKNVDPSDAIKVEGLFTPGQTCLVINDMVSSGKSIIETAVA
LEEEGLVVREALVFLDRQKGACQPLGPQGIKLSSVFTVPDLIKSLISYGKLSSGDLTLANKIIKIL
>gnl|CDD|237520 PRK13813, PRK13813, orotidine 5'-phosphate decarboxylase; Provisional
EKDSRIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYAPVIADLKVADIPNTNR
LICEAVFEAGAWGIIVHGFTGRDSLKAVVEAAAESGGKVFVVVEMSHPGALEFIQPHADKLAKLAQEAGA
FGVVAPATRPERVRYIRSRLGDELKIISPGIGAQGGKAADAIKAGADYVIVGRSIYNAADPREAAKAINE
EIRGA
>gnl|CDD|139876 PRK13814, pyrB, aspartate carbamoyltransferase
MNELPLHLLNMRSLTRDHIEKLIQRANYFLTQGMEKNSVFETLKGHVVANLFFEPSTRTRNSFEIAAKRL
GAMVLNPNLKISAISKGETLFDTIKTLEAMGVYFFIVRHSENETPEQIAKQLSSGVVINAGDGNHQHPSQ
ALIDLMTIKQHKPHWNKLCVTIIGDIRHSRVANSLMDGLVTMGVPEIRLVGPSSLLPDKVGNDSIKKFTE
LKPSLLNSDVIVTLRLQKERHDNSVDIDAFRGSFRLTPEKLYSAKPDAIVMHPGPVNREVEINSDVADNQ
QSVILQQVRNGVAMRMAVLELFLLRDFRFF
>gnl|CDD|172345 PRK13815, PRK13815, ribosome-binding factor A; Provisional
MFKRSEKVAEAIHELISGLLVKGLKDPRIGFVTITGVKVTDDLHLATIYFTVIGDDEAKKSTEAGLNSAR
GFIRKELGKVLRMRYAPELIFKYDESQEYGNRIDSLLKEIGTEHDGDDSEDS
>gnl|CDD|184344 PRK13816, PRK13816, ribosome-binding factor A; Provisional
GNQRLKRMADSVQRELSELIRQELKDPRLGGLVTISSVKVSPDLGYADVYVTVMGRELSDDQNEVAHRET
LDVLNKASGFLRTELSRRIKTRITPRLRFHYDKTNAYGNYMFGLIEKAVQDLPKRESDDEE
>gnl|CDD|139879 PRK13817, PRK13817, ribosome-binding factor A; Provisional
MSQRQQRVADLIHQQLAELLKKEVRDSRLSKISLTAVSISPDLKQAKVFYSLLENQNEKEVQKALNKATG
YLRHLLAQATVLRYVPKLEFVYDESIERAHRISLLIERALKKDDSDESS
>gnl|CDD|184345 PRK13818, PRK13818, ribosome-binding factor A; Provisional
MKHRIGRVEGEILRELTKILRKNIRDPRLSDVTITAVECTNDLSYATVYYSLLTEDEAKEKEVQEGLEKA
KGMMRHLLGQTLTVYKVPELIFKRDNSVAYGSKIDRLIAEVKKQDQERENK
>gnl|CDD|237521 PRK13820, PRK13820, argininosuccinate synthase; Provisional
MMKKVVLAYSGGLDTSVCVPLLKEKYGYDEVITVTVDVGQPEEEIKEAEEKAKKLGDKHYTIDAKEEFAK
DYIFPAIKANALYEGYPLGTALARPLIAEKIVEVAEKEGASAIAHGCTGKGNDQLRFEAVFRASDLEVIA
PIRELNLTREWEIEYAKEKGIPVPVGKEKPWSIDENLWSRSIEGGKLEDPAFEPPEEIYAWTVSPEDAPD
EPEIVEIEFEEGVPVAINGEKMDGVELIRKLNEIAGKHGVGRTDMMEDRVLGLKSRENYEHPAATVLLTA
HKALEQLVLTREELKFKEIVDSKWAELAYEGLVDEPLREDLNAFIDKTQERVTGTVTVKLYKGSARVVGR
ESPYALYSEELVSFDSKTIDQRDAEGMAKYHGLQARLYNKVKRK
>gnl|CDD|184347 PRK13821, thyA, thymidylate synthase; Provisional
MKQYLDLVRTILDTGTWQENRTGIRTISIPGAMLRFDLQQGFPAVTTKKLAFKSAIGELVGFLRASRSAA
DFRALGCKVWDQNANENAQWLANPYRQGVDDLGDVYGVQWRQWPGYKVLDASADAQIADATSRGFRIVAR
FDEDGAPKVLLYKAIDQLRQCLDTIMNNPGSRRILFHGWNPAVLDEIALPACHLLYQFLPNVETREISLC
LYIRSNDVGLGTPFNLTEGAALLSLVGRLTGYTPRWFTYFIGDAHIYENQLDMLQEQLTREPYESPRLVI
SDRVPEYAKTGVYEPEWLEKIEPSDFSLVGYRHHEPLTAPMAV
>gnl|CDD|237522 PRK13822, PRK13822, conjugal transfer coupling protein TraG; Provisional
RMTTNRQLLLILPPILMGALTIFLVGWEWWLAAFGKTPQAAYWLGRAGPALPLVLAAAAGLLFLFAAAGH
RRIKPAGWGVLAGFLGVIAIYALREYIRLSPFVGQVPATDSALSYADPATVIGAVVGFFAGAFALRVSLV
GNAAFARAEPRRIRGKRAIHGDADWMKMKEAAKLFPPDGGIVIGERYRVDKDSVAALPFRPDDRTTWGKG
GKAPLLTFDGDFGSTHGLVFAGSGGFKTTSVVVPTALKWGGPLVVLDPSTEVAPMVSEHRRDAGREVIVL
DPTNPGTGFNVLDWIGRSGGTKEEDIVAVASWILSDSKRTESSRDDFFRNSAHQLLTALLAHVCLSGEYE
GKERTLRTLRAILSEPEPSLRARLRDIYENSESDFIRENVGVFVNMTEQTFSGVYATASKDTQWLSYPNY
AALVSGNSFSTSDLAAGNTDVFINIPLKILESYPGLARVIIGSLLNAMYNADGNVKGRALFLLDEVARLG
YMRILETARDAGRKYGITLMLIYQSIGQLREHFGGRGATSWFESASWISFAAIKDLDTADYISERCGEMT
VEVDQTSRSSGWSGSSRSRSKQLQRRPLIMPHEILQSMRADEQIIFVQGNPPLRCGRAIYFRRKEMKACV
GENRFAKQATG
>gnl|CDD|184348 PRK13823, PRK13823, conjugal transfer protein TrbD; Provisional
MALRRIPIRRAGNRPNLFMGGDRELVMFSGLLAGILIFVAQTWRAALFGIALWFGALFALRLMAKADPKM
RHVYLRHRRYKPYYPARSTPFREN
>gnl|CDD|184349 PRK13824, PRK13824, replication initiation protein RepC; Provisional
METGSVTTPFGRRPMTLALLASQRAAREIPPGKSVDKWKLFRDLCEARALLGVSDRALAVLNALLSFYPE
TELSEEAGLVVFPSNAQLSLRAHGMAGATLRRHLAALVEAGLIIRRDSPNGKRYARKGRGGEIEEAFGFD
LAPLLARAEEFEALAEQVAAERKALRRLRERLTLCRRDIAKLIEAAIEEGVPGDWEGVEQRFRAIVARLP
RRATLAELEPILDELEALREEVVNLLESHLKSENMSGNESQNERHIQNSNPDSIFELEPSSEKKQGASAA
EKPEPRREPIKSFPLGMVLRACPEIADYAPGGAIRSWRDLMAAAVVVRSMLGVSPSAYQEACEVMGPENA
AIVIACILERAGHINSAGGYLRDLTRRAERGEFSLGPMLMALLRANGAAARRAG
>gnl|CDD|237523 PRK13825, PRK13825, conjugal transfer protein TraB; Provisional
MRRDVLQALALILAGAAIGFLGWSGHVLLLPLALAFPVLWANSPSRLAAALVSAGYFLAASRGLPQGVAA
FFGSDLWPGLALWLAASLSFVLVHAALWTAPRGRARALRYLLAAVLMAVPPFGITGWAHPLTAAGVLFPG
WGWWGLGATAAGLAGLTTRLWPAVAIALVGLWLWSAAAWTLPRAPAGWVGVDTQLGRSLGRDASLERRRE
LIATVRAAAAAGARVVVLPESALGFWTPTTERLWRESLRGSDVTVIAGAAVVDPGGYDNVLVAISAGGGR
ILYRERMPVPVSMWQPWRPWTGQGGGARAHFFANPVVEIDGRRAAPLICYEQLLVWPVLQSMLHSPDVIV
AVGNGWWTKGTSIVAIQRASAEAWARLFGVPLVRAFNR
>gnl|CDD|237524 PRK13826, PRK13826, Dtr system oriT relaxase; Provisional
MAIPHFSVSIVSRGSGRSAVLSAAYRHCAKMEYEREARTIDYTRKQGLLHEEFVLPADAPEWVRSMIADR
SVSGASEAFWNKVEAFEKRSDAQLAKDVTIALPLELTAEQNIALVRDFVEKHILAKGMVADWVYHDAPGN
PHVHLMTTLRPLTEDGFGAKKVAVIGEDGQPVRTDAGKIVYELWAGSTDDFNALRDGWFACQNHHLALAG
LDLRIDGRSYEKQGIELEPTIHLGVGAKAIERKAEQQGVRPELERIELQEERRSENARRIQRRPEIVLDL
ITREKSVFDERDVAKVLHRYVDDPAVFQSLMARILQSPEVLRLERERIDFATGIRVPARYTTRAMIRLEA
EMARRAIWLSGRSSHGVREAVLAATFARHARLSDEQKTAIEHVAGPARIAAVVGRAGAGKTTMMKAAREA
WEAAGYRVVGGALAGKAAEGLEKEAGIQSRTLSSWELRWNQGRDQLDNKTVFVLDEAGMVASRQMALFVE
AVTRAGAKLVLVGDPEQLQPIEAGAAFRAIADRIGYAELETIYRQREQWMRDASLDLARGNVGKALDAYR
ANGRVIGSRLKAEAVESLIADWNRDYDPTKTTLILAHLRRDVRMLNEMARAKLVERGIVGEGHAFRTADG
ERRFAAGDQIVFLKNEGSLGVKNGMIGKVVEAAPNRIVAEIGEGEHRRQVTVEQRFYNNLDHGYATTIHK
SQGATVDRVKVLASLSLDRHLTYVAMTRHREDLQLYYGRRSFAFNGGLIPVLSRRNAKETTLDYERGKLY
RQALRFAENRGLHLVNVARTLARDRLDWTLRQKQKLADLGARLRAIGERLGLAQSPKTQTMQNSKEAAPM
VAGITTFPKSVADTVEDKLAADPALKKQWEEVSTRFHLVYADPETAFKAVNFDAMLKDKEVAKSTLQKLA
AEPESFGALKGKTGILASKADRQDRERAEVNVPALKRDLERYLRMREEAERKHEAEERALRQRVSIDIPA
LSPAARQVLERVRDAIDRNDLPAALEYALADRMVKAEIDGFNKAVTERFGERTFLPNAAREPSGKTFEKV
TAGMTPGQKEELKSAWPVMRTAQQLAAHERTTEALKQAETLRQTQSQGLSLK
>gnl|CDD|184351 PRK13828, rimM, 16S rRNA-processing protein RimM; Provisional
VRGEVRLKSFTEDPLAIADYGPLTTEDGARSFTVALARPAKDGLVARLKGVATREAAEALRGLELYVPRD
RLPELDDDEFYHADLIGLAAVDTGGALLGRVKAVHNFGAGDILEIAPPGGGPTLLLPFTRAVVPTVDLAA
GRVVADPPAEIEGDEPPEPDA
>gnl|CDD|184352 PRK13829, rimM, 16S rRNA-processing protein RimM; Provisional
MRRTEIGRFGGPYGVQGGLKFRGEPVVLDLPRVYVEGLGWRAIERAERVGPELVLHLAGVTSREGAEALV
GLRVYADDADLPPLEEGSYYYHELRGLPVYVDGEPLGEVVDVEDAGAQDLLVIRHVGGSLRARATYFVPL
QAPYVRVELDGITADAIPGLLD
>gnl|CDD|237525 PRK13830, PRK13830, conjugal transfer protein TrbE; Provisional
MVALKRFRHSGPSFADLVPYAGLVDNGVILLKDGSLMAGWYFAGPDSESSTDAERNEVSRQINAILSRLG
SGWMIQVEAVRVPTIDYPAEDDCHFPDPVTRAIDAERRAHFERESGHFESRHALILTYRPPEPRRSGLTR
YIYSDEESRSASYADTALDSFRTSIREVEQYLANVVSIRRMETRETVERGGFRVARYDELFQFIRFCITG
ENHPVRLPDIPMYLDWLVTAELQHGLTPKVENRFLGVVAIDGLPAESWPGILNSLDLMPLTYRWSSRFIF
LDAEEARQKLERTRKKWQQKVRPFFDQLFQTQSRSVDQDAMMMVAETEDAIAQASSQLVAYGYYTPVIVL
FDEDQERLQEKAEAIRRLIQAEGFGARIETLNATDAFLGSLPGNWYANIREPLINTRNLADLIPLNSVWS
GSPVAPCPFYPPNSPPLMQVASGSTPFRLNLHVDDVGHTLIFGPTGSGKSTLLALIAAQFRRYAGAQIFA
FDKGRSMLPLTLAAGGDHYEIGGDAAEEGEGLAFCPLAELSTDGDRAWAAEWIETLVALQGVTITPDHRN
AISRQIGLMAEARGRSLSDFVSGVQMREIKDALHHYTVDGPMGQLLDAEEDGLALGAFQTFEIEELMNMG
ERNLVPVLTYLFRRIEKRLTGAPSLIILDEAWLMLGHPVFRDKIREWLKVLRKANCAVVLATQSISDAER
SGIIDVLKESCPTKICLPNGAAREPGTREFYERIGFNERQIEIVATAIPKREYYVASPEGRRLFDMSLGP
VALSFVGASGKEDLKRIRALHSEHGADWPIHWLQQRGIAHAATLFPAA
>gnl|CDD|172358 PRK13831, PRK13831, conjugal transfer protein TrbI; Provisional
MVQSLQLGGAANSEDASGMRRLNRLPIIVAIVLVVLFLGVIFYGLSSRGLYFRRDDGPETSSGTPASTFA
DQLKRGVTDGIIGEPQQQQTFQPTPVETQQEEKAVNPFTPQPGQREERRPTLESEEEWRARLKREQEEQY
LRERQRQRMARLQANAAAYDSPLAVDIGKVEKRTADTNDTATQTTNATSTAGASDLYAAAMRAGLGGQNV
DPNGQKSKEDFFNADIKDLGYLPNRVVPQQSPYELKRGSVIPATLITGINSDLPGRITAQVSQNVYDSAT
GHRLLIPQGTKLFGRYDSKVSFGQSRVLVVWTDIIFPNGSTLQIGGMAGTDAEGYGGFKDKVDRHYLRTF
GSAILIALIGTGIDMAVPESSTLATQDTASDAARRNFAETFGRVAERTISKNLNVQPTLEIRPGYKFNVL
VDQDIVFPGAYR
>gnl|CDD|184353 PRK13832, PRK13832, plasmid partitioning protein; Provisional
MELRKVDPRALKDNPDNTRRSKSSPQSDALLLATIKAVGIVQPPVVSPEEDGGNGYIIQAGHRRVKQAIA
AGLEEIEVLVTEAANDNGAMRSMVENIAREPLNPVDQWRAIERLVALGWTEEAIAVALALPVRQIRKLRL
LANVLPAMLDHMAKGDMPNEQQLRTIAAASLDEQKEVWKAHKPKKGDPQVSWWDIARALSKTRMYARDAS
FGDDLAQAYGIVWVEDLFAPADEDSRYTTDVEAFLGAQQEWMANNLPKKGAIIEVNEWGQPKLPPKAERV
YGKPGKSDHVGMYLDRDGKVQSVAYRMPEPKKPKKGGAAVGGADADDTPVAAKPRPDVTQKGLDMIGDFR
TDALHEALGRAPIEDDTLMALLVLAFAGQNVRVDSGASDTVYGHKRFARHAARLIGEDGKLAFDRETLRV
AARSVLIDVLSCRRNMSNSGVVARIAGDAIGADAFLPNMGTEDFLSCLSRPALEAACKDTGVLPRQKVKE
TRAALVEHFKDGHFVHPAALFAPDPEDIAE
>gnl|CDD|172360 PRK13833, PRK13833, conjugal transfer protein TrbB; Provisional
MTQLRSHPRLVRKLQDALGDQLCVALDDATVVEIMLNPDGKLFIERLGHGVAPAGEMSAAAAEVVIGSVA
HALQSEADDERPIISGELPIGGHRFEGLLPPVVSGPAFTIRRRASRLIPLDDYVTSKIMTEAQASVIRSA
IDSRLNIVISGGTGSGKTTLANAVIAEIVASAPEDRLVILEDTAEIQCAAENAVALHTSDTVDMARLLKS
TMRLRPDRIIVGEVRDGAALTLLKAWNTGHPGGVTTIHSNTAMSALRRLEQLTAEASQQPMQEVIGEAVD
LIVSIERTGKGRRVREVIHVEGFANGRYQTEHYAQIDEDSHVA
>gnl|CDD|172361 PRK13834, PRK13834, putative autoinducer synthesis protein; Provisional
MRILAISPDQYEREASLLKQMHRLRARVFGGRLGWDVSITDGEERDQFDDLKPTYILAISDSGRVAGCAR
LLPAIGPTMLAQVFPQLLPAGRLNAHPAMIESSRFCVDTALAEGRGGGQLHEATLTMFAGIIEWSMANGY
TEIVTATDLRFERILARAGWPMQRLGEPKAIGNTMAVAGILPADRDSFERVRPPGYRSDLGAIRRAA
>gnl|CDD|172362 PRK13835, PRK13835, conjugal transfer protein TrbH; Provisional
LRRLLAACILALLLSGCQTLATDGLTTSSAPAELSGPAASAIAGDMVSRLAEQIGPGTTTIKLKKDTSPF
GQALEAALKGWGYAVVTDQKTDKGPKPVELAYVVDSFDGQVLARLSTPSIELGRAYTVTATGATPASPLS
VMKRG
>gnl|CDD|172363 PRK13836, PRK13836, conjugal transfer protein TrbF; Provisional
MAGNTPPDNPYLAARQEWNERYGSYVKAAAAWRIVGILGLTMAVIGFGYALYQSTQVKLVPYIVEVDKLG
TAVNAGFPQQIEYADPRVVRATLGSFVTNFRSVTPDAVVQKQYIDRTYALLRTSDPSTEKVNAWFRSNSP
FEKAKNATVAIEVNNIVALSNQSYQIDWTEFERDRKGKETATRRFRGIATVTLTPPQDEATIRLNPIGLY
LRDFDWTAQL
>gnl|CDD|237526 PRK13837, PRK13837, two-component system VirA-like sensor kinase
MKAAPWSILVLLVAALLFALLAIGLWQDNERYDAILRALDAIDMAEASLQRDVLRARAGLLRNYDPLVRR
LGALRDALADLRRLADGDAELDQLLDRLKASVDRTDAAVEAFKSQNALLQNSLAYFNSLSSALPRSDSTD
APARAASELASAMLRFSLDPSPALAAEIRRRLDRLAQRAGSDPASVRALLRHGRMILRLLPRVDDTVRVL
QASDTLASAEALRRAILEAYSLAQARARRVRLFLGAVSVALLGYIISLVLRLRARTRVLRRRAAFEEVIA
AISRCFEAASPHELEASIEAALGILAKFFDADSAALALVDVGGRARIWTFPGLTPDPVWPDRLRALASTV
KAAERDVVFVDRNGPVRKRSCLTRRGPALWACLAFKSGDRIVALLGLGRQRYGLRPPAGELQLLELALDC
LAHAIERRRLETERDALERRLEHARRLEAVGTLASGIAHNFNNILGAILGYAEMALNKLARHSRAARYID
EIISAGARARLIIDQILAFGRKGERNTKPFDLSELVTEIAPLLRVSLPPGVELDFDQDQEPAVVEGNPAE
LQQVLMNLCSNAAQAMDGAGRVDISLSRAKLRAPKVLSHGVLPPGRYVLLRVSDTGAGIDEAVLPHIFEP
FFTTRAGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSSKVPVAPQAFFGPGPLPRGRGETV
LLVEPDDATLERYEEKLAALGYEPVGFSTLAAAIAWISKGPERFDLVLVDDRLLDEEQAAAALHAAAPTL
PIILGGNSKTMALSPDLLASVAEILAKPISSRTLAYALRTALATARAAAARAEGTPAL
>gnl|CDD|172365 PRK13838, PRK13838, conjugal transfer pilin processing protease TraF; Provisional
MRRRRALLLLAVAAVAASGLAATAWIGGYRINLTPSEPLGLWRIEALDRPVAVGDLVFICPPETAAFREA
RERGYLRRGLCPGGFAPLIKTVAALAGQRVEIGGSVSIDGRPLPSSSVRRRDGEGRPLTPFPGGVVPPGH
LFLHSSFAGSYDSRYFGPVPASGLLGLARPVLTFDP
>gnl|CDD|237527 PRK13839, PRK13839, conjugal transfer protein TrbG; Provisional
RTGLTLAAGCLVALVVPFGALLSSRALAAQSMTANEAKGTGISGQWRGSPGLVTKGPDGKVIFLFGETQP
SVVCSPLQVCDIELQGGEVVRDVLVGDTVRWKVEPATSGAAGGQAIHLIVKPSEPGLVTSMVVTTSRRTY
HIQLKSHPTQYMARVGFEYPEDVSTKLADINARLEASTIPGAGVPAEQLNFSYSVSGSASWRPTRVYSDG
LKTYIQFPRSISGQDAPVLFVVSGGQNRIVNYRMKNDMMVVDYNIDRAVLVSGVGWKQQKITIRRGG
>gnl|CDD|237529 PRK13841, PRK13841, conjugal transfer protein TrbL; Provisional
RRKLERAFLIAGIVALAYAAPAFAQQGSVLTTLENQVVTAAKGWETTVMNAARSLFWILAGIEIGIAAVW
LAIQAASLDSWFAELVRRIMFIGFFAFILDQGPTFAKAVVDSLFQIGAGGGSASPANVFDAGIRVASKMS
EQAKFGLFEDNALAIAAVFAMVVVVISFSLVAAIFVSVMVEMYVGLLAGMIMLGLGGSSFTKDFAVRYLV
YAFSVGMKLMALVMIAKIGSDVLLGLAEAPTATSDQFITTLAIAGISVVVFIIAMYVPNIIQGVVQGASV
SGGMEAIRHGGQAASFAAGAAFLAAGAAGAGFAAASAARAGGSSLAGAALRGMGAGIGSAGSAAGSAAKE
KAIGSPGAYAGSLLGLANAKLDQQRGGPSAPPPPPPVNDKK
>gnl|CDD|172369 PRK13842, PRK13842, conjugal transfer protein TrbJ; Provisional
MPHRFSKPNRALAVAMIAALTIGVASPAFAGGATGGATEWTQLLNNAELISLVGQSAEQINNQITQISQL
AEQIQNQLNIYQNMLQNTAQLPNHIWGQVENDLNRLRSIVNQGQGIAFSMGNADDVLKQRFQSYADLKTN
LPDGQSFSSTYQTWSDTNRDTIAGTLKAASLTADQFSSEESTMSSLRSMSESADGQMKALQVGHQIAAQQ
VAQMQKLRGLVSQQMTMMGTWLQSEQTDKDLAQARREKFFNATVPSIPGGQKMEPRW
>gnl|CDD|237530 PRK13843, PRK13843, conjugal transfer protein TraH; Provisional
MVDAALIKQCADPSLKPAIVEQFIEAAGSPDPLAVTVRSGGRLVLVPKPKTPDEAMALIRQYVGQAVVRV
GLTQYPAGVGVVDAGQLKPDLVDACENLRMGTALFAKVYRIVTKWYGNPTSKDVLPQVFDDAIYAWKTGY
FEGVAVFRAEDPGDVKLAEPEPGDSDEAEESSDPPENAEDASEPAEPDDPNKAGIRIDLSGIGAQKQ
>gnl|CDD|172371 PRK13845, PRK13845, putative glycerol-3-phosphate acyltransferase PlsX; Provisional
NEPRSKTNRPRAIRRLVIWYRRNSAVTSLVDTAASSASAAGNVAGTVVSSAGSVVSTAGSIAKSTLQPLV
FDPLRRLQGSDNNLDKEEISDSDRIWVAVDGMGGDYAPGPILEGCLQAISRLPLNIKFVGEIEKVKEAAE
ALGLEELLEKAIDAGHLELIASGPSIGMDEEATAVRKKKDASINVAMDLVKKGKALAVYSAGNSGAMMAS
AIFRLGRLKGIDRPAIGALFPTKDPGQPVLVLDVGANMDCKPSYLHQFALLGNIYSRDVLQVKKPRIGLL
NIGEEECKGNDLSLKTFELLSEEKRFHFAGNCEGRDVLSGDFDVVVCDGFTGNVLLKFLESVGSVLLDVL
RAELPRGRRGKVGSAFLRSNLKRIKKRLDHAEHGGALLLGVNGICVIGHGSSKALSVVSALRLAHSAASH
GVMDDLAQLQKLQVLNS
>gnl|CDD|139906 PRK13846, PRK13846, phosphate acyltransferase PlsX
MKVQIGIDLMGGDHSPLVVWEVLGDVLLSSSSEQPVEFTVFASSEVHHQILSNSPLSRSPRIITAEDFVS
MEDSPLAAIRKKSSSMALGLDYLQEDKLDAFISTGNTAALVTLARAKIPMFPAVPRPALLVSVPTMRGFA
VILDVGANVSVNPEEMVGFARMGLAYRQCLGSNQPPTLGLLNIGSEERKGTEAHRQTFRMLRETFGSAFL
GNIESGDVFSGKVDIVVTDGFTGNIFLKTAEGVFDFLRHILGDKLEKDIKRQLDYTIYPGSIVCGLSKLV
IKCHGKACGTSLFGGISGSIDLARARVCSRILSRLG
>gnl|CDD|172372 PRK13847, PRK13847, type IV conjugative transfer system coupling protein TraD
MARTMTSDARKKDTREKIELGGLIVKAGLRYEKRALLLGALIDAGRRIKGDEGERSRLTAIGAEAFGNDG
E
>gnl|CDD|172373 PRK13848, PRK13848, conjugal transfer protein TraC; Provisional
MKKPSSKIREEIAKLQEQLKQAETREAERIGRIALKAGLGEIEIEEAELQAAFEELAKRFRGGKGAATGK
RNGGDGRTASESTATVASGAAAGGTGEA
>gnl|CDD|139909 PRK13849, PRK13849, conjugal transfer ATPase VirC1
MKLLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEADENRPLTRWKENALRSNTWDPACEVYAADELP
LLEAAYEDAELQGFDYALADTHGGSSELNNTIIASSNLLLIPTMLTPLDIDEALSTYRYVIELLLSENLA
IPTAILRQRVPVGRLTTSQRAMSDMLESLPVVDSPMHERDAFAAMKERGMLHLTLLNLSTDPTMRLLERN
LRIAMEELVTISKLVSEALEA
>gnl|CDD|237531 PRK13850, PRK13850, type IV secretion system protein VirD4; Provisional
MNSSKTTPQRLAVSIVCSLAAGFCAASLYVTFRHGFNGEAMMTFDVFAFWYETPLYLGYATPVFYRGLAI
VVSTSVVVLLSQLIVSLRNREHHGTARWAEEGEMRHAGYLQRYSRITGPIFGKTCGPRWFGSYLTNGEQP
HSLVVAPTRAGKGVGVVIPTLLTFKGSVIALDVKGELFELTSRARKASGDAVFKFAPLDPERRTHCYNPV
LDIAALPPERRFTETRRLAANLITAKGKGAEGFIDGARDLFVAGILACIERGTPTIGAVYDLFAQPGEKY
KLFAQLAEETQNKEAQRIFDNMAGNDTKILTSYTSVLGDGGLNLWADPLVKAATSRSDFSVYDLRRKRTC
IYLCVSPNDLEVVAPLMRLLFQQVVSILQRSLPGKDERHEVLFLLDEFKHLGKLEAIETAITTIAGYKGR
FMFIIQSLSALTGTYDEAGKQNFLSNTGVQVFMATADDETPTYISKAIGDYTFKARSTSYSQARMFDHNI
QISDQGAPLLRPEQVRLLDDDTEIVLIKGQPPLKLRKVRYYSDRELKRIFEAQTGSLPEPASLMLPDDTN
ARRKHLPQPAASSTDQAPAKIALIPDPDEPASPQNRTVADVPKPLSKGMDAPARAKEVDDAREYDGADDV
TPEALVVPELAPALTAQRQLLDQIIALQQRSRVASGDAYG
>gnl|CDD|172375 PRK13851, PRK13851, type IV secretion system protein VirB11; Provisional
MEVDPQLRFLLKPVLEWLDDPRTEEVAINRPGEAFVRQAGVFTKFPLPLSYDDLEDIAILAGALRKQDVG
PRNPLCATELPGGERLQICLPPTVPSGTVSLTIRRPSSRVSELKEVSSRYDASRWNQWQERRKRRDQLDE
AILRHYDNGDLEAFLHACVVGRLTMLLCGPTGSGKTTMSKTLISAIPPQERLITIEDTLELVIPHENHVR
LLYSKNGAGLGAVTAEHLLQASLRMRPDRILLGEMRDDAAWAYLSEVVSGHPGSISTIHGANPVQGFKKL
FSLVKSSAQGASLEDRTLIDMLATAIDVIVPFRAYGDVYEVGEIWLAADARRRGETIGDLLNQQ
>gnl|CDD|139912 PRK13852, PRK13852, type IV secretion system protein
MNFSIPAPFTAIHTIFDTAFTTSLDSDLGSIQSAVSAPLVACVTLWIIVQGILVMRGELDARGGITRVIT
VSIVVALIVGQANYHDYVVSVFEKTIPNFVQQFSGSGLPLQTIPAQLDTMFALTQAAFQKIASEIGPMND
QDILAFQGAQWVFYGTLWSAFGVYDAVGILTKVLLAIGPLILVGYLFDRTRDIAAKWIGQLITYGILLLL
LNIVATIVILTEATALNLMLGVITTAGTTAAKIIGLYELDMFFLTGDALIVALPAIAGNIGGSYWSGATQ
SANSLYRRFAQVERR
>gnl|CDD|139913 PRK13853, PRK13853, type IV secretion system protein VirB4; Provisional
MLGASGRTERSGEIYLPYVGHLSDHIVLLEDGSIMTMAHISGLPFELEEVEMRNARCRAFNTLLRNIADD
NVSIYAHLVRHNDVPPPPARHFRSAFAASLSEAFEERVLSGKLLRNDHFLTLIVSPRTALGKVKRRFTKR
YGKKENDLAGQIRNLEDLWHVVAGALDAYGLRRLGIREKQQVLFTEIGEALRLIMTGRFTPVPVVSGSLG
ASIYTDRVICGKRGLEIRTPKDSYVGSIFSFREYPAKTRPGMLNTLLSLDFPLVLTQSFSFLTRAQAHAK
LSLKSSQMTSSGDKAVTQISELAEAEDALASNEFVMGSHHLSLCVYADDLNSLADRGARARTRLADAGAV
VVQEGIGMEAAYWSQLPGNHKWRTRPGAITSRNFAGLVSFENFPEGARSGHWGNAIARFRTNGGTPFDYI
PHEHDVGMTAIFGPIGRGKTTLMTFILAMLEQSMVDRAGAVVFFDKDRGGELLVRATGGTYLALRRGVPS
GLAPLRGLENTAASRDFLREWIVALIESDGRGGISPEENRRLVRGIQRQLSFDPNMRSLAGLREFLLHGP
AEGAGARLQRWCRGNALGWAFDGEVDEVKLDPSITGFDMTHLLEYEEVCAPAAAYLLHRIGAMVDGRRFV
MSCDEFRAYLLNPKFAAVVDKFLLTVRKNNGMLILATQQPEHVLESPLGASLVAQCMTKIFYPSPTADRS
AYIDGLKCTEKEFQAIREDMAVGSRKFLLKRESGSVICEFDLRDMREYVAVLSGRANTVRFADQLRETHG
DDPSAWLSEFMARYHEAQD
>gnl|CDD|139914 PRK13854, PRK13854, type IV secretion system protein VirB3; Provisional
MNDRLEEATLYLAATRPALFLGVPLTLAGVFMMLAGFVIVIVQNPLYEVVLLPLWFGARLVVERDYNAAS
VVLLFLRTAGRSVDGQAWGGASVSPNPIKVPQRGRGMR
>gnl|CDD|172376 PRK13855, PRK13855, type IV secretion system protein VirB10; Provisional
MNDDNQQSRHDVDASGSLVSDTHRRRLSGSQKLIVAGLVLALSLSLIWLGGRSKKENEPAPPSTMIATNT
KPFHPAPIDVPPDPPAAQEAVQPTAPPSAQSEPERNEPRPEETPIFAYSSGDQGGSKRAGHGDTDRRQDD
NREDNSLPAGEVSAENDLSIRMKPTELQPSRATLLPHPDFMVTQGTIIPCILQTAIDTNLAGYVKCVLPQ
DIRGTTNNVVLLDRGTTVVGEIQRGLQQGDARVFVLWDRAETPDHAMISLSSPGADELGRSGLPGTVDNH
FWQRFSGAMLLSVVQGAFQAASTYAGSSGGGTSFNSFQNNGEQTADTALKATINIPPTLKKNQGDTVSIF
VARDLDFSGIYQLRMTGGATRGRHRR
>gnl|CDD|172377 PRK13856, PRK13856, two-component response regulator VirG; Provisional
MKHVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLATK
SDVPIIIISGDRLEEADKVVALELGATDFIAKPFGTREFLARIRVALRVRPNVVRTKDRRSFCFADWTLN
LRQRRLISEAGGEVKLTAGEFNLLVAFLEKPRDVLSREQLLIASRVREEEVYDRSIDVLILRLRRKLEQD
PANPQLIKTARGAGYFFDADVDVSYGGVMAA
>gnl|CDD|172378 PRK13857, PRK13857, pilin major subunit VirB2
MACFERYRAHLNRLSLSNAVMRLLSPHAPSVGGAIGWSIFSSGPAAAQSAGGTDPATMVNNICTFILGPF
GQSLAVLGIVAIGISWMFGRASLGLVAGVVGGIVIMFGASFLGQTLTGGG
>gnl|CDD|237532 PRK13858, PRK13858, T-DNA border endonuclease VirD1
MSQSRGTSSDAAVDRRESAKVEGFKVVSTRLRSAEYESFSAQARLLGLSDSMAIRVAVRRIGGFLEIDAE
TREKMEAILQSIGTLSSNIAALLSAYAENPRPDLEALRAERIAFGKEFADLDGLLRSILSVSRRRIDGCS
LLQDALS
>gnl|CDD|172380 PRK13859, PRK13859, type IV secretion system lipoprotein VirB7; Provisional
MKYCLLCLALALAGCQTNDTLASCKGPIFPLNVGRWQPTPSDLQLTNAGGRNERV
>gnl|CDD|172381 PRK13860, PRK13860, pilin minor subunit VirB5
MKITQLVATALAICLLLSGPARAQFVVSDPATEAETLATALNTAANLEQTITMVTMLTSAFGVTGLLSSL
NQKNQYPSTGDLDKEMFSPQMPASTTARAITTDADRAVVGSDAEADLLRSQITGAANAAGVAADNLEAMD
KRLTANAETSAQLSRSRNIMQATVTNGLLLKQIHDAIIQNVQATSLLTMTTAQAGLHEAEEAAAQRKEHQ
KTAVIFGAAP
>gnl|CDD|172382 PRK13861, PRK13861, type IV secretion system protein VirB9; Provisional
MIKKLFLTLACLLFAAIGALAEDTPAAGKLDPRMRYLAYNPDQVVRLSTAVGATLVVTFGANETVTAVAV
SNSKDLAALPRGNYLFFKASKVLPPQPVIVLTASDAGMRRYVFSISSKTLSHLDKEQPDLYYSVQFTYPA
DDAAARRKEAEQKAVADRLRAEAQYQRRAEDLLDQPATDGGAGDKNWHYVAQGDRSLLPLEVFDNGFSTV
FRFPGNVRIPSIYTINPDGKEATANYSVKGSYVEVSSVSREWRLRDGHTVLCIWNTAYDPVGRRPGTGTV
RPDVKRVLKEAR
>gnl|CDD|172383 PRK13862, PRK13862, conjugal transfer protein VirC2
MGIRKPALSVGEARRLAAARPEIVHPEPTLASQNLALPQLPERADEEDRQTGPATAKRRDSPDRQSMLTA
DALSSTTAPEKVQVFLSARPPAPEVSKIYDNLILQYSPSKSLQMILRRALDDFENMLADGSFSTAPQSYP
IPHTTEKSIIVQTSRMFPVSLLEVARNHFDPLGLETARAFGHKLATAALASFFAREKARKE
>gnl|CDD|237533 PRK13863, PRK13863, T-DNA border endonuclease VirD2
MPDRAQVIIRIVPGGGTKTLQQIINQLEYLSRKGKLELQRSARHLDIPVPPDQIRELARSWVQETGTYDE
SQPDEERQQELTTHIIVSFPAGTSQVAAYAASREWAAEMFGSGAGGGRYNYLTAFHIDRDHPHLHVVVNR
RELLGHGWLKISRRHPQLNYDALRIKMAEISLRHGIVLDATSRAERGITERPMTYAQYRRLERQQANQIR
FEDADFEEFSPGEDHREPSQSFDTSPGEAPQGEPESAERPEKLQNESEVRLQEPAGSSIKADARIRVSLE
SERRAQPSASKIPVADDFGIETSYVAEGDVRKLEGNSGTPRLATEVATHTTSERQQRRKRPRDDEGEPSG
AKRTRLNGIAVGPEANAGEQDGRDDPITSPAQPPRSNPLADPVRASIATDSLPATADRQQQREPSSKRPR
DDDGEPSIRKRARDGRSQDGREGNRR
>gnl|CDD|237534 PRK13864, PRK13864, type IV secretion system lytic transglycosylase VirB1; Provisional
MLKAAGSLSIILLASMCPSSKAAPLSFAEFNQLARECAPSVAPSTLAAIAKVESRFDPLAVHDNTTGETL
HWQNHAQATQSVRHRLEARHSLDVGLMQINSKNFSVLGLTPDGALQPCTSLSAAANLLGSRYAGGDTADE
KQLALRRAISAYNTGDFTRGFANGYVRKVETAAQQLVPPLTQRPKDDREKPKSEETWDVWGSYKRRSPEG
GAGGSSAPPPAPDPDNRKSEDDDQVLFDLNQGGAQ
>gnl|CDD|172386 PRK13865, PRK13865, type IV secretion system protein VirB8; Provisional
MKGSEYALLVEREALAEHYKEVEAFQTARAKSARRLSRVLAAVAGIAVAGNVAQAFAIATMVPLEKLVPV
YLWVRPDGTVDSEVSVSRLPATQEQAVVNASLWEYVRLRESYDADTAQYAYDLVSNFSAPTVRQDYQQFF
NYPNPTSPQVIVGKRGRLEVEHISSNDVTPGVQQIRYKRTLTMDGKMPVVSTWTATVRYEKVTSLPGRLR
LTNPGGLIVTSYQTSEDTV
>gnl|CDD|172387 PRK13866, PRK13866, plasmid partitioning protein RepB; Provisional
MSRKDAIDSLFLKKQPATDRTSVDKSAVRVRTGAISAMGSSLQEMAEGAKAAARLQDQLAAGEAVVSLDP
SMIDGSPIADRLPADVDPKFEQLEASISQEGQQVPILVRPHPEAAGRYQIVYGRRRLRAAVNLRREVSAI
VRNLTDRELVVAQGRENLDRADLSFIEKALFALRLEDAGFDRATIIAALSTDKADLSRYITVARGIPLNL
ATQIGPASKAGRSRWVALAEGLGKPKATDAIEAVLESEQFKHSDSDARFDLIFNAVSKPPAKRPKKVRAW
STPKGKKAATIRQETGRTALVFDEKLVPTFGEYVADQLDSLYAQFIETNGGGKLDQ
>gnl|CDD|172388 PRK13867, PRK13867, type IV secretion system effector chaperone VirE1
MAIIKLNANKNRPVSPIEEPQEIHIEELSDNHQPNGFTSLDLEMIELENFVLRCPLPEDNLAGQK
>gnl|CDD|237535 PRK13868, PRK13868, type IV secretion system single-stranded DNA binding effector VirE2
MDPKAEGNGENITVTAGGNVENSDVVDPKRQKKEGVNSSTISDIQMTGSHETPEHNMHGSPTHTEDLSPR
LDEGMLDSQSSHDSGSVHGNQSEVENELSSLFANMALPGHDRRPDEYILVRQTGQDAFAGTAKGNLDHLP
TKAEFNASCRLYRDGAGNYYPPPLAFDKIDVPEQLEAQWHNLEPKERSKLRFQYKLEVWNRAHAEMGITG
TEIFYQTDKNIKLDRNYKLRPEDRYIQTEKYGRREIQKRYEHEFQAGSLLPDILIKTPQNDIHFVYRFAG
DAYANKRFEEFERAIKTKYGSDTEIKLKSKSGIMHDSKYLESWERGSADIRFAEFAGENRAHNRQFPAAT
VNMGRQPDGQGGTTRDRHVSVDFLMQNAPNSPWTQALKKGELWDRVQVLARDGNRYMSPARLEYSDPEHF
TQLMNRVGLPVSMGRQSHANSIKFEQFDAQAAVIVANGPNLRDIRDLSPEKLQQLSQKDVLIADRNEKGQ
RTGTYTSVAEYERLMMKLPDDAAQLLAEPTDKYSRDFVRPEPALRPISDSRRIYESRPRGQSVNSL
>gnl|CDD|139929 PRK13869, PRK13869, plasmid-partitioning protein RepA; Provisional
MSKAAAISRNDRPSVDVTIGEHAEQLSSQLQAMSEALFPPTSHKSLRKFTSGEAARLMKISDSTLRKMTL
AGEGPQPELASNGRRFYTLGQINEIRQMLAGSTRGRESIDFVPHRRGSEHLQVIAVTNFKGGSGKTTTSA
HLAQYLALQGYRVLAVDLDPQASLSALLGVLPETDVGANETLYAAIRYDDTRRPLRDVIRPTYFDGLHLV
PGNLELMEFEHTTPKALSDKGTRDGLFFTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVIT
VHPQMLDIASMSQFLLMTRDLLGVVKEAGGNLQYDFIRYLLTRYEPQDAPQTKVAALLRNMFEDHVLTNP
MVKSAAVSDAGLTKQTLYEIGRENLTRSTYDRAMESLDAVNSEIEALIKMAWGRA
>gnl|CDD|172390 PRK13870, PRK13870, transcriptional regulator TraR; Provisional
MQHWLDKLTDLAAIEGDECILKTGLADIADHFGFTGYAYLHIQHRHITAVTNYHREWQSVYFDKKFDALD
PVVKRARSRKHIFTWSGEQERPRLSKDERAFYAHAADFGIRSGITIPIKTANGSMSMFTLASEKPVIDLD
REIDAVAAAATIGQIHARISFLRTTPTAEDAAWLDPKEATYLRWIAVGKTMEEIADVEGVKYNSVRVKLR
EAMKRFDVRSKAHLTALAIRRKLI
>gnl|CDD|172391 PRK13871, PRK13871, conjugal transfer protein TrbC; Provisional
MSRKTRITLALAALAAVSFIGLADPAFASSGGGSLPWESPLQQIQQSITGPVAGFIALAAVAIAGAMLIF
GGELNDFARRLCYVALVGGVLLGATQIVALFGATGASIGELEARAGPGIYEPSMTLRTRGEGAHG
>gnl|CDD|184356 PRK13872, PRK13872, conjugal transfer protein TrbF; Provisional
MRFKRPSVRYGRTPEPETPYQRAAQVWDERIGSARVQARNWRLMAFGCLALSAGLAGGLVWQSARGTVVP
WVVEVDRLGQAQAVAPAAADYRPTDPQIAWHLARFIELVRSLSADPIVVRQNWLRAYDFTTDRGAAALND
YARANDPFARVGKQQVAVEVSSVIRASPDSFRVAWTERRYENGALAGTERWTAILTIVIQPPRDAERLRK
NPLGIYVNAINWSRELGQ
>gnl|CDD|237536 PRK13873, PRK13873, conjugal transfer ATPase TrbE; Provisional
MLNLAEYRRRPARLADFLPWAALVAPGVVLNKDGSFQRTARFRGPDLDSATPAELVAVAARLNNALRRLG
SGWAIFVEAQRRPAADYPESDFPDPASWLVDEERRAQFEEAGAHFESRYFLTLLYLPPAEDAARAERWLY
EGRERRGVDWRERLRGFVDRTDRVLDLLDGFMPEIAWLDDAETLTYLHSTISTRRHRVRVPETPMYLDAL
LADQPLTGGLEPRLGDAHLRVLTIRGFPTATWPGILDDLNRLAFPYRWSTRAICLDKTDATKLLTKIRRQ
WFAKRKSVAAILKEVMTNEASALVDTDAANKAADADAALQELGADQVGFGYVTATVTVWDADPAIADEKL
RLVEKVIQGRGFTCIPETLNAVEAWLGSLPGHVYANVRQPPVSTLNLAHMMPLSAVWAGPERNEHLDAPP
LLYARTEGSTPFRLSLHVGDVGHTLVVGPTGAGKSVLLALMALQFRRYPGAQVFAFDFGGSIRAATLAMG
GDWHDLGGGADGSVALQPLARIDDEAERAWAAEWIAGILAREGVAVTPEVKEHIWSALTSLASAPVEERT
LTGLSVLLQSNALKQALAPYCLGGPHGRLLDADAERLGSADVQAFEMEGLMGTKAAAPAVLSYLFHRIED
RFDGRPTLLILDEAWLFLDDPVFAAQLREWLKTLRKKNVSVIFATQSLADIDGSAIAPAIIESCPTRIFL
PNERAIEPQIAAIYRRFGLNDRQIEILARATPKRDYYYQSRRGNRLFELGLGPVALAFCAASSKADQALI
DRVLAEHGRDGFAAAWLRHRGLDWAADLLPDLPNLPQEKSP
>gnl|CDD|184358 PRK13874, PRK13874, conjugal transfer protein TrbJ; Provisional
RKRLLALALAAALALSPLLAPPAHAQWIVYDPTNYAQNVLTAARALQQINNQITSLQNEAQMLINQARNL
ASLPYSSLQQLQQSLARTQQLLAQAQGIAYDVQSIDRAFQRLYPEASATVSDAQLVADARERWQNTVGGL
QDALRVQAGVVGNLDTDRSQLSALVGQSQSATGALQAAQAGNQLLALQAQQLADLQALMAAQGRAQALEA
ARQAAAEEQGREQRRRFLGP
>gnl|CDD|237537 PRK13875, PRK13875, conjugal transfer protein TrbL; Provisional
MNDTGVIDRFLNTFTRYIDSGFGLLGGEVAFLATTLIVIDVTLAGLFWAWGADEDVIARLVKKTLYVGVF
AYIIGNFNNLARIVFESFAGLGLKASGSGLSAADFLRPGRLAQTGLDAGRPLLESISDLMGFPSFFENFV
QIAVLLLAWLLVLLAFFILAIQLFVTLIEFKLTTLAGFVLIPFALFGKTAFLAERVLGNVVSSGIKVLVL
AVIVGIGSTLFSQFTAGFGGAEPTIDDAMAIVLAALSLLGLGIFGPGIANGLVSGAPQLGAGAAVGTGLA
AGGAAVAAAAGAGLAAGGGAAAAGGAAAAARGGAAAAGGASSAYSAGAAGGSGAAGVAAGLGGVARAGAS
AAASPLRRAASRAAESMKSSFRAGARSTGGGAGGAAAAAAAGAAAAGPPAWAKRMKRRQQLTHGATTAAH
ALRSGDSGGGGSSPSLSESD
>gnl|CDD|237538 PRK13876, PRK13876, conjugal transfer coupling protein TraG; Provisional
MSATKILWGQIAVVFLIVLAGVWAATQWTAWALGFQPQLGSPWFDLFGWPVYYPPAFFWWWYFFDAYAPH
VFDEGGAIAASGGFVAIAVAIAMSVWRAREAKRVTTYGSARWAERREIRAAGLLGPDGVVLGRHDRDYLR
HDGPEHVLCFAPTRSGKGVGLVVPTLLTWPGSAIVHDIKGENWQLTAGFRARFGRVLLFDPTNAKSAAYN
PLLEVRRGEWEVRDVQNIADILVDPEGSLERRNHWEKTSHALLVGAILHVLYAEEDKTLAGVANFLSDPK
RPIEATLRAMMTTPHLGEAGPHPVVASAARELLNKSDNERSGVLSTAMSFLGLYRDPVVAEVTSRCDWRI
ADLVAGERPVSLYLVVPPSDISRTKPLIRLILNQIGRRLTEDLDGKARRHRLLLMLDEFPALGRLDFFES
ALAFMAGYGIKSFLIAQSLNQIEKAYGQNNSILDNCHVRVSFATNDERTAKRVSDALGTATELRAMKNYA
GHRLSPWLGHLMVSRQETARPLLTPGEVMQLPPDDEIVMVSGVPPIRAKKARYYEDARFKERVLPPPDLA
PPAGPPARPDDWSGLPIPAVPAPAAAAAADGDDDGDPDNGGIRRQPELPEHEEIVPEPRPPENEFDLLDD
DDDDDAARPRQLDRAMQGVARQASLDPNDGIEL
>gnl|CDD|184361 PRK13877, PRK13877, conjugal transfer transcriptional regulator TraJ
DEKKPTRKRGRHLRVPVLPDEKAEIEANAAAAGLSVARYLRDVGQGYQIKGVIDYEYVRELARINGDLGR
LGGLLKLWLTDDVRTAQFGEATILALLGRIEATQDEMSEVMKKV
>gnl|CDD|237539 PRK13878, PRK13878, conjugal transfer relaxase TraI; Provisional
MIAKHVPMRSLKKSDFAGLVKYITDEQSKDERLGHVQVTNCEAGTVQDAITEVLATQHTNTRAKGDKTYH
LIVSFRAGEQPSADTLRAIEERICAGLGYGEHQRVSAVHHDTDNLHIHIAINKIHPTRHTIHEPYYAYRT
LAELCTKLERDYGLERDNHEPRKRGAEGRAADMERHAGVESLVGWIKRECLEEIKGAQSWQELHQVMRDN
GLELRERGNGLVIEAGDGTMVKASTVARDLSKPKLEARLGPFEPSPERQAQTKAKRQYRKDPIRLRVNTV
ELYAKYKAEQQTLTAARAQALERARRRKDRLIEAAKRSNRLRRAAIKLVGEGRLNKKLLYAQASKALKSE
IQAINKQYQQERQALYEKHRRRTWADWLKKEATQGNAEALAALRAREAAQGLKGNTIAGEGQAKPGHAPV
VDNITKKGTIIYRAGMSAVRDDGDRLQVSREATREGLQAALRLAMERYGNRITVNGTDEFKAQVIRAAVD
SQLPITFDDPALESRRQALLNKENTHERTERPEHRGRTGRGRGGPGQRPAADQHAAGAAAVARAGDGRPA
AGRGDRAGAGVHAAGVHRKPNVGRIGRKPPPQSQNRLRALSQLGVVRIAGGSEVLLPRDVPRHVEQQGTQ
PDHALRRGVSRPGTGVGQTPPGVAAADKYIAEREAKRLKGFDIPKHSRYTAGDGALTFAGTRNVEGQSLA
LLKRGDEVMVLPIDQATARRLKRIAVGDAVTVTPKGSIKTSKGRSR
>gnl|CDD|184363 PRK13879, PRK13879, P-type conjugative transfer protein TrbJ
KKFLAAKLALAVALSAGTLAVTPVQAGIPVIDGTNLSQNIMTAIESVAQTLKQIEQYQTQLQQYENMLQN
TMAPAAYIWDQAQSTINGLMNAVDTLNYYKNQLGSLDSYLGKFQDVAYYRSSPCFNGAGCSPAERAAMEE
NRRLASESQKKANDALFKGLDQQQQNLKADARTLQRLQSAAQGAQGQMQAIQYANQLASQQANQLLQIRG
LLIAQQNAIATRMQADADKEAQQAAAAEQLRSGSYRKSPAKNW
>gnl|CDD|237540 PRK13880, PRK13880, conjugal transfer coupling protein TraG; Provisional
MKIKMNNAVGPQVRAAKPKASKLLPILGALSLVAGLQAATQFFAHTFGYHASLGPNVGHVYAPWSILHWA
FKWYSQYPDEFMRAGSIGMVVSTVGLLGVAVAKVVTSNSSKANEYLHGSARWAEKKDIQAAGLLPRERNV
LEIVTGKAAPTATGVYVGGWQDKDGNFHYLRHNGPEHVLTYAPTRSGKGVGLVVPTLLSWGHSSVITDLK
GELWALTAGWRQKHAKNKVLRFEPASLSGSVCWNPLDEIRLGTEYEVGDVQNLATLIVDPDGKGLESHWQ
KTAFALLVGVILHALYKAKNEGGTATLPSVDAMLADPNRDIGELWMEMTTYGHVDGQNHPAIGSAARDMM
DRPEEEAGSVLSTAKSYLALYRDPVVARNVSRSDFRIKDLMHHDDPVSLYIVTQPNDKARLRPLVRVMVN
MIVRLLADKMDFENGRPVAHYKHRLLMMLDEFPSLGKLEILQESLAFVAGYGIKCYLICQDINQLKSRET
GYGHDESITSNCHVQNAYPPNRVETAEHLSKLTGQTTVVKEQITTSGRRTSAMLGQVSRTYQEVQRPLLT
PDECLRMPGPKKDAKGEIEEAGDMVVYVAGYPAIYGKQPLYFKDPVFQARAAIPAPKVSDRLRAVAQATE
GEGITI
>gnl|CDD|237541 PRK13881, PRK13881, conjugal transfer protein TrbI; Provisional
MSENADQMSPDASPGEVSKKSGVRRVNNMPMYILGGVLLSFVLVMALVAADRAAKQNAPAQGPKEKAGNT
SMFAKEIAGDQTGGLIEPASPLKVPEMPTGPASAPLPIARPDNPDAPPTPPANPGNPGQVNDDEAQRIRM
AKLQMFEEAVKAKTTVRVDAPRSNGSAPGGPSTYTGTPQTRDEMLARIAAVRQQIDAQRSNDPTAAYQAR
LAQLRGMGVGGGMAAPAGGGMGAGGAPQLLQTSTSGGGRNSYAQFGGNGQGDRWKLDSQPEAPRSPFELR
AGFVVPATLISGINSDLPGQIMAQVSQNVYDTATGKHLLIPQGSRLVGSYSSDVAYGQARVLVAWQRIVF
PDGKAMDIGAMPGADSAGYAGFRDQVNNHYVRIFGSAFLMSGVTAGITYSQDQNQNNNGYGQPTASSALS
EALGQQLGQVTAQLIAKNLNIAPTLEIRPGYRFNVIVTKDMTFSKPYRSFDY
>gnl|CDD|237542 PRK13882, PRK13882, conjugal transfer protein TrbP; Provisional
MKALRMSSGTREALKWLALLLMTGDHVNKYLFNGTLPVLFEAGRVALPLFVFVLAYNLARPGALERGDYG
RTMKRLALFGLLASVPFVALGGLFGGWWPLNVLFTLLVATATAYLVERGGKLHLVAAGVVFLVGGSLVEY
WWPAVAFGLAAWSYFRRPSWAAAAVALLACAALCFVNGNLWALAALPVLLLASRVDLRLPRLRWAFYAYY
PLHLAALWLIRIPMSKAGYLFF
>gnl|CDD|184367 PRK13883, PRK13883, conjugal transfer protein TrbH; Provisional
MRKIVLLALLALALGGCATSQYGNFVQASAADQQKLATDAVQQLATLYPPAQTRFELQQPTPDAFGQALV
KALRDKGYALLEYNPAGASAAAPAAAASAASGGLPLRYVLDQAGDSNLYRVTLMVGNQSISRAYLAQNGT
FAPAGYWVRKE
>gnl|CDD|184368 PRK13884, PRK13884, conjugal transfer peptidase TraF; Provisional
MSRILKRITAGVAVAGLAALLLAALGYAAGARVNTTKSIPVGLYWTSSAPVEKGAYVLFCPPQRGVFDDA
KERGYIGAGFCPGGYGYMMKRVLAAKGDAVSVTDDGVRVNGELLPLSKPILADGAGRPLPRYQANSYTLG
ESELLLMSDVSATSFDGRYFGPINRSQIKTVIRPVITW
>gnl|CDD|237543 PRK13885, PRK13885, conjugal transfer protein TrbG; Provisional
MKKTLSALILGAALLVPSLALAAPGDDLADKYFSKNNPTLTAQERAALAIAKRWQAGSATGIKPVAGSDG
SIKFVYGAQQPSIVCAVLQVCDIALQPGEQVNSINLGDTARWTVEPAITGSGANEVQHLIIKPMDVGLET
SLVVTTDRRTYHFRLRSHRTEYMPQVSFTYPEDALAKWDAIQRREAQERTDNTLPQTGEYLGDLSFDYEI
SGSASWKPVRVYNDGRKTIIEMPGTMQQTEAPTLLVVRKEGGLFTDDETVMVNYRVQGNRYIVDTVFDKA
ILIAGVGSSQDRVTITRRK
>gnl|CDD|184370 PRK13886, PRK13886, conjugal transfer protein TraL; Provisional
MAKIHMVLQGKGGVGKSFIAATIAQYKASKGQKPLCIDTDPVNATFEGYKALNVRRLNIMDGDEINTRNF
DALVEMIASTEGDVIIDNGASSFVPLSHYLISNQVPALLQDMGHELVVHTVVTGGQALLDTVSGFAQLAS
QFPAECLFVVWLNPYWGPIEHEGKGFEQMKAYTANKDRVSAIIQIPALKEETYGRDFSEMLQDRLTFDEA
LADSSLTIMTRQRLKIVKDQLFAQLDNAAVL
>gnl|CDD|237544 PRK13887, PRK13887, conjugal transfer protein TrbF; Provisional
MSIADTLKGLIFKKPANSAKEAGGRRAGETENPYLNARRTWNDHVGGVVSQRQTWQVVGILSLLIALAAV
GGVIHIGSQSKFIPYVVQVDKLGQTVAAGPVDAAGKADPRVIHAAVADFIENARMVTPDVALQRKAVFKV
YSYLAPNDPATPKMNEWLNGTPDSSPFKRAAKEMVSVEIKSVLPQTPDTWQVDWVETTRDRQGTLKGQPV
TMRALVTVYQAEVTPDTTDEQLRNNPHSIYVRDFSWSRIL
>gnl|CDD|237545 PRK13888, PRK13888, conjugal transfer protein TrbN; Provisional
MPFFADLPPQLQERVVCSISAAVKYEVPANIVLAVAEKEGGKPGQWVRNTNGTHDVGPMQFNTAYLGDLA
RYGITANDVAAAGCYSFDLAAWRLRMHIRNDKGDLWTKAANYHSRTPQYNAVYRADLMRKASKWADWLEA
RFVTLDVTKAGATPSTPSQPATVAQRATPAARPAPAPKQAAPAAAAARSLSVAGYVPRTISFNTSP
>gnl|CDD|237546 PRK13889, PRK13889, conjugal transfer relaxase TraA; Provisional
MAIYHLHVKVIGRKAGSSAVASAAYRSASRLRDERLDRSHDFSAKRGVVHSEVMLPEGAPEAWSDRERLW
NDVEAFEKRKDAQLAREVEFAIPREMTQAQGIELARDFVQAEFVDRGMIADLNVHWDIGEDGMAKPHAHV
MLTMRAVDENGFGAKVRDWNRTELVERWRERWAELANERLAELDIDARIDHRSLEAQGIALEPQSQIGAA
AQRIEGEGIEADRAEMHREIARRNGERIIADPSIALDAITHQQSTFTRRDLAKFAHRHSDGIDQFNAVMG
AMRAAPDLVELGKDGRGEDRFTTRAMIETEQRLHRAAELMAERERHAVSDADREAALARAEARGLVLSGE
QADALAHVTDGRDLGVVVGYAGTGKSAMLGVAREAWEAAGYEVRGAALSGIAAENLEGGSGIASRTIASL
EHGWGQGRDLLTSRDVLVIDEAGMVGTRQLERVLSHAADAGAKVVLVGDPQQLQAIEAGAAFRSIHERHG
GAEIGEVRRQREDWQRDATRDLATGRTGEALDAYEAHGMVHAAATREQARADLIDRWDRDRQAAPDRSRI
ILTHTNDEVRALNEAARERMRAAGDLGDDVRVTVERGERSFASGDRVMFLQNERGLGVKNGTLGTIEQVS
AQSMSVRLDDGRSVAFDLKDYDRIDHGYAATIHKAQGMTVDRTHVLATPGMDAHSSYVALSRHRDGVDLH
YGRDDFADRDRLVRTLSRDRAKDMASDYERADPAQSYAERRGITFRERVAEIVRKIVPEKLRGMFDGLRL
PDPVPGPEAGRRPERESAAATTDAPARTVAADPEAALRQARTRALVRHARAVDAIFRMQEQGGPVLPHQV
KELQEARKAFEEVRPYGSHDAEAAYKKNPELAAEAASGRPARAIRALQLETELRTDPARRADRFVERWQK
LDRASQRQYQAGDMSGYKATRAAMGDMAKSLERDPQLESLLAGRKRELGIGFESGRRLGRELAFSHGIDL
GRGRGLGL
>gnl|CDD|237547 PRK13890, PRK13890, conjugal transfer protein TrbA; Provisional
MYNYIFFTNVLRLLDERHMTKKELSERSGVSISFLSDLTTGKANPSLKVMEAIADALETPLPLLLESTDL
DKEALDALAGGKAPRSLPPGFERVAAVLPEHQAFIVKKWGEATRKKLRGS
>gnl|CDD|184375 PRK13891, PRK13891, conjugal transfer protein TrbE; Provisional
MIEAIAIAIAVLGAVLLLILFARIRAVDAELKLKKHRSKDAGLADLLNYAAVVDDGVIVGKNGSFMAAWL
YKGDDNASSTDEQREMVSFRINQALAGLGSGWMVHVDAVRRPAPNYSERGVSHFPDPVSAAIDEERRRLF
EGLGTMYEGYFVLTLTWFPPVLAQRKFVELMFDDDAVAPDHKARTHGLIEQFKREITSLESRLSSAVKLT
RLRGQKVVNEDGREVTHDDFLSWLQFCVTGLNHPVMLPSNPMYLDALIGGQELWGGVVPKIGRKFIQVVA
IEGFPLESYPGILSALAELPIEYRWSSRFIFMDQHEAVKHLDKFRKKWKQKIRGFFDQVFNTNTGSIDQD
ALSMVGDAEAAIAEVNSGLVAQGYYTSVVVLMDEDRERLEASALLVEKAINRLGFAARIETINTMDAYLG
SLPGHGVENVRRPLINTMNLADLLPTSSIWTGSATAPCPMYPPLSPALMHCVTVGATPFRLNLHVRDLGH
TFMFGPTGAGKSTHLGIIAAQLRRYAGMSIYAFDKGMSMYPLAAGIRAATKGKSGLHFTVAADDDRLAFC
PLQFLETKGDRAWAMEWIDTILALNGVNTTPAQRNEIGNAIMSMHASGARTLSEFSVTIQDEAIREAIKQ
YTVDGSMGHLLDAEEDGLSLSDFTVFEIEELMNLGEKFALPVLLYLFRRIERALKGQPAVIILDEAWLML
GHPAFRAKIREWLKVLRKANCLVLMATQSLSDAANSGILDVIVESTATKIFLPNVYARDEDTSALYRRMG
LNARQIEILATAIPKRQYYYVSENGRRLYDLALGPLALAFVGASDKESVAAIKSLEAKFGHEWVHEWLAG
RGLNLNDYLEAA
>gnl|CDD|184376 PRK13892, PRK13892, conjugal transfer protein TrbC; Provisional
MQATFPAFRLNRNALFYLGLFALLAFFLLAPQHAFASEGTGGSLPYESWLTNLRNSVTGPVAFALSIIGI
VVAGGILIFGGELNGFFRTLIFIVLVMALLVGAQNMMSTFFGRGAEIAALTDGALHQVKVAALD
>gnl|CDD|237548 PRK13893, PRK13893, conjugal transfer protein TrbM; Provisional
MKKKLLALAALVAALGSTAGTASAQDVLTGDTRLACEAILCLSSGTRPSECTPSLSRYFSITKRKLSDTI
KARLNFLQLCPVANQTPEMQSLVSAISRGAGRCDAQSLNSTLVVWTGYDDGRTYISNQLPDYCAAYTGHA
YTDFASGTLPRYVGTPERGGYWVEARDYDRALAEYNERIRREDEERRRQSWDN
>gnl|CDD|184377 PRK13894, PRK13894, conjugal transfer ATPase TrbB; Provisional
TDQKEEHNSIKERAKKKLERDMGPELLAALNDPKTVEIMLNADGKLWQERLGEPMRCIGTLRVAQAQAII
ETIAGYHGKEVTRSKPILEGELPLDGSRFAGQLPPVVPAPTFAIRKKAVAIFTLDQYVERGIMTAAQREA
IIAAVRAHRNILVIGGTGSGKTTLVNAIINEMVIQDPTERVFIIEDTGEIQCAAENYVQYHTSIDVNMTA
LLKTTLRMRPDRILVGEVRGPEALDLLMAWNTGHEGGAATLHANNAKAGLDRLKSLISMHPDAPKPIEPL
IGEAVHVVVHIARTPGGRRIQEILEVSGYANGQYITKTL
>gnl|CDD|184378 PRK13895, PRK13895, conjugal transfer protein TraM; Provisional
MDDKIEELIKEIAAKHGIAVGRDDPILILQTINDRLMQDSAKAQQEMLDQFKEELESIASRWGDDAKEKA
ERILNAALAASKEAMAKGMQEGAKAAAEAVRREISASLAELAAPVREARRVAMMNLVASGMAVLAACVAL
WASL
>gnl|CDD|184379 PRK13896, PRK13896, cobyrinic acid a,c-diamide synthase; Provisional
MKGFVLGGTSSGVGKTVATLATIRALEDAGYAVQPAKAGPDFIDPSHHEAVAGRPSRTLDPWLSGEDGMR
RNYYRGEGDICVVEGVMGLYDGDVSSTAMVAEALDLPVVLVVDAKAGMESVAATALGFRAYADRIGRDID
VAGVIAQRAHGGRHADGIRDALPDELTYFGRIPPRDDLEIPDRHLGLHMGSEAPLDDDALDEAAEHIDAE
RLAAVAREPPRPEPPEEAPATGDPTVAVARDAAFCFRYPATIERLRERADVVTFSPVAGDPLPDCDGVYL
PGGYPELHADALADSPALDELADRAADGLPVLGECGGLMALAESLTTTDGDTHEMAGVLPADVTMQDRYQ
ALDHVELRATDDTLTAGAGETLRGHEFHYSSATVGSDARFAFDVERGDGIDGEHDGLTEYRTLGTYAHVH
PESGAFDRFLEAL
>gnl|CDD|237549 PRK13897, PRK13897, type IV secretion system component VirD4; Provisional
EWHKILNHIRNILGHAIIHFVVLEFCFYISGAFFALFTWGPGALDFNAINPSIADFPWAYWPTIFNYIIN
VWGQPKIYDYNLKLKLLASLLGPAIIVIIFYIKLRERIKSWRPFKKKEKVHGDARWASESDIRKAGLRSK
KGMLLGKDKGGYFVADGFQHALLFAPTGSGKGVGFVIPNLLFWEDSVVVHDIKLENYELTSGWREKQGQK
VFVWEPANPDGISHCYNPLDWVSTKPGQMVDDVQKIANLIMPEQDFWNNEARSLFLGVVLYLLADPEKVK
SFGEVVRTMRSDDVVYNLAVVLDTLGKVIHPVAYMNIAAFLQKADKERSGVISTMNSSLELWANPLIDTA
TASSDFNIQEFKKKKTTVYVGLTPDNLTRLQPLMQVFYQQATEFLCRKLPDKDEPYGVLFLMDEFPTLGK
MEQFKTGIAYFRGYRVRLFLIIQDTEQLKGIYEEAGMNSFLSNSTYRITFAANNIETANLISQLVGNKTV
EQESLNKPKFLDLNPASRSLHISEVQRALLLPQEVIMLPRDEQILLIESTYPIKSKKIKYYEDKFFTSRL
LPPTFVPTQEPYDPRANNNEASEETETITVPENNEEDEEDDDEDDD
>gnl|CDD|172418 PRK13898, PRK13898, type IV secretion system ATPase VirB4; Provisional
MKLFRTRAAKEKRSKRERHTSHFIPYKCHWNSSTILTKDNSLLKVIKLSGFAFETADDEDLDIQKNIRNQ
LLKSMSSGSFGLYFHTIRRRKAVFSDDFPTVKVPNDFATYVNVEWRKKHATKQSFFNELYITILRKPDTK
GVEILEYFLKKLRQKSNKEAWENDMKEMYENLEEMTNRVVTSLRNYGPRLLGVRQTPSGVFCEILEFLSS
IVNCGDSPGPVALPRGTIDEYLPTHRLFFGSKTIEAVSHNESKYAGIISIKEYGPNTSAGMLDGFLQLPY
EFIITQSFQFTNRQVAIGKMQLQQNRMIQSGDKAVSQIAEISTALDDATSGDIAFGEHHLTILCIEKNIK
ALENALSLAEVELSNCGVYPVREKVNLEPAFWAQLPGNFDYIVRKATISTLNMAGFASQHNYPLGKKFDN
HWGEAVTVFDTTSGTPFYFNFHVRDVGHTLIIGPTGAGKTVLMNFLCAQAMKFSPRMFFFDKDRGAEIFI
RALNGVYTVIEPRLKCNFNPLQLDDTSENRTFLMEWLKVLVTSNGESLTAQDIKRINDAVEGNFKLKKED
RRLSNLVAFLGIDGPNTLAGRIAMWHGKGSHAAIFDNEEDLLDFQKARVFGFEMGELLKDPVSLAPVLLY
LFHRISISLDGTPSMIVLDEAWALIDNPVFAPKIKDWLKVLRKLNTFVIFATQSVEDASKSAISDTLVQQ
TATQIFLPNLKATDIYRSVFMLSEREYILIKHTDPTTRFFLIKQGVSAVVARINLDGMDDIISVLSGRAE
TVLLLDQIREEVGDDPNKWLPIFYEAVKTL
>gnl|CDD|237550 PRK13899, PRK13899, type IV secretion system protein VirB3; Provisional
MAGSLAADQLFKGLTRPPMIFGVSYKFAALNMIISMMVFIWTNDFRILFIAAPGIHGIGYIICFKEPLFI
ELFLNKMQKCSKCPNRFYHGANSYDIM
>gnl|CDD|184381 PRK13900, PRK13900, type IV secretion system ATPase VirB11; Provisional
MTEEYAALETYLEPLKNIFAEDGVNEISINKPGEVWVEKKGDIRCEQIPELDLSHLKALGRLVAQATEQK
ISEEKPLLSATLPNGYRIQIVFPPACEIGQIVYSIRKPSGMQLTLDDYEKMGAFDETATESLVDEDDVIL
NELLAEKKIKEFLEHAVISKKNIIISGGTSTGKTTFTNAALREIPAIERLITVEDAREIVLSNHPNRVHL
LASKGGQGRAKVTTQDLIEACLRLRPDRIIVGELRGAEAFSFLRAINTGHPGSISTLHADSPAMAIEQLK
LMVMQAGLGMPPDQIKKYILNVVDIVVQLKRGSGGKRYVSEIYFTKNKNKNG
>gnl|CDD|237552 PRK13903, murB, UDP-N-acetylmuramate dehydrogenase
MKRSGVGSAFAGAEVAEDVPLAPLTTLRVGGPARRLVTCTSTEELVAAVRELDAAGEPLLVLGGGSNLVI
ADDGFDGTVVRVATRGVTVDCGGGLVRAEAGAVWDDVVARTVEAGLGGLECLSGIPGSAGATPVQNVGAY
GQEVSDTITRVRLLDRRTGEVRWVPAADLGFGYRTSVLKHSDRAVVLEVEFQLDPSGLSAPLRYGELARA
LGVEPGERVPPAAVREAVLALRAGKGMVLDPADHDTWSAGSFFTNPVVSPAVAERLAARVAERLGDPVPR
YPAGDGGVKLSAAWLIERAGFGKGYPGGGAPARLSTKHTLALTNRGGATTADLVALAREVRDGVRDAFGV
TLVPEPVLVGCSL
>gnl|CDD|184384 PRK13904, murB, UDP-N-acetylmuramate dehydrogenase
MTKIIDFSKYSSVKIGPPLEVLVLEEIDDFSQDGQIIGGANNLLISPNPKNLAILGKNFDYIKIDGECLE
IGGATKSGKIFNYAKKNNLGGFEFLGKLPGTLGGLVKMNAGLKEYEISNNLESICTNGGWIEKEDIGFGY
RSSGINGVILEARFKKTHGFDEELLEAFKSMRKNQPKGPSFGSCFKNPKGDYAGRLIEAVGLKGYCKGGA
GFSEEHANFLVNLGGATFEDALDLIELAKKRVLEEFGINLEEEVIIL
>gnl|CDD|237553 PRK13905, murB, UDP-N-acetylmuramate dehydrogenase
LLKELLPALRGRLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRD
GGIRGVVIRLGKGLNEIEVEGNRITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNAGAYGG
ETADVLESVEVLDRDGEIKTLSNEELGFGYRHSALQEEGLIVLSATFQLEPGDKEEIKARMDELLARREA
TQPLEYPSAGSVFKNPPGHFAGKLIEEAGLKGYRIGGAQVSEKHANFIINTGGATAADIEDLIEHVQKTV
KEKFGVELEWEVRIIGEF
>gnl|CDD|184386 PRK13906, murB, UDP-N-acetylmuramate dehydrogenase
MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGS
NIIIREGGIRGIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNA
GAYGGEVKDCIDYALCVNEQGSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLT
ERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHY
VQKTVKEKFGIELNREVRIIGEHPKES
>gnl|CDD|139967 PRK13907, rnhA, ribonuclease H; Provisional
MIEVYIDGASKGNPGPSGAGVFIKGVQPAVQLSLPLGTMSNHEAEYHALLAALKYCTEHNYNIVSFRTDS
QLVERAVEKEYAKNKMFAPLLEEALQYIKSFDLFFIKWIPSSQNKVADELARKAILQN
>gnl|CDD|184387 PRK13908, PRK13908, recombination protein RecO
MQGFILDTQKVRDEDLIVRILTPNKLKTLYRFYGARHSVINLGYKIDFELEENDKFLPRLRDVLHLGFKW
LRDRERLLIWQRFIRLLYRHLKDVESLDSFYFDLLDDCAKKLEKQNPKRVIIESYAKLLEFEGRLHKDFI
CFLCDEKIENEIALARAFLPAHPSCIKSKSFELEKIKEFFRTKSTIFLEDEEVEELWRILLEGL
>gnl|CDD|237554 PRK13909, PRK13909, RecB-like helicase
LALKASAGSGKTFALSVRFLALLFKGANPSEILALTFTKKAANEMKERIIDTLLNLEKEKEESELNELEE
KLGLSKEELLNKRDKVYQEFLNSELKISTIDAFFQKILRKFCLNLGLSPDFSIKEDTKEELNEKFLSALS
KEELLELLAFIKQCESKKNNSFFELLEKLYEKNNELKLFEKAKNPIEFDEEKFLEELRSLKQQIQSIETA
SKNAKKAFKKEDFEELLNSSKTWLEKESEYRYFKKLYNEELDAEFEELKNALKRYYDAKENYKLSKLFKL
LQLYKEAKNELNKKKNALDFDDISKKVYELLGEEEIDKDFLYFRLDSKISHILIDEFQDTSVLQYKILLP
LIDEIKSGEGQKKFRSFFYVGDVKQSIYRFRGGKKELFDKVSKDFKQKVDNLDTNYRSAPLIVDFVNEVF
KKKYKNYKTQYAEQHKSGGYVEVVEVADESEELLEQLLQEIQFLLEKGIDPDDIAILCWTNDDALEIKEF
LQEQFGIKAVTESSAKLINQPEVKALIEALKYCLFGEEIYKHNVLKLLGKEPDKIPSFLPKEESVAEFVK
KLIEELKLYDENLLKFLELASGYEDIEEFLFKLEPCDKEIASEESKGVQIMTVHKSKGLEFEHVIVCDRL
GKPNSDSSNLLFEYDGIELWQIYYRIKGRENFDKDYARALEKEKALKYEEEINVLYVAFTRAKNSLIVVK
KDESSGSMFEILDLKPLERGEIEIKEPKISPKKESLITSVKLKPHGYQEQVKEIEEEPKEDNDLEAIYFG
IALHYCLEMLYAFKIENLEVLKNLLKNRYGHFLDESDLEDLEKRLELLINNKEFQALLKDGKLLKEQALL
FNGELKQIDLLLEKDEEICVIDYKSSKKYQEEHKAQVSHYKEAIKEILPKKKVEAYIVYLLEDKIEILEV
>gnl|CDD|172427 PRK13910, PRK13910, DNA glycosylase MutY; Provisional
MSQQTQINTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPND
YQSLLKLPGIGAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNLNESFNHN
QALIDLGALICSPKPKCAICPLNPYCLGKNNPEKHTLKKKQEIVQEERYLGVVIQNNQIALEKIEQKLYL
GMHHFPNLKENLEYKLPFLGAIKHSHTKFKLNLNLYLAAIKDLKNPIRFYSLKDLETLPISSMTLKILNF
LKQKNLFGG
>gnl|CDD|139971 PRK13911, PRK13911, exodeoxyribonuclease III; Provisional
MKLISWNVNGLRACMTKGFMDFFNSVDADVFCIQESKMQQEQNTFEFKGYFDFWNCAIKKGYSGVVTFTK
KEPLSVSYGINIEEHDKEGRVITCEFESFYLVNVYTPNSQQALSRLSYRMSWEVEFKKFLKALELKKPVI
VCGDLNVAHNEIDLENPKTNRKNAGFSDEERGKFSELLNAGFIDTFRYFYPNKEKAYTWWSYMQQARDKN
IGWRIDYFLCSNPLKTRLKDALIYKDILGSDHCPVGLELV
>gnl|CDD|184389 PRK13912, PRK13912, nuclease NucT; Provisional
KMKKIVGVFLLVGCLGVLQAKSSLYFLPYEQKDALNKLVSLISNARSSIKIAIYSFTHKDIAKALKSAAK
RGVKISIIYDYESNHNNDQSTIGYLDKYPNIKVCLLKGLKAKNGKYYGIMHQKVAIIDDKIVVLGSANWS
KNAFENNYEVLLITDDTETILKAKEYFQKMLGSCVGF
>gnl|CDD|184390 PRK13913, PRK13913, 3-methyladenine DNA glycosylase; Provisional
MLDSFELLKALKSLDLLKNAPAWWWPNALKFEALLGAVLTQNTKFEAVEKSLENLKNAFILENDDEINLK
KIAYIEFSKLAECVRPSGFYNQKAKRLIDLSENILKDFGSFENFKQEVTREWLLDQKGIGKESADAILCY
VCAKEVMVVDKYSYLFLKKLGIEIEDYDELQHFFEKGVQENLNSALALYENTISLAQLYARFHGKIVEFS
KQKLELKL
>gnl|CDD|237555 PRK13914, PRK13914, invasion associated endopeptidase
MNMKKATIAATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQ
VNEVAAAEKTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLT
DKVTSTPVAPTQEVKKETTTQQAAPAAETKTEVKQTTQATTPAPKVAETKETPVVDQNATTHAVKSGDTI
WALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTANTATPKAEVKTEAPAAEKQAAPVVKENTNTNTA
TTEKKETTTQQQTAPKAPTEAAKPAPAPSTNTNANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSN
TNANQGSSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTT
RISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINAQDNGVKYDNIHGSGWGKYLVGFGRV
>gnl|CDD|237556 PRK13915, PRK13915, putative glucosyl-3-phosphoglycerate synthase; Provisional
MLPAVEAWLEDRTWHAPDWTIEELVAAKAGRTVSVVLPALNEEETVGKVVDSIRPLLMEPLVDELIVIDS
GSTDATAERAAAAGARVVSREEILPELPPRPGKGEALWRSLAATTGDIVVFVDADLINFDPMFVPGLLGP
LLTDPGVHLVKAFYRRPLRVSGGVDATGGGRVTELVARPLLNLLRPELAGFVQPLGGEYAGRRELLESLP
FVPGYGVEIGLLIDTLDRLGLDAIAQVDLGVRAHRNQPLRALGRMARQIIATALSRLGRPDSGVGLTQFL
RDGDGFTPRTTDVSLVERPPMRTLRP
>gnl|CDD|139976 PRK13916, PRK13916, plasmid segregation protein ParR; Provisional
MDKKETKHLLKIKKEDYPQIFDFLENVPRGTKTAHIREALRRYIEEIGENPPIPSKEHTAPLKEHTEPIK
RNKESFKDAMERKDQLKQAEMPKIEEK
>gnl|CDD|184393 PRK13917, PRK13917, plasmid segregation protein ParM; Provisional
NVYVMALDFGNGFVKGKINDEKFVIPSRYGRKTNENNQLSGFVDNKLDVSEFIINGNEDEVLLFGNDLDK
TTNTGKDTYSTNDRYDIKQFKTLVKCALAGLAARTVPEEVVEVVVATGMPSEEIGTDKVAKFEKLLNKSR
LIEINGIAVTINVKGVKVVAQPMGTLLDLYLDNDGVVADKAFEEGKVSVIDFGSGTTDLDTIQNLKRVEE
ESFVIPKGTIDVYKRIASHISKKEEGASITPYMLEKGLEYGACKLNQKTVIDFKDEFYKEQDSVIDEVMS
GFEIAVGNINSFDRVIVTGGGANIFFDSLSHWYSDVEKADESQFANVRGYYKYGELLKNKVEQE
>gnl|CDD|237557 PRK13918, PRK13918, CRP/FNR family transcriptional regulator; Provisional
MSTTVVDTVTYRPGAVILYPGVPGPSDMLYRVRSGLVRLHTVDDEGNALTLRYVRPGEYFGEEALAGAER
AYFAEAVTDSRIDVLNPALMSAEDNLVLTQHLVRTLARAYESIYRLVGQRLKNRIAAALLELSDTPLATQ
EDSGETMIYATHDELAAAVGSVRETVTKVIGELSREGYIRSGYGKIQLLDLKGLEELAESAA
>gnl|CDD|184395 PRK13919, PRK13919, putative RNA polymerase sigma E protein; Provisional
MGLPLESLSDEALLALVARGEEEALRALFRRYAGAFLALARRMGLDGAAAEDVVQEVFIRVWKKAKEFDP
RRGSARAWLLALAHHAAVDHVRRRAARPQPLEPDEREPEAFDLPGPGLDEEGHLDRTRLGRALKALSPEE
RRVIEVLYYQGYTHREAAQLLGLPLGTLKTRARRALSRLKEVLREP
>gnl|CDD|237558 PRK13920, PRK13920, putative anti-sigmaE protein; Provisional
LPLYALGALSPEERARVEAALEAYPELWAELRALQEALAALAEGLPPVPVPPGLEERVLARLRPRRLPLL
PLLARAAAALALLLAGYGLAAGLSWTLSLREPATLRHYARLPGRVYALVGPEGEPVGRAVWRKDGRALVV
LKRPPPAGRVYQAWGLKKGQPVSLGTFRGPLKLTRLPPGADALAVSLEPPGGSPQPTEPLGLPQPL
>gnl|CDD|237559 PRK13921, PRK13921, CRISPR-associated Cse2 family protein; Provisional
MSPAQGFIAWLERLQEKDTAARAALRRSLAFTPGAYPPAYPYVEPFVANESHAQDWRREAFYLVAGLYAA
HPHEGRRSLAESLGEACAKRASGSASIEKRFIALLGADADQLAHRLRQAIALLKEQGIDFEELLRDLLYW
LNPRDRVQQRWARDYYRALANETEHHNDKEVSE
>gnl|CDD|237560 PRK13922, PRK13922, rod shape-determining protein MreC; Provisional
MPLFSRGKKLLLLLLLILLLLLALALLLADRRLGSLSPVRQVVGDVVSPVQRVVNAPREFVSGVFESLAS
LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNLKESLDYQFITARVISRSPDPWSQQVTIDK
GSNDGVKKGMPVIDPGGLVGRVIEVSPNTSRVLLLTDPNSRVPVQVGRNGIRGILSGNGSGDNLKLEFIP
RSADIKVGDLVVTSGLGGIFPAGLPVGKVTSVERDDYGLFKTVYVKPAADLDRLRYVLVVKRKPES
>gnl|CDD|237561 PRK13923, PRK13923, putative spore coat protein regulator protein YlbO; Provisional
MKTRQDAWTQERDGLLAEVVLRHIREGGTQLKAFEEVGDALKRTAAACGFRWNSVVRKQYQEQIKLAKKE
RKELRRQLGFSPSNLPDNVKTGDEIITSGISDLTLEDVLSEQIGKLQEEEEKLSWENQTLKQELAITEED
YRALIVIMNRARRMAILVEDERKSLAAFEM
>gnl|CDD|184399 PRK13925, rnhB, ribonuclease HII; Provisional
PMMENISELIAGVDEVGRGALFGPVFAAAVILSEKAEPQLLQAGLTDSKKLSPKRRAQLVPLILTLASDW
GIGQASAREIDRLGIRQATELAMLRALKKLKSPPSLCLVDGNLPLRLWPGPQRTIVKGDSKSAAIAAASI
LAKVWRDDLIKRLAKKYPGYGLEKNKGYGTAQHRQALLKLGPTPLHRKSFLPKLILID
>gnl|CDD|184400 PRK13926, PRK13926, ribonuclease HII; Provisional
MATPPLEPDWAYEREHWRRGYLRVAGVDEAGRGAWAGPVVVAAVILPPGEYPFRDSKTLSPAAREALAEE
VRRVALAWAVGHAEAAEIDRLNVLKATHLAAARALARLAVAPEALVTDYLRLPTPLPLLAPPKADALSPT
VAAASLLAKTERDRLMRELDARYPGYGFARHKGYGTPAHREALAALGPSPVHRRSFAPVRRLLTAAQ
>gnl|CDD|237562 PRK13927, PRK13927, rod shape-determining protein MreB; Provisional
FGLFSNDLGIDLGTANTLVYVKGKGIVLNEPSVVAIRTDTKKVLAVGEEAKQMLGRTPGNIVAIRPMKDG
VIADFDVTEKMLKYFIKKVHKNFRPSPRVVICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGA
GLPVTEPTGSMVVDIGGGTTEVAVISLGGIVYSKSVRVGGDKFDEAIINYVRRNYNLLIGERTAERIKIE
IGSAYPGDEVLEMEVRGRDLVTGLPKTITISSNEIREALQEPLSAIVEAVKVALEQTPPELAADIVDRGI
VLTGGGALLRGLDKLLSEETGLPVHVAEDPLTCVARGTGKALENIDLLKGVLFS
>gnl|CDD|237563 PRK13928, PRK13928, rod shape-determining protein Mbl; Provisional
MFGRDIGIDLGTANVLVYVKGKGIVLNEPSVVAIDKNTNKVLAVGEEARRMVGRTPGNIVAIRPLRDGVI
ADYDVTEKMLKYFINKACGKRFFSKPRIMICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAG
LDISQPSGNMVVDIGGGTTDIAVLSLGGIVTSSSIKVAGDKFDEAIIRYIRKKYKLLIGERTAEEIKIKI
GTAFPGAREEEMEIRGRDLVTGLPKTITVTSEEIREALKEPVSAIVQAVKSVLERTPPELSADIIDRGII
MTGGGALLHGLDKLLAEETKVPVYIAEDPISCVALGTGKMLENIDKLPKSELVKDI
>gnl|CDD|184403 PRK13929, PRK13929, rod-share determining protein MreBH; Provisional
MFQSTEIGIDLGTANILVYSKNKGIILNEPSVVAVDTETKAVLAIGTEAKNMIGKTPGKIVAVRPMKDGV
IADYDMTTDLLKQIMKKAGKNIGMTFRKPNVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAI
GADLPVDEPVANVVVDIGGGTTEVAIISFGGVVSCHSIRIGGDQLDEDIVSFVRKKYNLLIGERTAEQVK
MEIGYALIEHEPETMEVRGRDLVTGLPKTITLESKEIQGAMRESLLHILEAIRATLEDCPPELSGDIVDR
GVILTGGGALLNGIKEWLSEEIVVPVHVAANPLESVAIGTGRSLEVIDKLQKATK
>gnl|CDD|237564 PRK13930, PRK13930, rod shape-determining protein MreB; Provisional
MPLFGFFSKDIGIDLGTANTLVYVKGKGIVLNEPSVVAIDTKTGKVLAVGEEAKEMLGRTPGNIEAIRPL
KDGVIADFEATEAMLRYFIKKARGRRFFRKPRIVICVPSGITEVERRAVREAAEHAGAREVYLIEEPMAA
AIGAGLPVTEPVGNMVVDIGGGTTEVAVISLGGIVYSESIRVAGDEMDEAIVQYVRRKYNLLIGERTAEE
IKIEIGSAYPLDEEESMEVRGRDLVTGLPKTIEISSEEVREALAEPLQQIVEAVKSVLEKTPPELAADII
DRGIVLTGGGALLRGLDKLLSEETGLPVHIAEDPLTCVARGTGKALENLDLLRKV
>gnl|CDD|184405 PRK13931, PRK13931, 5'/3'-nucleotidase SurE
MRILITNDDGINAPGLEVLEQIATELAGPDGEVWTVAPAFEQSGVGHCISYTHPMMIAELGPRRFAAEGS
PADCVLAALYDVMKDAPPDLVLSGVNRGNNSAENVLYSGTVGGAMEAALQGLPAIALSQYYGPRNEGLDD
PFEAARTHGARVVRKLLEAGPWDDEDYRLFYNVNFPPVPAADVKGIRVAAQGFREGTRFGVEPHMSPSGR
RFLWIKGGAQQVPTAPGTDAAVNLDGYISVTPMRADLTAHDRLAELEALLG
>gnl|CDD|172445 PRK13932, PRK13932, stationary phase survival protein SurE; Provisional
NQDKKPHILVCNDDGIEGEGIHVLAASMKKIGRVTVVAPAEPHSGMSHAMTLGVPLRIKEYQKNNRFFGY
TVSGTPVDCIKVALSHILPEKPDLIVSGINYGSNTATNTLYSGTVAAALEGAIQGIPSLAFSLTTYENAD
FTYAGKFARKLARKVLREGLPPDTILSVNIPNVPESDIQGVLITRQGRSRWEEDAIERHDMYGNPYYWLN
GTLQLLDDSLTQDEYAVRHNYVAVTPLSCDLTNHDFLSSLEQWKLKK
>gnl|CDD|184406 PRK13933, PRK13933, stationary phase survival protein SurE; Provisional
MNILLTNDDGINAEGINTLAELLSKYHEVIIVAPENQRSASSHSITIYEPIIIKEVKLEGINSKAYSISG
TPADCVRVALDKLVPDNIDMVISGINKGLNIGNDILYSGTVSAAIEGAIYKVPSIAVSADVKKGKDENYK
IAAKYALEVLNILKKEDLKNDVVLNLNVPFCSEEEIKGIKVCKVGNKTFNTYFSEEIDEEGNKVYKLEGD
INKDIYEGTDVYYIRQGYVTLTPLHYDLTNFKILEEVEKLFLS
>gnl|CDD|237565 PRK13934, PRK13934, stationary phase survival protein SurE; Provisional
MKILVTNDDGVHSPGLRLLYEFVSPLGEVDVVAPETPKSATGLGITLHKPLRMYEVDLCGFKVYATSGTP
SDTIYLATYGLGRKYDLVLSGINLGDNTSLQVILSSGTLGAAFQAALLGIPAVAYSAYVDDWEELLEDGE
ALEIMKAVVRATAEYVLKRGMPKGVDVISVNFPRRLRRGVKAKLVKAAKLRFAQQVERRVDPRGRAYYWL
YGTPLEPEPGTDVYVVLKEGNIAITPLTLNLNALDGERAADLEALKRLVDYVNEAL
>gnl|CDD|237566 PRK13935, PRK13935, stationary phase survival protein SurE; Provisional
MNILVTNDDGITSPGIIILAEYLSEKHEVFVVAPDKERSATGHAITIRVPLWAKKVFISERFVAYATTGT
PADCVKLGYDVIMDKKVDLVISGINRGPNLGTDVLYSGTVSGALEGAMMGVPSIAISSADFENPDYETAA
RFLLNFLEEFDFSLLPPFTALNINVPSVPYGEIKGWKLTRQSRRRYNDYFEERVDPFGNKYYWMMGEIIE
DDPDDDVDYKAVREGYVSVTPIHVFLTNEECLKKLKEVYEDKT
>gnl|CDD|237567 PRK13936, PRK13936, phosphoheptose isomerase; Provisional
MDLQSRIRQHFEDSIDTKQQAMEVLAPPIAQAVELMVQALLNEGKILACGNGGSAADAQHFSAELLNRFE
RERPSLPAIALTTDTSTLTAIANDYSYNEVFSKQVRALGQPGDVLLAISTSGNSANVIQAIQAAHEREMH
VVALTGRDGGKMASLLLPEDVEIRVPAERTARIQEVHLLAIHCLCDLIDSQLLGSEE
>gnl|CDD|184408 PRK13937, PRK13937, phosphoheptose isomerase; Provisional
LITKHFRESQAVMEAFLESLLEAIAKVAEALIEALANGGKILLCGNGGSAADAQHIAAELVGRFKKERPA
LPAIALTTDTSALTAIGNDYGFERVFSRQVEALGRPGDVLIGISTSGNSPNVLAALEKARELGMKTIGLT
GRDGGKMKELCDHLLIVPSDDTPRIQEMHITIGHILCDLVERALFEKV
>gnl|CDD|139997 PRK13938, PRK13938, phosphoheptose isomerase; Provisional
MCTARTAEEIFVETIAVKTRILNDRVLLEAARAIGDRLIAGYRAGARVFMCGNGGSAADAQHFAAELTGH
LIFDRPPLGAEALHANSSHLTAVANDYDYDTVFARALEGSARPGDTLFAISTSGNSMSVLRAAKTARELG
VTVVAMTGESGGQLAEFADFLINVPSRDTGRIQESHIVFIHAISEHVEHALFAPRQ
>gnl|CDD|172450 PRK13940, PRK13940, glutamyl-tRNA reductase; Provisional
MALISLAIDYKKSPIEVRSEFALSGLDVSMLYRSILAIDNVVHAVILSTCNRTEVYLEISDLRVVDDILV
WWQGYVRNPNYKIKDYFKLRQGTEVIMHLMKLACGLESMVLGEPQILGQVKDSYTLSKKNHAIGKELDRV
FQKVFATAKRVRSETRIGHCPVSVAFSAITLAKRQLDNISSKNVLIIGAGQTGELLFRHVTALAPKQIML
ANRTIEKAQKITSAFRNASAHYLSELPQLIKKADIIIAAVNVLEYIVTCKYVGDKPRVFIDISIPQALDP
KLGELEQNVYYCVDDINAVIEDNKDKRKYESSKAQKIIVKSLEEYLEKEKAIISNSAIKELFQKADGLVD
LSLEKSLAKIRNGKDAEEIIKRFAYEIKKKVLHYPVVGMKEASKQGRSDCLVCMKRMFGLNVEK
>gnl|CDD|184409 PRK13942, PRK13942, protein-L-isoaspartate O-methyltransferase; Provisional
MPLEEKRRVIEELIREGYIKSKKVIDALLKVPRHLFVPEYLEEYAYVDTPLEIGYGQTISAIHMVAIMCE
LLDLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKKLGYDNVEVIVGDGTLGY
EENAPYDRIYVTAAGPDIPKPLIEQLKDGGIMVIPVGSYSQELIRVEKDNGKIIKKKLGEVAFVPLIGKN
GF
>gnl|CDD|237568 PRK13943, PRK13943, protein-L-isoaspartate O-methyltransferase; Provisional
MCEFFMREKLFWILKKYGISDHIAKAFLEVPREEFLTKSYPLSYVYEDIVLVSYDDGEEYSTSSQPSLMA
LFMEWVGLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVRRLGIENVIFVCGDG
YYGVPEFAPYDVIFVTVGVDEVPETWFTQLKEGGRVIVPINLKLSRRQPAFLFKKKDPYLVGNYKLETRF
IKAGGNLGNLLERNRKLLREFPFNREILVVRSHIFVELVDLLTRRLTEIDGTFYYAGPNGVVEFLNGRMR
IYGDAPEIENLLTQWESCGYRSFEYLMLHVGYNAFSHISCSI
>gnl|CDD|140001 PRK13944, PRK13944, protein-L-isoaspartate O-methyltransferase; Provisional
MAKRLVEELVREGIIKSERVKKAMLSVPREEFVMPEYRMMAYEDRPLPLFAGATISAPHMVAMMCELIEP
RPGMKILEVGTGSGYQAAVCAEAIERRGKVYTVEIVKELAIYAAQNIERLGYWGVVEVYHGDGKRGLEKH
APFDAIIVTAAASTIPSALVRQLKDGGVLVIPVEEGVGQVLYKVVKRGEKVEKRAITYVLFVPLR
>gnl|CDD|184410 PRK13945, PRK13945, formamidopyrimidine-DNA glycosylase; Provisional
MPELPEVETVRRGLEQLLLNFIIKGVEVLLERTIASPGGVEEFIKGLKGSLIGQWQRRGKYLLASLKKEG
SENAGWLGVHLRMTGQFLWVEQSTPPCKHTRVRLFFEKNQELRFVDIRSFGQMWWVPPGVSPESIITGLQ
KLGPEPFSPEFSVEYLKKKLKKRTRSIKTALLDQSIVAGIGNIYADESLFKAGIHPTTPAGQLKKKQLER
LREAIIEVLKTSIGAGGTTFSDFRDLEGVNGNYGGQAWVYRRTGKPCRKCGTPIERIKLAGRSTHWCPNC
QK
>gnl|CDD|184411 PRK13946, PRK13946, shikimate kinase; Provisional
EERARAALGKRTVVLVGLMGAGKSTVGRRLATMLGLPFLDADTEIERAARMTIAEIFAAYGEPEFRDLER
RVIARLLKGGPLVLATGGGAFMNEETRAAIAEKGISVWLKADLDVLWERVSRRDTRPLLRTADPKETLAR
LMEERYPVYAEADLTVASRDVPKEVMADEVIEALAAYLEKEEAA
>gnl|CDD|184412 PRK13947, PRK13947, shikimate kinase; Provisional
MKNIVLIGFMGTGKTTVGKRVATTLSFGFIDTDKEIEKMTGMTVAEIFEKDGEVRFRSEEKLLVKKLARL
KNLVIATGGGVVLNPENVVQLRKNGVVICLKARPEVILRRVGKKKSRPLLMVGDPEERIKELLKEREPFY
DFADYTIDTGDMTIDEVAEEIIKAYLKLKNG
>gnl|CDD|184413 PRK13948, PRK13948, shikimate kinase; Provisional
FARLEIERPVTWVALAGFMGTGKSRIGWELSRALMLHFIDTDRYIERVTGKSIPEIFRHLGEAYFRRCEA
EVVRRLTRLDYAVISLGGGTFMHEENRRKLLSRGPVVVLWASPETIYERTRPGDRPLLQVEDPLGRIRTL
LNEREPVYRQATIHVSTDGRRSEEVVEEIVEKLWAWAEARGA
>gnl|CDD|140006 PRK13949, PRK13949, shikimate kinase; Provisional
MARIFLVGYMGAGKTTLGKALARELGLSFIDLDFFIENRFHKTVGDIFAERGEAVFRELERNMLHEVAEF
EDVVISTGGGAPCFFDNMELMNASGTTVYLKVSPEVLFVRLRLAKQQRPLLKGKSDEELLDFIIEALEKR
APFYRQAKIIFNADKLEDESQIEQLVQRL
>gnl|CDD|172457 PRK13951, PRK13951, bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB
MRIFLVGMMGSGKSTIGKRVSEVLDLQFIDMDEEIERREGRSVRRIFEEDGEEYFRLKEKELLRELVERD
NVVVATGGGVVIDPENRELLKKEKTLFLYAPPEVLMERVTTENRPLLREGKERIREIWERRKQFYTEFRG
IDTSKLNEWETTALVVLEALDEKEISTIEKPHLVKIILGGFKRVRNEELVFTTERVEKIYGRYLPENRLL
FPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDAS
VGGKNAIDFAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSGRGVELFDEPEKIEKR
NLRVLSEMVKISVEEKARIVMEDPYDMGLRHALNLGHTLGHVYEMLEGVPHGIAVAWGIEKETMYLYRKG
IVPKETMRWIVEKVKQIVPIPVPSVDVEKARNLILNDKKILKGSRVRLPYVKEIGKIEFLEVDPLELL
>gnl|CDD|237569 PRK13952, mscL, large conductance mechanosensitive channel protein MscL
MSMLKEFKEFALKGNVMDLAVGVIIGGAFGKIVDSLVNDLIMPIIGLITGGLDFSNYFIQLGGAPAGNPT
TLAAAKKAGVAVFAYGNFITVLINFLILAFIIFLMVKAINRLRRKEEAAPPPAPPEDVVLLREIRDLLKK
KQ
>gnl|CDD|184415 PRK13953, mscL, large conductance mechanosensitive channel protein MscL
MLVEFRDFALKGNVLDLAVAVVIGAAFGKIVSSLVNNIIMPLVGVLLGGLDFSDLSWKVGKSVIQYGAFI
QSIVDFLIIAFAIFIFVKVLTSFIKKKEQQEEETPVPPTEEYLKEIRDLLKQQQK
>gnl|CDD|172460 PRK13954, mscL, large conductance mechanosensitive channel protein MscL
MLKEFKEFALKGNVLDLAIAVVMGAAFNKIISSLVENIIMPLIGKIFGSVDFAKEWSFWGIKYGLFIQSV
IDFIIIAFALFIFVKIANTLMKKEEAEEEAVVEENVVLLTEIRDLLREK
>gnl|CDD|184416 PRK13955, mscL, large conductance mechanosensitive channel protein MscL
MWNEFKKFAFKGNVIDLAVGVVIGAAFGKIVSSLVKDIITPLLGMVLGGVDFTDLKFTFGKSSIMYGNFI
QTIFDFLIIAASIFMFVKVFNKLTSKKEEEKEEEIPEPTKEEELLGEIRDLLKQQNSSKD
>gnl|CDD|184417 PRK13956, dut, dUTP diphosphatase
MKIRGFELVSSFTNENLLPKRETAHAAGYDLKVAERTVIAPGEIKLVPTGVKAYMQPGEVLYLYDRSSNP
RKKGLVLINSVGVIDGDYYGNPANEGHIFAQMKNITDQEVVLEVGERIVQGVFMPFLIADGDQADGERTG
GFGSTGK
>gnl|CDD|140013 PRK13957, PRK13957, indole-3-glycerol-phosphate synthase; Provisional
MHRVLREIIETKQNEIEKISRWDPLPDRGLPLRDSLKSRSFSIIAECKRKSPSAGELRADYHPVQIAKTY
ETLGASAISVLTDQSYFGGSLEDLKSVSSELKIPVLRKDFILDEIQIREARAFGASAILLIVRILTPSQI
KSFLKHASSLGMDVLVEVHTEDEAKLALDCGAEIIGINTRDLDTFQIHQNLVEEVAAFLPPNIVKVGESG
IESRSDLDKFRKLVDAALIGTYFMEKKDIRKAWLSLF
>gnl|CDD|184418 PRK13958, PRK13958, N-(5'-phosphoribosyl)anthranilate isomerase; Provisional
MKLKFCGFTTIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIDKVCVVVNPDLTTIEHI
LSNTSINTIQLHGTESIDFIQEIKKKYSSIKIIKALPADENIIQNINKYKGFVDLFIIDTPSVSYGGTGQ
TYDWTILKHIKDIPYLIAGGINSENIQTVEQLKLSHQGYDIASGIETNGRKDINKMTAIVNIVKGDR
>gnl|CDD|237570 PRK13959, PRK13959, phosphoribosylaminoimidazole-succinocarboxamide synthase; Provisional
MGSVKDFYVDEEPTETDLGRGRFVFSDRYSVFDWGIMPDEIPDKGASLCTMGAYNFELLEEEGIKTHYIG
VVEDGEVVRLAEASEPPNEMAVKLTQVPDLPFEGGSYDYDAYHEAAGENYLIPLEVIFRNYVPVGSSLRD
RIKEGKIKPEDLGLDADEWPEEGVKLPEPIVEFSTKYEEQDRYLSRKEADEIAGLSRAEIEELEELALKV
DEIITEEAEKRGLIHEDGKIEFALYEEREIRVVDVVGTFDENRFSYEGQELSKEVVRQYYRRTEWVEAVK
EAKEEDVADWRSLCEPDPPPLPDEVVEAVSDLYKAGTNAYTGREWFDAPPLKDAVDRVREL
>gnl|CDD|184420 PRK13960, PRK13960, phosphoribosylaminoimidazole-succinocarboxamide synthase; Provisional
MSLADKVLAVNDDLPIRTDKPVHSGKVRSVYWLTEEDSRRLIKEKGYNVPADAPLAIMVISDRISAFDCI
WHGEGGLNGVPGKGAALNAISNHWFKLFKENGLADSHILDIPHPFVWIVQKARPVMIEAICRQYITGSMW
RAYSKGEREFCGITLPEGLEKDQKLPELLITPSTKGILTGIPGVPEADDVNISRSDIEANYQAFNFSSAD
DIDLYEKLLKEGFKVISDALAKLDQIFVDTKFEFGYVTDAAGNEKLIYMDEVGTPDSSRIWDGAAYRDGK
IVENSKEGFRQFLLNHFPDPDILLNKDRMPEREALARDNALPLEAMMDVSRTYTGIAEKITGAKIVLSAN
PKAEIIDILREEYGLID
>gnl|CDD|237571 PRK13961, PRK13961, phosphoribosylaminoimidazole-succinocarboxamide synthase; Provisional
MSTLMESDLPSLPLLGRGKVRDIYAVDDDRLLMVATDRISAFDVILPEPIPDKGRVLTQMSNFWFDKLAH
IVPNHLTGIDVDDVVPADEADQVLGRAVVVKKLKPLPVECVVRGYLTGSGWKDYQATGTVCGIKLPAGLV
EASKLPEPIFTPATKAELGDHDENISFEEVVELVGAELAAQLRDATLAIYKEAADYAATRGIIIADTKFE
FGLDEDGTLTLMDEVLTPDSSRFWPADSYQPGTSQPSFDKQFVRDWLETSGWDKTAPAPPLPADVIEKTR
AKYREALERLTGKSLD
>gnl|CDD|237572 PRK13962, PRK13962, bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
MNKKTIRDIDVKGKRVIVRVDFNVPLDENGNITDDTRIRAALPTIKYLLDHGAKVILVSHLGRPKGEFDP
KFSMAPVAKRLSELLGKEVIFAKDVIGDDAKKAVAQLKEGDVLLLENVRFHKEETKNDPEFAKELASLAD
IYVNDAFGTAHRAHASTAGVAEYLPAVAGFLMEKEIEFLGKALANPQRPFVAILGGAKVSDKIGVIENLL
EKVDKLLIGGGMAYTFLKAKGYEVGKSLVEEDKLDLAKELLAKAEEKGVKLLLPVDSVVAKEFKNDAEHK
VVPSDAIPEDWMGLDIGPETIELFAKKIADAKTIVWNGPMGVFEFDNFAEGTRAVAEAVAESGAITIIGG
GDSAAAVEKLGFADKMSHISTGGGASLEFLEGKVLPGIACLLDKNPRKPIIAGNWKMNKTPAEAKEFVNE
LKKYVKDAQAEVVVCPPFTALPSVKEAVDGSNIKLGAQNVFYEEKGAYTGEISGPMLAEIGVEYVIIGHS
ERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLSAEQVKKVVIAY
EPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGA
SLKAQEFAAIANYFI
>gnl|CDD|237573 PRK13963, PRK13963, rRNA maturation RNase YbeY
MKSSRSSKSARAEAAQPASPRLSLFDAKGKARTVDAQALRIDFADGRSLMFDLSGSSGDAAVAIVAQHAD
PAMRAMLALRPEHYDSVTLRVGAEPAPDFVDDEDAPAREPELDLTVQYGDEIGGAQRKALPKRKLIAEWI
EPALFADAQLTVRFVGEEEGRTLNRGYRGKDYATNVLTFAYAEEPDGPVIGDLVLCCPVVEKEAREQGKP
LEAHYAHLLVHGALHAQGYDHEDDEDAAEMEALETDILAKLGFPNPYR
>gnl|CDD|184425 PRK13965, PRK13965, ribonucleotide-diphosphate reductase subunit beta; Provisional
QSYYDRSQSPIEYALSETQKPLRSINWNYLNDDKDLEVWNRVTQNFWLPEKVPVSNDLNSWRSLGEDWQQ
LITRTFTGLTLLDTVQATVGDVAQIPHSQTDHEQVIYTNFAFMVAIHARSYGTIFSTLCSSEQIEEAHEW
VVSTESLQRRARVLIPYYTGDDPLKSKVAAAMMPGFLLYGGFYLPFYLSARGKLPNTSDIIRLILRDKVI
HNYYSGYKYQQKVARLSPEKQAEMKAFVFDLLYELIDLEKAYLRELYAGFDLAEDAIRFSLYNAGKFLQN
LGYESPFTEEETRVSPEVFAQLSARADENHDFFSGNGSSYVMGITEETTDDDWEF
>gnl|CDD|140022 PRK13966, nrdF2, ribonucleotide-diphosphate reductase subunit beta; Provisional
MTGNAKLIDRVSAINWNRLQDEKDAEVWDRLTGNFWLPEKVPVSNDIPSWGTLTAGEKQLTMRVFTGLTM
LDTIQGTVGAVSLIPDALTPHEEAVLTNIAFMESVHAKSYSQIFSTLCSTAEIDDAFRWSEENRNLQRKA
EIVLQYYRGDEPLKRKVASTLLESFLFYSGFYLPMYWSSRAKLTNTADMIRLIIRDEAVHGYYIGYKFQR
GLALVDDVTRAELKDYTYELLFELYDNEVEYTQDLYDEVGLTEDVKKFLRYNANKALMNLGYEALFPRDE
TDVNPAILSALSPNADENHDFFSGSGSSYVIGKAVVTEDDDWDF
>gnl|CDD|140023 PRK13967, nrdF1, ribonucleotide-diphosphate reductase subunit beta; Provisional
MTGKLVERVHAINWNRLLDAKDLQVWERLTGNFWLPEKIPLSNDLASWQTLSSTEQQTTIRVFTGLTLLD
TAQATVGAVAMIDDAVTPHEEAVLTNMAFMESVHAKSYSSIFSTLCSTKQIDDAFDWSEQNPYLQRKAQI
IVDYYRGDDALKRKASSVMLESFLFYSGFYLPMYWSSRGKLTNTADLIRLIIRDEAVHGYYIGYKCQRGL
ADLTDAERADHREYTCELLHTLYANEIDYAHDLYDELGWTDDVLPYMRYNANKALANLGYQPAFDRDTCQ
VNPAVRAALDPGAGENHDFFSGSGSSYVMGTHQPTTDTDWDF
>gnl|CDD|184426 PRK13968, PRK13968, putative succinate semialdehyde dehydrogenase; Provisional
MTITPATHAISVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEE
MAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPL
WQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTV
TGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGI
ASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPT
VLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN
GYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVWKDRI
>gnl|CDD|184427 PRK13969, PRK13969, proline racemase; Provisional
MRFSKSIQTIDSHTMGEPTRIVVGGLPKIPGKTMAEKKEYLEENNDSLRTALMSEPRGHNDMFGSIYTEP
ADETADFGIIFMDGGGYLNMCGHGSIGAATCAVETGIVKVEEPYTHIKLEAPAGMINARVKVEDGKAKEV
SIVNVPAFLYKKDVEIDVPDYGKVTLDISFGGSFFAIVDAEQLGIKISPANSQKLNDLGMKIRHAVNEQI
EIKHPVLEHIKTVDLVEIYDEAKHPDADYKNVVIFGQGQVDRSPCGTGTSAKMATLYAKGKLKVGEEFVY
ESIIGTKFKGKILEETKVGEYDAIIPEITGSAYITGFNQFVIDEEDPVKYGFVL
>gnl|CDD|172473 PRK13970, PRK13970, 4-hydroxyproline epimerase
MMKRIQIIDSHTGGEPTRLVVSGFPSLGGGTMAERRDVLAREHDRYRTACILEPRGSDVLVGALLCEPVS
PDAAAGVIFFNNSGYLGMCGHGTIGVVRTLHHMGRIGPGVHRIETPVGTVEATLHDDLSVSVRNVLAYRH
AKDVVVDVPGYGPVKGDIAWGGNWFFLISDHGQRVAGDNVAALTAYASAVRAGLERAGITGANGGEIDHI
ELFADDPEHDSRSFVLCPGHAYDRSPCGTGTSAKLACLAADGKLAPGVVWRQASVIGSVFSASYAAAEGG
IVPTIRGSAHLSAEATLLIEDDDPFGWGIAS
>gnl|CDD|184428 PRK13971, PRK13971, 4-hydroxyproline epimerase
MARHTFFCIDAHTCGNPVRLVAGGGPLLQGATMSEKRAHFLREYDWIRTGLMFEPRGHDMMSGSILYPPT
RPDCDFAILFIETSGCLPMCGHGTIGTVTAAIEEGLVTPKTPGKLRLDTPAGLVDIEYEQDGEKVESVRL
TNVPSYLAAEDLEVEIPGLGPLKVDVAYGGNFYAIVEPQENFPGLDHYSASDILRWSPVLRQALNEKYEF
VHPEDPRIRGVSHVLWTGKPISPGADARNAVFYGDKAIDRSPCGTGTSARMAQLAAKGKLKVGDEFVHES
IIGSLFEGRVEAAATVGGRPAILPSIEGWARVTGHNTIFVDDRDPYAHGFQVK
>gnl|CDD|172475 PRK13972, PRK13972, GSH-dependent disulfide bond oxidoreductase; Provisional
MIDLYFAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSPADGGEPLSLF
ESGAILLYLAEKTGLFLSHETRERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRL
YHVLNKRLENSPWLGGENYSIADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQLGD
ERSDS
>gnl|CDD|237575 PRK13977, PRK13977, myosin-cross-reactive antigen; Provisional
MYYSNGNYEAFARPRKPEGVDNKKAYIIGSGLASLAAAVFLIRDGQMPGENITILEELDVPGGSLDGAGN
PEKGYVARGGREMENHFECLWDLFRSIPSLEDPGASVLDEFYWFNKDDPNYSKARLIHKRGEILDTDKFG
LSKKDRKELLKLLLTPEEKLDDKTIEDWFSPEFFETNFWYYWRTMFAFEKWHSALEMRRYMHRFIHHIGG
LPDLSGLKFTKYNQYESLVLPLIKYLEDHGVDFQYGTKVTDIDFDITGGKKTATAIHLTRNGKEETIDLT
EDDLVFVTNGSITESSTYGDMDTPAPLNRELGGSWTLWKNIAAQSPEFGNPDKFCGDIPESNWESFTVTT
KDPKILPYIERITGRDPGSGKTVTGGIVTFKDSNWLMSITVNRQPHFKNQPKNETVVWGYGLYPDRPGNY
VKKPMRECTGEEILQELLYHLGVPEDKIEELAADSANTIPVMMPYITSQFMPRAKGDRPLVVPEGSTNLA
FIGQFAETPRDTVFTTEYSVRTAMEAVYTLLGVDRGVPEVFPSQYDIRVLLKATYKLNDGKLLLKEGLKK
IKGTYIEELLKEYGLI
>gnl|CDD|184433 PRK13978, PRK13978, ribose 5-phosphate isomerase A
MKDVKALKLMTLNDVLSQINGDMTLGIGTGSTMELLLPQMAQLIKERGYNITGVCTSNKIAFLAKELGIK
ICEINDVDHIDLAIDGADEVDPSLNIIKGGGGALFREKVIDEMASRFVVVVDETKIVQYLGETFKLPVEV
DKFNWYHILRKIESYADIKVERRVNEDVAFITDNGNYILDCKLPKGIDPYKFHEYLIHLTGVFETGYFLD
MADQVIVGTQEGVKILEK
>gnl|CDD|237576 PRK13979, PRK13979, DNA topoisomerase IV subunit A; Provisional
MAKKIVIPKDNNIIKIPLEEAMPENYLPYAVEVAKDRALPDVRDGLKPVHRRILYGAYMLKAFPDKPYYK
SARIVGDILGKYHPHGDSSVYDAMVILAQDFTTRMPLIDGHGNWGSIDGDSAAAMRYTEARLTPIAMEML
RDIDKDVVNMVDNYSDSEKEPEVLPARYPNLLVNGAFGIAVGLATNIPPHNLKEVIDGTLAYIDNNEITT
KELMNYIKGPDLPTGGILIGKKSLLSAYETGEGKVTLRAKTKIEKLENGRLGIVITEFPYRRNKAKLLQT
ISEMTADKKHSKALENISDIRDESDRNGIRAVIEFKKSADEDVAEKVLKYLYKKTDLQCNISFNMVALAD
GKPETMGLKTMLKHYVEHQKEVVTRRTKKELEIAEKRFHIVEGFIKAIGIMDEIIKTIRSSKSKKDASEN
LIEKFGFTDEQAEAILELMLYRLTGLEIVAFEKEYKELEKLIKKLTKILSSEKELLKVIKKELKEVKEKY
GDERRTSIIEDDEKAKIDVEELIVVEDVVITLSNEGFIKRIPLKSYNRSNSNVEDIEYREGDFNKFLIQS
NTKDTLLIFTDKGNMYQIKGINIPEFKWKEKGERLDEIIKGIDLESEKIIEAYSIEDFTPQKDFIFITDS
GGIKKTSLDKFVTNYTKLMALKLKKGEKLIKVKLVDRTREEKFIKIKTKKGLSFTVEEPELEPVDRNIIG
YQLFDLLPNDSIKKVDFCDNYEYKEFYVNINKKGIIKISDKDNKSSISVFTNSSKNLLIFSDEGKVYKIP
AFMLQNIKNEGINISALTGDFEKDEKIIKIISIFEFEEDLSIYFFSKKGLVKKTLLNEFKGEGNSTQAYK
FKHKEDELVNVDIKEHEEKNILLITEKGMAIRFKSEAVNPMGKIASGVTGISLKDEDKVIYGSIIDENDT
RKIKLKSKAKDKGEIEIKDIKLQNRAGRGNSLMPLLLNDFIKDVEIK
>gnl|CDD|184435 PRK13980, PRK13980, NAD synthetase; Provisional
LDLRVLALDYEKVREIIVDFIREEVEKAGAKGVVLGLSGGIDSAVVAYLAVKALGKENVLALLMPSSVSP
PEDLEDAELVAEDLGIEYKVIEITPIVDAFFSAIPDADRLRVGNIMARTRMVLLYDYANRENRLVLGTGN
KSELLLGYFTKYGDGAVDLNPIGDLYKTQVRELARHLGVPEDIIEKPPSADLWEGQTDEGELGFSYETID
EILYLLFDKKMSREEILEELGVPEDLVDRVRRLVQRSQHKRRLPPIPKLSGRTIG
>gnl|CDD|237577 PRK13981, PRK13981, NAD synthetase; Provisional
LRIALAQLNPTVGDIAGNAAKILAAAAEAADAGADLLLFPELFLSGYPPEDLLLRPAFLAACEAALERLA
AATAGGPAVLVGHPWREGGKLYNAAALLDGGEVLATYRKQDLPNYGVFDEKRYFAPGPEPGVVELKGVRI
GVPICEDIWNPEPAETLAEAGAELLLVPNASPYHRGKPDLREAVLRARVRETGLPLVYLNQVGGQDELVF
DGASFVLNADGELAARLPAFEEQIAVVDFDRGEDGWRPLPGPIAPPPEGEAEDYRALVLGLRDYVRKNGF
PGVVLGLSGGIDSALVAAIAVDALGAERVRAVMMPSRYTSEESLDDAAALAKNLGVRYDIIPIEPAFEAF
EAALAPLFAGTEPDITEENLQSRIRGTLLMALSNKFGSLVLTTGNKSEMAVGYATLYGDMAGGFAPIKDV
YKTLVYRLCRWRNTVSPGEVIPERIITKPPSAELRPNQTDQDSLPPYDVLDAILERLVEEEQSVAEIVAA
GFDRATVRRVERLLYIAEYKRRQAAPGVKITRRAFGRDRRYPITNRFRDR
>gnl|CDD|172484 PRK13982, PRK13982, bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Provisional
MASLTIRKLDDAIKAELRQRAAQNGRSMEEEVRVILRDATTPRHGPAASSAAPVSAAAPPAAREQASLAS
KRVTLIIGGGIAAYKALDLIRRLKERGAHVRCVLTKAAQQFVTPLTASALSGQRVYTDLFDPESEFDAGH
IRLARDCDLIVVAPATADLMAKMANGLADDLASAILLAANRPILLAPAMNPLMWNNPATRRNVAQLKRDG
VHMIGPNAGEMAERGEAGVGRMAEPLEIAAAAEALLRPPQPKPLAGRRVLITAGPTHEPIDPVRYIANRS
SGKQGFAIAAAAAAAGAEVTLISGPVDLADPQGVKVIHVESARQMLAAVEAALPADIAIFAAAVADWRVA
TEGGQKLKKGAAGPPPLQLVENPDILATISKLAENRPPLVIGFAAETEHLIDNARAKLARKGCDWIVAND
VSPATGVMGGDRNTVHLLSRDGDAEKVESWPVMTKDEVATALVARIASTFTTPHA
>gnl|CDD|237578 PRK13983, PRK13983, M20 family metallo-hydrolase
DELRDEMIELLSELIAIPAVNPDFGGEGEKEKAEYLESLLKEYGFDEVERYDAPDPRVIEGVRPNIVAKI
PGGDGKRTLWIISHMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPK
YNLGLAFVSDEETGSKYGIQYLLKKHPELFKKDDLILVPDAGNPDGSFIEIAEKSILWLKFTVKGKQCHA
STPENGINAHRAAADFALELDEALHEKFNAKDPLFDPPYSTFEPTKKEANVDNINTIPGRDVFYFDCRVL
PDYDLDEVLKDIKEIADEFEEEYGVKIEVEIVQREQAPPPTPPDSEIVKKLKRAIKEVRGIEPKVGGIGG
GTVAAFLRKKGYPAVVWSTLDETAHQPNEYAKISNLIEDAKVFALLLLES
>gnl|CDD|172486 PRK13984, PRK13984, putative oxidoreductase; Provisional
MPEKDFFAPLKAWKFLFRKPVTIKVPNVKREAAERYRGFHINDWEKCIGCGTCSKICPTDAITMVEVPDL
PQEYGKKPQRPVIDYGRCSFCALCVDICTTGSLKMTREYIHISPDPEDFIFMPTEKGINAKEPDNAPLGW
VRDENSELLDLERVEMEEIPPEERVKSFIEIVKGYSKEQAMQEAARCVECGICTDTCPAHMDIPQYIKAI
YKDDLEEGLRWLYKTNPLSMVCGRVCTHKCETVCSIGHRGEPIAIRWLKRYIVDNVPVEKYSEILDDEPE
KKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKI
HLNTRVGKDIPLEELREKHDAVFLSTGFTLGRSTRIPGTDHPDVIQALPLLREIRDYLRGEGPKPKIPRS
LVVIGGGNVAMDIARSMARLQKMEYGEVNVKVTSLERTFEEMPADMEEIEEGLEEGVVIYPGWGPMEVVI
ENDKVKGVKFKKCVEVFDEEGRFNPKFDESDQIIVEADMVVEAIGQAPDYSYLPEELKSKLEFVRGRILT
NEYGQTSIPWLFAGGDIVHGPDIIHGVADGYWAAEGIDMYLRKQ
>gnl|CDD|184438 PRK13985, ureB, urease subunit alpha
KKISRKEYVSMYGPTTGDKVRLGDTDLIAEVEHDYTIYGEELKFGGGKTLREGMSQSNNPSKEELDLIIT
NALIIDYTGIYKADIGIKDGKIAGIGKGGNKDMQDGVKNNLSVGPATEALAGEGLIVTAGGIDTHIHFIS
PQQIPTAFASGVTTMIGGGTGPADGTNATTITPGRRNLKWMLRAAEEYSMNLGFLGKGNSSNDASLADQI
EAGAIGFKIHEDWGTTPSAINHALDVADKYDVQVAIHTDTLNEAGCVEDTMAAIAGRTMHTFHTEGAGGG
HAPDIIKVAGEHNILPASTNPTIPFTVNTEAEHMDMLMVCHHLDKSIKEDVQFADSRIRPQTIAAEDTLH
DMGIFSITSSDSQAMGRVGEVITRTWQTADKNKKEFGRLKEEKGDNDNFRIKRYLSKYTINPAIAHGISE
YVGSVEVGKVADLVLWSPAFFGVKPNMIIKGGFIALSQMGDANASIPTPQPVYYREMFAHHGKAKYDANI
TFVSQAAYDKGIKEELGLERQVLPVKNCRNITKKDMQFNDTTAHIEVNPETYHVFVDGKEVTSKPANKVS
LAQLFSIF
>gnl|CDD|184439 PRK13986, PRK13986, urease subunit beta
MKLTPKELDKLMLHYAGELAKKRKEKGIKLNYVEAVALISAHIMEEARAGKKTVAELMQEGRTLLKPDDV
MDGVASMIHEVGIEAMFPDGTKLVTVHTPIEANGKLVPGELFLKDEDITINAGKKAVSVKVKNVGDRPVQ
VGSHFHFFEVNRCLEFDREKAFGKRLDIASGTAVRFEPGEEKSVELIDIGGNRRIFGFNALVNRQADNES
KKIALHRAKERGFHG
>gnl|CDD|237579 PRK13987, PRK13987, cell division topological specificity factor MinE; Provisional
MDLFKFFSKKPTSKDVAKERLKLILIHDRGDISPDVLEMIKEDILKVISKYVEIDNEDVDIKMTKSEEID
EGMSPALIANIPIKKIKKKIR
>gnl|CDD|184441 PRK13988, PRK13988, cell division topological specificity factor MinE; Provisional
MTLRDLLEKLFGRQPASASTARERLQLVLAHDRADLSPELLEQMRKEILEVVARYVEIDPEEGEVSLETE
DRMTALVANLPIRRVKRGEIKFKESSK
>gnl|CDD|184442 PRK13989, PRK13989, cell division topological specificity factor MinE; Provisional
MSILSFLLGEKKKTASVAKERLQIIIAHERVGGRQPPDYLPALQKELVAVISKYVKISPDDIRVSLERQD
NLEVLEVKIELPQA
>gnl|CDD|172492 PRK13990, PRK13990, cell division topological specificity factor MinE; Provisional
MLAKLFGLSKKQQSASVAKERLQIIVAHQRSELHPRSSKISSHLLAELKDEIIEVVKKYVALSEENIRDI
DLKVEDSSKNSTIEVNIPFN
>gnl|CDD|172493 PRK13991, PRK13991, cell division topological specificity factor MinE; Provisional
MSFLDGLFGRKRDSSSELAKQRLLTVLVHDRVKLTPEMMEQMKADLAEVIKRYVPAIDAEAIEVTLSRGE
AHDHLKADIPLRRTTQK
>gnl|CDD|237580 PRK13992, minC, septum site-determining protein MinC
MIDFKMTKEGLVLLIKDYQNLEDVLNEIDAKITQMGGFFAKGDKISLMIENHEKHIQDIPKIVSKLRNLG
LEVSQILVGSTKEKDVKVKSRTDVESTGKVIKKNLRSGQTVVHSGDVIVFGNVHKGAEILAGGSVVIFGK
AQGIVRAGLNEGEQSVIAALSLQTSLIQISGFITQSKGEYNVPVIAHVKGGRIVIEPFDKVKFEE
>gnl|CDD|237581 PRK13994, PRK13994, potassium-transporting ATPase subunit C; Provisional
MMNTSVTNTARLLWAGLRALLVLTLVTGVVYPLAVTGVAQGLFHDKANGSEIKADGKVVGSSLIGQRYNL
PLKDGEETPEPDLKWFQPRPANGLGTNSVNTQYSLILSGATNRSADNEELIQWVKDAKAAVVEDNSVPGY
EVKPSDVPADAVTSSGSGLDPDISPAYADLQVHRVAARNGLNVARVQKLVDEHTTGRTLGFIGEPRVNVL
ELNIALRELVAG
>gnl|CDD|184445 PRK13995, PRK13995, K(+)-transporting ATPase subunit C
MKTLKKALLVTIVLLVVCGLIYPLVLTGVSQVVFPKQANGSLVTVNGKEVGSELIGQSFTDARFFKGRVS
AVNYNTYTKEDKGNGNYGGVSSGSQNYAPTNPELHDRVQKDIDKFLKTNPTVKKEDIPTDLLTASGSGLD
PHISPKSAAIQIPAVSKATGISESKLKKIVKDNTEGKTFGVLGEDRVNVLKVNLEIAKILGLF
>gnl|CDD|172497 PRK13996, PRK13996, potassium-transporting ATPase subunit C; Provisional
KKVFPKALLIFLVFTILCGGIYTIFITGLAQLIFPKQANGSIIEVDGKKYGSELLGQQFTDEKHLWGRIM
NIDTGTFVDANGKKLAYSAPSNLSPASKEYEALVQERVEKIRANHPEQDEKPIPVDLVTCSGSGLDPHIS
VAAAKYQVDRIAKNNNMSVKDVEDIIDKYTSGKLFGVLGEKTVNVLKVNLALDGILK
>gnl|CDD|172498 PRK13997, PRK13997, K(+)-transporting ATPase subunit C
MAKKQSILSPIIRITFTFLVLCGLVYPLIVTGIAQAVMKDNADGSLIYNDKNEVIGSKLIGQNFTDPRYF
HGRVSSIEYKAEASGSNNYAPSNPDLEKRVEKSIEEWKKQNPSVPVTEVPIDLVTNSGSGLDPDISPKAA
SVQVERISKLTNIPKETLDQLIKDQTEGAALGLFGETRVNVLKLNLELQKLMK
>gnl|CDD|172499 PRK13998, PRK13998, K(+)-transporting ATPase subunit C
MNTIRNSICLTIITMVLCGFLFPLAITLIGQIFFYQQANGSLITYDNRIVGSKLIGQHWTETRYFHGRPS
AVDYNMNPEKLYKNGVSSGGSNESNGNTELIARMKHHVKFGNSNVTIDAATSSGSGLDPHITVENALKQA
PRIADARHVSTSRVADLIQHRKQRGVLTNDYVNVLELNIALDKMKD
>gnl|CDD|172500 PRK13999, PRK13999, K(+)-transporting ATPase subunit C
MLKELRPALVLLVALTAITGLAYPLAMTGLAGVLFPAQAAGSLIERDGQVIGSALIGQSFTGDRYFHGRP
SATTAADPADASKTVPAPYNAANSMGSNLGPTSKALADRVKEDVDALKAENPGAPVPVDLVTTSGSGLDP
DISPEAALFQVPRVAKARGLPEDRLRDLVAAQVEGRTLGLLGEPRVNVLALNLALDAAAAR
>gnl|CDD|184446 PRK14000, PRK14000, K(+)-transporting ATPase subunit C
MQTIRKSLGLVLIMFVLCGFIFPLTVTALGQVLFPEQANGSLVKQDGKVIGSKLIGQQWTEPKYFHGRIS
AVNYNMNANEVKESGGPASGGSNYGNSNPELKKRVQETIKQEGKKISSDAVTASGSGLDPDITVDNAKQQ
VKRIAKERNIDASKINHLIDENKQASPMADDYVNVLKLNITLDKL
>gnl|CDD|172502 PRK14001, PRK14001, K(+)-transporting ATPase subunit C
MRRQLLPALTMLLVFTVITGIVYPLAVTGVGQLFFGDQANGALLERDGQVIGSAHIGQQFTAAKYFHPRP
SSAGDGYDAAASSGSNLGPTNEKLLAAVAERVTAYRKENNLPADTLVPVDAVTGSGSGLDPAISVVNAKL
QAPRVAQARNISIRQVERLIEDHTDARGLGFLGERAVNVLRLNLALDRL
>gnl|CDD|172503 PRK14002, PRK14002, K(+)-transporting ATPase subunit C
MKNLLKSLKLTLVFCVFFSVFYILALWGFAQLAPNKGNGETITLNGKVVGYANIGQSFTQDIYFWGRPSA
VGYNAAGSGGSNKGPSNPEYLAEVQARIDTFLVHHPYLSRKDIPAEMVTASGSGLDPNISPQAAYVQVKR
VAKARGMSEEKVKQLVDQHVEKPLLGMFGTEKVNVLKLNIALDQLK
>gnl|CDD|184447 PRK14003, PRK14003, K(+)-transporting ATPase subunit C
MSFIREAIRAIRSTLVLWLLTALIYPFLMIAIGQTVFPYQANGSLIKNNQGQVIGSALIGQPFTSDRYFN
SRPSTVNYSTGEPAKPTGISGASNLAPSNPALIERIKEEANRLQDAGIQPTADLVYTSGSGLDPHISPEA
ARAQIERVAKARGLPPDQLEILITKNTDGRFLGIFGEPGVNVLRLNLALDLQKI
>gnl|CDD|172505 PRK14004, hisH, imidazole glycerol phosphate synthase subunit HisH; Provisional
MIAILDYGMGNIHSCLKAVSLYTKDFVFTSDPETIENSKALILPGDGHFDKAMENLNSTGLRSTIDKHVE
SGKPLFGICIGFQILFESSEETNQGTKKEQIEGLGYIKGKIKKFEGKDFKVPHIGWNRLQIRRKDKSKLL
KGIGDQSFFYFIHSYRPTGAEGNAITGLCDYYQEKFPAVVEKENIFGTQFHPEKSHTHGLKLLENFIEFV
>gnl|CDD|184448 PRK14010, PRK14010, K(+)-transporting ATPase subunit B
MAETTKIFESHLVKQALKDSVLKLYPVYMIKNPIMFVVEVGMLLALGLTIYPDLFHQESVSRLYVFSIFI
ILLLTLVFANFSEALAEGRGKAQANALRQTQTEMKARRIKQDGSYEMIDASDLKKGHIVRVATGEQIPND
GKVIKGLATVDESAITGESAPVIKESGGDFDNVIGGTSVASDWLEVEITSEPGHSFLDKMIGLVEGATRK
KTPNEIALFTLLMTLTIIFLVVILTMYPLAKFLNFNLSIAMLIALAVCLIPTTIGGLLSAIGIAGMDRVT
QFNILAKSGRSVETCGDVNVLILDKTGTITYGNRMADAFIPVKSSSFERLVKAAYESSIADDTPEGRSIV
KLAYKQHIDLPQEVGEYIPFTAETRMSGVKFTTREVYKGAPNSMVKRVKEAGGHIPVDLDALVKGVSKKG
GTPLVVLEDNEILGVIYLKDVIKDGLVERFRELREMGIETVMCTGDNELTAATIAKEAGVDRFVAECKPE
DKINVIREEQAKGHIVAMTGDGTNDAPALAEANVGLAMNSGTMSAKEAANLIDLDSNPTKLMEVVLIGKQ
LLMTRGSLTTFSIANDIAKYFAILPAMFMAAMPAMNHLNIMHLHSPESAVLSALIFNALIIVLLIPIAMK
GVKFKGASTQTILMKNMLVYGLGGMIVPFIGIKLIDLIIQLFV
>gnl|CDD|184450 PRK14012, PRK14012, IscS subfamily cysteine desulfurase
MKLPIYLDYSATTPVDPRVAEKMMPYLTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIV
FTSGATESDNLAIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAA
MRDDTILVSIMHVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGP
KGIGALYVRRKPRVRLEAQMHGGGHERGMRSGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNG
IKDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGLNDELAH
SSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEWAHH
>gnl|CDD|237583 PRK14013, PRK14013, hypothetical protein; Provisional
STLRYFRWSFIVTVIGLVLAAWLGGLSALFIVAILAVLEISLSFDNAVVNATVLKRMSPKWQKRFLTWGI
LIAVFGMRLVFPLLIVAVAAGLGPIEALKLALNDPDEYAEILTDAHPQIAAFGGTFLLMVFLNFFFDEEK
DVHWLGWIERPLAKLGKLDGISVIVALVLLLIFSLLLPADEALTVLIAGLLGLLTYLIVEGLGGLFEEEE
EDAMTAVGKAGLGGFLYLEVLDASFSFDGVIGAFAITNDIFIIALGLGIGAMFVRSLTIYLVEKGTLDEY
VYLEHGAHYAIGALAVIMLLSIGVHIPEVITGLIGVALIGLAFWSSIRYNRREANAAT
>gnl|CDD|237584 PRK14014, PRK14014, putative acyltransferase; Provisional
MMNFLLAPLRGLLSILLLILNTLFWSVPIIILGLLKLLLPIPAIRRACSRLLNFIAEAWISINNVILRLL
PRTQWDVEGLEGLSKKGWYLVISNHQSWVDILVLQYVFNRRIPMLKFFLKQELIWVPFLGLAWWALDFPF
MKRYSKAYLAKNPELKGKDLETTRRACEKFKRMPTTIVNFVEGTRFTPEKHQQQQSPYQHLLKPKAGGIA
FALNAMGEQFDGLLDVTIVYPDGRPSFWDLLSGRVKKIVVHVRLLPIPEELIGDYFNDKEFRRRFQQWLN
QLWQEKDQLIEQLLAQYNQNK
>gnl|CDD|237585 PRK14015, pepN, aminopeptidase N; Provisional
MRTQQPQAIYLKDYRPPDYLIDTVDLDFDLDPDKTRVTARLQVRRNPDAAHSAPLVLDGEDLELLSLALD
GQPLAPSAYELDEEGLTIENLPDRFTLEIETEIDPEANTALEGLYRSGGMFCTQCEAEGFRRITYFLDRP
DVLARYTVRIEADKAKYPVLLSNGNLVESGELPDGRHWATWEDPFPKPSYLFALVAGDLDVLEDTFTTRS
GREVALEIYVEPGNLDKCDHAMDSLKKSMKWDEERFGLEYDLDIFMIVAVDDFNMGAMENKGLNIFNSKY
VLADPETATDADYERIESVIAHEYFHNWTGNRVTCRDWFQLSLKEGLTVFRDQEFSADLGSRAVKRIEDV
RVLRAAQFAEDAGPMAHPVRPDSYIEINNFYTATVYEKGAEVIRMLHTLLGEEGFRKGMDLYFERHDGQA
VTCEDFVAAMEDASGRDLSQFRRWYSQAGTPRVTVSDEYDAAAGTYTLTLSQSTPPTPGQPEKQPLHIPV
AIGLLDPDGKELPLQLEGEPVERVLELTEAEQTFTFENVAERPVPSLLRGFSAPVKLEYDYSDEDLLFLM
AHDSDPFNRWEAGQRLATRLLLANVARHGQPLSLDEALIDAFRAVLLDESLDPAFAAELLTLPSEAELAE
QMEVIDPDAIHAAREALRRALATALKDELLALYEALQTDGPYSPDAEAAGRRALRNVCLSYLAAADDEEA
AELAEAQFDQADNMTDRLAALSALVNADLPERDEALADFYDRWKDDPLVMDKWFALQATSPAPDTLERVR
ALMQHPAFDLKNPNRVRSLIGAFAAANPAGFHAADGSGYRFLADQILALDKINPQVAARLATPLIRWRRY
DPKRQALMRAALERIAALPNLSKDVREIVSKALAA
>gnl|CDD|237586 PRK14016, PRK14016, cyanophycin synthetase; Provisional
MKILRIRALRGPNIWSRRPVIEAWVDLEELEDIPSNDIPGFNERLLALLPSLIEHRCSVGERGGFLQRLK
EGTWLGHVLEHVALELQNLAGMPVGFGRTRETSEPGVYQVVFEYKEEEVGREALELAVDLVNAAINDTPF
DLEAALARLRELDEDERLGPSTAAIVDAAEARGIPYIRLGDGSLVQLGYGKYQRRIQAAETDQTSAIAVD
IACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVNITTREEIEAAYA
VASKESSDVIVERYIPGKDHRLLVVGGKLVAAARREPPHVIGDGKHTIRELIEIVNQDPRRGEGHEKPLT
KIKLDDIALLELAKQGYTLDSVPPKGEKVYLRRNANLSTGGTAIDVTDEVHPENAAIAERAAKIIGLDIA
GVDVVCEDISKPLEEQGGAIVEVNAAPGLRMHLAPSEGKPRNVGEAIVDMLFPEGDDGRIPIVAVTGTNG
KTTTTRLIAHILKLSGKRVGMTTTDGVYIDGRLIDKGDCTGPKSARRVLMNPDVEAAVLETARGGILREG
LAYDRCDVGVVTNIGEDHLGLGGINTLEDLAKVKRVVVEAVKPDGYAVLNADDPMVAAMAERCKGKVIFF
SMDPDNPVIAEHRAQGGRAVYVEGDYIVLAEGGWEIRIISLADIPLTLGGKAGFNIENALAAIAAAWALG
IDIELIRAGLRTFVSDAAQAPGRFNLF
>gnl|CDD|184455 PRK14017, PRK14017, galactonate dehydratase; Provisional
MKITKLETFRVPPRWLFLKIETDEGIVGWGEPVVEGRARTVEAAVHELADYLIGKDPRRIEDHWQVMYRG
GFYRGGPILMSAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARARVERGF
TAVKMNGTEELQYIDSPRKVDAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEE
PVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDV
ALAPHCPLGPIALAACLQVDAVSPNAFIQEQSLGIHYNQGADLLDYVKNKEVFAYEDGFVAIPTGPGLGI
EIDEAKVRERAKTGHDWRNPVWRHADGSVAEW
>gnl|CDD|184456 PRK14018, PRK14018, bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide reductase MsrB
MKHRTFFSLCAKFGCLLALGACSPKILDAGTATVPHTLSTLKTADNRPASVYLKKDKPTLIKFWASWCPL
CLSELGETEKWAQDAKFSSANLITVASPGFLHEKKDGDFQKWYAGLDYPKLPVLTDNGGTLAQSLNISVY
PSWAIIGKDGDVQRIVKGSISEAQALALIRNPNADLGSLKHSYYKPDGQKKDSKIMNTRTIYLAGGCFWG
LEAYFQRIDGVVDAVSGYANGNTKNPSYEDVYRHSGHAETVKVTYDADKLSLDTILQYYFRVVDPTSLNK
QGNDTGTQYRSGVYYTDPADKAVIAAALKREQQKYQLPLVVENEPLKNFYDAEEYHQDYLIKNPNGYCHI
DLRKADEPLPGKTKTAPQGKGFDAATYKKPSDAELKRTLTEEQYQITQNAATERAFSHEYDHLFKPGIYV
DVVSGEPLFSSADKYDSGCGWPSFTRPIDAKVVTEHDDFSYNMRRTEVRSRAADSHLGHVFPDGPRDKGG
LRYCINGASLKFIPLEQMDAAGYGALKKKVK
>gnl|CDD|237587 PRK14019, PRK14019, bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II
MTLASIEEIIADIRAGRMVILVDEEDRENEGDLVMAAEFVTPEAINFMAKHGRGLICLTLTEERCEQLGL
PLMTYRNGTQYGTNFTVSIEAAEGVTTGISAADRARTIQAAVARDAKPEDIVQPGHIFPLMAQPGGVLVR
AGHTEAGCDLAALAGLTPAAVICEIMKDDGTMARLPDLEEFAKEHGLKIGTIADLIHYRSRTESIVERVA
ERPMQTAHGEFRLVAYRDKPSGSTHLALVKGTICPDEETLVRVHEPLSVLDLLEVGQPTHSWSLDAAMAA
IAEAGSGVVVLLNCGDDGEHLLDRFRAEEAAAALKRRPVDYRTYGIGAQILRDLGVGKMRLLSSPRKFPS
MSGFGLEVTGYVPMPGS
>gnl|CDD|184458 PRK14021, PRK14021, bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
GKPTRRPQAVIIGMMGAGKTRVGKEVAQMMRLPFADADVEIEREIGMSIPSYFEEYGEPAFREVEADVVA
DMLEDFDGIFSLGGGAPMTPSTQHALASYIAHGGRVVYLDADPKEAMERANRGGGRPMLNGDANKRWKKL
FKQRDPVFRQVANVHVHTRGLTPQAAAKKLIDMVAERTVHVTGAGIEPYDVRIGEGAMNHLPQVLGPKPV
KVALIHTQPVQRHSDRARTLLRQGGYEVSDIVIPDAEAGKTIEVANGIWQRLGNEGFTRSDAIVGLGGGA
ATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGKTGINTPQGKNLVGSFYTPAGVLADTKTLATLPND
IFIEGLGEVAKSGFIRDPEILRILEDHAAELRAFDGSTFLGSPLEDVVAELIERTVKVKAYHVSSDLKEA
GLREFLNYGHTLGHAIEKLEHFRWRHGNAVAVGMVYAAELAHLLGYIDQDLVDYHRSLLASLGLPTSWNG
GSFDDVLALMHRDKKARGNELRFVVLDEIGHPVHLDNPPAEAVEEAFRRIQQ
>gnl|CDD|237588 PRK14022, PRK14022, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase
ITIETLLDILKKDHNFREIIDQDHYHYNYSGVQFDDISYDSRTADEGTLFFAKGAYFKHKFLQNAITQGL
KLYVSEKDYEVGIPQVIVPDIKKAMSLIAMEFYDNPQHKLKLLAFTGTKGKTTAAYFAYHILKQLHKPAM
LSTMNTTLDGETFFKSALTTPESLDLFKMMAEAVDNGMTHLIMEVSSQAYLVGRVYGLTFDVGVFLNITP
DHIGPIEHPTFEDYFYHKRLLMENSKAVVVNSDMDHFSELLEQVTPQEHDFYGIDSENQIMASNAFSFEA
TGKLAGTYDIQLIGKFNQENAMAAGLACLRLGASLEDIQKGIAQTPVPGRMEVLTQSNGAKVFIDYAHNG
DSLNKLIDVVEEHQKGKLILLLGAAGNKGESRRPDFGRVANRHPYLQVILTADDPNNEDPKMITQEIASH
ITHPVEIIDDRAEAIKHAMSITEGPGDAVIIAGKGADAYQIVPGHRDDYIGDEAAAKKYLG
>gnl|CDD|184460 PRK14023, PRK14023, homoaconitate hydratase small subunit; Provisional
MARVWKFGDNINTDDILPGKYAPFMVGEDRFHNYAFAHLRPEFASTVRPGDILVAGRNFGLGSSREYAPE
ALKMLGIGAIIAKSYARIFYRNLVNLGIPPFESEEVVDALEDGDEVELDLETGVLTRGGETFQLRPPPEF
LLEALKEGSILEYYRKHGRFPGEVPV
>gnl|CDD|237589 PRK14024, PRK14024, phosphoribosyl isomerase A; Provisional
TMSLTLLPAVDVVDGQAVRLVQGEAGSETSYGSPLDAALAWQRDGAEWIHLVDLDAAFGRGSNRELLAEV
VGKLDVKVELSGGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAVGLDVRGHTLAARG
WTRDGGDLWEVLERLDSAGCSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRALAE
LVPLGVEGAIVGKALYAGAFTLPEALAVVRR
>gnl|CDD|184462 PRK14025, PRK14025, multifunctional 3-isopropylmalate dehydrogenase/D-malate dehydrogenase; Provisional
MHKICVIEGDGIGKEVVPAALHVLEATGLPFEFVYAEAGDEVFEKTGKALPEETIEAAKEADAVLFGAAG
ETAADVIVKLRRILDTYANVRPVKSYKGVKCLYPDIDYVIVRENTEGLYKGIEAEIADGVTVATRVITRK
ASERIFRFAFEMAKRRKKMGKEGKVTCAHKANVLKKTDGLFKKTFYEVAKEYPDIKAEDYYVDAMNMYII
TRPQTFDVVVTSNLFGDILSDGAAGLVGGLGLAPSANIGDKYGLFEPVHGSAPDIAGKGIANPTATILTA
VLMLRHLGENEEADKVEKALEEVLALGLTTPDLGGNLSTMEMAEEVAKRV
>gnl|CDD|172521 PRK14027, PRK14027, quinate/shikimate dehydrogenase (NAD+)
MNDSILLGLIGQGLDLSRTPAMHEAEGLAQGRATVYRRIDTLGSRASGQDLKTLLDAALYLGFNGLNITH
PYKQAVLPLLDEVSEQATQLGAVNTVVIDATGHTTGHNTDVSGFGRGMEEGLPNAKLDSVVQVGAGGVGN
AVAYALVTHGVQKLQVADLDTSRAQALADVINNAVGREAVVGVDARGIEDVIAAADGVVNATPMGMPAHP
GTAFDVSCLTKDHWVGDVVYMPIETELLKAARALGCETLDGTRMAIHQAVDAFRLFTGLEPDVSRMRETF
LSL
>gnl|CDD|172522 PRK14028, PRK14028, pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
MRIETVWLGRGGQGIVTATYIIANAAVIDGFYAIANPEFGAERRGAPVKAFLTISKNPIEDQEPVKTPDV
AVIFDDKLIDPMRFAIDAVKPGGYVILNTGKQPEEARKLVGRDDVYIVVLDAIGIARKHLKLDVPNGPLA
GAFSKVMGFPSLESIRTAFETQLGKAVEENFAATKEAYEVAVVIPPEKVDASAKPKGIISTTSAFLTGPY
ELVGWQEVNKAGAVFPGSSFPYLTGGWRIDKPVIDHSKCIMCRKCWLYCPDDAIIEAWREAEGPRGRKFR
MKMIDFDYQYCKGCGVCAEVCPTGAIQMVREI
>gnl|CDD|172523 PRK14029, PRK14029, pyruvate/ketoisovalerate ferredoxin oxidoreductase subunit gamma; Provisional
MIEIRFHGRGGQGAVTAANILAEAAFLEGKYVQAFPFFGVERRGAPVTAFTRIDEKPIRIKTQIYEPDVV
VVLDPSLLDTVDVTAGLKDGGIVIVNTEKSKEEVLEKLKKKPKKLALVDATTIALEILGLPITNTAILGA
VAKATGLVKIESVEEAIKDTFSGELGEKNAKAAREAFEKTVVYEL
>gnl|CDD|184463 PRK14030, PRK14030, glutamate dehydrogenase; Provisional
MNIEKIMTSLEAKHPGESEYLQAVKEVLLSVEDVYNQHPEFEKAKIIERIVEPDRIFTFRVPWVDDKGEV
QVNLGYRVQFNNAIGPYKGGIRFHPSVNLSILKFLGFEQTFKNALTTLPMGGGKGGSDFSPRGKSDAEIM
RFCQAFMLELWRHIGPDTDVPAGDIGVGGREVGYMFGMYKKLTREFTGTLTGKGLEFGGSLIRPEATGFG
ALYFVHQMLETKGIDIKGKTVAISGFGNVAWGAATKATELGAKVVTISGPDGYIYDPDGISGEKIDYMLE
LRASGNDIVAPYAEKFPGSTFFAGKKPWEQKVDIALPCATQNELNGEDADKLIKNGVLCVAEVSNMGCTA
EAIDKFIAAKQLFAPGKAVNAGGVATSGLEMSQNAMHLSWSAEEVDEKLHQIMSGIHEQCVKYGKEGDGY
INYVKGANIAGFMKVAKAMLAQGVV
>gnl|CDD|184464 PRK14031, PRK14031, NADP-specific glutamate dehydrogenase
MNAAKVLEDLKRRFPNEPEYHQAVEEVLSTIEEEYNKHPEFDKANLIERLCIPDRVYQFRVTWVDDKGNV
QTNMGYRVQHNNAIGPYKGGIRFHASVNLGILKFLAFEQTFKNSLTTLPMGGGKGGSDFSPRGKSNAEVM
RFCQAFMLELWRHIGPETDVPAGDIGVGGREVGFMFGMYKKLSHEFTGTFTGKGREFGGSLIRPEATGYG
NIYFLMEMLKTKGTDLKGKVCLVSGSGNVAQYTAEKVLELGGKVVTMSDSDGYIYDPDGIDREKLDYIME
LKNLYRGRIREYAEKYGCKYVEGARPWGEKGDIALPSATQNELNGDDARQLVANGVIAVSEGANMPSTPE
AIKVFQDAKILYAPGKAANAGGVSVSGLEMTQNSIKLSWSSEEVDEKLKSIMKNIHEACVQYGTEADGYV
NYVKGANVAGFMKVAKAMMAQGIV
>gnl|CDD|184465 PRK14032, PRK14032, citrate synthase; Provisional
MLEEFLDELSELCEKNNKIDPELYDKYDVKRGLRNEDGTGVLVGLTNIGDVHGYEIDDGEKIPDEGKLYY
RGYDIKDLVNGFLKEKRFGFEEVAYLLLFGELPTKEELAEFTELLGDYRELPDGFTRDMILKAPSKDIMN
SLARSVLALYSYDDNPDDTSIDNVLRQSISLIARFPTLAVYAYQAYRHYHDGKSLYIHPPKPELSTAENI
LYMLRPDNKYTELEARLLDLALVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIK
VMEMFEDIKENVKDWEDEDEIADYLTKILNKEAFDKSGLIYGMGHAVYTISDPRAVILKKFAEKLAKEKG
REEEFNLYEKIEKLAPELIAEERGIYKGVSANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIEE
LVNGGKIIRPAYKSVLERREYVPLEER
>gnl|CDD|237590 PRK14033, PRK14033, bifunctional 2-methylcitrate synthase/citrate synthase
MTTDETPEIKKGLAGVVVDTTAISKVVPETNSLTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALF
SQRERAYRRLDRSVLSLIDKLPTTCHPMDVVRTAVSYLGAEDPEADDSSPEANLAKALRLFAVLPTIVAA
DQRRRRGLDPIAPRSDLGYAENFLHMCFGEVPEPEVVRAFEVSLILYAEHSFNASTFTARVITSTLSDIY
SAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAAEWLRDALARKEKVMGFGHRVYKHGDSRVPTMKAA
LRRVAAVRDGQRWLDIYEALEKAMAEATGIKPNLDFPAGPAYYLMGFDIDFFTPIFVMSRITGWTAHIME
QRASNALIRPLSEYNGPEQREVPPI
>gnl|CDD|184467 PRK14034, PRK14034, citrate synthase; Provisional
MTVTRGLEGVVATTSSVSSIIDDTLTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENA
KVPGEIIEHLKQYDLKKVHPMSVLRTAISMLGLYDEEAEIMDEEANYRKAVRLQAKVPTIVAAFSRIRKG
LDPVEPRKDLSLAANFLYMLNGEEPDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAI
GALKGPLHGGANENVMKMLTEIGEEENVESYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSKRLTVL
LGEEKWYNMSIKIEEIVTKEKGLPPNVDFYSASVYHCLGIDHDLFTPIFAISRMSGWLAHILEQYENNRL
IRPRADYVGPTHQVYVPIEERI
>gnl|CDD|184468 PRK14035, PRK14035, citrate synthase; Provisional
AELQRGLEGVIAAETKISSIIDSQLTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYM
TLNDRVYQHFEEYSTDHVHPMTALRTSVSYLAHFDPDAEEESDEARYERAIRIQAKVASLVTAFARVRQG
KEPLKPRPDLSYAANFLYMLRGELPTDIEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAV
GSLKGPLHGGANERVMDMLSEIRSIGDVDAYLDEKFANKEKIMGFGHRVYKDGDPRAKYLREMSRKITKG
TGREELFEMSVKIEKRMKEEKGLIPNVDFYSATVYHVMGIPHDLFTPIFAVSRVAGWIAHILEQYKDNRI
MRPRAKYIGETNRKYIPIEER
>gnl|CDD|237591 PRK14036, PRK14036, citrate synthase; Provisional
VCEYRPGLEGVPATQSSISYVDGQKGILEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVR
MHRRVKYRIRDMMKCFPETGHPMDALQASAAALGLFYSRRALDDPEYIRDAVVRLIAKIPTMVAAFQLIR
KGNDPIQPRDDLDYAANFLYMLTEREPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIAS
AVGTLAGPLHGGANEDVLAMLEEIGSVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAEELF
ARFGHDEYYEIALELERVAEERLGPKGIYPNVDFYSGLVYRKLGIPRDLFTPIFAIARVAGWLAHWREQL
GANRIFRPTQIYTGSHNRRYIPLEERS
>gnl|CDD|184470 PRK14037, PRK14037, citrate synthase; Provisional
MSVISKGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLN
EEYEVPQEVIDSIYLMPRDSDAIGLMEAAFAALASIDKNFKWKENDKEKAISIIAKMATIVANVYRRKEG
NKPRIPEPSDSFAESFLLASFAREPTAEEIKAMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAAL
AALKGPLHGGAAEEAFKQFVEIGDPNNVEMWFNDKIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIE
RNSEAKKYFEIAQKLEELGIKQFGSKGIYPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLAHIIEYV
EEQHRLIRPRALYVGPEHREYVPIDKR
>gnl|CDD|172532 PRK14038, PRK14038, ADP-specific glucokinase
MNWDELYASAFERVRNSIGKVKGVLLAYNTNIDAIKYLKREDLERRIEKAGKEEVLRYSEELPKRINSIP
QLLGSILWSIRRGKAAELFVESCEVRFYMRQWGWDELRMGGQVGIMANLLGGVYGVPVIAHVPQLSKLQA
SLFLDGPIYVPTFEGGELKLVHPREFVGDEENCIHYIYEFPRGFRVFDFEAPRENRFIGAADDYNPNLYI
RPEFRERFEEIAKKAELAIISGLQALTEENYREPFETVREHLKVLNERGIPAHLEFAFTPDETVREEILG
LLGKFYSVGLNEVELASIMEVMGEKTLAEKLLAKDPVDPIAVTEAMLKLAEKTGVKRIHFHTYGYYLALT
KYRGEHVRDALLFAALAAAAKAMLGNIEKIDDVRKALDVPVNEKALEVEEALEKEYGMENGIGEVEDYQL
AFIPTKIVAKPKSTVGIGDTISSSAFVGEFALR
>gnl|CDD|184471 PRK14039, PRK14039, ADP-dependent glucokinase; Provisional
MNILCGYNVNIDSVYRITGAEIEELLRTFEKAEILEKIENPPGKILSLSDFVAGLIHCMKNGCGAEWLVF
EQSVFEFLKNRFFDNSEIRMGGNAGIMANVLSELGASRVVPNVAVPSKTQLSLFSKKAVYFPGMPLQASE
TDGEKVGASSSDQEPIHFVFDFREGETFSLYGTRIRAPRENRFIATFDHLNFRLFINPAFEQYALEHAGE
MDGALISGFHLLLETYPDGSTYREKLEDSLAQLKWWKSKNEKLRIHAELGHFASKEIANSVFLILAGIVD
SIGMNEDELAMLANLHGIPAEGILEMNAEAIGEAACQLASESGLQRLIIHTREFVLCVSKPDVKMAKKKI
EAMEFGLKCAGVYAASGSLDGREFVEKEASKLQESDFGREQVELFLKAFGGKALGLGAYGLREGYSVCIL
PTLVSKSPVTTVGLGDTLTAGTFLRLLELDVQA
>gnl|CDD|237592 PRK14040, PRK14040, oxaloacetate decarboxylase subunit alpha
MSKPLAITDVVLRDAHQSLFATRLRLDDMLPIAAKLDKVGYWSLESWGGATFDACIRFLGEDPWERLREL
KKAMPNTPQQMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHA
QGTLSYTTSPVHTLQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRVDVPLHLHCHATTG
LSTATLLKAIEAGIDGVDTAISSMSMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAK
FEGQLKGVDSRILVAQVPGGMLTNMESQLKEQGAADKLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQAV
LNVLTGERYKTITKETAGVLKGEYGATPAPVNAELQARVLEGAEPITCRPADLLAPELDKLEAELRRQAQ
EKGITLAENAIDDVLTYALFPQIGLKFLENRHNPAAFEPVPQAEAAQPAAKAEPAGSETYTVEVEGKAYV
VKVSEGGDISQITPAAPAAAPAAAAAAAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKM
ETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA
>gnl|CDD|237593 PRK14041, PRK14041, pyruvate carboxylase subunit B
MKVMFVDTTLRDGHQSLIATRMRTEDMLPALEAFDRMGFYSMEVWGGATFDVCVRFLNENPWERLKEIRK
RLKNTKIQMLLRGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQG
AISYTVSPVHTLEYYLEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKFGVPVEVHSHCTTGLA
SLAYLAAVEAGADMFDTAISPFSMGTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYD
VGMKSPDSRILVSQIPGGMYSNLVKQLKEQKMLHKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQAVLN
VLTGERYKRVTNETKNYVKGLYGRPPAPIDEELMKKILGDEKPIDCRPADLLEPELEKARKELGILAETD
EDLLIYVILGEVGKKFLKKKYEEKIGVDFNLLEELSGFTDDMPVYPV
>gnl|CDD|172536 PRK14042, PRK14042, pyruvate carboxylase subunit B; Provisional
MSKTFITDVTLRDAHQCLIATRMRTEDMLPICNKMDDVGFWAMEVWGGATFDACLRFLKEDPWSRLRQLR
QALPNTQLSMLLRGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQ
GAICYTTSPVHTLDNFLELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLKQATGLPVHLHSHSTSGL
ASICHYEAVLAGCNHIDTAISSFSGGASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQF
ESEAQNIDPRVQLYQVPGGMISNLYNQLKEQNALDKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQAVI
NVLTGERYKTITNEVKLYCQGKYGTPPGKISSALRKKAIGRTEVIEVRPGDLLPNELDQLQNEISDLALS
DEDVLLYAMFPEIGRQFLEQRKNNQLIPEPLLTQSSAPDNSVMSEFDIILHGESYHVKVAGYGMIEHGQQ
SCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMK
METEIKAPANGVVAEILCQKGDKVTPGQVLIRVEVS
>gnl|CDD|172537 PRK14045, PRK14045, 1-aminocyclopropane-1-carboxylate deaminase; Provisional
MHPKVDALLSKFPRVELIPWETPIQYLPNISRELGADVYVKRDDLTGLGIGGNKIRKLEYLLGDALSRGA
DVVITVGAVHSNHAFVTGLAAKKLGLDAVLVLRGKEELKGNYLLDKIMGIETRVYEAKDSFELMKYAEEV
AEELKGEGRKPYIIPPGGASPVGTLGYVRAVGEIATQVKKLGVRFDSIVVAVGSGGTLAGLSLGLAILNA
EWRVVGIAVGSFGEKMKEKVKNLVKKTKELLGVKVKVQEPELYDYSFGEYGKITKEVAKLIRSVGTMEGL
ILDPVYTGKAFYGLMDLAKKGELGEKILFIHTGGISGTFHYGDKMLSLL
>gnl|CDD|237594 PRK14046, PRK14046, malate--CoA ligase subunit beta; Provisional
MDIHEYQAKELLASFGVAVPRGALAYSPEQAVYRARELGGWHWVVKAQIHSGARGKAGGIKLCRTYNEVR
DAAEDLLGKKLVTHQTGPEGKPVQRVYVETADPIERELYLGFVLDRKSERVRVIASARGGMEIEEIAAKE
PEAIIQVVVEPAVGLQQFQAREIAFGLGLDIKQVSRAVKTIMGCYRAFRDLDATMLEINPLVVTKDDRVL
ALDAKMSFDDNALFRRPNIAEMRDPSQEDPREAQAAEHGLSYVGLDGDIGCIVNGAGLAMATMDMIKLAG
GEPANFLDVGGGASPERVAKAFRLVLSDRNVKAILVNIFAGINRCDWVAEGVVQAAREVGIDVPLVVRLA
GTNVEEGRKILAESGLPIITADTLAEAAEKAVEAWKGAKAAK
>gnl|CDD|172540 PRK14048, PRK14048, ferrichrome/ferrioxamine B periplasmic transporter; Provisional
LLLCRRSLVRLVAFLAIAFLALSALAEVQWPMTVTDAVGREVTIPAPPKAVLLGSGFNLIALSLIHPDPV
SLLAGWSGDMKGDNPEIYESFLRKFPELADVPLIDDGSGPGLSFETILTLKADLAILANWQADTEAGQRA
IEYLESIGVPVIVVDFNNEALKNTPDNMRLLGKVFEREEQAEDFARFYEERLARIRDRVAKHSEPGPTVL
MEAFPAADRCCWAYGRGGLGEFIALTGSRNIAEGALPRPGGMMNAEAIMAENPDVYIATSSPGGKYSGFS
IGPGVSAEEAETTLANVVDKPVMASIAAVRDGRVHGLWNFFNAVPLNIVAAEAFASWLRPELFADIDPAA
TLAEINRRFAAVPFEGSYWISLKK
>gnl|CDD|172541 PRK14049, PRK14049, ferrioxamine B receptor precursor protein; Provisional
RSADLLPLIRAALAGTSALALVATAQAQDAGQESVSNEASTALETLVVNGGSGGVITADGYVATSSATGA
KVDTPFLETPQSISSVTEQQLKDRNPQTLLETLAYTPGARVGAFGFDPRFDAFFVRGFDVTYTGVFRDNL
RQPGASSSIFKTEPYGLEGVSILRGPSSALYGASGAGGLFNLITKRPTEEPLREVQVQYGTNNRYQGQFD
FSGPVNETDPVYYRLTGLLRDADTEQVGVPDDRAYIAPAFTWKPDEDTRLTVLGEYSRTKTGGTAAYYND
PLTGEVTDIFAGNPAFNDSVQKQGRIGYEFEHRLNDTFVFRQNARVSTLNIDADWAFAYAPNAADPTLLD
SSAGTYDERLTAFVIDNQLEAKFDTGAFEHTLLAGVDYTKLRFRALNGRGVSPPLDTKNPTQGRPVAAID
FSTRTVQDQWQLGTYLQDQIRYDAWTLTAGGRYDWVSTDTDTTDLATDSLTTVSQKDKEFSGRIGLTYET
DFGLAPYISYSTAFSPNAGFNRATNQPFKPTESEQQEVGVKYLLPNSNTLITAALFNIDQTNGLYYEVVF
LAAGPTNIQVQRGKLRSRGFELEANTSLDNGLSLIASYTYTDVKIIQGPEGTIGNEVSSVPNHMASAWAH
YTLPEGGPLYGLGLGAGARFVGSSYGNDQNTFKNSSRVLFDASVGYDFAAIDKKYEGLMLQVNATNLFDR
RKAVCTAGFCYRDQGRTVIGSLRYNW
>gnl|CDD|237595 PRK14050, PRK14050, TonB-dependent siderophore receptor
MMCRSRGLHFMMLLAAGVALAALVLSGLVAAQEGNTTQLETIVVEGGNAASATATGPVDGYVAKATATGS
KTDTPITEIPQSVSVVGRQEMDDRGVTNKVDEALRYTPGVLSQPFGTDGDTDWFYIRGFDATQTGVFLDG
LNLFSYGFGGFQIDPFMLERVEVLKGPASVLYGGSNPGGIVNMVSKRPLDEPLYYTEIGINSYGNAFTGF
DVGDKLSDDGTVRYRVTGKVAGGDNYSDYSEDLRGFIMPQITYAPDDATSLTVYGYLSGLDQVHVGNGFL
PYVGTVVDAPFGKIDRDAFYGEPDIDNGSYAQQMLGYEFSHEFDNGWTFSQNARYGHLHKHEKGPYTYGY
VGGATGLPDPTGPDYMLNRIGFEHRSKVDSFSIDNRLEGEFDTGALTHNLLFGLDYKYYRLDQVQACCGA
TPISATNPVYGTTQGANFVYLDQILTQQQIGIYAQDQIRFGDGWLVTLNGRYDYVDTDSDARIGTSYESN
DGALSGRAGLAYEFDNGLTPYVSAATFFNPLVGTLASGPPLKPEEGEQYEAGIKYEPSFIDGLITASVFQ
ITKKNVTVTDPLTFASTQLGEVRSRGFELEGKVNLDDNWKALASFTYTDLEITEDANPSLIGNSPYLVPE
TQASLWLDYAVTDGAFEGVSLGAGVRYQGESWADEANTLKVPAATLFDAAIRYEKNDWGASLNVANLFDK
EYVAGCQGLLVCGYGESRTITLKLSKKW
>gnl|CDD|184476 PRK14051, PRK14051, negative regulator GrlR; Provisional
MIMKDGIYSIIFISNEDSCGEGILIKNGNMITGGDIASVYQGVLSEDEDIILHVHRYNYEIPSVLNIEQD
YQLVIPKKVLSNDNNLTLHCHVRGNEKLFVDVYAKFIEPLVIKNTGMPQVYLK
>gnl|CDD|184477 PRK14052, PRK14052, adenosine monophosphate-protein transferase vopS
MISFGNVSALQAAMPQARNEILNEGKLSIGGKEYHINADTQQFTRTNPTSSAVARFFEATGKLFREGSSQ
SVAKAITKAVFDNEQGQAQRLQSASSVEHGQMLFKDGNLKTPSDVLNAFAKLDSKMVKSHSAELNQLAER
AMSESLLDTKSGKNLKSLIGEQATKSLAGKVVKDYGGGVSAAQKNPTNAINQLEAVFDMEVKNLKAAQRH
IEGLASTDLSQGVYAEGLAEDAFNKNGVTDNVERAAAWIINASTSKGNDAENITALLKEYAHNGKDLLNM
DNLKELHARLVPNIERDYRGPAISGGTLPSSIGGEGMLKQHIEGFLKENPVADKDLGKQLFAGVIGYHGF
TDGNGRMGRMLYAIAELRNDSFNPLAMNAENSLHGIK
>gnl|CDD|237596 PRK14053, PRK14053, methyltransferase; Provisional
MKTIAEKWPVVKGDYTVGNPESRIAVVTLASSIESFPEAAIWGSSKTENLGVEKIIVNVISNSNIRYVLL
CGGESRGHLAGHSLLAIHANGIDEKGRIVGSEGAIPFIENISREAVQRFQQQVELLDRIGLTDLEEIRKI
VDDYKDKGEAYPEEPVLVCSPKKRQQTFAVPISGDIIISEEFVMDSFAGIIYTA
>gnl|CDD|172547 PRK14055, PRK14055, aromatic amino acid hydroxylase; Provisional
MHYCERTLDPKYILKIALKLRQSLSLFFQNSQSLQRAYSTPYSYYRIILQKENKEKQALARHKCISILEF
FKNLLFVHLLSLSKNQREGCSTDMAVVSTPFFNRNLWYRLLSSRFSLWKSYCPRFFLDYLEAFGLLSDFL
DHQAVIKFFELETHFSYYPVSGFVAPHQYLSLLQDRYFPIASVMRTLDKDNFSLTPDLIHDLLGHVPWLL
HPSFSEFFINMGRLFTKVIEKVQALPSKKQRIQTLQSNLIAIVRCFWFTVESGLIENHEGRKAYGAVLIS
SPQELGHAFIDNVRVLPLELDQIIRLPFNTSTPQETLFSIRHFDELVELTSKLEWMLDQGLLESIPLYNQ
EKYLSGFEVLCQ
>gnl|CDD|237598 PRK14056, PRK14056, aromatic amino acid hydroxylase
KKTELPSHLKPFVSPQHYDQYTPVDHAVWRYVMRQNHSFLKDVAHPAYLNGLQSTGINIERIPKVEEMNE
CLAEIGWGAVAVDGFIPPVAFFEFQGHGVLPIATDIRKVENIEYTPAPDIIHEAAGHAPILADPTYAEYL
RRFGEIGAKAISSKEDHDVFEAVRTLSIVKESPTSTPEEVAAAENRVIEKQNLVSGLSEAEQISRLFWWT
VEYGLIGTLDNPKIYGAGLLSSVGESKHCLTDAVEKVPFSIEACTSTTYDITKMQPQLFVCPDFEELSEV
LEEFAETMAFRTGGLEGLEKAIRSENLATAELSSGLQITGTFTETIENDAGELIYMRTTGPTALAYHNKE
LAGHSTSVHSDGFGTPIGKLKGNIALEDCTPEQLQALGITIGNIAELEFESGIHVKGTVTDGVKNDGKIA
LISFINCTVTYNGRVLFDPSWGAFDMAVGSTITSVFPGPADAAAFFPMTHGPGEETIKIKAPLELNELER
LYQTVRDIREGGILHDATIEQLVAIQEVLKKFHPKDWLLRLEILELLLEHNKGHELSAALLQQLSTLTTD
EPEVTRLINNGLTLLPVK
>gnl|CDD|172549 PRK14057, PRK14057, epimerase; Provisional
MNSQFAGLTREACVALLASYPLSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVG
QLPQTFIKDVHLMVADQWTAAQACVKAGAHCITLQAEGDIHLHHTLSWLGQQTVPVIGGEMPVIRGISLC
PATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVAQLLCLLGDKREGKIIVIDGSLTQDQLPSL
IAQGIDRVVSGSALFRDDRLVENTRSWRAMFKVAGDTTFLPSTA
>gnl|CDD|237599 PRK14058, PRK14058 [LysW]-aminoadipate/[LysW]-glutamate kinase
MIVVKIGGSVGIDPEDALIDVASLWADGERVVLVHGGSDEVNELLERLGIEPRFVTSPSGVTSRYTDRET
LEVFIMAMALINKQLVERLQSLGVNAVGLSGLDGGLLEGKRKKAVRVVEEGKKKIIRGDYTGKIEEVNTD
LLKLLLKAGYLPVVAPPALSEEGEPLNVDGDRAAAAIAGALKAEALVLLSDVPGLLRDPPDEGSLIERIT
PEEAEELSKAAGGGMKKKVLMAAEAVEGGVGRVIIADANVDDPISAALAGEGTVIVNG
>gnl|CDD|184482 PRK14059, PRK14059, pyrimidine reductase family protein
DTALTLLSSVRELDDGELAELYAYPDGLDRPWLRANFVTSLDGAATVDGRSGGLGGPADRRVFGLLRALA
DVVVVGAGTVRAENYGGVRLSAAARQQRQARGQAEVPPIAVVSRSGDLDPDSRLFTETEVPPLVLTCAAA
AADRRRRLAGLAEVADVVVAGPDTVDLAAAVAALAARGLRRILCEGGPTLLGQLLAADLVDELCLTIAPV
LAGGVARRIVTGPGQAPTRMRLAHVLTDDDGYLFLRYVRAR
>gnl|CDD|172552 PRK14061, PRK14061, unknown domain/lipoate-protein ligase A fusion protein; Provisional
MARTKLKFRLHRAVIVLFCLALLVALMQGASWFSQNHQRQRNPQLEELARTLARQVTLNVAPLMRTDSPD
EKRIQAILDQLTDESRILDAGVYDEQGDLIARSGESVEVRDRLALDGKKAGGYFNQQIVEPIAGKNGPLG
YLRLTLDTHTLATEAQQVDNTTNILRLMLLLSLAIGVVLTRTLLQGKRTRWQQSPFLLTASKPVPEEEES
EKKECPITTRKEIVMSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKEC
NTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVV
KTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGIP
HEQVCEAITEAFFAHYGERVEAEIISPDKTPDLPNFAETFARQSSWEWNFGQAPAFSHLLDERFSWGGVE
LHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFPDQEKELRELSTWIAGA
VR
>gnl|CDD|184483 PRK14063, PRK14063, exodeoxyribonuclease VII small subunit; Provisional
MENKLSFEEAISQLEHLVSKLEQGDVPLEEAISYFKEGMELSKLCDEKLKNVQEQMAVILGEDGELEPFT
ALGDEA
>gnl|CDD|172554 PRK14064, PRK14064, exodeoxyribonuclease VII small subunit; Provisional
MATKKKTFEEAIAELETIVEALENGSASLEDSLDMYQKGIELTKLCQDKLQSAEKRMAKVVTDAGEEIPF
EADGE
>gnl|CDD|184484 PRK14065, PRK14065, exodeoxyribonuclease VII small subunit; Provisional
MQDELFETEKAPQKNTKNAKNAPKKSFEEHVHSLEQAIDRLNDPNLSLKDGMDLYKTAMQELFLAQKLLE
NAYLEYEKLQTPDKKA
>gnl|CDD|172556 PRK14066, PRK14066, exodeoxyribonuclease VII small subunit; Provisional
MAVEKFETALKKLEEVVKKLEGGELSLDDSLKAFEEGVKHAAFCSKKLDEAERRVEVLLKQKDGSFVREP
FRLDD
>gnl|CDD|172557 PRK14067, PRK14067, exodeoxyribonuclease VII small subunit; Provisional
AGRKKTADFEQQLARLQEIVDALEGGDLPLEESVALYKEGLGLARACREQLAKARNEIRLFTEGEVKDFD
PEEDDDGADD
>gnl|CDD|184485 PRK14068, PRK14068, exodeoxyribonuclease VII small subunit; Provisional
MTKETQSFEEMMQELEQIVQKLDNETVSLEESLDLYQRGMKLSAACDTTLKNAEKKVNDLIKEEAEDVKN
DESTDE
>gnl|CDD|172559 PRK14069, PRK14069, exodeoxyribonuclease VII small subunit; Provisional
MVEKKSKISFEDALRELEQIAEKLERQDFSLEESLKAYERGMELKKICSGILDDAEGKIEALTKDESGKT
NKTGFRKESKTKDTSPSKQAEEDLF
>gnl|CDD|184486 PRK14070, PRK14070, exodeoxyribonuclease VII small subunit; Provisional
MKELEEIVNRLENEDLPLEESIKLFERGVELYRKCKEILQQNRLKIIDVMKELEGEIDASGRDQENELR
>gnl|CDD|184487 PRK14071, PRK14071, ATP-dependent 6-phosphofructokinase
MGEKKRIGILTSGGDCAGLNAVIRAVVHRARGTYGWEVIGIRDATQGLMARPPQYIELDLDQVDDLLRMG
GTILGTTNKGDPFAFPMPDGSLRDRSQEIIDGYHSLGLDALIGIGGDGSLAILRRLAQQGGINLVGIPKT
IDNDVGATEVSIGFDTAVNIATEALDRLHFTAASHNRVMILEVMGRDAGHIALAAGIAGGADVILIPEIP
YTLENVCKKIRERQEEGKNFCLVVVSEAVRTEEGEQVTKTQALGEDRYGGIGQYLAEQIAERTGAETRVT
VLGHIQRGGIPSPRDRLLASAFGVAAVDLIAQGKFDRMVAWQNRQVVSVPIAEAIATYRAVDPEGTLVKT
ARGLGIYLGD
>gnl|CDD|237600 PRK14072, PRK14072, diphosphate--fructose-6-phosphate 1-phosphotransferase
MMKGNALYAQSGGPTAVINASAAGVIEEARKHKKIGKVYGARNGIIGILDEDLIDLSKESDEALAALAHT
PSGALGSCRYKLKSLEEDRAEYERLLEVFKAHDIGYFFYNGGNDSMDTALKVSQLAKKMGYPIRCIGIPK
TIDNDLPGTDHCPGFGSAAKYIATSVLEAALDVAAMANTSKVFILEVMGRHAGWLAAAAALAKQNPDDAP
HLIYLPERPFDEEKFLADVRAIVKRYGYCVVVVSEGIRDADGKFIAEAGLAEDAFGHAQLGGVAPVLANL
IKEKLGKKVHWAVLDYLQRAARHIASKTDVEEAYAVGKAAVEYALAGKNGVMPAIRRTSDDPYKWKIGLV
PLSKVANKEKKMPPEFINEDGNGITEAFRRYLRPLIQGEPYPPYKNGLPDYVRLKNVLVPKKLPAF
>gnl|CDD|184489 PRK14075, pnk, NAD(+) kinase
MKLGIFYREEKEKEAKFLKEKISKEHEVVEFCEASASGKVTADLIIVVGGDGTVLKAAKKVGTPLVGFKA
GRLGFLSSYTLEEIDRFLEDLKNWNFREEKRWFLKIESELGNHLALNDVTLERDPSQKMVEIEVSFEDHS
SMWFFADGVVISTPTGSTAYSLSLGGPIILPNCEVFEITPIAPQFLATRSIVIPSNEKVTVESQRDINLI
VDGVLVGKTNRITVKKSRRYVRILRPKDYDFVTVIKEKLGYGRRIL
>gnl|CDD|237601 PRK14076, pnk, bifunctional NADP phosphatase/NAD kinase
MAMDMLKIALKVAKEIEKKIKPLIGWEKAGEVVKIGADGTPTKRIDLIAENIAINSLEKFCSGILISEEI
GFKKIGKNKPEYIFVLDPIDGTYNALKDIPIYSASIAIAKIDGFDKKIKEFIGKNLTINDLEVGVVKNIA
TGDTYYAEKGEGAYLLKKGEKKKIEISNISNLKDASIGLFAYGLSLDTLKFIKDRKVRRIRLFGSIALEM
CYVASGALDAFINVNETTRLCDIAAGYVICKEAGGIITNKNGKPLNMKLDINEKTSVICSNEILHKKLVG
IFGNKWRIKPTKFGIVSRIDNEEAINLALKIIKYLDSKGIPYELESFLYNKLKNRLNEECNLIDDIEEIS
HIISIGGDGTVLRASKLVNGEEIPIICINMGTVGFLTEFSKEEIFKAIDSIISGEYEIEKRTKLSGFILK
DGHQNILPSALNEVVITTKNPAKMLHFEVYVNGELVEEVRADGIIISTPTGSTAYSLSAGGPIVEPTVDG
FIIVPICPFKLSSRPLVVSANSEIKIKLLKKSALVVIDGSIEFEAKKGDEIIFRKSDSYAYFVKGDNFYN
KLKKLSLMG
>gnl|CDD|172567 PRK14077, pnk, NAD(+) kinase
MQNKIDHKNIKKIGLVTRPNVSLDKEILKLQKILSIYKVEILLEKESAEILDLPGYGLDELFKISDFLIS
LGGDGTLISLCRKAAEYDKFVLGIHAGHLGFLTDITVDEAEKFFQAFFQGEFEIEKPYMLSVFLEKKQGK
ILEKLAFNDVVISKNNQASMAHIEAFLNEKYFNEYFGDGVIVATPAGSTAYNMSANGPIIYPLSQVFILT
PVCSHSLTQRPIVLPKGFEVEFKTKSDCILCIDGQDRYKMNDFKSIKVGLSDKNVALIRHKNRDYFQILK
EKLHWGN
>gnl|CDD|184491 PRK14079, recF, recombination protein F; Provisional
MRLLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIYLALTGELPNGRLADLVRFGEGEAWVH
AEVETGGGLSRLEVGLGPGRRELKLDGVRVSLRELARLPGAVLIRPEDLELVLGPPEGRRAYLDRLLSRL
SARYAALLSAYERAVQQRNAALKSGGGWGLHVWDDELVKLGDEIMALRRRALTRLSELAREAYAELGSRK
PLRLELSESTAPEGYLAALEARRAEELARGATVVGPHRDDLVLTLEGRPAHRYASRGEARTVALALRLAE
HRLLWEHFGEAPVLLVDDFTAELDPRRRGALLALAASLPQAIVAGTEAPPGAALTLRIEAGVFTPEAPP
>gnl|CDD|237602 PRK14081, PRK14081, triple tyrosine motif-containing protein; Provisional
MEELNLKFDKESPQEKNSEINIKIINNPNDKLLYKFIIGKNGIWNTIRDFSKEDEINWIPKEEGEYTIMV
QAKKEDSNKPFDYVSKEDYVIGKAEEKLIKNIYLDKDTLNVGEKIEIKVDSNKEPLMYRYWIKEDNNWKL
IKDYSTENSLSYTANKPGKYELLVECKRIDSTKDFDDFKKVKFKVKEIDKVEITDFKCLNKELICDEELV
FEVESVYEEDRTILYKFVKIDSDGKQTCIQDYSTKNIVSYKEKKSGDYKLLCLVKDMYSNNEFDDRAVLV
YTVKPYKDIKIRNFTTDLSSPQLTDTDIELKAVAEGGKELLYRFIIKGKESEDSGYIRNNIYTWKPKIAG
KYSITLWVKDISSKGEYEDKSSIDYTIEEKSKEPIKIEDVILDKGKHILKGEEIKIRVIAEGGTNLRYSF
IIKKDGKEEEKIDYGKNNWVNFIPEEKGNYELEVRVKDKYSDKEYDAHTIVYIKVHEYIPAEIDYILLPV
KEYYLVGDDIEIEVIIQNTKDVLIKYILKINGHKVEETDYIKNKKYKFIPKCSGKYTIEVLAKNIKSTEE
YDSKKEVKFYVREALPITNTKIKTSKKKFKCNEEVTFSVKSEGGKDVCYEFYIMEKGEWKLVQKYSRKNY
YSFMPFNKGKYKVLVLCKSYYKKCAYEDYDIFEFKVE
>gnl|CDD|184493 PRK14082, PRK14082, hypothetical protein; Provisional
MNKEKDDTEEIEHLIENFSPMIKKKLSNTSYQEREDLEQELKIKIIEKADMLLCQEVPGFWEFIT
>gnl|CDD|237603 PRK14083, PRK14083, HSP90 family protein; Provisional
MSHRFQVDLRGVIDLLSRHLYSSPRVYVRELLQNAVDAITARRALDPTAPGRIRIELTDAGGGTLIVEDN
GIGLTEEEVHEFLATIGRSSKRDENLGFARNDFLGQFGIGLLSCFLVADEIVVVSRSAKDGPAVEWRGKA
DGTYSVRKLETERAEPGTTVYLRPRPDAEEWLERETVEELAKKYGSLLPVPIRVEGEKGGVNETPPPWTR
DYPDPETRREALLAYGEELLGFTPLDVIPLDVPSGGLEGVAYVLPYAVSPAARRKHRVYLKRMLLSEEAE
NLLPDWAFFVRCVVNTDELRPTASREALYEDDALAAVREELGEAIRKWLIGLATTDPERLRRLLAVHHLG
VKALASHDDELLRLILPWLPFETTDGRMTLAEIRRRHGVIRYTSSVDEFRQLAPIARAQGMGVINGGYTY
DSELLERLPRLRPGLTVERLDPAELTDRLEPLTPEEELALRPFLAEAREVLAPFGCDVVIRHFEPADLPA
LYLHDRAAQHSREREEAVEEADDLWADILGSLDESQPAPRARLVLNLRNPLVRRLATLGDPKLLSRAVEA
LYVQALLLGHRPLRPAEMALLNRSLLGLLELALDADIRDER
>gnl|CDD|184495 PRK14084, PRK14084, DNA-binding response regulator
MKALIVDDEPLARNELTYLLNEIGGFEEINEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQK
MKEPPAIIFATAHDQFAVKAFELNATDYILKPFEQKRIEQAVNKVRATKAKDDNNASAIANDMSANFDQS
LPIEIDDKIHMLNQQDIIAIGVHNGITTIHTTNHKYETTEPLNRYEKRLNPTYFIRIHRSYIINKKHIKE
VEQWFNYTYQVILTNGVKMQVSRSFMKDFKASIGLL
>gnl|CDD|237605 PRK14086, dnaA, chromosomal replication initiator protein DnaA
MADVQADLAAVWPRVLEQLLGEGDGQSVPAKDEAWLKRCQPLALVADTALLAVPNEFAKEVLEGRLAPII
SETLSRELGRPIRIAITVDPSAGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLP
TARPAYPAYQQRPEPGAWPRAADDYGWQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRD
YDHPRPDWDRPRRDRTDRPEPPPGAGHVHRGGPGPPERDDAPVVPIRPSAPGPLAAQPAPAPGPGEPTAR
LNPKYTFDTFVIGASNRFAHAAAVAVAEAPAKAYNPLFIYGESGLGKTHLLHAIGHYARRLYPGTRVRYV
SSEEFTNEFINSIRDGKGDSFRRRYREMDILLVDDIQFLEDKESTQEEFFHTFNTLHNANKQIVLSSDRP
PKQLVTLEDRLRNRFEWGLITDVQPPELETRIAILRKKAVQEQLNAPPEVLEFIASRISRNIRELEGALI
RVTAFASLNRQPVDLGLTEIVLRDLIPEDSAPEITAAAIMAATADYFGLTVEDLCGTSRSRVLVTARQIA
MYLCRELTDLSLPKIGQQFGRDHTTVMHADRKIRALMAERRSIYNQVTELTNRIKNG
>gnl|CDD|184499 PRK14090, PRK14090, phosphoribosylformylglycinamidine synthase subunit PurL
MRYLNILEEKLGREPTFVELQAFSVMWSEHCGYSHTKKYIRRLPKTGFEGNAGVVNLDDYYSIAFKIESH
NHPSAIEPYNGAATGVGGIIRDVLAMGARPTAIFDSLHMSRIIDGIIEGIADYGNSIGVPTVGGELRISS
LYAHNPLVNVLAAGVVRNDMLVDSKASRPGQVIVIFGGATGRDGIHGASFASEDLTGEKATKLSIQVGDP
FAEKMLIEAFLEMVEEGLVEGAQDLGAGGVLSATSELVAKGGLGAIVHLDRVPLREPDMEPWEILISESQ
ERMAVVTSPEKASRILEIAKKHLLFGDIVAEVIDDPIYRVMYRDDLVMEVPVQLLANAPEEEIVEYTPGE
IPEFKRVEFEEVNAREVFEQYDHMVGTDTVLPPGFGAAVMRIKRDGGYSLVTHSRADLALQDTYWGTFIA
VLESVRKTLSVGAEPLAITNCVNYGDPDVDPVGLSAMMTALKDACEFSGVPVASGNASLYNTYQGKPIPP
TLVVGMLGKVNPQKVAKPKPSKVFAVGWNDFELEREKELWREIRKLSEEGAFILSSSQLLTRTHVETFRE
YGLKIKLKLLEVRPAHQMVLVFSERTPVVDVPVKEIGTLSR
>gnl|CDD|237607 PRK14091, PRK14091, RNA chaperone Hfq
QEANMAEKVNNLQDIFLNSLRKTKTPVTMFLVKGVKLQGIITWFDNFSILLRRDGQSQLVYKHAISTIMP
AHPLDLSRFSKSLDANKKSRLLQDVFLSAVRDSGEPVTMFLVNGVMLQGEIAAFDLFCMLLERDGYVQLV
YKHAVSTVQPAGPVDLTDTEDDEDD
>gnl|CDD|172582 PRK14092, PRK14092, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
MNGSPASALAYVGLGANLGDAAATLRSVLAELAAAPGILACKASRLYRTAPVDAQGPDFVNAVAALDTTL
APLDLLDLLQALEQRHGRERPYRNAPRTLDLDLLLYGEQAIDHPRLSVPHPRMHERAFVLAPLCELAPAL
RLAQGDCAALLAALEDQAIEPLR
>gnl|CDD|184501 PRK14093, PRK14093, UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; Provisional
MSKRPLWTSDAMAEAMGATRSGALPRDVTGISIDSRTLAPGDAYFAIKGDVHDGHAFVAAALKAGAALAV
VERAQRDKFAADAPLLVVDDVLAALRDLGRAARARLEAKVIAVTGSVGKTSTKEALRGVLGAQGETHASV
ASFNNHWGVPLSLARCPADARFAVFEIGMNHAGEIEPLVKMVRPHVAIITTVEPVHLEFFSGIEAIADAK
AEIFTGLEPGGAAVLNRDNPQFDRLAASARAAGIARIVSFGADEKADARLLDVALHADCSAVHADILGHD
VTYKLGMPGRHIAMNSLAVLAAAELAGADLALAALALSQVQPAAGRGVRHTLEVGGGEATLIDESYNANP
ASMAAALGVLGRAPVGPQGRRIAVLGDMLELGPRGPELHRGLAEAIRANAIDLVFCCGPLMRNLWDALSS
GKRGGYAEDAAALESQVVAAIRAGDVIMVKGSLGSRMKTIVTALEKRFPGNAALDDAAV
>gnl|CDD|172584 PRK14094, psbM, photosystem II reaction center protein PsbM
METTNFGFVASLLFVGVPTIFLIGLFISTQDGEKSSFYSDSSKGKLGPKR
>gnl|CDD|237608 PRK14095, pgi, glucose-6-phosphate isomerase; Provisional
MMNYKNFLDLESFKILQELAPEPLDLTLPGVLSEERIKKYSLSGEGFTYNYATERVDDRILAALQNLADE
AELIEKMKAMQNGAVINRIEGFPSENRPVLHTATRGQVGDSVLTDEAEDMAEFSKRELERLAEFLKKVRS
GEIKNSNGKKFTTVVQIGIGGSDLGPKALYLALKNYAKKDKRVHFISNVDPDDAAEVLSEIDLAKTLFIV
VSKSGTTLETAANEEFVRDALKKAGLDYKKHFIAVTSEGSPMDDESGYLEVFHMWDSIGGRFSSTSMVGG
VVLGFAFGFEVFKEFLKGAAAMDKAALNPNIRENLPLLAALIGIWNRNFLGYPTTAVIPYSQALERFPAH
LQQLDMESNGKSVNRFGEPINFKTGPIIWGEPGTNGQHSFFQLLHQGTDIVPVEFIGFKESQLGQDIVIQ
GSTSQQKLFANLIAQIIALACGKENTNPNKNFKGNRPSSLLVAKQLTPYTLGALLAHYENKVMFQGFCWN
INSFDQEGVQLGKVLANQILGIMKGEAPGEFPEADGLLKLFNK
>gnl|CDD|237609 PRK14096, pgi, glucose-6-phosphate isomerase; Provisional
MDALQLWQRYCDWLYYHPELGLWLDISRMNFDDAFLESLEPKFQKAFAAMAALEAGAIANPDEGRMVGHY
WLRNPELAPTPEIRAEITETLAQIEAFAAKVHSGTIKPPNGEKFTDVLWIGIGGSALGPQFVAEALQPNS
DGLNIHFIDNTDPDGIDRVLAELGDRLATTLVVVISKSGGTPETRNGMLEAKAAYEAAGLDFASHAVAIT
MKGSKLDQLAQSEGWLARFPMWDWVGGRTSETSAVGLLPAALQGIDIRAFLAGAKQMDEATRVPDLKNNP
AALLALAWYYAGDGKGKKDMVVLPYKDRLLLFSRYLQQLVMESLGKELDLDGNVVHQGIAVYGNKGSTDQ
HAYVQQLRDGVDNFFVTFIEVLEDRQGSSIEVEPGVTSGDYLSGFLQGTRQALYENGRQSITITIPEVNP
RTLGALIALFERAVGLYASLVNINAYHQPGVEAGKKAAAAILDLQKKVEELLKEDGGELSIEEIAAALGA
PEQVETIYKILRHLAANNRGVVLEGDWSNPASLRISKG
>gnl|CDD|184504 PRK14097, pgi, glucose-6-phosphate isomerase; Provisional
MTHIKFDYSKALSFVGEHELEYLQPQVKAAHQTLHNGTGAGNDFLGWLDLPENYDKEEFARIKKAAEKIK
SDSDVLVVIGIGGSYLGARAAIEFLNHSFYNLLPKEQRKAPQIIFAGNSISSTYLADLLEYLKDKDFSIN
VISKSGTTTEPAIAFRIFKELLEKKYGKEEAKKRIYATTDKAKGALKTLADAEGYETFVIPDDVGGRFSV
LTAVGLLPIAVAGIDIDALMKGAADARKDYSSSDLSENPAYQYAAVRNILYRKGYTTEILVNYEPSLQYF
SEWWKQLFGESEGKDQKGIFPASANFSTDLHSLGQYIQEGRRNLFETVIKVEKPRKDLTIPEDEEDLDGL
NYLAGKTVDFVNKKAFEGTLLAHTDGGVPNIVVNIPELDEYTFGYLVYFFEKACAISGYLLGVNPFDQPG
VEAYKKNMFALLGKPGFEELKAELEARL
>gnl|CDD|172588 PRK14098, PRK14098, starch synthase
MSRRNFKVLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYGTINDRKFRLHDVLRLSDIEV
PLKEKTDLLHVKVTALPSSKIQTYFLYNEKYFKRNGLFTDMSLGGDLKGSAEKVIFFNVGVLETLQRLGW
KPDIIHCHDWYAGLVPLLLKTVYADHEFFKDIKTVLTIHNVYRQGVLPFKVFQKLLPEEVCSGLHREGDE
VNMLYTGVEHADLLTTTSPRYAEEIAGDGEEAFGLDKVLEERKMRLHGILNGIDTRQWNPSTDKLIKKRY
SIERLDGKLENKKALLEEVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYE
KRFQDFAEEHPEQVSVQTEFTDAFFHLAIAGLDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETI
EEVSEDKGSGFIFHDYTPEALVAKLGEALALYHDEERWEELVLEAMERDFSWKNSAEEYAQLYRELLGP
>gnl|CDD|237610 PRK14099, PRK14099, glycogen synthase GlgA
MTPLRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYPAVLAGIEDAEQVHSFPDLFGGP
ARLLAARAGGLDLFVLDAPHLYDRPGNPYVGPDGKDWPDNAQRFAALARAAAAIGQGLVPGFVPDIVHAH
DWQAGLAPAYLHYSGRPAPGTVFTIHNLAFQGQFPRELLGALGLPPSAFSLDGVEYYGGIGYLKAGLQLA
DRITTVSPTYALEIQGPEAGMGLDGLLRQRADRLSGILNGIDTAVWNPATDELIAATYDVETLAARAANK
AALQARFGLDPDPDALLLGVISRLSWQKGLDLLLEALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPG
QIGVVIGYDEALAHLIQAGADALLVPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVDANEMAIATGV
ATGVQFSPVTADALAAALRKTAALFADPVAWRRLQRNGMTTDVSWRNPAQHYAALYRSLVAERRP
>gnl|CDD|184506 PRK14100, PRK14100, 2-phosphosulfolactate phosphatase; Provisional
MRLRVDLLPHENLSYPDVVLVVDVIRATTTAVAFLEAGAEALYLTPTPESALAFRDEDVVLAGERGGLKP
PGFDLGNSPVEALEAQVAGRTVVMSTTNGTKAAHLAARTAKHVLLASLYNAHAAARLARALATEEVAILC
AGKEGRVGLDDVYTAGVLAEYLLALGEFELDDGARIALTTRRAYPDPLEALSLSAAAQALKQVGLEDDVP
FCAQVATSTAVPVLVGRVGEALIFKRG
>gnl|CDD|184507 PRK14101, PRK14101, bifunctional transcriptional regulator/glucokinase
MSTGAQTKAAEASQHADGPRLLADVGGTNARFALETGPGEITQIRVYPGADYPTLTDAIRKYLKDVKIGR
VNHAAIAIANPVDGDQVRMTNHDWSFSIEATRRALGFDTLLVVNDFTALAMALPGLTDAQRVQVGGGTRR
QNSVIGLLGPGTGLGVSGLIPADDRWIALGSEGGHASFAPQDEREDLVLQYARKKYPHVSFERVCAGPGM
EIIYRALAARDKKRVAANVDTAEIVERAHAGDALALEAVECFCAILGTFAGNLALTLGALGGIYIGGGVV
PKLGELFTRSSFRARFEAKGRFEAYLANIPTYLITAEYPAFLGVSAILAEQLSNRTGGASSAVFERIRQM
RDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTGTIPM
SHSQVHLGDTATDFGAKVLDNTVSAILQLREHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKF
FRFGIPTIAYGDLYMQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITSSNTPLAKRAT
VALETDHIEMRESQLSMISRILHLVMIDILAVGVAIRRAAPNAELAEAVARAKARAGDDEAADVLDWLSH
GAAPAAKD
>gnl|CDD|184508 PRK14102, nifW, nitrogenase-stabilizing/protective protein NifW
MTKTLKEFKKLVDAEDYFQFFELPYDPTVVNVNRLHILKQFSQLIAEIDANFPDLSEEEKLEKYQLALEE
AYQVFLTSTPLEQKLFKVFQDKPKNVVLLTELTKD
>gnl|CDD|184509 PRK14103, PRK14103, trans-aconitate 2-methyltransferase; Provisional
MWDPDVYLAFADHRGRPFYDLLARVGAERARRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAAR
ERGVDARTGDVRDWKPKPDTDVVVSNAALQWVPEHADLLVRWVDELAPGSWIAVQVPGNFDAPSHAAVRA
LARREPWAKLLRDIPFRVGAVVQTPAGYAELLTDAGCKVDAWETTYVHQLTGEDPVLDWITGTALRPVRE
RLSDDSWEQFRAELIPLLREAYPPRADGTTFFPFRRVFVVARVGG
>gnl|CDD|172594 PRK14104, PRK14104, chaperonin GroEL; Provisional
MSAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMG
AQMVREVASKSADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTS
NDEIAQVGTISANGDAEIGKFLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADK
MRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPG
FGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKKVMIDKENTTIVNGAGKKADIEARVAQIK
AQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHATRAAVEEGIVPGGGVALL
RASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQYSYGFDSQTGEYGNLV
SKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPAMPPGGGMGGMDF
>gnl|CDD|237611 PRK14105, PRK14105, selenide, water dikinase SelD
KMEEKIKLTEMVKLHGUACKLPSTELENLVKGIILEEDLKHTKVGLGDDAAVIIKNGLAIVKTVDVFTPI
VDDPYIQGKIAACNSTSDVYAMGLSEIIGVLVILGIPPELPIEVAKEMLQGFQDFCRENDTTIIGGHTIL
NPWPLIGGAVTGVGKEEDILTKAGAKEGDVLILTKPLGTQSAMALSRVPEEFEDLIDITKEEKEYIINKA
IELMTTSNRYALLALREAEEEVGEKIANAMTDVTGFGILGHSQEMAEQSNVEIEISTLPVIKGTPELSSL
FGHALLDGYGAETAGGLLISVKPEYKDKLIDKLEKNNVYAFEVGKVVKNGVGKAKLSENVKILEI
>gnl|CDD|184511 PRK14106, murD, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
MELKGKKVLVVGAGVSGLALAKFLKKLGAKVILTDEKEEDQLKEALEELGELGIELVLGEYPEEFLEGVD
LVVVSPGVPLDSPPVVQAHKKGIEVIGEVELAYRFSKAPIVAITGTNGKTTTTTLLGEIFKNAGRKTLVA
GNIGYPLIDAVEEYGEDDIIVAEVSSFQLETIKEFKPKVGCILNITPDHLDRHKTMENYIKAKARIFENQ
RPSDYTVLNYDDPRTRSLAKKAKARVIFFSRKSLLEEGVFVKNGKIVISLGGKEEEVIDIDEIFIPGEHN
LENALAATAAAYLLGISPDVIANTLKTFKGVEHRIEFVAEINGVKFINDSKGTNPDAAIKALEAYETPIV
LIAGGYDKGSDFDEFAKAFKEKVKKLILLGETAQEIAEAARKYGFDNILFAETLEEAVKKAYEIAKPGDV
VLLSPACASWDMFKNFEERGRLFKELVLEL
>gnl|CDD|237612 PRK14108, PRK14108, bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase
SAMMAEADKASLAARFLAALRPLDPEEAKARLADLLADARPEELAALAALLAREPKARDFLSAIAELSPF
LRDLLRADPARLLRLLSADPEARLAALIAEARAAAVAAAPSEAEVMAALRRLKREAALLIALADLGGVFP
VEQTTAWLTDLAEAAVGAALRFLLRDAHAAGKLNLPDRDAPEKGSGLIVLGMGKLGAGELNYSSDIDLIV
FFDETAPILGDPIEAQPFFVRLTRRLVRILQERTGDGYVFRVDLRLRPDPGSTPLAIPVEAALHYYEGRG
QNWERAAMIKARPVAGDLAAGEAFLAELSPFVWRKYLDYAAIADVHSIKRQIHAHKGHGEIAVEGHNVKL
GRGGIREIEFFVQTQQLIAGGRFPELRGRQTLEALAELAERGWITAQARDELTEAYWFLRDVEHRIQMVA
DEQTHLLPEDDEALERFARMMGYEDRASFAEDLLAVLKVVEGHYAALFEQEPELSAELGNLVFTGDPDDP
DTLETLSRLGFERPSDIARVIRTWHAGRYRATQSAEARERLTELTPALLKAFAETRRADEALLRFDRFLQ
GLPAGIQLFSLLQSNPDLLSLLVLIMGAAPRLADIIARRPHVFDGLLDPAFFSELPTRAYLSARLAAFLA
DAGSYEEVLDRLRIFAQEQRFLIGIRILTGTISGQRAGRAFADLAELIIGAALDAVEEEFARAHGRIKGG
RVAILAMGKLGSRELTAGSDVDLILLYDFDDDAPESDGEKPLDGAQYFARFTQRLIAALSAPTAEGVLYE
VDMRLRPSGNKGPVATRIDAFAKYQREEAWTWEHMALTRARVISGDPAFIARIEAIIREVLARPRDIAKI
AGDVAEMRRLIAQEKPPRDIWDLKLAPGGIVDLEFIAQYLQLVHAAKGPDILGVSTAEVLDNLGRLLLDP
ADADILREAARLYTNLSQILRLCVSDKFDPDDAPPGLLDLLCRAGDAPDFSRLEAELKETQKEVRAIFDR
LLKAGA
>gnl|CDD|237613 PRK14109, PRK14109, bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase
MTAPSRRRSSLPSLARLGFTDPDRAAALLAELGLAGVDDDDAHADLLWALSRAADPDLALLALVRLAEAL
EDWAELLAALRADPGLRGRLLAVLGASSALGDHLVAHPEDWRALLRDPVALPSAEELRAALLEAVGADPG
APTPVAGVTGAEAVDALRVAYRRQLLRIAARDLAATDPVLPFPTVAAELADLADAALEAALAVARAEVPG
SAPVRLAVIAMGKCGARELNYVSDVDVIFVAEPAEGVDEAAALAVATRLASELMRICSAPTAEGALWEVD
AALRPEGKDGPLVRTLDSHVAYYERWAKTWEFQALLKARPVAGDAELGQRYVDAVAPMVWSAAEREGFVE
DVQAMRRRVEDLIPAAERDRELKLGPGGLRDVEFAVQLLQLVHGRSDESLRVRSTLDALAALAAGGYVGR
EDAANLAAAYRFLRLLEHRLQLQRLRRTHLLPDDEDELRWLARAAGLRPDGRRDAAEELRAEWRRTRRRV
RRLHEKLFYRPLLEAVARLSAEEARLSPEAARRRLAALGYADPDGALRHIEALTSGVSRRAAIQRTLLPV
LLGWLADGPDPDAGLLAYRRLSEALGTTPWYLRLLRDEGAVAERLAHVLGTSRYVADLLMRAPESVAWLG
DDAKLLPRSREALARELLAAASRHDDPERAVAAARALRRRELLRIASADLLGLLDVEEVCRALSDVWDAV
LEAALRAAIRAVEAEGGDPAPARIAVIGMGRLGGRELGYGSDADVMFVHEPAPGADEAEAVRWATAVAEE
LRRLLGGPSPDPPLEVDADLRPEGRNGPLVRTLASYAAYYARWSQTWEAQALLRARPVAGDAELGERFLA
LIDPLRYPAGGLSEAAVREIRRIKARVEAERLPRGADPARHTKLGRGGLSDVEWTVQLLQLQHAHEVPAL
RTTSTLEALDAAAAAGLLSEEDAELLREAWLLATRARNALVLVRGRPTDQLPGDGRDLAAVARALGYPPG
DGGEFLDDYLRVTRRARAVVERVFYGE
>gnl|CDD|184514 PRK14110, PRK14110, F0F1 ATP synthase subunit gamma; Provisional
MAKLSPRDIKRKIQGIKNTRRITNAMKVVSAAKLRKAQELLYASRPYSEKLYELISDLAAHIDRESHPLL
ERREEKNVDLVIITADRGLAGAFNSNVIKTAERLIQEKQSEGVRVNLILIGRKGVQYFSKRGYNIIKSYE
DVFRKEINFSVVKEVGGILASRYIEEETDAVYLINNEMITRATYKPKVRKFLPFEVEAQEKKLDELSVYN
IEVSEEEFLDKLLQLYLNYQLYRALVESNAAEHFARMVAMDNATRNAGELIRKWTLIFNKARQEAITTEL
IDIVNAAEAMK
>gnl|CDD|184515 PRK14111, PRK14111, F0F1 ATP synthase subunit gamma; Provisional
MPSTREIRRRIRSVKNTAQITRAMEMVSASKMRRAQRNVLATRPYADRIRDVMGDLTARTVGAARVGPLL
EKRPTVKRVALILVTPDRGLAGSLNANVLRRAIRFITDERSMGRTVDVIAIGRKGRDFMVRTGQALVAEF
TRLGDAPKLEAILPVATSAINGFQSGKYDEVYVLYSEFINTLVQRPTIKQLLPIEPPEISTTTVVDYTYE
PSPEEVLRALLPRFVEVQLYQAVLESIASEHSARMVAMRNATDNAKELVRDLTLTYNKARQAAITKEVSE
IASGAAALGS
>gnl|CDD|172602 PRK14112, PRK14112, urease accessory protein UreE; Provisional
MTVFKEILDNIANIKNVESYQIENIHLTSDDVLKRVIIISSDQNVEYGIRLEEDKKLMDGDILYKDDYKL
VVIRLELSDVLIITAHTIGEMAKIAHNLGNRHMPAQFTETQMIVPYDYLVEEYLQDNKALYERKKIKLKE
AFKHCSDAK
>gnl|CDD|237614 PRK14113, PRK14113, urease accessory protein UreE; Provisional
MLDIYERLTHCHDPIYDSITLDHDTRKKGRIKSVTDNGEEIGVFLERGHPLLVGEILKTECGKIIQVKGK
AEDVATASAEDWLAFSKACYHLGNRHTKLQIGERWVRFKPDHVLEDLAENYGLSVNHEPAVFEPESGAYG
VRSHGHSHHHDS
>gnl|CDD|172604 PRK14114, PRK14114, 1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase
MLVVPAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLS
EFAEHIQIGGGIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKFLKEIDVEPVFSLDTRGGKVAFKGWLA
EEEIDPVSLLKRLKEYGLEEIVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISSENSLKTAQRVH
RETNGLLKGVIVGRAFLEGILTVEVMKRYAR
>gnl|CDD|184516 PRK14115, gpmA, 2,3-diphosphoglycerate-dependent phosphoglycerate mutase
TKLVLIRHGESQWNKENRFTGWTDVDLSEKGVSEAKAAGKLLKEEGYTFDVAYTSVLKRAIRTLWIVLDE
LDQMWLPVEKSWRLNERHYGALQGLNKAETAAKYGDEQVKIWRRSYDVPPPALEKDDERYPGHDPRYAKL
PEEELPLTESLKDTIARVLPYWNETIAPQLKSGKRVLIAAHGNSLRALVKYLDNISDEEILELNIPTGVP
LVYELDENLKPIKHYYLGDADEIAAAAAAVANQGKAK
>gnl|CDD|172606 PRK14116, gpmA, 2,3-diphosphoglycerate-dependent phosphoglycerate mutase
MAKLVLIRHGQSEWNLSNQFTGWVDVDLSEKGVEEAKKAGRLIKEAGLEFDQAYTSVLTRAIKTLHYALE
ESDQLWIPETKTWRLNERHYGALQGLNKKETAEKYGDEQVHIWRRSYDVLPPLLDADDEGSAAKDRRYAN
LDPRIIPGGENLKVTLERVIPFWEDHIAPDLLDGKNVIIAAHGNSLRALTKYIENISDEDIMNLEMATGE
PVVYDFDEKLNVVSKEKL
>gnl|CDD|184517 PRK14117, gpmA, phosphoglyceromutase; Provisional
MVKLVFARHGESEWNKANLFTGWADVDLSEKGTQQAIDAGKLIKEAGIEFDLAFTSVLKRAIKTTNLALE
ASDQLWVPVEKSWRLNERHYGGLTGKNKAEAAEQFGDEQVHIWRRSYDVLPPAMAKDDEYSAHTDRRYAS
LDDSVIPDAENLKVTLERALPFWEDKIAPALKDGKNVFVGAHGNSIRALVKHIKGLSDDEIMDVEIPNFP
PLVFEFDEKLNVVKEYYLGK
>gnl|CDD|172608 PRK14118, gpmA, 2,3-diphosphoglycerate-dependent phosphoglycerate mutase
MELVFIRHGFSEWNAKNLFTGWRDVNLTERGVEEAKAAGKKLKEAGYEFDIAFTSVLTRAIKTCNIVLEE
SNQLWIPQVKNWRLNERHYGALQGLDKKATAEQYGDEQVHIWRRSYDTLPPDLDPQDPNSAHNDRRYAHL
PADVVPDAENLKVTLERVLPFWEDQIAPALLSGKRVLVAAHGNSLRALAKHIEGISDADIMDLEIPTGQP
LVYKLDDNLKVVEKFYL
>gnl|CDD|184518 PRK14119, gpmA, phosphoglyceromutase; Provisional
MPKLILCRHGQSEWNAKNLFTGWEDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTTHYILT
ESKQQWIPVYKSWRLNERHYGGLQGLNKDDARKEFGEEQVHIWRRSYDVKPPAETEEQREAYLADRRYNH
LDKRMMPYSESLKDTLVRVIPFWTDHISQYLLDGQTVLVSAHGNSIRALIKYLEDVSDEDIINYEIKTGA
PLVYELTDDLEVIDKYYL
>gnl|CDD|184519 PRK14120, gpmA, phosphoglyceromutase; Provisional
MMMTYTLVLLRHGESEWNAKNLFTGWVDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRTANL
ALDAADRLWIPVRRSWRLNERHYGALQGKDKAETKAEYGEEQFMLWRRSYDTPPPPIEDGSEYSQDNDPR
YADLGVGPRTECLKDVVARFLPYWEDDIVPDLKAGKTVLIAAHGNSLRALVKHLDGISDEDIAGLNIPTG
IPLVYELDEDFKPLNPGGTYLDPEAAAAGAAAVANQGKK
>gnl|CDD|237615 PRK14121, PRK14121, tRNA (guanine-N(7)-)-methyltransferase; Provisional
MPHFLAKKFKELKYPFIKDDVEFLWEAKSLKHPNESLIYVSFKDEEFLLQIKKKKNGFLIKGDKATRPSK
VGILKKALKIFSELFCADIISHNLAENSKKLSLKKPYILDIDNFLDFISKNQEKILIEIGFGSGRHLLYQ
AKNNPNKLFIGIEIHTPSIEQVLKQIELLNLKNLLIINYDARLLLELLPSNSVEKIFVHFPVPWDKKPHR
RVISEDFLNEALRVLKPGGTLELRTDSELYFEFSLELFLKLPKAKIEIKKNAQLEVSSKYEDRWKKQNKD
IYDLRIYNLEESEEPDLNGDFSFSFVTNLKKIEKNFKNKKIIKDDFFVHFENIYEIDDGLLLKVSFGDFD
RPEHCYLLIENNKISYLFKSPLKTKENIKAHKLLKEILSQ
>gnl|CDD|184523 PRK14125, PRK14125, cell division suppressor protein YneA; Provisional
LKLKESKIHVSIFFVLTALVLLIFVYATVPVDKNQYVEITVQEGDTLWALADQYAGKHHMAKNEFIEWVE
DVNNLPSGHIKAGDKLVIPVLKSKSDSYILAAV
>gnl|CDD|172616 PRK14126, PRK14126, cell division protein ZapA; Provisional
MQKGKKTRINVEIYGQQYTIVGDESTSHIRMVAAIVDDKMRELNEKNPSLDTSKLAVLTAVNVIHDYIKL
KEEYEKLKESMTKKG
>gnl|CDD|237616 PRK14127, PRK14127, cell division regulator GpsB
MASIKLTPKDILEKEFKTSMRGYDQDEVDKFLDDVIKDYEAFQKEIEELQQENARLKAQVDELTKQVSVG
ASSSSVATTQPSSSATNYDILKRLSNLEKHVFGSQLYED
>gnl|CDD|184525 PRK14128, iraD, anti-adapter protein IraD
HNVSDKRLQSWYCRQLRSALLFHEPRIAALQVNLKEAYCHTLAISLEAMLYHDDEPLTFDLVWDNGGWR
>gnl|CDD|184526 PRK14129, PRK14129, heat shock protein HspQ; Provisional
MIASKFGIGQQVRHSLLGYLGVVVDIDPEYSLEEPSPDELAVNDELRAAPWYHVVMEDDDGQPVHTYLAE
AQLSSELQDEHPEQPSMDELAESIRKQLQAPRLRN
>gnl|CDD|237617 PRK14131, PRK14131, N-acetylneuraminate epimerase
TLTTLALLLAAASSFAANAEQLPDLPVPFKNGTGAIDNNTVYVGLGSAGTSWYKLDLNAPSKGWTKIAAF
PGGPREQAVAAFIDGKLYVFGGIGKTNSEGSPQVFDDVYKYDPKTNSWQKLDTRSPVGLAGHVAVSLHNG
KAYITGGVNKNIFDGYFEDLAAAGKDKTPKDKINDAYFDKKPEDYFFNKEVLSYDPSTNQWKNAGESPFL
GTAGSAVVIKGNKLWLINGEIKPGLRTDAVKQGKFTGNNLKWQKLPDLPPAPGGSSQEGVAGAFAGYSNG
VLLVAGGANFPGARENYQNGKLYAHEGLKKSWSDEIYALVNGKWQKVGELPQGLAYGVSVSWNNGVLLIG
GETAGGKAVSDVTLLSWDGKKLTVEN
>gnl|CDD|237618 PRK14132, PRK14132, riboflavin kinase; Provisional
MKIFGRVVSGLGEGAYFLSLPPYKEKFKEKLGFTPYEGTLNIKLGENFNIDIFNYIETEDFEINGKKFFG
VKVLPIAILNKGKEIDGAIVFPKKTDHSKNVLEIIAPIKLRKFLNLKDGDVVKIVI
>gnl|CDD|184529 PRK14133, PRK14133, DNA polymerase IV; Provisional
MDRVIIHVDMDAFFASVEQMDNPKLKGKPVIVGGISERGVVSTCSYEARKYGVHSAMPVFMAKKRCPHGI
FLPVRHERYKEVSKNIFKILYEVTPIVEPVSIDEAYLDITNIKEEPIKIAKYIKKKVKKETGLTLSVGIS
YNKFLAKLASDWNKPDGIKIITEDMIPDILKPLPISKVHGIGKKSVEKLNNIGIYTIEDLLKLSREFLIE
YFGKFGVEIYERIRGIDYREVEVSRERKSIGKETTLKKDTKDKEELKKYLKDFSNIISEELKKRNLYGKT
VTVKIKTSDFQTHTKSKTLNDYIRDKEEIYNVACEILEHINIKEPIRLIGLSVSNLSENKIEQLSFL
>gnl|CDD|184530 PRK14134, recX, recombination regulator RecX; Provisional
MSNIITKIEVQKRNKDRVNVYIDEEFAFACSAELVYYHNLKKGKVIDVNSLNDIIKEDNYIKCKGYALKY
IEKSYKTEKQIKEKLYLKEYDEDAVNRVIRFLKEYNFIDDDKYCDMYIREKINSYGRNKIKYTLLNKGIK
ENIIIEKINNIDEEKEKKVAYKLAEKKYKILILSEKNKFKIYKKLGPYLISRGYSSNIAEWILNELIKNE
ALYKDNNSQNIENNIKDENIEELHNLARKRYDIIIKSEDDKNKIYRRLSNYLLRRGYSWEEVKKSLNELL
YER
>gnl|CDD|237619 PRK14135, recX, recombination regulator RecX; Provisional
ITKITVQKKNKERYNIFLDEKYAFSVDEDTLVKFMLKKGKELDEEDLEEIQYADQVSKGKNLALYYLSYQ
MRTEKEVRDYLKKHEISEEIISEVIDKLKEEKYIDDKEYAESYVRTNINTGDKGPRVIKQKLLQKGIEDE
IIEEALSEYTEEDQIEVAQKLAEKLLKKYQKLPFKALKQKIIQSLLTKGFSYEVIKAALEELDLEQDEEE
EQELLQKELEKAYRKYSKYDGYELKQKLKQALYRKGFSYDDIDSFLREYGIED
>gnl|CDD|237620 PRK14136, recX, recombination regulator RecX; Provisional
MRRRRQGADPQEADHPARAARAGRPHASRETDRTVSGEGRPAGRTATRASDDALVSFEIAAPDEPFDDDE
SFDAHDRARRRVSGVGVRDAGAPGGRAADARAANLSSAAKRAEAAGDVYTRTSQHPRRTRRAAGPFHSDS
SPSASSEDDGAARSRASSRPARSLKGRALGYLSRREYSRAELARKLAPYADESDSVEPLLDALEREGWLS
DARFAESLVHRRASRVGSARIVSELKRHAVGDALVESVGAQLRETEFERAQAVWRKKFGALPQTPAERAK
QARFLAARGFSSATIVKLLKVGDDEFGDD
>gnl|CDD|172626 PRK14137, recX, recombination regulator RecX; Provisional
MYRARRRASTPGEGEAPGTDTEGPVRPERRTPPTPDEAREALLAYAFRALAARAMTAAELRAKLERRSED
EALVTEVLERVQELGYQDDAQVARAENSRRGVGALRVRQTLRRRGVEETLIEETLAARDPQEEQQEARNL
LERRWSSFARKRDPRASAYAFLARRGFSGAVIWPAIREVAALAGLDVSDVPEDES
>gnl|CDD|172627 PRK14138, PRK14138, NAD-dependent deacetylase; Provisional
MKEFLELLNESRLTVTLTGAGISTPSGIPDFRGPQGIYKKYPQNVFDIDFFYSHPEEFYRFAKEGIFPML
EAKPNLAHVLLAKLEEKGLIEAVITQNIDRLHQKAGSKKVIELHGNVEEYYCVRCGKRYTVEDVIEKLEK
SDVPRCDDCSGLIRPNIVFFGEALPQDALREAIRLSSKASLMIVMGSSLVVYPAAELPLITVRSGGKLVI
VNLGETPLDDIATLKYNMDVVEFANRVMSEGGIS
>gnl|CDD|237621 PRK14139, PRK14139, heat shock protein GrpE; Provisional
MENTQQNPSEQEAEEAGAAAQAAAAAAAAAEDAAPALEAELAEAEAKAAELQDSFLRAKAETENVRRRAQ
EDVAKAHKFAIESFAESLLPVKDSLEAALADESGDLEKLREGVELTLKQLTSAFEKGRVVEINPVGEKFD
PHQHQAISMVPAEQEPNTVVAVLQKGYTIADRVLRPALVTVAAPK
>gnl|CDD|237622 PRK14140, PRK14140, heat shock protein GrpE; Provisional
MEEKNEQVEEEVEETEVEEAVEDEVEEETVEEESEAELLDEEQAKIAELEAKLDELEERYLRLQADFENY
KRRIQKENEAAEKYRAQSLASDLLPALDNFERALQIEADDEQTKSLLKGVEMVHRQLLEALKKEGVEVIE
AVGEQFDPNLHQAVMQDEDEDFESNEVVEELQKGYKLKDRVIRPSMVKVNQ
>gnl|CDD|172630 PRK14141, PRK14141, heat shock protein GrpE; Provisional
MTDEKNKNGNPADAARDANNPVDREAKPYEMEDDPEPDPLEALKAENAELKDRMLRLAAEMENLRKRTQR
DVADARAYGIAGFARDMLSVSDNLRRALDAIPAEARAAADAGLKALIEGVEMTERAMLNALERHGVKKLD
PEGQKFDPNFHQAMFEVPNPDVPNNTVVQVVQAGYTIGERVLRPAMVGVAKGGPKAAAEAGASTSEDDA
>gnl|CDD|237623 PRK14142, PRK14142, heat shock protein GrpE; Provisional
KPDGNSGEQVTVTDKRRIDPETGEVRHVPPGDMPGGTAAADAAHTEDKVAELTADLQRVQADFANYRKRA
LRDQQAAADRAKASVVSQLLGVLDDLERARKHGDLESGPLKSVADKLDSALTGLGLVAFGAEGEDFDPVL
HEAVQHEGDGGQGSKPVIGTVMRQGYQLGEQVLRHALVGVVDTVVVDAAELESVDDGTAVADTAENDQAD
QGNSADTSGEQAE
>gnl|CDD|237624 PRK14143, PRK14143, heat shock protein GrpE; Provisional
STPEQDPLEVKLAVISESEAEDNSPESSEEVTEQEAELTNPEGDAAEAESSPDSGSAASETAADNAARLA
QLEQELESLKQELEELNSQYMRIAADFDNFRKRTSREQEDLRLQLKCNTLSEILPVVDNFERARQQLKPE
GEEAQALHRSYQGLYKQLVDVLKRLGVSPMRVVGQEFDPNLHEAVLREPSDEHPEDVVLEELQRGYHLGG
RVLRHAMVKVSMGPGPSSPAEEDQATPA
>gnl|CDD|184535 PRK14144, PRK14144, heat shock protein GrpE; Provisional
MSKQNKKDWKKFKDEHKEEHKVENEILEEETDEESQHQEPALGHPSYTALEEQLTLAEQKAHENWEKSVR
ALAELENVRRRMEREVANAHKYGVEKLISALLPVVDSLEQALQLADKNSDPSMHEGLELTMKLFLDALQK
FDVEQIDPLGQTFDPQQHEAMSMQPAPGAPPNSVITVFQKGYKLSDRVIRPARVIVSTK
>gnl|CDD|184536 PRK14145, PRK14145, heat shock protein GrpE; Provisional
MEEVEKEINKEEEKDVNNLSSNEQMEGPPEDEQAQQNQPQQQTVDEIEELKQKLQQKEVEAQEYLDIAQR
LKAEFENYRKRTEKEKSEMVEYGKEQVILELLPVMDNFERALASSGDYNSLKEGIELIYRQFKKILDKFG
VKEIEAEGQIFDPYKHHAVMQEEVEGKQPNEIIEVFQKGYYLKDKVIRPSLVKVAK
>gnl|CDD|172635 PRK14146, PRK14146, heat shock protein GrpE; Provisional
MAETSNNKTSEEAKANEKKSQSQTLEESKLENMNSEESQTITEETQEQAVEGAETETSLQKELDNAKKEI
ESLKDSWARERAEFQNFKRRSAQEFVSIRKEAVKSLVSGFLNPIDNLERVGATQNQSEELKPFVEGVKMI
LKEFYSVLEKSNVIRFDPKGEPFDPMSMEALSSEEGDQYSEETVIDVYQAGYYYKENEDKFTLRPARVRI
GKPKS
>gnl|CDD|237625 PRK14147, PRK14147, heat shock protein GrpE; Provisional
MNQDHPEFDSEDLAQNPPETDPLKAEVESLRSEIALVKADALRERADLENQRKRIARDVEQARKFANEKL
LGELLPVFDSLDAGLTAAGTEPSPLRDGLELTYKQLLKVAADNGLTLLDPVGQPFNPEHHQAISQGEAEG
VAPGHVVQVFQKGYLLNERLLRPALVVVAKQD
>gnl|CDD|172637 PRK14148, PRK14148, heat shock protein GrpE; Provisional
MSKQEKSNVEDKSLDIETAAQVETAQESASGALEELSVEEQLERAKDTIKELEDSCDQFKDEALRAKAEM
ENIRKRAERDVSNARKFGIEKFAKELLPVIDSIEQALKHEVKLEEAIAMKEGIELTAKMLVDILKKNGVE
ELDPKGEKFDPNLHEAMAMIPNPEFEDNTIFDVFQKGYMLNGRIVRAAKVVIVKN
>gnl|CDD|184538 PRK14149, PRK14149, heat shock protein GrpE; Provisional
MKDEHNQEHDHLSQKEPESEEKACACKEQQGEEKQEASEKEGEIKEDFELKYKEMHEKYLRVHADFENVK
KRLERDKSMALEYAYEKIALDLLPVIDALLGALKSAAEVDKESALTKGLELTMEKLHEVLARHGIEGIEC
LEEFDPNFHNAIMQVKSEEKENGKIVQVLQQGYKYKGRVLRPAMVSIAKND
>gnl|CDD|184539 PRK14150, PRK14150, heat shock protein GrpE; Provisional
MSNEEQKTPQEQVSEEIEAEVEQQEEADEAELEDELDEADARIAELEAQLAEAQAEERDSVLRARAEVEN
IRRRAEQDVEKAHKFALEKFANELLPVIDNLERALQAADKENEALKALIEGVELTLKSLLDTVAKFGVEV
VGPVGEPFNPEVHQAISMQESEDHEPNTVMMVMQKGYTLNGRLLRPAMVMVSK
>gnl|CDD|172640 PRK14151, PRK14151, heat shock protein GrpE; Provisional
MADEQTLDLQAPEAAQAEAAAGDDLTARVQELEEQLAAAKDQSLRAAADLQNVRRRAEQDVEKAHKFALE
KFAGDLLPVVDSLERGLELSSADDEAIKPMREGVELTLKMFQDTLKRYQLEAVDPHGEPFNPEHHQAMAM
QESADVEPNSVLKVFQKGYLLNGRLLRPAMVVVSKA
>gnl|CDD|184540 PRK14153, PRK14153, heat shock protein GrpE; Provisional
MTSKEVGKDKAENSEARNSGSSAEEAEELKEEPEDSTADSETEKCREEIESLKEQLFRLAAEFDNFRKRT
AREMEENRKFVLEQVLLDLLEVTDNFERALESARTAEDMNSIVEGIEMVSKQFFSILEKYGLERIECEGE
EFDPHRHEAMMHVETSEVPDNTIVDVCKPGYALNSKVIRPAMVSVARNPDEEEK
>gnl|CDD|237626 PRK14154, PRK14154, heat shock protein GrpE; Provisional
MGGCMSSKNNPESETKAKNKWEKVMEAEEEQEEGGGDGSQEMEPHREGLEFPSREKLEGQLTRMERKVDE
YKTQYLRAQAEMDNLRKRIEREKADIIKFGSKQLITDLLPVADSLIHGLESPASEDPQVKSMRDGMSLTL
DLLHNTLAKHGVQVINPNPGDPFDPALHEAMSVQAVPDAKPDTIIQVLQKGYQLNGRVLRAARVIVAG
>gnl|CDD|237627 PRK14155, PRK14155, heat shock protein GrpE; Provisional
MTDEQTPAEDGPFEADDAAQEIEALKAEVAALKDQALRYAAEAENTKRRAEREMNDARAYAIQKFARDLL
GAADNLGRATAASPKDSADPAVKNFIIGVEMTEKELLGAFERNGLKKIDPAKGDKFDPHLHQAMMEQPST
EVAAGGVLQVMQAGYELMGRLVRPAMVAVAAKGSTGPAAPAEPAAGANPYASAAADGDGSGGSFDTKA
>gnl|CDD|237628 PRK14156, PRK14156, heat shock protein GrpE; Provisional
MSEEIKNEEVEEEVEATETEETVEEVVEETPEKSELELANERADEFENKYLRAHAEMQNIQRRANEERQQ
LQRYRSQDLAKAILPSLDNLERALAVEGLTDDVKKGLEMVQESLIQALKEEGVEEVAVDSFDHNLHMAVQ
TLPADDEHPADSIAQVFQKGYKLHERLLRPAMVVVYN
>gnl|CDD|184543 PRK14157, PRK14157, heat shock protein GrpE; Provisional
MSDFNKDDYLNDLPDADDLEAQGQAAQASSGADASAESGEQQDSAAQADANAGADAAPAAAEGEAKAAAE
KTGEAQSDSDDTLTPLGQAKKEAAEYLEALQRERAEFINYRNRTQKEQDRFRQHGIIDVLTALLPALDDI
DRIREHSEMDDSFKAVAAKIDKAFEKFGVEKFGEKGEDFDPTKHDAILHKPDPDAEKETVDTVVEAGYRI
GDRVIRAARVVVASPQN
>gnl|CDD|172646 PRK14158, PRK14158, heat shock protein GrpE; Provisional
MDKKKHGSHQIAEALKAKAAKEAEAAQGKPEAAQPVAAADRIKELEEALAAKEAEAAANWDKYLRERADL
ENYRKRVQKEKEELLKYGNESLILEILPAVDNMERALDHADEESMSAIIEGIRMTLSMLLSTLKKFGVTP
VEAEKGTPFDPAYHQAMCQVESAEQEPNTVVAVFQKGYLLNERLLRPAMVSVAT
>gnl|CDD|172647 PRK14159, PRK14159, heat shock protein GrpE; Provisional
MSEQKQEFENENAENSEHLQDENLQNIEDVEQNKLQKDYDELKDKYMRANAEFENIKKRMEKEKLSAMAY
ANESFAKDLLDVLDALEAAVNVECHDEISLKIKEGVQNTLDLFLKKLEKHGVALIKEEKEFDPNLHEAMF
HVDSENHQSGEVVQVLQKGYKIADRVIRPTKVSVAK
>gnl|CDD|237629 PRK14160, PRK14160, heat shock protein GrpE; Provisional
MEKECKDAKHENMEEDCCKENENKEEDKGKEEDLEFEEIEKEEIIEDSEESNEVKIEELKDENNKLKEEN
KKLENELEALKDRLLRTVAEYDNYRKRTAKEKEGIYSDACEDVLKELLPVLDNLERAAAVEGSVEDLKKG
IEMTVKQFKTSLEKLGVEEISTEGEFDPNLHNAVMHVEDENYGENEIVEVFQKGYKRGDKVIRYSMVKVA
N
>gnl|CDD|237630 PRK14161, PRK14161, heat shock protein GrpE; Provisional
MIDDNIENNEQTINDIAEEIVETANPEITALKAEIEELKDKLIRTTAEIDNTRKRLEKARDEAKDYAIAT
FAKELLNVSDNLSRALAHKPANSDVEVTNIIAGVQMTKDELDKVFHKHHIEEIKPEIGSMFDYNLHNAIS
QIEHPDHAPNSIITLMQSGYKIRDRLLRPATVQVVKKP
>gnl|CDD|237631 PRK14162, PRK14162, heat shock protein GrpE; Provisional
MSKEEFPSEKDLPQEETTDEAPKKEAKEAPKEEDQEKQNPVEDLEKEIADLKAKNKDLEDKYLRSQAEIQ
NMQNRYAKERAQLIKYESQSLAKDVLPAMDNLERALAVKADDEAAKQLKKGVQMTLDHLVKALKDHGVTE
IKADGEKFDPTLHQAVQTVAAENDDQKDHVVQVLQKGYQYKDRTLRPAMVVVAQ
>gnl|CDD|184546 PRK14163, PRK14163, heat shock protein GrpE; Provisional
MTEETPGFEEKPDVPSGATPDDAEPKAASEEGAAPAGDAAATAGLTAQLDQVRTALGERTADLQRLQAEY
QNYRRRVERDRVTVKEIAVANLLSELLPVLDDVGRAREHGELVGGFKSVAESLETTVAKLGLQQFGKEGE
PFDPTIHEALMHSYAPDVTETTCVAILQPGYRIGERTIRPARVAVAEPQPGAQTAKAKEAEGADDKESGG
PEEG
>gnl|CDD|237632 PRK14164, PRK14164, heat shock protein GrpE; Provisional
MTTSNGMPDNPGDPENTDPEATSADRAEAAAEEAALAQGVPEDDPFGDAVEGEIDPDLEADLEDLLDDVD
PELADDGEASTVEAQLAERTEDLQRVTAEYANYRRRTERERQAIIETAKAGVATDLLPILDDLDLAEQHG
DLNEGPLKAFSDKLTNVLAGLKVEKFGEEGDAFDPEIHEAVQDLSSGDEKVLGTVLRKGYRMGDRVLRTA
MVIIADPA
>gnl|CDD|184548 PRK14165, PRK14165, winged helix-turn-helix domain-containing protein/riboflavin kinase; Provisional
MPDIEALKKLALLGAVNNTVKISSSEFANHTGTSSKTAARILKQLEDEGYITRTIVPRGQLITITEKGLD
VLYNEYADYSRIFSIKDNLELEGNVVKGLGEGKYYINIKGYKIQFEEKLGFIPYPGTLNVKLDNSSSPLL
RKLRESPGIRIEGFTDGERTFGGVKCYPVKVEGIECAVIVPERTHYPSDLIEIISPVYLRKELNLKDGDR
VEVLVKK
>gnl|CDD|172654 PRK14166, PRK14166, bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
MTLLDGKALSAKIKEELKEKNQFLKSKGIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNEN
TTQNELLALINTLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESGFLPCT
PLGVMKLLKAYEIDLEGKDAVIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGC
VNLLRSDMVKEGVIVVDVGINRLESGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNR
LN
>gnl|CDD|184549 PRK14167, PRK14167, bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
MTEIIDGNAVAAQIRDDLTDAIETLEDAGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDP
DAPAEELYDTIDELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCT
PHGIQKLLAAAGVDTEGADVVVVGRSDIVGKPMANLLIQKADGGNATVTVCHSRTDDLAAKTRRADIVVA
AAGVPELIDGSMLSEGATVIDVGINRVDADTEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLY
NTVKAASLQEGVDVDLP
>gnl|CDD|237633 PRK14168, PRK14168, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MSAKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQ
SVDITEEELLALIDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKF
LPCTPAGIQEMLVRSGVETSGAEVVVVGRSNIVGKPIANMMTQKGPGANATVTIVHTRSKNLARHCQRAD
ILIVAAGVPNLVKPEWIKPGATVIDVGVNRVGTNESTGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTI
AMLMRNTLKSAKFHLSL
>gnl|CDD|184550 PRK14169, PRK14169, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
ATRLDGRAVSKKILADLKQTVAKLAQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEA
TTQADLLAKVAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTP
YGIMALLDAYDIDVAGKRVVIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVP
HFIGADAVKPGAVVIDVGISRGADGKLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKRRA
NG
>gnl|CDD|172658 PRK14170, PRK14170, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MGEIIDGKKLAKEIQEKVTREVAELVKEGKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPE
NVTEEKLLSVVEELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCT
PAGIIELIKSTGTQIEGKRAVVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGL
AKFVKKDYIKPGAIVIDVGMDRDENNKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKRI
WKMN
>gnl|CDD|172659 PRK14171, PRK14171, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MNNIIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLS
TTIHTNDLISKINELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISQGFIP
CTALGCLAVIKKYEPNLTGKNVVIIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAI
GSPLKLTAEYFNPESIVIDVGINRISGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFK
DSLYTLDT
>gnl|CDD|172660 PRK14172, PRK14172, bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
MGQIINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLD
ESISEEDLINEIEELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPC
TPNSVITLIKSLNIDIEGKEVVVIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIG
RPKFIDEEYVKEGAIVIDVGTSSVNGKITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKNVCEALK
>gnl|CDD|184551 PRK14173, PRK14173, bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
MAARELSGPPAAEAVYAELRARLAKLPFVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPEST
SQEELLELIARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPA
GVVRLLKHYGIPLAGKEVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPH
LITPEMVRPGAVVVDVGINRVGGNGGRDILTGDVHPEVAEVAGALTPVPGGVGPMTVAMLMANTVIAALR
RRGGRAG
>gnl|CDD|172662 PRK14174, PRK14174, bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
MLIIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPA
DTTEEHLLKKIEDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDKCFVS
CTPYGILELLGRYNIETKGKHCVVVGRSNIVGKPMANLMLQKLKESNCTVTICHSATKDIPSYTRQADIL
IAAIGKARFITADMVKPGAVVIDVGINRIEDPSTKSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAM
LLKNTLQSFERVNNL
>gnl|CDD|184552 PRK14175, PRK14175, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MVAKILDGKQIAKDYRQGLQDQVEALKEKGFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLE
ETATEEEVLNELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPC
TPLGIMEILKHADIDLEGKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVG
KPGLVTKDVVKEGAVIIDVGNTPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKM
RRGIDS
>gnl|CDD|184553 PRK14176, PRK14176, bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
MMDESYESRIIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRA
EDQFLPADTTQEELLELIDSLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGD
EGLVPCTPHGVIRALEEYGVDIEGKNAVIVGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADI
LVVATGVKHLIKADMVKEGAVIFDVGITKEEDKVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVL
MCAEKSL
>gnl|CDD|172665 PRK14177, PRK14177, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MSPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRL
KEQTTTEELLGVIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLP
CTPYGMVLLLKEYGIDVTGKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAV
GKPEFIKADWISEGAVLLDAGYNPGNVGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKEHFT
PPVE
>gnl|CDD|172666 PRK14178, PRK14178, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MILDGKAVSEKRLELLKEEIIESGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTR
TVLERIRRLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIM
TLLHEYKISIAGKRAVVVGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFIT
PDMVKPGATVIDVGINQVNGKLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAKMRCCHFM
>gnl|CDD|237634 PRK14179, PRK14179, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase
MTEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLP
ETISQEELLDLIERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPC
TPAGIMEMFREYNVELEGKHAVVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIG
RGHFVTKEFVKEGAVVIDVGMNRDENGKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALR
SLHK
>gnl|CDD|172668 PRK14180, PRK14180, bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
MILIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPE
HTTESELLELIDQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLRDKKCLESC
TPKGIMTMLREYGIKTEGAYAVVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVG
KPNFITADMVKEGAVVIDVGINHVDGKIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQEL
NR
>gnl|CDD|172669 PRK14181, PRK14181, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MLLKGAPAAEHILATIKENISASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLS
DILKLIHRLNNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGETDGFIPCTPAGI
IELLKYYEIPLHGRHVAIVGRSNIVGKPLAALLMQKHPDTNATVTLLHSQSENLTEILKTADIIIAAIGV
PLFIKEEMIAEKAVIVDVGTSRVPAANPKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWE
SYLRHSS
>gnl|CDD|172670 PRK14182, PRK14182, bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
MNLIDGKQIAAKVKGEVATEVRALAARGVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPAT
TTQAELLALIARLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVPRPCT
PAGVMRMLDEARVDPKGKRALVVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGK
AELVKGAWVKEGAVVIDVGMNRLADGKLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRT
AR
>gnl|CDD|184555 PRK14183, PRK14183, bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
MQILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPS
TISQKEILETIAMMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCT
PLGVMELLEEYEIDVKGKDVCVVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGK
PNLITEDMVKEGAIVIDIGINRTEDGRLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNR
A
>gnl|CDD|237635 PRK14184, PRK14184, bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
MLLLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPA
DTTQEELEDLIAELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCT
PAGVMTLLERYGLSPAGKKAVVVGRSNIVGKPLALMLGAPGKFANATVTVCHSRTPDLAEECREADFLFV
AIGRPRFVTADMVKPGAVVVDVGINRTDDGLVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSW
KERVGL
>gnl|CDD|184556 PRK14185, PRK14185, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MQLIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYES
DVTEEELLAKVRELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSAT
PNGILELLKRYHIETSGKKCVVLGRSNIVGKPMAQLMMQKAYPGDCTVTVCHSRSKNLKKECLEADIIIA
ALGQPEFVKADMVKEGAVVIDVGTTRVPDATRKSGFKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLM
KNTLLAGKKAIYK
>gnl|CDD|237636 PRK14186, PRK14186, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLP
ADTSQAEVEALIAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSC
TPAGVMRLLRSQQIDIAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAG
RPNLIGAEMVKPGAVVVDVGIHRLPSSDGKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVL
SWQKRHGLSSTLNDLLP
>gnl|CDD|172675 PRK14187, PRK14187, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
ETNIIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLP
STISESSLIEKINELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNCLI
PCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAA
VGIPNFVKYSWIKKGAIVIDVGINSIEEGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTV
IAACNQKGIDDFVE
>gnl|CDD|184558 PRK14188, PRK14188, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLP
ADTSQAELLALIARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPC
TPLGCMMLLRRVHGDLSGLNAVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVG
RPEMVKGDWIKPGATVIDVGINRIPAPEKGEGKTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLAN
TLTAACRAAGLPKPKF
>gnl|CDD|184559 PRK14189, PRK14189, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase
MTAQLIDGNALSKQLRAEAAQRAAALTARGHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYP
ADLSEAELLARIDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPC
TPYGVMKMLESIGIPLRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVG
KRNVLTADMVKPGATVIDVGMNRDDAGKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER
AAAAA
>gnl|CDD|184560 PRK14190, PRK14190, bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
MMAVIIDGKEVAKEKREQLKEEVVKLKEQGIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFP
ADITEEELLALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPC
TPHGILELLKEYNIDISGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVG
KPKLITADMVKEGAVVIDVGVNRLENGKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR
AGGR
>gnl|CDD|172679 PRK14191, PRK14191, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MVLLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQE
NTTEAELLSLIKDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPAT
PMGVMRLLKHYHIEIKGKDVVIIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGK
PDLIKASMVKKGAVVVDIGINRLNDGRLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKR
QRKGF
>gnl|CDD|184561 PRK14192, PRK14192, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
MMALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVEL
PQETTTEQLLAKIEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGS
ATPAGIMRLLKAYNIELAGKHAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAV
GKPELIKKDWIKQGAVVVDAGFHPRDGGGVGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEK
ALG
>gnl|CDD|237637 PRK14193, PRK14193, bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
MTAIILDGKATADEIKADLAERVAALKEKGITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLP
ADATQEELNAVIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPC
TPRGIVHLLRRYDVELAGAHVVVIGRGVTVGRPIGLLLTRRSENATVTLCHTGTRDLAAHTRRADIIVAA
AGVAHLVTADMVKPGAAVLDVGVSRAGDGKLVGDVHPDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAE
RRAG
>gnl|CDD|172682 PRK14194, PRK14194, bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD
LMSAKLIDGKAAAARVLAQVREDVRTLKAAGIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRL
PADTSQARLLALIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTP
CTPSGCLRLLEDTCGDLTGKHAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAV
GRPRLIDADWLKPGAVVIDVGINRIDDDGRSRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVT
AARLQAHAQRSQSEAVCLSIY
>gnl|CDD|184563 PRK14195, PRK14195, fluoride efflux transporter CrcB
MINILLVAAGGALGSVARYLVGVGALRLMGPAFPWGTLAVNVTGSFLIGVLAGLLAHRWNASQEWRLFLI
VGVLGGFTTFSAFSLDAALLIERGAYGAAAAYIAASVVLSVAALFAGLAIARALF
>gnl|CDD|184564 PRK14196, PRK14196, fluoride efflux transporter CrcB
MLQSLLAVFIGAGLGALLRWLLGLRLNPLFPALPLGTLAANLIGGYIIGVAVAWFARMPGLDPEWRLLII
TGFCGGLTTFSTFSAEVVTLLQEGRFGWALLNVALHLLGSLAMTALGFWTFSALAAH
>gnl|CDD|172685 PRK14197, PRK14197, fluoride efflux transporter CrcB
MNNVLFVALGGSIGAVLRYLISIFMIQVFGSSFPFGTLLVNVLGSFLMGVIYALGQMSHVSPELKALIGV
GLLGALTTFSTFSNETLLLMQEGAWLKAALNVVLNLSLCLFMVYLGQQLVFSRI
>gnl|CDD|172686 PRK14198, PRK14198, fluoride efflux transporter CrcB
MNYLLVFVGGGLGASLRHAVNMASARLLGTSFPYGTFIINVSGSLVMGLIAGYLAFKGGAPQHWRLFLMT
GILGGYTTFSAFSLDAALLYERGALGLAALYVLGSVALGIAGLFAGLALIRHFT
>gnl|CDD|172687 PRK14199, PRK14199, fluoride efflux transporter CrcB
MEKLILAIIVGLGGFIGASLRYLISIFAAKMFNGNFPYGTLIVNIVGALLIGFIMEFSMDTALISSNMKL
FLTTGIMGGLTTFSTFSYETINLITNGNILLGIENIILNLGLSLLGVVIGQKLARILF
>gnl|CDD|237638 PRK14200, PRK14200, fluoride efflux transporter CrcB
MGQFAILGFIALGGAFGACSRYLVSELCVVLLGRGFPYGTLTVNVVGSFIMGLLIAAFENELLATEPWRQ
IIGLGFLGALTTFSTFSMDNVLLMQQGAFFKMGLNVLLNVVLSISAAWIGFQLLMKS
>gnl|CDD|184566 PRK14201, PRK14201, fluoride efflux transporter CrcB
MQYVYIFIGGALGALLRYLLSFLNTDGGFPIGTLIANLTGAFLMGLLTALTIAFFSNHPTLKKAITTGFL
GALTTFSTFQFELIHMFDHQQFITLLLYAVTSYIFGILLCYVGIKLGGGLS
>gnl|CDD|172690 PRK14202, PRK14202, fluoride efflux transporter CrcB
MMEQFSAVLLVGAGGFLGSVARYLVALALSFIGTGFPFATFTVNLLGSFLIGFISELALSTTLVSPEARL
LLVTGFCGGFTTFSSYMYEIAALLRDGELFYASLYLAGSLVGGFVALYSGTLLAKLWS
>gnl|CDD|237639 PRK14203, PRK14203, fluoride efflux transporter CrcB
MLDVLTGLIWVALGSVLGGPARFFLSGLVARRIGETFPWGTLTVNVSGAFAIGIFGALAASGHGLFALPA
PWLFAVTGFLGCYTTVSSFSLQTLTLARDGEFLRALGNVAFSLILCLIAVAIGFAAATGLLS
>gnl|CDD|172692 PRK14204, PRK14204, fluoride efflux transporter CrcB
MNFVFLWAALGGAIGSSLRYFVGKMMPSKFLMFESFPLGTFSVNIIGCFVIGFMGHLAAKKVFGDDFGIF
FVTGVLGGFTTFSSYGLDTLKLLQKSQYIEAISYVLGTNLLGLIGVAIGWFLAKNFV
>gnl|CDD|172693 PRK14205, PRK14205, fluoride efflux transporter CrcB
MIEALLVATGGFFGAITRFAISNWFKKRNKTSFPIATFLINITGAFLLGYIIGNGVTTGWQLLLGTGFMG
AFTTFSTFKLESVQLLNRKNFSTFLLYLSATYIVGILFAFLGMKLGGI
>gnl|CDD|172694 PRK14206, PRK14206, fluoride efflux transporter CrcB
MTYLWIALGSALGGTLRFWLSGLVAEATGGTFPWGTLVINVSGSFLIGFFATLTGPEGRVFVGESWRLFV
MVGVCGGFTTFSSFSLQTLNLARDGDWLRAGGNVVLSVVFCLLAVWLGHVAAVAINQ
>gnl|CDD|172695 PRK14207, PRK14207, fluoride efflux transporter CrcB
MNAKIALAVAIGGGLGALARYYISGLLPVYKDFPVGTLLVNSIASFILGYLYGLLFWGFDVSPEWRAFLG
TGFCGGLSTFSTFSYETFSLLREREYLLALLNISANVLITISLVFLGFILARR
>gnl|CDD|172696 PRK14208, PRK14208, fluoride efflux transporter CrcB
MARLLLVCLGGALGSGARYLTSAWALRAFGPDFPRGTLLVNVSGSFLLAGIMTASLQSEAVPPDLRLFLA
AGVMGGFTTYSSFNYETLALLEQGRLAAAAAYLLATVLGCLAAAFAATLLVRWLAG
>gnl|CDD|237640 PRK14209, PRK14209, fluoride efflux transporter CrcB
MISSLLQVALGGALGASARYLTNVGSMRLFGPAFPVGTMIVNVVGSFLMGVLVVVLAHKGNRYAPFLMTG
MLGGFTTFSAFSLDAVTLYERGQAGLAAAYVGLSVGLSLAGLMAGMAAVRGWMA
>gnl|CDD|172698 PRK14210, PRK14210, fluoride efflux transporter CrcB
MKEIIYIFIGGGMGSVTRYLTQIAVNERLSPALFPFPWGTFAVNIIGSLLIGFFYSFSERFNLSFELRLF
LTVGFCGGFTTFSTLANDSLSLLKGGFYGIFTFYVFISILLGLLAVLAGGYLGEQFK
>gnl|CDD|172699 PRK14211, PRK14211, fluoride efflux transporter CrcB
MTVLLVALGGALGATTRYLTGRYVDSYRSFPVATFLVNVAGCLILGLLSGASLSTQTFALLGTGFCGGLT
TYSTFAVESVGLLRIRQALLSVVYIVASVAAGLAAAWLGFRLTS
>gnl|CDD|184569 PRK14212, PRK14212, fluoride efflux transporter CrcB
MGEILLLAAGGALGAVSRYGLNNLTVKLLGDSFPYGTLIVNCLGCFVLGFLMQWGFSSDSHNTHLKLMLT
AGFLGAFTTFSTFSYETLDCFKAGDYFNGFSNILANVLLGLLMVFIGAYLGSLLKQNS
>gnl|CDD|184570 PRK14213, PRK14213, camphor resistance protein CrcB; Provisional
MTLAGIFIAGGIGAVLRFWLGNVITAKTKGLSLPIGIMTVNILGSFGLGIFTGLGVDNASVSIIIGTGFF
GAFTTFSTFSVEAVQLLMAKRVKESILYIALTLAGSLLAFWCGWTIIP
>gnl|CDD|184571 PRK14214, PRK14214, fluoride efflux transporter CrcB
MLVNFLLVGFGAALGAMLRYGISVLVKSKWKTNFPYATFFINITGSFLLGFLVSSALGPVWQLFLGTGFM
GGYTTFSTFKVESMELKWKTNYRVLFSYLGCTYVFGLIAAFLGMMLGV
>gnl|CDD|172703 PRK14215, PRK14215, fluoride efflux transporter CrcB
MNNILAIAVGAAIGANLRYGIGLWAAQRWGTSWPYGTFIINLLGCLLIGLLLTLATTRLTLSEPARLMLV
TGLLGGFTTFSTFGYESYSLLSSGNWLAAGGYVVGSVGGGLIAVIIGAGLGRWLGG
>gnl|CDD|184572 PRK14216, PRK14216, fluoride efflux transporter CrcB
MPRHDYRELAAVFAGGALGTLARAALSELAAPDPARWPWPTFTVNVVGAFLLGYFTTRLLERLPLSSYRR
PLLGTGLCGGLTTFSTMQVETIRMIEHGHWGLAAGYTAASIAAGLLAVHLATVLVRRVRIRR
>gnl|CDD|172705 PRK14217, PRK14217, fluoride efflux transporter CrcB
MVVAPYLAVAIGGSLGAMSRYLVTIMAQNAWGIKFPYGTLLVNTLGSFLAGFFLIVLVGRFSAEESFRLF
LFTGFLGAFTTFSSFAAESLFMFEQGYWFKLITNILVNNVGSLSMVFIGTLVAKYVLLGHQGSN
>gnl|CDD|184573 PRK14218, PRK14218, fluoride efflux transporter CrcB
MNAVVWWQSLLLVMLGGAFGSGLRFVIGSCLLQRFGAGFPWGTLAVNLIGSFVAGFLLIWLDKRGSAGWP
WRMLLIVGLIGGLTTFSSLMMECLVFVRSDRSLMVGIYLCITLLFGLLFVFLGARLGAFVCDD
>gnl|CDD|172707 PRK14219, PRK14219, fluoride efflux transporter CrcB
LIYIIVGIAGILGALSRYYLGLTIHEFWHHTFPLATLLINLAGCFLLAWLTTYIAKLNILPSDVITGIGT
GFIGSFTTFSTFSVETIQLINHSEWSIAFLYVSCSILGGLIMSGLGYTLGDFLLKKHLTEGD
>gnl|CDD|237641 PRK14220, PRK14220, fluoride efflux transporter CrcB
MTILLAGFGASIGAMLRYAITNYGKKHWEQFSNLPTPTLLINLTGAFILGLIFGRKFNPFIYALLGTGVL
GGYTTFSTLNTELVSLYKSKNYRVLKLYALLSYLGGLILVFCGYYLGSLL
>gnl|CDD|184575 PRK14221, PRK14221, fluoride efflux transporter CrcB
MKKEQFYPLGIFLAAMLGGLVRYLVSTWLPASPDFPWGTLFVNYLGIFCLIYLVKGYLVYKGTSKGLILA
LGTGFCGGLTTFSSLMLDTVKLLDTGRYLSLILYLLLSIGGGLLLAYYLGRKKW
>gnl|CDD|172710 PRK14222, PRK14222, fluoride efflux transporter CrcB
METLVYIALFGALGCLARYYLSGWVYALFGRAFPYGTLAVNVIGAFLIGLIMEFSLRSTLIPPTLRIGLT
IGFLGGLTTFSTFSYETFRLLEDGELLIASVNVLASVVVCLVCTWLGIMTARAL
>gnl|CDD|184576 PRK14223, PRK14223, fluoride efflux transporter CrcB
MRELLLIGIGGFFGAILRYLISGIIPVKFGIPTGTLIVNLIGSFILGFLLYSSLFGSISPEYRLFIITGF
CGALTTFSTFSYETFSLLEEGLYIKALLNILLNVFGCLIMIYFGRVLSLFIF
>gnl|CDD|237642 PRK14224, PRK14224, fluoride efflux transporter CrcB
MPSTYKDIDKLFLIGAGGFLGAICRFLICELIEGQLGTLSVNVLGSFMLGMIMYDTEYIGFIGPKGRLAF
GTGFLGAFTTFSTFAVQSFSMPFVPALGNISANLFLTLTGVFFGRSLIKALSGREI
>gnl|CDD|172713 PRK14225, PRK14225, fluoride efflux transporter CrcB
MRNWRQAENIRLYIAVGCGAAIGALLRFLSGWVIVAILGANPLWGTSFVNIVGSFIIMFFATLTGPEGRW
LVSPAWRQFVMGGLCGGLTTFSSMSLDTFLLVLHGNAAFALAYLCGLVFLSLSAAMLGLIAAQRINR
>gnl|CDD|172714 PRK14226, PRK14226, fluoride efflux transporter CrcB
MGLLLLLVGIGGGFGAMARFALTQATASISKQIPLGILLCNIIGSLIIGMMAAFLIETKLFNEDVSTYVR
FLLVTGFLGGFTTFSSFSLDILNLLQRGEIFIAIGYIMVSVLASLIAVILGFYIVMGVYK
>gnl|CDD|172715 PRK14227, PRK14227, fluoride efflux transporter CrcB
MMKYIVVAIGGSIGAILRYFTGVYSAKNLGLDFPYGTLIVNSVGSFILSFFMILFLEKLSLDPLWRLFVA
VGFCGSFTTFSSFTYETIALFQDGDYTKAMLNIILNNVLSITSAFSGIVLARVL
>gnl|CDD|237643 PRK14228, PRK14228, fluoride efflux transporter CrcB
MLTVLVWIGVMLIGGIGSVLRFLVDRTVARRLARTFPYGTLAVNVSGAALLGFLAGLALPKDAALLAGTA
FVGAYTTFSTWMLETQRLGEERQMRSALANIVVSVVLGLAAALLGQWLAQLL
>gnl|CDD|172717 PRK14229, PRK14229, fluoride efflux transporter CrcB
VIVYLAIACGLGALVRYFFSRYNQASKLPLGTLIANLLGCFLIGVFYNHVESKEVYAILATGFCGGLTTF
STLNDELQRLLSDKKVFYSYLTLTYIGGLVAIFLGILL
>gnl|CDD|172718 PRK14230, PRK14230, camphor resistance protein CrcB; Provisional
MLSNIIPLSIGAALGATARWLLNLAVPASLSPATGNLFANWTGALLIGIFAETVNHPQWKLLLITGFLGS
LTTLSGFSLETVTLLQSNRPASALANIFLHTAGSLLLTWLGLKIGTAVK
>gnl|CDD|184579 PRK14231, PRK14231, fluoride efflux transporter CrcB
MYFLYVGVFGALGGMCRYAMNLWLGGGDFPSATLAVNLIGCFLLAFLMQFLAEKSRISLVILNGIGTGFI
GAFTTFSAFSVDTIQLVQSGAWLLAVSYVLASFIGGLIMVKFGRMLSNKLLNRGEHRVS
>gnl|CDD|237644 PRK14232, PRK14232, fluoride efflux transporter CrcB
MNFVFVGIGGAFGSLARYQLGKVISKKSKSTFPVGTFIINITGAILLGIVSSSNISKNMYLLLGDGFLGA
YTTFSTFMYEGFNLFQEKEKLNAFIYILGSLIIGIIGYILGFWIGNLIKI
>gnl|CDD|172721 PRK14233, PRK14233, fluoride efflux transporter CrcB
MSVEASILVLVGGFIGGVMRFFLSGYVGRRIGETFPWGTFVVNVSGAFVIGTAAGLGARLGGIFSTTIFH
EFIMVGLLGGYTTVSSFCLQSVNLMLDGEQRQALFNIVASALLCVLAVAAGYGGIMWIMEWPG
>gnl|CDD|172722 PRK14234, PRK14234, fluoride efflux transporter CrcB
MIRLILAVSAGGIAGTLLRFATGNWVSANWPRHFYAATLAVNIVGCLLIGLLYGLFLLRPEVPIELRAGL
IVGFLGGLTTFSSFSLDTLRLLESGQVPLALGYAGISVFGGLLATWAGLSLTRL
>gnl|CDD|184585 PRK14239, PRK14239, phosphate transporter ATP-binding protein; Provisional
MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYN
GHNIYSPRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKD
RLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQA
SRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYISGKFG
>gnl|CDD|184588 PRK14243, PRK14243, phosphate transporter ATP-binding protein; Provisional
TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEG
KVTFHGKNLYAPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARINGYKGDMDELVERSLRQAALWDE
VKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM
QQAARVSDMTAFFNVELTEGGGRYGYLVEFDRTEKIFNSPQQQATRDYVSGRFG
>gnl|CDD|172734 PRK14246, PRK14246, phosphate ABC transporter ATP-binding protein; Provisional
MEAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVD
GKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLW
KEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSH
NPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVIGRIS
>gnl|CDD|172735 PRK14247, PRK14247, phosphate ABC transporter ATP-binding protein; Provisional
MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQ
DIFKMDVIELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRL
DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAAR
ISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYVTGRLY
>gnl|CDD|184593 PRK14258, PRK14258, phosphate ABC transporter ATP-binding protein; Provisional
MSKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVE
FFNQNIYERRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEI
KHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN
LHQVSRLSDFTAFFKGNENRIGQLVEFGLTKKIFNSPHDSRTREYVLSRLG
>gnl|CDD|184596 PRK14267, PRK14267, phosphate ABC transporter ATP-binding protein; Provisional
MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFG
RNIYSPDVDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVK
DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQ
AARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGALG
>gnl|CDD|172759 PRK14271, PRK14271, phosphate ABC transporter ATP-binding protein; Provisional
MACERLGGQSGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRM
NDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVA
QARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA
DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSGDVKDAKRGN
>gnl|CDD|237653 PRK14276, PRK14276, chaperone protein DnaJ; Provisional
MNNTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYDQYGA
AGANGGFGGGAGGFGGFDGSGGFGGFEDIFSSFFGGGGARRNPNAPRQGDDLQYRVNLDFEEAIFGKEKE
VSYNREATCHTCNGSGAKPGTSPVTCGKCHGSGVITVDTQTPLGMMRRQVTCDVCHGTGKEIKEPCQTCH
GTGHEKQAHTVSVKIPAGVETGQQIRLQGQGEAGFNGGPYGDLYVVFRVEPSKKFERDGSTIYYTLPISF
VQAALGDTVEVPTVHGDVELKIPAGTQTGKKFRLRGKGAPKLRGGGNGDQHVTVNIVTPTKLNDAQKEAL
KAFAKASGEKDVNPKKKGFFDKVKDAFEDE
>gnl|CDD|184599 PRK14277, PRK14277, chaperone protein DnaJ; Provisional
MAAKKDYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQF
GHAAFDPGGFGQGGFGQGGFGGGGFDFDFGGFGDIFEDIFGDFFGTGRRRAETGPQKGADIRYDLELTFE
EAAFGTEKEIEVERFEKCDVCKGSGAKPGSKPVTCPVCHGTGQVRTRQNTPFGRIVNIRTCDRCHGEGKI
ITDPCNKCGGTGRIRRRRKIKVNIPAGIDDGQMITLRGEGEPGIKGGPNGDLYIVIKVKPHPLFKREGYN
VYLEMPITFTDAALGGEIEIPTLDGKVKFTIPEGTQTGTKFRLRGKGIPHLRGRGRGDQIVKVYIEVPKK
LTEKQKELLREFEKLSGEEGTESRKSFFQRMKDAFG
>gnl|CDD|237654 PRK14278, PRK14278, chaperone protein DnaJ; Provisional
MARDYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVDLGGDP
LESAGGGGGGFGGGFGGLGDVFEAFFGGGAASRGPRGRVRPGSDSLLRMRLDLEECATGVTKQVTVDTAV
LCDRCHGKGTAGDSKPVTCDTCGGRGEVQTVQRSFLGQVMTSRPCPTCRGVGEVIPDPCHECAGDGRVRA
RREITVKIPAGVGDGMRIRLAAQGEVGPGGGPAGDLYVEVHEQPHDVFVRDGDDLHCTVSVPMVDAALGT
TVTVEAILDGPSEITIPPGTQPGSVITLRGRGMPHLRSGGRGDLHAHVEVVVPTRLDHEDIELLRELKAL
RGREVAEVRSTHAQGGLFSRLRETFTGR
>gnl|CDD|237655 PRK14279, PRK14279, molecular chaperone DnaJ
MAQREWVEKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKE
YDETRRLFAGGGFGGRRFDGGGGFGGFGTGGDGAEFNLNDLFDAAGRGGGGGIGDLFGGLFNRGGGSARP
SRPRRGNDLETETTLDFVEAAKGVTMPLRLTSPAPCTTCHGSGARPGTSPKVCPTCNGSGVISRNQGAFG
FSEPCTDCRGTGSIIEDPCEECKGTGVTTRTRTINVRIPPGVEDGQRIRLAGQGEAGLRGAPSGDLYVTV
HVRPDKVFGRDGDDLTVTVPVSFTELALGSTLSVPTLDGPVGVKVPAGTADGRILRVRGRGVPKRSGGAG
DLLVTVKVAVPPNLDGAAAEALEAYAEAERASGFDPRAGWAG
>gnl|CDD|237656 PRK14280, PRK14280, molecular chaperone DnaJ
MAKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYDQFGH
AGPNQGFGGGGFGGGDFGGGFGFEDIFSSFFGGGGRRRDPNAPRQGADLQYTMTLTFEEAVFGKEKEIEI
PKEETCDTCHGSGAKPGTSKETCSHCGGSGQVSVEQNTPFGRVVNRQTCPHCNGTGQEIKEKCPTCHGKG
KVRKRKKINVKIPAGVDNGQQIRVSGEGEPGVNGGPAGDLYVVFRVRPHEFFERDGDDIYCEMPLTFAQA
ALGDEIEVPTLHGKVKLKIPAGTQTGTQFRLKGKGVPNVRGYGQGDQYVVVRVVTPTKLTDRQKELLREF
AELSGEEIDEQPSSFFDKAKRAFKGE
>gnl|CDD|237657 PRK14281, PRK14281, chaperone protein DnaJ; Provisional
MKRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQFGH
AGVGSSAASGGGPGYGGGGGDFNDIFSAFNDMFGGGARRGGGSPFGFEDVFGGGGRRRRASAGIPGTDLK
IRLKLTLEEIAKGVEKTLKIKKQVPCKECNGTGSKTGATETCPTCHGSGEVRQASKTMFGQFVNITACPT
CGGEGRVVKDRCPACYGEGIKQGEVTVKVTVPAGVQDGNYLTLRGQGNAGPRGGAPGDLIVVIEEKPHEL
FVRNGDDVIYNLAVSYPDLVLGTKVEVPTLDGAVKLTIPAGTQPETMLRIPGKGIGHLRGSGRGDQYVRV
NVFVPKEVSHQDKELLKELKKSSHISPNAHNDKEEKSFFEKAKDIFS
>gnl|CDD|184603 PRK14282, PRK14282, chaperone protein DnaJ; Provisional
REKKDYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQKRAMYDRF
GYVGEQPPYQETESGGGFFEDIFKDFENIFNRDIFDIFFGERRTQEEQREYARRGEDIRYEIEVTLSDLI
NGAEIPVEYDRYETCPHCGGTGVEPGSGYVTCPKCHGTGRIREERRSFFGVFVSERTCERCGGTGKIPGE
YCHECGGSGRIRRRVRTTVKIPAGVEDGTVLRITGGGNAGYYGGPYGDLYVIVRVRPDPRFKRSGSDLIY
DVTIDYLQAILGTTVEVPLPEGGTTMLKIPPGTQPETVFRLKGKGLPNMRYGRRGDLIVNVHVEIPKRLS
REERKLLKELAKKRGVTIG
>gnl|CDD|184604 PRK14283, PRK14283, chaperone protein DnaJ; Provisional
MAEKRDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYDQFG
HAGMDGFSQEDIFNNINFEDIFQGFGFGIGNIFDMFGFGGGSRHGPQRGADIYTEVEITLEEAASGVEKD
IKVRHTKKCPVCNGSRAEPGSEVKTCPTCGGTGQVKQVRNTILGQMMNVTTCPDCQGEGKIVEKPCSNCH
GKGVVRETKTISVKIPAGVETGSRLRVSGEGEMGDRGGEPGDLYVVIKVKPHKIFRREGANLYYEKPISF
VQAALGDTVDVPTIDGPVELKIPAGTQSGTTFRLKGHGMPSLRWSGKGNLYVKVKVVVPKKLSPKQKELL
REFASISGDEIHHVKKGLFDKVKDAINH
>gnl|CDD|237658 PRK14284, PRK14284, chaperone protein DnaJ; Provisional
MDYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYDRYGKDG
PFAGAGGFGGAGMGNMEDALRTFMGAFGGEFGGGGSFFEGLFGGLGEAFGMRGGPAGARQGASKKVHITL
SFEEAAKGVEKELLVSGYKSCDACSGSGANSSQGIKVCDRCKGSGQVVQSRGFFSMASTCPECGGEGRVI
TDPCSVCRGQGRIKDKRSVHVHIPAGVDSGMRLKMEGYGDAGQNGAPAGDLYVFIDVEPHPVFERRGDDL
ILELPIGFVDAALGMKKEIPTLLKEGTCRLTIPEGIQSGTILKVRGQGFPNVHGKGRGDLLVRISVETPQ
NLSEEQKELLRQFAATEKAENFPKKRSFLDKIKGFFSDFAV
>gnl|CDD|172773 PRK14285, PRK14285, chaperone protein DnaJ; Provisional
MKRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYDRFGH
TAFEGGGGFEGFSGGFSGFSDIFEDFGDIFDSFFTGNRGQDKNRKHEKGQDLTYQIEISLEDAYLGYKNN
INITRNMLCESCLGKKSEKGTSPSICNMCNGSGRVMQGGGFFRVTTTCPKCYGNGKIISNPCKSCKGKGS
LKKKETIELKIPAGIDDNQQIKMRGKGSVNPDNQQYGDLYIKILIKPHKIFKRNGKDLYATLPISFTQAA
LGKEIKIQTIASKKIKIKIPKGTENDEQIIIKNEGMPILHTEKFGNLILIIKIKTPKNLNSNAIKLLENL
SKELKDIDEITLNKI
>gnl|CDD|172774 PRK14286, PRK14286, chaperone protein DnaJ; Provisional
MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFG
KAGVNAGAGGFGQGAYTDFSDIFGDFGDIFGDFFGGGRGGGSGGGRRSGPQRGSDLRYNLEVSLEDAALG
REYKIEIPRLESCVDCNGSGASKGSSPTTCPDCGGSGQIRRTQGFFSVATTCPTCRGKGTVISNPCKTCG
GQGLQEKRRTINIKIPPGVETGSRLKVSGEGEAGPNGGPHGDLYVVTHIKKHELFERQGNDLILVRKISL
AQAILGAEIEVPTIDGKKAKMKIPEGTESGQVFRLKGHGMPYLGAYGKGDQHVIVKIEIPKKITRRQREL
IEEFARESGENIPGSKGKIFTK
>gnl|CDD|237659 PRK14287, PRK14287, chaperone protein DnaJ; Provisional
MSKRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGH
TDPNQGFGGGGAGDFGGFSDIFDMFFGGGGGRRNPNAPRQGADLQYTMTLEFKEAVFGKETEIEIPREET
CGTCHGSGAKPGTKPETCSHCGGSGQLNVEQNTPFGRVVNRRVCHHCEGTGKIIKQKCATCGGKGKVRKR
KKINVKVPAGIDHGQQLRVSGQGEAGVNGGPPGDLYVVFNVKPHEFFERDGDDIYCEMPLTFPQVALGDE
IEVPTLNGKVKLKIPAGTQTGTSFRLRGKGVPNVHGRGQGDQHVQVRVVTPKNLTEKEKELMREFAGMSG
GRPDEQNDGFFAKVKRAFKGD
>gnl|CDD|172776 PRK14288, PRK14288, molecular chaperone DnaJ
MELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYGK
KGLNQAGASQSDFSDFFEDLGSFFEDAFGFGARGSKRQKSSIAPDYLQTIELSFKEAVFGCKKTIKVQYQ
SVCESCDGTGAKDKALETCKQCNGQGQVFMRQGFMSFAQTCGACQGKGKIIKTPCQACKGKTYILKDEEI
DAIIPEGIDDQNRMVLKNKGNEYEKGKRGDLYLEARVKEDEHFKREGCDLFIEAPVFFTTIALGHTIKVP
SLKGDELELKIPRNARDRQTFAFRNEGVKHPESSYRGSLIVELQVIYPKSLNKEQQELLEKLHASFGYEG
EPHKSVLETCISKIKDWFK
>gnl|CDD|237660 PRK14289, PRK14289, molecular chaperone DnaJ
MAEKRDYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQF
GHAGVGGAAGGGGFSGEGMSMEDIFSMFGDIFGGHGGGFGGFGGFGGGGSQQRVFRGSDLRVKVKLNLKE
ISTGVEKKFKVKKYVPCSHCHGTGAEGNNGSETCPTCKGSGSVTRVQNTILGTMQTQSTCPTCNGEGKII
KKKCKKCGGEGIVYGEEVITVKIPAGVAEGMQLSMNGKGNAGKHGGVNGDLLVVIEEEPHPELIRDENDL
IYNLLLSVPTAALGGAVEVPTIDGKAKVKIEAGTQPGKVLRLRNKGLPSVNGYGTGDLLVNVSVYIPETL
SKEEKQTLEKMENSDNFKPTTSIKEKIFKKFKSFFD
>gnl|CDD|172778 PRK14290, PRK14290, chaperone protein DnaJ; Provisional
MAKDYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAEEKFKEISEAYEVLSDPQKRRQYDQTG
TVDFGAGGSNFNWDNFTHFSDINDIFNQIFGGNFGSDFFSGFGNQQSTRNIDLDIYTNLDISLEDAYYGT
EKRIKYRRNAMCPDCSGTGAKNGKLITCPTCHGTGQQRIVRGQGFFRMVTVTTCRTCGGRGRIPEEKCPR
CNGTGTVVVNEDISVKIPKGATDNLRLRVKGKGQSYGGRTGDLYVVLRVNNDPNIQRINDDLYVDQKINF
PQAALGGEIEIKLFREKYNLKIPEGTQPGEVLKIKGAGMPHLNGHGSGDLLVRINVEVPKRLTSKQKELI
REFFDIKENHKSWFH
>gnl|CDD|237661 PRK14291, PRK14291, chaperone protein DnaJ; Provisional
AKKDYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQFGHA
AFSGSGQQQQGQEGFSDFGGGNIEDILEDVFDIFGFGDIFGRRRATRERRKTYQRPVKGEDIYQTVEISL
EEAYTGTTVSLEVPRYVPCEACGGTGYDPGSGEKVCPTCGGSGEIYQRGGFFRISQTCPTCGGEGVLREP
CSKCNGRGLVIKKETIKVRIPPGVDNGSKLRVPGKGHAGRFGGPPGDLYIIVKVKPHPLFERRGDNLYLD
VNITVAEAVLGTELEVPLLDGKKEKVKIPPGTKEGDKIRVPGKGMPRLKGSGYGDLVVRVHIDVPKISML
SKLMGDGKKAKKLLKELDKLLPEPERIVEKEE
>gnl|CDD|237662 PRK14292, PRK14292, chaperone protein DnaJ; Provisional
MMDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYDRFGTAP
GAGMPGGDPFGGMGFDPMDIFEQLFGGAGFGGGRGRRGPARGDDLETEARITLEQARAGEEVEVEVDRLT
ECEHCHGSRTEPGGKPPKTCPTCRGAGAVRAQARTIFGVVETQQPCPTCRGEGQIITDPCTVCRGRGRTL
KAETVKVKLPRGIDEGYRIRVAGMGNEGPGGNGDLYVHIEMEPHPELRREQEHLIYEARIGFAKAALGGQ
ITVPTLDGPQVIEVKPGTQHGDLHRLRGQGMPRLQGAGTGDLIVEYEIAVPKQLSPEAREALEAYARAVG
DEVPEPHEGLFDKVGKLFRRP
>gnl|CDD|237663 PRK14293, PRK14293, molecular chaperone DnaJ
MAADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYDQFGEA
GVSGAAGFPDMGDMGGFADIFETFFSGFGGAGGQGGRRRRRGPQRGDDLRYDLKLDFREAIFGGEKEIRI
PHLETCETCRGSGAKPGTGPTTCSTCGGAGQVRRATRTPFGSFTQVSECPTCNGTGQVIEDPCDACGGQG
VKQVTKKLKINIPAGVDTGTRLRVSGEGDAGLRGGPPGDLYVYLFVKNDPEFRRDGINILSEIKISYLQA
ILGDTLEVDTVDGPVELTIPAGTQPNTVLTLENKGVPRLGNPVARGDHLITVKVKIPTRISDEERELLEK
LAKIKGERQGKGGIEGFFGGLFGK
>gnl|CDD|237664 PRK14294, PRK14294, chaperone protein DnaJ; Provisional
MVKRDYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYDQYG
HEGLSGTGFSGFSGFDDIFSSFGDIFEDFFGFGGGRRGRSRTAVRAGADLRYDLTLPFLEAAFGTEKEIR
IQKLETCEECHGSGCEPGTSPTTCPQCGGSGQVTQSQGFFSIRTTCPRCRGMGKVIVSPCKTCHGQGRVR
VSKTVQVKIPAGVDTGSRLRLRGEGEAGVRGGPPGDLYVFLTVEPHEFFERDGNDVHCKVPISFVQAALG
AQIEVPTLEGERELKIPKGTQPGDIFRFKGKGIPSLRGGGRGDQIIEVEVKVPTRLTKKQEELLTEFARL
ESEKIGNKLRNLFKSK
>gnl|CDD|237665 PRK14295, PRK14295, molecular chaperone DnaJ
MSTKDYIEKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKE
YDEARSLFGNGGFRPGPGGGGGGGFNFDLGDLFGGGAQGGGGAGGGGGLGDVFGGLFNRGGRRTQPRRGA
DVESEVTLSFTEAIDGATVPLRLTSQAPCPACSGTGAKNGTTPRVCPTCSGTGQVSRNSGGFSLSEPCPD
CKGRGLIADDPCLVCKGSGRAKSSRTMQVRIPAGVSDGQRIRLRGKGAPGERGGPAGDLYVVVHVDPHPV
FGRSGDNLTVTVPVTFPEAALGAEVRVPTLGGPPVTVKLPPGTPNGRVLRVRGKGAVRKDGTRGDLLVTV
EVAVPKDLSGKAREALEAFREATADEDPRAELFQAAKGA
>gnl|CDD|237666 PRK14296, PRK14296, chaperone protein DnaJ; Provisional
MKKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYDQFGH
AAFDGSSGFSSNFGDFEDLFSNMGSSGFSSFTNIFSDFFGSNKSDYQRSTKGQSVSLDIYLTFKELLFGV
DKIIELDLLTNCSKCFGSGAESNSDIHICNNCHGTGEVLVQKNMGFFQFQQSAKCNVCNGAGKIIKNKCK
NCKGKGKYLERKKIEVNIPKGIRPNQQIKLSQKGHASLNNGVNGDLIIDIYLKESKVFEIINNNDILMTY
NISYLDAILGNEIIIKTLDGDIKYKLPKSINSNELIIINNKGLYKSINKDKRGDLIIKVNIVVPKNLSKK
EKELIEQIYEQTSFNPENNIDQ
>gnl|CDD|184611 PRK14297, PRK14297, molecular chaperone DnaJ
MASKDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQFG
TADFNGAGGFGSGGFGGFDFSDMGGFGDIFDSFFGGGFGSSSRRRNGPQRGADIEYTINLTFEEAVFGVE
KEISVTRNENCETCNGTGAKPGTSPKTCDKCGGTGQIRVQRNTPLGSFVSTTTCDKCGGSGKVIEDPCNK
CHGKGKVRKNRKIKVNVPAGVDTGNVIPLRGQGEHGKNGGPTGDLYINIRVAPHKTFKRKGFDIYIDKHI
SFAKAALGTEIKVPTVDGEVKYEVPAGTQPGTVFRLKGKGVPRVNSTGRGNQYVTVIVDIPKKLNSKQKE
ALTMFMEASGETVDGKEKKTIFEKIKKGFK
>gnl|CDD|184612 PRK14298, PRK14298, chaperone protein DnaJ; Provisional
MATTRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDRFG
HAGIDNQYSAEDIFRGADFGGFGDIFEMFFGGGGRRGRMGPRRGSDLRYDLYITLEEAAFGVRKDIDVPR
AERCSTCSGTGAKPGTSPKRCPTCGGTGQVTTTRSTPLGQFVTTTTCSTCHGRGQVIESPCPVCSGTGKV
RKTRKITVNVPAGADSGLRLKLSGEGEAGSPGAPSGDLYIVLHVKEHDYFERVGDDIISEIPISFTQAAL
GADIMVPTLYGKVKMNIPPGTQTHSVFRLKDKGMPRLHGHGKGDQLVKVIVKTPTKLTQEQKELLREFDE
LSNGKNPSKAGKKKKGIFDKVKDAFES
>gnl|CDD|237667 PRK14299, PRK14299, chaperone protein DnaJ; Provisional
MAYKDYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYDTYGT
TAASAGWQGPPPGPPGGGDFSGFNVGDFSDFFQQLFGGRGGFGGFGDLFGSVGRRARKGRDLEAELPLTL
EEAYRGGEKVVEVAGERLSVRIPPGVREGQVIRLAGKGRQGGDLYLVVRLLPHPVFRLEGDDLYATVDVP
APIAVVGGKVRVMTLDGPVEVTIPPRTQAGRKLRLKGKGWPRGPAGRGDQYAEVRITIPTRPTPEEERLY
KQLAELYKVRA
>gnl|CDD|172788 PRK14300, PRK14300, chaperone protein DnaJ; Provisional
MSQDYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGHD
AFQNQQSRGGGGNHGGFHPDINDIFGDFFSDFMGGSRRSRPTSSKVRGSDLKYNLTINLEEAFHGIEKNI
SFSSEVKCDTCHGSGSEKGETVTTCDACSGVGATRMQQGFFTIEQACHKCQGNGQIIKNPCKKCHGMGRY
HKQRNLSVNIPAGVENGTRIRHTGEGEAGIRGGNSGDLYVDIAIKPHDIYKVDGANLHCKLPISFVNAAL
GGEIEVPVIEGGKVNLTIPAGTQNGDQLRLRSKGMSKMRSTIRGDMLTHIHVEVPKNLSKRQRELLEEFK
KESINEKENDGSFFNKMKSLWS
>gnl|CDD|237668 PRK14301, PRK14301, chaperone protein DnaJ; Provisional
MSQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYDRFG
HAGVNGNGGFGGFSSAEDIFSHFSDIFGDLFGFSGGGSRRGPRPQAGSDLRYNLTVSFRQAAKGDEVTLR
IPKNVTCDDCGGSGAAPGTSPETCRHCGGSGQVRQSQGFFQIAVPCPVCRGEGRVITHPCPKCKGSGIVQ
QTRELKVRIPAGVDTGSRLRLRGEGEPGVHGGPPGDLYVVITVEDDKIFQRQGQDLVVTQEISFVQAALG
DRIEVPTLDDPVTLDIPKGTQSGEVFRLRGKGLPYLGSSQKGDLLVEVSVVTPTKLTKRQEELLREFEAL
EEEKPLEKVKKFFKKIGKAMGMD
>gnl|CDD|237675 PRK14328, PRK14328, (dimethylallyl)adenosine tRNA methylthiotransferase; Provisional
NKKYFIETYGCQMNEEDSEKLAGMLKSMGYERTENREEADIIIFNTCCVRENAENKVFGNLGELKKLKEK
NPNLIIGVCGCMMQQKGMAEKIKKKFPFVDIIFGTHNIHKFPEYLNRVKEEGKSVIEIWEKEDGIVEGLP
IDRKSKVKAFVTIMYGCNNFCTYCIVPYVRGRERSRKPEDIIAEIKELVSEGYKEVTLLGQNVNSYGKDL
EEKIDFADLLRRVNEIDGLERIRFMTSHPKDLSDDLIEAIADCDKVCEHIHLPVQSGSNRILKKMNRHYT
REYYLELVEKIKSNIPDVAITTDIIVGFPGETEEDFEETLDLVKEVRYDSAFTFIYSKRKGTPAAKMEDQ
VPEDVKHERFNRLVELQNKISLEKNKEYEGKIVEVLVEGPSKNDENKLTGRTRTNKLVNFIGDKELIGKL
VNVKITKANSFSLTGEVIE
>gnl|CDD|184632 PRK14336, PRK14336, (dimethylallyl)adenosine tRNA methylthiotransferase; Provisional
MPGYYLWTIGCQMNQAESERLGRLFELWGYSLADKAEDAELVLVNSCVVREHAENKVINRLHLLRKLKNK
NPKLKIALTGCLVGQDISLIRKKFPFVDYIFGPGSMPDWREIPEGFILPLKPPVSANVTIMQGCDNFCTY
CVVPYRRGREKSRSIAEIGCEVAELVRRGSREVVLLGQNVDSYGHDLPEKPCLADLLSALHDIPGLLRIR
FLTSHPKDISQKLIDAMAHLPKVCRSLSLPVQAGDDTILAAMRRGYTNQQYRELVERLKTAMPDISLQTD
LIVGFPSETEEQFNQSYKLMADIGYDAIHVAAYSPRPQTVAARDMADDVPVIEKKRRLKLIEDLQKETVG
KANAALMDTFAEVLVEGLQKNKWQGRTLGGKLVFLESDLPLEGCLVNVKIFKTSPWSLQAKLVNILES
>gnl|CDD|237680 PRK14341, PRK14341, lipoyl(octanoyl) transferase LipB
APPVEWRISDGLVPYPEALAFMEARVAAIAAGTADELVWLLEHPPLYTAGTSAKAEDLLDPDRFPVYETG
RGGQYTYHGPGQRVAYVMLDLKRRRRDVRAFVAALEEWIIATLAAFNIRGERREDRVGVWVRRPDKGSGA
EDKIAAIGVRLRRWVSFHGISINVEPDLSHFSGIVPCGISEHGVTSLVDLGLPVTMDDVDAALKKAFEKV
FGP
>gnl|CDD|237681 PRK14342, PRK14342, lipoyl(octanoyl) transferase LipB
MMQNKLIVRQLGLQPYEPVWQAMQEFTDTRDEETPDEIWLVEHPPVFTQGQAGKPEHILNPGDIPVVQSD
RGGQVTYHGPGQLVMYVLLDLKRLKLGVRQLVTAIEQTVINTLAEYGIEAHAKPDAPGVYVDGKKIASLG
LRIRRGCSFHGLALNVNMDLSPFLRINPCGYAGLEMTQLSDLGGPATVDEVAPRLLAELLALLGYNDQET
ITG
>gnl|CDD|237682 PRK14343, PRK14343, lipoyl(octanoyl) transferase LipB
AAASAAPAPAAALPVTVRWRGREPYEACFDAMRAFTDARTADTPDEIWLVEHPPVYTLGQAGDPAHLLVA
DSGIPLVKVDRGGQITYHGPGQVVAYLLLDLRRRKLMVRELVTRIEQAVIDTLAAYNLASERKAGAPGIY
VASGPHQGAKIAALGLKIRNGCSYHGLSLNVKMDLRPFLAINPCGYAGLETVDMASLGVAADWADVAQTL
ARRLIANLDGAAAAADLPQAAAQSN
>gnl|CDD|237683 PRK14344, PRK14344, lipoyl(octanoyl) transferase LipB
VDIGKLDTTPLSAQNRSAILFEPDNIVPFEDAWKWQKEWQQALIEDPSNPQAVWLLEHQLCYTLGRGASE
DNLLFSLNNPPADVFRIDRGGEVTHHMPGQLVTYLVLDLRRFNKDLNWYLRQLEQVLIDVLADLGIDGER
LDGLTGVWIGNKKVASIGIGCRRWITQHGFSLNVDCDLEGFNKIVPCGLEGCQVGRLSDWIPGLNIKEVK
PLLKKSLQERFGL
>gnl|CDD|184638 PRK14345, PRK14345, lipoyl(octanoyl) transferase LipB
MDGSIRSSTMPIEVRRLGLVDYQEAWDLQRELADARVAGEGPDTLLLLEHPAVYTAGKRTEPHERPTDGT
PVVDVDRGGKITWHGPGQLVGYPIIKLAEPLDVVDYVRRLEEALIAVCADLGLNAGRVDGRSGVWVPADG
GRPDRKIAAIGIRVSRGVTMHGFALNCDNDLAAFDAIVPCGISDAGVTTLSAELGRTVTVAEVVDPVAAA
LCDALDGRLPVRDHSPGSAVDSAL
>gnl|CDD|237684 PRK14346, PRK14346, lipoyl(octanoyl) transferase LipB
MAMDRRMLGRVDYLATVQAMQAFTAERTPETPDELWICEHPPVYTQGLAGKADHVLNPGDIPVVATNRGG
QVTYHGPGQVVAYPLIDLRRAGYFVKEYVYRIEEAVIRTLAHFGVTGHRVAGAPGIYVRLDDPFSHAALP
QRPQKRGGGAPQPPFRGLGKIAALGIKVSRHCTYHGVALNVAMDLEPFSRINPCGYAGLQTVDLSTIGVQ
TTWDEAASVLGQQLARYLAP
>gnl|CDD|172823 PRK14347, PRK14347, lipoyl(octanoyl) transferase LipB
MIRFITIPDFADYQVTLKLMEDYVNKVISDHEPEIVYLVEHSEVYTAGTNYKQEELLNYGDIPVIYTGRG
GKFTFHGPGQRVIYPILNLASPNRHKDLKLYIKMLEEWIINSLNYFGIKAYIIKDKVGIWVKVRKDEFAK
IAAIGVRVRKWVTYHGVAINISTDLSKFSGIIPCGLENSLVTSLNQLGIHVEMSEFDKIIQTEFNKIFK
>gnl|CDD|172824 PRK14348, PRK14348, lipoyl(octanoyl) transferase LipB
MKTITTDWELIPYSEAWSRQTEWFDALVHAKQNGESYENRIIFCEHPHVYTLGRSGKENNMLLGEEQLKT
IGATLYHIDRGGDITYHGPGQLVCYPILNLEEFGLGLKEYVHLLEEAVIRVCASYGVVAGRLEKATGVWL
EGDTSRARKICAIGVRSSHYVTMHGLALNVNTDLRYFSYIHPCGFIDKGVTSLQQELGHSIDMAEVKERL
GRELLAALLSK
>gnl|CDD|172825 PRK14349, PRK14349, lipoyl(octanoyl) transferase LipB
MIKWLARPADYASVWDAMKAFTAARGPGTADEIWLCEHAPVYTLGQAGRPEHLLNPGLIPVVHCDRGGQV
TYHGPGQVLAYTLFDLRRAGLYVREYVDMLEQATLATLRELGLEQACRKPGAPGIYVPQPGGELAKIAAL
GVKVRNGYAYHGLALNIDMDLSPFLGINPCGYEGLRTVDLAACGVRTSVERAGELLAAQLARAHGQAVQQ
RAAALAGVPG
>gnl|CDD|172826 PRK14350, ligA, NAD-dependent DNA ligase LigA; Provisional
MSKDIQDEILDLKKLIRKWDKEYYVDSSPSVEDFTYDKALLRLQELESKYPEYKTLDSPTLKFGSDLLND
FKEVEHSFPILSLDKVYDLKLLKLWIEKMDLENSNLGFDFGISVEPKIDGCSIVLYYKDGILEKALTRGD
GRFGNDVTENVRTIRNVPLFIDEKVELVLRGEIYITKENFLKINKTLEKPYTNARNLASGILRRIDSREV
ANFPLDIFVYDILYSSLELKTNHDAFDKLKKFGFKVNPFCRFFDGKNSIEEILNYVKDIEKKRNSFEYEI
DGVVLKVSDFALREILGYTSHHPKWSMAYKFESLSGFSKVNDIVVQVGRSGKITPVANIEKVFVAGAFIT
NASLHNQDYIDSIGLNVGDVVKISRRGDVIPAVELVIEKLSVGFFKIPDNCPSCKTALIKEGAHLFCVNN
HCPSVIVERIKYFCSKKCMNIVGLSDKTIEFLFEKKFISSEIDLYTFNFDRLINLKGFKDKRINNLKRSI
EASKKRPFSKLLLSMGIKDLGENTILLLINNNLNSFDKISTLCQDREFALSKLLKIKGIGEKIALNIIEA
FNDKIILDKFNFFKNLGFKMEEDSINIDVENSFLFGKKFCITGSFNGYSRSVLIDKLTKKGAIFNTCVTK
YLDFLLVGEKAGLKLKKANNLGIKIMSLFDIKSYVDLDD
>gnl|CDD|184640 PRK14351, ligA, NAD-dependent DNA ligase LigA; Provisional
MSTAAEEPDDNPYLRDPPTDFEPVEELSEDEAEEQAEQLREAIREHDHRYYVEADPVIADRAYDALFARL
QALEDAFDLDTENSPTRRVGGEPLDELETVEHVAPMLSIDQSGEADDVREFDERVRREVGAVEYVCEPKF
DGLSVEVVYEDGEYQRAATRGDGREGDDVTANVRTIRSVPQKLRGDYPDFLAVRGEVYMPKDAFQAYNRE
RIERGEEPFANPRNAAAGTLRQLDPSVVAERPLDIFFFDVLDASELFDSHWEELERFPEWGLRVTDRTER
VDDIDDAIAYRDRLLAARDDLNYEIDGVVIKVDDRDAREELGATARAPRWAFAYKFPARAEETTIRDIVV
QVGRTGRLTPVALLDPVDVGGVTVSRASLHNPAEIEELGVNVGDRVRVKRAGDVIPYVEEVVEKDSEGTF
EFPDTCPVCDSAVERDGPLAFCTGGLACPAQLERSIEHYASRDALDIEGLGEERVQQLVDAGLVESLADL
YDLTVADLAELEGWGETSAENLLAELEASREPPLADFLVALGIPEVGPTTARNLAREFGTFEAIMDADEE
ALRAVDDVGPTVAEEIREFFDSERNRAVIDDLLDHGVDPQPAESEGGDALDGLTFVFTGSLSGYTRSEAQ
ELVEAHGGNATGSVSGNTDYLVVGENPGQSKRDDAEANDVPTLDEEEFEELLAERGVAL
>gnl|CDD|184641 PRK14352, glmU, bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU
APRPTAVIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELAP
EVDIAVQDEQPGTGHAVQCALEALPADFDGTVVVTAGDVPLLDGETLADLVATHTAEGNAVTVLTTTLDD
PTGYGRILRDQDGEVTAIVEQKDATPSQRAIREVNSGVYAFDAAVLRSALARLSSDNAQGELYLTDVLAI
AREAGHRVGAHHADDSAEVAGVNDRVQLAALGAELNRRIVEAWMRAGVTIVDPATTWIDVDVTIGRDVVI
HPGTQLLGRTTIGEDAVVGPDTTLTDVTVGEGASVVRTHGSESEIGAGATVGPFTYLRPGTVLGEEGKLG
AFVETKNATIGRGTKVPHLTYVGDADIGEHSNIGASSVFVNYDGVNKHRTTIGSHVRTGSDTMFVAPVTV
GDGAYTGAGTVIREDVPPGALAVSEGPQRNIEGWVQRKRPGTPAAEAAEAASEAAAQQSTGP
>gnl|CDD|184642 PRK14353, glmU, bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU
MTDRTCLAIILAAGEGTRMKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAAKIA
PDAEIFVQKERLGTAHAVLAAREALAGGYGDVLVLYGDTPLITAETLARLRERLADGADVVVLGFRAADP
TGYGRLIVKGGRLVAIVEEKDASDEERAITLCNSGVMAADGADALALLDRVGNDNAKGEYYLTDIVAIAR
AEGLRVAVVEAPEDEVRGINSRAELAEAEAVWQARRRRAAMLAGVTLIAPETVFFSYDTVIGRDVVIEPN
VVFGPGVTVASGAVIHAFSHLEGAHVGEGAEVGPYARLRPGAELGEGAKVGNFVEVKNAKLGEGAKVNHL
TYIGDATIGAGANIGAGTITCNYDGFNKHRTEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDD
ALALGRARQETKPGWAKKLRERLRAK
>gnl|CDD|184643 PRK14354, glmU, bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU
MNRYAIILAAGKGTRMKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRSEFA
LQEEQLGTGHAVMQAEEFLADKEGTTLVICGDTPLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGR
IIRNENGEVEKIVEQKDATEEEKQIKEINTGTYCFDNKALFEALKKISNDNAQGEYYLTDVIEILKNEGE
KVGAYQTEDFEESLGVNDRVALAEAEKVMRRRINEKHMVNGVTIIDPESTYIDADVEIGSDTVIEPGVVI
KGNTVIGEDCVIGPGSRIVDSTIGDGVTITNSVIEESKVGDNVTVGPFAHLRPGSVIGEEVKIGNFVEIK
KSTIGEGTKVSHLTYIGDAEVGENVNIGCGTITVNYDGKNKFKTIIGDNAFIGCNSNLVAPVTVGDNAYI
AAGSTITKDVPEDALAIARARQVNKEGYVKKLPHKKKS
>gnl|CDD|237685 PRK14355, glmU, bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU
MNNLAAIILAAGKGTRMKSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGDV
SFALQEEQLGTGHAVACAAPALDGFSGTVLILCGDVPLLRAETLQGMLAAHRATGAAVTVLTARLENPFG
YGRIVRDADGRVLRIVEEKDATPEERSIREVNSGIYCVEAAFLFDAIGRLGNDNAQGEYYLTDIVAMAAA
EGLRCLAFPVADPDEIMGVNDRAQLAEAARVLRRRINRELMLAGVTLIDPETTYIDRGVVIGRDTTIYPG
VCISGDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGSVLEDSVVGDDVAIGPMAHLRPGTELSAHVKIGNF
VETKKIVMGEGSKASHLTYLGDATIGRNVNIGCGTITCNYDGVKKHRTVIEDDVFVGSDVQFVAPVTVGR
NSLIAAGTTVTKDVPPDSLAIARSPQVNKEGWKLRKKDK
>gnl|CDD|237686 PRK14356, glmU, bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU
DMASTTGALILAAGKGTRMHSDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPDED
ARFVLQEQQLGTGHALQCAWPSLTAAGLDRVLVVNGDTPLVTTDTIDDFLKEAAGADLAFMTLTLPDPGA
YGRVVRRNGHVAAIVEAKDYDEALHGPETGEVNAGIYYLRLDAVESLLPRLTNANKSGEYYITDLVGLAV
AEGMNVLGVNCGEDPNLLGVNTPAELVRSEELLRARIVEKHLESGVLIHAPESVRIGPRATIEPGAEIYG
PCEIYGASRIARGAVIHSHCWLRDAVVSSGATIHSFSHLEGAEVGDGCSVGPYARLRPGAVLEEGARVGN
FVEMKKAVLGKGAKANHLTYLGDAEIGAGANIGAGTITCNYDGVNKHRTVIGEGAFIGSNTALVAPVTIG
DGALVGAGSVITKDVPDGSLAIARGRQKNLPRKKKA
>gnl|CDD|237687 PRK14357, glmU, bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU
MRALVLAAGKGTRMKSKIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAELVKKLLPEWVKIFLQE
EQLGTAHAVMCARDFIEPGDDLLILYGDVPLISENTLKRLIEEHNRKGADVTILVADLEDPTGYGRIIRD
GGKYRIVEDKDAPEEEKKIKEINTGIYVFSGDFLLEVLPKIKNENAKGEYYLTDAVNFAEKVRVVKTEDL
LEITGVNTRIQLAWLEKQLRMRILEELMENGVTILDPNTTYIHYDVEIGMDTIIYPMTFIEGKTRIGEDC
EIGPMTRIVDCEIGNNVKIIRSECEKSVIEDDVSVGPFSRLREGTVLKKSVKIGNFVEIKKSTIGENTKA
QHLTYLGDATVGKNVNIGAGTITCNYDGKKKNPTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDV
PPYSLALGRARQIVKEGWVLKKRKEEEN
>gnl|CDD|237688 PRK14358, glmU, bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
MTEQTRPLDVVILAAGQGTRMKSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQG
SGVAFARQEQQLGTGDAFLSGASALTEGDADILVLYGDTPLLRPDTLRALVADHRAQGSAMTILTGELPD
ATGYGRIVRGADGAVERIVEQKDATDAEKAIGEFNSGVYVFDARAPELARRIGNDNKAGEYYLTDLLGLY
RAGGAQVRAFKLSDPDEVLGANDRAGLAQLEATLRRRINEAHMKAGVTLQDPGTILIEDTVTLGRDVTIE
PGVLLRGQTRVADGVTIGAYSVVTDSVLHEGAVIKPHSVLEGAEVGAGSDVGPFARLRPGTVLGEGVHIG
NFVETKNARLDAGVKAGHLAYLGDVTIGAETNVGAGTIVANFDGVNKHQSKVGAGVFIGSNTTLIAPRVV
GDAAFIAAGSAVHDDVPEGAMAVARGKQRNLEGWSRRYWAGRHEKVAKKLPWLAGWLSRQG
>gnl|CDD|237689 PRK14359, glmU, bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU
MKLSIIILAAGKGTRMKSSLPKVLHTICGKPMLFYILKEAFAISDDVHVVLHHQKERIKEAVLEYFPGVI
FHTQDLENYPGTGGALMGIEPKHERVLILNGDMPLVEKDELEKLLENDADIVMSVFHLADPKGYGRVVIE
NGQVKKIVEQKDANEEELKIKSVNAGVYLFDRKLLEEYLPLLKNQNAQKEYYLTDIIALAIEKGETIKAV
FVDEENFMGVNSKFELAKAEEIMQERIKKNAMKQGVIMRLPETIYIESGVEFEGECELEEGVRILGKSKI
ENSHIKAHSVIEESIIENSDVGPLAHIRPKSEIKNTHIGNFVETKNAKLNGVKAGHLSYLGDCEIDEGTN
IGAGTITCNYDGKKKHKTIIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLAISRAPQKNIK
NFYYKFFKKK
>gnl|CDD|184646 PRK14360, glmU, bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU
MLAVAILAAGKGTRMKSSLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAHLPGLEF
VEQQPQLGTGHAVQQLLPVLKGFEGDLLVLNGDVPLLRPETLEALLNTHRSSNADVTLLTARLPNPKGYG
RVFCDGNNLVEQIVEDRDCTPAQRQNNRINAGIYCFNWPALAEVLPKLSSNNDQKEYYLTDTVSLLDPVM
AVEVEDYQEINGINDRKQLAQCEEILQNRIKEKWMLAGVTFIDPASCTISETVELGPDVIIEPQTHLRGN
TVIGSGCRIGPGSLIENSQIGENVTVLYSVVSDSQIGDGVKIGPYAHLRPEAQIGSNCRIGNFVEIKKSQ
LGEGSKVNHLSYIGDATLGEQVNIGAGTITANYDGVKKHRTVIGDRSKTGANSVLVAPITLGEDVTVAAG
STITKDVPDNSLAIARSRQVIKENWKKKSS
>gnl|CDD|172837 PRK14361, PRK14361, Maf-like protein; Provisional
VILASGSPRRRELLENLGVPFQVVVSGEAEDSTETDPARLAAELALLKARAVARLHPDAVVIAADTVVAL
GGVLLAKPADEAENEAFLRVLSGRTHQVYTGVAVLSRGTEQVGVERTDVTFRALTAAEISFYARSGEGLD
KAGGYGIQGVGMALVSRVEGDYSNVVGFPLSLVIRLLRGAGVPVWGE
>gnl|CDD|172838 PRK14362, PRK14362, Maf-like protein; Provisional
PFTSTGPFTAACPVVLASGSPRRREFLEQMGLPFEVILPGAAEPSPIEGEQPEAYARRAAEAKARAVAAD
HAGRLVIAADTVVALDGMILGKPADRADALSMLRRLAGRTHEVVSACCVVLPDGGREVFHAITRVTMWDW
PEAALAAYVATGEPSDKAGAYGIQGIGAFLVRSIEGSWSNVVGLPVAELTALLLRRGVILPVGAVHA
>gnl|CDD|184647 PRK14363, PRK14363, Maf-like protein; Provisional
MRIILASSSPRRRQLMELLGIEFEVEKPDVEEEFLESPEETVRELSLRKAEWVFKKRKEEEILVIGSDTV
VVLDGNILGKPESLEEAKGMLKKLSGRWHVVYTGVAFVSSETKDVIVSSTKVRFRELPESVIDYYVEKYR
PLDKAGAYGIQDFAAVFVEKIEGDFFTVVGFPLGMVWQYLYEKGWWKFASKREDDKGGARVAFG
>gnl|CDD|184648 PRK14364, PRK14364, Maf-like protein; Provisional
LASSSPRRRELLQQLGLNFEIYSPDIDESVHEGELVHQYVERLAREKAQAVLNIFPDSVIIAADTSLGLD
GQIIGKPDSKQHAFDIWKQLSGRWHDVFSGICIATQQQILSQVVQTQVEFASLTTQDMEDYWATGEPVGK
AGAYAIQGIASQYIPKIQGSYSNVVGLPLYEFSQLFKRVKT
>gnl|CDD|237690 PRK14365, PRK14365, Maf-like protein; Provisional
MRRIILASASPRRKELLKQLIGDNFLVYPSSYEEPPQPGLDPEELLLKHSLEKARDVAKHFDSGIIISAD
TSVFCNGEVLGKPASPENAEEMLEKLSGRKFLVITGLTVLDLDSGKEISEIESTDVWMTELSREQILAYV
RTGEPLDKAGAFAIQGKGAVLVEKIEGDFFNVVGLPLFRLGKILEKLGVSVFDEGFS
>gnl|CDD|237691 PRK14366, PRK14366, Maf-like protein; Provisional
MLKFDNLILASSSKQRLALLEQIGVVPGEIVSPDIDESPLKKELPKDYSIRMAKEKAEKVQSLRPDKFVL
GADTVVCCGRRILLKAETEEQAEEYLELLSGRRHRVYTSVCLYTPGGKLHIRSVVTVVKFKRLSKQEIKY
YIASGEWKGKAGGCNIQGLAGKFVLSINGSYSSIIGLPLHETYCLLSGYFNLKHI
>gnl|CDD|237692 PRK14367, PRK14367, Maf-like protein; Provisional
MNTLYLGSNSPRRMEILTQLGYRVVKLPAGIDETVKAGETPARYVQRMAEEKNRTALTLFCETNGTMPDF
PLITADTCVVSDGIILGKPRSQAEAIEFLNRLSGKQHTVLTAVCIHYRGKTSSRVQTNRVVFKPLSSEEI
SAYVQSGEPMDKAGAYAVQGIGGIFIQSIEGSFSGIMGLPVYETVSMLQDLGYRSPLSALKP
>gnl|CDD|237693 PRK14368, PRK14368, Maf-like protein; Provisional
MMANSPIVLASASPRRSELLASAGIEFDVVPADIPEEPLPGEEPVDHVLRLAREKARAAAALAEGRFFIG
ADTIVVCDGEIMGKPKDEADAVRMLKKLSGVPHEVITGFAVYDRERDGCVTKAVRTKVFFKPLRDEEIRD
YIATGCPMDKAGAYAIQGGAAHMVRKIDGSYTNVVGLPLCEVVEALRTIGALG
>gnl|CDD|184650 PRK14369, PRK14369, membrane protein insertion efficiency factor YidD
MKYPLLALIKLYQWTISPLLGPVCKYYPSCSHYGYTAIDRHGAIKGTALTAWRILRCNPWSLGGVDHVPP
RKRPRWHEMLRNAWRARKGGESAAEPATEGHVSEPSSPAAETSPHAQGA
>gnl|CDD|184651 PRK14370, PRK14370, hypothetical protein; Provisional
FIKPINKYLYKLLLAFIHFYQRIISPILPARCRYYPTCSNYGKQAIAWHGVGKGSLLLLKRIGRCHPLGG
HGIDFVPLPLASYHYQAISLSVSRETLVGRYVYKDNISYVARLNHMMKLT
>gnl|CDD|172847 PRK14371, PRK14371, hypothetical protein; Provisional
MRKLALVPIQFYRYAISPLMASHCRFYPSCSCYAYEAIENHGLLRGGWLSVRRLGRCHPWNPGGYDPVPP
APTSRSSSMAE
>gnl|CDD|172848 PRK14372, PRK14372, membrane protein insertion efficiency factor YidD
MIRGIRWYQQRISANTPPCCKYYPSCSNYAIEAIERFGAFKGGVLAVLRLLRCRPWSRGGIDDVPQRYSL
FYRCSWSKAHEEPRLTPLPTTQKEAQR
>gnl|CDD|172849 PRK14373, PRK14373, hypothetical protein; Provisional
MNFLLSKLLLGLIRFYQYCISPLIPPRCRYTPTCSQYAVEAVKKYGAFKGGRLAIKRIARCHPFGGHGHD
PVP
>gnl|CDD|237694 PRK14374, PRK14374, membrane protein insertion efficiency factor YidD
MRNNKTPFLSAIFTASIRGYQRFFSAFTFSSCRFYPTCSNYALWLLCFENPLSAMGKIAIRILSCNPFCS
GGIAYPTTRLKRPSLLQSHKDFNRNFKTITFWLVPTTKSRATYYIIKV
>gnl|CDD|172851 PRK14375, PRK14375, membrane protein insertion efficiency factor YidD
MLINLYRYCISPFIPARCRYYPTCSEYALEALKTHGILKGLYLTTRRLLRCHPLSKRDYYDLVPCKNKKG
>gnl|CDD|237695 PRK14376, PRK14376, membrane protein insertion efficiency factor YidD
AGLGVALAVAAVVDLVLASIATSRRLPTVARTADGAVRGPLAWTFAGLVRLYRAGWSGRNAGCCRFEPSC
SAYALTAVRRHGGVRGGLLAVRRLLRCQPLSAGGYDPVPGEAPGTSVGPGTVRKPRGRTRTAGGPVGAVD
AGTPHRSRRPTGGHGTASLHRGTRSEIVGSRRGTRV
>gnl|CDD|172853 PRK14377, PRK14377, membrane protein insertion efficiency factor YidD
MQTSRISSFFRGLVHLYRWAISPFLGAPCRFFPTCSEYALVALKKHPLRKSLFLIAKRLLKCGPWCIGGI
DLVPRTSVEEYLSSPTPLAESPDDRTVPHTQETS
>gnl|CDD|237696 PRK14378, PRK14378, membrane protein insertion efficiency factor YidD
MKRALTSVVLAPRNAAIAVIRLYRRVVSPFYGDVCRYYPSCSAYGLEAVQEHGLIFGGYLAVWRVCRCHP
WAEGGIDDVPARGVQQYRRTRFGFVVAPSHGKG
>gnl|CDD|237697 PRK14379, PRK14379, membrane protein insertion efficiency factor YidD
MRKILIFLVRVYQKFISPILPPSCRYYPTCSSYMIDALKKHGPILGLIMGLARILRCNPFIRGGVDPVPD
YFTLRRNPHPERYEDEIIAQKFHSN
>gnl|CDD|184654 PRK14380, PRK14380, hypothetical protein; Provisional
MGKINLMLRQIVCLPIKMYQYFISPLITPCCRYYPSCSEYADSAIKHYGVIKGLLMALNRLSRCHPWSKG
GYDPLFPNDKN
>gnl|CDD|172857 PRK14381, PRK14381, membrane protein insertion efficiency factor YidD
MSFKRFLQNLPVRICLGLIHLYRWTISPLLGSPCRFFPSCSQYALQALKHHGCIMGLWLTIKRIGKCGPW
HPGGIDLVPMTTLEEVLDPSQEIDDDDSSDFSA
>gnl|CDD|172858 PRK14382, PRK14382, hypothetical protein; Provisional
MKRLLIKFIKFYQKFISPLYPSSCRFYPTCSTYAILSIEKYGALKGSLKAFWRILRCNPFSKGGVDYP
>gnl|CDD|237698 PRK14383, PRK14383, membrane protein insertion efficiency factor YidD
MSMAARGLVRAVRWYQRVLSPRKPAPTCRFSPTCSQYAVEAIERHGALKGGWLALWRVLRCNPLVPGGFD
PVPEHFPARRPRHP
>gnl|CDD|172860 PRK14384, PRK14384, hypothetical protein; Provisional
MSSCRFYPSCSCYAETALKRFGVIKGSGLTVWRLLRCHPFHPGGVDFVPEKSNEMV
>gnl|CDD|172861 PRK14385, PRK14385, membrane protein insertion efficiency factor YidD
MIIKKIFIILNLILILLIKIYQNTLSKIVGFQCIYKPSCSNYALECLKKYNILTALILITLRIIRCNALF
KGGNESLPTKKPILNSLKEFKTRLIK
>gnl|CDD|172862 PRK14386, PRK14386, membrane protein insertion efficiency factor YidD
MVRILRWFIRLYQIAISPLLGPRCRYIPTCSQYALEALQTHGAIKGVWLSSKRICRCHPWGGSGYDPVPP
KAIRFISFHQIDSQTHHVAVPFRDRLMKQNLSNHLG
>gnl|CDD|184655 PRK14387, PRK14387, membrane protein insertion efficiency factor YidD
MTFYERTVDLGLRAYKLTLSPLIGRQCRFTPSCSEYTAAALKDHGPLKGSWLGLRRICRCNPFGGSGYDP
PPPRHQPRKWKCEE
>gnl|CDD|172864 PRK14388, PRK14388, membrane protein insertion efficiency factor YidD
MTRILLLLLRFYQYFISPLLGNNCRFHPTCSEYAKEAISMHGSIKGLWFTFKRIIKCQPFCDGGYDTVPI
SIKNSKPLNKKI
>gnl|CDD|184656 PRK14389, PRK14389, membrane protein insertion efficiency factor YidD
MMRRLLMALVRGYRLLLSPWLGSACRFEPTCSAYSLQALEQHGAAAGSYLTLRRLARCHPWCDGGHDPVP
QEKPRGMRLFSRLTPAPDTAPSSPKKSS
>gnl|CDD|172866 PRK14390, PRK14390, hypothetical protein; Provisional
MISFYQKWFSPFFGPRCRFIPSCSSYGYEAITRHGPWKGGWLTLRRLSRCHPLTPCGCDPVPD
>gnl|CDD|172867 PRK14391, PRK14391, membrane protein insertion efficiency factor YidD
MNQFVIQLIQLYKKIISPLLPPACRFTPTCSEYAAQAFQECGFFQAIQLSAWRILRCNPLSQGFDDPLPP
NTKGTNLTHGRQTK
>gnl|CDD|237700 PRK14397, PRK14397, membrane protein; Provisional
MGSLLWIATAYVMGSIPFGLVFARTFCGIDPRTGGSRNVGATNVARLCGTKWGVLTLVCDVLKGAVPVAV
AMSISDSPVFHSLTALAALLGHLYSCFLGFRGGKAVATTIGVFIPLAFWQLLLSGILCLLVIWRSGFVSL
GSLTLVTALPVMLLITGKWKLIPLALVVMALVYWSHRENIGRLARGEEKPWQKKHHDAAQGTAAGAAPTA
NADAADAGTVDC
>gnl|CDD|237702 PRK14399, PRK14399, membrane protein; Provisional
MKGFYMYYLGIILASVFGYFLGSISWSIIIVKKVGNIDIRTVGSGNPGATNTVRILGKKWGLVVAFLDAL
KVLFTAIFAILLSMIPNELFSQTSYFIPCIFALIGHCWPIYYKFKGGKAVSCFLGLLFVVNYLYLIIFLI
VWFISVAISRKVSVASIFSAATILLIMWIPYLYGVSYFIWQWNGLESFIVAWKNYILFSLLNSFHYWFSN
IWASGMLEGNIIILIGGLILVVRHSQNIKRIKNKTEPDTFPKKEKNVK
>gnl|CDD|184658 PRK14401, PRK14401, membrane protein; Provisional
MLLLVAVLAYLLGSLVAGVLYSRARGEDIRERDLPGGSGTYRQFGPGAALLVAAADILKGVAAALLARWL
APPATWLAGAAVVAGHCWPVFFRFRGGGGIAPTLGFFLVLAPGTTLGTVAFGLAVAGLYRALLWRQRRKG
LYPIPFGAVVGYPVGLLVATRSGGFLALLAGSGVVALRGLQLLASRR
>gnl|CDD|237706 PRK14405, PRK14405, membrane protein; Provisional
MILLLLAVVLSYLLGSVSFSYLIAKKIKGIDIRQHGSGNAGATNTLRVLGKGPAILVLLLDVVKGIAAVW
IGRLLTGDGAAWFPALAGLAAIIGHNWPIYFGFRGGKGIATTIGVVATLVFLPALIAGVIAIISIVITRY
VSLGSLLFVTLTPVLLYIFDYPIPYIWLSLIIAIFAFWRHRTNIVRLLSGTENKLGKKKGRK
>gnl|CDD|184663 PRK14411, PRK14411, membrane protein; Provisional
MARFWATLIGYVFGNFLTAMIVGKIFLHKDPTKYGSGNPGTANMGAVFGKKWGILTCIGDLLKTLIALFI
VYFIYHGHLNIAYAGLGVVLGHCFPIWNHFKGGKGVAVTAQVAVFYDWRAGLITLLIALVLTAIMQNLTI
PPLVFMLLFSIYTFWNNQEAGLVFLIITLIMIFKFRKDIVDFFTGHGKRVDILYTIKKKLGIYK
>gnl|CDD|184665 PRK14414, PRK14414, glycerol-3-phosphate acyltransferase
MNSLIMVIIALIAAYFIGSTPAPYLAGRIFKGIDIRTVGSKNMGSMNVFYNVGFWPGILVLAVDIGKGAL
AMAVANWLGEGLGIQMLCALMAIAGHNYPVWLKFKGGKGGATAIGILAYMMPEGIPIYIACFLILMAITR
FPTLSYGISFISFILVAWLGQHDMGKVLFSLLVVMIPILMYIPRMKEIKNKAGSGNAKRAIFRKNLKERL
>gnl|CDD|184667 PRK14416, PRK14416, membrane protein; Provisional
LLGSIPSAYLVTRRLTGRDIRQMGGGNVGGLNTFREVGTGAGIAVVFIDLVKGALAVSVSYYLLTQNAQW
VILTGFAAVIGHNWSVWLDFKGGKGLGPAFGAMLFLLPVYGLPQQLGILALLVFIPLALTRNIALATGIA
LFSLPFLVWYGSHSEFATLISVLLFLMIGIKFVLDNRKSLRDPANRRNLIVDHWKRPDKG
>gnl|CDD|184668 PRK14417, PRK14417, membrane protein; Provisional
MSPVFLIMIPAGYLVGAIPMAYLLSRWRRGIDIRRYGSGNVGASNVIKTAGKRLGLAVFVFDVSKGALMI
LLAGWLGLELWQQIVVGLATIAGHNWPVFLRFNGGRGIATSLGVALVMAPVPALIALSTALTFGFFKKMA
PGVFLGVGALPVMSGYFHGFFGVQEPQTVTWGFIGIFLIMIVRRLMAPDSEYSSTVSKAELVFNRLFLDR
DIRDRSVWINRNSAAHKESLGI
>gnl|CDD|237709 PRK14419, PRK14419, membrane protein; Provisional
LLMALLIILLAYLLGSFPSGYLAGRWLKGIDLREIGSGSTGATNVLRNVGKGPALFVFIIDVGKGVLAVL
LAYALGLQPWLQVLAGLAALLGHIWPVWLGFKGGKAVATGLGMLLALSWPVGLASLGIFLIVLALSRIVS
LSSISAAIALPLLMFLLNIPLPYILFSLAAGLLVIWRHRSNIERLLAGTEPKIGQKNKT
>gnl|CDD|237710 PRK14420, PRK14420, acylphosphatase; Provisional
MLQYHIIVDGRVQGVGFRYFVQMEADKRKLTGWVKNRDDGTVEIEAEGPEEALQLFLDAIEKGSPFSKVT
DVHIEERDVLSGEKQFRIMYG
>gnl|CDD|237711 PRK14421, PRK14421, acylphosphatase; Provisional
MSEIVRQVTIRGRVQGVGYRAWVARTAEALGLEGWVRNRRDGSVEALFAGPADAVAEMIARCRRGPSAAR
VDAVEDEPAAPDALNLRRPGERFSILPTV
>gnl|CDD|237712 PRK14422, PRK14422, acylphosphatase; Provisional
MMAPDVRLTAWVHGHVQGVGFRWWTRSRALELGLTGYAANLADGRVQVVAEGPRAACEKLLQLLRGDDTP
GRVDKVVEDWSEPRGQITGFVER
>gnl|CDD|237713 PRK14423, PRK14423, acylphosphatase; Provisional
MSDRTRAHVFVSGRVQGVYYRASTRDTARELGVDGWVRNLDDGRVEAVFEGPRDAVEAMVEWCHEGSPAA
VVEDVEVEYEEPEGLDGFEIRR
>gnl|CDD|184674 PRK14424, PRK14424, acylphosphatase; Provisional
ELDERIETYYVRVRGVVQGVGFRHATVREAHALGLRGWVANLEDGTVEAMIQGPAAQIDRMLAWLRHGPP
AARVTEVTFEERRTEKRFERFQQH
>gnl|CDD|172901 PRK14425, PRK14425, acylphosphatase; Provisional
MSDHREAVRVRITGRVQGVGFRDWTRDEAERLGLTGWVRNESDGSVTALIAGPDSAISAMIERFRRGPPG
ASVSGVETEAAQLEEAPTDFRITR
>gnl|CDD|184675 PRK14426, PRK14426, acylphosphatase; Provisional
MSKVCIIAWVYGRVQGVGFRYHTQHEALKLGLTGYAKNLDDGSVEVVACGEEEQVEKLMEWLKEGGPRSA
RVDRVLTEPHSPRGELTGFSIR
>gnl|CDD|172903 PRK14427, PRK14427, acylphosphatase; Provisional
PAAHQVRLSARVFGVVQGVGFRYWTMRKAEELGLTGTVRNLDDGSVALVAEGTGEQVEKLLDWLNSDRAP
GRVERVDHTVSEATGEFREFRARD
>gnl|CDD|172904 PRK14428, PRK14428, acylphosphatase; Provisional
MRQSANLVRKHIVVTGLVQGVGFRYFTVTQARRLGVQGWVRNCRDGSVELEAQGSSDAVQALVEQLAIGP
RWSEVSHVAVHDMPIIDETARAFGVRQ
>gnl|CDD|184676 PRK14429, PRK14429, acylphosphatase; Provisional
MKRVLIKLTGKVQGVGCRRATLTKARALGVTGYVTNCEDGSVEILAQGSDPAVDNLIAWCEVGVPCTEVL
RVTVEEDEADEIYLDFSIVQ
>gnl|CDD|172906 PRK14430, PRK14430, acylphosphatase; Provisional
MTKETWRLVAHGRVQGVGYRAACADAADDLGLGGWVRNRADGTVEVMASGTVRQLEALRAWMEAGPPAAQ
VTKVEVGPGAGEFAGFDLRPTA
>gnl|CDD|184677 PRK14431, PRK14431, acylphosphatase; Provisional
MRHIHLQVFGRVQGVGFRYFTQRIAMNYNIVGTVQNVDDYVEIYAQGDDADLERFIQGVIEGASPASNVT
SYQLEELELNQKLSDFRSI
>gnl|CDD|184678 PRK14432, PRK14432, acylphosphatase; Provisional
MYKQQYFISGKVQGVGFRFFTEQIANNMKLKGFVKNLNDGRVEIVAFFNTKEQMKKFEKLLKNGNKYSNI
ENIEKKVLDENYPFQFNDFKIYY
>gnl|CDD|184679 PRK14433, PRK14433, acylphosphatase; Provisional
MRLTALVSGRVQGVGYRAFVQKKARELGLSGYAENLSDGRVEVVAEGPKEALERLLHWLRRGPRHARVEA
VDVQWSEATGLKGFHVY
>gnl|CDD|184680 PRK14434, PRK14434, acylphosphatase; Provisional
MQKVRMIVSGRVQGVGFRYSVYSLALEIGDIYGRVWNNDDGTVEILAQSDDSAKLAKFIQEIRKGPSKWA
KVTYVDVTMANFEDFSDFKIAN
>gnl|CDD|184681 PRK14435, PRK14435, acylphosphatase; Provisional
MKALKIRVEGIVQGVGFRYFTRRVAKSLGVKGYVMNMDDGSVFIHAEGDENALRRFLNEVAKGPPAAVVT
NVSVEETTPEGYEDFTIKYY
>gnl|CDD|172912 PRK14436, PRK14436, acylphosphatase; Provisional
MEIVRAHLRIYGRVQGVGFRWSMQREARKLGVNGWVRNLPDGSVEAVLEGDEERVEALIGWAHQGPPLAR
VTRVEVKWEEPKGEKGFRVVG
>gnl|CDD|172913 PRK14437, PRK14437, acylphosphatase; Provisional
MGSDYVKISIEGLNMTQKEKNETCIHATVSGKVQGVFFRESVRKKAEELQLTGWVKNLSHGDVELVACGE
RDSIMILTEWLWEGPPQAAVSNVNWEEIVVEDYSDFRVR
>gnl|CDD|172914 PRK14438, PRK14438, acylphosphatase; Provisional
MKIRAMVTVKGLVQGVAFRHHTQQTAQRLNVSGWVKNLPNGSVQGCFEGEETDVAALIDWCHHGPSRARV
SGVIVEREEFRGEFDDFDIRY
>gnl|CDD|237714 PRK14439, PRK14439, acylphosphatase; Provisional
MVSPRLALPSMRATAPEKTHGWRRSNDFSRPLANTKRTLIIYFSVDAKKWASLSGVFHGFATRPLRIRRA
AMSKVCIIAWVYGRVQGVGFRYTTQYEAKKLGLTGYAKNLDDGSVEVVACGEEGQVEKLMQWLKSGGPRS
ARVERVLSEPHHPSGELTDFRIR
>gnl|CDD|172916 PRK14440, PRK14440, acylphosphatase; Provisional
MLKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGSVEVVAEGYEEALSKLLERIKQGPPAAEV
EKVDFSFSEYKGEFEDFETY
>gnl|CDD|172917 PRK14441, PRK14441, acylphosphatase; Provisional
MADRVRARIVVSGRVQGVAFRQSAADEARRLGVEGWVRNLPDGRVEAEAEGERAAVGALVRWCHAGPPAA
RVDRVEVEWVEPAGDLGAFEIRF
>gnl|CDD|172918 PRK14442, PRK14442, acylphosphatase; Provisional
MARICLHAYVGGRVQGVGFRQATREEADRLELDGWVRNLDDGRVEVVWEGEEDRAKALERWLGRGPRHAE
VSAVEVEQMPLQGIAGFVVRR
>gnl|CDD|172919 PRK14443, PRK14443, acylphosphatase; Provisional
MARDTAILRVTGFVQGVGFRYTTKHVAYKYDISGTVKNLDDGSVEIHAIAEEENLNKFIDAIKKGPSPGC
RIEHVYIYKGAPVEERKTFDIVY
>gnl|CDD|172920 PRK14444, PRK14444, acylphosphatase; Provisional
MDMVRAHVFISGRVQGVNFRAYTRDRAREAGVKGWVRNLSDGRVEAVFEGSRPAVQKMISWCYSGPSHAR
VERVEVHWEEPTGEERTFTIVW
>gnl|CDD|172921 PRK14445, PRK14445, acylphosphatase; Provisional
MMEKRVHLIVSGLVQGVGFRMFIDRAASELNLSGWVRNLPDGTVEIEAQGSSGMIDELIKQAERGPSRSS
VTSIMVEELEPDSSLKGFSII
>gnl|CDD|172922 PRK14446, PRK14446, acylphosphatase; Provisional
MQAARFVVSGVVQGVWYRASTRERAVALGLVGHARNQADGSVEVVAAGSAAALEALEAWLWQGPPAATVA
AVTRTPCAVPPTEDFVTG
>gnl|CDD|172923 PRK14447, PRK14447, acylphosphatase; Provisional
MEMVRAHLFIRGKVQGVFFRQSMKEVANRNGVRGWVRNRSDGRTVEAVLEGPRDAVLKVIEWARVGPPGA
RVEDVEVKWEEYKGEFQDFRILPTE
>gnl|CDD|172924 PRK14448, PRK14448, acylphosphatase; Provisional
MLKKQFIVYGHVQGVGFRYFTWQEATKIGIKGYVKNRPDGSVEVVAVGSDAQIAAFRDWLQHGPPTAVVC
NVIEQDYQGSRQFTHFSVRR
>gnl|CDD|184682 PRK14449, PRK14449, acylphosphatase; Provisional
MKKTVHLRITGHVQGVGLRYSVYQKAVSLGITGYAENLYDGSVEVVAEGDEENIKELINFIKTGLRWARV
DNVEERWSDYKGEYRDFRIY
>gnl|CDD|184683 PRK14450, PRK14450, acylphosphatase; Provisional
MHCLKAIVKGKVQGVYFRDFTRTQATRLGLCGYAKNLANGNEVEVVAEGDKDSLLEFLDLLRSGPPRAEV
KEVETSWETATANYSDFRIKY
>gnl|CDD|237715 PRK14451, PRK14451, acylphosphatase; Provisional
KELCMRCYISGRVQGVWFRASAKKLAEQLMISGWARNLADGRVEVFACGKEDKLEEFYTWLQKGPLNARV
DVCTRENLPWQDYISFDVL
>gnl|CDD|237716 PRK14452, PRK14452, acylphosphatase; Provisional
MIARRFVDRQQPRRLQIFAERWRFLIEGRVQGVGFRASCCRRALDLGLSGWVRNLSDGSVEVQAEGPPLA
LSELRAWCERGPPGARVKRVDPSQLPVTGDDWFEVRY
>gnl|CDD|184685 PRK14453, PRK14453, chloramphenicol/florfenicol resistance protein; Provisional
KQTKTKYGKMKQILSNLKLPDYRYEQITKAIFKQRIDNFEDMHILPKALRESLINEFGKNVLSVIPVFEQ
DSKQVTKVLFELTDGERIEAVGLKYKQGWESFCISSQCGCGFGCRFCATGSIGLKRNLTADEITDQLLYF
YLNGHRLDSISFMGMGEALANPELFDALKILTDPNLFGLSQRRITISTIGIIPGIQRLTQEFPQVNLTFS
LHSPFESQRSELMPINKRFPLNEVMKTLDEHIRHTGRKVYIAYIMLEGVNDSKEHAEAVVGLLRNRGSWE
HLYHVNLIPYNSTDKTPFKFQSSSAGQIKQFCSTLKSAGISVTVRTQFGSDISAACGQLYGNYENEL
>gnl|CDD|237718 PRK14461, PRK14461, ribosomal RNA large subunit methyltransferase N; Provisional
MHNAMEQRNLYDLNLAELTELLTAWGQPAFRARQLYRHLYVNLADSVLAMTDLPLALRERLTAELPLSTL
RLEQVQIGDNGLTRKALFRLPDGAVVETVLMIYPDRATVCVSTQAGCGMGCVFCATGTLGLLRNLSSGEI
VAQVIWASRELRAMGAAISKRHAGPVGRVTNLVFMGMGEPFANYDRWWQAVERLHDPQGFNLGARSMTVS
TVGLVKGIRRLANERLPINLAISLHAPDDALRSELMPVNRRYPIADLMAATRDYIAKTRRRVSFEYVLLQ
GKNDHPEQAAALARLLRGEAPPGPLLVHVNLIPWNPVPGTPLGRSERERVTTFQRILTDYGIPCTVRVER
GVEIAAACGQLAGRHTLPVNT
>gnl|CDD|184691 PRK14464, PRK14464, RNA methyltransferase
MRIQDLRQRLRALGAKPCHEGRILRAWLQGLPLDTRRQRAEDFLPLALREALPALEAELDGLARLRSEHP
GEDGSARLLVELADGQMVESVLLPRDGLCVSTQVGCAVGCVFCMTGRSGLLRQLGSAEIVAQVVLARRRR
AVKKVVFMGMGEPAHNLDNVLEAIDLLGTEGGIGHKNLVFSTVGDPRVFERLPQQRVKPALALSLHTTRA
ELRARLLPRAPRIAPEELVELGEAYARATGYPIQYQWTLLEGVNDSDEEMDGIVRLLKGKYAVMNLIPYN
SVDGDAYRRPSGERIVAMARYLHRRGVLTKVRNSAGQDVDGGCGQLRARAAKAAAVRRIRRRQA
>gnl|CDD|172945 PRK14470, PRK14470, ribosomal RNA large subunit methyltransferase N; Provisional
MLHLSGQDSRALARPAGISLEDARRITGAVIGRGAPLRSARNVRRSVLDEVDALATPGELRLVERVDAKD
GFRKYLFELPDGLRVEAVRIPLFDTHHVVCLSSQAGCALGCAFCATGKLGLDRSLRSWEIVAQLLAVRAD
SERPITGVVFMGQGEPFLNYDEVLRAAYALCDPAGARIDGRRISISTAGVVPMIRRYTAEGHKFRLCISL
NAAIPWKRRALMPIEQGFPLDELVEAIREHAALRGRVTLEYVMISGVNVGEEDAAALGRLLAGIPVRLNP
IAVNDATGRYRPPDEDEWNAFRDALARELPGTPVVRRYSGGQDEHAACGMLASRRR
>gnl|CDD|184695 PRK14471, PRK14471, F0F1 ATP synthase subunit B; Provisional
MDLLTPDFGLFFWQTILFLILLLLLAKFAWKPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLK
EARAERDAILKEAREIKEKMIADAKEEAQVEGDKMIEQAKASIESEKNAAMAEIKNQVANLSVEIAEKVL
RKELSNKEKQHKLVEKMLGDVKLN
>gnl|CDD|172947 PRK14472, PRK14472, F0F1 ATP synthase subunit B; Provisional
MLTSGIILLSGGLLSPNPGLIFWTAVTFVIVLLILKKIAWGPILSALEEREKGIQSSIDRAHSAKDEAEA
ILRKNRELLAKADAEADKIIREGKEYAEKLRAEITEKAHTEAKKMIASAKEEIEQEKRRALDVLRNEVAD
LAVKGAEKIIRTSLDADKQKKVVDSMIQDLSTKRN
>gnl|CDD|172948 PRK14473, PRK14473, F0F1 ATP synthase subunit B; Provisional
MEKLGINLGLLIAQLINFLLLIFLLRTFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELA
KARQEAAKIVAQAQERARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVL
GAELQARGHDALIAESLAALGRRN
>gnl|CDD|184696 PRK14474, PRK14474, F0F1 ATP synthase subunit B; Provisional
MLIDWFTVVAQIINFLILVYLLRRFLYKPIIQVMKKRQQRIANRWQDAEQRQQEAGQEAERYRQKQQSLE
QQRASFMAQAQEAADEQRQHLLNEAREDVATARDEWLEQLEREKQEFFKALQQQTGQQMVKIIRAALADL
ANATLEQQIVGIFIARLEHLSEAERQALANSNTTPEMLRIRTSFELSQDLRAQILESLHQTHLIPGTDIH
FVTSPELICGIELKTEGYKIAWTLAEYLDALESQLTTVLA
>gnl|CDD|184697 PRK14475, PRK14475, F0F1 ATP synthase subunit B; Provisional
HQSFFNLSNPEFWVGAGLLIFFGILIALKVLPKALAGALDAYAAKIQAELDEAQRLREEAQALLADVKAE
REEAERQAAAMLAAAKADARRMEAEAKEKLEEQIKRRAEMAERKIAQAEAQAAADVKAAAVDLAAQAAET
VLAARLAGAKSDPLVDAAIGQMGAKLQ
>gnl|CDD|172952 PRK14477, PRK14477, bifunctional nitrogenase molybdenum-cofactor biosynthesis protein NifE/NifN; Provisional
MAKPDYYDEPDCETHEKGAPKFCKKSEPGEGAERSCAYDGARVVLMPITDVIHLVHGPIACAGNSWDNRG
ARSSGSQLYRRGFTTEMLENDVIFGGEKKLYRAILELAERYQPKAVFVYATCVTALTGDDVEAVCKAAAE
KVGIPVIPVNTPGFIGDKNIGNRLAGEALLKHVIGTAEPEVTTPYDINLIGEYNIAGDLWGMLPLFDRLG
IRVLSCISGDAKFEELRYAHRAKLNVIICSKSLTNLARKMEKRYGIPYLEESFYGMTDTAKALRDIAREL
DDAGGGLEKRVLQDRVEKLIAEEEAKCRAALAPYRARLEGKRVVLFTGGVKTWSMVNALRELGVEVLAAG
TQNSTLEDFARMKALMHKDAHIIEDTSTAGLLRVMREKMPDLIVAGGKTKFLALKTRTPFLDINHGRSHP
YAGYEGMVTFARQLDLTVNNPIWPALRAPAPWEKGAGELRADLALAAGHAARFLAEDLKASRVKVPTKAA
TVNPQKNSPALGATLAYLGIDGMLPLLHGAQGCSTFIRLQLSRHFKESIALNTTAMSEVTAIFGGWENLK
QGILRVIEKFKPKVIGVMTTGLTETMGDDVRSAIVQFREEHPELDDVPVVWASTPDYCGSLQEGYAAAVE
AIVATLPEPGERIPGQVNILPGAHLTPADVEEIKEIVEAFGLDPVVVPDISNALDGHIDETVSPLSTGGT
TVEDIRAAGRSAATLAVGDSLARAAEKLQERFGIPAYGFTSLTGLKEVDRFMATLSALSGRPVPEKLRRW
RSRLMDAMVDSHYQFGGKKVALALEPDLLKALTSFLAGMGCEIQAAVAATRSRGLDRLPAENVFVGDLED
LETAAAGADLLVANSNGRQAAARLGIKAHLRAGLPVFDRLGAHQKMWVGYRGTMNLLFEVANLFQANAKE
AQKLAHN
>gnl|CDD|237723 PRK14479, PRK14479, dihydroxyacetone kinase; Provisional
MKKLINDPSTFVEEMLEGFVAAHPDLVRLVPGGVVRRTPTPEGKVAVVSGGGSGHEPAFAGYVGPGMLDA
AVCGNVFTSPSADQVYAAIRAADGGAGVLLIVGNYAGDVMNFGLAAELARAEGIDVRTVVVTDDVASAPS
GETAGRRGIAGTVLVFKIAGAAAEAGLDLDEVAAIARKANARTRSMGVALDGCTLPGAGEPLFTLPEGEM
ELGLGIHGEPGIEREALPTADELADRLVDRILADLPLGAGERVAVLVNGLGATPYEELFVVYGAVARLLA
ARGITVVRPEVGEFVTSLDMAGASLTLMKLDDELEELWDAPADTPAFRRGGAVEPVEYVEAAEEDDAEEP
PRASKASRATAANLVAALDAVAEALIDNEDELGELDAVAGDGDHGIGMARGSKAALAAARAAVEAGAGAG
SVLAAAGDAWADHAGGTSGPLWGTALRAAGKALGDKDEPTAADFAAAVRAAVDAIQELGGAQVGDKTMVD
ALVPFADALEAAAAAGADLAEAWAAAAEAAEEGAEATADLVPRMGRARYLGERSLGTPDAGAVSLALIFT
AIAGSLKD
>gnl|CDD|237724 PRK14481, PRK14481, dihydroxyacetone kinase subunit DhaK; Provisional
MKKLINDPETVVDEMLEGLVAAHPDLVTRIDDTDVIVRKDKPPGKVALVSGGGSGHEPAHAGFVGEGMLD
AAVCGAVFTSPTPDQILEAIKAVDTGAGVLLIVKNYSGDVMNFEMAAELAEMEGIEVASVVVDDDVAVED
SLYTQGRRGVAGTVFVHKIAGAAAEAGASLDEVKALAEKVNPNIRSMGVALSPCTVPAVGKPGFDLGDDE
IEIGIGIHGEPGRRREKLKPADEIAEELLEKILEDLKLVAGDEVLVLVNGMGATPLMELYIVYNDVAELL
EERGVTVARSLVGNYMTSLDMAGFSITLLKLDDELLELLDAPVDTPALRWG
>gnl|CDD|172956 PRK14483, PRK14483, DhaKLM operon coactivator DhaQ; Provisional
MKKIMNDVQNIVQDMLHGFYFAHPNLDETNNIPYVYDIEKDDQLVPIISGGGSGHEPAHIGYVGKGMLTA
AVNGSIFTPPTAEQILAATRLVPKGKGVFFIIKNFEADVAEFSAAIQIARQEGRQIKYIIVHDDISVEDD
ASFNKRRRGVAGTVLLHKILGAAALEGASLDELEQLGLSLTENIATLGVALSPANLPVAGLPSFDLNEDE
ISYGIGIHGEPGYRKEPFSSSEILAIELVNKLKSKYRWQKGDNFILLINGLGATTLMEQYIFANDIRRLL
ELEGLQITFVKVGTLLTSLDMKGISLTLLKVKDPDWLDWLKAPTRAAAW
>gnl|CDD|184702 PRK14484, PRK14484, phosphotransferase mannnose-specific family component IIA; Provisional
MVGIVIVSHSKKIAEGVKDLIKQMAPDVPIIYAGGTEDGRIGTSFDQIQEAIEKNESDGVLIFFDLGSAE
MNAEMAIEMLDGEKKIIIIDAPIVEGAFTAAVLLSAGASLDEILAELKELSINK
>gnl|CDD|184703 PRK14485, PRK14485, putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional
MELEQFYYDNKIVRKFLIATIIWGIVGMLVGLLVALQLVFPNLNFGISWLTFGRLRPLHTNAVIFAFVGN
AIFAGVYYSTQRLLKARMFSDLLSKIHFWGWQLIIVSAAITLPLGFTTSKEYAELEWPIDIAIALIWVVF
GVNFFGTLIKRRERHLYVAIWFYIATIVTVAVLHIVNSLELPVSALKSYSVYAGVQDALVQWWYGHNAVA
FFLTTPFLGLMYYFVPKAANRPVYSYRLSIIHFWSLIFIYIWAGPHHLLYTALPDWAQNLGVVFSVMLIA
PSWGGMINGLLTLRGAWDKVRTDPVLKFFVVAITFYGMATFEGPMLSLKNVNAIAHYTDWIIAHVHVGAL
GWNGFLTFGMLYWLLPRLFKTKLYSTKLANFHFWIGTLGIILYALPMYVAGFTQGLMWKEFTPDGTLAYP
NFLETVLAIRPMYWMRAIGGSLYLVGMIVMAYNIIKTVRAGSAVENELAEAAPLTKVYHPRASGEKWHRW
LERKPIQLTVLTTIAILIGGMVEIIPTFLVKSNVPTIASVKPYTPLELEGRDLYIREGCYNCHSQMIRPF
RSEVERYGEYSKAGEFVYDHPFLWGSKRTGPDLAREGGKYPDSWHYNHMEDPQSTSPGSIMPAYPWLLEN
ELDISDTPAKIKAMQTLGVPYTDGYEENAQADLREQAEAIAADLAADGFKVAPDKEIVALIAYLQRLGTD
IKVKETSEAKSS
>gnl|CDD|184704 PRK14486, PRK14486, putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional
SESSIYRKPVVFLLLATVTVLAGTIATMAYPMFRNDMHPKVEGLKPYTPLELAGRDVYQREGCVNCHTQT
VRPLKSEVVRYGQYSKAGEFAYDHPFLWGSKRTGPDLARIGGKYPDAWHYAHFEDPQAVVPRSNMPAYAF
LKGKPLDAALTQRKMRALGFPYTDADLAALAGKTEMDAMVAYMQSLGKAIPRRAAGGAEVDLELPNPFAT
DVAAIAKGKALYDANCAACHGDEAQGQEGVALNDIDDGDLPDAAYFGMIKGGSDAKGMPGFGGDLSDDDI
WAIVAYIRSQKAHE
>gnl|CDD|237725 PRK14487, PRK14487, cbb3-type cytochrome c oxidase subunit II; Provisional
KHEILEKNPGLLAVLTLLVVSIGGLVEIVPLFFQKSTTEPVEGVRPYTALELAGRDIYIREGCYNCHSQM
IRPFRAETERYGHYSLAGESVYDHPFLWGSKRTGPDLARVGGRYSDEWHRNHLINPRSVVPESNMPAYPW
LAENDLDGTDTAEKMTALRVVGVPYTDEDIAGAKAAVKGKADPIADDGDPGEITEMDALIAYLQSLGTAV
KFKRYDA
>gnl|CDD|237726 PRK14488, PRK14488, cbb3-type cytochrome c oxidase subunit I; Provisional
QANSPTEYNYKVVRQFAIATVVWGIVGMLVGVLIAAQLAWPELNFDLPWLTFGRLRPLHTNAVIFAFGGS
ALFATSYYVVQRTCQARLFSDFLAWFTFWGWQLVIVLAAITLPLGYTQSKEYAELEWPIDILITIVWVAY
AVVFFGTIAKRKEPHIYVANWFYGAFILTIAMLHIVNNLAVPVSLFKSYSAYSGVQDAMVQWWYGHNAVG
FFLTAGFLGMMYYFVPKQAGRPVYSYRLSIVHFWALIFLYIWAGPHHLHYTALPDWAQTLGMVFSLILLA
PSWGGMINGLMTLSGAWHKLRTDPILRFLVVALAFYGMSTFEGPMMSIKTVNALSHYTDWTIGHVHSGAL
GWVGMISIGALYHLIPRLWGRERMYSLKLVNWHFWLATIGIVLYIASMWVAGIMQGLMWRAVDEDGTLTY
SFVETVEAMHPYYVIRALGGLLFLSGMLIMAYNVWKTIRAGKALPAAAAPAAA
>gnl|CDD|237727 PRK14489, PRK14489, putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional
MQISQIAGVILAGGLSRRMNGRDKALILLGGKPLIERVVDRLRPQFARIHLNINRDPARYQDLFPGLPVY
PDILPGFQGPLSGILAGLEHADSEYLFVVACDTPFLPENLVKRLSKALAIEGADIAVPHDGERAHPLFAL
YHRSCLPALRRYLAEGERRLFDFFQRQRVRYVDLSTQKDAFFNVNTPEDLEQLRAIPDGTTTGAPPLLGV
VGYSGTGKTTLLEKLIPELIARGYRIGLIKHSHHRVDIDKPGKDSHRLRAAGANPTMIVCPERWALMRET
PEEAVPFKVLIATFDPEEVDLILVEGFKHEPLPKIQLHRQLISKPLPELDLWTIATATDYPLARDPRLDI
NDVKQIADFVRQWLLG
>gnl|CDD|237728 PRK14490, PRK14490, putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional
MLFHPFEIAFCGYSGSGKTTLITALVRRLSERFSVGYYKHGCHRFDIDREGKDSDLARKAGASTVMISDP
EKHALIAGGPPDPLLERGAFLDCDLLLVEGLKELPLPKILLVDRERKILDLLEQGSVTNVVALVVPDDPA
SYPDFGLPVFHRDDIAAIADFIEGHLLGRAEEVPLSGLVLAGGRSSRMGSDKALLSYHESNQLVHTAALL
RPHCQEVFISCRAEQAEQYRSFGIPLITDSYLDIGPLGGLLSAQRHHPDAAWLVVACDLPFLDEATLQQL
VEGRNPFRFATAFRHPDSGRPEPLCAIYEPKSRLRLLLRHAAGNNSLRSFLATSRIEELEPTDPEALQNI
NDPEEMDRAERALSTTKEN
>gnl|CDD|237729 PRK14491, PRK14491, putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
STPFTNPLSIPLLGFCAYSGTGKTTLLEQLIPELNQRGLRLAVIKHAHHNFDVDQPGKDSYRLRKAGASQ
MLVASRVRWALMTETPRDGEPELPHLLKQIDADKVDIVLVEGFKKLALPKIELHRAAHGKPWIYPHDENI
IAIACDDTPLPSELPRLDINDVAAIADFVLEYAQNWQAPAQDLPLAPACCCDLLSPAFLSVSQGLDKILS
LVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPESYTLVGEVLAGHQYDGTL
QAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPE
QGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSE
AALEATLEQAAAQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGN
PVAVMVSFLQFVEPALRKLAGEQNWQPLLFPAIADETLRSRQGRTEFSRGIYHLGADGRLHVRTTGKQGS
GILSSMSEANCLIEIGPAAETVNAGETVTIQPLAGLL
>gnl|CDD|237730 PRK14493, PRK14493, putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoaE; Provisional
MKVLSIVGYKATGKTTLVERLVDRLSGRGRVGTVKHMDTERLNPDGTDTGRHFDAGADVVYGLTDGEWVA
SGRDRSLDDALDDLAPGMDYAVVEGFKDSRLPKVVLGDMDADSDVVARAPTAADLDTEDLVAALESQPPY
VTLESLVAKVKRSPDADKAGAIATFTGRVRAKEDADDEPTEYLEFEKYDGVADERMAAIREELKQRDGVF
EVLLHHRTGVIEAGEDIVFVVVLAGHRQEAFRAVSDGIDRLKDEVPIFKKEVTVDEEFWVHDRE
>gnl|CDD|237731 PRK14494, PRK14494, putative molybdopterin-guanine dinucleotide biosynthesis protein MobB/FeS domain-containing protein protein; Provisional
MRAIGVIGFKDSGKTTLIEKILKNLKERGYRVATAKHTHHEFDKPDTDTYRFKKAGAEVVVVSTDETAAF
LYDRMDLNEILSLLDADFLLIEGFKELLNIPKILCLRDAEGVELLDDGTALAIDDFKYGTEEIDELADLV
LERAFVLPYNLNCGHCGFNCKGFAKAIVKGEAKWDDCVSLSGRVKLIVDGKIIPLNPFVQEIVENTIKGM
LSALKGYENPKKIEIIIDD
>gnl|CDD|172967 PRK14495, PRK14495, putative molybdopterin-guanine dinucleotide biosynthesis protein MobB/unknown domain fusion protein; Provisional
MRVYGIIGWKDAGKTGLVERLVAAIAARGFSVSTVKHSHHDVDPDPPGSDSHRHRAAGAAEVVLAGPRRL
ILTREHRGEPPRLAAILERMAPVDLVLVEGYKTEPHPKIEVFRKAAGHALRQPEDPWVRAVASDTQMALP
VPVLDLDDTEAVADFLLTDSGLVRSGFDTVIAVDWSGASVPSPRKPSSDAIWIGVASPLGETVSYHRTRA
DAEAHLNDLFAFELTAGRRVLAGFDFPFGYPEGFAPRLTGQAFAPALWDWLEARIEDGPDNANTRFQFAD
RINAGFPGQGPFWGRPGGLALDHLPDRKLCDHEALGIAERRRVEQAVPKAHPVWKLYTTGSVGSQALLGL
PVIARLRRRFHAQAWPFEPATGPIVLAEIYPSLLGPAISKATREGEIKDSAQVRLMARALWRMARDGSLA
ALLADVPDWPGRAEEGWILGAGQAEQLRLALI
>gnl|CDD|172968 PRK14497, PRK14497, putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
MRVFVGDESLYSIDEAIKVFLSSLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSC
TPGEFKVIDKIGIGEFKEIHIKECEAVEVDTGSMIPMGADAVIKVENTKVINGNFIKIDKKINFGQNIGW
IGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHY
LYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGTSAGEKDFVHQAIRELGNIIVHGLKI
KPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLYPSRKEILGLGKIKARLALRVKADEHRNT
LIPVYLFKSDNSYYALPVPFDSYMVGTFSLTDGYIMLGPNEEIEEGKEVEVDLKKLDDRPSIIGEEDKRI
LNLDTRNVLLGSLPASKAIKYKFGDVAVISSLFTEPIENYDKVLCRQILVNGEGEEIGYDDWIGMSKIVK
NPVVKLKSPSTIYSLVGKAKVIAPEGYIVGDKVAEEKLYMIGISERGKRYLSGIKV
>gnl|CDD|237732 PRK14498, PRK14498, putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
MKRKIFLTLVSLEEAREILESLLSELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAAD
TFGASEANPVRLKLGGEVHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVA
PGENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKI
YDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVLLSGGTSAGAGDVTYRVIEELGEV
LVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLRKLAGLPPPERATVKARLARRVRSE
LGREEFVPVSLGRVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTEGLEAGEEVEVELFGPLVEPPTLV
IIGSHDPGLDLLLDLLARRGLRLRSLHVGSMGGLMALKRGEADIAGIHLLDPETGEYNIPYIKKYLLGED
AVLVKGYRREQGLVVRKGNPKGIEGIEDLVRKDVRFVNRQRGSGTRILLDYHLKELAIDPERINGYDREE
KTHMAVAAAVAQGRADAGLGIRAAAKALGLDFIPLAEEEYDLLIPKERLEKPAVRAFLEALKSPEFKAAL
EEL
>gnl|CDD|237733 PRK14499, PRK14499, cyclic pyranopterin monophosphate synthase MoaC/MOSC-domain-containing protein
MEFTHFNKDGLPQMVDVSSKEPTFRVAVASGRIYVGKEVIEAIEERLLPKGDVFSVAKIAAIMAAKKTSE
LIPLCHNIFLSGVDVSYEINREEGYIEAVSEVKTEAKTGAEMEAITAVSIFLETIYDMCKAVKKDMVITD
VRLIEKSGGKSGHYIFERRNKTAKVVSINISRQKGTPKEPVEEAVLIENHGIEGDAHAGTWHRQVSLLDI
SSIKKMEEYGLKGLCFGKFAENITTENLDLQKISLGTKLKIGDNVVLEISQIGKKCHGSGCEIARQVGVC
IMPKEGLFAKVLKGGKIKPGDIIEILNN
>gnl|CDD|237734 PRK14500, PRK14500, putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; Provisional
MFTHLNENQQPRMVDISQKVVSDRRAVAQAIVQLPPAIKDYVTGQDIFLKKGPVIQTAIIAGTMAVKRTA
DLIPFCHTLPIHGCKFDINIVYQKRDLEIFLQCAVKTNYKTGVEMEALCGVAVAALTIYDMCKSISPHII
IKETRLIEKSGGKADLSQTPLYGLVLTGGKSRRMGKDKALLNYQGQPHAQYLYDLLAKYCEQVFLSARPS
QWQGTPLENLPTLPDRGESVGPISGILTALQSYPGVNWLVVACDLAYLNSETVEKLLAHYRQDLVATCYE
NPDQGFPEALCAIYTPQALQVFEKAYAEGLYCPVKILQRAPCQLIKPDNLFDIANINTPEEYGQIN
>gnl|CDD|184712 PRK14501, PRK14501, putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
SRLIIVSNRLPVTVVREDGGVELTPSVGGLATGLRSFHERGGGLWVGWPGLDLEEESEEQRARIEPRLEE
LGLVPVFLSAEEVDRYYEGFCNSTLWPLFHYFPEYTEFEDRFWESYERVNQRFAEAIAAIARPGDVVWVH
DYQLMLLPAMLRERLPDARIGFFLHIPFPSFEVFRLLPWREEILEGLLGADLIGFHTYDYVRHFLSSVLR
VLGYETELGEIRLGGRIVRVDAFPMGIDYDKFHNSAQDPEVQEEIRRLRQDLRGRKIILSIDRLDYTKGI
PRRLLAFERFLEKNPEWRGKVRLVQVAVPSRTGVPQYQEMKREIDELVGRINGEFGTVDWTPIHYFYRSL
PFEELVALYRAADVALVTPLRDGMNLVAKEYVASRTDGDGVLILSEMAGAAAELAEALLVNPNDIEGIAA
AIKRALEMPEEEQRERMQAMQERLRRYDVHKWASDFLDELREAAEKNKAFASKPITPAAAEEIIARYRAA
SRRLLLLDYDGTLVPFAPDPELAVPDKELRDLLRRLAADPNTDVAIISGRDRDTLERWFGDLPIHLVAEH
GAWSRAPGGEWQLLEPVATEWKDAVRPILEEFVDRTPGSFIEEKEASLAWHYRNADPELGEARANELILA
LSSLLSNAPLEVLRGNKVVEVRPAGVNKGRAVRRLLEAGPYDFVLAIGDDTTDEDMFRALPETAITVKVG
PGESRARYRLPSQREVRELLRRLLDI
>gnl|CDD|184713 PRK14502, PRK14502, bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; Provisional
MRIESLRPAEHLGNVTIHGVRRFLELDSGAPNLPHLQESREVEMVDQQAISDVEKKMAIVLPIKDEDLKV
FEGVLSGIPHDCLMIVISNSSKQEVDNFKNEKDIVNRFCRITHRQAIVVHQKNPELANAIADAGYPELLG
EDGLIRSGKAEGMILGIILTMFSGRDYVGFIDTDNYIPGAVWEYAKHFATGFNLAQSPYSMVRILWKYKP
KLVGDLYFKRWGRVSEVTNKHLNHLISSKGKFETEIIKTGNAGEHAMSIELAKRLTYGTGYAVETKEIMS
ILEQFSGILPIEDREVAEEGVEILQTETINPHLHEDKGGDHLLQDMLLPSLAVIYHSPLADEAGRKMIET
QLAGIEGLESGPEIPQIKLIPPPQKMDLPKFSAIIEKYLPQMVLPDGELISRAARPSRLPSSGQFKKIVY
TDLDGTLLNPLTYSYSTALDALRLLKDKELPLVFCSAKTMGEQDLYRNELGIKDPFITENGGAIFIPKDY
FRLPFAYDRVAGNYLVIELGMAYKDIRHILKKALAEACTEIENSEKAGNIFITSFGDMSVEDVSRLTDLN
LKQAELAKQREYSETVHIEGDKRSTNIVLNHIQQSGLEYSFGGRFYEVTGGNDKGKAIKILNELFRLNFG
NIHTFGLGDSENDYSMLETVDSPILVQRPGNKWHKMRLRNPSYVKGVGPEGFSRAVTDIILPME
>gnl|CDD|172976 PRK14505, PRK14505, bifunctional photosynthetic reaction center subunit L/M; Provisional
MSAVPRALPLPSGETLPAEAISSTGSQAASAEVIPFSIIEEFYKRPGKTLAARFFGVDPFDFWIGRFYVG
LFGAISIIGIILGVAFYLYEGVVNEGTFNILAMRIEPPPVSEGFNIDPAKPGFFWFLTMVAATIAFIGWL
LRQIDISLKLDMGMEVPIAFGAVVSSWITLQWLRPIAMGAWGHGFPLGITHHLDWVSNIGYQYYNFFYNP
FHAIGITLLFASTLFLHMHGSAVLSEAKRNISDQNIHVFWRNILGYSIGEIGIHRVAFWTGAASVLFSNL
CIFLSGTFVKDWNAFWGFWDKMPIWNGIGQGALAAGLALLGVGLVLGRARETPEPIDLHDEEYRDGLEGT
IAKPPGHVGWMQRLLGEGQVGPIYVGLWGVISFITFFASAFIILVDYGRQVEWNAIIYLREFWNLAVYPP
PTEYGLSWNVPWDKGGAWLAATFFLHISVLTWWARLYTRAKATGIGTHLAWGFASALSLYFVIYLFHPLA
LGNWSAAPGHGFRAILDWTNYVSIHWGNFYYNPFHMLSIFFLLGSTLLLAMHGATIVATSKWKSEMEFTE
MMAEGPGTQRAQLFWRWVMGWNANSYNIHIWAWWFAAFTAITGAIGLFLSGTLIPDWYAWGESAKIVAPM
PNLDYWWAQFIFR
>gnl|CDD|237737 PRK14507, PRK14507, malto-oligosyltrehalose synthase
SASNVSGLERLCDLVGIALGYTDAWGKRVDTPLDVRRALLAALGVPAADEEEARASLAAVEAVRAGVLPP
LLVVEAWAPRRALRVPVRVTGGALRWRLVDEHGTEREGRATPAALEEGAGFDLPRTLVLAIPLTPGYHRL
TVTVGDLRAEAWVIAAPQRCWRPPALAEGARDWGLAAQLYGLRSARNWGIGDFGDLGRLVRDAALRGASF
LGLSPLHALFPTDPAKASPYSPSSRLFLNTLYIDVEAVPDFAECEAARLLVHAPEFQARLEALRAAELVD
YAGVAEAKFEVLEALWRHFRARHLERNTGRDAGFRAFRAEGGESLRSHALFEALQEHFRAEDAHWWGWPD
WPEAYRDPGTPAVRAFAEEHAERVEYHEYLQWLADLQLAAAGERAQALGMRLGLYRDLAVGVDRGGSETW
SHPELFANGASIGAPPDELNPKGQDWGLPPFDPLELERDGYAPFRALLRANMRHAGALRIDHVMQLMRLF
WIPLGRSAREGAYVAYPFEPMLAVLALESHRNRCLVIGEDLGTVPEGFRDALARAGVLSYRILYFEREDG
GAFKPPAAYPADALAAVTTHDLPTLVGWWRGVDTDLRQSLGLYPDAERAEAQRTERVAERRRLLEALAAE
GLLPSGEPPDAAPFPELTAELAEAVARYLARAPSALTAVQLEDVLGELEQANVPGTTEGYPNWRRKLDRN
LEAIAAPPRLQAVGGALAKLRPRLSAEERGPRSGAARLAAAPPRATYRLQFHKDFTFADAEAILPYLAAL
GISHVYASPILKARPGSTHGYDIVDHSQINPEIGGEEGFERFCAALKAHGLGQLLDIVPNHMGVGGADNP
WWLDVLENGPASPAADAFDIDWEPLGAELRGKVLLPVLGDRYGEVLEKGELELKFDPEAGAFSVWYYEHR
FPIDPLSYPRILNRALAALGEAGDDMSAELLSLSEALRHLPPRDETDPERRAERPRDKELLKRRLAELVA
ASPQLAAAIARALALLNGNRGEPDSFDALHRLLEAQAYRLAHWRVAADDINYRRFFDINSLAALRMERPD
VFEATHALLFRLIAEGRIDGLRIDHPDGLADPAGYFRRLQAAVGAGPGPAGRPPPGLYIVVEKILAPGEK
LPRDWPVHGTTGYDFANQVNGLFVDTAAAPAFERIYRWFTGEDEDYGEQLRAAKAEIMETSLASELEVLA
GDLKRIADADRRTRDFTRNALRRALAEIVARFPVYRTYLPPTEVSAEDVRYIEGAVRKAKRRSRLPDRSV
HDFVRDVLLGRIDLGGAGHPLRQLVLRFRRRFQQFTAPVMAKSLEDTLFYRYVRLVSLNEVGGDPGEFGL
DAEHFHALNAARARDWPHAMLATSTHDTKRSEDVRARILVLSEMPEEWRLALDRWRRLNEPHRKRVEGEP
APSPNDEYLLYQALLGAWPLELDDAGALADLRERLDAYMEKAAREAKRHSSWVNPDEGYEAAVAGLVRAL
LSPGSDFLRDLRPFVRRLAWFGMINSLGRTLLKLTLPGVPDTYQGTEFWDFSLVDPDNRRPVDYAARARA
LEALGAMHAEGGHAACPDALLGSWQDGRIKLAVLWRLLADRRARPALFRDGDYRPLKAEGARAEHVVAFA
RRRGGDDLVVAVPRLVARLAGEDGELPWSAEAWAGTVVPLVLPAGSRWVDVLTGRELAAEGGGLDLGRLF
ARLPYAVLRRATA
>gnl|CDD|237738 PRK14508, PRK14508, 4-alpha-glucanotransferase; Provisional
MMMKRKSGILLHITSLPGSYGIGDFGKGAYEFIDFLAEAGQSYWQILPLGPTGYGDSPYQSFSAFAGNPL
LIDLEALVDDGLLDESDLEGLPFGSNPERVDYDLVREAKRPLLRKAFERFLRASLERAEAFEAFCEEEAY
WLDDYALFMALKEHFGGLPWNEWPEPLRKRDPEALAKAREELADEILYHKFLQYLFFRQWKALKAYANDK
GIEIIGDLPIYVAYDSADVWANPELFKLDEDGKPTVVAGVPPDYFSETGQLWGNPVYNWDALRKDGYRWW
IERLRRSFKLYDIVRIDHFRGFEAYWEIPAGEKTAINGRWVPGPGKDLFEAVKEELGDLPIIAEDLGVIT
PDVEELRDRFGFPGMKILQFAFDGDSDNPYLPHNYPRNSVVYTGTHDNDTTVGWWESLDPEERKRVADYL
GRSSEEEIHWALIRLALASVADLAILPMQDLLGLGSEARMNTPGTVGGNWSWRLLPDDLTDDLADRLREL
TELYGRA
>gnl|CDD|237739 PRK14510, PRK14510, bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase
VLMSHNSVSPGFREPLGAVPDGGGVNLALFSGAAERVEFCLFDLWGVREEARIKLPGRTGDVWHGFIVGV
GPGARYGNRQEGPGGPGEGHRFNPPKLLVDPYARPLDRPFWLHQAIFDDRFFNGDEDLTDSAVLVPKVVV
PTPFTWAPRSPLHGDWDDSPLYEMNVRGFTLRHDFFPGNLRGTFAKLAAPEAISYLKKLGVSIVELNPIF
ASVDEHHLPQLGLSNYWGYNTVAFLAPDPRLAPGGEEEFAQAIKEAQSAGIAVILDVVFNHTGESNHYGP
TLSAYGSDNSPYYRLEPGNPKEYENWWGCGNLPNLERPFILRLPMDVLRSWAKRGVDGFRLDLADELARE
PDGFIDEFRQFLKAMDQDPVLRRLKMIAEVWDDGLGGYQYGKFPQYWGEWNDPLRDIMRRFWLGDIGMAG
ELATRLAGSADIFPHRRRNFSRSINFITAHDGFTLLDLVSFNHKHNEANGEDNRDGTPDNQSWNCGVEGY
TLDAAIRSLRRRRLRLLLLTLMSFPGVPMLYYGDEAGRSQNGNNNGYAQDNNRGTYPWGNEDEELLSFFR
RLIKLRREYGVLRQGEFSSGTPVDASGGKDVEWLRRKGEQNQDRFWDKRSTEALVAVLNRPAGERQVDDR
FAVLLNSHHEELTLHLPENALELAAINTGEARASLAELLEPLSARALPVVMCLYPCTGVDIALVGAAAMV
DEALEFVIRYEDGHYFKQEVMGRACGILMHLYSLRSQRPWGIGDFEELYALVDFLAEGGQSLWGVNPLHP
LGLGDPERASPYQPSSRRAGNPLLISLDLLPEAGLLTENEAALGSAGPELAKLSALGSVDYAWVEALKEK
LLRAAYEAFRDKLPRYPLDLSSPEFDRFIEEGGDWLRRYAIFKALKAKFPGKGWHQWPEEYRLRKPPALE
AFAEKYAEEVNYAKFLQYIADRQWQAAKDYAQEQGLSIGFYGDLAIGVAPDGADAWAERSCFALDVSIGA
PPDYFNPEGQNWGLPPYDPRALRRDGYRWFIERIRANMRHAGALRIDHVRGLERLFEVPQGASAKEGAYL
KGPGEELFGQVALESQRAQCPVIGEDLGTIPSGVRELLAILGILSYRVLQFERLGEGNFLPPPLYNALAA
AYVGTHDLPTLAGWWEGVDLSEKEQLGAAEAVIEMLARSPAILVIIQLQDLLGSNVRMNLPGTIRENPNW
RRKLSAPVERLTLTQRACARLRGLAEKRGRL
>gnl|CDD|237740 PRK14511, PRK14511, malto-oligosyltrehalose synthase
AMRVPRATYRLQFHAGFTFDDAAELVPYFADLGVSHLYLSPILAARPGSTHGYDVVDHTRINPELGGEEG
LRRLAAALRAHGMGLILDIVPNHMAVGGPDNPWWWDVLEWGRSSPYADFFDIDWDSGEGKVLLPVLGDQY
GEVLAAGELRLAFDDDGAFVLRYYDHRFPIAPGTYALILRHRLDLEALAAEFPALGELESILTAAQHLAS
PAVRAFIEQALAAFDGRKGDGRSRLDRLLERQHYRLASWRVADDEINYRRFFDVNTLAAVRVEDPEVFEE
THALILRLLREGLVDGLRIDHPDGLADPRGYLRRLRRRTGRGAYIVVEKILEPGERLPEDWPVDGTTGYD
FLNQVNGLLVDPAGEEPLTELYARFTGRPADFDELVRQAKRLVLDGSLAGEVERLAQLLLRVARDDLRTR
DFTLGALRRALVELIAAFPVYRTYLPACGRSARDRQVIEQAAARARRRLPEADWPVLDFLEDVLLGRAAR
ELPRGRRKLRLEFAVRFQQLTGPVMAKGVEDTAFYRYNRLLSLNEVGGDPERFSASVEDFHAANAERLRR
FPHSMLTTSTHDTKRGEDVRARISVLSELPDEWAAAVERWRRLAAPLRGPAPDGNDEYLLYQTLVGSWPL
DDAAALPAYRERIRAYMLKALREAKVHTSWTAPNEEYEAAVLAFVDAALDDPEFRRDLAAFAARIAPAGA
LNSLAQTLLKLTSPGVPDVYQGTELWDFSLVDPDNRRPVDFAARAAALARLDEGAELLPWDDGRIKLLLI
ARALRLRRDRPELFAGGEYLPLEVSGPHAGHVLAFARGGGGGRALTVAPRLPAGLLGAGGWGDTRLVLPE
ILSGGRWRDLLTGEEVSGGELPLAELLGDFPVALLVRAS
>gnl|CDD|237741 PRK14512, PRK14512, ATP-dependent Clp protease proteolytic subunit; Provisional
MTDEKDDNKQTGIDKSLEKFLKSRSIVIAGEINKDLSELFQEKILLLEALDSKKPIFVYIDSEGGDIDAG
FAIFNMIRFVKPKVFTIGVGLVASAAALIFLAAKKESRFSLPNARYLLHQPLSGFKGVATDIEIYANELN
KVKSELNDIIAKETGQELDKVEKDTDRDFWLDSSSAVKYGLVFEVVETRLELEEFIS
>gnl|CDD|237742 PRK14513, PRK14513, ATP-dependent Clp protease proteolytic subunit; Provisional
MSVIPYVIEQTGRGERMYDIYSRLLKDRIIFVGTPIESQMANTIVAQLLLLDSQNPEQEIQMYINCPGGE
VYAGLAIYDTMRYIKAPVSTICVGIAMSMGSVLLMAGDKGKRMALPNSRIMIHQGSAGFRGNTPDLEVQA
KEVLFLRDTLVDIYHRHTDLPHEKLLRDMERDYFMSPEEAKAYGLIDSVIEPTRVKRGDQG
>gnl|CDD|184722 PRK14514, PRK14514, ATP-dependent Clp endopeptidase proteolytic subunit ClpP
MNDFRKYATKHLGMNAMVLDDVIKSQASYLNPYILEERQLNVTQMDVFSRLMMDRIIFLGTQIDDYTANT
IQAQLLYLDSVDPGKDISIYINSPGGSVYAGLGIYDTMQFISSDVATICTGMAASMASVLLVAGTKGKRS
ALPHSRVMIHQPLGGAQGQASDIEITAREIQKLKKELYTIIADHSGTPFDKVWADSDRDYWMTAQEAKEY
GMIDEVLIKKP
>gnl|CDD|237743 PRK14515, PRK14515, aspartate ammonia-lyase; Provisional
MATLTEVKNGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVG
RLELNKGGAIAEAAQEILDGKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSH
VNMAQSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAY
SRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEYIEAVVKHLAAISELPLVGAEDLVDATQNTDAY
TEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGND
HTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYVEKSVGIITAVNP
HIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHPGIAGATLLKKN
>gnl|CDD|184724 PRK14520, rpsP, 30S ribosomal protein S16; Provisional
MAVKIKLKRLGKIRNPQYRIVVADSRTKRDGRAIEEIGRYHPKEEPSLIEIDSERAQYWLSVGAQPTEPV
LALLKITGDWQKFKGLPGAEGTLKVAEPKPSKLELFNAALAEADGGPTAEATTPKKKKAAAEAAAAEAAA
PAAEAAAAAAAEEEA
>gnl|CDD|237744 PRK14521, rpsP, 30S ribosomal protein S16; Provisional
MAVKIRLQRHGRKGKAFYWIVAADSRAPRDGKFIEKIGTYNPNTNPATVDLNFDRAVYWLMNGAQPTDTA
RNILSYEGVLLKKHLLGGVAKGAFTEAQAEAKFEAWKEEKEGKVNAKKDKLSKAKKAAKKAALEAEKKVN
EARAEAVAEKKAAEAAAVAAEEAAAAEEEEAEEAPAEEAPAEESAE
>gnl|CDD|172988 PRK14522, rpsP, 30S ribosomal protein S16; Provisional
MALKIRLRQQGRRNHVVYRLVLADVESPRDGKYIELLGWYDPHSEQNYQLKSERIFYWLNQGAELTEKAG
ALVKQGAPGVYSELMAKKVARKAVVRQKRRAYRQRRSARRAEAAAK
>gnl|CDD|172992 PRK14526, PRK14526, adenylate kinase; Provisional
MKLVFLGPPGSGKGTIAKILSNELNYYHISTGDLFRENILNSTPLGKEIKQIVENGQLVPDSITIKIVED
KINTIKNNDNFILDGFPRNINQAKALDKFLPNIKIINFLIDEELLIKRLSGRRICKSCNNIFNIYTLPTK
EKGICDVCKGDLYQRKDDKEESLKTRLQEYKLQTKPLIEFYSKCNRLNNIDASKDIDEVKKKLIEIISKK
N
>gnl|CDD|237745 PRK14527, PRK14527, adenylate kinase; Provisional
MTQTKNKVVIFLGPPGAGKGTQAERLAQELGLKKLSTGDILRDHVARGTELGQRAKPIMEAGDLVPDELI
LALIRDELAGMEPVRVIFDGFPRTLAQAEALDRLLEELGARLLAVVLLEVPDEELIRRIVERARQEGRSD
DNEETVRRRQQVYREQTQPLVDYYEARGHLKRVDGLGTPDEVYARILKALG
>gnl|CDD|172994 PRK14528, PRK14528, adenylate kinase; Provisional
MKNIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAMGIEAKRYMDAGDLVPDSVVIGIIK
DRIREADCKNGFLLDGFPRTVEQADALDALLKNEGKSIDKAINLEVPDGELLKRLLGRAEIEGRADDNEA
TIKNRLDNYNKKTLPLLDFYAAQKKLSQVNGVGSLEEVTSLIQKEL
>gnl|CDD|237746 PRK14529, PRK14529, adenylate kinase; Provisional
MNILIFGPNGSGKGTQGALVKKKYDLAHIESGAIFREHIGGGTELGKKAKEYIDRGDLVPDDITIPMILE
TLKQDGKNGWLLDGFPRNKVQAEKLWEALQKEGMKLDYVIEILLPREVAKNRIMGRRLCKNDNNHPNNIF
IDAIKPDGDVCRVCGGELSTRADDQDEEAINKRHDIYYDTETGTLAAAYFFKDLAAKGSTKYIELDGEGS
IDEIKETLLKQLS
>gnl|CDD|237747 PRK14530, PRK14530, adenylate kinase; Provisional
MSQPRILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALRANKQMDISDMDTEYDTPGEYMDAGELVPDAV
VNEIVEEALSDADGFVLDGYPRNLEQAEYLESITDLDVVLYLDVSEEELVDRLTGRRVCPDCGANYHVEF
NQPEEEGVCDECGGELIQRDDDTEETVRERLDVFEENTEPVIEHYRDQGVLVEVDGEQTPDEVWADIQDA
IDDAT
>gnl|CDD|172997 PRK14531, PRK14531, adenylate kinase; Provisional
MKQRLLFLGPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEVAAGSALGQEAEAVMNRGELVSDALVLAIV
ESQLKALNSGGWLLDGFPRTVAQAEALEPLLEELKQPIEAVVLLELDDAVLIERLLARGRADDNEAVIRN
RLEVYREKTAPLIDHYRQRGLLQSVEAQGSIEAITERIEKVLA
>gnl|CDD|184729 PRK14532, PRK14532, adenylate kinase; Provisional
MNLILFGPPAAGKGTQAKRLVEERGMVQLSTGDMLRAAIASGSELGQRVKGIMDRGELVSDEIVIALIEE
RLPEAEAAGGAIFDGFPRTVAQAEALDKMLASRGQKIDVVIRLKVDDEALIERIVKRFEEQGRPDDNPEV
FVTRLDAYNAQTAPLLPYYAGQGKLTEVDGMGSIEAVAASIDAALEGV
>gnl|CDD|184730 PRK14533, groES, co-chaperonin GroES; Provisional
MKVIPLGERLLIKPIKEEKKTEGGIVLPDSAKEKPMKAEVVAVGKLDDEEDFDIKVGDKVIFSKYAGTEI
KIDDEDYIIIDVNDILAKIEE
>gnl|CDD|173000 PRK14534, cysS, cysteinyl-tRNA synthetase; Provisional
MLLKLYNTKTKDLSELKNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIG
HLTGDFDDGEDKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEEN
GFTYFVNGNVYFDTSCFKSYGQMAGINLNDFKDMSVSRVEIDKSKRNKSDFVLWFTNSKFKDQEMKWDSP
WGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIMEYEKM
SKSNNNFITIKDLEDQGFSPLDFRYFCLTAHYRTQLKFTFNNLKACKIARENMLNKLTYFYSSLDQFDLN
LLNKDLENIEFSLEKEYYDSFLEKIAFDLNIPQGLALLWDIIKDDNLSFLSKLRLAFKFDEVLSLGLREE
ILREIENHRIVIDDNMKSLIEERRLAKCEKDFKRADEIREYFASKGFVLIDTEEGTKVKRG
>gnl|CDD|173001 PRK14535, cysS, cysteinyl-tRNA synthetase; Provisional
MTTITEKRLTFAFPEDYYVTKYDEWEHYKIFQNSCNLRNKIDTNEKGKNGINQSVDDDNGSSGVDIIALH
ESTLWLIEIKDYYRLGLEPNAQSIDEKLSDLPYLIARKIRDSLAGLVSAKFKAEKQEEKDFSRLALDCNE
IKIVLHIEMPSIRSKLYPSSSDLANLLKDKFKLSEFTKNFANCYAEPIFTNISHINNPQLRNVPWSVSTG
TEQKLSSEQQRLIHNPMTTIYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWL
RECGYPLTYVRNITDIDDKIIARAAENGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAM
IETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSLDDLRAGERVEVDGFKRDPLDFVLWKAAKAGEPAW
ESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSVGATGHTCGHHHAQTHHGQSIA
SHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDAHLDDAKGALTR
LYTTLKNTPAAEFMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKTNDAQLAGCLKALGGIIG
LLQRDPTEFLQGGAASDGLSNEEIEDLIARRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTWRRG
>gnl|CDD|184731 PRK14536, cysS, cysteinyl-tRNA synthetase; Provisional
MALRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITD
VGHLTDDADSGEDKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLE
ARGHTYCAGGNVYFDIRTFPSYGSLASAAVEDLQAGARIEHDTNKRNPHDFVLWFTRSKFENHALTWDSP
WGRGYPGWHIECSAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKM
SKSAGQFLTLSSLQEKGFQPLDYRFFLLGGHYRSQLAFSWEALKTAKAARRSLVRRVARVVDAARATTGS
VRGTLAECAAERVAESRASESELLLTDFRAALEDDFSTPKALSELQKLVKDTSVPPSLCLSVLQAMDTVL
GLGLIQEATASLSAQVPAGPSEEEIGQLIEARAHARQTKDFPLADEIRDKLKAEGIELEDTHLGTIWKRV
>gnl|CDD|237748 PRK14537, PRK14537, 50S ribosomal protein L20/unknown domain fusion protein; Provisional
MAKISFTPARHRRRKKVLKMAKGYFGSKSTLYKTAHEQVMRSLQYAYRDRKQRKRDFRKLWISRINAGAM
LCGIKYSRLMHGLALAKVDINRKVLSDLAHLQPEVFVQYVELAKKFLSQFQSTTITKPKKVLINEVLQEK
TINQNEEKTSLQNEKVLSPELSEEKSDSELETQPQKTQLKEKKPSIEHIDLSKMLLKELKKLAKEHKIPN
FNKLKKTEIIKALKKALKKK
>gnl|CDD|173004 PRK14538, PRK14538, putative bifunctional signaling protein/50S ribosomal protein L9; Provisional
MFSKNKHKTKFIVIAIVIVVLILIFLCFDLQNIQEIIEQINQLTNNSGMRKKIIFFTFNFLGKIILAILI
ISFLLNIKKNAQIKRLQNKLSLWSKLSFHVSQIGEEVLNELPIGIVLIDISSKEIQWLNPYANFILKNPE
INTPLAQINESMAQLLLTSDKIPKTIITLKNQKFECFYKKDLNVFYLFNATEKEQIKHLFLQKTLALAMI
TFDNLEESLIRYDLSEQSQIQGEYLSALSDFIEPYEGYLKQLIDDRFLLLINRQNLDKMIENKFSILDTI
RNISHKYQLKVTLSMGIACWNLSYDKLATYSQNAIELAQKRGGDQAVVNIENEKIKYFGAKIASLSKQSK
VNARVNAQNLVDILKKNPHCFIMGHNHTDLDSLGSMIAFYKIALTIHPDNNNYIILDEEKLDKSLTPVYH
QLIKQEHKVTLNIITTQQASKMIKKNDLIAVLDTQTKDIVNSPELLSLTNNIIVIDHHRATEEIIPSIFS
YVDSSASSTVELLVELMGFLEKEIHITAFEASIMYAGILIDTNAFIYRTSSRTFEVASKLKDLGADAIEV
KSWLRKDFDKVLEINKLISKMEIFMDRFAIIKSEEIYDNRSFLAQVAESVLNIQNVDAAFMIAKISDNTI
AISARSYNEINVQTIMEQMEGGGHLNSAATQIKGTNIKTVTQTLKHLLKLEYEKGEKNMEIILLTDIKNK
GKKHEIIKVNNGYGNFLIQNKKALLADKENLAKIKKKKILEQEKKRNHELLMKKLKSEIDNKKITLDIQL
GPKGKIYGKITLKQIVEEFHKIHNITIDRKKISLENEIISVGIYPVDVFLTDQIKATFFLNVIERKSK
>gnl|CDD|184732 PRK14539, PRK14539, 50S ribosomal protein L11/unknown domain fusion protein; Provisional
MAKKEVVKVAKLQFNAGQAKPGPSLAGVGINMPEFTKQFNDATRDRGGEPVPVQITVYKDKSFDFKLFTA
PASFKIKQAAKIKSGSANSKTTIVGTITLSQLEEIAKYKLPDLNTDDVEEAMHTIAGTAKNMGVLVEGYD
DVVKAKEEAKAAAKAAALAKAKEASLKSAEAELKASKGKSIEVNVIGEEDEGEKDE
>gnl|CDD|184733 PRK14540, PRK14540, nucleoside diphosphate kinase; Provisional
EKERTFVALKPDAVERKLIGKIIQRFENKGFEIVEMKMLKLTREMAEEYYEEHKGKEFYERLINFMTSGR
IVAMVIEGENAISTVRKMIGKTNPAEAEPGTIRGDFGLYTPANIIHASDSKESAEREIKLFFGE
>gnl|CDD|173007 PRK14541, PRK14541, nucleoside diphosphate kinase; Provisional
MERTLTILKPDCVRKQLIGAVIDKIERAGFRVVAMKKTRLTKETAGEFYAVHRERPFYGELVEFMSSGPC
VPMILEKENAVADFRTLIGATDPAEAAEGTVRKLYADSKGENIVHGSDSAENAAIEAGFFFSAEEVVRVN
>gnl|CDD|173008 PRK14542, PRK14542, nucleoside diphosphate kinase; Provisional
MSRTFIMIKPDGVKNKHVGNILQRIEKEGFKILGLKYLKLSLEDAKQFYKVHSARPFYNDLCNYMSSGPI
VAAALERDNAVLHWREVIGATDPKEAAAGTIRALYAESKEANAVHGSDSDANAALEISFFFKGNELF
>gnl|CDD|237749 PRK14543, PRK14543, nucleoside diphosphate kinase; Provisional
MSTLIQKTLCIIKPDGVRRGLIGNVVSRFERVGLKIVAAKMLLVDRSMAEKHYLYDDIAVRHGEAVWKSL
IKFISSSPVFVFVVEGVESVEVVRKFCGSTEPKLAIPGTIRGDFSYHSFNYANEKGFSVYNVIHASANED
DALREIPIWFKDNEILTYKRDDECEHYYC
>gnl|CDD|173010 PRK14544, PRK14544, nucleoside diphosphate kinase; Provisional
MPIERTLVILKPDAVKRGLVGEIISRFEKAGLKIVAMKMVKATPEQIERFYPSSEEWYRSVGNKLLKAYQ
ELGIDPRARLGTDDPVEVGKKVKESLVKYMTSGPIVAMVLKGNRAVEVVRKLVGPTSPHKAPPGTIRGDY
SIDSPDLAAEEGRVVYNLVHASDSPEEAEREIKFWFREEEILD
>gnl|CDD|184734 PRK14545, PRK14545, nucleoside diphosphate kinase; Provisional
MAGNRTFTMIKPDAVENGHIGGILDMITAAGFRIVAMKLTQLTVADAETFYAVHAERPFYGELVEFMSRG
PIVAAILEKENAVEDFRTLIGATNPADAAEGTIRKKYAKSIGENAVHGSDSDENAQIEGAFHFAGREMF
>gnl|CDD|237750 PRK14548, PRK14548, 50S ribosomal protein L23P; Provisional
PYSIIKYPLVTEKAMNLIEKENKLTFIVDRRATKPDIKRAVEELFDVKVEKVNTLITPKGEKKAYVKLAE
EYDAEEIASRLGVF
>gnl|CDD|237751 PRK14549, PRK14549, 50S ribosomal protein L29P; Provisional
MAILRASEIREMSPEEREEKLEELKLELLKERAQAAMGGAPENPGRIREIRRTIARILTIQREKKREAK
>gnl|CDD|173015 PRK14550, rnhB, ribonuclease HII; Provisional
MTLGIDEAGRGCLAGSLFVAGVACNEKTALEFLKMGLKDSKKLSPKKRFFLEDKIKTHGEVGFFVVKKSA
NEIDSLGLGACLKLAIQEILENGCSLANEIKIDGNTAFGLNKRYPNIQTIIKGDETIAQIAMASVLAKAF
KDREMLELHALFKEYGWDKNCGYGTKQHIEAIIKLGATPFHRHSFTLKNRILNPKLLEVEQRLI
>gnl|CDD|237753 PRK14552, PRK14552, C/D box methylation guide ribonucleoprotein complex aNOP56 subunit; Provisional
KIYIAEHVIGAFAFDENGKLIDKIFNPEDIPKIVEELLNNEKGEPTNALFELLEELKELGPDEVVVENEE
ESRKLQELGYRVTVEPPNKIGEFLRENLPELGVEYGFFEDEEEFYEKLHEWSVELTRRKLRSAAQKRDKL
AIQAIRAIDDIDKTINLFSERLREWYSLHFPELDELVKKHEEYVKLVSELGDRENYTREKLKKLGLPENK
ARKIAEAAKKSMGADLSEFDLEAIKKLANEILDLYKLREELEDYLETVMKEVAPNLTALVGPSLGARLIS
LAGGLEELAKMPASTIQVLGAEKALFRHLRTGAKPPKHGVIFQYPAIHGSPWWQRGKIARALAAKLAIAA
RVDYFSGRYIGDELKEELNKRIEEIKEKYPKPPKKKREEKKPQKRKKKKKRKKKGKKRKKKGRK
>gnl|CDD|184740 PRK14553, PRK14553, ribosomal-processing cysteine protease Prp
MIKVTIKRKNGQIISFTMSGHAGSGEHGQDIVCASVSAISITAVNALEELGKVEPVIESEDGYLEFELPD
FDEENNEKLQLLLETLELGLKSLEFQYPKYIKLIEEEV
>gnl|CDD|237754 PRK14554, PRK14554, tRNA pseudouridine(54/55) synthase Pus10
MDILEKARAILEKYPLCDHCLGRLFAKLGYGLTNEERGRAIKTALAMELDEPYKEHKEVDLDEILENLGP
IAERLYKLYFIEEFEERCYICGGIFDEIDEFAEKAAEALSGYEFDTFLVGTRLPPEIKEKEEEIWEEFGL
TYGESIKSEINREVGKRLAARTGKEVDFENPDVVIVVDLETDKVELQVNPLFIYGRYRKLVRGIPQTRWP
CRKCKKQYPESVEELIAKPVIEAFGGEDAVFHGAGREDVDARMLGTGRPFVIEVKEPRKRKVDLEALEEE
INADGKVEVENLRFATRKEVERIKEEKASKTYRALVESDEPVSEEELEKLLDELSGATIEQRTPRRVKHR
RADLVRVRKVYDISGELIDDKHFELRIKCEGGLYIKELISGDEGRTTPSLSELLGTPAIVTELDVLDVEG
ED
>gnl|CDD|237755 PRK14555, PRK14555, RNA-binding protein
MIHYIDLRVFCHATEDEDKVLEALRNFLSIDPEDIEIEVEEAEGHYGNPITILSARLEKKEAREVLKHLL
ELLDETELEKLLSELDERVDDEGKLYLRFDKQAAYLGELKLSDGDDVIRLKIKVKAYLPPAKKEKAKENV
RELLE
>gnl|CDD|237756 PRK14559, PRK14559, serine/threonine phosphatase
MLICPQCQFENPNNNRFCQKCGTSLTHKPCPQCGTEVPVDEAHCPNCGAETGTIWWAIIAQASPNSEVLE
SGEATQQSESSLTPSSSPLYGSYLDPGQRYQLLASSEEIPTAAAHTELQGRVLDCQPLQPSPLEALLEQL
EDLLNPLADPTEVLPTLLWQQLGIPALAIPYLALQDQFPTEIPKIHDAWQDGDLQVILLEDRSHWQPLLD
LWQDQTLPTLQILYWLNQMTQLWKALEPWGCCQSLLELENLRVDEDQTLGLQQLYQDPPEQPPSLQDLGQ
VWQQLFTQSQRTQFESLIPLLQDLQSGKIQTIAQLRLRLQELATELEAEGEAEFESTEGETTLAPSILQS
DDSESPIHETEDAPTAVLPMQLVSLEDAGRTDVGRQRHHNEDYFGINTRIQKLENPHGRIVQARGLYILC
DGMGGHAAGEVASALAVETLQQYFQQHWQDELPDEETIREAIYLANEAIYDLNQQNARSGSGRMGTTLVM
ALVQDTQVAVAHVGDSRLYRVTRKGGLEQLTVDHEVGQREIQRGVEPQIAYARPDAYQLTQALGPRDNSA
IQPDIQFLEIEEDTLLLLCSDGLSDNDLLETHWQTHLLPLLSSSANLDQGLNKLIDLANQYNGHDNITAI
LVRLKVRPQLSLETW
>gnl|CDD|237757 PRK14560, PRK14560, putative RNA-binding protein; Provisional
MEVKSRHHLSKKEVKEIKEELKEKFGVDIDGKDAVEEVETDKKEEIYLVDGEPLFFKVDDELFPTLRGAL
KLKPEKRRVVVDAGAVKFVSNGADVMAPGIVEADEDIKEGDIVFVVEETHGKPLAVGRALMDGDEMVEEK
KGKAVKNIHHVGDEIWEFEV
>gnl|CDD|184745 PRK14561, PRK14561, hypothetical protein; Provisional
MKAGVLFSGGKDSSLAAILLERFYDVELVTVNFGVLDSWKHAREAAKALGFPHRVLELDREILEKAVDMI
IEDGYPNNAIQYVHEHALEALAEEYDVIADGTRRDDRVPKLSRSEIQSLEDRKGVQYIRPLLGFGRKTID
RLVERLFEIEEGESEEIPKSDYETELRELLRERGGDPLEIFPEHEQSRVVGRKK
>gnl|CDD|184746 PRK14562, PRK14562, haloacid dehalogenase superfamily protein; Provisional
KIEEIIDSIREELEEKDEAREEALKLSREIVRLSGDAIRAIHRGDFEEAEKLLKEAEELVKELKELLKDH
PELYYAGYVGTALQEYVEALLVYSLLFENKIPSPEELGVPEAAYLLGLADAIGELRRHILELLRKGEIEE
AEKLLEIMEEIYEFLMTLDYPDAITPGLRRKQDVARSLLERTRGDLTNAILNRKLEEALKKFES
>gnl|CDD|184747 PRK14563, PRK14563, ribosome modulation factor; Provisional
MKRQKRDRLERAFSRGYQAGIAGRSKEMCPYQTLDARSQWLGGWREAMEDRVVGL
>gnl|CDD|237758 PRK14565, PRK14565, triosephosphate isomerase; Provisional
MSFLIVANWKMNGDFSLFSSFLKELSNKLANNEITLKLVICPPFTAMSSFVECNPNIKLGAQNCFYGSSG
GYTGEISAKMLKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDV
LLEQCSNCLPKHGEFIIAYEPVWAIGGSTIPSNDAIAEAFEIIRSYDSKSHIIYGGSVNQENIRDLKSIN
QLSGVLVGSASLDVDSFCKIIQQVEEV
>gnl|CDD|173033 PRK14569, PRK14569, D-alanyl-alanine synthetase A; Provisional
MKNEKIVVLYGGDSPEREVSLKSGKAVLDSLISQGYDAVGVDASGKELVAKLLELKPDKCFVALHGEDGE
NGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPTPMAKFLTDKLVAEDEISFPVAVKPSSG
GSSIATFKVKSIQELKHAYEEASKYGEVMIEQWVTGKEITVAIVNDEVYSSVWIEPQNEFYDYESKYSGK
SIYHSPSGLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNFYIMEINSSPGMTDNSLSPKSAAAE
GVDFDSFVKRIIEQAQ
>gnl|CDD|173034 PRK14570, PRK14570, D-alanyl-alanine synthetase A; Provisional
MKKNLMLIFGGVSFEHEISLRSAYGIYSALLKLDKYNIYSVFIDKCTGIWYLLDSVPDPPKLIKRDVLPI
VSLIPGCGIFVNNKNLEIDVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSF
NIPLVPFIGFRKYDYFLDKEGIKKDIKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTV
VIEKFIEAREIECSVIGNEQIKIFTPGEIVVQDFIFYDYDAKYSTIPGNSIVFNIPAHLDTKHLLDIKEY
AFLTYKNLELRGMARIDFLIEKDTGLIYLNEINTIPGFTDISMFAKMCEHDGLQYKSLVDNLIDLAFQSY
IKRKKRIDFERLEN
>gnl|CDD|184751 PRK14571, PRK14571, D-alanyl-alanine synthetase A; Provisional
MRVALLMGGVSREREISLRSGERVKKALEKLGYEVTVFDVDEDFLKKVDQLKSFDVVFNVLHGTFGEDGT
LQAILDFLGIRYTGSDAFSSMICFDKLLTYRFLKGTVEIPDFVEIKEFMKTSPLGYPCVVKPRREGSSIG
VFICESDEEFQHALKEDLPRYGSVIVQEYIPGREMTVSILETEKGFEVLPILELRPKRRFYDYVAKYTKG
ETEFILPAPLNPEEERLVKETALKAFVEAGCRGFGRVDGIFSDGRFYFLEINTVPGLTELSDLPASAKAG
GIEFEELVDIIIKSAFLKG
>gnl|CDD|173036 PRK14572, PRK14572, D-alanyl-alanine synthetase A; Provisional
MAKIAVFFGGSSTEHSISIRTGCFICATLHTMGHSVKPILLTPDGGWVVPTVYRPSIPDESGNSEDLFLE
EFQKANGVSEPADISQLDADIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQ
SGQKVAPFFELEKLKYLNSPRKTLLKLESLGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKV
MSQSFLSGTEVSCGVLERYRGGKRNPIALPATEIVPGGEFFDFESKYKQGGSEEITPARISDQEMKRVQE
LAIRAHESLGCKGYSRTDFIIVDGEPHILETNTLPGMTETSLIPQQAKAAGINMEEVFTDLIEIGLK
>gnl|CDD|184752 PRK14573, PRK14573, bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase
MMKSLFYHFIGIGGIGMSALAHILLDRGYSVSGSDLSEGKTVEKLKAKGARFFLGHQEEHVPEDAVVVYS
SSISKDNVEYLSAKSRGNRLVHRAELLAELMQEQISILVSGSHGKTTVSSLITAIFQEAKKDPSYAIGGL
NQEGLNGYSGSSEYFVAEADESDGSLKHYTPEFSVITNIDNEHLSNFEGDRELLLASIQDFARKVQQINK
CFYNGDCPRLKGCLQGHSYGFSSSCDLHILSYYQEGWRSYFSAKFLGVVYQDIELNLVGMHNVANAAAAM
GIALTLGIDEGAIRNALKGFSGVQRRLERKNSSETFLFLEDYAHHPSEISCTLRAVRDAVGLRRIIAICQ
PHRFSRLRECLDSFPSAFQDADEVILTDVYSAGEEPEDSISYQKLAEAISQSSIVKCTYVPFHEIQRYLE
QSIRVHDVCVSLGAGNIYTLGEALKDFEPKKLSLGLVCGGKSCEHDISLLSAKNIAKYLSPEFYDVSYFL
INRQGLWETVSSLETAIEEDSGKSVLSSEIAQALAKVDVVLPILHGPFGEDGTMQGFLEIIGKPYTGPSL
AFSAIAMDKVLTKRFASDVGVPVVPYQPLTLAGWKREPELCLAHIVEAFSFPMFVKTAHLGSSIGVFEVH
NVEELRDKISEAFLYDTDVFVEESRLGSREIEVSCLGDGSSAYVIAGPHERRGSGGFIDYQEKYGLSGKS
SAQIVFDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMNPIPGMTEASPFLTAFVR
KGWTYEQIVHQLIIDGLHKFDQRQRLISTFFKDQALAAR
>gnl|CDD|173038 PRK14574, hmsH, poly-beta-1,6 N-acetyl-D-glucosamine export porin PgaA
MYNAFTTLLRPLHWHRMTLLALFISGFVVNPAMADTQYDSLIIRARAGDTAPVLDYLQEESKAGPLQSGQ
VDDWLQIAGWAGRDQEVIDVYERYQSSMNISSRGLASAARAYRNEKRWDQALALWQSSLKKDPTNPDLIS
GMIMTQADAGRGGVVLKQATELAERDPTVQNYMTLSYLNRATDRNYDALQASSEAVRLAPTSEEVLKNHL
EILQRNRIVEPALRLAKENPNLVSAEHYRQLERDAAAEQVRMAVLPTRSETERFDIADKALADYQNLLTR
WGKDPEAQADYQRARIDRLGALLVRHQTADLIKEYEAMEAEGYKMPDYARRWAASAYIDRRLPEKAAPIL
SSLYYSDGKTFRNSDDLLDADDLYYSLNESEQLDKAYQFAVNYSEQTPYQVGVYGLPGKEPNDDWIEGQT
LLVQSLVALNDLPTAQKKLEDLSSTAPANQNLRIALASIYLARDLPRKAEQELKAVESLAPRSLILERAQ
AETAMALQEWHQMELLTDDVISRSPEDIPSQELDRQRKVHNMYELRVSGNRVISSNSPVSGNKDYGVETL
LYSPPIAENWRVFGGGSYNNGQFEEGTGISRILRLGGEWTSRDHWVEGEISNQNYGNGNKVGARLSTWYD
LNDHWRVGGQVERLAKDTPLRALKNKVTANSASAYVFWKADDKRDAELSVTPSRFSDGNNRWEYEFNGRQ
RIWTGPYLTADFNLGLAASQNSKEDVIYYNPKRDFAYVPAVTLNHIMYRRYKTIWSQQVQLGVGGYWEKN
YGNGLVTTAGYGQRVQWNDVIDTGVAVVYDKRPYDGKREHDVTLSFDLNYRF
>gnl|CDD|173039 PRK14575, PRK14575, putative peptidase; Provisional
MNSEKKEHLNTVSRKLRTIMERDNIDAVIVTTCDNFYHVTGILSFFMYTFRNTGTAIAVVFRDVKIPSLI
IMNEFEAASLTLDMPNAELKTFPVWVDVDDPFNMRDSANNNKERPIGPPIESVCNILKDALNDARVLNKK
IAIDLNIMSNGGKRVIDAVMPNVDFVDSSSIFNELRVIKSPWEIKRLRKSAEITEYGITEASKLIRVGCT
SAELTAAYKAAVMSKSETHFSRFHLISVGADFSPKLIPSNTKACSGDLIKFDCGVDVDGYGADIARTFVV
GEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSGLPNYNRGHLGHGNGVFLGLEESPF
VSTHATESFTSGMVLSLETPYYGYNLGSIMIEDMILINKEGIEFLSKLPRDLVSFN
>gnl|CDD|173040 PRK14576, PRK14576, putative endopeptidase; Provisional
MGKEKIEHLEAVSRKARVVMEREGIDALVVTVCDNFYYLTGFASFFMYTFRHTGAAVAIMFRDANIPSQI
IMNEFEAASTHFDMPNSVLKTFPVWVDVDDPRNPHHHYKKRDRPIGPPVEAVFSLVKNALEDAGVLDKTI
AIELQAMSNGGKGVLDKVAPGLKLVDSTALFNEIRMIKSPWEIEHLRKSAEITEYGIASAAKKIRVGCTA
AELTAAFKAAVMSFPETNFSRFNLISVGDNFSPKIIADTTPAKVGDLIKFDCGIDVAGYGADLARTFVLG
EPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDSTMAVIKTSGLPHYNRGHLGHGDGVFLGLEEVPFV
STQATETFCPGMVLSLETPYYGIGVGSIMLEDMILITDSGFEFLSKLDRDLRRYF
>gnl|CDD|173042 PRK14578, PRK14578, elongation factor P; Provisional
MYTTSDFKKGLVIQLDGAPCLLLDVTFQSPSARGANTMVKTKYRNLLTGQVLEKTFRSGDKVEEADFERH
KGQFLYADGDRGVFMDLETYEQFEMEEDAFSAIAPFLLDGTEVQLGLFQGRMVNVDLPMTVELTVTDTAP
VMKNATATAQTKEAVLETGLRLQVPPYLESGEKIKVDTRDGRFISRA
>gnl|CDD|184753 PRK14581, hmsF, outer membrane N-deacetylase; Provisional
MAKLLIFIKSLIVGMMIVSTMGCAEKPTFVPPAQRALPQSERPWQKNTFVVIAYHDVEDDSADQRYLSVR
SSALNEQFVWLRDNGYHVVSVDQILAARNGGPTLPDKAVLLTFDDGYSSFYRRVYPLLKAYKWSAVLAPV
GTWIDTATDKKVDFGGLSTDRDRFATWKQITEMSKSGLVEIGAHTYASHYGVIANPQGNTEPAAANLQYD
PKTKQYETVEAFKQRMEKDVALITQRIVQATGKQPRVWVWPYGAPNGTVLNILRQHGYQLAMTLDPGVAN
INDLMNIPRILISNNPSLKDFALTVTSVQEKNIMRVAHVDLDYLYDPDPAQEKENLDKLVQRISDLRVTH
VFLQAFSDPKGDGNIRQVYFPNRWIPMRQDLFNRVVWQLASRPDVEVYAWMPVLAFDMDPSLPRITRIDP
KTGKTSIDPDQYRRLSPFNPEVRQRIIDIYRDMAYSAPIDGIIYHDDAVMSDFEDASPDAIRAYEKAGFP
GSITTIRQDPEMMQRWTRYKSKYLIDFTNELTREVRDIRGPQVKSARNIFAMPILEPESEAWFAQNLDDF
LANYDWVAPMAMPLMEKVPLSESNEWLAELVNKVAQRPGALEKTVFELQSKDWTQPEGNNAISGPILAGW
MRQLQLSGAQSFGYYPDNFITGEPPLKDVRPVLSSAWYPLYD
>gnl|CDD|184754 PRK14582, pgaB, poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB
MLRNGNKYLLMLVSILMLTACISQSRTSFIPPQDRPSLLAEQPWPHNGFVAIAYHDVEDEAADQRFMSVR
TSALREQFAWLRENGYQPVSVAQILEAHRGGKPLPEKAVLLTFDDGYSSFYTRVFPILQAFQWPAVWAPV
GSWVDTPADQPVKFGGEMVPREYFATWQQVREVARSRLVEIASHTWNSHYGIQANPQGSLLPAAVNRAYF
TDHARYETAAEYRERIRLDAVKMTEYIRTKAGKNPRVWVWPYGEANGIALEELKKLGYDMAFTLESGLAN
ASQLDSIPRVLIANNPSLKEFAQQIITVQEKSPQRVMHIDLDYVYDENPQQQDRNIDVLIQRVKDMQIST
VYLQAFADPDGDGLVKELYFPNRLLPMRADLFNRVAWQLRTRAGVNVYAWMPVLSFDLDPTLPRVKRLDT
GEGKAQIHPEQYRRLSPFDDRVRAQVGMLYEDLAGHAAFDGILFHDDAVLSDYEDASAPAITAYQQAGFS
GSLSEIRQNPEQFKQWTRFKSRALTDFTLELSARVKAIRGPQVKTARNIFALPVIQPESEAWFAQNLDDF
LKSYDWTAPMAMPLMEGVAEKSSDAWLIQLVNQVKNIPGALDKTIFELQARDWQKNGQQAISSQQLAHWM
SLLQLNGVKNYGYYPDNFLHNQPEIDLIRPEFSTAWYPKND
>gnl|CDD|184756 PRK14584, hmsS, hemin storage system protein; Provisional
MSTPLIFTEQRLLPRLIDIILTALAWFGFLFLLVRGLLEMISRAPHMGPIPLRIYILSGLTTIALYLAIA
AFNAVLLIIWAKYNQVRFQVERRGHRPDLDDDELASSFALSPELIAQLKSGSCLTLYNDEHGHIIDVKEG
LQLPEPVIHLRQG
>gnl|CDD|173049 PRK14585, pgaD, putative PGA biosynthesis protein; Provisional
MNNLIITTRQSPVRLLVDYVATTILWTLFALFIFLFAMDLLTGYYWQSEARSRLQFYFLLAVANAVVLIV
WALYNKLRFQKQQHHAAYQYTPQEYAESLAIPDELYQQLQKSHRMSVHFTSQGQIKMVVSEKALVRA
>gnl|CDD|173051 PRK14587, PRK14587, tRNA pseudouridine synthase ACD; Provisional
MPYLYRIAYDGTLFYGFTGHPNSLEPALRRVFGEILGRGSRTDPGVSAVGNVVMTSQKLPLGYVNSKLPR
GVWAWAVAEVPEGFNPRRAKRRRYLYVAPHWGEDVEAMREAAELLAGTHDYSSFIQRRGEKATPTVTTVY
EIGVELRGDLIYLYFVGRGFRNKMIRKMAWAILAAGRGVLSRRDIAELLERPRPGAVPSAPAEGLVLLDI
EYDVKFQVDYTALRKAYVYFLSKYRHLEAHAAALKAAGEALAFWED
>gnl|CDD|173054 PRK14590, rimM, 16S rRNA-processing protein RimM; Provisional
ISLGQLGKPFGIKGWLRVNVRGETLHTLKAPATLKLGKEDPQFPESEIALLEIRPHGGKFLVRFEGYDTP
EEAVKWRGGSLFLPQELLPKIETKGEFYSEDLIGLQAIDETGKPLNWKLTDVQDNPAHPILVFIKGEGEE
ILIPFLNVFVGDLDLEKQTIVLIQPEQWNEL
>gnl|CDD|173055 PRK14591, rimM, 16S rRNA-processing protein RimM; Provisional
MSQDFVEIAKIGATYKLNGELNLYPLANSIETLLSYGDWYIQLPATNVWQQLKGESVLKRADKVYIKLAN
INNADTAKKYVNALIGVPKRALPQLAEDEVYFKDLIGCSVKNINNDSFGVVVDIIETGANEVLVCKEDNS
EYLIPYVKQYIVSEDLNSKKIVVDWEYDY
>gnl|CDD|173056 PRK14592, rimM, 16S rRNA-processing protein RimM; Provisional
DLICLGVITSPHGIKGHVKIKTFTEDPENISAYGKLTDGSNTYKISVVSVIGANLVIAKISGINSRTEAE
LLRNKKLYVERSKLPNLNEDEFYQSDLIGMEVKLEDNTIYGYIKKIYNFGSCDIIEISLTSTKKSTMLPF
TKEIFPHINVKERYIILVPPEIIGV
>gnl|CDD|237760 PRK14593, rimM, ribosome maturation factor RimM
MVSMLLVGRIGKSVGLNGGLKLHLESDFPECLKKGVKVSVAPLNAFSCASSFKDYVIHSYEHAKNLLFLE
TIHTPEKAKELTNLGLFMSEAESKKLCVLKEGEFFYCDLVGLSVVEENEILGKVIEIQRISQTDYFMVET
TLSLVEKGLAKIFLIPYRDFYIQEILLQDKKITTHNAKTLLENS
>gnl|CDD|173058 PRK14594, rimM, 16S rRNA-processing protein RimM; Provisional
MFVKGIILSSYGINGYAKVKSISNNFCDFINLKNNKLVLKKSNCSSIEVKVEDVSLKNNSLLLKFEEFNA
PEPIKPLIGFELWVDDELASKLEEGEYYFGKLIGYAIVNDGKELGEVVSFFECLNSVLLEVKVGIKLFFV
PFLSIYLGDINRELKTIELKVLDLLK
>gnl|CDD|184757 PRK14595, PRK14595, peptide deformylase; Provisional
MAIKKLVPASHPILTKKAQAVKTFDDSLKRLLQDLEDTMYAQEAAALCAPQIGQSLQVAIIDMEMEGLLQ
LVNPKIISQSNETITDLEGSITLPDVYGEVTRSKMIVVESYDVNGNKVELTAYDDVARMILHIIDQMNGI
PFTERADRILTDKEVEAYFIND
>gnl|CDD|173063 PRK14599, trmD, tRNA (guanine-N(1)-)-methyltransferase/unknown domain fusion protein; Provisional
MKFNFITLFPEKIQSYFSEGLQQKAIESGVFSINPIQLRDFSGNKHNRVDDTIYGGGPGMLLRVEPIHKA
LLSLGEKKGIVILTSPSGIPFNQTIARELKESGKPLTFISGYYEGVDHRVTEHLVDMEMSLGNYVISAGD
LASICIADAVSRLLPGFLGAEESLLDESHNEPDELEYPQFTKPSEYNGWKVPDVLLSGNHASILAWREQN
RKKINHSNYEST
>gnl|CDD|173064 PRK14600, ruvA, Holliday junction branch migration protein RuvA
MIGSLSGIVEEVRSDYIILNVGNVGYIVYLSAKVLSTCKIGDNIKLYIETYVNRDNVTQLYGFLNREEQD
CLRMLVKVSGVNYKTAMSILSKLTPEQLFSAIVNEDKAALKVNGIGEKLINRIITELQYKVSKLEINETN
FIIINDDALAALISLGYEKTKAFNAIQKIKPNLSTQDIIRKALKEL
>gnl|CDD|237764 PRK14607, PRK14607, bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase
MIILIDNYDSFTYNIYQYIGELGPEEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHF
SGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPE
CLEVTAKSDDGEIMGIRHKEHPIFGVQFHPESILTEEGKRILKNFLNYQREEIDIKSYLKKLVEGEDLSF
EEAEDVMEDITDGNATDAQIAGFLTALRMKGETADELAGFASVMREKSRHIPAPSPRTVDTCGTGGDGFG
TFNISTTSAFVVAAAGVPVAKHGNRAVSSKSGSADVLEALGVKLEMTPEEAASVLRETGFSFLFAPLFHP
AMKHAAPARRELGIRTAFNLLGPLTNPARVKYQIVGVFDPSYAEPLAQALQRLGTERAMVVSGIDGYDEI
STCGPTQILELEDGEIVTYTFDPEELGLKRVDPEELKGGDPQENYRLAEDVLKGEPRRPQRDAVALNAGA
ALYLVGEADSIKEGVGKALDLIDDGRAYKKLEEVMDLSKTLGNS
>gnl|CDD|237765 PRK14608, PRK14608, 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Provisional
QSAMPSLTEFAPAKINLALHVTGRRADGYHLLESLVAFADVGDRLTLEPAEALSLTVSGPFAAGLGDGDD
NLVLRAARALRARVGPGLPPGAFHLEKNLPVAAGIGGGSADAAAALRLLARLWGLALDDERLAALALSLG
ADVPVCLDSRPLIMRGIGEELTPLPGLPSLPAVLVNPGVPVATPDVFRALGLRDGPPLPGAPDPLASADA
LLAALAATRNDLEPPALALAPVIGEVLAALRAQPGALLARMSGSGATCFALFADEAAAEAAAAAIAAAHP
GWWVKATRLR
>gnl|CDD|184767 PRK14611, PRK14611, 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase
MEVLLSPAKVNLGLWILGKRPDGYHEIFTIYHTIDLYDRIYIKEHHTLEVKTSSPQIKEEENIVYKALRL
FERYTGIDINYSIFIEKNIPVGAGLGGGSSNAAVVLKYLNELLGNPLSEEELFELASSISADAPFFLKGG
FALGRGIGDKLEFLEKPISREITLVYPNIKSSTGRVYSKVTKQILTNKEDLNIIISLLREGEEKKIEEVI
ENTLGEIALELYPEIKEVYRFLEYLGYKPFVSGSGSSVYVFGKPSEEVKKAAAVRGWKLIETKLK
>gnl|CDD|173077 PRK14613, PRK14613, 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase
MISPAKINLGLEIPFKREDGFHEIRSVFLKISWGDDIEIEPAPNGVFELFSTNEIILEKRKLYDQVSERG
DIKQNILYKTFIKARSLFPELPGVKIHLTKRISPAGGLGGGSTNAASLLNFLFSWRNFFTSDEMQVFAKE
IGSDVPFFLGEGHAFVTGKGEIMEEIEVHKGQGILALTPQVMNTGEMYALLKKPLQESASQKNGNTLSED
LISSLKVGDWVSLQGRLENDFEPVAFQLHPELGVLKDKFLEFGSSYCSLTGSGSSMYGLVQGLEIQEELL
PRLRQEFSNLTFVRFNF
>gnl|CDD|237770 PRK14618, PRK14618, NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
MHHGMRVAVLGAGAWGTALAVLAASKGVPVRLWARRPEFAAALAAERENREYLPGVALPAELYPTADPEE
ALAGADFAVVAVPSKALRETLAGLPRALGYVSCAKGLAPDGGRLSELARVLEFLTQARVAVLSGPNHAEE
IARFLPAATVVASPEPGLARRVQAAFSGPSFRVYTSRDRVGVELGGALKNVIALAAGMVDGLKLGDNAKA
ALITRGLREMVRFGVALGAEEATFYGLSGLGDLIATATSPHSRNRAAGEAIVRGVDREHLEAGGKVVEGL
YTVKALDAWAKAHGHDLPIVEAVARVARGGWDPLAGLRSLMGREAKEE
>gnl|CDD|237771 PRK14619, PRK14619, NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
TTQPKTIAILGAGAWGSTLAGLASANGHRVRVWSRRSGLSLAAVLADADVIVSAVSMKGVRPVAEQVQAL
NLPPETIIVTATKGLDPETTRTPSQIWQAAFPNHPVVVLSGPNLSKEIQQGLPAATVVASRDLAAAETVQ
QIFSSERFRVYTNSDPLGTELGGTLKNVIAIAAGVCDGLQLGTNAKAALVTRALPEMIRVGTHLGAQTET
FYGLSGLGDLLATCTSPLSRNYQVGYGLAQGKSLEQILAELEGTAEGVNTANVLVQLAQQQNIAVPITEQ
VYRLLQGEITPQQALEELMERDLKPEFN
>gnl|CDD|173083 PRK14620, PRK14620, NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
MKISILGAGSFGTAIAIALSSKKISVNLWGRNHTTFESINTKRKNLKYLPTCHLPDNISVKSAIDEVLSD
NATCIILAVPTQQLRTICQQLQDCHLKKNTPILICSKGIEKSSLKFPSEIVNEILPNNPIAILSGPSFAK
EIAEKLPCSIVLAGQNETLGSSLISKLSNENLKIIYSQDIIGVQIGAALKNIIAIACGIVLGKNLGNNAH
AAVITKGMNEIKTLYSAKNGSIDLNTLIGPSCLGDLILTCTTLHSRNMSFGFKIGNGFNINQILSEGKSV
IEGFSTVKPLISLAKKLNIELPICESIYNLLYENISLEKTISVILS
>gnl|CDD|184772 PRK14625, PRK14625, hypothetical protein; Provisional
MKDLGGLMKQAQAMQQKLADAQARLAETTVEGTSGGGMVTVTLMGNGELVRVLMDESLVQPGEGEVIADL
IVAAHADAKKKLDAKQAQLMQEAAGPMAGLMGGLPGMKF
>gnl|CDD|173093 PRK14630, PRK14630, ribosome maturation factor RimP
MVKIFDNSEVYNLIKNVTDRLGIEIIEINTFRNRNEGKIQIVLYKKDSFGVDTLCDLHKMILLILEAVLK
YNFSLEISTPGINRKIKSDREFKIFEGKKIKLMLDNDFEEGFILEAKADSFIFKTDSKEVNVLYSDVKKA
KLS
>gnl|CDD|237772 PRK14631, PRK14631, ribosome maturation factor RimP
MKLSNKSQALTDIIAPAVAACGVDLWGIEFLPQGKRSLLRIYIDRLVEENAEPVINEDGEVEQGRGIGVE
DCVRVTQQVGAMLDVHDPISGEYALEVSSPGWDRPFFQLEQLQGYIGQQVALRLIAAVENRRKFQAKLLA
VDLENEEIQVEVEGKHVLDIDSNNIDKANLIYQD
>gnl|CDD|173095 PRK14632, PRK14632, ribosome maturation factor RimP
MTKQALDATIADMAGPFLASLGLELWGIELSYGGRTVVRLFVDGPEGVTIDQCAEVSRHVGLALEVEDVI
SSAYVLEVSSPGLERPFFRAEQMSPYVGRQIELTLIDPTPEWPGRRKFRGELLAVEGDTVVLRPEGAPAP
EAEEAVLRTSWQGVRKANLIHVFPEPGHKPRR
>gnl|CDD|173096 PRK14633, PRK14633, ribosome maturation factor RimP
MLLDDLYEIVEPITADLGYILWGIEVVGSGKLTIRIFIDHENGVSVDDCQIVSKEISAVFDVEDPVSGKY
ILEVSSPGMNRQIFNIIQAQALVGFNVKAVTLAPVGSQTKFKGVLERVEGNNVILNLEDGKEISFDFDEL
KKLRVSPDFS
>gnl|CDD|173097 PRK14634, PRK14634, ribosome maturation factor RimP
MPHPLLPDLETLASATAADKGFELCGIQVLTHLQPMTLQVQIRRSSGSDVSLDDCAGFSGPMGEALEASQ
LLTEAYVLEISSPGIGDQLSSDRDFQTFRGFPVEVSHRDDDGSEQRLEGLLLERNEDHLQINIRGRIKRI
PRDSVISVRLTNPTG
>gnl|CDD|184774 PRK14635, PRK14635, ribosome maturation factor RimP
MTVSEEEISEILDRVLALPVKLYSLKVNQRPNHSLIEVVLDNLEHPYGSVSLLECEQVSRKLKEELERIS
PDLDFTLKVSSAGAERKLRLPEDLDRFRGIPVRLVFRSEESEKWQEGIFRLVNRDGDQVELEKFQKGKKS
KVKKQTTLNLKDILKGNLYVEI
>gnl|CDD|237773 PRK14636, PRK14636, ribosome maturation protein RimP
MADIAALTALIEPEAKALGLDLVRVAMFGGKSDPTLQIMAERPDTRQLVIEDCAALSRRLSDVFDELDPI
EDAYRLEVSSPGIDRPLTRPKDFADWAGHEARIALSEPLDGRKQFRGELKGIDGDTVTIADNKAGEVILP
FAAIESAKLILTDALIAATQPLDSEGADEIVEEGDD
>gnl|CDD|237774 PRK14637, PRK14637, ribosome maturation factor RimP
MNFSKKDLGYFSECEPVVEGLGCKLVDLSRRVQQAQGRVRAVIYSAGGVGLDDCARVHRILVPRLEALGG
VRDVFLEVSSPGIERVIKNAAEFSIFVGETVKVWFECTGQWQVGTIAEADETCLVLTSDGVPVTIPYVQI
TKAQLHPAVRA
>gnl|CDD|184777 PRK14638, PRK14638, ribosome maturation factor RimP
MFEEMILEKVRKEAERIAEEQGLEIFDVQYRRESRGWVLRIIIDNPVGYVSVRDCELFSREIERFLDRED
LIEHSYTLEVSSPGLDRPLRGPKDYVRFTGKLAKIVTKDGKTFIGRIESFVDGTITISDEKEKYEINIDD
VKRANLEVEF
>gnl|CDD|173102 PRK14639, PRK14639, ribosome maturation factor RimP
MNLEALCKECGVSFYDDELVSENGRKIYRVYITKEGGVNLDDCERLSELLSPIFDVEPPVSGEYFLEVSS
PGLERKLSKIEHFAKSIGELVKITTNEKEKFEGKIVSVDDENITLENLENKEKTTINFNDIKKAKTYVEW
>gnl|CDD|173103 PRK14640, PRK14640, hypothetical protein; Provisional
MATLEQRLTDLLEAPVVALGFELWGIEFIRAGKHSTLRVYIDGENGVSVENCAEVSHQVGAIMDVEDPIT
EEYYLEVSSPGLDRPLFKVAQFEKYVGQEAAVTLRMATNNRRKFKGVIKAVQGDMITLTVDGKDEVLAFT
NIQKANIVPNFG
>gnl|CDD|173104 PRK14641, PRK14641, ribosome maturation factor RimP
MEEKINNCVLQVLEASAGTKGEGVYLVSMTVKGSGKGRKIEVLLDADTGIRIDQCAFFSRRIRERLEEDE
ELLGLVGEDFDLMVSSPGLGEPIILPRQYGRHVGRLLRVTYRDEEGSEHEVTGHLQEVSLTEGEGASIVL
KPEQKKKKGKQEETENITLELDAVIRAVPEAEL
>gnl|CDD|237775 PRK14642, PRK14642, ribosome maturation factor RimP
MALQQIVEQTVTGLGYDLVEIERSAGGLLRVTIDLPWVPPTEGAPVGPEQFVTVEDCEKVTRQLQFALEV
DGVDYKRLEVSSPGIDRPLRHEQDFERFAGEVIDITLKAPIGAAAGGQVSANRKKFRGTLERAESGGWQI
VWSDEPPVKPGQRVSKKRVPAPLQALGFTLDELREARLAPIVDFKGRGAKPGPAPSG
>gnl|CDD|173106 PRK14643, PRK14643, ribosome maturation factor RimP
MKDFESIKFQINELVNKELEVLNLKVYEINNLKEFENDMIQILVEDILQANKPLDFDILIKANDLVSNKI
DQFIKTSEKYLLEISSSGIEKQIRSQEELVKALNQWVYVQLNNEIKKVKEFEGYVTKYNVNTNTFRFTFF
IKGQKKKLDVKYEQIKFIRYAVRF
>gnl|CDD|184779 PRK14644, PRK14644, hypothetical protein; Provisional
MTWKEKLLEKFGNKINEIKIVKEDGDLFLEVILNSRDLKDIEELTKEISDFIDNLSVEFDFDSLDISSPG
FDMDYETDELENHIGEIIDVSLNKEVNKTDFITGELLENNPETITLKWNCKGQFRKVEINKENIKK
>gnl|CDD|184780 PRK14645, PRK14645, ribosome maturation factor RimP
MNNATENNPDLQQLAEGALEPLGYEVLEVQVQRSGGKRIVLVRIDRKDEQPVTVEDLERASRALEAELDR
LDPIEGEYRLEVESPGPKRPLFTARHFERFAGLKAKVRGPGENFTGRIKAVSGDQVTFDVGGEDRTLRIG
TFQANLAEWPDRPR
>gnl|CDD|173109 PRK14646, PRK14646, ribosome maturation factor RimP
MNKENKSKLEILLEKVANEFDLKICSLNIQTNQNPIVIKIIIKKTNGDDISLDDCALFNTPASEEIENSN
LLNCSYVLEISSQGVSDELTSERDFKTFKGFPVNVELNQKNSKIKFLNGLLYEKSKDYLAINIKGKIKKI
PFNEVLKISLCTLKD
>gnl|CDD|173110 PRK14647, PRK14647, ribosome maturation factor RimP
MAKVDVVDRVTELAEQVLSSLGLELVELEYKREGREMVLRLFIDKEGGVNLDDCAEVSRELSEILDVEDF
IPERYTLEVSSPGLDRPLKKEADYERYAGRLVKVRTFELLADEAGNKRKTFLGELEGLADGVVTIALKEG
QQARIPLDKIAKANLEFEF
>gnl|CDD|173111 PRK14648, PRK14648, UDP-N-acetylmuramate dehydrogenase
MSAHRIRARRITRRNVPLAERCSFRIGGAAQFWAEPRSCTQLRALIEEAQRARIPLSLIGGGSNVLIADE
GVPGLMLSLRRFRSLHTQTQRDGSVLVHAGAGLPVAALLAFCAHHALRGLETFAGLPGSVGGAAYMNARC
YGRAIADCFHSARTLVLHPVRSRAKELPEVRKNAQDKRGECLGLDGGPFTCSSFQTVFARAGDWGYKRSP
FQSPHGVELHAGRRLILSLCVRLTPGNPAQIRKHMQEKIADRISKGQFRFPSAGSAFKNNPAFGKPSGIL
IEEAGLRGTSCGAAQVAPWHGNLIINTGNATAHQVRTLLRVVRQRVFETHGVWLEREIIFSGESVRMTSS
SRDS
>gnl|CDD|173112 PRK14649, PRK14649, UDP-N-acetylmuramate dehydrogenase
ITLRENEPLAPYTSWRIGGPARYFVEPTTPDEAIAAAAWAEQRQLPLFWLGGGSNLLVRDEGFDGLVARY
RGQRWELHEHGDTAEVWVEAGAPMAGTARRLAAQGWAGLEWAEGLPGTIGGAIYGNAGCYGGDTATVLIR
AWLLLNGSECVEWSVHDFAYGYRTSVLKQLRADGITWRPPLVLAARFRLHRDDPTALAARMEAIAAERKQ
KTPAGSSCGSVFKNPPGDSAGRLIEAAGLKGTRIGDAEIATRHANYIINLGGARAADILRLIDLARTRVL
AQFGIELELEVRIIG
>gnl|CDD|173113 PRK14650, PRK14650, UDP-N-acetylmuramate dehydrogenase
MLKNINNFLKKINIKPQTKNLANYTTYKIGGISKLFLTPKTIKDAEHIFKAAIEEKIKIFILGGGSNILI
NDEEEIDFPIIYTGHLNKIEIHDNQIVAECGTNFEDLCKFALQNELSGLEFIYGLPGTLGGAIWMNARCF
GNEISEILDKITFIDEKGKTICKKFKKEEFKYKISPFQNKNTFILKATLNLKKGNKKHIEEIMKQNKQIR
INKGHYLFPSSGSTFKNNKAFLKPTGQIIEECKLKGLSIGGATVSHYHGNFIININNATSKDIKTLIEKV
KTEVQIKTGFLLEEEVLYIGFN
>gnl|CDD|237776 PRK14651, PRK14651, UDP-N-acetylmuramate dehydrogenase
GARVERVPLARYTTLGVGGPAELWTVETHEQLAEATEAPYRVLGGGSNLLVSDAGVPERVIRLGGEFAEW
DLDGWVGGGVPLPGLVRRAARLGLSGLEGLVGIPAQVGGAVKMNAGTRFGEMADALHTVEIVHDGGFHQY
SPDELGFGYRHSGLPPGHVVTRVRLKLRPSTPEAVLAKMALVDAARKGQPKKKSAGCAFKNPPGDSAGRL
IDEAGLKGTRVGDAMISPEHGNFIVNLGGATAADVHALLRRVRARVGLPLELEWELWPEQLPE
>gnl|CDD|237777 PRK14652, PRK14652, UDP-N-acetylmuramate dehydrogenase
MVEATWRDEIARRVRGEVLRDAPLAPRTAVRVGGPADLLVRPADPDALSALLRAVRELGVPLSILGGGAN
TLVADAGVRGVVLRLPQDFPGESTDGGRLVLGAGAPISRLPARAHAHGLVGMEFLAGIPGTLGGAVAMNA
GTKLGEMKDVVTAVELATADGAGFVPAAALGYAYRTCRLPPGAVITRVEVRLRPGDVAASEALMRADRER
RRRTQPLDRPTFGSTFTNPPGDYAGRLVEAVGLKGHRVGGAIWSPVHANFVTNLGGATARDVLALVRLAR
ARVKERFGIALETEVRLLGEFL
>gnl|CDD|237778 PRK14653, PRK14653, UDP-N-acetylmuramate dehydrogenase
ITRKIIETLLKYGNDVFINEEMKCHVSFKIGGPVPLFAIPNSTNGFIETINLLKEGIEVKILGNGTNVLP
KDEPMDFVVVSTERLDDIFVDNDKIICESGLSLKKLCLVAAKNGLSGFENAYGIPGSVGGAVYMNAGAYG
WETAENIVEVVAYDGKKIIRLGKNEIKFSYRNSIFKEEKDLIILRVTFKLKKGNKNEIYNLMLETMKKRV
EKQPLEFPSAGSVFKRPRKDFYVGSAIEKLGLKGFSIGGAQISEKHAGFIINYNNAKAEDVLKLIEYVKD
KIYENYNVELETEIEIW
>gnl|CDD|237779 PRK14656, acpS, holo-[acyl-carrier-protein] synthase
MIFGTGVDIVDISRFERFVDEGNVALLERIFTPHEQEYCAGKKHSAQHYALRFAAKEAFLKALGTGLRDG
ISWHDMEVVNDQLGKPELRLYGRALELFAQAGLSKTFLSLSHDGGCAVAMVVLERP
>gnl|CDD|173120 PRK14657, acpS, holo-[acyl-carrier-protein] synthase
MIVGLGIDITELDRIAKALERFGDRFARRILHPAELAAMPAAPVAFLAGRFAAKEAAVKALGTGFSQGIG
PRDIEVGVLPAGAPQLVLHGKALARAEALGATSTHVSLTHGRDTAAAVVVLEG
>gnl|CDD|173121 PRK14658, acpS, holo-ACP synthase
MKLVHGIDIIEWNREELNNPLFAKRILIDNELEYYFQLNSSREKKRYLASVFACKEAVMKALKLKYGYGD
ILILKTENQRQVYLNKILIKELELSISYTETYIVASVVGLINNMN
>gnl|CDD|237780 PRK14659, acpS, holo-[acyl-carrier-protein] synthase
MIVGIGTDIVYIPRILNLLKKFGNKFLNRVFSEKEIEDSLKYTSQEARARHFAKRFAAKEAYVKALGTGF
GRGIKMKDISVYNDLYGKPQITVSKSNIDHKIELSLSDDGDYAIAFVVLHVE
>gnl|CDD|173123 PRK14660, acpS, holo-[acyl-carrier-protein] synthase
MILGTGVDIVEVERIARSIERHGDRFLRRIYTPGEIAYCTSKANRAERLAARFAAKEAVMKAIGTGLREG
VRWTDFEVCRDERGRPTVRLHGRAAEIAAALGATRIHLSLSHTQEYAVAQVILEG
>gnl|CDD|184782 PRK14661, acpS, holo-[acyl-carrier-protein] synthase
MIVGVGIDVLEVERVPEKFAERILGESEKRLFLTRKRRREFIAGRFALKEAFFKALGTGLNGHSFTDVEF
LESNGKPVLCVHKDFGFFNYAHVSLSHDRFAVALVVLEKRKGDIIVEGDESFLRKRFEVLERSVEGWEIE
TSLPPFTLKKLLESSGCRLVRYGNILIGE
>gnl|CDD|184783 PRK14662, acpS, 4'-phosphopantetheinyl transferase; Provisional
MIVAIGHDLVEIARIRRVLERHGERALERLFHPEELAYCLAKADPAPSLAARFAAKEAFQKCWPESHGWR
EVWVEREGARPVLGFAPKIAARMEEEGWVAHLSLSHEKEHALAVVVLEAR
>gnl|CDD|237781 PRK14663, acpS, holo-[acyl-carrier-protein] synthase
VDIVDLERIEKAYNRYGVKFLEKILTPEEIELCLQKPQPVASIAGRFAAKEAVVKALGTGFSQGVHWKSF
AILNDAAGRPFVKVIDDGCLPPGCVIKISISHDRHSAVATALIERG
>gnl|CDD|173127 PRK14664, PRK14664, tRNA-specific 2-thiouridylase MnmA; Provisional
MKESKKRVLVGMSGGIDSTATCLMLQEQGYEIVGVTMRVWGDEPQDARELAARMGIEHYVADERVPFKDT
IVKNFIDEYRQGRTPNPCVMCNPLFKFRMLIEWADKLGCAWIATGHYSRLEERNGHIYIVAGDDDKKDQS
YFLWRLGQDILRRCIFPLGNYTKQTVREYLREKGYEAKSKEGESMEVCFIKGDYRDFLREQCPELDTEVG
PGWFVNSEGVKLGQHKGFPYYTIGQRKGLEIALGKPAYVLKINPQKNTVMLGDAEQLKAEYMLAEQDNIV
DEQELFACPDLAVRIRYRSRPIPCRVKRLEDGRLLVRFLAEASAIAPGQSAVFYEGRRVLGGAFIASQRG
IGLVIEQNKDKK
>gnl|CDD|173128 PRK14665, mnmA, tRNA-specific 2-thiouridylase MnmA; Provisional
MMEKNKRVLLGMSGGTDSSVAAMLLLEAGYEVTGVTFRFYEFNGSTEYLEDARALAERLGIGHITYDARK
VFRKQIIDYFIDEYMSGHTPVPCTLCNNYLKWPLLAKIADEMGIFYLATGHYVRKQWIDGNYYITPAEDV
DKDQSFFLWGLRQEILQRMLLPMGGMTKSEARAYAAERGFEKVAKKRDSLGVCFCPMDYRSFLKKCLCDE
SGDKNRNIYRKVERGRFLDESGNFIAWHEGYPFYTIGQRRGLGIQLNRAVFVKEIHPETNEVVLASLKAL
EKTEMWLKDWNIVNESRLLGCDDIIVKIRYRKQENHCTVTITPDNLLHVQLHEPLTAIAEGQAAAFYKDG
LLLGGGIITM
>gnl|CDD|237782 PRK14666, uvrC, excinuclease ABC subunit C; Provisional
MQKPDLSTIPLTPGVYLYKDEAGRIIYVGKARHLRRRVASYFRDVSALTPKTVAMLRHAVTIDTLSTTTE
KEALLLEASLIKKHRPRYNIVLRDDKQYVLFRLGAKHPYPRLEIVRKARRDGARYFGPFTSASAARETWK
TIHRAFPLRRCSDRAFGNRVRACLYHFMGQCLGPCVNDVPRETYAALVRKVEMLLSGRSGELVDALRTEM
EAASEALEFERAAVLRDQIRAVERTVERQAAVLPGGGDLDVVGLVEAEGGLALGVLFVRQGVLLDGRAFF
WPGLGFEEAPELLWSFLGQFYGPQSTIPPRIVVPWLPDTEGREGDDLAPTAVCTDAGLLPDTPLLPDAPE
GSSDPVVPVAAATPVDASLPDVRTGTAPTSLANVSHADPAVAQPTQAATLAGAAPKGATHLMLEETLADL
RGGPVRIVPPRNPAENRLVDMAMSNAREEARRKAETPLQDLLARALHLSGPPHRIEAVDVSHTGGRNTRV
GMVVFEDGKPARDAYRTYAFEDGEGDDYGTLAAWAGRRVESGPPWPDLLLVDGGRGQLAAVVRALEEAGM
GGLFAVASIAKARTEEGRADRRAGNVADRIFLPGRANPLPLRAGAPELLFLQHVRDTVHDYAIGRHRRAR
AGAALTGELQRVEGIGPATARLLWERFGSLQAMAAAGEEGLAAVPGIGPARAAALHEHLKTLFG
>gnl|CDD|237783 PRK14667, uvrC, excinuclease ABC subunit C; Provisional
AKTMDALELIEKAPEEPGVYLFKKKKRYIYIGKAKNIKNRLLQHYKQSETDPKERAIFSESSSLEWIITR
NEYEALVLEIDLIQQYKPKYNVLLKSGSGYPMLLITDDEYPTVKIVRGTGEKGEYFGPFLPARKARKVKK
LIHKLFKLRTCDPMPKRKEPCMDYHLGLCSGPCCGKISKEDYELSVKSAKAFLSGNVKEVLPELYDKIEE
YSQKLMFEKAAVIRDQILALENLIKGQEVSGLPIEEADIFYFMGSRLGLFLVRSSKLVGKEEFRLESEEQ
EEEEVILGYYYSNYIPQKIITNFELSDNLKQWLSKRKGGDVEFLTLIPKELEKFIEENIGIKVDLEVLKE
EFKKTFGFPLPERIEGFDISHFYGEFTVGSCVVWEDGSMNKKEYRRYKIKTVDGIDDYASLREVLTRRAR
RYKEGENPMPDLWLIDGGKGQLSVGIEVRDRLGLNIKVFSLAKKEEILYTEDGKEIPLKENPILYKVFGL
IRDEAHRFALSYNRKLREKEGLKDILDKIKGIGEVKKEIIYRNFKTLYDFLKADDEELKKLGIPPSVKQE
VKKYLSG
>gnl|CDD|184785 PRK14668, uvrC, excinuclease ABC subunit C; Provisional
MDADEVRERAAELPREPGVYQFVAGGTVLYVGKAVDLRDRVRSYADPRSERIRRMVERADDIDFAVTDTE
TQALLLEANLIKRHQPRYNVRLKDDKSYPLVQLTDHPVPRIEVTRDPDEGATVFGPYTDKGRVETVVKAL
RETYGLRGCSDHKYSNRDRPCLDYEMGLCTAPCTGEIDEEAYAEDVESAERFFEGETGVLADPLRREMEA
AAQAQEFERAANLRDRLEAVEAFHGGGGEAVSSTGDERAVDVLGVAIEGDRATVARLHAEGGQLVDRDRH
RLEAPDGEDRGAAVLAAFIVQYYAERELPDALLLSERPGDDDVRAWLEAEGVDVRVPGAGREATLVDLAL
KNARRRGGRDDEVGALADALGIDRPERIEGFDVSHAQGRAVVGSNVCFVDGSAETADYRRKKLTERNDDY
ANMRELVRWRAERAVEGRDDRPDPDLLLIDGGDGQLGAARDALAETGWDVPAIALAKAEELVVTPDRTYD
WPDDAPQLHLLQRVRDEAHRFAVQYHQTLRDDVSTVLDDVPGVGPETRKRLLRRFGSVEGVREASVEDLR
DVPGVGEKTAETIRERL
>gnl|CDD|237784 PRK14669, uvrC, excinuclease ABC subunit C; Provisional
MDLRDKIRTLPTSPGVYLYKNAGGEVIYVGKAKNLRSRVRSYFSEDKLGNIKTGSLIREAVDIDYILVDN
EKEALALENNLIKQYKPRFNILLRDDKTYPYVKLTLGEKYPRVYVTRRLRKDGAQYYGPFFPANLAYRLV
DLIHRHFLVPSCKVDLTRYHPRPCLQFYIHRCLGPCVQGLTTDEAYAEAVRDVRLFLEGRHSDLARSLRA
RMEAAALEMQFELAAKYRDLITTVEELEEKQRMAAAKGDDADVFGYHYENPMVAVNLFHMRGGKIVDRRE
FFWEDLGEVQVEFEYDEGLFFSSLLKQIYLDQQYVPREIYVPVEFEDREALEELLTEQRHRRIEIRVPQR
GDKRSLLDLVEQNAKQSYDQRFRVMKPSSRAIQEALQDALNLPELPSRIECFDISHIQGAETVASMVVWE
DGKMKKSDYRKFIIKTVVGVDDFASMREVVTRRYSRLQEEKQPMPGLVLIDGGLGQLHAAAEALEAIGIT
DQPLASIAKREEIIYVFGQEDEPIVLDRFSPVLHLVQSIRDEAHRFAITFHRKRRETRDRTSELLEIPGV
GAKTVQRLLKHFGSLERVRAATETQLAAVVGRAAAEAIIAHFTTEEAAPEPVASVAQSEDAAPD
>gnl|CDD|173133 PRK14670, uvrC, excinuclease ABC subunit C; Provisional
MYSENNKILYIGKAKNLRSRVKNYFLEKISHKTKILMKNVKNIEVITTNSEYEALLLECNLIKTHKPDYN
IKLKDDKGYPMIRITCEKYPRIFKTRKIINDGSEYFGPYVNVKKLDLVLDLINKTFKTRKCKKKSKNPCL
YFHMGQCLGVCYREDLEKEYQKEVDKIKHILNGNISKLLSQIEIKMKEAIQKEDFEAAIKLKETKRSLIE
ISQTQIITKINKLSIDYVYIHPTENLNTIVILKYKDGKLVEKDINFDESIYEEDELILQFITQYYTSINM
IVPDKIHIFKKIDTKNITKLINELKNTKTEIIYKETKEIIKIMEMAISNAKLALREYENEKNKALESLKI
ILEMDKLPKTIEGFDIAHLNGQKTVASLVTFKMGKPFKDGYRVYKINSLLKGEIDDFKAIKEVISRRYSK
LINEQLELPNLILIDGGKGQLNAAYSILKGLKIENKVKVCALAKKEETIFLPNKKQGIKLPKGNPALRIL
QNVRDEAHRKANGFNKKLRENIKLNYTKIKGIGEKKAKKILKSLGTYKDILLLNEDEIAEKMKINIKMAK
KIKKFAEKQNLINT
>gnl|CDD|173135 PRK14672, uvrC, excinuclease ABC subunit C; Provisional
MRPSESLVETLRIQALSAPSTSGVYLWKDVHGVVIYVGKAKSLRTRLTSYFRCRHDPKTRVLMSRAAALE
YLQTQHEYEALLLENTLIKKHTPRYNICLKDGKTYPLLKLTCEPFPRIFRTRQFCQDGARYFGPFPDVQI
LDSFLKLILRTYKIRTCTTLRKRKNPCLYYHLKRCDAPCCGWVSPRTYQKDIHEITLLLEGNIDATVARL
EKRMKRAVRQEAFEAAARIRDDIQAIRCITHKSLVQDMDERARDYIAWSSTGAIVTFAVLRMRGGKLNGR
ELFRTRSLKNEEEILSEFLITYYSDHTIPPHLFVHSSAGLAEHWLSHKAGTQCTVTLIPLHTFPTPQTPS
STVTTNAPTLAASQNSNAVQDSGLRSCSETSTMHTLQKAHDACTASEGTRENTPHESAHTPHHRAILAMA
QLNAHEDITRYLKNRGADDALKELQKQLHLARIPTLIEGFDISHLGGKYTVASLICFKNGAPDTKNYRLF
NLRAHDTRIDDFASMREAIARRYTHTPEGYTLPDLILVDGGIGHVSAAQHVLDALGLSIPLVGLAKRAEE
LFIPNSPTPLVLDRRNPALHMLQRIRDEAHRFAITRNRHLRTKKELVLSFERLPHVGKVRAHRLLAHFGS
FRSLQSATPQDIATAIHIPLTQAHTILHAATRSTTAPVREEYKEHEHDPQGESPGPGRKTD
>gnl|CDD|237786 PRK14673, PRK14673, hypothetical protein; Provisional
MCHAREASPGGGAPGDNFSGAAGSTRAVGAAFEDRALAFLQRAGLALVARNYRCRGGEIDLVMRERDGTL
VFVEVRARASRRFGGAAASIGARKQRRLVAAALHFLARHGGAPACRFDVVAFEGGRLEWLRDAFRAD
>gnl|CDD|184788 PRK14674, PRK14674, hypothetical protein; Provisional
MLVAQQLGQWAEQTALKLLKEQNYEWVASNYHSRRGEVDLIVKRGNELIFVEVKARGQGNYGQACEMVTL
SKQKKIIKTAMRFLQRYPSYQDFYCRFDVICFDFPQKIAKTVQQDFSKFHYDLQWIENAFTLD
>gnl|CDD|173138 PRK14675, PRK14675, hypothetical protein; Provisional
GEDKSHNKSLGEIGESIAVTYLKGLRYKIVERNFRCRCGEIDIIARDGKTLVFVEVKTRKNYAYGVPQLA
VTPFKQRQISKAALTWLAKKKLLDAEARFDVIAITQRDHAVPEIEHIKNAFELAY
>gnl|CDD|173139 PRK14676, PRK14676, hypothetical protein; Provisional
MSGEVSYYAGQTAEEAVARIYDRSGRPVAARRWRGVSGEIDLIAREGAEVIFIEVKKSKSHAAAAARLSR
RQMDRIYGAASEFLAGEPRGQLTASRFDVALVDALGRVEIIENAFAA
>gnl|CDD|184789 PRK14677, PRK14677, hypothetical protein; Provisional
MDWKEAEELACKFLKKKGYKILERNYRTKYGEIDIVARDGREIVFVEVKSGSGKVDPLERIDLKKVRNLE
QTARFYMIQNKLKGPARVDFVRVTPEGIDHFEGIWLG
>gnl|CDD|173141 PRK14678, PRK14678, hypothetical protein; Provisional
MPTPKRRLGDWGEQVAAAYLERCGYTIIARNWRCRAGEIDIVAREGDQLVFVEVRTRRDQDALESITLAK
RQRLVALAYHYLAAHDLPATTPWRIDVIALTVRGGRIVDIDHVIAAVGED
>gnl|CDD|173142 PRK14679, PRK14679, hypothetical protein; Provisional
MRPPADPAARRRATHGRGLSAEGLALLALMLKGYRPLARRFAAAGGEIDLIVRRGRTIAFVEVKARATLD
AAATAIDARKRARFSRAARAWLARHPLAAGATLRADAVFVAPRRWPRHLPNAFEIEGL
>gnl|CDD|173143 PRK14680, PRK14680, hypothetical protein; Provisional
MADARHAIGQHGEDAAAALLQRTGHRILARNWRHGGLELDIVCEDGDTIVFVEVKTRAAHGLTSPTDALT
HSKRHRLIRAARAWLAAHDAWDKPCRFDLVCVTQRGATLTLEHYTHAFDLTETLGGGDTSWQPW
>gnl|CDD|237787 PRK14681, PRK14681, hypothetical protein; Provisional
TTKSGIDAMNAFHQPMLPSPTPPAEQPLESLAAMLGDRNLTPKQIGALGEQYAAAWLEEHGWTTLSRNWH
CRYGELDIVALNPEYTIVFVEVKTRRSMHYGYPQEAVTAAKQHNLRKAACDWLLERRNRVPHIGVRFDVV
TVVVRVGRPLVHHIENAF
>gnl|CDD|173145 PRK14682, PRK14682, hypothetical protein; Provisional
MQTIEIGNKAELQACKFLHTQALEILAHNFKALPYGEIDIIALDKDTLVFIEVKYRSKTKFAQAEEMLTY
SKQQKLVNSASIYLQHNPQYQDYQCRFDLIAINESNINWIKNAFGVI
>gnl|CDD|173146 PRK14683, PRK14683, hypothetical protein; Provisional
MPYKKNYKRVAYNTLGYLGEVLIILFLKCKLYHIIKHRYRCPLGEIDIIAHKNKQLVFIEVKTSLFNKNI
PITYKQQKSILKSAKYFIAFHRKFANYSIRFDLYFFSLSTGLIHIPNAWQES
>gnl|CDD|173147 PRK14684, PRK14684, hypothetical protein; Provisional
MFSLTQKIGFNAEKTACRYLQKQGLSFITKNFRYKQGEIDLIMSDQSMLVFIEVRYRRFSDFIHPVATVT
PLKQRRLIKTALHYLQKHRLLDKISCRFDIVGITADRQITWIKNAIEVEY
>gnl|CDD|173148 PRK14685, PRK14685, hypothetical protein; Provisional
MTDTATRLAFARAAQAQRRLHRRPPASPRARPGARDGGSPTQRCGQAYESAALRWLARQGLRPLARNLRC
RAGEIDLAMRDGEVLVLVEVRARAHAGYGGAAASIGASKQGRLARAAALLLPVLLRRHWPGAPPPVRFDV
VAFEAGRPHWLRGAFWLAEHAPAQGRRGQDAQGWRVR
>gnl|CDD|184791 PRK14686, PRK14686, hypothetical protein; Provisional
MAEHNELGKEGEDLAVEFLIKKGYTILERNYRFQKAEIDIIAQKGNILVIVEVKTRSSSDFGNPQDFVKP
KKIQLLVKAVNHYIEDKDLDVEIRFDIIAIVKNKAGFKIEHIEDAFYHF
>gnl|CDD|237788 PRK14687, PRK14687, hypothetical protein; Provisional
MMCYDNSEMLSRLIDVMANDKPLMLTSPKQRQGGGFEQLACEFLQEQGLILIARNWQQPKVGELDLVMLE
KGQAWSTLVFAEVRQRKLSGFGDAAASVTAGKQRKIIKTARYFLRQHPEYADYECRFDVIAYNTRNGKNG
QNEPNITLDNQPNQRLEILQPEWLQGAFIASAW
>gnl|CDD|184792 PRK14688, PRK14688, hypothetical protein; Provisional
MAYNRKETGEFGEKLAAEYLKGMGYSIIQTNCRLPEGEIDIVGQDGEYLVFIEVRTKRRLGYGLPAESVT
PRKKAHLMASAESYIQKHRLEHFPCRIDFVSVDLSQPEPRLELIKNALGEE
>gnl|CDD|173152 PRK14689, PRK14689, hypothetical protein; Provisional
HPLMMKSQALGAWAEERVLRLLQRRGWRLLDRNWSCRWGELDLVLEKQQRLLVVEVKGRRRRGLDGWGLA
AFHPRKRRRLARAINCWRAAHPYSAEHLLEVVLALVPLPPSRGTVRWIRIDDLD
>gnl|CDD|237789 PRK14690, PRK14690, molybdopterin biosynthesis protein MoeA; Provisional
PPPLTPPPLKNDCFALPPGVDWTPVDTALDLLRARLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQAN
SAVDGYGFAGAAPEGAQVLPLIEGRAAAGVPFSGRVPEGMALRILTGAALPEGVDTVVLEEDVAGDGHRI
AFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLRVAVLSTGDELVEPGA
LAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGASAGDEDHVSAL
LREAGAMQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAGEGWSEPQGFTVPA
AFEKRKKPGRREYLRARLRQGHAEVFRSEGSGRISGLSWAEGLVELGDGARRIAPGDPVRFIPYGSFGL
>gnl|CDD|173154 PRK14691, PRK14691, 3-oxoacyl-(acyl carrier protein) synthase II; Provisional
MGRWWRYKWITFHPSLTHADNTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLA
AGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHF
NSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYR
AMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESNALAITSTKSATGHLLGAAGGLETIF
TVLALRDQIVPATLNLENPDPAAKGLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKRWVD
>gnl|CDD|173155 PRK14692, PRK14692, flagellar hook-associated protein FlgL
MRITNKLNFTNSVNNSMGGQSALYQISQQLASGLKIQNSYEDASTYIDNTRLEYEIKTLEQVKESTSRAQ
EMTQNSMKALQDMVKLLEDFKVKVTQAASDSNSQTSREAIAKELERIKESIVQLANTSVNGQYLFAGSQV
ANKPFDSNGNYYGDKNNINVVTGAGTESPYNIPGWDLFFKADGDYKKQISTNVSFTDNRWDLNKNPDKTK
YLTGDSKWQQLIGQNYVKDGSLDPDKDFEYDDSKLDFPPTTLYVQGTKPDGTSFKSAVLVKPEDTLEDVM
ENIGALYGNTPNNKVVEVSMNDSGQIQITDLKQGNNKLDFHAVAFTPQADDKTEITNIIQAAQNEGITMD
DVTNRVMTAALNPNNGDITNLNNPVTVTINNQQFTIDLKQTDFIKSKMTDTDGNATNGADYDNVYFEKNG
NTVYGNVSQVIKGSNAYATDSTKLSEVMAGDSLNGTTLNLKVNSKGGNSYDVTINLQTSTVSYPDPNNPG
QTISFPITHTNPATGNSGVVTGSNDITYGQINDIIGMFAADNIPTATIQANNGQINNNDYTQIQQLMKDS
QATVDVSMDYKGRISVTDKLSSGTNIEISLSDSQSGQFPAPPFTTTSTVQNGPNFSFSANNSLTIDEPNV
DIIKDLDSMIDAVLKGNMRADSESEDPRNTGMQGALERLDHLADHVSKLNTTMGAYHNTIEGVNTRTSFL
SVNVQSIKSNVIDVDYGEAMMNLMQVQLAYQASLKASTTISQLSLLNYM
>gnl|CDD|173156 PRK14693, PRK14693, hypothetical protein; Provisional
MLDRAAANPDLVTRVPTLSSLSSAAMTSSAVSTTGTTNTVASGGAAAGAPSFAPPAADAFPQADGAPRNP
AVLQFPVPGGAPAPADARVAAPVVYSAQGEQAAIMKAGLQQASWNNPFVSHALPAVLQLQRHLAAGPLNQ
AAIRTQLGLEVRLYRERLAASGCEWEQIRDASYLLCTYLDETVNDAAREHAQVVYDGERSLLVEFHDDAW
GGEDAFADLSRWMKTEPPPIPLLSFYELILSLGWQGRYRVLDRGDVLLQDLRSQLHALIWHHVPPEPLGT
ELVAPAKRRRSWWTAGRAAAVALGVLVLAYGAISFWLDSQGRPIRNALAAWMPPTRTINIAETLPPPLPQ
ILTEGWLTAYKHPQGWLLVFKSDGAFDVGKANVRADFMHNIERLGLAFAPWPGDLEVIGHTDSRPIRTSE
FPDNQALSEARARNVADELRKTALPGGARAPENAVQRNIEYSGRGDAQPIDTAKTAAAYERNRRVDVLWK
VIPDGAQQSGRSLNLQQPEKPGQVPMRPAMPEGVEIAPDGQLPYATSTTMPATRPTTEGRQP
>gnl|CDD|173158 PRK14695, PRK14695, serine/threonine transporter SstT; Provisional
MIGTFAAALVAVLASFIVPIEITLNSANTEIAPPDGIGQVLSNLLLKLVDSPVNALLTANYIGILSWAVI
FGIAMREASKNSKELLKTIADVTSKIVEWIINLAPFGILGLVFKTISDKGVGSLANYGILLVLLVTTMLF
VAPVVNPLIAFFFMRRNPYPLVWNCLRVSGVTAFFTRSSATNIPVNMKLCHDLGLNPDTYSVSIPLGSTI
NMAGVAITINLLTLVTVNTLGIPVDFATAFVLSVVAAISACGASGIAGGSLLLIPVACSLFGISNDIAIQ
IVGVGFVIGVIQDSCETALNSSTDVLFTAVAEYAATRKK
>gnl|CDD|184793 PRK14696, tynA, primary-amine oxidase
MVPLDKTLKEFGADVQWDDYAQTFTIIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDGKAWVSDTFIN
DVFQSGLDQTFQVEKRPHPLNALTADEIKQAVEIVKASADFKPNTRFTEISLKEPDKEAVWAFALENKPV
DQPRKADVIMLDGKHVIEAVVDLQNNKVLSWQPIKDAHGMVLLDDFASVQNIINNSEEFAAALKKRGITD
VKKVITTPLTVGYFDGKDGLKQDARLLKVVSYLDVGDGNYWAHPIENLVAVVDLEQKKIIKIEEGPVVPV
PMTARPYDGRDRVAPAVKPLQIIEPEGKNYTITGDTIHWRNWDFHLSLDSRVGPMLSTVTYNDNGTKRKV
MYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMGTLTSPIARGKDAPSNAVLLDETIADYTGVPMEIPRA
IAVFERYAGPEYKHQEMGQPNVSTERRELVVRWISTVGNYDYIFDWVFHENGTIGIDAGATGIEAVKGVK
AKTMHDETAKEDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQVN
QYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQIIPYAGGTHPVAKGANFAPDEWIYHRLSFMDK
QLWVTRYHPGERFPEGKYPNRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWVHT
LLKPWNFFDETPTLGLLKKDQ
>gnl|CDD|184794 PRK14697, PRK14697, bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Provisional
MNRIGIIGAMQIEIDLLLEKLVVQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVD
AIINTGVAGGLHPDVKVGDIVISTNVTHHDVSKTQMKNLFPFQEEFIASKELVELARKACNSSSLHIEIH
EGRIVSGECFVEDSKLKAKLIDEYAPHCTEMEGAAIGHVAYINEVPFLVIRCISDSADDEAQISYDDFAK
TAANYCSEIIVEMLKNISSKTVL
>gnl|CDD|184795 PRK14698, PRK14698, V-type ATP synthase subunit A; Provisional
MPAKGRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGS
SLSVELGPGLLTSIYDGIQRPLEVIREKSGDFIARGISAPALPRDKKWHFIPKVKVGDKVVGGDIIGEVP
ETSIITHKIMVPPGIEGEIVEIADEGEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVP
LITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDGDTLILTKEFGLIKIKDLYEILDGKGKKTVEGNEEWT
ELEEPITLYGYKDGKIVEIKATHVYKGASAGMIEIKTRTGRKIKVTPIHKLFTGRVTKDGLEIEEVMAKD
IKKGDRIAVAKKIDGGERVKLNIRVDQKRGKKIKIPDVLDEELAEFLGYLIADGTLKPRTVAIYNNDESL
LKRANELAMELFGIEGKIVKERTVKALLIHSKALVDFFKKLGIPGNKKARTWKVPKELLISEPEVVKAFI
KAYIACDGYYDEEKGEIEIVTASEEAAYGFSYLLAKLGIYAIIREKIIGDKEYYRVVISGEANLEKLGIE
REARGYTSIDIVPVDVEEIYEALGRPYAELKKAGIEIHNYLSGENMSYEMFRKFAKFVGLEEIAENHLQH
ILFDEIVEINYISEGQEVYDITTETHNFIGGNMPTLLHNTVTQHQLAKWSDAQVVIYIGCGERGNEMTDV
LEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALR
EISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV
KVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGP
DALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAISRGVPLEEIAKLP
VREEIGRMKFEPDIEKIKALIDKTNEQFDELFKKYGA
>gnl|CDD|173162 PRK14699, PRK14699, replication factor A; Provisional
MTDIETIYKKLSHVISKEDFLQRIQEKVENMGGLCDEPMAAMLVANELGFSDAGRDSVKIENITPESGPV
NFIARVVSVFDTKEFTRNDGTIGRVGNLIVGDETGKIKLTLWDNMADLIKAGKIKAGQTLQISGYAKQGY
SGVEVNIGNNGVLTESEEEIDVAANSQKIKDIKDGMGDLNLTGKVLEISEIRTFQRKDGTSGKVGNLLLG
DETGTLRVTLWDDKTDFLNQIEYGDTVELINAYARENAFTQKVELQVGNRSIIRKSEKKVEYEEEFTPIE
DIKADMNNINISGRVLDISEVRTFEKKDGSPGRVGNLLLGDSTGKIRLTLWDEKTNFLDEIDFDETVEVL
NAYSRENTFSQQVELNLGARGIIQKSEKKVEYREKFTDIADIIPGESYSVQGKVSEIGELREFEREDGTE
NVVANLQLKDETGSIRLTLWGEQAYVIEDLDIDSEIQIIDAYARYGLNEEIELSVGNRSRVIIL
>gnl|CDD|173163 PRK14700, PRK14700, recombination factor protein RarA; Provisional
MPYVESGKIILIGATTENPTYYLNDALVSRLFILRLKRLSLVATQKLIEKALSQDEVLAKHKFKIDDGLY
NAMHNYNEGDCRKILNLLERMFLISTRGDEIYLNKELFDQAVGETSRDFHREGKEFYEQLSAFHKSVRGT
DPDAAIFWLSVMLDNGVDPLVIARRMLCIASEDIGNADPQALRVAMDAWNAYEKLGMPEGRLVLAQAAIY
LAVAPKSNACYKALAQAQQLVKSLGNIDVPQHLKNYKDSNYLYPHNYPNSYVIQQYLPDNIIQNFYQPTA
SGFEAKIKTKLDSINKIKKL
>gnl|CDD|237792 PRK14702, PRK14702, insertion element IS2 transposase InsD; Provisional
DGRRSRHTDDTDVLLRIHHVIGELPTYGYRRVWALLRRQAELDGMPAINAKRVYRLMRQNALLLERKPAV
PPSKRAHTGRVAVKESNQRWCSDGFEFCCDNGERLRVTFALDCCDREALHWAVTTGGFNSETVQDVMLGA
VERRFGNDLPSSPVEWLTDNGSCYRANETRQFARMLGLEPKNTAVRSPESNGIAESFVKTIKRDYISIMP
KPDGLTAAKNLAEAFEHYNEWHPHSALGYRSPREYLRQRACNGLSDNRCLEI
>gnl|CDD|237793 PRK14703, PRK14703, glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
MSDAPRPRMLVSPNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRM
DDTNPETEDTEYVEAIKDDVRWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGT
VTEPGTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEW
CIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWPPRPRQYEFARLALGYTVMSKRKLR
ELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVMA
VLDPLKVVIENLPAGKVEELDLPYWPHDVPKEGSRKVPFTRELYIERDDFSEDPPKGFKRLTPGREVRLR
GAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDTGRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEA
ADEDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTWGARA
REAAREKRAAAPKKTAKPRRSKAEARAEAAALNPEQRARFDRYLSELGLNEEDARTLARDPALAAFFEAA
LAAGKSPVQLANWVVNDLAGLLRDRELAALPFTPAALARLVALVDAGRISTRIAKDVLAELAASGGDPEA
IVEAKGLEQVSDAGALEPIVEEVLAAHPDKVAAYRAGKTKLLGFFVGQVMRETGGKANPQQVRELLQKKL
G
>gnl|CDD|184798 PRK14704, PRK14704, anaerobic ribonucleoside triphosphate reductase; Provisional
MLQKNTRGEELMRVFETIVHGNEQDLMQENANVDGRSPMGVMGTFASESAKYYAVENLLSDQVKKAINEN
ILYPHDLDFYATGTTTCSQIPLAQMLANGFHTGHGHMRQPQDIKSALALSSIIFQANQNMQHGGQSFALF
DVDLAPYVRKTVERHKKRLQSYPLTKEQIEEFAWKETENDTYQACEAFIHNSNSMHSRGGGQVPFISINY
GTDTSKEGRLLIKQLLKATQAGLGKGETPIFPIQIFKMKKGVNFEESDPNYDLFELALETTAERLFPNFS
FLDAPFNAVHYDGRPESEVCYMGCRTRVMSNIHGEETAIGRGNLSFTSINLVKLALISGSKEAFFEALNY
YLDLGIKQLLERFEYQCTKRARDFRFLYSQGVWRGGEKLQPEDSVASILKQGTLSLGFIGLAECLVALTG
KHHGEDEESWKLGYEIISFMRDRMDKATEEHELNFSVIATPAEGLSGKFVKKDREEFGVISGITNHNYYT
NSFHIPVYYNIQAINKIRLEGPFHALCNGGHITYIELDGAAMHNKKALKQIVQAMAEHGVGYGSINHPVD
RCKCCSYHGVIGNECPSCGNEDEANIERIRRITGYLVGDMSKWNSAKRSEEMDRVKHK
>gnl|CDD|237794 PRK14705, PRK14705, glycogen branching enzyme; Provisional
MSQANLNPSLEGLLRNWLPGQRWFPVKSPDFALSQVGSFSLPDTSGEAGLEVFLLAVTHRTADGGSRTDV
VQVPLSYRSQPLTGAESALVGEFTDPDLGRRWVYDAVHDPDFVTAWLELMRSEGTVAGGVARGHLTRGDY
RLPTAPGSVKVLSGEQSNTSVIVDDGDSAAIVKFFRVLSAGKNPEVELGAALTAAGTSEVPATLGWVTGE
WDGPASNAGATARAVTGELAVAHEFLAGGLDAWRLAVDAAASGKDFTAEARALGAATATVHRRLAETLGT
HDGQEQGPDIAAGVARRVRGSWAEAGPAVGPYDHALDELLSALDGRNAGQLQRIHGDLHLGQILQVPGAE
GQPERWAILDFEGEPLRPIDERNSPDVPLRDVTGMLRSFDYAAGAATRENEGAHVPESWVDDCAAAFLAG
YSEVTPGTIDRRSPLFVALWLDKALYEVVYELRNRPDWLSIPVNASRRLLDNTGRGKHAAAAAEGNDMTG
SARTERPGAPLHVDSETLEKVAAGEYHAPHSVLGAHLDDHGHVTVRTVKHLAKAVSVVTAAGRVPMTHEA
HGVWAAVLEPLQAGHVPDYRLEVTYDGAEPVTIDDPYHYLPTVGEVDLHLIGEGRHEKLWDVLGAHVQHY
KSSLGDVDGVSFAVWAPNAQAVRVKGDFNGWDGREHSMRSLGSSGVWELFIPGVVAGACYKFEILTKAGQ
WVEKADPLAFGTEVPPLTASRVVEASYAFKDAEWMSARAERDPHNSPMSVYEVHLGSWRLGLGYRELAKE
LVDYVKWLGFTHVEFMPVAEHPFGGSWGYQVTSYFAPTSRFGHPDEFRFLVDSLHQAGIGVLLDWVPAHF
PKDSWALAQFDGQPLYEHADPALGEHPDWGTLIFDFGRTEVRNFLVANALYWLDEFHIDGLRVDAVASML
YLDYSREEGQWRPNRFGGRENLEAISFLQEVNATVYKTHPGAVMIAEESTAFPGVTAPTSHGGLGFGLKW
NMGWMHDSLKYASEDPINRKWHHGTITFSLVYAFTENFLLPISHDEVVHGKGSMLRKMPGDRWQQLANLR
AFLAYQWAHPGKQLIFMGTEFGQEAEWSEQHGLDWFLADIPAHRGIQLLTKDLNELYTSTPALYQRDNEP
GGFQWINGGDADRNVLSFIRWDGDGNPLVCAINFSGGPHKGYTLGVPAAGAWTEVLNTDHETYGGSGVLN
PGSLKATTEGQDGQPATLTVTLPPLGASFFAPAE
>gnl|CDD|237795 PRK14706, PRK14706, glycogen branching enzyme; Provisional
SFLPLPLDHGHLQKLVTADLVRPDHLLGAHPATEGGVEGVRFAVWAPGAQHVSVVGDFNDWNGFDHPMQR
LDFGFWGAFVPGARPGQRYKFRVTGAAGQTVDKMDPYGSFFEVRPNTASIIWEDRFEWTDTRWMSSRTAG
FDQPISIYEVHVGSWARRDDGWFLNYRELAHRLGEYVTYMGYTHVELLGVMEHPFDGSWGYQVTGYYAPT
SRLGTPEDFKYLVNHLHGLGIGVILDWVPGHFPTDESGLAHFDGGPLYEYADPRKGYHYDWNTYIFDYGR
NEVVMFLIGSALKWLQDFHVDGLRVDAVASMLYLDFSRTEWVPNIHGGRENLEAIAFLKRLNEVTHHMAP
GCMMIAEESTSFPGVTVPTPYGLGFDYKWAMGWMNDTLAYFEQDPLWRKYHHHKLTFFNVYRTSENYVLA
ISHDEVVHLKKSMVMKMPGDWYTQRAQYRAFLAMMWTTPGKKLLFMGQEFAQGTEWNHDASLPWYLTDVP
DHRGVMNLVRRLNQLYRERPDWHRGDKREEGLYWVSADDTDNSVYAYVRRDSESGAWSLAVANLTPVYRE
QYRIGVPQGGEYRVLLSTDDGEYGGFGTQQPDLMASQEGWHGQPHSLSLNLPPSSVLILEFVGDVPTLTY
RQPEDSPQA
>gnl|CDD|173170 PRK14707, PRK14707, hypothetical protein; Provisional
MSMAYDNELAHRMRNGMALPFLEESVNAQVNAQRLDKYLQLIATARRARAGVTPRDLDRCTELAAQYLSG
TGWFEGASLAQLAHVGNKLSKHPNQPACMEAIAWIAGELTQADDLVGLGGYPSALFLNAFSKNLDSGRCE
RAVARLARHLRREDKARQTLNAQNISLALNAFSKWSDNPDCQAVAPRFAALVASDDRLRSAMDAQGVATV
LNALCKWPDTPDCGNAVSALAERLADESRLRNELKPQELGNALNALSKWADTPVCAAAASALAERLVDDP
GLRKALDPINVTQALNALSKWADLPVCAEAAIALAERLADDPELCKALNARGLSTALNALSKWPDNPVCA
AAVSALAERLVADPELRKDLEPQGVSSVLNALSKWPDTPVCAAAASALAEHVVDDLELRKGLDPQGVSNA
LNALAKWPDLPICGQAVSALAGRLAHDTELCKALDPINVTQALDALSKWPDTPICGQTASALAARLAHER
RLRKALKPQEVVIALHSLSKWPDTPICAEAASALAERVVDELQLRKAFDAHQVVNTLKALSKWPDKQLCA
VAASGLAERLADEPQLPKDLHRQGVVIVLNALSKWPDTAVCAEAVNALAERLVDEPDLRKELDPVDVTNV
LNALSKWPGTEVCAEVARLLAGRLVGDRLLRKTFNSLDVANALNALSKWPDTPVCAAAAGGMAERLAADP
GLRKELNPVDVANALNALSKWPRTPVCAAVASALAARVVAEPRLRKAFDAQQVATALNALSKWPDNQACA
AAANTLAERQLREPDVRDVLKPREMTNALNALSKWPDTPACAAAASALAARVADDPRLREAFDVQHVATV
LNAMSKWPDNAVCAAAAGAMAERLADEPELRHTLTAHGVVIVLNALSKWPNVPVCAAAASALAERLADEP
ELRKALSAHRVATALNALSKWPDIPVCATAASALAERLSDDPDLREALDASNLPQVLNALSKWPDVPAGG
EVVDALAERLVDEPALRNALDPIGMANALNALSKWLQMPVCAATVEALAARLSNDPGLCKALSSQGLTTV
LNALCKWPEMPVCLAAASALAERLSDDLVLRNALDSQGFGNALNALSKWPDSPVCAAAASALAKRLTDDA
GLRHVFDPINVSQALNALSKWPGTQACESAIDVLAATLANAPGLRNALSAQGVAIALNALSKCLARPVCR
SAFVLLAERAGSAELPWRQFEMRGIAVVANAMSRLSPLDEEDDEQFRTLAVAKLQAMAGHLDLHRELFAS
ASVADIGVLFKALASARLQRQMRSLGQPALERVSALIGDDGLRQTSLEGIGSLCMGLLPLIRSPELTPRH
RGQALHVFNTLQPIVARKIDLYLRSDGARASAAVEQHATRCPALTFYQVLKAYAVVSRQWKARHLDGPRK
QLRQRRDELLKWVDLTLARTREAIEADLGEMSWNLIAQIEAGEQVFDALDLRMAKDAPAITQAHPPTRFD
LDSGRLSMASVPGRPVAPAPGRGSTTHVVVDLVGKELSTNRSESDKPYSLFARLTGLPLVEVQLPGELST
FMLARTFNYNGEPWRFDLFGGSRAARSKSGSGSLVLSHRKESASLLPAFRYADTAPGSSLMHLAAKLAPQ
REDWSRMQRSLLEMVPSDHVVEGTLRLGVFDDVEGPAHPFKPLAVDGTALALCPNDGCGFLKLEVALAIP
AFRKHYDAWHAVQANQATEEQRDLVAKDKGPSMMPAQALHHYPRDAAALEEAHAAMQERLQTLEPAGDDP
LWVYRPLIGGGYKGQRVRAVPSADDKVHLPQQRSQAFDVTGGPLLLGKPPYDKENLLPVPEQRIATVAKG
DATAAFLSQCFGIQYSYTGFDDRSGVDPQMLHSKGMLVVVPEQQWPAAFSDTDLACSKEDLKTLSCWTNG
RDRGALPRDILSTGSLRLKDIVEPGRLGALPIDELRKRDMDTDGDDAFIYAGYPKLAALISRVMDRKARL
GRQKSFKPPKTATPAIDPVSGHYQPGRLSEIMALKRGQRITSAAATLAARFMGQPDELREAMARDMMFGT
YDGIERGLRDGLRELLEEQVRDPQVLATLRVQAREAIKRAHLPEAREAAELLHAQLRALAADPAADSAAP
ALPEALAEAFPGLAKAYEAASGVDARIHAILDNYPVCRLSHAQFPDGQPGLVPGEPELTMRNLFTIAIKV
GTDALKSDTGTALFAKIVEACERAERCFAERVRSLPYSRVTARAMQDGRFDPEQTKLLLQRMPSMAAGVM
EDALEALQQAGWIDRSQPPAERLRDVQPQDIALKAQTLLGRARQMEPQVTDMLQNIAARHGGQLAGTQHQ
LKSYSSLQEKLKQRVALKKQSLEEAAASVNDALRYSVVLEPQGFTAGLRAVLAALDDQGHARVKLTNQFT
EYSPSFKAINLTLRSPEGALWEIQFHTPETFALKERFHDLYKRTHALALGGASRAEQRTLQAPALEAFKR
VASPPGCEEIDDWQEETVPALAGTPPALASEQTPVNAGASPAHRVFNAATGKQASLTPVLNTLADGLGAR
LWGNVRYKASQGRIEQVQQAPFQKSLASIKDKIRRHLRAGMTAEQATQSVGDALRYALELPSEGFVAKVQ
AAQDALRRQGMTCVNLQNYFTSGDGTYRGINASFTDAEGYAFEVQFHTAESFNAKAQTHLSYKRMQLAQA
RLDRERQKPQPDPIRQANLTQEIAGHKKAMHEMTANVSKPAYIERLGGRA
>gnl|CDD|173171 PRK14708, PRK14708, flagellin; Provisional
MSGVVLSNAVRQNLSSLQATADLLATTQSRLSSGKKVNTALDNPTNFFTAASLDSRASDINNLLDGIGNG
VQILQAANTGITSLNKLVDSAKSIANQALQTNVGYATKSNVSATIAGATADDLRGTQSFSNAVATSNVIF
DGTAGGTSTASGTDTLGGGIVSIAAGTAVTVLGAADATALGSVLSVGTAAATATGADLISSLTNGSTATA
TGPAAGDSITVNGKTITFTTAGAATADSNGNYTIGLDQTLTALLATIDTINGNTTNPSVVTAGKLELHSG
TNSPLTISDNAGGAVLAKLGLGAQVTTTAGTTAAANISATTQLFNTHGGLSTTAIADGTTLTVNGKTITF
KTSDAPQGNNILTGSGVLGRIGTDGNGNSTIYLGTQNTFTNATVGDVLTAIDLANGVKSATISNGVATIS
TNAGQTASIVTAGIVTIQSSTGADLNVTGPTDLLKNLGLTTSTGSGPLTLTKQRTTSGTTMGTLIADGST
LNVNGKTITFKNAAVPTASASHTGISGNVETDGQGNSTVYLQKGTLDDVLKAIDLATGVQTATLGQSGAT
ISTANGSANSSITSGSLKLSTGLASDLSITGTGNAMLALGLTGPSGTSTSFTASRGASAGSLNGKTLTFT
SFNGGAPVNVTFGDGTNGTVKSLAQLNVALAANNMTASIDNANGKLTISTSNDYASHTLGGADGGVLGGT
ITSTLTFTTPNAPVADVNAQNTRAGLVKQFNDVLDQIKTTAQDASFNGVNLLNGDTLKLVFNETGKSTIS
IQGVTFNPTGLGLSTLVSGVDFIDNNATNAVLAKLSTASTTLRSQASAFGSNLSIVQARQDFSKSLINVL
QTGSSNLTLADTNEEAANSQALSTRQSIAVSALSLANQSQQGVLQLLR
>gnl|CDD|173172 PRK14709, PRK14709, hypothetical protein; Provisional
MSAAETLGRPGDAEPEAKRKSAPKSDARMFDDLLTEDSVAAVFAERYGGRLRFCHDTGKWFEWTGTAWKQ
DRVGLAFHWARELVREMCRGEPPKLRYIASKASFAGGVEKFARTDPRFAVTSEDWDADPWLLGTPGGTVD
LRTGKLRAADPEDMITRLTAVAPADTADCPRWLRFLDEATGGDDELIRFLQQWCGYCLTGDTREHALVFV
FGGGGNGKSVFLNVLAGILGDYATTAAMDTFTASKHDRHPTDLAMLRGARLVTASETEEGRAWAEARIKQ
MTGGDTITARFMRQDFFEFVPQFKLTIVGNHKPRLRNVDEAARRRFNIVPFTRKPARPDPDLEAKLRAEW
PAILRWMIDGCLDWQANGLVRPAAVTEATEEYFAEQDTFGQWLEERCIVDPGNPVCWDVLQDLYASWCEF
ARAEGEPAGTAKEFGERMEKLGFKKDRKNRGRGFRGIQLRPLPDLSGES
>gnl|CDD|173173 PRK14710, PRK14710, hypothetical protein; Provisional
MLAISSNLSKMIIFIFAIIIIVVLCVITYLYLYKDESLVSKHYINYMAIPENDGVFTWLPDFFPHVAVDI
SIYTNVEDDYFFLIFP
>gnl|CDD|173174 PRK14711, ureE, urease accessory protein UreE; Provisional
MIIIEGIVGNSHDPQWRDRLADAKIDWLVLDQWEAQKSRLRKATSGDVELALSLDRNTHLHDGDILLWNE
GDKCAVVARVHLKEVMVIDLASVIGEDGNAIVRTVFELGHALGNQHWPAVVKETKVFVPLTVDRKVMASV
MKTHNLPGVTYEFMPGADVIPYMAPHEARRLFGGADSMLQSHGHQHGQEHH
>gnl|CDD|237796 PRK14712, PRK14712, conjugal transfer nickase/helicase TraI; Provisional
VLTGNLVMALFNHDTSRDQEPQLHTHAVVANVTQHNGEWKTLSSDKVGKTGFIENVYANQIAFGRLYREK
LKEQVEALGYETEVVGKHGMWEMPGVPVEAFSGRSQTIREAVGEDASLKSRDVAALDTRKSKQHVDPEVR
MAEWMQTLKETGFDIRAYRDAAEQRAYTRTQTPGPASQDGPDVQQAVTQAIAGLSERKVQFMYTDLLART
VGILPPENGVIERARAGIDEAISREQLIPLDREKGLFTSGIHMLDELSVRALSRDIMKQNRVTVHPEKSV
PRTAGYSDAVSVLAQDRPSLAIVSGQGGAAGQRERVAELVMMAREQGREVQIIAADRRSQMNLKQDERLS
GELITGRRQLLEGMAFTPGSTVIVDQGEKLSLKETLTLLDGAARHNVQVLITDSGQRTGTGSALMAMKDA
GVNTYRWQGGEQRPATIISEPDRNVRYARLAGDFAASVKAGEESVAQVSGVREQAILTQAIRSELKTQGV
LGHPEVTMTALSPVWLDSRSRYLRDMYRPGMVMEQWNPETRSHDRYVTERVTAQSHSLTLRNAQGETQVV
RISSLDSSWSLFRPEKMPVADGERLRVTGKIPGLRVSGGDRLQVASVSEDAMTVVVPGRAEPATLPVSDS
PFTALKLENGWVETPGHSVSDSATVFASVTQMAMDNATLNGLARSGRDVRLYSSLDETRTAEKLARHPSF
TVVSEQIKARAGETLLETAISLQKAGLHTPAQQAIHLALPVLESKNLAFSMVDLLTEAKSFAAEGTGFAD
LGGEINAQIKRGDLLYVDVAKGYGTGLLVSRASYEAEKSILRHILEGKEAVTPLMERVPGELMEKLTSGQ
RAATRMILETSDRFTVVQGYAGVGKTTQFRAVMSAVNMLPESERPRVVGLGPTHRAVGEMRSAGVDAQTL
ASFLHDTQLQQRSGETPDFSNTLFLLDESSMVGNTDMARAYALIAAGGGRAVASGDTDQLQAIAPGQPFR
LQQTRSAADVVIMKEIVRQTPELREAVYSLINRDVERALSGLERVKPSQVPRLEGAWAPEHSVTEFSHSQ
EAKLAEAQQKAMLKGEAFPDVPMTLYEAIVRDYTGRTPEAREQTLIVTHLNEDRRVLNSMIHDAREKAGE
LGQVQVMVPVLNTANIRDGELRRLSTWENNPDALALVDNVYHRIAGISKDDGLITLQDAEGNTRLISPRE
AVAEGVTLYTPDTIRVGTGDRIRFTKSDRERGYVANSVWTVTAVSGDSVTLSDGQQTRVIRPGQERAEQH
IDLAYAITAHGAQGASETFAIALEGTEGNRKLMAGFESAYVALSRMKQHVQVYTDNRQGWTDAINNAVQK
GTAHDVFEPKPDREVMNAERLFSTARELRDVAAGRAVLRQAGLAGGDSPARFIAPGRKYPQPYVALPAFD
RNGKSAGIWLNPLTTDDGNGLRGFSGEGRVKGSGDAQFVALQGSRNGESLLADNMQDGVRIARDNPDSGV
VVRIAGEGRPWNPGAITGGRVWGDIPDNSVQPGAGNGEPVTAEVLAQRQAEEAIRRETERRADEIVRKMA
ENKPDLPDGKTEQAVREIAGQERDRAAITEREAALPESVLREPQRVREAVREVARENLLQERLQQMERDM
VRDLQKEKTPGGD
>gnl|CDD|237797 PRK14713, PRK14713, bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase
TPSEPLLVPTATGMSAMTNSAAAASAAATPRVLSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQ
NTRGVRAVHVPPADFLRAQLDAVSDDVTVDAVKIGMLGDAEVIDAVRTWLAEHRPPVVVLDPVMVATSGD
RLLEEDAEAALRELVPRADLITPNLPELAVLLGEPPATTWEEALAQARRLAAETGTTVLVKGGHLDGQRA
PDALVGPDGAVTEVPGPRVDTRNTHGTGCSLSSALATRLGRGGDWAAALRWATAWLHGAIAAGAALQVGT
GNGPVDHFHRARRLAADASAEAGVSAEPAPDAVVGPAGPFTAALWQASGPIREAIEDLPFVRALADGTLP
EEAFEFYLAQDALYLNGYSRALARLAALAPDPAEQVFWAQSAQACLEVESELHRSWLGDRDADTAPSPVT
LAYTDFLLARAAGGSYAVGAAAVLPCFWLYAEVGAELHARAGNPDDHPYAEWLQTYADPEFAAATRRAIA
FVDRAFRAASPAERAAMARAFLTACRYELEFFDQARRRAG
>gnl|CDD|237798 PRK14714, PRK14714, DNA-directed DNA polymerase II large subunit
MEMSPEMERYFERLERELDKAYEVAEAARARGLDPSPEVEIPIARDMADRVENLLGIDGVAERIRELEGE
MSREEAALKIVDDFVEGKFGDYDTKEGKAEGAVRTAVALLTEGVVAAPIEGIARVEIKKNDDGTEYLAVY
YAGPIRSAGGTAQALSVLVGDYVRAKLGIDRYKPREEEIERYAEEIDLYDSETGLQYSPSEKEIRLIAEN
CPIMIDGEATGDEEVSGHRDLERVETNSLRGGMCLVLAEGIALKAPKIQKYTRKMKEEGWDWLQELIDGT
IEGKSDAGEEGEEEELSTDADEYEKGPPRIAPSDKYLRDLIGGRPVFSHPSRNGGFRLRYGRSRNTGFAT
AGVHPATMHLVDDFLAVGTQMKTERPGKAAGVVPVDTIEGPTVKLANGDVRRVDDPEEALEVRNGVEEIL
DVGEYLVNYGEFVENNHPLLPASYCEEWWIQELVKAGADVQALEDKPFVDLTRPTVEEAAHWATEYGAPL
HPYYTYLWHDISVEQVRALADAVADAETRGIGFADDGVLVLPLTPTVKRTLELLLVPHTVREDRIRIPDW
RPLLRSLGLDLSSEAALEWEFAPKDGHNAIDLINELAPFKVRERAPTRIGNRMGRPEKSKPRKMKPPVHT
LFPIGEAGGAQRDVAKAAKHAPDMSDEGGVIEVEVGRRRCPSCGTETYENRCPDCGTHTEPVYVCPDCGA
EVPPDESGRVECPRCDVELTPYQRRTINVKEEYRSALENVGERENAFDLLKGVKGLTSREKIPEPLEKGI
LRAKHDVYVFKDGTVRYDMTDLPVTHFRPREIGVSVEKLRELGYTQDIHGDPLVHEDQVVELKVQDIVLS
DGAAEYLLKVAKFVDDLLEKFYGLPRFYNVEKREDLVGHLVIGLAPHTSAGVVGRIIGFTSANVGYAHPY
FHAAKRRNCFHGDTRILVQDDGGWHRDPIRIFVEERLDLEDPGYDDFGTVYQKPKRDVKVYSVDENGKVV
LTDITSVSKHPAPDHLIRFETERGRSLTVTPDHAMLVWDGGYLEKKRAFEVKEGDAVPVPEGVEETGVVL
ADEVVSIEYVESDDDFVYCLTVAEYHTVVANGIFTGQCDGDEDCVMLLLDGLLNFSKSFLPEKRGGKMDA
PLVLTSRIDPSEIDDEAHNMDVVRYYPLEFYEATLEMADPKDVEDLIERVEDRLGTPEQYEGFGFTHDTS
DIALGPKLSAYKTLGSMLDKMDAQLELARKIRAVDEHDVAERVINYHFIPDLIGNLRAFSRQEFRCLKCG
TKYRRMPLAGKCRKCGGRIILTVHEGSVEKYLDTAKMVATEYNVREYTKQRLEVLDRDIESLFENDKNKQ
SGLADFM
>gnl|CDD|237799 PRK14715, PRK14715, DNA-directed DNA polymerase II large subunit
MVHVAYSEEMKAYFENIQREVDRIYKIAEKCRAKGKDPSDDVEIPLATDMADRVEGLVGPKGVAERIREL
VKELGKEPAALEVAKEIVEGKFGDLSKEKYAEQAVRTALAILTEGIVAAPLEGIADVKIKRNEDGSEYLA
IYYAGPIRSAGGTAQALSVLVGDYVRKKMGLDRYKPSEDEIERYVEEVDLYQSEVGRFQYSPEADEIRTA
MRNIPIEITGEETDDVEVSGHRDLPRVETNHLRGGALLVLVEGVLLKAPKILRHVDKLGIEGWDWLKELK
EKKEEKDEEKSEEVKTEEVDEEFEEEEKGFYYELYEKVNIEANKKFIKEVIAGRPVFAHPSTNGGFRLRY
GRSRNTGFATWGFHPALMYLVDEFMAIGTQLKTERPGKATCVVPVDSIEPPIVKLKNGSVVRVDTIEKAI
EVRNRVEEILFLGDALVNYGDFLENNHTLLPSNWCEEWYEQELIAKNIEYDPEFINNPTPEEAIHFALVT
DTPLHPRYTYYWHDVSKEEIELLRKWLLGGKEEWFEGKKNVWAVKVVLEDDKKIKRILELIGCPHRVERS
ENRNKVIVIEEYYPLLYSLGTDLENLKDLVQNWEEKAKPFKNVIHFINLLSRFELRRRGYSYIGARMGRP
EKAAPRKMKPPVNVLFPIGNAGGQVRLINKAVEENKTDDIEIAFFKCPKCGKVGLYHVCPFCGTRVELKP
YARREIPPKDYWYAALENLKINKPGDVKCIKGMTSKYKIVEPLEKGILRAKNDVYVFKDGTIRFDCTDVP
ITHFKPSEINVSVEKLRELGYDKDIEGKPLERDDQILELKVQDVIIPYNCAEYFLKVARFIDDLLEKFYK
LDRFYNVKKKEDLIGHLVIGMAPHTSAGMVGRIIGYSDALVGYAHPYFHAAKRRNCFPGDTRILVNIDGN
VERITLRELYELFDDEVYENMAYVRKKPKNDIKVYSFDPENKKVVLTDIEEVIKAQSPNHLIRIELDLGR
SFETTVDHPVMVYENGKFIKKRAMDVKEGDLMLIPKLDFEEDNIEEIDLLKEFSKEEFKDLWDRLRVRGI
SNWIKENIGKHVKEELKLAKYLRRDTIPLDVLLIVLKEKELSIDDVPKDCYIAVKRDKVNIKRIIKIEPL
LKVIGYYLAEGYARESKSVYQINFSNAEEEVREDIKKALREAFGDGFGIYERGGKVTVGSRILYLLFTEV
LKAGKNAHSKRVPSFVFKLPKEKVKLMLSAYFEGDGSALKTVPRVVVYSANKKLLEDIDTLLLAKFGIRG
YWTADKNANRGGARVRKYHEERGTEAPKSKVYALNIAGEYYDRFFEEIGFVSERKQSIYELHKNKVRKAD
KYLSENGWIVKVRRVEIIKPEDEFVYSLNAKKYHNVIINENIQTHQCDGDEDAVFLLLDAFLNFSKYFLP
DKRGGQMDAPLVLTTRLDPKEVDGEVHNMDTMWYYPLEFYEKTLEMPSPKEVKEFIETVEDRLGKPEQYE
GIGYTHETDDIGLGPKICAYKTLGSMLEKTARQLAVAEKIRATDERDVAEKVIQSHFVPDLIGNLRAFSR
QEFRCKCGAKYRRVPLKGKCPKCGSKLILTVSKGAVEKYMPVAKMMAEKYNVNDYTKQRLCIIKEGIKSL
FENDKRKQVKLDDFFKS
>gnl|CDD|237800 PRK14716, PRK14716, glycosyl transferase family protein
RGWLVELIAAMLDALRVVLLVVAVLILLSGLDDLFIDAVYLARRLYRRRSRIPRLSLATLRSVPEKRIAI
FVPAWREADVIGRMLEHNLATLDYENYRIFVGTYPNDPATLREVDRLAARYPRVHLVIVPHDGPTSKADC
LNWIYQAIFAFERERGIRFAIIVLHDAEDVIHPLELRLYNYLLPRHDFVQLPVFSLPRDWGEWVAGTYMD
EFAESHLKDLPVREALGGLIPSAGVGTAFSRRALERLAAERGGQPFDSDSLTEDYDIGLRLKRAGFRQIF
VRVRADDTTDRPDRRGEPIATREFFPDTFKAAVRQKARWIYGIAFQGWERLGWKGPAATKYMLWRDRKGL
LTNLLLFLAYLLLLLVALVLFGSWLGGWAWSYGSPLPPGPWLQALLWVNLAILLLRVLVRAYFVGRLYGW
REALLSIPRMVVGNIINFAATARAWRLYIRSLLTGKPLVWDKTEHDFPSAEALAGVRRRLGDLLLSWRAA
SSADLPVALALRRA
>gnl|CDD|184803 PRK14717, PRK14717, putative glycine/sarcosine/betaine reductase complex protein A; Provisional
MDLENQKRIKELAEKYGAENIVVILGAAEAEAAGLAAETVTNGDPTFAGPLAGVQLGLPVYHIVEPEIKE
AVDPDVYDEQVGMMEMVLDVDEIIAEMKDIREEYCKF
>gnl|CDD|237801 PRK14719, PRK14719, bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional
MDKQESLEKLLLIIDDLKLLAEKGIPILVEGPNDILSLKNLKINANFITVSNTPVFQIADDLIAENISEV
ILLTDFDRAGRVYAKNIMEEFQSRGIKVNNLIRKEIIKYSRGDLKDIESLYPYISRRININSDLSDIMLP
YVISNVGMTLDGKLATIENDSRISGENDLKRVHEIRKDVDAIMVGIGTVLKDDPRLTVHKINASPKDNPL
RIVVDSNLKIPLNARVLNKDAKTVIATTTPISDEKEEKIRKLKEMGITVLQAGVQKVDLRKIMNEIYKMG
INKILLEGGGTLNWGMFKENLINEVRVYIAPKVFGGANSPTYVDGEGFKNVEECTKLELKNYYPLDDGIV
LEYRVIGSFK
>gnl|CDD|184804 PRK14720, PRK14720, transcription elongation factor GreA
MSNIDIDKLTSLLNEEKWTRADANNYSLSKFKELDDLIDAYKSENLTDEAKDICEEHLKEHKKSISALYI
SGILSLSRRPLNDSNLLNLIDSFSQNLKWAIVEHICDKILLYGENKLALRTLAEAYAKLNENKKLKGVWE
RLVKADRDNPEIVKKLATSYEEEDKEKAITYLKKAIYRFIKKKQYVGIEEIWSKLVHYNSDDFDFFLRIE
RKVLGHREFTRLVGLLEDLYEPYKALEDWDEVIYILKKILEHDNKNNKAREELIRFYKEKYKDHSLLEDY
LKMSDIGNNRKPVKDCIADFEKNIVFDTGNFVYHRTWGVGKITSISDNGIFVDFVSKRGHKLSIQMAITA
LKPLKRDHIWVLKAVEPKEELVDKFKKDIPWALKTIIKSYDNRMDLKDIKSELVPSLLTQSEWSKWSTKA
KQILKKNPNFGMDPKKKDEYVYRERPINLSEKLSDKFKAEKDFNKRLEIAMEYCKGAVDDSDIAEEMLEY
FLIFYNEFEKVDDPVISAYLILKSLGNELPDEEFKRNIEEDELLELILKLYSKDIVELFDAILNAEIKKE
FVDLIKKHLSNWEEYYKGLFPHKVNKYVFDSLYEEGKFDELNSLFKYVIKNYKEYPEAFIWVAKSILSYS
WELDYLDSSEELLLNLIRILKDPLRKIENKGNKLKNKRIYKMVKNILFGKDKYLLRVIIHSGDEEYIRRL
YALVPYVKDLEPKDLYELKVEIKPDFAWFEFEDEKEQDGDKLTRVPEIGFLVTRRALNKKKKELEHLKDV
EMPENSKDIGEAQELGDLRENAEYKAAKEKQQQLQAALKRLEAEIDSAKILDLTDVKTSKVGFGTKVKLK
NEDTGEEESYSILGPWESDPEEGIISYQSPLGKSLLGKKEGDSLEFVINDTETRYTVLKIERASLQ
>gnl|CDD|173184 PRK14721, flhF, flagellar biosynthesis regulator FlhF; Provisional
MKVRKFLAATSHEVLRKVKEELGPDAVILSNKQVPGGIEIMALAGKDISSLTSDTPEEATIPETTVKPTA
PPRQKPASGQPQPPAIHKQPATQPPAADIPSANIMQEIRAMRQMLEEQLTTMGWSNFSQRDPGGMKVLRT
LLSAGFSPLLSRHLLEKLPADRDFEQSLKKTISLLTLNLRTIGGDEIIEQGGVYALIGPTGVGKTTTTAK
LAARAVIRHGADKVALLTTDSYRIGGHEQLRIYGKLLGVSVRSIKDIADLQLMLHELRGKHMVLIDTVGM
SQRDQMLAEQIAMLSQCGTQVKHLLLLNATSSGDTLDEVISAYQGHGIHGCIITKVDEAASLGIALDAVI
RRKLVLHYVTNGQKVPEDLHEANSRYLLHRIFKPSRENSPFSLQDPEFALVMANTAGDQNDKRQRERIEA
>gnl|CDD|173185 PRK14722, flhF, flagellar biosynthesis regulator FlhF; Provisional
MRNAARRLPADEPAAAKPALRLPEDTAAAVADAVKARIERIVNDTVMQELGSLRELMEEQFAGLMWNERQ
RRNPVHGALTKYLFAAGFSAQLVRMIVDNLPEGEGYDTLDAAADWAQSVLAANLPVLDSEDALMERGGVF
ALMGPTGVGKTTTTAKLAARCVMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQLAL
AELRNKHMVLIDTIGMSQRDRTVSDQIAMLHGADTPVQRLLLLNATSHGDTLNEVVQAYRSAAGQPKAAL
PDLAGCILTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPENLYVATKKFLLKSAFCAPREDSPFVPHD
DDLPAMLSALSTRTGNELHEVRFG
>gnl|CDD|237802 PRK14723, flhF, flagellar biosynthesis regulator FlhF; Provisional
MSVAKFVAASSREAMRQVREALGPDALVLSNRSVAEGVEIVAMLDEDLGAVAASAQAYAPPAPAPLPAAL
VAPAPAAASIAAPAAVPAPGAIGDLRGELQSMRGMLERQLAGLLWAAGEVAGRDPLRASLFRWLLGAGFS
GQLARALLERLPVGYDRPAAMAWIRNELATHLPVLRDEDALLAQGGVLALVGPTGVGKTTTTAKLAARCV
AREGADQLALLTTDSFRIGALEQLRIYGRILGVPVHAVKDAADLRFALAALGDKHLVLIDTVGMSQRDRN
VSEQIAMLCGVGRPVRRLLLLNAASHGDTLNEVVHAYRHGAGEDVDGCIITKLDEATHLGPALDTVIRHR
LPVHYVSTGQKVPEHLELAQADELVDRAFATPRRGALFAPSEADLAALWAADEAAPAERQRGGLADVLRS
LGDSADALGACALELLAADLGFDQARSLWRQRSAGAAALRAMAQAVRAAVRRDVAAACDRYVLALHGTLA
LKVAGLPGAQPLQHTLLLSDRDGAPLAATVAPTGRAAQPPGEPDADWPAEALRARLDAARAVVNLLPAVP
AAALLAAWQQAGERWLARCAGTARVIHDGCPTKLDAVADTLGFHPAGEVTVRGRDAVLWAAGAEVRLPAT
GEGGIDLRLVVARLADAASGELLAQRYGLTNLAAAQDAAQVARWLLWAEAADGAFRTLRHAWDALPQDAG
AAAMAARALAAGQLGAAVWRLEHAPAATARAFLAGLAGRTARRGRPVPGRVLPEGLGKLFALLEMLE
>gnl|CDD|237803 PRK14724, PRK14724, DNA topoisomerase III; Provisional
TKTLVIAEKPSVAQDIVRALTPVAGKFEKHDEHFESDSYVVTSAVGHLVEIQAPEEFDVKRGKWSFANLP
VIPPYFDLKPVDKTKTRLNAVVKLAKRKDVTELVNACDAGREGELIFRLIEQYAGGAKGGLGKPVKRLWL
QSMTPQAIRDGFDNLRSDAQMQGLASAARSRSEADWLVGINGTRAMTAFNSRDGGFFLTTVGRVQTPTLS
LVVEREEKIRKFVSRDYWEIHAGFHAEAGEYLGKWFDPQWKKASDDPEARADRVWSEREARAIADAVRGK
AATVTEESKPTTQASPLLFDLTSLQREANGKFGFSAKTTLALAQSLYERHKALTYPRTDSRALPEDYLPV
AKQTFEMLATSGMRHLAPFAQQALDGNYVRPSKRIFDNSKVSDHFAIIPTTQAPSGLSEAEQKLYDLVVR
RFMAVFFPSAEYQVTTRISQVVGHSFKTEGKVLVKPGWLAIYGKEAANEVEDAKDGDKGQPLVPVKPGEM
VRTEFAEAKGLKTKPPARYSEATLLGAMESAGKQIDDDELREAMQEKGLGTPATRAAIIEGLLTEKYMLR
EGRELIPTAKAFQLMTLLRGLGVEELSRAELTGEWEYKLAQMEKGQLSREAFMQQIAAMTEKLVKKAKEY
DRDTIPGDYATLSTPCPNCGGVVKENYRRYACTGANGAGEGCGFSFTKSPAGRTFETAEAEQLLRDRRIG
PLEGFRSKAGWPFTAEVVIKRDEEAKNYKLEFDFGDDKNAEDTGEIVDFAGQESLGPCPKCGAPVFEHGS
NYVCEKSVPTLAQPTPSCTFKSGQVILQQPIEREQMQKLLATGKTDLLDKFVSMRTRRAFKAFLAWDKEA
GKVNFEFEPRESKFPPRKTAAAKAGAASAAFGGTVAVKAAKPAKKAAAKKVAAKTAAAKTPRKAAKKKAA
PPAAGLKPSAALAAVIGAEPVARPEVIKKLWDYIKANNLQDPADKRAINADAKLRPVFGKDQVTMFELAG
IVGKHLS
>gnl|CDD|237804 PRK14725, PRK14725, pyruvate kinase; Provisional
MSSAATVTPSDQEELQRLLEALDELRARLAAAEAAHADWLAAVDPSHRASARNLLHYLALRQHDLRDLQE
ALADLGLSSLGRAEAHVLAALDAVLAVLRALLGEGPAYPPEDTAVTFEEGDELLDEHAEALLGPPPSGRP
TRIMVTLPTEAADDPDLVRRLLAAGMDIARINCAHDDPEAWRAMIANVRTAEEELGRRCRIAMDLAGPKL
RTGPIAPGPRVIKLRPTRDALGRVLTPARLWLTASESPPPSPPPGPVGLPVDPEWLARLEPGDELRFTDA
RGKKRKLTVTEVDDEGVLAEGSQTAYLANGTLLRLGRHDSTRVGGLPPVEQKLRLKVGDRLVLTRDDAPG
DPAQGDAPPARISCTLPEAFRAARVGERVWFDDGKIGAVVVKVEADEVELRITHARPGGSKLKAGKGINL
PDSHLPLPALTDKDLEDLAFVAKHADIVALSFVRSPEDVRLLLDALEKLGADDLGVVLKIETRRAFENLP
RILLEAMRHPRFGVMIARGDLAVEVGFERLAEVQEEILWLCEAAHVPVIWATQVLESLAKKGLPSRAEIT
DAAMALRAECVMLNKGPHIVEAVRVLDDILRRMEEHQRKKRSLLRRLR
>gnl|CDD|237805 PRK14726, PRK14726, protein translocase subunit SecDF
MLHFSRWKTILIWLVVLAGVAIAAPNLLSEAQLASLPSWLPHRQVTLGLDLQGGSHIVLKVERSDIVKDR
LEETVANIRNALRDAGIRYTGLTGNGQTVQVRITDPAQTQAAVDALKPLTAPVSAGGLGGSSIQELTLQE
GGEGQLRLQLTDAGIDYRVSSALTQSIEVVRRRVAELGTTEPLIRRQGDDRIVVQVPGLVDPQRLKNLLN
QPAKLSFRLVDSSMPAQEALNGRPPATSEVLYSLDDPPVPYLVERRAFVSGENLVDAQPVFDPQTNEPVV
TFRLDAEGTQRFAQATQQNVGKHFAIVLDGQVISAPVIDEAITGGEGRISGNFSEQGANDLAVLLRAGAL
PATLTVVEERTVGPGLGADSIAAGLVAGLIAAILVAALMIGFYGFLGVIAVIALIVNVVLIIAVLSLLGA
TLTLPGIAGIVLTIGMAVDSNVLIYERIREEEKTGHSLIQALDRGFSRALATIVDANVTILIAAVILFFL
GSGAVRGFAVTLAVGILTTVFTAFTLTRSLVAVWLRRRRPKHLPKGVRTGLFEGANIRFMGIRRYVFTLS
AALSLASLVLFATVGLNLGIDFTGGSLIEVRAKQGNADIADIRARLNELNLGEVQVERFGSPRDALIRIA
SQDGGENAEQSAVTLVRGELEDDYDFRRVEVVGPAVSGELTMAATLGVLAALAAILIYIWIRFEWQFAVG
AIIATLHDVILTLGLFVLTGIEFNLTSIAAILTIVGYSLNDTVVVYDRVRENLRRYKKMPLPILIDASIN
QTLSRTVLTSATTLLALLALYLFGGEVIRSFTFAMLFGVAVGTFSSIYIAAPVLIVFKLRPESLDGEESN
KTDAGVKSGTVVGAV
>gnl|CDD|237808 PRK14734, coaE, dephospho-CoA kinase; Provisional
MLRIGLTGGIGSGKSTVADLLSSEGFLIVDADQVARDIVEPGQPALAELAEAFGDDILNPDGTLDRAGLA
AKAFASPEQTALLNAITHPRIAEETARRFNEARAQGAKVAVYDMPLLVEKGLDRKMDLVVVVDVDVEERV
RRLVEKRGLDEDDARRRIAAQIPDDVRLKAADIVVDNNGTREQLLAQVDGLIAEILSRVN
>gnl|CDD|173197 PRK14735, atpC, F0F1 ATP synthase subunit epsilon; Provisional
MPIHLEIVTAERVVLSDDVDMISAPTKDGRVGILPRHAPLLTILEPGELDIVKNGVRTPFAISGGFMEVL
PHRVTILADTAERADEIDEARAEQARAEAEQRRRERQSEQDLALAEAKLRRAMVRLRVAQLHKIRRRQS
>gnl|CDD|173198 PRK14736, atpC, F0F1 ATP synthase subunit epsilon; Provisional
MATFHFDLVGPERTLYSGEVEAVQLPGSEGEMTVLPGHAPVLTTLKVGVITVTETTGNGKRIYVRGGFAE
IGPTSVTVLAERAAPVEELTPEMIDREIEAVEMERDATQDLDKREALNAQIVQMQEAKATLSL
>gnl|CDD|173199 PRK14737, gmk, guanylate kinase; Provisional
KASPKLFIISSVAGGGKSTIIQALLEEHPDFLFSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFL
EWAEVHDNYYGTPKAFIEDAFKEGRSAIMDIDVQGAKIIKEKFPERIVTIFIEPPSEEEWEERLIHRGTD
SEESIEKRIENGIIELDEANEFDYKIINDDLEDAIADLEAIICGKK
>gnl|CDD|237809 PRK14738, gmk, guanylate kinase; Provisional
MMNPWLFNKPAKPLLVVISGPSGVGKDAVLARMRERKLPFHFVVTATTRPKRPGEIDGVDYHFVTPEEFR
EMISQNELLEWAEVYGNYYGVPKAPVRQALASGRDVIVKVDVQGAASIKRLVPEAVFIFLAPPSMDELTR
RLELRRTESPEELERRLATAPLELEQLPEFDYVVVNPEDRLDEAVAQIMAIISAEKSRVHPRRIEL
>gnl|CDD|173201 PRK14740, kdbF, K(+)-transporting ATPase subunit F
MTVLDWLSLALATGLFVYLLVALLRADRA
>gnl|CDD|173202 PRK14741, spoVM, stage V sporulation protein SpoVM
MKFYTIKLPKFLGGIVRAMLGSFKKG
>gnl|CDD|173203 PRK14742, thrL, thr operon leader peptide; Provisional
MRQTDNMRYISLNTTIITTTETTGYGAG
>gnl|CDD|173204 PRK14743, thrL, thr operon leader peptide; Provisional
MNRIGMITTIITTTITTGNGAG
>gnl|CDD|173205 PRK14744, PRK14744, leu operon leader peptide; Provisional
MSHIVRFTGLLLLNAFIVRGRPVGGIQH
>gnl|CDD|173206 PRK14745, PRK14745, RepA leader peptide Tap; Provisional
MLRKFQYLFLWHLLLPCIVSAGRSD
>gnl|CDD|173207 PRK14746, PRK14746, RepA leader peptide Tap; Provisional
MFRKVQYLLRLLLLPCNISAGRCD
>gnl|CDD|184810 PRK14747, PRK14747, cytochrome b6-f complex subunit PetN; Provisional
MDILTLGWVSVLVLFTWSIAMVVWGRNGF
>gnl|CDD|173209 PRK14748, kdpF, K(+)-transporting ATPase subunit F
MSAGVITGVLLVFLLLGYLVYALINAEAF
>gnl|CDD|173210 PRK14749, PRK14749, cytochrome bd-II oxidase subunit CbdX
MWYLLWFVGILLMCSLSTLVLVWLDPRLKS
>gnl|CDD|173211 PRK14750, kdpF, K(+)-transporting ATPase subunit F
MNFSIVCGALLVLLLLGYLVYALFNAEDF
>gnl|CDD|173212 PRK14751, PRK14751, tetracycline resistance determinant leader peptide; Provisional
MLCMPMVMHKNPSDKSIYHWDFYALLGF
>gnl|CDD|173213 PRK14752, PRK14752, delta-lysin family phenol-soluble modulin
MSCLILRIFILIKEGVISMAQDIISTIGDLVKWIIDTVNKFTKK
>gnl|CDD|184811 PRK14753, PRK14753, 30S ribosomal protein Thx; Provisional
MGKGDRRTRRGKIWRGTYGKYRPRKKK
>gnl|CDD|173215 PRK14754, PRK14754, toxic peptide TisB; Provisional
MSLVDIAILILKLIVAALQLLDAVLKYLK
>gnl|CDD|173216 PRK14755, PRK14755, transcriptional regulatory protein PufK; Provisional
MVPYRNPRHQHVASVLRSGG
>gnl|CDD|341227 PRK14756, small_mem_YnhF, YnhF family membrane protein; Validated
MDTDLKFALLTTVGALAVILGFGLTAILH
>gnl|CDD|173218 PRK14757, PRK14757, putative protamine-like protein; Provisional
MRSFDQGSTRAPARERCRRQRPEGRSAQR
>gnl|CDD|173219 PRK14758, PRK14758, hypothetical protein; Provisional
MVGRYRFEFILIILILCALIAARFYLS
>gnl|CDD|173220 PRK14759, PRK14759, K(+)-transporting ATPase subunit F
MILDYSLAGAVSLGLLIYLTYALLRPERF
>gnl|CDD|173221 PRK14760, PRK14760, protein YoaJ
MKKSTIIMLVVAIVAVAGTQFGWW
>gnl|CDD|173222 PRK14761, PRK14761, fur leader peptide
MIRIISRANSVTSSNEVNRLVTGQIPHD
>gnl|CDD|173223 PRK14762, PRK14762, protein YohP
MKIILWAVLIIFLIGLLVVTGVFKMIF
>gnl|CDD|184813 PRK14763, PRK14763, pyrroloquinoline quinone precursor peptide PqqA
MWTTPAATEMRFGFEVTMYVMNK
>gnl|CDD|173227 PRK14766, PRK14766, lipoprotein signal peptidase; Provisional
WIKDKLVELKVFLKNHNYLWKFKLIVCLPIFISLISFDWIIKAVVVSHMKLGETKTFISGFLNFQYVINL
GMAYGRLADKLYLVIIFATIFSLFLTIVFIFLNNKKWLIVLSILLAGSWGNLLARLWAPGNEQNIYGGVV
DFLTWDFSLLNSRDYVFNLADLYVNIAIGLTILFTIIELVLYIKSKIKTKKEKIENEQNNS
>gnl|CDD|237811 PRK14767, PRK14767, lipoprotein signal peptidase; Provisional
MENNKKKKSLIKYGILFVILVILDQITKYLAVSHLADKPSFVIIPGVFELIYLENSGAAFGMLSGKAVFF
LVITVAVVIIMAFVFFKLPATKKYNPLHIILVFIVAGAAGNLIDRILNGYVVDFIYFKLINFPIFNVADI
YVTVSTFLFIILFLFYYKEDDFSFLSFKKKDENR
>gnl|CDD|173229 PRK14768, PRK14768, lipoprotein signal peptidase; Provisional
MLYILIIILLIGLDQLSKIWVLNNLVDVSTIPIINNVFHLTYVENRGAAFGLLQNNQWIFIIVALLATVF
GLYYLNTRKVHIFGRLGIILIISGALGNLIDRVRLGFVVDYFDFRVIWEYVFNVADVFVVVGTVFLCIYV
LFFESKSR
>gnl|CDD|173230 PRK14769, PRK14769, lipoprotein signal peptidase; Provisional
MRRARITVLLAAVIIAGIDLGAKAWSERQLAGSSVDLGLLHLRLAFNSGVAFSMGDTLPVGVIVAVTAVI
VVALAVYAWRRAPTAGWVERIAGGAVIGGALANVVDRARDGLVTDYLHTGWWPTFNLADTFLVTGFAVIA
LLHARPERTADTAAAT
>gnl|CDD|173231 PRK14770, PRK14770, lipoprotein signal peptidase; Provisional
GISRPNRLRRTLGAALLVAVLLLDQASKYWILYGLDLPDRGSVPVLPFLNFTMVWNHAVTFGMLGGLGGI
GRVVFSAVSLAAVLLLGVWLTRTPRPLVAAALGAIMGGAIGNVIDRMRYGAVVDFLHAHAFGWSWYVFNL
ADAAIDCGVAVLLIDSLLARRQAAPGA
>gnl|CDD|184816 PRK14771, PRK14771, lipoprotein signal peptidase; Provisional
MTNQQGRLRTRVAVFACIAIAALIVDQLTKAWAQAALSDGQTIRVIPGLLSLTLVRNPGASLGMGSGATW
VISLLAIVACVALVVAAVRTISMKWTVALALAFAGALGNLIDRVMYAQGFLNGKVVDFLNYGWSVGNVAD
IFLMIAGIALVILILMGEPFSHKDL
>gnl|CDD|237812 PRK14772, PRK14772, lipoprotein signal peptidase; Provisional
MTDEFAATATQPTPPTRRPRRWRLLILFAGFAVFAYVFDQLTKLWVTSTMVEGERIPVLPPLLHWYYIRN
SGAAFSIGENVTWVFSIIMAAVAVAILVQLRKLGSAWWALALGLLLGGALGNLTDRLFREPSFGMGHVVD
FIQLPNFAIFNIADSAVVSGVVIICLLTLRGVSLDGTRHRGSKDGEDADA
>gnl|CDD|173234 PRK14773, PRK14773, lipoprotein signal peptidase; Provisional
PVSKWALLALLFVALLAADQWTKYLAVERLTTVFERGGDETLAERVAGFYTEQHLEPLSTEPYYVWRPVW
RMNYVENPGAAWGLFRGHSEEFRNAFFTLVSLAAVAFILHYYRKLRQEQRYLQVALALVLGGAVGNFVDR
LARGYVIDFIEWYWWNRPDIRWPTFNVADSLIVVGVAMLVLHPGSRKEAPRA
>gnl|CDD|173235 PRK14774, PRK14774, lipoprotein signal peptidase; Provisional
MRLAALTAFGVFVLDQLTKWLVVWGLDLANRGAIDLVAPWLTFRMAWNRGINFGIGSSDQEIVRWGLVIV
SLAISAWVWRWVWRSTPTRLARISGGLLIGGALGNVVDRVLYGAVADFLNMSCCGIENPYAFNVADIAIF
AGAFGLVLFTRETKPEPEKPKGTPKRKPAERKANGSGRPGGGKTP
>gnl|CDD|237813 PRK14775, PRK14775, lipoprotein signal peptidase; Provisional
MKSKIVGVIAIVLVFALDQVSKAYAIDWYSQSGATEVFKFCSLVEVWNRGISFGMFGALESSNLIFTYVS
LGVILMLFVLFVQSKCNKSTICMGVVIGGALGNLADRLRFGAVYDFISLHAGEFHWPAFNFADVCVTCGV
ICFLCLEVMYHAKACVDTSGDPDALSVKKY
>gnl|CDD|173237 PRK14776, PRK14776, lipoprotein signal peptidase; Provisional
MLIIGKKLSPYALLSISGLLAASDQAVKWLVQQSMAYGEYVSVTPFFNWVHLWNTGAAFSLFANGGGWQR
YFFIGIAVVVSIFLIKLILENRHKGEAIAYSLILGGAMGNLIDRVFRGYVVDSFDFYWRDWHWPAFNLAD
IAIVLGALLFVSSSLLGKKANTNAEPDGSD
>gnl|CDD|237814 PRK14777, PRK14777, lipoprotein signal peptidase; Provisional
MWVFSRQLNILRIVPILPERQRGVPAWAPLVLATLLIVLDQALKAWALANLQLGAPAIPVLPGVLDWVLT
FNTGAAWSLFSGSALPLALMRLLVGLGLLVYLLRRPQPRFLTVVLSLIAAGAIGNAIDGLRFGRVTDMLH
SPALSAVTRALGQGDFPIFNLADMCVVGGTLLLLFASFQQDRKR
>gnl|CDD|173239 PRK14778, PRK14778, lipoprotein signal peptidase; Provisional
MMFVIVLTIVLDQLTKRIASEIHGTFFIVPGFLRFVKATNRGVALGLFSNLSEQVLWTVLFVVVFLSLLP
YIFRFSRLERMAMGFILGGALGNLLDRIRFGYVLDFLNLTFLPTIFNLADVFIIVGGALMILGVFRGGDN
ESLESRKKRRGLETGSVFEGEDTVLDIEIVDSKSDKRGQSEGQRSD
>gnl|CDD|184818 PRK14779, PRK14779, lipoprotein signal peptidase; Provisional
MGKKSLAYLGTFFLVLVLDLITKYLAEKYLFDKDISVIPFLDLVLVYNKGVAFGLLSEAPDFIRLPILLL
TPIIALIITFLYALKSNDKLSNLSMGLIGGGALGNLYDRFFLGQVRDFIDIYIGDFHWPAFNIADASISI
GIALFILYEHFFKKRKKTN
>gnl|CDD|173241 PRK14780, PRK14780, lipoprotein signal peptidase; Provisional
MIKKIKNSNFYIIIKKFNNSLRKINFFSKIILKISNKQLRDYFLSITHLDVIFYKIINFIICALIVLLSG
FLVREWAINLVQSTKELIHGPIFHFTLNNGIALGRINNNSGIVYFLQSIPIILGFLSFIFLKNSLLYIPL
LFLLFGGLGNIIDRSIPEVELYKALPGIFHNSLINPNSVGGGDDVINGVVDYWKFVNSIINLFDVYIVVG
VCVLVVILIISFIIKWKKDKDSEDNKKKIADENDLEINEPSNKPFGYDDLQKS
>gnl|CDD|237815 PRK14781, PRK14781, lipoprotein signal peptidase; Provisional
RRRGGLLLWAALLAGADLLVKAQAEAGLSRGEVIDLGLINIRLLYNTGVAFSLGAGLPTWFVIAGTGLII
AALLWYLTSSAPKMSRLSRAGAALLLGGAVGNFIDRLDGRGVVDYLHSGWFPTFNLADVFVTTGVALLVL
GMLRPPKDPENGT
>gnl|CDD|173244 PRK14783, PRK14783, lipoprotein signal peptidase; Provisional
MKYFEKRFLDVYRPGYLGVIFLGIFLDLVTKFLVILYFYPHRYLEVLGSFFRMTLTFNTGFVFGAFQDNA
IPSLIATGFAIVFLIGYRWKNSDLGNPWGWNLVMAGAFGNFLDKFFVKIPGTGFRFGFQPNKGEYIGVVD
FLDFDWPDFLLFSRWPAFNVADSCVTIGLTILIFTMKLEEEK
>gnl|CDD|184819 PRK14784, PRK14784, lipoprotein signal peptidase; Provisional
MTRGLVFFVSTACGILADQLSKFIITANLTTGTSIPESGFFQIVHVHNTGAAFSIFRGHIEWLIAASVLG
VILAMTAFFIRKKLPFLDTRPGLIALGVILAGTVGNLIDRVRLGYVTDFIRVGDFPTFNIADSCLTVGVI
GLLLLYLVSSHVSGDTSENV
>gnl|CDD|184820 PRK14785, PRK14785, lipoprotein signal peptidase; Provisional
LNKTPKMVANGRRALNWYLLSLVVLILDQWTKWLAETKLTFLEPVPVIEPFLNWTLAYNYGAAFSFLADA
GGWQKWFFAGLALIMSLFLIVYLKKAPRQAKLLSLGLALVLGGAIGNLIDRLLHGHVIDFIHVHYADVWH
YPIFNIADIGICVGVALIVIDMLFLEKKRNA
>gnl|CDD|173247 PRK14786, PRK14786, lipoprotein signal peptidase; Provisional
MFYIFIITILTGIDQWTKYLIETQLKPIGAIPIVKDIFHLTYARNTGAAFSILRDKQAFLILVTTIVVGA
LIYYLIKILKTGEVAFKLSLAIIIGGALGNLIDRVRLNYVTDFLDFTLINYPIFNLADVFVVSGVVMLSY
MLLFKGDMPKISKM
>gnl|CDD|173248 PRK14787, PRK14787, lipoprotein signal peptidase; Provisional
MKLFFLLALAVIVLDQFTKKLAITFLRDGPQSITIIPDWFKLTYAENRGIAFGLEFAPPEVLLLLTGAIS
AGVLWYVLRSKNRTPLFLLAFGLILGGGIGNLIDRITSGRVVDFIYFDLYQGYIFGIWVSLWPIFNIADS
AITIGACMLLLFHNRIFPD
>gnl|CDD|237816 PRK14788, PRK14788, lipoprotein signal peptidase; Provisional
LKKAFLIILLVLLIDQISKIYVKTHFVLGQSVLVFDWFKIHFVENPGMAFGMELGGEYGKLFLTLFRIVA
VGGIGYYLWKLVKKNSSKGLIICISLILAGAIGNIIDSVFYGVIFDNGSYGQIATFFPEGGGYSTWFHGK
VVDMFYFPIIDGYLPEWVPFWGGEHFVFFKPVFNIADSAISIGVILLLLFNKKAFPEPLD
>gnl|CDD|173250 PRK14789, PRK14789, lipoprotein signal peptidase; Provisional
LRSRWMLLVLVAIPVFVIDQLSKVWLSDVLLRYNRPIPLLFDWVQLAYHENTGVAFGLFPDQGGVLSVGA
GLVLLLLALTYQYILPADSRWITVAVGMIFGGGLSNLVDRIRQGYVVDFIQFGWWPVFNLADSAITIGVA
ALAFHIIFIGEEPAPTEPEPIDDELLSELLSRDPSPPAATDARTSSSESLS
>gnl|CDD|173251 PRK14790, PRK14790, lipoprotein signal peptidase; Provisional
MKSLLQARWITPALVAATILALDQASKRWILATLGPVPMTKFIPLIGEDIRLAYSHNTGIAFSLFDGKSD
ILTVVALVISLGAIYLYRTQLPNRRLLIQVAMGLILGGALGNVIDRIRLGYVVDFIQVGWFPIFNLADSA
ITVGAALLMLQYALDEIALRRLRQAMMSQ
>gnl|CDD|237817 PRK14791, PRK14791, lipoprotein signal peptidase; Provisional
MEIIIIILGIFLDQLTKIWALKNLASGGDIPVIKNFFSLTYVENRGAAFGILQNKTLFLILITIIVILGL
IYYIIKYKPTSKLYKISLSLIISGAIGNLIDRIRYGYVVDFIDFHFKDYYFPVFNVADILVVVGTILLAI
YILKEE
>gnl|CDD|173265 PRK14804, PRK14804, ornithine carbamoyltransferase; Provisional
MSESNVKHLISWEDWSDSEILDLLDFAVHVKKNRVNYAGHMSGRSLAMLFQKTSTRTRVSFEVAMTEMGG
HGIYLDWMASNFQLSDIDLEARYLSRNVSVIMARLKKHEDLLVMKNGSQVPVINGCDNMFHPCQSLADIM
TIALDSPEIPLNQKQLTYIGVHNNVVNSLIGITAALGIHLTLVTPIAAKENIHAQTVERAKKKGTLSWEM
NLHKAVSHADYVYTDTWLDMEFFNDPSYADKKKQRMELMMPYQINSSLMEKTNAKVMHDMPIHAGYEITR
EVVLSDRSIIFQQAENRLDAQKAVILKLLEN
>gnl|CDD|237819 PRK14805, PRK14805, ornithine carbamoyltransferase; Provisional
MKHLLSIKELTQQQLLDLLALAKTIKANPAEYRQALAGKSVVMLFEKPSLRTRVSFDIGINKLGGHCLYL
DQQNGALGKRESVADFAANLSCWADAIVARVFSHSTIEQLAEHGSVPVINALCDLYHPCQALADFLTLAE
QFGDVSKVKLAYVGDGNNVTHSLMYGAAILGATMTVICPPGHFPDGQIVAEAQELAAKSGGKLVLTSDIE
AIEGHDAIYTDTWISMGDDTPLAEIKAKFAPYQVNKALMEKAGATFVMHCQPAHRGVEITSEVMDGEGSL
ILQQAENRMHAQNAVLVTLLSQ
>gnl|CDD|237820 PRK14806, PRK14806, bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
PLFGRVVVIGLGLIGGSFAKALRERGLAREVVAVDRRAKSLELAVSLGVIDRGEEDLAEAVSGADVIVLA
VPVLAMEKVLADLKPLLSEHAIVTDVGSTKGNVVDAARAVFGELPAGFVPGHPIAGSEKSGVHAANADLF
RNHKVILTPLAETDPAALARVDRLWRAVGADVLHMDVAHHDEVLAATSHLPHLLAFSLVDQLANREDNLD
IFRYAAGGFRDFTRIAASDPVMWHDIFLANKEAVLRALDHFRDDLDALRAAIEAGDGHALLGVFTRARAA
REHFSKMLARRAYVEAMNANDVSYSVLPGGAVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDA
LATLQAFRDMGVVIEGPHNGRVTIHGVGLHGLKAPPGPLYMGNSGTSMRLLSGLLAAQSFDSVLTGDASL
SKRPMERVAKPLREMGAVIETGEEGRPPLSIRGGQRLKGIHYDLPMASAQVKSCLLLAGLYAEGETSVTE
PAPTRDHTERMLRGFGYPVKVEGNTISVEGGGKLTATDIEVPADISSAAFFLVAASIAEGSELTLEHVGI
NPTRTGVIDILKLMGADITLENEREVGGEPVADIRVRGARLKGIDIPEDQVPLAIDEFPVLFVAAACAEG
RTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEGGIFGGGEVESHGDHRIAMSFSVASLRA
SGPITIHDCANVATSFPNFLELANQVGIRIEVEQS
>gnl|CDD|173271 PRK14810, PRK14810, formamidopyrimidine-DNA glycosylase; Provisional
MPELPEVETVARGLAPRAAGRRIATAEFRNLRIPRKGDPDLMAARLAGRKILSVKRVGKHIVADLEGPGE
PRGQWIIHLGMTGKLLLGGPDTPSPKHTHAVLTLSSGKELRFVDSRQFGCIEYSEAFPKRFARPGPEPLE
ISFEDFAALFRGRKTRIKSALLNQTLLRGVGNIYADEALFRAGIRPQRLASSLSRERLRKLHDAIGEVLR
EAIELGGSSVSDYVDAEGRSGFFQLSHRVYQRTGEPCLNCKTPIRRVVVAGRSSHYCPHCQK
>gnl|CDD|184831 PRK14811, PRK14811, formamidopyrimidine-DNA glycosylase; Provisional
MPELPEVETTRRKLEPLLLGQTIQQVVHDDPARYRNTELAEGRRVLGLSRRGKYLLLHLPHDLELIVHLG
MTGGFRLEPGPHTRVTLELPGRTLYFTDPRRFGKWWVVRAGDYREIPLLARMGPEPLSDDFTEPEFVRAL
ATARPVKPWLLSQKPVAGVGNIYADESLWRARIHPARPATSLKAPEARRLYRAIREVMAEAVEAGGSTLS
DGSYRQPDGEPGGFQFQHAVYGREGQPCPRCGTPIEKIVVGGRGTHFCPQCQPLRPLRS
>gnl|CDD|173273 PRK14812, PRK14812, hypothetical protein; Provisional
MAGSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLKPTDQVTVDLEQQKI
ISPVEEFTFEIDSEWKHKLLNSLDDIGITLQYEELIAAYEKQRPAYWQD
>gnl|CDD|173274 PRK14813, PRK14813, NADH dehydrogenase subunit B; Provisional
MGLLDAGISNHNVLVTSVDNVLNWARLSSLWPMGFGLACCAIEMMATNASNYDLERFGIFPRSSPRQSDL
MIVAGTVTMKMAERVVRLYEQMPEPRYVLSMGSCSNCGGPYWEHGYHVLKGVDRIIPVDVYVPGCPPRPE
ALIGGLMKVQELIRMEQIGISRADALKKLAEKSVDPQQVIEQERKSATA
>gnl|CDD|173275 PRK14814, PRK14814, NADH dehydrogenase subunit B; Provisional
MGLSDLSKKPGQALGDMFQLGNLESVIQWGRSFSLWPYPFATACCGIEYMSTACSDYDIARFGAERPSFS
PRQADMILVLGTITYKMAPVLRQIYDQMAEPKFVISVGACASSGGMFHTYGVLQGVDRILPVDVYVPGCP
PRPEAILDALVKLQTKLKTQGLEARRQEVMQKIQELNERNKPLVVR
>gnl|CDD|237821 PRK14815, PRK14815, NADH dehydrogenase subunit B; Provisional
MVTTNTTLTYESGVEGNVVVTTLDAAINWIRKNSLWPMPMGLACCAIELMAVACSRFDISRFGAEVMRFS
PRQADVMIVAGTVTYKMALAVRRIYDQMPEPKWVIAMGACASSGGMYRSYSVLQGVDRILPVDVYISGCP
PRPEAILDALIKLQKKIDTERAARTLFKKEAPREANAPVPVNT
>gnl|CDD|173277 PRK14816, PRK14816, NADH-quinone oxidoreductase subunit B
IPYEDFIDNESLEKMVKELNEGGANVFVGVLDDLINWGRSNSLWPLTFATSCCGIEFMALGAARYDMARF
GFEVARASPRQADMIMVCGTITNKMAPVLKRLYDQMADPKYVIAVGGCAVSGGPFKKSYHVLNGVDKILP
VDVYIPGCPPRPEAFYYGMMQLQRKVKIEKFFGGVNRKEKKP
>gnl|CDD|173278 PRK14817, PRK14817, NADH-quinone oxidoreductase subunit B
ASELDGLPVIATRREEAEGFLQGLVSKSLGWARKYSLFTYPFVTACCGMEYMTMASARYDSDRFGAAMPR
FSPRQADLLMVVGTVNCKQAPILQRVYEQMADPKWVMAFGVCASSGGFYDNYATVQGIDRIIPVDVYVPG
CPPRPEQVLDGIMLLQKKIQNQSHKLIDRKPLPVIAGGAGR
>gnl|CDD|173279 PRK14818, PRK14818, NADH dehydrogenase subunit B; Provisional
MAARMDPGIGGDVTLLHTSQLDNLINLARASSLYYLTFGLACCGIELMQTGGPRADVMRFGAIPRASPRQ
ADFMIVAGTLTYKMAERARLLYDQMPEPKYVISMGSCSNCGGLFQLGYSVCKGVDKVIPVDVYVPGCPPR
PEALTEGLLRLQEIVRSEPWSTKRRPAAQAEGA
>gnl|CDD|237822 PRK14819, PRK14819, NADH-quinone oxidoreductase subunit B
MSDLDPTQLELEKQGVLLTTVNRFYNWGRRSSVWPMAFGLACCAIEMMATGLSRYDLARFGAELFRASPR
QADLMIVAGTVTKKMAPQVVRLYNQMPEPRYVISMGACATSGGPFRDGYNVLRGIDLLIPVDVYIPGCPP
RPEALLHALMTLQKQIDAQSLGRVRWYGSGDKGQTKEFPVPTFGAHGLEIDGKLVDPVGGLPLLSPYTSP
SHGEHRSGQIEHPEVVRPFPIMDPEVELESALKARGIAPEIAADDLKRGAVEVA
>gnl|CDD|184833 PRK14820, PRK14820, NADH-quinone oxidoreductase subunit B
MSDIKIVEAPEGYEGEGFFATSLDSVIGLARKNSLWPLPFATSCCGIEFMATMASHYDLARFGSERPSFS
PRQADMLMVMGTIAKKMAPVLKQVYLQMAEPRWVVAVGACASSGGIFDTYSVLQGIDRIIPVDVYVPGCP
PRPEQIIDGVMRVQELVKNESLRRRNSPEYQELLASYNIQ
>gnl|CDD|184834 PRK14821, PRK14821, XTP/dITP diphosphatase
MKIYFATGNKGKVEEAKIILKPLGIEVEQIKIEYPEIQADTLEEVAAFGAKWVYNKLNRPVIVEDSGLFI
EALNGFPGPYSAFVYKTLGNEGILKLLEGEENRRAYFKSVIGYCDPGGEKLFTGIVEGKIANEIRGKGGF
GYDPIFIPEGEEKTFAEMTTEEKNKISHRKRAFDEFKEWLKENL
>gnl|CDD|184835 PRK14822, PRK14822, XTP/dITP diphosphatase
MKEIVIATKNKGKVREFKEIFEKFDIEVKSLADFPPIPEVEETGTTFEENAILKAEAAAKALNKPVIADD
SGLEVDALNGAPGVYSARYAGEAKDDAANNEKLLKELGGVPFEKRTARFHCVIAVAFPGGETKTVEGTCE
GEILEEPRGENGFGYDPLFYVPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEWLKVE
>gnl|CDD|237823 PRK14823, PRK14823, putative deoxyribonucleoside-triphosphatase; Provisional
MKLVFATNNKHKLEEIRSILPEKIELLSLSDIGCHEDIPETADTLEGNALLKAEYVYKKYGYDCFADDTG
LEVEALNGAPGVYSARYAGGEHNAEANMRKLLEELEGKDNRKAQFRTVIALILDGKEHLFEGIIKGEIIK
EKRGDSGFGYDPIFVPEGYDKTFAELGLEIKNQISHRAKAVQKLIDFLSKA
>gnl|CDD|237824 PRK14824, PRK14824, putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
MKILLATTNEGKVREIKRLLSDLGIEVLSPDKKIEVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLE
VPALEGYPGVYSSRFYQIEFGGKEEVVESKDEANIRKLLRLLEGKQNRKARFVAFVVLYFGDWGIWTEGE
CRGKIAEEPRGSGGFGYDPVFIPEGYNKTMAELSPEEKNKISHRGKAVRKLVEILKYGGML
>gnl|CDD|173286 PRK14825, PRK14825, putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
MKTLFFATTNINKINEVKQILDIPNIKIEIPQNFDIKETGKTFKENSLLKAKALFEILNNKQPVFSEDSG
LCIEALNLEPGIYSKRYDQYKLGKKLSTNEKNHLIIDLMKNEKNRTAYFICNISYISKDGTILNFEGIIK
GTIALSIDDYKKNGFGYDPIFLTKNNKRLSELTLEEKNKISHRGIAFDKFKKFLMQSLF
>gnl|CDD|173287 PRK14826, PRK14826, putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
MPQIATETITIVLATGNRDKVRELRPLLEHISPLFSVRSLADLGVEVDIEETEETLEGNALLKADAIFEL
LSDRFPFLIALADDTGLEVDALGGAPGVYSARFAPVPEGEKPTYEDNVRHLLSEMEGKTERSARFRTVIA
LKGRLPGKNGAFEFEETAEGVVEGSITTEKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAVQ
KAVKFLRTILSQ
>gnl|CDD|173288 PRK14827, PRK14827, undecaprenyl pyrophosphate synthase; Provisional
MARDARKRKSSNFPQLPPAPDDYPTFPDKSTWPVVFPELPPAPYGGPCRPPQHTSKAAAPRIPADRLPNH
VAIVMDGNGRWATQRGLARTEGHKMGEAVVIDIACGAIELGIKWLSLYAFSTENWKRSPEEVRFLMGFNR
DVVRRRRDNLNKMGVRIRWVGSRPRLWRSVINELAIAEEMTKSNDVITINYCVNYGGRTEITEATREIAR
EAAAGRLNPERITESTIARHLQRPDIPDVDLFLRTSGEQRSSNFMLWQAAYAEYIFQDKLWPDYDRRDLW
AACEEYASRNRRFGSA
>gnl|CDD|237825 PRK14828, PRK14828, undecaprenyl pyrophosphate synthase; Provisional
MRLNLRRLLYKVYARRLLGELDGAQVPGHVGIIVDGNRRWARKAGFTDVSQGHRAGAAKIGEFLGWCDET
DVNVVTLYLLSTDNLGRPSEELNPLLDIIEDVVRQLAPDGRWRVRHVGSLDLLPAPSANRLKEAEEATVG
NDGIKVNVAVGYGGRQEIVDAVRSLLTEHKDKGTSIDELAESVTVDAISTHLYTGGQPDPDLVIRTSGEQ
RLSGFMLWQSAHSEYYFCETYWPAFRKVDFLRALRDYSQRERRFGK
>gnl|CDD|237826 PRK14829, PRK14829, undecaprenyl pyrophosphate synthase; Provisional
SDPLIPPDIPKNKLPRHIAVVMDGNGRWATQRGLKRTEGHKAGEPVLFDVVAGAIEAGVPYLSLYTFSTE
NWKRSPDEVRFLMGFSRDVIHRRREQMDEWGVRVRWSGRRPRLWKSVIDELEAAEELTKNNTTMDLVFCV
NYGGRAEIADAAAAIAREVRDGKISGDRVTEKMISDHLYNPDMPDVDLFLRTSGEQRTSNFLLWQSAYAE
LDFVPKLFPDFGRDDLWAAIDEYAHRDRRFGGV
>gnl|CDD|184840 PRK14830, PRK14830, undecaprenyl pyrophosphate synthase; Provisional
MFKFFKKKKKTSFDEELDKGNIPKHIAIIMDGNGRWAKKRMLPRIAGHKAGMDTVKKITKAASELGVKVL
TLYAFSTENWKRPKDEVKFLMNLPVEFLDKFVPELIENNVKVNVIGDTDRLPEHTLRALEKAIEKTKNNT
GLILNFALNYGGRAEIVSAVKEIAKDVLDGKLNPEDITEELISNYLMTKGLPDPDLLIRTSGELRLSNFL
LWQLAYSEFYFTDVLWPDFDEEELLKAIKDYQSRQRRFGGV
>gnl|CDD|184841 PRK14831, PRK14831, undecaprenyl pyrophosphate synthase; Provisional
TTVQPTKLQDLPADLDPQRLPKHVAVIMDGNGRWAKRRGLPRIMGHRRGVDALKDLLRCCKDWGIGALTA
YAFSTENWSRPLEEVNFLMTLFERVLRRELEELMEENVRIRFVGDLDPLPKSLQEEISRSTELTKNNNGI
HFNVCTNYGGRQEIVQAARAIAQQVQQGELDPSEIDENLFESELYTAGIKDPDLLIRTSGEMRISNFLLW
QLAYAEIYVTDVLWPDFDRDEFHKALLDYQSRERRFGGV
>gnl|CDD|237827 PRK14832, PRK14832, undecaprenyl pyrophosphate synthase; Provisional
MNNFDYVMRPPDLDPQKIPQHIAVIMDGNGRWATSQGLPRIAGHRQGARTLKELLRCCKDWGIKALTAYA
FSTENWQRPIEEVDFLMLLFERLLRRELAQMHREGVRISFIGDLSALPKSLQTEMERSMTETLNNQAIHF
TVAVNYGSRNEITRACRQVAELVQQGKLSADAVNEQLVEQHLYTADTPPPDLLIRTSGEMRLSNFLLWQM
AYTEMYFTDILWPDFDRAAFHQALLSYQKRDRRFGQVKALIPA
>gnl|CDD|237828 PRK14833, PRK14833, di-trans,poly-cis-decaprenylcistransferase
MDNTLKHLAIIMDGNGRWAKLRGKARAAGHKKGVKTLREITIWCANHKLECLTLYAFSTENWKRPKSEVD
FLMKLLKKYLKDERSTYLENNIRFKAIGDLEGFSKELRDTILQLEEDTRSFKGFTQVLALNYGSKDEISR
AFKKLLESPPSHIGELESLEEEISNCLDTADLPEVDLLIRTGGEMRLSNFLLWQSSYAELFFTPILWPDF
TPKDLENIISDFYKRVRKFGGLK
>gnl|CDD|237829 PRK14834, PRK14834, isoprenyl transferase
AAAPAKDESDAMSVPRHVAIIMDGNGRWAKARGLPRAAGHRAGVEALRRVVRAAGELGIGYLTLFAFSSE
NWSRPASEVSDLFGLLRLFIRRDLAELHRNGVRVRVIGERAGLEADICALLNEAEELTRNNTGLNLVIAF
NYGSRDEIARAVRRLAREVAEGRLDPASIDAETISANLDTADIPDPDLIIRTSGEQRLSNFLLWQAAYSE
LLFVPIHWPDFDKAALEAAIEEYARRERRFGGLAAKTGA
>gnl|CDD|237830 PRK14835, PRK14835, isoprenyl transferase
MVRAPLKSAVRTAQRTRSAARGPLYWGYEQRLEREVKHGKLPRHLGLILDGNRRFARALGLQREMGHEFG
VQKAYEVLEWCLELGIPTVTIWVFSTDNFSRSPAEVETLMNLFEREARRMAVDPRIHANRVRVRAIGRHD
GFPPKVLEALEELEERTEGHEGMLLNIAVGYGGREEIVDAVKSLLLEAAATGKSPEEVAAELTPEHISAH
LYTAGVPDPDFIIRTSGEIRLSGFLLWQSAYSEYYFCDVYWPGFRKVDFLRALRDYQGRERRFGR
>gnl|CDD|237831 PRK14836, PRK14836, undecaprenyl pyrophosphate synthase; Provisional
AFSSIQMIPANENIPRHIAIIMDGNGRWAKRRGKPRVEGHRAGVRAVRRTIEFCLEKGIEMLTLFAFSSE
NWLRPADEVSALMELFLKALDREVDKLHRNGIRVRFIGDRSRLSPKLQERMEYAERLTASNTRLILSLAV
SYGGRWDIVTAARALAREVAAGKLAPDEIDEALLAQHLALADLPEPDLFIRTSGELRISNFLLWQLAYTE
LYFTDTLWPDFDAQELQQALEDYASRERRFGKTSAQIADRATE
>gnl|CDD|173298 PRK14837, PRK14837, undecaprenyl pyrophosphate synthase; Provisional
MNKNSLPSHVGIIMDGNRRWALKKGLSFFEGHKEGLKRAKEIVKHSLKLGIKYLSLYVFSTENWNRTDSE
IEHLMFLIADYLSSEFNFYKKNNIKIIVSGDIESLSEEVKKSIKDAISFTKNFDGLVLNLAINYGGRNEI
VRAVKKFLSSGLDLETLNENVFSKFLDNPELPDLDLLIRTGGDMRISNFLLWRIAYCEFIFSNVLWPEYY
VNHYSKDLECFKNRKRNFGR
>gnl|CDD|184846 PRK14838, PRK14838, isoprenyl transferase
YKEQIDMNRIPQHIAIIMDGNGRWAKERGKERSFGHQAGAETVHIITEEAARLGVKFLTLYTFSTENWNR
PSDEVAALMSLLLDSIEEETFMKNNIRFRIIGDIAKLPEEVQERLNECEEHTAKNTGMCLVLALSYSSRW
EITEATRQIATLVQNGELNPEEITEESISEHLTTNFMPDPDLLIRTGGEIRLSNYLLWQCAYSELYFCDT
FWPDFDEEELCKAIYDYQKRERRFGKTSEQIS
>gnl|CDD|237832 PRK14839, PRK14839, di-trans,poly-cis-decaprenylcistransferase
MQSSLDRRSGLHVAIIMDGNGRWATARGLPRLAGHRAGVEAIRRVVEAAPDLGIGTLTLYAFSSDNWRRP
AAEVGGLMRLLRAYLRNETERLARNGVRLTVIGRRDRLPDGIPEAIARAEAATAGGDRLHLRIAVDYSAR
DAILAAAAKALGPEGLSREAFSDLLTGDGGDVDLLIRTGGEKRLSDFLLWESAYAELHFTDRMWPDFGAD
DLAAAVADFHGRERRFGGLPAPAVPAAAS
>gnl|CDD|173301 PRK14840, PRK14840, undecaprenyl pyrophosphate synthase; Provisional
MSLALEQAQENFPSLQSLPRHVAIIMDGNRRWYRKHEQFCQKRAISGHYYGAKSLPQIVDTALHLGIEVL
TLFAFSTENFSRSKEEVAELFSLFNSQLDSQLPYLHENEIRLRCIGDLSKLPQELQNNIEQASSATAHYS
RMELVLAINYGGKDELVRAFKKLHQDLANKKISSDDISEELISSYLDTSGLPDPDLLIRTGGEMRVSNFL
LWQIAYTELYVTDVLWPDFTPNDLLEAIKTYQQRSRRGGK
>gnl|CDD|173302 PRK14841, PRK14841, undecaprenyl pyrophosphate synthase; Provisional
MRIPQHVAIIMDGNGRWAKKRGLPRIKGHQRGAEVLHNTVKWSLELGIKYLTAFSFSTENWKRPKEEVEF
LMDLFVQMIDREMELLRRERVRVRILGRKEGLPEKVLKKWQEVEEKTKEFDRMTLVIAFNYGGRREILDA
VESILKDVSQGKKIELTEETFRQYLYLPDVPDPDLIIRTSGEMRLSNFLLWQSAYSELYFFKKLWPDFTK
RDFLRAIESYSKRERRFGGLING
>gnl|CDD|173303 PRK14842, PRK14842, undecaprenyl pyrophosphate synthase; Provisional
MGLFESTIPAHIAVIMDGNGRWAESQGKKRSEGHREGANAIDRLMDASLEYGLKNISLYAFSTENWKRPI
TEIRSIFGLLVEFIETRLDTIHARGIRIHHSGSRKKLTRTVLDKIDFAMAKTKKNKNLTVNFCLNYGSHD
ELLRAAQEVFLARKAKKVTLEKPLKEKEFEKFLYTSPLPPVDLLIRTAGEQRLSNFLLWQSAYAELYFTD
TLWPDFDKNSLVDSLKWYETRTRKFGGLLNG
>gnl|CDD|184847 PRK14843, PRK14843, dihydrolipoamide acetyltransferase; Provisional
MADDKLRATPAARKLADDLGINLYDVSGSGANGRVHKEDVETYKDTNVVRISPLAKRIALEHNIAWQEIQ
GTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDNVTPYGEIERIPMTPMRKVIAQRMVESYLT
APTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNY
VNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGP
IINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI
>gnl|CDD|173305 PRK14844, PRK14844, DNA-directed RNA polymerase subunit beta/beta'
MVDSSYMCASGAFVPRVSYSRSIDLKDSLLDLVKVQKESYDSFTPKNKGNERLEVIFHTIFPINDPLHRA
TIEFISCRVDDPKYDESECIKRGITFSAQVIASIRLVIMQDGISLDEYKSIKESGDHSKLATVIKSIEEQ
EVHFCELPMMTDKGTFIINGVEKVIVSQMHRSPGVFFDSDKGKTYNSGKLIYSARVIPYRGSWLDIEFDV
KDHLYFRIDRKRKLPISVLLKALGLSNNDILDRFYEKIKYIKHKDGWKVPFVPDKFKGVRLPFDLMDVEG
NVLLKANVRITSRLAKKLYDNELKEYLVPFDSICGLFLAEDLIDSASSTKILSAGESIKLEDIKKLELLS
IDEISVLNIDNLSVGPYILNTLFLDENMSYQDALYEIYKVLRPGEVPVLEIVEEFFRNLFFSPEYYDLSN
IGRLKLNSYLGLNYDEDLTVLTHEDIIEIVRKIVLLRDGQGSVDDIDHLGNRRVRSVGEFIENQFRTGLL
KLERAVVDSMSTSSLDKVSPSDFINPKVLTNVLRDFFNSSQLSQFMDQTNPLSEITHKRRLSALGPGGLT
RERAGFEVRDVHPTHYGRICPIETPEGQNIGLINSLAIYARINKYGFIESPYRKVVNRVVTDQIEYLSAI
DEGLYYIADTSAKLDENNCFVDDMLYCRYAGSFVMVSSDQVSYIDVSPKQVISVAASLIPFLENDDANRA
LMGSNMQRQAVPLLKPTAPLVATGMESFVASGSGAVVLAKRDGIVDSSDSNSIVIRAFDKERVNYLDVDI
YHLRKFQRSNHNTCINQKPLVCVGDYVKEGDVIADGPAINSGELALGQNLLVAFMSWQGYNFEDSIIISS
EVVKKDLFTSIHIEEFECVVHDTPLGSEKITRAIPGVNEENLYHLDDSGIVKIGTRVGPGYILVGKVTPK
PSLSLPPETKLLMTIFGEKSFDCADSSLYTSPDVEGTVIDVQVFTRRGVEENERALLIKQKEINDFEKER
DYIINVTSEYFYDELKKLLINSGSQDREKFDSIEREQWWGIGLKNQSISEQVKSLKKDFDEKVSHAIAQF
KRKVEKLHEGYDLPQGVSMSVKVFIAVKHSLQPGDKMAGRHGNKGVISRVVPVEDMPYLEDGTPVDIILN
PLGVPSRMNVGQILETHVGWACKKLGEKVGNILDEINKIKSAFCKGIRSLNDDNFTKFAAAYLDNKKIEN
IDDDEITASVLNTPNKNALNDELNELVENYLNSCKSAYSNLRNFLIEVYSCGSNVSICNNIRDISDNNLI
EFARKLRDGIPVAAPVFEGPKDEQIAKLFELAGLDNSGQAVLYDGCSGEKFDRKVTVGYMYMLKLHHLVD
GKIHARSVGPYSLVTQQPLGGKSHFGGQRFGEMECWALQAYGAAYTLQEMLTVKSDDINGRVKIYESIIK
GDSNFECGIPESFNVMIKELRSLCLNVDLKQNDVVIEDISHTNIAQSFNEVSISIASPESIKRMSYGEIE
DVSTANYRTFKVEKGGLFCPKIFGPVNDDECLCGKYKKRRHRGRICEKCGVEVTSSKVRRERMGHIELAS
PVAHIWFLKSLPSRIGALLDMSLRDIENILYSDNYIVIDPLVSPFEKGEIISEKAYNEAKDSYGIDSFVA
MQGVEAIRELLTRLDLHEIRKDLRLELESVASEIRRKKIIKRLRIVENFIKSGNRPEWMILTTIPILPPD
LRPLVSLESGRPAVSDLNHHYRTIINRNNRLRKLLSLNPPEIMIRNEKRMLQEAVDSLFDNSRRNALVNK
AGAVGYKKSISDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPTLKLNQCGLPKRMALELFKPFVYSKLKM
YGMAPTIKFASKLIRAEKPEVWDMLEEVIKEHPVLLNRAPTLHRLGIQAFEPILIEGKAIQLHPLVCTAF
NADFDGDQMAVHVPISLEAQLEARVLMMSTNNVLSPSNGRPIIVPSKDIVLGIYYLTLQEPKEDDLPSFG
AFCEVEHSLSDGTLHIHSSIKYRMEYINSSGETHYKTICTTPGRLILWQIFPKHENLGFDLINQVLTVKE
ITSIVDLVYRNCGQSATVAFSDKLMVLGFEYATFSGVSFSRCDMVIPETKATHVDHARGEIKKFSMQYQD
GLITRSERYNKVIDEWSKCTDMIANDMLKAISIYDGNSKYNSVYMMVNSGARGSTSQMKQLAGMRGLMTK
PSGEIIETPIISNFREGLNVFEYFNSTHGARKGLADTALKTANSGYLTRRLVDVSQNCIVTKHDCKTKNG
LVVRATVEGSTIVASLESVVLGRTAANDIYNPVTKELLVKAGELIDEDKVKQINIAGLDVVKIRSPLTCE
ISPGVCSLCYGRDLATGKIVSIGEAVGVIAAQSVGEPGTQLTMRTFHIGGVMTRGVESSNIIASINAKIK
LNNSNIIIDKNGNKIVISRSCEVVLIDSLGSEKLKHSVPYGAKLYVDEGGSVKIGDKVAEWDPYTLPIIT
EKTGTVSYQDLKDGISITEVMDESTGISSKVVKDWKLYSGGANLRPRIVLLDDNGKVMTLASGVEACYFI
PIGAVLNVQDGQKVHAGDVITRTPRESVKTRDITGGLPRVIELFEARRPKEHAIVSEIDGYVAFSEKDRR
GKRSILIKPVDEQISPVEYLVSRSKHVIVNEGDFVRKGDLLMDGDPDLHDILRVLGLEALAHYMISEIQQ
VYRLQGVRIDNKHLEVILKQMLQKVEITDPGDTMYLVGESIDKLEVDRENDAMSNSGKRPAHYLPILQGI
TRASLETSSFISAASFQETTKVLTEAAFCGKSDPLSGLKENVIVGRLIPAGTGLIMNKVRALSLCDNVDK
YEKYFDIETYDEKLLMDNGCHLHSDEEESVVASHYD
>gnl|CDD|237833 PRK14845, PRK14845, translation initiation factor IF-2; Provisional
KDKKEKRLRCPIVAVLGHVDHGKCLLPEEKVILPEHGLITIKELFDLAKEVVEKDEEKEIRKLNIKVTGV
GEDGELSLLNAPYVWKVRHKGKMIKVKLKNWHSVTVTPEHPFLTNRGWVKADELKPGDYVAIPRKIYGNE
DFEKFLSFVYSKLNGEKPKHYIKLPKSLEEWKAFFYLAGVMFGRRKSSYEIEFTNGKNALLNLIKVLFDY
PESHNIEVPQILFLAPKELVAEFLRGYFDADGHVNLRSVRIEVSSASHEFIEDLSLLLLRFGIVSKIYRS
TLIISGKRNLENFRKYIGFSVKEKAEALEKIIEKSKKSERYPINEELKRLRLLFGFTRNELSSNIPFYSK
YESEEAPSYEILMEILNSIERGSKNLDKKIAVLEGKIRDHNYLKAFESDGLIKDGKLTELGRELLEVWRN
REFDSKDVDYIRNLIENLVFVPVEDVEEIEYDGYVYDLTTETHNFIANGILVHNTTLLDKIRKTRVAKKE
AGGITQHIGATEIPIDVIKKICGPLLKLLKAEIKIPGLLFIDTPGHEAFTSLRKRGGSLADLAVLVVDIN
EGFKPQTIEAINILRQYKTPFVVAANKIDLIPGWNISEDEPFLLNFNEQDQHALTELEIKLYELIGKLYE
LGFDADRFDRVQDFTRTVAIVPVSAKTGEGIPELLMMVAGLAQKYLEERLKLNVEGYAKGTILEVKEEKG
LGTTIDAIIYDGTLRRGDTIVVGGPDDVIVTKVRALLKPKPLDEIRDPRDKFDPVDEVTAAAGVKIAAPG
LEEVLAGSPIRIVPTKEKIEKAKEEVMKEVEEAKIETDKEGILIKADTLGSLEALANELRKAGIPIKKAE
VGDITKKDVIEALSYKQENPLYGVILGFNVKVLPEAQEEAEKYGVKIFVDNIIYKLVEDYTEWVKEEEEK
KKRELFEKLIKPGIIRLLPDCIFRRSNPAIVGVEVLEGTLRVGVTLIKEDGMKVGTVRSIKDRGENVKEA
KAGKAVAIAIEGAILGRHVDEGETLYVDVPESHVRELYHKYMDRLRDDEKEALKMYMELKQKNNPFWGR
>gnl|CDD|237834 PRK14846, truB, tRNA pseudouridine synthase B; Provisional
MSNYWLNIYKPRGISSAQLVSIVKKILGKTKIGHAGTLDVEAEGILPFAVGEATKLIHLLIDARKTYIFT
VKFGMQTNSGDCAGKVIATKDCIPSQEEAYAVCSKFIGNVTQIPPAFSALKVNGVRAYKLAREGKKVELK
PRNITIYDLKCLNFDEKNATATYYTECSKGTYIRTLAEDLALSLQSLGFVIELRRTQVGIFKEENAIRIK
SPDEITKNALEEKSIKIEAILDDILVLDATDSQAQQIKYGQKCLFNYEKDFRHLAKFAYREEFKGNTERS
TTAYTLVREDASTGLTYKLPLEVEFGKMSVDLLWVRYKGTLLAIGSLNKSCFNSLRVFNLTQDFF
>gnl|CDD|184849 PRK14847, PRK14847, 2-isopropylmalate synthase
MLAHPATKYRPFAPFAADHAERAWPARRPAAAPIWMSTDLRDGNQALIEPMDGARKLRLFEQLVAVGLKE
IEVAFPSASQTDFDFVRKLIDERRIPDDVTIEALTQSRPDLIARTFEALAGSPRAIVHLYNPIAPQWRRI
VFGMSRAEIKEIALAGTRQIRALADANPGTQWIYEYSPETFSLAELDFAREVCDAVSAIWGPTPQRKMII
NLPATVESSTANVYADQIEWMHRSLARRDCIVLSVHPHNDRGTAVAAAELAVLAGAERIEGCLFGNGERT
GNVDLVALALNLERQGIASGLDFRDMAALRACVSECNQLPIDVFHPYAWLDQD
>gnl|CDD|184850 PRK14848, PRK14848, type III secretion system effector deubiquitinase SseL
VSDEALALLIGEVENGNQNCIDLLCNLALRNDDLGHKVEKLLFDLFSGKRSGSPDIDKKINQACLVLHQI
ANNDITKNNTEWKKLHAPSRLLYMAGSATTDLSKKIGIAHKIMGDQFAQTDQEQVGVENLWCGARMLSSD
ELAAATQGLVQESPLLSVNYPIGLIHPTTKENILSTQLLEKIAQSGLSHNEVFLINTGDHWLLCLFYKLA
EKIKCLIFNTYYDLNENTKQEIIEAAKIAGISENEDVNFIETNLQNNVPNGCGLFCYHTIQLLSNAGQND
PATTLREFAENFLTLSVEEQTLFNTQTRRQIYEYSLQ
>gnl|CDD|184851 PRK14849, PRK14849, autotransporter barrel domain-containing lipoprotein
MNRIYRVIWNCTLQVFQACSELTRRVGKTSTVNLRKSSGLTTKFSRLTLGVLLALSGSASGASLEVDNDQ
ITNIDTDVAYDAYLVGWYGTGVLNILAGGNASLTTITTSVIGANEDSEGTVNVLGGTWRLYDSGNNARPL
NVGQSGTGTLNIKQKGHVDGGYLRLGSSTGGVGTVNVEGEDSVLTTELFEIGSYGTGSLNITDKGYVTSS
IVAILGYQAGSNGQVVVEKGGEWLIKNNDSSIEFQIGNQGTGEATIREGGLITAENTIIGGNATGVGTLN
VQDQDSVITVRRLYNGYFGNGTVNISNNGLINNKEYSLVGVQDGSHGVVNVTDKGHWNFLGTGEAFRYIY
IGDAGDGELNVSREGKVDSGIITAGMKETGTGNITVKDKNSVITNLGTNLGYDGHGEMNISNEGLVVSNG
GSSLGYGETGVGNVSITTGGMWEVNKNVYTTIGVAGVGNLNISDGGKFVSQNITFLGDKASGIGTLNLMD
ATSSFDTVGINVGNFGSGIVNVSNGATLNSTGYGFIGGNASGKGIVNISTDSLWNLKTSSTNAQLLQVGV
LGKGELNITTGGIVKARDTQIALNDKSKGDVRVDGQNSLLETFNMYVGTSGTGTLTLTNNGTLNVEGGEV
YLGVFEPAVGTLNIGAAHGEAAADAGFITNATKVEFGLGEGVFVFNHTNNSDAGYQVDMLITGDDKDGKV
IHDAGHTVFNAGNTYSGKTLVNDGLLTIASHTADGVTGMGSSEVTIASPGTLDILASTNSAGDYTLTNAL
KGDGLMRVQLSSSDKMFGFTHATGTEFAGVAQLKDSTFTLERDNTAALTHAMLQSDSENTTSVKVGEQSI
GGLAMNGGTLIFDTDIPAATLAEGYISVDTLVVGAGDYTWKGRNYQVNGTGDVLIDVPKPWNDPMANNPL
TTLNLLEHDDSHVGVQLVKAQTVIGSGGSLTLRDLQGDEVEADKTLHIAQNGTVVAEGDYGFRLTTAPGD
GLYVNYGLKALNIHGGQKLTLAEHGGAYGATADMSAKIGGEGDLAINTVRQVSLSNGQNDYQGATYVQMG
TLRTDADGALGNTRELNISNAAIVDLNGSTQTVETFTGQMGSTVLFKEGALTVNKGGISQGELTGGGNLN
VTGGTLAIEGLNARYNALTSISPNAEVSLDNTQGLGRGNIANDGLLTLKNVTGELRNSISGKGIVSATAR
TDVELDGDNSRFVGQFNIDTGSALSVNEQKNLGDASVINNGLLTISTERSWAMTHSISGSGDVTKLGTGI
LTLNNDSAAYQGTTDIVGGEIAFGSDSAINMASQHINIHNSGVMSGNVTTAGDVNVMPGGTLRVAKTTIG
GNLENGGTVQMNSEGGKPGNVLTVNGNYTGNNGLMTFNATLGGDNSPTDKMNVKGDTQGNTRVRVDNIGG
VGAQTVNGIELIEVGGNSAGNFALTTGTVEAGAYVYTLAKGKGNDEKNWYLTSKWDGVTPPDTPDPINNP
PVVDPEGPSVYRPEAGSYISNIAAANSLFSHRLHDRLGEPQYIDSLHSQGSASSMWMRHVGGHERSRAGD
GQLNTQANRYVLQLGGDLAQWSSNAQDRWHLGVMAGYANQHSNTQSNRVGYKSDGRISGYSAGLYATWYQ
NDANKTGAYVDSWALYNWFDNSVSSDNRSADDYDSRGVTASVEGGYTFEAGTFSGSEGTLNTWYVQPQAQ
ITWMGVKDSDHTRKDGTRIETEGDGNVQTRLGVKTYLNSHHQRDDGKQREFQPYIEANWINNSKVYAVKM
NGQTVGREGARNLGEVRTGVEAKVNNNLSLWGNVGVQLGDKGYSDTQGMLGVKYSW
>gnl|CDD|237835 PRK14850, PRK14850, penicillin-binding protein 1b; Provisional
MFFNFKKYIMRFLIYVFFFVLLLILCYGVYLYVKINRFINGKVWNFPTSIYSRIVNLEPGNSYSQKDVIH
LLKSTMYRKVDLVTLPGEFSVKNNTIELIRRSFDFPDIREDEIHARLYFNKDKLVRIKNIDNNHDFSFLR
LDPKLIAMLYSPEGKKRLFIPRNQYPEMLIKTLLAIEDKYFYEHDGIHLSSIGRAFLVNLMSGHTIQGGS
TLTQQLVKNLFLTNTRSLWRKINEIYMALILDRFYSKDRILELYLNEVYLGQDGNEQIRGFPLASIYYFG
RPINELNLDQYALLVGMVKGASLYNPWTNPNLTLKRRNLVLFLLYKQKVITRKLYKDLCSRPLNVQSKGN
IISSHPAFIQLVCEEFHKKIHYPFKNFSGTKIFTTLDYISQNAAEQAVKIGIPILKRKKRLKDLEVAMVI
IDRFSGEVRALIGSSKPEFNGYNRALKARRSIGSLSKPITYLTALSQPEKYHLNTWISDTPISIKLDNGQ
YWTPKNNNFSFSGKVMLIDALIHSINIPTVHLSINLGLKKLVDSWILLGISSNYITPLPSISLGAINLTP
MEVAQVFQIIGSGGYKSSLSSIRSIISDDNKVLYQNFPQSKHVESSQASYLTLYAMQQVVKSGTAKSLGT
IFKEFSLAGKTGTTNNLVDSWFVGIDGKQVVITWIGRDNNHTTKLYGSSGAMKIYKRYLQYQNPVPLVLK
APNNINMFYINNLGELFCKKGNNQYNRMLPIWSINNKKICNDKLSERFSIKKKKNFLFWLKNLF
>gnl|CDD|184853 PRK14851, PRK14851, hypothetical protein; Provisional
MKIDSHLETLQTLGISSAAEYREAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRF
HIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSINPFLEITPFPAGINADNMDAFLDGVDVVLDG
LDFFQFEIRRTLFNMAREKGIPVITAGPLGYSSAMLVFTPQGMGFDDYFNIGGKMPEEQKYLRFAMGLAP
RPTHIKYMDLSKVDLKGGKGPSLNIACQLCSGMAGTEAVRIILGKGGLRPVPCYLQFDPFLQKLRKGRLS
RGNKTPSQRAKLWYVQNVLIRNTDQARVREPEPPVSVAHFDSLPQGVGDYILQAGIQAPSGDNVQPWQFA
LAGNDIHLYLDPEADVSFFNVRQTASIISCGAVMENMRIAATTFGLDATTQYRPDAAQEDLMATVRLQPG
DHTKDPLADHIWKRCTNRKPYSKRPLPEWVLNDLKTRIRSIPGAHLHFITGRDQLRKLAKVIYLADRIRT
EHQGLHEHFTSMIRFNMKEALQKRDGFPLKNLEAGVAGEAFLRLTRPWPVMNIANKIGLGRLVALHSYQG
ILESSGAALVVVDGFETRDFLLGGQALERIWLTLEHHGLQMQPMTAVTLFWLRWLLEGPSSFSEKHRKLL
ERIWQDYKGLFASVDFEKQGQVMLFRFGYGPGIKHRTLRRGAGDFCVMK
>gnl|CDD|184854 PRK14852, PRK14852, hypothetical protein; Provisional
MLAIADKRRTIRIKRSSLLQNKLGALDRPAIKIAETPDEYTRAFRLVYEEYIRSGYLKPHPSRMYYNVWS
ILPATSVFIFKSYHDVLCTLTHIPDSGLFGLPMDTLYKPEVDALRAQGRNVVEVGALATQYSRRWTNLMV
FLAKAMFQYSMMSEVDDILVTVNPKHVKFYTDIFLFKPFGEVRHYDTVDAPAVALRIDLHEAMDELQEKY
GDEEDFETNLFAFFARMNSDETETSENPVRRDRPLEPYTAYYLLQQRPELLDHLAEPQRDHIETIYHRAV
FNHFSTNPVHPETPGGVPLDMLKLETRDAYTDIAFSRNLGLVDYAGQRRLLRSRVAIAGLGGVGGIHLMT
LARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPFLDIRSFPEGVAAETIDAFL
KDVDLLVDGIDFFALDIRRRLFNRALELGIPVITAGPLGYSCALLVFMPGGMNFDSYFGIDDDTPPMEGY
LRFGMGLAPRPAHLGYMDRRFVSLHDRRGPSLDIACHLCAGMAATEAVRILLHRRGIRPVPYFRQFDPLT
GRHVRGRLRKGLRSPLQRLKLAIARRFFMGAPRTGTPPPPEPDVVALRQDIPLETLHYVARAAMQAPSGD
NVQPWRFVPHATGLHIHLDRQADGSFFDYRHVASLLACGAAVQNAVYASGSAGLDATLSLFPDATKPDRV
ASLHCTPLGVPSHEIMTAALWRRHTNRRMYAARPLPVEVCERIEHLVSEEQDATLLWATDAAQRKTLARA
VYLADRVRVERRDMHEHLMRFIRFDGQAEQQGEVGQQGHTGQAGHHSHAGNGPYGDGLPLANLEAGLAGE
LYLRAVRPWRNMSIANALGLGRLMPLHGAMGVLRSGGIGLLLANGETETDIARAGMAWQRAWCALEHMGY
AMQPLAALPLLHLRLAMGDPQTLDTAHQRLLEEAWTLLEQVLPHPKGRLPVMMFRAGVAAPIRHGTFRRP
LSDFLLPAE
>gnl|CDD|184856 PRK14854, nhaA, pH-dependent sodium/proton antiporter; Provisional
MSASQKNQELIGGLILFSAALLAIVVNNSPLASYYAMLETINVKLGIENLVIDKNLMHWINDGLMAIYFL
YIGLEIKREIIVGTLSKPSNIITPAIAAFAGLAMPSLIYLSINHDIKVINGWAIPSATDIAFTLGILALL
GTRVPAKLKLLVITIAIFDDIAAIAIIAIFYTKSLSLLSLSLGTLFILAMIICNRIFKINRSSVYVVLGF
FAWFCTIKSGVHATLAGFTTALCIPFRENDKDSPANFMEDSLHPWIIYFILPVFAFANAGISFSGISFSI
LFEPITLGIILGLFVGKQLGIFSILAVFKKLKWFKLGESFSNLQLYGISLLCGIGFTMSLFIGVLAFNDT
HLLNAIKIGVVVGSVLSGFFGYIVLRFIVTNPS
>gnl|CDD|237836 PRK14855, nhaA, pH-dependent sodium/proton antiporter; Provisional
MIQTLLSPFQRFVESEAFAGLLLVGTAVAAFIWANSPWREGYFTLQHTHLALSLGGWSLDLSLEHWVNDG
LMAVFFLLVGLEIKRELLIGELSSPRQAALAVVAALGGMLVPAALYTALNAGGPGASGWGVPMATDIAFA
LGVLALLGSRVPLGLKVFLTALAIVDDLGAVLVIALFYTSGLNLLALLLAALTWALALLAGRLGVTSLKI
YAVLGALLWFFVLKSGLHPTVAGVLLALAVPIRRRDPLPYLASLLDAAAPGRPEVVGARLRDLEDLLERA
QSPLHRLEHALHPWSTFLILPVFALFNAGVSVSGGGLGTVSLGVFLGLLLGKPLGVVGGAWLAVRLGLAS
LPRRVNWLHMLGAGLLAGIGFTMSLFISNLAFADAALLTQAKLGVLAASVLAALLGAGWLWWAVRGQPGE
PND
>gnl|CDD|184858 PRK14856, nhaA, sodium/proton antiporter NhaA
MNLKKTENALSLTLKNFIKSESFGGIFLFLNAVLAMVVANSFLKESYFALWHTPFGFQIGDFFIGFSLHN
WIDDVLMALFFLMIGLEIKRELLFGELSSFKKASFPVIAALGGMIAPGLIYFFLNADTPSQHGFGIPMAT
DIAFALGVIMLLGKRVPTALKVFLITLAVADDLGAIVVIALFYTTNLKFAWLLGALGVVLVLAVLNRLNV
RSLIPYLLLGVLLWFCVHQSGIHATIAAVVLAFMIPVKIPKDSKNVELLELGKRYAETSSGALLTKEQQE
ILHSIEEKASALQSPLERLEHFLAPISGYFIMPLFAFANAGVSVDSSINLEVDKVLLGVILGLCLGKPLG
IFLITFISEKLKITARPKGISWWHILGAGLLAGIGFTMSMFISNLAFTSEHKDAMEVAKIAILLGSLISG
IIGALYLFALDKRAALKK
>gnl|CDD|184859 PRK14857, tatA, TatA/E family twin arginine-targeting protein translocase
MNIFGIGLPEMAVILVIALLVFGPKKLPEIGRSLGKTLKGFQEASKEFENEIKREMAEPEQEVKAPAELE
SNQTNEANQEQVDAENSPES
>gnl|CDD|184860 PRK14858, tatA, twin arginine translocase protein A; Provisional
MFGIGMPELIVILVIALIVIGPQKLPDLARSLGRGLAEFKKATDDFKQSMQEESRTAEEKEKAEKLAETK
KEAEAPEAKAEEDQAPKPKGAGEPPATVASKAGDGAKA
>gnl|CDD|184861 PRK14859, tatA, twin arginine translocase protein A; Provisional
MFGIGMPELIVILVIVLIVFGAGKLPEIGGGLGKSIKNFKKATSEKEEIEIKPTKKEDKKKKK
>gnl|CDD|184862 PRK14860, tatA, twin arginine translocase protein A; Provisional
MFGFGMPELIVILVIALVVFGPAKLPQLGQALGGAIRNFKKASNEEDVVTINNEKGKEDQARSD
>gnl|CDD|237837 PRK14861, tatA, twin arginine translocase protein A; Provisional
MFSNIGFPGLILILVVALIIFGPKKLPELGKALGKTLREFKKATKELTDDDFQEKKKKEKM
>gnl|CDD|184865 PRK14863, PRK14863, bifunctional regulator KidO; Provisional
MSSPVSKLGLAAAQFGLDPGSSSAPRGRTPEAEARDILNIAARAGLSVLDASGLFGRAETVLGQLIPRPV
PFRVTLSTVRADRGPDFVEAEARASLRRMGVERADAILVHSPTELFGPHGAALWERLQALKDQGLFAKIG
VSAHASDDPVGVARRFKPDILQAPASLLDQRLLADGSLQRIAGMGVEVHLRSIFLNGLLFLPPDRVPAQL
KGASGRLSRVRRMIAEGRSDPLQAALGFALSRPEGSAVLVGVNSAAELSAVVAAASSPPPDLDWDDMAID
DPVALDPRRWVA
>gnl|CDD|184866 PRK14864, PRK14864, biofilm peroxide resistance protein BsmA
RNMVMRRFASLLLTLLLSACSALQGTPQPAPPPADHAQEIRRAQTQGLQKMGTVSALVRGSPDDAEREIQ
AKANAAGADYYVIVMVDETVVPGQWYSQAILYRK
>gnl|CDD|237840 PRK14866, PRK14866, hypothetical protein; Provisional
MMIAIVVSRADPASVHIREHLLELLDWEERSDEGRPDGGGTYYRSDGFELREFDERHIHLDGIAEAFFDP
DLLIFASRHSSVDTGPLLTAHFTGNFGPAEYGGEPGSLAPAAPNAMKAVLEALAEHAPEGYDVSMECTHH
GPTDVGVPSLFVELGSTEKEWDDPDAARAVARAILDLRGVPPHTDRPLVGFGGGHYAPRQTRIVLETDWA
FGHIAADWQLGALGDPAVLRAAFEASGADAAYIDRKAMSSGDRPRLEALLEELGLRVLSETWLRETGGVP
LSLVRALEDLAGTIDPGLRFGEPARLGDGDPVVVDLPGELLDEAQGVDREAVRAALDEHPVAFLTTGGGT
RLGGFIAFEAADSDIREDLVDLCVKVLKEKYDSVYRGDNELVIRKERFDPELARKLGVPEGPAFGKLAAG
QPVEVDGETITPEMVHRETTKRIHLPGLERY
>gnl|CDD|237841 PRK14867, PRK14867, DNA topoisomerase VI subunit B; Provisional
NVVMEESLFDEFKEHSISEFFRKNKHMLGYSGKLRSMTTIIHELVTNSLDACEEAEILPDIKVEIEKLGS
DHYKVAVEDNGPGIPPEFVPKVFGKMLAGSKMHRLIQSRGQQGIGAAGVLLFSQITTGKPLKITTSTGDG
KIHEMEIKMSVEKNEGDIVSHKVREGFWRGTRVEGEFKEVTYNRREQGPFEYLRRISLSTPHAKITLKDP
EETVVFDRTVDEIPEKPEEMKPHPYGLTTDELLYIARKTDSSKVSSMLNSELSRVTTKRIKELEEYVLRD
LLLENYRDSVFWDTVVSCYLNFDFTKYFDKYGHYFDKKEIEDVKMLINGLPESLGELKTYCLKYLVMEYL
FNKLDEEEIKEIKNHFKKKPENFMEWAEKNYLNASLLDEFRKKVKNITKSPEEFVKELKDKAMVSDEELE
KYRKEIKDLLKKNPKEMTWKEAELIVNVLQDMDFMAPSTTGLRPIGAENIEKSLETLEPDFLKTLTRKPK
TYKGGIPFAVEVGLAYGGNAGRQGDEGRKMEIMRFSNHVPLLFDTSGCGLTNAVKSVNWRRYGLRSDEDA
PITVFVNLISTHIPYTSAGKQAIACSEEENEEIFNEIRQALMICARELEKYISRIRREKEEEQKRKYVMK
YAVIFAEGLASITGKPKEEIEENVVKLLR
>gnl|CDD|237842 PRK14868, PRK14868, DNA topoisomerase VI subunit B; Provisional
MTSFQSTLGDEEGIAEELAESQREISIAEFFEKNKHMLGFDSGARGLVTAVKEAVDNALDATEEAGILPD
IYVEIEEVGDYYRLVVEDNGPGITKEQIPKVFGKLLYGSRFHAREQSRGQQGIGISAAVLYSQLTSGKPA
KITSRTQGSEEAQYFELIIDTDTNEPEISVEETTTWDRPHGTRIELEMEANMRARQQLHDYIKHTAVVNP
HARIELREPDESLKFERATDQLPAETEEIRPHPHGVELGTLLKMLEATDSYSVSGFLQEEFTRVGKKTAD
SVIDNFRDRHFGREMAWRPPQAHEDVDLEAAVADAVANKGADATAAFARAVADAVADRDRIAHHELEAIV
DSAADDVEDDTGTTFGETVRENAVEAAWSALTDDREADCYALVDDATTTRKDDAAVEGLAERLAAKFDDG
GDRHRLTRDTLREYVDRAADMTEEYDDATFGETARENVVEALWSRMATVPDDPPNVSEIADDRDAASDLL
EAMRETDIIAPPTDCLSPISAELVEAGLRKEFDADFYAAATRDAEVHGGDPFIVEAGIAYGGEIDSEGSV
DVMRFANRVPLVYQRGACATTDVVKSIGWRNYGLDQPGGSGLPNGPAVIMVHVASTNVPFTSESKDAIAN
VPEIEDEIELAIREAARELKSYLNKRRSMQKRREKQDVLGTILPEMATKVAEVTGREEPDIDDSLARIMN
NVLVEREVEDDTVTLVVENHSDTNEDVEITDIVSAEPDGLGDDATVVEMDGEWFVKWSPTVPSGDTATLE
YSVDDDAEFDLSVDGVETEKLTVNA
>gnl|CDD|237843 PRK14869, PRK14869, putative manganese-dependent inorganic diphosphatase
MMKPIYVIGHKNPDTDSICSAIAYAELKNKLGEGNYIPARLGELNPETKFVLDYFGVEAPELIEDVKPQV
RDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYMDILDPEILSKSPTSL
ENIIRTLDGEVLVGAEEDKVEEGKVVVAAMAPESLLERIEEGDIVIVGDREDIQLAAIEAGVRLLIITGG
APVSEDVLELAKENGVTVISTPYDTFTTARLINQSIPVSYIMTTEDLVTFSKDDYLEDVKEVMLKSRYRS
YPVVDEDGKVVGVISRYHLLSPVRKKVILVDHNEKSQAVEGIEEAEILEIIDHHRLGDIQTSNPIFFRNE
PVGSTSTIVARMYRENGIEPSPEIAGLLLAAILSDTLLFKSPTTTELDREAAEWLAEIAGIDPEEFAKEM
FKAGSSLEGKTPEEIFNRDFKEFTIGGVKFGVGQVETMDFEEFFELKEELLEALEKLREEEGYDLLLLMV
TDIIEEGSELLVAGDEKEIVARAFGVPLEDNSFYLPGVVSRKKQVVPPLTKALRTL
>gnl|CDD|184872 PRK14872, PRK14872, rod shape-determining protein MreC; Provisional
NTLGPRHKKVRFIVYLIIALGIIVSWSLPRPVYEKIQDTFVSLCSKFFPKFRQGPSSHALVLETENFLLK
ERIALLEERLKSYEEANQTPPLFSEILSPYFQKLIMGRVIFRDPAHWGSSCWINVGKRQGIKKNSPVLSG
KVLVGLVDYVGEHQSRVRLITDVGMKPSVMAVRGGIQTWVVKDQLRTLARQVERLPTSYILEKDKYEKLH
QLQELESSLQLSEENDFLLRGILSGRGGPLWKPESLILSGEGFGFSDGKTLRVGDILVTTGLDGVFPPGL
LVATVTKVLPPREGACSYKIEAQSLAPDLSTLDSVLVLPPMEFNPNDRPDIFGLLWD
>gnl|CDD|237844 PRK14873, PRK14873, primosomal protein N'
MAATRVPAEELPVARVLPDLGLPHLDRLFDYLVPEELSDDAQPGVRVRVRFGGRLVDGFVLERRSDSDHE
GKLRWLERVVSPEPVLTPEIRRLARAVADRYAGTRADVLRLAVPPRHARVEKEPVATPPPPLTAPPPDPS
GWAAYGRGPRFLAALAAGRAARAVWQALPGEDWARRLAAAAAATLRAGRGALVVVPDQRDVDRLEAALRA
LLGAGDVAVLSAGLGPADRYRRWLAVLRGQARVVVGTRSAVFAPVEDLGLVAIWDDGDDLLAEPRAPYPH
AREVALLRAHQHGCALLIGGHARTAEAQALVESGWAHDLVAPRPVVRARAPRVRALGDSGLALERDPAAR
AARLPSLAFRAARDALEHGPVLVQVPRRGYVPSLACARCRTPARCRHCTGPLGLPSAGGTPRCRWCGRAA
PDWRCPRCGSDRLRAVVVGARRTAEELGRAFPGVPVVTSGGDQVVDTVDAGPALVVATPGAEPRVEGGYG
AALLLDAWALLGRQDLRAAEDTLRRWMAAAALVRPRADGGQVVVVAESSLPTVQALIRWDPVGHAERELA
ERAEVGFPPAVRMAAVDGRPAAVAALLEAAGLPDGAEVLGPVPLPPGVRRPAGIDAREDRVRALVRVPRA
RGAELAAALRRAVAVRSARREPGPLRVQIDPLDIG
>gnl|CDD|237845 PRK14874, PRK14874, aspartate-semialdehyde dehydrogenase; Provisional
GYNVAVVGATGAVGREMLNILEERNFPVDKLRLLASARSAGKELSFKGKELKVEDLTTFDFSGVDIALFS
AGGSVSKKYAPKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEALAEHRKKGIIANPNCSTIQMVVALKP
LHDAAGIKRVVVSTYQAVSGAGKAGMEELFEQTRAVLNAAVDPVEPKKFPKPIAFNVIPHIDVFMDDGYT
KEEMKMVNETKKILGDPDLKVSATCVRVPVFTGHSESVNIEFEEPISVEEAREILAEAPGVVLVDDPENG
GYPTPLEAVGKDATFVGRIRKDLTVENGLHLWVVSDNLRKGAALNAVQIAELLI
>gnl|CDD|184875 PRK14875, PRK14875, acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVG
ALLAVVADAEVSDAEIDAFIAPFARRFAPEGIDEEDAGPAPRKARIGGRTVRYLRLGEGDGTPVVLIHGF
GGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDALGIERAHLVGHSMGGAV
ALRLAARAPQRVASLTLIAPAGLGPEINGDYIDGFVAAESRRELKPVLELLFADPALVTRQMVEDLLKYK
RLDGVDDALRALADALFAGGRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLPDGVAVHVLPGAGH
MPQMEAAADVNRLLAEFLGKA
>gnl|CDD|237846 PRK14876, PRK14876, conjugal transfer mating pair stabilization protein TraN; Provisional
MRSHNYFMRTVASLLTVTMSALPIHSYANGAQAQDITAVGKEAQSFGQNLSNSFKSSSGTVQDGTISMPT
LKDGQFQMGGGSSVNVNDLFPGTSGTNNKPDYFPDANKPDVDGLQGIYDSGDDMDDVGNSAKGSLWSDAN
SANPSISGAAYKVLLDSSNRSRPDFSNDPVLNLSKKTYEDMDLIAGGFGDCSAETTINQNTINAHIPEYE
RCQRVVDQSGDCEVVHDYDAGVVKHYSGPYNLQSCGEGCTELWVGTVGDNYWSGNCKIYEEYTRVQVSNP
DAIISATLERAKWDDYMQVLVGKSGQETKVWSGPDGVFPPETAGRCERSTSWERNPNVDITPKFKSVKDG
DVVTFKIRTSVTGAGEGYGRIKIRYDPAKAITKDEWAPQSCMDSAKGVEDGFCEGEITCIDDPTDANGCT
VINGVKVCESDLKPSPLPGIPKLCKKVRVKADCDFYKGQMDCWTDPQGVTHCPVNDGGNLNSCQKYEENP
QCGFISSKCIDGAQGSSGTCYVFEDTYDCGTDVSVPTLEKETEYQCGGPIRCMGDDCLDLTKTQSTDFAR
ATALLNAAQFATQDMSCTGQDTDDNPAGDENVICSVFKGEAGECKIAVGGVSDCCEKPTNISLADYLNLI
MAVPKLDGAVMGLARTDGNALKGAYQVLREPAMQGWTEVTKPFTSYIENVSGAVDSFFQPVEQFVDQLIG
QLKEQVKQVMMDVMKSAGADAATEAAAAAASEQAAEALMETATTWLSTAMTVYTVYVVAMVMIQMIWKCE
EEEFTMNAKRALKNCTYVGSYCKSKVLGACIEKREAYCCFNSPLSRIIQEQVRPQLGLNFGDPKNPQCEG
IPLDKIAEIDWSKVNLDEWLGILQQNGKLPTPASINLDSLTGAGSDFNIDGTRKNAQERALERLEGIDVD
AKRKEATNSIDPQTGAPT
>gnl|CDD|184877 PRK14877, PRK14877, conjugal transfer mating pair stabilization protein TraN; Provisional
MKLRKTISSAIIASMIANTMSWAFYVSLINMVMTPRIYAADAIFDQLENNFNLANPNANRNATTSAQDIV
EKYKNADSGENVSGKITEKYVGKAESANLNLGKYGAGNSNESVMKNAASDGKSIGSAVQLPSMSGGTINS
NYTKEGAKLLSRDANGNIGISSNPNTTPGTKTNTGEIFSSEQKHSDIKFNAADRYGDEDGFVNDIKNRKS
QLFDAQSYDGVAYRTLVNANKDNPASSIKPNDPMFTAGRNEITNAVAGTGNWLQNCNVETSKKTVTTHYP
DYKEFYCNSPKQDNFSSCTITRDFSVPVYISGGNGDMSMCGDNCVRIWFGRRDDNYWSDGVYDNELTLKF
HPDAKLASAKIVNAEWDDHMRVTLDGTQIFAHIDGAYRESDYPAPKGSWELKKSWKLDKVYDVTEKVRKS
VYEEPDREVTMASRVWVGGGGEGYFEVELTFENMKLEDKHVQEPAGCYDAVQTPNTFCRFDRFKDMDVGT
KRLPESVLSMAKPLYEGDKGFLTWKTNLEGYFCDPLAKDKICSYDASGKIMKDANGKDLCYNYEEIKSMP
DACSTYKNDAACVLDKQTCAEGWFDEGTNSCYMYEQKYTCDRGKDVVREVESSTNACVGMIPCSGGTCET
GPKEENNDFGKVAAYSNMVQYMQGEAKCEDPNDANSCSVFEGKPEWCGRSVGFVNGLAKTDCCEAPQGTA
GALEGIMLAGSMIRNTNWTRVNAQLIKWTGGDTGTWASMSNAVGEWTASAGKTVGQMWNNVTSSLTSVYE
NVAGNLSRAVGSSATSGGAGGAGQLAQETMSSFGIGQLKQMAMKKAYELLPDTVRDFVFKNVATTGGEVV
FSAAVQNFMLALNVIGWIYTAYQVTKMLLEMLVACDQKEMEASIHKNQKSCFTLDTERCVKYLNVGFTKK
CVKKATDMCCYNSMLSRVIMQQAYPQLGIDPVASNCVGLSIKQIQQLDFDKIDLTEWINDAVQVGEVPDQ
YSKFSEESIVENLPFQNENYQLPSERTKEAMGGEENMIKARQENAQAIKEENVDCSYLPRPAICEVGSTT
LDPVTGKQLPKY
>gnl|CDD|184878 PRK14878, PRK14878, UGMP family protein; Provisional
LGIESTAHTLGVGIVKEDKVLANVRDTYVPEKGGIHPREAAQHHAEVAPELLRKALEKAGISIEDIDAVA
VSQGPGLGPALRVGATAARALALKYNKPLVPVNHCIAHIEIGRLTTGAKDPVVLYVSGGNTQVLAFRGGR
YRVFGETLDIAIGNALDTFAREVGLAPPGGPAIEKCAEKGEKYIELPYVVKGQDLSFSGLLTAALRLYKG
KERLEDVCYSLRETAFAMLVEVTERALAHTGKKEVLLVGGVAANRRLREKLEIMAEDRGAKFYVVPPEYA
GDNGAMIAYTGLLAYKHGVTIPPEESFVRQRWRLDEVDVPWRN
>gnl|CDD|237847 PRK14879, PRK14879, Kae1-associated kinase Bud32
MKLIKRGAEAEIYLGDFLGIKAVIKWRIPKRYRHPELDERIRRERTRREARIMSRARKAGVNVPAVYFVD
PENFIIVMEYIEGEPLKDLINSNGMEELELSREIGRLVGKLHSAGIIHGDLTTSNMILSGGKIYLIDFGL
AEFSKDLEDRAVDLHVLLRSLESTHPDWAEELFEAFLEGYREVMGEKAEEVLERVKEIRLRGRYVEERRK
K
>gnl|CDD|237848 PRK14886, PRK14886, KEOPS complex subunit Cgi121
MEMMIIEGTVTIEDVDGFLEEIDAIADEHGVTVQAFNADCIAGREHVEHAIILALRAFERGRNIAKDLGV
EILLRAAGRRQISRAIKIIGAKEGENNIVVVVDEEEAADAVIDLLGGLVDDSVLELDEAKEEKIRSLFDI
TEAELAACDGELVELVLERVALLEVLK
>gnl|CDD|237849 PRK14887, PRK14887, KEOPS complex Pcc1-like subunit; Provisional
MRMHKFTLEFEFETEERARIIYRSVLPEHGDSQGERSKADLSLDGNTIVITIEAEDLSALRASLNSWLRL
IKVAEEVLELGKAA
>gnl|CDD|237850 PRK14888, PRK14888, KEOPS complex Pcc1-like subunit; Provisional
VAKALEPDNLDIMETEVDGDTVVYTIESEKIGTLLNTVDDYLMNLKVAEKVIEALSKET
>gnl|CDD|184883 PRK14889, PRK14889, VKOR family protein; Provisional
IILLGNGILYLLLAFSLVGLIASIASYLLFTLLVKPPPFCTINSVINCSSVLSSPYARFLGIPLDYLGAA
WFSANIALALLGVGTLKRILGRVISLWSIIGLAIVPYLVYLEVFVLGAICIYCTIAHVSILAAFILILIK
LKV
>gnl|CDD|184884 PRK14890, PRK14890, putative Zn-ribbon RNA-binding protein; Provisional
ISEMMEPPKCTSCGIEIAPREKAVKFLCPNCGEVIIYRCEKCRKQSNPYTCPKCGFEGP
>gnl|CDD|184885 PRK14891, PRK14891, 50S ribosomal protein L24e/unknown domain fusion protein; Provisional
MVETRTCDYTGEEIEPGTGTMFVRKDGTVLHFVDSKCEKNYDLGREARDLEWTEAGRAEKGPAAAATAAA
EAAEEAEAADADEDADEAAEADAADEADEEEETDEAVDETADEADAEAEEADEEEDEEAEA
>gnl|CDD|184886 PRK14892, PRK14892, putative transcription elongation factor Elf1; Provisional
MGRRRKKRKKIIRPKPKLPKIFECPRCGKVSISVKIKKNIAIITCGNCGLYTEFEVPSVYDEVDVYNKFI
DLYLEGKIEIKERKNEETEEENEIEGESE
>gnl|CDD|184887 PRK14893, PRK14893, V-type ATP synthase subunit K; Provisional
MVEIALGTALAAIGAGVAVGFAGLGSGLGQGIAAAGSVGAVAEDSDMFARGIIFSALPETQAIYGFLIAI
LLLVFSGLLGGGEGLSVTAGLVAIGAGAAIGFAGLGSGMGQGIASASSVGAVVEDPDMFARGIIFSALPE
TQAIYGFLIAILLMVFGGILG
>gnl|CDD|237851 PRK14894, PRK14894, glycyl-tRNA synthetase; Provisional
MPATSLDQIVALAKRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIADWWRTNVYERDDMEGLDAAILM
NRLVWKYSGHEETFNDPLVDCRDCKMRWRADHIQGVCPNCGSRDLTEPRPFNMMFRTQIGPVADSDSFAY
LRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQMEIEYFVMPGTDEEWHQ
RWLEARLAWWEQIGIPRSRITIYDVPPDELAHYSKRTFDLMYDYPNIGVQEIEGIANRTDYDLGSHSKDQ
EQLNLTARVNPNEDSTARLTYFDQASGRHVVPYVIEPSAGVGRCMLAVMCEGYAEELTKAIPGEKLAAVG
DALEAFLKSVGRSEKLAGEARDAILARGEALLQALPERLPEVEQLLAMPGADQIELGKKLRGQAQPLIDE
HYRTVLRLKPRLAPIKVAVFPLKRNHEGLVATAKAVRRQLQVGGRMRTVYDDTGAIGKLYRRQDEIGTPF
CITVDFDTIGQGKDPALAGTVTVRDRDTMAQERVPISELEAYLRDRVSA
>gnl|CDD|237852 PRK14896, ksgA, 16S ribosomal RNA methyltransferase A
IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDD
EIAAGNVEIIEGDALKVDLPEFNKVVSNLPYQISSPITFKLLKHGFEPAVLMYQKEFAERMVAKPGTKEY
GRLSVMVQYYADVEIVEKVPPGAFSPKPKVDSAVVRLTPREPKYEVYDEDFFDDFVKALFQHRRKTLRNA
LKNSAHISGKEDIKAVVEALPEELLNKRVFQLSPEEIAELANLLYEVG
>gnl|CDD|237853 PRK14897, PRK14897, unknown domain/DNA-directed RNA polymerase subunit A'' fusion protein; Provisional
NNLLWKDTFKNIEEIIENVPVYYAVDFEVPKNITDGYITLKKKEFTYHVIISKIAPYSNSNGIIKKKKPV
LKTVLEIESEEKIEAIDLMEFKRLFGRILDENMSFSTGELLTAEEKEYYEENSNEDVLKVIDDVKKLGFR
LPPSVIEEIAKAMKKKELSDDEYEEILRRIREEYERARVDPYEAVGIVAAQSIGEPGTQMTMRTFHYAGV
AEMNVTLGLPRLIEIVDARKKPSTPTMTIYLKKDYREDEEKVREVAKKIENTTLIDVADIITDIAEMSVV
VELDEEKMKERLIEYDDILAAISKLTFKTVEIDDGIIRLKPQQPSFKKLYLLAEKVKSLTIKGIKGIKRA
IARKENDERRWVIYTQGSNLKDVLEIDEVDPTRTYTNDIIEIATVLGIEAARNAIIHEAKRTLQEQGLNV
DIRHIMLVADMMTFDGSVKAIGRHGISGEKSSVLARAAFEITGKHLLRAGILGEVDKLAGVAENIIVGQP
ITLGTGAVSLVYKGRKKVK
>gnl|CDD|237854 PRK14898, PRK14898, DNA-directed RNA polymerase subunit A''; Provisional
MDIEALREKIEDLDLPRSLKDELFEKLSKRDGVTEEMVEEIIDEVVSAYLNALVEPYEAVGIVAAQSIGE
PGTQMSLPYDEKIIVKEGGETRVTEIGKLVDELIDKFGFEKIGGHEVCDLPIEIYALSLDQDEKVHWKRI
ISVIRHKANGKLIKIKTESGRTIRATPYHSFVTRKDNEVIPVEGSELKIGDWLPVVRSLPANCQEAIDLR
EYLPASDYGEIEEHAVYPVQGTVGLPETFPLDEETGYFVGAYLAEGSLTDHYVSISNVDETFQNRVRAFA
ERFDLSVNEYENDSGFATGYDIRLNGTVLSDFLRNFCTDDGEKKIPDFAFGANKEFVRGLLQGYFDGDGN
VGTNKKAIRISSTSKELIDGISLLLARFDIYATKGTQKDSFTLRIPKKYVKKFTEEIGMSVGERGDELED
LATSLDSDGTPDSIDMIPSIGDALTKLAEKAGYPSRQVNKFEKRQRIGRSRLQRHLRRIEELAVERGPEL
LALKEYKKAVESDVVWDEIVSIEEVECDKKYVYDISVEGLETFTTADGVVTHNTMRTFHYAGVAEINVTL
GLPRMIEIVDARKEPSTPIMTVHLKGEYATDREKAEEVAKKIESLTLGDVATSIAIDLWTQSIKVELDEE
TLADRGLTIESVEEAIEKKLGVKIDRKGTVLYLKPKTPSYKALRKRIPKIKNIVLKGIPGIERVLVKKEE
HENDEEYVLYTQGSNLREVFKIEGVDTSRTTTNNIIEIQEVLGIEAARNAIINEMMNTLEQQGLEVDIRH
LMLVADIMTADGEVKPIGRHGVAGEKGSVLARAAFEETVKHLYDAAEHGEVDKLKGVIENVIVGKPIKLG
TGCVDLRIDREYEEGKND
>gnl|CDD|237855 PRK14900, valS, valyl-tRNA synthetase; Provisional
MSNPNPIENENRTELAKGYEHREVEARWYPFWQERGYFHGDEHDRTRPPFSIVLPPPNVTGSLHLGHALT
ATLQDVLIRWKRMSGFNTLWLPGTDHAGIATQMIVEKELKKTEKKSRHDLGREAFLERVWAWKEQYGSRI
GEQHKALGASLDWQRERFTMDEGLSRAVREVFVRLHEEGLIYREKKLINWCPDCRTALSDLEVEHEEAHQ
GELWSFAYPLADGSGEIVVATTRPETMLGDTAVAVHPLDPRYMALHGKKVRHPITGRTFPIVADAILVDP
KFGTGAVKVTPAHDFNDFEVGKRHGLEMITVIGPDGRMTAEAGPLAGLDRFEARKEVKRLLAEQGLDRGA
KPHVLPLGRCQRSATILEPLLSDQWYVRIEPLARPAIEAVEQGRTRFIPEQWTNTYMAWMRNIHDWCISR
QLWWGHQIPAWYCPDGHVTVARETPEACSTCGKAELRQDEDVLDTWFSSGLWPFSTMGWPEQTDTLRTFY
PTSVMETGHDIIFFWVARMMMMGLHFMGEVPFRTVYLHPMVRDEKGQKMSKTKGNVIDPLVITEQYGADA
LRFTLAALTAQGRDIKLAKERIEGYRAFANKLWNASRFALMNLSGYQERGEDPARLARTPADRWILARLQ
RAVNETVEALEAFRFNDAANAVYAFVWHELCDWYIELAKEALASEDPEARRSVQAVLVHCLQTSYRLLHP
FMPFITEELWHVLRAQVGASAWADSVLAAEYPRKGEADEAAEAAFRPVLGIIDAVRNIRGEMGIPWKVKL
GAQAPVEIAVADPALRDLLQAGELARVHRVAGVEGSRLVVAAATAPAPQSAVGVGPGFEVRVPLAGVIDL
AAETARVDKEIGKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRARAEELREKRGKLEAHRAMLSGSEANS
ARRDTMEIQNEQKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQAATAVASGIEKVAEAVRKTVRR
SVKKAAATRAAMKKKVAKKAPAKKAAAKKAAAKKAAAKKKVAKKAPAKKVARKPAAKKAAKKPARKAAGR
KA
>gnl|CDD|237856 PRK14901, PRK14901, 16S rRNA methyltransferase B; Provisional
LNARQLAWEILQAVARGAYADVALERVLRKYPLSGADRALVTELVYGCIRRRRTLDAWIDQLGKKPAHKQ
PPDLRWLLHLGLYQLRYMDRIPASAAVNTTVELAKQNGLGGLAGVVNGILRQYLRAREAGDPLPLPEDPI
ERLAILHSFPDWLVKLWLEWLGLEEAEQLCKWFNQPPSLDLRINPLRTSLEEVQAALAEAGITATPIPGL
PQGLRLTGNPGSIRQLPGYEEGWWTVQDRSAQLVAPLLDPQPGEVILDACAAPGGKTTHIAELMGDQGEI
WAVDRSASRLKKLQENAQRLGLKSIKILAADSRNLLELKPQWRGYFDRILLDAPCSGLGTLHRHPDARWR
QTPEKIQELAPLQAELLESLAPLLKPGGTLVYATCTLHPAENEAQIEQFLARHPDWKLEPPKQKIWPHRQ
DGDGFFMAVLRKKS
>gnl|CDD|237857 PRK14902, PRK14902, 16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB
MKMNARELALEVLIKVENNGAYSNIALNKVLKKSELSDKDKALLTELVYGTIQRKLTLDYYLAPFIKKRK
KLDPWVRNLLRMSLYQLLYLDKVPDHAAVNEAVEIAKKRGHKGIAKFVNGVLRNILREGLPDIDEIKDPV
KRLSIKYSHPVWLVKRWIDQYGEEKAEKILESLNEPPKASIRVNTLKISVEELIEKLEEEGYEVEESLLS
PEALVIEKGNIAGTDLFKDGLITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVA
LDIHEHKLKLIEENAKRLGLTNIETKALDARKVHEKFAEKFDKILVDAPCSGLGVIRRKPDIKYNKTKED
IESLQEIQLEILESVAQYLKKGGILVYSTCTIEKEENEEVIEAFLEEHPEFELVPLQHEKPDELVYEVKD
GYLQILPNDYGTDGFFIAKLRKKG
>gnl|CDD|184896 PRK14903, PRK14903, 16S rRNA methyltransferase B; Provisional
MKTNVRLLAYRLLRKYEKEKFIFREDVDSVLSFLDDKDRRFFKELVWGVVRKEELLDWYINQLLKKKDIP
PAVRVALRMGAYQLLFMNSVPDYAAVSETVKLVKNENFKKLVNAVLRRLRTVPEPKELHLKYSHPKWLVN
YWRSFLPEEAVLRIMEWNQEPLPTMLRVNSLAITREEVIKILAEEGTEAVPGKHSPFSLIVRKLGVNMND
SRVIKDGLATVQGESSQIVPLLMELEPGLRVLDTCAAPGGKTTAIAELMKDQGKILAVDISREKIQLVEK
HAKRLKLSSIEIKIADAERLTEYVQDTFDRILVDAPCTSLGTARNHPEVLRRVNKEDFKKLSEIQLRIVS
QAWKLLEKGGILLYSTCTVTKEENTEVVKRFVYEQKDAEVIDIRDKLEEFEVEGIWDGYGFLMLPDETLT
PFYVSVLRKMG
>gnl|CDD|237858 PRK14904, PRK14904, 16S rRNA methyltransferase B; Provisional
MMTARELALQVLQELETGERKSDTLLHRMLERSSLERNDRALATELVNGVLRYRLQLDFIISRFYHHDLE
KAAPVLKNILRLGVYQLLFLDRVPRWAAVNECVKLARKYKGEHMAKLVNGVLRNISPETISLDEWLKGMP
EAERLSLLYSHPEWLLERWIARYGEERTEAMLSYNNQAPLFGFRINRLKTTPEKFLAAPADASVTFEKSG
LPNFFLSKDFSLFEPFLKLGLVSVQNPTQALACLLLNPQPGSTVLDLCAAPGGKSTFMAELMQNRGQITA
VDRYPQKLEKIRSHASALGITIIETIEGDARSFSPEEQPDAILLDAPCTGTGVLGRRAELRWKLTPEKLA
ELVGLQAELLDHAASLLKPGGVLVYATCSIEPEENELQIEAFLQRHPEFSAEPSPGSLPEPFHEVAHPKG
AILTLPGEHEGFDGGFAQRLRKNAG
>gnl|CDD|184898 PRK14905, PRK14905, triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; Provisional
MAKKIYFGTNLKMYKGNAETVDYLSELLAFAEKFKSDYDIELFVIPSYIALKDAVEAAASETGHPKIKIG
AQNMNAKDKGQFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLE
QKNYNISDEVLRTQLKIGLHGVSAEQLPHLFIAYEPVWAIGEGGIPASAEYADEKHAIIKQCLFELFAEE
SKKIPVLYGGSVNLENANELIMKPHIDGLFIGRSAWDAQCFHALIADALKALAGSKIDPIIHKFSEIAIQ
LIDHLGGKDNISALTHCASRIRVMLRNDGHIDKSAIEKIDCVKGLFSIANQYQIILGAGIVEKIHEEMKA
LLARE
>gnl|CDD|184899 PRK14906, PRK14906, DNA-directed RNA polymerase subunit beta'
MTEFDVTNFDALRISLASAEDIRSWSHGEVKKPETINYRTLKPEKDGLFCEKIFGPTKDWECACGKYKRI
RFKGIVCERCGVEVTRAKVRRERMGHIELAAPVSHIWYFKGSPSRLGYLLDIKPKDLEKVLYFASYIITS
VDKEAREEDADDLRDELAADLEELDAERDRLIEATRRLSVDYVPEDDEFVDDIGDDERLTAEEVRAEVAD
IYEEYNERKALRREAFDAFMQIEPKQLISDEALYREMRLNYSIYFKGGMGAEAVRDLLDAIDLEKEAEEL
RAIIANGKGQKREKAVKRLKVVDAFLKSGNDPADMILDVIPVIPPDLRPMVQLDGGRFATSDLNDLYRRV
INRNNRLKRLLDLGAPEIIVNNEKRMLQEAVDSLFDNGRRGRPVTGPGNRPLKSLADMLKGKQGRFRQNL
LGKRVDYSGRSVIVVGPHLKLHQCGLPSAMALELFKPFVMKRLVELEYAANIKAAKRAVDRGASYVWDVL
EEVIQDHPVLLNRAPTLHRLGIQAFEPVLVEGKAIKLHPLVCTAFNADFDGDQMAVHVPLSTQAQAEARV
LMLSSNNIKSPAHGRPLTVPTQDMIIGVYYLTTERDGFEGEGRTFADFDDALNAYDARADLDLQAKIVVR
LSRDMTVRGSYGDLEETKAGERIETTVGRIIFNQVLPEDYPYLNYKMVKKDIGRLVNDCCNRYSTAEVEP
ILDGIKKTGFHYATRAGLTVSVYDATIPDDKPEILAEADEKVAAIDEDYEDGFLSERERHKQVVDIWTEA
TEEVGEAMLAGFDEDNPIYMMADSGARGNIKQIRQLAGMRGLMADMKGEIIDLPIKANFREGLSVLEYFI
STHGARKGLVDTALRTADSGYLTRRLVDVAQDVIVREEDCGTDEGVTYPLVKPKGDVDTNLIGRCLLEDV
CDPNGEVLLSAGDYIESMDDLKRLVEAGVTKVQIRTLMTCHAEYGVCQKCYGWDLATRRPVNIGTAVGII
AAQSIGEPGTQLTMRTFHSGGVAGDDITQGLPRVAELFEARKPKGEAVLAEISGTLQITGDKTEKTLTIH
DQDGNSREYVVSARVQFMPGVEDGVEVRVGQQITRGSVNPHDLLRLTDPNTTLRYIVSQVQDVYVSQGVD
INDKHIEVIARQMLRKVAVTNPGDSDYLPGRQVNRYEFEDTANNLILEGKQPPVGQPLLLGITKASLATD
SWLSAASFQETTKVLTDAAIEGKVDHLAGLKENVIIGKPIPAGTGLSRYRDVGLTYHGQKVDGPTSKSLP
DWAPEELRDIEELLPQPQDWSLGDDYLGYGGVYSKNSYRGLRGRTLSDEDARLYLYDDLGVSQRWANKFS
EAGIETVGDLIGKTEEDLLRIEGIGAKAIEELKDGLEAHNLLYILEDDLEATSDDMSQLLDMVFSPDDTI
LIGGDAPATFNTDGEDMLGEALPPRSYNRDLGELDALLGQVGDLGASAEERSDAEDDDEE
>gnl|CDD|184900 PRK14907, rplD, 50S ribosomal protein L4; Provisional
MAETKKTTKKKTTEEKKPAAKKATTSKETAKTKKTAKTTSTKAAKKAAKVKKTKSVKTTTKKVTVKFEKT
ESVKKESVAKKTVKKEAVSAEVFEASNKLFKNTSKLPKKLFASEKIYSQAIFDTILSERASRRQGTHKVK
TRAEVSGTGKKPWRQKGTGRARAGSTRSPIFVGGGRAFGPTPERNYKLKVNKKVRFNAFVSALTLLANSK
AVLVDDFKLEKISTKDLIKKLTKLKINNLKHILIVSNDENIFKSARNLQNVIVVKPTSLSVELLIAADVL
VLSKESIENLEGRIK
>gnl|CDD|237859 PRK14908, PRK14908, glycine--tRNA ligase
SSQPLTMQDMLLALLRYWSEQGCIIHQGYDLEVGAGTFNPATFLRVLGPEPWRVAYVEPSRRPDDGRYGQ
NPNRLQTYTQFQVILKPVPGNPQELYLESLKAIGIDLRDHDIRFVHDDWENPTIGAWGLGWEVWLDGMEI
TQFTYFQQAGGKPLDPISGEITYGIERIAMYLQKVNHFKDIAWNDGLTYGEIFQQAEYEMSRYNFDDANT
EMWLKHFEDYAAEALRLLDAGLPVPAYDFVLKASHAFNILDARGAISVTERTRYIARIRQLARAVADLYV
EWREELGFPLLKVPPPPAAVTPKKTPDICGPETLLFEIGSEELPATFVPIGIQQLESALRELLADTRLGY
EKLEVLGTPRRLALLVEDVAPREPDAEREKRGPRLSAAFDADGTPTPAGEGFFRSQGVDISHLSALDQDG
AIEIREINGVEYLFLVRPEPGRDAAAILANELPELIQSLRFPKKMRWDDPGLSYARPIRWLVALYGDQIV
PISVGTLASGRTTRGHRQLDPPPVEIPSADGYVETLRQACVILSPKERREIIVQGLQNLAADVQIDAIAE
PRLIDEVTNLVEHPFVILGQFDEKFLELPKELLIAEMVKHQRYFPVRDAQGTLLNHFVIVADGSPDDEIV
RGNEKVLRARLTDGAFLFKADLKTPLETFVEKLKSVTYFEALGSLADKVERIKAHAEELAALLPLSARET
LDRAAELCKFDLVSQMVNEFPELQGIMGRYYAQRAGEPEAVAQALGEHELPRTAGDSLPASTTGALLSLA
DRLDNLLGCFALGLKPTSSSDPYALRRQALGVLTLLRATPASLDLEDLLARLARHFPSTTVWVKEAVLDE
VLEFVWGRLKTQLLDLGFDKDEIAAVLPDACKNPAEADKTAQALQELKSTEIFAEIAAALNRLKRILASL
SFSVTDASLLLEPAELNLKQALDAFREELTELPIDLKDYVAAAAELPQAVNTFFDEVLVMADDEAIRNAR
LGLLAAIRDLKFGVLDWDAL
>gnl|CDD|184902 PRK14938, PRK14938, Ser-tRNA(Thr) hydrolase; Provisional
MIILFIHASDFSFNVKEKAIKEPEEAKLKSIELKNVLVCFTTVEKGDDEEILNEAINDILDVYSKVKAAS
VVIYPYAHLSSNLANPDTAIKVLESLENLLKDKVKVYRAPFGWYKAFSISCYGHPLSELSRRIRKGEEYE
KSEELKYCEKFGFPTSPESAFMRRAVIEYLKNILQPIFESENNENVSNGEMSILYRNVEGRILPCINENP
RIIAVYGGVKELDFPKEFIDSKNRIKIWWVNESRTYVDVGLLVYYFLLESIRKQPPTLPDWLNPIQVRIL
PVKKDFLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRANNE
QKSMTVEELVKEIKRADELKERSNLPLYYSLYKHENR
>gnl|CDD|237860 PRK14939, gyrB, DNA gyrase subunit B; Provisional
SMMSNSYGASSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVYEVVDNAIDEALAGHCDDITVTIHADGS
VSVSDNGRGIPTDIHPEEGVSAAEVIMTVLHAGGKFDQNSYKVSGGLHGVGVSVVNALSEWLELTIRRDG
KIHEQEFEHGVPVAPLKVVGETDKTGTEVRFWPSPEIFENTEFDYDILAKRLRELAFLNSGVRIRLKDER
DGKEEEFHYEGGIKAFVEYLNRNKTPLHPNIFYFSGEKDGIGVEVALQWNDSYQENVLCFTNNIPQRDGG
THLAGFRAALTRTINNYIEKEGLAKKAKVSLTGDDAREGLTAVLSVKVPDPKFSSQTKDKLVSSEVRPAV
ESLVNEKLSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSE
LYLVEGDSAGGSAKQGRDRKFQAILPLKGKILNVEKARFDKMLSSQEIGTLITALGCGIGRDEFNPDKLR
YHKIIIMTDADVDGSHIRTLLLTFFYRQMPELIERGHLYIAQPPLYKVKKGKQEQYLKDDEALDDYLIEL
ALEGATLHLADGPAISGEALEKLVKEYRAVRKIIDRLERRYPRAVLEALIYAPALDLDDLADEAAVAALD
ADFLTSAEYRRLVELAEKLRGLIEEGAYLERGERKQPVSSFEEALDWLLAEARKGLSIQRYKGLGEMNPE
QLWETTMDPENRRLLQVTIEDAIAADEIFTTLMGDEVEPRREFIEENALNVANLDV
>gnl|CDD|184910 PRK14946, PRK14946, DNA polymerase III subunit beta; Provisional
MKFTIEKEIIEKQIERMQSAILNNGNSPLSGFFLKLTRSGLFIISTNSELSYKSFINKKDLIEINDVGSC
LIDGVFLKNIIKKSDNQISFELIGSELKVFWEDAQFSKTLRDSSFFPEINFEQKGIKLTVNAKNLKRAIK
NTAFATTNNPNQPILSAINLKSEDNFLHFSATDTIRFASEKIEISNPSRIDISISAKNLKDFIPPELDKD
IELFIESSKISYTYDNLTIQSRIFTIEYKDISNVLPKDSEILYSLTIEKKEILDLIDKATIITPGKDNVI
NFSLSKNELKGYISQYESGQSNVKTKNVLRFSGELAQVNVNYKYLKDAISVFDKVINIFINEKKTKMLIV
SPEKKEICQLVGLVLV
>gnl|CDD|237862 PRK14948, PRK14948, DNA polymerase III subunit gamma/tau
MAYEPLHHKYRPQRFDELVGQEAIATTLKNALISNRIAPAYLFTGPRGTGKTSSARILAKSLNCLNSDKP
TPEPCGKCELCRAIAAGNALDVIEIDAASNTGVDNIRELIERAQFAPVQARWKVYVIDECHMLSTAAFNA
LLKTLEEPPPRVVFVLATTDPQRVLPTIISRCQRFDFRRIPLEAMVQHLSEIAEKESIEIEPEALTLVAQ
RSQGGLRDAESLLDQLSLLPGPITPEAVWDLLGAVPEQDLLNLLKALASNDPESLLDSCRQLLDRGREPL
AILQGLAAFYRDLLLAKTAPNRPDLVAVSQQTWDELCKLAKQINLERILQWQQHLKGSEYQLKNSTQPRL
WLEVTLLGLLPSAFISEIANASAPANPTPAPNPSPPPAPIQPSAPKTKQAATTPSPPPAKASPPIPVPAE
PTEPSPTPPANAANAPPSLNLEELWQQILAKLELPSTRMLLSQQAELVSLDSNRAVIAVSPNWLGMVQSR
KPLLEQAFAKVLGRSIKLNLESQSGSASNTAKTPPPPQKSPPPPAPTPPLPQPTATAPPPTPPPPPPTAT
QASSNAPAQIPADSSPPPPIPEEPTPSPTKDSSPEEIDKAAKNLADFFNGEIIDLDEDFE
>gnl|CDD|237863 PRK14949, PRK14949, DNA polymerase III subunits gamma and tau; Provisional
MSYQVLARKWRPATFEQMVGQSHVLHALTNALTQQRLHHAYLFTGTRGVGKTSLARLFAKGLNCEQGVTA
TPCGVCSSCVEIAQGRFVDLIEVDAASRTKVDDTRELLDNVQYRPSRGRFKVYLIDEVHMLSRSSFNALL
KTLEEPPEHVKFLLATTDPQKLPVTVLSRCLQFNLKSLTQDEIGTQLNHILTQEQLPFEAEALTLLAKAA
NGSMRDALSLTDQAIAFGGGQVMLTQVQTMLGSIDEQHVIALLKALTDADIGVLMQTCAQVLAFGADAQE
VLRSLLELLHQITLTQFAPAAAQQSLYSEQIRAFAEQLSPEQVQLYYQILLTGRKDLPHAPDPKSGLEMA
LLRAVAFVPEKPVKRWQVDDPAEISLPEGQTPSALAAAVQAPHANEPQFVNAAPAEKKTALTEQTTAQQQ
VQAANAEAVAEADASAEPADTVEQALDDESELLAALNAEQAVILSQAQSQGFEASSSLDADNSAVPEQID
STAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAYQDDYVAFS
SESYNALSDDEQHSANVQSAQSAAEAQPSSQSLSPISAVTTAAASLADDDILDAVLAARDSLLSDLDALS
PKEGDGKKSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAALASGSAPAP
PPVPDPYDRPPWEEAPEVASANDGPNNAAEGNLSESVEDASNSELQAVEQQATHQPQVQAEAQSPASTTA
LTQTSSEVQDTELNLVLLSSGSITGHPLDLHWYKLMASLEVGGRVRQLAVNSVCQTQSNPLPLLLKPDQK
HLAADVAIVQLEQALSAALGNPRRVEVVIGVDPKRETPLELRKRFHQELLQQAHQSLITDDNVQWLIQRM
GAELDADSLVYPPELLNQRGQQIELLPESNFKAL
>gnl|CDD|237864 PRK14950, PRK14950, DNA polymerase III subunits gamma and tau; Provisional
MTVQVLYRKWRSQTFAELVGQEHVVQTLRNAIAEGRVAHAYLFTGPRGVGKTSTARILAKAVNCTTNDPK
GRPCGTCEMCRAIAEGSAVDVIEMDAASHTSVDDAREIIERVQFRPALARYKVYIIDEVHMLSTAAFNAL
LKTLEEPPPHAIFILATTEVHKVPATILSRCQRFDFHRHSVADMAAHLRKIAAAEGINLEPGALEAIARA
ATGSMRDAENLLQQLATTYGGEISLSQVQSLLGISGDEEVKALAEALLAKDLKAALRTLNAVAADGADLR
QFTRDLVEYLRQVMLLNSGADRSLLDLTADEKAALQKVSQIANLEALTKWVKAFSQLDFQLRTTSYGQLP
LELAVIEALLVPVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPP
VPHTPESAPKLTRAAIPVDEKPKYTPPAPPKEEEKALIADGDVLEQLEAIWKQILRDVPPRSPAVQALLS
SGVRPVSVEKNTLTLSFKSKFHKDKIEEPENRKITEELLSNFVGKTCAVRCTIEEKSEEPGDLREQIREA
RKDHLVKAAQNIFDAQIISVEEKNP
>gnl|CDD|237865 PRK14951, PRK14951, DNA polymerase III subunits gamma and tau; Provisional
MSYLVLARKYRPRSFSEMVGQEHVVQALTNALTQQRLHHAYLFTGTRGVGKTTVSRILAKSLNCQGPDGQ
GGITATPCGVCQACRDIDSGRFVDYTELDAASNRGVDEVQQLLEQAVYKPVQGRFKVFMIDEVHMLTNTA
FNAMLKTLEEPPEYLKFVLATTDPQKVPVTVLSRCLQFNLRPMAPETVLEHLTQVLAAENVPAEPQALRL
LARAARGSMRDALSLTDQAIAFGSGQLQEAAVRQMLGSVDRSHVFRLIDALAQGDGRTVVETADELRLNG
LSAASTLEEMAAVLQRMAVLQAVPQAAAAATDPEAAEVARLAALMPADETQLLYSICLHGRAELGLAPDE
YAALTMVLLRLLAFKPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAA
APPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTP
TEEGDVWHATVQQLAAAEAITALARELALQSELVARDGDQWLLRVERESLNQPGARERLRAALEAALGHA
VRLEVEVGAVTDSPARRNAAARAERQREAEEIIRNDPFVQQLMRDFGAKIVPGSIKPV
>gnl|CDD|237866 PRK14952, PRK14952, DNA polymerase III subunits gamma/tau
MALYRKYRPATFAEVVGQEHVTEPLSSALDAGRINHAYLFSGPRGCGKTSSARILARSLNCAQGPTATPC
GVCESCVALAPNGPGSIDVVELDAASHGGVDDTRELRDRAFYAPAQSRYRIFIVDEAHMVTTAGFNALLK
IVEEPPEHLIFIFATTEPEKVLPTIRSRTHHYPFRLLPPRTMRALIARICEQEGVVVDDAVYPLVIRAGG
GSPRDTLSVLDQLLAGAADTHVTYQRALGLLGATDVALIDDAVDALAADDAAALFGAIESVIDAGHDPRR
FATDLLERFRDLIVLQAVPDAAARGVVDAPEDVLERMREQAARIGLATLTRYAEVVQAGLGEMRGATAPR
LLLEVVCARLLLPSASDAESALLQRVERIETRLDMSIPANLLHNAPQAAPAPSAAAPEPKHQPAPEPRPV
LAPTPASGEPNAAAVRSMWSTVRDKVRQRSRTTEVMLAGATVRALEGNTLVLTHESAPLARRLSEQRNAD
VLAEALKDALGVNWRVRCETGKPAAAASPAGGGANAPPAKPVKPPPSCLSAQRDEEESMLAEAGRDDPST
PRRDPEEVALELLQNELGARRIDN
>gnl|CDD|237867 PRK14953, PRK14953, DNA polymerase III subunits gamma and tau; Provisional
MMYIPFARKYRPKFFKEVIGQEIVVRILKNAVKLQRVSHAYIFAGPRGTGKTTIARILAKVLNCLNPQEG
EPCGKCENCVEIDKGSFPDLIEIDAASNRGIDDIRALRDAVSYTPIKGKYKVYIIDEAHMLTKEAFNALL
KTLEEPPPRTIFILCTTEYDKIPPTILSRCQRFIFSKPTKEQIKEYLKRICNEEKIEYEEKALDLLAQAS
EGGMRDAASLLDQASTYGEGKVTIKVVEEFLGIVSQESVRKFLNLLLESDVDEAIKFLRTLEEKGYNLNK
FWKQLEEEIRNILLNKSLKNPEEVFQVEDFYRKLEKPLEALLYLEDVINKAFSEARTRDPLRAYELAILK
LLYVKDIVPISELLKEGSKQETKEQPEKKEEEKEELDIDKIILQIIKNEGKIISAILKNAEIKEEEGKIT
IKVEKSEEDTLDLEIKSIKKYFPFIEFEEVKKEKEKEKERPEFVEKVLELFKGSKIITYKKKKGKD
>gnl|CDD|184918 PRK14954, PRK14954, DNA polymerase III subunits gamma and tau; Provisional
MSYQVIARKYRPSKFADITAQEHITHTIQNSLRMDRVGHGYIFSGLRGVGKTTAARVFAKAVNCQRMIDD
PVYLQEVTEPCGECESCRDFDAGTSLNISEFDAASNNSVDDIRQLRENVRYGPQKGRYRVYIIDEVHMLS
TAAFNAFLKTLEEPPPHAIFIFATTELHKIPATIASRCQRFNFKRIPLDEIQSQLQMICRAEGIQIDADA
LQLIARKAQGSMRDAQSILDQVIAFSVGSEAEKVIAYQGVAELLNYIDDEQFFDVTDAIAENDAVKMLEV
ARFVIDNGYDEQDFLEKLIEHFRNFLVLYNLRSTRLIERPESVKERYQQSAGGLTPAAVMQMTDFLMKTQ
GELKFQFEYQFRFELALLRLIELVRNDGGVAPSPAGSPDVKKKAPEPDLPQPDRHPGPAKPEAPGARPAE
LPSPASAPTPEQQPPVARSAPLPPSPQASAPRNVASGKPGVDLGSWQGKFMNFTRNGSRKQPVQASSSDA
AQTGVFEGVAELEKLRMEWNQFLEHLLKKGQKVLVTHLRSCELTSCSPHGVVVMTCCRKFSYEELMQDAA
LLSKEIESFYGIPLKLQIRYDAARDACTREKSIFTLFRELSETNDVVKYLIKEFGGELVY
>gnl|CDD|184919 PRK14955, PRK14955, DNA polymerase III subunits gamma and tau; Provisional
MSYQVIARKYRPKKFADITAQEHITRTIQNSLRMGRVGHGYIFSGLRGVGKTTAARVFAKAVNCQRMIDD
ADYLQEVTEPCGECESCRDFDAGTSLNISEFDAASNNSVDDIRLLRENVRYGPQKGRYRVYIIDEVHMLS
IAAFNAFLKTLEEPPPHAIFIFATTELHKIPATIASRCQRFNFKRIPLEEIQQQLQGICEAEGISVDADA
LQLIGRKAQGSMRDAQSILDQVIAFSVESEGEGSIRYDKVAELLNYIDDEHFFAVTDAVADGDAVAMLDV
AQFVIRNGYDEQDFLEKLIEHLRNFLVVHNLRSTRLVERPDAVRERYERDAAKFSPEVIMQMTDLLLQTQ
KELKFQFEYQFRFELALLKLIEIGHPAPTAAAAPTGGAQKKKPLLSL
>gnl|CDD|184920 PRK14956, PRK14956, DNA polymerase III subunits gamma and tau; Provisional
MSGTHEVLSRKYRPQFFRDVIHQDLAIGALQNALKSGKIGHAYIFFGPRGVGKTTIARILAKRLNCENPI
GNEPCNECTSCLEITKGISSDVLEIDAASNRGIENIRELRDNVKFAPMGGKYKVYIIDEVHMLTDQSFNA
LLKTLEEPPAHIVFILATTEFHKIPETILSRCQDFIFKKVPLSVLQDYSEKLCKIENVQYDQEGLFWIAK
KGDGSVRDMLSFMEQAIVFTDSKLTGVKIRKMIGYHGIEFLTSFIKSLIDPDNHSKSLEILESLYQEGQD
IYKFLWDSIEFTHTLNLIRDSLADRESVNFPKEDLQKMKSDFENVDSSKLNFLSGKLFEIYEKIKTIRLR
NSFEIKVFTEIQIKKLVEELTYPSLAGLLDKINHLILMVQGSKNIPEDVEPVKKISTPPPLQQEASKKKD
PTTSDQKLNSQFESNQQDSNLDNNPLPSKSESQSEPPSSKFDTSTEIKKKFLGTEVDPNQFPKL
>gnl|CDD|184921 PRK14957, PRK14957, DNA polymerase III subunits gamma and tau; Provisional
MSYQALARKYRPQSFAEVAGQQHALNSLVHALETQKVHHAYLFTGTRGVGKTTLGRLLAKCLNCKTGVTA
EPCNKCENCVAINNNSFIDLIEIDAASRTGVEETKEILDNIQYMPSQGRYKVYLIDEVHMLSKQSFNALL
KTLEEPPEYVKFILATTDYHKIPVTILSRCIQLHLKHISQADIKDQLKIILAKENINSDEQSLEYIAYHA
KGSLRDALSLLDQAISFCGGELKQAQIKQMLGIIDSEEVYSIINAIIDNDPKAILPAIKNLALTESSADA
VLDRIAEIWFACCIYSFTQSLDAVNDIDVDIINNILAKISIEQAHFLYQLTITAKKDIALAPNFETGVTM
AILRLIAFQKKNLIDKTQTSKSNISPIVSKNDINLLKNTFKSEQPKQTVKAVVAQNNDSTASENTQEQSL
DKKWFNLLNRIKLKGFTKTLAFNSHLISDNSETFVIHLNEDAKKILELDPQSIAKLQASISEYLNNPSFR
LDIKNLAMDKVSTDQKSPAEIKRENAISKIHNDENTKLIKQALAIDIKDQNIILTD
>gnl|CDD|184922 PRK14958, PRK14958, DNA polymerase III subunits gamma and tau; Provisional
MAHQVLARKWRPRCFQEVIGQAPVVRALSNALDQQYLHHAYLFTGTRGVGKTTISRILAKCLNCEKGVSA
NPCNDCENCREIDEGRFPDLFEVDAASRTKVEDTRELLDNIPYAPTKGRFKVYLIDEVHMLSGHSFNALL
KTLEEPPSHVKFILATTDHHKLPVTVLSRCLQFHLAQLPPLQIAAHCQHLLKEENVEFENAALDLLARAA
NGSVRDALSLLDQSIAYGNGKVLIADVKTMLGTIEPLLLFDILEALAAKAGDRLLGCVTRLVEQGVDFSN
ALADLLSLLHQIAIIQTVPEALIENDSEQLRQLAKLLDREDVQLFYQIGLIGQRDLAYSPTPQTGFEMTL
LRMLAFYPSAANAIPETESKEAVVTPTPKSSETSWPQLLSQLKLTGATLALAQQCSLKELTDNRLYLMLN
PKQKPLLQQKHIERISEALSEHFNRTITVKIDISNHQTETPAALAQKKAQDRQTEAEKRMMNDRQVQRIM
QTFDATLVKESIVPHDEGA
>gnl|CDD|184923 PRK14959, PRK14959, DNA polymerase III subunits gamma and tau; Provisional
MSHASLTARYRPQTFAEVAGQETVKAILSRAAQENRVAPAYLFSGTRGVGKTTIARIFAKALNCETAPTG
EPCNTCEQCRKVTQGMHVDVVEIDGASNRGIDDAKRLKEAIGYAPMEGRYKVFIIDEAHMLTREAFNALL
KTLEEPPARVTFVLATTEPHKFPVTIVSRCQHFTFTRLSEAGLEAHLTKVLGREGVDYDPAAVRLIARRA
AGSVRDSMSLLGQVLALGESRLTIDGARGVLGLAGQELFLRLMEALAAQDCLGVANVVRELLDRGVDMGF
FLRELVATWRNLFMLRQAGEAALASLDLPEDEARQWLGWAKRFEPAHIHACWQMTLEGQRRVLTSLEPAM
ALELLLLNLAMLPRLMPVESLRPSGGGASAPSGSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAA
PATPAPSAAPSPRVPWDDAPPAPPRSGIPPRPAPRMPEASPVPGAPDSVASASDAPPTLGDPSDTAEHTP
SGPRTWDGFLEFCQGRNGQGGRLATVLRQATPEHADGRLRLATMSSVQYERLTDAATETTLAGLVRDYFG
DACRVEVLPPTRVRRTEAELRKEAEAHPAVQLLKEEMGACILKCTPLADLRRPEDTTEQGDNKP
>gnl|CDD|237868 PRK14960, PRK14960, DNA polymerase III subunit gamma/tau
MYQVLARKYRPRNFNELVGQNHVSRALSSALERGRLHHAYLFTGTRGVGKTTIARILAKCLNCETGVTST
PCEVCATCKAVNEGRFIDLIEIDAASRTKVEDTRELLDNVPYAPTQGRFKVYLIDEVHMLSTHSFNALLK
TLEEPPEHVKFLFATTDPQKLPITVISRCLQFTLRPLAVDEITKHLGAILEKEQIAADQDAIWQIAESAQ
GSLRDALSLTDQAIAYGQGAVHHQDVKEMLGLIDRTIIYDLILAVHQNQREKVSQLLLQFRYQALDVSLV
LDQLISTLHELALLQYLPELGLKYSEEINAKILQLSKLISAQDLQLYYQIACKGRSDLQLAVTQEQGFEM
CVLRLLAFRPLAPNEILVSEPVQQNGQAEVGLNSQAQTAQEITPVSAVQPVEVISQPAMVEPEPEPEPEP
EPEPEPEPEPEPEPEPEPEPEPQPNQDLMVFDPNHHELIGLESAVVQETVSVLEEDFIPVPEQKLVQVQA
ETQVKQIEPEPASTAEPIGLFEASSAEFSLAQDTSAYDLVSEPVIEQQSLVQAEIVETVAVVKEPNATDN
SQLMPQDILKLPSQTLEGEWTLEKWEFWFRNSQLSPAVQELAQHGVMTGEIGGNTVFHIPQEYENMLTQL
QQALIEALKQQWPNTQFTVEYGAVNTATPYVMQSVRKEKAFHRATELLQQQPVIKSLIETFDGELQNIQL
KP
>gnl|CDD|184925 PRK14961, PRK14961, DNA polymerase III subunits gamma and tau; Provisional
MNYQILARKWRPQYFRDIIGQKHIVTAISNGLSLGRIHHAWLLSGTRGVGKTTIARLLAKSLNCQNGITS
NPCRKCIICKEIEKGLCLDLIEIDAASRTKVEEMREILDNIYYSPSKSRFKVYLIDEVHMLSRHSFNALL
KTLEEPPQHIKFILATTDVEKIPKTILSRCLQFKLKIISEEKIFNFLKYILIKESIDTDEYALKLIAYHA
HGSMRDALNLLEHAINLGKGNINIKNVTDMLGLLNEKQSFLLTDALLKKDSKKTMLLLNKISSIGIEWEN
ILIEMLRFLHHISMSQSFPKIWNTIFIKNYKNQIQKIAQNNKKTNIQLCYQILLNGRKELKFAPDQKIGV
EMTLLRAINAITK
>gnl|CDD|237869 PRK14962, PRK14962, DNA polymerase III subunits gamma and tau; Provisional
MEALYRKYRPKTFSEVVGQDHVKKLIINALKKNSISHAYIFAGPRGTGKTTVARILAKSLNCENRKGVEP
CNECRACRSIDEGTFMDVIELDAASNRGIDEIRKIRDAVGYRPMEGKYKVYIIDEVHMLTKEAFNALLKT
LEEPPSHVVFVLATTNLEKVPPTIISRCQVIEFRNISDELIIKRLQEVAEAEGIEIDREALSFIAKRASG
GLRDALTMLEQVWKFSEGKITLETVHEALGLIPIEVVRDYINAIFNGDVKRVFTVLDDVYYSGKDYEVLI
QQAIEDLVEDLERERANDIIQVSRQLLNILREIKFAEEKRLVCKLGSASIATRFSSPNVQENDVEEKNDN
SNVQQKEKKKEESKAKEEKQEDIEFEKRFKELMEELKEKGDLSIFVALSLSEVEEDGDKVKISFDSSKAM
HYELMKEKLPELENLFSRKLGKNVEVELRLMGKEETEDKVLQKLKRLFEQEG
>gnl|CDD|184927 PRK14963, PRK14963, DNA polymerase III subunits gamma and tau; Provisional
MSALYQRARPITFDEVVGQEHVKEVLLAALRQGRLGHAYLFSGPRGVGKTTTARLIAMAVNCSGEDPKPC
GECESCLAVRRGAHPDVLEIDAASNNSVEDVRDLREKVLLAPLRGGRKVYILDEAHMMSKSAFNALLKTL
EEPPEHVIFILATTEPEKMPPTILSRTQHFRFRRLTEEEIAGKLRRLLEAEGREAEPEALQLVARLADGA
MRDAESLLERLLALGTPVTRKQVEEALGLPPQERLRGIAAALAQGDAAEALSGAAQLYRDGFAARTLVEG
LLEAFRAALYAELGLGGGPRLEGAEPRLLAAMTALDEQMERFARRSDALSLELALLHALLALGGAPSEGV
AAVAPPAPAPADLTQRLNRLEKEVRSLRSAPTAAATAAGAPLPDFDPRPRGPPAPEPARSAEAPPLVAPA
AAPAGLALRWRDVLAALKMQLRAFLREARPHVEEGYVSLTFPERASFHYKQAQKKLAELAALVREVFGPE
TVELILPEGGRKKK
>gnl|CDD|237870 PRK14964, PRK14964, DNA polymerase III subunits gamma and tau; Provisional
MNLALKYRPSSFKDLVGQDVLVRILRNAFTLNKIPQSILLVGASGVGKTTCARIISLCLNCSNGPTSDPC
GTCHNCISIKNSNHPDVIEIDAASNTSVDDIKVILENSCYLPISSKFKVYIIDEVHMLSNSAFNALLKTL
EEPAPHVKFILATTEVKKIPVTIISRCQRFDLQKIPTDKLVEHLVDIAKKENIEHDEESLKLIAENSSGS
MRNALFLLEQAAIYSNNKISEKSVRDLLGCVDKHILEDLVEAILLGDAQSALNVFRELCNTSNPVIILEG
MLQIIYEICYFSITKEIDFLLGEDLITRIKSLKIGSTIFLSRLWQMLLKGIQEVKSSTCVKQAAEMMIIR
LCYLSDLPSPQQIIKKILSKSVEQAPRQIKVNNKQQNYDFDKLLQLLKSNNMIDLYNQLCSSLQEIDCKS
DYTLNIKANSQLDSNFCNDLKNFLNQLTNKKWNICIDKNSNLVYNPELDEAVKDILQEFDGAKVVNIENI
K
>gnl|CDD|237871 PRK14965, PRK14965, DNA polymerase III subunits gamma and tau; Provisional
MSYLVLARKYRPQTFSDLTGQEHVSRTLQNAIDTGRVAHAFLFTGARGVGKTSTARILAKALNCEQGLTA
EPCNVCPPCVEITEGRSVDVFEIDGASNTGVDDIRELRENVKYLPSRSRYKIFIIDEVHMLSTNAFNALL
KTLEEPPPHVKFIFATTEPHKVPITILSRCQRFDFRRIPLQKIVDRLRYIADQEGISISDAALALVARKG
DGSMRDSLSTLDQVLAFCGDAVGDDDVAELLGVVDRRLLLDISAAVFGRDTRALLEIVERVDEFGYNMRQ
FCQELIDHLRNLVVLRAVGEPGDLLDLSEAELAELRAQAAAADAADLQRHLTLLLRAEGEMAHASFPRLV
LEMALLKMATLAPGAPVSELLDRLEALERGAPAPPSAAWGAPTPAAPAAPPPAAAPPVPPAAPARPAAAR
PAPAPAPPAAAAPPARSADPAAAASAGDRWRAFVAFVKGKKPALGASLEQGSPLGVSAGLLEIGFPEGSF
ELSAMQDPDSRAELKALAEQFFGRPTRLRITVLAAPPGAAPPSLAEKKAAEREQRQARLREEAREHPLVQ
EALRVFGGEIDEVEEL
>gnl|CDD|184930 PRK14966, PRK14966, unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional
MQEQNRKPSFPIVMLLVSVALWIASLSNVAFYLGNHGSMEGLTVLILGSIFASLDIRYCAVYANYVWLAA
IVLLALRKKVVPVHAALWGLALVAFSVKAVYVDEAGNTSDIVRYGAGFYLWYAAFAVATIGTFAGKNKER
KAASAADGIKMTFDEWLGLSKLPKNEARMLLQYASEYTRVQLLTRGGEEMPDEVRQRADRLAQRRLNGEP
VAYILGVREFYGRRFAVNPNVLIPRPETEHLVEAVLARLPENGRVWDLGTGSGAVAVTVALERPDAFVRA
SDISPPALETARKNAADLGARVEFAHGSWFDTDMPSEGKWDIIVSNPPYIENGDKHLLQGDLRFEPQIAL
TDFSDGLSCIRTLAQGAPDRLAEGGFLLLEHGFDQGAAVRGVLAENGFSGVETLPDLAGLDRVTLGKYMK
HLK
>gnl|CDD|184931 PRK14967, PRK14967, putative methyltransferase; Provisional
AATTPPDALLRAPGVYRPQEDTQLLADALAAEGLGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRR
AVRSARLNALLAGVDVDVRRGDWARAVEFRPFDVVVSNPPYVPAPPDAPPSRGPARAWDAGPDGRAVLDR
LCDAAPALLAPGGSLLLVQSELSGVERTLTRLSEAGLDAEVVASQWIPFGPVLRARAAWLERRGLLPPGQ
REEELVVIRADKP
>gnl|CDD|237872 PRK14968, PRK14968, putative methyltransferase; Provisional
LNDEVYEPAEDSFLLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNI
RNNGVEVIRSDLFEPFRGDKFDVILFNPPYLPTEEEEEWDDWLNYALSGGKDGREVIDRFLDEVGRYLKP
GGRILLLQSSLTGEDEVLEYLEKLGFEAEVVAEEKFPFEELIVLELVK
>gnl|CDD|237873 PRK14969, PRK14969, DNA polymerase III subunits gamma and tau; Provisional
MSYQVLARKWRPKSFSELVGQEHVVRALTNALEQQRLHHAYLFTGTRGVGKTTLARILAKSLNCETGVTA
TPCGVCSACLEIDSGRFVDLIEVDAASNTQVDAMRELLDNAQYAPTRGRFKVYIIDEVHMLSKSAFNAML
KTLEEPPEHVKFILATTDPQKIPVTVLSRCLQFNLKQMPPPLIVSHLQHILEQENIPFDATALQLLARAA
AGSMRDALSLLDQAIAYGGGTVNESEVRAMLGAIDQDYLFALLEALLAQDGAALLAIADAMEERSLSFDA
ALQDLAALLHRLAIAQTVPDSIADDLPERDRLLDLAKRLSPEDIQLYYQIALHGRRDLGLAPDEYAGFTM
TLLRMLAFRPSEQDSGAGRAPGAVPGVNRTRAVPTAAPAAPAAATPSDRQSFNGNWRALVDQLKLSGLAR
ELAQNCELKSFSEDRIELRVPEAHKHLLDKPYQDKLQAALEQHFGRPVQLIFSLGGVSGNTPAELVSREK
AERQSQAESAIESDGFVQELIEDFDATLIPSSIKPIQ
>gnl|CDD|184934 PRK14970, PRK14970, DNA polymerase III subunits gamma and tau; Provisional
MENFVVSARKYRPQTFDDVVGQSHITNTLLNAIENNHLAQALLFCGPRGVGKTTCARILARKINQPGYDD
PNEDFSFNIFELDAASNNSVDDIRNLIDQVRIPPQTGKYKIYIIDEVHMLSSAAFNAFLKTLEEPPAHAI
FILATTEKHKIIPTILSRCQIFDFKRITIKDIKEHLAGIAVKEGIKFEDDALHIIAQKADGALRDALSIF
DRVVTFCGKNITRQAVTENLNILDYDTYINVTDLILENKIPELLLAFNEILRKGFDGHHFIAGLASHFRD
LMVSKTPATIALLEVGEQAKKRYEVQSQKVSQSFLLSGIDIANDCDLKYKLSKNQRLLVELALMQLASIN
FDGISAKKKLSDLKKKV
>gnl|CDD|237874 PRK14971, PRK14971, DNA polymerase III subunit gamma/tau
MENYIVSARKYRPSTFESVVGQEALTTTLKNAIATNKLAHAYLFCGPRGVGKTTCARIFAKTINCQNLTA
DGEACNECESCVAFNEQRSYNIHELDAASNNSVDDIRNLIEQVRIPPQIGKYKIYIIDEVHMLSQAAFNA
FLKTLEEPPSYAIFILATTEKHKILPTILSRCQIFDFNRIQVADIVNHLQYVASKEGITAEPEALNVIAQ
KADGGMRDALSIFDQVVSFTGGNITYKSVIENLNILDYDYYFRLTDALLAGKVSDSLLLFDEILNKGFDG
SHFITGLASHFRDLLVCKDAATLQLLEVGESIRQRYLEQAQKCPMSFLYRALKLCNQCDLNYRASKNKRL
LVELTLIQLAQLTQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQP
AGTPPTVSVDPPAAVPVNPPSTAPQAVRPAQFKEEKKIPVSKVSSLGPSTLRPIQEKAEQATGNIKEAPT
GTQKEIFTEEDLQYYWQEFAGTRPQEEKALKETMINCRPKLLNGTTFEVAVDNELQEKELTNLIPDLLGF
LRGRLKNSKITMTVRVSEPTEVNRAYSSVEKFQYLAQKNPALLELREELGLELD
>gnl|CDD|184936 PRK14973, PRK14973, DNA topoisomerase I; Provisional
MHLIIAEKNIAANRIAQILAGKTKVQVKKDGGVSTYSFDDTVVVGLRGHVVEVDFEPGYTNWRSEEHTPR
SLIDADTIKKPTEKKIVGLIQKLAKKADRVTIATDFDTEGELIGKEAYELVRAVNPKVPIDRARFSAITK
EEIVTAFAEPTDLDFALAAAGEARQIIDLIWGASLTRFISLAAHRGGDNILSVGRVQSPTLAMIVDREKE
IEAFVPEKYWMLSLATEKDGEGIEARHTHGRFTDSAAAEAAYDATKEPLVVTEVKEGHKVDRAPTPFDTT
TFIVAASRLGFSAANAMRIAEDLYMNGYISYPRTDNTIYPKSLDLNGVLATLAKGAFSKDVAWVKDNRRP
VPTRGKKSSTDHPPIHPTGVATREELGDDRWKLYELVVRRFLATLSPDAEWATMKVNFDAGGEPYTATGG
RLLEAGWRTVYPYSEAKENILPAFALGEKLPILAVNLEEKETQPPARYSQSRLIQRMEELGLGTKSTRHE
VIGKLVSRKYIEGNPLRPTLVGRAVTESLEEHAGTITEPDMTQTLEEHMQQIKERKRTRDDVVTESRKML
HRAFDELEANEAVIGRDIMERTAEELTIGPCPVCGKDLRIKHIGSSQFIGCSGYPDCTFNIGLPGTTWGW
AIRTDEVCPIHHLNHVRLIRKGARPWDIGCPLCSHIESNTESLLLMPSMTEELLQKLNAVHIYTVSELAS
REPEALAKSLGLSKKEAEKLIREAGDVLELLRRRSELRKFVRKHVPPRRGRSHAKIMKALISSGINDIAA
LARADPADLKKAGLSEAEAASLLAEAKSLCNISRLKEIGVPAVSLKKYQEAGFDTPEDFCSVHPAYLALK
TGISPETICRHAKLVCEKLGRPVPEKISKAAFERGRAELLSVPGLGETTLEKLYLAGVYDGDLLVSADPK
KLAKVTGIDEKKLRNLQAYAKKVLEK
>gnl|CDD|237875 PRK14974, PRK14974, signal recognition particle-docking protein FtsY
MFDKLKEKLSKFVEKVEEKIEEEEEEEAPEAEEEEEEEDEEEKKEKPGFFDKAKITEIKEKDIEDLLEEL
ELELLESDVALEVAEEILESLKEKLVGKKVKRGEDVEEIVKNALKEALLEVLSVGDLFDLIEEIKSKGKP
VVIVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAV
AYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKKIVRVTKPDLVIFVGDALAGNDAVEQAREFNEAVG
IDGVILTKVDADAKGGAALSIAYVIGKPILFLGVGQGYDDLIPFDPDWFVDKLLGE
>gnl|CDD|237876 PRK14975, PRK14975, bifunctional 3'-5' exonuclease/DNA polymerase; Provisional
MDMKVILAPEELGAALERLSPAGVVAGDTETTGDDAAAAAAQEGEEEPRWVWASTAALYPRLLAAGVRVE
RCHDLMLASQLLLGSEGRAGSSLSAAAARALGEGLDKPPQTSALSDPPDEEQLLYAAADADVLLELYAVL
ADQLNRIAAAAHPGRLRLLAAAESAGALAAAEMELAGLPWDTDVHEALLAELLGPRPAAGGRPARLAELA
AEIREALGRPRLNPDSPQQVLRALRRAGIELPSTRKWELREIDHPAVEPLLEYRKLSKLLSANGWAWLDY
WVRDGRFHPEYVPGGVVTGRWASRGPNAQQIPRDIRSAFVADPGWKLVVADASQIELRVLAAYSGDERMI
EAFRTGGDLHRLTASVGFGKPEEEKEERALAKAANFGAIYGATSKGLQEYAKNYGEAARLLERLRRAYPR
AVGWVERAAREGERGGVVRTLLGRTSPPPGFAWRARRRARSRGRFTRNFPVQGTAADWAKLALALLRRRL
AEGLDAELVFFVHDEVVVECPEEEAEEVAAAIEEAMEEAGRLLFGPVPFPVEVAVVESYAEAK
>gnl|CDD|237877 PRK14976, PRK14976, 5'-3' exonuclease; Provisional
MMKKALLIDGNSLIFRSYYATLKQGPKLKNNKGLPTNAIHTFLTMIFKILKKLNPSYILIAFDAGRKTFR
HQLYDEYKQGRKKTPESLISQIPLLKKILKLAGIKWEEQPGYEADDLIGSLAKKLSKQNITVLIYSSDKD
LLQLVNENTDVLLKKKGTSHFILNTNNFFELYGIEPKQIIDYKGLVGDSSDNIKGVKGIGPKTAIKLLNK
YGNIENIYENIDKIKKKIKNKLSEAKEKALLSKKLATIKTDVPLDFQIEDIKLKKLDQPELKKIFEELEL
K
>gnl|CDD|184940 PRK14977, PRK14977, bifunctional DNA-directed RNA polymerase A'/A'' subunit; Provisional
EEILAVKAIDGIIFGLISPADARKIGFAEITAPEAYDEDGLPVQGGLLDGRLGTIEPGQKCLTCGNLAAN
CPGHFGHIELAEPVIHIAFIDNIKDLLNSTCHKCAKLKLPQEDLNVFKLIEEAHAAARDIPEKRIDDEII
EEVRDQVKVYAKKAKECPHCGAPQHELEFEEPTIFIEKTEIEEHRLLPIEIRDIFEKIIDDDLELIGFDP
KKARPEWAVLQAFLVPPLTARPSIILETGERSEDDLTHILVDIIKANQKLKESKDAGAPPLIVEDEVDHL
QYHTSTFFDNATAGIPQAHHKGSGRPLKSLFQRLKGKEGRFRGNLIGKRVDFSARTVISPDPMIDIDEVG
VPEAIAMKLTIPEIVNENNIEKMKELVINGPDEFPGANAIRKGDGTKIRLDFLEDKGKDALREAAEQLEI
GDIVERHLADGDIVIFNRQPSLHKLSILAHRVKVLPGATFRLHPAVCPPYNADFDGDEMNLHVPQIEDAR
AEAIELMGVKDNLISPRTGGPIIGALQDFITAAYLITKDDALFDKNEASNIAMLAGITDPLPEPAIKTKD
GPAWTGKQLFSLFLPKDFNFEGIAKWSAGKAGEAKDPSCLGDGYVLIKEGELISGVIDDNIIGALVEEPE
SLIDRIAKDYGEAVAIEFLNKILIIAKKEILHYGFSNGPGDLIIPDEAKQEIEDDIQGMKDEVSDLIDQR
KITRKITIYKGKEELLRGMKEEEALEADIVNELDKARDKAGSSANDCIDADNAGKIMAKTGARGSMANLA
QIAGALGQQKRKTRIGFVLTGGRLHEGYKDRALSHFQEGDDNPDAHGFVKNNYREGLNAAEFFFHAMGGR
EGLIDKARRTEDSGYFQRRLANALEDIRLEYDETVRDPHGHIIQFKFGEDGIDPQKLDHGEAFNLERIIE
KQKIEDRGKGASKDEIEELAKEYTKTFNANLPKLLADAIHGAELKEDELEAICAEGKEGFEKAKVEPGQA
IGIISAQSIAEPGTQMTLRTFHAAGIKAMDVTHGLERFIELVDARAKPSTPTMDIYLDDECKEDIEKAIE
IARNLKELKVRALIADSAIDNANEIKLIKPDKRALENGCIPMERFAEIEAALAKGKKFEMELEDDLIILD
LVEAADRDKPLATLIAIRNKILDKPVKGVPDIERAWVELVEKDGRDEWIIQTSGSNLAAVLEMKCIDIAN
TITNDCFEIAGTLGIEAARNAIFNELASILEDQGLEVDNRYIMLVADIMCSRGTIEAIGLQAAGVRHGFA
GEKDSPLAKAAFEITTHTIAHAALGGEIEKIKGILDALIMGQNIPIGSGKVDLLMDFSGKA
>gnl|CDD|237878 PRK14979, PRK14979, DNA-directed RNA polymerase subunit D; Provisional
MITIKEKEKTRIGEEFKFSLKAPISFSSALRRIMISEVPTYAIENVYFYENSSSMYDEILAHRLGLIPIK
GKPVSGDEVITFTLSKEGPCTVYSSDLKSENGEVAFKNIPIVKLAEGQKLEIECEALVGTGKIHAKWQPC
NAVYKQISNDEVEFKVESFGQMDAEDILRSALEILKNKAEKFLQELEGIELSDEN
>gnl|CDD|184942 PRK14980, PRK14980, DNA-directed RNA polymerase subunit G; Provisional
MMESKAQEIILSCKINSIEKGSLKNLSIIHMSCNDFNISFDIIDSINIFSQKEKVKAIISKERPSYTNDD
FCAHGYIVTESSNNGNRYTTIISLFGLLVKIISKESFLKTHQLNVMDHVYFCVKKNT
>gnl|CDD|184943 PRK14981, PRK14981, RNA polymerase Rpb4 family protein
MIGKKILEEEYITIAEAKEILSEIEEERELSYELRRTLDYLNRFSKLDPEDAEELVEELLELEKMKEKTA
VKIADILPETRDELRAIFAKERYTLSPEELDEILDIVKKYRE
>gnl|CDD|237880 PRK14984, PRK14984, gluconate transporter
MPLVIVAIGVALLLLLMIRFKMNGFIALVLVALAVGLMQGMPLDKVIGSIKAGVGGTLGSLALIMGFGAM
LGKMLADCGGAQRIATTLIAKFGKKHIQWAVVLTGFTVGFALFYEVGFVLMLPLVFTIAASANIPLLYVG
VPMAAALSVTHGFLPPHPGPTAIATIFNADMGKTLLYGTILAIPTVILAGPVYARFLKGIDKPIPEGLYS
AKTFTEEEMPSFGVSVWTSLVPVILMAMRAIAEMILPKGHAFLPVAEFLGDPVMATLIAVLIAMFTFGLN
RGRSMDQINDTLVSSIKIIAMMLLIIGGGGAFKQVLVDSGVDKYIASMMHETNISPLLMAWSIAAVLRIA
LGSATVAAITAGGIAAPLIATTGVSPELMVIAVGSGSVIFSHVNDPGFWLFKEYFNLTIGETIKSWSMLE
TIISVCGLVGCLLLNMVI
>gnl|CDD|237881 PRK14985, PRK14985, maltodextrin phosphorylase; Provisional
SQPIFNKKQFQAALTRQWQRFGLNSAAEMTPRQWWQAVSAALAELLRAQPAAKPVANQRHVNYISMEFLI
GRLTGNNLLNLGWYDDVQDVLKAYDINLTDLLEEETDPALGNGGLGRLAACFLDSMATVGQPATGYGLNY
QYGLFRQSFVDGKQVEAPDDWHRDSYPWFRHNEALDVQVGIGGKVTKQDGRERWEPAFTITGEAWDLPVV
GYRNGVAQPLRLWQATHAHPFDLTKFNDGDFLRAEQQGIDAEKLTKVLYPNDNHTAGKKLRLMQQYFQCA
CSVADILRRHHLAGRKLHELPDYEVIQLNDTHPTIAIPELLRVLLDEHQLSWDDAWAITSKTFAYTNHTL
MPEALECWDEKLVKSLLPRHMQIIKEINTRFKTLVEKTWPGDKKVWAKLAVVHDKQVRMANLCVVSGFAV
NGVAALHSDLVVKDLFPEYHQLWPNKFHNVTNGITPRRWIKQCNPALAALLDKTLKKEWANDLDQLINLE
KYADDAAFRQQYREIKQANKVRLAEFVKQRTGIEINPQAIFDVQIKRLHEYKRQHLNLLHILALYKEIRE
NPQADRVPRVFLFGAKAAPGYYLAKNIIFAINKVAEVINNDPLVGDKLKVVFLPDYCVSAAELLIPAADI
SEQISTAGKEASGTGNMKLALNGALTVGTLDGANVEIAEQVGEENIFIFGHTVEQVKALLAKGYDPVKWR
KKDKVLDAVLKELESGKYSDGDKHAFDQMLHSLKQGGDPYLVLADFAAYVEAQKQVDALYRDQEAWTRAA
ILNTARCGMFSSDRSIRDYQARIWQAKR
>gnl|CDD|184948 PRK14986, PRK14986, glycogen phosphorylase; Provisional
MNAPFTYASPTLSVEALKHSIAYKLMFTIGKDPVIANKHEWLNATLFAVRDRLVERWLRSNRAQLSQETR
QVYYLSMEFLIGRTLSNALLSLGIYDDVQGALEAMGLDLEELIDEENDPGLGNGGLGRLAACFLDSLATL
GLPGRGYGIRYDYGMFKQNIVNGRQKESPDYWLEYGNPWEFKRHNTRYKVRFGGRIQQEGKKTRWIETEE
ILAVAYDQIIPGYDTDATNTLRLWSAQASSEINLGKFNQGDYFAAVEDKNHSENVSRVLYPDDSTYSGRE
LRLRQEYFLVSATVQDILSRHYQLHKTYDNLADKIAIHLNDTHPVLSIPELMRLLIDEHKFSWDDAFEVC
CQVFSYTNHTLMSEALETWPVDMLGKILPRHLQIIFEINDYFLKTLQEQYPNDTDLLGRASIIDESNGRR
VRMAWLAVVVSHKVNGVSELHSNLMVQSLFADFAKIFPGRFCNVTNGVTPRRWLALANPSLSAVLDEHIG
RTWRTDLSQLSELKQHCDYPMVNHAVRQAKLENKKRLAEYIAQQLNVVVNPKALFDVQIKRIHEYKRQLM
NVLHVITRYNRIKADPDAKWVPRVNIFAGKAASAYYMAKHIIHLINDVAKVINNDPQIGDKLKVVFIPNY
SVSLAQLIIPAADLSEQISLAGTEASGTSNMKFALNGALTIGTLDGANVEMLEHVGEENIFIFGNTAEEV
EALRRQGYKPREYYEKDEELHQVLTQIGSGVFSPEEPGRYRDLVDSLINFGDHYQVLADYRSYVDCQDKV
DELYRNQEEWTRKAMLNIANMGYFSSDRTIKEYADEIWHIDPVRL
>gnl|CDD|184949 PRK14987, PRK14987, HTH-type transcriptional regulator GntR
MKKKRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLL
PSLTNQVFAEVLRGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEV
AGIPVVELMDSQSPCLDIAVGFDNFEAARQMTTAIIARGHRHIAYLGARLDERTIIKQKGYEQAMLDAGL
VPYSVMVEQSSSYSSGIELIRQARREYPQLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIG
QVMEPRLASVLTPRERMGSIGAERLLARIRGESVTPKMLDLGFTLSPGGSI
>gnl|CDD|237882 PRK14988, PRK14988, GMP/IMP nucleotidase; Provisional
MHIDIAWQDVDTVLLDMDGTLLDLAFDNYFWQKLVPETLGAQRGISPQEAQEYIRQEYHAVQHTLNWYCL
DYWSERLGLDICAMTTEQGPRAVLREDTVPFLEALKASGKRRILLTNAHPHNLAVKLEHTGLDAHLDLLL
STHTFGYPKEDQRLWQAVAEHTGLKAERTLFIDDSEPILDAAAQFGIRYCLGVTNPDSGIAEKQYQRHPS
LNDYRRLIPSLMLR
>gnl|CDD|184951 PRK14989, PRK14989, nitrite reductase subunit NirD; Provisional
MSKVRLAIIGNGMVGHRFIEDLLDKADAANFDITVFCEEPRIAYDRVHLSSYFSHHTAEELSLVREGFYE
KHGIKVLVGERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEA
CARRSKRGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNT
LEIVQEGVEARKTMRFADGSELEVDFIVFSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIG
ECASWNNRVFGLVAPGYKMAQVAVDHLLGSENAFEGADLSAKLKLLGVDVGGIGDAHGRTPGARSYVYLD
ESKEIYKRLIVSEDNKTLLGAVLVGDTSDYGNLLQLVLNAIELPENPDSLILPAHAGSGKPSIGVDKLPD
SAQICSCFDVTKGDLIAAINKGCHTVAALKAETKAGTGCGGCIPLVTQVLNAELAKQGIEVNNNLCEHFA
YSRQELFHLIRVEGIKTFEELLAKHGKGYGCEVCKPTVGSLLASCWNEYILKPQHTPLQDTNDNFLANIQ
KDGTYSVIPRSAGGEITPEGLMAVGRIAREFNLYTKITGSQRIGLFGAQKDDLPEIWRQLIEAGFETGHA
YAKALRMAKTCVGSTWCRYGVGDSVGLGVELENRYKGIRTPHKMKFGVSGCTRECAEAQGKDVGIIATEK
GWNLYVCGNGGMKPRHADLLAADLDRETLIKYLDRFMMFYIRTADKLQRTAVWLENLEGGIDYLKAVIID
DKLGLNAQLEEEMARLREAVVCEWTETVNTPSAQTRFKHFINSDKRDPNVQMVPEREQHRPATPYERIPV
TLVEENA
>gnl|CDD|184952 PRK14990, PRK14990, anaerobic dimethyl sulfoxide reductase subunit A; Provisional
MKTKIPDAVLAAEVSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSAIPTKSDEKVIWSACTVNCGSR
CPLRMHVVDGEIKYVETDNTGDDNYDGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISW
EEAYDIIATNMQRLIKEYGNESIYLNYGTGTLGGTMTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQIA
EGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGGGVTYYLEQARQKSNARMIIIDPRYTDTGAG
REDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDEKTLPASAPKNGHYKAYILGEGPDGVA
KTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGA
REGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWNYAGNCLINQH
SEINRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPR
FECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGIFKKRDPQGHHVA
YKAFREDPQANPLTTPSGKIEIYSQALADIAATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGF
HYKSRVHSTYGNVDVLKAACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGE
GAWYDPDAKRVDKGGCINVLTTQRPSPLAKGNPSHTNLVQVEKV
>gnl|CDD|237883 PRK14991, PRK14991, tetrathionate reductase subunit TtrA
MDKTRRQLLKGGLAAGGLAAFAAGYSDTAKRAAKGLLNGTSGKPTRDRIHGNSLTPEYRVDAQGQLQPNP
QQRVANTQCLGCWTQCGVRVRVDNATNKILRIAGNPYHPLSTDHHIDMSTPVKEAFESLSGESGLEGRST
ACARGNAMLEQLDSPYRVLQPLKRVGKRGSGKWQRISFEQLVEEVVEGGDLFGEGHVDGLRAIRDLDTPI
DAKNPEYGPKANQLLVTNASDEGRDAFIKRFAFNSFGTRNFGNHGSYCGLAYRAGSGALMGDLDKNPHVK
PDWDNVEFALFIGTSPAQSGNPFKRQARQLANARTRGNFEYVVVAPALPLSSSLAAGDNNRWLPIRPGTD
SALAMGMIRWIIDNQRYNADYLAQPGVAAMQAAGEASWTNATHLVIADPGHPRYGQFLRASDLGLPFEGE
ARGDGEDTLVVDAADGELVPATQAQPARLFVEQYVTLADGQRVRVKSSLQLLKEAARKLSLAEYSEQCGV
PEAQIIALAEEFTSHGRKAAVISHGGTMSGNGFYNAWAIMMLNALIGNLNLKGGVVVGGGKFPGFGDGPR
YNLASFAGKVKPKGVSLSRSKFPYEKSSEYRRKVEAGQSPYPAKAPWYPFVAGLLTEMLTAALEGYPYPL
KAWINHMSNPIYGVPGLRAVIEEKLKDPKKLPLFISIDAFINETTALADYIVPDTHTYESWGFTAPWGGV
PTKASTARWPVVEPRTAKTADGQPVCMESFLIAVAKRLQLPGFGDNAIKDAQGNTHPLNRAEDFYLRGAA
NIAYLGKTPVADASDEDIALTGVSRILPALQATLKPDEVRRVAFIYARGGRFAPAESAYDEERMGNRWKK
PLQIWNEDVAAARHSMTGERYSGCPTWYPPRLADGTPLREQFPESQWPLLLISFKSNLMSSMSIASPRLR
QVKPANPVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEHGYGHRELGARAHSIDG
KPMPANPQIRAGVNLNDLGLADPTREITNVWVDWVSGAAVRQGLPAKIEKI
>gnl|CDD|184954 PRK14992, PRK14992, tetrathionate reductase subunit TtrC
IIEEVLAHPQDISWLPWAVQYFFFIGIAACAALFACYLHWRKKDAATEENRALLIAVTCAITAPLALTAD
LHQTARVWHFYAWPTPWSWMPWGALFLPLFTGFLALWFLAQQIKRLFNKSYNVTKWLALASALCAVGLLI
YTGREVSVVLARPIWFSYAFPVAMFLSALQAFFALMIVAARRDSVRLPKILWGQIWTLAALGLVVAMWVS
GDTLSGTAIRQWITVALSAKYYAVGWLALWVFTLLFCSLALRHPLSQLRRVLLVLSALALCWLMRWTLLI
QVQTVPKFNAQFNPYSLPGGTDGWLAILGTFGLWIALLIIIRETLNGLTRRLQHG
>gnl|CDD|184955 PRK14993, PRK14993, tetrathionate reductase subunit TtrB
MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTP
QGAFRTTVNQYQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQ
ACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLK
PENGTSPHVFYLGLDDAFVTPLMGRAQPALWQEV
>gnl|CDD|184956 PRK14994, PRK14994, SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional
MKQHQSADNSQGQLYIVPTPIGNLADITQRALEVLQAVDLIAAEDTRHTGLLLQHFAINARLFALHDHNE
QQKAETLLAKLQEGQNIALVSDAGTPLINDPGYHLVRTCREAGIRVVPLPGPCAAITALSAAGLPSDRFC
YEGFLPAKSKGRRDALKALEAEPRTLIFYESTHRLLDSLEDIVAVLGESRYVVLARELTKTWETIHGAPV
GELLAWVKEDENRRKGEMVLIVEGHKAQEDDLPADALRTLALLQAELPLKKAAALAAEIHGVKKNALYKY
ALEQQGE
>gnl|CDD|184957 PRK14995, PRK14995, SmvA family efflux MFS transporter
MFRQWLTLVIIVLVYIPVAIDATVLHVAAPTLSMTLGASGNELLWIIDIYSLVMAGMVLPMGALGDRIGF
KRLLMLGGTLFGLASLAAAFSPTASWLIATRALLAIGAAMIVPATLAGIRATFTEEKQRNMALGVWAAVG
SGGAAFGPLVGGILLEHFYWGSVFLINVPIVLVVMGLTARYVPRQAGRRDQPLNLGHALMLIVAILLLVY
SAKTALKGFLSLWVTSLTLLTGALLLGLFIRTQLAASRPMIDMRLFTHRIILSGVVMAMTAMITLVGFEL
LMAQELQFVHGLSPLEAGMFMLPVMVASGFSGPIAGILVSRLGLRLVATGGMALSALSFYGLAMTDFSTQ
QWQAWGLMALLGFSAASALLASTSAIMAAAPPEKAAAAGAIETMAYELGAGLGIAIFGLLLSRSYSASIR
LPAGLPAQLIEKASSSIGEAVQLANSLPPTLGQALLDAAKQAFIWSHSVVLSSAGSMLLLLAVGVWFSLA
KAQRR
>gnl|CDD|184958 PRK14996, PRK14996, TetR family transcriptional regulator; Provisional
MSYLNRDERREVILQAAMRVALAEGFAAMTVRRIASEAQVAAGQVHHHFSSAGELKALAFIHLIRQLLDA
EQVPQTASWRERLHAMLGSEDGRFEPYIRLWREAQILADRDPEIKDAYLLTMQMWHQETVAIIEQGKAAG
EFRSTSNATDIAWRLIALVCGLDGIYVLGIPGLADPAFKRHLDRMITLELFA
>gnl|CDD|184959 PRK14997, PRK14997, LysR family transcriptional regulator; Provisional
KTDLNDFAWFVHVVEEGGFAAAGRALDEPKSKLSRRIAQLEERLGVRLIQRTTRQFNVTEVGQTFYEHCK
AMLVEAQAAQDAIAALQVEPRGIVKLTCPVTLLHVHIGPMLAKFMARYPDVSLQLEATNRRVDVVGEGVD
VAIRVRPRPFEDSDLVMRVLADRGHRLFASPDLIARMGIPSAPAELSHWPGLSLASGKHIHRWELYGPQG
ARAEVHFTPRMITTDMLALREAAMAGVGLVQLPVLMVKEQLAAGELVAVLEEWEPRREVIHAVFPSRRGL
LPSVRALVDFLTEEYARMVEE
>gnl|CDD|184960 PRK14998, PRK14998, cold shock-like protein CspD; Provisional
METGTVKWFNNAKGFGFICPEGGGEDIFAHYSTIQMDGYRTLKAGQSVRFDVHQGPKGNHASVIVPIEAE
AVA
>gnl|CDD|184961 PRK14999, PRK14999, histidine utilization repressor; Provisional
MYSSRSRSAPAPFYETVKQDICKKIAGGVWQPHDRIPSEAELVAQYGFSRMTINRALRELTDEGWLVRLQ
GVGTFVAEPKGQSALFEVRSIAEEIAARRHQHRCEVLTLERVRANAIQASALNVNESDVIFHSIMVHYEN
DLPVQIEDRCVNADIAVDYLTQDYRQTTPHAYLSRIAPLTEGEHIVEAVRATAQECAWLTIKEHEPCLLI
RRTTWSASRIVSHARLLFPGSRYRLQGRFIS
>gnl|CDD|184962 PRK15000, PRK15000, peroxiredoxin C
MVLVTRQAPDFTAAAVLGSGEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVE
VVGVSFDSEFVHNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQ
VVNDLPLGRNIDEMLRMVDALQFHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAENISSL
>gnl|CDD|184963 PRK15001, PRK15001, 23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG
MSHLDNGFRSLTLQRFPATDDVNPLQAWEAADEYLLQQLDDTEIRGPVLILNDAFGALSCALAEHKPYSI
GDSYISELATRENLRLNGIDESSVKFLDSTADYPQQPGVVLIKVPKTLALLEQQLRALRKVVTSDTRIIA
GAKARDIHTSTLELFEKVLGPTTTTLAWKKARLINCTFNEPPLADAPQTVSWKLEGTDWTIHNHANVFSR
TGLDIGARFFMQHLPENLEGEIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEAL
DRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVAWEMFHHARRCLKINGELYIVANRHLDYFHKL
KKIFGNCTTIATNNKFVVLKAVKLGRRR
>gnl|CDD|184964 PRK15002, PRK15002, redox-sensitive transcriptional activator SoxR
MEKKLPRIKALLTPGEVAKRSGVAVSALHFYESKGLITSIRNSGNQRRYKRDVLRYVAIIKIAQRIGIPL
ATIGEAFGVLPEGHTLSAKEWKQLSSQWREELDRRIHTLVALRDELDGCIGCGCLSRSDCPLRNPGDRLG
EEGTGARLLEDEQN
>gnl|CDD|184965 PRK15003, PRK15003, cytochrome d ubiquinol oxidase subunit II
MIDYEVLRFIWWLLVGVLLIGFAVTDGFDMGVGMLTRFLGRNDTERRIMINSIAPHWDGNQVWLITAGGA
LFAAWPMVYAAAFSGFYVAMILVLASLFFRPVGFDYRSKIEETRWRNMWDWGIFIGSFVPPLVIGVAFGN
LLQGVPFNVDEYLRLYYTGNFFQLLNPFGLLAGVVSVGMIITQGATYLQMRTVGELHLRTRATAQVAALV
TLVCFALAGVWVMYGIDGYVVKSTMDHYAASNPLNKEVVREAGAWLVNFNNTPILWAIPALGVVLPLLTI
LTARMDKAAWAFVFSSLTLACIILTAGIAMFPFVMPSSTMMNASLTMWDATSSQLTLNVMTWVAVVLVPI
ILLYTAWCYWKMFGRITKEDIERNTHSLY
>gnl|CDD|184966 PRK15004, PRK15004, adenosylcobalamin/alpha-ribazole phosphatase
MRLWLVRHGETQANVDGLYSGHAPTPLTARGIEQAQNLHTLLRDVPFDLVLCSELERAQHTARLVLSDRQ
LPVHIIPELNEMFFGDWEMRHHRDLMQEDAENYAAWCNDWQHAIPTNGEGFQAFSQRVERFIARLSAFQH
YQNLLIVSHQGVLSLLIARLLGMPAEAMWHFRVEQGCWSAIDINQGFATLRVLNSRAVW
>gnl|CDD|184967 PRK15005, PRK15005, universal stress protein UspF
MNRTILVPIDISDSELTQRVISHVEAEAKIDDAEVHFLTVIPSLPYYASLGLAYSAELPAMDDLKAEAKS
QLEEIIKKFKLPTDRVHVHVEEGSPKDRILELAKKIPADMIIIASHRPDITTYLLGSNAAAVVRHAECSV
LVVR
>gnl|CDD|184968 PRK15006, PRK15006, thiosulfate reductase cytochrome B subunit; Provisional
MNPSQHAEQFQSQLANYVPQYTPDYWPVWLIIAGVLLVGMWLVLGLHALLRRRLAPKSATGHGERLYLYS
KAVRLWHWSNALLFVLLLLSGLINHFALVGATAVKSLVAVHEVCGFLLLACWLGFVLINAVGGNGHHYRI
RRQGWLERCAKQTRFYLFGIMQGEEHPFPATTQSKFNPLQQLAYLGVMYGLVPLLLLTGLLCLYPQAVGD
VFPGVRYWLLQLHFALAFISLFFIFGHLYLCTTGRTPGETFRSMVDGYHRH
>gnl|CDD|184969 PRK15007, PRK15007, arginine ABC transporter substrate-binding protein
MKKVLIAALIAGFSLSATAAETIRFATEASYPPFESIDANNQIVGFDVDLAQALCKEIDATCTFSNQAFD
SLIPSLKFRRVEAVMAGMDITPEREKQVLFTTPYYDNSALFVGQQGKYTSVDQLKGKKVGVQNGTTHQKF
IMDKHPEITTVPYDSYQNAKLDLQNGRIDAVFGDTAVVTEWLKDNPKLAAVGDKVTDKDYFGTGLGIAVR
QGNTELQQKLNTALEKVKKDGTYETIYNKWFQK
>gnl|CDD|184970 PRK15008, PRK15008, HTH-type transcriptional regulator RutR; Provisional
MTQGAVKTTGKRSRAVSAKKKAILSAALDTFSQFGFHGTRLEQIAELAGVSKTNLLYYFPSKEALYIAVL
RQILDIWLAPLKAFREDFAPLAAIKEYIRLKLEVSRDYPQASRLFCMEMLAGAPLLMDELTGDLKALIDE
KSALIAGWVKSGKLAPIDPQHLIFMIWASTQHYADFAPQVEAVTGATLRDEAFFNQTVENVQRIIIEGIR
PR
>gnl|CDD|184971 PRK15009, PRK15009, GDP-mannose pyrophosphatase NudK; Provisional
MTQQITLIKDKILSDNYFTLHNITYDLTRKDGEVIRHKREVYDRGNGATILLYNAKKKTVVLIRQFRVAT
WVNGNESGQLIETCAGLLDNDEPEVCIRKEAIEETGYEVGEVRKLFELYMSPGGVTELIHFFIAEYSDSQ
RANAGGGVEDEDIEVLELPFSQALEMIKTGEIRDGKTVLLLNYLQTSHLMD
>gnl|CDD|184972 PRK15010, PRK15010, lysine/arginine/ornithine ABC transporter substrate-binding protein ArgT
MKKSILALSLLVGLSAAASSYAALPETVRIGTDTTYAPFSSKDAKGDFVGFDIDLGNEMCKRMQVKCTWV
ASDFDALIPSLKAKKIDAIISSLSITDKRQQEIAFSDKLYAADSRLIAAKGSPIQPTLDSLKGKHVGVLQ
GSTQEAYANETWRSKGVDVVAYANQDLVYSDLAAGRLDAALQDEVAASEGFLKQPAGKDFAFAGPSVKDK
KYFGDGTGVGLRKDDAELTAAFNKALGELRQDGTYDKMAKKYFDFNVYGD
>gnl|CDD|184973 PRK15011, PRK15011, sugar efflux transporter SetB
MHNSPAVSSAKSFDLTSTAFLIVAFLTGIAGALQTPTLSIFLTDEVHARPAMVGFFFTGSAVIGILVSQF
LAGRSDKRGDRKSLIVFCCLLGVLACTLFAWNRNYFVLLFVGVFLSSFGSTANPQMFALAREHADKTGRE
AVMFSSFLRAQVSLAWVIGPPLAYALAMGFSFTVMYLSAAVAFIVCGVMVWLFLPSMRKELPLATGTLEA
PRRNRRDTLLLFVICTLMWGTNSLYIINMPLFIINELHLPEKLAGVMMGTAAGLEIPTMLIAGYFAKRLG
KRFLMRVAAVAGVCFYAGMLMAHSPAILLGLQLLNAIYIGILGGIGMLYFQDLMPGQAGSATTLYTNTSR
VGWIIAGSLAGIVAEIWNYHAVFWFALVMIIATLFCLLRIKDV
>gnl|CDD|184974 PRK15012, PRK15012, menaquinone-specific isochorismate synthase; Provisional
MQSLTTALENLLRHLSQEIPATPGIRVIDIPFPLNDAFDALSWLASQQTYPQFYWQQRNGDEEAAVLGAI
TRFTSLDQAQRFLRQHPEHADLRIWGLNAFDPSQGNLLLPRLEWRRCGGKATLRLTLFSESSLQHDAIQA
KEFLATLVSIKPLPGLHLTTTREQHWPDKTGWTQLIELATKTIAEGELDKVVLARATDLHFASPVNAAAM
MAASRRLNLNCYHFYMAFDAENAFLGSSPERLWRRRDKALRTEALAGTVANHPDDKQAQQLGEWLMADDK
NQRENMLVVEDICQRLQADTQTLDVLPPQVLRLRKVQHLRRCIWTSLNKADDVICLHQLQPTAAVAGLPR
DLARQFIARHEPFTREWYAGSAGYLSLQQSEFCVSLRSAKVSGNVVRLYAGAGIVRGSDPEQEWQEIDNK
AAGLRTLLQME
>gnl|CDD|184975 PRK15014, PRK15014, 6-phospho-beta-glucosidase BglA; Provisional
MKKLTLPKDFLWGGAVAAHQVEGGWNKGGKGPSICDVLTGGAHGVPREITKEVVPGKYYPNHEAVDFYGH
YKEDIKLFAEMGFKCFRTSIAWTRIFPKGDEAQPNEEGLKFYDDMFDELLKYNIEPVITLSHFEMPLHLV
QQYGSWTNRKVVDFFVRFAEVVFERYKHKVKYWMTFNEINNQRNWRAPLFGYCCSGVVYTEHENPEETMY
QVLHHQFVASALAVKAARRINPEMKVGCMLAMVPLYPYSCNPDDVMFAQESMRERYVFTDVQLRGYYPSY
VLNEWERRGFNIKMEDGDLDVLREGTCDYLGFSYYMTNAVKAEGGTGDAISGFEGSVPNPYVKASDWGWQ
IDPVGLRYALCELYERYQKPLFIVENGFGAYDKVEEDGSINDDYRIDYLRAHIEEMKKAVTYDGVDLMGY
TPWGCIDCVSFTTGQYSKRYGFIYVNKHDDGTGDMSRSRKKSFNWYKEVIASNGEKL
>gnl|CDD|184976 PRK15015, PRK15015, carbon starvation protein CstA
MNKSGKYLVWTVLSVMGAFALGYIALNRGEQINALWIVVASVCIYLIAYRFYGLYIAKNVLAVDPTRMTP
AVRHNDGLDYVPTDKKVLFGHHFAAIAGAGPLVGPVLAAQMGYLPGMIWLLAGVVLAGAVQDFMVLFVST
RRDGRSLGELVKEEMGPTAGVIALVACFMIMVIILAVLAMIVVKALTHSPWGTYTVAFTIPLALFMGIYL
RYLRPGRIGEVSVIGLVFLIFAIISGGWVAESPTWAPYFDFTGVQLTWMLVGYGFVAAVLPVWLLLAPRD
YLSTFLKIGTIVGLAVGILIMRPTLTMPALTKFVDGTGPVWTGNLFPFLFITIACGAVSGFHALISSGTT
PKMLANEGQACFIGYGGMLMESFVAIMALVSACIIDPGVYFAMNSPMAVLAPAGTADVVASAAQVVSSWG
FAITPDTLNQIASEVGEQSIISRAGGAPTLAVGMAYILHGALGGMMDVAFWYHFAILFEALFILTAVDAG
TRAARFMLQDLLGVVSPGLKRTDSLPANLLATALCVLAWGYFLHQGVVDPLGGINTLWPLFGIANQMLAG
MALMLCAVVLFKMKRQRYAWVALVPTAWLLICTLTAGWQKAFSPDAKVGFLAIANKFQAMIDSGNIPPQY
TESQLAQLVFNNRLDAGLTIFFMVVVVVLALFSIKTALAALKEPKPTAKETPYEPMPENVEEIVAQAKGA
H
>gnl|CDD|184977 PRK15016, PRK15016, isochorismate synthase EntC; Provisional
MDTSLAEEVQQTMATLAPDRFFFMSPYRSFTTSGCFARFDEPAVNGDSPDSPFQQKLAALFADAKAQGIK
NPVMVGAIPFDTRQPSSLYIPESWQSFSRQEKQRSARRFTRSQSLNVVERQAIPEQTTFEAMVARAAALT
ATPQVDKVVLSRLIDITTDAAIDSGALLERLIAQNPVSYNFHVPLADGGVLLGASPELLLRKDGERFSSL
PLAGSARRQPDEVLDREAGNRLLASEKDRHEHELVTQAMKEVLRERSSELHVPSSPQLITTPTLWHLATP
FEGKANAQENALTLACLLHPTPALSGFPHQAAKQVIAELEPFDRELFGGIVGWCDSEGNGEWVVTIRCAK
LRENQVRLFAGAGIVPASSPLGEWRETGVKLSTMLNVFGLH
>gnl|CDD|184978 PRK15017, PRK15017, cytochrome o ubiquinol oxidase subunit I; Provisional
MFGKLSLDAVPFHEPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLL
RGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPF
LNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFV
TILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW
AWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGI
TTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHF
HNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQ
FHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHE
RDAFWEMKEKGEAYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSF
DEDVDYYVPVAEIEKLENQHFDEITKAGLKNGN
>gnl|CDD|184979 PRK15018, PRK15018, 1-acyl-sn-glycerol-3-phosphate acyltransferase; Provisional
MLYIFRLIITVIYSILVCVFGSIYCLFSPRNPKHVATFGHMFGRLAPLFGLKVECRKPADAESYGNAIYI
ANHQNNYDMVTASNIVQPPTVTVGKKSLLWIPFFGQLYWLTGNLLIDRNNRTKAHGTIAEVVNHFKKRRI
SIWMFPEGTRSRGRGLLPFKTGAFHAAIAAGVPIIPVCVSTTSNKINLNRLHNGLVIVEMLPPIDVSQYG
KDQVRELAAHCRSIMEQKIAELDKEVAEREAAGKV
>gnl|CDD|184980 PRK15019, PRK15019, cysteine desulfurase sulfur acceptor subunit CsdE
MTNPQFAGHPFGTTVTAETLRNTFAPLTQWEDKYRQLIMLGKQLPALPDELKAQAKEIAGCENRVWLGYT
VAENGKMHFFGDSEGRIVRGLLAVLLTAVEGKTAAELQAQSPLALFDELGLRAQLSASRSQGLNALSEAI
IAATKQV
>gnl|CDD|237884 PRK15020, PRK15020, ethanolamine utilization cob(I)yrinic acid a,c-diamide adenosyltransferase EutT
MKDFITEAWLRANHTLSEGAEIHLPADSRLTPSARELLESRHLRIKFIDEQGRLFVDDEQQQPQPVHGLT
SSDEHPQACCELCRQPVAKKPDTLTHLSAEKMVAKSDPRLGFRAVLDSTIALAVWLQIELAEPWQPWLAD
IRSRLGNIMRADALGEPLAAQAIVGLSDEDLHRLSHQPLRYLDHDHLVPEASHGRDAALLNLLRTKVRET
ETVAAQVFITRSFEVLRPDILQALNRLSSTVYVMMILSVTKQPLTVKQIQQRLGETQ
>gnl|CDD|184982 PRK15021, PRK15021, microcin C ABC transporter permease; Provisional
MSRLSPVNQARWARFRHNRRGYWSLWIFLVLFGLSLCSELIANDKPLLVRYDGSWYFPLLKNYSESDFGG
PLASQADYQDPWLKQRLENNGWVLWAPIRFGATSINFATDKPFPSPPSRQNWLGTDANGGDVLARILYGT
RISVLFGLMLTLCSSVMGVLAGALQGYYGGKVDLWGQRFIEVWSGMPTLFLIILLSSVVQPNFWWLLAIT
VLFGWMSLVGVVRAEFLRTRNFDYIRAAQALGVSDRSIILRHMLPNAMVATLTFLPFILCSSITTLTSLD
FLGFGLPLGSPSLGELLLQGKNNLQAPWLGITAFLSVAILLSLLIFIGEAVRDAFDPNKAV
>gnl|CDD|184983 PRK15022, PRK15022, non-heme ferritin-like protein
MATAGMLLKLNSQMNLEFYASNLYLHLSEWCSEQSLNGTATFLRAQAQSNVTQMMRMFNFMKSAGATPIV
KAIDVPGEKLNSLEELFQKTLEEYEQRSSTLAQLADEAKALNDDSTLNFLRDLEKEQQHDGLLLQTILDE
VRSAKLAGLCPVQTDQHLLNVVSHQLH
>gnl|CDD|184984 PRK15023, PRK15023, L-serine deaminase; Provisional
MISLFDMFKVGIGPSSSHTVGPMKAGKQFVDDLVEKGLLDSVTRVAVDVYGSLSLTGKGHHTDIAIIMGL
AGNEPATVDIDSIPGFIRDVEERERLLLAQGRHEVDFPRDNGMRFHNGNLPLHENGMQIHAYNGDEVVYS
KTYYSIGGGFIVDEEHFGQDAANEVSVPYPFKSATELLAYCNETGYSLSGLAMQNELALHSKKEIDEYFA
HVWQTMQACIDRGMNTEGVLPGPLRVPRRASALRRMLVSSDKLSNDPMNVIDWVNMFALAVNEENAAGGR
VVTAPTNGACGIVPAVLAYYDHFIESVSPDIYTRYFMAAGAIGALYKMNASISGAEVGCQGEVGVACSMA
AAGLAELLGGSPEQVCVAAEIGMEHNLGLTCDPVAGQVQVPCIERNAIASVKAINAARMALRRTSAPRVS
LDKVIETMYETGKDMNAKYRETSRGGLAIKVQCD
>gnl|CDD|184985 PRK15025, PRK15025, ureidoglycolate dehydrogenase; Provisional
MKISRETLHQLIKNKLCKAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRFE
ETGPCSAILHADNAAGQVAAKMGMEHAIETAKQNGVAVVGISRMGHSGAISYFVQQAARAGLIGLSMCQS
DPMVVPFGGAEIYYGTNPLAFAAPGEGDEIITFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTD
PFAVHALLPAAGPKGYGLMMMVDVLSGVLLGLPFGRQVSSMYDDLHAGRNLGQLHIVINPAFFSSSELFR
QHISQTMRELNAITPAPGFNQVYYPGQDQDIKQKKAAVEGIEIVDDIYQYLISDALYNTSYETKNPFAQ
>gnl|CDD|184986 PRK15026, PRK15026, aminoacyl-histidine dipeptidase; Provisional
MSELSQLSPQPLWDIFAKICSIPHPSYHEEQLAEYIVGWAKEKGFHVERDQVGNILIRKPATAGMENRKP
VVLQAHLDMVPQKNNDTVHDFTKDPIQPYIDGEWVKARGTTLGADNGIGMASALAVLADENVVHGPLEVL
LTMTEEAGMDGAFGLQSNWLQADILINTDSEEEGEIYMGCAGGIDFTSNLHLDREAVPAGFETFKLTLKG
LKGGHSGGEIHVGLGNANKLLVRFLAGHAEELDLRLIDFNGGTLRNAIPREAFATIAVAADKVDALKSLV
NTYQEILKNELAEKEKNLALLLDSVANDKAALIAKSRDTFIRLLNATPNGVIRNSDVAKGVVETSLNVGV
VTMTDNNVEIHCLIRSLIDSGKDYVVSMLDSLGKLAGAKTEAKGAYPGWQPDANSPVMHLVRETYQRLFN
KTPNIQIIHAGLECGLFKKPYPEMDMVSIGPTITGPHSPDEQVHIESVGHYWTLLTELLKEIPAK
>gnl|CDD|184987 PRK15027, PRK15027, xylulokinase; Provisional
MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKA
LGIAGQMHGATLLDAQQRVLRPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEP
EIFRQIDKVLLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITG
ALLPEVAKAWGMATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHA
LPQRWHLMSVMLSAASCLDWAAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFF
GLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGG
DVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLYQQLLPLMA
>gnl|CDD|184988 PRK15028, PRK15028, cytochrome d ubiquinol oxidase subunit II
MFDYETLRFIWWLLIGVILVVFMISDGFDMGIGCLLPLVARNDDERRIVINSVGAHWEGNQVWLILAGGA
LFAAWPRVYAAAFSGFYVAMILVLCSLFFRPLAFDYRGKIADARWRKMWDAGLVIGSLVPPVVFGIAFGN
LLLGVPFAFTPQLRVEYLGSFWQLLTPFPLLCGLLSLGMVILQGGVWLQLKTVGVIHLRSQLATKRAALL
VMLCFLLAGYWLWVGIDGFVLLAQDANGPSNPLMKLVAVLPGAWMNNFVESPVLWIFPLLGFFCPLLTVM
AIYRGRPGWGFLMASLMQFGVIFTAGITLFPFVMPSSVSPISSLTLWDSTSSQLTLSIMLVIVLIFLPIV
LLYTLWSYYKMWGRMTTETLRRNENELY
>gnl|CDD|184989 PRK15029, PRK15029, arginine decarboxylase; Provisional
MKVLIVESEFLHQDTWVGNAVERLADALSQQNVTVIKSTSFDDGFAILSSNEAIDCLMFSYQMEHPDEHQ
NVRQLIGKLHERQQNVPVFLLGDREKALAAMDRDLLELVDEFAWILEDTADFIAGRAVAAMTRYRQQLLP
PLFSALMKYSDIHEYSWAAPGHQGGVGFTKTPAGRFYHDYYGENLFRTDMGIERTSLGSLLDHTGAFGES
EKYAARVFGADRSWSVVVGTSGSNRTIMQACMTDNDVVVVDRNCHKSIEQGLILTGAKPVYMVPSRNRYG
IIGPIYPQEMQPETLQKKISESPLTKDKAGQKPSYCVVTNCTYDGVCYNAKEAQDLLEKTSDRLHFDEAW
YGYARFNPIYADHYAMRGEPGDHNGPTVFATHSTHKLLNALSQASYIHVREGRGAINFSRFNQAYMMHAT
TSPLYAICASNDVAVSMMDGNSGLSLTQEVIDEAVDFRQAMARLYKEFTADGSWFFKPWNKEVVTDPQTG
KTYDFADAPTKLLTTVQDCWVMHPGESWHGFKDLPDNWSMLDPIKVSILAPGMGEDGELEETGVPAALVT
AWLGRHGIVPTRTTDFQIMFLFSMGVTRGKWGTLVNTLCSFKRHYDANTPLAQVMPELVEQYPDTYANMG
IHDLGDTMFAWLKENNPGARLNEAYSGLPVAEITPREAYNAIVDNNVELVSIENLPGRIAANSVIPYPPG
IPMLLSGENFGDKNSPQVSYLRSLQSWDHHFPGFEHETEGTEIIDGIYHVMCVKA
>gnl|CDD|184990 PRK15030, PRK15030, multidrug efflux RND transporter periplasmic adaptor subunit AcrA
MNKNRGFTPLAVVLMLSGSLALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRP
QVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISK
QEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLD
PIYVDVTQSSNDFLRLKQELANGTLKQENGKAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIF
PNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATVLVVGADDKVETRPIVASQAIGDKWLVT
EGLKAGDRVVISGLQKVRPGVQVKAQEVTADNNQQAASGAQPEQSKS
>gnl|CDD|184991 PRK15031, PRK15031, 5-carboxymethyl-2-hydroxymuconate Delta-isomerase
MPHFIAECTENIREQADLPGLFAKVNQALAATGIFPLGGIRSRAHWLDTWQMADGKHDYAFVHMTLKIGA
GRSLESRQEVGEMLFALIKAHFAALMESRYLALSFEIEELHPTLNFKQNNVHALFK
>gnl|CDD|184992 PRK15032, PRK15032, pentaheme c-type cytochrome TorC
MRKLWNALRRPSARWSVLALVAVGIVIGIALIVLPHVGIKVTSTTEFCVSCHSMQPVYEEYKQSVHFQNA
SGVRAECHDCHIPPDIPGMVKRKLEASNDIYQTFIAHSIDTPEKFEAKRAELAEREWARMKENNSATCRS
CHNYDAMDHAKQHPEAARQMKVAAKDNQSCIDCHKGIAHQLPDMSSGFRKQFDELRASANDSGDTLYSID
IKPIYAAKGDKEASGSLLPASEVKVLKRDGDWLQIEIEGWTESAGRQRVLTQFPGKRIFVASIRGDVQQQ
VKTLEKTTVADTNTEWSKLQATAWMKKGDMVNDIKPIWAYADSLYNGTCNQCHGAPEIAHFDANGWIGTL
NGMIGFTSLDKREERTLLKYLQMNASDTAGKAHGDKKEEK
>gnl|CDD|237885 PRK15033, PRK15033, tricarballylate utilization 4Fe-4S protein TcuB
MQQLEKLIIEARALAGGGTVLTAPEAEVARQMQICNACRYCEGFCAVFPAMTRRLEFGKADIHYLANLCH
NCGACLHACQYAPPHEFAVNVPKAMAQVRLETYQEYAWPAALGALYRRNGLTLSLALAVGLALFLLLAVA
LKGSLLHAPLAGNFYAIFPHNLLALMFGSVFLFAILALGIGVRRFWRDVSPGTAGAAVSAAAAEAAHNAL
TLKYLDGGHGKGCNEADDAFTLARRRFHHLTFYGFMLCFAATVVATLYHYVLGWHAPYPFFSLPVLLGTL
GGIGLLIGPAGLLWLNLRRHPLHGDAAQKPMDRGFIALLFLTSASGLALLAGRDTSAMALLLALHLGVVM
ALFLTLPYGKFAHGFFRSAALLKWAIEKRQPKKLGLGGD
>gnl|CDD|184994 PRK15034, PRK15034, nitrate/nitrite transport protein NarU; Provisional
MALQNEKNSRYLLRDWKPENPAFWENKGKHIARRNLWISVSCLLLAFCVWMLFSAVTVNLNKIGFNFTTD
QLFLLTALPSVSGALLRVPYSFMVPIFGGRRWTVFSTAILIIPCVWLGIAVQNPNTPFGIFIVIALLCGF
AGANFASSMGNISFFFPKAKQGSALGINGGLGNLGVSVMQLVAPLVIFVPVFAFLGVNGVPQADGSVMSL
ANAAWIWVPLLAIATIAAWSGMNDIASSRASIADQLPVLQRLHLWLLSLLYLATFGSFIGFSAGFAMLAK
TQFPDVNILRLAFFGPFIGAIARSVGGAISDKFGGVRVTLINFIFMAIFSALLFLTLPGTGSGNFIAFYA
VFMGLFLTAGLGSGSTFQMIAVIFRQITIYRVKMKGGSDEQAQREAVTETAAALGFISAIGAVGGFFIPQ
AFGMSLNMTGSPVGAMKVFLIFYIVCVLLTWLVYGRRKFSQK
>gnl|CDD|184995 PRK15035, PRK15035, cytochrome bd-II oxidase subunit 1; Provisional
MWDVIDLSRWQFALTALYHFLFVPLTLGLIFLLAIMETIYVVTGKTIYRDMTRFWGKLFGINFALGVATG
LTMEFQFGTNWSFYSNYVGDIFGAPLAMEALMAFFLESTFVGLFFFGWQRLNKYQHLLVTWLVAFGSNLS
ALWILNANGWMQYPTGAHFDIDTLRMEMTSFSELVFNPVSQVKFVHTVMAGYVTGAMFIMAISAWYLLRG
RERDVALRSFAIGSVFGTLAIIGTLQLGDSSAYEVAQVQPVKLAAMEGEWQTEPAPAPFHVVAWPEQDQE
RNAFAIKIPALLGILATHSLDKPVPGLKNLMAETYPRLQRGRMAWLLMQEISQGNREPHVLQAFRELEGD
LGYGMLLSRYAPDMNHVTAAQYQAAMRGAIPQVAPVFWSFRIMVGCGSLLLLVMLIALVQTLRGKIDQHR
WVLKMALWSLPLPWIAIEAGWFMTEFGRQPWAIQDILPTYSAHSALTTGQLAFSLIMIVGLYTLFLIAEV
YLMQKYARLGPSAMQSEQPTQQQG
>gnl|CDD|184996 PRK15036, PRK15036, hydroxyisourate hydrolase; Provisional
MLKRYLVLSVITAAFSLPSLVYAAQQNILSVHILNQQTGKPAADVTVTLEKKADNGWLQLNTAKTDKDGR
IKALWPEQTATTGDYRVVFKTGDYFKKQNLESFFPEIPVEFHINKVNEHYHVPLLLSQYGYSTYRGS
>gnl|CDD|184997 PRK15037, PRK15037, D-mannonate oxidoreductase; Provisional
MTTIVDSNLPVARPSWDHSRLESRIVHLGCGAFHRAHQALYTHHLLESTDSDWGICEVNLMPGNDRVLIE
NLKKQQLLYTVAEKGAESTELKIIGSMKEALHPEIDGCEGILNAMARPQTAIVSLTVTEKGYCADAASGQ
LDLNNPLIKHDLENPTAPKSAIGYIVEALRLRREKGLKAFTVMSCDNVRENGHVAKVAVLGLAQARDPQL
AAWIEENVTFPCTMVDRIVPAATPETLQEIADQLGVYDPCAIACEPFRQWVIEDNFVNGRPDWDKVGAQF
VADVVPFEMMKLRMLNGSHSFLAYLGYLGGYETIADTMTNPAYRKAAFALMMQEQAPTLSMPEGTDLNAY
ATLLIERFSNPSLRHRTWQIAMDGSQKLPQRLLDPVRLHLQNGGSWRHLALGVAGWMRYTQGVDEQGNAI
DVVDPMLAEFQKINAQYQGADRVKALLGLSGIFADDLPQNADFVGAVTAAYQQLCERGARECVAAL
>gnl|CDD|184998 PRK15038, PRK15038, autoinducer 2 ABC transporter permease LsrD
MRRRYGWELALAALLVIEILAFGLINPRMLDINVLLFSTSDFICIGIVALPLTMVIVSGGIDISFGSTIG
LCAIALGVLFQSGVPMPLAILLTLLLGALCGLINAGLIIYTGVNPLVITLGTLYLFGGSALLLSGMAGAT
GYEGIGGFPMAFTDFANLDVLGLPVPLIIFLICLLVFWLLMHRTHAGRNVFLIGQSPRVALYSAIPVNRT
LCALYAMTGLASAIAAVLLVSYFGSARSDLGASFLMPAITAVVLGGANIYGGSGSIIGTALAVLLVGYLQ
QGLQMAGVPNQISSALSGALLIVVVVGRSVSLHRHQIKEWLARRRNNPLP
>gnl|CDD|184999 PRK15039, PRK15039, Ni(II)/Co(II)-binding transcriptional repressor RcnR
MSHTIRDKQKLKARASKIQGQVVALKKMLDEPHECAAVLQQIAAIRGAVNGLMREVIKGHLTEHIVHQGD
ELKREEDLDVVLKVLDSYIK
>gnl|CDD|185000 PRK15040, PRK15040, L-serine ammonia-lyase
MISAFDIFKIGIGPSSSHTVGPMNAGKSFIDRLESSGLLTATSHIVVDLYGSLSLTGKGHATDVAIIMGL
AGNSPQDVVIDEIPAFIELVTRSGRLPVASGAHIVDFPVAKNIIFHPEMLPRHENGMRITAWKGQEELLS
KTYYSVGGGFIVEEEHFGLSHDVETSVPYDFHSAGELLKMCDYNGLSISGLMMHNELALRSKAEIDAGFA
RIWQVMHDGIERGMNTEGVLPGPLNVPRRAVALRRQLVSSDNISNDPMNVIDWINMYALAVSEENAAGGR
VVTAPTNGACGIIPAVLAYYDKFRRPVNERSIARYFLAAGAIGALYKMNASISGAEVGCQGEIGVACSMA
AAGLTELLGGSPAQVCNAAEIAMEHNLGLTCDPVAGQVQIPCIERNAINAVKAVNAARMAMRRTSAPRVS
LDKVIETMYETGKDMNDKYRETSRGGLAIKVVCG
>gnl|CDD|185001 PRK15041, PRK15041, methyl-accepting chemotaxis protein
MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRA
GIRYMMDQNNIGSGSTVAELMQSASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELI
QLLGAGKINEFFDQPTQGYQDGFEKQYVAYMEQNDRLYDIAVSDNNASYSQAMWILVGVMIVVLAVIFAV
WFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSG
ASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQT
MRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSL
IEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAAL
VEESAAAAAALEEQASRLTEAVAVFRIQQQQQQQRETSAVVKTVTPATPRKMAVADSGENWETF
>gnl|CDD|237886 PRK15042, pduD, propanediol/glycerol family dehydratase medium subunit
MEINEKLLRQIIEEVLKEMQGSDKPVSFNAPAASTAPSGEGFLTEVGEAKPGTQQDEVVIAVGPAFGLAQ
TKTIVGIPHKEILREVIAGIEEEGLKARVVRVFRTSDVAFVAVEGARLSGSGIGIGIQSKGTTVIHQKDL
PPLSNLELFPQAPLLTLETYRAIGKNAARYAKGESPQPVPTLNDQMARPKYQAKAALLHIKETKYVVTGK
KPVELRVAF
>gnl|CDD|185003 PRK15043, PRK15043, HTH-type transcriptional regulator MlrA
MALYTIGEVALLCDINPVTLRAWQRRYGLLKPQRTDGGHRLFNDADIDRIREIKRWIDNGVQVSKVKMLL
SNENVDVQNGWRDQQETLLTYLQSGNLHSLRTWIKERGQDYPAQTLTTHLFIPLRRRLQCQQPTLQALLA
ILDGVLINYIAICLASARKKQGKDALVVGWNIHDTTRLWLEGWIASQQGWRIDVLAHSLNQLRPELFEGR
TLLVWCGENRTSAQQQQLTSWQEQGHDIFPLGI
>gnl|CDD|185004 PRK15044, PRK15044, transcriptional regulator SirC; Provisional
MVLPSMNKSVEAISNNHLQQPNKFPLINGLADVRDYYVANCLLFKLNKGSLRIENEFGEFIEQSAPCLFL
LEKDQTITLSMSEIEGHIDFSSLEVSYDLMQKFYKVFYSTRNYNDRELSLKTKPKYFFHADLLPGMSDTF
DSILHGVACPRVCSNVSIDDHDYSYFSLMYLISAFVRKPGGFDFLERAIKITTKEKVYNIIISDLTRKWS
QAEVAGKLFMSVSSLKRKLAAEEVSFSKIYLDARMNQAIKLLRMGAGNISQVATMCGYDTPSYFIAIFKR
HFKITPLSFMRTMNH
>gnl|CDD|185005 PRK15045, PRK15045, cellulose biosynthesis protein BcsE; Provisional
VDPVFSIGISSLWDELRHMPAGGVWWFNVDRHEDAISLANQTIASQAETAHVAVISMDSDPAKIFQLDDS
QGPEKIRLFSMPNHEKGLYYLPRDLQCSIDPHNYLFILVCANNAWQNIPAERLRSWLDKMNKWSRLNHCS
LLVINPGNNNDKQFSLLMEEYRSLFGLASLRFQGDQHLLDIAFWCNEKGVSARQQLSVQQQNGIWTLVQQ
EEAEIQPRSDEKRILSNVAVLEGAPPLSEHWQLFNNNEVLFNEARTAQAATVVFSLQQNAQIEPLARSIH
TLRRQRGSAMKILVRENTASLRATDERLLLGCGANMVIPWNAPLSRCLTMIESVQGQKFSRYVPEDITTL
LSMTQPLKLRGFQKWDVFCNAVNNMMNNPLLPAHGKGVLVALRPVPGIRVEQALTLCRPNRTGDIMTIGG
NRLVLFLSFCRVNDLDTALNHIFPLPTGDIFSNRMVWFEDDQISAELVQMRLLAPEQWGMPLPLTQSSKP
VINAEHDGRHWRRIPEPMRLLDDAVERSS
>gnl|CDD|237887 PRK15046, PRK15046, 2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
MRSTNRAAAAAAMKLAAAAAAAAFGGGAAPAWAADAVTVYSADGLEDWYQDVFPAFTKATGIKVNYVEAG
SGEVVNRAAKEKSNPQADVLVTLPPFIQQAAAEGLLQPYSSVNAKAVPAIAKDADGTYAPFVNNYLSFIY
NPKVLKTAPATWADLLDPKFKGKLQYSTPGQAGDGTAVLLLTFHLMGKDKAFDYLAKLQANNVGPSKSTG
KLTPLVSKGEIYVANGDLQMNLAQAEHGGPNVKIFFPAKDGGERSTFALPYVIGLVKGAPNSENGKKLID
FLLSKEAQTKVSDMAWGIPVRTDVPPSDKNGEAVKAALEGVKLWPPDWDDVMAKLDADIARWKKATGSE
>gnl|CDD|185007 PRK15047, PRK15047, N-hydroxyarylamine O-acetyltransferase; Provisional
MTPFLNAYFARINWSGAAAVNIDTLRALHLKHNCTIPFENLDVLLPREIQLDDQSLEEKLVIARRGGYCF
EQNGLFERVLRELGFNVRSLLGRVVLSNPPALPPRTHRLLLVELEGEKWIADVGFGGQTLTAPIRLVADI
VQTTPHGEYRLLQEGDDWVLQFNHHQHWQSMYRFDLCEQQQSDYVMGNFWSAHWPQSHFRHHLLMCRHLP
DGGKLTLTNFHFTHYENGHAVEQRNLPDVASLYAVMQEQFGLGVDDAKHGFTVAELAAVMAAFDTHPEAG
K
>gnl|CDD|185008 PRK15048, PRK15048, methyl-accepting chemotaxis protein II; Provisional
MINRIRVVTLLVMVLGVFALLQLISGSLFFSSLHHSQKSFVVSNQLREQQGELTSTWDLMLQTRINLSRS
AVRMMMDSSNQQSNAKVELLDSARKTLAQAATHYKKFKSMAPLPEMVATSRNIDEKYKNYYTALTELIDY
LDYGNTGAYFAQPTQGMQNAMGEAFAQYALSSEKLYRDIVTDNADDYRFAQWQLAVIALVVVLILLVAWY
GIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTR
EIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMH
EIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIE
DSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQ
ESAAAAAALEEQASRLTQAVSAFRLAASPLTNKPQTPSRPASEQPPAQPRLRIAEQDPNWETF
>gnl|CDD|185009 PRK15049, PRK15049, L-asparagine permease
MSKHDTDTSDQHAAKRRWLNAHEEGYHKAMGNRQVQMIAIGGAIGTGLFLGAGARLQMAGPALALVYLIC
GLFSFFILRALGELVLHRPSSGSFVSYAREFLGEKAAYVAGWMYFINWAMTGIVDITAVALYMHYWGAFG
GVPQWVFALAALTIVGTMNMIGVKWFAEMEFWFALIKVLAIVTFLVVGTVFLGSGQPLDGNTTGFHLITD
NGGFFPHGLLPALVLIQGVVFAFASIEMVGTAAGECKDPQTMVPKAINSVIWRIGLFYVGSVVLLVMLLP
WSAYQAGQSPFVTFFSKLGVPYIGSIMNIVVLTAALSSLNSGLYCTGRILRSMAMGGSAPSFMAKMSRQH
VPYAGILATLVVYVVGVFLNYLVPSRVFEIVLNFASLGIIASWAFIIVCQMRLRKAIKEGKAADVSFKLP
GAPFTSWLTLLFLLSVLVLMAFDYPNGTYTIAALPIIGILLVIGWFGVRKRVAEIHSTAPVVEEDEEKQE
IVFKPETAS
>gnl|CDD|237888 PRK15050, PRK15050, 2-aminoethylphosphonate transport system permease PhnU; Provisional
AAARVRASAAAHAAAARRRRRLRPLLWLLLPLLVLAPLVVYPLVRVVLQSLTGEHGLGLATYRAVLGSPD
FRGALLTTLQIAFASTAGCLVLGVLLALVLAFVPFPGASLVGRFIDTFVAFPSFLITLAFTFLYGSAGSV
NIALQRLFGLEAPPLDFLYSPGGVILAEITFYTPFVVRPLLAAFAQLDARQLEAAASLGASPWRVARRVI
LPEAWPALAAGGSLCLLLTLNEFGIVLFTGAKDVVTLPVLIYSKAIVDFDYPTACAIAVVNLALSLGLYA
LYRRVNRRAGGGSRDR
>gnl|CDD|185011 PRK15051, PRK15051, 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnE; Provisional
MIWLTLVFASLLSVAGQLCQKQATRPVAIGKRRKHIVLWLGLALACLGLAMVLWLLVLQNVPVGIAYPML
SLNFVWVTLAAVKLWHEPVSPRHWCGVAFIIGGIVILGSTV
>gnl|CDD|237889 PRK15052, PRK15052, tagatose-bisphosphate aldolase subunit GatZ
MKTLIARHKAGEHIGICSVCSAHPLVIEAALAFDLNSTRKVLIEATSNQVNQFGGYTGMTPADFREFVYG
IADKVGFPRERIILGGDHLGPNCWQQEPADAAMEKSVELVKAYVRAGFSKIHLDASMSCADDPIPLAPET
VAERAAVLCQAAESVATDCQREQLSYVIGTEVPVPGGEASAIQSVHVTRVEDAANTLRTHQKAFIARGLT
EALTRVIAIVVQPGVEFDHSNIIHYQPQEAQALSAWIENTPMVYEAHSTDYQTRQAYRELVRDHFAILKV
GPALTFALREAIFALAQIEQELIAPENRSRCLAVIEEVMLDEPQYWKKYYRPGFSDALLDIHFSLSDRIR
YYWPHSRIKNSVETLIVNLEGVDIPLGLISQYLPKQFERIQSGELSAIPHQLIMDKIQDVLRAYRYGCAE
D
>gnl|CDD|185013 PRK15053, dpiB, sensor histidine kinase DpiB; Provisional
MLQLNENKQFAFFQRLAFPLRIFLLILVFSIFVIAALAQYFSASFEDYLTLHVRDMAMNQAKIIASNDSV
ISAVKTRDYKRLATIANKLQRDTDFDYVVIGDRHSIRLYHPNPEKIGYPMQFTKPGALEKGESYFITGKG
SMGMAMRAKTPIFDDDGKVIGVVSIGYLVSKIDSWRLEFLLPMAGVFVVLLGILMLLSWFFAAHIRRQMM
GMEPKQIARVVRQQEALFSSVYEGLIAVDPHGYITAINRNARKMLGLSSPGRQWLGKPIAEVVRPADFFT
EQIDEKRQDVVANFNGLSVIANREAIRSGDDLLGAIISFRSKDEISTLNAQLTQIKQYVESLRTLRHEHL
NWMSTLNGLLQMKEYDRVLEMVQGESQAQQQLIDSLREAFADRQVAGLLFGKVQRARELGLKMVIVPGSQ
LSQLPPGLDSTEFAAIVGNLLDNAFEASLRSDEGNKIVELFLSDEGDDVVIEVADQGCGVPESLRDKIFE
QGVSTRADEPGEHGIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIPKVKPNDS
>gnl|CDD|185014 PRK15054, PRK15054, nitrate reductase molybdenum cofactor assembly chaperone
MQILKVIGLLMEYPDELLWECKEDALALIRRDAPMLTDFTRNLLNAPLLDKQAEWCEVFDRGRTTSLLLF
EHVHAESRDRGQAMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRL
KQREAPWYALFDALLQLAGSTLSSDSVTKQVNSEERDDTRQALDAVWEEEQVKFIEDNATACDSSPLNQY
QRRFSQDVAPQYVDISAGGGK
>gnl|CDD|185016 PRK15056, PRK15056, manganese/iron ABC transporter ATP-binding protein
MMQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP
TRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQI
GELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD
YTVMVKGTVLASGPTETTFTAENLELAFSGVLRHVALNGSEESIITDDERPFISHRPAAVQR
>gnl|CDD|185017 PRK15057, PRK15057, UDP-glucose 6-dehydrogenase; Provisional
MKITISGTGYVGLSNGLLIAQNHEVVALDILPSRVAMLNDRISPIVDKEIQQFLQSDKIHFNATLDKNEA
YRDADYVIIATPTDYDPKTNYFNTSSVESVIKDVVEINPYAVMVIKSTVPVGFTAAMHKKYRTENIIFSP
EFLREGKALYDNLHPSRIVIGERSERAERFAALLQEGAIKQNIPTLFTDSTEAEAIKLFANTYLAMRVAY
FNELDSYAESLGLNTRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQLLANYQSVPNNLISAIVDAN
RTRKDFIADAILSRKPQVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEPVMKEDSFFNSRLE
RDLATFKQQADVIISNRMAEELKDVADKVYTRDLFGSD
>gnl|CDD|185018 PRK15058, PRK15058, cytochrome b562; Provisional
MRKSLLAILAVSSLVFSSASFAADLEDNMETLNDNLKVVEKTDNAAEVKDALTKMRAAALDAQKATPPKL
EDKAPDSPEMKDFRHGFDILVGQIDGALKLANEGKVKEAQAAAEQLKTTRNAYHKKYR
>gnl|CDD|185019 PRK15059, PRK15059, 2-hydroxy-3-oxopropionate reductase
MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVE
EVLFGENGCTKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEA
VFERVKPLFELLGKNITLVGGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFAS
SRILEVHGERMIKRTFNPGFKIALHQKDLNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALV
QALELMANHKLA
>gnl|CDD|185020 PRK15060, PRK15060, 2,3-diketo-L-gulonate transporter large permease YiaN
MAVLIFLGCLLGGIAIGLPIAWALLLCGAALMFWLDMFDVQIMAQTLVNGADSFSLLAIPFFVLAGEIMN
AGGLSKRIVDLPMKLVGHKPGGLGYVGVLAAMIMASLSGSAVADTAAVAALLVPMMRSANYPVNRAAGLI
ASGGIIAPIIPPSIPFIIFGVSSGLSISKLFMAGIAPGIMMGATLMLTWWWQASRLNLPRQPKATMREIW
QSLVSGIWALFLPVIIIGGFRSGLFTPTEAGAVAAFYALFVAVVIYREMTFSTLYHVLINAAKTTSVVMF
LVASAQVSAWLITIAELPMMVSDLLQPLVDSPRLLFIVIMVAIMVVGMVMDLTPTVLILTPVLMPLVKEA
GIDPIYFGVMFIINCSIGLITPPVGNVLNVISGVAKLKFDDAVRGVFPYVLVLYSLLVLFIFIPELIILP
LKWIN
>gnl|CDD|237891 PRK15061, PRK15061, catalase/peroxidase
SSAGKCPVMHGAGGGTSNRDWWPNQLNLDILHQHSSKSNPMGEDFDYAEEFKKLDLEALKKDLKALMTDS
QDWWPADYGHYGPLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGN
KISWADLMILAGNVALESMGFKTFGFAGGREDVWEPEEDVYWGPEKEWLGGDERYSGERDLENPLAAVQM
GLIYVNPEGPNGNPDPLAAARDIRETFARMAMNDEETVALIAGGHTFGKTHGAGDASHVGPEPEAAPIEE
QGLGWKNSYGSGKGADTITSGLEGAWTTTPTQWDNGYFENLFGYEWELTKSPAGAWQWVPKDGAAEDTVP
DAHDPSKKHAPTMLTTDLALRFDPEYEKISRRFLENPEEFADAFARAWFKLTHRDMGPKSRYLGPEVPKE
DLIWQDPVPAVDHELIDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDKRGGANGARIRLAPQKD
WEVNEPAQLAKVLAVLEGIQAEFNAAQSGGKKVSLADLIVLGGNAAVEQAAKAAGHDVTVPFTPGRTDAT
QEQTDVESFAVLEPKADGFRNYLKKGYSVSPEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGV
FTDRPGVLTNDFFVNLLDMGTEWKPTDEDEEVYEGRDRKTGEVKWTATRVDLVFGSNSQLRALAEVYASD
DAKEKFVRDFVAAWTKVMNLDRFDLA
>gnl|CDD|237893 PRK15063, PRK15063, isocitrate lyase; Provisional
MMMTRTQQIEELEKDWATNPRWKGITRPYSAEDVVRLRGSVQIEHTLARRGAEKLWELLHGEPYVNALGA
LTGNQAVQQVKAGLKAIYLSGWQVAADANLAGQMYPDQSLYPANSVPAVVKRINNALRRADQIQWSEGDK
GYIDYFAPIVADAEAGFGGVLNAFELMKAMIEAGAAGVHFEDQLASEKKCGHMGGKVLVPTQEAIRKLVA
ARLAADVMGVPTLVIARTDAEAADLLTSDVDERDRPFITGERTAEGFYRVKAGIEQAIARGLAYAPYADL
IWCETSTPDLEEARRFAEAIHAKFPGKLLAYNCSPSFNWKKNLDDATIAKFQRELGAMGYKFQFITLAGF
HSLNYSMFDLAHGYAREGMAAYVELQEAEFAAEERGYTAVKHQREVGTGYFDAVTTVIQGGQSSTTALTG
STEEEQFH
>gnl|CDD|237894 PRK15064, PRK15064, ABC transporter ATP-binding protein; Provisional
MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLR
QDQFAFEEFTVLDTVIMGHTELWEVKQERDRIYALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLL
GVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISH
DRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAK
QATSRAKQIDKIKLEEVKPSSRQNPFIRFEQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAI
IGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLTLFDWMSQWRQEGDDEQAVRG
TLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIF
VSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQGIE
>gnl|CDD|237895 PRK15065, PRK15065, mannose/fructose/sorbose family PTS transporter subunit IIC
MEISTIQIILVFIVAFIAGMESILDEFQFHRPLVACTLIGLVLGDLKTGIILGGTLEMIALGWMNIGAAV
APDAALASVISAILVIAGHQGIGTGIAIAIPLAAAGQVLTIIVRTITVAFQHAADKAAEEGNFRAIEWLH
VSALLLQALRIAIPAALVALAVGTSAVQSMLNAIPEVLTGGLNIGGGMIVVVGYAMVINMMATRELMPFF
YLGFVLAAFTNLNLIALGVIGVVLALIYLQLSPKYGRVAGGGAAGSGDPLDD
>gnl|CDD|237896 PRK15066, PRK15066, inner membrane transport permease; Provisional
MMFQLYWIALKTIVRKEIRRFLRIWVQTLVPPVITMTLYFLIFGNLIGSRIGEMGGFSYMQFIVPGLIMM
SVITNSYSNVASSFFSAKFQRNIEELLVSPVPNHVIILGYVGGGVARGLCVGILVTLISLFFVPLQVHHW
GIVLLTVLLTAILFSLGGLINAVFAKSFDDISIIPTFVLTPLTYLGGVFYSISLLPPFWQGVSKLNPIVY
MVNAFRYGFLGISDVPLWLAFAVLLVFIVVLYLLAWYLLERGRGLRS
>gnl|CDD|237897 PRK15067, PRK15067, ethanolamine ammonia-lyase subunit EutB
MKYKTTLGGRVYQFKDLKEVLAKANPLRSGDQLAGVAAASAEERVAAKMVLADLPLKDFLNNPVIPYEED
EVTRLIIDDHDAAAFAPIKHLTVGELREWLLSDETDEADLAAIAPGLTPEMVAAVSKLMSNQDLILVAKK
IRVVTRFRTTIGLPGTLSARLQPNHPTDDPDGIAASILDGLSYGVGDAVIGINPATDSVENVSRLLHMLD
EVIQRFEIPTQSCVLAHVTTQIEAIERGAPVDLVFQSIAGTEKANKSFGISLALLDEAREAALSLGRGTV
GPNVMYFETGQGSALSAGAHHGVDQQTLEARAYGVARHFDPLLVNTVVGFIGPEYLYDGKQIIRAGLEDH
FMGKLLGLPMGCDICYTNHAEADQDDMDNLLTLLGAAGCNFIMGVPGADDVMLNYQTTSFHDALYLRELL
GLRPAPEFEAWLEKMGIADANGRLTKRAGDPSLFFYALRAA
>gnl|CDD|237898 PRK15068, PRK15068, tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB
MIDFSNFYQLIAKNPLSHWLETLPAQLAAWQREQLHGDFKKWEKALEQLPELTPDRLDLLDSVTIGSEEP
LSEGQRKRIENLLRALMPWRKGPFSLFGIHIDTEWRSDWKWDRVLPHLSPLKGRTVLDVGCGNGYHMWRM
LGAGAKLVVGIDPSQLFLCQFEAVRKLLGNDQRAHLLPLGIEQLPALKAFDTVFSMGVLYHRRSPLDHLK
QLKDQLVPGGELVLETLVIDGDENTVLVPGDRYAKMRNVYFIPSVPALKNWLERAGFKDVRIVDVSVTTT
EEQRKTEWMTTESLADFLDPNDPSKTIEGYPAPKRAVLIARK
>gnl|CDD|185029 PRK15069, PRK15069, histidine ABC transporter permease HisM
MIEILQEYWKALLWTDGYRFTGLAITLWLLVASVVIGFVLAVPLAIARVSSNKWIRFPVWLYTYVFRGTP
LYVQLLVFYTGMYSLEIVRGTDLLDAFFRSGLNCTILAFTLNTCAYTTEIFAGAIRSVPHGEIEAARAYG
MSTFKLYRRIILPSALRRALPAYSNEVILMLHATTLAFTATVPDILKIARDINSATYQPFQAFGIAAVLY
LIISFVLISLFRRAERRWLAHLKP
>gnl|CDD|237899 PRK15070, PRK15070, phosphate propanoyltransferase
MDRELLEKIVREVVKEMLSAREREIPVGVSNRHVHLSQEDLEILFGPGYELTPKKDLSQPGQYAAEETVT
LVGPKGVIENVRILGPLRKKTQVEISRTDAFKLGIKAPVRMSGDLEGTPGITLVGPKGEVELEEGVIVAK
RHIHMSPEDAEKFGVKDGDIVSVKVEGERGLIFDNVLVRVSPDFALEMHIDTDEANAAGLKNGDKVKIIK
K
>gnl|CDD|237901 PRK15072, PRK15072, D-galactonate dehydratase family protein
MKIVDAEVIVTCPGRNFVTLKITTDDGVTGLGDATLNGRELAVASYLQDHVCPLLIGRDAHRIEDIWQYL
YRGAYWRRGPVTMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYGHANGRDIDELLDDVARHLE
LGYKAIRVQCGVPGLKTTYGVSKGKGLAYEPATKGLLPEEELWSTEKYLRFVPKLFEAVRNKFGFDLHLL
HDVHHRLTPIEAARLGKSLEPYRLFWLEDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQL
IDYIRTTVTHAGGITHLRRIADFAALYQVRTGSHGPTDLSPVCMAAALHFDLWVPNFGIQEYMGHSEETL
EVFPHSYTFEDGYLHPGDAPGLGVDFDEKLAAKYPYEPAYLPVARLEDGTMWNW
>gnl|CDD|185033 PRK15074, PRK15074, inosine/guanosine kinase; Provisional
MKFPGQRKSKHYFPVNARDPLLQQIQPENETSRTYIVGIDQTLVDIEAKVDDEFLERYGLSKGHSLVIED
DVAEALYQELKQNNLITHEFAGGTIGNTLHNYSVLADDRSVLLGVMSSNIEIGSYAYRYLCNTSSRTDLN
YLQGVDGPIGRCFTLISEDGERTFAISPGHMNQLRPESIPEDVIAGASALVLTAYLVRCKPGEPMPEATM
KAIEYAKKHNVPVVLTLGTKFVIEDNPQWWQEFLKEHVSILAMNEDEAEALTGESDPLLASDKALDWVDL
VLCTAGPIGLYMAGYTEDEAKRETQHPLLPGAIAEFNRYEFSRAMRKKDCQNPLRVYSHIAPYMGGPEKI
MNTNGAGDGALSALLHDITANSYHRSNVPNSSKHKRTYLTYSSLAQVCKYANRVSYEVLNQHSPRLSRGL
PEREDSLEESYWER
>gnl|CDD|237902 PRK15075, PRK15075, tricarballylate/proton symporter TcuC
MSTMTPAASRESKARAILRVTSGNFLEMFDFFLFGFYATAIAKTFFPAGNEFASLMLTFAVFGAGFLMRP
LGAIVLGAYIDRVGRRKGLIVTLSIMASGTLLIAFVPGYATIGLAAPLLVLLGRLLQGFSAGVELGGVSV
YLAEIATPGRKGFYTSWQSASQQVAVVFAALLGYLLNQWLSPAQMAEWGWRIPFLIGCLIVPFIFLIRRS
LEETEEFLARKHRPSMREIFRSLAANWRIVLAGMLMVAMTTVSFYLITVYTPTFGKTVLHLSAADSLLVT
LCVGVSNFIWLPIGGALSDRIGRRPVLIAFTVLAILTAYPALSWLVAAPSFARMLAVELWLSFLYGSYNG
AMVVALTEVMPAEVRTAGFSLAYSLATAIFGGFTPAISTWLIHVTGDKAAPGYWLSFAAVCGLIATLVLY
RRRGARLQAAEAAA
>gnl|CDD|185035 PRK15076, PRK15076, alpha-galactosidase; Provisional
MPKITFIGAGSTVFTKNLLGDILSVPALRDAEIALMDIDPERLEESEIVARKLAESLGASAKITATTDRR
EALQGADYVINAIQVGGYEPCTVTDFEIPKKYGLRQTIGDTLGIGGIMRALRTIPVLLDICEDMEEVCPD
ALLLNYVNPMAMNTWAMNRYPGIKTVGLCHSVQGTAEQLARDLGVPPEELRYRCAGINHMAWYLELERKG
EDLYPELRAAAAEGQTRCQDKVRYEMLKRFGYFVTESSEHFAEYVPWFIKPGRPDLIERFNIPLDEYPRR
CEEQIANWEKEREELANAERIEIKRSREYASTIIEAIETGEPSVIYGNVRNNGLIDNLPQGCCVEVPCLV
DRNGIQPTKVGDLPPQLAALNRTNINVQELTVEAALTGDRDHVYHAAMLDPHTAAVLSLDEIWALVDELI
AAHGDWLPEYL
>gnl|CDD|237903 PRK15078, PRK15078, polysaccharide export protein Wza; Provisional
MMKSKMKLMPLLLSVTLLSGCTVLPGSNLSTSGKDVIEQQDADFDLDKMVNVYPLTPRLIDQLRPRPNVA
QPNPELEQEIANYEYRVGPGDVLNVTVWDHPELTTPAGQYRSASDTGNWVHADGTIFYPYIGKVHVAGKT
VTEIRSDITGRLAKYIESPQVDVNIAAFRSQKAYVTGEVNKSGQQAITNVPLTILDAINAAGGLTDDADW
RNVVLTHNGKEERISLQALMQNGDLSQNRLLYPGDILYVPRNDDLKVFVMGEVKKQSTLKMDRSGMTLTE
ALGNAEGIDQTTADATGIFVIRPLKGEGGRNGKIANIYQLDASDATALVMGTEFRLQPYDIVYVTTAPVA
RWNRVISQLVPTISGVNDLTETALRIRNW
>gnl|CDD|185037 PRK15079, PRK15079, oligopeptide ABC transporter ATP-binding protein OppF; Provisional
VTEGKKVLLEVADLKVHFDIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGL
VKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDR
VKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRE
MGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIQL
LEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGSFRHAVSCLKVDPL
>gnl|CDD|237904 PRK15080, PRK15080, ethanolamine utilization protein EutJ; Provisional
EWANPRLQKFAALINKTPVATESPLKVGVDLGTANIVLAVLDEDGQPVAGALEWADVVRDGIVVDFIGAV
TIVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNGAVV
DIGGGTTGISILKDGKVVYSADEPTGGTHMSLVLAGAYGISFEEAEQYKRDPKHHKEIFPVVKPVVEKMA
SIVARHIEGQDVEDIYLVGGTCCLPGFEEVFEKQTGLPVHKPQHPLFVTPLGIALSC
>gnl|CDD|185039 PRK15081, PRK15081, glutathione ABC transporter permease GsiC; Provisional
MLNYVIKRLLGLIPTLLIVAVLVFLFVHLLPGDPARLAAGPEADAQVVALVRQQLGLDQPLPHQFWHYIS
NALQGDFGTSMVSRRPVSEEIASRFMPTLWLTITSMVWAVIFGMAIGIASAVWRNRWPDRLGMTLAVSGI
SFPAFALGMLLMQVFSVELGWLPTVGADSWQHYILPSLTLGAAVAAVMARFTRASFVEVLSEDYMRTARA
KGVSETWVVLKHGLRNAMIPVVTMMGLQFGFLLGGSIVVEKVFNWPGLGRLLVDSVEMRDYPVIQAEVLL
FSLEFILINLVVDVLYAAINPAIRYK
>gnl|CDD|185040 PRK15082, PRK15082, glutathione ABC transporter permease GsiD; Provisional
LFNWRRQAVLNAMPLVKPDQVRTPWHEFWRRFRRQHVALVAGLFVLLLIVVAIFAPWIAPYDAENYFDYD
ALNAGPSLQHWFGVDSLGRDIFSRILVGARISLAAGFFSVAIGAAIGTVLGLLAGYYEGWWDRIIMRICD
VLFAFPGILLAIAVVAILGSGMANVIIAVAIFSIPAFARLVRGNTLVLKQQTYIESARSIGASDWTILLR
HILPGTVSSIVVYFTMRIGTSIITAASLSFLGLGAQPPTPEWGAMLNEARADMVIAPHVALFPSLAIFLT
VLAFNLLGDGLRDALDPKIKG
>gnl|CDD|237905 PRK15083, PRK15083, PTS system mannitol-specific transporter subunit IICBA; Provisional
MMSSDIKIKVQSFGRFLSNMVMPNIGAFIAWGIITALFIPTGWLPNETLAKLVGPMITYLLPLLIGYTGG
KLVGGERGGVVGAITTMGVIVGADMPMFLGAMIAGPLGGWAIKHFDRWVDGKIKSGFEMLVNNFSAGIIG
MILAILAFLGIGPAVEVLSKMLAAGVNFMVVHDLLPLTSIFVEPAKILFLNNAINHGIFSPLGIQQSHEL
GKSIFFLIEANPGPGMGVLLAYMFFGRGSAKQSAGGAAIIHFFGGIHEIYFPYVLMNPRLILAVILGGMT
GVFTLTLLNGGLVSPASPGSILAVLAMTPKGAYFANIASVAAAMAVSFVVSAILLKTSKVKEEDDLEAAT
RRMQDMKAESKGASPLAAGDVTNDLSHVRKIIVACDAGMGSSAMGAGVLRKKVQDAGLSQISVTNSAINN
LPPDVDLVITHRDLTERAMRQVPQAQHISLTNFLDSGLYTSLTERLVAAQRHTENEEKVKDSLKDSFEDS
SANLFKLGAENIFLGLKAATKEEAIRFAGEQLVKGGYVEPEYVDAMLDREKLTSTYLGESIAVPHGTVEA
KDRVLKTGVVFCQYPEGVRFGEEEDDIARLVIGIAARNNEHIQVITSLTNALDDESVIERLAHTTSVDEV
LELLAGKKA
>gnl|CDD|185042 PRK15084, PRK15084, formate hydrogenlyase maturation protein HycH; Provisional
MSGKVVFYQLSRKFVDENDATPEEAQQVMYYSLAIGHHVGVIDCLEAALTCPLDEYLAWIATLEEGEARR
KMEGVPKFGEIVIDSSHVALLARAFDEAAAAQTSQQQEWSTQLLSLLHDIHQEPAIYLMVRRL
>gnl|CDD|237906 PRK15086, PRK15086, ethanolamine utilization protein EutH; Provisional
MGINEIIIYIMMFFMLIGAIDRIIGNKFEGLGEQFEEGIMAMGPLALAMVGIMALAPVLAHVLGPVIIPI
YEALGADPSMFATTLLAVDMGGYQLAKELAGDPEAWLFSGLILGSMMGATIVFTIPVALGIIEKEDRKYL
ALGVLAGIITIPIGCLIGGLVAGFDFALILRNLIPVIIFAILLALGLKFIPEKMIKGFLIFGKFIVALIT
IGLAAAIVQSLTGWKLIPGFDPIKFEAIEIVGSIAIVLAGAFPMVYLITKVFKKPLMKVGKLLGMNEVAA
AGMVATLANNIPMFGMMKDMDPRGKVINVAFAVSAAFVLGDHLGFTAGVQPTMIFPMIVGKLIGGITAIG
VAILLSVKKAAALEKTEAEAQS
>gnl|CDD|185044 PRK15087, PRK15087, hemolysin; Provisional
MVQKPLITQGYSLAEEIANSISHGIGLVFGIVGLVLLLVQAVDANADATAITSYSLYGGSMILLFLASTL
YHAIPHQRAKRWLKKFDHCAIYLLIAGTYTPFLLVGLDSPLARGLMIVIWSLALLGILFKLAFAHRFKVL
SLVTYLAMGWLSLIVIYQLAIKLAIGGVTLLAVGGVVYSLGVIFYVCKRIPYNHAIWHGFVLGGSVCHFL
AIYLYVGQA
>gnl|CDD|185045 PRK15088, PRK15088, PTS system mannose-specific transporter subunits IIAB; Provisional
MTIAIIIGTHGWAAEQLLKTAEMLLGEQENVAWIDFVPGENAETLIEKYNAQLAKLDTSKGVLFLVDTWG
GSPFNAASRIVVDKENYEVITGVNIPMLVETFMARDDDPSFDELVAIALETGREGVKALKAKPVEKAAPA
PAAAAPAPAAATPAKPMGPNDHMVIGLARIDDRLIHGQVATRWTKETNVSRIIVVSDEVAADTVRKTLLT
QVAPPGVTAHVVDVAKMIRVYNNPKYAGERVMLLFTNPTDVERLVEGGVKITSVNIGGMAFRQGKTQVNN
AVSVDEKDIEAFKKLNARGIELEVRKVSSDPKLKMMDLISKI
>gnl|CDD|185046 PRK15090, PRK15090, DNA-binding transcriptional regulator KdgR; Provisional
ADLDKQPDSVSSVLKVFGILQALGEEREIGITELSQRVMMSKSTVYRFLQTMKTLGYVAQEGESEKYSLT
LKLFELGAKALQNVDLIRSADIQMREISRLTKETIHLGALDEDSIVYIHKIDSMYNLRMYSRIGRRNPLY
STAIGKVLLAWRDRDEVREILSGVEFKRSTEKTITSTEALLPVLDQVREQGYGEDNEEQEEGLRCIAVPV
FDRFGVVIAGLSISFPTLRFSEERKQEYVAMLHTAARKISEQMGYHD
>gnl|CDD|185047 PRK15091, PRK15091, phospholipid-binding lipoprotein MlaA
MKLRLSGLALGSTLLVGCASSGTDQQGRSDPLEGFNRTMFNFNYNVLDPYVVRPVAVAWRDYVPQPARNG
LSNFTGNLEEPASMVNYFLQGDPYQGMVHFTRFFLNTLLGMGGLIDVAGMANPKLAKEEPHRFGSTLGHY
GVGYGPYVQLPGYGSFTLREDGGDMADTLYPVLSWLTWWMSAGKWTLEGIETRAQLLDSDGLLRNSSDPY
IMVREAYFQRHDFLANGGKLKPQENPNAQAIQDDLKDIDSE
>gnl|CDD|237907 PRK15092, PRK15092, DNA-binding transcriptional repressor LrhA; Provisional
MINANRPIINLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEH
GIQLLGYARKILRFNDEACSSLMYSNLQGVLTIGASDDTADTILPFLLNRVSSVYPKLALDVRVKRNAFM
MEMLESQEVDLAVTTHRPSSFPALNLRTSPTLWYCAAEYVLQKGEPIPLVLLDEPSPFRDMALATLNAAG
IPWRIAYVASTLSAVRAAVKAGLGVTARPVEMMSPDLRVLGESEGLPPLPDTEYLLCRDPNSNNELAQVI
FQAMESYHNPWQYSPLSAEEGDDSLLIERD
>gnl|CDD|185049 PRK15093, PRK15093, peptide ABC transporter ATP-binding protein SapD
MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRF
DDIDLLRLSPRERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRWWQRFGWRKRRAIELL
HRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNT
TILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALIRAIPDFGSAMPHKSRLNTLPG
AIPLLEHLPIGCRLGPRCPYAQRECIETPRLTGAKNHLYACHFPLNMEEE
>gnl|CDD|185050 PRK15094, PRK15094, magnesium/cobalt transporter CorC
MSDDNSHSSDTPSPKKGFFSLLLSQLFHGEPKNRDELLALIRDSEQNDLIDEDTRDMLEGVMDIADQRVR
DIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLR
QAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRH
TWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVK
IPDDSPQPKLDE
>gnl|CDD|237908 PRK15095, PRK15095, FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
MSESVQSNSAVLVHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAA
FGVPSPDLIQYFSRRDFMDAGEPEIGAIMLFTAMDGSEMPGVIREINGDSITVDFNHPLAGQTVHFDIEV
LEIDPALEAVHADIAG
>gnl|CDD|185052 PRK15097, PRK15097, cytochrome bd-I ubiquinol oxidase subunit CydA
MLDIVELSRLQFALTAMYHFLFVPLTLGMAFLLAIMETVYVLSGKQIYKDMTKFWGKLFGINFALGVATG
LTMEFQFGTNWSYYSHYVGDIFGAPLAIEGLMAFFLESTFVGLFFFGWDRLGKVQHMCVTWLVALGSNLS
ALWILVANGWMQNPIASDFNFETMRMEMVSFSELVLNPVAQVKFVHTVASGYVTGAMFILGISAYYMLKG
RDFAFAKRSFAIAASFGMAAVLSVIVLGDESGYEMGDVQKTKLAAIEAEWETQPAPAAFTLFGIPDQETM
ENKFAIQIPYALGIIATRSVDTPVIGLKDLMVQHEERIRNGMKAYSLLEQLRSGSTDQAVRDQFNSMKKD
LGYGLLLKRYTPNVADATEAQIQQATKDSIPRVAPLYFAFRIMVACGFLMLAIIALSFWSVIRNRIGEKK
WLLRAALYGIPLPWIAVEAGWFVAEYGRQPWAIGEVLPTAVANSSLTAGDLLFSMVLICGLYTLFLVAEL
FLMFKFARLGPSSLKTGRYHFEQSTTTTQPAR
>gnl|CDD|185053 PRK15098, PRK15098, beta-glucosidase BglX
MKWLCSVGLAVSLALQPALADDLFGNHPLTPEARDAFVTDLLKKMTLDEKIGQLRLISVGPDNPKEAIRE
MIKAGQVGAIFNTVTRQDIRAMQDQVMQLSRLKIPLFFAYDVVHGQRTVFPISLGLASSWDLDAVATVGR
VSAYEAADDGLNMTWAPMVDISRDPRWGRASEGFGEDTYLTSIMGKTMVKAMQGKSPADRYSVMTSVKHF
ALYGAVEGGRDYNTVDMSPQRMFNDYLPPYKAGLDAGSGGVMVALNSLNGTPATSDSWLLKDLLRDQWGF
KGITVSDHGAIKELIKHGVAADPEDAVRLALKSGIDMSMSDEYYSKYLPGLVKSGKVTMAELDDAVRHVL
NVKYDMGLFNDPYSHLGPKESDPVDTNAESRLHRKEAREVARESLVLLKNRLETLPLKKSGTIAVVGPLA
DSQRDVMGSWSAAGVADQSVTVLQGIKNAVGDKAKVLYAKGANVTDDKGIIDFLNQYEEAVKVDPRSPQA
MIDEAVQAAKQADVVVAVVGEAQGMAHEASSRTDITIPQSQRDLIAALKATGKPLVLVLMNGRPLALVKE
DQQADAILETWFAGTEGGNAIADVLFGDYNPSGKLPMSFPRSVGQIPVYYNHLNTGRPYNPDKPNKYTSR
YFDEANGPLYPFGYGLSYTTFTVSDVKLSSPTMKRDGKVTASVTVTNTGKREGATVVQLYLQDVTASMSR
PVKELKGFEKIMLKPGETQTVSFPIDIEALKFWNQQMKYVAEPGKFNVFIGLDSARVKQGSFELL
>gnl|CDD|185054 PRK15099, PRK15099, lipid III flippase WzxE
MSLAKASLWTAASTLVKIGAGLLVVKLLAVSFGPAGVGQAGNFRQLITVLGVLAGAGIFNGVTKYVAQYH
DQPQQLRAVVGTSSAMVLGFSTLLALVFLLAAAPISQGLFGHTDYQGVVRAVALIQMGIAWANLLLAILK
GFRDAAGNALSLIVGSLIGVAAYYLCYRLGGYEGALLGLALVPALVVLPAGIMLIRRGTIPLSYLKPSWD
NGLAGQLGKFTLMALITSVTLPVAYVMMRNLLAAHYSWDEVGIWQGVSSISDAYLQFITASFSVYLLPTL
SRLTEKRDITREIVKALKFVLPAVAAASFTVWLLRDFAIWLLFSNKFTAMRDLFAWQLVGDVLKVGAYVF
GYLVIAKASLRFYILAEVSQFTLLTGFAHWLIPLHGALGAAQAYMATYIVYFSLCCGVFLLYRRRA
>gnl|CDD|185055 PRK15100, PRK15100, cystine ABC transporter permease
MQESIQLVIDSAPFLLKGAGYTLQLSIGGMFFGLLLGFILALMRLSPIWPVRWLARFYVSIFRGTPLIAQ
LFMIYYGLPQFGIELDPIPAAMIGLSLNTAAYAAETLRAAISSIDKGQWEAAASIGMTRWQTLRRAILPQ
AARTALPPLSNSFISLVKDTSLAATIQVPELFRQAQLITSRTLEVFTMYLAASLIYWIMATVLSALQNRF
ENQLNRQERE
>gnl|CDD|185056 PRK15101, PRK15101, protease3; Provisional
MPRSTWFKALLLLLALWAPLSQAETGWQPLQETIRKSEKDPRQYQAIRLDNGMTVLLVSDPQAVKSLAAL
ALPVGSLEDPDAQQGLAHYLEHMVLMGSKKYPQPDSLAEFLKKHGGSHNASTASYRTAFYLEVENDALPP
AVDRLADAIAEPLLDPKNADRERNAVNAELTMARSRDGMRMAQVSAETINPAHPGSRFSGGNLETLSDKP
GSKLQDALVDFYQRYYSANLMKAVIYSNQPLPELAKLAADTFGRVPNKNASVPEITVPVVTDAQKGIIIH
YVPAQPRKVLRVEFRIDNNSAKFRSKTDEYISYLIGNRSPGTLSDWLQKQGLAEGISAGADPMVDRNSGV
FAISVSLTDKGLAQRDQVVAAIFSYLNLLREKGIDKSYFDELAHVLDLDFRYPSITRDMDYIEWLADTML
RVPVEHTLDAPYIADRYDPKAIKARLAEMTPQNARIWYISPQEPHNKTAYFVDAPYQVDKISEQTFADWQ
QKAQNIALSLPELNPYIPDDFSLIKADKAYKHPELIVDEPGLRVVYMPSQYFADEPKADISLVLRNPKAM
DSARNQVLFALNDYLAGLALDQLSNQASVGGISFSTNANNGLMVNANGYTQRLPQLLQALLEGYFSFTPT
EEQLAQAKSWYREQLDSAEKGKAYEQAIMPAQMLSQVPYFERDERRKLLPSITLKDVLAYRDALLSGATP
EFLVVGNLTEEQVTTLARDVQKQLGADGTEWWRGKDVVVDKKQSVNFEKAGSSTDSALAAVYVPTGYDEY
QSSAYSSLLGQIIQPWFYNQLRTEEQLGYAVFAFPMSVGRQWGMGFLLQSNDKQPAYLWQRYQAFFPQAE
AKLRAMKPEEFAQYQQALINQLLQAPQTLGEEASRLSKDFDRGNMRFDSRDKIIAQIKLLTPQKLADFFH
QAVIEPQGLAILSQISGSQNGKADYAHPKGWKTWENVSALQQTLPVMEKNE
>gnl|CDD|237909 PRK15102, PRK15102, trimethylamine-N-oxide reductase TorA
ASRRRFLKGLGGLSAAGMLGPSLLTPRSALAAQAAAAETTKEWILTGSHWGAFRAKVKNGRFVEAKPFEL
DKYPTKMINGIKGHVYNPSRIRYPMVRLDWLRKRHKSDTSQRGDNRFVRVSWDEALDLFYEELERVQKTY
GPSALHTGQTGWQSTGQFHSATGHMQRAIGMHGNSVGTVGDYSTGAGQVILPYVLGSTEVYEQGTSWPLI
LENSKTIVLWGSDPVKNLQVGWNCETHESYAYLAQLKEKVAKGEINVISIDPVVTKTQNYLGCEHLYVNP
QTDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFLPYLLGEKDGVPKTPEWAEKICGIDAETIRELARQ
MAKGRTQIIAGWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGGISYGHHYSGIGVPSSGGAIPGGFPGNL
DTGQKPKHDNSDYKGYSSTIPVARFIDAILEPGKTINWNGKKVTLPPLKMMIFSGTNPWHRHQDRNRMKE
AFRKLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNRGIIAMKKVVEPLFESRSDFDIFRE
LCRRFGREKEYTRGMDEMGWLKRLYQECKQQNKGKFHMPEFDEFWKKGYVEFGEGQPWVRHADFREDPEL
NPLGTPSGLIEIYSRKIADMGYDDCQGHPMWFEKIERSHGGPGSDKYPLWLQSVHPDKRLHSQLCESEEL
RETYTVQGREPVYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGAWYGPDKGGEI
GALCTYGDPNTLTLDIGTSQLAQATSAHTCLVEIEKYQGKVPPVTSFNGPVEVVA
>gnl|CDD|237910 PRK15103, PRK15103, membrane integrity-associated transporter subunit PqiA
MCEHHHAAKHILCPQCDMLVALPRLEHGQKAACPRCGTTLTVRWDEPRQRPTAYALSALFMLLLANLFPF
VNMNVAGITSEITLLEIPGVMFSEDYASLATFFLLFVQLVPAFCMVTILLLVNRAPLPVRLKEQLARVLF
QLKTWGMAEIFLAGVLVSFVKLMAYGDIGIGSSFIPWCLFCLLQLRAFQCVDRRWLWDDIAPMPALPQPL
KPGVTGLRQGLRSCSCCTAILPADQPVCPRCHTKGYVRRRNSLQWTLALLVTSIMLYIPANILPIMVTEL
LGSKMPSTIMAGVILLWSEGSYPVALVIFIASIMVPTLKMIAIAWLCWDAKGHGKRDSERMHLIYEVVEF
VGRWSMIDVFVIAVLSALVRMGGLMSIYPAIGALLFALVVILTMFSAMTFDPRLSWDREPESEHEESQG
>gnl|CDD|185059 PRK15104, PRK15104, oligopeptide ABC transporter substrate-binding protein OppA; Provisional
MTNITKKSLIAAGVLAALMAGNVALAADVPAGVQLAEKQTLVRNNGSEVQSLDPHKIEGVPESNISRDLF
EGLLISDPDGHPAPGVAESWDNKDFKVWTFHLRKDAKWSNGTPVTAQDFVYSWQRLADPKTASPYASYLQ
YGHIANIDDIIAGKKPPTDLGVKAIDDHTLEVTLSEPVPYFYKLLVHPSMSPVPKAAVEKFGEKWTQPAN
IVTNGAYKLKDWVVNERIVLERNPTYWDNAKTVINQVTYLPISSEVTDVNRYRSGEIDMTYNNMPIELFQ
KLKKEIPDEVHVDPYLCTYYYEINNQKPPFNDVRVRTALKLGLDRDIIVNKVKNQGDLPAYGYTPPYTDG
AKLTQPEWFGWSQEKRNEEAKKLLAEAGYTADKPLTFNLLYNTSDLHKKLAIAAASIWKKNLGVNVKLEN
QEWKTFLDTRHQGTFDVARAGWCADYNEPTSFLNTMLSNSSNNTAHYKSPAFDKLMAETLKVKDEAQRAA
LYQKAEQQLDKDSAIVPVYYYVNARLVKPWVGGYTGKDPLDNIYVKNLYIIKH
>gnl|CDD|185060 PRK15105, PRK15105, peptidoglycan synthase FtsI; Provisional
KAAAKTQKLKRQEEQANFISWRFALLCGCILLALVFLLGRVAWLQVINPDMLVREGDMRSLRVQEVSTSR
GMITDRSGRPLAVSVPVKAIWADPKEVHDAGGISVDDRWKALADALNIPLDQLSARINANPKGRFIYLAR
QVNPDMADYIKKLKLPGIHLREESRRYYPSGEVTAHLIGFTNVDSQGIEGVEKSFDKWLTGQPGERIVRK
DRYGRVIEDISSTDSQAAHNLALSIDERLQALVYRELNNAVAFNKAESGSAVLVDVNTGEVLAMANSPSY
NPNNLSGTPKDAMRNRAITDVFEPGSTVKPMVVMTALQRGVVKENSVLNTVPYRINGHEIKDVARYSELT
LTGVLQKSSNVGVSKLALAMPSSALVDTYSRFGLGKATNLGLVGERSGLYPQKQRWSDIERATFSFGYGL
MVTPLQLARVYATIGSYGIYRPLSITKVDPPVPGERVFPESIVRTVVHMMESVALPGGGGVKAAIKGYRI
AIKTGTAKKVGPDGRYINKYIAYTAGVAPASQPRFALVVVINDPQAGKYYGGAVSAPVFGAIMGGVLRTM
NIEPDALPTGDKNEFVIN
>gnl|CDD|237911 PRK15106, PRK15106, nucleoside-specific channel-forming protein Tsx; Provisional
MKKTLLAAGAVLALSSSFTVNAAENDKPQYLSDWWHQSVNVVGSYHTRFGPQLNNDTYLEYEAFAKKDWF
DFYGYVDAPKFFGVGNSNDKGIWDHGSPLFMEIEPRFSIDKLTGTDLSFGPFKEWYFANNYIYDMGRNKD
SRQSTWYMGLGTDIDTGLPMSLSLNVYAKYQWQNYGAANENEWDGYRFKVKYFVPITDLWGGSLSYIGFT
NFDWGSDLGDDSGKTRTNNSIASSHILALNYDHWHYSVVARYFHNGGQWNDGAELNFGNGNFNVRSTGWG
YYLVVGYNF
>gnl|CDD|185062 PRK15107, PRK15107, glutamate/aspartate ABC transporter permease GltK
MYEFDWSSIVPSLPYLLDGLVITLKITVTAVVIGILWGTILAVMRLSSFKPVAWFAKAYVNVFRSIPLVM
VLLWFYLIVPGFLQNVLGLSPKTDIRLISAMVAFSMFEAAYYSEIIRAGIQSISRGQSSAALALGMTHWQ
SMKLIILPQAFRAMVPLLLTQGIVLFQDTSLVYVLSLADFFRTASTIGERDGTQVEMILFAGFVYFVISL
SASLLVSYLKKRTV
>gnl|CDD|185064 PRK15109, PRK15109, antimicrobial peptide ABC transporter periplasmic binding protein SapA; Provisional
MRLVLSSLLVIAGLLSGQAIAAPESPPHADIRQSGFVYCVSGQVNTFNPQKASSGLIVDTLAAQLYDRLL
DVDPYTYRLMPELAESWEVLDNGATYRFHLRRDVPFQKTDWFTPTRKMNADDVVFSFQRIFDRNHPWHNV
NGGNYPYFDSLQFADNVKSVRKLDNYTVEFRLAQPDASFLWHLATHYASVLSAEYAAKLTKEDRQEQLDR
QPVGTGPFQLSEYRAGQFIRLQRHDDYWRGKPLMPQVVVDLGSGGTGRLSKLLTGECDVLAYPAASQLSI
LRDDPRLRLTLRPGMNIAYLAFNTRKPPLNNPAVRHALALAINNQRLMQSIYYGTAETAASILPRASWAY
DNEAKITEYNPEKSREQLKALGLENLTLKLWVPTASQAWNPSPLKTAELIQADLAQVGVKVVIVPVEGRF
QEARLMDMNHDLTLSGWATDSNDPDSFFRPLLSCAAIRSQTNYAHWCDPAFDSVLRKALSSQQLASRIEA
YDEAQSILAQELPILPLASSLRLQAYRYDIKGLVLSPFGNASFAGVYREKQEEVKKP
>gnl|CDD|185065 PRK15110, PRK15110, peptide ABC transporter permease SapB
MIIFTLRRLLLLIVTLFLLTLVGFSLSYFTPHAPLQGASLWDAWVFWFNGLLHWDFGVSSINGQPISEQL
KEVFPATMELCILAFGFALLVGIPVGIIAGVTRHKWQDNLISALALLGFSIPVFWLALLLTLFFSLTLGW
LPVSGRFDLLYEVKPVTGFALIDAWLSDSPWRDEMIMSAIRHMILPVITLAVAPTTEVIRLMRISTIEVY
DQNYVKAAATRGLSRFTILRRHVLHNALPPVIPRLGLQFSTMLTLAMITEMVFSWPGLGRWLINAIRQQD
YAAISAGVMVVGSLVIIVNVLSDILGAMANPLKHKEWYALR
>gnl|CDD|185066 PRK15111, PRK15111, peptide ABC transporter permease SapC
MPYDSVYSEKRPPGTLRTAWRKFYSDALAMVGLYGCAGLALLCLFGGWLAPYGIDQQFLGYQLLPPSWSR
YGEVSFFLGTDDLGRDVLSRLLSGAAPTVGGAFVVTLAATLCGLVLGVFAGATHGLRSAVLNHILDTLLS
IPSLLLAIIVVAFAGPSLSHAMFAVWLALLPRMVRSIYSAVHDELEKEYVIAARLDGASTLNILWYAVLP
NITAGLVTEITRALSMAILDIAALGFLDLGAQLPSPEWGAMLGDSLELIYVAPWTVMLPGAAIMLSVLLV
NLLGDGIRRAIIAGVE
>gnl|CDD|185067 PRK15112, PRK15112, peptide ABC transporter ATP-binding protein SapF
VETLLEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL
LIDDHPLHFGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLP
DHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHL
GMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAGHFGEALTADAWRKDR
>gnl|CDD|185068 PRK15113, PRK15113, glutathione transferase
MSKPAITLYSDAHFFSPYVMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFELS
ESSAIAEYLEERFAPPAWERIYPADLQARARARQIQAWLRSDLMPLREERPTDVVFAGAKKAPLSEAGKA
AAEKLFAVAERLLAPGQPNLFGEWCIADTDLALMLNRLVLHGDEVPERLADYATFQWQRASVQRWLALSA
KRSG
>gnl|CDD|185069 PRK15114, PRK15114, tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ; Provisional
MLQNIRIVLVETSHTGNMGSVARAMKTMGLTNLWLVNPLVKPDSQAIALAAGASDVIGNATIVDTLDEAL
AGCSLVVGTSARSRTLPWPMLDPRECGLKSVAEAANAPVALVFGRERVGLTNDELQKCHYHVAIAANPEY
SSLNLAMAVQVIAYEVRMAWLATQENGEPQVEHEETPYPLVDDLERFYGHLEQTLLATGFIRENHPGQVM
NKLRRLFTRARPESQELNILRGILASIEQQNKGNK
>gnl|CDD|185070 PRK15115, PRK15115, response regulator GlrR; Provisional
MSRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAE
IQKVQPGMPVIILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPATDERWREAIVTRS
PLMLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHAR
GAFTGAVSNREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDL
PKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWP
GNVRQLVNVIEQCVALTSSPVISDALVEQALEGENTALPTFVEARNQFELNYLRKLLQITKGNVTHAARM
AGRNRTEFYKLLSRHELDANDFKE
>gnl|CDD|185071 PRK15116, PRK15116, sulfur acceptor protein CsdL; Provisional
MSVVISDAWRQRFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNT
NRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYMSAGFSYVIDAIDSVRPKAALIA
YCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLAAKLRERLKSDFGVVKNSKGKLGVDCVFSTEAL
VYPQADGSVCAMKSTAEGPKRMDCASGFGAATMVTATFGFVAVSHALKKMMAKAARQG
>gnl|CDD|237912 PRK15117, PRK15117, phospholipid-binding protein MlaC
MFKRLLMVALLVIAPLSAATAADQTNPYKLMDEAAQKTFDRLKNEQPKIRANPDYLRTIVDQELLPYVQV
KYAGALVLGRYYKDATPAQREAYFAAFREYLKQAYGQALAMYHGQTYQIAPEQPLGDATIVPIRVTIIDP
NGRPPVRLDFQWRKNSQTGNWQAYDMIAEGVSMITTKQNEWADLLRTKGIDGLTAQLKSIAQQPITLDEK
K
>gnl|CDD|185073 PRK15118, PRK15118, universal stress protein UspA
MAYKHILIAVDLSPESKVLVEKAVSMARPYNAKVSLIHVDVNYSDLYTGLIDVNLGDMQKRISEETHHAL
TELSTNAGYPITETLSGSGDLGQVLVDAIKKYDMDLVVCGHHQDFWSKLMSSARQLINTVHVDMLIVPLR
DEEE
>gnl|CDD|185076 PRK15121, PRK15121, MDR efflux pump AcrAB transcriptional activator RobA
MDQAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTS
RPILDIALQYRFDSQQTFTRAFKKQFAQTPALYRRSPEWSAFGIRPPIRLGEFTLPEHEFVTLPETPLVG
VTQSYSCSLEQISDFRHEMRVQFWRDFLGNAPTIPPVLYGLHETRPSQEKDDEQEVFYTTALEPDQADGY
VQTGHPVMLQGGEYVMFTYEGLGTGLQEFILTVYGTCMPMLNLTRRKGQDIERYYPAEDAKAGDRPINLR
CEYLIPIRR
>gnl|CDD|237914 PRK15122, PRK15122, magnesium-transporting ATPase; Provisional
MIKARRTNRKASEARKNHKKSMRIAREAANSLEETLANLNTHRQGLTEEDAAERLQRYGPNEVAHEKPPH
ALVQLLQAFNNPFIYVLMVLAAISFFTDYWLPLRRGEETDLTGVIIILTMVLLSGLLRFWQEFRSNKAAE
ALKAMVRTTATVLRRGHAGAEPVRREIPMRELVPGDIVHLSAGDMIPADVRLIESRDLFISQAVLTGEAL
PVEKYDTLGAVAGKSADALADDEGSLLDLPNICFMGTNVVSGTATAVVVATGSRTYFGSLAKSIVGTRAQ
TAFDRGVNSVSWLLIRFMLVMVPVVLLINGFTKGDWLEALLFALAVAVGLTPEMLPMIVSSNLAKGAIAM
ARRKVVVKRLNAIQNFGAMDVLCTDKTGTLTQDRIILEHHLDVSGRKDERVLQLAWLNSFHQSGMKNLMD
QAVVAFAEGNPEIVKPAGYRKVDELPFDFVRRRLSVVVEDAQGQHLLICKGAVEEMLAVATHVRDGDTVR
PLDEARRERLLALAEAYNADGFRVLLVATREIPGGESRAQYSTADERDLVIRGFLTFLDPPKESAAPAIA
ALRENGVAVKVLTGDNPIVTAKICREVGLEPGEPLLGTEIEAMDDAALAREVEERTVFAKLTPLQKSRVL
KALQANGHTVGFLGDGINDAPALRDADVGISVDSGADIAKESADIILLEKSLMVLEEGVIKGRETFGNII
KYLNMTASSNFGNVFSVLVASAFIPFLPMLAIHLLLQNLMYDISQLSLPWDKMDKEFLRKPRKWDAKNIG
RFMLWIGPTSSIFDITTFALMWFVFAANSVEMQALFQSGWFIEGLLSQTLVVHMLRTQKIPFIQSTAALP
VLLTTGLIMAIGIYIPFSPLGAMVGLEPLPWSYFPWLAATLLGYCLVAQGMKRFYIRRFGQWF
>gnl|CDD|237915 PRK15123, PRK15123, lipopolysaccharide core heptose(I) kinase RfaP; Provisional
MMLELKEPFATLWRGKDPFEEVKTLQGEVFRELEGRRTLRFELAGKSYFLKWHRGTGWGEIFKNLLSLRM
PVLGADREWRAIHRLHEVGVDTMTGVAFGERGSNPATRTSFIITEDLAPTISLEDYCADWATNPPDPRLK
RMLIKRVATMVRDMHAAGINHRDCYICHFLLHLPFPGREEDLKLSVIDLHRAQIRARVPRRWRDKDLAGL
YFSAMDIGLTQRDILRFLRVYFGRPLRDILKQEAGLLAQAEAKAEKLYERTIRKGLAL
>gnl|CDD|185079 PRK15124, PRK15124, RNA 2',3'-cyclic phosphodiesterase
MSEPKRLFFAIDLPDEIRQQIIHWRATHFPPEAGRPVAAANLHLTLAFLGEVSAEKQQALSQLAGRIRQP
GFTLTLDDAGQWPRSRVVWLGMRQPPRGLLQLANMLRSQAARSGCYQSPQPFHPHITLLRDASRPVAIPP
PGFNWSFPVTEFTLYASSFARGRTRYTPLQRWPLTQ
>gnl|CDD|185080 PRK15126, PRK15126, HMP-PP phosphatase
MARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRV
HSLEGELLHRQDLPADVAELVLHQQWDTRASMHVFNDDGWFTGKEIPALLQAHVYSGFRYQLIDLKRLPA
HGVTKICFCGDHDDLTRLQIQLNEALGERAHLCFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAF
GDAMNDREMLGSVGRGFIMGNAMPQLRAELPHLPVIGHCRNQAVSHYLTHWLDYPHLPYSPE
>gnl|CDD|185081 PRK15127, PRK15127, multidrug efflux RND transporter permease subunit AcrB
MPNFFIDRPIFAWVIAIIIMLAGGLAILKLPVAQYPTIAPPAVTISASYPGADAKTVQDTVTQVIEQNMN
GIDNLMYMSSNSDSTGTVQITLTFESGTDADIAQVQVQNKLQLAMPLLPQEVQQQGVSVEKSSSSFLMVV
GVINTDGTMTQEDISDYVAANMKDPISRTSGVGDVQLFGSQYAMRIWMNPNELNKFQLTPVDVINAIKAQ
NAQVAAGQLGGTPPVKGQQLNASIIAQTRLTSTEEFGKILLKVNQDGSRVRLRDVAKIELGGENYDIIAE
FNGQPASGLGIKLATGANALDTAAAIRAELAKMEPFFPSGLKIVYPYDTTPFVKISIHEVVKTLVEAIIL
VFLVMYLFLQNFRATLIPTIAVPVVLLGTFAVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVM
AEEGLPPKEATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGSTGAIYRQFSITIVSAMALSVLVALILTP
ALCATMLKPIAKGDHGEGKKGFFGWFNRMFEKSTHHYTDSVGNILRSTGRYLVLYLIIVVGMAYLFVRLP
SSFLPDEDQGVFLTMVQLPAGATQERTQKVLNEVTDYYLTKEKNNVESVFAVNGFGFAGRGQNTGIAFVS
LKDWADRPGEENKVEAITMRATRAFSQIKDAMVFAFNLPAIVELGTATGFDFELIDQAGLGHEKLTQARN
QLLGEAAKHPDMLVGVRPNGLEDTPQFKIDIDQEKAQALGVSISDINTTLGAAWGGSYVNDFIDRGRVKK
VYVMSEAKYRMLPDDIGDWYVRAADGQMVPFSAFSSSRWEYGSPRLERYNGLPSMEILGQAAPGKSTGEA
MELMEELASKLPTGVGYDWTGMSYQERLSGNQAPALYAISLIVVFLCLAALYESWSIPFSVMLVVPLGVI
GALLAATFRGLTNDVYFQVGLLTTIGLSAKNAILIVEFAKDLMDKEGKGLIEATLEAVRMRLRPILMTSL
AFILGVMPLVISSGAGSGAQNAVGTGVMGGMVTATVLAIFFVPVFFVVVRRRFSRKNEDIEHSHTVDHH
>gnl|CDD|185082 PRK15128, PRK15128, 23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI
MTVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDP
DESIDIAFFTRRLQQAQKWRDWLAQKDGLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAAL
ISALQTLYPECAIYDRSDVAVRKKEGMELTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRD
SRLATRRYVENKRVLNCFSYTGGFAVSALMGGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDV
FKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGYKDINMLAIQLLNPGGILLTFSCSGLMTSDLFQ
KIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM
>gnl|CDD|185083 PRK15129, PRK15129, L-Ala-D/L-Glu epimerase; Provisional
MRTVKVYEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMAQIMSVVPQLE
KGLTREALQKLLPAGAARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASAL
WQAGAKLLKVKLDNHLISERMVAIRSAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDD
AALENFIHPLPICADESCHTRSSLKALKGRYEMVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTS
RAISAALPLVPQVRFADLDGPTWLAVDVEPALQFTTGELHL
>gnl|CDD|237916 PRK15130, PRK15130, spermidine N1-acetyltransferase; Provisional
MPSAHSVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAG
LVELVEINHVHRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGF
EVEGELIHEFFINGEYRNTIRMCIFQHQYLAEHKTPGQTLLKPTAQ
>gnl|CDD|185085 PRK15131, PRK15131, mannose-6-phosphate isomerase; Provisional
MQKMINSVQNYAWGSKTALTELYGIANPDNQPMAELWMGAHPKSSSRVQDANGDIVSLRDVIESDKSALL
GEAVAKRFGELPFLFKVLCAAQPLSIQVHPNKRAAEIGFAKENAAGIPLDAAERNYKDPNHKPELVFALT
PFLAMNAFREFSEIVSLLQPVAGAHPAIAHFLQQPDAERLSELFASLLNMQGEEKSRALAVLKSALNSQQ
GEPWQTIRLISEFYPDDSGLFSPLLLNVVKLNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPK
YIDIPELVANVKFEAKPANQLLTQPVKQGAELDFPIPVDDFAFSLHDLSDQPTTLSQQSAAILFCVEGEA
VLWKGEQQLTLKPGESAFIAANESPVTVSGHGRLARVYN
>gnl|CDD|185086 PRK15132, PRK15132, tyrosine transporter TyrP; Provisional
MKNRTLGSIFIVAGTTIGAGMLAMPLAAAGVGFSVTLILLIGLWALMCYTALLLLEVYQHVPADTGLGTL
AKRYLGRYGQWLTGFSMMFLMYALTAAYISGAGELLASSISDWTGISMSPTAGVLLFTLVAGGVVCVGTS
SVDLFNRFLFSAKIIFLVVMLALMMPHIHKVNLLTLPLQQGLALSAIPVIFTSFGFHGSVPSIVSYMGGN
IRKLRWVFIIGSAIPLVAYIFWQLATLGSIDSTTFMGLLANHAGLNGLLQALREVVASPHVELAVHLFAD
LALATSFLGVALGLFDYLADLFQRRNTVGGRLQTGLITFLPPLAFALFYPRGFVMALGYAGVALAVLALL
LPSLLVWQSRKQNPQAGYRVKGGRPALALVFLCGIAVIGIQFLIAAGLLPEVG
>gnl|CDD|185087 PRK15133, PRK15133, microcin C ABC transporter permease YejB; Provisional
MGAYLIRRLLLVIPTLWAIITINFFIVQIAPGGPVDQAIAAIEFGQAGGLPGAGGEGVRASHAQTGVGNI
SDSNYRGGRGLDPEVIAEITHRYGFDKPLHERYFKMLWDYIRFDFGDSLFRSASVLTLIKDSLPVSITLG
LWSTLIIYLVSIPLGIRKAVRNGSRFDVWSSAFIIIGYAIPAFLFAILLIVFFAGGSYFDLFPLRGLVSA
NFDSLPWYQKITDYLWHITLPVLATVIGGFAALTMLTKNSFLDEIRKQYVVTARAKGVSEKNILWKHVFR
NAMLLVIAGFPATFISMFFTGSLLIEVMFSLNGLGLLGYEATVSRDYPVMFGTLYIFTLIGLLLNIVSDI
SYTLVDPRIDFEGR
>gnl|CDD|237917 PRK15134, PRK15134, microcin C ABC transporter ATP-binding protein YejF; Provisional
MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGD
IRFHGESLLHASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDR
VGIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGL
LFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNSEPSGDPVPLPEPASPLLDVEQ
LQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLH
NLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRH
RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVR
ALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLALS
>gnl|CDD|185089 PRK15135, PRK15135, histidine ABC transporter permease HisQ
MLYGFSGVILQGALVTLELALSSVVLAVIIGLIGAGGKLSQNRLLGLIFEGYTTLIRGVPDLVLMLLIFY
GLQIALNSVTEALGVGQIDIDPMVAGIITLGFIYGAYFTETFRGAFMAVPKGHIEAATAFGFTRGQVFRR
IMFPAMMRYALPGIGNNWQVILKATALVSLLGLEDVVKATQLAGKSTWEPFYFAIVCGVIYLVFTTVSNG
VLLWLERRYSVGVKRADL
>gnl|CDD|185090 PRK15136, PRK15136, multidrug efflux MFS transporter periplasmic adaptor subunit EmrA
MSANAETQTPQQPVKKKGKRKRALLLLTLLFIIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSG
SVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSVRQTHQLMINSKQYQANIELQKTALAQAQ
SDLNRRVPLGNANLIGREELQHARDAVASAQAQLDVAIQQYNANQAMILNTPLEDQPAVQQAATEVRNAW
LALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYG
DDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQHPLRIGLSTLVTVDTANR
DGQVLANQVRSTPAYESNALEIDLAPVNKLIDDIIQANAG
>gnl|CDD|185091 PRK15137, PRK15137, DNA-specific endonuclease I; Provisional
MYRNLSIAAVLLSAAFSGPALAEGINNFSQAKAAAVKVHADAPGTFYCGCKINWQGKKGVVDLQSCGYQV
RKNENRASRIEWEHVVPAWQFGHQRQCWQDGGRKNCAKDPVYRKMESDMHNLQPAIGEVNGDRGNFMYSQ
WNGGEGQYGQCAMKVDFKNKLAEPPARARGAIARTYFYMRDQYQLTLSRQQTQLFNAWDKQYPVTDWECE
RDERIAKVQGNHNPYVQRACQARKS
>gnl|CDD|185092 PRK15138, PRK15138, alcohol dehydrogenase
MNNFNLHTPTRILFGKGAIAGLREQIPADARVLITYGGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNPT
YETLMKAVKLVREEKITFLLAVGGGSVLDGTKFIAAAANYPENIDPWHILETGGKEIKSAIPMGSVLTLP
ATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDA
KIQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLD
HAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNITEGSDDERIDAAIAATRNFFEQMGVPTRLSDYGLDG
SSIPALLKKLEEHGMTQLGEHHDITLDVSRRIYEAAR
>gnl|CDD|185093 PRK15171, PRK15171, lipopolysaccharide 3-alpha-galactosyltransferase
HYFNEEEVINKTIDFNYQPHASKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADK
QRFSALAKQYNTRINIYLINCERLKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKEL
IDLDFAENEIAAVVAEGDAEWWSKRAQSLQTPGLASGYFNSGFLLINIPAWAQENISAKAIEMLADPEIV
SRITHLDQDVLNILLAGKVKFIDAKYNTQFSLNYELKDSVINPVNDETVFIHYIGPTKPWHSWADYPVSQ
YFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYINGIMNYIKYFKEKIF
>gnl|CDD|237918 PRK15172, PRK15172, aldose-1-epimerase
MQITNMHSSGQTISLAAGDYQATIVTVGAGLAELTFQGRHLVIPHKPEEMPLAHLGKVLIPWPNRIANGC
YRYQGQEYQLPINEHVSKAAIHGLLAWRDWQISELTATSVTLTAFLPPSYGYPFMLASQVIYSLDAATGL
SVEIASQNIGDVPAPYGVGIHPYLTCNLTSVDEYLLQLPANQVLAVDEHANPTTLHHVDELDLDFSQAKK
IAATKIDHTFKTANDLWEVRITHPQQALSVSLCSDQPWLQIYSGEKLQRQGLAVEPMSCPPNAFNSGIDL
LLLEPGKTHRLFFNIGGQRK
>gnl|CDD|185095 PRK15173, PRK15173, peptidase; Provisional
MPNAELKTFPVWVDVDDPFNMRDSANNNKERPIGPPIESVCNILKDALNDARVLNKKIAIDLNIMSNGGK
RVIDAVMPNVDFVDSSSIFNELRVIKSPWEIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVM
SKSETHFSRFHLISVGADFSPKLIPSNTKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQT
IRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSGLPNYNRGHLGHGNGVFLGLEESPFVSTHATESFTSGM
VLSLETPYYGYNLGSIMIEDMILINKEGIEFLSKLPRDLVSFN
>gnl|CDD|185096 PRK15174, PRK15174, Vi polysaccharide transport protein VexE
MSLHSTFKKISPTTLLKQEDWEGLCLYFSQHPEKVRDSAGNEQNIILFAIACLRKDETDVGLTLLSDRVL
TAKNGRDLLRRWVISPLASSQPDAVLQVVNKLLAVNVCQPEDVLLVASVLLKSKQYATVADLAEQAWLAF
SGNSQIFALHLRTLVLMDKELQAISLARTQAQEVPPRGDMIATCLSFLNKSRLPEDHDLARALLPFFALE
RQESAGLAVDTLCAVGKYQEAIQTGESALARGLDGAALRRSLGLAYYQSGRSREAKLQAAEHWRHALQFN
SDNVRIVTLYADALIRTGQNEKAIPLLQQSLATHPDLPYVRAMYARALRQVGQYTAASDEFVQLAREKGV
TSKWNRYAAAALLQAGKTSEAESVFEHYIQARASHLPQSFEEGLLALDGQISAVNLPPERLDWAWEVAGR
QSGIERDEWERRAKWGYLADNFLLDWLECRGEQADEPMYRLADISHVEQFFQRLQLDQRGCIIVSAHLGA
MYAGPMILSLLEMNSKWVASTPGVLKGGYGERLISVSDKSEADVVRACMQTLHSGQSLVVAIDGALNLSA
PTIDFFGQQITYSTFCSRLAWKMHLPTVFSVPIWKNRHIHFVLERMVDPLKFESQLSFTERWKENYLQCV
TRILQSDPENLRLSGGIWRNIIRRDS
>gnl|CDD|185097 PRK15175, PRK15175, Vi polysaccharide ABC transporter protein VexA
MKKIIILLTTFFLLSGCTIPRAVFKSSLINQDDPRYNLVEVTPTLKLSAPDTVPKTIVDPVFAANNWHWT
SLAKGDVLHITILSSGGAGYLSNNASGDRADFENILVTDSNTVQVPYAGTIPVSGLDVTQLADEIKKRLS
RVVLNPQVIVTLTARTGAMVTVEGSGKTGRYPLEQSMNRLSHLLATAVAVENTSTDMMEVHVTRQQHYFT
ARLSDIYQYPGLDIALQPDDRITLRQVTEYVNVLGAAGVQGKHALVQRHSSVVDALALAKGLNDNLADPQ
AIFLYKHNEAEQAKQQMRKLNIYHVDMSQPNSVFLAQAIRVDNGDVIYISNASLTDFAKVKAAFDSFLTR
GTNSF
>gnl|CDD|185098 PRK15176, PRK15176, Vi polysaccharide ABC transporter inner membrane protein VexB
MNILKNNSYYFMKLITVCELIILLMSRDIKTRYNGNLLNYMMVLAVPLVWISITVISFQYLNRSVPISTD
DISFVIAGILPYLLFRYTITATMRTHSFSTSLAVVSQVKKRHVIFSLAAIEFVNAVIIYIIISLINFLIF
SRWEAQKPFLIFEGMVIAWLLGLSFGYFCDALSERFPLVYKAVPVMLRPMFLISAVFYTANELPYSLLSI
FSWNPLLHANEIVREGMFEGYHSLYLEPFYPLAFSATLFLAGLIFHLICDTENH
>gnl|CDD|185099 PRK15177, PRK15177, Vi polysaccharide ABC transporter ATP-binding protein VexC
VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIGLRGDALPLGANSFILPGLTGEENA
RMMASLYGLDGDEFSHFCYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQ
LRMQAALACQLQQKGLIVLTHNPRLIKEHCHAFGVLLHGKITMCEDLAQATALFEQYQSNQATIQTEDYS
FDI
>gnl|CDD|185100 PRK15178, PRK15178, Vi polysaccharide ABC transporter inner membrane protein VexD
MENSERIKKWKEERAKVAQESRASRLQQKEDERALRQTEKSADAKSHHNPDAGWSATDADSVRRASLVIK
ERRVQQAKQSLRRLFLYIALPLLVIMLMSWILTSHFYSADATFIVQTDASQDNFSGTSFFGAGNKMSEGF
QVREFILSKEMMDRMEKELGFLSYFAQDDIALFSRFHAPLGINDDPYRYYLSKVSVAVDIQQGMLRLNVK
ARSAKQAEFFAQRILSFAEQHVNTVSARMQKERILWLENDVKSAQENLGAARLELLKIQHIQKDIDPKET
ITAIYQLIAGFETQLAEAKAEYAQLMVNGLDQNPLIPRLSAKIKVLEKQIGEQRNRLSNKLGSQGSSESL
SLFEDLRLQSEIAKARWESALQTLQQGKLQALRERQYLLIISQPMAESDTTRYADGTKWLLFFVLLGITY
LVTSLLITIRRMRE
>gnl|CDD|185101 PRK15179, PRK15179, Vi polysaccharide biosynthesis protein TviE; Provisional
MFSFLSRIRKPRRADTAAGPTGGPASGPTILDLLEAALAEPGESEEAGRELLQQARQVLERHAAVHKPAA
ALPELLDYVRRYPHTELFQVLVARALEAAHRSDEGLAVWRGIHQRFPDSSEAFILMLRGVKRQQGIEAGR
AEIELYFSGGSSSAREILLEAKSWDEIGQSEQADACFERLSRQHPEFENGYVGWAQSLTRRGALWRARDV
LQAGLDAIGDGARKLTRRLVDLNADLAALRRLGVEGDGRDVPVSILVLEKMLQEIGRRRNAEYDAGPESF
VGPVLMINGSLGAGGAERQFVNTAVALQSAIQQGQSIAGYGVLGPVQVVCRSLRSREGADFFAATLADAG
IPVSVYSDMQAWGGCEFSSLLAPYREYLRFLPKQIIEGTTKLTDVMRSSVPSVVHIWQDGSIFACALAAL
LAGVPRIVLSVRTMPPVDRPDRYRVEYDIIYSELLKMRGVALSSNSQFAAHRYADWLGVDERRIPVVYNG
LAPLKSVQDDACTAMMAQFDARTSDARFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLL
ESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAV
QEGVTGLTLPADTVTAPDVAEALARIHDMCAADPGIARKAADWASARFSLNQMIASTVRCYQMP
>gnl|CDD|185102 PRK15180, PRK15180, Vi polysaccharide biosynthesis protein TviD; Provisional
MNLMKSSGMFTLTAIGSCRIVSPVKRAQPYFNFQANFKRIYGFTHTSSEALQQIRFILGLIDIPEKVRPF
IFRPNVNYSNTDVHSRSDFYIIEISSQKKIMAYGFCLQINYLTRHFYEFFSQTERACMYWSLATQGNRHK
LLAYLKDDPCFAGMSEDDRALLSNINVEQMDEHAIEQDMMEIVQLLGRDRVMFMTHVDAVTRAGTVILSR
SRLIKNVDTIAARMDIPCVNPTNLMEKWGQKRALEKNGDDLTHYTDMFGDAIVAAIFKGVINNTNHHLDE
GRQEKQDQIREITLSITKQLADGDIIAASQQLFAALRNQQQDPVLIQLRSVIFSHLGYYEQAYQDISDVE
KIIGTTDSTLRCRLRSLHGLARWREALSTAEMMLSNEIEDEEVLTVAAGSADALQLFDKSYHYWKRVLLL
NPETQSGWVNFLSSTQYFNDGNAFSEAFHAGIQSQRLNDTFMETALSLAIKFSDELIFMHALEQLLRHES
EFALTVLSTIHDTGLVIRTAFCIKNMSYHQALRTSYKDKIHDVFEAWNNTALSLHSVDDFVSLSTSLAYS
YSAFMVYPHSRISRFNNEVKMAWRDKLREMYEREDYENILAGAKIVWPLLKFDPVGTVYCARTLVNLGAW
KDACTLAHMTLIRNSNITSLQSIMLRSIRHINNIPFLIDLIANVMSITLSFQNASMNKLFEKECRNVATR
ALKYVRQKKTEGRLDEALSVLISLKRIEPDVSRLMREYKQIIRLFNESRKDGGSTITSYEHLDYAKKLLV
FDSENAYALKYAALNAMHLRDYTQALQYWQRLEKVNGPTEPVTRQISTCITALQKNTSGKS
>gnl|CDD|185103 PRK15181, PRK15181, Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC
MTAYEELRTKLVLAPKRWLITGVAGFIGSGLLEELLFLNQTVIGLDNFSTGYQHNLDDVRTSVSEEQWSR
FIFIQGDIRKFTDCQKACKNVDYVLHQAALGSVPRSLKDPIATNSANIDGFLNMLTAARDAHVSSFTYAA
SSSTYGDHPDLPKIEERIGRPLSPYAVTKYVNELYADVFARSYEFNAIGLRYFNVFGRRQNPNGAYSAVI
PRWILSLLKDEPIYINGDGSTSRDFCYIENVIQANLLSATTNDLASKNKVYNVAVGDRTSLNELYYLIRD
GLNLWRNEQSRAEPIYKDFRDGDVKHSQADITKIKTFLSYEPEFDIKEGLKQTLKWYIDKHSTLYSSV
>gnl|CDD|185104 PRK15182, PRK15182, Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB
MFGIDEVKIAIIGLGYVGLPLAVEFGKSRQVVGFDVNKKRILELKNGVDVNLETTEEELREARYLKFTSE
IEKIKECNFYIITVPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEECVPILARMSG
MTFNQDFYVGYSPERINPGDKKHRLTNIKKITSGSTAQIAELIDEVYQQIISAGTYKAESIKVAEAAKVI
ENTQRDLNIALVNELAIIFNRLNIDTEAVLRAAGSKWNFLPFRPGLVGGHCIGVDPYYLTHKSQGIGYYP
EIILAGRRLNDNMGNYVSEQLIKAMIKKGINVEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKV
DIFDPWVDAEEVRREYGIIPVSEVKSSHYDAIIVAVGHQQFKQMGSEDIRGFGKDKHVLYDLKYVLPAEQ
SDVRL
>gnl|CDD|185105 PRK15183, PRK15183, Vi polysaccharide biosynthesis regulator TviA
VNLNRYSLLNALNFFTRMSDINKIIVIISSSRLMPLARFWLTECKNVIAVFDAATSVQDIIRNVSQHQSG
EKILTEQRDYRFRINRKDIVKMKYFLSESGMEELQDRFMNSSSTMYRWRKELAVKFGVREPRYLLLPDSV
TLL
>gnl|CDD|185106 PRK15184, PRK15184, curli production assembly/transport protein CsgG; Provisional
MQRLFLLVAVMLLSGCLTAPPKEAARPTLMPRAQSYKDLTHLPAPTGKIFVSVYNIQDETGQFKPYPASN
FSTAVPQSATAMLVTALKDSRWFIPLERQGLQNLLNERKIIRAAQENGTVAINNRIPLQSLTAANIMVEG
SIIGYESNVKSGGVGARYFGIGADTQYQLDQIAVNLRVVNVSTGEILSSVNTSKTILSYEVQAGVFRFID
YQRLLEGEVGYTSNEPVMLCLMSAIETGVIFLINDGIDRGLWDLQNKAERQNDILVKYRHMSVPPES
>gnl|CDD|185107 PRK15185, PRK15185, transcriptional regulator HilD; Provisional
MENVTFVSNSHQRPAADNLQKLKSLLTNTRQQIKSQTQQVTIKNLYVSSFTLVCFRSGKLTISNNHDTIY
CDEPGMLVLKKEQVVNVTLEEVNGHMDFDILEIPTQRLGALYALIPNEQQTKMAVPTEKAQKIFYTPDFP
ARREVFEHLKTAFSCTKDTSKGCSNCNNKSCIENEELIPYFLLFLLTAFLRLPESYEIILSSAQITLKER
VYNIISSSPSRQWKLTDVADHIFMSTSTLKRKLAEEGTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKC
GYDSTSYFIQCFKKYFKTTPSTFIKMANH
>gnl|CDD|185108 PRK15186, PRK15186, AraC family transcriptional regulator; Provisional
MLKVFNPSPVQVGSIECLQSAQNWQRKSLSLQGLNLLQSVLIKLTTGKISITTSSGEYITASGPMLIFLA
KDQTIHITMEETHEQLNYNLIELDSASIKNAYNFFLYEHADFSAPLTKPTTKHLLAPIETGVARVFNLLH
SSNKSQKLSQDKKEYLIRFLLSEFIYEPEAFALFRELSQNTLAENIYNIIISDISRKWALKDISDSLYMS
CSTLKRKLKQENTSFSEVYLNARMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSEFLA
FLSSSRHQYVN
>gnl|CDD|185109 PRK15187, PRK15187, fimbrial protein BcfA; Provisional
MKKPVLALMVSAIAFGGMLSTAQADTTTVTGGTVNFVGQVVDAACSVSADSVDQTVTLGQVRASKLTEAG
MVANQKEDFTIKLEDCDTQTSQNAAVIFNGQQDANQPGSLANTAGAGSATNVALQLYGPDGQALNIGESS
STVTLNDGENVIPLSVDYIATGTATAGNVTATATFSMVYS
>gnl|CDD|185110 PRK15188, PRK15188, fimbrial chaperone protein BcfB; Provisional
MKKNVPIFLRLLLLLSAAGLSFAAQAGGIALGATRVIYPQGSKQTSLPIINSSASNVFLIQSWVANADGS
RSTDFIITPPLFVIQPKKENILRIMYVGPSLPTDRESVFYLNSKAIPSVDKNKLTGNSLQIATQSVIKLF
IRPKNLAEAPAHAPSTLRCRNERGQLTITNPSPYYVSMVELYSAGKKLPNTMVPPKGAITLPATPGQVSL
RTVNDFGATTPARVCPAS
>gnl|CDD|185111 PRK15189, PRK15189, fimbrial protein BcfD; Provisional
MKIPLLFALLAGSVVSQYAFADVCKNVNGVPSSINYDLTTTLTAEQNQVGKTVQLEKSQEVNVQAVCPAG
ASTYSQTYRSYVSPYPVVETSGNWKYLKLDPDYLEGGMRIEDSSAGDIYPPMNNVLMGYDENVKAGQPFY
VRDSNLEFQLKIVKPFVGTVNISPKTMFNVYVMTAAGDPLTDVVYSILYSGTVTVPQSCEINAGQTILVN
FGALYSGNFNHAGQKPEGVRAKKFSVPVKCSGLDSQVNLTMRLIATPDSHVPQAIASDNADVGVVVETDE
GNALIPNDVQSVAPFITDSAGRANITLQAYPVSTTGETPAEGAFTALASLRVDFD
>gnl|CDD|185112 PRK15190, PRK15190, fimbrial protein BcfE; Provisional
MNRSHCALFAMGLMLCPQINASADDLAYNLEFTGTIVAQTCDIDISSLSQSIDLGQFAVGDFPSTGTTTK
FKPFNINLKNCSRGIAGAKIWFTGEPDPDNPALLAITDTGMGSGNMLASGVGVEILNDDQDTISINNADS
VVYPLKAGRNTLSFYIRYKSTRPTVTSGNATAVMYFDMQYE
>gnl|CDD|185113 PRK15191, PRK15191, fimbrial protein BcfF; Provisional
MRNDILYGIGMLLAASGVQAHDGRVYVSGTITDNTCSLSPGSENINVAMGAVSQRQFYRAGDGSAWQPFA
IDLQNCGSTASGVTVSFSGAADSRNTDLLALTAGESDASGIGIALYDQNKTLIPLGQESDVVTLSPGQAS
AHLQFYARYLADGGAVTPGDANASATFILAYE
>gnl|CDD|185114 PRK15192, PRK15192, pili/flagellar-assembly chaperone
MNKFFLRCAIYWCLLPISWAQAGVVIGGTRFIYHAGAPALSVPVSNHSEASWLIDTHILPGGRWPGTKNE
GNITPFVVTPPLFMLSARQENSMRVVYTGAPLPADRESLFTLSIAAIPSGKPEANRVQMAFRSALKLLYR
PEGLAGNPQQAYRHLIWSLTPDGATVRNPTPYYVTLFLLRANERAQDNAGVVAPFATRQTDWCRHTVRCT
VRWQSINDYGRVMTAQTVDLTRIH
>gnl|CDD|237919 PRK15193, PRK15193, outer membrane usher protein; Provisional
NMYRTHRQHSLLSSGGVPSLALGIVVFVSAGNAQAETYFNPAFLSDDPSMVADLSRFEKGAKIAAGVYRV
DIVLNNTFVATRDVNFVEIKTTGKSAPTDDKGLAACLTTESLDAMGVNTDAFPAFKQLAKGACPPLASII
PDASVTFDFNKQRLDISVPQIAIKSSARGYIPPERWDEGINALLLNYSFSGANSIHSSADSDSGDSYFLG
LNSGVNLGPWRLRNYSTWNRSSGQTAEDSDWQHISSYLERAVIPLKGELTAGDSYTAGDFFDSVSFRGVQ
LASDDNMLPDSLKGFAPTVRGIAKSNAQVTIKQNGYTIYQTYVSPGAFEISDLYPTSSSGDLLVEVKEAD
GSINSYSVPYSAVPLLQREGRIKYAVTLAKYRTNSNEQQEVKFAQATLQWGLPHGFTWYGGTQLSEYYHA
LAFGLGFNLGDWGAISFDATQAKSTLADQSEHKGQSYRFLYAKSLNQLGTNFQLMGYRYSTSGFYTLSDT
MYKHMDGYEFDDGDDEDKSTPMWSDYYNLFYTKRGKLQVNISQQLGEYGSFYLSGSQQTYWHTDQKDRLL
QFGYNTQIKDISLGVSYNYSKSRGQPDADQVFALNFSLPLNLWLPRSNDTRKKHNAYATSSTSIDNEGHV
TQNAGLTGTLLDDNNLSYSVQQGYNNEGKGASGSASLDYKGAFGDANVGYNYSDNGSQQQLNYGLSGGLV
AHSQGITLSQPLGETNVLIAAPGAENVRVANSTGLKTDWRGYAVVPYATSYRENRIALDAASLKDNVDLE
NAVVNVVPTKGALVLAEFNAHVGARALMTLSHQGIPLPFGATVTLDDQHNSGIVDDDGSVYLSGLPAQGV
LHVRWGEAPDQICVASYHLTEQQINSALTRMDAICR
>gnl|CDD|237920 PRK15194, PRK15194, type 1 fimbrial protein subunit FimA
MKLRFISSAIASLLFVAGAAYAADPTPVSVDGGTIHFEGELVNAACSVNTDSADQTVTLGQYRTAIFTAV
GNTTALIPFTIQLNDCDPVVAATAAVAFSGQADATNDNLLAVASSTNTTTATGVGIEILDNTSSILKPDG
ATFSANQNLIEGTNTLHFSARYKATGTSASAGQANADATFIMKYE
>gnl|CDD|185117 PRK15195, PRK15195, molecular chaperone FimC
MMTKIKLGMIIIFYLIISASVHAAGGIALGATRVIYPADAKQTSLAIRNSHTNERYLVNSWIENSSGVKE
KSFIVTPPLFVSEPKSENTLRIIYAGPPLAADRESLFWMNVKAIPSVDKNALEGRNVLQLAILSRIKLFV
RPINLQELPEEAPDTLKFSRSGNHLKVHNPSPYYVTLVNLQVGSQKLGNAMIAPKVNSQIPLPSGVQGKL
KFQTVNDYGAVTPAREVNL
>gnl|CDD|185118 PRK15196, PRK15196, type III secretion system effector PipB2
MERSLDSLAGMATSAFGAGTSAAMRQATSPKTILEYIINFFTCGGIRRRNETQYQELIETMAETLKSTMP
DRGAPLPENIILDDMDGCRVEFNLPGENNEAGQVIVRVSKGDHSETREIPLASFEKICRALLFRCEFSLP
QDSVILTAQGGMNLKGAVLTGANLTAENLCDADLSGANLEGAVLFMADCEGANFKGANLSGTSLGDSNFK
NACLEDSIMCGATLDHANLTGANLQHASLLGCSMIECNCSGANMDHTNLSGATLIRADMSGATLQGATIM
AAIMEGAVLTRANLRKASFISTNLDGADLAEANLNNTCFKDCTLTHLRTEDATMSTSTQTLFNEFYSENI
>gnl|CDD|185119 PRK15197, PRK15197, type III secretion system effector PipB
MPITNASPENILRYLHAAGTGTKEAMKSATSPRGILEWFVNFFTCGGVRRSNERCFREVIGKLTTSLLYV
NKDAFFDGNKIFLEDVNGCTICLSCGAASENTDPMVIIEVNKNGKTVTDKVDSERFWNVCRMLKLMSKHN
IQQPDSLITEDGFLNLRGVNLAHKDFQGEDLSDIDASNADFRETTLSNVNLVGANLCCANLHAVNLMGSN
MTKANLTHADLTCANMSGVNLTAAILFGSDLTDTKLNGAKLDKIALTLAKALTGADLTGSQHTPTPLPDY
NDRTLFPHPIF
>gnl|CDD|185120 PRK15198, PRK15198, outer membrane usher protein FimD
MQRYTWCLAGVALSSLAILPPFLSYAESYFNPAFLSEDTASVADLSRFERGNHQPPGVYRVDIWRNDEFI
GTQDIRFESTTVNTGDKSGGLMPCFTQELLERLGVNSSAFPELAQQQDNKCINLLKAIPGAEIAFDFASM
RLNISLPQIALLNSARGYIPPEEWDEGIPAALLNYSFTGNRGNDNDSYFLSLLSGLNYGPWRLRNNGAWN
YFRGNGYHSEQWNNIGTWVQRAIIPLKSELVMGDSNTGNDVFDSVGFRGARLYSSDNMYPDSLQGYAPTV
RGIARTAAKLTIRQNGYVIYQSYVSPGAFAITDLNPTSSSGDLDVTVDEKDGNQQRYTVPYSTVPLLQRE
GRVKYDLVAGDFRSGNSQQSSPFFFQGTAIGGLPQGFTAYGGTQLAARYTAVLLGAGRNLGDWGAVSVDV
THARSQLADDSRHEGQSLRFLYAKSLNTFGTNFQLLGYRYSTQGFYTLDDVAYRSMEGYEYDYDSDGEHR
DVPIIQSYHNLRFSKKGRFQLNISQSLGDYGSLYISGSHQKYWNTSDSNTWYQLGYASGWQGISYSLSWS
WNESVGIPGNDRIVGFNVSVPFSVLTKRRYTRDNALDRAYATFNANRNSNGDNSWQTGVGGTLLEGRNLS
YSVTQGDTSNNGYSGSASANWQATYGTLGVGYNYDRDQHDVNWQLSGGVVGHEDGITFSQPLGDTNVLIK
APGAGGVRIENQTGVKTDWRGYAVMPYATVYRYNRVALDTNTMGNSTDVENNVSSVVPTQGALVRANFDT
RIGVRALITVTQGGKPVPFGALVRETSSGITSMVGDDGQIYLSGLPLSGELLIQWGDGANSRCIAHYVLP
EQSLQQAITVISAVCTRPGS
>gnl|CDD|237921 PRK15199, fimH, type 1 fimbrin D-mannose specific adhesin FimH
MKIYSALLLAMACLCLANPAWATVCANSTGVAEDEHYDLSNVFNSTNNQPGQIVTLPEKSGWVGVNAICP
PGTLVNYTYRSYVTNFPVQETIDNYKYMKLNDYLLGAMSIVDSVAGIFYPPQNYIRMGTDPNVSQNLPFG
VMDSKLIFRLKVIRPFINMVEIPRQTMFTVYVTTTPYDPLVTPVYTISYSGRVEVPQNCELNAGQVVEFD
FGDIGASLFSQAGAGNRPQGVMPQTKTIAIKCTNVAAQAYLTMRLEAEKVSGQAMVSDNPDLGFIVADQN
GTPLTPNNLNSKIPFRLDDAAAANVGIRAWPISITGQKPTEGPFTARGYLRVDYD
>gnl|CDD|185122 PRK15200, PRK15200, type 1 fimbrial protein subunit FimI
MIRKGAALVGLVLMSPVIAQPVMVESGRVHLRGQLVNGGCAVATESQDLRVLMGQYRTNAFTGPGSFAPV
SVPFSLRLISCSAEVWRHVGIAFAGVTPAEDPHVFLASGEGIGNAGIGLALFDDQQRQIIPNTLPLHYAP
ILTSEMTLHFTARYRAISENMTPGRIHSEVWFTLVYP
>gnl|CDD|185123 PRK15201, PRK15201, fimbriae biosynthesis transcriptional regulator FimW
MLSIAIKEQNSHFEHGLKIIMTRLANQWQQKIDFLPPEEIDNADIAFLALDDDWFSAGCYQIPMHTQHQL
RVIICNKCDKEKLMFRPCLYMLPHIYREDDVEEITRKMILILHKRALRHSVPSGICHYCTTRHFSVTERH
LLKLIASGYHLSETAALLSLSEEQTKSLRRSIMRKLHVKTEQQFLKYIRVNLHFLLSK
>gnl|CDD|237922 PRK15202, PRK15202, type III secretion system chaperone
MESLLNRLYDALGLDAPEDEPALIIDDDIQIYFNESDHTLEMCCPFMPLPDNILTLQHFLSLNYTSAVTL
AADAENTALVALYRLPQTSTEEEALTGFELFISNVKQLKEEYARRMK
>gnl|CDD|185125 PRK15203, PRK15203, 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
MKGTIFAVALNHRSQLDAWQEAFQQSPYKAPPKTAVWFIKPRNTVIRCGEPIPFPQGEKVLSGATVALIV
GKTATKVREEDAAEYIAGYALANDVSLPEESFYRPAIKAKCRDGFCPIGETVALSNVDNLTIYTEINGRP
ADHWNTADLQRNAAQLLSALSEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLENPVVDEREVT
THKSFPTPPHPHGTLFALGLNYADHASELEFKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELV
VVIGKQARKVSEADAMDYVAGYTVCNDYAIRDYLENYYRPNLRVKSRDGLTPILSTIVPKEAIPDPHNLT
LRTFVNGELRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLSDVVPGDEVVVEVEGVGRLVN
RIVSEETAK
>gnl|CDD|185126 PRK15204, PRK15204, undecaprenyl-phosphate galactose phosphotransferase; Provisional
MDNIDNKYNPQLCKIFLAISDLIFFNLALWFSLGCVYFIFDQVQRFIPQDQLDTRVITHFILSVVCVGWF
WIRLRHYTYRKPFWYELKEIFRTIVIFAIFDLALIAFTKWQFSRYVWVFCWTFALILVPFFRALTKHLLN
KLGIWKKKTIILGSGQNARGAYSALQSEEMMGFDVIAFFDTDASDAEINMLPVIKDTEIIWDLNRTGDVH
YILAYEYTELEKTHFWLRELSKHHCRSVTVVPSFRGLPLYNTDMSFIFSHEVMLLRIQNNLAKRSSRFLK
RTFDIVCSIMILIIASPLMIYLWYKVTRDGGPAIYGHQRVGRHGKLFPCYKFRSMVMNSQEVLKELLAND
PIARAEWEKDFKLKNDPRITAVGRFIRKTSLDELPQLFNVLKGDMSLVGPRPIVSDELERYCDDVDYYLM
AKPGMTGLWQVSGRNDVDYDTRVYFDSWYVKNWTLWNDIAILFKTAKVVLRRDGAY
>gnl|CDD|237923 PRK15205, PRK15205, long polar fimbrial protein LpfE; Provisional
MKNKRALLPLALLLLTASGMAAPTDLGPAGDIHFTITIKAKACELEKDSLEVDMGTMVLQKPVKVGTELN
QKNFSIGLKDCDGISKASVTMDGSPDPDDPSLFALDAGGATGVALKIKTSKGTQQYPKSTDGTPVEWAIN
GDGTTQLNYIASYVPVNADATVGTANATVNFSVTYE
>gnl|CDD|237924 PRK15206, PRK15206, long polar fimbrial protein LpfD; Provisional
MLKKLMMFTGLLGGSVLFSGQALAAADWGPCTPEGGTHIFSATINKTISDTSKNTTGATFVDFDSWNLGG
TYAASCECPDDTSLINDTYFKAVVPLAFVTNIESRSYYQINNNIAIASDVLVSGGRGEYVNTPFENVGNL
TANRSQCTQNASSKDAIWTTGGKGHLSLYILHPFVGESIIPSTKIMDLFGTKKPSVYNSIPAASVYISGS
ITVPQGCELSSGSTLEIPFGEFKATDFKDRKGQVAKNATKFTKELQFKCTNISDGVKIFLRIEGMPNAND
SNAIDMGNPDIGAVIEGANGKILVPNDASVNQELSVSGLVDDTHRTASTTISAYPISTTGKLPAAGDFEG
IATMRIDVE
>gnl|CDD|185129 PRK15207, PRK15207, outer membrane usher protein LpfC
MHWMHLPLGHYRAHFSFSLLALTIASTLPAYAGKFNPKFLEDVQGIDQHVDLSMYESPVGQQLPGKYRVS
VFVNEEKMESRTLEFKAATEAQRKAMGESLVPCLSRVQLEEMGVRVDSFPALKMAPPEACVAFDEIIPQA
TSHFDFNTQTLHLSFPQAAMMQTARGTVPESRWDEGIPALLLDYSFSGSNGSYDGTGSSSSYTSDSYYLN
LRSGLNLGAWRLRNYSTWNRTDGKNQWDNIGTSLSRAIIPLKSQLTLGDTATAGDIFDSVQMRGALLASD
EEMLPDSQRGFAPVVRGIAKSNAEVSIEQNGYVIYRTFVQPGAFEINDLYPTSNSGDLTVIIKEADGSEQ
RFIQPFSSVAIFQREGHLKYSLAAGEYRAGNYDSAKPKFGQLDAMYGLPWGMTAYGGALLSADYNALALG
LGKNFGYIGAISIDVTQAKSQLRNNEKSEGQSYRFLYSKSFESGTDFRLLGYKYSTSGYYTFQEATDVRS
DADSDYRRYHKRSQIQGNITQQLGAYGSVYFNMTQQDYWNDDGKQNSLSAGYNGRIGRVNYSVAYTWTKS
PEWDESDRLWSFSMSIPLGRAWSNYRMTTDQNGRTNQQLGVSGTLLEDRNLSYSVQEGYTSNGVGNSGSV
NLGYQGGSGNISVGYNYSKDNQQVNYGVRGGVIVHSEGITLSQPLGESMAIISAPGARGAHVVNNGGVEV
DWMGNAVVPYLTPYRETEVSLRSDSLGQNVDLQEAFQKVVPTRGAIVRARFDTRVGYRVLMSLKQANGNA
VPFGATATLIDTTKEASSIVGEEGQLYISGMPEEGELQVSWGNDQAQQCRVPFRLPEQKDNTGIVMVNAV
CR
>gnl|CDD|237925 PRK15208, PRK15208, molecular chaperone LpfB
MRLISFTALALALIAQNSFAGGVALSSTRVIYDGSKKEASLTVNNKSKTEEFLIQSWIDDANGNKKTPFI
ITPPLFKLDPTKNNVLRIVNITNTLPQDRESVYWINVKAIPAKSEDAENKNVLQIAVRTRLKLFYRPAGL
KGNSMDAWNKLRFTRAGNQIKVENPSAFNLTFNQFYANGRDIEKAGMVPAKGSLNIELPAGTGKVSEVKY
NIINDFGTAGEMLTKRVN
>gnl|CDD|185131 PRK15209, PRK15209, long polar fimbrial protein LpfA; Provisional
MKKVVFALSALALTSTSVFAAESGDGTVKFTGEIVDAPCVVSTDSQNQEVVLGQVKKSVFKAIGDKSSAK
PFQIKLEDCDITTNKKVNVSFNGVGDADDSTLVSVSTEAGAATGVGIGIYDNANTLVELNTGKSTTTLAA
GQTVLYFTANYVSTKDTVTTGYGNAEVDFNLSYE
>gnl|CDD|185132 PRK15210, PRK15210, fimbrial protein
MRNKIILAMAAAGMMYGASVFAADTTPTAGPFGSGKILFTGTITNSPCDIAPGDDAITVPFGQISYRKLN
TADATTESKPFTIHLQNCAFDPNIPDTAGSAGKMSKVTVSFSGTANTSKKAYTTSGSAQHVGVQLLKSDN
TSIIEPNTPMPDGDAQQLQAGNNELNFFARLIALDNGVTPGDFNASVTYTLKYL
>gnl|CDD|185133 PRK15211, PRK15211, fimbrial chaperone
NKMMKWGLVSLLSLAVCGQAMAAFVLNGTRFIYDEGRKNISFEVTNQADQTYGGQVWIDNTTQGSSTVYM
VPAPPFFKVRPKEKQIIRIMKTDSALPKDRESLFWLNVQEIPPKPKASEGNVLAVALNTQVKLIYRPKAL
KEGRENAEKNLQIIHRGGETYLKNPTPYYFAVTGVKLNGQPVKLSDRVMNEIAQLAPFSEVSLGKLSLNG
TVTVQAVNDWGGTQDYTLK
>gnl|CDD|185134 PRK15212, PRK15212, virulence protein SpvA; Provisional
MNMNQTTSPALSQVETAIRVPAGNFAKYNYYSVFDIVRQTRKQFINANMSWPGSRGGKAWDLAMGQAQYI
RCMFRENQLTRRVRGTLQQTPDNGTNLSSSAVGGIQGQAERRPDLATLMVVNDAINQQIPTLLPYHFPHD
QVELSLLNTDVSLEDIISESSIDWPWFLSNSLTGDNSNYAMELASRLSPEQQTLPTEPDNSTATDLTSFY
QTNLGLKTADYTPFEALNTFARQLAITVPPGGTVDCGYSACQPAV
>gnl|CDD|237926 PRK15213, PRK15213, outer membrane usher protein PefC
MSFHHRLFKLSALALAIFTHLGFASAVAGEELNMSFIQGGGGIPPEVLASNGDYPPGRYLVDVIFNGKKI
GKAILSITPQEAEALCLSPEWLKKAGIPVSLEYYRSGYDAARQCYVLSKAPSVQVDFDYSTQSLTLSIPQ
AGLVKKPEPVEWDYGVPAFRLNYSANASKTSRQNTSAYGNADLKANLGRWVLSSRASASRGAGGSNEFTT
NDFTLTTAIKSLQGDLLVGKTQTGNSLLGSFGFYGASLRSNNDMLPWENRGYAPVISGIANGPSRVTISQ
NGYTLYSEVVPAGPFQLDDVPLVGSGDLTVTVEEEDGHKTTQVFPVAVLPGLLRPGEHEYNVAAGLKDDN
YDLKKPENGLFFAGSYGYGFDGLTLNAAGILNQNYQGGGVGVVQGLGYFGAVSASGNLSQAKYQNGDNKS
GNSVSLKYAKSLSDTNNLQLLSYRYQSEGYVDFADFYPTDLYTRSNTKRRYEDIFSQGLSQSLFFLSLSG
WQEDYWPSSGKETGATVSLSTTIKGVSVNLNGSYSKRNSLGENDYSASLSISIPFTLFDKRHYSSTSVSY
SRSGGTGFNSGVSGSLNDRLSYGLNTNRDRDGGRSSSLNASYGFDRAQTNGMLSHQGGGNTSGSVSVSGS
VLGTPDAGILFTRVTGDTVAVVNVKDVPGVKFNGSGPTDSKGNTVVPLSSYDLNTVTVNAENLPLNTELT
TTSQNVVPTDKAVVYREFKALKVLRYILRVKQKDGRFVPGGSWARNEQGTPLGFVANNGVLLMNLLDAPG
DISVGQCRFPAAKLVQNTGKVQEITCE
>gnl|CDD|185136 PRK15214, PRK15214, fimbrial protein PefA; Provisional
MKKSIIASIIALGVLGGTAHAANEVTFLGSVSATTCDLTTSVNGAAQPNQVVQLGTVQANQTGNAVEFAM
KPVDPTAQACGNLAQKTATITWASAALDGEGFGATSGTAADAKVLVDSVNSKNPGAVNANASSVDFDGAK
LTTDGLKFTAKLKGGATEGDFKSVASFAVTYK
>gnl|CDD|185137 PRK15215, PRK15215, fimbriae biosynthesis regulatory protein; Provisional
MMLNRKDADYYLGKEIMLARIRRGALIPAKVNEEHFWLLIGISSIHSEKIIQALRDYLVFGVSRKDVCER
YEVNNGYFSTSLNRLSRISQAAAQMVVYYS
>gnl|CDD|185138 PRK15216, PRK15216, putative fimbrial biosynthesis regulatory protein; Provisional
MKRLLFLLMMMQFTQLGYAACNATLTNTKDYTIQSDSLMLGGEESAIITNGFTDANCSNSDVVTKLETSD
HIIGMGPNDSVKLKLKVEWQSSSAINMRNQNGVIEAPYKITISEINSLEAVTVSARGGYSVTIDNITVMS
GAKNQWSSSDWVVFILRYIGCWGNRECVANVITDLNGKGVYKANLTINYNRKETTCAPQNLTITLDPVPM
TKLRAKGEVSEFSKQGDIILDCKNQVRNAMLTSRQIAVNLRSDLVWDENEAVLKPDNDNGVGFILRDSNR
SLLKINKGVAINSIFKTYAKGSAVNSVEAIPVFATYYVLDPAKVKAGPLQSKALIVVSYN
>gnl|CDD|185139 PRK15217, PRK15217, fimbrial outer membrane usher protein; Provisional
MLRMTPLASAIVALLLGIEAYAAEETFDTHFMIGGMKGQKVSNYRLDDNQPLPGQYEIDIYVNKQWRGKY
EIIVKDNPQETCLSRELIKRLGIKSDNFATEKQCITLKQLVQGGSYTWDIGVFRLDLSVPQAYVEELEAG
YVPPENWDRGINAFYTSYYASQYYSDYKASGNSKSTYVRFNSGLNLLGWQLHSDASFSKTDNNPGEWKSN
TLYLERGFAQLLGTLRVGDMYTSSDIFDSVRFSGVRLFRDMQMLPNSKQNFTPRVQGIAQSNALVTIEQN
GFVVYQKEVPPGPFAIADLQLAGGGADLDVSVKEADGSVTTYLVPYASVPNMLQPGVSKYDFAAGRSHIE
GASKQSDFVQAGYQYGFNNLLTLYGGTMLANNYYAFTLGTGWNTRIGAISVDATKSHSKQDNGDVFDGQS
YQIAYNKYLSQTSTRFGLAAWRYSSRDYRTFNDHVWANNKDNYRRDENDVYDIADYYQNDFGRKNSFSAN
ISQSLPEGWGSVSLSALWRDYWGRSGSSKDYQLSYSNNWQRISYTLSASQTYDENHHEEKRFNIFISIPF
DWGDDVTTPRRQIYLSNSTTFDDQGFASNNTGLSGTAGSRDQFNYGVNLSHQRQGNETTAGANLTWNAPV
ATVNGSYSQSSNYRQAGGSISGGLVAWSGGVNLANRLSDTFAIMNAPGLEGAYVNGQKYRTTNRKGVVVY
DGLTPYRENHLMLDVSQSDSETELRGNRKIAAPYRGAVVLVNFDTDQRKPWFIKALRADGQPLTFGYEVN
DIHGHNIGVVGQGSQLFIRTNEVPPSVKVAIDKQQGLSCTITFGKEIDESKNYICR
>gnl|CDD|185140 PRK15218, PRK15218, fimbrial assembly chaperone
MKWMIALCLACAAMPAWSGIYIYGTRIIYPAQKKDITVQLMNDGKRSSLIQAWIDNGDTSLPPEKLQVPF
IMTPPVIRVAANSGQQLKIKKLANNLPGDRESLFYLNVLDIPPNSDENKDKNIIKFALQNRIKLIYRPPG
VQKVDKATFSRLQLLRAPGSISVKNNSANWITIPEIKAKSKVNKETLLLAPWSSQSITTTVVVNSYTVTL
IDDSGNYLNETVKIEN
>gnl|CDD|237927 PRK15219, PRK15219, carbonic anhydrase; Provisional
MEQNHPNQPSRRAVLKAALAMTAASVIGLAGLGVPQISYAASLTKEERDKMTPDQIIESLKQGNKRFRSG
KPAQHDYLAQKRASAAGQYPAAVILSCIDSRAPAEIILDTGIGETFNSRVAGNISNDDLLGSMEFACAVA
GAKVVLVMGHTACGAVKGAIDNVELGNLTGLLDRIKPAIEVTEFDGERSSKNYKFVDAVARKNVELTIEN
IRKNSPILRKLEQEGKIKIVGSMYNLNGGKVEFFM
>gnl|CDD|237928 PRK15220, PRK15220, fimbrial protein YehD
MKRSLIAASVLSAVFMSAGAFAADEDMGELKINGKVVGTTCQFLGTNSATIELNQVGVDRLANLNPGQIY
TGYTNPTAMPLKVKCTQGAAPRISFSRSQFVDNMDITKNNGSANGAGFAVYYDGTDVKPDPETGVTLNPN
KFENGVYTLNFSARYARVDNDVTSGDVESTLTLTVVTD
>gnl|CDD|185143 PRK15221, PRK15221, Saf-pilin pilus formation protein SafA; Provisional
MKSIKKLIIASALSMMAASCYAGSFLPNTEQQKSVDINFASPQQLTVSLDPVSGLKAGKNKSDTAIAKLT
VSSTSAKEFGVRGDANAVVDNAGDVWTVTGKNTGNGIKVGFSGEACTRSKGNVNWNGHKWITFDTNDKLD
IKLAGAQNVPADTYPITLDVVGYQA
>gnl|CDD|185144 PRK15222, PRK15222, putative pilin structural protein SafD; Provisional
MWMKIQRVKTVIYSVSLLVTASSLIPIANAAEKLQTTLRVGAYFRAGHVPDGMVLAQGWVTYHGSHSGFR
VWSDEQKAGNTPTVLLLSGQQDPRHHIQVRLEGEGWQPDTVSGRGAILRTAADNASFSVVVDGNQEVPAD
TWTLDFKACALAQEDT
>gnl|CDD|185145 PRK15223, PRK15223, fimbrial biogenesis outer membrane usher protein
MKFKQPALLLFIAGVVHCANAHTYTFDASMLGDAAKGVDMSLFNQGVQQPGTYRVDVMVNGKRVDTRDVV
FKLEKDGQGTPFLAPCLTVSQLSRYGVKTEDYPQLWKAAKTPDECADLTAIPQAKAVLDINNQQLQLSIP
QLALRPEFKGIAPEDLWDDGIPAFLMNYSARTTQTDYKMDMERRDNSSWVQLQPGINIGAWRVRNATSWQ
RSSQLSGKWQAAYTYAERGLYSLKSRLTLGQKTSQGEIFDSVPFTGVMLASDDNMVPYSERQFAPVVRGI
ARTQARVEVKQNGYTIYNTTVAPGPFALRDLSVTDSSGDLHVTVWEADGSTQMFVVPYQTPAIALHQGYL
KYSLLAGRYRSSDSATDKAQIAQATLMYGLPWNLTAYGGIQSATHYQAASLGLGGSLGRWGSLSVDGSDT
HSQRQGEAVQQGASWRLRYSNQLTATGTNFFLTRWQYASQGYNTLSDVLDSYRHDGNRLWSWRENLQPSS
RTTLMLSQSWGRHLGNLSLTGSRTDWRNRPGHDDSYGLSWGTSIGGGSLSLNWNQNRTLWRNGAHRKENI
TSLWFSMPLSRWTGNNVSASWQMTSPSHGGQTQQVGVNGEAFSQQLDWEVRQSYRADAPPGGGNNSALHL
AWNGAYGLLGGDYSYSRAMRQMGVNIAGGIVIHHHGVTLGQPLQGSVALVEAPGASGVPVGGWPGVKTDF
RGDTTVGNLNVYQENTVSLDPSRLPDDAEVTQTDVRVVPTEGAVVEAKFHTRIGARALMTLKREDGSAIP
FGAQVTVNGQDGSAALVDTDSQVYLTGLADKGELTVKWGAQQCRVNYQLPAHKGIAGLYQMSGLCR
>gnl|CDD|185146 PRK15224, PRK15224, pili assembly chaperone PapD
MAAVLFVSNSITPVYAAEQKLNLNTKSFSVKLGATRVIYHAGTAGATLSVSNPQNYPILVQSSVKAADKS
SPAPFLVMPPLFRLEANQQSQLRIVRTGGDMPTDRETLQWVCIKAVPPENEPSDTQAKGATLDLNLSINV
CDKLIFRPDAVKGTPEDVAGNLRWVETGNKLKVENPTPFYMNLASVTVGGKPITGLEYIPPFADKTLNMP
GSAHGDIEWRVITDFGGESHPFHYVLK
>gnl|CDD|185147 PRK15228, PRK15228, fimbrial protein SefA; Provisional
MRKSASAVAVLALIACGSAHAAGFVGNKAEVQAAVTIAAQNTTSANWSQDPGFTGPAVAAGQKVGTLSIT
ATGPHNSVSIAGKGASVSGGVATVPFVDGQGQPVFRGRIQGANINDQANTGIDGLAGWRVASSQETLNVP
VTTFGKSTLPAGTFTATFYVQQYQN
>gnl|CDD|185148 PRK15231, PRK15231, fimbrial adhesin protein SefD; Provisional
MQMNQYNSSIPKFIVSVFLIVTGFFSSTIKAQELKLMIKINEAVFYDRITSNKIIGTGHLFNREGKKILI
SSSLEKIKNTPGAYIIRGQNNSAHKLRIRIGGEDWQPDNSGIGMVSHSDFTNEFNIYYFGNGDIPVDTYL
ISIYATEIEL
>gnl|CDD|185149 PRK15233, PRK15233, fimbrial chaperone SefB
MYILNKCIRITVIFFFFCYLPIASSESKKIEQPLLTQKYYGLRLGTTRVIYKEDAPSTSFWIMNEKEYPI
LVQTQVYNDDKSSKAPFIVTPPILKVESNARTRLKVIPTSNLFNKNEESLYWLCVKGVPPLNDNESNNKN
NITTNLNVNVVTNSCIKLIYRPKTIDLTTMEIADKLKLERKGNSIVIKNPTSSYVNIANIKSGNLSFNIP
NGYIEPFGYAQLPGGVHSKITLTILDDNGAEIIRDY
>gnl|CDD|185150 PRK15235, PRK15235, outer membrane fimbrial usher protein SefC; Provisional
MKKTTITLFVLTSVFHSGNVFSRQYNFDYGSLSLPPGENASFLSVETLPGNYVVDVYLNNQLKETTELYF
KSMTQTLEPCLTKEKLIKYGIAIQELHGLQFDNEQCVLLEHSPLKYTYNAANQSLLLNAPSKILSPIDSE
IADENIWDDGINAFLLNYRANYLHSKVGGEDSYFGQIQPGFNFGPWRLRNLSSWQNLSSEKKFESAYIYA
ERGLKKIKSKLTVGDKYTSADLFDSVPFRGFSLNKDESMIPFSQRTYYPTIRGIAKTNATVEVRQNGYLI
YSTSVPPGQFEIGREQIADLGVGVGVLDVSIYEKNGQVQNYTVPYSTPVLSLPDGYSKYSVTIGRYREVN
NDYIDPVFFEGTYIYGLPYGFTLFGGVQWANIYNSYAIGASKDIGEYGALSFDWKTSVSKTDTSNENGHA
YGIRYNKNIAQTNTEVSLASHYYYSKNYRTFSEAIHSSEHDEFYDKNKKSTTSMLLSQALGSLGSVNLSY
NYDKYWKHEGKKSIIASYGKNLNGVSLSLSYTKSTSKISEENEDLFSFLLSVPLQKLTNHEMYATYQNSS
SSKHDMNHDLGITGVAFDSQLTWQARGQIEDKSKNQKATFLNASWRGTYGEIGANYSHNEINRDIGMNVS
GGVIAHSSGITFGQSISDTAALVEAKGVSGAKVLGLPGVRTDFRGYTISSYLTPYMNNFISIDPTTLPIN
TDIRQTDIQVVPTEGAIVKAVYKTSVGTNALIRITRTNGKPLALGTVLSLKNNDGVIQSTSIVGEDGQAY
VSGLSGVQKLIASWGNKPSDTCTVFYSLPDKNKGQISFLNGVCK
>gnl|CDD|237929 PRK15238, PRK15238, inner membrane transporter YjeM; Provisional
MMSNTKKKLSLIGLILMIFTSVFGFANSPRAFYLMGYSAIPWYILSAILFFIPFALMMAEYGSAFKDEKG
GIYSWMNKSVGPKFAFIGTFMWFASYIIWMVSTASKIWIPFSTFIFGKDTTQTWHFLGLNSTQVVGILAV
IWMILVTFVASKGINKIAKVTSIGGIAVMLLNIVLLLVSIIILILNGGHFAQPIGVSSFVTSPNPAYQSP
IAVLSFVVFAIFAYGGIEAVGGLVDKTENPEKNFPKGIIIAAIVISIGYSLAIFLWGVSTNWQQVLSNKS
VNLGNITYVLMNNLGYTLGHALGLSPAASLTLGVWFARITGLSMFLAYTGAFFTLSYSPLKQLIEGTPKA
LWPKKMTKLNKNGMPANAMWLQCIIVSVFILLVSFGGDAASAFFNILTLMANVSMTLPYLFLAGAFPFFK
KKKDIDRPFVVFKTKKSTLIATIVVVLVVGFANVFTIIQPVIEGDYQSTFWMIGGPVFFSILAWIIYQNY
EKKMAN
>gnl|CDD|185152 PRK15239, PRK15239, putative fimbrial protein StaA; Provisional
MKKVLLATAVFMALGSSSVMAVEGGRINFEGLVSAETCKKVVSSAVGNSNIDGTVTLKTAHVSDVTAEVQ
NSTAGVNAEDFSIIIDCSDAGAGLVKSHLTMSSSFSNTKGTLDNDETLTRSGIEAAKAVDIAVHHVDDAN
ALSLVKINDPSNTMEESFTNGIATYNFKASYVKSSDAGASVTTGLVSTNAIYTFTYE
>gnl|CDD|185153 PRK15240, PRK15240, resistance to complement killing; Provisional
MKKIVLSSLLLSAAGLAAVPVAQADTHSVSVGYAQSRIEHFKDIRGVNLKYRYEAQTPLGLMASFSWQSG
KRGESGGIPGGMSWRDDVKATYWSLMAGPAVRVNELVSLYALAGAGTGRAEVKERISMPGYNGRFTGSER
RTGFAWGAGVQFNPVENVVIDLGYEGSKVGAAKLNGVNVGVGYRF
>gnl|CDD|185154 PRK15241, PRK15241, putative fimbrial protein StaD; Provisional
MKRNKYLLAASVLAMIFPLTSQAEDINVDFTATVLATTCSMSIAALDGSNVSGDATSGYTLNVGDVGLDK
IIKKSAESQKNFKFVAKDCSAALTKITTALGSSADASGNFIKNQSAASDAASNIGMGFKRKSTTDETYFT
PGSGSITWTDDERTANEVEMTVALRELTDGAGTMGAFSSTATFNFTYQ
>gnl|CDD|185155 PRK15243, PRK15243, virulence genes transcriptional activator SpvR
MDFLINKKLKIFITLMETGSFSIATSVLYITRTPLSRVISDLERELKQRLFIRKNGTLIPTEFAQTIYRK
VKSHYIFLHALEQEIGPTGKTKQLEIIFDEIYPESLKNLIISALTISGQKTNIMGRAVNSQIIEELCQTN
NCIVISARNYFHRESLVCRTSVEGGVMLFIPKKFFLCGKPDINRLAGTPVLFHEGAKNFNLDTIYHFFEQ
TLGITNPAFSFDNVDLFSSLYRLQQGLAMLLIPVRVCRALGLSTDHALHIKGVALCTSLYYPTKKRETPD
YRKAIKLIQQELKQSTF
>gnl|CDD|185156 PRK15244, PRK15244, type III secretion system effector NAD(+)--protein-arginine ADP-ribosyltransferase SpvB
MLILNGFSSATLALITPPFLPKGGKALSQSGPDGLASITLPLPISAERGFAPALALHYSSGGGNGPFGVG
WSCATMSIARRTSHGVPQYNDSDEFLGPDGEVLVQTLSTGDAPNPVTCFAYGDVSFPQSYTVTRYQPRTE
SSFYRLEYWVGNSNGDDFWLLHDSNGILHLLGKTAAARLSDPQAASHTAQWLVEESVTPAGEHIYYSYLA
ENGDNVDLNGNEAGRDRSAMRYLSKVQYGNATPAADLYLWTSATPAVQWLFTLVFDYGERGVDPQVPPAF
TAQNSWLARQDPFSLYNYGFEIRLHRLCRQVLMFHHFPDELGEADTLVSRLLLEYDENPILTQLCAARTL
AYEGDGYRRAPVNNMMPPPPPPPMMGGNSSRPKSKWAIVEESKQIQALRYYSAQGYSVINKYLRGDDYPE
TQAKETLLSRDYLSTNEPSDEEFKNAMSVYINDIAEGLSSLPETDHRVVYRGLKLDKPALSDVLKEYTTI
GNIIIDKAFMSTSPDKAWINDTILNIYLEKGHKGRILGDVAHFKGEAEMLFPPNTKLKIESIVNCGSQDF
ASQLSKLRLSDDATADTNRIKRIINMRVLNS
>gnl|CDD|185157 PRK15245, PRK15245, type III secretion system effector phosphothreonine lyase
MPINKPNLKLNLPPLNVVAAYEGPQMPSTNEHLKNNFNSLHNQMRQMPASHFKEALDVPDYSGMRQSGFF
AMSQGFQLVNHGYDVFIHARRESPQSKGDFAGDKFHISVARDQVPQAFQALSGLLFSEDSPVDKWKVTDM
ERVSQQSRVGLGAQFTLYVKPDQENSQYSASFLHKTRQFIECLESRLSENGVISGQCPESDVHPENWKYL
SYRNELRSGRDGGEMQRQALREEPFYRLMTE
>gnl|CDD|185158 PRK15246, PRK15246, fimbrial assembly chaperone
LTGWYGPAQAAVNIDRTRIIFASDDVAQSLTLSNDNTTPMLLQVWTDAGNIDASPDNSKTPLVALPPVFK
MQPGELRTLRLLLSSRQQLATDRESLFWLNIYQIPPVTQDIKNHPRKLVLPLRLRLKILIRPTGLKAPTE
AEEKKLRFIAKENTIRIVNPTSWYMSLTLTMDNKKSIGDIMVAPKTALDVPLTRSPTPGASINYAVINDS
GNWRQYTAILEKYISESDFIPEF
>gnl|CDD|185159 PRK15247, PRK15247, fimbrial usher protein StbD
MLFSFRTLLFITSLFVSAGTWSSCIKVTDKSALSDAAIKAGYTAQNWIGATDTNTGNIGLPTVISVSNSE
TFQPSGTLLASGIGNFLTAATGTPYSSKQVLYRCDSADAGKLYEMYSTNGDSAFAGAFFTPEVEGAYYDV
ERNVAVRMTNLSTGEYYSRFWKERQLTADSWFQDDKYIYIPASAFSNVLYEMFKIDSRKYFAYQNPMDRD
TWTQPRGYIAFKGPGLITERIKAGLDHASDYYGWPSYWPGAWSTYNSVTYVRGALCKITDYPAIVKIPPV
AVGILAAGGNSQAPFHVSLECESGAVSSALPSTSAANVAMGFVVNQPTAVAAARRLGLTTSAGGLSWLLD
THYGEPGVASGVGIRIYNDAGTPINLLPDRIKTGTGNARGWYGYKDLTTRVSSGSVETYSGDFTASLEAI
GGQTVTAGSVNAQLQAVVSFQ
>gnl|CDD|185160 PRK15248, PRK15248, fimbrial outer membrane usher protein
MSPTINLNRKSLALLIAIVCSGSAQGEEYYFDPALLQGATYGQNIARFNEQQTPSGDYLADVYVNGTLVT
SSTNIRFNAVKEGQQTEPCLPLSVMKAAQIKSLPATDAATECRPLREWVPHAGWQFDSATLRLLLTIPMT
ELTHKPRGYISPSEWDSGALALFLRHNTNWTHTENTDSHYRYQYLWSGLNMGVNLGLWQVRHQSNLRYAN
SNQSGSAWRYNSVRTWVQRPVASINSILSLGDSYTDSSLFGSLSFNGIKLVTDERMRPQGKRGYAPEVRG
VAASSAHVVVKQLGKVIYETNVPPGPFYIDDLYNTRYQGDLEVEVIEASGKTSRFTVPYSSVPDSVRPGN
WHYSLAFGRVRQYYDIENRFFEGTFQHGVNNTITLNLGSRIAQRYQAWLAGGVWATGMGAFGLNATWSNA
RAEHNDRQQGWRAELSYSKTFTTGTNLVLAAYRYSTNGFRDLQDVLGVRREAKTGIDYYSDTLHQRNRLS
ATVSQPLGRLGTLNLSASTADYYNNQSRITQLQMGYSNQWRNISYGVNIARQRTTWDYDRFYHGVNEPLD
VSSRQKYTETTMSFNVSIPLDWGENRTSVAMNYNQSSQSRSSTVSMTGSSGENSDLSWSVYGGYERYRNS
NSDSSAPTTFGGNLQQNTRFGALRANYDQGDNYRQEGLGASGTLVLHPGGLTAGPYTSDTFALIHADGAQ
GAIVQNGQGAVVDRFGYAILPSLSPYRVNNVTLDTRKMRSDAELTGGSQQIVPYAGAIARVNFATISGKA
VLISVKMPDGGIPPMGADVFNGEGTNIGMVGQSGQIYARIAHPSGSLLVRWGTGANQRCRVAYQLDLHTK
EPFLYLNKICEKE
>gnl|CDD|237930 PRK15249, PRK15249, fimbrial chaperone
MKMDTRHSALYYLIVFLFLALPATASWASVTILGSRIIYPSTASSVDVQLKNNDAIPYIVQTWFDDGDMN
TSPENSSAMPFIATPPVFRIQPKAGQVVRVIYNNTKKLPQDRESVFWFNVLQVPPTNIGSDSGQNKMLVM
LRSRIKLFYRPDGLGKPDNLAKKLQIKTVNKGSGKSGIVIVNPQPWFASLSNLNVKVNGASYNLDADMIA
PFSSQTWWLPGKRSLKSFSGTVTVTLVNDQGARISESYDVPHH
>gnl|CDD|185162 PRK15250, PRK15250, type III secretion system effector cysteine hydrolase SpvD
MRVSGSASSQDIISRINSKNINNNDSNEVKRIKDALCIESKERILYPQNLSRDNLKQMARYVNNTYVHYS
GNCVLLSACLHYNIHHRQDILSSKNTASPTVGLDSAIVDKIIFGHELNQSYCLNSIDEVEKEILNRYDIK
RESSFIISAENYIAPIIGECRHDFNAVVICEYDKKPYVQFIDSWKTSNILPSLQEIKKHFSSSGEFYVRA
YDEKHD
>gnl|CDD|237931 PRK15251, PRK15251, cytolethal distending toxin subunit B family protein
KLVFMKLILLIILLFSFAFANLEDYKVATWNLQGSSASTESKWNVNVRQLLSGENPADILMVQEAGSLPS
SAVPTGRHVQPGGVGIPIDEYTWNLGTRSRPNQVYIYYSRVDVGANRVNLAIVSRRRADEVIVLRPPTVA
SRPIIGIRIGNDVFFSIHALANGGTDAGAIVRAVHNFFRPNMRHINWMIAGDFNRSPDRLESTLDTEHLR
NRVNIVAPTEPTQRSGGTLDYAVTGNSNQTFGPPLLAASLMLASLRSQLASDHFPVNFRRF
>gnl|CDD|237932 PRK15252, PRK15252, putative fimbrial-like adhesin protein
MEIRIMLFIVMMMVMPVSYAACYSELSVQHNLVVQGDFALNQTQSATYEHNFNDSSCVSTNTITPMSPSD
IIVGLYNDTIKLNLHFEWTNKNNITLSNNQTSFTSGYSVTVTPAASNAKVNVSAGSGGSVMINGVATLSS
ASSSTRGSAAVQFLLCLLGGKSWDACVNSYRNALAQNAGVYSFNLTLSYNPITTTCKPDDLLITLPSIPV
SQLPATGNKTTINSKDGDIILRCKNLLGQQNQTSRKMQVYLSSSDLLTNSNTILKGAENNGVGFILESNG
KPVTLLNITNSSKGYTNLKEIAAKSKLTDTTVSIPITASYYVYDTNKVKSGALEATALINVKYD
>gnl|CDD|185165 PRK15253, PRK15253, putative fimbrial assembly chaperone protein StcB; Provisional
RRRSSPVFYKQGRVNMKILSAVLLSAIILPAHAGIVIYGTRVIYPAEKKEVVVQLVNQGEQASLVQSWID
DGNTSLPPEKIQVPFMLTPPVARVAAESGQQIKIKKMPNSLPDNKESLFYLNVLDIPPNSQENAGKNVLK
FAMQNRIKLIWRPSRIAAVTKDSFQRIGLFRSNKTVIMKNDTANWITVTDVKAGNTKINDQTIMLPPLST
QNINMKYASTSQYEVTIIDDNGNYISSKINVK
>gnl|CDD|185166 PRK15254, PRK15254, fimbrial chaperone protein StdC; Provisional
VILLALAAAWSQYSPAAVNVDRTRIIMDAPQKTVAITLNNDDKTTPFLAQSWVTDADGVRTDALMALPPL
QRIDAGQKSQVRITQVRGLTDKLPQDRETLFWFNVRGVPPKPEDDNVLQLAMQSQLKLFYRPKAIIRSSS
DQPERKLTAERNAGHLTLRNPTPYYITVAWLGADRSHRLSGFREGVMVPPLGSLPLKAVLPAETRTLWVG
YIDDYGGLQMNRYACDALNCAFKDAGATS
>gnl|CDD|185167 PRK15255, PRK15255, fimbrial outer membrane usher protein StdB; Provisional
MKITRLAILITLTFSVLKSQATEFNASLLDSGNLSNVDLTAFSREGYVAPGNYILDIWLNDQPVREQYPV
RVVPVAGRDAAVICVTTDMVAMLGLKDKIIHGLKPVTGIPDGQCLELRSADSQVRYSAENQRLTFIIPQA
WMRYQDPDWVPPSRWSDGVTAGLLDYSLMVNRYMPQQGETSTSYSLYGTAGFNLGAWRLRSDYQYSRFDS
GQGASQSDFYLPQTYLFRALPALRSKLTLGQTYLSSAIFDSFRFAGLTLASDERMLPPSLQGYAPKISGI
ANSNAQVTVSQNGRILYQTRVSPGPFELPDLSQNISGNLDVSVRESDGSVRTWQVNTASVPFMARQGQVR
YKVAAGRPLYGGTHNNSTVSPDFLLGEATWGAFNNTSLYGGLIASTGDYQSAALGIGQNMGLLGALSADV
TRSDARLPHGQKQSGYSYRINYAKTFDKTGSTLAFVGYRFSDRHFLSMPEYLQRRATDGGDAWHEKQSYT
VTYSQSVPVLNMSAALSVSRLNYWNAQSNNNYMLSFNKVFSLGDLQGLSASVSFARNQYTGGGSQNQVYA
TISIPWGDSRQVSYSVQKDNRGGLQQTVNYSDFHNPDTTWNISAGHNRYDTGSNSSFSGSVQSRLPWGQA
AADATLQPGQYRSLGLSWYGSVTATAHGAAFSQSMAGNEPRMMIDTGDVAGVPVNGNSGVTNRFGVGVVS
AGSSYRRSDISVDVAALPEDVDVSSSVISQVLTEGAVGYRKIDASQGEQVLGHIRLADGASPPFGALVVS
GKTGRTAGMVGDDGLAYLTGLSGEDRRTLNVSWDGRVQCRLTLPETVTLSRGPLLLPCR
>gnl|CDD|185168 PRK15260, PRK15260, fimbrial protein SteF; Provisional
MNRIFQTAGHLIGGVMLWAVCNTLPAATPNVHYSGKLVAGACNLVVDNDTMATVDFHTIGSDNFDASGQT
TPVPFTLSLQDCKTALANGVLVTFQGVEDSTLPGLLALEPSSEASGFAIGVETAAQQPVSINATVGTAFV
LKEGITTINLQARLQKYAGEEVMPGEFSGSATVSFEYQ
>gnl|CDD|185169 PRK15261, PRK15261, fimbrial protein SteA; Provisional
MKSSHFCKLAVTASLVMGIVSGAQAAGSNTAKVTFLGNIVDSPCSVTLDTEDQTVNMGSSIGNGTLSNGK
TTINNARTFHIDLEGCTWATEKNMNVVFTTGSGTTAATGATDNLALMKTDGTGAISNVSLAIGDAGKNNI
KLGDTYTQAIADLDGDTILDEKQSLNFTAWLVGAATGTVGTGEFSSAANVTISYL
>gnl|CDD|237933 PRK15262, PRK15262, putative fimbrial protein StaF; Provisional
TQRKLMKKIILFLGLLFALTSPPAYAGQDVDLTANIKNSTCQSGISNNGNVDLGTVGVGYFADNVTAETY
YPGGKEFTITVVDCALQGTGSVLNQLHFDFRPQSGVMATGSQQIFANEAVAGGAKNVGVVIFSIQDPANT
FNVLNSDGSSRSVYPVMTSALNNSSWKFYARMQKIDPALDVTSGQVTSHVLVDVYYE
>gnl|CDD|185171 PRK15263, PRK15263, fimbrial-like protein
LLYGLSASVVLAAGLFSVAAYAGTDSLGLTVNTTVEMGTCTAQLVDDSDTPISTIAFGDVYISELNAKTK
VKTFKIRFSDCAGLPNKKAQIKLTPRATCEGSSNDGAGFANGSTAADKATAVAVEVWTTDTPATDGATQF
SCVTPATQEVTISNATGTQVVDYPMSARLVVAKGKTVSDVTAGDFTAPATFTVTYQ
>gnl|CDD|185172 PRK15265, PRK15265, subtilase cytotoxin subunit B-like protein; Provisional
MRYLLSLSVFLIVSLNPAFAEWTGDNVEGMHSGMIINKFHSGQVDGKPYFCIEAFKPSTTITACSVKDTS
IWGASYNTLYDQAMYYYTTGKRIRVYYAPDVWTNNSFVRALTANALVGFSTCISESSCFGPDRK
>gnl|CDD|185173 PRK15266, PRK15266, subtilase cytotoxin subunit B; Provisional
IKKFVPVYTLLILIYSFNASAEWTGDNTNAYYSDEVISELHVGQIDTSPYFCIKTVKANGSGTPVVACAV
SKQSIWAPSFKELLDQARYFYSTGQSVRIHVQKNIWTYPLFVNTFSANALVGLSSCSATQCFGPK
>gnl|CDD|185174 PRK15267, PRK15267, subtilase cytotoxin subunit B-like protein; Provisional
MKKKLKVLTLALASISSVCYAAMADYDTYVSNVQINNLSYGVYTSGGKETQFFCIGLKHGSEAISINAMC
KVDVYGNHKQGFDNMLNTAKYYYTTGGDVRIYYKENVWRDPDFKSAFSSRELIAITTCSSSSYCMGPTVT
N
>gnl|CDD|185175 PRK15272, PRK15272, pertussis-like toxin subunit ArtA
MKKLIFLTLSIVSFNNYAVDFVYRVDSTPPDVIFRDGFSLLGYNRNFQQFISGRSCSGGSSDSRYIATTS
SVNQTYAIARAYYSRSTFKGNLYRYQIRADNNFYSLLPSITYLETQGGHFNAYEKTMMRLQREYVSTLSI
LPENIQKAVALVYDSATGLVKDGVSTMNASYLGLSTTSNPGVIPFLPEPQTYTQQRIDAFGPLISSCFSI
GSVCQSHRGQRADVYNMSFYDARPVIELILSK
>gnl|CDD|185176 PRK15273, PRK15273, fimbrial biogenesis outer membrane usher protein
MLLSASPYSASGKDIEFNTDFLDVKNRDNVNIAQFSRKGFILPGVYLLQIKINGQTLPQEFPVNWVIPEH
DPQGSEVCAEPELVTQLGIKPELAEKLVWITHGERQCLAPDSLKGMDFQADLGHSTLLVNLPQAYMEYSD
VDWDPPARWDNGIPGIILDYNINNQLRHDQESGSEEQSISGNGTLGANLGAWRLRADWQASYDHRDDDEN
TSTLHDQSWSRYYAYRALPTLGAKLTLGESYLQSDVFDSFNYIGASVVSDDQMLPPKLRGYAPEIVGIAR
SNAKVKVSWQGRVLYETQVPAGPFRIQDLNQSVSGTLHVTVEEQNGQTQEFDVNTASVPFLTRPGMVRYK
MALGRPQDWDHHPITGTFASAEASWGVTNGWSLYGGAIGESNYQAVALGSGKDLGVVGAVAVDITHSIAH
MPQDDGFDGETLQGNSYRISYSRDFDEIDSRLTFAGYRFSEKNFMSMSDYLDAKTYHHLNAGHEKERYTV
TYNQNFREQGMSAYFSYSRSTFWDSPDQSNYNLSLSWYFDLGSIKNLSASLNGYRSEYNGDKDDGVYISL
SVPWGNDSISYNGTFNGSQHRNQLGYSGHSQNGDNWQLHVGQDEQGAQADGYYSHQGALTDIDLSADYEE
GSYRSLGMSLRGGMTLTTQGGALHRGSLAGSTRLLVDTDGIADVPVSGNGSPTSTNIFGKAVIADVGSYS
RSLARIDLNKLPEKAEATKSVVQITLTEGAIGYRHFDVVSGEKMMAVFRLADGDFPPFGAEVKNERQQQL
GLVADDGNAWLAGVKAGETLKVFWDGAAQCEASLPPTFTPELLANALLLPCKMLEGQPPTAPQKSSPLPA
QPLIQEHTQTDGQPAAPVATTTQTPPIPLADNHAVNRKDME
>gnl|CDD|185177 PRK15274, PRK15274, putative periplasmic fimbrial chaperone protein SteC; Provisional
MNKTNHFKRQALIASVLLAAPLVSHSAIVPDRTRVIFNGNENSITVTLKNGNATLPYLAQAWLEDDKFAK
DTRYFTALPPLQRIEPKSDGQVKVQPLPAAASLPQDRESLFYFNVREIPPKSDKPNTLQLALQTRIKFFY
RPVAVARQVDKTHPWQTKLTLTYQGDGVIFDNPTPFYLVISNAGSKENETASGFKNLLIAPREKVTSPIK
GASLGSSPVVGYVDDYGGHRLLVFTCSGNTCKVNEEKTRDAEKKANK
>gnl|CDD|185178 PRK15275, PRK15275, putative fimbrial protein SteD; Provisional
MLTRWKILVLLCGGFVTGTEAAGTKTVQLELHLVVTQPPPCTVGGASVEFGDVLTTKVGDASQTKPVGYS
LNCDGRASDYLKLQIQGTTTTISGEQVLQTSVQGLGIRIQQAGNKQLVPVGITDWLNFTLSGSNGPELEA
VPVKEPTTQLAGGDFNASATLVVDYQ
>gnl|CDD|185179 PRK15276, PRK15276, putative fimbrial subunit SteE; Provisional
VLILTLLITQFACADNLTFHGKLINPPACTINNGETLEVSFGSVIIDNIDGVNYLTEIPWTLTCDSSFRD
DALTFTLSYLGTATPYSAKALTTNVPELGIELQQNGTVFPPGTSLTINESSLPTLKAVPVKQPGKEPAEG
DFEAFATLQVDYQ
>gnl|CDD|185180 PRK15278, PRK15278, type III secretion protein BopE; Provisional
MTYNPRIGGFTHVKQASFDVHVKRGEAQPRTSFAQQIKRIFSKIGETLGQLFRHRAPDSAPGRVRLQGVR
YVGSYRPTGDAKQAIRHFVDEAVKQVAHARTPEIRQDAEFGRQVYEATLCAIFSEAKDRFCMDPATRAGN
VRPAFIEALGDAARATGLPGADKQGVFTPSGAGTNPLYTEIRLRADTLMGAELAARPEYRELQPYARQQA
IDLVANALPAERSNTLVEFRQTVQTLEATYRRAAQDASRDEKGATNAADGA
>gnl|CDD|185181 PRK15279, PRK15279, type III secretion system guanine nucleotide exchange factor SopE
MTKITLSPQNFRIQKQETTLLKEKSTEKNSLAKSILAVKNHFIELRSKLSERFISHKNTESSATHFHRGS
ASEGRAVLTNKVVKDFMLQTLNDIDIRGSASKDPAYASQTREAILSAVYSKNKDQCCNLLISKGINIAPF
LQEIGEAAKNAGLPGTTKNDVFTPSGAGANPFITPLISSANSKYPRMFINQHQQASFKIYAEKIIMTEVA
PLFNECAMPTPQQFQLILENIANKYIQYTP
>gnl|CDD|185182 PRK15280, PRK15280, type III secretion system guanine nucleotide exchange factor SopE2
MTNITLSTQHYRIHRSDVEPVKEKTTEKDIFAKSITAVRNSFISLSTSLSDRFSLHQQTDIPTTHFHRGN
ASEGRAVLTSKTVKDFMLQKLNSLDIKGNASKDPAYARQTCEAILSAVYSNNKDQCCKLLISKGVSITPF
LKEIGEAAQNAGLPGEIKNGVFTPGGAGANPFVVPLIASASIKYPHMFINHNQQVSFKAYAEKIVMKEVT
PLFNKGTMPTPQQFQLTIENIANKYLQNAS
>gnl|CDD|185183 PRK15283, PRK15283, fimbrial major subunit StfA
MNTAVKAAVAAALVMGVSSFANAAGSNTGTVTFTGTIEDSPCSIVVGDEHQTVNLGHIGTGSLMGGKESS
KVDFHIGLENCAFTTEKEASTVFSAIGNESSANPGSVALMRIGGGEMAGSSIVIGNHLGSAIKLGDAYSE
NLTMNGSVAAAKQTLNFKAWVKGDSAASTIDTGEFSSTVNFTISYL
>gnl|CDD|185184 PRK15284, PRK15284, putative fimbrial outer membrane usher protein StfC; Provisional
MPDHSLFRLRILAWCIALAMSGGYVNAWAEDDIQFDSRFLELKGDTKIDLKRFSSKGYVEPGKYNLQVQL
NKQPLAEEYDIYWYASENDPSKTYACLTPELVAQLGLKEDIAKNLQWIHDGKCLKPGQLEGMEIKADLSQ
SALVISLPQAYLEYTDPDWDPPSRWDDGIPGLIADYSINAQTRHEENGGDDSNDISGNGTVGVNLGAWRL
RADWQTNYQHTRSNDDDDEFSGSSTQKNWDWSRYYAWRALPSLKAKLALGEDYLNSDIFDGFNYVGGSVS
TDDQMLPPNLRGYAPDISGVAHTTAKVTVSQMGRVIYETQVPAGPFRIQDIGDSVSGTLHVRIEEQNGQV
QEYDVSTASMPFLTRPGQVRYKLMMGRPQDWGHHVEGGFFSGAEASWGIANGWSLYGGALGDENYQSAAL
GVGRDLALFGAVAFDVTHSHTKLDKDSAYGKGSLDGNSFRVSYAKDFDELNSRVTFAGYRFSEENFMTMS
EYLDASDSDMVRTGNDKEMYTATYNQNFRDAGVSVYLNYTHHTYWDRPEQTNYNLMLSHYFNMGSIRNMS
ISVTGYRYEYDNQADKGVYISLSIPWGDNSTVSYNGNYGSGSDSSQVGYFSRVDDATHYQLNVGTSDNHT
SVDGYYSHDGSLAQVDLSANYHEGQYTSAGLSLQGGATLTAHGGALHRTQNMGGTRLLIDADGVANVPVE
GNGAAVYTNMFGKAVVADVNNYYRNQAYIDLNNLPEDAEATQSVVQATLTEGAIGYRKFAVISGQKAMAV
LRLRDGSHPPFGAEVKNDNQQQVGLVDDDGNVYLAGVKPGEHMQVFWEGVAHCEINLPDPLPADLFNGLL
LPCQQKGNSAPATPPEIKPVIQEQTQQVTPTEPPTSISANQ
>gnl|CDD|185185 PRK15285, PRK15285, fimbrial chaperone StfD
MMPLKRYNLAAVLLLLLGGYGSAQAAIAPDRTRLVFRGEDKSISVDLKNANSKLPYLAQSWVEDEKGVKI
TSPLIVVPPVQRIEPSAIGQVKIQGMPALASLPQDRETLFYYNVREIPPQSDKPNTLQIALQTRIKVFYR
PQALSKIDMQHPWQYKITLQRQGNGYQVSNPTGYYVVLSNASNRMDGTPARGFSPLVIAPKSNVTLGGDA
SELGHSPVLTYVNDYGARLPLIFNCTDNSCAVDEAKSRKS
>gnl|CDD|185186 PRK15286, PRK15286, putative minor fimbrial subunit StfE; Provisional
MRQWRLRLGTVTCAAMLSAVSMPLAAGSKTVNMTLTIVVNAAPPCTVTGGEVEFGNVLTTKVDGVNYRQA
VGYRLSCNGRVSDYLKLQIQGNAVTINGESVLQTDVDGLGIRLQTATDGALISPGNTQWLSFQYSGGSGP
AIEAIPVKNNGVTLTGGAFNAGATLVVDYQ
>gnl|CDD|185187 PRK15287, PRK15287, fimbrial minor subunit StfF
MKKMALTMLMGGSLAAQAADNLKFHGTLISPPNCTINNDQTIDVKFGNLLINKIDGTRYAQNVPYEITCD
STVRDETMAMTLTLSGSVSDFNPAAVNTSVAGLGIELRQNDQPFTLGSTITVNEQSIPVLKAIPVKKSGA
SLKEGGFDATATLQVDYQ
>gnl|CDD|185188 PRK15288, PRK15288, putative minor fimbrial subunit StfG; Provisional
MAKRQALLHGAACILCGALILPVSAADNLHFSGSLVASPCTLTMQGTGIAEVDFSSLDSSDFTPDGQSAR
KPLVFELTDCDSALSNGVQVTFTGTEATGMRGILAIDSYSGASGIGIGIETLSGVPVGMNDEEGAIFTLV
TGKNTLSLNAWVQRLPGEDLIPGRFSASALATFEYL
>gnl|CDD|185189 PRK15289, lpfA, fimbrial protein; Provisional
MKRNIIGGAFTLASLMLAGHALAEDGVVHFVGEIVDTTCEVTSDTADQIVPLGKVSKNAFSGVGSLASPQ
KFSIKLENCPATYTQAAVRFDGTEAPGGDGDLKVGTPLTAGNPGDFTGTGQAIAATGVGIRIFNQSDNSQ
VKLYNDSAYTAIDAEGKAEMKFIARYVATNATVTAGTANADSQFTVEYKK
>gnl|CDD|237934 PRK15290, lfpB, fimbrial chaperone
MSRKSCLIRLFKTTVSCKLFTAIILSVFLGQPALTYAGVVIGGTRVVYLSNNPDKSISVFSKEEKIPYLI
QAWVDPFNKEDKSKAPFTVIPPVSRLEPSQEKVLRIIHTKGVSLPDDRESVFWLNIKNIPPSASNKATNS
LEIAVKTRIKLFWRPASIRLIPEDAAPKVKWRREGRNLIAENPNPIHISVMDVIVDGHDVPLNMIRPFET
LTLPLPANSAGGQMTWRFINDYGAVSDPIKMTL
>gnl|CDD|185191 PRK15291, PRK15291, fimbrial protein StgD; Provisional
MRLWTIILFSCFMVLISPVCRAGDGICHAVKGTYIYNLNLNDARIPAEKNKAGTEVRDLETLTSSESYKV
GCSCLTHFSSTFREVYYTARSPLSIDTTRNGYTYYTLNDNLSIATSIAVLGRGFIAVPFEAEPNVVKDGM
NCYTDTVEGNLATLYTGSEVKVSFLINKPFVGQVAIPGTIVANLYGGLDASSSTASTDKLAEVRIVGDIV
APQSCEIDSGQVIEVNFGKIPVADFSTTQGTAAAGHKVTKTVQVKCTGMLDENIVYSTFNADPVDSSANM
MKVLGNDDVGIMIYDKWDRMVKVTGGKMDMDMGVNNGGAETNSLTFSAAPASATGARPQPGTFEAYATIT
LEITN
>gnl|CDD|237935 PRK15292, PRK15292, type 1 fimbrial protein
RRLYLALILLFLYSSHSYASCKRSGNEGAVSITPLPEQIVVDSGSYTAGTVLYDSGWISTSEVTMDNCSR
DYKVGFLYEAQSNTGATIGANIYSTGISGVGVRVKTQTNAGPYDDVMPIDNTYHNGDGNKYLGTHTAMAP
AYNLQLVATGGPITSGTATFQSPLARVSFRDSATEDSGGDILSHLYLGNTQLIMKAMGCRVETPALTFDM
GSINAGSFANSQTVGTAEQDILLSCEPGTNVSASVSAQPASGDNPDNTVIALSNASAPTSATGVGVQLNI
QAPDAGFFTDSLPINTKIDLFTSTRTTNADGSQTVSYSYFTNPDSPGGAMNMSTTLKISANYYKTGATVT
AGQANATGTLTLTYN
>gnl|CDD|185193 PRK15293, PRK15293, fimbrial protein SthD
MNMNRFAALAALLTFTGLALWSPSISAAYNTADAVDINVTGLIYADPCTVTVPDTLSLGQYARADIAVAG
GNTATIPFTIKMTNCPATTTKAAISFNGVPYPDPNYASAIYANSAANPAQDLGLQLFNLDGKSLVNLANN
VTYTVDINSNTHEANLPVAARMYTPYGKVTAGDFTSVVTITIAWQ
>gnl|CDD|185194 PRK15294, PRK15294, fimbrial outer membrane usher protein
MQFSRVEPRSQLALSFLFICCSIKPALAHDHFNPLSLENDEPGVENVDLSVFEKGGQAEGTYNVDIYINN
TSVETKNIAFKNKKSADNKLSLQPCLSVEQLKQWGVKTENFPELKNDPNGCTDLSLLAGAVAKFNVIGNR
LDLAIPQIALIADPREFVPTSEWDEGINAFLLNYSFTGSQDHDIDENRTENSEYANLRPGINIGAWRFRN
YSTWNHDSDGQNSWDSAYTYVSRDIEFLKGQLIAGENNTPADVFDSISFKGVQISSDDDMLPDSMKGFAP
VIRGVAKSSAQVTVEQNGYTIYKTNVPAGPFAINDLYPTGGSGDLYVTIKESDGSEQHFIVPYASVPVLQ
REGHLKYDLTVGRTRSSDTHSAQQNFAELTALYGLAGGITAYGGIESTLSNDVYHAALIGTGLNLGDLGA
LSLDVTNSWSKIKAGDVVSDTLTGQSWRIRYSKDIQSTGTNFTVAGYRYSTKDYYALEDVLDTYSDNSHY
DHVRNRTDLSLSQDIIYGSISLTLYNEDYWNDTHTTSLGIGYNNTWHNVSYGINYSYTLNADNSQDEDDD
TEDSNDQQISINISIPLDAFMPSTYATYNMNSAKDGDTTHTVGLNGTALAQKNLSWSVQEGYSSQEKATS
GNVSATYNGTYADINGGYSYDNHMRRLNYGVQGGVLLHRNGLTLSQPMDDTIILVKAPGAAGVPVNNETG
VDTDFRGYAVVPYASPYHRNEVSLDTTGIRKNIELIDTSKTLVPTRGAVVRAEYKTNIGYKALMVLTRIN
NLPVPFGATVSSLTKPDNHSSFVGDAGQAWLTGLEKQGRLLVKWGPTAADRCQVSYRIPSSPSASGVEIL
HEQCQ
>gnl|CDD|237936 PRK15295, PRK15295, fimbrial assembly chaperone
KHIKKSVLVVLLTSHVAHASIVVGGTRLVFDGNNDESSINVENKDSKANLVQSWLSVVDPQVTNKQAFII
TPPLFRLDAGQKNSIRVIRSGAPLPADRESMYWLNIKGIPSIDDNASANRVEISINTQIKLIYRPPALTK
STPDSQSQQLKWQTAGDVITVNNPTPYYMNFASVTLNSHEVKSATFVPPKSSASFKLGSTAAPHGTVTWR
LISDYGMSLEPHSGSF
>gnl|CDD|185196 PRK15296, PRK15296, fimbrial protein SthA
MFNKKIIILAMLTAVASTPVFAQNTITFNGKIYDQACTVQVNGSTDTTIDLGNYSKERIAEKGATTDYVP
FTVSLVSCPEAGTGVPTQAMFRFHGATDDSNPTYFKNADEGSETGAAGVGISIQNASHSDVTDNTDDAAV
NLPTDGSTADFTYYAAMANDGSATVTGGDVSTQVTYTVSYQ
>gnl|CDD|185197 PRK15297, PRK15297, fimbrial protein
MKNLWMLLALSLFSGHALADGTMGNGSGWCQPTSGTHNFFFPLDQTITDTDENQAGKIVKESWSVGGEYS
ARCDCDNKDYQGVNYFTATTGDLTQKGTYSEAGSNGQQMDFYVLVAGKLEIGTETYIVGNLKQYIPVPFS
AISNQDPTAGGCTGADINKMSAGNKGNVRIYITHPLVGEITIPETTIMNLYLSKTPGSSGDNIPPSVPPM
AHVTMSGTITVPQSCSINAGQVIEVRLPDIEGKDIRHLGDSPQNSHVTTQVNFTCSNVADGTNLSMSLNG
ATDPHNPDYLKTDNENLGIRISDKYDNTIVPGGSAELPIEDYTDGKGSTEFTAAPVNTTGHVPHTGEYQA
TATLEIQIR
>gnl|CDD|185198 PRK15298, PRK15298, fimbrial outer membrane usher protein
MRKRQHRVFYLSRCAVCIALGSTFAHVAWARDYFNPAFIENHGQANRTSVDLSTFDNDKSQLPGTYYVTI
NINKTEIGARNVDFQLATLSDGQQALQGCLRLQELKDNGVKTDLFPTLESEKGCVDLSVIPGASQRFDFQ
QQALSVSIPQLYIANNARGYVPPEKWQEGITALMLNYSFSGYKEYGSSEDSDDAESKYLALQPGFNLGPW
RFRNYSNWSSNNGESGSWNSVYNYLQRDIIALKSQFTAGDSNTPSDVFDSVPFRGLQLTSDDQMQPNSQR
GYAPTIRGIARSNAQVIVRQNGYIAYQTAVSPGEFEINDMFPTGSNGDYDVTVKEADGSEQHFIVPYSSL
PILQRTGRAKYSVTVGKYRDYNNHTLDDFGQATLLYGLPWGITLYGGSQIAGDKYQSVAFGVGQNMQMLG
AISLDGIWSHAKFDDGRKEIGQSWRVRYSKGVVSTGTTFSLAGYRYASENYNSLSEVINPDDDFYDNYGK
RHNRFEASVNQQISNTLGSLTLSWVKEDYWHSAQQMESLSASYNNSWGPVSYTLSYSYNKNTYQYRSDND
DDDNDDDRYNQNDRLFTLSLHVPFTVFDSRLYASYMLNTRKHDATVNSTTLSGTALRDRNLNWSLQQSHS
TQDGDSGGVNASYKGTYANLNAGYNQSPDSQQVSYGISGGILAHENGITLSQPITGAAILIKAPGASGVS
VENQTGVATDFRGYTVIPNVTPYYRYDISLDSSTFADNVDIPLNNQTVYPTRNAVVRAAYDTHKGYRVLL
TLTRSNGEPVPFGATASVDGQDANLASIVGDKGQVFLSGLPEEGLLLVNWGSASCRADYRLDISKNMNGI
VMANAVCQ
>gnl|CDD|185199 PRK15299, PRK15299, fimbrial chaperone protein StiB; Provisional
MNSLAKAGLLCCLLCGSLAHAAGINIGTTRVIFHGDAKDASISISNSDNVPYLIQSWAQSISETGASGDA
PFMVTPPLFRLNGGQKNVLRIIRTGGNLPEDRESLYWLDIKSIPSSNPDNKHNTLMLAVKAEFKLIYRPK
ALTQKPEEVADRLTWSRQGRTLTVKNPTPYYMNFATLSVGSQKVKAPRYVAPFGNAQYTLPAAASGPIAW
SIINDFGGTGPEHKQTP
>gnl|CDD|185200 PRK15300, PRK15300, fimbrial protein StiA; Provisional
MKLSLKTLTVALAAITLSPAALADTAKDGTVHITGLIKQNACTVKTDSVEVTLQEEFASLFTAAGQTAGD
TDFTIELENCDANVYSSVQARFEGTLDGTDATILKNEDDAENIGVQILDKTSTPMTFNDLQAWSAAVALP
TAEGVTELSMPFTARYIATAVPVKSGTVDATATFYLQYN
>gnl|CDD|185201 PRK15301, PRK15301, hypothetical protein; Provisional
SKWLGIAILCAFAALLLPSARADDDCQLTLSRPEVNYGQMRRDDIVGSQQNWNKMPEREVNVSVSCPEPQ
QMALFVQGAAGEKGRFLFGNNGGLAVKVSQMILDGKSYPIGKTTDRVNFTPEDSALDSLLLRNNEGIIAM
DNNQVASGKQMNFTLTLTPVLNDSQFTHVTDNTMLESNLQWEVLTK
>gnl|CDD|185202 PRK15302, PRK15302, hypothetical protein; Provisional
MKKILLITAIAASFATTSVNADTTAVLKVTGQLVVGGCTPELSGGGVVDYGTIRLATLSATDVNQLGTKD
VSLSISCPSATKAAWTITDDRADTHPGASVISIANGDMTNGIVSDTTMSYGVGKTTEGVKIGAFSIYTDT
ANVTADGVKSDAISGTVDSPVWQKSTTGIIKNGNMEMFTVATKGTTEPVPYTLAIFPLKTSLAIQNTATL
AITDDTDLDGQATITLKYL
>gnl|CDD|185203 PRK15303, PRK15303, hypothetical protein; Provisional
MKKLLIATSVIIGLSTSAQAVESTAVLKLTGVLTNGACIPELSDGGVVDFGTKAVSDLLPTETNQLGYKD
ITLTIQCLAPAKVGWTVTDNHGDSATTLTIDNATFGGQNNRIPNYQLGLGKTADGIKIGAYGLSIDANNS
TADGVKTKMVASSDSNPGVWALASNEYVALTNTFPTRTTYSVGDGNGPAAFTTATFPIRVAAAIQGTDTL
AITDNTTLDGQATFTLVYL
>gnl|CDD|237937 PRK15304, PRK15304, putative fimbrial outer membrane usher protein; Provisional
MKKKLLLALYIATAFYCSLPTTTFTALAAEVTFDTDILKSRGLDPNIAHYFSRAPRFLPGSHSVMVKING
KKRGSLAARFDEEGQLCVDDDFLQAAGLVPLPISAKETCHDLQEDYPSATITPLPNQESLELVVPPEALD
NDLLRLNNVIHGGTAALLNYSLFSSRYEYSGGDSDYSQASLEAGFNFADWTLRSRQFLTDTDGEFSTDSL
YTYAQHTFTDQKTLMQVGQINVNNSLFSGASIYGVQLMPENALQQDGSGVTVTGIARTSQARVEIRQSGQ
LIYSTLVPAGAFTLDDVPVINGNTDLNVTVVETDGSTSHFTVPASSFNLNELSRPQGLTMAIGRVRDTDS
DYSQPWVYNASDGWRLTPWMNLLAGGVLAENYQAAGARLDWVPLPKWTVSASMLGSQDSFGDSLQGHKTE
LDAGYSLPGSLGLSVSTARYSDGYRELTEALDDDYYSYKSSYSANVNWSHSLLGTFSLGYYYNQATDGDN
DSRYINASWGKTFKYASVSVNWQHAVSQDDENSNDDDMFYVNISIPLGRSRSINAYMRNQGDKTSYGLRN
MGSLSDNTSYYVSADRDHDESENSFNGSLNSNLHYTQLSVGAGTDGDDNRNYNATLSGGIAAHDQGVTFS
PYTIKDTFAIARLDEPVAGVEIATPQGPVWTDFWGQAVIPGLTEWRKSRVEVNTNTLPKNMDLANGTKMI
KAAHGAVSKVDFSVLNQRRVMLNVKRADGSPLPKGVSIVDEKGNYLTSAVDDGRVFLNDIDDIPALYAKD
DDMNRLCRIHYTLPEDQDKEAFYETAKGVCQ
>gnl|CDD|185205 PRK15305, PRK15305, fimbrial protein StkG
MKLFPYLAALLLLSASGVAYGALECKFYNGDTRQIMSPGVQPIITFHPSVQTATLLASGITMELTPEMHS
HCAVGDDGENIYQMTDNTLLEGYVDGKALFRTNIPGITYAIGLYPAGKGITGWFPVNPGQYYMTAYADDN
EGYFEHEKKWYAVMEIYQMPGFNGVPSGVGFISSIGGPLGHIVLGDPIGSESDHPRPLITISDMMFNIPF
SEPTCILTAPTTVNLGDWYRSDVEKDQTTEVPFQITGTCTGTIKVSFVAKSSYTNADKNLFTNSITSNSS
VTAAGGVGVKISSPAYSQIHADSSPEYIAVGNIIGMPVTSVNANFKAKLVKTGTEAVTPGIFGSSVTFQV
TYE
>gnl|CDD|237938 PRK15306, PRK15306, fimbrial protein
MKRNRLSLPIAALAVMAASGSALAANSTNLDVNFTATILETTCDMKLVGGTGSDTVQELIIGNSSGEVRI
DDVRAGTATADFKLVIVECPASLQSLKTSINGTPSGYSTKILTNGTKGSADYIGVSVARASKPDEPFVIN
STADSERLVWSEVEINSKEVPLIAIMKETKANSATTGAFSAVATFVFSYE
>gnl|CDD|185207 PRK15307, PRK15307, major fimbrial protein StkA; Provisional
MFLKKYGLAAAVAMTLSASSAMAADPDTGTITFHGLVTNNTCNISLDNKIDQDGNDFDITLPTVFVKDFA
TALGVNSTLGEKQFTLNLSECDNATLKDASAQFNSWGGSSATSGGLLVPPANLQGSATNVNLVLANNGNT
ATDLIKIDQPNNTQKATISTDGTGDLFYRVAYTQGQKWNADTSPVTSGTVQAQVAFTMIYN
>gnl|CDD|237939 PRK15308, PRK15308, fimbrial protein TcfA
GVLLCVAMLACGHARANMLVYPMAAEIGAGREEATSLFVYSKSDHTQYVRTRIKRIEHPATPQEKEVPAG
NDIETGLVVSPEKFALPAGTTRTVRVISLQAPEREEAWRVYFEPVAELEDDPQAGGKQNSSVSVNLVWGV
LLRVLPSDPRPALVTDGHHLLNTGNVRLGLIRAGNCDTTCHWQNIDRSVYPGGSADLPAGISSNAVRVEY
RTGANSPVISADLTAAGKDTMTAP
>gnl|CDD|185209 PRK15309, PRK15309, fimbrial protein TcfB
MYTECTYITVINNKARLFFMNMKTSFIAAAVALATVYSFSVSAVQKDITVTANIDSTLELLQADGSSLPS
TMKLDFMPGKGLVHKSLQTRLYSNDQTKSVNVKLLNAPQLINVLDPTKTIDMEVTLGGRSLTTTNSVLEA
KTLFPDGKTGDASALLNLDIGQKAGAALQNLPAGEYSGLVSLVISQAVTAG
>gnl|CDD|185210 PRK15310, PRK15310, fimbrial outer membrane usher protein TcfC; Provisional
MSRYFWMYYLLGLCSFTSQATLIPPPGFESLLEGQTEQIEVLLPGHSLGLFPVVVKPDTVQFMSPLMVLE
SSGLAALPAAERQKALAALSRPLLRNSNLVCGVSEAKDSSECGYVATDKEDVAVIFDENNGQLSLFLNRD
WLPDEERRDKRWLTPTPEGVSAFIHRQTLYLSDDLHSRNMTLNGSGALGLGDGRYLGGNWAAIWNQSEHY
NNSQAWFDNLFVRQDLGNQYYLQAGRMDQRNLSSATGGDFGFSLLPLSRFDGLRTGTTQAYVNHEVDQNA
TPVMVQVTRNARIDIYRGSELLGSQFLTPGMHTLDTHSLPPGSYPLALRVYEDGILRRTETQPFSKGGNS
FSAQTQWFIQGGLEDTGDKASHYDGETVMAAGFQTGLRKNISLTEGISLAHEAWYSETRLNSQHAVLDGT
LDLSAGILHGTDSTSGNTEQVTYNDGFSASLWRNHTESDACSGRHPQSVHASMTCQTSMNASLSVPVGNW
YALLGYSTSRTEGRPVYRGYDDNSDKENVFWRQAYIPASHRESAQASATYSLNMAGMNINTHGGVWRTRN
DGVNDDGLFMSVSVSYASQPPTMTGSNGYTSAGTDIHSSRNQKTQTSWNVNHVRSWQQDLYRELSVGFSG
YNDDSWSGSLGGRMSGRMGELSATISNSHQRNAGSASSLTAGYSSSLALSRNGLFWGGGQDGEPASGMAV
NVESEGDEGSSGKVVSVRGSSQPFSLGFGQQSLLLMEGYNATEVTIEDAGVSSQGMAGVKAGGGSRRYFL
TPGHLLVHNISASMSRLYVGRVLDKDGRPLLDAQPLNYPFLSLGPSGRFSLQSEHKESSLWLLSKNRILR
CPMSVHKRRDVMQVVGDVRCELSDVDALPQALQISPRVIRLLNVAGLLRHSVQEA
>gnl|CDD|185211 PRK15311, PRK15311, fimbrial protein TcfD
MSNKMKWTSMTAHWSAIINFIRKYVYPARIIAILLMAGATLPQVADAITVDLNYDKNNVPVITPVWSQEW
SVANVLGGWVCRSNRNENEGACEETHLVWWYAFGAYSKIRLRFREQISHAEITLILLGSVRDACYTGVIN
MNAAACQWGRSLKLRIPSEELAKIPTSGTWKATLVLDYLQWGGDDPLGTSTTDITLNVTDHFAENAAIYF
PQFGTATPRVDLNLHRMNASQMSGRANLDMCLYDGGVKARSLQMKIEGSNKSGTGFQVIKSDSADTIDYA
VSMNYGGRSIPVTRGVEFSLDNVDKAATRPVVLPGQRQAVRCVPVPLTLTTQPFNIREKRSGEYQGTLTV
TMLMGTQTP
>gnl|CDD|185212 PRK15312, PRK15312, antimicrobial resistance protein Mig-14; Provisional
MKIQEVKRILTRWQPSSFTLYREVFTQYGGSINMHPDIVDYFMKRHNWHFKFFHYKEDDKIKGAYFICND
QNIGILTRRTFPLSSDEILIPMAPDLRCFLPDRTNRLSALHQPQIRNAIWKLARKKQNCLVKETFSSKFE
KTRRNEYQRFLRNGGSVKSVADCSSDELTHIFIELFRSRFGNTLSCYPADNLANFFSQLRHLLFGHILYI
EGIPCAFDIVLKSESQMNVYFDVPNGAVKNECMPLSPGSILMWLNISRARHYCQERQKKLIFSIGILKPE
WEYKRMWSTPYFTGKSIC
>gnl|CDD|237940 PRK15313, PRK15313, intestinal colonization autotransporter adhesin MisL
MPTPQNYSFIAIAVSAALASMVFPSQAAWVDVDSLPSSGLVSQLPPELQAIIPAQASTGFTKVGTMPNYV
YQWNTGTIPVYGNGLTLNGPGAEAFEHTVTVIQNSGTGSPGVIFGNDLTIRTQSANAANNGRDVDGIRTH
GANTPDNPVFIITGDRTRIYVDGQDGDGINAGYNSLGQGWTGSANIYVGDDLYIKTTGSQGRGITANAMR
DASRAKNTIVVGNRAHIVTTGDSSEGLRTGQSGSLIRLGDDATIETSGASSTGIYAASSSRTELGNNATI
TVNGASAHAVYATNATVNLGENATISVNSASKAASYSKAPAGLYALSRGAINLAGGAAITMAGDNSSESY
AISTETGGIVDGSSGGRFVIDGDIRAAGATAASGTLPQQNSTIKLNMTDNSRWDGASYITSATAGTGVIS
VQMSDATWNMTSSSTLTDLTLNSGATINFSHEDGEPWQTLTINEDYVGNGGKLVFNTVLNDDDSETDRLQ
VLGNTSGNTFVAVNNIGGAGAQTIEGIEIVNVAGNSNGTFEKASRIVAGAYDYNVVQKGKNWYLTSYIEP
DEPIIPDPVDPVIPDPVIPDPVDPDPVDPVIPDPVIPDPVDPDPVDPEPVDPVIPDPTIPDIGQSDTPPI
TEHQFRPEVGSYLANNYAANTLFMTRLHDRLGETQYTDMLTGEKKVTSLWMRNVGAHTRFNDGSGQLKTR
INSYVLQLGGDLAQWSTDGLDRWHIGAMAGYANSQNRTLSSVSDYHSRGQVTGYSVGLYGTWYANNIDRS
GAYVDTWMLYNWFDNKVMGQDQAAEKYKSKGITASVEAGYSFRLGESAHQSYWLQPKAQVVWMGVQADDN
REANGTLVKDDTAGNLLTRMGVKAYINGHNAIDDNKSREFQPFVEANWIHNTQPASVKMDDVSSDMRGTK
NIGELKVGIEGQITPRLNVWGNVAQQVGDQGYSNTQGLLGVKYSF
>gnl|CDD|185214 PRK15314, PRK15314, outer membrane protein RatB; Provisional
MKSKKCVGFLPWLLLCALSLTPFFAQAVRSSGAWQELTEQTAAINGTPPQADSVTIPVYQGSVQLRSDAA
NPVDYSAKPSQFSTSDAGSALTLTNPHDTEGDIFAVPPLVWQAERAPTVTLVWADAATPDTPLDPQPVSN
ISFCAQNLAGRHLVVWSQLDTSTAIPPLWLLTRTGVPYNTAVEVLDQKFAVDIAPAVGDPVTLAADHLDE
SLNAAKVKAGESIMLTVTTKDCGGEPEGNVDFVITRGDAQNRQGVVNNAAPVRVGNTELTTTATEYHGTT
NAEGVATVVVTQANGPGVKTPLIAHPSSAPALKASVDVIFTTLTSPDSSSANMYGHMAETSTATVDGASY
TFYRPKLAAETDGEDRTASINNETWAQFNWGHADAHCDILPDARQLEGLKIARGDLATTLGWPVGLTSGD
EEYWSSSQGSTATDHISIDMRSRALTQMPDATQSLVSCVDKAPPAVTPKLVISADNFDSTVNAAKVKVGE
EINMKITVTDSATNKPLPYRYFNVYLGDEQNRQNQKNADIDAAHQWTDDPVIITNLAGSDGHYHGVTDAN
GQFSLVLTQDKGAGVLTPVRVVLFDGTEATQNVIFTVVTSPDVAQARMWGHMQGVVEAGNIYKRPLLAEE
AAQDTGSEFENNEYWATFNSVTAATNQCGTGQVPGQLLLDTLYQAHSGNAMETTYGWPTQKHSYIAADTD
GSTTAHVNLATGADSMFSGAEPNYLSCSGNELVTSLDVYFNGDESLRNAVAKVGEQITMNVHSVNALNGL
SVPNASFTVTMSHGKNRDNATTGFTDPSDGTLVMGGTPFGSSQASMTYQGMTDAEGNATLVIEQPQGVGL
LTPLSVLPVNSLITTPVNRSVKFTVPTSPDTPEAQMWGHMADTLTVGDMEFQRPKLAAEATAATRTQEQD
NETWARVSHADALNNPNAGGCEAGHLPRADQLAALYASSDGNKIHTVSGWPTTYDYWSSTFASAATWQAV
SLAAGGYTASGDASDYVSCLVSKNPTAASITIEPVDAALWYNANSEHAVKVKKGDTLQLKVTVKDASGNP
LPQAPFVLSRGDGYTRQGEKHIAGSGDGIVSAVVIDGDSLNDSATQIGGMTGENGSKIINVTRPDAHGTK
VAITAALYNNASATASIDTIFTVVTSPDSDKAKMWGHMPETTTAANGEVFKRPLLSAEIASGVTHGDNTE
NNEAWGIVDFEMANDACGAGYVPTLADMQSLYDARPGGAMNTQQGWPLDGKNYQDSTADLSRSTQNRYVK
SINLRDGGVGSLLWNEQLYFVCLQNAHPAATQITLTSPVYNDSDGFAKAKVGETIPVIITTRDAQGNPAA
DTPVIFTRGDSVGRANQEVNSSAAADIQINHSDGRSSGANYYTATGADGTLTLNISQDSGAGFKTPLTAA
IEHNGVTSAPLPVIFTVVTSPDTPKANYWGHMAETLTDSSGVAYRRPLLASEFSATPGKTLTIANGYYDK
GETWGMITVDKAWNGTGGGCGRDTLPTVANLQTLYGTYPDNAMRSRNGWPMTSSGNNNVSRYWWAGDYVI
SSDGTKSLYAAVNLFNDGNDVKTTTSTSMYYMQTCLASPRSAAASLTLTLAGQDETTGSAKAKKGEQMAA
TIDVKDAAGQPMKNVMVKISRGSSYNRANSATSSSSVTDDITLRNVMPSGLATYLLDTSAKYLYAQTDAQ
GQVTFTLAQDSTAGLKTTISAATMDGSNLTDSKDAIFTVVTSPDSDKAKYWGHMPETFTNSKGVEFKRPL
LRAELSSTADTSGYTENNETWYTWSRYPNMYQDTASPCDRLGLPTVNDLQTLYTDYPNGALTTTLGLPVA
SGKYWGAGNSVPDATHSDSQFQYVRLSDNNTLTTKANTATAQLCLAKRRDLSIELTSSDMDADKGAPVAK
KGESLPLTVTVRDGSGTPQPNTAIRLGRTLSIDRAGVVDGSSGGGMVLTSVAPSTGSMTFNCTVSSCTSY
WYGITDEDGKAQLEVTQDDSRGLRTPLQAMLVDDPLTVSDMDVIFTVITSPDSDKAKYWGHMPETVTNSA
GVKFRRPLLAAEMTSNSGTYLVNNETWPLVTAANTEKAGATGCDAEYQPLSGDLQTLYSDNPNGAIGTNY
GWPVAGNKSWWAADRAPNTGYYQFINLNSGGKGTASSSTATGAQVCLVEPRTSTPASITLTSTAMDSAKN
AAVVAKGSAMPLTVTVKDSSGNPVANVGFTLSRGDSKNRAGMVITDGDVAADAGADDLMLKELTPASASQ
SMTTTGIVFTGTTGSDGTATFTLNQDKSLGLKTPLTVKVTDNTTLHASLDVIFMVLTSPDTDKALFWGNM
SDTTSVNGKTLHRPWLQAEMLSGVTPVFTNGVHANNEYWAMAHTVDNTKWDIAKQCGSLSKAPDNNDLLT
LYHSISSLGWPTLGYPYLSKSTSSGGMYCGVDENTKSQNCAIKPAGTAGYATCVE
>gnl|CDD|237941 PRK15315, PRK15315, outer membrane protein RatA; Provisional
MDRNRQVNKVVHFLLTLLIMFAASIAPAQALLKGGTWQELNSVTGAVNGTAPLADGAIIPLYQGSTLLDP
SKTHDIEFSAMPRDFSADATSTSMRAVNSTDTEGDLFSDPPTIAWENRQPPAMGLVWADAATPDTPLSPQ
PVPNLTFCAQNLAGRQLVAWAQVEDETNVPALWLFTRTGVPNYATIPLLSPKVTLNIKPAVSDPVSVSGD
HVDASFEASKVKVGESITLTVTTKACDGEPAINAPFVIRREDAINRQGVVNNANPVRVGNTELTTAQTEY
HGVTDGQGNATVVVTQENGPGVKTRLIVSSQNYPTLTDNVDVIFTTITSPDSDKASMYGHMLESATATLN
GITYTFTRPKLAAEASGADKSVVDTNETWALFDWNGADNHCNILPDAEQLVQMRHEHSTLATYTGWPATD
DAEYWSSTKDQMSGYHAAVHMNSASVVRAADSDTLLVSCVDKAQPAAHPQITLSPQGPYKAQVGESIDLT
MTVVDRDTQKPLPYRYMELFIDPAKNRKGEHQDAWDNLRVTVDSEGMSASSPEHYTGVTDVNGQAHLTLK
HNSGLGVETPIRIVMPDDEGGNVELPFSVIFTVVTSPDVDGANMWGHMRGVVDAGNLYKRPLLAVEASHK
DGQFSENNEEWATFNSVASATAQCGVGQVPDQSSLAHLYSEHAGGQMESEHGWPTEDYFIAADSDASGTV
HVNLENGDSGKFTDTPNYLTCSANEMVAVLDVYFNDDPVIKNADAKVGEQVKMNIHSRNALNGMAIGNTD
FTITMANGRRRDGLTTGFTDTSNGEMQFDDVGYVAGQVYHGITDANGDATIILTQKKGVGLLTPLSIAPV
DSLISTPVSRSVKFTVATSPDTAKAKMWGHMADTITVGDWTFERPKLAGEVSNPLRTQDESNETWARVAH
SDAVGNPDAGGCAANRLPRIDQLEALYNANSGGKIHSIQGWPTYLNYWSSTYQSATTWKLIALTNGSEFA
NSNVSIYASCLASDNPVAASITIEPVDPSQWYDGSDVHAVKVKKGETMQLKVTVKDASGNPIPEAPFVLT
RGDGYDRRGEKYTAQDGDDLQGIVTPVVIDGESLAWTTTKMGSQTGTDGTRIISVTRPDTHGTRTAINAT
LYENAAVSASIDTIFTVVTSPDVSVARMWGHMAPSLTAADGAVYQRPLLYAELSSTDNTASKQETNETWA
VFHGPASEGANPARCAAGYYPAVEALDSLYSKYPSRTINTAQGWPVYYSYWSGSNSTSFSSGAKLDFYYA
VDLADGSRRSENSASSSDWQYQICATTPLPQATQITLTSPQAMDDAIQAVKAKNSESIPLLITTTDAMGN
PVPYATFSLKRDAGKARNTDYNKFVATNGTNMTVTPLTGAQQQFYYATSVLTGATGADGTLALTLAEPGG
IGLKNQLTANLNDTPTATSSLPVVFTVLTSPDSDKANMYGHMPETFTASNGAEFKRPLVYGEPSSEAHTD
TYFETNENWIMVNSFNTGNYGGCPMNQMAAIDDFTALYNDHPSGKVATDIGLPVGKRWWAGDSLLKGSTL
YWQYKDLKTGKNYSMSENPGNYYLQLCLTTSRSGLNIALSSDAWNADKSAAVAKKGETIPMTVTVTNDAG
QPQAGVAVLLTRDYAYSRGAVDKQYIEPGVIGEPVPFTTSPANMMLTPVAPAGTAVAFNNQNGLSTKWSG
FTGDDGKLRFTLTQDKSLGLKTSVTAALANQFDEAASVDAIFTVQTSPDTPYASYWGHMPDTVQVNGVTL
RRPYLKAELSAAPRDTWPFNNETWGTNYYYQSEHVETSLTHLCGSQENIASLDDLKALQSVIGTLQWPTT
SSWDYVSQDEGQSNKYYCSFNETTGQTTCTREKATTSGLGSCRVP
>gnl|CDD|185216 PRK15316, PRK15316, RatA-like protein; Provisional
MSLTLNKILVLCALLISAMLPGWSWAESAWQDSSDTVGEFNGTVPTADSASIPVYQGSVFLDPAKTHDVA
FTAKPSEFSADVSVSKLLVTNPQDREGDIIATPRWENQTPPAVSLVWADAATPDTLLDPQPVADRSFCAQ
GLAGRSLVAWAQPDPQQTMPLLYLLTSTGYPYESVLALADQKVTLKIAPAQGDLISVSAAGYDESSGAAK
MTVGGSITLTVTTKDCVGNVVGNIPFVIKRKDAENRQGVVNNTAPVKLGTTELTTTATEYRGTTDANGVA
TVTVTQANGPGVKTPLVASLAGIAQASETAVIFTVLTSPDVPQATMWGHMPDTLKARDYTFSRPKLAAEV
DNEGGTVNDHNETWSTFTWSGADKHCDILPGMRQFGALATVVPTSVQDVAGWPMQGNFYWSSLAGMSGQH
HAADVSNRSEAQKPDDTTFIVSCVDKEAPDVEPKLVLTPGSYDSTIKAMKVKVGEEASLRLTITDSKNND
QPLAYYYFSLHLDDGINRKNQTDAAWETHPVQIDGGSNVRKVDAHTYEGITDANGEATLTLTQPGGVGVK
THITARMRSDFTASDEKDVIFTVITSPDTDKARMWGHMLGIIEANNIFKRPRLADETDNELGSVRENNED
WALFDQNSSMQAECGLGHIPSQSSLHSLFAAHPANAIGTEYGWPTLQKAYLSAVEETSHASVNLATGNID
TYSGFKQNYLSCSGNEMVAKIAATTDRDVSAGSRAQAKVGDTITMTVRTFNALNNAPVPYTAFTITKDMG
KNRQGQTTGFDDPTRGAIEMNGTLYGTSQPSLVYAGTTDAQGFATVEIKQSQGVGLSTPLNIVPVNSYIP
NTVNYNVIFTTLTSPDAVGAQMWGHMDETITVDALTFARPRLAAEVFSPDGTLTENNEVWSRVSQANASS
TSKGGCGANMLPRRSQLSALYDANNGNGVQTVHGWPTQRQPYWSSSPADQVPHYYTIALNDGARTVGGST
AVYVSCLTTANNPASSITLEVVDPAQWNAAANAAKLKKGETLQVKVTVKDAQGNPLGDIPFTLKRGDGYT
RSEEKHVAGSGDALVAPVVVNGGLADETSLNNTAAAYSAMTGSDGTKILTITRPDTHGTKTSLTATLYSD
TTKKATLDTIFTVVTSPDSDKAKMWGHMPETVTAADGTVFKRPLLLKELSSTSGRTAIAEDNEDWAQFTQ
AQAISTSSNGCGSEYVPSQAGLESLYEANRGNAMKTVQGWPVASSYLSSTTGSSSLEQRDFKAVNLSSGT
SSIIPSATKELLTCQTTPIVKASQIVLEAADPTKFDRTNNVVKAKKGEEAVLRVTTKDAQGNPVGNTAFT
LKRNTSVNRANVSTTTSIASLAVTDAWGNTQNDFLSTTLVIYGVTGADGTTTFTLKQDQTTGLKTELTAA
LDSSSSTKSTLPVVFTVLTSPDSPKAKFWGHMAETATGDDGLIYRRPLLRDENSATTSIGTLVEEGEAWS
TFPSGQANDTSINGCGAEYVPTDNELRAIYAHQGSSALHDAIGWPVSRFYISNTVADTFTQTFTYDVVSL
KTGDETQMPSSGGALLSCRTTPVAVASQIIVEANDTAQFVKVDDTLSALKVKKGEDAVIRVVTKNAQGNS
VPNVPFILRREGSKNRQNAEMINKSITVINAAGASARMNSSSSLLYGVTGADGTTSFTVKQDDSMGLVTN
MYAQLYQLTIESNKLPVMFTVITSPDTPLASYWGHMAETFTTRSGIAFKRPLLTAEHPAGQSTMANNESW
LSLNTAAKNDVSKSDCGEPYQPLLSEFQELYSEHPNGAIGTDLGLPLTNTWWAYDKIAYANVWYDQSINL
SNGSSSRALSNTVAFVSCLVNPHAVAASIEMTSTALDAEKTASNDGRPSATAAKGTAIRMTVIVRDSGGN
LLPGANFNLIRGTALDRAKNRLDSTYDDLTIVPVTPAGVNMSLYNNGAQALLTTGSDGKATFDVTQNETY
GLATPLTATLMRDTTKSATMDVIFTVITSPNSPKAKYWGHMPDTFTSRAGVTFKRPLLAAEATLGSSVSN
NNESWSYLFYTNKVTPDCPVEYQPRLNELQGLYNDHPGGTILTDLGLPITAGSGNWWTYEMSTTDALTWY
YGVINLKTGQSTTTINGYALMLCLTQPHSAPASLTLSSTAYDEGRTASNGGTPTSSVKKGEMLPIVVTIK
DANGNPVGGEGVTLKRVQAKSRSGISVSSNTVDDLILDEVTPTSARISFNQNTSAWSGFTGSDGTITFNV
TQNNTVGLVTPFTASLARNPQVTANQDLIFTVVTSPDSAKANYWGHMPATLTAVNGAVFERPKLWSELTS
TSGVGKINNNNEDWPYFTPTQKSDASVSPCEVARQPLFNDLSSLSARYPNNTFVTETGWPAYYTWWAEDK
SADGKDQSVDLRNGTLYTGSTKSFQPCLANARSTVSSVTLTSTAFDAATQAAKVKKGEAMSVTVTVKDSA
GNTVPNVEFTLKRGEASPRNAGATLYGNVVAMDDLTVQPLSGSAVTLSESGNTISGMTGADGTASFTLRQ
DNTPGYKTPLTVTLANYASATDTLDAIFTVPTSPNVSSAHFWGHMADTVVVNSKSLHRPLLTTELPSGAN
PVSSPIINYENWASAHIIDASKWDIARQCGSIENAPTYNELELLHTVFNSLGWPSSPSFPYLSSQQCGMD
EGTGAQDCSITLINKPGLVTCFQ
>gnl|CDD|237942 PRK15317, PRK15317, alkyl hydroperoxide reductase subunit F; Provisional
MLDANLKTQLKQYLELLERPIELVASLDDSEKSAELKELLEEIASLSDKITVEEDSLDVRKPSFSITRPG
EDTGVRFAGIPMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNL
MAVLNPNITHTMIDGALFQDEVEARNIMAVPTVFLNGEEFGQGRMTLEEILAKLDTGAAARAAEELNAKD
PYDVLVVGGGPAGAAAAIYAARKGIRTGIVAERFGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYD
VDIMNLQRASKLEPAAGLIEVELANGAVLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFK
GKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGDKV
TGLTYKDRTTGEEHHLELEGVFVQIGLVPNTEWLKGTVELNRRGEIIVDARGATSVPGVFAAGDCTTVPY
KQIIIAMGEGAKAALSAFDYLIRNSAA
>gnl|CDD|237943 PRK15318, PRK15318, intimin-like protein SinH; Provisional
MLRWLRIIFLTFISGAAFAAPGADNSKEINVKSHESLPDLGSQSAEQEEQTNKGKSLKERGADYFINSAT
QGFENLTPEALESQARSYLQNQITSTAQSYLEDTLSPYGKVRTNLSVGEGGDLDGSSIDYFVPWYDNQST
VYFSQFSAQRKEDRTIGNIGLGVRQNFGKWLLGGNIFYDYDFTRGHRRLGLGTEAWTDYLKFSGNYYHPL
SDWKDSEDFDFYEERPARGWDIRAEGWLPAYPQLGGKLVYEQYYGDEVALFGTDNLQKDPHAVTLGLKYQ
PVPLVTVGTDYKAGTGDNNDLSVNATLNYQFGTPLKDQLDPDNVKAAHSLMGSRHDFVDRNNFIVLEYKE
KDPLDVTLWLKADATNEHPECVIKDTPEAAVGLEKCKWTINALINHHYKIVAASWQAKNNAARTLVMPVV
KANALTEGNNNHWNLVLPAWQYASTEEEQEALNTWRVRLALEDEKGNRQNSGVVEITVQQDRKIELIVNN
IADVDRSNHSHEASAQADGVDGVVMDLDITDSFGDNTDRNGNTLPEDNMTPQLYDANDKKVTLTNKPCTT
ETPCVFIASRDKEAGTVTLSSTLPGTFRWKAKAAPYGDSNYVDVTFLGDNIGGLNAFIYRVGAAKPVNLI
GKEKPHPTVNNTYRFVLWRDKNKDGVFQQSEKLTEEEMAQYDYKWEFTGKSTNGHVGAQANTMNEDLVIP
ATNKEAAQKFAANVEDGVQGYGIRVTYSKK
>gnl|CDD|185219 PRK15319, PRK15319, fibronectin-binding autotransporter adhesin ShdA
MRNMYVVASELARGHSKVKAQVCASETHSPNQKSEYGQIIKATRAALACAVAAALGFFSPLAMADNQVSY
ADAQTHVLDASTPPISYSGTDEGAALYVSGVATVGWQPTTVTGTGLVIETSGGGADDPDGGKYVSNAISL
DHYAILELTDAKITTTGIYTQGISAADGSTLTLTDSTLTIDGNFGVMTLYTGSEATLDGTIVEAANSSSA
QVQQGSTLNVLDGSTITLAQGQINVVAGNTATDEGSTLNLSDSSVSSAGTMSTIQGTNKAALNLTNATIT
HTNASGAAVQANNATTLDISGGNITSAGTGVYILASDARIDGATINADGDGIFITSKRKLTGYEDLNALT
VSDANVTSDTVALHVDGSTTINDPIELTDSTFTAPTAIKLGSKATIQAENTTLTGNIVQTDASSSSLSLS
QGSTLTGSVDAMFTTLSLDDTSQWNMTDPSTVGNLTNDGDITLGNASGSTGTLLTVDNTLTLQDGSQINA
TLDTANSSPIIKAANVTLDGTLNLSSTATFVAPETDEHFGSITLIDSQTAITTDFDSVTLDADTSAMPDY
LTINAGVDANDNTNYELSTGLSWYAGANSARAAHGTFTVDAGSTFTVTSELDETTATSNWNGSKLTKQGD
GTLILSNTGNDYGDTEIDGGILAAKDAAALGTGDVTIAESATLALSQGTLDNNVTGEGQIVKSGSDELIV
TGDNNYSGGTTISGGTLTADHADSLGSGDVDNSGVLKVGEGELENILSGSGSLVKTGTGELTLSGDNTYS
GGTTITGGTLTADHADSLGSGDIDNSGVLKVGEGDLENTLSGSGSLVKTGTGELTLSGGNDYSGGTTIIG
GTLTADHADSLGSGDIDNSGVLQVGEGELKNTLFGSGSLVKTGTGELTLNGDNDYSGGTTIDDGVLIADH
ADSLGTGAVANSGVLQVGEGELKNTLSGSGSLVKTGTGELTLSGDNSYSGGTTIIGGTLIADHADSLGTG
AVANSGVLQVGEGELENTLSGSGSLVKTGTGELTLGGDNSYSGDTTIADGTLIAANVNALGSGNIDNSGT
LMLDANGAFELANITTHSGATTALAAGSTLDAGQLTQEDGSTLSIDLGAATDDAVITADSVTLGGTLNVT
GIGSVTDSWTPEAYTYTLIDSDSAITSDFDDLTIAGMNREDVDFLTIDGKVDEADNTHYDLTASLSWYAD
RDNATTDAHGTFTLSDPDGSFNVAATLTDVDDTLDPGSRWDGKSLTKEGAGTLILSGDNDYSGGTTINEG
TLVAASTTALGTGLVDNNATLVLDADGEVSAVGGITTHSGATTQLALGTSLDLGDSALIQQDGSTLNVEL
NSDSVQPLITGGSATLGGDLVVSDASLQARASDAEFQSFKLMDMDSDISGDFTSLTMNLTDQPDYLTVTG
TINPEDASEYLLTEGLSWNATATSATPAHGTFTLGAGDSFEVTSVLGDKTGNGDWDGKSLTKLGAGKLTL
SGANTYTGDTNVQEGTLWLSGDGSIGEMGSQQAVNVASGATFGGSNGTTVNGKVTNEGTLVFGDSEETGA
IFTLNGDLINMGTMTSGSSSSTPGNTLYVDGNYTGNGGSLYLNTVLGDDDSATDKLVITGDASGTTDLYI
NGIGDGAQTTNGIEVVDVGGVSTSDAFELKNEVNAGLYTYRLYWNESDNDWYLASKAQSDDDDSGGDDTP
SDGGDDGGNVTPPDDGGDGGNVTPPDDGGDGGDVTPPDHGGDVAPQYRADIGAYMGNQWMARNLQMQTLY
DREGSQYRNADGSVWARFKAGKAESEAVSGNIDMDSNYSQFQLGGDILAWGNGQQSVTVGVMASYINADT
DSTGNRGADGSQFTSSGNVDGYNLGVYATWFADAQTHSGAYVDSWYQYGFYNNSVESGDAGSESYDSTAN
AVSLETGYRYDIALSNGNTVSLTPQAQVVWQNYSADSVKDNYGTRIDGQDGDSWTTRLGLRVDGKLYKGS
RTVIQPFAEANWLHTSDDVSVSFDDATVKQDLPANRAELKVGLQADIDKQWSVRAQVAGQTGSNDFGDLN
GSLNLRYNW
>gnl|CDD|185220 PRK15320, PRK15320, transcriptional activator SprB; Provisional
MRNVIIYGINWTNCYALQSIFKQKYPEKCVKTCNSLTALLHSLSDMPDAGLILALNPHEHVYLFHALLTR
LQNRKVLVVADRLYYIDRCVLQYFGVMDYVLKDELSCAIRSEREKLRLPEAWLRFCHRPQKKTVAATYAF
NAGETPEEVLFNINQYAWWNLPPGVTQAKYALLILLSSGHPAIELAKKFGLGTKTVSIYRKKVMYRLGMD
SSPLSLFRGLKLDAHLQRTAFAHNPAVPDDNCALPIAVGMN
>gnl|CDD|185221 PRK15321, PRK15321, type III secretion system effector protein OrgC
MLNNVDSAPLSNGGDVDLYDAFYQRLLALPESASSETLKDSIYQEMNAFKDPNSGDSAFVSFEQQTAMLQ
NMLAKVEPGTHLYEALNGVLVGTMNAQSQMTSWMQEIILSGGENKEAIDW
>gnl|CDD|185222 PRK15322, PRK15322, oxygen-regulated invasion protein OrgB
ILIKRETLERYFSAERLEQQARRRAKRILRQAEEEAETLRMYAYQEGYEQGMIDALQQVAAYLTDNQTMA
WKWMEKIQIYARELFSAAVDHPETLLTVLDEWLRDFDKPEGQLFLTLPVNAKKDHQKLMVLLMENWPGTF
NLKYHQEQRFIMSCGDQIAEFSPEQFVETAVGVIKHHLDELPQDCRTISDNAINALIDEWKTKTQAEVIR
>gnl|CDD|185223 PRK15323, PRK15323, oxygen-regulated invasion protein OrgA
LQIAPEMIVRPAARAAANELILAAWRLKNGEKECIQNSLTQLWLRQWRRLPQVAYLLGCHKLRADLARQG
ALLGLPDWAQAFLAMHQGTSLSVCNKAPNHRFLLSVGYAQLNALNEFLPESLAQRFPLLFPPFIEEALKQ
DAVEMSILLLALQYAQKYPNTVPAFAC
>gnl|CDD|185224 PRK15324, PRK15324, EscJ/YscJ/HrcJ family type III secretion inner membrane ring protein
MIRRYLYTFLLVMTLAGCKDKDLLKGLDQEQANEVIAVLQMHNIEANKIDSGKLGYSITVAEPDFTAAVY
WIKTYQLPPRPRVEIAQMFPADSLVSSPRAEKARLYSAIEQRLEQSLQTMEGVLSARVHISYDIDAGENG
RPPKPVHLSALAVYERGSPLAHQISDIKRFLKNSFADVDYDNISVVLSERSDAQLQAPGTPVKRNSFATS
WIVLIILLSVMSAGFGVWYYKNHYARNKKGITADDKAKSSNE
>gnl|CDD|185225 PRK15325, PRK15325, type III secretion system inner rod protein PrgJ
METDIVSLDDRLLQAFSGSAIATAVDKQTITNRIEDPNLVTDPKELAISQEMISDYNLYVSMVSTLTRKG
VGAVETLLRS
>gnl|CDD|185226 PRK15326, PRK15326, type III secretion system needle complex protein
MATPWSGYLDDVSAKFDTGVDNLQTQVTEALDKLAAKPSDPALLAAYQSKLSEYNLYRNAQSNTVKVFKD
IDAAIIQNFR
>gnl|CDD|237944 PRK15327, PRK15327, PrgH/EprH family type III secretion inner membrane ring protein
METSKDKTTTSPDPYIVRLLNSSLKGCEFPLLTGKTLFVVGQSDALTASGQLPDLPADSFFIPLDHGGVN
FEIQVDTDATEIILHELKEGNSEERSVQLNTPIQVGELLILIRPESEPWVPEILQPEKLEASAKKNEPRF
KNGIVAALAGFFIVGIGTVGTLWILNSPQRQAAELDSLLGQEKERFQVLPGRDKMLYVAAQNERDTLWAR
QSLARGDYDKNARVINENEENKRVSTWLDTYYPQLAYYRLHFDEPRKPVLWLSRQRNVLSKKELEVLSQK
LRALMPYADSVNITLMDDVTAAGQAEAGLKQQALPYSRRDHKGSVTFVIQGALDDGEIQRARQFVDSYYR
TWGGRYVQFAIELKDDWLKGKSFQYGAQGYVKMSPGHWYFPSP
>gnl|CDD|185228 PRK15328, PRK15328, type III secretion system invasion protein IagB
MHYFFIIVIWLLSINTAWADCWLQAEKMFNIESELLYAIAQQESAMKPGAIGHNRDGSTDLGLMQINSFH
MKRLKKMGISEKQLLQDPCISVIVGASILSDMMKIYGYSWEAVGAYNAGTSPKRSDIRKRYAKKIWENYR
KLKGMSAEEKNKRLSIASNK
>gnl|CDD|237945 PRK15329, PRK15329, chaperone SicP
MNTHTEWLAALGEALGLPLTFDDNGQCLLLLDTDLMISIRAKDDIWLLYGMIIPLSPVAGDSIWRQILVI
NLELAENGEGTLAYIDAAEALLLIHAITDLTNGYHEIVDQLEAFVSRVEALKNTLQEYAKVDADARGL
>gnl|CDD|185230 PRK15330, PRK15330, type III secretion system needle tip protein SipD
MLNIQNYSASPHPGIVAERPQTPSASEHVEIAVVPSTTEHRGTDIISLSQAATKIQQAQQTLQSTPPISE
ENNDERTLARQQLTSSLNALAKSGVSLSAEQNENLRSAFSAPTSALFSASPMAQPRTTISDAEIWDMVSQ
NISAIGDSYLGVYENVVAVYTDFYQAFSDILSKMGGWLLPGKDGNTVKLDVTSLKNDLNSLVNKYNQINS
NTVLFPAQSGSGVKVATEAEARQWLSELNLPNSCLKSYGSGYVVTVDLTPLQKMVQDIDGLGAPGKDSKL
EMDNAKYQAWQSGFKAQEENLKTTLQTLTQKYSNANSLYDNLVKVLSSTISSSLETAKSFLQG
>gnl|CDD|185231 PRK15331, PRK15331, type III secretion system translocator chaperone SicA
MDYQNNVSEERVAEMIWDAVSEGATLKDVHGIPQDMMDGLYAHAYEFYNQGRLDEAETFFRFLCIYDFYN
PDYTMGLAAVCQLKKQFQKACDLYAVAFTLLKNDYRPVFFTGQCQLLMRKAAKARQCFELVNERTEDESL
RAKALVYLEALKTAETEQHSEQEKE
>gnl|CDD|185232 PRK15332, PRK15332, SpaR/YscT/HrcT type III secretion system export apparatus protein
MFYALYFEIHHLVASAALGFARVAPIFFFLPFLNSGVLSGAPRNAIIILVALGVWPHALNEAPPFLSVAM
IPLVLQEAAVGVMLGCLLSWPFWVMHALGCIIDNQRGATLSSSIDPANGIDTSEMANFLNMFAAVVYLQN
GGLVTMVDVLNKSYQLCDPMNECTPSLPPLLTFINQVAQNALVLASPVVLVLLLSEVFLGLLSRFAPQMN
AFAISLTVKSGIAVLIMLLYFSPVLPDNVLRLSFQATGLSSWFYERGATHVLE
>gnl|CDD|185233 PRK15333, PRK15333, EscS/YscS/HrcS family type III secretion system export apparatus protein
MDDLVFAGNKALYLVLILSGWPTIVATIIGLLVGLFQTVTQLQEQTLPFGIKLLGVCLCLFLLSGWYGEV
LLSYGRQVIFLALAKG
>gnl|CDD|185234 PRK15334, PRK15334, type III secretion system protein SpaN
MGDVSAVSSSGNILLPQQDEVGGLSEALKKAVEKHKTEYSGDKKDRDYGDAFVMHKETALPVLLAAWRHG
APAKSEHHNGNVSGLHHNGKGELRIAEKLLKVTAEKSVGLISAEAKVDKSAALLSSKNRPLESVSGKKLS
ADLKAVESVSEVTDNATGISDDNIKALPGDNKAIAGEGVRKEGAPLARDVAPARMAAANTGKPDDKDHKK
VKDVSQLPLQPTTIADLSQLTGGDEKMPLAAQSKPMMTIFPTADGVKGEDSSLTYRFQRWGNDYSVNIQA
RQAGEFSLIPSNTQVEHRLHDQWQNGNPQRWHLTRDDQQNPQQQQHRQQSGEEDDA
>gnl|CDD|185235 PRK15335, PRK15335, type III secretion system protein SpaM; Provisional
MHSLTRIKVLQRRCTVFHSQCESILLRYQDEDRGLQAEEEAILEQIAGLKLLLDTLRAENRQLSREEIYT
LLRKQSIVRRQIKDLELQIIQIQEKRSELEKKREEFQKKSKYWLRKEGNYQRWIIRQKRFYIQREIQQEE
AESEEII
>gnl|CDD|185236 PRK15336, PRK15336, type III secretion system chaperone SpaK; Provisional
MQHLDIAELVRSALEVSGCDPSLIGGIDSHSTIVLDLFALPSICISVKDDDVWIWAQLGADSMVVLQQRA
YEILMTIMEGCHFARGGQLLLGEQNGELTLKALVHPDFLSDGEKFSTALNGFYNYLEVFSRSLMR
>gnl|CDD|237946 PRK15337, PRK15337, EscV/YscV/HrcV family type III secretion system export apparatus protein
MLNSLLNQARSRPELIILVLMVMIIAMLIIPLPTYLVDFLIGLNIVLAILVFMGSFYIDRILSFSTFPSI
LLITTLFRLALSISTSRLILLDADAGEIITTFGQFVIGDSLVVGFVIFSIVTVVQFIVITKGSERVAEVA
ARFSLDGMPGKQMSIDADLKAGIIDADGVKERRSVLERESQLYGSFDGAMKFIKGDAIAGIIIIFVNLIG
GISVGMTQHGMDLSSALSTYTILTIGDGLVAQIPALLISISAGFIVTRVNGDSDNLGRNIMSQLLSNPFV
LVVTAILALSIGLLPGFPLPVFLLLAVVLGVLFYFKKFRKKKKSAAEPDTSGGEAPLDIDEKAGSSLGLI
GDLDKVIPETVPLILLVPEARRPDLEKENLAERLRSQFFIDYGVRLPDILLRYSEGLDDNSIVVLINEIR
AAQFTIYFDLHRVVNYSDELVSLGINPTIIDSGGEQYYWVPHEDTEKLAKLGYVLRSAIDELYHCLSVLL
LHNINEFFGIQETKHLLDQLEKKYPDLLKEVYRHATVQRISEVLQRLLSERISIRNMKLIMEALALWAPR
EKDVIMLVEHVRGALARYICHKFAAGGELRAVVLSAEVEDAIRKGIRQTSGGTFLNLDPAESENLMDLLT
LALDDLGIAHRDIVLLVSVDIRRFVKKLIEGRFPELEVLSFGEIADSVEVNVIKTI
>gnl|CDD|237947 PRK15338, PRK15338, YopN/LcrE/InvE/MxiC type III secretion system gatekeeper
MIPGSTIGISFSRILARETSHQDATQHTDAQQAEAQQAAEDSSPGAEVQKFVQSTDEMSAALAQFRNRRD
YEKKSSNLSDSFERVLEDEALPKAKQILKLISVHGGALEEFLRQARKLFPDPSDLVLVLRELLRRKQLEE
IVRKKLESLLKHVEEETDPKTLKAGINCALKARLFGKALSLKPGLLRASYRQFLQSESHEVEIYSDWIAS
YGYQRRLVVLDFIEGSLLTDIDANDASCSRLEFGQLLRRLTQLKMLRSADLLFVKTLLSYPFTKAFNAEE
SSWLLLMLSLLQQPEEVDSLLADILGLNALLLSHKDHASLLQAIYQVCKALPSSLFYEEEWQEELLEALR
QMTDIAYKHEMAEQRRTNKKLS
>gnl|CDD|237948 PRK15339, PRK15339, EscC/YscC/HrcC family type III secretion system outer membrane ring protein
KKIILIARVLLCAALVLVVGALSSEKIPATGSGYVAKKDSLRSFFDAMSSQLKKPVIVSKLAARKQISGN
FDLHDPNALLEKLSLQLGLIWYFDGQAIYIYDASEMRNAVVSLRNVSLNEFNNFLKRSGLYNKRYPLRGD
NRKGTFYVSGPPVYVDLVVNAATLMDKQNDGIELGRQKIGVIRLNNTFVGDRTYNLRGQKIVIPGIATVI
ERLLNGEEQPSGRQASSEPPAMPPFSANGEKGKAANYAGGMSLQEALKQNAAAGDIKIIAYPDTNSLLVK
GTAEQVHFIEMLVKALDVAKRHVELSLWIIDLDKSDLEQLGVNWSGSITIGDKLGVSLNQSSISTLDGSR
FIAAVMALEQKKKANVVSRPVVLTQENIPAIFDNNRTFYTKLVGERNVALEHVTYGTMISVLPRFSADGQ
IEMSLDIEDGNEKTPQSDTTTSVDALPEVGRTLISTIARVPQGKSLLIGGYTRDANTDEVQSIPFLGSLP
LIGSLFRYSSKNKSNIVRVFLIEPREIVEPLTPDASESANDILKQSGQWSGDDKLQKWVRVYLDREVIK
>gnl|CDD|185240 PRK15340, PRK15340, AraC family transcriptional regulator InvF
MSFSESRHNENCLIQEGALLFCEQAVVAPVSGDLVFRPLKIEVLSKLLAFIDGAGLVDTTYAESDKWVLL
SPEFRAIWQDRKRCEYWFLQQIITPSPAFNKVLALLRKSESYWLVGYLLAQSTSGNTMRMLGEDYGVSYT
HFRRLCSRALGGKAKSELRNWRMAQSLLNSVEGHENITQLAVNHGYSSPSHFSSEIKELIGVSPRKLSNI
IQLADK
>gnl|CDD|185241 PRK15341, PRK15341, type III secretion system invasion lipoprotein InvH
MKKFYSCLPVFLLIGCAQVPLPSSVSKPVQQPGAQKEQLANANSIDECQSLPYVPSDLAKNKSLSNQNAD
NSASKNSAISSSIFCEKYKQTKEQALTFFQEHPQYMRSKEDEEQLMTEFKKVLLEPGSKNLSIYQTLLAA
HERLQAL
>gnl|CDD|185242 PRK15344, PRK15344, type III secretion system needle protein SsaG; Provisional
MDIAQLVDMLSHMAHQAGQAINDKMNGNDLLNPESMIKAQFALQQYSTFINYESSLIKMIKDMLSGIIAK
I
>gnl|CDD|237949 PRK15345, PRK15345, SepL/TyeA/HrpJ family type III secretion system protein
IKINEIKMTPPTAFTPGQVIEEQEVISPSMLALQELQETTGAALYETMEEIGMALSGKLRESYKFTDAEK
LERRQQALLRLIKQIQEDNGAALRPLTEENSDPDLQNAYQIIALAMALTAGGLSKKKKRDLQSQLDTLTA
EEGWELAVFSLLELGEVDTATLSSLKRFMQQAIDNDEMPLSQWFRRVADWPDRCERVRILLRAIAFELSI
CIEPSEQSRLAAALVRLRRLLLFLGLEKECQREEWICQLPPNTLLPLLLDIICERWLFSDWLLDRLTAIV
SSSKMFNRLLQQLDAQFMLIPDNCFNDEDQREQILETLREVKINQV
>gnl|CDD|237950 PRK15346, PRK15346, EscC/YscC/HrcC family type III secretion system outer membrane ring protein
MKKLLILIFLFLLNTAKFAASKSIPWQGNPFFIYSRGMPLAEVLHDLGANYGIPVVISPEINDTFSGKIR
DGPPVKILNELARRYHLTWYYDGNTLYVYKASEIKRQVITPTYLSAGRLIKYLQSQGILNGKSCEVKAIT
GTNALEVSGVPECIERVTQLAKVLDEQAQKRKQNKETVKVFPLKYASATDTTYQYRDQNVVVPGVVSVLR
EMAQGNSLPLPGSNAVEGSPASQALPVFSADPRQNAVIVRDRAANMAIYRSLITQLDQRPQMIEISVSII
DVDAGDINQLGIDWSASASLGGGKISFNSGFADGNASGFSTVISNTGNFMVRLNALEKNSKAKILSQPSV
VTLNNIQAVLDKNVTFYTKLQGEKVAKLESITTGSLLRVTPRLIDDNGTQKVMLNLNIQDGQQSATQSET
DPLPEVQNSEIATQATLKAGQSLLLGGFIQDKQIESQNKIPLLGDIPLIGGLFRSTDKQSHSVVRLFLIK
AEPVNNGIS
>gnl|CDD|237951 PRK15347, PRK15347, two component system sensor kinase
MKMTWQTSLVIRLTLLLGLTLIIIWLLSVATTAYFSFEQTRQHIIEELSHLSSMRADLSNQRFEGAERDA
KNLMYRCQSATEIDHNDIKPEVSRYIPFNPKNCDPTLNGKKDRWFIQAYGIAGQSYYLDSFILKPKEGIS
LFSPDKSSSDYLTLRPLELKQLPLQPTHNGIYWGKPEYIPGGGWHVSVAVADKQGVLVGFTVKLNDLISY
NHPVLDDDINLWLDQNGELLPFSTIPLSSNQLQKILNQLENVKLHDGWQQIPDYLVLRTQLKGPGWQQVT
LYPRRNLANEALKPALQQLPFALLILVLLTSVLFLLLRRYLAKPLWRFVDIINKTGPAALEPRLPENRLD
ELGSIAKAYNQLLDTLNEQYDTLENKVAERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGAL
ELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQS
KSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQ
QQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLNEYAPPEPLKGELSAP
LALHRQLSAWGITCQPGHQNPALLDPELAYLPGRLYDLLQQIIQGAPNEPVINLPLQPWQLQILLVDDVE
TNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDPDCMIV
ALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALELAAEYQLLRGIELSPQDSSCSPLLDTDDMALNS
KLYQSLLLLLAQIEQAVENQEVLSQLLHTLKGCAGQAGLTELQCAVIDLENALETGEILSLEELTDLREL
IHALFKNPTTC
>gnl|CDD|185246 PRK15348, PRK15348, EscJ/YscJ/HrcJ family type III secretion inner membrane ring protein SsaJ
MKVHRIVFLTVLTFFLTACDVDLYRSLPEDEANQMLALLMQHHIDAEKKQEEDGVTLRVEQSQFINAVEL
LRLNGYPHRQFTTADKMFPANQLVVSPQEEQQKINFLKEQRIEGMLSQMEGVINAKVTIALPTYDEGSNA
SPSSVAVFIKYSPQVNMEAFRVKIKDLIEMSIPGLQYSKISILMQPAEFRMVADVPARQTFWIMDVINAN
KGKVVKWLMKYPYQLMLSLTGLLLGVGILIGYFCLRRRF
>gnl|CDD|185247 PRK15349, PRK15349, EscT/YscT/HrcT family type III secretion system export apparatus protein
MAQQVNEWLIALAVAFIRPLSLSLLLPLLKSGSLGAALLRNGVLMSLTFPILPIIYQQKIMMHIGKDYSW
LGLVTGEVIIGFLIGFCAAVPFWAVDMAGFLLDTLRGATMGTIFNSTIEAETSLFGLLFSQFLCVIFFIS
GGMEFILNILYESYQYLPPGRTLLFDRQFLKYIQAEWRTLYQLCISFSLPAIICMVLADLALGLLNRSAQ
QLNVFFFSMPLKSILVLLTLLISFPYALHHYLVESDKFYIYLKDWFPSV
>gnl|CDD|185248 PRK15350, PRK15350, EscS/YscS/HrcS family type III secretion system export apparatus protein
MNDSELTQFVTQLLWIVLFTSMPVVLVASVVGVIVSLVQALTQIQDQTLQFMIKLLAIAITLMVSYPWLS
GILLNYTRQIMLRIGEHG
>gnl|CDD|185249 PRK15351, PRK15351, type III secretion system apparatus protein SsaP
MRITKVEGSLGLPCQSYQDDNEAEAERMDFEQLMHQALPIGENNPPAALNKNVVFTQRYRVSGGYLDGVE
CEVCESGGLIQLRINVPHHEIYRSMKALKQWLESQLLHMGYIISLEIFYVKNSE
>gnl|CDD|185250 PRK15352, PRK15352, type III secretion system apparatus protein SsaO
METLLEIIARREKQLRGKLTVLDQQQQAIITEQQICQTRALAVSTRLKELMGWQGTLSCHLLLDKKQQMA
GLFTQAQSFLTQRQQLENQYQQLVSRRSELQKNFNALMKKKEKITMVLSDAYYQS
>gnl|CDD|185251 PRK15353, PRK15353, type III secretion system apparatus protein
MDWDLITERNIQLFIQLAGLAERPLATNMFWRQGQYETYLNYHNGRIHLCQILKQTFLDEELLFKALARW
KPAAFQGIPQRLFLLRDGLAMSCSPPLSSSAELWLRLHHRQIKFLESQCVHG
>gnl|CDD|185252 PRK15354, PRK15354, type III secretion system apparatus protein SsaK
MSFTSLPLTEINHKLPARNIIESQWITLQLTLFAQEQQAKRVSHAIVSSAYRKAEKIIRDAYRYQREQKV
EQQQELACLRKNTLEKMEVEWLEQHVKHLQEDENQFRSLVDHAAHHIKNSIEQVLLAWFDQQSVDSVMCH
RLARQATAMAEEGALYLRIHPEKEALMRETFGKRFTLIIEPGFSPDQAELSSTRYAVEFSLSRHFNALLK
WLRNGEDKRGSDEY
>gnl|CDD|185253 PRK15355, PRK15355, type III secretion system protein SsaI; Provisional
MSVVPVSTQSYVKSSAEPSQEQINFFEQLLKDEASTSNASALLPQVMLTRQMDYMQLTVGVDYLARISGA
ASQALNKLDNMA
>gnl|CDD|185254 PRK15356, PRK15356, type III secretion system protein SsaH; Provisional
MFAGVNHSLISQVHAMLPALTVIVPDKKLQLVCLALLLAGLNEPLKAAKILSDIDLPEAMALRLLFPAPN
EGFEN
>gnl|CDD|185255 PRK15357, PRK15357, pathogenicity island 2 effector protein SseG; Provisional
MKPVSPNAQVGGQRPVNAPEESPPCPSLPHPETNMESGRIGPQQGKERLLAGLAKRVIECFPKEIFSWQT
VILGGQILCCSAGIALTVLSGGGAPLVALAGIGLAIAIADVACLIYHHKHHLPMAHDSIGNAVFYIANCF
ANQRKSMAIAKAVSLGGRLALTATVMTHSYWSGSLGLQPHLLERLNDITYGLMSFTRFGMDGMAMTGMQV
SSPLYRLLAQVTPEQRAPE
>gnl|CDD|185256 PRK15358, PRK15358, type III secretion systems effector SseF
IQAKEASFPPPEIPAPGTPAAPVLLTPEQIRQQRDYAIHFMQYTIRALGATVVFGLSVAAAVISGGAGLP
IAILAGAALVIAIGDACCAYHNYQLICQQKEPLQTASDSVALVVSALALKCGASLNCANTLANCLSLLIR
SGIAISMLVLPLQFPLPAAENIAASLDMGSVITSVSLTAIGAVLDYCLARPSGDDQENSVDELHADPSAL
LAEQMAALCQSATTPALMDSSGHTSRGEP
>gnl|CDD|185257 PRK15359, PRK15359, type III secretion system chaperone protein SscB; Provisional
MMMKEDQKNKIPEDILKQLLSVDPETVYASGYASWQEGDYSRAVIDFSWLVMAQPWSWRAHIALAGTWMM
LKEYTTAINFYGHALMLDASHPEPVYQTGVCLKMMGEPGLAREAFQTAIKMSYADASWSEIRQNAQIMVD
TLIA
>gnl|CDD|185258 PRK15360, PRK15360, pathogenicity island 2 effector protein SseE; Provisional
VQEIEQWLRRHQVFTEPAYLGETAILLGQQFILSPYLVIYRIEAKEMIICEFRRLTPGQPRPQQLFHLLG
LLRGIFVHHPQLTCLKMLIITDVLDEKKAMLRRKLLRILTVMGATFTQLDGDNWTVLSAEHLIQRRF
>gnl|CDD|185259 PRK15361, PRK15361, type III secretion system translocon protein SseD
MEASNVALVLPAPSLLTPSSTPSPSGEGMGTESMLLLFDDIWMKLMELAKKLRDIMRSYNVEKQRLSWEL
QVNVLQTQMKTIDEAFRASMITAGGAMLSGVLTIGLGAVGGETGLIAGQAVGHTAGGVMGLGAGVAQRQS
DQDKAIADLQQNGAQSYNKSLTEIMEKATEIMQQIIGVGSSLVTVLAEILRALTR
>gnl|CDD|237952 PRK15362, PRK15362, type III secretion system translocon protein
IHSNSDSAAGVTALTHHHLSNVSCVSSGSLGKRQHRVNSTFGQGNAACALSGPVSLQEASNALKRILDAV
PGNHKRPLSLSDFEQTPMDVMSMMATLLILSVFGDNAQSLCQALEIATEVQEALRDKQVKEYQEQIQKAI
EQEDKARKAGIFGAIFDWIVGIFETVIGALKVVEGFLSGNPAEMAGGAAYLAAGCAGMVKAAAETAMLCG
ADHDKCQAIIDVASKIQLGCEIVAMALDVFQIGRAFMATRGIAKAAEKVLDSGAGEELVERMVGGSEEAI
EELAEEFGKQVSEQVSKQVANELAEESAEFSRNVEKNMTRSLGKAFTKEAIEAMVTEAVEEALKKAVQEG
VKFLLKEFTKQVVKEVFKKVIKALIRACSFKGLQAIRCTTEGANQINTGMINTEKAKLQKKIEQLILQQR
FLDFIMEQYEKQKKIEQKRLEELYKGSGAALRDALDAIDQYGSVQARIAGSRA
>gnl|CDD|185261 PRK15363, PRK15363, CesD/SycD/LcrH family type III secretion system chaperone SscA
MKKDPTLQQAHDTMRFFRRGGSLRMLLDDDVTQPLNTLYRYAMQLMEVKEFAGAARLFQLLTIYDAWSFD
YWFRLGECCQAQKHWGEAIYAYGRAAQIKIDAPQAPWAAAECYLACDNVCYAIKALKAVVRICGEVSEHQ
ILRQRAEKMLQQLSDRS
>gnl|CDD|185262 PRK15364, PRK15364, type III secretion system translocon protein SseB
MSSGNILWGSQNPIVFKNSFGVSNTDTGSQDDLSQQNPFAEGYGVLLILLMVIQAIANNKFIEVQKNAER
ARNTQEKSNEMDEVIAKAAKGDAKTKEEVPEDVIKYMRDNGILIDGMTIDDYMAKYGDHGKLDKGGLQAI
KAALDNDANRNTDLMSQGQITIQKMSQELNAVLTQLTGLISKWGEISSMIAQKTYS
>gnl|CDD|185263 PRK15365, PRK15365, type III secretion system chaperone SseA; Provisional
MIKKKAAFSEYRDLEQSYMQLNHCLKKFHQIRAKVSQQLAERAESPKKSRETESILHNLFPQGVAGVNQE
AEKDLKKIVSLFKQLEVRLKQLNAQAPVEIPSGKTKR
>gnl|CDD|185264 PRK15366, PRK15366, type III secretion system chaperone SsaE; Provisional
MTTLTRLEDLLLHSREEAKGIILQLRAARKQLEENNGKLQDPQQYQQNTLLLEAIEQAENIINIIYYRYH
NSALVVSEQE
>gnl|CDD|185265 PRK15367, PRK15367, EscD/YscD/HrpQ family type III secretion system inner membrane ring protein
PKSSWKIRFLGHVLQGREVWLNEGNLSLGEKGCDICIPLTINEKIILREQADSLFVDAGKARVRVNGRRF
NPNKPLPSSGVLQVAGVAIAFGKQDCELADYQIPVSRSGYWWLAGVFLIFIGGMGVLLSISGQPETVNDL
PLRVKFLLDKSNIHYVRAQWKEDGSLQLSGYCSSSEQMQKVRATLESWGVMYRDGVICDDLLIREVQDVL
IKMGYPHAEVSSEGPGSVLIHDDIQMDQQWRKVQPLLADIPGLLHWQISHSHQSQGDDIISAIIENGLVG
LVNVTPMRRSFVISGVLDESHQRILQETLAALKKKDPALSLIYQDIAPSHDESKYLPAPVAGFVQSRHGN
YLLLTNKERLRVGALLPNGGEIVHLSADVVTIKHYDTLINYPLDF
>gnl|CDD|185266 PRK15368, PRK15368, type III secretion system protein SpiC
MLAVLKGIPLIQDIKAEGNSRSWIMTIDGHPARGEIFSEAFSISLFLNDLESLPKPCLAYVTLLLAAHPD
VHDYAIQLTADGGWLNGYYTTSSSSELIAIEIEKHLALTCILKNVIRNHHKLYSGGV
>gnl|CDD|185267 PRK15369, PRK15369, two component system response regulator
MKNYKILLVDDHELIINGIKNMLAPYPRYKIVGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQ
LHQRWPAMNILVLTARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTVAVGKRYIDPALNREAILALL
NADDTNPPLLTPRERQILKLITEGYTNRDIAEQLSISIKTVETHRLNMMRKLDVHKVAELLNWARRLGLI
E
>gnl|CDD|185268 PRK15370, PRK15370, type III secretion system effector E3 ubiquitin transferase SlrP
MFNITNIQSTARHQSISNEASTEVPLKEEIWNKISAFFSSEHQVEAQNCIAYLCHPPETASPEEIKSKFE
CLRMLAFPAYADNIQYSRGGADQYCILSENSQEILSIVFNTEGYTVEGGGKSVTYTRVTESEQASSASGS
KDAVNYELIWSEWVKEAPAKEAANREEAVQRMRDCLKNNKTELRLKILGLTTIPACIPEQITTLILDNNE
LKSLPENLQGNIKTLYANSNQLTSIPATLPDTIQEMELSINRITELPERLPSALQSLDLFHNKISCLPEN
LPEELRYLSVYDNSIRTLPAHLPSGITHLNVQSNSLTALPETLPPGLKTLEAGENALTSLPASLPPELQV
LDVSKNQITVLPETLPPTITTLDVSRNALTNLPENLPAALQIMQASRNNLVRLPESLPHFRGEGPQPTRI
IVEYNPFSERTIQNMQRLMSSVGYQGPRVLFAMGDFSIVRVTRPLHQAVQGWLTNLEEEDVNQWRAFETE
VNAAAFSMFLDRLSDTQNTRHPDFKEQVSAWLMRLAEDSALRETAFIIAMDATISCEDRVTLAYHQMQEA
TLVHDAERGAFDSHLAELIMAGREIFRLEQIESLAREKVKRLFFIDEIEVFLGFQNQLRESLSLTTMTQD
MRFYNVSGITESDLDEAEIRIKIAENRDFHKWFALWGPWHKVLERIAPEEWREMMAKRAECIETDEYQSR
VNAELEALGIAGDPDAERMAGMRIMEEINQTLFTEIMENILLKKEVSSLMSAYW
>gnl|CDD|185269 PRK15371, PRK15371, YopJ family type III secretion system effector serine/threonine acetyltransferase
MIGPISQINIEGNSSEKETSSEISNEELKNIITQLEDDIADGSWIHKNYARTDLEVMPALVAQANNKYPE
MNLKLVTSPLDLSIEIKETIENGVESSRFIVNMGSGGIHFSVIDYKHIDGKTSLILFEPANFNSMGPAML
AIRTKTALEREQLPDCHFSMVEMDIQRSSSECGIFSLALAKKLYLERDKLLKLHEDNIKGILCDGENPLP
HDKLDPYLPVTFYKHTQGKKRLNEYLNTNPQAVGTVVNKKGETLVERFDNNLSIVDGKELSVSVHKKRIA
EYKSLLK
>gnl|CDD|185270 PRK15372, PRK15372, type III secretion system effector SseI
MSSWEKMKEFFCSTHQTEALECIWTICHPPAGTTREDVVSRFELLRTLAYDGWEENIHSGLHGENYFCIL
DEDSQEILSVTLDDVGNYTVNCQGYSETHHLTMATEPGVERTDITYNLTSDIDAAAYLEELKQNPIINNK
IMNPVGQCESLMTPVSNFMNEKGFDNIRYRGIFIWDKPTEEIPTNHFAVVGNKEGKDYVFDVSAHQFENR
GMSNLNGPLILSADEWVCKYRMATRRKLIYYTDFSNSSIAANAYDALPRELESESMAGKVFVTSPRWFNT
FKKQKYSLIGKM
>gnl|CDD|185271 PRK15373, PRK15373, IpaC/SipC family type III secretion system needle tip complex protein
MLISNVGINPAAYLNNHSVENSSQTASQSVSAKDILNSIGISSSKVSDLGLSPTLAAPAPLVLTQTPGTI
TSFLKASIQNTDMNQDLNALANKVTTKANEVVQTQLREQQAEVGKFFDISGLSSSAVALLAAANVLMSAL
RTADSKLSGKLSLVSFDATKTTASSMVREGMAALSSSISQSVLQVGITGVGAKKEYKGLQNERGALKHNA
AKIDKLTTESHSIKNVLNGQNSVKLGAEGDSLKSLNMKKTGTDATKNLNDATLKSNAGTSATESLGKNKL
KPSNKQLSPEHQAILSSRLESLESKIRLEQNTMDMTRLDAQKKQMTGDAIMKNSATAGNIAGASGRYAAT
LERSEQQISQASSRVASTASDEARESSRKSTSLIQELLKTMESINQSKASALAAIAGNIRA
>gnl|CDD|185272 PRK15374, PRK15374, type III secretion system needle tip complex protein SipB
MVNDASSISRSGYTQNPRLAEAAFEGVRKNTDFLKAADKAFKDVVATKAGDLKAGTKSGESAINTVGLKP
PTDAAREKLSSEGQLTLLLGKLMTLLGDVSLSQLESRLAVWQAMIESQKEMGIQVSKEFQTALGEAQEAT
DLYEASIKKTDTAKSVYDAAEKKLTQAQNKLQSLDPADPGYAQAEAAVEQAGKEATEAKEALDKATDATV
KAGTDAKAKAEKADNILTKFQGTANAASQNQVSQGEQDNLSNVARLTMLMAMFIEIVGKNTEESLQNDLA
LFNALQEGRQAEMEKKSAEFQEETRKAEETNRIMGCIGKVLGALLTIVSVVAAVFTGGASLALAAVGLAV
MVADEIVKAATGVSFIQQALNPIMEHVLKPLMELIGKAITKALEGLGVDKKTAEMAGSIVGAIVAAIAMV
AVIVVVAVVGKGAAAKLGNALSKMMGETIKKLVPNVLKQLAQNGSKLFTQGMQRITSGLGNVGSKMGLQT
NALSKELVGNTLNKVALGMEVTNTAAQSAGGVAEGVFIKNASEALADFTLARFAMDQIQQWLKQSVEIFG
ENQKVTAELQKAMSSAVQQNADASRFILRQSRA
>gnl|CDD|185273 PRK15375, PRK15375, type III secretion system effector GTPase-activating protein SptP
LNNLTLSSFSKVGVSNDARLYIAKENTDKAYVAPEKFSSKVLTWLGKMPLFKNTEVVQKHTENIRVQDQK
ILQTFLQALTEKYGETAVNDALLMSRINMNKPLTQRLAVQITECVKAADEGFINLIKSKDNVGVRNAALV
IKGGDTKVAEKNNDVGAESKQPLLDIALKGLKRTLPQLEQMDGNSLRENFQEMASGNGPLRSLMTNLQNL
NKIPEAKQLNDYVTTLTNIQVGVARFSQWGTCGGEVERWVDKASTHELTQAVKKIHVIAKELKNVTAELE
KIEAGAPMPQTMSGPTLGLARFAVSSIPINQQTQVKLSDGMPVPVNTLTFDGKPVALAGSYPKNTPDALE
AHMKMLLEKECSCLVVLTSEDQMQAKQLPPYFRGSYTFGEVHTNSQKVSSASQGEAIDQYNMQLSCGEKR
YTIPVLHVKNWPDHQPLPSTDQLEYLADRVKNSNQNGAPGRSSSDKHLPMIHCLGGVGRTGTMAAALVLK
DNPHSNLEQVRADFRNSRNNRMLEDASQFVQLKAMQAQLLMTTAS
>gnl|CDD|185274 PRK15376, PRK15376, type III secretion system effector SipA
MQTEIKTQATNLAANLSAVRESATETLSGEIKGPQLEDFPALIKQASLDALFKCGKDAEALKEVFTNSNN
VAGKKAIMEFAGLFRSALNATSDSPEAKTLLMKVGAEYTAQIIKDGLKEKSAFGPWLPETKKAEAKLENL
EKQLLDIIKNNTGGELSKLSTNFVMQEVMPYIASCIEHNFGCTLDPLTRSNLTGLVDKAAAKAVEALDMC
HQKLTQEQGTSVGREARHLEMQTLIPLLLRNVFAQIPADKLPDPKIPEPAAGPVPDGGKKAEPTGININI
NIDSSNHSVDNSKHINNSRSHVDNSQRHIDNSNHDNSRKTIDNSRTFIDNSQRHGESHHSTNSSNVSHSH
SRVDSTTHQTETAHSASTGAIDHGIAGKIDVTAHATAEAVTNASSESKDGKVVTSEKGTTGETTSFDEVD
GVTSKSIIGKPVQATVHGVDDNKQQSQTAEIVNVKPLASQLAGVENVKTDTLQSDTTVITGNKAGTTDND
NSQTDKTGPFSGLKFKQNSFLSTVPSVTNMHSMHFDARETFLGVIRKALEPDTSTPFPVRRAFDGLRAEI
LPNDTIKSAALKAQCSDIDKHPELKAKMETLKEVITHHPQKEKLAEIALQFAREAGLTRLKGETDYVLSN
VLDGLIGDGSWRAGPAYESYLNKPGVDRVITTVDGLHMQR
>gnl|CDD|185275 PRK15377, PRK15377, type III secretion system effector HECT-type E3 ubiquitin transferase
MKISSGAINFSTIPNQVKKLITSIREHTKNGLASKITSVKNTHGSLNEKIKTGKDSPIEFALPQKIKDFF
QPKDKNTLNKTLITVKNIKDTNNAGKKNISAEDVSKMNAAFMRKHIANQTCDYNYRITGAAPLPGGVSVS
ANNRPTVSEGRTPPVSPSLSLQATSSPSSPADWAKKLTDARLRQEAGEELTYADRDFSNADFRNINFSKI
NPSGFMLRDGDIIKGFNFSNSKFTYSDISHLHFDECRFTYSTLSDVVCSNTKFSNSDMNEASLKYSITTQ
QQPSFIETTLKNTIIIHKANLSGVILNEPDNSSPPSVSLGGNFIRLGDIWLQMPLLWTENAIDGFLNHEH
NNGKSILMTINTLPDKYNQEKVRAMEELVKSIRLGRLTEAAIRPVESSLVSVLAHPPYTQSALIQEWLEP
VQERFFAHQCQTYNDVPLPAPDTYYQQRSLPVLLDSFDRNSAAMTTHSGLFNQVILHCMTGVDCTDGMRQ
KAAALYEQYLAHPAVSPHIHNGLFGNYDGSPDWTTRAADNFLLLSSQDSDTAMMLSTDTLLTMLNPTPDT
AWDNFYLLRAGENVSTAQISPVELFRHDFPVFLAAFNQQASQRRFGELIDIILSTEEHGELNQQFIAATN
QKHSTVKLIDDASVSRLATIFNPLLPEGKLSPAHYQHILSAYHLTDATPQKQAETLFCLSTAFARYSSSA
IFGTEHDSPPALRGYAEALMQKAWELSPAIFPSSEQFTDWSDRFHGLHGAFTCTSVVADSMQRHARKYFP
SVLSSILPLAWA
>gnl|CDD|237953 PRK15378, PRK15378, type III secretion system effector inositol phosphate phosphatase
MQIQSLYHSASFKTQEAFKSLQKTLYNGMQILSGQGKAPAKAPDARPEIIVLRNKGATWGNYLQHQKTSN
HSLHNLYNLQRDLLTVAATALKLAGKQDPVLKAMANQMELAKVKADRPATKQEEAAAKALKKNLIELIAA
RTQQQLGLPAKEAHRFAALAFSDAQVKQLNNQPWQTIKNTLSHNGHHYTNTQLPAAEMKIGAKDIFPKAY
EGKGVCSWDTRNIHHANNLWMSTVSVHEDGKDKTLFCGIRHGVLSPYHEKNPLLRAVGAENKAKEVLTAA
LFSKPELLNQALEGEAVSLKLVSVSLLTASNIFGKEGTMLEDQMRAWQSLTQPGKMIHLKIRNKDGDLQT
VKVKLDVAAFNFGVNELALKLGFGLKNSDKYNAEALHQLLGNDLRPEARPGGWVGEWLAQYPDNYEVVNT
LARQIKDIWKNNQHHKDGGEPYKLAQRLAMLAYEIDAVPAWNCKSGKDRTGMMDSEIKREIISLHQTGML
SAPGSLPSSGEQKIFQKILLNSGNLEIQKINTGGAGNKVMKNLSLEVLNLSYQKRIGDENIWQSVKGISS
LITS
>gnl|CDD|185277 PRK15379, PRK15379, type III secretion system effector SopD
MPVTLSFGNHQNYTLNESRLAHLLSADKEKAIHMGGWDKVQDHFRAEKKDHALEVLHSIIHGQGRGEPGE
MEVNVEDINKIYAFKRLQHLACPAHQDLFTIKMDASQTQFLLMVGDTVISQSNIKDILNISDDAVIESMS
REERQLFLQICEVIGAKMTWHPELLQESISTLRKEVTGNAQIKAAVYEMMRPAEAPDHPLVEWQDSLTED
EKSMLACINAGNFEPTTQFCKIGYQEVQGEVAFSMMHPCISYLLHTYSPFAEFKPTNSGFLKKLNQDYND
YHAKKMFIDVILEKLYLTHERSLHIGKDGCSRNILLT
>gnl|CDD|185278 PRK15380, PRK15380, type III secretion system effector SopD2
MPVTLSFGNRHNYEINHSRLARLMSPDKEEALYMGVWDRFKDCFRTHKKQEVLEVLYTLIHGCERENQAE
LNVDITGMEKIHAFTQLKQYANPSQQDRFVMRFDMNQTQVLFEIDGKVIDKCNLHRLLNVSENCIFKVME
EDEEELFFKICIKYGEKIARYPELLEGFANKLKDAVNEDDDIKDEVYKLMRSGEDRKMECVEWNGTLTEE
EKNKLRCLQMGSFNITTQFFKIGYWELEGEVLFDMVHPTLSYLLQAYKPSLSSDLIEANTMLFSDVLNKD
YDDYQNNKREIDAILRRIYRSHNNTLFISEKSSCRNMLI
>gnl|CDD|185279 PRK15381, PRK15381, type III secretion system effector
MPLSVGQGYFTSSISSEKFNAIKESARLPELSLWEKIKAYFFTTHHAEALECIFNLYHHQELNLTPVQVR
GAYIKLRALASQGCKEQFIIESQEHADKLIIKDDNGENILSIEVECHPEAFGLAKEINKSHPKPKNISLG
DITRLVFFGDSLSDSLGRMFEKTHHILPSYGQYFGGRFTNGFTWTEFLSSPHFLGKEMLNFAEGGSTSAS
YSCFNCIGDFVSNTDRQVASYTPSHQDLAIFLLGANDYMTLHKDNVIMVVEQQIDDIEKIISGGVNNVLV
MGIPDLSLTPYGKHSDEKRKLKDESIAHNALLKTNVEELKEKYPQHKICYYETADAFKVIMEAASNIGYD
TENPYTHHGYVHVPGAKDPQLDICPQYVFNDLVHPTQEVHHCFAIMLESFIAHHYSTE
>gnl|CDD|185280 PRK15382, PRK15382, NleB family type III secretion system effector arginine glycosyltransferase
MLNVLQTSFRGSTALSQSSPLQTVSFAGKEYELEPIDEKTPILFQWFEARPERYKKGEVPILNTKEHPYL
SNIINAAKIENERIIGVLVDGDFTYEQKKEFLSLENEFQNIKIIYREDVDFSMYDKKLSDIYLENIHEQE
SYPASERDNYLLGLLREELKNIPEGKDSLIESYAEKREHTWFDFFRNLALLKAGELFTETGKTGCHNISP
CEGCIYLDADMIITDKLGVLYAPDGIAVHVDCNDDSKSLENGAIVVNRSNHPALLAGLDIMKSKVDAHPY
YDGLGKGIKRHFNYSSLHNYNHFCDFIEFKHENIIPNTSMYTCSSW
>gnl|CDD|185281 PRK15383, PRK15383, type III secretion system effector arginine glycosyltransferase
MFSRIRGLISCQSNTQTIAPTLSPPSSGHVSFAGIDYPLLPLDHHTPLVFQWFERNPDRFGQNEIPIINT
QKNPYLNNIINAAIIEKERIIGIFVDGDFSKGQRKALGKLEQNYRNIKVIYNSDLNYSMYDKKLTTIYLE
NITKLEAQSASERDEVLLNGVKKSLEDVLKNNPEETLISSHNKDKGHLWFDFYRNLFLLKGSDAFLEAGK
HGCHHLQPGGGCIYLDADMLLTDKLGTLYLPDGIAIHVSRKDNHVSLENGIIAVNRSEHPALIKGLEIMH
SKPYGDPYNDWLSKGLRHYFDGSHIQDYDAFCDFIEFKHENIIMNTSSLTASSWR
>gnl|CDD|185282 PRK15384, PRK15384, type III secretion system effector arginine glycosyltransferase SseK1
MIPPLNRYVPALSKNELVKTVTNRDIQFTSFNGKDYPLCFLDEKTPLLFQWFERNPARFGKNDIPIINTE
KNPYLNNIIKAATIEKERLIGIFVDGDFFPGQKDAFSKLEYDYENIKVIYRNDIDFSMYDKKLSEIYMEN
ISKQESMPEEKRDYHLLQLLKKELSDIQEGNDSLIKSYLLDKGHGWFDFYRNMAMLKAGQLFLEADKVGC
YDLSTNSGCIYLDADMIITEKLGGIYIPDGIAVHVERIDGRASMENGIIAVDRNNHPALLAGLEIMHTKF
DADPYSDGVCNGIRKHFNYSLNEDYNSFCDFIEFKHDNIIMNTSQFTQSSWARHVQ
>gnl|CDD|185283 PRK15385, PRK15385, MgtC family protein
MFPYILNLLAAMLLGALIGAERQWRQRMAGLRTNALVATGAAVFILSSMTTSPDSPGRIAAQIVSGIGFL
GAGVIMREGMNVRGLNTAATLWCSAGIGVLCGLGQFKNALAATIIILCANILLREAAQRINQLPVSAEGE
KRYILKVTCNKEDESAVRQWLLNIVKEAAICLQGLGSVPAQEQGYKEIRAELVGHADYRKTRELIISRIG
DNDNITAIHWSIDSQ
>gnl|CDD|237954 PRK15386, PRK15386, type III secretion effector GogB
VEIEFLSTENEKNKEAMLSTSQLEPDGTFCSNSTETSAEIRSEITPQIEEARASGRLYIKDCDIESLPVL
PNELTEITIENCNNLTTLPGSIPEGLEKLTVCHCPEISGLPESVRSLEIKGSATDSIKNVPNGLTSLSIN
SYNPENQARIDNLISPSLKTLSLTGCSNIILPEKLPESLQSITLHIEQKTTWNISFEGFPDGLDIDLQNS
VLLSPDVFKDKNITFQGNALDVALHFRLGDIVYGLSSPREKVVNSIKLVNDFSKKDIIIQNTLTDAVWDH
RNRRKYKQDALIKEALNDHDRGIKFKQFLKNHNKYNITMADYSVYNNEECWAKTSKAGLEFQTLERNETV
IFCIDNLVNSIKLIANKKPGYGQSITASELRWIYRNKDNPQVKKNVKFYLEGKEISAEEVFSLPGWKDYF
PKRSGN
>gnl|CDD|185285 PRK15387, PRK15387, type III secretion system effector E3 ubiquitin transferase SspH2
MPFHIGSGCLPATISNRRIYRIAWSDTPPEMSSWEKMKEFFCSTHQTEALECIWTICHPPAGTTREDVIN
RFELLRTLAYAGWEESIHSGQHGENYFCILDEDSQEILSVTLDDAGNYTVNCQGYSETHRLTLDTAQGEE
GTGHAEGASGTFRTSFLPATTAPQTPAEYDAVWSAWRRAAPAEESRGRAAVVQKMRACLNNGNAVLNVGE
SGLTTLPDCLPAHITTLVIPDNNLTSLPALPPELRTLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPAL
PSGLCKLWIFGNQLTSLPVLPPGLQELSVSDNQLASLPALPSELCKLWAYNNQLTSLPTLPSGLQELSVS
DNQLASLPTLPSELYKLWAYNNRLTSLPALPSGLKELIVSGNRLTSLPVLPSELKELMVSGNRLTSLPML
PSGLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNPLSERTLQALREITSAPGYSGPIIRFDMAGASAPR
ETRALHLAAADWLVPAREGEPAPADRWHMFGQEDNADAFSLFLDRLSETENFIKDAGFKAQISSWLAQLA
EDEALRANTFAMATEATSSCEDRVTFFLHQMKNVQLVHNAEKGQYDNDLAALVATGREMFRLGKLEQIAR
EKVRTLALVDEIEVWLAYQNKLKKSLGLTSVTSEMRFFDVSGVTVTDLQDAELQVKAAEKSEFREWILQW
GPLHRVLERKAPERVNALREKQISDYEETYRMLSDTELRPSGLVGNTDAERTIGARAMESAKKTFLDGLR
PLVEEMLGSYLNVQWRRN
>gnl|CDD|185286 PRK15388, PRK15388, superoxide dismutase [Cu-Zn]
MKYTILSLVAGALISCSAMAENTLTVKMNDALSSGTGENIGEITVSETPYGLLFTPHLNGLTPGIHGFHV
HTNPSCMPGMKDGKEVPALMAGGHLDPEKTGKHLGPYNDKGHLGDLPGLVVNADGTATYPLLAPRLKSLS
ELKGHSLMIHKGGDNYSDKPAPLGGGGARFACGVIEK
>gnl|CDD|237955 PRK15389, PRK15389, fumarate hydratase; Provisional
SMPPFKYQDLFPLGKDDTEYRLLTSDGVSVAEFEGREILKVEPEALTLLAEEAFHDISHLLRPAHLQQLA
KILDDPEASDNDKFVALDLLKNANIAAGGVLPMCQDTGTAIIMGKKGQRVWTGGDDEEALSRGVYDTYTE
LNLRYSQNAPLDMYEEKNTGTNLPAQIDIYATEGDEYKFLFMAKGGGSANKTFLYQETKALLNPDRLLAF
LVEKMRTLGTAACPPYHLAIVIGGTSAEANLKTVKLASAKYLDALPTEGNEHGHAFRDLELEQEVLKLTQ
KLGIGAQFGGKYFCHDVRVIRLPRHGASCPVGIGVSCSADRNIKAKITRDGIFLEQLETNPARYLPEVLR
EKLEGEVVKIDLNRPMAEILAELSKYPVKTRLSLTGTIIVARDIAHAKLKERLDAGEGLPQYLKDHPVYY
AGPAKTPEGYASGSFGPTTAGRMDSYVDLFQAAGGSMVMLAKGNRSQQVTDACKKHGGFYLGSIGGPAAR
LAQDCIKKVEVLEYPELGMEAVWKIEVEDFPAFILVDDKGNDFFKE
>gnl|CDD|185288 PRK15390, PRK15390, fumarate hydratase FumA; Provisional
MSNKPFHYQAPFPLKKDDTEYYLLTSEHVSVSEFEGQEILKVAPEALTLLARQAFHDASFMLRPAHQQQV
ADILRDPEASENDKYVALQFLRNSDIAAKGVLPTCQDTGTAIIVGKKGQRVWTGGGDEAALARGVYNTYI
EDNLRYSQNAPLDMYKEVNTGTNLPAQIDLYAVDGDEYKFLCIAKGGGSANKTYLYQETKALLTPGKLKN
YLVEKMRTLGTAACPPYHIAFVIGGTSAETNLKTVKLASAKYYDELPTEGNEHGQAFRDVELEKELLIEA
QNLGLGAQFGGKYFAHDIRVIRLPRHGASCPVGMGVSCSADRNIKAKINRQGIWIEKLEHNPGKYIPEEL
RKAGEGEAVRVDLNRPMKEILAQLSQYPVSTRLSLNGTIIVGRDIAHAKLKERMDNGEGLPQYIKDHPIY
YAGPAKTPEGYASGSLGPTTAGRMDSYVDQLQAQGGSMIMLAKGNRSQQVTDACKKHGGFYLGSIGGPAA
VLAQGSIKSLECVEYPELGMEAIWKIEVEDFPAFILVDDKGNDFFQQIQLTQCTRCVK
>gnl|CDD|185289 PRK15391, PRK15391, class I fumarate hydratase
MSNKPFIYQAPFPMGKDNTEYYLLTSDYVSVADFDGETILKVEPEALTLLAQQAFHDASFMLRPAHQKQV
AAILHDPEASENDKYVALQFLRNSEIAAKGVLPTCQDTGTAIIVGKKGQRVWTGGGDEEALSKGVYNTYI
EDNLRYSQNAALDMYKEVNTGTNLPAQIDLYAVDGDEYKFLCVAKGGGSANKTYLYQETKALLTPGKLKN
FLVEKMRTLGTAACPPYHIAFVIGGTSAETNLKTVKLASAHYYDELPTEGNEHGQAFRDVQLEQELLEEA
QKLGLGAQFGGKYFAHDIRVIRLPRHGASCPVGMGVSCSADRNIKAKINREGIWIEKLEHNPGQYIPQEL
RQAGEGEAVKVDLNRPMKEILAQLSQYPVSTRLSLTGTIIVGRDIAHAKLKELIDAGKELPQYIKDHPIY
YAGPAKTPAGYPSGSLGPTTAGRMDSYVDLLQSHGGSMIMLAKGNRSQQVTDACHKHGGFYLGSIGGPAA
VLAQQSIKHLECVAYPELGMEAIWKIEVEDFPAFILVDDKGNDFFQQIVNKQCANCTK
>gnl|CDD|185290 PRK15392, PRK15392, class I fumarate hydratase
MSKPFIWQEPFLQNKDGTEYTLISDQHITVTELDGEEVIKIAPEALTLLARQAFYEASFFLRSAHLQQVA
SILNDPQASSNDKYVALQLLRNAEVSAKGVLPNCQDTGTATIVASKGQQIWTGGNDAEALSKGIYSTFQE
NNLRFSQNAPLDMYTEVNTQTNLPAQIDISAVAGDEYHFLCVNKGGGSANKAALYQETKSLLQPEKLTAF
LIEKMKSLGTAACPPYHIAFVVGGLSADQTLKVAKLASTKYYDNLPTSGNEQGQAFRDIELEKVLLEASQ
QFGIGAQFGGKYFAHDIRVIRLPRHGGSCPIAMALSCSADRNIKAKINKHGIWLEKLEHNPGQYIPASLR
EENHAQHVQLDLNRPLRDVMQDLARLPVGTRVSLSGPIVVARDIAHAKIKARLDSGEPMPEYLKHHIVYY
AGPAKTPENMACGSLGPTTGGRMDGYVDTFQAAGGSLVMLSKGNRSQQVTDACHKHGGFNLGSIGGAAAL
LAQEYVKSLRCLEYPELGMEAVWMMEVENLPAFILVDDKGNNFFSQFEQQHRCASCPAGH
>gnl|CDD|185291 PRK15393, PRK15393, NUDIX hydrolase YfcD; Provisional
VEQRRLASTEWVDIVNENNEVIAQASREQMRAQCLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDAT
AGGVVQAGEQLLESARREAEEELGIAGVPFAEHGQFYFEDENCRVWGALFSCVSHGPFALQEEEVSEVCW
MTPEEITARCDEFTPDSLKALALWLTRNAKNEAVETETAE
>gnl|CDD|185292 PRK15394, PRK15394, 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD; Provisional
MTKVGLRIDVDTFRGTREGVPRLLEILSKHGIQASFFFSVGPDNMGRHLWRLLKPRFLWKMLRSNAASLY
GWDILLAGTAWPGKEIGKALADIIREAAKAHEVGLHAWDHHAWQAWSGVWSRQQLIEQIARGVDALEEII
GQPVTCSAAAGWRADQRVVEAKEAFGFRYNSDCRGTHPFRPLLPDGSLGTVQIPVTLPTWDEVIGRDVKA
EDFNDFILDRILRDKGTPVYTIHAEVEGIAYAHNFEDLLKRAAQEGITFCPLSELLPDDLETLPLGKVVR
GNIPGREGWLGCQQIA
>gnl|CDD|185293 PRK15395, PRK15395, galactose/glucose ABC transporter substrate-binding protein MglB
NKKVLTLSALMASMLFGAAAAAADTRIGVTIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQ
NDQIDVLLAKGVKALAINLVDPAAAPTVIEKARGQDVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGII
QGDLIAKHWKANPAWDLNKDGKIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQA
KDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTVLNDA
NNQAKATFDLAKNLADGKGAAEGTNWKIENKVVRVPYVGVDKDNLAEFTK
>gnl|CDD|185294 PRK15396, PRK15396, major outer membrane lipoprotein
MNRTKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLD
NQATKYRK
>gnl|CDD|185295 PRK15397, PRK15397, nicotinamide riboside transporter PnuC; Provisional
MDFFSTNNILVHIPLGAGGYDLSWIEAVGTIAGLLCIWLASLEKIINYLFGLINVTLFAIIFFQIQLYAS
LLLQLFFFAANIYGWYAWSRQTSQNEAELKIRWLPLPKALAWLAVCVVAIGLMTVFIDPVFAFLTRVAVM
IMQALGLQVAMPELQPDAFPFWDSCMMVLSIVAMILMTRKYVENWLLWVIINVISVVIFALQGVYAMSLE
YIILTFIALNGSRLWIKSARENGSRALSH
>gnl|CDD|237956 PRK15398, PRK15398, aldehyde dehydrogenase
MNQQDIEQVVKAVLAEMLSSQTVSPPAAVGEMGVFASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREA
LLPHAEELAELAVEETGMGRVEDKIAKNVAAAEKTPGVEDLTTEALTGDNGLTLIEYAPFGVIGAVTPST
NPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAAGGPENLVVTVAEPTIETAQRLMKH
PGIALLVVTGGPAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIV
VDSVADELMRLMEKNGAVLLTAEQAEKLQKVVLKNGGTVNKKWVGKDAAKILEAAGINVPKDTRLLIVET
DANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNRHTAIMHSRNVDNLNKMARAIQTSIFVKNGPS
YAGLGLGGEGFTTFTIATPTGEGVTSARTFTRRRRCVLVDGFRIR
>gnl|CDD|185297 PRK15399, PRK15399, lysine decarboxylase
MNIIAIMGPHGVFYKDEPIKELESALQAQGFQTIWPQNSVDLLKFIEHNPRICGVIFDWDEYSLDLCSDI
NQLNEYLPLYAFINTHSTMDVSVQDMRMALWFFEYALGAAEDIAIRIRQYTNEYLDNITPPFTKALFTYV
KEGKYTFCTPGHMGGTAYQKSPVGCLFYDFFGGNTLKADVSISVTELGSLLDHTGPHLEAEEYIARTFGA
EQSYIVTNGTSTSNKIVGMYAAPAGSTLLIDRNCHKSLAHLLMMSDVVPIWLKPTRNALGILGGIPRREF
TRDSIEEKVAATTQAQWPVHAVITNSTYDGLLYNTDWIKQTLDVPSIHFDSAWVPYTHFHPIYQGKSGMS
GERVPGKVIFETQSTHKMLAAFSQASLIHIKGEYDEETFNEAFMMHTSTSPSYPIVASVETAAAMLRGNP
GKRLINRSVERALHFRKEVQRLREESDGWFFDIWQPENVDEAECWPVAPGEQWHGFKDADADHMFLDPVK
VTILTPGMDEQGNMSEEGIPAALVAKFLDERGIVVEKTGPYNLLFLFSIGIDKTKAMGLLRGLTEFKRAY
DLNLRVKNMLPDLYAEDPDFYRNMRIQDLAQGIHKLIRKHDLPGLMLRAFDVLPEMIMTPHQAWQRQIKG
EVETVALEQLVGRVSANMILPYPPGVPLLMPGEMITEESRAVLDFLLMLCSIGQHYPGFETDIHGAKRDE
DGVYRVRVLKMAG
>gnl|CDD|185298 PRK15400, PRK15400, lysine decarboxylase
MNVIAILNHMGVYFKEEPIRELHRALERLNFQIVYPNDRDDLLKLIENNARLCGVIFDWDKYNLELCEEI
SKMNENLPLYAFANTYSTLDVSLNDLRLQVSFFEYALGAADDIANKIKQTTDEYIDTILPPLTKALFKYV
REGKYTFCTPGHMGGTAFQKSPVGSLFYDFFGPNTMKSDISISVSELGSLLDHSGPHKEAEEYIARVFNA
DRSYMVTNGTSTANKIVGMYSAPAGSTVLIDRNCHKSLTHLMMMSDVTPIYFRPTRNAYGILGGIPQSEF
QHATIAKRVKETPNATWPVHAVITNSTYDGLLYNTDFIKKTLDVKSIHFDSAWVPYTNFSPIYEGKCGMS
GGRVEGKVIYETQSTHKLLAAFSQASMIHVKGDVNEETFNEAYMMHTTTSPHYGIVASTETAAAMMKGNA
GKRLINGSIERAIKFRKEIKRLRTESDGWFFDVWQPDHIDTTECWPLRSDSTWHGFKNIDNEHMYLDPIK
VTLLTPGMKKDGTMSDFGIPASIVAKYLDEHGIVVEKTGPYNLLFLFSIGIDKTKALSLLRALTDFKRAF
DLNLRVKNMLPSLYREDPEFYENMRIQELAQNIHKLIVHHNLPDLMYRAFEVLPTMVMTPYAAFQKELHG
MTEEVYLDEMVGRVNANMILPYPPGVPLVMPGEMITEESRPVLEFLQMLCEIGAHYPGFETDIHGAYRQA
DGRYTVKVLKEESK
>gnl|CDD|237957 PRK15401, PRK15401, DNA oxidative demethylase AlkB
MMLDLFADAEPWQEPLAPGAVLLRGFALAAAEALLAAIEAVAAQAPFRHMVTPGGYTMSVAMTNCGALGW
VTDRRGYRYSPIDPLTGKPWPAMPASFLALAQRAAAAAGFPGFQPDACLINRYAPGAKLSLHQDKDERDF
RAPIVSVSLGLPAVFQFGGLKRSDPLQRILLEHGDVVVWGGPSRLRYHGILPLKAGEHPLTGECRINLTF
RKA
>gnl|CDD|185300 PRK15402, PRK15402, MdfA family multidrug efflux MFS transporter
LSPLARLGRQALLFPLCLVLFEFATYIANDMIQPGMLAVVEDFNAGAEWVPTSMTAYLAGGMFLQWLLGP
LSDRIGRRPVMLAGVAFFILTCLAILLAQSIEQFTLLRFLQGIGLCFIGAVGYAAIQESFEEADAIKITA
LMANVALLAPLLGPLVGAALIHVLPWRGMFVLFAALAALSFFGLWRAMPETAGRVGEKLSLKELGRDYKL
VLKNRRFVAGALALGLVSLPLLAWIALSPVILISGEQLSSYEYGLLQVPVFGALIAGNLTLARLTSRRPL
RSLIRMGLWPMVAGLLLAALATVISSHAYLWLTAGLSLYAFGIGLANAGLYRLTLFSSDVSKGTVSAAMG
MLSMLIFTVGIELSKHAYLGGGNGLFNLFNLANGLLWLLLVRIFLKDKPMGNAHEG
>gnl|CDD|237958 PRK15403, PRK15403, multidrug efflux MFS transporter MdtM
MQRMPRFFARHAATLFFPMALILYDFAAYLTTDLIQPGIINVVRDFNADVSLAPASVSLYLAGGMALQWL
LGPLSDRIGRRPVLITGALIFTLACAATLFTTSMTQFLIARFIQGTSICFIATVGYVTVQEAFGQTKGIK
LMAIITSIVLVAPIIGPLSGAALMHFVHWKVLFAIIAVMGLIAFVGLLLAMPETVKRGAVPFSAKSVLRD
FRNVFRNRLFLTGAATLSLSYIPMMSWVAVSPVILIDAGGMTTSQFAWTQVPVFGAVIVANAIVARFVKD
PTEPRFIWRAVPIQLVGLALLIVGNLLWPHVWLWSVLGTSLYAFGIGLIFPTLFRFTLFSNNLPKGTVSA
SLNMVILMVMAVSVEIGRWLWFNGGRLPFHLLAVVAGVIVVFTLAGLLNRVRQHQAAELAEEQ
>gnl|CDD|237959 PRK15404, PRK15404, high-affinity branched-chain amino acid ABC transporter substrate-binding protein
MKSKGKTLLAGCIALALSHAALADDIKIAIVGPMSGPVAQYGDMEFTGARQAIEDINAKGGIKGDKLEGV
EYDDACDPKQAVAVANKVVNDGIKYVIGHLCSSSTQPASDIYEDEGILMITPAATAPELTARGYQLIFRT
IGLDSDQGPTAAKYILEKVKPKRIAVLHDKQQYGEGLARSVKDGLKKAGANVVFFEGITAGDKDFSALIA
KLKKENVDFVYYGGYHPEMGQILRQAREAGLKTQFMGPEGVGNKSLSNIAGPASEGMLVTLPKRYDQDPA
NKAIVDAFKAKKQDPSGPFVWTTYAAVQSLAAGINRAGSDDPAKVAKYLKANTFDTVIGPLSWDEKGDLK
GFEFGVFEWHADGTKTAAK
>gnl|CDD|185303 PRK15405, PRK15405, ethanolamine utilization microcompartment protein EutL
MALDLIRPSVLAMRVIANVNAGLARELKLPPHIRSLGLITADSDDVTYTALDEATKQAMVEVVYARSFYA
GAAHASTPLAGEVIGILAGPNPAEVRAGLDAMVAFIENGAAFQSANDDDSTAFFAHVVSRTGSYLSKTAG
IAEGEPLAYLIAPPLEAMYGIDAALKAADVQLVTFVGPPSETNFGGALLTGSQSACKAACNAFTDAVLEV
ARNPIQY
>gnl|CDD|185304 PRK15406, PRK15406, oligopeptide ABC transporter permease OppC; Provisional
MMLSKKNSEALENFSEKLEVEGRSLWQDARRRFMHNRAAVASLIVLVLIALFVILAPMLSQFAYDDTDWG
MMSSAPDMESGHYFGTDSSGRDLLVRVAIGGRISLMVGVAAALVAVVVGTLYGSLSGYLGGKVDSVMMRL
LEILNSFPFMFFVILLVTFFGQNILLIFVAIGMVSWLDMARIVRGQTLSLKRKEFIEAAQVGGVSTRGIV
LRHIVPNVLGVVVVYASLLVPSMILFESFLSFLGLGTQEPLSSWGALLSDGANSMEVSPWLLLFPAGFLV
VTLFCFNFIGDGLRDALDPKDR
>gnl|CDD|237960 PRK15407, PRK15407, lipopolysaccharide biosynthesis protein RfbH; Provisional
DMTEEELRQQILELVREYAELAHAPKPFVPGKSPIPPSGKVIDAKELQNLVDASLDFWLTTGRFNDAFEK
KLAEFLGVRYALLVNSGSSANLLAFSALTSPKLGDRALKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDV
ELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFG
DIATLSFYPAHHITMGEGGAVFTNDPLLKKIIESFRDWGRDCWCAPGCDNTCGKRFGWQLGELPFGYDHK
YTYSHLGYNLKITDMQAAIGLAQLEKLPGFIEARKANFAYLKEGLASLEDFLILPEATPNSDPSWFGFPI
TVKEDAGFTRVELVKYLEENKIGTRLLFAGNLTRQPYFKGVKYRVVGELTNTDRIMNDTFWIGVYPGLTE
EMLDYVIEKIEEFFGLNF
>gnl|CDD|237961 PRK15408, PRK15408, autoinducer 2 ABC transporter substrate-binding protein LsrB
RKKKIALVSALGIALISMTVQAAERIAFIPKLVGVGFFTSGGNGAKEAGKELGVDVTYDGPTEPSVSGQV
QLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGTPEQLGSMLVEMA
AKQVGKDKAKVAFFYSSPTVTDQNQWVKEAKAKIAKEHPGWEIVTTQFGYNDATKSLQTAEGILKAYPDL
DAIIAPDANALPAAAQAAENLKRDKVAIVGFSTPNVMRPYVKRGTVKEFGLWDVVQQGKISVYVANELLK
KGKLNVGDSLDVPGIGKVEVSPNSVQGYDYEAKGNGIVLLPERVVFTKENIDKYDF
>gnl|CDD|185307 PRK15409, PRK15409, glyoxylate/hydroxypyruvate reductase GhrB
MKPSVILYKALPDDLLQRLEEHFTVTQVANLSPETVEQHAAAFAEAEGLLGSGEKVDAALLEKMPKLRAA
STISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVEVAERVKAGEWTASIGPDWFG
TDVHHKTLGIVGMGRIGMALAQRAHFGFNMPILYNARRHHKEAEERFNARYCDLDTLLQESDFVCIILPL
TDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQEPLSVDSPLLSLPNV
VAVPHIGSATHETRYNMAACAVDNLIDALQGKVEKNCVNPQVA
>gnl|CDD|185308 PRK15410, PRK15410, DgsA anti-repressor MtfA; Provisional
MIKWPWKAQEPAHQTALPWQEALSIPLLTPLTEQEQQKLVALAERFLQQKRLVPLQGLELDSLMSARIAL
LFCLPVLELGIEWLDGFHEVLIYPAPFVVDDEWEDDIGLVHNQRIVQSGQSWQQGPIVLNWLDIQDSFDA
SGFNLIIHEVAHKLDMRNGDRASGVPFIPLREVAGWEHDLHAAMNNIQEEIDLVGENAASIDAYAASDPA
ECFAVLSEYFFSAPELFAPRFPALYQRFCQFYRQDPLQRLHRWNDTDSFS
>gnl|CDD|185309 PRK15411, rcsA, transcriptional regulator RcsA
MSTIIMDLCSYTRLGLTGYLLSRGVKKREINDIETVDDLAIACDSLRPSVVFINEDCFIHDASNSQRIKQ
IINQHPNTLFIVFMAIANIHFDEYLLVRKNLLISSKSIKPESLDDLLGDILKKETTITSFLNLPTLSLSR
TESSMLRMWMAGQGTIQISDQMNIKAKTVSSHKGNIKRKIKTHNKQVIYHVVRLTDNVTNGIFVNMR
>gnl|CDD|185310 PRK15412, PRK15412, thiol:disulfide interchange protein DsbE; Provisional
MKRNVLLIPLIIFLAIAAALLWQLARNAEGDDPTNLESALIGKPVPKFRLESLENPGQFYQADVLTQGKP
VLLNVWATWCPTCRAEHQYLNQLSAQGIRVVGMNYKDDRQKAISWLKELGNPYALSLFDGDGMLGLDLGV
YGAPETFLIDGNGIIRYRHAGDLNPRVWESEIKPLWEKYSKEAAQ
>gnl|CDD|185311 PRK15413, PRK15413, glutathione ABC transporter substrate-binding protein GsiB; Provisional
MARAVHRSWLVALGIATALAASPAFAAKDVVVAVGSNFTTLDPYDANDTLSQAVAKSFYQGLFGLDKEMK
LKNVLAESYTVSDDGLTYTVKLREGVKFQDGTDFNAAAVKANLDRASNPDNHLKRYNLYKNIAKTEAVDP
TTVKITLKQPFSAFINILAHPATAMISPAALEKYGKEIGFHPVGTGPYELDTWNQTDFVKVKKFAGYWQP
GLPKLDSITWRPVADNNTRAAMLQTGEAQFAFPIPYEQAALLEKNKNLELVASPSIMQRYISMNVTQKPF
DNPKVREALNYAINRQALVKVAFAGYATPATGVVPPSIAYAQSYKPWPYDPAKARELLKEAGYPNGFSTT
LWSSHNHSTAQKVLQFTQQQLAQVGIKAQVTAMDAGQRAAEVEGKGQKESGVRMFYTGWSASTGEADWAL
SPLFASQNWPPTLFNTAFYSNKQVDDDLAQALKTNDPAEKTRLYKAAQDIIWKESPWIPLVVEKLVSAHS
KNLTGFWIMPDTGFSFEDADLK
>gnl|CDD|185312 PRK15414, PRK15414, phosphomannomutase
MKKLTCFKAYDIRGKLGEELNEDIAWRIGRAYGEFLKPKTIVLGGDVRLTSETLKLALAKGLQDAGVDVL
DIGMSGTEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPISGDTGLRDVQRLAEANDFPPVDE
TKRGRYQQINLRDAYVDHLFGYINVKNLTPLKLVINSGNGAAGPVVDAIEARFKALGAPVELIKVHNTPD
GNFPNGIPNPLLPECRDDTRNAVIKHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPG
AKIIHDPRLSWNTVDVVTAAGGTPVMSKTGHAFIKERMRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLL
VAELVCLKGKTLGELVRDRMAAFPASGEINSKLAQPVEAINRVEQHFSREALAVDRTDGISMTFADWRFN
LRSSNTEPVVRLNVESRGDVPLMEARTRTLLTLLNE
>gnl|CDD|185313 PRK15415, PRK15415, propanediol utilization microcompartment protein PduB
MSNELVEQIMAEVMKKVEAQAAPKNPQPIRETAMAEKSCGLTEFVGTAIGDTIGLVIANVDSALLEAMKL
EKKYRSIGILGARTGAGPQIMAADEAVKATNTEVVSIELPRDTKGGAGHGSLIIFGAEDVSDVRRAVEVA
LKELDRTFGDVYGNEAGHLELQYTARASYALEKAFGAPLGKAFGIIVGAPAGIGVVMADTALKSANVDVV
AYSSPAHGTSFSNEVILTISGDSGAVRQAVIAAREVGLTLLATLGSEPKSDTPPYI
>gnl|CDD|185314 PRK15416, PRK15416, lipopolysaccharide core heptose(II)-phosphate phosphatase; Provisional
MLAFCRSSSKSKKYFFILLGALAAIAGLTTQAAWSSNGLPRIDNKTLAELAKQHPVVVLFRHAERCDRSD
NQCLSDKTGITVKGTQDARELGKAFSADIPDYDLYSSNTVRTIQSATWFSAGKKLTVDKRLSDCGNGIYS
AIKDLQRKSPDKNIVIFTHNHCLTYIAKDKRGVKFKPDYLDALVMHVEKGKLYLDGEFVNH
>gnl|CDD|185315 PRK15417, PRK15417, integron integrase
MKTATAPLPPLRSVKVLDQLRERIRYLHYSLRTEQAYVHWVRAFIRFHGVRHPATLGSSEVEAFLSWLAN
ERKVSVSTHRQALAALLFFYGKVLCTDLPWLQEIGRPRPSRRLPVVLTPDEVVRILGFLEGEHRLFAQLL
YGTGMRISEGLQLRVKDLDFDHGTIIVREGKGSKDRALMLPESLAPSLREQLSRARAWWLKDQAEGRSGV
ALPDALERKYPRAGHSWPWFWVFAQHTHSTDPRSGVVRRHHMYDQTFQRAFKRAVEQAGITKPATPHTLR
HSFATALLRSGYDIRTVQDLLGHSDVSTTMIYTHVLKVGGAGVRSPLDALPPLTSER
>gnl|CDD|237962 PRK15418, PRK15418, transcriptional regulator LsrR; Provisional
TINDSLISEQGMCEEELVARIAWFYYHDGLTQSEIGERLGLTRLKVSRLLEKGRQSGIIRVQINSRFEGC
LELENALRQHFSLQHIRVLPALADADIGGRLGIGAAHMLMSLLQPQQLLAVGFGEATMNTLQHLSGFISS
QQIRLVTLSGGVGPYMTGIGQLDAACSVSIIPAPLRASSAEIARTLRNENSVRDVMLAAQAADVAIVGIG
AVNQKDDATILRSGYISQGEQLMIGRKGAVGDILGYFFDADGELVPDIKIHNELIGLPLSSLKTIPTVIG
VAGGEEKAEAIIAALKGGYINALVTDEKTARAILALLV
>gnl|CDD|185317 PRK15419, PRK15419, sodium/proline symporter PutP
MAISTPMLVTFCVYIFGMILIGFIAWRSTKNFDDYILGGRSLGPFVTALSAGASDMSGWLLMGLPGAVFL
SGISESWIAIGLTLGAWINWKLVAGRLRVHTEYNNNALTLPDYFTGRFEDKSRILRIISALVILLFFTIY
CASGIVAGARLFESTFGMSYETALWAGAAATILYTFIGGFLAVSWTDTVQASLMIFALILTPVIVIISVG
GFGDSLEVIKQKSIENVDMLKGLNFVAIISLMGWGLGYFGQPHILARFMAADSHHSIVHARRISMTWMIL
CLAGAVAVGFFGIAYFNEHPAVAGAVNQNAERVFIELAQILFNPWIAGILLSAILAAVMSTLSCQLLVCS
SAITEDLYKAFLRKHASQKELVWVGRVMVLVVALVAIALAANPENRVLGLVSYAWAGFGAAFGPVVLFSV
MWSRMTRNGALAGMIIGALTVIVWKQFGWLGLYEIIPGFIFGSIGIVVFSLLGKAPSAAMQKRFAEADAH
YHSAPPSRLQEE
>gnl|CDD|185318 PRK15420, fucU, L-fucose mutarotase; Provisional
MLKTISPLISPELLKVLAEMGHGDEIIFSDAHFPAHSMGPQVIRADGLLVSDLLQAIIPLFELDSYAPPL
VMMAAVEGDTLDPEVERRYRNALSLQAPCPDIIRINRFAFYERAQKAFAIVITGERAKYGNILLKKGVTP
>gnl|CDD|185319 PRK15421, PRK15421, HTH-type transcriptional regulator MetR
MIEVKHLKTLQALRNCGSLAAAAATLHQTQSALSHQFSDLEQRLGFRLFVRKSQPLRFTPQGEILLQLAN
QVLPQISQALQACNEPQQTRLRIAIECHSCIQWLTPALENFHKNWPQVEMDFKSGVTFDPQPALQQGELD
LVMTSDILPRSGLHYSPMFDYEVRLVLAPDHPLAAKTRITPEDLASETLLIYPVQRSRLDVWRHFLQPAG
VSPSLKSVDNTLLLIQMVAARMGIAALPHWVVESFERQGLVVTKTLGEGLWSRLYAAVRDGEQRQPVTEA
FIRSARNHACDHLPFVKSAERPTYDAPTVRPGSPARL
>gnl|CDD|185320 PRK15422, PRK15422, septal ring assembly protein ZapB; Provisional
MSLEVFEKLEAKVQQAIDTITLLQMEIEELKEKNNSLSQEVQNAQHQREELERENNHLKEQQNGWQERLQ
ALLGRMEEV
>gnl|CDD|185321 PRK15423, PRK15423, hypoxanthine phosphoribosyltransferase; Provisional
MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSY
GSGMSTTRDVKILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVP
VEFIGFSIPDEFVVGYGIDYAQRYRHLPYIGKVILLDE
>gnl|CDD|237963 PRK15424, PRK15424, propionate catabolism operon regulatory protein PrpR; Provisional
MRSMAHPPRDNDDKPVIWTVSVSRLFELFRDISLEFDHLANITPIQLGFEKAVTYIRKRLATERCDAIIA
AGSNGAYLKSRLSVPVILIKPSGFDVMQALARARKLTSSIGVVTYQETIPALVAFQKTFNLRIEQRSYVT
EEDARGQINELKANGIEAVVGAGLITDLAEEAGMTGIFIYSAATVRQAFEDALDMTRMTLRHNTHYATRN
ALRTRYVLGDLLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHREYFARHDARQGKKSHP
FVAVNCGAIAESLLEAELFGYEEGAFTGSRRGGRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKE
VTRVGGHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSL
AALSAPFSAALRQGLQQCETLLLHYDWPGNVRELRNLMERLALFLSVEPTPDLTPQFLQLLLPELARESA
KTPAPRLLAATLQQALERFNGDKTAAANYLGISRTTLWRRLKAEAKAQ
>gnl|CDD|185323 PRK15425, gapA, glyceraldehyde-3-phosphate dehydrogenase
MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGK
KIRVTAERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYA
GQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTG
AAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVV
STDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNKVLDLIAHISK
>gnl|CDD|237964 PRK15426, PRK15426, cellulose biosynthesis regulator YedQ
MPHETRLENQSWLKKLARRLGPGHVVNLCFIVVLLFSTLLTWREVVVLEDAYISSQRNHLENVANALDAQ
LQYNVDKLIFLRNGMREALVAPLDFPALDAAVTQFEQHRDEHVWQLELPRRRTLPVNGVSDAFVSGLTLL
SRDDEDLANELTAALELGYLLRLAHNSSSLVERAMYVSRAGFYVSTYPTLFPSDVPTRYYQYVTQPWFIG
QSQRRNPGRGVRWFTSQPDDASNTEPQVTASVPVDAGNYWYGVLAMDIPVRSLQQFLRNAIDKDLDGEYQ
LYDSHLRLLTSSAPGVRTGNIFDPRELALLARAMEHDTRGGIRMGSRYVSWERLDHFDGVLVRVHTLREG
VRGDFGSISIALTLLWALFTAMLLISWYVIRRMVSNMFVLQSSLQWQAWHDPLTRLYNRGALFEKARALA
KRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASL
AEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAEEDGDYDFEQLQSLADRRLYLAKQAGRNRVCA
SDNAHEREVK
>gnl|CDD|185326 PRK15428, PRK15428, putative propanediol utilization protein PduM; Provisional
MNGEMLQRIVEEVVARLQRRAQSTATLSVAQLRDADSPTLFCQHASLRILLVDLPLLRQLAEADTSDPAA
RKIHEALAWGVRVQLSLHRQLLPALPVKKLARLPLTFTDEQGQPVVLHAGSVLSYADVALLSRGILVLRR
KCIVTALAREAASARNIQLIKQE
>gnl|CDD|237965 PRK15429, PRK15429, formate hydrogenlyase transcriptional activator FlhA
TPMSDLGQQGLFDITRTLLQQPDLASLCEALSQLVKRSALADNAAIVLWQAQTQRASYYASREKGTPVKY
EDETVLAHGPVRRILSRPDTLHCSYEEFCETWPQLAAGGLYPKFGHYCLMPLAAEGHIFGGCEFIRYDDR
PWSEKEFNRLQTFTQIVSVVTEQIQSRVVNNVDYELLCRERDNFRILVAITNAVLSRLDMDELVSEVAKE
IHYYFDIDAISIVLRSHRKNKLNIYSTHYLDKQHPAHEQSEVDEAGTLTERVFKSKEMLLINLHERDDLA
PYERMLFDTWGNQIQTLCLLPLMSGDTMLGVLKLAQCEEKVFTTTNLKLLRQIAERVAIAVDNALAYQEI
HRLKERLVDENLALTEQLNNVDSEFGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIH
NLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKL
LRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRSDLYYRLNVFPIHLPPLRERPEDIPLLV
KAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRGNVLQLSLPDITLPEPETPP
AATVVAQEGEDEYQLIVRVLKETNGVVAGPKGAAQRLGLKRTTLLSRMKRLGIDKS
>gnl|CDD|185328 PRK15430, PRK15430, EamA family transporter RarD
MDAKQTRQGVLLALAAYFIWGIAPAYFKLIYYVPADEILTHRVIWSFFFMVVLMSICRQWSYLKTLIQTP
QKIFMLAVSAVLIGGNWLLFIWAVNNHHMLEASLGYFINPLVNIVLGMIFLGERFRRMQWLAVILAICGV
LVQLWTFGSLPIIALGLAFSFAFYGLVRKKIAVEAQTGMLIETMWLLPVAAIYLFAIADSSTSHMGQNPM
SLNLLLIAAGIVTTVPLLCFTAAATRLRLSTLGFFQYIGPTLMFLLAVTFYGEKPGADKMVTFAFIWVAL
AIFVMDAIYTQRRKSK
>gnl|CDD|185329 PRK15431, PRK15431 [Fe-S]-dependent transcriptional repressor FeoC
MASLIQVRDLLALRGRMEAAQISQTLNTPQPMINAMLQQLESMGKAVRIQEEPDGCLSGSCKSCPEGKAC
LREWWALR
>gnl|CDD|185330 PRK15432, PRK15432, autoinducer 2 ABC transporter permease LsrC; Provisional
MLKFIQNNRELTALLAIVLLFVLLGFLDRQYLSLQTLTMVFSSAQILILLAIGATLVMLTRNIDVSVGSI
TGLCAVLVGMLLNAGYSLPVACLATLLLGLLAGFFNGVLVAWLRIPAIVATLGTLGLYRGIMLLWTGGKW
IEGLPAELKQLSAPILLGISPIGWLTLILILAMAWLLAKTAFGRSFYATGDNLQGARQLGVRTEAIRIVA
FSLNGCMAALAGIVFASQIGFIPNQTGTGLEMKAIAACVLGGISLLGGSGTIIGAVLGAYFLTQIDSVLV
LLRIPAWWNDFIAGLVLLGVLVFDGRLRCALERNLRRQKYARFMTPPPSVKPAASGHNKKKEAA
>gnl|CDD|185331 PRK15433, PRK15433, branched-chain amino acid transporter carrier protein BrnQ
MTHQLRSRDIIALGFMTFALFVGAGNIIFPPMVGLQAGEHVWTAAFGFLITAVGLPVLTVVALAKVGGGV
DSLSTPIGKVAGVLLATVCYLAVGPLFATPRTATVSFEVGIAPLTGDSALPLFIYSLVYFAIVILVSLYP
GKLLDTVGNFLAPLKIIALVILSVAAIVWPAGSISTATEAYQNAAFSNGFVNGYLTMDTLGAMVFGIVIV
NAARSRGVTEARLLTRYTVWAGLMAGVGLTLLYLALFRLGSDSASLVDQSANGAAILHAYVQHTFGGGGS
FLLAALIFIACLVTAVGLTCACAEFFAQYVPLSYRTLVFILGGFSMVVSNLGLSQLIQISVPVLTAIYPP
CIALVVLSFTRSWWHNSSRVIAPPMFISLLFGILDGIKASAFSDILPSWAQRLPLAEQGLAWLMPTVVMV
VLAIIWDRAAGRQVTSSAH
>gnl|CDD|237966 PRK15434, PRK15434, GDP-mannose mannosyl hydrolase
MFLRQEDFATVVRSTPLISLDFIVENSRGEFLLGKRTNRPAQGYWFVPGGRVQKDETLEAAFERLTMAEL
GLRLPITAGQFYGVWQHFYDDNFSGTDFTTHYVVLGFRLRVAEEDLLLPDEQHDDYRWLTPDALLASDNV
HANSRAYFLAEKRAGVPGL
>gnl|CDD|185333 PRK15435, PRK15435, bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada
MKNATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCK
RCQPDKANPQQHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRL
REALAKGESVTTSILNAGFPDSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGI
CAILLGDDDAALISELQQMFPAADNAPADLTFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALR
TIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIPCHRVVRGDGALSGYRWGVSRKAQLLRREAE
NEE
>gnl|CDD|185334 PRK15437, PRK15437, histidine ABC transporter substrate-binding protein HisJ; Provisional
MKKLVLSLSLVLAFSSATAAFAAIPQNIRIGTDPTYAPFESKNSQGELVGFDIDLAKELCKRINTQCTFV
ENPLDALIPSLKAKKIDAIMSSLSITEKRQQEIAFTDKLYAADSRLVVAKNSDIQPTVESLKGKRVGVLQ
GTTQETFGNEHWAPKGIEIVSYQGQDNIYSDLTAGRIDAAFQDEVAASEGFLKQPVGKDYKFGGPSVKDE
KLFGVGTGMGLRKEDNELREALNKAFAEMRADGTYEKLAKKYFDFDVYG
>gnl|CDD|185335 PRK15438, PRK15438, erythronate-4-phosphate dehydrogenase PdxB; Provisional
MKILVDENMPYARELFSRLGEVKAVPGRPIPVAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTD
HVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLHDRTVGIVGVGNVGRRLQARLEALGI
KTLLCDPPRADRGDEGDFRSLDELVQEADILTFHTPLFKDGPYKTLHLADEKLIRSLKPGAILINACRGA
VVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLKKVDIGTPHIAGYTLEGKARGTTQVFEAYSKFIGH
EQHVALDTLLPAPEFGRITLHGPLDQPTLKRLVHLVYDVRRDDAPLRKVAGIPGEFDKLRKNYLERREWS
SLYVICDDASAASLLCKLGFNAVHHPAR
>gnl|CDD|185336 PRK15439, PRK15439, autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI
GGNPCARLTPAKAHQLGIYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGS
LEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRI
SVMRDGTIALSGKTADLSTDDIIQAITPAAREKSLSASQKLWLELPGNRRQQAAGAPVLTVEDLTGEGFR
NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSS
GLYLDAPLAWNVCALTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEA
SPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI
NVDTIMRLAFGEHQAQEASC
>gnl|CDD|185337 PRK15440, PRK15440, L-rhamnonate dehydratase; Provisional
MTLPKIKHVRAWFVGGGGADYHDQGANHWIDDHIATPMSKYPEYRQSRQSFGINVLGTLVVEVEAENGQV
GFAVSTAGEMGAFIVEKHLNRFIEGKCVSDIELIWDQMLNATLYYGRKGLVMNTISCVDLALWDLLGKVR
GLPVYKLLGGAVRDELQFYATGARPDLAKEMGFIGGKMPLHHGPADGDAGLRKNAAMVADMREKVGDDFW
LMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRNAPAGMMVTSGEHEATLQGFRTLL
EMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSVYSHHFVITRTNSPFSEFLMMSPDADTVV
PQFDPILLDEPVPVNGRIHKSVLDKPGFGVELNRDCNLKRPYSH
>gnl|CDD|185338 PRK15441, PRK15441, peptidyl-prolyl cis-trans isomerase C; Provisional
MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCP
VLEPTGPLHTQFGYHIIKVLYRN
>gnl|CDD|185339 PRK15442, PRK15442, beta-lactamase TEM; Provisional
IQHFRVALIPFFAAFCLPVFAHPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKV
LLCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGG
PKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTMPAAMATTLRKLLTGELLTLASRQQLIDWMEAD
KVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNRQIAEIGASL
IKHW
>gnl|CDD|185340 PRK15443, pduE, diol dehydratase small subunit
RTATVSDYPLATKRPELVKTPTGKSLDDITLENVLSGKVTAEDLRITPETLRMQAQIAEDAGRPQLAMNF
RRAAELTAVPDDRILEIYNALRPYRSTKEELLAIADELENKYQAKICAAFVREAAEVYERRKKLKGDD
>gnl|CDD|185341 PRK15444, pduC, propanediol/glycerol family dehydratase large subunit
MRSKRFEVLAKRPVNQDGFVKEWPEEGLIAMESPNDPKPSIKIENGKVVELDGKPREDFDLIDHFIARYG
IDLERAEEVMAMDSVKLARMLVDPNVPREEIVRLTTAMTPAKIVEVVSQMNVVEMMMAMQKMRARRTPSN
QAHVTNVKDNPVQIAADAAEAALRGFDEQETTVAVARYAPFNAIALLVGSQVGRPGVLTQCSLEEATELK
LGMRGLTSYAETISVYGTEPVFTDGDDTPWSKAFLASAYASRGLKMRFTSGTGSEVQMGYAEGKSMLYLE
ARCIYITKAAGVQGLQNGSVSCIGVPAAVPSGIRAVLAENLIASMLDLECASGNDQTFSHSDIRRTARLL
MQFLPGTDFIFSGYSAVPNYDNMFAGSNFDAEDFDDYNVLQRDLKVDGGLRPVREEEVIAVRNKAARALQ
AVFRELGLPPITDEEVEAATYAHGSKDMPERNVVEDLKAAQEIMNRGITGLDVVKALAKGGFTDVAENIL
NMLKQRVTGDYLQTSAIIDEDFNVLSAVNDPNDYAGPGTGYRLSGERWEEIKNIPQALDPEEIE
>gnl|CDD|185342 PRK15445, PRK15445, arsenical efflux pump membrane protein ArsB
LLAIAIFLLTLVLVIWQPKGLGIGWSALLGAVLALLTGVVSLGDVPVVWGIVWNATLTFIAIIIISLLLD
EAGFFEWAALHVARWAKGNGRKLFVYIVLLGAAVAALFANDGAALILTPIVLAMLLALGFSKKATLAFVM
AAGFIADTASLPLVVSNLVNIVSADYFGIGFAEYASVMVPVNLVSLAASLLVLWLYFRKDIPKTYDLELL
KEPASAIKDPALFKLGWIVLALLLVGYFVLEPLGIPVSAIAGVGALILLLVARRGHAINTKKVLKGAPWQ
IVIFSLGMYLVVYGLRNAGLTDYLAGVLNYLADQGLFAATLGTGFLAAFLSSVMNNMPTVLIGALAIDGS
NATGVIKEAMIYANVIGSDLGPKITPIGSLATLLWLHVLAQKGVKISWGYYFKVGIIITLPVLLVTLLAL
ALRLSLF
>gnl|CDD|237967 PRK15446, PRK15446, phosphonate metabolism protein PhnM; Provisional
MMEMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGAIDAEGDYLLPGLVDLHTDNLEKHLAPRP
GVDWPADAALAAHDAQLAAAGITTVFDALSVGDEEDGGLRSRDLARKLIDAIEEARARGLLRADHRLHLR
CELTNPDALELFEALLAHPRVDLVSLMDHTPGQRQFRDLEKYREYYAGKYGLSDEEFDAFVEERIALSAR
YAPPNRRAIAALARARGIPLASHDDDTPEHVAEAHALGVAIAEFPTTLEAARAARALGMSVLMGAPNVVR
GGSHSGNVSALDLAAAGLLDILSSDYYPASLLDAAFRLADDGGLDLPQAVALVTANPARAAGLDDRGEIA
PGKRADLVRVRRAGGLPVVRAVWRGGRRVFLAG
>gnl|CDD|237968 PRK15447, PRK15447, putative protease; Provisional
MKLSLGPVLYYWPKETVRDFYQRAADSPVDIVYLGETVCSKRRELKVGDWLELAERLAAAGKEVVLSTLA
LVEAPSELKELRRLVENGEFLVEANDLGAVRLLAERGLPFVAGPALNCYNAATLALLARLGATRWCMPVE
LSRDWLANLLAQCPELGRNQFEVEVFAYGRLPLAYSARCFTARHEDLPKDNCQFVCIKYPDGLPVLTQEG
QPFLALNGIQTQSGYCYNLLNELPSMQALGVDVVRLSPQSTDMVAVADAFRAVLNGAAPAAEALARLLPL
APAADCNGYWHGRAGLELVAR
>gnl|CDD|185345 PRK15448, PRK15448, ethanolamine utilization microcompartment protein EutN
MKLAVVTGQIVCTVRHHGLAHDKLLMVEMIDPQGNPDGQCAVAIDNIGAGTGEWVLLVSGSSARQAHKSE
TSPVDLCVIGIVDEVVSGGQVIFHK
>gnl|CDD|185346 PRK15449, PRK15449, ferredoxin-like protein FixX; Provisional
MTSPVNVDVKLGVNKFNVDEEHPHIVVKADADKQALELLVKACPAGLYKKQDDGSVRFDYAGCLECGTCR
ILGLGSALEQWEYPRGTFGVEFRYG
>gnl|CDD|185347 PRK15450, PRK15450, signal transduction protein PmrD; Provisional
MEWLVKKSCCNKQDNRHVLVLCDAGGALKMIAEVKSDFALKVGDLLSPLQNALYCINREKLQTLKILSAS
CYSPDEWERQCKKAG
>gnl|CDD|185348 PRK15451, PRK15451, carboxy-S-adenosyl-L-methionine synthase CmoA
MSHRDTLFSAPIARLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLAERFVQPGTQVYDLGCSLGAA
TLSVRRNIHHDNCKIIAIDNSPAMIERCRRHIDAYKAPTPVDVIEGDIRDIAIENASMVVLNFTLQFLEP
SERQALLDKIYQGLNPGGALVLSEKFSFEDAKVGELLFNMHHDFKRANGYSELEISQKRSMLENVMLTDS
VETHKARLHKAGFEHSELWFQCFNFGSLVALKAEDAA
>gnl|CDD|237969 PRK15452, PRK15452, putative protease; Provisional
MFKPELLSPAGTLKNMRYAFAYGADAVYAGQPRYSLRVRNNEFNHENLALGINEAHALGKKFYVVVNIAP
HNAKLKTFIRDLEPVIAMKPDALIMSDPGLIMMVREHFPEMPIHLSVQANAVNWATVKFWQQMGLTRVIL
SRELSLEEIEEIRQQCPDMELEVFVHGALCMAYSGRCLLSGYINKRDPNQGTCTNACRWEYKVHEAKEDD
VGDIVHKHPIPVQNVEPTLGIGAPTDKVFLLEEAQRPGEYMPAFEDEHGTYIMNSKDLRAIQHVERLTKM
GVHSLKIEGRTKSFYYVARTAQVYRKAIDDAVAGKPFDPSLLGTLEGLAHRGYTEGFLRRHVHDEYQNYE
YGYSVSDRQQFVGEFTGERAGTGLAEVEVKNKFSVGDSLELMTPQGNINFTLERMENRKGEAMEVAPGSG
HTVWLPVPADVDLDYALLMRNLS
>gnl|CDD|237970 PRK15453, PRK15453, phosphoribulokinase; Provisional
MSAKHPIIAVTGSSGAGTTTVKRAFEKIFRRENINAAVVEGDSFHRYTRPEMKAAIAKARAAGRHFSHFG
PEANLFDELEQLFREYGETGTGKTRKYLHTDDEAVPYNQVPGTFTPWEPLPEGTDLLFYEGLHGGVVTDQ
VDVAQHVDLLIGVVPIVNLEWIQKIHRDTSERGYSREAVMDTILRRMPDYINYITPQFSRTHINFQRVPT
VDTSNPFIARDIPTPDESFVVIRFRNPKGIDFPYLLSMIQGSFMSRANTIVVPGGKMGLAMELILTPLIQ
RLMERKRIAA
>gnl|CDD|185351 PRK15454, PRK15454, ethanolamine utilization ethanol dehydrogenase EutG
MQAELQTALFQAFDTLNLQRVKTFSVPPVTLCGPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLT
RSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMS
ETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTG
IDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESMLLASCMAGMAFSSAGLGLC
HAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRALRTKKSDDRDAINAVSELIAEVGIGK
RLGDVGATSAHYGAWAQAALEDICLRSNPRTASLEQIVGLYAAAQ
>gnl|CDD|185352 PRK15455, PRK15455, PrkA family serine protein kinase; Provisional
MDIFDHYQQRYEAAKEEEFSLQEYLELCKQDPSAYANAAERLLMAIGEPEMVDTAKDPRLSRIFSNRVIK
RYPAFEEFYGMEEAIEQIVSYFRHAAQGLEEKKQILYLLGPVGGGKSSLAERLKSLMERVPIYVLKANGE
RSPVNESPLGLFDPDEDGPILEEEYGIPRRYLGTIMSPWAVKRLHEFGGDISKFRVVKVYPSILRQIAIA
KTEPGDENNQDISSLVGKVDIRKLEHYAQNDPDAYSYSGGLCRANQGLLEFVEMFKAPIKVLHPLLTATQ
EGNYNGTEGIGAIPFDGIILAHSNESEWQTFRNNKNNEAFLDRIYIVKVPYCLRVSEEIKIYEKLLRNSE
LAHAPCAPGTLEMLARFSVLSRLKEPENSSIYSKMRVYDGESLKDTDPKAKSYQEYRDYAGVDEGMNGLS
TRFAFKILSRVFNFDHTEVAANPVHLMYVLEQQIEREQFPQETEERYLEFIKGYLAPRYAEFIGKEIQTA
YLESYSEYGQNIFDRYVTYADFWIQDQEYRDPDTGQLFDREALNAELEKIEKPAGISNPKDFRNEIVNFV
LRARANNGGRNPSWTSYEKLRTVIEKKMFSNTEDLLPVISFNAKTSTDEQKKHDDFVDRMMEKGYTEKQV
RLLCEWYLRVRKSS
>gnl|CDD|185353 PRK15456, PRK15456, universal stress protein UspG; Provisional
MYKTIIMPVDVFEMELSDKAVRHAEFLAQDDGVIHLLHVLPGSASLSLHRFAADVRRFEEHLQHEAEERL
QTMVSHFTIDPSRIKQHVRFGSVRDEVNELAEELGADVVVIGSRNPSISTHLLGSNASSVIRHANLPVLV
VR
>gnl|CDD|185354 PRK15457, PRK15457, ethanolamine utilization acetate kinase EutQ
MKKLITANDIREAHARGEQAMSVVLRASIITPEAREVADLLGFTITECDESIPVTASVPASVPADKTESQ
RIRETIIAQLPEGQFTESLVAQLMEKVMKEKQSLEQGAMQPSFKSVTGKGGIKVIDGSSVKFGRFDGAEP
HCVGLTDLVTGDDGSSMAAGFMQWENAFFPWTLNYDEIDMVLEGELHVRHEGETMIAKAGDVMFIPKGSS
IEFGTPSSVRFLYVAWPANWQSL
>gnl|CDD|185355 PRK15458, PRK15458, tagatose 6-phosphate aldolase subunit KbaZ; Provisional
MKHLTEMVQQHKAGKTNGIYAVCSAHPLVLEAAIRYALANDSPLLIEATSNQVDQFGGYTGMTPADFRGF
VCQLADSLNFPQEALILGGDHLGPNRWQNLPAAQAMANADDLIKSYVAAGFKKIHLDCSMSCADDPIPLT
DEIVAERAARLAKIAEETCREHFGESDLVYVIGTEVPVPGGAHETLSELAVTTPDAARATLEAHRHAFEK
QGLNAIWPRIIGLVVQPGVEFDHTNVIDYQPEKASALSQMVENYETLVFEAHSTDYQTPQALRQLVIDHF
AILKVGPALTFALREALFSLAAIEEELVPAKACSGLRQVLEDVMLDRPEYWQSHYHGDGNARRLARGYSY
SDRVRYYWPDSQIDDAFAHLVRNLADSPIPLPLISQYLPLQYVKVREGELQPTPRELIINHIQDILAQYH
TACEGQ
>gnl|CDD|185356 PRK15459, PRK15459, flagella biosynthesis chaperone FlgN
MTRLAEILDQMTAVLNDLKTVMDQEQQHLSMGQINGSQLQRITEQKSSLLATLDYLEQQRRKEQNTANSV
NDDISQRWQEITEKTQQLRQLNQHNGWLLEGQIERNQQALEMLKPHQEPTLYGANGQTSTTHRGGKKISI
>gnl|CDD|185357 PRK15460, cpsB, mannose-1-phosphate guanyltransferase; Provisional
MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAE
QLRQLNKLTENIILEPAGRNTAPAIALAALAAKRHSPESDPLMLVLAADHVIADEDAFRAAVRNAMPYAE
AGKLVTFGIVPDLPETGYGYIRRGEVSAGEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRA
GRYLEELKKYRPDILDACEKAMSAVDPDLDFIRVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDV
GSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTTVGVKDLVVVQTKDAVLIADRNAVQDVKK
VVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQMHHHRAEHWVVVAGTAKVT
IDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGRV
>gnl|CDD|185358 PRK15461, PRK15461, sulfolactaldehyde 3-reductase
MAAIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDL
VRSVLFGENGVCEGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGT
AEQVERATPILMAMGNELINAGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSGTA
AGKGHFTTTWPNKVLKGDLSPAFMIDLAHKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWS
AILEQVRVSAGLTAKV
>gnl|CDD|237971 PRK15462, PRK15462, dipeptide permease
MNKHASQPRAIYYVVALQIWEYFSFYGMRALLILYLTNQLKYDDNHAYELFSAYCSLVYVTPILGGFLAD
KVLGNRMAVMLGALLMAIGHVVLGASEIHPSFLYLSLAIIVCGYGLFKSNVSCLLGELYEPTDPRRDGGF
SLMYAAGNVGSIIAPIACGYAQEEYSWAMGFGLAAVGMIAGLVIFLCGNRHFTHTRGVNKKVLRATNFLL
PNWGWLLVLLVATPALITVLFWKEWSVYALIVATIIGLGVLAKIYRKAENQKQRKELGLIVTLTFFSMLF
WAFAQQGGSSISLYIDRFVNRDMFGYTVPTAMFQSINAFAVMLCGVFLAWVVKESVAGNRTVRIWGKFAL
GLGLMSAGFCILTLSARWSAMYGHSSLPLMVLGLAVMGFAELFIDPVAMSQITRIEIPGVTGVLTGIYML
LSGAIANYLAGVIADQTSQASFDASGAINYSINAYIEVFDQITWGALACVGVVLMIWLYQALKFRNRALA
LES
>gnl|CDD|185360 PRK15463, PRK15463, cold shock-like protein CspF; Provisional
MSRKMTGIVKTFDGKSGKGLITPSDGRKDVQVHISALNLRDAEELTTGLRVEFCRINGLRGPTAANVYLS
>gnl|CDD|185361 PRK15464, PRK15464, cold shock-like protein CspH; Provisional
MSRKMTGIVKTFDRKSGKGFIIPSDGRKEVQVHISAFTPRDAEVLIPGLRVEFCRVNGLRGPTAANVYLS
>gnl|CDD|185362 PRK15465, pabB, aminodeoxychorismate synthase component 1
MKTLSPAVITLPWRQDAAEFYFSRLSHLPWAMLLHSGYADHPYSRFDIVVADPICTLTTFGKETVVSESE
KRTTTTDDPLQVLQQVLDRADIRPTHNEDLPFQGGALGLFGYDLGRRFESLPEIAEQDIVLPDMAVGIYD
WALIVDHQRQTVSLLSHNDVNARRAWLESQQFSPQEDFTLTSDWQSNMTREQYGEKFRQVQEYLHSGDCY
QVNLAQRFHATYSGDEWQAFLQLNQANRAPFSAFLRLEQGAILSLSPERFILCDNSEIQTRPIKGTLPRL
PDPQEDSKQAEKLANSAKDRAENLMIVDLMRNDIGRVAVAGSVKVPELFVVEPFPAVHHLVSTITARLPE
QLHASDLLRAAFPGGSITGAPKVRAMEIIDELEPQRRNAWCGSIGYLSFCGNMDTSITIRTLTAINGQIY
CSAGGGIVADSQEEAEYQETFDKVNRILRQLEK
>gnl|CDD|185363 PRK15466, PRK15466, ethanolamine utilization microcompartment protein EutK
MINALGLLEVDGMVAAIDAADAMLKAANVRLLSHEVLDPGRLTLVVEGDLAACRAALDAGCAAAMRTGRV
ISRKEIGRPDDDTQWLVTGFNRQPKQPVKEPDAPVIVAESADELLALLTSVRQGMTAGEVAAHFGWPLEK
ARNALEQLFSAGTLRKRSSRYRLKPH
>gnl|CDD|185364 PRK15467, PRK15467, ethanolamine utilization acetate kinase EutP
MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIY
VHGANDPESRLPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVD
YLASLTKQEEAGEKTHHS
>gnl|CDD|185365 PRK15468, PRK15468, ethanolamine utilization microcompartment protein EutS
MDKERIIQEFVPGKQVTLAHLIAHPGEELAKKIGVPDAGAIGIMTLTPGETAMIAGDLALKAADVHIGFL
DRFSGALVIYGSVGAVEEALSQTVSGLGRLLNYTLCEMTKS
>gnl|CDD|185366 PRK15469, ghrA, glyoxylate/hydroxypyruvate reductase GhrA
MDIIFYHPTFDTQWWIEALRKALPQARVRAWKSGDNDPADYALVWHPPVEMLAGRDLKAVFALGAGVDSI
LSKLQAHPEMLDPSVPLFRLEDTGMGEQMQEYAVSQVLHWFRRFDDYQALQNSSHWQPLPEYHREDFTIG
ILGAGVLGSKVAQSLQTWGFPLRCWSRSRKSWPGVQSFAGREELSAFLSQTRVLINLLPNTPETVGIINQ
QLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREPLPPESPLWQHPRVAITPHVAAVT
RPAEAVEYISRTIAQLEKGERVCGQVDRARGY
>gnl|CDD|185367 PRK15470, emtA, membrane-bound lytic murein transglycosylase EmtA
MKLRWFAFLIVLLAGCSSKHDYTNPPWNAKVPVQRAMQWMPISQKAGAAWGVDPQLITAIIAIESGGNPN
AVSKSNAIGLMQLKASTSGRDVYRRMGWSGEPTTSELKNPERNISMGAAYLNILETGPLAGIEDPKVLQY
ALVVSYANGAGALLRTFSSDRKKAISKINDLDADEFLEHVARNHPAPQAPRYIYKLEQALDAM
>gnl|CDD|185368 PRK15471, PRK15471, chain length determinant protein WzzB; Provisional
MRVENNNVSGQNHDPEQIDLIDLLVQLWRGKMTIIISVIVAIALAVGYLAVAKEKWTSTAIITQPDVGQI
AGYNNAMNVLYGDNAPKVSDVQATLIGRFSSAFSALAETLDNQEEPEKLTIEPSVKGQALPLSVSYVGQT
AEGAQKKLAQYIQQVDDQVAKELEKDLKDNIALRTKTLQDSLETQEVVAQEQKDLRIKQIQEALQYANQA
NITKPQIQQTQDVTQDTLFLLGSEALESMIKHEATRPLVFSPNYYQTRQNLLDIENLKVDEDDIHAYRYV
MKPTLPVRRDSPKKAITLVLAVLLGGMIGAGIVLGRNALRNYNAK
>gnl|CDD|185369 PRK15472, PRK15472, nucleoside triphosphatase NudI; Provisional
MRQRTIVCPLIQNDGAYLLCKMADDRGVFPGQWALSGGGVEPGERIEEALRREIREELGEQLLLTEITPW
TFRDDIRTKTYADGRKEEIYMIYLIFDCVSANRDVKINEEFQDYAWVKPEDLVHYDLNVATRKTLRLKGL
L
>gnl|CDD|185370 PRK15473, cbiF, cobalt-precorrin-4 methyltransferase
MSETFDPRCVWFVGAGPGDKELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAECHDSAELHLEQII
DLMEAGVKAGKTVVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSL
IITRMEGRTPVPAREQLESFASHQTSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRG
TLADIAEKVRDAGIRKTALILVGNFLGEEYHYSKLYDADFSHEYRKA
>gnl|CDD|185371 PRK15474, PRK15474, ethanolamine utilization microcompartment protein EutM
MEALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELV
SVHVIPRPHGDLEEVFPIGLKGDSSNL
>gnl|CDD|185372 PRK15475, PRK15475, oxaloacetate decarboxylase subunit beta; Provisional
MESLNALLQGMGLMHLGAGQAIMLLVSLLLLWLAIAKKFEPLLLLPIGFGGLLSNIPEAGMALTALESLL
AHHDAGQLAVIAAKLNCAPDVHAIKEALALALPSVQGQMENLAVDMGYTPGVLALFYKVAIGSGVAPLVI
FMGVGAMTDFGPLLANPRTLLLGAAAQFGIFATVLGALTLNYFGLISFTLPQAAAIGIIGGADGPTAIYL
SGKLAPELLGAIAVAAYSYMALVPLIQPPIMKALTTETERKIRMVQLRTVSKREKILFPVVLLLLVALLL
PDAAPLLGMFCFGNLMRESGVVERLSDTVQNGLINIVTIFLGLSVGAKLVADKFLQPQTLGILLLGVIAF
GIGTAAGVLMAKLLNLCSKNKINPLIGSAGVSAVPMAARVSNKVGLESDPQNFLLMHAMGPNVAGVIGSA
IAAGVMLKYVLAM
>gnl|CDD|185373 PRK15476, PRK15476, oxaloacetate decarboxylase subunit beta; Provisional
MESLNALLQGMGLMHLGAGQAIMLLVSLLLLWLAIAKKFEPLLLLPIGFGGLLSNIPEAGMALTALESLL
AHHDAGQLAVIAAKLNCAPDVHAIKEALALALPSVQGQMENLAVDMGYTPGVLALFYKVAIGSGVAPLVI
FMGVGAMTDFGPLLANPRTLLLGAAAQFGIFATVLGALTLNYFGLISFTLPQAAAIGIIGGADGPTAIYL
SGKLAPELLGAIAVAAYSYMALVPLIQPPIMKALTTEKERKIRMVQLRTVSKREKILFPVVLLLLVALLL
PDAAPLLGMFCFGNLMRESGVVERLSDTVQNGLINIVTIFLGLSVGAKLVADKFLQPQTLGILLLGVIAF
GIGTAAGVLMAKLLNLCSKNKINPLIGSAGVSAVPMAARVSNKVGLESDPQNFLLMHAMGPNVAGVIGSA
IAAGVMLKYVLAM
>gnl|CDD|185374 PRK15477, PRK15477, oxaloacetate decarboxylase subunit beta; Provisional
MESLNALLQGMGLMHLGAGQAIMLLVSLLLLWLAIAKKFEPLLLLPIGFGGLLSNIPEAGMALTALESLL
AHHDAGQLAVIAAKLNCAPDVHAIKEALALALPSVQSQMENLAVDMGYTPGVLALFYKVAIGSGVAPLVI
FMGVGAMTDFGPLLANPRTLLLGAAAQFGIFATVLGALTLNYFGLISFTLPQAAAIGIIGGADGPTAIYL
SGKLAPELLGAIAVAAYSYMALVPLIQPPIMKALTTEKERKIRMVQLRTVSKREKILFPVVLLLLVALLL
PDAAPLLGMFCFGNLMRESGVVERLSDTVQNGLINIVTIFLGLSVGAKLVADKFLQPQTLGILLLGVIAF
GIGTAAGVLMAKLLNLCSKNKINPLIGSAGVSAVPMAARVSNKVGLESDPQNFLLMHAMGPNVAGVIGSA
IAAGVMLKYVLAM
>gnl|CDD|185375 PRK15478, cbiH, precorrin-3B C(17)-methyltransferase
MLSVIGIGPGSQAMMTMEAIEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCKEIERCQAAIELAQAG
HNVALISSGDAGIYGMAGLVLELVSKQKLDVEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWP
VIEKRIVAAGEADFVICFYNPRSRGREGHLARAFDLLAASKSAQTPVGVVKSAGRKKEEKWLTTLGDMDF
EPVDMTSLVIVGNKTTYVQDGLMITPRGYTL
>gnl|CDD|185376 PRK15479, PRK15479, transcriptional regulator TctD
MRLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRG
QTLPVLLLTARSAVADRVKGLNVGADDYLPKPFELEELDARLRALLRRSAGQVQEVQQLGELIFHDEGYF
LLQGQPLALTPREQALLTVLMYRRTRPVSRQQLFEQVFSLNDEVSPESIELYIHRLRKKLQGSDVRITTL
RGLGYVLERGD
>gnl|CDD|185377 PRK15480, PRK15480, glucose-1-phosphate thymidylyltransferase RfbA; Provisional
MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGD
GSQWGLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHV
NDPERYGVVEFDQNGTAISLEEKPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQ
GRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIEERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNA
YGQYLLKMIKGY
>gnl|CDD|185378 PRK15481, PRK15481, transcriptional regulatory protein PtsJ; Provisional
MITGKTANEIFDSIRQLIQAGRLRPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQGRNGTVIR
GSPSPVALEGGDPGTPLHDLAGGNPDPQRLPDLSRYFARLSRTPRLYGDAPVSPELHAWAARWLRDDCPV
AFEIDLTSGAIDAIERLLCAHLLPGDSVAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQPEKLERALAQ
GARAVILTPRAHNPTGCSLSARRAAALRNLLARYPQVLVIIDDHFALLSSSPYHSVIPQTTQRWALIRSV
SKALGPDLRLAFVASDSATSARLRLRLNSGTQWVSHLLQDLVYACLTDPEYQARLAQARLFYAQRRQKLA
RALQQYGIAIPSPGDGLNLWLPLDTDSQATALTLAKSGWLVREGEAFGVSAPSHGLRITLSTLNDAEINR
LAADLHQALNR
>gnl|CDD|185379 PRK15482, PRK15482, HTH-type transcriptional regulator MurR
MLYLTKIRNAESEFTENEQKIADFLRANVSELKSVSSRKMAKQLGISQSSIVKFAQKLGAQGFTELRMAL
IGEYSASREKTNATALHLHSSITSDDSLEVIARKLNREKELALEQTCALFDYARLQKIIEVISKAPFIQI
TGLGGSALVGRDLSFKLMKIGYRVACEADTHVQATVSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGA
TVIAITSLADSPLRRLAHFTLDTVSGETEWRSSSMSTRTAQNSVTDLLFVGLVQLNDVESLKMIQRSSEL
TQRLK
>gnl|CDD|237972 PRK15483, PRK15483, type III restriction-modification system endonuclease
MGILLEELPHQEQALAAILAAFTGIDIASADPNHYANPLIKLRYENGIPGRSRTRIDDKANIDIKMETGT
GKTYVYTRLMYELHQKYGLFKFIIVVPTPAIKEGTRNFIQSDYAKQHFSQFYENTRIELYVINAGDKKKS
GRKNFPAQLSNFVKASRQNSNTIHVLLINAGMLNSASMTRDDYDQTLLGGFTSPVDALAATRPVVIIDEP
HRFPRDNKFYQAIEALKPQMIIRFGATFPDITEGKGKNKCTRKDYYNLQFDLNAVDSFNDGLVKGVDIFY
PEMPEEQANNVKIVDSVTAKKLILRRGKKTFELAVGENLADIDPGFEGLTIEYAGKTSVVLSNGLELEKG
MALVPGTYSQSYQELMIQQAIDKHFETERANFLRRNEPPKIKTLSLFFIDSIASYRDDNELEGWLKLKFE
RLLKKKLERLIKTYQRKTLPREVEYLSYLQATLADLSSVHAGYFSEDNGSSDEAIQAEVNDILHNKEKLL
SFKDEDGNWNTRRFLFSKWTLREGWDNPNVFQIAKLRSSGSETSKLQEVGRGLRLPVDENGHRVSQEEFR
LNYLIDYDEKDFASKLVGEINSDSKVQLNEEKLTEEMIQKIVTEKQKVDPDFTELRLLEDLDDKKIIDRS
NNFKEDGFDWLLEAYPELFQTGLRKGKVRDNKPASKLTVKLRKENYEELKSLWEQINRRYMLQFEIISEA
SLEQLAAEVLRDPALYIRQIPTQVQQRLVSNDDNGRVEVSQREGELAASEYLNGMKYGEFLKQLAQRTKL
PVNVLHQALMALLKEVLHGDSRYLNEITLDNIIRAFNRWLNEHFAQRFSYKPLDFQASTTAFTDKDGQFR
EEISAGIIGKNVDTGAIPDERYLYDPLRYDSPDEELNILKNDYIDQVSVFGKIPRRSIQIPKYTGGTTSP
DFMYVIEKDGGKSLNLVVETKAVDEAENLRVGEERKIDAAKKFFDMLSEDGINVVFKTQTSAKAVASLIN
GLIEGK
>gnl|CDD|185381 PRK15484, PRK15484, lipopolysaccharide N-acetylglucosaminyltransferase
MIDKIIFTVTPIFSIPPRGAAAVETWIYQVAKRTSIPNRIACIKNPGYPEYTKVNDNCDIHYIGFSRIYK
RLFQKWTRLDPLPYSQRILNIAHKFTITKDSVIVIHNSMKLYRQIRERAPQAKLVMHMHNAFEPELLDKN
AKIIVPSQFLKKFYEERLPNADISIVPNGFCLETYQSNPQPNLRQQLNISPDETVLLYAGRISPDKGILL
LMQAFEKLATAHSNLKLVVVGDPTASSKGEKAAYQKKVLEAAKRIGDRCIMLGGQPPEKMHNYYPLADLV
VVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLAEPMTSDSIISDINRTLADPELTQI
AEQAKDFVFSKYSWEGVTQRFEEQIHNWFD
>gnl|CDD|185382 PRK15485, PRK15485, energy-coupling factor ABC transporter transmembrane protein
MTGIDKLSYQSRWIHVAPQRKFLLYLAMMILAFTLPPLGQAIELLIIAGLTCWLLRISLWRYLRWLAIPF
GFLLVGLLTILFSISRDPQSLLAGISIGPYWIGISRAGVVTANQTFWRSLAALAATLWFVLNLPFPQLIK
LLKRAHIPRLLTEQILLTWRFIFILLEEAAAIRRAQSLRFGYCSLPNGYRSLAMLVGLLFTRVLMRYQQM
TTTLDIKLYQGDFHL
>gnl|CDD|185383 PRK15486, hpaC, 4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional
MQLDEQRLRFRDAMASLSAAVNIVTTAGDAGRCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKL
CINVLNHEQELMARHFAGMTGMAMEERFSLSCWQKGPLGQPVLKGSLASLEGEISDVQTIGTHLVYLVEI
KNIILSAEGHGLIYFKRRFHPVMLEMEAAV
>gnl|CDD|185384 PRK15487, PRK15487, O-antigen ligase RfaL; Provisional
SFTLNKENWKPYWNRALVFLFIATYFLDGITRYKHLIIILMTITAIYYLSRDPKHFLSLFKNSLFYSVAV
LSLALLYSILISPDMKLSFKEFNKTILEGFLLYTLLIPVLLKDETKETVAKIVLFSFITGLGLRCLSELI
LYIKDYNQGIMPFTNYAHRSISDSMVFLFPALLNLWLIKKNHYKISFLVLSAIFLFLILGTLSRGAWLAV
LVVGLLWIILNRQWKLLLVGAIVLAIAGALVFTQHNNKEDTAKLLYKLQQTDSSYRYTNGTQGTAWDLIL
ENPIKGYGYGNDVYHDVYNKRVVDYPTWTFRQSIGPHNTILYIWFAAGILGLISLLYLYGAIIKETASST
FRKVEISPYNAHLILLLSFIGFYIVRGNFEQVDINQIGIITGLLLALRNK
>gnl|CDD|237973 PRK15488, PRK15488, thiosulfate reductase PhsA; Provisional
MSLSRRDFLKGAGAGCAACALGSLLPGALAANEIAQLKGKTKLTPSICEMCSTRCPIEARVVNGKNVFIQ
GNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPE
SVAFSSKSGSLSSHLFHLATAFGSPNTFTHASTCPAGYAIAAKVMFGGKLKRDLANSKYIINFGHNLYEG
INMSDTRGLMTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERY
TSGFEELAASVKEYTPEWAEAISDVPADDIRRIARELAAAAPHAIVDFGHRATFTPEEFDMRRAIFAANV
LLGNIERKGGLYFGKNASVYNKLAGEKVAPTLAKPGVKGMPKPTAKRIDLVGEQFKYIAAGGGVVQSIID
ATLTQKPYQIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERDEEI
SDKSGKNPAYALRQRVVEPIGDTKPSWQIFKELGEKMGLGQYYPWQDMETLQLYQVNGDHALLKELKKKG
YVSFGVPLLLREPKMVAKFVARYPNAKAVDEDGTYGSQLKFKTPSGKIELFSAKLEALAPGYGVPRYRDV
ALKKEDELYFIQGKVAVHTNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKAL
VTPGIRPDTLFAYMGFGSKNKELTRATGKGIHCGNLLPHVTSPVSGTNVHTTGVTLSKA
>gnl|CDD|237974 PRK15489, nfrB, glycosyl transferase family protein
MSSLFWPYWLAHYYAVLETAAVATALVILISSLDDLFIDAWYWVRELYRWLTRERRYRPLTAEQLRERDE
QPLAIMVPAWKEYDVIAKMIENMLATLDYRRYVIFVGTYPNDAETITEVERMRRRYKRLVRVEVPHDGPT
CKADCLNWIIQAIFRYEAGHGIEFAGVILHDSEDVLHPLELKYFNYLLPRKDLVQLPVLSLERKWYEWVA
GTYMDEFAEWHQKDLVVRESLTGTVPSAGVGTCFSRRALLALMKERGNQPFNTSSLTEDYDFSFRLAELG
MQEIFVRFPVQFRVRRTSWFGPRRERTREMLLCVREYFPDTFRTAYRQKARWVLGIAFQGWEQMGWRGSL
ATRYLLFRDRKGIVTSLVSIIAYVLLLNFLLLAVLRRAGWWTMSFPSLFVTGGWMQYLLAANAVALANRL
AQRFYFVGRLYGWEQGLLSIPRMVVGNFINFMAVCRAWRIFLIYLVTGKPIVWDKTMHDFPSNDALGQTR
RRLGELLLTWQAVTPEQLQAALAEQQTRGKPLGRILLSQGWLDDETLAEAIAFQADLPRVSLDNVVLGAL
ADCLPRDLCVRWRVVPFSIGEDGTLNIAVASPLPGEALQEVARAAGRKVAQFIARDSEISAELRLLAGPE
RQATVVFVPLLGDLLLEVGLLDRAAFEKAMDDYRPHVDGRIGDYLVAAGVTPREAIEPAVEEQHRRAAVA
DST
>gnl|CDD|185387 PRK15490, PRK15490, Vi polysaccharide biosynthesis glycosyltransferase TviE
MITQEEKLAALGKTCLTLKQEKKLAQAVALIDSELPTEALTSLAMLKKAEFLHDVNETERAYALYETLIA
QNNDEARYEYARRLYNTGLAKDAQLILKKVSNGVQKKYNNYLGKINKICDLLERLEGKAIPVGTNTCIIA
MKHAILFYRNRQPRQLPVGSFGRLALCTGSLGSGGAERQISRLAIEIARKYRQKGKIGGLKVEEPVELII
RSLTPELRQDFFLKEVLEEQVEVLEIAKITGNLFDDATIESPELRLLLSHLPPVCKYGIKHLVPHLCERK
LDYLSVWQDGACLMIALAALIAGVPRIQLGLRGLPPVVRKRLFKPEYEPLYQALAVVPGVDFMSNNHCVT
RHYADWLKLEAKHFQVVYNGVLPPSTEPSSEVPHKIWQQFTQKTQDADTTIGGVFRFVGDKNPFAWIDFA
ARYLQHHPATRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLI
EAQMVGVPVISTPAGGSAECFIEGVSGFILDDAQTVNLDQACRYAEKLVNLWRSRTGICQQTQSFLQERF
TVEHMVGTFVKTIASQPR
>gnl|CDD|185388 PRK15491, PRK15491, replication factor A; Provisional
MDEIDTIYEKLEGIISREDFEAKVDEKVEQMSGLCDVKTAALLVAHDLGVTDTGVDTTKIADINESSSNV
NFTAKVVSIFEPKEFNRNDGTTGRVGNIIVADETGSIRLTLWDDLADLIKTGDIEVGKSLNISGYAKEGY
SGIEVNIGRYGGISESDENVKASINSQKISDIKDGDSDINIVGKVLDISDVRTFQKKDGSQGRVRNITIG
DETGKIRVTLWDGKTDLADKLENGDSVEIINGYARTNNYSQEVEIQIGNHGSLRKTDRNVEYEEDFTPIA
DIIPGQPYSIKGAVSGLGDLKEFTKSDGSENKVSNIYVSDDTGRIRIALWGEKAELVDKLDIDTPIKIID
AFSKSGYNEDVELSAGNRSRVVVD
>gnl|CDD|185389 PRK15492, PRK15492, triosephosphate isomerase; Provisional
MKKIYFGTNLKMYKGIADATDFLAKLSELADDIPADKDIELFVIPSFTAIQDAIAATLAIPHDHPIIIGA
QNMNPNDNGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQ
KNYGISDEILRTQLKIGLHGINPDQLAKLRIAYEPVWAIGEAGIPASADYADEKHAVIKQCLIELFGDAG
DDIPVFYGGSVNAENANELFGQPHIDGLFIGRSAWDADKFFAIIEGILNK
>gnl|CDD|185390 PRK15493, PRK15493, bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase
MKTTYVNATIVTMNEQNEVIENGYIIVENDQIIDVNSGEFASDFEVDEVIDMKGKWVLPGLVNTHTHVVM
SLLRGIGDDMLLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQDAIMETVS
RSGMRAAVSRTLFSFGTKEDEKKAIEEAEKYVKRYYNESGMLTTMVAPHSPYTCSTELLEECARIAVENQ
TMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNL
KLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEEMRIATLLQKGIHQDATALPVETALTLATKGAAE
VIGMKQTGSLEVGKCADFITIDPSNKPHLQPADEVLSHLVYAASGKDISDVIINGKRVVWNGECKTLDEE
RIIFEASRYKRGLQR
>gnl|CDD|240225 PTZ00004, PTZ00004, actin-2; Provisional
MSVEETNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKY
PIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAV
LSLYASGRTTGIVLDSGDGVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIV
RDIKEKLCYIALDFDEEMGNSAGSSDKYEESYELPDGTIITVGSERFRCPEALFQPSLIGKEEPPGIHEL
TFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELTTLAPSTMKIKVVAPPERKYSVWIGGSILS
SLPTFQQMWVTKEEYDESGPSIVHRKCF
>gnl|CDD|173310 PTZ00005, PTZ00005, phosphoglycerate kinase; Provisional
MLSNKLGIDDVDDQLKGKRVLIRVDFNVPIKEGVIKDATRIKATLPTIKYLLEQGAKSVVLMSHLGRPDG
RRVEKYSLKPVVPKLEELLGKKVTFLNDCVGPEVEEACANAKNGSVILLENLRFHIEEEGKGVDANGNKV
KADKEEVKKFRKSLTKLGDIYVNDAFGTAHRAHSSMVGVDLPVKVAGFLMKKELDYFSKALENPQRPFLA
ILGGAKVADKIQLIKNLLDKVDEMIIGGGMAFTFKKVLDNMPIGKSLFDEEGAKIVKEIMEKAKEKNVKI
HLPVDFVCADKFDNNANTKVVTDKEGIPDGWMGLDAGPKSIEEFAEAILRAKTIVWNGPQGVFEMPNFAK
GSIAMLDAVVKATEKGAITIVGGGDTASLVEKTGAANKVSHVSTGGGASLELLEGKELPGVVALSNK
>gnl|CDD|240226 PTZ00007, PTZ00007, (NAP-L) nucleosome assembly protein -L; Provisional
MATAEDNQPIPMEDESDIIEGLDSIELDDEKLSHLTDEQRETLKKLQLLQKEFDDLEVEYNAELRKLRSK
YEDLYNPIYDKRKEALVQNGGAEIGTPGLPQFWLTAMKNNNTLGSAIEEHDEPILSYLSDISCEYTEPNK
QEGFILVFTFAPNPFFSNTVLTKTYHMKVLDGDDEPLLSNTVATEIDWKQGKDVTKKVVTKKQRHKKTKE
TRTVTETVDRESFFNFFTSHEVPSDEELEKMSKHEIAELEMIVETDYEIGITIRDKLIPYAVYWFLGEAI
DEDSDYSSDEDDDDYDSYDSSDSASSDSNSDVDTNEEDDRGEKESNGAKSNELHLTS
>gnl|CDD|185394 PTZ00008, PTZ00008, (NAP-S) nucleosome assembly protein-S; Provisional
MELDEECAKEQMNIQRQFDEKKKPLFEKRQEIIEKIPGFWADTLRRHPALSYLVPEDIDILEHLKKIDLE
DNLDNNGSYKITLIFDEKAKEFMEPLVLVKHVIFKNNQEKVVEVTKIKWKEGKSPIAAAEKARSDLDDEC
IVWSIFEWFTEEEWQDRPDVGEIIRREIWHAPLLYYLDTVSIDDE
>gnl|CDD|240227 PTZ00009, PTZ00009, heat shock 70 kDa protein; Provisional
MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDA
KRLIGRKFDDSVVQSDMKHWPFKVTTGGDDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQV
KDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSL
LTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQDFKRKNRGKDLSSNQRALRRLRTQCERAKRTLSSST
QATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQS
LIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTPLSLGLETAGGVMTKLIERNT
TIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDIDANGILNV
SAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKV
KGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQAAGGGMPGGMPGGMPG
GMPGGAGPAGAGASSGPTVEEVD
>gnl|CDD|240228 PTZ00010, PTZ00010, tubulin beta chain; Provisional
MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEP
GTMDSVRAGPYGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLG
GGTGSGMGTLLISKLREEYPDRIMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADESMCIDNEALYDI
CFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAVNLVPFPRLHFFMMGFAPLTSRGSQQ
YRGLSVPELTQQMFDAKNMMCAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNIK
SSVCDIPPKGLKMSVTFIGNSTAIQEMFRRVGEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATVEEEGEFDEEEEAYEI
>gnl|CDD|140051 PTZ00013, PTZ00013, plasmepsin 4 (PM4); Provisional
MDIAVKEQDYSNGLIKNSAAFENLKFSNIKNFKVQKRFQILYLILFVFVTGIFFFFLISTYFFSPNYKVN
KIVQNTEHLTLAFKIERPYDKVLKTISKKNLKNYVKETFNFFKSGYMKQNYLGSENDVIELDDVANIMFY
GEGEVGDNHQKFMLIFDTGSANLWVPSKKCDSIGCSIKNLYDSSKSKSYEKDGTKVDITYGSGTVKGFFS
KDLVTLGHLSMPYKFIEVTDTDDLEPIYSSSEFDGILGLGWKDLSIGSIDPIVVELKNQNKIDNALFTFY
LPVHDVHAGYLTIGGIEEKFYEGNITYEKLNHDLYWQIDLDVHFGKQTMQKANVIVDSGTTTITAPSEFL
NKFFANLNVIKVPFLPFYVTTCDNKEMPTLEFKSANNTYTLEPEYYMNPLLDVDDTLCMITMLPVDIDDN
TFILGDPFMRKYFTVFDYDKESVGFAIAKN
>gnl|CDD|240229 PTZ00014, PTZ00014, myosin-A; Provisional
MARTKEKAKTANKLFRRNSNVEAFDKSGNVLKGFYVWTDKAPAVKEDPDLMFAKCLVLPGSTGEKLTLKQ
IDPPTNSTFEVKPEHAFNANSQIDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFK
DLGNTTNDWIRRYRDAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASS
KSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQE
DDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIED
IFSILSGVLLLGNVEIEGKEEGGLTDAAAISDESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEG
PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNE
MLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCN
TNLKNNPKYKPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVE
KGKLAKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQL
GFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQR
EKLAAWEPLVSVLEALILKIKKKRKVRKNIKSLVRIQAHLRRHLVIAEIKP
>gnl|CDD|185397 PTZ00015, PTZ00015, histone H4; Provisional
MSGMGKGKKSLGAKGGQKRQKKVLRDNIRGITKGAIRRLARRGGVKRISGDIYEEVRGVLKAFLENVVRD
STAYTEYARRKTVTAMDVVYALKRQGRTLYGF
>gnl|CDD|240230 PTZ00016, PTZ00016, aquaglyceroporin; Provisional
MQSEKDNVCYPMELQLVPIQNNMDEEVAEAQKRPPGGQNFWAPREYRPNVREYVAEFLGTFVLLFFGEGV
VATTHTVGNNGDYLAITIGWGLGVTFGLLVSAGISGGHLNPAVTLGNAVFGKFPWKKLPGYFVAQLLGAF
VGAACVYGLYYGFFKDHGIPELPWETMANGFAGVFATYPREGNFYAIFSELILTAILLLVILAITDPNNC
PAFNYLPVAVGLLVFVIGISFGGNTGYALNPARDLGPRLFSAILWGSEVFTKDNYYFWVPLVAPFVGAVL
GMFLYDKFIPPLIE
>gnl|CDD|185399 PTZ00017, PTZ00017, histone H2A; Provisional
KGGKGKTGGGKAGKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAG
NAAKDNKKKRITPRHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQNKQ
>gnl|CDD|185400 PTZ00018, PTZ00018, histone H3; Provisional
MARTKQTARKSTGGKAPRKQLASKAARKSAPVTGGIKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQR
LVREIAQDFKTDLRFQSSAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERS
>gnl|CDD|240231 PTZ00019, PTZ00019, fructose-bisphosphate aldolase; Provisional
TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTTEGLEQYISGVILF
EETVYQKAPSGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRA
VLKIDPAKGKPSELAIQENAWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALN
DHGVLLEGCLLKPNMVTPGSDCGVKATPQEVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMN
KLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKALLHRAKANSLAQLGKYKGGDGGAAASESLYV
KDYKY
>gnl|CDD|240232 PTZ00021, PTZ00021, falcipain-2; Provisional
MEYHMEYSPNESIKQEKERFVGKYFDGTILKGKKSLLVVLSVSAICLVAGSAFYFTRTEKTSGLFTNSLD
ENNNDDYIINSLLKSPNGKKFIVSKLQELISSYDKEKNNQETKNSGELKTFADFDGKNNKSVENFRKNFG
NLKNVKKVYLINFADSKFLMTNLENVNSFYLFIKEHGKKYQTPDEMQQRYLSFVENLAKINAHNNKENVL
YKKGMNRFGDLSFEEFKKKYLTLKSFDFKSNGKKSPRVINYDDVIKKYKPKDATFDHAKYDWRLHNGVTP
VKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDCSFKNNGCYGGLIPNAFEDMIELGGLCSED
DYPYVSDTPELCNIDRCKEKYKIKSYVSIPEDKFKEAIRFLGPISVSIAVSDDFAFYKGGIFDGECGEEP
NHAVILVGYGMEEIYNSDTKKMEKRYYYIIKNSWGESWGEKGFIRIETDENGLMKTCSLGTEAYVPLIE
>gnl|CDD|173322 PTZ00023, PTZ00023, glyceraldehyde-3-phosphate dehydrogenase; Provisional
MVVKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGS
KKVHVFFEKDPAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQY
DKSQRIVSNASCTTNCLAPLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSKGGKDWRAGRCAGVNIIP
ASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTD
DEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGYSNRLLDLAHYITQKY
>gnl|CDD|240233 PTZ00024, PTZ00024, cyclin-dependent protein kinase; Provisional
NMSFSISERYIQKGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKDRQLVGMCGIHFTTLRE
LKIMNEIKHENIMGLVDVYVEGDFINLVMDIMASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYF
MHRDLSPANIFINSKGICKIADFGLARRYGYPPYSDTLSKDETMQRREEMTSKVVTLWYRAPELLMGAEK
YHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFELLGTPNEDNWPQAKKLPLYTEFTPRKPKDLKT
IFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFKSDPLPCDPSQLPFNFLTK
>gnl|CDD|185402 PTZ00026, PTZ00026, 60S ribosomal protein L15; Provisional
MGAYKYLNELWKKKQSDVMRFLLRVRTWEYRQLPVIHRVSRPTRPDKARRLGYKAKQGFVIYRVRVRRGG
RKRPVRKGIVYGKPKTQGVNKLKSTRNLRAVAEERVGKRCGNLRVLNSYWVGQDSTYKFYEVILVDPFHN
AIRNDPRINWICNPVHKHRELRGLTSAGRKSRGLRVKGHRASKLRPSRRANWKRRNRIVLRRYR
>gnl|CDD|240234 PTZ00027, PTZ00027, 60S ribosomal protein L6; Provisional
MKTIFSSEKIRIPEGVTVTVKSRKVTVTGKYGELTRSFRHLPVDIKLSKDGKYIKVEMWFGTPSHLACIR
TVCSHIKNMMTGVTKKFQYKMRLVYAHFPINSNITDNGKTIEIRNFLGEKRVRTVKMLPGVVVEKSESVK
DEIIVTGADLELVSRSAALIHQSTLVRNKDIRKFLDGIYVSEKGTVDKDE
>gnl|CDD|185404 PTZ00028, PTZ00028, 40S ribosomal protein S6e; Provisional
MKLNIANPFTGLQKCIEIDDEKKLLPFFEKRIGAEVPGDSLGDEFKGYIFKISGGNDKQGFPMMQGVLTN
NRVRLLFRKGMKCYRPRRTGEMKRKSVRGCIVGHDLSVLNLVLVKKGPQEIPGLTDGERPRRLGPKRASK
IRKLFNLSKSDDVRKFVVRRKIEGKNKTKAPKIQRLVTPQRLQRKRRYRKTLKKKVLQSREEAKEYQKLL
EEYKNEKR
>gnl|CDD|185405 PTZ00029, PTZ00029, 60S ribosomal protein L10a; Provisional
MSKLSSEALRKAIAEILEGSEEKKRKFVETVELQIGLKDYDTQKDKRFSGSVKLPNVPKPNLKVCVLGDA
VHCDEAKKLGLDFMDIEGLKKFNKNKKLVKKLAKKYDAFLASQSLLPQIPRLLGPGLNKAGKFPTLITHN
DDIEDKINELKSSVKFQLKKVLCLGVAVGNVEMTEEQLRQNIVLSINFLVSLLKKNWQNIKTLHIKSTMG
KPQRIY
>gnl|CDD|185406 PTZ00030, PTZ00030, 60S ribosomal protein L20; Provisional
MKIPRDKVFKLAKGFRGRSKNCFKLARNRVMKALLYSYISRRKRKRILRVHWIQTINAATREHNMTYSRF
INGLNNSNIQLNRKILANLAITEPFSFKALVDESKYQLNERKEKPRDISNL
>gnl|CDD|173329 PTZ00031, PTZ00031, ribosomal protein L2; Provisional
SSMYSPNVKRNIPEYIDFETFFPKKEIKPDLLPTPFTMAKQQRLLKLLENNPLVLYKGRVVKQLSCRRVK
NSGRNNVGRITTRHRGGGHVQRLRFIDFKRSRKDIYSTVLRIEYDPSRSAHIALLQYEDGVLSYILAPLL
LRPGDKIIASKYANINPGNSLPLRNIPVGSIVHNVEMRPGAGGQIIRAGGTYATVVSKDEQFATLKLKST
EIRKFPLDCWATIGQVSNLEHHMRILGKAGVNRWLGKRPVVRGVAMNPSKHPHGGGTSKKGTKRPKCSLW
GICRDGYKTRSKKKPLGLIIRRKICGRLQKKYGVTKA
>gnl|CDD|240235 PTZ00032, PTZ00032, 60S ribosomal protein L18; Provisional
MLLLPIILLYLGVLNSFITNKAVYPPNPLSLFSSPNRKKSAPEQVPTGKNKLLLTKRSKLKGIPKPRKLH
KHGFWAEIFEEKVEREELGNPCKDLDKDIIKGKRRPRLTLKNTNNQMYATIVDDYTRHVLCFSCTNFKYL
SHIFGTYPTKTTNRVRNNGGTIKAAYELGKLIGRKALSKGISKVRFDRAHYKYAGKVEALAEGARAVGLQ
F
>gnl|CDD|140068 PTZ00033, PTZ00033, 60S ribosomal protein L24; Provisional
MRTIACEFSHFAVHPGHGRRYVPFAFLSTKPVLTFLRPKCFALYMRKKNPRFLPWTRTYRRINRKTTTDR
VQRRRAARTVKVQRAIVGADLSYIQEVRAYVQKVDRSAKAKAVRAEKAERKAAKK
>gnl|CDD|173331 PTZ00034, PTZ00034, 40S ribosomal protein S10; Provisional
MVYVPKANRKAIYRYLFKEGVIVCKKDPKGPWHPELNVPNLHVMMLMRSLKSRGLVKEQFAWQHYYYYLT
DEGIEYLRTYLHLPPDVFPATHKKKSVNFERKTEEEGSRGGRGGRGRGRGYGRG
>gnl|CDD|185407 PTZ00035, PTZ00035, Rad51 protein; Provisional
EQESQNEQQEEEEEEEAEGFQEIEKLQSAGINAADIKKLKEAGICTVESVAYATKKDLCNIKGISEAKVE
KIKEAASKLVPMGFISATEYLEARKNIIRITTGSTQLDKLLGGGIETGSITELFGEFRTGKTQLCHTLCV
TCQLPIEQGGGEGKVLYIDTEGTFRPERIVQIAERFGLDPEDVLDNIAYARAYNHEHQMQLLSQAAAKMA
EERFALLIVDSATALFRVDYSGRGELAERQQHLGKFLRALQKLADEFNVAVVITNQVMADVDGASMFVAD
PKKPIGGHIIAHASTTRLSLRKGRGEQRICKIYDSPNLPESEAVFAISEGGIIDAKD
>gnl|CDD|173333 PTZ00036, PTZ00036, glycogen synthase kinase; Provisional
MKDWPIDEDINIYEEKNHKANKGGSGKFEMNDKKLDEEERSHNNNAGEDEDEEKMIDNDINRSPNKSYKL
GNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIMKNLNHINIIFLKDYYYTECFKKNEKNI
FLNVVMEFIPQTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHTL
KLCDFGSAKNLLAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQL
VRIIQVLGTPTEDQLKEMNPNYADIKFPDVKPKDLKKVFPKGTPDDAINFISQFLKYEPLKRLNPIEALA
DPFFDDLRDPCIKLPKYIDKLPDLFNFCDAEIKEMSDACRRKIIPKCTYEAYKEFLMSDENDANIIADKI
SKDFGESNIDAKNNNAKNHA
>gnl|CDD|240236 PTZ00037, PTZ00037, DnaJ_C chaperone protein; Provisional
MFFSGFPFDGMPGGGFDGGRRKREVDNEKLYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPEKFKEI
SRAYEVLSDPEKRKIYDEYGEEGLEGGEQPADASDLFDLIFGGGRKPGGKKRGEDIVSHLKVTLEQIYNG
AMRKLAINKDVICANCEGHGGPKDAFVDCKLCNGQGIRVQIRQMGSMIHQTQSTCNSCNGQGKIIPESKK
CKNCSGKGVKKTRKILEVNIDKGVPNQHKITFHGEADEKPNEIPGNVVFILNEKPHDTFKREGGDLFITK
KISLYEALTGFVFYITHLDGRKLLVNTPPGEVVKPGDIKVINNEGMPTYKSPFKKGNLYVTFEVIFPVDR
KFTNEEKEILKSLFPQNPEEKKDLEDTEIEVVTAQNVDPEEVKDRDQKQQYQEDEDDEHHQEGERVACRQ
Q
>gnl|CDD|240237 PTZ00038, PTZ00038, ferredoxin; Provisional
RSGMKSSFLFLLLTLLGTYSSVSVNYMSADLAFSICSGRRRSSASFISSSASPNRASCYSLGNSKGNTSR
PSSNGVTPGSSPVRSLLSLRRNPLFYNITLQTPDGEKVIECDEDEYILDAAERQGVELPYSCRGGSCSTC
AAKLLEGEVDNEDQSYLDDEQLKKGYCLLCTCYPKSDCTIETHKEDELHDE
>gnl|CDD|173336 PTZ00039, PTZ00039, 40S ribosomal protein S20; Provisional
MKKIKKGGEEEEQNRLHKIRITLTSKNLKSIEKVCADIITGAKEKNLKVTGPVRMPVKTLRITTRKSPCG
EGTNTWDRFEMRIYKRVIDLYSSSDVVTQITSINIDPGVEVEVII
>gnl|CDD|240238 PTZ00040, PTZ00040, translation initiation factor E4; Provisional
MTEGTVVSKYLTFNKSIEDALDLSELFEETKIPLSTPLPLSYKWVIWEQVVKETIRKSNDYKDYTKPLAS
FDSVQKFWQLWFNIPQPSELLTGKRMIRESSDGSEHVVDAVMIFKDGIQPMWEDPMNATGGHFEYRFWPT
DVSPGQIDEYWNNLVLALIGSSLEHSSLINGIRLVDKLSGRFGVIRIEIWFTNLGDQSDRNQLMKEIETC
MARRLDGSSGFPPKFDLKSHSKS
>gnl|CDD|240239 PTZ00041, PTZ00041, 60S ribosomal protein L35a; Provisional
MHQLTKKKKKTNRKKKPVRLYVKAVFLGYKRSKVNQYPNVALLKIEGVNTREDARFYLGKRVAYVYKAKK
LKNGTKFRAIWGKITRPHGNSGVVRARFNKNLPPKAIGSRVRVFLYPSNI
>gnl|CDD|240240 PTZ00043, PTZ00043, cytochrome c oxidase subunit; Provisional
MLKLFGKNFTSLTRTFGRSLGASLLSNRASLLSNKQQKRTYLHFHRTSPEDFELPLDTMPEDIDELMAKD
PKELDFFESYWYWRIRGESTLLDPETLPKKSYKQLARDMGMQIVNEPSEHMLGLLELYEYLKSSSFVGPF
GTIENPVLVPSVGTERVVGCTGGTGEHEHVPLWFRCREGFLYRCGECDQIFMLVRVLYSLPDGEDPFPND
PDVDDVFDLKLIEKGHKMWNKDEYVRWPVGNATYKQLFLQGKWGNMVPEHTRVNSSEV
>gnl|CDD|185411 PTZ00044, PTZ00044, ubiquitin; Provisional
MQILIKTLTGKKQSFNFEPDNTVQQVKMALQEKEGIDVKQIRLIYSGKQMSDDLKLSDYKVVPGSTIHMV
LQLRGG
>gnl|CDD|240241 PTZ00045, PTZ00045, apical membrane antigen 1; Provisional
NKMKYKTQSKTSSRHMRKLYCLSFLSVLCSVHIFNLGLNQNQTRLTSSRTPASLSLIQSNSSLSPIHNPK
RAGLSERNPFGKGEIGGRSNRKQNPWKKFMEKFDIPRVHGSGIYVDLGEDAEVGGKKYREPAGKCPVFGK
AIILENPDNDFLDPVPTGNPYPKEGGFAFPATKVASNSSPTGQLISPISAELLRERYYDNGHCKALNDLA
LCAEYASNFVPANNKNSKYRYPFVYDEKKKLCYILYLSMQENQGPKYCSVDGEEGTLTWACFKPDKSKED
NHLLYGSKNVPDDWESKCPRKPLRNAIFGLWVDGNCVPIPPVFEVEAESLEECAKIVFENSPVASDQPTQ
YEELTDYEKIKEGFKNNNLSMIKSAFLPLGSFDSDNYKSKGVGYNWANYDKESGKCEIFDVVPTCLISDS
GYYALTALSSPNEVDANFPCSIKEKIVLPRIFISTDKDSPFCPATPLKVSNSTCSFYVCERVEKSCGVKE
NNEVVVKEEFKCTYENILEDKKKRILIIIIAATGAVVLVLLAYFSYRYYRKKGNKDKYDKMDEAEDYGKT
YNTDNDEMQDPEASFWGEHKRDASHVTPVLMEKPY
>gnl|CDD|240242 PTZ00046, PTZ00046, rifin; Provisional
MKLHYINILLFALPLNILVYNQKNHPSTTPHTTTTTTTRLLCECELYSSNYDNDPEMKSVMENFDRQTSQ
RFEEYDERMKEKRQKCKEQCDKEIQKIILKDKLEKELMEKFATLQTDIQSDAIPTCVCEKSLADKVEKGC
LRCGCGLGGVAPSWGLIGGIAVNAWKKAALAAAIKAAIKAGAAAGEAAGIAAGKKAVIEGLKSIFGISTL
GGKDLKSIITATNYTNVMSLVDAVYSLYNTSCCGSPANKSSPFCNSVEGKYISPEEVIEKTVETIVSKAA
DAAEAAAEAATAAETAALEAAKTAAVETTTTILQTAIIASIVAIVVIVLIMVIIYLILRYRRKKKMKKKL
QYIKLLEE
>gnl|CDD|240243 PTZ00047, PTZ00047, cytochrome c oxidase subunit II; Provisional
MNLLRSLLGPANISNANEEGEVKLQDVSAEDYPIPQKYLEDPDLIPKYYSFQSNLVTDEDLKPGMLRQLE
VDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFM
PIVVEAVSPEAYAAHAKKYYKD
>gnl|CDD|185414 PTZ00048, PTZ00048, cytochrome c; Provisional
MSRPEPDVTVPEGDAKKGAKLFKAKCAQCHTINKGGAVKQGPNLHGFYGRKSGSADFPYSDANKNSGIVW
SDKHLFEYLVNPKLYIPGTKMVFAGIKKEKERADLIAYLKEASSK
>gnl|CDD|240244 PTZ00049, PTZ00049, cathepsin C-like protein; Provisional
MSRRRNCLSFGLVLLHLLYLNLIGTVADLPTHVEIKNLVGKWKIQRTQTSPKVTTCGSSQPNNNTFNVKI
TDYKKYLLDNHYKFTSELYVILSDDFVLYGDMHDTTGNEHRKNWKVLVVYDEHKRKIGTWTTICDEGFEI
RLGNETYTAFMHYEPTGKCGEAKDDDLTDSNGETDCYTTNYNKIRFGWVDIQNEKDEKLYGCFYAERPKA
ASSTPAAYVVSKEPTDVEPVSQNFIGETLKDSSSLNSHNFLYPASSASSSGSGDKPTFTKRNNMDIDFNS
ELYWHKMKHHGKKKPILKFMQMNSKQRYACPCNKDEHVQDEVNLGDSDQPVSPVSPVSLMQLGNTNFLAH
VHGSDATNEMDLENYEDTEKAPHRELEIDELPKNFTWGDPFNNNTREYDVTNQLLCGSCYIASQMYAFKR
RIEIALTKNLDKKYLNNFDDLLSIQTVLSCSFYDQGCNGGFPYLVSKMAKLQGIPLDKVFPYTATEQTCP
YQVDQSANSMNGSANLRQINAVFFSSETQSDMHADFEAPISSEPARWYAKDYNYIGGCYGCNQCNGEKIM
MNEIYRNGPIVASFEASPDFYDYADGVYYVEDFPHARRCTVDLPKHNGVYNITGWEKVNHAIVLVGWGEE
EINGKLYKYWIGRNSWGKNWGKEGYFKIIRGKNFSGIESQSLFIEPDFSRGAGKILLEKLENE
>gnl|CDD|240245 PTZ00050, PTZ00050, 3-oxoacyl-acyl carrier protein synthase; Provisional
VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLVAAMPCQIAAEVDQSEFDPSDFAP
TKRESRATHFAMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIP
KILGNMAAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRM
RALCTKYNDDPQRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHP
DGRGARRCMENALKDGANININDVDYVNAHATSTPIGDKIELKAIKKVFGDSGAPKLYVSSTKGGLGHLL
GAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHPLQSIDAVLSTSFGFGGVNTALLFTK
Y
>gnl|CDD|173347 PTZ00051, PTZ00051, thioredoxin; Provisional
MVHIVTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENIT
SMPTFKVFKNGSVVDTLLGANDEALKQL
>gnl|CDD|185416 PTZ00052, PTZ00052, thioredoxin reductase; Provisional
HLTFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIG
SIFHHDSQMYGWKTSSSFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDNSQE
ETITAKYILIATGGRPSIPEDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTV
AVRSIPLRGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIKVLFSDGTTELFDTVLYATGRKPDI
KGLNLNAIGVHVNKSNKIIAPNDCTNIPNIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTF
IPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTLEIAAVHREKHERARKDEYDFDVSSNCLAKL
VCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVFMNLSVTRRSGESFAAK
GGCGGGKCG
>gnl|CDD|240246 PTZ00053, PTZ00053, methionine aminopeptidase 2; Provisional
AMNENGENEVKQQKQQNKQKGTKKKNKKSKKDVDDDDAFLAELISENQEAENKQNNKKKKKKKKKKKKKN
LGEAYDLAYDLPVVWSSAAFQDNSHIRKLGNWPEQEWKQTQPPTIPVSKQFKDGEYPVGEIQEYPGENSS
RTSSEEKRELEKLSEEQYQDLRRAAEVHRQVRRYAQSVIKPGVKLIDICERIESKSRELIEADGLKCGWA
FPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFTVAFNPKYDPLLQATKDATNTGI
KEAGIDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGENTRMEEG
ELFAIETFASTGRGYVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRH
LLALKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGDDY
>gnl|CDD|185418 PTZ00054, PTZ00054, 60S ribosomal protein L23; Provisional
MKRGRGGVGGNKFRVTLGLPVGAVVNCADNSGAKNLYIIAVKGIHGRLNRLPSASLGDMVLATVKKGKPE
LRKKVLNAVIIRQRKAWRRKDGVFIYFEDNAGVIVNPKGEMKGSAITGPVAKECADLWPKISSAAPAIV
>gnl|CDD|240247 PTZ00055, PTZ00055, glutathione synthetase; Provisional
LEHRVNVFYDVINREILNFFTCKNDENEDKIKDAIRYLSYKRIMILKQDLIDYLNEDSFYIFTKAKQLEA
NDGILKMVSFVLFPLPFPRKLLEDCCLCTLLLVELFDNMSCDLELLLDVFEQLKKYDKFVRDLLEICNEV
YGSGERNIKDDIRCYIGRSDYFIHIDNLTKNKTQGENEFCKTCYYDHCLCNISANNQSLEFKLVEYNTIS
VAFGNLSGLLFRAHKKLLRTVYRECFDLEGKGAERPMVGSILLEKFKNHFYNGIVTCFKKCHRMYLDEYK
PLFGKNKVCVMSIVHEDLFNFFDKYKTANELFDKYGIHVKTLTINELILLYEKKKLFLNYPWETLEDGLV
RVKKYQDDLHKLHPGRLLIDLNSQENGLNRLYKRDCFEVSVVYFRSLYSPDHMESDERIWLVREFLEFSD
AVKIPSLPAQLVGSKRIQMYLLDPSILKRLVSLYNKRKKSDKQINHDMKLLKKTFALQVDPSLESNEHIV
QDAIQNPSNYLLKPQREGGKNNLHGNEISEKLRLGYKNNKEKLSQYVLMQKIFPPSQPAVFVRNLKSGSF
EFSPENSLTELGLYHNFIFDGNECILNEQKGYLARTKNEFETGGGAISGISSVNSLLLY
>gnl|CDD|240248 PTZ00056, PTZ00056, glutathione peroxidase; Provisional
MFSFFKKITVSKDELRKSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNP
LGLEILAFPTSQFLNQEFPNTKDIRKFNDKNKIKYNFFEPIEVNGENTHELFKFLKANCDSMHDENGTLK
AIGWNFGKFLVNKSGNVVAYFSPRTEPLELEKKIAELLGVKDYQELFKNYDKLHPESIE
>gnl|CDD|173353 PTZ00057, PTZ00057, glutathione s-transferase; Provisional
MAEEIVLYYFDARGKAELIRLIFAYLGIEYTDKRFGENGDAFIEFKNFKKEKDTPFEQVPILEMDNIIFA
QSQAIVRYLSKKYKICGESELNEFYADMIFCGVQDIHYKFNNTNLFKQNETTFLNEELPKWSGYFENILK
KNHCNYFVGDNLTYADLAVFNLYDDIETKYPNSLKNFPLLKAHNEFISNLPNIKNYISNRKESVY
>gnl|CDD|185420 PTZ00058, PTZ00058, glutathione reductase; Provisional
MRQLSYFHFLLFFALLNPSIKLIRSFSFYHNLEASSAPTHLKKKPRMVYDLIVIGGGSGGMAAARRAARN
KAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFSFNLPLLVERRDKYIRRLNDI
YRQNLKKDNVEYFEGKGSLLSENQVLIKKVSQVDGEADESDDDEVTIVSAGVSQLDDGQVIEGKNILIAV
GNKPIFPDVKGKEFTISSDDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETI
INELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALNIKT
PKGYIKVDDNQRTSVKHIYAVGDCCMVKKNQEIEDLNLLKLYNEEPYLKKKENTSGESYYNVQLTPVAIN
AGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVYDMDP
AQKEKTYLKLVCVGKEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTMAPWM
K
>gnl|CDD|185421 PTZ00059, PTZ00059, dynein light chain; Provisional
MMSDRKAVVKNADMSEDMQQDAIDCANQALEKFNIEKDIAAYIKKEFDKKYNPTWHCIVGRNFGSYVTHE
TKHFIYFYLGQVAILLFKSG
>gnl|CDD|240249 PTZ00060, PTZ00060, cyclophilin; Provisional
FFKLFSQSFPEMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVGSSGKNLHYKGSI
FHRIIPQFMCQGGDITNHNGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWL
DGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPVVVTDCGELQ
>gnl|CDD|173356 PTZ00061, PTZ00061, DNA-directed RNA polymerase; Provisional
MDDSETRFFRCRRTCCEMLEDRGYIITSQEKLETFATFKERFEENERLRSRMLMVASHKTDPTNRIIVYF
ADETKKTGVKPIRELTEKMEEHDIQRAILVTQNVLTPFAKDAILEAAPRHIIENFLETELLVNITKHELV
PKHIPLTDDEKLNLLQRYKVKESQLPRIQSADPVARYFGLSKGQVVKIIRPSETAGRYVTYRLVV
>gnl|CDD|240250 PTZ00062, PTZ00062, glutaredoxin; Provisional
MNFIKKEEKDKLIESNTGKLVLYVKSSKEPEYEQLMDVCNALVEDFPSLEFYVVNLADANNEYGVFEFYQ
NSQLINSLEGCNTSTLVSFIRGWAQKGSSEDTVEKIERLIRNHKILLFMKGSKTFPFCRFSNAVVNMLNS
SGVKYETYNIFEDPDLREELKVYSNWPTYPQLYVNGELIGGHDIIKELYESNSLRKVIPDDCFE
>gnl|CDD|240251 PTZ00063, PTZ00063, histone deacetylase; Provisional
SMRKRVSYFYDPDIGSYYYGPGHPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDF
LSSISPENYRDFTYQLKRFNVGEATDCPVFDGLFEFQQSCAGASIDGAYKLNNHQADICVNWSGGLHHAK
RSEASGFCYINDIVLGILELLKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFGDFFPGTGDVTD
IGVAQGKYYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAA
CVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNKHDEMSDQISLNDYYDYYAPDFQLHLQPSNIP
NYNSPEHLEKIKVKILENLRYLEHAPGVQFAYVPPDFFDRDIDDEDEKNQYELSDEGGGRAAGSTAKRHS
TNSHRLRRKDYADDFY
>gnl|CDD|173359 PTZ00064, PTZ00064, histone acetyltransferase; Provisional
MVNMALRSRSSNFQKQQANNTPSNTSNNNEAVSSELISSENQRKKTNARIYSSIEEHSDKTLDECKEDEA
VNTIEKGPTADFPSVNQWVLALFEEEGKQMLARVVGWKLYGTQVTHLSHLVNKKTSGNKQNSLIKVSSSS
NESQIKEDYEFYVHFRGLNRRLDRWVKGKDIKLSFDVEELNDPNLIERFQKQGIKFISSLSVSNSANKSG
NKSKKRNVGVLDISDGEDPDEHEGMDHSAILDHEETTRLRTIGRVRIGKFILDTWYFSPLPDEYQNVDTL
HFCEYCLDFFCFEDELIRHLSRCQLRHPPGNEIYRKDNISVFEIDGALTRGYAENLCYLAKLFLDHKTLQ
YDVEPFLFYIVTEVDEEGCHIVGYFSKEKVSLLHYNLACILTLPCYQRKGYGKLLVDLSYKLSLKEGKWG
HPERPLSDLGRAIYNNWWAHRISEYLLEYFKQNKICERGGSKQPLQVSNYWKFIDNVVRSTGIRREDVIR
ILEENGIMRNIKDQHYIFCNQEFLKGIVKRSGRPGITLIDKYFNWVPFSRAPPSEVESLPQE
>gnl|CDD|240252 PTZ00065, PTZ00065, 60S ribosomal protein L14; Provisional
MPLFKRFVEPGRLCLIQYGPDAGKLCFIVDIVTPTRVLVDGAFITGVKRQSIPLKRLKLTDEKIKINRGA
RTGTLKKALKKDNALEEFNKTSLGKKLIIKEKRANMTDFERFKLMVAKKERRKLMKSLKK
>gnl|CDD|173361 PTZ00066, PTZ00066, pyruvate kinase; Provisional
MSRLASTSSVMGCSLGKATNISLDKILEPISDNDLRQKKTHIVCTMGPACKNVETLVKLIDAGMNICRFN
FSHGDHESHKKTLNNVREAAKARPNANLGILLDTKGPEIRTGFLKNHKPITLKEGQTLKITTDYTFLGDE
TCISCSYKKLPQSVKVGNIILIADGSLSCKVLEVHDDYIITKVLNNATIGERKNMNLPGVKVELPVIGEK
DKNDILNFAIPMGCDFIALSFVQSADDVRLCRQLLGERGRHIKIIPKIENIEGLINFDEILAESDGIMVA
RGDLGMEIPPEKVFLAQKMMISKCNVAGKPVITATQMLESMIKNPRPTRAESTDVANAVLDGTDCVMLSG
ETANGKFPVEAVNIMAKICFEAETCIDYRVLYHAIHLAVPTPVSVQEAVARSAVETAEDINAKLIIALTE
TGNTARLISKYRPSCTILALSASPSVVKSLSVARGVTTYVVNSFQGTDVVIRNAIALAKERGLVESGDSA
IAVHGVKEEVAGSSNLMKVVKIP
>gnl|CDD|185422 PTZ00067, PTZ00067, 40S ribosomal S23; Provisional
MGKPRGLRAARKLRRHRRVNRWADKEYKKAHLGTRYKANPFGGASHAKGIVVEKIGIEAKQPNSAIRKCV
RVQLIKNGKKITAFVPNDGCLNFINENDEVLVSGFGRSGHAVGDIPGVRFKVVKVAGVSLLALYKGKKEK
PRN
>gnl|CDD|240253 PTZ00068, PTZ00068, 60S ribosomal protein L13a; Provisional
MFKKVIVIDCKGHLLGRLASVVAKELLLGQKIVVVRCEDLNISGSLFRNKVKYEEFLRKRMNTNPRRGPF
HHRAPSDIFWRTVRGMLPHKTKRGAAALKRLKVFEGVPAPYDKVKRVVIPSALRVLRLKPERPYTVLGDL
SAHVGWKYADVVAKLEEKRKERAAAYYKKKVKLRKAWKEARKKALAKLPKAIVAVLKKFGYA
>gnl|CDD|240254 PTZ00069, PTZ00069, 60S ribosomal protein L5; Provisional
MAFVKVVKNKAYFKRFQVKYRRRREGKTDYYARRRLILQDKNKYNSPKYRLVVRITNKDIICQIVYATIV
GDKVLAAAYSHELPRFGIPVGLTNYAAAYATGLLLARRLLKKLGLDKQFEGVKEADGEYYHVDEEDDEER
RPFKAILDVGLARTTTGNRVFGALKGAVDGGLHIPHSPNRFPGYSKEKDSYDAEVHRDRIFGKHVAEYMK
QLKEEDPDKYKKQFSKYIKAGVGPDSLEDMYKKAHAAIRANPSKVKKKKKKKKKVVHKKYKTKKLTGKQR
KARVKAKKAQRRERLQKKIK
>gnl|CDD|240255 PTZ00070, PTZ00070, 40S ribosomal protein S2; Provisional
AAAARGGEGRGFGRRGRGGRGRGRGRGRGGEGEEKEWVPVTKLGRLVKAGKITSLEEIFLFSIPIKEYQI
VDHFFAESKLKDEVMKIMPVQKQTSAGQRTRFKAFVVVGDGNGHIGLGAKVAKEVATAIRGAIIAAKLNL
VPVRRGYWGNKIGEPHTVPMKVTGKCGSVRVRLVPAPRGTGIVAAPTPKKILEFAGVEDVFTSSRGKTRT
RGNFLKATFYALRKTYGFLTPDLWKETELSRSPYDEHSEFLAEKKKM
>gnl|CDD|240256 PTZ00071, PTZ00071, 40S ribosomal protein S24; Provisional
KKKAEFTVRTRKFLVNPLLNRKQFVVEVLHPGKGTVSKKDIKEKLAKQYKVADARTIVLFGFKTKFGGGK
TTGFGLIYDNLAALKKFEPKYRLIRLGLIKKKKAGRKARKELKNRRKKVRGKEKTKVSGKKK
>gnl|CDD|185427 PTZ00072, PTZ00072, 40S ribosomal protein S13; Provisional
MYGKGKGISSSALPYRRKPPSWLKLSSSEVEDQICKLAKKGLTPSQIGVILRDSMGIPQVKNVTGSKILR
ILKKNGLAPEIPEDLYFLIKKAVSIRKHLEKNRKDKDSKFRLILVESRIHRLARYYKRTKQLPPNWKYES
STASALVA
>gnl|CDD|240257 PTZ00073, PTZ00073, 60S ribosomal protein L37; Provisional
MTKGTGSFGKRHGKTHTLCRRCGKRSFHVQKKRCASCGYPSAKMRRYNWSVKAKRRRTTGTGRCRYLKTV
ARRAKNGFREGTKAKPKVKAA
>gnl|CDD|185429 PTZ00074, PTZ00074, 60S ribosomal protein L34; Provisional
MAQRVTYRRRNSYNTRSNKVRLVKTPGGRLVVQKRKKKSSGPKCGDCGKVLAGIKALRPTEYKQLSRRER
TVSRAYGGVLCHKCVRDRIVRAFLVEEQKIVKQVLKEKAKQKKQKKKKKKKKKKKTSKKAAKKKK
>gnl|CDD|240258 PTZ00075, PTZ00075, Adenosylhomocysteinase; Provisional
PMTDYKVKDISLAEFGRKEIELAENEMPGLMALREEYGPSKPLKGARITGCLHMTVQTAVLIETLKALGA
EVRWCSCNIFSTQDHAAAAIAKAGSVPVFAWKGETLEEYWWCTEQALKWPNGDGPNLIVDDGGDATLLVH
EGVKAEKLYEEKGILPDPLDPSNEDEKCLLTVLKKLLTKNPDKWTNLVKKIVGVSEETTTGVHRLYKMLK
KGELLFPAINVNDSVTKSKFDNIYGCRHSLIDGIFRATDVMIAGKTVVVCGYGDVGKGCAQALRGFGARV
VVTEIDPICALQAAMEGYQVVTLEDVVETADIFVTATGNKDIITLEHMRRMKNNAIVGNIGHFDNEIQVA
ELEAYPGIEIVEIKPQVDRYTFPDGKGIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELWENRDT
GKYPNGVYKLPKELDEKVARLHLKKLGAKLTKLTDKQAEYIGVPVDGPYKSDHYRY
>gnl|CDD|173371 PTZ00076, PTZ00076, 60S ribosomal protein L17; Provisional
MGYSSTLKFVNLGVRRRLFRRAHGQPHHRWDSIKNQLDELLRYGRLELTLPRAKELQQYAEELIYLAKKD
TPESNLKVESMLRTPQGRRKLYEKYVPLYRDRPFFFTRVVNQWRLRLRDAAPMAYIEFVDRPGEIRPAKP
VGFDKIKYIYEEMKKTRRNFRKYFNIAKKFGLLDENGNLISDISALEKPWYEEWEEEDEEEIQIDPELIR
RYLQFIEPMLAGPKKGREPFYVDLPPPTETERAFLNYRKKFKP
>gnl|CDD|185431 PTZ00077, PTZ00077, asparagine synthetase-like protein; Provisional
MCGILAIFNSKGERHELRRKALELSKRLRHRGPDWSGIIVLENSPGTYNILAHERLAIVDLSDGKQPLLD
DDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPKDFWNHLDGMFATVIYDMKTNT
FFAARDHIGIIPLYIGYAKDGSIWFSSELKALHDQCVEVKQFPPGHYYDQTKEKGEFVRYYNPNWHDFDH
PIPTGEIDLEEIREALEAAVRKRLMGDVPFGLFLSGGLDSSIVAAIVAKLIKNGEIDLSKRGMPKLHSFC
IGLEGSPDLKAARKVAEYLGTEHHEFTFTVEEGIDALPDVIYHTETYDVTTIRASTPMYLLSRRIKALGI
KMVLSGEGSDELFGGYLYFHKAPNREEFHRELVRKLHDLHKYDCLRANKATMAWGIEARVPFLDKDFLEY
VMNIDPKYKMCNAFEGQMEKYILRKAFEGLEKPYLPDEILWRQKEQFSDGVGYSWIDGLKEYAEKKISDQ
EFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTVPYGPSIACSTEKALEWDESFKKNTDESGRAV
LSVHNDAKQDSDVKEEDKSTDESIKV
>gnl|CDD|185432 PTZ00078, PTZ00078, Superoxide dismutase [Fe]; Provisional
PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLENKTLEELIKEYSGAVFNNAAQIWNHN
FYWLSMGPNGGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNP
IKDNTGKPLLTCDIWEHAYYIDYRNDRASYVNSWWNKVNWDFANKNLKKLMQK
>gnl|CDD|185433 PTZ00079, PTZ00079, NADP-specific glutamate dehydrogenase; Provisional
KSGYNSELSVAQEMDALRKRVKSRDPNQPEFLQAFHEVMTSLKPLFQKNPKYLGVLERLVEPERVIQFRV
PWVDDKGEQRVNRGFRVQYNSALGPYKGGLRFHPSVNLSILKFLGFEQIFKNSLTTLPMGGGKGGSDFDP
KGKSDNEVMRFCQSFMTELYRHIGPDTDVPAGDIGVGGREIGYLFGQYKKLRNNFEGTLTGKNVKWGGSN
IRPEATGYGLVYFVLEVLKKLNDSLEGKTVVVSGSGNVAQYAVEKLLQLGAKVLTMSDSDGYIHEPNGFT
KEKLAYLMDLKNVKRGRLKEYAKHSSTAKYVPGKKPWEVPCDIAFPCATQNEINLEDAKLLIKNGCKLVA
EGANMPTTIEATHLFKKNGVIFCPGKAANAGGVAISGLEMSQNAARLQWTAEEVDEKLREIMKSIFEACV
KYAEKYGGKSDLVAGANIAGFLKVADSMIEQGCV
>gnl|CDD|240259 PTZ00081, PTZ00081, enolase; Provisional
MSTIKSIKAREILDSRGNPTVEVDLTTEKGVFRAAVPSGASTGIYEALELRDGDKSRYLGKGVLKAVENV
NEIIAPALIGKDVTDQKKLDKLMVEQLDGTKNEWGWCKSKLGANAILAVSMAVARAAAAAKGVPLYKYLA
QLAGKPTDKFVLPVPCFNVINGGKHAGNKLAFQEFMIAPVGAPSFKEALRMGAEVYHSLKSVIKKKYGLD
ATNVGDEGGFAPNIKDPEEALDLLVEAIKKAGYEGKVKICMDVAASEFYDKEKKVYDLDFKNPNNDKSNK
LTGEELVELYLDLVKKYPIVSIEDPFDQDDWEAYAKLTAAIGQKVQIVGDDLLVTNPTRIKKAIEKKACN
ALLLKVNQIGTVTEAIEAAKLAQKNGWGVMVSHRSGETEDTFIADLVVGLGTGQIKTGAPCRSERLAKYN
QLLRIEEELGSNAVYAGEN
>gnl|CDD|173376 PTZ00082, PTZ00082, L-lactate dehydrogenase; Provisional
MTMIKRRKISLIGSGNIGGVMAYLIVLKNLGDVVLFDIVKNIPQGKALDISHSNVIAGSNSKVIGTNNYE
DIAGSDVVIVTAGLTKRPGKSDKEWNRDDLLPLNAKIMDEVAEGIKKYCPNAFVIVITNPLDVMVKLLQE
HSGLPKNKVCGMAGVLDSSRLRTYIAEKLGVNPRDVHASVIGAHGDKMVPLPRYVTVGGIPLSEFIKKGL
ITQEEIDEIVERTRNTGKEIVDLLGTGSAYFAPAAAAIEMAEAYLKDKKRVLPCSAYLEGQYGHKDIYMG
TPAVIGANGVEKIIELDLTPEEQKKFDESIKEVKRLEALLK
>gnl|CDD|185434 PTZ00083, PTZ00083, 40S ribosomal protein S27; Provisional
MGFMDVDLLYPDPESEARKHKLKRLVQGPNSYFMDVKCPGCSQITTVFSHAQTVVLCGGCSSQLCQPTGG
KAKLTEGCSFRRKKD
>gnl|CDD|240260 PTZ00084, PTZ00084, 40S ribosomal protein S3; Provisional
SMGQISKKRKFVADGVFYAELNEFLSRELAEDGYSGVEVRVTPIRTEIIIRATRTREVLGDKGRRIRELT
SLLQKRFGFPEGKVELFAERVENRGLCAMAQAESLRYKLLEGLPVRRAAYGVLRHVMESGAKGCEVIVSG
KLRAQRAKSMKFRDGYMISTGQPKKDFVDSAVRHVLMRQGVIGVKVKIMLPYDPSGKNGPSAPLPDVITV
LEPKEETAEE
>gnl|CDD|240261 PTZ00085, PTZ00085, 40S ribosomal protein S28; Provisional
EVVTQDTEQPKLAKVIKVLGRTGSRGGVTQVRVQLMGEEGDAGRTLIRNVKGPVREGDILSLMETEREAR
RLR
>gnl|CDD|185437 PTZ00086, PTZ00086, 40S ribosomal protein S16; Provisional
MAEKTTKLKQVQTFGKKKTAVAVALVTKGKGLIRVNGVPLDLINPETLRAKVFEPLLLVGKERFSRLDIR
VRVRGGGQVAQAYAIRQAIAKGLVAYYQKYVDEATKAELKDKLLAYDRSLLVADPRRCEPKKFGGPGARA
RFQKSYR
>gnl|CDD|185438 PTZ00087, PTZ00087, thrombosponding-related protein; Provisional
MRSFTFLAVLLITICYQCISNLFKRQNTNYFLQLLQKNGNYKIVTLEPECTVGKGLQLGQAKQESDVNRK
EFLLHNYVVIKNSQFTNEKTLELYSSKEENNKSHLVLTFYIGDFNFSVGHNSPYEVNLILSVMAGNKKST
CKNNNYNIVLLKSADVFNPSELEILSEPIKFSISKTSGSFRININNFFLDGTWRAFVKDRLTFLLKPEDN
CYTVLENKLNKPSLIIEKKNMFYTEWGEWSNCSMECDHPDNVQIRERKCAHPSGDCFKGDLKETRPCQVP
LPPCNSLFEHKESSTFKILIILLPIVLIICVMGILYHIFYKKKGAEKELYENVAGRFMYD
>gnl|CDD|240262 PTZ00088, PTZ00088, adenylate kinase 1; Provisional
MKLKGPLKIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTIGKEIQKVVTSGNLVPDNLV
IAIVKDEIAKVTDDCFKGFILDGFPRNLKQCKELGKITNIDLFVNIYLPRNILIKKLLGRRICNTCNRNF
NIAHIRSDPYDMPPILPPADCEGCKGNPKLQKRSDDTEEIVAHRLNTYESTNSPIIQFFKNENCNLVDFE
ITRGLRDFDDFYRIVLQRL
>gnl|CDD|173383 PTZ00089, PTZ00089, transketolase; Provisional
MDGAIDEKCANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHAS
ALLYSMLHLTGYDLSMEDLKNFRQLGSRTPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKFN
RPGHPIFDNYVYVICGDGCLQEGVSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAY
GWHVIEVDNGNTDFDGLRKAIEEAKKSKGKPKLIIVKTTIGYGSSKAGTEKVHGAPLGDEDIAQVKELFG
LDPEKKFHVSEEVRQFFEQHVEKKKENYEAWKKRFAKYTAAFPKEAQAIERRFKGELPPGWEKKLPKYTT
NDKAIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFTKASPEGRYIRFGVREHAMCAIMN
GIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRATPNLL
VIRPADGTETSGAYALALANAKTPTILCLSRQNTPPLPGSSIEGVLKGAYIVVDFTNSPQLILVASGSEV
SLCVEAAKALSKELNVRVVSMPCWELFDQQSEEYQQSVLPSGGVPVLSVEAYVSFGWEKYSHVHVGISGF
GASAPANALYKHFGFTVENVVEKARALAARF
>gnl|CDD|173384 PTZ00090, PTZ00090, 40S ribosomal protein S11; Provisional
MYKCSLGRKGNRLFTYKNLILTRGIVNSSDFSNLRRSLFSGGISPSSSFTTLSCVAVKAITNLKEEVKKP
PKKKKNITKEELKNFQGHKRRYKLFGGRPEFHNIDRDKNGLIIEPTDRFMLVITTSKNNVHAQVVNKSKN
YKTVFGSFAGNVGFRKKLQQSERCAYRIGENIAKKCRRLGIFAVDIKFRRIMRVETVLQAFYANGLQVTQ
IIHEPRLPKCGLNAVKPRKRRRV
>gnl|CDD|185439 PTZ00091, PTZ00091, 40S ribosomal protein S5; Provisional
MSANEPKLFGKWSYDDVQVSDLSLKDYIAVTTKASVFVPHTAGRYQKKRFRKAQCPIVERLVNSLMFHGR
NNGKKLLAVRIVKHAFEIIHLLTDKNPLQVLVDAVQNGGPREDSTRVGSGGVVRRQAVDVSPLRRVNQAI
YLICKGAREAAFRNIKTIAECLADEIINASKESSNSYAIKKKDEVERVAKANR
>gnl|CDD|240263 PTZ00092, PTZ00092, aconitate hydratase-like protein; Provisional
RLRQQLRMSSSRPNPFEKVLKTLKDGGSYKYYSLNELHDPRLKKLPYSIRVLLESAVRNCDEFDVTSKDV
ENILNWEENSKKQIEIPFKPARVLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQV
DFSRSPDALELNQEIEFERNLERFEFLKWGSKAFKNLLIVPPGSGIVHQVNLEYLARVVFNKDGLLYPDS
VVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRK
RGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQTGRSEEKVELIEKYLKAN
GLFRTYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPVGFKGFGIPEEKHEKKV
KFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVTKYLE
ASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLAS
PPLVVAYALAGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQW
NELQVPKGKLYEWDEKSTYIHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAA
KYLMERGVERKDFNTYGARRGNDEVMVRGTFANIRLINKLCGKVGPNTVHVPTGEKMSIYDAAEKYKQEG
VPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNGENADSLGLTGKE
QFSIDLNSGELKPGQDVTVKTDTGKTFDTILRIDTEVEVEYFKHGGILQYVLRKLVKG
>gnl|CDD|173387 PTZ00093, PTZ00093, nucleoside diphosphate kinase, cytosolic; Provisional
SSERTFIMVKPDGVQRGLVGEIIKRFEKKGYKLVALKMLQPTPEIAEEHYKEHKGKPFFPGLVKYISSGP
VVCMVWEGKNVVKQGRKLLGATNPLESAPGTIRGDFCVDVGRNVIHGSDSVESAKREIALWFKPEELVSW
TSHSSKWIY
>gnl|CDD|240264 PTZ00094, PTZ00094, serine hydroxymethyltransferase; Provisional
TERSRNLVLPLNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNR
YYGGNEVVDKIENLCQKRALEAFGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTH
GFYTAKKKVSATSIYFESLPYQVNEKGLIDYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVG
AYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSGLIFYRKKVKPDIENKINEAVFPGLQGG
PHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVTGGTDNHLVLVDLRPFGITGSKM
EKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVKLAQEIQKQVGKKL
VDFKKALEKNPELQKLRQEVVEFASQFPFPGI
>gnl|CDD|140127 PTZ00095, PTZ00095, 40S ribosomal protein S19; Provisional
METSMDKIKNKIKRIGKPVPYRRKNATLKDVSPWRFIKAFAQHFKLEGKIFVPKCTEIVKTSHGRELAPQ
NPDWYYIRCAAVLRALYLRPDVGYGGLRKRFSSKKRRGSAPNHTVRASGKILRWICQQLEKLGLVEQGPK
KKGRRLTRKGCNFANAFARQVTIRKFGKE
>gnl|CDD|185442 PTZ00096, PTZ00096, 40S ribosomal protein S15; Provisional
EMYEQLKKKRTFKKFTYRGVELEKLLALPEEELVELFRARQRRRINRGIKRKHPTLLKKLRKAKKATKPG
EKPKAVKTHLRDMIIVPEMVGSVVGVYNGKQFNNVEIKPEMIGHYLGEFSITYKPVRHGKPGVGATHSSR
FIP
>gnl|CDD|185443 PTZ00097, PTZ00097, 60S ribosomal protein L19; Provisional
NLRLQKRLAASVLKCGKNRVWLDPNEASEISLANSRFSIRKLIKDGLIIRKPVAVHSRARARRFHEAKRK
GRHTGIGKRRGTREARMPTKVLWMRRQRVLRRLLRKYRAAKKIDRHMYHEFYLKSKGNQFKNKRVLIEAI
HKTKNEKVKEKKIQDQLEARRAKAKALRNKRKAKK
>gnl|CDD|173391 PTZ00098, PTZ00098, phosphoethanolamine N-methyltransferase; Provisional
MESENVDITYLENNQYSDEGIKAYEFIFGEDYISSGGIEATTKILSDIELNENSKVLDIGSGLGGGCKYI
NEKYGAHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILKKDFPENTFDMIYSRDAILHLSYADKKKLFE
KCYKWLKPNGILLITDYCADKIENWDEEFKAYIKKRKYTLIPIQEYGDLIKSCNFQNVVAKDISDYWLEL
LQVELKKLEEKKEEFLKLYSEKEYNSLKDGWTRKIKDTKRKLQKWGYFKAQKM
>gnl|CDD|185444 PTZ00099, PTZ00099, rab6; Provisional
MYDTFDNNYQSTIGIDFLSKTLYLDEGPVRLQLWDTAGQERFRSLIPSYIRDSAAAIVVYDITNRQSFEN
TTKWIQDILNERGKDVIIALVGNKTDLGDLRKVTYEEGMQKAQEYNTMFHETSAKAGHNIKVLFKKIAAK
LPNLDNSNSNDANVVDIQLTNNSNANDKNMLSKCMC
>gnl|CDD|240265 PTZ00100, PTZ00100, DnaJ chaperone protein; Provisional
MMWPIVALTFGGGVLAVRYGYRYLKNQKIFGSNNMSFPLSGFNPSLGSLFLKNDLKGFENPMSKSEAYKI
LNISPTASKERIREAHKQLMLRNHPDNGGSTYIASKVNEAKDLLLK
>gnl|CDD|185445 PTZ00101, PTZ00101, rhomboid-1 protease; Provisional
MSNIHTLAEYRDDYGENTPFNRAEKYYQSQSSFIQRSKPIDVLNLIFPHFTWKSFIMAISIIQIIVFIIS
VSIKPADFLTPSDSLLVTLGANVASRIKQGEIHRLILPIFLHANIFHTFFNVFFQLRMGFTLEKNYGIVK
IIILYFLTGIYGNILSSSVTYCPIKVGASTSGMGLLGIVTSELILLWHVIRHRERVVFNIIFFSLISFFY
YFTFNGSNIDHVGHLGGLLSGISMGILYNSQMENKPSWYDHMKMASYACLALLAIVPPIVLFAVPRTC
>gnl|CDD|240266 PTZ00102, PTZ00102, disulphide isomerase; Provisional
IGFRSILSSLFLLLILLAFAVFGSAEEHFISEHVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPE
YKKAAKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFNKGNPVNYSGGRTADGIVSWIKKLTGP
AVTEVESASEIKLIAKKIFVAFYGEYTSKDSELYKKFEEVADKHREHAKFFVKKHEGKNKIYVLHKDEEG
VELFMGKTKEELEEFVSTESFPLFAEINAENYRRYISSGKDLVWFCGTTEDYDKYKSVVRKVARKLREKY
AFVWLDTEQFGSHAKEHLLIEEFPGLAYQSPAGRYLLPPAKESFDSVEALIEFFKDVEAGKVEKSIKSEP
IPEEQDGPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDNDSIIVAKMNGTAN
ETPLEEFSWSAFPTILFVKAGERTPIPYEGERTVEGFKEFVNKHATNPFEDDTHEEL
>gnl|CDD|240267 PTZ00103, PTZ00103, 60S ribosomal protein L3; Provisional
MSHRKFEHPRHGSLGFLPRKRCRRHRGRIRSFPKDDPTQPPHLTAFMGYKAGMTHIVRDVDRPGSKLHKK
EVVEAVTIIEAPPMVVVGIVGYRETPRGLRALTTVWAHHLSDEFRRRFYKNWYKSKKKAFTKYKKFAATK
KAEERTLKRIKKYCSVIRVIAHTQPSKLPLGQKKAHVMEIQVNGGSVAEKVDFAKSLLEKEVPVDSVFQQ
NEMIDVIGVTKGHGFEGVVKRWGVTRLPRKTHRGLRKVACIGAWHPARVQYTVPRAGQHGYHHRTELNKK
IYRIGVAEDPNNATTEADLTEKTITPMGGFPHYGTVRNDFLMLKGCVVGPKKRVITLRKSLVPQTSRKAL
EKITLKFIDTSSKIGHGRFQTKEEKAKFYGPLKKDRIRRE
>gnl|CDD|240268 PTZ00104, PTZ00104, S-adenosylmethionine synthase; Provisional
PTFLKMSVGHFLFTSESVSEGHPDKLCDQISDAVLDACLAQDPLSKVACETCAKTGMVMVFGEITTKAVV
DYQKVVRDTVKEIGYDDTEKGLDYKTCNVLVAIEQQSPDIAQGVHVGKKEEDIGAGDQGIMFGYATDETE
ELMPLTHELATKLAKRLSELRKNGILPWLRPDAKTQVTVEYEYDTRGGLTPKRVHTILISTQHDEGVSNE
EIREDLMEHVIKPVIPAKLLDEETKYHLNPSGRFVIGGPHGDAGLTGRKIIVDTYGGWGAHGGGAFSGKD
PSKVDRSAAYAARWIAKSLVAAGLCKRCLVQVSYAIGVAEPLSIHVNTYGTGKKGYDDEDLLEIVQKNFD
LRPGDIIKELDLRRPIFQKTASYGHFGRSDPEFTWEVPKDLEHEKDVA
>gnl|CDD|240269 PTZ00105, PTZ00105, 60S ribosomal protein L12; Provisional
SSLAPKVGPLGLSPKKVGDDIAKATKDWKGLKVTVKLTVQNRQATVEVVPTASSLLIKALKEPPRDRKKV
KNIKHSGNLTFDQVIKIARTMRPKSMAKTFKGTVKEVLGTCVSIGCTVDGESPRDIQEKINNGEIKVPES
>gnl|CDD|185450 PTZ00106, PTZ00106, 60S ribosomal protein L30; Provisional
MMKKKKKKAQESINSKLQLVMKSGKYTLGTKSTLKALRNGKAKLVIISNNCPPIRRSEIEYYAMLSKTGV
HHYAGNNNDLGTACGRHFRVSVMSITDAGDSDILRALE
>gnl|CDD|240270 PTZ00107, PTZ00107, hexokinase; Provisional
EMRYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLEAHRRHRNLWIPNECSFKMLDSCVYNLPTG
KEKGVYYAIDFGGTNFRAVRVSLRGGGKMERTQSKFSLPKSALLGEKGLLDKKATATDLFDHIAKSIKKM
MEENGDPEDLNKPVPVGFTFSFPCTQLSVNNAILIDWTKGFETGRATNDPVEGKDVGELLNDAFKRNNVP
ANVVAVLNDTVGTLISCAYQKPKNTPPCQVGVIIGTGSNACYFEPEVSAYGYAGTPINMECGNFDSKLPI
TPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLKAPPKMWQSGSFESEDASMILNDQSPDL
QFSRQVIKEAWDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAPAKKTRTVQGKATVAIDGSVYVKNPW
FRRLLQEYINSILGPDAGNVVFYLADDGSGKGAAIIAAMVANDK
>gnl|CDD|240271 PTZ00108, PTZ00108, DNA topoisomerase 2-like protein; Provisional
KKNKTVEERYQKKTQIEHILLRPDTYIGSIETQTEDMWVYDEEKNRMVYKTITYVPGLYKIFDEILVNAA
DNKARDKGGHRMTYIKVTIDEENGEISVYNDGEGIPVQIHKEHKIYVPEMIFGHLLTSSNYDDTEKRVTG
GRNGFGAKLTNIFSTKFTVECVDSKSGKKFKMTWTDNMSKKSEPRITSYDGKKDYTKVTFYPDYAKFGMT
EFDDDMLRLLKKRVYDLAGCFGKLKVYLNGERIAIKSFKDYVDLYLPDGEEGKKPPYPFVYTSVNGRWEV
VVSLSDGQFQQVSFVNSICTTKGGTHVNYILDQLISKLQEKAKKKKKKGKEIKPNQIKNHLWVFVNCLIV
NPSFDSQTKETLTTKPSKFGSTCELSEKLIKYVLKSPILENIVEWAQAKLAAELNKKMKAGKKSRILGIP
KLDDANDAGGKNSEECTLILTEGDSAKALALAGLSVVGRDYYGVFPLRGKLLNVRDASLKQLMNNKEIQN
LFKILGLDIGKKYEDPKGLRYGSLMIMTDQDHDGSHIKGLLINMIHHFWPSLLKNPGFLKEFITPIVKAT
KKGNQVISFFTIPDFEKWKQTVGLKGWKIKYYKGLGTSTDKEGKEYFSNIDKHRIRFVYVDDSDDDSIDL
AFSKKRVEDRKEWITNYKGGTYVDHSKKKLTYSDFVNKELILFSIADNERSIPSLVDGLKPGQRKILFAC
FKRNLKNEIKVAQLSGYVSEHSAYHHGEQSLQQTIVGMAQNFVGSNNINLLYPCGQFGSRLQGGKDHAAA
RYIFTKLSKITRYIFPEEDDPILDYLEDDGQSVEPFYYVPIIPMVLVNGAEGIGTGFSTSIPNYNPLDII
DNLRRRLNGEEVRPLVPWYRGFKGTIERNPKGKFISKGIYEKVPDGTVEITELPIGKWTEDYKEFLESET
LKEKDVIVDYRDYSTANTVHFTVKLNDGVLEQWEEEGIEKVFKLKSTISTTNMVLFDENGKIKKYSDALD
ILKEFYLVRLDLYKKRKEYLLGKLERELARLSNKVRFIKHVINGELVITNAKKKDLVKELKKLGYVRFKD
IIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSLTKEKVEKLNAELEKKEKELEK
LKNTTPKDMWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSK
KASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEF
SSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKK
TARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDDEDDEDDD
>gnl|CDD|240272 PTZ00109, PTZ00109, DNA gyrase subunit b; Provisional
CRLLYTLIILCIIIPTVFKVSSGYLLNGNGIIRNTQINIPNLGNRTYSRKEESLNKKLNNKKIYKFFLNN
QRLEDAEPSKVKDVEQQKERVPQLQRCSEYDADDIVVLEGLEAVRKRPGMYIGNTDEKGLHQLLFEILDN
SVDEYLAGECNKITVVLHKDGSVEISDNGRGIPCDVSEKTGKSGLETVLTVLHSGGKFQDTFPKNSRSDK
SEDKNDTKSSKKGKSSHVKGPKEAKEKESSQMYEYSSGLHGVGLSVVNALSSFLKVDVFKGGKIYSIELS
KGKVTKPLSVFSCPLKKRGTTIHFLPDYKHIFKTHHQHTETEEEEGCKNGFNLDLIKNRIHELSYLNPGL
TFYLVDERIANENNFYPYETIKHEGGTREFLEELIKDKTPLYKDINIISIRGVIKNVNVEVSLSWSLESY
TALIKSFANNVSTTAGTHIDGFKYAITRCVNGNIKKNGYFKGNFVNIPGEFIREGMTAIISVKLNGAEFD
GQTKTKLGNHLLKTILESIVFEQLSEILEFEPNLLLAIYNKSLAAKKAFEEAKAAKDLIRQKNNQYYSTI
LPGKLVDCISDDIERNELFIVEGESAAGNAKQARNREFQAVLPLKGKILNIEKIKNNKKVFENSEIKLLI
TSIGLSVNPVTWRQYDLSHGTKASKDESVQNNNSTLTKKKNSLFDTPLRYGKIILLTDADVDGEHLRILL
LTLLYRFCPSLYEHGRVYVACPPLYRITNNRMKQFNVSTKNSKKYIYTWSDEELNVLIKLLNKDYSSKET
TRSVEEKGNAPDLDNEYEDEKLDNKNMRENNVDEVELKTELGTNVADTEQTDELDINKAFFKFSKHYEIQ
RFKGLGEMMADQLWETTMDPKKRILIRITVSDAMRASELIFLLMGEDVQSRKQFIFENSPAFG
>gnl|CDD|240273 PTZ00110, PTZ00110, helicase; Provisional
MRSTDGSSSNGSVSSGPSNNYNSYGPYPDSSNPYGNYQANHQDNYGGFRPGYGNYSGGYGGFGMNSYGSS
TLGKRLQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITIIAGENVPKPVVSFEYTSFPDY
ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLA
PTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTY
LVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDLTACHNI
KQEVFVVEEHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVL
NEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLAR
DLVKVLREAKQPVPPELEKLSNERSNGTERRRWGGYGRFSNNVNNIPLGGSNRFY
>gnl|CDD|173403 PTZ00111, PTZ00111, DNA replication licensing factor MCM4; Provisional
MDFTPRSRQVLSGRVDSLRPDSQVFNPNNTRDESNNETQYTMYGKTPNLVRRIRNARNDIGDLGRETFMD
QRDVARLPFLLDNRLEELSERFTNFLKNFTEFSDVLEFKDEQQSKPEYTELYYLWKLMNFIKENLRDHST
GYSRILPFEVDLMHVYSFDKVLYKLLVTFPADCIAELDKVLVKLFNELLSKHYSDLSLENNSFFPRARLM
NKPVSDCVGNLEPSMADSLVQFSGTVVRQTWIVPEITMACFRCRGQKKIGLNDYQPCTCEHYEYVIQGEV
NEPLLCNECNSKYTFELNHNMCVYSTKKIVKLLQSNSSLNNPDKDGLDNSVDNSGLNGEIYMKDNEVINL
NLYDDLIDSVKTGDRVTVVGILKVTPIRTSTTRRTLKSLYTYFVNVIHVKVINSTNANQPEKGLKYLGNE
NDFSDLQVYKILELSRNPMIYRILLDSFAPSIKARNNVKIGLLCQLFSGNKNSSDFNKSPDACYKVDNFR
GIINVLLCGDPGTAKSQLLHYTHLLSPRSIYTSGKSSSSVGLTASIKFNESDNGRAMIQPGAVVLANGGV
CCIDELDKCHNESRLSLYEVMEQQTVTIAKAGIVATLKAETAILASCNPINSRYNKNKAVIENINISPSL
FTRFDLIYLVLDHIDQDTDQLISLSIAKDFLLPHMTGSGNDEDTYDRSNTMHVEDESLRSEKDYNKNDLD
MLRMYIKFSKLHCFPKLSDEAKKVITREYVKMRQGNFQTSNLDELEHAQEDDDDDLYYQSSGTRMIYVSS
RMISSIIRISVSLARMRLSTVVTPADALQAVQIVKSSTFQSLVDPTTGKIDFDQLHQGITTNKMQQLNQM
YEQVLSVLTRSSNQDSNKSLDLNEVLSLCHKTFKDNRDHKDGEIYKLISEVLNKMVQEGTAVRENNSYYL
KKIFS
>gnl|CDD|240274 PTZ00112, PTZ00112, origin recognition complex 1 protein; Provisional
MTPKKKIHKSYESHKICQPRENRETNKVPNFHNFHLNDNEILSPTKGGIKLDVSKLSILSFENTPRKEEK
KKKNLNLPDYNQIQNNTHDFYIDLNERSKTPIKNNDNVTTPIKANKKEKHNLDSSSSSSISSSLTNISFF
SSPTSIYSCLSNSLSSKHSPKVIKENQSTHVNISSDNSPRNKEISNKQLKKQTNVTHTTCYDKMRRSPRN
TSTIKNNTNDKNKEKNKEKDKNIKKDRDGDKQTKRNSEKSKVQNSHFDVRILRSYTKENKKDEKNVVSGI
RSSVLLKRKSQCLRKDSYVYSNHQKKAKTGDPKNIIHRNNGSSNSNNDDTSSSNHLGSNRISNRNPSSPY
KKQTTTKHTNNTKNNKYNKTKTTQKFNHPLRHHATINKRSSMLPMSEQKGRGASEKSEYIKEFTMEEVAK
LTKDTTIKLVEENSCQYEDGVIYESIQINDVEYSIGDDVLIFCTGNGNTYNGKSGTKKNQNNKNIKENIY
QLRKGKISSFYKNTNSNQVEAEVCIYYDQHDAQYIKELEEKQKSRRCKADFEVFLDDDTKNFYLLGNIHF
KILDAKMILKKIYVYNEKELYDEDKTAKQGKDKFLCTHYLKEREERICFIQNSEHWDNLVLGSSDLYYSF
SNEKKSNKNKSLKLIIEKLKINEQGGQKKNSKKEYMNPAQTTTSSKAKTHSKTKNDHNKSKTSKNKEPSS
TSFLQDVKKKSDPHNVDFKSFIKQDQENYYVNLLRNITDPTDKAIRMMQLDVVPKYLPCREKEIKEVHGF
LESGIKQSGSNQILYISGMPGTGKTATVYSVIQLLQHKTKQKLLPSFNVFEINGMNVVHPNAAYQVLYKQ
LFNKKPPNALNSFKILDRLFNQNKKDNRNVSILIIDEIDYLITKTQKVLFTLFDWPTKINSKLVLIAISN
TMDLPERLIPRCRSRLAFGRLVFSPYKGDEIEKIIKERLENCKEIIDHTAIQLCARKVANVSGDIRKALQ
ICRKAFENKRGQKIVPRDITEATNQLFDSPLTNAINYLPWPFKMFLTCLIVELRMLNDFIIPYKKVLNRY
KVLVETSGKYIGMCSNNELFKIMLDKLVKMGILLIRPYIPLESLAKNKNKEALLGFNESSKKNANETSKS
TRTQVSAEIDKESGDMGLELNVETQLIITALMKDAECSQKLNFY
>gnl|CDD|240275 PTZ00113, PTZ00113, proliferating cell nuclear antigen; Provisional
MLEAKLNNASVLRRLFECIKDLVSDGNIDFDETGLKLQALDGNHVALVHLKLHDSGFSHYRCDRERALGI
NIASVTKVFKLCSNNDSVLIQSEEDKDNINFVFENNVEDKVSSFSLKLMSIEQDALSIPENEEGFDAEVT
LSSKELTNICRQMNEFSDTVKIEIDSNSIKFTTQGDLGDGEVVLKPRPPTSEDDCGVTIKVRKPIKQSYA
TKYLNMFAKSGCLSDVVTLGLSDNRPIEVKYEIKDTSPDARHTHKLGEVKFFLAPKMDDDMDTKE
>gnl|CDD|185455 PTZ00114, PTZ00114, Heat shock protein 60; Provisional
NRSKMFSSRYRFKGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKA
IEFSDRFENVGAQLIRQVASKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLE
SLKEQSRPVKTKEDILNVATISANGDVEIGSLIADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGY
ISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKRPLLIIAEDVEGEALQTLIINKLRG
GLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDNVGLKLDDFDPSMLGSAKKVTVTKDETVILTGGGD
KAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALNATRAAVE
EGIVPGGGVALLRASKLLDKLEEDNELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKDP
SFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKKNKNSAAPPM
>gnl|CDD|240276 PTZ00115, PTZ00115, 40S ribosomal protein S12; Provisional
MRVISVNRQSNIRLNFIIPTFACSRPPIGSSNSFSFRRFGSIPSSSFNSLRSGPSGEDNFPSSFSSIPSP
LSHFSKLPQPSNINAVRQFSTRNISGRLFYKRRPKQVPKLKPKNRRSKWLEGAPQKKGICVKVRVQTPRK
PNSGLRKVARVRLSTGRTVTVYIPGIGHNLNTHSVVLVRGGRCKDVPGCNYKAVRGVYDLLPVKNRARSR
SKYGVKLSEEKKKKRLERKNEKHITIKKDRELFNKYRWFDWVNGDGTLREKPLGPDEPVPIDIFHFNTRY
RNIKHKSQSE
>gnl|CDD|173408 PTZ00116, PTZ00116, signal peptidase; Provisional
MDNVLNRLNVLSYSMALCFLILCLFNYGTSFYLFDEKEMSTNIKVKSVKRLVYNRHIKGDEAVLSLDLSY
DMSKAFNWNLKQLFLYVLVTYETPEKVKNEVIIQDYIITNKKQAKKTYKNFITKYSLKDYNNGLRNNNIN
LQVCYKYMPIVGLSRSYEGAKISYKLPAEYFDNLPSNYPLYYPDK
>gnl|CDD|173409 PTZ00117, PTZ00117, malate dehydrogenase; Provisional
TVVKRKKISMIGAGQIGSTVALLILQKNLGDVVLYDVIKGVPQGKALDLKHFSTLVGSNINILGTNNYED
IKDSDVVVITAGVQRKEEMTREDLLTINGKIMKSVAESVKKYCPNAFVICVTNPLDCMVKVFQEKSGIPS
NKICGMAGVLDSSRFRCNLAEKLGVSPGDVSAVVIGGHGDLMVPLPRYCTVNGIPLSDFVKKGAITEKEI
NEIIKKTRNMGGEIVKLLKKGSAFFAPAAAIVAMIEAYLKDEKRVLVCSVYLNGQYNCKNLFVGVPVVIG
GKGIEKVIELELNAEEKELFDKSIESIQELTQKAKALIV
>gnl|CDD|240277 PTZ00118, PTZ00118, 40S ribosomal protein S4; Provisional
MGKGIKKHMKRINAPSHWMLDKLGGQYAPKTSPGPHKLRECLPLVILLRNRLKYALTYDEVKLIVIQKIV
KVDGKVRTDCTYPVGFMDVVSLTKTNEYFRLLYDTKGRFVPHKITNEEAKYKLCRVKKTFLGPKEVSIAV
THDGRTIRYVHPDVKVGDSLRLDLETGKVLEFLKFEVGNLVMITGGHNVGRVGTIVSKEKHPGSFDLIHV
KDSRGKTFATRLSNVFVIGVGTKPYVSLPRERGIKKDIIEERRNRLAKALRN
>gnl|CDD|240278 PTZ00119, PTZ00119, 40S ribosomal protein S15; Provisional
MNIKNRILKHNNLHVLDPKDHNLPFLRIAKRYESRVKAHRYTGITAIKTHAQKTEWYLKAERDFLSERNQ
IPNGYIGLWQYDDIKHLRKNIINMLHLNCANSKQIHKYKKLCIRRCLQRRPFDTGSAPVQIGCLTEKILN
LRAHLILRCKDHPKKRTMSILLARRQKLMKYLYKTDFELYKHTCNLLKIKCILFAIPDSRDRSKAINAAA
VDGDRCKFLIRQKLWKGKYRPRPIKDPKGQTIRYTRHPIEQPPSDYALPKEYKPQLSNSWPYGVKENYQK
GKYTIYNPTAPGLGYCPVPMLF
>gnl|CDD|185458 PTZ00120, PTZ00120, D-tyrosyl-tRNA(Tyr) deacylase; Provisional
MRVVIQRVLSASVTVEGEVVGSIGKGLVLLVGIHEEDTWEDADYIIRKCLKLRLWPDEGGKMWDRSVKDK
DYEVLVVSQFTLFNVKKGNKPDFHLAMSPEDALPLYNKFVEKFKKEYAPEKIKTGKFGQYMNVSLVNDGP
VTIILDSKEKNLAK
>gnl|CDD|173412 PTZ00121, PTZ00121, MAEBL; Provisional
MGLLKFFAFLAFLCICKAKAIANPQEAFMDRFDIAKNHINIKWSNNGIHGEGDFKYDIDDGDNLDFEGNE
EEKSGICPDHGAEEMYKGGCPDYGKTFLMDFEDDEYNEEFLDEISFGFLNKKLKLPIEIPLEKSGLAMYQ
GLFKRCPLDEKHSSLIKKEHEYDMCFEKFYNNMEISDRIKKRGKQNRKYIHFGSHGLGGRFGANIDEPLH
DYKNDEHHVTKKMGFPEKIKNLFDCSIYSHCIGPCFGKDFNNECFLNLPILFNHQTKECVIIGTHEAKRI
HNCLSGNSDQGFERCFLPMKKEAGKEWTYASSFIRPDYETKCPPRFPLNDTMFGYFNHRTGECESAVKNH
EGNYKLSFKKCIEGLFNHIEGDDDNGNNNFLWGVWFIEGNAEEKTNLASMDDIGMCSFLKEKPNCVLKKE
KHFSFTILTANSFDFAQNIIYPELEEMHDKENGSSLIGEKAPEGREERIDLEENDGKKEEAGSEDKEIKE
FEIPQNLNKNEKEEINEHEVKGLPKENINYILKVHMRFENNHFNIHNDSIFKRKDEPIHKMIELNIPSDN
KLHNLGAQGIGDSNISHWNSNNINGGSVSQNEGNIGEKLNGNPQQKFMERFDIPKNHIFIEWKKDGEFGE
DEFKYDIISNKTAGTAQSLFHDNKDDTCPNHSIEGRAHGSCPNYGKAIIVENLEGEEEDKNFNLEFLNEI
HTGYLGKIFIKDVEIPYDKSGIAMHHGFLASCPIDENEEKLFQRKNDYNYDMCKSKIFPNPFSMKELDPK
NRLFKYYGLYGFGGRLGANISINKRDKGKEEKREDNITLPMKNPGLIKNLFDCSIYSYCLGPCLEGSFGN
KCFRNLPAYYNHATNECVILGTHEQERNNNCRKEKEDKKKPNCQIIRKTLDSKDWTYVSSFIRPDYEEKC
PPRFPLKSKSFGIFDEKTGKCKSLIDEANEVGINKFGGCLEYLFINSPKDLYNSDRKKYWGIWAADEPVN
DNNIEIANGECYHILQKPTCVIDKENHFSFTALTANTIDFNQNFNIEKIEELTEYGNNDDVLKEKDIIDE
DIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEA
KKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKA
EELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEA
RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK
ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA
EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK
KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK
KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE
EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA
KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK
KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLV
INDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEI
EKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIKISKKDMCINDFSSKFCDYMKDN
ISSGNCSDEERKELCCSISDFCLKYFDHNSNEYYDCMKEEFADKDYKCFKKKEFSNMAYFAGAGIVLILL
FVIGSKAIIGKWFEEATFDEFDENYDKIYTLAMINNEEIQEAGPLDFSEEMIDK
>gnl|CDD|240279 PTZ00122, PTZ00122, phosphoglycerate mutase; Provisional
FTFRRFFSKVNIGKLASPLLRGRTFSFSESVFKATPAKEKKARYISASGVSSLLLSVALTYAKENFGYYK
TWGVPWNEDWDGNYKHRPKARGKRADKSASHQRQIILVRHGQYINESSNDDNIKRLTELGKEQARITGKY
LKEQFGEILVDKKVKAIYHSDMTRAKETAEIISEAFPGVRLIEDPNLAEGVPCAPDPPSRGFKPTIEEIL
EDMKRIEAAFEKYFHRPVEDEDSVEIIVCHGNVIRYLVCRALQLPPEAWLRLSLYNCGITWIVISSEGHV
SLSGFGSVGHLPPDMVTYH
>gnl|CDD|240280 PTZ00123, PTZ00123, phosphoglycerate mutase like-protein; Provisional
WNKENRFTGWTDVPLSEKGVQEAREAGKLLKEKGFRFDVVYTSVLKRAIKTAWIVLEELGQLHVPVIKSW
RLNERHYGALQGLNKSETAEKHGEEQVKIWRRSYDIPPPPLEKSDERYPGNDPVYKDIPKDALPNTECLK
DTVERVLPYWEDHIAPDILAGKKVLVAAHGNSLRALVKYLDKMSEEDILELNIPTGVPLVYELDENLKPI
KKYYLLDEEELKAKMEAVANQGKAKS
>gnl|CDD|173415 PTZ00124, PTZ00124, adenosine deaminase; Provisional
MNILQEPIDFLKKDELNIDLSQMDKKERYKIWKRIPKCELHCHLDLCFSVDFFLSCIRKYNLQPNLSDEE
ILDYYLFAKGGKSLGEFVEKAIRVADIFNDYEVIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKHNLDI
DLIHQAIVKGIKEAVELLDHKIEVGLLCIGDTGHDAAPIKESADFCLKHKADFVGFDHAGHEVDLKPFKD
IFDYVREAGVNLTVHAGEDVTLPNLNTLYSAIQVLKVKRIGHGIRVAESQELIDMVKEKDILLEVCPISN
VLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFMKMNEWALEKSFLD
KDIKLKIKKLYF
>gnl|CDD|240281 PTZ00125, PTZ00125, ornithine aminotransferase-like protein; Provisional
LENQYGAHNYHPLPVVLKRGKGVFVWDVEGKKYYDFLSAYSAVNQGHCHPKILAALINQAQKLTLTSRAF
YNDVLGLAEKYITDLFGYDKVLPMNSGAEAGETALKFARKWGYEVKGIPENQAKIIFCNGNFSGRTIGAC
SASTDPKCYNNFGPFVPGFELVDYNDVEALEKLLQDPNVAAFIVEPIQGEAGVIVPDDGYLKQVYELCKK
YNVLLIVDEIQTGLGRTGKLLAHDHEGVKPDIVLLGKALSGGLYPISAVLANDDVMLVIKPGEHGSTYGG
NPLACAVAVEALEVLKEEKLAENAQRLGEVFRDGLKELLKKSPWVKEIRGKGLLNAIVFDHSDGVNAWDL
CLKLKENGLLAKPTHDNIIRFAPPLVITKEQLDQALEIIKKVLKSFDSNK
>gnl|CDD|240282 PTZ00126, PTZ00126, tyrosyl-tRNA synthetase; Provisional
TNPGEEFKSGSCSIKVGLREELETGFRGSPPQSKLSLEERVKLCLSIGEECIQPEELRELLKLKERPICY
DGFEPSGRMHIAQGILKAINVNKLTKAGCVFVFWVADWFALLNNKMGGDLEKIRKVGEYFIEVWKAAGMD
MDNVRFLWASEEINKNPNDYWLRVMDIARSFNITRIKRCSQIMGRSEGDEQPCAQILYPCMQCADIFYLK
ADICQLGMDQRKVNMLAREYCDKKKIKKKPIILSHHMLPGLLEGQEKMSKSDPNSAIFMEDSEEDVNRKI
KKAYCPPGVIEGNPILAYFKSIVFPAFNSFTVLRKEKNGGDVTYTTYEELEKDYLSGALHPGDLKPALAK
YLNLMLQPVRDHFQNNPEAKSLLSEVKSYKVTK
>gnl|CDD|240283 PTZ00127, PTZ00127, cytochrome c oxidase assembly protein; Provisional
LAFSKVLFSIINTRNVLPNRLKPLLAQRSRKFFTATKFKLAEESRVAESTDASTQWVAPGGEKKVGHWLL
GCAGLVGGMVVLGGYTRLTESGLSMTDWKFIGVKPPITQEEWEKEFDKYKQFPEYKQVHYGMTLEEFKKI
FFWEWLHRMLGRSIGLFFGLPLLYFAAKGYLKPRMLKRLSAIGGLGGAQGFVGWWMVKSGLDEPLTENKK
PRVSPYRLAAHLFNAFVIYSLLLWNGLTLILFALPSIAPFPELLKMRLLARGLFALVFLTAMSGAFVAGN
DAGLAYNTWPKMGGKFVPDDVHNFVPWYKNFFENTAVVQFNHRVLAYLTFLSSLGLYYKARKLNLPKSVR
RLLMALLGALTLQVLLGITTLLSQVPVHLAVAHQFGALVLLTTLLRLCHVLRR
>gnl|CDD|185464 PTZ00128, PTZ00128, cytochrome c oxidase assembly protein-like; Provisional
MIPFTAVSSLPTTTPPTSDNRGSSANKSELFRSFKHSKNSGKENELKKFKKERGQFFYYNLSLYIAMFGC
SFAFVPLYRLFCQSTGYGGDADKKDYSMKKKYPVPKRLIKIRFLADTGSTMPWEFEPLQKEVEVLPGETA
LAFYRAKNRSDKPVIGVATYHIAPPEAGLYFNKIQCFCFEEQRLNPHEEVDMPVFFYIDPDILNDPRLKW
VDEITLSYTFFEAESEIPYEYR
>gnl|CDD|185465 PTZ00129, PTZ00129, 40S ribosomal protein S14; Provisional
SKKKATKMSKKQEVATLGPNVAKGELVFGVAHIFASFNDTFIHVTDLSGRETLVRVTGGMKVKADRDESS
PYAAMMAAQDVAARCKELGINALHIKLRATGGVRTKTPGPGAQAALRALARAGLKIGRIEDVTPIPTDST
RRKGGRRGR
>gnl|CDD|185466 PTZ00130, PTZ00130, heat shock protein 90; Provisional
MKLNRVFFCAFVICALQPNWVPQLCNVLCESDEGKSEEKEEKEEVKKDRDNIPEIEDGEKPTSGIEQHQY
QTEVTRLMDIIVNSLYTQKEVFLRELISNAADALEKIRFLSLSDESVLGEEKKLEIRISANKEKNILSIT
DTGIGMTKEDLINNLGTIAKSGTSNFLEAISKSGGDMSLIGQFGVGFYSAFLVADKVIVYTKNNNDEQYI
WESTADAKFTIYKDPRGSTLKRGTRISLHLKEDATNLMNDKKLVDLISKYSQFIQYPIYLLHENVYTEEV
LADIAKEMENDPNYDSVKVEETDDPNKKTRTVEKKVKKWKLMNEQKPIWLRPPKELTDEDYKKFFSVLSG
FNDEPLYHIHFFAEGEIEFKCLIYIPSRAPSINDHLFTKQNSIKLYVRRVLVADEFVEFLPRYMSFVKGV
VDSDDLPLNVSREQLQQNKILKAVSKRIVRKILDTFRTLYKEGKKNKETLRAELAKETDEEKKKEIQKKI
NEPSTYKLIYKEYRKYLKTGCYEDDINRNKIVKLLLFKTMLHPKSISLDTYIENMKPDQKFIYYASGDSY
EYLSKIPQLQIFKKKNIDVVFLTESVDESCVQRVQEYDGKKFKSIQKGEITFELTEDEKKKEEKVKKMYK
ALIDVISDTLRNQIFKVEISRRLVDAPCAVVSTEWGLSGQMEKLMKINVNNSDQIKAMSGQKILEINPDH
PIMIDLLKRSVSNPKDSQLTESIKIIYQSAKLASGFDLEDTADLAQIVYDHINQKLGVDNNLKIDDLDPA
IFETKKIEQEDSPDGQKFHEEINIDDEIQKQDNANESNDKNDEL
>gnl|CDD|185467 PTZ00131, PTZ00131, glycophorin-binding protein; Provisional
MRLSKASDIKSAGDSNCKNFNSKNSSKYSLMDVQEKNEKKNSLGAFHSKKIILIFGIIYVALLNAYICGD
KYEKAADYGFREGRILAECEDACANKEKTSLRKCAQKTSTSADPEGQIMKAWAADPEYRKHIEIFYKILT
HTDPNDEVERRNADNKEDLTSADPEGQIMKAWAADPEYRKHLEIFYKILTHTDPNDDTSADPEGQIMKAW
AADPEYRKHLEVFHKILTHTDPNDETSADPEGQIMKAWAADPEYLKHLEIFYKILTHTDPNDETSADPEG
QIMKAWAADPEYLKHLEIFYKILTNTDPNDEVERRNADNKEDLTSADPEGQIMKAWAADPEYRKHLEIFY
KILTHTDPNDDVERRNADNKEDLTSADPEGQIMKAWAADPEYRKHLEVFHKILTNTDPNDESE
>gnl|CDD|240284 PTZ00132, PTZ00132, GTP-binding nuclear protein Ran; Provisional
MQQMDEVPEFKLILVGDGGVGKTTFVKRHLTGEFEKKYIPTLGVEVHPLKFYTNCGPICFNVWDTAGQEK
FGGLRDGYYIKGQCAIIMFDVTSRITYKNVPNWHRDIVRVCENIPIVLVGNKVDVKDRQVKARQITFHRK
KNLQYYDISAKSNYNFEKPFLWLARRLTNDPNLVFVGAPALAPEEIQIDPELVAQAEKELQAAANVPLPD
DDDDL
>gnl|CDD|173423 PTZ00133, PTZ00133, ADP-ribosylation factor; Provisional
MGLWLSSAFKSLFGKKEVRILMVGLDAAGKTTILYKLKLGEVVTTIPTIGFNVETVEYKNLKFTMWDVGG
QDKLRPLWRHYYQNTNGLIFVVDSNDRERIGDAREELERMLSEDELRDAVLLVFANKQDLPNAMSTTEVT
EKLGLHSVRQRNWYIQGCCATTAQGLYEGLDWLSANIKKSMQ
>gnl|CDD|185469 PTZ00134, PTZ00134, 40S ribosomal protein S18; Provisional
MSLTLEKADDFQHILRILNTNVDGKRKVPYALTAIKGIGRRFAYLVCKKAGIDVTKRAGELTAEEIEKIV
EIIANPLQFKIPDWFLNRQRDPKDGKNSHLTSNMLDTKLREDLERLKKIRLHRGLRHHWGLRVRGQHTKT
TGRRGRTVGVSRKK
>gnl|CDD|240285 PTZ00135, PTZ00135, 60S acidic ribosomal protein P0; Provisional
MAKPEKKAKKKAYFEKLYELLEKYKKILIVSVDNVGSKQMQDIRRSLRGKAELLMGKNTLIRKALKQRLE
ELPELEKLLPHVKGNVGFVFTKDDLFEVKPVILENKVPAPARAGVIAPIDVVIPAGPTGMDPSQTSFFQA
LGIATKIVKGQIEITNEVHLIKEGQKVGASQAVLLQKLNIKPFSYGLEVLSIYDNGSIYDAKVLDITDED
IVAKFQEGVQNVAAISLAAGYPTEASAPHSILNAFKNLAAIGLESGFTFPLAEKIKEALANPSAAAAAAA
AAAAAAAAAAAAPAEEEEEEEDDMGFGLFD
>gnl|CDD|185471 PTZ00136, PTZ00136, eukaryotic translation initiation factor 6-like protein; Provisional
MALRTQFENSNDIGVFSKLTNSYCLVALGGSENFYSVFESELAPHIPVVHTTIGGTRVIGRLTVGNRKGL
LVPSICTDQELQHLRNSLPDSVKVQRVEERLSALGNCIACNDYVALIHPDLDRETEEIIQDVLGVEVFRT
TIAGNVLVGTYCVFTNQGGLVHPKTSVQEMDELSSLLQVPLVAGTVNRGSDVIGAGLVVNDWAAFCGMDT
TATEISVIERIFKLRRAGGKEGNDLQKLRSSLIDTLA
>gnl|CDD|173427 PTZ00137, PTZ00137, 2-Cys peroxiredoxin; Provisional
MKLTGISLIPSASYIRNMRPLKNTTTAFHTLNTRNCFKSVDRISSLKSVNGVRNYSTSEGLCNTVTSSLV
GKLMPSFKGTALLNDDLVQFNSSDYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSV
DSPFSHKAWKELDVRQGGVSPLKFPLFSDISREVSKSFGLLRDEGFSHRASVLVDKAGVVKHVAVYDLGL
GRSVDETLRLFDAVQFAEKTGNVCPVNWKQGDQAMKPDSQSVKQYLSNRFN
>gnl|CDD|185472 PTZ00138, PTZ00138, small nuclear ribonucleoprotein; Provisional
MMMTKRKLQKIMTQPINQIFRFFTEKTRVQIWLYDHPNLRIEGKILGFDEYMNMVLDDAEEVYTKKNTRK
DLGRILLKGDNITLIMAAK
>gnl|CDD|240286 PTZ00139, PTZ00139, Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional
RFAVPAFNRLTRTFFSGHLSSAYPVIDHTYDAVVVGAGGAGLRAALGLVELGYKTACISKLFPTRSHTVA
AQGGINAALGNMTEDDWRWHAYDTVKGSDWLGDQDAIQYMCREAPQAVLELESYGLPFSRTKDGKIYQRA
FGGQSLKFGKGGQAYRCAAAADRTGHAMLHTLYGQSLKYDCNFFIEYFALDLIMDEDGECRGVIAMSMED
GSIHRFRAHYTVIATGGYGRAYFSCTSAHTCTGDGGAMVSRAGLPLQDLEFVQFHPTGIYGAGCLITEGC
RGEGGILRNSEGERFMERYAPTAKDLASRDVVSRAMTIEILEGRGCGPNKDHIYLDLTHLPPETLHERLP
GISETAKIFAGVDVTKEPIPVLPTVHYNMGGIPTNWKTQVLTQRNGDDDKIVPGLLAAGEAACASVHGAN
RLGANSLLDIVVFGRAAANTVMEILKPGRPQPDLPKDAGEASIARLDKIRHNKGDISTAQIRKRMQRTMQ
KHAAVFRIGESLQEGVEKIKEIYSDFKDVKIKDKSLVWNTDLIETLELENLLTQAKQTILSAEARKESRG
AHARDDFPERDDKNWMKHTLSYIRDVKKGKVRLTYRPVITTPLDNEMETVPPAKRVY
>gnl|CDD|173430 PTZ00140, PTZ00140, sexual stage antigen s45/48; Provisional
MLKGILAKLLLVAALLYGFLVKKCIKGNVKYTKPYKCDFSFNPVHNIKPVLTEKRSIYEEVWCSIHNPFL
YDKIALICPKKNNGDYSEFKIVPENCFEKHLYSPYENERTEKDIENLGLDEYELSENRTFNDFTLKILTI
PPFYKKDKTIYCRCDNSKTVKSIPGEKIVKGKVGLVKINVLKYPHKITSINLTKEPFTYLPDTYEKSDFV
SNGLDLELKDKELDVLAFEFKDNKCFKIGKCENLYNSKKGFLHKNLLIFKAPAYFLSNDVCTECSCKVNN
TPYKIVLKPQKTKKIDGCDFTKPKGKGDYTNGFDIADLGSSEKITCTIHLVSTKYNHLAGIKCPYKLIPT
YCFQHVLYEKESPELKPYKPFLLDDVLNTGDVEYYSNAKEGSYIFGLPTSIPKTTSFRCICEKGGKIGYM
ELKIASSSWGFLSKTLILLIVLLLLYF
>gnl|CDD|185474 PTZ00141, PTZ00141, elongation factor 1- alpha; Provisional
MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERG
ITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLA
FTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPW
YKGPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSV
EMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLD
CHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQT
VAVGVIKSVEKKEGSGTKAAAKAKKK
>gnl|CDD|240287 PTZ00142, PTZ00142, 6-phosphogluconate dehydrogenase; Provisional
MSDIGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVKKAKEGNTRVKGYHTLEELVNSLKKPRKV
ILLIKAGEAVDETIDNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGPSL
MPGGNKEAYDHVKDILEKCSAKVGDSPCVTYVGPGSSGHYVKMVHNGIEYGDMQLISESYKLMKHILGMS
NEELSEVFNKWNEGILNSYLIEITAKILAKKDDLGEEHLVDKILDIAGSKGTGKWTVQEALERGIPVPTM
AASVDARNISALKEERTKASSHLAGPNPANKTETEDKKYFIDDLKNALYCSKIISYTQGFFLIKEASKEF
GWNLNLGEIARIWRGGCIIRAVFLDRIKNAFKKNPQLDLLFLDPDFNDELKNKQPSWRKVVSMATKNGIP
TPAFSASLAYYQMYRSQNLPANLVQAQRDYFGAHTYKRLDRPGAFHTNWE
>gnl|CDD|240288 PTZ00143, PTZ00143, deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
MHLKILPLNDEVRELYKNHKTFHEGDSGLDLFIVKDQTIKPGETAFIKLGIKAAAFQKDEDGSDGKNVSW
LLFPRSSISKTPLRLANSIGLIDAGYRGELIAAVDNIKDEPYTIKKGDRLVQLVSFDGEPITFELVDELD
ETTRGEGGFGSTGRL
>gnl|CDD|240289 PTZ00144, PTZ00144, dihydrolipoamide succinyltransferase; Provisional
STVNLVKRLNKPLLSSVKGMFRRFSLRKLQPACSAHFSKSYFSIKVIKVPTMGDSISEGTVVEWKKKVGD
YVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAAPAAAAAAKAEKT
TPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQN
TCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYV
DISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPI
INPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL
>gnl|CDD|240290 PTZ00145, PTZ00145, phosphoribosylpyrophosphate synthetase; Provisional
MSFFTSKACATTKWYKRSRFGWQRFREGNYERTAAVLLSSSVVYYCTLSDEESRREFRSFSKNVKGGLSS
FLLCGQPNAGNERLFFSKNISFCDTSKKGFRHPLWRSEEKRPFEKKMENAILFSGSSNPLLSKNIADHLG
TILGRVHLKRFADGEVSMQFLESIRGKDVYIIQPTCPPVNENLIELLLMISTCRRASAKKITAVIPYYGY
ARQDRKLSSRVPISAADVARMIEAMGVDRVVAIDLHSGQIQGFFGPRVPVDNLEAQLIGLDYFTKKDLYK
PVIVSPDAGGVYRARKFQDGLNHRGISDCGIAMLIKQRTKPNEIEKMDLVGNVYDSDVIIVDDMIDTSGT
LCEAAKQLKKHGARRVFAFATHGLFSGPAIERIEASPLEEVVVTDTVKSNKNIDSCKKITKLSVSVLVAD
AIRRIHQKESLNDLFNVKG
>gnl|CDD|240291 PTZ00146, PTZ00146, fibrillarin; Provisional
GMGGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPGKVIVVPHRFPGVFIA
KGKSDALVTKNMVPGESVYGEKRISVEDAEGGEKIEYRVWNPFRSKLAAAIIGGVANIPIKPGSKVLYLG
AASGTTVSHVSDLVGPEGVVYAVEFSHRSGRDLTNMAKKRPNIVPIIEDARYPQKYRMLVPMVDVIFADV
AQPDQARIVALNAQYFLKNGGHFIISIKANCIDSTAKPEVVFASEVQKLKKEGLKPKEQLTLEPFERDHA
VVIGVYRPVKKKK
>gnl|CDD|140176 PTZ00147, PTZ00147, plasmepsin-1; Provisional
MNLTIKEEDFTNTFMKNESSFNTFRVDNKVKRWKIQKLFQILYVTVFIVLAGGLFYYIFENVVFQKNRKI
NEIIKTSKHSTIGFNIENSHDRIMKTIKEHKLKNYIKESVKFFNKGLTKKSYLGSEFDNVELKDLANVMS
YGEAKLGDNGQKFNFIFDTGSANLWVPSIKCTTEGCETKNLYDSSKSKTYEKDGTKVEMNYVSGTVSGFF
SKDLVTIGNLSVPYKFIEVTDTNGFEPFYTESDFDGIFGLGWKDLSIGSVDPYVVELKNQNKIEQAVFTF
YLPPEDKHKGYLTIGGIEERFYEGPLTYEKLNHDLYWQVDLDVHFGNVSSEKANVIVDSGTSVITVPTEF
LNKFVESLDVFKVPFLPLYVTTCNNTKLPTLEFRSPNKVYTLEPEYYLQPIEDIGSALCMLNIIPIDLEK
NTFILGDPFMRKYFTVFDYDNHTVGFALAKKNL
>gnl|CDD|240292 PTZ00148, PTZ00148, 40S ribosomal protein S8; Provisional
MGISRDSRHKRRLTGGKMPIHRKKRKFELGRQPANTKLGSKRVRPVRCRGGNFKFRALRLDTGNFSWGSQ
GIAKKTRILDVVYNASNNELVRTKTLVKNAIVQIDAAPFKQWYAKHYGIDLGKKKKYKKEEENKKAKKKS
ESLVAKLEVRKKNHKIDKALLEQFQSGRLLARISSRPGQSGRADGYILEGKELEFYLKKLEKKKK
>gnl|CDD|240293 PTZ00149, PTZ00149, hypoxanthine phosphoribosyltransferase; Provisional
MKIPNNPKRSTAATSSYDYVGAGEDRKEPIYIKDDDFYDLDSFLIPPHYKNYLTKILLPNGLIKDRVEKL
AYDIKQVYGNEELHILCILKGSRGFFSALVDYLNRIHNYSSTESPKPPYQEHYVRVKSYCNDESTGKLEI
VSDDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIATLFEKRTPLSNGFKGDFVGFSIPDHF
VVGYCLDYNEHFRDLDHVAVLNDEGIKKYKK
>gnl|CDD|240294 PTZ00150, PTZ00150, phosphoglucomutase-2-like protein; Provisional
MMESLEAQVELWLKWDKDPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQ
TAQGLCAYVIETFGQALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLK
CLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYLTETLVEDPLAEVSDA
YFATLKSEYNPACCDRSKVKIVYTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEG
KGALKLSMETAEAHGSTVVLANDPDADRLAVAEKLNNGWKIFTGNELGALLAWWAMKRYRRQGIDKSKCF
FICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIELNAENGLTTLFAYEEAIGFMLGTRVRDKDGVT
AAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFTNNSYYICYDPSRIVSIFNDIRNNGSYPTKLGGYPV
TRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLKWYAELSGTKDEAVEKELA
ALVDEVVEQLMQPEKYGLVPRKED
>gnl|CDD|173440 PTZ00151, PTZ00151, translationally controlled tumor-like protein; Provisional
MKVYKDVFTGDEVCSDSYKQLDPFGNAEFSEIAFEVKSKKVIKGNEDYGIADNSEEGDVEGVDADVETVI
DIVDAFKLQSTPFTKKEYSTYIKKYMQRIKAYLEEKNPDRVEKFKTNAQPFVKHILENFDDFEFYLGESL
DCEAGLIYGYYKGEELAPRFVYIKDGLKEERY
>gnl|CDD|173441 PTZ00152, PTZ00152, cofilin/actin-depolymerizing factor 1-like protein; Provisional
MISGIRVNDNCVTEFNNMKIRKTCRWIIFVIENCEIIIHSKGATTTLTELVGSIDKNDKIQCAYVVFDAV
NKIHFFMYARESSNSRDRMTYASSKQALLKKIEGVNVLTSVIESAQDVADLK
>gnl|CDD|173442 PTZ00153, PTZ00153, lipoamide dehydrogenase; Provisional
AGETAGTCIWLGALLLLVTQGGIAKSTAGGHQLHALHEKGFPVPLGKSTSSTFIRCNFVPSPANPISLGA
SKQESPGILTPMPSSARLSSPQPRSEKSLRANGFATSQSMNFSDEEYDVGIIGCGVGGHAAAINAMERGL
KVIIFTGDDDSIGGTCVNVGCIPSKALLYATGKYRELKNLAKLYTYGIYTNAFKNGKNDPVERNQLVADT
VQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYERGHIVDKNTIKSEKSGKEFKVKNIII
ATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPL
LDADVAKYFERVFLKSKPVRVHLNTLIEYVRAGKGNQPVIIGHSERQTGESDGPKKNMNDIKETYVDSCL
VATGRKPNTNNLGLDKLKIQMKRGFVSVDEHLRVLREDQEVYDNIFCIGDANGKQMLAHTASHQALKVVD
WIEGKGKENVNINVENWASKPIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEISFYKANSKVL
CENNISFPNNSKNNSYNKGKYNTVDNTEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVK
DLAHMVHSHPTISEVLDAAFKAIAGVRTH
>gnl|CDD|240295 PTZ00154, PTZ00154, 40S ribosomal protein S17; Provisional
MGRVRTKTVKRAARQIVEKYYSKLTLDFHTNKKIVEEVAIIPSKRLRNKIAGFVTHLMKRIQKGPVRGIS
LKLQEEERERRMDYVPEKSEVDIDNITVDQDTKDMLKSLGLGVPRPVKVPDVARKKQKQARRRR
>gnl|CDD|185484 PTZ00155, PTZ00155, 40S ribosomal protein S9; Provisional
MGRNYRNHSKTYKTPRRPFEKERLDAELKLCGEYGLKNKREIWRVQYTLAKIRKAARELLTLDEKDPKRL
FEGEALLRRMHRLGLLDEDERKLDYVLGLTVEKLLERRLQTKVFKLGLAKSIHHARVLIRQRHIRVGKQI
VDIPSFLVRVDSEKHIDFADTSPFGNGRPGRVKRKAAKAAK
>gnl|CDD|185485 PTZ00156, PTZ00156, 60S ribosomal protein L11; Provisional
ESKKENPMRKIRIEKLVLNICVGESGDRLTRAAKVLEQLTGQKPVFSKARYTVRSFGIRRNEKIACHVTV
RGDKAEEILERGLKVKEFELKKRNFSDTGNFGFGIQEHIDLGIKYDPSTGIYGMDFYVVLGRPGFRVARR
KRKQSKVGKSHRVTKEEAMKWFKTTFDGIILN
>gnl|CDD|240296 PTZ00157, PTZ00157, 60S ribosomal protein L36a; Provisional
MVNVPKNRKTYCKKCGKHTSHKVSQYKKGKESLFAQGKRRYDRKQSGYGGQTKPIFRKKAKTTKKIVLKL
ECTKCKSKRQKVLK
>gnl|CDD|185487 PTZ00158, PTZ00158, 40S ribosomal protein S15A; Provisional
MVRMSVLADCLRSIVNAEKQGKRQVLIRPSSKVVVKFLQVMQKHGYIGEFEIVDDHRSGKIVVNLNGRLN
KCGVISPRFDVTLGEFEKWANNILPSRQFGHVVLTTSYGIMDHEEARRRHTGGKILGFFY
>gnl|CDD|240297 PTZ00159, PTZ00159, 60S ribosomal protein L32; Provisional
MVKPKVKKKIVKKRTKKFTRFQSERFPRVKPSWRKPRGIDNRVRRRFKGTRLMPKIGYGSDKKTRYLLPS
GFYKFPVRNVKDLEMLLMHNRKYAAEIAHNVSARKRKAIVERAKELNVRVLNGNARLRKEEKE
>gnl|CDD|185489 PTZ00160, PTZ00160, 60S ribosomal protein L27a; Provisional
MPTRFKKCRKMRGHVSHGYGRVGKHRKHPGGRGNAGGQHHHRINFDKYHPGYFGKVGMRHFHLKKNKYYC
PTINVDKLWSLVPEETRYKYAKKGDKAPVIDVTKAGYFKVLGKGHLPKQPVIVKARYFSKKAEKKIKAVG
GACVLTA
>gnl|CDD|240298 PTZ00162, PTZ00162, DNA-directed RNA polymerase II subunit 7; Provisional
MFFVVELWKNVSLKPSQLGPRYQQIIEDMLRSQVEGQCTRKYGYVICVIRIIHNEPGRVQDGTGMIVVNV
KYQAIVFKPFKDEVLDAIVTDVNKLGFFAQAGPLKAFVSRSAIPPDFVYDSDSAYPCYISSDGQIQIKPN
TEVRLRLQGVRYDASNLFAIATINSDYLGPIESSIL
>gnl|CDD|185490 PTZ00163, PTZ00163, hypothetical protein; Provisional
MNYFLSLFNVSLFFLLIFKYSYKNIVKKDLQDKFNKSIITINIASRILTENNKKWYKKYIYTSIFSGNKN
PQKRERKNEEENQKDNTKVDNDNNMENEMENHIDDSIDDPMDDLMNDKWEHHNSLEDRIKEYYTLTDPSD
GEENNSFFKKLKLIMNILDEVHSDLLINNSVTDGSIFSPELVPISVLSTMTLACPPIGTVTLPYITNRIN
FLNRYEGQNIHTEHDLKIFK
>gnl|CDD|240299 PTZ00164, PTZ00164, bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
SEDYSSLKDFSIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITTYVREEKYEKSPKKQNAVIMGRKTWES
IPKKFRPLKNRINVVLSRTLTEEEADPGVLVFGSLEDALRLLAEDLSIEKIFIIGGASVYREALSANLLD
KIYLTRVNSEYECDVFFPKIPESFFIVAIVSQTFSTNGTSYDFVIYEKKNDDEEDLLGKIFGQMKMTGRK
KSPKEQLYKACPSLKIREHEEFQYLDLIADIIKNGNVKEDRTGVGTISKFGYQMRFDLRESFPLLTTKKV
FLRGIIEELLWFIRGETNGNLLLDKGVRIWEGNGSREFLDSRGLTHREENDLGPVYGFQWRHFGAEYKDM
HDDYTGQGVDQLKNIIETIKNNPDDRRLILTAWNPSALDQMALPPCHLLSQFYVNDGKLSCMMYQRSCDM
GLGVPFNIASYALLTHMIAQVCGLRPGEFVHFLGDAHVYSNHVDALKEQLERVPYPFPTLKLKREVENIE
DFTIEDIEVIGYVPHPKIKMEMAV
>gnl|CDD|240300 PTZ00165, PTZ00165, aspartyl protease; Provisional
MKYNVIRVLILIFCLYVSAFPAVSLLFLSNGSTLKGLSNKIKSNIGANLGYPRMLSNQLFNKPAHKVELH
RFALLKKKRKKNSEKGYISRVLTKHKYLETKDPNGLQYLQQDLLNFHNSQYFGEIQVGTPPKSFVVVFDT
GSSNLWIPSKECKSGGCAPHRKFDPKKSSTYTKLKLGDESAETYIQYGTGECVLALGKDTVKIGGLKVKH
QSIGLAIEESLHPFADLPFDGLVGLGFPDKDFKESKKALPIVDNIKKQNLLKRNIFSFYMSKDLNQPGSI
SFGSADPKYTLEGHKIWWFPVISTDYWEIEVVDILIDGKSLGFCDRKCKAAIDTGSSLITGPSSVINPLL
EKIPLEEDCSNKDSLPRISFVLEDVNGRKIKFDMDPEDYVIEEGDSEEQEHQCVIGIIPMDVPAPRGPLF
VLGNNFIRKYYSIFDRDHMMVGLVPAKHDQSGPNFQELSSSSFSVPDGATIGITIILSLLLF
>gnl|CDD|240301 PTZ00166, PTZ00166, DNA polymerase delta catalytic subunit; Provisional
MSGDTQIMENIDKTFFTSSIPYGLLFSKLRRPLPPISLQKDLVFFQLDADYTEKDDKSQGNPHNTVSGVR
HVEVPIIRLYGVTKEGHSVLVNVHNFFPYFYIEAPPNFLPEDSQKLKRELNAQLSEQSQFKKYQNTVLDI
EIVKKESLMYYKGNGEKDFLKITVQLPKMVPRLRSLIESGVVVCGGGWDGIRLFQTYESNVPFVLRFLID
NNITGGSWLTLPKGKYKIRPPKKKTSTCQIEVDCSYEDLIPLPPEGEYLTIAPLRILSFDIECIKLKGLG
FPEAENDPVIQISSVVTNQGDEEEPLTKFIFTLKECASIAGANVLSFETEKELLLAWAEFVIAVDPDFLT
GYNIINFDLPYLLNRAKALKLNDFKYLGRIKSTRSVIKDSKFSSKQMGTRESKEINIEGRIQFDVMDLIR
RDYKLKSYSLNYVSFEFLKEQKEDVHYSIISDLQNGSPETRRRIAVYCLKDAILPLRLLDKLLLIYNYVE
MARVTGTPIGWLLTRGQQIKVTSQLLRKCKKLNYVIPTVKYSGGGSEEKYEGATVLEPKKGFYDEPIATL
DFASLYPSIMIAHNLCYSTLVPPNDANNYPEDTYVTTPTGDKFVKKEVRKGILPLIVEELIAARKKAKKE
MKDEKDPLLKKVLNGRQLALKISANSVYGYTGAQVGGQLPCLEVSTSITSFGRQMIDKTKELVEKHYTKA
NGYKHDATVIYGDTDSVMVKFGTDDIQEAMDLGKEAAERISKKFLKPIKLEFEKVYCPYLLMNKKRYAGL
LYTNPEKYDKIDCKGIETVRRDNCLLVQQMVETVLNKILIEKDVESAIEFTKGKISDLLQNRIDISLLVI
TKSLGKDDYEGRLAHVELAKKLRQRDPGSAPNVGDRVSYVIVKGAKGAPQYERAEDPLYVLENNIPIDTQ
YYLDQIKNPLLRIFEGVMDNPDSLFSGEHTRHITISSSSKGGLSKFVKKQLQCLGCKSVIKEGALCDNCN
QNKEPSIYGKKLAKRRHKEAEYSQLWTQCQRCQGSLHQEVICTNRDCPIFYRRKKVQKDLAELQELLSRF
GLDW
>gnl|CDD|185493 PTZ00167, PTZ00167, RNA polymerase subunit 8c; Provisional
MSLPSCLFEDRFVVRSVDNSKFERVSRIKAKSTGFDAELILDINSDLFPVREKQSLYIGLTNQLSSGPDD
NVWESSEPQSLMDQYEYVMYGKIFKFEEKSSERRTLYASFGGLLMALTADKQVVGDLELDMRIYLLVRRS
DDIR
>gnl|CDD|185494 PTZ00168, PTZ00168, mitochondrial carrier protein; Provisional
MEHFHNLVTGALSGVIVDAVLYPIDSIKTNIQAKKSFSFSDIKKLYSGILPTLVGTVPASAFFYCFYELS
KKLLTEYRENISKTNLYLISTSIAEITACIVRLPFEIVKQNMQVSGNISVLKTIYEITQREGLPSFLGKS
YFVMIVREIPFDCIQYFLWETLKEKAKKDFGKFSKKYPSITSAICGGLAGGIAGFLTTPVDVIKSRQIIY
GKSYIETVTEIAEEGYLTFYKGCCFRSSYLFFGGLIFFGSLRFFSFKKE
>gnl|CDD|240302 PTZ00169, PTZ00169, ADP/ATP transporter on adenylate translocase; Provisional
MDKKTNFATDFLMGGISAAISKTAVAPIERVKMLIQTQDSIPEIKSGKVPRYSGIVNCFRRVSKEQGVLS
LWRGNTANVIRYFPTQAFNFAFKDYFKNMFPKYNQKTDFWKFFGVNILSGGLAGASSLLIVYPLDFARTR
LASDIGKGGDREFTGLFDCLMKISKQTGFLSLYQGFGVSVQGIIVYRGAYFGLYDSAKALLFGNDKNTNI
LYKWAVAQTVTILAGLISYPFDTVRRRMMMMSGRKAKSEIQYTGTLDCWKKILKNEGLGGFFKGAWANVL
RGAGGALVLVFYDELQKLLK
>gnl|CDD|240303 PTZ00170, PTZ00170, D-ribulose-5-phosphate 3-epimerase; Provisional
MKQPLKAIIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTFLDC
HLMVSNPEKWVDDFAKAGASQFTFHIEATEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTDLVD
MVLVMTVEPGFGGQSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDR
KQAIELLRESVQKHLSKR
>gnl|CDD|240304 PTZ00171, PTZ00171, acyl carrier protein; Provisional
MRRNIIRKFFFVKGFLLLLPVIRSFVLQGKLLHISPIYRCVVRKARFFYSGEKNDERSSKSKQYLLSKED
VLTRVKKVVKNFEKVDASKITPESNFVKDLGADSLDVVELLIAIEQEFNLTIPDHDAEKIKTVQDAIDYI
EQNNMAKT
>gnl|CDD|185497 PTZ00172, PTZ00172, 40S ribosomal protein S26; Provisional
MTSKRRNNGRSKHGRGHVKPVRCSNCGRCVPKDKAIKRFVVRNIVDAASVRDIAEASVYYGYPLPKLYMK
QQYCVSCAIHSRVVRVRSREDRKIRTPPKRPFRPTGKK
>gnl|CDD|185498 PTZ00173, PTZ00173, 60S ribosomal protein L10; Provisional
MGRRPARCYRYCKNKPYPKSRFCRGVPDPKIRIYDIGRKKATVDEFPVCVHIVSDEYEQISSEALEAARI
SANKYMVKRAGKDGFHLRIRVHPFHVLRINKMLSCAGADRLQTGMRGAFGKPNGTCARVRIGQILLSIRT
KEAYVPQAIEALRRAKYKFPGRQKIVVSNKWGFTNYTREEYQKLRAEGKLIQDGVHVKLISPKGPLTKVN
PMA
>gnl|CDD|240305 PTZ00174, PTZ00174, phosphomannomutase; Provisional
MEMKKTILLFDVDGTLTKPRNPITQEMKDTLAKLKSKGFKIGVVGGSDYPKIKEQLGEDVLEDFDYVFSE
NGLVAYKDGELFHSQSILKFLGEEKLKKFINFCLRYIADLDIPVKRGTFIEYRNGMINISPIGRNCSQEE
RDEFEKYDKEHHIREKFIQDLKKEFSDLGLKFSIGGQISFDVFPKGWDKTYCLRHLENDFKEIHFFGDKT
FEGGNDYEIYNDPRTIGHSVKNPEDTIKILKELFLKK
>gnl|CDD|185500 PTZ00175, PTZ00175, diphthine synthase; Provisional
MMLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILINSNKEKLEEFYGKPVIEADREMVEEGCDEI
LEEAKEKNVAFLVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTE
TWKPDSFYDKIKANRDNGLHTLCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKGGGV
IAEDTLVVGVARVGSDDQQIVSGTLEDLLDVDFGPPLHSLVICAPTLHDIEEEFFELYRI
>gnl|CDD|140204 PTZ00176, PTZ00176, erythrocyte membrane protein 1 (PfEMP1); Provisional
MALKKGVINESKLSARNVLENIGNEIKDKRENESKYTDKLKGSLWEARFSDGLSSSFGDVRSGYYDSCSL
DHKFHTNINNGYPPARNPCDGRNQNRFDENGESYCNSDKIRGNENNSNAGACAPFRRQNMCDKNLEYLIN
KNTENTHDLLGNVLVTAKYEGESIVNNHPDKDKSSVCTALARSFADIGDIVRGKDMFKRNKHDNVENGLR
EVFKKIYEGLKNNGAREHYKEVKNGNYIKLREDWWTANRDQVWKAMTCVAPENAYFRKTEADGIGISSLI
LPYSKCGRDTDPPVVDYIPQRLRWMSEWSEYFCNVLNKEIDEMNNQCKDCEMSRRCNNDTEGEKCKKCKE
QCQIFKELVSKWKNQFDKQSMKYMELYNKASTNITKQNSSAPERGYRRNHRRRGYDDDTNVQLFLKKVIE
NNECKVESLGKYLDKTSHCGNYNFNYDNTPGSNRSNAFEITPEKFKKACKCKIPNPLEKCPNEENKNVCT
RFDKVYSCTSLSFKNDLSEWNNSGVKNKENDNNGVLVPPRRRNLCINLFSKKDYKMKDENDFKEDLLNAA
FSQGKLLGKKYSNYSNEAYEAMKFSYADYSDIVKGTDMMNDLKKLNKELNTLLKETEKGDISVDRKTWWD
DNKNVVWNAMLCGYKTENENQQLNSSWCNVPDDDNIDQFLRWLTEWAQQYCKEKLIKAHIINTKCKDIVE
GRKHKSMVDITDVECKRLFIDYEEWFRYRYNQWKGLSEKYIKIKKSKNSGVNIPSEECAASYVTKHCNGC
ICNLRDMEDIHKNINNQNELMKEMINIIKFDTDQYRTQLQNISNSMEINPKSVKTAVDTTKDIVSYGLAG
TMGVAAIGLQAGDFLGKKIQDLYNEFMKPVEKKLDTSSKNLNIYEDPNIMVPAGIGVALTLGLLLFKMRR
KAKRQVDMIRILQMSQNEYGIPTTKSPNKYVPYGSQRYKGKTYLYVEGDTDEEKYMFMSDTTDITSSESE
YEEMDINDIYVPGSPKYKTLIEVVLEPSKRDTQNDIPSDNTPSYKLTDEEWNQLKDDFISQYLPNTEPNN
NYRSGNSPTNTNNTTTSHDNMGEKPFIMSIHDRNLYTGEEISYNINMSTNTMDDPKYVSNNVYSGIDLIN
DTLSGNQHIDIYDEVLKRKENELFGTNHVKQTSIHSVAKNTYSDDAITNKINLFHKWLDRHRDMCEKWEN
HHERLAKLKEKWENDNDGGNVPSDNHVLNTDVSIEIDMDNPKPINQFSNMDINVDTPTMDNMEDDIYYDV
NDNDDDNDQPSVYDIPMDHNKVDVDVPKKVHIEMKILNNTSNGSLEQQFPISDVWNI
>gnl|CDD|240306 PTZ00178, PTZ00178, 60S ribosomal protein L17; Provisional
MVKYARKPQNPSKSAKAKGSDLRVHFKNTYETARAIKGMKLARAQKYLEDVLAKKRCVPFRRFNGGVGRT
AQAKEFGHTQGRWPEKSVKFVLSLLKNAEANAEAKGLDVEKLVISHVQVNRAPRGRRRTYRAHGRINPFM
SSPCHIELIATEKDETVPKPKEAPKKQTKKQLARSKLRVGN
>gnl|CDD|140206 PTZ00179, PTZ00179, 60S ribosomal protein L9; Provisional
MKIKSQDTITIPEDVTVSVKDRIVTVKGKRGTLTKDLRHLQLDFRVNKKNRTFTAVRWFGSKIPNSTINT
ALSHVRNMITGVTKGFRFKVRFAYAHFPISVSVENQLVEIRNFLGEKRVRRQVVADTVKVYRTDPSKVKD
ELVLEGNDLEQVSREAAVMHQLCLVKKKDIRKFLDGIYVQTKTNVEAEE
>gnl|CDD|173464 PTZ00180, PTZ00180, 60S ribosomal protein L8; Provisional
MGRVIRAQRKGNGSVFKAHGHKRLGPAKLRILDYAERHGYIRGVVKDIEHDPGRGAPLARVEFRDPYKYK
RVKELMVAPEGMYTGQYVYCGAKAPLAIGNVLPLGQIPEGTIVCNVEEKPGDRGTLARASGCYATIIGHS
DDGGKTRIRLPSGQKKTVSSLSRAMIGIVAGGGRIDKPVLKAGNAFHKYRGKRNCWPKVRGVAMNPVEHP
HGGGNHQHIGHPSTVSRHAPPGQKVGLIAARRTGLLRGGKKVKGAWHPEE
>gnl|CDD|140208 PTZ00181, PTZ00181, 60S ribosomal protein L38; Provisional
MPREIKTLKEFLAICSRKDARCVKVKHNPSATKFKVRCSRYLYTLVVADKKKADKIERSIHPSVKKITVT
ARSHAKTNAGSK
>gnl|CDD|185502 PTZ00182, PTZ00182, 3-methyl-2-oxobutanate dehydrogenase; Provisional
ASSFSSTLLGSRLPNSFSSASRSSSTESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYK
CTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGGQF
DCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRE
SVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVK
SVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTPFPYAKNLEPAYLPDKEKVVEA
AKRVL
>gnl|CDD|185503 PTZ00183, PTZ00183, centrin; Provisional
MRKRRSERPGLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKI
DFEEFLDIMTKKLGERDPREEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGD
GEISEEEFYRIMKKTNLF
>gnl|CDD|185504 PTZ00184, PTZ00184, calmodulin; Provisional
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFL
TLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYE
EFVKMMMSK
>gnl|CDD|140212 PTZ00185, PTZ00185, ATPase alpha subunit; Provisional
MRRFVAQYVAPAMGRLASTAAAGKSAAPGQKSFFKATEMIGYVHSIDGTIATLIPAPGNPGVAYNTIIMI
QVSPTTFAAGLVFNLEKDGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVGLL
TRSRALLESEQTLGKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTI
INQVRINQQILSKNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTM
GEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTA
LPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGI
LAEYRKLAADSVGGSQVQTVPMIRGARFVALFNQKNPSFFMNALVSLYACLNGYLDDVKVNYAKLYEYLL
VNKDLSVMYGTATNKFFYMYVQQLNYVIRFFTLNHPILNAEVEEMLKQHTHLFLQHYQSKMNAIKTEKEI
KALKNLLYSCKRAV
>gnl|CDD|140213 PTZ00186, PTZ00186, heat shock 70 kDa precursor protein; Provisional
MFARRVCGSAAASAARLARHESQKVQGDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGS
EKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQKDIKNVPYKIVRAGNGDAWVQDGNGKQYSPSQI
GAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIAGLNVIRVVNEPTAAALAYGMDKTK
DSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEEFRKTSGIDLSKERMALQ
RVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMHISRSKFEGITQRLIERSIAPCKQCMKDAGVE
LKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVKGLVLLDVTPLSLG
IETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVP
QIEVTFDIDANGICHVTAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAE
TQLTTAERQLGEWKYVSDAEKENVKTLVAELRKAMENPNVAKDDLAAATDKLQKAVMECGRTEYQQAAAA
NSGSSSNSGEQQQQQQQQQQQNSEEKK
>gnl|CDD|240307 PTZ00187, PTZ00187, succinyl-CoA synthetase alpha subunit; Provisional
LKGAAFMILKVSFRARSSTSAPRVWVNKNTKVICQGITGKQGTFHTEQAIEYGTKMVGGVNPKKAGTTHL
KHGLPVFATVKEAKKATGADASVIYVPPPHAASAIIEAIEAEIPLVVCITEGIPQHDMVKVKHALLSQNK
TRLIGPNCPGIIKPGECKIGIMPGHIHKKGKIGIVSRSGTLTYEAVAQTTAVGLGQSTCVGIGGDPFNGT
NFIDCLKLFLNDPETEGIILIGEIGGTAEEEAAEWIKNNPIKKPVVSFIAGITAPPGRRMGHAGAIISGG
KGTAPGKIEALEAAGVRVVKSPAQLGKTMLEVMKKKG
>gnl|CDD|240308 PTZ00188, PTZ00188, adrenodoxin reductase; Provisional
MNWRNFLCSPAQRTLARGWHLGGKLPFTGKCFFTNEAKPFKVGIIGAGPSALYCCKHLLKHERVKVDIFE
KLPNPYGLIRYGVAPDHIHVKNTYKTFDPVFLSPNYRFFGNVHVGVDLKMEELRNHYNCVIFCCGASEVS
IPIGQQDEDKAVSGGETNPRKQNGIFHARDLIYFYNNMYNDVRCKAVDNYLNSFENFTTSIIIGNGNVSL
DIARILIKSPDDLSKTDISSDYLKVIKRHNIKHIYIVGRRGFWQSSFTNAELRELISLENTKVILSKKNY
DLCCHLKSDEENTNMKKRQHEIFQKMVKNYEEVEKNKEFYKTYKIIEFIFYFEIRQIRPIDGAMKNVELE
LNKNVPMSFSSFKENKVLVTPLVIFATGFKKSNFAENLYNQSVQMFKEDIGQHKFAIFKAGWFDKGPKGN
IASQILNSKNSTHLVLNFLQKVDIFFDNDISSLLKEKQIPYVSFDDWTYLHQLEKQMGAQQNKIAQKFSQ
TGEVLRILKDRMGKSR
>gnl|CDD|240309 PTZ00189, PTZ00189, 60S ribosomal protein L21; Provisional
MPHSYGYRAGTRHKFAKPFRKHGVPSLSTYLTTFKVGDYVDIVVDSAVHKGMPYKYYHGRTGRVFNVTPR
AVGVIVNKRVRGRIVRKRIHVRIEHVRKSRCREDFLKRVAANDAIKAEAKKKGELPSTKRQPAQPRPAGF
VKPKPTEVVTVRPLPFVEIY
>gnl|CDD|140217 PTZ00190, PTZ00190, 60S ribosomal protein L29; Provisional
MAKSKNHTNHNQSSKNHRNGIKGPLPLHLHNSKRGSWLPALVNARRVRKHNQKAALKARRERIAAFAAKN
>gnl|CDD|185507 PTZ00191, PTZ00191, 60S ribosomal protein L23a; Provisional
KAPAKKAKKKAKKAAKAAKKGVKVKKRKVRTSVRFFRPKTLRLPKKPKYPRRVKPASKKLDKYSIIKYPL
TTEKAMKKIEDNNTLVFIVDQRANKTQIKKAVEKLYDVKVVKVNTLITPDGLKKAYIRLSPDVDALDVAN
KIGII
>gnl|CDD|173472 PTZ00192, PTZ00192, 60S ribosomal protein L13; Provisional
MPKGNNAIPHVHQRKHWNPCSSQKGNVKVFLNQPAQKHRRRRLRLLKAKKIFPRPLKALRPQVNCPTVRH
NMKQRLGRGFSLAELKAAGLNPRFARTIGIRVDRRRKNKSEEGMNVNVQRLKTYMSKLVLFPMNHKKVQK
GEAKEEEVKAATQDRSRFGDAAVGGVVTPSREAPRVVSKEERSKNVYAFLKKNHSAVRFFGVRSRRAARK
EAKKEEKK
>gnl|CDD|140220 PTZ00193, PTZ00193, 60S ribosomal protein L31; Provisional
MTRAGFKGKVLGKEKKQALLDARKKAVESRKSRDDRRWKRVLAKMDEEKRKKYHGVGNTAEHSRVRGITR
ASLRKRTGRKPDNISMEATIHLSKLLKKKTFHKRAPIAIKRIKAFVGRLMKTKDNRIDASLNTYIWHKGV
KGVPGRVRVLVERKSETLEGGKRKHFYTVISNVPVASFKNLTTKVVEQ
>gnl|CDD|185508 PTZ00194, PTZ00194, 60S ribosomal protein L26; Provisional
FNSIVSSSRRKARKAHFTAPSHLRRKLMSAPLSKELRAKYNVRSMPVRKDDEVMVVRGHHKGREGKVTAV
YRKKWVIHIEKITREKANGEPVQIGIHPSNVIITKLKLNKDRKAILERKARSTKSDKGKGKYTAADKAMQ
QMD
>gnl|CDD|140222 PTZ00195, PTZ00195, 60S ribosomal protein L18; Provisional
MGVDLTGISKKSRVVRHHTYSTNPYIKLLIKLYKFLAKRTSSGFNKVVYQRLIKSRSNRAPISLSRIAVV
MKRKAVFTAKGKKAPIAVVVGDVLDDVRMARIPAMRVCALRFSKSARQSIVAAGGECLTFDQLAMIAPTG
KNTYLLRGRKSGRESVRHFGASGVPGSHSKPYATNRGKETKRGRRTGRSYKRKAFRHV
>gnl|CDD|185509 PTZ00196, PTZ00196, 60S ribosomal protein L36; Provisional
PRTGIAVGLNKGHIVTKRARKPSPSKRKGLLSKRKRLVKDVIREVCGFSPYERRMIELLKVGKDKRALKY
AKKRLGTHKRAKAKRDEIQEALRAQRKK
>gnl|CDD|185510 PTZ00197, PTZ00197, 60S ribosomal protein L28; Provisional
MTHSTDLQWLLVRQNSKFLQKRNGIRLSSDPFNNNANWTKRHCGFLNTKAAVVKTKGDRILVTTKDGSSN
NKPKQMYKKTVMAAGVRASVVSRAVAAVRPDLASVAFRRARKMACTASRMKKVAAARKERSSKIKFSRKS
VRPKRN
>gnl|CDD|173474 PTZ00198, PTZ00198, 60S ribosomal protein L22; Provisional
AKVGSRGRKRQKQVKKKKKKFKIDCTIPAEDGIIDLSGFEQFLQDRIKVDGKTGNLGNKVRVSREKNKIT
VTTTIPFSKRYLKYLTKKYLKKKQLRDFLRVVATGKGTYELKYFNIQDEEEE
>gnl|CDD|185511 PTZ00199, PTZ00199, high mobility group protein; Provisional
MAKKQGKVLVRKNKRKKKDPNAPKRALSAYMFFAKEKRAEIIAENPELAKDVAAVGKMVGEAWNKLSEEE
KAPYEKKAQEDKVRYEKEKAEYAK
>gnl|CDD|240310 PTZ00200, PTZ00200, cysteine proteinase; Provisional
SAVVSNPNQRLVDNRFDDVEESVRDSTISTLSSSFRRISRKKRVIIISFLVFLFLAIGGSIVSYVLVSKS
KMVKSFKSDLEEHIDKDFPRLDKSKRDSYVDELTRLFKDGYISDDPKLEFEVYLEFEEFNKKYNRKHATH
AERLNRFLTFRNNYLEVKSHKGDEPYSKEINKFSDLTEEEFRKLFPVIKVPPKSNSTSHNNDFKARHVSN
PTYLKNLKKAKNTDEDVKDPSKITGEGLDWRRADAVTKVKDQGLNCGSCWAFSSVGSVESLYKIYRDKSV
DLSEQELVNCDTKSQGCSGGYPDTALEYVKNKGLSSSSDVPYLAKDGKCVVSSTKKVYIDSYLVAKGKDV
LNKSLVISPTVVYIAVSRELLKYKSGVYNGECGKSLNHAVLLVGEGYDEKTKKRYWIIKNSWGTDWGENG
YMRLERTNEGTDKCGILTVGLTPVFYSS
>gnl|CDD|240311 PTZ00201, PTZ00201, amastin surface glycoprotein; Provisional
MACSIPLVVYVVVQFVAFLLVLVGTPIDMFRAHNRPGVTPCLTLWGFKLECKSTEYDVTVDMLWANCPAR
ILQFRVAQALAVISILVYGAAFVLGLVLLYGCTIHRWVCLALNIVGAVTLGVVWAAMVVTYYKDDGPLCP
RVRDMGYRFGTGFALLVVAWILDILNIIFLLLPCTVPASKANEKPESPTAQE
>gnl|CDD|240312 PTZ00202, PTZ00202, tuzin; Provisional
AAVPAFFGKSSSATRAPIAGGHVKAQIAGSVYAVHLQHLFLSPIVEVGSRVYVEYGRDAENEGAVVGGLV
VRVNGNGTLGVLLDNNRFDLAVPAEMIVLSEGRSKFISNAKYLEVVEWVRSAGVARRADQESTACILYHR
GWRADRLYLLEASDVHCMTHLPKSVRMSVLEKSEWQRDHHRQMRELLRERVKERDFRYVLTKYSGVVSAS
VALLGVASVFGWNFKNYRTQQRSYQLKVAVSTLTQPLNPRPSTLQSAPAVIRQFVSREAEESWVRQVLRR
LDTAHPRIVVFTGFRGCGKSSLCRSAVRKEGMPAVFVDVRGTEDTLRSVVKALGVPNVEACGDLLDFISE
ACRRAKKMNGETPLLVLKLREGSSLQRVYNEVVALACDRRLCHVVIEVPLESLTIANTLLPRLDFYLVPN
FSRSQAFAYTQHAIDALSLEHFVDVVGTNSNDLDELLAAVRQRRVSAAEYTNQKLLKAMRQLQAAWAGDP
QLRAAVKRLAAFPYDEGQHEGYDASSLRSPALRDIVLYDPVQDVWMFRNKVFHTAARCCL
>gnl|CDD|185513 PTZ00203, PTZ00203, cathepsin L protease; Provisional
MATSRAALCAVAVVCVVLAAACAPARAIYVGTPAAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMR
EHQARNPHARFGITKFFDLSEAEFAARYLNGAAYFAAAKQHAGQHYRKARADLSAVPDAVDWREKGAVTP
VKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFT
EKSYPYVSGNGDVPECSNSSELAPGARIDGYVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTS
CIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVNACLLTGYPVSVHVSQSPTPYL
>gnl|CDD|140231 PTZ00204, PTZ00204, hypothetical protein; Provisional
MFQLVSAAEVNKAYVSYPGGVSMCLRFPFCHCVWAHAMTLIEISGHYHRWVARGESEDWDYSNSFVVVCA
VLLENIAANEREGKCHLTFHAATSMHKNYMLVALRGKVVKAKVSFRFKEV
>gnl|CDD|140232 PTZ00205, PTZ00205, DNA polymerase kappa; Provisional
MCGGEENGGLDQAHVSYSGSASEQNIAEMIVDPSGSRQPTAFQLTLDCNKAGMGNVDKERVEAIIRNVSE
GSSFLMNEQRLAEGREKQLQELKRKSSLFTQLLGGERNAAQRKQWELKVSKIEQELEATRRLGTYIHLDM
DMFYAAVEIKKHPEYAAIPLAIGTMTMLQTANYVARGRGIRQGMPGFLALKICPNLLILPPDFDAYNEES
NTVRRIVAEYDPNYISFGLDELTLEVSAYIERFEGTKTAEDVASELRVRVFGETKLTASAGIGPTAALAK
IASNINKPNGQHDLNLHTRGDVMTYVRDLGLRSVPGVGKVTEALLKGLGITTLSDIYNRRVELCYILHNN
LFRFLLGASIGIMQWPDAATAANTENCEGATGGQRKAISSERSFTTPRTKEGLQEMVDTVFNGAYEEMRK
SELMCRQISLTIRWASYRYQQYTKSLIQYSDDSATLRRAVDGLLLPHAAKYSEMCLLGVRFLDLISAKDF
HMKRKGGNQLSISQFIRPKKPGEVTATTGIKRERTTEPKQVVEIIISSDDEDENDSVGLASSSTILVSTD
KGTVEREVTII
>gnl|CDD|240313 PTZ00206, PTZ00206, amino acid transporter; Provisional
MTSINAQPPNSATYPQDDHGSAEVVNLNAEVERPQPEEQKDGGGCFARVSLFMATIIPPGGIAASAFNIA
SSTVGAGIVGLPSAANSSGLVMAMIYLIIITAMTIFSIYALGVAADKTNIRTYEGVARVLLGPWGSYYVA
ATRAFHGFSACVAYVISVGDILSATLKGTNAPDFLKQKSGNRLLTSLMWLCFMLPLVIPRHIDSLRYVST
IAVSFMVYLVIVIVVHSCMNGLPENIKNVSVGKDDNAEIILFNSGNRAIEGLGVFIFAYVFQITAYEVYM
DMTNRSVGKFVLASTIAMGMCFTMYVLTAFFGYMDFGRNVTGSVLLMYDPVNEPAIMVGFVGVLVKLFVS
YALLGMACRNALYDVIGWDARKVAFWKHCIAVVTLSVVMLLCGLFIPKINTVLGFAGSISGGLLGFILPA
LLFMYSGGFTWQKVGPFYYISTYVVLITGVIAIVFGTGATIWGVTVG
>gnl|CDD|140234 PTZ00207, PTZ00207, hypothetical protein; Provisional
MSAPVDNVVVERLSTANQKPINEPRRFALLVLGAFCSICTSFMYAFNLISGAMQARYNLTQRDLSTITTV
GIAVGYFLLPYSFIYDYLGPRPIFVLSMTVFCLGTLLFALTFQEVIEGSVVRLSVYNGLMTLGCMLFDLG
AVVTVLSVFPSNRGAVVAIMKTFTGLGSAILGSIQLAFFSDNTSAYFFFLMSFALVVGILAIVFMRLPPF
HLTGYQEKHLDEEEKAQRLMRKGVYLKQKAPMWRFVYGFVILIILIVFLPLQGALVAYLKLGSNFKVGFA
VTVIVLTVIFPFMAFPLTTFDGKRPHDDSDGKAKEHVEAGEEVSAAEDKVVETDVDYIAPQFQETFIEGL
KTARLWCLLWSIFCCVGAHFVIIFNARFIYTALAGEAPDDALNTLLTVLNGVGSAVGRLCMSYFEIWSQK
RRAEDRVPITIALFIPSVCIITMLTLFLTLPKAALPLPYFIAAFANGFMAATIALVTRTIFAKDPAKHYN
FCFLGSVLSAIFLNRLLYGEWYTQQADKLGQDVCTERVCVVMPLAFLLGLSFLAFITSTYVHLQYRRLCL
KALEERRRIREEERALNELSSNPTEPTGNAN
>gnl|CDD|240314 PTZ00208, PTZ00208, 65 kDa invariant surface glycoprotein; Provisional
MMKYLLVFAIIATRIPVLLVANSGDKHVKANKKLTKEGAAALCKMKHLADKVAEERADKLKDRTQNFAGY
IEFELDRLDYWLEKLNGPKHSNDGYAKLSDSDTEKVKEIFEKAKDGIAKQLPEAKKAGEEAEKLHQEVKK
AAKNARGWRLDDEGQNSSGLYRVLEWYCGKKGENAGKSDNCDGIKFKVHYLGRRRNVIDCSSTGYEENYD
WSANALQVALNSWENVKPKKVESAGSDMNCNIGQSSESHPCTMTEEWQTDYKSAVEKLRELEDAHERGKK
AHDAMLGYANTAYAVNTKVEQEKPLSEVIVAAKEAGKKGAKIIIPAAAPATATESTKGEDSAISEHVDRG
IATNETQVEVGIDADFDSLLEASEAAEVSSRHQRTAMIILAVLVPAIILAIIAVAFFIMVKRRRNSSEDV
DTGKAEGGVSSVKVVM
>gnl|CDD|140236 PTZ00209, PTZ00209, retrotransposon hot spot protein; Provisional
MIQNNGNMRNTQNVFNERFNRAQGEVQERGGRQMQNPSVTGKRKSREEELYESLYYAKWSYVMSGYNQEP
LGMKVFFGRPQHIWTEEEVDITPEHCEVDAELEERPTGLEIFVLTSKMGWPSDRFQCSLISLYDESGIMD
NNVYIRREMMRVWYIIQRKLNAWWVQKTESTPPTHIVIGISGIGKSCGVGSFLLHSLLHFHEGMLDVVVY
FTDVKAYLIYNKKGNEEGRVVLYKRKDVTNVIEEMRLKKRGHIIFDINSPKETLPYEIPRNVWGVTVLAP
PDGVRYKYWMKNLEQTRIILNCDDVRDIKAFVAWKKLSLFPNYTTLDENARAKVKEELEDEWRLVERRVD
VVGPLPRYVFSNGATCREAAVIDYLSSLSCNRRDGYDMMMGKYFEWKGNHFTESLIKIVRERSRYGNLES
YHCRPLSVAIGNMILCTLFATVAESMSSHEFMMEYGKVGAYSLKTRALVSLLFPRVFCVVTKHLNYLRRL
GETEDKRSILKDMTPQQFQIFEQKFLPKTGQNAIGNCKYKVLYRSLEESKLFVDGFFFVEDCSRRVADMR
DGFPQLGVASKTIVLIQITDNYRKEASVSELQEFMTNIARYFSDWDTFSRNMAWEMIYVNAIYGGVIKTR
QRCVNNNTADAEQQTEETQVFWDGIDQYQITFDNKIQKELIIAYHEERKYRDAPAFTRKRGHE
>gnl|CDD|140237 PTZ00210, PTZ00210, UDP-GlcNAc-dependent glycosyltransferase; Provisional
MSPLKMRPTQARRRPRTADIAVILLLVMSLLIICCNLHRIHVVSTFLDENQAGVSQPIDEDEYLMFVPSN
VAAVWKAQRFLAVLGIPSVDNSERSRRRDLQRQTCWKYSGVATRSNNFSGSLLPLYLLAPHQSNSYLISH
SLKEEAARTHDIITLPTNDVSPSTRKKIGENGNWGIEAEVAMSRKTYLWLRFALHMFPNVSYIVKGDDDI
FIRVPKYLADLRVMPRHGLYMGRYNYYNRIWRRNQLTYVNGYCITLSRDTAQAIISYKPLERLVNMPFSM
WDYFDFLDLGMFYEDVMVGMILREKVVYRNLISVEMGRCHFHNAGKFGVRKSVRNMSVVIHHIQEADYEM
LMDYFPEGVIPPAPSKVMWLNSNWAAMQCEFR
>gnl|CDD|240315 PTZ00211, PTZ00211, ribonucleoside-diphosphate reductase small subunit; Provisional
HKEAMKENEEEEPLLKENPDRFVLFPIKYPDIWRMYKKAEASFWTAEEIDLGNDLKDWEKLNDGERHFIK
HVLAFFAASDGIVLENLAQRFMREVQVPEARCFYGFQIAMENIHSETYSLLIDTYITDEEEKDRLFHAIE
TIPAIKKKAEWAAKWINSSNSFAERLVAFAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLH
TDFACLLYSHLKNKLPRERVQEIIKEAVEIEREFICDALPVDLIGMNSRLMAQYIEFVADRLLVALGVPK
IYNSKNPFDWMDMISLQGKTNFFEKRVGEYQKAGVMAERTSKVFSLDADF
>gnl|CDD|185514 PTZ00212, PTZ00212, T-complex protein 1 subunit beta; Provisional
MIMANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSEGPRSGNVTVTNDGA
TILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVAR
KALEEIAFDHGSDEEKFKEDLLNIARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGT
LRDSYLEDGFILEKKIGVGQPKRLENCKILVANTPMDTDKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNK
VDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDL
IEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLMA
NAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEKGTVGDM
KELGITESYKVKLSQLCSATEAAEMILRVDDIIRCAPRQREQV
>gnl|CDD|185515 PTZ00213, PTZ00213, asparagine synthetase A; Provisional
TSSDPSAYIDLQEQILKVKQIFSEALAKELNLIRVEAPLLAEVGDGTQDNLSGVEKAVQVHVKGIPNSVF
EVVHSLAKWKRLTLGEHKFPVGEGIYTDMNALRVEEELDNIHSVYVDQWDWEMVIAPADRNLEYLKNTVR
RLYAAIRKTEEAICNEYPNLKRILPKEITFLHTEHLLKMYPNLSPKEREREIVKKYGAVFLIGIGCKLSS
GDTHDLRAPDYDDWSSPVSASKIGFPTADPTMNSLMSLQGLNGDILVYNPVLDDVLELSSMGIRVDAEAL
RRQLEITNNTDRLKCMWHQMLLNGELPQTIGGGIGQSRLCMFMLRKKHIGEVQCSVWPHETREQYALL
>gnl|CDD|173479 PTZ00214, PTZ00214, high cysteine membrane protein Group 4; Provisional
MLGLLPLLLLASFCGASTDTYYNKFGVECGGKQENCAQNRCILLGSDELCTQCVSGYVPINGKCQLYPGD
ASSVCIPDDASSPTRCIECKSEQNVFLFYGGCYTIDQSTVGSFICSQASNGRCTECNVSTTEKYVFTNPD
TSAAEKCILCSDTVGFNGYKGASGCLDCLPPITDKIGIALCTKCHYTEQNRHFYPIDYQCQAKGLHNCVN
GYCTSCYKTHLFYEYGCYSRHSSTGFAICAEANQYELDNVTICKECVNTSYAPKNGGCTLVGESASIESL
FSDCTKDASKGLCTACSSSAKSFLFYGGCYDRDSHIGSRLCSRIGSGVCTQWNSAFDFIFSKNDDNNGDG
YLCGDATNGGVSGCATCGYNSGAVTCTRCSAGYLGVDGKSCSESCSGDTRGVCTKVAEGSESTEVSCRCV
CKPTFYNSSGTCTPCTDSCAVCKDGTPTGCQQCSPGKILEFSIVSSESADCVDQCSVGSECAECGITIDG
SRYCTRCKDASTYPFNGVCIPNTQRDAYCTSTANGACTTCSGAAFLMNGGCYTTEHYPGSTICDKQSNGK
CTTTKKGYGISPDGKLLECDPTCLACTAPGPGRCTRCPSDKLLKRASGAATGSCVDPGACVDGYYADGDA
CLPCATPGCKTCGHASFCTECAGELFVSLDGQSCLEECTGDKVVGEVSGGVRRCWCERGFLPALDRSGCV
LPTECPPDMPSCAACDESGRCLLCVTSGHNVQVDQRTCAEGCGARASSNQGVCMCELDAVLTKGVCVPAK
ELAKKRTAAIAGGTVAGVLVIGVLVGFLCW
>gnl|CDD|185516 PTZ00215, PTZ00215, ribose 5-phosphate isomerase; Provisional
MQKKVAIGSDHAGFDLKNEIIDYIKNKGKEYKIEDMGTYTAESVDYPDFAEKVCEEVLKGEADTGILVCG
SGIGISIAANKVKGIRCALCHDHYTARMSRQHNNANVLAFGGRTTGIEVAKEIIDTFLSTPFEGGRHTER
IDKISAIEEEN
>gnl|CDD|240316 PTZ00216, PTZ00216, acyl-CoA synthetase; Provisional
MGGCVVSLMDKRNSRSEVPDPDIEEYRRYGPQNVPVPGTETENASAIYRIAGVTDEEHERLRNEWYYGPN
FLQRLERICKERGDRRALAYRPVERVEKEVVKDADGKERTMEVTHFNETRYITYAELWERIVNFGRGLAE
LGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNLLRL
MKSGGMPNTTIIYLDSLPASVDTEGCRLVAWTDVVAKGHSAGSHHPLNIPENNDDLALIMYTSGTTGDPK
GVMHTHGSLTAGILALEDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGFGSPRTLTDTF
ARPHGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEGKDTPYWNEKVFS
APRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEM
KLLDTEEYKHTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKA
LAKNCLGEYIALEALEALYGQNELVVPNGVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILK
DPEFQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFADE
>gnl|CDD|240317 PTZ00217, PTZ00217, flap endonuclease-1; Provisional
MGIKGLSKFLADKAPNAIKEQELKNYFGRVIAIDASMALYQFLIAIRDDSQGGNLTNEAGEVTSHISGLF
NRTIRLLEAGIKPVYVFDGKPPELKSGELEKRRERREEAEEELEKAIEEGDDEEIKKQSKRTVRVTKEQN
EDAKKLLRLMGIPVIEAPCEAEAQCAELVKKGKVYAVATEDMDALTFGTPVLLRNLNFSEAKKRPIQEIN
LSTVLEELGLSMDQFIDLCILCGCDYCDTIKGIGPKTAYKLIKKYKSIEEILEHLDKTKYPVPENFDYKE
ARELFLNPEVTPAEEIDLKWNEPDEEGLKKFLVKEKNFNEERVEKYIERLKKAKTKKTQTRLDSFFTATK
KPIKKSNSKAKLKKKKKKAGASAVPKSETSQEAKSSGKKKVKK
>gnl|CDD|185518 PTZ00218, PTZ00218, 40S ribosomal protein S29; Provisional
MGHLFNTHPRTYGKGSRQCRVCSNRHGLIRKYGLNVCRQCFRENAELIGFHKYR
>gnl|CDD|185519 PTZ00219, PTZ00219, Sec61 alpha subunit; Provisional
MAKMTRFLNLLRPAMAILPEVAEPDRKIPFKEKVLWTAIALFVFLVCCQIPLYGIRSSSSSDPFYWMRVI
LASNRGTLMELGISPIVTSSMVMQLLAGSKIIDVDQNNKEDRALFEGAQKLLGLLITLGEAVAYVWSGMY
GDISEIGAGNAILIILQLFFAGIVVILLDELLQKGYGLGSGISLFIATNICETIIWKAFSPTTINTGRGT
EFEGAIIALFHLLFTRSDKLRALKEAFYRPHLPNLTNLLATVLVFLVVIYFQGFRVDLPLKSQKVRGQQQ
SYPIKLFYTSNIPIILQTALVSNLYFFSQILYRRFKNNFLINLLGQWQEVEYSGQSVPVGGLAYYLSPPN
SFSDIINDPIHTILYIVFVLFSCALFSKTWIEVSGSSAKDVAKQLKDQGMGMVGYRDSSSMVRVLNRYIP
TAASFGGMCIGALTILADFLGAIGSGTGILLAVTIIYQYYETFAKEKEQYGFLF
>gnl|CDD|173484 PTZ00220, PTZ00220, Activator of HSP-90 ATPase; Provisional
FYVPPEVLYNAFLDAYTLTRLSLGSPAEMDAKVGGKFSLFNGSVEGEFTELEKPKKIVQKWRFRDWEEDV
YSKVTIEFRAVEEDHTELKLTQTGIPSLDKFGNGGCLERCRNGWTQNFLDRFEKILGYPKKK
>gnl|CDD|140248 PTZ00221, PTZ00221, cyclophilin; Provisional
MPFRKLKPRRDAPQALPDPPSREQVYNDIEERRLKEWENYQKSHRMKEEQNSCRAFLDISIGDVLAGRLV
FELFEDVVPETVENFRALITGSCGIDTNTGVKLDYLYTPVHHVDRNNNIIVLGELDSFNVSSTGTPIADE
GYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRPLLP
VTVSFCGALTGEKPPGRQQLLAAADDSASSEHVACAAEE
>gnl|CDD|140249 PTZ00222, PTZ00222, 60S ribosomal protein L7a; Provisional
MPGKEVKKATQPAKAASPYKKPAAASHFVARPKNFGIGQDVPYARDLSRFMRWPTFVTMQRKKRVLQRRL
KVPPALNQFTKVLDRSSRNELLKLIKKYAPETRKARRDRLHKVAEEKKKDPKKTVSTKAPLAVVTGLQEV
TRAIEKKQARMVVIANNVDPVELVLWMPNLCRANKIPYAIVKDMARLGDAIGRKTATCVAITDVNAEDEA
ALKNLIRSVNARFLSRSDVIRRQWGGLQLSLRSRAELRKKHARNAGVDAAAVI
>gnl|CDD|140250 PTZ00223, PTZ00223, 40S ribosomal protein S4; Provisional
MAKKHLKRLYAPKDWMLSKLTGVFAPRPRAGPHKLRECLPLLIIIRNRLKYALNAREAQMILRQGLVCVD
GKPRKDGKYPAGFMDVVEIPKTGDRFRILYDVKGRFALVKVSEAEAQIKLMKVVNVYTATGRIPVAVTHD
GHRIRYPDPRTSRGDTLVYNVKEKKVVDLIKNRNGKVVMVTGGANRGRIGEIVSIERHPGAFDIARLKDA
SGHEFATRAANIFVIGKDMNSVPVTLPKQQGLRINVIQEREEKLIAAEARKNAQARGARKARK
>gnl|CDD|240318 PTZ00224, PTZ00224, protein phosphatase 2C; Provisional
MGIMLPKPVLSKLVDRAGNSIFRCASACVNGYRESMEDAHLLYLTDDWGFFGVFDGHVNDECSQYLARAW
PQALEKEPEPMTDERMEELCLEIDEEWMDSGREGGSTGTFCVIMKDVHLQVGNVGDSRVLVCRDGKLVFA
TEDHKPNNPGERQRIEACGGRVVSNRVDGDLAVSRAFGDRSFKVKGTGDYLEQKVIAVPDVTHLTCQSND
FIILACDGVFEGNFSNEEVVAFVKEQLETCDDLAVVAGRVCDEAIRRGSKDNISCLIVQLKDGASYAKLF
GHTSFVPGPPSPRRNQPFRKAYAQMAEKGGTTTAAALEKRYDLLKAFEKKTLNEQEPVMQTAFEMSDELD
GETEQSFFGKGPAPGNEMEFFQSLAQQGGIP
>gnl|CDD|140252 PTZ00225, PTZ00225, 60S ribosomal protein L10a; Provisional
MSKIPPQTLSEAIQAVLKVDKERKFKESIDLQVNLKNYDPQKDKRFSGSLKLPNVCRPRMTVCLLCDLVH
EDIAKKEGVPTMNQEELKKLNKNKKLVKKMCNQYDAFLCSESIIKTVPRLVGPHMHRMGKFPTVCSPSES
LPDKVVELRSTVKFQLKKVLCLGTCVGHVEMTEEQLRQNVVMAINFLVSLLKKNWQNLKSAYIKSTMGKP
QRIY
>gnl|CDD|240319 PTZ00226, PTZ00226, fumarate hydratase; Provisional
MSLCSNCELLCSRAGIRDIEDAAAVNPEFNFVPIFQPVDPHDTEEYRRLEDLSDYVEVVEVGGGGKEILK
VPPEALTKLTSYAFSDIQHFLRKSHLAQLRRILDDPEASDNDRFVAMTLLKNACIAAGRVLPGCQDTGTA
IVLGKRGELIWTGGEDEKALSKGVYNAYTNRNLRYSQLAPLDMFDEKNTGCNLPAQIDLYATPGNEYEFL
FIAKGGGSANKTFLYQQTKSLLNPKSLRKFLEEKIKTIGTSACPPYHLAVVIGGLSAEMTLKTVKLASCR
YYDSLPTSGDEYGRAFRDLEWEEIILEKTQNIGIGAQFGGKYFAHDVRVIRLPRHGASCPIGIGVSCSAD
RQILAKINKDGVYLEQLEHDPAQYLPDITEDDLSKTPVVKIDLNQPMEEILKQLSKYPVKTRLSLTGTLI
VARDIAHAKIVEMLENGEPLPEYMKNHPIYYAGPAKTPDGYASGSFGPTTAGRMDSYVDLFMENGGSFIT
LAKGNRSKAVTNACKKYGGFYLGSIGGPAAILAKDNIKKVEVLDFPELGMEAVWKIEVENFPAFIVVDDK
GNDFYSQWLG
>gnl|CDD|140254 PTZ00227, PTZ00227, variable surface protein Vir14; Provisional
MFDLDSGGSQVEADDETISESTIQGERIIFKHLPAYLFEQKLKEDASGNEYSTYYNGLSNISKRYPWLQD
LFKKLSRNIKLVHDSYVEGDEFNKKRCYDLNYWLYNEVYNNLQSSSENDTKYFKDISTRLQEVWKNIVDD
NFKGQPYQCYPDKKLLLNMGYLQEIKDLFDFYEDYNEMKKEIIADTYNSCRRYVDYLKQRIPVYYTWRDS
CKVDEFACKRYIDDYMKYRPASIVPDLSPLVVLTYPGNPCYSSVYDLFVKAKEQPKRNDGIYKKKMEKLE
KLNPGGNLLLTDMGDGLRGSEFFIPGDHDDYWLRLKWDILLYITDDITPPLLGIVGVLLILWALYKFTPL
GKSFKHTRAKVRKRIRPNINYDDIKLLYGSEESLNSSTDSYDYNNDYDYDDSSSNSSYNLSYASSLDY
>gnl|CDD|240320 PTZ00228, PTZ00228, variable surface protein Vir21; Provisional
MTSDKEFSLDNIKDEYKFIQDSNFYKIYNEFNKSCDSINYGDKGSSCYKGSLEKWTQFPDVTDLLKNLYS
NLYRIYSTVKGNNNDYFENVNSEDKKIGCTYLKYWLYDQIITNNLDESKIKKLFQGWENYVKSKIKYKSL
NPCIFYNLKKDEIKKIKKIYAFNTILYPNANKFKTCASNQCKYMDYFGEGLDEFINSINKCSSNSPNDNY
CKEFNEFLNICKDESLYAGISIYHEYNKSSSDSAKKYLLSVEEYENQPLYIYLKNKNWLNFLKTSHFLSN
KNRTTIAATSVVGSAIGLSSIFYYFYKFTPFGSSLRKGKGKNIVNIDEEAHNSLLYTSDTEQIPFKNREY
>gnl|CDD|140256 PTZ00229, PTZ00229, variable surface protein Vir30; Provisional
MIFHIHIMNKAKWIYKFFKDIDNYIAKAKDVESIDISDDAPSACTSFSRAWESKLKINGTAKNICEKFIK
LYNSLDNINKTLPTDTNYKKDCEFLNYWLNLKLYNNKINETTCVSMFYDELEAHCAGDFLGSFSDFQFMY
NIKNEELDKMNILYSLYYNYSKLRNIIDTASNKDAKSLLEPSTLCCNDYRIAAYKCNDKNNKFCKLLENF
KNKYDKLYNTVETKKPEFLKNFIKLSGCENNKIISTAVTGTIVGLIPLVGILYKFTPMGQLLKPKKGKLM
DGQINNDKEMRNISLMDQESEHISSQQGTYNIKYQSA
>gnl|CDD|240321 PTZ00230, PTZ00230, variable surface protein Vir7; Provisional
MNNYLGDQDLDNLNTKYYYGKLDEGWKNCQDYSFYNEAKEELDKNRVLRDDSDKILKALCYVYRESSSSS
FDSNICNFLYFWLGDILLEKLINKDLFSEIILMLFNTLINKNGKICTAPHYYMHKDDFKKFKLIFDCSED
YKSYKTQYIYPNMSCNNNYKSYLDTHVNIYNEFYSECEVEDKEKNYCKNFKKYFPDKKPNLLSTWKCKLE
ETDPQSKQLEEGDEGERVQQPTLTAIPGLEGEESLSVPPSDEXSPGSTLSRGFSDVRVPDSGIELGSIAD
PSNDSPTSITSKSITGAVSVAGFLVPSYLMYNYTPAGTWINKLLGRKTRTNHNPLTDAQLMANFSQPENF
NSERSGYNISYRPV
>gnl|CDD|140258 PTZ00231, PTZ00231, variable surface protein Vir17; Provisional
KLESYIKSFNLNMLISQLNNFKYENCYELTLDYLRSINETDNEALKNIGCSLESGYTFLTARDGETLTDL
CKYLNLWLDEQKSTHVIDKSIVSEEEWQKVENLWNKLMQGQTPDHKCKRQHEEKDISEYSKRLDLMSYCI
NRDYFKRLCQSPIGSDGYKAQKCKGFSDYTNDNYAKLIKGNKCIDKKSDINNYKYHISDDCTLYNIPKTF
PKCDENTQTIVDNDNSKTDIKRCESTPQVEVGGTELSENNADVVREPSELDNDDLGSEDALAESKFRHPE
QEVILDDIPELFLPSSTDVNLTDNGPSKPIYYAGLSVSGVFFTSMVLYKYTALGPFIRSLVSKKEKLRQT
TNKHLAEQWLQRTSEYMDSNSENSHYNFPYHSMQN
>gnl|CDD|240322 PTZ00232, PTZ00232, variable surface protein Vir27; Provisional
MFKDSQKENIKKLTSNFHYSYFERGIRGCENLNFYTNIKDELQGRYQLPGVSEKIVKALCYIYNTKKNKK
ETFNEDLCSYLYYWLGDKIYPNVHDKQVFSNIIKMIYDELYSTDLFIVCRPLYNKIDEDTFNKNKLLFDY
SKDYQNIRLSTLHAETTCDEHYKKVINKYINMYNDAYSDCNKINKKKYDCNKFSELFRNKLYKELSSLSC
KQSDPGTVSSDKTGDREQEGHSLSEIGSKXMTXFSXLHPATXRKPGRIXRSGAYLTHGSETPHELDTIET
IPVDDTAEGGSSKNIAGSVVPVLGVSSISLLLYKVTPVGGYINRLLGRNRNMYNPVEYMDAFNPYNDGMD
PGDRRMNISYHRL
>gnl|CDD|240323 PTZ00233, PTZ00233, variable surface protein Vir18; Provisional
MAWPFRGFNRIINLYQTYKTAPCMNTYSTLKSDIEQKIDDFNKATHTNIYTQWDQLNKYIITKDAELKHC
YDNGYINSDLNNDEKIKNFKSKCNNKGTCNNGAFPAKKPPLIKPTTQEPCKGGKGCKTETPQRVDTKSQS
KLRPVPSKAKSLEIKDPQEQSQNQADAQESNKESVVLQPQSDSMPSPSSIGTEDKEPQSIVNHHSTTSGM
GETQTQQLNASGDSPIRELDSSAGDPPSECVSGKESDLTCTSTGENLDTSLFQTNLSSGKTLDANHPETQ
DSAGNVIEVQTHGDKDIITEAADNLSSLEGTPGSVQLADEDSVDTDTDRGSTGAVASDPENTGTEETSSE
SLVSAPSGDVSNGGITEVDISNDDKAVDGESNGVEISHDQEHDSETICNESTCREEQNGELTDDGGDKLD
ILAQIFNVIQSNKNIIKTSMPIGIALLLGLLFKYTPLWRVLTKKNRKKGAGINEELNSVLQEPSIMDEER
SIPFSYSAFEYSSFDQNSY
>gnl|CDD|240324 PTZ00234, PTZ00234, variable surface protein Vir12; Provisional
MAKPAAASVISAEKLEKAAEELKLKTFYDDFFLKNEQPKSADPCKIFDTHDKKKENEKNICLKLVRHLEK
IGEITEKQKRDDHCNYLTYWFYDEIGKIYKDYSKKKEDISSFKDLIGVVNKVNVPQSRYPKCTLKSESGV
SLDEWKKRKLSYIYMKNYNDIKSKVFSQKKEKCDKYTKYLDNINKLYINYKTNKCGWFFGSTDYADCSTK
YNPNPLITELAKCKTQGSNGSQSSFLGWFWGSSSPKTAPSKGSPGAQEPAKTAVVKSPGGIPSAGGKRAG
AEGAGANKGLASVAPSQSREVLNGTQNPVPVAPLGSSQAGVHMPHGSKDIQQVSYTTLPTAPEVNPDTSN
FLEKTFGILKSEYFRHSIVGASIIGVLVFLFFFFKSTPIRSQTNKGEKKKRKPQNNYYDEYEEELPRYES
QQSLAESQMSDAY
>gnl|CDD|185521 PTZ00235, PTZ00235, DNA polymerase epsilon subunit B; Provisional
MFYDFENEKEKKEVEEYEIIVRKNDKRHNWIIMHDVYLDSPYTFEVLDKMLSLYVNTYPENELPVGFIFM
GDFISLKFDYNRNFHKVYIKGFEKLSVMLISKFKLILEHCYLIFIPGINDPCACKNSIPKMPILPYYIRK
FKQNIESFFSSKRNIIFATNPCRIRHLSKKMIFFRHDILNDLIWSSTINATNNERNNLQNILVSTIVGQS
HIYPIPHDNRILKRYSPFLFLYPLPHFICVCDNSCNSFISYASEDTSDCIISNSDMSFTRKKTFTVYSAL
HHEAKRYVVPL
>gnl|CDD|173487 PTZ00236, PTZ00236, mitochondrial import inner membrane translocase subunit tim17; Provisional
MQERDLSREPCPDRIIEDMGGAFSMGCIGGFIWHFLKGMRNSPKGERFSGGFYLLRKRAPILGGNFAIWG
GLFSTFDCTLQYLRGKEDHWNAIASGFFTGGVLAIRGGWRSAVRNAIFGGILLGIIELVSIGMNRRQMRT
PRQQFQQQQEMEKQLEEEDKKEQA
>gnl|CDD|240325 PTZ00237, PTZ00237, acetyl-CoA synthetase; Provisional
MYKLSDPFDYENDSNYANSNPESFWDEVAKKYVHWDKMYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVK
NPLKRDQDALIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARI
GATHCVLFDGYSVKSLIDRIETITPKLIITTNYGILNDEIITFTPNLKEAIELSTFKPSNVITLFRNDIT
SESDLKKIETIPTIPNTLSWYDEIKKIKENNQSPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHL
VGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGGIIKNKHIEDDLWNTIEKHKV
THTLTLPKTIRYLIKTDPEATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEIGIT
YLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPPSFATTFYKNDEKFKQLFSKF
PGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGL
LVLKQDQSNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDSNYQLPD
NVNDSEIFYKIKELYMK
>gnl|CDD|140265 PTZ00238, PTZ00238, expression site-associated gene (ESAG); Provisional
MKVTIVELVILLFFVICIDGAEEEGACTLVDDYEGDANLNESVCYLSCLSDALNKLYTDGERKLFVNEEV
YANASRILDDMEGKTGESVKYLSVISSVMEGEHDKLEKLISYGNAMGDLVAKVGGLFAEVNESVRAVRKE
IPDALIKANKYYTAIAEITRTVWDDVKAVESDDDAKCKNGEFKGVGEFKVKCGDHTCPLRNGVSESTLQK
YKDGCLEINVMSGSVSECLNLPRNNLYKSGAVKNSSDVLEWREDGATFFQLTLKVQDIFGPLIAPFAAGQ
PPSVLLDMMSNITSLYSHFNEVHSNFTSLLLDTNITDNVNSTNSTI
>gnl|CDD|173488 PTZ00239, PTZ00239, serine/threonine protein phosphatase 2A; Provisional
MDIDRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPN
ANYIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNPWRLFM
DVFDCLPLAALIEGQILCVHGGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYWAVNSRGAG
YLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYWFPDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTW
KTFKEVPESAKSINPKNVLPYFL
>gnl|CDD|140267 PTZ00240, PTZ00240, 60S ribosomal protein P0; Provisional
MPSITTAKREYEERLVDCLTKYSCVLFVGMDNVRSQQVHDVRRALRGKAEFVMGKKTLQAKIVEKRAQAK
KASAEAKLFNDQCEEKNLLSGNTGLIFTNNEVQEITSVLDSHRVKAPARVGAIAPCDVIVPAGSTGMEPT
QTSFFQALNIATKIAKGMVEIVTEKKVLSVGDKVDNSTATLLQKLNISPFYYQVEVLSVWDRGVLFTRED
LSMTEDVVEKMLMEGLSNVAAMSLGAGIPTAATIGPMLVDAFKNLLAVSVATSYEFEEHNGKELREAALE
GLLGGGGSAAAEAAAAAPAAASAAAKEEEEESDEDDFGMGALF
>gnl|CDD|240326 PTZ00241, PTZ00241, 40S ribosomal protein S11; Provisional
MADVQTERAFQKQEGVFQNSKRLLKKKTSKGVRYWKKVGLGFKTPKEAIEGKYIDKKCPFTGNVSIRGRI
LRGVVISTKMKRTIIIRRDYLHYVKKYNRYEKRHKNIPVHCSPCFDVKEGDIVVVGQCRPLSKTVRFNVL
KVEKNEIIGNVRKQFVLF
>gnl|CDD|185524 PTZ00242, PTZ00242, protein tyrosine phosphatase; Provisional
STLIECKDRQIEYVLFKFLILDAPSPSNLPLYIKELQRYNVTHLVRVCGPTYDAELLEKNGIEVHDWPFD
DGAPPPKAVIDNWLRLLDQEFAKQSTPPETIAVHCVAGLGRAPILVALALVEYGGMEPLDAVGFVREKRK
GAINQTQLQFLKKYKPRKKAAGCTIM
>gnl|CDD|240327 PTZ00243, PTZ00243, ABC transporter; Provisional
HETDEEELPIEMAPSQRSHPQPGTDNGHQSAPLHDYRTEHLELQERLAELWGPEAPYTPVPEETASWFQR
YYYGWVYEYVLLASKEQLTEEDLPPPTRDVRAHECGLRLSRAVQAAMYERNAWNCMVGAEVVSTLDASSR
GVLRWVGVPQQGGYTRMMAGVEWSVPPALRTAARSDDSGASPFFNGVAHGEHLFTPEQSNMSTLEEPTDV
RLYLSSTGSVVRPGPPPTPKRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNAT
WGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSLAQPDMNTGRIINMM
STDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKA
ADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVVFTV
YYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNATCSTVQDMEEYWRE
QREHSTACQLAAVLENVDVTAFVPVKLPRAPKVKTSLLSRALRMLCCEQCRPTKRHPSPSVVVEDTDYGS
PSSASRHIVEGGTGGGHEATPTSERSAKTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKS
TLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGG
GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATH
QVHVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLAAELKENKDSKEGDADAEVAEVDAAPGGAVDHE
PPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVS
SGVWLSMWSTRSFKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFD
TTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNS
ANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEF
LSNIVVTVIALIGVIGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEV
PHEDMPELDEEVDALERRTGMAADVTGTVVIEPASPTSAAPHPVQAGSLVFEGVQMRYREGLPLVLRGVS
FRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTV
RQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILM
DEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFH
SMVEALGRSEAKRFLQLVGR
>gnl|CDD|140271 PTZ00244, PTZ00244, serine/threonine-protein phosphatase PP1; Provisional
MSLVQTLIEKMLTVKGNRTQRQILIREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRI
FEKCGFPPYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYN
IKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEIERPCDVPDRGILCDLLWADPEDEVRG
FLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNI
DDKLQCSFLIIPAR
>gnl|CDD|140272 PTZ00245, PTZ00245, ubiquitin activating enzyme; Provisional
MRDAEAVRYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNY
LMQGEAGGTRGARALGALQRLNPHVSVYDAVTKLDGSSGTRVTMAAVITEEDAVPHVQAALPCADIVALH
VTCGPTVLALFLYRRLPAHSLAEQWRCLVAEPSLLAEKPRGYQRAVLALHVRTEAVSLGFAAAAAKAYEV
VSRLQLQQLTAADVQEVLQTCAHGAGSADCVSDTIAGACIAQHLIRQIGALNQPPDAQSYHWMLCECGAE
VECLVGL
>gnl|CDD|173491 PTZ00246, PTZ00246, proteasome subunit alpha; Provisional
MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDS
HIFCAVAGLTADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYD
ENLGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSPKADKI
EVGILSHGETDGEPIQKMLSEKEIAELLKKVTQEYAKENTNNN
>gnl|CDD|240328 PTZ00247, PTZ00247, adenosine kinase; Provisional
TSSAPKKLLGFGNPLLDISAHVSDEFLEKYGLELGSAILAEEKQLPIFEELESIPNVSYVPGGSALNTAR
VAQWMLQAPKGFVCYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVCGKERSLVANLGAA
NHLSAEHMQSHAVQEAIKTAQLYYLEGFFLTVSPNNVLQVAKHARESGKLFCLNLSAPFISQFFFERLLQ
VLPYVDILFGNEEEAKTFAKAMKWDTEDLKEIAARIAMLPKYSGTRPRLVVFTQGPEPTLIATKDGVTSV
PVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTYPEKPPFLPW
>gnl|CDD|240329 PTZ00248, PTZ00248, eukaryotic translation initiation factor 2 subunit 1; Provisional
EADLLDCRFYEQKFPEEDDLVMVKVVRITEMGAYVSLLEYDDIEGMILMSELSKRRIRSINKLIRVGRHE
VVVVLRVDKEKGYIDLSKKRVSPEDIEACEEKFSKSKKVHSIMRHIAQKHGMSVEELYTKIIWPLYKKYG
HALDALKEALTNPDNVFEGLDIPEEVKESLLQDIQRRLKPQPLKLRADIEVSCFDYEGIDAVKEALIAGQ
EVATDECKITIKLIAPPQYVIVTTCSDKDKGMEIIGAALEAIKEVIKKKGGDFKVKGEPEVVGGDEEDLE
ELLEKAEEEEEEDDYSESEDEDEEDEDEEEEEDDDEGDK
>gnl|CDD|140276 PTZ00249, PTZ00249, variable surface protein Vir28; Provisional
MATNPQYIKYQDYYIVKKSFDYTPTDEFNISFVNALIKDIRNTPTKEKLLYKTFYELKKFILRHHCFIRY
GKETCCNYINYWLNKTVRDSEYNVNKENFKIFDKFMQDDPKIKEGPFTCISKLSYMDTDSFQKMEKLYDL
YDYFTELKESKDSSTLCRNISDLAEKYESMMKEYNEKDNKLCDKLTNLKNVIEKDKLVAKNICTKNTFDS
FILKIDPPREEQKAVTAHAHRRISGEARPPKHISFSSPHAHGRPPVETRPPNPVSVSSPQAHGRHPGETH
TPPLVTVPSSKAHDRNPVQTPTPTSVSGYSSQAKGLEKQAGGESERTSSVPSEQFPLPLPVLLPLGQSGP
LESSESEETDEYAGPKGLPEPELELVELQEEDQRHGLKHDVDTFREDEEDTFLQEGDQPAGSMQSTFDTG
TIMGTIKGAVSNVLEAVEPVPVLGVSGGMGALYLLLKYTPIGSLFRRNRRNNQNIPNFFDPRYGEQFSGY
YPQYYNEGFPNYRMNIAYHPSSEELD
>gnl|CDD|140277 PTZ00250, PTZ00250, variable surface protein Vir23; Provisional
IHYLSIERSGDKEPANKETYSIIKNLNLYDFYEKLDNELDKKIEETPEIDDKCDHCKGHIASDAENGAEL
IDLCKKCCNIILNVHGILDKCKDRDDKKACQYMEHWLYDKVTRITEEQNIFIKFYALLSMYSSFKKDNFK
NCSLKNFAIDKEAFDIKHILYEFIEIYDDIKNEIDNENKLNTKLYCKHIKENFLFYNIIKEECKSKDSCD
YFDELIEFKEKFKEPDVINFICEKCDYIKTSCKHGSNGEDDVPCLQAKGIPFILPIFGNDADDIINILLK
VAIISAPFLAIFLILFKFTPFGKKLNKIKAEGKKSGHKKKEENIEDYMKNYAAHLDNEMKNRVHLGYHAS
>gnl|CDD|140278 PTZ00251, PTZ00251, fatty acid elongase; Provisional
MQWLDNYGINHYDGHAVQKWLASNVDICVYIAAAYLTFVFKGPQLVDAIFHGNPPVPLIKKCWALWNIGL
SVFSMYGVYRVVPPLLNNLRKYGLHDTLCTFREDEFYTGKVGVAMGLFSISKVPEFGDTFFLIMGGKKLP
FLSWFHHVTIFLYAWMSYQQGSSIWICAAAMNYFVHSIMYFYFALSEAGFKKLVKPFAMYITLLQITQMV
GGLFVSGYVIVQKLTKGDPKGCSGTTMATARGQLMIYIFNFYLFSEMFVKGYVLPRKAKAGD
>gnl|CDD|240330 PTZ00252, PTZ00252, histone H2A; Provisional
MATPKQAKKKASKSGSGRSAKAGLIFPVGRVGSLLRRGQYARRIGASGAVYMAAVLEYLTAELLELSVKA
AAQQAKKPKRLTPRTVTLAVRHDDDLGSLLKNVTLSRGGVMPSLNKALAKKHKSGKKAKATPSA
>gnl|CDD|140280 PTZ00253, PTZ00253, tryparedoxin peroxidase; Provisional
MSCGDAKINHPAPSFEEVALMPNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELN
CEVLACSMDSEYAHLQWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLR
QITVNDMPVGRNVEEVLRLLEAFQFVEKHGEVCPANWKKGDPTMKPDPNKSKEGFFSKA
>gnl|CDD|240331 PTZ00254, PTZ00254, 40S ribosomal protein SA; Provisional
VSSGPKVLTPKEDDIKKMLACKCHIGTKNLENAMKKYVYKRTKEGVHIINLAKTWEKLKLAARVIAAIEN
PADVVVVSSRPYGQRAVLKFAQYTGASAIAGRFTPGTFTNQIQKKFMEPRLLIVTDPRTDHQAIREASYV
NIPVIALCDTDSPLEYVDIAIPCNNRGKESIALMYWLLAREVLRLRGTLPRDEEWDVMVDLFFWRDPEEA
EEKEEAAAETAGVEDAAAAAAEAEEGEEWVAAANNEWEN
>gnl|CDD|240332 PTZ00255, PTZ00255, 60S ribosomal protein L37a; Provisional
MAKRTKKVGITGKYGTRYGASLRKQIKKIEISQHAKYFCPFCGKHAVKRQAVGIWRCKGCKKTVAGGAWT
LSTPAASTVRSTIRRLRKLK
>gnl|CDD|173495 PTZ00256, PTZ00256, glutathione peroxidase; Provisional
MGSLLFKKGLEQIQPPTKSFFEFEAIDIDGQLVQLSKFKGKKAIIVVNVACKCGLTSDHYTQLVELYKQY
KSQGLEILAFPCNQFMEQEPWDEPEIKEYVQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNNTN
EARQIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQDIEKLLNA
>gnl|CDD|240333 PTZ00257, PTZ00257, Glycoprotein GP63 (leishmanolysin); Provisional
MPLDSSSTHRRRSVAARLMRLAAAGLVMAVGAAAVWAQAAGHHCIHDKLQARVLQSVAQQRSPPVSVSAL
GLPYVSAGTISSAHTVDWALADSTSPSVVRAADWGTLRIAVSTADLTDPDYHCTRVGQRVSNHAGAFVTC
TAEDILTEEKRDILVSYLIPQALQLHVERLRVRQVQGSWRVTGMTGPICGDFKVPKAHVTVGVSNADFVL
YVASVPSEPGVLAWATTCQVFSDDHPAVGVMNIPAANIVSRYDQGTTRTVTHEVAHALGFSSVFFENAGI
VKSVTNLRGKPFAAPVINSSTAVAKAREQYGCPTLEYLEVEDQGGSGSAGSHLKGRNAKDELMAPASAAG
YYTALTMAVFEDLGFYKADFSMAEVMPWGRNASCDFLTNKCMEDNITQWPEMFCNTTERRYRCPTDRLKL
GTCGIRTYSTPMPTYFQYFTNAFLGGFSAFLDYCPFIVGYSNGACNQDPSTASPSLKEFNVFSDAARCLD
GVFQPRNSNARSEPNNALCANVMCDTAARTYSVQVRGSSGYVACTPGESIDLATLSAAFVEGSYITCPPY
VEVCQANIKGVIDFERDAADTAAMRQWSERMTALATVTAVLLGIVLAAMAGLVVGLLVISLS
>gnl|CDD|240334 PTZ00258, PTZ00258, GTP-binding protein; Provisional
MPPKKKMEEEKKVLLGRPGNNLKMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERF
DWLCKHFKPKSIVPAQLDITDIAGLVKGASEGEGLGNAFLSHIRAVDGIYHVVRAFEDEDITHVEGEIDP
VRDLEIISSELILKDLEFVEKRLDELTKKRKKKKKKKEEKVELDVLKKVLEWLEEGKPVRDGDWTDKEIE
ILNEYQLLTAKPMIYLVNMSEKDFIRQKNKWLAKIKEWVGEKGGGPIIPYSAEFEEELAELGSEEERKEY
LEEYGIKQSMLDKIIKTGYKLLNLIHFFTAGPDEVRCWTIQKGTKAPQAAGVIHSDFEKGFICAEVMKYE
DFLELGSEAAVKAEGKYRQEGKDYVVQDGDIIFFKFNVSK
>gnl|CDD|240335 PTZ00259, PTZ00259, endonuclease G; Provisional
MKSAIVRLLGAAIVTAIGAKVYWTLLGQNSKSAQLPVSPGQSVNSAIKYLSSTLSKGSDGVVKSVVSGNA
LKKVTELPPPYPSEQASTARADTLPFCKEYPSFGLPSTENLRLYEGYVSSLNYERRIPNWVAEYIPYRGI
SVEAGEKKANRADCVFYADPTVPEAFRAENKDYTGSGYSRGHLAAAGFHKASQTAMDDTFLLSANIVPQD
LTNNAGDWLRLENLTRKLAREYEVGVYVVSGPLFVPRYMREKLRKWRLAEPSEIHKPDSPADKTPKKVVT
YEVIGDNNVAVPTHLFKVILAEKNDGPPHEVAAFLMPNEPISKEKPLTAYQVPLEEIEKLTGLQFFPKLD
AFTKLPNLCKESRCEARTSARFQSWRQVGQLRAAKSIPELQQEYTTLNIEKMVTASGITDKLDELVVREY
ENRLKELGDRAEAF
>gnl|CDD|240336 PTZ00260, PTZ00260, dolichyl-phosphate beta-glucosyltransferase; Provisional
KGNIWKVIFKHRMLIVLGLVVGLALLFYPYISWPDDDKVIRQVKSSVIHEKSKEVDKENYINNILKDSDV
DLSIVIPAYNEEDRLPKMLKETIKYLESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINPNIDIR
LLSLLRNKGKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQNGLGIVFGSRNHLVDSDV
VAKRKWYRNILMYGFHFIVNTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLP
IAEVPVNWTEVEGSKLNVISASIQMARDILLVRSFYLLGIWKVKDPSLLGRPC
>gnl|CDD|240337 PTZ00261, PTZ00261, acyltransferase; Provisional
MGAAVARVVHETAARLPHLMGSNSGALLAVALAIWYVLLRQRLVPVKLMRKWFLLVNTATILPVSALTKL
IDQLGRLGVPTYCVQRLCIIPLVVAFRAVWWLNPQIRMHLCFDADEHGKPLSWDDISRHGCAYVGNHTSF
WDVYAFIGLTPFRHLLNTRTLMKSSLRKIPIFGGVFDRVGHFPVHFKSDSDGNFEVDKEKQAQVQQAIDA
HLRLGGSLAFFPEGAINKHPQVLQTFRYGTFATIIKHRMEVYYMVSVGSEKTWPWWMMIGGLPADMHIRI
GAYPIDYDRDSSKDVAVGLQQRMQKVRDEIAAEVAAAEEARRRRRGIVAEAKASKTLDIAPPHAAREAHA
TRATA
>gnl|CDD|240338 PTZ00262, PTZ00262, subtilisin-like protease; Provisional
MTIRKYHCAFVCLLLFGMVKNLSVERDVTSRRKHNTARNDDGEKIGSELRFLGKVERGAETSNLRGEGVE
ADVNSSNPDSASPKEELQKIQGQQESSPPQVSHLLQDDSHNMDEMKTKLRKKKKILRLIVSENHATSPSF
FQESLLEENVVSFLGSKGRLSNLKNIHSYIIELFSDITDRELKNYIQLLESKGALIESDKLVHADEIGIC
GIKDAVRRGEDRVIWESGMDDMIPIKEEGHIRGEAPVRNGNSLRGNSSNYDDHPGSDGSFSLSNQMAFNN
FLGKYQFNDEGRNLQWGLDLTRLDETQELIEPHEVNDTNICVIDSGIDYNHPDLHDNIDVNVKELHGRKG
IDDDNNGNVDDEYGANFVNNDGGPMDDNYHGTHVSGIISAIGNNNIGIVGVDKRSKLIICKALDSHKLGR
LGDMFKCFDYCISREAHMINGSFSFDEYSGIFNESVKYLEEKGILFVVSASNCSHTKESKPDIPKCDLDV
NKVYPPILSKKLRNVITVSNLIKDKNNQYSLSPNSFYSAKYCQLAAPGTNIYSTFPKNSYRKLNGTSMAA
PHVAAIASLILSINPSLSYEEVIRILKESIVQLPSLKNKVKWGGYLDIHHAVNLAIASKHGRTEIAKSQS
WFRWKKRVR
>gnl|CDD|140289 PTZ00263, PTZ00263, protein kinase A catalytic subunit; Provisional
MKAAYMFTKPDTSSWKLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKS
ILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDII
YRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIA
GYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTDHTKRLGTLKGGVADVKNHPYFHGANWD
KLYARYYPAPIPVRVKSPGDTSNFEKYPDSPVDRLPPLTAAQQAEFAGF
>gnl|CDD|173500 PTZ00264, PTZ00264, circumsporozoite-related antigen; Provisional
MKLLSAVFLLFCAILCKHALGENTNGTGSGVPKKKKPKSKSPEPLIDVHELISEMVRKEEELVNVTKKKS
KYKLATTVLASALGVVSAVLLGGAGLVFYNAGNGRHPFSLGGGKGGDAAPPEADPESNGPPNAGPQVTAQ
DVTPEQPQ
>gnl|CDD|240339 PTZ00265, PTZ00265, multidrug resistance protein (mdr1); Provisional
MKKDQRQKKDNNSGGGNLSIKDEVEKELNKKGTFELYKKIKTQKIPFFLPFKCLPASHRKLLGVSFVCAT
ISGGTLPFFVSVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSV
FYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLI
YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFME
SLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFHGGSVISILLGVLISMFMLTIILPNITEYMK
SLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGES
GCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDL
EALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKKVLIHD
FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEN
RITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNA
GSYIIEQGTHDALMKNKNGIYYTMINNQKVSSKKSSNNDNDKDSDMKSSAYKDSERGYDPDEMNGNSKHE
NESASNKKSCKMSDENASENNAGGKLPFLRNLFKRKPKAPNNLRIVYREIFSYKKDVTIIALSILVAGGL
YPVFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENIL
YQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFI
FMRVFAIRARLTANKDVEKKEINQPGTVFAYNSDDEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEK
AIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLM
SLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFS
CDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSL
TKEGGSGEDSTVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKR
ACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT
IVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTGSFVQAHGTHEELLSVQDGVYKKYVKLAK
>gnl|CDD|173502 PTZ00266, PTZ00266, NIMA-related protein kinase; Provisional
MPGKYDDGESRLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELK
HKNIVRYIDRFLNKANQKLYILMEFCDAGDLSRNIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNLKDG
PNGERVLHRDLKPQNIFLSTGIRHIGKITAQANNLNGRPIAKIGDFGLSKNIGIESMAHSCVGTPYYWSP
ELLLHETKSYDDKSDMWALGCIIYELCSGKTPFHKANNFSQLISELKRGPDLPIKGKSKELNILIKNLLN
LSAKERPSALQCLGYQIIKNVGPPVGAAGGGAGVAAAPGAVVARRNPSKEHPGLQLAAMEKAKHAEAANY
GISPNTLINQRNEEQHGRRSSSCASRQSANNVTNITSITSVTSVASVASVASVPSKDDRKYPQDGATHCH
AVNGHYGGRVDKDHAERARIEKENAHRKALEMKILEKKRIERLEREERERLERERMERIERERLERERLE
RERLERDRLERDRLDRLERERVDRLERDRLEKARRNSYFLKGMENGLSAGGGPGDGPGVGAGVGAGVGTS
DGRNHSGVRSGIHCSIQSSARGGVHDSVRSGVHDSVRGGVHDSMRSGVHDSLRGGVHDSIRGGAHDGVRS
GAHDGVRKSSGVKVEGMGNARAPPPNQGTHDGNFSRGKDSSDHVSSYKPYAYDSRKAKNYQDTFDRNDMH
GYMKNSPISTIVPSSHMMHTKGNTGMNVNCKYLGGAAYGGYSNNHAATGPYIGNPMESTKYRDHNKYSVG
GLAKNAKEMYKEAVNPICSAEAHYERVYNHGNRGGHAHSGSGRGGDGGRSIDGGRSIDGGRSIDGGEGGD
ERDGGTCKSNRVSNIYFNDNARRSVSALPHMNAINAKKASIYNNTCDEGTLSKKGGEVDRSYKHLEKDRE
YLLEKRKMLMEKEKGIYDRLRHNNDYAYAPARAFDRGEDKKPNELDRRNRSLSMCMNEQEKRRDSATYNA
KKEYHDEEERAELANSYTLQKRNMYALKNFAHKGPDAYTCR
>gnl|CDD|140293 PTZ00267, PTZ00267, NIMA-related protein kinase; Provisional
MPNNEVEHGSASAELLNQYAKYFPHVLFTSEEAFEKYCADLDPEAYKKCVDLPEGEEVPESNNPREHMYV
LTTLVGRNPTTAAFVATRGSDPKEKVVAKFVMLNDERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKL
LLIMEYGSGGDLNKQIKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKL
GDFGFSKQYSDSVSLDVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIM
QQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFLKYVANLFQDIVRHSETISPHDREE
ILRQLQESGERAPPPSSIRYGVVTSDVTHGGYLYKYSSDMRWKKRYFYIGNGQLRISLSENPENDGVAPK
SVNLETVNDVFPVPEVYSQKHPNQLVLWFNNGQKIIAYAKTAEDRDQWISKFQRACGM
>gnl|CDD|140294 PTZ00268, PTZ00268, glycosylphosphatidylinositol-specific phospholipase C; Provisional
MLPESDDFTNTAWHPQSWMHDLRSFIGEMAITQVCLVGSHNAASYGIHKDSPFGADAPGFLLGDSVVASL
SRFLFRGISASWSKCQGMSVRAQLDHGVRYLDLRVATNPEDANRLYISHTQISVPLADVLEDVKAFLNDP
SSANEFIVLDFQHLYLTDDSDGKGKFFRELDRLSDRFIPVDVPLTTPLEILWRVSRRRRIFLVVASGRNY
VPYPAARIRSKCMVSRWVNQMSLRKLLQALENLLLDDLKYPQTGVPSKLYVTQAVYTPRNSDIFRGIFPK
ISRKVVSSIYDVAKRKNPSLLEWFYLLNANGLLDGAKVMIPSGINTHGNILMLDCVELGRCQIMDGTTET
NAVGMCVYLNILRASRLREDSSAAPSLNEG
>gnl|CDD|140295 PTZ00269, PTZ00269, variant surface glycoprotein; Provisional
MYWVVFLVAVLQGIHLVSGQEDIVNQQEFEALCRMINWAERGLKHIKLAKQVTQEALKIGVRYLEVAGEE
EAAELAKAQEDSCTKKMEDRKRNCGLYKTFWEEAQEALKERTARSEAPHRKRNSLQYHTAEEIKKKVMEV
ADIYHEVEAESLSGKVEKMEEQLNQALYGMEYFTEEIKGGDDRSRVCGQNLRNEMATGGWSLAVDLLCLC
AMHSSWKGRKVCCADCTTGENSNEWNPESNGAPRWEFLKQKCAGRNTNYHDTGERLREAKQNFMDTVTKI
GTIPYTTLYKLGEKQNSEIKDCGADINKGQGICVLYGSDNGVNLPWMKALEKVENEMEVLLQDKQDKSAK
LERIKELSQEIESLIKGDTGRGGQRGRQKRSVDTENSVPETPADPSDPTQSTTHTNEKKRSVRKPISTGN
GASKSYGGDEVDSYDSKCDGENSACSDSPAKPTVKSSKSAINCPLGLILLLV
>gnl|CDD|240340 PTZ00270, PTZ00270, variable surface protein Vir32; Provisional
MGGSLLSGGLDQYFIELSLWLPSDKFYNKLDHSVENLRKYNDVCTSLCSINKKFANRRLCAIVLRYLENT
YKKSENENSAYDDCILFNYWIYGKLYEQYKYNYNSAIYHSFGELQSVWNDLIKDSSKTSYYDKCQPDFHI
VMKDDWKKRKELYDYCVNYETLKGIVPFYDTNCREIYTYLKDKAVLYKEFKTHCSSTDENMCPKFYAKCN
EYDPDIVLKKLSCYEEMRKEEALALEQQASVEPDPGLTADGASSPDNSQLAGDGTNPVTKSGNVLLGVVA
TSMTSGALYKFTPLGRMLRNGFGWNRNMRNINGHDNGLFDYAPESFNPYSGGG
>gnl|CDD|140297 PTZ00271, PTZ00271, hypoxanthine-guanine phosphoribosyltransferase; Provisional
MSNSAKSPSGPVGDEGRRNYPMSAHTLVTQEQVWAATAKCAKKIAEDYRSFKLTTENPLYLLCVLKGSFI
FTADLARFLADEGVPVKVEFICASSYGTGVETSGQVRMLLDVRDSVENRHILIVEDIVDSAITLQYLMRF
MLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGYGMDYAESYRELRDICVLKKEYYEKPESK
V
>gnl|CDD|240341 PTZ00272, PTZ00272, heat shock protein 83 kDa (Hsp83); Provisional
MTETFAFQAEINQLMSLIINTFYSNKEIFLRELISNASDACDKIRYQSLTDPSVLGESPRLCIRVVPDKE
NKTLTVEDNGIGMTKADLVNNLGTIARSGTKAFMEALEAGGDMSMIGQFGVGFYSAYLVADRVTVTSKNN
SDESYVWESSAGGTFTITSTPESDMKRGTRITLHLKEDQMEYLEPRRLKELIKKHSEFIGYDIELMVEKT
TEKEVTDEDEEDTKKADEDGEEPKVEEVKEGDEGKKKKTKKVKEVTKEYEVQNKHKPLWTRDPKDVTKEE
YAAFYKAISNDWEDPAATKHFSVEGQLEFRSIMFVPKRAPFDMFEPNKKRNNIKLYVRRVFIMDNCEDLC
PDWLGFVKGVVDSEDLPLNISRENLQQNKILKVIRKNIVKKCLEMFDEVAENKEDYKQFYEQFGKNIKLG
IHEDTANRKKLMELLRFYSTESGEEMTTLKDYVTRMKAGQKSIYYITGDSKKKLETSPFIEQARRRGLEV
LFMTEPIDEYVMQQVKDFEDKKFACLTKEGVHFEESEEEKQQREEEKAACEKLCKTMKEVLGDKVEKVIV
SERLSTSPCILVTSEFGWSAHMEQIMRNQALRDSSMAQYMMSKKTMELNPRHPIIKELRRRVGADENDKA
VKDLVFLLFDTSLLTSGFQLEDPTGYAERINRMIKLGLSLDEEEEEAAEAPVAETAPAEVTAGTSSMEQV
D
>gnl|CDD|140299 PTZ00273, PTZ00273, oxidase reductase; Provisional
MTRASLPVIDVSPLFGGESAEKMRVAKQIDEACRTWGFFYIVGHPIPQERIEKVLKMAKTFFSLPMEEKL
KIDIRKSRLHRGYGAFGAEQLDPSKPYDYKETFDMGCHLPKDHPDVMAGKPLRGPNNHPTQVEGWMELME
THYRDMQALALVLLRALALAIGLREDFFDSKFMEPLSVFRMKHYPALPQTKKGRTVCGEHTDYGIITLLY
QDSVGGLQVRNLSGEWMDVPPLEGSFVVNIGDMMEMWSNGRYRSTPHRVVNTGVERYSMPFFCEPNPNVI
IKCLDNCHSEENPPKYPPVRAVDWLLKRFAETYAYRKSKM
>gnl|CDD|140300 PTZ00274, PTZ00274, cytochrome b5 reductase; Provisional
MRFVVSFVAGAVGAWVWRPLDSGQDAECYRSIENALHFRNKPRPGRVFSQRYEPYQLGEVIPITHDTALF
RFLLHSEEEFNLKPCSTLQACYKYGVQPMDQCQRFYTPVTANHTKGYFDIIVKRKKDGLMTNHLFGMHVG
DKLLFRSVTFKIQYRPNRWKHVGMIAGGTGFTPMLQIIRHSLTEPWDSGEVDRTKLSFLFCNRTERHILL
KGLFDDLARRYSNRFKVYYTIDQAVEPDKWNHFLGYVTKEMVRRTMPAPEEKKKIIMLCGPDQLLNHVAG
TPMGTMSSMSSGMNIQPMAPDLNNLVSLGGILGELGYDNDDVYRF
>gnl|CDD|185536 PTZ00275, PTZ00275, biotin-acetyl-CoA-carboxylase ligase; Provisional
MEDPPKAFERFYPELNALRLHFDVLDSTQLYCKRNMKRFIQNGKLQDDNMIIVSCNEQTNGIGTRDTKKN
QDRIWLSEKGNLFTTFVFLWNRNDIEKVKYLAQTCTVAISKTLEYFHLVTQIKWINDVLVNYKKIAGCLV
HLYYLDDFPNLNSRYVCVMVGIGINVTLEDKHNLLNNNYTSIKKELQRDFNTPKSIPSVEQVTEKLIINL
KAVINKLRKEGFSSFLDYITPRLLYKDKKVLIDQDNELIVGYLQGLLHDGSLLLLREKNKLVRVNTGHLR
LKDDD
>gnl|CDD|140302 PTZ00276, PTZ00276, biotin/lipoate protein ligase; Provisional
MPADVPPNIHFVGEVTSTMDVARTMLAAAGGKPFAVLAESQTAGRGTGGRTWTSPKGNMYFTLCIPQKGV
PPELVPVLPLITGLACRAAIMEVLHGAAVHTKWPNDIIYAGKKIGGSLIESEGEYLIIGIGMNIEVAPPV
TDAGRESTMVNEIAEDLGVKSVTPQDLAEAVWKHFFDICSDPELTREILIESFDAAMDKSLKLHKRTPTG
RDPEELTALSLNEWGHLIVRRPDGTEEDLMAEYLF
>gnl|CDD|240342 PTZ00278, PTZ00278, ARP2/3 complex subunit; Provisional
MATTYQPYYDCIRKTLEAALCLGNFPSQIIERHNKPEVELNGYEGKSKELVLNPIYIVRSEKEKCLIEPS
INSVRISFSFKKSDELDVIIARKFVSFLAQRAEQFVILRRKPIPGYDISFLITNFHTENMFKHKLIDFII
DFMEDIDKDISDMKLNVNTRARIAAPEFFKALAN
>gnl|CDD|240343 PTZ00280, PTZ00280, Actin-related protein 3; Provisional
ASTLPVVVIDNGTGYTKMGYAGNTEPTYIIPTLIADNSKQSRRRSKKGFEDLDFYIGDEALAASKSYTLT
YPMKHGIVEDWDLMEKFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQA
VLALRASWTSKKAKELGGTLTGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGE
PIPAEDILLLAQRIKEKYCYVAPDIAKEFEKYDSDPKNHFKKYTAVNSVTKKPYTVDVGYERFLGPEMFF
HPEIFSSEWTTPLPEVVDDAIQSCPIDCRRPLYKNIVLSGGSTMFKGFDKRLQRDVRKRVDRRLKKAEEL
SGGKLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDEYGPSICRYNNVFHSV
>gnl|CDD|173506 PTZ00281, PTZ00281, actin; Provisional
MDGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKY
PIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAV
LSLYASGRTTGIVMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIV
RDIKEKLAYVALDFEAEMQTAASSSALEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTY
NSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAPSTMKIKIIAPPERKYSVWIGGSILASL
STFQQMWISKEEYDESGPSIVHRKCF
>gnl|CDD|240344 PTZ00283, PTZ00283, serine/threonine protein kinase; Provisional
MMASGDAMIGRVCRTFPDTFAKDEATAKEQAKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGM
SEADKNRAQAEVCCLLNCDFFSIVKCHEDFAKKDPRNPENVLMIALVLDYANAGDLRQEIKSRAKTNRTF
REHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAATVSDDVGRTFCGTPY
YVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDPLPPSISPEMQEIVTAL
LSSDPKRRPSSSKLLNMPICKLFISGLLEIVQTQPGFSGPLRDTISRQIQQTKQLLQVERRRIVRQMEES
LSTAASTTILEGATPLTTLGGLTLYEGIVKKQSSDLSWKRRYLCIRGELEKGETLTVDVAPKFKSLDLVL
AVSKDTLEQQCISTPFSDLEDVFPVPSKYTGSNAAHVFAVAFKTGRRLLFQARSDPERDAWMQKIQSVLG
IGDADD
>gnl|CDD|140307 PTZ00284, PTZ00284, protein kinase; Provisional
MDTRAAGLSAARAGLYQYTSGAPVNALSGNSPKANNSASTGQTTSRSTNSARRSGSKRDRETATSTDSGR
TKSHEGAATTKQATTTPTTNVEVAPPPKKKKVTYALPNQSREEGHFYVVLGEDIDVSTQRFKILSLLGEG
TFGKVVEAWDRKRKEYCAVKIVRNVPKYTRDAKIEIQFMEKVRQADPADRFPLMKIQRYFQNETGHMCIV
MPKYGPCLLDWIMKHGPFSHRHLAQIIFQTGVALDYFHTELHLMHTDLKPENILMETSDTVVDPVTNRAL
PPDPCRVRICDLGGCCDERHSRTAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKLLYDTHDN
LEHLHLMEKTLGRLPSEWAGRCGTEEARLLYNSAGQLRPCTDPKHLARIARARPVREVIRDDLLCDLIYG
LLHYDRQKRLNARQMTTHPYVLKYYPECRQHPNYPDNRSMLRPTPIM
>gnl|CDD|140308 PTZ00285, PTZ00285, glucosamine-6-phosphate isomerase; Provisional
MRIVISEDADAVADYTSNYIIKRINDFKPTSDRPFVLGLPTGSTPLPTYQELIRAYREGRVSFSNVVTFN
MDEYVGLPRDHPQSYHYFMKENFFDHVDIKEENRHILNGTAPDLEEECRRYEEKIRAVGGIDLFLAGIGT
DGHIAFNEPGSSLDSRTRVKSLNQETIDANARFFGNDISKVPTMALTVGIRTIMEAREVLLLATGASKAI
AVARCVEGGVTHMCPASALQMHPAAVLCLDEDATLELKVKTTK
>gnl|CDD|185539 PTZ00286, PTZ00286, 6-phospho-1-fructokinase; Provisional
TCEIERVNNLIIDLPDAPLPSVVNPDLGECNLRGVFGGNGFLPREAFVDTNSYILSTPRFGPDDVIVNTK
RWLRAGPRKHLYFNPKEVKAGIVTCGGLCPGLNVVIRELVMNLINNYGVKTIYGAKYGYKGLYKEDWIKL
DPKDVKTIHRLGGTILGSSRGGFDPKVMVDTLIRHGINILFTLGGDGTHRGALAIYKELRRRKLNISVVG
IPKTIDNDIPIIDESFGFQTAVEEAQNAIRAAYVEAKSAKNGVGIVKLMGRDSGFIALHASVASADVNVC
LIPEFDIPLEGVLEYIEQRLQKKGHCVIVVAEGAGQSLKDADLDLGTDASGNKKLWDIGVYLKDEITKYL
KKKKPEHTVKYIDPSYMIRAVPANAADAKFCTQLAQNAVHGAMAGFTGFIIGHVHNNYVMIPIKEMSGNY
RRRVNPEGRLWQRMLAITGQPSFLNNEEIERHQRRQLES
>gnl|CDD|240345 PTZ00287, PTZ00287, 6-phosphofructokinase; Provisional
MDNKNGDKNEAKKPSADGLVKTMSVLLRDNECAFNIEENEDQNSKDQLPCDKKDSEMIDCLMQKLTSKKF
LVEKETKNSFYLVDNENMKIKKLKEHGHSASLNDDLSPLQYERIKYQPTLPKALASEYQILEENHGDDFI
NKKDYEEVKRFLKNLHNLPILNVKETNNHESFKGGNVLKIGIILSGGPAPGGHNVISGIYDYAKRYNEQS
QVIGFLGGIDGLYSKNYVTITDSLMNRFRNLGGFNMLWSGRGKVRNKDDLIAIENIVAKLKLNGLVIIGG
DGSNSNAALISEYFAERQIPISIIGIPKTIDGDLKSEAIEISFGFDTATKTYSEVIGNLCTDVKTGHNVY
HVVRVMGRSASHVVLECALQTRPNIVLIGEEVEKENLSLKDIVSNIVNTILKRRSLNKNYGVILIPEGLI
EFVPEMKILIGELNVILKEGPFDASKLKHSREVWDFLPSIIRDQLLMDRESTGYIQVGKIATERLIIVLV
ESELAKLNDNNLNIQFMAHYLGYEGRCAIPSNFDCNYCYALGYNAALLIDHKKTGYMSIIQNLEDSYANW
IPAAIPFLRIMHVNRDNTGKEFPAVKRYLVDLNSPLFNVLKEVRSLWSLYDLYRSPGPIQFNGHLSNSRC
YTVKIPTKDNLLCQNSDDLQLIINLANKNNHEGNGDNGGSSETSGAKQMDLSGSDDNNQSKGNELGAVSA
TYNGTHEKSLSGNTTLLGTAYSGNGAGKNILNPDSNSEDVLNSEPVNNGFYEQHCSSYKSLGCMSELQTS
RLYNKLELPELCSDLKAKVRAGKQYISNDPYTQKQILSNYPHMSYENKFQIQEIFHDKYATPISFEIKIG
IVFLSRQAPGAMNVLCGLYRRLKLLKGVCIAFYGLYGLLNNKYIIIDDDNIAKHVNQGGLELTGNSPEHS
LFDKENRNKVCETVTNLQLNGLVMPGSNVTITEAALLAEYFLEKKIPTSVVGIPLTGSNNLIHELIETCV
GFDSSTKVYASLIGNVLTDAVSMPKYWHFIRLMGRSPSHEVLECALQTHPNMVIISEEYGAADKTLWRVV
QDIADVVCARAELGKNYGTVLIPDALLMHLPHMKILLSEISDILNDANEKGQLVEARNDLVNLSTTQHGH
LGSTAGTVAGAEQPLSASPWVSKLTPWSLALLKTFPQFIIKELLHVDLRSMRFEKLETEQLLLQMVKEEL
HQRKQKGKYSGSFMGLTHFFGYQGRSSLPSEFDCKLAYSYGHAASIVIESGLTGYIVSIRGLCGNIKDWK
LFAIPFISLMKILPRGQGSKYLKSASKGDLPVIPSAPVDLNGKAYRSLKIALQKWQMEDRFCNPGPIQFE
GNASNYYNRILFEEQSEYFEMLRYVECYANILKDTCRFGVSADYLKNVFVQLCGMLVLAYKPNDILSNMP
YIGSIEDYYDWENQRKRMD
>gnl|CDD|240346 PTZ00288, PTZ00288, glucokinase 1; Provisional
MVVTDEIFLEQLAEELKTDASWSSGPIFVGCDVGGTNARVGFAREVQHDDSGVHIIYVRFNVTKTDIREL
LEFFDEVLQKLKKNLSFIQRVAAGAISVPGPVTGGQLAGPFNNLKGIARLTDYPVELFPPGRSALLNDLE
AGAYGVLAVSNAGRLSEYFKVMWKGTQWDALSEGKPAGSVIGRGRCMVLAPGTGLGSSLIHYVGVSDQYI
VIPLECGHLSISWPANEDSDYVQALAGYLASKALSKGIDSTVYPIYEDIVSGRGLEFNYAYEKRGNKPSA
PLKEAAEVAKLAKYGSDVAAVKAMKRHYKYLMRLAAEISMQFLPLTVVLMGDNIVYNSFFFDNPENVKQL
QARITEHKMERLKFLSRTTFLRQKKSVNLNLLGCLQFGSQLSHLKDQHAPTKSSL
>gnl|CDD|240347 PTZ00290, PTZ00290, galactokinase; Provisional
MPAESYSDERLDSTLSTLKPIFLETFKVENDADVEWLLFTFAPGRVNFIGEHVDYMGGYVCPAAVLEGCH
ILVGRVKHFCDHKLRFATETDEHFVLDHLGGAKHNKAWTTFVRGAATLRLNRLGVAIDAPSLQGVCMVVH
GTLPMGAGMSASASFGVALLNAINTVVTRRYKGCPTSPGRRYSILPPMSKEELIELAKQARRIETEFCGV
NVGIMDQFISAFAEEDKFMFLDCKSLTFESHDMTPLLGDGACFLLIDSMIKHDLLGGTAGMYNTVRSDQE
GAQKKIGKHRYRGKPFTFSDLVRNPKKYTFDGDVVAFMESCKPLMTPGEFERGTYNIMEQIRTLEFIKLN
DPELPLSREERFRKAGEILNAGHQGMRDLMKITTPELDFIHELINEEKGVAGGRMMGGGFGGCIILLLKK
NAVDRVVAHVREKFKARFGVENDVYPVVAGDGAFVVSLKNWSGAGSKL
>gnl|CDD|185541 PTZ00292, PTZ00292, ribokinase; Provisional
MHRAGEVASHGGEAEPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVA
MVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMIFVDTKTGNNEIVIIPGANNALTPQMVDAQ
TDNIQNICKYLICQNEIPLETTLDALKEAKERGCYTVFNPAPAPKLAEVEIIKPFLKYVSLFCVNEVEAA
LITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGSM
AYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSELPADVKE
>gnl|CDD|185542 PTZ00293, PTZ00293, thymidine kinase; Provisional
MYRGTISVIIGPMFSGKTTELMRLVKRFTYSEKKCVVIKYSKDTRYSDEQNISSHDKQMLKAIKVSKLKE
VLETAKNYDVIAIDEGQFFPDLVEFSEAAANLGKIVIVAALDGTFQRKPFGQILNLIPLAERVTKLTAVC
MFCGKEASFSKRIVQSEQIELIGGEDKYIATCRKCFRTKQLAEKELEKQDLVEFADFSNEENIFNQQNNA
C
>gnl|CDD|240348 PTZ00294, PTZ00294, glycerol kinase-like protein; Provisional
MKYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGP
SFKIKAIGITNQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGSNFFQKITGLPISTYFSAF
KIRWMLENVPAVKDAVKEGTLLFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGI
PKETLPEIKSSSENFGTISGEAVPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTE
IVFSKHGLLTTVCYQLGPNGPTVYALEGSIAVAGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVP
AFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNK
LLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLIRRSNSTFSPQMSAEERKAIYKE
WNKAVERSLKWAKL
>gnl|CDD|240349 PTZ00295, PTZ00295, glucosamine-fructose-6-phosphate aminotransferase; Provisional
LSIKKNIEDIDSCFIKKSRFYDYCCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGELKTTK
YASDGTTSDSIEILKEKLLDSHKNSTIGIAHTRWATHGGKTDENAHPHCDYKKRIALVHNGTIENYVELK
SELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPL
LVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYTQRRVEKIPEEVIEKSPEPYPHWTL
KEIFEQPIALSRALNNGGRLSGYNNRVKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCF
NTVQVIDASELTLYRLPDEDAGVIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYL
NAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCSNYKCSSLINSLHRLPTYIGMTLKSCEEQCKRIA
EKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEKNTPVILIILDDEHK
ELMINAAEQVKARGAYIIVITDDEDLVKDFADEIILIPSNGPLTALLAVIPLQLLAYEIAILRGINPDKP
RGLAKTVTVD
>gnl|CDD|240350 PTZ00296, PTZ00296, choline kinase; Provisional
MESISRTYDNIKNDKNNFSNVENENEGNEKASQNGTVCCPDDLKMYSTIQLNQEIDISKNPFPLHEINKK
NDIPLCAQEFSDLTDPLYIKKICLEKVPEWRRFTEDDVRVNQILSGLTNQLFEVSLKEETANNYPSIRRR
VLFRIYGKDVDELYNPISEFEVYKTMSKYRIAPQLLNTFSGGRIEEWLYGDPLRIDDLKNPSILIGIANV
LGKFHTLSRKRHLPEHWDRTPCIFKMMEKWKNQLSKYKNIEKYQRDIHKYIKESEKFIKFMKVYSKSDNL
ANDIVFCHNDLQENNIINTNKCLRLIDFEYSGYNFLATDIANFFIETTIDYSVSHYPFFAIDKKKYISYE
NRKLFITAYLSNYLDKSLVVPNPKIIDQILEAVEVQALGAHLLWGFWSIIRGYQTKSYNEFDFFLYAKER
FKMYDEQKEYLISNNIIKTYDS
>gnl|CDD|140318 PTZ00297, PTZ00297, pantothenate kinase; Provisional
MPASDAGCAQARVLSYNFNILPRGCGGFQHERIETFLASVDAYDVVLLQEVYAASVLPYFLQKQLCFQKM
LVDELKARGFHHYVISKQPSYLTMLRYNVCSDNGLIIASRFPIWQRGSYTFRNHERGEQSVRRGCLFAEV
EVPLAEGGSQRIVFFNVHLRQEDSLPSTSSQVQETRRFVESVIANVYEQNNDGAEIPFVIAGDFNINGID
PHNGGHPTKRFQELLNELQDLGSGVREVIYDETGQHPPTRPPILFFPEQSKLERYSSTPQRQDYFFVTPC
VQVEKPRIEKFVVSSRRPYTYLSDHFGVSARLTLPLNPSVIFEGRSLLRLNFSSLSEAAVHEHSNPSSSA
RLEAILLAAFAWAAFSFSFMSLVLCAAVWLLRWAQNSSIHPLLSERPFLTVEALKEKGEECFALNLPREY
NPLAGVRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRPGDVIGVDCE
ASRNIVILEVACALYGFTTLPLVGKGSTMRTLIDEHKIKVVFADRNSVAAILTCRSRKLETVVYTHSFYD
EDDHAVARDLNITLIPYEFVEQKGRLCPVPLKEHVTTDTVFTYVVDNTTSASGDGLAVVRVTHADVLRDI
STLVMTGVLPSSFKKHLMVHFTPFAMLFNRVFVLGLFAHGSAVATVDAAHLQRAFVKFQPTILVAAPSLF
STSRLQLSRANERYSAVYSWLFERAFQLRSRLINIHRRDSSLLRFIFFRATQELLGGCVEKIVLCVSEES
TSFSLLEHISVCYVPCLREVFFLPSEGVFCVDGTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKGEPRRTL
PIAAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRPIIAIVSPNRDTVE
FEWRQSHCMGEGGGPARQLGWTELVAYASSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTP
YGKIRRDAVHSYFSSVIERFYSDVETTPLPTPCADLQEDVSDVESSGTKLSSDCDFSLQVPVTIDIGGTF
AKIAYVQPPGGFAFPTYIVHEASSLSEKLGLRTFHFFADAEAAESELRTRPHSRVGTLRFAKIPSKQIPD
FADYLAGSHAINYYKPQYRTKVRATGGGAFKYASVAKKVLGINFSVMREMDAVVKGLNLVIRVAPESIFT
VDPSTGVHHPHQLVSPPGDGFSPFPCLLVNIGSGISIIKCLGPDGSHVRVGGSPIGGATFWGLVRTMTNV
TSWEEVMEIMRLDGPGDNKNVDLLVGDIYGYNAKDLPAMLSVDTVASTFGKLGTERFYEMMRGVSTAHFS
DDDAAGEILSPKALKSPTVISELPVRNGTKKASAIDIVRSLLNMISSNVTQLAYLHSRVQGVPNIFFAGG
FVRDNPIIWSHISSTMKYWSKGECHAHFLEHDGYLGALGCATLDPDGDAASE
>gnl|CDD|240351 PTZ00298, PTZ00298, mevalonate kinase; Provisional
MRKAVKEKTTGKHIGYGKVILFGEHFVVYGAEAIVAGIDEYTECRLELTKGVPGLQVVDQRPAVPGYIVE
KREEQRKAHQLVLRHLNIDTSVDGLKMHLGGPLVPSSGIGASASDVVSLSRALSELYQLNLTEEEVNLSA
FVGEGGYHGTPSGADNTAATYGGLISYRRVNGKSVFKRIAFQQPLYLVVCSTGITASTTKVVGDVRKLKE
NQPTWFNRLLENYNACVSEAKEALQKGNLFRVGELMNANHDLCQKLTVSCRELDSIVQTCRTYGALGAKM
SGTGRGGLVVALAASEDQRDAIAKAVRARCPEAKFVWRYTVQPSSAKN
>gnl|CDD|140320 PTZ00299, PTZ00299, homoserine kinase; Provisional
MSPLPKKVVLRVPATTANIGPAYDTLGMALSIFMELTVEHADAFSMTVEGEGSEHISTDEDNMVVQACRL
AFEEYAHKSMPPLKFIMHSNIPYGCGCGSSSAAAVAGFVAGMKLCGLTMETENEEALLQAIAKFEGHPDN
AAPAIYGGIQLVYKKDNGRFLTYRVPTPPNLSVVLFVPHNKMKANTHVTRNLIPTSVSLEDAVFNISRTS
ILVLALSTGDLRMLKSCSDKLHEQQRSDALFPHFRPCVKAAREAGAHYAFLSGAGPSVCALVGGRHGDPL
TQPREERKAESVAEAMIKAAEAVGVAGRVIITQPSDQGVHLVGTTCIRPNIQYTSI
>gnl|CDD|140321 PTZ00300, PTZ00300, pyruvate kinase; Provisional
MSVARMNFSHGSHEYHQTTINNVRQAAAELGVNIAIALDTKGPEIRTGLFVGGEAVMERGATCYVTTDPA
FADKGTKDKFYIDYQNLSKVVRPGGYIYIDDGILILHVQSHEDEQTLKCTVTNAHTISDRRGVNLPGCDV
DLPAVSAKDCADLQFGVEQGVDMIFASFIRSAEQVGEVRKALGAKGGDIMIICKIENHQGVQNIDSIIEE
SDGIMVARGDLGVEIPAEKVVVAQKILISKCNVAGKPVICATQMLESMTYNPRPTRAEVSDVANAVFNGA
DCVMLSGETAKGKYPNEVVQYMARICLEAQSAVNEYVFFNSIKKLQPIPMSAEEAVCSSAVNSVYETKAK
ALVVLSNTGRSARLVAKYRPNCPIVCVTTRLQTCRQLNITQGVESVFFDAERLGHDEGKEQRVAMGVGFA
KSKGYVQSGDLMVVVHADHKVKGYANQTRIILVS
>gnl|CDD|140322 PTZ00301, PTZ00301, uridine kinase; Provisional
MPCTVIGISGASGSGKSSLSTNIVSELMAHCGPVSIGVICEDFYYRDQSNIPESERAYTNYDHPKSLEHD
LLTTHLRELKSGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDIC
LIRRAKRDMRERGRTFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLRAKLNHDLENM
>gnl|CDD|240352 PTZ00302, PTZ00302, N-acetylglucosamine-phosphate mutase; Provisional
MSMFLESLFKQLIELCGSKFPLRHSAIENPLTYGTAGFRTKAELPPLEPVAYRVGILAALRSFLYGGKRA
KRGNKSVGVMITASHNPIQDNGVKIIDPDGGMLEESWEKICTDFANARTGEDLVSVLMDCLTEHGIKLSN
LKLDLNKSNCSKAKVHVGRDTRPSSPELVSALLRGLKLLIGSNVRNFGIVTTPQLHFLVAFANGLGVDVV
ESSDELYYAYLLAAFKELYRTLQEGGPVDLTQNNSKILVVDCANGVGGYKIKRFFEALKQLGIEIIPINI
NCDEEELLNDKCGADYVQKTRKPPRAMKEWPGDEETRVASFDGDADRLVYFFPDKDGDDKWVLLDGDRIA
ILYAMLIKKLLGKIQLKKKLDIGVVQTAYANGASTNYLNELLGRLRVYCAPTGVKNLHPKAHKYDIGIYF
EANGHGTVLFNEKALAEWAKFLAKQNALNSACRQLEKFLRLFNQTIGDAISDLLAVELALAFLGLSFQDW
LNLYTDLPSRQDKVTVKDRTLITNTEDETRLLEPKGLQDKIDAIVSKYDNAARAFIRPSGTEPVVRVYAE
APTLEQADELANEVKGLVLRYCSGA
>gnl|CDD|140324 PTZ00303, PTZ00303, phosphatidylinositol kinase; Provisional
MSDALAATAAAEAATTARTENPVAVCPATPPPTNCIGSVWLGVYDRVSHTRFRIHIEDPVFLCILSNTVV
PAAESDGSLPFEMQEFVEYLDAYERERLRQAYAARRGANTSGGTVGSGRCGVHGDPAAAAATAGSCGAGG
AVSGSGAIHSGVSGIPSMCCLNSCSPAGGPVPRKLEETLRETLSENSDFFFRVSSVAYHLDPNPQGASAC
TAASASAGSGVMGNAGVGARSPRRGEGLASAAAGGVASLLTNTIAAASATGPPPRRNYSVHSGYSAAFHL
CGRLFADVYRDHCRALAQKIASGFSGLRVEDCVKFRKAVWSGFHLKALEPYRSGARSESNLELRWVSEKI
KDDQHLFPSRGVAPQQQSSHVSRLVDATLSYVANARLRGRPSSSIGGNANSSTGGNGAAGAGGAGAAGKG
GGSAAARATVGGVAEENELNTFGLTKLLHNPSWQKDDESSDSCPSCGRAFISLSRPLGTRAHHCRSCGIR
LCVFCITKRAHYSFAKLAKPGSSDEAEERLVCDTCYKEYETVSQLHYLGALFAFAGLGFSDLVLCRTVNE
QWREAAELCISEYRLLLHNCDADLHSVKTPVGILLQNSLFLLLGDGPTSSIPVVHHPEAALLLLKFIATE
NLWVPDASYYFIWRLSSSVLNRADTVLTSLPSLSSSAASAVESKHHSFQLPVVPNFSHWHLFCTAFCSKI
GSSYFFVKCAELLCAAPAKVYDAYVASALERMTRVYLSTTPLWKRLAEANQATAAVFAARTSSPPTTAPL
PLPMLSDVTEGQVVTVWLLDMLHKDALVPAQRRRFQQLLERVIPTVAGSSLSLVFIMLLSLQSTYSYYGY
DEDLFGLWRTRIVAEVGRKDPVARDRVVATLDFFHELDRFCAQSSVVSQTSVVGWIVAYCRRGAPKAPAS
ATGAPGEATAPSARRIYHHSYIDLPHPILNPFKPYIVLKSIRLSGVKVAPNAASKPTWLAFSTWSAAEHL
ERDTMTAANNFGAHTLPTGESHAERSGEGREKGTGAAKTYTSTKTSAPVTSPVTAVNGVSPESLHDSLPQ
ECMFLYKRENVERDQLMCISSRLLQMLLSSEIGNAEMLDYSVLPLSCDSGLIEKAEGRELSNLDNMDIAS
YVLYRGTRSCINFLASAKLFLLLNYIFSIGDRHKGNVLIGTNGALLHIDFRFIFSEKTFVEKLARSTVRI
DDAFLAAVEQCQQRQCSCFAGPSPAATSSRARGCASPPGSSGSGGCGSPASPTKAPEPSSAEIREAFFSS
AAEWFVHVRPFAAVFYELWLYAVHRHTVPYNDAEMLNMLNTLFDRHASQTSSASKFSTTMKESVNVCRLK
DVTHSSAEVLRTFADQVSRRVSESSVDAMKMMGSMWSSWWSRGG
>gnl|CDD|185547 PTZ00304, PTZ00304, NADH dehydrogenase [ubiquinone] flavoprotein 1; Provisional
LRRAQGFLRLTASLLVRVHGGLKDQDRIFTNLYRDFDTYIDGALKRGDWYRTKDILLKGHDWIIDEIKKS
GLRGRGGAGFPSGLKWSFMPKVKPDGRPSYLVVNADESEPGTCKDREIMRHDPHKLVEGALLAGFAMRAR
AAYIYIRGEFYNEARALQQAIDEAYKKGFLGKNACGSGYDFDVYVHRGAGAYICGEETALIESIEGKPGK
PRLKPPFPANVGLYGCPTTVTNVETVAVSPTILRRGPQWFASFGRPNNAGTKLFCISGHVNNPCTVEEEM
SIPLRELIERHCGGVRGGWDNLLCVIPGGSSVPLIPKEICDNVLMDFDALKEVQSGLGTAAVIVMDKSTD
IIDAILRLSKFYKHESCGQCTPCREGTPWLVKMMERFVVGNADKEEIDTLEEVSKQIEGHTICALGDAAA
WPVQGLIRHFRPEIEERIERYWEANPHWGKSGSPWRRWKTH
>gnl|CDD|140326 PTZ00305, PTZ00305, NADH:ubiquinone oxidoreductase; Provisional
MKRLAARFPLWYAAPPLLMARRFFKSDGTPYNSDMTDILHGSEYNHRGGVEAAAEGVAAGQYAEHKPRAI
MFVNKRPVEIIPQEENLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLVVSCATVALPGMSI
ITDSRLVRDAREGNVELILINHPNDCPICEQATNCDLQNVSMNYGTDIPRYKEDKRAVQDFYFDPQTRVV
LNRCIHCTRCVRFLNEHAQDFNLGMIGRGGLSEISTFLDELEVKTDNNMPVSQLCPVGKLYLGDADENNA
IARELDAAEQTAAVATS
>gnl|CDD|140327 PTZ00306, PTZ00306, NADH-dependent fumarate reductase; Provisional
MGACATQTQRRCAMADGRTSASVVVVDPEKAAKERDRAARALLQDNFPELHVNQRAQLLYKGLEHTVPYT
LKVVVAGPVARQDADAVAKEVLRSAFQMVDTHLNSFNPNSEVSRVNRMPVGEKHQMSAHLKRVMACCQRV
YNSSGGCFDPAAGPLVHELREAARRQKSVEAEFVIEELAGRFTLTNSFAIDLEEGTIARKHEDAMLDLGG
VNKGYTVDYVVDRLNAAGFDDVLFEWGGDCRASGVNVQRQPWAVGIVRPPSVDEVRAAAKSGKSAPPDHK
SLLRVMSLNNEALCTSGDYENVLEGPASKVYSSTFDWKRRSLLEPTESELAQVSVKCYSCMYADALATAS
LVKRDPVKVRYMLENWRYVRNRVTDYTTYTREGERVAHMFEIATEDAEMRKKRIAGSLPARVIVVGGGLA
GCSAAIEAASCGAQVILLEKEAKLGGNSAKATSGINGWGTRAQAKQDVLDGGKFFERDTHLSGKGGHCDP
GLVKTLSVKSADAISWLSSLGVPLTVLSQLGGASRKRCHRAPDKKDGTPVPIGFTIMRTLEDHIRTKLSG
RVTIMTETTVTSLLSESSARPDGVREIRVTGVRYKQASDASGQVMDLLADAVILATGGFSNDHTPNSLLR
EYAPQLSGFPTTNGPWATGDGVKLARKLGATLVDMDKVQLHPTGLIDPKDPSNRTKYLGPEALRGSGGVL
LNKNGERFVNELDLRSVVSQAIIAQGNEYPGSGGSKFAYCVLNEAAAKLFGKNSLGFYWKRLGLFQRVDD
VKGLAKLIGCPVENLHRTLETYERLSTKKVACPLTGKVVFPCVVGTQGPYYVAFVTPSIHYTMGGCLISP
SAEMQMEDNSVNIFEDRRPILGLFGAGEVTGGVHGGNRLGGNSLLECVVFGKIAGDRAATILQKKKYGLS
KDKWTTVVVREVREGGQFGTGSRVLRFNLPGALQRSGLTLGQFIAIRGDWDGQQLIGYYSPITLPDDLGV
ISILARGDKGTLKEWISALRPGDSVEMKACGGLRIERRPADKQFVFRGHVIRKLALIAGGTGVAPMLQII
RAALKKPYVDSIESIRLIYAAEDVSELTYRELLESYRKENPGKFKCHFVLNNPPEGWTDGVGFVDRALLQ
SALQPPSKDLLVAICGPPVMQRAVKADLLALGYNMELVRTVDEDEPL
>gnl|CDD|140328 PTZ00307, PTZ00307, ethanolamine phosphotransferase; Provisional
MPPKSTARRISLNPLENEYIPPAYLPNLKKYKYSSTDSSIISRYVLQRYWNFIVNLVPMTVAPNCITFTG
FLIGMSSAALLLYFYFFEEGVYPSWVLYYAAFALFAYQTLDAIDGKQARRTGTGSPLGELFDHGCDAFLT
PFVLLNVSLATYMTPVERFWLSTISSMSLFTAIWEQFSTGTFDLGYVNGPTEGIILNCVLFIVSGVYGES
IWDTPAVGPYDVAYPPVLSSFFPGCSGTVHIESVRSVLFLLFLVSCPFTILTNVVHVVLRPTVHASKVTP
MLAALPILTMTALHVHVFVVFPNLHVKFPFALELSYGLLMSITVTRLTLARLSAMPYRTFNWHIVITFLA
LTAASLMHYAGDASVEHKYVEPSLGWALTGLAVFAAWQYGHMILSAFTQIARYLSISIMSIKPRKSD
>gnl|CDD|140329 PTZ00308, PTZ00308, ethanolamine-phosphate cytidylyltransferase; Provisional
TSPIPPKKPGTIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALR
ACKWVDEVVEGYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVG
RMLLCTKSHLLKSVDEVQLESSLFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIR
VLQKARELGDYLIVGVHEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHIN
VVVGGKFSDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE
IKP
>gnl|CDD|240353 PTZ00309, PTZ00309, glucose-6-phosphate 1-dehydrogenase; Provisional
APESGRASQSAYVAEVDLITDVLRAQTLVDKPDNGTESCDRIPCKVKDEDKSRALTIIVLGASGDLAKKK
TFPALFQLYCEGLLPSEVNIVGYARSKMSDVERWKKETLARFFKRLDDRECHLEQFLKHISYISGSYDED
EDFKRLNKLIERMEEAFQGPEKGGNRLFYLALPPSVFASVCEGIHRGCMSKNGWVRVIVEKPFGRDLESS
EELSNQLEPLFDESQLYRIDHYLGKEMVQNLIVLRFANRVFEPLWNRNNIACVQITFKEDIGTEGRGGYF
DSYGIIRDVMQNHLLQILALLAMEKPVSLSAEDIRDEKVKVLKCIEPIKMEECVLGQYTASADGSIPGYL
EDEGVPKDSTTPTFAAAVLHINNDRWEGVPFILEAGKALEERYVEIRIQFKGVDEFRPSGDDTQRNELVI
RAQPSEAMYLKITAKVPGLSNDLHQTELDLTYKTRYNVRLPDAYERLILDALLGDSTNFVRKDELDVAWR
IFTPLLHQIDRGEVKPEPYPFGSRGPKEADELIKKNGFKSSKGYQWLQSNDQ
>gnl|CDD|240354 PTZ00310, PTZ00310, AMP deaminase; Provisional
TDSQSKVSGGATFPISPELSHGHLRQPASSHSGSFSEFRFSDRAQRLFSGHGAPEVSLAAVASTMFRVVI
DGDDGGVDMRKVHGRIAAAIRVRQLYKPTDTKVPEGEREQPSDSTPMPSLVTIVQRDGVYRFSGMDTSVV
LPPPWEQYVRDVQAVYLTVGNGPCLSACRHRLTIIQERSRMFFLLNAEIEERADLYKAGGVFSPCTKVDN
AVLLSTSVDAQELLEFVVTTYREQPRAPLRLRDGSNSTLREYLEAHGVRDPRELTVEGLGWQPTKYRNKY
GQYDLFDAKNPMGALGAELRQSFLSLHGNLCGKLLRRELERREYQKQQPQATEYSLPLYGHHPEELTDLA
EWVRRQGFGPFSRNRWILAISFKELGPFQVPSSCTTVQDQLDNIFLPLFKATLCPSDPQWSDVAWLLCQV
GGLQILTHAVVRSEDFDETAPDPDQVPYTAKCSDLYYFYYVYANLAVLNSLRKRKGLNTLQLRPSGEKAP
AYDQLISSYLLGDVITRATSIADYPVLQYLCGLHRVGLTVSPLRDHALSITAYFDHPLPKFLHRCLRVSI
STSDPLYFHHHSQPLIEEYATAMKLFSLSPLDTTELARNSVLNSSFPPEVKQQWLGERFQLGVEGNDFER
SGVTNYRLAFREEAWALEEALLNDLLLNVPSGDSGAGPSRWHYISNVQEVEYDTVLDQRVRFPRTVLYGP
HKSGKAVTAAPALARALDLRHKYIWNPPPPWETTQRNVVEEDFQRTTRQFNEDQWTYAAYDGVFILSPKG
AVHAWPRFLPTLTEFIRDLSELRDICSSVEVKRLATKRLENLEHKFRLHLALNHSNEAGTTEERESSNRD
FYQAYKVDTHIHMAAGMTARQLLEFVVDKLLESGDDIAFKRGDHIVTLGQLFSKYGITPNLTVDQLNVQA
DHTLFERFDNFNSKYNPMENPDLRSLLLKTDNFMKGRYFAELIKDVFEQYSRDRFTYAENRLSIYGINVK
EWDDLAHWFDTHGMASKHNKWMIQVPRVYKVFRAQNVIGSFGQYLDNIFQPLWEASLHPSKHPKFHYFLN
HVSGFDSVDNEATIDLPFTDVSPWAWTSVENPPYNYYLYYLYANIRTLNEFRASRGFSTFALRPHCGESG
SMDHLYGAFLCANSICHGINLRNDPPMQYLYYLAQIGLHVSPLSNNALFLAFLENPFPVFFHRGLNVSLS
TDDPLMFHQTQEPLIEEYSIAARVWGLSLNDLCEIARNSVLQSGFDAAFKRNAIGDRWYLSSSLGNDSLR
THLSDIRVAFRFETYHTELNFLELCSGRPIPRAMKTLEEELAICEKIVDVRAETVLLSTHDQAMEVMLRE
METTNERIVHLRAQVDSLRRQQRSLVERLTEEGIRRQEVSEQVAGENNSIALRVNRLRERLQSEGLTVGG
GLYGRSNEEESEASSTQQGETVKRLLRWKPMPPDVMRAVTVASVPGSRGRPLP
>gnl|CDD|185549 PTZ00311, PTZ00311, phosphoenolpyruvate carboxykinase; Provisional
RNLAHHKPQGKSLTSKDILTLSQEQQETQLEEELHKLGLHNTTIHRNLTVPELYEHALKYEKNTSITSTG
ALCVYSGAKTGRSPKDKRIVKEDSSEDDIWWGKVNIPLSEESFEINKKRAIDYLNTRERLFVVDGYAGWD
PKYRLKVRVITTRAYHALFMRNMLIRPTNEELKKFGEDFVPDFTIYNAGEFKANRLIEGVTSETSVALNF
KRREMVILGTQYAGEMKKGILTVMMYLMPKQGVLPLHSSANVGKKGDVTLFFGLSGTGKTTLSADPNRKL
IGDDEHVWTDDGVFNIEGGCYAKCIDLSKETEPEIYNAIRFGAVLENVVLDKVTREVDFNDISITENTRC
AYPLEHIPNAKIPAVGGHPKNIIFLTCDAFGVLPPVSKLTPEQAMYHFISGYTAKVAGTEVGVKEPTATF
SACFGEPFLVLHPTVYAEMLAEKIKKHNTRVWLLNTGWIGGSYGSGGKRMPLKYTRAIIDAIHDGELKKA
EYEKFPIFGLQIPKSCAGVPSELLDPRNAWKDKAAFDKQLKELAAKFQKNFKKYADKASPEVLAAGPKLV
E
>gnl|CDD|140333 PTZ00312, PTZ00312, inositol-1,4,5-triphosphate 5-phosphatase; Provisional
MDENEDAQRFTAIGSIVFLSPRMCPISSILSFPHRTFVPVVDDPLTYGSSPTRLFHGGKFSGAGRSRKGF
LLLSLRLGTVVVNVLNVHLYNDDDNRVAAASSPSLYTGQRQEALLEAIAECSAFISPSDPLFIFGDFNVR
LDGHNLLEWLKEKMQIDVKIEVKRVRAPDRFWELFTNPQTQGEIRRFDLELQRLMDVVAQQSGVELAEFA
IRFPPTYPRVAERTNTGAQIESAGANVAASVYGVKDVAAKLDNQQRKKAAKDLKGTADAILASVVLTRVT
AIPHRNYCRDRLPAWCDRVLWNPAGLELMTGDRSRSASPQSAAASKGDQASGQSCRYAYRSIDLIHTDHD
GVFLLF
>gnl|CDD|140334 PTZ00313, PTZ00313, inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
MPKPVILDHDGNHDDLVALALLLGNPEKVKVIGCICTDADCFVDDAFNVTGKLMCMMHAREATPLFPIGK
SSFKGVNPFPSEWRWSAKNMDDLPCLNIPEHVAIWEKLKPENEALVGEELLADLVMSSPEKVTICVTGPL
SNVAWCIEKYGEEFTKKVEECVIMGGAVDVGGNVFLPGTDGSAEWNIYWDPPAAKTVLMCPHIRKVLFSL
DSTNSVPVTSEVVKKFGAQNKYLLSQFVGSTWAMCTHHELLRPGDGYYAWDVLTAAYVIERNLAELEPVP
LEVVVEKAKNEGRTRRAAEGAACTYVAKNTNAELFYDMVLDSARIC
>gnl|CDD|240355 PTZ00314, PTZ00314, inosine-5'-monophosphate dehydrogenase; Provisional
MADGMSADELFNSIPTGLTYDDVILLPGYIDFSRDDVDLSTRLTRNIRLKIPIVSSPMDTVTEHKMAIAM
ALMGGIGVIHNNCSIEEQVEEVRKVKRFENGFIMDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKVGG
KLLGIVTSRDIDFVKDKSTPVSEVMTPREKLVVGNTPISLEEANEVLRESRKGKLPIVNDNGELVALVSR
SDLKKNRGYPNASLDSNGQLLVGAAISTRPEDIERAAALIEAGVDVLVVDSSQGNSIYQIDMIKKLKSNY
PHVDIIAGNVVTADQAKNLIDAGADGLRIGMGSGSICITQEVCAVGRPQASAVYHVARYARERGVPCIAD
GGIKNSGDICKALALGADCVMLGSLLAGTEEAPGEYFFKDGVRLKVYRGMGSLEAMLSKESGERYLDENE
TIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELHEKLYSGQVRFERRSGSAIKEGGVHS
LHKFE
>gnl|CDD|240356 PTZ00315, PTZ00315, 2'-phosphotransferase; Provisional
MPAAPNSQMAAELVTSTLATPSRLPPSGQRPQRNTVAAAQSAASSQFPEIAPQPFDAYVVLDFEATCEAD
RRIEDAEVIEFPMVLVDARTATPVAEFQRYVRPVKNPVLSRFCTELTGITQSMVSRADPFPVVYCEALQF
LAEAGLGDAPPLRSYCVVTCGDWDLKTMLPSQMRVSGQQGTPLSFQRWCNLKKYMSQLGFGNGSGCGGGA
TPPLGPSDMPDMLQMLGLPLQGRHHSGIDDCRNIAAVLCELLRRGLVIDPTFDTAPFRRWHAPTEASLPA
LDALPSTLADGAAQHSRDCREPGRRHARTEGDARASDTVNNQQSMPERKHRSAYRHEDPLDFLLPLLVLD
RNRDAVQELLSDTRPADAPSRVFDEEKLVTYSKFMSRLLRHKADQWRVPITSNGYVLLDDILRQPPMRND
PVSVQDVARVVRDSDKQRFKLAYGAADGRLYIRANQGHSIDGVEPELRTLTSVEEVPVAVHGTYWSAWKA
IQRCGYLSTMTRQHIHFAKGLINDEQVISGMRNNVQLFLYLDVAAVLADGVALYESSNGVILTPGVGHTR
QLPLKYVAKVVDRSTGRTIYPA
>gnl|CDD|140337 PTZ00316, PTZ00316, profilin; Provisional
MSWQAYVDDSLIGSGNMHSAAIVGLADGSYWAYGGSYIPQPEEVAHILKCLGNFSLVQSSGVTIYGVKFF
GLQSGTEGDMKYIFFKKGAAGGCIYTSKQTAIIAVYGNPGDTSSLQQDLEKNEAHAVAVNPADCNTTVKR
IAEYLISLDY
>gnl|CDD|240357 PTZ00317, PTZ00317, NADP-dependent malic enzyme; Provisional
MSLAKMAHSKEKVPSNARGVDVLRNRFLNKGTAFTAEEREHLGIEGLLPPTVETLEQQVERLWTQFNRIE
TPINKYQFLRNIHDTNETLFYALLLKYLKELLPIIYTPTVGEACQNYSNLFQRDRGLYLSRAHKGKIREI
LKNWPYDNVDVIVITDGSRILGLGDLGANGMGISIGKLSLYVAGGGINPSRVLPVVLDVGTNNEKLLNDP
LYLGLREKRLDDDEYYELLDEFMEAVSSRWPNAVVQFEDFSNNHCFDLLERYQNKYRCFNDDIQGTGAVI
AAGFLNALKLSGVPPEEQRIVFFGAGSAAIGVANNIADLAAEYGVTREEALKSFYLVDSKGLVTTTRGDK
LAKHKVPFARTDISAEDSSLKTLEDVVRFVKPTALLGLSGVGGVFTEEVVKTMASNVERPIIFPLSNPTS
KAECTAEDAYKWTNGRAIVASGSPFPPVTLNGKTIQPSQGNNLYVFPGVGLGCAIAQPSYIPDEMLIAAA
ASLATLVSEEDLREGKLYPPLEDIREISAHIAVDVIEEAQEMGIAKNKDLPDNRDELLALVKDRMWVPK
>gnl|CDD|185553 PTZ00318, PTZ00318, NADH dehydrogenase-like protein; Provisional
MRSRTARLKKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRP
ALAKLPNRYLRAVVYDVDFEEKRVKCGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFL
KEVNHARGIRKRIVQCIERASLPTTSVEERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEE
CKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVLKDGEVIPTGLVVWSTGVGP
GPLTKQLKVDKTSRGRISVDDHLRVKPIPNVFALGDCAANEERPLPTLAQVASQQGVYLAKEFNNELKGK
PMSKPFVYRSLGSLAYLGNYSAIVQLGAFDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRD
ITRF
>gnl|CDD|173521 PTZ00319, PTZ00319, NADH-cytochrome B5 reductase; Provisional
MVVLAVIIALGVAAFFAFMFSRSPPVALDPDMFQHFKLIKKTEVTHDTFIFRFALHSPTQRLGLPIGQHI
VFRCDCTTPGKPETVQHSYTPISSDDEKGYVDFLIKVYFKGVHPSFPNGGRLSQHLYHMKLGDKIEMRGP
VGKFEYLGNGTYTVHKGKGGLKTMHVDAFAMIAGGTGITPMLQIIHAIKKNKEDRTKVFLVYANQTEDDI
LLRKELDEAAKDPRFHVWYTLDREATPEWKYGTGYVDEEMLRAHLPVPDPQNSGIKKVMALMCGPPPMLQ
MAVKPNLEKIGYTADNMFTF
>gnl|CDD|140341 PTZ00320, PTZ00320, ribosomal protein L14; Provisional
MFRFFRLRLAPTTTDAAAKLPAGNPVNKSWFRHNLIIRRKASYRSRWGTGAEGYGTGVPFSDQVKLHCVD
NTNCKHVRLISKATAERFAHCRVFPAVAHRVSVQRFKSGRGEVSRHRVKPGNIYWVCLLSRRQTNTRMSG
LQTNFDRNTCILMNDQRVPLGTRVMYCAGRHVNHKYHLKAVVLANFFV
>gnl|CDD|240358 PTZ00321, PTZ00321, ribosomal protein L11; Provisional
MLRRGTVSLLRARPKTVNVEPGSNRMLDAAVMAKAKDIFAVPEFPGKRVLHNWRFFIKAGKAATGPPVGQ
EFSKLGLKAMDFAKSFNDRTKPHFKDDVELIVRIQVYFDKSYLFTIEPPPTAWFILRALRKKRRETGPVP
LRGHYCALMTLEMAYEIAKMKPRSWGRPEYPLIETRVRRVVGQARRMGVCFIGVDTPHSSPVKGMTEKQY
AEESERYRAMHMEQYEALRQRELEEAPLIERLHRPNMAPLTEAQIEEGLKDPGLLHALWQASHPKSPYHR
DLRQREMARRYLNARGWVKDMTPEEMRVVFMNYRLPEIERGHQMDEGGMEGQVYWTRDGAQP
>gnl|CDD|140343 PTZ00322, PTZ00322, 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
MSFLVCSVASSAFAAQLFFGTEGSRKRRAKPISFERMAAIQEEIARIDTHLEALEATENKDATPDHNLTT
EEVIDPVVAHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD
PTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDSFTGKPPSLEDSPISSHHPDFSAVPQ
PMMGSLIVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIFIHQAYRRRLERRGGAVSSPTGAAEVEFRIAK
AIAHDMTTFICKTDGVAVLDGTNTTHARRMALLRAIRETGLIRMTRVVFVEVVNNNSETIRRNVLRAKEM
FPGAPEDFVDRYYEVIEQLEAVYKSLNPVTDCDLTYIRIEDTQTFSLNNISGWMPSRLAYMLHNLNPTPM
NLYLTRAGEYVDLLSGRIGGNSRLTERGRAYSRALFEYFQKEISTTSFTVMSSCAKRCTETVHYFAEESI
LQQSTASAASSQSPSLNCRVLYFPTLDDINHGDCEGQLLSDVRRTMPNTLQSMKADPYYTAWPNGECIHQ
VFNARLEPHIHDIQASTTPVLVVSHLHLLQGLYSYFVTDGDNIVAPQNAYKIDIPFEHVIKIRMVGFNRV
AELIDLSKEVDRIQQSRTGLVTKATQQSSRSGKK
>gnl|CDD|185554 PTZ00323, PTZ00323, NAD+ synthase; Provisional
MMPVAPLHPELQRVLKEVRRKRAFNPAAWIEKKCAKLNEYMRRCGLKGCVTSVSGGIDSAVVLALCARAM
RMPNSPIQKNVGLCQPIHSSAWALNRGRENIQACGATEVTVDQTEIHTQLSSLVEKAVGIKGGAFARGQL
RSYMRTPVAFYVAQLLSQEGTPAVVMGTGNFDEDGYLGYFCKAGDGVVDVQLISDLHKSEVFLVARELGV
PENTLQAAPSADLWEGQTDEDELGFPYDFVELYTEWYLKLNETEKKSFLSSLSEEARKQFEEYSAACELV
HRRNAHKLQGPVNL
>gnl|CDD|240359 PTZ00324, PTZ00324, glutamate dehydrogenase 2; Provisional
MMRHTVSQAIAALRGRYLPASHAFTSVTLDGTADLATSSRFASQAQSVKKIVKTRAVFSKKIVESEADQF
YSKLGLSSYYFNTSQAEMIAHNQGSLTAAKRLREGSGFEYFHENDGTAFYICRASPQKRLRMQCFRSTFV
SFNDDPKLGVRLRLYFLQDPVFAIYTASIEPFVEDGVEEGETDLSKLLDQTFLKQKREEQKEIIQELLNR
QVSSVGPVLHVNEVPRGGVSFTMAMAFRRRYYTASFFSRFGEIVTFHGAYSMSKYVEPFSNGVQVYTFFI
RGLTADDNPDLSIEDRASLIRLLYILPFSSLTRLHEERVLSCEETAYADAAVIFAFHFTPSPTTDDYRHL
EALLAKEPNGVSRLNNLRTRLTQEVFSERYIGEAIALYPEFVKLLYEDFRLGHTPERRAAITQKIEETAR
LKEDIRNELDRTIFSAFLSFNEHILKTNFYKTEKTALAFRLDPSFLSELEYPRVPYGVFLVAGAQFRGFH
IRFTDIARGGVRMIQSFKEQAYRRNKRSVFDENYNLASTQLLKNKDIPEGGSKGTILLSSRYLNKFAQVR
CQHAFLQYIDALLDVMLPGEKVVDHLKQEEIIFLGPDEHTTGTLMDWAALHAKKRGYPFWKSFTTGKSPS
MGGIPHDTYGMTTRSVRAYVTGILEKLGLNEEEVTKFQTGGPDGDLGSNELLLSKEKTVGIVDGSGVLHD
PEGLNREELRRLAHHRLPAREFDESKLSPQGFLVLTDDRDVKLPDGTIVESGLRFRNEFHLLPYSDADVF
VPCGGRPRSVTLFNVGRFFDEKNGKLRFKIIVEGANLFITQDARLALEECGVILFKDASANKGGVTSSSL
EVLAALALSDEEFAEHMCVKDATDAPEFYKKYVKEILDRIEENARLEFNAIWREELRTGKPRCLLADVLS
RKIVRLRADILSSDLWQDDDLVRYVMSQAIPKTLQEVVPVETLMKRVPESYQKAIFAMWLASRYVYQTGD
NSNEFAFFRYMTELKQQAAKSA
>gnl|CDD|240360 PTZ00325, PTZ00325, malate dehydrogenase; Provisional
MRPSALKMFKVAVLGAAGGIGQPLSLLLKQNPHVSELSLYDIVGAPGVAADLSHIDTPAKVTGYADGELW
EKALRGADLVLICAGVPRKPGMTRDDLFNTNAPIVRDLVAAVASSAPKAIVGIVSNPVNSTVPIAAETLK
KAGVYDPRKLFGVTTLDVVRARKFVAEALGMNPYDVNVPVVGGHSGVTIVPLLSQTGLSLPEEQVEQITH
RVQVGGDEVVKAKEGAGSATLSMAYAAAEWSTSVLKALRGDKGIVECAFVESDMRPECPFFSSPVELGKE
GVERVLPIGPLNAYEEELLEAAVPDLKKNIEKGLEFARKKL
>gnl|CDD|240361 PTZ00326, PTZ00326, phenylalanyl-tRNA synthetase alpha chain; Provisional
MMQKELEENTILSKLESENEIVNSLALAESLNIDHQKVVGAIKSLESANYITTEMKKSNTWTLTEEGEDY
LKNGSPEYRLWQKLKEGGISKADDAKKLGGKVADIGLGNAMKKKWIKLNKGDKKVFLSRKLVDSVVDTVR
LLLKIVAKGSQAEKIDSKELKELKKRKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAE
FKEYNFNALGKKIGGGNLHPLLKVRREFREILLEMGFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDT
FFLSKPETSKVNDLDDDYVERVKKVHEVGGYGSIGWRYDWKLEEARKNILRTHTTAVSARMLYKLAQEYK
KTGPFKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVIDRNLTLGDLIGTIREFFRRIGITKLRFKPAFN
PYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGLSLERPTMIKYGIKNIRDLFGH
KVDL
>gnl|CDD|240362 PTZ00327, PTZ00327, eukaryotic translation initiation factor 2 gamma subunit; Provisional
VIDTDDGLAKQDLSKLDLDKLTPLTPEVISRQATINIGTIGHVAHGKSTVVKALSGVKTVRFKREKVRNI
TIKLGYANAKIYKCPKCPRPTCYQSYGSSKPDNPPCPGCGHKMTLKRHVSFVDCPGHDILMATMLNGAAV
MDAALLLIAANESCPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIADNAPI
IPISAQLKYNIDVVLEYICTQIPIPKRDLTSPPRMIVIRSFDVNKPGEDIENLKGGVAGGSILQGVLKVG
DEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNELQYAVPGGLIGVGTTIDPTLTRADRLVGQVLGYP
GKLPEVYAEIEIQYYLLRRLLGVKSQDGKKATKVAKLKKGESLMINIGSTTTGGRVVGIKDDGIAKLELT
TPVCTSVGEKIALSRRVDKHWRLIGWGTIRKGVPVKLLNS
>gnl|CDD|140349 PTZ00328, PTZ00328, eukaryotic initiation factor 5a; Provisional
MSDEDHDFSHQGGGDNASKTYPLPAGALKKGGYVCINGRPCKVIDLSVSKTGKHGHAKVSIVATDIFTGN
RLEDQAPSTHNVEVPFVKTFTYSVLDIQPNEDPSLPAHLSLMDDEGESREDLDMPPDAALATQIKEQFDS
GKEVLVVVVSAMGTEQVLQTKNAAEK
>gnl|CDD|185558 PTZ00329, PTZ00329, eukaryotic translation initiation factor 1A; Provisional
MPKNKGKGGKNRRRGKNDNEGEKRELVFKEEGQEYAQVLRMLGNGRLEAYCFDGVKRLCHIRGKMRKRVW
INIGDIILVSLRDFQDSKADVILKYTPDEARALKQHGELPETAKINETDIFDDEGDDGIEFQDDESDEEA
TDEMLNLTKADIDDI
>gnl|CDD|140351 PTZ00330, PTZ00330, acetyltransferase; Provisional
SDMSGSLELRDLEEGDLGSVLELLSHLTSAPALSQEELEQIAARRRLAGVVTRVFVHSPTQRIVGTASLF
VEPKFTRGGKCVGHIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTEDMVAFYKKLGFRACE
RQMRLDL
>gnl|CDD|240363 PTZ00331, PTZ00331, alpha/beta hydrolase; Provisional
MSTSCITVSSTNDALIIVDVQNDFCKGGSLAVPDAEEVIPVINQVRQSHHFDLVVATQDWHPPNHISFAS
NHGKPKILPDGTTQGLWPPHCVQGTKGAQLHKDLVVERIDIIIRKGTNRDVDSYSAFDNDKGSKTGLAQI
LKAHGVRRVFICGLAFDFCVLFTALDAVKLGFKVVVLEDATRAVDPDAISKQRAELLEAGVILLTSSDLV
AS
>gnl|CDD|240364 PTZ00332, PTZ00332, paraflagellar rod protein; Provisional
MVPEVDATGLEAARKQKIHNLKLKTACLENEELVQELHVSDWSETQRQKLRGAHEKAEELLASVEVGTKW
NLTEAYDLAKLMRVCGLEMSQRELYRPEDKPQFMDIIALKKVLQDLKQNRNKTRVVSFTQMIDNAIAKME
KVEEELRRSQLDATQLAQVPTATLKNIEDIMNVTQIQNALASTDDQIKTQLAQLEKTNEIQNVAMHDGEM
QVAEEQMWTKVQLQERLIELVADKFRLIGKCEEENKSFSKIHEVQKQANQETSQMKDAKRRLKQRCETDL
KHIHDAIQKADLEDAEAMKRYATNKEKSERFIRENEDRQEEAWNKIQDLERQLQRLGTERFEEVKRRIEE
NDREEKRRVEYQQFLEVAGQHKKLLELTVYNCDLALRCTGLVEELVSEGCAAVKARHDKTNQDLAALRLQ
VHKEHLEYFRMLYLTLGSLIYKKEKRLEEIDRNIRTTHIQLEFCVETFDPNAKKHADMKKELYKLRQGVE
EELAMLKEKQAQALEMFKESEEALDAAGIEFVHPVDENNEEVLTRRSKMVEYRSHLAKQEEVKIAAEREE
IKRARLLRSQGYRGEQIRIGGNTAPAILE
>gnl|CDD|240365 PTZ00333, PTZ00333, triosephosphate isomerase; Provisional
MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPNNVDVVVAPPSLHIPLVQEKLKNKNFKISSQNVSL
TGSGAFTGEISAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQ
TSDVLSKQLEAIVKKVSDEAWDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRI
IYGGSVNEKNCKELIKQPDIDGFLVGGASLKPDFVDIIKSAEQSK
>gnl|CDD|240366 PTZ00334, PTZ00334, trans-sialidase; Provisional
MLSRVAAVKAPRTHNRRRVTGSSGRRREGRESEPQRPNMSRRVFTSAVLLLLVVMMCCGSGGAAATENGA
SGQGSSPSKSFVWRDKNGGETVSSLRVPVLVEMDGGVFAVAEAQLKEGGNSGFTGIASELLEWTDKESKE
LDTTKLKTQVLEECPAENGKCASQTGAQEASQSRTKVRVSRPTTVVNGSDIYMFAGTYSFEVTDKAGNTA
AAAKWGLLVAVGNVSNDGSSGKKKIYWKDASVIPWTDFEKQHESLTRLIGGGGSGVQMKDGTLVFPVEGT
KKDGKAVSLIIYSSATESGNLSKGMSADGCSDPSVVEWKEGKLMMMTACDDGRRRVYESGDKGDSWTEAL
GTLSRVWGNKQKGNEKGVGSGFSTATIENRDVMLVTLPVYSNRKGKEKGELHLWLTDNTHIVDIGPVSGD
DDAAASSLLYKSAGSGNNNNERLIALYEKKKGGGESSLGMVSVRLTAQLKRVREVLATWKEVDERVSKLC
PSKTAAKNPSTGNGCSAVKITDGLVGFLSGNFSGNTWRDEYLGVDATVKKGTNGVATGYADGVTFQGAWA
EWPVGKQGENQLYHFANHNFTLVATVSVHGEPKGDTPIPLMGATMNDNKNTVLLGLSYDKEGKWQVLCGG
KTTKELRSNWEPETTHQVAIVLRNGKQGSAYVDGQRVGDASCELKNTDSKGISHFYIGGDGGSAGSKEDV
PVTATNVLLYNRPLDDNEIRVLNANKISIPKLTGLKTLAAGATGVGTARHFGAHGDGSTVCGGGLLPLLL
LLGLWGIAAS
>gnl|CDD|185562 PTZ00335, PTZ00335, tubulin alpha chain; Provisional
MREVISIHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDKNIGVEDDAFNTFFSETGAGKHVPRCVFLDL
EPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHA
VGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIY
DICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPIISAEK
AYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTG
FKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDLAALEKDYEEVGAESADEEGEEDV
>gnl|CDD|185563 PTZ00337, PTZ00337, surface protease GP63; Provisional
MRQPRHTALLPLLLPWLMMVVCCAGVCVAADRAVKHRCGFDAMMKKYGRLPTAVVREVPRRGQGAVQAYT
AASEDGDDGWAPIRIKVSAEDMHNPLRHCTAAGDLRIDHDGRAITCEADDVLTEERRSIILRQTLPAAIQ
LHAERLSVRPVTRPVLIPRTGLGMCDNFTIPHKHHTVGVAGADMILYANIFPTSGPAAWAIPCFLLDDGR
PFAAAVNFDPRQIAVTNGDVRVAAHELGHALGFVRDQFLMLHMISEVPNVRGMSKVSVISTPKTKAMARQ
YHNCPTLEGIELEDEGGPGTALSHWKKRNMRDEMMTSDVGVGLYSALTLAAFEDMGVYLANYSAAEMLWW
GNNSGCGLLEKKCLTDGISEYPDLFCNQFDDDEKFFCTYDRLSLGRCDLKRHEEALPEEYRYFADPRVGG
DDLYMSRCPYVKAYSNGGCTNGDPSVMPGSVVGPNSRCVKGQDLQFDDEYIGDVCVDTRCGDGTLSVRFL
DDDAWHECQEGETVTPPSGPWRGSIVCPQYADVCTAFPNISSHPIPVVDPPLADDPTSAEDAEGDEGEVP
RKRPRRL
>gnl|CDD|240367 PTZ00338, PTZ00338, dimethyladenosine transferase-like protein; Provisional
TGGSKSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRM
VAELKKRFQNSPLASKLEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFA
LRLLAQPGDELYCRLSVNTQLLCRVTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRIC
FSRKNKTLSAIFKTKSVLQTLEHNYKSWCTMINKKVPVSLEPFKEFIAEILEDSGMFEKRSVKLDIDDFL
KLLLAFNKKGIHFV
>gnl|CDD|240368 PTZ00339, PTZ00339, UDP-N-acetylglucosamine pyrophosphorylase; Provisional
CLKVLTGDGQDHLREALKRRSEGEFTPLATQILSSLTNVDFKHRNAVLEPKLEEYNAEAPVGIDIDSIHN
CNIEPPNNNTFIDIYEKEKERKELKESGLEIIKKGEVAVLILAGGLGTRLGSDKPKGLLECTPVKKKTLF
QFHCEKVRRLEEMAVAVSGGGDDPTIYILVLTSSFNHDQTRQFLEENNFFGLDKEQVIFFKQSSLPCYDE
NTGRFIMSSQGSLCTAPGGNGDVFKALAKCSELMDIVRKGIKYVQVISIDNILAKVLDPEFIGLASSFPA
HDVLNKCVKREDDESVGVFCLKDYEWQVVEYTEINERILNNDELLTGELAFNYGNICSHIFSLDFLKKVA
ANRLYESTPYHAARKKIPYINGPTDKTMGIKLEAFIFDIFRYAKNVLILEVDREDEFAPIKNADGAAADT
ILNAQKLLLSLHTRWLEAALETVAGNPREGLNLCEISPLVSYGGEGLFQYPGKKILGLPEIL
>gnl|CDD|240369 PTZ00340, PTZ00340, O-sialoglycoprotein endopeptidase-like protein; Provisional
FLALGIEGSANKLGVGIVTSDGEILSNVRETYITPPGTGFLPRETAQHHREHILSLVKEALEEAKITPSD
ISLICYTKGPGMGAPLSVGAVVARTLSLLWGKPLVGVNHCVAHIEMGRLVTGAENPVVLYVSGGNTQVIA
YSEHRYRIFGETIDIAVGNCLDRFARLLNLSNDPAPGYNIEQLAKKGKNLIELPYVVKGMDMSFSGILTY
IEDLVEHPQFKDVVSEIVPPEEEFFTDDLCFSLQETIFAMLVEVTERAMSHCGSNEVLIVGGVGCNLRLQ
EMMQQMAKERGGKLFAMDERYCIDNGAMIAYAGLLEYLSGGFTPLKDATVTQRFRTDEVDVTWRD
>gnl|CDD|173534 PTZ00341, PTZ00341, Ring-infected erythrocyte surface antigen; Provisional
MKPFHAYSSAFSKQYMDTKNVKAKNPTIYSFDDEEKQNENKSFLKSLCSKRGVLPIIGILYIILNGNFGY
NGSSNSGAQFTDRCSRNLYCETLPINPYADSENPIVVSQVFGLPFEKPTFTLEGPPDIDHTNILGFNEKF
MTDVNRYRYSNNYEAIPHIREFNPLIVDKVLFDYNEKVDNLGRSGGDIIKKMQTLWDEIMDINKRKYDFL
KEKLQKTYSQYKVQYDMPKEAYESKWGQCIKLIDQGGDNLEERLNSQFKNWYRQKYLNLEEYRRLTVLNQ
IAWKALSNQIQYSCRKIMNSDISSFKHINELKSLEHRAAKAAEAEMKKRAEKPKKKKSKRRGWLCCGGGD
IETVEPQQEEPVQDVGEHQINEYGDILPSLKASINNSAINYYDAVKDGKYLDDDSSDALYTDEDLLFDLE
KQKYMDMLDGSEDESVEDNEEEHSGDANEEELSVDEHVEEHNADDSGEQQSDDESGEHQSVNEIVEEQSV
NEHVEEPTVADIVEQETVDEHVEEPAVDENEEQQTADEHVEEPTIAEEHVEEEISTAEEHIEEPASDVQQ
DSEAAPTIEIPDTLFYDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFHKFKKINEAYQILGDIDK
KKMYNKFGYDGIKGVNFIHPSIFYLLASLEKFADFTGSPQIVTLLKFFFEKKLSMNDLDNKSEHLLKFME
QYQKEREAHISENLINILQPCIAGDRKWDVPIIDKIEELKGSPFDIAIIDSIGWIFKHVAKSHLKKPKKA
AKKLEQRSKANKEELANENNKLMNILKEYFGNNEQINSITYNFENINLNEDNENGSKKILDLNHKDQKEI
FEEIISYIVDISLSDIENTAKNAAEQILSDEGLDEKKLKKRAESLKKLANAIEKYAGGGKKDKKAKKKDA
KDLSGNIAHEINLINKELKNQNENVPEHLKEHAEANIEEDAEENVEEDAEENVEENVEENVEENVEENVE
ENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAE
ENVEENIEENIEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAE
EYDDENPEEHNEEYDE
>gnl|CDD|240370 PTZ00342, PTZ00342, acyl-CoA synthetase; Provisional
MIIYSLCLFFIYLIYVAPCCTQSLSKGKGYSEICEKATNENESSVYCMKDHKKKSSLYVYKHIMKLLLEK
YKLNNNKIAIVEHSCGEPQNYITYGNFFKKVLSFSHSLNTYEGKGIPEKKYNEEQNNGKFKLLGLYGSNS
INWLVADLACMLSGVTTLVMHSKFSIDVIVDILNETKLEWLCLDLDLVEGLLERKNELPHLKKLIILDTL
IKSKEININKEEKNNGSNVNNNGNKNNKEEQKGNDLSNELEDISLGPLEYDKEKLEKIKDLKEKAKKLGI
SIILFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNPKTH
LSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPP
LKRFLVKKILSLRKSNNNGGFSKFLEGITHISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYY
QGYGLTETTGPIFVQHADDNNTESIGGPISPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKE
QTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSM
DGPLAIISVDKYLLFKCLKDDNMLESTGINEKNYLEKLTDETINNNIYVDYVKGKMLEVYKKTNLNRYNI
INDIYLTSKVWDTNNYLTPTFKVKRFYVFKDYAFFIDQVKKIYKNK
>gnl|CDD|240371 PTZ00343, PTZ00343, triose or hexose phosphate/phosphate translocator; Provisional
MEKDKKKNEYGTFPITNNEGYSDALPEKAFPSKGIYHSLFESFPNFKWKLALLFLTWYALNVLYVVDNKL
ALNMLPLPWTISSLQLFVGWLFALLYWATGFRKIPRIKSLKLFLKNFLPQGLCHLFVHFGAVISMGLGAV
SFTHVVKAAEPVFTALLSILFLKQFLNLYAYLSLIPIVGGVALASVKELHFTWLAFWCAMLSNLGSSLRS
IFAKKTMKNKSEIGENLTASNIYMLLTLIASLISLPLVLFFEGKKWVPVWTNYTANMTNYTKGIIIFKIF
FSGVWYYLYNEVAFYCLGKVNQVTHAVANTLKRVVIIVSSIIIFQTQVTLLGYLGMAVAILGALLYSLFK
>gnl|CDD|240372 PTZ00344, PTZ00344, pyridoxal kinase; Provisional
MSMEKKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLR
ANNLLSDYTYVLTGYINSADILREVLATVKEIKELRPKLIFLCDPVMGDDGKLYVKEEVVDAYRELIPYA
DVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVITSFREDEDPTHLRFLLSCRDKDTKNNKRF
TGKVPYIEGRYTGTGDLFAALLLAFSHQHPMDLAVGKAMGVLQDIIKATRESGGSGSSSLMSRELRLIQS
PRDLLNPETVFKVTPL
>gnl|CDD|240373 PTZ00345, PTZ00345, glycerol-3-phosphate dehydrogenase; Provisional
RSLFQKLRCGPLKVSVIGSGNWGSAISKVVGENTQRNYIFHNEVRMWVLEEIVEGEKLSDIINTKHENVK
YLPGIKLPDNIVAVSDLKEAVEDADLLIFVIPHQFLESVLSQIKENNNLKKHARAISLTKGIIVENGKPV
LCSDVIEEELGIPCCALSGANVANDVAREEFSEATIGCEDKDDALIWQRLFDRPYFKINCVPDVIGVEVC
GALKNIIALAAGFCDGLGLGTNTKSAIIRIGLEEMKLFGKIFFPNVMDETFFESCGLADLITTCLGGRNV
RCAAEFAKRNGKKSWEEIEAELLNGQKLQGTVTLKEVYEVLESHDLKKEFPLFTVTYKIAFEGADPSSLI
DVLSTNELRPIKTVP
>gnl|CDD|240374 PTZ00346, PTZ00346, histone deacetylase; Provisional
MHAVHKDDAEAPLLNTESRGRVALIDTSGYASDMNISAFVPQHAMKPYRVLAAMEIVRSLKIDAHCRTVV
PPLVKVEELMAYHTDTYLANLGLHSCRSWLWNAETSKVFFSGDCPPVEGLMEHSIATASGTLMGAVLLNS
GQVDVAVHWGGGMHHSKCGECSGFCYVNDIVLGILELLKCHDRVLYVDIDMHHGDGVDEAFCTSDRVFTL
SLHKFGESFFPGTGHPRDVGYGRGRYYSMNLAVWDGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADS
LAGDRLGLLNLSSFGHGQCVQAVRDLGIPMLALGGGGYTIRNVAKLWAYETSILTGHPLPPNTVLPVAEM
PLSGWLFQDSPLLIVAQDRSNHVLPGLHCQRAYQMMTEQIDRHVPHIQPHPRLQKAATAAAAADKQVEDG
TTAVEDFKR
>gnl|CDD|240375 PTZ00347, PTZ00347, phosphomethylpyrimidine kinase; Provisional
THQFYHEPVFGGLSEALWKENQDLAMMSLHLPFVQGLGDGTLDQNAFRTYIAQDTLYLNGYIRILSYCIT
KSDVTATGGGLLELLKGVLEELKNCHHHYIDNPDAAGPEAACRKYVDFLLASGNADTLGPSVVIAAVIPC
ARLYAWVGQELTNEVELTESHPFRRWLLSYSDEPINTSVEQLESLLDKYIRPGEFSEVAQAYRRAMELEY
DFFDSFGYCLGRPVENPMKIPTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQ
VVNEDFFAAQIDSVMSDFNISVVKLGLVPTARQLEIVIEKLKNLPMVVDPVLVATSGDDLVAQKNADDVL
AMYKERIFPMATIITPNIPEAERILGRKEITGVYEARAAAQALAQYGSRYVLVKGGHDLIDPEACRDVLY
DREKDRFYEFTANRIATINTHGTGCTLASAISSFLARGYTVPDAVERAIGYVHEAIVRSCGVPLGQGTNR
PLVHSLNSVWANYV
>gnl|CDD|173541 PTZ00348, PTZ00348, tyrosyl-tRNA synthetase; Provisional
MNTDERYKLLRSVGEECIQESELRNLIEKKPLIRCYDGFEPSGRMHIAQGIFKAVNVNKCTQAGCEFVFW
VADWFALMNDKVGGELEKIRIVGRYLIEVWKAAGMDMDKVLFLWSSEEITNHANTYWRTVLDIGRQNTIA
RIKKCCTIMGKTEGTLTAAQVLYPLMQCADIFFLKADICQLGLDQRKVNMLAREYCDLIGRKLKPVILSH
HMLAGLKQGQAKMSKSDPDSAIFMEDTEEDVARKIRQAYCPRVKQSASEITDDGAPVATDDRNPVLDYFQ
CVVYARPGAVATIDGTTYATYEDLEQAFVSDEVSEEALKSCLIDEVNALLEPVRQHFASNPEAHELLEAV
KSYRKGGATLPLAETALPAAPEKPHACMWMPALIKVPLDVAEGMIDATKDFIAAHSDGTVTLVLPDWSAV
ASDEITGEEKDISAALEVNCALLKAYGLPSEVKIVRENEVILGNPNDFWVSVIGIARKNLLSHVEELYGG
ELRNAGQVIAALMRVATALMLSASHVISTSLDGGINEFAREYTKGRIECIQALEGRVPALHRPGAAPAVL
GADDVLYLDDNDMDIRRKIKKAYSAPNEEANPVISVAQHLLAQQGALSIERGEANGGNVAYNTPEALVAD
CGSGALHPADLKAAVSQLLLDRSAAARALLSGELKKNMQTLRNAEKKLSKRS
>gnl|CDD|185571 PTZ00349, PTZ00349, dehydrodolichyl diphosphate synthetase; Provisional
MALNIIERFITSLLRDFINIKHISIIMDGNRRFAKEKGLHSAIGHFMGSKALIQIIEICIKLKIKILSVF
SFSLLNYNRSPEEIHFLFYLNLLILINEDFFFKFIKDNKIKIKIIGNLSYINDAYRKIIHDIEEKTENFD
NILLNIFFSYTSRNEMSLCKFNPNLYFDTYKNLLEEKKILCGSNILTDPIKEGTFAIPDDEDECDYLDHE
LENERIDLDLKFDGDCICGEKSFLNEEQIEIVNYHKKLLTSDLPPPNILIRTSGEKRLSDFMLYQISEFT
EIYFINEYWPIFNFLQFIYIILHYTIFQTTKLDFSYSNPCPH
>gnl|CDD|240376 PTZ00350, PTZ00350, adenylosuccinate synthetase; Provisional
SFEHDSLNGLKSKVVVILGAQWGDEGKGKLVDILSEKADIVARFNGGANAGHTIVVDGKKYALHLLPCGI
LYPNCINVLGNGVVIHLPSLLEEIEQLTKKGINLLGRLYISDRAHLVFDLHQAIDGIQESEKGKGGTQIG
TTKRGIGPCYSTKASRTGLRVGDLLNFETFEKKYRKLVEKLQEQYNIEEYDAEEELERYKGYAEKLKDMI
VDTVYFMNKAIKEGKRVLVEGANATMLDIDFGTYPYVTSSNTTVGGVCTGLGIPPNAIILVIGVVKAYTT
RVGEGPFPTELFDENGDYLRKKGHEYGTTTGRPRRCGWLDIPALRYVQMINGFDSINLTKLDVLSGLKEI
KICVNYKNKGTGLEIGRYPSSIEELEEYEPVYETMPGWKTDISKCKTFEELPENAQKYVLFIEELLGVPI
VWIGVGPNRENMIVKK
>gnl|CDD|173544 PTZ00351, PTZ00351, adenylosuccinate synthetase; Provisional
MPVRRYGGRYNNSSPGVSNALSPSSTAGLPLSPSPAEGSKPASTHHDPVPQEAYYVKDEADACHQQQAPF
REPSVEVEVEIIDDEPPRGSQKPLSVAPHTANANNSSGSSKCNAITASDYTFYTNEDQKKVYEALRSLRP
LPELQEPRRVKEYAETSLKDSLYRIVEAHDVIMVAGAFFGDEGKGKTVDAVAHHPLCTCIARVNSGENAG
HTVYDKAGRKFVFNLAPSGLLLPGKRNYIGPECVMDPVSFMEKEIIQLIDAGIDYRDRLFIGNVCIVTPY
HKLLDLLGSAANSSTLKGMAPVHGSKVMKRGIRLDHIFNDDETLRKRLEKDMDTYLGLLKVKNLSDADVV
RLCREENSDGVVRVPDYVIAFAQAKDKVEFLVKLYRDRVRHNPDFPARCDVTYELHAAVLRGEKVLLEGP
QSYWLSNARTKFWESTTSADTTAAGLLAASQLNFQKFKSVVLNVHKAPGSSRVGIGACPSSFVPQDYFSA
QNIKTLRDLPSATCANFEAVQRTLFRDGFPHSNDKARHNGIMAPVEYSDETGDYNIGVAMAIASAQHHGE
CGAVTKKPRVCGFFDCVLQHEVNSIQGPYLTISALDRGDEYDKVGVTIAYVYYNPEGKQVDVNGHVYKNG
DIIRAGDPVPSEPALYHCHPIVKLIDGWRDNPIAAAKRRRNAPLPRGVCELLSTIEYFTNCKILSIGNGP
NGDDIIYLRQ
>gnl|CDD|240377 PTZ00352, PTZ00352, 60S ribosomal protein L13; Provisional
MKHNNVLPNVHLHKHWQRFVKTWYNQPGRKKRRRLARQKKAAAAGPRPVELLRPVVHGPTQRYNMKVRLG
RGFTLEELKAAGLNAQAARSIGIAVDHRRRNRSQESLNLNVKRLKAYLSKLVLFPRKGKKPKKGFAGIPA
DTSKEEVVALPVKQNKNSEVIPFQRTPKREKARVITKEERAFNAYRTLRQAKLNAKFVGKKEKKKQAKEK
KK
>gnl|CDD|173546 PTZ00353, PTZ00353, glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
LPITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGASIRVVGEQIVLN
GTQKIRVSAKHDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDER
LSASLPVCCAGAPIAVALAPVIRALHEVYGVEECSYTAIHGMQPQEPIAARSKNSQDWRQTRVAIDAIAP
YRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISK
RDMISVDCIPNGKLCYDATSSSSSREGEVHKMVLWFDVECYYAARLLSLVKQLHQIHAPPGM
>gnl|CDD|173547 PTZ00354, PTZ00354, alcohol dehydrogenase; Provisional
MMRAVTLKGFGGVDVLKIGESPKPAPKRNDVLIKVSAAGVNRADTLQRQGKYPPPPGSSEILGLEVAGYV
EDVGSDVKRFKEGDRVMALLPGGGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKK
GQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEEKVDFCKKLAAIILIRYPDEEGFAPKVKKLTGEKG
VNLVLDCVGGSYLSETAEVLAVDGKWIVYGFMGGAKVEKFNLLPLLRKRASIIFSTLRSRSDEYKADLVA
SFEREVLPYMEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLTVNEPLSL
>gnl|CDD|173548 PTZ00355, PTZ00355, Rhoptry-associated protein 2; Provisional
MKKFILISFLIFLCLNNVVDGNKCTKELYNMNTKDLSLTSIVLAHKTDRKTLGSWVYFFFNHFSNPDEAI
KYLEDININALDNEDHTCFARAFTIYLIQNYAKDIKSMSNTDNYESFFKNKLKDINPDISNDFLSILKSE
TFLGYLDSLILKEQDASHLVNDVNIFQKILSKADRNTHATYKSNPIKVFIFYDIRTFRRTYLLKEDPSIP
DSELYAARDYNFLIYLGVSENYYNSDITQPARGTSNIISKRKRLGLKKRSSSLSLLGPHNNNPIFAFCEK
DGKEEYFGTPDDLIPSFFSVMKTKMIYGHKRFLREFDYALKHKTYKMPNLKGFRFLKSLFQRKNLENFVG
MYSNLMSTEIDFLAEDFVELFDITMNCYMRQHFDRAAVNYHMIKEKNMES
>gnl|CDD|185573 PTZ00356, PTZ00356, peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
MEGDTVRAAHLLIKHTGSRNPVSRRTGKPVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAK
GGDLGFFGRGQMQKPFEDAAFALKVGEISDIVHTDSGVHIILRLA
>gnl|CDD|173550 PTZ00357, PTZ00357, methyltransferase; Provisional
MHRRIHKNGEVYTLTKHPPSRSSYLRLLLFPQSPGMSVDGGGISNGPEAQATASAMEEDYCLHGRERFQN
QWARAGVFSPASLRVYGITGEPVLMRSIKQARMLGATFGTCFLGRFPRSKSPPSSGDNDAAAVTQKDNAS
NAAGPSRSGSSYDSLPFSSLLLGPCPPPNMTADPHMLDQAWRREVAGTWSALHMPSEWCQTMNGVVTELS
WSTRAQRQRIAEQLELAAFMCLRAVQVPLPFYAADVAWSGGDDDDSRDEEDNEGGATAGTRGGAQPMSDE
EENQRNIRVACLAADVVLSFIQQCTRVKVWVRCDACNPAHRYQLQRLRQAVLYGYSTLKTDSERVIYRIN
TPCSVTSMTTSLMSDALPPSSSSSPRCGVVHTEAASSLMALLYYSTWNPRMLLPSEWFGEEVVGFECPTA
SALLACLAPHGVAPQEHPHYRPDAPGTTLAEEDVVEAQEYEHPNHGYPDEDGAPLRRTPPTYHDGESEGS
QADYSLFDWYDSVTELETSHEADSAVAAAKGGSKGSGSASDTSYEAAADCRRSHVLRSRYTYVMPEDLQP
LVASRWAGTYPPFVSALTFIVELLRRRAMPVFDRTFFDQYPLLNYLHFKGVEEPTRDVFASFEGQLQLPL
QPLSHHLSSGVYEVFERDARKYRQYREAVFHYVRDWYAAGAEQQHAHQNSEFFAKHGVMQRVPVPSPDER
TLHLVLLGCGRGPLIDECLHAVSALGVRLRIFAIEKNLPAAAFTRMRWANDPEWTQLAYTFGHTLEVIVA
DGRTIATAAENGSLTLPADFGLCDLIVSELLGSLGDNELSPECLEAFHAQLEDIQLSRGIAFNPHLMCIP
QQYTAWVAPLMSATFDAAVTEAAVKGLTVPPPGCHDHHAALNHTLLVTNLSRAVTLAPPQPCWTFEHRFH
GGSDNDYKGDRGAMKRREPVSLERAASLLFEVPPCGRCCGLAGYFSAVLYQSATAPATIIATAPVERTED
MYSWFPCVFALEPAQQAELQDVGQAAAEESRMVAIRVQLDRRTSLAEQRVWYEWSVTYGDAAVERQSPST
SHDASAAPLVHNKNGWAASMLL
>gnl|CDD|240378 PTZ00358, PTZ00358, hypothetical protein; Provisional
MDTSTCTTIVLVLLWLYLCCQALGSLVALIDEYSTTPVLPTTTTLSTVLLGVCLWQCKKAGYLVSPMTWY
HWVLLVLLVLLQVVAVVLEYLELQGWLSVSLGIKWTYPIYGIAVVLLGILGGTLYCGWKCNLFCRPCCKS
QYICYGSAIVVVLVILIVLAVTASLIAFVGRSEFVYSGDGNTEKLIIGYLGKMVVPITQCYTMAVIWNTI
LKLPYTVPEVVALIASALAVASLLAVLAIYGGTNSVLLSTQGYPFLALHLVALGITLYCLEYKKVFYWPK
DYMCFGVLAAVLLLVLVVVVVIIIDGFSQEAKNVGVKYTLLGYSMLLMIPTLWYAYRCGLFTWCLPKKKG
LKATDTAENTTPDTDIA
>gnl|CDD|173552 PTZ00359, PTZ00359, hypothetical protein; Provisional
MPGIKAGIGPYSDEAAPKVADQVRYLMPIAKLLFILVAILGFGFCMAMLLNATVEAIEIKALQTEEFKLK
NADMTALSIAICLSHLALHFLGYKCRFMKLHWTSWDSGLFILGFVVVISAFFAVFIVVMPDEGIKLGGDD
TYAGHRVYGAMGFTGLELLAMFGFIICAMKTHCFGGCMTLNKKVFYTFAFIYMLVFAAHAYTLGEFKENG
KKYGKDKETWHVHRFMAALNYIFVIGLCISAYQVNLCCMSFTKCDGVFIFLTGTVVGILITVCLSMFPEI
KQYQWTLVGLIAMLYILTVALFLYIHAKRPLCQYYNPDVITFGIFALLFLLLVSTLIALGAKHHQHISGI
AKDFKGIASIAIFVYGFVVFVLMLIFGFKGNAIKVMKAFFKQARDQRLLPNAHELEVEPLYDPGVETPGS
ECNLRGPESSGGVFRDSWLHPAK
>gnl|CDD|240379 PTZ00360, PTZ00360, sexual stage antigen; Provisional
LNLLKLAVFIFLIIYSTTSCLAATGLPSIHLSLSNAKKQVDDYFKEPEDFTPEDESVNEVILAPGDELKF
TCGNGARDEDGTHTMYPSDPKTKMLLPPEDEDFTSAVEREVANHDIFRSDDLLIESKKAKHGGVYLKISY
PVDTVIVAKDPENFSLNFACKYQPKDGNKAPVYRWLEVKFDAVYPMAYGCESGNNMLFKNSIPILPDLSH
SDVQERAQCEIEPEPGMIFGIYCKPGERLYPDDCFRDASLMDGNGDIIMFNQFRDPYFPHSGISGRFRLF
KVSDKGFDKDVYFSCYCRGKNGKTTRILIVNKLKNESCDFTKIFNNYKPGLNIPLKACRYNLSPGMSLKV
TVPKNDSIFLGRNGKVSGLLEPTNFQVYAYGQLLDDSHLREIRLNDIIGSKGLDIEKTEVKGGVTYEFKY
KDDSILVLKSETPSLSYFWVLFDRFLGVRTKVNLVLSIYIVPTDPYTYGCGVDSADLFRKEGFQFSSEEI
QVKVTKCKVNPYLNSPVGFYCPKDFVLEPSNCFEEMLNATNEEVVKLSDFAPL
>gnl|CDD|185575 PTZ00361, PTZ00361, 26 proteosome regulatory subunit 4-like protein; Provisional
MGNAQGQGNNQKDKNKKKEKKKKESPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYL
LLEEEFITNQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKE
QLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYD
DIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIV
FIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIE
FPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKA
KEKVLYRKKGNIPEGLYL
>gnl|CDD|240380 PTZ00362, PTZ00362, hypothetical protein; Provisional
MSDVFNIFKKKKKKKKKASKESSNGSQNSKKTIFMYNLSRRKKRHNEEGTFNNYGTNESQSSSTQNSNKN
EENIVLEDFPKLPLKNVELCEDFYYIFYLRDQYLIGNKNIQINNDHEILLETLLDKIENAIYEEDKEKYY
ITKKILKSIYEKMYDIYESYKYLKSNIPQLSNLYECYLNNGIFLKPKNFTKFYVRDNIHNIYTYLDNSEE
QQDNLESNNEAIYINDINISGPVFINKSLLTSFIDNIEYLPSKINSGYIYKNKIIAYDYLENLVNHILYQ
RALDELVVVKALVDIPYIDLSEIEGFDFKEMKSGERQWLPIYIAKELSHFGLVTVEFPFWFYIKNLKNIY
EREFEDQNELTDLPSPYFFEISSMFLENNIFKKVTPIETIGQRTVYKYISKVAGLVEDIRYKRLKKIMNH
LENQDVHSSIIYIDNLQISETYCVNQLLSVFFQYDKNLNSLTNSFDQRSYLLDPFENNL
>gnl|CDD|185577 PTZ00363, PTZ00363, rab-GDP dissociation inhibitor; Provisional
MDETYDVIVCGTGLKECILSGLLSVNGKKVLHMDRNPYYGGESASLNLTQLYKKFKPGETPPESLGRNRD
WNVDLIPKFIMASGELVKILLHTDVTRYLEFKVIDGSYVYQKEGKIHKVPATDMEALSSPLMGFFEKNRC
KNFLQYVSNYDENDPETHKGLNLKTMTMAQLYKKFGLEDNTIDFVGHAVALYTNDDYLNKPAIETVMRIK
LYMDSLSRYGKSPFIYPLYGLGGLPQAFSRLCAIYGGTYMLNTPVDEVVFDENGKVCGVKSEGGEVAKCK
LVICDPSYFPDKVKKVGKVIRCICILNHPIPNTNNANSCQIIIPQKQLGRKNDIYIMLVSSNHGVCPKGK
YIAIISTTVETNNPEKEIEPALKLLGPIEEKFVSISDLYEPTEDGKKDNIFISKSYDATSHFESATEDVL
DLYKRITGKDLDLTNIPETADEE
>gnl|CDD|240381 PTZ00364, PTZ00364, dipeptidyl-peptidase I precursor; Provisional
MLLLAFFQLLLSEYTPARCLSDQYLGLWSFTITKFKYLKTNDRVECPASISSRVTKLIVTLMPNGAAQEQ
GGATGRWTPVYNHGFEIRIAGLVYLFISAWAEIPNEGHYKVSSRCDKSQPGMGWATKQGIQPRSQACLYA
SLIKPLINTNVNIHYVQRPGPVNPRRLPVLVPTGDPYSKSRSARKAKTASFGFRQSFSHQLGDPPPAAWS
WGDVGGASFLPAAPPASPGRGCNSSYVEAALAAMMARVMVASNRTDPLGQQTFLSARHVLDCSQYGQGCA
GGFPEEVGKFAETFGILTTDSYYIPYDSGDGVERACKTRRPSRRYYFTNYGPLGGYYGAVTDPDEIIWEI
YRHGPVPASVYANSDWYNCDENSTEDVRYVSLDDYSTASADRPLRHYFASNVNHTVLIIGWGTDENGGDY
WLVLDPWGSRRSWCDGGTRKIARGVNAYNIESEVVVMYWAPYPDVLHPEEYFLVVRCSTIILMAILLLVA
GLISISIIGLYIVIRIRKKRETLKCISISDLDAPQKVMPLIPSGQTEISTDTSSVLLD
>gnl|CDD|240382 PTZ00365, PTZ00365, 60S ribosomal protein L7Ae-like; Provisional
MKGSVKKSKKLPAPAPLKKSKKKKQKHPLFEKTPRNFRIGGDIRPKVDLSRYVRWPRYILLQRQRRVLLQ
RLKVPPALNQFTYTLDKNQASQLLRLLSKYKPETRAEKKARLLKEAEKAAAGEEVESKKPFMLKYGLNHV
TDLVEYKKAKLVVIAHDVDPIELVCFLPALCRKKEVPYCIIKGKSRLGKLVHQKTAAVVAIDNVRKEDQA
EFDNLCKNFRAMFNDNSELRRRWGGGIMGIKSQHVIAKREKLIAMENAKKLGLVAN
>gnl|CDD|240383 PTZ00366, PTZ00366, Surface antigen (SAG) superfamily; Provisional
MARTGRMQQRRGGFRSKARKLMAVCMGGVLLLSSGQAVAEKLREGLLRRNLQSSQSSTQSGPTISGQVAT
CTLTAAAAGSATAAAATSLTLSKENLTATLECSGDNNAAVPKDLTKVCDPSKGKDDSEKCKFGASAGSGK
AVTLQSLLGASRDIQWTKTQTSETDNNGEEWTLELTESDLPLTDKAFFVGCQKTASAKAVSATKPSCKVT
VNVEARPSSVADNNVVTCAYGKNSNPKPLEVEMTTEKNTLTIDCGSEGSLNPTDYTTQYCDPQEADLEKC
TEKKFVDILPKFEESWWTKDDDKNSATLTIPETGFPESEQQFRLGCVPKKATASTKKTKNETDQTTAAAT
SSCNVIVTVKAASSASSASSSLQVVATASGAAALTGLLVGSL
>gnl|CDD|240384 PTZ00367, PTZ00367, squalene epoxidase; Provisional
YFFATVLCVVSTLLLLNRILSRLRFKPARTNYDYDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLFSKP
DRIVGELLQPGGVNALKELGMEECAEGIGMPCFGYVVFDHKGKQVKLPYGAGASGVSFHFGDFVQNLRSH
VFHNCQDNVTMLEGTVNSLLEEGPGFSERAYGVEYTEAEKYDVPENPFREDPPSANPSATTVRKVATAPL
VVMCDGGMSKFKSRYQHYTPASENHSHFVGLVLKNVRLPKEQHGTVFLGKTGPILSYRLDDNELRVLVDY
NKPTLPSLEEQSEWLIEDVAPHLPENMRESFIRASKDTKRIRSMPNARYPPAFPSIKGYVGIGDHANQRH
PLTGGGMTCCFSDCIRLAKSLTGIKSLRSIDQNEMAEIEDAIQAAILSYARNRKTHASTINILSWALYSV
FSSPALRDACLDYFSLGGECVTGPMSLLSGLDPSPGGLLFHYFSVALYGVLNLIMETGAYSIFGKQLSSF
EKLTNVASFFVDPERIKHALYLLGAATTIAAPLAKSEFVSLWRFIDPTSILANISKRIKTMVYRRQFNGK
QRKPVGL
>gnl|CDD|173561 PTZ00368, PTZ00368, universal minicircle sequence binding protein (UMSBP); Provisional
MVCYRCGGVGHQSRECPNSAPAGAAKARPCYKCGEPGHLSRECPSAPGGRGERSCYNCGKTGHLSRECPE
APPGSGPRSCYNCGQTGHISRECPNRAKGGAARRACYNCGGEGHISRDCPNAGKRPGGDKTCYNCGQTGH
LSRDCPDK
>gnl|CDD|240385 PTZ00369, PTZ00369, Ras-like protein; Provisional
MASTEYKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTIEDSYRKQCVIDEETCLLDILDTAGQEEYSAMR
DQYMRTGQGFLCVYSITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLDSERQVSTGEGQELAKSF
GIPFLETSAKQRVNVDEAFYELVREIRKYLKEDMPSQKQKKKGGLCLIL
>gnl|CDD|240386 PTZ00370, PTZ00370, STEVOR; Provisional
MLLFTFLINTLVLPHYENYLNNHYNVSLIQNNTQRTTIKSRLLAQTQNHNPHYHNDPELKEIIDKMNEEA
IKKYQQTHDPYEQLKEVVEKNGTKYTGGNDAEPMSTLEKELLETYEEMFGDESDIMLKSGMYPNDDDKSD
KSSTCECTDINNVKLAKTKGRDKYLKHLKHRCTGGICSCSLGSALLTLIGLAAAKAAAIALIASFGTSYS
KCASSISIFNMLSEESIISALKAGGVTCVSGLAGTAASAASSAFYPYGIAALVLLILAVVLIILYIWLYR
RRKNSWKHECKKHLCK
>gnl|CDD|240387 PTZ00371, PTZ00371, aspartyl aminopeptidase; Provisional
MSKKARELAQEFLNFINKTGSPFHAVQELKERLKKSGFKQLNEGENWKLEKGGKYYLTRNNSTIVAFTVG
KKFDAPNGGFKIVGAHTDSPCLRLKPNSKVTKEGFQQVGVETYGGGLWHTWFDRDLGLAGRVVYKKDGKL
EEKLIRINKPILRIPNLAIHLQTSTERESFKPNKENHLKPIISTEVYEQLNGKQDNDNSNNNHSAPLLKL
IAKELGCSVEDIVDFDLCLMDTQPSCFGGLNEEFISSPRLDNLGSSFCAFKALTEAVESLGENSSNIRMV
CLFDHEEVGSSSSQGAGSSLLPDTIERILSSLSASNNSSDDSFAKLMARSFLLSVDMAHAVHPNYPEKHQ
ANHRPKFHEGIVIKYNANQRYATNGVTASLLKAIAKKANIPIQEFVVKNDSPCGSTIGPILSSNLGIRTV
DIGIPQLAMHSIREMCGVVDIYYLVKLIKAFFTNYSKVDGSSLLD
>gnl|CDD|240388 PTZ00372, PTZ00372, endonuclease 4-like protein; Provisional
FSLILCMILSFFSGTTQKSKLQPISYIYSNVLVLSKEILSTFSEEENKVATTSTKKDKKEDKNNESKKKS
EKKKKKKKEKKEPKSEGETKLGFKTPKKSKKTKKKPPKPKPNEDVDNAFNKIAELAEKSNVYIGAHVSAS
GGVDNSPINAYNIAGQAFALFLKNQRTWNSPPLSDETIDKFKENCKKYNYDPKFILPHGSYLINLANPDK
EKREKSYDAFLDDLQRCEQLGIKLYNFHPGSTVGQCSKEEGIKNIADCINKAHEETKSVIIVLENTAGQK
NSVGSKFEDLRDIIALVEDKSRVGVCLDTCHLFAAGYDIRTKESFDKVMKEFDEIVGLKYLKAVHLNDSK
SDLGSGLDRHENIGKGKLGMETFKFIMNSKYFKNIPIILETPDVNNDEGVYKQEIKLLYSLVE
>gnl|CDD|185582 PTZ00373, PTZ00373, 60S Acidic ribosomal protein P2; Provisional
MAMKYVAAYLMCVLGGNENPTKKEVKNVLSAVNADVEDDVLDNFFKSLEGKTPHELIAAGMKKLQNIGGG
VAAAAAPAAGAATAGAKAEAKKEEKKEEEEEEEDDLGFSLFG
>gnl|CDD|240389 PTZ00374, PTZ00374, dihydroxyacetone phosphate acyltransferase; Provisional
MRFDTTRLALPEEFRRVVIVSPIDGCWLTAACACAIATSPIVPLNCRGDPKSIVVVSRIDVSRGSLYSDN
GSAHGACSSSSFAAFERACRDLTRGVSITHHTQFTTDAPSMSEASCFVPDVADDLFVYVSAWSSLSSDTH
SGLSSLDSLLRRLWSAAGASQALETASQQTRVRGSLVILADDATRRSACEMAQTHLVGWVVLLFYVPAFA
PPAFEFHLTESAVRACSGISGTLECVCLGVALGTVKHLPVGFRDPATVTPLDVALNTALLAVLLLCHGGL
AECVECAAEMQLCGAPGDNSLVWGMVAEYLMDYYGRFGDQALAAFPVAQLLDTSPTLQLPASVSDWVNYG
PSPMMPFRCYYGHRAAQRRKRLMEEVPNSTAARYLKGYLTQIDSVVKCITRTARAAASRSKASAYFAASK
PPTASSSFNVALYHSLLRRVTSDATLRPLHPYIALVEVDWDAYVKVIAQAVLEHLARQIFRSPFAFPPPR
PLYHNDIVFHGAERIPPTPLLTRKYFDDVVWTQRVGLTANGWRFAATPGLTPESLTSILAQPSIQRLMTA
LAKKEGASEKDVEARAKAILRTCGDNLNHVQCRLFGLMVRRILFRLYDRVSLNSGAFERLHRYVAMPRVA
VVLLPLHRSYIDFIIMTYLLAVMGLPLPHVCAGDDFLRMGPIATLMRGSGAFFMRRSFRDDPLYAALFKE
YVRHLVLRRRPLEFFIEGTRSRTGKTMAPKLGLLKFICDTFYEGQQELDDVLIIPVSLSYDELLETTLYA
KEQLGVSKPKENPGNLLRARSLLKRRHGKIHVHIGEPVSLRSFKDHPLQCPLPFEPKGEATTSVCKTLDT
TPSIARKSSITPPRVLTNIAWHLTHKLQRNTIITPTALVAAVLECLGPTAGAMPLAEVQQGMTWLRTNIR
RRGAALSDDCANLNPETMVRKALTHLQEFVEITDEMSEVIYVRQDVVTRLGVNICSNQLIHVFMDEAVVA
VVARAFGEVTAPHRVRRVEADVLKEQCQLLRQLLSAEFQDYLPACPYTFASWHGLELKPVAKEAAYTIPA
TADRTVLLERLQQLMRHVCEMRSSSPHLLRAEEQKKAREDILKEYVKVLRRMKRPSKM
>gnl|CDD|185583 PTZ00375, PTZ00375, dihydroxyacetone kinase-like protein; Provisional
MVSKKFINSPEKVVSEAVDGLCMTNNDSLKRIENTNVVVRSDIDKTKVLLISGGGSGHEPAHAGFVGKGW
LTAAVCGSVFASPSTKHVLAAIEYVPNGPGCLLIVKNYTGDILNFELAVEQARARGIQVETVLVADDAAF
GTKDIANRRGIAGTVLLYKILGAAAEKGASLTQLKKLADRISSNMRSIGVSLSSCSLPGNDPSSTVPPGT
MEVGLGIHGEKGLARIPFQGAKDLVKFLIGILLGKGKKRGGGKTTAIREGAKVALLVNNLGSTTDLEMSI
LAHHALRQLAQAGLTVVGVHSGRLMTSLEMHGFSLTLLPIEDEDDLQLLDTNQKPLLNFHTPQSSWATAK
GPLSALQLAKPEAEAASRKAATPTNSLLRSVLERVFETLIESENYLNELDAEVGDGDLGSGLERSSKAVL
ESLPYLPLEANVRKTLTLISKAVADAFGGSSGPLYGAFLLGGANALAEALNGGNAVDAVRAALAAGSHSI
QELGGARVGDRTMVDVLIPFAEALNSCPSVNEAASSPELLKACSEEAREAAEATALLPAKHGRSRYLEGK
ELGKKDPGAELVVAWVEALASESS
>gnl|CDD|240390 PTZ00376, PTZ00376, aspartate aminotransferase; Provisional
MDSLFSQVPLGPPDPILGLAAAFKADPSPSKVNLGIGAYRDENGKPYVLESVRKAEKIIAEKNLDKEYLP
IEGLQSFIEAAQKLLFGEASYALAEKRIATVQALSGTGALRLGFEFLKRFLPAGTTVYVSNPTWPNHVNI
FKSAGLNVKEYRYYDPKTKGLDFDGMLEDLRTAPNGSVVLLHACAHNPTGVDPTEEQWKEIADVMKRKNL
IPFFDMAYQGFASGDLDKDAYAIRLFAERGVEFLVAQSFSKNMGLYGERIGALHIVCANKEEAANVLSQL
KLIIRPMYSSPPIHGARIADRILSDPELRAEWLSELKEMSGRIQNMRQLLYDELKALGSPGDWEHIINQI
GMFSFTGLTKEQVERLIEKYHIYLLDNGRISVAGLTSKNVDYVAEAIHDVVRNV
>gnl|CDD|240391 PTZ00377, PTZ00377, alanine aminotransferase; Provisional
TMKSFTVEDINPRVVAAEYAVRGLVPARAAEIKEELKTGKGKYPFDSIVYCNIGNPQALGQKPLTFYRQV
LSLVEYPFLLEDPSVSSLFPADVVARAKEYLNAIGGGTGAYTDSAGYPFVRKAVAAFIERRDGVPKDPSD
IFLTDGASSGIKLLLQLLIGDPSDGVMIPIPQYPLYSAAITLLGGKQVPYYLDEEKGWSLDQEELEEAYE
QAVRNGITPRALVVINPGNPTGQVLTRDVMEEIIKFCYEKGIVLMADEVYQENIYDGEKPFISFRKVLLE
LPAEYNTDVELVSFHSTSKGIIGECGRRGGYFELTNIPPEVREQIYKLASINLCSNVVGQLMTGLMCNPP
REGDASYPLYKRERDAIFTSLKRRAELLTDELNKIEGVSCQPVEGAMYAFPRIELPEKAIQEAKERGLAP
DVLYCLELLESTGIVVVPGSGFGQKPGTYHFRITILPPEEQIEEMVKKIKEFHESFMKKYG
>gnl|CDD|173571 PTZ00378, PTZ00378, hypothetical protein; Provisional
MESVSWKRYDDEFKLSGILTEAARSCVDAHPARPKEYLAAYFREKCSGDEIRALVHNEVLSPAGETVLRF
TLELLNGMEVSSGALLSPSHGERDGEADATLDPAEYTTEALQNSYFPRLLQLGARDQREFDSTLRAALST
SPLANVGSAVQWALSIVASLAAARCRSVPLFQYLRALFGSLTSVETFSMPQLCITFFGPGNPSTARLALK
SVLFSPVMPSGTVLRERMQKIFAAFHHFCQSHNSSVRSDGSLHWDGFANLTDAVKLATEALRAVQLTPGT
DVCLGLRMAASTTRVPATAVADGGAWKEAKDDCEVLYSLFPGEPDVTGDQLSEYVREQLQAVPDIVVYVE
DTHCDEDTFGLQRLQAALGDSIVLSGVDVYARSEYKKVESGLRGLWTSNIVLNPCAIGTLSDVVEIVRAV
GEDEGRAVTVLVQTLAGNAATAAHLAVAMGARFLCSGGLFSAHQCEVVSQLASRQDELTHSRMLAPEAPK
FNRMDLPPLPTDEVPEIKRRGDKKKRKK
>gnl|CDD|173572 PTZ00380, PTZ00380, microtubule-associated protein (MAP); Provisional
MSAYHSSNPVEARRAECARLQAKYPGHVAVVVEAAEKAGSKVHFLALPRDATVAELEAAVRQALGTSAKK
VTLAIEGSTPAVTATVGDIADACKRDDGFLYVSVRTEQAMGAFASLCFSTY
>gnl|CDD|240392 PTZ00381, PTZ00381, aldehyde dehydrogenase family protein; Provisional
QEPDNPEIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVL
LTVAEIEHLLKHLDEYLKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTV
VLKPSELSPHTSKLMAKLLTKYLDPSYVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLT
PCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGED
PKKSEDYSRIVNEFHTKRLAELIKDHGGKVVYGGEVDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPIL
TYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNSGMGAY
HGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKSWVLSFLLKLSIPVQSEVLKSRLFVSALVFVAL
LQK
>gnl|CDD|173574 PTZ00382, PTZ00382, Variant-specific surface protein (VSP); Provisional
MTPAVCTSCDSDKKPNKDGSGCVLCSVGNCKSCVVDGVCGECNSGFSLDNGKCVSSGANRSGLSTGAIAG
ISVAVVAVVGGLVGFLCWWFVCRGKA
>gnl|CDD|240393 PTZ00383, PTZ00383, malate:quinone oxidoreductase; Provisional
MQRIKSSFSRYRSSTLNSNAVKEASRDTSNQSLNTSSGNRLGSDVYDVVIVGGGVTGTALFYTLSKFTNL
KKIALIERRSDFALVASHGKNNSQTIHCGDIETNYTLEKARKVKRQADMLRNYLTKLPPSERDSIIFKMQ
KMVLGVGEKECEFLEKRYPVFKELFPSMQLLDKKEIHRVEPRVVLKNNHTLREEPLAALYVPNELTTVDY
QKLSESFVKHARRDALVPGKKISINLNTEVLNIERSNDSLYKIHTNRGEIRARFVVVSACGYSLLFAQKM
GYGLEYSCLPVAGSFYFSGNILNGKVYTVQNPALPFAAVHGDPDIIAKGKTRFGPTALPLPLLERYNMSS
LPDFLKVWNPDLNLLAVYFDLFKDSTMRKYVLRNFLFEVPLLNKYLFLKDARKIVPSLTRKDLRYCVGYG
GVRPQLIDKVSKKLLLGEGKIDPGKGIIFNITPSPGATTCLGNAESDMREICERLGATIDEKGVKKTLLE
GEYPVDY
>gnl|CDD|173576 PTZ00384, PTZ00384, choline kinase; Provisional
MLNSNYDTSLGLEHENKTKFDSLTFKYDHSHSNLKSLCIRHVPFWNNVNPEFIEIKKMNNGITNQVYQAT
LVDGDKDRYPIKSVCIKKSSTYNSLVIDNDLQYNIAKLLGDNNFGPKIIGRFGDFTIQEWVEGNTMGIDS
LQNLSVLTGIASSLAKFHKRVTELVPKEWDRTPMFLTKISTWSQHVERIIKKYNLDFDYNELVQNYELFK
KILNNHLNTSNSITNSVLFCHNDLFFTNILDFNQGIYFIDFDFAGFNYVGWEIANFFVKLYIVYDPPTPP
YFNSDDSLALSEEMKTIFVSVYLSQLLGKNVLPSDDLVKEFLQSLEIHTLGVNLFWTYWGIVMNDKPKNE
LSKPVKFEAYAKFQYNLFKNNLRKLTDNKIVNT
>gnl|CDD|185588 PTZ00385, PTZ00385, lysyl-tRNA synthetase; Provisional
MRRWGVYSFQCLCACRLTAARQAVKGPLLPGLQLRQVASLSSSRSPLELKKPISKASATKTVTQEASRAP
RSKLDLPAAYSSFRGITPISEVRERYGYLASGDRAAQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVV
GQVGEHFTREDLKKLKVSLRVGDIIGADGVPCRMQRGELSVAASRMLILSPYVCTDQVVCPNLRGFTVLQ
DNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANA
MDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQL
AMRVNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVYDEIQRMSGVEFPPPNELNTPKGIAYMSVVMLRYN
IPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSE
LNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP
LLRQDIRSHDSKRRHKTASFFDFNKQMTLFCLSSLEQEFRRNGLSEDSCANVRELRRVIMELGQRGGENG
LPTAGGRLSEWRITLTFAIIRFICGTPRR
>gnl|CDD|240394 PTZ00386, PTZ00386, formyl tetrahydrofolate synthetase; Provisional
LLPMTTRKLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKY
VVVAGMNPTPLGEGKSTTTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLH
GTGDIHAITAANNLLAAALDTRIFHERTQSDAALYRRLTDELKKFTPIMLKRLEKLGISKTDPKQLTEEE
RVRFARLDIDPDTISWRRVTDVNDRMLREITIGQGKEEKGITRKTGFDISVASEVMAILALATDLADMRQ
RLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLEGTPVLVHAGPFGNIAHGNSSIVADQI
ALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKFHGGVEPVVAGKENLEAVR
KGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELALQEGGAADVVVTDHWAKGGAGAVDLAQA
LIRVTENVPSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCMAKTQYS
FSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGLS
>gnl|CDD|240395 PTZ00387, PTZ00387, epsilon tubulin; Provisional
PREIVTVQVGQCGNQLGHRFWDVALKEHKKINANPQYDDARDSFFENVSENVNRPGKENLKARAVLVDME
EGVLNQILKSPLGDLFDENFFVSDVSGAGNNWAVGHMEYGDKYIDSISESVRRQVEQCDSLQSFFLMHSL
GGGTGSGLGTRILGMLEDEFPHVFRFCPVVFPSAVDDVITSPYNSFFALRELIEHADCVLPLDNDALANI
ADSALSRKKKKLAKGNIKRGPQPHKYSVAKPTETKKLPYDKMNNIVAQLLSNLTSSMRFEGSLNVDINEI
TTNLVPYPRLHFLTSSIAPLVSLKDVAVGPRRLDQMFKDCLDPDHQMVAATPEAGKYLATALIVRGPQNV
SDVTRNILRLKEQLNMIYWNEDGFKTGLCNVSPLGQPYSLLCLANNCCIRNKFESMLERFNKLYKRKSHV
HHYTEYLEQAYFDETLETIQNLIDDYAYLQTAEPPKDLPRSMPDL
>gnl|CDD|240396 PTZ00388, PTZ00388, 40S ribosomal protein S8-like; Provisional
KAQKLRGIKAKLFNKKRYAEKAEMKKTIKAHEEKDVKEKVPEKVPDGAVPSYLLDREQVNRAKVLSNMLK
QKRKEKAGKWDVPIPKVKAMNEDEMFKVVKSGKRKKKSWKRLVNKVTFVGEDFTRKPPKYERFIRPTGLR
FKKAHVTHPELKTTFYLDIIGVKKNPQSNLYTSLGVITKGTIIEVNVSELGLVTQTGKVVWGKYAQVTNN
PENDGCINAVLLV
>gnl|CDD|185592 PTZ00389, PTZ00389, 40S ribosomal protein S7; Provisional
IKKLKKAEPSELEKQVAKALFELEASSKDLKADLKNLKISSVKEVTVGKDKKKAVVVFVPYRMLMIYRKI
QRKLIPELEKKLKKHVVIVAQRTILKKPVKNYKLKTRPRSRTLTAVHEAILEDLVYPSEIVGKRTRVRVD
GSKLLKVFLDPKDRKNVEEKLDAFSAVYKKLTGRDVVFEFPWDP
>gnl|CDD|240397 PTZ00390, PTZ00390, ubiquitin-conjugating enzyme; Provisional
MSISKRIEKETQNLANDPPPGIKAEPDPGNYRHFKILMEGPDGTPYEGGYYKLELFLPEQYPMEPPKVRF
LTKIYHPNIDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPEPDDPLDTSVADHFKNNRADAEKVAR
EWNQKYAKHNKL
>gnl|CDD|240398 PTZ00391, PTZ00391, transport protein particle component (TRAPP) superfamily; Provisional
VSLSSFAFLFSEIVQYCLSKSKRGYRLEDKLHEMGLRVGYKLNELLPYREKNQKRETKILSILTFISKHV
WKYLFGHSSDLLKSQDSDDEYMINDKNLLLNKFISVPKDLGHINCAAFAAGIVEGILCSAEFPANVTAHT
VEDTPKNFSTTILIKFYPEVIEREKSIQ
>gnl|CDD|240399 PTZ00393, PTZ00393, protein tyrosine phosphatase; Provisional
MPNSSDCSTLNCESHPPCNNRISGSSRGRDGVCSRSSASIPNIGRRRNCDQVIHTVYVKYFAMDSYLGNI
NYNMDYLNPVLNHPTKIEHGKIKILILDAPTNDLLPLYIKEMKNYNVTDLVRTCERTYNDGEITSAGINV
HELIFPDGDAPTVDIVSNWLTIVNNVIKNNRAVAVHCVAGLGRAPVLASIVLIEFGMDPIDAIVFIRDRR
KGAINKRQLQFLKAYKKKKKKKNCLRKCHFM
>gnl|CDD|173585 PTZ00394, PTZ00394, glucosamine-fructose-6-phosphate aminotransferase; Provisional
MCGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDGTAASAPTPRPCVVRSVG
NISQLREKVFSEAVAATLPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSNNGEFTIVHNGIVTNYMT
LKELLKEEGYHFSSDTDTEVISVLSEYLYTRKGIHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRK
GSPLMVGIRRTDDRGCVMKLQTYDLTDLSGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYN
AAERQRSIVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFTQQSIRA
ILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMA
LQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLLSSDSVRLQER
RNEIIRGLAELPAAISECLKITHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGIH
SGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAASEIVLVPKTV
DCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ
>gnl|CDD|185594 PTZ00395, PTZ00395, Sec24-related protein; Provisional
MNNHIGEEASAEVLSGRNNTGDDGVHGGSCHPSHCSPQPRGDKFNDKFEFAGEGEKPNLLVDANENHINT
RSSDNNSCENANMNRDANSSSENVGNANGNNYDNRAHVGRAYGAGACEQSNQQSNIPIGDPVNHLRGHPN
FGEPRERAEDAAPHAQHNHSGKTNGDNPPTGGQYHQSGGTSRNHQMMDSNKNCPADALFNETNPSGEHKR
NSIDGDIPSDIYIDSQPNEGDVQKTNPWQGKQGNSATSPPANENNAVTLSCSNDQQRGASSAAESGYAHH
RGSNIASHTPNDNIMHAANNPLNNTNDAQRNAIQGDLVRGAPNDKNSFDRGNEKTYQIYGGFHDGSPNAA
SAGAPFNGLGNQADGGHINQVHPDARGAWAGGPHSNASYNCAAYSNAAQSNAAQSNAGFSNAGYSNPGNS
NPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNPPYSNLPYSNTPYSNAPLSNAPPSSAKDHHSAYHAAYQH
RAANQPAANLPTANQPAANNFHGAAGNSVGNPFASRPFGSAPYGGNAATTADPNGIAKREDHPEGGTNRQ
KYEQSDEESVESSSSENSSENENEVTDKGEEIYSLLKKTINRIDMNKIPRPIINTQEKKKKKNLKVFETC
KYISPPSYYQPYISIDTGKADPRFLKSTLYQIPLFSETLKLSQIPFGIIVNPFACLNEGEGIDKIDMKDI
INDKEENIEILRCPKCLGYLHATILEDISSSVQCVFCDTDFLINENVLFDIFQYNEKIGHKESDHNEHGN
SLSPLLKGSVDIIIPPIYYHNVNKFKLTYTYLNKNINQTAFMITNKIMSFTKHISNSLVANDSKGGNKAT
SASAFGDSGDANFLAGGGYTNYGGAGGYNTYDNQSGYNNHDVVNNRGGSGAGNHLYGKDHDVQNFDNVMD
NANFTIHDMKNLICEKNGEPDSAKIRRNSFLAKYPQVKNMLPPYFVFVVECSYNAIYNNITYTILEGIRY
AVQNVKCPQTKIAIITFNSSIYFYHCKGGKGVSGEEGDGGGGSGNHQVIVMSDVDDPFLPLPLEDLFFGC
VEEIDKINTLIDTIKSVSTTMQSYGSCGNSALKIAMDMLKERNGLGSICMFYTTTPNCGIGAIKELKKDL
QENFLEVKQKIFYDSLLLDLYAFNISVDIFIISSNNVRVCVPSLQYVAQNTGGKILFVENFLWQKDYKEI
YMNIMDTLTSEDIAYCCELKLRYSHHMSVKKLFCCNNNFNSIISVDTIKIPKIRHDQTFAFLLNYSDISE
SKKQIYFQCACIYTNLWGDRFVRLHTTHMNLTSSLSTVFRYTDAEALMNILIKQLCTNILHNDNYSKIII
DNLAAILFSYRINCASSAHSGQLILPDTLKLLPLFTSSLLKHNVTKKEILHDLKVYSLIKLLSMPIISSL
LYVYPVMYVIHIKGKTNEIDSMDVDDDLFIPKTIPSSAEKIYSNGIYLLDACTHFYLYFGFHSDANFAKE
IVGDIPTEKNAHELNLTDTPNAQKVQRIIKNLSRIHHFNKYVPLVMVAPKSNEEEHLISLCVEDKADKEY
SYVNFLCFIHKLVHKRIDES
>gnl|CDD|240400 PTZ00396, PTZ00396, Casein kinase II subunit beta; Provisional
MDMEFSDEESSYSEEPSEESMGWIEWFCSLKGHEFLCEVDEDFIRDEFNLYGLKSKFPFYNEALDMILDS
EPPDDEDLEDEQFLEVYQEASDLYGLIHARFITTPKGLALMREKYLQGKFGHCPRVLCEGQNVLPIGLSD
VLKTSRVKVYCPRCQEVYHPKKSSLLDIDGAFFGTSFPHLFLMTYPELIPTKPPQYYVPKIFGFKVHKKK
SSKEYKLQNGEFGKSAIEQFLKKSPKGNIELQEQEQQAIQT
>gnl|CDD|240401 PTZ00397, PTZ00397, macrophage migration inhibition factor-like protein; Provisional
MPCCQVSTNVNATDDQADAALSDIENAIADVLGKPLSYIMSGYDYQKHMRFGGSHDGCCFVRVTSIGGIS
RSNNSSIAAAITKILASHLKVKSERVYIEFKDCSAQNWAFNGSTFG
>gnl|CDD|173589 PTZ00398, PTZ00398, phosphoenolpyruvate carboxylase; Provisional
MSGQSKDSKIHNSNLYPDGFKKDFCTFLEDQQKLKSEKLKVILEDFQEPLDLDIKALEFLLFDLVKDHWP
EDGFEIIFDILKLSMKFSENEDSESFNTLWKKIYNLDSGYLGLVVRLFNHMCVLSNYAEWAHRIRRRRAF
ERSFTDNDRIFTESLKNTIEMLLQAGFDKEEIYKQLCNQEIDLVLTAHPTQAQRISVLKNCQRLGELLLS
LDNTDLTPFEIKDLKKNLQRLLAMLWKTDTIRRAKPTPLDEAQNLINTIENTIFDALPNFIRYIDNVLYE
YNLDPLPPTKKLFTFSSWVGGDRDGNPFVTAEVTRQVVYFNRIRACELFIHMIEKLMYDLPLKSCTEKLK
EYVDNLPDEISFYITDKDATYLLREFMGFIPEKELYRRALLHVRAKLIATRDYYKDLISNHSVDPEFRRE
LAYHSTDEILEPLIECYNSLEDVGNTILARGRLLDVIRQVKTFGLHLMKLDIRQESSKHEKAMDEICEYL
GLGNYSELSEEEKQDFLLDILPSKRPLIPHDLNWPSEVNEVLDTFKVCSELENEALGAYIISMCRNPSDI
LLVHVFQKEILKSGASKRQRVVPLLETIESLNSSSKTLEELFSNPWYLKHLKTVDNGIQEIMIGYSDSGK
DGGRLTSAWELYKAQERLSNIARQYGVEIRFFHGRGGSVSRGGGPQHLAILSQPPNTIKSYLRITIQGET
ITQNFGLKGICLRTWELYMSALLKCSLLADPIPVKQEWRELMDEMSEISMKEYRKVVRENPDFVPYFRSV
TPEKEIGELNIGSRPSKRKEGGIETLRAIPWVFAWTQNRLHLPVWLGLEDALEELKKKGKLNLIADMYKN
WPFCKSFFNLVSMVLLKTDVQITEEYNKMLVPEQLQYIGNLLRNKLKKTTNLILLVTKEKQLLDNDIVTK
RSILLRFKWVAPCNLIQIEALKRLRKINDSTYDEDTKNEIEDTSLEDALIISIKAIAAGMQNTG
>gnl|CDD|240402 PTZ00399, PTZ00399, cysteinyl-tRNA-synthetase; Provisional
FKNNIIFLALAGLNGTGQVSKSRLPEWKKPSKEGKYLTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTV
YDSSHLGHARTYVTFDIIRRILEDYFGYDVFYVMNITDIDDKIIKRAREEKLSIFLELARKWEKEFFEDM
KALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESNGSVYFDVEAFRKAGHVYPKLEPESVADEDRIA
EGEGALGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKF
PHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKP
MNYSDESMDEAIEKDKVFFNFFANVKIKLRESELTSPQKWTQHDFELNELFEETKSAVHAALLDNFDTPE
ALQALQKLISATNTYLNSGEQPSAPLLRSVAQYVTKILSIFGLVEGSDGLGSQGQNSTSENFKPLLEALL
RFRDEVRDAAKAEMKLISLDKKKKQLLQLCDKLRDEWLPNLGIRIEDKPDGPSVWKLDDKEELQREKEEK
EALKEQKRLRKLKKQEEKKKKELEKLEKAKIPPAEFFKRQEDKYSAFDETGLPTHDADGEEISKKERKKL
SKEYDKQAKLHEEYLAKGGKS
>gnl|CDD|240403 PTZ00400, PTZ00400, DnaK-type molecular chaperone; Provisional
MASLNKKLIVKSLLTPSIALVLSSAMRSLCTSAIRFAKATGDIVGIDLGTTNSCVAIMEGSQPKVIENSE
GMRTTPSVVAFTEDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDATKKEQKILPYKIVRASNGDA
WIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIAGLDVLRIINE
PTAAALAFGMDKNDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAEFKK
QQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSGPKHLQIKLSRAKLEELTHDLLKKT
IEPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEI
KDLLLLDVTPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQ
FDLVGIPPAPRGVPQIEVTFDVDANGIMNISAVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQD
EKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKDELKQKITKLRSTLSSEDVDSIKDKTKQLQEASW
KISQQAYKQGNSDNQQSEQSTNSEESEEKNDNA
>gnl|CDD|173592 PTZ00401, PTZ00401, aspartyl-tRNA synthetase; Provisional
MSSNHADAGAPAVEKKQSDKEARKAARLAEEKARAAEKAALVEKYKDVFGAAPMVQSTTYKSRTFIPVAV
LSKPELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEGDVPKEMIDFIGQIPTESIVDVEAT
VCKVEQPITSTSHSDIELKVKKIHTVTESLRTLPFTLEDASRKESDEGAKVNFDTRLNSRWMDLRTPASG
AIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGDVP
RVFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYYEVLDLAESLFNYIFERLATHTKELKAVCQQYPF
EPLVWKLTPERMKELGVGVISEGVEPTDKYQARVHNMDSRMLRINYMHCIELLNTVLEEKMAPTDDINTT
NEKLLGKLVKERYGTDFFISDRFPSSARPFYTMECKDDERFTNSYDMFIRGEEISSGAQRIHDPDLLLAR
AKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTTP
>gnl|CDD|240404 PTZ00402, PTZ00402, glutamyl-tRNA synthetase; Provisional
MFRFMRRFGPMIMLINILLKALTSFLSNTYFTAANANEENDKLQLTNAEEGKVVTRFPPEASGFLHIGHA
KAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDLMYEKAEELI
KKGLAYCDKTPREEMQKCRFDGVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDNENKAMRDP
VIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFS
RLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWY
FNTQILDPSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVALLKEG
DEVTLMDWGNAYIKNIRRSGEDALITDADIVLHLEGDVKKTKFKLTWVPESPKAEVMELNEYDHLLTKKK
PDPEESIDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVDDVTPKKVLIAIPDGREKVNHLSA
KAQYLKTLPKKGIASAANDLAAKRAAKAAKKAAQKQASKSS
>gnl|CDD|173594 PTZ00403, PTZ00403, phosphatidylserine decarboxylase; Provisional
MKKNKRDSNFFSLYKKYLITGVTILSFILMFQYKYHEVLTLHDNSENAQQSSKLFWARLLFGRTRSRITG
SIFNIEIPNTYRLPIYNFLIKYMGINKEEIKYPIESYKSIGDFFSRYIREETRPIGDVSDYSIVSPCDSE
LTDYGELSSEYLENVKGVKFNVNTFLGSDMQKKYNDGSTKFFYAIFYLSPKKYHHFHAPFNFKYKIRRHI
SGELFPVFQGMFKIINNLFNINERVILSGEWKGGNVYYAAISAYNVGNIKIINDEELVTNNLRTQLSYMG
GDINTKIYDSYKSVEVGDEVGEFRMGSSIVVIFENKKNFSWNVKPNQTVSVGQRLGGVGEPVREKNRFIK
IRS
>gnl|CDD|173595 PTZ00404, PTZ00404, cytochrome P450; Provisional
MMLFNIILFLFIFYIIHNAYKKYKKIHKNELKGPIPIPILGNLHQLGNLPHRDLTKMSKKYGGIFRIWFA
DLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYHGIVTSSGEYWKRNREIVGKAMRKTNLKHIY
DLLDDQVDVLIESMKKIESSGETFEPRYYLTKFTMSAMFKYIFNEDISFDEDIHNGKLAELMGPMEQVFK
DLGSGSLFDVIEITQPLYYQYLEHTDKNFKKIKKFIKEKYHEHLKTIDPEVPRDLLDLLIKEYGTNTDDD
ILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIK
ETLRYKPVSPFGLPRSTSNDIIIGGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDSNDAFM
PFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSIDGKKIDETEEYGLTLKPNKFKVLLEKR
>gnl|CDD|173596 PTZ00405, PTZ00405, cytochrome c; Provisional
MPPKARAPLPPGDAERGEKLFKGRAAQCHTATKGGSNGVGPNLFGIVNRKSGTVEGFAYSKANADSGVIW
TPEVLDVYLENPKKFMPGTKMSFAGIKKPQERADVIAYLETLKD
>gnl|CDD|173597 PTZ00407, PTZ00407, DNA topoisomerase IA; Provisional
MLRRTVRALEKLVIVESPNKVIKVEGLLSDPKVIPDWSFKQSHLRRIGTGAEKAVAMATTGHFMALKEIT
WSPQASSPASVVGAGDEPFPSNGTLAEYTLEWELLPGRRIQETLERYIEEKADNVTEIILATDPDREGEL
IAVHALQTIKRLYPKLKVPFSRAYMHSITEDGIRKAMRERHVEACDYDLANAAETRHAMDRIFGFLGSSV
VRAANSQMRSIGRVQTPALILINEREDKIKAFLESNKSTFEVQAMCQFPSPHGTTFSQVVTITPDRKGGA
SHWATEAEARRCLEQWKLNNCTGFSVPLEPKPQPSVVPPPQPFTMATAIAKANRQLKYSSEMVSGCLQDL
FQLGHITYPRTDSTRIDESALPDIYAAVKKEFGKEFLYRLEDRTVSAQEGKGSKKTGKKRSTKQKKGADT
PVGNVEDAHEAIRPTNIDTTGESLSLSPPTRAVYDLVRRNTLAVFMIPMKTEKIVATVKFTSGSGEKLEF
ELQGKRVVEPGWTRAFHKGDKGTTGPAEETDEDITAVEEGAPVVPSLSQEEFKAIMNLRSQLGSGVQKGF
FELRSPQVRENRPVPPLPHSEGTLIEELKNNGVGRPSTYPMIVKTLLARGYIAVNPKGRCETTPVGRMLV
ETAKSTFPSIVDIGFTAAFEKKLDRIAKPGPAKRPALLRPTNVSQADYVLSMFLSTFLNYVTEATKAQRA
AIVERSMRLKQEQEGGSGTDDAEFEESVVKAKKKVALAVPDLVDLPKTYRNFTALQRSLNDYLRRNFPPS
RLGAAAVAPASADGNARSYGSSPSTKKKLSKGSTV
>gnl|CDD|240405 PTZ00408, PTZ00408, NAD-dependent deacetylase; Provisional
MKACRCITILTGAGISAESGISTFRDGNGLWENHRVEDVATPDAFLRNPALVQRFYNERRRALLSSSVKP
NKAHFALAKLEREYRGGKVVVVTQNVDNLHERAGSTHVLHMHGELLKVRCTATGHVFDWTEDVVHGSSRC
KCCGCVGTLRPHIVWFGEMPLYMDEIESVMSKTDLFVAVGTSGNVYPAAGFVGRAQFYGATTLELNLEEG
TNYSQFDESIYGKASVIVPAWVDRVLKLSNAN
>gnl|CDD|173599 PTZ00409, PTZ00409, Sir2 (Silent Information Regulator) protein; Provisional
MGNLMIFFQKKVTKSITLEDLADMIRKCKYVVALTGSGTSAESNIPSFRGPSSSIWSKYDPKIYGTIWGF
WKYPEKIWEVIRDISSDYEIELNPGHVALSTLESLGYLKFVVTQNVDGLHEESGNTKVIPLHGSVFEARC
CTCRKTIQLNKIMLQKTSHFMHQLPPECPCGGIFKPNVILFGEVIPKSLLKQAEKEIDKCDLLLVVGTSS
SVSTATNLCYRAHRKKKKIVEVNISKTYITNRISDYHVRAKFSELAQISDILKGRSEKNKK
>gnl|CDD|185600 PTZ00410, PTZ00410, NAD-dependent SIR2; Provisional
MSPRAPHQEHVVGEPTFEGLARYIERNNVTKILVMVGAGISVAAGIPDFRSPHTGIYAKLGKYNLNSPTD
AFSLTLLREKPEVFYSIAREMDLWPGHFQPTAVHHFIRLLADEGRLLRCCTQNIDGLERAAGVPPSLLVE
AHGSFSAASCIECHTPYDIEQAYLEARSGKVPHCSTCGGIVKPDVVFFGENLPDAFFNVHHDIPEAELLL
IIGTSLQVHPFALLACVVPKDVPRVLFNLERVGGLMFRFPTDPLTTFHADSVAKEGRSSSSSSRSSSDSS
TSSSSDGYGQFGDYEADPGGVCRDIFFPGDCQESVRRLAEALGLGEALAKRVREGEAAPETARRCENET
>gnl|CDD|240406 PTZ00411, PTZ00411, transaldolase-like protein; Provisional
MPNQLEALKEHTTVVADTGDFSLLKKFQPEDATTNPSLVLAAAQMPEYAHLIDDAIKYAKANVSRLRDPL
LSDEEKEELVELVVDKLTVNFGVEILKIVPGRVSTEVDARLSFDKQAMVDKARKIIKMYEEAGISKDRIL
IKLASTWEGIQAAKALEKEGIHCNLTLLFSFAQAVACAQAGVTLISPFVGRILDWYKKPEKAESYVGAQD
PGVISVTKIYNYYKKHGYKTIVMGASFRNTGEILELAGCDKLTISPKLLEELANTEDGPVERKLDPEKLT
EDTEKLPELTEKEFRWELNEDAMATEKLAEGIRNFAKDLEKLENVIRAKLTEA
>gnl|CDD|240407 PTZ00412, PTZ00412, leucyl aminopeptidase; Provisional
MLKRVLSRGPLPISLSVGPWFSQDIGRVAGKSKLTANAGKVAKSRGVSVHFLTPAECAEALGDASAPIPF
GFRKAAGNRRLDEERRELFAGMGAKPTVRDYRLAVTAAVREAKKLNASALVLHSLPQDVFSMGDLFQPPS
RLPSHDVVEKTAIFAVTAAYQYDRLKSGAKGGLTRARRAESRAKPPAAPQPPMELVIDSSNAQAIAAGNI
IGHCVNEARNLGNLREDEGVPQFYAEWIKKELAPLGIKVRKVLRGEQLEGAGLNLMYNVGKGSRHEPYLV
VFEYIGNPRSSAATALVGKGVTFDCGGLNIKPYGSMETMHSDMMGAATVMCTLKAIAKLQLPVNVVAAVG
LAENAIGPESYHPSSIITSRKGLTVEVLNTDAEGRLVLADTLTYVQKDAKLDKKPTTIIDIATLTGAIIV
GLGSRRAGLFSNDAHLAQSLMASGRSSGEELWPMPIGDEHKDAMKGGIADLINVASGREAGSCTAAAFLS
NFVEPEVKWAHLDIAGVGMGGDKPKGFQPAGAPGFGVQLLVDYFRHNKPPKRKGIKKAQNAKKDLKVVQK
KRHGRRRKQ
>gnl|CDD|240408 PTZ00413, PTZ00413, lipoate synthase; Provisional
MFLTPSFYLYSFFSAAARAKCGIGKPSESTKSAVADVPPKDPQVKQIFLERFRERLNSDKTGKNSLEGFV
DLPEGLKPSAASIGPIKRGEEPLPPWFKVKVPKGASRRPRFNRIRRSMREKKLHTVCEEAKCPNIGECWG
GGDEEGTATATIMVMGDHCTRGCRFCSVKTSRKPPPLDPNEPEKVAKAVAEMGVDYIVMTMVDRDDLPDG
GASHVARCVELIKESNPELLLEALVGDFHGDLKSVEKLANSPLSVYAHNIECVERITPYVRDRRASYRQS
LKVLEHVKEFTNGAMLTKSSIMLGLGETEEEVRQTLRDLRTAGVSAVTLGQYLQPTKTRLKVSRYAHPKE
FEMWEEEAMKMGFLYCASGPLVRSSYRAGEYYIKNLVKQRRKAKTHAN
>gnl|CDD|173604 PTZ00414, PTZ00414, 10 kDa heat shock protein; Provisional
MFRFTVPALKKLQPLGQRVLVKRTLAAKQTKAGVLIPEQVAGKVNEGTVVAVAAATKDWTPTVKVGDTVL
LPEFGGSSVKVEGEEFFLYNEDSLLGVLQG
>gnl|CDD|185603 PTZ00415, PTZ00415, transmission-blocking target antigen s230; Provisional
MGKIAKLKNLFLIILLVIFAEEKDHGANAIIGNGICDDEDKRFHLFIHREILEGTHESKEGKNKKECFDK
NGGIYNLGDAIRMGKDTSVKIKQRTCPFHKEGSSFEMGSKNITCFYPIHGKAEIGDLDMIIIKRRRARHL
AEEDMSPRDNFVIDDDDEDEDEDDDDEEDDEEEEEEEEEIKGFDDEDEEDEGGEDFTYEKSEVDKTDCFK
FIEAGAGDDVFDKIDEAFETTEKGDGAVLQASDDEVDKFASNNTNKEYVCDFTDHIKMKEAGKKVKICEM
KINEPLIKVKIICPLKGADEIKYDNIEFFPKKAPYVTLTKANEGSEEKEEKLKEKLLAALIHGLIISPEV
NEKENNFEEGVIEFTLPPVLHEAKKFYFICDNGKSADDDNKHGDRGIAAITIEPYGNKIKGCAFLDEDEE
EEKYGNQIEEDEHNEKGKGKHFFSQDIEEGADIKHPCVFKLNAGDIGGILFPEGIKSTSCFDEMIPHNAE
EKWDKEKKSLGNLINGAVVYNKDFKAKYFNVKYFHIPKSFKDALHLFCHIILKDEDSNLISKKHLVYISI
NEELNFSLFDFYEAFANIKKTIQIAKKNDDKKEHDYTCDFTDKLDKKAGESANGKKLFICRKHLKEFDSF
NLKCAINKAKYANIEIFPKMLKDEKKKKKEVLKLDLDIQYELFKKFFHFHDKNAKYLNGYPSFFIFPFNH
IAKKELKKNPLFKNHKDSKYFDESAVLSPLSPADGFGKLLNFLDAQDTVCLNEKIRYLDLSINEEGSDED
LFSLQFQIPPYIDIKEPFYFLFGCNNNKDEGNIGIVELLISKNEEKIKGCNFHDGKLDHFNENIGSDGEE
CNIHAFENDIIGFNCLETTLHPNDEAEDSADAEIVIEPEGCFNNVYKGLNKTDITSILKGALLYNINAKK
SKAFIKIPPVLLKDDFEFSCKCKIEQVQKEIEVIIRKERESKDAVIAELEQEAESTGDDKDEGGMIYKCA
HENFIEPKLEKLDDENVENTCHIDAEEFFNYIEIFCPAKDLGIHKNINLYFDIVKPTKVEQFKKFNNEEL
EKLIPHAEMLHKTKEILILQSCTSGEEKVDILHFYLFFPIYIKDEQEFNILCDNSKTMFEGKLGGKLIYH
IKVPKREKKIKGCDFDAEHAEAFSLNESNAKDCIIDAKPKDLIGFVCPPGTLKITNCFKDAIVGDNLINI
NEALELKDNLANFTHKHQFNYLEIPALMDKDISFKCICVDLKKKDYALKSPLGAKLLEAIYKKLNIKFGD
GYNKGEDKNKFLMSSLDLHLSHKKNQIKEIFHDLDAKKPADEDANPEQIFEELAGNESNDDVTGAPCPMG
DIDAEHIIGDDYDTFESLSDELLEETITNDIESLEAKDFEQYTLKVNLKAPKLLKPAKIHDNEHLCDFSK
KNLIVPEPLKEEEELGGNPPDIHCYAALKPLDTLYVKCPTEKAAYEAAKGKIGEEDEEEAKGIIALIEGD
FADAEDLESKKPGNGDVVVHNGVVDSAPPLDDASFEKYFEKIKIKPDGFFEKVINEYDDGDEEEDIERIL
PGAANSPMIVLKKKDPFTSYAAFIIPPIVPKDLFFKVECNNDEYKDEAKNIGGYKGIIHIDISNSEKKII
GCDFSAENSSIFTKGVKLPNGESKECEIEANKNDIFGIICDNESNFDPEKCFHEIYDKAGGKVKKFKELI
PDIDIFSLHNSNKKKVAYAKIPLDYINKILFSCSCKKADDNTIGTIKVILNKDEAEEEDFKLADAIKHGN
VHFCNFFDDEALMFDKNPEKIVLCKIDADLFSEVIIILPIFGSKNGEEGVQNAEHKKFSLKPPLTFDDEG
EDIKVIGDEKNEVSISLALKGVYGNRIFSFDKNGKKGEGISFFIPPIFEDKDFKFIINESGDLSNIKQRG
IIFIFVRKNSEEGSFKLCDFTSGENSLAELDHQNKEKKCSVKIAKGDIFGIKCPKGFAIFPEACFSNVLL
DYYKGDLEDVGGEAEVEGYDADINYYIAEDKKTNLKIKDLIELLDDEDRELEDIQKFSEFSNIPDMLHFE
NFHLGNLHLDFKKAYSSAYAKVPDKFNSAIKFSCNCYNPEKHVFGTMDVESDNANFDEEKPIKADNFIKN
FLLPLIEKIAIDADDEEPIKEIDAQDDEEAQEQILKDQDDRLEGCDDENGNCGNILSDGIEHICDFEKNE
SLFSLIEGDTKKIQKNICKIDAKALDVVTIKCPAIANFTHADGFADEALITEDEKIIITFDDENFVTYID
EKPKKKTFSLKDIYDKEFYGMSLDELNKIKKIDAEWDDHHLFYPPHNVLHDVVLANHITKLEEALEGVLF
LKSKVNDDETATKKNTELIADGVSRFIIPPYVKEDFQFHLFCGKSSEKKPNGKNTSLALIHIHISANRKE
IHGCDFLYLENQTNDAINEKEDNHLSIFTHKKETANNLICDISLIPKTVIGIKCPNGKLLPDSCFDETYY
VAEEDAPSKTIAADKVGSFPKDKIGNIIKGAIPINNFAEKDNTYTYLILPEDFEEELADLKKHFACTCDN
EGIIHMKIEKITLDKIKIDEDKRIDKDICKYDSTKKVATCEIIDFIDSLALKDHHTNHYSIQLAKWDKLI
IKYPTNEKEHFEKFFINPFNIKDKVLFNYKKPIHIEDILPGAITTDILDSRTKIIEYILRIPPYVHKDIH
FSIEFNNSLSLKKQNQNIAYGGVAEIFIHINEGYKEIHGCDFTGKYNHLFSHNFAPLLKDDDICNVTFGN
NSFAGFACLSHFEIKPHNCFASVYDRNDAEKVKKLFDLSEEAELDFIKQNSRGVSLSYIIFKKDSKKHKF
SCKCSSNQSNHTINITFDPDADHPEPKSRAIIKYFDLQDANFAKHLRGG
>gnl|CDD|240409 PTZ00416, PTZ00416, elongation factor 2; Provisional
MVNFTVDQIREIMDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITI
KSTGISLYYEHDLEDGDDKQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQA
LQERIRPVLFINKVDRAILELQLDPEEIYQNFVKTIENVNVIIATYNDELMGDVQVYPEKGTVAFGSGLQ
GWAFTLTTFARIYAKKFGVEESKMMERLWGDNFFDAKTKKWIKDETNAQGKKLKRAFCQFILDPICQLFD
AVMNEDKEKYDKMLKSLNISLTGEDKELTGKPLLKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENL
YEGPMDDEAANAIRNCDPNGPLMMYISKMVPTSDKGRFYAFGRVFSGTVATGQKVRIQGPNYVPGKKEDL
FEKNIQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQYLVKSGTITTSETAHNIRDMKYSVSPVVRVAVEPK
NPKDLPKLVEGLKRLAKSDPLVVCTTEESGEHIVAGCGELHVEICLKDLEDDYANIDIIVSDPVVSYRET
VTEESSQTCLSKSPNKHNRLYMKAEPLTEELAEAIEEGKVGPEDDPKERANFLADKYEWDKNDARKIWCF
GPENKGPNVLVDVTKGVQYMNEIKDSCVSAFQWATKEGVLCDENMRGIRFNILDVTLHADAIHRGAGQII
PTARRVFYACELTASPRLLEPMFLVDITAPEDAMGGIYSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAE
SFGFTAALRAATSGQAFPQCVFDHWQVVPGDPLEPGSKANEIVLSIRKRKGLKPEIPDLDNYLDKL
>gnl|CDD|173607 PTZ00417, PTZ00417, lysine-tRNA ligase; Provisional
MFSFLLPILRYHKNVGSHFYKQHSFSKIILNKNKNIICPVHCKQCFVTMSEKKEHVMEGEKKVRSVQASK
DKKKEEEAEVDPRLYYENRSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQDLASGEHLEDTILNVTGR
IMRVSASGQKLRFFDLVGDGAKIQVLANFAFHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFP
KETIILSPCLHMLPMKYGLKDTEIRYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTM
NLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFY
WAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKDGPEKDPIEIDFTPPYPKVSIVEELEKLTNTKLEQP
FDSPETINKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKYPNKPFFIIEHPQIMSPLAKYHRSKPGL
TERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGID
RITMFLTNKNCIKDVILFPTMRPAN
>gnl|CDD|240410 PTZ00418, PTZ00418, Poly(A) polymerase; Provisional
MHTVYESENLLDCSNFELSSKLSIEAFSQLSSSKSENEETYLSYSIECALSYGVTDPISLNGPTEEDLKL
SNELINLLKSYNLYETEEGKKKRERVLGSLNKLVREFVVEASIEQGINEEEASQISGKLFTFGSYRLGVV
APGSDIDTLCLAPRHITRESFFSDFYAKLQQDPNITKLQPVPDAYTPVIKFVYDGIDIDLLFANLPLPTI
PDCLNSLDDDYILRNVDEKTVRSLNGCRVADLILASVPNKDYFRTTLRFIKLWAKRRGIYSNVLGYLGGV
SWAILTARICQLYPNFAPSQLIHKFFRVYSIWNWKNPVLLCKIKEVPNIPGLMNFKVWDPRVNPQDRAHL
MPIITPAFPSMNSTHNVTYTTKRVITEEFKRAHEIIKYIEKNSENTWTNVLEPLDFFTSYKHFLVIQVYA
TNEHVHNKWEGWIESKIRFLIKKLETLNNLKIRPYPKFFKYQDDGWDYASSFFIGLVFFSKNVYNNSTFD
LRYAIRDFVDIINNWPEMEKYPDQIDINIKYLKKSQLPAFVLSQTPEEPVKTKANTKTNTSSATTSGQSG
SSGSTSNSNSNESSPTMSSTELLNVSSTSTTGS
>gnl|CDD|240411 PTZ00419, PTZ00419, valyl-tRNA synthetase-like protein; Provisional
KMKKEEIKLSKDEKKNKKRNISSMAASYDPKEVESGWYEWWEKSGFFKPAEDAKSLNSGKKFVIVLPPPN
VTGYLHIGHALTGAIQDSLIRYHRMKGDETLWVPGTDHAGIATQVVVEKKLMKEENKTRHDLGREEFLKK
VWEWKDKHGNNICNQLRRLGSSLDWSREVFTMDEQRSKAVKEAFVRLYEDGLIYRDTRLVNWCCYLKTAI
SDIEVEFEEIEKPTKITIPGYDKKVEVGVLWHFAYPLEDSGQEEIVVATTRIETMLGDVAVAVHPKDERY
KKLHGKELIHPFIPDRKIPIIADDELVDMEFGTGAVKITPAHDPNDYEIAKRHNLPFINIFTLDGKINEN
GGEFAGMHRFDCRRKIEEELKEMGLLRDKVPNPMRLPRCSRSGDIVEPMLIPQWYVNCKDMAKRAVEAVR
NGELKIIPSSHENVWYHWLENIQDWCISRQLWWGHRIPAYRVISKGPETDPSDEEPWVVARSEEEALEKA
KKKFGLSEEDFELEQDEDVLDTWFSSGLFPFSTLGWPDQTDDLQRFFPTSLLETGSDILFFWVARMVMMS
LHLTDKLPFKTVFLHAMVRDSQGEKMSKSKGNVIDPLEVIEGISLQDLNQKLYEGNLPEKEIKRAIELQK
KEFPNGIPECGTDALRFGLLAYTQQGRNINLDINRVVGYRHFCNKLWNAVKFALMKLLKDFNLPNSTLFK
PNNVESLPWEDKWILHRLNVAIKEVTEGFKEYDFSEATQATYNFWLYELCDVYLELIKPRLSKQSDGERK
QHAQDVLHTVLDIGLRLLHPMMPFITEELYQRLPNYLRKSESISIAKYPQPNPGWNNEALDEEMKIIMSI
VKSIRSLIATLGIPNKTKPDCYVTAKDAELIELIESAENLISTLAKIGSVSVIPPIEEEAEVPKGCGFDV
VDNKVIIYLNLDEFIDLKKELAKLEKKLAKLQKSLESYLKKISIPNYEDKVPEDVRKLNDEKIDELNEEI
KQLEQAIEELKSLLK
>gnl|CDD|240412 PTZ00420, PTZ00420, coronin; Provisional
MYNVPLIKNLYPDPSNNLFDDLRICSRVIDSCGIACSSGFVAVPWEVEGGGLIGAIRLENQMRKPPVIKL
KGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHNDESVKEIKDPQCILKGHKKKISIIDWNPMNYYI
MCSSGFDSFVNIWDIENEKRAFQINMPKKLSSLKWNIKGNLLSGTCVGKHMHIIDPRKQEIASSFHIHDG
GKNTKNIWIDGLGGDDNYILSTGFSKNNMREMKLWDLKNTTSALVTMSIDNASAPLIPHYDESTGLIYLI
GKGDGNCRYYQHSLGSIRKVNEYKSCSPFRSFGFLPKQICDVYKCEIGRVYKNENNSSIRPISFYVPRKN
PTKFQEDLYPPILMHDPERSSRNWIDGKDNKMKRINIKDLTEDDLRITKKYKFVPQSFNSIIIGENYTSK
RTSIIRQFTKKFTFFKKGEHNDGFSSVDSFKESVFIYPKSFKEKELLTEKGGAQFSSANSLERGADEDYL
IVNGTNEPYEEEVIKTNENENFPLENESPCDGISRGTSELPVNDDDNNNLNRGNTLRSEGNNCFDNLRCA
RLCRSTAT
>gnl|CDD|173611 PTZ00421, PTZ00421, coronin; Provisional
MSVSRFRHTQGVPARPDRHFLNVTPSTALWDCSNTIACNDRFIAVPWQQLGSTAVLKHTDYGKLASNPPI
LLGQEGPIIDVAFNPFDPQKLFTASEDGTIMGWGIPEEGLTQNISDPIVHLQGHTKKVGIVSFHPSAMNV
LASAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHA
SAKSQRCLWAKRKDLIITLGCSKSQQRQIMLWDTRKMASPYSTVDLDQSSALFIPFFDEDTNLLYIGSKG
EGNIRCFELMNERLTFCSSYSSVEPHKGLCMMPKWSLDTRKCEIARFYALTYHSLYTIQMLLPRKQADSE
LQVDVYPPTFADHPAITADEYFSGGNAEPLVYDMSAVFDGTSPELMGASALSPSGKPRHSGVSVPASTSA
MTHSFDDNTSKHADPCAMGVKRMDEGILDERLGRLQALSEKLRTQHEEIKRCREALQKKESIVMETLEKI
QSI
>gnl|CDD|185607 PTZ00422, PTZ00422, glideosome-associated protein 50; Provisional
IMSFCKLVLFSLFVLIFISSYSVKAQLRFASLGNWGTGSKQQKLVASYLKQYAKNERVTFLVSPGSNFPG
GVDGLNDPKWKHCFENVYSEESGDMQIPFFTVLGQADWDGNYNAELLKGQNVYLNGHGQTDIEYDSNNDI
YPKWIMPNYWYHYFTHFTDTSGPSLLKSGHKDMSVAFIFIDTWILSSSFPYKKVSERAWQDLKATLEYAP
KIADYIIVVGDKPIYSSGSSKGDSYLSYYLLPLLKDAQVDLYISGYDRNMEVLTDEGTAHINCGSGGNSG
RKSIMKNSKSLFYSEDIGFCIHELNAEGMVTKFVSGNTGEVLYTHKQPLKKRKLRFQGNALQELPALPEV
ELYPVPKGAKMLSRDAFVKIVGTIGLLIGGVHLLLTAGGSLSKN
>gnl|CDD|240413 PTZ00423, PTZ00423, glideosome-associated protein 45; Provisional
MGNYCRKNKAKEPKRRDIDELAEREKLKKEVEEIPEQKPEDIVEELEDQPEEPPEQEEENEEQKPKEEID
YPIQENKSFDEKNLDDLERSNSDIYSESHKYDNASDKLETGSQLTLSTDATGIVQQVTKLSEPAHEESIY
NTYKSVTPCDMNKLDETAKVFSRRCGCDLGERHDENACKICRKIDLSDTPLLS
>gnl|CDD|185609 PTZ00424, PTZ00424, helicase 45; Provisional
MATSEQKNQSEQVASTGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIG
QAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDI
NKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSAT
MPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKV
DYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN
YIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL
>gnl|CDD|240414 PTZ00425, PTZ00425, asparagine-tRNA ligase; Provisional
MDIQVDEEVLQKAKALQVANEEEIKMKKLKPQSEGLLSPKSDLLQVTDRGCRSRIRICNVLNVPKSEKEF
NDNSRKNKYIDQIITVCGWSKAVRKQGGGRFCFVNLNDGSCHLNLQIIVDQSIENYEKLLKCGVGCCFRF
TGKLIISPVQNENKKGLLKENVELALKDNSIHNFEIYGENLDPQKYPLSKKNHGKEFLREVAHLRPRSYF
ISSVIRIRNALAIATHLFFQSRGFLYIHTPLITTSDCEGGGEMFTVTTLLGEDADYRAIPRVNKKNKKGE
KREDILNTCNANNNNGNSSSSNAVSSPAYPDQYLIDYKKDFFSKQAFLTVSGQLSLENLCSSMGDVYTFG
PTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNFDDIYYFEENVETGLISRL
KNILDEDFAKITYTNVIDLLQPYSDSFEVPVKWGMDLQSEHERFVAEQIFKKPVIVYNYPKDLKAFYMKL
NEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFER
LIMLVTGVDNIKDTIPFPRYPGHAEF
>gnl|CDD|173616 PTZ00426, PTZ00426, cAMP-dependent protein kinase catalytic subunit; Provisional
IQFLKNLQLHKKKDSDSTKEPKRKNKMKYEDFNFIRTLGTGSFGRVILATYKNEDFPPVAIKRFEKSKII
KQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQI
VLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDTRTYTLCGTPEYIAPEILLNVGHGKAAD
WWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLSHDLTKRYGNLKKGAQN
VKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFERVQEDLTIADKITNENDPFFDW
>gnl|CDD|173617 PTZ00427, PTZ00427, isoleucine-tRNA ligase, putative; Provisional
MLRRGAESSVKISNRRLVHITLHISRNGTFFNKRIIRRRGNKAKFTPSNVRIKTMEGAEMVTVTFTGVSE
NPNIVEEEEKVLKYWKSIDAFNTSNKLAKNKKAYIFYDGPPFATGLPHYGHLLAGIIKDCVTRYFYQCGF
SVERKFGWDCHGLPIEYEIEKENNINKKEDILKMGIDVYNEKCRGIVLKYSNEWVKTVERIGRWIDFKND
YKTMDKTFMESVWWVFSELYKNNYVYKSFKVMPYSCKCNTPISNFELNLNYKDTPDPSIIISFVLCSDFP
KVEEECNIEEDKQLLGEKYSVLYNNKRENSNNGNNNSTNNVCYAQHSEILAWTTTPWTLPSNLALCVNEH
FTYLRIHHVKSNRVVIVGECRLEWIMKELKWNVEDLKIVNRFKGKELKGLRYKPLFTNFYEKYNFKERAY
KILADDFVTDDAGTGIVHCAPTYGEDDFRVCKKNGVIDPEKNIFIDPLDANGYFTNEVEEVQNLYIKEAD
NVIKKKLKNENRLLSNNTIVHSYPFCWRSDTPLIYRAIPAWFIRVSNSTNELVKNNETTYWIPAHIKEKK
FHNWIKDAKDWCISRNRYWGTPIPIWADEKMETVICVESIKHLEELSGVKNINDLHRHFIDHIEIKNPKG
KTYPKLKRIPEVFDCWFESGSMPYAKVHYPFSTEKEDFHKIFPADFIAEGLDQTRGWFYTLLVISTLLFD
KAPFKNLICNGLVLASDGKKMSKRLKNYPDPLYILDKYGADSLRLYLINSVAVRAENLKFQEKGVNEVVK
SFILPFYHSFRFFSQEVTRYECLNKKQFLFNTDYIYKNDNIMDQWIFSSVQSLTKSVHTEMKAYKLYNVL
PKLLQFIENLTNWYIRLNRDRMRGSLGEENCLQSLCTTYRTLHLFTVLMAPFTPFITEYIYQQLRRVKST
NEHNENNETGNTKEGDLNRGVIHKSVHFIMLPQVDEKYIIDYEIIELIEKMKDVILLGRVLRERRKVASK
KPLKSITILHPNESYFKNFDQISNYIKEELNVLNVECSNDTSCLDFSAIPNYKTLGVKLGYNLKKVQNKI
KNMDSESIKLYQQEGKITLDNVTLEGDDIIIQMKPNFQNDNTDIISNNYVTILMDFTTDQQLENMASARE
LCNHIQKMRKNLSLNQNSPVKMHVYIADDTLRNNMVSEMEYIKKCLRRELNVIPSQEDYQNLADKMHDEE
ITLAGKPVRVVFANQ
>gnl|CDD|185611 PTZ00428, PTZ00428, 60S ribosomal protein L4; Provisional
MTARPVVSVYSASDKSVVGTVPLPAVFTAPIRPDLVQFVHTNMAKNRRQAYAVKPLAGMQHSAESWGTGR
AVARIPRVSGGGTHRSGQGAFGNMCRGGRMFAPTKTWRRWHRKVNLNQKRHAVASALAASGVPALVMARG
HRISNVPEVPLVVSDSVESYEKTKEAVAFLKALGAFDDVNRVNDSKKIRAGKGKMRNRRYVMRRGPLVVY
ANDNGVTKAFRNIPGVDLCNVTRLNLLQLAPGGHVGRFIIWTKSAFKKLDKIFGTYTEASALKKGYTLPR
PLMTNADIARIINSEEVQAVLRPAKKKPAKRRVQKKNPLKNRRVRLRLNPAAKKLRKLAVLAQEKATAKG
AQKVKNRRARKKAKKARLAKVAKALYKSIKA
>gnl|CDD|240415 PTZ00429, PTZ00429, beta-adaptin; Provisional
MENFLRKARERIQRKLEETKTGSKYFAQTRRGEGAELQNDLNGTDSYRKKAAVKRIIANMTMGRDVSYLF
VDVVKLAPSTDLELKKLVYLYVLSTARLQPEKALLAVNTFLQDTTNSSPVVRALAVRTMMCIRVSSVLEY
TLEPLRRAVADPDPYVRKTAAMGLGKLFHDDMQLFYQQDFKKDLVELLNDNNPVVASNAAAIVCEVNDYG
SEKIESSNEWVNRLVYHLPECNEWGQLYILELLAAQRPSDKESAETLLTRVLPRMSHQNPAVVMGAIKVV
ANLASRCSQELIERCTVRVNTALLTLSRRDAETQYIVCKNIHALLVIFPNLLRTNLDSFYVRYSDPPFVK
LEKLRLLLKLVTPSVAPEILKELAEYASGVDMVFVVEVVRAIASLAIKVDSVAPDCANLLLQIVDRRPEL
LPQVVTAAKDIVRKYPELLMLDTLVTDYGADEVVEEEAKVSLLWMLGEYCDFIENGKDIIQRFIDTIMEH
EQRVQLAILSAAVKMFLRDPQGMEPQLNRVLETVTTHSDDPDVRDRAFAYWRLLSKGITVAQMKKVVHGQ
MVPVNVDSTFSDAMTMADLKKSLNTAAIVFARPYQSFLPPYGLADVELDEEDTEDDDAVELPSTPSMGTQ
DGSPAPSAAPAGYDIFEFAGDGTGAPHPVASGSNGAQHADPLGDLFSGLPSTVGASSPAFQAASGSQAPA
SPPTAASAIEDLFANGMGSGSQTVPLPISAAPQSADRDTQLNDLFS
>gnl|CDD|185612 PTZ00430, PTZ00430, glucose-6-phosphate isomerase; Provisional
PDLESLKSYKNLLSLAEKLKKVHLRDLLKDEERNKSLIKEFKGVTLDLSRQRLDEETLKLLIELAEEAKL
KEKIKDMFNGEKINTTENRAVLHTALRAPRGEKVVVDGKNVLEDVHEVLDRIKKFSDKIRSGEILGSTGK
KLKNVICIGIGGSYLGTEFVYEALRTYGEAREASKGRKLRFLANVDPIDVRRATEGLDPEETLVVIISKT
FTTAETMLNAKTVRQWLLDNIKSKEALSKHLCAVSTNLKLTSEFGIPDENVFGFWDWVGGRFSVTSAVGI
LPLSIQFGYDIVQQFLNGCHDMDEHFRTAPLEENLPVLLGLTSFYNSTFLGYNCVAILPYCQALLKFPAH
VQQLLMESNGKSVTLDGNTLDYNTGEIYFGEPGTNGQHSFYQLLHQGRVVPSEFIGFAKSQNPIKLLGEP
VSNHDELMSNFFAQPDALAFGKTYEELEKEGVPEELIPHKVFPGNRPSLLLLFPELNPYTIGQLLALYEH
RTVVEGFLWNINSFDQWGVELGKVLAKDVRNLFKDNRSNSSPHAKESKFNGSTKRLLSYYLQ
>gnl|CDD|173621 PTZ00431, PTZ00431, pyrroline carboxylate reductase; Provisional
MENIRVGFIGLGKMGSALAYGIENSNIIGKENIYYHTPSKKNTPFVYLQSNEELAKTCDIIVLAVKPDLA
GKVLLEIKPYLGSKLLISICGGLNLKTLEEMVGVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKV
IDIFSACGIIQEIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKA
SDQPVQQLKDDVCSPGGITIVGLYTLEKHAFKYTVMDAVESACQKSKSMH
>gnl|CDD|240416 PTZ00432, PTZ00432, falcilysin; Provisional
DVQTKLLPKFGYLNIISNLGKYASSLHNKAEKRRYNVFSEDFLYSINTTNLYSFTADMNKSPEWVQEAMP
VEHEAYEKIEKRYLPDFGMVATVYSHKKTGLQVISLKTNDSSGKEMCFDFYVPTPPHNDKGIPHILEHSV
LSGSKKYNYKDSFSLLVQGGFNSFLNAYTFKDRTSYLFASTNEKDFYNTADVYMDSVFQPNILEDKDIFK
QEGWHYKVTKLKDDEKNADELGNVHDRHVSYSGIVYSEMKKRFSDPLSFGYSVIYQNLFSNVYKYDSGGD
PKDIVELTYEELVEFYKTYYGPKTATVYFYGPNDVTERLEFVDNYLTKHPKTGQLSHTAYREDADENLLY
EEYKDKPKHVKKKFSSHSEEEENLMSVSWLLNPKHNGSKDYDKSLIDPVDYLALLVLNYLLLGTPESVLY
KALIDSGLGKKVVGSGLDDYFKQSIFSIGLKGIKETNEKRKDKVHYTFEKVVLNALTKVVTEGFNKSAVE
ASLNNIEFVMKELNLGTYPKGLMLIFLMQSRLQYGKDPFEILRFEKLLNELKLRIDNESKYLEKLIEKHL
LNNNHRVTVHLEAVESSKYEKEFNKLVKDELKERLSHLTKEQVDEMEKAYEKFKKEREADDDPEHLDSFP
ILSLSDLNKETEEIPTKLYKLSSDSLKENMDLDSDGGSVTVLVHPIESRGILYLDFAFSLDSLTVDELKY
LNLFKALLKENGTDKLSSEEFTYKREKNLGGLSASTAFYSETNNLTYDDPYNGVGYLNVRAKVLKHKVNE
MVDIVLEALKDADFSNSKKGVEILKRKINGMKTVFSSKGHKFALKRMKSKFSVSDYADELVNGYSQLLFL
KETLVPLAEKDWSKVESKLNEIRNKLLSMKNLTVNVTGDSELLDSLLDDSTTFLKKLSSTFKENDNKSSD
KVWVKEVLDKKLMESVDKNEFIVLPTRVNFVGMGGKLFDKSDKVDGSFQVIVHYLKNSYLWKTVRMSLGA
YGVFADLLYTGHVIFMSYADPNFEKTLEVYKEVASALREAAETLTDKDLLRYKIGKISNIDKPLHVDELS
KLALLRIIRNESDEDRQKFRKDILETTKEDFYRLADLMEKSKEWEKVIAVVNSKTSDTAPSDFKQLHIN
>gnl|CDD|185613 PTZ00433, PTZ00433, tyrosine aminotransferase; Provisional
MSFWDVSMSKHAGRVFNPLRTVTDNAKPSPSPKSIIKLSVGDPTLDGNLLTPAIQTKALVEAVDSQECNG
YPPTVGSPEAREAVATYWRNSFVHKESLKSTIKKDNVVLCSGVSHAILMALTALCDEGDNILVPAPGFPH
YETVCKAYGIEMRFYNCRPEKDWEADLDEIRRLVDDRTKALIMTNPSNPCGSNFSRKHVEDIIRLCEELR
LPLISDEIYAGMVFNGATFTSVADFDTTVPRVILGGTAKNLVVPGWRLGWLLLVDPHGNGGDFLDGMKRL
GMLVCGPCSVVQAALGEALLNTPQEHLEQIVAKLEEGAMVLYNHIGECIGLSPTMPRGSMFLMSRLDLEK
FRDIKSDVEFYEKLLEEENVQVLPGEIFHMPGFTRLTISRPVEVLREAVERIKAFCERHKKV
>gnl|CDD|185614 PTZ00434, PTZ00434, cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
MAPIKVGINGFGRIGRMVFQAICDQGLIGTEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETTKSS
PSVKTDDVLVVNGHRIKCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASG
GAKTIVMGVNQHEYSPTEHHVVSNASCTTNCLAPIVHVLTKEGFGIETGLMTTIHSYTATQKTVDGVSVK
DWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKR
ASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNNLPGERRFFKIVSWYDNEWGYSHRVVDLVRY
MAAKDAASAKM
>gnl|CDD|240417 PTZ00435, PTZ00435, isocitrate dehydrogenase; Provisional
NTGGKIKVKNPVVELDGDEMTRIIWKMIKEKLILPYLDVPIKYYDLSIENRDKTDDKVTVDAAEAIKKHK
VGIKCATITPDEARVKEFNLKKMWKSPNGTIRNILDGTVFREPIIIKNIPRLVPGWKKPIVIGRHAFGDQ
YKATDFVVDGPGKLELVFTPADGSEPQRVDVFDFKGGGVAMGMYNTDESIEGFARSCFQYALDRKMPLYL
STKNTILKKYDGRFKDIFQEIYDEEYKAKFEKAGLWYEHRLIDDMVAQAIKSEGGFVWACKNYDGDVQSD
IVAQGYGSLGLMTSVLVCPDGKTVEAEAAHGTVTRHYRQHQKGKETSTNSIASIFAWTRGLAHRAKLDNN
QELVKFCQALERSCIETIEAGFMTKDLAICVHGSSKVTRSDYLNTEEFIDKVAEKLKKKLGAL
>gnl|CDD|185616 PTZ00436, PTZ00436, 60S ribosomal protein L19-like protein; Provisional
MVSLKLQARLAADILRCGRHRVWLDPNEASEISNANSRKSVRKLIKDGLIIRKPVKVHSRSRWRHMKEAK
SMGRHEGAGRREGTREARMPSKELWMRRLRILRRLLRKYREEKKIDRHIYRELYVKAKGNVFRNKRNLME
HIHKVKNEKKKERQLAEQLAAKRLKDEQHRHKARKQELRKREKDRERARREDAAAAAAAKQKAAAKKAAA
PSGKKSAKAAAPAKAAAAPAKAAAPPAKAAAAPAKAAAAPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAK
AAAPPAKAAAPPAKAAAAPAKAAAAPAKAAAAPAKAAAPPAKAAAPPAKAATPPAKAAAPPAKAAAAPVG
KKAGGKK
>gnl|CDD|240418 PTZ00437, PTZ00437, glutaminyl-tRNA synthetase; Provisional
MTATMAGPAAAEVPELETKRDLSLLQTGRPVPGCRNTPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAK
SMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTFSSDYFDQLHEFAVQLIKD
GKAYVDHSTPDELKQQREQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFIA
YRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVWEFSRL
NVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTL
REDLDERCERRLMVIDPIKVVVDNWKGEREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRTEDNNSKFY
GLAPGPRVVGLKYSGNVVCKGFEVDAAGQPSVIHVDIDFERKDKPKTNISWVSATACTPVEVRLYNALLK
DDRAAIDPEFLKFIDEDSEVVSHGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDK
EKATVAEPVPAKKK
>gnl|CDD|185618 PTZ00438, PTZ00438, gamete antigen 27/25-like protein; Provisional
MFKKCIVVISANLLLKTAFNSSPFFAHALAIQTDREPSNTREEIISVNYEPEEQDLSEACDYIAIEEYSA
CGNVASIANDKSDNENDVELEGLNIIVKNEEERGTQKEEEEDEDVEEIEEVEEVEVVEEEYDDDEDSEKD
DEKESDAEGDENELAGEYIIEEVDDDVAILNENINSIDELEDPLDSYKSIFLIFFTEFDTTETYLNKIIN
CATDEEKNELLDDHIGILKEMYENCKKHDNFRLPFEIRDSMALRISDRLRDFCFSDPLTDSNMLALKSIF
SIELEVFEGIFYYIEHKNTYREKKEVINDLELIKFYHEELITDNGLFLTDEQFDNAAMRVSNFVNDIYFL
CFSNCQDMIIFCEIQDAMDANITL
>gnl|CDD|240419 PTZ00440, PTZ00440, reticulocyte binding protein 2-like protein; Provisional
MRKGLIYRTILCYILFILIEKSHQNNIYKVNGNNENFQFSHLNFYNEKNEEKSSNNNNNNYNNSSINRKK
DNKNYMKRSLLQLSPSLVTLNNSNDNLDYIDVSDDNGNLISSVYPHYVNIYYFKEMIHYATSYYDDLKKY
SDKINEDVEPLNEEIIKNIEQCLGNKNDLDNLIIVLENPEKYNVRKTLYDEKFNEYKNKKEAFYNCLKNK
KEDYDKKIKKINNEIRKLLKNIKCTGNMCKTDTYVDMVELYLLRVNEVPSNNYDNYLNRAKELLESGSDL
INKIKKELGDNKTIYSINFIQEEIGDIIKRYNFHLKKIEKGKEYIKRIQNNNIPPQVKKDELKKKYFESA
KHYASFKFSLEMLSMLDSLLIKKEKILNNLFNKLFGDLKEKIETLLDSEYFISKYTNIISLSEHTLKAAE
DVLKENSQKIADYALYSNLEIIEIKKKYDEKINELKKSINQLKTLISIMKSFYDLIISEKDSMDSKEKKE
SSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKDEK
LKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILN
KFYKGDLQELLDELSHFLDDHKYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQNL
LSLKENIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDK
DLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQ
KFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKTLNIAINRSNSNKQLVEHLLNNKIDLK
NKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKEKIEKQLSDTKINNLKMQIEKTLEYYDKSKENINGNDG
THLEKLDKEKDEWEHFKSEIDKLNVNYNILNKKIDDLIKKQHDDIIELIDKLIKEKGKEIEEKVDQYISL
LEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNADKEKNK
QTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEVNEIEIEYERILIDHIVEQINNEAKKSKTIME
EIESYKKDIDQVKKNMSKERNDHLTTFEYNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELKEIK
LQVFSYLQQVIKENNKMENALHEIKNMYEFLISIDSEKILKEILNSTKKAEEFSNDAKKELEKTDNLIKQ
VEAKIEQAKEHKNKIYGSLEDKQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNASRGK
DKIDFLNKHEAIEPSNSKEVNIIKITDNINKCKQYSNEAMETENKADENNDSIIKYEKEITNILNNSSIL
GKKTKLEKKKKEATNIMDDINGEHSIIKTKLTKSSEKLNQLNEQPNIKREGDVLNNDKSTIAYETIQYNL
GRVKHNLLNILNIKDEIETILNKAQDLMRDISKISKIVENKNLENLNDKEADYVKYLDNILKEKQLMEAE
YKKLNEIYSDVDNIEKELKKHKKNYEIGLLEKVIEINKNIKLYMDSTKESLNSLVNNFSSLFNNFYLNKY
NINENLEKYKKKLNEIYNEFMESYNIIQEKMKEVSNDDVDYNEAKTLREEAQKEEVNLNNKEEEAKKYLN
DIKKQESFRFILYMKEKLDELSKMCKQQYNIVDEGYNYIKKKIEYIKTLNDENNLSDSLNQAEDKNKEVA
NLTHYTNKNEAKNLLGHVVKSANFIGIKIMTGLQPTELTPDASLETAPELTFESENNSDLELDHLSSNKN
ELDVYKNIQDAYKSSLQILKYSDDIDKKQRDCNKLVEDGNEIYLKSTAINELKNMINSVKNKESAISNKI
DNVSNKLSELNKITCNDESYDEILEKEEYEELKDLRNSFNQEKAETLNNLKLNKIKEDFNSYKNLLDELE
KSVKTLKASENIKKIVENKKTSIDAINTNIEDIEKEIESINPSLDELLKKGHKIEISRYTSIIDNVQTKI
SNDSKNINDIEKKAQIYLAYIKNNYNSIKKDISTLNEYFDEKQVSNYILTNIDKANKLSSELSEAVTNSE
EIIENIKKEIIEINENTEMNTLENTADKLKELYENLKKKKNIINNIYKKINFIKLQEIENSSEKYNDISK
LFNNVVETQKKKLLDNKNKINNIKDKINDKEKELINVDSSFTLESIKTFNEIYDDIKSNIGDLYKLEDTN
NDELKKVKLYIENITHLLNRINTLINDLDNYQDENYGKDKNIELNNENNSYIIKTKEKINNLKEEFSKLL
KNIKRNNTLCNNNNIKDFISNIGKSVETIKQRFSSNLPEKEKLHQIEENLNEIKNIMNETKRISNVDAFT
NKILQDIDNEKNKENNNMNAEKIDDLIENVTSHNEKIKSELLIINDALRRVKEKKDEMNKLFNSLTENNN
NNNNSAKNIVDNSTYIINELESHVSKLNELLSYIDNEIKELENEKLKLLEKAKIEESRKERERIESETQE
DNTDEEQINRQQQERLQKEEEQKAYSQERLNREVSGTDDTNKNHNTGHDESNYGRYSNKRNDYGQVRLAG
GVIIGLSVFSSIIFISFKEKDEEEKDHDFNGNVEAFEGNDNNNLRDKEEIIEVCFNENDYIY
>gnl|CDD|240420 PTZ00441, PTZ00441, sporozoite surface protein 2 (SSP2); Provisional
MKLLQNKSYLLVVFLLYVSIFARGDNKIVDEVKYREEVCNEEVDLYLLVDGSGSIGYHNWITHVIPMLMG
LIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDKEQALIIVKSLRKTYLPYGKTNMTDALLEVRKHL
NDRVNRENAIQLVILMTDGIPNSKYRALEESRKLKDRNVKLAVIGIGQGINHQFNRLLAGCRPREGKCKF
YSDADWEEAKNLIKPFIAKVCTEVERTASCGPWDEWTPCSVTCGKGTHSRSRPILHEGCTTHMVEECEEE
ECPVEPEPLPVPAPVPPTPEDDNPRPTDDEFAVPNFNEGLDVPDNPQDPVPPPNEGKDGNPNEENLFPPG
DDEVPDESNVPPNPPNVPGGSNSEFSSDVENPPNPPNPDIPEQEPNIPEDSNKEVPEDVPMEPEDDRDNN
FNEPKKPENKGDGQNEPVIPKPLDNERDQSNKNKQVNPGNRHNSEDRYTRPHGRNNENRNYNNKNSDIPK
HPERSEHEQPEDKKKKSSNNGYKIAGGVIAGLALVGCVGFAYNFVVPGGAAGMAGEPAPFDEAMAEDEKD
LDEADQFKLPEDNDWN
>gnl|CDD|185621 PTZ00442, PTZ00442, sexual stage antigen s48/45-like protein; Provisional
MRIKKACLGGQLLIWILSSVCEGFTHTCDFNDELKLEFDPNQMTNVEKICNLKPDVLDKVVIKCGSEKLN
YELLPNNCFEQVYTSKNMMNLQKLVEYLHGSAAIVKRKQNKYNSRDKNKYDDVSFRVPPNMDMEEKAIYC
FCQNKAKIRVNKSSGNSYDKDIFNRGIVEVIIPSLPEKIDGCDFTTNTSTLFTKGYDINFYKSIENQDDV
ICKVKATEGKLIGFKCPSNYSIEPEECFLQGFNLSGKKEQLENKLKLTDLVMDHYNKTFYARVPSRIYQN
MKFFCVCVLEEKRLVAHFEFSITSSDTKSASEDNTYNVLQGRSSFLTASGYGAFLTLLLSGVLSFIL
>gnl|CDD|185622 PTZ00443, PTZ00443, Thioredoxin domain-containing protein; Provisional
MKFIILACCILFGLIADEATNVKLDAEDANALVLLNDKNFEKLTQASTGATTGPWFVKFYAPWCSHCRKM
APAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEGGDRSTEKLAAFALGDFK
KALGAPVPAPLSFFALTIDFFVSGTNEALRIYDAAFAGFFTISSFAFLFGILMGLMIALFAFSKGNSTAH
ANKKPKVLNARKKD
>gnl|CDD|185623 PTZ00444, PTZ00444, hypothetical protein; Provisional
MRQRSLLFLLLLVFSYINFSACLLPWTKKRKAENQMGLIKDIAKELKLASETLPTPEQVSAKIHRIDKEV
IKKLDKDIIKEENEDKKKHHSCGEPSYERDYSYPCPEGWTKNSNGQCWGMDYKGPCEALQYFKWFSEEEK
REFENNCCAFWPKVKAEGKKKSHKKDLLRGSVSSSNGLIIAPKY
>gnl|CDD|240421 PTZ00445, PTZ00445, p36-lilke protein; Provisional
MPTSAQKKFHDAFKEYIESGLFDHLNPHESADKFVDLLNECGIKVIASDFDLTMITKHSGGYIDPDNDDI
RVLTSVTPDFKILGKRLKNSNIKISVVTFSDKELIPSENRPRYISGDRMVEAALKKSKCDFKIKKVYAYY
PKFWQEPSDYRPLGLDAPMPLDKSYHLKQVCSDFNVNPDEILFIDDDMNNCKNALKEGYIALHVTGNEGF
SFKEVDVLF
>gnl|CDD|240422 PTZ00446, PTZ00446, vacuolar sorting protein SNF7-like; Provisional
MRFWFGKKKNSSECSDNKKKNNDEIYKAILKNREAIDALEKKQVQVEKKIKQLEIEAKQKVEQNQMSNAK
ILLKRKKLYEQEIENILNNRLTLEDNMINLENMHLHKIAVNALSYAANTHKKLNNEINTQKVEKIIDTIQ
ENKDIQEEINQALSFNLLNNVDDDEIDKELDLLKEQTMEEKLLKELIGEMT
>gnl|CDD|185626 PTZ00447, PTZ00447, apical membrane antigen 1-like protein; Provisional
MFGTKFIFNIFKNKFNSISKKCVNYVIKSYKRTCPHISDFEPFASMYYFSGLHNYRTFYLLVKINEIFNI
NKYKHIYIIFSTDKYDFTTDEIPTNKKNRIHIDQRVDIKIRQCDETLRVDLFTTKLTKKVHIGQIKIDIN
ASVISKSFPKNEWFVCFKDGQEICKVQMSFYKIQKYACPSECMFIQDGLEIWKNKSKSGSKKNIDLQNIH
KNFDDDDKNLSLIDVDTDINDISLMQKLKLISFVLEQEICVFDFYAYVPKYMSAKEIMGEWFLCFLCFKD
GKEQDVINIETIIERNIHRDINIPMLNILRIVVDSKNNTNANIIYTYQNEKYQLSIHSEKNLSYIIDAIT
IFTNELKVLKESCGEKLELRKNMIMQEANMKKLMGKRRLSSPRFRRNIPKSAHKMIKEMYVQKDSLETTA
GERDEFKNDVLEEDEISGDNIGPDEIENDHYQEKEIENDNIQYDENKNEGKNDHIPNNTLPKGHIQMDEH
GRGENPPNEIFFKAQLEN
>gnl|CDD|185627 PTZ00448, PTZ00448, hypothetical protein; Provisional
MSLFQPSNQIKLTNVAVVRYKSHGKRFEVACYKNKILNWRSGVEWDLDEVLQIRTIFANVSKGQLANSDD
LNTVFGTNSIDNICKTILSKGEIQVSETERSYMLDKQFTDICHMLNRMTVNPKNNLPLSVKIIESELKDS
GFSVSLNKTTKEQALKAFDILKKRIPDQIERAKMMLKLSVDIVNKQNITKKLNEFNVFPISSEEKHNTYS
ITFLCEPRYYREIDQLDCKLLLLDSNVKTIDKNSNQDNVEAIQLELSNKSDILFNSITNDPRHIIDKKLE
KTEVSIKENANKFVKPIVSSLNIEESKREIKSNMLLCRKCNIQLMDHNAFKQHYRSEWHIFNTKRNARKM
EPISEEEFLELQQDIKLGFLAVE
>gnl|CDD|185628 PTZ00449, PTZ00449, 104 kDa microneme/rhoptry antigen; Provisional
MKFLILLFNILCLFPILAADEHGMGPIGASDVDPKITFDINSEVQSGPAFLNAVEMAGVKYLQLQHGPGV
NIHKLVEGDIVIWENAEMPLYTCAIVTNNDGPYMAYVELLEDPDLIFFIKEGDAWAPIPEDEYLAKLQEI
RQAIHIESFFSLNLAFQHENNKYEMESHAKHGAKMVTFIPKNGHICKMVYDKNIRIFKALGNDTVTSVIG
FFRGLKLLLINIFSIDDNGMIGNKYFQHLDDKYAPISQKGYEAGIPKLKDFAEAYHPIDLDIKDIDYTMF
HLADATYHDPCFKIIPKTGFCITKLFDGDEVIYESFNPLIECINEVHIYDKKNESIICLDLNHSPPSYKA
YLAKKDGGWEASTHIDLEEKIEELQDHRACELDVMFISDKDLNVAALTNADLEYFMVTPKPHRDIIIVFD
GSEVLWYYEGLDNFLVCAWIYVSDGAARLVHLRIKDRIPANNDIYMLKFDEYWTRISKIQFTQEIKKLIK
KSKKKLAPIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKK
PGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESP
KSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFE
SILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPLP
DILAEEFKEEDIHAETGEPDEAMKRPDSPSEHEDKPPGDHPSLPKKRHRLDGLALSTTDLESDAGRIAKD
ASGKIVKLKRSKSFDDLTTVEEAEEMGAEARKIVVDDDGTEADDEDTHPPEEKHKSEVRRRRPPKKPSKP
KKPSKPKKPKKPDSAFIPSIIAIFLVSLIVGIL
>gnl|CDD|185629 PTZ00450, PTZ00450, macrophage migration inhibitory factor-like protein; Provisional
MPFLQTIVSVSLDDQKRANLSQAYRMICREELGKPEDFVMTAFSDSTPMSFQGSTAPAAYVRVEAWGEYA
PSKPKMMTPRITAAITKECGIPAERIYVFYYSTKHCGWNGTNF
>gnl|CDD|185630 PTZ00451, PTZ00451, dephospho-CoA kinase; Provisional
MILIGLTGGIACGKSTVSRILREEHHIEVIDADLVVRELQAPNMACTRKIAARWPLCVHPETGELNRAEL
GKIIFSDAQARRALGRIMNPPIFRAILKRIAAAWWEDLWRSGAGSSPLIVVLDAPTLFETKTFTYFVSAS
VVVSCSEERQIERLRKRNGFSKEEALQRIGSQMPLEEKRRLADYIIENDSADDLDELRGSVCDCVAWMSR
QSNKRLTYIFGTVAAAAVGVAAAVGYVGYRLLLA
>gnl|CDD|185631 PTZ00452, PTZ00452, actin; Provisional
MQAQYPAVVIDNGSGYCKIGIAGDDAPTSCFPAIVGRSKQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEP
IQNGIINSWDDIEIIWHHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVL
SLYTSGKTIGLVVDSGEGVTHCVPVFEGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVK
NIKERLCYTALDPQDEKRIYKESNSQDSPYKLPDGNILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYS
SIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQLKIQVAAPPDRRFSAWIGGSIQCTLS
TQQPQWIKRQEYDEQGPSIVHRKCF
>gnl|CDD|185632 PTZ00453, PTZ00453, cyclin-dependent kinase; Provisional
KPAQDFFSLDANGQREALIMISKLQSKILYSDKYYDDEYEYRHVILPKDFARLVPRSRLMSESEWRQLGV
QQSVGWRHYMIHKPEPHVLLFKRPKT
>gnl|CDD|240423 PTZ00454, PTZ00454, 26S protease regulatory subunit 6B-like protein; Provisional
VATTAAAAVASSTTHTERDLYEKLKELEKELEFLDIQEEYIKEEQKNLKRELIRAKEEVKRIQSVPLVIG
QFLEMIDSNYGIVSSTSGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKP
DVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRV
VGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFD
QTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKI
SAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVRKTDRDYDFYS
>gnl|CDD|240424 PTZ00455, PTZ00455, 3-ketoacyl-CoA thiolase; Provisional
MFRSSLTTQAAKRVFVVGGHITPFVGKGSPLFIDKKHPDFGKKENKTLEELLATAIQGTLENTGLDGKAA
LVDKVVVGNFLGELFSSQGHLGPAAVGSLGQSGASNALLYKPAMRVEGACASGGLAVQSAWEALLAGTSD
IALVVGVEVQTTVSARVGGDYLARAADYRRQRKLDDFTFPCLFAKRMKYIQEHGHFTMEDTARVAAKAYA
NGNKNPLAHMHTRKLSLEFCTGASDKNPKFLGNETYKPFLRMTDCSQVSDGGAGLVLASEEGLQKMGLSP
NDSRLVEIKSLACASGNLYEDPPDATRMFTSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALG
IAEYGHAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEYQMKNIPALGAT
LNMGGDDKTAVSTVLQNI
>gnl|CDD|185635 PTZ00456, PTZ00456, acyl-CoA dehydrogenase; Provisional
MFRRVCSSAAASHAAAVSASARSLQYQPRIRDVQFLVEEVFNMYDHYEKLGKTDVTKELMDSLLEEASKL
ATQTLLPLYESSDSEGCVLLKDGNVTTPKGFKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMA
TANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADGS
YKITGTKIFISAGDHDLTENIVHIVLARLPNSLPTTKGLSLFLVPRHVVKPDGSLETAKNVKCIGLEKKM
GIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMRALS
GTKEPEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAAAKDAATREALDHEIGFYTPIAK
GCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIGRKVLSLKGGNEVARF
GKRVSKLVRAHLFSRGALGQYARRLWLLQKQWRLATTRVKMMAMSDRDAVGAASEDFLMYTGYMVLGYYW
LRMAEVAQKKVAAGQDADGFYQCKVDTCQYVFQRILPRADAHFQIMQAGPSIMASKEENWDL
>gnl|CDD|185636 PTZ00457, PTZ00457, acyl-CoA dehydrogenase; Provisional
MRRRFSSAPRQYVRHASYAAGLFNFKIVPEEMFPYPCRKLDGDEAENLQSLLEQIRSNDKILGNLYGARI
ATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWAT
EEGCGSDISMNTTKASLTDDGSYVLTGQKRCEFAASATHFLVLAKTLTQTAAEEGATEVSRNSFFICAKD
AKGVSVNGDSVVFENTPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQELRGSNAEEGATDT
VASFACAMYAMESTLYALTANLDLPTEDSLLECTLVSAFVQSTTNQLLSILETATPPSTTLEKCFANARL
FLSMMESRDFLYSSAVCCGVEDYGLFFQRASTLQMMQARTLRSLGVRDRVPIKNLPDCSLIDEAVVAFGN
AVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGELASAFIAMAVSRAR
QLSEESCNVGKTADDSYKRIALEMCDDALQ
>gnl|CDD|185637 PTZ00458, PTZ00458, acyl CoA binding protein; Provisional
MADLFEECVSFINSLPKTVNLSVEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNRED
AKKRYVEIVTELFPNWEKGE
>gnl|CDD|185638 PTZ00459, PTZ00459, mucin-associated surface protein (MASP); Provisional
MAMMMTGRVLLVCALCVLWCGAGGRCEAGVGVGAQQDGGKSPPESKGLETSSQGTQDLKGGAAGAKENSP
PLPTEEDDEDVDDDSEEGDDDDGGAEDEEEEKVRGQSGQEGTVALGSGSTEKKLIGSEKQTELSISSAES
ISPSGSRELNVNLTQTEVEGKKETDKNTPAVENPLTTGNGENTLPAGIVEGNPSPPPPQDGIHSREQDGE
GTTSEGQKNVPLPETAATPQSHHDKGSEGTGEDTKATTVTANTTDTTNTQNSDGSTAVSHTTSPLLLLLV
VACAAAAAVVA
>gnl|CDD|185639 PTZ00460, PTZ00460, acyl-CoA dehydrogenase; Provisional
TQMLEEARKQVQFPVLEMTHLLYGNKEQFETFLERQKFIDNEPMFKVHPDYYNWSRQDQILLNAEKTREA
HKHLNLANPNYYTPNLLCPQGTFISTVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGS
DVQNLETTATYDKQTNEFVIHTPSVEAVKFWPGELGFLCNFALVYAKLIVNGKNKGVHPFMVRIRDKETH
KPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARYIKVSEDGQVERQGNPKVSYASMMYMRNLI
IDQYPRFAAQALTVAIRYSIYRQQFTNDNKQENSVLEYQTQQQKLLPLLAEFYACIFGGLKIKELVDDNF
NRVQKNDFSLLQLTHAILSAAKANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQI
MYLQLARYLLKQLQHAVQKPEKVPEYFNFLSHITEKLADQTTIESLGQLLGLNCTILTIYAAKKIMDHIN
TGKDFQQSWDTKSGIALASAASRFIEYFNYLCFLDTINNANKSTKEILTQLADLYGITMLLNNPQGLIEK
GQITVEQIKLLQETREQLYPIIKPNALGLVEAFGLSDNSLRSLIGCHDGDPYENMYNWASKENSLNKQQV
HQGVNYLMKMEIKAKL
>gnl|CDD|185640 PTZ00461, PTZ00461, isovaleryl-CoA dehydrogenase; Provisional
MRRVLQSSLGRRSATCGWTAAATMTSASRAFMDLYNPTPEHAALRETVAKFSREVVDKHAREDDINMHFN
RDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRA
RWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWITNGTVADVFLIYAKVDGKIT
AFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVG
IAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLF
ATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKGLK
>gnl|CDD|185641 PTZ00462, PTZ00462, Serine-repeat antigen protein; Provisional
MKFFIPLFFIICVIFIINVIKCRGEEDDDNGNIGGGQAGGTGGDNAGNIDGSPIGNLDANIHASFGADPK
ESSGANLPGKKEKKKKEIRGHDIMSNSDSQNSSSIEKQDNIQIKSALLKDNKGLKITGPCNENFIIFLVP
HIYIDVDTEDNNIELKTELDEFNDAIKFEDNSGELEKKDDTKLNSNFNTGEQGDSLDKDRLQNICAEGKN
FKFVVYIKDNILILKWKVYGETEDGTENNKVDIRKYKIKEKERPFTNILIHAVKEHKDTHLIESKNYAIG
SDIPEKCDTLASNCFLSGNFNIEKCFECALLVEKEDKNDECFKYLSEDIREKFKEIKAEAEDDDEDDFRE
YHLTDSIDNILKKIFKINENEDKKELIKLEELDDFLKEEIMDYCKILKDIDTNGTLDNHELGNEMDIFNN
LIRLLILHKEENINTLHNKFRNAAICLKNPDDWIEKKRGLILPEVLNNDIEYFNEHEKLNEEKKRKIYDD
KDSPEDKDNKGKDIIHIDKTIEKEDTLKYDNNDKMFCNKEFCNRLKDENNCISKIQIEDQGNCAISWIFA
SKYHLETIKCMKGYEPHAISALYIANCSKGEHKDRCDEGSNPLEFLQIIEDNGFLPADSNYLYNYTKVGE
DCPDEEDHWMNLLDHGKILNHNKKEPNSLDGKAYRAYESEHFHDKMDAFIKIIKDEIMNKGSVIAYIKAE
NVLGYEFNGKKVQNLCGDDTADHAVNIVGYGNYINDEDEKKSYWIVRNSWGKYWGDEGYFKVDMYGPSHC
EDNFIHSVVIFNIDLPKNKKSPKKESFKIYDYYLKASPDFYHNLYFKNFNSGKSMKLVNASDEHKNIFSE
EDKVNHKKGSKILNSEVTTSLLSQEISQRRGEDDDIDKKIGDNPDIFEQDKAGKDEFGKESITHNNTALE
NAGKSNENSEKVHIYHIIKHIKDGKIKIGFRKYDDTNDIGKKHSCSRSYAEDPEKHEGCIKFCELHWKEC
EDKTSPGLCLSKLDGNNECFFCYV
>gnl|CDD|185642 PTZ00463, PTZ00463, histone H2B; Provisional
MVSKKPAKAKKAATGPDGKKKRKKSRYDSYGLYIFKVLKQVHPDTGISRKSMNIMNSFLVDTFEKIATEA
SRLCKYTRRDTLSSREIQTAIRLVLPGELAKHAVSEGTKAVTKFTSK
>gnl|CDD|240425 PTZ00464, PTZ00464, SNF-7-like protein; Provisional
MNRLFGKKNKTPKPTLEDASKRIGGRSEVVDARINKIDAELMKLKEQIQRTRGMTQSRHKQRAMQLLQQK
RMYQNQQDMMMQQQFNMDQLQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDT
QEIQEIMGRAYDVPDDIDEDEMLGELDALDFDMEKEADASYLADALAVPGTKLPDVPTDEKQQAEGQNTV
D
>gnl|CDD|185644 PTZ00465, PTZ00465, rhoptry-associated protein 1 (RAP-1); Provisional
MRIISGVVGCLFLVFSHHVSAFRHNQRVGSLAPAEVVGDLTSTLETADTLMTLRDHMHNITKDMKHVLSN
GREQIVNDVCSNAPEDSNCREVVNNYADRCEMYGCFTIDNVKYPLYQEYQPLSLPNPYQLDAAFRLFKES
ASNPAKNSVKREWLRFRNGANHGDYHYFVTGLLNNNVVHEEGTTDVEYLVNKVLYMATMNYKTYLTVNSM
NAKFFNRFSFTTKIFSRRIRQTLSDIIRWNVPEDFEERSIERITQLTSSYEDYMLTQIPTLSKFARRYAD
MVKKVLLGSLTSYVEAPWYKRWIKKFRDFFSKNVTQPTKKFIEDTNEVTKNYLKANVAEPTKKFMQDTHE
KTKGYLKENVAEPTKTFFKEAPQVTKHFFDENIGQPTKEFFREAPQATKHFLDENIGQPTKEFFREAPQV
TKHFLDENIAQPTKEFFRDVPQVTKKVITENIAQPTKEFLKEVPHTTMKVLNENIAQPAKEIIHEFGTGA
KNFISAAHEGTKQFLNETVGQPTKEFLNGALETTKDALHHLGKSSDEANIYDASENTTQSNDSTTSNGED
TAGYL
>gnl|CDD|240426 PTZ00466, PTZ00466, actin-like protein; Provisional
KMNEYAKQLYSNQPIIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRG
LLKVTYPINHGIIENWNDMENIWIHVYNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFI
SIQAILSLYSCGKTNGTVLDCGDGVCHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSA
EMEVVKNMKENCCYVSFNMNKEKNSSEKALTTLPYILPDGSQILIGSERYRAPEVLFNPSILGLEYLGLS
ELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDITIRISAPPERKFSTFIGGSI
LASLATFKKIWISKQEFDEYGSVILHRKTF
>gnl|CDD|185646 PTZ00467, PTZ00467, 40S ribosomal protein S30; Provisional
MGKIHGSLARAGKVKNQTPKVAKQEKPKQPRGRALKRLKYTRRFLAKTVKPGEKVHMNKQPPGKAG
>gnl|CDD|185647 PTZ00468, PTZ00468, phosphofructokinase family protein; Provisional
MSNYKQTELKRNKGDSRDVSLLSASSLHEGQSNMQMWRRRWEPCLPHILRSPLSIKEVSAFEGMGKMERS
DVSSYFPLTSGNSLVKFEAISDGSSSWKKFPARRIGVVLSGGQASGGHNVIAGLMSYIKLCNQSSQLFGF
LGGPEGVYSERYRELTEDDINGILNQGGFNIICSGRHKIETEEQMRASLEICEKLKLHGLVVIGGDDSNT
NAAVLAEYFKRNSSSTVVVGCPKTIDGDLKNEVIETSFGYDTAVKTYSEQIGSIMDAIKTEGYGYYFVRL
MGRSASHITLECGLQTRANMILIGEEIKEENRSLMSIVDEIVEMILKRDSLGKKHGIVLLPEGLIEFIPE
FETLIKELNLILLKTNDRKQIIDSLSQEMKTLFLELPSDVQNQLLLERDPHGNVQVAKIATEELLVHMAK
EKLEEVKKDYILDNVKTHYFGYEGRCALPSNFDASYCFALGHTAAALIDNQRSGYMAVVRKLSLTPEQWE
PAGCPLTYMMNIELRKGKSVPVIKKYLVDLKGQSYLAYCQVRSEWKLNDYYRNPGPIQFDGPNSGITNYM
ISPPRVEDLLRMEDRDENKMTHKLCGSELSQNRCKDDLKIPKILLSTASKFNDDLIISSSCRDLDAYIIT
KCLPHQTGRHNSKTLQLREEEYSSPFTEIRESSSSKSSVGNSLACESLGLILSCLSTPGTQNVICGLVNG
LPSLKQLIVFKSLSDFYEGKALKVDLTSEGSLEFFENSLNSGGCIFPNGVEIKMNVSEKKYSNTTLKAND
NQEFTNSSCVLSCKGLVSNDFLSQLLSFFNMRAIAIVGNSEAATFGASLSEQLICMSLNGMKSEIPVVFV
PVCLENSISHQMIETCIGFDSVTKSISTLVGNLLTDSASATKYWYFMKMIGDKTSNVALEVGIQTHPNLV
VIPERYADSKLSVYGSEMAGVTLDDIITEICDIICLRSNQGNNFGGLLVSEGLFDQVYPTREYRKIFSRF
STQNLCNASNSGNCEILGSESLSRYEKKVVEDFKLIFSDIDERLIENLINSRKICDVRTEIILSALVQKE
LKFRRSKNKIKNGMNPVCFSFTDQVRACIPSDFDSTLGLMYGMLASKIINSNLVGGYVTGIKGVLSQIDS
WNMYAIPISSLMTLNIEGDKIMDSRNNSNLSFESKKLLTESTLGNAGHQLEFICKLNSVNMRNNPSFKLL
MNHIEKWEVDNTYANPGPIQYFNLFKNLFNRTLFESEYVYTRNLKEMDQILLEIKTLCQLGVEKDILNST
IQHLKAIQNSISIMSSCNHRKSKPEQIECIQKTNSIANYTSNLKCKSSNNETNLEMIVNNIINQETCN
>gnl|CDD|185648 PTZ00469, PTZ00469, 60S ribosomal subunit protein L18; Provisional
MGIALKNVGRIKKHGRKNLVSKNPYLRLLVKLYRFLARRTNANFNKIIAKRLIMPKRFRPPLSLSKLHRH
MASYPDDVAVVVGSITDDKRLYDCKKLKVCALRFTETARKRILDAGGECLTFDQLALKYPTGQKCILLRG
PTKARTAEKHFGKAPGRPKSKARPYVRSKGRKFEKARGRRKSRAYKK
>gnl|CDD|240427 PTZ00470, PTZ00470, glycoside hydrolase family 47 protein; Provisional
NVNLREHLSVHNNADDNYNNNNNNNNQINSNNPNNNGNNQASKLPRGKKKQENPFNKIDEVYYQNEKLNI
KRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHHEWFGLGLTIIDSLDTLKIMGLKKEYKEGRDWVANN
LKQSKDTGLGVSVFETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPASEINLATGRKS
YPGWAGGCSILSEVGTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAINGLYPIFLNPDAGRFCGNH
ISLGALGDSYYEYLLKQWLYTNGREERYRRLFVESAKGIIEHLYKRSPKGLTYIAEMDGGSLTNKMEHLA
CFAGGMFALGAAINITPDDEKSARYMEVGEEVTKTCYETYATSPTGLGPEIFHFDPNSGDISPNVHDSHY
ILRPETVESIFILYRLTGDPKYREWAWKIFQAIEKHCKTENGYSGLKNVLTVHPQQDDFQESFFLAETLK
YLYLLFQPDHVIPLDKYVFNTEAHPIPIQKTN
>gnl|CDD|240428 PTZ00471, PTZ00471, 60S ribosomal protein L27; Provisional
MTKFLKPGKVVIVTSGRYAGRKAVIVQNFDTASKERPYGHALVAGIKKYPKKVVRGMSKRTIARRSQVGV
FLRVVNHKHFLPTRYNMDMSKELRGRINVSDASKKARSKQLVKKLFQARYNAGSSRWFFQRLRF
>gnl|CDD|240429 PTZ00472, PTZ00472, serine carboxypeptidase (CBP1); Provisional
PSILSTLALLVALLLATVPWNALYTVYAGTLRTTGSGWAPCDPSVNQWSGYFDIPGNQTDKHYFYWAFGP
RNGNPEAPVLLWMTGGPGCSSMFALLAENGPCLMNETTGDIYNNTYSWNNEAYVIYVDQPAGVGFSYADK
ADYDHNESEVSEDMYNFLQAFFGSHEDLRANDLFVVGESYGGHYAPATAYRINMGNKKGDGLYINLAGLA
VGNGLTDPYTQYASYPRLAWDWCKEKLGAPCVSEEAYDEMSSMVPACQKKIKECNSNPDDADSSCSVARA
LCNEYIAVYSATGLNNYDIRKPCIGPLCYNMDNTIAFMNREDVQSSLGVKPATWQSCNMEVNLMFEMDWM
KNFNYTVPGLLEDGVRVMIYAGDMDFICNWIGNKAWTLALQWPGNAEFNAAPDVPFSAVDGRWAGLVRSA
ASNTSSGFSFVQVYNAGHMVPMDQPAVALTMINRFLRNRPLS
>gnl|CDD|240430 PTZ00473, PTZ00473, Plasmodium Vir superfamily; Provisional
MEKLLRDTAIVKALKKEYPFLANWPDYHFEDLRGIYNATYESICEEISSVSDYNKVNKENCIKFFSILEN
IVRRGDLKKNDDIWKDFVEWFYNKQEKFDVFSNHLESFNYDFEYLIQKNILKNFNKFKKLYENNYELEDI
MKLFYFTENVGDIKSLMGAPDNEHYASSCKFVNDCLDIYRKYKDEKCSGNSYNTFRGSTICNELNNFFDK
YKEHLYPPLKYRRILIESLGDGIDTARVQCKVCEREYGSNPFFSFFANYKPDLSSFGKVLVISFSALGGS
LSLFILYKFTPLGSLFGPDKKRRRRRWRNMGHDSRGPYNANYGGQFNSRSGRTGSSESIRGFTYDSSTTY
GGSSYGTSQTDSTSTYGSRSTFDSSTGGGSQSGGGSTYGGSSTFDGSSRGSSDSFGVSYFGPQQTVGFST
>gnl|CDD|240431 PTZ00474, PTZ00474, tryptophan/threonine-rich antigen superfamily; Provisional
MELKKNNSALASQKSYSRTTPTRSYKSAPKTSTSTLSRLTILIFALSCAFFVNTASGASTNRPNKNGFVS
PNLIGFGELDIDESEEFKRMAWNNWMLRLESDWKHFNESVEEKKTKWLQETDSAWSDWLRSLQNKWSNYS
ENMLKEYKSNVMEKSATWNDEQWVEWIKTEGRNILEAQWEKWIKKKDTQLQKLILDKWVQWKNDKIRSWL
SSEWKTEEDYYWSNWERSTTAKWLNEAERKHWLKWKERIHRESEQWSNWVQMKENVYINVEWKKWSQWKN
DKKILFNKWSTNLVYKWTLKKQWNVWIKEANNSNKV
>gnl|CDD|185654 PTZ00475, PTZ00475, RESA-like protein; Provisional
MIIIVPFIFFNLIFTSDMMYEYIENTKVPIFVKLFFGKSIFIEDIFYYVGMIMKEMMEGQNIREEEVAEL
LKDRLDLYIDNEDEWEKLMENEISMLLKSSFSNFILESIGWTYENVSNIFLEEKANSGINKKDIYLKEAN
ERMIRNSIVLRQCKSRFISIITNYYPFKEQNNPFIKQAQYVSSSNYVLDDIINNIDYSIDNIHRAIDNLY
YEHILNLLEEEKNEILEEILRNILKIILCDVETTVRRSAQKVLQNAEGDTNLMLKRAKGLQSLGKMILQK
VN
>gnl|CDD|240432 PTZ00477, PTZ00477, rhoptry-associated protein; Provisional
MSVKSLFIILLLIYSLFRYANGVTLKKRNGGAGLKSQNTEEFVDETEKVVREVNHLRMVSDKMTDYLSKN
KYDPSMFCEGDLETCHTLVNRYVERCKAGDCYTLDNVKVFESGDRLGVLLPHLAQYETALYVFKNSGAHQ
GSDFYDRFRKIKNKYRMSTERTLRSFTNQILKRNLDAMNVENETMAVLNEVLYALTLYYQRYLNNSKLSK
FQNLGKFLRFFFSLGKRRYLNELAKDVVGGKKLDLSHSDLKSVVDSYVLYLTVGNYRKRHRLANYFGKLA
KHAVMKTMGYKKVSALMADQLLEYPPDPMDFCKGNAKVGCKELVTKFLERCDHGDCTTLDTVNLLDLKDW
LNVKLPDLPQVFAAFQIFNNSRAKKPNWLKAVFRQKGRMGNEQFKRMLYNRNFKNLTYKTKDQEVLERYL
SKAAVYFKYRSRKTELDKHTSTKVESFLMRTLRSLVGAGRVRLEVIRLDAMFLAYRNYLYKSGVDKNLDK
LNLFAQSCQHVVFSFLSMQYKGVKSKEYEKELEK
>gnl|CDD|185656 PTZ00478, PTZ00478, Sec superfamily; Provisional
MKMGLPEFLTDKSNPVGYVVSGVQEFANDSRRLIRKCTKPDAKEYTNIAYACSVGFFIMGFIGYSIKLVF
IPINNIIVGSP
>gnl|CDD|185657 PTZ00479, PTZ00479, RAP Superfamily; Provisional
MGLLRPRERVILRAIRHESRIRYIGRRMHKRFRSWAQQRVRKYWLPMKVCLTSPPDLMDGWYLSACVQKA
ATLRKHDLELWHGFTNRLLELSDTLTPQQIGYIFYGYGKSRFLNPEFYEKMLKFVQPLLPNFYSHSLMCI
AWALNRVQIRDEAFLSRFAKEVGEKFDDIRTTDLIKICNSLAKLGGYTNNLKKFLSEKMVEKLESLFAQD
FRNVVNDVTLIHLYDDNTQIYILERFSKMFICARPQHLQQAYKSAVAVRVLLPHVWFQLSKSVKSFYTRL
SMRRIPQSLRKPSPFQWDVSNCLAKLGISHRNTFYWGCFWIDIGEIDDKRNCWFIDGPSCFYTSTNEYTE
SVKLQHRILSNLGWNIRRVVWIDWVQLGDDTEAKVQYVRKLRESEPLGDTLTDGPSLSPQEIKEKLKKIK
QYKIKKEQQKVQSQE
>gnl|CDD|185658 PTZ00480, PTZ00480, serine/threonine-protein phosphatase; Provisional
MAKDKKGEIDVDNIIERLLSVRGSKPGKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQ
YFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYD
ECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSD
PDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDN
AGSMMTIDESLMCSFQILKPAEQGQGASQQNKPGSAKFVN
>gnl|CDD|185659 PTZ00481, PTZ00481, Membrane attack complex/ Perforin (MACPF) Superfamily; Provisional
LKKTLICLSILLILAQSQSLLNKRQMYKLLSSSNIEEAMQELCPFPGYYGDYCPQEQMAQASYKRQLQQG
IPNMPSGVGASFDISTGELKLPAIQLTYQKEPTQEQIYTDPLSDNQFIVADETQVEQIELQPDIKIFKNE
FELTNIWLDATQNGQWLGGQYSQSKDLNDVFEKFFKGNQETSIAQMAKNVIRMTFKTDNLKLNRFAQRAI
DALPEDYQPDVYNEFLNAWGTHISVDTFIGGMIEKQTVFKDCVFFTPQFNGGLSPEQVEQALRNELNGNP
AEGFFTARRQVTLDHKFGGNPEDVANWEQTISQNPALLKINRFLSWDNLTANPQVKANLQQAIMNRIESM
KQRQISYQQQVREQRRIERNGPRTAWAIQGNGNCNGQLPLPLNYSISRQFQMKAASVCPPGLDFNYSKSR
CSSGPFHTLLDIPKEVRYERDQEGNYRTILNNPLAEFTGGPRELYGNFVDRGCSVAQYYGFPQYTDLNQI
PPNETRFKMICTDCIPSVYNSPNGQVFQCSCPAF
>gnl|CDD|240433 PTZ00482, PTZ00482, membrane-attack complex/perforin (MACPF) Superfamily; Provisional
RLLNALLAIWCILSYLYEIPFVGSLRLGLRSNYLQSTVEDIEGPSAVDERTSGVLRDEGKHANILYNSIL
CNQKKHASFLNQRKSLDDDDDDEFDFLYEDDEDDAGNATSGESSTDDDSLLELPDRDEDADTQANNDQTN
DFDQDDSSNSQTDQGLKQSVNLSSAEKLIEEKKGQTENTFKFYNFGNDGEEAAAKDGGKSKSSDPGPLND
SDGQGDDGDPESAEEDKAASNTRAAYTKATSVFPGLYFLGIGYDSLFGNPLGEPDSLTDPGYRGQIILMN
WAQSNDGVANDLATLQPLNGWIRKENACSRSESIKECSSLSDYTKNLSAEASVSGSYMGINSFSASTGYK
KFLQEVSKRTTKTYLLKSNCVKYTAGLPPYFKWNQTTAFKNAVNGLPPVFDGLEAESECSSDVYEQDKTA
EECENVPIWISFFEQYGTHIIMELQLGGKITKQVTVKNSSVEQMKKDGVSVKAQVKAQFGFASAGGSTNV
SSDNSSASNEYSYNMSEQLLVIGGNPIKDVTKEENLAEWSKTVSTLPMPINIELLPISTLFPSDDLKESY
EKAVIYYSRLYGLSPHDTMQKDEKDIVKILTAATTVTWSGAPPISAECPHGQVVLFGFAMRQNFWDHTNK
LDNYEIEICEAGREKCTSKQGSSNKYDVSYIYIECGPQPLPFIEQVVAESGTTYNSAKCPNDYSVLFGFG
ISTSSGRHQSALYSYFTPCTPGQKSCSLNMNNGDDKSYIYMVCVDKTIWPGLNELSNIAEDGLHGKVNKR
KKNSDGELVVTCPADGTILTGFYGETHTSSPYVRDPFGKCAKSLKACSVHGSGQAIGMLNRHALFGWALC
KNNN
>gnl|CDD|185661 PTZ00483, PTZ00483, proliferating cell nuclear antigen; Provisional
MFECRLDGMFLRRLFETLKDICTDVSIDCSENGLKMQAMDNSHISLIHLNLAPDFFQLYRCDKPCVLGLN
ISFMLKILSVVKEKSTIYLFRGDNTEDPVLNIRIIEEEGQNSLESDSLEAQVKLINVQREHLEIPQCEYH
CKCVMNSKKFQEFAKYLHSIGDTVSISMKKDEMRLETEGEGIKASKQFHNDVGDVRVTSTESLSQEFATR
YLVLFSKATSLADEVSINLSAGIPLSVKFNFKDPLTDLQDSSFINFYLAPNIEE
>gnl|CDD|240434 PTZ00484, PTZ00484, GTP cyclohydrolase I; Provisional
MTNLAPGLSLQKSENGNEENGDISRNCRDGDIDNDANLSLLDEDASLGKGRQSNSGPSTESSPTCATLME
EKKGAIESARRKILKSLEGEDPDRDGLKKTPKRVAKALEFLTKGYHMSVEEVIKKALFKVEPKNNDEMVK
VRDIDIFSLCEHHLLPFEGECTIGYIPNKKVLGLSKFARIIEIFSRRLQVQERLTQQIANALQKYLKPMG
VAVVIVASHMCMNMRGVQKHDASTTTSAYLGVFRSDPKLRAEFFSLIKR
>gnl|CDD|240435 PTZ00485, PTZ00485, aldolase 1-epimerase; Provisional
MQFGIEVEPYGYDKLVWLETDRLKVGLTNYAASVASIQVYHPADNKWIEVNCGYPKNPEEAYADPDYMGA
TVGRCAGRVAGGVFTLDGVKYYTQKNRGENTCHCGDDAYHKKHWGMKLIETANVIGVRFNYTSPHMENGF
PGELVSKVTYSIERSKPNVLKTIYDSYIPETSPADATPVNIFNHAYWNLNGIPERNGKKNAVWVQPESVR
NHWLRVPASRVAEADRMAIPTGEFLSVEGTGLDFRQGRVIGDCIDDVALLDRDPCGYDHPLAIDGWEKGK
LMLHAEAKSPVTNICMKVYSTFPCMWVYTANNKPLPASGGPGQRYARWTGMGLEPQYFPDVANHYPKYPS
CIVRRGERRFTETILNEFTVECSSKM
>gnl|CDD|240436 PTZ00486, PTZ00486, apyrase Superfamily; Provisional
MPPMVTSSIILFLITIATLISFVLLISLLSIQNTPRYNGVLKMSNYRSYNKKSPLFRVALVADLDKASKD
KEGKKWRSKVIKGTIFRQGNGWSFRESEDESFELQSGLNEGGRGMELSELVSFNGKLYGFDDRTGIVYEI
DIDKKKAYPRHILSDGNGNSDKGMKIEWATVYDDKLYVGSIGKEFTTPNGDILNRNPMYIKKIDKNGKVE
VVNWSNVYNSIRNALGISYPGYIIHEAVTYSNLLRKWYFLPRRVSNEPYDEEKDEYRGSNYIIICDEDFQ
NPRVIKDPQYDPERGFSSIKFLPGNENIIVALKSVEVEDKQESYIGMFDINGKVLMKDKLIGKEKFEGIE
FI
>gnl|CDD|240437 PTZ00487, PTZ00487, ceramidase; Provisional
SFKKLIILISLVIILLSSNFIDSFKIPVQKNVKSSDDSSYQIGSGIYDITGPAAEVNMMGYAMPDQRTKG
IHFRQRARAFVFADSPGNRAVYVSTDSCMIFQEVKIGVVPKLQEIFGPDLYTLDNVLLSGTHTHSGPAGF
SFYALYGITTLGFYKKNFDTICEGIVQAIVKAHKSVQPARMYTNSGELWNSNINRSPTAYDNNPEEEKAM
YDGNVDKNMTVLRIEDMNGNPFAAISFFAVHCTSMNNTNHLISGDNKGYASYLWEKYKNGNDSFPGVGPF
IAAFGQSNEGDVSPNTRGPTCRDGIPCDYKTSTCNGTTEECWGLGPGKDGDMFESTQIIGGNQFNKALEL
FNNASIQVSGPIQYRHTWLNFTNVSVEPPYNSGVQVATTCRGAMGYSFAAGTTDGPGAFNFKQGDNSTKG
NPFWNFIGSFIAKPTPEQILCQSPKPILLDVGMVEPIPWVPDVMPIQIMTIGQIVLVAVPGEFTTMSGRR
LRNTVREIIGTSIENPIVLIAGLSNTYSGYIATFEEFQVQRYEGASTVFGPHTLGAYQQEFDKLAQSIVD
GQPISPGLKPRNLYGHTWFFLPPVIVDSAPFFDDFGDLYQDVDTEKVYSNNDTVSAEFYGGNPRNNFMTE
SSFLTVDKLNEKNQWTTILVDGDWDTKWHWKMHDLGFSLITIIWSIGPTTEPGTYRITHSGYAKKNPFSQ
NLTPYQGISSNFKVQ
>gnl|CDD|185666 PTZ00488, PTZ00488, Proteasome subunit beta type-5; Provisional
KFCGPEHFEHPPGAHPGDFLAEYTFDHGDANKAIEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSV
KKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMI
CGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSG
GAINLYHMQKDGWKKISADDCFDLHQKYAAEKEINKA
>gnl|CDD|240438 PTZ00489, PTZ00489, glutamate 5-kinase; Provisional
MADILKSVKRIVVKVGSSILVDNQEIAAHRIEALCRFIADLQTKYEVILVTSGAVAAGYTKKEMDKSYVP
NKQALASMGQPLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATA
LHELVFGDNDRLSALVAHHFKADLLVILSDIDGYYTENPRTSTDAKIRSVVHELSPDDLVAEATPNNRFA
TGGIVTKLQAAQFLLERGGKMYLSSGFHLEKARDFLIGGSHEIGTLFYPRVSSA
>gnl|CDD|185668 PTZ00490, PTZ00490, Ferredoxin superfamily; Provisional
MRMYRRLLPGVLLPRCMAALGPLSTSRALYSTPGKVKVCVKKRDGTHCDVEVPVGMSLMHALRDVAKLDV
EGTCNGCMQCATCHVYLSAASFKKLGGPSEEEEDVLAKALDVKETSRLACQVDLTPEMDGLEVELPSYVT
NRL
>gnl|CDD|240439 PTZ00491, PTZ00491, major vault protein; Provisional
KMTESVIRLKPYEYIHVLDNNTNVTRLIVGPQTFTRQDHERVLHPPQPMVVVPPRHYCIVENPHVRDPDG
SPVKDAYGQVKVRHGEREIRFSQDPFPLYPGEKLVTQVEPLKVLPANEALRVRALRDFTVEDGVRRVAGE
EWLFKGPGTYYPRVEERIVEEVKAVLIKPNQALKLRALETFTDRDGVPRVAGEEWLVRTPGAYLPGVFEE
VVGVVKGIVLSDKEALHLRALRTFTDVYGGIARKAGEEWLVTHEDCPTHIPDVYEKLVATVNATHLSARQ
YCVILNPVGDDGHNRFGAKELRKGECSFFLQPGESLEGDGIQDAYVLGEDEALLLRALETFTDEDGVERE
PGDRWLVHGPCEYIPPVLVEVVERRRRIPLDENEGIYVRNITTGEVRAVHGKPYMLGAHEELWEKPLPPN
VEELLAQPRSSMAYSERSGQASGKVPYEENPGFESHRDKHRVVTYKVPHNAAVQLYDYKTKKSRVVFGPD
LVMLEPDEEFTVLSLSGGKPKVPNQIHSLHLFLGPDFMTDVIHVETSDHARLALQLSYNWYFDVTDGNPE
DAQKCFSVPDFVGDACKTIASRVRAAVASEPFDEFHKNSAKIIRQAVFGSNDETGEVRDSLRFPANNLVI
TNVDVQSVEPVDERTRDSLQKSVQLAIEITTKSQEAAARHQAELLEQEARGRLERQKMHDKAKAEEQRTK
LLELQAESAAVESSGQSRAEALAEAEARLIEAEAEVEQAELRAKALRIEAEAELEKLRKRQELELEYEQA
QNELEIAKAKELADIEATKFERIVEALGRETLIAIARAGPELQAKLLGGLGLKGYLVTDGKSPINLFNTA
NGLIGGPLAK
>gnl|CDD|240440 PTZ00493, PTZ00493, phosphomethylpyrimidine kinase; Provisional
MEGVSNILSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFA
DVTIDVVKLGVLYSKKIISLVHNYITNMNKKRGKKLLVVFDPVFVSSSGCLLVENLEYIKFALDLICPIS
CIITPNFYECKVILEALDCQMDLSKANMTELCKLVTEKLNINACLFKSCNVGENSAEENEVYAVDHLCIR
NVGSYPTGEKQQIDAGGVTYLYDVYKLRSKRKPGKDIHGTGCTLSTAIACYLAKKHNILQSCIESKKYIY
NCIRYAYPFGSKSQGLNHLKASQELPTFTDLQVIPIVQDSP
>gnl|CDD|185671 PTZ00494, PTZ00494, tuzin-like protein; Provisional
MMALTLDPRWNAMRRGIAGIGVCAVDGRGGAAAPGSCRLSLCSCLSPASSGGCGGADSALSEGGHCRECV
CGMRGRLPSPKKPWNSLAGVLVGVRVTHAASVLEDRPVALGRLVSRLSEAAYKAEMLRTGKRDRDGEDRR
GDAAQLLVVDAGTRVTVRTEGDPASGAAVAPSAMHMKGTIAKVNGNATYIILMEKGEVELSVASERIVAL
QPRKKLLQSARLVALVNWLRSCVHDPRDVEAIALVLFSRGWRAERMYLLEGVDLLPFVFVSRVELDSVSE
KARWERDHDKAMQMLRRERVKDTNFRYALAKYKGTMSCIAGVLVVAYVFTANLRAYRRQQRGHQLRTAIE
TLSKAARPRKEEGMLAAAAEAFEVRREDEEALVRSVLTQMAPSHPRIVALAGGSGGGRCVPCRRAVRVEG
VALVHVDVGGTEDTLRSVVRALGVSNVEVCGDLLGFVEEAMRGATVKASDGVPFLVMRLREGSDLGRVYG
EVVSLVSDCQACHIVLAVPMKALTPLNVSSRRLDFYCIPPFSRRQAFAYAEHTLDALDLVCFVEVVGTRS
SDVDELCAALRQRGVDPVTYTSLMLARAMRRLQAALGPPGSPARAAIRQLASMPFADGVRDDATGAMSVL
GQPDVQEMVLYDPVQHEWRFAQQVYHTAARCILI
>gnl|CDD|272847 TIGR00001, 50S_ribosomal_protein_L35, ribosomal protein L35. This ribosomal protein is found in bacteria and organelles only. It is not closely related to any eukaryotic or archaeal ribosomal protein [Protein synthesis, Ribosomal proteins: synthesis and modification]
PKMKTHKAAAKRFKITGSGKIKRKKAGKRHLLTKKSSKRKRQLRKKAVVSKGDLKRVKLLLPY
>gnl|CDD|272848 TIGR00002, 30S_ribosomal_protein_S16_chloroplastic, ribosomal protein S16. This model describes ribosomal S16 of bacteria and organelles [Protein synthesis, Ribosomal proteins: synthesis and modification]
VKIRLKRGGRKKRPFYRIVVADSRSRRDGRYIEELGFYNPITKEDLVKLNVERIKHWLSKGAQPTDTVRK
LLKKAGVF
>gnl|CDD|188014 TIGR00003, COP-associated_protein, copper ion binding protein. This model describes an apparently copper-specific subfamily of the metal-binding domain HMA (pfam00403). Closely related sequences outside this model include mercury resistance proteins and repeated domains of eukaryotic eukaryotic copper transport proteins. Members of this family are strictly prokaryotic. The model identifies both small proteins consisting of just this domain and N-terminal regions of cation (probably copper) transporting ATPases [Transport and binding proteins, Cations and iron carrying compounds]
KQTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEVE
>gnl|CDD|129116 TIGR00004, RutC_family_protein, reactive intermediate/imine deaminase. This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes [Cellular processes, Other]
KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDD
VVKTTVFLTDLNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK
>gnl|CDD|161659 TIGR00005, Ribosomal_large_subunit_pseudouridine_synthase_D, pseudouridine synthase, RluA family. In E. coli, RluD (SfhB) modifies uridine to pseudouridine at 23S RNA U1911, 1915, and 1917, RluC modifies 955, 2504 and 2580, and RluA modifies U746 and tRNA U32. An additional homolog from E. coli outside this family, TruC (SP|Q46918), modifies uracil-65 in transfer RNAs to pseudouridine [Protein synthesis, tRNA and rRNA base modification]
EEQAGQRLDDFLASLLPDLSRSRIQKLIENGQVKVNGKVTANPKLKVKDGDRITVRVPEEEEHEVPPQDI
PLDILFEDEDIIVINKPSGLVVHPGGGNPFGTVLNALLAHCPPIAGVERVGIVHRLDRDTSGLMVVAKTP
LALRELQRQLKNRTVTKEYVALVHGQFDSGGGTVDAPLGRVPNNRGLMAVHPSSEGKPAVTHFRVLERFG
NASLVECELETGRTHQIRVHLQYLGHPLAGDPLYGNKPVPGNNLNGLLNFDRQALHAYELGFIHPATGEI
LEFEAPLPADLVLLLEALR
>gnl|CDD|272849 TIGR00006, Ribosomal_RNA_small_subunit_methyltransferase_H, 16S rRNA (cytosine(1402)-N(4))-methyltransferase. This model describes RsmH, a 16S rRNA methyltransferase. Previously, this gene was designated MraW, known to be essential in E. coli and widely conserved in bacteria [Protein synthesis, tRNA and rRNA base modification]
NFKHQSVLLDEVVEGLNIKPDGIYIDGTLGRGGHSKAILSQLGEGRLIGIDRDPQAIAFAKEILSDLRFV
IIHDNFANFFEYLKELLVTKIDGILVDLGVSSPQLDDPERGFSFMHDGPLDMRMDQSQKLSAAEILNTYS
EEDLEWILKKYGEERFSKRIARAIVERRKKKPIQTTKELAEVISKAVPGFSKYKSIHPATRVFQAIRIYV
NDELEELEEALQFAPNLLAPGGRLSIISFHSLEDRIVKNFFRELSKGPQVPPGLPVKEEQLYALGKRITK
KPITPSEEEIKENPRSRSAKLRVAEKK
>gnl|CDD|272850 TIGR00007, TIGR00007, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase. This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317) [Amino acid biosynthesis, Histidine family]
IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRE
TGVPVQVGGGIRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGEVAVKGWL
EKSEVSLEELAKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKL
GVYGVIVGKALYEGKITLEE
>gnl|CDD|188015 TIGR00008, Translation_initiation_factor_IF-1_chloroplastic, translation initiation factor IF-1. This family consists of translation initiation factor IF-1 as found in bacteria and chloroplasts. This protein, about 70 residues in length, consists largely of an S1 RNA binding domain (pfam00575) [Protein synthesis, Translation factors]
KEDKIEMEGKVTESLPNAMFRVELENGHEVLAHISGKIRMHYIRILPGDRVKVELSPYDLTRGRITYRL
>gnl|CDD|272851 TIGR00009, 50S_ribosomal_protein_L28, ribosomal protein L28. This model describes bacterial and chloroplast forms of the 50S ribosomal protein L28, a polypeptide about 60 amino acids in length. Mitochondrial homologs differ substantially in architecture (e.g. SP|P36525 from Saccharomyces cerevisiae, which is 258 amino acids long) and are not included [Protein synthesis, Ribosomal proteins: synthesis and modification]
MSRKCELTGKGPLSGNNVSHSHRKTKRRFKPNLQKKRVWVPGRFKRLRVSAKCLRT
>gnl|CDD|272852 TIGR00010, Uncharacterized_deoxyribonuclease_MG009, hydrolase, TatD family. PSI-BLAST, starting with a urease alpha subunit, finds a large superfamily of proteins, including a number of different enzymes that act as hydrolases at C-N bonds other than peptide bonds (EC 3.5.-.-), many uncharacterized proteins, and the members of this family. Several genomes have multiple paralogs related to this family. However, a set of 17 proteins can be found, one each from 17 of the first 20 genomes, such that each member forms a bidirectional best hit across genomes with all other members of the set. This core set (and one other near-perfect member), but not the other paralogs, form the seed for this model. Additionally, members of the seed alignment and all trusted hits, but not all paralogs, have a conserved motif DxHxH near the amino end. The member from E. coli was recently shown to have DNase activity [Unknown function, Enzymes of unknown specificity]
LIDAHCHLDFLDFEEDVEEVIERAKAAGVTAVVAVGTDLEDFLRALELAEKYPNVYAAVGVHPLDVDDDT
KEDIKELERLAAHPKVVAIGETGLDYYKADEYKRRQEEVFRAQLQLAEELNLPVIIHARDAEEDVLDILR
EEKPKVGGVLHCFTGDAELAKKLLDLGFYISISGIVTFKNAKSLREVVRKIPLERLLVETDSPYLAPVPY
RGKRNEPAFVRYTVEAIAEIKGIDVEELAQITTKNAKRLFGL
>gnl|CDD|272853 TIGR00011, Putative_Cys-tRNAPro/Cys-tRNACys_deacylase_EbsC, Cys-tRNA(Pro) deacylase. This model represents the YbaK family, bacterial proteins whose full length sequence is homologous to an insertion domain in proline--tRNA ligases. The domain deacylates mischarged tRNAs. The YbaK protein of Haemophilus influenzae (HI1434) likewise deacylates Ala-tRNA(Pro), but not the correctly charged Pro-tRNA(Pro). A crystallographic study of HI1434 suggests a nucleotide binding function. Previously, a member of this family was described as EbsC and was thought to be involved in cell wall metabolism [Protein synthesis, tRNA aminoacylation]
TNAIRLLDKAKIEYEVHEYEVDPDHLDGESAAEKLGVDPHRVFKTLVAEGDKKGPVVAVIPGDEELDLKK
LAKASGGKKAEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDL
IRLLDGTFADIA
>gnl|CDD|272854 TIGR00012, 50S_ribosomal_protein_L29, ribosomal protein L29. This model describes a ribosomal large subunit protein, called L29 in prokaryotic (50S) large subunits and L35 in eukaryotic (60S) large subunits [Protein synthesis, Ribosomal proteins: synthesis and modification]
ELREKSKEELAKKLDELKKELFELRFQKATGQLEKPHRIRQVRRDIARLLTVLRE
>gnl|CDD|129125 TIGR00013, Probable_tautomerase_K2, 4-oxalocrotonate tautomerase family enzyme. 4-oxalocrotonate tautomerase is a homohexamer in which each monomer is very small, at about 62 amino acids. Pro-1 of the mature protein serves as a general base. The enzyme functions in meta-cleavage pathways of aromatic hydrocarbon catabolism. Because several Arg residues located near the active site in the crystal structure of Pseudomonas putida are not conserved among all members of this family, because the literature describes a general role in the isomerization of beta,gamma-unsaturated enones to their alpha,beta-isomers, and because of the presence of fairly distantly related paralogs in Campylobacter jejuni, the family is regarded as not necessarily uniform in function [Energy metabolism, Other]
PFVNIYILKEGRTDEQKRQLIEGVTEAMAETLGANLESIVVIIDEMPKNNYGIGGELVSDRRR
>gnl|CDD|272855 TIGR00014, Putative_arsenate_reductase., arsenate reductase (glutaredoxin). This model describes a distinct clade, including ArsC itself, of the broader ArsC family described by Pfam pfam03960. This clade is almost completely restricted to the Proteobacteria. An anion-translocating ATPase has been identified as the product of the arsenical resistance operon of resistance plasmid R773. When expressed in Escherichia coli this ATP-driven oxyanion pump catalyses extrusion of the oxyanions arsenite, antimonite and arsenate. The pump is composed of two polypeptides, the products of the arsA and arsB genes. The pump alone produces resistance to arsenite and antimonite. This protein, ArsC, catalyzes the reduction of arsenate to arsenite, and thus extends resistance to include arsenate [Cellular processes, Detoxification]
VTIYHNPRCSKSRNTLALLEDKGIEPEVVKYLKNPPTKSELEAIFAKLGLTVAREMIRTKEALYKELGLS
DPNLSDQELLDAMVAHPILLERPIVVAGDGARIGRPPENVLDIL
>gnl|CDD|272856 TIGR00016, Acetate_kinase, acetate kinase. Acetate kinase is involved in the activation of acetate to acetyl CoA and in the secretion of acetate. It catalyzes the reaction ATP + acetate = ADP + acetyl phosphate. Some members of this family have been shown to act on propionate as well as acetate. An example of a propionate/acetate kinase is TdcD of E. coli (SP|P11868), an enzyme of an anaerobic pathway of threonine catabolism. It is not known how many members of this family act on additional substrates besides acetate [Energy metabolism, Fermentation]
MSSMKILVLNAGSSSLKFALFDAVNGEEVLASGLAERIFLPNARIKWVEDGGKKEAELLAGADHQEALKF
ILNTLLKDKIIKLLSEIDLIGHRVVHGGEKFTDSVIITDEVIQKIKDISPLAPLHNPAHLIGIEAALKLF
PLPKAKNVAVFDTAFHQTMPEEAYLYALPYSWYKEHGVRRYGFHGTSHKYVTQRAAKILNKPLDDLNLIV
CHLGNGASVCAIKNGKSIDTSMGFTPLEGLMMGTRSGDIDPAIIFYLAETLGMSADDIENTLNKKSGLLG
ISGLSSDLRDIEDAYAEGNEQAKLAIKVYVHRIAKYIGSYIASLEGNLDAIVFTGGIGENAAMVRELVLE
KLEVLGFELDPELNNAARSGKSGVISTPESKVKILVIPTNEELMIAQDAIRLTK
>gnl|CDD|129128 TIGR00017, Cytidylate_kinase, cytidylate kinase. This family consists of cytidylate kinase, which catalyzes the phosphorylation of cytidine 5-monophosphate (dCMP) to cytidine 5 -diphosphate (dCDP) in the presence of ATP or GTP. UMP and dCMP can also act as acceptors [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
MAMIIAIDGPSGAGKSTVAKAVAEKLGYAYLDSGAMYRAIALAALQNRVDLTSEDALAELISHLDIRFIP
TNGEVEVFLNGEDVSEAIRTQEVANAASKVAVFPKVREALLKRQQALAKNDGIIADGRDIGTVVFPNAEV
KIFLDASVEERAKRRYKQLQIKGNEVNFEELLAEIKERDDRDSNREVAPLKKADDALYLDTSNLSIDEVV
EKILEYA
>gnl|CDD|272857 TIGR00018, Pantothenate_synthetase, pantoate--beta-alanine ligase. This family is pantoate--beta-alanine ligase, the last enzyme of pantothenate biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
MRIIETIPLLRQYIRQLRMEGKTVGFVPTMGNLHDGHMSLIDRAVAENDVVVVSIFVNPMQFGPNEDLEA
YPRTLEEDCALLEKLGVDVVFAPSVHEMYPNGTEQHTTVDVPLGLSEVLEGASRPGHFRGVATIVTKLFN
LVQPDVAYFGEKDAQQLAVIRKLVADLFLDIEIVPVPIVREEDGLALSSRNVYLTAEQRKIAPGLYRALQ
AIAQAIQAGERDLDAVITIAGDILDTKSFRIDYVQLRDADTLEPVSETEPTSAVILVAAYVGDARLIDNI
VV
>gnl|CDD|129130 TIGR00019, Peptide_chain_release_factor_1, peptide chain release factor 1. This model describes peptide chain release factor 1 (PrfA, RF-1), and excludes the related peptide chain release factor 2 (PrfB, RF-2). RF-1 helps recognize and terminate translation at UAA and UAG stop codons. The mitochondrial release factors are prfA-like, although not included above the trusted cutoff for this model. RF-1 does not have a translational frameshift [Protein synthesis, Translation factors]
MKPSLLEKLESLLERYEELEALLSDPEVISDQDKLRKLSKEYSQLEEIVDCYREYQQAQEDIKEAKEILE
ESDPEMREMAKEELEELEEKIEELEEQLKVLLLPKDPNDEKNVILEIRAGTGGDEAAIFAGDLFRMYSRY
AESKGWKVEILSANETELGGYKEVIAEIKGDGVYSRLKFESGVHRVQRVPVTESQGRIHTSAATVAVMPE
LEEVEVDINPADLRIDTFRSSGAGGQHVNTTDSAVRITHLPTGIVVECQDERSQHKNKDKAMKVLRARLY
EAEQEKQQAAQASTRKSQVGSGDRSERIRTYNFPQNRVTDHRINLTLYKLDEVLEGDLDELIEALIAEDQ
AQQLAALSEE
>gnl|CDD|272858 TIGR00020, Peptide_chain_release_factor_2, peptide chain release factor 2. In many but not all taxa, there is a conserved real translational frameshift at a TGA codon. RF-2 helps terminate translation at TGA codons and can therefore regulate its own production by readthrough when RF-2 is insufficient. There is a Pfam model called "RF-1" for the superfamily of RF-1, RF-2, mitochondrial, RF-H, etc [Protein synthesis, Translation factors]
EINEVNNRIEDLTSRLDTVRGSLDPEKKKARLEELEKEMEDPNFWNDQERAQAVIKERSSLEAVLDTLEE
LKNSLEDLSELLELAVEEDDEETFNELDAELKALEKKLAELELRTMLSGEYDANNAYLTIQAGAGGTEAQ
DWASMLYRMYLRWAERRGFKVEIIDYSEGEEAGIKSVTILIKGPYAYGYLKSEQGVHRLVRISPFDANGR
RHTSFASVFVMPEVDDDIDIEIKPEDLRIDTYRASGAGGQHVNKTDSAVRITHIPTGIVVQCQNDRSQHK
NKDSAMKVLKAKLYELEMEKEQAEKDAKEGEKSEIGWGSQIRSYVLHPYSMVKDLRTGYETGNVQAVLDG
DIDQFIEAYLKWKL
>gnl|CDD|272859 TIGR00021, Ribose-5-phosphate_isomerase_A, ribose 5-phosphate isomerase. This model describes ribose 5-phosphate isomerase, an enzyme of the non-oxidative branch of the pentose phosphate pathway [Energy metabolism, Pentose phosphate pathway]
LKRAAAEAAAEYVEDGMVVGLGTGSTVAYFIEALGERVKQEGLDIVGVPTSKQTAELARELGIPLSSLDE
VPELDLAIDGADEVDPNLQLIKGGGGALLREKIVASASKRFIVIADESKLVDKLGKFPLPVEVVPFAWKA
VARKLEKLGGEPTLRQGNKGGPVVTDNGNYILDCHFGKIIPDPEALEEELKSIPGVVETGLFIDMADTVI
VGTKDGVK
>gnl|CDD|129133 TIGR00022, Uncharacterized_protein_HI_0227, YhcH/YjgK/YiaL family protein. This family consists of conserved hypothetical proteins, about 150 amino acids in length. Members with limited information include YhcH, a possible sugar isomerase of sialic acid catabolism, and YjgK [Unknown function, General]
MIIGSITNLNPKVGLPPAIAEAIDFLNATDLNALEPGRHDIDGDRIFMNVMEPETAEPVSKKAELHHRYL
DIQLLLRGEENIEVGTTPPNLSVYEDYLEEDDIQLCADIDDEQTVILKPGMFAVFYPGEPHKPGCVVNGP
EE
>gnl|CDD|272860 TIGR00023, Glycerol-3-phosphate_acyltransferase, acyl-phosphate glycerol 3-phosphate acyltransferase. This model represents the full length of acylphosphate:glycerol 3-phosphate acyltransferase, and integral membrane protein about 200 amino acids in length, called PlsY in Streptococcus pneumoniae, YneS in Bacillus subtilis, and YgiH in E. coli. It is found in a single copy in a large number of bacteria, including the Mycoplasmas but not Mycobacteria or spirochetes, for example. Its partner is PlsX (see TIGR00182), and the pair can replace PlsB for synthesizing 1-acylglycerol-3-phosphate [Fatty acid and phospholipid metabolism, Biosynthesis]
MSLLIVFLLLIGYLIGSIPFAYLVGKILKGIDIREHGSGNPGATNVLRTLGVKAALLVLIFDILKGMLAV
ALSFLLGLFDFLPGLVAIAAVLGHIFPIFFKFKGGKGVATSGGSLLPISPWLFLIMLATWLFVTLVTKYV
SLSSIVTAIVLPFYVLWFHLPYLYIPVTLLLIFVIYRHRANIQRLLNGTEPKVWQK
>gnl|CDD|129135 TIGR00024, Uncharacterized_protein_MJ0037, putative phosphoesterase, SbcD/Mre11-related. Members of this uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11. SbcD is a subunit of the SbcCD nuclease of E. coli that can cleave DNA hairpins to unblock stalled DNA replication. All members of this family are archaeal [Unknown function, Enzymes of unknown specificity]
LMDDLRIEDRVLIIGDKAVIADLHLGFERHLDEQGVMVPGFQFREIIERALSIADKYGIEALIINGDLKH
EFKKGLEWRFIREFIEVTFRDLILIRGNHDALIPYIGLSGEESIRIGKYLIFHGHAVPDEEDLDAKVLIF
GHEHPAVKLRDSAAGYKFPCFLLGEVEDKRVIVLPAFNPLCAGSDVLLDRPLSPILRKSLREFEVYAIED
FEIMLFGTLLDLRKF
>gnl|CDD|272861 TIGR00025, Mtu_efflux, ABC transporter efflux protein, DrrB family. The seed members for this model are a paralogous family of Mycobacterium tuberculosis. Nearly all proteins scoring above the noise cutoff are from high-GC Gram-positive organisms. The members of this paralogous family of efflux proteins are all found in operons with ATP-binding chain partners. They are related to a putative daunorubicin resistance efflux protein of Streptomyces peucetius. This model represents a branch of a larger superfamily that also includes NodJ, a part of the NodIJ pair of nodulation-triggering signal efflux proteins. The members of this branch may all act in antibiotic resistance
LLRVGAQIILTMFIPITFMVGLNLLPGGSVTHNRGATFIPVLMALAAISTAFTGQAIAVARDRRYGALKR
LGATPLPRLGILAGRSLAVVARVFLQTLILLVIGFVLGFRFAGGALTALTLGAVIIALGTALFAALGLVA
GGTLQAEIVLAVANLVWFIFALLSAGLVPLNLIPTWIKWFVRVQPSSYATEALRQAATVSVDTFGAVRDL
VVVLAFWVALAALAAIRLRRRT
>gnl|CDD|211538 TIGR00026, Hypothetical_protein_Rv1261c/MT1299/Mb1292c., deazaflavin-dependent oxidoreductase, nitroreductase family. This model represents a family of proteins found in paralogous families in the genera Mycobacterium and Streptomyces. Seven members are in Mycobacterium tuberculosis. Member protein Rv3547 has been characterized as a deazaflavin-dependent nitroreductase [Unknown function, Enzymes of unknown specificity]
GGIARGLPVLLLTTTGRKTGKPRTTPVYYVRHDPGVLVVASNGGAPRHPDWYKNLKANPRVRVRVGGKVF
VATARLVSGDERAQLWAGVVRLYPRYQRYQSRTDRPIPVVVLT
>gnl|CDD|272862 TIGR00027, Hypothetical_protein_Rv0893c/MT0917/Mb0917c., methyltransferase, TIGR00027 family. This model represents a set of probable methyltransferases, about 300 amino acids long, with essentially full length homology. Members share an N-terminal region described by Pfam model pfam02409. Included are a paralogous family of 12 proteins in Mycobacterium tuberculosis, plus close homologs in related species, a family of 8 in the archaeon Methanosarcina acetivorans, and small numbers of members in other species, including plants [Unknown function, Enzymes of unknown specificity]
GRTALGVAAARAIETQRPDRLFRDPYAAAFLGAAGRAAMPLDGLLRADAGAYDGLLRGFADFIAVRTRFF
DDFLLAAVAAGIRQVVILGAGLDTRAYRLPWPDGTRVFEVDQPAVLAFKEKVLAELGAEPPAHRRAVPVD
LRQDWPAALAAAGFDPTAPTAWLWEGLLMYLTEEAVDALLAFIAELSAPGSRLAFDYVRPLDGEWRAGMR
APVYHAARGVDGSGLVFGIDRADVAEWLAERGWRASEHTPGELARRYGRP
>gnl|CDD|272863 TIGR00028, Hypothetical_protein_Rv2872/MT2939/Mb2897., toxin-antitoxin system PIN domain toxin. Members of this protein consist almost entirely of a PIN (PilT N terminus) domain (see pfam01850). This family was originally defined a set of twelve closely related paralogs found in Mycobacterium tuberculosis, but additional members are found now Synechococcus sp. WH8102, etc. Inspection of genomic regions suggests these represent toxin components of toxin-antitoxin regions, potentially important to creating dormant persister cells
MLLLDVNVLLAAVNRDHPHHDAARAWLDRFAAGGDWATCPLTLAGFVRLLTNPRVLPAPLSPAEAIAVVA
AFLATPRHRLLWPGPRHLAVLRGLADPVIAGGRLVTDAHLAALAREHGAELVTFDRGFARFAGIRWRDPL
TG
>gnl|CDD|211539 TIGR00029, 30S_ribosomal_protein_S20, ribosomal protein S20. This family consists of bacterial (and chloroplast) examples of the bacteria ribosomal small subunit protein S20 [Protein synthesis, Ribosomal proteins: synthesis and modification]
MANIKSAEKRIRQNEKRRLHNASQKSKMKTIIKKVYAAIAAGDKDKAQEAFKEAAKKLDRAARKGIIHKN
KAARKKSRLAAQLNKLA
>gnl|CDD|129141 TIGR00030, 30S_ribosomal_protein_S21, ribosomal protein S21. This model describes bacterial ribosomal protein S21 and most mitochondrial and chloroplast equivalents [Protein synthesis, Ribosomal proteins: synthesis and modification]
PTVKVKEGESIDSALRRFKRKLEKEGILRELKKRRYYEKPSERRRRKEKAAAKRIRKK
>gnl|CDD|272864 TIGR00031, UDP-galactopyranose_mutase, UDP-galactopyranose mutase. This enzyme is involved in the conversion of UDP-GALP into UDP-GALF through a 2-keto intermediate. It contains FAD as a cofactor. The gene is known as glf, ceoA, and rfbD. It is known experimentally in E. coli, Mycobacterium tuberculosis, and Klebsiella pneumoniae [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
MFDYIIVGAGLSGIVLANILAQLNKRVLVVEKRNHIGGNCYDEVDETILFHQYGPHIFHTNNQYVWDYIS
PFFELNNYQHRVLALYNNLDLTLPFNFNQFRKLLGVKDAQELQNFFNAQFKYGDHVPLEELQEIADPDIQ
LLYQFLYQKVYKPYTVKQWGLPAEEIDPFVIGRVPVVLSEDSSYFPDRYQGLPKGGYTKLFEKMLDHPLI
DVKLNCHINLLKDKDSQLHFANKAIRKPVIYTGLIDQLFGYRFGALQYRSLKFEWERHEFKNFQGYAVVN
FPLNVPITRIVEYKHLTYVGSKQTIVSKEYPGEWKVGDPEPYYPVNDNKNMALFKKYLELASREDNLILL
GRLAEYQYYDMDQAILAALYKAEQLLS
>gnl|CDD|199987 TIGR00032, Argininosuccinate_synthase, argininosuccinate synthase. argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a very unusual clustering in the alignment, with a deep split between one cohort of E. coli, H. influenzae, and Streptomyces, and the other cohort of eukaryotes, archaea, and the rest of the eubacteria [Amino acid biosynthesis, Glutamate family]
KVVLAYSGGLDTSVCLKWLREKGYEVIAYTADVGQPEEDIDAIPEKALEYGAENHYTIDAREEFVKDYGF
AAIQANAFYEGTYPLSTALARPLIAKKLVEAAKKEGANAVAHGCTGKGNDQERFERSIRLLNPDLKVIAP
WRDLNFTREEEIEYAIQCGIPYPMSKEKPYSIDENLWGRSIEAGILEDPSTEPPEDIYMWTKFPDEATPD
EPEVVTIDFEQGVPVALNGVSLDPVELILEANEIAGKHGVGRIDIIENRIIGLKSREIYEAPGAALLIIA
HRDLETLTLTRDVLEFKDIVEEQYSELIYQGLWFDPLAEALDAFIRKTQERVTGTVRVKLFKGNAIVIGR
TSPYSLYDEELVSMEKDDVFDPRDAIGFITMRGLQIKDYREKKK
>gnl|CDD|272865 TIGR00033, Chorismate_synthase, chorismate synthase. Homotetramer (noted in E.coli) suggests reason for good conservation [Amino acid biosynthesis, Aromatic amino acid family]
FRVTTFGESHGKAVGAIIDGCPAGLPLTEEDIQPDLDRRRPGYSRGTRMRKENDEVEILSGVFEGKTTGA
PIALMIRNKDVRSSDYSDIRTFPRPGHADYTYWLKYGIDDYRGGGRSSARETAARVAAGAVAKKLLAETS
GIEIVAYVTQIGEVEIPRVYYDPEEKERVDSSPVRCPDPEAEKEMVAEIDKAKKDGDSIGGVVECVARNV
PVGLGEPLFDKLDARLAHAMMSIPAVKGVEIGDGFELASMRGSEANDEFVFEDGGIRRKTNNSGGILGGI
TNGEPIRVRIAFKPTPTIGKPQKTVDLDTEEPALATKGRHDPCVVPRAVPVVEAMTALVLADALLEQRAS
D
>gnl|CDD|129145 TIGR00034, aroFGH, phospho-2-dehydro-3-deoxyheptonate aldolase [Amino acid biosynthesis, Aromatic amino acid family]
DDLRIVRIDELLTPAELAAKFPLTPKQAANVAQSRQEIADIIAGKDDRLLVVIGPCSIHDPEAAIEYATR
LKALREELKDDLEIVMRVYFEKPRTTVGWKGLINDPDLNGSFRINHGLRIARKLLLDLVNLGLPIAGEFL
DMISPQYLADLFSWGAIGARTTESQVHRELASGLSCPVGFKNGTDGNLQVAIDAIRAAAAPHYFLSVTKD
GQMAIVQTSGNPDGHIILRGGKKPNYSAADVAAAKKQLEKAGLPPHLMIDFSHGNSNKDHRRQPDVAEDV
CEQIANGSKAIIGVMIESNLVEGNQSIPGGQPLKYGQSITDACIGWEDTEALLRQLADAVRTRR
>gnl|CDD|213495 TIGR00035, Aspartate_racemase, aspartate racemase. Asparate racemases and some close homologs of unknown function are related to the more common glutamate racemases, but form a distinct evolutionary branch. This model identifies members of the aspartate racemase-related subset of amino acid racemases [Energy metabolism, Amino acids and amines]
ENMIGILGGMGPLATAELFRRINEKTKAKRDQEHPAEVLFNNPNIPDRTAYILGRGEDRPRPILIDIAVK
LENAGADFIIMPCNTAHKFAEDIQKAIGIPLISMIEETAEAVKEDGVKKAGLLGTKGTMKDGVYEREMKK
HGIEIVTPDKEEQEAIMSGIYDEVKAGNIELGRELLLKIAKELEERGAEGIILGCTELSLILKADDLDVP
LIDPMDVIAEAAVKLALEG
>gnl|CDD|129147 TIGR00036, 4-hydroxy-tetrahydrodipicolinate_reductase, 4-hydroxy-tetrahydrodipicolinate reductase [Amino acid biosynthesis, Aspartate family]
TIKVAVAGAAGRMGRELIKAALAAEGLQLVAAFERHGSSLQGTDAGELAGIGKVGVPVTDDLEAVETDPD
VLIDFTTPEGVLNHLKFALEHGVRLVVGTTGFSEEDKQELADLAEKAGIAAVIAPNFSIGVNLMFKLLEK
AAKYLGDYDIEIIELHHRHKKDAPSGTALKTAEMIAEARGERLKNVAVTEREGLTGERGREEIGIHAVRG
GDVVGEHTVMFAGDGERLEITHRASSRACFANGAVRAARWLADKEAGVYDMEDVLD
>gnl|CDD|272866 TIGR00037, Translation_initiation_factor_5A, translation elongation factor IF5A. Recent work (2009) changed the view of eIF5A in eukaryotes and aIF5A in archaea, hypusine-containing proteins, from translation initiation factor to translation elongation factor [Protein synthesis, Translation factors]
MSATKQVEVSALRVGGYVVIDGEPCKIVDISTSKPGKHGHAKARVVAIGIFDGQKREFVSPVTSKVEVPI
VDRREAQVLAIMGGMVQLMDLETYETFELPIPEELGDSLEPGFEVEYIEALGQRKIIRFK
>gnl|CDD|272867 TIGR00038, efp, translation elongation factor P. function: involved in peptide bond synthesis. stimulate efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (by similarity). The trusted cutoff of this model is set high enough to exclude members of TIGR02178, an EFP-like protein of certain Gammaproteobacteria [Protein synthesis, Translation factors]
ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQ
YLYKDGDSYVFMDTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVK
GDTASGSTKPATLETGAVVQVPLFIEEGEKIKVDTRTGEYVERA
>gnl|CDD|272868 TIGR00039, Putative_6-carboxy-5678-tetrahydropterin_synthase, 6-pyruvoyl tetrahydropterin synthase/QueD family protein. This model has been downgraded from hypothetical_equivalog to subfamily. The animal enzymes are known to be 6-pyruvoyl tetrahydropterin synthase. The function of the bacterial branch of the sequence lineage had been thought to be the same, but many are now taken to be QueD, and enzyme of queuosine biosynthesis. Queuosine is a hypermodified base in the wobble position of some tRNAs in most species. A new model is built to be the QueD equivalog model [Protein synthesis, tRNA and rRNA base modification]
MFGIHKEFSFSAAHRLPGHEGKCGNLHGHSYKVDVEVSGERDPKTGMVMDFSDLKKIVKEVIDEPLDHKL
LNDDVNYLENPTSENVAVYIFDNLKEYLIPVENLVKVKEEETPAEIRIYRGPTL
>gnl|CDD|272869 TIGR00040, Putative_metallophosphoesterase, phosphoesterase, MJ0936 family. Members of this largely uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterized archaeal putative phosphoesterases described by TIGR00024. In this family, the His residue in GNHD portion of the motif is not conserved. The member MJ0936, one of two from Methanococcus jannaschii, was shown () to act on model phosphodiesterase substrates; a divalent cation was required [Unknown function, Enzymes of unknown specificity]
MKILVISDTHGPLRATELPVELFNLESNVDLVIHAGDLTSPFVLKEFEDLAAKVIAVRGNNDGERDELPE
EEIFEAEGIDFGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNG
NTPSYAILDVDKDKVTAL
>gnl|CDD|161676 TIGR00041, Thymidylate_kinase, dTMP kinase. Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
MRGMFIVIEGIDGAGKTTQANLLKKLLQENGYDVLFTREPGGTPIGEKIRELLLNENDEPLTDKAEALLF
AADRHEHLEDKIKPALAEGKLVISDRYVFSSIAYQGGARGIDEDLVLELNEDALGDMPDLTIYLDIDPEV
ALERLRKRGELDREEFEKLDFFEKVRQRYLELADKEKSIHVIDATNSVEEVEQDI
>gnl|CDD|272870 TIGR00042, Non-canonical_purine_NTP_pyrophosphatase, non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family. Saccharomyces cerevisiae HAM1 protects against the mutagenic effects of the base analog 6-N-hydroxylaminopurine, which can be a natural product of monooxygenase activity on adenine. Methanococcus jannaschii MJ0226 and E. coli RdgB are also characterized as pyrophosphatases active against non-standard purines NTPs. E. coli RdgB appears to act by intercepting non-canonical deoxyribonucleotide triphosphates from replication precursor pools [DNA metabolism, DNA replication, recombination, and repair]
KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFV
DALNGFPGIYSARYQGTDIGNLEKILKLLEGVENRQAYFVCVIGYCDPNGEPLVFEGIVKGKITREPRGT
YGFGYDPIFIPPEEGKTFAELTTEEKNKISHRGKAFKKFKKFLL
>gnl|CDD|272871 TIGR00043, Endoribonuclease_YbeY, rRNA maturation RNase YbeY. This metalloprotein family is represented by a single member sequence only in nearly every bacterium. Crystallography demonstrated metal-binding activity, possibly to nickel. It is a predicted to be a metallohydrolase, and more recently it was shown that mutants have a ribosomal RNA processing defect [Protein synthesis, Other]
GELSLLFVDDEEIQELNREYRDKDYPTDVLSFPYEEEEPPGGFPEEVLGDIVISLEVAKEQAKEYGHSLE
RELAHLTVHGLLHLLGYDHETEDEEKEMFALEEEILALLG
>gnl|CDD|129155 TIGR00044, Hypothetical_UPF0001_protein_yggS., pyridoxal phosphate enzyme, YggS family. Members of this protein family include YggS from Escherichia coli and YBL036C, an uncharacterized pyridoxal protein of Saccharomyces cerevisiae [Unknown function, Enzymes of unknown specificity]
MNDIAHYLEQIRTKIEAAATRCNRNPEEVKLLAVSKTKPASAIQEAYDAGQRAFGENYVQELVEKIRHLE
ELGLLEWHFIGPLQSNKSRLVVENFDWCHTIDSLKIATKLNEQREALLPPLNVLLQINISDEESKSGIQP
EELLELAAQLEELKHLKLRGLMTIGAPTDSYVDQEEVFRQMKVLFAQIKQRSPHGTIDTLSMGMSDDFEE
AIAAGATMVRIGTAIFGAR
>gnl|CDD|272872 TIGR00045, Glycerate_kinase, glycerate kinase. The only characterized member of this family so far is the glycerate kinase GlxK (EC 2.7.1.31) of E. coli. This enzyme acts after glyoxylate carboligase and 2-hydroxy-3-oxopropionate reductase (tartronate semialdehyde reductase) in the conversion of glyoxylate to 3-phosphoglycerate (the D-glycerate pathway) as a part of allantoin degradation [Energy metabolism, Other]
KIVIAPDSFKESLSAQEVAEAIKKGFRRVFPDAEYVLIPVADGGEGTVDALIHATDGERVTVRVTGPLGE
KVEASYGILGDQQTAVIEMAAASGLELVPAEKRNPLQTSSYGTGELIRHALDHGAKKIILGIGGSATNDG
GAGMLQALGVRFLDADGQELGPGGGALAELASIDLSNLDPRLKDVHFRVACDVTNPLCGENGAARVFGPQ
KGADPAMVEELDQALQHYARVIKRATGKDVRTIPGAGAAGGMGAGLLAFLGARLKPGIDLVLELLDLEQK
IKDADLVITGEGRLDRQSLMGKAPVGVAKRAKKYGVPVIAIAGSLGDGVDVLPQHGIDAAFSILPSPMPL
EDALQNASTNLERTAENIARLLLLG
>gnl|CDD|272873 TIGR00046, Ribosomal_RNA_small_subunit_methyltransferase_E, RNA methyltransferase, RsmE family. Members of this protein family, previously called conserved hypothetical protein TIGR00046, include the YggJ protein of E. coli, which has now been shown to methylate U1498 in 16S rRNA [Protein synthesis, tRNA and rRNA base modification]
RMRIVYHPEQLEEATISLTEEEAHHLVRVLRLKKGDKLKLLDGDGFIYHCEIKKISKKFVKCKVLEGESE
KRELPLKIHLAIVLIKGKKMEFIIRKLTELGVSKIIPFNAERSVVKLDIEAIKKLERWQKIAIEAAEQSG
RNIVPEIKPPMNLKEKCAEAYEEALKLNFHPEASPLSNNLPIPAGNIVIIIGPEGGFSEKEIQLLAEKGF
TPVLLGPRILRTETAPLYALSILQALLEDL
>gnl|CDD|272874 TIGR00048, Dual-specificity_RNA_methyltransferase_RlmN, 23S rRNA (adenine(2503)-C(2))-methyltransferase. Members of this family are RlmN, a 23S rRNA m2A2503 methyltransferase in the radical SAM enzyme family. Closely related is Cfr, a Staphylococcus sciuri plasmid-borne homolog to this family, Cfr, has been identified as essential to transferrable resistance to chloramphenicol and florfenicol. Cfr methylates 23S RNA at a different site [Protein synthesis, tRNA and rRNA base modification]
TAKDGKPSLLDLTLQELRQWLKDLGEKPFRAKQIMKWLYHKGCDSFDDMTNLSKVLREKLNEVFEIRTPE
IAHEQRSSDGTIKYLFALGDGQTIETVLIPEDDRATVCVSSQVGCALGCTFCATAKGGFNRNLEASEIIG
QVLRVQKIVGETGERVSNVVFMGMGEPLLNLNEVVKAMEIMNDDFGFGISKRRITISTSGVVPKIDKLAD
KMLQVALAISLHAPNDEIRSSLMPINKKYNIETLLAAVRRYLEKTGRRVTFEYVLLDGVNDQVEHAEELA
ELLKGTKCKVNLIPWNPFPEADYGRPSNSQIDRFAKVLMSYGFTVTIRKSRGDDIDAACGQLRAKDVIDR
TKRTL
>gnl|CDD|272875 TIGR00049, Uncharacterized_protein_in_nifU_5'region, Iron-sulfur cluster assembly accessory protein. Proteins in this subfamily appear to be associated with the process of FeS-cluster assembly. The HesB proteins are associated with the nif gene cluster and the Rhizobium gene IscN has been shown to be required for nitrogen fixation. Nitrogenase includes multiple FeS clusters and many genes for their assembly. The E. coli SufA protein is associated with SufS, a NifS homolog and SufD which are involved in the FeS cluster assembly of the FhnF protein. The Azotobacter protein IscA (homologs of which are also found in E.coli) is associated which IscS, another NifS homolog and IscU, a nifU homolog as well as other factors consistent with a role in FeS cluster chemistry. A homolog from Geobacter contains a selenocysteine in place of an otherwise invariant cysteine, further suggesting a role in redox chemistry [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
TLTDSAAKRIKALLAGEGEPNLGLRVGVKGGGCSGLQYGLEFDDEPNEDDEVFEQDGVKVVVDPKSLPYL
DGSEIDYVEELLGSGFTFTNPNAKGTCGCGKSFSV
>gnl|CDD|272876 TIGR00050, Uncharacterized_tRNA/rRNA_methyltransferase_LasT, RNA methyltransferase, TrmH family, group 1. This is part of the trmH (spoU) family of S-adenosyl-L-methionine (AdoMet)-dependent methyltransferases, and is now characterized, in E. coli, as a tRNA:Cm32/Um32 methyltransferase. It may be named TrMet(Xm32), or TrmJ, according to the nomenclature style chosen [Protein synthesis, tRNA and rRNA base modification]
LENIRIVLVEPSHPGNIGSIARAMKNMGLTELRLVNPRVKLEEEAYALAAGARDILDNAKVVDTLDEALD
DCDFVVGTSARSRNLQRPMLTPRELAPKLVAEKGKVALVFGREDSGLTNEELQKCHVLVSIPTSEEYPSL
NLSHAVAVILYELRMAWLAQQENLSEMPYATVDDLELLLEHLEETLLSLGFIPEHKPRQVMRKFRRLYGR
AGLEKRELHILRGILRSIEKRIK
>gnl|CDD|129161 TIGR00051, Acyl-CoA_thioesterase_YbgC, acyl-CoA thioester hydrolase, YbgC/YbaW family. This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon [Unknown function, General]
PVRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEGVAFVVVNINIEYKKPARLDDVLEI
RTQIEELNGFSFVFSQEIFNEDEALLKAATVIVVCVDPKKQKPVAIP
>gnl|CDD|129162 TIGR00052, GDP-mannose_pyrophosphatase_NudK, nudix-type nucleoside diphosphatase, YffH/AdpP family. Members of this family include proteins of about 200 amino acids, including the recently characterized nudix hydrolase YffH, shows to be highly active as a GDP-mannose pyrophosphatase. It also includes the C-terminal half of a 361-amino acid protein, TrgB from Rhodobacter sphaeroides, shown experimentally to help confer tellurite resistance. This model also hits a region near the C-terminus of a 1092-amino acid protein of C. elegans [Unknown function, Enzymes of unknown specificity]
NQQEIIIKDTLYSGFFSLLHNIFYHRLFKGGESIRVTREIYDRGNAAAVLLYDPKKDTVVLIEQFRIAAY
VNGEEPWLLELSAGMVEKGESPEDVARREAIEEAGYQVKNLRKLLSFYMSPGGVTELIHLFIAEVDDNQA
AGIGGGADEEEIEVLHLVFSQALQWIKEGKIDNGKTVILLQWLQL
>gnl|CDD|272877 TIGR00053, mRNA_interferase_YafQ, addiction module toxin component, YafQ family. This model represents a cluster of eubacterial proteins and a cluster of archaeal proteins, all of which are uncharacterized, from 85 to 102 residues in length, and similar in sequence. These include YafQ, a ribosome-associated endoribonuclease that serves as part of a toxin-antitoxin system, for which DinJ is the antidote component [Cellular processes, Adaptations to atypical conditions]
MLKIEYSKQFDKDLKKLQKRDGKDLKKLKKKMEELINTLPLPEHYKDHPLRGSWKGFRDCHIKPDVILIY
KVKDDTLIFVRLGHHSELFK
>gnl|CDD|272878 TIGR00054, Putative_zinc_metalloprotease_slr1821, RIP metalloprotease RseP. Members of this nearly universal bacterial protein family are regulated intramembrane proteolysis (RIP) proteases. Older and synonymous gene symbols include yaeL in E. coli, mmpA in Caulobacter crescentus, etc. This family includes a region that hits the PDZ domain, found in a number of proteins targeted to the membrane by binding to a peptide ligand. The N-terminal region of this family contains a perfectly conserved motif HEXGH as found in a number of metalloproteinases, where the Glu is the active site and the His residues coordinate the metal cation. Membership in this family is determined by a match to the full length of the seed alignment; the model also detects fragments as well matches a number of members of the PEPTIDASE FAMILY S2C. The region of match appears not to overlap the active site domain [Protein fate, Degradation of proteins, peptides, and glycopeptides]
SFLWILASILALAVLIFVHELGHFLAARLCGIKVERFSIGFGPKILKFKKNGTEYAISLIPLGGYVKMKG
LDKEMEVKPPETDGDLFNNKSVFQKAIIIFAGPLANFIFAIFVYIFISLIGVPGYEVGPVIELLDKNSIA
LEAGIEPGDEILSVNGNKIPGFKDVRQQIADIAGEPMVEILAERENWTFEVMKELIPRGPKIEPVLSDVT
PNSPAEKAGLKEGDYIQSINGEKLRSWTDFVSAVKENPGKSMDIKVERNGETLSISLTPEAKGKIGIGIS
PSLAPLEVSYGILNAFAKGASATVDIVKLILTNLGKLITGSFKLKNLSGPVGIVKGAGSSANSGIVYLLQ
FGAFLSINLGIMNLLPIPALDGGQLLFLFIEAIRGKPLPEKVQAFVYRIGVAFLLFLMGLGLFNDLLRL
>gnl|CDD|129165 TIGR00055, Isoprenyl_transferase, undecaprenyl diphosphate synthase. This enzyme builds undecaprenyl diphosphate, a molecule that in bacteria is used a carrier in synthesizing cell wall components. Alternate name: undecaprenyl pyrophosphate synthetase. Activity has been demonstrated experimentally for members of this family from Micrococcus luteus, E. coli, Haemophilus influenzae, and Streptococcus pneumoniae [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
RHVAIIMDGNGRWAKKKGKPRAYGHKAGVKSLRRILRWCANLGVECLTLYAFSTENWKRPKEEVDFLMEL
FEKKLDREVKELHRYNVRIRIIGDLSLLSKELQEKIKKAEEDTKNNTDFTLNIAFNYGGRNEILHAVKQI
AEKVKSGKLLPEDIDEETLNKHLYTANLPPVDLLIRTSGEMRISNFLLWQSSYAELYFTDILWPDFDPQD
FELAILDFQFRHRRFG
>gnl|CDD|129166 TIGR00056, Probable_ABC_transporter_permease_protein_HI_1086, ABC transport permease subunit. This model describes a subfamily of ABC transporter permease subunits. One member of this family has been associated with the toluene tolerance phenotype of Pseudomonas putida, another with L-glutamate transport, another with maintenance of lipid asymmetry. Many bacterial species have one or two members. The Mycobacteria have large paralogous families included in the DUF140 family but excluded from this subfamily on based on extreme divergence at the amino end and on phylogenetic and UPGMA trees on the more conserved regions [Hypothetical proteins, Conserved]
MHLNLLIAKLGKWIIETGRAFLLTGLMLFYLFKGKPNIRNFPLLLKQLNEVGPESLPIILLTSFFIGMVI
ALQGALQLIAFGAETSIGGLVALSLLRELGPVLTALVVAGRVGSAFTAEIGTMRITEQLDALEMMATNPV
EFLVLPRVLACVIMLPLLTVLSDVAGILGGAFIASSLLGIGSGSFWSKMQNAVGWWDIFAGLVKAPFFGV
AIAIIGCYYGFTTKGGTEGVGRSTTRSVVTSLLAILILDFILSAIMFGS
>gnl|CDD|272879 TIGR00057, Putative_threonylcarbamoyl-AMP_synthase, tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family. Has paralogs, but YrdC called a tRNA modification protein. Ref 2 authors say probably heteromultimeric complex. Paralogs may mean its does the final binding to the tRNA [Protein synthesis, tRNA and rRNA base modification]
IHPENPSQRGIEQAVKILRKGGIVVYPTDTVYGIGADALDEDAVRRLYRIKGRPSNKPLTVLVSDLSEIE
KYAYVPDDAKRLMKKFWPGPLTLVLKKTPEIPRRVSGKRKTIGIRVPDNPIALELLEELGKPIVATSANL
SGKPSATDVEEAVDELGKLVDLIIDAGPCLGGEPSTIIDLTDDTPKVLREGVGSEPIEKVL
>gnl|CDD|129168 TIGR00058, The_Polypeptide, hemerythrin family non-heme iron protein. This family includes oxygen carrier proteins of various oligomeric states from the vascular fluid (hemerythrin) and muscle (myohemerythrin) of some marine invertebrates. Each unit binds 2 non-heme Fe using 5 H, one E and one D. One member of this family,from the sandworm Nereis diversicolor, is an unusual (non-metallothionein) cadmium-binding protein. Homologous proteins, excluded from this narrowly defined family, are found in archaea and bacteria (see pfam01814)
IPEPYVWDESFKVFYDNLDEEHKTLFNGIFALAADNSATALKELIDVTVLHFLDEEAMMIAANYSDYDEH
KKAHDDFLAVLRGLKAPVPQDDLLYAKDWLVNHIKTTDFKYKGKL
>gnl|CDD|272880 TIGR00059, 50S_ribosomal_protein_L17, ribosomal protein L17. Eubacterial and mitochondrial. The mitochondrial form, from yeast, contains an additional 110 amino acids C-terminal to the region found by this model [Protein synthesis, Ribosomal proteins: synthesis and modification]
SYRKLGRTSAHRKALLRNLASALIRHEKIETTLAKAKELRRVVEKLITLAKVDNFNNRREAKAYIQNKEI
VHKLFSEIAPRYAQRPGGYTRILKLGPRRGDAAPMAIIELV
>gnl|CDD|272881 TIGR00060, 50S_ribosomal_protein_L18, ribosomal protein L18, bacterial type. The archaeal and eukaryotic type rpL18 is not detectable under this model [Protein synthesis, Ribosomal proteins: synthesis and modification]
KKSARLRRHKRIRRKLRGTGEANRPRLVVFRSNRHIYAQVIDDVKGVTLASASTLEKKLKSTGNKDAAKK
VGKLVAERLKEKGIKDVVFDRGGYKYHGRVAALAEAAREAGLNF
>gnl|CDD|129171 TIGR00061, 50S_ribosomal_protein_L21, ribosomal protein L21. Eubacterial and chloroplast [Protein synthesis, Ribosomal proteins: synthesis and modification]
YAIVEIGGKQYKVEEGQTVRIEKLDAAPGETVEFDKVLMVNKGDDVKIGKPYVEGAKVVAEVEKHGRGKK
VKVYKYRRRKHSRKKQGHRQPYTKVKVTKIV
>gnl|CDD|272882 TIGR00062, 50S_ribosomal_protein_L27, ribosomal protein L27. Eubacterial, chloroplast, and mitochondrial. Mitochondrial members have an additional C-terminal domain [Protein synthesis, Ribosomal proteins: synthesis and modification]
MATKKGVGSTKNGRDSAAKRLGVKKAGGQFVRAGSIIVRQRGTKFHPGENVGMGKDHTLFALSDGVVKFE
LKGFHRKRKFVSVV
>gnl|CDD|129173 TIGR00063, GTP_cyclohydrolase_1, GTP cyclohydrolase I. alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) catalyzes the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP. This reaction is the first step in the biosynthesis of tetrahydrofolate in prokaryotes, of tetrahydrobiopterin in vertebrates, and of pteridine-containing pigments in insects [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
IAGAMREILELIGEDLNREGLLETPKRVAKMYVEIFSGYDYANFPKITLAIFQEKHDEMVLVRDITFTST
CEHHLVPFDGKAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEATH
MCMKMRGIRKPGSATVTSALGGLFKSDQKTRAEFLRLVRH
>gnl|CDD|272883 TIGR00064, Signal_recognition_particle_receptor_FtsY, signal recognition particle-docking protein FtsY. There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein [Protein fate, Protein and peptide secretion and trafficking]
KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLLKNTDLEL
IVEENKPNVILFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKE
GADPAAVAFDAIQKAKARNIDVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQN
ALEQAKVFNEAVGLTGIILTKLDGTAKGGIILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF
>gnl|CDD|272884 TIGR00065, Cell_division_protein_FtsZ, cell division protein FtsZ. This family consists of cell division protein FtsZ, a GTPase found in bacteria, the chloroplast of plants, and in archaebacteria. Structurally similar to tubulin, FtsZ undergoes GTP-dependent polymerization into filaments that form a cytoskeleton involved in septum synthesis [Cellular processes, Cell division]
MDEIETEFRELIQPSNKAKIKVIGVGGGGNNTVNRMLEEGVEGVEFIAINTDAQHLKTTKADKKILIGKK
LTRGLGAGGNPEIGRKAAEESRDEIRKLLEGADMVFITAGMGGGTGTGAAPVVAKIAKELGALTVAVVTK
PFKFEGLKRRKKAEEGLERLKQAVDTLIVIPNDKLLEVVPNLPLNDAFKVADDVLVRAVKGISELITKPG
LINIDFADVRAVMSGGGVAMMGIGEALGEDTANRAFEAVRKALSSPLLDVDKISGAKGALVHITGGADLT
LLEAEEIQEIITSELDQDANIIWGAIIDPNLEDEIRVTIVATGVKSQIFFGSEKSKDTVSLPIDNVPKL
>gnl|CDD|129176 TIGR00066, Contains:_Gamma-glutamyltranspeptidase_large_chain, gamma-glutamyltranspeptidase. Also called gamma-glutamyltranspeptidase (ggt). Some members of this family have antibiotic synthesis or resistance activities. In the case of a cephalosporin acylase from Pseudomonas sp., the enzyme was shown to retain some gamma-glutamyltranspeptidase activity. Other, more distantly related proteins have ggt-related activities and score below the trusted cutoff [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
GMVASLHALASEIGEDILKEGGNAFDAAVAVGLALAVVEPFMTGLGGGGFMLISGKKTKDTTAIDFRERA
PAKATRDMFLDKSGNPLPGKSLTGGLAIGVPGTVAGLEAALKKYGTLPLKDLIEPAIKLARNGFPINEAL
ADTLELYEEVLLTTKEDSKDIFNPTGKPLKEGDTLVQKDLAKSLELIAENGPDAFYKGDIAESIIDTLQK
NGGIMTKKDLAAYDVEIRKPLSGDYRGYQVYTTPPPSSGGIHLLQALNILENFDLSQYGDGSAETYQLLA
EAMKLSYADRSRYLGDPEFVDVPLEELLDKRYAKELAQSIKINKVDPKSTIYPGAYQPNEGSQTTHFSVV
DRDGNAVSLTTTINLEFGSGVHAPDTGILLNNEMDDFSLKPGGANAVEPNKRPLSSMAPTIVLKDGKPDL
VVGSPGGSRIITTVLQTIVRHIDYGMPLAEAVSEPRIHHQWLPDELRLEKGFPDDVLQLLKDMGHKVTLK
EVFPMGVVQAIRVDPEGWLYGVSDPR
>gnl|CDD|272885 TIGR00067, Glutamate_racemase, glutamate racemase. This family consists of glutamate racemase, a protein required for making the UDP-N-acetylmuramoyl-pentapeptide used as a precursor in bacterial peptidoglycan biosynthesis. The most closely related proteins differing in function are aspartate racemases [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
IGVFDSGVGGLSVLKEIRKQLPKEHYIYVGDTKRFPYGEKSPEFILEYVLELLTFLKERHNIKLLVVACN
TASALALEDLQRNFDFPVVGVIEPAIKAAIRLTANGRVLVIATNATIKSNAYHEALKEIANDLLVEMLAC
PELVPLAEAGLLGEDYALECLKRYLRPLLDTLPDTVVLGCTHFPLLKEEIEQYLPEHVRLVDSGVHTARR
TAWLLEHKGPLAKSADAPDIEFCMSGTPIQFQELAKKWLGL
>gnl|CDD|272886 TIGR00068, Lactoylglutathione_lyase, lactoylglutathione lyase. Lactoylglutathione lyase is also known as aldoketomutase and glyoxalase I. Glyoxylase I is a homodimer in many species. In some eukaryotes, including yeasts and plants, the orthologous protein carries a tandem duplication, is twice as long, and hits this model twice [Central intermediary metabolism, Amino sugars, Energy metabolism, Other]
MAESGDLVADPKTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVI
ELTHNWGTEKYDLGNGFGHIAIGVDDVYKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQ
RKSTKDGLGN
>gnl|CDD|272887 TIGR00069, Histidinol_dehydrogenase, histidinol dehydrogenase. This model describes a polypeptide sequence catalyzing the final step in histidine biosynthesis, found sometimes as an independent protein and sometimes as a part of a multifunctional protein [Amino acid biosynthesis, Histidine family]
VKDIIEDVRARGDEALLEYTEKFDGVTLDSLRVSEEEIEAAYAAVDPELKEALELAAENIRAFHEAQLPR
SWEVETEPGVILGQRVRPIERVGLYVPGGRAPYPSTVLMTAIPAKVAGVKEIVVCTPPGKDGEINPAVLA
AAKLAGVDEVYKVGGAQAIAALAYGTETVPKVDKIVGPGNIYVTAAKKLVFGDVGIDMPAGPSEVLVIAD
ETANPEFVAADLLSQAEHDPDAQAILVTTSEELAEAVQEEIERQLATLPRREIARKSLEDNGAIILVDDL
EEAIEISNDYAPEHLELQTKNPEELLPKIRNAGSIFLGPYTPEAAGDYAAGPNHVLPTGGTARFYSGLSV
LDFLKRITVQRLSKEGLAELAPAVETLAEAEGLDAHANSVRIR
>gnl|CDD|272888 TIGR00070, hisG, ATP phosphoribosyltransferase. Members of this family from B. subtilis, Aquifex aeolicus, and Synechocystis PCC6803 (and related taxa) lack the C-terminal third of the sequence. The sole homolog from Archaeoglobus fulgidus lacks the N-terminal 50 residues (as reported) and is otherwise atypical of the rest of the family. This model excludes the C-terminal extension [Amino acid biosynthesis, Histidine family]
LRIALPKGRLLEDTLKLLEKAGLKLSREDGRKLIARDPDEGIEVLLLRPQDIPTYVEHGAADLGITGYDV
LLESGADVEELLDLGFGKCRLVLAVPQESDIDSLEDLKEGKRIATKYPNLARRYFEKKGIDVEIIKLNGS
VELAPLLGLADAIVDIVSTGTTLRENGLRIIEVILESSARLIA
>gnl|CDD|272889 TIGR00071, tRNA_pseudouridine_synthase_A, tRNA pseudouridine(38-40) synthase. Members of this family are the tRNA modification enzyme TruA, tRNA pseudouridine(38-40) synthase. In a few species (e.g. Bacillus anthracis), TruA is represented by two paralogs [Protein synthesis, tRNA and rRNA base modification]
RKIALKIAYDGSNYHGWQRQPNKRTVQGELEKALEAIGKKKITIMSAGRTDKGVHAMGQVISFDTPKEIP
DNKLNAKLNALLPPDIRVKALAPVNDNFHARFSASKRHYRYILYNHRHYYSPLDLEKMRAAAKQLLGKHD
FSNFSKAKSKSRSPIRTISDIKVSESGEYIIFDIIGNSFLWHMVRKIVGALVLVGRGKLPPEWVAKLLDA
KKRNLAPTTAPANGLYL
>gnl|CDD|272890 TIGR00072, hydrog_prot, hydrogenase maturation protease. HycI and HoxM are well-characterized as responsible for C-terminal protease activity on their respective hydrogenase large chains. A large number of homologous proteins appear responsible for the maturation of various forms of hydrogenase
LVLGIGNILRGDDGFGPRVAERLEERYEFPPGVEVLDGGTLGLELLDALEGADRVIVVDAVDSGAEPGTV
RRLDGEDLPAGLGGKLSTHQLGLAEALALLELLGALPPEIVLLGIQPESLEFGLGLSPEVAAAVPAAVEL
ILAEL
>gnl|CDD|272891 TIGR00073, nickel_incorporation_protein_HypB, hydrogenase accessory protein HypB. A GTP hydrolase for assembly of nickel metallocenter of hydrogenase. A similar protein, ureG, is an accessory protein for urease, which also uses nickel. hits scoring 75 and above are safe as orthologs [SS 1/05/04 I changed the role_ID and process GO from protein folding to to protein modification, since a protein folding role has not been established, but HypB is implicated in insertion of nickel into the large subunit of NiFe hydrogenases.] [Protein fate, Protein modification and repair]
DILSKNDRLAEKNRERLDKEGLVVLNFMSSPGSGKTTLIEKLIDNLDDEVKIAVIEGDVQTKFDADRLRK
YGVPAIQINTGKECHLDAHMVAHALKDLPLDEIDLLFIENVGNLVCPADFDLGEHMRVVLLSVTEGDDKV
LKYPTMFKEADLIVINKADLAEAVGFDVEKMKADAKKINPEAEIILMSLKTGKGLDEWLEFLEGKVKV
>gnl|CDD|129184 TIGR00074, Hydrogenase_expression/formation_protein, hydrogenase assembly chaperone HypC/HupF. See Medline:98153179 for function. This protein is suggested by act as a chaperone for a hydrogenase large subunit, holding the precursor form before metallocenter nickel incorporation [SS 12/31/03] More recently proposed additional function is to shuttle the iron atom that has been liganded at the HypC/HypD complex to the precursor of the large hydrogenase (HycE) subunit. . Added metallochaperone and protein mod GO terms [Protein fate, Protein folding and stabilization, Protein fate, Protein modification and repair]
MCIAIPGQVVEIDENIALVEFCGIKRDVSLDLVGEVKVGDYVLVHVGFAISVLDEEEARETLDALQELFD
AVEEGD
>gnl|CDD|272892 TIGR00075, Hydrogenase_isoenzymes_formation_protein_HypD, hydrogenase expression/formation protein HypD. HypD is involved in the hyp operon which is needed for the activity of the three hydrogenase isoenzymes in Escherichia coli. HypD is one of the genes needed for formation of these enzymes. This protein has been found in gram-negative and gram-positive bacteria and Archaea [Protein fate, Protein modification and repair]
MSNDHLRDEYRDARTVLALSEAIRELAFKLEKPLKIMEVCGGHTHTIMKYGLRDLLPENLELVHGPGCPV
CVTPMERIDEAIELATIPEIIFCTFGDMMRVPGSGGSLLQARAEGADVRIVYSPMDALKIAKENPDRKVV
FFAIGFETTAPTTASTLLSAKAEDINNFFFLSAHRLVPPAVEALLENPAVQIDAFLAPGHVSTIIGAKPY
APIAEKYKIPIVIAGFEPVDILQAIYMLLKQAISGEAKVENQYKRAVKPEGNVKAQKAIDEVFEREDREW
RGLGVIKRSGLGLREAFASFDAEEVFDIALQDKTPTPNKGCICGEILKGIAKPLDCPLFGTTCTPQNPIG
ACMVSSEGACAAYYRYRRQ
>gnl|CDD|272893 TIGR00077, Lipoprotein_signal_peptidase, lipoprotein signal peptidase. Alternate name: lipoprotein signal peptidase [Protein fate, Protein and peptide secretion and trafficking]
MSQSLSKGLLLYWLVAILFIGFDQLSKYLVLQNFDLGETYFVAFSGVFNITYVRNTGAAFSLLADQGGQV
YFLKGLAIAISLGLFVFLLRYKELFKITNIAFGLIFGGALGNFIDRLVRGGVVDFFDFYFGNYHFPIFNF
ADSSICIGVILLLLYFFFPKRKKKKD
>gnl|CDD|272894 TIGR00078, Probable_nicotinate-nucleotide_pyrophosphorylase, nicotinate-nucleotide pyrophosphorylase. Synonym: quinolinate phosphoribosyltransferase (decarboxylating) [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
LLDRWLREDLGSGDITTEALVPGSTRATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVKDGDRVEPGE
VVAEVEGPARSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGG
DNHRLGLSDAVMIKDNHIAAAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPE
EIKEAVQLLKGRVLLEASGGITLDNLEEYAETGVDVISSGALTHSVPALDFSLKI
>gnl|CDD|272895 TIGR00079, Peptide_deformylase, peptide deformylase. Peptide deformylase (EC 3.5.1.88), also called polypeptide deformylase, is a metalloenzyme that uses water to release formate from the N-terminal formyl-L-methionine of bacterial and chloroplast peptides. This enzyme should not be confused with formylmethionine deformylase (EC 3.5.1.31) which is active on free N-formyl methionine and has been reported from rat intestine [Protein fate, Protein modification and repair]
MLEVFHYPDDLLRKTAKPVEIVDKKIDQQLDDMIETMIAEKGIGLAAPQVGILKRMIVIELEDADKEPLL
FLINPKIIESSEESSYLEEGCLSVPVYYGLVPRKEKVKIRGDDRFGKPIILEADGLLAICIQHEIDHLNG
VFFVDYISPLNPKKLKKEMKE
>gnl|CDD|272896 TIGR00080, Protein-L-isoaspartate_O-methyltransferase, protein-L-isoaspartate(D-aspartate) O-methyltransferase. This is an all-kingdom (but not all species) full-length ortholog enzyme for repairing aging proteins. Among the prokaryotes, the gene name is pcm. Among eukaryotes, pimt [Protein fate, Protein modification and repair]
MDLESQKKALIDKLINEGYIKSKRVIDALLSVPREEFVPEHFKEYAYVDTPLEIGYGQTISAPHMVAMMT
ELLELKPGMKVLEIGTGSGYQAAVLAEIVGRDGLVVSIERIPELAEKAERRLRKLGLDNVIVIVGDGTQG
WEPLAPYDRIYVTAAGPKIPEALIDQLKEGGILVMPVGEYLQVLKRAEKRGGEIIIKDVEPVAFVPLVGG
EGFQG
>gnl|CDD|272897 TIGR00081, purC, phosphoribosylaminoimidazole-succinocarboxamide synthase. Alternate name: SAICAR synthetase purine de novo biosynthesis. E.coli example noted as homotrimer. Check length. Longer versions may be multifunctional enzymes [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
MQIKKRQKLYSGKAKDIYETDDPDLLRFVFRDDISAFDGEKKDQIPGKGRLNTKISAFIFEKLEEAGIPT
HYIDLIEDREMLVKKLDIIPLEVIVRNIAAGSLLKRLGIPEGLELEQPLVEFIFKPDEVGDPMLNESYAE
ALGLATEEELERIKELALKVNEVLKKYFDEKGIILVDFKLEFGLDEEGNLILADEVSPDTCRLWDKETYE
VGAPKLDKDIFRRTLGKLIEAYETVAR
>gnl|CDD|129191 TIGR00082, Ribosome-binding_factor_A, ribosome-binding factor A. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Essential for efficient processing of 16S rRNA. May interact with the 5'terminal helix region of 16S rRNA. Mutants lacking rbfA have a cold-sensitive phenotype [Transcription, RNA processing]
MASYRKERVESDIIREINRILIREIKDPRVGMLTVTKVEVSKDLQHAKVFVDCYGDEEAIDRVVKALNKA
KGFIRSLLGQAMRLRKTPELHFVKDNSLDKGMRIENLINSLKKE
>gnl|CDD|272898 TIGR00083, Putative_riboflavin_biosynthesis_protein_RibF, riboflavin kinase/FMN adenylyltransferase. multifunctional enzyme: riboflavin kinase (EC 2.7.1.26) (flavokinase) / FMN adenylyltransferase (EC 2.7.7.2) (FAD pyrophosphorylase) (FAD synthetase) [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]
SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPALTPLEDKARQLQIKGVEQ
LLVVVFDEEFANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFCQ
DIRISSSAIRQALKNGDLELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVV
LLNGEPYPGVGNIGNRPTFIGQQLVIEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDI
LQAKKWFN
>gnl|CDD|129193 TIGR00084, Holliday_junction_ATP-dependent_DNA_helicase_RuvA, Holliday junction DNA helicase, RuvA subunit. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions [DNA metabolism, DNA replication, recombination, and repair]
MIGFLFGKVIEVSKPKIIIEVNGVGYELQVPMTCAYELNLEQKAQVFTHLVVREDAELLFGFNTLEEREL
FKELIKVNGVGPKLALAILSNMSPEEFVYAIETEEVKALVKIPGVGKKTAERLLLELKGKLKGNKNLEMF
TPTEAARDELFEALVSLGYKPQEIQQALKKIKNKPDFAIEQDIEEALKQLL
>gnl|CDD|129194 TIGR00086, SsrA-binding_protein, SsrA-binding protein. This model describes the SsrA-binding protein, also called tmRNA binding protein, small protein B, and SmpB. The small, stable RNA SsrA (also called tmRNA or 10Sa RNA) recognizes stalled ribosomes such as occur during translation from message that lacks a stop codon. It becomes charged with Ala like a tRNA, then acts as mRNA to resume translation started with the defective mRNA. The short C-terminal peptide tag added by the SsrA system marks the abortively translated protein for degradation. SmpB binds SsrA after its aminoacylation but before the coupling of the Ala to the nascent polypeptide chain and is an essential part of the SsrA peptide tagging system. SmpB has been associated with the survival of bacterial pathogens in conditions of stress. It is universal in the first 100 sequenced bacterial genomes [Protein synthesis, Other]
LIASNKKAFFDYEILDTYEAGIVLKGSEVKSIRAGKVSLKDSYVIIKKGELWLKNMHIAPYKFGNYFNHD
PRRPRKLLLHKKEIDKLQGKVKEKGLTLVPLKLYFKNKGKVKVEIALAKGKKLHDKRESIKKRDAKRELK
RALK
>gnl|CDD|272899 TIGR00087, 5'-nucleotidase_SurE, 5'/3'-nucleotidase SurE. This protein family originally was named SurE because of its role in stationary phase survivalin Escherichia coli. In E. coli, surE is next to pcm, an L-isoaspartyl protein repair methyltransferase that is also required for stationary phase survival. Recent work () shows that viewing SurE as an acid phosphatase (3.1.3.2) is not accurate. Rather, SurE in E. coli, Thermotoga maritima, and Pyrobaculum aerophilum acts strictly on nucleoside 5'- and 3'-monophosphates. E. coli SurE is Recommended cutoffs are 15 for homology, 40 for probable orthology, and 200 for orthology with full-length homology [Cellular processes, Adaptations to atypical conditions]
MKILLTNDDGIFSPGIRALYQALKELGEVTVVAPAVQQSGTGHALTLFEPIRVGQVKVENGIHIYAVDGT
PTDCVILGIHELMPEVPDLVISGINAGENLGTDITYSGTVGAAMEAAIHGVPAIAISLQIFNFKENSSPL
DFEIAAKVTNAIVKNLLKNGLPGGDLLNVNVPLVPSIENTGIRITRLGRRMYQTSVEERTDPRGRSYYWI
GGDIKSPKARCDREPGTDVDAIRSGYISITPLKVDLT
>gnl|CDD|129196 TIGR00088, tRNA_guanine-N1--methyltransferase, tRNA (guanine-N1)-methyltransferase. This model is specfic for the tRNA modification enzyme tRNA (guanine-N1)-methyltransferase (trmD). This enzyme methylates guanosime-37 in a number of tRNAs.The enzyme's catalytic activity is as follows: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N1-methylguanine [Protein synthesis, tRNA and rRNA base modification]
MKIGVLTLFPEMFWPYLESSILGRAQKKNLVSFEVVNPRDFSKDKHKTVDDRPYGGGAGMVLKPEPIRDA
LHSVKAPAGTVILLSPQGRKFDQAGARELAQNEHLILICGRYEGFDERIIQLEVDEEISIGDFVLTGGEL
PALTLIDSVVRLIPGVLGKEASLIEESFANGLLDCPHYTRPYDLKGLKVPEVLLSGNHAKIEQWRLKQSL
LRTKLRRPDLLKKYLALTEEQNK
>gnl|CDD|272900 TIGR00089, Ribosomal_protein_S12_methylthiotransferase_RimO, radical SAM methylthiotransferase, MiaB/RimO family. This subfamily contains the tRNA-i(6)A37 modification enzyme, MiaB (TIGR01574). The phylogenetic tree indicates 4 distinct clades, one of which corresponds to MiaB. The other three clades are modelled by hypothetical equivalogs (TIGR01125, TIGR01579 and TIGR01578). Together, the four models hit every sequence hit by the subfamily model without any overlap between them. This subfamily is aparrently a part of a larger superfamily of enzymes utilizing both a 4Fe4S cluster and S-adenosyl methionine (SAM) to initiate radical reactions. MiaB acts on a particular isoprenylated Adenine base of certain tRNAs causing thiolation at an aromatic carbon, and probably also transferring a methyl grouyp from SAM to the thiol. The particular substrate of the three other clades is unknown but may be very closely related
KVYIETYGCQMNEADSEIMAGLLKEGGYEVTDDPEEADVIIINTCAVREKAEQKVRSRLGELAKLKKKNA
KIVVAGCLAQREGEELLKEIPEVDIVLGPQDKERIPEAIESAEEGKQVVFDISKEVYEELPRPRSFGKTR
AFLKIQEGCDKFCTYCIIPYARGRERSRPPEDILEEVKELVSKGVKEIVLLGQNVGAYGKDLEGKTNLAD
LLRELSKIDGIFRIRFGSSHPDDVTDDLIELIAENPKVCKHLHLPVQSGSDRILKRMNRKYTREEYLDIV
EKIRAKIPDAAITTDIIVGFPGETEEDFEETLDLVEEVKFDKLHSFIYSPRPGTPAADMKDQVPEEVKKE
RLERLIALQKEISLEKNKKYVGKTLEVLVEGKEGKKEGELTGRTENYKPVVFEGGVGKSLIGKFVKVKIT
EAAEYDLIG
>gnl|CDD|272901 TIGR00090, rsfS_iojap_ybeB, ribosome silencing factor RsfS/YbeB/iojap. This model describes a widely distributed family of bacterial proteins related to iojap from plants. It includes RsfS(YbeB) from E. coli. The gene iojap is a pattern-striping gene in maize, reflecting a chloroplast development defect in some cells. The conserved function of this protein is to silence ribosomes by binding the ribosomal large subunit and impairing joining with the small subunit in response to nutrient stress. Note that RsfS (starvation) is an author-endorsed change from the published symbol RsfA, which conflicted with previously published gene symbols [Protein synthesis, Translation factors]
LLELIVEALDDKKAEDIVVLDVRGKSSIADYFVIASGTSSRHVKAIADNVKEELKEAGLKPLGVEGLEEG
DWVLVDLGDVVVHIFTPEAREFYDLEKLW
>gnl|CDD|161703 TIGR00091, tRNA_guanine-N7--methyltransferase, tRNA (guanine-N(7)-)-methyltransferase. This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA [Protein synthesis, tRNA and rRNA base modification]
DYSLDKPDFATVFGNKAPLHLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPIVLAANNKANKLGLKNLHV
LCGDANELLDKFFPDGSLSKVFLNFPDPWPKKRHNKRRITQPHFLKEYANVLKKGGVIHFKTDNEPLFED
MLKVLSENDLFENTSKSTDLNNSPLSRPRNMTEYEQRFERLGHPVFDLCFERLP
>gnl|CDD|129200 TIGR00092, Ribosome-binding_ATPase_YchF, GTP-binding protein YchF. This predicted GTP-binding protein is found in a single copy in every complete bacterial genome, and is found in Eukaryotes. A more distantly related protein, separated from this model, is found in the archaea. It is known to bind GTP and double-stranded nucleic acid. It is suggested to belong to a nucleoprotein complex and act as a translation factor [Unknown function, General]
MGLSGGIVGLPNVGKSTLFAATTNLLGNEAANPPFTTIEPNAGVVNPSDPRLDLLAIYIKPEKVPPTTTE
FVDIAGLVGGASKGEGLGNQFLANIREVDIIQHVVRCFEDDIIHHVGNVDDPRDDFEIIDEELLKADEFL
VEKRIGRSKKSAEGGKDKKEELLLLEIILPLLNGGQMARHVDLSKEELILIKSLNLLTKKPIILIANVSE
DYLRNLNNNYLLIVEWIAAYSKGDPKVVFVCALEESELSELDDEERQEFLQKLGLTESAGLNIIIRARYK
LLLLSFFFTGGKEEVRAWTRKGGWAAPQAAGIIHTDFETGFIAAEVISWDDFIYKKSSQGAKKGGLMRLE
GKYYVVDDGDVLFFAFNV
>gnl|CDD|272902 TIGR00093, Ribosomal_large_subunit_pseudouridine_synthase_B, pseudouridine synthase. This model identifies panels of pseudouridine synthase enzymes that RNA modifications involved in maturing the protein translation apparatus. Counts per genome vary: two in Staphylococcus aureus, three in Pseudomonas putida, four in E. coli, etc [Protein synthesis, tRNA and rRNA base modification]
VGRLDRDSEGLLLLTNDGELVHRLTHPGHHHEKEYLVTVEGPVTDEDLEALRKGVQLEDGKTKPAKLKVI
TEPGFPTWLRVTLSEGRNRQVRRMFAAVGFPVLRLHRVRIGDVSLNGLPPGEWRPLTL
>gnl|CDD|272903 TIGR00094, tRNA_pseudouridine_synthase_D, tRNA pseudouridine synthase, TruD family. an EGAD loading error caused one member to be called surE, but that's an adjacent gene. MJ11364 is a strong partial match from 50 to 230 aa [Protein synthesis, tRNA and rRNA base modification]
EMLNEMPLNTLTNHPGTTGLIKASPRDFIVEEIPGYEFSGEGEFIHITVEKENWDTLEVLRVIAKFLGVS
RREIGFAGTKDKRAVTTQWVCLPVKLEEEPDASNFQLKGVKILSYNYHNRKIRLGDLKGNRFRIRIRDVE
LNSDELEETLNELCKKGFPNYFGSQRFGTFRIITHTVGRELLLSNWKGANHQYALKPLQGETKKSKEARR
IFWESDAKSALFNMPKAKRYERALLNSLLEGDNSYLAAIMSLPKNLRTMFVHAYQSYLFNIKSERIELMG
TAPLPGDGLIDELEREALRFEKKEVAPEGALDVKYKKALYARILSVEDFKALRVPKLKSHAKTLGSRRFS
WDFWEHVTSQKVVLKFYLPKGSYATSVLRELMKTKGS
>gnl|CDD|188022 TIGR00095, Putative_methylase_yhhF., 16S rRNA (guanine(966)-N(2))-methyltransferase RsmD. This model represents a family of uncharacterized bacterial proteins. Members are present in nearly every complete bacterial genome, always in a single copy. PSI-BLAST analysis shows homology to several families of SAM-dependent methyltransferases, including ribosomal RNA adenine dimethylases [Protein synthesis, tRNA and rRNA base modification]
KPNHSGSGKIRIIGGQYRGRKLKVPPGPSTRPTTDRVRESLFNILRPDIVGAHFLDLFAGSGALGLEALS
RGAASAVFVEQDRKVAQTLKENLSTLKKSGEQATVLNDAVRALLFLAKKQTPFDIIYLDPPFNRGLLEAL
LELLGENKWLNPKGLIVVEYDRENELPTVPETWSLLRQKVYGQSALRLYQ
>gnl|CDD|129204 TIGR00096, Ribosomal_RNA_small_subunit_methyltransferase_I, 16S rRNA (cytidine(1402)-2'-O)-methyltransferase. This protein, previously known as YraL, is RsmI, one of a pair of genes involved in a unique dimethyl modification of a cytidine in 16S rRNA. See pfam00590 (tetrapyrrole methylase), which demonstrates homology between this family and other members, including several methylases for the tetrapyrrole class of compound, as well as the enzyme diphthine synthase [Protein synthesis, tRNA and rRNA base modification]
LLYVVTTPIGNLEDITRRALELLACVDLFAEEDTRTSKLLLHLGIIATPKAFHIDNEFQEKQNLLAAKLE
IGNNIAVSSDAGPPLISDPGHLLVACREKANIIVVPLPGAAALTAALCASGPATDRFFFGGFLPKKSKRR
QALKAYIAEERTTVFFYESHHRLLTTLTDLNVFLGSERFVGAAELTKKESEYWFGTVGQLLPDITEDTNN
RKGGEVILIINGHKPQEECSDLQALALEILALLQAEVLLKKAAAYIAAEMTLKKNKLLYQFHLLEE
>gnl|CDD|272904 TIGR00097, HMP-P_kinase, hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase. This model represents a bifunctional enzyme, phosphomethylpyrimidine kinase (EC 2.7.4.7)/Hydroxymethylpyrimidine kinase (EC 2.7.1.49), the ThiD/J protein of thiamine biosynthesis. The protein is commonly observed within operons containing other thiamine biosynthesis genes. Numerous examples are fusion proteins with other thiamine-biosynthetic domains. Saccaromyces has three recent paralogs, two of which are isofunctional and score above the trusted cutoff. The third shows a longer branch length in a phylogenetic tree and scores below the trusted cutoff, as do putative second copies in a number of species [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDA
AKTGMLASAEIVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEA
LLGTKIRTEQDMIKAAKKLRELGPKAVLIKGGHLEGDQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLS
AAIAANLAKGLSLKEAVKEAKEFVTGAIRYGLNIGHGHGPLNHF
>gnl|CDD|272905 TIGR00099, Uncharacterized_protein_MCAP_0867, Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily. This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences [Unknown function, Enzymes of unknown specificity]
LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDD
QGEILYKKPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDD
ILKILLLFLDPEDLDLLIEALNKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAF
GDGMNDIEMLEAAGYGVAMGNADEELKALADYVTDSNNEDGVALAL
>gnl|CDD|272906 TIGR00100, Probable_hydrogenase_nickel_incorporation_protein, hydrogenase nickel insertion protein HypA. CXXC-~12X-CXXC and genetically seems a regulatory protein. In Hpylori, hypA mutant abolished hydrogenase activity and decrease in urease activity. Nickel supplementation in media restored urease activity and partial hydrogenase activity. HypA probably involved in inserting Ni in enzymes [Protein fate, Protein modification and repair]
MHELSLAEAMLEIVEEQAEKHQAKKVTRVTLEIGELSCVNPSQLQFAFEVVREGTVAEGAKLNIEDEPVE
CECEDCSEEVSPEIDLYRCPKCHGIMLQVRAGKELNLKSIEVEQE
>gnl|CDD|129208 TIGR00101, Urease_accessory_protein_UreG, urease accessory protein UreG. This model represents UreG, a GTP hydrolase that acts in the assembly of the nickel metallocenter of urease. It is found only in urease-positive species, although some urease-positive species (e.g. Bacillus subtilis) lack this protein. A similar protein, hypB, is an accessory protein for expression of hydrogenase, which also uses nickel [Central intermediary metabolism, Nitrogen metabolism]
MVKIGVAGPVGSGKTALIEALTRHMSKKYDMAVITNDIYTQEDAEFLCKNSVLPPERIIGVETGGCPHTA
IREDASMNLEAVEEMHGRFPNLELVFIESGGDNLSATFSPELADFTIFVIDVAEGDKIPRKGGPGITRSD
LLVINKIDLAPYVGADLKVMERDAKKMRGEKPFIFTNLRAKEGLDDVIAWIERYALLKD
>gnl|CDD|211546 TIGR00103, Uncharacterized_protein_MG134, DNA-binding protein, YbaB/EbfC family. The function of this protein is unknown, but it has been expressed and crystallized. Its gene nearly always occurs next to recR and/or dnaX. It is restricted to Bacteria and the plant Arabidopsis. The plant form contains an additional N-terminal region that may serve as a transit peptide and shows a close relationship to the cyanobacterial member, suggesting that it is a chloroplast protein. Members of this family are found in a single copy per bacterial genome, but are broadly distributed. A member is present even in the minimal gene complement of Mycoplasm genitalium [Unknown function, General]
SFGKNLGELMKQAQQMQEKMKKLQEEIAQFEVTGKSGAGLVKVTINGNLELKSIEIDPSLLEEDKEALED
MITEALNDAVKKVEETYKELMTSGMPLPPGL
>gnl|CDD|129210 TIGR00104, Probable_tRNA_adenine37-N6-methyltransferase, tRNA-Thr(GGU) m(6)t(6)A37 methyltransferase TsaA. This protein has been characterized by crystallography in complex with S-Adenosylmethionine, making it a probable S-adenosylmethionine-dependent methyltransferase. Analysis in EcoGene links this protein to the enzyme characterization mapped to the tsaA gene in Escherichia coli [Unknown function, Enzymes of unknown specificity]
MDLQLKPIGVIRSPYKEKFDAPRQGRFSDEVGEIEIFPEYADAVRGLEQFSHLIVLYWFDQAQRGKWQLT
VVPPRLGGNQRRGVFATRSPHRPNPIGLSVVELLEVECNILKVGGLDALDGTPVIDIKPYSEYIDSVPNA
QS
>gnl|CDD|272907 TIGR00105, 50S_ribosomal_protein_L31, ribosomal protein L31. This family consists exclusively of bacterial (and organellar) 50S ribosomal protein L31. In some species, such as Bacillus subtilis, this protein exists in two forms (RpmE and YtiA), one of which (RpmE) contains a pair of motifs, CXC and CXXC, for binding zinc [Protein synthesis, Ribosomal proteins: synthesis and modification]
MKKDIHPDYHEITVTCTCGNVFTTRSTWGKETLNLDICSKCHPFYTGKQKIVDTGGRVDKFNKKFGGL
>gnl|CDD|272908 TIGR00106, UPF0045_protein_MTH_1187, uncharacterized protein, MTH1187 family. This protein has been crystallized in both Methanobacterium thermoautotrophicum and yeast, but its function remains unknown. Both crystal structures showed sulfate ions bound at the interface of two dimers to form a tetramer [Unknown function, General]
VIAEVSIIPIGTVGASVSSYVAAAIEVLKESGLKYELHPMGTLIEGDLDELFEAIKAIHEAVLEKGSDRV
YTSIKIDTRTDKHRTLRDKVKAVEEKI
>gnl|CDD|188024 TIGR00107, Purine_nucleoside_phosphorylase_DeoD-type, purine-nucleoside phosphorylase, family 1 (deoD). Purine nucleoside phosphorylase (also called inosine phosphorylase) is a purine salvage enzyme. Purine nucleosides, such as guanosine, inosine, or xanthosine, plus orthophosphate, can be converted to their respective purine bases (guanine, hypoxanthine, or xanthine) plus ribose-1-phosphate. This family of purine nucleoside phosphorylase is restricted to the bacteria [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYV
YELIKFYEVKTIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKA
KGVDVHVGNVFSADAFYQPDKDVFDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEATT
AEERQTTFKDMIILALESVSQL
>gnl|CDD|272909 TIGR00109, Ferrochelatase_mitochondrial, ferrochelatase. Human ferrochelatase, found at the mitochondrial inner membrane inner surface, was shown in an active recombinant form to be a homodimer. This contrasts to an earlier finding by gel filtration that overexpressed E. coli ferrochelatase runs as a monomer [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
MKRKKTGVLLMNLGGPDKLEEVERFLKQLFADPRIIDISRAKWRKPLAKMILPLRSPKIAKNYEAIGGGS
PLLQITEQQAHALEKRLPNEIDFKVYIAMRYGEPFTEEAVKELLKDGVERAVVLPLYPHFSSSTTGSSFN
ELAEALKKLRSLRPTISVIESWYDNPKYIKALADSIKETLASFPEPDNAVLLFSAHGLPQSYVDEGDPYP
AECEATTRLIAEKLGFPNEYRLTWQSRVGPEPWLGPYTEELLEKLGEQGVQHIVVVPIGFTADHLETLYE
IDEEYREVAEDAGGDKYQRCPALNAKPEFIEAMATLVKKKLG
>gnl|CDD|272910 TIGR00110, Dihydroxy-acid_dehydratase, dihydroxy-acid dehydratase. This protein, dihydroxy-acid dehydratase, catalyzes the fourth step in valine and isoleucine biosynthesis. It contains a catalytically essential [4Fe-4S] cluster This model generates scores of up to 150 bits vs. 6-phosphogluconate dehydratase, a homologous enzyme [Amino acid biosynthesis, Pyruvate family]
ATGFTDEDFGKPFIGVANSYTTIVPGHMHLRDLAQAVKEGIEAAGGVAFEFNTIAVCDGIAMGHEGMKYS
LPSREIIADSVETMVNAHRFDGLVCIPSCDKITPGMLMAAARLNIPSIFVTGGPMLPGHTKLGKKIDLVS
AFEAVGEYAAGKISEEELEEIERSACPGCGSCSGMFTANTMACLTEALGLSLPGCSTMLATSAEKKRIAK
NSGKRIVELVKKNIKPRDILTKEAFENAITVDMALGGSTNTVLHLLAIANEAGVDLSLDDFDRLSRKVPH
IASLAPSGKYVMEDLHRAGGIPAVLKELDREGLLHGDTLTVTGKTLGEILEQAPVIPEGQDVIRPLDNPV
HQEGGLAILKGNLAPNGAVVKIAGVDEDMTKFEGPAKVFESEEEALEAILGGKIKEGDVVVIRYEGPKGG
PGMPEMLAPTSAIKGMGLGKSVALITDGRFSGGTRGLCIGHVSPEAAEGGPIALVEDGDIIIIDIPNRKL
DLQVSDEELAERRASWKAPEPRYVKGYLAKYAKLVSSADEGAVLD
>gnl|CDD|129217 TIGR00111, Protein_pelota_homolog, mRNA surveillance protein pelota. This model describes the Drosophila protein Pelota, the budding yeast protein DOM34 which it can replace, and a set of closely related archaeal proteins. Members contain a proposed RNA binding motif. The meiotic defect in pelota mutants may be a complex result of a protein translation defect, as suggested in yeast by ribosomal protein RPS30A being a multicopy suppressor and by an altered polyribosome profile in DOM34 mutants rescued by RPS30A. This family is homologous to a family of peptide chain release factors. Pelota is proposed to act in protein translation [Protein synthesis, Translation factors]
MSIVEESFNKGGAVIKLLPETLDDLWHLYQIIEKGDVEFAFTKRRTQDLDKIRSDKSKDTVKLGIEVESV
EFDMKTERLRYKGVIVTGPEDDVPVGSYHTLEIKYVYPLSIIKQNWKKWQLKRLREAVEISKRPKTAAVV
MEEGIAHVGLVRQYSVEEIQKIEYHMPGKKRTLKFGELRKEFYKEIAKKLLNFDDLKTIIVAGPGFYKND
FYDFIFERYPEEANKAVLENCSTGGRAGINEVLKRGLVARILQETRYAKEIMVIDEFLEHLAKDGDKAVY
GEDEVVKAAEYGAIEYLLVTDKVLVQREEIEKLLDSVESMGGKVVILSTEHELGKQLDSLGGIAGILRFP
I
>gnl|CDD|272911 TIGR00112, Pyrroline-5-carboxylate_reductase, pyrroline-5-carboxylate reductase. This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs [Amino acid biosynthesis, Glutamate family]
LLKAGALAPYDIYVINRSPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKD
KLLISIAAGVTLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVEL
PEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVT
SPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE
>gnl|CDD|272912 TIGR00113, queA, S-adenosylmethionine:tRNA ribosyltransferase-isomerase. This model describes the enzyme for S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA). QueA synthesizes Queuosine which is usually in the first position of the anticodon of tRNAs specific for asparagine, aspartate, histidine, and tyrosine [Protein synthesis, tRNA and rRNA base modification]
KVSSFDFELPESLIAQYPSEPRDSSRLLVLDKQTGKITHKTFVDVLDFFNEGDLLVLNNTKVIPARLFGR
KESGGKVEVLLLRMLDENRWLALIKPSKKPKIGAKVKFGEGYGEKIMAEMLAHNGRLFEFEFNDPNVLLD
VLESYGHMPLPPYIKRPDEKADEERYQTVYSKKPGAVAAPTAGLHFSEELLEKLKAKGVQYAFITLHVGA
GTFRPVEADNIEDHVMHAEYYEVPQETVEALNKTRENGGRIIAVGTTSVRSLESAAQEADGLIEPFFGDT
SIFIYPGYQFKVVDGLITNFHLPKSSLIMLVSALAGRENTMNAYKHAVEEKYRFFSYGDAMLIL
>gnl|CDD|211550 TIGR00114, 67-dimethyl-8-ribityllumazine_synthase, 6,7-dimethyl-8-ribityllumazine synthase. This enzyme catalyzes the cyclo-ligation of 3,4-dihydroxy-2-butanone-4-P and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione to form 6,7-dimethyl-8-ribityllumazine, the immediate precursor of riboflavin. Sometimes referred to as riboflavin synthase, beta subunit, this should not be confused with the alpha subunit which carries out the subsequent reaction. Archaeal members of this family are considered putative, although included in the seed and scoring above the trusted cutoff [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]
VRVGIVIARFNRFITDMLLKGAIDALKRLGAEVDNIDVIWVPGAFELPLAVKKLAESGKYDAVIALGTVI
RGGTPHFEYVADEAAKGIADLALDYGKPVIFGILTTETIEQAIERAGTKAGNKGVEAAVKALEMANLL
>gnl|CDD|272913 TIGR00115, tig, trigger factor. Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome [Protein fate, Protein folding and stabilization]
LKRKLTVEVPAEEVEEEVDKALKELAKTVKIPGFRKGKVPRSVVEKRYGESVLQEALNELLQEAFSEAVK
EEKIRPLGQPEIEVKELEDGKDLEFTAEFEVYPEVELGDYKGIEVEKPEVEVTDEDVDEELERLREQNAT
LVPVERGAAEKGDRVTIDFEGFIDGEAFEGGKAENFSLELGSGQFIPGFEEQLVGMKAGEEKEIKVTFPE
DYHAEELAGKEATFKVTVKEVKEKELPELDDEFAKSLGEEFETLEELKADIRKNLEEEKKERAKAKLKEQ
LLDKLVENNEFELPESLVEQEIDRLLEQAEQQLQQQGIDLEEYLKITEEELREEFREEAERRVKLGLILE
EIAKKEKIEVSEEEVEAEIEELAQQYGEDPEEVKKYYKKPGLLEQLRNDLLEEKVLDFLL
>gnl|CDD|272914 TIGR00116, Elongation_factor_Ts, translation elongation factor Ts. Translational elongation factor Ts (EF-Ts) catalyzes the exchange of GTP for the GDP of the EF-Tu.GDP complex as part of the cycle of translation elongation. This protein is found in Bacteria, mitochondria, and chloroplasts [Protein synthesis, Translation factors]
MMAITAQLVKELRERTGAGMMDCKKALVEANGDFEKAIKWLREKGIAKAAKKADRVAAEGVIVLKSDNHK
AVIVEVNSETDFVAKNEGFKEFANKLLDELKANPITTLEELQKQELENKEKVEYLASLAAKIGENIVLRR
VAVLEGQSNVIFSYLHANARIGVLVELKGKADEELAKHLAMHVAANKPQFIDQDDVSQEWVKKERQIITD
QAELSGKPKEILEKMVEGRMKKFLAEISLLGQKFVMDPSKTVGQFLKEKNAKVTEFVRFEVGEGIEKKAE
DFAEEVAAQMK
>gnl|CDD|129223 TIGR00117, Aconitate_hydratase_2, aconitate hydratase 2. Aconitate hydratase (aconitase) is an enzyme of the TCA cycle. This model describes aconitase 2, AcnB, which has weak similarity to aconitase 1. It is found almost exclusively in the Proteobacteria [Energy metabolism, TCA cycle]
MLEEYRKHVAERAAEGIPPLPLNANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAA
IAKGEAKCPLISPEKAIELLGTMQGGYNVHPLIDALDSQDANIAPIAAKALSHTLLVFDNFYDVEEKSKT
NEYAKQVMQSWADAEWFLNKPALAEKITVTVFKVTGETNTDDLSPAPDAWTRPDIPLHALAMLKNAREGI
EPQIEALKQKGFPVAYVGDVVGTGSSRKSATNSVLWHMGDDIPFVPNKRGGGLCLGGKIAPIFFNTMEDS
GALPIEVDVSNLNMGDVIDIYPYKGEITNHEGELLATFELKPETLLDEVRAGGRIPLIIGRGLTTKAREA
LGLPHSDVFRQPKAPAESDKGFTLAQKMVGRACGVKGIRPGTYCEPKMTTVGSQDTTGPMTRDELKELAC
LGFSADLVLQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVALRPGDGVIHSWLNRMLLPDTVGTGGDSHT
RFPLGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPLYAIKQGLLTVEKKGK
KNVFNGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDRRT
LERRIQGMEKWLANPELLEADADAEYAAVIEIDLAEIKEPILAAPNDPDDVRPLSEVQGDKIDEVFIGSC
MTNIGHFRAAGKILDAAGQLPTRLWVAPPTRMDEQQLTEEGYYSIFGAAGARTEIPGCSLCMGNQARVAD
GATVFSTSTRNFPNRMGTGANVYLGSAELAAVCALLGKIPTPEEYQTYVSEKDKTAVDKTYRYLNFNQLS
NFTE
>gnl|CDD|272915 TIGR00118, Probable_acetolactate_synthase_large_subunit, acetolactate synthase, large subunit, biosynthetic type. Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed [Amino acid biosynthesis, Pyruvate family]
MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLV
TSGPGATNLVTGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIK
EAFHIATTGRPGPVLVDLPKDVTTAEIEYPYPEKVNLPGYRPTVKGHPLQIKKAAELINLAKKPVILVGG
GVIIAGASEELKELAERIQIPVTTTLMGLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDD
RVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGDARNVLEELLKKLFELKERKESAWLEQINKWKK
EYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQFYPFRKPRRFITSGGLGTMGFGLPA
AIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQWQELFYEERYSHTHMG
SLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPMVAPGGGLDEMIGEK
>gnl|CDD|272916 TIGR00119, Probable_acetolactate_synthase_small_subunit, acetolactate synthase, small subunit. Acetolactate synthase is a heterodimeric thiamine pyrophosphate enzyme with large and small subunits. One of the three isozymes in E. coli K12 contains a frameshift in the large subunit gene and is not expressed. acetohydroxyacid synthase is a synonym [Amino acid biosynthesis, Pyruvate family]
RHILSVLVENEPGVLSRVAGLFTRRGFNIESLTVGPTEDPDLSRMTIVVVGDDKVLEQITKQLNKLVDVI
KVSDLTESAIVERELCLVKVSAPGEGRDEIIRLTNIFRGRIVDVSPDSYTVEVTGDSDKIDAFLELLRPF
GIKEVARTGKTALSRGP
>gnl|CDD|161718 TIGR00120, Includes:_Glutamate_N-acetyltransferase, glutamate N-acetyltransferase/amino-acid acetyltransferase. This enzyme can acetylate Glu to N-acetyl-Glu by deacetylating N-2-acetyl-ornithine into ornithine; the two halves of this reaction represent the first and fifth steps in the synthesis of Arg (or citrulline) from Glu by way of ornithine (EC 2.3.1.35). In Bacillus stearothermophilus, but not in Thermus thermophilus HB27, the enzyme is bifunctional and can also use acetyl-CoA to acetylate Glu (EC 2.3.1.1) [Amino acid biosynthesis, Glutamate family]
IPGGVTAPKGFLAAGIKEGKKKSYDLGLIISERPATAAAVFTTNKVRAAPVKVSEEVLKDGRSIRAIVVN
SGNANAFTGEQGMKDAREMARLVAELLGIEEESVLVASTGVIGRRLDMEKIRTGINKLYGELKNSSNSSD
NFAKAIMTTDTFPKEVAVEFELPGEKVRIGGVAKGAGMIAPNMATMLGFITTDAAIESKALQKMLRRATD
KSFNQITVDGDTSTNDTVLVLANGASRTKEITEDSPDFEVFEEALTAVCQELAKMIARDGEGATKFFEVQ
VKGAKNDEDAKIIARAIAGSSLVKTAVFGQDPNWGRIIAAAGYSGADVDPENVSVILGDNSEEVVLVDNG
VPLEFEETSRASEIMLESDEIEIVVDLGTGDGAGTAWGCDLSYDYVRINAEYTT
>gnl|CDD|272917 TIGR00121, Bifunctional_ligase/repressor_BirA, birA, biotin-[acetyl-CoA-carboxylase] ligase region. This model represents the biotin--acetyl-CoA-carboxylase ligase region of biotin--acetyl-CoA-carboxylase ligase. In Escherichia coli and some other species, this enzyme is part of a bifunction protein BirA that includes a small, N-terminal biotin operon repressor domain. Proteins identified by this model should not be called bifunctional unless they are also identified by birA_repr_reg (TIGR00122). The protein name suggests that this enzyme transfers biotin only to acetyl-CoA-carboxylase but it also transfers the biotin moiety to other proteins. The apparent orthologs among the eukaryotes are larger proteins that contain a single copy of this domain [Protein fate, Protein modification and repair]
EVIVLDVIDSTNQYALELAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPEGGLYFSLILRPDLPKSPAPGL
TLVAGIAIAEVLKELGDQVQVKWPNDILLKDKKLGGILTELTGKENRADYVVIGIGINVQNRKPAESLRE
QAISLSEEAGIDLDRGELIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIAR
GIDKDGALLLEDGGGIKKIISGEISLR
>gnl|CDD|272918 TIGR00122, Bifunctional_ligase/repressor_BirA, BirA biotin operon repressor domain. This model represents the amino-terminal helix-turn-helix repressor region of the biotin--acetyl-CoA-carboxylase ligase/biotin operon repressor bifunctional protein BirA. In many species, the biotin--acetyl-CoA-carboxylase ligase ortholog lacks this DNA-binding repressor region and therefore is not equivalent to the well-characterized BirA of E. coli. This model may recognize some other putative repressor proteins, such as DnrO of Streptomyces peucetius with scores below the noise cutoff but with significance shown by low E-value [Regulatory functions, DNA interactions]
MPLRLLALLADNPFSGEKLGEALGMSRTAVNKHIQTLREWGVDVLTVGKGYRLPPPIPLLNAKQIRGQL
>gnl|CDD|272919 TIGR00123, Cobalt_transport_protein_CbiM, cobalamin biosynthesis protein CbiM. A cutoff of 200 bits for trusted orthologs of cbiM is suggested. Scores lower than 200 but higher than 20 may be considered sufficient to call a protein cobalamin biosynthesis protein CbiM-related.The seed alignment for this model is a cluster of very closely related proteins from Methanobacterium thermoautotrophicum, Archaeoglobus fulgidus, Methanococcus jannaschii, and Salmonella typhimurium, each of which has greater than 50% identity to all the others. The ortholog from Salmonella is the source of the gene symbol cbiM for this set.In Methanobacterium thermoautotrophicum, Archaeoglobus fulgidus, and Methanococcus jannaschii, a second homolog of cbiM is also found. These cbiM-related proteins appear to represent a distinct but less well-conserved orthologous group. Still more distant homologs include sll0383 from Synechocystis sp. and HI1621 from Haemophilus influenzae; the latter protein, from a species that does not synthesize cobalamin, is the most divergent member of the group. The functions of and relationships among the set of proteins homologous to cbiM have not been determined [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
MHIMEGYLPPVWAAAWWVLSLPVLVYGLVRLKRIVEEKPEMKPLLAVSGAFIFVLSALKLPSVTGSCSHP
TGNGLAVVLFGPAVTAVLAAIVLLFQALLLAHGGLTTLGANGFSMGVIGPFVGWIVYKLACRAGLRRDVA
VFLAAMLGDLATYVVTSVQLALAFPIPHAGFTGSVVKFMGIFAYTQVPLAIAEGLLTVMIYDYITKLRPD
TLEK
>gnl|CDD|129230 TIGR00124, -lyase]_ligase [citrate (pro-3S)-lyase] ligase. ATP is cleaved to AMP and pyrophosphate during the reaction. The carboxyl end is homologous to a number of cytidyltransferases that also release pyrophosphate [Energy metabolism, Fermentation, Protein fate, Protein modification and repair]
FRRVWLENKLKACGIKNFLHQNELSLDAPLEIFIAVYEDEEIIGCGGIAGNVIKCVAIDESLRGEGLALQ
LMTELENLAYELGRFHLFIFTKPEYAALFEYCGFKTLAEAKDQGVLLENSATRLKRYCSTLPKPRTPGNK
IGSIVMNANPFTNGHRYLIEQAARQCDWLHLFVVKEDASLFSYDERFALVKQGIQDLSNVTVHNGSAYII
SRATFPAYFLKEQDVADDCYTEIDLKLFRYKIAPALGITHRFVGTEPLCPVTALYNQKMKYWLEEPNDAP
PIEVVEIQRKLAAGGPISASTVRELLAKGDWAAWAKLVPETTLHFLQNLLEE
>gnl|CDD|272920 TIGR00125, Phosphopantetheine_adenylyltransferase, cytidyltransferase-like domain. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate
RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV
>gnl|CDD|272921 TIGR00126, Deoxyribose-phosphate_aldolase, deoxyribose-phosphate aldolase. Deoxyribose-phosphate aldolase is involved in the catabolism of nucleotides and deoxyriibonucleotides. The catalytic process is as follows: 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. It is found in both gram-postive and gram-negative bacteria [Purines, pyrimidines, nucleosides, and nucleotides, Other, Energy metabolism, Other]
ELAKLIDHTALKADTTEEDIITLCAQAKTYKFAAVCVNPSYVPLAKELLKGTEVRICTVVGFPLGASTTD
VKLYETKEAIKYGADEVDMVINIGALKDGNEEVVYDDIRAVVEACAGVLLKVIIETGLLTDEEIRKACEI
CIDAGADFVKTSTGFGAGGATVEDVRLMRNTVGDTIGVKASGGVRTAEDAIAMIEAGASRIGASAGVAII
Q
>gnl|CDD|129233 TIGR00127, Isocitrate_dehydrogenase_cytoplasmic, isocitrate dehydrogenase, NADP-dependent, eukaryotic type. This model describes a eukaryotic, NADP-dependent form of isocitrate dehydrogenase. These eukaryotic enzymes differ considerably from a fairly tight cluster that includes all other related isocitrate dehydrogenases, 3-isopropylmalate dehydrogenases, and tartrate dehydrogenases. Several NAD- or NADP-dependent dehydrogenases, including 3-isopropylmalate dehydrogenase, tartrate dehydrogenase, and the multimeric forms of isocitrate dehydrogenase, share a nucleotide binding domain unrelated to that of lactate dehydrogenase and its homologs. These enzymes dehydrogenate their substates at a H-C-OH site adjacent to a H-C-COOH site; the latter carbon, now adjacent to a carbonyl group, readily decarboxylates. This model does not discriminate cytosolic, mitochondrial, and chloroplast proteins. However, the model starts very near the amino end of the cytosolic form; the finding of additional amino-terminal sequence may indicate a transit peptide [Energy metabolism, TCA cycle]
SKIKVANPVVEMDGDEMTRIIWELIKDKLILPYVELDLKYYDLGVEYRDATNDQVTVDAAEAIKKYNVGV
KCATITPDEARVEEFKLKKMWKSPNGTIRNILGGTVFREPIICKNIPRLVPGWEKPIIIGRHAFGDQYRA
TDFVVPGPGKLELVYKPKDGTQKVTLKVYDFEEGGGVAMAMYNTDESIEGFAHSSFQLALEKKWPLYLST
KNTILKKYDGRFKDIFQEVYEAQYKSKFEALGIWYEHRLIDDMVAQALKSEGGFIWACKNYDGDVQSDIV
AQGFGSLGLMTSVLICPDGKTFEAEAAHGTVTRHYRMYQKGQETSTNSIASIFAWSRGLAHRAKLDNNPE
LSKFANILESACINTVEAGIMTKDLALILGGSPVERSAYLNTEEFIDAVEERLKKKIAA
>gnl|CDD|272922 TIGR00128, Malonyl_CoA-acyl_carrier_protein_transacylase, malonyl CoA-acyl carrier protein transacylase. This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension [Fatty acid and phospholipid metabolism, Biosynthesis]
MKIAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQASEALGYDLKKLCQEGPAEELNKTQYTQPALYVVSA
ILYLKLKEQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAVPEGGGAMAAVIGLDEE
QLAQACEEATENDVDLANFNSPGQVVISGTKDGVEAAAALFKEMGAKRAVPLEVSGAFHSRFMKPAAEKF
AETLEACQFNDPTVPVISNVDAKPYTNGDRIKEKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLT
GLIKRIKNDL
>gnl|CDD|272923 TIGR00129, Protein_FdhD_homolog, formate dehydrogenase family accessory protein FdhD. FdhD in E. coli and NarQ in B. subtilis are required for the activity of formate dehydrogenase. The gene name in B. subtilis reflects the requirement of the neighboring gene narA for nitrate assimilation, for which NarQ is not required. In some species, the gene is associated not with a known formate dehydrogenase but with a related putative molybdopterin-binding oxidoreductase. A reasonable hypothesis is that this protein helps prepare a required cofactor for assembly into the holoenzyme [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]
VEDEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNINIEVQIDLSSR
RFMILKENRTGCSGCGRERLNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDLG
GLVSRMEDVGRHNAVDKLIGSALLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVA
EESNITLIGFARNGRFNIYTHPERLLE
>gnl|CDD|161726 TIGR00130, frhD, coenzyme F420-reducing hydrogenase delta subunit (putative coenzyme F420 hydrogenase processing subunit). FrhD is not part of the active FRH heterotrimer, but is probably a protease required for maturation. Alternative name: 8-hydroxy-5-deazaflavin (F420) reducing hydrogenase (FRH) subunit delta [Protein fate, Protein modification and repair]
LNHEILVVGCGNILFGDDGFGPAVIEYLKENGVEKPDNVCLIDAGTGAPHFVFTLIPQSKWKKIIVVDIA
DFGAEPGTLRVLNVDELPNGRYMDAHGWSLAYPLHDLEERIDIRVVGCQPKYVSQPDVDIGLTEEVNKAI
PRAVEIILKELGK
>gnl|CDD|272924 TIGR00131, Protein_GAL3, galactokinase. Galactokinase is a member of the GHMP kinases (Galactokinase, Homoserine kinase, Mevalonate kinase, Phosphomevalonate kinase) and shares with them an amino-terminal domain probably related to ATP binding.The galactokinases found by this model are divided into two sets. Prokaryotic forms are generally shorter. The eukaryotic forms are longer because of additional central regions and in some cases are known to be bifunctional, with regulatory activities that are independent of galactokinase activity [Energy metabolism, Sugars]
CESIQKIFASAFGAKPDFTARAPGRVNLIGEHTDYNDGSVLPCAIDFGTLCAVAVRDDKNVRIYLANADN
KFAERSLDLPLDGSEVSDWANYFKGVLHVAQERFNSFPLGADIVCSGNVPTGSGLSSSAAFECAVGAVLQ
NMGHLPLDSKQILLRIQVAENHFVGVNCGIMDQAASVLGKEDHALLVECRSLKATPFKFPQLGIAFVIAN
TNVKRTLAPSNYNTRRQECTTAANFLAATDKGALRDFMNEYFARYIARLTKMLPLVEERAKHVVSENLRV
LKAVKAMKDNDFKQFGALMNESHASCDDDYECTCPEIDELVCSAALVNGSGGSRMTGAGFGGCTVHLVPN
ENVDKVRQAVADKYPKKTGLELTFYVIVSKPGAGSC
>gnl|CDD|272925 TIGR00132, Glutamyl-tRNAGln_amidotransferase_subunit_A, aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, A subunit. In many species, Gln--tRNA ligase is missing. tRNA(Gln) is misacylated with Glu after which a heterotrimeric amidotransferase converts Glu to Gln. This model represents the amidase chain of that heterotrimer, encoded by the gatA gene. In the Archaea, Asn--tRNA ligase is also missing. This amidase subunit may also function in the conversion of Asp-tRNA(Asn) to Asn-tRNA(Asn), presumably with a different recognition unit to replace gatB. Both Methanococcus jannaschii and Methanobacterium thermoautotrophicum have both authentic gatB and a gatB-related gene, but only one gene like gatA. It has been shown that gatA can be expressed only when gatC is also expressed. In most species expressing the amidotransferase, the gatC ortholog is about 90 residues in length, but in Mycoplasma genitalium and Mycoplasma pneumoniae the gatC equivalent is as the C-terminal domain of a much longer protein. Not surprisingly, the Mycoplasmas also represent the most atypical lineage of gatA orthology. This orthology group is more narrowly defined here than in Proc Natl Acad Aci USA 94, 11819-11826 (1997). In particular, a Rhodococcus homolog found in association with nitrile hydratase genes and described as an enantiomer-selective amidase active on several 2-aryl propionamides, is excluded here. It is likely, however, that the amidase subunit GatA is not exclusively a part of the Glu-tRNA(Gln) amidotransferase heterotrimer and restricted to that function in all species [Protein synthesis, tRNA aminoacylation]
LRQLLKKKEISIKEVLEASLDRIEANKDKINAFLEVTVEKALKQAKKLDKAILTPLAGIPIAVKDNISTK
GIVTTCASKILENYIPPYDATVIERLKQAGALIIGKTNMDEFAMGSSTETSAFGPTKNPWNLDRVPGGSS
GGSAAAVAADLAPFSLGSDTGGSIRQPASFCGVVGFKPTYGRVSRYGLVAYASSLDQIGPFARTVEDIAL
LLDVISGHDKRDSTSAKVPDPEFFEELKKDLKGLKVGVVKEFSEEMDKEVQEKFENALEVLEELGAEIVE
VSFPHVKYALPIYYIISPSEASSNLARYDGIRYGYRIEEPNSLKELYAKTRAEGFGEEVKRRIMLGNYAL
SAGYYDKYYLKAQKVRTLIIDDFLKLFEEVDVIVSPTAPTLPFKIGEKLDDPLEMYLSDILTVPANLAGL
PAISVPCGVKEKGLPIGLQIIGKCFDDKTLLQVSYAFEQA
>gnl|CDD|272926 TIGR00133, gatB, aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit. The heterotrimer GatABC is responsible for transferring the NH2 group that converts Glu to Gln, or Asp to Asn after the Glu or Asp has been ligated to the tRNA for Gln or Asn, respectively. In Lactobacillus, GatABC is responsible only for tRNA(Gln). In the Archaea, GatABC is responsible only for tRNA(Asn), while GatDE is responsible for tRNA(Gln). In lineages that include Thermus, Chlamydia, or Acidithiobacillus, the GatABC complex catalyzes both [Protein synthesis, tRNA aminoacylation]
MIEYEAKIGLEIHVQLNTKTKLFCSCPNSFGSAPPNTNVCPVCLGLPGALPVLNEEAVKKAIKLALALNS
QINQPISVFDRKHYFYPDLPKGYQITQQDRPIAEGGKLEIELDGGEKRIGIERVHMEEDTGKSQHFGSDV
QSLVDFNRSGAPLIEIVTKPDINSPKEARAFLKKLRQILRYLGISDGNLEEGSMRCDVNVSIRLKGQEHL
GTRVEIKNINSFKGIEKAIKYEIERQVKALIRGEEVVQETRTFDEKSNITVSMRSKETSIDYRYFPEPDL
PPINIDELLVKEVAGKLPELPSAKRIRLKKEYGLSEQDAKVLTSDLTLADYFEEVVKLIGDPKLAANWIC
IELLGVLNKLQISLAECGLKPSDLAELIKLIKEGKISGKSAKQLIEEMLENGGDPSKLIEELGLEQISDE
KELIKIIEEVIKENPKEVEKYLSGKERALKFLVGQVMKRTRGRANPQLVNEILKEMLS
>gnl|CDD|213509 TIGR00134, Glutamyl-tRNAGln_amidotransferase_subunit_E, glutamyl-tRNA(Gln) amidotransferase, subunit E. This peptide is found only in the Archaea. It is paralogous to the gatB-encoded subunit of Glu-tRNA(Gln) amidotransferase. The GatABC system operates in many bacteria to convert Glu-tRNA(Gln) into Gln-tRNA(Gln). However, the homologous system in archaea instead converts Asp-tRNA(Asn) to Asn-tRNA(Asn). Glu-tRNA(Gln) is converted to Gln-tRNA(Gln) by a heterodimeric amidotransferase of GatE (this protein) and GatD. The Archaea have an Asp-tRNA(Asn) amidotransferase instead of an Asp--tRNA ligase, but the genes have not been identified. It is likely that this protein replaces gatB in Asp-tRNA(Asn) amidotransferase but that both enzymes share gatA [Protein synthesis, tRNA aminoacylation]
MDYEKVGLKVGLEIHQQLDTKSKLFCPCPTELRDSEPDHEIVRNLRPTQSELGEFDRAAFEEAMRKLHFI
YENYHDTTCLVEADEEPPHPLNPEALEIAVTVALLLNMRVVDEFHTMRKIVIDGSNTGGFQRTGLVATDG
HLETPQGTVGIENLCLEEDAARKIEDTGDGVVYRLDRLGIPLVEITTDPDISDPQMAKEVAYRIGQILRS
TGKVKRGLGTIRQDLNISIRDGARVEVKGVQDLDLIPKIVEREVKRQLNLLKIRDELQERGAVVEEKIFD
VTEVFADTKSKIISNAESVKAVLLRGFDGLVGVEIQPGRRLGTEFADYAKKRGVGGIFHTDELPAYGITE
EEVRGLRDAVGAEQGDAVVMVAHERVTVERALREVIERAKMALQGVPEETRKALEDGNTQYLRPLPGAAR
MYPETDIPPFRIEDELLEGIRRNLPELPEEKKERIMREYGLSEDLASQLVKSNYVDEFEALTEKFRVDPT
VIASLLAYTLRELRREGHDIDGLELRHLRDAIKLLEVGKIAKEGLREILKCMCDEPLAAEDAARKLKLKL
LAEEEIESIIQEIIEENLDMISERGEGAMGPLMGQAMGRLRGKADGKVVNRILRKKLKER
>gnl|CDD|129241 TIGR00135, Glutamyl-tRNAGln_amidotransferase_subunit_C, aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit. Archaea, organelles, and many bacteria charge Gln-tRNA by first misacylating it with Glu and then amidating Glu to Gln. This small protein is part of the amidotransferase heterotrimer and appears to be important to the stability of the amidase subunit encode by gatA, but its function may not be required in every organism that expresses gatA and gatB. The seed alignment for this model does not include any eukaryotic sequence and is not guaranteed to find eukaryotic examples, although it does find some. Saccharomyces cerevisiae, which expresses the amidotransferase for mitochondrial protein translation, seems to lack a gatC ortholog. This model has been revised to remove the candidate sequence from Methanococcus jannaschii, now part of a related model [Protein synthesis, tRNA aminoacylation]
ISDEEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPMTHPLEISNVLREDEPEEPLS
RDDILKNAPEKEDGFIKVPKIIE
>gnl|CDD|272927 TIGR00136, Mitochondrial_translation_optimization_protein, glucose-inhibited division protein A. GidA, the longer of two forms of GidA-related proteins, appears to be present in all complete eubacterial genomes so far, as well as Saccharomyces cerevisiae. A subset of these organisms have a closely related protein. GidA is absent in the Archaea. It appears to act with MnmE, in an alpha2/beta2 heterotetramer, in the 5-carboxymethylaminomethyl modification of uridine 34 in certain tRNAs. The shorter, related protein, previously called gid or gidA(S), is now called TrmFO (see model TIGR00137) [Protein synthesis, tRNA and rRNA base modification]
FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADK
TGLQFRVLNSSKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDNDEIKGVVTKDGNE
FRAKAVIITTGTFLRGKIHIGDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKL
EVQFGDTQPPAFSFTNKNFLPQQLPCYLTHTNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVR
FADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIRSIPGLENAEILRPGYAIEYDYFDPTQLKPT
LETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRNEAYIGVLIDDLVTKGTKEPY
RMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLSPSKEVKEELK
NLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN
VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK
>gnl|CDD|129243 TIGR00137, gid_trmFO, tRNA:m(5)U-54 methyltransferase. This model represents an orthologous set of proteins present in relatively few bacteria but very tightly conserved where it occurs. It is closely related to gidA (glucose-inhibited division protein A), which appears to be present in all complete eubacterial genomes so far and in Saccharomyces cerevisiae. It was designated gid but is now recognized as a tRNA:m(5)U-54 methyltransferase and is now designated trmFO [Protein synthesis, tRNA and rRNA base modification]
TPVHVIGGGLAGSEAAWQLAQAGVPVILYEMRPEKLTPAHHTEDLAELVCSNSLGAKALDRAAGLLKTEM
RQLSSLIITAADRHAVPAGGALAVDRGIFSRSLTEQVASHPNVTLIREEVTEIPEEGITVIATGPLTSPA
LSEDLKELTGMDYLYFYDAAAPIVEGDSIDKEKAFFASRYDKGEAAYLNCPFTEEEYFNFWEALCEAEQV
PLKDFEKAKFFEGCLPIEEMAQRGEKTMLFGPMKPVGLFDPRTGKKPYAVVQLRQEDKAGTLWNMVGFQT
NLRWGEQKRVFRLIPGLENAEFVRMGVMHRNTFINSPQLLTASLHFKDRQTLFFAGQLTGVEGYVASTAG
GWLAGINAARLALGEPLLTLPAETMMGALFNYISTASPKHFQPMNPNFGLLPELPQKIRNKKERYEQYAD
RALETLTTWQKSI
>gnl|CDD|272928 TIGR00138, Ribosomal_RNA_small_subunit_methyltransferase_G, 16S rRNA (guanine(527)-N(7))-methyltransferase RsmG. RsmG was previously called GidB (glucose-inhibited division protein B). It is present and a single copy in nearly all complete eubacterial genomes. It is missing only from some obligate intracellular species of various lineages (Chlamydiae, Ehrlichia, Wolbachia, Anaplasma, Buchnera, etc.). RsmG shows a methytransferase fold in its the crystal structure, and acts as a 7-methylguanosine (m(7)G) methyltransferase, apparently specific to 16S rRNA [Protein synthesis, tRNA and rRNA base modification]
LLAYLELLQKWNQRFNLTSIKTPEEIWQRHILDSLALLPYLDGKRVIDIGSGAGFPGIPLAIARPELKLT
LLESNHKKVAFLREVKAELGLNNVEIVNGRAEDYQHEEQFDIITSRALASLNVLLELTLNLLKVGGYFLA
YKGKKYLDEIEEAKEKIQVLGVEPLEVPPLTGPDRHLVVLK
>gnl|CDD|129245 TIGR00139, Homoaconitase_mitochondrial, homoaconitase. Homoaconitase is known only as a fungal enzyme from two species, where it is part of an unusual lysine biosynthesis pathway. Because this model is based on just two sequences from a narrow taxonomic range, it may not recognize distant orthologs, should any exist. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures, but 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble leuC and leuD over their lengths but are even closer to the respective domains of homoaconitase, and their identity is uncertain [Amino acid biosynthesis, Aspartate family]
GQNLTEKIVQKYAVGLPEGKFVHSGDYVSIKPAHCMSHDNSWPCALKFMGIGASKIHNPDQIVMTLDHDI
QNKSDKNLKKYKNIEEFAKKHGIDFYPAGRGIGHQIMIEEGFAFPGNLAVASDSHSNMYGGLGCLGTPIV
RTDAAAIWATGKTWWQIPPVAKVEFKGQLPPGVSGKDIIVALCGLFNKDDVLNHAIEFTGSEDSLNALPI
DHRLTIANMTTEWGALSGLFPIDKTLIDWLKGKATLAALGLADGPFINPAAERFTHPALEEKAEIPLKAD
KDAHYAKELFIDLASLSHYVSGPNSVKVANPLKDLEAQDIKIDKAYLVSCTNSRASDIAAAADVFCEAAD
KNGGKINKIAPGVEFYIAAASIEEEAAAEGNGAWEKLLEAGAIPLPAGCGPCIGLGAGLLEPGEVGISAS
NRNFKGRMGSKDAKAYLASPAVVAASALLGKISGPAEVLSPEGWTEIIFGEGDGIKEEDRMLTNEEALEK
IIGIIDDLVADEEKNAASEAPAQEESEQGLTEILEGFPEEFSGELVFCDADNINTDGIYPGKYTYQDDVP
KEKMAQVCMENYDAEFRTKAHEGDILVSGFNFGCGSSREQAATAILAKGINLVVSGSFGNIFSRNSINNA
LLGLEIPALIKKLREKFGGADKELTRRTGWFLKWDVADAKIEVQEGSLDGGPILEHKVGELGKNLQEIIA
KGGLEGWVKNAI
>gnl|CDD|129246 TIGR00140, Hydrogenase_expression/formation_protein_HupD, hydrogenase expression/formation protein. valid names: hupD, hynC, hoxM. C at 64 and 67 are believed to be metal binding. Postulated to be involved in processing or hydrogenase. Superfamily suggests that it is a peptidase/protease [Protein fate, Protein modification and repair]
VRLVEALQQRYAFPDNVTLLDGGTQGLYLLPLIESADRLIILDAVDYGLEPGTLYILRDEEVPKFLAKKM
SLHQTGFQEVLALAELLGHLPKELVLIGVQPEELEDYGGSLSPEVAEAIPPAIEIALAQLAEWG
>gnl|CDD|129247 TIGR00142, Putative_hydrogenase_maturation_protease_MJ0631, hydrogenase maturation protease HycI. Hydrogenase maturation protease is a protease that is involved in the C-terminal processing of HycE,the large subunit of hydrogenase 3 from E.Coli. This protein seems to be found in E.Coli and in Archaea [Protein fate, Protein modification and repair]
LVLLCVGNELMGDDGAGPYLAEKCAAAPKEENWVVINAGTVPENFTVAIRELRPTHILIVDATDMGLNPG
EVRIIDDDIIEMYSMSTHNMPLSYLVDYLKEDINGEIIFLGIQPDIVGFYYPMSQPVKDAVETLYQRLIG
WEGNGG
>gnl|CDD|272929 TIGR00143, Carbamoyltransferase_HypF [NiFe] hydrogenase maturation protein HypF. A previously described regulatory effect of HypF mutatation is attributable to loss of activity of a regulatory hydrogenase. A zinc finger-like region CXXCX(18)CXXCX(24)CXXCX(18)CXXC region further supported the regulatory hypothesis. However, more recent work (PUBMED:11375153) shows the direct effect is on the activity of expressed hydrogenases with nickel/iron centers, rather than on expression [Protein fate, Protein modification and repair]
TGDGVEIVLEADKEESFLNRLKKGLPPLARIEKIIIEPFDGAEHFTTFRIRESKNGGLSLLSIIPADVAT
CSDCLEEMLDKNDRRYLYPFISCTHCGPRFTIIEALPYDRENTSMADFPLCPDCAKEYKDPLDRRFHAQP
IACPRCGPQLNFVSRGGHAEQDDALLEAAKLLKKGKIIAIKGIGGFHLACDARNDEVVERLRLRKNRPLK
PFAVMSPDLESAEQHAELNNLECELLTSPAAPIVLLRKKPDIKLAPNIAPNLPTIGVMLPYTPLHHLLLQ
LLAFPLVMTSANLPGLPMAIDNAEILDKLQGIADGFLVHNRRIVNRVDDSVVQHVAGEILFLRRSRGFAP
QPLTLPPNGNPKKILALGAELKNTFSLLKGGQAYLSQHIGDLSVYETYKFFKEALNFFLRIYDFEPQDIV
CDLHPQYNTTQYAEELSLPVLRVQHHHAHALAVMADAGVLEEAVIGITWDGVGYGEDGKIWGGECLLIDL
GRIERLGRLEEFWLLGGDLATKYPLRILLSILLKHDLNDFLKRYQKYFKQEKELSVLQQALEKKINAPLT
TSTGRLFDAVAAALGLCGERTYEGEAAIALEALALRSDGIANYPFEIKNKVLDLKEFYQRFLEDLLVGED
RSKIAHIAHKFVASGLVEIATAIAVPFGIHKIVISGGVFYNRLLLERLAKYLKGLGFQFLFHRHLPPGDG
GISLGQAVAAA
>gnl|CDD|129249 TIGR00144, beta_RFAP_syn, beta-RFAP synthase. This protein family contains several archaeal examples of beta-ribofuranosylaminobenzene 5-prime-phosphate synthase (beta-RFAP synthase), an enzyme involved in methanopterin biosynthesis. In some species, two members of this family are found. It is unclear whether both act as beta-RFAP synthase. This family is related to the GHMP kinases (Galactokinase, Homoserine kinase, Mevalonate kinase, Phosphomevalonate kinase). Members are found so far only in the Archaea and in Methylobacterium extorquens [Unknown function, Enzymes of unknown specificity]
LIINTPSRIHLTLIDLNGSIGRVDGGVGLALEEPEIVIGLKESDDMGVEFTSHAEGKLGEEYRRSRIMEA
ARKTLKHIGSEGFHFTVRSMFPAHSGLGSGTQLSLAVGRLVSEYYGMKFTAREIAHIVGRGGTSGIGVAS
FEDGGFIVDGGHSSKEKSDFLPSSASSAKPAPVIARYDFPDWNIILAIPEIDSVSGRREVNIFQKYCPVP
LRDVERICHLILMKMMPAVVEGDLDAFGESVNEIQGLGFKKIERELQDPLIKRIIDSMISAPGAGMSSFG
PTVYAVTDEKPGNIAGAVADIFGPYGVYGRIIVTKARNRGAFII
>gnl|CDD|272930 TIGR00145, Uncharacterized_protein_slr0964, FTR1 family protein. A characterized member from yeast acts as oxidase-coupled high affinity iron transporter. Note that the apparent member from E. coli K12-MG1655 has a frameshift by homology with member sequences from other species [Unknown function, General]
MVSMVAVFLITLREGLEAALVVSVLLSYLKRAQRTRLRIWVWVGVLAGFAACLAIGIGVIGAYGSLQKDE
FKELLEGIFGVIAVVMLSYMGLWMLRMQRKWRVKIERQLVQALKRKRSGWAIALIAFIAVVREGLETVLF
LAGFQQGSHATAYIGPAVAGLIVAVVVGVLLYRGGSRLSLKIFFILSSSLLLFIAAGLLGGGNHRFNLAG
GGDGFGSYNFDKAVSCCNPELDWLLFNGLLGWIYYLSSSYSYNMYWLVLIIVLSLLLVEEALGHRPFGKL
QLK
>gnl|CDD|161732 TIGR00147, Putative_lipid_kinase_BmrU, lipid kinase, YegS/Rv2252/BmrU family. The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized [Unknown function, Enzymes of unknown specificity]
MAEAPAILNPTAGKSNDNKPLREVIMLLREEGMEIHVRVTWEKGDAARYVEEARKFGVDTVIAGGGDGTI
NEVVNALIQLDDIPALGILPLGTANDFARSLGIPEDLDKAAKLVIAGDARAIDMGQVNKQYCFINMAGGG
FGTEITTETPEKLKAALGSLSYILSGLMRMDTLQPFRCEIRGEGEHWQGEAVVFLVGNGRQAGGGQKLAP
DASINDGLLDLRIFTNDNLLPALVLTLMSDEGKHTDNPNIIYGKASRIDIQTPHKITFNLDGEPLGGTPF
HIEILPAHLRCRL
>gnl|CDD|129252 TIGR00148, Uncharacterized_protein, UbiD family decarboxylase. The member of this family in E. coli is UbiD, 3-octaprenyl-4-hydroxybenzoate carboxy-lyase. The family described by this model, however, is broad enough that it is likely to contain several different decarboxylases. Found in bacteria, archaea, and yeast, with two members in A. fulgidus. No homologs were detected besides those classified as orthologs. The member from H. pylori has a C-terminal extension of just over 100 residues that is shared in part by the Aquifex aeolicus homolog [Unknown function, General]
MRDFIQLLEKEGELLRITEEVDPDLEVAEIARRALRAGGPALLFKNPKGYGFPVLMNLFGSRERLALALG
VDGKRLAHLLEPDPPKFKEAFDFLARLKDKMEMPPKRTSVAPCKEKIISEDDVNLQELPILKCWPKDGGY
YITAGVVITQDPDTGKQNLGIYRMQVIDKDRLGIRWVPPRHGALHLRKAAERGEKLPVAIAIGVDPATLL
AASTPIPYGLSEYEFAGAIRGEKLRVVKCETNDLEVPADAEIVLEGTITAGETELEGPFGDHTGYYDIVR
PEPVITVKRMYHREDPIYHATYPGGPPHEDALMGVPTEPVFYPILRNQVPEIIDAVLPEGGCHWLLAVVS
IKKRYPGDAKNVIMAAWAALQFPYTKHVIVVDDDINIFDPNDVIWAIATRFDPDRDIVIVPGAPGDSLDP
ASPPSGLTGKMGIDATTK
>gnl|CDD|129253 TIGR00149, Hypothetical_UPF0047_protein_yjbQ., secondary thiamine-phosphate synthase enzyme. Members of this protein family have been studied extensively by crystallography. Members from several different species have been shown to have sufficient thiamin phosphate synthase activity (EC 2.5.1.3) to complement thiE mutants. However, it is presumed that this is a secondary activity, and the primary function of this enzyme remains unknown [Unknown function, Enzymes of unknown specificity]
QELLLKTTKRVELIDITSEIEAVLQSSGVKDGLLLVYVPHTTASLTINENADPDVLHDIERFFERLVPDD
GNYEHDEGDDNMDAHIKSSLLGTSQHVPVENGRLQLGTWQGIFFAEFDGPRTRRIIVKVQGE
>gnl|CDD|129254 TIGR00150, Hypothetical_UPF0079_protein_yjeE., tRNA threonylcarbamoyl adenosine modification protein YjeE. This protein family belongs to a four-gene system responsible for the threonylcarbamoyl adenosine (t6A) tRNA modification. Members of this family have a conserved nucleotide-binding motif GXXGXGKT and a nucleotide-binding fold. Member protein YjeE of Haemophilus influenzae (HI0065) was shown to have (weak) ATPase activity [Protein synthesis, tRNA and rRNA base modification]
ANPDEKAMDKFGKAFAKPLDFGTVVLLKGDLGAGKTTLVQGLLQGLGIQGNVTSPTFTLVNEYNEGNLMV
YHFDLYRLADPEELELMGLEDYFEGDGICLVEWPEEGLEILPDYDLQIKIDYVGDGREIELTA
>gnl|CDD|129255 TIGR00151, ispF, 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase. Members of this protein family are 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, the IspF protein of the deoxyxylulose (non-mevalonate) pathway of IPP biosynthesis. This protein occurs as an IspDF bifunctional fusion protein in about 20 percent of bacterial genomes [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
RIGQGFDVHRFGPGRPLILGGVEIPHEKGLLAHSDGDVLLHALTDALLGALGLGDIGKHFPDTDPRWKGA
DSRVLLRHAVALIKEKGYRIGNVDITIIAQRPKLLPHIPAMRENIAELLGIPLDSVNVKATTTEKLGFTG
RGEGIACQAVVLLVK
>gnl|CDD|272931 TIGR00152, Dephospho-CoA_kinase, dephospho-CoA kinase. This model produces scores in the range of 0-25 bits against adenylate, guanylate, uridine, and thymidylate kinases [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
LIALTGGIGSGKSTVLQYLADKYHFPVIDADKIAHQVVEPGQPAYHAIADHFGANILNQDGELDRKALGN
YVFNDPEELKWLNALTHPLIRQWMKKLIAQFQSKYALVLLDVPLLFENNLRSLVDYVIVVERSPELQLER
LMQRNDLTEEEVKKRLASQMDIEEKLARIDTVIDNSGPATLADLVKQLEE
>gnl|CDD|272932 TIGR00153, UPF0111_protein_MTH_1689, TIGR00153 family protein. An apparent homolog with a suggested function is Pit accessory protein from Sinorhizobium meliloti, which may be involved in phosphate (Pi) transport [Hypothetical proteins, Conserved]
FDRITMSVFGHERDNERQHIEKVGECVQLLIKSFELLKSGNNEKDEELRKEIIEIEHEADEIKREIRLNL
EKGAFLPNDRRDLLELAELLDEILDSLEHAAMLYELRKFEFPEELRDEFLLVLKITVDMIQHLHRVVEVI
ELETDLSLANDIIKEIKDLEDEIDVMQIRIYKKLYNLEVSNPWEGKILCKFIEKLGNISDYAEDAGDRIH
IIILHR
>gnl|CDD|188029 TIGR00154, 4-diphosphocytidyl-2-C-methyl-D-erythritol_kinase, 4-diphosphocytidyl-2C-methyl-D-erythritol kinase. Members of this family of GHMP kinases were previously designated as conserved hypothetical protein YchB or as isopentenyl monophosphate kinase. It is now known, in tomato and E. coli, to encode 4-diphosphocytidyl-2C-methyl-D-erythritol kinase, an enzyme of the deoxyxylulose phosphate pathway of terpenoid biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
MRHVFPAPAKINLFLYILGKRPDGYHELQMLMQFIDLGDKIIISVRSDDDIRLLKGDFDVPLEENLAYRA
AQLLKNFANSKIKSLDGVNIEITKNIPMAAGLGGGSSDAAAVLVGLNQLWNLGLSLEELAELGATLGADV
PFFVSGGTAFATGRGEIITPFEDPPEKWVVIAKPHVSVSTPVVYQAYKLPRNTPKRAKEWLKKISLECLQ
LLDSNGLNDLEKVALKRHTEVAQALNWLLEYGLAPERMSGSGPCVFALFDMESEAEQVLEQAPEWLNGFV
AKGYNVSPIGRAML
>gnl|CDD|272933 TIGR00155, Uncharacterized_protein_HI_1671, integral membrane protein, PqiA family. This family consists of uncharacterized predicted integral membrane proteins found, so far, only in the Proteobacteria. Of two members in E. coli, one is induced by paraquat and is designated PqiA, paraquat-inducible protein A [Unknown function, General]
MPKMCEHHPAAKHILCSQCDMLVALPRIESGQKAACPRCGTTLTVGWDWSLQRPAAYALAALFLMPFSNL
FPLLNMNLLGITIDATLLEGIWVMFSEGYASTGTMFFLCVQLVPAFCLITILLLWNRAELPVRLREVLLV
LFQLKTWVMADIYLVGVGVSFVKVMAYASIGVGSSLLPFCLFCVLTTRAFQCLNRRWLWDDFYPEMPELR
QPLKLRSCSACHTTILPAQEPVCPRCSTPLYVRRRNSLQWTWALLVASIMLLLPANLLPISVIYLLGSKM
EDTILSGVISLWSSGSYPVAAVVFLASIMVPTLKMIAMAWLLWDAHFKGQRDSERMHLLLEVVEFVGRWS
MLDLFVIALLMSLVRRGGIMSFTPGPGAFYFGAAVIMTMLSAMTFDSRLSWDR
>gnl|CDD|129260 TIGR00156, Uncharacterized_protein_HI_1709, TIGR00156 family protein. As of the last revision, this family consists only of two proteins from Escherichia coli and one from the related species Haemophilus influenzae [Hypothetical proteins, Conserved]
MKFQAIVLASALVMPYALADDQGGLSAPPPPHAIEGGFQGTDAKKMTVDFAKSMHDGASVTLRGNIISHI
GDDRYVFRDKSGEINVVIPAAVWNGREVQPKDMVNISGSLDKKSAPAEVDVTHIQK
>gnl|CDD|272934 TIGR00157, Putative_ribosome_biogenesis_GTPase_RsgA, ribosome small subunit-dependent GTPase A. Members of this protein were designated YjeQ and are now designated RsgA (ribosome small subunit-dependent GTPase A). The strongest motif in the alignment of these proteins is GXSGVGKS[ST], a classic P-loop for nucleotide binding. This protein has been shown to cleave GTP and remain bound to GDP. A role as a regulator of translation has been suggested. The Aquifex aeolicus ortholog is split into consecutive open reading frames. Consequently, this model was build in fragment mode (-f option) [Protein synthesis, Translation factors]
LVVGDRVVWEPGNPVKVYGGAIAERKNELTRPIVANIDQIVIVSSAVLPELSLNQLDRFLVVAEAQNIEP
IIVLNKIDLLDDEDMEKEQLDIYRNIGYQVLMTSSKNQDGLKELIEALQNRISVFAGQSGVGKSSLINAL
DPSVKQQVNDISSKLGLGKHTTTHVELFHFHGGLIADTPGFNEFGLWHLEPEQLTQGFVEFRDYLGLCKF
RDCLHQSEPGCAVRQAVEQGEISEWRYENYLKLIE
>gnl|CDD|129262 TIGR00158, 50S_ribosomal_protein_L9, ribosomal protein L9. Ribosomal protein L9 appears to be universal in, but restricted to, eubacteria and chloroplast [Protein synthesis, Ribosomal proteins: synthesis and modification]
MKVILLEDVANLGKRGDVVEVKDGYARNFLIPKGLAVPATKKNIEFFEARRKKLEEKLAANKAAAARLKE
VLELGTLTISKKVGDEGKLFGSITTKQIADALKAAGLDLDKKKIELPDGVIRTTGEHEVTIKLHEEVFAV
LKVIVVPE
>gnl|CDD|129263 TIGR00159, Uncharacterized_protein_MG105_homolog, TIGR00159 family protein. These proteins have no detectable global or local homology to any protein of known function. Members are restricted to the bacteria and found broadly in lineages other than the Proteobacteria [Hypothetical proteins, Conserved]
LVIIVVGIISLYLLLLTLSWLLNYIANILPIAIFIIFNKELRRFLEQLGRFTLLFRLSKKKEEQKKFIDE
ITKAVKRLSENKIGALIAIEKQDSLESYINIGYRIDSKFSSELLITIFYPETPLHDGAVIIRDNKIVAAG
SYLPLSEQSISKSLGTRHRAALGISEKSDALTIIVSEETGSISVAINGVLKRLLSNSDLKEDLEIEYLEN
T
>gnl|CDD|272935 TIGR00160, Methylglyoxal_synthase, methylglyoxal synthase. Methylglyoxal synthase (MGS) generates methylglyoxal (MG), a toxic metabolite (that may also be a regulatory metabolite and) that is detoxified, prinicipally, through a pathway involving glutathione and glyoxylase I. Totemeyer et al. propose that, during a loss of control over carbon flux, with accumulation of phosphorylated sugars and depletion of phosphate, as might happen during a rapid shift to a richer medium, MGS aids the cell by converting some dihydroxyacetone phosphate (DHAP) to MG and phosphate. This is therefore an alternative to triosephosphate isomerase and the remainder of the glycolytic pathway for the disposal of DHAP during the stress of a sudden increase in available sugars [Energy metabolism, Other]
MRKHIALIAHDKKKQDLVNFVQQHKPLLSQHDLYATGTTGNLISRATGLNINAMLSGPMGGDQQIGALIA
EGKIDAVIFFWDPLNAQPHEPDVKALLRLCTVWNIPLATNVATADFLIKSPHFNDAVDILIPDYQGYLAD
RLK
>gnl|CDD|129265 TIGR00161, Uncharacterized_protein_MJ0106, TIGR00161 family protein. This model represents one out of two closely related ortholgous sets of proteins that, so far, are found only in the Archaea. This ortholog set includes MJ0106 from Methanococcus jannaschii and AF1251 from Archaeoglobus fulgidus, but not MJ1210 or AF0525 [Hypothetical proteins, Conserved]
IKTETECTIYKEDVENPIVIEGFPGVGLVGNIAGWLLIEDLKLREIGYIDSKYFPPLAVLYKGVAIPPVR
IYEGKDGIVLFLSDFIIPPAVVYDMTNAIVEWMVRNNSRELISFNGMVVREKSQPVFGAANSQELIERLK
DLIEIFPFGNLNGISGTLLTRCAVNDIPAICLLAETLGPYPDPRAAASLVEVLNKMLNTNVDPEPLLKEA
EAIESRLKKLAEQVQGMMSKEAETPMYM
>gnl|CDD|129266 TIGR00162, Uncharacterized_protein_MJ1210, TIGR00162 family protein. This model represents one out of two closely related ortholgous sets of proteins that, so far, are found only in but are universal among the Archaea. This ortholog set includes MJ1210 from Methanococcus jannaschii and AF0525 from Archaeoglobus fulgidus while excluding MJ0106 and AF1251 [Hypothetical proteins, Conserved]
MKNEFYAWRSDGNGTDLIILVGNTQSLSPEGQYELVNAIIDVAKKYGARMIYTLGGYGVGKLVEEPYVYG
AATSPELVEELKEHGVKFREPGGGIIGASGLLLGVSELEGIPGACLMGETPGYMIDPKAAKAVLEVLCKM
LSLEVSVEALEERAKEMEKIIAKIKEMEEEMVQQWKAKPSEEDLRYIG
>gnl|CDD|272936 TIGR00163, Phosphatidylserine_decarboxylase_proenzyme, phosphatidylserine decarboxylase precursor. Phosphatidylserine decarboxylase is synthesized as a single chain precursor. Generation of the pyruvoyl active site from a Ser is coupled to cleavage of a Gly-Ser bond between the larger (beta) and smaller (alpha chains). It is an integral membrane protein. A closely related family, possibly also active as phosphatidylserine decarboxylase, falls under model TIGR00164 [Fatty acid and phospholipid metabolism, Biosynthesis]
LDEAEKPDLADYRSLNEFFIRPLKLERRPVDKEPNALVSPADGVISEVGIINPNQILQVKGMDYSLEELL
GEKNPLSPYFRNGGFFVVTYLSPRDYHRFHSPCDCRLRKMRYFPGDLFSVNPLGLQNVPNLFVRNERVIL
VFDTEFGNMLMIPVGATNVGSIRTNFDGNIQTNPRHEFTQTWTYNALGPVKLLKGEEMGYFELGSTVILL
FEADAFQLSAHLAVGQEVKIGELLAYEE
>gnl|CDD|129268 TIGR00164, Phosphatidylserine_decarboxylase_proenzyme, phosphatidylserine decarboxylase precursor-related protein. Phosphatidylserine decarboxylase is synthesized as a single chain precursor. Generation of the pyruvoyl active site from a Ser is coupled to cleavage of a Gly-Ser bond between the larger (beta) and smaller (alpha chains). It is an integral membrane protein. This protein has many regions of homology to known phosphatidylserine decarboxylases, including the Gly-Ser motif for chain cleavage and active site generation, but has a shorter amino end and a number of deletions along the length of the alignment to the phosphatidylserine decarboxylases. It is unclear whether this protein is a form of phosphatidylserine decarboxylase or is a related enzyme. It is found in Neisseria gonorrhoeae, Mycobacterium tuberculosis, and several archaeal species, all of which lack known phosphatidylserine decarboxylase [Unknown function, General]
VSMYHGWISILFWVFTLFTLQFFRDPDREIPQGPEAVLSPADGRIDVVERARRPFPDGDGLKISIFMSPF
DVHVNRAPAGGKVTYVKHIDGSFVPAFLRKASTENERNAVLIKTASGEVGVVQIAGFVARRIVCYVKEGE
KVSRGQRIGMIRFGSRVDLYLPENAQAQVKVGEKVTAGETVLARLPLTD
>gnl|CDD|272937 TIGR00165, 30S_ribosomal_protein_S18, ribosomal protein S18. This ribosomal small subunit protein is found in all eubacteria so far, as well as in chloroplasts. YER050C from Saccharomyces cerevisiae and a related protein from Caenorhabditis elegans appear to be homologous and may represent mitochondrial forms. The trusted cutoff is set high enough that these two candidate S18 proteins are not categorized automatically [Protein synthesis, Ribosomal proteins: synthesis and modification]
YFRRKKYCRFTAEGIQFIDYKDLDLLKKFISERGKILPRRITGTSAKYQRRLAVAIKRARYLALLPYVKD
>gnl|CDD|129270 TIGR00166, 30S_ribosomal_protein_S6, ribosomal protein S6. The ribosomal protein S6 ortholog family, including yeast MRP17, shows more than two-fold length variation from 95 residues in Bacillus subtilis to 215 in Mycoplasma pneumoniae. This length variation comes primarily from poorly conserved C-terminal extensions that are particularly long in the Mycoplasmas. MRP17 protein is a component of the small ribosomal subunit in mitochondria, and is shown here to be an ortholog of S6 [Protein synthesis, Ribosomal proteins: synthesis and modification]
RHYEIIFLVRPTLSEEVKGQIERYKKVITLNGAEIVRSEDWGKRRLAYPIKKQLRAHYVLMNFSGEAQVI
KEFERTARINDNVIRSLIIKLEH
>gnl|CDD|272938 TIGR00167, Fructose-bisphosphate_aldolase, ketose-bisphosphate aldolase. This model is under revision. Proteins found by this model include fructose-bisphosphate and tagatose-bisphosphate aldolase [Energy metabolism, Glycolysis/gluconeogenesis]
MMLVDVKELLQDAKEEGYAIPAFNINNLETINAVLEAAAEEKSPVIIQFSNGAAKYIAGLGAISAMVKAM
SEAYPYGVPVALHLDHGASEEDCAQAVKAGFSSVMIDGSHEPFEENIELTKKVVERAHKMGVSVEAELGT
LGGEEDGVSVADESALYTDPEEAKEFVKLTGVDSLAAAIGNVHGVYKGEPKGLDFERLEEIQKYVNLPLV
LHGGSGIPDEEIKKAISLGVVKVNIDTELQIAFAAAVRNYYAENKDYYDPRVWLRPGEKAMKEVVLEKIK
LFGSANKA
>gnl|CDD|129272 TIGR00168, Translation_initiation_factor_IF-3, translation initiation factor IF-3. infC uses abnormal initiation codons such as AUA, AUC, and CUG which render its expression particularly sensitive to excess of its gene product IF-3 thereby regulating its own expression [Protein synthesis, Translation factors]
INERIRFNEVRLIDENGEQLGIVSREEALEIAEEAGLDLVLISPNAKPPVCKIMDYGKYKYEQEKKKKEA
KKNQKIIQVKEVKMRPTIDEHDLQFKLKQAIRFLEKGDKVKFTVRFRGRESTHIELGEKVLDRFYTDVAD
VAEVEKPPTKSEGRMMSMLLAPKKK
>gnl|CDD|272939 TIGR00169, 3-isopropylmalate_dehydrogenase, 3-isopropylmalate dehydrogenase. Several NAD- or NADP-dependent dehydrogenases, including 3-isopropylmalate dehydrogenase, tartrate dehydrogenase, and the dimeric forms of isocitrate dehydrogenase, share a nucleotide binding domain unrelated to that of lactate dehydrogenase and its homologs. These enzymes dehydrogenate their substates at a H-C-OH site adjacent to a H-C-COOH site; the latter carbon, now adjacent to a carbonyl group, readily decarboxylates.Among these decarboxylating dehydrogenases of hydroxyacids, overall sequence homology indicates evolutionary history rather than actual substrate or cofactor specifity, which may be toggled experimentally by replacement of just a few amino acids. 3-isopropylmalate dehydrogenase is an NAD-dependent enzyme and should have a sequence resembling HGSAPDI around residue 340. The subtrate binding loop should include a sequence resembling E[KQR]X(0,1)LLXXR around residue 115. Other contacts of importance are known from crystallography but not detailed here.This model will not find all isopropylmalate dehydrogenases; the enzyme from Sulfolobus sp. strain 7 is more similar to mitochondrial NAD-dependent isocitrate dehydrogenases than to other known isopropylmalate dehydrogenases and was omitted to improve the specificity of the model. It scores below the cutoff and below some enzymes known not to be isopropylmalate dehydrogenase [Amino acid biosynthesis, Pyruvate family]
KIAVLPGDGIGPEVMAQALKVLKAVAERFGLKFEFEEHLIGGAAIDATGQPLPEETLKGCKEADAVLLGA
VGGPKWDNLPRDQRPEQGLLKLRKSLDLFANLRPAKVFPGLEDLSPLKEEIAKGVDFVVVRELTGGIYFG
EPKGREGEGEAWDTEVYTVPEIERIARVAFEMARKRRKKVTSVDKANVLESSRLWRKTVEEIAKEYPDVE
LEHQYIDNAAMQLVKSPTQFDVVVTSNLFGDILSDEASVITGSLGMLPSASLGSDGFGLFEPVHGSAPDI
AGKGIANPIAQILSAAMLLRYSFNLEEAADAIEAAVKKVLAEGYRTPDLGSSATTAVGTAEMGEEL
>gnl|CDD|272940 TIGR00170, 3-isopropylmalate_dehydratase_large_subunit, 3-isopropylmalate dehydratase, large subunit. Members of this family are 3-isopropylmalate dehydratase, large subunit, or the large subunit domain of single-chain forms. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are now described by a separate model of subfamily (rather than equivalog) homology type, and the priors and cutoffs for this model have been changed to focus this equivalog family more narrowly [Amino acid biosynthesis, Pyruvate family]
MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNR
DFNIKDEVAKIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGAL
AFGIGTSEVEHVLATQTLKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRD
LSMEGRMTVCNMAIEAGARAGLIAPDETTFEYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLE
ANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAERALAYMGLEPGTPLKDIKVDKVFIGSCTNS
RIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGFEWREPGCSMCLGMNNDRLPE
GERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF
>gnl|CDD|129275 TIGR00171, 3-isopropylmalate_dehydratase_small_subunit, 3-isopropylmalate dehydratase, small subunit. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The candidate archaeal leuD proteins are not included in the seed alignment for this model and score below the trusted cutoff [Amino acid biosynthesis, Pyruvate family]
MAPFKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFDWRFLDANGKEPNPDFVLNQPQYQGA
SILLARENFGCGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQVENQGL
QMTVDLENQLIHDSEGKVYSFEIDPFRKHCLINGLDEIGLTLQHEDEI
>gnl|CDD|129276 TIGR00172, Maf-like_protein_HP_1240, MAF protein. This nonessential gene causes inhibition of septation when overexpressed. A member of the family is found in the Archaeon Pyrococcus horikoshii and another in the round worm Caenorhabditis elegans [Cellular processes, Cell division]
MTKELILASQSPRRKELLEELGISFEQIVSEFDEKSLKTTSPRELVYRLAKEKAQAVAELLADALIIGAD
TVVILDGEIYGKPKDKEEAAEFLRKLSGQEHEVYTAVALIDSVHLLTFLDVTKVHFRALDPEEIEKYVES
GEPLEKAGAFGIEGFGAPLIKKIDGDYSNVVGLPLEKLLGALR
>gnl|CDD|272941 TIGR00173, menD, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase. MenD was thought until recently to act as SHCHC synthase, but has recently been shown to act instead as SEPHCHC synthase. Conversion of SEPHCHC into SHCHC and pyruvate may occur spontaneously but is catalyzed efficiently, at least in some organisms, by MenH (see TIGR03695). 2-oxoglutarate decarboxylase/SHCHC synthase (menD) is a thiamine pyrophosphate enzyme involved in menaquinone biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
WASVLVEELVRLGVRHVVISPGSRSTPLALALAEHPRLRVHVHIDERSAGFFALGLAKASGRPVAVVCTS
GTAVANLLPAVIEAYYSGVPLIVLTADRPPELRGCGANQTIDQPGLFGSYVRWSVDLPLPEADEPLAYLR
STVDRALAQAQGAPPGPVHINVPFREPLYPDPLLQPLQPWLRSGVPTISTGPPVLDPESLQELWDRLRQA
KRGLIIAGPLAGAEDAEALAALAEALGWPLLADPLSGLRGGPHPLVIDHYDLLLANAELREELQPDLVIR
FGGPPVSKRLRQWLARAPAEYWVVDPRPGWLDPFHHATTRLEASPAAFAEALAGLLKNPAAAWLDRWLEA
EAKARAALREVLAEEPLSELSLARALSQLLPDGSALFVGNSMPIRDLDTFSSPPDKPIRVFANRGASGID
GTLSTALGIAAA
>gnl|CDD|213512 TIGR00174, tRNA_dimethylallyltransferase, tRNA dimethylallyltransferase. Alternate names include delta(2)-isopentenylpyrophosphate transferase, IPP transferase, 2-methylthio-N6-isopentyladenosine tRNA modification enzyme. Catalyzes the first step in the modification of an adenosine near the anticodon to 2-methylthio-N6-isopentyladenosine. Understanding of substrate specificity has changed [Protein synthesis, tRNA and rRNA base modification]
VIFLMGPTASGKSQLSIQLAQKLNAEIISVDSMQIYKGMDIGTAKPSLQEREGIPHHLIDILDPSESYSA
ADFQTQALNAIADITARGKIPLLVGGTGLYLKALLEGLSPTPSADKLIREQLEILAEEQGWDFLYNELKK
VDPVAAAKIHPNDTRRVQRALEVFYATGKPPSELFKEQKIELFYDIVQIGLASSREPLHQRIEQRVHDML
ESGLLAEVKALYAQYDLCDLPSIQAIGYKEFLLYLEGTVSLEDAIERIKCNTRQYAKRQLTWFRKWSDVL
WLDSTDP
>gnl|CDD|272942 TIGR00175, Isocitrate_dehydrogenase_subunit_1_mitochondrial, isocitrate dehydrogenase, NAD-dependent, mitochondrial type. Several NAD- or NADP-dependent dehydrogenases, including 3-isopropylmalate dehydrogenase, tartrate dehydrogenase, and the multimeric forms of isocitrate dehydrogenase, share a nucleotide binding domain unrelated to that of lactate dehydrogenase and its homologs. These enzymes dehydrogenate their substates at a H-C-OH site adjacent to a H-C-COOH site; the latter carbon, now adjacent to a carbonyl group, readily decarboxylates. Mitochondrial NAD-dependent isocitrate dehydrogenases (IDH) resemble prokaryotic NADP-dependent IDH and 3-isopropylmalate dehydrogenase (an NAD-dependent enzyme) more closely than they resemble eukaryotic NADP-dependent IDH. The mitochondrial NAD-dependent isocitrate dehydrogenase is believed to be an alpha(2)-beta-gamma heterotetramer. All subunits are homologous and found by this model. The NADP-dependent IDH of Thermus aquaticus thermophilus strain HB8 resembles these NAD-dependent IDH, except for the residues involved in cofactor specificity, much more closely than it resembles other prokaryotic NADP-dependent IDH, including that of Thermus aquaticus strain YT1 [Energy metabolism, TCA cycle]
GGKYTVTLIPGDGIGPEISGSVKKIFRAANVPIEFEEIDVSPQTDGKTEIPDEAVESIKRNKVALKGPLE
TPIGKGGHRSLNVALRKELDLYANVVHCKSLPGFKTRHEDVDIVIIRENTEGEYSGLEHESVPGVVESLK
VITRDKSERIARYAFEYARKNGRKKVTAVHKANIMKLADGLFLNVCREVAKEYPDITFESMIVDNTCMQL
VSRPSQFDVMVMPNLYGNILSNLGAGLVGGPGLVPGANIGRDYAVFEPGVRHTGPDIAGQNIANPTALIL
SSVMMLNHLGLKEHADRIQKAVLSTIAEGKNRTKDLGGTATTSDFTEAVIKRL
>gnl|CDD|272943 TIGR00176, mobB, molybdopterin-guanine dinucleotide biosynthesis protein MobB. This molybdenum cofactor biosynthesis enzyme is similar to the urease accessory protein UreG and to the hydrogenase accessory protein HypB, both GTP hydrolases involved in loading nickel into the metallocenters of their respective target enzymes [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
VLQIVGPKNSGKTTLIERLVKALKARGYRVATIKHDHHDFDIDKNGKDSYRHREAGADQVIVASSRRYAF
MHETQEERDLEALLDRLPDLDIILVEGFKDSPLPKIVVFRNPAEESEIIRPKIIAIASDESLSALKLPVL
DLNDVEAIAAFIEKN
>gnl|CDD|272944 TIGR00177, Molybdopterin_molybdenumtransferase, molybdenum cofactor synthesis domain. The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis
PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVV
LTTGGTGVGPRDVTPEALEELGEKEIPGFGEFRMLSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALV
TFEVLILP
>gnl|CDD|129282 TIGR00178, Isocitrate_dehydrogenase, isocitrate dehydrogenase, NADP-dependent, monomeric type. The monomeric type of isocitrate dehydrogenase has been found so far in a small number of species, including Azotobacter vinelandii, Corynebacterium glutamicum, Rhodomicrobium vannielii, and Neisseria meningitidis. It is NADP-specific [Energy metabolism, TCA cycle]
MSTPKIIYTLTDEAPALATYSLLPIIKAFTASSGIAVETRDISLAGRILATFPEYLTEEQKISDALAELG
ELAQTPDANIIKLPNISASVPQLKAAIKELQDQGYDLPDYPAEPKTDTEKDIKARYAKIKGSAVNPVLRE
GNSDRRAPLSVKNYARKHPHSMGAWSADSKSHVAHMDNGDFYGSEKSATIDAAGSVKIELIAKDGSSTVL
KAKLPLLDGEIIDSSVMSKKALRNFIEEEIEDAKEEGVLLSLHLKATMMKVSDPIMFGHAVREFYKDAFA
KHAEVLKQLGVDVNNGIGDLYAKIESLPAAQQEEIEADLQAVYAQRPELAMVNSDKGITNLHVPSDVIVD
ASMPAMIRASGKMWGPDGKLKDTKAVIPDRCYAGVYQVVIEDCKQNGAFDPTTMGTVPNVGLMAQKAEEY
GSHDKTFQIPADGVVRVVDSSGEVLLEQSVEAGDIWRMCQVKDAPIQDWVKLAVTRARATGTPAVFWLDP
ARAHDAQLIKKVETYLKDHDTEGLDIQILSPVEATRFSLARIRRGEDTISVTGNVLRDYLTDLFPILELG
TSAKMLSIVPLMAGGGLFETGAGGSAPKHVQQFLEENHLRWDSLGEFLALAASLEHLGNATGNPKALVLA
DTLDAATGKLLDNNKSPSRKVGEIDNRGSHFYLALYWAQELAAQTEDKELQAQFASVAKALTKNETKIVA
ELAAAQGKPVDIGGYYHPNTDLTTKAMRPSATFNAALAALA
>gnl|CDD|272945 TIGR00179, UDP-N-acetylenolpyruvoylglucosamine_reductase, UDP-N-acetylenolpyruvoylglucosamine reductase. This model describes MurB, UDP-N-acetylenolpyruvoylglucosamine reductase, which is also called UDP-N-acetylmuramate dehydrogenase. It is part of the pathway for the biosynthesis of the UDP-N-acetylmuramoyl-pentapeptide that is a precursor of bacterial peptidoglycan [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGIDIED
DEGEYVHVGGGENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATGKT
EWLTNEQLGFGYRTSIFQHKYVGLVLKAEFQLTLGFGTRLDPETITAQQVFNKVCRMRTSHYPDPNAGSF
FKNPSPNHAGRLIEECGLKGYQIGGAAVSKQHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEV
KIIG
>gnl|CDD|272946 TIGR00180, Probable_chromosome-partitioning_protein_ParB, ParB/RepB/Spo0J family partition protein. This model represents the most well-conserved core of a set of chromosomal and plasmid partition proteins related to ParB, including Spo0J, RepB, and SopB. Spo0J has been shown to bind a specific DNA sequence that, when introduced into a plasmid, can serve as partition site. Study of RepB, which has nicking-closing activity, suggests that it forms a transient protein-DNA covalent intermediate during the strand transfer reaction
VAEGLIEIDIDLLQPNPYQPRKDFSEESLAELIESIKEQGQLQPILVRKHPDQPGRYEIIAGERRWRAAK
LAGLKTIPAIVRELDDEQMLADALIENIQREDLSPIEEAQAYKRLLEKFSMTQEDLAKKIGKSRAHITNL
LRLLKLPSEIQSAIPEASGLLSSGHARLLLALKKKPKLQELLASIII
>gnl|CDD|272947 TIGR00181, Oligoendopeptidase_F_homolog, oligoendopeptidase F. This family represents the oligoendopeptidase F clade of the family of larger M3 or thimet (for thiol-dependent metallopeptidase) oligopeptidase family. Lactococcus lactis PepF hydrolyzed peptides of 7 and 17 amino acids with fairly broad specificity. The homolog of lactococcal PepF in group B Streptococcus was named PepB (, with the name difference reflecting a difference in species of origin rather activity; substrate profiles were quite similar. Differences in substrate specificity should be expected in other species. The gene is duplicated in Lactococcus lactis on the plasmid that bears it. A shortened second copy is found in Bacillus subtilis [Protein fate, Degradation of proteins, peptides, and glycopeptides]
RSEVPKEYKWDLDDLYKNKEEWELFLEALEEDIKEIKAFKKGLLHSKETFLEALALEEKILILLNRLYNY
ASMKLSTDVTDPEANAISQKLSNLYTKVASATSFFEPEILEIEEKIIKEWLKDPEELADYKRALEEIFRD
KPHILSEEVEKLLSALSEVFGSPSDIYSTLTNADMDFGSIEDYKGKKYPITNSTYENFLQKNKDREIRKK
AYESFYKAYRKHKNTFAALYYGNVQKNVFLAKLRNYESYIDASLFSDEVPREVYDNLYDTIKKNAPVLQR
YYKLRKKVLKLDKMEPYDLYLPLVKEKNPKFSIEEAKELILKSLEPLGEEYIKILKRAFNERWVDYAENK
GKRSGAYSIGGYKVKPYILMNWDGTLNSVFTLAHELGHSMHSYFSSKHQPYPNSDYSIFYAEIASTFNEL
LLADYLLKNSNDPEMKIYILLERISNFFGTFTRQTLFAEFEYEAYELIEEGEPLTAETLNEIYANLLKKY
FGDLVKIDEGAGLTWMRIPHFYMGFYVYKYATGQVAATALYEKIKEEGKGAVEKYLKFLKSGGSKYPLET
LKIAGVDLTKPQPWQAAINIFSDWIDELEEL
>gnl|CDD|129286 TIGR00182, Phosphate_acyltransferase, fatty acid/phospholipid synthesis protein PlsX. This protein of fatty acid/phospholipid biosynthesis, called PlsX after the member in Streptococcus pneumoniae, is proposed to be a phosphate acyltransferase that partners with PlsY (TIGR00023) in a two-step 1-acylglycerol-3-phosphate biosynthesis pathway alternative to the one-step PlsB (EC 2.3.1.15) pathway [Fatty acid and phospholipid metabolism, Biosynthesis]
GGDHAPSEVIDGVLKYASANQDLHIILVGDKDAIEPHLDKLPKNITIIHAQSVIEMTDTPVRAIRRKVNS
SMQLAMNLVKEGRADAVISAGNSGALMGLALLRLGRIKGIDRPALMTLLPTVNGDWFVLLDVGANVDCKP
KYLVQFALMGSVYSKKVLGVDSPRVGLLNIGTEDNKGNDLHKETFQLLKEDPNINFIGNVEARDLLDGVC
DVLVCDGFTGNVVLKTMEGVAKTILSILKDEYKSTLRSKLAALFLKPILKSLKQKFDYANYGGAVLFGLN
KLVIKSHGSSDSRAFFSAIRQAHEAVKSQVINRIKSSLESLK
>gnl|CDD|272948 TIGR00183, Isocitrate_dehydrogenase, isocitrate dehydrogenase, NADP-dependent, prokaryotic type. Several NAD- or NADP-dependent dehydrogenases, including 3-isopropylmalate dehydrogenase, tartrate dehydrogenase, and the multimeric forms of isocitrate dehydrogenase, share a nucleotide binding domain unrelated to that of lactate dehydrogenase and its homologs. These enzymes dehydrogenate their substates at a H-C-OH site adjacent to a H-C-COOH site; Prokaryotic NADP-dependent isocitrate dehydrogenases resemble their NAD-dependent counterparts and 3-isopropylmalate dehydrogenase (an NAD-dependent enzyme) more closely than they resemble eukaryotic NADP-dependent isocitrate dehydrogenases [Energy metabolism, TCA cycle]
MYEKVKPPAQGEKITYENGKLNVPNNPIIPYIEGDGIGVDVTPAAIKVLDAAVEKAYKGEKKIVWFEVYA
GEKAYQLYGQDQWLPADTLDAIKEYRVAIKGPLTTPVGGGIRSLNVALRQELDLYVCLRPVRYYKGVPSP
VKHPEKVDMVIFRENTEDIYAGIEWAEGSEEAKKLIRFLQNELGVKKIRFPEDSGIGIKPISEEGTKRLV
RAAIEYAIENDRKSVTLVHKGNIMKFTEGAFRDWGYELAKKEFGAECITWGLWDKYKNPNPGKEIVIKDR
IADAFLQQILTRPDEYDVIATMNLNGDYISDALAAQVGGIGIAPGANIGDEIGIFEATHGTAPKYAGQDK
VNPGSIILSGEMMLEHMGWKEAADLIKKAMEKAIASKIVTYDFARLMDGAKEVKCSEFAEAIIENM
>gnl|CDD|272949 TIGR00184, Adenylosuccinate_synthetase, adenylosuccinate synthase. Alternate name IMP--aspartate ligase [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
VVVGGQWGDEGKGKIVDLLADKPDIVARYQGGHNAGHTIVIDGVKYGLHLIPSGFLYPDAKLLIGNGVVV
DPEVLLKEMEYLEKRGISVRDRLFVSYRCHLILPYHKKLDKAREKSKLAKKIGTTGKGIGPAYEDKVARS
GLRVGDLLDDEAFAEKAKNILEYLNEQLVKYYKDEGVDYEKKLDEYMKYAEELKPFVVDVSVELNEALDE
GEKVLFEGAQGTMLDIDYGTYPYVTSSNTTAGGVATGVGIGPTKVDEVIGVFKAYTTRVGAGPFPTELSD
EEGEKLGTKGAEFGTTTGRRRRCGWFDLVAARYACRLNGATQLALTKLDVLDGIDEIKVCVAYRMKGEIL
ELFPLDLKDLKGVEPIYETLPGWDKECTGVTEYSDLPENAKKYIERIEELTGVPVTIISTGPEREQTIDL
RKELL
>gnl|CDD|211559 TIGR00185, Putative_tRNA_cytidine34-2'-O-methyltransferase, tRNA (cytidine(34)-2'-O)-methyltransferase. TrmL (previously YibK) is responsible for 2'-O-methylation at tRNA(Leu) position 34 [Protein synthesis, tRNA and rRNA base modification]
MLNIVLYEPEIPPNTGNIARTCAATGTRLHLIEPLGFFLDDKRLKRAGLDYWEFVQVFYHKSWEEFLEAE
KPQKLFALTKKGTPAHSAVTYQDGDYLMFGPETRGLPQSILDNLMEQKIRIPMTNDVRSLNLSNAVAIVV
YEAWRQLGYPGLV
>gnl|CDD|129290 TIGR00186, Uncharacterized_tRNA/rRNA_methyltransferase_MG252, rRNA methylase, putative, group 3. this is part of the trmH (spoU) family of rRNA methylases [Protein synthesis, tRNA and rRNA base modification]
QEYLYGKNAVLEALLNQQRVFILKGLESKRLKKLIQLAKKQGINIQLVDRQKLDQLTKGGNHQGIAAKVK
PILYKDLNDLYKTAKSKKQPFLLILDEITDPHNLGAILRTAEAFGVDGVILPKRRSAPLNSTVVKTSSGA
VEYVPLARVTNLSRTITKLKESGFWTVGTDLDAQDTLYQVKLTKPLALVVGNEGEGVSRLIKENCDFLIK
IPMAGKVDSLNVSVAAGILLFEIKRQR
>gnl|CDD|272950 TIGR00187, Riboflavin_synthase, riboflavin synthase, alpha subunit. This protein family consists almost entirely of two lumazine-binding domains, described in the family Lum_binding from Pfam. The model generates lower scores against other proteins that also have two lumazine-binding domains, including some involved in bioluminescence.The name ribE was selected, from among alternatives including ribB and ribC, to match the usage in EcoCyc [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]
MFTGIIQGTAKLVSIKEKPLFISLVVNLADHMLDDLELGDSIAVNGVCLTVTEINKNHFSVDLSPETLKR
TNLGDLKVGTWVNIERALKADGEIGGHFVSGHIDTTAEIAKIETSENNVQFWFKLQDSELMKYIVEKGSI
AVDGISLTIGKVTETRFCVSLIPHTLENTILGLKKLGDRVNIEIDMLGKAVADTLERTLE
>gnl|CDD|211560 TIGR00188, Ribonuclease_P_protein_component, ribonuclease P protein component, eubacterial. This peptide is the protein component of a ribonucleoprotein that cleaves the leader sequence from each tRNA precursor to leave the mature 5'-terminus. The catalytic site is in the RNA component, M1 RNA. The yeast mitochondrial RNase P protein component gene RPM2 has no obvious sequence similarity to rnpA, but resembles eukaryotic nuclear RNase P instead [Transcription, RNA processing]
LKKPRRLRLKSEFQKVFQQGTRAFNPFLTIYVLKNELDHPRVGLSVSKKKVKNAVERNRIKRLIREVFRE
RQEELKALDVVVIVRKGFSELTYEALLKLLLQLFLRCKRLD
>gnl|CDD|272951 TIGR00189, Peroxisomal_acyl-coenzyme_A_thioester_hydrolase_1, acyl-CoA thioesterase II. Function: hydrolyzes a broad range of acyl-CoA thioesters. Physiological function is not known. Subunit: homotetramer [Fatty acid and phospholipid metabolism, Biosynthesis]
EKIDENLFRGSHLSKGRQFLNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERL
RDGRSFITRRVKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPESELPRENQLATKYPATLPRFLKH
VVPFERPFEIRPVNLLNYLGGKEDPPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFC
HSMAASLDHSIWFHRPFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR
>gnl|CDD|129294 TIGR00190, Phosphomethylpyrimidine_synthase, phosphomethylpyrimidine synthase. The thiC ortholog is designated thiA in Bacillus subtilis [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
MTQMHYARKGVITPEMKFVAERENVDPEFLRREVASGRIVIPSNINREESEPMGIGRNLRTKVNANIGTS
ADTSDIEEEVEKALIAIKYGADTVMDLSTGGDLDEIRKAILDAVPVPVGTVPIYQAAEKVHGAVEDMDED
DMFRAIEKQAKDGVDFMTIHAGVLLEYVERLKRSGRITGIVSRGGAILAAWMLHHHKENPLYKNFDYILE
IAKEYDVTLSLGDGLRPGCIADATDRAQISELITLGELVERAREADVQCMVEGPGHVPLDQIEANVRLQK
ELCDEAPFYVLGPLVTDIAPGYDHITSAIGAAIAGWAGADFLCYVTPKEHLALPNVEDVKEGVIAYKIAA
HAADLAKGHPGARERDLEMSKARKNFDWERQFELALDPEKAREYRDETPPEDEDFCSMCGKYCAMKIVQE
ARD
>gnl|CDD|129295 TIGR00191, Homoserine_kinase, homoserine kinase. Homoserine kinase is part of the threonine biosynthetic pathway.Homoserine kinase is a member of the GHMP kinases (Galactokinase, Homoserine kinase, Mevalonate kinase, Phosphomevalonate kinase) and shares with them an amino-terminal domain probably related to ATP binding.P.aeruginosa homoserine kinase seems not to be homologous (see PROSITE:PDOC0054) [Amino acid biosynthesis, Aspartate family]
FRVKVPASSANLGPGFDVLGAALSLYLGLTVTDVVAQESDDTEIEAEGEGVEKIPTEPTDNLIYQVAKRF
LDQLGIRMPPVKVTLEKNIPLGRGLGSSAAAIVAALAAANELCGLPLSKERLLDYASELEGHPDNVAPAL
LGGFQLAFVEDDKLEVLKIPIFSKLDWVLAIPNIEVSTAEARAVLPKAYPRQDLVFNLSHLAGLVHAIYQ
KKPDLGAIMMKDRIHQPYRESLIPNLFKIKQAALEKGAYGITISGSGPTILAMADEEFAEQKEQDLLEVL
HKQGIEGTVHVLDFDNDGARVE
>gnl|CDD|129296 TIGR00192, Urease_subunit_beta, urease, beta subunit. In a number of species, including B.subtilis, Synechocystis, and Haemophilus influenzae, urease subunits beta and gamma are encoded as separate polypeptides. In Helicobacter pylori UreA and in the fission yeast Schizosaccharomyces pombe, beta subunit-like sequence follows gamma subunit-like sequence in a single chain; the fission yeast protein contains additional C-terminal regions [Central intermediary metabolism, Nitrogen metabolism]
MIPGELQLAEGDITINEGRKTVSVKVKNTGDRPIQVGSHFHFFEVNRALDFDRELAFGMRLDIPSGTAVR
FEPGEEKSVELVAIGGNRRIYGFNGLVDGQL
>gnl|CDD|272952 TIGR00193, Urease_subunit_gamma, urease, gamma subunit. In a number of species, including B.subtilis, Synechocystis, and Haemophilus influenzae, urease subunits beta and gamma are encoded as separate polypeptides. In Helicobacter pylori UreA and in the fission yeast Schizosaccharomyces pombe, beta subunit-like sequence follows gamma subunit-like sequence in a single chain; the fission yeast protein contains additional C-terminal regions. Nomenclature for the various subunits of urease in Helicobacter differs from nomenclature in most other species [Central intermediary metabolism, Nitrogen metabolism]
MKLTPKEQDKLMLFYAGELAKKRKARGVKLNYPEAVAYISAHIMEGARDGKKVAELMQYGRTLLTPDDVM
EGVAEMLHEVQIEATFPDGTKLVTVHTPIRAN
>gnl|CDD|272953 TIGR00194, UvrABC_system_protein_C, excinuclease ABC, C subunit. This family consists of the DNA repair enzyme UvrC, an ABC excinuclease subunit which interacts with the UvrA/UvrB complex to excise UV-damaged nucleotide segments [DNA metabolism, DNA replication, recombination, and repair]
LKEKLKNLPDKPGCYLMKDRNGQVLYVGKAKNLKKRVSSYFRENNSAKTQALVKQIADIEYILTKNENEA
LILEANLIKQYQPRYNVLLKDDKGYPYIYITHEKYPRLLITRKLKQDKGKYFGPFTNAFALRETLDLLLK
LFPLRKCAKHNRNRPCLYYQIGRCLGPCVKEITEEEYQQIVEKIELFFNGRPQEVIKELEQKMEKASENL
EFEEAARIRDQIAAVRELNEKQHVSLTDLIDLDIIAVAFDGNVAAIQVFFIRQGKLIGRDQFDFSLPGTD
LDELVETFLIQFYQQGYQNRLIPSEILVSLSLEDLKLLEDLLSEQRGRKINVHQPKKGDKKKLLELAIKN
AKYALKQKWTQFERKTQALEDLASLLNLPKIKRIEIFDISHIDGSQTVGSMVVFEDGKPLKASYRRYNIN
SITGGDDYAAMREVLRRRYSSIQKKNNLPLPDLILIDGGKGQLNAALEVLKSLGVVNKPIVIGLAKAKRH
ETDIFLIGDKQGINIDLNSPALQLLQHIRDEAHRFAISFHRKKRLKASLQSPLLKIPGVGEKRVQKLLKY
FGSLKGIKKASVEE
>gnl|CDD|272954 TIGR00195, Exodeoxyribonuclease_III, exodeoxyribonuclease III. The model brings in reverse transcriptases at scores below 50, model also contains eukaryotic apurinic/apyrimidinic endonucleases which group in the same family [DNA metabolism, DNA replication, recombination, and repair]
MKIISWNVNGLRARPHKGLAWLKENQPDVLCLQETKVQDEQFPLEPFHKEGYHVFFSGQKGYSGVAIFSK
EEPISVRRGFGVEEEDAEGRIIMAEFDSFLVINGYFPNGSRDDSEKLPYKLQWLEALQNYLEKLVDKDKP
VLICGDMNIAPTEIDLHIPDENRNHTGFLPEEREWLDRLLEAGLVDTFRKFNPDEGAYSWWDYRTKARDR
NRGWRIDYFLVSEPLKERCVDCGIDYDIRGSEKPSDHCPVVLEF
>gnl|CDD|272955 TIGR00196, ADP-dependent_S-NADPH-hydrate_dehydratase, yjeF C-terminal region, hydroxyethylthiazole kinase-related. E. coli yjeF has full-length orthologs in a number of species, all of unknown function. However, yeast YNL200C is homologous and corresponds to the N-terminal region while yeast YKL151C and B. subtilis yxkO correspond to this C-terminal region only. The present model may hit hydroxyethylthiazole kinase, an enzyme associated with thiamine biosynthesis [Unknown function, General]
ETFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSV
SPELIVHRLMWKVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREG
EVILTPHPGEFKRLLGVNEIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGT
GDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGDLALKNHGAYGLTALDLIEKIPRVCKR
>gnl|CDD|272956 TIGR00197, NADPH-hydrate_epimerase, yjeF N-terminal region. The protein region corresponding to this model shows no clear homology to any protein of known function. This model is built on yeast protein YNL200C and the N-terminal regions of E. coli yjeF and its orthologs in various species. The C-terminal region of yjeF and its orthologs shows similarity to hydroxyethylthiazole kinase (thiM) and other enzymes involved in thiamine biosynthesis. Yeast YKL151C and B. subtilis yxkO match the yjeF C-terminal domain but lack this region [Unknown function, General]
KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKG
FGVEVFLLKKEKRIECTEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVE
SINELPAPIVSVDIPSGLDVDTGAIEGPAVNADLTITFHAIKPCLLSDRADVTGELKVGGIGIPP
>gnl|CDD|272957 TIGR00198, cat_per_HPI, catalase/peroxidase HPI. As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family [Cellular processes, Detoxification]
ASQGGVMHGANTTGQTGDWWPNALNLDILHQHDRKTNPMGEDFDYAEEFQQLDLAAVKQDLKHLMTDSQS
WWPADWGHYGGLFIRMAWHAAGTYRIADGRGGAATGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYGNKL
SWADLIILAGTVAYESMGLKVFGFAGGREDIWEPDKDIYWGAEKEWLTSSREDRESLENPLAATEMGLIY
VNPEGPDGHPDPLCTAQDIRTTFARMGMNDEETVALIAGGHTVGKCHGAGPAELIGPDPEGAPIEEQGLG
WHNQYGKGVGRDTMTSGLEVAWTTTPTQWDNGYFYMLFNYEWELKKSPAGAWQWEAVDAPEIIPDVEDPN
KKHNPIMLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLTHRDMGPKSRYIGPDVPQEDLIWQD
PLPPVDYTLSEGDIKELKQQILASGLSVSELVCTAWASASTFRSSDYRGGANGARIRLEPQKNWPVNEPT
RLAKVLAVLEKIQAEFAKGPVSLADLIVLGGGAAVEKAALDAGISVNVPFLPGRVDATQAMTDAESFTPL
EPIADGFRNYLKRDYAVTPEELLLDKAQLLTLTAPEMTVLIGGMRVLGANHGGSKHGVFTDRVGVLSNDF
FVNLLDMAYEWRAADNNRYLFEGGDRQTGEVKWTATRVDLVFGSNSILRAVAEVYAQDDAREKFVKDFVA
AWTKVMNLDRFDLPRG
>gnl|CDD|129303 TIGR00199, Putative_competence-damage_inducible_protein, amidohydrolase, PncC family. CinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species. Several bacterial species have a protein consisting largely of the C-terminal domain of CinA but lacking the N-terminal domain, including nicotinamide mononucleotide (NMN) deamidase (3.5.1.42) proteins PncC in Shewanella oneidensis and ygaD in E. coli [DNA metabolism, DNA replication, recombination, and repair]
LSERLKALGLTVATAESCTGGLLAHALTDISGASKYFGGGVVCYTNQVKINLLGVSQETLARFGAVSEEC
AAEMALGVKERFGADVGIAISGIAGPDGGEEEKPGGTVWFIWIIAKGQAYTAEMHFAGDRETIRALAVRY
ALHQLL
>gnl|CDD|161761 TIGR00200, Putative_competence-damage_inducible_protein, competence/damage-inducible protein CinA N-terminal domain. cinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species [DNA metabolism, DNA replication, recombination, and repair]
LKAEIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLG
PTSDDLTAETIATAKGEPLVLNEAWLKEIERYFHETGRVMAPNNRKQALLPAGAEFLANPVGTAPGMFAV
QLNRCLMLFTPGVPSEFRVMVEHEALPRLRERFSLPQPIVSLVLRFFGIGESQLEADLADSLDTLTNPTG
APMAYRGEVPLRELKLTGPESEQQRAMEKLWLDIKRVAGQSVIGEDTEGLPAQISRELQERGFTLTLAES
FTGGLLALQLTDHSGASKLFAGGVPLYANEVKPSQLGVLAETAHWIGAVSANHAAGLALGVSGFEGEDLG
IALTGPAGPDFAERVRFGTVRYGLAIRQEVAMHALNMLGRRLGIRDIAAEHGWIEVVESLTLS
>gnl|CDD|272958 TIGR00201, ComF_operon_protein_3, comF family protein. This protein is found in species that do (Bacillus subtilis, Haemophilus influenzae) or do not (E. coli, Borrelia burgdorferi) have described systems for natural transformation with exogenous DNA. It is involved in competence for transformation in Bacillus subtilis [Cellular processes, DNA transformation]
CSLCGRPYQSVHALCRQCGSWRTRIRDSLCLRQNLVSVYTYNEPLKELISRFKFRGQAEIIRALASLLSL
TVSKAYRDLPDVIVPVPLSKEREWRRGFNQADLLAQCLSRWLFNYHNIVIRLNNETQSKLKATLRFLNLE
NAFDLKNNSFQGRNIVLVDDVVTTGATLHEIARLLLELGAASVQVWTLAR
>gnl|CDD|272959 TIGR00202, Carbon_storage_regulator_homolog, carbon storage regulator (csrA). Modulates the expression of genes in the glycogen biosynthesis and gluconeogenesis pathways by accelerating the 5'-to-3' degradation of these transcripts through selective RNA binding. The N-terminal end of the sequence (AA 11-45) contains the KH motif which is characteristic of a set of RNA-binding proteins [Energy metabolism, Glycolysis/gluconeogenesis, Regulatory functions, RNA interactions]
MLILSRKVNESIQIGDDIEVKVLSVKGDQVKLGIEAPKEISIHREEIYERIQEENNKAALLSSDVISAI
>gnl|CDD|129307 TIGR00203, ubiquinol_oxidase_subunit_2, cytochrome d oxidase, subunit II (cydB). part of a two component cytochrome D terminal complex. Terminal reaction in the aerobic respiratory chain [Energy metabolism, Electron transport]
MIDYESLRFIWWLLVGVLLVGFFVTDGFDMGVGMLTRFLGRNELERRIMINTIGPHWDGNQVWLLTAGGA
IFAAWPNVYAAAFSGFYIAMVLVLAALFFRPVAFEYRGKIDHLRWRKVWDWGLFIGSLVPPLVFGVAFGN
LLQGVPFDFDENLRVHYTGSFFQLLNPFSLLCGVTSLGMCITHGAMWLQLRTVGDLHLRARKMAQKAALV
VLVAFLLAGVWSAYGIDGFVVRSQDHNAPSNPLNKEVAVEPGAWMNNFNEEPILWIFPALGVVCPLLTAV
FIRKKKDGWAFGMSSLTLAGVIGTAGISLFPFVMPSSLHPAYSLTMWDATSSQLTLKVMLIAALVLLPIV
LLYTIWSYYKMFGRVTTETIRRNEHSLY
>gnl|CDD|129308 TIGR00204, 1-deoxy-D-xylulose-5-phosphate_synthase, 1-deoxy-D-xylulose-5-phosphate synthase. DXP synthase is a thiamine diphosphate-dependent enzyme related to transketolase and the pyruvate dehydrogenase E1-beta subunit. By an acyloin condensation of pyruvate with glyceraldehyde 3-phosphate, it produces 1-deoxy-D-xylulose 5-phosphate, a precursor of thiamine diphosphate (TPP), pyridoxal phosphate, and the isoprenoid building block isopentenyl diphosphate (IPP) [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine, Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGH
QAYPHKLLTGRREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVI
GDGAITAGMAFEALNHAGDLKTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLP
PIKNYLAKRTEESMKGLVVPGTFFEELGFNYIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYK
PAEKDPIGWHGVGPFDLSTGCLPKSKSALPSYSKIFSDTLCELAKKDNKIVGITPAMPEGSGLDKFSRKF
PDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQVVHDVCIQKLPVLFAIDRAGIVGADGE
THQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGNAVGVELTPEPEKLPIGKSE
VLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELILEIAASHEKLVTVEENAIMG
GAGSAVLEFLMDQNKLVPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWLA
>gnl|CDD|272960 TIGR00205, Flagellar_hook-basal_body_complex_protein_FliE, flagellar hook-basal body complex protein FliE. fliE is a component of the flagellar hook-basal body complex located possibly at (MS-ring)-rod junction [Cellular processes, Chemotaxis and motility]
MVRNDAFAISPFINLNTQNPHTAVNLFSSKSKAQDNDSFSDLLKNSITDLNKTQLASDKVTEQAALGPSS
VDLHDVMIAMQKASMSMSILKEVRNKAVKAYQEIMRMQ
>gnl|CDD|129310 TIGR00206, Flagellar_M-ring_protein, flagellar basal-body M-ring protein/flagellar hook-basal body protein (fliF). Component of the M (cytoplasmic associated) ring, one of four rings (L,P,S,M) which make up the flagellar hook-basal body which is a major portion of the flagellar organelle. Although the basic structure of the flagella appears to be similar for all bacteria, additional rings and structures surrounding the basal body have been observed for some bacteria (eg Vibrio cholerae and Treponema pallidum) [Cellular processes, Chemotaxis and motility]
MNKTFTQFKVSAKEFFKKLSKVQKIALILAGFAIIAALVFLILFATKSQSYALLFVELSDQDLGRISQRL
DQENVPYFLSSDGRIILVPEDKVKELRAILAREGLPKTGMVGFELFDQDRFGITDFERSINLRRAIEGEL
SRTIEALDPVKAASVHLAMPKDALFVEEQEPPSASVRLTLRPGSDLDTNQIEGLVHLISYAVPGLESDNI
AIVDQNGTILNDSNLDGIDRIDLAEKQLKYKSKVEAMLQGEIDSILSPIVGVDNFVVARVNAKLDFSKET
TTEEEYAPNELESSDSTIRSSQTQEEEYQGQGYSPGGVPGQESNTPPPVQDLKDNTGNYEESQYEKNVQL
NEKKNYEVKRTIREIKVSLGIVVDLIWAVVVDEKGDFVLPDGKNKREYKPLSLEEIKNIEDLLQSAFGYS
PERGDSITVRNISFNRINNFREIEENYFASQRFLDFLTIASIVFLVLIVAFIIFFKIIRPLERRRREREE
ELAKQAHLREEQEDEVEGELIKLDDLVGGINEGDEEVSNAELRAMAKEKPEDVAKLIRTWLLKDA
>gnl|CDD|272961 TIGR00207, Flagellar_motor_switch_protein_FliG, flagellar motor switch protein FliG. The fliG protein along with fliM and fliN interact to form the switch complex of the bacterial flagellar motor located at the base of the basal body. This complex interacts with chemotaxis proteins (eg CHEY). In addition the complex interacts with other components of the motor that determine the direction of flagellar rotation. The model contains putative members of the fliG family at scores of less than 100 from Agrobacterium radiobacter and Sinorhizobium meliloti as well as fliG-like genes from treponema pallidum and Borrelia burgdorferi. That is why the suggested cutoff is set at 20 but was set at 100 to construct the family [Cellular processes, Chemotaxis and motility]
MATKDMSNLTGKQKAAILLISIGEDRSAEVFKHLSQEEIETLSAEIANVTQIDNQQKDDVLEEFEQIAEA
QAYINIGGLDYAREVLEKALGEEKAASILNDLTSSLQTAPGFEFLRKAEPQQIADFIQQEHPQTIALILS
HLDPAQAADILSLFPEEVQAEVARRIATMGRTSPEVVAEVERVLEGKLDSLNSDYTKMGGVRAVAEIINL
MDRKTEKTIITSLEEFDPELAEEIKKEMFVFEDIVDLDDRSIQRVLREVDSEDLLLALKGAEQPLREKFL
NNMSQRAAEILKEDMEFLGPVRLKDVEEAQKKIVSIVRKLEETGEIVIGRGGEEDVIV
>gnl|CDD|188033 TIGR00208, Flagellar_protein_FliS, flagellar biosynthetic protein FliS. The function of this protein in flagellar biosynthesis is unknown, but appears to be regulatory. The member of this family in Vibrio parahaemolyticus is designated FlaJ (creating a synonym for FliS) and was shown essential for flagellin biosynthesis [Cellular processes, Chemotaxis and motility]
MAIANPYQAYQQNSVNTASPGELTLMLYNGCLKFIRLAAQAIENDDIERKNENLIKAQNIIQELNFTLDR
EKNIELSASLGALYDYMYRRLVQANIKNDTSKLAEVEGYVRDFRDAWKEAIQSE
>gnl|CDD|129313 TIGR00209, Galactose-1-phosphate_uridylyltransferase, galactose-1-phosphate uridylyltransferase, family 1. This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087 [Energy metabolism, Sugars]
MTQFNPVDHPHRRYNPLTDQWILVSPHRAKRPWQGQQETPAKQVLPAYDPDCYLCPGNKRVTGDLNPDYT
GTYVFTNDFAALMSDTPDAPESHDPLMRCQSARGTSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAE
LGKTYPWVQIFENKGAAMGCSNPHPHGQIWANSFLPNEVEREDRLQKEYFAEHKSPMLVDYVKRELADKS
RTVVETEHWIAVVPYWAIWPFETLLLPKAHVLRITDLTDAQRSDLALILKKLTSKYDNLFETSFPYSMGW
HGAPFNGEENQHWQLHAHFYPPLLRSATVRKFMVGYEMLGETQRDLTAEQAAERLRALSDIHYRERG
>gnl|CDD|129314 TIGR00210, Sodium/glutamate_symport_carrier_protein, sodium--glutamate symport carrier (gltS) [Transport and binding proteins, Amino acids, peptides and amines]
IQFDIYATLVVAILVLLLGRYLVKKIKFLKSFNIPEPVVGGVLVALALLLIYKIFGTEVNFDFSLRDPLM
LIFFTTIGLSANFKSLLKGGKPLLIFLATAVGFLVIQNAVGIGMASLLGQAPLMGLLAGSITLSGGHGTG
AAWSPVFYDNYGFRNATEIAIACATFGLVFGGIIGGPVAKFLIIRNKLEPNCENDTKDVTIGFERPQDNR
QITYNSLIETIALIAVCLLVGYELNDLVAKTALMLPTFVWCLFVGVILRNPLSFKKFPWVAERAVSVIGN
VSLSLFLAIALMSLQLWELADLAGPIALILLVQVMFMALYAIFVTFRLMGKDYDAAVLCAGHCGFGLGAT
PTAIANMQAVTERFGPSHQAFIVVPLVGAFFIDIINALVIKQFLNLPG
>gnl|CDD|272962 TIGR00211, Glycine--tRNA_ligase_beta_subunit, glycyl-tRNA synthetase, tetrameric type, beta subunit. The glycyl-tRNA synthetases differ even among the eubacteria in oligomeric structure. In Escherichia coli and most others, it is a heterodimer of two alpha chains and two beta chains, encoded by tandem genes. The genes are similar, but fused, in Chlamydia trachomatis. By contrast, the glycyl-tRNA synthetases of Thermus thermophilus and of archaea and eukaryotes differ considerably; they are homodimeric, mutually similar, and not detected by this model [Protein synthesis, tRNA aminoacylation]
MSSQTFLVEIGTEELPAKALRSLATQFADKLTAELNKAGLEHGNVEIFATPRRLAVLVKDLAELQPDRKE
EKKGPAVKIAFDADGKPTKAALGFAKGQGINVEDAEIFQTDKGEWLFVRKIHEGQPTKDLLPPLVLEFLA
KLPFPKSMRWGNVDVRFIRPIHWIVVLLGDDVIPIEILNVKSDRTTRGHRFLGEDEVSIESPDAYPEQLK
ENHVIADPKERKAMILQQIETLAAKLGGIADIDEDLLDEVVSLVEYPTALLGKFEEEFLSLPAEVLVTTM
KEHQRYFPVYDKDGKLLPHFITVSNGNSKDPQKIILGNEKVLRARLSDAEFFYKTDLKKPLDDNLPRLET
VVFQQELGTLKDKVDRISIIAGYIAQQLGADENMLEHVKRAALLSKADLVTNMVYEFPELQGIMGEKYAR
HDGEDEAVAVAVNEQYLPRSAGDDLPSSLVGSVVAMADKLDTLASIFGIGQIPTGSKDPFALRRAALGVL
RIIVEKNLEIDLEELLTNFVLLQGDKLTNSNVLEDLEDFFLQRFRALLQDEGIDVDVIQAVLARRETDPA
DFDARAQALSHFRDLPKAEALAAANKRVANILKKGNPVLSSEIQANLFKEPKEKALFEAVLAIKMNAQES
FESGDYETALEALAELRAPVDEFFDSVMVMADDIELRQNRLNFLWGLRQLFLEVADISALQ
>gnl|CDD|272963 TIGR00212, Porphobilinogen_deaminase, hydroxymethylbilane synthase. Alternate name hydroxymethylbilane synthase Biosynthesis of cofactors, prosthetic groups, and carriers: Heme and porphyrin [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
LRIGTRGSKLALAQANLVREQLKAVYPELDTEIVIIKTTGDKIQDKPLYDIGGKGLFTKELEQALLDGEI
DLAVHSLKDVPTVLPEGLEIAAVLKREDPRDVLVSRKYLSLDSLPQGAKVGTSSLRRKAQLKAIRPDLKI
EPLRGNIDTRLRKLDEGEYDAIILAEAGLKRLGLEDVITEVLDPEVMLPAPGQGAIAVECRKDDTEIKEI
LKEINHPPTRVEATAERAFLKELGGGCQTPIGAYAEYNGNKLTLIAMVADLDGKEVIREEKEGNIEDAEL
GTEVAEELLKRG
>gnl|CDD|129317 TIGR00213, Hypothetical_protein_yaeD., D,D-heptose 1,7-bisphosphate phosphatase. This family of proteins formerly designated yaeD resembles the histidinol phosphatase domain of the bifunctional protein HisB. The member from E. coli has been characterized as D,D-heptose 1,7-bisphosphate phosphatase, GmhB, involved in inner core LPS assembly () [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
NKAIFLDRDGTINIDHGYVHEIDNFEFIDGVIDALRELKKMGYALVLVTNQSGIARGYFTEAQFEQLTEW
MDWSLAERDVDLDGIYYCPHHPEGVEEFRQVCDCRKPKPGMLLQARKELHIDMAQSYMVGDKLEDMQAGV
AAKVKTNVLVRTGKPITPEAENIADWVLNSLADLPQ
>gnl|CDD|272964 TIGR00214, Octanoyltransferase_mitochondrial, lipoate-protein ligase B. Involved in lipoate biosynthesis as the main determinant of the lipoyl-protein ligase activity required for lipoylation of enzymes such as alpha-ketoacid dehydrogenases. Involved in activation and re-activation (following denaturation) of lipoyl-protein ligases (calcium ion-dependant process) [Protein fate, Protein modification and repair]
FTDTKQRDRQTLDEIMLVEHYPVYTQGQAGKTEHLLFDPDIPPAEVVQSERGGQVTYHGPGQQVMYVILD
LKRFQLDVRWLVTQLEQTVIITLAELGIEGEPIADATGVWVEGKKVASLGIRVRRGCTFHGLALNINMDL
SPFSHINPCGYAGREMGSLNQFLPGATVENVAPLLIKAFAELLG
>gnl|CDD|129319 TIGR00215, Lipid-A-disaccharide_synthase, lipid-A-disaccharide synthase. Lipid-A precursor biosynthesis producing lipid A disaccharide in a condensation reaction. transcribed as part of an operon including lpxA [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
MRIFIPTIALVAGEASGDILGAGLRQQLKEHYPNARFIGVAGPRMAAEGCEVLYSMEELSVMGLREVLGR
LGRLLKIRKEVVQLAKQAKPDLLVGIDAPDFNLTKELKKKDPGIKIIYYISPQVWAWRKWRAKKIEKATD
FLLAILPFEKAFYQKKNVPCRFVGHPLLDAIPLYKPDRKSAREKLGIDHNGETLALLPGSRGSEVEKLFP
LFLKAAQLLEQQEPDLRRVLPVVNFKRRLQFEQIKAEYGPDLQLHLIDGDARKAMFAADAALLASGTAAL
EAALIKTPMVVGYRMKPLTFLIARRLVKTDYISLPNILANRLLVPELLQEECTPHPLAIALLLLLENGLK
AYKEMHRERQFFEELRQRIYCNADSERAAQAVLEF
>gnl|CDD|272965 TIGR00216, 4-hydroxy-3-methylbut-2-enyl_diphosphate_reductase, (E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate reductase (IPP and DMAPP forming). The IspH protein (previously designated LytB) has now been recognized as the last enzyme in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Escherichia coli LytB protein had been found to regulate the activity of RelA (guanosine 3',5'-bispyrophosphate synthetase I), which in turn controls the level of a regulatory metabolite. It is involved in penicillin tolerance and the stringent response [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
KIILAKPRGFCFGVKRAIQMAEEALKEPGKPVYTLGEIVHNPQVVERLRERGVVFFLEDLDEVAAGDTVI
FRAHGVPPEVREELEKKGLEVIDATCPLVTKVHNAAKKYAKEGYHVILIGKKNHPEVIGTRGYAPDGAIL
VETKEDLENFKFADEKRLGVVSQTTLSQEDTKEIVAALKARYPQKEVPAFNTICYATQNRQDAVRELAPE
VDLMIVIGGKNSSNTTRLFEIAEEHGGPSYLIETAEELPEEWLKGVKVVGITAGASTPDWIIEEVIRKLK
EL
>gnl|CDD|129321 TIGR00217, malQ, 4-alpha-glucanotransferase. This enzyme is known as amylomaltase and disproportionating enzyme [Energy metabolism, Biosynthesis and degradation of polysaccharides]
KKYKKPRILLNLKRKSGILLQLYSLPSEWGIGDLGDGAYKFIDFLKAGSQSVWQIHALYPADFTRSPPYS
ISSARALNVYYIDLEALDEFIDLPLSLLKEAELRESDRVDYSKKIALKDTALKEAFLNFINRASADEVRS
FAEFKKKQSDWLADFASFVAQKEAFFKESKNAGWVLWDKGIQKRNEPELFKLRNILSKEIKFQEWLQWLF
FSQFQALKRYANDMGIGLYGDLPVFVAYDSADVWADPELFCLRASAGAPKPAGLGPDYFLEQGQNWGLPP
YDWNVLKARGYEWWIKRLGANMQYADILRIDHFRGFVSLWWVPAGESTAFNGAWVHYPGDDFFNILANES
KDNLKIIGEDLGTVPEEVSRLRDEFNFPGMKVLYFAFDFDSSNRNLPHNYPKNAIVYTGTHDNDLTLGEF
LGISLDDYQKRYILHYLNCLPNFYVHWALIRSAMGSVNRNVIVYLQDLIGLGDEFSANIPGTTYDNWIFR
LLESLLDAFLSQNLSFITRLYGR
>gnl|CDD|272966 TIGR00218, Putative_mannose-6-phosphate_isomerase_YvyI, mannose-6-phosphate isomerase, class I. The names phosphomannose isomerase and mannose-6-phosphate isomerase are synonomous. This family contains two rather deeply branched groups. One group contains an experimentally determined phosphomannose isomerase of Streptococcus mutans as well as three uncharacterized paralogous proteins of Bacillus subtilis, all at more than 50 % identity to each other, plus a more distant homolog from Archaeoglobus fulgidus. The other group contains members from E. coli, budding yeast, Borrelia burgdorferi, etc [Energy metabolism, Sugars]
PLFIFPVFKERDWGGTALADLFGYSIPSQQTGECWAGSAHPKGPSTVLNGPYKGVSLIDLWEKHRELLGR
ADGDRFPFLFKVLDAAKPLSIQVHPDDKYAEIHEEGELGKTECWYIIDCDEAAEIIKGHLKNSKEELWTM
IEDGLFKLLLNRIKLKPGDFFYVPSGTPHAYKGGLVLEVMQNSDNVYRAGDTDKYLDIEKLVEVLTFPHV
PEFHLKGQPQKNGAEIVFMVPTEYFSVYKWDISGKAEFIQQQSALILSVLEGSGRIKSGGKTLPLKKGES
FFIPAHLGPFTIEGECEAIVSH
>gnl|CDD|129323 TIGR00219, Cell_shape-determining_protein_MreC, rod shape-determining protein MreC. MreC (murein formation C) is involved in the rod shape determination in E. coli, and more generally in cell shape determination of bacteria whether or not they are rod-shaped. Cells defective in MreC are round. Species with MreC include many of the Proteobacteria, Gram-positives, and spirochetes [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
MKFLVKPKLFIRLLLALIVSLGFIIADSRNSSIQKRRSDMFTAVTLNYYIQNRPREVFDGISENLKDVNN
LEYENYKLRQELLKKNQQLEILTQNLKQENVRLRELLNSPLSSDEYKISAEVIYLNYDNYSTQVVINKGF
NDGVYKDMPVIADGKGLVGKVVSVGSNTSRVLLLTDYTNFVPAQILRSDFRGLIEGNGYGKTLEMNLVNR
PAEKDIKKGDLIVTSGLGGRFPEGYPIGVVTSVHIDSYNSLLVIEVKPAAVLDRLRYVLLVWNDVPNKET
PEE
>gnl|CDD|272967 TIGR00220, Large-conductance_mechanosensitive_channel, large conductance mechanosensitive channel protein. Protein encodes a channel which opens in response to a membrane stretch force. Probably serves as an osmotic gauge. Carboxy terminus tends to be more divergent across species with a high degree of sequence conservation found at the N-terminus [Cellular processes, Adaptations to atypical conditions]
FWKEFKEFAMRGNVVDLAVGVVIGGAFGKIVSSLVADIIMPLLGLLLGGIDFSGLSFTLQDAQAVGKYGE
FIQNIINFLIIAFAIFMIIKAINKLRRKKKVEEEAAAEAPDAQENLLTEIRDLLKNQ
>gnl|CDD|272968 TIGR00221, N-acetylglucosamine-6-phosphate_deacetylase, N-acetylglucosamine-6-phosphate deacetylase [Central intermediary metabolism, Amino sugars]
MAESYLLKDIAIVTGNEVIDNGAVGINDGKISTVSTEAELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVD
TNDASFETLEIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKNAQALGLHLEGPFLSPEKK
GAHPPEYIREPDVELFKKFLCEAGGVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFK
AGATHATHLYNAMSPIHHREPGVIGAVLDHDDVYTEIIADGIHIHPLNIRLAKKLKGDSKLCLVTDSMAA
AGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEGARNLVEFTNISLTDAARMSSLNPARALGIDD
RLGSVTVGKDANLVVFTPDFEVILTIVNGN
>gnl|CDD|272969 TIGR00222, 3-methyl-2-oxobutanoate_hydroxymethyltransferase, 3-methyl-2-oxobutanoate hydroxymethyltransferase. Members of this family are 3-methyl-2-oxobutanoate hydroxymethyltransferase, the first enzyme of the pantothenate biosynthesis pathway. An alternate name is ketopantoate hydroxymethyltransferase [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
KKTTLSLLQKKKQEEKIVAITAYDYSFAKLFADAGVDVILVGDSLGMVVLGHDSTLPVTVADMIYHTAAV
KRGAPNCLIVTDLPFMSYATPEQALKNAARVMQETGANAVKLEGGEWLVETVQMLTERGVPVVGHLGLTP
QSVNILGGYKVQGKDEEAAKKLLEDALALEEAGAQLLVLECVPVELAAKITEALAIPVIGIGAGNVCDGQ
ILVMHDALGITVGHIPKFAKNYLAETETIRAAVRQYMAEVRSGVFPGEEHSFH
>gnl|CDD|129327 TIGR00223, Aspartate_1-decarboxylase, L-aspartate-alpha-decarboxylase. Members of this family are aspartate 1-decarboxylase, the enzyme that makes beta-alanine and C02 from aspartate. Beta-alanine is then used to make the vitamin pantothenate, from which coenzyme A is made. Aspartate 1-decarboxylase is synthesized as a proenzyme, then cleaved to an alpha (C-terminal) and beta (N-terminal) subunit with a pyruvoyl group [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
MIRTMLQGKLHRATVTHANLNYEGSITIDEDLLDAAGILENEKVDIVNVNNGKRFSTYAIAGKRGSRIIC
VNGAAARCVSVGDIVIIASYVTMPDEEARTHRPNVAYFEGDNEIKRTAKAIPVQVA
>gnl|CDD|161774 TIGR00224, Phosphoenolpyruvate_carboxykinase, phosphoenolpyruvate carboxykinase (ATP). Involved in the gluconeogenesis pathway. It converts oxaloacetic acid to phosphoenolpyruvate using ATP. Enzyme is a monomer. The reaction is also catalysed by phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32) using GTP instead of ATP, described in PROSITE:PDOC00421 [Energy metabolism, Glycolysis/gluconeogenesis]
TNNVLTPQELEALGISDVHDIVYNPSYAQLYEEELKPSLTGYEKGVLTSTGAVAVDTGIFTGRSPKDKYI
VEDETTKDTIWWGPVNKPLSEETWQHLKGLVTRQLSRKRLFVVDAFCGADPKYRLSVRVVTEVAWQAHFV
KNMFIRPTEEELAGFEPDFTVMNGAKFTNPNWKEQGLNSENFVAFNLTERMQLIGGTWYGGEMKKGMFSM
MNYLLPLKGILSMHCSANVGEKGDVALFFGLSGTGKTTLSTDPKRRLIGDDEHGWDDDGVFNFEGGCYAK
TIHLSEEKEPEIYNAIRRDALLENVVVREDGTVDFDDGSKTENTRVSYPIYHIDNIVKPVSAAGHATKVI
FLTADAFGVLPPVSKLTPEQTMYHFLSGFTAKLAGTERGITEPTPTFSACFGAAFLSLHPTQYAEVLVKR
MQAAGAQAYLVNTGWNGTGKRISIKDTRAIIDAILDGSLENAEMFTLPIFNLAIPTELPGVDTKILDPRN
TYASKEQWQEKAETLANLFVDNFKKYADTPAGAALVAAGPKL
>gnl|CDD|272970 TIGR00225, Tail-specific_protease, C-terminal peptidase (prc). A C-terminal peptidase with different substrates in different species including processing of D1 protein of the photosystem II reaction center in higher plants and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein in E.coli E.coli and H influenza have the most distal branch of the tree and their proteins have an N-terminal 200 amino acids that show no homology to other proteins in the database [Protein fate, Degradation of proteins, peptides, and glycopeptides, Protein fate, Protein modification and repair]
RYEYVKRVLDEKEEIYGAIKGMLASLNDPYTRYLSPETAKSFSETTSGSLEGIGIQVGMDDGKIVIVSPF
EGSPAEKAGIKPGDKIIKINGKSVAGMSLDDAVALIRGKKGTKVSLEILRAGKSKPLSFTLKRDRIELET
VKASVKKVGGHSVGYIRISSFSEHTAEDVAKALDKLEKKNAKGYILDLRGNPGGLLQSAVDISRLFITKG
PIVQTKDRNGSKRHYKANGRQKYNLPLVVLVNRGSASASEILAGALQDNGRATIVGEKTFGKGTVQQVRP
LNDGSGIKVTIAKYYTPNGGSIHKKGIEPDIVIEQPDYSKELEEKFELNALPED
>gnl|CDD|129330 TIGR00227, ribD_Cterm, riboflavin-specific deaminase C-terminal domain. Eubacterial riboflavin-specific deaminases have a zinc-binding domain recognized by the dCMP_cyt_deam model toward the N-terminus and this domain toward the C-terminus. Yeast HTP reductase, a riboflavin-biosynthetic enzyme, and several archaeal proteins believed related to riboflavin biosynthesis consist only of this domain and lack the dCMP_cyt_deam domain
GRPYVILKYAMSLDGKIATASGESSWITSEEARRDVHQLRAQSDAILVGSGTVLADDPRLTVRWVELDEL
RNPVRVVLDSRLRVPPTARLLNDDAPTWVATSEPADEEKVKELEDFGVEVLVLETKRVDLKKLMEILYEE
GIRSVMVEGGGTLNGSLLKEGLVDELIVYIAPKLLGGRDAPTLVDGEGFQKMADAPNLELKEIYQIGEDI
VLTAKL
>gnl|CDD|129331 TIGR00228, Crossover_junction_endodeoxyribonuclease_RuvC, crossover junction endodeoxyribonuclease RuvC. Endonuclease that resolves Holliday junction intermediates in genetic recombination. The active form of the protein is a dimer. Structure studies reveals that the catalytic center, comprised of four acidic residues, lies at the bottom of a cleft that fits a DNA duplex. The model hits a single Synechocystis PCC6803 protein at a score of 30, below the trusted cutoff, that appears orthologous and may act as authentic RuvC [DNA metabolism, DNA replication, recombination, and repair]
ILGIDPGSRVTGYGVIRQVGRQLSYLGSGCIRTKVDDLPSRLKLIYAGVTEIITQFQPNYFAIEQVFMAK
NADSALKLGQARGVAIVAAVNQELPVFEYAARQVKQTVVGIGSAEKSQVQHMVRRLLKLPANPQADAADA
LAIAITHAHVSQNALH
>gnl|CDD|272971 TIGR00229, Sensor_protein_FixL, PAS domain S-box. The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator [Regulatory functions, Small molecule interactions]
SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEG
EPEPVSEERRVRRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDITERKEAEEAL
>gnl|CDD|272972 TIGR00230, Sugar_fermentation_stimulation_protein_homolog, sugar fermentation stimulation protein. probable regulatory factor involved in maltose metabolism contains a putative DNA binding domain. Isolated as a gene which enabled E.coli strain MK2001 to use maltose [Energy metabolism, Sugars, Regulatory functions, Other]
MEFSEIPPLQRGTLIQRYKRFLADVEVDGRRLTAHCPNTGRMTGLATPGNTVWLSKSDNGKRKLPYTWEA
TQSDGAWVLVNTLLANRLTKEAILNESISELSGYSSLKREVKYGAERSRIDFLLQADSEPDCYVEVKSVT
LAEEELALFPDAPTERGQKHLRELESILAEGQRAVVLFAVLHSSITRFSPNREIDEEYAQLLRRAQQAGV
EVLPYKAEISAEGVLLKPSLPVVV
>gnl|CDD|272973 TIGR00231, GTP-binding_protein_placental_isoform, small GTP-binding protein domain. Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model [Unknown function, General]
DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGKTYKFNLLDTAGQEDYDAIRRL
YYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHADSGVPIILVGNKIDLKDADLKTHVASEFAKLNGE
PIIPLSAETGKNIDSAFKIVEA
>gnl|CDD|272974 TIGR00232, Transketolase_2, transketolase, bacterial and yeast. This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous [Energy metabolism, Pentose phosphate pathway]
KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSL
LHLTGYDLSIEDLKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEI
VDHYTYVFVGDGCLQEGISYEVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLE
VEDGHDLAAIDAAIEEAKASTDKPTLIEVKTTIGFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYNPF
EIPQEVYDHFKKTVKERGAKAEQEWNELFAAYKKKYPELAAEFTRRLSGELPADWDKQLPEFKVKLQALA
TRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDLHENPLGNYIHYGVREFAMGAIMNGIALHGG
FKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAIPNLSVWRPCDG
NETAAAWKYALESQDGPTALILSRQNLPQLEESSLEKVLKGGYVLKDSKGPDLILIATGSEVQLAVEAAK
KLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVTRLAIEAGAADEWYKYAGLVGAILGMDSFGESAP
GDKLFEEFGFTVENVVAKAKKLL
>gnl|CDD|272975 TIGR00233, Tryptophan--tRNA_ligase, tryptophanyl-tRNA synthetase. This model represents tryptophanyl-tRNA synthetase. Some members of the family have a pfam00458 domain amino-terminal to the region described by this model [Protein synthesis, tRNA aminoacylation]
KKFRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAITVKQTDPDALRKAREELAADYLAV
GLDPEKTFIFLQSDYPEHYELAWLLSCQVTFGELKRMTQFKDKSQAENVPIGLLSYPVLQAADILLYQAD
LVPVGIDQDQHLELTRDLAERFNKKFKNFFPKPESLISKFFPRLMGLSGKKMSKSDPNSAIFLTDTPKQI
KKKIRKAATDGGRVTLFEHREKPGVPNLLVIYQYLSFFLIDDDKLKEIYEAYKSGKLGYGECKKALIEVL
QEFLKEIQERRAEIAEEILDKILEPGAKKARETANKTLADVYKAMGL
>gnl|CDD|272976 TIGR00234, Tyrosine--tRNA_ligase, tyrosyl-tRNA synthetase. This tyrosyl-tRNA synthetase model starts picking up tryptophanyl-tRNA synthetases at scores of 0 and below. The proteins found by this model have a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples [Protein synthesis, tRNA aminoacylation]
MNNILLLLTKRGLEVQTPEEEKDLLKLLERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLL
GDFTALIGDPTGKSEVRKILTREEVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKIF
TVNRMLRRDAFSSRFEENISLHEFIYPLLQAYDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGL
TVPLLTPADGEKMGKSLGGAVSLDEGKYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVELKGPNPRE
VKENLALEITKYVHGPEAALAAEEISEAIFSGGLNPDEVPIFRPEKFGGPITLADLLVLSGLFPSKSEAR
RDIKNGGVYINGEKVEDLEPIRKELENN
>gnl|CDD|272977 TIGR00235, Uridine_kinase, uridine kinase. Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
MDKPKGIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDL
LYEHLKNLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRL
IRRIERDINERGRSLDSVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE
>gnl|CDD|272978 TIGR00236, UDP-N-acetylglucosamine_2-epimerase, UDP-N-acetylglucosamine 2-epimerase. This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine to UDP-N-acetyl-D-mannosamine. In E. coli, this is the first step in the pathway of enterobacterial common antigen biosynthesis.Members of this orthology group have many gene symbols, often reflecting the overall activity of the pathway and/or operon that includes it. Symbols include epsC (exopolysaccharide C) in Burkholderia solanacerum, cap8P (type 8 capsule P) in Staphylococcus aureus, and nfrC in an older designation based on the effects of deletion on phage N4 adsorption. Epimerase activity was also demonstrated in a bifunctional rat enzyme, for which the N-terminal domain appears to be orthologous. The set of proteins found above the suggested cutoff includes E. coli WecB in one of two deeply branched clusters and the rat UDP-N-acetylglucosamine 2-epimerase domain in the other [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
LKVMIVLGTRPEAIKMAPLIRALKKYPEIDSYVIVTAQHREMLDQVLDLFHLPPDYDLNIMSPGQTLGEI
TSNMLEGLEELLLEEKPDIVLVQGDTTTTLAGALAAFYLQIPVGHVEAGLRTGDRYSPMPEEINRQLTGH
IADLHFAPTEQAKDNLLRENVKADSIFVTGNTVIDALLTNVEIAYSSPVLSEFGEDKRMILLTLHRRENV
GEPLENIFKAIREIVEEFEDVQIVYPVHLNPVVREPLHKHLGDSKRVHLIEPLEYLDFLNLAANSHLILT
DSGGVQEEAPSLGKPVLVLRDTTERPETVEAGTNKLVGTDKENITKAAKRLLTDPDEYKKMSNASNPYGD
GEASERIVEELLNHY
>gnl|CDD|272979 TIGR00237, exodeoxyribonuclease_VII_large_subunit, exodeoxyribonuclease VII, large subunit. This family consist of exodeoxyribonuclease VII, large subunit XseA which catalyses exonucleolytic cleavage in either the 5'-_3' or 3'-_5' direction to yield 5'-phosphomononucleotides. Exonuclease VII consists of one large subunit and four small subunits [DNA metabolism, Degradation of DNA]
SVSELNRYIKELLERDFLPNVWVEGEISNLKRHSSGHLYFTLKDEKAQIRCVMFRSRARRLKFRPEEGMK
VLVRGRVSVYEPRGSYQLIVEDIEPAGLGELYLAFEQLKEKLAAEGLFDPERKKPLPRFPKRIGVITSPT
GAAIRDILNVLRRRWPLVEIVLYPALVQGEGAAASIIAAIERLNARGDVDVIIIGRGGGSIEDLWAFNDE
AVARAIAASPIPVISAVGHETDFTIADFVADLRAPTPTAAAELAVPDRAELLQRLDQLRERLRRALQRRL
ERERQRLDRLRSRLVLASPERLLERQRQRLDRLEQRLKRALRRRLERKRQRLELLAARLEALSPLATLKR
GYAIVRDEDGKVVRSAKQLKPGDELTIRLADGEIKARVK
>gnl|CDD|272980 TIGR00238, L-lysine_23-aminomutase, KamA family protein. This model represents essentially the whole of E. coli YjeK and of some of its apparent orthologs. YodO in Bacillus subtilis, a family member which is longer protein by an additional 100 residues, is characterized as a lysine 2,3-aminomutase with iron, sulphide and pyridoxal 5'-phosphate groups. The homolog MJ0634 from M. jannaschii is preceded by nearly 200 C-terminal residues. This family shows similarity to molybdenum cofactor biosynthesis protein MoaA and related proteins. Note that the E. coli homolog was expressed in E. coli and purified and found not to display display lysine 2,3-aminomutase activity. Active site residues are found in 100 residue extension in B. subtilis. Name changed to KamA family protein [Cellular processes, Adaptations to atypical conditions]
EIIEEFFGVTREEWFNWLWQLKNVVRDLKGLKKLLNISDEDLEEIERAAKKLIPLRVTPYYIDLMDKGNP
DDPVRRQVIPSSEEFVEAMGFSTDPLEEHDTSPVPGLTHRYVNRALFLVKGGCAVNCRYCFRRHFPYKEN
PGNKKKWQKALDYIAEHPEIIEILISGGDPLMAKDHELEWLLKRLEEIPHLVRLRIGTRLPVVIPQRITD
ELCELLASFELQLMLVTHINHCNEITEEFAEAMKKLRTVNVTLLNQSVLLRGVNDRAQILAKLSIALFKV
GIIPYYLHYLDKVQGAKHFLVPDAEAAQIVKELARLTSGYLVPKFAVEIMG
>gnl|CDD|161785 TIGR00239, 2-oxoglutarate_dehydrogenase_mitochondrial, 2-oxoglutarate dehydrogenase, E1 component. The 2-oxoglutarate dehydrogenase complex consists of this thiamine pyrophosphate-binding subunit (E1), dihydrolipoamide succinyltransferase (E2), and lipoamide dehydrogenase (E3). The E1 ortholog from Corynebacterium glutamicum is unusual in having an N-terminal extension that resembles the dihydrolipoamide succinyltransferase (E2) component of 2-oxoglutarate dehydrogenase [Energy metabolism, TCA cycle]
YLSGANQSYIEELYEDYLTDPDSVDASWRSTFDQLPGPGPAPDQFHSPTRSYFRRLAKDASRGSVTISDP
DTNVSQVKVLQLIRAYRFRGHLHANLDPLGLKQQDKVPELDLSFYGLTEADLQETFNIGSFVSGKDATMK
LSNLELLQALKQTYCGSIGAEYMHITSTEEKRWLQQRIESGERAQFNSEEKKRFLSRLTAAEGFERFLGA
KFPGAKRFSLEGLDALVPMLKEIIRHSVNSGTRDVVLGMAHRGRLNVLVNVLGKPPEDIFSEFAGKHKSH
LPDGTGDVKYHMGRFSSDFTTDGKLVHLALAFNPSHLEIVSPVVIGSTRARLDRLNDSPESTKVLAILIH
GDAAFAGQGVVQETLNMSKLRGYSVGGTIHIIINNQIGFTTNPLDARSTPYCSDLAKMIQAPIFHVNADD
PEAVAFATRLAVEYRNTFKRDVFIDLVGYRRHGHNEADEPSATQPLMYQKIKKHPTPRKVYADKLVSEGV
ATEEDVTEMVNLYRDALEAADCVVPSWREMNTASFTWSPELNHEWDEEYPNKVEMKRLQELAKRISEVPE
GVEMHSRVAKIYFDRTKAMAAGEKLFDWGGAENLAFATLVDDGIPVRLSGEDSERGTFFQRHAVLHDQSN
GSTYTPLQHLHNGQGAFRVWNSVLSEESVLGFEYGYATTSPRTLVIWEAQFGDFANGAQVVIDQFISSGE
QKWGQMSGLVMLLPHGYEGQGPEHSSGRLERFLQLAAEQNMQVCVPTTPAQVFHILRRQALRGMRRPLVV
MSPKSLLRHPLAVSSLEELAEGTFQPVIGEIEESGLSLDPEGVKRLVLCSGKVYYDLHEQRRKNGQKDVA
IVRIEQLYPFPHKAVKEVLQQYPNLKEIVWCQEEPLNMGAWYYSQPHLREVIPEGVSVRYAGRPASASPA
VGYMSLHQKQQQDLLNDAL
>gnl|CDD|272981 TIGR00240, Aspartate_carbamoyltransferase_regulatory_chain, aspartate carbamoyltransferase, regulatory subunit. The presence of this regulatory subunit allows feedback inhibition by CTP on aspartate carbamoyltransferase, the first step in the synthesis of CTP from aspartate. In many species, this regulatory subunit is not present. In Thermotoga maritima, the catalytic and regulatory subunits are encoded by a fused gene and the regulatory region has enough sequence differences to score below the trusted cutoff [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
MNELQVKKIKNGTVIDHIPAGKALKVLKILKLPEGTSRVTIAMNVPSSKMGKKDIVKIENTFLKEEEVDQ
IALIAPQATINIIRNYEVVEKSKPSLPEEIEGVLKCPNPNCISNAEPVSSKFYVRSEEPDIALRCYYCEK
EIEHNVVEAN
>gnl|CDD|129344 TIGR00241, Uncharacterized_protein_MJ0004, CoA-substrate-specific enzyme activase, putative. This domain is found in a set of closely related proteins including the (R)-2-hydroxyglutaryl-CoA dehydratase activase of Acidaminococcus fermentans, in longer proteins from M. jannaschii and M. thermoautotrophicum that share an additional N-terminal domain, in a protein described as a subunit of the benzoyl-CoA reductase of Rhodopseudomonas palustris, and in two repeats of an uncharacterized protein of Aquifex aeolicus.This domain may be involved in generating or regenerating the active sites of enzymes related to (R)-2-hydroxyglutaryl-CoA dehydratase and benzoyl-CoA reductase
ISLGIDSGSTTTKMVLMEDGKVIGYKWLDTTPVIEETARAILEALKEAGIGLEPIDKIVATGYGRHKVGF
ADKIVTEISCHGKGANYLAPEARGVIDIGGQDSKVIKIDDGKVDDFTMNDKCAAGTGRFLEVTARRLGVS
VEELGSLAEKADRKAKISSMCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQRLKIEAPIVFT
GGVSKNKGLVKALEKKLGMKVITPPEPQIVGAVGAALL
>gnl|CDD|129345 TIGR00242, Transcriptional_regulator_MraZ, division/cell wall cluster transcriptional repressor MraZ. Members of this family contain two tandem copies of a domain described by pfam02381. This protein often is found with other genes of the dcw (division cell wall) gene cluster, including mraW, ftsI, murE, murF, ftsW, murG, etc. Recent work shows MraW in E. coli binds an upstream region with three tandem GTGGG repeats separated by 5bp spacers. We find similar sites in other species [Cellular processes, Cell division, Regulatory functions, DNA interactions]
MFRGATNVTLDAKGRISVPAKYRAFLLESVVTNRGFENCLLLYPLQEWEKIEQKLNALPSTQKDTRRLQR
LIFGHATECEMDTAGRVLIANNLRNHAKLEKEIVLIGQFNKFEIWDKVLWEQYLAEDEDLETEVAERMKD
FS
>gnl|CDD|161787 TIGR00243, 1-deoxy-D-xylulose_5-phosphate_reductoisomerase, 1-deoxy-D-xylulose 5-phosphate reductoisomerase. 1-deoxy-D-xylulose 5-phosphate is converted to 2-C-methyl-D-erythritol 4-phosphate in the presence of NADPH. It is involved in the synthesis of isopentenyl diphosphate (IPP), a basic building block in isoprenoid, thiamin, and pyridoxal biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
MKQIVILGSTGSIGKSTLDVVRHNPDHFQVVALSAGKNVALMVEQILEFRPKFVAIDDEASLKDLKTMLQ
QQGSRTEVLVGEEGICEMAALEDVDQVMNAIVGAAGLLPTLAAIRAGKTIALANKESLVTAGHLFLDAVK
KYGVQLLPVDSEHNAIFQSLQHGLEELGVVSIILTASGGAFRDTPLEDLPTVTPQQALKHPNWSMGRKIT
IDSATMMNKGLEYIEARWLFGASAEQIDVLIHPQSIIHSMVEFQDGSVIAQLGEPDMRLPIAYAMAWPNR
VNSGVKPLDLCKLSALTFEEPDFDRYPCLKLAMEAFKAGQAATTVLNAANEVAVAAFLAQQIRFLDIAAL
ISKVLYRMQPRKPQSLEDVLEVDKNARETARKNVARVAS
>gnl|CDD|129347 TIGR00244, Transcriptional_repressor_NrdR, transcriptional regulator NrdR. Members of this almost entirely bacterial family contain an ATP cone domain (pfam03477). There is never more than one member per genome. Common gene symbols given include nrdR, ybaD, ribX and ytcG. The member from Streptomyces coelicolor is found upstream in the operon of the class II oxygen-independent ribonucleotide reductase gene nrdJ and was shown to repress nrdJ expression. Many members of this family are found near genes for riboflavin biosynthesis in Gram-negative bacteria, suggesting a role in that pathway. However, a phylogenetic profiling study associates members of this family with the presence of a palindromic signal with consensus acaCwAtATaTwGtgt, termed the NrdR-box, an upstream element for most operons for ribonucleotide reductase of all three classes in bacterial genomes [Regulatory functions, DNA interactions]
MHCPFCQHHNTRVLDSRLVEDGQSIRRRRECLECHERFTTFERAELLPPTVIKQDGVREPFNREKLLRGM
VRACEKRPVSFDDLEHAINHIEAQLRAQGEREVPSELIGQMVMQYLKKLDEVAYIRFASVYRSFQDIADF
VDELEQL
>gnl|CDD|272982 TIGR00245, UPF0014_membrane_protein_slr1647, TIGR00245 family protein [Hypothetical proteins, Conserved]
MDLISLTLALIFVIIAILLSYREKLGLEKDILWASIRAIIQLIIVGYVLLYIFSFDMPGAFLMLLMMLTI
AAVAAMNEINRSKNKTGLFWCSFIAFTTTTIVTLAVLIIPKVIKFEPIYVIPLMGMVIGNTMNTISLALN
RLISMVKSERDEIQGYLSLGATPKQAIAPFIRNAIKASLIPTVNSTKTVGLVSLPGMMTGQILAGADPIY
AAEYQILIMFMILSSAVLSTIIICYLTYREIFNAHQQL
>gnl|CDD|129349 TIGR00246, Ribosomal_RNA_large_subunit_methyltransferase_H, rRNA large subunit m3Psi methyltransferase RlmH. This protein, in the SPOUT methyltransferase family, previously designated YbeA in E. coli, was shown to be responsible for a further modification, a methylation, to a pseudouridine base in ribosomal large subunit RNA [Protein synthesis, tRNA and rRNA base modification]
KINLVAVGTKKPKWVKTGFEEYTRRFPKDAPFELIEIPAGKRGKNADIKRILDKEGDRILAAIGKAHVVT
LDIPGKPWTTPQLADTLEKWKTDGRDVTLLIGGPEGLSPTCKAAAEQSWSLSKLTLPHPLVRVIVAESLY
RAWSITTNHPYHR
>gnl|CDD|272983 TIGR00247, UPF0755_protein_HI_0457, conserved hypothetical protein, YceG family. This uncharacterized protein family, found in three of four microbial genomes, virtually always once per genome, includes YceG from Escherichia coli. This protein is encoded next to PabC, 4-amino-4-deoxychorismate lyase, in E. coli and numerous other proteobacteria, but that proximity is not conserved in other lineages. Numerous members of this family have been misannotated as aminodeoxychorismate lyase, apparently because of promiximty to PabC [Hypothetical proteins, Conserved]
MKKFLIIILLLFVLFFILGSILSYKIYFLNLSSLANKLVYEFNIEKGTGVSKIAKELKKQKLIKSEKLLQ
YLLKIKGSLKQFKAGTYLLNGDMTVFEILKLLLSGKENVQFDVTIPEGYTLRDIAKKLKEAPQVIDTLQD
FLFLINKKSTIYQLLELKNPLEGWLFPDTYKFTKGDTDLELLKRAFVKMFKAKLKAWGVRLSDLPSKELY
NLVIMASIVEKETRVKSERPKVASVFYNRLKSGMALQTDPTVIYGMGEEYNRSLPKRDLEIDSPYNTYIN
TGLPPTPIANAGISSLQAAAHPKKTDYLYFVAKGSGGHQFTSNLSSHNKAVQDYIKNFITKK
>gnl|CDD|129351 TIGR00249, Phosphohistidine_phosphatase_SixA_homolog, phosphohistidine phosphatase SixA [Regulatory functions, Protein interactions]
MQLFIMRHGDAALDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCLNLP
SSAEVLEGLTPCGDIGLVSDYLEALTNEGVASVLLVSHLPLVGYLVAELCPGENPIMFTTGAIASLLWDE
SKNGTLNWQMSP
>gnl|CDD|129352 TIGR00250, Putative_Holliday_junction_resolvase, putative transcription antitermination factor YqgF. This protein family, which exhibits an RNAse H fold in crystal structure, has been proposed as a putative Holliday junction resolvase, an alternate to RuvC [Unknown function, General]
LGLDFGTKSIGVAGQDITGWTAQGIPTIKAQDGEPDWSRIEELLKEWTPDKIVVGLPLNMDGTEGPLTER
AQKFANRLEGRFGVPVVLWDERLSTVEAESGLFARGGFRALRKGKIDKAAAVIILQSYLD
>gnl|CDD|129353 TIGR00251, UPF0235_protein_AF_2072, TIGR00251 family protein [Hypothetical proteins, Conserved]
VRENDDGLLIRIYVQPKASKDSIVGYNEWRKRVEVKIKAPPVEGKANRELIKFFGEIFGVDVEIVSGELS
RQKTIKIINPRDIPPEI
>gnl|CDD|129354 TIGR00252, UPF0102_protein_HI_1656, TIGR00252 family protein. the scores for Mycobacterium tuberculosis and Treponema pallidum are low considering the alignment [Hypothetical proteins, Conserved]
MFSLKTQLGQAGESQARAWLEQKGLKFIAANWNSPWGEIDLIMHDTKTIAFVEVRTRSGGNYGGALLSVN
ARKQEKILQTANLWLASQNPSWSDWNCRFDVMAFFPTGENAEWIFANLP
>gnl|CDD|129355 TIGR00253, Probable_RNA-binding_protein_MJ0652, putative RNA-binding protein, YhbY family. A combination of crystal structure, molecular modeling, and bioinformatic data together suggest that members of this family, including YhbY of E. coli, are RNA binding proteins [Unknown function, General]
LTGKQKRHLRGKAHHLKPVVLVGKNGLTEGVIKEIEQALEHRELIKVKVATEDREDKTLIAEALVKETGA
CNVQVIGKTIVLYRPTKERKIIELP
>gnl|CDD|272984 TIGR00254, Hypothetical_protein_yaiC., diguanylate cyclase (GGDEF) domain. The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein [Regulatory functions, Small molecule interactions, Signal transduction, Other]
QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSS
VRGSDVVGRYGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHGLTLE
ELLKRADEALYQAKKAGRNRVVVAD
>gnl|CDD|129357 TIGR00255, UPF0701_protein_HI_0467, TIGR00255 family protein. The apparent ortholog from Aquifex aeolicus as reported is split into two consecutive reading frames [Hypothetical proteins, Conserved]
MIRSMTGFARLEKKIDWGSASVELKSVNQRFLEFKFRLPEQFRGLELDLRELIRQYITRGKIECFLRVEY
KELVPSELFLNNPLAIEAISALRDSKAQTNIEGEINLGDFLRLPGVVIAQEQDLHQDAIYALILGALEEA
LLDFINMREFEGENLKSDIVQRLDLIEREVKKVRSAMPDILQWQRERLKARIEDLAQEFLDLNRLEQEAA
LLAQRIDIAEEIDRLDSHVKEFYNILKKGEAVGRKLDFMMQELNRESNTLASKAIDADITNLAVEMKVLI
EKIKEQIQNIE
>gnl|CDD|129358 TIGR00256, D-tyrosyl-tRNATyr_deacylase, D-tyrosyl-tRNA(Tyr) deacylase. This homodimeric enzyme appears able to cleave any D-amino acid (and glycine, which does not have distinct D/L forms) from charged tRNA. The name reflects characterization with respect to D-Tyr on tRNA(Tyr) as established in the literature, but substrate specificity seems much broader [Protein synthesis, tRNA aminoacylation]
MIALIQRVSQASVTVEGEVIGEIGAGLLVLLGVEKDDDEQKADKLAEKVLNYRIFSDSEGKMNLNVQQAG
GEILSVSQFTLAADTKKGMRPSFSKGASPDRAEELYEYFVELCREKGMKVQTGRFAADMQVSLTNDGPVT
FWLDV
>gnl|CDD|129359 TIGR00257, IMPACT_family_member_HI_0722, uncharacterized protein, YigZ family. This uncharacterized protein family includes YigZ, which has been crystallized, from E. coli. YigZ is homologous to the protein product of the mouse IMPACT gene. Crystallography shows a two-domain stucture, and the C-terminal domain is suggested to bind nucleic acids. The function is unknown. Note that the ortholog from E. coli was shown fused to the pepQ gene in GenBank entry X54687. This caused occasional misidentification of this protein as pepQ; this family is found in a number of species that lack pepQ [Unknown function, General]
MESYFVPKNAVTSKIEIKKSRFITYLAHTEGVDDAKKFIEKIKKEHPNATHHCVAFVIGAPDDIQQLGFS
DDGEPAGTAGKPMLSVLMGSGLGDITAVVVRYFGGILLGTGGLIKAYGKSVNEALNNITTEEKTELEILS
LQCDYHQLTGIEAELGKCQGEIINSNFSNNVLLRVALPTKEVAAFSEKLTEFSRGSLQLKAIEE
>gnl|CDD|272985 TIGR00258, Probable_non-canonical_purine_NTP_phosphatase, inosine/xanthosine triphosphatase [Purines, pyrimidines, nucleosides, and nucleotides, Other]
VGSTNPVKIEAILQAFEEIFGSVEIAGVEVESGVPEQPFGLEETVRGARNRAKNAFRLLECDFSVGIEAG
LDRVSTGYIDFQWCVIYDGEQRTEGRSAGFEYPKVVVEKVLEGEEVGPVMEEYTGIDEIGRKEGAIGYLT
AGKLTRTDLYRQSVIMALIPFMN
>gnl|CDD|129361 TIGR00259, Putative_sgc_region_protein_SgcQ, membrane complex biogenesis protein, BtpA family. Members of this family are found in C. elegans, Synechocystis sp., E. coli, and several of the Archaea. Members in Cyanobacteria have been shown to play a role in protein complex biogenesis, and designated BtpA (biogenesis of thylakoid protein). Homologs in non-photosynthetic species, where thylakoid intracytoplasmic membranes are lacking, are likely to act elsewhere in membrane protein biogenesis [Protein fate, Protein folding and stabilization]
EKPVIGMVHLLPLPGSPSFDDNLNAVIDKAWKDAMALEEGGVDAVMFENFFDAPFLKEVDPETVAAMAVI
AGQLKSDVSIPLGINVLRNDAVAALAIAMAVGAKFIRVNVLTGVYASDQGIIEGNAGELIRYKKLLGSEV
KILADIVVKHAVHLGNRDLESIALDTVERGLADAVILSGKTTGTEVDLELLKLAKETVKDTPVLAGSGVN
LENVEELLSIADGVIVATTIKKDGVFNNFVDQARVSQFVEKVAHGLK
>gnl|CDD|272986 TIGR00260, Threonine_synthase, threonine synthase. Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model [Amino acid biosynthesis, Aspartate family]
VWRYREFLPVTEKDLVDLGEGVTPLFRAPALAANVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGN
DTVLCASTGNTGAAAAAYAGKAGLKVVVLYPAGKISLGKLAQALGYNAEVVAIDGNFDDAQRLVKQLFED
KPALGLNSANSIPYRLEGQKTYAFEAVEQLGWEAPDKVVVPVPNSGNFGAIWKGFKEKKMLGLDSLPVKR
GIQAEGAADIVRAFLEGGQWEPIETPETLSTAMDIGNPANWPRALEAFRRSNGYAEDLSDEEILEAIKLL
AREEGYFVEPHSAVAVAALLKLVEKGTADPAERVVCALTGNGLKDPE
>gnl|CDD|129363 TIGR00261, traB, pheromone shutdown-related protein TraB. traB is a plasmid encoded gene that functions in the shutdown of the peptide sex pheromone cPD1 which is produced by the plasmid free recipient cell prior to conjugative transfer in Enterococcus faecalis. Once the recipient acquires the plasmid, production of cPD1 is shut down. The gene product may play another role in the other species in the family [Unknown function, General]
IHEKTIYILGTAHVSKKSSEEVANLIEILKPDYIAVELDERRYHSLLNTKWRNLDIDKVLKQGNAFFLII
NLILANFQKKLGEEQGIKPGSEMKTAIEKAKKHGIPLILIDRDIETTLKRAWISITFFEKAKIISSLFSS
TDAKIEDEIEKLLEQDALSKIMKELSKISPKVKKVLIDERDEFMANKLLEGEGNKNIIVAVVGAGHVSGI
MRTLKKLQNKNIINLEELEKVKKKHFSFSKVLSYLIAISIILLFVMISFYLNGFEFLYKNLKLWILSNGI
LSAIGSILARGHPLTILTAFLGAPITSLIPLIATGMVAGLVEAYIRKPTVKDFENLQEAESIKEYFKNKV
FRVLLVAILVNLGSTIGTIYGLKFLINVFG
>gnl|CDD|161792 TIGR00262, Tryptophan_synthase_alpha_chain, tryptophan synthase, alpha subunit. Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. The alpha chain is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria and plants each domain is found on a separate subunit (alpha and beta chains), while in fungi the two domains are fused together on a single multifunctional protein. The signature pattern for trpA contains three conserved acidic residues [LIVM]-E-[LIVM]-G-x(2)-[FYC]-[ST]-[DE]-[PA]-[LIVMY]-[AGLI]-[DE]-G and this is located between residues 43-58 of the model. The Sulfolobus solfataricus trpA is known to be quite divergent from other known trpA sequences [Amino acid biosynthesis, Aromatic amino acid family]
FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMT
PEKCFELLKKVRQKHPNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHG
VKPIFLVAPNADDERLKQIAEKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKP
EQVKQAIDAGADGVIVGSAIVKIIEENLNTPEKMLQALEEFVQNLK
>gnl|CDD|272987 TIGR00263, Tryptophan_synthase_beta_chain, tryptophan synthase, beta subunit. Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. the beta chain contains the functional domain for or the synthesis of tryptophan from indole and serine. The enzyme requires pyridoxal-phosphate as a cofactor. The pyridoxal-P attachment site is contained within the conserved region [LIVM]-x-H-x-G-[STA]-H-K-x-N] [K is the pyridoxal-P attachment site] which is present between residues 90-100 of the model [Amino acid biosynthesis, Aromatic amino acid family]
GYFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEALGGAKIYL
KREDLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPN
VFRMELLGAKVIPVTSGSGTLKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQ
ILEQEGRLPDAVIACVGGGSNAIGIFYAFIDDPSVQLIGVEAGGLGIDTHKHAATLSKGSPGVLHGMKTY
LLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHETGRATYEAITDDEALEAFKLLSRNEGIIPALESSHAL
AHLEKIAPTLPKDQIVVVNLSGRGDKDIFTIAKYL
>gnl|CDD|272988 TIGR00264, Nascent_polypeptide-associated_complex_protein, alpha-NAC-related protein. This hypothetical protein is found so far only in the Archaea. Its C-terminal domain of about 40 amino acids is homologous to the C-termini of the nascent polypeptide-associated complex alpha chain (alpha-NAC) and its yeast ortholog Egd2p and to the huntingtin-interacting protein HYPK. It shows weaker similarity, possibly through shared structural constraints rather than through homology, with the amino-terminal domain of elongation factor Ts. Alpha-NAC plays a role in preventing nascent polypeptides from binding inappropriately to membrane-targeting apparatus during translation, but is also active as a transcription regulator [Unknown function, General]
MFPGKMNPKMLKQMQKMMKQMGMEMEDLDVEEVIIVFDDEEWIFENPKVQVMDILGVKTYQITGKPKKEK
VEEEEEITEDDIELVMKQCNVSKEEARRALEECGGDLAEAIMKLEE
>gnl|CDD|272989 TIGR00266, TIGR00266, TIGR00266 family protein [Hypothetical proteins, Conserved]
MLYKIRHRPSYSMLELTLKPGERVLAETGAMVSMDGGVELSTECGGGLLGALKRSLGGESLFLNAFHAPQ
GPGSLQLAPALPGDITHLLLTKNGIYAQSGAFLAHTSGVEIDTKWGGLKTFFAGEGLFLLKLQGKGDVFL
SSYGTLNQLSVNGSFVVDTGHIVAFEPTLDYKVNKPVGGLKGDVLSGEGLVSLFKGSGKVYWQSRSLSSF
VGWLRSRLPSLR
>gnl|CDD|129368 TIGR00267, Uncharacterized_protein_MJ0645, TIGR00267 family protein. This family of uncharacterized proteins shows a low level of similarity (possibly meaningful) to the predicted membrane protein YLR220W, which is involved in calcium homeostatis. It shows no similarity to any other characterized protein.This family is represented in three of the first four completed archaeal genomes, with two members in A. fulgidus [Hypothetical proteins, Conserved]
RYVVRGTIDGTLSALGVVGGASGSVDNYVIILAGLGGGVANGMSNAFGAFTAERAEEEREMRELEKSMLM
DEGKLDDTIIYKQARRRVYMSGFIDGFSTFMGSFVPVLPFLVFDRMTATIVTVLLTLIALLVLGVYLGRI
SRENILISSLKMVVIGLLVAVVSLLIEGS
>gnl|CDD|129369 TIGR00268, Uncharacterized_protein_slr1717, TIGR00268 family protein. The N-terminal region of the model shows similarity to Argininosuccinate synthase proteins using PSI-blast and using the recognize protein identification server [Hypothetical proteins, Conserved]
KLENLRNFLKEFKKVLIAYSGGVDSSLLAAVCSDAGTEVLAITVVSPSISPRELEDAIIIAKEIGVNHEF
VKIDKMINPFRANVEERCYFCKKMVLSILVKEAEKRGYDVVVDGTNADDLFDHRPGYRAVKEFNGVSPWA
EFGITKKEIREIAKSLGISFPDKPSEACLASRFPFGREIDEEKLKMVDEAEEVLRNAGVGQVRVRNYDNL
AVIEVPEDELSKLLNEAEEVRDKFKDIGFRKVLIDLEGYRSG
>gnl|CDD|129370 TIGR00269, CTU1/ATPBD3_family_protein_MJ1157, TIGR00269 family protein [Hypothetical proteins, Conserved]
VPRIKPLRYIPEKEVVLYAFLNELKVHLDECPYSSLSVRARIRDFLYDLENKKPGVKFSVLRGFEKLIPL
LKELSEQEDLRRCERCGEPTSGRICKACKFLEEL
>gnl|CDD|129371 TIGR00270, TIGR00270, TIGR00270 family protein [Hypothetical proteins, Conserved]
MNCEICGRKIKGKGFKIVIEGSEMTVCGECRKFGKEIIKKPTVASQKGARKPVKRKRRKIDTTEELVEDY
GIIIRREREKRGWSQEQLAKKIQEKESLIKKIENAEIEPEPKVVEKLEKLLKIKLREQVPEIKIEKSGRK
SLGPTLGDFIKIKK
>gnl|CDD|129372 TIGR00271, Uncharacterized_protein_MJ0678, uncharacterized hydrophobic domain. This domain is in a family of archaeal proteins that includes AF0785 of Archaeoglobus fulgidus and in several eubacterial proteins, including the much longer protein sll1151 from Synechocystis PCC6803
STLSKTYIIFVILATIIAACGLVLDNAVLIIGAMIIAPLLGPIAGSAVGLVVGDVKLALRSAKNLLLAMA
FVIVFAMIMGLFHPSKLTVPQILSRTSPDFLSLIVAVLAGIAGSLSLTSGKSGSLVGVAISVSLLPPAAV
AGVALGIGDLLQSYSSLILLLINLVAIDVGGTIGL
>gnl|CDD|272990 TIGR00272, Diphthamide_biosynthesis_protein_2, diphthamide biosynthesis protein 2. This protein has been shown in Saccharomyces cerevisiae to be one of several required for the modification of a particular histidine residue of translation elongation factor 2 to diphthamide. This modified site can then become the target for ADP-ribosylation by diphtheria toxin [Protein fate, Protein modification and repair]
QSDVAFQKVPTHEIDESSYLGPCYNSDELEQDISAYYEIEPTVGYIKQGNEYQVALQFPDDLLKDSSKVV
RLLQSKFPHGKIKFWVLADTAYSSCCVDEVAAEHVHAEAVVHFGDACLSAIQNLPVVYVFGTPPIDLALV
VENFQRAFPDLSSKICLMADAPFSKHQSQLYNILKEVLPGDLHYTNIIYPQVNTSAVEEKFVTIGRTFHV
PEDVDQQEKNLVLFGQHSSEDLHLIHLTTYQDLSTVFQFVPIFDPILPESVTGPFPSLRRRYKLVHVARD
AGCIGIVVGTLGVRNTRETINELRKMIKTAGKKHYLFVVGKPNPAKLANFEDIDIFVLLGCSQSGIIDSN
EFYRPIVTPFELNLALSEEVTWVVDFRDSIDEIEQLLGGQDTISPSTTSDEAAPEFSLIRGKYTSTSRPL
RALTHLELEAADNDDSKQSTTRHTASGAVIKGTVSTSASALQNRSWKGLGDDVDSTEVDAKIEEGISGIA
RGYGGD
>gnl|CDD|129374 TIGR00273, Uncharacterized_electron_transport_protein_YkgF, iron-sulfur cluster-binding protein. Members of this family have a perfect 4Fe-4S binding motif C-x(2)-C-x(2)-C-x(3)-CP followed by either a perfect or imperfect (the first Cys replaced by Ser) second copy. Members probably bind two 4fe-4S iron-sulfur clusters [Energy metabolism, Electron transport]
IKDGILREALRNAQERLRANRKLLVEELGYWEEWRELVKEIKLKVLENLDFYLDQLKENVTQRGGHVYYA
KTAEEARKIIGKVAQEKNGKKVVKSKSMVSEEIGLNEVLEKIGIEVWETDLGELILQLDGDPPSHIVVPA
LHKNRQQIGEILKERLGYEGEESPEVLAREARKFMREKFLSADIGISGCNFAIAETGSIFLVENEGNGRL
STTLPKTHIAVMGIEKIVPTFDDELVLKSMLARSAVGTRLTAYINVLTGPRQEGDVDGPEEFHLILLDNG
RSNILATEFREVLACIRCGACQNECPVYRHIGGHWYGSIYPGPIGAVWSPLLGGYTDYKHLPYLSSLCGA
CREVCPVKIPLPELIREHRSDKVEKGRHSGMEKLAMKMFAKMASDGALWKFGLKMAQFFSPLGKLLAPIG
PVKEWASVRDLP
>gnl|CDD|272991 TIGR00274, N-acetylmuramic_acid_6-phosphate_etherase, N-acetylmuramic acid 6-phosphate etherase. This protein, MurQ, is involved in recycling components of the bacterial murein sacculus turned over during cell growth. The cell wall metabolite anhydro-N-acetylmuramic acid (anhMurNAc) is converted by a kinase, AnmK, to MurNAc-phosphate, then converted to N-acetylglucosamine-phosphate by this etherase, called MurQ. This family of proteins is similar to the C-terminal half of a number of vertebrate glucokinase regulator proteins and contains a Prosite pattern which is shared by this group of proteins in a region of local similarity [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGR
LGVLDASECPPTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTP
YVIAGLQYARSLGALTISIACNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIK
LGKVYENLMVDVQASNEKLKARAVRIVMQATDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLD
RHGGFLRQALD
>gnl|CDD|272992 TIGR00275, TIGR00275, flavoprotein, HI0933 family. The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae [Unknown function, Enzymes of unknown specificity]
IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIGKKLLISGGGRCNLTNSCPTPEFVAYYPRNGKFLRSAL
SRFSNKDLIDFFESLGLELKVEEDGRVFPCSDSAADVLDALLNELKELGVEILTNSKVKSIEKEDGGFGV
ETSGGEYEADKVIIATGGLSYPQLGSTGDGYEIAESLGHTIVPPVPALVPLTLDESFLKELSGISLDGVV
LSLVNGKKVLEEFGELLFTHFGLSGPAILDLSAFAARALLKHKGVELEIDLLPDLSEEELEQRLKRLRKS
NPKKTVKNILKGLLPKRLAELLLEQLGIDPDLPAAQLSKKEIKKLVQLLKNWPFTISGTRGFKEAEVTAG
GVSLKEINPKTMESKLVPGLYFAGEVLDIDGDTGGYNLQWAWSSGYLAGK
>gnl|CDD|272993 TIGR00276, iron-sulfur_cluster-binding_protein, epoxyqueuosine reductase. This model was rebuilt to exclude archaeal homologs, now that there is new information that bacterial members are epoxyqueuosine reductase, QueG, involved in queuosine biosynthesis for tRNA maturation [Protein synthesis, tRNA and rRNA base modification]
IKAWAKELGFDKIGITDADLFPEEKERLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDY
LPKLAPPAKSLKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERA
GLGWIGKHTLLINREAGSWFFLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISY
LTIELKGPIPEEFRPLIGNRIYGCDDCQLVCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLER
FGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALLDDPSPLVREHAAWALGQL
>gnl|CDD|272994 TIGR00277, Ribonuclease_Y, HDIG domain. This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits
YGQNVLQHSLEVAKLAEALARELGLDVELARRGALLHDIGKPITREGVIFESHVVVGAEIARKYGEPLEV
IDIIAEHHGK
>gnl|CDD|272995 TIGR00278, TIGR00278, putative membrane protein insertion efficiency factor. This model describes a family, YidD, of small, non-essential proteins now suggested to improve YidC-dependent inner membrane protein insertion. A related protein is found in the temperature phage HP1 of Haemophilus influenzae. Annotation of some members of this family as hemolysins appears to represent propagation from an unpublished GenBank submission, L36462, attributed to Aeromonas hydrophila but a close match to E. coli [Hypothetical proteins, Conserved]
LIALIRGYQIFISPFFPPSCRFYPTCSQYAIEALKTHGFLKGGWLTLKRILRCHPLHPGGNDPVPKKKQI
LESLK
>gnl|CDD|129380 TIGR00279, 50S_ribosomal_protein_L10e, ribosomal protein uL16(L10.e), eukarotic/archaeal form. This model finds the archaeal and eukaryotic forms of ribosomal protein uL16, previously L10.e. The protein is encoded by multiple loci in some eukaryotes and has been assigned a number of extra-ribosomal functions, some of which will require re-evaluation in the context of identification as a ribosomal protein. L10.e is distantly related to eubacterial ribosomal protein L16 [Protein synthesis, Ribosomal proteins: synthesis and modification]
MARRPARCYRYQKNRPYTRSEYIKGVPGSKIRIYDMGNKSAEFPVCVHLVAKEPEQIRHNALEAARIAAN
KYMTRRAGRMGYHLKIRVYPHHILRENKMATGAGADRIQQGMRGAFGKPVGTAARVKIGQKIFSVWTKPS
NFDVAKEALRRAAMKFPVPCKIVIEKGWELLK
>gnl|CDD|272996 TIGR00280, 50S_ribosomal_protein_L37Ae, ribosomal protein eL43. This model finds eukaryotic ribosomal protein eL43 (previously L37a) and its archaeal orthologs. The nomeclature is tricky because eukaryotes have proteins called both L37 and L37a [Protein synthesis, Ribosomal proteins: synthesis and modification]
MMKRTKKVGITGRFGPRYGLKLRRQVKKIEIQQKAKYVCPFCGKKTVKRGSTGIWTCRKCGAKFAGGAYT
PVTPAGKTVRKTIRRIVEMKEA
>gnl|CDD|213521 TIGR00281, Segregation_and_condensation_protein_B, segregation and condensation protein B. Shown to be required for chromosome segregation and condensation in B. subtilis [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
NLKAIIEALLFVSGEPGVTLAELVRILGKEKAEKLNAIMELLEDYLSRDTAGIEIIKFGQSYSLVTKPAF
ADYIHRFLPAKLKNLNSASLEVLAIIAYKQPITRARINEIRGVKSYQIVDDLVEKGLVVELGRKDTPGRS
FIYETTPKFYDYFGIDSLDELPKLEDFALKKFLQGEFFDSNRYGDD
>gnl|CDD|161802 TIGR00282, Uncharacterized_protein_MG246_homolog, metallophosphoesterase, MG_246/BB_0505 family. A member of this family from Mycoplasma Pneumoniae has been crystallized and described as a novel phosphatase [Unknown function, Enzymes of unknown specificity]
IKFLFIGDVYGKAGRKIVKNNLPQLKSKYQADLVIANGENTTHGKGLTLKIYEFLKQSGVNYITMGNHTW
FQKLILDVVINQKDLVRPLNFDTSFAGKGSLVFEFNGAKIAVTNLQGTSVNLPFKTTNPFKVLKELINML
KKDCDLIFVDFHAETTSEKNAFGMAFDGYVTAVVGTHTHVPTADLRILPKGTAYITDVGMTGPFGSVIGA
NPEQSIKLFCTGSPERFEVSECGTQLNGVFIEVDVKTKKAVKIERIRIVDDPRYLK
>gnl|CDD|161803 TIGR00283, Peptidyl-tRNA_hydrolase, peptidyl-tRNA hydrolase. This model describes an archaeal/eukaryotic form of peptidyl-tRNA hydrolase. Most bacterial forms are described by TIGR00447 [Protein synthesis, Other]
MKMVIVIRDDLGMGKGKIAAQVCHAAIIGFLKSKRKNPSLRRKWLDEGQKKVVLKVNSLEELLEIYHKAE
SLGLVTGLIRDAGHTQIPPGTITAVGIGPDEDEKIDKITGDLKLL
>gnl|CDD|272997 TIGR00284, Uncharacterized_protein_MJ0107, dihydropteroate synthase-related protein. This protein has been found so far only in the Archaea, and in particular in those archaea that lack a bacterial-type dihydropteroate synthase. The central region of this protein shows considerable homology to the amino-terminal half of dihydropteroate synthases, while the carboxyl-terminal region shows homology to the small, uncharacterized protein slr0651 of Synechocystis PCC6803 [Unknown function, General]
MKVLLITGRLAKGLIEGILKESDQEAEVIVLNVHVAGMLSTKTIAKILKSRRDLLERARSVDILLIPGLV
RGDAKVVEEVTGRPVFKGTVEAVDIPDIIEILRSGIKLSTEEPADEVVLEIKKLEEYTSKIEEREADFRI
GSLKIPLKPPPLRVVAEIPPTVAEDGIEGLAARMERDGADMVALGTGSFDDDPDVVKEKVKTALDALDSP
VIADTPTLDELYEALKAGASGVIMPDVENAVELASEKKLPEDAFVVVPGNQPTNYEELAKAVKKLRTSGY
SKVAADPSLSPPLLGLLESIIRFRRASRLLNVPLVFGAANVTELVDADSHGVNALLAAIALEAGASILYV
VEDSYKSYRSTAEAAEAAKMASAARKLNSLPKDIGTRLFVVKDKRRPPEPVEPPGERINVDYIEPSMDRT
GYAKIQVDHERGVIMLTFYPAGGEPVVTIEGKKPTSILRALIRRFPVSSLEHAGYIGYELAKAEIALALG
KTYVQDSPL
>gnl|CDD|129386 TIGR00285, DNA/RNA-binding_protein_Alba, DNA-binding protein Alba. Alba has been shown to bind DNA and affect DNA supercoiling in a temperature dependent manner. It is regulated by acetylation (alba = acetylation lowers binding affinity) by the Sir2 protein. Alba is proposed to play a role in establishment or maintenace of chromatin architecture and thereby in transcription repression. This protein appears so far only in the Archaea, but may be universal there. There is a single member in three of the first four completed archaeal genomes, and a second copy in A. fulgidus. In Sulfolobus shibatae there is a tandem second copy that is poorly conserved and scores below the trusted cutoff; all other members of the family are conserved at greater than 50 % pairwise identity [DNA metabolism, Chromosome-associated proteins]
ENVVYIGNKPVMNYVLAVLTQLNSGADEVIIKARGRAISRAVDVAEIVRNRFIPDIKIKKIKIGTEEIKS
EQGREVNVSTIEIVLAK
>gnl|CDD|211565 TIGR00286, TIGR00286, arginine decarboxylase, pyruvoyl-dependent. The three copies present in Archeoglobus fulgidus, one of which is only half-length and excluded from the seed alignment, are very closely related and clearly arose by duplication after the separation from well-studied species. The other completed archaeal genomes each contain a single copy. The lone, weak (below trusted cutoff) hit to a non-archaeal sequence is to an uncharacterized protein of Chlamydia, with the greatest similarity in the amino-terminal half of the model [Central intermediary metabolism, Polyamine biosynthesis, Energy metabolism, Amino acids and amines]
KLPNKVFFVSGVGEGETPLNAFDLALLDAGIGNVNLIRVSSIMPPECEIVELPKLPPGQIVFCVMSRMIS
NVPGETISAAVGVAIPKDKSLNGYIMEYSGKCSKEDAEKHAREMAKYMLKTRGWELARTFSITVEHTVEK
CGTAVAAAVFVI
>gnl|CDD|272998 TIGR00287, CRISPR-associated_endonuclease_Cas1, CRISPR-associated endonuclease Cas1. This model identifies CRISPR-associated protein Cas1, the most universal CRISPR system protein. CRISPR is an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, a system for heritable host defense by prokaryotic cells against phage and other foreign DNA. Cas1 is a metal-dependent DNA-specific endonuclease
TLYVLEYGSYLSRKGNTLVVEKEGKKKWNIPVANVDCIVLFGGVSISSAAIRLLAKRGIDIVFFGGDGNY
VGRLSPQESGSTVELRLAQVKAYLDEEKRLKLAKEFVSGKIANQAALLKYLTRRREDLRSYLEEYESLMK
ELASADSIEELMGIEGNAARAYYAALAQLLPDEFGFNGRSKRPPKDPFNALLSYGYSLLYSNVLTAIYIA
GLDPYIGFLHTDRSGRPSLVLDLMEEFKPQIVDRLVFSLINRNIITEEDFEKISNGVYLGEEGRKKFLQA
FEERLQTTVTHPGLNRRVSYLDIIILQARKLAKALRGEERYRP
>gnl|CDD|272999 TIGR00288, Uncharacterized_protein_MJ0482, TIGR00288 family protein. This family of orthologs is restricted to but universal among the completed archaeal genomes so far. Eubacterial proteins showing at least local homology include slr1870 from Synechocystis PCC6803 and two proteins from Aquifex aeolicusr, none of which is characterized [Hypothetical proteins, Conserved]
PTISKLQSLKEYISKKKKLSGERKIGLLVDGPNMLRKEFNINLDEIREILSEYGDIKIGKVFLNQYASDK
LIEAIENQGFEPIVTAGDVDVRMAVEAMELIYNPNIDAIALVTRDADFLPVIMKAKEMGKETIVIGAEPG
FSTALQNSADIAIVLNEEEE
>gnl|CDD|129390 TIGR00289, Uncharacterized_protein_MJ0570, TIGR00289 family protein. Homologous proteins related to MJ0570 of Methanococcus jannaschii include both the apparent orthologs found by this model above the trusted cutoff, the much longer protein YLR143W from Saccharomyces cerevisiae, and second homologous proteins from Archaeoglobus fulgidus and Pyrococcus horikoshii that appear to represent a second orthologous group [Hypothetical proteins, Conserved]
MKVAVLYSGGKDSILALYKALEEHEVISLVGVFSENEESYMFHSPNLHLTDLVAEAVGIPLIKLYTSGEE
EKEVEDLAGQLGELDVEALCIGAIESNYQKSRIDKVCRELGLKSIAPLWHADPEKLMYEVAEKFEVIIVS
VSAMGLDESWLGRRIDKECIDDLKRLNEKYGIHLAFEGGEAETLVLDAPLFKKRIEVDEIEKFWDGVRGY
CLIKRASLVDKT
>gnl|CDD|273000 TIGR00290, Uncharacterized_protein_MJ0570, MJ0570-related uncharacterized domain. Proteins with this uncharacterized domain include two apparent ortholog families in the Archaea, one of which is universal among the first four completed archaeal genomes, and YLR143W, a much longer protein from Saccharomyces cerevisiae. The domain comprises the full length of the archaeal proteins and the first third of the yeast protein
MKVAALISGGKDSCLALYHALKEHEVISLVNIMPENEESYMFHGVNAHLTDLQAESIGIPLIKLYTEGTE
EDEVEELKGILHTLDVEAVVFGAIYSEYQKTRIERVCRELGLKSFAPLWHRDPEKLMEEFVEEKFEARII
AVAAEGLDESWLGRRIDRKMIDELKKLNEKYGIHPAGEGGEFETLVLDAPIFKKRLEVKEIEKYWDGRNG
HLGIKRAALVSKS
>gnl|CDD|129392 TIGR00291, Ribosome_maturation_protein_SDO1_homolog, rRNA metabolism protein, SBDS family. This protein family, possibly universal in both archaea and eukaryotes, appears to be involved in (ribosomal) RNA metabolism. Mutations in the human ortholog are associated with Shwachman-Bodian-Diamond syndrome [Protein synthesis, Other]
MVSLENAVIARLKKHGERFEVLVDPYLAADLREGIEVDFEDVLAIEEVFRDASKGEKASEEDLRKIFGTT
DVDEVAEKIILKGEIQLTAEQRREMLEKKRNQIINIISRNTINPQTKKPHPPTRIEKALEEAKVHIDIFK
SVEEQVLEIVKALKQIIPIKFEKMKVAIKIPPERAGEAIEAISNFGAVTPEEWQEDGSWICVGEIPSGNY
RDLMTLLDKKTKGNVLTKVVK
>gnl|CDD|273001 TIGR00292, Putative_ribose_15-bisphosphate_isomerase, thiazole biosynthesis enzyme. This enzyme is involved in the biosynthesis of the thiamine precursor thiazole, and is repressed by thiamine. This family includes c-thi1, a Citrus gene induced during natural and ethylene induced fruit maturation and is highly homologous to plant and yeast thi genes involved in thiamine biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
ESKISRAIVERYFEDLLDYAESDVIIVGAGPSGLTAAYYLAKNGLKVCVLERSLAFGGGSWGGGMLFSKI
VVEKPAHEILDEFGIRYEDEGDGYVVADSAEFISTLASKALQAGAKIFNGTSVEDLITRDDTVGVAGVVI
NWSAIELAGLHVDPLTQRSRVVVDATGHDAEIVAVCAKKIVLEDQVPKLGGEKSMWAEVAEVAIHENTRE
VVPNLYVAGMAVAAVHGLPRMGPIFGGMLLSGKHVAEQILEKLK
>gnl|CDD|129394 TIGR00293, Prefoldin_subunit_alpha, prefoldin, archaeal alpha subunit/eukaryotic subunit 5. Members of this protein family, rich in coiled coil regions, are molecular chaperones in the class of the prefoldin (GimC) alpha subunit. Prefoldin is a hexamer of two alpha and four beta subunits. This protein appears universal in the archaea but is restricted to Aquifex aeolicus among bacteria so far. Eukaryotes have several related proteins; only prefoldin subunit 5, which appeared the most similar to archaeal prefoldin alpha, is included in this model. This model finds a set of small proteins from the Archaea and from Aquifex aeolicus that may represent two orthologous groups. The proteins are predicted to be mostly coiled coil, and the model may have a significant number of hits to proteins that contain coiled coil regions [Protein fate, Protein folding and stabilization]
LQQLAAELQILQQQVESLQAQIAALRALIAELETAIETLEDLKGAEGKETLVPVGAGSFVKAKVKDTDKV
LVSIGSGYYVEKDAEEAIEFLKKRIEELEKAIEKLQEALAELASRAQQLEQEAQQL
>gnl|CDD|129395 TIGR00294, GTP_cyclohydrolase_MptA, GTP cyclohydrolase, MptA/FolE2 family. This family includes type I GTP cyclohydrolases involved in methanopterin in archaea (MptA) and de novo tetrahydrofolate biosynthesis in bacteria (FolE2) [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
DVQTLLPKVPIRLTRVGVTGIKKLVPVEREGKRPIILISTFDVFVDLPSHQKGVHMSRNPEVITSVLEEA
EETTAANFEMLCNEIVNQLLKKHRYATLAEVYMNSDFILSKRSPKTGQFTQELAKIMGTASGTRDDDFIF
ERKMVGAEVVGITACPCAQELVKEKSQPFLQEAGFSDETIPKILDIVEFATHNQRGRGRIFTEVPSLPSI
VIADLIDIAESSMSAELHEILKRPDEKAVVETAHENPRFVEDCVRLMAARLVELFPHLPDDTEVECRQIN
EESIHRHNAFAEKVATFGELRDEIGSPD
>gnl|CDD|129396 TIGR00295, Uncharacterized_protein_MJ0778, TIGR00295 family protein. This set of orthologs is narrowly defined, comprising proteins found in three Archaea but not in Pyrococcus horikoshii. The closest homologs are other archaeal proteins that appear to be represent distinct orthologous clusters [Hypothetical proteins, Conserved]
VQRLLDKYKCDESVRRHCLAVARVAMELAENIRKKGHEVDMDLVLKGALLHDIGRARTHGFEHFVKGAEI
LRKEGVDEKIVRIAERHFGAGINAEEASKLGLPPKDYMPETLEEKIVAHADNLIMGVREVTIDEVIKKLE
ERLGKNHPSIERARKLKEELERLL
>gnl|CDD|273002 TIGR00296, Protein_MJ0810, uncharacterized protein, PH0010 family. Members of this functionally uncharacterized protein family have been crystallized from Pyrococcus Horikoshii, Methanosarcina Mazei, and Sulfolobus Tokodaii [Unknown function, General]
FALLSREEGSSAVRYARYAIESHLNGGKSSRLYPDLPIVFNEKRGVFITLKKKGNKHLRGCIGTPEPVMP
LIEAIEEAAISAATEDPRFPPVQLEELDDIKVEVSILTPPETIFVGGPKDYPFDIEIGRHGLIVEFGPKR
GLLLPQVAVEYGWDAEEFLANLCMKAGLPPDCFLTYGIEVYRFEGQIFEEFEPRGEVIEA
>gnl|CDD|213522 TIGR00297, Uncharacterized_membrane_protein_sll0875, TIGR00297 family protein [Hypothetical proteins, Conserved]
IFLWLSAVILCVFLLALAAYAPLLDPWGYGHAWIMGVIIILFAGFRGLLVILAFFFLGSAVTRYGQEEKK
AAGIAEKRSGQRGPKNVWGNGLTPALFALAIAFGPEWDLWLALGYVASVATALSDTMASEIGKAYGKNPR
LITTLQRVEPGTDGAISVEGTLAGFAGALAIALLGYLLGLISFKGILFSTLAAFAGTNLDSLLGATLERK
GYLTNEHVNLIATFLGAIIGIGIEATA
>gnl|CDD|273003 TIGR00298, 2-phosphosulfolactate_phosphatase, 2-phosphosulfolactate phosphatase. 2-phosphosulfolactate phosphatase catalyzes the sulfonation of phosphoenolpyruvate to form 2-phospho-3-sulfolactate, the second step in coenzyme M biosynthesis. Coenzyme M is the terminal methyl carrier in methanogenesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Energy metabolism, Methanogenesis]
CAIVIDVLRASTTITTALNLFDKVIPTNSIEEAMELKKENAIKAGERNGKKIEGFDVGNSPLEVLNYKTN
GDNLVLTTTNGTRVLESIKSDNILVGSINNAKAVAKKALEIADEEIELVMAGRKGNFAIEDFIGAGIIAK
YILKIANENITLELDELAKAAIILSKDDWKVKELILNSNSAEKLKNLGYEKDVEFCVLENIINNVGIYKN
NEIVKL
>gnl|CDD|129400 TIGR00299, TIGR00299, TIGR00299 family protein. Members of this family are found in the Archaea and in several different bacteria lineages. The function in unknown and the genomic context is not well conserved [Hypothetical proteins, Conserved]
VAYFDPFTGISGDMCLGALIDAGVPLEYLMEVLKPLGLTDEVRLSAGLVKKQGIAATKVEVKLLGPGHHG
MRHFKEILELIKSSNLPERVKRWALAIFHQLAIAEGKVHGVDPEEVHFHEVGATDAIADIVGAVLALDYL
NLIDQCYYTPVPVGSGFVRAAHGLLPVPAPAVLEILKGRQLPVYDNGLGGELVTPTGAAILVTLASQLGP
FPFNLKEVSYGAGSKDFPLPNILRLWRGTEITPHETITVLETNVDDISGEALGYLLESLLEQGALDVFTI
PIYMKKNRPGILLRVICAPENQEEVLNLLFRETGSLGVRIFQQHRYALEREWQTVKVPIGGIRIKVRYKV
GAGGKRILNAKPEFEDCAAIAKETGIPLQDVY
>gnl|CDD|129401 TIGR00300, TIGR00300, TIGR00300 family protein. All members of the family come from genome projects. A partial length search brings in two plant lysine-ketoglutarate reductase/saccharopine dehydrogenase bifunctional enzymes hitting the N-terminal region of the family [Hypothetical proteins, Conserved]
MESREIELEGHLIDSLILPKALDIILDMGGDFRVLEFNIGKRKNDPSYARILVSARDHQHLEEILTELID
LGAVIPEIEEVELETAPQDGVLPDDFYVTTNHPTFVRVGGEWVEVEGQRMDAAIVVTPNPPRARCKPIRE
IKKGDRVVVGVEGIRVIPPERPREGGTGVFEFMGSGVSSERPVETLIEQIAWEMYEIRDKGGKIGVVAGP
AVIHTGAAQALAHLIREGYVDALLAGNALAVHDIEQALYGTSLGVDIQRGIPVPGGHRHHLKAINSVRRA
GGIRDAVEQGIIKKGVMYECVKNNIPYVLAGSIRDDGPLPDVITDVVRAQSKMRELLQGADMVLMLSTML
HSIAVGNLLPSGVKTICVDINPAVVTKLSDRGSSQAVGVVTDVGLFLPLLVRQIKQL
>gnl|CDD|129402 TIGR00302, TIGR00302, phosphoribosylformylglycinamidine synthase, purS protein. In species such as Bacillus subtilis in which FGAM synthetase is split into two ORFs purL and purQ, this small protein, previously called yexA, is required for FGAM synthetase activity. Although the article does not make it clear whether this is a subunit or an accessory protein, it is encoded as part of the operon, which suggests stochiometric amounts, = subunit [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
YKVEVYIRLKKGVLDPEGAAIQRALALLGYNEVKDVRTGKVIELTIEADSEEAVEREVEEMCEKLLANPV
IHDYDIEIEE
>gnl|CDD|273004 TIGR00303, TIGR00303, TIGR00303 family protein. All current members of the family are from genome projects [Hypothetical proteins, Conserved]
LEKIKGRNPLFVCVIGSTETTLIPGITIAGAHPELIKYTPSADVELLFHGKSLTLPTPPITATGSPTPAT
ITKAAVELKNIPNLVIDAGAFVKPKIPYINIDEKPGGRIEEGRAMNNSEELYERGLLVGRQLSQLAELLI
VGESVPGGTTTALGVLLGLGYDAEGKVSSSMPHNPHELKRKVVREGGIEEKSSHNPFEVLNAVGDPMMPV
VAGIAIGSAENKPVILAGGTQMSAVLALIKAINKKVLDFSLIAIGTTKFVAEDATGDLKGIAEQIGPVPV
LASDPYFGKAKYPGLKNYEKGSVKEGVGAGGMAVYALVNGIEPEKIREFIE
>gnl|CDD|213523 TIGR00304, TIGR00304, TIGR00304 family protein. The member of this family from Pyrococcus horikoshii scores only 13.91 bits, largely because it is at least 15 residues shorter than other members of this family of small proteins and is penalized for not matching to the N-terminal section of the model. Cutoff scores are set so this hit is between noise and trusted cutoffs [Hypothetical proteins, Conserved]
IRSEILIPLGIILIVIGFLLTFLGGALTAGSESKDKGEVKYGGVVMIGPIPIVFGSSPNMAILSVLLAII
LMVVAYL
>gnl|CDD|129405 TIGR00305, TIGR00305, putative toxin-antitoxin system toxin component, PIN family. This uncharacterized protein family, part of the PIN domain superfamily, is restricted to bacteria and archaea. A comprehensive in silico study of toxin-antitoxin systems by Makarova, et al. (2009) finds evidence this family represents the toxin-like component of one class of type 2 toxin-antitoxin systems [Cellular processes, Other, Transcription, Degradation of RNA]
KVVIDTNVWISALIWKGLPGKLIKLIIDNKIVNCTSVEILQEVEFVLLYPKLQKYFALETILEILLLLGE
KSTIINPNPEFDDCRDKKDNKFLNTAYASKANALITGDTDLLVL
>gnl|CDD|273005 TIGR00306, apgM, phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form. Experimentally characterized in archaea as 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This model describes a set of proteins in the Archaea (two each in Methanococcus jannaschii, Methanobacterium thermoautotrophicum, and Archaeoglobus fulgidus) and in Aquifex aeolicus (1 member) [Energy metabolism, Glycolysis/gluconeogenesis]
VLIIIDGLADRPLEELDGKTPLQVAKTPNMDRLAEEGICGLMRTIKEGIRPGSDTAHLSILGYDPYEEYT
GRGPIEAAGVGVELKPGDVAFRCNLATVDEDFVIVDRRAGRISREEASKLIDELNRTELDGFVLFYSGTG
HRNLLVIRGPGLSDKVSDNDPKDIGKKVKAILPLAGSEEAKKTAELLNELMLESAEVLQNHPINTKRAKK
GKGPANMILPRGAGRMPRVESFKERYGLRGAMIAEVDLIKGLARLIGMDVIRVEGATGGIDTDYRGKVRA
LILALEEYDFVLVHTKGPDEAGHDGDPELKVRAIEKIDSKIVGPLLALDLDETRLILTADHSTPVEVKDH
SADPVPIVIVGPGVRVDEVKSFNEFACRKGALGRIRGEDLMDILLD
>gnl|CDD|129407 TIGR00307, 30S_ribosomal_protein_S8e, ribosomal protein eS8. Archaeal and eukaryotic ribosomal protein S8. This model could easily have been split into two models, one for eukaryotic S8 and one for archaeal S8; eukaryotic forms invariably have in insert of about 80 residues that archaeal forms of S8 do not [Protein synthesis, Ribosomal proteins: synthesis and modification]
MGIWQGRSRRKPTGGKYRQARKKRKYELGREPAETKIGERRIKKVRTRGGNKKVRLLRDETANVSDPETG
KVKKVEIAGVVENPANNHYVRRNVITKGAIVETDIGYARVTSRPGQDGVVNGVLIEE
>gnl|CDD|273006 TIGR00308, tRNA_guanine26-N2-dimethyltransferase, tRNA(guanine-26,N2-N2) methyltransferase. This enzyme is responsible for two methylations of a characteristic guanine of most tRNA molecules. The activity has been demonstrated for eukaryotic and archaeal proteins, which are active when expressed in E. coli, a species that lacks this enzyme. At least one Eubacterium, Aquifex aeolicus, has an ortholog, as do all completed archaeal genomes [Protein synthesis, tRNA and rRNA base modification]
VKEGKAEILVPKKETVFYNPRMQFNRDLSVTCIQAFDNLYGKECYINIADALSASGIRAIRYAHEIEGVR
EVFANDINPKAVESIKNNVEYNSVENIEVPNEDAANVLRYRNRKFHVIDIDPFGTPAPFVDSAIQASAER
GLLLVTATDTSALCGNYPKSCLRKYGANPVKTESCHESALRLLLGFVKRTAAKYEKALEPLLSHSIDHYV
RVYVKVKRSAIRADKVMESTGYTYHCSRCLHNKPVNGISQRKGRCKECGGEYHLAGPLYAGPLHDKEFIE
EVLRIAEEKEYGTRKRVLKMLSLIKNELSDPPGYYSPHHIASVLKLSVPPLKDVVAGLKSLGFEASRTHY
QPSGIKTDAPWDAIWEVLQKCDDE
>gnl|CDD|129409 TIGR00309, V-type_ATP_synthase_subunit_D, H(+)-transporting ATP synthase, vacuolar type, subunit D. Although this ATPase can run backwards, using a proton gradient to synthesize ATP, the primary biological role is to acidify some compartment, such as yeast vacuole (a lysosomal homolog) or the interior of a prokaryote [Transport and binding proteins, Cations and iron carrying compounds]
MEKVNPTRMELLKLKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSV
MGPFAVWIAALSVVTARFEVDMKSKNIMGVVVPVFDSYEIRRKVHERGYGLLFTSYKVDEAAEIYEEAVE
LIVELAEIETTIRLLAEEIEITKRRVNALEHVIIPRLKNTIKYINMRLDEMDRENFVRLKKIKSSKEKE
>gnl|CDD|273007 TIGR00310, Uncharacterized_ZPR1-like_protein_MJ0530, ZPR1 zinc finger domain. An orthologous protein found once in each of the completed archaeal genomes corresponds to a zinc finger-containing domain repeated as the N-terminal and C-terminal halves of the mouse protein ZPR1. ZPR1 is an experimentally proven zinc-binding protein that binds the tyrosine kinase domain of the epidermal growth factor receptor (EGFR); binding is inhibited by EGF stimulation and tyrosine phosphorylation, and activation by EGF is followed by some redistribution of ZPR1 to the nucleus. By analogy, other proteins with the ZPR1 zinc finger domain may be regulatory proteins that sense protein phosphorylation state and/or participate in signal transduction
IDCPSCGGECETVMKTVNDIPYFGEVLETSTICEHCGYRSNDVKTLGAKEPKRYILKIDDEADLNRRVVK
SESATIRIPELGLDIEPGPTSGGFITNLEGVLRRVEEELETAIRWQSEDEETKKRAEEILERLKEAIEGK
EKFTVILEDPLGGSYIQNVYAPKEILSEEEIEDLKTGKEINEDLGLSDEEVE
>gnl|CDD|129411 TIGR00311, Translation_initiation_factor_2_subunit_beta, translation initiation factor aIF-2, beta subunit, putative. The trusted cutoff is set high enough to select only archaeal members. The suggested cutoff is set to include most eukaryotic members but largely exclude the related eIF-5 [Protein synthesis, Translation factors]
DYEELLERAFEQLPDKVFVRERFEIPRVSIQIEGNRTIIKNFREIAKALNRDEDHLYKYLLKELGTAGNL
EGGRLILQGKFTESLLQKRIDDYVRLYVICRECNSPDTEIIKEGRVLLLKCLACGAKHPVRNI
>gnl|CDD|273008 TIGR00312, Cobalt-precorrin-5B_C1-methyltransferase, cobalamin biosynthesis protein CbiD. This protein has been shown by cloning into E. coli to be required for cobalamin biosynthesis. role_id [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
FACASAIAAVETLLTKGCPDSVVLELLEPGRTLEIAIEQGELLGGHRALAIVIKEPGNDLDLTRHTEIIA
EVEFTPGEGKLIIQGGEGVGIVTKPGLQVREGEAAINPYPRRMIRHNLQPYLSDDETLMVTLSLPLGRTL
ATRTSNPALGIVGGLSILGTTGIARPMSAEAYLASLACQIDTAAAQGHQCLVFVPGNIGLDLARQWGVPL
DDEIIKTANFLGSMLVAAAAVGVEEILLLGHAGKLIKLAGGIFHTHSHLADGRLEILAAQAVLAGLPYPL
VQEIGQAPTTEEGIKLLENCGWVSKVFNAIADTVDERSEERVYKLKVGSLIFDGDGPVLISTQGQKM
>gnl|CDD|129413 TIGR00313, Probable_cobyric_acid_synthase, cobyric acid synthase CobQ [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
IMVVGTTSSAGKSTLTAGLCRILARRGYRVAPFKSQNMSLNSFVTKEGGEIAIAQATQALAAGIEPSVHM
NPILLKPKGNFTSQVIVHGRAVGDMNYQEYYKNKVDFFLKAIKESLEILAREYDYVVIEGAGSPAEINLL
KRDLANMRIAELANADAILVADIDRGGVFASIYGTLKLLPENWRKLIKGIVINKFRGNVDVLKSGIEKLE
ELTGIPVLGVLPYDENLFPEEDSLVIQERRSRGNAKSIRIGVVRLPRISNFTDFEPLRYEAFVKFLDLDD
SLTGCDAVIIPGSKSTIADLYALKQSGFAEEILDFAKEGGIVIGICGGYQMLGKELIDKEKKESDVGDIE
GLGLLDAKTYFGEDKITKQSQGRVEGNNRGETVKGYEIHEGFTRSKEKPLFKIERFGNCGNDGNAWGTYL
HGLFENYEFRRYIINLLRKRKGPLEIYGGNYKDQREKSLDYLADVVERSVNLKPL
>gnl|CDD|129414 TIGR00314, cdhA, CO dehydrogenase/acetyl-CoA synthase complex, epsilon subunit. Acetyl-CoA decarbonylase/synthase (ACDS) is a multienzyme complex. Carbon monoxide dehydrogenase is a synonym. The ACDS complex carries out an unusual reaction involving the reversible cleavage and synthesis of acetyl-CoA in methanogens. The model contains the prosite signature for 4Fe-4S ferredoxins [C-x(2)-C-x(2)-C-x(3)-C-[PEG]] between residues 448-462 of the model [Energy metabolism, Chemoautotrophy]
ELKKGALFVDDMKNVSISIGEIVEEEEEEWEPMGPTPMPGILTLRKWDFKLLERYEPFYAPMCDMCCLCT
MGKCDLSMNKRGACGIDLKTQQARIVTIACCIGASAHTGHARHLVDHLIEELGEDYPIDLGGEVDVEAPI
TRTVTGIKPKTLGDLREALDYAEEQIVHVLSATHTGQEGSYLDYESKALHAGMADDLGREVADIAQIVAY
NFPKGEEDAPLVELGFGIIDKSKPVILVIGHNVMPGRPIADYLEENGMEDEVELCGICCTAIDMTRYNAK
AKIVGPLSRQLRVIRAGVADVIIVDEQCIRADILEECKKMGIPLIATNDKACLGLPDVSDEDPDKIVDYL
LSGNLPGALLLDPEKVGEVAVEVAEAIAKKRGDERKFLPDDEELMELANKCTQCGNCVRTCPNSLRVDEA
MAHAQKGDLSKLEQLEEQCYACGRCEQACPKNIPIISMITKAGEDRLKNEKGKTRAGRGPIQDVEIRKVG
APIVFGDIPGVIAAVGCSNYPNGMKDVAEIAKEFLERNYIVVTTGCHAMDIGMYKDEEGKTLYEKYPGNF
DAGGLVNTGSCVANAHIAGAAIKIANIFAKRPLRGNYAEIADYILNRVGAVGVAWGAYSQKAASIATGFN
RLGIPVVVGPHGSKYRRAYLGRPWKKEKWKVYDIKTGEKVFIEPAPEHLLVAAETKEEAIVMIAKLCIRP
NDTPQGRQIKLTHYIDLHQKYLGRMPDDWAVFVRTEADLPLKMKDQLLKVLEEKYGWKIDWDKKKIVEGP
VRHFDAGFNPTILE
>gnl|CDD|273009 TIGR00315, cdhB, CO dehydrogenase/acetyl-CoA synthase complex, epsilon subunit. Nomenclature follows the description for Methanosarcina thermophila. The complex is also found in Archaeoglobus fulgidus, not considered a methanogen, but is otherwise generally associated with methanogenesis [Energy metabolism, Chemoautotrophy]
FDPANIPGPKMATLVEPKPVANMIKKAKRPLLIVGPDLTEDEMFERVVKFIEKDIPVVATASAITRLIEA
GIGEKSEYAVLHEITQFLLDPDWKGFDGQGNYDLVLFLGSIYYYLSQMLSSLKHFAPHIRTLAIDKYYHP
NADMSFPNLWKEELYLKYLDEILAE
>gnl|CDD|129416 TIGR00316, cdhC, CO dehydrogenase/CO-methylating acetyl-CoA synthase complex, beta subunit. Nomenclature follows the description for Methanosarcina thermophila. The CO-methylating acetyl-CoA synthase is considered the defining enzyme of the Wood-Ljungdahl pathway, used for acetate catabolism by sulfate reducing bacteria but for acetate biosynthesis by acetogenic bacteria such as oorella thermoacetica (f. Clostridium thermoaceticum) [Energy metabolism, Chemoautotrophy]
MEADIPVDVSPMNEGERIRGPDMYVELAGPKSYGFELVKVVDKVEDMKVEIIGPDIDEMEEGQRYPFAII
VEVAGSNLEEDLEGVIERRIHEFLNYIEGVMHLNQRDQIWIRINKNAFNKGLRLKHIGKAVMMLFKEEFP
FIEKIEVTIITDPDKVKEELEKAREIYEKRDERTKALSDEDVDVFYGCVMCQSFAPTHVCIVTPDRPSLC
GAINWFDARAAAKIDPNGPIFEIPKGECLDPKLGEYSGVNEVVRERSQGTVERVKLHSAFEYPHTSCGCF
EAIVFYIPEVDGIGIVHRGYRGETPNGLPFSTMAGQCSGGKQVPGFVGISISYMRSPKFLQADGGWERVV
WMPKELKERVKDAIPEDLRDKIATEEDAKTTDELRKFLKEKGHPVVKRVVREVDEEEIEEEEEAMQPEEM
EMEGFEVPALQMPAASAAPAGIKIVLKNAKITIEKVII
>gnl|CDD|213524 TIGR00317, Adenosylcobinamide-GDP_ribazoletransferase, cobalamin 5'-phosphate synthase/cobalamin synthase. cobS is involved with cobalamin biosynthesis in part III of colbalmin biosynthesis. The enzyme catyalzes the reactions adenosylcobinamide-GDP + alpha-ribazole-5'-P = adenosylcobalamin-5'-phosphate + GMP and adenosylcobinamide-GDP + alpha-ribazole = adenosylcobalamin + GMP. The protein product is associated with a large complex of proteins and is induced by cobinamide [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
MGKLLRAAISFLTRLPVPGSWVDFERIARNIWLFPLVGILIGLASGIPGHILSAVLDNLLLAVVLYLFIE
GLTGGHHLDGLADFGDGLFAPGSKERKLEAMKDSYTGTGGVVALIVVVLLKILALSSLSQRGLASYALIG
AVCAKRSMLLLATASRPREEGTGRYFIEKARSRFTMIGVILGLPAVLALAGVPWLGLAALASAILIGLLV
GRYAKRHFGGVTGDVLGASNELGEVVSLLGL
>gnl|CDD|273010 TIGR00318, Putative_adenylate_cyclase_MJ0240, adenylyl cyclase CyaB, putative. The protein CyaB from Aeromonas hydrophila is a second adenylyl cyclase from that species, as demonstrated by complementation in E. coli and by assay of the enzymatic properties of purified recombinant protein. It has no detectable homology to any other protein of known function, and has several unusual properties, including an optimal temperature of 65 degrees and an optimal pH of 9.5. A cluster of uncharaterized archaeal homologs may be orthologous and serve (under certain circumstances) to produce the regulatory metabolite cyclic AMP (cAMP) [Regulatory functions, Small molecule interactions]
MIEVEVKAKIPDKEKVVEKLKNKGFKFIKKEFQHDIYFSNPCRDFASTDEALRIRKLTGEKFVTYKGPKI
DNESKTRKEIEFKIEDIENALQILKKLGFKKVYEVIKKRRIYQTNELNVSIDDVEGLGFFLEIEKIINNI
NDKDLALEEIFEIINQLGIKDNIERRSYLELLSL
>gnl|CDD|200008 TIGR00319, Desulfoferrodoxin_homolog, desulfoferrodoxin FeS4 iron-binding domain. This domain is found as essentially the full length of desulforedoxin, a 37-residue homodimeric non-heme iron protein. It is also found as the N-terminal domain of desulfoferrodoxin (rbo), a homodimeric non-heme iron protein with 2 Fe atoms per monomer in different oxidation states.This domain binds the ferric rather than the ferrous Fe of desulfoferrodoxin.Neelaredoxin, a monomeric blue non-heme iron protein, lacks this domain [Energy metabolism, Electron transport]
TNEGQVYKCEVCGNIVEVLHAGGGQLVCCGEPM
>gnl|CDD|273011 TIGR00320, Desulfoferrodoxin_homolog, desulfoferrodoxin. The short N-terminal domain contains four conserved Cys for binding of a ferric iron atom, and is homologous to the small protein desulforedoxin; this domain may also be responsible for dimerization. The remainder of the molecule binds a ferrous iron atom and is similar to neelaredoxin, a monomeric blue non-heme iron protein. The homolog from Treponema pallidum scores between the trusted cutoff for orthology and the noise cutoff. Although essentially a full length homolog, it lacks three of the four Cys residues in the N-terminal domain; the domain may have lost ferric binding ability but may have some conserved structural role such as dimerization, or some new function. This protein is described in some articles as rubredoxin oxidoreductase (rbo), and its gene shares an operon with the rubredoxin gene in Desulfovibrio vulgaris Hildenborough [Energy metabolism, Electron transport]
MPERLQVYKCEVCGNIVEVLNAGIGQLVCCNQPMKLMSENTTDAAKEKHVPVIEKTGNGYKVKVGSVAHP
MEEKHYIQWIELIADDKVYRKFLKPGDAPEAEFLIMADKVVAREYCNIHGHWKAE
>gnl|CDD|273012 TIGR00321, Probable_deoxyhypusine_synthase_1, deoxyhypusine synthase. Deoxyhypusine synthase is responsible for the first step in creating hypusine. Hypusine is a modified amino acid found in eukaryotes and in archaea in their respective forms of initiation factor 5A. Its presence is confirmed in archaeal genera Pyrococcus (), Sulfolobus, Halobacterium, and Haloferax (), but in an older report was not detected in Methanococcus voltae (J Biol Chem 1987 Dec 5;262(34):16585-9). This family of apparent orthologs has an unusual UPGMA difference tree, in which the members from the archaea M. jannaschii and P. horikoshii cluster with the known eukaryotic deoxyhypusine synthases. Separated by a fairly deep branch, although still strongly related, is a small cluster of proteins from Methanobacterium thermoautotrophicum and Archeoglobus fulgidus, the latter of which has two [Protein fate, Protein modification and repair]
KVMGPQISSGITVCELIDSMGRTGFQGRRIGEADKIWKEMCFDEEITIFMGYAGNLVPSGMREIIAYLIQ
HGMIDALVTTGANLEHDLIEALGPTHLGDFAVDDKKLREEGINRIGDVFVPNENFEVFEEWLVEIFSEML
GEQPIITPSEFIDEIGKRINDKRSSIRYAAYKRKIPIFCPALTDSSIGLMLFFYTKKNSLRIDIVRDIRK
LNDIVFNSERTGVIILGGGLPKHFILNACLLREGADYAVQITTDQPQDGSLSGAPLEEAVSWGKIKAKAK
SVTVFGDATIALPVLVAGLLA
>gnl|CDD|273013 TIGR00322, diphthamide_biosynthesis_protein_predicted, diphthamide biosynthesis enzyme Dph1/Dph2 domain. Archaea and Eukaryotes, but not Eubacteria, share the property of having a covalently modified residue, 2'-[3-carboxamido-3-(trimethylammonio)propyl]histidine, as a part of a cytosolic protein. The modified His, termed diphthamide, is part of translation elongation factor EF-2 and is the site for ADP-ribosylation by diphtheria toxin. This model includes both Dph1 and Dph2 from Saccharomyces cerevisiae, although only Dph2 is found in the Archaea (see TIGR03682). Dph2 has been shown to act analogously to the radical SAM (rSAM) family (pfam04055), with 4Fe-4S-assisted cleavage of S-adenosylmethionine to create a free radical, but a different organic radical than in rSAM
YNFEIDKTIEEIKKRGAKRVALQFPDGLLPDAVEVADILEKKPGAEVYILGDTTYGACCVDDVAAKHLGA
DLIIHYGHSCLSPITSRIPVLYVFVEIKIDVEHLVEALKENFPDKGKRIALVTTVQYAHALDEVKKILEE
AGYEPVIIPQGKPRTLSPGQVLGCTFPALRNDQDDAIIFIGDGRFHLLGLALATPKPKVYVYDPYSGELT
EEEYDANKLLRRRYALIEKAKDAKTVGIIVGTLGGQGRLELAERLKELLKKAGKKSYLISVGEINPAKLA
NFPEIDAFVQVACPRLSIDDGKDFYKPVLTPYELEMAL
>gnl|CDD|211569 TIGR00323, Translation_initiation_factor_6, translation initiation factor eIF-6, putative. This model finds translation initiation factor eIF-6 of eukaryotes, which is a ribosome dissociation factor. It also finds a set of apparent archaeal orthologs, slightly shorter proteins not yet shown to act as initiation factors; these probably should be designated as translation initiation factor aIF-6, putative [Protein synthesis, Translation factors]
RTQFSGNPEIGVYAKVTEEYALVPVNGSENFYSAFEEELEVPVLHTTIAGSSLVGALTVGNSRGLLVSDQ
VLDHELDSLPDSLVKVQRIEERLTALGNLILCNDYGALASPELDRDTEELISDVLGVEVFRGTIAGLITV
GSYAVVTNRGGLVHPQTSVQEQEELSSLLGVELVAGTVNRGTTVVGACMVANSKGAVVGLDTTGPELSII
EEALGL
>gnl|CDD|129424 TIGR00324, tRNA-splicing_endonuclease, tRNA-intron lyase. The enzyme catalyses the endonucleolytic cleavage of pre tRNA at the 5' and 3' splice sites to release the intron and produces two half tRNA molecules bearing 5' hydroxyl and 2', 3'-cyclic phosphate termini. The genes are homologous in Eucarya and Archea. The two yeast genes have been functionally studied (see MEDLINE; 97344075) and are two subunits of a heterotetramer enzyme in yeast the other two subunits of which have no known homologs [Transcription, RNA processing]
EIQGKLKGDEVIVKKKTIISDLTTREEYGNLDGDSLNLSLIESLYLIDLGKLRLIRSDSEPLSREELSDL
ARKVERGFMRKYLVYKDLRDRGYVVKTGFKFGADFRLYERGPLRDHSHSEYLVAIDDHDESIDLIDLSSG
VRVAHGVKKKLVIAYVDEEKEIHYLSIEWV
>gnl|CDD|273014 TIGR00325, UDP-3-O-_N-acetylglucosamine_deacetylase, UDP-3-0-acyl N-acetylglucosamine deacetylase. UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc deacetylase from E. coli, LpxC, was previously designated EnvA. This enzyme is involved in lipid-A precursor biosynthesis. It is essential for cell viability [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
IKQRTIKRSVQVTGVGLHSGVKVTLTLRPAPANTGVVFYRTDLNPPVDFPADPKSVRDTMLCTCLGNEGA
RISTVEHLLAALAALGIDNLVIEVNAPEIPIMDGSALPFVYLLLDAGIDELNAAKKFIRIKQTVRVEDGD
KFVEFKPYNGFSLDFTIDFNHPAIGKQRYAMNFSADAFMRQIARARTFGFMRDIEYLRSRGLCKGGSLDN
AIVLDDYRILNEDGLRFEDEFVRHKMLDAIGDLFMLGHNIIGAFTAYKSSHKLNNKLLQAILAKQEAWEY
VTFQDDAELPLAFKAPS
>gnl|CDD|273015 TIGR00326, eubact_ribD, riboflavin biosynthesis protein RibD. This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]
MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCS
HQGRTPPCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGL
PYVQLKLAASLDGKIATASGESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATEQPL
RVVLDTQLRIPEFAKLIPQIAPTWIFTTARDKKKRLEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEG
GPNLLGSFLDEGLVDELIIYIAPKLLGGTHAPGLCSEPGFQKMADALNFKFLEINQIGPDILLT
>gnl|CDD|273016 TIGR00327, Protein_translocase_subunit_SecE, protein translocase SEC61 complex gamma subunit, archaeal and eukaryotic. This model describes archaeal SEC61-like and eukaryotic SEC61 but not bacterial secE proteins, for which a Pfam pfam00584 (SecE) has been created [Protein fate, Protein and peptide secretion and trafficking]
KLIEAPVEFIKEGTRVLAVCKKPDLEEYLKVAKVTGIGIIIVGIIGYIIKIIAIPIRGVLK
>gnl|CDD|129428 TIGR00328, Flagellar_biosynthetic_protein_FlhB, flagellar biosynthetic protein FlhB. FlhB and its functionally equivalent orthologs, from among a larger superfamily of proteins involved in type III protein export systems, are specifically involved in flagellar protein export. The seed members are restricted and the trusted cutoff is set high such that the proteins gathered by this model play roles specifically related to flagellar structures. Full-length homologs scoring below the trusted cutoff are involved in peptide export but not necessarily in the creation of flagella [Cellular processes, Chemotaxis and motility]
EKTEEPTPKKLRKAREEGNVPKSREVNSAAVLLAGVLSLLFFGDGLADLLVVLMSFFLSFETSDILNLGS
LVGIFFQSIREVLLLLLPIFVLLLVVGVLSNIAQFGFLFTTKPLKPKFSKINPIKGLKRLFSLQSLVELL
KSLLKVFLVSFVAYFVLRNSLGELLSLSLYSLVQAITNFLDIAKSLLILVLLLLLVIAVFDYFFQRWQYI
KSLKMTKQEVKDELKQSEGDPEVKGRIRQMQREAARRRMMQEVPKADVVITNPTHYAVALKYDPGKMPAP
VVVAKGVDELALKIKEIARENNVPIVENPPLARALYRQVEIGQEIPPELYKAVAEVLAYVYKLKKKR
>gnl|CDD|129429 TIGR00329, tRNA_N6-adenosine_threonylcarbamoyltransferase, metallohydrolase, glycoprotease/Kae1 family. This subfamily includes the well-studied secreted O-sialoglycoprotein endopeptidase (glycoprotease, EC 3.4.24.57) of Pasteurella haemolytica, a pathogen. A member from Riemerella anatipestifer, associated with cohemolysin activity, likewise is exported without benefit of a classical signal peptide and shows glycoprotease activity on the test substrate glycophorin. However, archaeal members of this subfamily show unrelated activities as demonstrated in Pyrococcus abyssi: DNA binding, iron binding, apurinic endonuclease activity, genomic association with a kinase domain, and no glycoprotease activity. This family thus pulls together a set of proteins as a homology group that appears to be near-universal in life, yet heterogeneous in assayed function between bacteria and archaea [Protein fate, Degradation of proteins, peptides, and glycopeptides]
LGIETSCDDTGVAIVDEEGNVLANIKISQIPLHAKYGGVVPEEASRHHAENIPPLLERALIESNVDKSEI
DLIAVTRGPGLGGSLRVGATFARSLALALNKPLIGVNHLLGHIYIPRLDTNIPQFPFVSLLVSGGHTQII
LVKGIGDYEVLGETLDDAVGEAFDKVARLLGLGYPGGPKIEELAKKGDALPFYFPLPYTVKPMLDFSFSG
LKTAARRKIEKLGKNLNEATKEDIAYSFQETAFDHLIEKTKRALKDTNPKELVLVGGVSANKRLREKLET
LCQELNVEFYYPPLEFCSDNGAMIA
>gnl|CDD|129430 TIGR00330, Fructose-16-bisphosphatase_class_2, fructose-1,6-bisphosphatase, class II. This model represents GlpX, one of three classes of bacterial fructose-1,6-bisphosphatases. This form is homodimeric and Mn2+-dependent, and only very distantly related to the class I fructose-1,6-bisphosphatase, the product of the fbp gene, which is homotetrameric and Mg2+-dependent. A third class is found as one of two types in Bacillus subtilis. In E. coli, GlpX is found in the glpFKX operon together with a glycerol update protein and glycerol kinase [Energy metabolism, Pentose phosphate pathway]
RRSLAIEFSRVTEAAALAAYKWLGRGDKNTADGAAVNAMRIMLNQVNMDGTIVIGEGEIDEAPMLYIGEK
VGTGRGPAVDIAVDPIEGTRMTAMGQSNALAVLAVGDKGTFLNAPDMYMEKLVVGPGAKGTIDLNLPLAD
NLRNVAKALGKPLSDLTVTILAKPRHDAVIAEMQQLGVRVFAIPDGDVAASILTCMPDSEVDVLYGIGGA
PEGVVSAAAIRALGGDMQGRLLPRHDVKGDNEENRRIAEQEIARCKAMGVDVNKVLRLEDLVRGDNVIFS
ATGITKGDLLKGISRKGNIATTETLLIRGKSRTIRRIQSIH
>gnl|CDD|273017 TIGR00331, Heat-inducible_transcription_repressor_HrcA, heat shock gene repressor HrcA. HrcA represses the class I heat shock operons groE and dnaK; overproduction prevents induction of these operons by heat shock while deletion allows constitutive expression even at low temperatures. In Bacillus subtilis, hrcA is the first gene of the dnaK operon and so is itself a heat shock gene [Regulatory functions, DNA interactions]
TERQRKILKAIVEEYIKTGQPVGSKTLLEKYNLGLSSATIRNDMADLEDLGFIEKPHTSSGRIPTDKGYR
YYVDHLLKVDSLTEEEKRRIQNQFLQRRFYLEKVLQLAASLLSELTNYTAVVLGPRLSQDKLKHIELIPL
DPNLALAVIVTDSGRVKNKVIELPANISQEDLERAVNILNDRLRGRTLSEIREQIIELLSQLKIEIEEFE
DELVDLIISIFSEFNEEELYVDGKSNLLEQPEFFDPIERIRELLELLESKKFLELLLNEALHEPGVTVKI
GDENGDKSLEDFSVISSPYKIGGNPIGAIGVIGPKRMDYQRVIPLVNYIARLLSELL
>gnl|CDD|273018 TIGR00332, Putative_superoxide_reductase, desulfoferrodoxin ferrous iron-binding domain. This domain comprises essentially the full length of neelaredoxin, a monomeric, blue, non-heme iron protein of Desulfovibrio gigas said to bind two iron atoms per monomer with identical spectral properties. Neelaredoxin was shown recently to have significant superoxide dismutase activity. This domain is also found (in a form in which the distance between the motifs H[HWYF]IXW and CN[IL]HGXW is somewhat shorter) as the C-terminal domain of desulfoferrodoxin, which is said to bind a single ferrous iron atom.The N-terminal domain of desulfoferrodoxin is described in a separate model, dfx_rbo (TIGR00320) [Energy metabolism, Electron transport]
QTTDWGKEKHVPVIEVLRREGGVVYVKVSVGKEIPHPMEENHHIAWIELIFGDEVSRKPLVPGDAPFAEF
ASVDGPNKVEMSGKLTARSYCNIHGLWMYEATLSLE
>gnl|CDD|188042 TIGR00333, Protein_NrdI, ribonucleoside-diphosphate reductase 2, operon protein nrdI. Ribonucleotide reductases (RNRs) are enzymes that provide the precursors of DNA synthesis. The three characterized classes of RNRs differ by their metal cofactor and their stable organic radical. The exact function of nrdI within the ribonucleotide reductases has not yet been fully characterised [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
VYFSSKSGNTQRFIEKLGFQHIRIPVDETDRIHVDQPYVLICPTYTGGGTAGAVPKQVISFLNKKHNRAL
LRGVIASGNKNFGDNFGLAGDVISRKLNVPLLYKFELSGTKNDVEEVQKIVTNFFQK
>gnl|CDD|273019 TIGR00334, Ribonuclease_M5, ribonuclease M5. This family of orthologous proteins shows a weak but significant similarity to the central region of the DnaG-type DNA primase. The region of similarity is termed the Toprim (topoisomerase-primase) domain and is also shared by RecR, OLD family nucleases, and type IA and II topoisomerases [Transcription, RNA processing]
KIKEIIVVEGKDDQARIKQAFDVDVIETNGSALKDETINLIKKAQKKQGVIILTDPDFPGEKIRKKIEQH
LPGYENCFIPKHLAKPNKKKIGVEEASVEAIIAALENVHEETKAQQSDISWEDLLELGLIGPASKCKRLR
LCNLLKLGYFNHKQLFKRLNLFQIKKSDVMSALK
>gnl|CDD|273020 TIGR00335, DNA_primase_small_subunit_PriS, DNA primase, eukaryotic-type, small subunit, putative. Archaeal members differ substantially from eukaryotic members and should be considered putative pending experimental evidence. The protein is universal and single copy among completed archaeal and eukarotic genomes to date. DNA primase creates RNA primers needed for DNA replication.This model is named putative because the assignment is putative for archaeal proteins. Eukaryotic proteins scoring above the trusted cutoff can be considered authentic [DNA metabolism, DNA replication, recombination, and repair]
METKLYYKEKYNFYYSKNELELPRKFNREFAFREFGLLPDFVMHRHRYESFFRERILKNVPAKIYPSSAY
YSRAYEDKPEKRGWLGKGLIRDELAFDIDVKDQSFEKAECDGKQVCLEEAKLLAVLRADTGLRDFGLYDS
GGVFSGVRGYHEEVLDLGSRELREIVRYERLRYPKIVRVEKRFLNSNAVKRVLNRLLLKALEEEILTSKL
KILPNDLRKWKLIKEVIFKSEKKDYSALEIYIDKIVLDDKVTLDRIRLLRHPKSLHRVTGVICIESFNPE
KFAPLKGAEAIFVVKVE
>gnl|CDD|129436 TIGR00336, Orotate_phosphoribosyltransferase, orotate phosphoribosyltransferase. Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
ELLLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLEFDVIAGPALGGIPIAT
AVSVKLAKPGGDIPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAG
VIIAVDRQERSAGQEFEKEYGLPVISLITLKDL
>gnl|CDD|273021 TIGR00337, CTP_synthase, CTP synthase. CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7) [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLD
LGHYERFLDTNLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKISGPDVVIVE
IGGTVGDIESLPFLEAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIIC
RSSRPLDPNTKDKIALFCDVEEEAVISAKDVSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLV
EKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLDTKVNIKWIDSEDLEEEGVEFLKGLDGILVP
GGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQK
DISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQIENKGLIVSGTSPDGRLVEI
IELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA
>gnl|CDD|273022 TIGR00338, Phosphoserine_phosphatase, phosphoserine phosphatase SerB. Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins [Amino acid biosynthesis, Serine family]
DIAHSELSPLLRSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDFKASLRERVALLK
GLPVELLKEVRENLPLTEGAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDAAFANRLEVEDGKLT
GLVEGPIVDASYKGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKADICINKK
DLTDILPLL
>gnl|CDD|273023 TIGR00339, Sulfate_adenylyltransferase, ATP sulphurylase. This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free sulfate, the first step in the formation of the activated sulfate donor 3'-phosphoadenylylsulfate (PAPS). In some cases, it is found in a bifunctional protein in which the other domain, APS kinase, catalyzes the second and final step, the phosphorylation of APS to PAPS; the combined ATP sulfurylase/APS kinase may be called PAPS synthase. Members of this family also include the dissimilatory sulfate adenylyltransferase (sat) of the sulfate reducer Archaeoglobus fulgidus [Central intermediary metabolism, Sulfur metabolism]
PHGGKLVELVVRDPDEEHKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVESMRLS
DGVLFSVPITLDIDDEDADDIKLGDRIALTDPKGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVY
LNTAGNYYIGGPIEVINLPKFYDFPRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL
PNAGVLVHPLVGLTKPGDIPAEVRMRAYEVLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGA
THFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKYKAELGIKIVPFRHVAYCPDEDEYAPADQAGHTNLRT
LNISGTKLRGMLRNGVFPPEWFSRPEVVKILRE
>gnl|CDD|129440 TIGR00340, zpr1_rel, ZPR1-related zinc finger protein. This model describes a strictly archaeal family homologous to the domain duplicated in the eukaryotic zinc-binding protein ZPR1. ZPR1 was shown experimentally to bind approximately two moles of zinc; each copy of the domain contains a putative zinc finger of the form CXXCX(25)CXXC. ZPR1 binds the tyrosine kinase domain of epidermal growth factor receptor, but is displaced by receptor activation and autophosphorylation after which it redistributes in part to the nucleus. The proteins described by this model by analogy may be suggested to play a role in signal transduction. A model ZPR1_znf (TIGR00310) has been created to describe the domain shared by this protein and ZPR1 [Unknown function, General]
CPVCGSRTLKAVTYDYDIPYFGKIMLSTYICEKCGYRSTDVYQLEEKEPVRYIIKIENEDDLFTLVYRSR
SATIRIPELGIKIEPGPASQGYISNIEGVLERIEEVLDTASDDDEDDEAVKKCEEILKRIREVIEGKFKF
TLIIEDPFGNSFIESEKAITEKL
>gnl|CDD|273024 TIGR00341, Uncharacterized_protein_MJ0678, TIGR00341 family protein. This conserved hypothetical protein is found so far only in three archaeal genomes and in Streptomyces coelicolor. It shares a hydrophobic uncharacterized domain (see TIGR00271) of about 180 residues with several eubacterial proteins, including the much longer protein sll1151 of Synechocystis PCC6803 [Hypothetical proteins, Conserved]
GRHRTNDCLIPKEGVVMRKEIVRGEDLEEIAIELGDKTFIYDDRIELYVQDSDTEKIVSRLKDKLLGYKE
SIIVVYKPEFVISPASRREEAEEKTSLPVEELYEMAKSYASLNKGRSVVTILAGIIALSGLIMNNAVILI
GAMIIAPLLGPIHGFAVNLSVGDVKLAFRSAKNLLFDLFLVIVFSTIFAMMIGLVQLTPQILSRTEVSPV
SEILAVLAGIAGILSLSSGILESLAGVAISASLLPPAVATGILLVISPLPLAVKSLILTLINVAGLMAGS
LAGVYVYGIRAYRYYKKKVARKYLARSLIALTLLLIALLFLSILA
>gnl|CDD|273025 TIGR00342, Probable_tRNA_sulfurtransferase, tRNA sulfurtransferase ThiI. Members of this protein family are "ThiI", a sulfurtransferase involved in 4-thiouridine modification of tRNA. This protein often is bifunctional, with genetically separable activities, where the C-terminal rhodanese-like domain (residues 385 to 482 in E. coli ThiI), a domain not included in this model, is sufficient to synthesize the thiazole moiety of thiamine (see TIGR04271). Note that ThiI, because of its role in tRNA modification, may occur in species (such as Mycoplasma genitalium) that lack de novo thiamine biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine, Protein synthesis, tRNA and rRNA base modification]
ILARYGEIGIKGKNRLRFEKILKKNIKKALKKYEILRAVVYHFDRIVVIAIDKEQRDALLDLLTKIPGIV
SFSPAFKCDLPFDEIHILLKALKQLRKEGKTFKVRTKRRGKDFPLNSVEVNKYVGGGIVEKIGLKVDLTN
PDITVHIEIREDEFLIITERYEGIGGLPVGTQGKVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFNEPAA
SEKAREKVERLANSLNETGGSVKLYVFDFTDVQEEIIHIIPEGYTCVLCRRMMYKAASKVAEKEGCLAIV
TGESLGQVASQTLENLRVIQAVSNTPILRPLIGMDKEEIIELAKEIGTYEISIEPHEDCCTIFKPKHPTT
KAKPEKVEKLEEKLDFSRKLV
>gnl|CDD|129443 TIGR00343, Pyridoxal_biosynthesis_lyase_PdxS, pyridoxal 5'-phosphate synthase, synthase subunit Pdx1. This protein had been believed to be a singlet oxygen resistance protein. Subsequent work showed that it is a protein of pyridoxine (vitamin B6) biosynthesis, and that pyridoxine quenches the highly toxic singlet form of oxygen produced by light in the presence of certain chemicals [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPV
MAKVRIGHFVEAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRT
KGEAGTGNIVEAVRHMRKINEEIRQIQNMLEEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVAT
PADAALMMQLGADGVFVGSGIFKSSNPEKLAKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAE
RLQERGW
>gnl|CDD|273026 TIGR00344, Alanine--tRNA_ligase, alanine--tRNA ligase. The model describes alanine--tRNA ligase. This enzyme catalyzes the reaction (tRNAala + L-alanine + ATP = L-alanyl-tRNAala + pyrophosphate + AMP) [Protein synthesis, tRNA aminoacylation]
EIRQTFLDFFKEKGHQVIPSAPLVPRNDPTLLLTNAGMAQFKPIFTGIVKPPSNRLTNAQPCIRLNDLEN
VGRTARHHTLFEMLGNFSFGDYFKEEAIAFAWELLTEVLGLDKERLYVTVYEDDEEAYKIWEKIGIPADR
IIKCDAKDNFWDMGDGPCGPCTEIYYDFVGGKPGEPLEENDRYLEVWNLVFMQFNRDPDGNYTPLPKKNI
DTGMGLERFVAVLQGVPTNYDTDIFLPLIEKIEEITGVKYDSNNAGIMDEKRVEDLRSLRVIADHTRAIA
FMLADGVVPSNEGRGYVLRRLIRRALRHGKKLGLKEAFLYKLVPTLIEVLGDYYPELKEKQEFVEQILEL
EEERFAKTLERGLRLFEKLLKKTGKKELDGEDAFKLYDTYGFPVELTKEIAEERGLTVDMPGFEALMAEQ
RERSKQNSQFQEQEIALVNVYPATEFLGYDDLEFEAKVIGLFDDGYLVEQALAGQSVYVILDQTPFYAES
GGQIGDTGYLIANDGKFRVVDVQKPNGVVFHFGEVEGGSLKVGDKVIAVIDEKRRFRIMRNHSATHLLHA
ALQKVLGNHVWQAGSLVSFKKLRFDFSHFRALTREELEEIEDLANEQILANIPIKVIFMDLDEAKRKGAF
ALFGEKYVPGEKVRVVSVGDFSVELCGGTHVRNTGEIGLFKIVKESGIAAGVRRIEAVTGEAAIEYLNEQ
EDKLKELADILKVTPNELPKKVERFFEEWKALQKELESLKLKIADQKIDELKDKAETINGVKVLVEVVDA
KDMKSLKTMADRLKSKLGSAIYVLASFAEGKVKLVCGVSNDVLTKKIKAGELINQIAQVLGGKGGGRPDF
AQGGG
>gnl|CDD|273027 TIGR00345, Putative_arsenical_pump-driving_ATPase, transport-energizing ATPase, TRC40/GET3/ArsA family. Members of this family are ATPases that energize transport, although with different partner proteins for different functions. Recent findings show that TRC40 (GET3 in yeast) in involved in the insertion of tail-anchored membrane proteins in eukaryotes. A similar function is expected for members of this family in archaea. However, the earliest discovery of a function for this protein family is ArsA, an arsenic resistance protein that partners with ArsB (see pfam02040) for As(III) efflux [Hypothetical proteins, Conserved]
ISAATAIRLAEQGKKVLLVSTDPAHSLSDVFEQEIGHTPTKVTGVENLSAVEIDPQAALEEYRAKLVEQI
KGNLPDGDMLGDQLEGAALSPGIDEIAAFDEFLKHMTDAENEFDVVIFDTAPTGHTLRLLQLPEVLSSFL
EKFIKIRSKLGPMAKLFMGAGEDDEALEKLEELKEQIEAAREILSDPERTSFVLVVIPEKMSLYESERAH
KELAKYGIKVDAVIVNQVLPENAQDEFCQARWELQQKYLKQIPEKFADLPVAEVPLQKEEMVGLEALKRL
SKTL
>gnl|CDD|129446 TIGR00346, Uncharacterized_membrane_protein_HI_1738, 4-azaleucine resistance probable transporter AzlC. Overexpression of this gene results in resistance to a leucine analog, 4-azaleucine. The protein has 5 potential transmembrane motifs. It has been inferred, but not experimentally demonstrated, to be part of a branched-chain amino acid transport system. Commonly found in association with azlD [Transport and binding proteins, Amino acids, peptides and amines]
AFKDAFPYTIPILAGFLFLGIAYGILMVQLGFDYKYPLFMSLFIYAGSVEFVAATLLSAQFSPMNVLIVT
LMVNARQTFYGISMLDKYKNTGKKLPYLIHALTDESFSLNYLAAPPEGVDKGWFMFFVSLLNHSYWVFGA
AVGSLFGSHFSFNTQGMEFVMTALFIVIFMEQWKKTKNHKSALLGLGIAVVCLALFGTEYFLIPALVLIV
LALTLFRKQLE
>gnl|CDD|129447 TIGR00347, ATP-dependent_dethiobiotin_synthetase_BioD, dethiobiotin synthase. Dethiobiotin synthase is involved in biotin biosynthesis and catalyses the reaction (CO2 + 7,8-diaminononanoate + ATP = dethiobiotin + phosphate + ADP). The enzyme binds ATP (see motif in first 12 residues of the SEED alignment) and requires magnesium as a co-factor [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
FVTGTDTGVGKTVASSALAAKLKKAGYSVGYYKPVQTGIEKTNSDALLLQNISGTALDWDEVNPYAFALP
LSPHIAADQEGRPIDLEELSKHLRTLEQKYDFVLVEGAGGLCVPITEEYTTADLIKLLQLPVILVVRVKL
GTINHTLLTVEHARQTGLTLAGVILN
>gnl|CDD|273028 TIGR00348, R_protein, type I site-specific deoxyribonuclease, HsdR family. This gene is part of the type I restriction and modification system which is composed of three polypeptides R (restriction endonuclease), M (modification) and S (specificity). This group of enzymes recognize specific short DNA sequences and have an absolute requirement for ATP (or dATP) and S-adenosyl-L-methionine. They also catalyse the reactions of EC 2.1.1.72 and EC 2.1.1.73, with similar site specificity.(J. Mol. Biol. 271 (3), 342-348 (1997)). Members of this family are assumed to differ from each other in DNA site specificity [DNA metabolism, Restriction/modification]
EEEVEDLFIQRLKSLGWEYLKGSELNVEENEKQELIEALKIINDHIEPERWDEVYKKITNKGDLYETNKI
FYDYIKNGVKIKESQKGEKKRIVKLIDFRNISQNIFQFANQVSFKGHNIRPDVTLFVNGIPLVIIELKKR
SVTIREAFNQIKRYEKEIPELFKYVQIFVISNGTDTRYYTGSDEDDFDFTFNWKESDNKLIEDLKEFDIL
LLKKERLLDFIRNFIIFDKDTGLVTKPYQRYMQYRAVKKIVESITRKTWGKDERGGLIWHTQGSGKTLTM
LFAARKALELLKNPKVFFVVDRRELDYQLMKEFQSLQKDCAERIESIAELKELLEKDDGGIIITTIQKFD
DKLKEEEEKFPVDRKEVVVIFDEAHRSQYGELAKNLKKALKNASFFGFTGTPIFKKDRDTSLTFAYVFGR
YLHRYFITDAIRDGLTVKIDYEDRLPEDHLDKKKLDAFFDEIFELLPERIREITKESLKEKLQKTKKILF
NEDRLESIAKDIAEHYAKFKELFKFKAMVVAISRYACVEEKNALDEELNEKFEASAIVMTGKESDDAEIR
DYNKHIRTKFDKSDGFEIYYKDLERFKKNENPKLLIVVDMLLTGFDAPILNTLYLDKPLKYHGLLQAIAR
TNRIDGKDKTFGLIVDYRGLEKSLIDALSLYGNEAIK
>gnl|CDD|273029 TIGR00350, Transcriptional_regulator_LytR, cell envelope-related function transcriptional attenuator common domain. This model describes a domain of unknown function that is found in the predicted extracellular domain of a number of putative membrane-bound proteins. One of these is proteins psr, described as a penicillin binding protein 5 (PDP-5) synthesis repressor. Another is Bacillus subtilis LytR, described as a transcriptional attenuator of itself and the LytABC operon, where LytC is N-acetylmuramoyl-L-alanine amidase. A third is CpsA, a putative regulatory protein involved in exocellular polysaccharide biosynthesis. Besides the region of strong similarily represented by this model, these proteins share the property of having a short putative N-terminal cytoplasmic domain and transmembrane domain forming a signal-anchor [Regulatory functions, Other]
GRSDTLMVVTLDPKRKTAVVVSIPRDTRVTIPGCRTPASETKINSAYSFGGPQCLVKTVENLLGVPIDRY
VEVDFDGFEDVVDALGGVDVTVPFDFDDDESGTLLLKAGEHHLDGEEALAYLRMRKGDGRGDYGRIDRQQ
QVLSALLRRMKS
>gnl|CDD|273030 TIGR00351, Respiratory_nitrate_reductase_2_gamma_chain., respiratory nitrate reductase, gamma subunit. Involved in anerobic respiration the gene product catalyzes the reaction (reduced acceptor + NO3- = Acceptor + nitrite). Another possible role_id for this gene product is in nitrogen fixation (Role_id:160) [Energy metabolism, Anaerobic]
QFLNMFFFDIYPYIAGTVFLIGSWLRYDYGQYTWRAASSQMLDKKGMNLASNLFHIGILGIFVGHFFGML
TPHWMYAAWLPIEVKQKMAMFAGGASGVLCLIGGVLLLKRRLFSPRVRATSTGADILILSLLLIQCLLGL
LTIPFSAQHMDGSEMMKLVGWAQSIVTFRGGASQHLDGVAFIFRLHLVLGMTLFLLFPFTRLVHVWSVPV
EYLTRKYQLVRARH
>gnl|CDD|129451 TIGR00353, Cytochrome_c-type_biogenesis_protein_CcmF, c-type cytochrome biogenesis protein CcmF. The product of this gene is required for the biogenesis of C-type cytochromes. This gene is thought to have eleven transmembrane helices. Disruption of this gene in Paracoccus denitrificans, encoding a putative transporter, results in formation of an unstable apocytochrome c and deficiency in siderophore production [Energy metabolism, Electron transport]
AFGVLTYCFAVNDFSVIYVAQHSNSQLPWEYKLAAVWGGHEGSLLLWVLLLSAWSAAFAWFSRQQPDPLV
ARVLAILGLISVGFLLFVLFTSNPFVRIFPFPIEGRDLNPMLQDPGLIFHPPLLYMGYVGFSVAFAFALA
SLLRGELDSACARICRPWTLAAWSFLTLGIVLGSWWAYYELGWGGWWFWDPVENASLMPWLSGTALLHSL
SVTEQRGSFKAWTLLLAILAFSLSLLGTFIVRSGILVSVHAFALDNTRGVPLLALFVLVIGGSLALYAWR
GSDGRSAVNFSGLSRESLILANNILLCAALLVVLLGTLYPMVHKQLGWGSISVGAPYFNRMFLPIMTPFA
LLLGIGLLVRWGRDRTLLIRCGWIIVLSTLVAGLMLPQQLRNKSAVLGHAMAFVIATLAIWELFVRLWQW
KIKRSQWGMLLAHLGVALTAAGIVFSQNFSVEIDVRLKPGQSVTLGGYTFRFRCVDLEAGPNYTGEKAII
DVTKDGQPEAELTPERRFYEVRRMQMTEAAIDGGGTRDLYAVMGEKLGPGRWAFRLYYKPFVRWIWAGGL
LMALGALLSGFDGRYR
>gnl|CDD|273031 TIGR00354, DNA_polymerase_II_large_subunit, DNA polymerase, archaeal type II, large subunit. This model represents the large subunit, DP2, of a two subunit novel Archaeal replicative DNA polymerase first characterized for Pyrococcus furiosus. Structure of DP2 appears to be organized as a ~950 residue component separated from a ~300 residue component by a ~150 residue intein. The other subunit, DP1, has sequence similarity to the eukaryotic DNA polymerase delta small subunit [DNA metabolism, DNA replication, recombination, and repair]
EEMRRYFESLMVELDRIYRIAEAARKKGLDPELSVEIPLAKDMAERVEGLVGPQGLAKRIMELEGGLGRE
LIAFKIADEIVEGKFGEMDKEKAADQAVRTALAILTEGVVAAPLEGIARVRIKRNFDKSNYLAVYYAGPI
RSAGGTAQALSVLVADYVRRAAGLDRYKPTEEEIERYVEEVELYKSEVANLQYLPSDDEIRLAVSNIPIE
ITGEPTDSVEVSGHRDLPRVETNRVRGGALLVIVEGVALKAPKLLKMVDELGIEGWDWLDALIKGKGDKG
SEGEEKVVIKAKDKYLSDIIAGRPVLAHPSRKGGFRLRYGRARNTGFATVGVHPATMYLLEFVAVGTQLK
VERPGKAGCVVPVDTIEGPTVKLKNGDVIRINTLEEAKAVRGEVEEILFLGDILVNYGDFLENNHPLIPA
SWCEEWWIQEAEKANLSYLRGDYRKISEEEALKLCDEFHVPLHPRYTYLWHDVSVEDYRYLRNWLSDNGK
LEGKHGKSDLLLPEDSRVKRILEALGLEHKVRESFVVIETWRAFIRCLGLDEKLSKVLEVSKDVLEIVNG
ISPIKVRPKALSYIGARMGRPEKAKERKMSPPPHILFPIGMAGGNTRDIKNAINYTKEIEVEIAIRKCPQ
CGKESFWLKCPVCGELTEQLYYGKRKVDLRELYEEAIANLGEYKFDTIKGVKGMTSKTKIPEPLEKGILR
AKNGVYVFKDGTARFDATDLPITHFKPAEIGVSVEKLRELGYERDYYGAELKDENQIVELKPQDVIIPES
CAEYLVRVANFIDDLLEKFYKMERFYNVKSVEDLIGHLVIGLAPHTSAGVLGRIIGFTDALAGYAHPYFH
AAKRRNCDGDEDSFMLLLDALLNFSKKFLPDKRGGQMDAPLVLTTIVDPREVDKEVHNMDTMERYPLEFY
EATMRFPSPKEVEDYVEKVEDRLGKPEQYCGLFFTHDTSRIDAGPKVCAYKSLKTMQEKVYSQMELARKI
RAVDERDVAERVINSHFLPDIIGNLRAFSRQEVRCTKCNTKYRRIPLVGKCLKCGNNLTLTVSKGSVMKY
LELSKFLAENYNVSSYTKQRLMILEQGINSMFENGTSKQVSLSDF
>gnl|CDD|273032 TIGR00355, purH, phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase. PurH is bifunctional: IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) Involved in purine ribonucleotide biosynthesis. The IMP cyclohydrolase activity is in the N-terminal region [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHG
GILARRGDDDDADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTI
LVDPKDYSAILSELDEQGSISLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEKEPRQFNLNFTKKQTLR
YGENPHQKAAFYVTQNVKEGSVATAEQLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALG
KTILDAYDRAFGADPTSAFGGIIALNRELDVPTAKAIVRQFLEVIIAPGYSAEALEILAKKKNLRVLILG
IWANRVPELDFKRVNGGLLVQDRDDGMVDQSTLKVVTKRQPTEQELIDLLFAWKVAKHVKSNAIVYAKNN
MTVGVGAGQMSRVGSAKIAGIKADDEGLEAKGSSLASDAFFPFRDGVEEAAAAGITCIIQPGGSMRDEDS
IWAADEHGIVMVFTGMRHFRH
>gnl|CDD|129454 TIGR00357, Peptide_methionine_sulfoxide_reductase_MsrB, methionine-R-sulfoxide reductase. This model describes a domain found in PilB, a protein important for pilin expression, N-terminal to a domain coextensive to with the known peptide methionine sulfoxide reductase (MsrA), a protein repair enzyme, of E. coli. Among the early completed genomes, this module is found if and only if MsrA is also found, whether N-terminal to MsrA (as for Helicobacter pylori), C-terminal (as for Treponema pallidum), or in a separate polypeptide. Although the function of this region is not clear, an auxiliary function to MsrA is suggested [Protein fate, Protein modification and repair, Cellular processes, Adaptations to atypical conditions]
KPSDEELKKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPI
SEEVVAYERDESHGMIRTEVRCRNCDAHLGHVFDDGPEPTGLRYCINSAALKFIPLEEMEEEGY
>gnl|CDD|273033 TIGR00358, Ribonuclease_R, VacB and RNase II family 3'-5' exoribonucleases. This model is defined to identify a pair of paralogous 3-prime exoribonucleases in E. coli, plus the set of proteins apparently orthologous to one or the other in other eubacteria. VacB was characterized originally as required for the expression of virulence genes, but is now recognized as the exoribonuclease RNase R (Rnr). Its paralog in E. coli and H. influenzae is designated exoribonuclease II (Rnb). Both are involved in the degradation of mRNA, and consequently have strong pleiotropic effects that may be difficult to disentangle. Both these proteins share domain-level similarity (RNB, S1) with a considerable number of other proteins, and full-length similarity scoring below the trusted cutoff to proteins associated with various phenotypes but uncertain biochemistry; it may be that these latter proteins are also 3-prime exoribonucleases [Transcription, Degradation of RNA]
QLLATLKYALPEKDDLVKGVVKAHNKGFGFLRPDDDDKKDYFIPPPQMKKVMHGDLVEACPLSQPQRGRF
EAEVERILEPALTRFVGKFLGENDFGFVVPDDPRIYLDIIVPKASVKNELAEGDKVVVELTEYPLRRNLF
YGEITQILGNNDDPLIPWWVTLARHEIPFEFPDGVEQQAAKLQFDVDEQAKKYREDLTDLAFVTIDGADA
KDLDDAVYVKKLPDGGWKLYVAIADVSYYVAENSPLDKEAKHRGFSVYLPGFVIPMLPEELSNGLCSLNP
NEDRLVLVCEMTISAQGRITDNEFYPATIESKARLTYDKVNDWLENDDELQPEYETLVEQLKALHQLSQA
LGEWRHKRGLIDFEHPETKFIVDEEGRVIDIVAEVRRIAEKIIEEAMIVANICAARFLHNHKVPGIYRVH
PGPSKKKLQSLLEFLAELGLTLPGGNAENVTTLDGACWLREVKDRPEYEILVTRLLRSLSQAEYSPEPLG
HFGLGLEHYAHFTSPIRRYPDLTNHRLIKAVLAKEQTDTERYQPQDELLQIAEHCSDTERRARDAERDVA
DWLKCRYLLDKVGTEFSGEISSVTRFGMFVRLDDNGIDGLIHISTLHNDYYVFDQEKMALIGKGTGKVYR
IGDRVTVKLTEVNMETRSIIFELV
>gnl|CDD|273034 TIGR00359, NN'-diacetylchitobiose_permease_IIC_component, phosphotransferase system, cellobiose specific, IIC component. The family consists of the cellobiose specific form of the phosphotransferase system (PTS), IIC component [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
LVPIAGKIGGQRHLQALRDGFILTMPLTIIGSFFLLLTNLPFPGLADFMAIEFLNSWKGKLGYPVNATMG
IMSLFAVFGIGYRLAESYKVDALSAGAISLAAFLLLTPQSVPFSPDGATEAIMVGGVIPANLLGAKGLFV
AMIIALVSTEIYRFIVQKNLVIKMPDGVPPAVSKSFVALIPGFIILSVMWLINLAIESTPGTNFHNIIMD
LIGTPLSILGSSLGGTLVAEFFVMLLWFCGLHGANIIGALMNPIWYGAMDENIAAYQAGEELPHIFAKPF
LDIFVNIGGSGATLALVLTMFIRSRSKQMKQVGKLALAPGIFNINEPIIFGLPIVMNPILIIPFVLAPLV
TITVTYIAMSTGLVPPPVGIAVPWTMPPGISGFFATGGSVSGAVMQLINLLISFVIYLPFFKAWDKAKLA
EEK
>gnl|CDD|273035 TIGR00360, Uncharacterized_protein_MG316_homolog, ComEC/Rec2-related protein. The related model ComEC_Rec2 (TIGR00361) describes a set of proteins of ~ 700-800 residues, one each from a number of different species, of which most can become competent for natural transformation with exogenous DNA. The best-studied examples are ComEC from Bacillus subtilis and Rec-2 from Haemophilus influenzae, where the protein appears to form part of the DNA import structure. This model represents a region found in full-length ComEC/Rec2 and shorter homologs of unknown function from large number of additional bacterial species, most of which are not known to become competent for transformation (an exception is Helicobacter pylori) [Unknown function, General]
IAHLLAISGLHVSLLFGIVQYFLPKRGIHWYLALIVGLIFLLFYLFLTGFAPSALRAFLALVLVLAFKLS
LRKLNLIGALLLSAIVILLMNPVALLSFGFQLSFLATFGLVVMFPNFQQLLRPLSSLIHVQLILILWSTP
ILLYLFHGLSPISVLANLLAIPLYSFLLLPG
>gnl|CDD|273036 TIGR00361, Recombination_protein_2, DNA internalization-related competence protein ComEC/Rec2. Apparant orthologs are found in 5 species so far (Haemophilus influenzae, Escherichia coli, Bacillus subtilis, Neisseria gonorrhoeae, Streptococcus pneumoniae), of which all but E. coli are model systems for the study of competence for natural transformation. This protein is a predicted multiple membrane-spanning protein likely to be involved in DNA internalization. In a large number of bacterial species not known to exhibit competence, this protein is replaced by a half-length N-terminal homolog of unknown function, modelled by the related model ComEC_N-term. The role for this protein in species that are not naturally transformable is unknown [Cellular processes, DNA transformation]
SQNVSSYRQGTYQFQAVIDTIPKIDGMTDRMSMIVETPDKEKWAAAYRIQSAGEKEQLLYIEPGWSCELT
LREPNHALNPGGFDYQEYLYRQHIHWNGSVTSAQNISEVLSLRAHILSFTNSLLPPDSWTGIVQALTVGE
RFYVEKEVLTIYQKTGTAHLLAISGLHIGLAAGLFYILIRLGQIFLPGRIIHEKAPLLLGLFCAPLYAML
TGAAPPVLRAALALGVYLAGSLVKRRVSSATAICLSYIVLLLFDPYHLLSASFWLSFAAVFSLILWYSIF
PQVKTQLGPVLRAVVSLTHLQLGAQLGSLPIQLYHFHGFSLISFPANMLAVPFYTFCIVPLILAAVLLLS
LSGSFGRLQGSWFDLLISLALRLIWNIADVPEFTIMIAHPWQVLLFLFTVLIILLLLAIEKRSLSQLCVT
GGILCCVMFLLFIYPCLSSWQVDMLDVGQGLAMFIGANGKGILYDTGEPWREGSLGEKVIIPFLTAKGIK
LEALILSHADQDHIGGAEIILKHHPVKRLVIPKGFVEEGVAIEECKRGDVWQWQGLQFHVLSPEAPDPAS
KNNHSCVLWVDDGGNSWLLTGDLEAEGEQEVMRVFPNIKADVLQVGHHGSKTSTSEELIQQVQPKVAIIS
AGRNNRWHHPHQKVLQRLQRHSIRVLRTDQNG
>gnl|CDD|273037 TIGR00362, DnaA, chromosomal replication initiator protein DnaA. DnaA is involved in DNA biosynthesis; initiation of chromosome replication and can also be transcription regulator. The C-terminal of the family hits the pfam bacterial DnaA (bac_dnaA) domain family. For a review, see Kaguni (2006) [DNA metabolism, DNA replication, recombination, and repair]
WNRILERLEKELSEQEYNTWFKPLKLLSIEGNTLIISVPNEFVKEWIEKNYLDLIEELLQELFGAEIEIE
FTVGEDEEELEPNSKKPEPAPPEAPAPPSSASGLNPKYTFDNFVVGKSNRLAHAAALAVAENPGKAYNPL
FIYGGVGLGKTHLLHAIGNEILENNPNAKVLYVSSEKFTNDFVNALRNNKMEEFKEKYRSVDLLLIDDIQ
FLAGKERTQEEFFHTFNALHENNKQIVLTSDRPPKELPGLEDRLRSRFEWGLVVDIEPPDLETRLAILQK
KAEEEGLELPDEVLEFIAKNITSNVRELEGALNRLLAYASLTGKPITLELAKEALKDLLRAQKKEITIEN
IQKVVAKYYNIKVSDLKSKKRTRNIVRPRQIAMYLAKELTDLSLPEIGKAFGGRDHTTVLHAVRKIEKLI
ETDAELKEDIEELKRKL
>gnl|CDD|129460 TIGR00363, Probable_D-methionine-binding_lipoprotein_MetQ, lipoprotein, YaeC family. This family of putative lipoproteins contains a consensus site for lipoprotein signal sequence cleavage. Included in this family is the E. coli hypothetical protein yaeC. About half of the proteins between the noise and trusted cutoffs contain the consensus lipoprotein signature and may belong to this family [Cell envelope, Other]
LASALVLTGCKQDKKDPLHIKVGVISGAEQQVAEVAAKVAKEKYGLDVELVEFNDYALPNEAVSKGDLDA
NAFQHKPYLDQDAKAKGYKLVAVGNTFVYPLAGYSKKIKNVNELQDGAKVAVPNDPTNLGRALLLLQKQG
LIKLKDGNGLLPTVLDIVENPKKLNITELETSQLPRALDDPKVDLAVINTTYAGQVGLNPQDDGVFVEDK
DSPYVNIIVSREDNKDAENVKDFIQSYQSEEVYQAAQKHFNGGAVKGW
>gnl|CDD|129461 TIGR00364, 7-cyano-7-deazaguanine_synthase, queuosine biosynthesis protein QueC. Members of this protein family are QueC, involved in synthesizing pre-Q0 from GTP en route to tRNA modification with queuosine. This protein family is represented by a single member in nearly every completed large (_ 1000 genes) prokaryotic genome. In Rhizobium meliloti, the gene was designated exsB, possibly because of polar effects on exsA expression in a shared polycistronic mRNA. In Arthrobacter viscosus, the homologous gene was designated ALU1 and was associated with an aluminum tolerance phenotype [Unknown function, General]
AIVVLSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSRELESARKIAEALGIEHHLLDLSLLNQLGGSAL
TREQEIPEQKSNEEDTLPNTFVPGRNLVFLSIAASYAEAIGAEAIITGVCETDFSGYPDCRDEFVKAFNV
ALNLGMLTPVEIRAPLMDLTKAEIVKLADELGVLDLVIKLTYSCYAGGGEGCGKCPSCMLR
>gnl|CDD|188046 TIGR00365, TIGR00365, monothiol glutaredoxin, Grx4 family. The gene for the member of this glutaredoxin family in E. coli, originally designated ydhD, is now designated grxD. Its protein, Grx4, is a monothiol glutaredoxin similar to Grx5 of yeast, which is involved in iron-sulfur cluster formation [Energy metabolism, Electron transport]
TIERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGVPFAYVNVLEDPEIRQGIKEYSNWPTIPQ
LYVKGEFVGGCDIIMEMYQSGELQTLL
>gnl|CDD|273038 TIGR00366, Short-chain_fatty_acids_transporter, TIGR00366 family protein [Hypothetical proteins, Conserved]
RMSRFMTAFVSKWLPDPLIFALLLTLVTFVLVIVLTKQTPVSLVDMWGNGFWNLLGFGMQMALILVTGYA
LAYSPIVYKLLKTIASLPKTPKQAVALVTFIGSIACWINWGFGLVVGAIFAREVARRVKGSDYPLLIACA
YIGFLTWHGGLSGSMPLLAATPNNPLKHIFVELFGRETIPLNETIFSGYNLIITAIIIVFLPFITYMMMP
KRGELKSIDPKLLKKEKEEEKKLKKKEDATIAEKLENSRVLALLIGALGIIYLGMYFYEKGFNLTLNSVN
LIFLIVGLLLHKTPMAYMRAITRAARSVAGILVQFPFYAGIMGMMEHSGVGGGGPATLITEFFINVANKD
TFPLMTFFSAGLINIFIPSGGGHWAIQGPIVIPAAQALGVDLGKSVMAIAYGDAWTNMAQPFWALPALGI
AGLGARDIMGYCITALIF
>gnl|CDD|273039 TIGR00367, Uncharacterized_membrane_protein_MJ0091, K+-dependent Na+/Ca+ exchanger related-protein. This model models a family of bacterial and archaeal proteins that is homologous, except for lacking a central region of ~ 250 amino acids and an N-terminal region of _ 100 residues, to a functionally proven potassium-dependent sodium-calcium exchanger of the rat [Unknown function, General]
LLLIGYLILGLILLIYGADLFVKSSVRIARHLGISPLIIGVTVVAIGTSLPELFTSLIASLMGQPDIGVG
NVIGSNIFNILLILGLSAIFSPIIVDKDWLRRDILFYLLVSILLLFFGLDGQISRIDGVVLLILYIVYLL
FLVKNERWVKYDTYTEENLDENNRRPQIFFSLVLLIIGLIGLVVGSRLLVDGAVKIAEILGISEKIIGLT
LLAIGTSLPELVVSLAAARKGLGDIAVGNVIGSNIFNILVGLGVPSLFMPIPVEPLAYNLDAPVMVIVTL
LLMLFFKTSMKLGRWEGILLLALYIAY
>gnl|CDD|129465 TIGR00368, Uncharacterized_protein_YifB, Mg chelatase-related protein. The N-terminal end matches very strongly a pfam Mg_chelatase domain [Unknown function, General]
VYSRSSLGVEAPLITIEVDISKGLPGITIVGLPETTVKESRERVKSAIKNSGFHFPAKRITINLAPADLP
KEGGRFDLPIAIGILAASEQLDAKNLGEYLFLGELALDGKLRGIKGVLPAIALAQKSGRKFIIVPKENAE
EASLIDGLNIYGADHLKEVVKFLEGSEKLPPRTNTKPKSIINKSYIIDLDLKDIKGQQHAKRALEIAAAG
GHNLLLFGPPGSGKTMLASRLQGILPPLTNEEAIETARIWSLVGKLIDRKQIKQRPFRSPHHSASKPALV
GGGPIPLPGEISLAHNGVLFLDELPEFKRSVLDALREPIEDGSISISRASAKIFYPARFQLVAAMNPCPC
GHYGGKNTHCRCSPQQISRYWNKLSGPFLDRIDLSVEVPLLPPEKLLSTGSGESSAEVKQRVIKAREIQN
IRYEKFANINKNADLNSDEIEQFCKLSAIDANDLEGALNKLGLSSRATHRILKVARTIADLKEEKNISRE
HLAEAIEYR
>gnl|CDD|161843 TIGR00369, Putative_esterase, uncharacterized domain 1. Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown
PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNAN
HLRPAREGKVRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV
>gnl|CDD|129467 TIGR00370, Uncharacterized_protein_HI_1731, sensor histidine kinase inhibitor, KipI family [Hypothetical proteins, Conserved]
IGESAVVIRLGPPINEQVQGIVWAAAAYLEEQPGFVECIPGMNNLTVFYDMYEVYKHLPQRLSSPWEEVK
DYEVNRRIIEIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTP
RRASPRPSVPAGSVGIGGLQTGVYPISTPGGWQLIGKTPLALFDPQENPPTLLRAGDIVKFV
>gnl|CDD|273040 TIGR00372, conserved_hypothetical_protein, CRISPR-associated protein Cas4. This model represents a family of proteins associated with CRISPR repeats in a wide set of prokaryotic genomes. This scope of this model has been broadened since it was first built to describe an archaeal subset only. The function of the protein is undefined. Distantly related proteins, excluded from this model, include ORFs from Mycobacteriophage D29 and Sulfolobus islandicus filamentous virus and a region of the Schizosaccharomyces pombe DNA replication helicase Dna2p
ITPSDVKEYLYCPRKLWYMKKGGSERFSEVRMILGRLIHEEAESFLKSLGEVREEKEVPLKSKKYGLKGV
IDIVLEEDGELVPVEVKSGKPSPREAHKYQLLAYAYLLEEMYGEIVRGYILYINAGKKLEVEISEELRKK
AVKLIEKIRELLEGGKPPSPPKSGPKCKFCPYREICLP
>gnl|CDD|129469 TIGR00373, Transcription_factor_E, transcription factor E. This family of proteins is, so far, restricted to archaeal genomes. The family appears to be distantly related to the N-terminal region of the eukaryotic transcription initiation factor IIE alpha chain [Transcription, Transcription factors]
EELLNEVVGRAAEEEVGLVLFSLGIKGEFTDEEISLELGIKLNEVRKALYALYDAGLADYKRRKDDETGW
YEYTWRINYEKALDVLKRKLEETAKKLREKLEFETNNMFFICPNMCVRFTFNEAMELNFTCPRCGAMLDY
LDNSEAIEKLEEQIKFLK
>gnl|CDD|129470 TIGR00374, UPF0104_membrane_protein_MTH_1261, conserved hypothetical protein. This model is built on a superfamily of proteins in the Archaea and in Aquifex aeolicus. The authenticity of homology can be seen in the presence of motifs in the alignment that include residues relatively rare among these sequences, even though the alignment includes long regions of low-complexity hydrophobic sequences. One apparent fusion protein contains a Glycos_transf_2 region in the N-terminal half of the protein and a region homologous to this superfamily in the C-terminal region [Unknown function, General]
IVLSILFLLAIILYIGPGEILRALGNANPFYLLLAFLLQFLVLALWTLRWKLISNALGIKYSFRHLFMLL
FVGMFINNITPSAAGGEPMRAYMLKKKEGISASLGFSTVLAERVFDLVIFILLLPLSAIMVFVLSIPKLF
IYLILILITLLLFLIILYIFGNKKILQKIASKILKAVVKFFSRKNELESKLRSFLVRFLGATKFFLKDTA
ELVVLILLSLGMWLLEILRLYLIFLAFGVEVSFLEIIIIQLIALLVGLLPLTPGGLGVAEVSMIYLFSVF
GVPPSVAGAVVLLDRLISYWMITFLGAIAFFIYLREITK
>gnl|CDD|161657 TIGR00375, Uncharacterized_protein_MJ0043, TIGR00375 family protein. The member of this family from Methanococcus jannaschii, MJ0043, is considerably longer and appears to contain an intein N-terminal to the region of homology [Hypothetical proteins, Conserved]
NADLHIHIGRTRGAKTLTLDRILVEQSRLKGLELLGIIDCHSPLEEGISSGKRELDGGGIRYRSELSIYD
EACVDESGPIHVLLFMPTLADMKQFSNWLSARLKNIGRSSQRIYETGLNLEKVQDYGGLFGPAHIFTPWT
SLYKSGDSSSDCYVFDPDFVELGLSADTDMADHISELNDYPFLTNSDAHSLGPHRLGREFNQLEVQSADF
TEFALALKAIDDRKIIANYGLDPLLGKYHQTACEACGEPAVSEDAETACANCPCGGRIKKGVSDRLRELS
DQKLEHPVPRPPYVHLIPLAEVIGVGPKKGIFTKAVQSLWEKLKKAFGTEIAVLHEAAEEDLARVVPKVA
ALIVKFRSGKLELKPGGGGTYGKI
>gnl|CDD|273041 TIGR00376, DNA-binding_protein_SMUBP-2, DNA helicase, putative. The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases [DNA metabolism, DNA replication, recombination, and repair]
LERDAEISAMMNEIRRLSLKQRERRGRAILNLQGKIRGGLLGFLLVRFGRRKAIATEISVGDIVLVSRGN
PLQSDLTGVVTRVGKRFITVALEESVPQWSLKRVRIDLYANDVTFKRMKEALRALTENHSRLLEFLLGRE
APSKASEIHDFQFFDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPS
NIAVDNLLERLALCDQKIVRLGHPARLLKSNKQHSLDYLIENHPKYQIVADIREKIDELIEERNKKTKPS
PQKRRGLSDIKILRKALKKREARGIESLKIASMAEWIETNKSIDRLLKLLPESEERIMNEILAESDATNS
MAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHKQLPPTILSHDAEELSLTLFERLIKE
YPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLPKVEATESEDDLETGIPLLFIDTSG
CELFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDLLRQLLEHRHIDIEVSSVD
GFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHGE
VREAFK
>gnl|CDD|273042 TIGR00377, Anti-sigma_F_factor_antagonist, anti-anti-sigma factor. This superfamily includes small (105-125 residue) proteins related to SpoIIAA of Bacillus subtilis, an anti-anti-sigma factor. SpoIIAA can bind to and inhibit the anti-sigma F factor SpoIIAB. Also, it can be phosphorylated by SpoIIAB on a Ser residue at position 59 of the seed alignment. A similar arrangement is inferred for RsbV, an anti-anti-sigma factor for sigma B. This Ser is fairly well conserved within a motif resembling MXS[STA]G[VIL]X[VIL][VILF] among homologous known or predicted anti-anti-sigma factors. Regions similar to SpoIIAA and apparently homologous, but differing considerably near the phosphorlated Ser of SpoIIAA, appear in a single copy in several longer proteins [Regulatory functions, Protein interactions]
MNLNIETEVQEGVVVVRLSGELDAHTAPLLREKVTPAAERTGIRPIVLDLEDLEFMDSSGLGVLLGRYKQ
VRRVGGQLVLVSVSPRVARLLDITGLLRIIPIYPTVEE
>gnl|CDD|273043 TIGR00378, cax, calcium/proton exchanger (cax) [Transport and binding proteins, Cations and iron carrying compounds]
LLVFVPLSVIGSLMHWPSTVLFAVYCLAIIPLAAYMGRATEELAIIAGPRIGGLLNATFGNAVELIISII
ALKEGLTGIVLASLTGSVLGNLLLVAGLSFFVGGLKYKRQEFNIHAARHNSSLLIFAIVAFLIPAAFEVF
SVGMENASKLNLSIGISIVMILVYVLALYFKLGTHRGLYQPNNAEQTEEMEEIEREPEHSWSGKVATIVL
LAATIVVAYISENLVGTFHSVAESFGLSELFIGVIVVPIVGNAAEHATAVIVAMKDKMDLAVEVAVGSSL
QIAMFVAPVLVIVGWFIPTPMPLNFTLFELVAMVSAVLLMNAISNDGDSNWLEGATLLAAYVIMAIAFF
>gnl|CDD|273044 TIGR00379, Probable_cobyrinic_acid_AC-diamide_synthase, cobyrinic acid a,c-diamide synthase. This model describes cobyrinic acid a,c-diamide synthase, the cobB (cbiA in Salmonella) protein of cobalamin biosynthesis. It is responsible for the amidation of carboxylic groups at positions A and C of either cobyrinic acid or hydrogenobrynic acid. NH(2) groups are provided by glutamine and one molecule of ATP hydrogenolyzed for each amidation [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
RVVIAGTSSGVGKTTISTGIMKALSRRKLRVQPFKVGPDYIDPMFHTQATGRPSRNLDSFFMSEAQIQEC
FHRHSKGTDYSIIEGVRGLYDGISAITDYGSTASVAKALDAPIVLVMNCQRLSRSAAAIVLGYRSFDPGV
KLKGVILNRVGSERHLEKLKIAVEPLRGIPILGVIPRQQDLKVPDRHLGLVPAGEREIIQQIFDWLAEVV
EKYLDLDKLLEIAETARNLPSPMSLLWEPQNSKYVRIAVAQDQAFNFYYQDNLDALTHNAAELVPFSPLE
DTELPDVDAVYIGGGFPELFAEELSQNQALRDSIKTFIHQGLPIYGECGGLMYLSQSLDNFEGQIFMVGM
LPTAATMTGRVQGLGYVQAEVVNDCLILWQGEKFRGHEFHYSRMTKLPNAQFAYRVERGRGIIDQLDGIC
VGSVLASYLHLHAGSVPKFAAAFVAFAKK
>gnl|CDD|273045 TIGR00380, Probable_cobalamin_biosynthesis_protein_CobD, cobalamin biosynthesis protein CobD. This protein is involved in cobalamin (vitamin B12) biosynthesis and porphyrin biosynthesis. It converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. It is part of the cob operon [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
MIEVIILLLAAILDFLIGEPPSWLHPVVWIGSLINFLENIIIRKVNDKNSRRLWGIFLTLIVIISFGLIA
FLIVYLAEKLPPPLNVIIQIILLSSCISGKSLVQAAQSVIESLKAGDLETARKKLQMIVSRDTNNLSEEQ
ILSAAVESVAENIVDGVTAPLFYAILFGLPGAFVYRAVNTLDAMVGYKREPYTDLGWFAARLDDILNYIP
SRLTVFMLLFLSGKPKGAFAIVLRDAPKDPSPNSGWTMAAYAAALGIQLEKPGVYKLGPLLGDGIDPEKI
LKAFKSLWYTRVVFLQIALGITVIL
>gnl|CDD|273046 TIGR00381, cdhD, CO dehydrogenase/acetyl-CoA synthase, delta subunit. This is the small subunit of a heterodimer which catalyzes the reaction CO + H2O + Acceptor = CO2 + Reduced acceptor and is involved in the synthesis of acetyl-CoA from CO2 and H2 [Energy metabolism, Chemoautotrophy]
LSELGKFLYHANMIEIYLQRLSAAELIPTPFAAQPQLIPATPAAPEEVPAVELKIPAELPRAKFEPPKEE
YPGKIEEVVLGATKAEGTREKTVTLGGQRALYRFEEPQPNPPVVTFDVFDIPMPGLPKPIRMHFEDVMED
PAEWARKCVKEFGADMVTIHLISTDPKLDDKSPSEAAKVLEDVLQAVDVPIVIGGSGNPEKDPLVLEKAA
EVAEGERCLLASANLDLDYEKIANAAKKYGHVVLSWTIMDINMQKTLNRYLLKRGLMPRDIVMDPTTCAL
GYGIEFSITNMERIRLSGLKGDTDLNMPMSSGTTNAWGAREAWMVDSEWGPREYRGPLWEIITGLTMMLA
GVDLFMMLHPVSVAVLKEIGNTLTGPKVSGGVADPGEWI
>gnl|CDD|273047 TIGR00382, clpX, endopeptidase Clp ATP-binding regulatory subunit (clpX). A member of the ATP-dependent proteases, ClpX has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpPX. The gene is also found to be involved in stress tolerance in Bacillus subtilis and is essential for the efficient acquisition of genes specifying type IA and IB restriction [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]
MTKKNETLYCSFCGKSQDEVRKLIAGPGVYICDECIELCHDILEEELGTRKESKEYEEEFELSYLPTPKE
IKAHLDEYVIGQEQAKKVLSVAVYNHYKRLNFEKNKKSDNGVELSKSNILLIGPTGSGKTLLAQTLARIL
NVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEG
VQQALLKIIEGTVANVPPQGGRKHPYQEFIQIDTSNILFICGGAFVGLEKIIKKRTGKSSIGFGAEVKKK
SKEKADLLRQVEPEDLVKFGLIPEFIGRLPVIATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELD
FEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSLEDLEKVVITKETVLKQSEPLLI
>gnl|CDD|273048 TIGR00383, Magnesium_and_cobalt_transport_protein_corA., magnesium Mg(2+) and cobalt Co(2+) transport protein (corA). The article in Microb Comp Genomics 1998;3(3):151-69 (Medline:98448512) discusses this family and suggests that some members may have functions other than Mg2+ transport [Transport and binding proteins, Cations and iron carrying compounds]
ITAIAIEKSRLIKIPFFEEFSQELNTVLWIDLIEPTDEERLAKLGQFFAIHPLALEDILNSPQRPKVEED
EDHLFIISFFLNEDEDDTFETEQVSFILGKNLLFTIHERELPAFDSIRERIRTSQKVFEKGADYLLYDIF
DAIIDSYFPLLENIEDELEELEDEIISGPTSTLMDEILSLRTELLALRRSLWPLRDVLNFLLRKTHLPIQ
TEEVREYLRDIYDHILSLLEMIETYRELLSSLMDLYLSLVNNKMNEIMKILTVVSTIFIPLTFIAGIYGM
NFKFMPELNWKYGYPAVLIVMAVIALGPLIYFRRKGWL
>gnl|CDD|273049 TIGR00384, Succinate_dehydrogenase_iron-sulfur_subunit, succinate dehydrogenase and fumarate reductase iron-sulfur protein. Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 (EC 1.3.11.1). In E. coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This model also describes a region of the B subunit of a cytosolic archaeal fumarate reductase [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]
VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKT
KVEDLGQPVMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGC
ILCGCCYSSCPAFWWNPEFLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGV
NPARAIEKLK
>gnl|CDD|129481 TIGR00385, Thiol:disulfide_interchange_protein_DsbE_homolog, periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily. Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins [Protein fate, Protein folding and stabilization]
LLLPLIIFLGIAAALLWQLARNAEGDDPKALPSALIGKPVPAFRLASLDEPGQFYTADVLTQGKPVLLNV
WASWCPPCRAEHPYLNELAKQGLPIVGVDYKDDRQNAIKFLKELGNPYQLSLFDPDGMLGLDLGVYGAPE
TFLVDGNGVIRYRHAGPLNPEVWTEEFLPLWEK
>gnl|CDD|273050 TIGR00387, Glycolate_oxidase_subunit_glcD., glycolate oxidase, subunit GlcD. This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity [Energy metabolism, Other]
VVFPKNTEQVARILKLCHEHRIPIVPRGAGTGLSGGALPEEGGLVLVFKHMNKILEIDVVNLTAVVQPGV
RNLELEQAVEEHNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEILRIGGKT
AKDVAGYDLTGLFVGSEGTLGIVTEATLKLLPKPENIVVALAFFDSIEKAMQAVYDIIAAGIIPAGMEFL
DNLSIKAVEDISGIGLPKDAGAILLVEIDGVHEAVERDEEKIEQICRKNGAVDVQIAQDEEERALLWAGR
RNAFKAASKLSPLYLIEDGTVPRSKLPEALRGIADIASKYDFTIANFGHAGDGNLHPTILTDPEDKGEME
RVEEAGGEIFELAIELGGTISGEHGIGVVKAEFMPYKFNEKELETMRAIKKAFDPDNILNPGK
>gnl|CDD|129483 TIGR00388, Glycine--tRNA_ligase_alpha_subunit, glycyl-tRNA synthetase, tetrameric type, alpha subunit. This tetrameric form of glycyl-tRNA synthetase (2 alpha, 2 beta) is found in the majority of completed eubacterial genomes, with the two genes fused in a few species. A substantially different homodimeric form (not recognized by this model) replaces this form in the Archaea, animals, yeasts, and some eubacteria [Protein synthesis, tRNA aminoacylation]
QTFQGLILKLQEYWANQGCLIVQPYDMEKGAGTMHPMTFLRSLGPEPWAVAYVEPSRRPTDGRYGENPNR
LQHYYQFQVVIKPSPDNIQELYLDSLRALGIDPTEHDIRFVEDNWENPTLGAWGLGWEVWLDGMEVTQFT
YFQQVGGLECKPVSVEITYGLERLAMYIQGVENVYDLEWSDGPLGKTTYGDVFHQNEVEQSTYNFETADV
DFLFQLFKQYEKEAQQLLENGLPLPAYEYVLKCSHSFNLLDARKAISVTERQRYILRIRNLAKGVAEAYY
EQREALGFPLCKK
>gnl|CDD|273051 TIGR00389, Glycine--tRNA_ligase, glycyl-tRNA synthetase, dimeric type. This model describes a glycyl-tRNA synthetase distinct from the two alpha and two beta chains of the tetrameric E. coli glycyl-tRNA synthetase. This enzyme is a homodimeric class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes His, Ser, Pro, and this set of glycyl-tRNA synthetases [Protein synthesis, tRNA aminoacylation]
VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEV
LKASGHVDNFTDWMVDCKSCKERFRADHLIEEKLGKRLWGFSGPELNEVMEKYDINCPNCGGENLTEVRS
FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFE
QAEIEFFVHPLDKSHPKFEEVKQDILPLLPRQMQESGIGEAVESGMIENETLGYFIARVKQFLLEIGINP
DKLRFRQHDKNEMAHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTK
WEIEPNKKKFGPKFRKDAKKIESNLSEDDLEEREEELDKNEVELDKDLVEIEMVTEVVHGEKYIPHVIEP
SFGIDRIIYALLEHSYQEEVLDGEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIK
YDDSGTIGKRYRRADEIGTPFCVTIDFETLEDETVTIRERDSMKQVRVKIKELPSYIKKLL
>gnl|CDD|273052 TIGR00390, ATP-dependent_protease_ATPase_subunit_HslU, ATP-dependent protease HslVU, ATPase subunit. This model represents the ATPase subunit of HslVU, while the proteasome-related peptidase subunit is HslV. Residues 54-61 of the model contain a P-loop ATP-binding motif. Cys-287 of E. coli (position 308 in the seed alignment), studied in MEDLINE:98389714, is Ser in other members of the seed alignment [Protein fate, Protein folding and stabilization]
MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKL
ANAPFIKVEATKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQW
GQTEQQQEPESAREAFRKKLREGELDDKEIEIDVSAKMPSGIEIMAPPGMEEMTMQLQSLFQNLGGQKKK
KRKLKIKDAKKALIAEEAAKLVDPEEIKQEAIDAVEQSGIIFIDEIDKIAKKGESSGADVSREGVQRDLL
PIVEGSTVNTKYGMVKTDHILFIAAGAFQLAKPSDLIPELQGRFPIRVELQALTTDDFERILTEPKNSLI
KQYKALMKTEGVNIEFSDEAIKRIAELAYNVNEKTENIGARRLHTVLERLLEDISFEAPDLSGQNITIDA
DYVSKKLGALVADEDLSRFIL
>gnl|CDD|273053 TIGR00391, small_subunit, hydrogenase (NiFe) small subunit (hydA). Called (hupA/hydA/hupS/hoxK/vhtG) Involved in hydrogenase reactions performing different specific functions in different species eg (EC 1.12.2.1) in Desulfovibrio gigas,(EC 1.12.99.3) in Wolinella succinogenes and (EC 1.18.99.1) in E.coli and a number of other species and (EC 1.12.99.-) in the archea [Energy metabolism, Electron transport]
NGDNTLIHSHRRQGINRRDFLKLCAALATTLGLSAKAAPEMAEAVENPQRPPVIWIHAQECTGCTESLLR
SAHPTVENLILETISLEYHETLMAAFGHQAEENKHDAIEKYKGQYILVVEGSIPLGDNGIYCMVAGEPIV
EHIRKAAEGAAAIIAIGTCSSWGGVQAAGPNPTGAVPLQKVIPDKPVINVPGCPPNPHNFLATVAYIITF
GKLPKLDDKNRPTFAYGRRIHDHCERRPHFDAGEFVKEFGDEGAREGWCLYKMGCKGPETYNNCSTLRFN
DGGSWPIAIGHGCYGCNEEGFWDGISQLANVENRTPRSQKPDVGAKEGADTVGATALGLLAGVVGLHAGV
SVMAVRELGNQQKKE
>gnl|CDD|273054 TIGR00392, Isoleucine--tRNA_ligase, isoleucyl-tRNA synthetase. The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ligase and is particularly closely related to the valyl tRNA synthetase. This model may recognize IleS from every species, including eukaryotic cytosolic and mitochondrial forms [Protein synthesis, tRNA aminoacylation]
KFPMRGNLSKREEKILAFWQENDIFEKVKKLNKGKPEFIFHDGPPYANGSIHLGHALNKILKDIILRYKT
MQGFNVTRKPGWDTHGLPIEHKVEKKLGISGKKEISSLEIEEFREKCREFALKQIEEQREQFQRLGVWGD
WENPYKTMDPSYEESQWWLFKEAHEKGLLYRGLKPVYWSPRCRTALAEAEVEYKENYKDVKDPSIYVKFP
VKKDKKTYLKVKLSSLLIWTTTPWTLPSNLAIAVHPDFEYALVQDNTKVEYFILAKKLVEKLYNKAGSDY
EIIKTFKGSDLEGLEYEHPLYDFVSQLKEGAPVVIGGDHVTTEDGTGIVHTAPGHGEEDYEIGKKYGLEV
LSPVDEKGVYTEGVNDFQGRFVKDADKDIIKANKIIIEQLKDKGLLLKAEKITHSYPHCWRTKTPVIYRA
TEQWFIKTKDIKDQMLEQIKKVNWVPEWGEGRFGNWLENRPDWCISRQRYWGIPIPIWYCEDTGEPIVVG
SIEELIELIELKGIDAWFEDLHRDFLDKITLKSGDGGEYRRVPDVLDVWFDSGSMPYASIHYPFENEKFK
EVFPADFILEGSDQTRGWFYSSLAIGTALFGQAPYKNVITHGFTLDEKGRKMSKSLGNVVDPLKVINKYG
ADILRLYVASSDPWEDLRFSDEILKQVVEKYRKIRWNTYRFLLTYANLDKFDPLFNSVAVEKFPEEDRWI
LSRLNSLVEEVNEALEKYNFHKVLRALQDFIVEELSNWYIRIIRDRLYCEAKDNDKRAAQTTLYYALLTL
VRLLAPFLPHTAEEIYQNLPGGEEEESVHLNLWPEVDEEFIDEALEANMAIVREIVEAFLALRDAANKKL
RQPLKELVIGKSLEAVLKAVE
>gnl|CDD|129488 TIGR00393, Probable_arabinose_5-phosphate_isomerase, KpsF/GutQ family protein. This model describes a number of closely related proteins with the phosphosugar-binding domain SIS (Sugar ISomerase) followed by two copies of the CBS (named after Cystathionine Beta Synthase) domain. One is GutQ, a protein of the glucitol operon. Another is KpsF, a virulence factor involved in capsular polysialic acid biosynthesis in some pathogenic strains of E. coli [Energy metabolism, Sugars]
GKLVIVGIGKSGLIGKKIVATFASTGTPSFFLHPTEAMHGDLGMVEPNDVVLMISYSGESLELLNLIPHL
KRLSHKIIAFTGSPNSSLARAADYVLDIKVEKEACPINLAPTTSTTLTLALGDALAVALMRARNFSQEDF
ASFHPGGALGRKLLVKVKDLMQTTDLPLIAPTTSFKDALLEMSEKRLGSAIVCDENNQLVGVFTDGDLRR
ALLGGGSLKSEVRDFMTLGPKTFKLDALLLEALEFLERRKITSLVVVDDHNKVLGVLH
>gnl|CDD|273055 TIGR00394, lac_pts_IIC, phosphotransferase system, lactose specific, IIC component. This family of proteins models the IIC domain of the phosphotransferase system (PTS) for lactose. The IIC domain catalyzes the transfer of a phosphoryl group from the IIB domain to lactose. When the IIC component and IIB components are in the same polypeptide chain they are designated IIBC [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
LKPFFEKISRNIYLRAIRDGFIAAMPVILFSSIFLLIAYVPNAWGFGWEDNVTNTLMTPYNYSMGLLAFF
VAGTTAKSLTDSDNRNLELTNQINFISTMLASEISFLALSIEPAKTGFLLAFMGTKGLLTAFIAAFITVN
VYKVCVKNNVTIKMPEEVPPNISQVFKDLIPFGLSVIILYALGLGIKAATGVNVAESIGTLLAPLFSAAD
GYLGITIIFGAYAFFWFVGIHGPSIVEPAIAAITYANIEANLHLIQAGQHADKVITSGTQMFIVTFGGTG
ATLVVPFMFMWACKSKRNKAIGRASVVPTFFGVNEPILFGAPIVLNPVFFIPFILAPIVNVWIFKFFVSV
LGMNSFSANLPWTTPGPIGIVLGTGFAVLSFVLALLLIVVDTIIYYPFVKVYDSQILAEEKA
>gnl|CDD|273056 TIGR00395, Leucine--tRNA_ligase, leucyl-tRNA synthetase, archaeal and cytosolic family. The leucyl-tRNA synthetases belong to two families so broadly different that they are represented by separate models. This model includes both archaeal and cytosolic eukaryotic leucyl-tRNA synthetases; the eubacterial and mitochondrial forms differ so substantially that some other tRNA ligases score higher by this model than does any eubacterial LeuS [Protein synthesis, tRNA aminoacylation]
IAIEKKWQKRWEEAHIFEADPDDREKFFLTMAYPYLNGVMHAGHCRTFTIPEVSARFERMKGKNVLFPLG
FHVTGTPILGLAELIKRRDELTIKNYTEVHAIPREELLKFTDPEYIVEYFSREAESACKSMGYSIDWRRS
FKTTDPYYDRFIEWQMNKLKELGLIVKGEHPVRYCPKDGNPVEDHDLLSGEGVTIVEYILIKFELEDGAF
YFVAATLRPETVYGVTNCWVNPTITYVIAEVGGEKWITSKEAFENLSYQKLKYKPIEEVPGKQFIGKKVH
NPVVGPEVPILPAEFVDTTKGTGVVMSVPAHAPDDYIALEDLLHDPEYLGIKPVVIDIEPVPLIHTDGYG
DLPAKEIVEEKGIKSQKDKNLLEEATKILYKEEYHTGVMIYNIPPYKGMKVSEAKEKVKADLIDAGLADV
MYEFSESPVICRCGTDCIVKVVEDQWFVKYSDESWKELAHECLEGMRIIPEEVKNAFEGKIDWLKDWACC
RRYGLGTRLPWDEKWLIESLSDSTIYMAYYTIAHYLNKDYYGNEQMTDEFFDYIFLGKGDVKNTNIPLPA
IQKLRREFEYWYPLDWRISGKDLIPNHLTFYIFHHVAIFPEKFWPRGIVVNGYVMLEGKKMSKSKGNVLT
LEQAVEKFGADVARLYIADAAETVQDADWKESEVEGTILRLERLYEFAEEITKESNLETGEETSFIDRWL
ESRMNAAIKETYEAMENFQTRKAVKYALFDLQADVDWYRRRGGVNHKDVLARYLETWIKLLAPFAPHFAE
EMWEEVGNEGFVSLAKFPEASEPAVDKEVEAAEEYLRNLVRDIQEIAKIDASKPKRVYLYTSEDWKSQCL
KIVAELFGEDTGEDMKKVMEEPEERKRGKEVISLVKQIIKDEKKEDELQISEIEVLKAAARFIKKEVGAL
VIIEFSADSFPENKKRNAVPGKPAIYLE
>gnl|CDD|273057 TIGR00396, Leucine--tRNA_ligase, leucyl-tRNA synthetase, eubacterial and mitochondrial family. The leucyl-tRNA synthetases belong to two families so broadly different that they are represented by separate models. This model includes both eubacterial and mitochondrial leucyl-tRNA synthetases. It generates higher scores for some valyl-tRNA synthetases than for any archaeal or eukaryotic cytosolic leucyl-tRNA synthetase. Note that the enzyme from Aquifex aeolicus is split into alpha and beta chains; neither chain is long enough to score above the trusted cutoff, but the alpha chain scores well above the noise cutoff. The beta chain must be found by a model and search designed for partial length matches [Protein synthesis, tRNA aminoacylation]
YNHIEIEEKWQQKWDENKTFKVTDDSSKPKYYILSMFPYPSGALHMGHVRNYTITDVLSRYYRMKGYNVL
HPIGWDAFGLPAENAAIKRGIHPAKWTYENIANMKKQLQALGFSYDWDREIATCDPEYYKWTQWIFLELF
EKGLAYVKEADVNWCPNDGTVLANEQVDSDGRSWRGDTPVEKKELKQWFLKITAYAEELLNDLEELDHWP
ESVKEMQRNWIGKSEGVEITFKIADHDEKITVFTTRPDTIFGVTYLALAPEHPLVEKAAENNPKVAAFIK
KILNKTVAERTKATKEKKGVDTGIKAIHPLTGEKIPIWVANYVLMEYGTGAVMGVPAHDERDFEFAQKYG
LPIKPVIDPAEKDLSLTAAYTEDGVLVNSGEFNGLNSSEARNAIIDMLEKEGKGKRKVNYRLRDWGFSRQ
RYWGEPIPIIHCEDGGVVPVPEEDLPVILPEDVVYDGDGGSPLSRIPEWVNVTCPSCGKPALRETDTMDT
FAGSSWYYLRYLDPKNTDGPFDKEKAEYWLPVDLYIGGIEHAILHLLYARFFHKFLRDIGYVNTKEPFKK
LINQGMVLGFYYPPNGKVPADVLTERDEKGKDKAGGELVYVGYEKMSKSKGNGIDPQEIVESYGADALRL
FIMFMGPIAASLEWNESGLEGARRFLDRVWNLVYEITGELDAASLTVTALEEAQKELRRDVHKFLKKVTE
DLEKRESFNTAISAMMELLNKLYKAKKEALMLEYLKGFVTVLSPFAPHLAEELWEKLGSEPFIIDNAKWP
VVDETALVEDKTLIVVQVNGKFRAKITVPKDADEEQVEELAKQDPEVKKYLENKTIKKVIYVPGKLVNFV
IK
>gnl|CDD|129492 TIGR00397, mauM_napG, MauM/NapG family ferredoxin-type protein. MauM is involved in methylamine utilization. NapG is associated with nitrate reductase activity. The two proteins are highly similar [Energy metabolism, Electron transport]
KPERRDAFADAARAVGVACVGGFFGAALLRSRPAVAARVLRPPGALPEQDFLAACVRCGLCVEACPYDIL
SLASWSDPAPLGTPFFTPREVPCRMCKDIPCARACPTGALDPLLTDIRKADMGVAVLVGHETCLNYKGLN
CSICVRVCPIRGEAISLKPIENERGRLQIPTVDSAKCTGCGTCEKHCVLSEAAIRVLPRELGLGVPGANS
AGR
>gnl|CDD|273058 TIGR00398, Methionine--tRNA_ligase, methionine--tRNA ligase. The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model appears to recognize the methionyl-tRNA synthetase of every species, including eukaryotic cytosolic and mitochondrial forms. The UPGMA difference tree calculated after search and alignment according to this model shows an unusual deep split between two families of MetG. One family contains forms from the Archaea, yeast cytosol, spirochetes, and E. coli, among others. The other family includes forms from yeast mitochondrion, Synechocystis sp., Bacillus subtilis, the Mycoplasmas, Aquifex aeolicus, and Helicobacter pylori. The E. coli enzyme is homodimeric, although monomeric forms can be prepared that are fully active. Activity of this enzyme in bacteria includes aminoacylation of fMet-tRNA with Met; subsequent formylation of the Met to fMet is catalyzed by a separate enzyme. Note that the protein from Aquifex aeolicus is split into an alpha (large) and beta (small) subunit; this model does not include the C-terminal region corresponding to the beta chain [Protein synthesis, tRNA aminoacylation]
ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKY
HEEFKDDWKWLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCP
KCGSEDARGDHCEVCGRHLEPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPAS
NVKNKAQNWLKGGLKDLAITRDLVYWGIPVPNDPNKVVYVWFDALIGYISSLGILSGDTEDWKKWWNNDE
DAELIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFSHGYLTVEGGKMSKSLGNVVDPSDLLARFGADIL
RYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFIKKYFNGVLPSEDITDEEDKKLLKLIN
EALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLKELLAVCSMLIRVLSILLYPIM
PKLSEKILKFLNFELEWDFKLKLLEGHKLNKAEPLFSKIE
>gnl|CDD|273059 TIGR00399, Methionine--tRNA_ligase, methionyl-tRNA synthetase C-terminal region/beta chain. The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model [Protein synthesis, tRNA aminoacylation]
DKKIEELKLKGAKKKEKKDEGEKALEPQKETITIDDFEKVDLRVGKILKAERVEKSDKLLKLKLDLGDEK
RQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDDGKVLFLLSPDQEAIAGERIK
>gnl|CDD|129495 TIGR00400, mgtE, Mg2+ transporter (mgtE). This family of prokaryotic proteins models a class of Mg++ transporter first described in Bacillus firmus. May form a homodimer [Transport and binding proteins, Cations and iron carrying compounds]
NIDIDELILRIRILLKEKSYSKIKEKFLKXQPXDIAEALKRLPGTELILLYRFLPKKIAVDTFSNLDQST
QNKLLNSFTNKEISEMINEMNLDDVIDLLEEVPANVVQQLLASSTEEERKAINLLLSYSDDSAGRIMTIE
YVELKEDYTVGKALDYIRRVAKTKEDIYTLYVTNESKHLKGVLSIRDLILAKPEEILSSIMRSSVFSIVG
VNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDVIQSEATEDFYMIAAVKPLDDSYFDTSILVM
AKNRIIWLLVLLVSSTFTATIISNYEDLLLSLVALANFIPLLMDTSGNAGSQSSAVVIRGLALETVKVKD
FFKVILREICVSILVGAILASVNFLRIVFFQGKLLIAFVVSSSLFVSLTVAKILGGLLPIVAKLLKLDPA
LMSGPLITTIADALTLIIYFNIAKWVLVS
>gnl|CDD|129496 TIGR00401, Peptide_methionine_sulfoxide_reductase_MsrA, methionine-S-sulfoxide reductase. This model describes peptide methionine sulfoxide reductase (MsrA), a repair enzyme for proteins that have been inactivated by oxidation. The enzyme from E. coli is coextensive with this model and has enzymatic activity. However, in all completed genomes in which this module is present, a second protein module, described in TIGR00357, is also found, and in several cases as part of the same polypeptide chain: N-terminal to this module in Helicobacter pylori and Haemophilus influenzae (as in PilB of Neisseria gonorrhoeae) but C-terminal to it in Treponema pallidum. PilB, containing both domains, has been shown to be important for the expression of adhesins in certain pathogens [Protein fate, Protein modification and repair, Cellular processes, Adaptations to atypical conditions]
EIATFAGGCFWGTEKYFRLIPGVVSTAVGYTNGYTPNPTYEEVCSGDTGHAEAVQVTYDPKVISYEELLD
VFWEIHDPTTGNRQGNDIGTQYRSGIYYHSDAQEKAAAASKERLQAAANYGDPIVTEIEPAENFYYAEEY
HQQYLKKNP
>gnl|CDD|273060 TIGR00402, Uncharacterized_protein_HI_1043, ferredoxin-type protein NapF. The gene codes for a ferredoxin-type cytosolic protein, NapF, of the periplasmic nitrate reductase system, as in Escherichia coli. NapF interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation [Energy metabolism, Electron transport]
RRGLLRGVFPATSSTIEKTQIRPPWSARESLFSAVCTRCGECASACENNILQLGQQGQPTVEFDNAECDF
CGKCAEACPTNAFHPRFPGDWLLRPQISSAC
>gnl|CDD|129498 TIGR00403, NADPH-quinone_oxidoreductase_subunit_I, NADH-plastoquinone oxidoreductase subunit I protein [Energy metabolism, Electron transport]
MFNILKGVGDYAQQSIQAARYIGQGFAVTLDHMNRLPITIQYPYEKLIPSERFRGRIHFEFDKCIACEVC
VRVCPINLPVVDWEFNKAIKKKQLKNYSIDFGVCIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYDQI
ALGRLPISITEDPTITPIRNLTYLPKGVIEPHKGSRRITQHPE
>gnl|CDD|129499 TIGR00405, Transcription_elongation_factor_Spt5, transcription elongation factor Spt5. This protein contains a KOW domain, shared by bacterial NusG and the uL24 (previously L24p/L26e) family of ribosomal proteins. The most recent papers and crystal structures make this a transcription elongation factor rather than a ribosomal protein
FAVKTSVGQEKNVARLMARKARKSGLEVYSILAPESLKGYILVEAETKIDMRNPIIGVPHVRGVVEGEID
FEEIERFLTPKKIIESIKKGDIVEIISGPFKGERAKVIRVDESKEEVTLELIEAAVPIPVTVKGDQVRII
QKEAD
>gnl|CDD|273061 TIGR00406, Ribosomal_protein_L11_methyltransferase, ribosomal protein L11 methyltransferase. Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis [Protein synthesis, Ribosomal proteins: synthesis and modification]
WIEIRINTTKELAEATSDALEEAGAVGVTFEDDKDTIYFEPHLPGEKRLWGNLDVIALFDAETDMNNSVI
PLLEAFCLDLGRNHKIEFDEFSKDWERAWKDNFHPVQFGKRFWICPSWRDVPSDEDALIIMLDPGLAFGT
GTHPTTSLCLEWLEDLDLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVSDR
LQVKLIYLEQPIEGKADVIVANILAEVIKELYPQFSRLVKPGGWLILSGILETQAQSVCDAYEQGFTVVE
IRQREEWC
>gnl|CDD|161862 TIGR00407, Gamma-glutamyl_phosphate_reductase, gamma-glutamyl phosphate reductase. The related model TIGR01092 describes a full-length fusion protein delta l-pyrroline-5-carboxylate synthetase that includes a gamma-glutamyl phosphate reductase region as described by this model. Alternate name: glutamate-5-semialdehyde dehydrogenase. The prosite motif begins at residue 332 of the seed alignment although not all of the members of the family exactly obey the motif [Amino acid biosynthesis, Glutamate family]
AKQAANILAQLSTAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENGLADALLDRLLLTEGRLKGIAD
GVKDVIELADPVGKVIDGRELDSGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEA
VRSNKALVEVIQDALAQTGLPVGAVQLIETPSRELVSELLDLDEYIDLLIPRGGNGLVRLIKQTSTIPVL
GHGDGICHIYLDESADLIKAIKVIVNAKTQRPSTCNAIETLLVNKAIAREFLPVLENQLLEKGVTIHADA
YALKLLELGPATEAIVCKTDFDKEFLSLDLSVKIVESLEAAIQHINQYGTQHSDAILTENKANAEQFQNG
VDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTSYK
>gnl|CDD|273062 TIGR00408, Proline--tRNA_ligase, prolyl-tRNA synthetase, family I. Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae [Protein synthesis, tRNA aminoacylation]
MASKMQDFSEWYHQILEKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESE
LAKEKDHIKGFEPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETK
HTRPFLRTREFTWQEAHTAHATAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFE
TIMPDGRTLQIATSHNLGQNFAKTFEIKFETPTGDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRV
APIQVVIIPIIFKKKENEKVMEAAREVRSRLKKAGFRVHIDDRDNRPGRKFYQWEIKGIPLRIEVGPNDI
EKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAWERFEQKIVIVETLEEIKQALNEKRGVV
LVPWCGEEECEEDLKEKVQVTILCIPEDGDVLQLCIFCGRKAPDYVLIARTY
>gnl|CDD|273063 TIGR00409, Proline--tRNA_ligase, prolyl-tRNA synthetase, family II. Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent groups. This group includes enzymes from Escherichia coli, Bacillus subtilis, Aquifex aeolicus, the spirochete Treponema pallidum, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. The other group includes the Pro-specific domain of a human multifunctional tRNA ligase and the prolyl-tRNA synthetases from the Archaea, the Mycoplasmas, and the spirochete Borrelia burgdorferi [Protein synthesis, tRNA aminoacylation]
MRTSQYLFPTLKETPADAEVKSHQLLLRAGFIRRLGSGLYNWLPLGLRVLKKVENIVREEMNKDGAIEVL
LPALQPAELWQESGRWDTYGPELLRLKDRKGREFVLGPTHEEVITDLARNEIKSYKQLPLNLYQIQTKFR
DEIRPRFGLMRGREFIMKDAYSFHSDEESLDATYQKMYQAYSNIFSRLGLDFRPVQADSGAIGGSASHEF
MVLAESGEDTIVYSDESDYAANIELAEALAPGERNAPTAELDKVDTPNTKTIAELVECFNLPAEKVVKTL
LVKAVDKSEPLVALLVRGDHELNEVKAPNLLLVAQVLELATEEEIFQKIASGPGSLGPVNINGGIPVLID
QTVALMSDFAAGANADDKHYFNVNWDRDVAIPEVADIRKVKEGDPSPDGQGTLKIARGIEVGHIFQLGTK
YSEALKATFLDENGKNQFMTMGCYGIGVSRLVSAIAEQHHDERGIIWPKAIAPYDVVIVVMNMKDEEQQQ
LAEELYSELLAQGVDVLLDDRNERAGVKFADSELIGIPLRVVVGKKNLDNGEIEVKKRRNGEKQLIKKDE
LVECLEEQ
>gnl|CDD|273064 TIGR00410, NN'-diacetylchitobiose_permease_IIC_component, PTS system, lactose/cellobiose family IIC component. Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. This family of proteins consists of both the cellobiose specific and the lactose specific forms of the phosphotransferase system (PTS) IIC component. The IIC domain catalyzes the transfer of a phosphoryl group from the IIB domain to the substrate. When the IIC component and IIB components are in the same polypeptide chain they are designated IIBC [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
LVPIAGKIGGQRHLQALRDGFILTMPLTIIGSFFLLLTNLPFPGLADFMAIEFLNSWKGKLGYPVNATMG
IMSLFAVFGIGYRLAESYKVDALSAGAISLAAFLLLTPQSVPFSVDGATEAIMVGGVIPANLLGAKGLFV
AMIIALVSTEIYRFIVQKNLVIKMPDGVPPAVSKSFVALIPGFIILSVMWLINLAIESTPGTNFHNIIMD
LIGTPLSILGSSLGGTLVAEFFVMLLWFCGLHGANIIGALMNPIWYGAMDENIAAYQAGEELPHIFAKPF
LDIFVNIGGSGATLALVLTMFIRSRSKQMKQVGKLALAPGIFNINEPIIFGLPIVMNPILIIPFVLAPLV
TITVTYIAMSTGLVPPPVGIAVPWTMPPGISGFFATGGSVSGAVMQLINLLISFVIYLPFFKAWDKAKLA
EEK
>gnl|CDD|129505 TIGR00411, Probable_Thioredoxin, small redox-active disulfide protein 1. This protein is homologous to a family of proteins that includes thioredoxins, glutaredoxins, protein-disulfide isomerases, and others, some of which have several such domains. The sequence of this protein at the redox-active disufide site, CPYC, matches glutaredoxins rather than thioredoxins, although its overall sequence seems closer to thioredoxins. It is suggested to be a ribonucleotide-reducing system component distinct from thioredoxin or glutaredoxin [Unknown function, General]
VKIELFTSPTCPYCPAAKRVVEEVAKEMGDAVEVEYINVMENPQKAMEYGIMAVPAIVINGDVEFIGAPT
KEELVEAIKKRL
>gnl|CDD|129506 TIGR00412, Uncharacterized_protein_MJ0581, small redox-active disulfide protein 2. This small protein is found in three archaeal species so far (Methanococcus jannaschii, Archeoglobus fulgidus, and Methanobacterium thermoautotrophicum) as well as in Anabaena PCC7120. It is homologous to thioredoxins, glutaredoxins, and protein disulfide isomerases, and shares with them a redox-active disulfide. The redox active disulfide region CXXC motif resembles neither thioredoxin nor glutaredoxin. A closely related protein found in the same three Archaea, described by redox_disulf_1, has a glutaredoxin-like CP[YH]C sequence; it has been characterized in functional assays as redox-active but unlikely to be a thioredoxin or glutaredoxin [Unknown function, General]
MKIQIYGTGCANCQMTEKNVKKAVEELGIDAEFEKVTDMNEILEAGVTATPGVAVDGELVIMGKIPSKEE
IKEILK
>gnl|CDD|273065 TIGR00413, RlpA-like_protein, rare lipoprotein A. This is a family of prokaryotic proteins with unknown function. Lipoprotein annotation based on the presence of consensus lipoprotein signal sequence. Included in this family is the E. coli putative lipoprotein rlpA [Cell envelope, Other]
GLASWYGPKFHGRKTANGEVYNMKALTAAHKTLPFNTYVKVTNLHNNRSVIVRINDRGPFSDDRIIDLSH
AAAREIGLISRGVGQVRIEVLHVAKNGNLSGAATKTFNKQAKKQEAKDRLVLESNTLFDNTKKSINALKG
TEFFCLQMGELRSRSQANKLITQLALANLQTEVNRSGPKYEVYIGPFDDKTKMAQVRTKSQKMANNLI
>gnl|CDD|273066 TIGR00414, Serine--tRNA_ligase, seryl-tRNA synthetase. This model represents the seryl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. The seryl-tRNA synthetases of two archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model [Protein synthesis, tRNA aminoacylation]
MLDRKLLRNNPDLVKESLKARGLSVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDK
IEEIKKELKELKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPK
PHWELGEKLGGLDFDRAVKVTGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTG
QLPKFEEDIFKLEDTDLYLIPTAEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVH
QFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYRE
ISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGRTIVAILENYQTEDGSVEIPEVLRKYL
>gnl|CDD|129509 TIGR00415, Type-2_serine--tRNA_ligase, seryl-tRNA synthetase, Methanococcus jannaschii family. The seryl-tRNA synthetases from a few of the Archaea, represented by this model, are very different from the set of mutually more closely related seryl-tRNA synthetases from Eubacteria, Eukaryotes, and other Archaea. Although distantly homologous, the present set differs enough not to be recognized by the pfam model tRNA-synt_2b that recognizes the remainder of seryl-tRNA synthetases among oither class II amino-acyl tRNA synthetases [Protein synthesis, tRNA aminoacylation]
LKFDLDGIIIFSKELPEEADDAEEEFLEAADDIFLKGVPEGKEHEAAHIKSWEFEGDILHIEIASGRRTR
AHDGLIRLKKPLAEKLGPKFRIGVRGIEIDDYTIEIEADGEDGAKKLAEIKFPECAAITDGNKIILRFKD
IEESDLKKHIFDRAIKFAKTELEKEDEDLTFKVCKAPPGEIIAESKAKRDFFFDGDPTDEAEKLGWVKKF
PGRGQWFYGPKITALFRALEEFFIEEIVKKIGFQECLFPKLIPLDIMNKMRYLEGLPEGMYYCCAPKRDP
ELFEEFKNELIIKKEIPIDKLKNGIKDPGYVIAPAQCEPFYQFFEGEVIDAEDKPIKFFDRSGWTYRWEA
GGAKGLDRVHEFLRVECVWIAEPEETEEIRDKTLELAEDAADELDLEWWTEVGDDPFYLEGRKKEDRGIE
FPDVPKYEMRLSLPGIEDERKGVAVTSANVHGTHFIEGFRIKDAKGLNIWTGCTGIGISRWIVGFLAQKG
FEFDDWHDFIGEKIEGLPENPQIITWPKKD
>gnl|CDD|273067 TIGR00416, DNA_repair_protein_RadA_homolog, DNA repair protein RadA. The gene protuct codes for a probable ATP-dependent protease involved in both DNA repair and degradation of proteins, peptides, glycopeptides. Also known as sms. Residues 11-28 of the SEED alignment contain a putative Zn binding domain. Residues 110-117 of the seed contain a putative ATP binding site both documented in Haemophilus (SP:P45266) and in Listeria monocytogenes (SP:Q48761) . for E.coli see (J. BACTERIOL. 178:5045-5048(1996)) [DNA metabolism, DNA replication, recombination, and repair]
MAKAKSKFVCQHCGADSPKWQGKCPACHAWNTITEERLHRSLGAQKNRRNSGKAGIPQAQKSQTISAIEL
EEVPRFSSGFGELDRVLGGGIVPGSLILIGGDPGIGKSTLLLQVACQLAKNQMKVLYVSGEESLQQIKMR
AIRLGLPEPNLYVLSETNWEQICANIEEENPQACVIDSIQTLYSPDISSAPGSVSQVRECTAELMRLAKT
RGIAIFIVGHVTKEGSIAGPKVLEHMVDTVLYFEGDRDSRFRILRSVKNRFGATNEIGIFEMTEQGLREV
LNPSAIFLSRREEPMSGSSITVTWEGTRPLLVEIQALVSPTSFANPRRVATGLDQNRLALLLAVLEKRLG
LPLADQDVFLNVAGGVKVSEPAADLALLIAIVSSFRDRPLDPDLVFLGEVGLAGEIRPVPSLEERLKEAA
KLGFKRAIVPKANSPKTAPEGIKVIGVKKVGDAL
>gnl|CDD|188048 TIGR00417, Polyamine_aminopropyl_transferase, spermidine synthase. the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine + S-adenosylmethioninamine = spermidine + 5'-methylthioadenosine) and is involved in polyamine biosynthesis and in the biosynthesis of spermidine from arganine. The region between residues 77 and 120 of the seed alignment is thought to be involved in binding to decarboxylated SAM [Central intermediary metabolism, Polyamine biosynthesis]
WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTH
PNPKHVLVIGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLA
DTENTFDVIIVDSTDPVGPAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPIT
EYYTAAIPTYPSGLWTFTIASKNKYRPLEVEIRRIKFEAEDGKTKYYNPDIHKAAFVLPKW
>gnl|CDD|273068 TIGR00418, Threonine--tRNA_ligase, threonyl-tRNA synthetase. This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether.  [Protein synthesis, tRNA aminoacylation]
RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSL
EEALEAFKVLEPYKLELLDEIPNGVKRTPYGWGKAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKN
KMLQRIYGTAWADKKQLAAYLLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFV
RQKQIKYGYMEVETPIMYDLELWEISGHWDNYKERMFPFTELDNREFMLKPMNCPGHFLIFKSSLRSYRD
LPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYEL
STRDPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDFAFKDALGREWQCATVQLDFEL
PERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVNERHLDYAKKVA
QKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLEKLR
KEV
>gnl|CDD|129513 TIGR00419, Triosephosphate_isomerase, triosephosphate isomerase. Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. The active site of the enzyme is located between residues 240-258 of the model ([AV]-Y-E-P-[LIVM]-W-[SA]-I-G-T-[GK]) with E being the active site residue. There is a slight deviation from this sequence within the archeal members of this family [Energy metabolism, Glycolysis/gluconeogenesis]
LVIGNWKTYNESRGMRALEVAKIAEEVASEAGVAVAVAPPFVDLPMIKREVEIPVYAQHVDAVLSGAHTG
EISAEMLKDIGAKGTLINHSERRMKLADIEKKIARLKELGLTSVVCTNNVLTTAAAAALEPDVVAVEPPE
LIGTGIPVSPAQPEVVHGSVRAVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD
>gnl|CDD|273069 TIGR00420, tRNA-specific_2-thiouridylase_MnmA, tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase. tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea [Protein synthesis, tRNA and rRNA base modification]
KKVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDKNDGHGCTSAEDLRDAQAICEKLGIPLEKVN
FQKEYWNKVFEPFIQEYKEGRTPNPDILCNKFIKFGAFLEYAAELLGNDKIATGHYARIAEIEGKSLLLR
ALDKNKDQSYFLYHLSHEQLAKLLFPLGELLKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKY
LPVKPGVIITVDGQSVIGEHDGLWFYTIGQRKGLGIGGAAEPWFVVEKDLETNELVVSHGKPDLASRGLL
AQQFHWLDDEPNPFEMRCTVKIRYRQVPVQCKLKLLDDNLIEVIFDEPQAGVTPGQSAVLYKGDICLGGG
II
>gnl|CDD|129515 TIGR00421, UbiX family flavin prenyltransferase. UbiX partners with UbiD for decarboxylation of the 3-octaprenyl-4-hydroxybenzoate precursor during ubiquinone biosynthesis, but the role of UbiX is as a flavin prenyltransferase that provides a cofactor UbiD requires.In E.coli, the protein UbiX (3-octaprenyl-4-hydroxybenzoate carboxy-lyase) has been shown to be involved in the third step of ubiquinone biosynthesis, the reaction [3-octaprenyl-4-hydroxybenzoate = 2-octaprenylphenol + CO2]. The knockout of the homologous protein in yeast confers sensitivity to phenylacrylic acid. Members are not restricted to ubiquinone-synthesizing species. This family represents a distinct clade within the flavoprotein family of pfam02441
RIVVAMTGASGVIYGIRLLEVLKEAGVEVHLVISDWAKETIKYETDIDPGEVEELATKYYDADDFAAPIA
SGSFPFDGMVVVPCSMKTLSAIANGYADNLITRAADVCLKERRKLVLVPRETPLNSIHLENMLRLSRMGA
IILPPMPAFYTRPKSVEDMIDFIVGRVLDQLGIENDLFRRW
>gnl|CDD|273070 TIGR00422, Valine--tRNA_ligase, valyl-tRNA synthetase. The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase [Protein synthesis, tRNA aminoacylation]
MPKDYDPHEVEKKWYKKWEKSGFFKPDGNSNKPPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKG
YNVLWLPGTDHAGIATQVKVEKKLGAEGKTKHDLGREEFREKIWEWKEESGGTIKNQIKRLGASLDWSRE
RFTMDEGLSKAVKEAFVRLYEKGLIYRGEYLVNWDPKLNTAISDIEVEYKEVKGKLYYIRYPLANGSKDY
LVVATTRPETMFGDTAVAVHPEDERYKHLIGKKVILPLTGRKIPIIADEYVDMEFGTGAVKVTPAHDFND
YEWGKRHNLEFINILDEDGLLNENAGKYQGLTRFEARKKIVEDLKEEGLLVKIEPHTHNVGTCWRSGTVV
EPLLSKQWFVKVEKLADKALEAAEEGEIKFVPKRMEKRYLNWLRNIKDWCISRQLIWGHRIPVWYCKECG
EVYVAKEEPLPDDKTNTGPSVELEQDTDVLDTWFSSSLWPFSTLGWPDETKDLKKFYPTDLLVTGYDIIF
FWVARMIFRSLALTGQVPFKEVYIHGLVRDEQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGD
DINFDWKRVESARNFLNKLWNASRFVLMNLSDDLELSGGEEKLSLADRWILSKLNRTIKEVRKALDKYRF
AEAAKALYEFIWNDFCDWYIELVKYRLYNGNEAEKKAARDTLYYVLDKALRLLHPFMPFITEEIWQHFKE
GADSIMLQSYPVVDAEFVDEEAEKAFELLKEIIVSIRNLKAESNIPPNAPLKVLLIYTEAETAERLKLNA
VDIKGAINFSEVEVVIEKPEVTEAVVELVPGFEIIIPVKGLINKAKELARLQKQLDKEKKEVIRIEGKLE
NEGFVKKAPKEVIEKEKEKLE
>gnl|CDD|273071 TIGR00423, FO_synthase_subunit_2, radical SAM domain protein, CofH subfamily. This protein family includes the CofH protein of coenzyme F(420) biosynthesis from Methanocaldococcus jannaschii, but appears to hit genomes more broadly than just the subset that make coenzyme F(420), so that narrower group is being built as a separate family [Hypothetical proteins, Conserved]
VTFVVNRNINFTNICVGKCKFCAFRAREKDKDAYVLSLEEILEKVKEAVAKGATEVCIQGGLNPQLDIEY
YEELFRAIKQEFPDVHIHAFSPMEVYFLAKNEGLSIEEVLKRLKKAGLDSMPGTGAEILDDSVRRKICPN
KLSSDEWLEVIKTAHRLGIPTTATMMFGHVENPEHRVEHLLRIRKIQEKTGGFTEFIPLPFQPENNPYLE
GEVRKGASGIDDLKVIAISRILLNNIRNIQASWVKLGLKLAQVALEFGANDLGGTLMEENISKAAGAKSG
VGLTVEELIEAIKDAGRVPAQRDTLYNIL
>gnl|CDD|273072 TIGR00424, APS_reductase, 5'-adenylylsulfate reductase, thioredoxin-independent. This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis [Central intermediary metabolism, Sulfur metabolism]
MALAVTSSSTAISGISLSRSGESTEAKAAQIGSFRLLDRPHTISPSVNLSRRRLSVKPLNAEPKRNESIV
PSAATTVAPEVEEKVVEVEDFEKLAKKLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRP
FRVFSLDTGRLNPETYRFFDAVEKQYGIRIEYMFPDAVEVQALVRSKGLFSFYEDGHQECCRVRKVRPLR
RALKGLKAWITGQRKDQSPGTRSEIPVVQVDPVFEGLDGGVGSLVKWNPVANVEGKDVWNFLRTMDVPVN
TLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNIKEETLDGAVNGNGSDAVADIFDS
NNVVSLSRPGIENLLKLEERKEAWLVVLYAPWCPFCQAMEASYLELAEKLAGSGVKVAKFRADGDQKEFA
KQELQLGSFPTILFFPKHSSRPIKYPSEKRDVDSLMSFVNLLR
>gnl|CDD|273073 TIGR00425, Probable_tRNA_pseudouridine_synthase_B, rRNA pseudouridine synthase, putative. This family, found in archaea and eukaryotes, includes the only archaeal proteins markedly similar to bacterial TruB, the tRNA pseudouridine 55 synthase. However, among two related yeast proteins, the archaeal set matches yeast YLR175w far better than YNL292w. The first, termed centromere/microtubule binding protein 5 (CBF5), is an apparent rRNA pseudouridine synthase, while the second is the exclusive tRNA pseudouridine 55 synthase for both cytosolic and mitochondrial compartments. It is unclear whether archaeal proteins found by this model modify tRNA, rRNA, or both [Protein synthesis, tRNA and rRNA base modification]
LKNFENLIVKEEHYTNIDYGCNPLKRDIEEYISYGVVNLDKPSGPSSHEVVAWVRRILNVEKTGHGGTLD
PKVTGVLPVCIERATRLVKSQQEAPKEYVCLMRLHRDAKEEDILRVLKEFTGRIFQRPPLKSAVKRQLRV
RTIYESELLEKDGKDVLFRVSCEAGTYIRKLCVDIGEALGTGAHMQELRRTRSGCFGEDDMVTLHDLLDA
YVFWKEDGDESYLRRIIKPMEYLLRHLKRVVVKDSAVDAICHGADLMVRGIARLEKGIEKGDTVVVITLK
GEAVAVGIALMSTKDIANADKGVVADVKRVIMERGTYPRMWK
>gnl|CDD|129520 TIGR00426, Hypothetical_protein_ybaV_precursor., competence protein ComEA helix-hairpin-helix repeat region. Members of the subfamily recognized by this model include competence protein ComEA and closely related proteins from a number of species that exhibit competence for transformation by exongenous DNA, including Streptococcus pneumoniae, Bacillus subtilis, Neisseria meningitidis, and Haemophilus influenzae. This model represents a region of two tandem copies of a helix-hairpin-helix domain (pfam00633), each about 30 residues in length. Limited sequence similarity can be found among some members of this family N-terminal to the region covered by this model [Cellular processes, DNA transformation]
SDEEGTRVNINTATAEELQRAMNGVGLKKAEAIVSYREEYGPFKTVEDLKQVPGIGNSLVEKNLAVITL
>gnl|CDD|129521 TIGR00427, UPF0056_membrane_protein_AF_2111, membrane protein, MarC family. MarC is a protein that spans the plasma membrane multiple times and once was thought to be a multiple antibiotic resistance protein. The function for this family is unknown [Unknown function, General]
MDILSFYFKFFISLFAIINPIGNIPIFISLTEYYTAAERNKIAKKANISSFIILLIFLVFGDTILKLFGI
SIDAFRIAGGILLFTIAMDMLSGEGEDKQHKDEKEESAEIDSIAVVPLALPLIAGPGAITTTMVLGARAS
SIGYKFLVVLAIALVALITWLLFRYSAFIIRRLGRTGINVITRIMGLLLAAIAVEFIVTGI
>gnl|CDD|129522 TIGR00430, Queuine_tRNA-ribosyltransferase, tRNA-guanine transglycosylase. This tRNA-guanine transglycosylase (tgt) catalyzes an exchange for the guanine base at position 34 of many tRNAs; this nucleotide is subsequently modified to queuosine. The Archaea have a closely related enzyme that catalyzes a base exchange for guanine at position 15 in some tRNAs, a site that is subsequently converted to the archaeal-specific modified base archaeosine (7-formamidino-7-deazaguanosine), while Archaeoglobus fulgidus has both enzymes [Protein synthesis, tRNA and rRNA base modification]
FELQKTDKHARVGKLNTPHGSVETPVFMPVGTLGTVKGLTPEELEATGAEIILANTYHLWLRPGQKIVKE
LGGLHKFMQWDGPILTDSGGFQVFSLSDLRKIEEEGVHFKSPIDGSKIFLTPEKSMEIQYALGSDIIMAF
DECTPYPADRDYAEKSTERTLRWAERCLEAHDRRGNKQALFGIVQGGTYEDLRSQSAEGLIELDFPGYAI
GGLSVGEPKEDMLRILEHTAPLLPKDKPRYLMGVGTPEDLLNAIRRGIDMFDCVMPTRNARNGTLFVTEG
RINIKNAKYKDDTRPLDEECDCYTCKNYSRAYLRHLIRCNELLGARLATLHNLHFYLRLMEKIRQAILED
RFLSFRTEFLERYGEEVP
>gnl|CDD|129523 TIGR00431, tRNA_pseudouridine_synthase_B, tRNA pseudouridine(55) synthase. TruB, the tRNA pseudouridine 55 synthase, converts uracil to pseudouridine in the T loop of most tRNAs in all three domains of life. This model is built on a seed alignment of bacterial proteins only. Saccharomyces cerevisiae protein YNL292w (Pus4) has been shown to be the pseudouridine 55 synthase of both cytosolic and mitochondrial compartments, active at no other position on tRNA and the only enzyme active at that position in the species. A distinct yeast protein YLR175w, (centromere/microtubule-binding protein CBF5) is an rRNA pseudouridine synthase, and the archaeal set is much more similar to CBF5 than to Pus4. It is unclear whether the archaeal proteins found by this model are tRNA pseudouridine 55 synthases like TruB, rRNA pseudouridine synthases like CBF5, or (as suggested by the absence of paralogs in the Archaea) both. CBF5 likely has additional, eukaryotic-specific functions. The trusted cutoff is set above the scores for the archaeal homologs of unknown function, so yeast Pus4p scores between trusted and noise [Protein synthesis, tRNA and rRNA base modification]
INGVLLLDKPQGMTSFDALAKVRRLLNVKKVGHTGTLDPFATGVLPILVGKATKLSPYLTDLDKEYRAEI
RLGVRTDTLDPDGQIVETRPVNPTTEDVEAALPTFRGEIEQIPPMYSALKVNGKRLYEYARQGIEVERKA
RPVTVYDLQFLKYEGPELTLEVHCSKGTYIRTLARDLGEKLGCGAYVSHLRRTAVGDFPLDQSVTLEEL
>gnl|CDD|273074 TIGR00432, tRNA-guanine15_transglycosylase, tRNA-guanine(15) transglycosylase. This tRNA-guanine transglycosylase (tgt) differs from the tgt of E. coli and other Bacteria in the site of action and the modification that results. It exchanges 7-cyano-7-deazaguanine (preQ0) with guanine at position 15 of archaeal tRNA; this nucleotide is subsequently converted to archaeosine, found exclusively in the Archaea. This enzyme from Haloferax volcanii has been purified, characterized, and partially sequenced and is the basis for identifying this family. In contrast, bacterial tgt (TIGR00430) catalyzes the exchange of preQ0 or preQ1 for the guanine base at position 34; this nucleotide is subsequently modified to queuosine. Archeoglobus fulgidus has both enzymes, while some other Archaea have just this one [Protein synthesis, tRNA and rRNA base modification]
AEIIEFQRHIGSDIGTPLDIPTPPDVDYARAESELEITLERARESIELLEGAENLLNVPVQGSTHPDLRR
FAAGEAAKLGGDIYPIGAVVPLMEAYRYRDLARVILESRSALPPVEPIHLFGCGHPMLFALAVALGCDLF
DSAAYALYAKDDRYLTVYGTKKLEELNLQYFPCSCPVCSNYTPEELRRMEKNERERLIAEHNLYVSFQEI
ETIKQAIKDGSLFELVEERVRAHPNLLEGYRQVKHYWDLIEKFDPRKKKSAFFYTGIESLYRPEVRRHVK
RIKNVELEEEVLVSYSSSDFGIYGGFSSLRPQSANVIYLDPVFGPIPAEMDEVYPLGQAEIPEEDDVEEE
ALKAAVEALMDLDAIVDDALMNSHPEKRFKVYVSKVETTVDDLDRVRWMKHYQNGPPNGELNVLSDVRIE
RSRNTGKIRHIYAGDELICTMRASDGLLVLGAEGAVRLHKGTDYPAWRVAVNEESEPFARKGKSVFAKFI
IDCDNNIRANDEVLIVNADDELLATGKALLCAEEMMDLNHGQAVKTRGGF
>gnl|CDD|273075 TIGR00433, biotin_synthase, biotin synthase. Catalyzes the last step of the biotin biosynthesis pathway. All members of the seed alignment are in the immediate gene neighborhood of a bioA gene [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
LELPDEPLLDLLAAAQRIRRHFFGNKVDLCSIINAKSGGCPEDCKYCAQSAHYKTGIEKYPLLSVEEVLE
AAKKAKAAGATRFCMVTSGRGPSDREFEKVLEAIREIKEETGLEVCASLGLLSEEQAQRLKEAGVDRYNH
NLETSPSYYPNICTTHTYDDRLETLKRARKAGLSVCSGGIIGMGETMEDRIELAFALAELDVDSVPINFL
VPIPGTPLEDAPPLDPEECLRTIALFRFIMPDAEIRLAGGRELMLRELQALCFLAGANSIFTGDYLTTAG
PEAEEDLEMIEDLGLE
>gnl|CDD|129526 TIGR00434, Phosphoadenosine_phosphosulfate_reductase, phosophoadenylyl-sulfate reductase (thioredoxin). This enzyme, involved in the assimilation of inorganic sulfate, is designated cysH in Bacteria and MET16 in Saccharomyces cerevisiae. Synonyms include phosphoadenosine phosphosulfate reductase, PAPS reductase, and PAPS reductase, thioredoxin-dependent. In a reaction requiring reduced thioredoxin and NADPH, it converts 3(prime)-phosphoadenylylsulfate (PAPS) to sulfite and adenosine 3(prime),5(prime) diphosphate (PAP). A related family of plant enzymes, scoring below the trusted cutoff, differs in having a thioredoxin-like C-terminal domain, not requiring thioredoxin, and in having a preference for 5(prime)-adenylylsulfate (APS) over PAPS [Central intermediary metabolism, Sulfur metabolism]
AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYPLNIK
VYKPDLSLAEQAAKYGDKLWEQDPNKYDYLRKVEPMHRALKELHASAWFTGLRRDQGPSRANLSILNIDE
KFGILKVLPLIDWTWKDVYQYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKTECGL
HE
>gnl|CDD|273076 TIGR00435, Cysteine--tRNA_ligase, cysteinyl-tRNA synthetase. This model finds the cysteinyl-tRNA synthetase from most but not from all species. The enzyme from one archaeal species, Archaeoglobus fulgidus, is found but the equivalent enzymes from some other Archaea, including Methanococcus jannaschii, are not found, although biochemical evidence suggests that tRNA(Cys) in these species are charged directly with Cys rather than through a misacylation and correction pathway as for tRNA(Gln) [Protein synthesis, tRNA aminoacylation]
LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDID
DKIIKRARENGESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGD
VYFDVSKFKDYGKLSKQDLDQLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSA
MNDKYLGDQIDIHGGGVDLIFPHHENEIAQSEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVL
KNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYKALRVLDTSLAYSGNQSLNKFPDEKEFEARF
VEAMDDDLNTANALAVLFELAKSINLTFVSKADAALLIEHLIFLESRLGLLLGLPSKPVQAGSNDDLGEI
EALIEERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTWRR
>gnl|CDD|129528 TIGR00436, GTPase_Era, GTP-binding protein Era. Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein [Protein synthesis, Other]
GFVAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFHEKKHSLNRLMM
KEARSAIGGVDLILFVVDSDQWNGDGEFVLTKLQNLKRPVVLTRNKLDNKFKDKLLPLIDKYAILEDFKD
IVPISALTGDNTSFLAAFIEVHLPEGPFRYPEDYVTDQPDRFKISEIIREKIIRYTKEEIPHSVRVEIER
KSFNEKGLLKIHALISVERESQKKIIIGKNGSMIKAIGIAARKDILELFDCDVFLELFVK
>gnl|CDD|273077 TIGR00437, Ferrous_iron_transport_protein_B_homolog, ferrous iron transporter FeoB. FeoB (773 amino acids in E. coli), a cytoplasmic membrane protein required for iron(II) update, is encoded in an operon with FeoA (75 amino acids), which is also required, and is regulated by Fur. There appear to be two copies in Archaeoglobus fulgidus and Clostridium acetobutylicum [Transport and binding proteins, Cations and iron carrying compounds]
GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGIYSLTTFSLEEEVARDYLLN
EKPDLVVNVVDASNLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEERLGVPVVPTSATEG
RGIERLKDAIRKAIGLKELKKRAIEIVPEAYQVVEVVEGLIEIIYSISKRGLEILLGLLEDLSLEIEKIE
RNLAEVVIKESPSNLSPTEIADEDRVLVEKSIGRKILDRFLGLPIFLFVMFILFLLTFLVGQPLVDLIET
GFSFLSEAVKSFIGNYWLASLLGDGLIGGVGAVLSFVPLIAILFLALSFLEDSGYLARAAFLMDGIMNKF
GLSGRAFIPLILGFGCNVPAIMATRTLETRRERLLTALVIPFMSCSARLPVIVLLFAAAFPGKYGGIVIF
SLYLLGFVAALITARLLPGEVFKGERSPFIMELPPYRLPRFRVVFIQTWTRLRSFIKKAGTIIVIGSVLI
WFLSSFPGGKILESWLAAIGSIMAPLFVPLGKILDWFASVALIFGFVAKEVVVATLGVLYGLGNILSSIG
HAMVPVEALSYMLFVLLYVPCLATLAAIARE
>gnl|CDD|273078 TIGR00438, Ribosomal_RNA_large_subunit_methyltransferase_E, cell division protein FtsJ. Methylates the 23S rRNA. Previously known as cell division protein ftsJ.// Trusted cutoff too high? [SS 10/1/04] [Protein synthesis, tRNA and rRNA base modification]
DFYYQKAKKEKYRSRASFKLLQLNQKFKLIKPGDTVLDLGAAPGGWSQVAVEQVGGKGRVIAVDLQPMKP
IENVDFIRGDFTDEEVLNKIRERVGDDKVDVVMSDAAPNISGYWDIDHLRSIDLVELALDIAKEVLKPKG
NFVVKVFQGEEIDEYLNELRKLFEKVKVTKPQASRKRSAEVYIVAKRF
>gnl|CDD|129531 TIGR00439, Cell_division_protein_FtsX, putative protein insertion permease FtsX. FtsX is an integral membrane protein encoded in the same operon as signal recognition particle docking protein FtsY and FtsE. It belongs to a family of predicted permeases and may play a role in the insertion of proteins required for potassium transport, cell division, and other activities. FtsE is a hydrophilic nucleotide-binding protein that associates with the inner membrane by means of association with FtsX [Cellular processes, Cell division, Protein fate, Protein and peptide secretion and trafficking]
SIIHYASVFSLQVEYARSALKQDLRQQPFGTLLTLIVIAVSLTLPLVMYLGIKNGQSALTQLYPSPQITV
YLEKALAQSDADTVVSLLTRDKGVENINYISREDGLAEFQSWSGFGNLLSMLDGNPLPAVFIVTPDPAFT
PAEMQAILRDNITKIPGVEEVRMDTEWVQTLYALNELIRKVLWFLSVLMGMAVFLVIGNSIRLQILSRRE
SIEVTKLLGATDSFILRPFLYQGMWQSIFGALVSLILSGWLLSAVRSAVDAVFKPFGLNFGWNGLYVGEL
GLLLGFCIALGVVGAWLATTQHLLCFKAK
>gnl|CDD|273079 TIGR00440, Glutamine--tRNA_ligase, glutaminyl-tRNA synthetase. This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases [Protein synthesis, tRNA aminoacylation]
VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKI
RYSSDYFDELYRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFK
EGKAILRAKIDMASPFPVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDN
RRLYDWVLDNIHIFPRPAQYEFSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASI
REFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDPVEVVIENLSDEYELATIPNHPNTPEFGE
RQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAAGKITTIFCTYDNKTLGKEP
ADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEHSLGDAVANKRF
QFEREGYFCLDSKESTTEKVVFNRTVSLKDAT
>gnl|CDD|129533 TIGR00441, Phosphoheptose_isomerase, phosphoheptose isomerase. This model describes phosphoheptose isomerase. Because a closely related paralo in Escherichia coli differs in function (DnaA initiator-associating protein diaA), this model has been rebuilt with a high stringency, and is likely to miss many true examples for phosphoheptose isomerase. Involved in lipopolysaccharide biosynthesis it may have a role in virulence in Haemophilus ducreyi [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
VVLLADSFKAGGKVLICGNGGSACDAQHFAAELTGRYRENRPGLPAIALSADVSHLTCVSNDYGYEDVFS
RQVEALGQKGDVLLGISTSGNSKNVLKAIEAAKDKGMKTITLAGKDGGKMAGLADIELRVPHFYTPRIQE
IHIKVIHILCQLIE
>gnl|CDD|273080 TIGR00442, hisS, histidyl-tRNA synthetase. This model finds a histidyl-tRNA synthetase in every completed genome. Apparent second copies from Bacillus subtilis, Synechocystis sp., and Aquifex aeolicus are slightly shorter, more closely related to each other than to other hisS proteins, and actually serve as regulatory subunits for an enzyme of histidine biosynthesis. They were excluded from the seed alignment and score much lower than do single copy histidyl-tRNA synthetases of other genomes not included in the seed alignment. These putative second copies of HisS score below the trusted cutoff. The regulatory protein kinase GCN2 of Saccharomyces cerevisiae (YDR283c), and related proteins from other species designated eIF-2 alpha kinase, have a domain closely related to histidyl-tRNA synthetase that may serve to detect and respond to uncharged tRNA(his), an indicator of amino acid starvation; these regulatory proteins are not orthologous and so score below the noise cutoff [Protein synthesis, tRNA aminoacylation]
QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGG
RSLTLRPEGTAPVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEII
ALAADILKELGLKDFTLEINSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQ
ELLKNAPKILDFLCEESRAHFEELKELLDALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGG
RYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGI
RVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQETVPL
>gnl|CDD|273081 TIGR00443, hisZ_biosyn_reg, ATP phosphoribosyltransferase, regulatory subunit. Apparant second copies of histidyl-tRNA synthetase, found in Bacillus subtilis, Synechocystis sp., Aquifex aeolicus, and others, are in fact a regulatory subunit of ATP phosphoribosyltransferase, and usually encoded by a gene adjacent to that encoding the catalytic subunit [Amino acid biosynthesis, Histidine family]
RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMT
APIARLVSTRLRDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKAL
GLKDFKIELGHVGLVRALLEEAGLPEEAREALREALARKDLVALEELVAELGLSPEVRERLLALPRLRGD
GEEVLEEARALAGSETAEAALDELEAVLELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAPLA
GGGRYDELLGRFGRPLPATGFALNLERLLEALT
>gnl|CDD|273082 TIGR00444, Nucleoside_triphosphate_pyrophosphohydrolase, MazG family protein. This family of prokaryotic proteins has no known function. It includes the uncharacterized protein MazG in E. coli [Unknown function, General]
IIAQLRDPENGCPWDKKQTFQSLIPYTLEETYEVLEAIAREDFDDLREELGDLLLQVVFYAQMAQEEGYF
DFDDVCAGISEKLVRRHPHVFADVKAEDESEVLARWEQIKAEEKAQKAQTSALDDVPRTLPALMRAAKIQ
KRCAKVGFDWEDVSPVWDKVYEELDEVMYEARQAVVEQNKLEEEMGDLLFATVNLARHLKTDAEIALQKA
NEKFERRFREVERIVAARGLELTGVDLEEMEELWQQVK
>gnl|CDD|161884 TIGR00445, mraY, phospho-N-acetylmuramoyl-pentapeptide-transferase. Involved in peptidoglycan biosynthesis, the enzyme catalyzes the first of the lipid cycle reactions. Also known as Muramoyl-Pentapeptide Transferase (murX) [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPYVLLVLFVLL
GYGFIGFVDDYRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGPDTFIYIPFIKDFMFDLGLFYILL
AYFVLVGTSNAVNLTDGLDGLAIGPSAIAFGALAILAWATGNANFAKYLHIPYLKDSGELVIFCTALVGA
SLGFLWFNAYPAKVFMGDTGSLALGGALGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIF
KMAPIHHHFELKGWSEPRVVVRFWIISLLLALVALATLKVR
>gnl|CDD|188051 TIGR00446, 25S_rRNA_cytosine2870-C5-methyltransferase, NOL1/NOP2/sun family putative RNA methylase [Protein synthesis, tRNA and rRNA base modification]
IRVNTLKINVEDLLERLENRGVVLEPTCEEYFFEVKESPFSIGSTPEYLFGYYYPQEASSMIPPIALEPR
EDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALISNINRMGVLNTIVINADGRKFGAYLLK
FDAILLDAPCSGEGVIRKDPSRKRNWSEEDIKYCSLLQKELIDAAIDALKPGGVLVYSTCSLEVEENEEV
IDYILRKRPDVVEEIIKGDEFFGINIGKGEVKGALRVFPQNYDCEGFFVAKLRK
>gnl|CDD|213531 TIGR00447, Peptidyl-tRNA_hydrolase, aminoacyl-tRNA hydrolase. The natural substrate for this enzyme may be peptidyl-tRNAs that drop off the ribosome during protein synthesis. Peptidyl-tRNA hydrolase is a bacterial protein; YHR189W from Saccharomyces cerevisiae appears to be orthologous and likely has the same function [Protein synthesis, Other]
IKLIVGLGNPGKKYAGTRHNAGFWVLDLLASRLGLSLRTEKKFFGYTERGLLSGKKVILLKPLTYMNLSG
EAVRALASFYRIKPAELLVVHDELDLPLGKVRLKMGGGAGGHNGLKSIISHLGTNNFNRLRIGIGSPGGS
NKVVEFVLSKFTKSELPLLEKALDKAVEALEMSFSEGAFLKAMNRFNS
>gnl|CDD|129540 TIGR00448, DNA-directed_RNA_polymerase_III_subunit_RPC8, DNA-directed RNA polymerase (rpoE), archaeal and eukaryotic form. This family seems to be confined to the archea and eukaryotic taxa and are quite dissimilar to E.coli rpoE [Transcription, DNA-dependent RNA polymerase]
MYILSKIADTVRIPPDQFGEDLEEVITHQLNEKFEGRLDKNVGLCITIYDIEDIGEGKVIPGDGSAYHNV
TFRALVFKPELGEIVEGEVIEIVEFGAFVSLGPFDGLFHVSQVTDDYCYYDPKESALIGKETKKVLDEGD
KVRARIVALSLKDRRPEGSKIGLTMRQPLLGKLEWIEEE
>gnl|CDD|129541 TIGR00449, Queuine_tRNA-ribosyltransferase, tRNA-guanine family transglycosylase. Different tRNA-guanine transglycosylases catalyze different tRNA base modifications. Two guanine base substitutions by different enzymes described by the model are involved in generating queuosine at position 34 in bacterial tRNAs and archaeosine at position 15 in archaeal tRNAs. This model is designed for fragment searching, so the superfamily is used loosely [Protein synthesis, tRNA and rRNA base modification]
FEIKKTDGHARVGRLKTPHGSVETPVFMPVGTLGTVKGLTPEELKKTGAQIILANTYHLYLRPGQKIVAL
LGGLHKFMQWDGPILTDSGGFQVFSLGDLRKIEEEGVHFKSPIDGSKIFLTPEKIMEIQYALGSDIIMAL
DECTPPPADYDYAEESLERTLRWAEESLEYHKRRNENALFGIVQGGTYPDLRRQSAEGLAELDFDGYAIG
GVSVGEPKRDMLRILEHVAPLLPKDKPRYLMGVGTPELLANAVSLGIDMFDCVAPTRYARNGTLLTTEGR
IKIKNAKYKDDTRPLDEPCDCYVCKNYSRAYLRHLIRCNELLGARLATEHNLHFSFRLIEKIRQAILEDR
LLSFVEEFLEAYGRLLP
>gnl|CDD|273083 TIGR00450, tRNA_modification_GTPase_MnmE, tRNA modification GTPase TrmE. TrmE, also called MnmE and previously designated ThdF (thiophene and furan oxidation protein), is a GTPase involved in tRNA modification to create 5-methylaminomethyl-2-thiouridine in the wobble position of some tRNAs. This protein and GidA form an alpha2/beta2 heterotetramer [Protein synthesis, tRNA and rRNA base modification]
ATPPFNSAIHIIRLSGPDSLSILKKITNKLNTASGMRIQYGHIIDSNNKCKDDELLFKFVAPNSYTGEDV
IEIQCHGSMLIVQEILQLCLKSGARLAQPGEFTQRAFLNGKMDLTQAEAINELILAPNNKVKDIALNKLA
GELDQKIEAIRKSLLQLLAQVEVNIDYEEDDDEQDSLNQLLLSIIAELKDILNSYKLEKLDDGFKLAIVG
SPNVGKSSLLNALLKQDRAIVSDIKGTTRDVVEGDFELNGILIKLLDTAGIREHADFVERLGIEKSFKAI
KQADLVIYVLDASQPLTKDDFLIIDLNKSKKPFILVLNKIDLKINSLEFFVSSKVLNSSNLSAKQLKIKA
LVDLLTQKINAFYSKERVELDDYLISSWQAMILLEKAIAQLQQFLSKLDRQLFLDMLVFHLREAINCLGQ
VTGEVVTEDVLDEIFSNFCLGK
>gnl|CDD|129543 TIGR00451, Uncharacterized_protein_MJ0066, uncharacterized domain 2. This uncharacterized domain is found a number of enzymes and uncharacterized proteins, often at the C-terminus. It is found in some but not all members of a family of related tRNA-guanine transglycosylases (tgt), which exchange a guanine base for some modified base without breaking the phosphodiester backbone of the tRNA. It is also found in rRNA pseudouridine synthase, another enzyme of RNA base modification not otherwise homologous to tgt. It is found, again at the C-terminus, in two putative glutamate 5-kinases. It is also found in a family of small, uncharacterized archaeal proteins consisting mostly of this domain
ILVDGEPLYFIYDDKVIPSLKGALKLMEDKKIVVVDNGAVKFLKNGADVMRPGIVDADEDIKEGDDVVVV
DENKDRPLAVGIALMSGEEMKEMDKGKAVKNIHHIGD
>gnl|CDD|273084 TIGR00452, methyltransferase_putative, tRNA (mo5U34)-methyltransferase. This model describes CmoB, the enzyme tRNA (mo5U34)-methyltransferase involved in tRNA wobble base modification [Unknown function, Enzymes of unknown specificity]
LYQALADTPLAHWLETLPAQLEAWLQPPRHGDLPRWQKALAQLPELPPSQVDLDSDAVTIGSAGDLSEGQ
RAQLENALRALMPWRKGPFELFGIHIDTEWRSDWKWDRLAPHISPLKGRRVLDVGCGNGYHMWRMLGAGA
KLVVGIDPSLLFLMQFLAIKHLLGDAPVHFLPLGIEDLPPNLKAFDTVFSMGVLYHRRSPLDHLLQLKDQ
LRPGGELVLETLVIDGDEGTVLVPEDRYAQMRNVWFLPSVAALKNWLERCGFKDVRCVDVSVTSTEEQRS
TDWMTFESLADFLDPEDPSLTIEGYPAPKRAVLIAR
>gnl|CDD|213532 TIGR00453, ispD, 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase. Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKI
VAGGDTRQDSVRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGF
VVETVDREGLWAAQTPQAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDL
ALAEALL
>gnl|CDD|200016 TIGR00454, Adenosylcobinamide-phosphate_guanylyltransferase, TIGR00454 family protein. At this time this gene appears to be present only in Archea [Hypothetical proteins, Conserved]
DALIMAGGKGTRLGGVEKPLIEVCGRCLIDHVLSPLLKSKVNNIIIATSPHTPKTEEYINSAYKDYKNAS
GKGYIEDLNECIGELYFSEPFLVVSSDLINLRSKIIDSIVDYYYCIKAPALAVVIPKEKYPNPSIDFNGL
VPAGVNIVSSKNGYQEEEIYSVIDELIVNINTKDD
>gnl|CDD|129547 TIGR00455, Probable_adenylyl-sulfate_kinase, adenylyl-sulfate kinase. This protein, adenylylsulfate kinase, is often found as a fusion protein with sulfate adenylyltransferase. Important residue (active site in E.coli) is residue 100 of the seed alignment [Central intermediary metabolism, Sulfur metabolism]
WHPAITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEE
DRKENIRRIGEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKK
ARNGEIKGFTGIDSPYEAPENPEVVLDTDQNDREECVGQIIEKL
>gnl|CDD|273085 TIGR00456, Arginine--tRNA_ligase, arginyl-tRNA synthetase. This model recognizes arginyl-tRNA synthetase in every completed genome to date. An interesting feature of the alignment of all arginyl-tRNA synthetases is a fairly deep split between two families. One family includes archaeal, eukaryotic and organellar, spirochete, E. coli, and Synechocystis sp. The second, sharing a deletion of about 25 residues in the central region relative to the first, includes Bacillus subtilis, Aquifex aeolicus, the Mycoplasmas and Mycobacteria, and the Gram-negative bacterium Helicobacter pylori [Protein synthesis, tRNA aminoacylation]
IKTLLKEEISQALLKAGLSKESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEII
EKVEAAGPFINFFLSPQKLLERLIQKILTQKEKYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDS
LARILEFLGYDVIREYYVNDWGRQFGLLALGVEKFGNEALNIAVKKPDHGLEGFYVEINKRLEENEELEE
EARELFVKLESGDEETIKLWKRLVEYSLEGIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLV
VEDGALWLDLTLFGDKKDRVLQKSDGTYLYLTTDIAYHLDKLERGFDKMIYVWGSDHHLHIAQMFAILEK
LGYKKKELEHLNFGMVPLYSMKTRRGNVISLDNLLDEASKRAGNVITIKNDLEEEKVADAVGIGAVRYFD
LSKNRTTDYVFDWDAMLSFEGNTAPYIQYAHARICSILRKAEIDGEKLIADDFELLEEKEKELLKLLLQF
PEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAENELAAARLALLKATRQTLKNGLDLLGIEPP
ERM
>gnl|CDD|273086 TIGR00457, Asparagine--tRNA_ligase, asparaginyl-tRNA synthetase. In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, asnS, represents asparaginyl-tRNA synthetases from the three domains of life. Some species lack this enzyme and charge tRNA(asn) by misacylation with Asp, followed by transamidation of Asp to Asn [Protein synthesis, tRNA aminoacylation]
SAAIKDLLQQVYKFVGDEVTVSGWVRTKRSSKKIIFLELNDGSSLGPIQAVINGEDNPYLFQLLKSLTTG
SSVSVTGKVVESPGKGQPVELQVKKIEVVGEAEPDDYPLQKKEHSLEFLRDIAHLRLRTNTLGAVMRVRN
ALSQAIHRYFQENGFTWVSPPILTSNDCEGAGELFRVSTGNIDFSQDFFGKEAYLTVSGQLYLETYALAL
SKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFD
KDLIKRLENIINNKFARITYTDAIEILKESDKNFEYEDFWGDDLQTEHERFLAEEYFKPPVFVTNYPKDI
KAFYMKLNDDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNWYLDLRKYGSVPHSG
FGLGFERLLAYITGLENIRDAIPFPRTPGNINF
>gnl|CDD|273087 TIGR00458, Aspartate--tRNAAsp/Asn_ligase, nondiscriminating aspartyl-tRNA synthetase. In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_arch, represents aspartyl-tRNA synthetases from the eukaryotic cytosol and from the Archaea. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn) [Protein synthesis, tRNA aminoacylation]
VYSADIKPEMDGQEVTFMGWVHEIRDLGGLIFVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAV
RGIVKIKEKAPGGFEIIPTKIEVINEAKEPLPLDPTEKVPAELDTRLDYRFLDLRRPTVQAIFRIRSGVL
ESVREFLAEEGFIEVHTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFR
AEEHNTHRHLNEATSIDIEMAFEDHHDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKFVRLTY
DEAIEMANAKGVEIGWGEDLSTEAEKALGEEMDGLYFITDWPTEIRPFYTMPDEDNPEISKSFDLMYRDL
EISSGAQRIHLHDLLVERIKAKGLNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP
RDRKRLTP
>gnl|CDD|211576 TIGR00459, Aspartate--tRNA_ligase, aspartyl-tRNA synthetase, bacterial type. Asparate--tRNA ligases in this family may be discriminating (6.1.1.12) or nondiscriminating (6.1.1.23). In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_bact, represents aspartyl-tRNA synthetases from the Bacteria and from mitochondria. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). This model generates very low scores for the archaeal type of aspS and for asnS; scores between the trusted and noise cutoffs represent fragmentary sequences [Protein synthesis, tRNA aminoacylation]
MRTHYCGQLRTEHLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPDADALKLAKGLRNEDVVQV
KGKVSARPEGNINRNLDTGEIEILAESITLLNKSKTPPLIIEKTDAEEEVRLKYRYLDLRRPEMQQRLKL
RHKVTKAVRNFLDQQGFLEIETPMLTKSTPEGARDYLVPSRVHKGEFYALPQSPQLFKQLLMVSGVDRYY
QIARCFRDEDLRADRQPEFTQIDMEMSFMTQEDVMELIEKLVSHVFLEVKGIDLKKPFPVMTYAEAMERY
GSDKPDLRFPLELIDVTDLFKDSEFKVFSNLINDGGRVKAIRVPGGWAELSRKSIKELRKFAKEYGAKGL
AYLKVNEDGINSPIKKFLDEKKGKILLERTDAQNGDILLFGAGSKKIVLDALGALRLKLGKDLGLVDPDL
FSFLWVVDFPMFEKDKEGRLCAAHHPFTMPKDEDLENLEAAPEEALAEAYDLVLNGVELGGGSIRIHDPE
VQKKVFEILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRDVIAFPKTTAAACLM
TEAPSFIDEKQLEELSIKYVVKK
>gnl|CDD|273088 TIGR00460, Methionyl-tRNA_formyltransferase, methionyl-tRNA formyltransferase. The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met [Protein synthesis, tRNA aminoacylation]
LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAGRGKKLTPPPVKVLAEEKGIPVFQPEKQRQLEE
LPLVRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVP
KMDAGDILKQETFPIEEEDNSGTLSDKLSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQER
IDWNQSAEELLNKIRALNPWPTAWLTFEGKNIKIHKAKVIDLSTYKAKPGEIVYHNKKGILVACGKDGIL
LLLSLQPPGKKVMRAEDFYNGSRHPWYVPGSSA
>gnl|CDD|273089 TIGR00461, gcvP, glycine dehydrogenase (decarboxylating). This apparently ubiquitous enzyme is found in bacterial, mammalian and plant sources. The enzyme catalyzes the reaction: GLYCINE + LIPOYLPROTEIN = S-AMINOMETHYL-DIHYDROLIPOYLPROTEIN + CO2. It is part of the glycine decarboxylase multienzyme complex (GDC) consisting of four proteins P, H, L and T. Active site in E.coli is located as the (K) residues at position 713 of the SEED alignment [Energy metabolism, Amino acids and amines]
RHLGPGETEQRQMLQTLGFDTLNALIDQAVPPAIRFPRPLQLPAPQSEYGALAQLKSIASKNQVFRSYIG
MGYYDTILPPVIQRNILENPGWYTAYTPYQPEISQGRLEALLNFQTVVMDLTGLEIANASLLDEGTAAAE
AMALSYGVSKSKANAFFVAQDCHPQTIEVIKTRANPFGIEVIVGDHHTFSFSTDVFGALLQYPATDGAIY
DYRSLIDKLHSHKALVSVAADPMALTLLTPPGELGADIVVGSTQRFGVPMGYGGPHAAFFATKDEYQRKM
PGRIVGVSKDAHGNTALRLALQTREQHIRRDKATSNICTAQVLLANMASMYGVYHGPTGLKNIALRIHQL
TVILAIGLKRLNYSLNNDYFFDTLRVGVGEQSAPAILKAAEGRGINLRPLVPGEVGISLDETTTVQDVLD
LWQVFAGKDNLPFTPEELWSDVKTSFPADLTRQDEILQDAVFNQYHSETEMLRYLHQLESKDLALNTSMI
PLGSCTMKLNATAEMMPITWPEFGKIHPFAPAGQTEGYQILIAQLEAWLGEITGFDAISLQPNSGAQGEY
AGLQVIRQYHESRGEEHRNICLIPESAHGTNPASAVMAGMQVVPVKCDGEGNIDLEDLTSKAEQYGDRLA
ALMVTYPSTHGVFEATIGTICDIVHRFGGQVYLDGANMNAQVGLTSPGDFGADVCHLNLHKTFCIPHGGG
GPGMGPIGVKSHLQPFLPRHSLNSTAELQGEDQSIGMVSAAPYGSASILPISWMYIAMMGPEGLTKASEV
AILNANYMAKRLEDYYPILFRGNNELVAHECILDLRPLKKQAGIEVEDVAKRLMDYGFHAPTVSFPVLGT
LMVEPTESESLGELDRFCDAMIAIYQEIQAITAGEIDPADNPLKNAPHTAQSLICGEWNHPYSREEAAYP
APWTKQFKFWPTVGRLDDTYGDRNLVCSC
>gnl|CDD|273090 TIGR00462, genX, EF-P lysine aminoacylase GenX. Many Gram-negative bacteria have a protein closely homologous to the C-terminal region of lysyl-tRNA synthetase (LysS). Multiple sequence alignment of these proteins with the homologous regions of collected LysS proteins shows that these proteins form a distinct set rather than just similar truncations of LysS. The protein is termed GenX after its designation in E. coli. Interestingly, genX often is located near a homolog of lysine-2,3-aminomutase. Its function is unknown [Unknown function, General]
FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVF
RNGERGRRHNPEFTMLEWYRPGFDYHDLMDEVEALLQELLGDPFAPAERLSYQEAFLRYAGIDPLTASLA
ELQAAAAAHGIRASEEDDRDDLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPRVAERFELY
IKGLELANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLAL
GADSIDDVLA
>gnl|CDD|273091 TIGR00463, Glutamate--tRNA_ligase, glutamyl-tRNA synthetase, archaeal and eukaryotic family. The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu) [Protein synthesis, tRNA aminoacylation]
MEELILRYALLNAVKYRGKANPKAVMGAVMSNNPELRKKAKEVLEAVEAAVEEVNSLSPEEQKELMKRLG
LDIKKKEKKRKGLRELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRV
DPEAYDMILEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDR
SVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAID
DHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALSTSSARKGILRGEYSGWDDP
RLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPE
PKRVERPLHPDHPEIGERVLILRGEIYVPKDDLEEGVEPVRLMDAVNVIYSKKELRYHSEGLEGARKLGK
SIIHWLPAKDAVKVKVIMPDASIVEGVIEADASELEVGDVVQFERFGFARLDSADKDGMVFVYTHP
>gnl|CDD|273092 TIGR00464, Glutamate--tRNA_ligase, glutamyl-tRNA synthetase, bacterial family. The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences [Protein synthesis, tRNA aminoacylation]
KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEG
PYYQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGI
PPVVRFKIPQEAVVSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISN
TPKQILIYQALGWKIPVFAHLPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQE
FFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKELPDEELFELLDPHLKSLVNTDTLNREQLAELL
LLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHLKKNVKEVLEALKKKLQALEEWTADEVKSAIKQIA
EELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKAQFIAA
>gnl|CDD|273093 TIGR00465, Ketol-acid_reductoisomerase, ketol-acid reductoisomerase. This is the second enzyme in the parallel isoleucine-valine biosynthetic pathway [Amino acid biosynthesis, Pyruvate family]
LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGLRKGGASWKKATEDGFKVGTVEEAIPQADLIMNLLPDE
VQHEVYEAEIQPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVE
QDPTGEAMAIALAYAKAIGGGRAGVLETTFKEETESDLFGEQAVLCGGLTALIKAGFDTLVEAGYQPELA
YFETVHELKLIVDLIYEGGITGMRDRISNTAEYGALTRRRIIKEELKPEMQKILKEIQNGEFAKEWALEN
EAGKPAFNTARKYESEHEIEKVGKELRAMVPAGK
>gnl|CDD|129558 TIGR00466, 3-deoxy-manno-octulosonate_cytidylyltransferase, 3-deoxy-D-manno-octulosonate cytidylyltransferase [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
MVIIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQKFGIEVCMTSKHHN
SGTERLAEVVEKLALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVK
VVLDSQGYALYFSRSLIPFDRDFFAKRQTPVGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLR
VLYYGEKIHVKIAQEVPSVGVDTQEDLE
>gnl|CDD|273094 TIGR00467, Lysine--tRNA_ligase, lysyl-tRNA synthetase, archaeal and spirochete. This model represents the lysyl-tRNA synthetases that are class I amino-acyl tRNA synthetases. It includes archaeal and spirochete examples of the enzyme. All other known examples are class IIc amino-acyl tRNA synthetases and seem to form a separate orthologous set [Protein synthesis, tRNA aminoacylation]
MHWADVIAEKLKKEKPKNLYTVASGITPSGHIHIGNFREVITADAIARALRDSGSEARFIYIADNYDPLR
KVYPFLPEELETYLGMPLTRIPDPEGCKTSYAEHFLIPFLESLPVLGINPEFIRASKQYTSGLYASQIKI
ALDHRKEISEILNEYRTSKLEENWYPISVFCENCGRDTTTVNNYDNEYSIEYSCECGNQESVDIYTGAIK
LPWRVDWPARWKIEKVTFEPAGKDHAAAGGSYDTGVNIAKEIFQYSPPVTVQYEWISLKGKGGKMSSSKG
DVISVKDVLEVYTPEITRFLFARTKPEFHISFDLDVIKLYEDYDKFERFYYGVKDKDEEKKRAFKRIYEL
SQPMPSERIPYQVPFRHLSVISQIFENNDIEKILEILKRVQYTVDDQKDKLINKRLNCARNWIRKYAPED
FKFSLRSKFDNMEILEENSKKAINELAEFLKKNFEVATEIHNLIYKISKENGIEPALAFQAIYKILLGKE
YGPKLGGFIKILGIDRVEKRTSKYV
>gnl|CDD|273095 TIGR00468, Phenylalanine--tRNA_ligase_alpha_subunit, phenylalanyl-tRNA synthetase, alpha subunit. Most phenylalanyl-tRNA synthetases are heterodimeric, with 2 alpha (pheS) and 2 beta (pheT) subunits. This model describes the alpha subunit, which shows some similarity to class II aminoacyl-tRNA ligases. Mitochondrial phenylalanyl-tRNA synthetase is a single polypeptide chain, active as a monomer, and similar to this chain rather than to the beta chain, but excluded from this model. An interesting feature of the alignment of all sequences captured by this model is a deep split between non-spirochete bacterial examples and all other examples; supporting this split is a relative deletion of about 50 residues in the former set between two motifs well conserved throughout the alignment [Protein synthesis, tRNA aminoacylation]
KLKDLLKQLGKLTKEETKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGS
LHPLTRVIDEIRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQL
RTMEEQEKPPIRIFSPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGETEIRFR
PSYFPFTEPSAEIDVYCPEGKGWLEVLGAGMFRPEVLEPMGIDPTYPGFAWGIGIERLAMLKYGITDIRD
LYENDLRFLRQFK
>gnl|CDD|129561 TIGR00469, Phenylalanine--tRNA_ligase_mitochondrial, phenylalanyl-tRNA synthetase, mitochondrial. Unlike all other known phenylalanyl-tRNA synthetases, the mitochondrial form demonstrated from yeast is monomeric. It is similar to but longer than the alpha subunit (PheS) of the alpha 2 beta 2 form found in Bacteria, Archaea, and eukaryotes, and shares the characteristic motifs of class II aminoacyl-tRNA ligases. This model models the experimental example from Saccharomyces cerevisiae (designated MSF1) and its orthologs from other eukaryotic species [Protein synthesis, tRNA aminoacylation]
SPLKPPHLEINGIKYATDGQTTNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKI
FDNFKPVVTTMENFDNLGFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDDSDNIKSGFLISA
DVYRRDEIDKTHYPVFHQADGAAIRKRTKADLFEKEPGYIEKFEEDIRGTEADLNKENVKIILDDDSIPL
KENNPKQEYASDLAVDLCEHELKHSIEGITKDLFGKKISSMIKNKANNTPKELKVRWIDAYFPFTAPSWE
IEIWFKDEWLELCGCGIIRHDILLRAGVHPSETIGWAFGLGLDRIAMLLFDIPDIRLFWSNDEGFLRQFS
EGDLHLIPKFKPISHHPGCFNDLAFWLPEDIEDDAGFHENDFMDIIRNIAGDLVEQIKLVDKFKHPKTGK
KSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVEI
>gnl|CDD|129562 TIGR00470, sepS, O-phosphoserine--tRNA ligase. This family of archaeal proteins resembles known phenylalanyl-tRNA synthetase alpha chains. Recently, it was shown to act in a proposed pathway of tRNA(Cys) indirect aminoacylation, resulting in Cys biosynthesis from O-phosphoserine, in certain archaea. It charges tRNA(Cys) with O-phosphoserine. The pscS gene product converts the phosphoserine to Cys [Amino acid biosynthesis, Serine family, Protein synthesis, tRNA aminoacylation]
MKFDIKKVLELAEKDFETAWRETRALLKDKHIDNKYPRLKFVYGKPHPLMETIERLREAYLRMGFSEMVN
PLIVDEMHIYKQFGPEAMAVLDRCFYLAGLPRPDVGLGNEKIEIIENLGIDIDDEKKERLREVFHLYKKG
AIDGDDLVFEIAKALNVSNEMGLKVLETVFPEFKDLKPESTTLTLRSHMTSGWFITLSSIIDKRKLPLKL
FSIDRCFRREQREDRSHLMTYHSASCVVVDEEVSVDDGKAVAEGLLAQFGFTKFRFRPDEKKSKYYIPET
QTEVYAYHPKLGEWIEVATFGVYSPIALAKYNIDVPVMNLGLGVERLAMILYGYEDVRAMVYPQIYGEYR
LSDRDIAGMIRVDKVPITDEGYNFANEIVDTCIAHADKPSPCSFEVKEGEFNGRRIKVEIFENEENTKLL
GPAVLNEVYVYDGNIYGIPPTFEGVKEQYIKAKEEGVSTGIRYIDGIAYKAAAKIEEALVSNVEEVKVRV
PIVRSLSDINLKIDELALRYIMGKNKVIDVRGPLFLTAKVEIK
>gnl|CDD|273096 TIGR00471, Phenylalanine--tRNA_ligase_beta_subunit, phenylalanyl-tRNA synthetase, beta subunit. Every known example of the phenylalanyl-tRNA synthetase, except the monomeric form of mitochondrial, is an alpha 2 beta 2 heterotetramer. The beta subunits break into two subfamilies that are considerably different in sequence, length, and pattern of gaps. This model represents the subfamily that includes the beta subunit from eukaryotic cytosol, the Archaea, and spirochetes [Protein synthesis, tRNA aminoacylation]
MPTVTVYKDDLEDLLIGTDRDEILEELPMMGDEIEGFDEESPEIKVEFNPNRPDLLSVEGLARSLRGYLG
IEKGLKSYDSKKGDVKLTVDESVLQIRPFITGAVVKGIILNDKVLESLIELQEKLHWNIGRNRRKVAIGI
HDLDKVEFPFHYKAVSPNGIKFVPLNSDQEMTPDEILEEHPKGIRYAHIIEDSDKFPLILDSKDDVLSMP
PIINSELTKLTVNTRNLLIDVTGTDKTAVEITLNIACTMFADRGDGRITVVEVERPDEHLGQPNLAPRFM
EVSVEYINSLLGLNLSADEIAHSLKKMRLDAVQSDEKLKVVIPAYRVDILHEVDIIEDVAIGYGYNNFPP
ELPLINTIGRLKPLNKVSDIIREIMVGLGFQEVIPLTLTSEEVNFKRMRIEDNNDVKVANPKTLEYTIVR
TSLLPGLLETLSENKHHELPQKIFEIGDVVVKDDKSETRSRVVTKLAVGITHSEANFNEIKSIVAALARE
LGIEYEIEESEHPSFIPGRGAKIVFEGKAIGHFGEIHPEVLTNFELEFPVSAFEVNIEVFL
>gnl|CDD|273097 TIGR00472, Phenylalanine--tRNA_ligase_beta_subunit, phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial. Every known example of the phenylalanyl-tRNA synthetase, except the monomeric form of mitochondrial, is an alpha 2 beta 2 heterotetramer. The beta subunits break into two subfamilies that are considerably different in sequence, length, and pattern of gaps. This model represents the subfamily that includes the beta subunit from Bacteria other than spirochetes, as well as a chloroplast-encoded form from Porphyra purpurea. The chloroplast-derived sequence is considerably shorter at the amino end [Protein synthesis, tRNA aminoacylation]
MKISLKWLREYVPLSEIDNEEIAEALTSIGLEVEAVIPFSKPLKGVVVGKVLEVEPHPNADKLKVCKVDI
GEKEMLQIVCGAPNVEAGKKVAVALPGAKLPNGLKIKKSKLRGVESEGMLCSESELGLDEKSDGIIVLDE
DAPLGTDIAEYLGLDDDIIEVSITPNRGDCLSILGIARELAALFDLNLETPVPFEPETTETIDEGFKIEI
EDPEVCPFYLGRVIKGVKVKPSPLWLKERLRRSGIRPINNIVDITNYVMLELGQPLHAFDADKIEGNIVV
RSAKEGESFTTLDGKERELKKGDLVIADDKKPLAIAGVMGGKESGVTDTTTNIFLESAYFNPESIRKTAR
RLGISTDSSYRFERGVDPELTELALDRALNLILEIFGGEVISVVSDNYKEKAKEKKISLRIKKLNKILGI
ELSDEEVRDILKRLGFKVEKQKDGWEVTVPSYRHDIEIEEDLIEEIARIYGYDNIPAEPLSVSSKLNKNN
ENYLLLRKLRTLLVGLGLNEVITYSFVDPEKAEKFNFPKLENLVEIKNPLSNERSVLRTSLLPSLLEVLA
YNQNRKNKDVKIFEIGKVFAKDGEAVKEQLRLAILISGEKNPSSWNHKEEKVDFYDLKGDVESLLELLGL
SDDVYFKNTAENEELHPGQSATIYLKGKKIGFIGELHPEIAKKYDLKEPTFVFELDLDRLLESLKKVPKY
RPISKFPAVTRDISFLVPKDVPANEIIKLIKKSGLELLEEVELFDVYQGKNIGEGKKSLALRLVLRDKER
TLTDEEINKIVEKVLNALKEKLGAELR
>gnl|CDD|273098 TIGR00473, pssA, CDP-diacylglycerol--serine O-phosphatidyltransferase. This enzyme, CDP-diacylglycerol--serine O-phosphatidyltransferase, is involved in phospholipid biosynthesis catalyzing the reaction CDP-diacylglycerol + L-serine = CMP + L-1-phosphatidylserine. Members of this family do not bear any significant sequence similarity to the corresponding E.coli protein [Fatty acid and phospholipid metabolism, Biosynthesis]
TMLNAFSGFLSILSLLRYTIVRACFLILLSMFFDFLDGRVARKTNRVSDFGKELDSLADVVSFGVAPAAL
AYSIGNFQTIGILVAALFFLCGILRLARFNVLNVKLPSFIGLPIPFAALLVVSLVLLYSYLLAAIAACLL
SVLMVSNIRYP
>gnl|CDD|273099 TIGR00474, selA, L-seryl-tRNA(Sec) selenium transferase. In bacteria, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelA. This model excludes homologs that appear to differ in function from Frankia alni, Helicobacter pylori, Methanococcus jannaschii and other archaea, and so on [Protein synthesis, tRNA aminoacylation]
LRALPSVDKLLEDPALAPLLARYGRALVVDAVREVLDELREKILAGEIDPDLSLEELVAEVERRLEARLR
PSLRRVINATGVVLHTNLGRAPLSEEAIEAVTDAARGYSNLEYDLETGKRGSRYSHVEGLLCELTGAEDA
LVVNNNAAAVLLALNTLAKGKEVIVSRGELVEIGGSFRIPDVMEQSGAKLVEVGTTNRTHLKDYEDAITE
NTALLLKVHTSNYRIVGFTEEVSIEELVALGREHGLPVMEDLGSGSLVDLSRYGLPDEPTVQEVIAAGVD
LVTFSGDKLLGGPQAGIIVGKKELIERLKKNPLKRALRVDKLTLAALEATLRLYLDPEKALEKIPTLRML
TQSPEELRARAERLAKRLKAALGPGFELEVVPGKSQVGGGSLPDERLPSYAVALTPDGLSAEKLEARLRE
LPPPIIGRIEDDRFLLDLRTLLEDELELLIEALR
>gnl|CDD|129567 TIGR00475, Selenocysteine-specific_elongation_factor, selenocysteine-specific elongation factor SelB. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes [Protein synthesis, Translation factors]
MIIATAGHVDHGKTTLLKALTGIAADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAG
GGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIKRTEMFMKQILNSYIFLKN
AKIFKTSAKTGQGIGELKKELKNLLESLDIKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLR
LLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDPKLRVVVKFIAEVPLLEL
QPYHIAHGMSVTTGKISLLDKGIALLTLDAPLILAKGDKLVLRDSSGNFLAGARVLEPPVRVKRKAFIAE
LIKAGDSCYCIFLLLERGAVDLGLEWFKQLTGILIMRLLLPPTTIRICGFGENIDFGEVEVKKILVKLGT
EQHDVKGVDKERLERMASLNEELLKTAIEKLIGTYKIGGWLHIPDHKSDFEKEEDIWQKIKGTFGTKGAW
VREFAEEVNGDEKVMLKRVRKAGHRGGETLIVKDRLLKKYINELKEEGGTFNVQQARDKLGLGRKLLIQL
LEYFDRLGFTRREGNDHRLRD
>gnl|CDD|273100 TIGR00476, selenide_water_dikinase, selenium donor protein. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelD, known as selenophosphate synthetase, selenium donor protein, and selenide,water dikinase. SelD provides reduced selenium for the selenium transferase SelA. This protein itself contains selenocysteine in many species; any sequence scoring well but not aligning to the beginning of the model is likely to have a selenocysteine residue incorrectly interpreted as a stop codon upstream of the given sequence. The SelD protein also provides selenophosphate for the enzyme tRNA 2-selenouridine synthase, which catalyzes a tRNA base modification. It also contributes to selenium incorporation by selenium-dependent molybdenum hydroxylases (SDMH), in genomes with the marker TIGR03309. All genomes with SelD should make selenocysteine, selenouridine, SDMH, or some combination
RLTEYSHGGGCGCKIGPGVLDKILASLPAAPDPNLLVGNDTGDDAAVYKLNDGLALVSTTDFFTPIVDDP
YDFGRIAATNALSDIYAMGGTPLTALAILGWPRNKLPPEVLREILAGGADVCAEAGAPLAGGHSIDDPEP
KYGLAVTGLVHPDKLKRNDGAQPGDVLILTKPLGVGVLTAALKKGGLAEEAYAAAIASMTTLNKQAAELA
ALAGVHAMTDVTGFGLLGHLLEMCRGSGVSAEIDFDAVPLLAEQGCVPGGTGRNFASYGEKVPEPAGEQR
DLLCDPQTSGGLLIAVAPEAA
>gnl|CDD|188054 TIGR00477, Tellurite_methyltransferase, tellurite resistance protein TehB. Part of a tellurite-reducing operon tehA and tehB [Cellular processes, Toxin production and resistance]
FYCKKEDYFSKKYNTTATHSDVVEAVKIVSPCKTLDLGCGQGRNSLYLSLLGYDVTAWDHNENSIAFVNE
TKEKENLNLSTALYDINAANIQENYDFIVSTVVFMFLNAERVPSIIANMQEHTNPGGYNLIVAAMDTADY
PCPLPFSFTFKENELREYYKDWEFLKYNENVGELHKTDANGNRIKLKFATMLARK
>gnl|CDD|129570 TIGR00478, Putative_rRNA_methyltransferase_YqxC, TlyA family rRNA methyltransferase/putative hemolysin. Members of this family include TlyA from Mycobacterium tuberculosis, an rRNA methylase whose modifications are necessary to confer sensitivity to ribosome-targeting antibiotics capreomycin and viomycin. Homology supports identification as a methyltransferase. However, a parallel literature persists in calling some members hemolysins. Hemolysins are exotoxins that attack blood cell membranes and cause cell rupture, often by forming a pore in the membrane. A recent study (2013) on SCO1782 from Streptomyces coelicolor shows hemolysin activity as earlier described for a homolog from the spirochete Serpula (Treponema) hyodysenteriae and one from Mycobacterium tuberculosis [Unknown function, General]
RLDILLVRRGLFESREKAKRLILKGFVLVNGKKVDKPSALVDFDAKIELLQNPLFVSRGGEKLKEALEEF
NIDVKNKIVLDVGSSTGGFTDCALQKGAKEVYGVDVGYNQLAEKLRQDERVKVLERTNIRYVTPADIFPD
FATFDVSFISLISILPELDLLLNPNDLTLLFKPQFEAGREKKNKKGVVRDKEAIALALHKVIDKGESPDF
QEKKIIFSLTKGKRGNVE
>gnl|CDD|129571 TIGR00479, 23S_rRNA_uracil1939-C5-methyltransferase_RlmD, 23S rRNA (uracil-5-)-methyltransferase RumA. This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA [Protein synthesis, tRNA and rRNA base modification]
LDHQGEGVARFNGKTVFVPGALPGEKAEVRVTEVKKQYARARVKKILEDSPERTTPPCPHFGQCGGCQLQ
HLSYELQLRSKQQQVIALLERIGKFVSEPIEDVPTIGDDPWGYRNKARLSLGRSPSGQLQAGFYQKGSHD
IVDVKQCPVQAPALNALLPKVRAILENFGASRYLEHKELGQARHGVLRIGRHTGELSSVDRTALERFPHK
EELDLYLQPDSPDVKSICQNINPEKTNVIFGEETEVIAGEMPIYDKSGDLSFTFSARDFIQVNSGQNEKL
VDRALEWLELQGEERVLDAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNAELNGIANVTFYHGTLE
TVLPKQPWAGNGFDKVLLDPPRKGCAAGVLRTIIKLKPERIVYVSCNPATLARDLEALCKAGYTIARVQP
VDMFPHTGHVE
>gnl|CDD|129572 TIGR00481, Uncharacterized_protein_YxkA, Raf kinase inhibitor-like protein, YbhB/YbcL family [Unknown function, General]
HAFEGFGRCDGPNISPPLSWDGVPEGAKSLALTCIDPDAPTGCGWWHWVVVNIPADTTVLPENASSDDKR
LPQGVPLQGRNDFGKSGYIGPCPPKGDHRYLFTVYALDTEKLDLDPGFSLADLGDAMEGHILAEASIEGL
Y
>gnl|CDD|273101 TIGR00482, Probable_nicotinate-nucleotide_adenylyltransferase, nicotinate (nicotinamide) nucleotide adenylyltransferase. This model represents the predominant bacterial/eukaryotic adenylyltransferase for nicotinamide-nucleotide, its deamido form nicotinate nucleotide, or both. The first activity, nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1), synthesizes NAD by the salvage pathway, while the second, nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) synthesizes the immediate precursor of NAD by the de novo pathway. In E. coli, NadD activity is biased toward the de novo pathway while salvage activity is channeled through the multifunctional NadR protein, but this division of labor may be exceptional. The given name of this model, nicotinate (nicotinamide) nucleotide adenylyltransferase, reflects the lack of absolute specificity with respect to substrate amidation state in most species [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASSHHRLAMLKLAIEDNPKFEVDDF
EIKRGGPSYTIDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEK
AILRMHHGNLTLLHNPRVPISSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY
>gnl|CDD|129574 TIGR00483, Elongation_factor_1-alpha, translation elongation factor EF-1 alpha. This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels [Protein synthesis, Translation factors]
MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERG
VTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFEVQPQTREHAFLARTLG
INQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTL
LEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQ
IEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPDNPPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIA
CRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVIEAVKEIPPLGRFAIRDMGQTVAAGMII
DVDPTK
>gnl|CDD|129575 TIGR00484, Elongation_factor_G, translation elongation factor EF-G. After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homolog to canonical (e.g. E. coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis PCC6803 has a few proteins more closely related to EF-G than to any other characterized protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G [Protein synthesis, Translation factors]
MARTTDLNRFRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVHDGAATMDWMEQEKERGITITSAATTV
FWKGHRINIIDTPGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKT
GANFLRVVNQIKQRLGANAVPIQLPIGAEDNFIGVIDLVEMKAYFFNGDKGTKAIEKEIPSDLLEQAKEL
RENLVEAVAEFDEELMEKYLEGEELTIEEIKNAIRKGVLNCEFFPVLCGSAFKNKGVQLLLDAVVDYLPS
PTDVPAIKGIDPDTEKEIERKASDDEPFSALAFKVATDPFVGQLTFVRVYSGVLKSGSYVKNSRKNKKER
VGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCDPKIDVILERMEFPEPVISLAVEPKTKADQE
KMGIALGKLAEEDPTFRTFTDPETGQTIIAGMGELHLDIIVDRMKREFKVEANVGAPQVAYRETIRSKVE
VEGKHAKQSGGRGQYGHVKIRFEPLEPKGYEFVNEIKGGVIPREYIPAVDKGLQEAMESGPLAGYPVVDI
KATLFDGSYHDVDSSEMAFKLAASLAFKEAGKKANPVLLEPIMKVEVEVPEEYMGDVMGDLSSRRGIIEG
MEARGNVQKIKAEVPLSEMFGYATDLRSFTQGRGTYSMEFLHYGEVPSSVANEIIEKRK
>gnl|CDD|129576 TIGR00485, Elongation_factor_Tu, translation elongation factor TU. This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation [Protein synthesis, Translation factors]
MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEY
ETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDM
VDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKP
FLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLR
GIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEM
VMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE
>gnl|CDD|213534 TIGR00486, Putative_GTP_cyclohydrolase_1_type_2, dinuclear metal center protein, YbgI/SA1388 family. The characterization of this family of uncharacterized proteins as orthologous is tentative. Members are found in all three domains of life. Several members (from Bacillus subtilis, Listeria monocytogenes, and Mycobacterium tuberculosis - all classified as Firmicutes within the Eubacteria) share a long insert relative to other members [Unknown function, General]
MNLDELIQLINRFLPKELAEDGDNNGLQVGSGNEEVKKVVVAVDASESVADEAVRLGADLIITHHPLIWK
PLKRLIRGIKPGRLKILLQNDISLYSAHTNLDAHDGGNNDALARALGLENPKEFEDYGLGRVGEFKAPIE
SLEEVLEIKKVLNVKPLLVVKNGPEYVKKVAVVSGSGLSFIMKALREGVDAYITGDLSHHTAHLARELGL
NVIDAGHYATERGGLRKLMEDLNENEGLEVVFSDIPTNA
>gnl|CDD|273102 TIGR00487, Translation_initiation_factor_IF-2, translation initiation factor IF-2. This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU [Protein synthesis, Translation factors]
VKPSVIVIGGTLTVSELANKMNIKVSDIIKKLMLLGVMVTINQVLDKETAELVAEEFGVKVEVRVTLEET
EAEEQDEDSGDLLVERPPVVTIMGHVDHGKTSLLDSIRKTKVAQGEAGGITQHIGAYHVENEDGKMITFL
DTPGHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQE
LSEYGLVPEDWGGDTIFVPVSALTGDGIDELLDMILLQSEVEELKANPNGQASGVVIEAQLDKGRGPVAT
VLVQSGTLRVGDIVVVGAAYGRVRAMIDENGKSVKEAGPSKPVEILGLSDVPAAGDEFIVFKDEKDARLV
AEKRAGKLRQKALSRSVKVTLDNLFEQIKEGELKELNIILKADVQGSLEAIKNSLEKLNNEEVKVKVIHS
GVGGITETDISLASASNAIIIGFNVRPDATAKNVAEAENVDIRYYSVIYKLIDEIRAAMKGMLDPEYEEE
IIGQAEVRQVFNVPKIGNIAGCYVTEGVIKRGNPLRVIRDGVVIFEGEIDSLKRFKDDVKEVSNGYECGI
GIKNYNDIKEGDIIEAFEVQEVKRTLA
>gnl|CDD|273103 TIGR00488, Uncharacterized_protein_MG240, putative HD superfamily hydrolase of NAD metabolism. The function of this protein family is unknown. Members of this family of uncharacterized proteins from the Mycoplasmas are longer at the amino end, fused to a region of nicotinamide nucleotide adenylyltransferase, an NAD salvage biosynthesis enzyme. Members are putative metal-dependent phosphohydrolases for NAD metabolism [Unknown function, Enzymes of unknown specificity]
LKQQLDEHRYQHCLGVGQTAKQLAEANKLDSKKAEIAGAYHDLAKFLPKEQLKQIAKREKMPAHLLYPSP
KLLHAYVGAYILKREFGVQDEDILDAIRNHTSGPPGMSLLDMIIYVADKLEPNRGAGIEIDELRKLAKTD
LKQAYIITLKYTMVLLKK
>gnl|CDD|129580 TIGR00489, Elongation_factor_1-beta, translation elongation factor aEF-1 beta. This model describes the archaeal translation elongation factor aEF-1 beta. The member from Sulfolobus solfataricus was demonstrated experimentally. It is a dimer that catalyzes the exchange of GDP for GTP on aEF-1 alpha [Protein synthesis, Translation factors]
MGTVLAKIKVMPTSPDVDLEKLKEKIKEVLEEGVEIRGLFDEPIAFGLYAIYTMIVMEDREGGTEPIEEA
LAEIEGVESVETVDVSLL
>gnl|CDD|129581 TIGR00490, Elongation_factor_2, translation elongation factor aEF-2. This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD [Protein synthesis, Translation factors]
ARAKMIDKIKELMWKPKFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITI
NAANVSMVHEYEGNEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVK
PVLFINKVDRLINELKLTPQELQERFIKIITEVNKLIKAMAPEEFRDKWKVRVEDGSVAFGSAYYNWAIS
VPSMKKTGIGFKDIYKYCKEDKQKELAKKSPLHQVVLDMVIRHLPSPIEAQKYRIPVIWKGDLNSEVGKA
MLNCDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQQVGVYMGPERVEVDEI
PAGNIVAVIGLKDAVAGETICTTVENITPFESIKHISEPVVTVAIEAKNTKDLPKLIEVLRQVAKEDPTV
HVEINEETGEHLISGMGELHLEIIVEKIREDYGLDVETSPPIVVYRETVTGTSPVVEGKSPNKHNRFYIV
VEPLEESVIQAFKEGKIVDMKMKKKERRRLLIEAGMDSEEAARVEEYYEGNLFINMTRGIQYLDETKELI
LEGFREAMRNGPIAREKCMGVKVKLMDAKLHEDAVHRGPAQVIPAVRSGIFAAMMQAKPVLLEPYQKVFI
NVPQDMMGAATREIQNRRGQILEMKQEGDMVTIIAKAPVAEMFGFAGAIRGATSGRCLWSTEHAGFELVP
QNLQQEFVMEVRKRKGLKLE
>gnl|CDD|273104 TIGR00491, Probable_translation_initiation_factor_IF-2, translation initiation factor aIF-2/yIF-2. This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region [Protein synthesis, Translation factors]
RLRQPIVVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGASEVPTDVIEKICGDLLKSFKIKLKIPG
LLFIDTPGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRIPGWKSH
EGYPFLESINKQEQRVRQNLDKQVYNLVIQLAEQGFNAERFDRIRDFTKTVAIIPVSAKTGEGIPELLAI
LAGLAQNYLENKLKLAIEGPAKGTILEVKEEQGLGYTIDAVIYDGILRKGDIIVLAGIDDVIVTRVRAIL
KPRPLQEMRLARKKFAQVDEVYAAAGVKVAAPNLDTVLAGSPIVVENNEEIEKYKEEIQKEVEEIKIYTD
EEGIVVKADTLGSLEALVNELRRRGIPIKKADIGDVSKRDVVEAEIVKQEAKEYGAIAAFNVKPLPGAEI
EAEKYDIKLFSDNIIYQLMENFEKWIEDIEESEKRKTLEAIIKPGKIKIIPGYVFRRSDPAIVGVEVLGG
IIRPGYPLIKKDGRRVGEVRQIQDNGKNVKRASAGMEVAIAIEDVVIGRQLEEGDELYVDVPERHAKVLE
RDLLDSLDEEEKRAFKEFLEIKRKDNPFWGK
>gnl|CDD|129583 TIGR00492, Alanine_racemase, alanine racemase. This enzyme interconverts L-alanine and D-alanine. Its primary function is to generate D-alanine for cell wall formation. With D-alanine-D-alanine ligase, it makes up the D-alanine branch of the peptidoglycan biosynthetic route. It is a monomer with one pyridoxal phosphate per subunit. In E. coli, the ortholog is duplicated so that a second isozyme, DadX, is present. DadX, a paralog of the biosynthetic Alr, is induced by D- or L-alanine and is involved in catabolism [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRK
AGITAPILLLGGFFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPKRLKVHLKIDTGMNRLGVKPDEA
ALFVQKLRQLKKFLELEGIFSHFATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWP
ESHFDMVRPGIILYGLYPSADMSDGAPFGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVA
IGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDLGPDLQDKTGDEVILWGEEISIDEIAEMLGTI
AYELICTLSKRVPRKYI
>gnl|CDD|188055 TIGR00493, ATP-dependent_Clp_protease_proteolytic_subunit, ATP-dependent Clp endopeptidase, proteolytic subunit ClpP. This model for the proteolytic subunit ClpP has been rebuilt to a higher stringency. In every bacterial genome with the ClpXP machine, a ClpP protein will be found that scores well with this model. In general, this ClpP member will be encoded adjacent to the clpX gene, as were all examples used in the seed alignment. A large fraction of genomes have one or more additional ClpP paralogs, sometimes encoded nearby and sometimes elsewhere. The stringency of the trusted cutoff used here excludes the more divergent ClpP paralogs from being called authentic ClpP by this model [Protein fate, Degradation of proteins, peptides, and glycopeptides]
MNLIPTVIEQTGRGERSFDIYSRLLKERIIFLSGEVNDNVANSIVAQLLFLEAEDPEKDIYLYINSPGGS
ITAGLAIYDTMQFIKPDVSTICIGQAASMGAFLLAAGAKGKRFSLPNSRIMIHQPLGGAQGQATDIEIQA
NEILRLKGLLNDILAEHTGQSLEQIERDTERDFFMSAEEAKEYGLIDKVLTR
>gnl|CDD|129585 TIGR00494, Putative_fluoride_ion_transporter_CrcB, protein CrcB. The role of this protein is uncharacterized, but phenotypes associated with overproduction include resistance to camphor, suppression of a mukB chromosomal partition mutant, and chromosome condensation, together suggesting a function related to chromosome folding [Unknown function, General]
LAIFLGGGPGALLRYLLGIFISAGLFGNSLPLGTLTVNIIGCFGIGFVTLFTQPAVISPDLKLLIGTGFL
GGFTTFSTFSLETTSLLQEGQLGEAVLYILGTLGGGLIGVALGWLLA
>gnl|CDD|273105 TIGR00495, Proliferation-associated_protein_2G4, 42K curved DNA binding protein. Proteins identified by this model have been identified in a number of species as a nuclear (but not nucleolar) protein with a cell cycle dependence. Various names given to members of this family have included cell cycle protein p38-2G4, DNA-binding protein GBP16, and proliferation-associated protein 1. This protein is closely related to methionine aminopeptidase, a cobolt-binding protein [Unknown function, General]
MSGKDEQQEQAYSLSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICEKGDAFIMEETAKIFKKEK
EMEKGIAFPTCISVNNCVGHFSPLKSDQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEEPVTGR
KADVIAAAHLAAEAALRLVKPGNTNTQVTEAINKVAHSYGCTPVEGMLSHQLKQHVIDGEKVIISNPSDS
QKKDHDTAEFEENEVYAVDILVSTGEGKAKDADQRTTIYKRDPSKTYGLKMKASRAFFSEIERRFDAMPF
TLRNFEDEKRARMGLVECVKHELLQPYPVLYEKEGEFVAQFKFTVLLMPNGPMRITSGEFEPDLYKSEME
VQDPEIKALLASPIKRKKQKKKAKKASKTGEAATEGETME
>gnl|CDD|129587 TIGR00496, Ribosome-recycling_factor, ribosome recycling factor. This model finds only eubacterial proteins. Mitochondrial and/or chloroplast forms might be expected but are not currently known. This protein was previously called ribosome releasing factor. By releasing ribosomes from mRNA at the end of protein biosynthesis, it prevents inappropriate translation from 3-prime regions of the mRNA and frees the ribosome for new rounds of translation. EGAD|53116|YHR038W is part of the frr superfamily [Protein synthesis, Translation factors]
KERMDKSIQALKRELSKIRTGRANPSLLDRILVEYYGAPTPLRQLASVTVPDARTLVIQPFDKSNINAIE
KAIQRSDLGLNPNNDGSVIRVNFPPLTEERRKELVKHAKKIAEQAKVAVRNVRRDANDKVKKLEKDKEIS
EDEERRLQEEIQKLTDEYIKKIDEILKDKEKELMEV
>gnl|CDD|211578 TIGR00497, hsdM, type I restriction system adenine methylase (hsdM). Function: methylation of specific adenine residues; required for both restriction and modification activities. The ECOR124/3 I enzyme recognizes 5'GAA(N7)RTCG. for E.coli see (J. Mol. Biol. 257: 960-969 (1996)) [DNA metabolism, Restriction/modification]
QRNELEKKIWEIANKLRGSVDGWDFKQYVLGGLFYRFISENLCKYINDSERRNDPSFSYANLTDDYEAID
ALKDAAIASKGFFIKPSQLFQNVVKSIRENEDLNTTLRDIFDDIEKSELGDGSKESFKGLFKDFNVSEVK
LGSTLTIRTEKLKELLTSIDTMELDEFEKNSIDAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLARI
AIGKKDTVDDVYDMACGSGSLLLQVIKVLGEKTSLVSYYGQEINHTTYNLCRMNMILHNIDYANFNIINA
DTLTTKEWENENGFEVVVSNPPYSISWAGDKKSNLVSDVRFKDAGTLAPNSKADLAFVLHALYVLGQEGT
AAIVCFPGILYREGKEQTIRKYLVDQNFVDAVIQLPSNLFSTTSIATSILVLKKNRKKDPIFFIDGSNEF
VREKKNNRLSPKNIEKIVDCFNSKKEEANFAKSVERDKIRESNYDLTVGKYVNSEAEKEELDIKVLNHSI
DEIVDKQKDLR
>gnl|CDD|273106 TIGR00498, LexA_repressor., SOS regulatory protein LexA. LexA acts as a homodimer to repress a number of genes involved in the response to DNA damage (SOS response), including itself and RecA. RecA, in the presence of single-stranded DNA, acts as a co-protease to activate a latent autolytic protease activity (EC 3.4.21.88) of LexA, where the active site Ser is part of LexA. The autolytic cleavage site is an Ala-Gly bond in LexA (at position 84-85 in E. coli LexA; this sequence is replaced by Gly-Gly in Synechocystis). The cleavage leads to derepression of the SOS regulon and eventually to DNA repair. LexA in Bacillus subtilis is called DinR. LexA is much less broadly distributed than RecA [DNA metabolism, DNA replication, recombination, and repair, Regulatory functions, DNA interactions]
MKPLTARQQEVLDLIRAHIESTGYPPSIREIARAVGLRSPSAAEEHLKALERKGYIERDPGKPRAIRILD
DEPKGVPLIGRVAAGEPILAEQHIEEYFPIDFSLLKKPSAVFLLKVMGDSMVDAGICDGDLLIVRSQKDA
RNGEIVAAMIDGEVTVKRFYKDGTKVELKPENPEFDPIVLNAEDVTILGKVVGVIRNFQ
>gnl|CDD|273107 TIGR00499, Lysine--tRNA_ligase, lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial. This model represents the lysyl-tRNA synthetases that are class II amino-acyl tRNA synthetases. It includes all eukaryotic and most bacterial examples of the enzyme, but not archaeal or spirochete forms [Protein synthesis, tRNA aminoacylation]
ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIRSMGK
ATFITLQDESGQIQLYVNKNKLPEDFYEFDEYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQP
LPDKWHGLTDQETRYRQRYLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKP
FITHHNALDMDLYLRIAPELYLKRLIVGGLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMD
LTENLFKFLAKELLGTFIINYNDLEIDLKPPWKRITMVDALEMVTGIDFDILKDDETAKALAKEHGIEVA
EDSLTLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFTERFELFIAGKEIANAYSELND
PLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSIRDVLLFPQLR
PQK
>gnl|CDD|129591 TIGR00500, Methionine_aminopeptidase, methionine aminopeptidase, type I. Methionine aminopeptidase is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. This model describes type I. The role of this protein in general is to produce the mature form of cytosolic proteins by removing the N-terminal methionine [Protein fate, Protein modification and repair]
ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISV
NEVVIHGIPDKKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGN
RIGEIGAAIQKYAEAKGFSVVREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEI
TTAADGWTVKTKDGSLSAQFEHTIVITDNGPEILTER
>gnl|CDD|129592 TIGR00501, Methionine_aminopeptidase, methionine aminopeptidase, type II. Methionine aminopeptidase (map) is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. The role of this protein in general is to produce the mature amino end of cytosolic proteins by removing the N-terminal methionine. This model describes type II, among which the eukaryotic members typically have an N-terminal extension not present in archaeal members. It can act cotranslationally. The enzyme from rat has been shown to associate with translation initiation factor 2 (IF-2) and may have a role in translational regulation [Protein fate, Protein modification and repair]
DIERAEKWIEAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIRELGAEPAFPCNISINECAAHFTPKAG
DKTVFKDGDVVKLDLGAHVDGYIADTAITVDLGDQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEV
IESYGVKPISNLTGHSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIYAFL
AERPVRLDSARNLLKTIDENYGTLPFARRWLDKLGDEKYLFALNNLIRHGLIYDYPVLNEISGGYVAQWE
HTILVEEHGKEVTTK
>gnl|CDD|129593 TIGR00502, Glucosamine-6-phosphate_deaminase, glucosamine-6-phosphate isomerase. The set of proteins recognized by this model includes a closely related pair from Bacillus subtilis, one of which is uncharacterized but included as a member of the orthologous set [Central intermediary metabolism, Amino sugars]
MRLIILQTYEELSKWAARHIANRINEFKPTAARPFVLGLPTGGTPIGTYKQLIELHQAGKISFQNVTTFN
MDEYAGLSEEHPESYHSFMHNNFFQHIDIKPENINILNGNAPDLEAECRRYEEKIRSYGGIDLFMGGIGP
DGHIAFNEPGSSLTSRTRIKTLTEDTIQANSRFFEGDVNQVPKYALTVGIGTILDSKEVLILVSGHQKAL
ALQKAVEGGVNHMWTISALQLHKHAIVVCDENATQELKVKTVEYFNELE
>gnl|CDD|129594 TIGR00503, Peptide_chain_release_factor_3, peptide chain release factor 3. This translation releasing factor, RF-3 (prfC) was originally described as stop codon-independent, in contrast to peptide chain release factor 1 (RF-1, prfA) and RF-2 (prfB). RF-1 and RF-2 are closely related to each other, while RF-3 is similar to elongation factors EF-Tu and EF-G; RF-1 is active at UAA and UAG and RF-2 is active at UAA and UGA. More recently, RF-3 was shown to be active primarily at UGA stop codons in E. coli. All bacteria and organelles have RF-1. The Mycoplasmas and organelles, which translate UGA as Trp rather than as a stop codon, lack RF-2. RF-3, in contrast, seems to be rare among bacteria and is found so far only in Escherichia coli and some other gamma subdivision Proteobacteria, in Synechocystis PCC6803, and in Staphylococcus aureus [Protein synthesis, Translation factors]
LSDLLKEVDKRRTFAIISHPDAGKTTITEKVLLYGGAIQTAGAVKGRGSQRHAKSDWMEMEKQRGISITT
SVMQFPYRDCLVNLLDTPGHEDFSEDTYRTLTAVDNCLMVIDAAKGVETRTRKLMEVTRLRDTPIFTFMN
KLDRDIRDPLELLDEVENELKINCAPITWPIGCGKLFKGVYHLLKDETYLYQSGTGGTIQAVRQVKGLNN
PALDSAVGSDLAQQLRDELELVEGASNEFDLAAFHGGEMTPVFFGTALGNFGVDHFLDGLLQWAPKPEAR
QSDTRTVEPTEEKFSGFVFKIQANMDPKHRDRVAFMRVVSGKYEKGMKLKHVRTGKDVVISDALTFMAGD
REHVEEAYAGDIIGLHNHGTIQIGDTFTQGEKIKFTGIPNFAPELFRRIRLKDPLKQKQLLKGLVQLSEE
GAVQVFRPLDNNDLIVGAVGVLQFDVVVYRLKEEYNVEARYEPVNVATARWVECADWKKFEEFKRKNETV
LALDGGDNLVYIAKNMVNLELAQERYPDVKFSATREH
>gnl|CDD|129595 TIGR00504, Pyrrolidone-carboxylate_peptidase, pyroglutamyl-peptidase I. Alternate names include pyroglutamate aminopeptidase, pyrrolidone-carboxylate peptidase, and 5-oxoprolyl-peptidase. It removes pyroglutamate (pyrrolidone-carboxylate, a modified glutamine) that can otherwise block hydrolysis of a polypeptide at the amino end, and so can be extremely useful in the biochemical studies of proteins. The biological role in the various species in which it is found is not fully understood. The enzyme appears to be a homodimer. It does not closely resemble any other peptidases [Protein fate, Degradation of proteins, peptides, and glycopeptides]
KVLLTGFEPFGVDPVNPSWEAAEELDGRTIGATVVAEILPNTFFEAIEALQQAIDEIEPDIVIMLGLAPG
RSMITVERVAINVNDARIPDNAGEQPIDEPIVPDGPAAYFATLPVRAMVLAMKKAGIPADVSYTAGTFVC
NHLMYGLLHHLAQKGLPVRAGFIHVPYLPSQVALKHGVPSMSLDTAVAGVTIAIETAIRQSADVKEPGGR
LQ
>gnl|CDD|129596 TIGR00505, GTP_cyclohydrolase-2, GTP cyclohydrolase II. Several members of the family are bifunctional, involving both ribA and ribB function. In these cases, ribA tends to be on the C-terminal end of the protein and ribB tends to be on the N-terminal. The function of archaeal members of the family has not been demonstrated and is assigned tentatively [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]
ERVAEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEA
ALKQIAEEGRGVLIYLRQEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVK
KVRLLTNNPKKIEILKKAGINIVERVPLIVGRNENNEGYLDTKAEKMGHLL
>gnl|CDD|273108 TIGR00506, 34-dihydroxy-2-butanone_4-phosphate_synthase, 3,4-dihydroxy-2-butanone 4-phosphate synthase. Several members of the family are bifunctional, involving both ribA and ribB function. In these cases, ribA tends to be on the C-terminal end of the protein and ribB tends to be on the N-terminal [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]
MFERVEEALEALKKGEIVLVYDDEDRENEGDLIVAAEFITPEQIAFMRRHAGGLICVAITPDIADKLDLP
PMVDINTSASGTASTFTITVAHRKTFTGISANDRALTIRAALADVVKPSDFRRPGHVFPLRAADGGVLTR
GGHTEASVDLAELAGLKPAGVICEMMNDDGTMARKPELMEYAKKHNLKLISIEDLIEYR
>gnl|CDD|161904 TIGR00507, Shikimate_dehydrogenase, shikimate dehydrogenase. This model finds proteins from prokaryotes and functionally equivalent domains from larger, multifunctional proteins of fungi and plants. Below the trusted cutoff of 180, but above the noise cutoff of 20, are the putative shikimate dehydrogenases of Thermotoga maritima and Mycobacterium tuberculosis, and uncharacterized paralogs of shikimate dehydrogenase from E. coli and H. influenzae. The related enzyme quinate 5-dehydrogenase scores below the noise cutoff. A neighbor-joining tree, constructed with quinate 5-dehydrogenases as the outgroup, shows the Clamydial homolog as clustering among the shikimate dehydrogenases, although the sequence is unusual in the degree of sequence divergence and the presence of an additional N-terminal domain [Amino acid biosynthesis, Aromatic amino acid family]
KLYGVIGNPIAHSKSPLIHNAFFKQLGLEGPYIAFLVPPDDLEDALSGFFALGFKGANVTSPFKERAFQF
LDEIDGRAKLAGAVNTLVLEDGKLVGYNTDGIGLVSDLEQLIPLRPNQNVLIIGAGGAAKAVALELLKAD
CNVIIANRTVSKAEELAERFQRYGEIQAFSMDELPLHRVDLIINATSAGMSGNIDEPPVPAEYLKEGKLV
YDLVYNPLETPFLAEAKSLGTKTIDGLGMLVYQAALSFELWTGVEPDIEKMFEQLISVLA
>gnl|CDD|273109 TIGR00508, hypothetical_protein_DESPIG_00326, adenosylmethionine-8-amino-7-oxononanoate transaminase. All members of the seed alignment have been demonstrated experimentally to act as EC 2.6.1.62, an enzyme in the biotin biosynthetic pathway. Alternate names include 7,8-diaminopelargonic acid aminotransferase, DAPA aminotransferase, and adenosylmethionine-8-amino-7-oxononanoate aminotransferase. The gene symbol is bioA in E. coli and BIO3 in S. cerevisiae [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
IWHPYTQMKEALPPLPIERAEGVYLYDEDGRRYIDGISSWWVNIHGHNHPRLNAAIKEQLDKLEHVMFGG
LTHEPAIELAERLVEITPEGLEKVFFSDSGSVAVEVALKMALQYWQNQGRPGRTRFLALRNGYHGDTFGA
MSVGDVGGFHALFEPLLFEQVFIPAPPCYRCYGWDPDDCEAECLAALEALLEEHADEIAAFIVEPLVQGA
GGMRFYPPGYLRKLRELCDEYGVLLIADEIATGFGRTGKLFACEHAGVTPDILCLSKGLTGGYLPLAATL
TTDEIYEAFYSDDAGKAFMHGHTYTGNPLACAAALASLDLLEEEDWLEQVARIEAQLRAGLAPLRDHPGV
ADVRVLGAIGAVELVRDVEPYPSIGAKIYQFFLERGVLLRPLGNVIYLMPPYIITDEELERLTAAIKEAI
D
>gnl|CDD|273110 TIGR00509, Trimethylamine-N-oxide_reductase_1, molybdopterin guanine dinucleotide-containing S/N-oxide reductases. This enzyme family shares sequence similarity and a requirement for a molydenum cofactor as the only prosthetic group. The form of the cofactor is a single molybdenum atom coordinated by two molybdopterin guanine dinucleotide molecules. Members of the family include biotin sulfoxide reductase, dimethylsulfoxide reductase, and trimethylamine-N-oxide reductase, although a single member may show all those activities and related activities; it may not be possible to resolve the primary function for members of this family by sequence comparison alone. A number of similar molybdoproteins in which the N-terminal region contains a CXXXC motif and may bind an iron-sulfur cluster are excluded from this set, including formate dehydrogenases and nitrate reductases. Also excluded is the A chain of a heteromeric, anaerobic DMSO reductase, which also contains the CXXXC motif
ASHWGVFTATVQDGRIVAVTPFESDPNPTPMLEGVPDQVYSESRIKYPMVRKGFLENGVKSDRSGRGREE
FVRVSWDEALDLVAEELKRVRKTHGPSAIFAGSYGWKSAGRLHNASTLLQRMLNLLGGYVGHAGDYSTGA
AQVIMPHVVGDMEVYEQQTTWPVILENSEVLVLWGADPLKTSQIAWGIPDHGGYEYLERLKAKGKRVISI
DPVRTETVEFFGAEWIPPNPQTDVALMLGLAHTLVTEGLYDKDFLAKYTSGFEKFLPYLLGETDGTPKTA
EWASKITGVPAETIKELARLFASKRTMLAAGWSMQRMQHGEQPHWMLVTLAAMLGQIGLPGGGFGFSYHY
SGGGTPSASGPALSQGSNSVSSTAGPEWDDGSASVIPVARISDALLNPGKEIDYNGKELKLPDIKMVYWA
GGNPFHHHQDTNRLIKAWRKLETIIVHEPQWTPTAKHADIVLPATTSFERNDLTMAGDYSNTGILAMKQV
VPPQFEARNDYDIFAALAERLGVEEAFTEGKDEMGWLKHLYEKAAKQAKADGVEMPAFDAFWAEGIVEFP
VPEGADFVRYAAFREDPLLNPLGTPSGLIEIYSKTIAKMGYDDCPGHPTWMEPAEWLGGPRGAKYPLHLI
SPHPKYRLHSQLDHTELRQAYKVQGREPVMIHPDDAAARGIADGDIVRVFNARGQILAGAVVTDGIRKGV
VQIHEGAWYDPADVREPGGLCKYGNPNVLTADIGTSSLAQGNSGNTVLVEIEKYTGPAPPLTAFDQPAAA
>gnl|CDD|273111 TIGR00510, Lipoyl_synthase, lipoate synthase. This enzyme is an iron-sulfur protein. It is localized to mitochondria in yeast and Arabidopsis. It generates lipoic acid, a thiol antioxidant that is linked to a specific Lys as prosthetic group for the pyruvate and alpha-ketoglutarate dehydrogenase complexes and the glycine-cleavage system. The family shows strong sequence conservation [Biosynthesis of cofactors, prosthetic groups, and carriers, Lipoate]
LIPVENPIPNKEILLRKPEWLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECWNHGTATFMILG
DICTRRCPFCDVAHGRNPLPPDPEEPAKLAETIKDMGLKYVVITSVDRDDLEDGGASHLAECIEAIREKL
PNIKIETLVPDFRGNIAALDILLDAPPDVYNHNLETVERLTPFVRPGATYRWSLKLLERAKEYLPNLPTK
SGIMVGLGETNEEIKQTLKDLRDHGVTMVTLGQYLRPSRRHLPVKRYVSPEEFDYYRSVALEMGFLHAAC
GPFVRSSYHADSLFAAGRLVKT
>gnl|CDD|188057 TIGR00511, Ribose_15-bisphosphate_isomerase, ribose-1,5-bisphosphate isomerase, e2b2 family. The delineation of this family was based originally, in part, on a discussion and neighbor-joining phylogenetic study by Kyrpides and Woese of archaeal and other proteins homologous to the alpha, beta, and delta subunits of eukaryotic initiation factor 2B (eIF-2B), a five-subunit molecule that catalyzes GTP recycling for eIF-2. Recently, Sato, et al. assigned the function ribulose-1,5 bisphosphate isomerase [Energy metabolism, Other]
EVLETAEKIRTMEIRGAGRIARAAAAALREQAEKSDAASPEEFRAEMRAAANILISTRPTAVSLPNALRY
VLKYMSGADVETLRQSVIERADEFINRSEKAQERIGEIGAKRIRDGDVIMTHCNSEAALSVIKTAFEQGK
DIEVIVTETRPRNQGHITAKELRDYGIPVTLIVDSAARYYMKEVDHVVVGADAITANGAVINKIGTSQLA
LAAREARVPFMVAAETYKFHPKTITGELVEIEERDPTEVLDEEDLKQLGNVKVRNPAFDVTPPEYVDAII
TERGQIPPEMAYTIIKELFGW
>gnl|CDD|273112 TIGR00512, methylthioribose-1-phosphate_isomerase_predicted, S-methyl-5-thioribose-1-phosphate isomerase. The delineation of this family was based in part on a discussion and neighbor-joining phylogenetic study, by Kyrpides and Woese, of archaeal and other proteins homologous to the alpha, beta, and delta subunits of eukaryotic initiation factor 2B (eIF-2B), a five-subunit molecule that catalyzes GTP recycling for eIF-2. This clade is now recognized to include the methionine salvage pathway enzyme MtnA [Amino acid biosynthesis, Aspartate family]
RAIKWSRGSLEILDQRLLPHESEYIEVTTVEDVADAIRDMRVRGAPAIGIVAAYGLALAAREGETDEGEE
FKAFLEEKLQYLVSSRPTAVNLSWALDRMRAALREAKTVADIKEALLAEAERILEEDLEDNRAIGENGAA
LIKKGVAAKEPVRVLTHCNTGSLATAGYGTALGVIRSAHEKGRLEHVYADETRPYNQGARLTAWELVQEG
IPATLITDSMAAHLMKHGEVDAVIVGADRIAANGDTANKIGTYQLAILAKHHGVPFYVAAPTSTIDLELA
DGAEIPIEERPPEEVTHVGGVRIAPPGIGVWNPAFDVTPAELITGIITEKGVITP
>gnl|CDD|273113 TIGR00513, accA, acetyl-CoA carboxylase, carboxyl transferase, alpha subunit. The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the alpha chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta [Fatty acid and phospholipid metabolism, Biosynthesis]
MMANYLDFEKPIAELEAKIESLRARSRDEDVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRP
YTLDYIELIFDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKA
LRLMKMAERFKMPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGV
GDKVNMLEYSTYSVISPEGCAAILWKDASKAPKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAA
ASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF
>gnl|CDD|129605 TIGR00514, Biotin_carboxylase, acetyl-CoA carboxylase, biotin carboxylase subunit. This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification [Fatty acid and phospholipid metabolism, Biosynthesis]
MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAA
EITGADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVED
EEENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVE
IQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDK
NGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPLSLKQEDVVVRGHAIECRINAEDPIKTFLP
SPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAIARMKRALSEFIIDGIKTTIP
FHQRILEDENFQHGGTNIHYLEKKLGMGE
>gnl|CDD|129606 TIGR00515, beta_chain., acetyl-CoA carboxylase, carboxyl transferase, beta subunit. The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the beta chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta [Fatty acid and phospholipid metabolism, Biosynthesis]
MSWIDRFKSKKKITSTRKAEVPEGVWTKCPKCGQVLYTKELERNLEVCPKCDHHMRMDARERIESLLDEG
SFEEFNSHLEPKDPLKFKDSKKYKDRIAKAQKETGEKDAVVTGKGTLYGMPIVVAVFDFAFMGGSMGSVV
GEKFVRAIEKALEDNCPLIIFSASGGARMQEALLSLMQMAKTSAALAKMSERGLPYISVLTDPTTGGVSA
SFAMLGDLNIAEPKALIGFAGPRVIEQTVREKLPEGFQTSEFLLEHGAIDMIVHRPEMKKTLASLLAKLQ
NLPSP
>gnl|CDD|273114 TIGR00516, Holo-_synthase, holo-[acyl-carrier-protein] synthase. Formerly dpj. This enzyme adds the prosthetic group, phosphopantethiene, to the acyl carrier protein (ACP) apo-enzyme to generate the holo-enzyme. Related phosphopantethiene--protein transferases also exist. There is an orthologous domain in eukaryotic proteins [Fatty acid and phospholipid metabolism, Biosynthesis]
GIGIDITEIARIAKCAGRFKKKFAERFLSPSEIDLCKDKSEKRKNEFIAGFFAAKEACSKAFGTGIGKEL
SFLDIEIRKDPKGAPLITLSKEICDKFNIAALHASISHDAEFAAAQVVIER
>gnl|CDD|213536 TIGR00517, Acyl_carrier_protein, acyl carrier protein. This small protein has phosphopantetheine covalently bound to a Ser residue. It acts as a carrier of the growing fatty acid chain, which is bound to the prosthetic group, during fatty acid biosynthesis. Homologous phosphopantetheine-binding domains are found in longer proteins. Acyl carrier proteins scoring above the noise cutoff but below the trusted cutoff may be specialized versions. These include those involved in mycolic acid biosynthesis in the Mycobacteria, lipid A biosynthesis in Rhizobium, actinorhodin polyketide synthesis in Streptomyces coelicolor, etc. This protein is not found in the Archaea.Gene name acpP.S (Ser) at position 37 in the seed alignment, in the motif DSLD, is the phosphopantetheine attachment site [Fatty acid and phospholipid metabolism, Biosynthesis]
MQEIFEKVKAIIKEQLNVDEDQITTDARFVEDLGADSLDTVELVMALEEEFDIEIPDEEAEKIATVGDAV
NYIEENQ
>gnl|CDD|129609 TIGR00518, Alanine_dehydrogenase, alanine dehydrogenase. The family of known L-alanine dehydrogenases (EC 1.4.1.1) includes representatives from the Proteobacteria, Firmicutes, Cyanobacteria, and Actinobacteria, all with about 50 % identity or better. An outlier to this group in both sequence and gap pattern is the homolog from Helicobacter pylori, an epsilon division Proteobacteria, which must be considered a putative alanine dehydrogenase. In Mycobacterium smegmatis and M. tuberculosis, the enzyme doubles as a glycine dehydrogenase (1.4.1.10), running in the reverse direction (glyoxylate amination to glycine, with conversion of NADH to NAD+). Related proteins include saccharopine dehydrogenase and the N-terminal half of the NAD(P) transhydrogenase alpha subunit. All of these related proteins bind NAD and/or NADP [Energy metabolism, Amino acids and amines]
MRIGVPKEIKNNEFRVALTPAGVAELTSRGHEVLVEAGAGEGSGFTDAAYKAAGAELVATAKQVWDAELV
LKVKEPLPEEYGYLRHGQILFTYLHLAAERALTDALLDSGTTAIAYETVQTADGALPLLAPMSEVAGRLA
AQVGAYHLEKTQGGRGVLLGGVPGVEPGDVTIIGGGVVGTNAAKMANGLGATVTILDINIDRLRQLDAEF
GGRIHTRYSNAYEIEDAVKRADLLIGAVLIPGAKAPKLVSNSLVAQMKPGAVIVDVAIDQGGCVETSRPT
THDQPTYAVHDVVHYCVANMPGAVPKTSTYALTNATMPYVLELANHGWRAACRSNPALAKGLNTHEGALL
SEAVATDLGVPFTEPASVLA
>gnl|CDD|129610 TIGR00519, Glutamyl-tRNAGln_amidotransferase_subunit_D, L-asparaginase, type I. Two related families of asparaginase are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity secreted enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type I of E. coli. Archaeal putative asparaginases are of this type but contain an extra ~ 80 residues in a conserved N-terminal region. These archaeal homologs are included in this model
LKDISIISTGGTIASKVDYRTGAVHPVFTADELLSAVPELLDIANIDGEALMNILSENMKPEYWVEIAEA
VKKEYDDYDGFVITHGTDTMAYTAAALSFMLETPKPVVFTGAQRSSDRPSSDAALNLLCAVRAATEYIAE
VTVCMHGVTLDFNCRLHRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRGEDELEVHDRL
EEKVALIKIYPGISPDIIRNYLSKGYKGIVIEGTGLGHAPQNKLQELQEASDRGVVVVMTTQCLNGRVNM
NVYSTGRRLLQAGVIGGEDMLPEVALVKLMWLLGQYSDPEEAKKMMSKNIAGEIEP
>gnl|CDD|273115 TIGR00520, L-asparaginase_2, L-asparaginase, type II. Two related families of asparaginase (L-asparagine amidohydrolase, EC 3.5.1.1) are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity periplasmic enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type II of E. coli. Both the cytoplasmic and the cell wall asparaginases of Saccharomyces cerevisiae belong to this set. Members of this set from Acinetobacter glutaminasificans and Pseudomonas fluorescens are described as having both glutaminase and asparaginase activitities. All members are homotetrameric [Energy metabolism, Amino acids and amines]
MELFKKSLNAAFVLSGSAAQARSLPNIKILATGGTIAGKGQSSASTAGYKVGELGVEDLIEAVPELKKIA
NIKGEQVVNVGSQDMNEEVLLKLAKGINELLASDDYDGIVITHGTDTLEETAYFLDLTVKSDKPVVIVGA
MRPATSVSADGPMNLYNAVSVAANPKSAGRGVLVVLNDRIASGRYVTKTNTTSLDTFKSRNQGYLGYIHN
GKIDYYYPPVRKHTCDTPFSVSNLDEPLPKVDIIYAYQNAPPLIVNAVLDAGAKGIVLAGVGNGSLSAAG
LKVNETAAKLGVPIVRSSRVGDGMVTPDAEPDGFIASGYLNPQKARVLLQLALTKTYDPEKIQQVFEGY
>gnl|CDD|273116 TIGR00521, coaBC_dfp, phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase. This model represents a bifunctional enzyme that catalyzes the second and third steps (cysteine ligation, EC 6.3.2.5, and decarboxylation, EC 4.1.1.36) in the biosynthesis of coenzyme A (CoA) from pantothenate in bacteria. In early descriptions of this flavoprotein, a ts mutation in one region of the protein appeared to cause a defect in DNA metaobolism rather than an increased need for the pantothenate precursor beta-alanine. This protein was then called dfp, for DNA/pantothenate metabolism flavoprotein. The authors responsible for detecting phosphopantothenate--cysteine ligase activity suggest renaming this bifunctional protein coaBC for its role in CoA biosynthesis. This enzyme contains the FMN cofactor, but no FAD or pyruvoyl group. The amino-terminal region contains the phosphopantothenoylcysteine decarboxylase activity [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
LENKKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHNA
LHIDLAKWADLILIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKD
DGYIFIEPRSGLLACGDEGKGRLAEPETIVKAAEREFSPKEDLEGKRVLITAGPTREPIDPVRFISNLSS
GKMGLALAEAAYKRGADVTLITGPVSLLTPPGVKSIKVSTAEEMLEAALNELAKDFDIFISAAAVADFKP
KTVFEGKIKKQGEELSLKLVKNPDIIAEVRKIKKHQVIVGFKAETNDDLIKYAKEKLKKKNLDMIVANDV
SQGRGFGSDENEVYIFSKHGHKELPLMSKLEVAERILDEIK
>gnl|CDD|273117 TIGR00522, Diphthine_synthase, diphthine synthase. Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent methyltransferase. This protein participates in the modification of a specific His of elongation factor 2 of eukarotes and Archaea to diphthamide. The protein was characterized in Saccharomyces cerevisiae and designated DPH5 [Protein fate, Protein modification and repair]
MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSIEEIEEFFGKRVVVLERSDVEENSFRLI
ERAKSKDVALLVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVCGLTGLQLYKFGKTATIVFFTD
NYRPQTPYNVIKENRKIGLHTLVLLDIHPKENRAMTIGEGLENLLEEEEKRKTGAITPDTYAVVIARAGS
GKPVVKCDKIENLKNYDFGEPLHCLVVLAKTLHFMEFEYLREFADAP
>gnl|CDD|273118 TIGR00523, Translation_initiation_factor_1A, eukaryotic/archaeal initiation factor 1A. Recommended nomenclature: eIF-1A for eukaryotes, aIF-1A for Archaea. Also called eIF-4C [Protein synthesis, Translation factors]
RGKQDSDGPRVRLPYKEEGEIYGVITQMLGAGRVKVRCFDGNKRLARIPGKLRKKIWIREGDVVLVKPWE
FQDDKCDIVWRYTLTEVEWLKRKGYLKE
>gnl|CDD|273119 TIGR00524, Putative_methylthioribose-1-phosphate_isomerase, eIF-2B alpha/beta/delta-related uncharacterized proteins. This model, eIF-2B_rel, describes half of a superfamily, where the other half consists of eukaryotic translation initiation factor 2B (eIF-2B) subunits alpha, beta, and delta. It is unclear whether the eIF-2B_rel set is monophyletic, or whether they are all more closely related to each other than to any eIF-2B subunit because the eIF-2B clade is highly derived. Members of this branch of the family are all uncharacterized with respect to function and are found in the Archaea, Bacteria, and Eukarya, although a number are described as putative translation intiation factor components. Proteins found by eIF-2B_rel include at least three clades, including a set of uncharacterized eukaryotic proteins, a set found in some but not all Archaea, and a set universal so far among the Archaea and closely related to several uncharacterized bacterial proteins [Unknown function, General]
CRTYEDVAEAIKSMVVRGAPAIGVAAAYGLALAALKISHVNVEEFKEDLEKAADFLLSTRPTAVNLFWAL
DRVLNSLKSGESVEEFKESLLREAIEIINEDLETNRKIGENGAKLIKDGDTVLTHCNAGALATSGYGTAL
GVIRSAWEDGKRIRVIADETRPRNQGSRLTAWELVQDGIPVTLITDSAAAYFMQTGEIDAVIVGADRIAR
NGDVANKIGTYQLAVLAKEFRIPFFVAAPLSTFDPKTSTGEDIIIEERDPEEVAQVGGVRIAPLGVKVYN
PAFDITPHDLIDAIITEKGIITP
>gnl|CDD|213537 TIGR00525, Dihydroneopterin_aldolase, dihydroneopterin aldolase. This model describes a bacterial dihydroneopterin aldolase, shown to form homo-octamers in E. coli. The equivalent activity is catalyzed by domains of larger folate biosynthesis proteins in other systems. The closely related parologous enzyme in E. coli, dihydroneopterin triphosphate epimerase, which is also homo-octameric, and dihydroneopterin aldolase domains of larger proteins, score below the trusted cutoff but may score well above the noise cutoff [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
DRVFIEGLEVFAYHGVFDHERVLGQRFVVDLELSVDETKAAESDDLGDTVNYAELYSAIEEIVAEKPRDL
IETVAYRIADRLFADFPQVQRVKVRVSKPNAPIPGHLDDVSVEIRR
>gnl|CDD|273120 TIGR00526, Probable_dihydroneopterin_aldolase_DHNA., FolB domain. Two paralogous genes of E. coli, folB (dihydroneopterin aldolase) and folX (d-erythro-7,8-dihydroneopterin triphosphate epimerase) are homologous to each other and homo-octameric. In Pneumocystis carinii, a multifunctional enzyme of folate synthesis has an N-terminal region active as dihydroneopterin aldolase. This region consists of two tandem sequences each homologous to folB and forms tetramers
MDRVHIKNLEMHTIIGVFEWERLLPQKVVVDLTLGYDASKAANSDDLSDSLNYAEIASNITKFVEENPFK
LIETLAKSVSEVVLDDYQKVTEVELEVSKPKPIPLLADGVSVIIRRER
>gnl|CDD|200024 TIGR00527, Glycine_cleavage_system_H_protein, glycine cleavage system H protein. This model represents the glycine cleavage system H protein, which shuttles the methylamine group of glycine from the P protein to the T protein. The mature protein is about 130 residues long and contains a lipoyl group covalently bound to a conserved Lys residue. The genome of Aquifex aeolicus contains one protein scoring above the trusted cutoff and clustering with other bacterial H proteins, and four more proteins clustering together and scoring below the trusted cutoff; it seems doubtful that all of these homologs are authentic H protein. The Chlamydial homolog of H protein is nearly as divergent as the Aquifex outgroup, is not accompanied by P and T proteins, is not included in the seed alignment, and consequently also scores below the trusted cutoff [Energy metabolism, Amino acids and amines]
QGPQDLRYSSEHEWVRVEGDKTATVGITKFAQDELGDIVFVELPEVGAEVAAGESLGSVESVKAASDIYA
PVDGTVVEVNTALEDSPELVNEDPYGDGWLIKVKLSDGESEVEGLMSAEQYEATLEHD
>gnl|CDD|273121 TIGR00528, Aminomethyltransferase_mitochondrial, glycine cleavage system T protein. The glycine cleavage system T protein (GcvT) is also known as aminomethyltransferase (EC 2.1.2.10). It works with the H protein (GcvH), the P protein (GcvP), and lipoamide dehydrogenase. The reported sequence of the member from Aquifex aeolicus starts about 50 residues downstream of the start of other members of the family (perhaps in error); it scores below the trusted cutoff. Eukaryotic forms are mitochondrial and have an N-terminal transit peptide [Energy metabolism, Amino acids and amines]
LKRTPLYDLHTELGGKMVDFGGWEMPVQYKGQIEEHNAVRTNAGLFDVSHMGQVKLSGPHSLKFLQRLTP
NDVNALTPGKAQYSVLLNPQGGVVDDLIIYKEGEDNRFYLVVNAATAEKDLEWFHEHLQNGSTLDCQSDI
ISLLALQGPKAKTILEPLLDQTVPGLKPFFFGQEAEFALKKAFIARTGYTGEDGFEISIANEKAVEFWEQ
LLAAPGVKPCGLGARDTLRLEAGMCLYGQELDESITPLEAGLGWVISKSRQKYDFIGRAVLMEQKENGTE
KKLVGLEMLEKGIARNGYPIFLPNGETEVGIVTSGTASPTLGKNIGLAYVPKEYHKIGTKLLVQVRNKFY
PIKVVKMPFVRT
>gnl|CDD|273122 TIGR00529, AF0261, integral membrane protein, TIGR00529 family. This protein is predicted to have 10 transmembrane regions. Members of this family are found so far in the Archaea (Archaeoglobus fulgidus and Pyrococcus horikoshii) and in a bacterial thermophile, Thermotoga maritima. In Pyrococcus, the gene is located between nadA and nadB, two components of an enzyme involved in de novo synthesis of NAD. By PSI-BLAST, this family shows similarity (but not necessarily homology) to gluconate permease and other transport proteins [Hypothetical proteins, Conserved]
TLSVLLSLFTVIVVLIVFKKVNIGLLIFVGVMILALLVRLGLEGFLWTLSLADSFWSLIVTIFIIAFLSG
MMEKSFGDLSKFSEGMRTIFSKNSDSFVPALIGLMPMPGGALFSAPMVKNSLKEERINPEKLTVKNYWFR
HTWEFFWPIYPAVVLVSALSGIHPGKVSLTLFPVFAIAFFLGWFFFNGKQLPCLSKPRNLFDSFFNLYPI
IIVLGTSVLILLDKLSGWFALLLSTSIYNVFRRRYLLETLKRVFNKWIFLLLFAVMIYKVVIEHSGVGES
IAAEFVSWNLPPWILLILLPLVSGISTGITQAYVGISLPLLMEFFSSAKYAVLTYMFGYGGVILSPVHLC
VVLSAEYFGVEVFKIYRKVLLPLVLTLILGALVLGVI
>gnl|CDD|129621 TIGR00530, 1-acyl-sn-glycerol-3-phosphate_acyltransferase, 1-acyl-sn-glycerol-3-phosphate acyltransferases. This model describes the core homologous region of a collection of related proteins, several of which are known to act as 1-acyl-sn-glycerol-3-phosphate acyltransferases (EC 2.3.1.51). Proteins scoring above the trusted cutoff are likely to have the same general activity. However, there is variation among characterized members as to whether the acyl group can be donated by acyl carrier protein or coenzyme A, and in the length and saturation of the donated acyl group. 1-acyl-sn-glycerol-3-phosphate acyltransferase is also called 1-AGP acyltransferase, lysophosphatidic acid acyltransferase, and LPA acyltransferase [Fatty acid and phospholipid metabolism, Biosynthesis]
GLKVEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFPPPIVFIAKKELKWIPFFGIMLWLTGAIFIDRE
NIRAIATALKAAIEVLKQGRSIGVFPEGTRSRGRDILPFKKGAFHIAIKAGVPILPVVLS
>gnl|CDD|273123 TIGR00531, BCCP, acetyl-CoA carboxylase, biotin carboxyl carrier protein. This model is designed to identify biotin carboxyl carrier protein as a peptide of acetyl-CoA carboxylase. Scoring below the trusted cutoff is a related protein encoded in a region associated with polyketide synthesis in the prokaryote Saccharopolyspora hirsuta, and a reported chloroplast-encoded biotin carboxyl carrier protein that may be highly derived from the last common ancestral sequence. Scoring below the noise cutoff are biotin carboxyl carrier domains of other enzymes such as pyruvate carboxylase.The gene name is accB or fabE [Fatty acid and phospholipid metabolism, Biosynthesis]
MNIREIKELIKLVEESGITELELKEEEFSVRLSKAAAAASFSVVQQAAAPVPAQVPAQSSAAVPAPAPAA
PAPAADIKGHIVRSPMVGTFYRAPSPDAKPFVEVGDKVNKGQTVCIVEAMKMMNEIEAEKAGTVVAILVE
NGQPVEYGEPLIVIE
>gnl|CDD|129623 TIGR00532, 3-hydroxy-3-methylglutaryl-coenzyme_A_reductase, hydroxymethylglutaryl-CoA reductase, degradative. Most known examples of hydroxymethylglutaryl-CoA reductase are NADP-dependent (EC 1.1.1.34) from eukaryotes and archaea, involved in the biosynthesis of mevalonate from 3-hydroxy-3-methylglutaryl-CoA. This model, in contrast, is built from the two examples in completed genomes of sequences closely related to the degradative, NAD-dependent hydroxymethylglutaryl-CoA reductase of Pseudomonas mevalonii, a bacterium that can use mevalonate as its sole carbon source [Energy metabolism, Other]
HNKEGKIRFAELSKIFGFYHKSVEEKLKEIAEFAELSDEEVKAFFSNGANEDFAFDRMIENVIGTFEFPI
GIAKNFKIDGKDYLIPIAIEEPSVVAAANFAAKIAEEADGFTSDGEGLGIIGQIQQIKIKNEKAAKFEFL
DLGDEIIERAEECDPMLNNLGGGCKDIEARVIDIIEGGILILHIIVDTCDAMGANALNSIAEKVAEFIEL
EFGGECVLKIISNDAAEFTAKARAKADFDHDLIGGEDSWNLAEGIELASAFAAADEERAATHNKGIMNGI
SALCIATFNDFRAIEAGAHKFAAIGGKYFPLSKFEVDRDGALVGEIEIPLAVGTIGGAIKFNEAAIISFK
ILGVNSAEEFAGIAAALGLAQNFAALRALAFEGIQKGHMELHA
>gnl|CDD|129624 TIGR00533, 3-hydroxy-3-methylglutaryl-coenzyme_A_reductase, 3-hydroxy-3-methylglutaryl Coenzyme A reductase, hydroxymethylglutaryl-CoA reductase (NADP). This model represents archaeal examples of the enzyme hydroxymethylglutaryl-CoA reductase (NADP) (EC 1.1.1.34) and the catalytic domain of eukaryotic examples, which also contain a hydrophobic N-terminal domain. This enzyme synthesizes mevalonate, a precursor of isopentenyl pyrophosphate (IPP), a building block for the synthesis of cholesterol, isoprenoids, and other molecules. A related hydroxymethylglutaryl-CoA reductase, typified by an example from Pseudomonas mevalonii, is NAD-dependent and catabolic [Central intermediary metabolism, Other]
MENNEILELVLNGKIKLYQLEKKLGTTRAVEIRRKFIEKLAGLESEHLPNYSIDYERAFGANIENVIGYM
QIPLGVAGPLKIDGEYAKGEYYIPLATTEGALVASVNRGCSAITAGGGATVRVTKDGMTRAPVVRTPSVV
RAGACRIWIDENQNAIKEAAESTTRHGKLQKIQPICLAGDLLYPRFVTTTGDAMGMNMVTIATEYALKQM
VEEYGWEGMEVVAVSGNYCTDKKPAAINLIEGRGKSIVAEATIPGDVVNKVLKTTVSALVEVNIAKNLIG
SAMAGSMGFNAHYANIIGAIFLATGQDEAHIVEGSLGITLAEEVDGDLYFSVSLPDVPVGTVGGGTVLET
QGECLDLLGVRGGNNARQFAEIVGCAVLAGELSLCGALAAGHLVQAHMELGR
>gnl|CDD|213538 TIGR00534, Putative_OxPP_cycle_protein_OpcA, glucose-6-phosphate dehydrogenase assembly protein OpcA. The opcA gene is found immediately downstream of zwf, the glucose-6-phosphate dehydrogenase (G6PDH) gene, in a number of species, including Mycobacterium tuberculosis, Streptomyces coelicolor, Nostoc punctiforme, and Synechococcus sp. PCC 7942. In the latter, disruption of opcA was shown to block assembly of G6PDH into active oligomeric forms [Protein fate, Protein folding and stabilization]
SLQDPTDITLNEINKELNQLWQSIGITGVSRVLTLVIVVYEPEELQESLAAANMASHKHPSRTLVALREE
PALRNPCRILDADLRVGAEVGAGCYVVLRGSGALAEHAGSVVIPLLLPDLPVVVWWPATAPNNPLFDRLG
ALANRRITDSTNFIDPEADLLRRLELYEAGDTDLAWRRLTYWRELLAAAVDQPALEPIDSAVVDYEKGNP
AQALLAGWLASRLGWQYRREVGDYDITKVELITNDETIVAGRPVEGDLITLRLTSKPDACVTLICSETGG
CMRMELRGGAQSEFYQVALLSEQKAEALLSQ
>gnl|CDD|273124 TIGR00535, SAM_DCase, S-adenosylmethionine decarboxylase proenzyme, eukaryotic form. This enzyme is a key regulatory enzyme of the polyamine synthetic pathway. This protein is a pyruvoyl-dependent enzyme. The proenzyme is cleaved at a Ser residue that becomes a pyruvoyl group active site [Central intermediary metabolism, Polyamine biosynthesis]
FEGPEKLLEIWFFEHKKFIDEGKGLRAIGRAQIDEILDLARCTILSSKKNKSLDSYVLSESSLFIYDHKI
IIKTCGTTKLLFALPKILQLAEQLSSWYKVFSVFYSRGCFLFPCAQPAIHRNFSEEVAYLNKFFGNGKAY
VVGDPAKPQKWHLYVAETERETPKIEDPDETLEMLMTGLDKEKASKFFKGPAASTHNLGYQMTKNSGIDK
IIPNSAQICDFDFEPCGYSMNAILGEKAYSTIHVTPEKGFSYASFESNGIDQGKQDYLDLVLRVLNCFQP
SEFSMTVFAKNYQNQSFQKLLSINESLPDYIKLDKQELDLGDYHLFYQKFQKKI
>gnl|CDD|273125 TIGR00536, Release_factor_glutamine_methyltransferase, HemK family putative methylases. The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase (Medline 95189105). Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain [Protein fate, Protein modification and repair]
MTIQEFLRWASSALSRAIARENPWLEALLLLEHDLGRERDLLLAFLTEELTPDEKERIFRLVLRRVKGVP
VAYLLGSKEFYGLEFFVNEHVLIPRPETEELVEKALASLISQPPILHILDLGTGSGCIALALAYEFPNAE
VIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKIDIIVSNPPYIDEEDLADLPNVVRFEPL
LALVGGDDGLNILRQIIELAPDYLKPNGFLVCEIGNWQQKSLKELLRIKFTWYDVENGRDLNGKERVVLG
FYHS
>gnl|CDD|129628 TIGR00537, Putative_protein_methyltransferase_AF_1784, HemK-related putative methylase. The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase (Medline 95189105). Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes [Unknown function, Enzymes of unknown specificity]
VYEPAEDSLLLEANLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNVGLDV
VMTDLFKGVRGKFDVILFNPPYLPLEDDLRRGDWLDVAIDGGKDGRKVIDRFLDELPEILKEGGRVQLIQ
SSLNGEPDTFDKLDERGFRYEIVAERGLFFEELFAIKAW
>gnl|CDD|129629 TIGR00538, Oxygen-independent_coproporphyrinogen-III_oxidase, oxygen-independent coproporphyrinogen III oxidase. This model represents HemN, the oxygen-independent coproporphyrinogen III oxidase that replaces HemF function under anaerobic conditions. Several species, including E. coli, Helicobacter pylori, and Aquifex aeolicus, have both a member of this family and a member of another, closely related family for which there is no evidence of coproporphyrinogen III oxidase activity. Members of this family have a perfectly conserved motif PYRT[SC]YP in a region N-terminal to the region of homology with the related uncharacterized protein [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
IEFDLELIQKYNYPGPRYTSYPTATEFNEEFGEQAFLTAVARHNYPKTPLSLYVHIPFCHKACYFCGCNV
IITRQKHKADPYLDALEKEIALVAPLFDGNRHVSQLHWGGGTPTYLSPEQISRLMKLIRENFPFNADAEI
SIEIDPRYITKDVIDALRDEGFNRLSFGVQDFNKEVQQAVNRIQPEEMIFELMNHAREAGFTSINIDLIY
GLPKQTKESFAKTLEKVAELNPDRLAVFNYAHVPWVKPAQRKIPEAALPSAEEKLDILQETIAFLTEAGY
QFIGMDHFAKPDDELAVAQRKGELHRNFQGYTTQKDTDLLGFGVTSISMLGDCYAQNQKTLKQYYKAVDE
GGNPVERGIALSQDDCIRREVIKSLMCNFKLDYSKIEEKFDLDFADYFAKELELLKPLEEDGLLDVDEKG
IEVTPKGRLLIRNIAMVFDTYLRQKAKEQQFSRTI
>gnl|CDD|129630 TIGR00539, hemN_rel, putative oxygen-independent coproporphyrinogen III oxidase. Experimentally determined examples of oxygen-independent coproporphyrinogen III oxidase, an enzyme that replaces HemF function under anaerobic conditions, belong to a family of proteins described by the model hemN. This model, hemN_rel, models a closely related protein, shorter at the amino end and lacking the region containing the motif PYRT[SC]YP found in members of the hemN family. Several species, including E. coli, Helicobacter pylori, Aquifex aeolicus, and Chlamydia trachomatis, have members of both this family and the E. coli hemN family. The member of this family from Bacillus subtilis was shown to complement an hemF/hemN double mutant of Salmonella typimurium and to prevent accumulation of coproporphyrinogen III under anaerobic conditions, but the exact role of this protein is still uncertain. It is found in a number of species that do not synthesize heme de novo [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
MSLYIHIPFCENKCGYCDFNSYENKSGPKEEYTQALCQDLKHALSQTDQEPLESIFIGGGTPNTLSVEAF
ERLFESIYQHASLSDDCEITTEANPELITAEWCKGLKGAGINRLSLGVQSFRDDKLLFLGRQHSAKNIAP
AIETALKSGIENISLDLMYGLPLQTLNSLKEELKLAKELPINHLSAYALSVEPNTNFEKNAKKLPDDDSC
AHFDEVVREILEGFGFKQYEVSNYAKAGYQVKHNLAYWGAKDYLGCGAGAHGCVANERFFAKKLIKNYIK
DPLQRGVETLNEKNVPKQDKRLEKLFLGLRCVLGVEKSFFDENKGLSQVKFLIEENKAFIKNNRLINSDS
FMADEHALWL
>gnl|CDD|273126 TIGR00540, TPR_hemY_coli, heme biosynthesis-associated TPR protein. Members of this protein family are uncharacterized tetratricopeptide repeat (TPR) proteins invariably found in heme biosynthesis gene clusters. The absence of any invariant residues other than Ala argues against this protein serving as an enzyme per se. The gene symbol hemY assigned in E. coli is unfortunate in that an unrelated protein, protoporphyrinogen oxidase (HemG in E. coli) is designated HemY in Bacillus subtilis [Unknown function, General]
ALAGNTGYVLIVYPPYRIELSLNFFVLLLVLLFVVLYILLRLIRRVFRLPRRVRAWRSRRKQRRAQQATR
EGLIALFEGRYSQAEKKATKAAEHSENPLLAYLLAARAAQQMGDEERRDRYLAEAAELAPNSELAVLLTR
AELLLDQRDYEAALAALDSLQAQAPRHTAVLRLALRAYQRSGNWDALLKLLPALRKAKALSPEEAARLEQ
QAYIGLLDEAREEDADALKTWWKQLPRAERQEPELAVAAAEALIQLGDHDEAEKLIEEALKKEWDPELLR
LYGRLQPGDPSPLIKRAEKWLKKHPDDALLLLALGRLCLRQQLWGKAQSYLEASLSLAPTEEAHLELAQL
FEQLGDTEAAAQHYRKS
>gnl|CDD|129632 TIGR00541, Contains:_Histidine_decarboxylase_alpha_chain, histidine decarboxylase, pyruvoyl type. This enzyme converts histadine to histamine in a single step by catalyzing the release of CO2. This type is synthesized as an inactive single chain precursor, then cleaved into two chains. The Ser at the new N-terminus at the cleavage site is converted to a pyruvoyl group essential for activity. This type of histidine decarboxylase appears is known so far only in some Gram-positive bacteria, where it may play a role in amino acid catabolism. There is also a pyridoxal phosphate type histidine decarboxylase, as found in human, where histamine is a biologically active amine [Energy metabolism, Amino acids and amines]
EKDAKLNALGIDKIAISPYDQWCDGYGEPGAIGNGYVSGLKVDAGTRDKSDDDLLDGIVSYDRAEIKDAY
IGQINMLTASSFCGVAGQVIGHDIARHDSIANDEAKPLFEEKQFDGSELKIYDAKPLLDAGIELFGTEKD
RRFTPAPGAFIICANKGATAERPKEDADLKEGEAYGVWSAIAISFAKDPDHCADLFIEDAGLWEKNDNED
DLKEFLEDHRKAMAKSIAECGQDAHASFERSWIGFAYTIMEPGEIGNAITCAPYVSLAIDAIPGGSILTP
DEDFEILENISLPEWLDDMGFDSLSANNAK
>gnl|CDD|129633 TIGR00542, Probable_L-ribulose-5-phosphate_3-epimerase_UlaE, hexulose-6-phosphate isomerase, putative. This family shows similarity by PSI-BLAST to other isomerases. Putative identification as hexulose-6-phosphate isomerase is reported in Swiss-Prot, attributing a discussion in Genome Sci. Technol. 1:53-75(1996). This family is conserved at better than 40 % identity among the four known examples from three species: Escherichia coli (SgbU and SgaU), Haemophilus influenzae, and Mycoplasma pneumoniae. The rarity of the family, high level of conservation, and proposed catabolic role suggests lateral transfer may be a part of the evolutionary history of this protein [Energy metabolism, Sugars]
KKHPLGIYEKALPKGECWLERLQLAKTCGFDFVEMSVDETDDRLSRLDWSREQRLALVNAIIETGVRIPS
MCLSAHRRFPLGSKDKAVRQQGLEIMEKAIQLARDLGIRTIQLAGYDVYYEEHDEETRRRFREGLKEAVE
LAARAQVTLAVEIMDTPFMSSISKWLKWDHYLNSPWFTLYPDIGNLSAWDNDVQMELQLGIDKIVAIHLK
DTKPGQFKDVPFGEGCVDFERCFKTLKQLNYRGPFLIEMWSEKAEEPVAEIIQARDWIEARMAKAGMVC
>gnl|CDD|273127 TIGR00543, Salicylate_biosynthesis_isochorismate_synthase, isochorismate synthases. This enzyme interconverts chorismate and isochorismate. In E. coli, different loci encode isochorismate synthases for the pathways of menaquinone biosynthesis and enterobactin biosynthesis (via salicilate) and fail to complement each other. Among isochorismate synthases, the N-terminal domain is poorly conserved [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
PRLFGGFPFDPEEPAAWEEFGEGYFVLPEVLVESDGGGTLLTCTIVAEPELNEADLLLYAKFAVSSGIRP
LRALPEQMTTLTTGEDPDKAAWRTAVEEALENIRQGPLDKVVLARALTLKFADDIDPIAVLANLRQQYPN
AYIFLLEPPQGGVFLGATPERLLSREKGELLTEALAGTAPRSADPEEDRKLGELLLKDDKNLREHRLVVE
YIRRRLQPICTSLDVSETPELLKLANVQHLYTPISARLKDGDSLLDLLKQLHPTPAVGGLPREEALDFIR
EHEPFDRGLYAAPLGWLDGEGNGEFAVGIRSALVEDGQVRLYAGAGIVADSDPESEWEETELKLQTMLRA
L
>gnl|CDD|273128 TIGR00544, Prolipoprotein_diacylglyceryl_transferase, prolipoprotein diacylglyceryl transferase. The conversion of lipoprotein precursors into lipoproteins consists of three steps. First, the enzyme described by this model transfers a diacylglyceryl moiety from phosphatidylglycerol to the side chain of a Cys that will become the new N-terminus. Second, the signal peptide is removed by signal peptidase II. Finally, the free amino group of the new N-terminal Cys is acylated by apolipoprotein N-acyltransferase [Protein fate, Protein modification and repair]
MNSSYLIRPPFPIAFQLGPFALHWYGLIYALGIIFAILMAVRRLNRKRGIQKDEFEDLVFWAVLGAVLGA
RIGYVLFYWPYYAQHPLNIFRIWDGGMAIHGGLIGVIIAGIIFSRERNLSFWQLLDLIAPSIPLGQAIGR
WGNFFNQELWGRAVPNDFPWGLLIPLMVWDGMMIDGQYRHPSFLYESFLEGFVVLFILVMLFIKGLRPMG
TIGGVYLIGYGIGRFIIEGFREPSLMLTGVYFIAIVMSIILILLMIAGIVFIMLLAYKLSKFWAEFK
>gnl|CDD|161920 TIGR00545, Probable_lipoate-protein_ligase_A, lipoyltransferase and lipoate-protein ligase. One member of this group of proteins is bovine lipoyltransferase, which transfers the lipoyl group from lipoyl-AMP to the specific Lys of lipoate-dependent enzymes. However, it does not first activate lipoic acid with ATP to create lipoyl-AMP and pyrophosphate. Another member of this group, lipoate-protein ligase A from E. coli, catalyzes both the activation and the transfer of lipoate. Homology between the two is full-length, except for the bovine mitochondrial targeting signal, but is strongest toward the N-terminus [Protein fate, Protein modification and repair]
TRILTSPSNDPYFNLALEEYLFKEFPKTQRGKVLLFWQNANTIVIGRNQNTWAEVNLKELEEDNVNLFRR
FSGGGAVFHDLGNICFSFITPKDGKEFENAKIFTRNVIKALNSLGVEAELSGRNDLVVDGRKISGSAYYI
TKDRGFHHGTLLFDADLSKLAKYLNVDKTKIESKGITSVRSRVVNVKEYLPNITTEQFLEEMTQAFFTYT
ERVETYILDENKTPDVEKRAKERFQSWEWNFGKTPKFNFKNKKRFTAGGFELHVQVEKGKIVDCKFFGDF
LSVADITPVTNRLIGQKYDYDTFAKELENLDVFKEYFGELTPEQ
>gnl|CDD|273129 TIGR00546, Apolipoprotein_N-acyltransferase, apolipoprotein N-acyltransferase. This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property [Protein fate, Protein modification and repair]
FGFGFFLAGLFWLGIALSVNGFIAFVAGLLVVGLPALLALFPGLAAYLLRRLAPFRKVLLALPLLWTLAE
WLRSFGFLGFPWGLIGYAQSSLPLIQIASIFGVWGLSFLVVFLNALLALVLLKKESFKKLLAIAVVVLLA
ALGFLLYELKSATPVPGPTLNVALVQPNIPQDLKFDSEGLEAILEILTSLTKQAVEKPDLVVWPETAFPF
DLENSPQKLADRLKLLVLSKGIPILIGAPDAVPGGPYHYYNSAYLVDPGGEVVQRYDKVKLVPFGEYIPL
GFLFKWLSKLFFLLSQEDFSRGPGPQVLKLPGGKIAPLICYESIFPDLVRASARQGAELLVNLTNDAWFG
DSSGPWQHFALARFRAIENGRPLVRATNTGISAVIDPRGRT
>gnl|CDD|129638 TIGR00547, Outer-membrane_lipoprotein_carrier_protein, periplasmic chaperone LolA. This protein, LolA, is known so far only in the gamma and beta subdivisions of the Proteobacteria. The E. coli major outer lipoprotein (Lpp) of E. coli is released from the inner membrane as a complex with this chaperone in an energy-requiring process, and is then delivered to LolB for insertion into the outer membrane. LolA is involved in the delivery of lipoproteins generally, rather than just Lpp, and is an essential protein in E. coli, unlike Lpp itself [Protein fate, Protein and peptide secretion and trafficking]
MKKIAIKCAALSLLGLANLALADAASDLKMRLAKVDSFHAEFTQKVTDGSGAAVQEGQGDLQIKRPNLFN
MEMKQPDESIIISDGKTLWFYDPFVEQATAQWLKDATGNTPFMLIARNDKSDWHQYNIKQNGDDFVLKPK
ASNGNIKQFDINVDADGIIHNFSATEKDDQRNLYQLKNIQNGALDAAKFQFKPEKGVEVDDQRK
>gnl|CDD|129639 TIGR00548, Outer-membrane_lipoprotein_lolB_precursor., outer membrane lipoprotein LolB. This protein, LolB, is known so far only in the gamma and beta subdivisions of the Proteobacteria. It is a processed, lipid-modified outer membrane protein. It is required in E. coli for insertion of the major outer lipoprotein (Lpp) into the outer membrane. Lpp is transferred to LolB from the carrier protein LolA in the periplasm. Previously, this protein was thought to play in role in 5-aminolevulinic acid synthesis and was designated HemM [Protein fate, Protein and peptide secretion and trafficking]
RFRLFLALSALALLTACAGLTSHEALEGQGDAQTWKQHKQQLSELDAYQIDGKVGYISPRDSGSGRFFWQ
QRNQGYYDLRLSGPLGRGALRLTGREGAVSLEDNGGGRYQAESPESTAGRTLGMRLPLSHLLWWVRGLPA
PDSDYRLTLDADLRLATYEQDGSQWQIEYTRYAEQNGYWMPENLKLHGQDQDVKLVIDDWIP
>gnl|CDD|273130 TIGR00549, Mevalonate_kinase, mevalonate kinase. This model represents mevalonate kinase, the third step in the mevalonate pathway of isopentanyl pyrophosphate (IPP) biosynthesis. IPP is a common intermediate for a number of pathways including cholesterol biosynthesis. This model covers enzymes from eukaryotes, archaea and bacteria. The related enzyme from the same pathway, phosphmevalonate kinase, serves as an outgroup for this clade. Paracoccus exhibits two genes within the phosphomevalonate/mevalonate kinase family, one of which falls between trusted and noise cutoffs of this model. The degree of divergence is high, but if the trees created from this model are correct, the proper names of these genes have been swapped [Central intermediary metabolism, Other]
APGKIILFGEHAVVYGEPAIAAPIPLRTTVTVIESSDGSFIESDLGRGSLDDAPDELDGLKYVLAEFLSR
FSELNPPPLEITIESEIPPGRGLGSSAAVAVALIRALADYFGSELSKEELAELANEAEKIAHGKPSGIDT
ATSTSGGPVYFEKGEGEFTKLISLDGYFVIADTGVSGSTKEAVARVRQLLERFPELIDSIMDAIGELTLE
AKAALQDGDVESLGELMNINQGLLKALGVSHPKLDQLVEIARKAGALGAKLTGAGGGGCMIAL
>gnl|CDD|129641 TIGR00550, Quinolinate_synthase_A, quinolinate synthetase complex, A subunit. This protein, termed NadA, plays a role in the synthesis of pyridine, a precursor to NAD. The quinolinate synthetase complex consists of A protein (this protein) and B protein. B protein converts L-aspartate to iminoaspartate, an unstable reaction product which in the absence of A protein is spontaneously hydrolyzed to form oxaloacetate. The A protein, NadA, converts iminoaspartate to quinolate [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
LSRDNLVEAILRLKKELNAVILAHYYQKDEIQQIADYTGDSLELAQIAAKTDADIIVFCGVHFMGETAKI
LNPEKTVLMPDLGAGCSMADMCPPEEFKKLKERHPDAFVVTYVNTTAEVKALADIVCTSSNAVKVVEHLD
KDNKKILFLPDKNLGRYVQEQTLKDMILWPEQGHCSVHEKFTTEDLERLKEKYPDAEILVHPECEPEVVD
LADFIGSTSQIIRFVLKSPAQKFIIGTEVGLVNRMEAESPDKNTIPLLNEAICPCCAMNRNTLEKLFEAL
EQEKNSNEIKVPEEIAERALLALNRMLRIS
>gnl|CDD|273131 TIGR00551, L-aspartate_oxidase, L-aspartate oxidase. L-aspartate oxidase is the B protein, NadB, of the quinolinate synthetase complex. Quinolinate synthetase makes a precursor of the pyridine nucleotide portion of NAD. This model identifies proteins that cluster as L-aspartate oxidase (a flavoprotein difficult to separate from the set of closely related flavoprotein subunits of succinate dehydrogenase and fumarate reductase) by both UPGMA and neighbor-joining trees. The most distant protein accepted as an L-aspartate oxidase (NadB), that from Pyrococcus horikoshii, not only clusters with other NadB but is just one gene away from NadA [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
MEMDVVVIGSGAAGLSAALALAEKGRVSVITKASVTDSNSYYAQGGIAAALAETDSIDAHVEDTLAAGAG
ICDEEAVWFVVSDGSEAVQFLVSHGVTFDRNEQGGVALTREGGHSYPRIFHAGDATGREIIPTLEKHARS
EPNVNIIEGEFALDLLIETGRCAGVFVQGSGTLETLHADAVVLATGGFGGLYRFTTNPKNSTGDGIALAW
RAGVPVRDLEFVQFHPTALIKPRVRYFLITEAVRGEGAKLVDRDGERFMADRHPRGELAPRDIVARAIDM
EMAEGGGDCVFLDASGIENFKDRFPTIYAVCRGAGIDPEREPIPVAPGAHYTMGGISVDAFGRTTIPGLY
AIGETACTGLHGANRLASNSLLECLVFGLRAARTISREPPYASREYQSGVWDEPRSENPLDRHELQHKMS
SLRSVLWNHAGIVRLEWSLREALRKLVEIQDEVDERMELSNLKLVAKLVTISALKREESRGAHYRLDYP
>gnl|CDD|273132 TIGR00552, Probable_NH3-dependent_NAD+_synthetase, NAD+ synthetase. NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
NLIKYVEEIEDFLRGYVQKSGAKGVVLGLSGGIDSAVVAALCVEALGEQNHALLLPHSVQTPEQDVQDAL
ALAEPLGINYKNIDIAPIAASFQAQTETGDELSDFLAKGNLKARLRMAALYAIANKHNLLVLGTGNKSEL
MLGYFTKYGDGGCDIAPIGDLFKTQVYELAKRLNVPERIIEKPPTADLFDGQTDETELGITYDELDDYLK
GIEELSQTVQEVVKRIESLVQKSEHKRRLPATIFDLFWKQ
>gnl|CDD|273133 TIGR00553, Aminodeoxychorismate_synthase_component_1, aminodeoxychorismate synthase, component I, bacterial clade. Members of this family, aminodeoxychorismate synthase, component I (PabB), were designated para-aminobenzoate synthase component I until it was recognized that PabC, a lyase, completes the pathway of PABA synthesis. This family is closely related to anthranilate synthase component I (trpE), and both act on chorismate. The clade of PabB enzymes represented by this model includes sequences from Gram-positive and alpha and gamma Proteobacteria as well as Chlorobium, Nostoc, Fusobacterium and Arabidopsis. A closely related clade of fungal PabB enzymes is identified by TIGR01823, while another bacterial clade of potential PabB enzymes is more closely related to TrpE (TIGR01824) [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
LVGYLSYEAGPDAAFEPYDAALLADHRRTPLLRFLVFERVEAQPRAAVEAEDDAPADRQAPTSDIQSEMT
RAEYGEAIDQLQDYIRAGDCYQANLTQQFHATWDGDPLAAFRKLRRRQPAPFSAFLDLGDGAILSLSPEL
FFSIDGSEIETRPIKGTLPRGADPQEDRAQASALAESAKDRAENLMIVDLLRNDLGRIAEVGSVKVPELF
VVETYPTVHQLVSTITARLREDLTLSDLFRALFPGGSITGAPKVRAMEIIDELEPQPRGVYCGAIGYLSP
EGDMDFNVAIRTLTLDGGRAVYGVGGGIVADSDPEAEYRECLLKAAPL
>gnl|CDD|273134 TIGR00554, Pantothenate_kinase, pantothenate kinase, bacterial type. Shown to be a homodimer in E. coli. This enzyme catalyzes the rate-limiting step in the biosynthesis of coenzyme A. It is very well conserved from E. coli to B. subtilis, but differs considerably from known eukaryotic forms, described in a separate model [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGS
VAVGKSTSARILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSG
KPNVTAPIYSHLIYDIIPDGDDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLL
KEWYIKRFLKFREGAFNDPDSYFHHYAKLSKEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGAN
HAVEEIKLRK
>gnl|CDD|273135 TIGR00555, Pantothenate_kinase_1, pantothenate kinase, eukaryotic/staphyloccocal type. This model describes a eukaryotic form of pantothenate kinase, characterized from the fungus Aspergillus nidulans and with similar forms known in several other eukaryotes. It also includes forms from several Gram-positive bacteria suggested to have originated from the eukaryotic form by lateral transfer. It differs in a number of biochemical properties (such as inhibition by acetyl-CoA) from most bacterial CoaA and lacks sequence similarity. This enzyme is the key regulatory step in the biosynthesis of coenzyme A (CoA) [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
SRIGIDIGGTLIKVVYEEKKGRRKFKTFETTNIDKFIEWLKNQIHRHSRITTLCATGGGAFKFAELIYES
AGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDFECQKKPIDLDDIYPYLLVNIGTGTSILYVDGDNYE
RVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLVGDIYGGDYSESGLDGSLTASSFGKVL
SKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLLMKVLSYATNFWSKKAL
FLEHEGYSGAIGALLS
>gnl|CDD|273136 TIGR00556, Holo-_synthase, phosphopantetheine--protein transferase domain. This model models a domain active in transferring the phophopantetheine prosthetic group to its attachment site on enzymes and carrier proteins. Many members of this family are small proteins that act on the acyl carrier protein involved in fatty acid biosynthesis. Some members are domains of larger proteins involved specialized pathways for the synthesis of unusual molecules including polyketides, atypical fatty acids, and antibiotics [Protein fate, Protein modification and repair]
DIVGIGIDIVEIKRIAEQIERSGTFAERFFTPSEIEDYCKLSPKSQTESLAGRWAAKEAFIKALGKGISL
GELLFTDIEIVKDLKGAPRVCLIGEAAKDAEKLGVCSVHVSISHDKEYAAAQVILERL
>gnl|CDD|273137 TIGR00557, pdxA, 4-hydroxythreonine-4-phosphate dehydrogenase. This model represents PdxA, an NAD+-dependent 4-hydroxythreonine 4-phosphate dehydrogenase (EC 1.1.1.262) active in pyridoxal phosphate biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
RIAITLGDPAGIGPEIILKALAQLAELCPPVVIGDPALLEARAKLLGLLPLVAIDAPEDAAAAFPGALPV
LPVPLAAPVTPGKPDPANGAAVFETLERAVELCLAGEADALVTAPIHKGAINAAGFPFPGHTEFLAELTG
VPDVVMMLAGPGLRVALATTHIPLKDVPAALTPELLLEKLRILHADLRRDFGIARPRIAVAGLNPHAGEG
GHLGREEIDIIIPALEALRAEGIDLIGPLPADTLFHPAALAKYDAVLAMYHDQGLIPLKYLGFDEGVNVT
LGLPFIRTSPDHGTAFDIAGKGKADPGSLIAAIKLAIELA
>gnl|CDD|273138 TIGR00558, Pyridoxine/pyridoxamine_5'-phosphate_oxidase, pyridoxamine-phosphate oxidase. This model is similar to Pyridox_oxidase from Pfam but is designed to find only true pyridoxamine-phosphate oxidase and to ignore the related protein PhzG involved in phenazine biosynthesis. This protein from E. coli was characterized as a homodimer with two FMN per dimer [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKA
ALLFPWHSLERQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARFPD
GEVPRPEFWGGYRVVPDEIEFWQGRPSRLHDRFRYRRDGDGSWRIERLAP
>gnl|CDD|188064 TIGR00559, Pyridoxine_5'-phosphate_synthase, pyridoxine 5'-phosphate synthase. PdxJ is required in the biosynthesis of pyridoxine (vitamin B6), a precursor to the enzyme cofactor pyridoxal phosphate. ECOCYC describes the predicted reaction equation as 1-amino-propan-2-one-3-phosphate + deoxyxylulose-5-phosphate = pyridoxine-5'-phosphate. The product of that reaction is oxidized by PdxH to pyridoxal 5'-phosphate [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
RLGVNIDHIATLRNARGTAEPDPLQAAFIAEQAGADGITVHLREDRRHIQDRDVRILKETLTTPMNIEMA
PTEEMLAIAVETKPHFVTLVPEKRQEVTTEGGLDVAGLKDKLREACKRLHDAGIEVSLFIDADKDQIKAA
AEVGADFIEIHTGCYANAKNDAEQAEELARIAKASTFAASLGLKVNAGHGLNYHNVKAFAAIPELHELNI
GHAIIARAVMTGLEDAIAEMKRLIKE
>gnl|CDD|273139 TIGR00560, pgsA, CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase. Alternate names: phosphatidylglycerophosphate synthase; glycerophosphate phosphatidyltransferase; PGP synthase. A number of related enzymes are quite similar in both sequence and catalytic activity, including Saccharamyces cerevisiae YDL142c, now known to be a cardiolipin synthase. There may be problems with incorrect transitive annotation of near homologs as authentic CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase [Fatty acid and phospholipid metabolism, Biosynthesis]
KNIPNWLTLFRIIALPIFILFFLENVLPIQVSPFIGALLFIFAAVTDWLDGYLARKWNQVSNFGKFLDPL
ADKVLVLAVLIILVYHGYVPAWFVIVIIAREIVISGLRVLAAEKKVVIAANWLGKWKTTAQMVAIGALLL
WRLTFKIFFEFIVQLLYYIAAFFTLWSFIEYLIKAYNSLKDE
>gnl|CDD|273140 TIGR00561, NADP_transhydrogenase_subunit_alpha, NAD(P) transhydrogenase, alpha subunit. This integral membrane protein is the alpha subunit of alpha 2 beta 2 tetramer that couples the proton transport across the membrane to the reversible transfer of hydride ion equivalents between NAD and NADP. An alternate name is pyridine nucleotide transhydrogenase alpha subunit. The N-terminal region is homologous to alanine dehydrogenase. In some species, such as Rhodospirillum rubrum, the alpha chain is replaced by two shorter chains, both with some homology to the full-length alpha chain modeled here. These score below the trusted cutoff [Energy metabolism, Electron transport]
LIGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAEIWQSDIIFK
VNAPLDDEIALLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRA
IIEAAHEFGRFFTGQITAAGKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEF
LEIDFKEEAGSGDGYAKVMSDAFIKAAMELFAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVI
VDLAAANGGNCEYTQAGEIFTTENGVKVIGYTDFPGRLPTQSSQLYGTNLVNLLKLLCKEKDGNINIDFD
DVVIRGVTVIRAGEETIPAAPIQVSAQPKAAQKAAPEAEKEEKCPCDPRRKYALMAGAGILFGWLASVAP
AAFLGHFTVFALACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGALLQIGQGGGNLFIDALAFIAILI
ASINIFGGFRVTQRMLAMFRKG
>gnl|CDD|213540 TIGR00562, Protoporphyrinogen_oxidase, protoporphyrinogen oxidase. This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
GKKHVVIIGGGISGLCAAYYLEKEIPELPVELTLVEASDRVGGKIQTVKEDGYLIERGPDSFLERKKSAP
DLVKDLGLEHVLVSDATGQRYVLVNRGKLMPVPTKIAPFVKTGLFSLGGKLRAGMDFIRPASPGKDESVE
EFVRRRFGDEVVENLIEPLLSGIYAGDPSKLSLKSTFPKFYQTEQKHGSLILGMKKTRNLPQGSGLQLTA
KKQGQDFQTLATGLETLPEEIEKRLKLTKVYKGTKVTKLSHRGSNYTLELDNGVTVETDSVVVTAPHKAA
AGLLSELSNSASSHLDKIHSPPVANVNLGFPEGSVDGELEGFGFLISRSSKFAILGCIFTSKLFPNRAPP
GKTLLTAYIGGATDESIVDLSENEIINIVLRDLKKVLNINNEPEMLCVTRWHRAIPQYHVGHDQRLKEAR
ELLESAYPGVFLTGNSFEGVGIPDCIDQGKAAASDVLTFLFS
>gnl|CDD|273141 TIGR00563, Ribosomal_RNA_small_subunit_methyltransferase_B, 16S rRNA (cytosine(967)-C(5))-methyltransferase. This protein is also known as sun protein. The reading frame was originally interpreted as two reading frames, fmu and fmv. The recombinant protein from E. coli was shown to methylate only C967 of small subunit (16S) ribosomal RNA and to produce only m5C at that position. The seed alignment is built from bacterial sequences only. Eukaryotic homologs include Nop2, a protein required for processing pre-rRNA, that is likely also a rRNA methyltransferase, although the fine specificity may differ. Cutoff scores are set to avoid treating archaeal and eukaroytic homologs automatically as functionally equivalent, although they may have very similar roles [Protein synthesis, tRNA and rRNA base modification]
RSIAAQALEQLEQGQSLSNLLPPLQQKVSDQDRALLQELCFGVLRTLSQLDWLIKKLMDRPMKGKPRTVH
YLILVGLYQLLYTRIPAHAAVAETVEGAKAIKRKGLKGLVNGVLRRFQREQEELLAEFNALDARYLHPEW
LVKRLQKAYPGQWQSICEANNQRPPMWLRINRTKHSRDEWLALLAEAGMKGFPHDLAPDAVRLETPAAVH
ALPGFEEGWVTVQDASAQWVATWLAPQNEETILDACAAPGGKTTHILELAPQAQVVALDIHEHRLKRVYE
NLKRLGLTIKAETKDGDGRGPSQWAENEQFDRILLDAPCSATGVIRRHPDIKWLRKPRDIAELAELQSEI
LDAIWPLLKTGGTLVYATCSVLPEENSEQIKAFLQEHPDFPFEKTGTPEQVRDGGLQILPHAEEGDGFFY
AKLIKK
>gnl|CDD|273142 TIGR00564, Anthranilate_synthase_component_1, anthranilate synthase component I, non-proteobacterial lineages. This enzyme resembles some other chorismate-binding enzymes, including para-aminobenzoate synthase (pabB) and isochorismate synthase. There is a fairly deep split between two sets, seen in the pattern of gaps as well as in amino acid sequence differences. Archaeal enzymes have been excluded from this model (and are now found in TIGR01820) as have a clade of enzymes which constitute a TrpE paralog which may have PabB activity (TIGR01824). This allows the B. subtilus paralog which has been shown to have PabB activity to score below trusted to this model. This model contains sequences from gram-positive bacteria, certain proteobacteria, cyanobacteria, plants, fungi and assorted other bacteria.A second family of TrpE enzymes is modelled by TIGR00565. The breaking of the TrpE family into these diverse models allows for the separation of the models for the related enzyme, PabB [Amino acid biosynthesis, Aromatic amino acid family]
ADTLTPISAYLKLAQPGSFLLESAEPGSERGRYSFIGLNPVLTIKTEGGTEYLGADDRRSGIVGNPLDEI
RDVMETFAQHSDPELPIPFTGGAVGYLGYDTVRLFEKITLPPPDPLNLPDAYLMLCDDFIIFDHVTDKLY
LIHNNRTTASRSAKAAADARLEALVADLQDPLLPEVPVPYPAALSFTSNYEKEEYEANVAKAKEYIKAGD
IFQVVLSQRFEAKTEAPPFELYRVLRIVNPSPYMYYLDFGDFQIVGSSPELLVKVTGGRITTRPIAGTRK
RGATPEEDEALAEELLADEKERAEHLMLVDLGRNDIGRVCEPGSVEVPEFMKIERYSHVMHIVSTVEGRL
KDGLTAIDALRATFPAGTVSGAPKIRAMELIDELEPEKRGIYGGAVGYLSFDGDMDTAIAIRTMVVKDGK
AYVQAGGGIVADSDPEAEYEETLNKARALLRAIE
>gnl|CDD|273143 TIGR00565, Anthranilate_synthase_component_1, anthranilate synthase component I, proteobacterial subset. This enzyme resembles some other chorismate-binding enzymes, including para-aminobenzoate synthase (pabB) and isochorismate synthase. There is a fairly deep split between two sets, seen in the pattern of gaps as well as in amino acid sequence differences. This group includes proteobacteria such as E. coli and Helicobacter pylori but also the gram-positive organism Corynebacterium glutamicum. The second group includes eukaryotes, archaea, and most other bacterial lineages; sequences from the second group may resemble pabB more closely than other trpE from this group [Amino acid biosynthesis, Aromatic amino acid family]
YIPYPTALFEKLCQSNPHTLLLESAEIESKAHLKSLLLVKAALKITCLGNIVTITALTPNGGAFLQKLSA
FLKAPVSAVIQDNALILTFTPNKKTLDEDLKLFSPSPFDALRLFKSLKTKPKHPFTLFSGGLFSYDLVAF
FEDLPHLKAKNNNCPDFIFYLAENLIIIDHQEKSVEILGACFAERFETQIAQALQDLKELQKSIKSDFVP
KKSKQSREVSANCSDSEFEGRVLSLQEEIKKGEIFQAVPSRRFSLECPEGLAAYYHLKLTNPSPYMFYMK
DSDFILFGASPESALKYNALTRQAEIYPIAGTRPRGKDAQGNIDYDLDSRMELELRHDHKERAEHLMLVD
LARNDMARVCKSGKRYVAKLLKVDRYSNVMHLVSRVVGELRKGLDALHAYRACMNMGTLSGAPKISAMQL
IYQLENQRRGSYGGAVGYLTSEGSMDTCIVIRSAFVKNGRAVVQAGAGIVLDSVPQNEADETRAKAQAVL
DAIRKTSL
>gnl|CDD|273144 TIGR00566, Aminodeoxychorismate_synthase_component_2, glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase. This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase
MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFA
GKLPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTC
FPVTAWEEENIEIMAIRHRDLPLEGVQFHPESILSEQGHQLLANFLHR
>gnl|CDD|273145 TIGR00567, Putative_3-methyladenine_DNA_glycosylase, DNA-3-methyladenine glycosylase. This families are based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). All proteins in this family for which the function is known are involved in the base excision repair of alkylation damage to DNA. The exact specificty of the type of alkylation damage repaired by each of these varies somewhat between species. Substrates include 3-methyl adenine, 7-methyl-guanaine, and 3-methyl-guanine [DNA metabolism, DNA replication, recombination, and repair]
MPPEFFQIDAVTLAPRLLGALLVRRLDDGTGVRGRIVETEAYMGPPDSAAHSYGGRQTPRTDVMFGPPGR
LYVYLIYGIHYMLNVVAAPEGVPAAVLIRAAEPESGAELMTERRGRSVRARELTNGPGKLCQALGITMAD
NGRDLIDPSSLVLLRGNDTHRARSGPRIGIDYAGERTQKPWRFWVTGNPWVS
>gnl|CDD|129659 TIGR00568, Alpha-ketoglutarate-dependent_dioxygenase_AlkB, DNA alkylation damage repair protein AlkB. Proteins in this family have an as of yet undetermined function in the repair of alkylation damage to DNA. Alignment and family designation based on phylogenomic analysis of Jonathan A. Eisen (PhD Thesis, Stanford University, 1999) [DNA metabolism, DNA replication, recombination, and repair]
LKRYFAFNAQEQLIRDINDVASQDPFRQYVTPGGYTMSVAMTNLGKLGWTTHGQGYLYSPKDPQTNKPWP
AMPQDLGDLCERVATAAGFPDFQPDACLVNRYAPGATLSLHQDRDEPDLRAPLLSVSLGLPAIFLIGGLK
RNDPPKRLRLHSGDVVIMGGESRLAFHGV
>gnl|CDD|129660 TIGR00569, Cyclin_CCL1, cyclin ccl1. All proteins in this family for which functions are known are cyclins that are components of TFIIH, a complex that is involved in nucleotide excision repair and transcription initiation. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, StanfordUniversity) [DNA metabolism, DNA replication, recombination, and repair]
YRNSSQKRHWTFTSEEQLQEKRADANAKFREAHEEEEKVLEAKPIFLTPEEELDLVKYYEKRLLDFCSAF
KPTMPTSVVGTAIMYFKRFYLNNSVMEYHPKIIMLTCVFLACKVEEFNVSIDQFVGNLKETPLKALEQVL
EYELLLIQQLNFHLIVHNPYRPLEGFLIDIKTRLPGLENPEYLRKHADKFLNRTLLTDAYLLYTPSQIAL
AAILHTASRAGLNMESYLTEQLSVPGNREELPQLIDIMRELRILVKKYEEPRSEKVAALKKKLDECHSIE
ENLSSVKIRKRKGYEDDTYISKKAK
>gnl|CDD|129661 TIGR00570, CDK-activating_kinase_assembly_factor_MAT1, CDK-activating kinase assembly factor MAT1. All proteins in this family for which functions are known are cyclin dependent protein kinases that are components of TFIIH, a complex that is involved in nucleotide excision repair and transcription initiation. Also known as MAT1 (menage a trois 1). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MDDQGCPRCKTTKYRNPSLKLMVNVCGHTLCESCVDLLFVRGSGSCPECDTPLRKNNFRVQLFEDPTVEK
EVDIRKRVLKIYNKREEDFPSLREYNDYLEEVEDIVYNLTNNIDLENTKKKIETYQKENKDVIQKNKEKS
TREQEELEEALEFEKEEEEQRRLLLQKEEEEQQMNKRKNKQALLDELETSTLPAAELIAQHKKNSVKLEM
QVEKPKPEKPNTFSTGIKMGYQISLVPVQKSEEALYPYQPLNIETEGPPVPTLEELVRQGYLNHVRAASP
QDIAGGYTSNLACERALQEAFSGLFWQPS
>gnl|CDD|273146 TIGR00571, DNA_adenine_methylase, DNA adenine methylase (dam). All proteins in this family for which functions are known are DNA-adenine methyltransferases. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). The DNA adenine methylase (dam) of E. coli and related species is instrumental in distinguishing the newly synthesized strand during DNA replication for methylation-directed mismatch repair. This family includes several phage methylases and a number of different restriction enzyme chromosomal site-specific modification systems [DNA metabolism, DNA replication, recombination, and repair]
MKPFLKWAGGKTSLLPEIKKHLPKKFNCLVEPFVGGGAVFFNLNPKRYLLNDINEDLINLYKAIKNNVDE
LILDVKKLYAEGNSTKEYYYEVREDFNKSTEPFERALLFLYLNRSCFNGLYRYNKKGEFNVPFGRYKTPN
FFDEKNLRHFSEKLQNTTFLCGSFEKILEMVDRDSFVYLDPPYLPLSATANFTGYHKNGFDEDEQKRLAN
FCKSLDERGIKFLLSNSDSSFIRELYRGFNIKRVKAKRSINSNASKRKKVDELLILN
>gnl|CDD|129663 TIGR00573, DNA_polymerase_III_subunit_epsilon, exonuclease, DNA polymerase III, epsilon subunit family. All proteins in this family for which functions are known are components of the DNA polymerase III complex (epsilon subunit). There is, however, an outgroup that includes paralogs in some gamma-proteobacteria and the n-terminal region of DinG from some low GC gram positive bacteria. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, Degradation of DNA]
ERQLVLDTETTGDNETTGLYAGHDIIEIGAVEIINRRITGNKFHTYIKPDRPIDPDAIKIHGITDDMLKD
KPDFKEIAEDFADYIRGAELVIHNASFDVGFLNYEFSKLYKVEPKTNDVIDTTDTLQYARPEFPGKRNTL
DALCKRYEITNSHRALHGALADAFILAKLYLVMTGKQTKYGENEGQQSRPYHAIKSIVKKDMLLKLIKAV
STELQAH
>gnl|CDD|273147 TIGR00574, DNA_ligase, DNA ligase I, ATP-dependent (dnl1). All proteins in this family with known functions are ATP-dependent DNA ligases. Functions include DNA repair, DNA replication, and DNA recombination (or any process requiring ligation of two single-stranded DNA sections). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
EYGIGEKLLIKAISEILGIPKDEIEEKVLEDGDLGEGIEGLFSKQKQTSFFPAPLTVKEVYEVLKFIARL
SGEGSQDKKIKSLKSLLKRASPLEAKYLIRLILGDLRIGIAEKTILDALAKAFLLSPPDVERAFNLTNDL
GKVAKILLEPGLRGLDKDLSIQLGIPFKPMLAERAKSIEEALKKKGNGFYVEYKYDGERVQVHKDGDKFK
IFSRRLENYTYQYPEIFTEFIKEAFPGIKSCILDGEMVAIDPETGKPLPFGTLLRRKRKYDIKAMDQKVP
VCLFVFDILYLNGKSLIDEPLIERREILESILKPIPNRIEIAEMKIVSNVEELEKFLNEAISEGCEGLML
KDLKSIYEPGKRGWLWLKIKPEYLEGMGDTLDLVVIGAYYGKGSRGGMYGSFLCACYDPESEEFKTITKV
GTGFTDADLQELGKKLPPLWIDPPGSRVPSILPDEPDIWPDPAIVWEVTGAEITKSPAYKANGISLRFPR
FSRIRDDKGPEDATTLEQIKELYE
>gnl|CDD|273148 TIGR00575, DNA_ligase, DNA ligase, NAD-dependent. All proteins in this family with known functions are NAD-dependent DNA ligases. Functions of these proteins include DNA repair, DNA replication, and DNA recombination. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). The member of this family from Treponema pallidum differs in having three rather than just one copy of the BRCT (BRCA1 C Terminus) domain (pfam00533) at the C-terminus. It is included in the seed [DNA metabolism, DNA replication, recombination, and repair]
LRKLIRHHDYRYYVLDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPML
SLDNAFDEDELAAFIKRIRRQLGLKVEYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTI
RSIPLRLAGDNPPERLEVRGEVFMPKEDFEALNEERREQGEKPFANPRNAAAGSLRQLDPRITAKRKLRF
FAYGLGEGLELPDATQYEALAWLKKWGFPVSPHIRLCDSIEEVLEYYREIEEKRDSLPYEIDGVVVKVDD
LALQDELGFTSKAPRWAIAYKFPAEEAQTKLLDVVVQVGRTGAITPVAKLEPVFVAGTTVSRATLHNEDE
IEELDIRIGDTVVVRKAGDVIPKVVRVLLEKRTGSERPIRFPTHCPSCGSPLVKIEEEAVIRCPNLNCPA
QRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYALKKEDLLELEGFGEKSAQNLLNAIEKSK
EKPLARLLFALGIRHVGEVTAKNLAKHFGTLDKLKAASLEELLSVEGVGPKVAESIVNFFHDPNNRQLIK
KLEELGVEMESLPEKVNAELAGSPLAGKTFVLTGTLSQMSRDEAKELLENLGGKVASSVSKKTDYVIAGE
KAGSKLAKAQELGIPIINEEEL
>gnl|CDD|273149 TIGR00576, Deoxyuridine_5'-triphosphate_nucleotidohydrolase, deoxyuridine 5'-triphosphate nucleotidohydrolase (dut). The main function of these proteins is in maintaining the levels of dUTP in the cell to prevent dUTP incorporation into DNA during DNA replication. Pol proteins in viruses are very similar to this protein family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Changed role from 132 to 123. RTD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGV
TIDNSPGVIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTEVEFEEVEELDETERGEGGFGST
GV
>gnl|CDD|273150 TIGR00577, Formamidopyrimidine-DNA_glycosylase, DNA-formamidopyrimidine glycosylase. All proteins in the FPG family with known functions are FAPY-DNA glycosylases that function in base excision repair. Homologous to endonuclease VIII (nei). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
PELPEVETVRRGLEPLVLGKTIKSVEVVLRNPVLRPAGSEDLQKRLLGQTILSIQRRGKYLLFELDDGAL
VSHLRMEGKYRLEAVPDAPDKHDHVDFLFDDGTELRYHDPRRFGTWLLLDRGQVENIPLLAKLGPEPLSE
DFTAEYLFEKLAKSKRKIKTALLDQRLVAGIGNIYADEVLFRAGIHPERLASSLSKEECELLHRAIKEVL
RKAIEMGGTTIRDFSQSDGHNGYFQQELQVYGRKGEPCRRCGTTIEKEKVGGRGTHFCPQCQ
>gnl|CDD|273151 TIGR00578, p70_Ku_lupus_autoantigen_partial, ATP-dependent DNA helicase II, 70 kDa subunit (ku70). Proteins in this family are involved in non-homologous end joining, a process used for the repair of double stranded DNA breaks. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Cutoff does not detect the putative ku70 homologs in yeast [DNA metabolism, DNA replication, recombination, and repair]
PEATGDYKYSGRDSLIFLVDASKAMFEESQGEDELTPFDMSIQCIQSVYTSKIISSDKDLLAVVFYGTEK
DKNSVNFKNIYVLQDLDNPGAKRVLELDQFKGDQGPKKFRDTYGHGSDYSLSEVLWVCANLFSDVQVRMS
HKRIMLFTNEDDPHGNDSAKASRARTKAGDLRDTGIFLDLMHLKKPGGFDISLFYRDIITDAEDEDLGVH
PEESSKLEDLLRKVRAKETKKRALSRLKFKLGKDVVMSVGIYNLVQKAGKPAPVRLYRETNEPVKTKTRT
FNMDTGSLLLPSDTKRSQTYGGRQIYLEKEETEELKRFDPPGLQLMGFKPLSMLKKQHHLRPSLFVYPEE
SLVRGSTTLFSALLQKCLEKEVAALCRYISRRNQPPYFVALVPQEEELDDQKIQVTPPGFHLVFLPFADD
KRKVPFTEKVKATPEQVDKMKAIVEKLRFTYRSDSFENPVLQQHFRNLEALALDMMEPEQAVDLTLPKVE
AMKKRLGSLVDEFKELVYPPGYNPEGKVAKRKQAGEGSQSKKPKVENSEEELREHAKKGTLGKLTVSVLK
DFCKAYGLRSGSKKQELLDALTKHLK
>gnl|CDD|273152 TIGR00580, Transcription-repair-coupling_factor, transcription-repair coupling factor (mfd). All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families [DNA metabolism, DNA replication, recombination, and repair]
LVELGYERVDLVEEEGEFSVRGEILDIFPPGSELPVRIEFFGDEIESIREFDVDSQRSLEELLEITILPA
KEFILLEEETIARLKDNAARVEDAKHLETIEALSEGTLPAGEEMFLPLFFEDLSSLFDYLPDNTPILLDD
PERFHSAARFLQRELEEFYNALEEAKKLINPPRLDLDPSELAFEASAISLSRVQLENEHLSLKASEAIEG
AQKHSRLEFGEILAFKEELFRWLKAGFKITVAAESESQAERLKSLLAEHDIAAQVIDESCIIIPAVRYVM
IGALSSGFILPTAGLAVITESELFGSRVLRRPKKSRLKSKPIESLNELNPGDYVVHLDHGIGRFLGLETL
EVGGIERDYLVLEYAGEDKLYVPVEQLHLISRYVGGSGKNPALDKLGGKSWEKTKAKVKKSVREIAAKLI
ELYAKRKAIKGHAFPPDLEWQQEFEDSFPFEETPDQLKAIEEIKADMESPRPMDRLVCGDVGFGKTEVAM
RAAFKAVLDGKQVAVLVPTTLLAQQHFETFKERFANFPVTIELLSRFRSAKEQNEILKELASGKIDILIG
THKLLQKDVKFKDLGLLIIDEEQRFGVKQKEKLKELRTSVDVLTLSATPIPRTLHMSMSGIRDLSIIATP
PEDRLPVRTFVMEYDPELVREAIRRELLRGGQVFYVHNRIESIEKLATQLRELVPEARIAIAHGQMTENE
LEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKKKAYAYLLYPHQ
KALTEDAQKRLEAIQEFSELGAGFKIALHDLEIRGAGNLLGEEQSGHIESIGFDLYMELLEEAIEELKGG
KPPKLEEETDIELPYSAFIPDDYIADDSLRLEFYKRIASAETEEELEKIRDELIDRFGPLPEEARTLLDV
ARLKLLARKLGIRKLK
>gnl|CDD|129670 TIGR00581, Molybdenum_cofactor, molybdenum cofactor biosynthesis protein MoaC. MoaC catalyzes an early step in molybdenum cofactor biosynthesis in E. coli. The Arabidopsis homolog Cnx3 complements MoaC deficiency in E. coli. Eukarotic members of this family branch within the bacterial branch, with the archaeal members as an apparent outgroup. This protein is absent in a number of the pathogens with smaller genomes, including Mycoplasmas, Chlamydias, and spirochetes, but is found in most other complete genomes to date. The homolog form Synechocystis sp. is fused to a MobA-homologous region and is an outlier to all other bacterial forms by both neighbor-joining and UPGMA analyses. Members of this family are well-conserved. The seed for this model excludes both archaeal sequences and the most divergent bacterial sequences, but still finds all candidate MoaC sequences easily between trusted and noise cutoffs. We suggest that sequences branching outside the set that contains all seed members be regarded only as putative functional equivalents of MoaC unless and until a member of the archaeal outgroup is shown to have equivalent function [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
LTHIDEQGAARMVDISAKAETVREAVASGFVRMKPETVAMISEGRVPKGDVLATARVAGIMAAKRTGDLI
PLCHPLPLSKVEVELTVREDRVEITATVRTTGRTGVEMEALTAVSVAALTVYDMCKAVDKDMVIGPVRLL
EKSGGKS
>gnl|CDD|273153 TIGR00583, Double-strand_break_repair_protein_MRE11, DNA repair protein (mre11). All proteins in this family for which functions are known are subunits of a nuclease complex made up of multiple proteins including MRE11 and RAD50 homologs. The functions of this nuclease complex include recombinational repair and non-homolgous end joining. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). The proteins in this family are distantly related to proteins in the SbcCD complex of bacteria [DNA metabolism, DNA replication, recombination, and repair]
EDTIRILVSTDNHVGYGENDPVRGDDSWNTFEEVLQIAKEQDVDMILLGGDLFHENKPSRKSLYQVLRSL
RLYCLGDKPCELEFLSDASVVFNQSAFGNVNYEDPNINVAIPVFSIHGNHDDPSGDGLLCALDLLHATGL
VNYFGKVPEIDNIIVSPILLQKGETKLALYGISNVRDERLVRTFKDNKVSFLRPNAGAEDWFNLLVLHQN
HAAHTSTSFLPESFIPDFFDLVIWGHEHECLPDPVYNPSDGFYVLQPGSTVATSLTPGEALPKHVFILNI
KGRKFASKPIPLQTVRPFVMKEILLDKVPGSRPILKTDNKKETDKRLIDEVEEMINEANAEWKAKRADGE
GDEPREPPLPLIRLKVDYTGPWLNYQVENPKRFSNRFVGRVANANDVVQFYKNNK
>gnl|CDD|273154 TIGR00584, G/T_mismatch-specific_thymine_DNA_glycosylase, mismatch-specific thymine-DNA glycosylate (mug). All proteins in this family for whcih functions are known are G-T or G-U mismatch glycosylases that function in base excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Used 2pf model [DNA metabolism, DNA replication, recombination, and repair]
EAEDTGTKNDNSSEANLTVKKQQRSADAPNMALVEEQEETSGVPKKAPTQEPSEEAPKFRKRKPRSNEPY
RPVEPKKPSDSKKSGKSTKSKEKQEKITDKFKVKRKVDRFNGVSEAELLTKTLPDILTFNLDIVIIGINP
GLMAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREG
GRILVQKLQKYQPRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPR
AQDKVHYYIKLKDLRDQLKGIERNLDVQEVQYTFDLQLAQEDAKKMAV
>gnl|CDD|273155 TIGR00585, DNA_mismatch_repair_protein_MutL, DNA mismatch repair protein MutL. All proteins in this family for which the functions are known are involved in the process of generalized mismatch repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPL
ACERHATSKIQSFEDLERIETLGFRGEALASISSVSRLTITTKTSAADGLAYQALLEGGMIESIKPAPRP
VGTTVEVRDLFYNLPVRRKFLKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKPNQSTKEN
RIRSVFGTAVLRKLIPLDEWEDLDLQLEGFISQPNVTRSRRSGWQFLFINGRPVELKLLLKAIREVYHEY
LPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR
>gnl|CDD|200031 TIGR00586, 8-oxo-dGTP_diphosphatase, mutator mutT protein. All proteins in this family for which functions are known are involved in repairing oxidative damage to dGTP (they are 8-oxo-dGTPases). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Lowering the threshold picks up members of MutT superfamily well [DNA metabolism, DNA replication, recombination, and repair]
KKLQQIAVGIIRNENGEIIITRRADGHMFAKLLEFPGGKEEGGETPEQAVVRELEEEIGIPQHFSEFEKL
EYEFYPRHITLWFWLLERWEGGPPGKEGQPEEWWVLVGLLADDFFPAANPVIIKLLRL
>gnl|CDD|273156 TIGR00587, Probable_endonuclease_4, apurinic endonuclease (APN1). All proteins in this family for which functions are known are 5' AP endonculeases that are used in base excision repair and the repair of abasic sites in DNA.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
KLLGAHVSAAGGLQAAYNRAAEIGATAFMFFLKSPRWWRRPMLEEEVIDWFKAALETNKNLSQIVLVHAP
YLINLASPDEEKEEKSLDVLDEELKRCELLGIMLYNFHPGSALKCSEEEGLDNLIESLNVVIKETKIVTI
LLENMAGQGSELGRSFEELAYIIKVIVDKRRIGVCLDTCHFFAAGYDITTKAYFEVVKNEFDVVVGFKYL
KAIHLNDSKNVLGSRKDRHENIGEGIIGFDAFRLIMDDERFKGIPIILETPENPKYYEEEIEML
>gnl|CDD|211589 TIGR00588, Includes:_DNA-apurinic_or_apyrimidinic_site_lyase, 8-oxoguanine DNA-glycosylase (ogg). All proteins in this family for which functions are known are 8-oxo-guanaine DNA glycosylases that function in base excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is distantly realted to the Nth-MutY superfamily [DNA metabolism, DNA replication, recombination, and repair]
MGHRWASIPIPRSELRLDLVLRSGQSFRWRWEESPAHWSGLLVIADQPVWTLTQTEEQLLCTVYRGDKPT
QDELETKLEKYFQLDVSLAQLYTHWGSVDKHFQYVAQKFQGVRLLRQDPFECLISFICSSNNNIARITRM
VERLCQAFGPRLITLDGVTYHGFPSLHALTGPEAEAHLRKLGLGYRARYIRETARALLEEQGGRAWLQQI
RGASYEDAREALCELPGVGPKVADCICLMGLDKPQAVPVDVHVWRIANRDYPWHPKTSRAKGPSPFARKE
LGNFFRSLWGPYAGWAQAVLFSADLRQGSH
>gnl|CDD|273157 TIGR00589, Methylated-DNA--protein-cysteine_methyltransferase, O-6-methylguanine DNA methyltransferase. All proteins in this family for which functions are known are involved alkyl-DNA transferases which remove alkyl groups from DNA as part of alkylation DNA repair. Some of the proteins in this family are also transcription regulators and have a distinct transcription regulatory domain. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGL
ERKEFLLEHE
>gnl|CDD|273158 TIGR00590, Proliferating_cell_nuclear_antigen, proliferating cell nuclear antigen (pcna). All proteins in this family for which functions are known form sliding DNA clamps that are used in DNA replication processes. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MFEARLIQASLLKKLLEAIKDLVNDANFDCSESGISLQAMDSSHVALVSLTLRAEGFEHYRCDRNLALGV
NLNSLSKILKCANNEDSVTLKAEDNADTLIFVFESPKQDKISDYELKLMDIDVEHLGIPDQDYDCVVEMP
SSEFARICRDLSQFSDSVVISCTKEGVKFSAKGDIGSANVKLKQNSDTDKEEEAVTIEMKQPVTLTFAIK
YLNLFTKATPLSDRVTLSMSNDVPLVVEYKIKDMGFLRFFLAPKIEDEE
>gnl|CDD|129679 TIGR00591, Deoxyribodipyrimidine_photo-lyase, photolyase PhrII. All proteins in this family for which functions are known are DNA-photolyases used for the direct repair of UV irradiation induced DNA damage. Some repair 6-4 photoproducts while others repair cyclobutane pyrimidine dimers. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MIFAKKRRRLLSETEKPDLRSSGVVVYWMSRDQRVQDNWALIAAQTLALKKKLPLHVCFCLVDFFLAATR
RHYFFMLGGLDEVANECERLIIPFHLLDGPPKELLPYFVDLHAAAAVVTDFSPLRQPEQWDEAVGKLLPK
DVPFQQVDAHNVVPCWAASKKLEYAARTIRGKIRKLLPEYLTEFPRVLKHPSPLDLEAGPVDWDAVRDSL
AVERSVEEVVWAKPGTTAGLIMLESFIEKRLCFFRTRRNDPNNDALSMLSPWLHFGQLSAQRAARAVERA
RGNAGESVEFFEEELVVRRELADNFCFYNPYYDSLCGAYWWARTTLDDHAKDKREHLYSLEQLEKSTTHD
YLWNAAQEQLVTEGKMHGFLRMYWAKKILEWTHSPEEALSIAIYLNDKYILDGRDPNGYVGCMWSICGIH
DQGWAERIVFGKIRYMNYAGCRRKFNVAYFERKY
>gnl|CDD|273159 TIGR00592, DNA_polymerase_alpha_catalytic_subunit, DNA polymerase (pol2). All proteins in this superfamily for which functions are known are DNA polymerases.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MVEDTDYIYEDVDEEEYSKRVQEKPIDDIFVKDDGEGYVEDGREFFPDEDDILDLDKDDGSAAEAKKKDK
ENHKKVTKPNNIKAVRIACAPKKKKDRKKSLGKDGLLGDILQELNKTETAQRKITPRLVSVPKLKFSSPA
DVPAINDFSNHHPAVVDIVKKAIPVSTRYLLEKILIPVPLKRAEFAGGDVQMEGDPELKLASFDIETYFH
DGKDFFPGDENPADEEIMISTTPVIAKQWDYESEPEARVVTWKKPDKPTTGSYVESVSEEISMIKRFWDV
IDQEDTDVEITVNGDNFDLVYLADRQVFQFYWDAYEDPAEKLGVVLLFGRDVDHVSPCVQVKGINRDLFF
LPREGKIDFDLGKVTRRTINLPDYYLEFVSELALGYKKEKFRAKPIAKKYEFEAPDIDAPYSSEYLEVTY
ELGKEFAPMEALPSDLKGQTFWHVFGSNTGNLERFLLLRKIKGPCWLAVKGPDELEYPRRSWCKYEGGYV
KPPNVEKGLDKTPPPLVVLDFSMKSLNPSIIRNEIVSIPDTLHREFALDKPPPEPPYDVHPCVGTRPKDC
SFPLDLKGEFPGKKPSLVEDLATERALIKKFMAKVKKIDPDEIVGHDYQQRALKVLANRINDLKIPTWSK
IGRLRRSPKFGRRFGERTCGRMICDVEISAKELIRCKSYDLSELVQQILKTERKVIPIDNINNMYSESSS
LTYLLEHTWKDAMFILQIMCELNVLPLALQITNIAGNIMSRTLMGGRSERNEFLLLHAFYENNYIVPDKQ
IFRKQQKLGDEDEEIDGYKKGKKAAYAGGLVLEPKVGLYDKYVLLMDFNSLYPSIIQEFNICFTTVQQKV
DEDELPELPDSELEMGILPRELRKLVERRKEVKKLMKQDLNPDLRLQYDIRQKALKLTANSMYGCLGYSK
SRFYAKPLAALVTAKGREILEHTRQLVEEMNLEVIYGDTDSIMINTPGTKYEEVFKIGKEFKSEVNKLYK
LLELDIDGVFKRLLLLKKKKYAAIKVEGDSDGNYTTKQEVKGLDIVRRDWSPLAKETGKKVLDTILSDKD
VEEAVEEVQEVLEKIGKNVLNGEVPLEKFVINKQLTRDPKDYPDGASLPHVHVALRINARGGRKVKAGDV
VSYVICKDGGNLSARQRAYALEELQRKHNNLIYDTQYYLEHQIHPVVLRILE
>gnl|CDD|273160 TIGR00593, DNA_polymerase_I, DNA polymerase I. All proteins in this family for which functions are known are DNA polymerases Many also have an exonuclease motif. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
LLLIDGHSLAFRAYFALKNKPLTNSKGEPTNAVYGFTKMLLKLLKEEKPTYVAVAFDSGTPTFRHEAYAE
YKANRAPTPEELIEQIPLIKELLDALGIPILEVEGYEADDVIATLAKQAEKEGYEVRIISGDKDLLQLVS
DNVKVLIPKGKTSFTEITPEYVVEKYGVTPDQLVDLKALVGDSSDNIPGVKGIGEKTAAKLLQEFGSLEN
IYENLDQIKSAKMREKLIAHKEDAFLSKELATIVTDVPLEVDLEDLRLSEPDRERLYALLQELEFKSLLD
RLENLESPVIDDHAPVLTEKTSCAKESEEAAPLANPAEKAEVGGFVLERLLDQLKKALALAFATENQSYV
AYASEADGIPLLTILTDDKFARWLLNEQIKKIGHDAKFLMHLLKREGIELGGVIFDTMLAAYLLDPAQVS
TLDTLARRYLVEELILDEKIGGKLAKFAFPPLEEATEYLARRAAATKRLAEELLKELDENKLLSLYREIE
LPLSKVLAEMEKTGIKVDADYLQELSQEFGEEIADLEEEIYELAGEEFNINSPKQLGEVLFEKLGLPVGK
KTKTGYSTDADVLEKLREKHPIIALILEYRQLTKLKSTYVDGLPELVNPDTGRIHTTFNQTGTATGRLSS
SNPNLQNIPIRSEEGRKIRKAFVAEKGWLLISADYSQIELRVLAHLSQDENLIEAFQNGEDIHTETASRL
FGVEIEDVTPNMRRIAKTINFGVVYGMSAFGLAQELGISRKEAKEFIERYFARYPGVKDYIENTVEEARK
KGYVETLFGRRRYIPDINSRNRNVREAAERMAINAPIQGSAADIMKIAMIKLDKRLKERKLKARLLLQVH
DELIFEAPEEEAEEVAALVKEVMEHAYPLAVPLEVEVGTGKNWGEAK
>gnl|CDD|273161 TIGR00594, DNA_polymerase_III_subunit_alpha, DNA-directed DNA polymerase III (polc). All proteins in this family for which functions are known are DNA polymerases. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
FVHLHVHSDYSLLDGAAKIKPLVKKAKELGMPALALTDHGNMFGAVEFYKACKKAGIKPIIGCEAYVAPG
SRFDKKRISKGKEAYHLILLAKNNTGYRNLMKLSSLAYLEGFYYKPRIDKELLEEHSEGLIALSACLSGE
VPYLLLLGEERLAEEAALKYQEIFGDDYYLELQDHGIPEQRVVNEALLEISEELGIPLVATNDVHYINPE
DAHAHEILLCIQTGKTLSDPKRLKFYSDEFYLKSPEEMAELFADIPEALANTVEIAERCNLVDVKLGPPR
LPSYQIPPDFTSQEDYLRHLADEGLRERLAAGPPGYKRRAQYKERLEYELDVINSMGFPGYFLIVWDFIK
WAKDHGIPVGPGRGSAAGSLVAYALKITDIDPIKHGLLFERFLNPERISMPDIDIDFCDERRDEVIEYVA
DKYGHDNVAQIITFGTMKAKAALRDVARVLDIPYAEADRIAKLIPPRPGKTLKEALEASPQLRQLYEEDP
EVKQLIDMARKLEGLNRNAGVHAAGVVISSEPLTDYVPLYKDKEGGAISTQYDMDDLEAVGLLKMDFLGL
KTLTLIQDATELIRKRRGIDLDIASIPLDDKKTFSLLQEGDTTGVFQLESRGMQDLLKRLKPDGFEDIIA
VNALYRPGPMESGMIPDFIDRKHGREPIEYPHPLLEPILKETYGVIVYQEQVMQIAQRLAGFSLGEADLL
RRAMGKKKAEEMAKEREKFVEGAEKNGYDPEIAENLFDLIEKFAGYGFNKSHAAAYGMISYQTAYLKANY
PAEFMAALLTSEINDIEKVAVYIAEAKKMGIEVLPPDINESGQDFAVEDKGIRYGLGAIKGVGESVVKSI
IEERNKNGPFKSLFDFINRVDFKKLNKKVLEALIKAGAFDSLGPNRKTLLASLDDALDAVSRKKKAEALG
QNSLFGALSEGTKPEYVFFPPDEEWPDKKLLALEKETLGLYVSGHPLDAYEKALKNTATPAAIEDLEAPN
DSQVRTLGGLNSVKKKITTKNGKPMAFLQLEDETGSIEVVVF
>gnl|CDD|273162 TIGR00595, Primosomal_protein_N', primosomal protein N'. All proteins in this family for which functions are known are components of the primosome which is involved in replication, repair, and recombination.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
LLFGVTGSGKTEVYLQAIEKVLALGKSVLVLVPEIALTPQMIQRFKYRFGSQVAVLHSGLSDSEKLQAWR
KVKNGEILVVIGTRSALFLPFKNLGLIIVDEEHDSSYKQEEGPRYHARDVAVYRAKKFNCPVVLGSATPS
LESYHNAKQKAYRLLVLTRRVSGRKPPEVKLIDMRKEPRQSFLSPELITAIEQTLAAGEQSILFLNRRGY
SKNLLCRSCGYILCCPNCDVSLTYHKKEGKLRCHYCGYQEPIPKTCPQCGSEDLVYKGYGTEQVEEELAK
LFPGARIARIDSDTTSRKGAHEALLNQFANGKADILIGTQMIAKGHHFPNVTLVGVLDADSGLHSPDFRA
AERGFQLLTQVAGRAGRAEDPGQVIIQTYNPNHPAIQAALTGDYEAFYEQELAQRRALNYPPFTRLIRLI
FRGKNEEKAQQTAQAAHELLKQNLDEKLEVLGPSPAPIAKIAGRYRYQILLKSKSFLVLQKLVNKTLLKE
IPSSSVYCEVDVDPI
>gnl|CDD|273163 TIGR00596, DNA_repair_endonuclease_XPF, DNA repair protein (rad1). All proteins in this family for which functions are known are components in a multiprotein endonuclease complex (usually made up of Rad1 and Rad10 homologs). This complex is used primarily for nucleotide excision repair but also for some aspects of recombinational repair in some species. Most Archaeal species also have homologs of these genes, but the function of these Archaeal genes is not known, so we have set our cutoff to only pick up the eukaryotic genes.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford Universit [DNA metabolism, DNA replication, recombination, and repair]
REKVYLEGGIFSITSRILVVDLLTGIIPPELITGILVLRADRIIESSQEAFILRLYRQKNKTGFIKAFSD
NPEAFTMGFSPLETKMRNLFLRHVYLWPRFHVEVASSLEKHKAEVIELHVSLTDSMSQIQSAILECLNKC
IAELKRKNPELDMEDWNLENALTKSFDRIIRRQLDPNWHRLSYKTKQLVGDLKILRHLLQSLVTYDAVSF
LGLLDTSLRANKPAVSRKYSESPWLLLDAAQLIFSYARQRVYYEGEGPNMKNEPVLEENPKWEVLTDVLK
EISHEMRMTNRLQGPGKVLIMCSDNRTCLQLRDYLTTSNKKRGSRAFLLNKLRWYRKWREETSKLAKEVQ
SQDTFPENASSNVNKTFRKEQVPTKRRRVRGGSEVAVEKLRNANTNDMQHFEEDHELEEEGDDLEDGPAQ
EINAANDSKIFEIIDEENDIDIYSGAEFDNLPQHITHFLWGERDEYVLRCSLEELMPRYVIMYEPDISFI
RQLEVYKASRPLRPLRVYFLYYGGSIEEQRYLTSLRREKDAFTKLIREKANMSIPFETNEDLESKFLRLV
NTRISKLRKSKTRNAGGQLGFANLTQPKVIVDMREFRSSLPSLLHRRGIRVIPCMLTVGDYILTPDICVE
RKSISDLIGSLNNGRLYNQCEKMLRYYAYPVLLIEFDQNKSFSLEPRNDLSQEISSVNNDIQQKLALLTL
HFPKLRIIWSSSPYATAEIFEELKLGKEEPDPATAAALGSDENTTAEGLKFNDGPQDFLLKLPGVTKKNY
RNLRKKVKSIRELAKLSQNELNELIGDEEAAKRLYDFLRTEKLE
>gnl|CDD|129685 TIGR00597, DNA_excision_repair_protein_ERCC-1, DNA repair protein rad10. All proteins in this family for which functions are known are components in a multiprotein endonuclease complex (usually made up of Rad1 and Rad10 homologs). This complex is used primarily for nucleotide excision repair but also for some aspects of recombination repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
NSILVNPRQKGNPLLKHVRNVPWEYGDVIPDYVLGQGTCALFLSLRYHNLHPDYIHRRLQSLGKNFNLRI
LLVQVDVKNPQQALKELAKMCILNDCTLILAWSFEEAARYLE
>gnl|CDD|273164 TIGR00598, DNA_repair_protein_complementing_XP-A_cells, DNA repair protein. All proteins in this family for which functions are known are used for the recognition of DNA damage as part of nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
CEECGKIFMDSYLFDHFDCAVCDNCRDKDDKYKLLTKTEAKEEYLLKDCDLDKREPLLRRIVKKNPHNPR
WGDMKLYLKLQVEKRALEVWGSEEALDEEKERREESKEEMKEKKFEKKLKELRRAVRSSEYTNKKEGRVH
EHEFGPETNGVEEDTYRRTCTTCGLEETYEKM
>gnl|CDD|273165 TIGR00599, rad18, DNA repair protein rad18. All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MDELDITDSSDWLTTPIPSLYPLDTSLRCHICKDFFDVPVLTSCSHTFCSLCIRRCLSNQPKCPLCRAED
QESKLRSNWLVSEIVESFKNLRPSLLEFLRIPKTTPVENPDLAGPENSSKIELIEESESDGVDAEDEDLQ
RSATSSRALAARSTADILQLSSDPSKRNDADYRSEPPNEGLVQCPICQQRMPEKAVERHLDSECLGSPSL
GASTTFPTESNPHNKSSSRFSFRTVDKSSTGETSHVDKYLNSMMSKPPERLPKINYSLLTDSQIRKKLSE
LGLSTNGTRQLLQKRHNEWETLWNSNCDSLEPVDKRELLRQLDSWERTQGKTPQNSGNKGGISKLMIMKS
NGKTGAYRKLKKFNGKGWMVMYRKDFADLIREAKMKIKRSTSDSNGS
>gnl|CDD|273166 TIGR00600, DNA_repair_protein_complementing_XP-G_cells, DNA excision repair protein (rad2). All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MGVQGLWKLLECSGRPVSPETLEGKRLAVDISIWLNQALKGVRDREGNAIKNSHLLTLFHRLCKLLFFRI
RPIFVFDGGAPLLKRQTLAKRRQRRDGASEDARKTAEKLLATFLKRQAIKTAFNSKKSTPEALPSVQQVP
RPQDLYVLPPLPEEEKHSSEEESEKEWEERMNQKQALQEEFFHNPSAIDIESEEFSSLPPEVKHEILTDM
KLFTKRRRTLFEAMPENSMDFSQYQLKGLLKKNDLNQHIENVTKEMNQQHSGNIQRQYRDEGGFLKEVEL
RRVVSEDTSHYILIKGIQGKTAVKAVDSDDESLPSLSSQLDSNSEDLKSSPWEKLKPESESIVEAEPPSP
RTLLAKQAAMSESSSEDSDESEWERQELKRNNVAFVDDGSLSPRTLQAIGQALDDDEDKKVSASSDDQAS
PSKKTKMLLISRIEVEDDDLDYLDQGEGIPLMAALQLSSVNSKPEAVASTKIAREVTSSGHEAVPKAVQS
LLLGATNDSPIPSEFTILDRKSELSIERTVKPVSSEFGLPSQREDKLAIPTEGTQNLQGISDHPEQFEFQ
NELSPLETKNNESNLSSDAETEGSPNPEMPSWSSVTVPSEALDNYETTNPSNAKEVRNFAETGIQTTNVG
ESADLLLISNPMEVEPMESEKEESESDGSFIEVDSVSSTLELQVPSKSQPTDESEENAENKVASIEGEHR
KEIEDLLFDESEEDNIVGMIEEEKDADDFKNEWQDISLEELEALEANLLAEQNSLKAQKQQQKRIAAEVT
GQMILESQELLRLFGIPYIVAPMEAEAQCAILDLLDQTSGTITDDSDIWLFGARHVYKNFFNQNKFVEYY
QYVDIHNQLGLDRNKLINLAYLLGSDYTEGIPTVGPVSAMEILNEFPGDGLEPLLKFKEWWHEAQKDKKK
RENPNDTKVKKKLRLLQLTPGFPNPAVADAYLRPVVDDSKGSFLWGKPDLDKIREFCQRYFGWNREKTDE
VLLPVLKKLNAQQTQLRIDSFFRLAQQEKYDAKDIKSQRLKRAVTCMLRKEKEK
>gnl|CDD|273167 TIGR00601, UV_excision_repair_protein_RAD23_homolog_A, UV excision repair protein Rad23. All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MTLTFKTLQQQKFKIDMEPDETVKELKEKIEAEQGKDAYPVAQQKLIYSGKILSDDKTVKEYKIKEKDFV
VVMVSKPKTGTGKVAPPAATPTSAPTPTPSPPASPASGMSAAPASAVEEKSPSEESATATAPESPSTSVP
SSGSDAASTLVVGSERETTIEEIMEMGYEREEVERALRAAFNNPDRAVEYLLTGIPEDPEQPEPVQQTAA
STAAATTETPQHGSVFEQAAQGGTEQPATEAAQGGNPLEFLRNQPQFQQLRQVVQQNPQLLPPLLQQIGQ
ENPQLLQQISQHPEQFLQMLNEPVGELASESDMEGGVGAIAEAGLPQMNQIQVTPEEKEAIERLCALGFD
RGLVIQAYFACDKNEELAANYLLSQNFD
>gnl|CDD|129690 TIGR00602, Checkpoint_protein_rad17, checkpoint protein rad24. All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MDVTDWVKPSFDDFLLSSLISTITKWSLSRPTSSHRRKNSPSTDIHARKRGFLSLEQDTGLELSSENLDG
NEPWVEKYKPETQHELAVHKKKIEEVETWLKAQVLENAPKRILLITGPSGCGKSTTIKILSKELGIQVQE
WSNPTLPDFQKNDHKVTLSLESCFSNFQSQIEVFSEFLLRATNKLQMLGDDLMTDKKIILVEDLPNQFYR
DTRALHEILRWKYVSIGRCPLVFIITESLEGDNNQRRLLFPAETIMNKEILEEPRVSNISFNPIAPTIMK
KFLNRIVTIEAKKNGEKIKVPKKTSVELLCQGCSGDIRSAINSLQFSSSKSGSLPIKKRMSTKSDAHASK
SKIKGKHSSNNENQEIQALGGKDVSLFLFRALGKILYCKRATLNELDSPRLPSHLSELSRDTLMVGPEEV
VEMSHMPGDKTFNLYSHQNYNDFFVEFDDEVKASEFLNFADILSGDWNTRSLLREYSTSSARRGVMHSNK
ARGIAHCQGGKSSFRPLHKPQWFLISKKYRENCLAAKALFKVEDFCLPADCLQTQLLPYLALDTIPMRND
AQISFIDDLGRLPLKRDFRRLKMEALTDREVGMIDPDSGDEETSFGDDPAVESDSDPSQAAGPETWSLPD
SDNSLSE
>gnl|CDD|273168 TIGR00603, repair_helicase_RAD25, DNA repair helicase rad25. All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
DYSKQLELKPDHGSRPLWVAPDGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSV
GLETEDIIEVLGRLSKTPIPKGIIEFIRLCTQSYGKVKLVLKHNRYFVESPHPEVLQRLLKDPVIAPCRI
DPTEEESLQTPTYGSKEDFIINKPGFTGGASAGQLEANQGESAVPKDIADFYELEEEEEDEDEETATHSF
EIDQEQVEEVKKRCIELDYPLLEEYDFRNDTVNPDLNIDLKPTTQIRPYQEKSLSKMFGNGRARSGIIVL
PCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWKQQFKMWSTIDDSQICRFTSDAKERFHGEAGVVVST
YSMVAHTGKRSYESEKVMEWLTNREWGLILLDEVHVVPAAMFRRVLTIVQAHCKLGLTATLVREDDKITD
LNFLIGPKLYEANWMELQKKGFIANVQCAEVWCPMTPEFYREYLRENSRKRMLLYVMNPNKFRACQFLIR
FHEQRGDKIIVFSDNVFALKEYAIKLGKPFIYGPTSQQERMQILQNFQHNPKVNTIFLSKVGDTSIDLPE
ANVLIQISSHYGSRRQEAQRLGRILRAKKGSDAEEYNAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFKV
ITHLPGMDNESNLAYSSKEEQLELLQKVLLAGDLDAELEVLEGEFGSRALGASRSMSSASGKAVRRGGSL
SSLSGGDDMAYMEYRKPAIKKSKKEVHPLFKK
>gnl|CDD|273169 TIGR00604, ATP-dependent_RNA_helicase_CHL1, DNA repair helicase (rad3). All proteins in this family for which funcitons are known are DNA-DNA helicases that funciton in the initiation of transcription and nucleotide excision repair as part of the TFIIH complex. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
ELLVYFPYEKIYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQEKPEVRKIIYASRTH
SQLEQATEELRKLMSYRTPRIGEESPVSGLSLASRKNLCLHPEVSKERQGKVVNGKCIKLTVSKIKEQRT
EKPNVESCEFYENFDELREVEDLLLSEIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLPYQYLLDPK
IRSAVSIELKDSIVIFDEAHNLDNVCISSLSSNLSVRSLKRCSKEIAEYFEKIEERKEVDARKLLDELQK
LVEGLKQEDLLTDEDIFLANPVLPKEVLPEAVPGNIRIAEIFLHKLSRYLEYLKDALKVLGVVSELPDAF
LEHLKEKTFIDRPLRFCSERLSNLLRELEITHPEDFSALVLLFTFATLVLTYTNGFLEGIEPYENKTVPN
PILKFMCLDPSIALKPLFERVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHILKRENLLTLIVTRGSD
QVPLSSTFEIRNDPSLVRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEKKKLIFVE
TKDAQETSDALERYKQAVSEGRGAVLLSVAGGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLARLEFL
RDQYPIRENQDFYEFDAMRAVNQAIGRVIRHKDDYGSIVLLDKRYARSNKRKKLPKWIQDTIQSSDLNGM
AISLT
>gnl|CDD|273170 TIGR00605, DNA_repair_protein_rhp41, DNA repair protein rad4. All proteins in this family for which functions are known are involved in targeting nucleotide excision repair to specific regions of the genome.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MNEDLAKEYFELIRKVENEKEAEKQPKSRRRKVRRENEPSLRRRKKRFKTGLNELPHEVVLMCNLDSTHS
DDRVVSVPDSLSVSEEIPSREEDYDSREFEDVYLSNLVAEFETISVEIKPSSKAESDDDAETLSRNVCSN
EARKDRKYIHILYLLCLMVHLFTRNEWSLSAPLKSAKLSNLIPEKVRLLLHPSVRKSEELPSRSLRGLRK
PLVEKLKKCMETWQKGLRKTTKGLLKLLNGGRYSRSKWEEIEKSSNRKLGGRKYRTLKRGSILENLNVPT
RLVFSDFLLSVSKGHNDPEISSEGFVPKLSACNANQRLIMSCESADRTSRFRMKKDPSLPGFSAYSDMDK
SPIFTCEEGDKFIDRWITYVDFWVEVFIEQEEKWVCVDAVHSGVVPKGVTCFEPATLMMTYVFAYDRDGY
VKDVTRRYCDQWSTKVRKRRVEKADFGETWFRPIFGALHKRKRTIDDIEDQEFLRRHESEGIPKSIQDLK
NHPLYVLERHLKKTQALKPGKKACTLGFVNGKAGVYSRKDVHDLKSAEQWYKKGRVIKLGEQPYKVVKAR
ARTVRLPKGEAEEEDLGLYSYEQTELYIPPPAVDGIVPKNAYGNIDLFVPSMIPKGAVHLRLPGAIKAAK
KLNIDYAPAVTGFDFHRGYSKPVLDGIIVCEEFREAIETAWEEIEQIQEEKEQEKHRKRALGNWKTLLKG
LRIRERLKETYGK
>gnl|CDD|129694 TIGR00606, RAD50_homologue_ceRAD50, rad50. All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University)
AKFLKMSILGVRSFGIEDKDKQIIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPK
VAQETDVRAQIRLQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVITRYKHGEKVSLSSKCAEIDREMI
SHLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELK
YLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQ
MEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQG
RLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSK
ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKA
EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSD
ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD
VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDL
QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ
ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDT
VVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ
DSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELN
TVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVL
QMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDL
DIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKG
DTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRN
FQLLVITHDEDFVELLGRSEYVEKFYRLKKNEDQCSEIVKCSPSSLGKRVH
>gnl|CDD|129695 TIGR00607, DNA_repair_protein_RAD52_homolog, recombination protein rad52. All proteins in this family for which functions are known are involved in recombination and recombination repair. Their exact biochemical activity is not yet known.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
AIQKALRQKLGPEYISSRSGGGGQKVCYIEGWKVINLANEIFGYNGWSHSITQQNVDFVDENNGKFSVGV
CAIVRVTLKDGSYHEDVGYGVSENLRSKALAFEKAKKEAVTDALKRALRNFGNALGNCLYDKDYLRKINK
LKQLPPEFDLGNLFRQDDEPS
>gnl|CDD|273171 TIGR00608, UPF0758_protein_aq_1610, DNA repair protein radc. The genes in this family for which the functions are known have an as yet porrly defined role in determining sensitivity to DNA damaging agents such as UV irradiation. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MPREKLLKFGAEALSDYELLAIILRTGTPKGLDVLSLSKRLLDVFGRQDSLGHLLSAPPEELSSVPGIGE
AKAIQLKAAVELAKRYAKSRMLERPVIRSPEAAAEFLHTDLAHETREHFMVLFLDRKNRLIAKEVVFIGT
VNHVPVHPREIFKEALKLSASALILAHNHPSGEPSPSQEDILITERLRKAAELLGIELLDHLIIGKGRYV
SFREEGLL
>gnl|CDD|273172 TIGR00609, RecBCD_enzyme_subunit_RecB, exodeoxyribonuclease V, beta subunit. The RecBCD holoenzyme is a multifunctional nuclease with potent ATP-dependent exodeoxyribonuclease activity. Ejection of RecD, as occurs at chi recombinational hotspots, cripples exonuclease activity in favor of recombinagenic helicase activity. All proteins in this family for which functions are known are DNA-DNA helicases that are used as part of an exonuclease-helicase complex (made up of RecBCD homologs) that function to generate substrates for the initiation of recombination and recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
LDPLTIPLNGTFLIEASAGTGKTFTIAQLYLRLLLEGGPLTVEEILVVTFTNAATEELKTRIRGRIHQAL
RALKAALTSQELPEPLKEAIQDEKVKQAITRLRNALATMDEAAIYTIHGFCQRMLEQHAFESDEIFDVEL
IEDESLLLAEITKDFWRRNFYNLPFDIAQIVLKTKKSPQAVLTQILADLLLQSYLAFPSPPLDLEQLIKW
HEQIYKDLDKLDHAVFEEIDKLNAERNNLFCLKDRVFLTLLKEVQEELKKEKKRRREIGFDDLLSRLETA
LKSAEGEKLAQAIREQYPIALIDEFQDTDPQQYRIFSKLFIAQKETSLFLIGDPKQAIYSFRGADIFTYL
QAKSKADARYTLGTNWRSTPALVGSLNKLFSLISNPFLEKPIFIPVLAHQKNSKGSFVINGQEQPPIHFF
TTEVESEGVDDYRQTIAQKCAREIALWLASAALGLANFIATFGGRPLRAGDIAVLVRGRKEANQIRKALK
KAQIPSVYLSDKSSVFATEEAQELLALLEALLEPENEGTLRAALASSIFGLSALELETLNQDEITWERVV
EKFREYHDIWRKIGVLAMFQRLMLEKGIGERLLSQPGGERILTNLLHLAELLQEAAHQERNKLSLLRWLE
DQISNEEEEEEEIIRLESDAELVKIVTIHKSKGLEYPIVFLPFITDAKKSNFASLHDQHSHEYQLYDFNQ
SEENQKLARVERLAEDLRLLYVALTRAKKQLFIGIAPLITSKLSNLAYSALHNSALGYQKQDGETDNITG
LKQCLAALADPAGISSIPAKPIGANSSKKEPASTALLEARTFHRRIRENWRITSFSSLKELEEAVTEEPA
PGLDYEVSSLEISAQDFPKGKKTGTLLHAILESLIFSQAADLEKQNNLIAEKLKKTGLEGLWEPELQEWL
EKMLNTPLTFSRAITLSQIDPEDRQREMEFLLPINPEFQKQKLNFVIRAYPDRAGSPDLHFQLLRGLLKG
FIDLVFEHNGRYYILDYKSNWLGKDASDYSPEALTEAILKERYDLQYLIYTLALHRYLRKRLKDYDYERH
FGGVIYLFLRGIDGNKGNGIFFWNPPANLIDLLKELF
>gnl|CDD|273173 TIGR00611, DNA_replication_and_repair_protein_RecF, recF protein. All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRDKPLIRFGAEAFVI
EGRVSKGDREVTIPLEGLLKKKGKKAKVNIDGQDKLSDLAGLLPMQLFAPEDLTLVKGSPKYRRRFLDWG
LFQVEPVYLSAWSDYQRVLKQRNAALKQAQRQYGDRTTLEVWDSQLAELGAKVSAWRAEFIEKLEPEAQK
AHQLLLPELESLSLFYRGELWDKETDYAEALARNFERDLERGYTLVGPHRDDLRFRLNGLPVEDFASQGQ
LRSLALALRLAEGELLREEGGEYPILLLDDVASELDDQRRRLLAELLQSLGVQVFVTAISLDHLKEMWDP
NRVTIALVSVDRGTI
>gnl|CDD|273174 TIGR00612, ispG_gcpE, 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase. This protein of previously unknown biochemical function has now been identified as an enzyme of the non-mevalonate pathway of IPP biosynthesis. Chlamydial members of the family have a long insert. The family is largely restricted to Bacteria, where it is widely but not universally distributed. No homology can be detected between the GcpE family and other proteins [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
RRKTRQVRVGNVKVGGDAPIVVQSMTNTDTHDVDATVAQIRRLEEAGCEIVRVTVPDKESAEALEEIKEG
SNVPLVADIHFAYSYAALAMAKGVAKVRINPGNIGFEERVRDIVEKARRHGKAMRIGVNHGSLERRLLEK
YGDPTAEAMVQSALEWAEILEKLGFRNVVVSMKASDVLQTVAAYRLLAERSDYPLHLGVTEAGMGVKGII
KSSVGIGILLAMGIGDTIRVSLTDDPVVEVPVAYEILQSLGLRRRGVEIVACPSCGRTGFDLEKVVKEVQ
EALSHLKTPLKVAVMGCVVNGPGEAKHADIGISGPGTGFAWLFKHGKPKAKVPETDMVDELIKLIQ
>gnl|CDD|273175 TIGR00613, DNA_repair_protein_RecO, DNA repair protein RecO. All proteins in this family for which functions are known are DNA binding proteins that are involved in the initiation of recombination or recombinational repair [DNA metabolism, DNA replication, recombination, and repair]
IKDEGIVLKSRDYGETDKIITLFTEEYGKVSFVAKGARKSKSRMKAVLQPFSLGDFVWYKRSGLSTLNQG
ELINSFEGIKSDLFLLAYASYIAELIDRLLPEGEPNPKLFELLLKTLELINEGGNPELLLRLFELKLLQI
LGYALDLDKCAVCGSKEDLIYFSMTYGGALCRQCGEKDPHAIPIDPKLLRLLRYLLKLDLEKLLSIEIKP
EIKLEARRILDEYYEEYLGKPLKSKKFLDQL
>gnl|CDD|129701 TIGR00614, Werner_syndrome_ATP-dependent_helicase, ATP-dependent DNA helicase, RecQ family. All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQ
LQALGIPATFLNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASNRLLQTLEERKGITLIAVDEAHCIS
QWGHDFRPDYKALGSLKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTP
KILEDLLRFIRKEFEGKSGIIYCPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVV
VATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGNF
RTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGFNKSFCIMGTEKCCDNCCKRLDYKTKDVTDKVYDFGP
QAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKDE
>gnl|CDD|273176 TIGR00615, Recombination_protein_RecR, recombination protein RecR. All proteins in this family for which functions are known are involved in the initiation of recombination and recombinational repair. RecF is also required. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
QYPPPISKLIESLKKLPGIGPKSAQRLAFHLLKRDPSEVLRLAQALLEAKENLRTCSVCGAISDQEVCNI
CSDERRDNSVICVVEDPKDVFALEKTKEFRGRYHVLGGHISPLDGIGPEDLTIAALLKRLQEESVKEVIL
ATNPTVEGEATALYIARLLQPFGVKVTRIASGLPVGGDLEYADEVTLARALEGRR
>gnl|CDD|129703 TIGR00616, Uncharacterized_protein_YqaK, recombinase, phage RecT family. All proteins in this family for which functions are known bind ssDNA and are involved in the the pairing of homologous DNA This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). RecT and homologs are found in prophage regions of bacterial genomes. RecT works with a partner protein, RecE [DNA metabolism, DNA replication, recombination, and repair, Mobile and extrachromosomal element functions, Prophage functions]
ATKQSPIIKNNLQKKQGNVPPVQVKGADVKGLLSSPSMIKRFEEVLPRHKRATRFTRIALSLIRSEPMLQ
KCDTMSVISAAMVAATLGLEPGKNLGYAYILPYGNKNEKAKNVQFILGYKGYIDLARRSGQYKSISAIPV
HEGDLFKWEPGLDEKLIHRPGRESDAPVGYYAVAELKDGGRKFVVMTKAQVEKHRKKFSKSDNGGPWKNH
WDAMAKKTVLRALLKYLPLSVEMQKAVIEDE
>gnl|CDD|273177 TIGR00617, Replication_protein_A_70_kDa_DNA-binding_subunit, replication factor-a protein 1 (rpa1). All proteins in this family for which functions are known are part of a multiprotein complex made up of homologs of RPA1, RPA2 and RPA3 that bind ssDNA and function in the recognition of DNA damage for nucleotide excision repairThis family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
AVSLSNGAIALIMTNGEANGYPPDPVLQVLDLKPINGAQDPRRYRIVISDGIYYSKAMLATQLNPLVREG
ELQEGTIIRLTKFEVNTIGKDGRKVLIVYELEVVKPELKVRDKIGNPVTYEKYLDSWHEEQVLASKPATN
PANPPNAKAPKNEVASYNNAANPERGNAPPAPNSGSTRRVMPIASLSPYQNKWTIKARVTNKSEIRTWSN
ARGEGKLFNVELLDESGEIRATAFNEQADKFYDIIQEGKVYYISKGSLKPANKQFTNLGNDYEMTLDRDT
VIEECEDETAIPKIQFNFVKIDDIGGYEGNSLVDVIGIVQSVSPTQTITSRKNNKEFPKRDITLVDDSGK
SVRVTLWGDDATKFDVSVQPVIAIKGVRVSDFGGKSLSTGGSSTIIVNPDIPEAEKLKGWYDNEGKGTMA
SSISDMMSGRVGGSNAERKTIAEIQAENLGKSDKPDYFSVKATISYLKPDNALYRACPSEDCNKKVVDQG
DGTYRCEKCNKNFAEFKYRYILQISISDETGQLWVTAFNDQAEQILGKSAAELGELKEEDPDEFEAIFQE
AQFVPYIFRLRVKQDTYNDESRQKYTVMSVDPVNYRAEAKYLLQEIEK
>gnl|CDD|129705 TIGR00618, Nuclease_SbcCD_subunit_C, exonuclease SbcC. All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MKPLRLTLKNFGSYKGTHTIDFTALGPIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAA
PSEAAFAELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDY
KTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCT
PCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLE
ETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTL
HSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFR
DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKA
VVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS
LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDV
RLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA
QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV
TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEK
SATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLAN
QSEGRFHGRYADSHVNARKYQGLALLVADAYTGSVRPSATLSGGETFLASLSLALALADLLSTSGGTVLD
SLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRILVKKTNAGSHVM
>gnl|CDD|273178 TIGR00619, Nuclease_SbcCD_subunit_D, exonuclease SbcD. All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MRILHTSDWHLGKTLEGVSRLAEQKAFLDDLLEFAKAEQVDALLVAGDVFDTANPPAEAQELFNAFFVNL
SDTGIRPIVVISGNHDSAQRLSAAKKLLAELGVFVVGSPGHDPQILLLKDGTNGEGLCVGLFLLPREAIL
TRAGLDGFGLELLLAHTDVKLRQAAEALKLRLDQDLPKILLAHLFTAGATKSDAERRIYIGTLYAFPLQN
FPEADYIALGHIHIHKISKGRERVRYSGSPFPLSFDEAGKDKY
>gnl|CDD|273179 TIGR00621, Single-stranded_DNA-binding_protein, single stranded DNA-binding protein (ssb). All proteins in this family for which functions are known are single-stranded DNA binding proteins that function in many processes including transcription, repair, replication and recombination. Members encoded between genes for ribosomal proteins S6 and S18 should be annotated as primosomal protein N (PriB). Forms in gamma-protoeobacteria are much shorter and poorly recognized by this model. Additional members of this family include phage proteins. Eukaryotic members are organellar proteins [DNA metabolism, DNA replication, recombination, and repair]
MRMVNKVILVGRLTRDPELRYTPSGNAVANFTLATNRRWKDQDGEWKEETEWHDIVIFGRLAEVAAQYLK
KGSLVYVEGRLRTRKWEDQNGQKRSKTEIIADNVQLLDLLGARAQGGEFSGGGGSGNRPQGGQEQSATGK
DPAQSAPQSGSADPIDGDDDEIPF
>gnl|CDD|129709 TIGR00622, General_transcription_factor_IIH_subunit_2, transcription factor ssl1. All proteins in this family for which functions are known are components of the TFIIH complex which is involved in the initiaiton of transcription and nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
GYFCPQCRAKVCELPVECPICGLTLILSTHLARSYHHLFPLKAFQEIPLEEYNGSRFCFGCQGPFPKPPV
SPFDELKDSHRYVCAVCKNVFCVDCDVFVHESLHCCPGCIHK
>gnl|CDD|129710 TIGR00623, Cell_division_inhibitor_SulA, cell division inhibitor SulA. All proteins in this family for which the functions are known are cell division inhibitors. In E. coli, SulA is one of the SOS regulated genes [DNA metabolism, DNA replication, recombination, and repair]
YTSGYANRSSSFSYTTRNVARNTTENKAAGLISEVVYREDQPMMAQLLLLPLLQQLGQQSRWQLWLTPQQ
KLSKEWVQSSGLPLTKVMQISQLSPCNTVESMIRALRTGNYSVVIGWLTDELTEEEHAKLVRAAEEGNAM
GFIMRPVRAISPPHRQLSGLKIHSNLYH
>gnl|CDD|129711 TIGR00624, DNA-3-methyladenine_glycosylase_1, DNA-3-methyladenine glycosylase I. All proteins in this family are alkylation DNA glycosylases that function in base excision repair This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
VRCGWASVDPLYRAYHDNEWGVPLRDSVALFERMSLEGFQAGLSWITVLRKRENYRRAFSGFDIVKVARM
TDADVERLLQDDGIIRNRGKIEATIANARAALQLEQNDLSEFLWSFVNHQPQPRQRPTDSEIPSSTPESK
AMSKELKKRGFRFVGPTICYALMQATGMVDDHIQGCWVY
>gnl|CDD|273180 TIGR00625, General_transcription_factor_IIH_subunit_4, Transcription factor tfb2. All proteins in this family are part of the TFIIH complex which is involved in the initiation of transcription and nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
SLQEFLEGLPPGVLDRLYGHPATCLAVFRELPSLAKNWVMRMLFNEQPVPLADVDLWVKKEFKKAQEEST
GLLSGLHIWHTQLLPGLQGIILNPIFRQNLRIALTGGGKANSFGVSQLGPDKHAVDVDSLDKYAEERWET
ILHFMVGTPSAKVPSEDVLQLLKQAGLMKSTEPGEPPCITSAGFQFLLQDINAQLWTLLLQYLKTAESRG
MDLVEVLHFLFMLGFLTLGKAYSVDGLSDTQLIMLQDLREYGLVFQRKRKSRRFYPTRLAINLTSDTKTV
SGAGGTVDDDLGFIIVETNYRLYAYTESPLQIALIALFSELLARFPNMVVGQITRESIRRALANGITAQQ
IIHYLRTHAHPQMRKEQTPVLPPTIVDQIRLWELERDRLRFTEGVLYNDFLTQVDFELLLAYARELGVLV
WENSAKRLFFITPAGHSDVKRFWKRQKH
>gnl|CDD|273181 TIGR00627, protein_ZK1128.4_partially, transcription factor tfb4. All proteins in this family are part of the TFIIH complex which is involved in the initiation of transcription and nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
NPSLLVVIIEANPCSWGMLALAHGKRTISKVLRAIVVFLNAHLAFNANNKLAVIASHSQDNKYLYPSTRC
EDRNASELDPKRLRELLYRDFRTVDETIVEEIKPLMAHADKHMKKDSRTVLAGALSDALGYINRSEQSET
ASEKLKSRILVISITPDMALQYIPLMNCIFSAQKQNIPIDVVSIGGDFTSGFLQQAADITGGSYLHVKKP
QGLLQYLMTNMLPDPTLRAVLSKPNHNSVDYRASCFCHHQLVSIGFVCSVCLSVLCQYTPICKTCKTAF
>gnl|CDD|273182 TIGR00628, Uracil-DNA_glycosylase, uracil-DNA glycosylase. All proteins in this family for which functions are known are uracil-DNA glycosylases that function in base excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
SPSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHG
LAFSVKRGVPIPPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERF
TDAVISRLSERLDGLVFMLWGAHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHG
K
>gnl|CDD|273183 TIGR00629, UV_DNA_damage_endonuclease, UV damage endonuclease UvdE. All proteins in this family for which functions are known are UV dimer endonucleases that function in an alternative nucleotide excision repair process. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
PWIGRLGYACLNTSLRDAKPAKFLSRTCRSKLIKTERDGKEAVLTLGKANLRDTMKTLHWNIGHGIPFYR
FSSSIFPFASHPDVGYDLVTFAQKELREIGELAKTHQHRLTFHPGQFTQFTSPRESVVKSAIRDLAYHDE
MLSAMKLAEQLNKDAVIIIHIGGAFGNKDTTLARFHQNYKRLSQSIKERLVLENDDVTWTVEDLLPVCEE
LNIPFVLDFHHHNINPGPLREGDLDVALPLIPRIIKTWERKGIQQKVHYSEPKDEQAIRSHARRVHAPRV
ERFPPCGPNMDLMIEAKQKEQAVFELMRELSL
>gnl|CDD|273184 TIGR00630, UvrABC_system_protein_A, excinuclease ABC, A subunit. This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPD
VDSIEGLSPAISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILAL
PEGTRVILLAPIVRGRKGEFRKLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNE
NRSRLAESVETALRLGDGLLEVEFDDDEEVAESKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPE
CSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKSTTSYYRQMFASLAEHLGFDLDTPWKDLPEEAQKAIL
YGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLEKFMSERPCPSCGGTRLKPEA
LAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYLSLSRAAGTLS
GGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI
DIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVS
IPLGLFTCITGVSGSGKSTLINDTLYPALANRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSN
PATYTGVFDEIRELFAETPEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKR
YNRETLEVKYKGKNIADVLDMTVEEAYEFFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKL
AKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGD
GGGTVVASGTPEEVA
>gnl|CDD|273185 TIGR00631, UvrABC_system_protein_B, excinuclease ABC, B subunit. All proteins in this family for wich functions are known are DNA helicases that function in the nucleotide excision repair and are endonucleases that make the 3' incision next to DNA damage. They are part of a pathway requiring UvrA, UvrB, UvrC, and UvrD homologs. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
LFKLHSPFQPAGDQPKAIAKLVEGLTDGEKHQTLLGVTGSGKTFTMANVIAQVNRPTLVIAHNKTLAAQL
YNEFKEFFPENAVEYFVSYYDYYQPEAYVPSKDTYIEKDASINDEIERLRHSATRSLLERRDVIVVASVS
CIYGLGSPEEYLKMVLHLEVGKEIDRRELLRRLVELQYERNDVDFQRGTFRVRGDVVEIFPAYEDEFAVR
IEFFGDEIERISRVDPLTGEVLRELDSFTIFPASHYVTPEERLERAIKNIEKELEERLKYFEEQGKLLEA
QRLKQRTEYDLEMLREMGYCSGIENYSRHLSGRAPGEPPYTLLDYFPDDFLLVIDESHVTLPQIGGMYNG
DRSRKQTLVEYGFRLPSALDNRPLKFEEFEERINQVVYVSATPGPYELEQSGNVVEQIIRPTGLLDPEIE
VRPTDGQVDDLLSEIRQRVARNERVLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLERVEIIRDLRL
GEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVIMYADKITDSMQKA
IEETERRRKIQMAYNEEHGITPQTIRKPIRDILDIELKEKEDAAKKKKKGEDLSDLSKKELKKLIKQLEK
EMKQAARNLEFEEAARLRDEILELK
>gnl|CDD|211591 TIGR00632, HpaII_very_short_patch_repair_endonuclease, DNA mismatch endonuclease Vsr. All proteins in this family for which functions are known are G:T mismatch endonucleases that function in a specialized mismatch repair process used usually to repair G:T mismatches in specific sections of the genome. This family was based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Members of this family typically are found near to a DNA cytosine methyltransferase [DNA metabolism, DNA replication, recombination, and repair]
ADKLSPATRSKNMQAIRTKGTKPEKALASLLTGLGLRFRLQDASLPGTPDIVFDEYRCVIFIHGCFWHGH
HCYLGKVPKTRTDFWSPKIEKNVERDRRVNSRLQELGWRVLRVWECE
>gnl|CDD|273186 TIGR00633, DNA-apurinic_or_apyrimidinic_site_lyase, exodeoxyribonuclease III (xth). All proteins in this family for which functions are known are 5' AP endonucleases that funciton in base excision repair and the repair of abasic sites in DNA.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MKIISWNVNGLRARLHKLFLDWLKEEQPDVLCLQETKVADEQFPAELFEELGYHVFFHGAKKGYSGVAIL
SKVEPLDVRYGFGGEPHDEEGRVITAEFDGFTVVNVYVPNGGSRDLERLEYKLQFWDALFQYLEKELDAG
KPVVICGDMNVAHTEIDLGNPKENKGNAGFTPEEREWFDELLEAGFVDTFRHFNPDTGDAYTWWDYRSGA
RDRNRGWRIDYFLVSEPLAERVVDSYIDSEIRGSDHCPIVLELD
>gnl|CDD|273187 TIGR00634, DNA_repair_protein_RecN, DNA repair protein RecN. All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair [DNA metabolism, DNA replication, recombination, and repair]
MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTT
ESLDDADYPALQAIELEEEDEDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLL
FRPDEQRQLLDTFAGANEKVKAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGE
DEALEAEQQRLSNLEKLRELSQNALAALRGDVDVQEGSLLEGLGEAQLALASVIDGSLRELAEQVGNALT
EVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKRKYGASVEEVLEYAEKIKEELDQLDDSDESLEA
LEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEFTVEIKTSLPSGAKARAGAYGAD
QVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGETAQAIAKKLAQL
SERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELARMLAGLEKSDLTLAHAQEL
LEA
>gnl|CDD|129721 TIGR00635, Holliday_junction_ATP-dependent_DNA_helicase_RuvB, Holliday junction DNA helicase, RuvB subunit. All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions [DNA metabolism, DNA replication, recombination, and repair]
KLLAEFIGQEKVKEQLQLFIEAAKMRQEALDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKPG
DLAAILTNLEEGDVLFIDEIHRLSPAVEELLYPAMEDFRLDIVIGKGPSARSVRLDLPPFTLVGATTRAG
MLTSPLRDRFGIILRLEFYTVEELAEIVSRSAGLLNVEIEPEAALEIARRSRGTPRIANRLLRRVRDFAQ
VRGQKIINRDIALKALEMLMIDELGLDEIDRKLLSVLIEQFQGGPVGLKTLAAALGEDADTIEDVYEPYL
LQIGFLQRTPRGRIATELAYEHLGL
>gnl|CDD|213544 TIGR00636, PduO_Nterm, ATP:cob(I)alamin adenosyltransferase. This model represents as ATP:cob(I)alamin adenosyltransferase family corresponding to the N-terminal half of Salmonella PduO, a 1,2-propanediol utilization protein that probably is bifunctional. PduO represents one of at least three families of ATP:corrinoid adenosyltransferase: others are CobA (which partially complements PduO) and EutT. It was not clear originally whether ATP:cob(I)alamin adenosyltransferase activity resides in the N-terminal region of PduO, modeled here, but this has now become clear from the characterization of MeaD from Methylobacterium extorquens [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
YTKTGDKGQTKLAGGDRVGKDSPRVEAYGTLDELNSFIGVALSLLKWEDLKEDLERIQNDLFDIGGDLAT
PGDTKKITEEDVKWLEERIDQYRKELPPLKLFVLPGGTPAAAFLHVARTVARRAERRVVALLKEEEINEV
VLVYLNRLSDLLFVLARVVNKRSGVPEVIWE
>gnl|CDD|273188 TIGR00637, Molybdenum-pterin-binding_protein_MopA, ModE molybdate transport repressor domain. ModE is a molybdate-activated repressor of the molybdate transport operon in E. coli. It consists of the domain represented by this model and two tandem copies of mop-like domain, where Mop proteins are a family of 68-residue molybdenum-pterin binding proteins of Clostridium pasteurianum. This model also represents the full length of a pair of archaeal proteins that lack Mop-like domains. PSI-BLAST analysis shows similarity to helix-turn-helix regulatory proteins [Regulatory functions, Other]
FADPRRVALLKAIARMGSISQAAKDAGISYKSAWDYIRAMNNLSGEPLVERATGGKGGGGAVLTEYGQRL
IQLYDLLERILEKAFSVLEDEVVVKPLKA
>gnl|CDD|273189 TIGR00638, Probable_molybdenum-pterin-binding_protein, molybdenum-pterin binding domain. This model describes a multigene family of molybdenum-pterin binding proteins of about 70 amino acids in Clostridium pasteurianum, as a tandemly-repeated domain C-terminal to an unrelated domain in ModE, a molybdate transport gene repressor of E. coli, and in single or tandemly paired domains in several related proteins [Transport and binding proteins, Anions]
LQTSARNQLKGKVVAIEDGDVNAEVDLLLGGGTKLTAVITLESVAELGLKPGKEVYAVIKAPWVILAVD
>gnl|CDD|161973 TIGR00639, Phosphoribosylglycinamide_formyltransferase, phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent. This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQA
IIEELRAHEVDLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVD
EEVDTGPIIAQAKVPILPEDTEETLEQRIHKQEHRIYPLAIAWFAQGRLK
>gnl|CDD|129726 TIGR00640, Methylmalonyl-CoA_mutase_mitochondrial, methylmalonyl-CoA mutase C-terminal domain. Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a reversible isomerization between L-methylmalonyl-CoA and succinyl-CoA. The enzyme uses an adenosylcobalamin cofactor. It may be a homodimer, as in mitochondrion, or a heterodimer with partially homologous beta chain that does not bind the adenosylcobalamin cofactor, as in Propionibacterium freudenreichii. The most similar archaeal sequences are separate chains, such as AF2215 and AF2219 of Archaeoglobus fulgidus, that correspond roughly to the first 500 and last 130 residues, respectively of known methylmalonyl-CoA mutases. This model describes the C-terminal domain subfamily. In a neighbor-joining tree (methylaspartate mutase S chain as the outgroup), AF2219 branches with a coenzyme B12-dependent enzyme known not to be 5.4.99.2
RRPRILVAKMGQDGHDRGAKVIATALADLGFDVDYGPLFQTPEEIARQAVEADVHVVGVSSLAGGHLTLV
PELIKELNKLGRPDILVVVGGVIPPQDYEELKEMGVAEVFGPGTPIPEIAIFVLKDIEKLLD
>gnl|CDD|273190 TIGR00641, Methylmalonyl-CoA_mutase_mitochondrial, methylmalonyl-CoA mutase N-terminal domain. Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a reversible isomerization between L-methylmalonyl-CoA and succinyl-CoA. The enzyme uses an adenosylcobalamin cofactor. It may be a homodimer, as in mitochondrion, or a heterodimer with partially homologous beta chain that does not bind the adenosylcobalamin cofactor, as in Propionibacterium freudenreichii. The most similar archaeal sequences are separate chains, such as AF2215 abd AF2219 of Archaeoglobus fulgidus, that correspond roughly to the first 500 and last 130 residues, respectively of known methylmalonyl-CoA mutases. This model describes the N-terminal domain subfamily. In a neighbor-joining tree, AF2215 branches with a bacterial isobutyryl-CoA mutase, which is also the same length. Scoring between the noise and trusted cutoffs are the non-catalytic, partially homologous beta chains from certain heterodimeric examples of 5.4.99.2
WHTAEGIPVKPLYTPALADWDYMEKLGTFPGEPPFTRGPYATMYRFRPWTIRQYAGFSTAEESNKFYRRN
LAAGQKGLSVAFDLPTHRGYDSDNPRVAGDVGMAGVAIDSIEDMRILFDGIPLDKVSVSMTMNGAVLPIL
ALYVVVAEEQGVPPEKLTGTIQNDILKEFMVRNTYIFPPEPSMRIIADIIAYTAKNMPKWNSISISGYHM
QEAGATAVQELAFTLADGIEYIRAGLSAGLDVDSFAPRLSFFFGIGMNFFMEIAKLRAARRLWAKLVKEW
FGAKNPKSMSLRTHCQTSGWSLTAQDPYNNIVRTAIEALAAVLGGTQSLHTNSFDEALGLPTDFSARIAR
NTQQIIQEESGVTRVIDPLGGSYYVEWLTDDIYERAWKYIQEIEEMGGMAKAIERGIPKLRIEEAAARTQ
ARIDSGRQVIVGVNKYQLEEEDEVEVLKVDNSSVREEQIAKLKKLRAERDQEKVEAALDALTKAAEKEDE
NLLALAIDAARARATLGEITDALEKVFGEYRAPIRT
>gnl|CDD|273191 TIGR00642, mmCoA_mut_beta, methylmalonyl-CoA mutase, heterodimeric type, beta chain. The adenosylcobalamin-binding, catalytic chain of methylmalonyl-CoA mutase may form homodimers, as in mitochondrion and E. coli, or heterodimers with a shorter, homologous chain that does not bind adenosylcobalamin. This model describes this non-catalytic beta chain, as found in the enzyme from Propionibacterium freudenreichii, for which the 3-dimensional structure has been solved [Central intermediary metabolism, Other]
LSLAGDFPKATREQWEREVEKVLNRGRPPEKQLTGAECEKRLTVHTVDGFDIVPMYRPKDAPKKLGLPGV
APFVRGTTVRNGDHDAWDVRALHVEDPDEAFTNKAILEGLERGVTSLLLRVDPDAIAPDHLDALLSDVLL
EMTKVEVFSRYDQGAAAEALVSVYERSDGKPAKDLALNLGLDPIKFALLQGVTEPDLTVLGDWVRRAAKF
SPDSRAVTVDANIYHNAGAGDVAELAWALATGAEYLRALTEQGFTATEAFDTINFRVTATHDQFMTIAKL
RALRELWARIGEVFGDDEDKRGARQHAITSWRNKTREDPYVNILRGSIATFSASVGGADSITVLPFDVAL
GLPEDDFPLRIARNTQLLLAEEVHIGRVNDPAGGSYYVESLTRSLADAAWKEFQEVEKLGGFSKAVMTEH
VTKVLDACNAERAKRLANRRQPITGVNEFPNIGARSIETEPFPAAPARKGLAWHRRSAVEFEALRDRSTS
VGERPKVFLLCLGTLADFGGREGFSSNVWHIAGIDTIQVEGGTTAEIVVEAFKKAGAQVAVLCSSDKVYA
QQGLEVAKALKAAGAKALYLAGAFKEFGDDAAEAIDGRLFMKMNVVDTLSSTLDILGVA
>gnl|CDD|273192 TIGR00643, ATP-dependent_DNA_helicase_RecG, ATP-dependent DNA helicase RecG [DNA metabolism, DNA replication, recombination, and repair]
LGIHTVQDLLFYFPRRYEDRTLLQTIGELLPGERATIVGEVLSHCIFGFKRRKVLKLRLKDGGYKKLELR
FFNRAFLKKKFKVGSKVVVYGKVKSSKFKAYLIHPEFISEKDGVEFELKILPVYPLTEGLTQKKLRKLIQ
QALDQLDKSLEDPLPEELREKYGLLSLEDALRAIHFPKTLSLLELARRRLIFDEFFYLQLAMLARRLGEK
QQFSAPPANPSEELLTKFLASLPFKLTRAQKRVVKEILQDLKSDVPMNRLLQGDVGSGKTLVAALAMLAA
IEAGYQVALMAPTEILAEQHYNSLRNLLAPLGIEVALLTGSLKGKRRKELLETIASGQIHLVVGTHALIQ
EKVEFKRLALVIIDEQHRFGVEQRKKLREKGQGGFTPHVLVMSATPIPRTLALTVYGDLDTSIIDELPPG
RKPITTVLIKHDEKDIVYEFIEEEIAKGRQAYVVYPLIEESEKLDLKAAEALYERLKKAFPKYNVGLLHG
RMKSDEKEAVMEEFREGEVDILVATTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCL
LVYKNPKSESAKKRLRVMADTLDGFVIAEEDLELRGPGDLLGTKQSGYPEFRVADLVRDREILVEAREDA
>gnl|CDD|273193 TIGR00644, recJ, single-stranded-DNA-specific exonuclease RecJ. All proteins in this family are 5'-3' single-strand DNA exonucleases. These proteins are used in some aspects of mismatch repair, recombination, and recombinational repair [DNA metabolism, DNA replication, recombination, and repair]
LGPILAQILASRGITDAEELENFLNPKLKDLPPPFLLLDMEKAVERLIEAVENNEKILIYGDYDVDGITS
TAILVEFLELLGVKVDYYIPNRFTEGYGPNPEAFRKLHEDGVSLIITVDNGITAHEEIKYAKELGLDVIV
TDHHLVPEDLPEAAAIVNPNRPDCNYPQKELAGVGVAFKLVQALYEELRKPKPDLEEFLDLVALGTIADV
VPLTGENRALVKKGLKVLRKQKRPGLKALLEVAGVDKDKLSSTDIGFIIGPRINAAGRLGDASLGVELLL
TDDPKEARELAEELDSLNQERKDIEQTVLEEALAIAEAEETNDSVIVVAKENWHEGVLGIVASRLAEEYN
KPVLVFAIDEGKGIAKGSGRSISGIDLYDALSEARESLFLKFGGHAMAAGLSLKRENLEEFREKLNELFS
KSLEKDESEPILEVDGELPPSDIDFELIRQLESLEPFGQGNPEPLFVLKDLRVEDIKLLGGNHLKLSLKS
GEKNIEAIAFNAGEQLLELNGGEPIDVAGKLKINEWNGNKTPQLIIKDI
>gnl|CDD|129731 TIGR00645, Hypothetical_UPF0114_protein_yqhA., TIGR00645 family protein. This conserved hypothetical protein with four predicted transmembrane regions is found in E. coli, Haemophilus influenzae, and Helicobacter pylori, among completed genomes. A similar protein from Aquifex aeolicus appears to share a central region of homology and a similar overall arrangement of hydrophobic stretches, and forms a bidirectional best hit with several members of the seed alignment. However, it is uncertain whether the observed similarity represents full-length homology and/or equivalent function, and so it is excluded from the seed and scores below the trusted cutoff [Hypothetical proteins, Conserved]
QENIIEKIIFASRWLLAPIYLGLSLTLVILSYKFIKELWHLLINVNDMDENDLMLGVLNLVDVVMIAGLL
VMVTIGGYEIFVSKLDTRNHPEQPEWLSHVDATVLKVKVSMSIVAISSIHLLQTFMNASNMPENTMMWQV
LIHLGFVVSAIALAYTDKILYSSNKTH
>gnl|CDD|129732 TIGR00646, Uncharacterized_protein_MG010_homolog, DNA primase-related protein. The DNA primase DnaG of E. coli and its apparent orthologs in other eubacterial species are approximately 600 residues in length. Within this set, a conspicuous outlier in percent identity, as seen in a UPGMA difference tree, is the branch containing the Mycoplasmas. This lineage is also unique in containing the small, DNA primase-related protein modelled here, which is homologous to the central third of DNA primase. Several small regions of sequence similarity specifically to Mycoplasma sequences rather than to all DnaG homologs suggests that the divergence of this protein from DnaG post-dated the separation of bacterial lineages. The function of this DNA primase-related protein is unknown [Unknown function, General]
MDLRNEKLEELFFIYHKNLKNQSKSKYRCAMNYLKKRGFNLQDFLKVGGGLAYLGEKEWLNLPLYNFDGN
LIGFLNRKVGFEKEFLYLPFNKPPSKSEAFLGLKELPIEDNSIYLVEGDFDWLAFRKAGILNCLPLCGLT
ISDKQMKFFKQKKIEKIFICFDNDFAGKNAAANLEEILKKAGFITKVIEIKAAAKDWNDLFLLNNKNWAA
ALRDHLAF
>gnl|CDD|273194 TIGR00647, DNA_bind_WhiA, DNA-binding protein WhiA. This family describes a DNA-binding protein widely conserved in Gram-positive bacteria, and occasionally occurring elsewhere, such as in Thermotoga. It is associated with cell division, and in sporulating organisms with sporulation [Cellular processes, Cell division]
TSEVKKELTQLEVIKKECRWAELSALLRMNGLLLLSNGQLSFKVQTENAAIARRLYTLIKDLYGINVELL
VRKKMKLKKNNRYIVRVFEAVQELLRQLGLLDDRGGLVRGLDEDVVSSEECDKKAYLRGAFLAGGSVSDP
ESSSYHLEISSPYEEHAEALVKLANRFGLNAKVTERRNGDIVYLKEAEKIGDFLTIIGAHDALLAFEEVR
IVREMRNSVNRLVNCETANLRKTARAAVAQAERIKLIIKILGLDDLPDNLQEAAQLRLDHPDASLEELGE
LADPGPITKSGVNHRLRKLLKIAD
>gnl|CDD|129734 TIGR00648, Holliday_junction_resolvase_RecU, recombination protein U. The Bacillus protein has been shown to be required for DNA recombination and repair. RJD 11/20/00 [DNA metabolism, DNA replication, recombination, and repair]
NRGMLLETDVNQTNARYLDHPIAVIHKKPTPVQIVNVRYPKRSGAVINEAYFRQKSTTDYNGIYKGMYID
FEAKETKNKTSFPLANIHDHQLEHMKRIDQQGGISFLLIYFQTKDQVYALHTKKLLEFWKRQESNIKKSI
KRDEIEQKSYKIPLLYPPRIDYISIIQSL
>gnl|CDD|273195 TIGR00649, Ribonuclease_J, beta-CASP ribonuclease, RNase J family. This family of metalloenzymes includes RNase J1 and RNase J2, involved in mRNA degradation in a wide range of organism [Transcription, Degradation of RNA]
IKIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHED
HIGAVPYLLHQVGFFPIYGTPLTIALIKSKIKEHGLNVRTDLLEIHEGEPVEFGENTAIEFFRITHSIPD
SVGFALHTPLGYIVYTGDFKFDNTPVIGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQL
NDIFKNADGRIIVATFASNIHRVQQLIQIARKNGRKVAVYGRSMESLIGIARRLGYIKCPHNNFISLKEI
NNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRPGDTVVFSAPPIPGNENIAVSITLDIRLNRAGA
RVIKGIHVSGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKLAEEEGYPGENIFILRNGEVLEINGD
EI
>gnl|CDD|273196 TIGR00651, Phosphate_acetyltransferase, phosphate acetyltransferase. Alternate name: phosphotransacetylase Model contains a gene from E.coli coding for ethanolamine utilization protein (euti) and also contains similarity to malate oxidoreductases [Central intermediary metabolism, Other, Energy metabolism, Fermentation]
IVFPEGWEPRVLKAAALLAERGIATPVVLGNPEEIQPKAAGCNLDLGHVVIIDPDVSPDRESYAERYVEL
RKHKGMTEAQARKQLRDESYFATMMVALGEADGLVSGAVHTTADTLRPALQIIKTLPGVKIVSSVFIMDL
GEEVLVFADCAVNPDPNAEQLAEIAIQSANSAKSFGEIEPKVALLSYSTKGSGKGEEVEKVREATRIAKE
KRPDLTIDGELQFDAAFVEKVAEKKAPNSPVAGSANVFVFPDLDAGNIGYKIVQRLGDAEAIGPILQGLN
KPVNDLSRGCSVEDIVNTGAITA
>gnl|CDD|273197 TIGR00652, Diaminopimelate_epimerase, diaminopimelate epimerase [Amino acid biosynthesis, Aspartate family]
MRFTKMHGLGNDFVLVDSFDAELVKEPELARQVCDRHTGIGADGLLFVEPGSPEADYKMRIFNSDGSEAE
MCGNGIRCFAKFVYEHGGKKKDIRVETLAGLIVLEVKEENKVKVDMGEPDFKPAEIPLTVWGFEEPEVLL
FGEVLAVDTGNPHLVVFVDDVETLNLTILGPLLEYHERFPEGVNVNFVQVKGDDTIRLRTYERGEGETLA
CGTGACASAAAALLLGGTNKKVTVHLPGGNLEIEWKEDGTVYMTGPAVRVFRGVLFL
>gnl|CDD|273198 TIGR00653, Glutamine_synthetase, glutamine synthetase, type I. Alternate name: glutamate--ammonia ligase. This model represents the dodecameric form, which can be subdivided into 1-alpha and 1-beta forms. The phylogeny of the 1-alpha and 1-beta forms appears polyphyletic. E. coli, Synechocystis PCC6803, Aquifex aeolicus, and the crenarcheon Sulfolobus acidocaldarius have form 1-beta, while Bacillus subtilis, Thermotoga maritima, and various euryarchaea has form 1-alpha. The 1-beta dodecamer from the crenarcheon Sulfolobus acidocaldarius differs from that in E. coli in that it is not regulated by adenylylation [Amino acid biosynthesis, Glutamate family]
EEVFKLIKEENVKFVDLRFTDIKGKPQHVEIPASALDKEAFEEGIMFDGSSIRGFQGIEESDMLLKPDPS
TAVIDPWRAEKTLRVICDVYEPFTGEPYERDPRSIAKRAEEYLKSGIGDTAYFGPEPEFFLFDSVEFGSL
ANGSFYEVDSEEGRWNEESGNRGYKPRDKGGYFPVAPTDTAVDIRREMVLYLEQLGFDVEVHHHEVATGQ
HEIDFKFDTLLKTADDIQTYKYVVKNVARKHGKTATFMPKPLFGDNGSGMHCHQSLWKDGENLFAGEEYA
GLSETALYYIGGILKHAKALAAFTNPTVNSYKRLVPGYEAPVYLAYSARNRSALIRIPASGNPKAKRIEF
RFPDPSANPYLAFAAMLMAGLDGIKNKIDPGEPVDKNLYELSPEELREKGIPQLPGSLEEALDELESDHL
VEGGVFGEEFIEAFIELKRKEWDPYRLRPHPWEFELYYD
>gnl|CDD|129739 TIGR00654, Uncharacterized_isomerase_YddE, phenazine biosynthesis protein PhzF family. Members of this family show a distant global similarity to diaminopimelate epimerases, which can be taken as the outgroup. One member of this family has been shown to act as an enzyme in the biosynthesis of the antibiotic phenazine in Pseudomonas aureofaciens. The function in other species is unclear [Cellular processes, Toxin production and resistance]
LMVPFYQVDVFTSQPFMGNPAAVVNFAEILSEEEMQAIANETNYSETTFLLKPSSEKYDYRLRIFTPRSE
LPFAGHPTIGSCYALLEFTKLTTATTLVQECKAGAVPVTINEKNGDLRISLEQPMPDFEPISGEMRADLA
KALGLTEDDFIKGLPIQLLSTGPEWIVIPLKDEEACFNASPNFAMLAHQLKQNDHVGVIPFGPKKEAAGK
NDYHGRMFAPVIGIYEDPVTGSGSGALGAYLQHVYKNEKTHDITIEQGGALGRDGLMEATVKKEGDNSTK
VYIAGTAVTVIDGKIKI
>gnl|CDD|273199 TIGR00655, Formyltetrahydrofolate_deformylase, formyltetrahydrofolate deformylase. This model describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
GILLVSCPDQKGLVAAISTFIAKHGANIISNDQHTDPETGRFFMRVEFQLEGFRLEESSLLAAFKSALAE
KFEMTWELILADKLKRVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSLVERFGIPFHYIPA
TKDNRVEHEKRQLELLKQYQVDLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGV
KIIGATAHYVTEELDEGPIIEQDVVRVDHTDNVEDLIRAGRDIEKVVLARAVKLHLEDRVFVYENKTVVF
>gnl|CDD|273200 TIGR00656, Lysine-sensitive_aspartokinase_3, aspartate kinase, monofunctional class. This model describes a subclass of aspartate kinases. These are mostly Lys-sensitive and not fused to homoserine dehydrogenase, unlike some Thr-sensitive and Met-sensitive forms. Homoserine dehydrogenase is part of Thr and Met but not Lys biosynthetic pathways. Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. In E. coli, a distinct isozyme is inhibited by each of the three amino acid products. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenases and form homotetramers, while the Lys-sensitive form (III) is a monofunctional homodimer. The Lys-sensitive enzyme of Bacillus subtilis resembles the E. coli form but is an alpha 2/beta 2 heterotetramer, where the beta subunit is translated from an in-phase alternative initiator at Met-246. The protein slr0657 from Synechocystis PCC6803 is extended by a duplication of the C-terminal region corresponding to the beta chain. Incorporation of a second copy of the C-terminal domain may be quite common in this subgroup of aspartokinases [Amino acid biosynthesis, Aspartate family]
ELIVQKFGGTSVGSGERIKNAARIVLKEKMKGHKVVVVVSAMGGVTDELVSLAEEAISDEISPRERDELV
SHGELLSSALFSSALRELGVKAIWLDGGEAGIRTDDNFGNAKIDIIATEERLLPLLEEGIIVVVAGFQGA
TEKGDTTTLGRGGSDYTAALLAAALKADRVDIYTDVPGVYTTDPRVVEAAKRIDKISYEEALELATFGAK
VLHPRTVEPAMRSKVPIEVRSSFDPSEGTLITNSMENPPLVKGIALRKNVTRVTVHGLGMLGKRGFLAEI
FGALAERNINVDLISQTPSETSISLTVDTTDADEAVRALKDQSGAAELDRVEVEEGLAKVSIVGAGMVGA
PGVASEIFSALEKKNINILMISSSETNISFLVDENDAEKAVRKLHEVFEE
>gnl|CDD|273201 TIGR00657, Aspartokinase_Aspartate_kinase, aspartate kinase. Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. In E. coli, a distinct isozyme is inhibited by each of the three amino acid products. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenases and form homotetramers, while the Lys-sensitive form (III) is a monofunctional homodimer.The Lys-sensitive enzyme of Bacillus subtilis resembles the E. coli form but is an alpha 2/beta 2 heterotetramer, where the beta subunit is translated from an in-phase alternative initiator at Met-246. This may be a feature of a number of closely related forms, including a paralog from B. subtilis [Amino acid biosynthesis, Aspartate family]
ALIVQKFGGTSVGNAERIRRVAKIVLKEKKKGNQVVVVVSAMAGVTDALVELAEQASPGPSKDFLEKIRE
KHIEILERLIPQAIAEELKRLLDAELVLEEKPREMDRILSFGERLSAALLSAALEELGVKAVSLLGGEAG
ILTDSNFGRARVIIEILTERLEPLLEEGIIPVVAGFQGATEKGETTTLGRGGSDYTAALLAAALKADECE
IYTDVDGIYTTDPRIVPDARRIDEISYEEMLELASFGAKVLHPRTLEPAMRAKIPIVVKSTFNPEAPGTL
IVASTKEMEEPIVKGLSLDRNQARVTVSGLGMKGPGFLARVFGALAEAGINVDLISQSSSETSISFTVDK
EDADQAKELLKSELNLSALSRVEVEKGLAKVSLVGAGMKSAPGVASKIFEALAQNGINIEMISSSEINIS
FVVDEKDAEKAVRLLHNALFE
>gnl|CDD|129743 TIGR00658, Ornithine_carbamoyltransferase, ornithine carbamoyltransferase. This family of ornithine carbamoyltransferases (OTCase) is in a superfamily with the related enzyme aspartate carbamoyltransferase. Most known examples are anabolic, playing a role in arginine biosynthesis, but some are catabolic. Most OTCases are homotrimers, but the homotrimers are organized into dodecamers built from four trimers in at least two species; the catabolic OTCase of Pseudomonas aeruginosa is allosterically regulated, while OTCase of the extreme thermophile Pyrococcus furiosus shows both allostery and thermophily [Amino acid biosynthesis, Glutamate family]
RHLLSLLDLSPEEIRYLLQLAKKLKKGKKKGKEHKKLKGKTLALIFEKPSTRTRVSFEVAAYQLGGHPLY
LNPNDLQLGRGESIKDTARVLSRYVDGIMARVYKHEDVEELAKYASVPVINGLTDLFHPCQALADLLTII
EHFGKLKGVKVVYVGDGNNVCNSLMLAGAKLGMDVVVATPEGYEPDADIVKKAQEIAKENGGSVELTHDP
VEAVKGADVIYTDVWVSMGEEDKKEERLKLFRPYQVNEELMELAKPEVIFMHCLPAHRGEEVTDEVIEGP
HSIVFDQAENRLHAQKAVMVALLG
>gnl|CDD|273202 TIGR00659, Uncharacterized_protein_HI_1298, TIGR00659 family protein. Members of this small but broadly distibuted (Gram-positive, Gram-negative, and Archaeal) family appear to have multiple transmembrane segments. The function is unknown. A homolog, LrgB of Staphylococcus aureus, in the same small superfamily but in an outgroup to this subfamily, is regulated by LytSR and is suggested to act as a murein hydrolase. Of the three paralogous proteins in B. subtilis, one is a full length member of this family, one lacks the C-terminal 60 residues and has an additional 128 N-terminal residues but branches within the family in a phylogenetic tree, and one is closely related to LrgB and part of the outgroup [Hypothetical proteins, Conserved]
MKTIGAFITLTLYAFFSALYLYSRKKNPFLNPVLLSILTIGVILKAFGISYDSYMEGARVINFLLGPAVV
ALAIPLYEQLKQIKEYWKEITIGIIIGSVTAMFSGTILALLAGHAPEILASFLPKSVTTPIAMGVSEKIG
GIPALTAVLVILTGILGNAFGPELLDLFKVKDRVARGLGTGVSSHALGTARCIEEDELAGAVSSLGLVLC
GIITSFIAPFLFEVIV
>gnl|CDD|273203 TIGR00661, conserved_hypothetical_protein, conserved hypothetical protein. This model represents nearly the full length of MJ1255 from Methanococcus jannaschii and of an unpublished protein from Vibrio cholerae, as well as the C-terminal half of a protein from Methanobacterium thermoautotrophicum. A small region (~50 amino acids) within the domain appears related to a family of sugar transferases [Hypothetical proteins, Conserved]
KILYSVCGEGFGHTTRSVAIGEALKNDYEVSYIASGRSKNYISKYGFKVFETFPGIKLKGEDGKVNIVKT
LRNKEYSPKKAIRREINIIREYNPDLIISDFEYSTVVAAKLLKIPVICISNQNYTRYPLKTDLIVYPTMA
ALRIFNERCERFIVPDYPFPYTICPKIIKNMEGPLIRYDVDDVDNYGEDYILVYIGFEYRYKILELLGKI
ANVKFVCYSYEVAKNSYNENVEIRRITTDNFKELIKNAELVITHGGFSLISEALSLGKPLIVIPDLGQFE
QGNNAVKLEDLGCGIALEYKELRLLEAILDIRNMKRYKRND
>gnl|CDD|273204 TIGR00663, DNA_polymerase_III_subunit_beta, DNA polymerase III, beta subunit. All proteins in this family for which functions are known are components of the DNA polymerase III complex (beta subunit). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
MKFTIQKDDLLKELSKVQRVLSNRPTIPILSNILLEVSDDKLTITGTDLDISIESQIPIVTIEQPGSVTI
NAKKFLDIVRALPDSKIELEVKNDKLAITSGKSRFKLPTLDADEYPNLPQIEEGVSIEIPSDVLKEAINQ
TAFAASTDETRPVLNGVNIKQEGKELLLVATDGHRLAVRKAKSEISDEEDFSVIIPGKALNELLKLLSDN
GELVLISLVDTQVYFELKNYKFTSRLIDGNYPDYKSVIPKEQKTSITVNRKELKEAIKRVSLLADEKRNL
VLTLSEKGEKLKESSDTQEIGKAEEEIEADYDGEDLVIAFNPKYLLDALKALKSEEIRIQFNDPSKPFLI
RPENDETIVYLIMPVRL
>gnl|CDD|273205 TIGR00664, DNA_polymerase_III_subunit_psi, DNA polymerase III, psi subunit. This small subunit of the DNA polymerase III holoenzyme in E. coli and related species appearsto have a narrow taxonomic distribution. It is not found so far outside the gamma subdivision proteobacteria [DNA metabolism, DNA replication, recombination, and repair]
TSRRDWQLQQLGITQWSLRRPGALQGEIAIAIPAHVRLVMVANDLPALTDPLVSDVLRALTVSPDQVLQL
TPEKIAMLPQGSHCNSWRLGTDEPLSLEGAQVASPALTDLRANPTARAALWQQI
>gnl|CDD|273206 TIGR00665, DnaB, replicative DNA helicase. This model describes the helicase DnaB, a homohexameric protein required for DNA replication. The homohexamer can form a ring around a single strand of DNA near a replication fork. An intein of _ 400 residues is found at a conserved location in DnaB of Synechocystis PCC6803, Rhodothermus marinus (both experimentally confirmed), and Mycobacterium tuberculosis. The intein removes itself by a self-splicing reaction. The seed alignment contains inteins so that the model built from the seed alignment will model a low cost at common intein insertion sites [DNA metabolism, DNA replication, recombination, and repair]
PPHNIEAEQAVLGAILLDNEAIDDVAEILKPEDFYRPAHRLIFQAILDLYEKGEPIDLVTVAEELEKDGE
LEEVGGLAYLAELASNVPSAANIEYYAEIVKEKAILRRLIQAGTEIVELAYDPTGDVEELLDEAEQKIFE
IAESRTSKGFKSIKEILKEAVEEIEELYERKGGITGVPTGFTDLDKLTSGLQPSDLIILAARPSMGKTAF
ALNIAENAAIKEGKPVAFFSLEMSAEQLVMRMLSSESRVDSQKLRTGRLSDEDWEKLTEAAGELSEAPLY
IDDTPGLTITELRAKARRLKREHGLGLIVIDYLQLMSGSGRSENRQQEVSEISRSLKALAKELNVPVIAL
SQLSRSVEQREDKRPQLSDLRESGSIEQDADIVMFLYRDEYYNPDSEDKGIAEIIIAKQRNGPTGTVKLA
FLGEYTRFENLA
>gnl|CDD|200042 TIGR00666, D-alanyl-D-alanine_carboxypeptidase_DacB, D-alanyl-D-alanine carboxypeptidase, serine-type, PBP4 family. In E. coli, this protein is known as penicillin binding protein 4 (dacB). A signal sequence is cleaved from a precursor form. The protein is described as periplasmic in E. coli (Gram-negative) and extracellular in Actinomadura R39 (Gram-positive). Unlike some other proteins with similar activity, it does not form transpeptidation. It is not essential for viability. This family is related to class A beta-lactamases [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
TSQPLYDYHGDTFMLPASTQKVITAAAALLQLGPNFRFTTTVETKGNVENGNLKGNLVLRFGGDPTLKRQ
DIRNMVATLKKSGVTQIDGNVLVDTSAFSSHDRAPGWPWNDLTQCFSAPPAAAIIDANCPQPLTFAVQRP
ASYALDLLQQLLKQQGISVAGVILASEPPQAGQVLASHQSAPLHDLLKIMMKKSDNMIAETLFREIGHAF
NRPGSWQAGVDAVRSILQQAGVDTGNTILADGSGLSRHNLVAPATLMQVLQYIAQQSNELNYLSSLPVAG
YDGTLGERAGLHDTPLVGKVRAKTGSLTGVYSLAGFITTASGQKLAFVQYLNG
>gnl|CDD|273207 TIGR00667, aat, leucyl/phenylalanyl-tRNA--protein transferase. The N-terminal residue controls the biological half-life of many proteins via the N-end rule pathway. This enzyme transfers a Leu or Phe to the amino end of certain proteins to enable degradation [Protein fate, Degradation of proteins, peptides, and glycopeptides]
DLSPARLLAAYQQGIFPWFDPGDPILWWSPDPRAVLWPESLHIARSMKRFLKRSPYRVSVNYAFGQVIEG
CASDRPEGTWISDELVEAYHRLHELGHAHSFEVWQGDELVGGMYGIAQGGLFCGESMFSRMTNASKTALL
VFCEHFIRHGGQLIDCQVQNPHLASLGAYEVPRKDYLKALNYRCH
>gnl|CDD|273208 TIGR00668, Bis5'-nucleosyl-tetraphosphatase_symmetrical, bis(5'-nucleosyl)-tetraphosphatase (symmetrical). Diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) is a regulatory metabolite of stress conditions. It is hydrolyzed to two ADP by this enzyme. Alternate names include diadenosine-tetraphosphatase and Ap4A hydrolase [Cellular processes, Adaptations to atypical conditions]
MATYLIGDLHGCYDELQALLERVEFDPGQDTLWLTGDLVARGPGSLEVLRYVKSLGDAVRLVLGNHDLHL
LAVFAGISRNKPKDRLDPLLEAPDADELLNWLRRQPLLQHDEEKKLVMAHAGITPQWDLQTAKECARDVE
AVLSSDSYPFFLDAMYGDMPNRWSPELQGLARLRFIINAFTRMRFCFPNGQLDMYSKESPEDAPAPLKPW
FAIPGPVYEEYSIAFGHWASLEGEGTPEGIYALDTGCCWGGRLTCLRWEDKQYFTQPSNRHKDLGEAAA
>gnl|CDD|129752 TIGR00669, Aspartate--ammonia_ligase, aspartate--ammonia ligase, AsnA-type. This model represents one of two non-homologous forms of aspartate--ammonia ligase (asparagine synthetase) found in E. coli. This type is also found in Haemophilus influenzae, Treponema pallidum and Lactobacillus delbrueckii, but appears to have a very limited distribution. The fact that the protein from the H. influenzae is more than 70 % identical to that from the spirochete Treponema pallidum, but less than 65 % identical to that from the closely related E. coli, strongly suggests lateral transfer [Amino acid biosynthesis, Aspartate family]
MKKAFILQQQQISFVKSTFTQQLEERLGLIEVQGPILSQVGDGTQDNLSGREKAVQVKVKAIPDAQFEVV
HSLAKWKRHTLARHDFSAGEGLFVHMKALRPDEDRLDPLHSVYVDQWDWEKVMPDGERNFAYLKSTVEAI
YAAIRATEAAVSERFGLAPFLPDQIHFVHSEELVSRYPDLDSKGRERAICKELGAVFLIGIGGKLSDGKP
HDVRAPDYDDWTTPSELGYKGLNGDILVWNPVLGDAFELSSMGIRVDEDALRHQLALTGDEDRLELEWHQ
DLLNGELPQTIGGGIGQSRLAMLLLQLKHIGEVQASVWPAAVREEFPNIL
>gnl|CDD|273209 TIGR00670, Aspartate_carbamoyltransferase, aspartate carbamoyltransferase. Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
RHLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVN
FSDSETSSVAKGETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYT
IYEEFGRLDGLKIALVGDLKYGRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESL
EEVIDEADVLYVTRIQKERFPDPEEYEKVKGSYGITLERLEAAKKGVIIMHPLPRVDEIDPSVDDTPHAK
YFKQAFNGVPVRMALLALLLG
>gnl|CDD|273210 TIGR00671, baf, pantothenate kinase, type III. This model describes a family of proteins found in a single copy in at least ten different early completed bacterial genomes. The only characterized member of the family is Bvg accessory factor (Baf), a protein required, in addition to the regulatory operon bvgAS, for heterologous transcription of the Bordetella pertussis toxin operon (ptx) in E. coli [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
LLLIDVGNTRIVFALNSGNKVYQFWRLATNLMKTYDEHSEFLKELFGKSLNKAFISSVVPELTEAVRNMI
PKIKNIKPEIFFPLVYDGLPNLYKSPKELGIDRVANALAAIKFYGFNVVVVDAGTALTIDLVDQEGKFLG
GAIAPGLGISLHALKDRAAALPKFEIARPDEVLGKSTREAVQSGAVYGVLGLIQGLLKDWKKYFKRKFAV
VITGGDGKYLSAFLPFSIYDPHLTVEGMRNLLR
>gnl|CDD|129755 TIGR00672, CDP-diacylglycerol_pyrophosphatase, CDP-diacylglycerol diphosphatase, bacterial type. This model finds only bacterial examples of CDP-diacylglycerol pyrophosphatase. The member from Mycobacterium tuberculosis, the only non-proteobacterial example, is only tentatively identified and scores below the trusted cutoff. No homology is detected to functionally similar mammalian enzymes. Alternate names for this enzyme include CDP-diglyceride hydrolase and CDP-diacylglycerol hydrolase [Fatty acid and phospholipid metabolism, Biosynthesis]
MKKAGLLFLAVIVIVVVAGIGYWKLTGEEPDTLRKIVLEECLPNQQQNQNPSPCAEVKPNAGYVVLKDLN
GPLQYLLMPTYRINGTESPLLLDPSTPNFFWLAWQARDFMSKKYGQPIPDRAVSLAINSRTGRSQNHFHI
HISCIRPDVRKQLDNNLKKISSRWLPLPGGLNGHEYLARRVTESELVQRSPFMMLAEEVPEAREHMGRYG
LAVVRQSDNSFVLLATQRNLLTLNRASAEEIQDHQCAILR
>gnl|CDD|213549 TIGR00673, Cyanate_hydratase, cyanase. Alternate names include cyanate C-N-lyase, cyanate hydratase, and cyanate hydrolase [Cellular processes, Detoxification]
MIQSQINRLADALLESKKKKGLTFADIADGLGLAEVFVAAALYGQAAAPADEARLVGAKLDLDEDSILEL
QMAPLRGCIDPVIPTDPTMYRFYEMLQVYGTTLKAVVHEKFGDGIMSAIDFKLDVEKVADPGGERAVITL
NGKYLPYKKF
>gnl|CDD|129757 TIGR00674, 4-hydroxy-tetrahydrodipicolinate_synthase, 4-hydroxy-tetrahydrodipicolinate synthase. Members of this family are 4-hydroxy-tetrahydrodipicolinate synthase, previously (incorrectly) called dihydrodipicolinate synthase. It is a homotetrameric enzyme of lysine biosynthesis. E. coli has several paralogs closely related to dihydrodipicoline synthase (DapA), as well as the more distant N-acetylneuraminate lyase. In Pyrococcus horikoshii, the bidirectional best hit with E. coli is to an uncharacterized paralog of DapA, not DapA itself, and it is omitted from the seed. The putative members from the Chlamydias (pathogens with a parasitic metabolism) are easily the most divergent members of the multiple alignment [Amino acid biosynthesis, Aspartate family]
GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPV
IAGTGSNATEEAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSL
YPETVKRLAEEPNIVAIKEATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKL
MKEMVNNALEGDFAEAREIHQKLMPLHKALFIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRD
VLKDL
>gnl|CDD|273211 TIGR00675, Modification_methylase, DNA-methyltransferase (dcm). All proteins in this family for which functions are known are DNA-cytosine methyltransferases. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
FIDLFAGIGGIRLGFEQAGFKCVFASEIDKYAQKTYEANFGNKVPFGDITKISPSDIPDFDILLGGFPCQ
PFSIAGKRKGFEDTRGTLFFEIVRILKEKKPKFFLLENVKGLVSHDKGRTFKVIIETLEELGYKVYYKVL
NAKDFGVPQNRERIYIVGFRDFDDKLNFEFPKPIYVAKKKRIGDLLDLSVDLEEKYYLSEEKKNGLLLLL
ENMRKKEGTGEQIGSFYNRESKSSIIRTLSARGYTFVKGGKSVLIVPHKSTVVHPGRIRRLTPRECARLQ
GFPDDFKFPVSDSQLYKQAGNAVVVPVIEAIAKQI
>gnl|CDD|273212 TIGR00676, 510-methylenetetrahydrofolate_reductase., 5,10-methylenetetrahydrofolate reductase, prokaryotic form. The enzyme activities methylenetetrahydrofolate reductase (EC 1.5.1.20) and 5,10-methylenetetrahydrofolate reductase (FADH) (EC 1.7.99.5) differ in that 1.5.1.20 (assigned in many eukaryotes) is defined to use NADP+ as an acceptor, while 1.7.99.5 (assigned in many bacteria) is flexible with respect to the acceptor; both convert 5-methyltetrahydrofolate to 5,10-methylenetetrahydrofolate. From a larger set of proteins assigned as 1.5.1.20 and 1.7.99.5, this model describes the subset of proteins found in bacteria, and currently designated 1.7.99.5. This protein is an FAD-containing flavoprotein [Amino acid biosynthesis, Aspartate family]
FSFEFFPPKTDEGEENLWETVDRLSPLDPDFVSVTYGAGGSTRDRTVRIVRRIKKETGIPTVPHLTCIGA
TREEIREILREYRELGIRHILALRGDPPKGEGTPTPGGFNYASELVEFIRNEFGDFDIGVAAYPEKHPEA
PNLEEDIENLKRKVDAGADYAITQLFFDNDDYYRFVDRCRAAGIDVPIIPGIMPITNFKQLLRFAERCGA
EIPAWLVKRLEKYDDDPEEVRAVGIEYATDQCEDLIAEGVPGIHFYTLNRADATLEICENLG
>gnl|CDD|129760 TIGR00677, Methylenetetrahydrofolate_reductase_1, methylenetetrahydrofolate reductase, eukaryotic type. The enzyme activities methylenetetrahydrofolate reductase (EC 1.5.1.20) and 5,10-methylenetetrahydrofolate reductase (FADH) (EC 1.7.99.5) differ in that 1.5.1.20 (assigned in many eukaryotes) is defined to use NADP+ as an acceptor, while 1.7.99.5 (assigned in many bacteria) is flexible with respect to the acceptor; both convert 5-methyltetrahydrofolate to 5,10-methylenetetrahydrofolate. From a larger set of proteins assigned as 1.5.1.20 and 1.7.99.5, this model describes the subset of proteins found in eukaryotes and designated 1.5.1.20. This protein is an FAD-containing flavoprotein [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
TFSFEFFPPKTEEGVQNLYERMDRMVASGPLFIDITWGAGGTTAELTLTIASRAQNVVGVETCMHLTCTN
MPIEMIDDALERAYSNGIQNILALRGDPPHIGDDWTEVEGGFQYAVDLVKYIRSKYGDYFCIGVAGYPEG
HPEAESVELDLKYLKEKVDAGADFIITQLFYDVDNFLKFVNDCRAIGIDCPIVPGIMPINNYASFLRRAK
WSKTKIPQEIMSRLEPIKDDDEAVRDYGIELIVEMCQKLLASGIKGLHFYTLNLEKAALMILERLGLLDE
S
>gnl|CDD|273213 TIGR00678, DNA_polymerase_III_subunit_delta', DNA polymerase III, delta' subunit. This model describes the N-terminal half of the delta' subunit of DNA polymerase III. Delta' is homologous to the gamma and tau subunits, which form an outgroup for phylogenetic comparison. The gamma/tau branch of the tree is much more tighly conserved than the delta' branch, and some members of that branch score more highly against this model than some proteins classisified as delta'. The noise cutoff is set to detect weakly scoring delta' subunits rather than to exclude gamma/tau subunits. At position 126-127 of the seed alignment, this family lacks the HM motif of gamma/tau; at 132 it has a near-invariant A vs. an invariant F in gamma/tau [DNA metabolism, DNA replication, recombination, and repair]
YQQLKRALEKGRLAHAYLFTGPEGVGKELLALALAKALLCEQRGGGEPCGECHSCRLIEAGNHPDLHRLE
PEGQSIKVDQVRELVEFLSRTPQESGRRVVIIEDAERMNEAAANALLKTLEEPPPNTLFILITPSPEKLL
PTIRSRCQRLPFPPLSEEALLQWLIRQGISEEAAELLLALAGGSPGRA
>gnl|CDD|273214 TIGR00679, HPr_kinase/phosphorylase, Hpr(Ser) kinase/phosphatase. Members of this family are the bifunctional enzyme, HPr kinase/phosphatase. All members of the seed alignment (n=57) have a gene tightly clustered with a gene for the phospocarrier protein HPr, its target [Regulatory functions, Protein interactions, Signal transduction, PTS]
ITVSELFEKLNLELVAGEDGLDREITEPDINRPGLELAGYFNYFHPKRVQVIGNTELSYLESLDEEERKE
RLEKLLKLKPPCLIVTRGLEPPEELLELAEEYNVPLLRTSLSTSELITTLTTYLEEQLAPRTTVHGVLVD
VFGVGVLITGESGIGKSETALELIKRGHRLVADDAVEIKRISGNTLIGRAPELLRHFMEVRGLGIINIRR
LFGISAVRDSKKIDLVIELEKWDDEKEYDRLGLEEQYYEILGVKIPKITIPVRPGRNLAVLIEVAARNHR
LKQMGYNAAEEFNERLRKAI
>gnl|CDD|273215 TIGR00680, Potassium-transporting_ATPase_A_chain, K+-transporting ATPase, KdpA. Kdp is a high affinity ATP-driven K+ transport system in Escherichia coli. It is composed of three membrane-bound subunits, KdpA, KdpB and KdpC and one small peptide, KdpF. KdpA is the K+-transporting subunit of this complex. During assembly of the complex, KdpA and KdpC bind to each other. This interaction is thought to stabilize the complex [medline:9858692]. Data indicates that KdpC might connect the KdpA, the K+-transporting subunit, to KdpB, the ATP-hydrolyzing (energy providing) subunit [medline:9858692] [Transport and binding proteins, Cations and iron carrying compounds]
MMLQGFLQIALILAVLVATAPLLGRYLARVFLDQSTPGDKIAGPLERVIFAGSGVTKHPEMGWTQYVSAA
LISNLVMGVFLFLILMFQGSLPLNPTGLPAPSWDLALNTAVSFVTNTNWQSYSGETTYSYFSQMGGLGVQ
NFTSAATGIAVAIALIRGLTRQSMSTLGNFWVDLVRSILRILLPISLVGAILLLVQGVPQNLAGPAQVNT
LEGATQLIPRGPVASQEAIKELGTNGGGFFNINSAHPFENPTNFANFVETVAIMVIPAALCFAFGIMAGD
RRQGWLILWMMFIIYGILIAIAMVGEFQGNPLLNALGGESQPNLEGKEVRFGVVLSALWAVSTTGTSCGA
VNGMHDSLTPLGGMVPLSDMFLGEVIWGGQGTGLAGLFVFLILAVFIAGLMVGRTPEYLGKKIEKREMKL
ASLIILIHPIAILIPAAITLAFPDTLAGISNPGPHGISEVLYAYASAANNNGSAFAGLAANTLWWNLSAS
FSMIAGRFVPIIPVIAIAGSLARKQPVPETSGTLPTHTPLFVGLTIGAVLIVGALTFLPALALGPVAEAL
SLV
>gnl|CDD|129764 TIGR00681, Potassium-transporting_ATPase_C_chain, K+-transporting ATPase, C subunit. This chain has a single predicted transmembrane region near the amino end. It is part of a K+-transport ATPase that contains two other membrane-bound subunits, KdpA and KdpB, and a small subunit KdpF. KdpA is the K+-translocating subunit, KdpB the ATP-hydrolyzing subunit. During assembly of the complex, KdpA and KdpC bind to each other. This interaction is thought to stabilize the complex [MEDLINE:9858692]. Data indicates that KdpC might connect the KdpA, the K+-transporting subunit, to KdpB, the ATP-hydrolyzing (energy providing) subunit [MEDLINE:9858692] [Transport and binding proteins, Cations and iron carrying compounds]
RNLVPALRSTALLWIITGLVYPLIVTVIGQLVFPYQANGSLITDSGQVVGSALIGQTFTEEGYFHSRPSA
INYSEYPTGASGGSNLAPSNPDLLSRIAARVEAQRLENLDAAVQVPVDLVTSSGSGLDPHISPAAAQAQF
PRVAKARNISPQQLQSLITKHTEGRFLGIFGEPGVNVLTLNLALDNL
>gnl|CDD|273216 TIGR00682, Tetraacyldisaccharide_4'-kinase, tetraacyldisaccharide 4'-kinase. Also called lipid-A 4'-kinase. This essential gene encodes an enzyme in the pathway of lipid A biosynthesis in Gram-negative organisms. A single copy of this protein is found in Gram-negative bacteria. PSI-BLAST converges on this set of apparent orthologs without identifying any other homologs [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
FSYLYELISNFRRFLYDLGLKKAWRAPVPVVIVGNLSVGGNGKTPVVVWLAELLKDRGVRVGVLSRGYGS
KTKKYTLYGSKKHSAEEVGDEPVLMAKRLHASVVASKDRYDAILLALEQLSPDIIILDDGLQHRKLHRDV
EIVVVDGQRLFGNRFLLPAGPLREPPKRLKSVDALIVNGGENEPGFIPMFLMPRIACCVNLSTGERVPFD
ILKERVIAFSGIGNPQRFFKTLKNLGIQIKGFMSFPDHQALNEDYSSFAPEEGQILLTTEKDAVKLQGLA
NENWLYLPVDLEIEEKEKPALLYKIFYKAKN
>gnl|CDD|273217 TIGR00683, N-acetylneuraminate_lyase, N-acetylneuraminate lyase. N-acetylneuraminate lyase is also known as N-acetylneuraminic acid aldolase, sialic acid aldolase, or sialate lyase. It is an intracellular enzyme. The structure of this homotetrameric enzyme related to dihydrodipicolinate synthase is known. In Clostridium tertium, the enzyme appears to be in an operon with a secreted sialidase that releases sialic acid from host sialoglycoconjugates. In several E. coli strains, however, this enzyme is responsible for N-acetyl-D-neuraminic acid synthesis for capsule production by condensing N-acetyl-D-mannosamine and pyruvate [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars]
LRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGSTGEAFVQSLSEREQVLEIVAEEAKGKI
KLIAHVGCVNTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSG
VKLTLDQINTLVTLPGVGALKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMG
WRYQGIVKALKEGDIQTAQKLQTECNKVIDLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLPE
LKALAQQLMQERG
>gnl|CDD|273218 TIGR00684, Probable_nitrate_reductase_molybdenum_cofactor, nitrate reductase molybdenum cofactor assembly chaperone. This protein is termed NarJ in most species that have a single copy, and has been called the delta subunit of nitrate reductase. However, although it is required for correct assembly of active enzyme, it dissociates and is not part of the enzyme. Two hits to this model are found each in E. coli and in Mycobacterium tuberculosis, but in each case duplication to create paralogs appears to be recent. The NarX protein of Mycobacterium tuberculosis includes one of these paralogs as a domain, fused to structural domains of nitrate reductases before and after the NarJ-homologous region [Protein fate, Protein folding and stabilization]
SILLSYPDEDLEELLRMREALKALLIGEDAEALGLFMEFLEKLDPEAADAQYVETFDMGRKTSMYLTYLL
KGEERMRGQEMLELKSHYEQQGDMPVDRELPDYLPLMLEYLALVDPEAARRFAKKYLQPWVGELASRLEK
NRSLYALLAKAL
>gnl|CDD|273219 TIGR00685, Trehalose-6-phosphate_phosphatase, trehalose-phosphatase. Trehalose, a neutral disaccharide of two glucose residues, is an important osmolyte for dessication and/or salt tolerance in a number of prokaryotic and eukaryotic species, including E. coli, Saccharomyces cerevisiae, and Arabidopsis thaliana. Many bacteria also utilize trehalose in the synthesis of trehalolipids, specialized cell wall constituents believed to be involved in the uptake of hydrophobic substances. Trehalose dimycolate (TDM, cord factor) and related substances are important constituents of the mycobacterial waxy coat and responsible for various clinically important immunological interactions with host organism. This enzyme, trehalose-phosphatase, removes a phosphate group in the final step of trehalose biosynthesis. The trehalose-phosphatase from Saccharomyces cerevisiae is fused to the synthase. At least 18 distinct sequences from Arabidopsis have been identified, roughly half of these are of the fungal type, with a fused synthase and half are like the bacterial members having only the phosphatase domain. It has been suggested that trehalose is being used in Arabidopsis as a regulatory molecule in development and possibly other processes [Cellular processes, Adaptations to atypical conditions]
ARKRAFFFDYDGTLSEIVPDPDAAVVSDRLLTILQKLAARPHNAIWIISGRKFLEKWLGVKLPGLGLAGE
HGCEMKDNGSCQDWVNLTEKIPSWKVRANELREEITTRPGVFIERKGVALAWHYRQAPVPELARFRAKEL
KEKILSFTDLEVMDGKAVVELKPRFVNKGEIVKRLLWHQPGSGISPVYLGDDITDEDAFRVVNNQWGNYG
FYPVPIGSGSKKTVAKFHLTGPQQVLEFLGLLVG
>gnl|CDD|273220 TIGR00686, Protein_PhnA_homolog, alkylphosphonate utilization operon protein PhnA. The protein family includes an uncharacterized member designated phnA in Escherichia coli, part of a large operon associated with alkylphosphonate uptake and carbon-phosphorus bond cleavage. This protein is not related to the characterized phosphonoacetate hydrolase designated PhnA by Kulakova, et al. (2001, 1997) [Unknown function, General]
DLPPCPKCNSEYTYHDGTQLICPSCLYEWNENEVNDDDDELIVKDCNGNLLANGDSVILIKDLKVKGSSL
VLKKGTKIKNIRLVNGDHNVDCKIEGGSLSLKSEFLKKA
>gnl|CDD|273221 TIGR00687, Pyridoxamine_kinase, pyridoxal kinase. E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAIN
KLNQCDAVLSGYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVAD
IITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVTHLIRAGSQRDRSFEGLVATQEGRWHISRP
LAVFDPPPVGTGDLIAALLLATLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSK
FDAEKVE
>gnl|CDD|129771 TIGR00688, Uncharacterized_transporter_HI_0680, rarD protein. This uncharacterized protein is predicted to have many membrane-spanning domains [Transport and binding proteins, Unknown substrate]
FKGIIVSLLASFLFGYMYYYSKLLKPLPATDILGHRMIWSFPFMLLSVTLFRQWAALIERLKRIQKRPLI
LSLLLCGLLIGFNWWLFIWAVNNGSSLEVSLGYLINPLVMVALGRVFLKERISRFQFIAVIIATLGVISN
IVLKGSLPWEALVLAFSFTAYGLIRKALKNTDLAGFCLETLSLMPVAIYYLLQTDFATVQQTNPFPIWLL
LVLAGLITGTPLLAFVIAANRLPLNLLGLLQYIGPTIMMLCVSFLI
>gnl|CDD|129772 TIGR00689, Probable_ribose-5-phosphate_isomerase_B, sugar-phosphate isomerase, RpiB/LacA/LacB family. Proteins of known function in this family act as sugar (pentose and/or hexose)-phosphate isomerases, including the LacA and LacB subunits of galactose-6-phosphate isomerases from Gram-positive bacteria and RpiB. RpiB is the second ribose phosphate isomerase of E. coli. It lacks homology to RpiA, its inducer is unknown (but is not ribose), and it can be replaced by the homologous galactose-6-phosphate isomerase of Streptococcus mutans, all of which suggests that the ribose phosphate isomerase activity of RpiB is a secondary function. On the other hand, there appear to be a significant number of species which contain rpiB, lack rpiA and seem to require rpi activity in order to complete the pentose phosphate pathway
IAIGSDHAGLELKSEIIEHLKQKGHEVIDCGTLYDERVDYPDYAKLVADKVVAGEVSLGILICGTGIGMS
IAANKFKGIRAALCVDEYTAALARQHNDANVLCLGSRVVGVELALSIVDAFLTTQFEGGRHQRRIDKIIE
YERE
>gnl|CDD|188073 TIGR00690, DNA-directed_RNA_polymerase_subunit_omega, DNA-directed RNA polymerase, omega subunit. This small component of highly purified E. coli RNA polymerase is not required for transcription, but acts in assembly and is present in stochiometric amounts. The trusted cutoff excludes archaeal homologs but captures some organellar sequences [Transcription, DNA-dependent RNA polymerase]
MARPTIEDAMKKIGSRYDLVLVAARRARQLQLEGGDPIVPEENDKPTVIALREIAAGLVS
>gnl|CDD|213552 TIGR00691, PppGpp_synthetase., (p)ppGpp synthetase, RelA/SpoT family. The functions of E. coli RelA and SpoT differ somewhat. RelA (EC 2.7.6.5) produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT (EC 3.1.7.2) degrades ppGpp, but may also act as a secondary ppGpp synthetase. The two proteins are strongly similar. In many species, a single homolog to SpoT and RelA appears reponsible for both ppGpp synthesis and ppGpp degradation. (p)ppGpp is a regulatory metabolite of the stringent response, but appears also to be involved in antibiotic biosynthesis in some species [Cellular processes, Adaptations to atypical conditions]
ALEIAKDLHEGQKRKSGEPYIIHPLAVALILAELGMDEETVCAALLHDVIEDTPVTEEEIEEEFGEEVAE
LVDGVTKITKLKKKSRQELQAENFRKMILAMAQDIRVIVIKLADRLHNMRTLDFLPPEKQKRIAKETLEI
YAPLAHRLGMSSIKTELEDLSFKYLYPKEYENIKSLVNEQKVNRENKLEKFKSELEKRLEDSGIEAELEG
RSKHLYSIYQKMTRKGQNFDEIHDLLAIRIIVKSELDCYRVLGIIHLLFKPIPGRFKDYIASPKENGYQS
LHTTVRGPKGLPVEIQIRTEDMDRVAEYGIAAHWIYKEGNPQKEALIDDMRWLNYLVEWQQESANFFEFI
ENLKSDLFNEEIYVFTPKGDVVELPSGSTPVDFAYAVHTDVGNKCTGAKVNGKIVPLDKELENGDVVEII
TGKNSNPSVIWLNFVVTSKARNKIRQWLKKLRREVAISEGKNILEKELGRSGLKLEDLTQYIQKRLNRLR
FKKLSELLAEIGKGNFSSKEVAKLLAQNNSKWQALTKPLKFAFSPKVFENSSFESIEGIEITKIVIAKCC
SPIPGDPIIGIVTKGKGLSVHHKDCKNLKNYKQEKIIEVEWNASKPRRFIVDINIEAVDRKGVLSDLTTA
ISENDSNIVSISTKTYGKREAILNITVEIKNYKHLLKIMLKIKTKNDVIVVKR
>gnl|CDD|129775 TIGR00692, L-threonine_3-dehydrogenase, L-threonine 3-dehydrogenase. This protein is a tetrameric, zinc-binding, NAD-dependent enzyme of threonine catabolism. Closely related proteins include sorbitol dehydrogenase, xylitol dehydrogenase, and benzyl alcohol dehydrogenase. Eukaryotic examples of this enzyme have been demonstrated experimentally but do not appear in database search results.E. coli His-90 modulates substrate specificity and is believed part of the active site [Energy metabolism, Amino acids and amines]
ALMKTKPGYGAELTEVPVPEPGPGEVLIKVLATSICGTDVHIYNWDEWAQSRIKPPQVVGHEVAGEVVGI
GPGVEGIKVGDYVSVETHIVCGKCYACRRGQYHVCQNTKIFGVDTDGCFAEYAVVPAQNIWKNPKSIPPE
YATIQEPLGNAVHTVLAGPISGKSVLVTGAGPIGLMAIAVAKASGAYPVIVSDPNEYRLELAKKMGATYV
VNPFKEDVVKEVADLTDGEGVDVFLEMSGAPKALEQGLQAVTPGGRVSLLGLPPGKVTIDFTNKVIFKGL
TIYGITGRHMFETWYTVSRLIQSGKLDLDPIITHKFKFDKFEKGFELMRSGQTGKVILSL
>gnl|CDD|273222 TIGR00693, Thiamine-phosphate_synthase, thiamine-phosphate diphosphorylase. This model represents the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria, and N-terminal domains of bifunctional thiamine proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the C-terminal domain corresponds to the bacterial hydroxyethylthiazole kinase (EC 2.7.1.50), ThiM. This model includes ThiE from Bacillus subtilis but excludes its paralog, the regulatory protein TenI (SP:P25053), and neighbors of TenI [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
GLYLITDPQDGPADLLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLAL
ALGADGVHLGQDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGV
ELLREIAATLIDIPIVAIGGITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL
>gnl|CDD|188074 TIGR00694, Hydroxyethylthiazole_kinase, hydroxyethylthiazole kinase. This model represents the hydoxyethylthiazole kinase, ThiM, of a number of bacteria, and C-terminal domains of bifunctional thiamine biosynthesis proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the N-terminal domain corresponds to the bacterial thiamine-phosphate pyrophosphorylase (EC 2.5.1.3), ThiE [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
LKRVREHRPLVHNITNYVAMNFTANGLLALGASPVMSEAEEEVAELAKIAGALVINIGTLDKESIEAMIA
AGKSANELGKPVVLDPVGVGATKFRTETSLELLSEGRVAAIKGNAGEIAALAGEEGKMRGVDSGEGAEDA
IRAAQQAAREYGTVVVVTGEVDYVSDGRRVYTIHNGTELLGKVTGSGCLLGSVVAAFCAVEEDPLDAAIS
ACLLYKIAGELAAERSKGPGSFHVELLDALSQLTEEVIQ
>gnl|CDD|129778 TIGR00695, Mannonate_dehydratase, mannonate dehydratase. This Fe2+-requiring enzyme plays a role in D-glucuronate catabolism in Escherichia coli. Mannonate dehydratase converts D-mannonate to 2-dehydro-3-deoxy-D-gluconate. An apparent equivalog is found in a glucuronate utilization operon in Bacillus stearothermophilus T-6 [Energy metabolism, Sugars]
MEQTWRWYGPNDPVSLADVRQAGATGIVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPVHED
IKTHTGNYEQWIANYKQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHI
LKRPGAEADYTEEEIAQAAERFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKEKLRE
NLAVFLKEIIPVAEEVGVRMAIHPDDPPRPILGLPRIVSTIEDMQWMVDTVNSPANGFTMCTGSYGVRAD
NDLVDMIKQFAPRIYFTHLRSTMREDNPKTFHEAAHLNGDVDMYEVVKAIVEEEHRRKAEGKEDLIPMRP
DHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGLELAIQRAFFSR
>gnl|CDD|129779 TIGR00696, UDP-N-acetyl-D-mannosaminuronic_acid_transferase, bacterial polymer biosynthesis proteins, WecB/TagA/CpsF family. The WecG member of this superfamily, believed to be UDP-N-acetyl-D-mannosaminuronic acid transferase, plays a role in enterobacterial common antigen (eca) synthesis in Escherichia coli. Another family member, the Bacillus subtilis TagA protein, is involved in the biosynthesis of the cell wall polymer poly(glycerol phosphate). The third family member, CpsF, CMP-N-acetylneuraminic acid synthetase has a role in the capsular polysaccharide biosynthesis pathway [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
EVINQAELVTPDGIGVVWGLKLLGYPQQSRVAGPDLMEELCQRAGKEKLPIFLYGGKPDVLQQLKVKLIK
EYPKLKIVGAFGPLEPEERKAALAKIARSGAGIVFVGLGCPKQEIWMRNHRHLKPDAVMIGVGGSFDVFS
GLVKRAPRWLMRLGLEWLYRLRMEPWRWKRMLLIPKY
>gnl|CDD|129780 TIGR00697, Uncharacterized_protein_HI_0862, conserved hypothetical integral membrane protein. All known members of this family are proteins or 210-250 amino acids in length. Conserved regions of hydrophobicity suggest that all members of the family are integral membrane proteins [Hypothetical proteins, Conserved]
RGKIWLSAWHSLAIIIANYFVLKPITLFGFEVTWGNVYYPGTFLATDVLREIYGKKDARKAIFVGFISAL
LFSVLTQLHLFFIPSPGDESQTHFEALFSSSPRIALASLVAYIVSQLLDVKVFTFLKKRTPGRFLWLRSN
GSTLFSQLIDTFIFSFIAFYGSPPFPAENLLNIMIFSYLIKGTIGVLATPPVYLAKLNILRK
>gnl|CDD|129781 TIGR00698, UPF0324_membrane_protein_HI_1643, conserved hypothetical integral membrane protein. Members of this family are found so far only in one archaeal species, Archaeoglobus fulgidus, and in two related bacterial species, Haemophilus influenzae and Escherichia coli. It has 9 GES predicted transmembrane regions at conserved locations in all members. These proteins have a molecular weight of approximately 35 to 38 kDa [Hypothetical proteins, Conserved]
LPFSRGLLQMALILLLAGAAGSIINLADPALSALFLAILLGMVAGNTIYPQRDEEKKRGVLFAKPFLLRI
GITLYGFRLTFPYIADVGPNEIVADTLILTSTFFLTVFLGSSRLKLDKQMSILLGAGSSICGAAAVAAIE
PVIKAEKEKVSVAIAIVVIFGTTGIFLYPSIYHYASHLISPDEFGIYAGSTVHEVAQVKASGQLIGPIVE
NEAVIIKMLRVMMLAPFLLILSIIYSRSDGISENESSKITIPWFAVLFIGVAIFNSFDLLPGEVVQALVP
LDTFLLATAMAALGLTTNVSAVKKAGVKPLFASYAGYLWLVGGGFVLNYLISGAI
>gnl|CDD|129782 TIGR00699, 4-aminobutyrate_aminotransferase, 4-aminobutyrate aminotransferase, eukaryotic type. This enzyme is a class III pyridoxal-phosphate-dependent aminotransferase. This model describes known eukaryotic examples of the enzyme. The degree of sequence difference between this set and known bacterial examples is greater than the distance between either set the most similar enzyme with distinct function, and so separate models are built for prokaryotic and eukaryotic sets. Alternate names include GABA transaminase, gamma-amino-N-butyrate transaminase, and beta-alanine--oxoglutarate aminotransferase [Central intermediary metabolism, Other]
KVYFPNEPTGPLMKTEIPGPKSKAAMKQLNEVFDARAVHFLADYEKSRGNYLVDVDGNRLLDLYSQISSI
PIGYNNPALLKAAQSPEMATTLINRPALGNFPSKDWAKILKEGILKVAPKGQDQVWTGMSGSDANELAFK
AAFMYYRSKQRGYQADFSEEENESCMDNQAPGSPDLSILSFKGAFHGRLFGSLSTTRSKPIHKLDIPAFD
WPQAPFPSLKYPLEEHVKENAKEEQRCLEEVEDLIKKWHKPVAAIIVEPIQSEGGDNHASPDFFRKLRDI
TKKHNVAFIVDEVQTGVGATGKFWAHEHWNLDDPPDMVTFSKKFQTAGYFFHDPAFRPNKPYRQFNTWMG
DPSRALILREIIQEIKRKDLLENVAHVGDYLYTGLEDLQKKYPEFIQNLRGKGRGTFIAWDTPDEAKRDK
LLKKARNNGVNIGGCGVKAIRLRPMLVFQKHHADIFLEIISKII
>gnl|CDD|129783 TIGR00700, semialdehyde_transaminase_GABA_aminotransferase, 4-aminobutyrate aminotransferase, prokaryotic type. This enzyme is a class III pyridoxal-phosphate-dependent aminotransferase. This model describes known bacterial examples of the enzyme. The best archaeal matches are presumed but not trusted to have the equivalent function. The degree of sequence difference between this set and known eukaryotic (mitochondrial) examples is greater than the distance to some proteins known to have different functions, and so separate models are built for prokaryotic and eukaryotic sets. E. coli has two isozymes. Alternate names include GABA transaminase, gamma-amino-N-butyrate transaminase, and beta-alanine--oxoglutarate aminotransferase [Central intermediary metabolism, Other]
QRRAAAVSSGVGVTLPVFAARAEGAILEDVDGNRLIDFASGIAVLNIGHSHPRVVDAVRTQVAEFTHTCF
MVTPYEGYVALAEKLNRIAPGSGPKKSVFFNSGAEAVENAVKIARSYTGRPGVVAFDHGFHGRTNMTMAL
TAKVMPYKSGFGPFAPEVYRAPLPYPYRDGLLDKQLSTDGELAAARAIFVIDVGANNVAALVIEPVQGEG
GFIVPAKGFVPALLDWCREHGIVFIADEVQTGFARTGAMFACEHEGPEPDLITTAKSLADGLPLSGVTGR
AEIMDAPAPGGLGGTYAGNPLACAAALAVLAIIESEGLIERARQIGRLVTDRLTTLKAVDPRIGDVRGLG
AMIAVELVDPGTTEPDAGLAERIATAAHAAGLLLLTCGMFGNIIRFLPPLTIGDELLSEGLDILCAILAD
>gnl|CDD|273223 TIGR00701, UPF0093_membrane_protein_HP_1484, TIGR00701 family protein. It appears this conserved hypothetical integral membrane protein is found only in gram negative bacteria. Completed genomes that include a member of this family include Rickettsia prowazekii, Synechocystis sp. PCC6803, and Helicobacter pylori. These proteins have 3 (Helicobacter pylori) to 5 (Synechocystis sp. PCC 6803) GES predicted transmembrane regions. Most members have 4 GES predicted transmembrane regions [Hypothetical proteins, Conserved]
YYLWFKAFHLISAICWMAGLFYLPRLFVYHAEAKIGSELDSTLQVMEKKLYRFIMNPAMISTFIFGIINA
HIEPFVAKSGWLHFKLFAVLLLLIYHFYCARWMKDLAKGKNVHSKKFYRIVNEAPTILMVIIVILVVVKP
FD
>gnl|CDD|273224 TIGR00702, Uncharacterized_protein_Rv1375/MT1419, YcaO-type kinase domain. This protein family includes YcaO and homologs that can phosphorylate a peptide amide backbone (rather than side chains), as during heterocycle-forming modifications during maturation of the TOMM class (Thiazole/Oxazole-Modified Microcins) of bacteriocins. However, YcaO domain proteins also occur in contexts that do not suggest peptide modification [Hypothetical proteins, Conserved]
ASPEETIAAFQQKLSPIGFTGIEEITWLDCLGIPVVWAVRPRDKDGALSISNGKGATKKAALASALMEAF
ERLSAEYFFADGLFVAYPNDKWFPLTDDPAPEGLILPSLYDAGVKLEWLTGETLIDLESGNVPAGAVFVP
YARQSDWQTLFRPNTNGLASGNTRDEAILHGLSEVIERDAWSLAEAARLPEIEVDVDDRYNSIIAHLIEK
LEAAGVPIDLADLTLGGGYPVVAAVLDDPTLGTLFGGFGAHLDPEVALERALTEVAQSRATQIHGVREDP
PFAIEEFAERANYERHKRDSSGWFSEDLIKRDTMYRFADWDFSGDLEEEAATLMAIGSGTEKLVYVDDYA
DVGVPAVRVIVPGMEVYSADPLRLARR
>gnl|CDD|129786 TIGR00703, UPF0128_protein_aq_756, TIGR00703 family protein. The function of this family is unknown. These proteins are from 222 to 233 residues in length, lack hydrophobic stretches, and are found so far only in thermophiles [Hypothetical proteins, Conserved]
EKMLENTLVFETLGVPEKEREFRMKDLKRWGFDLILGKIEGERTYFISKTGERHEGDKYIFKGKEYEVSE
TLKELPENARLLAHIEIERGNAYIVVWLREEDVNFELLREPARTLLKAFWKKEKLNQLLKHVKAVGLTTE
FYKQNGFQGIPLPYEELPPVARRFLREAKKVEKLTGFGRFVFAYFGETDKMHNRYRLSWLLPTIALFDID
IANKVDKVLGMLK
>gnl|CDD|273225 TIGR00704, Uncharacterized_protein_YqeW, Na/Pi-cotransporter. This model describes essentially the full length of an uncharacterized protein from Bacillus subtilis and correponding lengths of longer proteins from E. coli and Treponema pallidum. PSI-BLAST analysis converges to demonstrate homology to one other group of proteins, type II sodium/phosphate (Na/Pi) cotransporters. A well-conserved repeated domain in this family, approximately 60 residues in length, is also repeated in the Na/Pi cotransporters, although with greater spacing between the repeats. The two families share additional homology in the region after the first repeat, share the properly of having extensive hydrophobic regions, and may be similar in function [Transport and binding proteins, Cations and iron carrying compounds]
MLILIHFLAAIAFFLAGMHILRKGLIRMAGAKIEERLLLFTDHKLKAFCAGIGFTAILQSSNAFMMIVIG
FVAADLLAFAPAIPIILGADVGSAFMAEFIAFDLDILIPLLIFGGLIFFLGGKQSPAGQLGRSFIGLGII
FFAIEGFSHAAGPITKAKGGADIFAHLNDDILLAALIGAMFAAIIHSSLAAIGILASFMAAGIIGFPQAL
CLVIGANIGSCILAMLAASAAGAAAKQTALAHLLFKLLGSAIILPFLHAAAEFMEKLSLDKAEKIAHFHL
FFNLVRALLFLPFTDLFARFCHLIIPAE
>gnl|CDD|273226 TIGR00705, Protease_4, signal peptide peptidase SppA, 67K type. This model represents the signal peptide peptidase A (SppA, protease IV) as found in E. coli, Treponema pallidum, Mycobacterium leprae, and several other species, in which it has a molecular mass around 67 kDa and a duplication such that the N-terminal half shares extensive homology with the C-terminal half. This enzyme was shown in E. coli to form homotetramers. E. coli SohB, which is most closely homologous to the C-terminal duplication of SppA, is predicted to perform a similar function of small peptide degradation, but in the periplasm. Many prokaryotes have a single SppA/SohB homolog that may perform the function of either or both [Protein fate, Degradation of proteins, peptides, and glycopeptides]
WMVLNFVRLLVLNVVFLLLVLLGVKILVGDSSGRPSQKLVSSGALLLDLPVGDVTDQSPRVSLQGTLLGN
PKGRAISLFDIVNAIRQAADDRRIEGLVFDLSNFSGWDSPHLVEIGSALSEFKDSGKPVYAYGTNYSQGQ
YYLASFADEIILNPMGSVDLHGFYTETLFYKGMLDKLGVRWHXFRVGTYKGAVEPFSRKDMSPEARRNYQ
RWLGELWQNYLSSVSRNRAIPVQQLAPYAQGLLELLQKLNGDGARYALAEKLVTAVCSYAEAGKALKFLF
EDDYDKAKNFISLDDYNRDRPQRHDVQDKIGIVHLEGPIADGRDTEGNTGGDTVAALLRVARSDPDIKAV
VLRINSPGGSVFASEIIRRELARAQARGKPVIVSMGAMAASGGYWIASAADYIVASPNTITGSIGVFSVL
PTFENSLDRIGVHVDGVSTHELANVSLLRPLTAEDQAIMQLSVEAGYRRFLSVVSAGRNLTPTQVDKVAQ
GRVWTGEDAVSNGLVDALGGLDEAVAKAAKLAHCREQWSVEVYKDSATLGSELLQNLWDGLQKRSLAFLP
APLVILEREWGELAQFNDPKGTYA
>gnl|CDD|273227 TIGR00706, Putative_signal_peptide_peptidase_SppA, signal peptide peptidase SppA, 36K type. The related but duplicated, double-length protein SppA (protease IV) of E. coli was shown experimentally to degrade signal peptides as are released by protein processing and secretion. This protein shows stronger homology to the C-terminal region of SppA than to the N-terminal domain or to the related putative protease SuhB. The member of this family from Bacillus subtilis was shown to have properties consistent with a role in degrading signal peptides after cleavage from precursor proteins, although it was not demonstrated conclusively [Protein fate, Degradation of proteins, peptides, and glycopeptides]
KIAVLEVSGAIADVSPEDFDKKLERIKDDKTIKALVLRINSPGGTVVASEEIYKKLEKLKAKKPVVASMG
GMAASGGYYISMAADEIFANPGTITGSIGVILQGANVEKLAEKLGISFEVIKSGAYKDIGSPTRELTPEE
KNILQSLVNESYEQFVQVVSKGRNLPVEEVKKFADGRVFTGRQALKLRLVDKLGTLDDAIKWLKKLSG
>gnl|CDD|273228 TIGR00707, Acetylornithine_aminotransferase, transaminase, acetylornithine/succinylornithine family. This family of proteins, for which ornithine aminotransferases form an outgroup, consists mostly of proteins designated acetylornithine aminotransferase. However, the two very closely related members from E. coli are assigned different enzymatic activities. One is acetylornithine aminotransferase (EC 2.6.1.11), ArgD, an enzyme of arginine biosynthesis, while another is succinylornithine aminotransferase, an enzyme of the arginine succinyltransferase pathway, an ammonia-generating pathway of arginine catabolism (See MEDLINE:98361920). Members of this family may also act on ornithine, like ornithine aminotransferase (EC 2.6.1.13) (see MEDLINE:90337349) and on succinyldiaminopimelate, like N-succinyldiaminopmelate-aminotransferase (EC 2.6.1.17, DapC, an enzyme of lysine biosynthesis) (see MEDLINE:99175097)
YMMNTYGRLPVKIVRGKGSYVYDVNGKEYLDFVAGIAVNALGHAHPKLVEALKEQAEKLWHTSNLYYTEP
QEELAEKLVEHSGADRVFFCNSGAEANEAALKLARKYTGDKGSEKKKIVAFENAFHGRTMGTLSATGQPK
YQKGFEPLVPGFSYAPYNDIESLKAAIDDETAAVIVEPIQGEGGVVPASAEFLKALREICKDKDALLIFD
EVQTGVGRTGKLFAYEHYGVEPDIITLAKGLGGGVPIGATLAKEEVAEAFTPGDHGSTFGGNPLACAAAL
AVLEVIEKERLLENVKEKGDYFVERLEELGKNYGLKEVRGKGLMLGIELEAPYKDIVKEALEAGLLVNTA
GPNVLRFLPPLIITEEEIDEAVDALEAAI
>gnl|CDD|129791 TIGR00708, cobA, cob(I)alamin adenosyltransferase. Alternate name: corrinoid adenosyltransferase [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
AREERGIIIVHTGNGKGKTTAAFGMALRALGHGKKVGVIQFIKGAWPNGERAAFEPHGVEFQVMGTGFTW
ETQNREADTAIAKAAWQHAKEMLADPELDLVLLDELTYALKYGYLDVEEVVEALQERPGHQHVIITGRGC
PQDLLELADLVTEMRPVKHPFDAGVKAQRGIEY
>gnl|CDD|129792 TIGR00709, Diaminobutyrate--2-oxoglutarate_aminotransferase, 2,4-diaminobutyrate 4-transaminases. This family consists of L-diaminobutyric acid transaminases. This general designation covers both 2.6.1.76 (diaminobutyrate-2-oxoglutarate transaminase, which uses glutamate as the amino donor in DABA biosynthesis), and 2.6.1.46 (diaminobutyrate--pyruvate transaminase, which uses alanine as the amino donor). Most members with known function are 2.6.1.76, and at least some annotations as 2.6.1.46 in current databases at time of model revision are incorrect. A distinct branch of this family contains examples of 2.6.1.76 nearly all of which are involved in ectoine biosynthesis. A related enzyme is 4-aminobutyrate aminotransferase (EC 2.6.1.19), also called GABA transaminase. These enzymes all are pyridoxal phosphate-containing class III aminotransferase [Central intermediary metabolism, Other]
QNDLSRQNEMESNVRSYPRKLPTAFAKAQGCWVTDVEGKEYLDFLAGAGTLALGHNHPNMKQKILDYLQS
GLPLHTLDLTTPLKDAFIEALLNIIPKRKMDYKLQFPGPSGADAVEAAIKLAKTYTGRTNVISFSGGFHG
MTIGALAVTGNLFAKNAVGMLMPGVQFMPYPHEYRCPFGIGGEAGSNASIEYFENFIEDVESGVDKPAAV
ILEAIQGEGGVVAAPSEWLQKIREVTRKHDIKLILDEVQAGFGRSGTMFAFEHAGIEPDFVVMSKAVGGG
LPLAVLLIAPEFDAWQPAGHTGTFRGNQLAMVTGTEALNYWKDDNLAQNAQERGERITSFLDDMIKEHPC
IGNVRGRGLMQGIMIVDERQSKDATGAYPRDCELAAAIQGACFENGLLLETGGREGEVFRLLCPITIDQE
ECEEGISRFKQAVEEALAEVRL
>gnl|CDD|273229 TIGR00710, Bicyclomycin_resistance_protein_homolog, drug resistance transporter, Bcr/CflA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 12 membrane-spanning regions. Members with known activity include Bcr (bicyclomycin resistance protein) in E. coli, Flor (chloramphenicol and florfenicol resistance) in Salmonella typhimurium DT104, and CmlA (chloramphenicol resistance) in Pseudomonas sp. plasmid R1033
KSAKAFALLLGCLSILGPLGIDMYLPAFPEIAADLSTPASIVQMTLTLYLLGFAAGQLLWGPLSDRYGRR
PVLLLGLFIFALSSLGLALSNNIETLLVLRFVQAFGASAGSVISQALVRDIYPGEELSRIYSILMPVLAL
APAVAPLLGGYILVWLSWHAIFAFLSLAGILLSALIFFILPETLPYEARIQISTYFETFLLLLKSKMFWG
YALIYGASFGGFFAFFSGAPFVYIDIMGVSPSVFGLLFALNIIAMIFGGFLNGRFIKKWGAKSLLRMGLI
LFAVSAVLLEITAILGLGSWAMIIGPMMFVGIGNSMISSIAMAYALEDFPHVAGTASALFGTLRLVLGAI
VGYLVSLIHGNTAWPMSLSCLVLAVVSVLAFYYLS
>gnl|CDD|129794 TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other]
LLLTIVLMLGTFMAVLDSTIVNVAIPTIAGDLGSSLSQVQWVITSYMLANAISIPLTGWLAKRFGTRRLF
LISTFAFTLGSLLCGVAPNLELMIIFRVIQGFGGGPLIPLSFSTLLNIYPPEKRGRAMAIWGLTVLVAPA
LGPTLGGWIIENYHWRWIFLINVPIGIIVVVVAFFILPRDKPAASENFDFLGLLLLSVGLGSLLYGLSEG
PERGWFDSNEILILSITGLVAIIAFVVWELTDDNPLVDLRLFKYRNFTIGCVYMSLLGLGLYGSFYLLPL
YLQQVLGYTALQAGLHILPVGLAPMLSSPIAGRMGDKIDPRKLVTIGLILYAVGFYWRAFTFTPDTPFLA
IALPQFIRGFGMGCFFMPLTTIALSGLPPHKIARGSSLSNFTRQLGGSIGTALITTILTNRTQFHHSQLT
ETINPVNPNFLSGYSQLAALGNPEQQVYALIAQQITLHAFSIAINEIFWMATLLFVSGLILIWFL
>gnl|CDD|129795 TIGR00712, Glycerol-3-phosphate_transporter, glycerol-3-phosphate transporter. This model describes a very hydrophobic protein, predicted to span the membrane at least 8 times. The two members confirmed experimentally as glycerol-3-phosphate transporters, from E. coli and B. subtilis, share more than 50 % amino acid identity. Proteins of the hexose phosphate and phosphoglycerate transport systems are also quite similar [Transport and binding proteins, Other]
SIFKPAPHIARLPAAKIDPTYKRLRWQVFLGIFFGYAAYYLVRKNFALAMPYLVEQGFSKGELGFALSAI
SIAYGFSKFIMGSVSDRSNPRVFLPAGLILSAAVMLLMGFVPWATSSIAIMFVLLFLNGWFQGMGWPPCG
RTMVHWWSQSERGTIVSIWNCAHNIGGGIPPLLVLLGMAWFNDWHAALYFPAICAIIVALFAFAMMRDTP
QSCGLPPIEEYRNDYPDDYNEKAEQELTAKEIFMQYVLPNKLLWYIAIANVFVYLLRYGVLDWSPTYLKE
VKHFALDKSSWAYFLYEYAGIPGTLLCGWMSDKVFKGNRGATGVFFMTLVTIAVIVYWMNPAGNPLVDMI
CMIVIGFLIYGPVMLIGLHALELAPKKAAGTAAGFTGLFGYLGGSVAASAIVGYTVDFFGWDGGFMVMIG
GSILAVILLIVVMIGEKR
>gnl|CDD|273230 TIGR00713, Glutamate-1-semialdehyde_21-aminomutase, glutamate-1-semialdehyde-2,1-aminomutase. This enzyme, glutamate-1-semialdehyde-2,1-aminomutase (glutamate-1-semialdehyde aminotransferase, GSA aminotransferase), contains a pyridoxal phosphate attached at a Lys residue at position 283 of the seed alignment. It is in the family of class III aminotransferases [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
KSEKLFSEACQVIPGGVNSPVRAFKAVGGTPFFIARGKGAYLYDVDGNRYIDYVLSWGPLILGHAHPRVV
EAVAEALERGTSFGAPTELEIELAKLIIEYVPSVEMVRFVNSGTEATMSAVRLARGFTGRDKIVKFEGCY
HGHHDALLVKAGSGAATLGSPTSPGVPEDFAKLTLVLPYNDLEALEEAFEEYGEEIAGVIVEPVAGNMGV
VPPEPGFLAGLRALTREYGALLIFDEVMTGFRVSLGGAQEYYGVEPDLTTLGKIIGGGLPVGAFGGRREI
MERLAPEGPVYQAGTLSGNPLAMAAGLATLKLLREPGVYTQLDELAERLAEGLSEVLTDTGIPHTINRVG
SMFGFFFTEEEVRNYADAKKSDTERFAKFFHAMLEKGVYLPPSQFEACFLSAAHTEEDIENTIEAAEEVF
AEL
>gnl|CDD|211601 TIGR00714, Co-chaperone_protein_HscB_homolog, Fe-S protein assembly co-chaperone HscB. This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock [Protein fate, Protein folding and stabilization]
WQLDQSRLRKRYRQLQAQYHPDASGMAQEQLAASQQSTTLNQAYHTLKDPLRRAEYMLKLLNIDLTQEQT
SERDTAFPMELLKVRDELDEIEQMDDEAGLELLEKQNKEMIQDIEAQLGQCLNDQDWAAAVKYTVKLKYW
YKLASAFEDWEEGKQ
>gnl|CDD|273231 TIGR00715, Cobalt-precorrin-6A_reductase, precorrin-6x reductase. This enzyme catalyzes a step in cobalamin biosynthesis. It has been identified experimentally in Pseudomonas denitrificans and has been shown to be part of cobalamin biosynthetic operons in several other species. This enzyme was found to be a monomer by gel filtration [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
MTVLLMGGTVDSRAIAKGLIAQGIEILVTVTTSEGKHLYPIHQALTVHTGALDPQELREFLKRHSIDILV
DATHPFAAQITTNATAVCKELGIPYVRFERPPLALGKNIIEVPDIEEATRVAYQPYLRGKRVFLTAGASW
LSHFSLSQDEAVVFVRVLPYPQALAQALKLGFPSDRIIAMRGPFSEELEKALLREYRIDAVVTKASGEQG
GELEKVKAAEALGINVIRIARPQTIPGVAIFDDISQLNQFVARLLP
>gnl|CDD|129799 TIGR00716, Ribonuclease_HIII, ribonuclease HIII. This enzyme cleaves RNA from DNA-RNA hybrids. Two types of ribonuclease H in Bacillus subtilis, RNase HII (rnhB) and RNase HIII (rnhC), are both known experimentally and are quite similar to each other. The only RNase H homolog in the Mycoplasmas resembles rnhC. Archaeal forms resemble HII more closely than HIII. This model describes bacterial RNase III [DNA metabolism, DNA replication, recombination, and repair]
VLKISPSEAEKIQNYLVSSGFTKSNPPYTVFQLEGPGVKVTYYQSGKLLIQGKNSEKVLKRWGTAEVLNL
LEKKKLPADPRSVIGCDESGKGDIFGPLVLCCVYIPEENYLKVSSLNPRDSKRLSDKRIERLALNLKPLV
KAYCYELKPEKYNKLYRKFRNLNKMMAHFHKLLIERLLKEECGVSEVVVDQFAPSNPFFNHLKGRDIVGE
DVIFETEAERNLAVAAASIFARYKFLQSLKELERELGIKLPKGASKEVKELAKSLILKKGPSALERFIKL
HFNV
>gnl|CDD|273232 TIGR00717, 30S_ribosomal_protein_S1, ribosomal protein S1. This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned [Protein synthesis, Ribosomal proteins: synthesis and modification]
ESFAQLLEESLKTEETRPGSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEFLDAPLEIQVGDEVEVYLDR
VEDRFGETVLSREKAQRHELWIKLEKAYEEGSIVEGKIVGKVKGGFIVDLNGVEAFLPGSQVDVKPIKDL
DSLIGKTLKFKIIKLDQKRNNIVVSRRAYLEEERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGV
DGLLHITDMSWKRVKHPSEYVKVGQEVKVKVIKFDKEKGRISLSLKQLGEDPWEAIEKKFPVGDKITGRV
TNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNSHPSKVVKKGDEVEVMILDIDPERRRLSLGLKQCKANPW
EQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDKDGREADHLYKKGDEIEAVVLAVDK
EKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRNSELSENRDEDKTDE
IKVGDEVEAKVVDIDKKNRKVSLSVK
>gnl|CDD|129801 TIGR00718, Probable_L-serine_dehydratase_alpha_chain, L-serine dehydratase, iron-sulfur-dependent, alpha subunit. This enzyme is also called serine deaminase. L-serine dehydratase converts serine into pyruvate in the gluconeogenesis pathway from serine. This model describes the alpha chain of an iron-sulfur-dependent L-serine dehydratase, found in Bacillus subtilis. A fairly deep split in a UPGMA tree separates members of this family of alpha chains from the homologous region of single chain forms such as found in Escherichia coli. This family of enzymes is not homologous to the pyridoxal phosphate-dependent threonine deaminases and eukaryotic serine deaminases [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis]
MFNNAKEIIDICKEKGIKISDLMIAEEIENSEKTEEDIFKKLDANIDVMEAAAQKGLTEGDTSETGLIDG
DAKKLQAYANSGKSISGDFIADAMAKAFATNEVNAAMGKICAAPTAGSAGIMPAMLFAAKEKLNFDREQI
INFFFTAGAFGFVIAKNASFAGAAGGCQAECGSASAMAAAAIVEMAGGTPEQAAEAAAITIINMLGLVCD
PIAGLVEVPCTFRNAMGAINAFIAADLALAGIESLIPCDEVIDAMGEIGNSMIEALRETGLGGLAASKTG
QEIEKDFFGGAEGD
>gnl|CDD|129802 TIGR00719, Probable_L-serine_dehydratase_beta_chain, L-serine dehydratase, iron-sulfur-dependent, beta subunit. This enzyme is also called serine deaminase. This model describes the beta chain of an iron-sulfur-dependent L-serine dehydratase, as in Bacillus subtilis. A fairly deep split in a UPGMA tree separates members of this family of beta chains from the homologous region of single chain forms such as found in E. coli. This family of enzymes is not homologous to the pyridoxal phosphate-dependent threonine deaminases and eukaryotic serine deaminases [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis]
MKDRSAFDIIGPIMIGPSSSHTAGAAKIANVARSIFGNEPEQIEFQFHGSFAETFKGHGTDRAIIGGILD
FDPDDDRIKTAFEIAEAAGIDIEFRTEDAGDNVHPNSAKITFSDEKGEEEELIGISIGGGAIEITEINGF
AIEFRGEHPAILLEHNDKFGTIAGVANLLAGFEINIEHLETAKKDIGNIALLTIEIDKNIDDHIKDAI
>gnl|CDD|273233 TIGR00720, hypothetical_protein_NEICINOT_00681, L-serine dehydratase, iron-sulfur-dependent, single chain form. This enzyme is also called serine deaminase and L-serine dehydratase 1. L-serine ammonia-lyase converts serine into pyruvate in the gluconeogenesis pathway from serine. This enzyme is comprised of a single chain in Escherichia coli, Mycobacterium tuberculosis, and several other species, but has separate alpha and beta chains in Bacillus subtilis and related species. The beta and alpha chains are homologous to the N-terminal and C-terminal regions, respectively, but are rather deeply branched in a UPGMA tree. This enzyme requires iron and dithiothreitol for activation in vitro, and is a predicted 4Fe-4S protein. Escherichia coli Pseudomonas aeruginosa have two copies of this protein [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis]
ISVFDLFKIGIGPSSSHTVGPMRAAKQFADDLRDKGLLEQTTRVQVDLYGSLALTGKGHGTDKAVLLGLM
GFLPETVDIDSIEARIEEVLENKRLLLGGQHEIPFDYEKDLIFHNEFLPLHPNGMRFTAYNGDGEVLYEK
TYYSVGGGFIVDEEHFGKEGEEECDVPYPFSSAAELLALCQEHGLSISELMLENEKALRGENEIRAGLAH
IWHVMQECIERGLNTEGILPGGLRVRRRAPSLYRKLLASPETGNDPLAAIDWVNLYALAVNEENAAGGRV
VTAPTNGAAGIIPAVLHYYKKFIPGLSEEGVVRFLLTAGAIGILYKENASISGAEVGCQGEVGVACSMAA
AGLAELLGGTPEQVENAAEIAMEHNLGLTCDPVGGLVQIPCIERNAIAAVKAINAARMALRDDGAHRVSL
DKVIKTMYETGKDMNAKYKETSLGGLAVNV
>gnl|CDD|129804 TIGR00721, Tfx_protein, DNA-binding protein, Tfx family. PSI-BLAST starting with one member of this family converges with significant hits only to other members of the family, which is restricted to the Archaea. Homology is strongest in the helix-turn-helix-containing N-terminal region. Tfx from Methanobacterium thermoautotrophicum is associated with the operon for molybdenum formyl-methanofuran dehydrogenase and binds a DNA sequence near its promoter [Regulatory functions, DNA interactions]
MSKKTFLTERQIKVLELREKGLSQKEIAKELKTTRANVSAIEKRAMENIEKARNTLDFVKFIKSPVRILC
RRGDDLDEIPKRLFKKADEEGIKVIYDTIELIFLIREKASHRIEHRVVKSDFEIGVLRDGDIIVDLN
>gnl|CDD|273234 TIGR00722, Putative_fumarate_hydratase_subunit_alpha, hydro-lyases, Fe-S type, tartrate/fumarate subfamily, alpha region. A number of Fe-S cluster-containing hydro-lyases share a conserved motif, including argininosuccinate lyase, adenylosuccinate lyase, aspartase, class I fumarate hydratase (fumarase), and tartrate dehydratase (see PROSITE:PDOC00147). This model represents a subset of closely related proteins or modules, including the E. coli tartrate dehydratase alpha chain and the N-terminal region of the class I fumarase (where the C-terminal region is homologous to the tartrate dehydratase beta chain). The activity of archaeal proteins in this subfamily has not been established
ITEAVKEAIKEAVTRLPEDVVDAIKEAYDREESEIAKINLEAILDNIEIAEKLGVPVCQDTGVPIFFVKV
GSRFVLIGKLYEAIKQGVEEATEEVPLRPNAVHPLTRENTGDNTGLGVPQIHVEIVPGDELEIVVFPKGA
GSENPSALKMLKPSDGIEGVKKFVLETVKNAGGKPCPPIIVGVGIGGSFETAAKLAKKALLRPIGERHPN
PKIAKLELELLEEINSLGIGPMGLGGKTTALDVKIESAHCHTASLPVAVNIQCWAHRRATLVV
>gnl|CDD|129806 TIGR00723, L+-tartrate_dehydratase_beta_subunit_L-TTD, hydro-lyases, Fe-S type, tartrate/fumarate subfamily, beta region. A number of Fe-S cluster-containing hydro-lyases share a conserved motif, including argininosuccinate lyase, adenylosuccinate lyase, aspartase, class I fumarate hydratase (fumarase), and tartrate dehydratase (see PROSITE:PDOC00147). This model represents a subset of closely related proteins or modules, including the E. coli tartrate dehydratase beta chain and the C-terminal region of the class I fumarase (where the N-terminal region is homologous to the tartrate dehydratase alpha chain). The activity of archaeal proteins in this subfamily has not been established
EQILKLKVGDVVYLTGTIFTARDEAHARLLELIDEGKELPFDLNGSVIYHAGPIVTKNGEWEVVSVGPTT
SARMNPFEPELLEKLGVMAIIGKGGMSKEVVEACRKYKAVYLAFPGGCAALLAQSVKKVEGVAWEDLGMP
EAIWELEVEDFGPLIVAIDSHGNSIFQE
>gnl|CDD|129807 TIGR00724, Uncharacterized_protein_HI_1730, biotin-dependent carboxylase uncharacterized domain. Urea amidolyase of Saccharomyces cerevisiae is a 1835 amino acid protein with an amidase domain, a biotin/lipoyl cofactor attachment domain, a carbamoyl-phosphate synthase L chain-like domain, and uncharacterized regions. It has both urea carboxylase and allophanate hydrolase activities. This model models a domain that represents uncharacterized prokaryotic proteins of about 300 amino acids, regions of prokaryotic urea carboxylase and of the urea carboxylase region of yeast urea amidolyase, and regions of other biotin-containing proteins [Unknown function, General]
MIEILRAGSHTLIQDLGRVGYRRIGVPHSGAMDAYSLRLANRLVGNPDDTPAIEVTLGGPTIRFHCDVIF
AVTGADTDLCLNDGQVIPQWRPYEVKRGQILSLGRLKSGMRGYLAVRGGIDVPPVLGSCSTDLRANIGGY
EGRPLKAGDVLPLGSNELDLNEPQGLIPQIPEWRIEIRVLPGPEYDFFKRESIEAFWRSEWKVSSNSDRM
GYRLQGPKLKHARPNRELLTHGIVYGSIQVPPNGQPIILMADAQTTGGYPKIAVVIEADLWKVAQVRPGQ
SIKFVPLSLEEALKLRESQERYIKQLRGTLLREN
>gnl|CDD|129808 TIGR00725, TIGR00725, TIGR00725 family protein. This model represents one branch of a subfamily of uncharacterized proteins. Both PSI-BLAST and weak hits by this model show a low level of similarity and suggest an evolutionary relationship of the subfamily to the DprA/Smf family of DNA-processing proteins involved in chromosomal transformation with foreign DNA. Both Aquifex aeolicus and Mycobacterium leprae have one member in each of two branches of this subfamily, suggesting the branches may have distinct functions. This family is one of several families within the scope of pfam03641, several members of which are annotated as lysine decarboxylases. That larger family, and the branch described by this model, have a well-conserved motif PGGXGTXXE [Hypothetical proteins, Conserved]
MVQIGVIGSSNKSEELYEIAYRLGKELAKKGHILINGGRTGVMEAVSKGAREAGGLVVGILPDEDFAGNP
YLTIKVKTGMNFARNFILVRSADVVVSVGGGYGTAIEILGAYALGGPVVVLRGTGGWTDRLSQVLIEGVY
LDERVIVEITPAEAVKLAI
>gnl|CDD|273235 TIGR00726, Laccase_domain_protein, YfiH family protein. PSI-BLAST converges on members of this family of uncharacterized bacterial proteins and shows no significant similarity to any characterized protein. No completed genome to date has two members. Members of the family have been crystallized but the function is unknown [Unknown function, General]
GVSYLPFRSLNLGKHVGDNKAFVLANRERLIAYFNLPNKIVWLKQVHGDRVLKVTDKDSTLPEADGLITN
TPNLVLAVYTADCVPVLFYDRVGKIVAAVHAGWRGLKNGIIAKTVKMFKKFGSKPKDLIAVIGPAIGGCC
YEVDKEVYEAFRAVLPNASLPFIPDGKYLFDLRAIARLQLRELGVKQIFVSDRCTYTEPETFFSYRRDKT
KTGRMASVIWL
>gnl|CDD|129810 TIGR00727, unnamed_protein_product, small oligopeptide transporter, OPT family. This model represents a family of transporters of small oligopeptides, demonstrated experimentally in three different species of yeast. A set of related proteins from the plant Arabidopsis thaliana forms an outgroup to the yeast set by neighbor joining analysis but is remarkably well conserved and is predicted here to have equivalent function [Transport and binding proteins, Amino acids, peptides and amines]
EFDSPYPEVRAAVPPTDDPTIPVNTIRAWFIGLIWSTVGSGFNMFFSHRVPSISLNTPIIQMLAYPCGKA
WAKIIPDWTITIRGRKYNIIPGPFNVKEHMFITLMYAVSFGAAYTTDIILAQKLFYKSAFGFGYQFLLSL
STQFIGFGFAGILRRFVVYPARALWPTNLVTITINKALHGKENHEANGWKISRYKFFFLVFFASFIWNWF
PTYIFQALSTFNWMTWIKPNNINLNQIFGGSTGLGINPISSFDWNQISGYINSPLVYPAWSYLTIYLGCI
LAFWIVIPAVYYSNTWYCQYLPISSNGLYDNFGHSYNVTEILDKDNKFDVKKYQSYSPPFYSTTNAVSYG
LSFASIPLMITHSIIVHGKLLFNALKDDDYPDPHSNLMKAYKEVPDWWYLAVFLGFFGMGIATVEHWPTE
TPVWGLFVCLIFNFVFLIPTTILQATTNISFGLNVLTEFIVGYALPGRPLAMMIFKTFGYITDGQADNFV
SDLKIGHYMKIPPRALFRGQCVATIWQIFVQIGVLNWAIGNIDNFCTADQNAKYTCPNAVVFFNASVIWG
VIGPKRIFSHGYIYPGLKWFWLIGACIGIFFWLVWKKWPKFYPRYLDWPMLFVGTGYIPPATPYNYMYYT
SVGLFFQYYMKKHHLNWWEKYNYVLSAGLDTGLVLSAIIIFFCLQLKDTAF
>gnl|CDD|273236 TIGR00728, Putative_oligopeptide_transporter_YGL114W, oligopeptide transporter, OPT superfamily. This superfamily has two main branches. One branch contains a tetrapeptide transporter demonstrated experimentally in three different species of yeast. The other family contains EspB of Myxococcus xanthus, a protein required for normal rather than delayed sporulation after cellular aggregation; its role is unknown but is compatible with transport of a signalling molecule. Homology between the two branches of the superfamily is seen most easily at the ends of the protein. The central regions are poorly conserved within each branch and may not be homologous between branches
QEVRAVPPTDDPSLPELTFRAWFLGILIGVVFAAVNQFFGLRTGSVSISSIVAALLAYPLGKLWALIIPD
WEGWKFSLNPGPFNVKENNLIQTAASACGGLAYAIFILPAQKMFYTSNFSWGYQILLVWSTQLGFLGFGF
AGLLRRALVVPAKLPWPSGLATAELFKALHGKINSFHTANGWTIARNLLRVLLKYFSVSFLWSFVSWFFP
GFTALPTFGGLGSASIGIGWQQSSAYIGSGLITPFTVGLNILLGFVLAFGIVLPILYYKNTWPADADPID
SSSTIDSTGVRYNSVGLIVVDGLWTLVKPLYPIYSPLVLSIDFYALLFNAFSDTIYSFALAHGRDIISAR
RDHYKLGRDDHVRLLSRDEDLKVKNYKEVPAWWYLSLLLASFGLGIVVVEYYFGITQLPWWGVIVALIIA
LVLAIPIGILAGITNPASGLNIITELIIGYILPGRPLANLAFKAYGFITAQQAGDFMQDLKTGHYMKAPP
RAQFAAQLIGTIVGSLVNAPVLEWLYHAIGNQNNNFTCPNALVFFNASLIWGVIGPKIFSGKGLYCGLMW
FFLVGVGAVLVWLVRKLFPKWIKYINPPVAVGGGGYIPPATAVNYSTWAAVGGFFNYRWRKRKRADKNAE
KYNYVLAAGLIAGEALAGVIIFFCLGL
>gnl|CDD|129812 TIGR00729, Ribonuclease_HII, ribonuclease H, mammalian HI/archaeal HII subfamily. This enzyme cleaves RNA from DNA-RNA hybrids. Archaeal members of this subfamily of RNase H are designated RNase HII and one has been shown to be active as a monomer. A member from Homo sapiens was characterized as RNase HI, large subunit [DNA metabolism, DNA replication, recombination, and repair]
VAGIDEAGRGPVIGPLVVGVFAIEEKREEELRKLGVKDSKKLTPGRREELFSKIRNKLGRYEVLKITPEE
IDRERNINLNENEIEKFSKAAIILIEKPSEVYVDSVDVNPKRFKREIKIKERIEGIKVIAEHKADAKYPV
VSAASIIAKVERDREIESLKRKYGDFGSGYPSDPRTREWLEEYFKSHGELPDIVRRTWKTVRKLLD
>gnl|CDD|129813 TIGR00730, LOG_family_protein_YJL055W, TIGR00730 family protein. This model represents one branch of a subfamily of proteins of unknown function. Both PSI-BLAST and weak hits by this model show a low level of similarity to and suggest an evolutionary relationship of the subfamily to the DprA/Smf family of DNA-processing proteins involved in chromosomal transformation with foreign DNA. Both Aquifex aeolicus and Mycobacterium leprae have one member in each of two branches of this subfamily, suggesting that the branches may have distinct functions [Hypothetical proteins, Conserved]
KTVCVYCGSSPGGNAAYKELAAELGAYLAGQGWGLVYGGGRVGLMGAIADAAMENGGTAVGVNPSGLFSG
EVVHQNLTELIEVNGMHERKAMMAELADAFIAMPGGFGTLEELFEVLTWAQLGIHQKPIILFNVNGHFDG
LVEWLKYSIQEGFISESHLKLIHVVSRPDELIEQVQNY
>gnl|CDD|273237 TIGR00731, 50S_ribosomal_protein_L25, ribosomal protein bL25, Ctc-form. This model models a family of proteins with full-length homology to the general stress protein Ctc of Bacillus subtilis, a mesophile, and ribosomal protein TL5 of Thermus thermophilus, a thermophile. Ribosomal protein L25 of Escherichia coli and H. influenzae appear to be orthologous but consist only of the N-terminal half of Ctc and TL5. Both short (L25-like) and full-length (CTC-like) members of this family bind the E-loop of bacterial 5S rRNA. This protein appears to be restricted to bacteria and organelles, and consists of at most one copy per prokaryotic genome.Ctc of Bacillus subtilis has now been localized to ribosomes and can be viewed as the long form, or Ctc form, of L25. The C-terminal domain of sll1824, an apparent L25 of Synechocystis PCC6803, matches the N-terminal domain of this family. Examples of L25 and Ctc are not separated by a UPGMA tree built on the region of shared homology [Protein synthesis, Ribosomal proteins: synthesis and modification]
LEVKSRTSFGKSAARRIRKEGRIPAVVYGKGKENVNLELKSKEFIKYLRKGATSTVLTLEIGGKEFKVLV
KDYQYNPVTNEVIHVDFLEVVEGVKLKVEVPIKLIGTPIGVKNGGILTQVKRRIEVECKPKDIPDFLELD
VSSLGVGESLKLSDLELPAGVSFITDDDEVVVTVIK
>gnl|CDD|273238 TIGR00732, Protein_smf, DNA protecting protein DprA. Disruption of this gene in both Haemophilus influenzae and Helicobacter pylori drastically reduces the efficiency of transformation with exogenous DNA, but with different levels of effect on chromosomal (linear) and plasmid (circular) DNA. This difference suggests the DprA is not active in recombination, and it has been shown not to affect DNA binding, leaving the intermediate step in natural transformation, DNA processing. In Strep. pneumoniae, inactivation of dprA had no effect on the uptake of DNA. All of these data indicated that DprA is required at a later stage in transformation. Subsequently DprA and RecA were both shown in S. pneumoniae to be required to protect incoming ssDNA from immediate degradation. Role of DprA in non-transformable species is not known. The gene symbol smf was assigned in E. coli, but without assignment of function [Cellular processes, DNA transformation]
LEWIQRMGIKFITPDDKEYPFLLKAIYDPPPVLFYKGDLPLLSQRKVAIVGTRRPTKYGERWTRKLAEEL
AKNGVTIVSGLALGIDGIAHKAALKVNGRTIAVLGTGLDQIYPRQNSKLAAKIAENGGLLLSEYPPDTKP
IKYNFPKRNRIISGLSRAVLVVEAPLKSGALITARYALEQGREVFAYPGDLNSPESDGCHKLIEQGAALI
TSAKDILETL
>gnl|CDD|273239 TIGR00733, TIGR00733, putative oligopeptide transporter, OPT family. This protein represents a small family of integral membrane proteins from Gram-negative bacteria, a Gram-positive bacteria, and an archaeal species. Members of this family contain 15 to 18 GES predicted transmembrane regions, and this family has extensive homology to a family of yeast tetrapeptide transporters, including isp4 (Schizosaccharomyces pombe) and Opt1 (Candida albicans). EspB, an apparent equivalog from Myxococcus xanthus, shares an operon with a two component system regulatory protein, and is required for the normal timing of sporulation after the aggregation of cells. This is consistent with a role in transporting oligopeptides as signals across the membrane [Transport and binding proteins, Amino acids, peptides and amines]
EYTVRGFILGALITIIFTAANVYLGLYVGMTFAASIPAAVISMAVLMAFRDRSILENNMVQTAASAAGTL
SSVIFVLPALLMLGYWTEFPYWITTVICALGGSLGVLFTIPLRRAFVVESKLPYPEGVACAEVLKAGDKA
RNGTGAKPIAYGGILASIYAFLGSLRVWSGTLSAAKLVGRRALYFGSDLSLALIGVGYLVGLNIGFAMFL
GGAIAWGVAIPIYTAKMGSPGDLSALDLAWTIWSTKVRYIGVGAIVVAALWTLLKLRGPIARGIKAGLEA
ARRRQAGEAVLRTEEDLPINIVLTLVALFVIPLADFLLYAPILHNIGMAIAVMAVLMLIIGFFVAAIAGY
MAGLVGSSNSPISGIGIMSVLFTALILKGLGLSGTGSQIPELMAATIFTAAVVCTAAAISNDNLQDLKTG
YLVGATPWRQQVALIIGTFVGALVMAPVLNLLIKAYGIAGTPTAKGENALPAPQAFLMAAVTEGVFTGTL
EWTMVFIGAGIGIALIIIDEILAKRGSKFRTPVMAVGVGIYLPLSLGVPILLGAFLARILVSRGRKEGES
FTDKKRLGVLGAAGLIVGESLTGVVFAAIIA
>gnl|CDD|273240 TIGR00734, Uncharacterized_protein_MJ0703, hisA/hisF family protein. This model models a family of proteins found so far in three archaeal species: Methanobacterium thermoautotrophicum, Methanococcus jannaschii, and Archaeoglobus fulgidus. This protein is homologous to phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase (HisA) and, with lower similarity, to the cyclase HisF, both of which are enzymes of histidine biosynthesis. Each species with this protein also encodes HisA. The function of this protein is unknown [Unknown function, General]
MKIIPVIDLKDGIAVAGKSGERESYPPLESVSRLSSSPDDAAKVIEEIGARFIYIADLDRIVGLGDNFSL
LSKLSKRVELIADCGVRSPEDLETLPFTLEFASRVVVATETLDITELLRECYTVVSLDFKEKFLDASGLF
ESLEEVRDFLNSFDYGLIVLDIHSVGTMKGPNLELLTKTLELSEHPVMLGGGISGVEDLELLKEMGVSAV
LVATAVHKGKI
>gnl|CDD|273241 TIGR00735, Imidazole_glycerol_phosphate_synthase_subunit_HisF, imidazoleglycerol phosphate synthase, cyclase subunit [Amino acid biosynthesis, Histidine family]
MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTA
ETVFIPLTVGGGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNSYC
WYEVYIYGGRESTGLDAVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGK
PEHFYEAFTKGKADAALAASVFHYREITIGEVKEYLAERGIPVR
>gnl|CDD|129819 TIGR00736, Uncharacterized_protein_MJ0144, TIM-barrel protein, putative. Members of this family show a distant relationship by PSI-BLAST to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase. At least two closely related but well-separable families among the bacteria, the nifR3/yhdG family and the yjbN family, share a more distant relationship to this family of shorter, exclusively archaeal proteins [Unknown function, General]
MAGITDAEFCRKFKDLFAIVTLGGYNADRATYKASRDIEKRGRKEFSFNLEEFNSYIIEQIKKAESRALV
SVNVRFVDLEEAYDVLLTIAEHADIIEINAHCRQPEITEIGIGQELLKNKELLKEFLTKMKELNKPIFVK
IRGNCIPLDELIDALNLVDDGFDGIHVDAMYPGKPYADMDLLKILSEEFNDKIIIGNNSIDDIESAKEML
KAGADFVSVARAILKGNVEFI
>gnl|CDD|129820 TIGR00737, Probable_tRNA-dihydrouridine_synthase, putative TIM-barrel protein, nifR3 family. This model represents one branch of COG0042 (Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 family). This branch includes NifR3 itself, from Rhodobacter capsulatus. It excludes a broadly distributed but more sparsely populated subfamily that contains sll0926 from Synechocystis PCC6803, HI0634 from Haemophilus influenzae, and BB0225 from Borrelia burgdorferi. It also excludes a shorter and more distant archaeal subfamily.The function of nifR3, a member of this family, is unknown, but it is found in an operon with nitrogen-sensing two component regulators in Rhodobacter capsulatus.Members of this family show a distant relationship to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase [Unknown function, General]
IGNIQLKSRVVLAPMAGVTDSPFRRLVAEYGAGLTVCEMVSSEAIVYDSQRTMRLLDIAEDETPISVQLF
GSDPDTMAEAAKINEELGADIIDINMGCPVPKITKKGAGSALLRDPDLIGKIVKAVVDAVDIPVTVKIRI
GWDDAHINAVEAARIAEDAGAQAVTLHGRTRAQGYSGEANWDIIARVKQAVRIPVIGNGDIFSPEDAKAM
LETTGCDGVMIGRGALGNPWLFRQIEQYLTTGKYKPPPTFAEKLDAILRHLQLLADYYGESKGLRIARKH
IAWYLKGFPGNAALRQTLNHASSFQEVKQLLDDFFETVG
>gnl|CDD|273242 TIGR00738, Putative_HTH-type_transcriptional_regulator, Rrf2 family protein. This model represents a superfamily of probable transcriptional regulators. One member, RRF2 of Desulfovibrio vulgaris is an apparent regulatory protein experimentally (MEDLINE:97293189). The N-terminal region appears related to the DNA-binding biotin repressor region of the BirA bifunctional according to results after three rounds of PSI-BLAST with a fairly high stringency [Unknown function, General]
MKLTKKTEYALRALLDLALNPDEGPVSVKEIAERQGISRSYLEKILRTLRKAGLVESVRGPGGGYRLARP
PEEITVGDVVRAVEGSLAPVQCIGLNGCHPGEEVCLLHAVWRELEDAIEDFLREITLADLVK
>gnl|CDD|273243 TIGR00739, UPF0092_membrane_protein, preprotein translocase, YajC subunit. While this protein is part of the preprotein translocase in Escherichia coli, it is not essential for viability or protein secretion. The N-terminus region contains a predicted membrane-spanning region followed by a region consisting almost entirely of residues with charged (acidic, basic, or zwitterionic) side chains. This small protein is about 100 residues in length, and is restricted to bacteria; however, this protein is absent from some lineages, including spirochetes and Mycoplasmas [Protein fate, Protein and peptide secretion and trafficking]
SFLTTLLPLVLIFLIFYFLIIRPQRKRRKAHKKLIESLKKGDKVLTIGGIIGTVTKIAENTIVIELNDNT
EITFSKNAIVEVLP
>gnl|CDD|273244 TIGR00740, tRNA_cmo5U34-methyltransferase, tRNA (cmo5U34)-methyltransferase. This tRNA methyltransferase is involved, together with cmoB, in preparing the uridine-5-oxyacetic acid (cmo5U) at position 34 [Unknown function, Enzymes of unknown specificity]
KDTLFSAPIAKLGDFIFDENVAEVFPDMIQRSVPGYSNIISAIGMLAERFVQADSNVYDLGCSLGAATLS
ARRNIHHDNCKIIAIDNSPAMIERCRQHIAAYHAEIPVDIICGDIRDIAIENASMVILNFTLQFLEPEDR
IALLDKIYEGLNPGGALVLSEKFRFEDAKIGELLFDLHHDFKRANGYSELEISQKRSALENVMLTDSIET
HKARLHNAGFEHSELWFQCFNFGSLIALK
>gnl|CDD|129824 TIGR00741, Probable_sigma54_modulation_protein_ORF3_ORF95., ribosomal subunit interface protein. This model includes a small protein encoded by one of two genes, both downstream of the gene rpoN for sigma 54, whose deletion leads to increased expression from sigma 54-dependent promoters. It also includes the N-terminal half of a light-repressed protein LtrA of Synechococcus PCC 7002 and the N-terminal region (after removal of the transit peptide) of a larger plastid-specific ribosomal protein of spinach. The member of this family from E. coli is now recognized as a protein at the interace between ribosomal large and small subunits, with about 1/3 as many copies per cell as the number of ribosomes [Protein synthesis, Translation factors]
MNINITGNNVEITEALREYVEEKLARLERYFTRIINVDVVLSVERNRFKVEATLYVNGGVIRASAESEDM
YAAIDLAIDKLERQLRKLKEKRKEH
>gnl|CDD|129825 TIGR00742, Probable_tRNA-dihydrouridine_synthase_2, tRNA dihydrouridine synthase A. This model represents one branch of COG0042 (Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 family). It represents a distinct subset by a set of shared unique motifs, a conserved pattern of insertions/deletions relative to other nifR3 homologs, and by subclustering based on cross-genome bidirectional best hits. Members are found in species as diverse as the proteobacteria, a spirochete, a cyanobacterium, and Deinococcus radiodurans. NifR3 itself, a protein of unknown function associated with nitrogen regulation in Rhodobacter capsulatus, is not a member of this branch. Members of this family show a distant relationship to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase [Protein synthesis, tRNA and rRNA base modification]
GRFSVAPMLDWTDRHFRYFLRLLSKHTLLYTEMITAKAIIHGDKKDILKFSPEESPVALQLGGSDPNDLA
KCAKIAEKRGYDEINLNVGCPSDRVQNGNFGACLMGNADLVADCVKAMQEAVNIPVTVKHRIGIDPLDSY
EFLCDFVEIVSGKGCQNFIVHARKAWLSGLSPKENREIPPLRYERVYQLKKDFPHLTIEINGGIKNSEQI
KQHLSHVDGVMVGREAYENPYLLANVDREIFNETDEILTRKEIVEQMLPYIEEYLSQGLSLNHITRHLLG
LFQGKPGAKQWRRYLSENAPKAGAGIEVLETALETVPE
>gnl|CDD|273245 TIGR00743, UPF0381_protein_HI_0400, conserved hypothetical protein. These small proteins are approximately 100 amino acids in length and appear to be found only in gamma proteobacteria. The function of this protein family is unknown [Hypothetical proteins, Conserved]
AIQKCKAIETVGCNCFDVGTIIDNSDCSQVISRFYATEAEAEEALAFLTEKARDTESEPCEIQSEITKVE
DGVLLDADFTFSCQAEMVIFELRLR
>gnl|CDD|273246 TIGR00744, Glucokinase_Glucose_kinase., ROK family protein (putative glucokinase). This model models one branch of the ROK superfamily of proteins. The three members of the seed alignment for this model all have experimental evidence for activity as glucokinase, but the set of related proteins is crowded with paralogs of different or unknown function. Proteins scoring above the trusted_cutoff will show strong similarity to at least one known glucokinase and may be designated as putative glucokinases. However, definitive identification of glucokinases should be done only with extreme caution [Unknown function, General]
IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVDAIASAVDSFIQHIAKVGHEIVAIGIGAPGPVN
RQRGTVYFAVNLDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGII
INGEIRHGHNGVGAEIGHIRMVPDGRLLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGD
GISAKHVFVAARQGDPVAVDSYREVARWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWL
FGGARQVADIIAAQLGNDAGLVGAADLARTYIIEPDPI
>gnl|CDD|273247 TIGR00745, Putative_2-dehydropantoate_2-reductase, 2-dehydropantoate 2-reductase. This model describes enzymes that perform as 2-dehydropantoate 2-reductase, one of four enzymes required for the de novo biosynthesis of pantothenate (vitamin B5) from Asp and 2-oxoisovalerate. Although few members of the seed alignment are characterized experimentally, nearly all from complete genomes are found in a genome-wide (but not local) context of all three other pantothenate-biosynthetic enzymes (TIGR00222, TIGR00018, TIGR00223). The gene encoding this enzyme is designated apbA in Salmonella typhimurium and panE in Escherichia coli; this protein functions as a monomer and functions in the alternative pyrimidine biosynthetic, or APB, pathway, used to synthesize the pyrimidine moiety of thiamine. Note, synthesis of the pyrimidine moiety of thiamine occurs either via the first five steps in de novo purine biosynthesis, which uses the pur gene products, or through the APB pathway. Note that this family includes both NADH and NADPH-dependent enzymes, and enzymes with broad specificity, such as a D-mandelate dehydrogease that is also a 2-dehydropantoate 2-reductase [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
AVGSLYGAYLARAGHDVTLLARGEQLEALNQEGLRIVSLGGEFQFRPVSAATSPEELPPADLVIITVKAY
QTEEAAALLLPLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIGD
YVGENEAVEALAELLNEAGIPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLM
DEVVRVARAEGVDLPDDEVEELVRAVIRMTAENTSSMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVN
RTLYALLKALEAE
>gnl|CDD|273248 TIGR00746, Carbamate_kinase, carbamate kinase. In most species, carbamate kinase works in arginine catabolism and consumes carbamoyl phosphate to convert ADP into ATP. In the pathway in Pyrococcus furiosus, the enzyme acts instead to generate carbamoyl phosphate.The seed alignment for this model includes experimentally confirmed examples from a set of phylogenetically distinct species. In a neighbor-joining tree constructed from an alignment of candidate carbamate kinases and several acetylglutamate kinases, the latter group forms a clear outgroup which roots the tree of carbamate kinase-like proteins. This analysis suggests that in E. coli, the ArcC paralog YqeA may be a second isozyme, while the paralog YahI branches as an outlier and is less likely to be an authentic carbamate kinase. The homolog from Mycoplasma pneumoniae likewise branches outside the set containing known carbamate kinases and also scores below the trusted cutoff [Energy metabolism, Amino acids and amines]
KRVVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVGNLLLQNQAADSEVP
AMPLDVLGAMSQGMIGYMLQQALNNELPKRGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKR
LAAEKGWIVKEDAGRGWRRVVPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAELKGVEAVID
KDLASEKLAEEVNADILVILTDVDAVYINYGKPDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEF
VESGGKRAIITSLENAVEALEGKAGTRVTK
>gnl|CDD|273249 TIGR00747, 3-oxoacyl-_synthase_3, 3-oxoacyl-(acyl-carrier-protein) synthase III. FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity. Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment [Fatty acid and phospholipid metabolism, Biosynthesis]
MYAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISK
DDIDLIIVATTTPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAE
KLSSTLDWTDRGTCVLFGDGAGAVVLGESEDPGGIISTHLGADGTQGEALYLPAGGRPTSGPSPFITMEG
NEVFKHAVRKMGDVVEETLEANGLDPEDIDWFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAAS
IPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAALVRF
>gnl|CDD|273250 TIGR00748, UPF0219_protein_MJ1546, hydroxymethylglutaryl-CoA synthase, putative. This family of archaeal proteins shows considerable homology and identical active site residues to the bacterial hydroxymethylglutaryl-CoA synthase (HMG-CoA synthase, modeled by TIGR01835) which is the second step in the mevalonate pathway of IPP biosynthesis. An enzyme from Pseudomonas fluorescens involved in the biosynthesis of the polyketide diacetyl-phloroglucinol is more closely related, but lacks the active site residues. In each of the genomes containing a member of this family there is no other recognized HMG-CoA synthase, although other elements of the mevalonate pathway are in evidence. The only archaeon currently sequenced which lacks a homolog in this pathway is Halobacterium, which _does_ contain a separate HMG-CoA synthase. Thus, although there is no experimental evidence supporting this name, the bioinformatics-based conclusion appears to be sound [Fatty acid and phospholipid metabolism, Biosynthesis]
DAGIVGYGAYIPKYRIKNEEIARVWGKDPESIKKGFLIEEKAVPGLDEDAATIAIEAARNALKRAEIDPK
DIGAIWFGSESHPYAVKPSATIIAEAIDATPDLEAADFEFACKAGTAAIQAAIGFVASGLAKYALAIGAD
TAQGAPGDALEFTAAAGGAAFIIGEKNSETIAEFEGSYSYTTDTPDFWRREGEHYPRHGGRFTGEPAYFH
HVINAAKGLMDELGLKPEDFDYAVFHQPNGKFPIRAAKILGFKEEKVKIGLLSGRIGNTYSGATMLGISA
VLDIAEGGDRILAVSFGSGAGSDAFDITVQDAIEEKKDKAPKTADYIERKEVIDYAIYAKARKKIII
>gnl|CDD|129832 TIGR00749, Glucokinase_Glucose_kinase., glucokinase, proteobacterial type. This model represents glucokinase of E. coli and close homologs, mostly from other proteobacteria, presumed to have equivalent function. This glucokinase is more closely related to a number of uncharacterized paralogs than to the glucokinase glcK (fromerly yqgR) of Bacillus subtilis and its closest homologs, so the two sets are represented by separate models [Energy metabolism, Glycolysis/gluconeogenesis]
LVGDIGGTNARLALCEIAPGEISQAKTYSGLDFPSLEAVVRVYLEEHKVELKDPIAKGCFAIACPITGDW
VAMTNHTWAFSIAELKQNLGFSHLEIINDFTAVSYAIPGLKKEDLIQFGGAEPVEGKPIAILGAGTGLGV
AHLIHQVDGRWVVLPGEGGHVDFAPNSELEAIILEYLRAKIGHVSAERVLSGPGLVNIYEALVKADPERQ
FNKLPQENLKPKDISERALAGSCTDCRRALSLFCVIYGRFAGNLALNLGTRGGVYIAGGIVPRFIEFFKA
SGFRAAFEDKGRMKEYVHDIPVYVVLHDNPGLLGAG
>gnl|CDD|129833 TIGR00750, Hypothetical_protein_Rv1496/MT1543/Mb1533., LAO/AO transport system ATPase. In E. coli, mutation of this kinase blocks phosphorylation of two transporter system periplasmic binding proteins and consequently inhibits those transporters. This kinase is also found in Gram-positive bacteria, archaea, and the roundworm C. elegans. It may have a more general, but still unknown function. Mutations have also been found that do not phosphorylate the periplasmic binding proteins, yet still allow transport. The ATPase activity of this protein seems to be necessary, however [Transport and binding proteins, Amino acids, peptides and amines, Regulatory functions, Protein interactions]
GDRRALARAITLVENRHPEAKELLDRIMPYTGNAHRVGITGTPGAGKSTLLEALGMELRRRGLRVAVIAV
DPSSPFTGGSILGDRTRMQRLATDPGAFIRSMPTRGHLGGLSQATRELVLLLDAAGYDVIIVETVGVGQS
EVDIANMADTFVLVTIPGTGDDLQGIKAGVMEIADIYVVNKADGEGATNVRIARLMLSLALEEIRRREDG
WRPPVLTTSAVEGRGIDELWDAIEEHKTFLTASGLLQERRRQRSVEWLKKLVEEEVLKKVFANEDVYRDL
LLAVLAGELDPYTAAEQILE
>gnl|CDD|129834 TIGR00751, 14-dihydroxy-2-naphthoate_octaprenyltransferase, 1,4-dihydroxy-2-naphthoate octaprenyltransferase. This membrane-associated enzyme converts 1,4-dihydroxy-2-naphthoic acid (DHNA) to demethylmenaquinone, a step in menaquinone biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
RPKTLPLAIAPIVAGTALAAWLHAFVWLVALLALATAVLLQILSNYANDYGDGIKGSDTDDRIGPLRGVQ
KGLITPREVKTALITSVALGALSGLVLALLAAPNLSDLFWFIALGALCIAAAITYTVGSKPYGYAGLGDI
SVLVFFGPLAVLGTQYLQAHRVDWVGILPAVATGLLACAVLNINNLRDIPTDARAGKNTLAVRLGDARTR
MYHQGLLAVAGVCTFVFMLATPISWWCVLFLLAAPLLLKAAGPVRSGRGPRELRPVLRDTGLAMLLWNLL
FALG
>gnl|CDD|273251 TIGR00752, Hypothetical_lipoprotein_yeaY_precursor., outer membrane lipoprotein, Slp family. Slp superfamily members are present in the Gram-negative gamma proteobacteria Escherichia coli, which also contains a close paralog, Haemophilus influenzae and Pasteurella multocida and Vibrio cholera. The known members of the family to date share a motif LX[GA]C near the N-terminus, which is compatible with the possibility that the protein is modified into a lipoprotein with Cys as the new N-terminus. Slp from Escherichia coli is known to be a lipoprotein of the outer membrane and to be expressed in response to carbon starvation [Cell envelope, Other]
NGKKGLLFTALCFGLTGCIAPPKGIKGERPFSQNSYVEVSPQPLLYVGQTARFGGKVVNVTNLANQTKLE
IASLPLDSIAKPFVELQSDGRFIAYFNGFLDPVNLRERYVTVGGQIAGTEKGKIEQAPYTFPVVQADGYR
IWHLSTTVDYTPTDDWDYGGDDWPFFGWGHLWYVQPEIHVYL
>gnl|CDD|129836 TIGR00753, undec_PP_bacA, undecaprenyl-diphosphatase UppP. This is a family of small, highly hydrophobic proteins. Overexpression of this protein in Escherichia coli is associated with bacitracin resistance, and the protein was originally proposed to be an undecaprenol kinase and called bacA. It is now known to be an undecaprenyl pyrophosphate phosphatase (EC 3.6.1.27) and is renamed UppP [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
AIILGIVQGLTEFLPISSTGHLIIVRHILGSGDAGKSFTIVIQLGSILAVVIYFWRRILRLLGIWIRFST
RKTESSDLLLLKLILLGLIPTVVLGLLFKDLIKSLLFNFLLTVVIALIVGAGLLILAEEVNRQTLKRDFE
RLTLRDAIMMGLFQCLALIPGVSRSGSTISGGLFIGLNRKAAAEFSFLLAIPIMFGAGLLSLKKSWDSFT
SGDFPELIVGFITAFVVALFAIAWFLKFLNKHSLYIFVIYRFILG
>gnl|CDD|162022 TIGR00754, Bacterioferritin_BFR., bacterioferritin. Bacterioferritin, predominantly an iron-storage protein restricted to Bacteria, has also been designated cytochrome b1 and cytochrome b-557.Bacterioferritin is a homomultimer most species. In Neisseria gonorrhoeae, Synechocystis PCC6803, Magnetospirillum magnetotacticum, and Pseudomonas aeruginosa, two types of subunit are found in a heteromultimeric complex, with each species having one member of each type. At present, both types of subunit are including in this single model [Transport and binding proteins, Cations and iron carrying compounds]
MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPN
LQDLGKLRIGETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLEL
IDKLGLENYLQAQVSEE
>gnl|CDD|273252 TIGR00755, Ribosomal_RNA_small_subunit_methyltransferase_A, ribosomal RNA small subunit methyltransferase A. In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]
FRPRKSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKL
LSLYNNLEIIEGDALKFDLNELAKDLTKVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAK
PGSKDYGRLSVLVQYYANVEIVFKVPPSAFYPPPKVDSAVVRLVPLKRKPSPKDFALFEELLKAAFQQRR
KTLRNNLKNLLSELVELLEELGIDPDKRVEQLSPEDFLRLANLL
>gnl|CDD|273253 TIGR00756, PPR, pentatricopeptide repeat domain (PPR motif). This model describes a domain called the PPR motif, or pentatricopeptide repeat. Its consensus sequence is 35 positions long and typically is found in four or more tandem copies. This family is strongly represented in plant proteins, particularly those sorted to chloroplasts or mitochondria. The pfam01535, domain of unknown function DUF17, consists of 6 copies of this repeat. This family has a similar consensus to the TPR domain (tetratricopeptide), pfam00515, a 33-residue repeat. It is predicted to form a pair of antiparallel helices similar to that of TPR
VTYNTLIDGLCKAGRVEEALELFKEMKERGIEPDV
>gnl|CDD|273254 TIGR00757, Ribonuclease_E/G-like_protein, ribonuclease, Rne/Rng family. This model describes ribonuclease G (formerly CafA, cytoplasmic axial filament protein A), the N-terminal domain of ribonuclease E in which ribonuclease activity resides, and related proteins. In E. coli, both RNase E and RNase G have been shown to play a role in the maturation of the 5' end of 16S RNA. The C-terminal half of RNase E (excluded from the seed alignment for this model) lacks ribonuclease activity but participates in mRNA degradation by organizing the degradosome [Transcription, Degradation of RNA]
TRVALVEGGRLFDLIIERPKSRQLKGNIYKGRVTRILPSLQAAFVDIGLEKNGFLHASDIGPNYECLAPA
EAKREAGPSISELLRPGQSVLVQVVKEPRGNKGARLTTDISLPGRYLVLMPNNSHVGVSRRIESGEERER
LKKLLRSEELPEGMGLIIRTAAEGASEEALIKDLEFLLRKWEKIKEKAQKRPAPCLIYGEPDIIKRVIRD
YLDTDVKEILIDSKEIYEEAKEFIQLYAPELVSKLKLYRGSDPLFEGFQIEKQIDKATQRKVWLPSGGYI
VIDQTEALTTIDVNSGRFTGGGNLEETALNTNLEAAKEIARQLRLRNLGGIIIIDFIDMKSEKNQRRVLE
RLKEALRRDRARIQISGISEFGLVEMTRKRLRESLMEVLGTVCPHCSGTGIVKTSESVLLEIER
>gnl|CDD|129841 TIGR00758, UDG_fam4, uracil-DNA glycosylase, family 4. This well-conserved family of proteins is about 200 residues in length and homologous to the N-terminus of the DNA polymerase of phage SPO1 of Bacillus subtilis. The member from Thermus thermophilus HB8 is known to act as uracil-DNA glycosylase, an enzyme of DNA base excision repair. Its appearance as a domain of phage DNA polymerases could be consistent with uracil-DNA glycosylase activity [DNA metabolism, DNA replication, recombination, and repair]
CRRCELHKTRTNAVPGDGNPDANIMFVGEAPGREEDRKGRPFVGRAGKLLDEMLAAIGLSRENVYITNVV
KCRPPNNRDPTPEEVEACAPYLVKQIELIRPKVIICLGRTAAQSILGKNDGITKIRGRVFEYRYIGTKIK
ITATYHPAALLRNPQLRRELEEDFKKLKELLSN
>gnl|CDD|273255 TIGR00759, Pyruvate_dehydrogenase_E1_component, pyruvate dehydrogenase E1 component, homodimeric type. Most members of this family are pyruvate dehydrogenase complex, E1 component. Note: this family was classified as subfamily rather than equivalog because it includes a counterexample from Pseudomonas putida, MdeB, that is active as an E1 component of an alpha-ketoglutarate dehydrogenase complex rather than a pyruvate dehydrogase complex. The second pyruvate dehydrogenase complex E1 protein from Alcaligenes eutrophus, PdhE, complements an aceE mutant of E. coli but is not part of a pyruvate dehydrogenase complex operon, is more similar to the Pseudomonas putida MdeB than to E. coli AceE, and may have also have a different primary specificity
SQPNDVDPIETQEWLESLDSVLAEEGPARARYLLEQLLEYAREHGVPIPAGTTTDYINTIPVEEQPAYPG
DLELERRIRSIIRWNAIAMVLRANKKDLGLGGHISTYASAATLYEVGFNHFFRGHSEGGGGDLVFFQGHA
APGIYARAFLEGRLTEEQLDNFRQEVQGDGLSSYPHPWLMPDFWQFPTVSMGLGPINAIYQARFMKYLEN
RGLKDTGDQKVWAFLGDGEMDEPESKGAITFAAREKLDNLTFVINCNLQRLDGPVRGNGKIIQELESLFR
GAGWNVIKVLWGSEWDALLARDTSGVLVKLMNETVDGDYQTYKAKDGAYVREHFFNRTPELKALVADMSD
ADIWALNRGGHDPRKVYAAYAAAQEHKGQPTVILAKTIKGYGMGDAAESRNTAHQVKKLEVDALKNFRDR
FELPLSDAQVEELPYYHPGEGSPEVRYLLARRQALGGYLPARRTFAEHLTVPALEFFGALLKGSGEREVS
TTMAFVRILNKLLKDKEIGKRIVPIVPDEARTFGMEGLFRQIGIYSPHGQTYTPVDADSLLAYKESKDGQ
ILQEGINEAGAMASWIAAATSYATHGEPMIPFYIYYSMFGFQRIGDLCWAAADQRARGFLLGATAGRTTL
NGEGLQHEDGHSLLQAATIPNCIAYDPAFAYEVAVIMEDGLRRMYGEQEDVFYYVTVMNENYVQPPMPEG
AEEGILKGLYRFETSTEEKAKGHVQLLGSGAIMRAVIEAAQLLAADWGVASDVWSVTSFTELARDGHDVE
RWNLLHPTETPRVSYVAQVLNEADAPVIASTDYVRAFAEQIRPYVPRKYVTLGTDGFGRSDTRENLRHFF
EVDAKSVVLAALYALADDGEIDGDVVADAIAKYGIDPDKANPVYR
>gnl|CDD|129843 TIGR00760, L-ribulose-5-phosphate_4-epimerase, L-ribulose-5-phosphate 4-epimerase. E. coli has two genes, sgaE and sgbE (YiaS), that are very close homologs of araD, the established L-ribulose-5-phosphate 4-epimerase of E. coli. SgbE, part of an operon for L-xylulose metabolism, also has L-ribulose-5-phosphate 4-epimerase activity; L-xylulose-5-phosphate may be converted into L-ribulose-5-phosphate by another product of that operon. The homolog to this family from Mycobacterium smegmatis is flanked by putative araB and araA genes, consistent with it also being araD [Energy metabolism, Sugars]
MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGS
KKPSSDTPTHLALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGE
YELETGKVIVETFEKRGIDPAQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPM
QQTLLDKHYLRKHGANAYYGQ
>gnl|CDD|273256 TIGR00761, Acetylglutamate_kinase, acetylglutamate kinase. This model describes N-acetylglutamate kinases (ArgB) of many prokaryotes and the N-acetylglutamate kinase domains of multifunctional proteins from yeasts. This enzyme is the second step in the "acetylated" ornithine biosynthesis pathway. A related group of enzymes representing the first step of the pathway contain a homologous domain and are excluded from this model [Amino acid biosynthesis, Glutamate family]
TIVIKIGGAAISDLLEAFASDIAFLRAVGIKPVIVHGGGPEINELLEALGIPPEFKNGLRVTDKETLEVV
EMVLIGQVNKELVALLNKHGINAIGLTGGDGQLFTARYLDKEDLGYVGEIKKVNKALIEALLKAGYIPVI
SSLALTAEGQALNVNADTAAGALAAALGAEKLVLLTDVPGILNGDGQSLISEIPLDEIEQLIKQGIIKGG
MIPKVNAALEALRGGVRSVHI
>gnl|CDD|273257 TIGR00762, DegV, EDD domain protein, DegV family. This family of proteins is related to DegV of Bacillus subtilis and includes paralogous sets in several species (B. subtilis, Deinococcus radiodurans, Mycoplasma pneumoniae) that are closer in percent identity to each than to most homologs from other species. This suggests both recent paralogy and diversity of function. DegV itself is encoded immediately downstream of DegU, a transcriptional regulator of degradation, but is itself uncharacterized. Crystallography suggested a lipid-binding site, while comparison of the crystal structure to dihydroxyacetone kinase and to a mannose transporter EIIA domain suggests a conserved domain, EDD, with phosphotransferase activity [Unknown function, General]
IAIVTDSTADLPPELIEEYDITVVPLTVIIDGKTYRDGVDITPEEFYEKLKESKELPKTSQPSPGEFLEL
YEKLLEEGDEVLSIHLSSGLSGTYQSARQAAEMVDEAKVTVIDSKSASMGLGLLVLEAAKLAEEGKSLEE
IVAKLEELRERTKLYFVVDTLEYLVKGGRISKAAALIGSLLNIKPILTVDDGKLVPIEKVRGRKKAIKKL
VELVKEDIKDGKPKRVAIIHADAEEEAEELKEKLKEKFPVKEILISEIGPVIGTHTGPGALGVAF
>gnl|CDD|273258 TIGR00763, Lon_protease, endopeptidase La. This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock [Protein fate, Degradation of proteins, peptides, and glycopeptides]
PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLGLFLQKDDDNEEPEEDDIYSVGVVAQILEM
LPLPSSGTATYKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEEPFDKDDEEIKALTREIKETFRELISLS
KLFREQPALLSALEDIDEPGRLADFVAASLQLKEKDELQEVLETVNIEKRLKKALELLKKELELLKLQNK
ITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLE
PSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPIL
CLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLL
DEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELS
GYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE
QGEKKKSEAESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLEL
TGQLGDVMKESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKP
VRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEV
LKKAF
>gnl|CDD|273259 TIGR00764, Archaeal_Lon_protease, lon-related putative ATP-dependent protease. This model represents a set of proteins with extensive C-terminal homology to the ATP-dependent protease La, product of the lon gene of E. coli. The model is based on a seed alignment containing only archaeal members, but several bacterial proteins match the model well. Because several species, including Thermotoga maritima and Treponema pallidum, contain both a close homolog of the lon protease and nearly full-length homolog of the members of this family, we suggest there may also be a functional division between the two families. Members of this family from Pyrococcus horikoshii and Pyrococcus abyssi each contain a predicted intein [Protein fate, Degradation of proteins, peptides, and glycopeptides]
GIKFETTEEIPVPERLIDQVIGQEEAVEIIKKAAKQKRNVLLIGEPGVGKSMLAKAMAELLPDEELEDIL
VYPNPEDPNMPRIVEVPAGEGREIVEDYKKKAFKQPSSRNLLLFMIGFIVLSEYFLKNLPPNYLLAAVIA
AALILLIFGFFIPRTSIMVPKLLVDNSGKKKAPFVDATGAHAGALLGDVRHDPFQGSGGLGTPAHERVEA
GAIHRAHKGVLYIDEIKTMPLEVQQYLLTALQDKKFPITGQSENSSGAMVRTEPVPCDFILVASGNLDDL
EGMHPALRSRIRGYGYEVYMKDTMPDTPENRDKLVQFVAQEVKKDGRIPHFTRDAVEEIVREAQRRAGRK
DHLTLRLRELGGLVRAAGDIAKSSGKVYVTAEHVLKAKKLAKTLEKQLADNYIERKKRYKVIVNEGGEVG
RVNGLAVIGEASGIVLPIKAIVAPAESKEEGRIIATGKLGEIAKEAVTNVSALIKKYTGEDISNYDIHIQ
FLQTYEGVEGDSASISVATAVISALEEIPVDQDVAMTGSLSVRGEVLPVGGVTEKIEAAIEAGIKKVIIP
KSNMIDVILEKETEGKIEIIPVETLDEVLEHVLDLDKKKGSLIERFNE
>gnl|CDD|273260 TIGR00765, tRNA_processing_ribonuclease_BN_RNase_BN., YihY family inner membrane protein. Initial identification of members of this protein family was based on characterization of the yihY gene product as ribonuclease BN in Escherichia coli. This identification has been withdrawn, as the group now finds the homolog in E. coli of RNase Z is the true ribonuclease BN rather than a strict functional equivalent of RNase Z. Members of this subfamily include the largely uncharacterized BrkB (Bordetella resist killing by serum B) from Bordetella pertussis. Some members have an additional C-terminal domain. Paralogs from E. coli (yhjD) and Mycobactrium tuberculosis (Rv3335c) are part of a smaller, related subfamily that form their own cluster [Unknown function, General]
AFLKFLWRRFDEDELFQYAGSLAFYTLLSLVPLLAVMFSLFAAFPVFQDVSGELEEFIFPNFAPSLGDMI
KDYIEQFVKNSNKLTAVGIVSLIVTALLLINNIDSTLNKIWRVKPRRSAIFSFAIYWTILTLGPLLLGVS
LAISSVVIFDVFAQSFFLSVNAALLSVVPLLFTWIFFWLLYTIVPNKKVKHRHAFVGAFFAAVLFELAKW
LFTFYVSTFATYQLIYGALAVLPFLMLWVYLSWLVVLLGAEITSSLDYF
>gnl|CDD|188082 TIGR00766, Uncharacterized_protein_Dda3937_02003, inner membrane protein YhjD. This family, including YhjD in E. coli, is a conserved inner membrane protein homologous YihY, which in turn was incorrectly assigned to be ribonuclease BN. This, any suggestion this family is similar to ribonucleases should be removed [Transcription, Degradation of RNA]
AHVIRAFTRFNDRNGNQFGAAITYFSFLSIIPILMVSFAVFALVSRRPELLTTLEERIRSSVSPALAQTL
KNTMNTAVDQRTTVGLIGLATALYSGLNWMGNLREAISDVWERPPAPAEKLRTKYLDDFASLIGLLVALV
ATLALTSVAGSAQVLIWLALPLFSVFDEIFRGISVLVSVLVSWVLFTWMPREPVRLVTLARGTLMAAIGF
ELFKQVMTIYLPILLRSPSGAAFGSVLGLMVFFYFFARLTLFCAAWIATASAK
>gnl|CDD|162030 TIGR00767, Transcription_termination_factor_Rho, transcription termination factor Rho. This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding [Transcription, Transcription factors]
YNIEELKNMPLEELRKLAEQLGVENTSSLKKQELIFAILKAHAEQGGLIFGEGVLEILPDGFGFLRSPDS
SYLPGPDDIYVSPSQIRRFNLRTGDTIEGQIRSPKEGERYFALLKVESVNGDDPEKAKNRVLFENLTPLY
PNERLRLETSTEDLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLLIDERP
EEVTDMQRSVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGK
VLSGGVDANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLADRR
IFPAIDIKKSGTRKEELLLTPEELQKIWVLRKIISPMDSIEAMEFLISKLKKTKTNEEFLESMKR
>gnl|CDD|273261 TIGR00768, Tetrahydromethanopterin:alpha-L-glutamate_ligase, alpha-L-glutamate ligase, RimK family. This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001)
KIAILYDRIRLDEKMLKEAAEELGIDYKVVTPPAINLTFNEGPRALAELDVVIVRIVSMFRGLAVLRYLE
SLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVS
LARDRQAAESLLEHFEQLNGPQNLFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRITSGHWRSNLARGGKA
EPCSLTEEIEELAIKAAKALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI
>gnl|CDD|273262 TIGR00769, ADPATP_carrier_protein_1, ADP/ATP carrier protein family. These proteins are members of the ATP:ADP Antiporter (AAA) Family (TC 2.A.12), which consists of nucleotide transporters that have 12 GES predicted transmembrane regions. One protein from Rickettsia prowazekii functions to take up ATP from the eukaryotic cell cytoplasm into the bacterium in exchange for ADP. Five AAA family paralogues are encoded within the genome of R. prowazekii. This organism transports UMP and GMP but not CMP, and it seems likely that one or more of the AAA family paralogues are responsible. The genome of Chlamydia trachomatis encodes two AAA family members, Npt1 and Npt2, which catalyse ATP/ADP exchange and GTP, CTP, ATP and UTP uptake probably employing a proton symport mechanism. Two homologous adenylate translocators of Arabidopsis thaliana are postulated to be localized to the intracellular plastid membrane where they function as ATP importers [Transport and binding proteins, Nucleosides, purines and pyrimidines]
IEVHELKKFLPLFLMFFCILFNYTILRDTKDTLVVTAKGSGAEIIPFLKTWVVVPMAVIFMLIYTKLSNI
LSKEALFYTVISPFLGFFALFAFVIYPLSDLLHPTALADKLLSLLPPGFMGFIAILRIWSFALFYVMAEL
WGSVVLSLLFWGFANQITTIDEAKRFYALFGLGANVALIFSGRTIKYFSKLRASLGPGVDGWHVSLKNLM
VIVICSGLAIILLYWWVNRNVLTDPRSYNPALKEKKVKPKMSTMESLKFLVSSPYILDLALLVIAYGISI
NLVEVTWKSKLKAQYPSPNEYSAFMGDFSTWTGVVSVTMMLLSGNVIRKYGWLTAALITPLVMLLTGVAF
FSLIFFGGPAAPLVAKLGMTPLLLAVYVGAIQNILSKSTKYSLFDATKEMAYIPLDEEQKVKGKAAIDVV
AARLGKSGGALIQQGLLVIFGSLAASTPYLAVILLIIVTAWLAAAKSLNKEF
>gnl|CDD|273263 TIGR00770, Anaerobic_C4-dicarboxylate_transporter_DcuA, anaerobic c4-dicarboxylate membrane transporter family protein. These proteins are members of th C4-Dicarboxylate Uptake (Dcu) Family (TC 2.A.13). Most proteins in this family have 12 GES predicted transmembrane regions; however one member has 10 experimentally determined transmembrane regions with both the N- and C-termini localized to the periplasm. The two Escherichia coli proteins, DcuA and DcuB, transport aspartate, malate, fumarate and succinate, and function as antiporters with any two of these substrates. Since DcuA is encoded in an operon with the gene for aspartase, and DcuB is encoded in an operon with the gene for fumarase, their physiological functions may be to catalyze aspartate:fumarate and fumarate:malate exchange during the anaerobic utilization of aspartate and fumarate, respectively [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
QIIIVLLCIFLGARLGGIGLGYAGGLGVLILCFGFGLKPGKIPFDVILIIMAVIAAIAAMQAAGGLDYLV
QIAEKLLRRNPKYITILAPSVTYFLTILAGTGHVVYSTLPVIAEVAKEQGIKPERPLSLAVVSSQIAITA
SPVSAAVVFMSAILEPLGIEYLDLLMVTIPSTFLGCMLTAFFVNFFGKKLDKDPEYQERLKAGKIVPTRG
KKEKETSKSAKLSVWIFLGGVVAVVLYAAAISKRPGFVGKPILGMDHAIVMFMLSVATLIIIFCKIDTDA
ILKSSVFKSGMQACICVLGVAWLGDTFVSNHIDEIKGYAGELIEGYPWLLAVALFLASMLLYSQAATAKA
LIPVALALGVSPYTIVASFAAVSGLFVLPTYPTLLAAIQMDDTGTTKIGKFVFNHSFIIPGLLGVSLSVA
LGFVVAPLVL
>gnl|CDD|129854 TIGR00771, Putative_cryptic_C4-dicarboxylate_transporter_DcuD, c4-dicarboxylate anaerobic carrier family protein. These proteins are members of the C4-dicarboxylate Uptake C (DcuC) Family (TC 2.A.61). The only functionally characterized member of this family is the anaerobic C4-dicarboxylate transporter (DcuC) of Escherichia coli. DcuC has 12 GES predicted transmembrane regions, is induced only under anaerobic conditions, and is not repressed by glucose. It may therefore function as a succinate efflux system during anaerobic glucose fermentation. However, when overexpressed, it can replace either DcuA or DcuB in catalyzing fumarate-succinate exchange and fumarate uptake [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
GYLIVDIYNEILRMLSNRIAGLGLSIMAVGGYARYMERIGASRAMVSLLSRPLKLIRSPYIILSATYVIG
QIMAQFITSASGLGMLLMVTLFPTLVSLGVSRLSAVAVMASPGSIHSAMISEMSGLAAQQVNMSHAPYNF
HYMLPGAIGAIILTAIAHFFKQRGEDKKQAYIAHEKESEIKVIEGVPVLYAILPLIPLIILLLFIGGTGL
QQVPLHEWTKMGVPQAMLIGAEFGRIVNRISPVKITEEFFNGMGNSFANVVGLIVAASVFAAGLKTIGAV
DAAISFAKESGLGNIFVMWGATIGPFLMALITGSGNAPFIAFNTAIPPHAVELGYTHVNLGMPMAIAGAL
GRTASPIAGVVVVCAGLAMVSPFEVVKRTAPPMIVGVV
>gnl|CDD|273264 TIGR00773, Na+/H+_antiporter_NhaA, Na+/H+ antiporter NhaA. These proteins are members of the NhaA Na+:H+ Antiporter (NhaA) Family (TC. 2.A.33). The Escherichia coli NhaA protein probably functions in the regulation of the internal pH when the external pH is alkaline. It also uses the H+ gradient to expel Na+ from the cell. Its activity is highly pH dependent. Only the E. coli protein is functionally and structurally well characterized [Transport and binding proteins, Cations and iron carrying compounds]
FFKSESAGGILLVIAAALAMVMANSALSEWYHDFLHTPVQLQIGSFVIGKSLLHWINDGLMAVFFLLIGL
EVKRELLEGALSSLRQAIFPVIAAIGGMIAPALIYLAFNANDPITREGWAIPAATDIAFALGVMALLGKR
VPLALKIFLLALAIIDDLGAIVIIALFYTNDLSMAALLVAAVAIAVLAVLNRCGVRRLGPYMLVGVILWF
AVLKSGVHATLAGVIIGFFIPLKGKKGESPLKRLEHVLHPWVAYLILPLFAFANAGVSLQGVSLNGLTSM
LPLGIILGLLIGKPLGIFLFSWIAVKLKLAKLPEGINFKQIFAVGVLCGIGFTMSIFIASLAFGSVDPEL
ITWAKLGILLGSTTSAVLGYSWL
>gnl|CDD|129856 TIGR00774, Na+/H+_antiporter_2_Sodium/proton_antiporter_2., Na+/H+ antiporter NhaB. These proteins are members of the NhaB Na+:H+ Antiporter (NhaB) Family (TC 2.A.34). The only characterised member of this family is the Escherichia coli NhaB protein, which has 12 GES predicted transmembrane regions, and catalyses sodium/proton exchange. Unlike NhaA this activity is not pH dependent [Transport and binding proteins, Cations and iron carrying compounds]
MEISLGNAFIKNFLGKSPDWYKLAIIAFLIINPIVFFLISPFVAGWLLVAEFIFTLAMALKCYPLQPGGL
LAIEAIAIGMTSAAHVKHELVANIEVLLLLVFMVAGIYFMKQLLLFIFTKLLLGIRSKTLLSLAFCFAAA
FLSAFLDALTVVAVVISVAVGFYGIYHKVASGNPIGDHDHTDDDTITELTRDDLENFRAFLRSLMMHAGV
GTALGGVMTMVGEPQNLIIADQAGWLFGEFFLRMSPVTLPVFICGLLTCALVEKLKVFGYGEKLPDNVRQ
ILVDFDREERKTRTNQDKIKLWVQALIAVWLIVALALHLAAVGLIGLSVIILATSFTGVTDEHSIGKAFE
ESLPFTALLAVFFSVVAVIIDQELFSPIIDFVLAAEEKTQLALFYVFNGLLSSISDNVFVGTVYINEAKA
ALTEGLITREQFELLAVAINTGTNLPSVATPNGQAAFLFLLTSALAPLIRLSYGRMVYMALPYTIVLAIV
GLLGIEFFLEPATAWFYDAGWILPH
>gnl|CDD|129857 TIGR00775, CT857_hypothetical_protein, Na+/H+ antiporter, NhaD family. These proteins are members of the NhaD Na+:H+ Antiporter (NhaD) Family (TC 2.A.62). A single member of the NhaD family has been characterized. This protein is the NhaD protein of Vibrio parahaemolyticus which has 12 GES predicted transmembrane regions. It has been shown to catalyze Na+/H+ antiport, but Li+ can also be a substrate [Transport and binding proteins, Cations and iron carrying compounds]
MLKFQLCLLFLFGYLTIVFEHIVRVNKSAIWLAMGGLMWLVCFSHIPDVDHAALEEEIADMAQVIFFLFV
AMAIVELIDAHKGFSALVAWCVGKSRKKLLWLLGFLSFFLSAALDNLTSIIIIISILKRLVKAREDRLLL
GAICVIAVNAGGAWTPLGDVTTTMLWINGKIRFSGIIMPLFVPSLVCVVVAGFCGQLFLPKRKPNTIHED
VELKRALPKSRRIVLLGVGSLLMVPSWKAVLGFPPFMGALLGLGLVWLFSDWIHSPHGEKRLHLRVPHIL
TRIDISSLTFFIGILLAVNALSLLGYLEDVSNVMDTQFSRNWAAVMVGLLSSVLDNVPLVAATLGMYPLP
MSDGLWKLIAYTAGTGGSILIIGSAAGVALMGAEKVQFTWYFKHLSWIALASYFGGLVLYFICENVSLFV
>gnl|CDD|273265 TIGR00776, L-rhamnose-proton_symporter, RhaT L-rhamnose-proton symporter family protein. These proteins are members of the L-Rhamnose Symporter (RhaT) Family (TC 2.A.7). This family includes two characterized members, both of which function as L-rhamnose:H+ symporters and have 10 GES predicted transmembrane domains [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MDILIALIPALFWGSFVLINVKIGGGPYSQTLGTTFGALILSIAIAIFVLPEFWALSIFLVGLLSGAFWA
LGQINQFKSMRYMGVSKTMPISTGFQLVGGTLFGVIVFGEWSTSIQTLLGLLALILIIIGVYLTSRSKDK
SAGIKSEFNFKKGILLLLMSTIGYLVYVVVAKAFGVDGLSVLLPQAIGMVIGGIIFNLGHILAKPLKKYA
ILLNILPGLMWGIGNFFYLFSAQPKVGVATSFSLSQLGVIISTLGGILILGEKKTKREMIAISVGIILII
IAANILGIGK
>gnl|CDD|129859 TIGR00777, AhpD_protein., alkylhydroperoxidase, AhpD family. Members of this family are alkylhydroperoxidases, which catalyze the reduction of peroxides to their corresponding alcohols via oxidation of cysteine residues. In these alkylhydroperoxidases, the cysteines are located in a conserved -CXXC- motif located towards the COOH terminus. In Mycobacterium tuberculosis, two non-homologous alkylhydroperoxidases, AhpD and AhpC, are found in the same operon [Cellular processes, Detoxification]
SIEKLKAALPDYAKDLKLNLSSITRSSVLDQEQLWGTLLASAAATRNPQVLRDIGAEATAHLSAEARHAA
LGAAAIMAMNNVFYRGRHLLEGARYDDLRPGLRMNIIANPGIPKVNFELWSFAVSAINGCGHCLDSHEHT
LRTVGVDREAIQEALKIAAVVSAVAQTLAAEAALSPS
>gnl|CDD|273266 TIGR00778, Uncharacterized_protein_H16_B0147, alkylhydroperoxidase AhpD family core domain. This model represents a 51-residue core region of homology among a family of mostly uncharacterized proteins of 110 to 227 amino acids. Most members of this family contain the motif EXXXXXX[SA]XXXXXC[VIL]XCXXXH. Members of the family include the alkylhydroperoxidase AhpD of Mycobacterium tuberculosis, a macrophage infectivity potentiator peptide of Legionella pneumophila, and an uncharacterized peptide in the tetrachloroethene reductive dehalogenase operon of Dehalospirillum multivorans. We suggest that many peptides containing this domain may have alkylhydroperoxidase or related antioxidant activity [Unknown function, General]
GALDAATKELIAIAVSQINGCGYCLDAHTKLARKAGVTREELAEALAWAA
>gnl|CDD|129861 TIGR00779, quaternary_amine_transporter, cadmium resistance transporter (or sequestration) family protein. These proteins are members of the Cadmium Resistance (CadD) Family (TC 2.A.77). To date, this family of proteins has only been found in Gram-positive bacteria. The CadD family includes several closely related Staphylococcal proteins reported to function in cadmium resistance. Members are predicted to span the membrane five times; the mechanism of resistance is believed to be export but has also been suggested to be binding and sequestration in the membrane. Closely related but outside the scope of this model is another staphylococcal protein that has been reported to possibly function in quaternary ammonium ion export. Still more distant are other members of the broader LysE family (see Vrljic. et al, ) [Transport and binding proteins, Amino acids, peptides and amines]
YIATGVDLLVILLIFFARAKRKEYKDIYIGQYLGSIILILVSLLLAFGVNLIPEKWVLGLLGLIPIYLGI
KVAIKGECDEDERAILSLNESGKLNKLFLTVAFITIASGADNIGIYVPYFVTLSMTNLLLTLIVFLIMVF
FLCFTAYRLANFPGISETVEKYSRWIMPIVFIGLGIYIIIENDTIQALLSFIF
>gnl|CDD|129862 TIGR00780, ccoN, cytochrome c oxidase, cbb3-type, subunit I. This model represents the largest subunit, I, of the ccb3-type cytochrome c oxidase, with two protohemes and copper. It shows strong homology to subunits of other types of cytochrome oxidases. Species with this type, all from the Proteobacteria so far, include Neisseria meningitidis, Helicobacter pylori, Campylobacter jejuni, Rhodobacter sphaeroides, Rhizobium leguminosarum, and others. Gene symbols ccoN and fixN are synonymous [Energy metabolism, Electron transport]
LSYDYSVVRLFLIATVGWGIVGMLVGVVLAFQLSFPALNLSDIAGEYGIFGRLRPLHTNAVIFAFGGGGL
IATSYYVVQRTYHQRLFGGIVGLFHFWGWQILIVLAVISLFAGLTQSKEYAELEWPLDIIVTVVWVLYGV
VFFGTISKRKENHIYVANWFYIAFIVGIAVLHIVNNLSIPTYLVAWKSISMYSGSNDAMIQWWYGHNAVG
FFLTAGFLGMMYYFLPKQAGRPVYSYKLSLFHFWALIFVYIWAGPHHLHYTALPDWVQTLGMVFSVILIL
PSWGGMINGLMTLSGAWDKLRTDPIIKFLVVASTFYGMSTFEGPMMSIKSVNALSHYTDWTIGHVHDGAL
GWVGFTTIGSMYYMTPRLFGRERIYSTRLVDFHFWIATIGIVLYFASMWIAGIMQGLMWRDVDQYGNLTY
QFIDTVKVLIPYYVIRGVGGLLYLIGFIIMAYNIFMTITAGKKLEREPNAVTPM
>gnl|CDD|129863 TIGR00781, cytochrome_oxidase_component_FixO, cytochrome c oxidase, cbb3-type, subunit II. This model describes the monoheme subunit of the cbb3-type cytochrome oxidase, found in a subset of Proteobacterial species. Species having this protein also have CcoN (subunit I, containing copper and two heme groups), CcoP (subunit III, containing two hemes), and CcoQ (essential for incorporation of the prosthetic groups) [Energy metabolism, Electron transport]
HQFLEKNATLLLVFFLLVVSIGGLVEIAPLFFLSNTIEPVEGLRPYTPLELAGRDIYIREGCYHCHSQMI
RPFRAEVERYGHYSLAGESMYDHPFQWGSKRTGPDLARVGGRYSDEWHVKHLFDPRSVVPESIMPAYKHL
ATKKVDVDTAYAEAKTQKKVGVPYDDEMIAKAGADEEAQKDPNADAKKLTADYKDKRVLEAFDGGPLTEM
DALVAYLQSLGTSVDNSTQNAK
>gnl|CDD|129864 TIGR00782, di-heme_cytochrome_cp, cytochrome c oxidase, cbb3-type, subunit III. This model describes a di-heme subunit of approximately 26 kDa of the cbb3 type copper and heme-containing cytochrome oxidase [Energy metabolism, Electron transport]
KDPKSQGEVQTTGHEWDGIEEYDNPLPRWWLWTFYATIVWGFGYLVAYPAWPLVSGATKGLLGWSSRSQV
EEEIKKFNEKNAAKWAKLAQTPLEDIAKDPELKQYARNAGAAIFRTWCAQCHGSGAGGAKGFPNLLDNDW
LWGGTLEGIHTTIKHGIRDPDDGDTYVGEMPAFGPLLEEADIKDVASYVMSLSSGKPKDEALAAKGQELF
ADNCTTCHGEDGKGLQELGAPNLTDDVWLYGGDLKTITTTITNGRGGVMPAWGPRLSEAQIKALAAYVHS
LGGGQ
>gnl|CDD|129865 TIGR00783, Citrate-sodium_symporter, citrate carrier protein, CCS family. These proteins are members of the Citrate:Cation Symporter (CCS) Family (TC 2.A.24). These proteins have 12 GES predicted transmembrane regions. Most members of the CCS family catalyze citrate uptake with either Na+ or H+ as the cotransported cation. However, one member is specific for L-malate and probably functions by a proton symport mechanism [Unclassified, Role category not yet assigned]
AILVFYNILPQNVIDATSNFMKGSNFLYLYIACLIVGSILGMNRKLLLKALMRFIPPALIGMVLAVIVGI
LVGTLFGLGFDHSLMYIVMPIMAGGVGAGIVPLSIIYSAITGRSSEEIFSQLIPAVIIGNIFAIICAGLL
SRIGKKRPKLNGHGELVRSEKREDAEKAKEITEIKIDVKLMGSGVLFAVALFMAGGLLKSFPGIPAYAFM
ILIAAALKAFGLVPKEIEEGAKMLSQFISKNLTWPLMVGVGVSYIDLDDLVAALSWQFVVICLSVVVAMI
LGGAFLGKLMGMYPVESAITAGLCNSGMGGTGDVAVLSASNRMNLIPFAQISTRLGGAITLVIAGIL
>gnl|CDD|162036 TIGR00784, Mg2+/citrate_complex_secondary_transporter, citrate transporter, CitMHS family. This family includes two characterized citrate/proton symporters from Bacillus subtilis. CitM transports citrate complexed to Mg2+, while the CitH apparently transports citrate without Mg2+. The family also includes uncharacterized transporters, including a third paralog in Bacillus subtilis [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MLAILGFSMMTVFMILIMTKRLSPLVALTITPIVFALIGGFGKGIGDMMIEGIQTVAPTAAMLLFAILYF
GIMIDAGLFDPLIEKILSIVKGDPLKIAVGTAVLTMLIALDGDGTTTYMITVSAMLPLYKRLGMNPMVLA
GIAMLGLGIMNMIPWGGPTTRAISVLGLDPSEFFVPLIPTMLGGILCVIAVAYLLGKKERKRLGVIQLEP
RASQSYPAAALESELKRPRLIWFNLLLTISLMVFLVLGTKHLSVLFLIAFVLALTVNYPNVKMQKERIAA
HSGNALTVVSMVFAAGVFTGILSGTKMVDAMAGSLVSIIPSSMGGFFPVIVALTSIPFTFVMSNDAYYFG
VLPIFAEAASAYGIDPVEIARASIMGQPVHLLSPLVPSTVLLVGMLGVSLGDHQKFAVKWAVITSIVMTL
LALLIGAISIL
>gnl|CDD|273267 TIGR00785, Uncharacterized_transporter_HI_0020, anion transporter. The Divalent Anion:Na+ Symporter (DASS) Family (TC 2.A.47) Functionally characterized proteins of the DASS family transport (1) organic di- and tricarboxylates of the Krebs Cycle as well as dicarboxylate amino acid, (2) inorganic sulfate and (3) phosphate. The animal NaDC-1 cotransport 3 Na+ with each dicarboxylate. Protonated tricarboxylates are also cotransported with 3Na+ [Transport and binding proteins, Anions, Transport and binding proteins, Cations and iron carrying compounds]
PVPDGLNSGAWLLLAIFVAAIVGWILEPLPLPVTALLAIPIIAVLLGVLSAFKFKNALSGFADPTIWLFF
GAFILATALVKTGLGKRIAYKLVGKMGGTTLGLGYFLVFLETLLAPMWPSNTARAGGILLPIIKSLLPLL
GSKPEKSPRKIGKYLMLGIAYSASIGSSGFLTGSAPNALAAGILSKILGIQISWGDWFLAGLPLGIILLL
LVPLLLYVLFPPELKLKDEVDLWAKEELEEMGPMSFREKALLGIFLLALLLWIFGGSLGINASVVALLAV
VLMLFLGIVTWKDIQKNKVAWNTLILFGGLIGLAGGLKKSGFIKWFSEKLVGILDGLSPTIAVLVLVVLF
YIILYFFASNTAHTAALVPIFFSVASAQGIPLELLALALALSASLMGFLTPYATPPNAIAYGSGYVKIKD
MWRVGAIIGIVGLIVLLLVGTLWW
>gnl|CDD|129868 TIGR00786, TRAP_transporter_permease_protein_SiaT, TRAP transporter, DctM subunit. The Tripartite ATP-independent Periplasmic Transporter (TRAP-T) Family (TC 2.A.56)- DctM subunit TRAP-T family permeases generally consist of three components, and these systems have so far been found in Gram-negative bacteria, Gram-postive bacteria and archaea. Only one member of the family has been both sequenced and functionally characterized. This system is the DctPQM system of Rhodobacter capsulatus (Forward et al., 1997). DctP is a periplasmic dicarboxylate (malate, fumarate, succinate) binding receptor that is biochemically well-characterized. DctQ is an integral cytoplasmic membrane protein with 4 putative transmembrane a-helical spanners (TMSs). DctM is a second integral cytoplasmic membrane protein with 12 putative TMSs. These proteins have been shown to be both necessary and sufficient for the proton motive force-dependent uptake of dicarboxylates into R. capsulatus [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
GVPVAFALGISALLLMFLLDGGDVDTIAQKLFGGTDSFTLLAIPFFILAGNLMNRGGLARRLLNFAKALV
GHLRGGLGHVNVLACALFAAVSGSSVATAAALGSLLIPAMTKAGYPKAFAAGVIAASGIIGPLIPPSIVM
IIYGVAAGVSIAKLFIAGILPGLLLALSLMLTIWWVARRLGYPRPPKASLRQRLRAFRKSIWALLLPVLI
IGGIFSGIFTPTEAAAVAAVYALALSTFVYRELTLKSLCDVLLESLRTTSMVMLIIAGATVFSWLLTHAQ
IPQRLADLLANAISSPIVFLIMINILLLIVGMFMDLTPAILILTPILLPVAVHLGIDPVHFGVMFVLNLE
IGLLTPPVGTNLFVASGVAKMSITEVTRALWPFLLAQFLVLLLVTYFPALSLALP
>gnl|CDD|129869 TIGR00787, Uncharacterized_protein_HI_1028, tripartite ATP-independent periplasmic transporter solute receptor, DctP family. TRAP-T (Tripartite ATP-independent Periplasmic Transporter) family proteins generally consist of three components, and these systems have so far been found in Gram-negative bacteria, Gram-postive bacteria and archaea. The best characterized example is the DctPQM system of Rhodobacter capsulatus, a C4 dicarboxylate (malate, fumarate, succinate) transporter. This model represents the DctP family, one of at least three major families of extracytoplasmic solute receptor for TRAP family transporters. Other are the SnoM family (see pfam03480) and TAXI (TRAP-associated extracytoplasmic immunogenic) family [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
FGHNAARSSPKHKAAEKFAKLVNEKTNGEIKISVFPSSQLGSDRAMLEALQGGALDMTAPSSSKFGPLVP
ELAVFDLPFLFRDYNHVHKVLDGEVGKALKKSLEKKGLKGLAYWDNGFRQFTSSKKPITKPEDLKGLKIR
IPNSPMNEAQFKALGANPEPMAFSEVYTALQTGVVDGQENPLSNVYSSKFYEVQKYLSMTNHGYLGYLVV
VNKAFWKSLPPDLQAVVKEAAKEAGEYQRKLSAEDEQKLIEKFKKQG
>gnl|CDD|273268 TIGR00788, hypothetical_protein, folate/biopterin transporter. The Folate-Biopterin Transporter (FBT) Family (TC 2.A.71)The only functionally characterized members of the family are from protozoa and include FT1, the major folate transporter in Leishmania, and BT1, the Leishmania biopterin/folate transporter. A related protein in Trypanosoma brucei, ESAGIO, shows weak folate/biopterin transport activity [Cell envelope, Other]
HPDSARLLRAAPFLGYIPVFSFHPRVVLAIGLQVLFVKGIAGLMRLPLSPMLTDDLGLDGARYQRLVGLS
SLGWALKPFAGVMSDTFPLFGYTKRWYLVLSGLLGSAILYGLLPGKVSSAKVAAAFIFLAALAKALYDVL
VDSLYSERIRESPSAGPSLVSWMWGASATGGLISSLLGGPLLDKTLTRILFLITAALLLLQLFVSNLSKE
RRAFVRPRIGTYLEMNMALLTLGVLANVKVQILGLRGAIQLLEIAKPLIFIFLSYANLPGASGSVFCATT
QCLPGGPSFSGMSKVVGNLGSLCGVGGYDRFLKTFPYRLLFGVTTLLYTLSSLFDLILVKRWNLAFGISD
EVFVLGDSIIAEVLAQLKFMPFLVLLARLCPSGCESSVFALLASILHLGSSVSGFLGVLLMETIGITCDN
SNNLWLLILGHSLAPLLPLPLLHLLPRLEDVIDTEGKRAISKAAPENR
>gnl|CDD|129871 TIGR00789, hypothetical_protein_Cj0848c, flhB C-terminus-related protein. This model describes a short protein (80-93 residues) homologous to the C-terminus of the flagellar biosynthetic protein FlhB. It is found so far only in species that also have FlhB. In a phylogenetic tree based on alignment of both this family and the homologous region of FlhB and its homologs, the members of this family form a monophyletic set [Unknown function, General]
KIKKAVALSYDTGKDKAPKVVASGVGEVAERIIEIAKKHGIPIVEDPDLVDVLLKLDLDDEIPEELYEVV
AEIFAFLYTQDN
>gnl|CDD|273269 TIGR00790, Probable_formate_transporter, formate/nitrite transporter. The Formate-Nitrite Transporter (FNT) Family (TC 2.A.44)The prokaryotic proteins of the FNT family probably function in the transport of the structurally related compounds, formate and nitrite. The homologous yeast protein may function as a short chain aliphatic carboxylate H+ symporter,transporting formate, acetate and propionate, and functioning primarily as an acetate uptake permease. The putative formate efflux transporters (FocA) of bacteria associated with pyruvate-formate lyase (pfl) comprise cluster I; the putative formate uptake permeases (FdhC) of bacteria and archaea associated with formate dehydrogenase comprise cluster II; the putative nitrite uptake permeases (NirC) of bacteria comprise cluster III, and the single yeast protein, the putative acetate:H+ symporter alone comprises cluster IV. The energy coupling mechanisms for proteins of the FNT family have not been extensively characterized. HCO2 -, CH3CO2 - and NO2 - uptakes are probably coupled to H+symport. HCO2 - efflux may be driven by the membrane potential by a uniport mechanism or by H+ antiport [Transport and binding proteins, Anions]
KAALSLLNLLVLSILAGAFIALGLVFYITGFTLINGAPPGLAKLVGGATFPIGLILVVIAGSDLFTGNTL
FVTMALLRGKISWGDLLINWVVSWLGNLVGALFVAYLFSYLGGILTAVDPWGVGSLALAEHKAHHTFVEL
FFLGILCNWLVCLAVWMSLSGKDLAGKFFAMWFPIFAFVASGFEHSVANMFLIPMGIFIGHFDLTVGQFI
GKNLIPVTLGNIIGGAVFVGLIYWYIYLK
>gnl|CDD|129873 TIGR00791, Gluconate_permease, gluconate transporter. This family includes known gluconate transporters of E. coli and Bacillus species as well as an idonate transporter from E. coli [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MPLVIVALGIVLLLLLIMKFKLNTFVALLVVSFGVGLASGMPLDKVVHSIEAGIGGTLGFLALIVGLGAM
LGKLLADSGAAQRIALTLLAKFGKSRVQWAVVIAGLIVGLALFFEVGFVLLIPLVFSIAAEAKISLLKLG
IPMVAALSVAHGFLPPHPGPTAIANEYGADIGEVLLYGLIVAIPTVIIAGPLFTKFLGRIVPPSPEASLG
SQKTFSEEEMPSFGISLFTALLPVILMAVKTIAELTLPKGSTAYEVVEFIGNPSTAMFIALLVAIYTLGI
RRGMPMDQVMDSCGSAIGSIAMILLIIGGGGAFKQVLIDSGVGDYIAELMSGMNISPILMAWLIAAILRI
ALGSATVAALTAAGLVAPLLGQYSGVNPALLVLATGAGSVIASHVNDAGFWLFKEYFGLTVKETLKTWTL
LETIISVVGLIGVLLLSLVL
>gnl|CDD|273270 TIGR00792, Melibiose_carrier_protein, sugar (Glycoside-Pentoside-Hexuronide) transporter. The Glycoside-Pentoside-Hexuronide (GPH):Cation Symporter Family (TC 2.A.2) GPH:cation symporters catalyze uptake of sugars in symport with a monovalent cation (H+ or Na+). Members of this family includes transporters for melibiose, lactose, raffinose, glucuronides, pentosides and isoprimeverose. Mutants of two groups of these symporters (the melibiose permeases of enteric bacteria, and the lactose permease of Streptococcus thermophilus) have been isolated in which altered cation specificity is observed or in which sugar transport is uncoupled from cation symport (i.e., uniport is catalyzed). The various members of the family can use Na+, H+ or Li, Na+ or Li+, H+ or Li+, or only H+ as the symported cation. All of these proteins possess twelve putative transmembrane a-helical spanners [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
KLSYGFGDFGNDFIFAIVSTYLLFFYTDVLGLSAAFVGTLFLVARILDAITDPIMGNIVDRTRTRWGKFR
PWLLIGAIPFSIVLVLLFTTPDFSGTGKLVYAYITYILLGLFYSFVNIPYWSLVPAITLDPRERESLSTF
RRFGATLGGLLVAVIVLPLVSYFGGGDDKFGWFMFALVLALIGVVSLIICFFGTKERYSEIPKNIEKKLS
LKQIFKALFKNDQLLILCLAYLFYNLAFNIKNGVQVYYFTYVLGDPELFSYMGSIAIVAGLIGVLLFPRL
VKKFGRKILFAGGILLMVLGYLIFFFAGSNLPLILVLIILAGFGQNIVTGLVWALVADTVDYGEWKTGIR
AEGLVYSVRTFVRKLGQALAGFFVGLILGIIGYVANAAQSPITLNGIKILMFAVPALFLLLAAIIIGRFY
KLTEKKHAEIVEELEQR
>gnl|CDD|273271 TIGR00793, 2-keto-3-deoxygluconate_permease, 2-keto-3-deoxygluconate transporter. This family includes the characterized 2-Keto-3-Deoxygluconate transporters from Bacillus subtilis and Erwinia chrysanthemi. There are homologs of this protein found in both gram-positive and gram-negative bacteria [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MHIKASIEKIPGGMMIIPLFLGAACHTFAPGAAEFFGGFTGALISGTLPILAVFFFCMGASIDFRASGTI
ARKGGTLLLGKIAFAALLAAIAAQFIPDDGIESGFFAGLSTLAIVAAMDETNGGLYAAIMNHMGRKEDAG
AFAFISLESGPFMTMVIFGTAGIAAFEPETFAAAVIPFLLGCALGNLDHDLRDFFSKAVPAIIPFFAFAL
GNTIDFGMIGQSGLLGIFIGISVIIISGIPLFLADKFIAGGDGTAGIAASSSAGAAVATPVAIAEANAAF
APVAEAATAIIATSVIVTSLLTPIATAMVDKKIK
>gnl|CDD|129876 TIGR00794, kup, potassium uptake protein. Proteins of the KUP family include the KUP (TrkD) protein of E. coli, a partially sequenced ORF from Lactococcus lactis, high affinity K+ uptake systems (Hak1) of the yeast Debaryomyces occidentalis as well as the fungus, Neurospora crassa, and several homologues in plants. While the E. coli KUP protein is assumed to be a secondary transporter, and uptake is blocked by protonophores such as CCCP (but not arsenate), the energy coupling mechanism has not been defined. However, the N. crassa protein has been shown to be a K+:H+ symporter, establishing that the KUP family consists of secondary carriers. The plant high affinity (20mM) K+ transporter can complement K+ uptake defects in E. coli [Transport and binding proteins, Cations and iron carrying compounds]
LAFQSLGVIYGDIGTSPLYVLSSTFSGGFPTERDIFGVLSLIFWLLTFIVSFKYIFIVLRADNNGEGGTF
ALYSLIGRYAKISARPVHQELDRAESSYSTKSPNLLNKTTSLKTKLELSKFISKFLVIFGLLGGSMVMGD
GVLTPAISVLSAVSGLEIVAPSLSDTWVVPISCIILVLLFLIQRFGTAKVGFTFAPIILVWLLLLAGIGI
YNIVKFNPEVLKALSPYYAVQFFIEYGTVGWVSLGGVVLSITGVEAMFADLGHFGKLPIQLAWFTFVYPS
LILCYIGQAAYLSKHPEAIKNPFFLSIPDWALWPLFIIATLAAIIASQAVISGVFSITSQAVRLGCFPRV
KIIHTSEKYHGQIYIPFVNWLLMLGVIAVTAGFRDTNNLGAAYGIAVTGTFLVTTCLMTVVMTIVWKWNI
YFVALFLLVFLSVELIYFSSNLDKVPEGGWFPLSLSGIFMSVMTTWRYGRFRKLRRDHEHRVSISALIAS
LQPKPGLVRVPGIGIYYSNLVNGIPAVFGHLVTKFPSIHEVFIFLSLRTLDAPTVHNEERVQISQVGPTE
GMYRCVIRYGFMDTPNEPKELAAHIVNSIVEFVEHECGFNLNNLEELSDKRCRMPIEEIFENAMETKEHG
YSYFMGEESLILKKRSPILRKIRVNHVFLFIRRNARRAPKVLEIPPDRLLEVGTVVEI
>gnl|CDD|162041 TIGR00795, L-lactate_permease, L-lactate transport. The Lactate Permease (LctP) Family (TC 2.A.14) The only characterized member of this family, from E. coli, appears to catalyze lactate:H+ uptake. Members of this family have 12 probable TMS [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MQVYDWLSAIVALLPILLFFFLLAVLKLKGYYAAPISVALSVIIALFYYKMPVIMTSAAFLYGFLYGLWP
IAWIIIAAIFLYKLSVKSGAFEIIRSSILSISPDRRIQVLLIGFCFGAFLEGAAGFGTPVAITAAILVGL
GFKPLYAAGLCLIANTAPVAFGAVGIPIWAGAQATGLSALEISSMTGFQLPFISLLIPFFLVFLMDGWKG
IKETFPAVLVAGLSFAIPQFLSSNYLGPELPSILGALVSLVITALFLKFWQPKEIFRFNGKLDAGEVSAH
HICKIVKAWSPFVLLTAFIVLWSIPPFKALFMKGGALIFSSFTFGSPGLSQHIFKLPPIVNQATNFPAVF
KLLLIIATGTSILLAAIVSFFILRVSISDAIGVFGETLKEMRLPILTIGMVLAFANVSNYSGMSKTLALA
LAHTGLAFTFFSPFLGWLGVFLTGSDTSSNLLFGSLQLLTAEQIGLPETLLLAANTVGGVMGKMISPQSI
AIACAAVGLVGQESDLFRKTVKYSLIYAIIVGVVALLLAY
>gnl|CDD|273272 TIGR00796, Branched-chain_amino_acid_transport_system, branched-chain amino acid uptake carrier. The Branched Chain Amino Acid:Cation Symporter (LIVCS) Family (TC 2.A.26) Characterized members of this family transport all three of the branched chain aliphatic amino acids (leucine (L), isoleucine (I) and valine (V)). They function by a Na+ or H+ symport mechanism and display 12 putative transmembrane helical spanners [Transport and binding proteins, Amino acids, peptides and amines]
GFMLFALFFGAGNIIFPPMLGLAAGEHVWTAALGFLLTGVGLPLLGLIALALVGGGYDSLSARIGKVFGI
LFTVILYLTIGPLFAIPRTATVSFEMGIAPLLHSPTSLLALFIFSLIFFAVVLLLSLNPSKLIDRVGKFL
TPALLVTLLALIIKALLWPAGPILAASGAYASQQAFSKGFLEGYLTMDALAALVFGIIVVNAIRSRGVTK
PKKITKYTIKAGLIAAVLLAFIYLSLFYLGATSAAAAGDAVNGAQILSAYSQHLFGSLGSFLLGLIITLA
CLTTAVGLTTACSEYFHKLVPKLSYKTWVIVFTLFSFIVANLGLTQIISISIPVLMIIYPLAIVLILLSF
LRKLWDSKRAVYQITLIVALLFSILDGL
>gnl|CDD|273273 TIGR00797, Multidrug_resistance_protein_HmrM, putative efflux protein, MATE family. The Multi Antimicrobial Extrusion (MATE) Family (TC 2.A.66) The MATE family consists of probable efflux proteins including a functionally characterized multi drug efflux system from Vibrio parahaemolyticus, a putative ethionine resistance protein of Saccharomyces cerevisiae, and the functionally uncharacterized DNA damage-inducible protein F (DinF) of E. coli. These proteins have 12 probable TMS [Transport and binding proteins, Other]
PAILANILQPLLGLVDTAFVGHLGPVDLAAVSLGSSVFMFLFSILMGLGTATTALVAQAVGAGNYQRLGR
QAQQSLLLALLLGLPVLLVGYFFIDPLLSLMGADGEVAELAQDYLRILILGIPAYLLNFVLRGFLRGQGD
TKTPMYITLIGNVINIILNYILIFGKFGFLGIVGAALATVISYWLMFLLLLYYIKKAKKIGLKWEGLLKP
DWEVLKRLLKLGLPIAFRVILESLSFALLALLVARLGSIALAAHQIALNVESLLFMPAFGFGIAVSILVG
QALGAGDPKRAKEVARVALKLSLLLGLVLAIILILFREFIARLFTNDPEVLELAAIYLIFVA
>gnl|CDD|129880 TIGR00798, Putative_sideroflexin-1.1, tricarboxylate carrier. The MTC family consists of a limited number of homologues, all from eukaryotes. A single member of the family has been functionally characterized, the tricarboxylate carrier from rat liver mitochondria. The rat liver mitochondrial tricarboxylate carrier has been reported to transport citrate, cis-aconitate, threo-D-isocitrate, D- and L-tartrate, malate, succinate and phosphoenolpyruvate. It presumably functions by a proton symport mechanism [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
PTFDISKPRWDQSTFLGRARHFFEITNPLTLFSSEKQLEKAREIVEDYKAGKASPLTVDELWRAKKLYDS
AFHPDTGEKMFLPGRMSAQVPMNMVITGGMLTPYRSTPGVVFWQWINQSFNAAVNYTNRSGDSPLTLSQL
LVSYCAAVTGACGVALGLNMMVKKSPSLSPLIGRLVPFAAVAVANAINIPMMRGNELTEGIEVFDEDGET
VGKSKKAAALAIAQVVLSRVIMAVPDMVMPPLIMNRLERTAWLRARPWMQIPIQTLLCGLGLAFATPLAC
ALFPQKSAISVDKLEPSLQNLIQKLGNPPKVVYYNKGL
>gnl|CDD|273274 TIGR00799, Lysosomal-associated_transmembrane_protein_4A, Golgi 4-transmembrane spanning transporter. The proteins of the MET family have 4 TMS regions and are located in late endosomal or lysosomal membranes. Substrates of the mouse MTP transporter include thymidine, both nucleoside and nucleobase analogues, antibiotics, anthracyclines, ionophores and steroid hormones. MET transporters may be involved in the subcellular compartmentation of steroid hormones and other compounds.Drug sensitivity by mouse MET was regulated by compounds that inhibit lysosomal function, interface with intracellular cholesterol transport, or modulate the multidrug resistance phenotype of mammalian cells. Thus, MET family members may compartmentalize diverse hydrophobic molecules, thereby affecting cellular drug sensitivity,nucleoside/nucleobase availability and steroid hormone responses [Transport and binding proteins, Unknown substrate]
RSDRVRQTCCCFNVRTATIALAIYHMVMSVLLFIEHTVEVAHGKNSCPAVNMQYLRIADLYSSFLLINAL
FIISVSLLMGVVKNREKYLYPFLSLQIMDFLLCLLTLLGSYIELPAYLKLARPRPGPSKIPLMTLQLLDF
CLSILTLCSSYMEVPTYLNFKSMNHMNYLPSQEDLPHLQFICMMFIFSVAFITVLIFKVYMFKCVWNCYK
YIKNMNSIAEYPASKMPPKVVLPSYEEALSLPEKTPEGDPAPPPYSEV
>gnl|CDD|273275 TIGR00800, Purine-cytosine_permease, NCS1 nucleoside transporter family. The Nucleobase:Cation Symporter-1 (NCS1) Family (TC 2.A.39) The NCS1 family consists of bacterial and yeast transporters for nucleobases including purines and pyrimidines. Members of this family possess twelve putative transmembrane a-helical spanners (TMSs). At least some of them have been shown to function in uptake by substrate:H+ symport mechanism [Transport and binding proteins, Nucleosides, purines and pyrimidines]
NEDLQPVKEEERTWSFLNYFSLWLGAAFNIATWAIGALGLPLGLSWWQSVIAIILGNLLGGIFVALNSRA
GAKYGLPFPVLSRASFGIYGSLLPSLLRIVMAIGWYGVQAWVGGLCVALMLDSIFPGYLHLGNGMTTLEL
ICFIIFWALVLVFLFFFGYKIRHLFEWLAVVPPFAAFGMLIWALSKAHGKGPLGELTGTLHGSTGAWAFL
YALSLVIGSFATWATNAPDFTRFGKSKKTAIWGQFLALPGGFTLTCFFGILGAAAAYAAYGEPYWSPLDI
LARFLGLTYAVGARAVFGFGFCFVVAQLSTNISANSYSAGLDIAALLPKYIKIKRGSLICAIIALLICPW
NLYNSSSKFTTFLSSIGGFLSPIAGVMIADYFVVRRGYLHLTTLYSDSKGEYYPGGIKGVNWRAVVAVIC
GLAPCLPGFVGEVGRDIGVLGG
>gnl|CDD|273276 TIGR00801, Uric_acid_permease, uracil-xanthine permease. The Nucleobase:Cation Symporter-2 (NCS2) Family (TC 2.A.40) Most of the functionally characterized members of the NCS2 family are transporters specific for nucleobases including both purines and pyrimidines. However, two closely related rat members of the family, SVCT1 and SVCT2, localized to different tissues of the body, cotransport L-ascorbate and Na+ with a high degree of specificity and high affinity for the vitamin. The NCS2 family appears to be distantly related to the NCS1 family (TC #2.A.39) [Transport and binding proteins, Nucleosides, purines and pyrimidines]
RPPLLQTIFLSLQHLLAMFAGAVLVPLLVGIALGLSAELQYLVSIALLTSGVGTLLQLFRTGGFIGLPSV
LGSSFAFIAPMIMIGSGLGVPAIYGALIATGLLYFLVSFIIKKLGPLLDRLFPPVVTGPVVMLIGLSLIP
VAIDNAAGGEGAATYGSLENLGLAFVVLALIILLNRFFKGFLKSISILIGILVGYILALAMGLVDFSPVI
EAPWFSLPTPFTFPPSFEWPAILTMLPVAIVTLVESIGDITATADVSGRDLSGDPRLHRGVLADGLATLI
GGLFGSFPNTTFAQNIGVIALTRVASRWVIVGAAVILIALGLVPKIAALITSIPSPVLGGAMLVMFGMVA
ASGIRILSRSKLDFRRNLLIIAASVGLGLGVTGVPDIFGNLPLLLLSGIALAGIVAILLNLI
>gnl|CDD|273277 TIGR00802, Hydrogenase_nickel_incorporation_protein_HupN, high-affinity nickel-transporter, HoxN/HupN/NixA family. This family is found in both Gram-negative and Gram-positive bacteria. The functionally characterized members of the family catalyze uptake of either Ni2+ or Co2+ in a proton motive force-dependent process. Topological analyses with the HoxN Ni2+ transporter of Ralstonia eutropha (Alcaligenes eutrophus) suggest that it possesses 8 TMSs with its N- and C-termini in the cytoplasm [Transport and binding proteins, Cations and iron carrying compounds]
ALLAYVLGLRHAFDADHIAAIDNTTRKLMQQGRRPLGVGFFFSLGHSTVVVLATVLIAVASALLTERLDG
LHEIGGLIGTLVSALFLLIIALLNLVILRNLLRLFRKVRRGIYDEADLEALLGNRGLLTRLLGPLFRLVT
KSWHMYPVGFLFGLGFDTATEVALLGLSASAAARGLSIAAVLSLPVLFAAGMALFDTADSLFMVGAYGWA
FSDPLRKLYYNITITGASVAVALFIGGIELLGLIANKLMLKGLFWLLIGALNENFENLGFAVVAAFVLTW
>gnl|CDD|129885 TIGR00803, UDP-N-acetylglucosamine_transporter_YEA4, UDP-galactose transporter. The 10-12 TMS Nucleotide Sugar Transporters (TC 2.A.7.10)Nucleotide-sugar transporters (NSTs) are found in the Golgi apparatus and the endoplasmic reticulum of eukaryotic cells. Members of the family have been sequenced from yeast, protozoans and animals. Animals such as C. elegans possess many of these transporters. Humans have at least two closely related isoforms of the UDP-galactose:UMP exchange transporter.NSTs generally appear to function by antiport mechanisms, exchanging a nucleotide-sugar for a nucleotide. Thus, CMP-sialic acid is exchanged for CMP; GDP-mannose is preferentially exchanged for GMP, and UDP-galactose and UDP-N-acetylglucosamine are exchanged for UMP (or possibly UDP). Other nucleotide sugars (e.g., GDP-fucose, UDP-xylose, UDP-glucose, UDP-N-acetylgalactosamine, etc.) may also be transported in exchange for various nucleotides, but their transporters have not been molecularly characterized. Each compound appears to be translocated by its own transport protein. Transport allows the compound, synthesized in the cytoplasm, to be exported to the lumen of the Golgi apparatus or the endoplasmic reticulum where it is used for the synthesis of glycoproteins and glycolipids
KLSVPIHIIFKQNNLVLIALGNLLAAGKQVTQLKILSTALMTLGSLVASLGDDQWFSLKLLKLGVAIVQM
VQSSAKTLMFGNPVVGLSAVLSALLSSGFAGVYFEKILKDGDTMFWSRNLQLPLFGLFSTFSVLLWSDGT
LISNFGFFIGYPTAVWIVGLLNVGGGLCIGGVVRYADNTTKSFVTALSIILSTLASVRLFDAKISSTFYL
GAILVFLATFLY
>gnl|CDD|273278 TIGR00804, Purine_nucleoside_transport_protein_NupG, nucleoside transporter. The Concentrative Nucleoside Transporter (CNT) Family (TC 2.A.41) Members of the CNT family mediate nucleoside uptake. In bacteria they are energized by H+ symport, but in mammals they are energized by Na+ symport. The different transporters exhibit differing specificities for nucleosides. The E. coli NupC permease transports all nucleosides (both ribo- and deoxyribonucleosides) except hypoxanthine and guanine nucleosides. The B. subtilis NupC is specific for pyrimidine nucleosides (cytidine and uridine and the corresponding deoxyribonucleosides). The mammalian permease members of the CNT family also exhibit differing specificities. Thus, rats possess at least two NupC homologues, one specific for both purine and pyrimidine nucleosides and one specific for purine nucleosides. At least three paralogues have been characterized from humans. One human homologue(CNT1) transports pyrimidine nucleosides and adenosine, but deoxyadenosine and guanosine are poor substrates of this permease. Another (CNT2) is selective for purine nucleosides. Alteration of just a few amino acyl residues in TMSs 7 and 8 interconverts their specificities [Transport and binding proteins, Nucleosides, purines and pyrimidines]
LISFVGLVVFILIAFLCSSNKKAISWRTVVSALVLQFLLGLIVLRTPPGFWAFQGLADQIQILLSYANEG
SSFVFGPPLVQDLFVFAFQVLPIIIFFSALISILYYLGIMQWVIRKIGWFLQKAMGTTKLESFSAAANIF
LGQTEAPLVIRPYLGDMTDSELFTVMTSGMATIAGSVLGAYISMGVPATYLIAASVMAAPCALAFAKLIY
PEVEESKEKSEEDVKLEEGDQNFFEAASNGALAGVKVVANVAAMLIAFVALLALINGILSWVGGWVGYGG
LSFQLIFGYVFRPLAFLMGVPWSDAPLVAQLMGTKLAVNEFVAYLDLSQYLQTRLWLSPKTEAIITFALC
GFANFSSIGIILGGLGSLVPKRKSVISRLVLRALCAGTLVSLMSATIAGLY
>gnl|CDD|273279 TIGR00805, oat, sodium-independent organic anion transporter. The Organo Anion Transporter (OAT) Family (TC 2.A.60)Proteins of the OAT family catalyze the Na+-independent facilitated transport of organic anions such as bromosulfobromophthalein and prostaglandins as well as conjugated and unconjugated bile acids (taurocholate and cholate, respectively). These transporters have been characterized in mammals, but homologues are present in C. elegans and A. thaliana. Some of the mammalian proteins exhibit a high degree of tissue specificity. For example, the rat OAT is found at high levels in liver and kidney and at lower levels in other tissues. These proteins possess 10-12 putative a-helical transmembrane spanners. They may catalyze electrogenic anion uniport or anion exchange
MGETEKDIATHESSAGLKPRPRCLQSLFSKIKMFSLLLTCARLQGLLVNGLVNSMLTSIERRFKIPTSRS
GFINGSYEIGNLLLIIFVSYFGTKLHRPIVIGAGCAIMGLGSLLSSLPHFLMGRYSYSTTVSSTGNLSSA
NSFLCMENLTQTLRPTQDPSECQKQHKSLMWLLFLVSNILRGIGATPIFPLGISYIDDFAKSKNSPLYIG
ILESGSVFGPAFGFLLGSFCLQIYVDTGSVNTEDLIITPTDPRWIGAWWIGFLVCGFVALLTSIPLFFFP
KTLPKEGKRVNVDVHEAEKLEKSRGEDRKKNSGITKDFPKFIKRLLCNKIYMLVILAQVIDVLAFNGYIT
FLPKYLENQYGISSAEANLLIGVVNVPPIGLGYLIGGFIMKKFKLNVKKAAYFAICLSTLEYLLYSPKFL
ITCESAPVAGVNNPSNDQPLYVENRTDCNRQCSCDSSIWDPVCGDNGLAYLSPCHAGCRMSVGTGSNMVF
TNCSCIQTPGNSSAKKGLCDPPCATSLQYFLILFIPLSFIYFITAVPGYMVLLRCVKSEERSLGLGLQWF
CIRVFGTIPAPILFGALIDVTCLHWQTLKCGASGACRMYDNDNLRVIYLGLTIALRGSSLLPLFFILILA
RK
>gnl|CDD|129888 TIGR00806, Folate_transporter_1, RFC reduced folate carrier. The Reduced Folate Carrier (RFC) Family (TC 2.A.48) Members of the RFC family mediate the uptake of folate, reduce folate, derivatives of reduced folate and the drug, methotrexate. Proteins of the RFC family are so-far restricted to animals. RFC proteins possess 12 putative transmembrane a-helical spanners (TMSs) and evidence for a 12 TMS topology has been published for the human RFC. The RFC transporters appear to transport reduced folate by an energy-dependent, pH-dependent, Na+-independent mechanism. Folate:H+ symport, folate:OH- antiport and folate:anion antiport mechanisms have been proposed, but the energetic mechanism is not well defined [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MVPTGQVAEKQACEEPRQDRELKSWRVLVLYLCFYGFMAQFRPGESFITPYLLTVLNFTEETVTNEIIPV
LPYSHLAVLVPVFLLTDYLRYKPVLVLQALSFVCVWLLLLLGTSVWHMQLMEVFYSVTMAARIAYSSYIF
SLVPPSRYQRAAAYSRAAVLLGVFLSSVLGQLLVTLGWISYSTLNIISLVFMTFSVFLALFLKRPKRSLF
FNRLEDVRGALPCELDQMVPGPGGKLEDYLGTCRDSFLVRMLSELVTIYRNPQLLLWSLWWVFNSAGYYL
ITYYVHTLWGTLDESLNKYNGAVDAASTLLGAITSFIAGFVNIRWARWSKLLIAVVSAIQAGLVFWMSQS
HDIWVLYVTYVLFRGIYQFLVPIATFQIASSLSKELCALVFGINTFVATALKTIITAVVSDKRGLGLQVR
KQFRIYSVYFLVLSIICFFGAGLDGLRYCKRGTHQPLAPAQELRSPLEESVQAISLQDRDLRGPQPSAPQ
LLPEDGTVEDDRADLRVEAKA
>gnl|CDD|129889 TIGR00807, malonate_carrier_protein_MdcL, malonate transporter, MadL subunit. The MSS family includes the monobasic malonate:Na+ symporter of Malonomonas rubra. It consists of two integral membrane proteins, MadL and MadM. The transporter is believed to catalyze the electroneutral reversible uptake of H+-malonate with one Na+, and both subunits have been shown to be essential for activity [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MIIYGVALLAVCHLLGVYLGNILGMALGVKANVGGVGIAMILLIISKELLAKRGHLPQVTQFGVGFWSAM
YIPIVVAMAAGQNVVAALSGGMLALLASVAALIVTVLVIRWISKSSYGTYEPAVE
>gnl|CDD|129890 TIGR00808, malonate_transporter, malonate transporter, MadM subunit. The MSS family includes the monobasic malonate:Na+ symporter of Malonomonas rubra. It consists of two integral membrane proteins, MadL and MadM.The transporter is believed to catalyze the electroneutral reversible uptake of H+-malonate with one Na+, and both subunits have been shown to be essential for activity [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MWEIVTAVLTKNGLITAFAVVGLMMYVSHLLSKYLTKGKLHGSAIAITMGLVLAYVGGVYTGGEKGLADI
AIFGGFGLMGGAMLRDLAIVATAFEVDVKEVKKAGKVGMVALLLGCVIPFVIGAMVAWAFGYRDAVSMTT
IGAGAVTYIVGPVTGAAVGASSEVIALSIAIGLIKAILVMVGTPLLAKFMYLDNPRSAMVFGGLAGTTSG
VTAGLAATDVRLVPYGALTATFYTGLGCLLGPSVLFLTVNGIFG
>gnl|CDD|213561 TIGR00809, Protein-export_protein_SecB, protein-export chaperone SecB. This protein acts as an export-specific cytosolic chaperone. It binds the mature region of pre-proteins destined for secretion, prevents aggregation, and delivers them to SecA. This protein is tetrameric in E. coli. The archaeal Methanococcus jannaschii homolog MJ0357 has been shown () to share many properties, including chaperone-like activity, and scores between trusted and noise [Protein fate, Protein and peptide secretion and trafficking]
EEAQPVFQIQRIYVKDLSFEAPNAPHIFQLDWRPEVDLDLDTNSTQLSDDFYEVVLNITVTARLEEYTAF
LCEVKQAGVFNIIGIESEQMAHCLGVHCPNMLFPYAREIISSCVQRGTFPPLNLAPVNFDALYMQQQMAE
>gnl|CDD|273280 TIGR00810, secG, protein translocase, SecG subunit. This family of proteins forms a complex with SecY and SecE. SecA then recruits the SecYEG complex to form an active protein translocation channel [Protein fate, Protein and peptide secretion and trafficking]
YTVLLILHIIVAILLIVLVLLQSGKGGGLGGAFGGGASQSLFGSRGAEKFLSRLTAVLAVLFFILSLALA
YLS
>gnl|CDD|273281 TIGR00811, silicon_transporter, silicon transporter. Marine diatoms such as Cylindrotheca fusiformis encode at least six silicon transport protein homologues which exhibit similar size and topology. One characterized member of the family (Sit1) functions in the energy-dependent uptake of either Silicic acid [Si(OH)4] or Silicate [Si(OH)3O-] by a Na+ symport mechanism. The system is found in marine diatoms which make their "glass houses" out of silicon [Transport and binding proteins, Other]
MVSVIDGIKQFYSMALVIFSVVIVTALMFTDNTKLAKDAHPVAALVIMWLGILWMSMVEGGQCSMVGLPP
IDRDLYKESHPITYKICSLGHKGNNLDRYLMGRQFMVIFINFTINLCGAPLEGAEVLGLPEILTDIFLGS
GIAMVLTVVTIGQLTAQVNASHCMLDYINTHFMTFTLYVTLIIEATGVMHSCYLIRDMFYHAAGKPVETN
EPPRSAVQNLFHWGRVVFSLGVLCFALAVTIEALFNGQTTMWEFIPNGVAIVLFILLMSVVGLLEGMQIA
FFAVAKIPKAERGDHPFARKTCELLFKGNGRNLPGFMVGRQMTVTLCFFIIARVTTLDIEVGVDDNIFGV
SDGIQEFFNLGFLGAIITTILASIAWQLVASAFPIAFLSNPIVYIVLRIVLLIEATGICAGAWFLGMIHK
KVAGFQLDEVYVGTAEERAAGEKPDHSVHAGREFTMGTNVLNDPANWEEAIANLSALETFSVRRERMLKN
IRELREMINNAISDEEKTTFEAALAIEVKALDKLNAEEEEEATNKKEGKDTEASA
>gnl|CDD|273282 TIGR00813, Sodium/glucose_cotransporter_1, transporter, SSS family. The Solute:Sodium Symporter (SSS) Family (TC 2.A.21) Members of the SSS family catalyze solute:Na+ symport. The solutes transported may be sugars, amino acids, nucleosides, inositols, vitamins, urea or anions, depending on the system. Members of the SSS family have been identified in bacteria, archaea and animals, and all functionally well characterized members catalyze solute uptake via Na+ symport. Proteins of the SSS generally share a core of 13 TMSs, but different members of the family may have different numbers of TMSs. A 13 TMS topology with a periplasmic N-terminus and a cytoplasmic C-terminus has been experimentally determined for the proline:Na+ symporter, PutP, of E. coli [Transport and binding proteins, Cations and iron carrying compounds]
AGRSLGGWVVAASLFASYISASQFLGLPGAIYAYGFAIGFYELGALVLLIILGWLFVPIFINNGAYTMPE
YLEKRFGKRILRGLSVLSLILYIFLYMSVDLFSGALLIELITGLDLYLSLLLLGAITILYTVFGGLKAVV
WTDTIQAVIMILGTFILPVFAFSEVGGLGTFVEKASQAAPTNPSPDDLYDFFRDPSTSDLPWGAGVFGLP
HVALWYWTNQVIVQRCLAAKSAKHAKKGCLISGVLKLLPMFGAVLPGLIARALYTDIDPALAGAVNQNSD
QAYPLLVQELMPPGLAGLFLAAILAAVMSTLSSQLNSASTVFTMDLYKKIIRPNASGEKKIVMRGRIAVL
VAAVIAGFVAAAQGGQVLQYVQEAFGGLGAPFLPVFLLGIFWKRMNAKGALAGMIAG
>gnl|CDD|273283 TIGR00814, membrane_transport_protein_YhjV, serine transporter. The Hydroxy/Aromatic Amino Acid Permease (HAAAP) Family- serine/threonine subfamily (TC 2.A.42.2) The HAAAP family includes well characterized aromatic amino acid:H+ symport permeases and hydroxy amino acid permeases. This subfamily is specific for hydroxy amino acid transporters and includes the serine permease, SdaC, of E. coli, and the threonine permease, TdcC, of E. coli.//added GO terms, none avaialbelf or ser/thr specifically [SS 2/6/05] [Transport and binding proteins, Amino acids, peptides and amines]
WTKTDTGWMLGLYGTAIGAGVLFLPIQAGLGGLWVLVLMAIIAYPLTYFGHRALARFLLSSKNPCEDITE
VVEEHFGKNWGILITLLYFFAIYPILLIYSVAITNDSASFLVNQLGTAPPLRGLLSLALILILVAIMSFG
EKLLFKIMGPLVFPLVLILVLLSLYLIPHWNGANLTTFPSFNGFLKTLWLTIPVMVFSFNHSPIISSFAI
SYREEYGDKEFAERKCLRIMKGASLILVATVMFFVFSCVLSLSPAEAVAAKEQNISILSYLANHFNAAWI
SYAGPIVAIVAISKSFFGHYLGAREGLNGIVLNSLKMKGKKINIRKLNRAIAIFIVLTTWIVAYINPSIL
SFIEALGGPIIAMILFLMPMYAIYKVPALKKYRGRISNVFVTVIGLL
>gnl|CDD|273284 TIGR00815, Sulfate_transporter, high affinity sulphate transporter 1. The SulP family is a large and ubiquitous family with over 30 sequenced members derived from bacteria, fungi, plants and animals. Many organisms including Bacillus subtilis, Synechocystis sp, Saccharomyces cerevisiae, Arabidopsis thaliana and Caenorhabditis elegans possess multiple SulP family paralogues. Many of these proteins are functionally characterized, and all are sulfate uptake transporters. Some transport their substrate with high affinities, while others transport it with relatively low affinities. Most function by SO42- :H+symport, but SO42- :HCO3- antiport has been reported for the rat protein (spP45380). The bacterial proteins vary in size from 434 residues to 566 residues with one exception, a Mycobacterium tuberculosis protein with 784 residues. The eukaryotic proteins vary in size from 611 residues to 893 residues with one exception, a protein designated "early nodulin 70 protein" from Glycine max which is reported to be of 485 residues. Thus, the eukaryotic proteins are almost without exception larger than the prokaryotic proteins. These proteins exhibit 10-13 putative transmembrane a-helical spanners (TMSs) depending on the protein. The phylogenetic tree for the SulP family reveals five principal branches. Three of these are bacterial specific as follows: one bears a single protein from M. tuberculosis; a second bears two proteins, one from M. tuberculosis, the other from Synechocystis sp, and the third bears all remaining prokaryotic proteins. The remaining two clusters bear only eukaryotic proteins with the animal proteins all localized to one branch and the plant and fungal proteins localized to the other. The generalized transport reactions catalyzed by SulP family proteins are: (1) SO42- (out) + nH+ (out) --_ SO42- (in) + nH+ (in). (2) SO42- (out) + nHCO3- (in) SO42- (in) + nHCO3- (out) [Transport and binding proteins, Anions]
PVLRWLRKYRLKKFKGDLMAGLTVGILLIPQAIAYAKLAGLPPIYGLYTSFVPPIIYALFGSSRHIAIGP
TASVSLLLGSLVQREGLQGLFDDYIRLAFTATLLAGIFQVIMGLLRLGFLIEYLSHAVLVGFTAGAAITI
GLSQLKGLLGLSIFVKTDILGVVISTWASLHQNNWCTLVIGLLFLLFLLATKELGKRNKKLLWAPAPAPL
LVVVLATLIVTIGLHDSQGVSIVGHIPQGLSFFPPITFTWQHLPTLAPDAIAIAIVGLTESILTARVFAA
MTGYEIDANKELVALGIANIVGSFFSCYPATGSLSRTAVNYKAGCKTQLSAIVMAIVVLLVLLVLAPLFY
YIPLAALAAIIISAAVGLIDIRELYLLWKADKMDFVVWLGTFLGVVFTSIEIGLLVGVSLSAFFFILRVA
RPRAAVLGRIPGTEDYENIEQYPKAQTPPGILIFRVDGPLYFANAEDLKERLLKWLETLELDPQIIILDM
SAVPFLDTSGIHALEELFKELKARGIQLLLANPNPAVISTLARAGFVELIGEEHFFPSVHDA
>gnl|CDD|273285 TIGR00816, Uncharacterized_transporter_MJ0762, C4-dicarboxylate transporter/malic acid transport protein. The Tellurite-Resistance/Dicarboxylate Transporter (TDT) Family (TC 2.A.16)Two members of the TDT family have been functionally characterized. One is the TehA protein of E. coli which has been implicated in resistance to tellurite; the other is the Mae1 protein of S. pombe which functions in the uptake of malate and other dicarboxylates by a proton symportmechanism. These proteins exhibit 10 putative transmembrane a-helicalspanners (TMSs) [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
FPWGWFAIVLGTGGLALASLSYSFYLPILKDLSDVLFILAIALFFLFTSCWLARLIRYPSNVLAELKHPV
LSSFIPLIPISTMLLGIDFIIWGYPLALGLWYIGAIGQLLFSVIVPFYLFKNESIEIEHTHPGWYLPPVA
LIFISAAALAILPYLTHELTVLFYFGWGAGFFLYLSLEAVLLLRLRLHGLLPSALRPTMFINLAPIGVGI
VALINIVNHGEFITIKEPFLILAIILWGFGLWQLLFAIRLLLWYVKLKLPFAMGWWAFIFPLAAYANSTH
LVYKGFDFKVFQYIGFGLYVFLNFFWAILLIRTVNKLYVG
>gnl|CDD|129898 TIGR00817, Triose_phosphate/phosphate_translocator, Tpt phosphate/phosphoenolpyruvate translocator. The 6-8 TMS Triose-phosphate Transporter (TPT) Family (TC 2.A.7.9)Functionally characterized members of the TPT family are derived from the inner envelope membranes of chloroplasts and nongreen plastids of plants. However,homologues are also present in yeast. Saccharomyces cerevisiae has three functionally uncharacterized TPT paralogues encoded within its genome. Under normal physiologicalconditions, chloroplast TPTs mediate a strict antiport of substrates, frequently exchanging an organic three carbon compound phosphate ester for inorganic phosphate (Pi).Normally, a triose-phosphate, 3-phosphoglycerate, or another phosphorylated C3 compound made in the chloroplast during photosynthesis, exits the organelle into thecytoplasm of the plant cell in exchange for Pi. However, experiments with reconstituted translocator in artificial membranes indicate that transport can also occur by achannel-like uniport mechanism with up to 10-fold higher transport rates. Channel opening may be induced by a membrane potential of large magnitude and/or by high substrateconcentrations. Nongreen plastid and chloroplast carriers, such as those from maize endosperm and root membranes, mediate transport of C3 compounds phosphorylated atcarbon atom 2, particularly phosphenolpyruvate, in exchange for Pi. These are the phosphoenolpyruvate:Pi antiporters (PPT). Glucose-6-P has also been shown to be asubstrate of some plastid translocators (GPT). The three types of proteins (TPT, PPT and GPT) are divergent in sequence as well as substrate specificity, but their substratespecificities overlap [Hypothetical proteins, Conserved]
LQTGLLFGLWYFLNVYFNIYNKKLLNVFPYPYFKTLISLAVGSLYCLLSWSSGLPKRLKISSALLKLLLP
VAIVHTIGHVTSNVSLSKVAVSFTHTIKAMEPFFSVVLSAFFLGQEFPSTLWLSLLPIVGGVALASDTEL
SFNWAGFLSAMISNITFVSRNIFSKKAMTIKSLDKTNLYAYISIMSLFLLSPPAFITEGPPFLPHGFMQA
ISGVNVTKIYTVSLVAAMGFFHFYQQVAFMLLGRVSPLTHSVGNCMKRVVVIVVSILFFGTKISPQQVFG
TGIAIAGVFLYSRVKAQKPKPK
>gnl|CDD|273286 TIGR00819, putative_efflux_pump_component_MtrF, p-Aminobenzoyl-glutamate transporter family. The p-Aminobenzoyl-glutamate transporter family includes two transporters, the AbgT (YdaH) protein of E. coli and MtrF of Neisseria gonorrhoea. AbgT is apparently cryptic in wild type cells, but when expressed on a high copy number plasmid, or when expressed at higher levels due to mutation, it allows utilization of p-aminobenzoyl-glutamate as a source of p-aminobenzoate for p-aminobenzoate auxotrophs. p-Aminobenzoate is a constituent of and a precursor for the biosynthesis of folic acid [Hypothetical proteins, Conserved]
MQMDSIPARRQGGFLRGVEELGGMKPHHPFLFFIFIIILLIASAAGASAFGSSADNPPVGAKGRADDGLI
HVVKLLDADEGIHIFPHTIKNFSGFAPLGAILALLLGAGIAEKSGLIPALMRKLASHSNAKLASFMVLFI
AFFSHIASDAALVILIPLGALIFHALGRHPLAGLAAAFAGVGCGFSANLFIGTIDPLLAGISQEAAAAFH
PDMHVGPEANWFFMAASTFVIAIIGGFITDKIIEPQLGPWQGDLNQDEKDIRHLNEITELERFGLIIAGV
VFIAFIAAIALMIIPADGILRDPENGLVAGSPFIKGIVPFIFLFFALPGIAYGIATRSIRGEADLPHAMA
EPMKELAGFIVIIFFAAQFVAFFNWSNIGKFIAVGGADFLEESGLAGIPAFIGFALICAFICLFIASASA
IWAILAPIFVPMFMLAGFAPAFAQAAFRIADSSTLIIAPMMPFFGLFLAFLMKYKKDAGLGTLISLMLPY
PAFFLIAWIALFCAWVFVLGLPIGPGAPTIYPAL
>gnl|CDD|273287 TIGR00820, Zinc-regulated_transporter_1, ZIP zinc/iron transport family. The Zinc (Zn2+)-Iron (Fe2+) Permease (ZIP) Family (TC 2.A.5)Members of the ZIP family consist of proteins with eight putative transmembrane spanners. They are derived from animals, plants and yeast. Theycomprise a diverse family, with several paralogues in any one organism (e.g., at least five in Caenorabditis elegans, at least five in Arabidopsis thaliana and two inSaccharomyces cervisiae. The two S. cerevisiae proteins, Zrt1 and Zrt2, both probably transport Zn2+ with high specificity, but Zrt1 transports Zn2+ with ten-fold higher affinitythan Zrt2. Some members of the ZIP family have been shown to transport Zn2+ while others transport Fe2+, and at least one transports a range of metal ions. The energy source fortransport has not been characterized, but these systems probably function as secondary carriers [Transport and binding proteins, Cations and iron carrying compounds]
CSHEDDNSCNNKEGALKLKIVAIFSILLASVIGVMFPLIGKNVPSLRPEGNFFFVAKAFAAGVILATGFM
HVLPEAFEMLSSPCLESTPWGKFPFAGFIAMISAILTLLVDLFATSYYERKHGKGDHGSKEIKVGDGEEG
TAGGTKHGHEYYEDHVHTNSEVVQLLRQRVVAQVLELGIIVHSVVIGLSLGASQSPDTIKPLIAALSFHQ
FFEGLGLGGCISQAEFKCKSVTIMCTFFAVTTPLGIAIGMGISSSYDDSSPTALIVEGVLNAASAGILIY
MALVDLLAADFMHPKMQSNLRLQIMAYIALLLGAGLMSLLAKWA
>gnl|CDD|129901 TIGR00821, Glucitol/sorbitol_permease_IIC_component, PTS system, glucitol/sorbitol-specific, IIC component. Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Gut family consists only of glucitol-specific transporters, but these occur both in Gram-negative and Gram-positive bacteria.E. coli consists of IIA protein, a IIC protein and a IIBC protein. This family is specific for the IIC component [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
MIEAITHGAEWFIGLFQKGGEVFVGMVTGILPLLISLLVIMNALIAFIGQDRIERFAQFCAGNPVLRYLV
LPFIGTFVFCNPMTLSLGKFLPEKYKPSYYAAASYSCHSMNGLFPHINPGELFVYLGIANGLTTLGLPLG
PLAVSYLLVGLVTNFFRGWVTDLTTKIFEKKMGIELSNQVH
>gnl|CDD|129902 TIGR00822, Mannose-permease_IIC_component_Phosphotransferase, PTS system, mannose/fructose/sorbose family, IIC component. Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Man (PTS splinter group) family is unique in several respects among PTS permease families. It is the only PTS family in which members possess a IID protein. It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue. Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars. The mannose permease of E. coli, for example, can transport and phosphorylate glucose, mannose, fructose, glucosamine,N-acetylglucosamine, and other sugars. Other members of this family can transport sorbose, fructose and N-acetylglucosamine. This family is specific for the sorbose-specific IIC subunits of this family of PTS transporters [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
MEITTLQIILLFILACIAGIGSVLDEFQTHRPLIACTLVGLILGDLKTGIILGGTLELIALGWMNVGAAQ
APDPALASIISTILVISGHQSIGTGIALALPLAAAGQVLTIFVRTITVLFQHAADKAAKEANTAAISRLH
VTAMLIQALRVAIPALIVALVSQSAVQAMLKAIPEVVTHGLQIAGGIIVVVGYAMVLRMMFKAYLMPFFY
LGFLFAAYTDFSLLAFGAVGGAGALLYIQLNPKSHRAQAAPSPAASKNELDDYDD
>gnl|CDD|129903 TIGR00823, PTS_system_lactose-specific_IIA_component, phosphotransferase system enzyme II, lactose-specific, factor III. The PTS Lactose-N,N?-Diacetylchitobiose-b-glucoside (Lac) Family (TC 4.A.3)Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains.The Lac family includes several sequenced lactose (b-galactoside) permeases of Gram-positive bacteria as well as the E. coli N,N?-diacetylchitobiose (Chb)permease which can transport aromatic b-glucosides and cellobiose as well as the chitin disaccharide, Chb, but only Chb induces expression of the chboperon. While the Lac permeases consist of two polypeptide chains (IIA and IICB), the Chb permease of E. coli consists of three (IIA, IIB and IIC). In B. subtilis, a PTS permease similar to the Chb permease of E. coli is believed to transport lichenan (a b-1,3;1,4 glucan) degradation products, oligosaccharides of 2-4 glucose units. This model is specific for the IIA subunit of the Lac PTS family [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
EEMELLGFEIVAYAGDARSKALEALKAAKAGDFAKARALVEQAGMCINEAHLAQTSLLAQEAGGGKMEVS
LTMVHGQDHLMTTILLKDLAAELIELYKR
>gnl|CDD|129904 TIGR00824, EIIA-man, PTS system, mannose/fructose/sorbose family, IIA component. Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains.The Man family is unique in several respects among PTS permease families It is the only PTS family in which members possess a IID protein. It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue. Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars. The mannose permease of E. coli, for example, can transport and phosphorylate glucose, mannose, fructose, glucosamine, N-acetylglucosamine, and other sugars. Other members of this can transport sorbose, fructose and N-acetylglucosamine. This family is specific for the IIA components [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
MIAIIISGHGQAAIALLKSAEMIFGEQNNVGAVPFVPGENAETLQEKYNAALADLDTEEEVLFLVDIFGG
SPYNAAARIIVDKPHMDVIAGVNLPLLLETLMARDDLSFDDLVALL
>gnl|CDD|129905 TIGR00825, EIIBC-GUT, PTS system, glucitol/sorbitol-specific, IIBC component. Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Gut family consists only of glucitol-specific permeases, but these occur both in Gram-negative and Gram-positive bacteria.E. coli consists of IIA protein, a IIC protein and a IIBC protein. This family is specific for the IIBC component [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
NAIKIVKGSGGWGGPLTVKPTEGKKIVYITAGTEPAIVDKLVNLTGWKAVDGFKTGEPPEEEIGVAVIDC
GGTLRCGIYPKRRIPTINIHPTGKSGPLAQFITEDIYVSGVGLNQISVANDASAEPIKSTKVPEEGKREF
KYGRDYDTSKKITEQSDGLLAKVGMGMGSVVATLFQSGRDTIDTVLKTILPFMAFVSALIGIIMASGLGD
WIAHGLVPLAGNPIGLVILALICSFPLLSPFLGPGAVIAQVIGVLIGVQIGKGTIPPHLALPALFAINAQ
AACDFIPVGLSLAEARQETVRVGVPSVLVSRFMTGAPTVLVAWVASIFIYQ
>gnl|CDD|273288 TIGR00826, IIB_component_Phosphotransferase_enzyme_II, PTS system, glucose-like IIB component. The PTS Glucose-Glucoside (Glc) Family (TC 4.A.1) Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Glc family includes permeases specific for glucose, N-acetylglucosamine and a large variety of a- and b-glucosides. However, not all b-glucoside PTS permeases are in this class, as the cellobiose (Cel) b-glucoside PTS permease is in the Lac family (TC #4.A.3). These permeases show limited sequence similarity with members of the Fru family (TC #4.A.2). Several of the E. coli PTS permeases in the Glc family lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). Most of these permeases have the B and C domains linked together in a single polypeptide chain, and a cysteyl residue in the IIB domain is phosphorylated by direct phosphoryl transfer from IIAglc(his~P). Those permeases which lack a IIA domain include the maltose (Mal), arbutin-salicin-cellobiose (ASC), trehalose (Tre), putative glucoside (Glv) and sucrose (Scr) permeases of E. coli . Most, but not all Scr permeases of other bacteria also lack a IIA domain. This model is specific for the IIB domain of the Glc family PTS transporters [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
TRLRLKTPGREKADEEAIAAGEGVKGVFTAAGQIQALGGTGNVNKVDACITRLRVGVADVSKVDDAVLKK
LGAHGVNPLQRAVQVISG
>gnl|CDD|129907 TIGR00827, PTS_system_galactitol-specific_IIC_component, PTS system, galactitol-specific IIC component. Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The only characterized member of this family of PTS transporters is the E. coli galactitol transporter. Gat family PTS systems typically have 3 components: IIA, IIB and IIC. This family is specific for the IIC component of the PTS Gat family [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
ILDLGATVILPIAIILLGLIFGQKPGKAFKAGLTIGIGFVGIGLVIDLLVDSLGPAAKGMVERFGLDLHV
IDVGWPATSSIAWASVIAAFIIPLGLLVNVAMLVTRTTKTMNVDIWNFWHYTFTGAVVYLVTGSIIQGLI
GAVMHAAVALKVADWTAPMVSNFYELEGISIPTGSTISYAPGIVLVDAIIEKIPGIKHWNADADTIQRRF
GIFGEPVFIGLVLGLIIGLLAGYNVKGVIELGMAMAAVMVLMPRMIKIIMEGLMPISESAREWLQKRFGG
REIHIGLDAAVLLGHPSVISTALILIPLTVLLAVILPGNAVLPFGDLATIPFFVAMAVGAHRGNLIRTLI
SGVIMMALSLYIATQIAPVFTKMAENSGFNMAGGSALISSIDQGGNLVNWIIWKLFS
>gnl|CDD|129908 TIGR00828, Mannose-permease_IID_component_Phosphotransferase, PTS system, mannose/fructose/sorbose family, IID component. Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Man family is unique in several respects among PTS permease families.It is the only PTS family in which members possess a IID protein. It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue. Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars. The mannose permease of E. coli, for example, can transport and phosphorylate glucose, mannose, fructose, glucosamine,N-acetylglucosamine, and other sugars. Other members of this can transport sorbose, fructose and N-acetylglucosamine. This family is specific for the IID subunits of this family of PTS transporters [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
KKITKKDITSMFLRSNLLQASFNFERMQALGFCYAMIPAIKKLYPDDKAGRSAALKRHLEFFNTHPNLVG
PIMGVTAAMEEKRANGAGIDDGAINGIKVGLMGPIAGVGDPIFWGTLRPIMAALGASLALSGNLLGPLLF
FFLFNLVRLATRYYGLHYGYSKGVKIVDDMGGNNLQKLTEGASILGLFVMGALVAKWTHINVPLVVSRIN
DHSGKVDVATVQNILDQLMPGLLPLGLTLLMYWLLRKKVNPVLLIGGTFVLGIVGYAFGFL
>gnl|CDD|129909 TIGR00829, Phosphotransferase_enzyme, PTS system, fructose-specific, IIB component. Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Fru family is a large and complex family which includes several sequenced fructose and mannitol-specific permeases as well as several PTS components of unknown specificities. The fructose components of this family phosphorylate fructose on the 1-position. The Fru family PTS systems typically have 3 domains, IIA, IIB and IIC, which may be found as 1 or more proteins. The fructose and mannitol transporters form separate phylogenetic clusters in this family. This family is specific for the IIB domain of the fructose PTS transporters [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
VAVTACPTGIAHTFMAAEALEKAAKKRGWEVKVETQGSVGAQNALTAEDIAAADGVILAADREIDLSRRF
AGKNVYETSTGDAIK
>gnl|CDD|273289 TIGR00830, phosphotransferase_enzyme_IIB_component, PTS system, glucose subfamily, IIA component. These are part of the The PTS Glucose-Glucoside (Glc) SuperFamily. The Glc family includes permeases specific for glucose, N-acetylglucosamine and a large variety of a- and b-glucosides. However, not all b-glucoside PTS permeases are in this class, as the cellobiose (Cel) b-glucoside PTS permease is in the Lac family (TC #4.A.3). The IIA, IIB and IIC domains of all of the permeases listed below are demonstrably homologous. These permeases show limited sequence similarity with members of the Fru family (TC #4.A.2). Several of the PTS permeases in the Glc family lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). Most of these permeases have the B and C domains linked together in a single polypeptide chain, and a cysteyl residue in the IIB domain is phosphorylated by direct phosphoryl transfer from IIAglc(his~P). Those permeases which lack a IIA domain include the maltose (Mal), arbutin-salicin-cellobiose (ASC), trehalose (Tre), putative glucoside (Glv) and sucrose (Scr) permeases of E. coli . Most, but not all Scr permeases of other bacteria also lack a IIA domain. The three-dimensional structures of the IIA and IIB domains of the E. coli glucose permease have been elucidated. IIAglchas a complex b-sandwich structure while IIBglc is a split ab-sandwich with a topology unrelated to the split ab-sandwich structure of HPr [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
IVSPISGEIVPLDQVPDEVFASKIVGDGFAILPTDGKVVAPVDGKIGKIFPTKHAFGIESDNGVEILIHI
GIDTVKLNGEGFTSHVEEGDRVKKGDPLLEFDLKAIKKKGYSITTPVVVTN
>gnl|CDD|129911 TIGR00831, Putative_Na+/H+_exchanger_Rv2287/MT2345/Mb2309., Na+/H+ antiporter, bacterial form. The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A.36) The CPA1 family is a large family of proteins derived from Gram-positive and Gram-negative bacteria, blue green bacteria, yeast, plants and animals. Transporters from eukaryotes have been functionally characterized, and all of these catalyze Na+:H+ exchange. Their primary physiological functions may be in (1) cytoplasmic pH regulation, extruding the H+ generated during metabolism, and (2) salt tolerance (in plants), due to Na+ uptake into vacuoles. This model is specific for the bacterial members of this family [Transport and binding proteins, Cations and iron carrying compounds]
VEIIELVMLATAVAVTVKFIRLPYPIALILAGLLLGLAGLLPEVPLDREIVLFLFLPPLLFEAAMNTDLR
ELRENFRPIALIAFLLVVVTTVVVGFSLNWILGIPLALALILGAVLSPTDAVAVLGTFKSIRAPKKLSIL
LEGESLLNDGAALVVFAIAVAVALGKGVFDPLNAALDFAVVCVGGIAAGLAVGYLAYRLLRAKIDDPLVE
IALTILAPFAGFLLAERFHFSGVIAVVAAGLILTNYGRDFSMSPTTRLIALDFWSVIVFLVNGIIFILIG
VQTPGTIFSAWKEILVAPAAVILALFTNAFVIYPVMTYVRFLWTMKPFSNRFLKKKPMEFGTRWKHVVSW
AGLRGAIPLALALSFPNQLLSGMAFPARYELVFLAAGVILFSLLVQGISLPIFVKRKFVSEHSERELEEI
IARYIAARSAKFALMKAVEQLRIVEPVARELLPELDARIEELRADGEEKIRSGMGEKNLRRRARLYVLDA
KRSAVVDLRAGGLISQEVLLELMRELDLKEAELME
>gnl|CDD|213563 TIGR00832, Uncharacterized_transporter_slr0944, arsenical-resistance protein. The Arsenical Resistance-3 (ACR3) Family (TC 2.A.59) The first protein of the ACR3 family functionally characterized was the ACR3 protein of Saccharomyces cerevisiae. It is present in the yeast plasma membrane and pumps arsenite out of the cell in response to the pmf. Similar proteins are found in bacteria, often as part of a four gene operon with an regulatory protein ArsR, a protein of unknown function ArsH, and an arsenate reductase that converts arsenate to arsenite to facilitate transport [Cellular processes, Detoxification, Transport and binding proteins, Anions]
LSLLERYLTLWIFLAIAAGVGLGVLFPSVFQALAALEVATVSIPIAIGLILMMYPPLAKVDYSALGDVFK
DPKGLILSLFINWIIGPFLMFLLAWLFLRDLFEYIAGLILLGLARCIAMVFVWNQLAKGDPEYTLVLVAV
NSLFQVFLYAPLAWLLLGVSPIWLGLTVITVPWETIAKSVLIYLGIPLIAGILTRYWLLKRKGREWYEKV
FLPKISPWSLIALLFTIVLLFAFQGETIIELPLDIALIAIPLLIYFYIMFFLTFALAKKLGLPYSITAPA
AFTGASNNFELAIAVAISLFGLNSGAALATVVGPLIEVPVMLSLVNVA
>gnl|CDD|129913 TIGR00833, Putative_membrane_protein_ActII-3, Transport protein. The Resistance-Nodulation-Cell Division (RND) Superfamily- MmpL sub family (TC 2.A.6.5)Characterized members of the RND superfamily all probably catalyze substrate efflux via an H+ antiport mechanism. These proteins are found ubiquitously in bacteria, archaea and eukaryotes. This sub-family includes the S. coelicolor ActII3 protein, which may play a role in drug resistance, and the M. tuberculosis MmpL7 protein, which catalyzes export of an outer membrane lipid, phthiocerol dimycocerosate [Transport and binding proteins, Unknown substrate]
RSAYGIIGVWIATAISLQLLAPLLEDVSYFRLQAELPGGAASSIAVKEMSAAFQEAIRDPKIILVLESNE
RLGDKDYATYDALIAKLRADIMHVISVVDFWGPPEAAEGLRSDDGKATIIIVNLAGEKGQKEAQEAINAV
RRIVEQTNAPDGLTVHVTGPLATIADILESGDKDMNRITATTGIIVLIILLLVYRSPITMLVPLVSVGFS
VVVAQGIVSLLGIPGLIGVNAQTTVLLTALVIGAGTDYAVFLTGRYHEERRKGESLEEAAAEALRGTGKA
ILGSALTVAVAFLALSLARLPSFKTLGVSCAVGVLVALLNAVTLTPALLTLEGREGLMKPGRKSKIRFIW
RRLGTAVVRRPWPILVTTLIISGVSLLALPLIRTGYDDEKMIPTDLESVQGYEAADRHFPGNSMDPMVVM
IKSDHDVRNPALLADIDRFEREIKAVPGINMVQETQRPDGVVIKKTYLTFQAGNLGDQLDEFSDQLTSRQ
AYLLQDAEKIAEAIAGLRLVQAGMRLDGENLGQVSLAVRLMQQAISKLQGSAGDVFDIFDPLRRFVAAIP
ECRANPVCSVAREIVQAADTVVSSAAKLADAAGQLARGIADVASALSQVSGLPNALDGIGTQLAQMRESA
AGVQDLLNELSDYSMTMGKLKGNAMGVDFYAPPRIFTDPNFKAVLDYFLSPDGHAARLLVYGDGSPAGDQ
GAQEFNAIRTVAEEAIQRADLEPAKVELAGVSAVNRDLRDLVNSDLGLISIITLAIVFMILALLLRAPVA
PIVLIGSVALSYLWALGLSVLAFQHILGAELHWSVLAGVFVLLVALGVDYNMLLVSRIKEESPAGNRTGI
IRALGSTGGVITAAGLVFAGTMAALASAQLTAIAQFGFTVGVGILLDTFIVRSVTVPALTLLLGRWIWWP
>gnl|CDD|273290 TIGR00834, Band_3_anion_transport_protein, anion exchange protein. The Anion Exchanger (AE) Family (TC 2.A.31)Characterized protein members of the AE family are found only in animals.They preferentially catalyze anion exchange (antiport) reactions, typically acting as HCO3-:Cl- antiporters, but also transporting a range of other inorganic and organic anions. Additionally, renal Na+:HCO3- cotransporters have been found to be members of the AE family. They catalyze the reabsorption of HCO3- in the renal proximal tubule [Transport and binding proteins, Anions]
FVELNELMLDRNQEPEWRETARWIKFEEDVEEGGGRWGKPHVATLSFHSLLELRRCFAKGAILLDLAATS
LPGVANMVVDHLIYSGQIRPEDRDEVLRALLLKHSHQSDAKKLGGLSRARSQSSIGKTLSHDASEMPNPD
NGAPLLPHQPLTEMQLLSVPGDIGSREKSKLKFLKKIPEDAEATNVLVGEVDFLEQPALAFVRLKEAVPL
EALLEVPVPVRFLFVLLGPSGPGKDYHEIGRAIATLMSDEVFHDAAYLADDRDDLLAGIDEFLDCSIVLP
PGEWDPEIRLEPPAPLQRELLRKRYEPSTVRPENPTMGGDTEPEDGGSEGPHGDDDPLQRTGRPFGGLIR
DIKRRYPHYLSDFTDALNPQCLAAVIFIYFAALSPAITFGGLLGEKTRNMMGVSELLISTAVQGVLFALL
AAQPLLVVGFSGPLLVFEEAFFSFCESNGLEYLVGRVWIGLWLVLLVLLLVATEGSFLVRYISRFTQEIF
SFLISLIFIYETFSKLIKIFQEHPLQVFYNTLFCVPPKPQGPSVSALLEKDCSKLGGTLGGNNCRFQPNT
ALLSLVLMLGTFFLAMFLRKFKNSRYFPGKARRLIGDFGVPISILIMVLVDIFIGDTYTQKLSVPSGLKV
TNPSARGWFIPPLGENRPFPWWMMFAAALPALLVFILIFMEQQITTLIVSKKERKLKKGSGFHLDLLLVV
GMGGVAALFGLPWLSAATVRSVTHANALTVMSKASAPGEKAQIQEVREQRVTGLLVAVLVGLSILMEPIL
KRIPLAVLFGIFLYMGVTSLSGIQLFDRLLLLLMPPKYHPDVPYVRRVKTWRMHLFTAIQILCLALLWVV
KSTPASLAFPFVLILTVPLRRLLLPRLFTERELKCLDKEDAKVTFDEEDGEDEYNEVPMP
>gnl|CDD|273291 TIGR00835, carrier_protein, amino acid carrier protein. The Alanine or Glycine: Cation Symporter (AGCS) Family (TC 2.A.25) Members of the AGCS family transport alanine and/or glycine in symport with Na+ and or H+
WGYPMFILLLGTGLFFTIRLGFVQFRYLPAAFRLLFGKRKEQGKGGVSSFQALFTSLAARVGIGNIVGVA
TAIAIGGPGAVFWMWVTAFIGMATKFVESTLAQKYRERDADGVFRGGPMYYIKKGLGMRWLAVLFAVFLI
ASFGIGNMVQANAIASALSNAFNVPKLVTGIVLTVLTALIIFGGLKRIAKISSVVVPFMALLYVIMALYI
IIMNIEQLPAVISLIFRSAFGGDAAAGGFAGSTVAQAIMIGVKRGLFSNEAGMGSAPIAAAAAQVSHPVR
QGLVQMLGVFIDTMIVCTATALVILLSGVWNNGEGLSGAQLTQQALSYGLGSFGAVFVAVALFLFAFSTI
IGWYYYGEKNAEFLKGNKKVKLYRLVFLAAVFVGAFLSLDLVWNLADLSMGLMAIPNLIAILLLRKVVYE
LTKDY
>gnl|CDD|273292 TIGR00836, Ammonium_transporter, ammonium transporter. The Ammonium Transporter (Amt) Family (TC 2.A.49) All functionally characterized members of the Amt family are ammonia or ammonium uptake transporters. Some, but not others, also transport methylammonium. The mechanism of energy coupling, if any, to methyl-NH2 or NH3 uptake by the AmtB protein of E. coli is not entirely clear. NH4+ uniport driven by the pmf, energy independent NH3 facilitation, and NH4+/K+ antiport have been proposed as possible transport mechanisms. In Corynebacterium glutamicum and Arabidopsis thaliana, uptake via the Amt1 homologues of AmtB has been reported to be driven by the pmf [Transport and binding proteins, Cations and iron carrying compounds]
TAWLLIAAALVFFMQPGFALLYAGLVRSKNVLNIMMKNLLDFAIGSLLWWLFGYSLAFGEDNPINGFIGT
GGFGLKNFLYPGKISLAGTLPDLLFFLFQMMFAAIAATIISGAVAERMKFSAYLLFSVLWTTLVYPPVAH
WVWGGGGWLYKLGVLDFAGGGVVHIVGGVAGLAAALVLGPRIGRFPRPVAIRPHNVPLVVLGTFILWFGW
FGFNAGSALAANGTAAYAAVNTNLAAAAGGLTWLLIDWLKHGKPTLLGACNGILAGLVAITPGCGVVTPW
GAIIIGLVAGVLCYLAVSKLKKKLKIDDPLDAFAVHGVGGIWGLIATGLFAAPKVGGVGTGGLLGGNGKQ
LGVQLIGIAAIIAWAFVVTFIILKILDKTIGLRVSEEEEKIGLDLAEHGEFAY
>gnl|CDD|273293 TIGR00837, Tyrosine-specific_transport_protein, aromatic amino acid transport protein. The Hydroxy/Aromatic Amino Acid Permease (HAAAP) Family- tyrosine/tryptophan subfamily (TC 2.A.42.1) The HAAAP family includes well characterized aromatic amino acid:H+ symport permeases and hydroxy amino acid permeases. This subfamily is specific for aromatic amino acid transporters and includes the tyrosine permease, TyrP, of E. coli, and the tryptophan transporters TnaB and Mtr of E. coli [Transport and binding proteins, Amino acids, peptides and amines]
GGALIIAGTTIGAGMLALPTSTAGAWFIWTLLLLILLWFLMLHSGLLLLEVYLTYPGGASFNTIAKDLLG
KTGNIIAGLSLLFVLYILTYAYISGGGSILSRLIGEYFGFPWSARAIVLIFTVLFGSFVWLSTSAVDRIT
RVLIFGKIIAFALVFSGLLPHVKGDLLLDVALDTSYWPYILSALPVCLTSFGFHGNVPSLYKYYDGNVKK
VKKSILIGSAIALVLYILWQLATMGNLPRSEFLPIIAKGGNLDGLVNALQGVLKSSAIELALELFSNFAL
ASSFLGVTLGLFDYLADLFKFDDSKKGRFKTGLLTFLPPLVFALFYPEGFLYAIGYAGLAATIWAVIIPA
LLAWKARKKFPNAGYRVWGGNKLLLLVLLFG
>gnl|CDD|129918 TIGR00838, Argininosuccinate_lyase, argininosuccinate lyase. This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens [Amino acid biosynthesis, Glutamate family]
LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREG
PFILDPDDEDIHMAIERELIDRVGEDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIEL
AEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYL
AELLGFDAVTENSLDAVSDRDFILELLFVAALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQ
KKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQEDKEPLFDALKTVELSLEMATGMLDTITVN
KERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGLEELTLEELQKFSPEFDEDVY
EALDPESSVEKRDAKGGTAPEEVLQAIAEAKARLG
>gnl|CDD|213564 TIGR00839, Aspartate_ammonia-lyase, aspartate ammonia-lyase. This enzyme, aspartate ammonia-lyase, shows local homology to a number of other lyases, as modeled by pfam00206. Fumarate hydratase scores as high as 570 bits against this model [Energy metabolism, Amino acids and amines]
RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDIPEFVRGMVMVKKAAALANKELGTIPESIANA
IVAACDEILNNGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTN
DAYPTGFRIAVYSSLIKLVDAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEV
KNIKRTAELLLEVNLGATAIGTGLNTPPEYSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALK
RLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDTTVTLAAE
AGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGYVFNSIGIVTYLNPFIGHHNGD
IVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHPAYKAKRYK
>gnl|CDD|273294 TIGR00840, Endosomal/prevacuolar_sodium/hydrogen_exchanger, sodium/hydrogen exchanger 3. The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A.36)The CPA1 family is a large family of proteins derived from Gram-positive and Gram-negative bacteria, blue green bacteria, yeast, plants and animals.Transporters from eukaryotes have been functionally characterized, and all of these catalyze Na+:H+ exchange. Their primary physiological functions may be in(1) cytoplasmic pH regulation, extruding the H+ generated during metabolism, and (2) salt tolerance (in plants), due to Na+ uptake into vacuoles.This model is specific for the eukaryotic members members of this family [Transport and binding proteins, Cations and iron carrying compounds]
DYEHVQSPYEFILWILLASLAKIGFHLTHKVIRAVPESVLLIVYGLLVGGIIKASPHIDPPTLDSSYFFL
YLLPPIVLDAGYFMPQRNFFENLGSILIFAVVGTLINAFVIGLSLYGICLIGGFGSIDIGLLDNLLFGSL
ISAVDPVAVLAVFEEYHVNEKLYIIIFGESLLNDAVTVVLYNTFIKFHKTADEPVTIVDVFEGCASFFVV
TCGGLLVGVVFGFLVAFITRFTHHIRQIEPLFVFLISYLSYLFAETLHLSGILALIFCGITMKKYVEANM
SRRSQTTIKYFMKMLSSLSETLIFIFLGVSLVTENHEWNWAFVVATLSFCVIYRVLGVRTLSWITNEFRP
VEIPYKDQLVIFYAGLRGAVAFALALLLDEKIFPYKFLFVTTTLVVVFFTVIFQGGTIKPLVEVLKVKKG
CISKTKINEELHDREFDHLLPGIEDICGQIGHDRAIDKLNGFDIKYLLKPLIRRNSPKSSDIVAVYHKLN
LKQAISLVEGGSLSFVGTNPEPSNSEPIIPALSSEDKEEIRDILGTNLYKPRQRFQSYSRHVLKPVPLE
>gnl|CDD|188087 TIGR00841, Ileal_sodium/bile_acid_cotransporter, bile acid transporter. The Bile Acid:Na+ Symporter (BASS) Family (TC 2.A.28) Functionally characterized members of the BASS family catalyze Na+:bile acid symport. These systems have been identified in intestinal, liver and kidney tissues of animals. These symporters exhibit broad specificity, taking up a variety of non bile organic compounds as well as taurocholate and other bile salts. Functionally uncharacterised homologues are found in plants, yeast, archaea and bacteria [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
ILSTNLSTILLILLFLIMFSMGCTLEFEDFKGHLRKPWGVIIGLLAQYGIMPLTGFLLAKVFKLPPELAV
GVLIVGCCPGGTASNVFTYLLKGDMALSISMTTCSTLLALGMMPLLLYIYAKMWVDGTLVVPYLGIGLSL
VIVLIPVSIGMLVKHKLPQIAKIILKVGLISVFLLSVIIAVVGGINVENLATIGPLLLLVGILLPLAGFL
LGYLLAKLAGLPWARCRTISIEVGMQNSQLCSTIAQLSFSPEVAVPSAIFPLIYALFQLAFALLFLIIHF
CYLKCH
>gnl|CDD|213565 TIGR00842, Probable_transport_protein_Rv0917/MT0942/Mb0941., choline/carnitine/betaine transport. The Betaine/Carnitine/Choline Transporter (BCCT) Family (TC 2.A.15) Proteins of the BCCT family share the common functional feature of transporting molecules with a quaternary ammonium group [R-N+(CH3)3]. The BCCT family includes transporters for carnitine, choline and glycine betaine. BCCT transporters have 12 putative TMS, and are energized by pmf-driven proton symport. Some of these permeases exhibit osmosensory and osmoregulatory properties inherent to their polypeptide chains [Transport and binding proteins, Other]
GWAYILTVTLFLGFVLYIAFSRYGKIRLGRDDEKPEFSTLSWLAMLFAAGMGAGLMFWGVAEPLTYYLTP
PFGAGPTSTTAQEQALAYTLFHWGIHPWAIYALVGLALAYFHFRKGLPLRLSSALVPLLGEKVNGPIGKA
IDILALVATVFGVATSLGLGAPQINAGLSALFGIPDSFWLQALIILCVTALACISVASGVGKGIKILSNI
NMALAFLLLLFVLIVGPTVFLLNSFVDSIGNYLQNFPQMSFRTDPDDGKGGWPGGWTVFYWAWWISWSPF
VGMFIARISRGRTIREFIFGVLLGPTAFTWLWFSVFGNSALLLQQNGGFINGPFVVETNGARALFGLLAA
LPLGTITMALALILIIIFFITSADSASLVLANTTSRGGQLGEEPPKWVRVFWAVAIGLIALVLLFSGGSL
AALQTTTIIAALPFSFVMLVVMFSLIKDLKQD
>gnl|CDD|129923 TIGR00843, Benzoate_membrane_transport_protein, benzoate transporter. The benzoate transporter family contains only a single characterised member, the benzoate transporter of Acinetobacter calcoaceticus, which functions as a benzoate/proton symporter [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MLRCLKAIKHDVSLRLASIPPPTLIAGFLAVLIGYAGPAAIFFQAAIKAGASTAMIIGWITAIGIAAAVS
GIFLSIRFKTPVLTAWSAPGAALLVTGFPGISLNEAIAAFITAAALIFLCGITGLFAKLLKIIPHGIAAA
MLAGILFQFGLGAFAALDGLFLICFSMLLCWLASKAFAPRYAMIAALICGIAFSFALGDMNPTDLDFKIA
LPQFIAPDFSFAHSLNLALPLFLVSLAGQFAPGIAALKAAGYNAPAKPIIAAAGLAALFAAFAGGISIGI
AAITAAICMGKDAHEDKDKRWIAAAAAGIFYLLAGLFAGAITALFAALPKELIAALAGLALLGAIAGNIK
IALHEDQERDAALIAFLATASGLHFLGIGSAFWGLCAGGLAYFIL
>gnl|CDD|273295 TIGR00844, Na+/H+_antiporter_1, na(+)/h(+) antiporter. The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A.36) The CPA1 family is a large family of proteins derived from Gram-positive and Gram-negative bacteria, blue green bacteria, yeast, plants and animals. Transporters from eukaryotes have been functionally characterized, and all of these catalyze Na+:H+ exchange. Their primary physiological functions may be in (1) cytoplasmic pH regulation, extruding the H+ generated during metabolism, and (2) salt tolerance (in plants), due to Na+ uptake into vacuoles. This model is specific for the fungal members of this family [Transport and binding proteins, Cations and iron carrying compounds]
MIWEQLEVTKAHVAYSCVGIFSSIFSLVSLFVKEKLYIGESMVASIFGLIVGPHCLNWFNPLSWGNTDSI
TLEISRILLCLQVFAVSVELPRKYMLKHWVSVTMLLVPVMTSGWLVIALFVWILVPGLNFPASLLMGACI
TATDPVLAQSVVSGTFAQKVPGHLRNLLSCESGCNDGLAFPFVFLSMDLLLYPGRGGEIVKDWICVTILW
ECIFGSILGCIIGYCGRKAIRFAEGKNIIDRESFLAFYLILALTCAGFGSMLGVDDLLVSFFAGTAFAWD
GWFAQKTHESNVSNVIDVLLNYAYFVYLGSILPWKDFNNGDIGLDVWRLIILSLVVIFLRRIPAVLILKP
LIPDIKSWREAMFIGHFGPIGVGAVFAAILSKSQLESHLTDEETPLNVTPGKGSKHWQLMACIWPITCFS
IVTSVIVHGSSVAVIMLGRYLNTVTLTATPTTRTTNTNTKNSWLQRLPSLDKSGRPFSLQRLDKEMSLSP
GQIGVRTSGMPARPALGMRQRWRQKLRNNKEMEDDIEMNDLGRERLQKEKEAHAATFDLSTTTTTQLGTE
NGRGGGLEERSKTNIKERSENVNTIYGLDKLARDTENRDVTYVPTSRYDGIESEIDDVYTYENDSESIAS
SERRRIKKLREEEQQAYIAYTEDNQVIIENRQGEILEYVDIHDRGARDAEVGVHNGGRLKRALSPPLEKL
HQITNEAKKSKYYAYKVGNDLIIEDESGEVFRRYRISPHGGKRKIKKRNDSVVSVDEEKAIEGPSRVPER
GNHDLLHSEDEMADDEAESENMDDYEDSDDNAYESKDHAD
>gnl|CDD|273296 TIGR00845, Sodium/calcium_exchanger_1, sodium/calcium exchanger 1. The Ca2+:Cation Antiporter (CaCA) Family (TC 2.A.19)Proteins of the CaCA family are found ubiquitously, having been identified in animals, plants, yeast, archaea and widely divergent bacteria.All of the characterized animal proteins catalyze Ca2+:Na+ exchange although some also transport K+. The NCX1 plasma membrane protein exchanges 3 Na+ for 1 Ca2+. The E. coli ChaA protein catalyzes Ca2+:H+ antiport but may also catalyze Na+:H+ antiport. All remaining well-characterized members of the family catalyze Ca2+:H+ exchange.This model is specific for the eukaryotic sodium ion/calcium ion exchangers of the Caca family [Transport and binding proteins, Other]
MLRLSLSPLFSVGFHLLTAVSLLFLHVDHARALTEASSSGSNTGECTGSYYCKEGVILPIWEPQNPSVGD
KIARATVYFVAMVYMFLGVSIIADRFMASIEVITSQEKEITIKKPNGETTVTTVRIWNETVSNLTLMALG
SSAPEILLSVIEVCGHNFEAGDLGPSTIVGSAAFNMFIIIAICVYVIPDGETRKIKHLRVFFVTAAWSVF
AYVWLYLILAVFSPGVVEVWEGLLTFFFFPLCVVFAWVADRRLLFYKYVYKRYRAGKQRGMIIETEGDRP
KSKTEIEMDGKMVNSHVDNFLDGALVLEVKEFDEARREMIRILKELKQKHPDKDLEQLEEMANYQVLSRQ
QKSRAFYRIQATRLMTGAGNILKKHAADAARKAVSMHEVATDDEENDPVSKIFFEPGHYTCLENCGTVAL
TVVRRGGDLTNTVYVDYRTEDGTANAGSDYEFTEGTLVFKPGETQKEFRIGIIDDDIFEEDEHFYVRLSN
LRVGSEDGILEANHVSAVAQLASPNTATVTILDDDHAGIFTFEEDVFHVSESIGIMEVKVLRTSGARGTV
IVPYRTVEGTARGGGKDFEDTCGELEFENDETEKTIRVKIVDDEEYEKNDTFFIELGEPRWAKRGIKAAL
LLNETITDDDQKLTSKEEEERRIAEMGKPRLGEHTKLEVIIEESYEFKSTVDKLIKKTNLALVVGTHSWR
EQFIEAITVSAGDDDDDDEDGEEKLPSCFDYVMHFLTVFWKVLFAFVPPTEYWGGWACFVVSILMIGVLT
AFIGDLASHFGCTIGLKDSVTAVVFVALGTSVPDTFASKVAATQDQYADASIGNVTGSNAVNVFLGIGVA
WSIAAIYHAANGTQFKVSPGTLAFSVTLFTIFAFICIGVLLYRRRPEIGGELGGPRTAKLLTSALFVLLW
LLYILFSSLEAYCHIKGF
>gnl|CDD|273297 TIGR00846, Putative_ionic_transporter_y4hA, calcium/proton exchanger. The Ca2+:Cation Antiporter (CaCA) Family (TC 2.A.19)Proteins of the CaCA family are found ubiquitously, having been identified in animals, plants, yeast, archaea and widely divergent bacteria.All of the characterized animal proteins catalyze Ca2+:Na+ exchange although some also transport K+. The NCX1 plasma membrane protein exchanges 3 Na+ for 1 Ca2+. The E. coli ChaA protein catalyzes Ca2+:H+ antiport but may also catalyze Na+:H+ antiport. All remaining well-characterized members of the family catalyze Ca2+:H+ exchange.This model is generated from the calcium ion/proton exchangers of the CacA family [Transport and binding proteins, Cations and iron carrying compounds]
VLLGSWLNILLIFVPAAIILGHWGSSQTLIFLLNLLGILPLAARVSFHTEELAHRLGETLGGLLNATFGN
AVELIVSIMALGNGKVEVVRDSLLGSILSNLLLVLGLCLLLGGIANIRREQTFDRGAAQTNFALLLLAIL
SLLLPAALPAAKPHEKSDHFQDMILGLSRGTAIVSLILYGAFLVFQLWTHRQLFEAQEEEDSEVDDEVHE
KPTVLSPWSAAAWLVGTTIAIILLADYLVDTIDDAVDSWGLSVAFIGLILAPIVGNAAEHVTAVKAALKN
KLDLALGVALGSALQIILFVVPLVVLVAWMLGIPMDLNFGTFETIVLALSLFLTTITLQDGRSNYLEGAV
LLALYIIIAMAFF
>gnl|CDD|129927 TIGR00847, Nitrogen_fixation_protein_FixS, cytochrome oxidase maturation protein, cbb3-type. CcoS from Rhodobacter capsulatus has been shown essential for incorporation of redox-active prosthetic groups (heme, Cu) into cytochrome cbb(3) oxidase. FixS of Bradyrhizobium japonicum appears to have the same function. Members of this family are found so far in organisms with a cbb3-type cytochrome oxidase, including Neisseria meningitidis, Helicobacter pylori, Campylobacter jejuni, Caulobacter crescentus, Bradyrhizobium japonicum, and Rhodobacter capsulatus [Energy metabolism, Electron transport, Protein fate, Protein modification and repair]
MEILTILIPISLLLGGVGLVAFLWSLKSGQYDDLKGAAWRILGDYDDDPNQ
>gnl|CDD|273298 TIGR00848, Includes:_Phosphotransferase_enzyme_IIA_component, PTS system, fructose subfamily, IIA component. 4.A.2 The PTS Fructose-Mannitol (Fru) Family Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Fru family is a large and complex family which includes several sequenced fructose and mannitol-specific permeases as well as several putative PTS permeases of unknown specificities. The fructose permeases of this family phosphorylate fructose on the 1-position. Those of family 4.6 phosphorylate fructose on the 6-position. The Fru family PTS systems typically have 3 domains, IIA, IIB and IIC, which may be found as 1 or more proteins. The fructose and mannitol transporters form separate phylogenetic clusters in this family. This model is specific for the IIA domain of the fructose PTS transporters. Also similar to the Enzyme IIA Fru subunits of the PTS, but included in TIGR01419 rather than this model, is enzyme IIA Ntr (nitrogen), also called PtsN, found in E. coli and other organisms, which may play a solely regulatory role [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISDTEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQ
PFVAIARLVKGVDWQSLDGKPVKLIFLIAVPKDEAGNTHLKALSQLARLLLNDEFRAKL
>gnl|CDD|129929 TIGR00849, gutA, PTS system, glucitol/sorbitol-specific IIA component. Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. This family consists only of glucitol-specific transporters, and occur both in Gram-negative and Gram-positive bacteria.The system in E.Coli consists of a IIA protein, and a IIBC protein. This family is specific for the IIA component [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
MTIIYENTVKDIGDLAITFLEEGMIITFGEGAPDDLAEYCFIHNIKEVKGTLKPGQVFMIGGIAYPVTAV
GDVAEKNLRSLGHITVRFDGSNVAEFPGTVHVEGKEPPKIKPGSKFSIVAE
>gnl|CDD|129930 TIGR00851, mtlA, PTS system, mannitol-specific IIC component. Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Fru family is a large and complex family which includes several sequenced fructose and mannitol-specific permeases as well as several putative PTS permeases of unknown specificities.The Fru family PTS systems typically have 3 domains, IIA, IIB and IIC, which may be found as 1 or more proteins. The fructose and mannitol transporters form separate phylogenetic clusters in this family. This family is specific for the IIC domain of the mannitol PTS transporters [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
KVQRFGSFLSGMIMPNIGAFIAWGIITALFIPTGWFPNETLAKLVGPMITYLLPLLIAYTGGKLIYDLRG
GVVGATATMGVIVGSDIPMFLGAMIMGPLGGWLIKKTDEFVQGKVKQGFEMLVNNFSAGIIGFILTILAF
EGIGPIVKAISKILAAGVEAIVHAHLLPLASIFVEPAKILFLNNAINHGIFSPLGIEQAAHTGKSILFLI
EANPGPGLGVLLAYMFFGKGSAKQTAPGAAIIHFFGGIHEIYFPYVLMRPLLILAVILGGMTGVLTYTIL
DAGLVAPASPGSIIALLAMTPKGEYLGVLAGVLVAAAVSFVVSAIILKSSKDPEEDLI
>gnl|CDD|273299 TIGR00852, IIBC_component_Phosphotransferase_enzyme_II, PTS system, maltose and glucose-specific subfamily, IIC component. The PTS Glucose-Glucoside (Glc) Family (TC 4.A.1) Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Glc family includes permeases specific for glucose, N-acetylglucosamine and a large variety of a- and b-glucosides. However, not all b-glucoside PTS permeases are in this class, as the cellobiose (Cel) b-glucoside PTS permease is in the Lac family (TC #4.A.3). These permeases show limited sequence similarity with members of the Fru family (TC #4.A.2). Several of the E. coli PTS permeases in the Glc family lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). Most of these permeases have the B and C domains linked together in a single polypeptide chain, and a cysteyl residue in the IIB domain is phosphorylated by direct phosphoryl transfer from IIAglc(his~P). Those permeases which lack a IIA domain include the maltose (Mal), arbutin-salicin-cellobiose (ASC), trehalose (Tre), putative glucoside (Glv) and sucrose (Scr) permeases of E. coli . Most, but not all Scr permeases of other bacteria also lack a IIA domain. This model is specific for the IIC domain of the Glc family PTS transporters [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
GSAAFFFLPLLFAIGAAKGFGGNPYLGAALAGILVHPVLNNAMGVGAQAVGNFFGFEIAKVGYTGVVGPI
IVGAIALALHERFLDKKLPDVLGFFLGPRFVVIIAGFVAILLIGPLGRVWPPVGISALLHWLYSAGGALG
GAIFGFLYRLLVPTGLHHIFYAIFIQLIAGGTVIGGGQVIPGDALANMAQGGAALAVFFTAGDAKFKSIG
LPAAFSAGLGITEPAMYGVALRERRPFVAGLIGSALLTAFLTGITEPLEFLFLFGAPGLYSIHAVLAGSI
FTVAIGMGI
>gnl|CDD|273300 TIGR00853, IIB_component_Phosphotransferase_enzyme, PTS system, lactose/cellobiose family IIB component. Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains.The Lac family includes several sequenced lactose (b-galactoside) permeases of Gram-positive bacteria as well as those in E. coli. While the Lac family usually consists of two polypeptide components IIA and IICB, the Chb permease of E. coli consists of three IIA, IIB and IIC. This family is specific for the IIB subunit of the Lac PTS family [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
MNETNILLLCAAGMSTSLLVNKMNKAAEEYGVPVKIAAGSYGAAGEKLDDADVVLLAPQVAYMLPDLKKE
TDKKGIPVEVINGAQYGKLTGAGVL
>gnl|CDD|129933 TIGR00854, pts-sorbose, PTS system, mannose/fructose/sorbose family, IIB component. Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains.The Man family is unique in several respects among PTS permease families.It is the only PTS family in which members possess a IID protein. It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue. Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars. The mannose permease of E. coli, for example, can transport and phosphorylate glucose, mannose, fructose, glucosamine, N-acetylglucosamine, and other sugars. Other members of this can transport sorbose, fructose and N-acetylglucosamine. This family is specific for the IIB components of this family of PTS transporters [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
NIVLARIDDRLIHGQVGTTWTKVAGANRIIVVNDDVANDEVRQTLMGIVAPTGFKVRFVSLEKTINVIHK
PAYHDQTIFLLFRNPQDVLTLVEGGVPIKTVNVGGMHFSNGKKQITKKVSVDDQDITAFRFLKQRGVKLF
LRDVPSDPSED
>gnl|CDD|273301 TIGR00855, 50S_ribosomal_protein_L7/L12, ribosomal protein L7/L12. Ribosomal proteins L7 and L12 are synonymous except for post-translational modification of the N-terminal amino acid. THis model resembles pfam00542 but matches the full length of prokaryotic and organellar proteins rather than just the C-terminus [Protein synthesis, Ribosomal proteins: synthesis and modification]
LSKEQIIEALKSMTVLELSELVKALEEKFGVSAAAPVAAGAAGAAAGAAAAEEKTEFDVILKGAGDNKIA
VIKVVREITGLGLKEAKDLVEGAPKALKEGVSKEEAEELKKKLEEAGAKVEVK
>gnl|CDD|129935 TIGR00856, pyrC_dimer, dihydroorotase, homodimeric type. This homodimeric form of dihydroorotase is less common in microbial genomes than a related dihydroorotase that appears in a complex with aspartyltranscarbamoylase or as a homologous domain in multifunctional proteins of pyrimidine biosynthesis in higher eukaryotes [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
ELTIRRPDDWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAGHDFTPL
MTLYLTDSLTPEELERAKNEGVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHG
DIDIFDREARFIESVLEPLRQRFPALKVVLEHITTKDAIDYVEDGNNRLAATITPQHLMFTRNDLLGGGV
NPHLYCLPILKRNIHQQALLELAASGFPKFFLGTDSAPHARHRKESSCGCAGCFSAPTALPSYAEVFEEM
NALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESIALTDDTLVPFRAGETLSWSVK
>gnl|CDD|273302 TIGR00857, Probable_dihydroorotase-like_protein, dihydroorotase, multifunctional complex type. In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
GKETEVDILVEGGRIKKIGKLRIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGG
FTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNQGKELTEAYELKEAGAVGRMFTDDG
SEVQDILSMRRALEYAAIAGVPIALHAEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKH
AGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEG
LKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGL
PDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED
>gnl|CDD|273303 TIGR00858, Putative_8-amino-7-oxononanoate_synthase, 8-amino-7-oxononanoate synthase. 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEEL
AEWKGTEAALLFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLE
KNRGERRKLIVTDGVFSMDGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDI
QVGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIAR
LRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPG
DIDRLAEALK
>gnl|CDD|273304 TIGR00859, Amiloride-sensitive_sodium_channel_subunit_alpha, sodium channel transporter. The Epithelial Na+ Channel (ENaC) Family (TC 1.A.06)The ENaC family consists of sodium channels from animals and has no recognizable homologues in other eukaryotes or bacteria. The vertebrate ENaC proteins from epithelial cells cluster tightly together on the phylogenetic tree: voltage-insensitive ENaC homologues are also found in the brain. Eleven sequenced C. elegans proteins, including the degenerins, are distantly related to the vertebrate proteins as well as to each other. At least some ofthese proteins form part of a mechano-transducing complex for touch sensitivity. Other members of the ENaC family, the acid-sensing ion channels, ASIC1-3,are homo- or hetero-oligomeric neuronal H+-gated channels that mediate pain sensation in response to tissue acidosis. The homologous Helix aspersa(FMRF-amide)-activated Na+ channel is the first peptide neurotransmitter-gated ionotropic receptor to be sequenced.Mammalian ENaC is important for the maintenance of Na+ balance and the regulation of blood pressure. Three homologous ENaC subunits, a, b and g, havebeen shown to assemble to form the highly Na+-selective channel.This model is designed from the vertebrate members of the ENaC family [Transport and binding proteins, Cations and iron carrying compounds]
SYRELLVWFCNNTTTHGAIRIVCSRGGRLKRALWALLTLLALALLLWQCGLLVRYYLSYPVSVSLSVNSD
KLTFPAVTLCNLNPYRYSKVKHLLEELDLETAQTLLSLYGYNSSLARSARSNNRNRIPLVVLDETLPRHP
VPRDLFTRQVHNKLISNRSNSPQVNASDWKVGFKLCNNNGSDCFYRTYTSGVQAVREWYRFHYINIFAQV
PAEDKDRMGYQLEDFILTCRFDGESCDARNFTHFHHPMYGNCYTFNSGENSNLLTSSMPGAENGLKLVLD
IEQDEYLPLLSTEAGARVMVHSQDEPPFIDDLGFGVRPGTETSISMQEDELQRLGGPYGDCTENGSDVPV
ENLYNSSYSIQACLRSCFQRYMVENCGCAYYHYPLPGGAEYCNYEQHPDWAYCYYKLYAEFDQEELGCFS
VCREPCNFTEYKLTLSMARWPSAASEDWLLHVLSRQNEYNITLIRNGIAKLNIFFEELNYRTIEESPAYN
VVTLLSNLGGQMGLWMGASVLCVLELLELIIDLIFITLLRLLWRFRKWWQRRRGPPYAEPPEPVSADTPP
SLQLDDPPTFPSALPLPHASGLSLPGTPPPNYNTL
>gnl|CDD|273305 TIGR00860, Neuronal_acetylcholine_receptor_subunit_alpha-7, Cation transporter family protein. The Ligand-gated Ion Channel (LIC) Family of Neurotransmitter Receptors TC 1.A.9)Members of the LIC family of ionotropic neurotransmitter receptors are found only in vertebrate and invertebrate animals. They exhibit receptor specificity for (1)acetylcholine, (2) serotonin, (3) glycine, (4) glutamate and (5) g-aminobutyric acid (GABA). All of these receptor channels are probably hetero- orhomopentameric. The best characterized are the nicotinic acetyl-choline receptors which are pentameric channels of a2bgd subunit composition. All subunits arehomologous. The three dimensional structures of the protein complex in both the open and closed configurations have been solved at 0.9 nm resolution.The channel protein complexes of the LIC family preferentially transport cations or anions depending on the channel (e.g., the acetylcholine receptors are cationselective while glycine receptors are anion selective) [Transport and binding proteins, Cations and iron carrying compounds]
LSQILLALLLFASLAAVSLAGNAKSNLKEVERKLLDELLKNYDARVRPVFGGPPVTVSFNLFLRSIMDVD
EKNMDYTTNIWLRQEWTDERLQWNPEEYPGVTLVRTPDDSIWVPDIFFYNEKDARFHGITMTNVLVRIHP
NGSVLYSPRITLTLACPMDLRNFPFDVQNCSLKFESWGYTTNDIKLEWKEQGAVQVDDSLFISLPEFELL
GVYGTRYCTSETNTGEYPCLTFSFVLRRRPLYYLLQLYIPSILIVILSWVSFWLPADASGARVSLGITTL
LTMTTFSSGVRESLPAVSYVKAIDVYFAVCMAFVFLALLETAFVNYVHHKDPAQGKRHLLLERCAWRLCK
QEPGEDYRRPALDHASLSSVEMRAKDGGRGLESPTERQRLLHSPPPAEGDLDLAGILEEVRIAHRFRKRD
ESEEVVRDWKFRAKVIDKLSRMAFPLAFLLFNIGYWMSY
>gnl|CDD|273306 TIGR00861, Glycerol_uptake_facilitator_protein, MIP family channel proteins. 1.A.8 The Major Intrinsic Protein (MIP) FamilyThe MIP family is large and diverse, possessing over 100 members that all form transmembrane channels. These channel proteins function in water, smallcarbohydrate (e.g., glycerol), urea, NH3, CO2 and possibly ion transport by an energy independent mechanism. They are found ubiquitously in bacteria, archaeaand eukaryotes. The MIP family contains two major groups of channels: aquaporins and glycerol facilitators.The known aquaporins cluster loosely together as do the known glycerol facilitators. MIP family proteins are believed to form aqueous pores that selectively allow passive transport of their solute(s) across the membrane with minimal apparent recognition. Aquaporins selectively transport water (but not glycerol) while glycerol facilitators selectively transport glycerol but not water. Some aquaporins can transport NH3 and CO2. Glycerol facilitators function as solute nonspecific channels, and may transport glycerol, dihydroxyacetone, propanediol, urea and other small neutral molecules in physiologically importantprocesses. Some members of the family, including the yeast FPS protein (TC #1.A.8.5.1) and tobacco NtTIPA may transport both water and small solutes [Transport and binding proteins, Unknown substrate]
AEFLGTFLLVFFGVGSALGVNVAGAYGAVGGGQFLGVALAFGLAVATLVYCVGGISGAHLNPAVTIALLL
GRRFPLKRVPVYIVAQLIGAILGAALLYGLTSGLFPGNLAVNGSASAGVSSGQAFFVEFIGTAILVLVIF
ATTDDRNRVPRGGFAPLAIGLLVFLIHLSMGPYTGTGMNPARSLGPALFAGLAGWGNHWVYWVGPIIGAI
LGALVY
>gnl|CDD|129941 TIGR00862, Chloride_intracellular_channel_protein_1, intracellular chloride channel protein. The Organellar Chloride Channel (O-ClC) Family (TC 1.A.12) Proteins of the O-ClC family are voltage-sensitive chloride channels found in intracellular membranes but not the plasma membranes of animal cells. They are found in human nuclear membranes, and the bovine protein targets to the microsomes, but not the plasma membrane, when expressed in Xenopus laevis oocytes. These proteins are thought to function in the regulation of the membrane potential and in transepithelial ion absorption and secretion in the kidney [Transport and binding proteins, Anions]
PEIELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPEDLQNLAPGTHPPFLTYNTEVKT
DVNKIEEFLEETLCPPRYPKLSPKHPESNTAGLDIFAKFSAYIKNSNPEANDNLEKGLLKALKKLDDYLN
SPLPEEIDEDSAEDEKVSRRKFLDGDELTLADCNLLPKLHIVKVVAKKYRNFDIPAEFTGVWRYLSNAYA
REEFTNTCPDDKEIELAYADVAKRLK
>gnl|CDD|273307 TIGR00863, P2X_purinoceptor_1, cation transporter protein. ATP-gated Cation Channel (ACC) Family (TC 1.A.7)Members of the ACC family (also called P2X receptors) respond to ATP, a functional neurotransmitter released by exocytosis from many types of neurons.These channels, which function at neuron-neuron and neuron-smooth muscle junctions, may play roles in the control of blood pressure and pain sensation. They may also function in lymphocyte and plateletphysiology. They are found only in animals.ACC channels are probably hetero- or homomultimers and transport small monovalent cations (Me+). Some also transport Ca2+; a few also transport small metabolites [Transport and binding proteins, Cations and iron carrying compounds]
MARRLAAGLSSFFFDYKTPKYVLVRNKKVGVIYRLVQLLILVYVIGWVFLAEKGYQESDTSPQSSVITKV
KGVAVTQTSELGNRVWDVADYVKPPQGENVFFVMTNFIVTPNQTQGRCPEHPSVPLAICWSDSDCTAGEA
GTHGNGIKTGRCVPFNGTVKTCEIFAWCPVEVDTVPSPPLLKEAENFTLFIKNSIRFPKFNFSKRNILET
WDATYLKTCLFDPDSDPYCPIFRLGDIVEEAGQDFQDLALKGGVVGITINWDCDLDKAASHCNPKYSFRR
LDNKEKNVSPGYNFRFAKYYRDNAGVETRTLLKAYGIRFDILVTGKAGKFDIIPTMITIGSGLASLGVGT
FLCDLILLYFMKKRHFYRDKKF
>gnl|CDD|188093 TIGR00864, PCC, polycystin cation channel protein. The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half
DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPL
LGIPLLDSGCDEEYVACLKDNSSGGGAARSELVIFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLC
GAAQPSEANFACESLCSGPPPPPAAACRGPQLLEHIFPALPGAPIQGPHGPIASGQLAAFHAAAPLAPTA
MRWDFGDGSAEVDAAGAGGTTAASHKYGHPGRYHVSAMGALGAGKALAGGDVQVEAAPAALELHCPSLVQ
ADESLDLSIQNRGGSDLDAAWKITAHGEEPAKASHPHCPKDGEIFEENGHCFQIVPEEAAWLDAQEQCLA
RAGAALAIVDNDALQNFLARKVTHSLDRGVWIGFSDVNGAEKGPAHQGEAFEAEECEEGLAGEPHPARAE
HCVRLDPRGQCNSDLCNAPHAYVCELNPGGPVPDAENFAMGAASFDLHGLLQALAAMDGLPAPPHEGVEV
LLFPALRFSRAAFLSSAEFGTQELRRPAHILFQIYRLRCRLPGAGGPACGPEAECRPPDNRSADAPACMK
GEQWCPFAHICLPLDAPCHPQACANGCSQGHGLPGAARMPLYALQREFLFSLPAGPAAHVLLQDHGEDLL
MLPGDLIALQHDAGPAALIHCQPAPGHPGPRAPVFAANASEWFGHNNTPVPPDNLAGDGADPLPDPELDL
KALLEGTRASWLECAACAIRLLAAGEQETRLLGAELNAGLPLPGLYELLAESAKGSDLHNASCSFDVLPP
LAGLRVIHPAPQDGRLFLESNGSALLLQVDSGANAEAKAFWPGGNSSARFENVCPAEFASRLCHPSTFEG
GCAEEAEDSLFAVLALNWLKEGEHTGPVQVDLMAENNASEANLSLLVQAEEPICGLRAQPHPAARVLMES
LVRYSASVEAGSDMTFKWTIDDKPFFTFQNTVFNVIYQHAAVFKLSLTAMNHVSNLTEDFNVTVDRLNPM
QGLQVKGVPAVLPPGATLALTAGVLIDMAVEAAFLWSFGDGEQALFEFKPPYNESFPCPDPSPAQVLLEH
NVMHIYAAPGEYLATVLASNAFENISQQINMSVRAILPRVAIGTEDGLLLAGKPADFEAHPLPSPGGIHY
EWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISGAAACADMFAFEEIEGLSADMSLATELGAAT
TVRAALQSGDNITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARIIHVEVFVFEVAGI
EPAACIGEHADANFRARVSGNAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLALTISSGVNKAH
FFTQICVEPELGKISLQAEKQFFALGDEAQFQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPG
CYLVTVAASNNISAANDSALIEVLEPVGATSFKHNGSHGNNLELGQPYLFSAFGRARNASYLWDFGDGGL
LEGPEILHAFNSPGDFNIRLAAANEVGKNEATLNVAVKARVRGLTINASLTNVPLNGSVHFEAHLDAGDD
VRFSWILCDHCTPIFGGNTIFYTFRSVGTFNIIVTAENDVGAAQASIFLFVLQEIEGLQILGETAEGGGG
GVQELDGCYFETNHTVQFHAGFKDGTNLSFSWNAILDNEPDGPAFAGSGKGAKLNPLEAGPCDIFLQAAN
LLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAELAEGSGLQYRWFLEEGDDLETSEPFMSHSF
PSAGLHLVTMKAFNELGSANASEEVDVQEPISGLKIRAADAGEQNFFAADSSVCFQGELATGTNVSWCWA
IDGGSSKMGKHACMTFPDAGTFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAAIGEKVEFQIL
LAAGSAVNFRLQIGGAAPEVLQPGPRFSHSFPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDC
CAAGIATGEEKNFTANVQRGKPVAFAWTFDLHHLHGDSLVIHMGKDVSYTAEAAGLLEIQLGAFNALGAE
NITLQLEAQDALMDAALQAGPQDCFTNKMAQFEAATSPKPNFMACHWDFGDGSAGQDTDEPRAEHEYLHP
GDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRSQPNLLEAHVDLKDCLRYGAEYLW
EILRAASCDNDGHFARGALNGATRSFPVIPLPAEVDVQRLQLSLPKLALAAGHYCFVFSLSFEDTPLKKA
ACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDPNLDDDDQSLLHFHWACQASSKGEAGCCALN
FGLGGKGPTLGIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQALYEVSQ
NSYVYLEGRCLNCQSGFHRGRWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEGYNFTLHVLDD
SGDEEGAASIRLHHNMPPDGGECHLFPGGETGQEHGDKEDEVWAIEALLDKVHFECSGWHDAEDAEAPLL
YALLLNRCRDDHCEEFCVYKGSLPEHGAFLPPGFRSAHFEVGLAITVEDHLGAAIRALNKSIAITLPDPN
GEASGLPHWLHDLIASKLKGLLDQADFQHVIELSLALITVLNEYEQALDSAAEPKHERGHRAQIRKNITE
ALTALDLHTVDDIQQIAAALAQCMAPSREFICEECLKQTLHKLEAMLEILQADTKAGIVTPTAIADNILN
IMGDLIHLAS
>gnl|CDD|273308 TIGR00865, Apoptosis_regulator_Bcl-2, apoptosis regulator. The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the apoptosis regulator, Bcl-X, and its homologues. Bcl-X is a dominant regulator of programmed cell death in mammalian cells. The long form (Bcl-X(L)) displays cell death repressor activity, but the short isoform (Bcl-X(S)) and the b-isoform (Bcl-Xb) promote cell death. Bcl-X(L), Bcl-X(S) and Bcl-Xb are three isoforms derived by alternative RNA splicing. Bcl-X(S) forms heterodimers with Bcl-2. Homologues of Bcl-X include the Bax (rat; 192 aas; spQ63690) and Bak (mouse; 208 aas; spO08734) proteins which also influence apoptosis. Using isolated mitochondria, recombinant Bax and Bak have been shown to induce Dy loss, swelling and cytochrome c release. All of these changes are dependent on Ca2+ and are prevented by cyclosporin A and bongkrekic acid, both of which are known to close permeability transition pores (megachannels). Coimmimoprecipitation studies revealed that Bax and Bak interact with VDAC to form permeability transition pores. Thus, even though they can form channels in artificial membranes at acidic pH, proapoptotic Bcl-2 family proteins (including Bax and Bak) probably induce the mitochondrial permeability transition and cytochrome c release by interacting with permeability transition pores, the most important component for pore fomation of which is VDAC [Regulatory functions, Other]
MAGSNRELVMKFISYKLSQRGGSWTAGEQIMKNGAPLLHGFIQHRAGPMTGETPSEGPPQDPPPSAVHQA
LRRAGDEFERRYRRAFSDMTSQLHITPFTARQSFFQVAAELFRDGVNWGRIVAFFSFGGALCVESVNKEM
SELVSRIAGWMTEYLNEHLHPWIQENGGWDGFVELYGNNAAQLFDFSWESFNTLLTAGLVTAVLTLGAYM
GRK
>gnl|CDD|273309 TIGR00867, Degenerin-like_protein_asic-2, degenerin. The Epithelial Na+ Channel (ENaC) Family (TC 1.A.06)The ENaC family consists of sodium channels from animals and has no recognizable homologues in other eukaryotes or bacteria. The vertebrate ENaC proteins from epithelial cells cluster tightly together on the phylogenetic tree: voltage-insensitive ENaC homologues are also found in the brain. Eleven sequenced C. elegans proteins, including the degenerins, are distantly related to the vertebrate proteins as well as to each other. At least some ofthese proteins form part of a mechano-transducing complex for touch sensitivity. Other members of the ENaC family, the acid-sensing ion channels, ASIC1-3,are homo- or hetero-oligomeric neuronal H+-gated channels that mediate pain sensation in response to tissue acidosis. The homologous Helix aspersa(FMRF-amide)-activated Na+ channel is the first peptide neurotransmitter-gated ionotropic receptor to be sequenced.Mammalian ENaC is important for the maintenance of Na+ balance and the regulation of blood pressure. Three homologous ENaC subunits, a, b and g, havebeen shown to assemble to form the highly Na+-selective channel.This model is designed from the invertebrate members of the ENaC family [Transport and binding proteins, Cations and iron carrying compounds]
DFCYKTTFHGIPMVATASNSFSRAFWVALFLICLLMFAYQAYILISKYFQYEKIVDIQLKFETAPFPAIT
VCNLNPYKYSLVRSVPEISETLDAFDRAIGASNKSEGDELELITERKLHSKTRRQKLKAKGAPELEDGMY
EPVFSQCTCDEQGMGECKSQRSAEPRGHTSRCICAYDRVTGDAWPCFPYSTWTTKKCSLCNDNGFCPKPN
KKGAKEQKDPCLCQSESNHCVSHPGKGIIREIWPNLENNDPTTGKPTTEAPETLEALGFGNMTDEVAITT
QAKENLIFAMAALSDKAREALSYTKHELILKCSFNGKPCDIDRDFTLHIDPVFGNCYTFNYNRSVNLSSS
RAGPMYGLRLLLFVNQSDYLPTTEAAGVRLTIHDKDEFPFPDTFGYSAPTGYISSFGVRLKQMSRLPAPY
GNCVDTGKDSSYIYKGYIYSPEGCHRSCFQRLIIAKCGCADPRFPVPEGTRHCQAFNKTDRECLETLTGD
LGELHHSIFKCRCQQPCQESIYTTTYSAAKWPSGSLKITLGSCDSNTASECNEYYRENAAMIEVFYEQLN
YELLTESEAYTLVNLIADFGGQLGLWLGASVITVCEFVFL
>gnl|CDD|129946 TIGR00868, Epithelial_chloride_channel_protein, calcium-activated chloride channel protein 1. The Epithelial Chloride Channel (E-ClC) Family (TC 1.A.13). Mammals have multiple isoforms of epithelial chloride channel proteins. The first member of this family to be characterized was a respiratory epithelium, Ca 2+-regulated, chloride channel protein isolated from bovine tracheal apical membranes. It was biochemically characterized as a 140 kDa complex. The purified complex when reconstituted in a planar lipid bilayer behaved as an anion-selective channel. It was regulated by Ca 2+ via a calmodulin kinase II-dependent mechanism. When the cRNA was injected into Xenopus oocytes, an outward rectifying, DIDS-sensitive, anion conductance was measured. A related gene, Lu-ECAM, was cloned from the bovine aortic endothelial cell line, BAEC. It is expressed in the lung and spleen but not in the trachea. Homologues are found in several mammals, and at least three paralogues(hCaCC-1-3) are present in humans, each with different tissue distributions [Transport and binding proteins, Anions]
MGPFRSVLFFLVLHLLEGAQSSMIQLNNNGYEGIVIAIDPSVPEDERLIQNIKDMVTKASTYLFEATEKR
FYFKNVSILIPMTWKSKPEYLMPKLESYKNADVIVAEPNLPHGDDPYTLQYGNCGEKGEYIHFTPDFLLG
KKLLIYGPRGRVFVHEWAHLRWGVFDEYNNDQPFYLSRNKKIEATRCSAAITGTNVVPKCQGGSCVTRPC
RRDSVTGLYEKKCTFIPDKQQTEKASIMFMQSIDSVVEFCTEKNHNKEAPNLQNKKCNLRSTWEVIQNSE
DFKNTTPMTTQPPPPTFSLLKIRQRIVCLVLDKSGSMTVEDRLKRMNQAAKLFLLQTVEKGSWVGMVTFD
SAAYIKNELIQITSSAERDALTANLPTAASGGTSICSGLKAAFQVIKKSYQSTDGSEIVLLTDGEDNTIS
SCFEEVKQSGAIIHTIALGPSAAKELEELSDMTGGLRFYASDQADNNGLIDAFGALSSGNGSASQQSIQL
ESKGLTLQNNAWMNGTVPVDSTVGKDTFFLITWEFLKPEIFLQDPSGKSTSDFLVDKLNKMAYLQIPGTA
KVGTWTYSLQASANPQTLTLTVTSRARSPTLPPVTVTAKMNKDTAKFPSPMIVYAKISQGFLPVLGANVT
ALIESENGHTVTLELLDNGAGADTVKNDGIYSRYFTAYDGNGRYSLKVRALGGVNTARLSLRPPWNKALY
IPGWIENGEIKLNPPRPDINKDDLQATQEDFSRTASGGSFVVSGVPPGPHPDVFPPSKITDLEAGFQGDN
IILTWTAPGDVLDHGRADRYIIRISTSILDLRDDFNDATQVNTTDLIPKEANSKEVFVFKPEGIPIENGT
DLFIAVQAIDKANLTSEVSNIAQ
>gnl|CDD|273310 TIGR00869, Translocation_protein_SEC62, protein translocation protein, Sec62 family. Members of the NSCC2 family have been sequenced from various yeast, fungal and animals species including Saccharomyces cerevisiae, Drosophila melanogaster and Homo sapiens. These proteins are the Sec62 proteins, believed to be associated with the Sec61 and Sec63 constituents of the general protein secretary systems of yeast microsomes. They are also the non-selective cation (NS) channels of the mammalian cytoplasmic membrane. The yeast Sec62 protein has been shown to be essential for cell growth. The mammalian NS channel proteins has been implicated in platelet derived growth factor(PGDF) dependent single channel current in fibroblasts. These channels are essentially closed in serum deprived tissue-culture cells and are specifically opened by exposure to PDGF. These channels are reported to exhibit equal selectivity for Na+, K+ and Cs+ with low permeability to Ca2+, and no permeability to anions [Transport and binding proteins, Amino acids, peptides and amines]
LRSHKELKQRPGILNGKRTDFFRVKRFVRALHSEEYANKSAKQPEIYPTIPSRLEAIEIFILLIKNQMVI
RVDKLPSQECKEHKQKPSQDFPHLQVNNKQQFEDDMYYVWNYNPRPYMDYLIVILVVSIILALVLFPLWP
RFMRRGSWYLSLGALGIIGGFFAVAILRLILFVLTLIVVKPGIWIFPNLFADVGFLDSFKPLWGWHEKDK
YSYKKKLKSKKLKKKQAKREAN
>gnl|CDD|273311 TIGR00870, Short_transient_receptor_potential_channel_4, transient-receptor-potential calcium channel protein. The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999) [Transport and binding proteins, Cations and iron carrying compounds]
RGPLDIVPAEESPLSDEEKAFLPAAERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIENENLELTE
LLLNLSCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELANDQYTSEFTPGITALHLAAHRQN
YEIVKLLLERGASVPARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNT
LLHLLVMENEFKAEYEELSCQMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAIK
YKQKKFVAWPNGQQLLSLYWLEELDGWRRKQSVLELIVVFVIGLKFPELSDMYLIAPLSRLGQFKWKPFI
KFIFHSASYLYFLYLIIFTSVAYYRPTRTDLRVTGLQQTPLEMLIVTWVDGLRLGEEKLIWLGGIFEYIH
QLWNILDFGMNSFYLATFLDRPFAILFVTQAFLVLREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRGN
QHLGPLQIMIGRMILGDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSNPHARSCEKQGNAYSTLF
ETSQELFWAIIGLGDLLANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQR
AKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGKKRQRWCRRVEEVNWTTWERKAETLIEDGLH
YQRVMKRLIKRYVLAEQRPRDDEGTTEEETKELKQDISSLRFE
>gnl|CDD|273312 TIGR00871, Glucose-6-phosphate_1-dehydrogenase, glucose-6-phosphate 1-dehydrogenase. This enzyme (EC 1.1.1.49) acts on glucose 6-phospate and reduces NADP(+). An alternate name appearing in the literature for the human enzyme, based on a slower activity with beta-D-glucose, is glucose 1-dehydrogenase (EC 1.1.1.47), but that name more properly describes a subfamily of the short chain dehydrogenases/reductases family. This is a well-studied enzyme family, with sequences available from well over 50 species. The trusted cutoff is set above the score for the Drosophila melanogaster CG7140 gene product, a homolog of unknown function. G6PD homologs from the bacteria Aquifex aeolicus and Helicobacter pylori lack several motifs well conserved most other members, were omitted from the seed alignment, and score well below the trusted cutoff [Energy metabolism, Pentose phosphate pathway]
DPCILVIFGASGDLARKKLFPALYRLFRNGLLPPDFRIVGVARRDWSVEEFRKVVREAIIKFETDEIDEQ
WDEFAQRLSYVSGDVDDDESYDSLAELLEQLDKTYGTEGNRLFYLATPPSLFGTIIKQLKKHGLNEQGKW
SRVVVEKPFGHDLASAQELNKALRAVFKEDQIYRIDHYLGKETVQNLLVLRFANQIFEPLWNRRYIDHVQ
ITVAESFGVEGRGGYYDKSGALRDMVQNHLLQLLALVAMEPPVSFDADSIRDEKVKVLKALRPIDPDDNN
TVRGQYGAGEIGGVSVPGYLEEEGVDKDSNTETFAALKLEIDNWRWAGVPFYLRTGKRLPEKVTEIRIQF
RDVPSLLFKANERDANPRNALVIRIQPDEGVYLKFNAKKPGLNFETRPVKLDFSYASRFGELLPEAYERL
LLDALLGDHTLFARDDEVEEAWRIVTPILEAWAANKGPSPPNYPAGSWGPKEADELIRKDGRSWRKP
>gnl|CDD|273313 TIGR00872, Putative_6-phosphogluconate_dehydrogenase_YqeC, 6-phosphogluconate dehydrogenase (decarboxylating). This family resembles a larger family (gnd) of bacterial and eukaryotic 6-phosphogluconate dehydrogenases but differs from it by a deep split in a UPGMA similarity clustering tree and the lack of a central region of about 140 residues. Among complete genomes, it is found is found in Bacillus subtilis and Mycobacterium tuberculosis, both of which also contain gnd, and in Aquifex aeolicus. The protein from Methylobacillus flagellatus KT has been characterized as a decarboxylating 6-phosphogluconate dehydrogenase as part of an unusual formaldehyde oxidation cycle. In some sequenced organisms members of this family are the sole 6-phosphogluconate dehydrogenase present and are probably active in the pentose phosphate cycle [Energy metabolism, Pentose phosphate pathway]
MQLGLIGLGRMGANIVRRLAKRGHDCVGYDHDQDAVKAMKEDRTTGVANLRELSQRLSAPRVVWVMVPHG
IVDAVLEELAPTLEKGDIVIDGGNSYYKDSLRRYKLLKEKGIHLLDCGTSGGVWGRERGYCFMIGGDGEA
FARAEPLFADVAPEEQGYLYCGPCGSGHFVKMVHNGIEYGMMAAIAEGFEILRNSQFDFDIPEVARVWRR
GSVIRSWLLDLTAIAFRESPDLAEFSGRVSDSGEGRWTVIAAIDLGVPAPVIATSLQSRFASRDLDDFAN
KVLAALRKEFGGHAEKKK
>gnl|CDD|273314 TIGR00873, 6-phosphogluconate_dehydrogenase_decarboxylating, 6-phosphogluconate dehydrogenase (decarboxylating). This model does not specify whether the cofactor is NADP only (EC 1.1.1.44), NAD only, or both. The model does not assign an EC number for that reason [Energy metabolism, Pentose phosphate pathway]
DIGVIGLAVMGQNLALNMEDHGFTVSVYNRTPSKTDEFLAEEAKGKSIIGAYSIEDFVQSLERPRKIMLM
VKAGAPVDAVIDSLLPLLEKGDIIIDGGNSHYPDTERRYKELKAKGILFVGSGVSGGEEGARKGPSIMPG
GSPEAWPLVAPIFQSIAAKVDGEPCCTWVGPGGAGHYVKMVHNGIEYGDMQLICEAYDILKRGLGLSNEE
IAEIFTEWNNGELDSYLIEITADILAKKDEDGNPLVDKILDTAGQKGTGKWTAINALDLGVPLTLITESV
FARYLSSLKEERVAASKVLPGPEAPKKGVDKEEFIEDVRQALYASKIISYAQGFMLLREASEEYGWDLNL
GEIALIWRGGCIIRSVFLDKITKAFAENPDLENLLLAPYFKQALTDAQSGWRKVVALAITYGIPVPAFSA
ALSFYDGYRTARLPANLLQAQRDYFGAHTYERTDKPRGEFFHTNWTG
>gnl|CDD|162081 TIGR00874, Transaldolase_NQM1, transaldolase. This family includes the majority of known and predicted transaldolase sequences, including E. coli TalA and TalB. It excluded two other families. The first includes E. coli transaldolase-like protein TalC. The second family includes the putative transaldolases of Helicobacter pylori and Mycobacterium tuberculosis [Energy metabolism, Pentose phosphate pathway]
NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVEN
ALDKLAVNFGLEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRA
AEELEKEGIHCNLTLLFSFVQAIACAEAKVTLISPFVGRILDWYKAATGKKEYSIEEDPGVASVKKIYNY
YKKHGYPTEVMGASFRNKEEILALAGCDRLTISPALLDELKESTGPVERKLDPESAKKVDKQPIILDESE
FRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEKL
>gnl|CDD|129953 TIGR00875, Probable_transaldolase, fructose-6-phosphate aldolase, TalC/MipB family. This model represents a family that includes the E. coli transaldolase homologs TalC and MipB, both shown to be fructose-6-phosphate aldolases rather than transaldolases as previously thought. It is related to but distinct from the transaldolase family of E. coli TalA and TalB. The member from Bacillus subtilis becomes phosphorylated during early stationary phase but not during exponential growth [Energy metabolism, Pentose phosphate pathway]
MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRSFWEVLKEIQEAVEGPVSAETISLDAEGMVEEA
KELAKLAPNIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDG
MKLIEEVKTIFENHAPDTEVIAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWN
AAF
>gnl|CDD|129954 TIGR00876, tal_mycobact, transaldolase, mycobacterial type. This model describes one of three related but easily separable famiiles of known and putative transaldolases. This family and the family typified by E. coli TalA and TalB both contain experimentally verified examples [Energy metabolism, Pentose phosphate pathway]
AEFSLWCDDIERDFLENGDFLELIDKGAICGATSNPSIFCEAISEGAFYDAEIAELAAKGADADAIIETL
ALDDILQACDALMPLWEDSDGNDGRISIEIDPFLADDAAKSIDEAIELFKILDRPNLFIKIPASEAGIEA
ISALLAAGIPVNVTLIFSPKIAGEIADALAKEAEKARQAGHSLSKIHAVASFFVSRFDKEIDKLLDKIGS
RQALELQAQAGIANARLAYATYREVFEDSDCYRQIKQDAAKLQRPLFASTGVKNNDLADDLYIKALCAKH
SINTAPEEAIDAVADDGNIECDTPLGTASDAEAFFDELGAHGIDLEDTAAKLEEEGLIAFEASFEELLQE
>gnl|CDD|273315 TIGR00877, Phosphoribosylamine--glycine_ligase, phosphoribosylamine--glycine ligase. Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAII
GPEAPLVLGLVDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGA
PIVVKADGLAAGKGVIVAKTNEEAIKAVEDILEQKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPP
AQDHKRALEGDKGPNTGGMGAYSPAPVFTEEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGP
KVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDEVELRFDNRAAVTVVLASEGYPEDYRKGDPIT
GEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERAYEAVEYIKFEGMFYRKDIGFRA
LE
>gnl|CDD|273316 TIGR00878, Phosphoribosylformylglycinamidine_cyclo-ligase, phosphoribosylaminoimidazole synthetase. Alternate name: phosphoribosylformylglycinamidine cyclo-ligase; AIRS; AIR synthase This enzyme is found as a homodimeric monofunctional protein in prokaryotes and as part of a larger, multifunctional protein, sometimes with two copies of this enzyme in tandem, in eukaryotes [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGDKYKEPVLVSGTDGVGTKLLVAEA
MNKHDTIGIDLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMP
GMYRGGHYDLAGTAVGVVEKDEIITGEKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDYEDTPEEF
GKTLGEELLEPTRIYVKPILELIKSVIVHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQ
EAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLNAYGEKAWVIGEVKKG
>gnl|CDD|273317 TIGR00879, Membrane_transporter, MFS transporter, sugar porter (SP) family. This model represent the sugar porter subfamily of the major facilitator superfamily (pfam00083) [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MSDANLADASELLVTPAGLGSTYWKVALLSLIAAIGGLMFGYDTGVIGGALALPAFEFKFTSANSDSYSS
SLWGLVVSIFLVGGFIGALFAGWLSDRFGRKKSLLIIALLFVIGAILMGLAAFALSVEMLIVGRVLLGIG
VGIASALVPMYLSEIAPKALRGALTSLYQLAITFGILVAYGFGSGKVSLNNTLGWRIPLGLQLIPAGLLF
LGLFFLPESPRWLVGKGRVEEARKSLARLRGTSGEDKELLDELELIDIKRSIEKRSVQPSWGSLFSSTRR
IRRRLFLGVVLQWFQQFTGINAIMYYSPTIFENAGVSTDHAFLVSIIVGAVNFAFTFVAIFLVDRFGRRP
LLLIGAAGMAICLFVLGILGASFVTGSSKSSGNVAIVFILLFIAFFAMGWGPVPWVIVSEIFPLSLRPKG
ISIAVAANWLANFIVGFLFPTMLESIGVGGVFIFFGGLNVLGLIFVYFFLPETKGRTLEEI
>gnl|CDD|273318 TIGR00880, Chromaffin_granule_amine_transporter, Multidrug resistance protein
GLLLAGYALGQLIYSPLSGLLTDRFGRKPVLLVGLFIFVLSTAMFALSSNITVLIIARFLQGFGAAFALV
AGAALIADIYPPEERGVALGLMSAGIALGPLLGPPLGGVLAQFLGWRAPFLFLAILALAAFILLAFLLPE
T
>gnl|CDD|273319 TIGR00881, Glycerol-3-phosphate_transporter, phosphoglycerate transporter family protein [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
FIGYAAYYLVRKNFALAMPYLVEEIGLSKTDLGLLLSSFSIAYGISKFVMGSVSDRSNPRVFLPIGLILC
AIVNLFFGFSTSLWVMAALWALNGIFQGMGWPPCGRTVTKWFSRSERGTWVSFWNCSHNVGGGLLPPLVL
FGIAELYSWHWVFIVPGIIAIIVSLICFLLLRDSPQSCGLPPAEEMPNEEPDGDAEKKEEELTKKQIFLQ
YVLLNKVLWYISLGYVFVYVVRTGILDWSPLYLTQEKGFSKEKASWAFTLYELGGLVGTLLAGWLSDKLF
NGRRGPLAVFFMALIIVSLLVYWLNPAANPLMDLICLFALGFLVYGPQMLIGVIASELAPKKAAGTAAGF
VGFFAYLGGILAGLPLGYLADGFGWAGAF
>gnl|CDD|211613 TIGR00882, Lactose_permease, oligosaccharide:H+ symporter [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
NTNFWMFGLFFFLYFFIMSAYFPFFPIWLHDVNGLSKTDTGIVFSCISLFSILFQPLFGLISDKLGLKKH
LLWIISGLLVLFAPFFIYVFGPLLQSNILVGAIVGGLYLGFVFSAGAGAIEAYIEKVSRNSNFEYGKARM
FGCVGWALCASIAGILFSIDPQIVFWLGSGFALILMLLLMFAKPKAPSSATVANALGANASAFSLKLALE
LFRQRKFWMFVLYVVGVACVYDVFDQQFANFFTSFFATPQQGTRVFGYVTTMGELLNALIMFCAPLIINR
IGAKNALLIAGTIMSVRIIGSSFATTALEVVILKMLHAFEVPFLLVGCFKYITSQFDVRLSATIYLIGFQ
FAKQLAMIFLSTLAGNMYDSIGFQGAYLVLGCIVLLFTLISVFTLS
>gnl|CDD|273320 TIGR00883, Putative_metabolite_transport_protein, metabolite-proton symporter. This model represents the metabolite:H+ symport subfamily of the major facilitator superfamily (pfam00083), including citrate-H+ symporters, dicarboxylate:H+ symporters, the proline/glycine-betaine transporter ProP, etc [Transport and binding proteins, Unknown substrate]
GNAVEWFDFYLYGFAAVLVFHTFFPPSGDPLVALLATFATFAAGFLARPLGAIVFGHFGDRIGRKKTLVI
TLLMMGIGTLLIGLLPSYATIGIWAPILLLLARLIQGFSLGGEWGGAALYLAEYAPPGKRGFYGSFQQVG
APVGLLLAALTVLLLSYLLGDDALLEWGWRIPFLVSAVLVLIGLYLRRNLEETPVFEKAQEKHKKKRGPI
AETLTKHRKPFLLGLGLVIATTTTFYLITTYLPTYLTQTLGLSANSALLVLMLSLILFFITIPLSGALSD
RIGRRPVLIIFTVLAALLAVPLLMALLDSGSFTLFFFLVLGMALIGGMYTGPMGSFLPELFPTEVRYTGA
SLAYNLAGAIFGGFAPYIAAALVAMTGDWYAIGYYLAALALIGL
>gnl|CDD|273321 TIGR00884, GMP_synthase, GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit. This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This C-terminal region would be the larger subunit [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
NFIEEAVEEIREQVGDAKVIIALSGGVDSSVAAVLAHRAIGDRLTCVFVDHGLLRKGEAEQVVKTFGDRL
GLNLVYVDAKERFLSALKGVTDPEEKRKIIGRVFIEVFEREAKKIGDAEYLAQGTIYPDVIESAAGTAHV
IKSHHNVGGLPEDMKLKLVEPLRELFKDEVRKLGKELGLPEEIVWRHPFPGPGLAVRVLGEVTKEKLEIL
RRADAIVIEELKKAGLYDKVWQAFAVLLPVKSVGVMGDGRTYGYVIALRAVESIDGMTADWARLPYDFLE
RISNRITNEVPGVNRVVYDITSKPPATIEWE
>gnl|CDD|211614 TIGR00885, L-fucose-proton_symporter, L-fucose:H+ symporter permease. This family describes the L-fucose permease in bacteria. L-fucose(6-deoxy-L-galactose) is a monosaccharide found in glycoproteins and cell wall polysaccharides. L-fucose is used in bacteria through an inducible pathway mediated by atleast four enzymes: a permease, isomerase, kinase and an aldolase which are encoded by fucP, fucI, fucK, fucA respectively. The fuc genes belong to a regulon comprising of four linked operons: fucO, fucA, fucPIK and fucR. The positive regulator is encoded by fucR, whose protein responds to fuculose-1-phosphate, which acts as an effector [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
YIIPFALITSLFALWGFANDITNPMVPQFQQAFTLTAFQAALVQSAFYGGYFIMAIPAAIFMKKLSYKAG
ILLGLFLYALGAFLFWPAAEIMNYTLFLVGLFILTAGLGFLETAANPYILVMGPESTATRRLNLAQSFNP
FGSIIGMVVAQQLILSNLPHQSQDVLDKLSPEELSAIKHSDLASVQTPYMIIGAVVLAVALLIMLTKMPA
LNHSDAKQISFSASLSRLARIRHYREGVIAQFFYVGVQIMCWTFIIQYAVRLIPGMTAGFAANYNIGAMV
IFFISRFIGTWLISYLAAHKVLMAYAIIGMALCLGSIFAGGHVGLYCLTLCSAFMSLMFPTIYGIALKGL
GQDTKYGAAGLVMAIIGGGIVPPLQGFIIDMKEIAAAPAVNTSFILPLLCFAVIFIYG
>gnl|CDD|273322 TIGR00886, Nitrate/nitrite_transporter_NarK, nitrite extrusion protein (nitrite facilitator) [Transport and binding proteins, Anions]
RNLFFSWFGFFLSFLVWFAFSPLAVFLIKDDLGLSTAQLGNLVAVPVLAGAVLRIILGFLVDIFGPRYTT
ALSLLLLAIPCLWAGLAVQSYSVLLLIRLFIGIAGGSFASCMPWISFFFPKKIQGTALGLAAGWGNMGGG
VAQFVMPPIIGSLIFGGGQPAHLAWGWAFVIVPAGILLLPALLIFFVGADTPPGKPATGKLSFKEALKVF
GNRHTWILALLYSVTFGSFLGVSSIFAMLFKDQFGLSKVQAGAYASLGGFLGSLARPAGGAISDRLGGAR
KLLMNFLGVAMGAFLVVLGLVSDGSLAAFIVLFVALFFFAGAGNGSTFALVPHIFRRATGAVSGLIGAIG
NLGG
>gnl|CDD|129965 TIGR00887, Inorganic_phosphate_transporter_PHO84, phosphate:H+ symporter. This model represents the phosphate uptake symporter subfamily of the major facilitator superfamily (pfam00083) [Transport and binding proteins, Anions]
ALEEADTAPFGWQHFRAIVIAGVGFFTDSYDLFCISLVTKMLGYVYYHGKGPLPSSVSAAVNGSASIGTL
AGQLFFGWLADKLGRKRVYGMELIIMIIATVASGLSPGSSPKSVMATLCFWRFWLGVGIGGDYPLSAIIT
SEFATKKWRGAMMAAVFAMQGFGILAGAIVALIVLAGFKHSLEAAADEASCTGSCVPAVDYMWRILIGFG
AVPALLALYFRLTIPETPRYTADVAKDVEQAASDMSAVLQVKIEAEPDEVEKASTAVEVPKASWSDFFTH
FFKWRHGKHLLGTAGSWFLLDIAFYGVNLNQKVILSAIGYSPPAATNNAYEELYKTAVGNLIIALAGTVP
GYWVTVFLVDIIGRKPIQLMGFFILTVLFFVLGFAYNHLSTHGFLAIYVLAQFFANFGPNATTFIVPGEV
FPTRYRSTAHGISAASGKAGAIIGQFGFLYLAQHGDPTKGYPTGIWMGHVLEIFALFMFLGILFTLLIPE
TKGKSLEELSGE
>gnl|CDD|129966 TIGR00888, GMP_synthase, GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit. This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELG
VPVLGICYGMQLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKELPEGFKVL
ATSDNCPVAAMAHEEKPIYGVQFHPEVTHTEYGNELLENFVYDVCGCE
>gnl|CDD|129967 TIGR00889, Putative_nucleoside_transporter_YegT, nucleoside transporter. This family of proteins transports nucleosides at a high affinity. The transport mechanism is driven by proton motive force. This family includes nucleoside permease NupG and xanthosine permease from E.Coli [Transport and binding proteins, Nucleosides, purines and pyrimidines]
MKTTAKLKFMSFLQWFIWGSWLVTLGSYMSKTLHFSGAEIGWVYSSTGIAAILMPILVGIIADKWLSAQK
VYAVCHFAGALLLFFAAQVTTPAGMFPVLLANSLAYMPTIALTNSISYANLPQAGLDVVTDFPPIRVMGT
IGFIAAMWAVSLLDIELSNIQLYITAGSSALLGVFALTLPDIPVAKSTAKMSIKVMLGLDAFILFKNKRM
AIFFFFSMLLGAPLQITNIFGNGFLHEFGRNPEFADSFVVKNASIWMSLSQFSEIFFILTIPFFLKRFGI
KKVMLLSLVAWALRFGFFAYGDPEYFGYALLFLSMIVYGCAFDFFNISGSVFVEKEVPVHIRASAQGLFT
LMCNGFGSLLGYILSGVMVEKMFAYGTFDWQTMWLFFAGYIAILAVLFMIFFKYSHNAIKVDDRDVAH
>gnl|CDD|273323 TIGR00890, Uncharacterized_MFS-type_transporter_YhjX, oxalate/formate antiporter family transporter. This subfamily belongs to the major facilitator family. Members include the oxalate/formate antiporter of Oxalobacter formigenes, where one substrate is decarboxylated in the cytosol into the other to consume a proton and drive an ion gradient [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
RWWYVLVGTVIMCFTSGYVYTWTLLAPPLGRYFGVGVTAVAIWFTLLLIGLAMSMPVGGLLADKFGPRAV
AMLGGILYGLGFTFYAIADSLAALYLTYGLASAGVGIAYGIALNTAVKWFPDKRGLASGIIIGGYGLGSF
ILSPLITSVINLEGVPAAFIYMGIIFLLVIVLGAFLIGYPPGQLIKTNIEVSVKDYTVWEMLRTPQFWVL
YLSFFLNAVSGLLLIGLYKPYGQSLGLSDGFLVLAVSISSIFNGGGRPFLGALSDKIGRQKTMSIVFGIS
AVGMAAMLFIPMLNDVLFLATVALVFFTWGGTISLFPSLVSDIFGPANSAANYGFLYTAKAVAGIFGGLI
ASHALTEIGFEYTFIVTGAFALTSLAL
>gnl|CDD|273324 TIGR00891, Carboxylic_acid_transporter_protein_homolog, putative sialic acid transporter [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
PWYRHLTRAQWNAFSAAWLGWLLDAFDFFLVALVLAEVAGEFGLTTVDAASLISAALISRWFGALMFGLW
GDRYGRRLPMVTSIVLFSAGTLACGFAPGYITMFIARLVIGIGMGGEYGSSAAYVIESWPKHLRNKASGL
LISGYAVGAVVAAQVYSLVVPVWGDGWRALFFISILPIIFALWLRKNIPEAEDWKEKHAGKALVRTMVDI
LYGGEHRIANIVMTLAAAMVQSAGKRWPTFVYLVVLVLFANLYSHPIQDLLPTYLKADLGLSPHTVANIV
VFSNIGAIVGGCVFGFLGDWLGRRKAYVCSLLAGQLLIIPVFAIGANVAVLGLGLFFQQMLVQGIWGILP
KHLGEYFPTDQRAAGLGFTYQLGNLGGALAPIIGALLAQRLDEYGTALASLSFSL
>gnl|CDD|273325 TIGR00892, Monocarboxylate_transporter_2, monocarboxylate transporter 1 [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MPPALPPEGPPPDGGWGWVVLGATFVSIGFSYAFPKAVTVFFKELQQIFQATYSETAWISSIMLAVLYAG
GPISSILVNRFGCRPVVIAGGLLASLGMILASFSSNVIELYLTAGFITGLGLAFNFQPSLTMLGKYFYRR
RPLANGLAMAGSPVFLSTLAPLNQYLFESFGWRGSFLILGGLLLHCCVCGALMRPVGPSQRVSKSKSKEG
LPPDGSTKKLSKKSTAEKINRFLDFSLFTHRGFLVYLSGNVIMFLGFFAPIIFLVPYAKDKGVDEYEAAF
LLSIIGFVDIFARPSCGLIAGLKWIRPHVQYLFSFALLFNGLTHLLCALAGDYTGLVIYCIFFGLSFGSV
GALLFEVLMDLVGAQRFSSAVGLVTIVECCAVLIGPPLAGRLVDATKNYKYIFYASGSIVVSAGLFLAIG
NYINYRLLAKEQKAALEREGARDKKDAEGDSRESE
>gnl|CDD|273326 TIGR00893, Probable_glucarate_transporter, D-galactonate transporter [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
LVTVINYLDRANLSFAAPMLQEDLGLSAAQYGYVFSAFSWGYVVGQFPGGWLLDRFGARKTLAVFIVIWG
VFTGLQAFAGAYVSLYILRVLLGAAEAPFFPGIILIVASWFPASERATAVSIFNSAQGLGGIIGGPLVGW
ILIHFSWQWAFIIEGVLGIIWGVLWLKFIPDPPQKAKWLTEEEKYIVVGGLLAEQQGKGPSTPKKYQIKE
LLKDRRVWGLALGQFLVNIGLGFFLTWFPTYLVQERGLSILEAGFMASLPGIVGFIGMILGGRLSDLLLR
RGKSLVFARKTAIIAGLVLSLLMFATNYVNIPYAALALVALGFFGLGAGAIGWALISDNAPGNIAGLTGG
LINSLGNLGGIVGPIVIGAIAATTGSFAGALMVVAALALIGALSYLLLV
>gnl|CDD|129972 TIGR00894, Sodium-dependent_phosphate_transport_protein_1, Na(+)-dependent inorganic phosphate cotransporter [Transport and binding proteins, Anions]
MENVFASTKLPYFCSFRLFLSFLLHICNVIIIAQRICLSLTMVAMVNKENSTDLACLSAENELDNIKNPN
FKWSGALQGLILSSHFYGQIIIQIPVGYLAGKYVFKWSIGIGMFLSSVISIVIPWAAGGGIALVVFCRVI
QGLAQGSVSPATHKIIVKWAPPKERSRLLGMSTSGFQLGTFIFLPISGWLCESWGGWPMIFYVFGIVGCA
WSLLWFVFPADDPSIHPCISKFEKKYINSSLQGQKGSTRQSLPIKAIPKSLPVWAIWFAIFGHFWLYTIL
PTYLPTFISWVLRVSGKENGLLSSLPYLFAWLCSIFAGYLADFLKSSKTLSLTAARKIFNGIGGLGPGIF
AYALPYLSAAFYLTIIILTLANAVSSGPLAGVLINSLDLAPRFLGFIKGITGLPGFIGGLIASTLAGNIL
SQDSKNVWLIVFLIMAFVNILCVIFYLIFGSAERQDWAKEEKDTR
>gnl|CDD|273327 TIGR00895, transport_protein, benzoate transport [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
DVQNNIRKQPLSRYQWRAIILSFLIMLMDGYDLAAMGFAAPAISAEWGLDPVQLGFLFSAGLIGMAFGAL
FFGPLADRIGRRRVLLWSILLFSVFTLLCALATNVTQLLILRFLAGLGLGGLMPNLNALVSEYAPKRFRG
TAVGLMFCGYPIGAAVGGFLAGWLIPVFGWRSLFYVGGIAPLLLLLLLMRFLPESIDFLVSKRPETVRRI
VNAIAPQMQAEAQSALPEQKSTQGTKRSVFKALFQGKTARITVLLWLLYFMLLVGVYFLTNWLPKLMVEL
GFSLSLAATGGALFNFGGVIGSIIFGWLADRLGPRVTALLLLLGAVFAVLVGSTLFSPTLLLLLGAIAGF
FVNGGQSGLYALMALFYPTAIRATGVGWAIGIGRLGAIIGPILAGYLL
>gnl|CDD|129974 TIGR00896, Inner_membrane_transport_protein_YeaN, cyanate transporter. This family of proteins is involved in active transport of cyanate. The cyanate transporter in E.Coli is used to transport cyanate into the cell so it can be metabolized into ammonia and bicarbonate. This process is used to overcome the toxicity of environmental cyanate [Transport and binding proteins, Other]
LILGIVLIALNLRPALTSVGPLLPQIRSALGMSFSVAGLLTALPVLCFAVLAPLAPWLARRFGEERSVAA
GLLLIAAGILIRSAPGTALLFAGTALIGVGIAIINVLLPSLIKRDFPQRVGLMTGLYSMALMGGAALAAA
ATVPLAQHSGGHWQQALAWWALPALLALLAWIPQVRRRVAANQTTTRLTPVRIWRSPLAWQVTVFFGLQS
GLYYSLIGWLPAILISHGASAATAGSLLALMQLAQAASALLIPALARRVKDQRGIVAVLAVLQLVGLCGL
LFAPMHGLWAWALVLGLGQGGAFPLALTLIGLRSRQAAQAAALSAMAQSIGYLLAALGPLFVGVLHDISG
NWLMP
>gnl|CDD|162096 TIGR00897, Alpha-ketoglutarate_permease, polyol permease family. This family of proteins includes the ribitol and D-arabinitol transporters from Klebsiella pneumoniae and the alpha-ketoglutarate permease from Bacillus subtilis [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MSINNLQKIGIPLNLLWGYIGVVVFMTGDGLEQGWLSPFLKALGLSPQQSASAFTLYGIAAAISAWISGV
VAEIIGPLKTMMIGLLLWCVGHAAFIVFGLGHANYPLILLFYGIRGLGYPLFAYSFLVWVVYNTKQDNLS
SAVGWFWAVYSIGIGVFGSYYSSYAIPAFGEMNTLWSALAFVLTGGVIALFSNKDIFTPQHMQTREKFSE
LGKAATILFTNPNVLLGGMVRIINTIGLFGFAVFLPMFVAELGFSTSEWLQIWGTFFFTNIVFNVIFGIV
GDKLGWMNTVRWFGGVGCGIFTLALYYIPQHFGHSFAVALIIAIALGIFLAGYVPLAAVFPTLAPKHKGA
AMSVLNLSAGLSAFLAPAIAVLFIGFFGAIGVVWIFAALYVVSAFLTAFIRI
>gnl|CDD|273328 TIGR00898, organic_anion_transporter, cation transport protein [Transport and binding proteins, Cations and iron carrying compounds]
GEFGPFQRRTFLLLALPIALLAFHFVLIVFLGATPEHHCRLPDAANLSSRCELNLTLPRLPDGRPESCLR
FMVDQWANPSLLGCEPLKLSDLGLAATEPCLDGWEYSYDTFSSTIVTEWDLVCEDAWKVDLTQSCFFVGV
LLGSFVFGYLSDRFGRKKVLLLSTLVTAVSGVLTAFSPNYTVFLVFRLLVGMGIGGIWVQAVVLNTEFLP
KKQRAIVGTLIQVFFSLGLVLLPLVAYFIPDWRWLQLAVSLPTFLFFLLSWFVPESPRWLISQGRIEEAL
KILQRIAKINGKKLPAEVLSLSLEKDLSSSKKQYSFLDLFRTPNLRKTTLCLMMLWFTTAFSYYGLVLDL
GNLGGNIYLDLFISGLVELPAKLITLLLIDRLGRRYTMAASLLLAGVALLLLLFVPVDLYFLRTALAVLG
KFGITSAFQMVYLYTAELYPTVVRNLGVGVCSTMARVGSIISPFLVYLGEKWLFLPLVLFGGLALLAGIL
TLFLPETKGVPLPET
>gnl|CDD|129977 TIGR00899, Sugar_efflux_transporter_A, sugar efflux transporter. This family of proteins is an efflux system for lactose, glucose, aromatic glucosides and galactosides, cellobiose, maltose, a-methyl glucoside and other sugar compounds. They are found in both gram-negative and gram-postitive bacteria [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
AFLLVAFLTGIAGALQFPTLSLFLSEEVRARPAMIGLFYTGSAIVGIAVSQLLATRSDYQGDRKGLILFC
CLLAALACLLFAWNRNYFLLLVLGVLLSSFASTANPQLFALAREHADRTGREAVMFSSVMRAQISLAWVI
GPPLAFWLALGFGFTVMFLTAALAFVLCGVLVWLFLPSYPRGAPGALTRLEVRGLLASRDTRLLFVACTL
MWGCNILYIINMPLLIIHELGLPDKLAGLMMGTAAGLEIPFMLLAGYLIKRFGKRRLMLLAALAGVAFYT
GLAADNSLWALLMLQLLNAIFIGILAGIGMLYFQDLMPGRAGAATTLYTNTGRVGWIIAGSVGGILAERW
SYHAVYWFAIVMLIVALFCLLLIKD
>gnl|CDD|162098 TIGR00900, multidrug_transporter, H+ Antiporter protein [Transport and binding proteins, Cations and iron carrying compounds]
FRLLFAAQLISLIGTAITQVALPLYVLAGTGSASVLSLAALAGMLPYVVLSPIAGALADRYDRKKVMIGA
DLIRAVLVAVLPFVALLGGLNIWQVYVLAGILAIAQAFFTPAYQAMLPDLVPEEQLTQANSLSQAVRSLF
YIVGPGIGGLMYATLGIKWAIWVDAVGFAISALLIVSVRIPELAASEIQALSNAVLRDTREGIKFVLKNP
LLRTLLLLALLFNLVFAPAIVALFPYVQSKYLGRGSTHYGWVLAAFGLGALLGALLLGLLGRYFKRMALM
TGAIFVIGLAILVVGLTPPNFPLFLVLWFAIGVGYGPINVPQGTLLQRRVPAELLGRVFGAQFSLSHAAW
PLGLILAGPLADHLG
>gnl|CDD|273329 TIGR00901, Uncharacterized_protein_HI_0350, AmpG-like permease [Cellular processes, Adaptations to atypical conditions]
GLPLGLVGNTLPYWLRSKNVSLKTIGFFSLVGLPYSLKFLWSPLVDTVYLPFFGRRRSWLVLTQVLLLSL
LLILSFLVPSTDLPLLAGLAFLIAFFSATQDIALDAWRLEILSDEELGYGSTIYIVGYRAGMLLSGSLAL
VLASPEFANTGLITLWGYIFFWTALLILPGLLVTLFLAKEPQEDASVPKPLTQAVLKPIREFFQRKNMIQ
ALLLLLLIVLYKLGDSAATVLTTLFLLDMGFSKEEIALVAKINGLLGAILGGLIGGIIMQPLNILYALLL
FGIVQALTNAGFVWLASNGHHDGITFPHLLMLFLTITLEAVTGGLGTVAFVAFLSKLSNPKFGATQMALL
SSLSAL
>gnl|CDD|129980 TIGR00902, Probable_3-phenylpropionic_acid_transporter, phenyl proprionate permease family protein. This family of proteins is involved in the uptake of 3-phenylpropionic acid. This uptake mechanism is for the metabolism of phenylpropanoid compounds and plays an important role in the natural degradative cycle of these aromatic molecules [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MQLQPFRWLALGFFGYFCAYGIFLPFFPAWLKGIGLGEEMIGLLIGAALIARFAGGLFFAPLIKDANHII
IALRLLALASAIFAAAFSAGAHNAWLLFIAIGLFALFFSAGMPIGDALANTWQKQFGLDYGKVRLIGSAA
FIIGSALFGGLIGMFDEQNILAILTAGLAFMLIGFLIKPTIPPKDAIPEDESQGDSAFIALLKNPMNLRF
LAAVCLIQGAHAAYYGFSAIYWQAAGISASATGLLWGIGVLAEIIIFAFSNKLFQNCSARDLLLISAIAC
VGRWAIIGAIEAFPLIFLLQILHCGTFAVCHLAAMRYIAAQPGSEIAKLQALYNALAMGGLIAIFTAFAG
FIYPTLGAGTFVFMAIIAAAAFFLIPKKLNAC
>gnl|CDD|129981 TIGR00903, 2A0129, major facilitator 4 family protein. This family of proteins are uncharacterized proteins from archaea. This family includes proteins from Archaeoglobus fulgidus and Aeropyrum pernix [Transport and binding proteins, Other]
FASQAIWVTFSPVLSLVAEDIDVSKEELGLLAITYPAAFLALTIPSGLLLDRAFKRWFLFGSLATFAAAA
GRLLDPFNYEWLLACQLLAALGQPFLLNAFAPAASQIREERRDLVISLLSFAMYLGIIFALAAGLKIYTA
GGLQLLIIPIAAVAAAGIILVLAALPALPFQAAEGFGFKDAVKEFGALAGRKDLWIIGAILGFGVALFDN
LAIWLEAALRPAGLEDIAGDAVALAILAGLIGVAVIPDRVARAGLRSIYIRAAALLIAAFFLALAFELNR
LALFAFIGIAGLLMLPAYAIIMDWIGKFCDKELHGKAAGAIGFTSRAISVALALAAMLFISSAEAYFTFL
AILITIAFAIALLLPNDR
>gnl|CDD|129982 TIGR00904, mreB, cell shape determining protein, MreB/Mrl family. MreB (mecillinam resistance) in E. coli (also called envB) and the paralogous pair MreB and Mrl of Bacillus subtilis have all been shown to help determine cell shape. This protein is present in a wide variety of bacteria, including spirochetes, but is missing from the Mycoplasmas and from Gram-positive cocci. Most completed bacterial genomes have a single member of this family. In some species it is an essential gene. A close homolog is found in the Archaeon Methanobacterium thermoautotrophicum, and a more distant homolog in Archaeoglobus fulgidus. The family is related to cell division protein FtsA and heat shock protein DnaK [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
FSSDIGIDLGTANTLVYVKGRGIVLNEPSVVAIRTDRDAKTKSILAVGHEAKEMLGKTPGNIVAIRPMKD
GVIADFEVTEKMIKYFIKQVHSRKSFFKPRIVICVPSGITPVERRAVKESALSAGAREVYLIEEPMAAAI
GAGLPVEEPTGSMVVDIGGGTTEVAVISLGGIVVSRSIRVGGDEFDEAIINYIRRTYNLLIGEQTAERIK
IEIGSAYPLNDEPRKMEVRGRDLVTGLPRTIEITSVEVREALQEPVNQIVEAVKRTLEKTPPELAADIVE
RGIVLTGGGALLRNLDKLLSKETGLPVIVADDPLLCVAKGTGKALEDIDLIKG
>gnl|CDD|129983 TIGR00905, Arginine/ornithine_antiporter, transporter, basic amino acid/polyamine antiporter (APA) family. This family includes several families of antiporters that, rather commonly, are encoded next to decarboxylases that convert one of the antiporter substrates into the other. This arrangement allows a cycle that can remove proteins from the cytoplasm and thereby protect against acidic conditions [Transport and binding proteins, Amino acids, peptides and amines]
MSEAKSKKLGLFALTALVIGSMIGSGIFSLPQNLASVAGPGAVIIGWIITGVGMLALAFVFAILATKKPE
LDGGIYAYAREGFGPYIGFMSGWGYWLSAWIGNVAYAVLLFSALGYFFPLFGSGNPVPSILGASVLLWVF
TFLVLRGVRQAAFINTITTIAKLIPLFLFIIIGWFWFKLDLFTADFWGHDVPSLGSVFSQVKNTMLVTLW
VFIGIEGAVVSSGRAKNKSDVGKATVLGTLGALVIYILITLLSLGVLPQQELANLPNPSMAAVLEMIVGK
WGAVLISLGLIISVLGSLLSWTMLAAEVPFSAAKDGLFPKIFGRVNKNGAPSVALLLTNILIQLFLLLTL
LTSSAYNVLVSLAVVMILVPYLLSAAYLLKLAKVGTYPKIKNRKALIVGVIACVYSIWLLYAAGLKYLLL
GFILYAPGIIFYGRARKERGKHVFNKKEILIATIIVIAAIIAIWLLVNGSISI
>gnl|CDD|273330 TIGR00906, Low_affinity_cationic_amino_acid_transporter_2, cationic amino acid transport permease [Transport and binding proteins, Amino acids, peptides and amines]
RAVLTFARCLIRRKIVDLDSREESKMKRCLTTWDLMALGIGSTIGAGIYVLTGEVARNDSGPAIVLSFLI
SGLAAVLSGFCYAEFGARVPKAGSAYLYSYVTVGELWAFITGWNLILEYVIGTAAVARSWSAYFDELLNK
QIGQFRRTYFKLNYDGLAEYPDFFAVCLILLLAVLLSFGVKESAWVNKIFTAINILVLLFVIIAGFTKAD
VANWSITEEKGAGGFMPYGFTGVLSGAATCFFAFIGFDAIATTGEEVKNPQRAIPIGIVTSLLVCFVAYF
LMSAALTLMMPYYLLDPDAPFPVAFEYVGWDPAKYIVAVGALCGMSTSLLGGMFPLPRVIYAMARDGLLF
KWLAQINSKTKTPINATVVSGAIAALMAFLFDLKALVDLLSIGTLLAYSLVAACVLILRYQPGLVYDQAK
DTDEKDTLDSWVPFTSKSESQSEGFSLRTLFSGLILGLSILTTYGRAAIAEEAWSIALLTLFLVLFLLVV
LTIWRQPQNKQKVAFKVPLVPFLPALSILINIFLMVQLDADTWVRFAIWMAIGFLIYFLYGIRHSLE
>gnl|CDD|273331 TIGR00907, Choline_transport_protein, amino acid permease (GABA permease) [Transport and binding proteins, Amino acids, peptides and amines]
LVALGYKPELKREFSLWSIFGFAFSISNSWTGISTTYNYGLSSGGAMSIVWGWIIAGAGSICIALSLAEL
SSAYPTSGGQYFWSAKLAPPRQMPFASWMTGWFNLAGQVAGTASTDLSVAQLILGIVSLTTPGREYIPTR
WHIFGIMIGIHLIHALINSLPTKWLPRITSSAAYWSLLGFLTICITLLACKSPKFNDGKFVFTNFNNSTG
GWKPGGFAFLLGLLNPAWSMTGYDGTAHMAEEIENPEVVGPRAIIGAVAIGIVTGFCFNIVLFFSMGDID
SLISSTTGQPIAQIFYNALGNKAGAIFLLCLILVTSFFCAITCMTANSRMIYAFSRDGGLPFSPLWSRVN
PRTQVPLNAVWLSAVWIILIGLLGLGSSTAFQAIFSVCTVALDVSYVIPIICKLAKGRNTIAPGPFWLGK
YGFFVNAVAVAWTVFSSVLFSFPPVLPVTPENMNYAVVVFAGVLAISLVYWKYKGRKEFTGP
>gnl|CDD|129986 TIGR00908, putative_ethanolamine_permease, ethanolamine permease. The three genes used as the seed for this model (from Burkholderia pseudomallei, Pseudomonas aeruginosa and Clostridium acetobutylicum are all adjacent to genes for the catabolism of ethanolamine. Most if not all of the hits to this model have a similar arrangement of genes. This group is a member of the Amino Acid-Polyamine-Organocation (APC) Superfamily [Transport and binding proteins, Amino acids, peptides and amines]
QHRQLKKTLATWQLWGIGVGYVISGDYAGWNFGLAQGGWGGFVVATLLVATMYLTFCFSLAELSTMIPTA
GGGYGFARRAFGPWGGFLAGTAILIEFAFAPPAIACFIGAYCESLFPVGPGWLAALVFYIVFIGINILGV
GEAAKLEFVVTAVAIIALGVFIGAMVPHFDSANLFNGPQTGASSFLPGAYVGVFAAIPFAIWFFLAVEGV
AMAAEETKNPKRDIPRGLIGAILTLLALAAGILVVGPGAADAKELMGSNNPLPEALESIYGGSTWMSQFV
NLVGLFGLIASFHGIIYGYSRQIFALSRAGYLPESLSKVNRKKAPVLAIVVPGVIGFGLSLTGQTALIIL
VSVFGAIISYVLSMAAHFTLRIRRPDMERPYRTPGGILTPGVALVLACVALVTGFYVDPRVVVGAVAIFV
VLIGYYFLYSRHHLVSGTPEEE
>gnl|CDD|129987 TIGR00909, putative_amino_acid_transporter, amino acid transporter [Transport and binding proteins, Amino acids, peptides and amines]
LSRELGLFDLTMLGIGAMIGTGIFVVTGIAAGKAGPAVILSFVLAGLTALFIALVYAELAAMLPVAGSPY
TYAYEAMGELTAFIIGWSLWLEYGVAVAAVAVGWGGYLQEFLPGVGLDLPAVLTAKPGNGGVFNLPALLI
VLFLTYILYLGAKESGKVNDILVVLKVAALLLFAALGAIHFASNNYTPFMPMGFGGVGAATALVFFAFIG
FEAISTAAEEVKNPERDIPKAIILSLIVVTLLYVLVAAVILGAVPWRQLAGSTAPLSLVGYDLGQGIGGL
ILTAGAVFSIASVMLAGIYGTSRVLFAMSRDGLLPGSLSKVHPKTGTPHMSIIIFSLTAALLASLVPLEG
LAELTSIGTLIAFAAVNVAVIILRRRRPDIQRAFRCPLVPVLPVLVVSYCIYLLLNLGPGTTVWFLVWML
LGSVFYFIY
>gnl|CDD|129988 TIGR00910, Glutamate/gamma-aminobutyrate_antiporter, glutamate:gamma-aminobutyrate antiporter. Lowered cutoffs from 1000/500 to 800/300, promoted from subfamily to equivalog, and put into a Genome Property DHH 9/1/2009 [Transport and binding proteins, Amino acids, peptides and amines]
GKAKKLSLFGFFAITASMVLAVYEYPTFATSGFHLVFFLLLGGILWFIPVALCAAEMATVDGWEEGGIFA
WVSNTLGERFGFAAIFFGWFQIAIGFIPMIYFILGALSYILKFPALNEDPIIKFIAALIIFWALAFSQFG
GTKRTAKIAKAGFFAGILIPAFILFALAAAYFHGGAPIAIEIDSHAFFPDFSKVGTLVVFVAFIGAYMGV
EASASHINELENPGRDYPLAMILLMIAAICLDAIGGFSIAAVIPGKEINLSAGVIQTFQTLILHFAHEIE
WLVKVIAALIAFGVLAEIASWIVGPSRGMFAAAQKGLLPAAFAKMNKHEVPVPLVIIQGIITSIAGAILT
FGGGGNNLSFLIAIALTVVIYLCAYFLFFIGYFVLILKHPDLKRTFNIPGGIGGKLIIAGIGFLLSIFAF
FISFLPPANIAGDETDMYQEILLISFLVTAALPFIIYALHDKKGHANTGVTIEEINHFKAGDGHFAIHPA
ARGEHHIIKKDEHILKH
>gnl|CDD|273332 TIGR00911, High-affinity_methionine_permease, L-type amino acid transporter [Transport and binding proteins, Amino acids, peptides and amines]
MSKGRVFRSQSNATNYQFSSSGRKKSVSASTVDGGEAVALKKEITLLSGVGIIVGTIIGSGIFVSPKGVL
KNAGSVGLALIMWAVCGIFSIVGALVYAELGTTIPKSGGEYNYILEVFGPLLAFLRLWIELLVIRPGSQA
VNALNFAIYILTPVFPDCEVPEWAIRLVAVLCVLLLTLVNCLSVKWATRVQDIFTACKLLALLLIIITGW
VQLGKGGVESLNPKNAFEGTETSAGGIVLAFYSGIWAYGGWNYLNFVTEEVKNPYRTLPIAIIISMPIVT
FIYVLTNIAYFTVLSPEELLASLAVAVDFGERLLGVMSWAMPALVGLSCFGSVNGSLFSSSRLFFVGGRE
GHLPSLLSMIHVKRLTPLPSLLIVCTLTLLMLFSGDIYSLINLISFANWLFNALAVAGLLWLRYKRPEMN
RPIKVPLFFPVFFLLSCLFLIILSLYSPPVGCGVGFIIMLTGVPVYFFGVWWQNKPKWFRYLIVSKTVLL
QKVLEVVKPQK
>gnl|CDD|273333 TIGR00912, Spore_germination_protein_A2, spore germination protein (amino acid permease). This model describes spore germination protein GerKB and paralogs from Bacillus subtilis, Clostridium tetani, and other known or predicted endospore-forming members of the Firmicutes (low-GC Gram positive bacteria). Members show some similarity to amino acid permeases [Transport and binding proteins, Amino acids, peptides and amines]
DKISSKQLIFLISSTMIGSGLLTLPALVSQSAGQDGWISIILGGLIIIFLLCLMIKIMSKFPEKNFSEIL
SKYLGKILGRLLSILFILYFFLIAAYLIRIFADFIKTYLLPRTPIIVIIILIIIVSIYIVRKGIEVLLRT
AEILLIIFLILFILVLILLAPKLGNIKNLLPVLENGLSPILKGAYPVVTFAFGEIEIFFLLFPLLSKKKK
IKKSIIKAIIIGVLLYILTTFVSISVFGGNVTKNLYWPTLELIKLINIGDFIERFELIVMTFWVFIIFVK
IAFYLYIAVKGLSKLFKKRKYSILILPVLMVIFSISFFPDSSNQLFDYLEFLPIIAIVFFLLLPLILFII
VKIKNKKKA
>gnl|CDD|273334 TIGR00913, General_amino_acid_permease, amino acid permease (yeast) [Transport and binding proteins, Amino acids, peptides and amines]
KKSLKQRHIQMIALGGTIGTGLLVGSGTALATGGPAGLLIGYAIMGSIIYCVMQSLGEMATFYPVVSGSF
ATYASRFVDPAFGFAVGWNYWLQWLIVLPLELVTASMTIQYWTDKVNPAVWIAIFYVFIVIINLFGVKGY
GEAEFWFSSIKILAIIGFIILSIILNCGGGPNHGYIGFRYWHDPGAFAGGTIGGRFKGVCSVFVTAAFSF
GGTELVALTAGEAANPRKSIPRAAKRTFWRILVFYILTLFLIGFLVPYNDPRLLSSSSSSDSAASPFVIA
IQNHGIKVLPHIFNAVILISVLSAANSSLYASSRTLYALAHQGLAPKIFAYVDRRGVPYVAVIVSSLFGL
LAFLAVSKKEAEVFTWLLNISGLSGFFTWMCICLSHIRFRKAMKAQGRSLDELPYKSQTGPYGSYYALFF
NILILIAQGYVAFAPVKFSAKSFFEAYLSLPIFIALYIGHKVYKRDKLIIKLDDIDLD
>gnl|CDD|129992 TIGR00914, Nickel-cobalt-cadmium_resistance_protein_NccA, heavy metal efflux pump, CzcA family. This model represents a family of H+/heavy metal cation antiporters. This family is one of several subfamilies within the scope of pfam00873 [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds]
MIERIISFSVAQRWLVLLATLVMAILGIWSYNRLPIDAVPDITNVQVQINTSAPGYSPLEVEQRVTYPIE
TAMAGLPGLETTRSLSRYGLSQVTVIFKDGTDLYFARQLVNERLQQARDNLPEGVSPEMGPISTGLGEIF
LYTVEAEEGARKKDGGAYTLTDLRTIQDWIIRPQLRTVPGVAEVNSIGGYVKQFLVAPDPEKLAAYGLSL
ADVVNALERNNQNVGAGYIERRGEQYLVRAPGQVQSMDDIRNIVIATGEGVPIRIRDVARVQIGKELRTG
AATENGKEVVLGTVFMLIGENSRTVAQAVGDKLETINKTLPEGVEIVTTYDRSQLVDAAIATVKKNLLEG
ALLVIVILFLFLGNIRAALIAATVIPLSLLITFIGMVFQGISANLMSLGALDFGLIVDGAVVIVENAHRR
LAEAQHHHGRQLTLKERLHEVFAASREVRRPLIFGQLIITLVFLPIFTLTGVEGKMFHPMAFTVVLALAG
AMILSLTFVPAAVALFIRGKVAEKENRLMRVLKRRYEPLLERVLAWPAVVLGAAAVSIVLVVWIASRVGG
EFIPSLNEGDLAYQALRIPGTSLAQSVAMQQTLEKLIKSFPEVARVFAKTGTAEIATDPMPPNASDTYII
LKPESQWPEGKKTKEDLIEEIQEATVRIPGNNYEFTQPIQMRFNELISGVRSDVAVKVFGDDLDDLDATA
EKISAVLKGVPGAADVKVEQTTGLPYLTVEIDREKAARYGLTVGDVQDTVATAVGGRMSGETFEGDRRFD
IVIRLPESLRESPQALRQLPIPLPLSEDARKQFIPLSDVADLRVSPGPNQISRENGKRRVVVSANVRGRD
LGSFVDDAKKAIAEQVKLPPGYWITWGGQFEQLQSATKRLQIVVPVTLLLIFVLLYAAFGNVKDALLVFT
GIPFALTGGVFALWLRGIPLSISAAVGFIALSGVAVLNGLVMISFIRKLLEEGPSLDEAVYEGALTRVRP
VLMTALVASLGFVPMAIATGTGAEVQRPLATVVIGGIITATLLTLFVLPALYRLVHRRRHKGRKEHEPLE
G
>gnl|CDD|273335 TIGR00915, Probable_aminoglycoside_efflux_pump, The (Largely Gram-negative Bacterial) Hydrophobe/Amphiphile Efflux-1 (HAE1) Family. Proteins scoring above the trusted cutoff (1000) form a tight clade within the RND (Resistance-Nodulation-Cell Division) superfamily. Proteins scoring greater than the noise cutoff (100) appear to form a larger clade, cleanly separated from more distant homologs that include cadmium/zinc/cobalt resistance transporters. This family is one of several subfamilies within the scope of pfam00873 [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
MAKFFIDRPIFAWVIAIIIMLAGTLSILSLPVSQYPSIAPPAITVSASYPGASAQTVQDTVTQVIEQNMN
GIDGLRYMSSSSDSDGSMTITLTFEQGTDPDIAQVQVQNKLQLATPLLPQEVQRQGVRVEKASSNFLMVI
GLVSDDGSMTKEDLSDYAASNMVDPLSRLEGVGDVQLFGSQYAMRIWLDPAKLNSYQLTPADVISAISAQ
NAQISAGQLGGLPAVPGQQLNATIIAQTRLQTPEQFENILLKVNTDGSQVRLKDVARVELGGENYSISAR
FNGKPASGLAIKLATGANALDTAKAVKAELAVLEPFFPQGMKYVYPYDTTPFVEASIEEVVHTLIEAIVL
VFLVMYLFLQNFRATLIPTIAVPVVLLGTFAVLAAFGFSINTLTMFAMVLAIGLLVDDAIVVVENVERVM
AEEGLPPKEATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGSTGAIYRQFSITIVSAMALSVLVALILTP
ALCATMLKPIEKGEHHEKKGGFFGWFNRMFDSSTHGYENGVGKILRRRGRYLLVYVLLVGGMVFLFVRLP
TSFLPDEDQGVFMTIVQLPAGATAERTQAVLAQVTKYLLAKEKANVESVFTVNGFSFAGRGQNMGMAFIR
LKDWEERTGKENSVFAIAGRATGHFMQIKDAMVIAFVPPAILELGNATGFDFFLQDRAGLGHEALLQARN
QLLGLAAQNPALTRVRPNGLEDEPQLKIDIDREKAQALGVSIADINTTLSTAWGSSYVNDFIDRGRVKRV
YVQAEEDARMSPEDINKWYVRNASGEMVPFSAFATVRWEYGSPQLERYNGLPSMEILGSAAPGVSTGQAM
AAMEAIAQKLPPGFGFSWTGMSYEERLSGSQAPALYALSLLVVFLCLAALYESWSIPVSVMLVVPLGIIG
ALLATTLRGLSNDVYFQVGLLTTIGLSAKNAILIVEFAKELMAQGKSIVEAALEAARLRLRPILMTSLAF
ILGVVPLAISTGAGSGSQHAIGTGVFGGMVTATVLAIFFVPLFYVVVRRLFKRKAHEKEMSVEH
>gnl|CDD|273336 TIGR00916, Protein_translocase_subunit_SecF, protein-export membrane protein, SecD/SecF family. The SecA,SecB,SecD,SecE,SecF,SecG and SecY proteins form the protein translocation appartus in prokaryotes. This family is specific for the SecD and SecF proteins [Protein fate, Protein and peptide secretion and trafficking]
LDEEGAKIFADFAANIGKPAIVLDNAKVISAPVVGTVGPTLGGELIKAGIIALLIGLVLVLLYMLLRYEW
RGAIAAIAALVHDVILILGVLSLFGATLTLPGIAGLLTIIGYSVDDTVVIFDRIREELRKYKGRTFREAI
NLGINQTLSRIIDTNVTTLLAVLALYVFGGGAIKGFALTLGIGVIAGTYSSI
>gnl|CDD|273337 TIGR00917, Niemann-Pick_C_disease_protein, Niemann-Pick C type protein family. The model describes Niemann-Pick C type protein in eukaryotes. The defective protein has been associated with Niemann-Pick disease which is described in humans as autosomal recessive lipidosis. It is characterized by the lysosomal accumulation of unestrified cholesterol. It is an integral membrane protein, which indicates that this protein is most likely involved in cholesterol transport or acts as some component of cholesterol homeostasis [Transport and binding proteins, Other]
CAMYDICGARSDGKVLNCPYNIPSVKPPDLLSSLIQSLCQYSHPTISGNVCCTETQFDTLRSNVQQAIPF
IVRCPACLRNFLNLFCELTCSPDQSLFINVTSTTKVKTNSTVDGIQYYITDDFAAGMYNSCKNVKFGSSN
SRALDFLGGGAKNFKEWFNWIGQKAGVNLPGAPYGIAFLPTPCPVSSGMRPMNVSIYSCGDESLGCSCGD
CPSAATCSCKAKVPTQKKHSCSIKLGVKCVDFILAILYIVLVSVFLGGGLLHPVRGKKKTSQMGTLSEAD
GEINSVNQQKDQNTPQRNWGQLSTVQGHLARFFGKYGIWVARHPTLVICLSVSVVLLLCVGLIRFKVETR
PVKLWVAPGSRAALEKQYFDTHFGPFYRIEQLIIATVQTSSHEKAPEILTDDNLKLLFDIQKKVSQLFAN
YEGELITLDSPCFKPNHPYNCFIYSTCKKLQNMYSKLKPENYDDYGGVDYVKYCFEHFTSPESCLSAFGG
PVDPTTVLGGFSGNNFSEASAFVVTFPVNNFVNKTNKTEKAVAWEKAFIQLAKDELLPMVQATISFSAER
SIEDELKRESTADVITIAISYLVMFAYISLTLGDSPRLKSLYVTSKVLLGLSGILIVMLSVLGSVGVFSA
VGLKSTLIIMEVIPFLVLAVGVDNIFILVFFYFYLEYFYRQVGVDNEQELTLERRLSRALMEVGPSITLA
SLSEILAFALGALIKMPAVRVFSMFAVLAVFLDFLLQITAFVALLVLDFKRTEDKRVDCFPCIKTSKSSI
SAEKGSGQRKAGLLTRYFKEVYAPVLLHWIVKIVVIAFFVGLLMAGIALSTRVEIGLDQQIVLPQDSYLQ
IYFASLTPLLEVGPPFYIVIKGDYNYTDFESQNKLCTMGGCDKDSIVNVFNNLSYIAKPASSWLDDYLVW
LSPQASCCCRKFTNGTFCNGPDPQCFRCADLSSDAQGRPSTTQFKEKLPWFLNALPSADCAKGGHAAYSS
AVDLQGYATIIQASSFRTYHTPLNTQVDFINAMRAAQEFAAKVSRSSKMEVYPYSVFYVFFEQYLTIWKT
AIINLSIALGAIFIVCLFLLQLNALSVVNLIMSVGMAVVFCVGIMHLWSISLNAVSVVNSVMHKGIAIEF
CTHINAQFSTGKHFSRNHRAKEALGGMGSSVFSGITLTKLVGVVVLGFSRSEIFVVYYFRMYLALVLLGF
LHGLVFLPVLLSVLG
>gnl|CDD|273338 TIGR00918, Protein_patched_homolog_1, The Eukaryotic (Putative) Sterol Transporter (EST) Family
RTAAPDSEYLQRPSYCDAAFALEQIDKGKATGRRAPLWLRAKFQRLLFTLGCYIQKHCGKVLFVGLLVFS
AFAVGLRAANIETNVEQLWVEVGGRVSQELAYTRQKIGEEAMFTPQLLIQTPHQEGANVLTPEALLQHLD
SALKASRVHVYLYNRQWGLEHLCYKSGEPSTEGGYIEQILEKLIPCLIITPLDCFWEGAKLQGGTAYLPG
KPPLQWTNLDPASFLEELKQKMSQVESWEEMLKKAAVGQGYMERPCLNPADPDCPDTAPNKNSTQPPDVA
AVLSGGCYGLSAKYMHWQEELIVGGTKRNRSGKLLSAQALQSMFQLMTPKQMYEHFKGYYKVHHIGWNEE
KAAAVLEAWQRNFSEEVQQSLPKNSSQKILVFSSTTLDDILKKFSDVSAIRIVSGYLLMLAYACLTMLRW
DCAKSQGSVGLAGVLLVALSVAAGLGLCALLGISFNAATTQVLPFLALGVGVDDVFLLAHAFSETGQNIP
FEERTGECLKRTGASVVLTSISNVTAFFMAALIPIPALRAFSLQAAIVVVFNFAAVLLVFPAILSLDLRR
REDRRLDIFCCFFSPCSARVIQIEPQAYADGSAPPVYSSHMQSTVQLRTEYDPGTQHYYTTNEPRSHLSV
QPSDPLSCQSPDIAGSTRDLLSQFEDSKAACLSLPCARWTLATFAEKHYAPFLLQSWAKVVVIFLFLALL
GLSLYGTTRVQDGLDLTDIVPRDTNEHDFLDAQFRYFSFYNMYAVTQGNFDYPTQQQLLYDLHQSFSSVK
YVLKEDNGQLPRMWLHYFRDWLQGLQKAFDEDWRDGRITKENYRNGSDDAVLAYKLLVQTGHRDKPVDKE
QLTTQRLVNADGIINPNAFYIYLSAWVSNDPVAYAASQANIYPHPPEWLHDKNDYDPENLRIPAAEPLEY
AQFPFYLNGLRETSQFVEAIEHVRAICNNYEGFGLPSYPSGYPFLFWEQYMGLRHWLLLSISVVLACTFL
VCALLLLNPWTAGLIVLVLALMTVELFGMMGLLGIKLSAIPVVILIASVGIGVEFTVHIALGFLTAIGDR
NRRAVLALEHMFAPVLDGALSTLLGVLMLAGSEFDFIVRYFFAVLAVLTCLGVLNGLVLLPVLLSMFGPE
PEVSPAEGRSRLPTPSPEPPPGGVR
>gnl|CDD|273339 TIGR00920, 3-hydroxy-3-methylglutaryl-coenzyme_A_reductase, 3-hydroxy-3-methylglutaryl-coenzyme A reductase [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MLSRLFRAHGQFCASHPWEVIVATLTLTICMLSMNQFTGLEKICGWNYECPKFEEEYLSSDVIVMTITRC
IAVLYIYYQFCNLRQLGSKYILGIAGLFTIFSSFVFSTAVIHFLGSELTGLNEALPFFLLLIDLSKASAL
AKFALSSNSQDEVRDNIARGMAILGPTITLDTVVETLVIGVGTMSGVRRLEVLCCFGCMSVLANYFVFMT
FFPACLSLVLELSRSGREGRPVWHLSKFALVLEEEEDQKPNPVVQRVKMIMSTGLVLVHAHSRWVSPNST
TMVDKTVTLTLDLNVSKRIEPSMPLWQFYLSRMLTMDLDYIVTLILAIVLAVKYIFFSQRETESTVSLKN
PVVNPVSDQKKQSEPCCIRELASSTTTIDVSHVEEEKDTSKSAAVETIKPLPEETSSASEASFPVGKSGS
EQPDLLPLKERLVEPPKEPRPVDECLDILNSTEKGAQALSDAEVISLVNAKHIPAYKLETVLDNPERGVA
IRRQILSKKLPMPDALDVLPYKNYDYSKVMGACCENVIGYMPIPVGVAGPLLLDGKEYQVPMATTEGCLV
ASTNRGCRALMLGGGVRSRVLADGMTRGPVVRLPSACRAAEAKAWLEVPENFAVIKDAFDSTSRFARLKK
IHIAMAGRNLYIRFQAKTGDAMGMNMISKGTEQALAELQEHFPDMQILSLSGNYCTDKKPAAINWIEGRG
KSVVCEATIPAKIVRSVLKTSAEALVDVNINKNLIGSAMAGSIGGFNAHAANIVTAIYIATGQDAAQNVG
SSNCMTLMEAWGPTGEDLYISCTMPSIEIGTVGGGTVLPPQSACLQMLGVRGANATRPGENAKQLARIVC
ATVMAGELSLMAALAAGHLVKSHMRHNRSSINLQSSLPGTCTKKSA
>gnl|CDD|273340 TIGR00921, Predicted_exporter_of_the_RND_superfamily, The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family. Characterized members of the RND superfamily all probably catalyze substrate efflux via an H+ antiport mechanism. These proteins are found ubiquitously in bacteria, archaea and eukaryotes. They fall into seven phylogenetic families, this family (2.A.6.7) consists of uncharacterised putative transporters, largely in the Archaea [Transport and binding proteins, Unknown substrate]
MRFRTAIILVFLALLILSAYGAQHLNVESDTEKQLPKDFESYKWYHVLQREFGTSTKTLLVVIEGDDVTR
KPVLDYMRRLEQRLREKPYVTNVRSAADIMRQIPGNFPLPVTMPEVRPLMSEYPRSKEMFLSKDHTVAII
IVQLKSDADYKQVVPIYNDVERSLERTNPPSGKFLDVTGSPAINYDIEREFGKDMGTTMAISGILVVLVL
LLDFKRWWRPLLPLVIILFGVAWVLGIMGWLGIPLYATTLLAVPMLIGVGIDYGIQTLNRYEEERDIGRA
KGEAIVTAVRRTGRAVLIALLTTSAGFAALALSEFPMVSEFGLGLVAGLITAYLLTLLVLPALLQSIDIG
REKVKKEIIAIGGKSSEIEEELSKVLSITVRHPVPALVAALIITGLGLYGAAGIKPEVNIEKFIPQDLPS
LQARKVIESHMGGSHDFATILVKADDVRDPELVRFMDELSRDIKATGVAARVFGAPSIIDLVKEVEGLPA
PERSALEPIPEDEEGGYISGGQIKVAVIQVQLKQGEPKVQGRKILRDVQHEHPPPGVKVGVTGLPVAFAE
MHELVNEGMRRMTIAGAILVLMILLAVFRNPIKAVFPLIAIGSGILWAIGLMGLRGIPSFLAMATTISII
LGLGMDYSIHLAERYFEERKEHGPKEAITHTMERTGPGILFSGLTTAGGFLSLLLSHFPIMRNFGLVQGI
GVLSSLTAALVVFPALLVL
>gnl|CDD|273341 TIGR00922, Transcription_antitermination_protein_nusG., transcription termination/antitermination factor NusG. NusG proteins are transcription factors which are aparrently universal in prokaryotes (archaea and eukaryotes have homologs that may have related functions). The essential components of these factors include an N-terminal RNP-like (ribonucleoprotein) domain and a C-terminal KOW motif (pfam00467) believed to be a nucleic acid binding domain. In E. coli, NusA has been shown to interact with RNA polymerase and termination factor Rho. This model covers a wide variety of bacterial species but excludes mycoplasmas which are covered by a separate model (TIGR01956).The function of all of these NusG proteins is likely to be the same at the level of interaction with RNA and other protein factors to affect termination; however different species may utilize NusG towards different processes and in combination with different suites of affector proteins.In E. coli, NusG promotes rho-dependent termination. It is an essential gene. In Streptomyces virginiae and related species, an additional N-terminal sequence is also present and is suggested to play a role in butyrolactone-mediated autoregulation. In Thermotoga maritima, NusG has a long insert, fails to substitute for E. coli NusG (with or without the long insert), is a large 0.7 % of total cellular protein, and has a general, sequence non-specific DNA and RNA binding activity that blocks ethidium staining, yet permits transcription.Archaeal proteins once termed NusG share the KOW domain but are actually a ribosomal protein corresponding to L24p in bacterial and L26e in eukaryotes (TIGR00405) [Transcription, Transcription factors]
WYVVQTYSGYEKKVKQNLEELIELLGMGDYIFEVIVPTEEVVEIKKGKKKVVERKIFPGYVLVKMDLTDV
SWHLVKNTPGVTGFVGSGGKPKALSEDEEVKNILNALEEGKDKPKPKIDFEVGEQVRVNDGPFANFTGTV
EEVDYEKSKLKVSVSIFGRETPVELEFSQVEK
>gnl|CDD|273342 TIGR00924, putative_Di/Tri_peptide_transporter, amino acid/peptide transporter (Peptide:H+ symporter), bacterial. The model describes proton-dependent oligopeptide transporters in bacteria. This model is restricted in its range in recognizing bacterial proton-dependent oligopeptide transporters, although they are found in yeast, plants and animals. They function by proton symport in a 1:1 stoichiometry, which is variable in different species. All of them are predicted to contain 12 transmembrane domains, for which limited experimental evidence exists [Transport and binding proteins, Amino acids, peptides and amines]
GEKTFFGHPKPLFTLFFVELWERFSYYGMQGILAVYLVQQAGLGFSQEQAFIIFGAYSALVYLLTSVGWW
FGDRVWGTKKTMVLGGIVLMLGHFMLAMSIYPDLIFYGLGTIAVGSGLFKANPSSMVGKLYERGDMPRRD
GGFTLFYMSINIGSFISPLLAGVIAENYGYHVGFNLAAVGMVIGLLTFFAGRHMLRDIGSVPDPLSGQGK
TYGKLLLALLAALALVFFCAWLMHHVVIANILLMTVTLAVIIFFFRLAFKPRLDAVARNKMYAYIVLFLE
AVVFWVLYAQMPTSLNFFADNNMHHEMLGMSVPVIWFQSLNPFWVVVGSPVLAMIWTRLGRKGKDPTTPL
KFTLGMLFCGASFLTFAASIWFADAGGLTSPWFMVLIYLFQTLGELMISPLGLSWWTKIAPQRLMGQMLG
MWFLAQAMGSLLGGYLATFGAVPQGVTGVFGKIGLVTLLVGVVMALMVPWLNRMM
>gnl|CDD|273343 TIGR00926, Peptide_transporter_family_1, Peptide:H+ symporter (also transports b-lactam antibiotics, the antitumor agent, bestatin, and various protease inhibitors) [Transport and binding proteins, Amino acids, peptides and amines]
FSYYGMRTILVLYFLNFLGFSESTSTVLFHTFTYLCYLTPLIGAIIADGWLGKFKTILYLSIVYVVGHAL
LSFGAIPSSGHPLHDLLDLLGLALIALGTGGIKPCVSAFGGDQFEERQLSLRSRFFSFFYFAINAGSLIS
TIITPILRGDVGCFGCQDCYPLAFGVPAILMILALIVFMAGSKMYKKKPPKGNIVSKVIKCIVTALRKRF
STRSEHWPLHWLDYAKDKHDIRMIRSTKRLLRVLVLFIPLPMFWALFDQQGSRWTLQATRMDGDVGGFEI
QPDQMQVVNPLLILIFVPIFDYIVYPAIAKCGTRFTSLRKMAVGGLLAALSFFVAALVQLKVNPTLPEEP
SANEIFLQVLNTDCTICDFSVLSKRVLPHDVYLHLDKKNTSGDQGLFTTKSSAKGWTLTYDLSYDGACGL
TGNCPKTTDAHELEPKISYVLLLSQGGYQLTANTDKPTDAKTEKGMGSVRLVNTLNGEFGMISLCTSDSD
SVTPCNPRDPYDFYFRGTKYPANTCDRIDNAKSSTFLSNQLDMGIYYLIVITENSKIDELQAQIVELVSV
NTVSILWQIPQYVILTAGEVLFSVTGLEFSYSQAPPNMKSVLQALWLLTVAIGNLIVVVIAEFENFSVQA
AEFFLFASLMLVVMAIFSILAYFY
>gnl|CDD|273344 TIGR00927, retinal_rod, K+-dependent Na+/Ca+ exchanger [Transport and binding proteins, Cations and iron carrying compounds]
MGKLIRMGTQERRLLRPKRLHWSRLLFLLGMLIIGSTYQHLRRPQGLPSLWAAVSSQQPIKLASRDLSND
EMMMVSSDPPKSSSEMEGEMLAPQATVGRDEATPSIAMENTPSPPRRTAKITPTTPKNNYSPTAAGTERV
KEDTPATPSRALNHYISTSGRQRVKSYTPKPRGEVKSSSPTQTREKVRKYTPSPLGRMVNSYAPSTFMTM
PRSHGITPRTTVKDSEITATYKMLETNPSKRTAGKTTPTPLKGMTDNTPTFLTREVETDLLTSPRSVVEK
NTLTTPRRVESNSSTNHWGLVGKNNLTTPQGTVLEHTPATSEGQVTISIMTGSSPAETKASTAAWKIRNP
LSRTSAPAVRIASATFRGLEKNPSTAPSTPATPRVRAVLTTQVHHCVVVKPAPAVPTTPSPSLTTALFPE
APSPSPSALPPGQPDLHPKAEYPPDLFSVEERRQGWVVLHIFGMMYVFVALAIVCDEYFVPALGVITDKL
QISEDVAGATFMAAGGSAPELFTSLIGVFISHSNVGIGTIVGSAVFNILFVIGTCALFSREILNLTWWPL
FRDVSFYILDLMMLILFFLDSLIAWWESLLLLLAYALYVFTMKWNKQIELWVKEQLSRRPVAKVMALGDL
SKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIE
AKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGET
EAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAE
NQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQKQAIYLF
LLPIVFPLWLTVPDVRRQEARKFFVITFLGSIMWIAMFSYLMVWWAHQVGETIGISEEIMGLTILAAGTS
IPDLITSVIVARKGLGDMAVSSSVGSNIFDITVGLPVPWLLFSLINGLQPVPVSSNGLFCAIVLLFLMLL
FVISSIASCKWRMNKILGFTMFLLYFVFLIISVMLEDRIISCPVSV
>gnl|CDD|273345 TIGR00928, Adenylosuccinate_lyase, adenylosuccinate lyase. This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFTEVDLERIKEIEAVTR
HDVKAVVYALKEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVML
GRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLVEEVEERVTEFLGL
KPVPISTQIEPRDRHAELLDALALLATTLEKFAVDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDF
ENVCGLARVIRGYASPALENAPLWHERDLTDSSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRN
LDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEVDEPDLLEFLLEDERITKYLKEEELAELLD
PETYIGNAGEIVERV
>gnl|CDD|273346 TIGR00929, CAG_pathogenicity_island_protein_23, type IV secretion/conjugal transfer ATPase, VirB4 family. Type IV secretion systems are found in Gram-negative pathogens. They export proteins, DNA, or complexes in different systems and are related to plasmid conjugation systems. This model represents related ATPases that include VirB4 in Agrobacterium tumefaciens (DNA export) CagE in Helicobacter pylori (protein export) and plasmid TraB (conjugation)
HVPKEYSMSDFIPYAGHYDDHVILTKNGSLMGIIKLEGISFESASDEDLNLLHRELNAALKSIGSGQVAL
WVHTVRRKIVIDYPDPEFKNGFAAAIDEEWRRKFASSDLYENDLYLTLEYKPDSIGVLEKFKKSLTKKTR
EEFQDNYRETLESIKALEDIKRNLLELLREYGAELLKEYDKTGHIYSELLEFLAFLVNGNDIPVTPPVIP
GYLDSYIPSSEVLFGKDGFVIRSPKDNRFFSVISIKEYPEKTEPGILNALLELDCEFILTHSFSFLSKEA
ALSKLGRKRKRLISKGDRAKSQIAELDEALDELTSGDFVMGEHHLSLVVYAEDLEKLDAALREARSLLNA
CGIVAVIETLGLEAAFWSQLPGNFSWNPRKSLITSRNFASLIPFHNFNLGKLRGNPWGPALTLLKTQSGT
PFYFNFHVRDAKVLGHTLIFGPTGSGKTTLLNFLLAQMQKYGGMTIFAFDKDRGMEIFIRAFGGAYLEIK
DGEPFGFNPFQLEDTERNRAFLKEWLAMLVTLDGSTDISAEDRNALSSAIDTVYREGPLIRSLSDLLNFL
PKDYIDLADRLEPWLKGGDYGWLFDNPTDDLDLSKITGFDLTELLDNPKVATPVLMYLFHRINEALDGRP
FLIIIDEAWQYLGNPVFAAKIRDWLKTLRKANGIVVLATQSINDALGSRIADSILEQCATKIFLPNPEAD
REDYAEGFKLTEREFELLKSTPEESRKFLIKQGQSSVVAELNLGGMDNYLRVLSSDTENVEIIDALIKEY
GDDPDDWLPIFYRAL
>gnl|CDD|273347 TIGR00930, Solute_carrier_family_12_member_1, K-Cl cotransporter [Transport and binding proteins, Other]
NTVDAVPRIEHYRNSEGQGGPKRNRPSLEELHDLLDKVVSLLGPLADYTNNGQGMKEHEEAEDAEGTKEK
PPAGAVKFGWVMGVLVPCLLNIWGVILFLRLSWIVGQAGIGLSLLIILLCCCVTTITGLSMSAIATNGVV
KGGGAYYLISRSLGPEFGGSIGLIFAFANAVAVAMYVVGFAETVLDLLRENGSKIMVDPINDIRIYGTVT
VVVLLGISFAGMEWENKAQVLFLVIVLLSILNIFVGTIIPAFDKPAKGFFGLGNEIFSENFIPGIPGPEG
GFFSLFGIFFPSVTGILAGANISGDLKDPQKAIPKGTLLAILTTTVVYLGSVVLFGACVVRDATGDKNDT
LVTNCTSAACFSECAHNTCSYGLMNNLQVMSLVSPFPPLITAGIFSATLSSALASLVSAPRLFQALCKDN
IYPFLQFFGKGYGKNGEPLRAYLLTAFIAEGFILIAELNTIAPIISNFFLASYALINFSCFHASLLRSPG
WRPRFKYYHWWLSLLGASLCCAIMFLISWWAALVAMVIALFLYKYVTYKKPDVNWGSSTQALSYSLALYS
LLRLEEVEDHVKNWRPQCLVLTGPPVCRPALLDFASQFTKGKGLMICGSVIQGPRLECVKEAQAAEAKIQ
TWLEKNKVKAFYAVVVADDLREGVRHLIQASGLGRMKPNTLVMGYKKDWRQAEPRAWETYIGIIHDAFDA
HLAVVVVRNSEGLPISVLQVQEELENDCSEDSIELNDGKISTQPDMHLEASTQFQKKQGKGTIDVWWLVD
DGGLTLLLPYLLTTKKVWKKCKIRIFVGAQKDDRSEQEKKDMATLLYKFRIDAEVIVVLMDINAKPQTES
MEAFEEMIRPFRLHKTEKDREAKDPKMTWTKPWKITDAELQSNVRKSYRQVRLNELLLEYSRDAALVVLS
LPVPRKGSIPDELYMAWLEVLSEDLPPVLLVRGNHRNVLTFYS
>gnl|CDD|188097 TIGR00931, Uncharacterized_Na+/H+_antiporter_HI_1107, Na+/H+ antiporter NhaC. A single member of the NhaC family, a protein from Bacillus firmus, has been functionally characterized.It is involved in pH homeostasis and sodium extrusion. Members of the NhaC family are found in both Gram-negative bacteria and Gram-positive bacteria. Intriguingly, archaeal homolog ArcD (just outside boundaries of family) has been identified as an arginine/ornithine antiporter [Transport and binding proteins, Cations and iron carrying compounds]
RKPTVGETLLLLGVMLALIITSMFVLDLPPHIPLVVSLLIAAVLGRYLGVGYNDLESAIIDGIKIGIKAI
LILALVGILIGTWIMGGTVPTLIYYGLSIISPEWFAVSTLLICMIVSSFTGTSWGTVGTIGVAMMGIGTG
LGIDLAIAAGAVVCGAYFGDKLSPLSDTTNFASGIVGVDLFDHIRHLLYTTVPSFVITAILFLVIGRSYA
TSNTQPDKVQAMLTALDSQFTLSVLTLIPPLLVVILAMRKKPTIPVLVVGALTGIITAAFVQGADVARWI
TIAQNGFSMETGNEVLDGLLNRGGLQSMMWSLSLVMIALTFGGVLQRIGVLDVILQSLTRKLSSRGHLIA
ATATSSIGVNVVTCEQYLSILLPGKTFESFYTKLNLAKKNLSRTLEDAGTLVNPLIPWGVSGAYMAGTLG
VDTISYLPFAFLLFLSIFMAIIYGYLGIGIGKEK
>gnl|CDD|273348 TIGR00932, Na+/H+_antiporter, transporter, monovalent cation:proton antiporter-2 (CPA2) family [Transport and binding proteins, Cations and iron carrying compounds]
LLAAVLAVPLSRRLGIPSVLGYLLAGVLIGPSGLGLISNVEGVNHLAEFGVILLMFLIGLELDLERLWKL
RKAAFGVGVLQVLVPGVLLGLLLGHLLGLALGAAVVIGIILALSSTAVVVQVLKERGLLKTPFGQTVLGI
LLFQDIAVVPLLALLPLLATSASTEHVALALLLLKVFLAFLLLVLLGRWLLRPVLRLTAELRPSELFTAG
SLLLMFGSAYFADLLGLSMALGAFLAGVVLSESEYRHKLESDLEPIGGVLLPLFFISVGMSVD
>gnl|CDD|273349 TIGR00933, Trk_system_potassium_uptake_protein_trkH., potassium uptake protein, TrkH family. The proteins of the Trk family are derived from Gram-negative and Gram-positive bacteria, yeast and wheat. The proteins of E. coli K12 TrkH and TrkG as well as several yeast proteins have been functionally characterized.The E. coli TrkH and TrkG proteins are complexed to two peripheral membrane proteins, TrkA, an NAD-binding protein, and TrkE, an ATP-binding protein. This complex forms the potassium uptake system [Transport and binding proteins, Cations and iron carrying compounds]
LLALPFVISSGLPLSFIDALFTATSAVTTTGLTVLDTLESLPKAGLFLRSLLQQIGGLGFMVLAVAILIL
LGKKISLGARLYLAEALGPLSDDKLLPLIKNTAKFIFVIYLLGTILLAVRFVLTGWMPLFDAIFHSISAF
NNGGFSTHSDSSIGYFHDPSVNLVIAFLIILGGLGFTVHYDVYLHLRKRVFKSLSLDTKVRLFVTFLLLA
IGFILFLLLERGNTLYSYSFGALLLSAFFQSSTLRTAGFSTIDFAALPTATLVLLLLLMFIGGCSGSTAG
GIKTTTFAILLKQVYREIRRGIHPRIIFSRRIGGKTIDKAILISVWSFFLVFALIFLLSILELISSGYDF
LTSLFEVVSAFGTVGLSVGLTTANLPDAGKLILIVLMFIGR
>gnl|CDD|130009 TIGR00934, High-affinity_potassium_transport_protein, potassium uptake protein, Trk family. The proteins of the Trk family are derived from Gram-negative and Gram-positive bacteria, yeast and wheat. The proteins of E. coli K12 TrkH and TrkG as well as several yeast proteins have been functionally characterized.The E. coli TrkH and TrkG proteins are complexed to two peripheral membrane proteins, TrkA, an NAD-binding protein, and TrkE, an ATP-binding protein. This complex forms the potassium uptake system. This family is specific for the eukaryotic Trk system [Transport and binding proteins, Cations and iron carrying compounds]
IGRTMSRYPTFIHIKLRSFGHISRDVIAKIAKVCRPLAKYVFPFFIAVHYFYIISLTIIASILLYPSTVK
NPAYIDALFLAAGALTQGGLNTVDMNDLSLYQQIVLYILMLLTTPIFVHSCLAFVRLYWFERYFDGIRDS
SKQRFFLRRTKTLLQRELEDRPETGVAGRVTVPHGSAKRRDFQDKLFSGEFVKRDEPDQNSPDVKSDTRA
DESISDLEFEKFAKRRGSRDVDPEDLYRSIMMLQGIHERIREKSSANSRSDERSSESIQEQVERRPSTSD
IERNSQSLTRRYDDKSFDKAVRLRRSKTIDRAEACDLEELDRAKDFEKMTYDNWKAHHRKKKNFRPRGWN
LKFRKASRFPKDSDRNYEDNGNHLSASSSFGSEEPSLSSEENLYPTYNKKREDSRHTLSKTMSTNYLSWQ
PTIGRNSNFVGLTKEQKDELGGIEYRALKCLCSIVLVYFLGFNILGFVLLLPWINHVKTYSEVVRSKGVS
PTWWGFFTAMSAFANLGLTLTPESMVSFNKNSYLLLLMIWFIIIGNTGFPIFLRLIIWILFKISPDLSKR
KESLGFLLDHPRRCFTLLFPSGATWWLFFTLVGLNAIDLILFIILDWGSSVVDGLSKGIKVLNGLFQSVS
TRTAGFTVVDLSQLHPAIQVSYMLMMYVSVLPLAISIRRTNVYEEQSLGLYNEENEEHEGESSTKSFIGA
HLRRQLSFDLWYIFLGLFIICICEGRKIQDPDPPNFNVFNILFEVVSAYGTVGLSLGYSCSNYSFSGQFT
TLSKLVIIAMLIRGRHRGLPYALDRAIILP
>gnl|CDD|213571 TIGR00935, arsenical_pump_membrane_protein, arsenite/antimonite efflux pump membrane protein. Members of this protein family are ArsB, a highly hydrophobic integral membrane protein involved in transport processes used to protect cells from arsenite (or antimonite). Members of the seed alignment were selected by adjacency to the ATPase subunit ArsA that energizes the transport [Cellular processes, Detoxification, Transport and binding proteins, Other]
ILAVLIFLLTLVLVIWQPKGLGIGWSATIGAVLALLSGVVSFGDVPVVTGIVWNATLTFVAIIIISLILD
EIGFFEWAALHMARWAKGNGRKMFIYISLLGAIVAALFANDGAALILTPIVLAMVRALGFDEAAVLPFIM
ASGFIADTTSLPLIVSNLVNIVSADFFGIGFNEYAAVMIPPNIFALIASILVLYLYFRKDIPARYDVSQL
REPKEAIKDQKLFKFSWVVLALLLVGYFGSEFLNIPVSFVAATIALIFLVVAAKSHAVDTRKVIKGAPWN
IVVFSLGMYLVVYGLRNVGLTDLLAGVLDYFADQGLFVATMGMGFLAAFLSSIMNNMPTVLINALSIDGS
NATGVMKEAMIYANVIGSDLGPKITPIGSLATLLWLHVLAQKGVKISWGYYFKVGIVITVPVLFITLAGL
YLRLSI
>gnl|CDD|213572 TIGR00936, ahcY, adenosylhomocysteinase. This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the regeneration of the methyl donor S-adenosylmethionine. Species that lack this enzyme are likely to have adenosylhomocysteine nucleosidase (EC 3.2.2.9), an enzyme which also acts as 5'-methyladenosine nucleosidase (see TIGR01704) [Energy metabolism, Amino acids and amines]
AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQ
DDVAAALAKGAGIPVFAWRGETNEEYYWAIEQVLDHEPNIIIDDGADLIFLLHTERPELLEKIIGGSEET
TTGVIRLRAMEAEGVLKFPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKG
IAMRARGMGARVIVTEVDPIRALEAAMDGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVA
NIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGRRIYLLAEGRLVNLAAAEGHPSEVMDMSFANQAL
AAEYLWKNHDKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQKEYLGSWEEGT
>gnl|CDD|273350 TIGR00937, Chromate_transport_protein, chromate transporter, chromate ion transporter (CHR) family. Members of this family probably act as chromate transporters, and are found in Pseudomonas aeruginosa, Alcaligenes eutrophus, Vibrio cholerae, Bacillus subtilis, Ochrobactrum tritici, cyanobacteria and archaea. The protein reduces chromate accumulation and is essential for chromate resistance [Transport and binding proteins, Anions]
FLKLGLLSFGGPVAHAGYMREELVDERQWMSEASYNDLVALAQFLPGPASSQVAIYLGYLLGGIVGAILA
GLAFTLPSFLLVVALAWAYVHYGSLPAVGAWFYGLQAAVIALIAQAVWKLGKKLVGPDRLLWGIALVTAL
GTILWPSEWIQLLLGILVLVLGWRRPPAKIPKVWLRQYALVAFLALGLALLALLLPLADSSLASVLGIFF
YKAGALVFGGGYVVVPFLEGGVVDRGNWLTAGQFLDGIALAQITPGPLFITATFIGYLVAGFPGAIAATV
AIFLPSFLLVLGVLPYFKKLGKNPIIRAFLDGVNAGVVGLLVAATIDLARTSAVDIPTLLVFVSLFAALL
KFKKLPEWVVVLLAALAG
>gnl|CDD|273351 TIGR00938, homoserine_kinase_homolog, homoserine kinase, Neisseria type. Homoserine kinase is required in the biosynthesis of threonine from aspartate.The member of this family from Pseudomonas aeruginosa was shown by direct assay and complementation to act specifically as a homoserine kinase [Amino acid biosynthesis, Aspartate family]
MAVYTSVSDEEMSSFLDGYDLGELLSLKGIAEGVENSNYLLTTDVGRYILTLYEKRVKAEELPFFLALTT
HLAARGLPVPKPVKSRDGRQLSTLAGKPACLVEFLQGLSVGRPTAMHCRPVGEVLAWMHLAGAHFPENRK
NSLRLEAWHILAEKCFEAAPQLEAHMGAELDKELDYLDKFWPRDLPRGVIHADLFPDNVLFDGDSVKGVI
DFYFACTDARAYDLAITVNAWCFDADDHFDADHAKALIKGYHQSRPLTEEEKAAFPVLLRGAAMRFLLTR
LWDWVFTPAGALVVPKDPRDFERRLRF
>gnl|CDD|273352 TIGR00939, Equilibrative_nucleoside_transporter_2, Equilibrative Nucleoside Transporter (ENT) [Transport and binding proteins, Nucleosides, purines and pyrimidines]
FFMLGVGVLLPWNAFITAPQYFIEYYKYAQNIPEAIPSSSKMWKHFNTYYTLASQLPSLLFNSLNLFLIF
RIPVTVRLLGGLVILLVVVILVMVLVKVQTSETGFFVTTMASVVIINSGMALLQGSLFGLAGVFPSTYSS
AVMSGQGLAGVLTSLAMILVKASGNDSHGLKKSALGYFGTPCVVQLICIVCYLLLPKLPFARYYLQKKLD
KGAGEDETKGELRSKAEQNGIPHGGDQPSPTLVLDWEKEPESPDEPQKPLKTSVWVVFTKVWLLAFSVVF
VFTVTLSVFPAITTAVTSSGLGLSNWFYPIICFLLFNLFDWLGRSLTSKFMWPDEDSRWLPILSFLRVLF
IPLFLLCNYPQRSRLPVFFPGDAYFIILMLLFGFSNGYLGSLSMCLAPRQVDPHEREVAGALMVIFLLVG
LALGAVLSFLFVAILDK
>gnl|CDD|273353 TIGR00940, 2a6301s01, Tmonovalent cation:proton antiporter. This family of proteins constists of bacterial multicomponent K+:H+ and Na+:H+ antiporters. The best characterized systems are the PhaABCDEFG system of Rhizobium meliloti which functions in pH adaptation and as a K+ efflux system and the MnhABCDEFG system of Staphylococcus aureus which functions as a Na+:H+ antiporter [Transport and binding proteins, Cations and iron carrying compounds]
LHSAFILPPFAASLIPILYPSDQRIHIGWFVLAIPLVCFLYTLGLYPYTASGGVLHYTIDWVPELGLNFT
LYMDGLALLFSLLITGIGVLVVLYSIYYLSKEEPLPNFYAYLLAFMGAMLGVVLSDNLILLYVFWELTSI
VSFLLISYWHHRAHSRYGAQKSLTITVFGGLAMLGGLILLGKITGSFSIDAVIASADAIRNSPLFGTAMV
LVLLGAFTKSAQFPFHIWLPDAMEAPTPVSAYLHSATMVKAGLYLLARFTPVFAGTEAWFWIVGLAGLIT
LLWGSYFAIFQQDLKGILAFSTISQLGLIMVLLGLGSPSYHYQGDDSKIYALAAVAAVFHLINHATFKGS
LFMAAGIIDHETGTRDIRKLGGLFHIMPITFTLAMIASAAMAGVPPFNGFLSKEMFFAEAITAHLVNPFD
TVTLGYLFPYVATVASVFTFVYSLRFIHGVFFGRPKPEDLPRKPHEPPRWMLASPDILVLLVLVFGLFPA
QLTGPIIEPAVLSILREGVPDDYSLSVWHGWNPPLIMTFVALSGGILLYFLMRSWLATAVEGPPVFRLNR
IYERSLVTLSWKSARWTEQRLTTRRRQPQMRLLVFLILLAGASPLLLGNFEIPPLVVSGIDPAFALLWAI
GIACAIGIAFQAHRLASIILLGGAGLVTCITFVWFSAPDLALTQLLVEIVTTVLFLLGFYHLPKLIEEPV
AAKFSLSNSAIAGGVGLSVIIIGLIAYGNRHFESISKFYQEHVYDLAHGKNMVNVILVDFRGMDTLFESS
VLGIAGLAVYTMIKLRQTQGNEV
>gnl|CDD|273354 TIGR00941, 2a6301s03, Multicomponent Na+:H+ antiporter, MnhC subunit [Transport and binding proteins, Cations and iron carrying compounds]
MESIFALIIGILTASGVYLLLSRSVVRVVLGLALLGYAVNLFILTMGGLENKAPPILTLPVGPYVDPLPQ
ALILTAIVIGFATTALFLVVALRAYQVAGTDDVE
>gnl|CDD|130017 TIGR00942, 2a6301s05, Monovalent Cation (K+ or Na+):Proton Antiporter-3 (CPA3) subfamily [Transport and binding proteins, Cations and iron carrying compounds]
WLFVTQSVTPGSIVLGLIFSTVLAWVTLNLQPARSRLHRWSRIIGFILRFLGDVIKANIDVTLIILRPRR
PVNPGFMTVSTDLKDENALALLANVITLTPGTAWLEYDRDRKIILFHVLDISNEELWRETITRSYEKDLK
EIFE
>gnl|CDD|130018 TIGR00943, 2a6301s02, monovalent cation:proton antiporter. This family of proteins constists of bacterial multicomponent K+:H+ and Na+:H+ antiporters. The best characterized systems are the PhaABCDEFG system of Rhizobium meliloti which functions in pH adaptation and as a K+ efflux system and the MnhABCDEFG system of Staphylococcus aureus which functions as a Na+:H+ antiporter.This family is specific for the phaB and mnhB proteins [Transport and binding proteins, Cations and iron carrying compounds]
LFLRGHNAPGGGFVAGLLTASSLILITIAFGIETVRKILPLDPKRLIGIGLLLAIATGVGSWFLGKPFLT
SVTGYFPLPILGKFELATAVLFDLGVFCVVVGTTMLI
>gnl|CDD|130019 TIGR00944, 2a6301s04, Multicomponent K+:H+antiporter [Transport and binding proteins, Cations and iron carrying compounds]
NLLILPILIPLAVAILLIFINKRRTLKRAIGFASTLVVFVLSMILMRLVAAPGSGVYQLGNWKAPYGIVL
VLDRFSALLLCTTSIIALAVQLYSMARWGTARERHHYYSLVQFLLAGLNGAFLTGDLFNLFVFFEMMLAA
SYGLLVHGSTKIQLKEGLKYIAVNLVSSALFVIGVSLLYGVAGTLNMADLSTKLAALEPRSRGLVEMGSA
LLGVVFLVKAGMFPLSFWLPTAYYAPPPPIAAVFGALLTKVGIYAIIRLHLLVFGTAAGFGHEWLVTLAM
LTIIFGGIGVLAYQNMGKIAGYNVLVAVGVILAGVALGTDGMLAGAIYYLVHDMLTKGALFLLIGLVIRG
TGTATLEAYGGLIKRYPVLGWCFFICALSLAGIPPLSGFIGKFAIISGLFDMGDWTYVTLLLLSSLAVLY
SVNRIFIRTFWGSIKTIPRVNVIEIKPLVVLAGACIFLSLLAG
>gnl|CDD|273355 TIGR00945, Sec-independent_protein_translocase_protein_TatC, Twin arginine targeting (Tat) protein translocase TatC. This model represents the TatC translocase component of the Sec-independent protein translocation system. This system is responsible for translocation of folded proteins, often with bound cofactors across the periplasmic membrane. A related model (TIGR01912) represents the archaeal clade of this family. TatC is often found in a gene cluster with the two other components of the system, TatA/E (TIGR01411) and TatB (TIGR01410). A model also exists for the Twin-arginine signal sequence (TIGR01409) [Protein fate, Protein and peptide secretion and trafficking]
LFEHLEELRKRLLISLIAFLVAFFICFYFSKPIIELLQAPLLALGVTFIATSPTEPFFTYIKISLIVGII
LASPVILYQIWAFILPGLYEHERRLLLPLLLGSILLFLAGLAFAYYVLFPAALNFLLTLGADVVEPLLSI
DQYFEFVLKLLFSFGVAFQVPVLQVLLGKLGIVTPEQLRSKRRYVIVGAFVIGAILTPPDPLSQILLAIP
LLLLY
>gnl|CDD|273356 TIGR00946, Uncharacterized_transporter_MTH_1382, he Auxin Efflux Carrier (AEC) Family [Transport and binding proteins, Other]
MITYVILETVLPILVVILLGYILGKRFGILDEEHASGINRFVINFALPLTIFHSISTTLADILQKSQSPV
VLFLWGAFSGSYALIWLITKPLFKADYGKLSGFLLVSALPNTAFIGYPLLLSLFGEEGAKILIAALFIDT
GAVLMTIALGLFLVSEDGAGGEGSGESTRLMLIFVWKKLIKFPPLWAPLLSVILSLVGFKMPGLILKSIS
ILSGATTPMALFSLGLALSPRKIKLGVRDAILALIVRFLVQPAVMAGISKLIGLRGLELSVAILQAALPG
GAVAAVLATEYEVDVELASTAVTLSTVLSLISLPLFIILLG
>gnl|CDD|273357 TIGR00947, 2A73, putative bicarbonate transporter, IctB family. This family of proteins is suggested to transport inorganic carbon (HCO3-), based on the phenotype of a mutant of IctB in Synechococcus sp. strain PCC 7942. Bicarbonate uptake is used by many photosynthetic organisms including cyanobacteria. These organisms are able to concentrate CO2/HCO3- against a greater than ten-fold concentration gradient. Cyanobacteria may have several such carriers operating with different efficiencies. Note that homology to various O-antigen ligases, with possible implications for mutant cell envelope structure, might allow alternatives to the interpretation of IctB as a bicarbonate transport protein [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
LVGWLGSWRASSWLLQWLEPLAGGLLALLLVLAPFVSTTGLGLVLAACGALWLLLTLVDQPQKRLTPIHL
LVLLYWGIAALATGLSPVPAAALKGLLKLTLYLLVFALAARLLRNPRWRDRLVTVYLLVSLLVSVYGLRQ
WIYGAEELATWVDPESVLAGTTRVYSYLGNPNLLAGYLVPAIPLSLVALLVWRGWAAKLLAATALGVNAL
CLLFTYSRGGWLGLLAALAVLLVLLLLWWSPRLPPFWRRWVPPALLGGAAAALLVAVVQVEPLRTRVLSI
FAGRGDSSNNFRINVWMAVFEMIRDRPWLGIGPGNAAFNAIYPLYQRPRFSALSAYSVPLEILVETGIVG
LLAFLWLLLVTLVQGVRQLKRLRRARNPQGLWLMGALAAIAGLLVHGLVDTIWFRPEVQTLWWLAVALIA
SQWLR
>gnl|CDD|130023 TIGR00948, Hypothetical_protein_Rv0488/MT0507/Mb0498., L-lysine exporter [Transport and binding proteins, Amino acids, peptides and amines]
LILPIGAQNAFVLRQGIRREHVLLIVALCCICDLVLIAAGVFGVAALLAASPILLAVLTWGGALFLLWYG
FLAAKTAWRGPGALVPDEPKKMGLKKVLAMTLAVTLLNPHVYLDTVVLIGALGLQFSDLLRWLFAAGAIA
ASLVWFASLAFGAARLSPLLASPKVWRIINLVVAVVM
>gnl|CDD|273358 TIGR00949, Uncharacterized_membrane_protein_YahN, The Resistance to Homoserine/Threonine (RhtB) Family protein [Transport and binding proteins, Amino acids, peptides and amines]
SPGPNFFVVMQTSLSSGRRAGVLTILGIALGDAIWIVLSLLGLAVLISKSVILFTVIKWLGGAYLIYLGI
KMLRKKSKKQSPAAQVELAEQTTWKKSFRRGLLTNLSNPKAVLFFISIFSQFINPNTPTWQLIVLGLTII
VETILWFYVLSLIFSRPAVRRKYSKQQKWIDGITGALFVGFGIRL
>gnl|CDD|273359 TIGR00950, Uncharacterized_inner_membrane_transporter_YicL, Carboxylate/Amino Acid/Amine Transporter [Transport and binding proteins, Amino acids, peptides and amines]
WGTTGVVIGQYLEGQVPLYFAVFRRLIFALLLLLPLLRRRPPLKRLLRLLLLGALQIGVFYVLYFVAVKR
LPVGEAALLLYLAPLYVTLLSDLMGKERPRKLVLLAAVLGLAGAVLLLSDGNLSINPAGLLLGLGSGISF
ALGTVLYKRLVKKEGPELLQFTGWVLLLGALLLLPFAWFLGPNPQALSLQWGALLYLGLIGTALAYFLWN
KGLTLVDPSAASILALAEPLVALLLGLLILGETLSLPQLIGGALIIAAVL
>gnl|CDD|130026 TIGR00951, Cystine_transporter, Lysosomal Cystine Transporter [Transport and binding proteins, Amino acids, peptides and amines]
ILLSQILGWGYVAAWSISFYPQIIKNWRRKSAEGLSFDFVMLNLVGFTAYVIFNFLQLYCWSITNEFPLS
SPGVTQNDVFFTLHAILICFIVLHQCGDYERGWQRVSNPWILRILVALLACFATLLVALLSPITPLAFVT
MLSYIKVAVTLVKYFPQAATNYHNKSTGQLSIITVFLDFTGLLQRIFQSVNETGDPLKAGLFVVSSLFNG
LFAAQVFFYW
>gnl|CDD|130027 TIGR00952, 30S_ribosomal_protein_S15, ribosomal protein S15, bacterial/organelle. This model is built to recognize specifically bacterial, chloroplast, and mitochondrial ribosomal protein S15. The homologous proteins of Archaea and Eukarya are designated S13 [Protein synthesis, Ribosomal proteins: synthesis and modification]
TKERKQEIIKEFQLHEKDTGSPEVQIALLTERINQLTEHLKANKKDHHSRRGLLKLVGRRRRLLKYLKRT
DVERYRSLIKRLGLRR
>gnl|CDD|273360 TIGR00954, Peroxisomal_long-chain_fatty_acid_import_protein_1, Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protei [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MAVLSKYRLLRSTSNNKTDKQDSPAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKHSTIEGAKKKAH
VNGVFLGKLDFLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFK
WFLIAPPASFINSAIKYLLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCD
SVVELYSNLTKPILDVILYSFKLLTALGSVGPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYV
HSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIF
DKTHPAFLEMSEEELMQEFYNNGRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKR
PRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCG
KSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDN
VQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGI
TLFSVSHRKSLWKYHEYLLYMDGRGGYQF
>gnl|CDD|273361 TIGR00955, Protein_white, The Eye Pigment Precursor Transporter (EPP) Family protein [Transport and binding proteins, Other]
LTYSWRNSDVFGRVAQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNA
LAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRER
VDEVLQALGLRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLK
GLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLA
VIPGSENESRERIEKICDSFAVSDIGRDMLVNTNLWSGKAGGLVKDSENMEGIGYNASWWTQFYALLKRS
WLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQNVFPVINVFTAELP
VFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFG
YLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIEC
TSANTTGPCPSSGEVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRRKR
>gnl|CDD|273362 TIGR00956, Multidrug_resistance_protein, Pleiotropic Drug Resistance (PDR) Family protein [Transport and binding proteins, Other]
EEFNAKAWVKNFRKLIDSDPIYYKPYKLGVAYKNLSAYGVAADSDYQPTFPNALLKILTRGFRKLKKFRD
TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDV
VYNAETDVHFPHLTVGETLDFAARCKTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNDFVRGV
SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDK
VIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADFLTSLTSPAERQIKPGYEKKVPRTPQEFETYWR
NSPEYAQLMKEIDEYLDRCSESDTKEAYRESHVAKQSKRTRPSSPYTVSFSMQVKYCLARNFLRMKGNPS
FTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNAFSSLLEIASMYEARPIVEKHRKYAL
YHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLFRSIGAVTKTL
SEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGRRFECSQYVPSGGGYD
NLGVTNKVCTVVGAEPGQDYVDGDDYLKLSFQYYNSHKWRNFGIIIGFTVFFFFVYILLTEFNKGAKQKG
EILVFRRGSLKRAKKAGETSASNKNDIEAGEVLGSTDLTDESDDVNDEKDMEKESGEDIFHWRNLTYEVK
IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQRSIGY
VQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRL
TIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGG
QTVYFGDLGENSHTIINYFEKHGAPKCPEDANPAEWMLEVIGAAPGAHANQDYHEVWRNSSEYQAVKNEL
DRLEAELSKAEDDNDPDALSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVG
TSLQGLQNQMFAVFMATVLFNPLIQQYLPPFVAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGT
IFFFIWYYPVGFYWNASKTGQVHERGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLS
FCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLADVPVTCKVKELLTFNPPSGQTCGEYMKPYLENA
GGYLLNPNATDSCSFCQYSYTNDFLEPISSKYSGRWRNFGIFIAFIFFNIIATVFFYWLARVPK
>gnl|CDD|188098 TIGR00957, Multidrug_resistance-associated_protein_1, multi drug resistance-associated protein (MRP). This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved [Transport and binding proteins, Other]
CSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTA
LGFLLWIVCWADLFYSFWERSHGRAPAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVAL
VCALAILRSKILLALKEDAIVDPFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFL
SRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPVSAVYGKKDPSKPK
GSSQLDANEEVEALIVKSPHKPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDP
MAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNL
MSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMK
SKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFA
VYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIK
PGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS
VAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVS
LARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKIS
EMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSWTALVSGEGKEAKLIENGMLVTDVVGKQLQRQLSAS
SSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVS
ALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLR
SPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFF
VQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRW
LAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYS
ETEKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTL
GLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHL
KTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED
CTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL
>gnl|CDD|273363 TIGR00958, Antigen_peptide_transporter_2, Conjugate Transporter-2 (CT2) Family protein [Transport and binding proteins, Other]
AALAYLLPWFSLLLVDWALLRDLLQGIFGLLLPFEKGLYVLWLEGTLRLGVLWLGALGILLNKAGGLLAA
VKPLVAALCLATPSLSSLRALAFWEALDPAVRVALGLWSWFVWSYGAALPAAALWAVLSSAGASEKEAEQ
GQSETADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLL
SIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVN
VLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGM
RTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNL
VSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPN
RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALV
GQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIAR
ALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQL
MEDQGCYKHLV
>gnl|CDD|273364 TIGR00959, Signal_recognition_particle_protein, signal recognition particle protein. This model represents Ffh (Fifty-Four Homolog), the protein component that forms the bacterial (and organellar) signal recognition particle together with a 4.5S RNA. Ffh is a GTPase homologous to eukaryotic SRP54 and also to the GTPase FtsY (TIGR00064) that is the receptor for the signal recognition particle [Protein fate, Protein and peptide secretion and trafficking]
FESLSERLQRIFKKLSGRGTITEKNIKEALREIRLALLEADVNLQVVKDFIKKVKEKALGQEVLKSLSPG
QQFIKIVHEELVAILGGENAELNLAKKPPTVILMVGLQGSGKTTTCGKLAYYLKKKQGKKVLLVACDLYR
PAAIEQLKVLGQQVGVPVFALGKGQSPVEIARRALEYAKENGFDVVIVDTAGRLQIDEELMEELAAIKEI
LNPDEILLVVDAMTGQDAVNTAKTFNERLGLTGVVLTKLDGDARGGAALSVRSVTGKPIKFIGVGEKIDD
LEPFHPERMASRILGMGDILSLVEKAQEVVDEEEAKKLAEKMKKGQFDLEDFLEQLRQIKKMGPLSSLLK
MIPGMGGVKPSLSDADLDEKQFKRIEAIISSMTPEERRNPKILNPSRRKRIAAGSGTTVQDVNKLIKRFE
QMKKMMKK
>gnl|CDD|273365 TIGR00962, ATP_synthase_subunit_alpha, proton translocating ATP synthase, F1 alpha subunit. The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit [Energy metabolism, ATP-proton motive force interconversion]
QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSV
GAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKS
VHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRK
LEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPP
GREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNS
GIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDLDEATKKQLERGQRVVELLK
QPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKLTEELEAKLKE
ALKNFKKTFAW
>gnl|CDD|273366 TIGR00963, Protein_translocase_subunit_SecA, preprotein translocase, SecA subunit. The proteins SecA-F and SecY, not all of which are necessary, comprise the standard prokaryotic protein translocation apparatus. Other, specialized translocation systems also exist but are not as broadly distributed. This model describes SecA, an essential member of the apparatus. This model excludes SecA2 of the accessory secretory system [Protein fate, Protein and peptide secretion and trafficking]
INALEEDYEKLSDEELRNKTNEFKDRLAKQGETLDDLLPEAFAVVREASKRVLGMRPFDVQLIGGIALHK
GKIAEMKTGEGKTLTATLPAYLNALTGKGVHVVTVNDYLAQRDAEWMGQVYRFLGLSVGLILSGMSPEER
REAYACDITYGTNNELGFDYLRDNMAHSKEEKVQRPFHFAIIDEVDSILIDEARTPLIISGPAEKSTELY
VQANKFAKALEKEVDYEVDEKNRAVLLTEQGMKKAEDLLGVDNLYDLENSPLIHYINNALKAKELFQKDV
DYIVRDGEVVIVDEFTGRIMEGRRWSDGLHQAIEAKEGVEIQNENQTLATITYQNFFRLYEKLSGMTGTA
KTEEEEFRKIYNLEVVVVPTNRPVIRKDRPDLVYKTEEEKWKAVVEEIKERHAKGQPVLVGTTSVEKSEL
LSNLLKERGIPHNVLNAKNHEREAEIIAQAGRKGAVTIATNMAGRGTDIKLEEVKELGGLYVIGTERHES
RRIDNQLRGRSGRQGDPGSSRFFLSLEDNLMRIFGGDRLEGLMRRLGMDDDEPIESKMVSRALESAQKRV
EGRNFDIRKQLLEYDDVLNKQREVIYAERRRVLESEDLSELILQMLESTLDRIVDAYINEEKLSEEWDLE
GLIEKLKTLFLLDGDLTPEDLENLTSEDLKELLLEKIRAAYDEKEEQLESERMREFERYVLLQSIDRKWK
EHLDAMDLLREGIGLRSYGQKDPLIEYKNEGFNLFEEMLEDI
>gnl|CDD|273367 TIGR00964, Protein_translocase_subunit_SecE, preprotein translocase, SecE subunit, bacterial. This model represents exclusively the bacterial (and some organellar) SecE protein. SecE is part of the core heterotrimer, SecYEG, of the Sec preprotein translocase system. Other components are the ATPase SecA, a cytosolic chaperone SecB, and an accessory complex of SecDF and YajC [Protein fate, Protein and peptide secretion and trafficking]
IFKFFKEVKAELKKVVWPSRKELITYTIVVIVFVLFFSLFLFGIDYVFGKLISLI
>gnl|CDD|130038 TIGR00965, dapD, 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase. This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-succinyltransferase. The closely related TabB protein of Pseudomonas syringae (pv. tabaci), SP|P31852|TABB_PSESZ, appears to act in the biosynthesis of tabtoxin rather than lysine. The trusted cutoff is set high enough to exclude this gene. Sequences below trusted also include a version of this enzyme which apparently utilize acetate rather than succinate (EC: 2.3.1.89) [Amino acid biosynthesis, Aspartate family]
QLQNIIETAFERRAEITPANADTVTKEAVNEVIALLDSGALRVAEKIDGQWKVNEWLKKAVLLSFRINDN
QVINGAENRYFDKVPMKFADYDEARFKKAGFRVVPGAAVRQGAFIAKNVVLMPSYVNIGAYVDEGTMVDT
WATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVFIGQST
KIYDRETGEIHYGRVPAGSVVVSGNLPSKDGKYSLYCAVIVKKVDAKTRGKVSINELLR
>gnl|CDD|273368 TIGR00966, Protein_translocase_subunit_SecF, protein-export membrane protein SecF. This bacterial protein is always found with the homologous protein-export membrane protein SecD. In numerous lineages, this protein occurs as a SecDF fusion protein [Protein fate, Protein and peptide secretion and trafficking]
GFNFGIDFTGGTVIETRLEQAADVAEVRDVLEKAGIEGVVIQEFGSSHTIMIRIPTLDTEQSEELREALE
EALKNVDPDAEIRSIDAVGPSVGGELARKAVLALLAALVLILIYITVRFEWRFALGAIVALVHDVIITVG
VYSLFGIEVNLTTVAALLTIIGYSINDTVVVFDRIRENLRKYTRKTFTEVINLSINQTLSRTINTSLTTL
LAVLALYVFGGGVIKDFSLALLVGVIVGTYSSIFIA
>gnl|CDD|273369 TIGR00967, Protein_translocase_subunit_SecY, preprotein translocase, SecY subunit. Members of this protein family are the SecY component of the SecYEG translocon, or protein translocation pore, which is driven by the ATPase SecA. This model does not discriminate bacterial from archaeal forms [Protein fate, Protein and peptide secretion and trafficking]
REKLLFTLGLLVLFRIGTFIPIPGIDASAFQNLIQQNPIFGLLNTFSGGALGQISIFALGISPYITASII
IQLLTGDVPPLLQLQKKEGEIGRRKINQLTRYLTLILAFIQSLGIVMTGMYGYVGDPGAFFYLLIVIQLT
TGSMIVMWLGEQITKYGIGNGISLLIFAGIAATIPSGLLQPTEVRQSKVRDLISFLQNLPFLLYLIATII
VFAVVVFVQQARRKIPIQSAKRQGGRRGSQSTYLPLKLNYAGVIPVIFASALLSNPATISQFLNSNQGGA
WFLNPILSLSLSDPIGAILYLILIIFFSFFYVELQLNPEDMAKNLKKQGMFIPGIRPGKMTEKYLKRVIP
RLTFVGSLFLGLIALLPNFLGAIGGLPTSKGLGGTSLLIVVGVAIDTYKQLESELISRNY
>gnl|CDD|130041 TIGR00968, 3a0106s01, sulfate ABC transporter, ATP-binding protein [Transport and binding proteins, Anions]
IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR
DRKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVA
LARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIE
QIGSPDEVYDHPANPFVMSFLGEVNVL
>gnl|CDD|273370 TIGR00969, Sulfate_transport_system_permease_protein_CysT, sulfate ABC transporter, permease protein. This model describes a subfamily of both CysT and CysW, paralogous and generally tandemly encoded permease proteins of the sulfate ABC transporter [Transport and binding proteins, Anions]
MTALPSARFRFIKWGKLSLGIALLYVFLILILPVAALFVQAFSKGLGQFWQNATDPIAVSAYNLTLLMAL
IAVPLNGVFGLLIAWVLTRYQFPGRKLLDALIDLPFALSPVVAGLTLALLYGSNGWLGSWLASFGIQIIF
TWPGMALAMIFVSLPFVVREVQPVLEELGTEAEEAAATLGASGWQTFWRVTLPSIRWALLYGVVLTFARA
LGEFGAVVVVSGNIPGKTLTLPLLIEERLEQYDYPGAYVIAAVLLLVSLVTLFLINALQAR
>gnl|CDD|273371 TIGR00970, 2-isopropylmalate_synthase, 2-isopropylmalate synthase, yeast type. A larger family of homologous proteins includes homocitrate synthase, distinct lineages of 2-isopropylmalate synthase, several distinct, uncharacterized, orthologous sets in the Archaea, and other related enzymes. This model describes a family of 2-isopropylmalate synthases as found in yeasts and in a minority of studied bacteria [Amino acid biosynthesis, Pyruvate family]
PSNKYKPFAPIRLRNRTWPDRVITRAPRWLSTDLRDGNQALPDPMSPARKRRYFDLLVRIGFKEIEVGFP
SASQTDFDFVREIIEQGAIPDDVTIQVLTQSREELIERTFEALSGAKRATVHFYNATSILFREVVFRASR
AEVQAIATDGTKLVRKCTKQAAKYPGTQWRFEYSPESFSDTELEFAKEVCEAVKEVWAPTPERPIIFNLP
ATVEMTTPNVYADSIEYFSTNIAEREKVCLSLHPHNDRGTAVAAAELGFLAGADRIEGCLFGNGERTGNV
DLVTLALNLYTQGVSPNLDFSNLDEIRRTVEYCNKIPVHERHPYGGDLVYTAFSGSHQDAINKGLDAMKL
DAAAADMLWQVPYLPLDPRDVGRTYEAVIRVNSQSGKGGVAYIMKTDHGLDLPRRLQIEFSSVVQDIADG
EGGELSPKEISDLFAEEYLAPVEPLERISQHVYAADDDGTGTTSITATVKINGVETDIEGSGNGPLSALV
DALADVGNFDFAVLDYYEHAMGSGDDAQAASYVEASVTIASPAQPGTVWGVGIAPDVTTASLRAVVSAVN
RAAR
>gnl|CDD|130044 TIGR00971, Thiosulfate-binding_protein, sulfate/thiosulfate-binding protein. This model describes binding proteins functionally associated with the sulfate ABC transporter. In the model bacterium E. coli, two different members work with the same transporter; mutation analysis says each enables the uptake of both sulfate and thiosulfate. In many species, a single binding protein is found, and may be referred to in general terms as a sulfate ABC transporter sulfate-binding protein [Transport and binding proteins, Anions]
LAATSLLAKDIQLLNVSYDPTRELYEQYNKAFEAHWKQETGDNVVIRQSHGGSGKQATSVINGIEADVVT
LALAYDVDAIAERGRIDKDWIKRLPDNSAPYTSTIVFLVRKGNPKQIHDWNDLIKPGVSVITPNPKSSGG
ARWNYLAAWGYALHHNNGDQAKAQQFVTALLKNVEVLDSGARGATNTFVERGIGDVLIAWENEALLARKE
LGKDKFEIVTPSESILAEPTVSVVDKVVEKKGTKKVAEAYLKYLYSPEGQEIAAKNYYRPRDAEVAKKYE
DKFPKLKLFTIDDKFGGWPKAQKTHFANGGTFDQI
>gnl|CDD|273372 TIGR00972, Phosphate_import_ATP-binding_protein_PstB_2, phosphate ABC transporter, ATP-binding protein. This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters [Transport and binding proteins, Anions]
AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDI
YDKKIDVVELRRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHD
SALGLSGGQQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARIS
DRTAFFYDGELVEYGPTEQIFTNPKEKRTEDYISGRF
>gnl|CDD|130046 TIGR00973, 2-isopropylmalate_synthase, 2-isopropylmalate synthase, bacterial type. This is the first enzyme of leucine biosynthesis. A larger family of homologous proteins includes homocitrate synthase, distinct lineages of 2-isopropylmalate synthase, several distinct, uncharacterized, orthologous sets in the Archaea, and other related enzymes. This model describes a family of 2-isopropylmalate synthases found primarily in Bacteria. The homologous families in the Archaea may represent isozymes and/or related enzymes [Amino acid biosynthesis, Pyruvate family]
RIIIFDTTLRDGEQSPGASLTVEEKLQIALALERLGVDIIEAGFPVSSPGDFEAVQRIARTVKNPRVCGL
ARCVEKDIDAAAEALKPAEKFRIHTFIATSPIHLEHKLKMTRDEVLERAVGMVKYAKNFTDDVEFSCEDA
GRTEIPFLARIVEAAINAGATTINIPDTVGYALPAEYGNLIKGLRENVPNIDKAILSVHCHNDLGLAVAN
SLAAVQNGARQVECTINGIGERAGNAALEEVVMALKVRKDFLGVETGINTKEIYRTSRLVSQLTGMPVQP
NKAIVGDNAFAHESGIHQDGVLKNKETYEIMSPEDIGLTAEQLVLGKHSGRHAFKDRLEELGFKLDDEEL
DKLFEKFKELADKKKEVTDEDLEALVFEEKRQEPEEGYKLLHFQVHSGTNQVPTATVKLKNGGEKREAAA
TGNGPVDAVYKAINRALGIEVELLEYSITAVGEGKDALGQVDVVLRHNGVKYSGRGVATDIVEASAKAYL
NALN
>gnl|CDD|273373 TIGR00974, 3a0107s02c, phosphate ABC transporter, permease protein PstA. This model describes PtsA, one of a pair of permease proteins in the ABC (high affinity) phosphate transporter. In a number of species, this permease is fused with the PtsC protein (TIGR02138). In the model bacterium Escherichia coli, this transport system is induced when the concentration of extrallular inorganic phosphate is low. A constitutive, lower affinity transporter operates otherwise [Transport and binding proteins, Anions]
DKIFTFISLLSALLALLPLIWILWYILIKGLPALNLEFFTKSPTPTGAEGGIGPAIVGTLLLTLLAIVIA
VPLGIGAAIYLAEYANGSRFTKIIRFAVDILAGVPSIVVGLFGYGFFVLTYLGGGFSLLAGALALALLIL
PVIIRTTEEALKAVPKDLREASLALGATKWQTIFKVVLPAALPGILTGIILSIARAAGETAPLLFTAGGS
AFTPPNLFDPFATLPVLIYNLASEGPYVEAQQLAWAAALVLIVLVLLLNLIARLLRRRFKK
>gnl|CDD|273374 TIGR00975, precursor_PBP-3_PstS-3_Antigen_Ag88., phosphate ABC transporter, phosphate-binding protein. This family represents one type of (periplasmic, in Gram-negative bacteria) phosphate-binding protein found in phosphate ABC (ATP-binding cassette) transporters. This protein is accompanied, generally in the same operon, by an ATP binding protein and (usually) two permease proteins [Transport and binding proteins, Anions]
LTGAGSTFPAPLYTKWFPDFQKSNPGVTINYQGIGSGAGIAQFAAGTVDFGASDAPLSEADLAAAGSGLL
NFPTVIGAIVVTYNLPGVSEKLKLDGPVLAKIFLGKIKQWNDPAIAALNPGVKLPGTAITVVHRSDGSGT
TFNFTNYLSKVSPEWGKKVGAGKTVQWPAGVGGKGNDGVVAGVKQTPGAIGYVEWSFAKQNKLSFAALKN
SAGKFVLPDAESIKAAAAGAKISTPKNDAISMTDPPGPGAYPIVSYTYLIVYKKQKDPAKAKALKAFLTW
AITNGQSFLDDLGYIPLPPSVVKRVRTAVNTIS
>gnl|CDD|273375 TIGR00976, Hypothetical_protein_Rv1835c/MT1883/Mb1866c., putative hydrolase, CocE/NonD family. This model represents a protein subfamily that includes the cocaine esterase CocE, several glutaryl-7-ACA acylases, and the putative diester hydrolase NonD of Streptomyces griseus (all hydrolases). This family shows extensive, low-level similarity to a family of xaa-pro dipeptidyl-peptidases, and local similarity by PSI-BLAST to many other hydrolases [Unknown function, Enzymes of unknown specificity]
VPMRDGTRLAIDVYRPAGGGPVPVILSRTPYGKDAGLRWGLDKTEPAWFVAQGYAVVIQDTRGRGASEGE
FDLLGSDEAADGYDLVDWIAKQPWCDGNVGMLGVSYLAVTQLLAAVLQPPALRAIAPQEGVWDLYRDIAF
PGALRLDVLLGWWALLATDSMRPRADDRPPRYAAAARLAQSYDDCQTALSHTPRSSVLALDRFIGWWIQV
VDDDYDESWVSISLWRDLGGSDVPTLVTGGWYDNHSRGSIRLFLAVHRGGAQRLVVGPWTHSGLGGRVGD
GNYGMAALSWVDEAEQLAFFDRHLKGGTTGVRSEPKVRLFTMGDDAWRAETTWPLPGTRTTPYYLGGSYG
TADGASGGALSTAPPSPTEGADPYLYDPWDPVPSLGGQLSGAGGPAGPAKQDRIDDRDDVLTYTSEPLTE
PLEVTGTVRVRLFARSDAPDGDFAVKLTDVDPDGRAIALDEGICRVRYRRTSVNGEIYEVDIDLGATANL
FAPGHRLRVEVGSSNFPHYDRNPGTGPVAVKNLVAMATARNTLHRGPEHQSHILLPIIPG
>gnl|CDD|130050 TIGR00977, citramal_synth, citramalate synthase. This model includes GSU1798 and is now known to represent citramalate synthase. Members are related to 2-isopropylmalate synthases and homocitrate synthases but phylogenetically distinct. The role is isoleucine biosynthesis, the first dedicated step [Unknown function, General]
SLWLYDTTLRDGAQREGVSFSLEDKIRIAERLDDLGIHYIEGGWPGANPKDVQFFWQLKEMNFKNAKIVA
FCSTRRPHKKVEEDKMLQALIKAETPVVTIFGKSWDLHVLEALQTTLEENLAMIYDTVAYLKRQGDEVIY
DAEHFFDGYKANPEYALATLATAQQAGADWLVLCDTNGGTLPHEISEITTKVKRSLKQPQLGIHAHNDSG
TAVANSLLAVEAGATMVQGTINGYGERCGNANLCSLIPNLQLKLGYDVIPPENLKKLTSTARLVAEIVNL
PPDDNMPYVGRSAFAHKGGVHVSAVQRNPFTYEHIAPELVGNERRIVVSELAGLSNVLSKAKEFGIEIDR
QSPACRTILAKIKELEQQGYHFEAAEASFELLMRQAMGDRKPYFLFQGFQVHCDKLRDAESYRNALATVR
VTVEGQNEHTAAEGNGPVSALDRALRKALERFYPQLKDFHLTDYKVRILNEGAGTSAKTRVLIESSDGKR
RWGTVGVSGNIIEASWQALVESIEYKLRKDEEELTN
>gnl|CDD|273376 TIGR00978, Aspartate-semialdehyde_dehydrogenase, aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms). Two closely related families of aspartate-semialdehyde dehydrogenase are found. They differ by a deep split in phylogenetic and percent identity trees and in gap patterns. Separate models are built for the two types in order to exclude the USG-1 protein, found in several species, which is specifically related to the Bacillus subtilis type of aspartate-semialdehyde dehydrogenase. Members of this type are found primarily in organisms that lack peptidoglycan [Amino acid biosynthesis, Aspartate family]
MRVAVLGATGLVGQKFVKLLAKHPYFELAKVVASPRSAGKRYGEAVKWIEPGDMPEYVRDLPIVEPEPVA
SKDVDIVFSALPSEVAEEVEPKLAEAGKPVFSNASNHRMDPDVPLIIPEVNSDHLELLKVQKERGWKGFI
VTNPNCTTAGLTLALKPLIDAFGIKKVHVTTMQAVSGAGYPGVPSMDILDNIIPHIGGEEEKIERETRKI
LGKLENGKIEPAPFSVSATTTRVPVLDGHTESVHVEFDKKFDIEEIREALKSFRGLPQKLGLPSAPEKPI
IVRDEEDRPQPRLDRDAGGGMAVTVGRLREEGGSLKYVVLGHNLVRGAAGATLLNAELAYK
>gnl|CDD|130052 TIGR00979, Fumarate_hydratase_class_II, fumarate hydratase, class II. Putative fumarases from several species (Mycobacterium tuberculosis, Streptomyces coelicolor, Pseudomonas aeruginosa) branch deeply, although within the same branch of a phylogenetic tree rooted by aspartate ammonia-lyase sequences, and score between the trusted and noise cutoffs [Energy metabolism, TCA cycle]
FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAI
VQAADEILAGKLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDT
FPTAMHIAAVLAIKNQLIPALENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLE
RIAYSLPHLYELAIGGTAVGTGLNTHPGFDEKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKT
LAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPGKVNPTQCEALTMVCVQVMGNDATIGFAGSQ
GNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLNNSLMLVTALNPHIGYDNAAK
IAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG
>gnl|CDD|130053 TIGR00980, 3a0801so1tim17, mitochondrial import inner membrane translocase subunit tim17 [Transport and binding proteins, Amino acids, peptides and amines]
MEEYTREPCPYRILDDFGGAFAMGTIGGSIFQAFKGFRNSPKGEKLVGAMRAIKTRAPVLGGNFAVWGGL
FSTIDCAVVAIRKKEDPWNSIISGFLTGAALAVRGGPRAMRGSAILGACILAVIEGVGLVLTRWAAAQMD
PTAPEAPDDPSSLPQSAQAEPGLDQTRPFG
>gnl|CDD|130054 TIGR00981, 30S_ribosomal_protein_S12, ribosomal protein S12, bacterial/organelle. This model recognizes ribosomal protein S12 of Bacteria, mitochondria, and chloroplasts. The homologous ribosomal proteins of Archaea and Eukarya, termed S23 in Eukarya and S12 or S23 in Archaea, score below the trusted cutoff [Protein synthesis, Ribosomal proteins: synthesis and modification]
MPTINQLIRKGRKKKKKKSKSPALEACPQKRGVCTRVYTTTPKKPNSALRKVARVRLTNGFEVTAYIPGE
GHNLQEHSVVLIRGGRVKDLPGVRYHIVRGALDTAGVKNRKQGRSKYGAKRPKA
>gnl|CDD|273377 TIGR00982, 30S_ribosomal_protein_S12, ribosomal protein uS12, eukaryotic/archaeal form. This model represents eukaryotic and archaeal forms of ribosomal protein uS12. This protein was known previously as S23 in eukaryotes and as either S12 or S23 in the Archaea [Protein synthesis, Ribosomal proteins: synthesis and modification]
GLFAARKLKLKRKKFRWSDRRYKRRVLRLKEKADPLEGAPQARGIVLEKIGVEAKQPNSAIRKAVRVQLI
KNGKVVTAFCPGDGAINFIDEHDEVIIEGIGGPKGRSMGDIPGVRYKVVKVNNVSLKELVKGRKEKPRR
>gnl|CDD|130056 TIGR00983, 3a0801s02tim23, mitochondrial import inner membrane translocase subunit tim23 [Transport and binding proteins, Amino acids, peptides and amines]
LAPLDKDPEYLVQEEDELSLLTGANPSRGWFEDLCFGTGTCYLTGLAIGALNGLRLGLKETQSMPWTKLR
LNQILNMVTRRGPFWGNTLGILALVYNGINSIIEATRGKHDDFNSVAAGALTGALYKSTRGLRGMARSGA
LGATAAGVW
>gnl|CDD|130057 TIGR00984, 3a0801s03tim44, mitochondrial import inner membrane, translocase subunit. The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents.These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of the Tom channel complex, five proteins of the inner membrane translocase (Tim) and three "motor" proteins. This family is specific for the Tim proteins [Transport and binding proteins, Amino acids, peptides and amines]
DTFRDELQKSQELQESIKQLQDRSGKLNESDALKKARKAYEKAESGTLKSSEVVGKTLGKLGDTMKKMAH
KAWESELGKKMKKAGAETAKTAAEHVDKSAEPVRDTAVYKHVSQSMKDGKDSSRYGFIADKEQRRRPREL
TKRTDGRDFAKSRVVEANESVTDVVLHSDSSWYSKVEDFKESNVVYRKIQELKKKYDESENPLVRMMRGV
TDKIGGVFSGMFSETEVSEVLTEFKKIDPTFDKEHFLRFLREYIVPEILEAYVKGDLEVLKSWCSEAPFS
VYATVVKEYKKMGVSTKGRILDIRGVEIASGKLLEPGDIPVLIVTFRAQEINVTKNAKSGEVVAGDPDNI
QRINYAWVFTRDVEELDNPETLGWKILE
>gnl|CDD|273378 TIGR00985, Mitochondrial_import_receptor_subunit_TOM20, mitochondrial import receptor subunit translocase of outer membrane 20 kDa subunit [Transport and binding proteins, Amino acids, peptides and amines]
MLGSNKSNVVIAAGIAAAAFLGYAIYFDYKRRNDPDFRKKLRRRRKKQAGAEKQYGGLAKEKQRQRIRPA
AAGLAKAPDPTDPSEKEAFFLQEVQLGEELMAQGTNVDEGAVHFYNALKVYPQPQQLLSIYQQTLPEPIF
RLMIAQLP
>gnl|CDD|273379 TIGR00986, Mitochondrial_import_receptor_subunit_tom22, mitochondrial import receptor subunit Tom22. The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents.These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of the Tom channel complex, five proteins of the inner membrane translocase (Tim) and three "motor" proteins. This family is specific for the Tom22 proteins [Transport and binding proteins, Amino acids, peptides and amines]
MVQLTEVEDEHFQQPEQQTVVEPEEDDEDFTDVDSEDSVDSDFESLEEETFTDRIYALKDIVPPTTRGWI
YHKYSTTTNFVKSTLSFAGRAAWAVSTSALLLGVPFAISFAEEQQLAEMEKEARMQELANDVLAAGGEGQ
AGTAE
>gnl|CDD|130060 TIGR00987, Integration_host_factor_alpha-subunit_IHF-alpha., integration host factor, alpha subunit. This protein forms a site-specific DNA-binding heterodimer with the integration host factor beta subunit. It is closely related to the DNA-binding protein HU [DNA metabolism, DNA replication, recombination, and repair]
ALTKAEMSEYLFDELGLSKREAKELVELFFEEIRRALENGEQVKLSGFGNFDLRDKNQRPGRNPKTGEEI
PITARRVVTFRPGQKLKSRVENASPK
>gnl|CDD|130061 TIGR00988, Integration_host_factor_subunit_beta, integration host factor, beta subunit. This protein forms a site-specific DNA-binding heterodimer with the homologous integration host factor alpha subunit. It is closely related to the DNA-binding protein HU [DNA metabolism, DNA replication, recombination, and repair]
MTKSELIERIATQQSHLPAKDVEDAVKTMLEHMASALAQGDRIEIRGFGSFSLHYRAPRTGRNPKTGDSV
ELDGKYVPHFKPGKELRDRANIYE
>gnl|CDD|130062 TIGR00989, Mitochondrial_import_receptor_subunit_TOM40, mitochondrial import receptor subunit Tom40. The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents.These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of the Tom channel complex, five proteins of the inner membrane translocase (Tim) and three "motor" proteins. This family is specific for the Tom40 proteins [Transport and binding proteins, Amino acids, peptides and amines]
LSNPGTIENLAKEVSRDTLLSNYMFTGLRADVTKAFSLAPLFQVSHQFAMGSQRLPPYAFSALFGTNQLF
AQGNLDNDGAVSTRLNYRWGDRTISKVQFQISGGQPDMCQFEHDHLGDDFSASLKAINPSFLEKGLTGIF
VGSYLQSVTPRLGLGLEALWQ
>gnl|CDD|273380 TIGR00990, Mitochondrial_import_receptor_subunit_TOM70, mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70) [Transport and binding proteins, Amino acids, peptides and amines]
MAPTIPPPPAATPVTVPADSSIWDRMSNWISENKTAVYTIAGVTVVATGAGVVYYQRKGQQQRESKPKIS
KKERRKRKQAEKETEGKTEEKKSTAPKNAPVEPADELPEIDESSVANLSEEERKKYAAKLKEKGNKAYRN
KDFNKAIKLYSKAIECKPDPVYYSNRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANAYDGLGKY
ADALLDLTASCIIDGFRNEQSAQAVERLLKKFAESKAKEILETKPENLPSVTFVGNYLQSFRPKPRPAGL
EDSNELDEETGNGQLQLGLKSPESKADESYEEAARAFEKALDLGKLGEKEAIALNLRGTFKCLKGKHLEA
LADLSKSIELDPRVTQSYIKRASMNLELGDPDKAEEDFDKALKLNSEDPDIYYHRAQLHFIKGEFAQAGK
DYQKSIDLDPDFIFSHIQLGVTQYKEGSIASSMATFRRCKKNFPEAPDVYNYYGELLLDQNKFDEAIEKF
DTAIELEKETKPMYMNVLPLINKALALFQWKQDFIEAENLCEKALIIDPECDIAVATMAQLLLQQGDVDE
ALKLFERAAELARTEGELVQAISYAEATRTQIQVQEDYPVLASKLQGMLGGLRER
>gnl|CDD|130064 TIGR00991, GTP-binding_protein, GTP-binding protein (Chloroplast Envelope Protein Translocase) [Transport and binding proteins, Nucleosides, purines and pyrimidines]
MASPQTPREWVGIQQFPPATQTKLLELLGKLKEEDVSSLTILVMGKGGVGKSSTVNSIIGERIATVSAFQ
SEGLRPMMVSRTRAGFTLNIIDTPGLIEGGYINDQAVNIIKRFLLGKTIDVLLYVDRLDAYRVDTLDGQV
IRAITDSFGKDIWRKSLVVLTHAQFSPPDGLEYNDFFSKRSEALLRVIHSGAGLKKRDYQDFPIPVALVE
NSGRCKKNESDEKILPDGTPWIPKLMKEITEVISNGSKPIHVDKKLIDGPNPNNRGKMFIPLIFAVQYLL
VVKPIRRAIHADIANEKKDAWEQRDRGLVNRKA
>gnl|CDD|130065 TIGR00992, chloroplast_import-associated_channel_homolog, chloroplast envelope protein translocase, IAP75 family. Two families of proteins are involved in the chloroplast envelope import appartus.They are the three proteins of the outer membrane (TOC) and four proteins in the inner membrane (TIC). This family is specific for the TOC IAP75 protein [Transport and binding proteins, Amino acids, peptides and amines]
GGLGGGVGDLPPMGGGGGGELAGAHGNFWAQVASPVAAVADENLSADWDSHNLPAHIEVQLPLLSGFKKY
KESDIVFFDRTEETTGVTEDSFEEMVSFTPGGVYTKAQLQKELEVLATCGMFEKVDYEGKTTQDGRLGTT
ISFAESVWAIADRFRCINVGLMPQSKPLEMDVDMEVKEKPEFTRRLEIRYKRRIAEARPCLLPQEVVDET
FGMLYGQGIVSARLLQEIRDRVQEWYHNEGYACAQVVNFGNLNTDEVVCEVVEGDITNLQIQFFDKLGNV
VEGNTRDPVVTRELPKQLKPGDVFNIEAGKTALQNINSLGLFSNIEVNPRPDEMNEGEIIVEIKLKELEQ
KSAEVSTEWSIVPGRGGRPTLASSQPGGTITFEHRNLQGLNRSLGGSVTTSNFLNPQDDLLFKVEYTHPY
LDGVDNPRNRTYTASCFNSRKLSPVFTGGPGVNEVPSIWVDRAGVKANITENFARQSKFTYGLVMEEIFT
RDESRHINANGQRSLPSGPISADGPPTTLSGTGVDRMAFLQANITRDNTNFVNGPTVGSRVRFQVDQGLG
VGSGFPFFNRHQLTYTKFIQLNWVELGAGKSPPPVLVLHGHYGGCVGDLPSYDAFILGGPYSVRGYNMGE
LGAARNIFEATAEIRIPIKATHVYAFVEHGSDLGSSKDVKGNPTIVYRRPGQGSSYGAGVKLGLVRAEYA
VDHNEGTGAIFFRFGERF
>gnl|CDD|273381 TIGR00993, putative_chloroplast_outer_membrane_protein, chloroplast protein import component Toc86/159, G and M domains. The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M [Transport and binding proteins, Amino acids, peptides and amines]
RPAGLGRSLPLLKPASAPRQSRVNGFGSSNQFQQAEDSTTTLSEEHKEKLEKLQLIRVKFLRLAQRLGQT
PENSIAAQVLYRLGLLAGRQGGGAFSLDAAKAMAEQLEAEGQDPLDFSLNILVLGKSGVGKSATINSIFG
EVKFSTDAFGMGTTSVQEIEGLVQGVKIRVIDTPGLKSSASDQSKNEKILSSVKKFIKKNPPDIVLYVDR
LDMQTRDSNDLPLLRTITDVLGPSIWFNAIVTLTHAASAPPDGPNGTPLSYDVFVAQRSHIVQQAIGQAV
GDLRLMNPNLMNPVSLVENHPACRKNRAGQKVLPNGQVWKPHLLLLCYSSKILSEANALLKLQENIDGRR
PFGFRSRAPPLPYLLSWLLQSRAHPKLPEQQGGDEEDSDIELEDSSDSDEESGEDEYDQLPPFKPLTKAQ
MAKLSKEQRKAYLEEYDYRVKLLQKKQWREELKRMKMMKKFGKEIGELPDGYSEEVDEENGGPAAVPVPL
PDMVLPASFDSDNPAYRYRYLEPSSQLLTRPVLDTHGWDHDCGYDGVNAERSFAVKEKFPASVTVQVTKD
KKDFNIHLDSSVSAKHGENGSTMAGFDIQNVGKQLAYTVRGETKFKNFRRNKTAAGLSVTFLGENVSTGV
KLEDQIALGKRLVLVGSTGTMRSQGDSAYGANLEVRLREADFPLGQDQSSLGLSLVDWRGDLALGANIQS
QVSIGRSSKLAARAGLNNKGSGQISVRTSSSDQLQIALVAILPLAKKIYKYYYPQTTENYSQY
>gnl|CDD|273382 TIGR00994, putative_chloroplast_protein_import_component, chloroplast protein import component, Tic20 family. Two families of proteins are involved in the chloroplast envelope import appartus.They are the three proteins of the outer membrane (TOC) and four proteins in the inner membrane (TIC). This family is specific for the Tic20 protein [Transport and binding proteins, Amino acids, peptides and amines]
MIGNGATTTNGGSLTFLAHSPISKKFVNPRVFFPNKDASSKIRLSASSISRRCPREIAPLSASASSDFAL
AGTSNGLPPTAPGLPTHRRSIEPPRAAKDDFSKFRFPPMTEKPRWWWRTLACVPYLIPLHISWMYADTAY
HLHPFLEKFDAITYPFLGAIGRLPTWFLMAYFLLAYMWVVRRKEWPHFFRFHMMMGMLLEIALQVIGCVS
RWFPLIHYWGKFGMYYWTAIGFTYLFTLLECIRCALAGMYADVPFMCDAAYIQIPFN
>gnl|CDD|273383 TIGR00995, Tic22-like_protein, chloroplast protein import component, Tic22 family. Two families of proteins are involved in the chloroplast envelope import appartus.They are the three proteins of the outer membrane (TOC) and four proteins in the inner membrane (TIC). This family is specific for the Tic22 protein [Transport and binding proteins, Amino acids, peptides and amines]
MESSFRRNPFLSFSRFIKHKIFVKIKFLLSRLEETKRTAKTLLRIGATLGTIPTFAIGTWLGTTLQALTL
PPEEVAKILAGTSVFTVSNAQNEFVLASDNDGEKSIGLLCFRQEDAEAFLAQLRKRKPEVGSQAKVVPIT
LDQVYKLKVEGIGFRFLPDPAQIKNALELPAANSEYFDGVPVFQSGLLVVQKKNERYCPVYFSKEDIEQE
LSKFKRESPGMADSQVIMVGSMEDVLSKMETSEKDSGWEDQIFIPPGQEAIQHMQSLIAQ
>gnl|CDD|273384 TIGR00996, Mtu_fam_mce, virulence factor Mce family protein. Members of this paralogous family are found as six tandem homologous proteins in the same orientation per cassette, in four separate cassettes in Mycobacterium tuberculosis. The six members of each cassette represent six subfamilies. One subfamily includes the protein mce (mycobacterial cell entry), a virulence protein required for invasion of non-phagocytic cells [Cellular processes, Pathogenesis]
RLGTVAVVVLALVVVLAVVFLRLPFTGFGPGTTTVVAYFTDAGGLYPGDKVRVAGVPVGKVTAIEPRGAR
ARVTFSLDRSVTLPANATAAIRTTTLLGSRYIELTPPGGPPGGRLSDGGTIPLSRTTVPLELDDLLGSLT
RLLNGLDPEKLNAILNALAQALAGQGPQLRNLLDGLAQLTAALNERDGDIGELIRNLNRVLDVLADRSDQ
LDRLLDNLPTLIATLADRSDALDDALAALSAASAQVRDLLAENRPNLGQALANLAPVLTLLVDYSPELEQ
LLHLLPTYAAN
>gnl|CDD|130070 TIGR00997, Probable_intracellular_septation_protein_A, intracellular septation protein A. This partially characterized protein, whose absence can cause a cell division defect in an intracellularly replicating bacterium, is found only so far only in the Proteobacteria [Cellular processes, Cell division]
MKLALDLLPLIVFFATYKMTGIFAATIALLVATIIAIGLSYVKYKKVEKMQWISFVLIVVFGGLTLIFHD
SRFIKWKPTIIYGLFAVILLGSQLFGKTPGIKYMLGKEFQLTEKGWLKLNFRWAGFFIFMAVLNEYVATN
FSEEIWVNFKVFGVTILTFIFIIAQGPYLYRNMLKDGK
>gnl|CDD|273385 TIGR00998, Probable_multidrug_resistance_protein_EmrK, efflux pump membrane protein (multidrug resistance protein A) [Transport and binding proteins, Other]
RKYFLLLLVVLLIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVL
VRLDPTNAELALAKAEANLAALVRQTKQLEITVQQLQAKVESLKIKLEQAREKLLQAELDLRRRVPLFKK
GLISREELDHARKALLSAKAALNAAIQEQLNANQALVRGTPLKKQPAVQEAKERLKTAWLALKRTVIRAP
FDGYVARRFVQVGQVVSPGQPLMAVVPAEQMYVEANFKETQLKNVRIGQPVTIRSDLYGSDVVFEGKVTG
ISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKELDEHPLRIGLSAEVEI
>gnl|CDD|273386 TIGR00999, Nickel-cobalt-cadmium_resistance_protein_NccB, Membrane Fusion Protein cluster 2 (function with RND porters) [Transport and binding proteins, Other]
GDPVKKGQVLAVVDSPELAKMAAELKVAQKRVELARKTYEREKKLFEQGVIPRQEFESAEYALEEAQAEV
QAAKSELRSAREAKDGSYVEVRSPFDGYITQKSVTLGDYVAPQAELFRVADLGAVWVEAEVPAKDVSRIR
KGSKATVLLENGRPLPARVDYVGPEVDGSSRTAKVRVLIKNENLTLKPGLFVQVRVETKIGEPAIAVPED
AVQDLGGRKVVFVRTQEGFRPRPVKVGRRLGGYYEVLEGLKPGERVAVENTFLLK
>gnl|CDD|273387 TIGR01000, Mesentericin_Y105_secretion_protein_MesE, bacteriocin secretion accessory protein. This family represents an accessory protein that works with the bacteriocin maturation and ABC transport secretion protein described by TIGR01193 [Transport and binding proteins, Other]
MDKKFLESSEFYQKRYHNFSTLVIVPIFLLLVFLVLFSLFAKKEIVIRTTGTIEPAKILSKIQSTSNNAI
KENYLKENKFVKKGDLLVVYDNGNEENQKQLLEQQLDNLKDQKKSLDTLKQSIENGRNQFPTDDSFGYRN
LFNGYLAQVESLTSETQQQNDKSQTQNEAAEKTKAQLDQQISKTDQKLQDYQALKNAISNGTKVANFNPY
QSLYENYQAQLKSASDKDQKNQVKSTILATIQQQIDQLQKSIASYQVQKAGLTKSTASNYASSQNSKLAQ
LKEQQLAKVKQEITDLNQKLLELESKIKSLKEDSQKGVIKAPEDGVLHLNPETKGIKYVPKGTLIAQIYP
ILEKERKLKVTAYLPSNDISGIKVGQKVRFKLTQNVPKPIILDGTITSISSAPTATKKGNFYKVIATIKI
TKNQAELIRYGLTGKISTITGKKTYFNYYKDKLLNNN
>gnl|CDD|130074 TIGR01001, Homoserine_O-succinyltransferase, homoserine O-succinyltransferase. The apparent equivalog from Bacillus subtilis is broken into two tandem reading frames [Amino acid biosynthesis, Aspartate family]
MPIRVPDGLPAVKVLRKENIFVMTESRASHQDIRPLEILILNLMPKKIETENQFLRLLSNSPLQVNITLL
RTDSRKSKNTPIEHLNKFYTTFEAVKDRKFDGLIITGAPVELVPFEDVAYWEELTEIMEWSKHNVTSTMF
ICWAAQAGLKYFYGIPKYTLPEKLSGVYKHDIAPDSLLLRGFDDFFLAPHSRYADFDAEDIDKVTDLEIL
AESDEAGVYLAANKDERNIFVTGHPEYDAYTLHQEYVRDIGRGLKPPIPANYFPNDDPTKTPIASWRSHA
HLLFANWLNYCVYQKTPYDL
>gnl|CDD|273388 TIGR01002, synergohymenotropic_toxin, beta-channel forming cytolysin. This family of cytolytic pore-forming proteins includes alpha toxin and leukocidin F and S subunits from Staphylococcus aureus, hemolysin II of Bacillus cereus, and related toxins [Cellular processes, Toxin production and resistance]
KILLSATLTLVALVILSNPLTGAKTSTPKTSEEDIDDKITVYKSTATTSSDKLGITQSITFSFIKDKYYD
KDTLIIKTAGNINSKYTKNNPDGTNNSGLYWPSAYNISILSESNNSVQIVDYAPKNTIETKQVQSTLGYS
IGGSIEISENKIGGSINGSFSFSETIKYVQPDYKTILEKHTDKKIGWKVKFNSFVNAGWGPYGRDSFNPV
YGNELFMKGRQSNLNATDNFLDDNQMPKLITGGFNPNFIAVLTADKNASKSSKIKVTYEREMDCYTLYWN
SFNWVGTNYKDAFNATFTSTYKIDWKTHEVTL
>gnl|CDD|273389 TIGR01003, Phosphocarrier_protein_HPr, Phosphotransferase System HPr (HPr) Family. The HPr family are bacterial proteins (or domains of proteins) which function in phosphoryl transfer system (PTS) systems. They include energy-coupling components which catalyze sugar uptake via a group translocation mechanism. The functions of most of these proteins are not known, but they presumably function in PTS-related regulatory capacities. All seed members are stand-alone HPr proteins, although the model also recognizes HPr domains of PTS fusion proteins. This family includes the related NPr protein [Signal transduction, PTS]
MLSKEVTIINKVGLHARPAAILVKLASGFDSEITLTKNGKEVNAKSIMGIMMLGAGQGTEVTVSADGEDE
AEALEALAKLFE
>gnl|CDD|273390 TIGR01004, Pullulanase_secretion_protein_PulS, lipoprotein, PulS/OutS family. This family comprises lipoproteins from four gamma proteobacterial species: PulS protein of Klebsiella pneumoniae, the OutS protein of Erwinia chrysanthemi and Pectobacterium chrysanthemi, and the functionally uncharacterized E. coli protein EtpO. PulS and OutS have been shown to interact with and facilitate insertion of secretins into the outer membrane, suggesting a chaperone-like, or piloting function for members of this family [Transport and binding proteins, Amino acids, peptides and amines]
MMVNSLKVVLFGVCCVSLSGCQQNTASRSAASVPANEQLEQLASLVAASRYLKVQCNRSDLPDDGTILKT
AVNVAVQKGWDTGRYQSLPQLSENLYQGLLKDSTPEATKCSSFNRTLTPFIDALRTVR
>gnl|CDD|273391 TIGR01005, Putative_tyrosine-protein_kinase_EpsB, exopolysaccharide transport protein family. The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
DGEIDLDRLLAALFANARLIAAFAAAFIALGAAYAFFARPVYEADIMILLDDNLNKAAEEEGDPSNLFDL
DTDAAAAIEILKSGELAGKAVDKLHLSENAKILNPPRFPVDLIGAWIKSAAGLFSEPGGFDLGEEAAGNE
RIDKAAADIPEALAGEPFKLISLGAGAFRLEDKLLAAPIAGGVAEALEADQLIANFEAQENALTAKAEAL
FDLEQDSQAAALEMAHDKAEIAEKAAQGEIIGEAQLADLNPALIAAIADQAAAEARADNIKRIADEAEEN
AVFLAGILPKEGDELEIADLKTNELRNGKGEFDLSDEFGADHPEAVCSAPSLQELKAKIAEELQQFTASH
KGEQAIAQQIEESLRGKINGIAGKLKDAPEIEQDLRELEQDAAADKELYESLLGDMEQAKLQKAFKIAKA
RLIDEAAVPEEPSKPKKLMTLALAAVLGMMLGGAAAAFLEALEGGFRDEGDIEEHLGHRSLATVPLLDTQ
MDKKAQLTHAHFGSVKRHDEAVDDTMPFQLLARIVPDAPRSTFAEAFRNAKLACDFALADAENNLIAIAG
ALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKPGLLDLLAGEASIEAGIHRDQRPG
LAFIAAGGASHFPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAAFAALADGILFVTEFER
SPLGEIRDLIHQEPHANSDVLGVIFNALDMNELGKYGDFDGAEKYRHRQGGYTSENKIPEAEAA
>gnl|CDD|130079 TIGR01006, Capsular_polysaccharide_biosynthesis_protein_CapA, polysaccharide export protein, MPA1 family, Gram-positive type. This family contains members from Low GC Gram-positive bacteria; they are proposed to have a function in the export of complex polysaccharides [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MKQENTEIDLLQLLKKLWKRKLLILIVALIFLIISFIYTFFIISPEYTSTTRIYVVNRNQDNKGLTAQDL
QAGIQLVNDYKEIILSPDILDKVSKDLKLDLSPKELSSMVTVTNPTDTRLISISVKDKTPQDASKIANSL
REVASKKIPKITNVSDVTTLEEAKPATTPSSPNPKRNLLIGFLLGLVVALIIVLLKELLDTRVKRPEDVE
DVLGMTLLGIVPDFDK
>gnl|CDD|273392 TIGR01007, Tyrosine-protein_kinase_CpsD, capsular exopolysaccharide family. This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
EYYNAIRTNIQFSGAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNK
ITGLTNFLSGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGT
VTDAAIIARACDASILVTDAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYGYYGYYG
>gnl|CDD|273393 TIGR01008, 30S_ribosomal_protein_S3, ribosomal protein uS3, eukaryotic/archaeal type. This model describes ribosomal protein S3 of the eukaryotic cytosol and of the archaea. TIGRFAMs model TIGR01009 describes the bacterial/organellar type, although the organellar types have a different architecture with long insertions and may score poorly [Protein synthesis, Ribosomal proteins: synthesis and modification]
IERKFVAEGVKRTLIDEFLEKELREAGYSGVDVRVTPLGTKVIIFAERPGLVIGRGGRRIRELTEKLQKK
FGLENPQIYVEEVENPELNAKVQAERIARALERGLHFRRAAYAAVRRIMEAGAKGVEVTISGKLTGERAK
TEKFAAGYLKHSGEPAEELVDKGFAIALLKLGVLGVKVKIMPPDAKLPDEVEIKE
>gnl|CDD|130082 TIGR01009, 30S_ribosomal_protein_S3, ribosomal protein S3, bacterial type. This model describes the bacterial type of ribosomal protein S3. Chloroplast and mitochondrial forms have large, variable inserts between conserved N-terminal and C-terminal domains. This model recognizes all bacterial forms and many chloroplast forms above the trusted cutoff score. TIGRFAMs model TIGR01008 describes S3 of the eukaryotic cytosol and of the archaea [Protein synthesis, Ribosomal proteins: synthesis and modification]
MGQKVNPIGFRLGITKDWKSRWYANPKEYAKLLHEDLKIRNYIKKELSNAGISDVEIERPADKIRVTIHT
ARPGIVIGKKGSEIEKLRKDLQKLTGKEVQINIAEVKRPELDAQLVADNIARQLENRVSFRRAMKKAIQS
AMKAGAKGIKVQVSGRLGGAEIARTEWYKEGRVPLHTLRADIDYATAEAHTTYGIIGVKVWIFKGEVLGG
G
>gnl|CDD|130083 TIGR01010, BexC_CtrB_KpsE, polysaccharide export inner-membrane protein, BexC/CtrB/KpsE family. This family contains gamma proteobacterial proteins involved in capsule polysaccharide export [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
KKLKPLFFLTVIIPTAISLLYFGIFASDRYVSESSFVVRSPDSQSSLSGVGALLQGSGFSRSQDDTYTVQ
EYMRSRDMLAALEKELPFREFFSQKGDLLSRFNRLHKNGTQEAFYRYYKKRLSVDVDSVSGILTLNVTAF
DAEEAQKINQRLLKEGERLINRLNERARKDTIAFAENEVKEAEQRLNATKAELLKYQIKNKVFDPKAQSS
AQLSLISTLEGELIRVQAQLAQLRSITPEQNPQVPSLQARIKSLRKQIDEQRNQLSGGLGDSLNEQTADY
QRLVLQNELAQQQLKAALTSLQQTRVEADRQQLYLEVISQPSLPDDALEPYRLYNILATFVILLILYGVL
SLLLASIREHKN
>gnl|CDD|130084 TIGR01011, 30S_ribosomal_protein_S2, ribosomal protein S2, bacterial type. This model describes the bacterial, ribosomal, and chloroplast forms of ribosomal protein S2. TIGR01012 describes the archaeal and cytosolic forms [Protein synthesis, Ribosomal proteins: synthesis and modification]
VVSMKDLLEAGVHFGHQTRRWNPKMKPFIFGERNGIHIIDLQKTLQLLKEAYNFVKDVAANGGKILFVGT
KKQAKEIIKEEAERCGMFYVNQRWLGGMLTNFKTIRKSIKKLKKLEKMEEDGTFDDLTKKEALMLSREKE
KLEKSLGGIKDMKKLPDLLFVIDPVKEKIAVAEARKLGIPVVAIVDTNCDPDLVDYPIPGNDDAIRSIRL
LTNLIADAVLEGKQE
>gnl|CDD|273394 TIGR01012, 30S_ribosomal_protein_S2, ribosomal protein uS2, eukaryotic/archaeal form. This model describes the ribosomal protein of the cytosol and of Archaea, homologous to S2 of bacteria. It is designated typically as Sa in eukaryotes and Sa or S2 in the archaea. TIGR01011 describes the related protein of organelles and bacteria [Protein synthesis, Ribosomal proteins: synthesis and modification]
EYLVPVDMYLAAGVHIGTQNKTFDMEKFIYKVRQDGLYVLDLRKTDERLRVAAKFLVAIEPQDILVVSAR
IYGQKPVLKFAKVTGARAIAGRFTPGTFTNPAQKSFREPRVLIVTDPRADHQAVKEASEVGIPIVALCDT
DNPLRYVDLVIPTNNKGRRSLALIYWLLAREILRMRGTISPDEDWDVMVEEFFYRD
>gnl|CDD|162157 TIGR01013, Sodium-dependent_phosphate_transport_protein, Phosphate:Na+ Symporter (PNaS) Family [Transport and binding proteins, Cations and iron carrying compounds]
LVLLFVFVCSLAVLSAAFILLGAKVGGAIFADILITDNPWASPLLGFLGTVLLQSSSTSRSIVVGMVSAG
LLLVLLAIPLIMGANIGSSVTNAIVAIMQSGDRAWFRRAFIGATVADIFNSSLALVLLPLELTTGGIESV
TLLVVLVFGANGGGDAPDLLNSLTAPATALIVQLDNLIIRLIGSLLILPLIDILASTLSSLPVPESNLPI
EAHIFVNVGLILLALPFVRLCARLILVVIPLNSLLDGQVAPVILDVINLDTPVPFLWVTGYEALLVGDAM
TFIIQSSSVFTSALTPLVGKGVISLERAYPLVLGSNIGTTLTAVLAALLSEDEKRRSALQIAYCHNLFNI
SGIVLFYPLPCTRKPIAAARGFGDDGSKYRWFLIVYLVLNFLLAPSLLFGLDLNLARRLVGVKIPFRILE
LFSSLLHVLQLRCPRPQSLQTWSFLPDWLRSLKRLD
>gnl|CDD|273395 TIGR01015, Homogentisate_12-dioxygenase, homogentisate 1,2-dioxygenase. Missing in human disease alkaptonuria [Energy metabolism, Amino acids and amines]
ELKYLSGFGNEFESERVPGALPVGQNSPQKCPYGLYAEQLSGSAFTAPRHENKRSWLYRIRPSAAHEPFE
PRDGNPGHVTANFDEQAPDPNQLRWSPFPIPSDEAVDFVDGLHTLCGAGDATSRTGLAIHIYLCNASMEN
RAFYNADGDFLIVPQQGALLITTEFGRLLVEPNEICVIPRGVRFRVTVLEPARGYICEVYGAHFQLPDLG
PIGANGLANPRDFEAPVAAFEDREVPGPYTVINKFQGSLFAAKQDHSPFDVVAWHGNYVPYKYDLKRFNV
INSVSFDHPDPSIFTVLTAPSDRPGTAIADFVIFPPRWLVAEKTFRPPYYHRNCMSEFMGLITGAYDAKE
GGFVPGGGSLHNMMTPHGPDFDCFEKASNAKLKPERIADGTMAFMFESSLSLAVTKWGATCQKLQEDYYK
CWQPLKRHF
>gnl|CDD|273396 TIGR01016, Succinyl-CoA_ligase_subunit_beta, succinyl-CoA synthetase, beta subunit. This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases model (pfam00549). The C-terminal half is described by the ATP-grasp model (pfam02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G [Energy metabolism, TCA cycle]
MNLHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAGPVVVKAQVHAGGRGKAGGVKVAKSKEEAR
AAAEKLLGKELVTNQTDPLGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKS
PEKIIKYAIDPLTGLLPYQAREIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLI
ALDAKLTIDDNALFRHPDLEEMRDYSQEDPREVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYG
GEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFGGITRCDLVAKGLVEALKEVGVNVPVVVRLE
GTNVEEGKKILAESGLNIIFATSMEEAAEKAVEAAE
>gnl|CDD|200066 TIGR01017, 30S_ribosomal_protein_S4, ribosomal protein S4, bacterial/organelle type. This model finds organelle (chloroplast and mitochondrial) ribosomal protein S4 as well as bacterial ribosomal protein S4 [Protein synthesis, Ribosomal proteins: synthesis and modification]
RYTGPKFKLSRRLGVNLFGKSRKLLLKRKYPPGQHGQRRKKLSDYGLQLQEKQKLKFMYGITEKQFRKYF
KEAKKLKGNTGENLLRLLESRLDNVVYRLGFAPTRFAARQLVSHGHILVNGKKVDIPSYQVRPGDIISIK
EKSKKIPLVKENLETNGQRNIPSWLEVDKKTLEGKVLRVPERSQLPLPINESLVVEYYSR
>gnl|CDD|273397 TIGR01018, 30S_ribosomal_protein_S4, ribosomal protein uS4, eukaryotic/archaeal type. This model finds eukaryotic ribosomal protein S9 as well as archaeal ribosomal protein S4 [Protein synthesis, Ribosomal proteins: synthesis and modification]
MGDPRRQRKKYETPRHPWIKERLDRELKLMGKYGLRNKKEVWKAETTLRKYRRAARELLTLDDEQRLFEG
NQLLRRLVRLGILDEENAKLDDVLGLTVEDFLERRLQTQVYKKGLARTIHQARQLIVHGHIAVNGRVVTS
PSYIVRLEEEKKIDFALSSPFG
>gnl|CDD|130091 TIGR01019, Succinyl-CoA_ligase_subunit_alpha, succinyl-CoA synthetase, alpha subunit. This model describes succinyl-CoA synthetase alpha subunits but does not discriminate between GTP-specific and ATP-specific reactions. The model is designated as subfamily rather than equivalog for that reason. ATP citrate lyases appear to form an outgroup [Energy metabolism, TCA cycle]
ILLDKDTKVIVQGITGSQGSFHTEQMLAYGTNIVGGVTPGKGGTTVLGLPVFDSVKEAVEETGANASVIF
VPAPFAADAIFEAIDAGIELIVCITEGIPVHDMLKVKRYMEESGTRLIGPNCPGIITPGECKIGIMPGHI
HKPGNVGIVSRSGTLTYEAVHQLTKAGFGQSTCVGIGGDPVNGTSFIDVLEAFEKDPETEAIVMIGEIGG
SAEEEAADFIKQNMSKPVVGFIAGATAPPGKRMGHAGAIISGGKGTAESKIEALEAAGVTVVKSPSDIGE
LLAEIL
>gnl|CDD|273398 TIGR01020, 30S_ribosomal_protein_S5, ribosomal protein uS5, eukaryotic/archaeal form. This model finds eukaryotic ribosomal protein uS5 (previously S2 in yeast and human) as well as archaeal ribosomal protein uS5 [Protein synthesis, Ribosomal proteins: synthesis and modification]
AKAELEEWEPKTKLGRLVKEGKIKSIDEIFLRNLPIKEPEIIDALLPDLNEEEVLDISLVQRMTDSGRRT
RFRAFVAVGNRDGYVGLGIGKAKEVAPAIRKAIINAKLNIIPVRRGCGSWECGCGRPHSVPFKVTGKCGS
VRVRLIPAPRGTGLVAGDVAKKVLRLAGIDDVWTQTRGETRTTVNFAKATFDALKKTYYVTPSLWAEERL
GI
>gnl|CDD|130093 TIGR01021, 30S_ribosomal_protein_S5, ribosomal protein S5, bacterial/organelle type. This model finds chloroplast ribosomal protein S5 as well as bacterial ribosomal protein S5. A candidate mitochondrial form (Saccharomyces cerevisiae YBR251W and its homolog) differs substantially and is not included in this model [Protein synthesis, Ribosomal proteins: synthesis and modification]
ELEERLIAVNRVSKVVKGGRRFSFSALVVVGDGKGRVGFGFGKAKEVPDAIKKAVEAARKNLINVPLTKG
TIPHEVIGRSGAAKVLLKPASPGTGVIAGGAVRAILELAGVKDILAKSLGSNNPINVVRATFDALLKLKS
PEDVAELRGKPVEE
>gnl|CDD|130094 TIGR01022, 50S_ribosomal_protein_L36, ribosomal protein L36, bacterial type. Proteins found by this model occur exclusively in bacteria and organelles [Protein synthesis, Ribosomal proteins: synthesis and modification]
MKVRASVKKICEKCKIIKRKGVVRVICKNPKHKQRQG
>gnl|CDD|273399 TIGR01023, 50S_ribosomal_protein_L33, ribosomal protein L33, bacterial type. This model describes bacterial ribosomal protein L33 and its chloroplast and mitochondrial equivalents [Protein synthesis, Ribosomal proteins: synthesis and modification]
MAKKGARELIRLVCTACTGINYTTTKNRRNKPEKLELRKYCPVCRKHVLHKEAK
>gnl|CDD|130096 TIGR01024, 50S_ribosomal_protein_L19, ribosomal protein L19, bacterial type. This model describes bacterial ribosomoal protein L19 and its chloroplast equivalent. Putative mitochondrial L19 are found in several species (but not Saccharomyces cerevisiae) and score between trusted and noise cutoffs [Protein synthesis, Ribosomal proteins: synthesis and modification]
QNLIKQIEQEQLKKDLPDFRVGDTVRVHVKIVEGKKERIQVFEGVVIARRGGGIGETFTVRKISYGVGVE
RIFPLHSPRIDSIEVVRRGKVRRAKLYYLRERRGKAARIKERR
>gnl|CDD|273400 TIGR01025, 30S_ribosomal_protein_S19, ribosomal protein uS19, eukaryotic/archaeal form. This model represents eukaryotic ribosomal protein uS19 (previously S15) and its archaeal equivalent. It excludes bacterial and organellar ribosomal protein S19. The nomenclature for the archaeal members is unresolved and given variously as S19 (after the more distant bacterial homologs) or S15 [Protein synthesis, Ribosomal proteins: synthesis and modification]
TFKEFRYRGYTLEELQDMSLEELAKLLPARQRRRLKRGLTPKQKKLLKKLRKAKKEAPPGEKPEVIRTHC
RDMIILPEMVGSTVGVYNGKEFVQVEIKPEMIGHYLGEFSITRKPVKHGRPGVGATRSSMFVPLK
>gnl|CDD|273401 TIGR01026, Flagellum-specific_ATP_synthase, ATPase, FliI/YscN family. This family of ATPases demonstrates extensive homology with ATP synthase F1, beta subunit. It is a mixture of members with two different protein functions. The first group is exemplified by Salmonella typhimurium FliI protein. It is needed for flagellar assembly, its ATPase activity is required for flagellation, and it may be involved in a specialized protein export pathway that proceeds without signal peptide cleavage. The second group of proteins function in the export of virulence proteins; exemplified by Yersinia sp. YscN protein an ATPase involved in the type III secretory pathway for the antihost Yops proteins [Energy metabolism, ATP-proton motive force interconversion]
MERNLTTFYNRLCQEMDLRLVKRVGRVTKVKGLLIEAVGPQASVGDLCLIERRGSEGRLVAEVVGFNGEF
VFLMPYEEVEGVRPGSKVLATGEGLSIKVGDGLLGRVLDGLGKPIDGKGKFLDNVETEGLITAPINPLKR
APIREILSTGVRSIDGLLTVGKGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEH
DLGEEGLKRSVVVVATSDQSPLLRLKGAYVATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPP
ATKGYTPSVFSTLPRLLERAGASGKGSITAFYTVLVEGDDMNEPIADSVRGILDGHIVLSRALAQRGHYP
AIDVLASISRLMTAIVSEEHRRAARKFRELLSKYKDNEDLIRIGAYQRGSDRELDFAIAKYPKLERFLKQ
GINEKVNFEESLQQLEEIFR
>gnl|CDD|162163 TIGR01027, Glutamate_5-kinase, glutamate 5-kinase. Bacterial ProB proteins hit the full length of this model, but the ProB-like domain of delta 1-pyrroline-5-carboxylate synthetase does not hit the C-terminal 100 residues of this model. The noise cutoff is set low enough to hit delta 1-pyrroline-5-carboxylate synthetase and other partial matches to this family [Amino acid biosynthesis, Glutamate family]
QRIVVKVGSSSLTGSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALGLPERPKTLAEKQA
LAAVGQVRLMQLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEI
KFGDNDTLSALVAILVGADLLVLLTDVDGLYDADPRTNPDAKLIPVVEEITDLLLGVAGDSGSSVGTGGM
RTKLQAADLATRAGVPVIIASGSKPEKIADALEGAPVGTLFHAQARRLRNRKFWIAFASEPAGEITVDAG
AEEALLERGKSLLPAGIVGVEGNFSRGEVVEILNPEGQDIGRGLVNYSSDELEKIKGHKSSEIEAVLGYE
YGDEVVHRDDMVL
>gnl|CDD|273402 TIGR01028, 30S_ribosomal_protein_S7, ribosomal protein uS7, eukaryotic/archaeal. This model describes the members from the eukaryotic cytosol and the Archaea of the family that includes ribosomal protein uS7 (previously S5 in yeast and human). A separate model describes bacterial and organellar S7 [Protein synthesis, Ribosomal proteins: synthesis and modification]
EIKVFGKWSTEEVEVKDPSLKDYINLEPIYVPHTAGRHAKKQFRKAKVPIVERLINKVMRSGRNNGKKLK
AYRIVKEAFEIIEKRTKKNPIQVLVDAIENAGPREDTTRVGYGGIAYRQAVDISPLRRVDQALRNIALGA
REAAFRNKKSIAECLAEEIILAANGDSKSYAIKKKEELERVAKSAR
>gnl|CDD|273403 TIGR01029, 30S_ribosomal_protein_S7, ribosomal protein S7, bacterial/organelle. This model describes the bacterial and organellar branch of the ribosomal protein S7 family (includes prokaroytic S7 and eukaryotic S5). The eukaryotic and archaeal branch is described by model TIGR01028 [Protein synthesis, Ribosomal proteins: synthesis and modification]
RKRKAEKRKIPPDPVYGSVLLNKFINRVMKDGKKSLAESIVYKAFERIAKKTGEDPLEVFEQALENVKPL
VEVKSRRVGGATYQVPVEVRPSRRYALAIRWLIEAARKRGGKSMAERLANEILDAANNTGAAIKKREDTH
RMAEANKAFAHYRW
>gnl|CDD|130102 TIGR01030, 50S_ribosomal_protein_L34, ribosomal protein L34, bacterial type. This model describes the bacterial protein L34 and its equivalents in organelles [Protein synthesis, Ribosomal proteins: synthesis and modification]
MKRTYQPSNLKRKRTHGFRARMATKNGRKVLRRRRAKGRHKLTV
>gnl|CDD|273404 TIGR01031, 50S_ribosomal_protein_L32, ribosomal protein L32. This protein describes bacterial ribosomal protein L32. The noise cutoff is set low enough to include the equivalent protein from mitochondria and chloroplasts. No related proteins from the Archaea nor from the eukaryotic cytosol are detected by this model. This model is a fragment model; the putative L32 of some species shows similarity only toward the N-terminus [Protein synthesis, Ribosomal proteins: synthesis and modification]
VPKRKTSKSRKRKRRSHDAKLTAPTLVVCPNCGEFKLPHRVCPSCGYYKGRQVLE
>gnl|CDD|130104 TIGR01032, 50S_ribosomal_protein_L20, ribosomal protein L20. This model describes bacterial ribosomal protein L20 and its chloroplast equvalent. This protein binds directly to 23s ribosomal RNA and is necessary for the in vitro assembly process of the 50s ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. GO process changed accordingly (SS 5/09/03) [Protein synthesis, Ribosomal proteins: synthesis and modification]
MRVKRGVVARRRRKKILKQAKGFRGTRKRHYRVAKQTVIKAMAYAYRDRRQRKRDFRSLWITRINAAARQ
HGLSYSRFINGLKKANIEINRKVLSELAINDPEAFKEIVEKAK
>gnl|CDD|273405 TIGR01033, Probable_transcriptional_regulatory_protein, DNA-binding regulatory protein, YebC/PmpR family. This model describes a minimally characterized protein family, restricted to bacteria excepting for some eukaryotic sequences that have possible transit peptides. YebC from E. coli is crystallized, and PA0964 from Pseudomonas aeruginosa has been shown to be a sequence-specific DNA-binding regulatory protein. In silico analysis suggests a role in Holliday junction resolution [Regulatory functions, DNA interactions]
MAGHSKWANIKHRKAAQDAKRGKIFTKLIKEIIVAAKLGGGDPESNPRLRTAIEKAKAANMPKDNIERAI
KKGAGELDGSNYEEITYEGYAPGGVAIIVECLTDNKNRTASEVRSAFNKNGGSLGEPGSVSYLFSRKGVI
EVPKNEVDEEDLMEAAIEAGAEDIDVDDDEFEVYTAPEELEKVKEALEAKGFPIESAEITMIPLTTVDLD
DEQAEKLLKLIDALEDDDDVQEVYHNFE
>gnl|CDD|273406 TIGR01034, S-adenosylmethionine_synthase, S-adenosylmethionine synthetase. Tandem isozymes of this S-adenosylmethionine synthetase in E. coli are designated MetK and MetX [Central intermediary metabolism, Other]
LFTSESVSEGHPDKIADQISDAVLDAILKQDPKSKVACETFVKTGLVLIGGEITTSAYVDIQEVARNTIK
DIGYTDSDYGFDAKTCAVLDAIGNQSPDIAQGVDKANPEEQGAGDQGIMFGYATNETPELMPLPITLAHK
LLKRAAELRKSGTLPWLRPDGKSQVTIQYEDNKPVRVDTVVLSTQHDPDISQKDLREAIIEEIIKPVLPA
EFLDEKTKFFINPTGRFVIGGPMGDTGLTGRKIIVDTYGGWARHGGGAFSGKDPSKVDRSAAYAARYIAK
NIVAAGLADRCEVQLSYAIGVAEPVSIMVETFGTSKKSSEELLNVVKENFDLRPGGIIEKLDLLKPIYRK
TAAYGHFGREEFPWEKPDKLEELKRAL
>gnl|CDD|273407 TIGR01035, Glutamyl-tRNA_reductase, glutamyl-tRNA reductase. This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase (TIGR00713), leads to the production of delta-amino-levulinic acid from Glu-tRNA [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
ILVLGVSHKSAPVEVREKLSIDEIKLKKALDTLKAEPSIEEAMVLSTCNRVEIYAVVDNLHEGKSALLQI
LAENKNMSNEDLEKYLYILTGESAVEHLFRVASGLDSMVVGETQILGQVKNAYKVAQEEKTVGKVLERLF
QKAFSVGKRVRTETDISAGAVSISSAAVELAERIFGSLKGKKALLIGAGEMGELVAKHLLRKGVGKILIA
NRTYERAEDLAKELGGEAVKFEDLEEYLAEADIVISSTGAPHPIVSKEDVERALRERTRPLFIIDIAVPR
DVDPAVARLEGVFLYDVDDLQPVVEENLAERREEAEKAEEIVEEETAEFKQWLRSLEVEPTIKALRSLAE
IVREKELEKALKKLPGLSKDVEEVLEDLARKLINKLLHAPTVRLKQLADKEESEVCLEALKNLFGLE
>gnl|CDD|273408 TIGR01036, Dihydroorotate_dehydrogenase_quinone, dihydroorotate dehydrogenase, subfamily 2. This model describes enzyme protein dihydroorotate dehydrogenase exclusively for subfamily 2. It includes members from bacteria, yeast, plants etc. The subfamilies 1 and 2 share extensive homology, particularly toward the C-terminus. This subfamily has a longer N-terminal region [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
YPLVRKLLFLLDPESAHELTFQFLRLGTGTPFLALLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGE
AIDALGAMGFGFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGIN
IGKNKDTPSEDAKEDYAACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHR
VPVLVKIAPDLTESDLEDIADSLVELGIDGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRR
LYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYSGFIYWGPPLVKEIVKEI
>gnl|CDD|130109 TIGR01037, Putative_dihydroorotate_dehydrogenase, dihydroorotate dehydrogenase (subfamily 1) family protein. This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase
LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGL
QNPGVEAFLEELKPVREEFPTPLIASVYGSSVEEFAEVAEKLEKAPPYVDAYELNLSCPHVKGGGIAIGQ
DPELSADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINTLRGMKIDIKTGKPILANKT
GGLSGPAIKPIALRMVYDVYKMVDIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGFAFKKIIEGL
IAFLKAEGFTSIEELIGIAH
>gnl|CDD|273409 TIGR01038, 50S_ribosomal_protein_L22, ribosomal protein uL22, eukaryotic/archaeal form. This model describes the ribosomal protein uL22 of the eukaryotic cytosol and of the Archaea, previously designated as L17, L22, and L23. The corresponding bacterial form of uL22 is described by a separate model [Protein synthesis, Ribosomal proteins: synthesis and modification]
YSYKPEDPTKSAKARGRNLRISFKNARETCRAIRGMELDKARKYLEDVIAMKRAVPFRRYNGKVGHRAGL
WGWTAGRYPVKAAKFILKVLQNAEANAEYKGLDVEKLKIIHIQANKGPVIRRWMPRAFGRATPYNSSTTH
IELVVEEK
>gnl|CDD|211621 TIGR01039, ATP_synthase_subunit_beta, ATP synthase, F1 beta subunit. The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit [Energy metabolism, ATP-proton motive force interconversion]
TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVI
DTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPY
AKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQM
NEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGEL
QERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSV
VGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQRFLSQPFFVAEVFTGQPGKYV
PLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL
>gnl|CDD|273410 TIGR01040, V-type_proton_ATPase_subunit_B, V-type (H+)-ATPase V1, B subunit. This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase [Transport and binding proteins, Cations and iron carrying compounds]
EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFT
GDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIAR
GQKIPIFSAAGLPHNEIAAQICRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSM
ERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFP
GYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINV
LPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFIA
QGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSAD
>gnl|CDD|200071 TIGR01041, V-type_ATP_synthase_beta_chain, ATP synthase archaeal, B subunit. Archaeal ATP synthase shares extensive sequence similarity with eukaryotic and prokaryotic V-type (H+)-ATPases [Energy metabolism, ATP-proton motive force interconversion]
EYSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFT
GETLKLPVSEDMLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVR
GQKLPIFSGSGLPHNELAAQIARQATVRGEESEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNL
ADDPAVERIVTPRMALTAAEYLAFEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLAT
IYERAGRVKGKKGSITQMPILTMPGDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMK
DGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALSERDRKYLKFADLFERKFVRQGFNENRSI
EETLDIGWELLSILPESELKRIDEEYIEKYHPKYRKKK
>gnl|CDD|273411 TIGR01042, V-type_proton_ATPase_catalytic_subunit_A, V-type (H+)-ATPase V1, A subunit. This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase [Transport and binding proteins, Cations and iron carrying compounds]
EYGYIYKVSGPVVVAENMAGAAMYELVRVGHDELVGEIIRLEGDKATIQVYEETSGLTVGDPVLRTGKPL
SVELGPGILGNIFDGIQRPLKAIAEQSQSIYIPRGVNVPALDRDKKWEFTPKKLRVGDHITGGDIYGTVF
ENSLIKHKIMLPPRARGTITYIAPAGNYTVDDTVLEVEFQGVKKKFSMLQTWPVRSPRPVTEKLPANTPL
LTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIVYVGCGERGNEMAEVLMDFPELTME
VDGREESIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAE
MPADSGYPAYLGARLASFYERAGRVKCLGSPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDK
KLAQRKHFPSVNWLISYSKYMRALEEFYEKFYPEFVPLRTKAKEILQEEEDLNEIVQLVGKDALAETDKI
TLEVAKLIKEDFLQQNGYTPYDRFCPFYKTVGMMRNMIAFYDLARQAVERTAQDDNKITWSIIKESLGDL
LYRLSSMKFEDPSDGEAKIKADYEKLNEDMQ
>gnl|CDD|130115 TIGR01043, V-type_ATP_synthase_alpha_chain, ATP synthase archaeal, A subunit. Archaeal ATP synthase shares extensive sequence similarity with eukaryotic and prokaryotic V-type (H+)-ATPases [Energy metabolism, ATP-proton motive force interconversion]
KGRIIRVSGPLVVADGMKGAQMYEVVKVGEEGLIGEIIRIEGDKAFIQVYEETSGIKPGEPVVGTGAPLS
VELGPGLLGSIYDGVQRPLDVLKEKTGDFIARGVDAPGLDRDKKWHFKPTVKEGDKVEGGDIIGVVPETS
LIEHKILVPPNVEGEIVEIAEEGDYTVEDTIAVVDTDGDEEIKMYQKWPVRIPRPYKEKLPPEVPLITGQ
RILDTFFPIAKGGTAAIPGPFGSGKTVTQHQLAKWSDADIVVYIGCGERGNEMTDVLEEFPELKDPKTGK
PLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEAMREISGRLEEMPGEEG
YPAYLASRLAEFYERAGRVKTLGGEERVGSVTVIGAVSPPGGDFSEPVTQNTLRIVKVFWALDADLAQRR
HFPAINWLQSYSLYVDLVQDWWHENVDPDWREMRDEAMDLLQKESELQEIVQLVGPDALPERQKLILEVA
RMIREAFLQQNAFDPVDTYCPPQKQYRILRAIMNFYDEAMEALERGVPVEEILKLEVKEEIGRMKYEPDN
DILAKIDEILEKIEKEFK
>gnl|CDD|130116 TIGR01044, 50S_ribosomal_protein_L22, ribosomal protein L22, bacterial type. This model decribes bacterial and chloroplast ribosomal protein L22 [Protein synthesis, Ribosomal proteins: synthesis and modification]
AKARFVRISPRKARLVADLIRGKQVGEALDILRFTPKKASPIIEKVLASAIANAEHNYGLDANNLVVVTA
FVDEGPTLKRIRPRAKGRASRIRKRTSHITVVV
>gnl|CDD|273412 TIGR01045, Uncharacterized_protein_RP474, Rickettsial palindromic element RPE1 domain. This model describes protein translations of the first family described, RPE1, of Rickettsia palindromic elements (RPE). In Rickettsia conorii, 19 copies are found within protein coding regions, where they encode an insert relative to homologs from other species but do not disrupt the reading frame. Insertion is always in the same reading frame. This model finds RPE-encoded regions in several Rickettsial species and, so far, no where else
RHLSKLAYREEFKGNTERSTTAYINVREDASTGSTYKLPLEAEFGK
>gnl|CDD|273413 TIGR01046, 30S_ribosomal_protein_S10, ribosomal protein uS10, eukaryotic/archaeal. This model describes the archaeal ribosomal protein uS10 and its equivalents (previously called S20) in eukaryotes [Protein synthesis, Ribosomal proteins: synthesis and modification]
HKARIKLTSTNVRSLEEVCRQIKNIAEKTGVRMSGPVPLPTKRLRVPTRKSPDGEGSKTWDRWEMRIHKR
LIDIEADERALRQIMRIRVPEDVEIEIEL
>gnl|CDD|273414 TIGR01047, carboxynorspermidine_decarboxylase, carboxynorspermidine decarboxylase. This protein is related to diaminopimelate decarboxylase. It is the last enzyme in norspermidine biosynthesis by an unusual pathway shown in Vibrio alginolyticus [Central intermediary metabolism, Polyamine biosynthesis]
IPTPAFVLEEEKLRKNLEILESVQQQSGAKVLLALKGFAFWGAFPILREYLKGCTASGLWEAKLAKEEFG
KEIHVYSPAYKEDDIPEIIPLADHIVFNSLAQWHRYRHKVQGKNSAVKLGLRINPEYSEVPTDLYNPCGR
FSRLGVQAKDFEEVLLDGIEGLHFHTLCEKDADALERTLEVIEEKFGEYLPQMKWVNFGGGHHITKKGYD
VEKLIAVIKAFSERHGVQVILEPGEAIGWQTGFLVASVVDIVENEKQIAILDVSFEAHMPDTLEMPYRPE
VLGARDPATRENEAQDKEGEFSYLLGGNTCLAGDVMGEYAFDKPLKVGDKIVFLDMIHYTMVKNTTFNGV
KLPSLGCLRAKGEFQMIRTFGYEDYKNRL
>gnl|CDD|273415 TIGR01048, Diaminopimelate_decarboxylase, diaminopimelate decarboxylase. This family consists of diaminopimelate decarboxylase, an enzyme which catalyzes the conversion of diaminopimelic acid into lysine during the last step of lysine biosynthesis [Amino acid biosynthesis, Aspartate family]
TVENEDGELFIEGVPLLELAQEFGTPLYVYDEDTIRRRFRAYKEAFGGRSLVCYAVKANSNLAVLRLLAE
LGSGFDVVSGGELYRALAAGFPPEKIVFSGNGKSRAELERALELGICINVDSFSELERLNEIAPELGKKA
RISLRVNPGVDAKTHPYISTGLKDSKFGIDVEEALEAYLYALQLPHLELVGIHCHIGSQITDLSPFVEAA
EKVVKLAESLAEGIDLEFLDLGGGLGIPYTPEEEPPDLSEYAQAILNALEGYADLGLDPKLILEPGRSIV
ANAGVLLTRVGFVKETGSRNFVIVDAGMNDLIRPALYGAYHHIIVLNRTNDAPTEVADVVGPVCESGDVL
AKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLVDGGQARLIRRRETYEDLWALEV
>gnl|CDD|130121 TIGR01049, 30S_ribosomal_protein_S10, ribosomal protein S10, bacterial/organelle. This model describes bacterial 30S ribosomal protein S10. In species that have a transcription antitermination complex, or N utilization substance, with NusA, NusB, NusG, and NusE, this ribosomal protein is responsible for NusE activity. Included in the family are one member each from Saccharomyces cerevisiae and Schizosaccharomyces pombe. These proteins lack an N-terminal mitochondrial transit peptide but contain additional sequence C-terminal to the ribosomal S10 protein region [Protein synthesis, Ribosomal proteins: synthesis and modification]
QKIRIKLKSYDHRLLDQSTKKIVETAKRTGAQVKGPIPLPTKKERYTVLRSPHVNKDSREQFEIRTHKRL
IDIIDPNPKTIDALMKLDLPAGVDIEIKL
>gnl|CDD|130122 TIGR01050, 30S_ribosomal_protein_S19, ribosomal protein S19, bacterial/organelle. The homologous protein of the eukaryotic cytosol and of the Archaea may be designated S15 or S19 [Protein synthesis, Ribosomal proteins: synthesis and modification]
MSRSLKKGPFVDHHLLKKVEKLNESGKKKVIKTWSRRSTIIPEMIGHTIAVHNGKKFIPVYITEDMVGHK
LGEFAPTRTFKGHAKSDKKSKR
>gnl|CDD|273416 TIGR01051, DNA_topoisomerase_1, DNA topoisomerase I, bacterial. This model describes DNA topoisomerase I among the members of bacteria. DNA topoisomerase I transiently cleaves one DNA strand and thus relaxes negatively supercoiled DNA during replication, transcription and recombination events [DNA metabolism, DNA replication, recombination, and repair]
LVIVESPAKAKTIKKYLGDEYEVEASMGHIRDLPKSRLGVDIEKDFEPEYVVSKGKKKVVKELKTLAKKA
DEVYLATDPDREGEAIAWHLAEVLKPKDPVYKRIVFNEITKKAIRAALKNPREIDMNLVNAQQARRILDR
LVGYTLSPLLWKKVAKGLSAGRVQSVALRLIVDREREIKRFVPEEYWTIDATFQKGEETFEALLTEVNGK
KLKAGSDLDEAEATALKEQLKGEELVVEEIEKKPKKSRPPPPFTTSTLQQEASRKLGFSAKKTMMIAQRL
YEGVSTGDGTIGLITYMRTDSTRLSNQAVNEARNLIDKNYGKEYLGPKPKRYKSKEKNAQEAHEAIRPTS
VFRTPEELKDYLKRDEFRLYELIWKRFVASQMADARYDSTSVRLTNEDGEYVFKATGRKLIFDGYYKVYV
EGSDDPLEEKDRILPPLKEGDAVKLVEVKPNQHFTQPPARYTEASLVKELEELGIGRPSTYASIISTIQD
RGYVKKENKRLYPTELGFAVTDLLEKHFGDVVDYDFTAKMEKDLDEIAEGKAEWKPVLKNFYTGFSSKVK
KLRNMRIIVDFKTSQDCPLCGRPMVVKLGKYGPFLACSNFPECKYTKSIV
>gnl|CDD|273417 TIGR01052, Type_2_DNA_topoisomerase_6_subunit_B, DNA topoisomerase VI, B subunit. This model describes DNA topoisomerase VI, an archaeal type II DNA topoisomerase (DNA gyrase) [DNA metabolism, DNA replication, recombination, and repair]
KEKFREMSVAEFFRKNKHMLGYSGKIRSLTTVIHELVTNSLDACEEAGILPDIKVEIEKIGKDHYKVTVE
DNGPGIPEEYIPKVFGKMLAGSKFHRIIQSRGQQGIGISGAVLYSQMTTGKPVKVISSTGGEIYVYKMKL
KIDVQKNEGEIVEKGEWNKPGWRGTRIELEFKGVSYRRSKQGVYEYLRRTAVANPHAKIVLVDPDGEIYV
FPRSTDEIPKPPKEMKPHPHGVTIDDLKSMARSTRASTLRSFLVSEFSRIGEKKIKELLEKYGIDVDPLD
KKPKELTWDEAEKIVNAFKEMKFMAPPTDGLSPIGEENIEKGLKEILQPEFVGAVTRSPKTYRGGIPFIV
EVGIAYGGNIGRRSEPEILRYANKVPLLYDAGSCVLTKAVKSINWKRYGIRDFPSAPLVVLVNLASTNVP
YTSTGKQSVADIPEIYNEIRLALMEVARRLRLYLSRKAREEEEIKRRKTLEKYLPEIAKSLAYILEKP
>gnl|CDD|130125 TIGR01053, zinc-finger_protein_Lsd1, zinc finger domain, LSD1 subclass. This model describes a putative zinc finger domain found in three closely spaced copies in Arabidopsis protein LSD1 and in two copies in other proteins from the same species. The motif resembles CxxCRxxLMYxxGASxVxCxxC
QVVCGGCRTLLMYPRGASSVRCALCQTVNLV
>gnl|CDD|273418 TIGR01054, rgy, reverse gyrase. This model describes reverse gyrase, found in both archaeal and bacterial thermophiles. This enzyme, a fusion of a type I topoisomerase domain and a helicase domain, introduces positive supercoiling to increase the melting temperature of DNA double strands. Generally, these gyrases are encoded as a single polypeptide. An exception was found in Methanopyrus kandleri, where enzyme is split within the topoisomerase domain, yielding a heterodimer of gene products designated RgyB and RgyA [DNA metabolism, DNA replication, recombination, and repair]
MIPAVYSNLCPNCGGEISSERLEKGLPCARCLPEVATPLKVCRALRKEGTLGALKEYCSIDEELKEFEEF
FKKAVGSEPWSIQKMWAKRVLRGDSFAIIAPTGVGKTTFGLAMSLFLAKKGKRCYIILPTTLLVIQVAEK
ISSLAEKAGVGTVNIGAYHSRLPTKEKKEFMERIENGDFDILITTTMFLSKNYDELGPKFDFIFVDDVDA
LLKASKNVDKLLKLLGFSEELIEKAWKLIRLRLKLYRALHAKKRLELLEAIPGKKRGCLIVSSATGRPRG
KRAKLFRELLGFEVGGGSDTLRNVVDVYVEDEDLKETLLEIVKKLGTGGIVYVSIDYGKEKAEEIAEFLE
NHGVKAVAYHATKPKEDYEKFAEGEIDVLIGVASYYGTLVRGLDLPERVRYAVFLGVPKFKVPLKEALSS
PRRLLLLLSILQEERIESLSEKARKLLGYLKRYIDLIERALEEVERHRGEVREIIEEVMKFLREQLKRED
VVEKILESEDLVLVARGGIPYLVVPDARTYIQASGRTSRLYAGGLTKGLSIVLVDDPEAFEALKKRLKWT
YEIEFKRIDEVDLEKLIREIDEDREKVRRIREGKGRKDLVKTALLVVESPNKARTIARFFGKPSVRKIGG
SVVYEVPVGDLILMITASGGHVFDLVTDKGFHGVLVENGRYVPVYTSIKRCRDCGYQFTEDRESCPKCGS
ENIEDSKSIIEILRELAHEVDEVFIGTDPDTEGEKIGWDLALLLSPYNPNVKRAEFHEVTRRAILEALES
PRSVDENLVKAQVVRRIEDRWIGFTLSQKLWEAFNKRWLSAGRVQTPVLGWIIDRYRESREKRGYLLIFA
LESDFRLGLEHDNRLEAKEFEKDLTWLDVEDIAEREEERNPLPPYTTDTMLEDANRKLGLSVKETMQIAQ
ELFENGLITYHRTDSTRVSDVGMRVAKEYLASRLGGEYFYPREWGEGGAHECIRPTRPLDVDDLQRLILE
GVIELEGLTREHLRLYDLIFRRFMASQMRPAKVDTKEITLKADGKEAEEEGIVEIVERGFELVYPLWRKN
ELEKGSTFIVKDKELRSVPKVYPYTQGEIVQEMKERGIGRPSTYATIVEKLLRRGYVVESKGFLIPTKLG
IEVYNYLTNRYPKLVSEDRTRELEEAMDKIERGELDYLEVLESVYREIKSI
>gnl|CDD|130127 TIGR01055, DNA_topoisomerase_4_subunit_B, DNA topoisomerase IV, B subunit, proteobacterial. Operationally, topoisomerase IV is a type II topoisomerase required for the decatenation of chromosome segregation. Not every bacterium has both a topo II and a topo IV. The topo IV families of the Gram-positive bacteria and the Gram-negative bacteria appear not to represent a single clade among the type II topoisomerases, and are represented by separate models for this reason. This protein is active as an alpha(2)beta(2) heterotetramer [DNA metabolism, DNA replication, recombination, and repair]
TTNYSAKDIEVLDGLEPVRKRPGMYTDTTRPNHLVQEVIDNSVDEALAGFASIIMVILHQDQSIEVFDNG
RGMPVDIHPKEGVSAVEVILTTLHAGGKFSNKNYHFSGGLHGVGISVVNALSKRVKIKVYRQGKLYSIAF
ENGAKVTDLISAGTCGKRLTGTSVHFTPDPEIFDSLHFSVSRLYHILRAKAVLCRGVEIEFEDEVNNTKA
LWNYPDGLKDYLSEAVNGDNTLPPKPFSGNFEGDDEAVEWALLWLPEGGELFMESYVNLIPTPQGGTHVN
GLRQGLLDALREFCEMRNNLPRGVKLTAEDIWDRCSYVLSIKMQDPQFAGQTKERLSSRQVAKFVSGVIK
DAFDLWLNQNVQLAEHLAEHAISSAQRRKRAAKKVVRKKLTSGPALPGKLADCTRQDLEGTELFLVEGDS
AGGSAKQARDREYQAILPLWGKILNTWEVSLDKVLNSQEIHDIEVALGIDPDSNDLSQLRYGKICILADA
DSDGLHIATLLCALFFLHFPKLVEEGHVYVAKPPLYRIDLSKEVYYALDEEEKEKLLYKLKKKKGKPNVQ
RFKGLGEMNPAQLRETTMDPNTRRLVQLTLDDVQDQRVDKIMDMLLAKKRSEDRFNWLQEKGDQI
>gnl|CDD|273419 TIGR01056, DNA_topoisomerase_3, DNA topoisomerase III, bacteria and conjugative plasmid. This model describes topoisomerase III from bacteria and its equivalents encoded on plasmids. The gene is designated topB if found in the bacterial chromosome, traE on conjugative plasmid RP4, etc. These enzymes are involved in the control of DNA topology. DNA topoisomerase III belongs to the type I topoisomerases, which are ATP-independent [DNA metabolism, DNA replication, recombination, and repair]
MTLVLCEKPSQARDLATVLAKKKKGNGYLEIGVGGFVTWAVGHLVELAEPEEYDEKYKNWRTYDLPLEPE
DWQLVVSDKTKKQFNVIKRILKENKVDEVVIATDPDREGELIAREILDYLKVTDKVTIKRLWISSLVDSS
IRKAFKNLRPKSETEGLYKSGVARARADWLVGINLTRAFTKLGREAGNDGVLSVGRVQTPTLAMVVKREN
EIKNFVGKPFYEVSATINKDEQEFTTEWQPYKDEEERELHEFLAENVVTDLTQKPALVTDIEKERKKTSA
PLFYDLSALQEDANKRFGISAKRTLDIAQKLYETHKLITYPRTDSRYLPEDEKEMLLEVLDALKVITPAL
LPIKKRDELTNNRLWNDKKIEDHHAIIPTGNDFNLSDLSEEERNVYKLIAQNYLMQFMPKEEYETTTIEI
AIGKLMFEAKGKILQDNGWKALLGKQEEDEETEDTTLPAFQKGDELDVETLELLEKQTKPPARYTEGTLL
SAMTNPAAFVQDKGLKKTLKETKGLGTEATRADIIENLFKRGFIQKKKNKIYITKNGKLLCLLLPELLTK
PDLTAQWEQYLNGISAGEKDDDDFINTINEMIKQTINEEKKNPETIQKVAKEPVSCGGIAKCPAKDNGRL
IDCKKFPECTEYGNGCEFTIPKKLREKSIP
>gnl|CDD|273420 TIGR01057, DNA_topoisomerase_1, DNA topoisomerase I, archaeal. This model describes topoisomerase I from archaea. These enzymes are involved in the control of DNA topology. DNA topoisomerase I belongs to the type I topoisomerases, which are ATP-independent [DNA metabolism, DNA replication, recombination, and repair]
IAEKPKVAAKIAGALSDGRVLKKSEYGVPYWEVRRDGKKIIVASAVGHLFGLHPKSRGGYPVFDIEWVPI
FEFDKGKGYVSKYIKALSKLAKGADEYINACDYDIEGEVIGFKALKYFCGVERAKRMKFSTLTKQDIRRA
YANPEEIDYGMVDAGMARHILDWYWGINLSRALMEAIRAAAGRWVILSAGRVQGPTLAFLVEREREINLF
VPKPYWVIKATLEKGGGVFDARPEKWKIWSEEEAKSIKEELKKSPWAAVEEVRSERSILKPPPPFDLGTL
QREAYRIFGFSPKKTQSIAQELYEEALISYPRTSSQKLPPSINYRAILDNLAKGPLYREAAERLLETGVL
KPVEGKKEDPAHPAIHPTGEIPSQELSKDEKKVYDLIVRRFLAAFSEEAIREKSKVLLRIGQEKFRLSGL
RVVKLGWLEYYHYSKFEEKELPPLDRGDKIKVVRVDVRVKETQPPARYDKASLIREMESRGLGTKATRAR
IIETLYKRGYIEGKKSIKVTPLGEAVIETLQRYCPEIISEELTRRFESKLEDIMSGRITKDEVIDEAKKR
LRKILEEFKKRLDDIGIELGKSLGSVEVVGKCPKCGGKLVSKYAKKGRFVGCSNYPEC
>gnl|CDD|130130 TIGR01058, DNA_topoisomerase_4_subunit_B, DNA topoisomerase IV, B subunit, Gram-positive. Operationally, topoisomerase IV is a type II topoisomerase required for the decatenation step of chromosome segregation. Not every bacterium has both a topo II and a topo IV. The topo IV families of the Gram-positive bacteria and the Gram-negative bacteria appear not to represent a single clade among the type II topoisomerases, and are represented by separate models for this reason [DNA metabolism, DNA replication, recombination, and repair]
MASKYNADAIKILEGLDAVRKRPGMYIGSTDSKGLHHLVWEIVDNSVDEVLAGYADNITVTLHKDNSITV
QDDGRGIPTGIHQDGNISTVETVFTVLHAGGKFDQGGYKTAGGLHGVGASVVNALSSWLEVTVKRDGQIY
QQRFENGGKIVQSLKKIGTTKKTGTLVHFHPDPTIFKTTQFNSNIIKERLKESAFLLKKLKLTFTDKRTN
KTTVFFYENGLVDFVDYINETKETLSQVTYFEGEKNGIEVEVAFQFNDGDSENILSFANSVKTKEGGTHE
NGFKLAITDVINSYARKYNLLKEKDKNLEGSDIREGLSAIISVRIPEELIQFEGQTKSKLFSPEARNVVD
EIVQDHLFFFLEENNNDAKLLIDKAIKARDAKEAAKKAREEKKSGKKPKKEKGILSGKLTPAQSKNPAKN
ELFLVEGDSAGGSAKQGRDRKFQAILPLRGKVLNVEKAKLADILKNEEINTIIFCIGTGIGADFSIKDLK
YDKIIIMTDADTDGAHIQVLLLTFFYRYMRPLIELGHVYIALPPLYKLSKKDGKKVKYAWSDLELESVKK
KLKNYTLQRYKGLGEMNADQLWETTMNPETRTLVRVKIDDLARAERQINTLMGDKVEPRKKWIEANINFS
VEEELQI
>gnl|CDD|273421 TIGR01059, DNA_gyrase_subunit_B, DNA gyrase, B subunit. This model describes the common type II DNA topoisomerase (DNA gyrase). Two apparently independently arising families, one in the Proteobacteria and one in Gram-positive lineages, are both designated toposisomerase IV. Proteins scoring above the noise cutoff for this model and below the trusted cutoff for topoisomerase IV models probably should be designated GyrB [DNA metabolism, DNA replication, recombination, and repair]
YDASSIKVLEGLEAVRKRPGMYIGSTGETGLHHLVYEVVDNSIDEAMAGYCDTISVTINDDGSVTVEDNG
RGIPVDIHPEEGISAVEVVLTVLHAGGKFDKDSYKVSGGLHGVGVSVVNALSEWLEVTVFRDGKIYRQEF
ERGIPVGPLEVVGETKKTGTTVRFWPDPEIFETTEFDFDILAKRLRELAFLNSGVKISLEDERDGKGKKV
TFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKEGIEVEVALQWNDGYSENILSFVNNINTREGGTHLEG
FRSALTRVINSYAKNNKLLKESKPNLTGEDIREGLTAVISVKVPDPQFEGQTKTKLGNSEVRSIVESLVY
EKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGLPGKLADCSSKDPSKSELYIVE
GDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKDFDLEKLRYHKIII
MTDADVDGSHIRTLLLTFFYRYMRPLIENGYVYIAQPPLYKVKKGKKERYIKDDKEKDLVGEALEDLKAL
YIYSDKEKEEAKTQIPVHLGRKGIEIQRYKGLGEMNADQLWETTMDPESRTLLKVTIEDAVEADRIFSTL
MGDEVEPRREFIEANALDVKNLDV
>gnl|CDD|213580 TIGR01060, eno, phosphopyruvate hydratase. Alternate name: enolase [Energy metabolism, Glycolysis/gluconeogenesis]
IVDIRAREILDSRGNPTVEVEVILEDGTFGRAAVPSGASTGEREALELRDGDKKRYLGKGVLKAVENVNE
IIAPELIGMDATDQREIDQILIELDGTPNKSKLGANAILGVSMAVAKAAADSLGLPLYRYLGGFNAYVLP
VPMMNIINGGAHADNNLDFQEFMIMPVGAPSFREALRMGAEVFHALKKLLKEKGLATGVGDEGGFAPNLA
SNEEALEIIVEAIEKAGYKPGEDVALALDCAASEFYDEEDGKYVYKGENKQLTSEEMIEYYEELVEKYPI
ISIEDGLSEEDWEGWAELTKRLGDKVQIVGDDLFVTNTEILREGIEMGVANSILIKPNQIGTLTETLDAI
ELAKKAGYTAVISHRSGETEDTTIADLAVATNAGQIKTGSLSRSERIAKYNQLLRIEEELGDSARYAGKN
SFYRF
>gnl|CDD|273422 TIGR01061, DNA_topoisomerase_4_subunit_A, DNA topoisomerase IV, A subunit, Gram-positive. Operationally, topoisomerase IV is a type II topoisomerase required for the decatenation of chromosome segregation. Not every bacterium has both a topo II and a topo IV. The topo IV families of the Gram-positive bacteria and the Gram-negative bacteria appear not to represent a single clade among the type II topoisomerases, and are represented by separate models for this reason [DNA metabolism, DNA replication, recombination, and repair]
IFNKPLEEVFGESFGKYAKYIIQDRALPDIRDGLKPVQRRILYAMFQDGNTFDKPYKKSARTVGEIMGKY
HPHGDSSIYDAMVRMSQDWKNNWTLVEMHGNNGSIDGDNAAAMRYTEARLSLIASELLKDIDKKTVSFIP
NFDDSEKEPTVLPALFPNLLINGATGIAAGYATNIPPHNLNEVIDALIYRIDHPNCSVDKLMEIVKGPDF
PTGGIIQGEDGISKAYETGKGKFIIRAKIEIEVNKNGLNQIVITEIPYETNKANIVKKIEEIIFDNKVAG
IEEVRDESDRNGIRIIIELKKDANAEKILNFLFKHTDLQINYNFNMVAIANRTPIQVGLLSYLDAYIKHC
HEVIINRSKYELEKASKRLEIVEGLIKAISIIDEIIKLIRSSEDKSDAKENLIDNFKFTENQAEAIVSLR
LYRLTNTDIFELKEEQNELEKKIISLEQIIASEKARNKLLKKQLEEYKKQFAQQRRSQIEDFINQIKINE
SELIENEDYYVLITKAGYIKRTSNRSFASSKYTDFGSKDDDILFAQTIANTTDQILIFTSLGNIINIPVH
KLADIRWKDLGEHLSNKITFDENETIVFVGTMNEFDVDQPILVLASKLGMVKRIELTELNIKRNSKATLC
IKLKDKDHLISAFLQQKDKLICLVSDLGYALVFHTNEIPVVGAKAAGVKGMKLKEDDQVKSGVIFEANES
LVLLTQRGSVKRLSISELVVTSRAATGKKLLPLKKKPH
>gnl|CDD|130134 TIGR01062, DNA_topoisomerase_4_subunit_A, DNA topoisomerase IV, A subunit, proteobacterial. Operationally, topoisomerase IV is a type II topoisomerase required for the decatenation of chromosome segregation. Not every bacterium has both a topo II and a topo IV. The topo IV families of the Gram-positive bacteria and the Gram-negative bacteria appear not to represent a single clade among the type II topoisomerases, and are represented by separate models for this reason [DNA metabolism, DNA replication, recombination, and repair]
IENIDLGNFTEEAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNANAKYKKSARTVGDVLGKY
HPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKISELLLEELGQGTVDFR
PNFDGTLLEPVILPARLPNILLNGTTGIAVGMATDIPPHNLHELADAALYLIDNPKAGLDDILNIVQGPD
FPTEAEIIDKAEEIRKIYETGRGSFRMRARWKKEDGQIVISALPHQISKSKVIEQIAIQMKDKKLPMISD
IRDESDHENPIRVVIVPRSNRVDPDIVMEHLFATTDLEKSYRLNMNMIGLDNVPAVKNLLEILQEWLVFR
RNTVIRRLTYRLNKVLQRLHILEGLRIAFLNIDEVIEIIREEDEPKTILMERFKLSAIQAEAILNLRLRH
LAKLEEHAIIDEQSELEKERAILEKILKSERELNQLVKKEIQADATKYGLARRSSLEEREEAKQVSEIDM
IPKEPVTIILSKMGWVRSAKGHDIDLSTLKYKAGDSEKAIIEGKSNQKVVFIDSTGRSYALDPDNLPSAR
GQGEPLTGKLLLPIGATITNILMYSPNQLLLMASDAGYGFLCNFNDLIARNKAGKALINLPENASVIAPL
PVNGDSDMIAAITEAGRMLVFPIDDLPELSKGKGNKLIRIPSANAKRGEDGLLDLKIFNKQDGLSWNDGK
RKIQLEPEELQKFLGERGRFGTTLPRGLPKNNRFS
>gnl|CDD|273423 TIGR01063, DNA_gyrase_subunit_A, DNA gyrase, A subunit. This model describes the common type II DNA topoisomerase (DNA gyrase). Two apparently independently arising families, one in the Proteobacteria and one in Gram-positive lineages, are both designated toposisomerase IV [DNA metabolism, DNA replication, recombination, and repair]
IVPVNIEEEMKRSYLDYAMSVIVSRALPDVRDGLKPVHRRILYAMYELGLTPDKPYKKSARIVGDVMGKY
HPHGDSAIYDTLVRMAQDFSLRYPLVDGQGNFGSIDGDPPAAMRYTEARLTKIAEELLRDIDKETVDFVP
NYDGSEQEPTVLPSRFPNLLVNGSSGIAVGMATNIPPHNLGEIIDALLAYIDNPDISIQELLEVIKGPDF
PTGGIILGRSGIRSAYETGRGSIVIRARAEIEEDSKGREAIIVTEIPYQVNKARLIEKIAELVREKKIEG
ISDIRDESDREGIRIVIELKRDAVAEVVLNNLYKQTQLQVSFGINMLALVKGLPKVLNLKELLEAFVEHR
KDVITRRTIFELRKAEERAHILEGLLIALDNIDEVIALIRASQNTEEAKTRLVERFSLSEIQAQAILDMR
LQRLTGLEREKLQEEYKELLELIADLEDILASEERVLEIIREELEEIKEQFGDPRRTEIVYDESEDIDIE
DLIARENVVVTLSHNGYVKRVPVSAYRLQKRGGKGVSGADMKDDDFIEQLLVASTHDYLLFFTNRGKVYW
LKVYQIPEASRTAKGKPIVNLLPLQPDERITAILSVKEFDDGLYLFFATKNGVVKKTSLTEFSNIRSNGI
IAIKLDDGDELISVRLTSGEDEVMLGSKNGKAVRFPEEDVRPMGRAARGVRGIKLKNEDFVVSLLVVSEE
SYLLIVTENGYGKRTSIEEYRETSRGGKGVKSIKITDRNGQVVGAIAVDDDDELMLITSAGKLIRTSVQD
VSEQGRNTQGVRLIRLDEDDKLVSVSKVAK
>gnl|CDD|273424 TIGR01064, Pyruvate_kinase, pyruvate kinase. This enzyme is a homotetramer. Some forms are active only in the presence of fructose-1,6-bisphosphate or similar phosphorylated sugars [Energy metabolism, Glycolysis/gluconeogenesis]
RRTKIVCTIGPATNSPEMLKKLLDAGMNVARLNFSHGSHEEHGKRIENVREAAEKLGRPVAILLDTKGPE
IRTGEIKGGEVKLKKGDKVIITTDDIKGEGDEEKVYVDYKGLTKDVVEGDKILVDDGKISLVVVSVEGDK
VICEVLNGGTLKSKKGVNLPGADVDLPALSEKDKKDLKFGVEQGVDMVAASFVRTAEDVLEVREVLGEKG
AKDVKIIAKIENQEGVDNIDEIAEASDGIMVARGDLGVEIPAEEVPIAQKKMIRKCNRAGKPVITATQML
DSMIKNPRPTRAEVSDVANAVLDGTDAVMLSGETAKGKYPVEAVQMMAKIAKEAEKALAYLTNFNDRKNS
DPKPSTITEAIALSAVEAAEKLDAKAIVVLTESGRTARLLSKYRPNAPIIAVTPNERVARQLALYWGVFP
FLVDEEPSDTDARVNKALELLKEKGIVKKGDLVVVIQGGPIGGEGGTNTIRV
>gnl|CDD|273425 TIGR01065, Hypothetical_UPF0073_protein_yqfA., channel protein, hemolysin III family. This family includes proteins from pathogenic and non-pathogenic bacteria, Homo sapiens and Drosophila. In Bacillus cereus, a pathogen, it has been show to function as a channel-forming cytolysin. The human protein is expressed preferentially in mature macrophages, consistent with a role cytolytic role
EEIANAITHGIGAVLSIIALALLVIYSWDHGGAVAVLGFSIYGISLILLFLVSTLYHSIPKGSKAKNWLR
KIDHSMIYVLIAGTYTPFLLLALPGPLGWTVLWIIWGLAIGGIIYKLFFHKRPRWLSLFLYLIMGWLVVL
VIKPLYHNLPGAGFSLLAAGGLLYTVGAIFYALKWPIPFTYHAIWHLFVLGASACHFVAILFYV
>gnl|CDD|162186 TIGR01066, 50S_ribosomal_protein_L13, ribosomal protein L13, bacterial type. This model distinguishes ribosomal protein L13 of bacteria and organelles from its eukarytotic and archaeal counterparts [Protein synthesis, Ribosomal proteins: synthesis and modification]
TLAKSSDDKERKWYVVDAAGKTLGRLASEVARLLRGKHKPTYTPHVDCGDYVIVINAEKVRLTGKKLEQK
VYYRHSGYPGGLKSRTFEEMIARKPEKVLELAVKGMLPKNRLGRQLFKKLKVYAGSEHPHEAQKPIVLDI
>gnl|CDD|273426 TIGR01067, 50S_ribosomal_protein_L14, ribosomal protein L14, bacterial/organelle. This model distinguishes bacterial and most organellar examples of ribosomal protein L14 from all archaeal and eukaryotic forms [Protein synthesis, Ribosomal proteins: synthesis and modification]
MIQQQSRLNVADNSGAKKVQCIKVLGGSPRRYATVGDVIVVVVKDAIPNGKVKKGDVVKAVIVRTKKGVR
RKDGSYIRFDDNACVLINKNKEPRGTRIFGPVARELRDKGFMKIVSLAPEVI
>gnl|CDD|200072 TIGR01068, Thioredoxin-like_protein_slr0233, thioredoxin. Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin [Energy metabolism, Electron transport]
LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIP
TLLLFKNGKEVDRSVGALPKAALKQLINKNL
>gnl|CDD|130141 TIGR01069, Endonuclease_MutS2, MutS2 family protein. Function of MutS2 is unknown. It should not be considered a DNA mismatch repair protein. It is likely a DNA mismatch binding protein of unknown cellular function [DNA metabolism, Other]
MREKDLIKLEFDKVKENLLKQTFTPLGKEDAIGLKPPKSVEESKEIIIKLTALGSIENNVRFFGFEDIRE
LLKRAELGGIVKGLEYILVIQNALKTVKHLKVLSEHVLDLEILFHLRLNLITLPPLENDIIACIDDDGKV
KDGASEELDAIRESLKALEEEVVKRLHKIIRSKELAKYLSDTIVTIRNGRYVLPLKSGFKGKIKGIVHDT
SSSGETFYIEPQAIVKLNNKLAQLKNEEECEIEKILRTLSEKVQEYLLELKFLFKEFDFLDSLQARARYA
KAVKGEFPMPSFTGKIILENARHPLLKEPKVVPFTLNLKFEKRVLAITGPNTGGKTVTLKTLGLLALMFQ
SGIPIPANEHSEIPYFEEIFADIGDEQSIEQNLSTFSGHMKNISAILSKTTENSLVLFDELGAGTDPDEG
SALAISILEYLLKQNAQVLITTHYKELKALMYNNEGVENASVLFDEETLSPTYKLLKGIPGESYAFEIAQ
RYGIPHFIIEQAKTFYGEFKEEINVLIEKLSALEKELEQKNEHLEKLLKEQEKLKKELEQEMEELKERER
NKKLELEKEAQEALKALKKEVESIIRELKEKKIHKAKEIKSIEDLVKLKETKQKIPQKPTNFQADKIGDK
VRIRYFGQKGKIVQILGGNKWNVTVGGMRMKVHGSELEKINKAPPPKKFKVPKTTKPEPKEASLTLDLRG
QRSEEALDRLEKFLNDALLAGYEVVLIIHGKGSGKLRKGVQELLKNHPKVKSFRDAPPNDGGSGVTIVYL
E
>gnl|CDD|273427 TIGR01070, DNA_mismatch_repair_protein_MutS, DNA mismatch repair protein MutS [DNA metabolism, DNA replication, recombination, and repair]
LTPMMQQYLKLKAEHPDALLFFRMGDFYELFYEDAKKAAQLLDISLTSRGQSADEPIPMAGIPYHAVEAY
LEKLVKQGESVAICEQIEDPKTAKGPVEREVVQLITPGTVSDEALLPERQDNLLAAIAQESNGFGLATLD
LTTGEFKVTELADKETLYAELQRLNPAEVLLAEDLSEMEAIELREFRKDTAVMSLEAQFGTEDLGGLGLR
NAPLGLTAAGCLLQYAKRTQRTALPHLQPVRLYELQDFMQLDAATRRNLELTENLRGGKQNTLFSVLDET
KTAMGSRLLKRWLHRPLRDREVLEARQDTVEVLLRHFFLREGLRPLLKEVGDLERLAARVALGNARPRDL
ARLRTSLEQLPELRALLEELEGPTLQALAAQIDDFSELLELLEAALIENPPLVVRDGGLIREGYDEELDE
LRAASREGTDYLARLEARERERTGIPTLKVGYNAVFGYYIEVTRGQLHLVPAHYRRRQTLKNAERYITPE
LKEKEDKVLEAEGKILALEKELFEELRELLKKYLEALQEAARALAELDVLANLAEVAETLHYTRPRFGDD
PQLRIREGRHPVVEQVLRTPFVPNDLEMAHNRRMLLITGPNMGGKSTYMRQTALIALLAQIGSFVPAESA
ELPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILHNATENSLVLFDEIGRGTSTYDGLALAWAIAEYL
HEHIRAKTLFATHYFELTALEESLPGLKNVHVAALEHNGTIVFLHQVLPGPASKSYGLAVAALAGLPKEV
IARARQILTQLEARSTESEAPQRKAQTSAPEQISLFDEAETHPLLEELAKLDPDDLTPLQALNLLYELKK
>gnl|CDD|273428 TIGR01071, 50S_ribosomal_protein_L15, ribosomal protein L15, bacterial/organelle [Protein synthesis, Ribosomal proteins: synthesis and modification]
KLHELKPAKGSKKRRKRVGRGIGSGLGKTSGRGHKGQKARSGGKVRRGFEGGQMPLYRRLPKRGFSNKRF
KKEYAEVNLGKLAKLFDNGEVVTLETLKEKGLITKKIKFVKVLGNGKLTKPLTVKAHRVSKSAKAAIEAA
GGSVE
>gnl|CDD|162190 TIGR01072, UDP-N-acetylglucosamine_1-carboxyvinyltransferase, UDP-N-acetylglucosamine 1-carboxyvinyltransferase [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNT
LEINTPNINSTEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIE
DGYVYASAKGRLVGAHIVLDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAG
SNTITIEGVEKLHGTEHSVIPDRIEAGTFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENG
IRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAEGTSVITETVFENRFMHVDELIRMGANIKLEG
NTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRGYEDLEEKLRALGAKIER
>gnl|CDD|273429 TIGR01073, ATP-dependent_DNA_helicase_PcrA, ATP-dependent DNA helicase PcrA. Designed to identify pcrA members of the uvrD/rep subfamily [DNA metabolism, DNA replication, recombination, and repair]
LLAHLNPEQREAVKTTEGPLLIMAGAGSGKTRVLTHRIAHLIAEKNVAPWNILAITFTNKAAREMKERVE
KLLGPVAEDIWISTFHSMCVRILRRDIDRIGINRNFSIIDPTDQLSLMKTILKDKNLDPKKFEPRSILGT
ISNAKNELLPPEDFAKEATNYFEKVVAEVYQEYQKRLLRNNALDFDDLIMTTINLFQRVPDVLEYYQRKF
QYIHVDEYQDTNRAQYTLVRLLASRFRNLCVVGDADQSIYGWRGADIQNILSFEKDYPNATTILLEQNYR
STKNILQAANEVIEHNSNRKPKNLWTENSSGDKITYYEADTERDEAQFVAGEIDKLVKNGERKYGDFAIL
YRTNAQSRVFEETLLKANIPYKIVGGLKFYDRKEIKDILAYLRVIANPDDDLSLLRIINVPKRGIGASSL
EKIVNYALELNISLFEAIGEIDEIGGLAAKSANALLAFATMIENLRQQQEYLSPTELVEEVLDKSGYREM
LKAEKTEEAQSRLENLDEFLSVTKEFEDESEDKSLIDFLTDLALVSDLDELEETEEGGAVTLMTLHAAKG
LEFPVVFLIGMEEGVFPHSRSLMDEKELEEERRLAYVGITRAEEELYLTHATMRTLFGRIQMNPPSRFLN
EIPAELLETASTGRRTGATDPKGPSIRQAGASRPTTSQPTAGGDTLSWAVGDRVNHKKWGIGTVVSVKGG
GDDQELDIAFPSIGVKRLLAAFAPIE
>gnl|CDD|130146 TIGR01074, ATP-dependent_DNA_helicase_Rep, ATP-dependent DNA helicase Rep. Designed to identify rep members of the uvrD/rep subfamily [DNA metabolism, DNA replication, recombination, and repair]
KLNPQQQEAVEYVTGPCLVLAGAGSGKTRVITNKIAYLIQNCGYKARNIAAVTFTNKAAREMKERVAKTL
GKGEARGLTISTFHTLGLDIIKREYNALGYKSNFSLFDETDQLALLKELTEGLIKDDKDLLDKLISTISN
WKNDLLTPEQALASARGEREQTFAHCYALYQAHLRAYNALDFDDLILLPTLLLQQNEEVRNRWQNKIRYL
LVDEYQDTNTSQYELVKLLVGDRARFTVVGDDDQSIYSWRGARPENLVLLKEDFPQLKVIKLEQNYRSTG
RILKAANILIANNPHVFEKKLFSELGYGEKIKVIECNNEEHEAERIAGEIIAHKLVNKTQYKDYAILYRG
NHQSRLLEKALMQNRIPYKLSGGTSFFSRPEIKDLLSYLRLLVNPDDDAAFLRIVNTPKREIGPATLEKL
GELAMERNKSLFTASFDMGLLQTLSGRGYESLQRFTDWLVEIRRLAERSEPIEAVRSLIEDIDYENWLYE
TSPSPKAAEMRMKNVNTLFSWFKEMLEGDEEDEPMTLTQVVTRLTLRDMLERGEDEEELDQVQLMTLHAS
KGLEFPYVFIVGMEEGILPHQSSIEEDNVEEERRLAYVGITRAQKELTFTLCKERRQYGELVRPEPSRFL
DELPQEDLQWEGDDPVVSAEEKMEKGQAHLANLR
>gnl|CDD|130147 TIGR01075, DNA_helicase_II, DNA helicase II. Designed to identify uvrD members of the uvrD/rep subfamily [DNA metabolism, DNA replication, recombination, and repair]
LLDGLNDKQREAVAAPPGNLLVLAGAGSGKTRVLTHRIAWLLSVENASPHSIMAVTFTNKAAAEMRHRIG
ALLGTSARGMWIGTFHGLAHRLLRAHHLDAGLPQDFQILDSDDQLRLLKRLIKALNLDEKQWPPRQAMWY
INNQKDEGLRPSHIQAFDNPVERTWIKIYQAYQEACDRAGLVDFAELLLRAHELLRNKPHILQHYQERFT
HILVDEFQDTNKIQYAWIRLLAGNTGNVMIVGDDDQSIYGWRGAQVENIQKFLKDFPGAETIRLEQNYRS
TANILAAANALIANNDERLGKNLWTDGEVGEPISLYSAFNELDEARFVVSRIKTWQRNGGALDECAVLYR
SNAQSRVLEEALLQASIPYRIYGGMRFFERQEIKDALAYLRLIANRNDDAAFERVINTPTRGIGDRTLDV
VRQAARDRGLTLWQAARELTQEKVLAGRAASALQRFVELIEALANETADMPLHVQTDHVIKDSGLREMYQ
QEKGEKGQARIENLEELVTATRQFSLPENDEDMTPLTAFLSHAALEAGEGQADAGQDAVQLMTLHSAKGL
EFPLVFLVGMEEGMFPSQMSLDEGGRLEEERRLAYVGITRAMQKLTITYAETRRLYGKEVYHIPSRFIRE
LPEECLHEVRLRAQVSRPTNLGRVGTPSVDEINDAGFKLGQRVRHPKFGEGTIINAEGSGEHSRLQIAFQ
GQGIKWLVAAYAKLE
>gnl|CDD|130148 TIGR01076, Uncharacterized_protein_YhcS, LPXTG-site transpeptidase (sortase) family protein. This family includes Staphylococcus aureus sortase, a transpeptidase that attaches surface proteins by the Thr of an LPXTG motif to the cell wall. It also includes a protein required for correct assembly of an LPXTG-containing fimbrial protein, a set of homologous proteins from Streptococcus pneumoniae, in which LPXTG proteins are common. However, related proteins are found in Bacillus subtilis and Methanobacterium thermoautotrophicum, in which LPXTG-mediated cell wall attachment is not known [Cell envelope, Other, Protein fate, Protein and peptide secretion and trafficking]
GYLEIPSIDIELPVYPGTAEDTLEKGLGHLEGTSLPVGGENTRIVITGHRGLPTATMFTNLDKLKKGDML
YLHVGNEVLTYQVTSTKIVEPTDTEVLLIQHGKDYLTLITCTPYMINTHRLLVRGKRIPYVATEDE
>gnl|CDD|162192 TIGR01077, 50S_ribosomal_protein_L13, ribosomal protein uL13, archaeal/eukaryotic form. This model represents ribosomal protein of L13 from the Archaea and from the eukaryotic cytosol. Bacterial and organellar forms are represented by model TIGR01066 [Protein synthesis, Ribosomal proteins: synthesis and modification]
TVIDGSGHILGRLASVVAKQLLNGEKVVVVNAEKIVISGNFYRNKLKYKEFLRKRTLTNPRRGPFHPRAP
SRIFRRTVRGMLPHKTARGRAALRRLKVYVGIPPELDKKKRVVVPEALVSRLSPTRKYVTLGELAKFLGW
KY
>gnl|CDD|273430 TIGR01078, Arginine_deiminase, arginine deiminase. Arginine deiminase is the first enzyme of the arginine deiminase pathway of arginine degradation [Energy metabolism, Amino acids and amines]
VYSEIGKLRKVLLHRPGRELENLTPSNLDELLFDDIPWVEDAQKEHDQFANTLRDNGIEVLYLEDLLAET
LDLPEAKEKFIDEFLSESEILGLGLKVELRDYLKSLDTRELVEKLMAGVAKNELPASEGSEKSLMDLGVE
GDSDFVIDPMPNLYFTRDPFASIGNGVTINPMYYKARQRETLFTRAIFKHHPRFANTEFPIWYDRSETAS
IEGGDVLVLNKDVLAIGISERTSAQSVEKLAKSLFANKGGFKKVLAINIPKNRALMHLDTVFTMVDYDKF
TVFPEVVDVFKFSIYDLPYGNNEPIIVEEKAPLEEVLASALGVKKLRLIPTGGGDSVEAEREQWNDGNNV
LAIAPGVVVGYSRNVYTNALLEKAGIKVLTIPGSELSRGRGGPRCMSMPLVRDDI
>gnl|CDD|273431 TIGR01079, 50S_ribosomal_protein_L24, ribosomal protein L24, bacterial/organelle. This model recognizes bacterial and organellar forms of ribosomal protein L24. It excludes eukaryotic and archaeal forms, designated L26 in eukaryotes [Protein synthesis, Ribosomal proteins: synthesis and modification]
MKIKKGDTVKVISGKDKGKRGKVLKVLPKKNKVIVEGVNMVKKHVKPVPANRQGGIIEKEAPIHISNVML
FDPKTGKATRVGYRFEEDGKKVRVFKKNGEII
>gnl|CDD|273432 TIGR01080, 50S_ribosomal_protein_L24P, ribosomal protein uL24, archaeal/eukaryotic form. This model represents the archaeal and eukaryotic branch of the ribosomal protein L24p/L26e family. Bacterial and organellar forms are represented by related model TIGR01079 [Protein synthesis, Ribosomal proteins: synthesis and modification]
SKQPRKQRKALFTAPLHERRKLMSAPLSKELREKYGKRALPIRKGDEVRIVRGDFKGHEGKVSKVDRKRY
RIYVEGVTKEKVDGTEVPVPLHPSNVMITKLHLDDEKRKKLLER
>gnl|CDD|130153 TIGR01081, mpl, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase. Alternate name: murein tripeptide ligase [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
HIHILGICGTFMGGLAMIAKQLGHEVTGSDANVYPPMSTQLEAQGIEIIEGFDAAQLEPKPDLVVIGNAM
KRGNPCVEAVLNLNLPYTSGPQWLHDFVLHDRWVLAVAGTHGKTTTASMLAWVLEQCGLKPGFLIGGVPG
NFGVSARLGESPFFVIEADEYDTAFFDKRSKFVHYRPRTLVLNNLEFDHADIFDDLKAIQRQFHHLVRTV
PGEGLILCPGRDQSLKDTLAKGCWSEQEFFGEQGEWQAEKITADGSHFDVLLDGEKVGEVKWSLVGRHNM
HNALMAIAAARHVGVAIEDACEALGSFVNAKRRLELKGEANGITVYDDFAHHPTAIEATLQGLRQKVGGA
RILAVLEPRSNTMKLGVHKDDLAPSLGRADQVFLYQPGQIPWDVAEVAAQCVQPANVSADFDAFVAMIVK
NAQPGDHILVMSNGGFGGIHGKLLDALR
>gnl|CDD|273433 TIGR01082, UDP-N-acetylmuramate--L-alanine_ligase, UDP-N-acetylmuramate--L-alanine ligase. This model describes the MurC protein in bacterial peptidoglycan (murein) biosynthesis. In a few species (Mycobacterium leprae, the Chlamydia), the amino acid may be L-serine or glycine instead of L-alanine. A related protein, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (murein tripeptide ligase) is described by model TIGR01081 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
KIHFVGIGGIGMSGIAEILLNRGYQVSGSDIAENATTKRLEALGIPIYIGHSAENLDDADVVVVSAAIKD
DNPEIVEAKERGIPVIRRAEMLAELMRFRHSIAVAGTHGKTTTTAMIAVILKEAGLDPTVVVGGLVKEAG
TNARLGSGEYLVAEADESDASFLHLQPNVAIVTNIEPDHLDTYGSSFERLKAAFEKFIHNLPFYGLAVIC
ADDPVLRELVPKATEQVITYGGSGEDADYRAENIQQSGAEGKFSVRGKGKLYLEFTLNLPGRHNVLNALA
AIAVALELGIDFEAILRALANFQGVKRRFEILGEFGGVLLIDDYAHHPTEIKATLKAARQGYPDKRIVVV
FQPHRYSRTRDLFDDFAKVLSDADELILLDIYAAGEEPINGIDGKSLARKITQLGKIEPYFVPDLAELVE
FLAAVLQSGDLILTMGAGDIIKLARELL
>gnl|CDD|273434 TIGR01083, nth, endonuclease III. This equivalog model identifes nth members of the pfam00730 superfamily (HhH-GPD: Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate). The major members of the superfamily are nth and mutY [DNA metabolism, DNA replication, recombination, and repair]
RQKAQEILERLRKNYPHPTTELDFNNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEEL
EEYIKSIGLYRNKAKNIIELCRKLVERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVF
RVSNRLGLSKGKDPIKVEEDLMKLVPREFWVKLHHWLILHGRYTCKARKPLC
>gnl|CDD|130156 TIGR01084, A/G-specific_adenine_glycosylase, A/G-specific adenine glycosylase. This equivalog model identifies mutY members of the pfam00730 superfamily (HhH-GPD: Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate). The major members of the superfamily are nth and mutY [DNA metabolism, DNA replication, recombination, and repair]
QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVL
KLWEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRV
LSRLFAVEGWPGKKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQG
TWEEYPVKKPKAAPPERTTYFLVLQNYDGEVLLEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQRG
>gnl|CDD|273435 TIGR01085, UDP-N-acetylmuramyl-tripeptide_synthetase, UDP-N-acetylmuramyl-tripeptide synthetase. Most members of this family are EC 6.3.2.13, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. An exception is Staphylococcus aureus, in which diaminopimelate is replaced by lysine in the peptidoglycan and MurE is EC 6.3.2.7. The Mycobacteria, part of the closest neighboring branch outside of the low-GC Gram-positive bacteria, use diaminopimelate. A close homolog, scoring just below the trusted cutoff, is found (with introns) in Arabidopsis thaliana. Its role is unknown [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
DLEVTGLTLDSREVKPGDLFVAIKGTHVDGHDFIHDAIANGAVAVVVERDVDFYVAPVPVIIVPDLRHAL
SSLAAAFYGHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGYRLGGNDLIKNPAALTTPE
ALTLQSTLAEMVEAGAQYAVMEVSSHALAQGRVRGVRFDAAVFTNLSRDHLDFHGTMENYFAAKASLFTE
LGLKRFAVINLDDEYGAQFVKRLPKDITVSAITQPADGRAQDIKITDSGYSFEGQQFTFETPAGEGHLHT
PLIGRFNVYNLLAALATLLHLGGIDLEDIVAALEKFRGVPGRMELVDGGQKFLVIVDYAHTPDALEKALR
TLRKHKDGRLIVVFGCGGDRDRGKRPLMGAIAEQLADLVILTSDNPRGEDPEQIIADILAGISEKEKVVI
IADRRQAIRYAISNAKAGDVVLIAGKGHEDYQIIGGETIPFDDR
>gnl|CDD|188107 TIGR01086, L-fuculose-1-phosphate_Aldolase_Complex_With_Pgh, L-fuculose phosphate aldolase. Members of this family are L-fuculose phosphate aldolase from various Proteobacteria, encoded in fucose utilization operons. Homologs in other bacteria given similar annotation but scoring below the trusted cutoff may share extensive sequence similarity but are not experimenally characterized and are not found in apparent fucose utilization operons; we consider their annotation as L-fuculose phosphate aldolase to be tenuous. This model has been narrowed in scope from the previous version [Energy metabolism, Sugars]
NRAELSQQIIDTCLEMTRLGLNQGTAGNVSVRYKDGMLITPTGIPYEKLTTEHIVYVDGNGKHEEGKLPS
SEWQFHLSVYQTRPDANAVVHNHAIHCAAVSILNKSIPAIHYMVAASGTDHIPCVPYATFGSHKLASYVA
TGIKESKAILLQHHGLIACEVNLEKALWLAHEVEVLASLYLKTLAITLEVPVLSKEQMAVVLGKFKTYGL
RIEE
>gnl|CDD|273436 TIGR01087, UDP-N-acetylmuramoylalanine--D-glutamate_ligase, UDP-N-acetylmuramoylalanine--D-glutamate ligase [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
KILILGLGKTGRAVARFLHKKGAEVTVTDLKPNEELEPSMGQLRLNEGSVLHTGLHLEDLNNADLVVKSP
GIPPDHPLVQAAAKRGIPVVGDIELFLRLVPLPVVAITGTNGKTTTTSLLYHLLKAAGLKAFLGGNIGTP
ALEVLDQEGAELYVLELSSFQLETTESLRPEIALILNISEDHLDWHGSFEDYVAAKLKIFARQTEGDVAV
LNADDPRFARLAQKSKAQVIWFSVEKDAERGLCIRDGGLYLKPNDLEGSLLGLHNAENILAAIALAKSLG
LNLEAILEALRSFKGLPHRLEYVGQKNGVHFYNDSKATNVHATLAALSAFDNPVILIVGGDDKGADFSPL
APAAAGKVKAVLAIGEDAAKIAPLLKEAGLSVYLVESLEEAVQAAREVASPGDVVLLSPACASFDQFKSY
EERGEKFKELVRA
>gnl|CDD|130160 TIGR01088, 3-dehydroquinate_dehydratase, 3-dehydroquinate dehydratase, type II. This model specifies the type II enzyme. The type I enzyme, often found as part of a multifunctional protein, is described by TIGR01093 [Amino acid biosynthesis, Aromatic amino acid family]
KILVLNGPNLNMLGLREPGVYGSQTLEEIVEIIETFAAQLNVELEFFQSNSEGQLIDKIHEAEGQYDGII
INPGALTHTSVALRDALAAVSLPVVEVHLSNVHAREEFRHHSYTAPVAGGVIVGLGAQGYLLALRYLVEI
L
>gnl|CDD|130161 TIGR01089, L-fucose_isomerase., L-fucose isomerase. This enzyme catalyzes the first step in fucose metabolism, and has been characterized in Escherichia coli and Bacteroides thetaiotaomicron [Energy metabolism, Sugars]
ISLPKIGIRPTIDGRRMGVRESLEEQTMNMAKAVAALLTEKLRHADGAAVECVIADTTIGGVAEAAACAE
KFSRENVGLTITVTPCWCYGSETIDMDPHRPKAIWGFNGTERPGAVYLAAALAGHSQKGLPAFSIYGHDV
QDADDTSIPEDVEEKLLRFARAGLAVASMRGKSYLSLGSVSMGIAGSIVNHNFFQEYLGMRNEAVDMTEI
RRRIDQKIYDEEELEMALAWADKYCKYGEDENNKEYQRNAEQSRAVWEEVVKMAIIIRDLMQGNPKLADI
GRVEEALGHNAIAAGFQGQRHWTDQYPNGDTAEAILNSSFDWNGVREPFVVATENDSLNGVAMLFGHQLT
GTAQIFADVRTYWSPEAVERVTGHKLDGLAEHGIIHLINSGSAALDGSGKQRDAEGNPTMKPHWEITQQE
ADACLAATEWCPAIHEYFRGGGYSSRFLTKGGVPFTMTRVNLIKGLGPVLQIAEGWSVELPKDVHDKLNK
RTNSTWPTTWFVPRLTGKGAFTDVYSVMANWGANHGVLTIGHVGADLITLASMLRIPVCMHNVEETKIFR
PSAWNAFGMDKEGQDYRACQNYGPLYK
>gnl|CDD|273437 TIGR01090, Adenine_phosphoribosyltransferase, adenine phosphoribosyltransferase. A phylogenetic analysis suggested omitting the bi-directional best hit homologs from the spirochetes from the seed for this model and making only tentative predictions of adenine phosphoribosyltransferase function for this lineage. The trusted cutoff score is made high for this reason. Most proteins scoring between the trusted and noise cutoffs are likely to act as adenine phosphotransferase [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGV
GFVPVRKPGKLPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVV
EAAFLIELKDLNGRAKLEPNVPVFSLLEY
>gnl|CDD|273438 TIGR01091, Uracil_phosphoribosyltransferase, uracil phosphoribosyltransferase. A fairly deep split in phylogenetic and UPGMA trees separates this mostly prokaryotic set of uracil phosphoribosyltransferases from a mostly eukaryotic set that includes uracil phosphoribosyltransferase, uridine kinases, and other, uncharacterized proteins [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
MVVVVDHPLIKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGRILGKKI
VLVPILRAGLGMVDGVLKLIPEAKVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIA
ALDLLKKRGPKKIKVLSIVAAPEGIEAVEKAHPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGTK
>gnl|CDD|130164 TIGR01092, Includes:_Gamma-glutamyl_phosphate_reductase, delta l-pyrroline-5-carboxylate synthetase. This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region [Amino acid biosynthesis, Glutamate family]
RAFLKDVKRIVVKVGTAVVTRGDGRLALGRLGSICEQLSELNSDGREVILVTSGAVAFGRQRLRHRILVN
SSFADLQKPQPELDGKACAAVGQSGLMALYETMFTQLDITAAQILVTDLDFRDEQFRRQLNETVHELLRM
NVVPVVNENDAVSTRAAPYSDSQGIFWDNDSLAALLALELKADLLILLSDVEGLYDGPPSDDDSKLIDTF
YKEKHQGEITFGTKSRLGRGGMTAKVKAAVWAAYGGTPVIIASGTAPKNITKVVEGKKVGTLFHEDAHLW
PTVEQTGERDMAVAARESSRMLQALSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAGYAASLVA
RLSMSPSKISSLAISLRQLAAMEDPIGRVLKRTRIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAI
RSGNGLLLKGGKEAARSNAILHKVITEAIPIHVGKKLIGLVTSREEIPDLLKLDDVIDLVIPRGSNKLVS
QIKKSTKIPVLGHADGICHVYVDKSASVDMAKRIVRDAKCDYPAACNAMETLLVHKDLLRNGLLDDLIDM
LRTEGVTIHGGPRFAAYLTFNISETKSFRTEYSSLACTVEIVDDVYDAIDHIHKHGSAHTDCIVTEDENV
AEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLLTTRWLLRGKGQVVSGDHG
LVYTHKDLPIPQRNT
>gnl|CDD|273439 TIGR01093, 3-dehydroquinate_dehydratase, 3-dehydroquinate dehydratase, type I. This model detects 3-dehydroquinate dehydratase, type I, either as a monofunctional protein or as a domain of a larger, multifunctional protein. It is often found fused to shikimate 5-dehydrogenase (EC 1.1.1.25), and sometimes additional domains. Type II 3-dehydroquinate dehydratase, designated AroQ, is described by the model TIGR01088 [Amino acid biosynthesis, Aromatic amino acid family]
KIFVPLTAPDLEEALAEAEKICEKGADIVELRVDLLKDVSSNNDVDALSEQLSELRVDKPLIFTIRTQSE
GGKFPGNEEEYFEELKRAAESLGPDFVDIELFLPDDAVKELINIAKKGGTKIIMSNHDFQKTPSWEEIVE
RLRKALSYGADIVKIAVMANSKEDVLTLLSATNKVDTHYDVPLITMSMGDRGKISRVLGAVFGSVLTFGS
LGKASAPGQISVDDLRELL
>gnl|CDD|273440 TIGR01096, ABC_transporter_arginine-binding_protein, lysine-arginine-ornithine-binding periplasmic protein [Transport and binding proteins, Amino acids, peptides and amines]
KSVLLAALVAGASSAATAAAAKEGSVRIGTETGYPPFESKDANGKLVGFDVDLAKALCKRMKAKCKFVEQ
NFDGLIPSLKAKKVDAIMATMSITPKRQKQIDFSDPYYATGQGFVVKKGSDLAKTLEDLDGKTVGVQSGT
THEQYLKDYFKPGVDIVEYDSYDNANMDLKAGRIDAVFTDASVLAEGFLKPPNGKDFKFVGPSVTDEKYF
GDGYGIGLRKGDTELKAAFNKALAAIRADGTYQKISKKWF
>gnl|CDD|273441 TIGR01097, PhnE, phosphonate ABC transporter, permease protein PhnE. Phosphonates are a class of compound analogous to organic phosphates, but in which the C-O-P linkage is replaced by a direct, stable C-P bond. Some bacteria can utilize phosphonates as a source of phosphorus. This family consists of permease proteins of known or predicted phosphonate ABC transporters. Often this protein is found as a duplicated pair, occasionally as a fused pair. Certain "second" copies score in between the trusted and noise cutoff and should be considered true hits (by context) [Transport and binding proteins, Anions]
RRRLIRIWLLALLVALYVWAFALLGFDLARLLAGPGQMADLLGRMFPPDWSYLPRILKALLETLAMAILG
TVLAAVLAVPLALLAARNITPSPWLYGLARLLLNFLRAIPELVWALIFVAAVGLGPFAGVLALAFHTVGF
LGKLFAEAIEEVDPGPVEALRATGASKLQVIRYGVLPQVLPQFLSYTLYRFEINVRAAAVLGLVGAGGIG
LELDTAIGLFDYDEVSAIILVILVVVVIIDLISARLRRRL
>gnl|CDD|273442 TIGR01098, Phosphonates-binding_periplasmic_protein, phosphate/phosphite/phosphonate ABC transporter, periplasmic binding protein. Phosphonates are a varied class of phosphorus-containing organic compound in which a direct C-P bond is found, rather than a C-O-P linkage of the phosphorus through an oxygen atom. They may be toxic but also may be used as sources of phosphorus and energy by various bacteria. Phosphonate utilization systems typically are encoded in 14 or more genes, including a three gene ABC transporter. This family includes the periplasmic binding protein component of ABC transporters for phosphonates as well as other, related binding components for closely related substances such as phosphate and phosphite. A number of members of this family are found in genomic contexts with components of selenium metabolic processes suggestive of a role in selenate or other selenium-compound transport. A subset of this model in which nearly all members exhibit genomic context with elements of phosphonate metabolism, particularly the C-P lyase system (GenProp0232) has been built (TIGR03431) as an equivalog. Nevertheless, there are members of this subfamily (TIGR01098) which show up sporadically on a phylogenetic tree that also show phosphonate context and are most likely competent to transport phosphonates [Transport and binding proteins, Anions]
MKRLLALLAALLGASLAAACSKKAAEAAAVPKELNFGILPGENASNLTRRWEPLADYLEKKLGIKVQLFV
ATDYSAVIEAMRFGRVDIAWFGPSSYVLAHYRANAEVFALTAVSTDGSPGYYSVIIVKADSPIKSLKDLK
GKTFAFGDPASTSGYLVPRYQLKKEGGLDADGFFSEVVFSGSHDASALAVANGKVDAATNNSSAIGRLKK
RGPSDMKKVRVIWKSPLIPNDPIAVRKDLPPELKEKIRDAFLTL
>gnl|CDD|273443 TIGR01099, UTP--glucose-1-phosphate_uridylyltransferase, UTP--glucose-1-phosphate uridylyltransferase. Built to distinquish between the highly similar genes galU and galF [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYEL
EHQLEKRGKEELLEEVRKISNLATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQ
MIKAYEKTGCSIIAVQEVPKEEVSKYGVIDGEGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIF
DLLEETPPGKGGEIQLTDAINKLLENETVLAYKFNGKRYDCGSKLGYLEA
>gnl|CDD|130170 TIGR01100, V-type_proton_ATPase_16_kDa_proteolipid_subunit, vacuolar ATP synthase 16 kDa proteolipid subunit. This model describes the vacuolar ATP synthase 16 kDa proteolipid subunit in eukaryotes and includes members from diverse groups e.g., fungi, plants, parasites etc. The principal role V-ATPases are the acidification of intracellular compartments of eukaryotic cells [Transport and binding proteins, Cations and iron carrying compounds]
FFGVMGAAAALVFSALGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIAGSLKP
KSNYSLYKGFIHLGAGLAVGLSGLAAGFAIGIVGDAGV
>gnl|CDD|130171 TIGR01101, V-type_proton_ATPase_subunit_F, vacuolar ATP synthase F subunit. This model describes the vacuolar ATP synthase F subunit (14 kDa subunit) in eukaryotes. In some archaeal species this protein subunit is referred as G subunit [Transport and binding proteins, Cations and iron carrying compounds]
SAEKGKLIAVIGDEDTVVGFLLGGIGEINKNRHPNFLVVDKNTTVSEIEDCFNRFLKRDDIAIILINQHI
AEMIRHAVDAHTRSIPAVLEIPSKDHPYDASKDSILRRARGMFNP
>gnl|CDD|130172 TIGR01102, Harpin_secretion_protein_HrcR, type III secretion apparatus protein, YscR/HrcR family. This model identifies the generic virulence translocation proteins in bacteria. It derives its name:'Yop' from Yersinia enterocolitica species, where this virulence protein was identified. In bacterial pathogenesis, Yop effector proteins are translocated into the eukaryotic cells [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
LIAVLAALSLLPFIIVVGTSFLKISVVLGILRNALGVQQVPPNMALYGIALILSMFVMAPVGHQAQDRFH
QEPVAYSNIDFLQKSLDAGLAPYREFLKKNTDEDEVAFFERSTQKMWPKEMADRLKKDSLLILLPAFTLS
ELTAAFKIGFLLYLPFIVIDLIVSNILLALGMMMVSPMTISLPFKLLLFVLIDGWSRLLHGL
>gnl|CDD|211625 TIGR01103, Flagellar_biosynthetic_protein_FliP, flagellar biosynthetic protein FliP. This model describes bacterial flagellar biogenesis protein fliP, which is one of the genes in motility locus on the bacterial chromosome that is involved in structure and function of bacterial flagellum. It was demonstrated that mutants in fliP locus were non-flagellated and non-motile, while revertants were flagellated and motile [Cellular processes, Chemotaxis and motility]
LLTVLSLAPAILIMMTSFTRIVIVLSILRSALGLQSTPPNQVLLGLALFLTFFVMAPTFDRIYDDAYQPL
LDNQISEQEAYQKAEEPLREFMLRQTRDKDLALFMRLAKIPKPQTPEAVPLRVLVPAFMLSELKTAFQIG
FLIFIPFLIIDLVVASVLMAMGMMMLPPVMISLPFKLMLFVLVDGWNLLVGSLVQSF
>gnl|CDD|273444 TIGR01104, V_PPase, vacuolar-type H(+)-translocating pyrophosphatase. This model describes proton pyrophosphatases from eukaryotes (predominantly plants), archaea and bacteria. It is an integral membrane protein and is suggested to have about 15 membrane spanning domains. Proton translocating inorganic pyrophosphatase, like H(+)-ATPase, acidifies the vacuoles and is pivotal to the vacuolar secondary active transport systems in plants [Transport and binding proteins, Cations and iron carrying compounds]
TEILIPVCAVIGIAYAVLQWVWVSRVKLGTAKMAEIQQAISEGATAFLFTEYKYVAVFMVAFAVLIFVFL
GSREGFSDFSTVAFLLGAVTSLLAGYLGMKIATYANARTTLEARKGVGKALIVAFRSGAVMGFLLAGLGL
LVLYITILVFKIYYGDDWEGLFEPITGYGFGASSMALFGRVGGGIYTKAADVGADLVGKVEAGIPEDDPR
NPAVIADNVGDNVGDIAGMGADLFESYAESSCAALVLASISSFGLPHDFTAMLYPLALSSVGILVCLLTT
LFVKIKPVKEIEPALKKQLIISTVLMTVGVAVISWVALPTGFTIFNFGTQKEVSNWQLFLCVAVGLWAGL
LIGFVTEYYTSNAYSPVQDVADSCRTGAATNVIFGLALGYKSVIIPIFAIAASIIVSFSFAGMYGIAMAA
LGMLSTAGTGLAIDAYGPISDNAGGIAEMAGLPHRVRERTDALDAVGNTTAAIGKGFAIGSAALVALALF
GAFVSRAVITTVDVLTPKVFIGLFVGAMLPYWFSSMTMKSVGRAALKMVEEVRRQFNTIPGLMEGTAKPD
YATCVKISTDASIKEMIPPGLLVMLTPLIVGFLFGVETLSGVLAGVLVSGVQIAISASNTGGAWDNAKKY
IEAGSEHARSLGPKGSEAHKAAVIGDTVGDPLKDTSGPSLNILIKLMAVESLVFAPFFATHGGLL
>gnl|CDD|130175 TIGR01105, UTP--glucose-1-phosphate_uridylyltransferase, UTP-glucose-1-phosphate uridylyltransferase, non-catalytic GalF subunit. GalF is a non-catalytic subunit of the UTP-glucose pyrophosphorylase modulating the enzyme activity to increase the formation of UDP-glucose [Regulatory functions, Protein interactions]
MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTS
YELESLLEQRVKRQLLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFVVVLPDIIIDDATA
DPLRYNLAAMIARFNETGRSQVLAKRMPGDLSEYSVIQTKEPLDREGKVSRIVEFIEKPDQPQTLDSDLM
AVGRYVLSADIWAELERTEPGAWGRIQLTDAIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRN
LKEGAKFRKSIEKLLSE
>gnl|CDD|273445 TIGR01106, Potassium-transporting_ATPase_alpha_chain, sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit. This model describes the P-type ATPases responsible for the exchange of either protons or sodium ions for potassium ions across the plasma membranes of eukaryotes. Unlike most other P-type ATPases, members of this subfamily require a beta subunit for activity. This model encompasses eukaryotes and consists of two functional types, a Na/K antiporter found widely distributed in eukaryotes and a H/K antiporter found only in vertebrates. The Na+ or H+/K+ antiporter P-type ATPases have been characterized as Type IIC based on a published phylogenetic analysis. Sequences from Blastocladiella emersonii (GP|6636502, GP|6636502 and PIR|T43025), C. elegans (GP|2315419, GP|6671808 and PIR|T31763) and Drosophila melanogaster (GP|7291424) score below trusted cutoff, apparently due to long branch length (excessive divergence from the last common ancestor) as evidenced by a phylogenetic tree. Experimental evidence is needed to determine whether these sequences represent ATPases with conserved function. Aside from fragments, other sequences between trusted and noise appear to be bacterial ATPases of unclear lineage, but most likely calcium pumps [Energy metabolism, ATP-proton motive force interconversion]
KKKRDLDELKKEVEMDDHKLSLDELERKYGTDLSKGLSAARAAEILARDGPNALTPPPTTPEWVKFCRQL
FGGFSMLLWIGAILCFLAYGIQASTEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVP
QQALVIRDGEKMSINAEQVVVGDLVEVKGGDRIPADLRIISAQGCKVDNSSLTGESEPQTRSPEFTHENP
LETRNIAFFSTNCVEGTARGIVVNTGDRTVMGRIASLASGLENGKTPIAIEIEHFIHIITGVAVFLGVSF
FILSLILGYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSD
KTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGVSFDKSSATWLALSRIAGLCNRAVFKAGQENVPILKRA
VAGDASESALLKCIELCLGSVMEMRERNPKVVEIPFNSTNKYQLSIHENEDPRDPRHLLVMKGAPERILE
RCSSILIHGKEQPLDEELKEAFQNAYLELGGLGERVLGFCHLYLPDEQFPEGFQFDTDDVNFPTDNLCFV
GLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVN
PRDAKACVVHGSDLKDMTSEQLDEILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALK
KADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIA
NIPLPLGTITILCIDLGTDMVPAISLAYEKAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGF
FTYFVILAENGFLPLHLVGLRVQWDDRWINDLEDSYGQEWTYEQRKYVEFTCHTAFFVSIVVVQWADLII
CKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEIRK
LIIRRNPGGWVEKETYY
>gnl|CDD|273446 TIGR01107, Potassium-transporting_ATPase_subunit_beta, Sodium Potassium ATPase beta subunit. This model describes the Na+/K+ ATPase beta subunit in eukaryotes. Na+/K+ ATPase(also called Sodium-Potassium pump) is intimately associated with the plasma membrane. It couples the energy released by the hydrolysis of ATP to extrude 3 Na+ ions, with the concomitant uptake of 2K+ ions, against their ionic gradients [Transport and binding proteins, Cations and iron carrying compounds]
MARGEKKSCGQRMGEWKKFIWNPETKEFLGRTGGSWFKILLFYLVFYGCLAGIFIGTIQVMLQTISDFTP
KYQDRVASPGLTQRPKVQKLEISFNVSDPSSYEGYVQTLHKFLKPYNDSAQEDKNLEDCGDPAEYKQRGP
FNAPYGTKKACQFKRDWLGNCSGLNDPTFGYSEGKPCVIIKMNRIIGFKPKPNPGVPPVDCTGKRDEDDE
NIGNVEYYPMNGGFPLQYFPYYGKKLQPNYLQPLVAVQFTNLTMNTEVRIECKIYGENIAYSNEKDRFQG
RVDFKITIKS
>gnl|CDD|273447 TIGR01108, Oxaloacetate_decarboxylase_alpha_chain, oxaloacetate decarboxylase alpha subunit. This model describes the bacterial oxaloacetate decarboxylase alpha subunit and its equivalents in archaea. The oxaloacetate decarboxylase Na+ pump is the paradigm of the family of Na+ transport decarboxylases that present in bacteria and archaea. It a multi subunit enzyme consisting of a peripheral alpha-subunit and integral membrane subunits beta and gamma. The energy released by the decarboxylation reaction of oxaloacetate is coupled to Na+ ion pumping across the membrane [Transport and binding proteins, Cations and iron carrying compounds, Energy metabolism, Other]
ITDVVLRDAHQSLFATRMRTEDMLPIAEKLDDVGYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPN
TPLQMLLRGQNLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISY
TTSPVHTLETYLDLAEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRFGLPVHLHSHATTGMAEMAL
LKAIEAGADGIDTAISSMSGGTSHPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFEGQLK
GPDSRILVAQVPGGMLSNLESQLKEQNALDKLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTG
ERYKTITKETKGYLKGEYGRTPAPINAELQRKILGDEKPIVDCRPADLLEPELDKLRAEVREAGAEKNSI
EDVLTYALFPQVGLKFLENRHNPAAFEPKPEEKVIEQEHAQVVGKYEETHASGSYTVEVEGKAFVVKVSP
GGDVSQITASAPANTSGGTVAAKAGAGTPVTAPIAGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAA
AAGTVREILVKVGDAVSVGQVL
>gnl|CDD|130179 TIGR01109, Oxaloacetate_decarboxylase_beta_chain_2, sodium ion-translocating decarboxylase, beta subunit. This model describes the beta subunits of sodium pump decarboxylases that include oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, and glutaconyl-CoA decarboxylase. Beta and gammma-subunits are integral membrane proteins, while alpha is membrane bound. Catalytically, the energy released by the decarboxylation reaction is coupled to the extrusion of Na+ ions across the membrane [Transport and binding proteins, Cations and iron carrying compounds, Energy metabolism, Other]
GQAIMLLVSLLLLYLAIAKKFEPLLLIPIGFGGILSNIPEAGLGLTAEGGILALFYKVGIGSGIAPLLIF
MGIGALTDFGPLLANPRTLLLGAAAQFGIFATVFGALTLNFFGIISFSLPQAAAIGIIGGADGPTAIYLS
GKLAPELLAAIAVAAYSYMALVPIIQPPIMKALTSEKERKIRMKQLRTVSKREKILFPIVLLLLVALLIP
KALPLVGMLMFGNLMRESGVVERLSKTASNELLNIVTILLGLSVGAKMRADKFLTPQTLGILLLGVVAFA
VATAGGVLMAKLMNLFLKEKINPLIGSAGVSAVPMAARVSNKLGLEEDPQNFLLMHAMGPNVAGVIGSAI
AAGV
>gnl|CDD|273448 TIGR01110, alpha_subunit_of_malonate_decarboxylase, malonate decarboxylase, alpha subunit. This model describes malonate decarboxylase alpha subunit, from both the water-soluble form as found in Klebsiella pneumoniae and the form couple to sodium ion pumping in Malonomonas rubra. Malonate decarboxylase Na+ pump is the paradigm of the family of Na+ transport decarboxylases. Essentially, it couples the energy derived from decarboxylation of a carboxylic acid substrate to move Na+ ion across the bilayer. Functional malonate decarboylase is a multi subunit protein. The alpha subunit enzymatically performs the transfer of malonate (substrate) to an acyl carrier protein subunit for subsequent decarboxylation, hence the name: acetyl-S-acyl carrier protein:malonate carrier protein-SH transferase [Transport and binding proteins, Cations and iron carrying compounds, Energy metabolism, Other]
WDKRRTEKQERLNAANELFSDGKVVPTQNGVELLEAVIAPGDRVVLEGNNQKQADFLSRCLASCDPEKIN
DLHMVQSSVPLPEHLDLFEKGIARKLDFSFAGPQSLRIAQLLEDGKLEIGAIHTYLELYSRYFVDLTPNV
SLIAAYEADRDGNLYTGPNTEDTPAIVEATAFRDGIVIAQVNELVDKLPRVDIPASWVDFVIESPKPFYI
EPLFTRDPANITDVQVLMAMMAIKGIYAEYQVQRLNHGIGFNTAAIELLLPTYGESLGLKGKICKNWALN
PHPTLIPAIESGWVESVHSFGGELGMEDYIEARPDVFFTGPDGSMRSNRAFSQTAGQYAVDMFIGSTLQI
DGYGNSSTATRGRLAGFGGAPNMGHDPHGRRHATPAWLKMGAEFTDGDLPRGRKLVVQMVETYQEGMKPT
FVETLDAWELAKKAGMPLAPVMIYGDDVTHIVTEEGIAYLYKCRSLEERMQAIRGVAGYTEVGLSADPKE
TKTLRQRGIIKTPEDLGIDRSDASRSLLAAKSVKDLVEWSGGLYNPPARFRNW
>gnl|CDD|130181 TIGR01111, mtrA, N5-methyltetrahydromethanopterin:coenzyme M methyltransferase subunit A. This model describes N5-methyltetrahydromethanopterin: coenzyme M methyltransferase subunit A in methanogenic archaea. This methyltranferase is a membrane-associated enzyme complex that uses methyl-transfer reaction to drive sodium-ion pump. Archaea have evolved energy-yielding pathways marked by one-carbon biochemistry featuring novel cofactors and enzymes. This transferase (encoded by subunit A) is involved in the transfer of 'methyl' group from N5-methyltetrahydromethanopterin to coenzyme M. In an accompanying reaction, methane is produced by two-electron reduction of methyl-coenzyme M by another enzyme, methyl-coenzyme M reductase [Transport and binding proteins, Cations and iron carrying compounds]
MAEKREPAPGWPIVKGEYVVGDPESPVLVVTLGSHIEEQIILDAGAAIAGPCKTENLGIEKVVANIISNP
NIRFLILCGSEVQGHITGQSFKALHENGVDDDGRIIGALGAIPYLENINEEAVERFQEQIEVVNLIDVED
MGAITSKVKECASKDPGAFDEDPMIIELEEEGGEEEEGGEVKPVSPETAVIESRMRAIEARMKDIGNLNK
FHAGYYSGKIQGIMIGLTSTLSLLGLLL
>gnl|CDD|273449 TIGR01112, mtrD, N5-methyltetrahydromethanopterin:coenzyme M methyltransferase subunit D. This model describes N5-methyltetrahydromethanopterin: coenzyme M methyltransferase subunit D in methanogenic archaea. This methyltranferase is membrane-associated enzyme complex that uses methy-transfer reaction to drive sodium-ion pump. Archaea domain, have evolved energy-yielding pathways marked by one-carbon biochemistry featuring novel cofactors and enzymes. This transferase is involved in the transfer of 'methyl' group from N5-methyltetrahydromethanopterin to coenzyme M. In an accompanying reaction, methane is produced by two-electron reduction of the methyl moiety in methyl-coenzyme M by another enzyme methyl-coenzyme M reductase [Transport and binding proteins, Cations and iron carrying compounds, Energy metabolism, Methanogenesis]
MDALLNILWLVLITIGGVLINWGVHFVPVGGAPAAMATATGVGTGTTQLAAGAGLTGLITAAAMMNVTDN
FLLIMASGAVGAMIMIAVTMLVGNLIYVYGVGVVPSSAKVKVDPITKYRQELYVTPGTEGHGIPTVSFVS
GIIGGALGGIGGALVYYALIEVGLSPGLEAMGAAGVAAIFAVGIFFINAVIASYNIGGTIEGFHDPKFKK
WPKAVVASLVASI
>gnl|CDD|130183 TIGR01113, mtrE, N5-methyltetrahydromethanopterin:coenzyme M methyltransferase subunit E. This model describes N5-methyltetrahydromethanopterin: coenzyme M methyltransferase subunit E in methanogenic archaea. This methyltranfersae is membrane-associated enzyme complex that uses methyl-transfer reaction to drive sodium-ion pump. Archaea have evolved energy-yielding pathways marked by one-carbon biochemistry featuring novel cofactors and enzymes. This transferase is involved in the transfer of 'methyl' group from N5-methyltetrahydromethanopterin to coenzyme M. In an accompanying reaction, methane is produced by two-electron reduction of methyl-coenzyme M by another enzyme methyl-coenzyme M reductase [Transport and binding proteins, Cations and iron carrying compounds, Energy metabolism, Methanogenesis]
LGVLALMGAAATIAGAAEDLESDVGSQSNPNSQVQLAPQMGNLHRIFNKAISGEPVSYGLYCGIAGAVAY
VLMSYFGLPPLIALAVGAVIAALVHLAYATTAYLGRIASSATFNQPVYLDMLTSHLGPIAGHGFIVTFCM
VGVAYLMTLPLKHPFPLPLLAMIWGITIGAIGSSTGDVHYGAEREYQHYPFGGGIPVANHGDITRKAELG
ARNGMDVSYFCSKYGGPLTGLAFGLIVFLSSWTTTIFDQQGLVIGIAGLIIVLILIIYNRKIEVFARNAY
GPY
>gnl|CDD|273450 TIGR01114, mtrH, N5-methyltetrahydromethanopterin:coenzyme M methyltransferase subunit H. This model describes N5-methyltetrahydromethanopterin: coenzyme M methyltransferase subunit H in methanogenic archaea. This methyltranfersae is membrane-associated enzyme complex that uses methyl-transfer reaction to drive sodium-ion pump. Archaea have evolved energy-yielding pathways marked by one-carbon biochemistry featuring novel cofactors and enzymes. This transferase is involved in the transfer of 'methyl' group from N5-methyltetrahydromethanopterin to coenzyme M. In an accompanying reaction, methane is produced by two-electron reduction of methyl-coenzyme M by another enzyme methyl-coenzyme M reductase [Energy metabolism, Methanogenesis]
MFKFDKEQEVFEIAGVKIGGQPGEYPTVLAGTIFYARHKIVEDEDKGIFDKAAAETLIKTQEELSDATGN
PYVVQIFGETPEAIVRYIDWVADITDAPFLIDSTSGEARAAAAKYATEVGLADRAIYNSINASIEEEEIQ
VLKESDLSAAIVLAFNPMDPTVEGKIDILEVGGGTSDKGMLEIAEECGIKYPLIDVAVTPLGAGAGAAVR
SSFAVKAKFGLPVGGGIHNVPSAWDWLREFKKTLKEAGAIHMVCDVGSNLVAQMAGGDYLLYGPIENANM
IFPAVAMVDIMIGEAAKDLGVEPAVENHPFTKLT
>gnl|CDD|273451 TIGR01115, Reaction_center_protein_M_chain, photosynthetic reaction center M subunit. This model decribes the photosynthetic reaction center M subunit in non-oxygenic photosynthetic bacteria. Reaction center is an integral membrane pigment-protein that carries out light-driven electron transfer reactions. At the core of reacion center is a collection light-harvesting cofactors and closely associated polypeptides. The core protein complex is made of L, M and H subunits. The common cofactors include bacterichlorophyll, bacteriopheophytins, ubiquinone and no-heme ferrous iron. The net result of electron tranfer reactions is the establishment of proton electrochemical gradient and production of reducing equivalents in form of NADH. Ultimately the process results in the reduction of C02 to carbohydrates(C6H12O6) In non-oxygenic organisms, the electron donor is some organic acid and not water. Much of our current functional understanding of photosynthesis comes from the structural determination, spectroscopic studies and mutational analysis on the reaction center of Rhodobacter sphaeroides [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]
MAEYQNIFTQVQVRGPPHMGVPLPRGDFPRIGKPIFSYLLGKIGDAQIGPIYLGFTGIVSIVFGLMAIFI
IGFNMLAQVGWNPIQFFRQFFWLGLEPPSPEYGLSIPPLNEGGWWLIAGFFLTVSILLWWVRVYTRARAL
GMGTHLAWAFAAAIFLYLVLGFIRPVLMGSWSEAVPFGIFPHLDWTNAFSLRYGNLYYNPFHMLSIAFLY
GSALLFAMHGATILAVSRFGGDRELEQITDRGTAAERAALFWRWTMGFNATMESIHRWAWWFAVLVTITG
GIGILLSGTVVDNWYLWAVKHGMAP
>gnl|CDD|273452 TIGR01116, ATPase-IIA1_Ca, sarco/endoplasmic reticulum calcium-translocating P-type ATPase. This model describes the P-type ATPase responsible for translocating calcium ions across the endoplasmic reticulum membrane of eukaryotes, and is of particular importance in the sarcoplasmic reticulum of skeletal and cardiac muscle in vertebrates. These pumps transfer Ca2+ from the cytoplasm to the lumen of the endoplasmic reticulum. In humans and mice, at least, there are multiple isoforms of the SERCA pump with overlapping but not redundant functions. Defects in SERCA isoforms are associated with diseases in humans. The calcium P-type ATPases have been characterized as Type IIA based on a phylogenetic analysis which distinguishes this group from the Type IIB PMCA calcium pump modelled by TIGR01517. A separate analysis divides Type IIA into sub-types, SERCA and PMR1, the latter of which is modelled by TIGR01522 [Transport and binding proteins, Cations and iron carrying compounds]
VLEQFEDLLVRILLLAACVSFVLAWFEEGEETVTAFVEPFVILLILVANAIVGVWQERNAEKAIEALKEY
ESEHAKVLRDGRWSVIKAKDLVPGDIVELAVGDKVPADIRVLSLKTLRVDQSILTGESVSVNKHTESVPD
ERAVNQDKKNMLFSGTLVVAGKARGVVVRTGMSTEIGKIRDEMRAAEQEDTPLQKKLDEFGELLSKVIGL
ICILVWVINIGHFNDPALGGGWIQGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRKMAKKNAIVRKL
PSVETLGCTTVICSDKTGTLTTNQMSVCKVVALDPSSSSLNEFCVTGTTYAPEGGVIKDDGPVAGGQDAG
LEELATIAALCNDSSLDFNERKGVYEKVGEATEAALKVLVEKMGLPATKNGVSSKRRPALGCNSVWNDKF
KKLATLEFSRDRKSMSVLCKPSTGNKLFVKGAPEGVLERCTHILNGDGRAVPLTDKMKNTILSVIKEMGT
TKALRCLALAFKDIPDPREEDLLSDPANFEAIESDLTFIGVVGMLDPPRPEVADAIEKCRTAGIRVIMIT
GDNKETAEAICRRIGIFSPDEDVTFKSFTGREFDEMGPAKQRAACRSAVLFSRVEPSHKSELVELLQEQG
EIVAMTGDGVNDAPALKKADIGIAMGSGTEVAKEASDMVLADDNFATIVAAVEEGRAIYNNMKQFIRYMI
SSNIGEVVCIFLTAALGIPEGLIPVQLLWVNLVTDGLPATALGFNPPDKDIMWKPPRRPDEPLITGWLFF
RYLVVGVYVGLATVGGFVWWYLLTHFTGCDEDSFTTCPDFEDPDCYVFEGKQPARTISLSVLVVIEMFNA
LNALSEDQSLLRMPPWVNKWLIGAICLSMALHFLILYVPFLSRIFGVTPLSLTDWLMVLKLSLPVILVDE
VLKFFSR
>gnl|CDD|130187 TIGR01117, methylmalonyl-CoA_decarboxylase_alpha-subunit, methylmalonyl-CoA decarboxylase alpha subunit. This model describes methymalonyl-CoA decarboxylase aplha subunit in archaea and bacteria. Metylmalonyl-CoA decarboxylase Na+ pump is a representative of a class of Na+ transport decarboxylases that couples the energy derived by decarboxylation of carboxylic acid substrates to drive the extrusion of Na+ ion across the membrane [Energy metabolism, ATP-proton motive force interconversion, Energy metabolism, Fermentation, Transport and binding proteins, Cations and iron carrying compounds]
EKIEELHEKKEKIKQGGGEKRIEKQHAQGKMTARERLALLFDPGSFVEIDQFVKHRCTNFGMDKKELPAE
GVVTGYGTIDGRLVYAFAQDFTVMGGSLGEMHAAKIVKIMDLAMKMGAPVVGLNDSGGARIQEAVDALKG
YGDIFYRNTIASGVVPQISAIMGPCAGGAVYSPALTDFIYMVDNTSQMFITGPQVIKTVTGEEVTAEQLG
GAMAHNSVSGVAHFIAEDDDDCIMLIRRLLSFLPSNNMEKAPLVKTGDDPTRETPELYDLLPDNPNKPYD
MRDVITAIVDNGDYLEVQPYYAPNIITCFARINGQSVGIIANQPKVMAGCLDIDSSDKIARFIRFCDAFN
IPIVTFVDVPGFLPGVNQEYGGIIRHGAKVLYAYSEATVPKVTIITRKAYGGAYLAMCSKHLGADQVYAW
PTAEIAVMGPAGAANIIFRKDIKEAKDPAATRKQKIAEYREEFANPYKAAARGYVDDVIEPKQTRPKIVN
ALAMLESKREKLPPKKHGNIPL
>gnl|CDD|130188 TIGR01118, Galactose-6-phosphate_isomerase_subunit_LacA, galactose-6-phosphate isomerase, LacA subunit. This family contains members from low GC gram-positive bacteria. Galactose-6-phosphate isomerase is involved in lactose catabolism by the tagatose-6-phosphate pathway [Energy metabolism, Biosynthesis and degradation of polysaccharides]
MAIIIGSDLAGKRLKDVIKNFLVDNGFEVIDVTEGDGQDFVDVTLAVASEVQKDEQNLGIVIDAYGAGSF
MVATKIKGMIAAEVSDERSAYMTRGHNNARMITVGAEIVGDELAKNIVKAFVEGKYDGGRHQIRVDMLNK
M
>gnl|CDD|130189 TIGR01119, Galactose-6-phosphate_isomerase_lacB_subunit., galactose-6-phosphate isomerase, LacB subunit. This family contains four members from low GC gram-positive bacteria. Galactose-6-phosphate isomerase is involved in lactose catabolism by the tagatose-6-phosphate pathway [Energy metabolism, Biosynthesis and degradation of polysaccharides]
MKIAIGCDHIVTDVKMEVSEFLKSKGYEVLDVGTYDFTRTHYPIFGKKVGEAVVSGEADLGVCICGTGVG
INNAVNKVPGVRSALVRDMTSALYAKEELNANVIGFGGAIIGKLLMFDIIDAFIKAEYKPTEENKKLIAK
IKHLETHNAKQADPHFFDEFLEKWDRGEYHD
>gnl|CDD|130190 TIGR01120, Ribose-5-phosphate_isomerase_B, ribose 5-phosphate isomerase B. Involved in the non-oxidative branch of the pentose phospate pathway [Energy metabolism, Pentose phosphate pathway]
KIAIGSDHAGFILKEEIKAFLVERGVKVIDKGTWSSERTDYPHYAKQVALAVAGGEVDGGILICGTGIGM
SIAANKFAGIRAALCSEPYMAQMSRLHNDANVLCLGERVVGLELAKSIVDAWLGTQFEGGRHQQRVEAIT
AIE
>gnl|CDD|130191 TIGR01121, D-alanine_aminotransferase, D-amino acid aminotransferase. This enzyme is a homodimer. The pyridoxal phosphate attachment site is the Lys at position 146 of the seed alignment, in the motif Cys-Asp-Ile-Lys-Ser-Leu-Asn. Specificity is broad for various D-amino acids, and differs among members of the family; the family is designated equivalog, but with this caveat attached [Energy metabolism, Amino acids and amines]
KVLWNGQLVEREEAKIDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQ
LLHELVEKNNLNTGHVYFQVTRGVAPRNHQFPAGTVKPVITAYTKEVPRPEENLEKGVKAITVEDIRWLR
CDIKSLNLLGNVLAKQEAHEKGAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILA
CAEENGIPVKEEPFTKEELLNADEVFVSSTTAEITPVIEIDGQQIGDGKPGPWTRQLQKAFEEKIP
>gnl|CDD|130192 TIGR01122, ilvE_I, branched-chain amino acid aminotransferase, group I. Among the class IV aminotransferases are two phylogenetically separable groups of branched-chain amino acid aminotransferase (IlvE). The last common ancestor of the two lineages appears also to have given rise to a family of D-amino acid aminotransferases (DAAT). This model represents the IlvE family more strongly similar to the DAAT family [Amino acid biosynthesis, Pyruvate family]
WMDGEFVDWEDAKVHVLTHALHYGTGVFEGIRAYDTDKGPAIFRLKEHIQRLYDSAKIYRMEIPYSKEEL
MEATRETLRKNNLRSAYIRPLVFRGDGDLGLNPRAGYKPDVIIAAWPWGAYLGEEALEKGIDAKVSSWRR
NAPNTIPTAAKAGGNYLNSLLAKSEARRHGYDEAILLDVEGYVAEGSGENIFIVKDGVLFTPPVTSSILP
GITRDTVITLAKELGIEVVEQPISREELYTADEAFFTGTAAEITPIREVDGRKIGNGRRGPVTKKLQEAF
FDLVTGGTEDYWGWLTYV
>gnl|CDD|233278 TIGR01123, ilvE_II, branched-chain amino acid aminotransferase, group II. Among the class IV aminotransferases are two phylogenetically separable groups of branched-chain amino acid aminotransferase (IlvE). The last common ancestor of the two lineages appears also to have given rise to a family of D-amino acid aminotransferases (DAAT). This model represents the IlvE family less similar to the DAAT family [Amino acid biosynthesis, Pyruvate family]
WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELF
LEALRQLVKANKDWVPPYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLAPVSIFVT
TEYDRAAPGGTGAVKVGGNYAASLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFITGDGELVTPP
LSGSILPGITRDSLLQLAKDLGMEVEERRIDIDELKAFVEAGEIVFACGTAAVITPVGEIQHGGKEVVFA
SGQPGEVTKALYDELTDIQYGDFEDPYGWIVEV
>gnl|CDD|130194 TIGR01124, L-threonine_dehydratase_biosynthetic_IlvA, threonine ammonia-lyase, biosynthetic, long form. This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (pfam00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain [Amino acid biosynthesis, Pyruvate family]
DYLRAILTARVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIA
ASAGNHAQGVAFSAARLGLKALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFI
HPFDDPLVIAGQGTLALEILRQVANPLDAVFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQA
LDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQYLDDIVTVDTDEVCAAIKDLFEDTRAVAEPAGALAL
AGLKKYVALHGIRGQTLVAILSGANMNFHRLRYVSERCELGEQREALLAVTIPEQPGSFLKFCELLGNRN
ITEFNYRYADRKDAHIFVGVQLSNPQERQEILARLNDGGYSVVDLTDDELAKLHVRYMVGGRPPHVENER
LYSFEFPERPGALLRFLNTLQGYWNISLFHYRNHGADYGRVLAGFQVPDHEPDQFEQFLAELGYRYHDET
NNPAYRLFL
>gnl|CDD|273453 TIGR01125, Ribosomal_protein_S12_methylthiotransferase_RimO, ribosomal protein S12 methylthiotransferase RimO. Members of this protein are the methylthiotransferase RimO, which modifies a conserved Asp residue in ribosomal protein S12. This clade of radical SAM family proteins is closely related to the tRNA modification bifunctional enzyme MiaB (see TIGR01574), and it catalyzes the same two types of reactions: a radical-mechanism sulfur insertion, and a methylation of the inserted sulfur. This clade spans alpha and gamma proteobacteria, cyano bacteria, Deinococcus, Porphyromonas, Aquifex, Helicobacter, Campylobacter, Thermotoga, Chlamydia, Streptococcus coelicolor and Clostridium, but does not include most other gram positive bacteria, archaea or eukaryotes [Protein synthesis, Ribosomal proteins: synthesis and modification]
KIGFISLGCPKNLVDSEVLLGVLREAGYEVVPNYEDADVVIVNTCGFIEDAKQESIDTIGEFADAGKKVI
VTGCLVQRYKEELKEEIPEVDAITGSGDVEEILNAIENGEPGDLVPFKSEIEMGEVPRILLTPRHYAYLK
IAEGCNRRCAFCIIPSIRGKLRSRPIEEILREAERLVDQGVKEIILIAQDTTAYGKDLYRESKLVDLLER
LGKLGGIFWIRMHYLYPDELTDDVIDLMAEGPKVLPYLDIPLQHASDRILKLMRRPGSGEEQLDMIERIR
EKCPDAVLRTTFIVGFPGETEEDFQELLDFVEEGQFDRLGAFTYSPEEGTDAFALPDQVPEEVKEERLER
LMQLQQRISAKKLQEFVGKKIEVLIDGYEPEFNLLIGRTYGQAPEVDGVVYVNGKGKIGDILRVVITETD
EYDLWG
>gnl|CDD|273454 TIGR01126, Putative_protein_disulfide-isomerase_C1F5.02, protein disulfide-isomerase domain. This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK [Protein fate, Protein folding and stabilization]
LTASNFDEIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDPKIVLAKVDATAEKDLASRFGVSGF
PTIKFFPKGSKPVDYEGGRDLEAIVEFVNEKS
>gnl|CDD|130197 TIGR01127, ilvA_1Cterm, threonine ammonia-lyase, medium form. A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes [Amino acid biosynthesis, Pyruvate family]
TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKF
GIKAVIVMPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGL
EIMEDIPDVDTVIVPVGGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADG
IAVKKPGDLTFNIIKEYVDDVVTVDEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVV
LSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLPDRPGALYHLLESIAEARANIVKIDHDRLSKEIPPGFA
MVEITLETRGKEHLDEILKILRDMGYNFYV
>gnl|CDD|273455 TIGR01128, DNA_polymerase_III_subunit_delta, DNA polymerase III, delta subunit. DNA polymerase III delta (holA) and delta prime (holB) subunits are distinct proteins encoded by separate genes. The delta prime subunit (holB) exhibits sequence homology to the tau and gamma subunits (dnaX), but the delta subunit (holA) does not demonstrate this same homology with dnaX. The delta, delta prime, gamma, chi and psi subunits form the gamma complex subassembly of DNA polymerase III holoenzyme, which couples ATP to assemble the ring-shaped beta subunit around DNA forming a DNA sliding clamp [DNA metabolism, DNA replication, recombination, and repair]
EEAADAIRAAALAQGFDEFNVFRIDGEEFDWNQLLEEAQTLPLFSERRLVELRNPEGKPGAKGLKALEEY
LANPPPDTLLLIEAPKLDKRKKLTKWLKALKNAEIVECKTPKEQELPRWIQARLKKLGLRIDPDAVQLLA
ELVEGNLLAIAQELEKLALYAPDGKITLEDVEEAVSDSARFNVFDLTDALLEGKAARALRILKGLLGEGE
EPLILLALLQRQLRLLLQLKRLAQQGGPLAQLASKLGIWPYRRKLALKALRRLSLAKLEQALQELAEADL
QLKGTGGGDPWLALERLLLKLA
>gnl|CDD|273456 TIGR01129, Protein_translocase_subunit_SecD, protein-export membrane protein SecD. Members of this family are highly variable in length immediately after the well-conserved motif LGLGLXGG at the amino-terminal end of this model. Archaeal homologs are not included in the seed and score between the trusted and noise cutoffs. SecD from Mycobacterium tuberculosis has a long Pro-rich insert [Protein fate, Protein and peptide secretion and trafficking]
LGLDLRGGARVLLEVDMSTAVVLKLSEAEVNAIRKDALEQVITILRNRVNALGVSEPVVQRQGKDRIVVE
LPGVTDTSRAKDILGGTATLEFRLVDDESTSPDDALAGNVPAGSELLDSRSGDPKYYLLKKSPVLTGDHI
TDATSSVDQRSGQPVVSFSLDSEGARIFGDFTQANIGKRLAIVLDNKVVSAPTIQEAITGGSGQITGNFT
AEEANDLALVLRSGALPAPLQILEERTIGPSLGADSIEAGIKAGLIGLVLVLVFMILYYRLFGLIAAIAL
VINIVLILAILSAFGATLTLPGIAGLILTIGMAVDANVLIYERIKEELRLGKSVRQAIEAGFERAFSTIF
DANITTLIAALILYVFGTGPVKGFAVTLAIGIIASLFTALVFTRLLL
>gnl|CDD|273457 TIGR01130, Protein_disulfide-isomerase, protein disulfide isomerase, eukaryotic. This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs)
EDVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEKDLAQK
YGVSGYPTLKIFRNGEDSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVVVIGFFKDL
DSELNDTFLSVAEKLRDVYFFFAHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEMDTDVSDLEKF
IRAESLPLVGEFTQETAAKYFESGPLVVLYYNVDESLDPFEELRNRFLEAAKKFRGKFVNFAVADEEDFG
RELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEAFVKDFLDGKLKPYLKSEPIPEDDEGPVKV
LVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKMDATANDVPPFEVEGF
PTIKFVPAGKKSEPVPYDGDRTLEDFSKFIAKHATFPLEGKA
>gnl|CDD|273458 TIGR01131, ATP_synthase_subunit_a, ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes). Bacterial forms should be designated ATP synthase, F0 subunit A; eukaryotic (chloroplast and mitochondrial) forms should be designated ATP synthase, F0 subunit 6. The F1/F0 ATP synthase is a multisubunit, membrane associated enzyme found in bacteria and mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. Individual subunits in each of these clusters are named differently in prokaryotes and in organelles e.g., mitochondria and chloroplast. The bacterial equivalent of subunit 6 is named subunit 'A'. It has been shown that proton is conducted though this subunit. Typically, deprotonation and reprotonation of the acidic amino acid side-chains are implicated in the process [Energy metabolism, ATP-proton motive force interconversion]
LFSQFDISPITLFSLTLLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKF
FPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLI
PFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSLMSSAIFALLLLILVALIILEIFVAFIQ
AYVFTLLTCLYLNDAL
>gnl|CDD|273459 TIGR01132, pgm, phosphoglucomutase, alpha-D-glucose phosphate-specific. This enzyme interconverts alpha-D-glucose-1-P and alpha-D-glucose-6-P [Energy metabolism, Sugars]
AIHPRAGQPAQQEDLINVAQLVAQYYVLQPEAGNAAHAVKFGTSGHRGSALRGTFNEPHILAIAQAIAEY
RAAQGITGPLYIGKDTHALSEPAFISVLEVLAANGVEVIVQENNGFTPTPAVSHAILTHNKKGEPLADGI
VITPSHNPPEDGGIKYNPPNGGPADTEATQAIEDRANALLANGLKGVKRLPLAQALASGTVKAHDLVQPY
VDGLADIVDMAAIQKAGLRLGVDPLGGSGIDYWKRIAEKYNLNLTLVNPQVDPTFRFMTLDKDGKIRMDC
SSPYAMAGLLALRDKYDLAFGNDPDYDRHGIVTPAGLMNPNHYLAVAINYLFQHRPQWGGDVAVGKTLVS
SAMIDRVVADLGRQLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFDGTPWSTDKDGIIMCLLAAEI
TAVTGKNPQQHYNELAAKFGAPSYNRIQAPATSAQKARLKKLSPEMVSATTLAGDPITARLTAAPGNGAA
IGGLKVTTDNGWFAARPSGTEDVYKIYCESFKGEEHLKQIEKEAVEIVSEVLK
>gnl|CDD|273460 TIGR01133, murG, undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase. RM 8449890 RT The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. RA Bupp K, van Heijenoort J. RL J Bacteriol 1993 Mar;175(6):1841-3 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
KKIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLK
TPLKLLKAVFKARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVL
VSFPGAKDHFEAVLVGNPVRKEIRSLPVPRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKGI
QIVHQGGKGDLEKVKNVYQELGQEKIVTFIDENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPY
AADDQYYNAKFLEDLGAGLVIRQKELLPEKLLEALLKLLLDPANLENMAEAARKLAKPDAAKRIAELI
>gnl|CDD|273461 TIGR01134, purF, amidophosphoribosyltransferase. Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
CGVVGIYGQEEVAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIG
HVRYSTAGSSGLENAQPFVVNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDE
SKDDLFDAVARVLERVRGAYALVLMTEDGLVAVRDPHGIRPLVLGRRGDGYVVASESCALDILGAEFVRD
VEPGEVVVIFDGGLESRQCARRPRAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARESPVEADVVVP
VPDSGRSAALGFAQASGIPYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIV
RGTTSRQIVEMLRDAGAKEVHVRIASPPIRYPCYYGIDMPTREELIAARRTVEEIRKIGADSLAYLSLEG
LKEAVGNPESDLCLACFTGEYP
>gnl|CDD|273462 TIGR01135, glmS, glucosamine--fructose-6-phosphate aminotransferase (isomerizing). The member from Methanococcus jannaschii contains an intein [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAELANKLGEKPLPGGVGIGH
TRWATHGKPTDENAHPHTDEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGG
DLLEAVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDG
DIAILTKDGVEIYNFEGAPVQREVRVIDWDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFE
ELGAEELLKNIDRIQIVACGTSYHAGLVAKYLIERLAGIPVEVEIASEFRYRKPVVDKDTLVIAISQSGE
TADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQLTVLYLLALALAKA
RGTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLKEISY
IHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDV
IKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE
>gnl|CDD|273463 TIGR01136, Cysteine_synthase, cysteine synthase. This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff [Amino acid biosynthesis, Serine family]
IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTG
IALAMVAAARGYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETNKYVMLDQFE
NPANPEAHYKTTGPEIWRDTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPG
PHKIQGIGAGFIPKILDLSLIDEVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADK
VIVAILPDTGERYLSTGLF
>gnl|CDD|273464 TIGR01137, Cystathionine_beta-synthase, cystathionine beta-synthase. Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven [Amino acid biosynthesis, Serine family]
ILDNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTS
GNTGIGLALVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGA
HILDQYRNPSNPLAHYDTTGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSIL
AQPEELNQTGRTPYKVEGIGYDFIPTVLDRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAA
LKAAEDELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDNGFLDDEDLTVKDVLWWHARVKDLHLPAPVTVH
PTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQPSDAVSKVMSKKFIQIGLGETL
SDLSKFLEMDSSAIVVEEGKPIGVVTKIDLLSFLA
>gnl|CDD|130208 TIGR01138, Cysteine_synthase_B, cysteine synthase B. CysM differs from CysK in that it can also use thiosulfate instead of sulfide, to produce cysteine thiosulfonate instead of cysteine. Alternate name: O-acetylserine (thiol)-lyase [Amino acid biosynthesis, Serine family]
TIEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNT
GIALAMIAALKGYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLLDQFN
NPDNPYAHYTSTGPEIWQQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPGIRRW
PTEYLPGIFDASLVDRVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDAVVVAIICDR
GDRYLSTGVF
>gnl|CDD|273465 TIGR01139, Cysteine_synthase, cysteine synthase A. This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate [Amino acid biosynthesis, Serine family]
ISELIGNTPLVRLNRIEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGI
ALAMVAAARGYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFE
NPANPEIHRKTTGPEIWRDTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPG
PHKIQGIGAGFIPKNLNRSVIDEVITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKL
IVVILPSTGERYLSTPLF
>gnl|CDD|273466 TIGR01140, L_thr_O3P_dcar, L-threonine-O-3-phosphate decarboxylase. This family contains pyridoxal phosphate-binding class II aminotransferases (see pfamAM:pfam00222) closely related to, yet distinct from, histidinol-phosphate aminotransferase (HisC). It is found in cobalamin biosynthesis operons in Salmonella typhimurium and Bacillus halodurans (each of which also has HisC) and has been shown to have L-threonine-O-3-phosphate decarboxylase activity in Salmonella. Although the gene symbol cobD was assigned in Salmonella, cobD in other contexts refers to a different cobalamin biosynthesis enzyme, modeled by pfam03186 and called cbiB in Salmonella [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
HGGNLRRAAARYGIPPEDWLDLSTGINPLGPPVPPIPLSAWARYPDPEYDELRAAAAAYYGLPAASVLPV
NGAQEAIYLLPRLLAPGRVLVLAPTYSEYARAWRAAGHEVVELPDLDRLPAALEEADLLVVCNPNNPTGR
LIPPETLLALAARLRARGGWLVVDEAFIDFTPDASLAPQAARFPGLVVLRSLTKFFGLAGLRLGFVVAHP
ALIARLREALGPWTVNGPALAAGRAALADTAWQAATRARLAAERARLAALLARLGGLRVVGGTALFLLVR
TPDAAALHEALARRGILIRDFDNFPGLDPRYLRFALPTDEENDRLLEALA
>gnl|CDD|273467 TIGR01141, Histidinol-phosphate_aminotransferase, histidinol-phosphate aminotransferase. Alternate names: histidinol-phosphate transaminase; imidazole acetol-phosphate transaminase Histidinol-phosphate aminotransferase is a pyridoxal-phosphate dependent enzyme [Amino acid biosynthesis, Histidine family]
RPDIKNLSPYQPGARELGGDEVIKLNSNENPFGPPEKAKEALRAELKKLHRYPDPDPAELKQALADYYGV
DPEQILLGNGSDEIIDLLIRAFLEPGDAVLVPPPTYSMYEISAKIHGAEVVKVPLDEDGQLDLEDILVAI
DDKPKLVFLCSPNNPTGNLFSRGDIEAVLERTPGDALVVVDEAYGEFSGEPSTLPLLAEYPNLIVLRTLS
KAFGLAGLRIGYAIANAEIIDALNKVRAPFNLSRLAQAAAIAALRDDDFIEATVEEINAERERLYDGLKK
LPGLEVYPSDANFVLIRFPGDADALFEALLEKGIIVRDLNSYPGLLPNCLRITVGTREENDRFLAALREI
>gnl|CDD|130212 TIGR01142, Phosphoribosylglycinamide_formyltransferase_2, phosphoribosylglycinamide formyltransferase 2. This enzyme is an alternative to PurN (TIGR00639) [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
RVLLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSYVINMLDGDALRAVIEREKPDYIVPEI
EAIATDALFELEKEGYFVVPNARATKLTMNREGIRRLAAEELGLPTSRYMFADSLDELREAVEKIGYPCV
VKPVMSSSGKGQSVVRGPEDIEKAWEYAQEGARGGAGRVIVEEFIDFDYEITLLTVRHVDGNTTFCAPIG
HRQIDGDYHESWQPQEMSEKALEEAQRIAKRITDALGGYGLFGVELFVKGDEVIFSEVSPRPHDTGMVTL
ISQGLSEFALHVRAILGLPIPGIPQLGPAASAVIKAKVTGYSPAFRGLEKALSVPNTQVRLFGKPEAYVG
RRLGVALATAKSVEAARERAEEVAHAVEVR
>gnl|CDD|273468 TIGR01143, murF, UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase. This family consists of the strictly bacterial MurF gene of peptidoglycan biosynthesis. This enzyme is almost always UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanyl ligase, but in a few species, MurE adds lysine rather than diaminopimelate. This enzyme acts on the product from MurE activity, and so is also subfamily rather than equivalog. Staphylococcus aureus is an example of species in this MurF protein would differ [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
TDSRAIKPGDLFIALKGERFDGHDFVEQALAAGAVAVVVDREVGPDNGLPQILVDDTLEALQALARAKRA
KFSGKVIGITGSSGKTTTKEMLAAILSHKYKVFATPGNFNNEIGLPLTLLRAPGDHDYAVLEMGASHPGE
IAYLAEIAKPDIAVITNIGPAHLEGFGSLEGIAEAKGEILQGLKENGIAVINADDPAFADLAKRLPNRNI
LSFGFEGGDFVAKDISYSALGSTSFTLVAPGGEFEVSLPLLGRHNVMNALAAAALALELGIPLEEIAEGL
AELKLVKGRFEVQTKNGLTLIDDTYNANPDSMRAALDALARFPGKKILVLGDMAELGEYSEELHAEVGRY
ANSLGIDLVFLVGEEAAVIYDSFGKQGKHFADKDELLAFLKTLVRKGDVVLVKGSRSVKLEKVVEAL
>gnl|CDD|130214 TIGR01144, ATP_synthase_subunit_b, ATP synthase, F0 subunit b. This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase [Energy metabolism, ATP-proton motive force interconversion]
QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENA
NKRGSEILEEAKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLI
DKLVAEL
>gnl|CDD|130215 TIGR01145, ATP_synthase_subunit_delta, ATP synthase, F1 delta subunit. This model describes the ATP synthase delta subunit in bacteria, mitochondria, and chloroplasts. It is sometimes called OSCP for Oligomycin Sensitivity Conferring Protein. F1/F0-ATP synthase is a multisubunit, membrane associated enzyme found in bacteria and organelles of higher eukaryotes, namely, mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. Delta subunit belongs to the F1 cluster or sector and functionally implicated in the overall stability of the complex. Expression of truncated forms of this subunit results in low ATPase activity [Energy metabolism, ATP-proton motive force interconversion]
VARPYAKALFEIANEKSSLEEWGEMLNFVKEVLKNNKELKKFLSNPLISAEKKKEFIKNVFGEQLDESSL
NLLLLLAENGRLAALPDILDQFLKLSYEAQQTADVEVISAKPLTEDQQAKIAEKLEKITGAAKVKLNCKV
DKDLIGGVIIRIGDRVIDGSVRGQLKRLSRQL
>gnl|CDD|273469 TIGR01146, ATP_synthase_gamma_chain, ATP synthase, F1 gamma subunit. This model describes the ATP synthase gamma subunit in bacteria and its equivalents in organelles, namely, mitochondria and chloroplast. F1/F0-ATP synthase is a multisubunit, membrane associated enzyme found in bacteria and organelles of higher eukaryotes, namely, mitochondria and chloroplast. This enzyme is principally involed in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. The gamma subunit is the part of F1 cluster. Surrounding the gamma subunit in a cylinder-like structure are three alpha and three subunits in an alternating fashion. This is the central catalytic unit whose different conformations permit the binding of ADP and inorganic phosphate and release of ATP [Energy metabolism, ATP-proton motive force interconversion]
ATLKEIRTRIKSVKNTQKITKAMKMVAASKLRRAQERAEAARPYAEKIRAVLGNLATKLLNVDHPLLKSR
EVKKVGILVITSDRGLCGGYNSNVLKRVRARAKELKAAGKEVKLVVIGRKGKSFFKRRGDNIVLSITGLS
DQPTFEEASGIADKLLDAFDAGEFDELYIVYNKFVSSISQEPTVKQLLPLSAQGPDEGFKFSQDYIFEPD
EEEILDDLLPRYLESQIYGALLESAASEQAARMTAMDNATDNAGDLIKKLTLSYNRARQAAITQELIEIV
AGASAL
>gnl|CDD|130217 TIGR01147, V-type_proton_ATPase_subunit_G, vacuolar ATP synthase, subunit G. This model describes the vacuolar ATP synthase G subunit in eukaryotes and includes members from diverse groups e.g., fungi, plants, parasites etc. V-ATPases are multi-subunit enzymes composed of two functional domains: A transmembrane Vo domain and a peripheral catalytic domain V1. The G subunit is one of the subunits of the catalytic domain. V-ATPases are responsible for the acidification of endosomes and lysosomes, which are part of the central vacuolar system [Energy metabolism, ATP-proton motive force interconversion]
MASQTQGIQQLLQAEKRAAEKVSEARKRKTKRLKQAKEEAQKEVEKYKQQREKEFKEFEAKHLGGNGAAE
EKAEAETQAKIREIKKAVQKNKDAVIKDLLHLVCDISPELHIN
>gnl|CDD|130218 TIGR01148, mtrC, N5-methyltetrahydromethanopterin:coenzyme M methyltransferase subunit C. This model describes N5-methyltetrahydromethanopterin: coenzyme M methyltransferase subunit C in methanogenic archaea. This methyltranferase is membrane-associated enzyme complex that uses methyl-transfer reaction to drive sodium-ion pump. Archaea have evolved energy-yielding pathways marked by one-carbon biochemistry featuring novel cofactors and enzymes. This transferase is involved in the transfer of 'methyl' group from N5-methyltetrahydromethanopterin to coenzyme M. In an accompanying reaction, methane is produced by two-electron reduction of the methyl moiety in methyl-coenzyme M by another enzyme methyl-coenzyme M reductase [Energy metabolism, Other]
MSAGGAGGEAKEAYPEQTIMALGIVGGLVGIYLGNFFPPAGPLIGGLGAICATVWGADAVRRVASYGLGT
GVPSIGMMSLGMGILAAVAGLALGGNTPAIAAPIIALVVAAIIGGVVGVLANKVIGMKIPIMERCMTEIS
CAGTLALLGLSVAIAGSFTWQAVISYVIANGYIALLFIIGGMAILHPFNACLGPNESQDRTLWLAVECGF
ITGFVSSLHEGLMVAGLNILVGAIIWYVAFSKFVALSKRDAAAVVWTGLLPKGEE
>gnl|CDD|130219 TIGR01149, mtrG, N5-methyltetrahydromethanopterin:coenzyme M methyltransferase subunit G. This model describes N5-methyltetrahydromethanopterin: coenzyme M methyltransferase subunit G in methanogenic archaea. This methyltranfersae is membrane-associated enzyme complex that uses methyl-transfer reaction to drive sodium-ion pump. Archaea have evolved energy-yielding pathways marked by one-carbon biochemistry featuring novel cofactors and enzymes. This transferase is involved in the transfer of 'methyl' group from N5-methyltetrahydromethanopterin to coenzyme M. In an accompanying reaction, methane is produced by two-electron reduction of the methyl moiety in methyl-coenzyme M by another enzyme methyl-coenzyme M reductase [Energy metabolism, Other]
DEKAPAVFVEPDEFNEVMKRLDEIEEKVEFVNGEVAQRIGKKVGRDIGILYGLVIGLILFLIYILLSSMF
>gnl|CDD|273470 TIGR01150, Reaction_center_protein_H_chain, photosynthetic reaction center, subunit H, bacterial. This model describes the photosynthetic reaction center H subunit in non-oxygenic photosynthetic bacteria. The reaction center is an integral membrane pigment-protein that carries out light-driven electron transfer reactions. At the core of reaction center is a collection light-harvesting cofactors and closely associated polypeptides. The core protein complex is made of L, M and H subunits. The common cofactors include bacterichlorophyll, bacteriopheophytins, ubiquinone and no-heme ferrous iron. The net result of electron tranfer reactions is the establishment of proton electrochemical gradient and production of reducing equivalents in the form of NADH. Ultimately, the process results in the reduction of C02 to carbohydrates(C6H12O6) In non-oxygenic organisms, the electron donor is an organic acid rather than water. Much of our current functional understanding of photosynthesis comes from the structural determination and spectroscopic studies on the reaction center of Rhodobacter sphaeroides [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]
MVGGALFGHFDLAQLVIYAFWIFLAGLIYYLRREDRREGYPLENPDGLVKLAPNQGQVFPLPYPKTFVLP
HGRTVTVPRREPETREIKLARTAVFEGAPFQPTGNPMVDAVGPASYAERRELPDLTVHGHNKIVPLRVAT
DFSVAAGDVDPRGLPVVAADGEVAGKVTDLWVDRPEQYFRYLEVELAGGARTALLPMGMCKVKSDRVVVN
SILSDLFANVPTIKSPDQITLREEDKVSAYYAGGLLYATPER
>gnl|CDD|130221 TIGR01151, Photosystem_QB_protein, photosystem II, DI subunit (also called Q(B)). This model describes the Photosystem II, DI subunit (also called Q(B)) in bacterial and its equivalents in chloroplast of algae and higher plants. Photosystem II is many ways functionally equivalent to bacterial reaction center. At the core of Photosystem II are several light harvesting cofactors including plastoquinones, pheophytins, phyloquinones etc. These cofactors are intimately associated with the polypeptides, which principally including subunits DI, DII, Cyt.b, Cyt.f and iron-sulphur protein. Together they participate in the electron transfer reactions that lead to the net production of the reducting equivalents in the form of NADPH, which are used for reduction of CO2 to carbohydrates(C6H1206). Phosystem II operates during oxygenic photosynthesis and principal electron donor is H2O. Although no structural data is presently available, a huge body of literature exits that describes function using a variety of biochemical and biophysical techniques [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]
MTATLQRRESASLWERFCEWITSTENRLYIGWFGVLMIPTLLTATSCFIIAFIAAPPVDIDGIREPVAGS
LLYGNNIISGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLIVFHFLLGVACYMGREWELSYRLGMR
PWICVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSL
FSAMHGSLVTSSLIRETTENESANYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPV
VGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLASGEVAP
VALTAPAING
>gnl|CDD|130222 TIGR01152, Photosystem_II_D2_protein, Photosystem II, DII subunit (also called Q(A)). This model describes the Photosystem II, DII subunit (also called Q(A)) in bacterial and its equivalents in chloroplast of algae and higher plants. Photosystem II is in many ways functionally equivalent to bacterial reaction center. At the core of Photosystem II are several light harvesting cofactors including plastoquinones, pheophytins, phyloquinones etc. These cofactors are intimately associated with the polypeptides, which principally including subunits DI, DII, Cyt.b, Cyt.f and iron-sulphur protein. Together they participate in the electron transfer reactions that lead to the net production of the reducting equivalents in the form of NADPH, which are used for reduction of CO2 to carbohydrates(C6H1206). Phosystem II operates during oxygenic photosynthesis and principal electron donor is H2O. Although no high resolution X-ray structural data is presently available, recently a 3D structure of the supercomplex has been described by cryo-electron microscopy. Besides a huge body of literature exits that describes function using a variety of biochemical and biophysical techniques [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]
MTIAIGRTKEERGLFDVLDDWLKRDRFVFVGWSGLLLFPCAYFALGGWFTGTTFVTSWYTHGLASSYLEG
CNFLTAAVSTPANSMGHSLLLLWGPEAQGDFTRWCQLGGLWTFVALHGAFGLIGFMLRQFEIARLVGLRP
YNAIAFSGPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALL
CAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLW
MSAIGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHENFIFPEEVLPRGN
AL
>gnl|CDD|213589 TIGR01153, psbC, photosystem II 44 kDa subunit reaction center protein (also called P6 protein, CP43), bacterial and chloroplast. This model describes the Photosystem II, 44kDa subunit (also called P6 protein, CP43) in bacterial and its equivalents in chloroplast of algae and higher plants. Photosystem II is in many ways functionally equivalent to bacterial reaction center. At the core of Photosystem II are several light harvesting cofactors including plastoquinones, pheophytins, phyloquinones etc. These cofactors are intimately associated with the polypeptides, which principally including subunits 44 kDa protein,DI, DII, Cyt.b, Cyt.f, iron-sulphur protein and others. Functinally 44 kDa subunit is imlicated in chlorophyll binding. Together they participate in the electron transfer reactions that lead to the net production of the reducting equivalents in the form of NADPH, which are used for reduction of CO2 to carbohydrates(C6H1206). Phosystem II operates during oxygenic photosynthesis and principal electron donor is H2O. Although no high resolution X-ray structural data is presently available, recently a 3D structure of the supercomplex has been described by cryo-electron microscopy. Besides a huge body of literature exits that describes function using a variety of biochemical and biophysical techniques [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]
YAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMTLFEVAHFTFDKPMYEQGLILMPHVATLGWGVGPG
GEVVDIFPFFVVGVLHLISSAVLGFGGIYHSLRGPEKLEEYSSFFGYDWKDKNQMTNILGYHLILLGIGA
LLLVAKACFFGGIYDTWAPGGGDVRLITNPTLDPRVIFGYLLKSPFGGEGWIISVNNMEDIIGGHIWIGL
TCIAGGIWHILTKPFGWARRAFIWSGEAYLSYSLGALSLMGFIASAYVWFNNTAYPSEFYGPTNAEASQA
QSFTFLVRDQRLGANIGSAQGPTGLGKYLMRSPTGEIIFGGETMRFWDFRGPWLEPLRGPNGLSLDKIQN
DIQPWQVRRAAEYMTHAPNGSLNSVGGVITEPNSVNFVSPRQWLAGSHFVLGFFFLVGHLWHAGRARAAA
AGFEKGIDRKTE
>gnl|CDD|130224 TIGR01156, Cytochrome_b6-f_complex_subunit_4, cytochrome b6/f complex subunit IV. This model describes the subunit IV of the cytochrome b6/f complex. The cyt b6/f complex is central to the functions of the oxygenic phosynthetic electron transport in cyanobacteria and its equivalents in algae and higher plants. Energetically, on the redox scale the cytb6/f complex is placed below the other components - Q(A); Q(B) of the photosystem II in the Z-scheme, along the pathway of the electron transport. The complex is made of the following subunits: cytochrome f; cytochrome b6; Rieske 2Fe-2S; and subunits IV; V; VI; VII. Subunit IV is one of the principal subunits for the binding of the redox prosthetic groups. Each monomer of the complex contains a molecule of chlorophyll a and beta-carotene [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]
MSVTKKPDLSDPVLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACVVGLAVLDPAMIGEPANPFA
TPLEILPEWYFYPVFQILRTVPNKLLGVLLMAAVPAGLLTVPFIENVNKFQNPFRRPVATTVFLFGTVVA
LWLGIGATLPIDKSLTLGL
>gnl|CDD|130225 TIGR01157, photosynthetic_reaction_center_L_subunit, photosynthetic reaction center L subunit. This model describes the photosynthetic reaction center L subunit in non-oxygenic photosynthetic bacteria. Reaction center is an integral membrane pigment-protein that carries out light-driven electron transfer reactions. At the core of reaction center is a collection light-harvesting cofactors and closely associated polypeptides. The core protein complex is made of L, M and H subunits. The common cofactors include bacterichlorophyll, bacteriopheophytins, ubiquinone and no-heme ferrous iron. The net result of electron tranfer reactions is the establishment of proton electrochemical gradient and production of reducing equivalents in form of NADH. Ultimately the process results in the reduction of C02 to carbohydrates(C6H12O6) In non-oxygenic organisms, the electron donor is some organic acid and not water. Much of our current functional understanding of photosynthesis comes from the structural determination, spectroscopic studies and mutational analysis on the reaction center of Rhodobacter sphaeroides [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]
FGVTTVFFAALGTALIVWAAALGPTWNPWLISINPPDLEYGLGFAPLAKGGLWQIITICATGAFVSWALR
EVEICRKLGIGYHIPFAFSFAILAYLTLVVIRPVMMGAWGYAFPYGIWTHLDWVSNTGYQYGNFHYNPAH
MIAISFFFTNALALALHGGLVLSAANPGKGEEVKTPEHEDTYFRDLVGYSVGTLGIHRVGLFLALSAVFW
SAICMIISGPIYFDSWPDWWEWWVKLPFW
>gnl|CDD|273471 TIGR01158, Protein_translation_factor_SUI1_homolog, translation initation factor SUI1, putative, prokaryotic. This family of archaeal and bacterial proteins is homologous to the eukaryotic translation intiation factor SUI1 involved in directing the ribosome to the proper start site of translation by functioning in concert with eIF-2 and the initiator tRNA-Met [Protein synthesis, Translation factors]
LVYSTECGLPKELCEEVAKPKEDQVVRIQRETRGRKGKGVTIIEGLDLSDIDLKELAKELKSKCGCGGTV
KDGVIEIQGDHRDRVKDLLEKKGFKVKLIGG
>gnl|CDD|273472 TIGR01159, DRP1, density-regulated protein DRP1. This protein family shows weak but suggestive similarity to translation initiation factor SUI1 and its prokaryotic homologs
PLRVLYCGVCSLPPEYCEFSGDLKRCKVWLSENAPDLYAKLYGTDSPTAEAEAVTIGEAQEEKGEKDLLG
IQKAQEAREGGKKKKKLPQKVTIKREPRTKRKFVTVIKGLETFDIDLKKASKTFAQKFATGCSVSKSVTG
KEEIVIQGDVMDDIEDYIHEKWPEVGDKDIKDL
>gnl|CDD|130228 TIGR01160, Eukaryotic_translation_initiation_factor_1, translation initiation factor SUI1, eukaryotic. Alternate name: MOF2. A similar protein family (see TIGRFAMs model TIGR01158) is found in prokaryotes. The human proteins complements a yeast SUI1 mutatation [Protein synthesis, Translation factors]
SIQNLKSFDPFADAGDDDSALPGTSNYIHIRIQQRNGRKTLTTVQGLPKEYDLKKIVKALKKEFACNGTV
IEDPEMGEVIQLQGDQRKNVCEFLISQGLLKKDQIKIHGF
>gnl|CDD|273473 TIGR01161, N5-carboxyaminoimidazole_ribonucleotide_synthase, phosphoribosylaminoimidazole carboxylase, PurK protein. Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, N5-carboxyaminoimidazole ribonucleotide synthetase, which hydrolyzes ATP and converts AIR to N5-CAIR. PurE converts N5-CAIR to CAIR. In the presence of high concentrations of bicarbonate, PurE is reported able to convert AIR to CAIR directly and without ATP [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
TVGILGGGQLGRMLALAARPLGIKVHVLDPDANSPAVQVADHVVLAPFFDPAAIRELAESCDVITFEFEH
VDVEALEKLEARGVKLFPSPDALAIIQDRLTQKQFLQKLGLPVPPFLVIKDEEELDAALQELGFPVVLKA
RTGGYDGRGQYRIRNEADLPQAAKELGDRECIVEEFVPFERELSVIVARSADGETAFYPVVENIHQDGIL
RYVVAPAAVPDAIQARAEEIARRLMEELGYVGVLAVEMFVLPDGRLLINELAPRVHNSGHYTLDGCSTSQ
FEQHLRAILGLPLGSTELLLPSVMVNLLGTEDDVIPLWEEILALPGAKLHWYGKAEVRPGRKVGHVNLVG
SD
>gnl|CDD|273474 TIGR01162, N5-carboxyaminoimidazole_ribonucleotide_mutase, phosphoribosylaminoimidazole carboxylase, PurE protein. Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, an N5-CAIR mutase [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
VGIIMGSDSDLPTMKKAADILEEFGIPYELRVVSAHRTPELMLEYAKTAEERGIKVIIAGAGGAAHLPGM
VAALTPLPVIGVPVPSKALSGLDSLLSIVQMPSGVPVATVAIGNAGNAALLAAQILGIKDPELAEKLKEY
RENQKEEVLKKNKKLE
>gnl|CDD|273475 TIGR01163, Ribulose-phosphate_3-epimerase, ribulose-phosphate 3-epimerase. This family consists of Ribulose-phosphate 3-epimerase, also known as pentose-5-phosphate 3-epimerase (PPE). PPE converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. It has been found in a wide range of bacteria, archebacteria, fungi and plants [Energy metabolism, Pentose phosphate pathway]
IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDR
YIEDFAEAGADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFG
GQKFIPDTLEKIREVRKMIDELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR
>gnl|CDD|273476 TIGR01164, 50S_ribosomal_protein_L16, ribosomal protein L16, bacterial/organelle. This model describes bacterial and organellar ribosomal protein L16. The homologous protein of the eukaryotic cytosol is designated L10 [Protein synthesis, Ribosomal proteins: synthesis and modification]
SPKRTKYRKQQRGRVKGKAKRGNTVAFGEYGLQALEPGWITARQIEAARVAMTRYVKRGGKLWIRIFPDK
PYTKKPLETRMGKGKGNPEYWVAVVKPGKILFEIAGVPEEVAREAFRLAASKLPI
>gnl|CDD|273477 TIGR01165, Cobalt_transport_protein_CbiN, cobalt transport protein. This model describes the cobalt transporter in bacteria and its equivalents in archaea. It principally functions in the ion uptake mechanism. It is a multisubunit transporter with two integral membrane proteins and two closely associated cytoplasmic subunits. This transporter belongs to the ABC transporter superfamily (ATP stands for ATP Binding Cassette). This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux [Transport and binding proteins, Cations and iron carrying compounds]
MSMKKTIWLLAAVAALVVLPLLIYAGKGEEEEYGGADGQAEEVIEEIGPDYKPWFSPLWEPPSGEIESLL
FALQAALGALVIGYVIGYYRG
>gnl|CDD|130234 TIGR01166, membrane_associated_cobalt_transport_protein_CbiO, cobalt transport protein ATP-binding subunit. This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux [Transport and binding proteins, Cations and iron carrying compounds]
YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRV
GLVFQDPDDQLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAG
AVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA
>gnl|CDD|273478 TIGR01167, Zinc_metalloprotease_ZmpB, LPXTG-motif cell wall anchor domain. This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region [Cell envelope, Other]
KLPKTGESGNSLLLLLGLLLLGLGGLLLRKRKKK
>gnl|CDD|273479 TIGR01168, M_protein_serotype, Gram-positive signal peptide, YSIRK family. Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus
AKKFNEKQQKYSIRKLSVGVASVLVASLFFGGGVAAAES
>gnl|CDD|211630 TIGR01169, 50S_ribosomal_protein_L1, ribosomal protein L1, bacterial/chloroplast. This model describes bacterial (and chloroplast) ribosomal protein L1. The apparent mitochondrial L1 is sufficiently diverged to be the subject of a separate model [Protein synthesis, Ribosomal proteins: synthesis and modification]
KLSKRYRAAREKVDRNKLYSLDEAIDLLKETATAKFDETVEVAIRLGIDPRKSDQQVRGSVVLPHGTGKT
VRVAVFAKGEKAKEAKAAGADYVGSDDLIEKIKKGWLDFDVVIATPDMMRVVGKLGRILGPRGLMPNPKT
GTVTTDVAKAVKNAKKGQVEFRADKAGNIHAPIGKVSFDSEKLKENLEALLDAIKKAKPSGAKGQYIKNI
ALSSTMGPGIKVDLNSL
>gnl|CDD|273480 TIGR01170, 60S_ribosomal_protein_L1_mitochondrial, ribosomal protein uL1, mitochondrial. This model represents the mitochondrial homolog of bacterial ribosomal protein L1. Unlike chloroplast L1, this form was not sufficiently similar to bacterial forms to include in a single bacterial/organellar L1 model [Protein synthesis, Ribosomal proteins: synthesis and modification]
YKVIKAFVYLKTKSISMYVPKQSVNLDIGLLMELGKESVQGMFSFPHPFGKEPKIAVFTKGASEVEEARE
AGADYVGGDDLIKKIEDGEIKPFDYLIAHPDIVPELAQLRRLLGPKGLMPSPKRGTVGDNLLSMIETFKK
G
>gnl|CDD|273481 TIGR01171, 50S_ribosomal_protein_L2, ribosomal protein L2, bacterial/organellar. This model distinguishes bacterial and organellar ribosomal protein L2 from its counterparts in the archaea nad in the eukaryotic cytosol. Plant mitochondrial examples tend to have long, variable inserts [Protein synthesis, Ribosomal proteins: synthesis and modification]
IKKYKPTTPGRRGAVVSDFAEITKGKPEKSLLEKLHKTGGRNNRGRITSRHRGGGHKRLYRIIDFKRDKD
GIPAKVATIEYDPNRSARIALLHYADGEKRYILAPKGLKVGDTVISGPEAPIKPGNALPLRNIPVGTTVH
NIELKPGKGGQLARSAGTSAQILAKEGKYVTLRLPSGEMRMVLKECRATIGEVGNEDHNNIVLGKAGRSR
WLGIRPTVRGVAMNPVDHPHGGGEGRTPIGRHPVTPWGKPTKGYKTRKKKKYSDKFIVRRRKK
>gnl|CDD|200082 TIGR01172, Serine_acetyltransferase, serine O-acetyltransferase. Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARI
GRGVFIDHGTGVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKI
GANSVVLKDVPPGATVVGVPAR
>gnl|CDD|273482 TIGR01173, Bifunctional_glmU_protein_., UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase. This protein is a bifunctional enzyme, GlmU, which catalyzes last two reactions in the four-step pathway of UDP-N-acetylglucosamine biosynthesis from fructose-6-phosphate. Its reaction product is required from peptidoglycan biosynthesis, LPS biosynthesis in species with LPS, and certain other processes [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars]
LSVVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVIDAARALGPQKIHVVYGHGAEQVRKALANRDVNWVL
QAEQLGTGHAVLQALPFLSDDGDVLVLYGDVPLISAETLERLLEAHRQNGITLLTAKLDDPTGYGRIIRE
NDGKVTAIVEDKDANAEQKAIKEINTGVYVFDGAALKRWLPKLSNNNAQGEYYLTDVIALAVADGETVRA
VQVDDSDEVLGVNDRLQLAQLERILQRRIAKKLLLAGVTLRDPARFDIRGTVEIGRDVEIDPNVILEGKV
KIGDDVVIGPGCVIKNSVIGSNVVIKAYSVLEGSEIGEGCDVGPFARLRPGSVLGAGVHIGNFVEVKNAR
IGKGSKAGHLSYLGDAEIGSNVNIGAGTITCNYDGANKHKTIIGDGVFIGSNTQLVAPVKVGDGATIAAG
STVTKDVPEGALAISRARQRNIEGWVRPKKK
>gnl|CDD|273483 TIGR01174, Cell_division_protein_FtsA, cell division protein FtsA. This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70 [Cellular processes, Cell division]
LIVGLDIGTSKICAIVAEVLEDGELNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRS
VIVSISGAHIKSQNSIGVVAIKDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLG
MSGVRLEVEVHIITGSSTILRNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDI
AVYTGGSIRYTKVIPIGGNHITKDIAKALRTPLEEAERIKIKYGCASIPLEGPDENIEIPSVGERPPRSL
SRKELAEIIEARAEEILEIVKQKELRKSGFKEELNGGIVLTGGGAQLEGIVELAEKVFDNPVRIGLPQNI
GGLTEDVNDPEYSTAVGLLLY
>gnl|CDD|273484 TIGR01175, pilM, type IV pilus assembly protein PilM. This protein is required for the assembly of the type IV fimbria in Pseudomonas aeruginosa responsible for twitching motility, and for a similar pilus-like structure in Synechocystis. It is also found in species such as Deinococcus described as having natural transformation (for which a type IV pilus-like structure is proposed) but not fimbria
KKSLLVGIDIGSTSVKVAQLKRSGDRYKLEHYAVEPLPAGIFTEGHIVEYQAVAEALKELLSELGINTKK
AATAVPGSAVITKVIPVPAGLDERELEFAVYIEASHYIPYPIEEVSLDFEKLGLKANNPESTVQVLLAAT
RKEVVDSRLHALKLAGLEPKVVDVESFALLRAWRLLGEQLASRTYRLTDAALVDIGATSSTLNLLHPGRM
LFTREVPFGTRQLTSELSRAYGLNPEEAGEAKQQGGLPLLYDPEVLRRFKGELVDEIRRSLQFFTAQSGT
NSLDGLVLAGGGATLSGLDAAIYQRLGLPTEVANPFALMALDAKVDAGRLAVDAPALMTALGLALRGF
>gnl|CDD|273485 TIGR01176, Fumarate_reductase_flavoprotein_subunit., fumarate reductase (quinol), flavoprotein subunit. The terms succinate dehydrogenase and fumarate reductase may be used interchangeably in certain systems. However, a number of species have distinct complexes, with the fumarate reductase active under anaerobic conditions. This model represents the fumarate reductase flavoprotein subunit from several such species in which a distinct succinate dehydrogenase is also found. Not all bona fide fumarate reductases will be found by this model
TAQHDIAVIGAGGAGLRAAIAAAEANPHLDVALISKVYPMRSHTVAAEGGSAAVTGDDDSLDEHFHDTVS
GGDWLCEQDVVEYFVAEAPKEMVQLEHWGCPWSRKPDGRVNVRRFGGMKKERTWFAADKTGFHMLHTLFQ
TSLTYPQIMRYDEWFVTDLLVDDGRVCGLVAIEMAEGRLVTILADAVVLATGGAGRVYPFNTNGGIVTGD
GMAMAFRHGVPLRDMEFVQYHPTGLPGTGILMTEGCRGEGGILVNKDGYRYLQDYGMGPETPVGEPKNKY
MELGPRDKVSQAFWHEHNKGNTIDTPYGDVVYLDLRHLGEDLLDERLPFICELAKAYVHVDPVKEPIPVR
PTVHYTMGGIETDINCETRIKGLFAVGECASVGLHGANRLGSNSLAELVVFGRRAGEAAAERAARHQKSN
ESAIRAQARTVELRLERLLSQHGGENWADIRAEMGATMESGCGIYRDGPLMQKTIDKLAELQERFKRAGI
DDHSRVFNTDLLYLIELGGGLDVAEAMVHSALRRKESRGAHQRLDEGCTERDDVHFLKHTLAFRESDGTL
RVGYSPVKITRWPPGERVYG
>gnl|CDD|273486 TIGR01177, tRNA_guanine10-N2-dimethyltransferase, putative methyltransferase, TIGR01177 family. This family of probable methyltransferases is found exclusively in the Archaea [Hypothetical proteins, Conserved]
FYVELSGEHPELPLAELKALAEVYGRVGDVEGVDRGLAIISAPIIDILERLAFTHEVGRSYDTCAAKDLY
DFVAGLEASDLDRKSFAVRVRDLRGYSVDKARLERKIGAILKKKGFKVSLRRPDIVVRVVITEDIFYLGR
VLEERDKEQFIERKPDRRPFFKPGSMDPKLARAMVNLARVTEGDRVLDPFCGTGGFLIEAGLMGAKVIGC
DIDWKMVAGARINLEHYGIEDFFVKRGDATKLPLSSESVDAIATDPPYGRSTTAAGDGLESLYERSLEEF
HEVLKSEGWIVYAVPTRIDLESLAEDAFRVVKRFEVRVHRSLTRHIYVA
>gnl|CDD|130246 TIGR01178, Adenine_deaminase, adenine deaminase. The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
DIVIKNAKIIDVYNGEIIPGDIAIANGHIAGVGKYNGVKVIDALGEYAVPGFIDAHIHIESSMLTPSEFA
KLVLPHGVTTVVSDPHEIANVNGEDGINFMLNNAKKTPLNFYFMLPSCVPALQFETSGAVLTAEDIDELM
ELDEVLGLAEVMDYPGVINADIEMLNKINSARKRNKVIDGHCPGLSGKLLNKYISAGISNDHESTSIEEA
REKLRLGMKLMIREGSAAKNLEALHPLINEKNCRSLMLCTDDRHVNDILNEGHINHIVRRAIEHGVDPFD
ALQMASINPAEHFGIDVGGLIAPGDPADFVILKDLRNFKVNKTYVKGKLLDLNEVFNDEISRIPLINEIP
INVKARSPKSISDFGIQFKTGNRIRVIKVISNQLITHKTSNSVAEEFGSDIEEDILKIAVIERHKDNGKI
GKGLIKGFGLKEGAIASTVAHDSHNIIAVGSNDEDLALAVNKLIQIGGGLCAAKNGEVTIILPLPIAGLM
SDDSAERVAEQIIALNDKCRNVGGSRDNPFLTLSFLSLPVIPHLKITDKGLFDVESFCFVDL
>gnl|CDD|273487 TIGR01179, UDP-glucose_4-epimerase, UDP-glucose-4-epimerase GalE. Alternate name: UDPgalactose 4-epimerase This enzyme interconverts UDP-glucose and UDP-galactose. A set of related proteins, some of which are tentatively identified as UDP-glucose-4-epimerase in Thermotoga maritima, Bacillus halodurans, and several archaea, but deeply branched from this set and lacking experimental evidence, are excluded from this model and described by a separate model [Energy metabolism, Sugars]
KILVTGGAGYIGSHTVRQLLESGHEVVILDNLSNGSREALPRGERITPVTFVEGDLRDRELLDRLFEEHK
IDAVIHFAGLIAVGESVQKPLKYYRNNVVGTLNLLEAMQQAGVKKFIFSSSAAVYGEPSSIPISEDSPLG
PINPYGRSKLMSEQILRDLQKADPDWSYVILRYFNVAGAHPSGDIGEDPPGITHLIPYACQVAVGKRDKL
TIFGTDYPTPDGTCVRDYIHVMDLADAHLAALEYLLNGGGSHVYNLGYGQGFSVLEVIEAFKKVSGKDFP
VELAPRRPGDPASLVADASKIRRELGWQPKYTDLEEIIKDAWRWESRN
>gnl|CDD|273488 TIGR01180, immunoreactive_89kD_antigen_PG87, alpha-1,2-mannosidase, putative. The identification of members of this family as putative alpha-1,2-mannosidases is based on an unpublished characterization of the aman2 gene in Bacillus sp. M-90 by Maruyama,Y., Nakajima,M. and Nakajima,T. (Genbank accession BAA76709, pid g4587313). Most members of this family appear to have signal sequences. Members from the dental pathogen Porphyromonas gingivalis have been described as immunoreactive with periodontitis patient serum [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
MDPPMPILYIVLIFAILCLFVGRALFAQSYDDYVTPYVNPLIGTELNTYGVTGPGAGLPNGMPMTGPPND
GWQYTYSYHKIRGFKQGFSHTPLSGDGAQFLSLILTMPQSPSSALTKWPTDWFSHKASTANEYARSGYYA
VYLDRVGIAVTETATERRAIYRGNFESGSGRWLLLLASTGGSEISIVDPHTVVGTISGYRGGFPANFACY
FRLFFDTPMSDVLLETTTGSSDEGTRAWAAQRFGYQLVTVRDLAGTDLASSFASSEVSEANAAENLGQEF
QARIFLAGREAWNKVWGRALGEVGTEGGTTTFYTIFYTALYHPLRFPEEDSDANGVYYSPDNGEHLPGYL
YDTYTWDSLWDTYRAVHPLYPLLNPEIQEDMVNSYIEMGFFSGWLPPWHRDCGETGNMSGSHSIDVILDA
YRKGLTRFNMNGAYHATKAVHPKISSTGRKPWRTDNDLYYVLGYVPADEQAARSLSYALEYAYDDWCLSR
LAWDRAAHDTLAHRFMNRSHLYRHEYNLERGFFQPGLFRGPFSPPFDPFEFTEGNAEHNAWSYFFDVQHD
IDGLGGLMGGASMFDSRLDTPFMTPYGSVIHEIRESQIADMTGYAGQYQPINEPSYHYPYLYHYWKQPWR
TQKLIRRLYRETFDNYPGGLPGNEDSGWLSAWAVFSMLGFYPVDPGSPGYPIGSPVFLSVTIGLPTGLHA
PATAADTPYINSYIVEVKLWGKPYLTHEILHSDISIGGHLELKMNYRPGM
>gnl|CDD|273489 TIGR01181, dTDP-glucose_46-dehydratase_2, dTDP-glucose 4,6-dehydratase. This protein is related to UDP-glucose 4-epimerase (GalE) and likewise has an NAD cofactor [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
RILVTGGAGFIGSNFVRYILNEHPDAEVIVLDKLTYAGNLENLADLEDNPRYRFVKGDIGDRELVSRLFT
EHQPDAVVHFAAESHVDRSISGPAAFIETNVVGTYTLLEAVRKYWHEFRFHHISTDEVYGDLEKGDAFTE
TTPLAPSSPYSASKAASDHLVRAYHRTYGLPALITRCSNNYGPYQFPEKLIPLMITNALAGKPLPVYGDG
QQVRDWLYVEDHCRAIYLVLEKGRVGETYNIGGGNERTNLEVVETILELLGKDEDLITHVEDRPGHDRRY
AIDASKIKRELGWAPKYTFEEGLRKTVQWYLDNEWWW
>gnl|CDD|273490 TIGR01182, KHG/KDPG_aldolase_., Entner-Doudoroff aldolase. 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an enzyme of the Entner-Doudoroff pathway. This aldolase has another function, 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) shown experimentally in Escherichia coli and Pseudomonas putida [Amino acid biosynthesis, Glutamate family, Energy metabolism, Entner-Doudoroff]
IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNP
EQLRQAVAAGAQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLK
ALAGPFPQVRFCPTGGINLANARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALEII
>gnl|CDD|130251 TIGR01183, Nitrate_transport_permease_protein_NrtB, nitrate ABC transporter, permease protein. This model describes the nitrate transport permease in bacteria. This is gene product of ntrB. The nitrate transport permease is the integral membrane component of the nitrate transport system and belongs to the ATP-binding cassette (ABC) superfamily. At least in photosynthetic bacteria nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA, ntrB, ntrC, ntrD, narB. Functionally ntrC and ntrD resemble the ATP binding components of the binding protein-dependent transport systems. Mutational studies have shown that ntrB and ntrC are mandatory for nitrate accumulation. Nitrate reductase is encoded by narB [Transport and binding proteins, Anions]
ILYPFFDNGGTDKGLFWQIIASLTRVAVGFSIAAIIGIAVGILIGLSKFLNAALDPIFQVLRTIPPLAWL
PIALAAFQDAQPAAIFVIFITAIWPIIINTAVGVQQIPQDYNNVARVLKLSKSDYFLKVLLPAAVPYIFT
GLRIAIGLSWLAIVAAEMLMGGVGIGFFIWDAYNSGSVSEIILAIIYVGLVGLLLDRFVAWL
>gnl|CDD|130252 TIGR01184, Nitrate_transport_ATP-binding_protein_NrtC, nitrate transport ATP-binding subunits C and D. This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase [Transport and binding proteins, Anions, Transport and binding proteins, Other]
LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLT
VRENIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE
PFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVPFPRPRDR
LEVVEDPSYYDLRNEALYFL
>gnl|CDD|130253 TIGR01185, membrane_spanning_subunit, DevC protein. This model describes a predicted membrane subunit, DevC, of an ABC transporter known so far from two species of cyanobacteria. Some experimental data from mutational analysis suggest that this protein along with DevA and DevB encoded in the same operon may be involved in the transport/export of glycolipids [Transport and binding proteins, Other]
IPLSWLQLTREKTRLAVALAGIAFADILMFMQIGFRDALYYSNVRLHTSLQGDIVLLNKQSNAVLAMKPF
SQRRLYKSLELPSVQSVHPIYLDYSIWKNPYTGLTRSILVFGINPETNIINLAGVQENLDKLKLPDVVLF
DRSSRPEYGPIAKNFEQGQSISAEVRRRRINVVGLFTLGASFGADGNLVTSDVNFLRLFPLRRQGLIDIG
LLRLKPGVNPNTAVQELRSYLPDDINVLTKQEFIDFERNYWASSTAIGFIFTLGTIMGFIVGTVIVYQIL
YTEVADHLSEYATLKAIGYTQKYLLGVILQEALLLACLGYLPGWGFAILLYTTARQATLLPVFMSYDRAI
TVLILTMIMCFVSGSIAVRKLRSADPADIF
>gnl|CDD|130254 TIGR01186, Choline_transport_ATP-binding_protein_OpuBA, glycine betaine/L-proline transport ATP binding subunit. This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature [Transport and binding proteins, Amino acids, peptides and amines]
KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRR
KKIGMVFQQFALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGL
ARALAAEPDILLMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQ
VGTPDEILRNPANEYVEEFIGKVDLSQVFDAERIAQRMNTGPITKTADKGPRSALQLMRDERVDSLYVVD
RQNKLVGVVDVESIKQARKKAQGLQDVLIDDIYTVDAGTLLRETVRKVLKAGIKVPVVDEDQRLVGIVTR
GSLVDALYDSREG
>gnl|CDD|162242 TIGR01187, potA, spermidine/putrescine ABC transporter ATP-binding subunit. This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included) [Transport and binding proteins, Amino acids, peptides and amines]
LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMR
KVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQ
LELKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEAT
VIERKSEQVVLAGVEGRRCDIYTDVPVEKDQPLHVVLRPEKIVIEEEDEANSSNAIIGHVIDITYLGMTL
EVHVRLETGQKVLVSEFFNEDDPHMSPSIGDRVGLTWHPGSEVVL
>gnl|CDD|130256 TIGR01188, drrA, daunorubicin resistance ABC transporter ATP-binding subunit. This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc [Transport and binding proteins, Other]
KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGI
VPQYASVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLI
HQPDVLFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE
LKRRLGKDTLESRPRDIQSLKVEVSMLIAELGETGLGLLAVTVDSDRIKILVPDGDETVPEIVEAAIRNG
IRIRSISTERPSLDDVFLKLTG
>gnl|CDD|273491 TIGR01189, ccmA, heme ABC exporter, ATP-binding protein CcmA. This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE
PHENILYLGHLPGLKPELSALENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALAR
LWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEARELRL
>gnl|CDD|200083 TIGR01190, Heme_exporter_protein_B, heme exporter protein CcmB. This model describes the cyt c biogenesis protein encoded by ccmB in bacteria. Bacterial c-type cytochromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome C [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
LIRRDLRLAFRAGGGILNPLWFFLIVVTLFPFGVGPELKLLSRIAPGIVWVGALLSSLLSLDRLFRDDFE
DGSLDLLALSPTPLELTVLAKVLAHWLVTGLPLVLLSPLLALLLNLDVPAWGALALTLLLGTPALSFLGA
IGAALTVGLKRGGLLLSLLVLPLYIPVLIFGSAAIQAAAEGLPFGGPLAILAALTLATVTLAPFAAAAAL
R
>gnl|CDD|273492 TIGR01191, Heme_exporter_protein_C, heme exporter protein CcmC. This model describes the cyt c biogenesis protein encoded by ccmC in bacteria. It must be noted an arabidopsis, a tritcum and a piscum plant proteins were recognizable in the clade. Quite likely they are of organellar origin. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes, ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in the heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
PVDYQQGASVRIMYVHVPAAWMAIGVYIMMAIASFIFLVWKHPLSDLAAKAAAPIGAVFTLIALVTGSLW
GKPMWGTWWVWDARLTSVLILFLLYLGYLALWEAIDNRDSAAKAAGILCLVGVVNIPIIKFSVEWWNTLH
QPASITRFGSPSIHVSMLIPLLLMFAGFLLLFLALLLLRTRLEI
>gnl|CDD|130260 TIGR01192, protein_chvA_Attachment_protein., glucan exporter ATP-binding protein. This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MSLFQVYVRALSYLNVHKNRVLLIVIANITLAAITIAEPILFGRIIDAISSKSDVLPTLALWAGFGVFNT
IAYVLVAREADRLAHGRRATLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLAT
FVALFLLIPTAFAMDWRLSIVLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHS
YNRIEAETSALKQFTNNLLSAQYPVLDWWALASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIG
FANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPELPNVKGAVEFRHITFEFANSSQG
VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGL
FNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNA
PILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKD
GRFYKLLRRSGLLTNQPATKPLRKA
>gnl|CDD|130261 TIGR01193, transport/processing_ATP-binding_protein, ABC-type bacteriocin transporter. This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
QVDEKDCGIAALSMILKKYGTEYSLAKLRQLAKTDLEGTTVLGLVKAAEYLNFEAKAIQADMSLFEDKNL
PLPFIAHVIKNGKLPHYYVVYGVTKNHLIIADPDPTVGITKISKEDFYEEWTGIAIFISPTPEYKPIKEK
ENSLLKFIPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQ
ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDM
WILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSL
TSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNAL
LSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNIL
SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIF
SGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDS
KVLILDESTSNLDTITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG
FYASLIHN
>gnl|CDD|130262 TIGR01194, ATP-binding_protein_SyrD, cyclic peptide transporter. This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
KKAAIGEILALLRSPFPAITAFSIALGLAGGLAIIALLASINNAIHEENFLGQGSLFSFGGLCLLALLFR
IGADIFPAYAGMHIIANLRIALCEKILGAPIEEIDRRGAHNLIPLLTHDIDQINAFLFIFPPIAIALAIF
FFCIAYLAYLSVPMFAITISAIIIGTAAQLLAFMGGFKFFHAARDEEDAFNEHTHAIAFGAKELKIHGIR
RLSFAHGAIQESANNIADLHIIEILIFIAAENFGQLLFFLLIGCALFAAAMFASIDAAAISAFVLALLYI
KGPLEMLVSALPILAQAQIACQRLADFGERFNEPEPELELSDADNVLLLAHDKSVDSIELKDVHMNPKAP
EGSEGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDYRDLFSA
IFADFHLFDDLIGPDEGEHASLDNAQQYLQRLEIADKVKIEDGGFSTTTALSTGQQKRLALICAWLEDRP
ILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHDDQYFELADQIIKLAAGCIVKDTECA
>gnl|CDD|273493 TIGR01195, Oxaloacetate_decarboxylase_gamma_chain, sodium pump decarboxylases, gamma subunit. This model finds the subfamily of distantly related, low complexity, hydrophobic small subunits of several related sodium ion-pumping decarboxylases. These include oxaloacetate decarboxylase gamma subunit and methylmalonyl-CoA decarboxylase delta subunit. Most sequences scoring between the noise and trusted cutoffs are eukaryotic sodium channel proteins
NSLLLEGATLTVLGMGIVFLFLSLLIYAVRGMGKVVGRKKVPEPPASAKKSKKAAVPAVQDEDEELVAAI
AAAVHEHLRKTA
>gnl|CDD|130264 TIGR01196, Phosphogluconate_dehydratase, 6-phosphogluconate dehydratase. A close homolog, designated MocB (mannityl opine catabolism), is found in a mannopine catabolism region of a plasmid of Agrobacterium tumefaciens. However, it is not essential for mannopine catabolism, branches within the cluster of 6-phosphogluconate dehydratases (with a short branch length) in a tree rooted by the presence of other dehydyatases. It may represent an authentic 6-phosphogluconate dehydratase, redundant with the chromosomal copy shown to exist in plasmid-cured strains. This model includes mocB above the trusted cutoff, although the designation is somewhat tenuous [Energy metabolism, Entner-Doudoroff]
HSRLLEITERIIERSKPTRELYLERIRSAKTQGPHRSQLGCGNLAHGFAACPESDKMPLGSMKRPNLAII
TAYNDMLSAHQPFKNYPDLIKKALQEANAVAQVAGGVPAMCDGVTQGYDGMELSLFSRDVIAMSTAIGLS
HNMFDGALFLGVCDKIVPGLLIGALSFGHLPAVFVPSGPMVSGIPNKEKAKVRQLFAEGKVGREELLKSE
MASYHAPGTCTFYGTANSNQMMMEFMGLHLPGASFVNPNTPLRDALTREAAKRLARMTGNGGEVLPLGEM
IDEKSIVNALVGLMATGGSTNHTMHLVAMARAAGIILNWDDFSELSDLVPLLARVYPNGSADVNHFQAAG
GLPFLIRELLKAGLLHEDVHTVAGKGLSRYTKEPFLENGQLVWREAPEHSLDTDILRPVDDPFSANGGLK
LLKGNLGRAVIKISAVKPEHRVIEAPAIVFNDQAEVLAAFKAGELERDFVAVVRFQGPKANGMPELHKLT
PPLGVLQDRGFKVALVTDGRMSGASGKVPAAIHVTPEAALGGPIAKIRDGDLIRVDAVNGELNVLVDDAE
LNAREPETPDLSANSFGCGRELFASLRLNVSSAEEGAMSFG
>gnl|CDD|162246 TIGR01197, Natural_resistance-associated_macrophage_protein, NRAMP (natural resistance-associated macrophage protein) metal ion transporters. This model describes the Nramp metal ion transporter family. Historically, in mammals these proteins have been functionally characterized as proteins involved in the host pathogen resistance, hence the name - NRAMP. At least two isoforms Nramp1 and Nramp2 have been identified. However the exact mechanism of pathogen resistance was unclear, until it was demonstrated by expression cloning and electrophysiological techniques that this protein was a metal ion transporter. It was also independently demonstrated that a microcytic anemia (mk) locus in mouse, encodes a metal ion transporter (DCT1 or Nramp2). The transporter has a broad range of substrate specificity that include Fe+2, Zn+2, Mn+2, Co+2, Cd+2, Cu+2, Ni+2 and Pb+2. The uptake of these metal ions is coupled to proton symport. Metal ions are essential cofactors in a number of biological process including, oxidative phosphorylation, gene regulation and metal ion homeostasis. Nramp1 could confer resistance to infection in one of the two ways. (1) The uptake of Fe+2 can produce toxic hydroxyl radicals via Fenton reaction killing the pathogens in phagosomes or (2) Deplete the metal ion pools in the phagosome and deprive the pathogens of metal ions, which is critical for its survival [Transport and binding proteins, Cations and iron carrying compounds]
RKLWAFIGPGFLMSIAYIDPGNYSTDLQAGAAAGYKLLWVLLLSNIMALLLQRLCARLGVVTGLDLAEVC
REHYPKVPRITLWILAELAIIATDMAEVIGTAIALNLLSHIPLWGGVLITIVDVFLFLFLDKPGLRILEA
FVALLVTIVAICFAYELFYAKPGQVKVLFGGFVPSCAVFGTDGLLQAVGILGATVMPHSLYLHSALVQSR
LVDRDVKEGVSEANMYRPIEAAIALSVSFSINEFVIALFTAALFVNTNILVVAGATLFNSNNNADAADLF
SIGVLLGCLFSPAAGYIFAVGLLAAGQSSGMVGTYSGQFVMEGFLNWRWSPWLRRLITRAIAIIPCLLVA
AFGGREGLTGALNASQVVLSLLLPFALIPLIMFTSSKKIM
>gnl|CDD|273494 TIGR01198, 6-phosphogluconolactonase_6PGL., 6-phosphogluconolactonase. This enzyme of the pentose phosphate pathway is often found as a part of a multifunctional protein with [Energy metabolism, Pentose phosphate pathway]
VFSNSAELAEALAERIATKLQTALAERGQFSLALSGGRSPIALLEALAAQPLDWSRIHLFLGDERYVPLD
HADSNTGLAREALLDRVAIPASNIHPMPTELSDIEEAAELYEQELAAAFQPIVFPVFDLLLLGMGPDGHT
ASLFPHTPALQETERLVTVLTKSPKPPHERITLTLPAINAARKVFLLIAGEEKRNALAEALAVEAEPYPL
PAAGVLHSGKTLWLLDYAAARKL
>gnl|CDD|273495 TIGR01200, conserved_hypothetical_protein, GLPGLI family protein. This protein family was first noted as a paralogous set in Porphyromonas gingivalis, but it is more widely distributed among the Bacteroidetes. The protein family is now renamed GLPGLI after its best-conserved motif
KKLLLLLLLLLFAFSSAQQQITIRVTYELIYKKKDDTDKNKPETETMILQIGKNKSKFYSLTFNKNDSLF
KKVNNEGIDANDSSAKGKEVGSSYEIYKNYKKGKFTFVDKIFGKKFLYEDTLPKINWKLTKETKTILGYE
CQKATTTFRGRTYTAWFTPEIPVSDGPYKFNGLPGLILEIEDGKKHYTFKAIKIELNKEKPIEIPKPKKG
KKITREKFKKIKEKYY
>gnl|CDD|273496 TIGR01201, HU_rel, DNA-binding protein, histone-like, putative. This model describes a set of proteins related to but longer than DNA-binding protein HU. Its distinctive domain architecture compared to HU and related histone-like DNA-binding proteins justifies the designation as superfamily. Members include, so far, one from Bacteroides fragilis, a gut bacterium, and ten from Porphyromonas gingivalis, an oral anaerobe [DNA metabolism, Chromosome-associated proteins]
MIKYKVKERKAKIGKTGKTMWYPQTVKSGVMDFEEIAELIAEESSLSPGDVKGIIDRLAYVLRRELANGK
TVRLGEIGTFRLSATAKGSGVEEAEEVSAEQVNKARVLFTPEKTLKTATREIRLALINRYLKKPDDAGGA
PNSPS
>gnl|CDD|130269 TIGR01202, bchC, 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
KTQAIVLSGPNQIELREVTLTPPSPGDLVVEIWYSGISTGTEKLFWNGLMPPFPGMGYPLVPGYESVGRV
VEAGPDTGFRPGDRVFVPGSNCYEDVRGLFGGASKRLVTPASRVCRLDPALGPQGALLALAATARHAVAG
AEVKVLPDLIVGHGTLGRLLARLTKAAGGSPPAVWETNPRRRDGATGYEVLDPEKDPRRDYRAIYDASGD
PSLIDTLVRRLAKGGEIVLAGFYTEPVNFDFVPAFMKEARLRIAAEWQPGDLHAVRELIESGALSLDGLI
THQRPASDAAEAYMTAFSDPDCLKMILD
>gnl|CDD|273497 TIGR01203, Hypoxanthine-guanine_phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase. Alternate name: hypoxanthine-guanine phosphoribosyltransferase. Sequence differences as small as a single residue can affect whether members of this family act on hypoxanthine and guanine or hypoxanthine only. The designation of this model as equivalog reflects hypoxanthine specificity and does not reflect whether or not guanine can replace hypoxanthine [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSG
DVKILKDLDLDIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEI
PDKFVVGYGLDYAERYRNLPYIGVLE
>gnl|CDD|130271 TIGR01204, 6-carboxyhexanoate--CoA_ligase, 6-carboxyhexanoate--CoA ligase. Alternate name: pimeloyl-CoA synthase [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
EKGGKHISGGERIVKKEELETAVKELLNKPKSHSRGEFDFMQIKVEKVKDFEIVKFNPLKISTYSFSSPE
EARKFARKKLTQEGVSEEVAKKAVEILSKGANMRGAVLMDIETGERLDEDKEKGVRVSRFDWKDAKKVTE
KLLKVGYTLRTVEALALAFKVLFCPAVVAELCWSDDPDYVTGYVSGKEIGYVRITPLKEKGDELGGRVFF
VSRKNELSEYIHCLEQKPILIE
>gnl|CDD|273498 TIGR01205, D-alanine--D-alanine_ligase, D-alanine--D-alanine ligase. This model describes D-Ala--D-Ala ligase, an enzyme that makes a required precursor of the bacterial cell wall. It also describes some closely related proteins responsible for resistance to glycopeptide antibiotics such as vancomycin. The mechanism of glyopeptide antibiotic resistance involves the production of D-alanine-D-lactate (VanA and VanB families) or D-alanine-D-serine (VanC). The seed alignment contains only chromosomally encoded D-ala--D-ala ligases, but a number of antibiotic resistance proteins score above the trusted cutoff of this model [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDKMGSWTYKDLPQLILELGALLEGIDVVFPV
LHGRYGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLTQNRASADELECEQ
VAEPLGFPVIVKPAREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNEEALPII
EIVPEIEGFYDYEAKYLDGSTEYVIPAPLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNE
INTIPGMTAISLFPKAAAAAGIEFSQLVERILELA
>gnl|CDD|273499 TIGR01206, lysW, lysine biosynthesis protein LysW. This very small, poorly characterized protein has been shown essential in Thermus thermophilus for an unusual pathway of Lys biosynthesis from aspartate by way of alpha-aminoadipate (AAA) rather than diaminopimelate. It is found also in Deinococcus radiodurans and Pyrococcus horikoshii, which appear to share the AAA pathway [Amino acid biosynthesis, Aspartate family]
MQFECPECGAEIELENPELGELVICDECGAELEVVSLDPLRLEAAPEEAEDWGE
>gnl|CDD|130274 TIGR01207, Glucose-1-phosphate_thymidylyltransferase_1, glucose-1-phosphate thymidylyltransferase, short form. Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQW
GINLSYAVQPSPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPE
RYGVVEFDSNGRAISIEEKPAQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLS
VELLGRGYAWLDTGTHDSLLEASNFIQTIEKRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQY
LLRLLE
>gnl|CDD|273500 TIGR01208, rmlA_long, glucose-1-phosphate thymidylylransferase, long form. The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase
KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERF
GAKITYIVQGEPLGLAHAVYTARDFLGDDDFVVYLGDNLIQDGISRFVKSFEEKDYDALILLTKVRDPTA
FGVAVLEDGKRILKLVEKPKEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVG
GSKVTGWWKDTGKPEDLLDANRLILDEVEREVQGVDDESKIRGRVVVGEGAKIVNSVIRGPAVIGEDCII
ENSYIGPYTSIGEGVVIRDAEVEHSIVLDESVIEGVQARIVDSVIGKKVRIKGNRRRPGDLRLTIGDYSQ
VEL
>gnl|CDD|273501 TIGR01209, Uncharacterized_protein_MJ0414, RNA ligase, Pab1020 family. Members of this family are found, so far, in a single copy per genome and largely in thermophiles, of which only Aquifex aeolicus is bacterial rather than archaeal. PSI-BLAST converges after a single iteration to the whole of this family and reveals no convincing similarity to any other protein. The member protein Pab1020 has been characterized as an RNA ligase with circularization activity [Transcription, RNA processing]
IAVKLGLPSKRLEKAEARGSLREDEFEGIKYLRFKKSFGDLERGTVVILRDELFVIRGFPHIKRILLLRP
GIKRHFKDPEVVVEEKMNGYNVRIVKYGGNVYALTRGGFICPFTTERLPDLIDLEFFDDNPDLVLCGEMA
GPENPYTPEYYPEVKEDLGFFLFDIREGKTNRSLPVEERLELAEKYGLPHVEILGVYTADEAVEEIYEII
ERLNKEGREGVVMKDPEMRVKPLKYTTSYANINDIKYAARYFFELGRDFFFSRILREAFQSYEFGEKGEE
FRRRAKELGEAILQPMVESIEDVERGERVYEEFELVFESEETAEEFLTHFEKLGVHIEIKDIEEIKDGWR
VTFKRIYPSTTDRIRELLGGKLWV
>gnl|CDD|273502 TIGR01210, Uncharacterized_protein_MJ0550, radical SAM enzyme, TIGR01210 family. This family of exclusively archaeal radical SAM enzymes has no characterized close homologs [Hypothetical proteins, Conserved]
VWMEEDNLRGFPGKSLTIILRTRGCYWAREGGCYMCGYLADSSPEVTEENLINQFDEAIEKYKEKIKDFV
IKIFTSGSFLDDREVPKETRNYIFEKIAQRDNLKEVVVESRPEFIDEEKLEELRKIGVNVEVAVGLETAN
DRIREKSINKGSTFEDFIRAAELARKYGAGVKAYLLFKPPFLSEKEAIADMISSIRKCIPVTDTVSINPT
NVQKGTLVEFLWNRGLYRPPWLWSVAEVLKEAKKIGAEVLSDPVGAGSDRGAHNCGKCDKRVKEAIRKFS
LTQDISVLEEVECECIEEWKAYVEVENKSIVPL
>gnl|CDD|273503 TIGR01211, Uncharacterized_protein_MJ1136, radical SAM enzyme/protein acetyltransferase, ELP3 family. This family includes elongator complex protein 3 (ELP3) from eukaryotes and related proteins from other lineages. ELP3 is a component of the RNA polymerase II holoenzyme. It has an N-terminal radical SAM domain and C-terminal GNAT acetyltransferase domain. Members of this family are found in eukaryotes, archaea, and a few bacteria (e.g. Atopobium sp). The activity discovered first was an acetyltransferase modification at the N-termini of all four core histones, shown in vitro in eukaryotes. More recently, the radical SAM domain was shown to play a role in zygotic paternal genome demethylation. Family TIGR01212, widespread in prokaryotes, lacks the GNAT acetyltransferase domain but shares extensive sequence similarity with this family (TIGR01211) [Transcription, DNA-dependent RNA polymerase]
EIVDSLLSGKTRDKEDLEDLKLEVSRKYGLSKVPSNSEILNSAPDEEKKKLEPILRKKPVRTISGVAVVA
VMTSPHRCPHGKCLYCPGGPDSENSPQSYTGYEPAAMRGRQNDYDPYEQVTARLEQLEQIGHPVDKVELI
IMGGTFPARDLDYQEWFIKRCLNAMNGFDQELKGNSTLEEAIRINETSKHRCVGLTIETRPDYCREEHID
RMLKLGATRVELGVQTIYNDILERTKRGHTVRDVVEATRLLRDAGLKVVYHIMPGLPGSSFERDLEMFRE
IFEDPRFKPDMLKIYPTLVTRGTELYELWKRGEYKPYTTEEAVELIVEIKRMMPKWVRIQRIQRDIPAPL
IVAGVKKSNLRELVYRRMKEHGITCRCIRCREVGHQMVKPVQPEEENVELIVEEYAASGGTEFFLSYEDP
KNDILIGFLRLRFPSEPAHRKEVDATALVRELHVYGSEVPIGERGDDEWQHRGYGRRLLEEAERIAAEEG
SEKILVISGIGVREYYRKLGYELDGPYMSKRL
>gnl|CDD|130279 TIGR01212, Uncharacterized_protein_MJ0486, radical SAM protein, TIGR01212 family. Members of this family are apparent radical-SAM enzymes, related to the N-terminal region of the bifunctional ELP3, whose C-terminal region is part of the elongator complex and appears to acetylate histones and other proteins. ELP3 binds S-adenosylmethionine (SAM) and was recently shown to be involved in a DNA demethylation process in eukaryotes. Close sequence similarity of this family (with lacks the GNAT family acetyltransferase domain) to the ELP3 N-terminal region and a strong match to the pfam04055 support identification of this family as radical SAM despite the atypical spacing between first and second Cys residues in the 4Fe4S-binding motif [Unknown function, Enzymes of unknown specificity]
LYNTLGDYLKERYGQKVFKITLHGGFSCPNRDGTKGRGGCTFCNDASRPIFADEYTQARIPIKEQIKKQM
KKYKKDKKFIAYFQAYTNTYAPVEVLKEMYEQALSYDDVVGLSVGTRPDCVPDEVLDLLAEYVERGYEVW
VELGLQTAHDKTLKKINRGHDFACYVDAVKRARKRGIKVCSHVILGLPGEDREEMMETAKIVSLLDVDGI
KIHPLHVVKGTKMAKMYEKGELKTLSLEEYISLACDFLEHLPPEVVIHRISGDAPRETLIAPEWCKNKWE
IMNKISEELERRGTYQGARFGR
>gnl|CDD|273504 TIGR01213, tRNA_pseudouridine_synthase_Pus10, tRNA pseudouridine(54/55) synthase. Members of this family show twilight-zone similarity to several predicted RNA pseudouridine synthases. All trusted members of this family are archaeal. Several eukaryotic homologs lack N-terminal homology including two CXXC motifs [Hypothetical proteins, Conserved]
ALEILAKYPLCDRCLGRLFAKLGHGTSNRERGEALQLALALELGRPVKEFVESEPCDVCGGIFDRFDEAA
DLVAEKVGDYDFSTFLVGTRFPPDVIELEEEIRKEFGSGGGESIKREFNREVGKLFVKRTGKEVDFERPD
LVIMVEFEYEFVDVQVNSLFIYGRYRKLVRGIPQTRWPCRKNYPESVEELIASPFLKATGGTDAYFHGAG
REDVDVRMLGTGRPFVLEVKEPRYRKIDLDPLEEEINTSGKGKVEVEGLKFATREEVEEVKEEKHRKVYR
ALVEVDGPVSDEDLEELCKELEGATIYQRTPLRVLHRRADLVRERRVYQVDLSGLDGNHAELIIEAEGGL
YIKELVSGDGGRTRPSVSEVLGVEAVCKELDVLKVCDE
>gnl|CDD|273505 TIGR01214, dTDP-4-keto-L-rhamnose_reductase, dTDP-4-dehydrorhamnose reductase. This enzyme catalyzes the last of 4 steps in making dTDP-rhamnose, a precursor of LPS core antigen, O-antigen, etc [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
RILITGANGQLGRELVQQLSPEGRVVVALTRSQLDLTDPEALERLLRAIRPDAVVNTAAYTDVDGAESDP
EKAFAVNALAPQNLARAAARHGARLVHISTDYVFDGEGKRPYREDDATNPLNVYGQSKLAGEQAVRAAGP
NALIVRTSWLYGGGGGRNFVRTMLRLAGRGEELRVVDDQIGSPTYAGDLARVIAALLQRLARARGVYHLA
NSGQVSWYEFAQAIFEEAGADGLLLHPQEVKPISSKEYPRPARRPAYSVLDNTKLVKTLGLPLPHWREAL
RRYLQEA
>gnl|CDD|188120 TIGR01215, Cell_division_topological_specificity_factor, cell division topological specificity factor MinE. This protein is involved in the process of cell division. This protein prevents the proteins MinC and MinD to inhibit cell division at internal sites, but allows inhibiton at polar sites. This allows for correct cell division at the proper sites [Cellular processes, Cell division]
MSLLEFFKSRKKNSAEVAKDRLKLILAHERAQLAPEYLEELRKEILEVISKYVEIDPEMVEVSLESQGDM
SVLELNITLPE
>gnl|CDD|273506 TIGR01216, ATP_synthase_epsilon_chain, ATP synthase, F1 epsilon subunit (delta in mitochondria). This model describes one of the five types of subunits in the F1 part of F1/F0 ATP synthases. Members of this family are designated epsilon in bacterial and chloroplast systems but designated delta in mitochondria, where the counterpart of the bacterial delta subunit is designated OSCP. In a few cases (Propionigenium modestum, Acetobacterium woodii) scoring above the trusted cutoff and designated here as exceptions, Na+ replaces H+ for translocation [Energy metabolism, ATP-proton motive force interconversion]
TLKLEIVTPEGEIYSGEVESVILPGSEGELGILPGHAPLITALKPGVVRIRKLGDDWEHIAVSGGFAEVQ
PDKVTILADGAVFADDIDEAEAEKALEAAEKLLESAEDDKDLAEALLKLKKARAQLEALE
>gnl|CDD|273507 TIGR01217, Acetyl-coenzyme_A_synthetase_1, acetoacetyl-CoA synthase. This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway [Central intermediary metabolism, Other]
ERPQPLWQPDAQRIAQARMTRFQAWAGEHHGAAEGGYDALHRWSVDELDTFWKAVWEWFDVRFSTPCARV
VDDRTMPGAQWFPGARLNYAENLLRAAGTEPALLYVDETHEPAPVTWAELRRQVASLAAALRALGVRPGD
RVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQIEPKLLFTVDGYRYNGKEHDRRDKVA
EVRKELPTLRAVVHIPYLGPRETEAPKIDGALDLEDFTAAAQAAELVFEQLPFDHPLWILFSSGTTGLPK
CIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWMMWNWLVSGLATGATLVLYDGSPGFPATNVLWD
IAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPPDGFRWVYDEIKADVWLASISGG
TDICSCFAGANPTLPVHIGEIQAPGLGTAVQSWDPEGKPVTGEVGELVCTNPMPSMPIRFWNDPDGSKYR
DAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDG
GYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQGTPVD
NPGAIDNPELLDLYEELAELRS
>gnl|CDD|273508 TIGR01218, conserved_hypothetical_protein, tandem five-transmembrane protein. Members of this family of proteins, with average length of 210, have no invariant residues but five predicted transmembrane segments. Strangely, most members occur in groups of consecutive paralogous genes. A striking example is a set of eleven encoded consecutively, head-to-tail, in Staphylococcus aureus strain COL
IKFINKNFRYKIIEYNGEYYLLDLSTSKWKSYFFPLLNWLIPKKLYEIDNDEFEKLKKVKKKKNSGLGIL
GQGISVLLYRLLRPLFDYFDISQSIFIKIILFLISILLVYLLRIYINKKNKKKLYNRLNNKKRYKIKIRP
TSFKYRIFILFLYIFFLGLSIFLFYLFINNGTENIILVINGIIFLFFFLFINMLPISYKKYHVKIKE
>gnl|CDD|273509 TIGR01219, Phosphomevalonate_kinase, phosphomevalonate kinase, ERG8-type, eukaryotic branch. This enzyme is part of the mevalonate pathway, one of two alternative pathways for the biosynthesis of IPP. In an example of nonorthologous gene displacement, two different types of phosphomevalonate kinase are found - the animal type and this ERG8 type. This model represents plant and fungal forms of the ERG8 type of phosphomevalonate kinase [Central intermediary metabolism, Other]
VASAPGKVLMAGGYLVLDKPYAGLVLGLNARFYAIVKPINEEVGAWKWDVRVKSPQFSDREWLYKISLNH
LTLQSVSASDSRNPFVNPFIQYAIAAVHLYFDKESLHKLLLQGLDITILGDNAYYSQPESLGTLAPFASI
TFNAAEKPEVAKTGLGSSAAMTTALVAALLHYLGVVDLSDPDKEGKFGCSDLDVIHNLAQTAHCLAQGKV
GSGFDVSAAVYGSQRYRRFSPELISFLQVAITGLPLNEVLGTIVKGKWDNKRTEFSLPPLMNLFMGDPGG
GSSTPSMVGKVKKWQMSDPEESRENWQNLSDANLELETKLNDLSKLAKDHWDVYLRVIKVLTSEKCVLHA
TEELLEAREAMLRIRRLMRQITEEASVDIEPESQTQLLDSTMSLEGVLLAGVPGAGGFDAIFAITLGDVD
SGTKLTQAWSSHNVLALDVREAPHGVCLESDPRT
>gnl|CDD|130287 TIGR01220, phosphomevalonate_kinase, phosphomevalonate kinase, ERG8-type, Gram-positive branch. This enzyme is part of the mevalonate pathway, one of two alternative pathways for the biosynthesis of IPP. In an example of nonorthologous gene displacement, two different types of phosphomevalonate kinase are found - the animal type and this ERG8 type. This model represents the low GC Gram-positive organism forms of the ERG8 type of phosphomevalonate kinase [Central intermediary metabolism, Other]
IVVHAPGKLFVAGEYAVVEPGNPAILVAVDRFVTVTVEDADGAADVIISSDLGPQPVGWRRHDGRLVVRD
PDARSALAYVVSAIETVERYAGERNQKLPALHLSVSSRLDEADGRKYGLGSSGAVTVATVKALNAFYDLE
LSNDEIFKLAMLATAELQPKGSCGDIAASTYGGWIAYSTFDHDWVLQLARRVGVDRTLKAPWPGLSIRPL
PAPKGLTLLIGWTGSPASTASLVSDVHRRKWRGSASYQRFLETSTDCVESAITAFETGDITSLQKEIRRN
RQELARLDDEVGVGIETEKLKALCDAAEAYGGAAKPSGAGGGDCGIAILDAEADITHVRQRWETAGILPL
PLTPYLEG
>gnl|CDD|273510 TIGR01221, dTDP-4-dehydrorhamnose_35-epimerase, dTDP-4-dehydrorhamnose 3,5-epimerase. This enzyme participates in the biosynthesis of dTDP-L-rhamnose, often as a precursor to LPS O-antigen [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
NFIRTEIPDVLLIEPRVFGDERGFFMETYNDEAFQEQGIPVRFVQDNHSKSYKGVLRGLHYQRPHPQGKL
VRVLRGEVFDVAVDLRRNSPTFGKWVGVLLSAENKRQLWIPEGFAHGFVVLSDEAEFLYKCTDYYAPEYE
RGIIWNDPDIGIDWPLEDAPILSEKDRNGPPLAEAE
>gnl|CDD|273511 TIGR01222, Probable_septum_site-determining_protein_MinC, septum site-determining protein MinC. The minC protein assists in correct placement of the septum for cell division by inhibiting septum formation at other sites. Homologs from Deinocoocus, Synechocystis PCC 6803, and Helicobacter pylori do not hit the full length of the model and score between the trusted and noise cutoffs [Cellular processes, Cell division]
MVDLKGTKLGLTVLHLDDQNLDELLQELSEKITQAPKFFAKGPIILDVIELPNPELKDLPALVSELRRHG
LEVVGISGGSEEITAKAQALDLLVLSSGRKNKKEATRVESTTKVIKTPVRSGQQIYAKHGDLIVLGNVNA
GAEVLADGNIHVYGKLRGRALAGANGDTSAVIFALDLQAELISIAGRYKVSDDIERNFWGKPVQASLKGN
RLVIEPL
>gnl|CDD|130290 TIGR01223, Probable_phosphomevalonate_kinase, phosphomevalonate kinase, animal type. This enzyme is part of the mevalonate pathway, one of two alternative pathways for the biosynthesis of IPP. In an example of nonorthologous gene displacement, two different types of phosphomevalonate kinase are found. One is this type, found in animals. The other is the ERG8 type, found in plants and fungi (TIGR01219) and in Gram-positive bacteria (TIGR01220) [Central intermediary metabolism, Other]
VLLFSGKRKSGKDFVTEALQSRLGADVCAVLRLSGPLKEQYAQEHGLNFQRLLDTSTYKEAFRKDMIRWG
EEKRQADPGFFCRKIVEGISQPIWLVSDTRRVSDIQWFREAYGAVTQTVRVVALEQSRQQRGWVFTPGVD
DAESECGLDNFGDFDWVIENHGVEQRLEEQLENLIEFIRSRL
>gnl|CDD|273512 TIGR01224, hutI, imidazolonepropionase. This enzyme catalyzes the third step in histidine degradation [Energy metabolism, Amino acids and amines]
IEDAVILIHGGKIVWIGQLAALPGEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLE
ILAQGGGILSTVRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQP
VDVVTTFLGAHAVPPEFQGRPDDYVDGICEELIPQVAEEGLASFADVFCEAGVFSVEQSRRILQAAQEAG
LPVKLHAEELSNLGGAELAAKLGAVSADHLEHASDAGIKALAEAGTVAVLLPGTTFYLRETYPPARQLID
YGVPVALATDLNPGSSPTLSMQLIMSLACRLMKMTPEEALHAATVNAAYALGLGEERGTLEAGRDADLVI
LSAPSYAEIPYHYGVNHVHAVIKNGNI
>gnl|CDD|200086 TIGR01225, Histidine_ammonia-lyase, histidine ammonia-lyase. This enzyme deaminates histidine to urocanic acid, the first step in histidine degradation. It is closely related to phenylalanine ammonia-lyase [Energy metabolism, Amino acids and amines]
VTLDGGSLTLEDVVAVARHGARVSLSAAAREAVAKSRAAIEQIIAGDETVYGINTGFGKLASTRIDSEDL
AELQRNLVRSHAAGVGDPLDEEVVRAIMALRLNSLAKGYSGVRAEVLDQLIALLNAGVHPVVPEKGSVGA
SGDLAPLAHMALVLMGEGKAFFKGERMPAAEALAAAGLEPVTLAAKEGLALINGTQAMTALALLALFDAE
DLLRAADITAALSVEALLGTTKPFDPDIHEARPHRGQIDVAARFRELLAGSEITLSHRDCDRVQDAYSLR
CQPQVHGAVLDTLDQVAEVLGIELNSATDNPLVFADGGEVVSGGNFHGEPVALAADFLAIAIAELGSISE
RRIERLLDPNLSGLPPFLAPDGGLNSGFMIAQYTAAALVSENKALSHPASVDSIPTSANQEDHVSMGAHA
ARKLREMIENVRRVIAIELLAACQGLEFRDPLKTSAKLEKAYQAVRSVVAPLDGDRFFAPDIEAARDLVA
KGSLIAAVPAGVLPPL
>gnl|CDD|130293 TIGR01226, Phenylalanine_ammonia-lyase, phenylalanine ammonia-lyase. Members of this subfamily of MIO prosthetic group enzymes are phenylalanine ammonia-lyases. They are found, so far, in plants and fungi. From phenylalanine, this enzyme yields cinnaminic acid, a precursor of many important plant compounds. This protein shows extensive homology to histidine ammonia-lyase, the first enzyme of a histidine degradation pathway. Note that members of this family from plant species that synthesize taxol are actually phenylalanine aminomutase, and are covered by exception model TIGR04473
DPLNWGTAAKTMAGSQLDEVKRMVAEYRNGPLIKLDGATLTISQVAAAARRGVAVELDESARVERVKASS
EWVMTQMSKGTDVYGVTTGFGGTSHRRTKQGGALQKELLRFLNAGILGTGSDNHNSLPEEATRAAMLVRI
NTLLQGYSGIRFEILEAITKLLNANVTPCLPLRGTITASGDLVPLSYIAGLITGRPNSKVYSPDGQIMSA
AEALKLAGIEGGFELQPKEGLAIVNGTAVGASMASLVLFEANILALLAEVLSAMFCEVMNGKPEFTDHLT
HKLKHHPGQIEAAAIMEHILDGSSYAKHAEKEVEMDPLQKPKQDRYALRTSPQWLGPQIEVIRSATKMIE
REINSVNDNPLIDVERGKAHHGGNFQGTPIGVSMDNTRLAIAAIGKLMFAQFSELVNDFYNNGLPSNLAG
GRNPSLDYGFKGAEIAMASYTSELQFLANPVTNHVQSAEQHNQDVNSLGLISARKTAEAVDILKLMLATY
LYALCQAVDLRHLEENFKSTVKNIVSEVAKKVLGMGLTGELHPKRFCEKDLLKVLDRETVFDYIDDPCSA
NYPLMQKLRQVLVEHALSNGEREKDLLSSFQKIQVFEAELKAVLPPDVRGARAAGDSGTSPAPNRIGECR
SYPLYRFVREELGTKYLTGEKYNSPGEEISKVYEAISEGKIIDPLLKCLD
>gnl|CDD|273513 TIGR01227, hutG, formimidoylglutamase. Formiminoglutamase, the fourth enzyme of histidine degradation, is similar to arginases and agmatinases. It is often encoded near other enzymes of the histidine degredation pathway: histidine ammonia-lyase, urocanate hydratase, and imidazolonepropionase [Energy metabolism, Amino acids and amines]
WQGRPDSEEGGSSFRDHQVTKPSDLIATWDDQDEKGVALIGFPLDKGVIRNKGRRGARHGPSAIRQALAH
LGDWHVSELLYDLGDIVIHGDDLEDTQHEIAQTAAALLADHRVPVILGGGHSIAYATFAALAQHYKGTTA
IGVINFDAHFDLRATEDGGPTSGTPFRQILDECQIEDFHYAVLGIRRFSNTQALFDYAKKLGVRYVTDDA
LRPGLLPTIKDILPVFLDKVDHIYLTVDMDVLDAAHAPGVSAPAPGGLYPDELLELVKRIAASDKVRGAE
IAEVNPTLDFDQRTARAAARLVLHFLK
>gnl|CDD|130295 TIGR01228, Urocanate_hydratase, urocanate hydratase. This model represents the second of four enzymes involved in the degradation of histidine to glutamate [Energy metabolism, Amino acids and amines]
REIRAPRGTKLECKGWLQEAALRMLMNNLDPEVAEDPENLVVYGGIGKAARNWEAFDKIVETLKRLENDE
TLLVQSGKPVGVFKTHENAPRVLIANSNLVPHWADWEHFHELEAKGLMMYGQMTAGSWIYIGTQGILQGT
YETFAELARQHFGGSLKGKWVLTAGLGGMGGAQPLAVTMNGGVSIAVEVDESRIDKRLETKYCDEQTDSL
DEALARAEEAKAEGKPISIGLLGNAAEVLPELLKRGVVPDVVTDQTSAHDPLNGYIPEGYTVEDADKLRQ
EEPEAYVKAAKQSMAKHVRAMLAFQKQGSVTFDYGNNIRQVAKEEGVEDAFDFPGFVPAYIRPLFCRGKG
PFRWVALSGDPADIYRTDAAVKELFPEDAHLHRWIDMAQERVSFQGLPARICWLGYGERAKLGLAINEMV
RSGELKAPVVIGRDHLDAGSVASPNRETEAMKDGSDAVSDWPLLNALLNTAAGATWVSFHHGGGVGMGFS
LHAGMVIVADGTDEAAERIARVLTNDPGMGVIRHADAGYEIAIDVAKEQGIDVPM
>gnl|CDD|162262 TIGR01229, rocF_arginase, arginase. This model helps resolve arginases from known and putative agmatinases, formiminoglutamases, and other related proteins of unknown specifity. The pathway from arginine to the polyamine putrescine may procede by hydrolysis to remove urea (arginase) followed by decarboxylation (ornithine decarboxylase), or by decarboxylation first (arginine decarboxylase) followed by removal of urea (agmatinase)
GIVGLPFSLGQPRRGVDKGPSRLREAGLLETLRDLEYDMQDLGQLPFAVRPKESPRYAVKNPRYVLAATE
QLAPKVYEVFEEGRFPLVLGGDHSIAIGTISGTARVHPDKKLGVLWLDAHADINTPETSDSGNIHGMPLA
FLLGRLKSEFPDSPGLGWVAPEISPKNLVYIGLRSVDPGERKILKELGIKVFSMHEIDELGIGKVVEETL
EYLKAEDGPIHLSLDVDGLDPSLAPATGTPVVGGLTFREGLLIMEMLYESGLLTALDVVEVNPTLDIKHV
NETIKTAVEIVRSLLGSTLL
>gnl|CDD|273514 TIGR01230, Agmatinase_Agmatine_ureohydrolase_AUH., agmatinase. Members of this family include known and predicted examples of agmatinase (agmatine ureohydrolase). The seed includes members of archaea, for which no definitive agmatinase sequence has yet been made available. However, archaeal sequences are phylogenetically close to the experimentally verified B. subtilis sequence. One species of Halobacterium has been demonstrated in vitro to produce agmatine from arginine, but no putrescine from ornithine, suggesting that arginine decarboxylase and agmatinase, rather than arginase and ornithine decarboxylase, lead from Arg to polyamine biosynthesis. Note: a history of early misannotation of members of this family is detailed in PUBMED:10931887
KLFMNSNPYYEEADWVIYGIPYDATTSYRPGSRHGPNAIREASWNLEWYSNRLDRDLAMLNVVDAGDLPL
AFGDAREMFEKIQEHAEEFLEEGKFPVAIGGEHSITLPVIRAMAKKFGKFAVVHFDAHTDLRDEFDGGTL
NHACPMRRVIELGLNVVQFGIRSGFKEENDFARENNIQVLKREVDDVIAEVKQKVGDKPVYVTIDIDVLD
PAFAPGTGTPEPGGLTSDELINFFVRALKDDNVVGFDVVEVAPVYDQSEVTALTAAKIALEMLLI
>gnl|CDD|273515 TIGR01231, Tagatose-6-phosphate_kinase, tagatose-6-phosphate kinase. This enzyme is part of the tagatose-6-phosphate pathway of lactose degradation [Energy metabolism, Biosynthesis and degradation of polysaccharides]
MILTVTLNPSVDISYPLETLKIDTVNRVKEVSKTAGGKGLNVTRVLYQSGDKVLASGFLGGKLGEFIESE
LDQSPIKHAFYKISGETRNCIAILHEGNQTEILEQGPTISHEEAEGFLDHFENLLKKSEVVAISGSLPKG
LPNDYYEQLIQLCSDEGVPVVLDCSGAPLETVLKSSAKPTVIKPNNEELSQLLGKEVTKDIEELKDALKE
PLFSGIEWIIVSLGRQGAFAKHGDTFYKVDIPDIPVVNPVGSGDSTVAGITSALNSKKSDADLLKKANTL
GMLNAQETMTGHVNLTNYDTLNSQIEVKEV
>gnl|CDD|130299 TIGR01232, Tagatose_16-diphosphate_aldolase, tagatose 1,6-diphosphate aldolase. This family consists of Gram-positive proteins. Tagatose 1,6-diphosphate aldolase is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation [Energy metabolism, Biosynthesis and degradation of polysaccharides]
SKSNQKIASIEQLSNNEGIISALAFDQRGALKRLMAKHQTEEPTVAQIEQLKVLVAEELTQYASSILLDP
EYGLPASDARNKDCGLLLAYEKTGYDVNAKGRLPDCLVEWSAKRLKEQGANAVKFLLYYDVDDAEEINIQ
KKAYIERIGSECVAEDIPFFLEVLTYDDNIPDNGSVEFAKVKPRKVNEAMKLFSEPRFNVDVLKVEVPVN
VKYVEGFAEGEVVYTKEEAAQHFKDQDAATHLPYIYLSAGVSAELFQETLKFAHEAGAKFNGVLCGRATW
SGAVQVYIEQGEDAAREWLRTTGFKNIDDLNKVLKDTATSWKQRK
>gnl|CDD|273516 TIGR01233, lacG, 6-phospho-beta-galactosidase. This enzyme is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation [Energy metabolism, Biosynthesis and degradation of polysaccharides]
TKTLPKDFIFGGATAAYQAEGATHTDGKGPVAWDKYLEDNYWYTAEPASDFYHKYPVDLELAEEYGVNGI
RISIAWSRIFPTGYGEVNEKGVEFYHKLFAECHKRHVEPFVTLHHFDTPEALHSNGDFLNRENIEHFIDY
AAFCFEEFPEVNYWTTFNEIGPIGDGQYLVGKFPPGIKYDLAKVFQSHHNMMVSHARAVKLYKDKGYKGE
IGVVHALPTKYPYDPENPADVRAAELEDIIHNKFILDATYLGHYSDKTMEGVNHILAENGGELDLRDEDF
QALDAAKDLNDFLGINYYMSDWMQAFDGETEIIHNGKGEKGSSKYQIKGVGRRVAPDYVPRTDWDWIIYP
EGLYDQIMRVKNDYPNYKKIYITENGLGYKDEFVDNTVYDDGRIDYVKQHLEVLSDAIADGANVKGYFIW
SLMDVFSWSNGYEKRYGLFYVDFDTQERYPKKSAHWYKKLAETQVIE
>gnl|CDD|130301 TIGR01234, L-ribulokinase, ribulokinase. This enzyme catalyzes the second step in arabinose catabolism. The most closely related protein subfamily outside the scope of this model includes ribitol kinase from E. coli [Energy metabolism, Sugars]
AYAIGVDFGTLSGRALAVDVATGEEIATAVEWYRHWVKGQFLPKTGAKLPNDQALQHPADYIEVLEAAIP
TVLAELGVDPADVVGIGVDFTACTPAPIDSDGNPLCLLPEFAENPHAYFKLWKHHAAQEEADRINRLAHA
PGEVDLSRYGGIISSEWFWAKILQITEEDPAIYQAADRWIELADWIVAQLSGDIRRGRCTAGYKALWHES
WGYPSASFFDELNPILNRHLPDKLFTDIWTAGEPAGTLTPEWAQRTGLPEGVVVAVGNFDAHVGAVAAGI
AQPGALVKIMGTSTCHVLIGDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGKVCVPPELKTE
ANASQKQLHEALSEAAAKQPSGEHGLVALDWFNGNRSPLVDQRLKGVITGLTLATDAPLLYRALIEATAF
GTRMIMETFTDSGVPVEELMAAGGIARKNPVIMQIYADVTNRPLQIVASDQAPALGAAIFAAVAAGVYAD
IPSAQAKMGSAVEKTLTPCSENAQRYEQLYARYQELAMSFGQYNPT
>gnl|CDD|130302 TIGR01235, Pyruvate_carboxylase_1, pyruvate carboxylase. This enzyme plays a role in gluconeogensis but not glycolysis [Energy metabolism, Glycolysis/gluconeogenesis]
KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLGPIEAYLSIDEIIRVA
KLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPET
MEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIE
VQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDN
DGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQLGVPNQEDIRTNGYAIQCRVTTEDP
ANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWASTPEEAAAKMDRALREFRIR
GVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNGHPEAKDKLKPLE
NAPRVVVLYADQNPVPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIAP
TTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYF
VKQAAQGGIDIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEK
AGAHILGIKDMAGLLKPAAAKLLIKALREKTDLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSG
LTSQPSLGAIVAALEGSERDPGLNVAWIRELSAYWEAVRNLYAAFESDLKGPASEVYLHEMPGGQYTNLQ
FQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSSKVVGDMALFMVSNDLTVDDVVEPAEELSFPDSVV
EFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAIRKDLQEKHEREVSDFDVASYAMYPK
VFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQGEREVFFELNGQPR
RIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDG
TIKEVLVKAGEQIDAKDLLLVLE
>gnl|CDD|273517 TIGR01236, D1pyr5carbox1, delta-1-pyrroline-5-carboxylate dehydrogenase, group 1. This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate [Energy metabolism, Amino acids and amines]
ANEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNERIPQVNPHNHQAVLAKATNATEED
AMKAVEAALDAKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFR
FNVKYARELYAQQPISAPGEWNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALS
NYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRI
VGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPD
DFRGFMGAVIDEQSFDKIVKYIEDAKKDPEALTILYGGKYDDSQGYFVEPTVVESKDPDHPLMSEEIFGP
VLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDKCTGAVVGQQPFG
GARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY
>gnl|CDD|200087 TIGR01237, D1pyr5carbox2, delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative. This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs [Energy metabolism, Amino acids and amines]
YKHEPFTDFADEENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEH
AEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYY
ARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIA
AKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVI
AEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDS
ADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAF
IRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDS
KAGGPDYLALFMQAKTVTEMF
>gnl|CDD|273518 TIGR01238, D1pyr5carbox3, delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain). This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase [Energy metabolism, Amino acids and amines]
DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHSYKADGEAQPVTNPADRRDIVGQVFH
ANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVD
FCRYYAKQVRDVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELM
QEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLIAETGGQNAMI
VDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVID
AEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACQHGTFVAPTLFELDDIAELSEEVFGPVLHVVRYKAREL
DQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPH
YLYRLTQVQY
>gnl|CDD|273519 TIGR01239, Galactose-1-phosphate_uridylyltransferase, galactose-1-phosphate uridylyltransferase, family 2. This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087 from Pfam [Energy metabolism, Sugars]
HVNQFIEYALENGDIEILDREYLRNRLLEALGITHPDENSSTSILQNQSSPDLLDQLLQWAAENGRMEAD
TTQRDILEAKLMDLITPRPSEVNRKFWETYASYPEQATKYFYQYSKRVYYVKTDAIAKNIHYTVPTEYGD
LEITINLSKPEKDPKAIAAAKEAKQSSYPACQLCMENEGFEGSVNHPARSNHRIIRVILEDEQWGFQFSP
YAYFPEHSIVLKGKHEPMEISKKTFERLLSFLGKFPHYFIGSNADLPIVGGSILSHDHYQGGRHDFPMAR
AEAEEVYELNDYPDVSAGIVKWPMSVLRLQGEDPGELAEAADHIFRTWQTYSDEKAGIAAYSDGTPHHTV
TPIARRRDGKYELDLVLRDNQTSEEYPDGIFHPHQDVHHIKKENIGLIEVMGLAILPGRLKTELKEVEAY
LLGQDNQLTAIHKEWADRLKEKRNITKENVDLVIKQEVGHVFARVLEDAGVFKQTAEGKQGFRKFIDFL
>gnl|CDD|130307 TIGR01240, Diphosphomevalonate_decarboxylase, diphosphomevalonate decarboxylase. This enzyme catalyzes the last step in the synthesis of isopentenyl diphosphate (IPP) in the mevalonate pathway. Alternate names: mevalonate diphosphate decarboxylase; pyrophosphomevalonate decarboxylase [Central intermediary metabolism, Other]
ASVTAYVNIATIKYWGKRNTKLNLPTNSSISLTLSQLRTLTSVAFADEFERDTFYLNGTLQHSIDNEKTS
NCLDDFRQLRKEQEKLHIVSQNNFPTAAGLASSASGLAALVSACAKLYQLPLDTSELSRIARKGSGSACR
SLFGGYVAWEKGKDDHSSAAVQVADDSDWPQXAMCVLVVNDIKKDVSSRQGMQLTVATSELFKEWIEHVV
PDFEVXRKAIKTKDFATFGKETEANSLSMHATTLDAFPPFFYLNDTSKRAMSAVHTLRQGGTICYFTMDA
GPNVKVLYLAENLSKLFEFIYKLFG
>gnl|CDD|273520 TIGR01241, ATP-dependent_zinc_metalloprotease_FtsH, ATP-dependent metalloprotease FtsH. HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]
SLLGFLFSLLPPILLLVGVWFFFRRQMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEI
VDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLF
EQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPAL
LRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNK
TEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQ
FLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYG
SDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEI
KELLA
>gnl|CDD|130309 TIGR01242, Proteasome-activating_nucleotidase, 26S proteasome subunit P45 family. Many proteins may score above the trusted cutoff because an internal
ISELDVRIRKLEDEKRSLEKEKIRLERELERLRSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVV
NVSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVEL
PLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFEL
AKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLR
PGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDY
VTMDDFIKAVEKVL
>gnl|CDD|273521 TIGR01243, Cell_division_cycle_protein_48_homolog_MJ1156, AAA family ATPase, CDC48 subfamily. This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus
SVELRVAEAYPRDVGRGIVRIDRQTAARLGVEPGDFVEIEKGDRSVVAIVWPLRPDDEGRGIIRMDGYLR
ANAGVTIGDTVTVERAEVKEAKKVVLAPTQPIRFGRDFVDYVKEFLLGKPISKGETVIVPVLEGALPFVV
VSTQPAGFVYVTEATEVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIE
PPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEI
DAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRA
RKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIREGKINFEAEEIPAEVLKE
LKVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGV
LLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAP
ARGARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEI
FKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLEVGEEEFLKDLKVEM
RHFLEALKKVKPSVSKEDMLRYERLAKELKRLT
>gnl|CDD|130311 TIGR01244, hypothetical_protein, TIGR01244 family protein. No member of this family is characterized. The member from Xylella fastidiosa is a longer protein with an N-terminal region described by this model, followed by a metallo-beta-lactamase family domain and an additional C-terminal region. Members scoring above the trusted cutoff are limited to the proteobacteria [Hypothetical proteins, Conserved]
DIRKLTEHLYVSPQLTKADAAQAAQLGFKTVINNRPDREEESQPDFAQIKAAAEAAGVTYHHQPVTAGDI
TPDDVETFRAAIGAAEGPVLAYCRSGTRSSLLWGFRQAAEGVPVEEIVRRAQAAGYDLSNFRPRL
>gnl|CDD|273522 TIGR01245, Anthranilate_phosphoribosyltransferase, anthranilate phosphoribosyltransferase. In many widely different species, including E. coli, Thermotoga maritima, and Archaeoglobus fulgidus, this enzymatic domain (anthranilate phosphoribosyltransferase) is found C-terminal to glutamine amidotransferase; the fusion protein is designated anthranilate synthase component II (EC 4.1.3.27) [Amino acid biosynthesis, Aromatic amino acid family]
LEKLIDGKDLSRDEAEQLMKEIMSGEASPAQIAAILTALRIKGETPEEITGFAKAMREHAVKVPGRPPED
LVDIVGTGGDGANTINISTASAFVAAAAGVKVAKHGNRSVSSKSGSADVLEALGVNLDLGPEKVARSLEE
TGIGFLFAPLYHPAMKHVAPVRRELGVRTVFNLLGPLTNPARPKYQVIGVYDPDLVEVMAEALKNLGVKR
ALVVHGDDGLDEISLTGPTTVAELKDGEIREYTLDPEDFGLPRAPLEELAGGSPEENAEILRDILRGKGS
GAKRDIVALNAAAALYVAGRASDLKEGVELALEAIDSGAAAEKLEELVAF
>gnl|CDD|162269 TIGR01246, Succinyl-diaminopimelate_desuccinylase, succinyl-diaminopimelate desuccinylase, proteobacterial clade. This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason [Amino acid biosynthesis, Aspartate family]
VTELAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGDTKNLWATRGTGEPVLAFAGHTDVVPAG
PEEQWSSPPFEPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKK
VVETLMARDELIDYCIVGEPSSVKKLGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAE
LTAIKWDEGNEFFPPTSLQITNIHAGTGANNVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYD
LEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELSTGGGTSDGRFIALMGAEVVEFGPVNATIHKVNEC
VSIEDLEKLSDVYQDLLENL
>gnl|CDD|130314 TIGR01247, drrB, daunorubicin resistance ABC transporter membrane protein. This model describes daunorubicin resistance ABC transporter, membrane associated protein in bacteria and archaea. The protein associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc [Transport and binding proteins, Other]
RELKRFIRSRSRIVGSILNPLLWLIFFGKGWSGAFRFPMIFGGVDYMTYLVPGIVAMTVFNMSFFSGISV
IWDRQFGFLKEILVAPASRVEMIVGRILGGSTVAMIQGAIILALSFIVAILKPSGVIPTLVLAFIVGVAL
SGLGVAIAARMDSMEGFQIIMSMLMLPMFFLSGAFYPITTMPAWMQGLAKINPLTYAVDGARYYLAGVSP
TFPLEQDLLVLTLLAVIFVGIAAVEF
>gnl|CDD|130315 TIGR01248, drrC, daunorubicin resistance protein C. The model describes daunorubicin resistance protein C in bacteria. This protein confers the function of daunorubicin resistance. The protein seems to share strong sequence similarity to UvrA proteins, which are involved in excision repair of DNA. Disruption of drrC gene showed increased sensitivity upon exposure to duanorubicin. However it failed to complement uvrA mutants to exposure to UV irradiation. The mechanism on how it confers duanomycin resistance is unclear, but has been suggested to be different from DrrA and DrrB which are antiporters [Unclassified, Role category not yet assigned]
AIFGSLFNAIDITIDREIGLLSRLWVLPIHRASALLARIIAETIRAFIGTILILAIALALGFRFRNGVAA
ALLFLLIPSIFGIAFAALVMAMALRKEGRFAMEALELAQAAAAFLNPGATPIKLFPDWAQPLIAHQPISP
AIEACADLAHGG
>gnl|CDD|130316 TIGR01249, Putative_proline_iminopeptidase, proline iminopeptidase, Neisseria-type subfamily. This model represents one of two related families of proline iminopeptidase in the alpha/beta fold hydrolase family. The fine specificities of the various members, including both the range of short peptides from which proline can be removed and whether other amino acids such as alanine can be also removed, may vary among members
TKPFVSGYLNVSDNHQLYYEQSGNPDGKPVVFLHGGPGSGTDPGCRRFFDPETYRIVLFDQRGCGKSTPH
ACLEENTTWDLVADIEKLREKLGIKNWLVFGGSWGSTLALAYAQTHPEVVTGLVLRGIFLLREKEWSWFY
EGGASMIYPDAWQRFMDSIPENERNEQLVNAYHDRLQSGDEETKLAAAKAWVDWESTTLLRPINEIVSTA
EDFKFSLAFARLENHYFVNKGFLDVENFILDNISKIRNIPTYIVHGRYDLCCPLQSAWALHKAFPEAELK
VTNNAGHSAFDPNNLAALVHALETYL
>gnl|CDD|188121 TIGR01250, Proline_iminopeptidase, proline-specific peptidase, Bacillus coagulans-type subfamily. This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase
EQIEGIITVDGGYHLFTKTGGEGEKIKLLLLHGGPGMSHEYLENLRELLKEEGREVIMYDQLGCGYSDQP
DDSDEELWTIDYFVDELEEVREKLGLDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSMLDSAPEYVKE
LNRLRKELPPEVRAAIKRCEASGDYDNPEYQEAVEVFYHHLLCRLRKWPEALKHLKSGGNTNVYNIMQGP
NEFTITGNLKDWDITDKLSEIKVPTLLTVGEFDTMTPEAAREMQELIAGSRLVVFPDGSHMTMIEDPEVY
FKLLSDFIR
>gnl|CDD|273523 TIGR01251, Ribose-phosphate_pyrophosphokinase, ribose-phosphate pyrophosphokinase. Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
MKIFSGSSNQELAQKVAKNLGLPLGDVEVKRFPDGELYVRINESVRGKDVFIIQQSTSAPVNDNLMELLI
MIDALKRASAKSITAVIPYYGYARQDKKFKSREPISAKLVANLLETAGADRVLTVDLHSPQIQGFFDVPV
DNLYASPVLAEYLKKKILDNPVVVSPDAGGVERAKKVADALGCPLAIIDKRRISATNEVEVMNLVGDVEG
KDVVIVDDIIDTGGTIAKAAEILKSAGAKRVIAAATHGVFSGPAIERIANAGVEEVIVTNTIPHEKHKPK
VSVISVAPLIAEAIRRIHNNESVSSLFD
>gnl|CDD|273524 TIGR01252, Alpha-acetolactate_decarboxylase, alpha-acetolactate decarboxylase. Puruvate can be fermented to 2,3-butanediol. It is first converted to alpha-acetolactate by alpha-acetolactate synthase, then decarboxylated to acetoin by this enzyme. Acetoin can be reduced in some species to 2,3-butanediol by acetoin reductase [Energy metabolism, Fermentation]
NQLFQYSTMAALMDGQYEGTTTLKELLEHGDFGIGTLNDLDGELIVLDGKAYQIKSDGKAQELPEEDKTP
FAVTTFFDADEKFKITEVMDREQLEKKIEELFPGKNVFYAIKITGTFKKVQTRTVPKQERPYPPLVEVVK
KQPEFHFDNVKGTIVGFWTPAYAAGINVPGYHLHFITEDRTSGGHVLDYIIDNGTLEISQIHEFNLQLPV
TRDFLHADLDQETLKKAIEAAE
>gnl|CDD|130320 TIGR01253, Thiamine_transport_system_permease_protein_ThiP, thiamine ABC transporter, permease protein. The model describes thiamine ABC transporter, permease protein in bacteria. The protein belongs to the larger ABC transport system. It consists of atleast three components: the inner mebrane permease; thiamine binding protein; an ATP-binding subunit. It has been experimentally demonstrated that the mutants in the various steps in the de novo synthesis of the thiamine and the biologically active form, namely thiamine pyrophosphate can be exogenously supplemented with thiamine, thiamine monophosphate (TMP) or thiamine pyrophosphate (TPP) [Transport and binding proteins, Other]
LIPGHLAGGVSAISFIIAFAGAAFLAIFALAGEDDWRAVFQDDYLQHLILFSFGQAFLSALLSIFFAIFL
ARALFRKPFLGKKALLKLCALTFILPALVAIFGIIGIYGRQGWLATLANLFGLEWQFHIYGLQGILIAHL
FFNIPLAAQLFLQALENIPGEQRQLAAQLGLQGWHFFKFVEWPVFRQQCLPTAALIFMLCFASFATVLSL
GGGPQATTIELAIYQAILFDFDLAKAALFALLQFVCCLGLFLLSQRFSKAIANGLSLLNGWFDPDDKLAS
KICDILLILLALFFLFPPLLAIIIDALNSRNLLEVLANPQLWQALGTSLRIALAAALLALTLAIALLLLS
RELEALHKMKAGQFIEMAGMLILAIPGIVLAMGFFLLLNDRDFLNIDADGIVIFCNALMAIPFALKILEA
PFHDIMARYEMLCNSLGIEGWQRFKLIELKALKAPLAQAFAFACALSIGDFGAIALFGNDDFRSLPFLLY
QQIGNYRNQDAAVTAGILLLLCFILFAFI
>gnl|CDD|130321 TIGR01254, Thiamine-binding_periplasmic_protein, ABC transporter periplasmic binding protein, thiB subfamily. The model describes thiamine ABC transporter, periplasmic protein in bacteria and archae. The protein belongs to the larger ABC transport system. It consists of at least three components: the thiamine binding periplasmic protein; an inner membrane permease; an ATP-binding subunit. It has been experimentally demonstrated that the mutants in the various steps in the de novo synthesis of the thiamine and the biologically active form, namely thiamine pyrophosphate can be exogenously supplemented with thiamine, thiamine monophosphate (TMP) or thiamine pyrophosphate (TPP) [Transport and binding proteins, Other]
QPVVTVYTYDSFAADWGLGPVVEKAFEADCNCKVKFVALEDAGELLNRLRLEGKNPKADVVLGLDNNLLE
AASKTGLLAPSGVALDKVNVPGGWNNATFLPFDYGYVAFVYDKNKLQNPPQSLKELVEPEQDLLVIYQDP
RTSSPGLGLLLWMQSVYGEDDAPQAWKQLRKKTVTVTKGWSEAYGTFLGGEYDLVLSYATSPAYHVLFEK
KDNYAALNFSEGHYLQVEGAARLKGAKQPELADKFVQFLLSPAVQNAIPTGNWMYPVVNGTLLPGFFKLT
QQPTTTAPTPAEVTAQRQAWISEW
>gnl|CDD|273525 TIGR01255, Formate_acetyltransferase, formate acetyltransferase 1. Alternate names: pyruvate formate-lyase; formate C-acetyltransferase This enzyme converts formate + acetyl-CoA into pyruvate + CoA. This model describes formate acetyltransferase 1. More distantly related putative formate acetyltransferases have also been identified, including formate acetyltransferase 2 from E. coli, which is excluded from this model [Energy metabolism, Fermentation]
AWEGFTKGDWQNEVNVRDFIQKNYKPYEGDESFLAGPTEATTKVWDKVMEVKLENRTHAPVDFDTAVAST
ITSHDAGYIDKQLEKIVGLQTEAPLKRALIPFGGIRMAEGSLKEYGRELDPMIHKIFTEYRKTHNQGVFD
AYTPDIRRARKAGVLTGLPDAYGRGRIIGDYRRVALYGIDYLMKEKLKQFTSLQADLENELIRLREEIAE
QHRALGEMKEMAAKYGYDISRPATNAKEAIQWTYFGYLAAVKSQNGAAMSLGRTSTFLDIYIERDLKAGK
ITEQEAQEMVDHFVMKLRMVRFLRTPEYDELFSGDPTWATESIAGMGLDGRTLVTKNSFRFLNTLYTMGP
APEPNMTVLWSEKLPLSFKKFAAKMSIDTSSIQYENDDLMRPDFNNDDYAIACCVSPMIVGKQMQFFGAR
ANLAKTMLYAINGGVDEKLKMQVVPDIEPIKDEVLDYDEVMENMDKFLDWLAKQYVTAMNIIHYMHDKYS
YEASQMALHDTKVIRTMAFGIAGFSVAADSLSAIKYAKVKPIRDENGLAIDFEIEGDFPQYGNDDDRVDD
IAVDLVERFMKKLQKHHTYRNAIPTQSVLTITSNVVYGKKTGNTPDGRRVGAPFGPGANPMHGRDQKGAL
ASLTSVAKLPFAYAKDGISYTFSIVPNALGKDDDVRKTNLVGIMDGYFHHEASIEGGQHLNVNVMNREML
LDAMENPEKYPQLTIRVSGYAVNFNSLTKEQQQEVITRTFHESL
>gnl|CDD|273526 TIGR01256, Molybdate-binding_periplasmic_protein, molybdenum ABC transporter, periplasmic molybdate-binding protein. The model describes the molybdate ABC transporter periplasmic binding protein in bacteria and archae. Several of the periplasmic receptors constitute a diverse class of binding proteins that differ widely in size, sequence and ligand specificity. It has been shown experimentally by radioactive labeling that ModA represent hydrophylioc periplasmic-binding protein in gram-negative organisms and its counterpart in gram-positive organisms is a lipoprotein. The other components of the system include the ModB, an integral membrane protein and ModC the ATP-binding subunit. Invariably almost all of them display a common beta/alpha folding motif and have similar tertiary structures consisting of two globular domains [Transport and binding proteins, Anions]
AASLTDALKEIAKQFEKRTGNKVVFSFGSSGTLYTQIENGAPADLFISADNKWPKKLVDKGLVVAGSRFT
YAGNKLVLISPKNRVVDDLDILKKWVADKRVAIGDPKHAPYGAAAKEVLQKLGLWETLKKKLVYGEDVRQ
ALQFVETGNAPAGIVALSDVIPSKKVGSVATFPEDLYKPIRYPAVIVKGGKNNAAAKAFIDYLKSPEAKE
ILRKYG
>gnl|CDD|130324 TIGR01257, Retinal-specific_ATP-binding_cassette_transporter, retinal-specific rim ABC transporter. This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease [Transport and binding proteins, Other]
MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWL
QGIFCNVNNPCFQSPTPGESPGIVSNYNNSILARVYRDFQELLMDAPESQHLGQVWAELRTLSQFMDTLR
THPERIAGRGIRIRDILKDEEALTLFLMKNIGLSDSVVYLLVNSQVRPEQFAYGVPDLELKDIACSEALL
ERFIIFSQRRGAQTVRDALCSLSQGTLQWIEDTLYANVDFFKLFHVLPTLLDSRSQGINLRSWGGILSDM
SPRIQEFIHRPSVQDLLWVTRPLLQNGGPETFTQLMGILSDLLCGYPEGGGSRVFSFNWYEDNNYKAFLG
IDSTRKDPIYSYDKRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKILFTPDSPAARRILKNANSTFEE
LERVRKLVKAWEEVGPQIWYFFDKSTQMTMIRDTLQNPTVKDFINRQLGEEGITAEAVLNFLYNGPREKQ
ADDMTNFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVFPDMYPWT
SSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQMQAEPPV
GIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTW
FLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYF
TLYLPHILCFAWQDRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSM
KMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPLTEEMEDPEHP
EGINDSFFERELPGLVPGVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLL
PPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTG
LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM
DEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGGCEGTCSCTSKGFSTRCPA
RVDEITPEQVLDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLS
SFGISDTPLEEIFLKVTEDADSGSLFAGGAQQKRENANLRHPCSGPTEKAGQTPQASHTCSPGQPAAHPE
GQPPPEPEDPGVPLNTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEY
PALTLHPWMYGQQYTFFSMDEPNSEHLEVLADVLLNKPGFGNRCLKEEWLPEYPCGNSTPWKTPSVSPNI
THLFQKQKWTAAHPSPSCRCSTREKLTMLPECPEGAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPA
LIRSSLKSKFWVNEQRYGGISIGGKLPAIPITGEALVGFLSDLGQMMNVSGGPVTREASKEMPDFLKHLE
TEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRDPEEYGITVISQPLNLTKEQLSEITVLTTSVDA
VVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQ
KKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLELFENNR
TLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYF
LLTLLIQHHFFLSRWIAEPAKEPIFDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVDRLCV
GVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGR
EHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTG
MDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMK
IKSPKDDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSLARIFQLLISHKDSLLIEEYSVTQTT
LDQVFVNFAKQQTETYDLPLHPRAAGASRQAK
>gnl|CDD|213596 TIGR01258, Phosphoglycerate_mutase_1, phosphoglycerate mutase, BPG-dependent, family 1. Most members of this family are phosphoglycerate mutase (EC 5.4.2.1). This enzyme interconverts 2-phosphoglycerate and 3-phosphoglycerate. The enzyme is transiently phosphorylated on an active site histidine by 2,3-diphosphoglyerate, which is both substrate and product. Some members of this family have are phosphoglycerate mutase as a minor activity and act primarily as a bisphoglycerate mutase, interconverting 2,3-diphosphoglycerate and 1,3-diphosphoglycerate (EC 5.4.2.4). This model is designated as a subfamily for this reason. The second and third paralogs in S. cerevisiae are somewhat divergent and apparently inactive (see PUBMED:9544241) but are also part of this subfamily phylogenetically
MKLVLVRHGESEWNALNLFTGWVDVKLSEKGQQEAKRAGELLKEEGYEFDVAYTSLLKRAIHTLNIALDE
LDQLWIPVKKSWRLNERHYGALQGLNKAETAAKYGEEQVNIWRRSFDVPPPPIDESDPRSPHNDPRYAHL
DPKVLPLTESLKDTIARVLPYWNDEIAPDLLSGKRVLIVAHGNSLRALVKHLEGISDEEILELNIPTGIP
LVYELDENLKPIKHYYLGDPEAAAAAAEAVANQGK
>gnl|CDD|213597 TIGR01259, ComE_operon_protein_1, comEA protein. This model describes the ComEA protein in bacteria. The com E locus is obligatory for bacterial cell competence - the process of internalizing the exogenous added DNA. Lesions in the loci has been variously described for the appearance of competence-related pheonotypes and impairment of competence, suggesting their intimate functional role in bacterial transformation [Cellular processes, DNA transformation]
GLRVWDAIEKAGGFTEQADGLSVNLAGKLMDEMFVYVPMKGEEAVSQQGTQSSAGKLAAVNINAASLEEL
QALPGIGPAKAKAIIEYREENGAFKSVDDLTKVSGIGEKSLEKLKDYATV
>gnl|CDD|130327 TIGR01260, ATP_synthase_subunit_c, ATP synthase, F0 subunit c. This model describes the subunit c in F1/F0-ATP synthase, a membrane associated multisubunit complex found in bacteria and organelles of higher eukaryotes, namely, mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. The functional role of subunit c, which is the part of F0 cluster, has been delineated in-vitro reconstitution experiments. Overall experimental proof exists that demonstrate the electrochemical gradient is converted into a rotational torque that leads to ATP synthesis [Energy metabolism, ATP-proton motive force interconversion]
AAIGAAIGIGILGGKFLESAARQPELKPLLRTTMFIGMGLVDAIPMIAVVIALILLFA
>gnl|CDD|130328 TIGR01261, Includes:_Histidinol-phosphatase, histidinol-phosphatase. This model describes histidinol phosphatase. All known examples in the scope of this model are bifunctional proteins with a histidinol phosphatase domain followed by an imidazoleglycerol-phosphate dehydratase domain. These enzymatic domains catalyze the ninth and seventh steps, respectively, of histidine biosynthesis [Amino acid biosynthesis, Histidine family]
QKILFIDRDGTLIEEPPSDFQVDALEKLRFEKGVIPALLKLKKAGYKFVMVTNQDGLGTPSFPQADFDGP
HNLMLQIFRSQGIIFDDVLICPHFPDDNCDCRKPKIKLLEPYLKKNLIDKARSYVIGDRETDMQLAENLG
IRGIQYDEEELNWDMIAEELL
>gnl|CDD|273527 TIGR01262, Maleylacetoacetate_isomerase, maleylacetoacetate isomerase. Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism [Energy metabolism, Amino acids and amines]
KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDGEQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIE
YLEETYPDPPLLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREKLGVEEEARNRWYQHWISKGFAA
LEALLQPHAGRFCVGDTPTLADLCLVPQVYNAERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP
>gnl|CDD|273528 TIGR01263, 4-hydroxyphenylpyruvate_dioxygenase, 4-hydroxyphenylpyruvate dioxygenase. This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine and phenylalanine catabolite, to homogentisate. Homogentisate can undergo a further non-enzymatic oxidation and polymerization into brown pigments that protect some bacterial species from light. A similar process occurs spontaneously in blood and is hemolytic (see . In some bacterial species, this enzyme has been studied as a hemolysin [Energy metabolism, Amino acids and amines]
DGFDFVEFYVGDAKQAARYYFTRLGFEKVAKETGHREKASTVLRQGQINLVLTAPLSPDSPAADFAAKHG
DGVKDVAFRVDDVAAAFEAAVERGAEPVQAPTEDEGDVWLATIKGIGDVVHTLVDRGGYKGSFYPGFFES
LLDAALHGPPPGVGLIAIDHLVGNVERGQMESWAEFYEKIFGFREFRSFDIKTEYSALNSIVMASPDGKV
KIPLNEPASGKDKSQIEEFLEFYNGAGVQHIALNTDDIVRTVRALRARGVEFLDTPDTYYDLLGERVGGH
VKEDLDTLRELNILIDGDEDGYLLQIFTKPLQDRGTLFFEIIQRKGAGGFGEGNFKALFEAIEREQERRG
VL
>gnl|CDD|273529 TIGR01264, tyrosine_aminotransferase, tyrosine aminotransferase, eukaryotic. This model describes tyrosine aminotransferase as found in animals and Trypanosoma cruzi. It is the first enzyme of a pathway of tyrosine degradation via homogentisate. Several plant enzyme designated as probable tyrosine aminotransferases are very closely related to an experimentally demonstrated nicotianamine aminotransferase, an enzyme in a siderophore (iron uptake chelator) biosynthesis pathway. These plant sequences are excluded from the model seed and score between the trusted an noise cutoffs [Energy metabolism, Amino acids and amines]
WSVKPSDHSKNTVNPIRAIVDNMKVKPNPEKPMIKLSIGDPTVFGNLPTDPEVMQAMKDSLDSGKYNGYA
PTVGALSAREAIASYYHNPDGPIEADDVVLCSGCSHAIEMCIAALANAGQNILVPRPGFPLYETLAESMG
IEVKLYNLLPDKSWEIDLKQLESLIDEKTAALIVNNPSNPCGSVFSRQHLEEILAVAERQCLPIIADEIY
GDMVFSGATFEPLASLSSTVPILSCGGLAKRWLVPGWRLGWIIIHDRRGILRDIRDGLVKLSQRILGPCT
IVQGALPSILLRTPQEYFDGTLSVLESNAMLCYGALAAVPGLRPVMPSGAMYMMVGIEMEHFPEFKNDVE
FTERLVAEQSVFCLPGSCFEYPGFFRVVLTVPVVMMEEACSRIQEFCERHY
>gnl|CDD|188123 TIGR01265, tyrosine_aminotransferase, tyrosine/nicotianamine family aminotransferase. This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley
WNFKGSDHSNKTVNPIRAIVDNLKVKPNPEKPVIPLSHGDPSVFGNLRTDPEAEEAVKDALRSGKFNGYA
PSVGALAAREAVAEYLSSDLPGKLTADDVVLTSGCSQAIEICIEALANPGANILVPRPGFPLYDTRAAFS
GLEVRLYDLLPEKDWEIDLDGLESLADEKTVAIVVINPSNPCGSVFSRDHLQKIAEVAEKLGIPIIADEI
YGHMVFGDAPFIPMASFASIVPVLSLGGISKRWVVPGWRLGWIIIHDPHGIFRDTVLQGLKNLLQRILGP
ATIVQGALPDILENTPQEFFDGKISVLKSNAELCYEELKDIPGLVCPKPEGAMYLMVKLELELFPEIKDD
VDFCEKLAREESVICLPGSAFGLPNWVRITITVPESMLEEACSRIKEFCERHA
>gnl|CDD|162276 TIGR01266, fum_ac_acetase, fumarylacetoacetase. This enzyme catalyzes the final step in the breakdown of tyrosine or phenylalanine to fumarate and acetoacetate [Energy metabolism, Amino acids and amines]
SFVPVAENSDFPIQNLPYGVFSTQANSSPRIGVAIGDQILDLSVIAHLFTGPALSKHQHVFDQSTLNAFM
ALGRPAWKEARARLQNLLSASQARLRDNAALRQRALTPQAEATMHLPAQIGDYTDFYSSIQHATNVGIMF
RGKENALLPNWKHLPVGYHGRASSIVVSGTPLRRPMGQTLPDNAKPPVFGPCKLLDMELEMAFFVGPGNR
LGEPIPISKAEEHIFGVVLMNDWSARDIQAWEYVPLGPFLAKSFGTTISPWVVPIDALEPFRVPNPKQDP
KPLPYLCHDAPYTFDINLEVSLKGEGMSEPATICRSNFKHMYWTMLQQLAHHSVNGCNLRPGDLLGSGTI
SGSEPGSFGSMLELSWKGKKPIDVAQGETRTFLEDGDEVILRGHCQGEGYRVGFGECAGKVLPAL
>gnl|CDD|130334 TIGR01267, Phe4hydrox_mono, phenylalanine-4-hydroxylase, monomeric form. This model describes the smaller, monomeric form of phenylalanine-4-hydroxylase, as found in a small number of Gram-negative bacteria. The enzyme irreversibly converts phenylalanine to tryosine and is known to be the rate-limiting step in phenylalanine catabolism in some systems. This family is of biopterin and metal-dependent hydroxylases is related to a family of longer, multimeric aromatic amino acid hydroxylases that have additional N-terminal regulatory sequences. These include tyrosine 3-monooxygenase, phenylalanine-4-hydroxylase, and tryptophan 5-monoxygenase [Energy metabolism, Amino acids and amines]
DFTDDQGFDHYSEEEHAVWNTLITRQLKLIEGRACQEYLDGIEQLGLPHDRIPDFDEINRKLQATTGWRI
AAVPGLIPFQTFFEHLANRRFPVTTWLRTPEELDYLQEPDIFHDIFGHVPLLTNPVFADFTHTYGKLGLK
ASALGRVEMLARLYWYTIEFGLVETDQGKRIYGAGILSSPKETVYSLESDEPLHVAFDLLEAMRTPYRID
IFQPLYFVLPSFKRLFDAAQEDFMALVHEAMDLGLHAP
>gnl|CDD|130335 TIGR01268, Probable_phenylalanine-4-hydroxylase_1, phenylalanine-4-hydroxylase, tetrameric form. This model describes the larger, tetrameric form of phenylalanine-4-hydroxylase, as found in metazoans. The enzyme irreversibly converts phenylalanine to tryosine and is known to be the rate-limiting step in phenylalanine catabolism in some systems. It is closely related to metazoan tyrosine 3-monooxygenase and tryptophan 5-monoxygenase, and more distantly to monomeric phenylalanine-4-hydroxylases of some Gram-negative bacteria. The member of this family from Drosophila has been described as having both phenylalanine-4-hydroxylase and tryptophan 5-monoxygenase activity (. However, a Drosophila member of the tryptophan 5-monoxygenase clade has subsequently been discovered
AEESYIADQVNENIAKTSLIFSLKEEAGALAETLKLFQAHDVNLTHIESRPSKTHPGEYEFFVEFDEASD
RKLEGVIEHLRQKAEVTVNILSRDNKQNKDSVPWFPRKINDIDRFANQILSYGAELDADHPGFKDPVYRA
RRKQFADIAFNYKHGQPIPRVEYTDEEIATWRTVFNNLTVLYPTHACQEYNHIFPLLQQNCGFREDNIPQ
LEDVSQFLQDCTGFTLRPVAGLLSSRDFLAGLAFRVFHSTQYIRHHSKPMYTPEPDICHELLGHVPLFAD
VEFAQFSQEIGLASLGAPDDYIEKLATLYWFTIEFGLCKQDGEKKAYGAGLLSSFGELQYCLSDKPEVVD
FDPEVTCVTKYPITEFQPLYFLAESFEDAKEKLKSFAATIPRPFSVRYNAYTQRVEILDKKAQLQRLADD
IRSEISILQEALGKLN
>gnl|CDD|130336 TIGR01269, Tyrosine_3-monooxygenase, tyrosine 3-monooxygenase, tetrameric. This model describes tyrosine 3-monooxygenase, a member of the family of tetrameric, biopterin-dependent aromatic amino acid hydroxylases found in metazoans. It is closely related to tetrameric phenylalanine-4-hydroxylase and tryptophan 5-monooxygenase, and more distantly related to the monomeric phenylalanine-4-hydroxylase found in some Gram-negative bacteria
KQSTVELARNEKDYGRIHSIIINFHPITHEQDSEAAMQNNQFYIRTKEISSLHRILKYIETFKLNLVHFE
TRPTRTLSNADVDYSCLITLEANEINMSLLIESLRGNSFISGINLLNNQNVKEDWFPKHISELDKCQHLL
TKFQPDLDTDHPGFHDKVYRQRREAIAEIAFQYKYGDPIPEVEYTKEEIETWRLVFTTMKDLHASHACRE
YIDAFQLLEKYCNYNSESIPQLQTISEFLHRTTGFRLRPVAGLLSARDFLASLAFRVFQCTQYIRHHSSP
MHTPEPDCIHELLGHMPMLADRQFAQFSQEIGLASLGASEEEIEKLSTLYWFTVEFGLCKENGETKAYGA
GLLSSYGELEHAFSDLSEKRPFNPNDAAVQPYQDQGYQKIYFVTESFEDAKRKLRNYINTSGRPFIVRFD
PITETVEVLDRFSKRKELLKHVKEEIGQLTTALNHLN
>gnl|CDD|130337 TIGR01270, Tryptophan_5-hydroxylase_1, tryptophan 5-monooxygenase, tetrameric. This model describes tryptophan 5-monooxygenase, a member of the family of tetrameric, biopterin-dependent aromatic amino acid hydroxylases found in metazoans. It is closely related to tetrameric phenylalanine-4-hydroxylase and tyrosine 3-monooxygenase, and more distantly related to the monomeric phenylalanine-4-hydroxylase found in some Gram-negative bacteria [Energy metabolism, Amino acids and amines]
EESTKQLFTPTRSVRREASIREGDEEEGVQRLSIIFSLSNVVGDLSKAIAIFQDRHINILHLESRDSKDG
TSKTMDVLVDVELFHYGLQEAMDLLKSGLDVHEVSSPIRPTLIEAQYTEPGSDDATTGVPWFPKKISDLD
KCANRVLMYGSELDADHPGFKDTEYRKRRMMFADLALNYKHGEPIPRVEYTEEERKTWGTIYRELRRLYK
THACKEFLDNLPLLEKYCGYREDNIPQLEDVSKFLKAKTGFRLRPVAGYLSARDFLSGLAFRVFHCTQYV
RHSADPFYTPEPDTCHELLGHMPLLADPSFAQFSQEIGLASLGASEEDIKKLATLYFFTIEFGLCKQDDE
QFKVYGAGLLSSVAELQHALSGSAKIKPFDPDRVCEQECLITTFQNAYFYTRSFEEAKEKMREFTNTIKR
PFGVRYNPYTESVEVLKNSKSITLAVNELRSDLNLVAGALHKIS
>gnl|CDD|273530 TIGR01271, CFTR_protein, cystic fibrosis transmembrane conductor regulator (CFTR). The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se [Transport and binding proteins, Anions]
MQRSPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNPKL
LNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLH
PAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVI
LLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEE
AMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALIKGIILRRIFTTISYCIVLRMT
VTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNVTASWDEGIGELFEKIKQNNKAR
KQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIS
FSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLA
RAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGT
FSELQAKRPDFSSLLLGLEAFDNFSAERRNSILTETLRRVSIDGDSTVFSGPETIKQSFKQPPPEFAEKR
KQSIILNPIASARKFSFVQMGPQKAQATTIEDAVREPSERKFSLVPEDEQGEESLPRGNQYHHGLQHQAQ
RRQSVLQLMTHSNRGENRREQLQTSFRKKSSITQQNELASELDIYSRRLSKDSVYEISEEINEEDLKECF
ADERENVFETTTWNTYLRYITTNRNLVFVLIFCLVIFLAEVAASLLGLWLITDNPSAPNYVDQQHANASS
PDVQKPVIITPTSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMK
AGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQ
QLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFV
FFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSG
GGGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKST
LLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEV
GLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSF
SNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAADRLKLFPLHRRNSSKRKP
QPKITALREEAEEEVQNTRL
>gnl|CDD|273531 TIGR01272, gluP, glucose/galactose transporter. This model describes the glucose/galactose transporter in bacteria. This belongs to the larger facilitator superfamily. Disruption of the loci leads to the total loss of glucose or galactose uptake in E.coli. Putative transporters in other bacterial species were isolated by functional complementation, which restored it functional activity [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
FGPAASQRYYVLFLGALFVLASGLTILQVAANPYVSILGPIETAASRLALTQAFNKLGTTVAPLFGGSLI
LSGAGDLSMQVATANAEAAKVHTPYLLLAGALAVLAIIFAFLPLPELQEADVARVSSGDTTQKTSAFQFT
HLVLGALGIFVYVGAEVSAGSFLVNFLSDPHALGLPEDQAAHFTAYTWGGAMVGRFIGSAVMPMISQGRY
LAFNAFLAVLLSIGAALTHGYVAMWFVLALGLFNSIMFPTIFSLALNALGRHTSQGSGILCLAIVGGAIV
PLLQGSLADCLGIQLAFALPVPCYLYILFY
>gnl|CDD|273532 TIGR01273, Biosynthetic_arginine_decarboxylase, arginine decarboxylase, biosynthetic. Two alternative pathways can convert arginine to putrescine. One is decarboxylation by this enzyme followed by removal of the urea moeity by agmatinase. In the other, the ureohydrolase (arginase) acts first, followed by ornithine decarboxylase. This pathway leads to spermidine biosynthesis, hence the gene symbol speA. A distinct biodegradative form is also pyridoxal phosphate-dependent but is not similar in sequence [Central intermediary metabolism, Polyamine biosynthesis]
WSASESRKTYNIAGWGAGYFAVNKLGNVSVRPGGDDTLQRIDLLELVKQVEARGLQLPLLVRFPDILQHR
IRSLNAAFKNAIEEYQYAGHYQGVYPIKVNQHRRVVEDIVASGKGEPYGLEAGSKPELMAAMAYATKPGA
PIVCNGYKDREYIELALIGRKLGHNVFIVIEKLSELDLVIDEAKKLGVKPKLGLRARLASKGSGKWASSG
GEKSKFGLSATQVLEVVRLLEQNGLLDSLQLLHFHIGSQISNIDDIKKGVREAARFYCELRKLGVKITYV
DVGGGLGVDYDGTSSSSDCSVNYGLEEYANDIVQALREICEEKGVPHPVIITESGRAITAHHAVLITNVL
GVERHEYDPDPKIAEDAPPLVRTLRELYGPIDRRSAIEILHDAQHLKEEAHEGFKLGYLDLEERAWAEQL
YLSICHKVHQLSAKNKDHRPILDELQERLADKYFVNFSVFQSLPDAWGIDQLFPIMPLERLDEKPTRRAV
LLDITCDSDGKIDQFIGGQGITSTLPLHELDPDEGYFLGFFLVGAYQEILGDMHNLFGDTSAVRVVFDGD
GGYEVELIREGDTTEDMLRYVQYDPKELLTLYRDKVANNKLDAEEKKQFLEELEAGLSGYPYLS
>gnl|CDD|130341 TIGR01274, 1-aminocyclopropane-1-carboxylate_deaminase, 1-aminocyclopropane-1-carboxylate deaminase. This pyridoxal phosphate-dependent enzyme degrades 1-aminocyclopropane-1-carboxylate, which in plants is a precursor of the ripening hormone ethylene, to ammonia and alpha-ketoglutarate. This model includes all members of this family for which function has been demonstrated experimentally, but excludes a closely related family often annotated as putative members of this family [Central intermediary metabolism, Other]
NLSRFPRYPLTFGPSPIHPLPRLSQHLGGKVTLYAKREDCNSGLAFGGNKTRKLEYLIPDAQAQGCTTLV
SIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQLSRIMGADVRLDPDGFDIGHRNSW
ERALEEVRGAGGKPYPIPAGCSDHPLGGLGFVGFAFEVREQEGELGFKFDYVVVCSVTGSTQAGMVAGFA
ADGRKDRVIGIDASATPEQTRAQILRIARNTAEKIGLERDITEDDVVLDTRFAYPEYGVPNEGTLEAIRL
CAKMEGVLTDPVYEGKSMHGMIEMIRRGEFKEGSNVLYAHLGGAPALNAYSFLFRTG
>gnl|CDD|273533 TIGR01275, ACC_deam_rel, pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family. This model represents a family of pyridoxal phosphate-dependent enzymes closely related to (and often designated as putative examples of) 1-aminocyclopropane-1-carboxylate deaminase. It appears that members of this family include both D-cysteine desulfhydrase (EC 4.4.1.15) and 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7)
LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHA
RATAAVAAKLGLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAETRIESCEEYTDIDAQLEELAERLEKE
GFKPYVIPVGGSNSLGALGYVEAALEIAQQLESEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVT
VSRFVADQTDKFVNLVQAIAEGLELTVSAVIPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTG
KAFYGLIDGIRKKEFGDKPILFIHTGGIPGLFAYHDHL
>gnl|CDD|130343 TIGR01276, Thiamine-binding_periplasmic_protein, thiamine ABC transporter, periplasmic binding protein. This model finds the thiamine (and thiamine pyrophosphate) ABC transporter periplasmic binding protein ThiB in proteobacteria. Completed genomes having this protein (E. coli, Vibrio cholera, Haemophilus influenzae) also have the permease ThiP, described by TIGRFAMs equivalog model TIGR01253 [Transport and binding proteins, Other]
KPVLTVYTYDSFAADWGPGPVVKKAFEADCNCELKLVALEDGVSLLNRLRLEGKNSKADVVLGLDNNLLD
AASKTGLFAKSGVAADAVNVPGGWNNDTFVPFDYGYFAFVYDKNKLKNPPQSLKELVESDQNWRVIYQDP
RTSTPGLGLLLWMQKVYGDDAPQAWQKLAKKTVTVTKGWSEAYGLFLKGESDLVLSYTTSPAYHILEEKK
DNYAAANFSEGHYLQVEVAARTAASKQPELAQKFLQFLVSPAFQNAIPTGNWMYPVANVTLPAGFEKLTK
PATTLEFTPAEVAAQRQAWISEWQRAVSR
>gnl|CDD|130344 TIGR01277, Thiamine_import_ATP-binding_protein_ThiQ, thiamine ABC transporter, ATP-binding protein. This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found [Transport and binding proteins, Other]
LALDKVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQR
PVSMLFQENNLFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALA
RCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV
SDC
>gnl|CDD|273534 TIGR01278, DPOR_BchB, light-independent protochlorophyllide reductase, B subunit. Alternate name: dark protochlorophyllide reductase This enzyme describes the B subunit of the dark form protochlorophyllide reductase, a nitrogenase-like enzyme. This subunit shows homology to the nitrogenase molybdenum-iron protein. It catalyzes a step in bacteriochlorophyll biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
MKLAYWMYEGPAHIGVLRIASSMKNVHAVMHAPQGDDYVNVMFSMLERTPNFPPVTTSVVDRRDLARGSQ
TRLVDTVRRVDDRFKPDLIVVTPSCTSSLLQEDLGNLAAAAGLDKSKVIVADVNAYRRKENQAADRTLTQ
LVRRFAKEQPKPGRTTEKPSVNLLGPASLGFHHRHDLIELRRLLKTLGIEVNVVAPWGASIADLARLPAA
WLNICPYREIGLMAAEYLKEKFGQPYITTTPIGVNATRRFIREIAALLNQAGADPYYESFILDGLSAVSQ
AAWFARSIDSQSLTGKRAFVFGDATHAVGMTKILARELGIHIVGAGTYCKYDADWVREQVAGYVDEVLIT
DDFQEVADAIAALEPELVLGTQMERHSAKRLDIPCGVISAPTHIQNFPLGYRPFLGFEGANVMADTVYNT
FKLGLEEHLLEMFGDAGHDTPAHLEPAATAAISSAPAPGELGWTAEAEAELKKVPFFVRGKVRRNTENFA
RERGYSVITLEVIYAAKEHFG
>gnl|CDD|273535 TIGR01279, DPOR_bchN, light-independent protochlorophyllide reductase, N subunit. This enzyme describes the N subunit of the dark form protochlorophyllide reductase, a nitrogenase-like enzyme involved in bacteriochlorophyll biosynthesis. This subunit shows homology to the nitrogenase molybdenum-iron protein NifN [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
REDGQYHTFCGLACVGWLYQKIKDSFFLIVGTHTCAHFLQNALGVMIFAEPRFAVALLEESDLSSAAPAE
ELDRVVEQIKRDRNPSVIFLLSSCTPEVIKMDLEGLAERLSTNFGVPVLFAPASGLDYTFTQGEDTVLAA
LVPFCPEAPASEQRALVLVGSVNDIVADQLRLELKQLGIPVVGFLPASHFTELPVIGPGTVVAPLQPYLS
DTATTLRRERGAKVLSAPFPFGPDGTRRFLEAIAAEFGIEVDKLSEREAQAWRALEPHTQLLRGKKIFFF
GDNLLELPLARFLKRCGMEVVECGTPYIHRRFHAAELALLEGGVRIVEQPDFHRQLQRIRATRPDLVVTG
LGTANPLEAQGFTTKWSIEFTFAQIHGFDNAADLAELFTRPLLRRTRLVELGWLEGI
>gnl|CDD|273536 TIGR01280, xseB, exodeoxyribonuclease VII, small subunit. This protein is the small subunit for exodeoxyribonuclease VII. Exodeoxyribonuclease VII is made of a complex of four small subunits to one large subunit. The complex degrades single-stranded DNA into large acid-insoluble oligonucleotides. These nucleotides are then degraded further into acid-soluble oligonucleotides [DNA metabolism, Degradation of DNA]
SFEEALAELEEIVEKLESGDLSLEESLKLYEEGIKLLKHCQKKLEEAEQKIEKL
>gnl|CDD|130348 TIGR01281, DPOR_bchL, light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein. The BchL peptide (ChlL in chloroplast and cyanobacteria) is an ATP-binding iron-sulfur protein of the dark form protochlorophyllide reductase, an enzyme similar to nitrogenase. This subunit resembles the nitrogenase NifH subunit [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
MILAVYGKGGIGKSTTSSNLSVAFAKLGKRVLQIGCDPKHDSTFTLTGRLIPTVIDVLQAVNYHYEDVRP
EDVIYTGYGGVDCVEAGGPPAGSGCGGYVVGETVKLLKEHHILDDYDVILFDVLGDVVCGGFATPLQYAD
YALVVAANDFDALFAANRIAASVQEKAKNYDVRLAGIIGNRSDATDLIERFNERVGMPVLGVVPDLEVIR
RSRVKGKTLFEMEESGPELAAVTQEYLRMAEYLLAGPEGVVPTPLIDREIFELLGGFD
>gnl|CDD|162284 TIGR01282, Nitrogenase_molybdenum-iron_protein_alpha_chain, nitrogenase molybdenum-iron protein alpha chain. Nitrogenase consists of alpha (NifD) and beta (NifK) subunits of the molybdenum-iron protein and an ATP-binding iron-sulfur protein (NifH). This model describes a large clade of NifD proteins, but excludes a lineage that contains putative NifD and NifD homologs from species with vanadium-dependent nitrogenases [Central intermediary metabolism, Nitrogen fixation]
LIDEVLEVYPEKAAKKRSKHLVVNEPEGKSDCGVKSNIKSVPGVMTIRGCAYAGSKGVVWGPIKDMVHIS
HGPVGCGQYSWGGRRNYYKGETGVDNFGTMQFTSDFQEKDIVFGGDKKLKKAIDEIEELFPLNKGISIQS
ECPVGLIGDDIEAVAKKASKELGKPVVPVRCEGFRGVSQSLGHHIANDAVRDWVLGKGDKEKFEPTPYDV
AIIGDYNIGGDAWESRILLEEIGLRVVAQWSGDGTLNEMENAPKAKLNLIHCYRSMNYISRHMEEKYGIP
WMEYNFFGPTKIAESLRKIAEFFDDEIKEKAEEVIAKYQPAVDAVIAKYRPRLEGKTVMLYVGGLRPRHV
IGAFEDLGMEVIGTGYEFAHNDDYERTTKYMKDGTLIYDDVTHYEFEEFVEKLKPDLVGSGIKEKYVFQK
MGVPFRQMHSWDYSGPYHGYDGFAIFARDMDMALNSPTWKLIKAPW
>gnl|CDD|188126 TIGR01283, nifE, nitrogenase molybdenum-iron cofactor biosynthesis protein NifE. This protein is part of the NifEN complex involved in biosynthesis of the molybdenum-iron cofactor used by the homologous NifDK complex of nitrogenase. In a few species, the protein is found as a NifEN fusion protein [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]
KKIKIAELLDEPACEHNKEKEEKGCKSGCANSLPGGATQRGCVFDGARIVLLPITDAAHLVHGPIGCAGS
SWDIRGSRSSGPELYRLGFTTDLTEKDVIFGGEKKLFHAIREIVERYHPPAVFVYSTCVPALIGDDLEAV
CKAAAEKTGIPVIPVDSEGFYGTKNLGNKLACDALLKHVIGTREPEPLPVGITVHDINLIGEFNVAGEFW
HVLPLLEKLGIRVLATITGDSRYAEVQTAHRAKLNMVQCSKAMINLARKMEEKYGIPYFEGSFYGIEDTS
KALRDIADLFGDPELLKRTEELIAREEAKIRPALEPYRERLKGKKAAIYTGGVKSWSVVSALQDLGMEVV
ATGTQKSTEEDYARIRELMGEGTVMLDDANPRELLKLLLEYKADILIAGGRERYTALKLGIPFLDINHER
EHPYAGYDGMVEFAREVDLTVESPIWQLVRQPA
>gnl|CDD|188127 TIGR01284, Nitrogenase_molybdenum-iron_protein_alpha_chain, nitrogenase alpha chain. This model represents the alpha chains of various forms of the nitrogen-fixing enzyme nitrogenase: vanadium-iron, iron-iron, and molybdenum-iron. Most examples of NifD, the molybdenum-iron type nitrogenase alpha chain, are excluded from this model and described instead by equivalog model TIGR01282. It appears by phylogenetic and UPGMA trees that this model represents a distinct clade of NifD homologs, in which arose several molybdenum-independent forms [Central intermediary metabolism, Nitrogen fixation]
ELFECDKEIPERKKHIYVKKQGEPEGDFLPACNTTTIPGCMSERGCAFCGAKGVIGGAIKDAIHVIHGPV
GCTYDTWHTKRYPTDNEKFNLKYITGTDLKESHVVFGGEKKLKRCILEAFREFPEIKRMYTYATCTTALI
GDDIDAIAREVMEEIPDVDVFAINAPGFAGPSQSKGHHVANITWINDKVGTAEPEITTEYDVNLIGEYNI
QGDLWVLKKYFERMGIQVLSTFTGNGCYDELRWMHRAKLNVVRCARSANYIANELEERYGIPRLDIDFFG
FEYCAKNLRKIGEFFGIEERAERVIEEEMAKWKPELDWYKERLRGKKVWVWSGGPKLWHWPRPLEDELGM
EVVAVSTKFGHEDDYEKIIARVREGTVIIDDPNELELEEIIEKYKPDIILTGIREGELAKKLGVPYINIH
SYHNGPYIGFEGFVNLARDMYNAIYNPVWDLLEFDID
>gnl|CDD|273537 TIGR01285, nifN, nitrogenase molybdenum-iron cofactor biosynthesis protein NifN. This protein forms a complex with NifE, and appears as a NifEN in some species. NifEN is a required for producing the molybdenum-iron cofactor of molybdenum-requiring nitrogenases. NifN is closely related to the nitrogenase molybdenum-iron protein beta chain NifK. This model describes most examples of NifN but excludes some cases, such as the putative NifN of Chlorobium tepidum, for which a separate model may be created [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]
ADILRTDKPLAVNPLKTSQPLGAALAFLGIEGAIPLFHGAQGCTAFAKVFFVRHFREPIPLQTTAMDEVS
TILGGDEHIEEAIDTLCQRNKPKAIGLLSTGLTETRGEDIARVVRQFREKHPQHKGTAVVTVNTPDFKGS
LEDGYAAAVESIIEAWVPPAPARAQRNRRVNLLVGSLLTPGDIEELRRMVEAFGLKPIILPDLSRSLDGH
LADDDFSPITQGGTTLEQIRQIGQSCCTLAIGESMRRAASLLADRCGVPYIVFPSLMGLEAVDAFLHVLM
KISGRAVPERFERQRRQLQDAMLDTHFFLGGKKVAIAAEPDLLAAWATFFTSMGAQIVAAVTTTGSPLLQ
KLPVETVVIGDLEDLEDLACAAGADLLITNSHGRALAQRLALPLVRAGFPLFDQLGSQRRCRIGYRGTRD
FLFDLANIMQAE
>gnl|CDD|130353 TIGR01286, Nitrogenase_molybdenum-iron_protein_beta_chain, nitrogenase molybdenum-iron protein beta chain. This model represents the majority of known sequences of the nitrogenase molybdenum-iron protein beta subunit. A distinct clade in a phylogenetic tree contains molybdenum-iron, vanadium-iron, and iron-iron forms of nitrogenase beta subunit and is excluded from this model. Nitrogenase, also called dinitrogenase, is responsible for nitrogen fixation. Note: the trusted cutoff score has recently been lowered to include an additional family in which the beta subunit is shorter by about 50 amino acids at the N-terminus. In species with the shorter form of the beta subunit, the alpha subunit has a novel insert of similar length [Central intermediary metabolism, Nitrogen fixation]
SQQVDKIKDHYPLFRDPEYQDMLAKKRDGFEEKYPQEKVQEVFEWTKTWEYREKNFAREALTVNPAKACQ
PLGAVLAALGFEGTMPFVHGSQGCVAYFRSHFNRHFKEPVSAVSSSMTEDAAVFGGLKNMVDGLQNCYAL
YKPKMIAVSTTCMAEVIGDDLNAFIGNAKKEGFIPDDFPVPFAHTPSFVGSHITGYDNMFKGILEYFTKG
SMDDKVVGSNGKINIIPGFETYIGNFREIKRILSLMGVGYTLLSDPEEVLDTPADGEFRMYAGGTTLEEM
KDAPNAEATVLLQPYTLRKTKEYIEKTWKQETPKLNIPLGVKGTDEFLMKVSEISGQPIPAELTKERGRL
VDAMTDSHAWLHGKRFAIYGDPDFVMGLVRFVLELGCEPVHILCTNGTKRWKAEMKALLAASPYGQNATV
WIGKDLWHLRSLVFTEPVDFLIGNSYGKYIQRDTLVPLIRIGFPIFDRHHLHRFPTIGYEGALQLLTTLV
NSILDELDRETRGMQVTDYSFDLVR
>gnl|CDD|273538 TIGR01287, Nitrogenase_iron_protein_2, nitrogenase iron protein. This model describes nitrogenase (EC 1.18.6.1) iron protein, also called nitrogenase reductase or nitrogenase component II. This model includes molybdenum-iron nitrogenase reductase (nifH), vanadium-iron nitrogenase reductase (vnfH), and iron-iron nitrogenase reductase (anfH). The model excludes the homologous protein from the light-independent protochlorophyllide reductase [Central intermediary metabolism, Nitrogen fixation]
RQIAIYGKGGIGKSTTTQNIAAALAEMGKKVMIVGCDPKADSTRLLLGGKAQPTVLDVLREKGAEDLELE
DVIKEGFGGIRCVESGGPEPGVGCAGRGVITAINLLEELGAYEDDLDFVFYDVLGDVVCGGFAMPIREGK
AQEIYIVTSGEMMALYAANNICKGILKYAKSGGVRLGGLICNSRNVDDEKELIDEFAKKLGTQLIHFVPR
SNIVQKAEIRKMTVIEYDPESEQANEYRELAKKIYENTEFVIPTPLTMDELEEILMKFGIMLKED
>gnl|CDD|130355 TIGR01288, Nod_factor_export_ATP-binding_protein_I, ATP-binding ABC transporter family nodulation protein NodI. This protein is required for normal nodulation by nitrogen-fixing root nodule bacteria such as Mesorhizobium loti. It is a member of the family of ABC transporter ATP binding proteins and works with NodJ to export a nodulation signal molecule. This model does not recognize the highly divergent NodI from Azorhizobium caulinodans [Cellular processes, Other, Transport and binding proteins, Other]
SNVAIDLVGVSKSYGDKVVVNDLSFTIARGECFGLLGPNGAGKSTIARMLLGMISPDRGKITVLGEPVPS
RARLARVAIGVVPQFDNLDPEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADVRVALLSGGM
KRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLES
GRKIAEGRPHALIDEQIGCNVIEIYGGDPDELRELIRPYARRIEVSGETLFCYARDPEQVRVQLRGRTDL
RLLQRPPNLEDVFLRLTGREMEK
>gnl|CDD|200089 TIGR01289, Light-dependent_protochlorophyllide_reductase, light-dependent protochlorophyllide reductase. This model represents the light-dependent, NADPH-dependent form of protochlorophyllide reductase. It belongs to the short chain alcohol dehydrogenase family, in contrast to the nitrogenase-related light-independent form [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
QQKPTVIITGASSGLGLYAAKALAATGEWHVIMACRDFLKAEQAAKSLGMPKDSYTIMHLDLGSLDSVRQ
FVQQFRESGRPLDALVCNAAVYFPTAKEPRFTADGFELSVGTNHLGHFLLCNLLLDDLKNSPNKDKRLII
VGSITGNTNTLAGNVPPKANLGDLSGLAAGFKAPIAMIDGKEFKGAKAYKDSKVCNMLTVRELHRRFHDE
TGITFASLYPGCIADTGLFREHVPLFRTLFPPFQKYITKGYVSEEEAGERLAQVVSDPKLKKSGVYWSWG
NRQESFVNQLSEEVSDDSKASKMWDLSEKLVGLA
>gnl|CDD|273539 TIGR01290, FeMo_cofactor_biosynthesis_protein_NifB, nitrogenase cofactor biosynthesis protein NifB. This model describes NifB, a protein required for the biosynthesis of the iron-molybdenum (or iron-vanadium) cofactor used by the nitrogen-fixing enzyme nitrogenase. NifB belongs to the radical SAM family, and the FeMo cluster biosynthesis process requires S-adenosylmethionine. Archaeal homologs lack the most C-terminal region and score between the trusted and noise cutoffs of this model [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]
VNPAIAEKIAQHPCYSVEAHHYFARMHLAVAPACNIQCNYCNRKYDCANESRPGVVSELLTPEQALRKAR
QVAAEIPQLSVVGIAGPGDPLANIGKTFQTLELVARQLPDVKLCLSTNGLMLPEHVDRLVDLGVGHVTIT
INAIDPAVGEKIYPWVWYEGERYTGREAADLLIERQLEGLEKLTERGILVKVNSVLIPGINDEHLVEVSK
QVKELGAFLHNVMPLISAPEHGTVYGLNGQREPDPDELAALRDRLEMGTPQMRHCHQCRADAVGLLGEDR
NADFPLETFPADEVYDLANRPQYLQELERRRRQTLHASIVARGGSEEADECLVAVATKGGGAVNQHFGHA
DEFTIFSLSAAGVMLIGQRKIDRYCRGPDDCEEDAAQNLDAIIELLSDCKALLCSRIGLTPRKALEAAGV
EPQVDYDGQPIETAIWENGGAV
>gnl|CDD|130358 TIGR01291, Nodulation_protein_J, ABC-2 type transporter, NodJ family. Nearly all members of this subfamily are NodJ which, together with NodI (TIGR01288), acts to export a variety of modified carbohydrate molecules as signals to plant hosts to establish root nodules. The seed alignment includes a highly divergent member from Azorhizobium caulinodans that is, nonetheless, associated with nodulation. This model is designated as subfamily in part because not all sequences derived from the last common ancestral sequence of Rhizobium sp. and Azorhizobium caulinodans NodJ are necessarily nodulation proteins [Cellular processes, Other, Transport and binding proteins, Other]
PERMVNWAAVWRRNALAWKKVAAASVLGNLADPLIYLFGLGVGLGKMVGSVDGVSYAAFLAAGMVATSAM
TASTFETIYATFARMRVTRTWEAMLYTPITVGDIVLGEVAWAATKASLAGTIIGVVTATLGYIEWWSLIY
ILPVIALTGLAFASLSMLVAALAPSYAYFAFYQSLVITPMLFLSGVVFPVFQLNDVIQGMTHFLPLAHSI
DDIRPVMLGGPGTQVGLHLGALCLYAVVPFFISAALLRRRLDD
>gnl|CDD|273540 TIGR01292, Thioredoxin_reductase, thioredoxin-disulfide reductase. This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070) [Energy metabolism, Electron transport]
DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFG
AEIIYEEVIKVDKSDRPFKVYTGDGKEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKN
KEVAVVGGGDSAIEEALYLTRIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDNKVEG
VKIKNTVTGEEEELEVDGVFIAIGHEPNTELLKGLLELDENGYIVTDEGMRTSVPGVFAAGDVRDKGYRQ
AVTAAGDGCIAALSAERYL
>gnl|CDD|213602 TIGR01293, potassium_channel_beta_2_subunit, voltage-dependent potassium channel beta subunit, animal. This model describes the conserved core region of the beta subunit of voltage-gated potassium (Kv) channels in animals. Amino-terminal regions differ substantially, in part by alternative splicing, and are not included in the model. Four beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions, and the structure of the complex is solved. The beta subunit belongs to a family of NAD(P)H-dependent aldo-keto reductases, binds NADPH, and couples voltage-gated channel activity to the redox potential of the cell. Plant beta subunits and their closely related bacterial homologs (in Deinococcus radiudurans, Xylella fastidiosa, etc.) appear more closely related to each other than to animal forms. However, the bacterial species lack convincing counterparts the Kv alpha subunit and the Kv beta homolog may serve as an enzyme. Cutoffs are set for this model such that yeast and plant forms and bacterial close homologs score between trusted and noise cutoffs
YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGW
RRSSYVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVIN
QGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLAC
GLVSGKYDSGIPPYSRATLKGYQWLKDKILSEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCLRNEGVS
SVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL
>gnl|CDD|273541 TIGR01294, Cardiac_phospholamban, phospholamban. This model represents the short (52 residue) transmembrane phosphoprotein phospholamban. Phospholamban, in its unphosphorylated form, inhibits SERCA2, the cardiac sarcoplasmic reticulum Ca-ATPase
MEKVQYLTRSAIRRASTIEMPQQARQKLQNLFINFCLILICLLLICIIVMLL
>gnl|CDD|273542 TIGR01295, Pediocin_PA-1_biosynthesis_protein_PedC, bacteriocin transport accessory protein, putative. This model describes a small family of proteins believed to aid in the export of various class II bacteriocins, which are ribosomally-synthesized, non-lantibiotic bacterial peptide antibiotics. Members of this family are found in operons for pediocin PA-1 from Pediococcus acidilactici and brochocin-C from Brochothrix campestris
YLDNIKGLEVTTVVRALEALDKKETATFFIGRKTCPYCRKFSGTLSGVVAQTKAPIYYIDSENNGSFEMS
SLNDLTAFRSRFGIPTSFMGTPTFVHITDGKQVSVRCGSSTTAQELQDIAAL
>gnl|CDD|273543 TIGR01296, Aspartate-semialdehyde_dehydrogenase, aspartate-semialdehyde dehydrogenase (peptidoglycan organisms). Two closely related families of aspartate-semialdehyde dehydrogenase are found. They differ by a deep split in phylogenetic and percent identity trees and in gap patterns. This model represents a branch more closely related to the USG-1 protein than to the other aspartate-semialdehyde dehydrogenases represented in model TIGR00978 [Amino acid biosynthesis, Aspartate family]
NVAIVGATGAVGQEMLKLLEERNFPIDKLVLLASARSAGRKLTFKGKELEVEEAETESFEGIDIALFSAG
GSVSKEFAPKAAKAGVIVIDNTSAFRMDPDVPLVVPEVNFEDLKEFNPKGIIANPNCSTIQMVVVLKPLH
DEAKIKRVVVSTYQAVSGAGNAGVEELYNQTKAVLEGAEQLPYIQPKANKFPYQIAFNAIPHIDSFVDDG
YTKEEQKMLFETRKIMGIPDLKVSATCVRVPVFTGHSESINIEFEKEISPEDARELLKNAPGVQLIDDPS
GNLYPTPLAAVGVDEVFVGRIRKDLPDGNGLHLWVVADNLRKGAALNSVQIAELLIKN
>gnl|CDD|273544 TIGR01297, Zinc_transporter, cation diffusion facilitator family transporter. This model describes a broadly distributed family of transporters, a number of which have been shown to transport divalent cations of cobalt, cadmium and/or zinc. The family has six predicted transmembrane domains. Members of the family are variable in length because of variably sized inserts, often containing low-complexity sequence [Transport and binding proteins, Cations and iron carrying compounds]
LLMLIKIVGGLLSGSLALLADAIHSLSDVAASAIALLALRISRRPADERHPFGHGRAEILAALLNGLFLV
VVALFILYEAIERLINPEPEIDGGTMLIVAIVGLIVNLILALYLHRVGHRLGSLALRAAALHVLSDALSS
VGVLIGALLIYFGWHWADPIAALLISLLILYTAFRLLKESINVLLDAAPDEEDLEEIKKAILSIPGVKGV
HDLHIWRIGPGKLFLDVHVVVDPDLDLKQAHDIALEIEREILKRHPGIEHVTIQVEPC
>gnl|CDD|188129 TIGR01298, Ribonuclease_T, ribonuclease T. This model describes ribonuclease T, an enzyme found so far only in gamma-subdivision Proteobacteria such as Escherichia coli and Xylella fastidiosa. Ribonuclease T is homologous to the DNA polymerase III alpha chain. It can liberate AMP from the common C-C-A terminus of uncharged tRNA. It appears also to be involved in RNA maturation. It also acts as a 3' to 5' single-strand DNA-specific exonuclease; it is distinctive for its ability to remove residues near a double-stranded stem. Ribonuclease T is a high copy suppressor in E. coli of a uv-repair defect caused by deletion of three other single-stranded DNA exonucleases [Transcription, RNA processing]
LARRFRGYLPVVVDVETGGFNAATDALLEIAAITLKMDEQGFLFPDHTYHFHIEPFEGANIEPEALEFTG
IDLDHPLRGAVQEEAALTEIFRGVRKAMKANGCQRAILVGHNASFDLGFLNAAVARTGIKRNPFHPFSSF
DTATLAGLAYGQTVLAKACQAAGMDFDNRQAHSALYDTEKTAELFCGIVNRWKELGGWPP
>gnl|CDD|130366 TIGR01299, synaptic_vesicle_protein_2C, synaptic vesicle protein SV2. This model describes a tightly conserved subfamily of the larger family of sugar (and other) transporters described by pfam00083. Members of this subfamily include closely related forms SV2A and SV2B of synaptic vesicle protein from vertebrates and a more distantly related homolog (below trusted cutoff) from Drosophila melanogaster. Members are predicted to have two sets of six transmembrane helices
MEDGFKDRAAFIKGAKDIAKEVKKHAAKKVNKALDRAQDEYSQRSYSRFEDEDDDDDFPAPADGYSRGEA
ADDEEEGEASSDATEGHDEDDEIYEGEYQGIPRAENGGKDEIMADGAPKAGVRDELKDGEGPPGGEGEAE
RRADEEELAQQYELIIQECGHGRFQWALFFVLGLALMADGVEVFVVGFVLPSAEKDLCIPDSGKGMLGLI
VYLGMMVGAFFWGGLADKLGRKQCLLICLSVNGFFAFFSSFVQGYGFFLFCRLLSGFGIGGAIPIVFSYF
AEFLAQEKRGEHLSWLCMFWMIGGIYAAAMAWAIIPHYGWSFQMGSAYQFHSWRVFVIVCAFPCVFAIGA
LTFMPESPRFFLENGKHDEAWMILKLIHDTNMRAKGHPEKVFSVNHIKTIHQEDELIEIESDTGTWYQRC
FVRALSEGGGIWGNFLRCFNPEVREITIKLMGVWFTLSFGYYGLSVWFPDMIKHLQADDYAALTKNFPGD
KVAHFSFNFTLENQIHRGGEYDNDKFIGLKFKSVSFEDSLFEECTFDDVTSSNTFFKNCTFIDTLFENTD
FEEYKFIDSEFQNCSFLHNKEGCPIDFDGDDEGAYMIYFVNFLGTLAVLPGNIVSALLMDKIGRLRMLAG
SMVLSCISCFFLSFGNSESAMIALLCLFGGLSIAAWNALDVLTVELYPSDKRATAFGFLNALCKAAAVLG
ILIFGSFVGITKAAPILFASAALACGGLLALKLPDTRGQVLM
>gnl|CDD|130367 TIGR01300, UPF0091_protein_PH1428, monovalent cation/proton antiporter, MnhG/PhaG subunit. This model represents a subfamily of small, transmembrane proteins believed to be components of Na+/H+ and K+/H+ antiporters. Members, including proteins designated MnhG from Staphylococcus aureus and PhaG from Rhizobium meliloti, show some similarity to chain L of the NADH dehydrogenase I, which also translocates protons [Transport and binding proteins, Cations and iron carrying compounds]
VLLLIGAFFTLLGAIGLVRFPDVYTRLHAATKGTTLGTILILLGVALIALVLDLAVSIKLLLIALFILLT
NPVGAHLLARAAYLSGVKPSRSVVDAL
>gnl|CDD|273545 TIGR01301, sucrose_transporter-like_protein, GPH family sucrose/H+ symporter. This model represents sucrose/proton symporters, found in plants, from the Glycoside-Pentoside-Hexuronide (GPH)/cation symporter family. These proteins are predicted to have 12 transmembrane domains. Members may export sucrose (e.g. SUT1, SUT4) from green parts to the phloem for long-distance transport or import sucrose (e.g SUT2) to sucrose sinks such as the tap root of the carrot
VPLRKLLRVASVAAGVQFGWALQLSLLTPYVQELGIPHAWASIIWLCGPLSGLLVQPLVGYLSDRCTSRF
GRRRPFIAAGAALVAFAVILIGFAADIGHLFGDNLDKKTKPRAIIVFVVGFWILDVANNMLQGPCRAFLA
DLTGGDARRTRIANAYFSFFMAIGNVLGYAAGAYSGLYKIFPFTKTEACGVSCANLKSCFLIDIILLAIL
TYIALSAVKENPLIGSDDFINSEAAPPSKHGEEAFFGELFGAFKYLPRPVWILLLVTCLNWIAWFPFILF
DTDWMGREVYGGSVNQGAKYDDGVRAGAFGLMLNSVVLGITSIGMEKLCRGWGAGKRLWGIVNIILAICL
AATVLVTYVAKNSRYYDGDGESLPPPTGIKASALIVFAILGIPLAITYSIPFALASIRSSNLGAGQGLSM
GVLNLAIVIPQIIVSLGSGPWDQLFGGGNLPAFVVGAVAAFVSGLLALILLPRPRVD
>gnl|CDD|273546 TIGR01302, Inosine-5'-monophosphate_dehydrogenase, inosine-5'-monophosphate dehydrogenase. This model describes IMP dehydrogenase, an enzyme of GMP biosynthesis. This form contains two CBS domains. This model describes a rather tightly conserved cluster of IMP dehydrogenase sequences, many of which are characterized. The model excludes two related families of proteins proposed also to be IMP dehydrogenases, but without characterized members. These are related families are the subject of separate models [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
GLTFDDVLLLPGFIDVEPDDVDLSTRITRNIKLNIPILSSPMDTVTESRMAIAMAREGGIGVIHRNMSIE
EQAEQVKRVKRAENGIISDPVTISPETTVADVLELMERKGISGIPVVEDGDMTGKLVGIITKRDIRFVKD
KGKPVSEVMTREEVITVPEGIDLEEALKVLHEHRIEKLPVVDKNGELVGLITMKDIVKRRKFPHASKDEN
GRLIVGAAVGTREFDKERAEALVKAGVDVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAK
ALIDAGADGLRVGIGPGSICTTRIVAGVGVPQITAVYDVAEYAAQSGIPVIADGGIRYSGDIVKALAAGA
DAVMLGSLLAGTTESPGEYEIINGRRYKQYRGMGSLGAMTKGSSDRYLQDENKTKKFVPEGVEGAVPYKG
SVLELLPQLVGGLKSGMGYVGARSIDELRE
>gnl|CDD|130370 TIGR01303, putative_inosine_monophosphate_dehydrogenase, IMP dehydrogenase family protein. This model represents a family of proteins, often annotated as a putative IMP dehydrogenase, related to IMP dehydrogenase and GMP reductase and restricted to the high GC Gram-positive bacteria. All species in which a member is found so far (Corynebacterium glutamicum, Mycobacterium tuberculosis, Streptomyces coelicolor, etc.) also have IMP dehydrogenase as described by TIGRFAMs entry TIGR01302 [Unknown function, General]
RFLNGHPPGYDLTYNDVFMVPSRSEVGSRFDVDLSTADGTGTTIPLVVANMTAVAGRRMAETVARRGGIV
ILPQDLPIPAVKQTVAFVKSRDLVLDTPITLAPHDTVSDAMALIHKRAHGAAVVILEDRPVGLVTDSDLL
GVDRFTQVRDIMSTDLVTAPADTEPRKAFDLLEHAPRDVAPLVDADGTLAGILTRTGALRATIYTPATDA
AGRLRIGAAVGINGDVGGKAKALLDAGVDVLVIDTAHGHQVKMISAIKAVRALDLGVPIVAGNVVSAEGV
RDLLEAGANIIKVGVGPGAMCTTRMMTGVGRPQFSAVLECAAEARKLGGHVWADGGVRHPRDVALALAAG
ASNVMVGSWFAGTYESPGDLMRDRDGRPYKESFGMASKRAVVARTGADNAFDRARKALFEEGISTSRMGL
DPDRGGVEDLIDHIISGVRSSCTYAGASSLEEFHERAVVGVQSGAGYAEGKPLPA
>gnl|CDD|273547 TIGR01304, Hypothetical_protein_Rv3410c/MT3518/Mb3444c., IMP dehydrogenase family protein. This model represents a family of proteins, often annotated as a putative IMP dehydrogenase, related to IMP dehydrogenase and GMP reductase. Most species with a member of this family belong to the high GC Gram-positive bacteria, and these also have the IMP dehydrogenase described by TIGRFAMs equivalog model TIGR01302 [Unknown function, General]
VEIGRGRTARRTYSLDDISVVPSRRTRSSKDVDTAWQIDAYRFELPFIAHPMDALVSPEFAIELGELGGL
GVLNLEGLWGRHEDPDPAIAKIAEAYEEGDQAAATRLLQELHAAPLKPELLGERIAEVRDSGVITAVRVS
PQNAREIAPIVVKAGADLLVIQGTLVSAEHVSTSGEPLNLKEFIGELDVPVIAGGVNDYTTALHLMRTGA
AGVIVGPGGANTTRLVLGIEVPMATAIADVAAARRDYLDETGGRYVHVIADGGIETSGDLVKAIACGADA
VVLGSPLARAAEAPGRGYFWPAAAAHPRLPRGVVTESGTVGEAPTLEEILHGPSTLPDGVENFEGGLKRA
MAKCGYTDLKEFQKVSLTV
>gnl|CDD|130372 TIGR01305, Probable_GMP_reductase, guanosine monophosphate reductase, eukaryotic. A deep split separates two families of GMP reductase. This family includes both eukaryotic and some proteobacterial sequences, while the other family contains other bacterial sequences [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSI
FTAIHKHYSVDEWKAFATNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEF
VKLVREAFPEHTIMAGNVVTGEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHG
LKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGG
VAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGAAKLKELSKRATFIRVTQQHNTVF
>gnl|CDD|130373 TIGR01306, GMP_reduct_2, guanosine monophosphate reductase, bacterial. A deep split separates two families of GMP reductase. The other (TIGR01305) is found in eukaryotic and some proteobacterial lineages, including E. coli, while this family is found in a variety of bacterial lineages [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
VFDYEDIQLIPNKCIVNSRSECDTSVTLGKHKFKLPVVPANMQTIIDEKLAEQLAENGYFYIMHRFDEES
RIPFIKDMQERGLFASISVGVKACEYEFVTQLAEEALTPEYITIDIAHGHSNSVINMIKHIKTHLPDSFV
IAGNVGTPEAVRELENAGADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTH
GDIAKSIRFGASMVMIGSLFAGHEESPGETVEKDGKLYKEYFGSASEFQKGEHKNVEGKKMFVEHKGSLS
DTLIEMQQDLQSSISYAGGKDLDSLRTVDYVIVKNSIFNGD
>gnl|CDD|130374 TIGR01307, pgm_bpd_ind, phosphoglycerate mutase (2,3-diphosphoglycerate-independent). This protein is about double in length of, and devoid of homology to the form of phosphoglycerate mutase that uses 2,3-bisphosphoglycerate as a cofactor [Energy metabolism, Glycolysis/gluconeogenesis]
KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGR
VVYQDLVRISQAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERGIEK
VVLHAFTDGRDTAPKSAESYLEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDGFEF
SDPVAYIQDAYARDITDEFIKPTIIGNGGALKDGDAVIFFNFRADRAREITRALVNSDFDGFPREKNPKL
DFVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAKHDLTQLRIAETEKYAHVTFFFNGGVEVPFAGETRTLI
PSPKVATYDLQPEMSAKAVTDAVLEAIAQGKFDLIVVNFANPDMVGHTGNFEAAIKAVEALDVCLGRIVE
ACKKVGGTLFLTADHGNAEEMIDENGNPHTAHTTNPVPFVCVGAKNVKLIREGGVLADIAPTILDLMGLE
QPAEMTGKSLL
>gnl|CDD|130375 TIGR01308, 50S_ribosomal_protein_L30, ribosomal protein L30, bacterial/organelle. This model describes bacterial (and organellar) 50S ribosomal protein L30. Homologous ribosomal proteins of the eukaryotic cytosol and of the archaea differ substantially in architecture, from bacterial L30 and also from each other, and are described by separate models [Protein synthesis, Ribosomal proteins: synthesis and modification]
IKVTLVRSLIGRPKKQRKTLKALGLRKIGRQVVHEDNPAIRGMVNKVKHLVKVEE
>gnl|CDD|130376 TIGR01309, 50S_ribosomal_protein_L30P, 50S ribosomal protein uL30, archaeal form. This model represents the archaeal ribosomal protein similar to longer (~ 250 residue) eukaryotic 60S ribosomal protein L7 and to the much shorter (~ 60 residue) bacterial 50S ribosomal protein L30. Protein naming follows the SwissProt designation as L30P, while the gene symbol rpmD follows TIGR usage [Protein synthesis, Ribosomal proteins: synthesis and modification]
LAVIRIRGTVDVPRDIADTLEMLRLHRVNHCVLYPETPTYLGMLQKVKDYVTWGEIDEDTLELLIRKRGR
LVGGDKVTDEYVKEVTGYESVDELAKALVEGEIKLSEAGLKPVFRLHPPRKGFKGGIKTPYRDGGELGYR
GEKINELLRRMR
>gnl|CDD|273548 TIGR01310, 60S_ribosomal_protein_L7-A, 60S ribosomal protein uL30, eukaryotic form. This model describes the eukaryotic 60S (cytosolic) ribosomal protein uL30 (previously L7) and paralogs that may or may not also be uL30. Human, Drosophila, and Arabidopsis all have both a typical L7 and an L7-related paralog. This family is designated subfamily rather than equivalog to reflect these uncharacterized paralogs. Members of this family average ~ 250 residues in length, somewhat longer than the archaeal L30P/L7E homolog (~ 155 residues) and much longer than the related bacterial/organellar form (~ 60 residues)
ELLLKKRKANQELAVAAAKQAKAKKKANKKKRKDYFKRAESFVKEYRKAERKIIRLKRLAKKPGKFYVPA
EHKLVFVIRIKGINGIPPKPRKVLRLLRLKQVHNGVFVKVNKATLEMLRIVEPYVAYGYPNLKSVRELIY
KRGFAKINGQRVPLTDNAIIEQHLGKYGIICIEDLIHEIYTVGPHFKEVNNFLWPFKLSSPVKGFGKRKK
VKHFIEGGDFGNREDHINELIKKMN
>gnl|CDD|273549 TIGR01311, Glycerol_kinase, glycerol kinase. This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases [Energy metabolism, Other]
PYILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDD
IAAIGITNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRW
LLDNVPGVREAAERGELLFGTIDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREI
LPEVRSSSEVYGYTDPGLLGAEIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKH
GLLTTVAYQLGGKKPVYALEGSVFVAGAAVQWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGA
PYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVEITKLRVDGGMTNNNLLMQFQA
DILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREARYAGWKEAVKRS
LGW
>gnl|CDD|273550 TIGR01312, Xylulose_kinase, D-xylulose kinase. This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see, was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization [Energy metabolism, Sugars]
LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKG
IGISGQMHGLVLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLALPGFTAPKLLWVRKH
EPEVFARIAKVMLPKDYLRYRLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEK
AGTVRPEVAARLGLSAGVPVAAGGGDNAAGAIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVHGF
CHALPGGWLPMGVTLSATSSLEWFRELFGKEDVEALNELAEQSPPGAEGVTFLPYLNGERTPHLDPQARG
SFIGLTHNTTRADLTRAVLEGVTFALRDSLDILREAGGIPIQSIRLIGGGAKSPAWRQMLADIFGTPVDV
PEGEEGPALGAAILAAWALGEKDLAALCSEAVVKQTESVLPIAENVEAYEELYERYKKLYQ
>gnl|CDD|273551 TIGR01313, Thermosensitive_gluconokinase, carbohydrate kinase, thermoresistant glucokinase family. This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases
FVLMGVAGSGKSTIASALAHRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKN
KVGIITCSALKRHYRDILREAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLADETD
VLRVDIDQPLEGVEEDCIAVVLK
>gnl|CDD|130381 TIGR01314, gntK_FGGY, gluconate kinase, FGGY type. Gluconate is derived from glucose in two steps. This model describes one form of gluconate kinase, belonging to the FGGY family of carbohydrate kinases. Gluconate kinase phosphoryates gluconate for entry into the Entner-Douderoff pathway [Energy metabolism, Sugars]
YMIGVDIGTTSTKAVLFEENGKIVAKSSIGYPLYTPASGMAEENPEEIFEAVLVTIREVSINLEDEDEIL
FVSFSTQMHSLIAFDENWQPLTRLITWADNRAVKYAEQIKESKNGFDIYRRTGTPIHPMAPLSKIIWLEA
EHPDIYQKAAKYLEIKGYIFQRLFGTYKIDYSTASATGMFNLFELDWDKEALELTGIKESQLPKLVPTTE
IEENLPHEYAKKMGIQSSTPFVIGASDGVLSNLGVNAIKKGEAAVTIGTSGAIRTVIDKPKTDEKGRIFC
YALTKEHWVIGGPVNNGGDVLRWARDEIFDSEIETATRLGIDPYDVLTEIAARVSPGADGLLFHPYLAGE
RAPLWNANARGSFFGLTYSHKKEHMIRAALEGVIYNLYTVALALVEVMGDPLNMIQATGGFASSEVWRQM
MSDIFEQEIVVPESYESSCLGACILGLKALGLIEDFSEVSTMVGTTETHTPIEKNFEIYREISPIFINLS
RSLLAEYEQIADFQR
>gnl|CDD|273552 TIGR01315, CG11594_isoform_A, FGGY-family pentulose kinase. This model represents a subfamily of the FGGY family of carbohydrate kinases. This subfamily is closely related to a set of ribulose kinases, and many members are designated ribitol kinase. However, the member from Klebsiella pneumoniae, from a ribitol catabolism operon, accepts D-ribulose and to a lesser extent D-arabinitol and ribitol (and JW Lengeler, personal communication); its annotation in GenBank as ribitol kinase is imprecise and may have affected public annotation of related proteins
HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLAESKVDPNSV
KGIGFDATCSLVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIP
KVLWLKNNMPPELFARCKFFDLTDFLTWRATGKEIRSFCSVVCKWGFVPVDGSNKGWQEDFYETIGLGEL
VTDNFIRMGGSWMSPGELVGGGLTAEAAQELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENGDVSQAFTR
LAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAEGGQSAAGELMDHMLETHVAYDETVKEAEAA
GKNIYDYLNEHLKEMAAKTNAPSISYLVRHFHVYPDLWGNRSPIADPNMRGVIIGLSMDRSKDGLALLYY
ATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPYVNEAVLHGAAMLGAK
AAGTTESLWDAMDRMSKPGKTVWPRGDPAKKLHDRKYEIFLQLARTQQEYR
>gnl|CDD|130383 TIGR01316, gltA, glutamate synthase (NADPH), homotetrameric. This protein is homologous to the small subunit of NADPH and NADH forms of glutamate synthase as found in eukaryotes and some bacteria. This protein is found in numerous species having no homolog of the glutamate synthase large subunit. The prototype of the family, from Pyrococcus sp. KOD1, was shown to be active as a homotetramer and to require NADPH [Amino acid biosynthesis, Glutamate family]
PPEERSKLFQEAALGYTEQLALVEAQRCLNCKDATKPCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTT
SLLPAICGRVCPQERQCEGQCTVGKMFKDVGKPVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIG
AGPAGLACASELAKAGHSVTVFEALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTA
TLEELFSQYDAVFIGTGAGLPKLMNIPGEELCGVYSANDFLTRANLMKAYEFPHADTPVYAGKSVVVIGG
GNTAVDSARTALRLGAEVHCLYRRTREDMTARVEEIAHAEEEGVKFHFLCQPVEIIGDEEGNVRAVKFRK
MDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSNPIMAETTRLKTSERGTIVVDEDQRTSIPGVFA
GGDIILGAATVIRAMGQGKRAAKSINEYL
>gnl|CDD|162300 TIGR01317, Glutamate_synthase, glutamate synthases, NADH/NADPH, small subunit. This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit or homologous region. TIGR01316 describes a family in several archaeal and deeply branched bacterial lineages of a homotetrameric form for which there is no large subunit. Another model describes glutamate synthase small subunit from gamma and some alpha subdivision Proteobacteria plus paralogs of unknown function. This model describes the small subunit, or homologous region of longer forms proteins, of eukaryotes, Gram-positive bacteria, cyanobacteria, and some other lineages. All members with known function participate in NADH or NADPH-dependent reactions to interconvert between glutamine plus 2-oxoglutarate and two molecules of glutamate
KPTGFLEYKRRKPTERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGTPFCHNDSGCPLNNLIPEFNDL
VFRGRWKEALDRLHATNNFPEFTGRVCPAPCEGACTLGISEDPVGIKSIERIIIDKGFQEGWVQPRPPSK
RTGKKVAVVGSGPAGLAAADQLNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDF
VTNTEIGVDISADELKEQFDAVVLAGGATKPRDLPIPGRELKGIHYAMEFLPSATKALLGKDFKDIIFIK
AKGKKVVVIGGGDTGADCVGTSLRHGAASVHQFEIMPKPPEARAKDNPWPEWPRVYRVDYAHEEAAAHYG
RDPREYSILTKEFIGDDEGKVTALRTVRVEWKKSQDGKWQFVEIPGSEEVFEADLVLLAMGFVGPEQILL
DDFGVKKTRRGNISAGYDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAVDRYLMGSSVLP
>gnl|CDD|273553 TIGR01318, glutamate_synthase_small_subunit_gltD, glutamate synthase small subunit family protein, proteobacterial. This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit and homologs. TIGR01317 describes the small subunit (or equivalent region from longer forms) in eukaryotes, Gram-positive bacteria, and some other lineages, both NADH and NADPH-dependent. TIGR01316 describes a protein of similar length, from Archaea and a number of bacterial lineages, that forms glutamate synthase homotetramers without a large subunit. This model describes both glutatate synthase small subunit and closely related paralogs of unknown function from a number of gamma and alpha subdivision Proteobacteria, including E. coli
FQFIDLPRQDPDKIPVEERKTDFREIYGPFDKGQAQYQADRCLDCGNPYCEWKCPVHNAIPQWLQLVQEG
RIDEAAELSHQTNTLPEICGRVCPQDRLCEGACTLNDEGGAVTIGNLERYITDTALAMGWRPDLSHVQPT
GKRVAVIGAGPAGLACADILARAGVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRL
NCEVGRDISLDDLLEDYDAVFLGVGTYRSMRGGLPGEDAPGVLPALPFLIANTRQLMGLPEEPEEPLIDV
EGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEANMPGSRREVANAREEGVEFLFNVQPVSIESDE
DGQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPHLMPWLAAHGITLDSWGRIITA
LSSGLTYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGILDWLGV
>gnl|CDD|130386 TIGR01319, glmL_fam, conserved hypothetical protein. This small family includes, so far, an uncharacterized protein from E. coli O157:H7 and GlmL from Clostridium tetanomorphum and Clostridium cochlearium. GlmL is located between the genes for the two subunits, epsilon (GlmE) and sigma (GlmS), of the coenzyme-B12-dependent glutamate mutase (methylaspartate mutase), the first enzyme in a pathway of glutamate fermentation. Members shows significant sequence similarity to the hydantoinase branch of the hydantoinase/oxoprolinase family (pfam01968)
LDFGSTWTKAAAFDIEGDAILATAHDITPIESDHLAGGFFNKANEKLNEDLAGKELNSGEVAKKACSSAA
GGLAMAAIGLVPEITAEAAKRAAHGAGAKIANVYAYDLNNKDIEAIEESNLDIILFAGGTDGGEEECGIH
NAKMLAEHGLDCAIIVAGNKDIQDEVQEIFDHADIFYRITDNVLPDLDHLNPEAAREAICDIFLKKIVEA
KGLDNAEDFIGEELMPTPAAVFEAAKAIAEGTDKDDGIGDFILIDIGGATTDVHSAAAGELSKPDTTLHG
LEEPFAKRTVEGDLGMRVSAISLGEASAKEKLNKNFADNPADLDACCHYLRHLAAHIDMLPANAEEIKFD
EALAGLATDMAMERHAGTIEEMCTCMGNIDLQIGKDLLNVKCVIGSGGVLSHASQFDMGEILKAGEFDDA
DARHLKPQEFEYYIDKRGILPALALLAEDDPDAAARIMIKCLT
>gnl|CDD|130387 TIGR01320, mal_quin_oxido, malate:quinone-oxidoreductase. This membrane-associated enzyme is an alternative to the better-known NAD-dependent malate dehydrogenase as part of the TCA cycle. The reduction of a quinone rather than NAD+ makes the reaction essentially irreversible in the direction of malate oxidation to oxaloacetate. Both forms of malate dehydrogenase are active in E. coli; disruption of this form causes less phenotypic change. In some bacteria, this form is the only or the more important malate dehydrogenase [Energy metabolism, TCA cycle]
TDVVLIGAGIMSATLGVLLRELEPNWSITLIERLDAVAAESSNPWNNAGTGHSALCELNYTPEMADGSID
IAKAVGINEQFQVSRQFWAHLVEEGILTDPKSFINPVPHVSFVHGSDGVAYLKKRYEALKGHPLFEGMEF
SEDPATFAEWLPLMAAGRDFSEPVAANWAAEGTDVDFGALTKQLLGYLVQNGTTIRFGHEVRNLKRQSDG
SWTVTVKNTRTGGKRTLNTRFVFVGAGGGALPLLQKSGIPEVKGFAGFPVSGLFLRCGNPELTEQHRAKV
YGQASVGAPPMSVPHLDTRVVDGKKWLLFGPYAGWSPKFLKHGSILDLPLSIRPDNLLSMLGVGLTEMDL
TKYLIGQLRKSEEERVSALREFYPEAIDSDWELIVAGQRVQVIKKDPEKGGGVLEFGTTLIADADGSIAG
LLGASPGASTAVSIMLDLLERCFPERYQSWLPKLKEMVPSYGKKLSSEPALFDEVWSRTTKVL
>gnl|CDD|130388 TIGR01321, Trp_operon_repressor_homolog, trp operon repressor, proteobacterial. This model represents TrpR, the repressor of the trp operon. It is found so far only in the gamma subdivision of the proteobacteria and in Chlamydia trachomatis. All members belong to species capable of tryptophan biosynthesis [Amino acid biosynthesis, Aromatic amino acid family, Regulatory functions, DNA interactions]
MSIQREQAWEAFLKLLKKADSEDDMQLLLELILTRSEREDLGDRIRIVNELLNGNMSQREIASKLGVSIA
TITRGSNNLKTMDPNFKQFLRKKI
>gnl|CDD|273554 TIGR01322, Sucrose-6-phosphate_hydrolase, sucrose-6-phosphate hydrolase [Energy metabolism, Biosynthesis and degradation of polysaccharides]
IEKLQPRALQSEWRPTFHIQPQTGLLNDPNGLIYFKGEYHLFYQWFPFGPVHGLKSWGHYTSKDLVHWED
EGVALAPDDPYDSHGCYSGSAVDNNGQLTLMYTGNVRDSDWNRESYQCLATMDDDGHFEKFGIVVIELPP
AGYTAHFRDPKVWKHNGHWYMVIGAQTETEKGSILLYRSKDLKNWTFVGEILGDGQNGLDDRGYMWECPD
LFSLDGQDVLLFSPQGLDASGYDYQNIYQNGYIVGQLDYEAPEFTHGTEFHELDYGFDFYAPQTFLAPDG
RRILVAWMGLPEIDYPTDRDGWAHCMTLPRELTLKDGKLVQTPLRELKALRTEEHINVFGDQEHTLPGLN
GEFELILDLEKDSAFELGLALTNKGEETLLTIDADEGKVTLDRRSSGNLEDYGGTRSCPLPNTKKVSLHI
FIDKSSVEIFINDGEEVMTSRIFPD
>gnl|CDD|188130 TIGR01323, nitrile_alph, nitrile hydratase, alpha subunit. This model describes both iron- and cobalt-containing nitrile hydratase alpha chains. It excludes the thiocyanate hydrolase gamma subunit of Thiobacillus thioparus, a sequence that appears to have evolved from within the family of nitrile hydratase alpha subunits but which differs by several indels and a more rapid accumulation of point mutations [Energy metabolism, Amino acids and amines]
ADSALRVRALESLLIEKGLITEAAVDGVIDTFENRMGPANGAKVVARAWTDPEFRERLLADGTAAIAELG
YTGPQGEHMVAVENTPEVHNVIVCTLCSCYPWPVLGLPPYWYKSPEYRSRAVREPRGVLAEFGVELPEDV
EVRVWDSSAETRYLVLPMRPAGTEGWSEEQLAELVTRDSMIGVALPKAP
>gnl|CDD|130391 TIGR01324, Cystathionine_beta-lyase, cystathionine beta-lyase, bacterial. This model represents cystathionine beta-lyase (alternate name: beta-cystathionase), one of several pyridoxal-dependent enzymes of cysteine, methionine, and homocysteine metabolism. This enzyme is involved in the biosynthesis of Met from Cys [Amino acid biosynthesis, Aspartate family]
TRLIHSGRQPRFSQGSVNPPLQRASTVLFDSHAAQRRAKGELTYGRRGTLTHFALQDAMCELEGGAGCYL
YPSGLAAVTNSILAFVKAGDHVLMVDSAYEPTRYFCDIVLKRMGVDITYYDPLIGEDIATLIQPNTKVLF
LEAPSSITFEIQDIPAIAKAARNPGIVIMIDNTWAAGLLFKPLEHGVDISIQAGTKYLVGHSDIMIGTVV
ANARTWDQLREHSYLMGQMVDADDAYTTLRGLRTLGVRLKQHQESSLAIAKWLSEQPEVARVLHPALPSC
PGHEFWKRDFSGSSGLFSFVLQRLTQKQVHAFLDHLQLFGLGYSWGGYESLALCNQPELGHRPNIKRNLE
GPLIRVHIGLENVDDLKADLKAGFEAI
>gnl|CDD|188131 TIGR01325, O_suc_HS_sulf, O-succinylhomoserine sulfhydrylase. This model describes O-succinylhomoserine sulfhydrylase, one of several related pyridoxal phosphate-dependent enzymes of cysteine and methionine metabolism. This enzyme is part of an alternative pathway of homocysteine biosynthesis, a step in methionine biosynthesis [Amino acid biosynthesis, Aspartate family]
ATLAVRGGMLRSGFEETAEALYLTSGYVYDSAAVAAKRFAGELPGFVYSRYGNPTVSVFEERLALLEGAE
AAVATASGMAAIFAALMALLGAGDHVVASRSLFGSCFVVCSEILPRFGVQTVFVDGTDLSAWEAALKPNT
KAVFVETPSNPLQELVDIAAVAELAHAAGAKVVVDNVFATPLLQQPLKLGADVVVYSATKHIDGQGRVLG
GAILGSEEYMDEPVQKLLRHTGPAMSPFNAWVLLKGLETLAIRVQHQNASALAIAEWLNGHPSVQWVYYP
GLPSHPQHELAKRQMSGGGTVVTFDLDCRQAAFKVLDAMRLVDISNNLGDAKSTITHPATTTHRRMGPEE
RAAAGIGDGLVRLSVGLEDVDDLIADIDRAL
>gnl|CDD|273555 TIGR01326, Includes:_O-acetylhomoserine_sulfhydrylase, OAH/OAS sulfhydrylase. This model describes a distinct clade of the Cys/Met metabolism pyridoxal phosphate-dependent enzyme superfamily. Members include examples of OAH/OAS sulfhydrylase, an enzyme with activity both as O-acetylhomoserine (OAH) sulfhydrylase (EC 2.5.1.49) and O-acetylserine (OAS) sulphydrylase (EC 2.5.1.47). An alternate name for OAH sulfhydrylase is homocysteine synthase. This model is designated subfamily because it may or may not have both activities [Amino acid biosynthesis, Aspartate family, Amino acid biosynthesis, Serine family]
HFETLQLHAGQEPDPTTGSRAVPIYQTTSYVFDSTEHAAALFGLQEPGNIYSRLMNPTTDVLEQRIAALE
GGVAALAVASGQAAITYAILNLAGAGDNIVSSSYLYGGTYNLFSHTLKRLGIEVRFVDPDDPESLEKAID
ENTKAVFAETIGNPQINVLDIEAIAEVAHRHGIPLIVDNTFATPYLCRPIKHGADIVVHSATKYIGGHGT
AIGGVIVDGGKFDWNNGRFPLFTTPDPSYHGLVFTETLGNPAFILKARVQLLRDLGAALSPFNAFLLLQG
LETLSLRMERHVENALKVAEFLESHPDVAWVNYPGLASHPHHALAKKYLPKGFGAVLSFEIKGGREAGKK
FIDALKLASHLANVGDAKSLVIHPASTTHSQLSEEEQLKAGVTPGLIRLSVGIENIDDIIADLEQALE
>gnl|CDD|273556 TIGR01327, D-3-phosphoglycerate_dehydrogenase, D-3-phosphoglycerate dehydrogenase. This model represents a long form of D-3-phosphoglycerate dehydrogenase, the serA gene of one pathway of serine biosynthesis. Shorter forms, scoring between trusted and noise cutoff, include SerA from E. coli [Amino acid biosynthesis, Serine family]
KVLIADPISPDGIDILEDVGVEVDVQTGLSREELLEIIPDYDALIVRSATKVTEEVIAAAPKLKVIGRAG
VGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEGEWDRKAFMGTELYGKT
LGVIGLGRIGSIVAKRAKAFGMKVLAYDPYISPERAEQLGVELVDDLDELLARADFITVHTPLTPETRGL
IGAEELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKEPPTDNPLFDLDNVIATPHLGA
STREAQENVATQVAEQVLDALKGLPVPNAVNAPGIDADVMEKLKPYLDLAEKLGKLAGQLLDGAVQSVEV
TYRGELATENSEPLTRAALKGLLSPVLDDEVNMVNAPAVAKERGITVEESKSESSPDYKNYLSVTVTGDS
GTVSVAGTVFGGFSPRIVEIDGFHVDLEPEGIMLIILHLDKPGVIGKVGTLLGTAGINIASMQLGRKEKG
GEALMLLSLDQPVPDEVLEEIKAIPDILSVFVVDL
>gnl|CDD|130395 TIGR01328, methionine_gamma-lyase, methionine gamma-lyase. This model describes a methionine gamma-lyase subset of a family of PLP-dependent trans-sulfuration enzymes. The member from the parasite Trichomonas vaginalis is described as catalyzing alpha gamma- and alpha-beta eliminations and gamma-replacement reactions on methionine, cysteine, and some derivatives. Likewise, the enzyme from Pseudomonas degrades cysteine as well as methionine [Energy metabolism, Amino acids and amines]
RMTFATRAIHAGYPPKDQFGALTPPIYQTSTFVFDSCEQGGNRFAGQESGYIYSRLGNPTVSNLEGRIAF
LEGTEAAVATSSGMGAIAATLLTILKAGDHLISDECLYGCTFALLEHALTKFGIQVDFINMAIPEEVKAH
IKDNTKIVYFETPANPTMKLIDMERVCRDAHSQGVKVIVDNTFATPMLTNPVALGVDVVVHSATKYIGGH
GDVVAGLICGKAELLQQIRMVGIKDMTGSVISPFDAWLILRGLKTLNIRMKRHSENAMKVAEYLKSHPAV
EKVYYPGFEDHPGHDIAAKQMRMGGGMITFELKGGFAGAKKLLNNLKLIRLAVSLGDAETLIQHPASMTH
AVVPKEEREAAGITDGMIRLSVGLEDADDLIADLKQALDAL
>gnl|CDD|273557 TIGR01329, Cystathionine_beta-lyase_chloroplastic, cystathionine beta-lyase, eukaryotic. This model represents cystathionine beta-lyase (alternate name: beta-cystathionase), one of several pyridoxal-dependent enzymes of cysteine, methionine, and homocysteine metabolism. This enzyme is involved in the biosynthesis of Met from Cys
LSTLLVNTDNKNDPYDASSMPIYQTATFKQPLAIENGPYDYTRSGNPTRTALESLLAKLDKADRAFAFSS
GMAALDVITRLLNNGDEIIAGDDLYGGTDRLLTQVVPRSGVVVVHVDTTDLDKVKAALGPKTKLVLLESP
TNPLQKIVDIRKISEMAHAQNALVVVDNTMMSPLLCNPLELGADIVYHSATKFLAGHSDVMAGVLAVKGE
EIAKKVYFLQNSTGSGLAPFDCWLLLRGIKTLAIRIEKQQENARAIAMFLSTHPRVKKVRYAGLPSHPGF
HLHFSQAKGAGSVLSFETGSVALSKRLVEATKLFSITVSFGSVNSLISMPCFMSHASIPAEVREERGLPE
DLVRLSVGIEDVDDLISDLDIAFVTAPA
>gnl|CDD|273558 TIGR01330, 3'2'5'-bisphosphate_nucleotidase, 3'(2'),5'-bisphosphate nucleotidase, HAL2 family. Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in plants of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. Sensitivity of this essential enzyme to sodium and other metal ions results is responsible for characterization of this enzyme as a salt tolerance protein. Some members of this family are active also as inositol 1-monophosphatase
ALERELDVATQAVRLASLLTKKVQSELISHKDSTVITKDDKSPVTVGDYGAQAIVINVLKSNFPDDPIVG
EEDSSGLSEADFTLGRVNELVNETLVYAKNYKKDDQFPLKSLEDVLQIIDFGNYEGGRKGRHWVLDPIDG
TKGFLRGDQYAVCLALIENGKVVLGVIGCPNLPLSSYGAQNLKGSESKGCIFRAVRGSGAFMYSLSSDAE
SPTKVHVSSVKDTKDAIFCEGVEKGHSSHDEQTAIANKLGISKSPLRLDSQAKYAALARGDADVYLRLPI
KLSYQEKIWDHAAGNVIVEEAGGIVTDAMGKPLDFGKGRTLALDKGVIAASGPRVLHDLVVSTSCDSIQS
RNA
>gnl|CDD|130398 TIGR01331, 3'2'5'-bisphosphate_nucleotidase_CysQ, 3'(2'),5'-bisphosphate nucleotidase, bacterial. Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in bacteria of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle [Central intermediary metabolism, Sulfur metabolism]
MLDDVIKIARAAGEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLT
PRQTWQRFWLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQAL
KAPIHVRPWPSGPLLVVISRSHAEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDT
AAGHAVLAAAGGAIFDLDGSPLLYGKRESFRNPNFVALG
>gnl|CDD|130399 TIGR01332, Cytochrome_b559_subunit_alpha, cytochrome b559, alpha subunit. This model describes the alpha subunit of cytochrome b559, about 83 residues in length. The N-terminal half is homologous to the ~ 40-residue beta subunit. Cytochrome b559 is associated with photosystem II. Sequences scoring between trusted and noise cutoffs are fragments [Energy metabolism, Photosynthesis]
SGTTGERPFSDIVTSIRYWVIHSITIPMLFIAGWLFVSTGLAYDAFGTPRPNEYFTQTRQELPLLQDRFD
ANQEIQEFNQ
>gnl|CDD|130400 TIGR01333, Cytochrome_b559_subunit_beta, cytochrome b559, beta subunit. This model describes the beta subunit of cytochrome b559, about 40 residues in length. It is homologous to the N-terminal half of the alpha subunit, a protein of about 83 residues. Cytochrome b559 is associated with photosystem II [Energy metabolism, Photosynthesis]
MAAKPLKPISYPIFTFRWLAIHALAIPTVFFFGAITAMQFIQR
>gnl|CDD|130401 TIGR01334, molybdenum_transport_system_protein, putative molybdenum utilization protein ModD. The gene modD for a member of this family is found with molybdenum transport genes modABC in Rhodobacter capsulatus. However, disruption of modD causes only a 4-fold (rather than 500-fold for modA, modB, modC) change in the external molybdenum concentration required to suppress an alternative nitrogenase. ModD proteins are highly similar to nicotinate-nucleotide pyrophosphorylase (also called quinolinate phosphoribosyltransferase). The function unknown [Unknown function, General]
LPISTGLIDNLLLEDIGYGDLTTRALGIQDHPAHITFTARDEGIVSGVSEAAKLLKQLGASIDYAVPSGS
RALAGTLLLEAKGSAGQLHQGWKSAQSVLEWSCGVATYTHKMVTLAKKISPMAVVACTRKAIPLTRPLAV
KAVLAAGGVIHRIGLSETLLVFANHRTFLNDNFDWGGAIGRLKQTAPERKITVEADTIEQALTVLQASPD
ILQLDKFTPQQLHHLHERLKFFDHIPTLAAAGGINPENIADYIEAGIDLFITSAPYYAAPCDIKVKL
>gnl|CDD|130402 TIGR01335, Photosystem_I_P700_chlorophyll_a_apoprotein_A1, photosystem I core protein PsaA. The core proteins of photosystem I are PsaA and PsaB, homologous integral membrane proteins that form a heterodimer. The heterodimer binds the electron-donating chlorophyll dimer P700, as well as chlorophyll, phylloquinone, and 4FE-4S electron acceptors. This model describes PsaA only [Energy metabolism, Photosynthesis]
MTISPPEREQKTAKILVDRDPVPTSFEKWAKPGHFSRTLAKGPKTTTWIWNLHADAHDFDSHTSDLEDIS
RKIFSAHFGQLSVIFIWLSGMYFHGARFSNYEAWLSDPTHIKPSAQVVWPIVGQEILNGDVGGGFHGIQI
TSGFFQLWRASGITNELQLYVTAIGGLVMAGLMLFAGWFHYHKAAPKLEWFQNVESMLNHHLAGLLGLGS
LSWAGHQIHVSLPINKLLDAGVDPKDIPLPHEFILNRELMAQLYPSFASGLTPFFTLNWGAYSDFLTFRG
GLNPVTGGLWLSDIAHHHLAIAVLFIIAGHMYRTNWGIGHSIKEILEAHKGPFTGSGHKGLYEALTTSWH
AQLAINLAMLGSLSIIVAHHMYAMPPYPYLATDYPTQLSLFTHHMWIGGFLIVGAAAHGAIFMVRDYDPS
QNYNNVLDRVIRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMRALGRPQDMFSDTAIQLQPVFAQWIQNL
HTLAPGNTAPNALATTSYAFGGEVVAVGGKVAMMPIKLGTADFMVHHIHAFTIHVTVLILLKGVLFARNS
RLIPDKANLGFRFPCDGPGRGGTCQVSGWDHVFLGLFWMYNCISVVIFHFSWKMQSDVWGTVSQNGLVSH
ITGGNFAQSAITINGWLRDFLWAQASQVIQSYGSSLSAYGLMFLGAHFIWAFSLMFLFSGRGYWQELIES
IVWAHNKLKVAPAIQPRALSIIQGRAVGVAHYLLGGIATTWAFFLARIISVG
>gnl|CDD|130403 TIGR01336, Photosystem_I_P700_chlorophyll_a_apoprotein_A2, photosystem I core protein PsaB. The core proteins of photosystem I are PsaA and PsaB, homologous integral membrane proteins that form a heterodimer. The heterodimer binds the electron-donating chlorophyll dimer P700, as well as chlorophyll, phylloquinone, and 4FE-4S electron acceptors. This model describes PsaB only [Energy metabolism, Photosynthesis]
ATKFPKFSQDLAQDPTTRRIWYGIATAHDFESHDGMTEENLYQKIFASHFGHLAIIFLWTSGNLFHVAWQ
GNFEQWIQDPLHVRPIAHAIWDPHFGQPAVEAFTRGGANYPVNISYSGVYHWWYTIGMRTNSDLYAGALF
LLILAALCLFAGWLHLQPKFKPSLSWFKNAESRLNHHLSGLFGVSSLAWAGHLIHVAIPASRGQHVGWNN
FLSTLPHPAGLKPFFTGNWGVYAQNPDTASHVFGTSQGSGTAILTFLGGFHPQTQSLWLTDMAHHHLAIA
VIFIIAGHMYRTNFGIGHSIKDMLEAHKPPPSGKFGLGHKGLYDTINNSLHFQLGLALACLGVITSLVAQ
HMYSLPPYAFIAQDFTTQAALYTHHQYIAGFLMVGAFAHGAIFFVRDYDPEQNKDNVLDRMLEHKEAIIS
HLSWVSLFLGFHTLGLYVHNDVVVAFGTPEKQILIEPIFAQWIQAAHGKTLYGFNVLLSSPSSSATTAYG
SVWLPGWLDAINSNTNSLFLTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCD
GPGRGGTCDISAWDAFYLAVFWMLNTIGWVTFYWHWKHITIWQGNVSQFNESSTYLMGWFRDYLWLNSSQ
LINGYNPYGMNNLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLVWAHERTPLANLIRWKDKPVAL
SIVQARLVGLAHFSVGYVLTYAAFLIASTAGKFG
>gnl|CDD|273559 TIGR01337, Allophycocyanin_subunit_beta-18, allophycocyanin, beta subunit. The alpha and beta subunits of allophycocyanin form heterodimers, six of which associate into larger aggregates as part of the phycobilisome, a light-harvesting complex of phycobiliproteins and linker proteins. This model describes allophycocyanin beta subunit. Other, homologous phyobiliproteins include allophycocyanin alpha chain and the phycocyanin and phycoerythrin alpha and beta chains [Energy metabolism, Photosynthesis]
QDAITNIINAYDLTGKYLDDNAVTKLKGYFQTGELRLRAAAIINANSATIIKEAAAQLFEEYPELIRPGG
NAYTTRRYAACLRDIDYYLRYATYAIIAGDNSILEERVLNGLKETYNSLGVPIGPTVRAIQIMKEVIISL
VGPDNDAGKEIGEPFDYMCSGLSENDV
>gnl|CDD|130405 TIGR01338, C-phycocyanin_alpha_chain, phycocyanin, alpha subunit. This model describes the phycocyanin alpha subunit. Other, homologous phyobiliproteins of the phycobilisome include phycocyanin alpha chain and the allophycocyanin and phycoerythrin alpha and beta chains. This model excludes the closely related phycoerythrocyanin alpha subunit [Energy metabolism, Photosynthesis]
KTPITEAIAAADSQGRFLSNGELQSIFGRFQRATASLEAAKSLTSNAQRLISGAAQAVYSKFPYTTQMNG
PNYASTATGKAKCARDIGYYLRMVTYCLVVGGTGPLDEYLIAGLEEINRSFDLSPSWYVEALKYIKANHG
LSGQAANEANTYLDYAINALS
>gnl|CDD|273560 TIGR01339, C-phycocyanin_subunit_beta, phycocyanin, beta subunit. This model describes the phycocyanin beta subunit. Other, homologous phycobiliproteins of the phycobilisome include phycocyanin beta chain and the allophycocyanin and phycoerythrin alpha and beta chains. This model excludes the closely related phycoerythrocyanin beta subunit [Energy metabolism, Photosynthesis]
FDAFTRVVSQADARGEFISSDKIDALKKVVSEGNKRSDAVSRITNNASSIVTNAARQLFADQPQLIAPGG
NAYTSRRMAACLRDMEIILRYVTYATFTGDASVLEDRCLNGLRETYLALGTPGASVAAGVRAMKDAALAI
VNDPAGITSGDCSSLQQEIETYFDRAAAAVA
>gnl|CDD|273561 TIGR01340, Homocitrate_dehydratase_mitochondrial, aconitate hydratase, mitochondrial. This model represents mitochondrial forms of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase [Energy metabolism, TCA cycle]
YEKLYNNLDEVRRRLNSRPLTLAEKILYSHLDDPEESLLSQDIGDVRGKSYLKLRPDRVAMQDASAQMAL
LQFMTCGLPQVAVPASIHCDHLIVGQKGGDKDLARAIATNKEVFDFLESAGKKYGIGFWKPGSGIIHQIV
LENYAFPGLMMLGTDSHTPNAGGLGTIAIGVGGADAVDALAGAPWELKAPKILGVKLTGKLNGWTSPKDI
ILKLAGLLTVRGGTGYIVEYFGPGVESLSCTGMATICNMGAEIGATTSIFPFNEAMSRYLKATNRAQIAE
DAKTGQYSFFKLKADEGAQYDELIEIDLSKLEPHINGPFTPDLSTPISKFKETVQKNGWPEKLSAGLIGS
CTNSSYEDMSRCASIVKDAEQAGLKPKSPFYVTPGSEQIRATLERDGILQTFEKFGGIVLANACGPCIGQ
WDRKDDVKKGEPNTILTSYNRNFRGRNDGNPATMNFLASPEIVTAMSYAGSLTFNPLTDSLTTPDGKEFK
FPAPKGDELPEKGFEAGRDTFQAPPGSPNPNVEVAVSPSSDRLQLLEPFEPWNGKDLSGLRVLIKVTGKC
TTDHISAAGPWLKYKGHLDNISNNTLIGAVNAETGEVNKAYDLDGSKGTIPELARDWKARGQPWVVVAEH
NYGEGSAREHAALEPRHLGGRIIITKSFARIHETNLKKQGVLPLTFANEADYDKIQPGDEVATLNLYEML
KNGGGGEVDLRVTKKNGKVFEIKLKHTVSKDQIGFFKAGSALNLM
>gnl|CDD|273562 TIGR01341, Aconitate_hydratase_1, aconitate hydratase 1. This model represents one form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It is found in bacteria, archaea, and eukaryotic cytosol. It has been shown to act also as an iron-responsive element binding protein in animals and may have the same role in other eukaryotes [Energy metabolism, TCA cycle]
KTYYYYSLKALEESGGKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEVADTEIAFKPARVV
MQDFTGVPAVVDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERY
QFLKWAQKAFRNFRVVPPGTGIIHQVNLEYLATVVFKAEVDGELTAYPDSLVGTDSHTTMINGLGVLGWG
VGGIEAEAAMLGQPYYMNVPEVIGVKLTGKLQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSL
ADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHVELVEKYARAQGLFYDDSEEPRYTDVVELDL
SDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTLRKEPLKKKVNGQNKQLEDGAVVIAAITSC
TNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYLEELGFNLVGYGCTTCI
GNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYTEPIGT
DKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPP
FFEEMKQDPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHE
VMMRGTFANIRIKNLMVKGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKG
TKLLGVKAVIAESFERIHRSNLVGMGVIPLQFPQGEDAETLGLTGDETIDIDGIKDLKPGKEVTVTFTNS
KGEKITFKCVLRIDTEVELDYYKHGGILQYVLRKFL
>gnl|CDD|130409 TIGR01342, acon_putative, aconitate hydratase, putative, Aquifex type. This model represents a small family of proteins homologous (and likely functionally equivalent to) aconitase 1. Members are found, so far in the anaerobe Clostridium acetobutylicum, in the microaerophilic, early-branching bacterium Aquifex aeolicus, and in the halophilic archaeon Halobacterium sp. NRC-1. No member is experimentally characterized [Energy metabolism, TCA cycle]
TLAEKIIDDHLVEGDLEPGEEIAIEIDQTLSQDATGTMCWLEFEALEMDEVKTELAAQYCDHNMLQFDFK
NADDHKFLMSAAGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAA
MAGEAFYLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNM
GAELGATSSIFPSDDITEAWLAAFDREDDFVDLLADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVRE
IAGIEVDQVMIGSCTNGAFEDLLPAAKLLEGREVHKDTEFAVAPGSKQALELIAQEGALAEFLAAGANFL
EAACGACIGIGFAPASDGVSLRSFNRNFEGRAGIEDAKVYLASPETATAAAIAGEIIDPRDLADDEGDLE
AIGFEMGEKFPGGYDAADIDIIPKEEREDDDIIKGPNIKPLPEFDPLGADIEGETALIMEDNITTDHIIP
AGADILKFRSNIEAISEFTLHRIDDEFAERAKAADEKGKAGIIIAGENYGQGSSREHAALAPMFLGVEAV
IAKSFARIHHANLFNFGILPLEFDNEEDYAKFELGDDIEIPDDLAAALADGEDEFTINKNDDEEALATLD
ASEREKEILAAGGKLNLIKNKHREESGA
>gnl|CDD|273563 TIGR01343, 3-isopropylmalate_dehydratase_large_subunit_2, homoaconitate hydratase family protein. This model represents a subfamily of proteins consisting of aconitase, homoaconitase, 3-isopropylmalate dehydratase, and uncharacterized proteins. The majority of the members of this family have been designated as 3-isopropylmalate dehydratase large subunit (LeuC) in microbial genome annotation, but the only characterized member is Thermus thermophilus homoaconitase, an enzyme of a non-aspartate pathway of Lys biosynthesis
TIAEKILSKKSGKEVYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIVFDHQVPADTIK
AAEMQKLAREFVKKQGIKYFYDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMA
YAIATGKTWFKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLA
NMAIEAGGKTGIIEPDEKTIQYLKERRKEPFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVS
EVEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVV
STPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGHPNAEIYLASPATAAASAVKGYIADPR
>gnl|CDD|188132 TIGR01344, Malate_synthase, malate synthase A. This model represents plant malate synthase and one of two bacterial forms, designated malate synthase A. The distantly related malate synthase G is described by a separate model. This enzyme and isocitrate lyase are the two characteristic enzymes of the glyoxylate shunt. The shunt enables the cell to use acetyl-CoA to generate increased levels of TCA cycle intermediates for biosynthetic pathways such as gluconeogenesis [Energy metabolism, TCA cycle]
VLTPEALEFLALLHRRFNPRRDQLLARRSNRQAKIDSGYLPDFLPETAQIREDDWTIAPIPPDLQDRRVE
ITGPVDRKMVINALNAGAKVFMADFEDSSSPTWENVIYGQINLRDAIRGQIDFTDPTSGKEYALNARLAV
LIVRPRGWHLPERHLTIDGEAIPGSLFDFGLYFFHNARALLKKGKGPYFYLPKLESHQEARLWNDVFHFA
QDFLGLPRGTIKATVLIETLPAAFEMDEILYELREHISGLNCGRWDYIFSFIKTLRNLPEFVLPDRDAVT
MTKPFLNAYSKLLIQTCHRRGAHAMGGMAAFIPIKGDPAANEAAFNKVRADKIREAKNGHDGTWVAHPDL
VPVAMEVFNNVMGTPNQLDRVRDEDVSITAAELLAVPDGSRTEAGLRHNIRVGLQYIEAWLRGSGCVPIY
HLMEDAATAEISRAQLWQWIKHGVVLDDGRVVTPELFRDLLNQEMGKLRSESGLEEFAAGRFEEAAKLFL
RLVTSKELEDFLTIPAYDELI
>gnl|CDD|130412 TIGR01345, malate_syn_G, malate synthase G. This model describes the G isozyme of malate synthase. Isocitrate synthase and malate synthase form the glyoxylate shunt, which generates additional TCA cycle intermediates [Energy metabolism, TCA cycle]
QTITQGRLQVAANLKRFVDEEVLPGTGLDAAAFWSGFDEIVHDLAPENRQLLAERDEIQAAIDEWHRSNP
GPIDKAAYKSFLREIGYLVPQPERVTIETTNVDSEITSQAGPQLVVPAMNARYALNAANARWGSLYDALY
GSNIIPEEDGMEKGKEYNPQRGEKVIAWVRRFLDESLPLENGSHQDVVAYKIVDKQLRIQLKNGKETRLK
TPAQFVGYRGDAADPTCILLKNNGLHIELQIDANHPIGKDDPAHIKDIVLESAITTIMDCEDSVAAVDAE
DKILLYRNWLGLMQGTLQEKMEKNGRQIVRKLNDDRHYTAANGSEISLHGRSLLFVRNVGHLMTIPVIWD
SEGEEIPEGILDGVMTGAIALYDLKVQNKMRNSRKGSVYIVKPKMHGPEEVAFANKLFTRIEDMLGLARH
TLKMGVMDEERRTSLNLRACIAQVRNRVAFINTGFLDRTGDEIHTSMEAGPMLRKNDMKSTPWIKAYERN
NVLAGLFCGLRGKAQIGKGMWAMPDLMAEMYEQKGDQLRAGANTAWVPSPTAATLHALHYHQTNVQSVQA
NLAQTEFNAELDDILTIPVAENTNWSAEEIQQELDNNVQGILGYVVRWVEQGIGCSKVPDIHNVALMEDR
ATLRISSQHIANWLRHGIVSKEQVQASLERMAKVVDQQNAGDPAYRPMAGNFANSCAFQAASDLIFLGTK
QPSGYTEPILHARRLEFKEKH
>gnl|CDD|273564 TIGR01346, Isocitrate_lyase, isocitrate lyase. Isocitrate lyase and malate synthase are the enzymes of the glyoxylate shunt, a pathway associated with the TCA cycle [Energy metabolism, TCA cycle]
AQEIQKWWDTNPRWNGTTRPYTARDVADLRGSVIPEHYLSRRMAEKLWRALTQHGDNKTYSNTFGALDPV
QASQMAKYLDAIYLSGWQCSSTANTSNEPGPDLADYPADTVPNKVEHLFNAQLFHDRKQREARDTSVDNE
RSKTPYIDYLVPIVADGDAGFGGATAVFKLQKAFIERGAAGVHWEDQLSSEKKCGHMAGKVLIPVQEHVN
RLVAARLAADIMGVPTLVVARTDAEAATLITSDVDERDHPFITGATNPNLKPLADVLARAMASGKSGADL
QAVEDEWMAMADLKLFSDCVVDGIKALNVSEKGRRLGEWMQQTNTGNVLSYYQAKELAEKLGISNLFWDW
DLPRTREGFYRVKGGLEPAIARAKAFAPYADLIWMETSTPDLELAKKFAEGVKSKFPDQLLAYNLSPSFN
WSAHMEDDEIAKFIQELGDLGYKWQFITLAGFHSLALGMFDFAYDFAQEGMKAYVEKVQQREMEDGVDAL
KHQKWSGAGYFDQLLKTVQGGNSATAAMKGGVTEDQF
>gnl|CDD|273565 TIGR01347, sucB, 2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component). This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase [Energy metabolism, TCA cycle]
IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQV
LAILEEGNDATAAPPAKSGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRV
TKEDIIKKTEAPASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSA
VMELRKRYKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVP
VVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIK
ERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL
>gnl|CDD|273566 TIGR01348, PDHac_trf_long, pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form. This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model [Energy metabolism, Pyruvate dehydrogenase]
TEIKVPDIGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVI
ATLEVGAGAQAQAEAKKEAAPAPTAGAPAPAAQAQAAPAAGQSSGVQEVTVPDIGDIEKVTVIEVLVKVG
DTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPATAPAPASAQPAAQ
SPAATQPEPAAAPAAAKAQAPAPQQAGTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQ
RFVKEPSVRAQAAAASAAGGAPGALPWPNVDFSKFGEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKA
DITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPN
GLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILG
VSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL
>gnl|CDD|273567 TIGR01349, PDHac_trf_mito, pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form. This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score [Energy metabolism, Pyruvate dehydrogenase]
KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKP
IAVLVEEKEDVADAFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRI
FASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAAAPVSTGSYED
VPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVP
EANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGT
FTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEF
LKSFKKYLENPIEMLL
>gnl|CDD|273568 TIGR01350, Dihydrolipoyl_dehydrogenase, dihydrolipoamide dehydrogenase. This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide
AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEV
ENVSVDWEKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEETLEAKNIIIATG
SRPRSLPGPFDFDGKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGED
AEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQVTYENKGGETETLTGEKVLVAVGRKPNTEGLGLEKLG
VELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDP
EVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVKIIADKKTGEILGAHIIGPHATELISEA
ALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH
>gnl|CDD|273569 TIGR01351, Adenylate_kinase, adenylate kinase. Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ATP as a phosphate donor for AMP. Most members of this family are known or believed to be adenylate kinase. However, some members accept other nucleotide triphosphates as donors, may be unable to use ATP, and may fail to complement adenylate kinase mutants. An example of a nucleoside-triphosphate--adenylate kinase (EC 2.7.4.10) is SP|Q9UIJ7, a GTP:AMP phosphotransferase. This family is designated subfamily rather than equivalog for this reason [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPLGKKAKEYMEKGELVPDEIVNQLVKER
LTQNDDNENGFILDGFPRTLSQAEALDALLEEPIDAVIELDVPDEELVERLSGRRICPSCGRVYHLKFNP
PKVPGCDDCTGELLVQREDDTEEVVKKRLEVYKEQTEPLIDYYKKRGILVQIDGNGPIDEVWKRILEALK
>gnl|CDD|273570 TIGR01352, Protein_TonB, TonB family C-terminal domain. This model represents the C-terminal of TonB and is homologs. TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Most members are designated as TonB or TonB-related proteins, but a few represent the paralogous TolA protein. Several bacteria have up to four TonB paralogs. In nearly every case, a proline-rich repetive region is found N-terminal to this domain; these low-complexity regions are highly divergent and cannot readily be aligned. The region is suggested to help span the periplasm [Transport and binding proteins, Cations and iron carrying compounds]
ARARRRGIEGTVVVRFTVDPSGRVTSVSVLKSSGDRALDRAALEAVRKARFEPPPPPGGVVAASVTIPVR
FKLP
>gnl|CDD|273571 TIGR01353, dGTP_triPase, deoxyguanosinetriphosphate triphosphohydrolase, putative. dGTP triphosphohydrolase (dgt) releases inorganic triphosphate, an unusual activity reaction product, from GTP. Its activity has been called limited to the Enterobacteriaceae, although homologous sequences are detected elsewhere. This finding casts doubt on whether the activity is shared in other species. In several of these other species, the homologous gene is found in an apparent operon with dnaG, the DNA primase gene. The enzyme from E. coli was shown to bind coopertatively to single stranded DNA. The biological role of dgt is unknown [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
ERTPFERDYDRIIHSSAFRRLQDKTQVFPLAENDFVRTRLTHSLEVAQVGRSIANLIGLRYDLELEELGP
FERLAETACLAHDIGNPPFGHAGERALNDWMREYGPGFEGNAQTFRILTTLEKRRRAKGGLNLTWRTLAG
ILKYPRPSSEDAFKGGYLNKKKGIYDSELAVFDRVAELLGLTWYRSPLAQLMEAADDIAYTVHDLEDAIK
LGLLTFDDLQHLLLIQAGFEELGSEMTDLSISAENEQIRSLRGKLITDLIESVAKAEFSSHLVAILIGTF
HHTLVEFSPRLAELLEALKKFLRKRVYRHPDVERIEYQGEQIITGLFDAFMPDLPPRLLPPELRSKLRKA
EDNYYKARVVCDYIAGMTDRYALEEYRRLFG
>gnl|CDD|273572 TIGR01354, Cytidine_deaminase, cytidine deaminase, homotetrameric. This small, homotetrameric zinc metalloprotein is found in humans and most bacteria. A related, homodimeric form with a much larger subunit is found in E. coli and in Arabidopsis. Both types may act on deoxycytidine as well as cytidine [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAI
AVADSADDPVSPCGACRQVLAEFAGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL
>gnl|CDD|273573 TIGR01355, Cytidine_deaminase, cytidine deaminase, homodimeric. This homodimeric zinc metalloprotein is found in Arabidopis and some Proteobacteria. A related, homotetrameric form with a much smaller subunit is found most bacteria and in animals. Both types may act on deoxycytidine as well as cytidine [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
PKFVFTAEQAQSLGTLSGLTDPKLLPKLIPKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLH
HSIHAEQFLISHLALNGERGLNDLAVSFAPCGHCRQFLNEIRNASSIKILLPDPHNKRDMSLQSYLPDRF
GPDDLLIKSAPLLLEERHNCLALIDPDSIRNSDICSDLKQQALKAANRSYAPYSKSPSGVALKDREGKVY
RGWYIESAAFNPSLGPLQAALVDFMANGGGKGFEDIVRAVLVEKADAKVSHEATARALLETIAPSCELKV
FHC
>gnl|CDD|273574 TIGR01356, 3-phosphoshikimate_1-carboxyvinyltransferase, 3-phosphoshikimate 1-carboxyvinyltransferase. This model represents 3-phosphoshikimate-1-carboxyvinyltransferase (aroA), which catalyzes the sixth of seven steps in the shikimate pathway of the biosynthesis of chorimate. Chorismate is last common precursor of all three aromatic amino acids. Sequences scoring between the trusted and noise cutoffs include fragmentary and aberrant sequences in which generally well-conserved motifs are missing or altererd, but no example of a protein known to have a different function [Amino acid biosynthesis, Aromatic amino acid family]
GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGGKEPQA
ELDLGNSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLP
GGIVYISGSASSQYKSALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGG
QKYGPQGYDVPGDYSSAAFFLAAAAITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGA
SGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYI
RGKKELKGAVVDTFGDHRIAMAFAVAGLVAEGEVLIDDPECVAKSFPSFFDVLERLGAN
>gnl|CDD|273575 TIGR01357, 3-dehydroquinate_synthase, 3-dehydroquinate synthase. This model represents 3-dehydroquinate synthase, the enzyme catalyzing the second of seven steps in the shikimate pathway of chorismate biosynthesis. Chorismate is the last common intermediate in the biosynthesis of all three aromatic amino acids [Amino acid biosynthesis, Aromatic amino acid family]
YPVHVGEGLLDQLVEELAEPSKLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRL
YDQLLEAGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLI
GTFYQPKAVLIDPDFLKTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELEHLEELIKRSI
EVKASIVAEDEKESGLRAILNFGHTIGHAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERL
VQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGKIRFVLLEEIGKAALAREVPDEMVLELLD
>gnl|CDD|130425 TIGR01358, Phospho-2-dehydro-3-deoxyheptonate_aldolase, 3-deoxy-7-phosphoheptulonate synthase, class II. This model represents the class II family of 3-deoxy-7-phosphoheptulonate synthase, aka phospho-2-dehydro-3-deoxyheptonate aldolase, as found in plants and some bacteria. It shows some similarity to the class I family found in many bacteria. The enzyme catalyzes the first of 7 steps in the biosynthesis of chorismate, that last common precursor of all three aromatic amino acids. Homologs scoring between trusted and noise cutoff include proteins involved in antibiotic biosynthesis; one example is active as this enzyme, while another acts on an amino analog [Amino acid biosynthesis, Aromatic amino acid family]
WSPQSWRSKPAAQQPTYPDAGALEAVLDTLRSLPPLVFAGEIRRLKRQLAQVAEGEAFLLQGGDCAESFK
DCTADHIRNKLRVLLQMAVVLTYGASLPVVKVGRIAGQYAKPRSAPTETRDGVTLPSYRGDIINGPAFTE
AARVPDPRRLVRAYHQSAATLNLVRALTTGGYADLHQVHYWNLEFVGYSPAGARYEKLASEIDEALRFMS
ACGLAPRYNLQTVEFYTSHEALLLPYEEALTRVDSRSGGWFDLSAHMLWIGERTRQLDGAHVEFLRGVRN
PIGIKVGPSMTPDELLRLIERLNPENEPGRLTLISRMGADKIADKLPPLLRAVKAAGRRVVWVCDPMHGN
TEEAASGYKTRRFDDIRSEVKGFFEVHRAEGTHPGGVHLELTGEDVTECLGGAREITETDLASRYETACD
PRLNAEQSLELAFLVAEKLRDVR
>gnl|CDD|273576 TIGR01359, UMP-CMP_kinase, UMP-CMP kinase family. This subfamily of the adenylate kinase superfamily contains examples of UMP-CMP kinase, as well as others proteins with unknown specificity, some currently designated adenylate kinase. All known members are eukaryotic
VVFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREGSENGSLIESYIKEGKIVPSEVTVELLKK
AIQEDGSSKKFLIDGFPRNEENLEAWEKLMDNKVNFKFVLFFDCPEETMIKRLLKRGQTSGRVDDNIETL
KKRFRTYNEETLPIIEHFENKGKVKEINAEGSVEEVFEDVEKIFA
>gnl|CDD|130427 TIGR01360, Adenylate_kinase_isoenzyme_1, adenylate kinase, isozyme 1 subfamily. Members of this family are adenylate kinase, EC 2.7.4.3. This clade is found only in eukaryotes and includes human adenylate kinase isozyme 1 (myokinase). Within the adenylate kinase superfamily, this set appears specifically closely related to a subfamily of eukaryotic UMP-CMP kinases (TIGR01359), rather than to the large clade of bacterial, archaeal, and eukaryotic adenylate kinase family members in TIGR01351
AKCKIIFIVGGPGSGKGTQCEKIVEKYGFTHLSTGDLLRAEVASGSERGKQLQAIMESGDLVPLDTVLDL
LKDAMVAALGTSKGFLIDGYPREVKQGEEFERRIGPPTLVLYFDCSEDTMVKRLLKRAETSGRVDDNEKT
IKKRLETYYKATEPVIAYYETKGKLRKINAEGTVDDVFLQVCTAIDKL
>gnl|CDD|273577 TIGR01361, DAHP_synth_Bsub, 3-deoxy-7-phosphoheptulonate synthase. This model describes one of at least three types of phospho-2-dehydro-3-deoxyheptonate aldolase (DAHP synthase). This enzyme catalyzes the first of 7 steps in the biosynthesis of chorismate, that last common precursor of all three aromatic amino acids and of PABA, ubiquinone and menaquinone. Some members of this family, including an experimentally characterized member from Bacillus subtilis, are bifunctional, with a chorismate mutase domain N-terminal to this region. The member of this family from Synechocystis PCC 6803, CcmA, was shown to be essential for carboxysome formation. However, no other candidate for this enzyme is present in that species, chorismate biosynthesis does occur, other species having this protein lack carboxysomes but appear to make chorismate, and a requirement of CcmA for carboxysome formation does not prohibit a role in chorismate biosynthesis [Amino acid biosynthesis, Aromatic amino acid family]
KLVSRKFHPEKTVVDVGGVKIGEGSPIVIAGPCSVESEEQIMETARFVKEAGAKILRGGAFKPRTSPYSF
QGLGEEGLKLLRRAADEHGLPVVTEVMDPRDVEIVAEYADILQIGARNMQNFELLKEVGKQGKPVLLKRG
MGNTIEEWLYAAEYILSSGNGNVILCERGIRTFEKATRNTLDLSAVPVLKKETHLPIIVDPSHAAGRRDL
VIPLAKAAIAAGADGLMIEVHPDPEKALSDSKQQLTPEEFKRLVKELRAL
>gnl|CDD|130429 TIGR01362, 2-dehydro-3-deoxyphosphooctonate_aldolase, 3-deoxy-8-phosphooctulonate synthase. This model describes 3-deoxy-8-phosphooctulonate synthase. Alternate names include 2-dehydro-3-deoxyphosphooctonate aldolase, 3-deoxy-d-manno-octulosonic acid 8-phosphate and KDO-8 phosphate synthetase. It catalyzes the aldol condensation of phosphoenolpyruvate with D-arabinose 5-phosphate: phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate In Gram-negative bacteria, this is the first step in the biosynthesis of 3-deoxy-D-manno-octulosonate, part of the oligosaccharide core of lipopolysaccharide [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
EKFFLIAGPCVIESEDHALRVAEKLKELTSKLGVPFIFKSSFDKANRSSIHSFRGPGLEEGLKILQKVKE
EFGVPILTDVHESSQCEPVAEVVDIIQIPAFLCRQTDLLVAAAKTGRIVNVKKGQFLSPWDMKNVVEKVL
STGNKNILLCERGTSFGYNNLVVDMRSLPIMRELGCPVIFDATHSVQQPGGLGGASGGLREFVPTLARAA
VAVGIDGLFMETHPDPKNAKSDGPNMLPLSELEGLLEKLLAIDALTKS
>gnl|CDD|273578 TIGR01363, pneumococcal_histidine_triad_A_protein, streptococcal histidine triad protein. This model represents the N-terminal half of a family of Streptococcal proteins that contain a signal peptide and then up to five repeats of a region that includes a His-X-X-His-X-His (histidine triad) motif. Three repeats are found in the seed alignment. Additional copies in more poorly conserved regions may be detected. Members of this family from Streptococcus pneumoniae are suggested to cleave human C3, and the member PhpA has been shown in vaccine studies to be a protective antigen in mice [Cellular processes, Pathogenesis]
MKINKKYLGGSAAILLLSVCSYELGKYQAGSAKEDNRVAYIDGSQAKQKKENLTPDEVSKREGINAEQIV
IKITDQGYVTSHGDHYHYYNGKVPYDAIISEELLMKDPNYRLKDSDIVNEIKGGYVIKVNGKYYVYLKDA
AHADNIRTKEEIARQKQEGSKEAKEKSKREDAAVAEARRQGRYTTDDGYIFNASDIIEDTGDAYIVPHGD
HYHYIPKNELSASELAAAEAYWSGKQGRGARPSDYRQGSRKASIPDVTPNPGQPAPPRPNDASQNKTQRQ
EFQGKTIKSLLDQLYRLPLSYRHVESDGLIFDPAQITSRTARGVAVPHGDHYHFIPYSQMSELEMRIA
>gnl|CDD|130431 TIGR01364, Phosphoserine_aminotransferase, phosphoserine aminotransferase. This model represents the common form of the phosphoserine aminotransferase SerC. The phosphoserine aminotransferase of the archaeon Methanosarcina barkeri and putative phosphoserine aminotransferase of Mycobacterium tuberculosis are represented by separate models. All are members of the class V aminotransferases (pfam00266) [Amino acid biosynthesis, Serine family]
AALPEEVLEQAQKELLNFNGTGMSVMEISHRSKEFEAVANEAESDLRELLNIPDNYEVLFLQGGATGQFA
AVPLNLLAEGKVADYIVTGAWSKKAAKEAKKYGVVNVVASGKEGNYTKIPDPSTWEISEDAAYVHYCANE
TIHGVEFRELPDVKNAPLVADMSSNILSRPIDVSKFGLIYAGAQKNIGPAGLTVVIVRKDLLGRASRITP
SMLNYKIHAENDSMYNTPPTFAIYVSGLVFKWLKEQGGVKAIEKRNQAKAQLLYDTIDNSNGFYRNPVDP
RNRSRMNVVFTLGNEELEKRFLKEAEERGLVSLKGHRSVGGMRASIYNAMPLEGVQALVDFMKEFQKKH
>gnl|CDD|130432 TIGR01365, Phosphoserine_aminotransferase, phosphoserine aminotransferase, Methanosarcina type. This model represents a variant form of the serine biosynthesis enzyme phosphoserine aminotransferase, as found in a small number of distantly related species, including Caulobacter crescentus, Mesorhizobium loti, and the archaeon Methanosarcina barkeri [Amino acid biosynthesis, Serine family]
RPANPCFSSGPCAKRPGWSIEELKNAPLGRSHRSKLGKEKLAEAIKKTREMLGVPADYLIGIVPASDTGA
VEMALWSMLGCRGVDVLAWESFGKGWVTDVTKQLKLPDVRVLEAEYGKLPDLKKVDFKNDVVFTWNGTTS
GVRVPNGDFIPADREGLTICDATSAAFAQDLDYHKLDVVTFSWQKVLGGEGAHGMLILSPRAVARLESYT
PAWPLPKIFRLTKGGKLNKKIFEGSTINTPSMLCVEDWLDALKWAESIGGLKPLIARADDNLAVLEAFVA
KNNWIHFLAETPEIRSNTSVCLKVVDPAIDALDEDAQADFAKELISTLEKEGVAYDIGSYRDAPSGLRIW
CGATVEKSDLECLCPWLDWAFALV
>gnl|CDD|130433 TIGR01366, Putative_phosphoserine_aminotransferase_PSAT., phosphoserine aminotransferase, putative. This model represents a putative variant form of the serine biosynthesis enzyme phosphoserine aminotransferase, as found in Mycobacterium tuberculosis and related high-GC Gram-positive bacteria [Amino acid biosynthesis, Serine family]
KPRDGRFGSGPSKVRLEQLQALTTTAASLFGTSHRQAPVKNLVGRVREGLAELFSLPDGYEVILGNGGAT
AFWDAATFGLIEKKSLHLSFGEFSSKFAKAVKLAPWLGEPIIVTADPGSAPEPQADPGVDVIAWAHNETS
TGVAVPVRRPEGSDDALVVIDATSGAGGLPVDIAETDVYYFAPQKNFASDGGLWLAIMSPAALERIEAIA
ASGRWVPEFLSLPTAVDNSLKNQTYNTPAIATLALLAEQIDWMNGNGGLDWAVARTADSSSRLYSWAQER
PYATPFVTDPGKRSQVVGTIDFVDDIDAATVAKILRANGIVDTEPYRKLGRNQLRVAMFPAIDPDDVEAL
TECVDWVVERL
>gnl|CDD|273579 TIGR01367, Orotate_phosphoribosyltransferase, orotate phosphoribosyltransferase, Thermus family. This model represents a distinct clade of orotate phosphoribosyltransferases. Members include the experimentally determined example from Thermus aquaticus and additional examples from Caulobacter crescentus, Helicobacter pylori, Mesorhizobium loti, and related species [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
DVLDIYKQAGALHEGHFLLSSGKHSPYFLQSATLLEHPEALMELGGELAQKILDYGLKVDFIVGPAMGGV
ILGYEVARQLSVRSIFAEREGGGMKLRRGFAVKPGEKFVAVEDVVTTGGSLLEAIRAIEGQGGQVVGLAC
IIDRSQGGKPDSGVPLMSLKELEFPTYDSHECPLCLAGIPAEKPGSR
>gnl|CDD|273580 TIGR01368, Carbamoyl-phosphate_synthase_small_chain, carbamoyl-phosphate synthase, small subunit. This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKG
IHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVE
KARVSPDITGINLVAEVSTKEPYTWGQRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIK
KYNPDGIFLSNGPGDPAAVEPAIETIRKLLEKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDL
ITGRVEITSQNHGYAVDPDSLPAGDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDE
FIDLMKK
>gnl|CDD|273581 TIGR01369, Carbamoyl-phosphate_synthase_large_chain, carbamoyl-phosphate synthase, large subunit. Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTP
EAVEKIIEKERPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGE
PVPESEIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLA
GWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGC
NVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAVGYTLDELKNPVTGTTPASFEPSLD
YVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDLPDREVEPDEDLW
RALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPELLRRAKKL
GFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVL
GSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKP
EGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFA
SEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLI
PGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPR
ASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGKEKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTG
EVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKGYKLYATEGTAKFLGEAG
IKPELVLKVSEGRPNILDLIKNGEIELVINTTSKGAGTATDGYKIRREALDYGVPLITTLNTAEAFAEAL
>gnl|CDD|273582 TIGR01370, Uncharacterized_protein_DR_0705, extracellular protein. Original assignment of this protein family as cysteinyl-tRNA synthetase is controversial, supported by but challenged by and by subsequent discovery of the actual mechanism for synthesizing Cys-tRNA in species where a direct Cys--tRNA ligase was not found. Lingering legacy annotations of members of this family probably should be removed. Evidence against the role includes a signal peptide. This family as been renamed "extracellular protein" to facilitate correction. Members of this family occur in Deinococcus radiodurans (bacterial) and Methanococcus jannaschii (archaeal). A number of homologous but more distantly related proteins are annotated as alpha-1,4 polygalactosaminidases. The function remains unknown [Unknown function, General]
CSIILLSAFFISSESTASGAGPAQTPPPVTVPMTPPSKKPALSAVQHWGYQLQNADLNEIHTSPFELVVI
DYSKDGTEDGTYSPEEIVRAAAAGRWPIAYLSIGAAEDYRFYWQKGWKVNAPAWLGNEDPDWPGNYDVKY
WDPEWKAIAFSYLDRVIAQGFDGVYLDLIDAFEYWAENGDNRPGAAAEMIAFVCEIAAYARAQNPQFVII
PQNGEELLRDDHGGLAATVSGWAVEELFYYAANRPTEAERQRRLLALYRLWQQGKFVLTVDYVDDGTKTN
ENPARMKDAAEKARAAGLIPYVAESDLELDELNQP
>gnl|CDD|273583 TIGR01371, methionine_synthase., 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase. This model describes the cobalamin-independent methionine synthase. A family of uncharacterized archaeal proteins is homologous to the C-terminal region of this family. That family is excluded from this model but, along with this family, belongs to pfam01717 [Amino acid biosynthesis, Aspartate family]
LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVML
GAIPERFGNYGGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAK
ELGIETKPVLLGPITFLKLSKAVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKED
LAAFKEAYTELSEALSGLKLLLQTYFDSVGDALEALVSLPVKGIGLDFVHGKGTLELVKAGFPEDKVLSA
GVIDGRNIWRNDLEASLSLLKKLLAHVGKLVVSTSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELK
ALKRALNGNDDAVAFALEANAAAIAARKSSPRVNDAQVKARLANLKEDDFRRRSPFKERLPLQQKRLNLP
LLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGLDVLVHGEFERNDMVEYF
GEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVTILNWSFV
RDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKD
ETQIHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFGYPNGIGPGVYDIHSPRVPSVEE
MADLIEKALQVLPAERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ
>gnl|CDD|273584 TIGR01372, sarcosine_oxidase_alpha_subunit, sarcosine oxidase, alpha subunit family, heterotetrameric form. This model describes the alpha subunit of a family of known and putative heterotetrameric sarcosine oxidases. Five operons of such oxidases are found in Mesorhizobium loti and three in Agrobacterium tumefaciens, a high enough copy number to suggest that not all members are share the same function. The model is designated as subfamily rather than equivalog for this reason.Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]
LSGGGRIDRSRPLRFTFDGKSYSGFAGDTLASALLANGVHLVGRSFKYHRPRGILTAGVEEPNALVTVGS
GAQREPNTRATTQELYDGLVATSQNRWPSLAFDIGAFNDLFAPLLSAGFYYKTFMWPAAFWWKIYEPFIR
RAAGLGVADTETDPDTYDKVNAHCDVLVVGAGPAGLAAALAAARAGARVILVDEQPEAGGSLLSEAETID
GKPAADWAAATVAELTAMPEVTLLPRTTAFGYYDHNTVGALERVTDHLDAPPKGVPRERLWRIRAKRVVL
ATGAHERPLVFANNDRPGVMLAGAARTYLNRYGVAPGKRIVVATNNDSAYRAAADLLAAGIAVVAIIDAR
ADVSPEARAEARELGIEVLTGHVVAATEGGKRVSGVAVARNGGAGQRLEADALAVSGGWTPVVHLFSQRG
GKLAWDAAIAAFLPGDAVQGCILAGAANGLFGLAAALADGAAAGAAAARAAGFEGTAAVLPSVAVPAGET
GPVALWPVPAGKGKAFVDYQNDVTAKDVELAVREGFESVEHLKRYTTLGMATDQGKTSNVNGLAIMAEAL
GKSIPEVGTTTFRPPYTPVSFGALAGRHRGELFDPARKTPLHSWHLAHGAVFEDVGQWKRPWYYPRRGED
MDEAVARECKAVRESVGLFDASTLGKIEVQGPDAAEFLNRVYTNAFTKLKVGKARYGLMLREDGMVFDDG
VTSRLAEDRFLMTTTTGGAARVLQHLEEWLQTEWPELDVYLTSVTDQWATLAVSGPKARDLLAELVDGLD
LSNEAFPFMAIKEGTLAGVPARLFRISFSGELAFEVNVPADYGEAVWEALMEAGQPFGITPYGTETMHVL
RAEKGFIIVGQDTDGTVTPADLGMGWMVSKKKPDFVGRRMLAREDLVAEDRKQLVGLLPLDPQRRLPEGA
HIVADDAEAIPMNMQGHVTSSYFSPALGRTIALALVKGGRARHGETVYVPDLGRFIAVEICDPVFFDPEG
TRLHG
>gnl|CDD|273585 TIGR01373, Sarcosine_oxidase_subunit_beta, sarcosine oxidase, beta subunit family, heterotetrameric form. This model describes the beta subunit of a family of known and putative heterotetrameric sarcosine oxidases. Five operons of such oxidases are found in Mesorhizobium loti and three in Agrobacterium tumefaciens, a high enough copy number to suggest that not all members are share the same function. The model is designated as subfamily rather than equivalog for this reason. Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]
RYSAFSLLKEGLRGHRGWKPAWRSPEPKPTYDVIIVGGGGHGLATAYYLAKEHGITNVAVLEKGWLGGGN
TGRNTTIVRSNYLYPESAELYEHAMKLWEGLSQDLNYNVMFSQRGVLNLCHSTADMDDGARRVNAMRLNG
VDAELLSPEQVRRVIPILDFSPDARFPVVGGLLQRRGGTARHDAVAWGYARGADRRGVDIIQNCEVTGFI
RRDGGRVIGVETTRGFIGAKKVGVAVAGHSSVVAAMAGFRLPIESHPLQALVSEPLKPIIDTVVMSNAVH
FYVSQSDKGELVIGGGIDGYNSYAQRGNLPTLEHVLAAILEMFPILSRVRMLRSWGGIVDVTPDGSPIIG
KTPLPNLYLNCGWGTGGFKATPASGTVFAHTLARGEPHDINAPFTLDRFHSGRLIDE
>gnl|CDD|130441 TIGR01374, Sarcosine_oxidase_subunit_delta, sarcosine oxidase, delta subunit family, heterotetrameric form. This model describes the delta subunit of a family of known and putative heterotetrameric sarcosine oxidases. Five operons of such oxidases are found in Mesorhizobium loti and three in Agrobacterium tumefaciens, a high enough copy number to suggest that not all members are share the same function. The model is designated as subfamily rather than equivalog for this reason. Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) form [Energy metabolism, Amino acids and amines]
LIPCPYCGPRPEEEFTYGGDAHIVRPADPAAASDEEWEDYLFLRDNPKGLHAERWVHSGGCRRWFNVVRD
TVTHEILATYRAGE
>gnl|CDD|273586 TIGR01375, Sarcosine_oxidase_subunit_gamma, sarcosine oxidase, gamma subunit family, heterotetrameric form. This model describes the gamma subunit of a family of known and putative heterotetrameric sarcosine oxidases. Five operons of such oxidases are found in Mesorhizobium loti and three in Agrobacterium tumefaciens, a high enough copy number to suggest that not all members are share the same function. The model is designated as subfamily rather than equivalog for this reason. The gamma subunit is the most divergent between operons of the four subunits. Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]
LRALPGGAIVAALAAALGLTLPARLGSVASGGEISVLWLGPDEWLIIAPQPEGAVLMAALAAALGPEPHA
VVDLSGGRTALRISGPMAEEVLAKGCAVDLSLSAFPVGAGRRTIFGKIAAVIWRTGEDTFEIIVRRSFAE
SLWHWLVDASEE
>gnl|CDD|273587 TIGR01376, Probable_outer_membrane_protein, Chlamydial polymorphic outer membrane protein repeat. This model represents a repeat region of about 27 residues that appears from twice to over twenty times in Chlamydial polymorphic outer membrane proteins (POMP). Characteristic motifs in the repeat are FXXN and GGAI. Except for a few apparently truncated examples, Chlamydial proteins have this repeat region if and only if they also have the autotransporter beta-domain (pfam03797) at the C-terminus, with Phe as the C-terminal residue. This repeat is observed, but is very rare, outside the Chlamydias
NNGTILFSSNSAKGSGGAIYATKISIS
>gnl|CDD|130444 TIGR01377, Monomeric_sarcosine_oxidase, sarcosine oxidase, monomeric form. Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]
FDVIVVGAGIMGCFAAYHLAKHGKKTLLLEQFDLPHSRGSSHGQSRIIRKAYPEDFYTPMMLECYQLWAQ
LEKEAGTKLHRQTGLLLLGPKENQFLKTIQATLSRHGLEHELLSSKQLKQRFPNIRVPRNEVGLLDPNGG
VLYAEKALRALQELAEAHGATVRDGTKVVEIEPTELLVTVKTTKGSYQANKLVVTAGAWTSKLLSPLGIE
IPLQPLRINVCYWREKEPGSYGVSQAFPCFLVLGLNPHIYGLPSFEYPGLMKVYYHHGQQIDPDERDCPF
GADIEDVQILRKFVRDHLPGLNGEPKKGEVCMYTNTPDEHFVIDLHPKYDNVVIGAGFSGHGFKLAPVVG
KILAELAMKLKPSYDLAIFSLNRFALKKKA
>gnl|CDD|273588 TIGR01378, Thiamine_pyrophosphokinase, thiamine pyrophosphokinase. This model has been revised. Originally, it described strictly eukaryotic thiamine pyrophosphokinase. However, it is now expanded to include also homologous enzymes, apparently functionally equivalent, from species that rely on thiamine pyrophosphokinase rather than thiamine-monophosphate kinase (TIGR01379) to produce the active TPP cofactor. This includes the thiamine pyrophosphokinase from Bacillus subtilis, previously designated YloS [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
LILAGGGPDSELPLRLLKEHDLVIAADGGANHLLKLGLTPDLIVGDFDSIDEEELDFYKETGVKIIVFPP
EKDTTDLELALKYALERGADEITILGATGGRLDHTLANLNLLLEYAKRGIEVRLIDEQNVIRLLLPGKYQ
IFKEPKGTYISLLPFGGDVHGLTTKGLKYPLNNADLKFGGTRGISNEFIGNKATVSVDSGILLVI
>gnl|CDD|273589 TIGR01379, Thiamine-monophosphate_kinase, thiamine-phosphate kinase. This model describes thiamine-monophosphate kinase, an enzyme that converts thiamine monophosphate into thiamine pyrophosphate (TPP, coenzyme B1), an enzyme cofactor. Thiamine monophosphate may be derived from de novo synthesis or from unphosphorylated thiamine, known as vitamin B1. Proteins scoring between the trusted and noise cutoff for this model include short forms from the Thermoplasmas (which lack the N-terminal region) and a highly derived form from Campylobacter jejuni. Eukaryotes lack this enzyme, and add pyrophosphate from ATP to unphosphorylated thiamine in a single step [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
GEFELIDRILRRLVQDPDVALGIGDDAALVSAPEGRDLVLTTDTLVEGVHFPPDTTPEDLGWKAVAVNLS
DLAAMGATPKWFLLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTVSSPELVVTVTAIGEAPKGR
ALLRSGAKPGDLVFVTGTLGDSAAGLALLLKGKKEPDEEDDEALLQRHLRPEPRVEEGLALAGYANAAID
VSDGLAADLGHIAEASGVGIVIDLDRLPLSSELAAWAEGKNPLEWALSGGEDYELVFTVPPERREALLDA
AKGPLTRIGRVTEGEGVVLLADGKTVELLDRLGWQHF
>gnl|CDD|130447 TIGR01380, Glutathione_synthetase, glutathione synthetase, prokaryotic. This model was built using glutathione synthetases found in Gram-negative bacteria. This gene does not appear to be present in genomes of Gram-positive bacteria. Glutathione synthetase has an ATP-binding domain in the COOH terminus and catalyzes the second step in the glutathione biosynthesis pathway: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione. Glutathione is a tripeptide that functions as a reductant in many cellular reactions [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
LKVAFQMDPIESINIGKDTTFALMEEAQKRGHELFFYEPGDLSVVNGEVFARARPVRVGPNKQDWYTLGE
KVRLSLGELDAVLMRKDPPFDMEYIYATYLLELADPTGTLVINSPQGLRDANEKLFTLQFPKVIPPTLVT
RDKAEIRAFLAEHGDIVLKPLDGMGGEGIFRLDPGDPNFNSILETMTQRGREPVMAQRYLPEIKEGDKRI
LLIDGEPIGAAVARIPAGGEFRGNLAVGGRGEATELSERDREICADVAPELKRRGLLFVGIDVIGGYLTE
VNVTSPTGIREIDRQKGVNIAGMLWDAIEKAV
>gnl|CDD|273590 TIGR01381, putative_ubiquitin_activating_enzyme_E1, E1-like protein-activating enzyme Gsa7p/Apg7p. This model represents a family of eukaryotic proteins found in animals, plants, and yeasts, including Apg7p (YHR171W) from Saccharomyces cerevisiae and GSA7 from Pichia pastoris. Members are about 650 to 700 residues in length and include a central domain of about 150 residues shared with the ThiF/MoeB/HesA family of proteins. A low level of similarity to ubiquitin-activating enzyme E1 is described in a paper on peroxisome autophagy mediated by GSA7, and is the basis of the name ubiquitin activating enzyme E1-like protein. Members of the family appear to be involved in protein lipidation events analogous to ubiquitination and required for membrane fusion events during autophagy
FVPFVSCVDTGFWNEVSKLKLNKWKLDDTPKCISGQLSLHQTEGFKCHLSLSYDSLSSLESTTGTHAQLS
VSGILLNYNTVESFKKVDKSDLLRSEAEKIWESIQTRKWLQDPSLLSQFFIISFADLKKFKFYYWFCFPA
LVYPSKVNKLSGLTESIKQEITPLESLGADHKILFDFYRKNNFPFFLYSKQSSKMLELSELENNTNPDDE
LCVGFADPSPVAYSAGWMLRNVLAAVAHLHPTWKHVHIFSLRSADSIGIKYLWTTLLPSAELSSDGAQNA
VPKAVGWERNANGKLQPISVDLSKEFDPKRLAERSVDLNLKLMKWRLHPDLQLERYSQLKVLLLGAGTLG
CNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCLLGGRGKAETAQKALKRIFPSIQATGHRLTV
PMPGHPIDEKDVPELEKDIARLEQLIKDHDVVFLLLDSREARWLPTVLCSRHKKIAISAALGFDSYVVMR
HGIGRSESVSDVSSSDSVPYSRLGCYFCNDVTAPGDSTTDRTLDQQCTVTRPGTAMIASGLAVELLVSVL
QHPLPSKTPASHDDNTTVLGALPHQIRGFLGRFQQILLSVKRFDQCVACSDAVAAEYQQRGWKFVRDAMN
SPGYLEDLTGLTELKNESSVNAIDIQDFESDDDD
>gnl|CDD|273591 TIGR01382, Uncharacterized_protein_MJ0967, intracellular protease, PfpI family. The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs [Protein fate, Degradation of proteins, peptides, and glycopeptides]
KLLVLTTDEFEDSELLYPLDRLREAGHEVDTVSKEAGTTVGKHGYSVTVDATIDEVNPEEYDALVIPGGR
APEYLRLNNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEVVV
VDGNLVTSRVPDDLPAFNREFLKLLG
>gnl|CDD|213612 TIGR01383, transcriptional_regulator_related_protein, DJ-1 family protein. This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of proteins. PfpI, represented by a distinct model, is a putative intracellular cysteine protease. DJ-1 is described as an oncogene that acts cooperatively with H-Ras. Many members of the DJ-1 clade are annotated (apparently incorrectly) as ThiJ, a protein of thiamine biosynthesis. However, published reports of ThiJ activity and identification of a ThiJ/ThiD bifunctional protein describe an unrelated locus mapping near ThiM, rather than the DJ-1 homolog of E. coli. The ThiJ designation for this family may be spurious; the cited paper refers to a locus near thiD and thiM in E. coli, unlike the gene represented here. Current public annotation reflects ThiJ/ThiD bifunctional activity, apparently a property of ThiD and not of this locus [Unknown function, General]
KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVAIAGLNGKLAVKGSRGVKILADASLEDVDLEKFDVIVLP
GGMPGAENLRNSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKKATCYPGFKEKLLNGNYSVNKT
VVVDGNLITSRGPGTAIEFALELVELLAGKEKAQEVAAG
>gnl|CDD|130451 TIGR01384, TFS_arch, transcription factor S, archaeal. This model describes archaeal transcription factor S, a protein related in size and sequence to certain eukaryotic RNA polymerase small subunits, and in sequence and function to the much larger eukaryotic transcription factor IIS (TFIIS). Although originally suggested to be a subunit of the archaeal RNA polymerase, it elutes separately from active polymerase in gel filtration experiments and acts, like TFIIs, as an induction factor for RNA cleavage by RNA polymerase. There has been an apparent duplication event in the Halobacteriaceae lineage (Haloarcula, Haloferax, Haloquadratum, Halobacterium and Natromonas). There appears to be a separate duplication in Methanosphaera stadtmanae [Transcription, Transcription factors]
KFCPKCGSLMTPKNGVYVCPSCGYEKEKKPEDDYKVTEKVKHKIKETIIIREEDSETLPTTRVECPKCGH
KEAYYWLLQTRRADEPETRFYKCTKCGYVWREYE
>gnl|CDD|273592 TIGR01385, Putative_transcription_elongation_factor_S-II, transcription elongation factor S-II. This model represents eukaryotic transcription elongation factor S-II. This protein allows stalled RNA transcription complexes to perform a cleavage of the nascent RNA and restart at the newly generated 3-prime end
SAEVASHAKALDKNKSSKNVEQCLDILHQLKEFPPTEELLQETKVGVKVNKLRKHPNEDISKLAKKIIKS
WKKVVDKNKSDHPGGNPEDKTTVGESVNSVKQEAKSQSDKIEQPKYVSSSPRNAKNDFVPTAVTNDKVRD
KCRELLYDALAKDSDHPPQSIDPEAKAIQIEELKFNNLGTTEAAYKARYRSIYSNLRDKNNPDLRHNVLT
GEITPEKLATMTAEEMASAELKQEREEITKENLFEAQGAKIQKAVTDLFTCGKCKQKKCTYYQLQTRSAD
EPMTTFVTCEECGNRWKFC
>gnl|CDD|273593 TIGR01386, Probable_sensor_protein_PcoS, heavy metal sensor kinase. Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc
PRSLTLRLALLFAAVTALVFALSGFMLYSSLERHFEERDREELQGKLEQVRRFLRDPADLDEDIKRLQEK
IDDLLVGHSDLALSILNPDGRLLFERAQGAALVPAVAANDALLELDQADAKMTHYRSILRSVAALPGGKG
RKPVQITVALDINAHTHLLDALRKWLILIAVLLVLLTALLGWWITRLGLEPLRRLSAVAARISPESLDQR
LDPSRAPAELRELAQSFNAMLGRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQVALSQPRTGEEYREVL
ESNLEELERLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEGLVRGD
PQMFRRAISNLLSNALRHTPDGGTITVRIERRSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSG
EGTGLGLAIVRSIMEAHGGRASAESPDGKTRFILRFP
>gnl|CDD|130454 TIGR01387, Transcriptional_regulatory_protein_PcoR, heavy metal response regulator. Members of this family contain a response regulator receiver domain (pfam00072) and an associated transcriptional regulatory region (pfam00486). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc. Most members encoded by genes adjacent to genes for encoding a member of the heavy metal sensor histidine kinase family (TIGRFAMs:TIGR01386), its partner in the two-component response regulator system [Regulatory functions, DNA interactions]
ILVVEDEQKTAEYLQQGLSESGYVVDAASNGRDGLHLALKDDYDLIILDVMLPGMDGWQILQTLRRSGKQ
TPVLFLTARDSVADKVKGLDLGADDYLVKPFSFSELLARVRTLLRRSHSLNSTVLEIADLRMDSVRHRVS
RGNIRITLTRKEFQLLWLLMRRTGEVLPRTVIASLVWGMNFDSDTNVVDVAIRRLRAKVDDPFEEKLIHT
IRGMGYVL
>gnl|CDD|130455 TIGR01388, Ribonuclease_D, ribonuclease D. This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA both in vitro and when overexpressed in vivo. Trusted members of this family are restricted to the Proteobacteria; Aquifex, Mycobacterial, and eukaryotic homologs are not full-length homologs. Ribonuclease D is not essential in E. coli and is deleterious when overexpressed. Its precise biological role is still unknown [Transcription, RNA processing]
WITTDDELATVCEAVRTFPFVALDTEFVRERTFWPQLGLIQVADGEQLALIDPLVIIDWSPLKELLRDES
VVKVLHAASEDLEVFLNLFGELPQPLFDTQIAAAFCGFGMSMGYAKLVQEVLGVELDKSESRTDWLARPL
TDAQLEYAAADVTYLLPLYAKLMERLEESGRLAWLEEECTLLTDRRTYVVNPEDAWRDIKNAWQLRPQQL
AVLQALAAWREREARERDLPRNFVLKEEALWELARQAPGNLTELASLGPKGSEIRKHGDTLLALVKTALA
LPEDALPQAPLNLMPPPGYKALFKLLKVLVKDVSETLGLASELLASRRQLEQLLAWGWKLKPNALPPLLQ
GWRRELGEEALKNLLSE
>gnl|CDD|273594 TIGR01389, recQ, ATP-dependent DNA helicase RecQ. The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ [DNA metabolism, DNA replication, recombination, and repair]
AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQV
DQLRAAGVAAAYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVS
QWGHDFRPEYQRLGSLAERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNN
KQKFLLDYLKKHRGQSGIIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVA
TNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPAEAILLYSPADIALLKRRIEQSEADDDYK
QIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDPPKSYDATVEAQKALSCVYRMGQRFG
VGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIYIGLQLTEAARKV
LKNEVEVLLRPFKVVAKEKTRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEKRP
ATLNALLKIKGVGQNKLDRYGEAFLEVIREY
>gnl|CDD|130457 TIGR01390, CycNucDiestase, 2',3'-cyclic-nucleotide 2'-phosphodiesterase. 2',3'-cyclic-nucleotide 2'-phosphodiesterase is a bifunctional enzyme localized to the periplasm of Gram-negative bacteria. 2',3'-cyclic-nucleotide 2'-phosphodiesters are intermediates formed during the hydrolysis of RNA by the ribonuclease I, which is also found to the periplasm, and other enzymes of the RNAse T2 family. Bacteria are unable to transport 2',3'-cyclic-nucleotides into the cytoplasm. 2',3'-cyclic-nucleotide 2'-phosphodiesterase contains 2 active sites which catalyze the reactions that convert the 2',3'-cyclic-nucleotide into a 3'-nucleotide, which is then converted into nucleic acid and phosphate. Both final products can be transported into the cytoplasm. Thus, it has been suggested that 2',3'-cyclic-nucleotide 2'-phosphodiesterase has a 'scavenging' function. Experimental evidence indicates that 2',3'-cyclic-nucleotide 2'-phosphodiesterase enables Yersinia enterocolitica O:8 to grow on 2'3'-cAMP as a sole source of carbon and energy () [Purines, pyrimidines, nucleosides, and nucleotides, Other]
VDLRIVETTDLHTNLMDYDYYKDKPTDKFGLTRTATLIKQARAEVKNSVLVDNGDLIQGSPLGDYMAAQG
LKAGQMHPVYKAMNLLKYDVGNLGNHEFNYGLPFLKQAIAAAKFPIVNANVVDAGTGQPAFTPYLIQERS
VVDTDGKPHTLKVGYIGFVPPQIMVWDKANLDGKVTTADIVDTARKYVPEMKAKGADIIVALAHSGISAD
PYQPGAENSAYYLTKVPGIDAVLFGHSHAVFPGKDFATIPGADITNGTINGVPAVMAGYWGNHLGVVDLQ
LNYDSGKWTVTSAKAELRPIYDKANKKSLVTPDPAIVRALKADHEGTRRYVSQPIGKAADNMYSYLALVQ
DDPTVQIVNNAQKAYVEAAIQSDPQLAGLPVLSAAAPFKAGGRKNDPSGYTEVEAGTLTFRNAADLYLYP
NTLVVVKVTGAQVKEWLECSAGQFKQIDPTSTKPQSLIDWDGFRTYNFDVIDGVNYEIDVTQPARYDGDC
KLINPNAHRIKNLTYQGKPIDPAAQFLVATNNYRAYGGKFPGTGDKHIAFASPDENRQVLAAYIADQSKK
EGEVNPAADNNWRLAPIPGNVKLDVRFETSPSDKAAKFIKEKGQYPMKQVATDDIGFAVYQIDLSK
>gnl|CDD|273595 TIGR01391, DNA_primase, DNA primase, catalytic core. Members of this family are DNA primase, a ubiquitous bacteria protein. Most members of this family contain nearly two hundred additional residues C-terminal to the region represented here, but conservation between species is poor and the C-terminal region was not included in the seed alignment. This protein contains a CHC2 zinc finger (pfam01807) and a Toprim domain (pfam01751) [DNA metabolism, DNA replication, recombination, and repair]
MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKF
LMEIEGISFVEAVEELAKRAGIDLPFEKDQQEKKEQKSKRKKLYELLELAAKFFKNQLKHTPENRAALDY
LQSRGLSDETIDRFELGYAPNNWDFLFDFLQNKKGFDLELLAEAGLLVKKENGKYYDRFRNRIMFPIHDP
KGRVVGFGGRALGDEKPKYLNSPETPLFKKSELLYGLHKARKEIRKEKELILVEGYMDVIALHQAGIKNA
VASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAALRAIELLLPLGINVKVIKLPGGKDPDEYLRKEG
VEALKKLLENSKSLIEFLIARLLSNYNLDTPEEKAKLVEELLPLIKKIPDPILRDYYLQKLAQLL
>gnl|CDD|273596 TIGR01392, Homoserine_O-acetyltransferase, homoserine O-acetyltransferase. This family describes homoserine-O-acetyltransferase, an enzyme of methionine biosynthesis. This model has been rebuilt to identify sequences more broadly, including a number of sequences suggested to be homoserine O-acetyltransferase based on proximity to other Met biosynthesis genes [Amino acid biosynthesis, Aspartate family]
RVKPLTLESGGVLSDVRVAYETYGTLNAERSNAVLVCHALTGDAHVAGYHDDGDPGWWDDLIGPGRAIDT
DRYFVVCSNVLGGCYGSTGPSSINPGGRPYGSDFPLITIRDDVKAQKLLLDHLGIEQIAAVVGGSMGGMQ
ALEWAIDYPERVRAIVVLATSARHSAWCIAFNEVQRQAILADPNWNDGDYYEDGQPDRGLALARMLAHLT
YRSEESMAERFGRAPQSGESPASGFDTRFQVESYLRYQGDKFVDRFDANSYLYLTRALDTHDLGRGRGSL
TEALSRIKAPFLVVSITSDWLFPPAESRELAKALPAAGLRVTYVEIESPYGHDAFLVETDQVEELIRGFL
R
>gnl|CDD|130460 TIGR01393, Elongation_factor_4, elongation factor 4. LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a GTP-binding membrane protein related to EF-G and EF-Tu. Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including GUF1 of yeast) originated within the bacterial LepA family. The function is unknown [Unknown function, General]
KNIRNFSIIAHIDHGKSTLADRLLEYTGAISEREMREQVLDSMDLERERGITIKAQAVRLNYKAKDGETY
VLNLIDTPGHVDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPE
RVKKEIEEVIGLDASEAILASAKTGIGIEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVR
VFEGTIKPGDKIRFMSTGKEYEVDEVGVFTPKLTKTDELSAGEVGYIIAGIKDVSDVRVGDTITHVKNPA
KEPLPGFKEVKPMVFAGLYPIDTEDYEDLRDALEKLKLNDASLTYEPESSPALGFGFRCGFLGLLHMEII
QERLEREFNLDLITTAPSVIYRVYLTNGEVIEVDNPSDLPDPGKIEHVEEPYVKATIITPTEYLGPIMTL
CQEKRGVQTNMEYLDPNRVELIYEMPLAEIVYDFFDKLKSISRGYASFDYELIGYRPSDLVKLDILINGE
PVDALSFIVHRDKAYSRGREICEKLKELIPRQQFEIPIQAAIGGKIIARETIKALRKDVTAKCYGGDITR
KRKLLEKQKEGKKRMKQIGKVEVPQEAFLAVLKVD
>gnl|CDD|273597 TIGR01394, GTP-binding_protein_TypA/BipA_homolog, GTP-binding protein TypA/BipA. This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITILAKNTAIRYNGTKINIVD
TPGHADFGGEVERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEV
FDLFAELGADDEQLDFPIVYASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDY
DEYLGRIAIGRVHRGTVKKGQQVALMKRDGTIENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINI
GETIADPEVPEALPTITVDEPTLSMTFSVNDSPLAGKEGKKVTSRHIRDRLMRELETNVALRVEDTESAD
KFEVSGRGELHLSILIETMRREGFELQVGRPQVIYKEIDGKKLEPIEELTIDVPEEHVGAVIEKLGKRKG
EMVDMEPSGNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFDEYEPWKGEIETRRNGSLVSMEDGT
ATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGKDEAVKLTPPRKLSL
EQALEYIEDDELVEVTPKSIRLRKRVLDPNERKR
>gnl|CDD|130462 TIGR01395, Flagellar_basal-body_rod_protein_FlgC, flagellar basal-body rod protein FlgC. This model represents FlgC, one of several components of bacterial flagella that share a domain described by pfam00460. FlgC is part of the basal body [Cellular processes, Chemotaxis and motility]
FSIFNVSASALSAQRVRMNVVSSNLANADSTRTPAGDPYRRRRPVFEAELFQDRASRPGGSGVKVAKIVE
DDSPFKLVYDPTHPDADAEGYVKMPNVNVVEEMVDMIEASRSYEANVQVFNTAKSMFLRTLEIGR
>gnl|CDD|273598 TIGR01396, Flagellar_basal_body_rod_protein_FlgB, flagellar basal-body rod protein FlgB. This model represents FlgB, one of several components of bacterial flagella that share a domain described by pfam00460. FlgB is part of the basal body [Cellular processes, Chemotaxis and motility]
FSNAFGLLQQALDVRSLRQEVIANNIANVDTPGYKAKDVSFEAELKKALDNERNSKLTLARTDTRPRHLN
AQDSNSVEPSLQYDYTTQVKNDGNNVDIDQEMAELAQNQMHYQALTQFLNGKIKGLNYVLR
>gnl|CDD|130464 TIGR01397, Flagellar_motor_switch_protein_FliM, flagellar motor switch protein FliM. Members of this family are the flagellar motor switch protein FliM. The family excludes FliM homologs that lack an N-terminal region critical to interaction with phosphorylated CheY. One set lacking this N-terminal region is found in Rhizobium meliloti, in which the direction of flagellar rotation is not reversible (i.e. the FliM homolog does not act to reverse the motor direction), and in related species. Another is found in Buchnera, an obligate intracellular endosymbiont with genes for many of the components of the flagellar apparatus, but not, apparently, for flagellin iself [Cellular processes, Chemotaxis and motility]
DILSQDEIDALLGGLSEGDDSDEPSAVEDEKKVKPYDFKRPDRVSKEQLRTLEIINERFARLLRTSLSNM
LRRFVEVSVASVDQLTYGEFLRSLPVPTSLNVFRMEPLRGTALIEIDPSLIYTMVDRLFGGQGRSVPEGR
EFTEIERRVIDRILDRVLEDLKEAWSPVMPLEPELDRSETNPQFAQIVPPNEIVVLVSFSVEVGETEGMI
NICLPYSTLEPIRSKLSQRFMQSEKVERDSSWRDALERELSTVPVDMRAVLGEVEVSLRQLLNLQVGDVI
PLNTDMPEEVSLRVGGRPKFRAQPGVRGGKLAVQITRVIE
>gnl|CDD|273599 TIGR01398, Flagellar_biosynthesis_protein_FlhA, flagellar biosynthesis protein FlhA. This model describes flagellar biosynthesis protein FlhA, one of a large number of genes associated with the biosynthesis of functional bacterial flagella. Homologs of many such proteins, including FlhA, function in type III protein secretion systems. A separate model describes InvA (Salmonella enterica), LcrD (Yersinia enterocolitica), HrcV (Xanthomonas), etc., all of which score below the noise cutoff for this model [Cellular processes, Chemotaxis and motility]
GRDLLLAIGVVAILAVMILPLPAFLLDILLALNIALSLLILLVTLFIQKPLDFSSFPTLLLIATLFRLSL
NVASTRLILTHGHEGPNAAGKVIEAFGQFVVGGNYVIGLIVFIILIIVNFIVITKGATRIAEVAARFTLD
AMPGKQMAIDADLNAGLITEEEAKKRREELEQEADFYGAMDGASKFVKGDAIAGIIITLINIIGGLIIGV
VQHGMSLSDAASTYTILTIGDGLVAQIPALIISTATGLIVTRASSEGSFGKAIVTQLGANPRALLIVAAV
LGLLALVPGLPTFPFLFLAGALAFLAWYLRRRSKQEEEAAAEAAKAQEEAAEEEEESINDILALDDLELE
LGYGLIPLVDDSQGGDLLDRIRSIRKQLAQEYGFVMPVIRIRDNLRLPPNEYRIKIKGVEVARGELRPGK
YLAMNPGNADGEIPGEETREPAFGLPAYWISEKNKEEAERLGYTVVDPATVLATHLSEVIKNNAAELLTR
QEVQNLLDRLKEEYPKLVEELIPDKVPLGTIQKVLQLLLRERVSIRNLPTILETLADYAPITKDPDLLVE
HVRQRLGRQITQQYLDEDGVLPVITLDPDLEAALAEALKRDGEGELLDLEPALLEELVRAVRKAVEKLAN
NGERPVLLTSPRVRPYVRRILERFFPELPVLSYNEIPDNVRVETVGVV
>gnl|CDD|273600 TIGR01399, Secretion_system_apparatus_protein_SsaV, type III secretion protein, HrcV family. Members of this family are closely homologous to the flagellar biosynthesis protein FlhA (TIGR01398) and should all participate in type III secretion systems. Examples include InvA (Salmonella enterica), LcrD (Yersinia enterocolitica), HrcV (Xanthomonas), etc. Type III secretion systems resemble flagellar biogenesis systems, and may share the property of translocating special classes of peptides through the membrane [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
ARSDLVLALLLLAIISMMILPLPTLLVDILIAINITISVLLLMIAIYIPRPLALSTFPSVLLITTLFRLA
LSISTTRLILLHADAGNIIEAFGQFVVGGNLAVGLVIFLIITIVQFIVITKGSERVAEVSARFSLDAMPG
KQMSIDADLRAGVIDADEARRRRSTLEKESQLYGAMDGAMKFVKGDAIAGIIIVLINIIGGISIGVTQHG
MSASEALHLYTVLTIGDGLVSQIPALLISVTAGIIVTRVPGEAERNLGREIGHQLTSQPRALLLAAVLLL
GFALIPGFPLLVFALLAVLLAAAGYLLSRRKRSRAKANKAQASGAVASAPGAAAPIKNLDPFAEACPLIL
RLSPDLQSSADKDTLDQEIERMRWALFEDLGIPLPGIIIRVGDSLPDNEFRILLYEVPVLRDTIPPGHVA
LNDGVDNIEVAGIPAISGKRWPGESQRVWVTEEGAEKLQGAGLGYFSDSQVITHRLKATLLRNAQEFIGI
QETRYLLDQMEREYPELVKEVQRVLPLQRIAEVLQRLVSEQVSIRNLRLILETLIEWAQREKDVVMLTEY
VRIALKRYICHRYANGGRQLSAVLIDPEIEELIRGAIRQTSTGTYLALDPDDSEQLLDQIRQAVGDLPRA
PSQPVLLTSMDIRRYVRKMIESEFPDLPVLSYQELGEEIEVQVLGRI
>gnl|CDD|130467 TIGR01400, Flagellar_biosynthetic_protein_FliR, flagellar biosynthetic protein FliR. This model recognizes the FliR protein of bacterial flagellar biosynthesis. It distinguishes FliR from the homologous proteins bacterial type III protein secretion systems, known by names such as YopT, EscT, and HrcT [Cellular processes, Chemotaxis and motility]
VSTFFLPFVRVGAFLMTMPFFSERLVPVRVRLYLALALTFIVLPFLPPSPPPVNLFSLFFVLLLLQEILI
GLLIGFILQLLFAAFVLAGEIISMQMGLGFASMVDPSSGEQTPILGQILYLLALLLFLALDGHHLLILGL
VDSFKSLPVGSFFLNGNFFELILKALSDMFLLGLLLALPIIAALLLVNLVLGLVNRAAPQINIFSIGFPL
KIALGLILLYLILPGMAILFKDLFEELLEALARLL
>gnl|CDD|130468 TIGR01401, Secretion_system_apparatus_protein_SsaT, type III secretion protein SpaR/YscT/HrcT. This model represents members of bacterial type III secretion systems homologous to the flagellar biosynthetic protein FliR (TIGRFAMs:TIGR01400) [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
MSQAFELLIALALAFARILPMFLLLPFFASGSLPGLIRNGVIVVLALPIAPHISTALLALDITFSLAGLL
LKEVIIGLLLGFLLALPFWIFEAAGFLIDNQRGATLSSIFNPATGVDTSPLGVLFNQFLIVIFLTSGGME
FLLGALYESYRLWPLTAFLNFSAQGLSFVLSQLDQMMALALLLAAPVIIVLFLIELALGLLSRFAPQLNV
FILSLPIKSLLALLILLLYFATLLEHIGEELLFLHDQLQLLDP
>gnl|CDD|130469 TIGR01402, Flagellar_biosynthetic_protein_FliQ, flagellar biosynthetic protein FliQ. This model describes FliQ, a protein involved in biosynthesis of bacterial flagella. A related family of proteins, excluded from this model, participates in bacterial type III protein secretion systems [Cellular processes, Chemotaxis and motility]
MTEETVLDLGREAIWLTLLLSAPVLLVALVVGLVISIFQAATQIQEQTLSFIPKIIAILLALALLGPWML
TKLLDFTREIFQRIPQGI
>gnl|CDD|130470 TIGR01403, Secretion_system_apparatus_protein_SsaS, type III secretion protein, HrpO family. This model represents one of several families of proteins related to bacterial flagellar biosynthesis proteins and involved in bacterial type III protein secretion systems. This family is homologous to, but distinguished from, flagellar biosynthetic protein FliQ. This model may not identify all type III secretion system FliQ homologs [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
DIVQLTNQALLLVLILSLPPVLVAAIVGLLVSLLQALTQLQDQTLPFAIKLIAVFITLMLTAGWLGAEIL
NFANQIFTMIP
>gnl|CDD|130471 TIGR01404, Surface_presentation_of_antigens_protein_SpaS, type III secretion protein, YscU/HrpY family. This model represents one of several families of proteins related to bacterial flagellar biosynthesis proteins and involved in bacterial type III protein secretion systems. This family is homologous to, but distinguished from, flagellar biosynthetic protein FlhB (TIGRFAMs model TIGR00328). This model may not identify all type III secretion system FlhB homologs [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
AEKTEKPTPKKLRDARKKGQVAKSKDLTSAVLLLAGFFYLLSLASVFEEMLIALLILPLDFDDQPFAYAL
AQVLSGLLQLILTVLLPLLAIVLLAGVLSGLLQVGFVLATEALKPDLSKLNPISGLKQIFSLRSLKELLK
SILKLVALALIFYLFLKNYLKELFALPYCGLDGLAPIVGELLKLLILVCLGFFLVVGLADFAFQRYLFMK
DLKMSKDEVKREYKEQEGDPEIKSKRRELHQEILSEQLKSDVKRSTLVVANPTHIAIGIYYKPGETPLPL
IICKGTDAQALAVRAYAEEAGIPVVRDIPLARQLYRTARVGQYIPEELFEAVAELLRWLEQV
>gnl|CDD|273601 TIGR01405, DNA_polymerase_III_PolC-type, DNA polymerase III, alpha chain, Gram-positive type. This model describes a polypeptide chain of DNA polymerase III. Full-length homologs of this protein are restricted to the Gram-positive lineages, including the Mycoplasmas. This protein is designated alpha chain and given the gene symbol polC, but is not a full-length homolog of other polC genes. The N-terminal region of about 200 amino acids is rich in low-complexity sequence, poorly alignable, and not included n this model [DNA metabolism, DNA replication, recombination, and repair]
EKINEEENRVKIEGYIFKIEIKELKSGRTLLKIKVTDYTDSLILKKFLKSEEDPEKFDGIKIGKWVRARG
KIELDNFSRDLQMIIKDIEEIPYAERKDNAKEKRVELHFHTKMSQMDAITSVQEYVKQAKKWGHKAIAIT
DHGVVQAFPEAYKAAKKDGIKIIYGMEANLVDDRVPIVYNPDDQKLLDDATYVVFDIETTGLSPQYDEII
EFGAVKVKNGRIIDKFQFFIKPHEPLSAFVTELTGITQDMLENAPEIEEVLEKFKEFFKDSILVAHNASF
DIGFLNTNFEKVGLEPLENPVIDTLELARALNPEYKSHRLGNICKKLGVDLDDHHRADYDAEATAKVFKV
MVEQLKEKGITNLEELNNKLSSEELYKRLRPNHIIIYAKNQAGLKNLYKLVSISLTKYFYTRPRILRSLL
KKYREGLLIGSACSEGELFDALLSKPDDELEEIAKRYDFIEIQPPGNYAHLIEREQVKDKEALKEIIKKL
IELAKELNKPVVATGDVHYIEPEDKIYRKILVASQGLGNPLNRHFNPKEVPELHFRTTNEMLDEFSFLGE
EKAYEIVVENTNKIADQIEEIQPIKDKLYTPKIEGADEKIRDLTYENAKKIYGDPLPEIVEQRIEKELKS
IIGNGFAVIYLISQLLVQKSLQDGYLVGSRGSVGSSLVATMTGITEVNPLPPHYLCPNCKYSEFITDGSV
GSGFDLPDKDCPKCGAPLKKDGQDIPFETFLGFKGDKVPDIDLNFSGEYQAKAHNYVKELFGEDHTFRAG
TIGTVAEKTAYGYVKKYFEDQGKHYRDAEIERLVQGCTGVKRTTGQHPGGIIIVPKYMDVYDFTPVQYPA
DDTNSDWKTTHFDFHSIHDNLLKLDILGHDDPTMIKMLQDLTGIDPKTIPMDDKEVMSIFSSPKALGVTP
EEILEKTGTLGIPEFGTKFVRGMLEETKPKTFADLVRISGLSHGTDVWLGNAQDLIKSGIKTLSDVIGCR
DDIMVYLIHKGLEPKLAFKIMEKVRKGKGLKAEYIELMKENKVPEWYIESCLKIKYMFPKAHAAAYVLMA
WRIAYFKVHYPLEYYAAYFSIRAKAFDLETMIKGKEFIKQKLEEINTRRKINKASPKEKDLLTVLEIVLE
MMARGFKFQPIDLYKSQATEFLIEGNTLIPPFNAIPGLGENVANSIVEARNEKPFLSKEDLKKRTKISKT
HIEKLDSMGVLDNLPETNQLSLF
>gnl|CDD|130473 TIGR01406, DNA_polymerase_III_subunit_epsilon, DNA polymerase III, epsilon subunit, Proteobacterial. This model represents DnaQ, the DNA polymerase III epsilon subunit, as found in most Proteobacteria. It consists largely of an exonuclease domain as described in pfam00929. In Gram-positive bacteria, closely related regions are found both in the Gram-positive type DNA polymerase III alpha subunit and as an additional N-terminal domain of a DinG-family helicase. Both are excluded from this model, as are smaller proteins, also outside the Proteobacteria, that are similar in size to the epsilon subunit but as different in sequence as are the epsilon-like regions found in Gram-positive bacteria [DNA metabolism, DNA replication, recombination, and repair]
RQIILDTETTGLDPKGGHRIVEIGAVELVNRMLTGDNFHVYVNPERDMPAEAAKVHGITDEFLADKPKFK
EIADEFLDFIGGSELVIHNAAFDVGFLNYELERLGPTIKKIGEFCRVIDTLAMARERFPGQRNSLDALCK
RFKVDNSHRTLHGALLDAHLLAEVYLALTGGQESLLELAESNSGEAAKPSKSAEMKLGATLRVLAPREAE
LQAHEAYLDKLLKKS
>gnl|CDD|273602 TIGR01407, dinG_rel, DnaQ family exonuclease/DinG family helicase, putative. This model represents a family of proteins in Gram-positive bacteria. The N-terminal region of about 200 amino acids resembles the epsilon subunit of E. coli DNA polymerase III and the homologous region of the Gram-positive type DNA polymerase III alpha subunit. The epsilon subunit contains an exonuclease domain. The remainder of this protein family resembles a predicted ATP-dependent helicase, the DNA damage-inducible protein DinG of E. coli [DNA metabolism, DNA replication, recombination, and repair]
RYAVVDLETTGTQLSFDKIIQIGIVVVEDGEIVDTFHTDVNPNEPIPPFIQELTGISDNMLQQAPYFSQV
AQEIYDLLEDGIFVAHNVHFDLNFLAKALKDCGYEPLPKPRIDTVELAQIFFPTEESYQLSELSEALGLT
HENPHRADSDAQATAELLLLLFEKMEKLPLDTLEQLLELSDQLLYESYDIIQETYRQYKIKPAPKSYEVV
EQIAYRKQVASKKPETNYNTLSSLFSKNIDRLGLEYRPEQLKLAELVLDQLTHSEKSLIEAPTGTGKTLG
YLLPALYYAITEKPVVISTNTKVLQSQLLEKDIPLLNEILNFKINAALIKGKSNYLSLGKFSQILKDNTD
NYEFNIFKMQVLVWLTETETGDLDELNLKGGNKMFFAQVRHDGNLSKKDLFYEVDFYNRAQKNAEQAQIL
ITNHAYLITRLVDNPELFPSFRDLIIDEAHHLPDIAENQLQEELDYADIKYQIDLIGKGENEQLLKRIQQ
LEKQEILEKLFDFETKDILKDLQAILDKLNKLLQIFSELSHKTVDQLRKFDLALKDDFKNIEQSLKEGHT
SWISIENLQQKSTIRLYIKDYEVGDVLTKRLLPKFKSLIFTSATLKFSHSFESFPQLLGLTDVHFNTIEP
TPLNYAENQRVLIPTDAPAIQNKSLEEYAQEIASYIIEITAITSPKILVLFTSYEMLHMVYDMLNELPEF
EGYEVLAQGINGSRAKIKKRFNNGEKAILLGTSSFWEGVDFPGNGLVCLVIPRLPFANPKHPLTKKYWQK
LEQEGKNPFYDYVLPMAIIRLRQALGRLIRRENDRGSIVILDRRLVGKRYGKRFEKSLPEYLQVKGDILG
ELLEAIKEFL
>gnl|CDD|273603 TIGR01408, ubiquitin_activating_enzyme, ubiquitin-activating enzyme E1. This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions
EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFL
SEDDVGRNRAEAVVKKLAELNPYVHVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQCPPIAF
ISADVRGLFGSLFCDFGDEFEVLDTDGEEPKTGFIASITQANPGIVTCLENHRHKLETGDFVTFREVNGM
TGLNDGSPRKITVISPYSFSIGDTTELGPYLHGGIATQVKTPKTVFFKSLREQLKDPKCLIVDFSKPERP
PEIHTAFQALDQFQEKYSRKPNVGCQQDAEELLKLATSISETLEEKVPDVDAKLVHWLSWTAQGFLSPMA
AAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAESLPSLGKPECEEFLPRGDRYDAQIAVFGDTFQQKLQNL
NIFLVGCGAIGCEMLKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKI
NPQIKIDAHQNRVGPETETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNTQV
VVPHLTESYGSSRDPPEKEIPFCTLKSFPAAIEHTIQWARDKFEGLFSHKPSLVNKYLSSPSSAEEVLQK
IQSGHSREGLEQIIKLLSKEKPRNFSQCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPFWSSPKRP
PSPLKFDLNEPLHLSFIQAAAKLYATVYGIPFAEEDLSADALLNILSEVKIPEFKPRSNKKIQTDETARK
PDTAPIDDRNAIFQLEKAILSNEATKSDFRMAPLSFEKDDDHNGHIDFITAASNLRAKNYSIEPADRFKT
KFIAGKIIPAIATSTATVSGLVCLELIKVTDGGYKFEVYKNCFLNLAIPLFVFTEPTEVRKTKIRNGISF
TIWDRWTLHGDFTLLEFINAVKEKYGLEPTMVSQGVKLLYVPVMPGHAERLKLKMHKLVKPTTKKKLPPY
RVHLTVSFACDDDGDEDVPGPPVRIY
>gnl|CDD|273604 TIGR01409, Periplasmic_hydrogenase_small_subunit, Tat (twin-arginine translocation) pathway signal sequence. Proteins assembled with various cofactors or by means of cytosolic molecular chaperones are poor candidates for translocation across the bacterial inner membrane by the standard general secretory (Sec) pathway. This model describes a family of predicted long, non-Sec signal sequences and signal-anchor sequences (uncleaved signal sequences). All contain an absolutely conserved pair of arginine residues, in a motif approximated by (S/T)-R-R-X-F-L-K, followed by a membrane-spanning hydrophobic region. Members with small amino acid side chains at the -1 and -3 positions from the C-terminus of the model should be predicted to be cleaved as are Sec pathway signal sequences. Members are almost exclusively bacterial, although archaeal sequences are also found. A large fraction of the members of this family may have bound redox-active cofactors [Protein fate, Protein and peptide secretion and trafficking]
LSRRDFLKGAAAAGAAAGLGALLPSPARA
>gnl|CDD|130477 TIGR01410, Sec-independent_protein_translocase_protein_tatB., twin arginine-targeting protein translocase TatB. This model represents the TatB protein of a Sec-independent system for transporting folded proteins, often with a bound redox cofactor, across the bacterial inner membrane. TatC is the multiple membrane spanning component. TatB, like the related TatA/E proteins, appears to span the membrane one time. The tat system recognizes proteins with an elongated signal sequence containing a conserved R-R in a motif approximated by RRxFLK N-terminal to the transmembrane helix. TIGRFAMs model TIGR01409 describes this twin-Arg signal sequence. A similar system, termed Delta-pH-dependent transport, operates on chloroplast-encoded proteins [Protein fate, Protein and peptide secretion and trafficking]
FDIGFSELLLIAVVALVVLGPERLPVAIRTVGGFVRALRGMASDVKNELDEELKLQELDDQLKKAQQARF
LNLTAELKDS
>gnl|CDD|273605 TIGR01411, Sec-independent_protein_translocase_protein_TatA, twin arginine-targeting protein translocase, TatA/E family. This model distinguishes TatA/E from the related TatB, but does not distinguish TatA from TatE. The Tat (twin-arginine translocation) system is a Sec-independent exporter for folded proteins, often with a redox cofactor already bound, across the bacterial inner membrane. Functionally equivalent systems are found in the chloroplast and some in archaeal species. The signal peptide recognized by the Tat system is modeled by TIGR01409 [Protein fate, Protein and peptide secretion and trafficking]
GLSPPEWLIILVVILLLFGAKKLPELGRDLGKAIKEFKKALKEEEDE
>gnl|CDD|273606 TIGR01412, Probable_deferrochelatase/peroxidase_EfeN, Tat-translocated enzyme. This model represents a small family of proteins with a typical Tat (twin-arginine translocation) signal sequence, suggesting that the family is exported in a folded state, perhaps with a bound redox cofactor. Members of this family show homology to Dyp, a dye-decolorizing peroxidase from Geotrichum candidum that lacks any typical heme-binding site
SANAPTQPSRRRLLKTAGAAGLAGAAAAAGAGAVAVATAAKTAFSLPDDESEAVPFYGKHQAGITTPQQA
RGHFVAFDVTAKDRKAIEALFRRWTARARRLTAGGAVGEGANNPLAPPDDTGEARDLGPSNLTVTFGFGH
SLFDRFGLADKRPVALADLPDFPNDNLDKNRSGGDLCVQICADDPQVAFHALRNIIRHAGGTAVVRWSQN
GFISGATKGKETPRNLLGFKDGTRNPKPGEDDLLDRVVWVDEEGEPAWMTGGSYQVVRRIRMHLETWDRT
SLKEQEDVFGRRKSSGAPLGGAKESDEPDLAKDPEGEVIPKDAHVRLAKPDQNGGAAMLRRAFSYTDGTD
ATGQLDAGLLFVCYQADPLKGFIPVQRNLAGDALNEYIQHIGSGLFAVPPGVKKGEYLGQRLLE
>gnl|CDD|273607 TIGR01413, Probable_deferrochelatase/peroxidase_EfeN, Dyp-type peroxidase family. A defined member of this superfamily is Dyp, a dye-decolorizing peroxidase that lacks a typical heme-binding region. A distinct, uncharacterized branch (TIGR01412) of this superfamily has a typical twin-arginine dependent signal sequence characteristic of exported proteins with bound redox cofactors
QPGILTPHQAAAIFLAFDVTADRAALEALLRALTALADLLTAGGAAGPPSRLTVTVGFGSSLWDRLGLAD
KRPKELKDFPELGGDSLDAPSTGGDLLFHIRADDPDVVFHAARALLRRFGDAVTVRDEVHGFRYPGAETG
RDLLGFVDGTENPKGPEALEAVLVIGEDPAWAAGGSYVVVQRIQHDLEEWDRLPLAEQEDVIGRRKSSGA
ELDGKERAPADSHVRLTNPREDGKGLKILRRGLPYGDGSDDTGQDAGLLFIAYQRSLENGEVQLQRMLGG
TDGATDRLLEFIRPVGGGYFFAPSGVAL
>gnl|CDD|273608 TIGR01414, Contains:_AIDA-I_translocator, outer membrane autotransporter barrel domain. A number of Gram-negative bacterial proteins, mostly found in pathogens and associated with virulence, contain a conserved C-terminal domain that integrates into the outer membrane and enables the N-terminal region to be delivered across the membrane. This C-terminal autotransporter domain is about 400 amino acids in length and includes the aromatic amino acid-rich OMP signal, typically ending with a Phe or Trp residue, at the extreme C-terminus [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
PGGAFNTLTVNGLYTGNGGFVMNTDLGGDNSQTDRLVVNGNASGTTGVVVNNIGGEGAQTGDGITLVTVN
GGSDAAFTLANGKVDAGAYTYTLYKNGTEDNNNWYLTSSLPDLTPPGQQLSPTYRAEAGSYAANANAALF
LAELDTLRQRMGDLRSAARDAGNGVWARIFGGDNHLDGDAGAAGYDQNTTGVQLGGDILLAGNADGDLHV
GLMAGYAKADIKTRSYKYGGKGKVDGYGLGLYGTWLQDSGAYVDGVLQYSRFRNDVSSTGSNGKVSGKYN
SNGFTASLEAGYRYNLGGNGWYVEPQAQLSYFGVSGDDYKESNGTRVLGGGGDSLQGRLGLRVGYQFDLG
TGRAVKPYLKANVLHEFKGGTGVRVNGVTIRNDFSGTRAEYGVGVNAKIKDNLSLYADVDYQKGGKKYTD
NQGNLGVRYSF
>gnl|CDD|273609 TIGR01415, Tryptophan_synthase_beta_chain_2, pyridoxal-phosphate dependent TrpB-like enzyme. This model represents a family of pyridoxal-phosphate dependent enzyme (pfam00291) closely related to the beta subunit of tryptophan synthase (TIGR00263). However, the only case in which a member of this family replaces a member of TIGR00263 is in Sulfolobus species which contain two sequences which hit this model, one of which is proximal to the alpha subunit. In every other case so far, either the species appears not to make tryptophan (there is no trp synthase alpha subunit), or a trp synthase beta subunit matching TIGR00263 is also found [Unknown function, Enzymes of unknown specificity]
IPKHWYNILPDLPEPLPPPLDPEGEEPIAIEKLKRIFPEKLLEQEVSGERWIKIPGEVLKRYAQIGRPTP
LIRAKGLEELLGTPARIYYKYESVSPTGSHKINTAIAQAYYAKIEGAKRLVTETGAGQWGSALSLAGALF
GLECKVFMVRVSFNQKPYRKYLMELYGAEVIPSPSEFTEFGREVLKEDPDHPGSLGIAISEAIEYALSDE
DTKYSLGSVLNHVLLHQTVIGLEAKKQMEEAGEDPDVIIGCVGGGSNFAGLAFPFVADKLSGKIDRRFIA
AEPKACPTLTRGEYRYDFGDTAGLTPLLKMYTLGHDFIPPPIHAGGLRYHGVAPTLSLLVNLGIVEARAY
DQEEAFEAAVIFAKTEGIVPAPESAHAIAAAIDEARKCRETGEEKVILFNLSGHGLLDLKAYAKYLHGE
>gnl|CDD|273610 TIGR01416, Rieske_proteo, ubiquinol-cytochrome c reductase, iron-sulfur subunit. This model represents the Proteobacterial and mitochondrial type of the Rieske [2Fe-2S] iron-sulfur as found in ubiquinol-cytochrome c reductase. The model excludes the Rieske iron-sulfur protein as found in the cytochrome b6-f complex of the Cyanobacteria and chloroplasts. Most members of this family have a recognizable twin-arginine translocation (tat) signal sequence (DeltaPh-dependent translocation in chloroplast) for transport across the membrane with the 2Fe-2S group already bound. These signal sequences include a motif resembling RRxFLK before the transmembrane helix [Energy metabolism, Electron transport]
TRRDFLYAATGAVGAVGAAAAAVPFIDSMNPSASVKAAGAPTEVDVSKIQPGQQLTVEWRGKPVFIRRRT
KKEIDELKALDLGALKDPNSEAQQPDYARVKRSGKPEWLVVIGICTHLGCIPTYGPEEGDKGGFFCPCHG
SHYDTAGRVRKGPAPLNLPVPPYKFLSDTTILIG
>gnl|CDD|273611 TIGR01417, Phosphoenolpyruvate-protein_phosphotransferase, phosphoenolpyruvate-protein phosphotransferase. This model recognizes a distinct clade of phophoenolpyruvate (PEP)-dependent enzymes. Most members are known or deduced to function as the phosphoenolpyruvate-protein phosphotransferase (or enzyme I) of PTS sugar transport systems. However, some species with both a member of this family and a homolog of the phosphocarrier protein HPr lack a IIC component able to serve as a permease. An HPr homolog designated NPr has been implicated in the regulation of nitrogen assimilation, which demonstrates that not all phosphotransferase system components are associated directly with PTS transport
ISGIGVSPGIAIGKALLLKKPDLVIDRKKISASQVDQEISRFLSARAKAKEDLETIKTKAGKTFGQEKAA
IFEAHILILEDPELTEEVIELIKKDHKNAEFAAHEVFEGQAKSLEEMDDEYLKERAADIRDIGNRLLGHL
LGVKISDLSEIQDEVILVAEDLTPSETAQLNLKYVKGFLTDAGGKTSHTAIMARSLEIPAIVGTKSVTSQ
VKNGDTVIIDGVKGIVIFNPSSETIDKYEAKQEAVSSEKAELAKLKDKPAITLDGHQVELAANIGTVDDV
EGAERNGGEGIGLFRTEFLYMSRDQLPTEEEQFAAYKTVLEAMESDAVIVRTLDIGGDKELPYLNFPKEE
NPFLGYRAIRLALEREEILRTQLRAILRASAYGKLRIMFPMVATVEEIRAVKQELEEEKQELNDEGKAFD
ENIEVGVMIEIPSAALIADHLAKEVDFFSIGTNDLTQYTLAVDRGNDLISNLYQPYNPAVLRLIKLVIDA
AKAEGIWVGMCGEMAGDERAIPLLLGLGLRELSMSASSILRIKMIIRKLNIEECKSLAEKALAQPTTEEV
HKLVN
>gnl|CDD|273612 TIGR01418, Phosphoenolpyruvate_synthase, phosphoenolpyruvate synthase. Also called pyruvate,water dikinase and PEP synthase. The member from Methanococcus jannaschii contains a large intein. This enzyme generates phosphoenolpyruvate (PEP) from pyruvate, hydrolyzing ATP to AMP and releasing inorganic phosphate in the process. The enzyme shows extensive homology to other enzymes that use PEP as substrate or product. This enzyme may provide PEP for gluconeogenesis, for PTS-type carbohydrate transport systems, or for other processes [Energy metabolism, Glycolysis/gluconeogenesis]
LILWLEEVRKDDVPLVGGKNASLGEMIQNLSPAGVPVPPGFVVTAEAYRYFLEENGIAQKIRDLLEELDV
EDVDALAAASAEIRELILNTPFPPDLEEAIREAYDKLSEDYGKEEADVAVRSSATAEDLPDASFAGQQET
YLNVTGEEEVLEHVKKCWASLFTDRAISYRVSQGFDHEKVAIAVGVQKMVRSDLGSSGVMFTIDTETGFK
DAVFIESAWGLGEAVVGGAVTPDEYVVFKPTLEQGKKAILERTLGSKKIKMVYDPDGGGVETKIVEVPEE
ERDAFSLSDEEILELAKLAVLIEKHYGRPMDIEWAKDGFDGEIFIVQARPETVQSRKKKENVEERYELKG
KGKVLVTGRAAGPGIASGKVKVIFDLKEMDKFEEGDILVTDMTDPDWEPAMKRASAIVTNEGGMTCHAAI
VARELGIPAVVGTGDATKTLKDGMEVTVDCAEGDTGYVYAGKLEHEVKEVELSNMPVTATKIYMNVGNPE
VAFRFAALPNDGVGLARIEFIILNWIGKHPLALIDDDDLESVEKNEIEELMAGNPRDFFVDKLAEGIAKV
AAAFYPKPVIVRTSDFKSNEYRNLIGGEEYEPDEENPMLGWRGASRYYSESYEEAFRLECRAIKRVREEM
GLTNVEVMIPFVRTPEEGKRALEIMAEEGLRRGKNGLEVYVMCEVPSNALLADEFAKEFDGFSIGSNDLT
QLTLGVDRDSGLVAHLFDERNPAVLRLIEMAIKAAKEHGKKVGICGQAPSDYPEVVEFLVEEGIDSISLN
PDAVLRTRLQVAEVEK
>gnl|CDD|162350 TIGR01419, nitro_reg_IIA, PTS IIA-like nitrogen-regulatory protein PtsN. This model describes a full-length protein of about 160 residues closely related to the fructose-specific phosphotransferase (PTS) system IIA component. It is a regulatory protein found only in species with a phosphoenolpyruvate-protein phosphotransferase (enzyme I of PTS systems) and an HPr-like phosphocarrier protein, but not all species have a IIC-like permease. Members of this family are found in Proteobacteria, Chlamydia, and the spirochete Treponema pallidum [Signal transduction, PTS]
SLIGLLLPEAIRVAMECGSKKRLLEIISLLAARELSLPEQDVFECLLAREKLGSTGVGNGIAIPHGRLSG
LKQPVGVFIRLDAPVDFDALDGKPVDLLFALLVPENATAEHLEALSRIARKLSDKTICRRLRAASAEEIY
QILTD
>gnl|CDD|273613 TIGR01420, pilT_fam, pilus retraction protein PilT. This model represents the PilT subfamily of proteins related to GspE, a protein involved in type II secretion (also called the General Secretion Pathway). PilT is an apparent cytosolic ATPase associated with type IV pilus systems. It is not required for pilin biogenesis, but is required for twitching motility and social gliding behaviors, shown in some species, powered by pilus retraction. Members of this family may be found in some species that type IV pili but have related structures for DNA uptake and natural transformation [Cell envelope, Surface structures, Cellular processes, Chemotaxis and motility]
SLEEILREAVKLGASDIHLTAGAPPAMRIDGDLVRIEFEPLTPEDTQKLAREILSEKQREEFEENGELDF
SFSLPGVGRFRVNAFYQRGGVALVLRLIPSKIPTFEELGLPPVLRELAERPRGLILVTGPTGSGKSTTLA
SMIDYINKNKAYHIITIEDPIEYVHTNKRSLINQREVGEDTLSFANALRAALREDPDVILIGEMRDLETV
ELALTAAETGHLVFGTLHTNSAAQTIERIIDVFPAEEQEQIRTQLAESLVAIISQRLLPKADGGGRVLAV
EILINTPAVRNLIREGKTHQIKSLIQTGQQLGMQTFDQHLAQLYKKGLITLEDALEAAPSPHE
>gnl|CDD|273614 TIGR01421, Glutathione_reductase, glutathione-disulfide reductase, animal/bacterial. The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria [Energy metabolism, Electron transport]
KHYDYLVIGGGSGGIASARRAAEHGAKALLVEAKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFY
QNDENTFNWPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRDYTAPHILIATGGK
PSFPENIPGAELGTDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMIS
ETITEEYEKEGINVHKLSKPVKVEKTVEGKLVIHFEDGKSIDDVDELIWAIGRKPNTKGLGLENVGIKLN
EKGQIIVDEYQNTNVPGIYALGDVVGKVELTPVAIAAGRKLSERLFNGKTDDKLDYNNVPTVVFSHPPIG
TIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSEKQKCRMKLVCAGKEEKVVGLHGIGDGVDEMLQGFA
VAIKMGATKADFDNTVAIHPTSSEELVTMR
>gnl|CDD|188140 TIGR01422, phosphonatase, phosphonoacetaldehyde hydrolase. This enzyme catalyzes the cleavage of the carbon phosphorous bond of a phosphonate. The mechanism depends on the substrate having a carbonyl one carbon away from the cleavage position. This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), and contains a modified version of the conserved catalytic motifs of that superfamily: the first motif is usually DxDx(T/V), here it is DxAxT, and in the third motif the normal conserved lysine is instead an arginine. Additionally, the enzyme contains a unique conserved catalytic lysine (B. cereus pos. 53) which is involved in the binding and activation of the substrate through the formation of a Schiff base. The substrate of this enzyme is the product of 2-aminoethylphosphonate (AEP) transaminase, phosphonoacetaldehyde. This degradation pathway for AEP may be related to its toxic properties which are utilized by microorganisms as a chemical warfare agent [Central intermediary metabolism, Other]
RIEAVIFDWAGTTVDFGSFAPTGAFVEAFAEFGVQITLEEARKPMGLGKWDHIRALLKMPAVAERWQAKF
GRLPTEADVQALYEAFEPMQLAKLAEYASPIPGAIEVIAYLRARGIKIGSTTGYTREMMDVVAPEAAAQG
YRPDYNVTADDVPAGRPAPWMALKNATELGVYDPAAVVKVGDTVPDIEEGRNAGMWTVGVILSSNELGLS
EEEYRALPPAELEERRARARARLKAAGAHYVIDTLADLPAVIA
>gnl|CDD|200098 TIGR01423, Trypanothione_reductase, trypanothione-disulfide reductase. Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase
SKAFDLVVIGAGSGGLEAGWNAATLYKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMD
TLRESAGFGWEFDRSSVKANWKALIAAKNKAVLDINKSYEGMFADTEGLTFFLGWGALEDKNVVLVRESA
DPKSAVKERLQAEHILLATGSWPQMLGIPGIEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAYK
PRGGKVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFESGKTLDVDVV
MMAIGRVPRTQTLQLDKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFG
NKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEKVAVYESSFTPLMHNISGSKYKKFVAKIVTNHAD
GTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEELCSMRTPSYYYQKGEKMEKL
>gnl|CDD|213618 TIGR01424, Glutathione_reductase_cytosolic, glutathione-disulfide reductase, plant. The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of plants and some bacteria, including cyanobacteria [Energy metabolism, Electron transport]
FDYDLFVIGAGSGGVRAARLAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWT
VGKARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKTYTAEKILIAVGG
RPPKPALPGHELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGFDDDMR
RGLAAALEERGIRILPEDSITSISKDDDGRLKATLSKHEEIVADVVLFATGRSPNTNGLGLEAAGVRLND
LGAIAVDEYSRTSTPSIYAVGDVTDRINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTV
GLTEEEARRKFGDIEVYRAEFRPMKATFSGRQEKTLMKLVVDAKDDKVLGAHMVGPDAAEIIQGLAIALK
MGATKDDFDSTVAVHPTSAEELVTMR
>gnl|CDD|273615 TIGR01425, Signal_recognition_particle_54_kDa_protein_homolog, signal recognition particle protein SRP54. This model represents examples from the eukaryotic cytosol of the signal recognition particle protein component, SRP54. This GTP-binding protein is a component of the eukaryotic signal recognition particle, along with several other protein subunits and a 7S RNA. Some species, including Arabidopsis, have several closely related forms. The extreme C-terminal region is glycine-rich and lower in complexity, poorly conserved between species, and excluded from this model
VLAQLGSSLVTALRSMSSATVIDEEVINTMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINK
RKLIQDAVFEELCNLVDPGVEAFTPKKGKTCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFR
AGAFDQLKQNATKAGIPFYGSYEESDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREA
IKPDSIIFVMDGSIGQAAFGQAKAFKDSVEVGSVIITKLDGHAKGGGALSAVAATKSPIIFIGTGEHVDE
FEIFDAEPFVSKLLGMGDLKGLIDKVQDLALNDEEKTLIEHLKEGTFTLRDWYEQFQNLLKMGPLGNIMS
MIPGLSHPMMSKGNEEETSAKIKVFMTIMDSMTDRELDSTAKTMLKDPSRIRRVARGSGRDIREVNELLE
QYKLFAQM
>gnl|CDD|273616 TIGR01426, Glycosyl_transferase, glycosyltransferase, MGT family. This model describes the MGT (macroside glycosyltransferase) subfamily of the UDP-glucuronosyltransferase family. Members include a number of glucosyl transferases for macrolide antibiotic inactivation, but also include transferases of glucose-related sugars for macrolide antibiotic production [Cellular processes, Toxin production and resistance]
FNIPAHGHVNPTLGVVEELVARGHRVTYATTEEFAERVEAAGAEFVLYGSALPPPDNPPENTEEEPIDII
EKLLDEAEDVLPQLEEAYKGDRPDLIVYDIASWTGRLLARKWDVPVISSFPTFAANEEFEEMVSPAGEGS
AEEGAIAERGLAEYVARLSALLEEHGITTPPVEFLAAPRRDLNLVYTPKAFQPAGETFDDSFTFVGPCIG
DRKEDGSWERPGDGRPVVLISLGTVFNNQPSFYRTCVEAFRDLDWHVVLSVGRGVDPADLGELPPNVEVR
QWVPQLEILKKADAFITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAELGLGRHLPPEEVTAEKLR
EAVLAVLSDPRYAERLRKMRAEIREAGGARRAADEIEGFLAE
>gnl|CDD|273617 TIGR01427, PTS_IIC_fructo, PTS system, fructose subfamily, IIC component. This model represents the IIC component, or IIC region of a IIABC or IIBC polypeptide of a phosphotransferase system for carbohydrate transport. Members of this family belong to the fructose-specific subfamily of the broader family (pfam02378) of PTS IIC proteins. Members should be found as part of the same chain or in the same operon as fructose family IIA (TIGR00848) and IIB (TIGR00829) protein regions. A number of bacterial species have members in two different branches of this subfamily, suggesting some diversity in substrate specificity of its members
ANTGTLEKKNFKKGIYKHLLTGVSYMLPFVVAGGIIIAISFLFGINAANNTGGNFNDLANWLMQIGGGVA
FALMVPILAGYIAYSIADRPGLAPGMIAGLIANNFNSGFLGGIIAGFLAGYVVKGLQKYIKKKLPQSLRG
LKPILIIPLLGTLIVGALIYGINIPVAYLNYGLSNWLNIMGSPNAALLGAIIGGMMAFDMGGPVNKAAYA
FGVGLIAAQGYIPMAAAMAAGMVPPLGIALATSIFKNRFTKEEREAGKACYVLGLCFISEGAIPFAAADP
KRVIPACIIGSAVTGAISMAFGVTLRAPHGGIFVLPILKAVVALLCYLIAIIVGSLVTAVIIGFLK
>gnl|CDD|130495 TIGR01428, Haloacetate_dehalogenase, 2-haloalkanoic acid dehalogenase, type II. Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related
IKALVFDVYGTLFDVHSVAERAAELYGGRGEALSQLWRQKQLEYSWLRTLMGPYKDFWDLTREALRYLLG
RLGLEDDESAADRLAEAYLRLPPHPDVPAGLRALKERGYRLAILSNGSPAMLKSLVKHAGLDDPFDAVLS
ADAVRAYKPAPQVYQLALEALGVPPDEVLFVASNPWDLGGAKKFGFKTAWINRPGEPP
>gnl|CDD|273618 TIGR01429, AMP_deaminase_3, AMP deaminase. This model describes AMP deaminase, a large, well-conserved eukaryotic protein involved in energy metabolism. Most members of the family have an additional, poorly alignable region of 150 amino acids or more N-terminal to the region included in the model
EDLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQGYPESVPLEEGLPDFHPPPDPQEDPYCLDDD
APPIELGYLVRMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLE
SKFNLHELLNEMSELKEQKSVPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKK
LTLREVFDSLHLDPYDLSVDTLDVHADRNTFHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVK
EVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLARWIIDHDVFSPNVRWLIQVPRLYDVYRSKKLVPNFGDM
LENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHEDHMFSRKFPSPDEWTSEQNPPYSYYLYYM
YANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRKVPVLQYLYYLTQIPIAMS
PLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMCELARNSVL
QSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL
>gnl|CDD|273619 TIGR01430, Putative_adenosine/adenine_deaminase, adenosine deaminase. This family includes the experimentally verified adenosine deaminases of mammals and E. coli. Other members of this family are predicted also to be adenosine deaminase, an enzyme of nucleotide degradation. This family is distantly related to AMP deaminase
LPKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDF
KRLAYEYVEKAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPE
AAEETLELAKPYKEQTIVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGA
TRIGHGVRALEDPELLKRLAQENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSY
LTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKKELLAKL
>gnl|CDD|273620 TIGR01431, salivary_gland_growth_factor-2, adenosine deaminase-related growth factor. Members of this family have been described as secreted proteins with growth factor activity and regions of adenosine deaminase homology in insects, mollusks, and vertebrates
YDETRNHLILKEKSMRLGGKLVLTTKEKLANERIMTLKIAEMKEAMRTPLIFPPSMHFFQAKHLIERSQV
FKILRMMPKGAALHLHDLGIVSMDWLVRNVTYRPNLHICFTKRNIMVLRFRHPTPRPSECCSKWILLEDY
RKSQNVEEFDDSLLRNFTLVTTHPEVDYTTQNVVWSRFETIFFTLSGLLHYAPVFRDYYFRALEEFYEDN
VQYMELRSRLFPLYELSGTHHDEEWSVKTYKEVTEKFVEEHPDFIGIKIIYSDLRSKDVEEIAEYIKMAM
GLRIKYPDFVAGFDLVGQEDTGHSLLDYKDALLIPSIGVKLPYFFHAGETNWQGTSVDRNLLDALLLNTT
RIGHGFALSKHPAVRTYSKERDIPIEVCPISNQVLKLVSDLRNHPVATLMADNYPMVISSDDPAFWGAKG
LSYDFYEAFMGIAGMKADLRTLKQLALNSIKYSALSEEEKNTAMAKWKKQWDKFIDDVL
>gnl|CDD|273621 TIGR01432, AA3-600_quinol_oxidase_subunit_II, cytochrome aa3 quinol oxidase, subunit II. This enzyme catalyzes the oxidation of quinol with the concomitant reduction of molecular oxygen to water. This acts as the terminal electron acceptor in the respiratory chain. This subunit contains two transmembrane helices and a large external domain responsible for the binding and oxidation of quinol. QuoX is (presently) only found in gram positive bacteria of the Bacillus/Staphylococcus group. Like CyoA, the ubiquinol oxidase found in proteobacteria, the residues responsible for the ligation of Cu(a) and cytochrome c (found in the related cyt. c oxidases) are absent. Unlike CyoA, QoxA is in complex with a subunit I which contains cytochromes a similar to the cyt. c oxidases (as opposed to cytochromes b) [Energy metabolism, Electron transport]
ALLTVVFVLSGCSNIEVLNPKGPVASSQSDLILYSIVFMLVIVFVVFVLFTIFLVKYRYRKDNGAYSPKM
HGNAILETIWTVIPIIIVIALAIPTVKTIYDYEKAPKSTKEKDPMVVYATSADWKWFFSYPDEHIETVNY
LNIPKDRPVLFKLQSADTMTSFWIPQLGGQKYAMTGMTMNWYLQADEVGTYRGRNANFNGEGFADQTFDV
NAVSEKDFDKWVKETK
>gnl|CDD|213620 TIGR01433, precursor_Cytochrome_o_subunit_2_Oxidase, cytochrome o ubiquinol oxidase subunit II. This enzyme catalyzes the oxidation of ubiquinol with the concomitant reduction of molecular oxygen to water. This acts as the terminal electron acceptor in the respiratory chain. Subunit II is responsible for binding and oxidation of the ubiquinone substrate. This sequence is closely related to QoxA, which oxidizes quinol in gram positive bacteria but which is in complex with subunits which utilize cytochromes a in the reduction of molecular oxygen. Slightly more distantly related is subunit II of cytochrome c oxidase which uses cyt. c as the oxidant [Energy metabolism, Electron transport]
LSLIAASLLLSGCNLVLLDPKGQIGLEERSLILTAFGLMLLVVIPVILMTLFFAWKYRATNKDADYSPNW
HHSTKIEIVVWTIPILIIIFLGVLTWITTHKLDPYRPLASDVKPITIEVVALDWKWLFIYPEQGIATVNE
IAFPVNTPINFKITSNSVMNSFFIPQLGSQIYAMAGMQTKLHLIANEPGVYDGISANYSGPGFSGMKFKA
IATDRAAFDQWVAKAK
>gnl|CDD|213621 TIGR01434, Glutamate--cysteine_ligase, glutamate--cysteine ligase. Alternate name: gamma-glutamylcysteine synthetase. This model represents glutamate--cysteine ligase, and enzyme in the biosynthesis of glutathione (GSH). GSH is one of several low molecular weight cysteine derivatives that can serve to protect against oxidative damage and participate in a biosynthetic or detoxification reactions [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
SQALAWLEKNPQALKGIQRGIERETLRVNADGTLATTGHPEALGSALTHKWITTDFSEALLEFITPTDGD
IAHMLTFLRDLHRFTASKLGDERMWPLSMPCYIADGQDIEIAQYGTSNIGRFKTLYREGLKNRYGALMQT
ISGIHYNFSLPMAFWQAKRGAEGGESAKDKISAGYFRLIRNYYRFGWVIPYLFGASPAISSSFLQGKPTK
LPFEKTDEGMYYLPYATSLRLSDLGYTNKSQSNLGITFNDLQEYIASLKQAIKTPSEEYAKIGTKKDGKR
LQLNTNILQIENELYAPIRPKRVTRSGESPSDALLRRGIEYVEVRSLDINPFSPIGIDEQQVRFLDLFLV
WCALADSPEMSSGELLCTTDNWNRVILEGRKPGLTLGIGCETAQFPLPVVGKDLFRDLKRVAQTLDSIRG
GEAYQKACDELVACFDNPELTFSAQILRSMIDTGIGGTGLAFAEAYRELFREEPLEILEQERFEAERSAS
LRRQQEIERADTEPFATWLAKH
>gnl|CDD|273622 TIGR01435, glu_cys_lig_rel, glutamate--cysteine ligase/glutathione synthase, Streptococcus agalactiae type. This model represents a bifunctional protein family for the biosynthesis of glutathione, and perhaps a range of related gamma-glutamyltripeptides of the form gamma-Glu-Cys-X(aa). The N-terminal region is similar to proteobacterial glutamate-cysteine ligase. The C-terminal region is homologous to cyanophycin synthetase of cyanobacteria and, more distantly, to D-alanine-D-alanine ligases. Members of this family are found in Listeria and Enterococcus, Gram-positive lineages in which glutathione is produced (see PUBMED:8606174), and in Pasteurella multocida, a Proteobacterium. In Clostridium acetobutylicum, adjacent genes include separate proteins rather than a fusion protein [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
LRKYLFSGHFGLEKENQRVTSDGKLATTPHPAVFGNREYHPYIQTDFSESQLELITPVTDSIDVYRWLEA
IHNVSLRSEPEELLWPLSMPPILPAEEDIIEYATLDSPDDVKYREYLAKGYGKKKQMVSGIHYNFSFPEA
LIDGLYAEQHENESKRDFKNRLYLKVAKNFLRYRWLLIYLTGASPVYEADYFKTNSEEVLNLHVRSLRNS
NYGYKNKESLFVSYNSFEAYIESISNYVEAGKLSEKEFYNPVRLRGDKTVESLAKTGIEYLEIRSIDLNP
FEPNGISKDELIFIHLFMIKGLLSEDREECANQQVADGNENNALVALAHPAENCDNEEEGGLLELEKMSM
LQSLIPNDNHEQVEKQKEQLLHPEKTVAGVQAQSAQEGSYVELGLNQAKQYMEEAFERAYKLVGFEDMEL
STQWKLFDVIQKGKVEILDEAEQFLRLQHGDHIEYVKNANMTSKDNYVSPLIMENKVVTKKVLAEAGFRV
PFGDEFSSQALALEAFSLFENKAIVVKPKSTNYGLGITIFKNGFTLEDFQEALNIAFSEDSSVIIEEFLP
GTEYRFFVLNDKVEAVLLRVPANVTGDGIHTVRELVAEKNTDPLRGTDHRKPLEKITGPEETLMLKEQGL
TIDSIPKKEQIVYLRENSNVSTGGDSIDMTDEMDDSYKQIAIRIATAVGAAICGVDLIIPDETIPDTDKH
AIWGVIEANFNPAMHMHCFPYAGEKRRLTDKVIKFLF
>gnl|CDD|130503 TIGR01436, Glutamate--cysteine_ligase_chloroplastic, glutamate--cysteine ligase, plant type. This model represents one of two highly dissimilar forms of glutamate--cysteine ligase (gamma-glutamylcysteine synthetase), an enzyme of glutathione biosynthesis. The other type is modeled by TIGR01434. This type is found in plants (with a probable transit peptide), root nodule and other bacteria, but not E. coli and closely related species [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
PLTSRDDLIAYLAAGCKPKEQWRIGTEHEKFGFEKNTLRPMKYEQKGGIAELLNGIAERFGWQKVMEGDK
IIGLKQDKQSISLEPGGQFELSGAPLETIHETCDEINSHLYQVKEVAEEMGIGFLGLGFQPKWRREDIPL
MPKGRYDIMRNYMPKVGKLGLDMMLRTCTVQVNLDFSSEADMVRKFRASLALQPLATALFANSPFLEGKP
NGFLSYRSHIWTDTDPDRTGMLPFVFDDSFGFERYVDYALDVPMYFAYRKGKYIDCTGMTFRAFLAGKLP
ALPGELPTLNDWENHLSTIFPEVRLKRYLEMRGADGGPWRRLCALPAFWVGLLYDEDLLQAALDLTKDWS
PAEREMLRNEVPVTGLKTLFRDGQSLKHLGEDVLKLAKDGLERRGYKNAGGQDESRFLNPVGEVVETGQT
PAERLLEMYNGEWGQSVDPVFQELLY
>gnl|CDD|273623 TIGR01437, selA_rel, uncharacterized pyridoxal phosphate-dependent enzyme. This model describes a protein related to a number of pyridoxal phosphate-dependent enzymes, and in particular to selenocysteine synthase (SelA), which converts Ser to selenocysteine on its tRNA. While resembling SelA, this protein is found only in species that have a better candidate SelA or else lack the other genes (selB, selC, and selD) required for selenocysteine incorporation [Unknown function, Enzymes of unknown specificity]
IYEKYGLKKVINASGKMTILGVSTVSDEVADAQKRGAQNYFEIKELVNKTGEYIANLLGVEDAVIVSSAS
AGIAQSVAAVITRGNRYLVENLHDSKIEVNEVVLPKGHNVDYGAPVETMVRLGGGKVVEAGYANECSAEQ
LEAAITEKTAAILYIKSHHCVQKSMLSVEDAAQVAQEHNLPLIVDAAAEEDLQKYYRLGADLVIYSGAKA
IEGPTSGLVLGKKKYIEWVKLQSKGIGRAMKVGKENILGLTAALEQYLSTGKESGAEMVAKLTPFIEALN
TLKGVSASIVQDEAGRDIARAEIRFDESELGMTAADVVQALRQGEPAIYTRGYKANEGIIEIDPRSVTGG
QLDIIVERIREIV
>gnl|CDD|273624 TIGR01438, Thioredoxin_reductase_1_cytoplasmic, thioredoxin and glutathione reductase selenoprotein. This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity
YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQAL
KDSRNYGWKVEETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEK
IYSAERFLIATGERPRYPGIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMV
RSILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEEYDTVLLAIGRDAC
TRKLNLENVGVKINKKTGKIPADEEEQTNVPYIYAVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICD
YENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLEWTIPSRDNHNKCYAKLVCNKKENERV
VGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSGQDILQQGCCG
>gnl|CDD|273625 TIGR01439, Uncharacterized_protein_Mb2626, looped-hinge helix DNA binding domain, AbrB family. This DNA-binding domain family includes AbrB, a transition state regulator in Bacillus subtilis, whose DNA-binding domain structure in solution was determined by NMR. The domain binds DNA as a dimer in what is termed a looped-hinge helix fold. Some members of the family have two copies of the domain in tandem. The domain is found usually at the N-terminus of a small protein. This model excludes members of family TIGR02609 [Regulatory functions, DNA interactions]
VTVDKKGQIVIPKEIREKLGLKEGDRLEVIRVEDGEIILRPKR
>gnl|CDD|130507 TIGR01440, TIGR01440, TIGR01440 family protein. Members of this family are uncharacterized proteins of about 180 amino acids from the Bacillus/Clostridium group of Gram-positive bacteria, found in no more than one copy per genome [Hypothetical proteins, Conserved]
KQLTTVLEELKDASNLKKGDLFVIGCSTSEVIGGKIGTNSSMEVAETIVNALDVVLKKTGVTLAFQGCEH
INRALVMERSVAEPLGMEEVSVVPDLHAGGSLATYAFQHMKDPVEVEHITAPAGIDIGDTLIGMHVKHVQ
VPVRTSIRQIGQAHVTAAYSRPKLIGGERAHY
>gnl|CDD|273626 TIGR01441, Germination_protease, GPR endopeptidase. This model describes a tetrameric protease that makes the rate-limiting first cut in the small, acid-soluble spore proteins (SASP) of Bacillus subtilis and related species. The enzyme lacks clear homology to other known proteases. It processes its own amino end before becoming active to cleave SASPs [Protein fate, Degradation of proteins, peptides, and glycopeptides, Cellular processes, Sporulation and germination]
YSVRTDLAVEAREMYCEQTANGDKTVEGFRVDEKRIEGIKITTVDVLDKGAERIGKKKGRYLTLEIQGIR
LYDSEIQEKISKVFADEFSKFISKLKIDKDMTCLVVGLGNWNVTPDALGPKVVENLLVTRHLFKLIPESV
DEGIRPVSAVAPGVMGITGIETSDIIRGIIEQIKPDFVIAIDALAARKMERVNSTIQISDTGIHPGSGVG
NKRKELSKKTLGVPVIAVGVPTVVDAVTIASDTIDYVLKHFGREVSEDKPSRALAPAGMTFGERRELTDE
DLPPEEKRKTFLGLLGTLDEEEKRQLIYEVLNPLGHNLMVTPKEVDMFIEDMANVIASGLNIALHPAVEQ
SNIGKYVH
>gnl|CDD|273627 TIGR01442, Small_acid-soluble_spore_protein_gamma-type, small, acid-soluble spore protein, gamma-type. This model represents a family of small, glutamine and asparagine-rich peptides that store amino acids in the spores of Bacillus subtilis and related bacteria. Most members of the family have two copies of the spore protease (GPR) cleavage motif, typically EFASE in this family, separating three low-complexity repeats [Cellular processes, Sporulation and germination]
SGTSAQQVKKQNAQSSMNQFGTEFASETNVQEVKQQNAQSAAAKAQSSGAQSANASYGTEFASETDVQQV
KKQNAKAEAKKQQSS
>gnl|CDD|213622 TIGR01443, DNA-directed_RNA_polymerase_subunit, intein C-terminal splicing region. This model represents the well-conserved C-terminal region of a large number of inteins. It is based on interated search results, starting with a curated collection of intein N-terminal splicing regions from InBase, the New England Biolabs Intein Database, as presented on its web site. Inteins are regions encoded within proteins from which they remove themselves after translation in a self-splicing reaction, leaving the remainder of the coding region to form a complete, functional protein as if the intein were never there. Proteins with inteins include RecA, GyrA, ribonucleotide reductase, and others. Most inteins have a central region with putative endonuclease activity
YVYDLTVEGNHNFIANGIVVH
>gnl|CDD|273628 TIGR01444, 2-O-methyltransferase_NoeI, methyltransferase, FkbM family. Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548
VVIDVGANIGDTSLYFARKGAEGRVIAFEPLPDAYEILEENVKLNNLPNVVLLNAAVGDRDGELEFNVSD
DDTGNSSLLPTPDADRESEIEVEVVTLDDLVEEFGLDKVDLLKIDVEGAELEVLRGAAETLLEKRPVIVL
EVH
>gnl|CDD|273629 TIGR01445, Probable_translation_initiation_factor_IF-2, intein N-terminal splicing region. This model is based on interated search results, starting with a curated collection of intein N-terminal splicing regions from InBase, the New England Biolabs Intein Database, as presented on its web site. It is designed to recognize inteins but not the related region of the sonic hedgehog protein
LTGDTKVLTEDGETVKIGELVEKEKDEKEPIKVKVLSLDGGKIVKARPVVVWKRRAEGKLIRIKTENGRE
IKATPDHPFLT
>gnl|CDD|273630 TIGR01446, replication_protein, DnaD and phage-associated domain. This model represents the conserved domain of DnaD, part of Bacillus subtilis replication restart primosome, and of a number of phage-associated proteins. Members, both chromosomal or phage-associated, are found in the Bacillus/Clostridium group of Gram-positive bacteria [DNA metabolism, DNA replication, recombination, and repair, Mobile and extrachromosomal element functions, Prophage functions]
LYDFFEENFGRMLSPFEMEDLKYWLDEFGNDPELVKEALKEAVSNNKANYKYIDAILNNWKNNGIKTVED
VEA
>gnl|CDD|273631 TIGR01447, recD, exodeoxyribonuclease V, alpha subunit. This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model [DNA metabolism, DNA replication, recombination, and repair]
LKKLVQQGVLRPLDVAFAQFLQHLAQKSNEEVALFAAVASALLRRGHPCLDLEKAAKSPGLTGISEPDLG
EKLNFDWLAALPASVLVGLPGETAPPLVLCDGRLYLRRYWREEEKLAAKLRTLLEARKRTAPSAILENLF
PLLNEQNWRKTAVALALKSNFSLITGGPGTGKTTTVARLLLALVKQSPKQGKLRIALAAPTGKAAARLAE
SLRKAVKNLAAAEALIAALPSEAVTIHRLLGIKPDTKRFRHHERNPLPLDVLVVDEASMVDLPLMAKLLK
ALPPNTKLILLGDKNQLPSVEAGAVLGDLCELASIGKSILYALCKKINSKTRNPLSDNVCFLKTSHRFGK
DSGIGQLAKAINSGDIEAVLNNLRSGQLIEFEFLNSKEDAIERLKNLYVKYRTFLQKLAALSDAKEILET
FDRLRLLTALRDGPFGVLGLNRRIEQELQEKYFDPDEEGWYIGRPIMVTENDYTLGLFNGDIGVLLRDPD
GILTVWFHFADGSKAVLPSRLPNYETAFAMTVHKSQGSEFDHVILILPNGNSPVLTRELLYTGITRAKDQ
LSVWSDKETLNAAIKRKNKRLS
>gnl|CDD|273632 TIGR01448, recD_rel, helicase, putative, RecD/TraA family. This model describes a family similar to RecD, the exodeoxyribonuclease V alpha chain of TIGR01447. Members of this family, however, are not found in a context of RecB and RecC and are longer by about 200 amino acids at the amino end. Chlamydia muridarum has both a member of this family and a RecD [Unknown function, Enzymes of unknown specificity]
FSGTVEKILFENSTNFYVVLAVLRDETGEDTDATVVGVLPPLDEGDTYTFEGQWEEHAKYGYQFRAERME
LEAPTSKEGIVAYLSSRSIKGVGKKLAQRIVKTFGEAAFDVLDDDPEKLLEVPGISKANLEKFVSQWSQQ
GDERRLLAGLQGLGIGIKLAQRIYKFYQADTLDRVEKDPYLLAEDVKGIGFLTADQLAQALGIALNDPRR
ITAGLVYSLQQACTEEGHTYLPRNRFIKQVVHLLNVQPQERLLVPEAVELERLYLDEEPKLAAEDGRIYL
PSLFRAEKQIASHIRRLLATSPAIGAINDQEHIWEVEKKLRKGLSEEQKQALDTAIQHKVVILTGGPGTG
KTTITRAIIELAEELGGLLPVGLAAPTGRAAKRLGEVTGLTASTIHRLLGYGPDTFRHNHLEDPIDCDLL
IVDESSMMDTWLALSLLAALPDHARLLLVGDTDQLPSVGPGQVLKDLILSQAIPVTRLTKVYRQAAGSPI
ITLAHGILHGEAPAWGDFKFLNLTRSEPEGAARHIPLMVEKIVGMARVGGIPGADIQVLAPMYKGPLGID
ALNQHLQALLNPYQKGQGGIEIAEGEYRKGDRVMQTKNDYNNEIFNGDLGMIVKIEGAKQGKKDQVVVDF
DGNEVELTRAELFNLTLAYATSIHKSQGSEFPTVILPIHTAHMRMLYRNLLYTALTRAKKRVILVGSAEA
FDIAAARQGQARNTGLLERI
>gnl|CDD|130516 TIGR01449, Phosphoglycolate_phosphatase, 2-phosphoglycolate phosphatase, prokaryotic. PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In Ralstonia (Alcaligenes) eutropha and Rhodobacter sphaeroides, the PGP gene (CbbZ) is located on an operon along with other Calvin cycle enzymes including RubisCO. The only other pertinent experimental evidence concerns the gene from E. coli. The in vitro activity of the Ralstonia and Escherichia enzymes was determined with crude cell extracts of strains containing PGP on expression plasmids and compared to controls. In E. coli, however, there does not appear to be a functional Calvin cycle (RubisCO is absent), although the E. coli PGP gene (gph) is on the same operon (dam) with ribulose-5-phosphate-3-epimerase (rpe), a gene in the pentose-phosphate pathway (along with other, unrelated genes). The E. coli enzyme is not expressed under normal laboratory conditions; the pathway to which it belongs has not been determined. In fact, the possibility exists, although unlikely, that the E. coli enzyme and others within this equivalog have as their physiological substrate another, closely related molecule. The other seed chosen for this model, from Xylella fastidiosa has no experimental evidence, but is a plant pathogen and thus may obtain phosphoglycolate from its host. This model has been restricted to encompass only proteobacteria as no related PGP has been verified outside of this clade. Sequences from Aquifex aeolicus and Treponema pallidum fall between the trusted and noise cutoffs. Just below the noise cutoff is a gene which is part of the operon for the biosynthesis of the blue pigment, indigoidine, from Erwinia (Pectobacterium) chrysanthemi, a plant pathogen. It does not seem likely, considering the proposed biosynthetic mechanism, that the dephosphorylation of phosphoglycolate or a closely related compound is required. Possibly, this gene is fortuitously located in this operon, or has an indirect relationship to the necessity for the biosynthesis of this compound. Sequences from 11 species have been annotated as PGP or putative PGP but fall below the noise cutoff. None of these have experimental validation. This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolase enzymes (pfam00702) [Energy metabolism, Sugars]
VLFDLDGTLVDSAPDIAAAVNMALAALGLPPATLARVIGFIGNGVPVLMERVLAWAGQEPDAQRVAELRK
LFDRHYEEVAGELTSVFPGVEATLGALRAKGLRLGLVTNKPTPLARPLLELLGLAKYFSVLIGGDSLAQR
KPHPDPLLLAAERLGVAPQQMVYVGDSRVDIQAARAAGCPSVLLTYGYRYGEAIDLLPPDVLYDSLNELP
PLL
>gnl|CDD|273633 TIGR01450, recC, exodeoxyribonuclease V, gamma subunit. This model describes the gamma subunit of exodeoxyribonuclease V. Species containing this protein should also have the alpha (TIGR01447) and beta (TIGR00609) subunits. Candidates from Borrelia and from the Chlamydias differ dramatically and score between trusted and noise cutoffs [DNA metabolism, DNA replication, recombination, and repair]
FRLYHSNRLDVLAALLAALLRDPPLDDPFEPELILVQSPGMAQWLQMTLAEDLGVAANLEFPLPASFIWQ
MFVAVLPEIPEESAFNKEVMSWRLMALLPALLERPEFRTLRHYLADDSDLRKRYQLAERLADLFDQYLVY
RPDWLAAWEAGDDVEGPGDLQAWQAILWRALVAGVGADGQPTHRANLHQRFIERLRSGTTHPPGLPARLF
IFGISALPPTYLQALAALAQHCDVHLFLTNPCREYWGDIIDFKYLARLLTRHRGADPLLPLRQDLEEHAA
GHPLLASWGKLGRDFIYLLPELEQSQEIDAFLEATPDTLLHQLQADILHLEPRPVDAKLPSAPLDRSIQF
HACHSPLREVEVLHDRLLALLEEDPTLQPRDIIVMVPDIDSYAPYIEAVFGQAPVDARFLPYSLSDRRLR
QREPLLEAFIHLLDLPESRFTASEILALLDIPPVRARFGIDEDDLETLRRWVAEAGIRWGLDAEHRRELG
LPATDQHNTWRFGLERMLLGYAMGEDAGIWQGVLPYDDVGGLQAELAGRLAEFLERLSHWRRGLAQPRPL
EQWLERLRDLLDALFAVDDTTELALTQLEREWVDWQAEAAGAQFAQPLPLEVVRDHLAALLDDEPTSARF
LAGGVNFCTLVPMRSIPFRVVCLLGMNDGDYPRQQHPAGFDLMAREPRKGDRSRRDDDRYLFLEALLSAQ
EQLYISYVGRSIRDNSERPPSVLLGELIDYLVQTHYLDGDSARLAARLTEQHPLQPFSPQNFQPGGRLKP
FSYAREWLAAAQAAEGKRPDFDQPLPGRPAEPPAELPLADLIRFWAHPVKAFFQQRLGVSFPWEVETIED
SEPFELDGLSRYQINEQLLRFALQDDEERDLAQLAARLRARGLLPSGAFGRIFAKEQQQRARQLATAVLA
HRKQPPQSVEIDLDLQDGIRLSGWLGQLYPDGLVRWRYGKLNSPQLLRAWLEHLILCASGPPVESVLFCR
KVGRLHIALPPLVPAEQALAYLSELVELYRQGMRQPLPFPPKTALAWAEARYDAQDEKALKKAREAYEGN
FFRKGEGDAP
>gnl|CDD|273634 TIGR01451, unnamed_protein_product, conserved repeat domain. This model represents the conserved region of about 53 amino acids shared between regions, usually repeated, of proteins from a small number of phylogenetically distant prokaryotes. Examples include a 132-residue region found repeated in three of the five longest proteins of Bacillus anthracis, a 131-residue repeat in a cell wall-anchored protein of Enterococcus faecalis, and a 120-residue repeat in Methanobacterium thermoautotrophicum. A similar region is found in some Chlamydial outer membrane proteins
KTVDKTVATIGDTITYTITVTNNGNVPATNVVVTDILPAGTTFVSNSVTVNGV
>gnl|CDD|273635 TIGR01452, PGP_euk, phosphoglycolate/pyridoxal phosphate phosphatase family. PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In mammals, PGP is found in many tissues, notably in red blood cells where P-glycolate is and important activator of the hydrolysis of 2,3-bisphosphoglycerate, a major modifier of the oxygen affinity of hemoglobin. Pyridoxal phosphate (PLP, Vitamin B6) phosphatase is involved in the degradation of PLP in mammals and is widely distributed in human tissues including erythrocyes. The enzymes described here are members of the Haloacid dehalogenase superfamily of hydrolase enzymes (pfam00702). Unlike the bacterial PGP equivalog (TIGR01449), which is a member of class (subfamily) I, these enzymes are members of class (subfamily) II. These two families have almost certainly arisen from convergent evolution (although these two ancestors may themselves have diverged from a more distant HAD superfamily progenitor). The primary seed sequence for this model comes from Chlamydomonas reinhardtii, a photosynthetic alga. The enzyme has been purified and characterized and these data are fully consistent with the assignment of function as a PGPase involved in photorespiration. The second seed, from Homo sapiens chromosome 22 has been characterized as a pyridoxal phosphatase. Biochemical characterization of partially purified PGP's from various tissues including red blood cells have been performed while one gene for PGP has been localized to chromosome 16p13.3. The sequence used here maps to chromosome 22. There is indeed a related gene on chromosome 16 (and it is expressed, since EST's are found) which shows 46% identity. The chromosome 16 gene is not in evidence in nraa but translated from the genomic sequence. The third seed, from C. elegans, is only supported by sequence similarity. This model is limited to eukaryotic species including S. pombe and S. cerevisiae, although several archaea score between the trusted and noise cutoffs. This model is closely related to a family of bacterial sequences including the E. coli NagD and B. subtilus AraL genes which are characterized by the ability to hydrolyze para-nitrophenylphosphate (pNPPases or NPPases). The chlamydomonas PGPase d
TAQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGLAEQLFSS
ALCAARLLRQPPDAGKAVYVIGEEGLRAELDAAGIRLAGDPGEKKQDEADGFMYDIKLDERVGAVVVGYD
EHFSYVKLMEACAHLREPGCLFVATNRDPWHPLSDGSRTPGTGSLVAAIETASGRQPLVVGKPSPYMFNC
ITEKFSIDPARTLMVGDRLETDILFGHRCGMTTVLVLSGVSQLEEAQEYLMAGQDDLVPDYVVESLADL
>gnl|CDD|273636 TIGR01453, unnamed_protein_product_partial_mitochondrion, group I intron endonuclease. This model represents one subfamily of endonucleases containing the endo/excinuclease amino terminal domain, pfam01541 at its amino end. A distinct subfamily includes excinuclease abc subunit c (uvrC). Members of pfam01541 are often termed GIY-YIG endonucleases after conserved motifs near the amino end. This subfamily in this model is found in open reading frames of group I introns in both phage and mitochondria. The closely related endonucleases of phage T4: segA, segB, segC, segD and segE, score below the trusted cutoff for the family
KSGIYKITNNINGKIYVGSSVNLEKRLKEHLKLLKKGNRIKLQKALNKYGWSNFSFEILEYYCNKDDLIE
RETYYIKLLNPDAGYNILKIAGSSLGYKHSEETKAKMSKLFSGKKNNPWYGKTHSEETKAKISKNKLGEN
NPFFGKKHSEETKKKISEKEKGAKKVNVYDKNNGLLIIFDSIAEAARHLGISRGTISKYIKSGKLFKNRY
YITK
>gnl|CDD|130521 TIGR01454, AHBA_synth_RP, 3-amino-5-hydroxybenoic acid synthesis related protein. The enzymes in this equivalog are all located in the operons for the biosynthesis of 3-amino-5-hydroxybenoic acid (AHBA), which is a precursor of several antibiotics including ansatrienin, naphthomycin, rifamycin and mitomycin. The role that this enzyme plays in this biosynthesis has not been elucidated. This enzyme is a member of the Haloacid dehalogenase superfamily (pfam00702) of aspartate-nucleophile hydrolases. This enzyme is closely related to phosphoglycolate phosphatase (TIGR01449), but it is unclear what purpose a PGPase or PGPase-like activity would serve in these biosyntheses. This model is limited to the Gram positive Actinobacteria. The most closely related enzyme below the noise cutoff is IndB which is involved in the biosynthesis of Indigoidine in Pectobacterium (Erwinia) chrysanthemi, a gamma proteobacter. This enzyme is similarly related to PGP. In this case, too it is unclear what role would be be played by a PGPase activity
VVFDLDGVLVDSFAVMREAFAIAYREVVGDGPAPFEEYRRHLGRYFPDIMRIMGLPLEMEEPFVRESYRL
AGEVEVFPGVPELLAELRADGVGTAIATGKSGPRARSLLEALGLLPLFDHVIGSDEVPRPKPAPDIVREA
LRLLDVPPEDAVMVGDAVTDLASARAAGTATVAALWGEGDAGELLAARPDFLLRKPQSLLALCRS
>gnl|CDD|130522 TIGR01455, glmM, phosphoglucosamine mutase. This model describes GlmM, phosphoglucosamine mutase, also designated in MrsA and YhbF E. coli, UreC in Helicobacter pylori, and femR315 or FemD in Staphlococcus aureus. It converts glucosamine-6-phosphate to glucosamine-1-phosphate as part of the pathway toward UDP-N-acetylglucosamine for peptidoglycan and lipopolysaccharides [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
FGTDGVRGRAGQEPLTAELALLLGAAAGRVLRQGRDTAPRVVIGKDTRLSGYMLENALAAGLNSAGVDVL
LLGPLPTPAVAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEADPLPRPES
EGLGRVKRYPDAVGRYIEFLKSTLPRGLTLSGLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGLN
INDGCGSTHLDALQKAVREHGADLGIAFDGDADRVLAVDANGRIVDGDQILYIIARALKESGELAGNTVV
ATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEMRESGYNLGGEQSGHIILLDYSTTGDGIVSALQVLTI
MKKSGSTLSELAAEFVPYPQTLVNVRVADRKLAAAEAPAVKAAIEDAEAELGGTGRILLRPSGTEPLIRV
MVEAADEELVQQLADTLADVVSA
>gnl|CDD|200106 TIGR01456, CECR5, HAD-superfamily class IIA hydrolase, TIGR01456, CECR5. This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all eukaryotes. One sequence (GP|13344995) is called "Cat Eye Syndrome critical region protein 5" (CECR5). This gene has been cloned from a pericentromere region of human chromosome 22 believed to be the location of the gene or genes responsible for Cat Eye Syndrome. This is one of a number of candidate genes. The Schizosaccharomyces pombe sequence (EGAD|138276) is annotated as "phosphatidyl synthase," however this is due entirely to a C-terminal region of the protein (outside the region of similarity of this model) which is highly homologous to a family of CDP-alcohol phosphatidyltransferases. (Thus, the annotation of GP|4226073 from C. elegans as similar to phosphatidyl synthase, is a mistake as this gene does not contain the C-terminal portion). The physical connection of the phosphatidyl synthase and the HAD-superfamily hydrolase domain in S. pombe may, however, be an important clue to the substrate for the hydrolases in this equivalog
FGFAFDIDGVLFRGKKPIAGASDALRRLNRNQGQLKIPYIFLTNGGGFSERARAEEISSLLGVDVSPLQV
IQSHSPYKSLVNKYEKRILAVGTGSVRGVAEGYGFQNVVHQDEIVRYFRDIDPFSGMSDEQVMEYSRDIP
DLTTKRFDAVLVFNDPVDWAADIQIISDALNSEGLPGEKSGKPSIPIYFSNQDLLWANEYKLNRFGQGAF
RLLLERIYLELNGKPLQYYTLGKPTKLTYDFAEDVLIDWEKRLSGTKPSTSPFHALYMVGDNPASDIIGA
QNYGWFSCLVKTGVYNGGDDLKECKPTLIVNDVFDAVTKIL
>gnl|CDD|130524 TIGR01457, HAD-SF-IIA-hyp2, HAD-superfamily subfamily IIA hydrolase, TIGR01457. This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram positive (low-GC) bacteria. Sequences found in this model are annotated variously as related to NagD or 4-nitrophenyl phosphatase, and this hypothetical equivalog, of all of those within the Class IIA subfamily, is most closely related to the E. coli NagD enzyme and the PGP_euk equivalog (TIGR01452). However, there is presently no evidence that this hypothetical equivalog has the same function of either those [Unknown function, Enzymes of unknown specificity]
YKGYLIDLDGTMYNGTEKIEEACEFVRTLKKRGVPYLFVTNNSTRTPEQVADKLVSFDIPATEEQVFTTS
MATAQYIAQQKKDASVYVIGEEGLREAIKENGLTFGGENPDYVVVGLDRSITYEKFAVACLAIRNGARFI
STNGDIAIPTERGLLPGNGSLTSVLTVSTGVKPVFIGKPESIIMEQAMRVLGTDVEETLMVGDNYATDIM
AGINAGIDTLLVHTGVTKREHMTDDMEKPTHAIDSLAEW
>gnl|CDD|162372 TIGR01458, hypothetical_protein, HAD-superfamily subfamily IIA hydrolase, TIGR01458. This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published [Unknown function, Enzymes of unknown specificity]
VKGVLLDISGVLYISDAGGGTAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEV
FTPAPAARQLLEEKQLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPEHFSYQILNQAFRLLLDGAKPVL
IAIGKGRYYKRKDGLALDVGPFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDV
GGAQDCGMRGIQVRTGKYRPSDEEKINVPPDLTCDSLPHAVDLILQH
>gnl|CDD|130526 TIGR01459, HAD-SF-IIA-hyp4, HAD-superfamily class IIA hydrolase, TIGR01459. This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram negative and primarily alpha proteobacteria. Only one sequence hase been annotated as other than "hypothetical." That one, from Brucella, is annotated as related to NagD, but only by sequence similarity and should be treated with some skepticism. (See comments for Class IIA subfamily model)
IFDLINDYDVFLLDLWGVIIDGNHTYPGAVQNLNKIIAQGKPVYFVSNSPRNIFSLHKTLKSLGINADLP
EMIISSGEIAVQMILESKKRFDIRNGIIYLLGHLENDIINLMQCYTTDDENKANASLITIYRSENEKLDL
DEFDELFAPIVARKIPNICANPDRGINQHGIYRYGAGYYAELIKQLGGKVIYSGKPYPAIFHKALKECSN
IPKNRMLMVGDSFYTDILGANRLGIDTALVLT
>gnl|CDD|273637 TIGR01460, Protein_nagD., Haloacid Dehalogenase Superfamily Class (subfamily) IIA. This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant [Unknown function, Enzymes of unknown specificity]
FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSLLGVDVSPDQIITSGSV
TKDLLRQRFEGEKVYVIGVGELRESLEGLGFRNDFFDDIDHLAIEKIPAAVIVGEPSDFSYDELAKAAYL
LAEGDVPFIAANRDDLVRLGDGRFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRDV
MVGDNLRTDILGAKNAGFDTLLVLTG
>gnl|CDD|130528 TIGR01461, greB, transcription elongation factor GreB. The GreA and GreB transcription elongation factors enable to continuation of RNA transcription past template-encoded arresting sites. Among the Proteobacteria, distinct clades of GreA and GreB are found. GreB differs functionally in that it releases larger oligonucleotides. This model describes proteobacterial GreB [Transcription, Transcription factors]
KTPLITPEGYEKLKQELNYLWREERPEVTQKVTWAASLGDRSENADYQYGKKRLREIDRRVRFLTKRLEN
LKVVDYSPQQEGKVFFGAWVELENDDGVTHRFRIVGYDEIDGRKNYISIDSPLARALLKKEVGDEVVVNT
PAGEASWYVNAIEYVK
>gnl|CDD|273638 TIGR01462, Transcription_elongation_factor_GreA, transcription elongation factor GreA. The GreA and GreB transcription elongation factors enable to continuation of RNA transcription past template-encoded arresting sites. Among the Proteobacteria, distinct clades of GreA and GreB are found. GreA differs functionally in that it releases smaller oligonucleotides. Because members of the family outside the Proteobacteria resemble GreA more closely than GreB, the GreB clade (TIGR01461) forms a plausible outgroup and the remainder of the GreA/B family, included in this model, is designated GreA. In the Chlamydias and some spirochetes, the region described by this model is found as the C-terminal region of a much larger protein [Transcription, Transcription factors]
PLTQEGYEKLKEELEYLKTVKRPEISEEIAEAREHGDLSENAEYHAAKEEQGFNEGRIAELEDLLANAQV
IDDSKLSTDVVGFGSTVTIKDLDTGEEETYTIVGSWEADPKEGKISIDSPLGKALIGKKVGDSVEVQTPK
GEKEYEILKIE
>gnl|CDD|273639 TIGR01463, methylthiol:coenzyme_M_methyltransferase, methyltransferase, MtaA/CmuA family. This subfamily is closely related to, yet is distinct from, uroporphyrinogen decarboxylase (EC 4.1.1.37). It includes two isozymes from Methanosarcina barkeri of methylcobalamin--coenzyme M methyltransferase. It also includes a chloromethane utilization protein, CmuA, which transfers the methyl group of chloromethane to a corrinoid protein
SEMTPKERLLAALTGQPVDKVPPCSPTQTGTVELMDECGATWPEAHTDPELMAKLAIAAYELSGLEAVRP
PFDLTVEAEAMGCEIDMGTKNQPSVTKHPYPKDLADARVPANLLKRGRIPVVLEAIKILREKYGPDVPII
GGMEGPFTVASDLIGVKSFMKWSITDPDLAEAALDIATDFVIAYAKAMVEAGADVIAIADPVASPDLISP
ETYREFLLPYQKKFAAEINSVTVLHICGNTNPILSDMADCGFEGFSVDEKPGMAHGKRVIGGRASLVGNL
SPPFTLLNGTPEKIKAEAKEVLEGGIDILAPGCGIAPMTPLENLKAMVEACKEIYY
>gnl|CDD|273640 TIGR01464, Uroporphyrinogen_decarboxylase, uroporphyrinogen decarboxylase. This model represents uroporphyrinogen decarboxylase (HemE), which converts uroporphyrinogen III to coproporphyrinogen III. This step takes the pathway toward protoporphyrin IX, a common precursor of both heme and chlorophyll, rather than toward precorrin 2 and its products [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
LFLRAAKGEVVDRPPVWFMRQAGRYLPEYRELRAKAGDFLELCRNPDLAVEVTLQPIRRFGVDAAIIFSD
ILVPLQALGLDVEFVEGKGPVISNPIRTAEDVERLKEFDPESELSYVYEAIKLLREELPGEVPLIGFAGA
PWTLASYMIEGGGSKDFAKAKRFMYQEPEALHALLNKLTDATIEYLVEQVKAGAQAVQIFDSWAGALSPE
DFEEFVLPYLAKIIEEVKARLPNVPVILFAKGAGHLLEELAETGADVVGLDWSVDLKEARKRVGKGKAIQ
GNLDPAVLYAPEEALEEKVEKILEAFGGKSGYIFNLGHGILPDTPPENVKALVEYVHS
>gnl|CDD|200107 TIGR01465, Precorrin-4_C11-methyltransferase, precorrin-4 C11-methyltransferase. This model represents precorrin-4 C11-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-3B C17-methyltransferase, EC 2.1.1.131). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
VYFIGAGPGDPDLITVKGRKLIESADVILYAGSLVPPELLAHCRPGAEVVNSAGMSLEEIVDIMSDAHRE
GKDVARLHSGDPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGRT
PMPEGEKLADLAKHGATMAIFLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLV
REEGIYRTTLILVGPALDPRIGKRSKLYDPDFSHSFR
>gnl|CDD|273641 TIGR01466, Probable_cobalt-factor_III_C17-methyltransferase, precorrin-3B C17-methyltransferase. This model represents precorrin-3B C17-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-4 C11-methyltransferase, EC 2.1.1.133). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. Members of this family may appear as fusion proteins with other enzymes of cobalamin biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
LYVVGIGPGAEELMTPEAKEALAEADVIVGYKTYLDLIEDLIPGKEVVTSGMREEIARAELAIELAAEGR
TVALVSSGDPGIYGMAALVFEALEKKGAEVDIEVIPGITAASAAASLLGAPLGHDFCVISLSDLLTPWPE
IEKRLRAAAEADFVIAIYNPRSKRRPEQFRRAMEILLEHRKPDTPVGIVRNAGREGEEVEITTLAELDEE
LIDMLTTVIIGNSETYVIDGWMITPRGYA
>gnl|CDD|273642 TIGR01467, Probable_cobalt-precorrin-2_C20-methyltransferase, precorrin-2 C(20)-methyltransferase. This model represents precorrin-2 C(20)-methyltransferase, one of several closely related S-adenosylmethionine-dependent methyltransferases involved in cobalamin (vitamin B12) biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
GKLYGVGVGPGDPELITVKALEALRSADVIAVPASKKGRESLARKIVEDYLKPNDTRILELVFPMTKDRD
ELEKAWDEAAEAVAAELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAGLP
LVEGDESLAILPATAGEAELEKALAEFDTVVLMKVGRNLPQIKEALAKLGRLDAAVVVERATMPDEKIVD
LVREAIDDALPYFSTILVRR
>gnl|CDD|273643 TIGR01469, Uroporphyrinogen-III_C-methyltransferase, uroporphyrin-III C-methyltransferase. This model represents enzymes, or enzyme domains, with uroporphyrin-III C-methyltransferase activity. This enzyme catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). Cobalamin contains cobalt while siroheme contains iron. Siroheme is a cofactor for nitrite and sulfite reductases and therefore plays a role in cysteine biosynthesis; many members of this family are CysG, siroheme synthase, with an additional N-terminal domain and with additional oxidation and iron insertion activities [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
KVYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLL
VELAREGKKVVRLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFV
TGHEADDKALEVDWEALAKGAGTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLG
DLAEKAAEANLKSPALIVIGEVVALR
>gnl|CDD|130536 TIGR01470, siroheme_synthase, siroheme synthase, N-terminal domain. This model represents a subfamily of CysG N-terminal region-related sequences. All sequences in the seed alignment for this model are N-terminal regions of known or predicted siroheme synthases. The C-terminal region of each is uroporphyrin-III C-methyltransferase (EC 2.1.1.107), which catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). The region represented by this model completes the process of oxidation and iron insertion to yield siroheme. Siroheme is a cofactor for nitrite and sulfite reductases, so siroheme synthase is CysG of cysteine biosynthesis in some organisms [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
LPVFANLEGRAVLVVGGGDVALRKARLLLKAGAQLRVIAEELESELTLLAEQGGITWLARCFDADILEGA
FLVIAATDDEELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGGAAPVLARLLRERI
ETLLPPSLGDLATLAATWRDAVKKRLPNGAARRRFWEKFFDGAFAERVLAGREEQAERVLATRLA
>gnl|CDD|273644 TIGR01472, GDP-mannose_46_dehydratase_1, GDP-mannose 4,6-dehydratase. Alternate name: GDP-D-mannose dehydratase. This enzyme converts GDP-mannose to GDP-4-dehydro-6-deoxy-D-mannose, the first of three steps for the conversion of GDP-mannose to GDP-fucose in animals, plants, and bacteria. In bacteria, GDP-L-fucose acts as a precursor of surface antigens such as the extracellular polysaccharide colanic acid of E. coli. Excluded from this model are members of the clade that score poorly because of highly dervied (phylogenetically long-branch) sequences, e.g. Aneurinibacillus thermoaerophilus Gmd, described as a bifunctional GDP-mannose 4,6-dehydratase/GDP-6-deoxy-D-lyxo-4-hexulose reductase (PUBMED:11096116) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
KIALITGITGQDGSYLAEFLLEKGYEVHGLIRRSSSFNTQRIEHIYEDPHNVNKARMKLHYGDLTDSSNL
RRIIDEIKPTEIYNLAAQSHVKVSFEIPEYTADVDGIGTLRLLEAVRTLGLIKSVKFYQASTSELYGKVQ
EIPQNETTPFYPRSPYAAAKLYAHWITVNYREAYGLFAVNGILFNHESPRRGENFVTRKITRAAAKIKLG
LQEKLYLGNLDAKRDWGHAKDYVEAMWLMLQQDKPDDYVIATGETHSVREFVEVSFEYIGKTLNWKDKGI
NEVGRCKETGKVHVEIDPRYFRPTEVDLLLGDATKAKEKLGWKPEVSFEKLVKEMVEEDLELA
>gnl|CDD|273645 TIGR01473, Protoheme_IX_farnesyltransferase, protoheme IX farnesyltransferase. This model describes protoheme IX farnesyltransferase, also called heme O synthase, an enzyme that creates an intermediate in the biosynthesis of heme A. Prior to the description of its enzymatic function, this protein was often called a cytochrome o ubiquinol oxidase assembly factor [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
KDYLQLTKPRIISLLLITAFAGMWLAPGGALVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTR
NRPLVTGRISPREALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFA
GAVPPLIGWAAVTGSISLGAWLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALY
TAALLPVSLLLAFLGGTGWLYLIVATLLGALFLYLAFKFYRDPTDRKKARKLFKFSLIYLALLFVALLID
>gnl|CDD|130539 TIGR01474, 4-hydroxybenzoate_octaprenyltransferase, 4-hydroxybenzoate polyprenyl transferase, proteobacterial. This model represents a family of integral membrane proteins that condenses para-hydroxybenzoate with any of several polyprenyldiphosphates. Heterologous expression studies suggest that for, many but not all members, the activity seen (e.g. octaprenyltransferase in E. coli) reflects available host isoprenyl pools rather than enzyme specificity. A fairly deep split by both clustering (UPGMA) and phylogenetics (NJ tree) separates this group (mostly Proteobacterial and mitochondrial), with several characterized members, from another group (mostly archaeal and Gram-positive bacterial) lacking characterized members [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
LLPYAKLMRADKPIGTLLLLWPCLWSLLLAAQAGGIPPLYLLGLFTVGAILMRGAGCVINDIWDRDFDPQ
VERTKSRPLASGAVSVRQAILFLLVQLLVALGVLLQLNPLTILLGVASLALVATYPFMKRITYWPQLVLG
LAFGWGALMGWAAVTGDLSTAAWVLYLANILWTLGYDTIYAMQDKEDDIKIGVKSTALRFGDNTKPWLGG
LYALMILLLALAGLIAGLGPVYYLGLAAAALLLIRQIATLDIRDPENCLKLFKANNYVGLLLFAGIALGW
L
>gnl|CDD|273646 TIGR01475, ubiA_other, putative 4-hydroxybenzoate polyprenyltransferase. A fairly deep split separates this polyprenyltransferase subfamily from the set of mitochondrial and proteobacterial 4-hydroxybenzoate polyprenyltransferases, described in TIGR01474. Protoheme IX farnesyltransferase (heme O synthase) (TIGR01473) is more distantly related. Because no species appears to have both this protein and a member of TIGR01474, it is likely that this model represents 4-hydroxybenzoate polyprenyltransferase, a critical enzyme of ubiquinone biosynthesis, in the Archaea, Gram-positive bacteria, Aquifex aeolicus, the Chlamydias, etc [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
KFKDILELIKFEHTVFALPFAYAGALLAAKGLPGLKTLILILIAAVSARTAAMAFNRIIDRAIDARNPRT
KNRPLVSGLISKKEARTMIILSLALFLSASYFLNPLAFILSPLVLLVLIIYPYTKRFTFLCHYVLGSTYG
LAPLAGWVAVIGTISFFLVAWLLGIGVGFWIAGFDLIYAIQDYEFDRKNGLHSIPARFGIKAALKIASLS
HVITFILLLLVGFYVGNGYIALLALILIGLILAYEHYIVDPGDQSKIQRAFFYANGFLSITFLIGVIIDV
LL
>gnl|CDD|130541 TIGR01476, Bacteriochlorophyll_synthase_33_kDa_chain, bacteriochlorophyll/chlorophyll synthetase. This model describes a subfamily of a large family of polyprenyltransferases (pfam01040) that also includes 4-hydroxybenzoate octaprenyltransferase and protoheme IX farnesyltransferase (heme O synthase). Members of this family are found exclusively in photosynthetic organisms, including a single copy in Arabidopsis thaliana [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
RAHIELMKPVTWIPPIWACFCGALASGYERGFPEHWWLMLLGMLMAGPLGTGFSQSINDYFDRDVDAINE
PQRPIPSGIISLREVRWNWLVLTVAGLLVALVLGNWLIVLFTVVGIVLAVIYSMPPIKLKRNGWLGPPAV
GLSYEGLPWMAGHAIFAPLTWQSVVVALIYSLGAHGIMTLNDFKSVEGDRQLGLRSLPVMIGVKRAAIVA
VTTINVFQAMVIGLLLIWGQPWVATIVFLLLVAQIYNQIKLFLRDPQQNYVRYNATANPFYVLGMLAAGF
ALG
>gnl|CDD|273647 TIGR01477, Plasmodium_falciparum_chromosome_2_section, variant surface antigen, rifin family. This model represents the rifin branch of the rifin/stevor family (pfam02009) of predicted variant surface antigens as found in Plasmodium falciparum. This model is based on a set of rifin sequences kindly provided by Matt Berriman from the Sanger Center. This is a global model and assesses a penalty for incomplete sequence. Additional fragmentary sequences may be found with the fragment model and a cutoff of 20 bits
MKLHYINILLFSLPLNILVNSQRNHKNTPHHTSNTTPTKTSRSLCECELYSSNYDNDPEMKSVMEQFDRQ
TSQRFEEYDERMQEKRQKCKEQCDKEIQKIILKDKLEKELTEKFSTLQTDIQTDAIPTCVCEKSLADKVE
KGCLRCGCGLGGGVAPGVGLLGGIAVNVVGWKQAALAAAAAAAIAAGIKAGINVVIEGLKKILGLSTLFG
KKLKQIINASNYTNPSLLSDAIYKEYNEMCGVVSSNKGLFCNTMERSINSPNQERTVETIVANAEDAAKA
AAKAATKATTATATKATTALVEATTTNYYTPIIASIIAILIIVLIMVIIYLILRYRRKKKMKKKLQYIKL
LNE
>gnl|CDD|130543 TIGR01478, Plasmodium_falciparum, variant surface antigen, stevor family. This model represents the stevor branch of the rifin/stevor family (pfam02009) of predicted variant surface antigens as found in Plasmodium falciparum. This model is based on a set of stevor sequences kindly provided by Matt Berriman from the Sanger Center. This is a global model and assesses a penalty for incomplete sequence. Additional fragmentary sequences may be found with the fragment model and a cutoff of 8 bits
MLLFTFLFNALLLSQNVNCHNKKYNVSYIQNNTQMTSTKSRLLAEIQRPKNPHYHNDPELKEIIDKLNEE
AIKKYQETHDPYEQLQELVEKNRTKSTGGNGAEPMSTIEKELLEKYEEMFGDESHIMLKSGMYTNDDDKL
KDKSCECTNQKIELLSSTKVHDNYLKNLKKGCTAGVGTCALSSALLGNIGIAAAKTAAIEVITGSYSLDI
ANKCTKALAGINFFFSSSIESAGKTGVGIFYGASDDAERAASAATSTFLPYGIAALVLIILTVVLIILYI
WLYRRRKKSWKHECK
>gnl|CDD|273648 TIGR01479, Mannose-1-phosphate_guanylyltransferase, mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREI
GKLASNIILEPVGRNTAPAIALAALLAARRNGEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVT
FGIVPTHPETGYGYIRRGAPLAGEDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKK
HAPDIYEACEAAVEASEPDLDFIRLDKEAFEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEI
SDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVGVEDLVVVETKDAVLVAHKDRVQDVKKIVEQLKADG
RTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHHHRAEHWIVVSGTARVTIGDETLLLT
ENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR
>gnl|CDD|273649 TIGR01480, unnamed_protein_product, copper-resistance protein, CopA family. This model represents the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is observed for a large number of periplasmic proteins that cross the inner membrane with metal-containing cofactors already bound. The combination of copper-binding sites and TAT translocation motif suggests a mechansism of resistance by packaging and export [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds]
SVMTAFDRRRFLQGLASGGAAAGLGLWATAAWAERSPLPESVLSGTEFDLTIGETMVNFTGRARPAITVN
GSIPGPLLRWREGDTVRLRVTNTLPEDTSIHWHGILLPFQMDGVPGVSFAGIAPGETFTYRFPVRQSGTY
WYHSHSGFQEQAGLYGPLIIDPAEPDPVRADREHVVLLSDWTDLDPAALFRKLKVMAGHDNYYKRTVADF
FRDVRNDGLKQTLADRKMWGQMRMTPTDLADVNGSTYTYLMNGTTPAGNWTGLFRPGEKVRLRFINGSAM
TYFDVRIPGLKLTVVAVDGQYVHPVSVDEFRIAPAETFDVIVEPTGDDAFTIFAQDSDRTGYARGTLAVR
LGLTAPVPALDPRPLLTMKDMGMGGMHHGMDHSKMSMGGMPGMDMSMRAQSNAPMDHSQMAMDASPKHPA
SEPLNPLVDMIVDMPMDRMDDPGIGLRDNGRRVLTYADLHSLFPPPDGRAPGREIELHLTGNMERFAWSF
DGEAFGLKTPLRFNYGERLRVVLVNDTMMAHPIHLHGMWSELEDGQGEFQVRKHTVDVPPGGKRSFRVTA
DALGRWAYHCHMLLHMEAGMFREVTVR
>gnl|CDD|130546 TIGR01481, catabolite_control_protein_A, catabolite control protein A. Catabolite control protein A is a LacI family global transcriptional regulator found in Gram-positive bacteria. CcpA is involved in repressing carbohydrate utilization genes [ex: alpha-amylase (amyE), acetyl-coenzyme A synthase (acsA)] and in activating genes involved in transporting excess carbon from the cell [ex: acetate kinase (ackA), alpha-acetolactate synthase (alsS)]. Additionally, disruption of CcpA in Bacillus megaterium, Staphylococcus xylosus, Lactobacillus casei and Lactocacillus pentosus also decreases growth rate, which suggests CcpA is involved in the regulation of other metabolic pathways [Regulatory functions, DNA interactions]
TVTIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIKRLDYRPNAVARGLASKRTTTVGVIIPDIS
NIYYAELARGIEDIATMYKYNIILSNSDEDPEKEVQVLNTLLSKQVDGIIFMGGTITEKLREEFSRSPVP
VVLAGTVDKENELPSVNIDYKQATKEAVGELIAKGHKSIAFVGGPLSDSINGEDRLEGYKEALNKAGIQF
GEDLVCEGKYSYDAGYKAFAELKGSLPTAVFVASDEMAAGILNAAMDAGIKVPEDLEVITSNNTRLTEMV
RPQLSTIIQPLYDIGAVAMRLLTKYMNDEELEEKTVVLPHGIELRGSTK
>gnl|CDD|273650 TIGR01482, Haloacid_dehalogenase-like_hydrolase_putative, sucrose-phosphate phosphatase subfamily. This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP
IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIGTPDPVIAENGGEISYNE
GLDDIFLAYLEEEWFLDIVIAKTFPFSRLKVQYPRRASLVKMRYGIDVDTVREIIKELGLNLVAVDSGFD
IHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEWADYVTESPYG
EGGAEAIGEILQAIG
>gnl|CDD|273651 TIGR01484, Putative_mannosyl-3-phosphoglycerate_phosphatase, HAD-superfamily hydrolase, subfamily IIB. This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear [Unknown function, Enzymes of unknown specificity]
LLFFDLDGTLLDPNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFY
PGEILYIEPSDVFEEILGIKFEEIGAELKSLSEHYVGTFIEDKAIAVAIHYVGAELGQELDSKMRERLEK
IGRNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV
>gnl|CDD|130549 TIGR01485, putative_sucrose-phosphate_phosphatase, sucrose-6F-phosphate phosphohydrolase. This model describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). SPP is a member of the Class IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. SPP catalyzes the final step in the biosynthesis of sucrose, a critically important molecule for plants. Sucrose phosphate synthase (SPS), the prior step in the biosynthesis of sucrose, contains a domain which exhibits considerable similarity to SPP albeit without conservation of the catalytic residues. The catalytic machinery of the synthase resides in another domain. It seems likely that the phosphatase-like domain is involved in substrate binding, possibly binding both substrates in a "product-like" orientation prior to ligation by the synthase catalytic domain
RLLLVSDLDNTLVDHTDGDNQALLRLNALLEDHRGEDSLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSV
GSEIYYGGAEVPDQHWAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRPHKVSFFLDPEAAPEVIKQLTE
MLKETGLDVKLIYSSGKDLDILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIGSVRGVIVS
NAQEELLQWYDENAKDKIYHASERCAGGIIEAIAHFDLL
>gnl|CDD|130550 TIGR01486, Mannosyl-3-phosphoglycerate_phosphatase, mannosyl-3-phosphoglycerate phosphatase family. This small group of proteins is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. Several members of this family from thermophiles (and from Dehalococcoides ethenogenes) are now known to act as mannosyl-3-phosphoglycerate (MPG) phosphatase. In these cases, the enzyme acts after MPG synthase to make the compatible solute mannosylglycerate. We propose that other mesophilic members of this family do not act as mannosyl-3-phosphoglycerate phosphatase. A member of this family is found in Escherichia coli, which appears to lack MPG synthase. Mannosylglycerate is imported in E. coli by phosphoenolpyruvate-dependent transporter (), but it appears the phosphorylation is not on the glycerate moiety, that the phosphorylated import is degraded by an alpha-mannosidase from an adjacent gene, and that E. coli would have no pathway to obtain MPG
WIFTDLDGTLLDPHGYDWGPAKEVLERLQELGIPVIPCTSKTAAEVEYLRKELGLEDPFIVENGGAIYGP
RGWRPEPEYPVIALGIPYEKIRARLRELSEELGFKFRGLGDLTDEEIAELTGLSRELARLAQRREYSETI
LWSEERRERFTEALVAVGLEVTHGGRFYHVLGAGSDKGKAVNALKAFYNQPGGAIKVVGLGDSPNDLPLL
EVVDLAVVVPGPNGPNVSLKPGDPGSFLLTPAPGPEGWREALEHLL
>gnl|CDD|273652 TIGR01487, Pglycolate_arch, phosphoglycolate phosphatase, TA0175-type. This group of Archaeal sequences, now known to be phosphoglycolate phosphatases, is most closely related to the sucrose-phosphate phosphatases from plants and cyanobacteria (TIGR01485). Together, these two models comprise a subfamily model (TIGR01482). TIGR01482, in turn, is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases
IKLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGPVVAENGGVIF
YNKEDIFLANMEEEWFLDEEKKKRFPRDRLSNEYPRASLVIMREGKDVDEVREIIKERGLNLVASGFAIH
IMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLKEIADYVTSNPYGEG
VVEVL
>gnl|CDD|273653 TIGR01488, Phosphoserine_phosphatase, Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like. This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences [Unknown function, Enzymes of unknown specificity]
LAIFDFDGTLTRQDSLIDLLAKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHRSRSEEVAKEFLAR
QVALRPGARELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDNGLLTGPIEGQVNPEG
ECKGKVLKELLEESKITLKKIIAVGDSVNDLPMLKLA
>gnl|CDD|213629 TIGR01489, Phosphoserine_phosphatase, 2,3-diketo-5-methylthio-1-phosphopentane phosphatase. This phosphatase is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. With the exception of OMNI|NTL01BS01361 from B. subtilis and GP|15024582 from Clostridium acetabutylicum, the members of this group are all eukaryotic, spanning metazoa, plants and fungi. The B. subtilus gene (YkrX, renamed MtnX) is part of an operon for the conversion of methylthioribose (MTR) to methionine. It works with the enolase MtnW, a RuBisCO homolog. The combination of MtnW and MtnX achieves the same overall reaction as the enolase-phosphatase MtnC. The function of MtnX was shown by Ashida, et al. (2003) to be 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, rather than 2,3-diketo-5-methylthio-1-phosphopentane phosphatase as proposed earlier. See the Genome Property for methionine salvage for more details. In eukaryotes, methionine salvage from methylthioadenosine also occurs. It seems reasonable that members of this family in eukaryotes fulfill a similar role as in Bacillus. A more specific, equivalog-level model is TIGR03333. Note that SP|P53981 from S. cerevisiae, a member of this family, is annotated as a "probable membrane protein" due to a predicted transmembrane helix. The region in question contains the second of the three conserved HAD superfamily catalytic motifs and thus, considering the fold of the HAD catalytic domain, is unlikely to be a transmembrane region in fact [Central intermediary metabolism, Other]
KVVVVSDFDGTITLNDSDDWITDKFGPPEANRLLDGVLSKTLSIKFMDRRMKGLLPSGLKEDEILEVLKS
APIDPGFKEFIAFIKEHGIDFIVISDGNDFFIDPVLEGIGEKDVFIEIYSNPASFDNDGRHIVWPHHCHG
CCSCPCGCCKGKVIHKLSEPKYQHIIYIGDGVTDVCPAKLSDVVFAKE
>gnl|CDD|273654 TIGR01490, Uncharacterized_protein_Rv3661/MT3761, HAD-superfamily subfamily IB hydrolase, TIGR01490. This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog [Unknown function, Enzymes of unknown specificity]
LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEFFLNRGLDYMAYYRAFALDALAGLLEE
DVRAIVEEFVNQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEDG
IYTGNIDGNNCKGEGKVHALAELLAEEQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL
>gnl|CDD|273655 TIGR01491, HAD-SF-IB-PSPlk, HAD-superfamily, subfamily-IB PSPase-like hydrolase, archaeal. This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all from archaeal species. The phylogenetically closest group of sequences to these are phosphoserine phosphatases (TIGR00338). There are no known archaeal phosphoserine phosphatases, and no archaea fall within TIGR00338. It is likely, then, that this model represents the archaeal branch of the PSPase equivalog
ERMIKLIIFDLDGTLTDVMSSWEYLHRRLETCGLAKKNAELFFSGRISYEEWARLDASLWKRRSGRLRRE
EVEEIFKEISLRDYAEELVRWLKEKGLKTAIVSGGIMCLAKKVAEKLNPDYVYSNELVFDEKGFIQPDGI
VRVTFDNKGEAVERLKRELNPSLTETVAVGDSKNDLPMFEVADISISLGDEGHADYLAKDL
>gnl|CDD|130556 TIGR01492, hypothetical_protein, Plasmodium falciparum CPW-WPC domain. This model represents a domain of about 61 residues in length with six well-conserved cysteine residues and six well-conserved aromatic sites. The domain can be found in tandem repeats, and is known so far only in Plasmodium falciparum. It is named for motifs of CPxxW and (less well conserved) WPC
KCEENYSSPCPENWIQKNDKYGCIAPDNYKGPCERKKIFDNMNKKEKEDYSKKCNVKWPCKN
>gnl|CDD|130557 TIGR01493, HAD-SF-IA-v2, Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid dehalogenase. This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called 'capping domain', or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 2 (this model) is distinctive of the type II haloacid dehalogenases, and nearly all of the sequences are also part of the HAD, type II equivalog model (TIGR01428). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model
AMVFDVYGTLVDVHGGVRACLAAIAPEGGAFSDLWRAKQQEYSWRRSLMGDRRAFPEDTVRALRYIADRL
GLDAEPKYGERLRDAYKNLPPWPDSAAALARVAILSNASHWAFDQFAQQAGLPWYFDRAFSVDTVRAYKP
DPVVYELVFDTVGLPPDRVLMVAAHQWDLIGARKF
>gnl|CDD|273656 TIGR01494, ATPase_P-type, ATPase, P-type (transporting), HAD superfamily, subfamily IC. The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. Another common name for these enzymes is the E1-E2 ATPases based on the two isolable conformations: E1 (unphosphorylated) and E2 (phosphorylated). Generally, P-type ATPases consist of only a single subunit encompassing the ATPase and ion translocation pathway, however, in the case of the potassium (TIGR01497) and sodium/potassium (TIGR01106) varieties, these functions are split between two subunits. Additional small regulatory or stabilizing subunits may also exist in some forms. P-type ATPases are nearly ubiquitous in life and are found in numerous copies in higher organisms (at least 45 in Arabidopsis thaliana, for instance). Phylogenetic analyses have revealed that the P-type ATPase subfamily is divided up into groups based on substrate specificities and this is represented in the various subfamily and equivalog models that have been made: IA (K+) TIGR01497, IB (heavy metals) TIGR01525, IIA1 (SERCA-type Ca++) TIGR01116, IIA2 (PMR1-type Ca++) TIGR01522, IIB (PMCA-type Ca++) TIGR01517, IIC (Na+/K+, H+/K+ antiporters) TIGR01106, IID (fungal-type Na+ and K+) TIGR01523, IIIA (H+) TIGR01647, IIIB (Mg++) TIGR01524, IV (phospholipid, flippase) TIGR01652 and V (unknown specificity) TIGR01657. The crystal structure of one calcium-pumping ATPase and an analysis of the fold of the catalytic domain of the P-type ATPases have been published. These reveal that the catalytic core of these enzymes is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily
FILFLVLLFVLLEVKQKLKAEDALRSLKDSLVNTATVLVLRNGWKEISSKDLVPGDVVLVKSGDTVPADG
VLLSGSAFVDESSLTGESLPVLKTALPDGDAVFAGTINFGGTLIVKVTATGILTTVGKIAVVVYTGFSTK
TPLQSKADKFENFIFILFLLLLALAVFLLLPIGGWDGNSIYKAILRALAVLVIAIPCALPLAVSVALAVG
DARMAKKGILVKNLNALEELGKVDVICFDKTGTLTTNKMTLQKVIIIGGVEEASLALALLAASLEYLSGH
PLERAIVKSAEGVIKSDEINVEYKILDVFPFSSVLKRMGVIVEGANGSDLLFVKGAPEFVLERCNNENDY
DEKVDEYARQGLRVLAFASKKLPDDLEFLGLLTFEDPLRPDAKETIEALRKAGIKVVMLTGDNVLTAKAI
AKELGIDVFARVKPEEKAAIVEALQEKGRTVAMTGDGVNDAPALKKADVGIAMGSGDVAKAAADIVLLDD
DLSTIVEAVKEGRKTFSNIKKNIFWAIAYNLILIPLALLLIVIILLPPLLAALAL
>gnl|CDD|130559 TIGR01495, early_transcribed_membrane_protein, Plasmodium ring stage membrane protein ETRAMP. This model describes a family of proteins from the malaria parasite Plasmodium falciparum, several of which have been shown to be expressed specifically in the ring stage as well as the rident parasite Plasmodium yoelii. A homolog from Plasmodium chabaudi was localized to the parasitophorous vacuole membrane. Members have an initial hydrophobic, Phe/Tyr-rich stretch long enough to span the membrane, a highly charged region rich in Lys, a second putative transmembrane region, and a second highly charged, low complexity sequence region. Some members have up to 100 residues of additional C-terminal sequence. These genes have been shown to be found in the sub-telomeric regions of both P. falciparum and P. yoelii chromosomes
MKVSKILYFFAALLAINFIAPGYCNNGKKVNKKGNLKKLTKAEKKKKNKKIILYSSIASGLALLVGAGVG
LGYYYKKKNKDDEKL
>gnl|CDD|273657 TIGR01496, Dihydropteroate_synthase, dihydropteroate synthase. This model represents dihydropteroate synthase, the enzyme that catalyzes the second to last step in folic acid biosynthesis. The gene is usually designated folP (folic acid biosynthsis) or sul (sulfanilamide resistance). This model represents one branch of the family of pterin-binding enzymes (pfam00809) and of a cluster of dihydropteroate synthase and related enzymes (COG0294). Other members of pfam00809 and COG0294 are represented by model TIGR00284 [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
QIMGIVNVTPDSFSDGGRFLSVDKAVAHAERMLEEGADIIDVGGESTRPGADRVSPEEELNRVVPVIKAL
RDQPDVPISVDTYRAEVARAALEAGADIINDVSGGQDPAMLEVAAEYGVPLVLMHMRGTPRTMQENPHYE
DVVEEVLRFLEARAEELVAAGVAAERIILDPGIGFGKTPEHNLELLKHLEEFVALGYPLLVGASRKSFIG
ALLGTPPEERLEGTLAASAYAVQKGADIVRVHDVKETRDALKVLEAL
>gnl|CDD|130561 TIGR01497, Potassium-transporting_ATPase_B_chain, K+-transporting ATPase, B subunit. This model describes the P-type ATPase subunit of the complex responsible for translocating potassium ions across biological membranes in microbes. In E. coli and other species, this complex consists of the proteins KdpA, KdpB, KdpC and KdpF. KdpB is the ATPase subunit, while KdpA is the potassium-ion translocating subunit. The function of KdpC is unclear, although cit has been suggested to couple the ATPase subunit to the ion-translocating subunit, while KdpF serves to stabilize the complex. The potassium P-type ATPases have been characterized as Type IA based on a phylogenetic analysis which places this clade closest to the heavy-metal translocating ATPases (Type IB). Others place this clade closer to the Na+/K+ antiporter type (Type IIC) based on physical characteristics. This model is very clear-cut, with a strong break between trusted hits and noise. All members of the seed alignment, from Clostridium, Anabaena and E. coli are in the characterized table. One sequence above trusted, OMNI|NTL01TA01282, is apparently mis-annotated in the primary literature, but properly annotated by TIGR [Transport and binding proteins, Cations and iron carrying compounds]
SRKKLKLFTKTIVVQAIKEAFKKLNPKAQWRNPVMFIVWVGSLLTTCITIAPASFGMPGNNLALFNAIIT
GILFITVLFANFAEAVAEGRGKAQADSLKGTKKTTFAKLLRDDGAIDKVPADQLKKGDIVLVEAGDVIPC
DGEVIEGVASVDESAITGESAPVIKESGGDFASVTGGTRILSDWLVVECTANPGETFLDRMIALVEGAQR
RKTPNEIALTILLIALTLVFLLVTATLWPFAAYGGNAISVTVLVALLVCLIPTTIGGLLSAIGIAGMDRV
LGFNVIATSGRAVEACGDVDTLLLDKTGTITLGNRLASEFIPAQGVDEKTLADAAQLASLADDTPEGKSI
VILAKQLGIREDDVQSLHATFVEFTAQTRMSGINLDNGRMIRKGAVDAIKRHVEANGGHIPTDLDQAVDQ
VARQGGTPLVVCEDNRIYGVIYLKDIVKGGIKERFAQLRKMGIKTIMITGDNRLTAAAIAAEAGVDDFIA
EATPEDKIALIRQEQAEGKLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAANMVDLDSDPTKLIEVV
HIGKQLLITRGALTTFSIANDVAKYFAIIPAIFAAAYPQLQALNIMCLHSPDSAILSALIFNALIIPALI
PLALKGVSYRPLTASALLRRNLWIYGLGGLIVPFIGIKVIDLLIT
>gnl|CDD|273658 TIGR01498, folK, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase. This model describes the folate biosynthesis enzyme 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase. Alternate names include 6-hydroxymethyl-7,8-dihydropterin diphosphokinase and 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase (HPPK). The extreme C-terminal region, of typically eight to thirty residues, is not included in the model. This enzyme may be found as a fusion protein with other enzymes of folate biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
AYIALGSNLGDRLKNLRAALAALAALPVRLLIVSSIYETPPWGFTDQPDFLNAVVEVETTLSPRELLALL
QAIEAEFGRVREFRWGPRTLDLDILLYGDEVLDTPDLTVPHPRALERPFVLLPLAEIAP
>gnl|CDD|273659 TIGR01499, Folylpolyglutamate_synthase, folylpolyglutamate synthase/dihydrofolate synthase. This model represents the FolC family of folate pathway proteins. Most examples are bifunctional, active as both folylpolyglutamate synthetase (EC 6.3.2.17) and dihydrofolate synthetase (EC 6.3.2.12). The two activities are similar - ATP + glutamate + dihydropteroate or tetrahydrofolyl-[Glu](n) = ADP + orthophosphate + dihydrofolate or tetrahydrofolyl-[Glu](n+1). A mutation study of the FolC gene of E. coli suggests that both activities belong to the same active site. Because some examples are monofunctional (and these cannot be separated phylogenetically), the model is treated as subfamily, not equivalog [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPIS
DEELAQAFEQVRPILESLSQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSI
GLDHTEILGDTLEEIAWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDENYL
SFSGANLFLEPLALSLLGDHQQENAALALAALEVLGKQNPKLSEEAIRQGLANTIWPGRLEILSEDNPNI
LLDGAHNPHSAEALAEWFKKRFNGRPITLLFGALADKDAAAMLAPLKPVVDKEVFVTPFDYPRADDAADL
AAFAEETGKSTVEDWREALEEALNASAEDDILVTGSLYLVGEVRKLL
>gnl|CDD|273660 TIGR01500, Sepiapterin_reductase, sepiapterin reductase. This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs
AVCLVTGASRGFGRTIAQELAKCLKSPGSVLVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAEAGL
EQLLKALRELPRPKGLQRLLLINNAGTLGDVSKGFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSP
GLNRTVVNISSLCAIQPFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVREESV
DPDMRKGLQELKAKGKLVDPKVSAQKLLSLLEKDKFKSGAHVDYYD
>gnl|CDD|130565 TIGR01501, Glutamate_mutase_sigma_subunit, methylaspartate mutase, S subunit. This model represents the S (sigma) subunit of methylaspartate mutase (glutamate mutase), a cobalamin-dependent enzyme that catalyzes the first step in a pathway of glutamate fermentation [Energy metabolism, Amino acids and amines, Energy metabolism, Fermentation]
KKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNLGVLSPQEEFIKAAIETKADAILVSSLYGHGEIDCK
GLRQKCDEAGLEGILLYVGGNLVVGKQDFPDVEKRFKEMGFDRVFAPGTPPEVVIADLKKDLNI
>gnl|CDD|213632 TIGR01502, Methylaspartate_ammonia-lyase, methylaspartate ammonia-lyase. This model describes methylaspartate ammonia-lyase, also called beta-methylaspartase (EC 4.3.1.2). It follows methylaspartate mutase (composed of S and E subunits) in one of several possible pathways of glutamate fermentation [Energy metabolism, Amino acids and amines, Energy metabolism, Fermentation]
KIVDVLCTPGLTGFFFDDQAAIKAGAGHDGFTYTGSPVTEGFTQIRQPGESLSVLLVLEDGQVVHGDCAA
VQYSGAGGRDPLFLAKDFIPVIEKEVAPKLIGRDITNFKDMAEVFEKMTVNRNLHTAIRYGVSQALLDAA
AKTRKTTMAEVIRDEYNPGAETNAVPVFAQSGDDRYDNVDKMILKEVDVLPHGLINSVEELGLDGEKLLE
YVKWLRDRIIKLGREGYAPIFHIDVYGTIGEAFGVDIKAMADYIQTLAEAAKPFHLRIEGPMDVGSRQAQ
IEAMADLRAELDGRGVDAEIVADEWCNTVEDVKFFTDAKAGHMVQIKTPDVGGVNNIARAIMYCKANGMG
AYVGGTCNETNRSAEVTTHVGMATGARQVLAKPGMGVDEGMMIVKNEMNRVLALVGRR
>gnl|CDD|130567 TIGR01503, Glutamate_mutase_epsilon_subunit, methylaspartate mutase, E subunit. This model represents the E (epsilon) subunit of methylaspartate mutase (glutamate mutase), a cobalamin-dependent enzyme that catalyzes the first step in a pathway of glutamate fermentation [Energy metabolism, Amino acids and amines, Energy metabolism, Fermentation]
LKNKKLTDEEFHKIREEVLQQWPTGKDVDLQDAVDYHKSIPAHKNFAEKLELAKKKGKTMAQPRAGVALL
DEHIELLRTLQEEGGADFLPSTIDAYTRQNRYDEAAVGIKESIKAGRSLLNGFPGVNHGVKGCRKVLEAV
NLPLQIRHGTPDARLLAEIILAGGFTSFEGGGISYNIPYAKNVTLEKSLEDWQYCDRLVGFYEEQGVHIN
REPFGPLTGTLVPPSISNAIGIIEGLLAAEQGVKNITVGYGQVGNLTQDIAALRALEEQTNEYLKAYGYN
DVFVTTVFHQWMGGFPEDESKAFGVISTATTIAALSGATKVIVKSPHEAIGIPTAEANAAGLKATKQALN
MLNEQKIPMSKEVETEMALIKAETRCILDKVFELGDGDLARGTVKAFEAGVLDIPFAPSKYNAGKMMPVR
DNLGCVRYLEFGNVPFTEEIKNYHRERLQERAKFEGREVSFQMVIDDIFAVSKGRLIGRP
>gnl|CDD|213633 TIGR01504, glyox_carbo_lig, glyoxylate carboligase. Glyoxylate carboligase, also called tartronate-semialdehyde synthase, releases CO2 while synthesizing a single molecule of tartronate semialdehyde from two molecules of glyoxylate. It is a thiamine pyrophosphate-dependent enzyme, closely related in sequence to the large subunit of acetolactate synthase. In the D-glycerate pathway, part of allantoin degradation in the Enterobacteriaceae, tartronate semialdehyde is converted to D-glycerate and then 3-phosphoglycerate, a product of glycolysis and entry point in the general metabolism
ARMRAVDAAVYVLEKEGITTAFGVPGAAINPFYSALKAHGGIRHILARHVEGASHMAEGYTRATAGNIGV
CIGTSGPAGTDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVSKMAVTVREAALVPR
VLQQAFHLMRSGRPGPVLIDLPFDVQVAEIEFDPDTYEPLPVYKPAATRAQIEKAVEMLNAAERPLIVAG
GGVINADAADLLQEFAELTGVPVIPTLMGWGCIPDDHELMAGMVGLQTSHRYGNATLLESDFVFGIGNRW
ANRHTGSVDVYTEGRKFVHVDIEPTQIGRVFAPDLGIVSDAKAALKLLVEVAQELKKAGRLPDRSEWAAD
CQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPL
GWTIPAALGVCAADPKRNVVALSGDYDFQFMIEELAVGAQHNIPYIHVLVNNAYLGLIRQAQRAFDMDYC
VQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEEIAPAFEQAKALMAEHRVPVVVEVILERVTNI
SMGSEIDNVVEFEDLADNAADAPTATCF
>gnl|CDD|130569 TIGR01505, 2-hydroxy-3-oxopropionate_reductase, 2-hydroxy-3-oxopropionate reductase. This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism
KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVE
EVAFGENGIIEGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQA
VFDRVKPLFEALGKNIVLVGGNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAG
STVLEVKGERVIDRTFKPGFRIDLHQKDLNLALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALV
QALELLANHKV
>gnl|CDD|130570 TIGR01506, Riboflavin_synthase, riboflavin synthase. This archaeal protein catalyzes the same reaction, the final step in riboflavin biosynthesis, as bacterial riboflavin biosynthesis alpha chain. However, it is more similar in sequence to 6,7-dimethyl-8-ribityllumazine synthase, which catalyzes the previous reaction and which (in bacteria) is called the riboflavin synthase beta chain [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]
KVGIADTTFARYDMGGAAIDELRKHTAGIKIIRRTVPGIKDLPVAAKKLLEEEGCEMVITLGWVGPEEKD
KLSYHEASTGLIQVQLMTNKHVIDVTVHEDEAEDPEELKVLADNRAREHAQNLIMLLFKPDRLTKEAGMG
LRQGYPDAGPI
>gnl|CDD|273661 TIGR01507, squalene-hopene_cyclase, squalene-hopene cyclase. SHC is an essential prokaryotic gene in hopanoid (triterpenoid) biosynthesis. Squalene hopene cyclase, an integral membrane protein, directly cyclizes squalene into hopanoid products [Fatty acid and phospholipid metabolism, Other]
MAEQLVEAPATARTVEAIDRAVDYLLSCQKDEGYWWGELESNVTIEAEYVLLCHILDRVDRDRMEKIRNY
LLHEQREDGTWALYPGGPGDLSTTVEAYVALKYIGMSRDEPPMQKALRFIQSQGGIESSRVFTRMWLALV
GEYPWRGVPMVPPEIMLLPKRFPFNIYEFSSWARATVVPLSIVCSRKPVFPLPERARVPELYETDVPKPR
RRGAKGGTGWGIFDALDRALHGYEKLSVHPFRRAAEIRALDWLLERQAGDGSWGGIQPAMFNALIALKIL
GMTQHDAFIKLGWEGIDLYGVELDDSWMFQACVSPVWDTALAVLALREAGLPADHDALVKAGEWLLDKQI
TVPGDWAVKRPNLEPGGWAFQFDNVYYPDVDDTAVVVWALNGLRLPDERRRRDAMTKAFRWIAGMQSSNG
GWGAFDVDNTSDLLNHIPFCDFGAVTDPPTADVTARVLECLGSFGYDDAWPVIERAVEYLKREQEPDGSW
FGRWGVNYLYGTGAVLSALKAVGIDTREPYIQKALAWLESHQNPDGGWGEDCRSYEDPAYAGKGASTASQ
TAWALIALIAAGRAESEAARRGVQYLVETQRPDGGWDEPYYTGTGFPGDFYLGYHMYRHVFPLLALARYK
QAIER
>gnl|CDD|130572 TIGR01508, rib_reduct_arch, 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 1'-reductase, archaeal. This model represents a specific reductase of riboflavin biosynthesis in the Archaea, diaminohydroxyphosphoribosylaminopyrimidine reductase. It should not be confused with bacterial 5-amino-6-(5-phosphoribosylamino)uracil reductase. The intermediate 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine in riboflavin biosynthesis is reduced first, and then deaminated, in both Archaea and Fungi, opposite the order in Bacteria. The subsequent deaminase is not presently known and is not closely homologous to the deaminase domain (3.5.4.26) fused to the reductase domain (1.1.1.193) similar to this protein but found in most bacteria
PYVIVNVAMSLDGKLATINRDSRISCEEDLIRVHEIRAEVDAIMVGIGTVLADDPRLTVKKIKSDRNPVR
VVVDSKLRVPLNARILNKDAKTIIATSEDEPEEKVEELEDKGVEVVKFGEGRVDLKKLLDILYDKGVRRL
MVEGGGTLIWSLFKENLVDEISVYIAPKIFGGRDAPTYVDGEGFKTEDCPKLELKNFYRLGEGIVLEFKV
>gnl|CDD|273662 TIGR01509, HAD-SF-IA-v3, haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED. This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model [Unknown function, Enzymes of unknown specificity]
AILFDLDGVLVDTEFAIAKLINREELGLVPDELGVSAVGRLELALRRFKAQYGRTISPEDAQLLYKQLFY
EQIEEEAKLKPLPGVRALLEALRARGKKLALLTNSPRAHKLVLALLGLRDLFDVVIDSSDVGLGKPDPDI
YLQALKALGLEPSECVFVDDSPAGIEAAKAAGMHTVGV
>gnl|CDD|273663 TIGR01510, Phosphopantetheine_adenylyltransferase, pantetheine-phosphate adenylyltransferase, bacterial. This model describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGL
LVDYAKELGATFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVS
NLVPPAVARRLKAKF
>gnl|CDD|273664 TIGR01511, ATPase-IB1_Cu, copper-(or silver)-translocating P-type ATPase. This model describes the P-type ATPase primarily responsible for translocating copper ions accross biological membranes. These transporters are found in prokaryotes and eukaryotes. This model encompasses those species which pump copper ions out of cells or organelles (efflux pumps such as CopA of Escherichia coli) as well as those which pump the ion into cells or organelles either for the purpose of supporting life in extremely low-copper environments (for example CopA of Enterococcus hirae) or for the specific delivery of copper to a biological complex for which it is a necessary component (for example FixI of Bradyrhizobium japonicum, or CtaA and PacS of Synechocystis). The substrate specificity of these transporters may, to a varying degree, include silver ions (for example, CopA from Archaeoglobus fulgidus). Copper transporters from this family are well known as the genes which are mutated in two human disorders of copper metabolism, Wilson's and Menkes' diseases. The sequences contributing to the seed of this model are all experimentally characterized. The copper P-type ATPases have been characterized as Type IB based on a phylogenetic analysis which combines the copper-translocating ATPases with the cadmium-translocating species. This model and that describing the cadmium-ATPases (TIGR01512) are well separated, and thus we further type the copper-ATPases as IB1 (and the cadmium-ATPases as IB2). Several sequences which have not been characterized experimentally fall just below the cutoffs for both of these models (SP|Q9CCL1 from Mycobacterium leprae, GP|13816263 from Sulfolobus solfataricus, OMNI|NTL01CJ01098 from Campylobacter jejuni, OMNI|NTL01HS01687 from Halobacterium sp., GP|6899169 from Ureaplasma urealyticum and OMNI|HP1503 from Helicobacter pylori). Accession PIR|A29576 from Enterococcus faecalis scores very high against this model, but yet is annotated as an "H+/K+ exchanging ATPase". BLAST of this sequence does not hit anything else annotated in this way. This error may come from the characterization paper published in 1987. Accession GP|7415611 from Saccharomyces cerevisiae appears to be mis-annotated as a cadmium resistance protein. Accession OMNI|NTL01HS00542 from Halobacterium which scores above trusted for this model is annotated as "molybdenum-binding protein" although no evidence can be found for this classification [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds]
AGRPFYKSAWKALRHKAPNMDTLIALGTTVAYGYSLVALLANQVLTGLHVHTFFDASAMLITFILLGRWL
EMLAKGRASDALSKLAKLQPSTATLLTKDGSIEEVPVALLQPGDIVKVLPGEKIPVDGTVIEGESEVDES
LVTGESLPVPKKVGDPVIAGTVNGTGSLVVRATATGEDTTLAQIVRLVRQAQQSKAPIQRLADKVAGYFV
PVVIAIALITFVIWLFALEFAVTVLIIACPCALGLATPTVIAVATGLAAKNGVLIKDGDALERAANIDTV
VFDKTGTLTQGKPTVTDVHVFGDRDRTELLALAAALEAGSEHPLAKAIVSYAKEKGITLVTVSDFKAIPG
IGVEGTVEGTKIQLGNEKLLGENAIKIDGKAGQGSTVVLVAVNGELAGVFALEDQLRPEAKEVIQALKRR
GIEPVMLTGDNRKTAKAVAKELGIDVRAEVLPDDKAALIKKLQEKGPVVAMVGDGINDAPALAQADVGIA
IGAGTDVAIEAADVVLLRNDLNDVATAIDLSRKTLRRIKQNLLWAFGYNVIAIPIAAGVLYPIGILLSPA
VA
>gnl|CDD|273665 TIGR01512, ATPase-IB2_Cd, heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type ATPase. This model describes the P-type ATPase primarily responsible for translocating cadmium ions (and other closely-related divalent heavy metals such as cobalt, mercury, lead and zinc) across biological membranes. These transporters are found in prokaryotes and plants. Experimentally characterized members of the seed alignment include: SP|P37617 from E. coli, SP|Q10866 from Mycobacterium tuberculosis and SP|Q59998 from Synechocystis PCC6803. The cadmium P-type ATPases have been characterized as Type IB based on a phylogenetic analysis which combines the copper-translocating ATPases with the cadmium-translocating species. This model and that describing the copper-ATPases (TIGR01511) are well separated, and thus we further type the copper-ATPases as IB1 and the cadmium-ATPases as IB2. Several sequences which have not been characterized experimentally fall just below trusted cutoff for both of these models (SP|Q9CCL1 from Mycobacterium leprae, GP|13816263 from Sulfolobus solfataricus, OMNI|NTL01CJ01098 from Campylobacter jejuni, OMNI|NTL01HS01687 from Halobacterium sp., GP|6899169 from Ureaplasma urealyticum and OMNI|HP1503 from Helicobacter pylori) [Transport and binding proteins, Cations and iron carrying compounds]
VDLLMALAALGAVAIGEYLEGALLLLLFSIGETLEEYASGRARRALKALMELAPDTARRLQGDSLEEVAV
EELKVGDVVVVKPGERVPVDGEVLSGTSSVDESALTGESVPVEKAPGDEVFAGAINLDGVLTIEVTKLPA
DSTIAKIVNLVEEAQSRKAPTQRFIDRFARYYTPAVLAIALAAALVPPLLGAGPFLEWIYRALVLLVVAS
PCALVISAPAAYLSAISAAARHGILIKGGAALEALAKIKTVAFDKTGTLTTGKPKVTDVHPADGHSESEV
LRLAAAAEQGSTHPLARAIVDYARARELAPPVEDVEEVPGEGVRAVVDGGEVRIGNPRSLSEAVGASIAV
PESAGKTIVLVARDGTLLGYIALSDELRPDAAEAIAELKALGIKRLVMLTGDRRAVAEAVARELGIDEVH
AELLPEDKLEIVKELREKAGPVAMVGDGINDAPALAAADVGIAMGASGSDVALETADVVLLNDDLSRLPQ
AIRLARRTRRIIKQNVVIALGIILVLILLALFGVLPLWLAVLGHEGSTVLVILNALRLLR
>gnl|CDD|273666 TIGR01513, Nicotinate_phosphoribosyltransferase_pncB1, putative nicotinate phosphoribosyltransferase. A deep split separates two related families of proteins, one of which includes experimentally characterized examples of nicotinate phosphoribosyltransferase, an the first enzyme of NAD salvage biosynthesis. This model represents the other family. Members have a different (longer) spacing of several key motifs and have an additional C-terminal domain of up to 100 residues. One argument suggesting that this family represents the same enzyme is that no species has a member of both families. Another is that the gene encoding this protein is located near other NAD salvage biosynthesis genes in Nostoc and in at least four different Gram-positive bacteria. NAD and NADP are ubiquitous in life. Most members of this family are Gram-positive bacteria. An additional set of mutually closely related archaeal sequences score between the trusted and noise cutoffs [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
ALLTDLYELTMAQGYFREGKANQPAVFEVFFRKLPFGRGYAVFAGLEDLLEFLENFRFDAEDIEYLASLG
IFDDAFLDYLREFRFSGTVRALPEGSLVFPNEPLLQVEGPLIEAQLLETLVLNIINFQTLIATKAARIVL
AAGGKPLLEFGLRRAQGPDAALKAARAAYIGGADGTSNVLAGRLYGIPVSGTMAHSFVMSFDNELAAFRA
YAKLYPKATVLLVDTYDTLRSGLPNAIAVAKELGEQGKVVGVRIDSGDLLYLSKQARKQLDAAGLTQVKI
VVSNDLDENSIAALKAEGAPIDVYGVGTSLVTASDAPALGGVYKLVAYEGRPVMKLSENPEKSTLPGRKQ
VFRLYDATGKFLGDELTLADEPIEDLNQEKCTPVFAPVEPLLRLVMKNGQRVRPLPSLAEIRARAREQLS
KLPPEYLRLLNPHVYPVSLSPRL
>gnl|CDD|130578 TIGR01514, Nicotinate_phosphoribosyltransferase, nicotinate phosphoribosyltransferase. This model represents nicotinate phosphoribosyltransferase, the first enzyme in the salvage pathway of NAD biosynthesis from nicontinate (niacin). Members are primary proteobacterial but also include yeasts and Methanosarcina acetivorans. A related family, apparently non-overlapping in species distribution, is TIGR01513. Members of that family differ in substantially in sequence and have a long C-terminal extension missing from this family, but are proposed also to act as nicotinate phosphoribosyltransferase (see model TIGR01513) [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
IIRSLLDTDLYKITMHQAVFHNFPDVHVTYEFICRSSQLFLKEAAEALREEISALGNLRFTDDEIEYLKQ
ELPYLKSDYIDYLRNFRFHPEEQVEVGIDDKGKLDIRISGSWRDTILYEIPLLAIISELYFRFRDAEADY
EQQLEVLESKLDQLKAEIAAETMFENGFRFSEFGTRRRFSLEVQDLVTQGLKQAAPSWLLGTSNVHLAKK
LGLKPIGTVAHEWFQGHQAISEYRNAQKVALECWINEYDGDLGIALTDTFTTDAFLRDFRPPFADAYDGL
RHDSGDPVEWGDKAIAHYQKLGIDPKSKIIIFSDSLDVEKAIELSHYFKGRVKASFGIGTNLTNDFGKVE
PLNIVIKLVECNGNPVAKLSDSPGKTMGEPATFLRALRELFDTP
>gnl|CDD|273667 TIGR01515, branching_enzym, alpha-1,4-glucan:alpha-1,4-glucan 6-glycosyltransferase. This model describes the glycogen branching enzymes which are responsible for the transfer of chains of approx. 7 alpha(1--4)-linked glucosyl residues to other similar chains (in new alpha(1--6) linkages) in the biosynthesis of glycogen. This enzyme is a member of the broader amylase family of starch hydrolases which fold as (beta/alpha)8 barrels, the so-called TIM-barrel structure. All of the sequences comprising the seed of this model have been experimentally characterized. This model encompasses both bacterial and eukaryotic species. No archaea have this enzyme, although Aquifex aolicus does. Two species, Bacillus thuringiensis and Clostridium perfringens have two sequences each which are annotated as amylases. These annotations are aparrently in error. GP|18143720 from C. perfringens, for instance, contains the note "674 aa, similar to gp:A14658_1 amylase (1,4-alpha-glucan branching enzyme (EC 2.4.1.18)) from Bacillus thuringiensis (648 aa); 51.1% identity in 632 aa overlap." A branching enzyme from Porphyromonas gingivales, OMNI|PG1793, appears to be more closely related to the eukaryotic species (across a deep phylogenetic split) and may represent an instance of lateral transfer from this species' host. A sequence from Arabidopsis thaliana, GP|9294564, scores just above trusted, but appears either to contain corrupt sequence or, more likely, to be a pseudogene as some of the conserved catalytic residues common to the alpha amylase family are not conserved here [Energy metabolism, Biosynthesis and degradation of polysaccharides]
DLHLFGEGSHFRSYELLGSHYMELDGVSGTRFCVWAPNAREVRVAGDFNYWDGREHPMRRRNDNGIWELF
IPGIGEGELYKYEIVTNNGEIRLKADPYAFYAEVRPNTASLVYDLEGYSWQDQKWQEKRKAKTPYEKPVS
IYELHLGSWRKHSDGRHLSYRELADQLIPYVKELGFTHIELLPVAEHPFDGSWGYQVTGYYAPTSRFGTP
DDFMYFVDACHQAGIGVILDWVPGHFPKDDHGLAEFDGTPLYEHKDPRDGEHWDWGTLIFDYGRPEVRNF
LVANALYWAEFYHIDGLRVDAVASMLYLDYSRDEGEWSPNEDGGRENLEAVDFLRKLNQTVYEAFPGVVT
IAEESTEWPGVTRPTDEGGLGFHYKWNMGWMHDTLDYMSTDPVERQYHHQLITFSMLYAFSENFVLPLSH
DEVVHGKKSLLNKMPGDYWQKFANYRALLGYMWAHPGKKLLFMGSEFAQGSEWNDTEQLDWHLLSFPMHQ
GVSVFVRDLNRTYQKSKALYEHDFDPQGFEWIDVDDDEQSVFSFIRRAKKHGEALVIICNFTPVVRHQYR
VGVPQPGQYREVLNSDSETYGGSGQGNKGPLSAEEGALHGRPCSLTMTLPPLATSWLR
>gnl|CDD|273668 TIGR01517, ATPase-IIB_Ca, plasma-membrane calcium-translocating P-type ATPase. This model describes the P-type ATPase responsible for translocating calcium ions across the plasma membrane of eukaryotes, out of the cell. In some organisms, this type of pump may also be found in vacuolar membranes. In humans and mice, at least, there are multiple isoforms of the PMCA pump with overlapping but not redundant functions. Accordingly, there are no human diseases linked to PMCA defects, although alterations of PMCA function do elicit physiological effects. The calcium P-type ATPases have been characterized as Type IIB based on a phylogenetic analysis which distinguishes this group from the Type IIA SERCA calcium pump. A separate analysis divides Type IIA into sub-types (SERCA and PMR1) which are represented by two corresponding models (TIGR01116 and TIGR01522). This model is well separated from those
MESVRRRTSIRDNFTDGFDVGVSILTDLTDIFKKAMPLYEKLGGAEGIATKLKTDLNEGVRLSSSTLERR
EKVYGKNELPEKPPKSFLQIVWAALSDQTLILLSVAAVVSLVLGLYVPSVGEDKADTETGWIEGVAILVS
VILVVLVTAVNDYKKELQFRQLNREKSAQKIAVIRGGQEQQISIHDIVVGDIVSLSTGDVVPADGVFISG
LSLEIDESSITGESDPIKKGPVQDPFLLSGTVVNEGSGRMLVTAVGVNSFGGKLMMELRQAGEEETPLQE
KLSELAGLIGKFGMGSAVLLFLVLSLRYVFRIIRGDGRFEDTEEDAQTFLDHFIIAVTIVVVAVPEGLPL
AVTIALAYSMKKMMKDNNLVRHLAACETMGSATAICSDKTGTLTQNVMSVVQGYIGEQRFNVRDEIVLRN
LPAAVRNILVEGISLNSSSEEVVDRGGKRAFIGSKTECALLDFGLLLLLQSRDVQEVRAEEKVVKIYPFN
SERKFMSVVVKHSGGKYREFRKGASEIVLKPCRKRLDSNGEATPISEDDKDRCADVIEPLASDALRTICL
AYRDFAPEEFPRKDYPNKGLTLIGVVGIKDPLRPGVREAVQECQRAGITVRMVTGDNIDTAKAIARNCGI
LTFGGLAMEGKEFRSLVYEEMDPILPKLRVLARSSPLDKQLLVLMLKDMGEVVAVTGDGTNDAPALKLAD
VGFSMGISGTEVAKEASDIILLDDNFASIVRAVKWGRNVYDNIRKFLQFQLTVNVVAVILTFVGSCISSS
HTSPLTAVQLLWVNLIMDTLAALALATEPPTEALLDRKPIGRNAPLISRSMWKNILGQAGYQLVVTFILL
FAGGSIFDVSGPDEITSHQQGELNTIVFNTFVLLQLFNEINARKLYEGMNVFEGLFKNRIFVTIMGFTFG
FQVIIVEFGGSFFSTVSLSIEQWIGCVLLGMLSLIFGVLLRLIPVE
>gnl|CDD|130581 TIGR01518, Glycerol-3-phosphate_cytidylyltransferase, glycerol-3-phosphate cytidylyltransferase. This model describes glycerol-3-phosphate cytidyltransferase, also called CDP-glycerol pyrophosphorylase. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most but not all species encoding proteins in this family are Gram-positive bacteria [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
VLTYGTFDLLHWGHINLLERAKQLGDYLIVALSTDEFNLQKQKKAYHSYEHRKLILETIRYVDLVIPEKS
WEQKKQDIIDFNIDVFVMGDDWEGKFDFLKDECPLKVVYLPRTEGVSTTKIKKEI
>gnl|CDD|130582 TIGR01519, hypothetical_protein_PFB0965c, Plasmodium falciparum uncharacterized domain. This model represents an uncharacterized domain present in roughly eight hypothetical proteins of the malaria parasite Plasmodium falciparum
SFFKRALLLMNIFDNIFIDKLIDNNVHNKGSIISEDVVPNSLLLSKALTPLTAIPILSYITKRINFLNKY
>gnl|CDD|130583 TIGR01520, Fructose-bisphosphate_aldolase, fructose-bisphosphate aldolase, class II, yeast/E. coli subtype. Members of this family are class II examples of the glycolytic enzyme fructose-bisphosphate aldolase (FBA). This model represents one of two deeply split, architecturally distinct clades of the family that includes class II fructose-bisphosphate aldolases, tagatose-bisphosphate aldolases, and related uncharacterized proteins. This family is well-conserved and includes characterized FBA from Saccharomyces cerevisiae, Escherichia coli, and Corynebacterium glutamicum. Proteins outside the scope of this model may also be designated as class II fructose-bisphosphate aldolases, but are well separated in an alignment-based phylogenetic tree [Energy metabolism, Glycolysis/gluconeogenesis]
IFDFVKPGVITGDDVHKLFQYAKENNFAIPAINCTSSSTINAALEAAADVKSPIIIQFSNGGAAFIAGKG
VKDEVPQGASILGAIAGAHHVHSIAEHYGVPVVLHTDHCAKKLLPWVDGLLEAGEKYFSAHGKPLFSSHM
IDLSEEPIEENIEICVKYLKRMAKIKMWLEIEIGITGGEEDGVDNSHMDAEALYTQPEDVYYAYEELSKI
SPNFSIAAAFGNVHGVYKPGNVKLTPDILADGQEYVSEKLGLPAAKPLFFVFHGGSGSTKQEIKEALSYG
VVKMNIDTDTQWAYWEGILNYYKNNEDYLQGQLGNPKGPDKPNKKFYDPRVWLREGEKSMKARVEKACQE
LNNINVL
>gnl|CDD|130584 TIGR01521, Fructose-bisphosphate_aldolase, fructose-bisphosphate aldolase, class II, Calvin cycle subtype. Members of this family are class II examples of the enzyme fructose-bisphosphate aldolase, an enzyme both of glycolysis and (in the opposite direction) of the Calvin cycle of CO2 fixation. A deep split separates the tightly conserved yeast/E. coli/Mycobacterium subtype (all species lacking the Calvin cycle) represented by model TIGR01520 from a broader group of aldolases that includes both tagatose- and fructose-bisphosphate aldolases. This model represents a distinct, elongated, very well conserved subtype within the latter group. Most species with this aldolase subtype have the Calvin cycle
LISMRQLLDHAAEFGYGVPAFNVNNMEQMRAIMEAADKTDSPVILQASRGARSYAGAPFLRHLILAAIEE
YPHIPVVMHQDHGNSPATCQRAIQLGFTSVMMDGSLREDAKTPADYDYNVRVTAEVVAFAHAVGASVEGE
LGCLGSLETGMGEAEDGHGFEGVLDHSQLLTDPEEAADFVKKTKVDALAVAIGTSHGAYKFTRKPTGEVL
AIQRIEEIHARLPDTHLVMHGSSSVPQEWLDIINEYGGEIKETYGVPVEEIVEGIKYGVRKVNIDTDLRL
ASTAAFRRFAAQNPSEFDPRKFLKPTVEAMRDVCIARYEAFGTAGNASKIKPISLEGMAQRYARGEL
>gnl|CDD|130585 TIGR01522, ATPase-IIA2_Ca, golgi membrane calcium-translocating P-type ATPase. This model describes the P-type ATPase responsible for translocating calcium ions across the golgi membrane of fungi and animals, and is of particular importance in the sarcoplasmic reticulum of skeletal and cardiac muscle in vertebrates. The calcium P-type ATPases have been characterized as Type IIA based on a phylogenetic analysis which distinguishes this group from the Type IIB PMCA calcium pump modelled by TIGR01517. A separate analysis divides Type IIA into sub-types, SERCA and PMR1, the former of which is modelled by TIGR01116
SKQYCELSVEETCSKLQTDLQNGLNSSQEASHRRAFHGWNEFDVEEDESLWKKFLSQFVKNPLILLLIAS
AVISVFMGNIDDAVSITLAILIVVTVGFVQEYRSEKSLEALNKLVPPECHLIREGKLEHVLASTLVPGDL
VCLSVGDRVPADLRIVEAVDLSIDESNLTGETTPVSKVTAPIPAATNGDLAERSNIAFMGTLVRCGHGKG
IVVGTGSNTEFGAVFKMMQAIEKPKTPLQKSMDLLGKQLSLVSFGVIGVICLVGWFQGKDWLEMFTISVS
LAVAAIPEGLPIIVTVTLALGVLRMSKKRAIVRKLPSVETLGSVNVICSDKTGTLTKNHMTVTKIWTSDG
LHTMLNAVSLNQFGEVIVDGDVLHGFYTVAVSRILEAGNLCNNAKFRNEADTLLGNPTDVALIELLMKFG
LDDLRETYIRVAEVPFSSERKWMAVKCVHRQDRSEMCFMKGAYEQVLKYCTYYQKKDGKTLTLTQQQRDV
IQEEAAEMASAGLRVIAFASGPEKGQLTFLGLVGINDPPRPGVKEAVTTLITGGVRIIMITGDSQETAVS
IARRLGMPSKTSQSVSGEKLDAMDDQQLSQIVPKVAVFARASPEHKMKIVKALQKRGDVVAMTGDGVNDA
PALKLADIGVAMGQTGTDVAKEAADMILTDDDFATILSAIEEGKGIFNNIKNFITFQLSTSVAALSLIAL
ATLMGFPNPLNAMQILWINILMDGPPAQSLGVEPVDKDVMRKPPRPRNDKILTKDLIKKILVSAIIIVVG
TLFVFVREMQDGVITARDTTMTFTCFVFFDMFNALACRSQTKSVFEIGFFSNRMFNYAVGGSIIGQLLVI
YFPPLQSVFQTEALSIKDLLFLLLITSSVCIVDEIRKKVERSRE
>gnl|CDD|130586 TIGR01523, ATPase-IID_K-Na, potassium and/or sodium efflux P-type ATPase, fungal-type. Initially described as a calcium efflux ATPase, more recent work has shown that the S. pombe CTA3 gene is in fact a potassium ion efflux pump. This model describes the clade of fungal P-type ATPases responsible for potassium and sodium efflux. The degree to which these pumps show preference for sodium or potassium varies. This group of ATPases has been classified by phylogentic analysis as type IID. The Leishmania sequence (GP|3192903), which falls between trusted and noise in this model, may very well turn out to be an active potassium pump
NAEFNAYFSDIADEAAEFIGTSIPEGLTHDEAQHRLKEVGENRLEADSGIDAKAMLLHQVCNAMCMVLII
AAAISFAMHDWIEGGVISAIIALNILIGFIQEYKAEKTMDSLKNLASPMAHVIRNGKSDAIDSHDLVPGD
ICLLKTGDTIPADLRLIETKNFDTDEALLTGESLPVIKDAHATFGKEEDTPIGDRINLAFSSSAVTKGRA
KGICIATALNSEIGAIAAGLQGDGGLFQRPEKDDPNKRRKLNKWILKVTKKVTGAFLGLNVGTPLHRKLS
KLAVILFCIAIIFAIIVMAAHKFDVDKEVAIYAICLAISIIPESLIAVLSITMAMGAANMSKRNVIVRKL
DALEALGAVNDICSDKTGTITQGKMIARQIWIPRFGTISIDNSDDAFNPNEGNVSGIPRFSPYEYSHNEA
ADQDILKEFKDELKEIDLPEDIDMDLFIKLLETAALANIATVFKDDATDCWKAHGDPTEIAIHVFAKKFD
LPHNALTGEEDLLKSNENDQSSLSQHNEKPGSAQFEFIAEFPFDSEIKRMASIYEDNHGETYNIYAKGAF
ERIIECCSSSNGKDGVKISPLEDCDRELIIANMESLAAEGLRVLAFASKSFDKADNNDDQLKNETLNRAT
AESDLEFLGLIGIYDPPRNESAGAVEKCHQAGINVHMLTGDFPETAKAIAQEVGIIPPNFIHDRDEIMDS
MVMTGSQFDALSDEEVDDLKALCLVIARCAPQTKVKMIEALHRRKAFCAMTGDGVNDSPSLKMANVGIAM
GINGSDVAKDASDIVLSDDNFASILNAIEEGRRMFDNIMKFVLHLLAENVAEAILLIIGLAFRDENGKSV
FPLSPVEILWCIMITSCFPAMGLGLEKAAPDLMDRLPHDNEVGIFQKELIIDMFAYGFFLGGSCLASFTG
ILYGFGSGNLGHDCDAHYHAGCNDVFKARSAAFATMTFCALILAVEVKDFDNSFFNLHGIPDGDSNFKEF
FHSIVENKFLAWAIAFAAVSAFPTIYIPVINDDVFKHKPIGAEWGLAAAATIAFFFGAEIWKCGKRRLFK
PQK
>gnl|CDD|130587 TIGR01524, Magnesium-transporting_ATPase_P-type_1, magnesium-translocating P-type ATPase. This model describes the magnesium translocating P-type ATPase found in a limited number of bacterial species and best described in Salmonella typhimurium, which contains two isoforms. These transporters are active in low external Mg2+ concentrations and pump the ion into the cytoplasm. The magnesium ATPases have been classified as type IIIB by a phylogenetic analysis [Transport and binding proteins, Cations and iron carrying compounds]
NKLHVKKQGNNLLKESQMGKETLLRKLGVHETGLTNVEVTERLAEFGPNQTVEEKKVPNLRLLIRAFNNP
FIYILAMLMGVSYLTDDLEATVIIALMVLASGLLGFIQESRAERAAYALKNMVKNTATVLRVINENGNGS
MDEVPIDALVPGDLIELAAGDIIPADARVISARDLFINQSALTGESLPVEKFVEDKRARDPEILERENLC
FMGTNVLSGHAQAVVLATGSSTWFGSLAIAATERRGQTAFDKGVKSVSKLLIRFMLVMVPVVLMINGLMK
GDWLEAFLFALAVAVGLTPEMLPMIVSSNLAKGAINMSKKKVIVKELSAIQNFGAMDILCTDKTGTLTQD
KIELEKHIDSSGETSERVLKMAWLNSYFQTGWKNVLDHAVLAKLDESAARQTASRWKKVDEIPFDFDRRR
LSVVVENRAEVTRLICKGAVEEMLTVCTHKRFGGAVVTLSESEKSELQDMTAEMNRQGIRVIAVATKTLK
VGEADFTKTDEEQLIIEGFLGFLDPPKESTKEAIAALFKNGINVKVLTGDNEIVTARICQEVGIDANDFL
LGADIEELSDEELARELRKYHIFARLTPMQKSRIIGLLKKAGHTVGFLGDGINDAPALRKADVGISVDTA
ADIAKEASDIILLEKSLMVLEEGVIEGRNTFGNILKYLKMTASSNFGNVFSVLVASAFIPFLPMLSLHLL
IQNLLYDFSQLTLPWDKMDREFLKKPHQWEQKGMGRFMLCIGPVSSIFDIATFLLMWFVFSANTVEEQAL
FQSGWFVVGLLSQTLVVHMIRTEKIPFIQSRAAAPVMIATLLVMALGIIIPFSPLGHSIGLVSLPLSYFP
WLIAILVGYMATMQLVKTFYIRRFGEW
>gnl|CDD|273669 TIGR01525, Copper-transporting_ATPase, heavy metal translocating P-type ATPase. This model encompasses two equivalog models for the copper and cadmium-type heavy metal transporting P-type ATPases (TIGR01511 and TIGR01512) as well as those species which score ambiguously between both models. For more comments and references, see the files on TIGR01511 and 01512
MDTLMALAAIAAYAMGLVLEGALLLFLFLLGETLEERAKSRASDALSALLALAPSTARVLQGDGSEEEVP
VEELQVGDIVIVRPGERIPVDGVVISGESEVDESALTGESMPVEKKEGDEVFAGTINGDGSLTIRVTKLG
EDSTLAQIVELVEEAQSSKAPIQRLADRIASYYVPAVLAIALLTFVVWLALGALWREALYRALTVLVVAC
PCALGLATPVAILVAIGAAARRGILIKGGDALEKLAKVKTVVFDKTGTLTTGKPTVVDIEPLDDASEEEL
LALAAALEQSSSHPLARAIVRYAKERGLELPPEDVEEVPGKGVEATVDGGREVRIGNPRFLGNRELAIEP
ISASPDLLNEGESQGKTVVFVAVDGELLGVIALRDQLRPEAKEAIAALKRAGGIKLVMLTGDNRSAAEAV
AAELGIDDEVHAELLPEDKLAIVKKLQEEGGPVAMVGDGINDAPALAAADVGIAMGSGSDVAIEAADIVL
LNDDLRSLPTAIDLSRKTRRIIKQNLAWALGYNLVAIPLAAGGLLPLWLAVLLHEGSTVLVVLNSLRL
>gnl|CDD|273670 TIGR01526, nadR_NMN_Atrans, nicotinamide-nucleotide adenylyltransferase, NadR type. The NadR protein of E. coli and closely related bacteria is both enzyme and regulatory protein. The first 60 or so amino acids, N-terminal to the region covered by this model, is a DNA-binding helix-turn-helix domain (pfam01381) responsible for repressing the nadAB genes of NAD de novo biosynthesis. The NadR homologs in Mycobacterium tuberculosis, Haemophilus influenzae, and others appear to lack the repressor domain. NadR has recently been shown to act as an enzyme of the salvage pathway of NAD biosynthesis, nicotinamide-nucleotide adenylyltransferase; members of this family are presumed to share this activity. E. coli NadR has also been found to regulate the import of its substrate, nicotinamide ribonucleotide, but it is not known if the other members of this model share that activity
KTIGVVFGKFYPLHTGHIYLIYEAFSKVDELHIVVGSLFYDSKAKRPPPVQDRLRWLREIFKYQKNQIFI
HHLNEDGIPEYPNGWDSWSNALKTLFHEKHFEPDIVFSSEPQYAAPYEKYLGLEVVLVDPDRTFFSVSAT
QIRENPFQHWKHIPREVRPFFVKTVAILGGESTGKSTLVNKLAAVFNTTSAWEYAREYVEEKLGGDEALQ
YSDYAQIALGQQRYIDYAVRHAHKIAFIDTDFITTQVFAKQYEGREHPFLDSDIAEYPFDLTLLLKPNTE
WVDDGLRSLGSQKQRQEFQQLLKKLLDEYGVPFVVIESPDYLDRY
>gnl|CDD|273671 TIGR01527, Nicotinamide-nucleotide_adenylyltransferase, nicotinamide-nucleotide adenylyltransferase. This model describes a family of archaeal proteins with the activity of the NAD salvage biosynthesis enzyme nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1). In some cases, the enzyme was tested and found also to have the activity of nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18), an enzyme of NAD de novo biosynthesis, although with a higher Km. In some archaeal species, a lower-scoring paralog, uncharacterized with respect to activity, is also present. These score between trusted and noise cutoffs [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
RGFYIGRFQPFHLGHLEVIKKIAEEVDELIIGIGSAQESHTLENPFTAGERILMITQSLKEVGDLTYYII
PIEDIERNSIWVSYVESMTPPFDVVYSNNPLVRRLFKEAGYEVKRPPMFNRKEYSGTEIRRRMLNGEDWE
HLVPKAVADVIKEIKGVERLRKIAG
>gnl|CDD|273672 TIGR01528, Protein_pnuC., nicotinamide mononucleotide transporter PnuC. The PnuC protein of E. coli is membrane protein responsible for nicotinamide mononucleotide transport, subject to regulation by interaction with the NadR (also called NadI) protein (see TIGR01526). This model defines a region corresponding to most of the length of PnuC, found primarily in pathogens. The extreme N- and C-terminal regions are poorly conserved and not included in the alignment and model [Transport and binding proteins, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
LSIIELIAGLMGILCVVLASEGKVSNYIFGLISAVIYLYIAYQTGLYAEVLLQLFFVIANIYGLFAWKKN
SQQEENGVTSGLKKLKGKGWTIILSTSVVLTVVIALILKFIGDNFPWLDSITFVIGIVAQILMVRRYREN
WILWLLSNVVSIILWFLAFTGSLAMLLTYIIYLFNSLYGFYNWNKSKKQ
>gnl|CDD|130592 TIGR01529, Arginine_repressor., arginine repressor. This model includes most members of the arginine-responsive transcriptional regulator family ArgR. This hexameric protein binds DNA at its amino end to repress arginine biosyntheis or activate arginine catabolism. Some species have several ArgR paralogs. In a neighbor-joining tree, some of these paralogous sequences show long branches and differ significantly in an otherwise well-conserved C-terminal region motif GT[VIL][AC]GDDT. These paralogs are excluded from the seed and score in the gray zone of this model, between trusted and noise cutoffs [Amino acid biosynthesis, Glutamate family, Regulatory functions, DNA interactions]
DQRQERIKEIITEEKISTQEELVALLKAEGIEVTQATVSRDLRELGAVKVRDEDGSYVYSLPADGVSDPT
SKLKRLLKNLVLSIDRAGNLIVIRTKPGEASVIANLLDRLDKDEILGTIAGDDTILVICRDPETAELLME
RLLELL
>gnl|CDD|211667 TIGR01530, Probable_5'-nucleotidase, NAD pyrophosphatase/5'-nucleotidase NadN. This model describes NadN of Haemophilus influenzae and a small number of close homologs in pathogenic, Gram-negative bacteria. NadN is a periplasmic enzyme that cleaves NAD (nicotinamide adenine dinucleotide) to NMN (nicotinamide mononucleotide) and AMP. The NMN must be converted by a 5'-nucleotidase to nicotinamide riboside for import. NadN belongs a large family of 5'-nucleotidases and has NMN 5'-nucleotidase activity for NMN, AMP, etc [Transport and binding proteins, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
LSILHINDHHSYLEPHETRINLNGQQTKVDIGGFSAVNAKLNKLRKKYKNPLVLHAGDAITGTLYFTLFG
GSADAAVMNAGNFHYFTLGNHEFDAGNEGLLKLLEPLKIPVLSANVIPDKASILYNKWKPYDIFTVDGEK
IAIIGLDTVNKTVNSSSPGKDVKFYDEIATAQIMANALKQQGINKIILLSHAGSEKNIEIAQKVNDIDVI
VTGDSHYLYGNDELRSLKLPVIYEYPLEFKNPNGEPVFVMEGWAYSAVVGDLGVKFSPEGIASITRKIPH
VLMSSHKLQVKNAEGKWYELTGDERKKALDTLKSMKSISLDDHDAKTDSLIEKYKSEKDRLAQEIVGVIT
GSAMPGGSANRIPNKAGSNPEGSIATRFIAETMYNELKTVDLTIQNAGGVRADILPGNVTFNDAYTFLPF
GNTLYTYKMEGSLVKQVLEDAMQFALVDGSTGAFPYGAGIRYEANETPNAEGKRLVSVEVLNKQTQQWEP
IDDNKRYLVGTNAYVAGGKDGYKTFGKLFNDPKYEGVDTYLPDAESFIKFMKKHP
>gnl|CDD|273673 TIGR01531, Includes:_Amylo-alpha-16-glucosidase, glycogen debranching enzymye. glycogen debranching enzyme possesses two different catalytic activities; oligo-1,4--_1,4-glucantransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). Site directed mutagenesis studies in S. cerevisiae indicate that the transferase and glucosidase activities are independent and located in different regions of the polypeptide chain. Proteins in this model belong to the larger alpha-amylase family. The model covers eukaryotic proteins with a seed composed of human, nematode and yeast sequences. Yeast seed sequence is well characterized. The model is quite rigorous; either query sequence yields large bit score or it fails to hit the model altogether. There doesn't appear to be any middle ground [Energy metabolism, Biosynthesis and degradation of polysaccharides]
LTRLEIGLPLDFPKDQSLLGKKVLVYTNYPVPGDGFVRTNRSLDWNTPFERKDFYKKYCHSSFHDDCIDL
NVYASGSYCFYFSFENDEEKLETTGGGYFVVLPMLYINADKFLPLDSIALQTVLAKLLGPLSEWEPRLRV
AKEKGYNMIHFTPLQELGGSNSCYSLYDQLQLNQHFKSQKDGKNDVQALVEKLHRDWNVLSITDIVFNHT
ANNSPWLLEHPEAAYNCITSPHLRPAIVLDRLNFSFGLDIAEWEHRGVPALIEHEHLNAIMYGIKVHVLP
KLKLWEFYQVDVQKAVNDFKAHWTQESSYVTNNIKDQSSDIIQDPEYRRFGVTVNFETALRIFNRHNGDL
KLEEDRGEKCSSSLATALNILNENLRLYRYDIDVALEQLLGGIKYERLADGGPKQGPVTVKHPLTTYYFT
FKGKDGSEEKFAYDPEKADFLMAHNGWVMGSDPLRDFASPGSRVYLRRELICWGDSVKLRYGNKPEDSPY
LWQHMKEYTEMTARIFDGVRIDNCHSTPIHVAEYLLDAARKYNPNLYVVAELFTGSETLDNVFVNRLGIS
SLIREAMSAWDSHEEGRLVYRYGGRPVGSFKQVSPRILTASIAHALFMDCTHDNESPIEKRSVYDTLPSA
ALVSMASCAIGSNRGYDELVPHHIHVVSEERYYISWPTGSPSSGIIKAKAALNKLHTSLGEKGFIQVYVD
QMDGDIVAVTRHSPKTHQSVVLVARTAFSDNDIDWDPNGLPPVVINGVLEEVIFEYALERVQEEWGREDP
NVINGIKGIPTELREHIDLSYSTSFKISDGEIELPNFPPGSVVIFRVSPSPEAQNAVDSLDNFITSGALK
FTSSALSRLTLESLNSVLYRCESEDSAGGGGAYDIPNFGKPVYCGLQGLVSVLRKIRPKNDLGHPLCNNL
RDGHWMLDYISSRLNSYSEELGEVSNWLRARFDPLKKIPRYLIPCYFDLIVSGLYGCLRLKAIKLMSRFI
GNSSLFVQSLSLSSLQFLSVIKSASLLPGPVPLQIEDQYCVSLAAGLPHFSVGYMRCWGRDTFIALRGML
LTTGRFDEARAIILAFAGTLRHGLIPNLLDEGINPRYNCRDAAWFWLQCIQDYVEIVPNGEKILKDPVRR
IYPDDDSIPVDDGRADQYLFEVIYEALQKHFQGIQFRERNAGPQIDRVMTDEGFNVTIGVDWETGFIYGG
NRFNCGTWMDKMGESEKAGNKGIPATPRDGAAVEIVGLLKSALRFLIELKEKGVFKRSGVETQKWSYIEW
NQKIQDNFEKRFFVDESQDADYDVAKLGVNRRGIYKDSYGSTKPWTDYQLRPNFAIAMTVAPELFVPEKA
WKALTIAEVLLGPLGMKTLDPSDWNYRGYYNNGEDSDDFATAKGRNYHQGPEWVWPIGYFLRARLHFHFK
TGPRCQAAAIKPVSYLLQQLYYHLKESPWRGLPELTNKDGEYCNDSCPTQAWSVACLLELLYDL
>gnl|CDD|130595 TIGR01532, D-erythrose-4-phosphate_dehydrogenase_E4PDH., erythrose-4-phosphate dehydrogenase. This model represents the small clade of dehydrogenases in gamma-proteobacteria which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase, whose substrate differs only in the lack of one carbon relative to E4P. Accordingly, this model is very close to the corresponding models for GAPDH, and those sequences which hit above trusted here invariably hit between trusted and noise to the GAPDH model (TIGR01534). Similarly, it may be found that there are species outside of the gamma proteobacteria which synthesize pyridoxine and have more than one aparrent GAPDH gene of which one may have E4PD activity - this may necessitate a readjustment of these models. Alternatively, some of the GAPDH enzymes may prove to be bifunctional in certain species [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
RVAINGFGRIGRNVLRALYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQDRDQLFVGDD
AIRVLHERSLQSLPWRELGVDLVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGASDLDATIVYGVNQDQL
RAEHRIVSNASCTTNCIVPVIKLLDDAYGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDT
KLAAGIERFFPQFNDRFEAIAVRVPTVNVTAIDLSVTVKKPVKANEVNLLLQKAAQGALRGIVDYTELPL
VSVDFNHDPHSAIVDGTQTRVSGAHLVKTLVWCDNEWGFANRMLD
>gnl|CDD|273674 TIGR01533, Lipoprotein_E, 5'-nucleotidase, lipoprotein e(P4) family. This model represents a set of bacterial lipoproteins belonging to a larger acid phosphatase family (pfam03767), which in turn belongs to the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases. Members are found on the outer membrane of Gram-negative bacteria and the cytoplasmic membrane of Gram-positive bacteria. Most members have classic lipoprotein signal sequences. A critical role of this 5'-nucleotidase in Haemophilus influenzae is the degradation of external riboside in order to allow transport into the cell. An earlier suggested role in hemin transport is no longer current. This enzyme may also have other physiologically significant roles [Transport and binding proteins, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
MKKTLKITLLAGLSLSVLTLKGCSSAQMKSEGTAQNTMSVAWMQRSAEYKALYLQAYNLAKMRLDNNLKK
VKDKKYAIVLDLDETVLDNSPYQGYQVLNNKPFDPETWDKWVQAAQAKPVAGALDFLNYANSKGVKIFYV
SNRSEKEKAATLKNLKRFGFPQADEEHLLLKKDKSSKESRRQKVQKDYEIVLLFGDNLLDFDDFFYKDKE
SQDRQALVLQNQEKFGKKFIILPNPMYGSWEGAIYKGNYKKDLKQIKERDKALKAF
>gnl|CDD|273675 TIGR01534, Glyceraldehyde-3-phosphate_dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, type I. This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model [Energy metabolism, Glycolysis/gluconeogenesis]
KVGINGFGRIGRLVLRRILEKPGNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKE
VISVFSERDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYD
GEERIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTG
AAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELV
SSDFIGSPYSSIVDATATKVTGLGDSLVKVYAWYDNEWGYSNRLVD
>gnl|CDD|130598 TIGR01535, glucan_glucosid, glucan 1,4-alpha-glucosidase. Glucan 1,4-alpha-glucosidase catalyzes the hydrolysis of terminal 1,4-linked alpha-D-glucose residues from non-reducing ends of polysaccharides, releasing a beta-D-glucose monomer. Some forms of this enzyme can hydrolyze terminal 1,6- and 1,3-alpha-D-glucosidic bonds in polysaccharides as well [Energy metabolism, Biosynthesis and degradation of polysaccharides]
SKVWFTLANGALSEVYYPRIDTADIKELKFAVTDGKSFVSDETKDTTSKVEKFTDKALAYKLTNTDKKGR
YRITKQIFTDPKRNALILKVTFEALKGSIGDYKLYLLLDPHLANTGGGNSGYVIKYANNEMLMAKGDNVY
LALVSSIGWKAASAGYVKVSDGMTDLDANGQLTKHYDSARDGNIILAAEIDLTKASETFELVLGFGASAY
EAAKTAVATLKEGYRRVKDAYIDEWEKYLNSLNNFNGKGNSLYYVSMMILKAHEDKTNPGAYIASLSIPW
GDGQADDNTGGYHLVWPRDLYQVANAFLAAGDVDSALRSLDYLAKVQQDNGMFPQNSWVDGKPYWTGIQL
DETAFPILLAYRLHRYDHAFYDKMLKPAADFIVKNGPKTGQERWEEIGGYSPSTLAAEIAGLTAAADIAE
QNGDAGSAQKYRETADNWQKLIENWTFTTNGPLGDGQYYLRIAGLGDPNADFLINIANGGGVYPEKEVLD
PGFLELVRLGVKSPDDPHILATLKEIDSTIKVDTPKGPSWYRYTHDGYGEPAKTEAYDGTGKGRLWPLLT
GERGHYELAAGKDATPYLKAMEKFANEGGMIPEQVWDQTDLPSRGLFYGLPTDSASPLNWAHAEYVKLLR
SNIDGSVLDMPDIVYKRY
>gnl|CDD|273676 TIGR01536, Asparagine_synthetase_1, asparagine synthase (glutamine-hydrolyzing). This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff [Amino acid biosynthesis, Aspartate family]
IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIEYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVI
VFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRF
GIKPLYYAYDGGQLYFASEIKALLAHPNIKPFPDGAALAPGFGFVRVPPPSTFFRGVFELEPGHDLPLDD
DGLNIERYYWERRDEHTDSEEDLVDELRSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPRGP
VHTFSIGFEGSPDFDESKYARKVADHLGTEHHEVLFSVEEGLDALPEVIYHLEEPTTIRASIPLYLLSKL
AREDGVKVVLSGEGADELFGGYLYFHEAPAAEALREELQYLDLELYMPGLLRRKDRMSMAHSLEVRVPFL
DHELVEYALSIPPEMKLRDGKEKYLLREAFEGYLPEEILWRPKEGF
>gnl|CDD|273677 TIGR01537, portal_protein, phage portal protein, HK97 family. This model represents one of several distantly related families of phage portal protein. This protein forms a hole, or portal, that enables DNA passage during packaging and ejection. It also forms the junction between the phage head (capsid) and the tail proteins. It functions as a dodecamer of a single polypeptide of average mol. wt. of 40-90 KDa [Mobile and extrachromosomal element functions, Prophage functions]
VDGETALKNSAVYSCVNLIAEDIAKLPLLLYEGTREEIRKHDLYYLLNTKPNKNLSAFQFWQQLILSLLL
DGNAYIVIIRDKSGEIYELDLLTPNKVTLDVDADDRLIYYVITFDDYNTIEKNFTFEDVLHLKLNSLDGL
VGISPLEYLGDTIGLDNAAQKYKKKFFKNGLRPSGVVKVAGSLDEEAREKLREEFEKAYSGAKNAGRVLL
LEAGMDYEPLSVSPVDAQILELKNDGRKEIANAFGVPPYLLGGGTTFANLEEQNLDFLRFTLNPIIEQIE
QELNRKLLTESEREGYYIKFDVTSILRYDSKERAEAYDKGIQSGFLTINEVREREGLPPLPG
>gnl|CDD|273678 TIGR01538, Portal_protein, phage portal protein, SPP1 family. This model represents one of several distantly related families of phage portal protein. This protein forms a hole, or portal, that enables DNA passage during packaging and ejection. It also forms the junction between the phage head (capsid) and the tail proteins. It functions as a dodecamer of a single polypeptide of average mol. wt. of 40-90 KDa [Mobile and extrachromosomal element functions, Prophage functions]
AEPDTEMIQKLIEEHNPEPVRRYECLNDIEKGRRTIYDAALKDDTKTDNRTSHNWHKYIVDQKTGYLVGN
PVKFTSDDKTLLDYLNELANQNDFHDILNELVKDLSNKGRAYELLYVDEDDETDVVIFDPEEMFVVYDDN
VEQDPLFAVRYYSKKDLMGETTQKAELYTDTHIYKYEKIDDVYQMDYSEGEYNPRPGFGRVPIIEFKNNE
ERMSDFEFYISLIDAYDSAQSDTANDFSDFSDQQLVYFGKNYDGEDPKEFRANLRYHSVIRESGDVDVKT
LRKEIDVDQTEKLLERIQDDIHKSTQVPDMSDEKFGGGASGEALKFKLFGLDNLANMAQRKFRAGLRRRY
KLFAEYSRNTGKGDFNDDKELKITFTRNRPKNLSEIVESLKQLGGIMSQETAVARNPFVQDP
>gnl|CDD|273679 TIGR01539, Portal_protein, phage portal protein, lambda family. This model represents one of several distantly related families of phage portal protein. This protein forms a hole, or portal, that enables DNA passage during packaging and ejection. It also forms the junction between the phage head (capsid) and the tail proteins. It functions as a dodecamer of a single polypeptide of average mol. wt. of 40-90 KDa [Mobile and extrachromosomal element functions, Prophage functions]
AAFGGQMAHWLPREAQSADALILQALRLLRARARDLVRNNDIVANAIDLHKDNIVGHMGIISYRPQWLGR
RGTLAKSFVDKIEAAWSEWAEGGEIDVTGKRTFTELQRLGVRTHARDGECFVQPVTGLETTQLVPFRLQA
LEPKRLPTPGHGMNNRFLRQGIEFNRYGRPVAYHICEDDFPGSGSGGWERIPRVRVTAEPVLHIFKPVRD
GQTRGAPWLASVLLRLKMLDSYEDAELQSARVAASYAGFIKSQDDTEKAADYIAGAEKDTNNVTLGGVKF
PHLFPGEDIKLQTPQDPDGGFEAFEQAQLRAIAAGLGVSYEQLSRDYSGVNYSSIRQGLNESRERFMGLQ
KFFIARLATPVFSRWLEEALLSGIIRVPRAFDFYQARSAWSRAEWIGAGRMWIDPLKEVQASVMRIRGGL
STYSKVVAEMGEDPQDVFREIARESKERQKLGLSFDVD
>gnl|CDD|273680 TIGR01540, Phage-like_element_PBSX_protein_XkdE, phage portal protein, PBSX family. This model represents one of several distantly related families of phage portal protein. This protein forms a hole, or portal, that enables DNA passage during packaging and ejection. It also forms the junction between the phage head (capsid) and the tail proteins. It functions as a dodecamer of a single polypeptide of average mol. wt. of 40-90 KDa. This family shows clear homology to TIGR01537. The alignment for this group was trimmed of poorly alignable N-terminal sequence of about 50 residues and of C-terminal regions present in some but not all members of up 180 residues [Mobile and extrachromosomal element functions, Prophage functions]
IYEPPVNIIELATLAEYNTIHQSCIDAKANNITSTGAEKDWARLEAFYKYLHFDESSEMILGYAIEDLEV
FGNGFLEVVRDGFGEPVRLEYLDAKYMRVCGAGESFVYEEDGKMKRIKKQKRYRTYVQQINAKKIFFIEL
PDPRQGVYGVPRYLGAIPSALLNRKATEFNRMYFKNGRHVGFIITVTDGMLSEESYRELQEYMNDLKGVG
NFRKFFLYEAEGIAKEKDLDGGEPVSVEIIPLAETLQKDAEFLEYKNKSRNDLRAAHRLPPLYTGITPAN
EGGRGDAEKARRVYEEQVVMPLQKILVEKLNTLLLPKLNI
>gnl|CDD|273681 TIGR01541, tail_length_tape, phage tail tape measure protein, lambda family. This model represents a relatively well-conserved region near the C-terminus of the tape measure protein of a lambda and related phage. This protein, which controls phage tail length, is typically about 1000 residues in length. Both low-complexity sequence and insertion/deletion events appear common in this family. Mutational studies suggest a ruler or template role in the determination of phage tail length. Similar behavior is attributed to proteins from distantly related or unrelated families in other phage [Mobile and extrachromosomal element functions, Prophage functions]
NQLLLLTQQIADRKLKKLNTADEKSLQSRSDEIIALIKLEKLLEEAEQKALEALKKLAEATASIRAQNKR
QLDRFGLGDKQRERLDARLQIDRTFRKQQRDLNKAMTAKGLAGSDLYKEQLAAIKASLNEALAELHAYYA
AEDALQGDWLAGARSGLADYGETATNVASATAQLATNAFGGMASNIAQMATTGKANFKSFAVSVLSDIAD
IIAKLAIAGLAQSIGSLIGGAASGGNSSSGAMASYGAAYVPNFAGGGYTAGGGKYEPSGVVHPGEFVFTK
GATRIGEGNLYAIMRGYAGGGGVLGVVAAGSGGLGPNGMFGGETAISINNDG
>gnl|CDD|130605 TIGR01542, minor_structural_protein_gp61, phage portal protein, putative, A118 family. This model represents a family of phage minor structural proteins. The protein is suggested to be the head-tail connector, or portal protein, on the basis of its position in the phage gene order, its presence in mature phage, its size, and its conservation across a number of complete genomes of tailed phage that lack other candidate portal proteins. Several other known portal protein families lack clear homology to this family and to each other [Mobile and extrachromosomal element functions, Prophage functions]
RRVGLTKSLKDIKDHPKINANDEEYKRIDMWKRYYQGDYAEVHNLNHNGNTVKRRLLSMNLPKVAAKKMA
SLLFNEQVKINVDDKAANEFVLNVLKTNGFTKNFERYLEYGEALGGFVIRPYVDGNKVKVAFATADCMYP
LQNDTENVDECAIANRTTESFNKNNKYYTLLEFHEWQGHDDYVITNELYRSDDPNEVGTKVPLTELYDDL
EPVVKLTDFTRPTFIYIKPNGANNKNLTSPLGISVYDNALTTIDTINLTFDSFYQEVKLGQRRVLVPSSF
VKTAVNGGQLDGSTTPYFDSDDEVYFLMQGDDDNGKAIKDITVPIRSTDYIESINAMLRIFEMQVGLSAG
TFTFDENGLKTATEVVSENSETYQTRNSHSQLVEQGIKELIVSILEVAKFIEAYSGEVVELDTITIDFDD
GVFQDEDTTINRYTNAVNAGMIPLKIALQRAWNITEEEADEWAAMIAKEKQAEMPN
>gnl|CDD|273682 TIGR01543, Putative_prohead_protease, phage prohead protease, HK97 family. This model describes the prohead protease of HK97 and related phage. It is generally encoded next to the gene for the capsid protein that it processes, and in some cases may be fused to it. This family does not show similarity to the prohead protease of phage T4 (see pfam03420) [Mobile and extrachromosomal element functions, Prophage functions, Protein fate, Other]
GTFEGYGSVFGNKDSDGWGYEVFLPGAFTNTLAEWNDKVRLLYNHDTALPVGRTVSGTKLEEDDHGLYGR
GKLPPDTPDAADVYALVKAGDVSGMSFGFRVIKDVWDDREEGDVISLLEAALYEVSVTTFPAYPEAGIAA
VKALY
>gnl|CDD|273683 TIGR01544, cytosolic_5'-nucleotidase_IIIB, haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544. This model represents a small group of metazoan sequences. The sequences from mouse are annotated as Pyrimidine 5'-nucleotidases, aparrently in reference to HSPC233, the human homolog. However, no such annotation can currently be found for this gene. This group of sequences was found during searches for members of the haloacid dehalogenase (HAD) superfamily. All of the conserved catalytic motifs are found. The placement of the variable domain between motifs 1 and 2 indicates membership in subfamily I of the superfamily, but these sequences are sufficiently different from any of the branches (IA, TIGR01493, TIGR01509, TIGR01549; IB, TIGR01488; IC, TIGR01494; ID, TIGR01658; IF TIGR01545) of that subfamily as to constitute a separate branch to now be called IE. Considering that the closest identifiable hit outside of the noise range is to a phosphoserine phosphatase, this group may be considered to be most closely allied to subfamily IB
LTQDHCRMRDPTEVERIINEFVIGGAEKMQIISDFDYTLSRFRTEDGGRVPTSHGIFDACQSLPEEFKAK
TDKLKHKYYPIEIDPHLTIEEKVPYMIEWWTKSHELTVGFPFDKSEIDQIVSKSTHALKDGTEEFFADLQ
RHGIPTLIFSAGIGNSVESVLRQANVLHPNVKVVSNFLQFDEDGLLDGFQQPLIHTFNKNETVLNETTEY
FDLVHTRDNIILLGDSIGDADMASGVPASSHILKIGYLNDHVDANLKKYMDTYDIVLVDDQTLDVARTIL
SLI
>gnl|CDD|130608 TIGR01545, Hypothetical_protein_yfhB., haloacid dehalogenase superfamily, subfamily IF hydrolase, YfhB. This model describes a clade of sequences limited to the gamma proteobacteria. This group is a member of the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases and all of the conserved catalytic motifs are present. Although structurally similar to subfamily IA in that the variable domain is predicted to consist of five consecutive alpha helices (by PSI-PRED), it is sufficiently divergent to warrant being regarded as a separate sub-family (IF). The gene name comes from the E. coli gene. There is currently no information regarding the function of this gene
AAGAKRIIFFDLDGTLHQQDMFGSFLRFLLRHLPLNALLVIPLLPIIAIALLIGGRAARWPMSLLLWACT
FGHREAHLQDLEADFVAAFRDKVTAFPLVAERLRQYLESSDADIWLITGSPQPLVEAVYFDSNFIHRLNL
IASQIERGNGGWVLPLRCLGHEKVAQLEQKIGSPLKLYSGYSDSKQDNPLLAFCEHRWRVSKRGELQQLE
>gnl|CDD|130609 TIGR01546, Glyceraldehyde-3-phosphate_dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, type II. This model describes the type II glyceraldehyde-3-phosphate dehydrogenases which are limited to archaea. These enzymes catalyze the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. In archaea, either NAD or NADP may be utilized as the cofactor. The class I GAPDH's from bacteria and eukaryotes are covered by TIGR01534. All of the members of the seed are characterized. See, for instance. This model is very solid, there are no species falling between trusted and noise at this time. The closest relatives scoring in the noise are the class I GAPDH's
VGVNGYGTIGKRVADAVTKQDDMKLVGVTKTSPDFEAYRAKELGIPVYAASEEFIPRFEEAGIEVAGTLE
DLLEKVDIVVDATPGGIGAKNKPLYEKAGVKAIFQGGEKAEVADVSFVAQANYEAALGKDYVRVVSCNTT
GLVRTLNAINDYSKVDKVRAVMVRRAADPNDVKKGPINAIVPDPVTVPSHHGPDVQTVIPNLNIETMAFV
VPTTLMHVHSIMVELKKPVTKDDIIDILENTPRVLLFEKKKGFESTAELIEFARDLHRERNDLYEIAVWK
ESINVKDNELFYMQAVHQESDVVPENIDAIRAMFELADKWDSIKKTNKSLGIL
>gnl|CDD|273684 TIGR01547, Uncharacterized_protein_YqaT, phage terminase, large subunit, PBSX family. This model detects members of a highly divergent family of the large subunit of phage terminase. All members are encoded by phage genomes or within prophage regions of bacterial genomes. This is a distinct family from pfam03354 [Mobile and extrachromosomal element functions, Prophage functions]
HEEIIAKGGRGSGKTFAIALKLVEKAARNKPQNILCARKVQNSIRDSVFKDIEDLLSIEGLNYEFKKSKS
SMEIKILNTGKKFIFKGLNDKPNKLKSGAGIAIIWFEEASQLTKEDIKELIPRLREPGGKRFIIFSSNPE
SPLHWVYKRFIENMEDEFRICIIHSTYRDNPFLSEVTIQEIEELKRRDPALYRRIWLGEWVSALGGILYK
KLDVKAAYIKESPNHPIDFGMDAGGQNSASASVVLGIEHGKKYIYVAEYYYSNAIEQVKDAVLEYAIEIK
QFLNVKQLIYADSGDKKTFSTFARLEHQFYQDVAAIKAQGAKLAVRDRIEVFRDLLASRKLKFLKEPCNT
YKKDIYNEYVWDDKTEDTKDEPVDLHDHAFDALRYAVLAFLRKM
>gnl|CDD|273685 TIGR01548, Imidazoleglycerol-phosphate_dehydratase, haloacid dehalogenase superfamily, subfamily IA hydrolase, TIGR01548. This model represents a small and phylogenetically curious clade of sequences. Sequences are found from Halobacterium (an archaeon), Nostoc and Synechococcus (cyanobacteria) and Phytophthora (a stramenophile eukaryote). These appear to be members of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases by general homology and the conservation of all of the recognized catalytic motifs. The variable domain is found in between motifs 1 and 2, indicating membership in subfamily I and phylogeny and prediction of the alpha helical nature of the variable domain (by PSI-PRED) indicate membership in subfamily IA. All but the Halobacterium sequence currently found are annotated as "Imidazoleglycerol-phosphate dehydratase", however, the source of the annotation could not be traced and significant homology could not be found between any of these sequences and known IGPD's
QALVLDMDGVMADVSQSYRRAIIDTVEHFGGVSVTHADIDHTKLAGNANNDWQLTHRLVVDGLNSASSER
VRDAPTLEAVTAQFQALYQGVGYYRDLATLGLIEDETLLTPKGLLRELHRAPKGMAVVTGRPRKDAAKFL
TTHGLEILFPVQIWMEDCPPKPNPEPLILAAKALGVEACHAAMVGDTVDDIITGRKA
>gnl|CDD|273686 TIGR01549, HAD-SF-IA-v1, haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E. This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model [Unknown function, Enzymes of unknown specificity]
AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKALKQAGGLAEEEWYRIATSALEELQGRFWSEYDA
EEAYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGSKPEPEIFLAALES
LGVPPEVLHVGDNLNDIEGARNAG
>gnl|CDD|273687 TIGR01550, Protein_kinase_doc, death-on-curing family protein. The characterized member of this family is the death-on-curing (DOC) protein of phage P1. It is part of a two protein operon with prevents-host-death (phd) that forms an addiction module. DOC lacks homology to analogous addiction module post-segregational killing proteins involved in plasmid maintenance. These modules work as a combination of a long lived poison (e.g. this protein) and a more abundant but shorter lived antidote. Members of this family have a well-conserved central motif HxFx[ND][AG]NKR. A similar region, with K replaced by G, is found in the huntingtin interacting protein (HYPE) family [Unknown function, General]
HISVEEIIAIHDANIERDGGLEFGMSNPGRAEATIERVSERLSYEESTDIFEVSAVLLYALIRSHPFNNA
NKRTALNALLLFLELNGYEFTDSPEELIDFTVGVATGETISVESLADWLRR
>gnl|CDD|233464 TIGR01551, major_capsid_P2, phage major capsid protein, P2 family. This model family represents the major capsid protein component of the heads (capsids) of bacteriophage P2 and related phage. This model represents one of several analogous families lacking detectable sequence similarity. The gene encoding this component is typically located in an operon encoding the small and large terminase subunits, the portal protein and the prohead or maturation protease [Mobile and extrachromosomal element functions, Prophage functions]
RQAYYAFAAQLAKHFGVPLDVLRGFAVKPPEAAKLGENIQESSEFLKGINMVQVDHTKGQKVFGGVEGGV
TGRKQTGRNLATLDHSQNGYELSETDSGIAINWALLDSWAIFKDRFVELLSEYFQNQVALDILQIGWNGQ
SAAADTDKTANPLLSDVNKGWLKLLQEQRAANVMTESKSSGKITIFGDNADYANLDALAFDLKQNQLDPR
HRNDPDLVVLVGADLVSKETKLIQQKHLTPSEKIALGSHNLMGSFGGMNAITPPNLPDRAAAVTTLKNLS
VYTQAGSVRRSLRNDEDRKRLVTSYYRQEGYVVEDLGLMTAIDHTKV
>gnl|CDD|273688 TIGR01552, Hypothetical_protein_Rv3357/MT3465/Mb3392., prevent-host-death family protein. This model recognizes a region of about 55 amino acids toward the N-terminal end of bacterial proteins of about 85 amino acids in length. The best-characterized member is prevent-host-death (phd) of bacteriophage P1, the antidote partner of death-on-curing (doc) (TIGR01550) in an addiction module. Addiction modules prevent plasmid curing by killing the host cell as the longer-lived killing protein persists while the gene for the shorter-lived antidote is lost. Note, however, that relatively few members of this family appear to be plasmid or phage-encoded. Also, there is little overlap, except for phage P1 itself, of species with this family and with the doc family [Cellular processes, Toxin production and resistance, Mobile and extrachromosomal element functions, Other]
SVSLSEAKNKLGELLKRVRDGEPVTITKRGRPVAVLVSAADYDRLQETLRLL
>gnl|CDD|273689 TIGR01553, Formate_dehydrogenase_major_subunit, formate dehydrogenase-N alpha subunit. This model describes a subset of formate dehydrogenase alpha chains found mainly in proteobacteria but also in Aquifex. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits of 32 and 20 kDa. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The electrons are utilized mainly in the nitrate respiration by nitrate reductase. In E. coli and Salmonella, there are two forms of the formate dehydrogenase, one induced by nitrate which is strictly anaerobic (fdn), and one incuced during the transition from aerobic to anaerobic growth (fdo). This subunit is one of only three proteins in E. coli which contain selenocysteine. This model is well-defined, with a large, unpopulated trusted/noise gap [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]
LISRRAFLKLTAGGATLSAFGGLGFDLAPAKAQARALKTVDAKQTTSVCCYCSVSCGLLVYSSSHTGDNK
TNRAIHVEGDPDHPINRGSLCPKGASTWDLVNNERRPANPLYRAPGSDQWEEISWDWAIDTIARRVKDTR
DATFVTKDAKGQVVNRCDGIASVGSSAMDNEECWLYQKWLRSLGLFYIEHQARIUHSPTVASLAPSFGRG
AMTNNWVDIKNSDLILVMGGNPAENHPIGFKWAIRAKKKGAKIIHIDPRFNRTATVADLYAPIRSGSDIA
FLNGMIKYILEKELYQKEYVVNYTNASFIVGEGFAFEDGLFAGYNKETRKYDKSKWGYEFDENGNPKRDE
TLKHPRCVFNILKEHYSRYTPEKVSAICGTPKELFLKVYEEYCKTGKPNKAMTILYALGWTQHSVGTQNI
RAMSINQLLLGNIGVPGGGINALRGHSNVQGSTDHGLLMHILPGYLGTPRASIPTYEQYTKKFTPVSKDP
QSANYWSNFPKFFASYIKSMWGDAATNENGWAYDYLPKGEDGYDSWLTLFDDMFQGKIKGFFAWGQNPLN
SGPNSNKTREALTKLKWMVVMDPFDNETGSFWRGPGMDPKEIKTEVFFLPTAVFIEKEGSISNSGRWMQW
RYKGPDPPGNAIPDGDIIVELAKRVQELYAKEGGKLAEPVTKLKWDYWVPDHPDAHEIAKEINGYALKDF
KVGDVEYKKGQQIATFGHLRDDGSTTSGCWLYTGSYTEKGNMAARRDKSDPAGLGLYPGWTWAWPANRRV
LYNRASVDLNGKPWDPERALVEWNAAEKKWVGDIPDYPPTAPPEKGKGAFIMKPEGYGRLFAPGKREDGP
LPEHYEPMESPVITNPFHPNVLHNPTALHYKTDEKAVGDPKRYPFVATTYRLTEHWHTWTRNTPWLLEAE
PQMFCEISEELATEKGIQNGDKVILESVRGKIWAKAIVTKRIKPLAIQGQQVHMIGIPIHWGWSFLKNGG
DATNILTPSVGDPNTGTPETKAFLVNIEK
>gnl|CDD|273690 TIGR01554, prophage_Lp3_protein_18, phage major capsid protein, HK97 family. This model family represents the major capsid protein component of the heads (capsids) of bacteriophage HK97, phi-105, P27, and related phage. This model represents one of several analogous families lacking detectable sequence similarity. The gene encoding this component is typically located in an operon encoding the small and large terminase subunits, the portal protein and the prohead or maturation protease [Mobile and extrachromosomal element functions, Prophage functions]
LKELREALAELAKELRKLTEDEKLAEAEEKKEEFDALKAEIDKLEAEIDRLEAALDELAAKAAAPGLGGG
GEEEGREADEEKAAFRFRNYLRGGDAAGAEERKALSTGTDSDGGYLVPEEFSTEIIELLKEYSPLRQLAT
VIPVSSGSITIPVDAGTPEAGWVGEGAARPESDPTFGQVELPVKKLAAIIPISNELLDDSAVDLEAYLAD
ELAEAFARAENAAILNGDGTGKPKGILTYAAVGKVVTTGAAGTITADDLIDLIYSLDPAYRANAVWVMNR
STLAALRKLKDGNGRYLWQPGLTAGQPATLLGRPVVETEDMPDVAAGAKPILFGDFSRGYLIVDRKGMTI
RVLRDPYTEKDQVGFRATKRVDGKVVDPEAIKLLKF
>gnl|CDD|130618 TIGR01555, Uncharacterized_protein_HI_1409, phage-related protein, HI1409 family. This model describes an uncharacterized family of proteins found in prophage regions of a number of bacterial genomes, including Haemophilus influenzae, Xylella fastidiosa, Salmonella typhi, and Enterococcus faecalis. Distantly related proteins can be found in the prophage-bearing plasmids of Borrelia burgdorferi [Mobile and extrachromosomal element functions, Prophage functions]
DYRNDLMLGLGKGHDRDNYSRQRLGTSKDLSQLEALYRSNWMAKKVVDIPAEDMTRNWWSLKTMQDDKVL
ALYESLERQLKARERLQQALTWERLYGDGFLSIGTIEKREYSPSEPLDFENIKSLPYLNAWSGKISNGQI
DEDVFSPNYGQIESYEINGRSLLNNVTYSRATTIHRSRVPHQLRFENELWGSSLLENLYDILTRADTAVW
SVGQILFEFIFDVYKIAGLSDLTSQDGTQKVEIETKMDYQFKSTEAILLLDAEEEYGKKSSSFAGIKELL
DFFWDYLAGAADMPKTVLFGQSGGGVTGGDYDIMNYYSRITAIQENQLRPVLEVLMRCLMWAEDGCDPDD
WSVEFNPLWNVDSKTDAEIRKLTAETDKIYIEAGVSDPDDVHEELFERFGITNT
>gnl|CDD|130619 TIGR01556, dTDP-rhamnosyl_transferase_RfbF, L-rhamnosyltransferase. This model subfamily is comprised of gamma proteobacteria whose proteins function as L-rhamnosyltransferases in the synthesis of their respective surface polysaccharides. Rhamnolipids are glycolipids containing mono- or di- L-rhamnose molecules. Rhamnolipid synthesis occurs by sequential glycosyltransferase reactions involving two distinct rhamnosyltransferase enzymes. In P.aeruginosa, the synthesis of mono-rhamnolipids is catalyzed by rhamnosyltransferase 1, and proceeds by a glycosyltransfer reaction catalyzed by rhamnosyltransferase 2 to yield di-rhamnolipids [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
VTFNPDLEHLGELITSLPKQVDRIIAVDNSPHSDQPLKNARLRGQKIALIHLGDNQGIAGAQNQGLDASF
RRGVQGVLLLDQDSRPGNAFLAAQWKLLSAENGQACALGPRFFDRGTSRRLPAIHLDGLLLRQISLDGLT
TPQKTSFLISSGCLITREVYQRLGMMDEELFIDHVDTEWSLRAQNYGIPLYIDPDIVLEHRIGDSKVRIL
GGLSLSIPNHSPLRRYYLFRNGILVLRRYARSLPLKLRENLFTLIQFLAVMILEKNKLLKLRCLIKGLWD
G
>gnl|CDD|130620 TIGR01557, unnamed_protein_product, myb-like DNA-binding domain, SHAQKYF class. This model describes a DNA-binding domain restricted to (but common in) plant proteins, many of which also contain a response regulator domain. The domain appears related to the Myb-like DNA-binding domain described by pfam00249. It is distinguished in part by a well-conserved motif SH[AL]QKY[RF] at the C-terminal end of the motif
KPRVVWTEDLHDRFLQAVQKLGGPDWATPKRILELMVVDGLTRDQVASHLQKYRLKQ
>gnl|CDD|273691 TIGR01558, hypothetical_protein, phage terminase, small subunit, putative, P27 family. This model describes a distinct family of phage (and integrated prophage) putative terminase small subunit. Members tend to be adjacent to the phage terminase large subunit gene [Mobile and extrachromosomal element functions, Prophage functions]
RAPDWLGKEGKDEWKRVAPELKGSGILTNLDRDALLRYCEAYDRYREATDDLEATGITATVEDGSPKANP
ALTVVEDAFKQLRSIGSALGLTPSSRSRLVINVAKEDKKADPLEEF
>gnl|CDD|188157 TIGR01559, Squalene_synthase, farnesyl-diphosphate farnesyltransferase. This model describes farnesyl-diphosphate farnesyltransferase, also known as squalene synthase, as found in eukaryotes. This family is related to phytoene synthases. Tentatively identified archaeal homologs (excluded from this model) lack the C-terminal predicted transmembrane region universally conserved among members of this family
PSLGFCYELLNLTSRSFAAVIQELPPELRNAVCIFYLVLRALDTVEDDMTISVDKKIPLLRDFHEKIYDP
DWRFTESDNEKDRQVLDDFPVVSLEFLKLKPKYQEVIADITRRMGNGMADFIDKEVTNEQTVGDYDKYCH
YVAGLVGIGLSRLFVASGFEDPSLGESEALSNSMGLFLQKTNIIRDYLEDINEGRMFWPREIWSKYAKKL
GDFKKPENSDKALQCLNELVTNALHHATDCLTYLSRLRDQSIFNFCAIPQVMAIATLALCYNNPQVFQGN
VKIRKGTTVKLILDSTNMPAVYDIFYRYARKIYHKIDPNDPNFSKTLIIISKIEQQC
>gnl|CDD|130623 TIGR01560, phage-related_hypothetical_protein, uncharacterized phage protein (possible DNA packaging). This model describes a small (~ 100 amino acids) protein found in phage and in putative prophage regions of a number of bacterial genomes. Members have been annotated in some cases as a possible DNA packaging protein, but the source of this annotation was not traced during construction of this model [Mobile and extrachromosomal element functions, Prophage functions]
TLDEVKLSLRIDHDDDDELIKLMIAAAQDYIQSAIGTGVKDSFDSKPLFKLACIKLVAHYYENRGLYADR
ALVNVPIMVNALIHQLRGRGD
>gnl|CDD|130624 TIGR01561, glycogen_debranching_enzyme, glycogen debranching enzyme, archaeal type, putative. The seed for this model is composed of two uncharacterized archaeal proteins from Methanosarcina acetivorans and Sulfolobus solfataricus. Trusted cutoff is set so that essentially only archaeal members hit the model. The notable exceptions to archaeal membership are the Gram positive Clostridium perfringens which scores much better than some other archaea and the Cyanobacterium Nostoc sp. which scores just above the trusted cutoff. Noise cutoff is set to exclude the characterized eukaryotic glycogen debranching enzyme in S. cerevisiae. These cutoffs leave the prokaryotes Porphyromonas gingivalis and Deinococcus radiodurans below trusted but above noise. Multiple alignments including these last two species exhibit sequence divergence which may suggest a subtly different function for these prokaryotic proteins [Energy metabolism, Biosynthesis and degradation of polysaccharides]
EWLIGNGLGGYASSTICGAGARTYHGLLIAALENFHGRFLILSKFDDEILIDGDTYKLATHKYPDNISPD
GFKYLIEFEKNPFPKILWHYDAGDFQLEKKLFMHHGSNAITILYDAIRGKEGALFKICPFISFRDFHLAA
KLGNEFFTQEAGPAGTELALSEGKRIFNFEIHDKLELFNDGIWYFNFEYDLDKELGLNFIEDIFNPFCFE
SKLEKGASRFFVAARPKDISSEELEHVDILKLLEAAGQNLLILDSKLIESFALKLLRATDDFVVKNHAKD
ENAIIAGYHWFDDWGRDSFISLEGLLLIDKQFDEAKEAILKFANLCKRGLIPNNFIAFGGDPIYNGVDAS
LWAIHAIDKTFAYSQDFLFIRDVVDKVLDIIDNYCAGNDFAIGMDNDLIFHKGAPLTWMDAKVDERAVTP
RAGAACEINALWYNALKTAEFLGNELGEDAESLEEKAAGVAKNFAEKFINPDGNCLFDLIHQDEAGNQVK
DKAIRPNQIFAISLPFPIIDDESIAKAILDLIEKDLLRPFGLKSLSRDDPLYKGQYKGDALSRDTAYHNG
SLPPWLHGALVKARL
>gnl|CDD|130625 TIGR01562, Protein_FdhE, formate dehydrogenase accessory protein FdhE. This model describes an accessory protein required for the assembly of formate dehydrogenase of certain proteobacteria although not present in the final complex. The exact nature of the function of FdhE in the assembly of the complex is unknown, but considering the presence of selenocysteine, molybdopterin, iron-sulfur clusters and cytochrome b556, it is likely to have something to do with the insertion of cofactors. The only sequence scoring between trusted and noise is that from Aquifex aeolicus, which shows certain structural differences from the proteobacterial forms in the alignment. However it is notable that A. aeolicus also has a sequence scoring above trusted to the alpha subunit of formate dehydrogenase (TIGR01553)
SRTILQPDQIEAAANPKIPPHLHPPLRDLFNRRAERLLQLAEGHPLGDYLRFVAGICRLQQALLDNPPAL
APLDPERLRKARAHGMPPLDYDLLVREGAWLPWLDALLAGYPAPANAAAGAALEQLREAEEGQLKAMAIA
LLAGDFDLLSAALVPFLGAALQVAWAHWALGLEGGAVVETRESRTLCPACGSPPVASMVRQGGKETGLRY
LSCSLCATEWHYVRVKCSHCEESKHLAYLSLEHDAEKAVLKAETCDSCQGYLKILYQEKDPHADAVADDL
ASLALDMRMAEDGYLRRSPNPFLAP
>gnl|CDD|273692 TIGR01563, hypothetical_protein_AGR_C_1752, phage head-tail adaptor, putative, SPP1 family. This family describes a small protein of about 100 amino acids found in bacteriophage and in bacterial prophage regions. Examples include gp9 of phage HK022 and gp16 of phage SPP1. This minor structural protein is suggested to be a head-tail adaptor protein (although the source of this annotation was not traced during construction of this model) [Mobile and extrachromosomal element functions, Prophage functions]
KFNDRITFQTYETTGRDGRGQKITKWVDYFTLWAAVKPMSGQEFYRAGQEGVEITHVILIRYRKDVTNKM
RVIYDGRIYTIGAVIDPSRTREELDLLTKEG
>gnl|CDD|273693 TIGR01564, S-layer_protein, S-layer protein, MJ0822 family. This model represents one of several families of proteins associated with the formation of prokaryotic S-layers. Members of this family are found in archaeal species, including Pyrococcus horikoshii (split into two tandem reading frames), Methanococcus jannaschii, and related species. Some local similarity can be found to other S-layer protein families [Cell envelope, Surface structures]
KKIGAIAVGAAMVAAALALGVAAPQVPEIPKDFKFVKDGEPNVKIVVGSEAAAMDVVSAADIAAKIGSLL
YKEGEVKVGSASVTVRADATSDDDDLKVFNNNTFYPAKNQAFIVAADDLDYSEAWWNGTAFSANYTASVL
NDGTKSGELVNLGDLTTELTVKDIDPSDWYNNEVNFIEDFKDMTVKIDSDALEITMAVYNWTKTKAKDTV
TGVTTLYASIAYKDDLENFQPATYSISEGTRSPFLGEEVTLVVFDKDDDIIYLGKAVSDGAIKEGDTYVY
GTGYGTKFYAILKEVEDGYDVYKLDIQIQKDGKVVAEKSDSDTKDGALVHVYFGGGIGIQVLDAWENVGG
DYGYVQLKIYKDLKTLELGEEYMPDWKAEFAIDDNNTVIKWDALVDEDPLEDKEIGIFLTYTGDYSDTVK
SGKEVGIIEYAVLKLDDEDKEDKLYIDFSMDEYKDATLTKGDKVEDLNGDINLEFKPAEAYIPVKLTAPI
AVLDTEVSLDNADKNLILVGGPVANKLTKELADAGKVPKTESSPATYAEKCGAANGYDVLVVAGGDREGT
REAAEALIEYL
>gnl|CDD|130628 TIGR01565, unnamed_protein_product, homeobox domain, ZF-HD class. This model represents a class of homoebox domain that differs substantially from the typical homoebox domain described in pfam00046. It is found in both C4 and C3 plants
KKRRRTKFTAEQKEKMRDFAEKLGWKLKDKRREEVREFCEEIGVTRKVFKVWMHNNKK
>gnl|CDD|130629 TIGR01566, unnamed_protein_product, ZF-HD homeobox protein Cys/His-rich dimerization domain. This model describes a 54-residue domain found in the N-terminal region of plant proteins, the vast majority of which contain a ZF-HD class homeobox domain toward the C-terminus. The region between the two domains typically is rich in low complexity sequence. The companion ZF-HD homeobox domain is described in model TIGR01565
LYKECLKNHAASIGGHALDGCGEFMPSSGEEGDPESLTCAACGCHRNFHRKEP
>gnl|CDD|273694 TIGR01567, predicted_protein, S-layer family duplication domain. This model represents a sequence region found tandemly duplicated in two proven archaeal S-layer glycoproteins, MA0829 from Methanosarcina acetivorans C2A and MM1976 from Methanosarcina mazei Go1, as well as in several paralogs of those L-layer proteins from both species. Members of the family show regions of local similarity to another known family of archaeal S-layer proteins described by model TIGR01564. Some members of this family, including the proven S-layer proteins, have the archaeosortase A target motif, PGF-CTERM (TIGR04126), at the protein C-terminus [Cell envelope, Surface structures]
LTWTADSFGGFYYDIETDEGTESLSISPDAGSNVIPEGGLVYETTPQEVEYEVPEMADYGEDWDNYSVLG
WFGEKYVAIGPDATKLSKILLDSDDKKSLKTGESLDLGEGYSLNVNQVDVDGEKVWLSLSKDGEEVDSEI
ISVSTVDDDDFTYTADLGDEEDVPIFIVYVDSVFEGEEDSAVFLKGLLLIDKDEPLEIENGDEFGEMEVV
ETSESGITLKNEDSITLWLDDDIYITEDLYFGTADAKINYLRFYPA
>gnl|CDD|130631 TIGR01568, hypothetical_protein, uncharacterized plant-specific domain TIGR01568. This model describes an uncharacterized domain of about 70 residues found exclusively in plants, generally toward the C-terminus of proteins of 200 to 350 amino acids in length. At least 14 such proteins are found in Arabidopsis thaliana. Other regions of these proteins tend to consist largely of low-complexity sequence
VAVAKESDDPYEDFRRSMEEMIEERELEADWKELEELLACYLDLNPKKSHRFIVRAFVDILSALLS
>gnl|CDD|273695 TIGR01569, hypothetical_protein, plant integral membrane protein TIGR01569. This model describes a region of ~160 residues found exclusively in plant proteins, generally as the near complete length of the protein. At least 24 different members are found in Arabidopsis thaliana. Members have four predicted transmembrane regions, the last of which is preceded by an invariant CXXXXX[FY]C motif. The family is not functionally characterized
LILRVLAFSATLAAAIVMGTNRETKVVFVQLITFKAKFSDLPAFVYFVVANAIACGYSLLSLVVSIFGLL
KRRVFFKLIALFFLDLVMLALLSSGTSAAAAVAYVGKLGNKEAGWLKICGVFGKFCDRIAGSLALSLFAV
ILLVLLSILSAISL
>gnl|CDD|273696 TIGR01570, hypothetical_protein, uncharacterized plant-specific domain TIGR01570. This model represents a region of about 170 amino acids found at the C-terminus of a family of plant proteins. These proteins typically have additional highly divergent N-terminal regions rich in low complexity sequence. PSI-BLAST reveals no clear similarity to any characterized protein. At least 12 distinct members are found in Arabidopsis thaliana
VTGTIFGYRKGRVNFCIQEDRRSLPILLLELAMPTSVLQKEMSSGLVRIALECETRKQDKDSKLLSEPVW
TMYCNGRKVGYAVKRSASEEDMTVLTALSKVSVGAGVLPCGKELGGFDEDELMYMRASFERVVGSKDSES
FYMINPEGNIGQELSIFFLRS
>gnl|CDD|273697 TIGR01571, PLAC8_family_protein, uncharacterized Cys-rich domain. This model describes an uncharacterized domain of about 100 residues. It is common in plants but found also in Homo sapiens, Dictyostelium, and Leishmania; at least 12 distinct members are found in Arabidopsis. Most members of this family contain more than 10 per cent Cys, but no Cys residue is invariant across the family
SNWSTGLFDCCEDIRLCLCGLFCPCCLFGQIAETLGTFAGECLCGGLTAIAMSALCGFCGCYTCFIRIKL
REKYGIQGAPCDDCLTHLFCCFCALCQEHRELKM
>gnl|CDD|273698 TIGR01572, Hypothetical_protein, Arabidopsis paralogous family TIGR01572. This model describes a paralogous family of hypothetical proteins in Arabidopsis thaliana. No homologs are detected from other species. Length heterogeneity within the family is attributable partly to a 21-residue repeat present in from zero to three tandem copies. The central region of the repeat resembles the pattern [VIF][FY][QK]GX[LM]P[DEK]XXXDDAL
EYYRQIRESDGFDVPIGIPTSLTPLYHYDCANNSRYPDGDLVKIYARVGLHRYNFLEGTNLELDHVDKFN
KRMCALSSYYITLLAVDPDSRFLQQTFQVRVDEQKLETLDLTVEIARPKPKVTTNEPFLKPWSDSAIDDI
YKGELPEWPSDDALMSDQKRFYRVKESELRENDWISLYLELALVSHDRGDMRLKSLSQLQIVKVVIETRE
DFKPNKEKLNAKTAIVYITFKGLNKPRIGEPVDRKAIVRRIIDEITGHLCLEGKC
>gnl|CDD|273699 TIGR01573, cas2, CRISPR-associated endonuclease Cas2. This model describes most members of the family of Cas2, one of the first four protein families found to mark prokaryotic genomes that contain multiple CRISPR elements. CRISPR systems protect against invasive nucleic acid sequences, including phage. Cas2 proteins have been characterized as either endoribonuclease (for ssRNA) or endodeoxyribonuclease (for dsDNA), depending on the system to which the Cas2 belongs. CRISPR is an acronym for Clustered Regularly Interspaced Short Palindromic Repeats. The cas genes usually are found near the repeats. A distinct branch of the Cas2 family shows a very low level of sequence identity and is modeled by TIGR01873 instead of by this model (TIGR01573)
MLVLVVYDIPTDGERKRRRKLRKLLEKYGLQRVQYSVFEGILEPNQLARKLIERLKRIIPDEGSIRIYPL
TEKQYAAAIVIGGEPVTSAEDNLLL
>gnl|CDD|273700 TIGR01574, Hypothetical_UPF0004_protein_yleA., tRNA-N(6)-(isopentenyl)adenosine-37 thiotransferase enzyme MiaB. This model represents homologs of the MiaB enzyme responsible for the modification of the isopentenylated adenine-37 base of most bacterial and eukaryotic tRNAs that read codons beginning with uracil (all except tRNA(I,V) Ser). Adenine-37 is next to the anticodon on the 3' side in these tRNA's, and lack of modification at this site leads to an increased spontaneous mutation frequency. Isopentenylated A-37 is modified by methylthiolation at position 2, either by MiaB alone or in concert with a separate methylase yet to be discovered (MiaC?). MiaB contains a 4Fe-4S cluster which is labile under oxidizing conditions. Additionally, the sequence is homologous (via PSI-BLAST searches) to the biotin synthetase, BioB, which utilizes both an iron-sulfur cluster and S-adenosym methionine (SAM) to generate a radical which is responsible for initiating the insertion of sulfur into the substrate. It is reasonable to surmise that the methyl group of SAM becomes the methyl group of the product, but this has not been shown, and the possibility of a separate methylase exists. This equivalog is a member of a subfamily (TIGR00089) which contains several other hypothetical equivalogs which are all probably enzymes with similar function acting on different substrates. These enzymes contain a TRAM domain (pfam01938) which is believed to be responsible for binding to tRNAs. Hits to this model span all major groups of bacteria and eukaryotes, but not archaea, which are known to lack this particular tRNA modification. The enzyme from Thermotoga maritima has been cloned, expressed, spectroscopically characterized and shown to complement the E. coli MiaB enzyme [Protein synthesis, tRNA and rRNA base modification]
KLFIQTYGCQMNVRDSEHMAALLTAKEGYALTEDAKEADVLLINTCSVREKAEHKVFGELGGFKKLKKKN
PDLIIGVCGCMASHLGNEIFQRAPYVDFVFGTRNIHRLPQAIKTPLTQKFMVVDIDSDESEVAGYFADFR
NEGIYKSFINIMIGCNKFCTYCIVPYTRGDEISRPFDDILQEVQKLAEKGVREITLLGQNVNAYRGKDFE
GKTMDFSDLLRELSTIDGIERIRFTSSHPLDFDDDLIEVFANNPKLCKSMHLPVQSGSSEILKLMKRGYT
REWYLNLVRKLRAACPNVSISTDIIVGFPGETEEDFEETLDLLREVEFDSAFSFIYSPRPGTPAADMPDQ
IPEEIKKRRLQRLQARHNEILDKKMRKQEGKTFKVLVEGLSRNNPEELAGRTENNFLVNFEGSEDLIGKF
VDVKITNVKRMSLRGEIV
>gnl|CDD|273701 TIGR01575, rimI, ribosomal-protein-alanine acetyltransferase. Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database [Protein synthesis, Ribosomal proteins: synthesis and modification]
DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQG
IGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM
>gnl|CDD|273702 TIGR01577, Uncharacterized_glycosyl_hydrolase_MJ1610, oligosaccharide amylase. The name of this type of amylase is based on the characterization of an glucoamylase family enzyme from Thermoactinomyces vulgaris. The T. vulgaris enzyme was expressed in E. coli and, like other glucoamylases, it releases beta-D-glucose from starch. However, unlike previously characterized glucoamylases, this T. vulgaris amylase hydrolyzes maltooligosaccharides (maltotetraose, maltose) more efficiently than starch (1), indicating this enzyme belongs to a class of glucoamylase-type enzymes with oligosaccharide-metabolizing activity
ILAVLGRYGEIHRLFYPQKDYAQHVNRSSAGVLIPKGVWWFHDPDWKHEQTYIEDTNILRTTLTCDEWIE
VVIEDEVVSGRNVLIRRYVITNCGEEKIPLKFFSYTNFHMGEMKRYNTTLFVGKKEALVHYRREYAVAIG
SVLPTTRFQAGSNKDKTSAYIDIEQGLLNCNKEDIGMHTDGACLWELGLCPPGSKCFTIFFAFGKTVEKA
LEELEELRTLGFERIRSQTLADWEAYFGQAKPVQTPCLEMDNKIYSLYRRSLAVLRLLTDGEYGSMIAAP
EFDEDFVRCGGYAYCWGRDASYIATALDRAGYHDRVDRFFRWAMQTQSRDGSWQQRYYLNGRLAPLQWGL
QIDETGSILWAMDQHYRLTNDRAFLEEIWESVQKAAQYLILFIDPETPLPCRDLWEEREGVFTYTASAVY
GGLDAAAAVADKLGEKRLAQNWKKAAEFIKRAVEERFWLPERQVFAKGIKLMVLDKTIDISILGISVPFN
LIAPDDERMVKMAEAIEKHLTSPIVGGIKRYENDPYVGGNPWILTTLWLSQLYIKQGRILKALNHNGADI
YLQKSKKLLKWVMDHRTDLGLLPEQVDKETGKPAWAVPLGWSHAMFLLTVLDLDKI
>gnl|CDD|273703 TIGR01578, MiaB-like-B, MiaB-like tRNA modifying enzyme, archaeal-type. This clade of sequences is closely related to MiaB, a modifier of isopentenylated adenosine-37 of certain eukaryotic and bacterial tRNAs (see TIGR01574). Sequence alignments suggest that this equivalog performs the same chemical transformation as MiaB, perhaps on a different (or differently modified) tRNA base substrate. This clade is a member of a subfamily (TIGR00089) and spans the archaea and eukaryotes. The only archaeal miaB-like genes are in this clade, while eukaryotes have sequences described by this model as well as ones falling within the scope of the MiaB equivalog model [Protein synthesis, tRNA and rRNA base modification]
KVYVETYGCTLNNGDSEIMKNSLAAYGHELVNNAEEADLAILNTCTVKNKTEDTMLYRIESLMRNGKHVV
VAGCMPQAQKESVYDNGSVASVLGVQAIDRLVEVVEETLKKKVHGRREAGTPLSLPKPRKNPLIEIIPIN
QGCLGNCSYCITKHARGKLASYPPEKIVEKARQLVAEGCKEIWITSQDTGAYGRDIGSRLPELLRLITEI
PGEFRLRVGMMNPKNVLEILDELANVYQHEKVYKFLHLPVQSGSDSVLKEMKREYTVSDFEDIVDKFRER
FPDLTLSTDIIVGFPTETDDDFEETMELLRKYRPEKINITKFSPRPGTPAAKMKRIPTNIVKKRSKRLTK
LYEQVLLEMRDNLIGTRVHVLVTKEGKGDSLDDEDAYRQVVIRSRTREPGEFAGVEITGAKTAYLIGEII
>gnl|CDD|273704 TIGR01579, MiaB-like-C, MiaB-like tRNA modifying enzyme. This clade of sequences is closely related to MiaB, a modifier of isopentenylated adenosine-37 of certain eukaryotic and bacterial tRNAs (see TIGR01574). Sequence alignments suggest that this equivalog performs the same chemical transformation as MiaB, perhaps on a different (or differently modified) tRNA base substrate. This clade is a member of a subfamily (TIGR00089) and spans low GC Gram positive bacteria, alpha and epsilon proteobacteria, Campylobacter, Porphyromonas, Aquifex, Thermotoga, Chlamydia, Treponema and Fusobacterium [Protein synthesis, tRNA and rRNA base modification]
IETLGCRVNQYESESLKNQLIQKGYEVVPDEDKADVYIINTCTVTAKADSKARRAIRRARRQNPTAKIIV
TGCYAQSNPKELADLKDVDLVLGNKEKDKINKLLSLGLKTSFYRVKNKNFSREKGVPEYEEVAFEGHTRA
FIKVQDGCNFFCSYCIIPFARGRSRSVPMEAILKQVKILVAKGYKEIVLTGVNLGSYGDDLKNGTSLAKL
LEQILQIPGIKRIRLSSIDPEDIDEELLEAIASEKRLCPHLHLSLQSGSDRVLKRMRRKYTRDDFLKLVN
KLRSVRPDYAFGTDIIVGFPGESEEDFQETLRMVKEIEFSHLHIFPYSARPGTPASTMKDKVPETIKKER
VKRLKELAEKNYQEFLKKNIGKELEVLVEKEKAGVLTGYSEYYLKVKVESDKGVAAGELISVRI
>gnl|CDD|162434 TIGR01580, Respiratory_nitrate_reductase_1_alpha_chain, respiratory nitrate reductase, alpha subunit. The Nitrate reductase enzyme complex allows bacteria to use nitrate as an electron acceptor during anaerobic growth. The enzyme complex consists of a tetramer that has an alpha, beta and 2 gamma subunits. The alpha and beta subunits have catalytic activity and the gamma subunits attach the enzyme to the membrane and is a b-type cytochrome that receives electrons from the quinone pool and transfers them to the beta subunit. This model is specific for the alpha subunit for nitrate reductase I (narG) and nitrate reductase II (narZ) for gram positive and gram negative bacteria.A few thermophiles and archaea also match the model The seed members used to make the model include Nitrate reductases from Pseudomonas fluorescens (GP:11344601), E.coli (SP:P09152) and B.subtilis (SP:P42175). All seed members are experimentally characterized. Some unpublished nitrate reductases, that are shorter sequences, and probably fragments fall in between the noise and trusted cutoffs. Pfam models pfam00384 (Molybdopterin oxidoreductase) and pfam01568(Molydopterin dinucleotide binding domain) will also match the nitrate reductase, alpha subunit [Energy metabolism, Anaerobic]
SKLLDRLRYFKQKGETFSDGHGQTLNENRDWENVYRQRWQYDKIVRSTHGVNCTGSCSWKIYVKNGLVTW
ETQQTDYPRTRPDLPNHEPRGCPRGASYSWYIYSANRLKYPMMRKRLMKLWREAKQTHSDPVEAWASIVE
NADKAKSYKQARGRGGFVRSSWQEVNELIAASNVYTVKNYGPDRVVGFSPIPAMSMVSYASGSRYLSLIG
GTCLSFYDWYCDLPPASPQTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAI
TPDYAEIAKLCDLWLAPKQGTDAALALAMGHVILREFHLDNPSQYFTEYAKRYTDMPMLVMLEERDGYYA
AGRFLRAADLVDALGQENNPEWKTVAFDTNGEMVAPQGSIGFRWGEKGKWNLEQRDGKTGEEIELQLSLL
GSQDEIAEVGFPYFGGDGTEHFNKVEGENVLLRKLPVKRLQLADGSTALVTTVFDLTLANYGLERGLGDV
NCATSYDDVKAYTPAWQEQITGVSREQIIRIAREFADNADKTHGRSMIIVGAGLNHWYHLDMNYRGLINM
LILCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPPRHMNGTSFFYNHSSQWRYETVTAEDLLS
PMADKSRYTGHLIDYNVRAERMGWLPSAPQLNTNPLTIAGEAEKAGMNPVDYVVKSLQEGSLRFAAEQPD
NGVNFPRNLFIWRSNLLGSSGKGHEYMLKYLLGTENGIMNKDLGQQGGVKPEEVDWQDNGLEGKLDLVVT
LDFRMSSTCLYSDIVLPTATWYEKDDMNTSDMHPFIHPLSAAIDPAWESKSDWEIYKAIAKAFSEVCVGH
LGKEKDIVTLPLQHDSAAELAQPFGVKDWKKGECDLIPGKTAPNIQVVERDYPAIYERFTSLGPLMEKIG
NGGKGIAWNTQSEMDLLRKLNYTKAEGSPAKGQPMINTAIDAAEMILTLAPETNGQVAVKAWAALSEFTG
RDHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNVHELIPWRTLTGRQQLYQDHQ
WMRDFGESLLVYRPPIDTRSFKEVIGQKSNGNQEIVLNFLTPHQKWGIHSTYSDNLLMLTLGRGGPVVWL
SEADAKDLGIADNDWIECFNSNGALTARAVVSQRVPAGMTMMYHAQERIVNVPGSEITQQRGGIHNSVTR
ITPKPTHMIGGYAQLAYGFNYYGTVGSNRDEFVVVRKMKNVDWLD
>gnl|CDD|130643 TIGR01581, Molybdenum_transport_system_permease_protein_modB., NifC-like ABC-type porter. This model describes a clade of ABC porter genes with relatively weak homology compared to its neighbor clades, the molybdate (TIGR02141) and sulfate (TIGR00969) porters. Neighbor-Joining, PAM-distance phylogenetic trees support the separation of the clades in this way. Included in this group is a gene designated NifC in Clostridium pasturianum. It would be reasonable to presume that NifC acts as a molybdate porter since the most common form of nitrogenase is a molybdoenzyme. Several other sequences falling within the scope of this model are annotated as molybdate porters and one, from Halobacterium, is annotated as a sulfate porter. There is presently no experimental evidence to support annotations with this degree of specificity
LIRRLGGSHILSALTDPENIKALRLSLATSLASLLLAVIIGIPTAYVLARVRFPLKKLLDTLLDLPMVLP
PLVAGLALLLLFGRNGLLGPYLEAAGIQVIFSTLGVVLAQTFVASPYYVRVARSTFKSVDPRYEDVARSL
GAGPLETFRKITLPMARPGLLAGLVLAWARALGEFGATLMFAGSIQGKTRTLPLAIYLNIQSDNIEAAVA
SALLLLVIAFLLLLV
>gnl|CDD|273705 TIGR01582, Formate_dehydrogenase_iron-sulfur_subunit, formate dehydrogenase, beta subunit, Fe-S containing. This model represents the beta subunit of the gamma-proteobacterial formate dehydrogenase. This subunit contains four 4Fe-4S clusters and is involved in transmitting electrons from the alpha subunit (TIGR01553) at the periplasmic space to the gamma subunit which spans the cytoplasmic membrane. In addition to the gamma proteobacteria, a sequence from Aquifex aolicus falls within the scope of this model. This appears to be the case for the alpha, gamma and epsilon (accessory protein TIGR01562) chains as well [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]
DIKRLSATKEPDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTPPILSRKVGGYQNPPDLLPETF
TLMRFKEGEESDGLEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNI
PRYDKVDNRPYKCTLCIDRVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPP
GVGGTHVMYVLHHGDKPKDYQDLPEDPRIDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPNKVLGG
KEE
>gnl|CDD|130645 TIGR01583, Formate_dehydrogenase_cytochrome_b556_subunit, formate dehydrogenase, gamma subunit. This model represents the gamma chain of the gamma proteobacteria (and Aquifex aolicus) formate dehydrogenase. This subunit is integral to the cytoplasmic membrane, consisting of 4 transmembrane helices, and receives electrons from the beta subunit. The entire E. coli formate dehydrogenase N (nitrate-inducible form) has been crystallized. The gamma subunit contains two cytochromes, heme b(P) and heme b(C) near the periplasmic and cytoplasmic sides of the membrane respectively. The electron acceptor quinone binds at the cytoplasmic heme histidine ligand. NiFe-hydrogenase and thiosulfate reductase contain homologous gamma subunits, and these can be found scoring in the noise of this model [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]
KIYRFSLFDRILHWIAAISFLILVFTGFVMMFGKFFWLGVILGELWVAKNLHPFAGILFFISIIPMFLKW
WRRMIPAKYDIRWMMKVGGYLSKIKRPVPSAGKYNAGQKSWYWILVLGGFLMIITGIFMWFLDFPSTAFS
IELLRISALIHNFSAIILAVGFIVHIYMAVFGVKGSIHGMVSGKVEETWAKIHHPYWYREVVNR
>gnl|CDD|130646 TIGR01584, Citrate_lyase_alpha_chain, citrate lyase, alpha subunit. This is a model of the alpha subunit of the holoenzyme citrate lyase (EC 4.1.3.6) composed of alpha (EC 2.8.3.10), beta (EC 4.1.3.34), and acyl carrier protein subunits in a stoichiometric relationship of 6:6:6. Citrate lyase is an enzyme which converts citrate to oxaloacetate. In bacteria, this reaction is involved in citrate fermentation. The alpha subunit catalyzes the reaction Acetyl-CoA + citrate = acetate + (3S)-citryl-CoA. The seed contains an experimentally characterized member from Lactococcus lactis subsp. lactis. The model covers both Gram positive and Gram negative bacteria. It is quite robust with queries scoring either quite well or quite poorly against the model. There are currently no hits in between the noise cutoff and trusted cutoff [Energy metabolism, Fermentation]
KSVEAKDPKINRVGAKVRQRVKKPNKLVDSLEEAIKKTGLKDGMTISFHHHFREGDYVVNMVMRIIADMG
FKDLTLAPSSLTSVHDPLVEHIKKGVVTGITSSGLRGTLGDEISKGILKKPVIIRSHGGRARAIETGELH
IDVAFLGVPCCDEMGNANGMTGKSPCGSLGYAIVDAQYADKVVAITDSLVPYPNTPASIKQTQVDYVVKV
DAVGDPKKIGSGATRFTKDPKELLIAKMANDVIVNSGYFKDGFSFQTGTGGAALAVTRFLKEKMIDHNIK
ASFGLGGITKQMVDLHEEGLIDKLFDVQSFDLGAAESIALNPNHQEIDASWYANPANKGAMVNKLDVVIL
SALEIDTKFNVNVMTGSDGVIRGASGGHQDTAAGAKLSIIVAPLVRGRIPTVVEKVTTVITPGESIDVLV
TEIGIAINPKRKDLIEKLSNKPGIPLYTIEELQEIAEEITGKPEPIEFTDKVVAVVEYRDGSIIDVIRKV
KD
>gnl|CDD|273706 TIGR01586, Cysteine_protease_avirulence_protein_AvrPphB, cysteine protease domain, YopT-type. The model represents a cysteine protease domain found in proteins of bacteria that include plant pathogens (Pseudomonas syringae), root nodule bacteria, and intracellular pathogens (e.g. Yersinia pestis, Haemophilus ducreyi, Pasteurella multocida, Chlamydia trachomatis) of animal hosts. The domain features a catalytic triad of Cys, His, and Asp. Sequences can be extremely divergent outside of a few well-conserved motifs, and additional members may exist that are detected by this model. YopT, a virulence effector protein of Yersinia pestis, cleaves and releases host cell Rho GTPases from the membrane, thereby disrupting the actin cytoskeleton. Members of the family from pathogenic bacteria are likely to be pathogenesis factors [Cellular processes, Pathogenesis]
LFRHPQAALYDRNQSGRCMGLSALWLRMRDAAQASYRMEHLDTGGQGDAHASERHQSYEQLQYSLLLQDA
APPDFALIDTWLQKQGLSPLGLEKVFHARSWSAQEGITVLTKAALDTGKDLLGLRFANLSGSAHALALSQ
QGGSFTFFDPNFGEFDFPSLEAALEWMAQLFKNLSGYYGSPSQRQQLASVVNYKVH
>gnl|CDD|273707 TIGR01587, CRISPR-associated_endonuclease/helicase_Cas3, CRISPR-associated helicase Cas3. This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model
LLVIEAPTGYGKTEAALLWALHSIKSQKADRVIIALPTRATINAMYRRAKELFGSELVGLHHSSSFSRIK
EMGDSEEFEHLFPLYIHSNDKLFLDPITVCTIDQVLKSVFGEFGHYEFTLASIANSLLIFDEVHFYDEYT
LALILAVLEVLKDNDVPILLMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVGEIS
SLERLLEFIKKGGSIAIIVNTVDRAQEFYQQLKEKAPEEEIILYHSRFTEKDRAKKEAELLREMKKSNEK
FVIVATQVIEASLDISADVMITELAPIDSLIQRLGRLHRYGRKIGENFEVYIITIAPEGKLFPYPYELVE
RTIQKLEES
>gnl|CDD|130649 TIGR01588, Citrate_lyase_subunit_beta, citrate lyase, beta subunit. This is a model of the beta subunit of the holoenzyme citrate lyase (EC 4.1.3.6) composed of alpha (EC 2.8.3.10), beta (EC 4.1.3.34), and acyl carrier protein subunits in a stoichiometric relationship of 6:6:6. Citrate lyase is an enzyme which converts citrate to oxaloacetate. In bacteria, this reaction is involved in citrate fermentation. The beta subunit catalyzes the reaction (3S)-citryl-CoA = acetyl-CoA + oxaloacetate. The seed contains an experimentally characterized member from Leuconostoc mesenteroides. The model covers a wide range of Gram positive bacteria. For Gram negative bacteria, it appears that only gamma proteobacteria hit this model. The model is quite robust with queries scoring either quite well or quite poorly against the model. There are currently no hits in-between the noise cutoff and trusted cutoff [Energy metabolism, Fermentation]
RLRRTMMFVPGNNPAMISDAFIYGADSVMFDLEDAVSLAEKDSARLLVYEALQTPDYGDTETVVRINGLD
TPFGLADIKAVVKAGVDVVRLPKTDTAEDIHELEKLIERIEKEIGREVGSTKLMAAIESALGVVNAVEIA
RASKRLMGIALGAEDYVTDMKTSRSPDGTELFYARCAILHAARAAGIAAFDTVYSDVNNEEGFLAEAQLI
KQLGFDGKSLINPRQIELVHKVYAPTEKEIDKAIEVIAAAEEAETKGSGVISLNGKMVDGPIIDRAQRVL
ALAKASGI
>gnl|CDD|130650 TIGR01589, hypothetical_protein_partial, uncharacterized plant-specific domain TIGR01589. This model represents an uncharacterized plant-specific domain 57 residues in length. It is found toward the N-terminus of most proteins that contain it. Examples include at least 10 proteins from Arabidopsis thaliana and at least one from Oryza sativa
IDLVQNRIETCIQGYMSKEETVSFLFENAGISPKFTRFVWYLLEKENADFFRCYKTH
>gnl|CDD|130651 TIGR01590, yir-bir-cir_Pla, yir/bir/cir-family of variant antigens, Plasmodium-specific. This model represents a large paralogous family of variant antigens from several Plasmodium species (P. yoelii, P. berghei and P. chabaudi). The seed was generated from a list of ORF's in P. yoelii containing a paralagous domain as defined by an algorithm implemented at TIFR. The list was aligned and reduced to six sequences approximating the most divergent clades present in the data set. The model only hits genes previously characterized as yir, bir, or cir genes above the trusted cutoff. In between trusted and noise is one gene from P. vivax (vir25) which has been characterized as a distant relative of the yir/bir/cir family. The vir family appears to be present in 600-1000 copies per haploid genome and is preferentially located in the sub-telomeric regions of the chromosomes. The genomic data for yoelii is consistent with this observation. It is not believed that there are any orthologs of this family in P. falciparum
DELDKSEEYYFKNGKSIKNYCPKTGSNCDNDIDKINAGCLWLLNQLYGISKDFKYKNNNNKAFIEYIIIW
LSYILNQKRQNGITKLNDFYTKHIKNNAEYDNFISTNEKYKNYKDVIDKKKDLMNINIKDISKFYDAFKL
LCNMHTEINKSNSNCNEYLKDANEFVNKYTKLNNDYSNIEGSSYNKILSVLSTDYDKFK
>gnl|CDD|130652 TIGR01591, Formate_dehydrogenase_subunit_alpha, formate dehydrogenase, alpha subunit, archaeal-type. This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related
TVCPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIREGDKFREVSW
DEAISYIAEKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQT
VGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPG
TDIALLNAMANVIIEEGLYDKAFIEKRTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSA
AILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGALPDFLPGYQPVSDEE
VREKFAKAWGVVKLPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIF
MTETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEIIQELANALGLDWNYNHPQEI
MDEIRELTPLFAGLTYERLDELGSLQWPCNDSDASPTSYLYKDKFATPDGKAKFIPLEWVAPIEEPDDEY
PLILTTGRVLTHYNVGEMTRRVAGLRRLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLRAKVSDR
VNKGAIYITMHFWDGAVNNLTTDDLDPISGTPEYKYTAVRI
>gnl|CDD|130653 TIGR01592, Uncharacterized_9.5_kDa_protein_in_ORF3_5'region, holin, SPP1 family. This model represents one of more than 30 families of phage proteins, all lacking detectable homology with each other, known or believed to act as holins. Holins act in cell lysis by bacteriophage. Members of this family are found in phage PBSX and phage SPP1, among others [Mobile and extrachromosomal element functions, Prophage functions]
MDAGTIVRTILLIIALVNQFLAMKGISPIPVDEEGISTVVDAVFTIGVSLWTWWKNNYITRKGKKQKQKL
KKYKL
>gnl|CDD|273708 TIGR01593, Uncharacterized_protein_CPE0383, toxin secretion/phage lysis holin. This model describes one of the many mutally dissimilar families of holins, phage proteins that act together with lytic enzymes in bacterial lysis. This family includes, besides phage holins, the protein TcdE/UtxA involved in toxin secretion in Clostridium difficile and related species [Protein fate, Protein and peptide secretion and trafficking, Mobile and extrachromosomal element functions, Prophage functions]
FEFLGSVMGTEFGKVDYSLTLLLVLIIIDFITGVLKAWKNKKLSSKKGIKGLVKKLATLILVILAHPFDV
LLPTNGFMLLLVIYNFYILNESLSILENLALLGVKVPEMLVDILETLKNKTKEKKKKD
>gnl|CDD|273709 TIGR01594, Uncharacterized_protein_HI_1416, phage holin, lambda family. This model represents one of a large number of mutally dissimilar families of phage holins. Holins act against the host cell membrane to allow lytic enzymes of the phage to reach the bacterial cell wall. This family includes the product of the S gene of phage lambda [Mobile and extrachromosomal element functions, Prophage functions]
MMIKEPDLWAALLSWLQDAWRSQGQGALLALAIAYLRIRYMGGKFKRKLIDALMCAAIALVAASALDFLG
LPTSLSPFLGGMIGFVGVDKIREFAKRFINKKAGVDD
>gnl|CDD|273710 TIGR01595, cas_CT1132, CRISPR-associated protein, CT1132 family. This protein is found in at least five widely species that contain CRISPR loci. Four cas (CRISPR-associated) proteins that are widely distributed and found near the CRISPR repeats. This protein is found exclusively next to other cas proteins. Its function is unknown
VKNRSEFLVIYDVKWANPNGDPLNGNRPRFDEETGRLFVSDVRIKRKVRDYLQECGDEILVVTKERIEDK
FRSLAKVPEDRVKEAGIKDVNKEEDACQKYIDIRLFGAVITQSKKESSITGPVQFRYAKSLEPVVIMTIQ
GTRAFAGEEAKNQRTMGEKYVVPYALYAFYGVINANSAKFTGFSEEDLSKFLEALWNGFENDRSRSKMEH
NPRLLMRKEGVNYHSGELDYLVKVVFEHESEEGRDISELKLDLTELKQVLESKKDKIERIRYYKDYRVKL
N
>gnl|CDD|273711 TIGR01596, CRISPR-associated_endonuclease_Cas3-HD, CRISPR-associated endonuclease Cas3-HD. CRISPR/Cas systems are widespread, mobile systems for host defense against invasive elements such as phage. In these systems, Cas3 designates one of the core proteins shared widely by multiple types of CRISPR/Cas system. This model represents an HD-like endonuclease that occurs either separately or as the N-terminal region of Cas3, the helicase-containing CRISPR-associated protein
LKEHLLDVAAVAEALPALRPRLAEKLGLELRELLKLAGLLHDLGKASPAFQKKLRKAEERGDRGEVRHST
LSAALLYDLLEELGLEEELALLLALAIAGHHGGLIDDDDLEELLELLERELEEALGELLEELEELLDEVL
KALPLRLLLDKEEPIELYLLARLLFGLLVDADWLAS
>gnl|CDD|130658 TIGR01597, PYST-B, Plasmodium yoelii subtelomeric family PYST-B. This model represents a paralogous family of Plasmodium yoelii genes preferentially located in the subtelomeric regions of the chromosomes. There are no obvious homologs to these genes in any other organism
MRVSILKFVFFSIIICSFEYAKNELYLVNERTICFERNIKIFRNNRILADADNQFDLNEFYQSTLSLANQ
FNDCNDDDKEIAHLRNIIDSHIKKHKERNTLPDLNNVDKKTKKLINKLQKELEELKKELDNEMNDELTIQ
PIHDKIIIKKDENNSVSEHEDFKQLENEKNSSVSEHEEFDIASSDNLKIKRKLKKLVKKLIVRCLTFIVI
VCSILVSGPVYLLALIIPSLISIYWSIWRFQYVKLYRTKLKNISK
>gnl|CDD|130659 TIGR01598, holin_phiLC3, holin, phage phi LC3 family. Phage proteins for bacterial lysis typically include a membrane-disrupting protein, or holin, and one or more cell wall degrading enzymes that reach the cell wall because of holin action. Holins are found in a large number of mutually non-homologous families [Mobile and extrachromosomal element functions, Prophage functions]
INWKVRLKNKATLIALLGALFLAIQSILDNFGVLWLSFNRQLNAPIAAITTILAVVGIIMDPTTSGLSDS
LRVQNYSE
>gnl|CDD|273712 TIGR01599, 93_kDa_protein, Plasmodium yoelii subtelomeric family PYST-A. This model represents a paralogous family of Plasmodium yoelii genes preferentially located in the subtelomeric regions of the chromosomes. Members of this family are expressed in both the Sporozoite and Gametozoite life stages. A single high-scoring gene was identified in the complete genome of P. falciparum as well as a single gene from P. chaboudi from GenBank which were included in the seed. There are no obvious homologs to these genes in any non-Plasmodium organism. These observations suggest an expansion of this family in yoelii from a common Plasmodium ancestor gene (present in a single copy in falciparum)
EKKPHLVCTDPKEIKRAEEIMEEAELRLKRHAINKNDYNLYSTPNPDSTVYYKKDHNTIIGKIHLTIQDP
NKYDAIIKTLWDFNDNKKFGRKFIKGKVVRVYSPNLIMIQQRYKDASGSPNKYFYALATKVKVSEDTTII
ACTSANINDHNKVDKKNFKNKIIESANSFKTDIDSEEDIRNGELKKMFVNLSGFIIKKKDDNIDITYV
>gnl|CDD|130661 TIGR01600, lambda_minor_tail, lambda-like phage minor tail protein L. This model detects members of the family of phage lambda minor tail protein L. This model was built as a fragment model to allow detection of fragmentary sequences, as might be found in cryptic prophage regions [Mobile and extrachromosomal element functions, Prophage functions]
DIQKLEPSALVELFELDLTAQGGERLFFHNELNEKGEAVTWQGRQYQPWPIDASGFEMTGQGSSPRPSLT
VSNLFGLVSAMAEDLDSLVGATVVRRRTLARFLDAVNFVAGNPEADPEQELPTERWFVEQKTSETAETVE
FELSSPTDTDGVQLPGRQILANTCMWDKYRGPECGYTGPAVFDEFDNPTTDIRKDRCSKRMRSCEMRFFA
NMVANFGGFLSANKL
>gnl|CDD|213640 TIGR01601, PYST-C1, Plasmodium yoelii subtelomeric domain PYST-C1. This model represents the N-terminal domain of a paralogous family of Plasmodium yoelii genes preferentially located in the subtelomeric regions of the chromosomes. There are no obvious homologs to these genes in any other organism. The C-terminal portions of the genes which contain this domain are divergent and some contain other yoelii-specific paralogous domains such as PYST-C2 (TIGR01604)
MNKRIFSLVCIVLYILLAVSIHCSEQKVSGVGNKSICGIKEINRSNEKNDIETKSEIQLNNNNPKDDIDD
KDNPQKDDKDNK
>gnl|CDD|130663 TIGR01602, PY-rept-46, Plasmodium yoelii repeat of length 46. This repeat is found in only 2 genes in Plasmodium yoelii, in each of these genes it is repeated 9 times. It is found in no other organism
KSKRSRFPTMFKKDKKDKEDKDANGSQESLNIDKSLESLNDDGDDN
>gnl|CDD|273713 TIGR01603, Uncharacterized_phage_related_protein, phage major tail protein, phi13 family. This model describes a set of proteins that share low levels of sequence similarity but similar lengths and similar patterns of charged, hydrophobic, and Gly/Pro residues. All members (except one attributed to mouse embryo cDNA) belong to phage of Gram-positive bacteria. Several are identified as phage major tail proteins. Some members of this family have additional C-terminal regions of about 100 residues not included in this model [Mobile and extrachromosomal element functions, Prophage functions]
KVAIGLENLYYAVLDSTAGVFTYETPKKLGGLKEAKVEPKGELVTAYADDIVYYQARNNGGTKVETELID
IPSDQRKFLLGEKLGSDGVLKYGKDDKPPEVAVLFEAPNTVGKNRYVGLYKGKFTPPDIDYKTKEGKPDF
SDDKVSGTAQPREEDEKKGQVEKYAFDCAEGEGEGINNNWLKQVLEPKKG
>gnl|CDD|130665 TIGR01604, PYST-C2, Plasmodium yoelii subtelomeric domain PYST-C2. This model represents a domain of a paralogous family of Plasmodium yoelii genes preferentially located in the subtelomeric regions of the chromosomes. There are no obvious homologs to these genes in any other organism. The genes found by this model often are associated with an N-terminal domain yoelii-specific domain such as PYST-C1 (TIGR01601)
VPLTILLNQTIQSFSNNEDLPKVVKKNGNVHDEYELKDQKHLEIYLNLNEKFEHRSSNENSLEPDYTLGS
DTIKELSNNKKSECLNCFIFKKEKKEKKSSNNNGSPSKVTLLVGNVPHSIPVQSPEHYQFLLNLKERLEN
YHPSNLKLNE
>gnl|CDD|130666 TIGR01605, PYST-D, Plasmodium yoelii subtelomeric family PYST-D. This model represents a paralogous family of Plasmodium yoelii genes preferentially located in the subtelomeric regions of the chromosomes. These genes are generally very short (ca. 50 residues). There are no obvious homologs to these genes in any other organism
LWVSIVFLEPIFGLGLSITLHLIFYNSNTNIIYVFSRMFNQKMVRKNENEDPYGK
>gnl|CDD|200119 TIGR01606, holin_BlyA, holin, BlyA family. This family represents a BlyA, a small holin found in Borrelia circular plasmids that prove to be temperate phage. This protein was previously proposed to be an hemolysin. BlyA is small (67 residues) and contains two largely hydrophobic helices and a highly charged C-terminus [Mobile and extrachromosomal element functions, Prophage functions]
MDTISINDFLLQLINIKLIKLMIFISIFILSLGLIFKPVIKDMLSILISKIKKNDNDKEKEDL
>gnl|CDD|162444 TIGR01607, PST-A, Plasmodium subtelomeric family (PST-A). This model represents a paralogous family of genes in Plasmodium falciparum and Plasmodium yoelii, which are closely related to various phospholipases and lysophospholipases of plants as well as generally being related to the alpha/beta-fold superfamily of hydrolases. These genes are preferentially located in the subtelomeric regions of the chromosomes of both P. falciparum and P. yoelii
SFRNKDGLLLKTYSWIVKNAIGIIVLIHGLKSHLRLQFLKINAKIVNNDRAVLIDTDNYYIYKDSWIENF
NKNGYSVYGLDLQGHGESDGLQNLRGHINCFDDLVYDVIQYMNRINDSIILENETKSDDESYDIVNTKEN
RLPMYIIGLSMGGNIALRLLELLGKSNENNDKLNIKGCISLSGMISIKSVGSDDSFKFKYFYLPVMNFMS
RVFPTFRISKKIRYEKSPYVNDIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIPKDIPILFIHSKG
DCVCSYEGTVSFYNKLSISNKELHTLEDMDHVITIEPGNEEVLKKIIEWISN
>gnl|CDD|130669 TIGR01608, Citrate_lyase_acyl_carrier_protein, citrate lyase acyl carrier protein. This is a model of the acyl carrier protein (aka gamma subunit) of the holoenzyme citrate lyase (EC 4.1.3.6) composed of alpha (EC 2.8.3.10), beta (EC 4.1.3.34), and acyl carrier protein subunits in a stoichiometric relationship of 6:6:6. Citrate lyase is an enzyme which converts citrate to oxaloacetate. In bacteria, this reaction is involved in citrate fermentation. The acyl carrier protein covalently binds the coenzyme of citrate lyase. The seed contains an experimentally characterized member from Leuconostoc mesenteroides. The model covers a wide range of Gram positive bacteria. For Gram negative bacteria, it appears that only gamma proteobacteria hit this model. The model is quite robust with queries scoring either quite well or quite poorly against the model. There are currently no hits in-between the noise cutoff and trusted cutoff [Energy metabolism, Fermentation]
MEIKKTALAGTLESSDVMIMVEPAMQVGIEIDLVSDVKKQFGDDIESTVKETLKLLGVENAVVKVVDKGA
LNCVIKARTLAAVQRAAEANDP
>gnl|CDD|273714 TIGR01609, Plasmodium_exported_protein_hyp11_unknown_function, Plasmodium falciparum uncharacterized protein TIGR01609. This model represents a family of at least four proteins in Plasmodium falciparum. An interesting feature is five perfectly conserved Trp residues
IRNERILSEQHDQKNDWRNEFSLVINEEELKNIPEEDQLGEQQEPEYIYKLNELCKNASKYWKNAIKDME
EEYKELTDYMDHNWRDDMWNREWVKYLRRVHGHINSDLNDPSLTLVDKEYIVNIWITWTREDFEFFLEYL
KEEWED
>gnl|CDD|273715 TIGR01610, Replication_protein_15, phage replication protein O, N-terminal domain. This model represents the N-terminal region of the phage lambda replication protein O and homologous regions of other phage proteins [DNA metabolism, DNA replication, recombination, and repair, Mobile and extrachromosomal element functions, Prophage functions]
ADLSNGYTRMANELQEALPGADLSGREFRVLLAIIRLTYGWNKKQDRVTATVIAELTGLSRTHVSDAIKS
LARRRIIFRQGMMGIVGVNTPLSEW
>gnl|CDD|130672 TIGR01611, tail_tube, phage contractile tail tube protein, P2 family. The tails of some phage are contractile. This model represents the tail tube, or tail core, protein of the contractile tail of phage P2, and homologous proteins from additional phage [Mobile and extrachromosomal element functions, Prophage functions]
AEPNRLTNANLFIDGVNLAGRVEEINLPKLAMKTEEYRAGGMVGPVELDMGFEKLEGEISWNGYRREALS
AFGPTKSLALNCRFRGRYSSQDLGDEIPLVIFLRGMFKEIDLGTWKAGEKAEFKSAFALTYYKQVVDGEE
LLELDYVNNIFRVNGVDQLADYRNAIGL
>gnl|CDD|130673 TIGR01612, 235kDa-fam, reticulocyte binding/rhoptry protein. This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii
MKKFIYITTTYIVLFTSLEIIYGKKIETEKKNHDAQLNNFYLYHNLEGINFNDSNSSNEEQYNNKNDAIN
DQKFIQPHSITYFENQKDTANDKIILYNDYTIKNDFDAFKIFNNDNEKTDRKATIVKNSFIQKSNAPRFD
PDIYNEIDIIYGASGPNENLEFFYAKLQFCQDLRTFDNKGYSNAKKLLDIILNKLKQIDKDIIAIIKECE
PLKTNIIGEMSKIHDPLYEFYKEPIHDDYNPYEISKKDYVDCIIPRFKKLAPIIDAAISSLKLEYDHLCY
YEYWDIDAAYKEHAAITHEHIDAELNDIKKHPMINDKELRPHGKRLIKILESEGEQGHIINKLIFLEKEF
EDTIHKSDIYKDECLSNHLFMEDYLKDDKISPYYYEFLEEIKKIAKQRAIFFYNAKKLKHLEILYKHQED
ILNNFHKTIERLIFEKPDPNNNNIFKDDFDEFNKPIPKSKLKALEKRFFEIFEEEWGSYDIKKDIDENSK
QDNTVKLILMRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQNIKAKLYKEIEAGLKESYELAKNWKKLI
HEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKNEYIKKAIDLKKIIE
NNNAYIDELAKISPYQVPEHLKNKDKIYSTIKSELSKIYEDDIDALYNELSSIVKENAIDNTEDKAKLDD
LKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNK
INDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFM
KDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEY
QNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELD
KAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIH
TSIYNIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDDI
KNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYD
EIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSP
EIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKN
LLDAQKHNSDINLYLNEIANIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDIN
LEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHIL
KIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFA
KTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFL
KISDIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELD
SEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEE
YNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTRINAQNEFLKIIEIEKKSKSYLDDIEAKEFD
RIINHFKKKLDHVNDKFTKEYSKINEGFDDISKSIENVKNSTDENLLFDILNKTKDAYAGIIGKKYYSYK
DEAEKIFINISKLANSINIQIQNNSGIDLFDNINIAILSSLDSEKEDTLKFIPSPEKEPEIYTKIRDSYD
TLLDIFKKSQDLHKKEQDTLNIIFENQQLYEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDELNKL
SCDSQNYDTILELSKQDKIKEKIDNYEKEKEKFGIDFDVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDF
SEEKDNIIQSKKKLKELTEAFNTEIKIIEDKIIEKNDLIDKLIEMRKECLLFSYATLVETLKSKVINHSE
FITSAAKFSKDFFEFIEDISDSLNDDIDALQIKYNLNQTKKHMISILADATKDHNNLIEKEKEATKIINN
LTELFTIDFNNADADILHNNKIQIIYFNSELHKSIESIKKLYKKINAFKLLNISHINEKYFDISKEFDNI
IQLQKHKLTENLNDLKEIDQYISDKKNIFLHALNENTNFNFNALKEIYDDIINRENKADEIENINNKENE
NIMQYIDTITKLTEKIQDILIFVTTYENDNNIIKQHIQDNDENDVSKIKDNLKKTIQSFQEILNKIDEIK
AQFYGGNNINNIIITISQNANDVKNHFSKDLTIENELIQIQKRLEDIKNAAHEIRSEQITKYTNAIHNHI
EEQFKKIENNSNKDEVYKINEIDNIIEKIINYNKEPEVKLHAIIDNKNEFASIIPDIKNLIALIESEYGN
NNNISYKVAIKHEEDANNIILDLNKSQNILNHLIHKNKKIIEDLGNIKHGIHNNNNLHTINKHEEISKIK
HPNNTSHNNNDDAKYKNHHHSNSDEKGSSKTKIAGDSIKFAGAIGFGLVACYAIAIFKKKDDKNEIDLDN
DEKFCGEGEIIYFERDDEIIEIDINED
>gnl|CDD|273716 TIGR01613, putative_primase, phage/plasmid primase, P4 family, C-terminal domain. This model represents a clade within a larger family of proteins from viruses of bacteria and animals. Members of this family are found in phage and plasmids of bacteria and archaea only. The model describes a domain of about 300 residues, found generally toward the protein C-terminus [DNA metabolism, DNA replication, recombination, and repair, Mobile and extrachromosomal element functions, Prophage functions]
YKLNVANGVYDLRTGQLEPHDPDEIHTRKITTEYDPKADCPTWNGFLLETFGGDNELIEYLQRVIGYSLT
GNYTEQKLFFLYGNGGNGKSTFQNLLSNLLGDYAITAVASLKMNELSEHRFGLARLEGKRAVIGDEVQKG
YRDDESTFKSLTGGDTITARFKNKDPFEFTPKFTLVQSTNHLPRIRGFDGGIKRRLRIIPFTKVFPGEKK
NKALKEDYINEKDVILYWAVEGIRLDQRIGDFSIPKAVLEATEEYKEENDVVARFLEECCDDSEGEKVPV
RFVYEAYKEWCEEGGYPILSRNKF
>gnl|CDD|273717 TIGR01614, unnamed_protein_product, pectinesterase inhibitor domain. This model describes a plant domain of about 200 amino acids, characterized by four conserved Cys residues, shown in a pectinesterase inhibitor from Kiwi to form two disulfide bonds: first to second and third to fourth. Roughly half the members of this family have the region described by this model followed immediately by a pectinesterase domain, pfam01095. This suggests that the pairing of the enzymatic domain and its inhibitor reflects a conserved regulatory mechanism for this enzyme family
MASSLSLLLFLLLLSLVATSSSNSLNATQSLIKRICKKTEYPNFCISTLKSDPSSAKADLQGLANISVSA
ALSNASDTLDHISKLLLTKGDPRDKSALEDCVELYSDAVDALDKALASLKSKDYSDAETWLSSALTDPST
CEDGFEELGGIVKSPLTKRNNNVKKLSSITLAIIKMLT
>gnl|CDD|273718 TIGR01615, unknown_protein, uncharacterized plant-specific domain TIGR01615. This model represents a domain found toward the C-terminus of a number of uncharacterized plant proteins. The domain is strongly conserved (greater than 30 % sequence identity between most pairs of members) but flanked by highly divergent regions including stretches of low-complexity sequence
RRIVMSLLRSLGYDAAICKSKWDSSGDIPAGKYEYIDVVDGDGSKKQEMRVIIDLDFRSEFEIARPTEEY
KRLLESLPEVFVGTTERLRQLVRLMCDAAKKSLKKKGMPLPPWRKNRYMQSKWLGPYKRTS
>gnl|CDD|273719 TIGR01616, Uncharacterized_15.7_kDa_protein_in_draG_3'region, nitrogenase-associated protein. This model describes a small family of uncharacterized proteins found so far in alpha and gamma proteobacteria and in Nostoc sp. PCC 7120, a cyanobacterium. The gene for this protein is associated with nitrogenase genes. This family shows sequence similarity to TIGR00014, a glutaredoxin-dependent arsenate reductase that converts arsentate to arsenite for disposal. This family is one of several included in pfam03960 [Unknown function, General]
ATIIFYEKPGCANNARQKAALKASGHDVEVQDILKEPWHADTLRPYFGNKPVGSWFNRAAPRVKSGEVNP
DSIDEASALALMVSDPLLIRRPLMDLGGIRCAGFDREPVLSWIGLQTQEHGDLEGC
>gnl|CDD|273720 TIGR01617, Uncharacterized_protein_UU176, transcriptional regulator, Spx/MgsR family. This model represents a portion of the proteins within the larger set covered by pfam03960. That larger family includes a glutaredoxin-dependent arsenate reductase (TIGR00014). Characterized members of this family include Spx and MgsR from Bacillus subtili. Spx is a global regulator for response to thiol-specific oxidative stress. It interacts with RNA polymerase. MgsR (modulator of the general stress response, also called YqgZ) provides a second level of regulation for more than a third of the proteins in the B. subtilis general stress regulon controlled by Sigma-B [Regulatory functions, DNA interactions]
IKVYGSPNCTTCKKARRWLEANGIEYQFIDIGEDGPTREELLDILSLLEDGIDPLLNTRGQSYRALNTSN
TFLDLSDKEALELLAEDPALLRRPLIVDTKNRLLIGFKSESIEEFKL
>gnl|CDD|130679 TIGR01618, phage_P_loop, phage nucleotide-binding protein. This model represents an uncharacterized family of proteins from a number of phage of Gram-positive bacteria. This protein contains a P-loop motif, G/A-X-X-G-X-G-K-T near its amino end. The function of this protein is unknown [Mobile and extrachromosomal element functions, Prophage functions]
KFIEAGNIKRIPNMYLIYGKPGTGKTSTIKYLPGKTLVLSFDMSSKVLIGDENVDIADHDDMPPIQAMVE
FYVMQNIQAVKYDNIVIDNISALQNLWLENIGRAAKNGQPELQHYQKLDLWFLDLLTVLKESNKNIYATA
WELTNQSSGESGQIYNRYQPDIREKVLNAFLGLTDVVGRIVLNGETGERGFILDPSKGNYAKNRLDNRKL
CKAEELFQTG
>gnl|CDD|130680 TIGR01619, Uncharacterized_protein_HI_0040, TIGR01619 family protein. This model represents a hypothetical equivalog of gamma proteobacteria, includes HI0040. These sequences do not have any similarity to known proteins by PSI-BLAST
DGANWQNYRSTLNDKLAIFSANIEDLEKFHGKGLDHIIQFKFDYAADDENALPDESEYDKLINQIFKILT
QLSALPDTFFAGHFICAGHAKIHFYCDHEELFLETLKQFDEIKAIEIQKDLHWDIYFDFLLASPLEIKIH
ATEELLDLLKKKGRDLAALYLIEHSFHFDEEAKMFAFMDELHLGDISFTSLQYSALAIMFEEDDEPVFLV
KLEQEISLDNSEIFEQVEQFEDIAEQFSGEYAGWECDAI
>gnl|CDD|130681 TIGR01620, Hypothetical_UPF0283_protein_ycjF., TIGR01620 family protein. This model includes putative membrane proteins from alpha and gamma proteobacteria, each making up their own clade. The two clades have less than 25% identity between them. We could not find support for the assignment to the sequence from Brucella (OMNI|NTL01BM0951) of being a GTP-binding protein
APVATALKPKFSFGKLGLGALGVLFGLAFVLQAVQWIRNLFQRSDWLGLTATIALIVIIFAGLALVGREW
RRLMRLNARQSLKADAETASLDKSPKPGRAIVCRLNAVLSGRAETAPGRAAWKETENEVIDGPELIELAE
REVLVPLDAQARALISNSAAESSVVTAVSPLAVVDMAFIAWRNLRLVNAIAELYGIELGYLGRLRLLRDV
LANIAFAGAIEVGDGLGMDWLSQDLAAKLSTRLAQGIGNGLLTARLGIKAMELCRPLPFRAVKKPGLGDF
MSDLTPDVK
>gnl|CDD|130682 TIGR01621, Uncharacterized_RNA_pseudouridine_synthase_HI_0042, pseudouridine synthase Rlu family protein, TIGR01621. This model represents a clade of sequences within the pseudouridine synthase superfamily (pfam00849). The superfamily includes E. coli proteins: RluA, RluB, RluC, RluD, and RsuA. The sequences modeled here are most closely related to RluA. Neisseria, among those species hitting this model, does not appear to have an RluA homolog. It is presumed that these sequences function as pseudouridine synthases, although perhaps with different specificity [Protein synthesis, tRNA and rRNA base modification]
MFEILFTHPDFLLINKHPGISVHKDDGETGLLQEVATQLGVGQVWLVHRLDKMTSGILLLALNAESASEL
SQGFAKRKIEKTYLALSSKKPKKKQGLICGDMEKSRRGSWKLVNSQENPAITRFFSASAATGLRLFILKP
HTGKTHQLRVAMKSLGSPILGDPLYGTTDESDRGYLHAFALRFDYQNEVIQWLCDPRQFQKWHEEAVNQG
IENWLSP
>gnl|CDD|273721 TIGR01622, transcription_coactivator_CAPER, splicing factor, CC1-like family. This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed
RYRDRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSRRPNRRY
RPREKRRRRGDSYRRRRDDRRSRREKPRARDGTPEPLTEDERDRRTVFVQQLAARARERDLYEFFSKVGK
VRDVQIIKDRNSRRSKGVGYVEFYDVDSVQAALALTGQKLLGIPVIVQLSEAEKNRAARAATETSGHHPN
SIPFHRLYVGNLHFNITEQDLRQIFEPFGEIEFVQLQKDPETGRSKGYGFIQFRDAEQAKEALEKMNGFE
LAGRPIKVGLGNDFTPESDANLAQRFQDQDGSAFSGAGLNTPARSQLMRKLARDNEKGTGGLAIPGTDVG
GVNMNNYSRDGLMRKLAPTDEPPAVIPETQILKPKAETSFVPVNVNLASRCLVLSNMFDPATEEEPNWDK
EIEDDVREECSKYGGVVHIYVDDKNSAGDIYLKFDSVQAAEAAIKALNGRYFGGKMITAAFVVDAVYSKS
RLPH
>gnl|CDD|130684 TIGR01623, hypothetical_protein, putative zinc finger domain, LRP1 type. This model represents a putative zinc finger domain found in plants. Arabidopsis thaliana has at least 10 distinct members. Proteins containing this domain, including LRP1, generally share the same size, about 300 amino acids, and architecture. This 43-residue domain, and a more C-terminal companion domain of similar size, appear as tightly conserved islands of sequence similarity. The remainder consists largely of low-complexity sequence. Several animal proteins have regions with matching patterns of Cys, Gly, and His residues. These are not included in the model but score between trusted and noise cutoffs
VCQDCGNQAKKECLFERCRTCCKSRGFHCVTHVKSTWIPAARR
>gnl|CDD|273722 TIGR01624, hypothetical_protein, LRP1 C-terminal domain. This model represents a tightly conserved small domain found in LRP1 and related plant proteins. This family also contains a well-conserved putative zinc finger domain (TIGR01623). The rest of the sequence of most members consists of highly divergent, low-complexity sequence
GFPGEVSAPAVFKCVRVTAIDDGEQAEYAYQATVTIGGHVFKGFLHDQGL
>gnl|CDD|130686 TIGR01625, unnamed_protein_product, AspT/YidE/YbjL antiporter duplication domain. This model represents a domain that is duplicated the aspartate-alanine antiporter AspT, as well as HI0035 of Haemophilus influenzae, YidE and YbjL of E. coli, and a number of other known or putative transporters. Member proteins may have 0, 1, or 2 copies of TrkA potassium uptake domain pfam02080 between the duplications. The domain contains several apparent transmembrane regions and is proposed here to act in transport [Transport and binding proteins, Unknown substrate]
LALGLLLGKIPIGLPGFSIKLGNAGGVLFVGLLLGHFGATGPLTWYIPFSANLFIREFGLMLFLYGVGLS
AGPGFFSSLKDGGGLLRINGGALITVVPTLLVAVALIKLLRINYALTAGMLAGATTNTPALDAANDTLRT
SDLPALGYATVYPL
>gnl|CDD|130687 TIGR01626, Uncharacterized_protein_HI_0045, conserved hypothetical protein YtfJ-family, TIGR01626. This model represents sequences from gamma proteobacteria that are related to the E. coli protein, YtfJ
MKKQILAAVCGVIFPSSAWAHNLQVEQSVPSVGVSEYGEIVLSGKDTVYQPWGSAELAGKVRVVHHIAGR
TSAKEXNASLIDAIKAAKFPPVKYQTTTIINADDAIVGTGMFVKSSAKKGKKENPWSQVVLDDKGAVKNA
WQLNSEDSAIIVLDKTGKVKFVKEGALSDSDIQTVISLVNGLLK
>gnl|CDD|130688 TIGR01627, putative_protein, uncharacterized plant-specific domain TIGR01627. This model represents an uncharacterized domain found in both Arabidopsis thaliana (at least 10 copies) and Oryza sativa. Most member proteins have only a short stretch of sequence N-terminal to this domain, but one has a long N-terminal extension that includes a protein kinase domain (pfam00069)
TTFPLSPADALQHYRASNGPTALMEKELKLLSDVLTRRSPCNILVFGLAHQYLMWSSLNHRGRTVFIEEE
KIMIAKAEVNPPNTRIYSVKYHTKVRNAYNLLQHARANPECRPVMNHQGSSDCKLELRDLPQQVYNTKWD
VIVVDGPRGDDLETPGRMSSIYTAAVLARKGSSGSTTDVFVHDVHRTVEKWLSWEFLCQENLVEANGTLW
HFRIKRQSNASRAFC
>gnl|CDD|130689 TIGR01628, Polyadenylate-binding_protein_3, polyadenylate binding protein, human types 1, 2, 3, 4 family. These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range
ASLYVGDLDPDVTEAKLYDLFKPFGPVLSVRVCRDSVTRRSLGYGYVNFQNPADAERALETMNFKRLGGK
PIRIMWSQRDPSLRRSGVGNIFVKNLDKSVDNKALFDTFSKFGNILSCKVATDENGKSRGYGFVHFEKEE
SAKAAIQKVNGMLLNDKEVYVGRFIKKHEREAAPLKKFTNLYVKNLDPSVNEDKLRELFAKFGEITSAAV
MKDGSGRSRGFAFVNFEKHEDAAKAVEEMNGKKIGLAKEGKKLYVGRAQKRAEREAELRRKFEELQQERK
MKAQGVNLYVKNLDDTVTDEKLRELFSECGEITSAKVMLDEKGVSRGFGFVCFSNPEEANRAVTEMHGRM
LGGKPLYVALAQRKEQRRAHLQDQFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGQPLGWPRMS
MMPTPMGPGGPLRPNGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQN
KKLAQVLASATPQMQKQVLGERLFPLVEAIEPALAAKITGMLLEMDNSELLHLLESPELLKSKVDEALEV
LK
>gnl|CDD|273723 TIGR01629, Replication-associated_protein_G2P, phage/plasmid replication protein, gene II/X family. This model represents a family of phage and plasmid replication proteins. In bacteriophage IKe and related phage, the full-length protein is designated gene II protein. A much shorter protein of unknown function, translated from a conserved in-frame alternative initiator, is designated gene X protein. Members of this family also include plasmid replication proteins. This model is built as a fragment model to better detect translations from alternate intiators and other fragments relative to full length gene II protein [Mobile and extrachromosomal element functions, Prophage functions, Mobile and extrachromosomal element functions, Plasmid functions]
IDWLVLRIPCKHSLPIERGDVLSRLPDGTVAWHSVKFSIVGGSFYTGIALRIFEGGNNFETHLELKGNPA
KLLQGHNVFGSDDLELLGIAFFGALIGVLAANPMPELYDLVDVGNTELTRVDVTYSFKLANDHIVRQWLS
AAENVANGQHKRTRALDYETTLYFGKNSRRWGLKAYSKHDEVQATIKEHGCLEELSKPDLVAWAVNLLRF
ELTLRTRFLENFIVKYADNWESGCDLWKKSFKDLFDEFKGSMEMYDDSKLYDALINNFSSVLRSGYISWS
KGNNVAQTMSRATFWRSRKELTSVGLDIAQLVSRDNSNVVPLVRVLEADPAQYPEWYVEPVLIFN
>gnl|CDD|130691 TIGR01630, psiM2_ORF9, phage uncharacterized protein (putative large terminase), C-terminal domain. This model represents the C-terminal region of a set of phage proteins typically about 400-500 amino acids in length, although some members are considerably shorter. An article on Methanobacterium phage Psi-M2 (calls the member from that phage, ORF9, a putative large terminase subunit, and ORF8 a candidate terminase small subunit. Most proteins in this family have an apparent P-loop nucleotide-binding sequence toward the N-terminus [Mobile and extrachromosomal element functions, Prophage functions]
DYSAGFIWGETKDKRAYVLDAIYDKEPPPETERLVIRLLNAHRVNLAIIESNQEGKSFGRSLVKILKEKG
IRTPARAVYPSGDKETRILSVAPWVEAGNVFPPNWAPWWPDLIQALEAFPREKAAHDDDPDAMTGAANSL
QD
>gnl|CDD|273724 TIGR01631, Trypano_RHS, trypanosome RHS (retrotransposon hot spot) family. This model describes full-length and part-length members of the RHS (retrotransposon hot spot) family in Trypanosoma brucei and Trypanosoma cruzi. Members of this family are frequently interrupted by non-LTR retrotransposons inserted at exactly the same relative position
AAQPPAIRQRTEEGPQWTMDSRVEDVLLEDYAGLRNMKLNDFLWKNFGGTYNVDETENVSMKVFVQSPED
YILDAGALNRIQATDEFERVKNNFVVFDEKVRYLDENEINTLSQWEEKAKGEIREFVGPVARGRLDPALE
AAKEAEKRAAQAADGVELEGVYDSIYNAKWSYVESGHGTEPLGMKVVDGRPPHMWTEEEVDVSPEPEDLA
EQLPRHGGLEIAVLTSEKGWPYTSFAKGVNSIQEEAEKDVYIRREVLRVWYIVKNGLTLWLSSHAKFEPE
RRVLIGTPGIGKSFGVGSFLLYQLLHYDAEKLQVVAYFVAGRAYLFDKTSGGGVGRVSFYEKDKAAADVV
EALSDEKVKGYIIYDFAKDDDEPPPADPPSGWGVILLSSPNESNFKEWSKQRGCTRIVMNCDEESDMKAF
VAWRGLSQAPEYKITEATPEELEEEWEVIKSRIDEVGPLPRYVFGEKKYTRRVQRCNEAIDEISSDDISH
YNGVVGNRGSWRCDKVSHKLVKIVRVRGEDCSGEEYRCRPVSAHIGNKILFKLAKIMQQKDANSLVLEST
RELAAENFERCAVFALLFGNVVRGIARRLRYLPRPGEQRQSHRVLLAVYEQELSTRHHVLPPDEHFSEII
DIEYGVLYKPEVGNFPVVDAFFFVESPAIAEDKQRREKKTIVGLQYTVAGRHHTTTGTVRKFTEYLAAYF
NGWDELSRQLVWEIIYVQHVDSTPITDWQRCDVVDSAEGADNNEIEVFWKNKVRQYQVKL
>gnl|CDD|233500 TIGR01632, 50S_ribosomal_protein_L11, 50S ribosomal protein uL11, bacterial form. This model represents bacterial, chloroplast, and most mitochondrial forms of 50S ribosomal protein L11 [Protein synthesis, Ribosomal proteins: synthesis and modification]
KKIVGIIKLQVPAGQANPAPPVGPALGQRGVNIMEFCKQFNARTADYEPGLPVPVVITVYEDKSFTFIVK
TPPVSYLLKKAAGVEKGSKNPKKEKVGKITRKQVREIAEIKMSDLNTKDIEAAMKIIAGTAKSMGIEIVG
>gnl|CDD|188159 TIGR01633, unnamed_protein_product, putative phage tail component, N-terminal domain. This model represents the best-conserved region of about 125 amino acids, toward the N-terminus, of a family of proteins from temperate phage of a number of Gram-positive bacteria. These phage proteins range in length from 230 to 525 amino acids [Mobile and extrachromosomal element functions, Prophage functions]
FSFNGVDLSELFLVTVIKRPMYSPSERNTTSEVPGDGGVLVNVKLGARELTVPVKINDIDPRDLRERFRE
LAGWLNRQEPVPLIFSDEPDKTYYARVDEEIDLDEDTNFGKGTLNFICPDPYKY
>gnl|CDD|130695 TIGR01634, unnamed_protein_product, phage tail protein, P2 protein I family. This model represents the family of phage P2 protein I and related tail proteins from a number of temperate phage of Gram-negative bacteria. This model is built as a fragment model and identifies some phage tail proteins with strong but local similarity to members of the seed alignment [Mobile and extrachromosomal element functions, Prophage functions]
LPPNATPLERAAARACARIENIPIPLRQLWNPDTCPANLLPWLAWAFSVDRWDSTWPEKVKRDVIRSAYF
IHRHKGTIGAVRRVVEPFGGIVNITEWWQTGPPGPPGTFELTLTVSGSGGTEETYLEVERLIADVKPTS
>gnl|CDD|130696 TIGR01635, Mu-like_prophage_FluMu_G_protein, phage virion morphogenesis (putative tail completion) protein. This model describes protein S of phage P2, suggested experimentally to act in tail completion and stable head joining, and related proteins from a number of phage [Mobile and extrachromosomal element functions, Prophage functions]
EDRSYIQVALERLLQVLDPKTRDKMLRRIAAQLASSTRKNIEAQQDPDGSAWAARKKKVRSKKGRIGKIL
KKFTQKRLMKSRTSDYGLVVALIGARERYAAIHQYGGKARSGRLRKVQYPARPFLGLTKTDEAEIEAAIR
KALS
>gnl|CDD|130697 TIGR01636, Transcriptional_activator_rinA, phage transcriptional activator, RinA family. This model represents a family of phage proteins, including RinA, a transcriptional activator in staphylococcal phage phi 11. This family shows similarity to ArpU, a phage-related putative autolysin regulator, and to some sporulation-specific sigma factors [Mobile and extrachromosomal element functions, Prophage functions, Regulatory functions, DNA interactions]
LRTSTFNYIEDELADYYKTEKYLRQREEELRHPYQEADLNAGGRGQGLHSVVTERMVITIAMDRRLWNLE
RNRDAIENCLNEADEQTRVIIQELYMKKRPLTLVGLAQQLFISKSTAYRLRNHIIEAVAEELGM
>gnl|CDD|273725 TIGR01637, Putative_autolysin_regulatory_protein_ArpU, phage transcriptional regulator, ArpU family. This model represents a family of phage proteins, including ArpU, called a putative autolysin regulatory protein. ArpU was described as a regulator of cellular muramidase-2 of Enterococcus hirae but appears to have been cloned from a prophage. This family appears related to the RinA family of bacteriophage transcriptional activators and to some sporulation-specific sigma factors. We propose that this is a phage transcriptional activator family [Mobile and extrachromosomal element functions, Prophage functions, Regulatory functions, DNA interactions]
LFPEIDEKKTRANVKRFLEDYRRLRRIAGRSLTPKLSPSLSLEPPSFTNEFHSKTEEAAIHNLDAEQEAR
AIVNAIVNQLDEISRQILYDKYLEPDQKYDYQIMMELGYSHRQYYRIKKRALLRFATLYGIG
>gnl|CDD|130699 TIGR01638, hypothetical_protein, Arabidopsis thaliana cystatin-related protein. This model represents a family similar in sequence and probably homologous to a large family of cysteine proteinase inhibitors, or cystatins, as described by pfam00031. Cystatins may help plants resist attack by insects
DWEAIRPIETNRDLLERLSYVASKKYNDTKFLNLELVEVVRANYRGGAKSKSYITFEARDKPDGPLGEYQ
QAAVVYLHRHPIVCRPTPKPLP
>gnl|CDD|130700 TIGR01639, P_fal_TIGR01639, Plasmodium falciparum uncharacterized domain TIGR01639. This model represents a conserved sequence region of about 60 amino acids found in over 40 predicted proteins of Plasmodium falciparum. It is not found elsewhere, including closely related species such as Plasmodium yoelii. No member of this family is characterized
IKYNDLSKKLTKEELNEMINSLDEIPNRNDMLIIWNQVHGIERDKFVKMQENLKEYIQKLV
>gnl|CDD|273726 TIGR01640, unnamed_protein_product, F-box protein interaction domain. This model describes a large family of plant domains, with several hundred members in Arabidopsis thaliana. Most examples are found C-terminal to an F-box (pfam00646), a 60 amino acid motif involved in ubiquitination of target proteins to mark them for degradation. Two-hybid experiments support the idea that most members are interchangeable F-box subunits of SCF E3 complexes. Some members have two copies of this domain
VVPCDGLICFSYGKRLVVWNPSTGQSRWLPTPKSRRSNKESDTYFLGYDPIEKQYKVLCFSDRSGNRNQS
EHQVYTLGSNSWRTIECSPPHHPLKSRGVCINGVLYYLAYTLKTNPDYFIVSFDVSSERFKEFIPLPCGN
SDSVDYLSLINYKGKLAVLKQKKDTNNFDLWVLNDAGKQEWSKLFTVPIPPLPDLVDDNFLSGFTDKGEI
VLCCEDENPFYIFYYNVGEN
>gnl|CDD|213641 TIGR01641, Uncharacterized_protein_MJ0329, phage putative head morphogenesis protein, SPP1 gp7 family. This model describes a region of about 110 amino acids found exclusively in phage-related proteins, internally or toward the C-terminus. One member, gp7 of phage SPP1, appears involved in head morphogenesis [Mobile and extrachromosomal element functions, Prophage functions]
VEDILADGVQRGLGPNELAKRLRKELGVQKHYAQRLARTETARIYNQTKLERYKKAGPIYEYIAIIDSRT
RPICRALNGKIFKVDDAVPGVNAPPLHPNCRCTLAPVP
>gnl|CDD|273727 TIGR01642, Splicing_factor_U2AF_59_kDa_subunit, U2 snRNP auxilliary factor, large subunit, splicing factor. These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi
RDEEPDREREKSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSS
VRRSRDRPRRRSRSVRSIEQHRRRLRDRSPSNQWRKDDKKRSLWDIKPPGYELVTADQAKASQVFSVPGT
APRPAMTDPEKLLAEGSIITPLPVLPYQQQATRQARRLYVGGIPPEFVEEAVVDFFNDLMIATGYHKAED
GKHVSSVNINKEKNFAFLEFRTVEEATFAMALDSIIYSNVFLKIRRPHDYIPVPQITPEVSQKNPDDNAK
NVEKLVNSTTVLDSKDRIYIGNLPLYLGEDQIKELLESFGDLKAFNLIKDIATGLSKGYAFCEYKDPSVT
DVAIAALNGKDTGDNKLHVQRACVGANQATIDTSNGMAPVTLLAKALSQSILQIGGKPTKVVQLTNLVTG
DDLMDDEEYEEIYEDVKTEFSKYGPLINIVIPRPNGDRNSTPGVGKVFLEYADVRSAEKAMEGMNGRKFN
DRVVVAAFYGEDCYKAGDY
>gnl|CDD|273728 TIGR01643, tRNA_nuclease_WapA, YD repeat (two copies). This model describes two tandem copies of a 21-residue extracellular repeat found in Gram-negative, Gram-positive, and animal proteins. The repeat is named for a YD dipeptide, the most strongly conserved motif of the repeat. These repeats appear in general to be involved in binding carbohydrate; the chicken teneurin-1 YD-repeat region has been shown to bind heparin
YDAAGRLTGSTDADGTTTRYTYDAAGRLVEITDADGGSTRYE
>gnl|CDD|273729 TIGR01644, Mu-like_prophage_FluMu_protein_gp45, phage baseplate assembly protein V. This model describes a family of phage (and bacteriocin) proteins related to the phage P2 V gene product, which forms the small spike at the tip of the tail. Homologs in general are annotated as baseplate assembly protein V. At least one member is encoded within a region of Pectobacterium carotovorum (Erwinia carotovora) described as a bacteriocin, a phage tail-derived module able to kill bacteria closely related to the host strain [Mobile and extrachromosomal element functions, Prophage functions]
LMRGLRNLIRRGVVAEVDDAAGRVRVLQGELLTGWLPWLVERAGNYRTWSAPSVGEQVLVLSPGGQLDTG
VVLPGVYSDDFRPPSLSAGDTVTYFADGARIEYDKAAHALTVCGIKTVYLDAGDGTTVTVDAPQITFTGG
VTTLKGPETVITGNVTIDGTLHTGGDASSNGISLDKHGHTGVHSGGTTSG
>gnl|CDD|130706 TIGR01645, Ro_ribonucleoprotein-binding_protein_1, poly-U binding splicing factor, half-pint family. The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA
SADIENQPVAAFRPAVSVPMPVLGDKWKPPQQTGEVKVGPGKKDAQKIGLGLPKLSSEQKDDIQKAKKYA
MEQSIKQVLLKQTKAHQQQQLENQQRQQQRQQALAIMCRVYVGSISFELREDTIRRAFDPFGPIKSINMS
WDPATGKHKGFAFVEYEVPEAAQLALEQMNGQMLGGRNIKVGRPSNMPQAQPIIDMVQEEAKKFNRIYVA
SVHPDLSETDIKSVFEAFGEIVKCQLARAPTGRGHKGYGFIEYNNLQSQSEAIASMNLFDLGGQYLRVGK
CVTPPDALLQPATVSAIPAAAAVAAAAATAKIMAAEAVAGAAVLGPRAQSPATPSSSLPTDIGNKAVVSS
AKKEAEEVPPLPQAAPAVVKPGPMEIPTPVPPPGLAIPSLVAPPGLVAPTEINPSFLASPRKKMKREKLP
VTFGALDDTLAWKEPSKEDQTSEDGKMLAIMGEAAAALALEPKKKKKEKEGEELQPKLVMNSEDASLASQ
EGMSIRGNSARHLVMQKLMRTNRSNVIVLRNMVTPQDIDEFLEGEIREECGKFGVVDRVIINFEKQGEEE
DAEIIVKIFVEFSDSMEVDRAKAALDGRFFGGRTVVAEAYDQILFDHADLSG
>gnl|CDD|273730 TIGR01646, conserved_hypothetical_protein, Rhs element Vgr protein. This model represents the Vgr family of proteins, associated with some classes of Rhs elements. This model does not include a large octapeptide repeat region, VGXXXXXX, found in the Vgr of Rhs classes G and E
YTVLSFEGNEILSQPFTYELILRSADADLDLAAMLGKDASLSLELPDAASTQRIFTGVIAGFSLGSTANG
DARYSLVLRPWLWLLTRRRNNRIFQDTSVPDIIEEILREYGFADFRFDVAREYPQREYCVQYGETDFDFI
LRLLEEEGIIYYFEHDPKKHILVAPDTSGQPQITLGYASLPFELPGAMDAREQSIYDWTRAQQVNSASVA
LVDYDFKNPTARLQAQSNISRQQAQVPDLEAYDYAGSYLDAQHGELYARLRLEALQSRAAKIQGEGNAAG
LAPGQLFVLSGHPRNDQNNGYLIVSAIHSIVQLGWDTGIQGYELPNQFIAIEVDVIWRPAATPLPKVNGP
QIAVVVGAQGEEIHTDKYGRIRVHFHWDRYGQSNDYSSCWIRVAQPWAGKNWGSLAIPRVGQEVIVGFLD
GDPDRPIVTGRVYNAANPPPYRLPAHNTQSGFKSRTLRGGSQNQLRFDDDKGKEQLQLHAERD
>gnl|CDD|273731 TIGR01647, Plasma_membrane_ATPase, plasma-membrane proton-efflux P-type ATPase. This model describes the plasma membrane proton efflux P-type ATPase found in plants, fungi, protozoa, slime molds and archaea. The best studied representative is from yeast
GLTSAEAKKRLAKYGPNELPEKKVSPLLKFLGFFWNPLSWVMEAAAIIAIALENWVDFVIILGLLLLNAT
IGFIEENKAGNAVEALKQSLAPKARVLRDGKWQEIPASELVPGDVVRLKIGDIVPADCRLFEGDYIQVDQ
AALTGESLPVTKKTGDIAYSGSTVKQGEAEAVVTATGMNTFFGKAAALVQSTETGSGHLQKILSKIGLFL
IVLIGVLVLIELVVLFFGRGESFREGLQFALVLLVGGIPIAMPAVLSVTMAVGAAELAKKKAIVTRLTAI
EELAGMDILCSDKTGTLTLNKLSIDEILPFFNGFDKDDVLLYAALASREEDQDAIDTAVLGSAKDLKEAR
DGYKVLEFVPFDPVDKRTEATVEDPETGKRFKVTKGAPQVILDLCDNKKEIEEKVEEKVDELASRGYRAL
GVARTDEEGRWHFLGLLPLFDPPRHDTKETIERARHLGVEVKMVTGDHLAIAKETARRLGLGTNIYTADV
LLKGDNRDDLPSGLGEMVEDADGFAEVFPEHKYEIVEILQKRGHLVGMTGDGVNDAPALKKADVGIAVAG
ATDAARSAADIVLTEPGLSVIVDAILESRKIFQRMKSYVIYRIAETIRIVFFFGLLILILNFYFPPIMVV
IIAILNDGTIMTIAYDNVKPSKLPQRWNLREVFTMSTVLGIYLVISTFLLLAIALDTTFFIDKFGLQLLH
GNLQSFIYLQVSISGHATIFVTRTHGFFWSERPGKLLFGAFVIAQIIATFIAVY
>gnl|CDD|273732 TIGR01648, Heterogeneous_nuclear_ribonucleoprotein_R, heterogeneous nuclear ribonucleoprotein R, Q family. Sequences in this subfamily include the human heterogeneous nuclear ribonucleoproteins (hnRNP) R, Q, and APOBEC-1 complementation factor (aka APOBEC-1 stimulating protein). These proteins contain three RNA recognition domains (rrm: pfam00076) and a somewhat variable C-terminal domain
RSREKQGSKVQEGTKGTPDEAALKALLERTGYTLVQENGQRKYGGPPPGWSGVQPGRGCEVFVGKIPRDL
YEDELVPLFEKAGPIYELRLMMDFSGQNRGYAFVTFCGKEEAKEAVKLLNNYEIRPGRLLGVCISVDNCR
LFVGGIPKNKKREEILEEFSKVTEGVVDVIVYHSAADKKKNRGFAFVEYESHRAAAMARRKLMPGRIQLW
GHVIAVDWAEPEEEVDEDVMAKVKILYVRNLMTTTTEEIIEKSFSEFKPGKVERVKKIRDYAFVHFEDRE
DAVKAMDELNGKELEGSEIEVTLAKPVDKKSYVRYTRGTGGRGKERQAARQSLGQVYDPASRSLAYEDYY
YHPPYAPSLHFPRMPGPIRGRGRGGAPSRAAGGRGYPPYGYEAYYGDYYGYHDYRGKYEDKYYGYDPGME
LTPMNPVRGKPGGRGGRPAIPPPRGRKNGAPPPAIGQDGRQLFLYKITIPAGYSQRPAPHPLGPPRGSAF
VRGARGGPAQYQQRGRGSRTSRGNGRGGTAGGKRKAFDGYAQPDATARQTNNQQNWGAQPIGGDYAGYYG
YEVYNNAVTDNQDFYQTY
>gnl|CDD|273733 TIGR01649, Heterogeneous_nuclear_ribonucleoprotein_L, hnRNP-L/PTB/hephaestus splicing factor family. Included in this family of heterogeneous ribonucleoproteins are PTB (polypyrimidine tract binding protein) and hnRNP-L. These proteins contain four RNA recognition motifs (rrm: pfam00067)
PSPVVHVRNLPQDVVEADLVEALIPFGPVSYVMMLPGKRQALVEFEDEESAKACVNFATSVPIYIRGQPA
FFNYSTSQEIKRDGNSDFDSAGPNKVLRVIVENPMYPITLDVLYQIFNPYGKVLRIVTFTKNNVFQALVE
FESVNSAQHAKAALNGADIYNGCCTLKIEYAKPTRLNVKYNDDDSRDYTNPDLPGRRDPGLDQTHRQRQP
ALLGQHPSSYGHDGYSSHGGPLAPLAGGDRMGPPHGPPSRYRPAYEAAPLAPAISSYGPAGGGPGSVLMV
SGLHQEKVNCDRLFNLFCVYGNVERVKFMKNKKETALIEMADPYQAQLALTHLNGVKLFGKPLRVCPSKQ
QNVQPPREGQLDDGLTSYKDYSSSRNHRFKKPGSANKNNIQPPSATLHLSNIPLSVSEEDLKELFAENGV
HKVKKFKFFPKDNERSKMGLLEWESVEDAVEALIALNHHQLNEPNGSAPYHLKVSFSTSRI
>gnl|CDD|130711 TIGR01650, PD_CobS, cobaltochelatase, CobS subunit. This model describes Pseudomonas denitrificans CobS gene product, which is a cobalt chelatase subunit that functions in cobalamin biosynthesis. Cobalamin (vitamin B12) can be synthesized via several pathways, including an aerobic pathway (found in Pseudomonas denitrificans) and an anaerobic pathway (found in P. shermanii and Salmonella typhimurium). These pathways differ in the point of cobalt insertion during corrin ring formation. There are apparently a number of variations on these two pathways, where the major differences seem to be concerned with the process of ring contraction. Confusion regarding the functions of enzymes found in the aerobic vs. anaerobic pathways has arisen because nonhomologous genes in these different pathways were given the same gene symbols. Thus, cobS in the aerobic pathway (P. denitrificans) is not a homolog of cobS in the anaerobic pathway (S. typhimurium). It should be noted that E. coli synthesizes cobalamin only when it is supplied with the precursor cobinamide, which is a complex intermediate. Additionally, all E. coli cobalamin synthesis genes (cobU, cobS and cobT) were named after their Salmonella typhimurium homologs which function in the anaerobic cobalamin synthesis pathway. This model describes the aerobic cobalamin pathway Pseudomonas denitrificans CobS gene product, which is a cobalt chelatase subunit, with a MW ~37 kDa. The aerobic pathway cobalt chelatase is a heterotrimeric, ATP-dependent enzyme that catalyzes cobalt insertion during cobalamin biosynthesis. The other two subunits are the P. denitrificans CobT (TIGR01651) and CobN (pfam02514 CobN/Magnesium Chelatase) proteins. To avoid potential confusion with the nonhomologous Salmonella typhimurium/E.coli cobS gene product, the P. denitrificans gene symbol is not used in the name of this model [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
MNAADPDIALLPDRTVSLKDAFGFDSDMKVPAFSHRDEHVPDIDPAYLFDKATTKAICAGFAYDRRVMVQ
GYHGTGKSTHIEQIAARLNWPCVRVNLDSHVSRIDLVGKDAIVLKDGKQITEFRDGILPWALQHNVALCF
DEYDAGRPDVMFVIQRVLEAGGKLTLLDQNRVIRAHPAFRLFATANTIGLGDTTGLYHGTQQINQAQMDR
WSIVTTLNYLEHDNEAAIVLAKAKGFDDTEGKDIINAMVRVADMTRNAFINGDISTVMSPRTVITWAENA
EIFDHDIALAFRLTFLNKCDELERPTVAEFFQRAFGEDLPESAANVK
>gnl|CDD|130712 TIGR01651, CobT, cobaltochelatase, CobT subunit. This model describes Pseudomonas denitrificans CobT gene product, which is a cobalt chelatase subunit that functions in cobalamin biosynthesis. Cobalamin (vitamin B12) can be synthesized via several pathways, including an aerobic pathway (found in Pseudomonas denitrificans) and an anaerobic pathway (found in P. shermanii and Salmonella typhimurium). These pathways differ in the point of cobalt insertion during corrin ring formation. There are apparently a number of variations on these two pathways, where the major differences seem to be concerned with the process of ring contraction. Confusion regarding the functions of enzymes found in the aerobic vs. anaerobic pathways has arisen because nonhomologous genes in these different pathways were given the same gene symbols. Thus, cobT in the aerobic pathway (P. denitrificans) is not a homolog of cobT in the anaerobic pathway (S. typhimurium). It should be noted that E. coli synthesizes cobalamin only when it is supplied with the precursor cobinamide, which is a complex intermediate. Additionally, all E. coli cobalamin synthesis genes (cobU, cobS and cobT) were named after their Salmonella typhimurium homologs which function in the anaerobic cobalamin synthesis pathway. This model describes the aerobic cobalamin pathway Pseudomonas denitrificans CobT gene product, which is a cobalt chelatase subunit, with a MW ~70 kDa. The aerobic pathway cobalt chelatase is a heterotrimeric, ATP-dependent enzyme that catalyzes cobalt insertion during cobalamin biosynthesis. The other two subunits are the P. denitrificans CobS (TIGR01650) and CobN (pfam02514 CobN/Magnesium Chelatase) proteins. To avoid potential confusion with the nonhomologous Salmonella typhimurium/E.coli cobT gene product, the P. denitrificans gene symbol is not used in the name of this model [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
EPFKRALAHCARSIAGDPDLEVVFAGDRPQLLGNRARLPELPKDLSSREAARTRGLGDSMALRLACHDAR
IHARARPSGPDARAIFDAVEQARVEAIGSNAMGGVAANLTAMLEAKYAKANLTVATDRADAPMAEALALM
VREKLTGDAPPHSAKALVDLWRNDIEAKAGKDLDRLSAAIDDQQAFARVVREMLRSMELAEEMGDDTESE
DEEDGDDDQPTENEQEEQGEGEGEGQEGSAPQESEATDRESESGEEEMVQSDQDDLPDESDDDSETPGEG
ARPARPFTSTGGEPDYKVFTTAFDETVDAEELCDEEELDRLRAFLDKQLAALSGVVGRLANRLQRRLMAQ
QNRSWTFDLEEGYLDVARLTRVIIDPMQPLSFKQEEDTEFRDTVVTLLIDNSGSMRGRPITVAATCADIL
ARTLERCGVKVEILGFTTRAWKGGQSREKWLKAGKPAAPGRLNDLRHIIYKSADAPWRRARRNLGLMMRE
GLLKENIDGEALMWAHQRLIARPEQRRILMMISDGAPVDDSTLSVNPGNYLERHLRAVIEEIETRSPVEL
LAIGIGHDVTRYYRRAVTIVDAEELAGAMTEQLAALFEEE
>gnl|CDD|273734 TIGR01652, Probable_phospholipid-transporting_ATPase_DRS2, phospholipid-translocating P-type ATPase, flippase. This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes
FCSNKISTTKYTVLTFLPKNLFEQFKRFANLYFLVVALLQQVPILSPTYRGTSIVPLAFVLIVTAIKEAI
EDIRRRRRDKEVNNRLTEVLEGHGQFVEIPWKDLRVGDIVKVKKDERIPADLLLLSSSEPDGVCYVETAN
LDGETNLKLRQALEETQKMLDEDDIKNFSGEIECEQPNASLYSFQGNMTINGDRQYPLSPDNILLRGCTL
RNTDWVIGVVVYTGHDTKLMRNATQAPSKRSRLEKELNFLIIILFCLLFVLCLISSVGAGIWNDAHGKDL
WYIRLDVSERNAAANGFFSFLTFLILFSSLIPISLYVSLELVKSVQAYFINSDLQMYHEKTDTPASVRTS
NLNEELGQVEYIFSDKTGTLTQNIMEFKKCSIAGVSYGDGFTEIKDGIRERLGSYVENENSMLVESKGFT
FVDPRLVDLLKTNKPNAKRINEFFLALALCHTVVPEFNDDGPEEITYQAASPDEAALVKAARDVGFVFFE
RTPKSISLLIEMHGETKEYEILNVLEFNSDRKRMSVIVRNPDGRIKLLCKGADTVIFKRLSSGGNQVNEE
TKEHLENYASEGLRTLCIAYRELSEEEYEEWNEEYNEASTALTDREEKLDVVAESIEKDLILLGATAIED
KLQEGVPETIELLRQAGIKIWVLTGDKVETAINIGYSCRLLSRNMEQIVITSDSLDATRSVEAAIKFGLE
GTSEEFNNLGDSGNVALVIDGKSLGYALDEELEKEFLQLALKCKAVICCRVSPSQKADVVRLVKKSTGKT
TLAIGDGANDVSMIQEADVGVGISGKEGMQAVMASDFAIGQFRFLTKLLLVHGRWSYKRISKMILYFFYK
NLIFAIIQFWYSFYNGFSGQTLYEGWYMVLYNVFFTALPVISLGVFDQDVSASLSLRYPQLYREGQKGQG
FSTKTFWGWMLDGIYQSLVIFFFPMFAYILGDFVSSGSVDDFSSVGVIVFTALVVIVNLKIALEINRWNW
ISLITIWGSILVWLIFVIVYSSIFPSPAFYKAAPRVMGTFGFWLVLLVIVLISLLPRFTYKAIQRLFRPP
DYDIVQE
>gnl|CDD|273735 TIGR01653, hypothetical_protein, bacteriocin, lactococcin 972 family. This model represents bacteriocins related to lactococcin 972. Members tend to be found in association with a seven transmembrane putative immunity protein [Cellular processes, Toxin production and resistance]
MKKKVVASLVSTTILATLGGLAAQVEAAQSTQGGTWWKTYGMGRHYSNYWHNKRNHWATVVNDKSGRRGK
DVHAGAWAKASLNKNWAEPATF
>gnl|CDD|273736 TIGR01654, unnamed_protein_product, bacteriocin-associated integral membrane (putative immunity) protein. This model represents a family of integral membrane proteins, most of which are about 650 residues in size and predicted to span the membrane seven times. Nearly half of the members of this family are found in association with a member of the lactococcin 972 family of bacteriocins (TIGR01653). Others may be associated with uncharacterized proteins that may also act as bacteriocins. Although this protein is suggested to be an immunity protein, and the bacteriocin is suggested to be exported by a Sec-dependent process, the role of this protein is unclear [Cellular processes, Toxin production and resistance]
MKTLILLLVLTSFFVISTLSAVIVVREQEQGQTGDKYDVQVFDINEPPFLEASENNIKSYLESFAKKDNV
LIAKSSGVPSKDNKTKDHFTFNKLYGNKTIPNKFQSYPTYSKEKPEQLKKEQFYFIKNGRLSITKLQDYL
NQLGSKFAKDDKVDTYPPAVSSLKDLNILVILALLLIVIFALFLIYYLMINMKRVAIYRLNGFSLRKILF
RLFSKNCTYLLISALLILLLSSFLLFIKGYTYLLKDFIFMLSLSVLLLLLLLLIISFLTLLLLSKMSLAN
SIKGKSSFKFLLIINYVCKLVLLVLVIATLITILSSLQDLNEILASQQQWASLKDYYTISLGYGLEQKLK
ESSLKSTDYAFYKEAEEKEGALYVDSNLLPVENDNQAFETSSPEGNSLYVNPNYLSKFPIVSQKGQKIKN
QEEKNNKVILVPESYKSQENKIKKYFEDYFYFYSMKYEEASKRLIEEMDVIIIYYENDQRFFSYDDYVFP
KRTENISDPIIVVVTPNDFSDSEKASFSHVTLSVNSIDQENFKTYQALLPLLKKYLLDGNISHLSSVNDI
VQEDIDEIQDALTNLNILFILFALISLSIIYFLVVLYFEQHRKKILIKRLFGYSLFRTYKQYLVINLAVY
VFILILALIFSHAFYILLLFAVIFVLEILLILGILSKLEKRFFVSILKG
>gnl|CDD|130716 TIGR01655, Uncharacterized_protein_YxeA, conserved hypothetical protein TIGR01655. This model represents a family of small (about 115 amino acids) uncharacterized proteins with N-terminal signal sequences, found exclusively in Gram-positive organisms. Most genomes that have any members of this family have at least two members [Hypothetical proteins, Conserved]
MKKGLAILLALIVVITIVGIEISHPVYSDRFNYYIKIKNDYKEVPKSKFKGYPLYEYKLDAYDSSGKKHK
VKFMAGTNLKSNAYLKIKYNKGKYVVQWKEVEKESVPKAVRKKL
>gnl|CDD|273737 TIGR01656, Imidazoleglycerol-phosphate_dehydratase, histidinol-phosphate phosphatase family domain. This domain is found in authentic histidinol-phosphate phosphatases which are sometimes found as stand-alone entities and sometimes as fusions with imidazoleglycerol-phosphate dehydratase (TIGR01261). Additionally, a family of proteins including YaeD from E. coli (TIGR00213) and various other proteins are closely related but may not have the same substrate specificity. This domain is a member of the haloacid-dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. This superfamily is distinguished by the presence of three motifs: an N-terminal motif containing the nucleophilic aspartate, a central motif containing an conserved serine or threonine, and a C-terminal motif containing a conserved lysine (or arginine) and conserved aspartates. More specifically, the domian modelled here is a member of subfamily III of the HAD-superfamily by virtue of lacking a "capping" domain in either of the two common positions, between motifs 1 and 2, or between motifs 2 and 3
PALFLDRDGVINEDTVSDYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNG
RLLELLRQLGVAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAA
AGLLVSG
>gnl|CDD|273738 TIGR01657, Probable_cation-transporting_ATPase, P-type ATPase of unknown pump specificity (type V). These P-type ATPases form a distinct clade but the substrate of their pumping activity has yet to be determined. This clade has been designated type V in
DKTIGISAYKISPFKLIIYLVTLILTFGLVLLLLTWLPEWKVKLRYVPVSNEDAETVVIVDPTPNSGSDY
IVELSNKSLSNDLQTENAVEGGEEPIYFDFRKQRFSYHEKELKIFSPLPYLFKEKSFGVYSTCAGHSNGL
TTGDIAQRKAKYGKNEIEIPVPSFLELLKEEVLHPFYVFQVFSVILWLLDEYYYYSLCIVFMSSTSISLS
VYQIRKQMQRLRDMVHKPQSVIVIRNGKWVTIASDELVPGDIVSIPRPEEKTMPCDSVLLSGSCIVNESM
LTGESVPVLKFPIPDNGDDDEDLFLYETSKKHVLFGGTKILQIRPYPGDTGCLAIVVRTGFSTSKGQLVR
SILYPKPRVFKFYKDSFKFILFLAVLALIGFIYTIIELIKDGRPLGKIILRSLDIITIVVPPALPAELSI
GINNSLARLKKKGIFCTSPFRINFAGKIDVCCFDKTGTLTEDGLDLRGVQGLSGNQEFLKIVTEDSSLKP
SITHKALATCHSLTKLEGKLVGDPLDKKMFEATGWTLEEDDESAEPTSILAVVRTDDPPQELSIIRRFQF
SSALQRMSVIVSTNDERSPDAFVKGAPETIQSLCSPETVPSDYQEVLKSYTREGYRVLALAYKELPKLTL
QKAQDLSRDAVESNLTFLGFIVFENPLKPDTKEVIKELKRASIRTVMITGDNPLTAVHVARECGIVNPSN
TLILAEAEPPESGKPNQIKFEVIDSIPFASTQVEIPYPLGQDSVEDLLASRYHLAMSGKAFAVLQAHSPE
LLLRLLSHTTVFARMAPDQKETLVELLQKLDYTVGMCGDGANDCGALKQADVGISLSEAEASVAAPFTSK
LASISCVPNVIREGRCALVTSFQMFKYMALYSLIQFYSVSILYLIGSNLGDGQFLTIDLLLIFPVALLMS
RNKPLKKLSKERPPSNLFSVYILTSVLIQFVLHILSQVYLVFELHAQPWYKPENPVDLEKENFPNLLNTV
LFFVSSFQYLITAIVNSKGPPFREPIYKNKPFVYLLITGLGLLLVLLLDPHPLLGKILQIVPLPQEFRSK
LLVW
>gnl|CDD|273739 TIGR01658, Developmental_protein_eyes_absent, eyes absent protein conserved domain. This domain is common to all eyes absent (EYA) homologs. Metazoan EYA's also contain a variable N-terminal domain consisting largely of low-complexity sequences
PENVYVWDMDETLILLHSLLNGSYAESFNGSKDHKRGVEIGRRWEEMILEICDTHFFYEEIEECNEPFLD
DVRSYDDGKDLSRYEFKTDGFSTPTDDLNKRKLAYRHRAVAEIYEKGLGPLLDPESMEALDELYSETDVY
TDRWLSSALKFLEQCSCVEESSDGTSLIEISSRDNCINVLVTSGQLIPSLAKCLLFRLDTIFRIENVYSS
IKVGKLQCFKWIKERFGHPKVRFCAIGDGWEECTAAQAMNWPFVKIDLHPDSSHRFPGLTLKTL
>gnl|CDD|273740 TIGR01659, Protein_sex-lethal, sex-lethal family splicing factor. This model describes the sex-lethal family of splicing factors found in Dipteran insects. The sex-lethal phenotype, however, may be limited to the Melanogasters and closely related species. In Drosophila the protein acts as an inhibitor of splicing. This subfamily is most closely related to the ELAV/HUD subfamily of splicing factors (TIGR01661)
MYGNNNNGGYPPYGYNNKSSGGRMWGMSHSLPSGMSRYAFSPQDTDFSSYPSTGRQHRQGYNDFYGNGGS
SACGLGSMGNMANMASTNSLNSLGSGGSDDNDTNNSGTNLIVNYLPQDMTDRELYALFRTIGPINTCRIM
RDYKTGYSFGYAFVDFGSEADSQRAIKNLNGITVRNKRLKVSYARPGGESIKDTNLYVTNLPRTITDDQL
DTIFGKYGQIVQKNILRDKLTGTPRGVAFVRFNKREEAQEAISALNNVIPEGGSQPLTVRLAEEHGKAKA
HHYMSQMGHGNMGNMGHGNMGMAGGSGMNPPNPPAFMGMNNMVHRGRQKKQRFQRIHPYNDAPKFI
>gnl|CDD|211677 TIGR01660, Respiratory_nitrate_reductase_1_beta_chain, nitrate reductase, beta subunit. The Nitrate reductase enzyme complex allows bacteria to use nitrate as an electron acceptor during anaerobic growth. The enzyme complex consists of a tetramer that has an alpha, beta and 2 gamma subunits. The alpha and beta subunits have catalytic activity and the gamma subunits attach the enzyme to the membrane and is a b-type cytochrome that receives electrons from the quinone pool and transfers them to the beta subunit. This model is specific for the beta subunit for nitrate reductase I (narH) and nitrate reductase II (narY) for gram positive and gram negative bacteria.A few thermophiles and archaea also match the model.The seed members used in this model are all experimentally characterized and include the following:SP:P11349, and SP:P19318, both E.Coli (NarH and NarY respectively), SP:P42176 from B. Subtilis, GP:11344602 from Psuedomonas fluorescens,GP:541762 from Paracoccus denitrificans, and GP:18413622 from Halomonas halodenitrificans. This model also matches Pfam pfam00037 for 4Fe-4S binding domain [Energy metabolism, Anaerobic]
MKIRSQIGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGIGYPKDWENQDKYKGGWVRKR
DGKLEPRIGGKWRVLANIFANPDLPSIDDYYEPFDFDYQHLHTAPEGKHQPTARPRSLITGERMEKIEWG
PNWEDDLGGEFAKRRKDKNFDKIQKDIYGEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEDGIVL
IDQDKCRGWRMCISGCPYKKIYFNWKTGKSEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIE
EAASTENEKDLYHRQLDVFLDPNDPEVIAQAKKDGIPLSVIEAAQQSPVYKMAMDWKLALPLHPEYRTLP
MVWYVPPLSPIQNAAEAGKVGANGIMPDVESLRIPVRYLANLLTAGDTKPVLLALKRMLAMRHYMRAETV
DGVVDTEVLEDVGLTEQQIEEMYRYLAIANYEDRFVIPSSHREIARDAFPERGGCGFSFGDGCHGSDTKN
LF
>gnl|CDD|273741 TIGR01661, ELAV-like_protein_4, ELAV/HuD family splicing factor. This model describes the ELAV/HuD subfamily of splicing factors found in metazoa. HuD stands for the human paraneoplastic encephalomyelitis antigen D of which there are 4 variants in human. ELAV stnds for the Drosophila Embryonic lethal abnormal visual protein. ELAV-like splicing factors are also known in human as HuB (ELAV-like protein 2), HuC (ELAV-like protein 3, Paraneoplastic cerebellar degeneration-associated antigen) and HuR (ELAV-like protein 1). These genes are most closely related to the sex-lethal subfamily of splicing factors found in Dipteran insects (TIGR01659). These proteins contain 3 RNA-recognition motifs (rrm: pfam00076)
ESKTNLIVNYLPQTMTQEEIRSLFTSIGEIESCKLVRDKVTGQSLGYGFVNYVRPEDAEKAVNSLNGLRL
QNKTIKVSYARPSSDSIKGANLYVSGLPKTMTQHELESIFSPFGQIITSRILSDNVTGLSKGVGFIRFDK
RDEADRAIKTLNGTTPSGCTEPITVKFANNPSSSNSKGLLSQLEAVQNPQTTRVPLSTILTAAGIGPMHH
AAARFRPSAGDFTAVLAHQQQQHAVAQQHAAQRASPPATDGQTAGLAAGAQISASDGAGYCIFVYNLSPD
TDETVLWQLFGPFGAVQNVKIIRDLTTNQCKGYGFVSMTNYDEAAMAILSLNGYTLGNRVLQVSFKTNKA
YR
>gnl|CDD|273742 TIGR01662, Uncharacterized_protein_YqeG, HAD-superfamily hydrolase, subfamily IIIA. This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme [Unknown function, Enzymes of unknown specificity]
KAVVLDLDGTLTDDVPYVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSRSFSGRVARRL
EELGVPIDILYACPGCRKPKPGMFLEALKRFNEIDPEESVYVGDQDLTDLQAAKRVGLATILVAP
>gnl|CDD|130724 TIGR01663, polynucleotide_kinase-3'-phosphatase, polynucleotide 5'-kinase 3'-phosphatase. This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78
GEVEAAGKDVAARICTLKPGEAEHHFIHLDAGALFLGRGPETGIRDRKCSKRQIELQADLEKATVALKQL
GVNPCGTGGLELKPGGEGELGHGDLLEIVNGLHPLTLQFEETFNPEPEPDKEKAEPLSSQDEKRDAEKPE
KRDRKGNPGWENLEKLLIFTAAGVKGQEKIAGFDLDGTIIKTKSGKVFPKGPDDWQIIFPEIPEKLKELE
ADGFKICIFTNQGGIARGKINADDFKAKIEAIVAKLGVPFQVFIAIGAGFYRKPLTGMWDHLKEEANDGT
EIQEDDCFFVGDAAGRPANGKAAGKKKKDFSCADRLFAANLGIPFATPEEFFLGKPAAGFEKPAFDPRSV
QDQGPLCDPDDLALDDAPCEMVIAVGFPGAGKSHFCKKFFQPAGYKHVNADTLGSTQNCLTACERALDQG
KRCAIDNTNPDAASRAKFLQCARAAGIPCRCFLFNAPLAQAKHNIAFRELSDSAHIKIKDMVFNGMKKKF
EAPALAEGFIAIHEINFKPLFADEKLEKLYCMFLEE
>gnl|CDD|211680 TIGR01664, Polynucleotide_3'-phosphatase, DNA 3'-phosphatase. This model represents a family of proteins and protein domains which catalyze the dephosphorylation of DNA 3'-phosphates. It is believed that this activity is important for the repair of single-strand breaks in DNA caused by radiation or oxidative damage. This domain is often (TIGR01663), but not always linked to a DNA 5'-kinase domain. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is usually replaced by an arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Alternatively, there is an additional conserved aspartate downstream of the ususal site which may indicate slightly different fold in this region
LFVFTADGPKPQSKVAAFDLDGTLITTRSGKVFPTSASDWRFLYPEIPAKLQELDDEGYKIVIFTNQSGI
GRGKLSAESFKNKIEAFLEKLKVPIQVLAATHAGLYRKPMTGMWEYLQSQYNSPIKMTRSFYVGDAAGRK
LDFSDADIKFAKNLGLEFKYPEEFFL
>gnl|CDD|273743 TIGR01665, structural_protein, phage minor structural protein, N-terminal region. This model represents the conserved N-terminal region, typically from about residue 25 to about residue 350, of a family of uncharacterized phage proteins 500 to 1700 residues in length [Mobile and extrachromosomal element functions, Prophage functions]
KDIKISEEKNNLDTLTFSLPFDDPLWEKIKEENYIKKHDDDLKNEQLFRINNVSEDASDDSISVEAIHVA
VDLLDHVIIPIKREKNTTSAALERLAKTTWEVWKLGECSDIKTISITFYQTSRNALQAIAKLYKLSIFYQ
WGGDNTITGKIVNLYKKIGSETGKEFEYGKNLVGLNRKEDTKNIVTRLIPFGKGEGGEKGLTIESSNVGD
EYIVDKDRQYKPNVDTTWVDGRYTDETTLRAYAKQKLMTLKKDMPKVSYEVTVADLENLSEYKSLEPIGI
GDTVRLKHTDFNIKVYARVIKVEYSPVTPKQNSIEFG
>gnl|CDD|130727 TIGR01666, Uncharacterized_protein_HI_1680, TIGR01666 family membrane protein. This model represents a clade of sequences from gamma and beta proteobacteria. These proteins are _700 amino acids long and many have been annotated as putative membrane proteins. The gene from Salmonella has been annotated as a putative efflux transporter. The gene from E. coli has the name yccS [Cell envelope, Other]
NYRLNAKVIYTIPIFIALNGAAVGIWFFDISSQSMPLILGIIAAALVDLDDRLTGRLKNVIFTLICFSIA
SFSVELLFGKPWLFAVGLTVSTFGFIMLGAVGQRYATIAFGSLLVALYTMLGYIEVNVWFIQPVMLLCGT
LWYSVVTLIVHLFFPNRPVQENLAKAFCQLAEYLETKSCFFDPDEVAEIQKKHLNFAMKNANVVTALNQV
KTALLTRIRGQHRHPLTQRMLRYYFAAQDIHERASSSHFDYQQLTEHFKNSDLLFRFQRLLELQAQACKE
ITASIRLNKPYQHDKRVERALLGTLHSLDLYRAQHLNDQDLLIDLGTLLNNLQSINWQLRQLAQDTTVTE
QLAQLHDEQIHGLKNIWARIFSHFTFESPLFRHAVRLSIVLFLGYAIIQFFGFNLGYWILLTTLFVCQPN
YSATKVRLRQRIIGTLLGVVIGSPLLYFNPSLELQLVLVVLTGVLFFAFRSNNYSFATFFITLLVLLCFN
VLGEGAAVLLPRLLDTLIGCAIAWAAVSYIWPDWQYLQLDKVSHQALRANAVYLLHIISQYQFGKSDDLK
YRIARRNAHNYDAALSTTVSNMNNEPVKYKAYLQKGFRLLKLNHSLLSYISALGAHRDRLKNLQQTAQFL
DGFYPVAKKLIYTLEHIEEIPEAIFNQQQESIETLELRKQEMTAEERAVFSLVYQQLNLITQLLPEFYGL
FKKE
>gnl|CDD|130728 TIGR01667, Uncharacterized_protein_HI_1680, integral membrane protein, YccS/YhfK family. This model represents two clades of putative transmembrane proteins including the E. coli YccS and YhfK proteins. The YccS hypothetical equivalog (TIGR01666) is found in beta and gamma proteobacteria, while the smaller YhfK group is only found in E. coli, Salmonella and Yersinia. TMHMM on the 19 hits to this model shows a consensus of 11 transmembrane helices separated into two clusters, an N-terminal cluster of 6 and a central cluster of 5. This would indicate two non-membrane domains one on each side of the membrane
NYALNQKLVYCLPVFIALMGAELRIWWFGLLFLLIPLCLGIIAAGLDDLDDRLTGRLKNLIITLSCFSIA
SFLVQLLFPKPWLFPFLLTLLTFGFILLGALGQRYATIAFASLLAAIYTMLGAGEVPVWFIEPLLILAGT
LWYGLLTLIWFLLFPNQPLQESLSRLYRELAEYLEAKSSLFDPDQHTDPEKALLPLAVRNGKVVDALNQC
KQQLLMRLRGNRTDPLTKRMLRYYFEAQDIHERASSSHHQYQELQELFEHSDVLFRIQRLLQTQAQACQV
LARDILLRQPYYHRLRTERALEKQIAALEKIRQNQAPDDLLGQLGYLLDNLQSIDWQLARIARVLATAKP
LYARDLLADKQPRGLKDILPRLKSHLTPESPLFRHAVRLSLVVMLGYAILMGTALHLGYWILLTTLFVCQ
PNYGATRLRLVQRIIGTVVGLVIGVALHFLIPSLEGQLTLMVITGVAFFAFRSKNYGWATVFITLLVLLC
FNLLGLDGEQYILPRLIDTLIGCLIAWGAVSYLWPDWQSRLLRKMLHDALEANQRYLRLILSQYPQGKPD
DLAYRIARRNAHNTDAALSTTLSNMMQEPAFNSHYLEDGFRLLTLSHTLLSYISALGAHRERLLNPELAA
ELLQACEIVAKAIQRCQARLEYDEEALAGDANIMEAQEMQPHEDAAGTLVYQQLQLIIGLLPTMHTLSSM
A
>gnl|CDD|273744 TIGR01668, Uncharacterized_protein_YqeG, HAD superfamily (subfamily IIIA) phosphatase, TIGR01668. This family of hypothetical proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. This family consists of sequences from fungi, plants, cyanobacteria, gram-positive bacteria and Deinococcus. There is presently no characterization of any sequence in this family
KFCLPHAIVKTLNDLTIDLLKKVGIKGVVLDKDNTLVYPDHNEAYPALRDWIEELKAAGRKLLIVSNNAG
EQRAKAVEKALGIPVLPHAVKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVH
PDQWFIKRIWRRVERTVLKFLVSRGGPAPE
>gnl|CDD|273745 TIGR01669, Uncharacterized_protein_YqcE, phage uncharacterized protein, XkdX family. This model represents a family of small (about 50 amino acid) phage proteins, found in at least 12 different phage and prophage regions of Gram-positive bacteria. In a number of these phage, the gene for this protein is found near the holin and endolysin genes [Mobile and extrachromosomal element functions, Prophage functions]
MHYASFEKVKTYYLWGYYSNEDVNKFVEKKLITREQYKVITGEKY
>gnl|CDD|130731 TIGR01670, KdsC-phosphatas, 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family. This family of proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. One member of this family, the YrbI protein from H. influenzae has been cloned, expressed, purified and found to be an active 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase. Furthermore, its crystal structure has been determined. This family consists of sequences from beta, gamma and epsilon proteobacteria, Aquifex, Fusobacterium, Porphyromonas and Methanosarcina. The Methanosarcina sequence is distinctive in that it is linked to an N-terminal cytidylyltransferase domain (pfam02348) and is annotated as acylneuraminate cytidylyltransferase. This may give some clue as the function of these phosphatases. Several eukaryotic sequences scoring between trusted and noise are also closely related to this function such as the CMP-N-acetylneuraminic acid synthetase from mouse, but in these cases the phosphatase domain is clearly inactive as many of the active site residues are not conserved [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
IRLLILDVDGVLTDGKIYYTNNGEEIKAFNVRDGYGIRCALKSGIEVAIITGRKAKLVEDRCKTLGITHL
YQGQSNKLIAFSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGA
VREVCELLLLAQGK
>gnl|CDD|273746 TIGR01671, hypothetical_phage_protein, phage uncharacterized protein TIGR01671. This model represents an uncharacterized, well-conserved family of proteins found in bacteriophage and prophage regions of Gram-positive bacteria [Mobile and extrachromosomal element functions, Prophage functions, Hypothetical proteins, Conserved]
AIGFRAFRKDNRKMISVNLMQFEDSEIATFSFADDRKRASTLTYAHFIINNIDEKTLMQSTGLKDKNGKE
IFEGDIVQVVLEIWPMEDEYIGVVKYDTDFCTVPDVIDGSWIIDTDSEDFDLWLYFDASVDSAAMEVIGN
IHENSELLEEQ
>gnl|CDD|273747 TIGR01672, Class_B_acid_phosphatase_precursor., HAD superfamily (subfamily IIIB) phosphatase, TIGR01672. This family of proteins is a member of the IIIB subfamily (pfam02767) of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of subfamily III and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. The AphA gene from E. coli has been characterized and shown to be an active phosphatase enzyme. This family has been previously described as the "class B non-specific bacterial acid phosphatase" (B-NSAP) family, where it is noted that the enzyme is secreted and has a broad substrate range. The possibility exists, however, that the enzyme is specific for an as yet undefined substrate. Supporting evidence for the inclusion in the HAD superfamily, whose phosphatase members are magnesium dependent, is the inhibition by EDTA and calcium ions, and stimulation by magnesium ion
MKKITQALSAVCLLFALASPAVALGSSPPYTQPGTNAARLAEQAPIHWISVAQIENSLEGRPPIAVSFDI
DDTVLFSSPGFWRGKKTFSPGSEDYLKNQVFWEKVNNGWDEFSIPKEVARQLIDMHQRRGDAIFFVTGRT
PGKTDTVSKTLAKNFHIPAMNPVIFAGDKPGQYQYTKTQWIQDKNIRIHYGDSDNDITAAKEAGARGIRI
LRASNSTYKPLPQAGGYGEEVLVNSEY
>gnl|CDD|130734 TIGR01673, putative_holin, phage holin, LL-H family. This model represents a putative phage holin from a number of phage and prophage regions of Gram-positive bacteria. Like other holins, it is small (about 100 amino acids) with stretches of hydrophobic sequence and is encoded adjacent to lytic enzymes [Mobile and extrachromosomal element functions, Prophage functions]
MDQILMTIFVIGLTVLGSVVSYYISHKLKIDKKTKSGDKLAKALDKLAKQAVSAVQQNFNESGGGAEKLE
QAFNYITEELKKAHIPKPSDAQIEGAIEAAVAEMKKNF
>gnl|CDD|273748 TIGR01674, phage_lambda_G, phage minor tail protein G. This model describes a family of bacteriophage proteins including G of phage lambda. This protein has been described as undergoing a translational frameshift at a Gly-Lys dipeptide near the C-terminus of protein G from phage lambda, with about 4 % efficiency, to produce tail assembly protein G-T. The Lys of the Gly-Lys pair is the conserved second-to-last residue of seed alignment for this family [Mobile and extrachromosomal element functions, Prophage functions]
MFLKSETFECNGSSVTLFELSALQRIEHLEFLKRQTEKVEVDSDFQAEAEFTVRSGAYLVAMSLWHWHPS
KSLQNENASQDVATIQQEVMTTWPTEALAAAEEKVLLLSGMIAPVIDEATENAEDRGEPAEPVTAEKS
>gnl|CDD|273749 TIGR01675, Acid_phosphatase_1, plant acid phosphatase. This model represents a family of acid phosphatase from plants which are most closely related to the (so called) class B non-specific acid phosphatase OlpA (TIGR01533, which is believed to be a 5'-nucleotide phosphatase) and somewhat more distantly to another class B phosphatase, AphA (TIGR01672). Together these three clades define a subfamily (pfam03767) which corresponds to the IIIB subfamily of the haloacid dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. It has been reported that the best substrate for this enzyme that could be found was purine 5'-nucleoside phosphates. This is in concordance with the assignment of the H. influenzae hel protein (from TIGR01533) as a 5'-nucleotidase, however there is presently no other evidence to support this specific function for these plant phosphatases. Many genes from this family have been annotated as vegetative storage proteins due to their close homology with these earlier-characterized gene products, which are highly expressed in leaves. There are significant differences however, including expression levels and distribution. The most important difference is the lack in authentic VSPs of the nucleophilic aspartate residue, which is instead replaced by serine, glycine or asparagine. Thus these proteins can not be expected to be active phosphatases. This issue was confused by the publication in 1992 of an article claiming activity for the Glycine max VSP. In 1994 this assertion was refuted by the separation of the activity from the VSP. This model explicitly excludes the VSPs which lack the nucleophilc aspartate. The possibility exists, however, that some members of this family may, while containing all of the conserved HAD-superfamily catalytic residues, lack activity and have a function related to the function of the VSPs rather than the acid phosphatases
LEILMKEKLSIDYGYCRSWRLGVETNNIRKWDTVPAECKDYVEDYMTSKQYKRDSKRVVDEAYFYAKSLA
LSGDGMDAWIFDVDDTLLSNIPYYKKHGYGTEKTDPTAFWDWLEKGEAPALPETLKLYQKLLELGIKIFL
LSGRWEELRSATVENLINAGFTGWKHLILRGLEDSQKTVVTYKSEVRKSLVEEGYRIVGNIGDQWSDLLG
SPPGRRTFKLPNPMYYVP
>gnl|CDD|130737 TIGR01676, L-galactono-gamma-lactone_dehydrogenase, galactonolactone dehydrogenase. This model represents L-Galactono-gamma-lactone dehydrogenase (EC 1.3.2.3). This enzyme catalyzes the final step in ascorbic acid biosynthesis in higher plants. This protein is homologous to ascorbic acid biosynthesis enzymes of other species: L-gulono-gamma-lactone oxidase in rat and L-galactono-gamma-lactone oxidase in yeast. All three covalently bind the cofactor FAD
DSELRKYIGYGALLIFCGAATYYSFPFPENAKHKKAQIFRYAPLPDDLHTVSNWSGTHEVLTRTFHQPEA
IEELEGIVKQANEKKARIRPVGSGLSPNGIGLSRAGMVNLALMDKVLEVDEEKKRVRVQAGIRVQQLVDA
IKEYGITLQNFASIREQQIGGIIQVGAHGTGAKLPPIDEQVIAMKLVTPAKGTIEISKDKDPELFFLARC
GLGGLGVVAEVTLQCVERQELVEHTFISNMKDIKKNHKKFLADNKHVKYLHIPYTDAIVVVTCNPISKSR
GPPKFKPKYTSEEAIQHVRDLYRESLKKYRGQVADSASEEPDIDEFSFTELRDKLLALDPLNKEHVIEIN
KAEAEFWRKSEGYKVGWSDEILGFDCGGHQWVSETCFPAGTLAKPNMKDIEYIEELKQLIEKENIPAPAP
IEQRWTACSKSPMSPASSSADDDIFSWVGIIMYLPTMDARQRKEITEEFFHYRHLTQALLWDHFSAFEHW
AKIEVPKDKDELAALQARLKKKFPVDASNKARKALDPNKILSNNKLEKLFI
>gnl|CDD|273750 TIGR01677, OSJNBb0057P11_genomic_sequence., plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown
PPDDPVRCVSGGANCTVSNAYGAFPDRSTCRAANVAYPKTEAELVSVVAAATAAGRKMKVVTRYSHSIPK
LACPDGSDGALLISTKRLNHVVAVDATAMTVTVESGMSLRELIVEAEKAGLALPYAPYWWGLTVGGMMGT
GAHGSSLWGKGSAVHDYVVGIRLVVPASAAEGFAKVRILSEGDTPNEFNAAKVSLGVLGVISQVTLALQP
MFKRSVTYTMRDDSDFEDQFVTFGKKHEFADITWYPSQGKAVYRRDDRVPVNASGNGVNDFLGFRSTLIA
AIAGIRALEETFERSRNANGKCVTATITSAALFLPGYGLTNSGGIIFTGYPVVGSQGRMQTSGSCLDSPQ
DGLLTACAWDPRYKGLFFFHQTTLSVPVSRFRDFVLDVKRLRDMEPKSLCGVELYNGILIRYVKASPAYL
GKEEDAVDFDFTYYRAKDPLTPRLYEDVIEEIEQMAFFKYGALPHWGKNRNLAFDGVIRKYPNADKFLKV
KDSYDPKGLFSSEWSDEILGIKGNASIKADGCALEGLCVCSEDAHCAPSKGYLCRPGKVYKEARVCT
>gnl|CDD|273751 TIGR01678, D-arabinono-14-lactone_oxidase, sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1
GVQFQNWAKTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSDIACTDGFLIHLDKMNKVL
QFDKEKKQITVEAGIRLYQLHEQLDEHGYSMSNLGSISEVSVAGIISTGTHGSSIKHGILATQVVALTIM
TADGEVLECSEERNADVFQAARVSLGCLGIIVTVTIQVVPQFHLQETSFVSTLKELLDNWDSHWKSSEFF
RVLWFPYTENVVIWRQNKTNKAPSSPSNSFWDYKLGFFLYEFLLWTSKYLPCLTPWIERFFFWMLYGEKS
STKKESSNLSHKIFTMECRFSQHVQEWGIPREKTKEALLELKAMLEAHAKNKEVYAHYPVEVRFTRGTLP
DECLLSPCFQVDTCYINAIMYRPFGKDVPRLDYFLAYETIMKKFGGKPHWAKAHNVCKQKDFEEMYPTLH
KFCDIRKKLDPTGVFLNS
>gnl|CDD|130740 TIGR01679, bact_FAD_ox, FAD-linked oxidoreductase. This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae
WSNWSGEQVAAPSAIVRPTDEGELADVIAQAAKPVRAVGSGHSFTDLACTDGTMISLTGLQGVVDVDQPT
GLATVEAGTRLGALGPQLAQRGLGLENQGDIDPQSIGGALGTATHGTGVRFQALHARIVSLRLVTAGGKV
LDLSEGDDQDMYLAARVSLGALGVISQVTLQTVALFRLRRRDWRRPLAQTLERLDEFVDGHRHFEFYVFP
FAGKALTITMDRSDEQPKPRQRDVDENFLGGLRLLRQTLRRFPSLRPRLNRLMTNMMSSETVVDRAYKVF
ATQRKVRFNEMEYHLPRENGRKALQEVIDLVERRSPPVMFPIEVRFSAPDDSWLSPFYGRPTCSIAVHQY
AGMDFESYFRAVEPIFRRYAGRPHWGKRHYLTAATLRERYPRWDDFAAVRDDLDPDRRFLNPYTRGLFG
>gnl|CDD|130741 TIGR01680, Stem_31_kDa_glycoprotein, vegetative storage protein. The proteins represented by this model are close relatives of the plant acid phosphatases (TIGR01675), are limited to members of the Phaseoleae including Glycine max (soybean) and Phaseolus vulgaris (kidney bean). These proteins are highly expressed in the leaves of repeatedly depodded plants. VSP differs most strinkingly from the acid phosphatases in the lack of the conserved nucleophilic aspartate residue in the N-terminus, thus, they should be inactive as phosphatases. This issue was confused by the publication in 1992 of an article claiming activity for the Glycine max VSP. In 1994 this assertion was refuted by the separation of the activity from the VSP
KCLVFFVAAILVASQCHGAAFDMFPLRMNTGYGAGARDPEVKCASWRLAVEAHNIFGFETIPEECVDATA
EYIEGEQYRSDSKTVNQQAYFFARDLEVHEKDTFLFNIDGTALSNIPYYKKHGYGSEKFDSELYDEEFVN
KGEAPALPETLKNYNKLVSLGFKIIFLSGRLKDKQAVTEANLKKAGYHTWEKLILKDPQDNSAENAVEYK
TAARAKLIQEGYNIVGIIGDQWNDLKGEHRGAIRSFKLPNPCTTFSSSFTSQQSSLLPIYLYVIK
>gnl|CDD|273752 TIGR01681, kDa_protein, HAD-superfamily phosphatase, subfamily IIIC. This model represents the IIIC subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. Subfamily III (also including IIIA - TIGR01662 and IIIB - pfam03767) contains sequences which do not contain either of the insert domains (between the 1st and 2nd conserved catalytic motifs, subfamily I - TIGR01493, TIGR01509, TIGR01549, TIGR01488, TIGR01494, TIGR01658, TIGR01544 and TIGR01545, or between the 2nd and 3rd, subfamily II - TIGR01460 and TIGR01484). Subfamily IIIC contains five relatively distantly related clades: a family of viral proteins (TIGR01684), a family of eukaryotic proteins called MDP-1 and a family of archaeal proteins most closely related to MDP-1 (TIGR01685), a family of bacteria including the Streptomyces FkbH protein (TIGR01686), and a small clade including the Pasteurella BcbF and EcbF proteins. The overall lack of species overlap among these clades may indicate a conserved function, but the degree of divergence between the clades and the differences in archetecture outside of the domain in some clades warns against such a conclusion. No member of this subfamily is characterized with respect to function, however the MDP-1 protein is a characterized phosphatase. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in subfamily IIIC
KVIVFDLDNTLWTGENIVVGEDPIIDLEVTIKEIRDKLQTLKKNGFLLALASYNDDPHVAYELLKIFEDF
GIIFPLAEYFDPLTIGYWLPKSPRLVEIALKLNGVLKPKSILFVDDRPDNNEEVDYYL
>gnl|CDD|273753 TIGR01682, Molybdopterin_synthase_sulfur_carrier_subunit, molybdopterin converting factor, subunit 1, non-archaeal. This model describes MoaD. It excludes archaeal homologs, since many Archaea have two MoaD-like proteins, suggesting two different functions. pfam02597 describes both the thiamine biosynthesis protein ThiS and this protein, MoaD, a subunit (together with MoaE, pfam02391) of the molybdopterin converting factor. Both ThiS and MoaD are involved in sulfur transfer reactions. Distribution of this family appears limited to species that also have a member of pfam02391, but a number of Archaea have two different members, suggesting functionally distinct subtypes. The C-terminal Gly-Gly of this model is critical to function [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
IKVLYFARLREQAGTDEETLELPDESTTVGELKEHLAKEGPELAASRGQVMVAVNEEYVTDDALLNEGDE
VAFIPPVSGG
>gnl|CDD|273754 TIGR01683, thiamine_biosynthesis_protein_ThiS, thiamine biosynthesis protein ThiS. This model represents ThiS, a small, ubiquitin-like thiamine biosynthesis protein related to MoaD, a molybdenum cofactor biosynthesis protein. Both proteins are involved in sulfur transfer. ThiS has a conserved Gly-Gly C-terminus that is modified, in reactions requiring ThiI, ThiF, IscS, and a sulfur atom from Cys, into the thiocarboxylate that provides the sulfur for thiazole biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
ITVNGEPVEVEDGTTLAALLESLGLDPRRVAVAVNGEIVPRSEWDDTILKEGDRIEIVTFVGGG
>gnl|CDD|273755 TIGR01684, kDa_protein, viral phosphatase. This model represents a family of viral proteins of unknown function. These proteins are members, however, of the IIIC (TIGR01681) subfamily of the haloacid dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. All characterized members of the III subfamilies (IIIA, TIGR01662; IIIB, pfam03767) are phosphatases, including MDP-1, a member of subfamily IIIC (TIGR01681). No member of this subfamily is characterized with respect to particular function. All of the active site residues characteristic of HAD-superfamily phosphatases are present in subfamily IIIC. These proteins also include an N-terminal domain (ca. 125 aas) that is unique to this clade
SWYCLRLRNPFFKRHVLFLASYADLKYVGFAALETIEFVVFLKDVVQMCFSKLIKQSDYKLQVFSCADDM
VDLRAHLKTAFKTSYFGHTFVLFHKPAMYACLNEWYVFELEEIYNLNLPSKVFEPPHVVVFDLDSTLITD
EEPVRIRDPRIYDSLTELKKRGCILVLWSYGDRDHVVESMRKVKLDRYFDIIISGGHKAEEYSTMSTEDR
QYRYVFTKTPFYLNTTDGKRLPKSPRVVLWYLYDLGVNYFKSITLVDDLADNNFNYDYFVNVSRCPVPVN
DWDSYHDQIVSNLREYDSLFV
>gnl|CDD|273756 TIGR01685, Putative_magnesium-dependent_phosphatase_YER134C, magnesium-dependent phosphatase-1. This model represents two closely related clades of sequences from eukaryotes and archaea. The mouse enzyme has been characterized as a phosphatase and has been positively identified as a member of the haloacid dehalogenase (HAD) superfamily by site-directed mutagenesis of the active site residues
LPRVIVFDLDGTLWDHYMISLLGGPFKPVKQNNSIIIDKSGTEVTLIKEVRDVLQTLKDAGTYLATASWN
DVPEWAYEILGTFEITYAGKTVPMHSLFDDRIEIYKPNKAKQLEMILQKVNKVDPSVLKPAQILFFDDRT
DNVREVWGYGVTSCYCPSGMDKGTFKKILEMWRS
>gnl|CDD|273757 TIGR01686, modular_polyketide_synthase, FkbH-like domain. This model describes a domain of a family of proteins of unknown overall function. One of these, however, is a modular polyketide synthase 4800 amino acids in length from Streptomyces avermilitis in which this domain is the C-terminal segment. By contrast, the FkbH protein from Streptomyces hygroscopicus aparently contains only this domain. The remaining members of the family all contain an additional N-terminal domain of between 200 and 275 amino acids which show less than 20% identity to one another. It seems likely then that these proteins are involved in disparate functions, probably the biosynthesis of different natural products. For instance, the FkbH gene is found in a gene cluster believed to be responsible for the biosynthesis of unususal "PKS extender units" in the ascomycin pathway. This domain is composed of two parts, the first of which is a member of subfamily IIIC (TIGR01681) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in this domain. The C-terminal portion of this domain is unique to this family (by BLAST)
PALKVLVLDLDNTLWGGVLGEDGIDNLNLSPLHKTLQEKIKTLKKQGFLLALASKNDEDDAKKVFERRKD
FILQAEDFDARSINWGPKSESLRKIAKKLNLGTDSFLFIDDNPAERANVKITLPVKTLLCDPAELAAILL
FLNELLPLANTKEDRIRAKDYAANALREELKELSDDEEYLQNLELSLNISKNDEQNVQRVEELLGRTNQF
NATYTRLNQEDVAQHMQKEEIVTVSMSDRFGDSGIIGIFVFEKKEGNLFIDDLCMSCRALGRGVETRMLR
WLFEQALDLGNHNARLYYRRTERNMPFLSFYEQIGFEDED
>gnl|CDD|273758 TIGR01687, long_hypothetical_molybdopterin, MoaD family protein, archaeal. Members of this family appear to be archaeal versions of MoaD, subunit 1 of molybdopterin converting factor. This model has been split from the bacterial/eukaryotic equivalog model TIGR01682 because the presence of two members of this family in a substantial number of archaeal species suggests that roles might not be interchangeable [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
VRVKYFATLRDITGKKSEEIEIEGKTVGDLLNELMARYPKEFSELFKEGLGLVPNVIILVNGRNVDWGLG
TELKDGDVVAIFPPVSGG
>gnl|CDD|130749 TIGR01688, D-alanine--polyphosphoribitol_ligase_subunit_2, D-alanine--poly(phosphoribitol) ligase, subunit 2. This protein is part of the teichoic acid operon in gram-positive organisms. Gram positive organisms incorporate teichoic acid in their cell walls, and in the fatty acid residues of the glycolipid component of the outer layer of the cytoplasmic membrane. This gene, dltC, encodes the alanyl carrier protein [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
KNGVLDILAEVTGSDDVKENPDLELFEEGLLDSFGTVQLLLEIQNQFDIDVPISEFDRDEWDTPNKIVAK
LEE
>gnl|CDD|273759 TIGR01689, capsular_polysaccharide_biosynthesis_protein, capsule biosynthesis phosphatase. This model describes a small family of highly conserved proteins (_60% ID). Two of these, BcbF and EcbF of Pasteurella multocida are believed to be part of the capsule polysaccharide biosynthesis machinery because they are cotranscribed from a locus devoted to that purpose. In pasteurella there are six different variant capsules (A-F), and these proteins are found only in B and E. The other two species in which this gene is (currently) found are both also pathogenic. These proteins are also members of the IIIC (TIGR01681) subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in this subfamily. Due to the likelihood that the substrates of these enzymes are different depending on the nature of the particular polysaccharides associated with each species, this model has been classified as a subfamily despite the close homology
MKRLVMDLDNTITLTENGDYANVAPILAVIEKLRHYKALGFEIVISSSRNMRTYEGNVGKINIHTLPIII
LWLNQHNVPYDEIYVGKPWCGHDGFYVDDRAIRPSEFSSLTYDEINTLTKIDKSCS
>gnl|CDD|162489 TIGR01690, ICE_RAQPRD, integrative conjugative element protein, RAQPRD family. This model represents a small family of proteins about 100 amino acids in length, including a predicted signal sequence and a perfectly conserved motif RAQPRD towards the C-terminus. Members are found in the Pseudomonas putida TOL plasmid pWW0 and in cryptic plasmid regions of Salmonella enterica subsp. enterica serovar Typhi and Pseudomonas syringae DC3000. The function is unknown [Mobile and extrachromosomal element functions, Plasmid functions]
LFLLLALALLVAASALADQASEREQLAAAIRQLDALERSAQRAAVVAPQSPGDRYHFDYPRLRADLKRIR
QGIQQYLTPSRAQPRDPSELAGDY
>gnl|CDD|273760 TIGR01691, putative_enolase-phosphatase, 2,3-diketo-5-methylthio-1-phosphopentane phosphatase. This enzyme is the enolase-phosphatase of methionine salvage, a pathway that regenerates methionine from methylthioadenosine (MTA). Adenosylmethionine (AdoMet) is a donor of different moieties for various processes, including methylation reactions. Use of AdoMet for spermidine biosynthesis, which leads to polyamine biosynthesis, leaves MTA as a by-product that must be cleared. In Bacillus subtilis and related species, this single protein is replaced by separate enzymes with enolase and phosphatase activities [Central intermediary metabolism, Sulfur metabolism]
IKNVLLDIEGTTGSISFVHDVLFPYAASRLESFVNDNYESTIVENLRELGKTPEELILLRKLHAEMDKDR
KATPLKTLQGLIWRQGYESGELTSHLYPDVPPALEAWLQLGLRLAVYSSGSVPAQKLLFGHSDAGNLTPY
FSGYFDTTVGLKTEAQSYVKIAGQLGSPPREILFLSDIINELDAARKAGLHTGQLVRPGNDPVVDPSFPV
YPQFPDLNAV
>gnl|CDD|130753 TIGR01692, 3-hydroxyisobutyrate_dehydrogenase_mitochondrial, 3-hydroxyisobutyrate dehydrogenase. 3-hydroxyisobutyrate dehydrogenase is an enzyme that catalyzes the NAD+-dependent oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde of the valine catabolism pathway. In Pseudomonas aeruginosa, 3-hydroxyisobutyrate dehydrogenase (mmsB) is co-induced with methylmalonate-semialdehyde dehydrogenase (mmsA) when grown on medium containing valine as the sole carbon source. The positive transcriptional regulator of this operon (mmsR) is located upstream of these genes and has been identified as a member of the XylS/AraC family of transcriptional regulators. 3-hydroxyisobutyrate dehydrogenase shares high sequence homology to the characterized 3-hydroxyisobutyrate dehydrogenase from rat liver with conservation of proposed NAD+ binding residues at the N-terminus (G-8,10,13,24 and D-31). This enzyme belongs to the 3-hydroxyacid dehydrogenase family, sharing a common evolutionary origin and enzymatic mechanism with 6-phosphogluconate. HIBADH exhibits sequence similarity to the NAD binding domain of 6-phosphogluconate dehydrogenase above trusted (pfam03446) [Energy metabolism, Amino acids and amines]
FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVY
SGDEGILPKVAKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFA
AAEPVLGPMGRNIVHCGDHGAGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWS
SDTYNPVPGVMPQAPASNGYQGGFGTALMLKDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDF
SSVIQLLR
>gnl|CDD|273761 TIGR01693, UTase_glnD [Protein-PII] uridylyltransferase. This model describes GlnD, the uridylyltransferase/uridylyl-removing enzyme for the nitrogen regulatory protein PII. Not all homologs of PII share the property of uridylyltransferase modification on the characteristic Tyr residue (see Prosite pattern PS00496 and document PDOC00439), but the modification site is preserved in the PII homolog of all species with a member of this family [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, Protein interactions]
REELLEEFARGGDGRELREGRSDLTDLLLIRLWDFIGISEHSGIALVAVGGYGRGELAPYSDIDLLFLHD
GKPAEEVEPKIERFLYPLWDLGFEVGHSVRTLEECARIAKADLTVATNLLEARHLAGDEALFFRLKERVR
REDWRNTARSFLAAKVEEQDERHARYGDTAYNLEPDIKEGPGGLRDLHTLFWVALYQLGVRRLEDLVKQG
FLTDAEYKLLAEARDFLWDVRFALHLTTGRADDRLLFDHQDEIAAALGYGDEGNPAVERFMRRYFQAARR
IGYLTEAFLRHYEEALLSRGPSARVRRPKRRPLDEGFVEDGGELVLARTAVFERDPALLLRLFAIAAQRG
LPIHPAALRQLTASLPLLPTPLREDPEARELFLELLTSGNGTVRALRAMNRAGVLGRFLPEWGRIVGQMQ
FDLFHVYTVDEHTLRTVVHLAPFARGRLAREHPLASELMPKIEDPELLYLAALLHDIGKGRGGDHSVLGA
EDARDVCPRLGLDRPDTELVAWLVRNHLLMSITAQRRDLNDPKTVFAFAEAVGDPERLEYLLALTVADIR
ATGPGVWNSWKASLLRDLYNRTEQVLRGGLEPPADPAEPIAEQRKLAVALLRTDYTSNEAEVLWLRAYDD
YFLRFTHKEIAWHAESLRRALSSGGPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQ
VNTTKDGVALDTFVVQDLFGSPPAAERVFQELLQGLVDVLAGLAKDPDTISARRARRRRLQHFAVPPRVT
ILNTASRKATIMEVRALDRPGLLARVGRTLEELGLSIQSAKITTFGEKAEDVFYVTDLFGLKLTDEEEQR
LLEVLAASVA
>gnl|CDD|273762 TIGR01694, S-methyl-5'-thioadenosine_phosphorylase, 5'-deoxy-5'-methylthioadenosine phosphorylase. This model represents the methylthioadenosine phosphorylase found in metazoa, cyanobacteria and a limited number of archaea such as Sulfolobus, Aeropyrum, Pyrobaculum, Pyrococcus, and Thermoplasma. This enzyme is responsible for the first step in the methionine salvage pathway after the transfer of the amino acid moiety from S-adenosylmethionine. The enzyme from human is well-characterized including a crystal structure. A misleading characterization is found for a Sulfolobus solfataricus enzyme, which is called a MTAP. In fact, as uncovered by the genome sequence of S. solfataricus, there are at least two nucleotide phosphorylases and the one found in the MTAP clade is not the one annotated as such. The sequence in this clade has not been isolated but is likely to be the authentic SsMTAP as it displays all of the conserved active site residues found in the human enzyme. This explains the finding that the characterized enzyme has greater efficiency towards the purines inosine, guanosine and adenosine over MTA. In fact, this mis-naming of this enzyme has been carried forward to several publications including a crystal stucture. In between the trusted and noise cutoffs are: 1) several archaeal sequences which appear to contain several residues characteristic of phosphorylases which act on guanosine or inosine (according to the crystal structure of MTAP and alignments). In any case, these residues are not conserved. 2) sequences from Mycobacterium tuberculosis and Streptomyces coelicolor which have better, although not perfect retention of the active site residues, but considering the general observation that bacteria utilize the MTA/SAH nucleotidase enzyme and a kinase to do this reaction, these have been excluded pending stronger evidence of their function, and 3) a sequence from Drosophila which appears to be a recent divergence (long branch in neighbor-joining trees) and lacks some of the conserved active site residues [Central intermediary metabolism, Other, Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
MIGVIGGSGLYDLEGLKDVEEVNVDTPYGNPSAPIVVGRVAGVDVAFLPRHGRGHDIPPHEVNYRANIWA
LKSLGVKYVISVNAVGSLREEYPPGDLVVPDQFIDRTSGRPSTFFDGGKVVHVDFGDPYCEDLRQRLIES
LRRLGLTVHDGGTYVCTEGPRFSTRAESRMFKSWGADIVGMTGVPEAVLARELELCYATLALVTDYDCWI
SADHVTAEEVEEVMGENVEKAKRILLEAIKK
>gnl|CDD|273763 TIGR01695, Putative_lipid_II_flippase_MurJ, murein biosynthesis integral membrane protein MurJ. This model represents MurJ (previously MviN), a family of integral membrane proteins predicted to have ten or more transmembrane regions. Members have been suggested to act as a lipid II flippase, translocated a precursor of murein. However, it appears FtsW has that activity. Flippase activity for MurJ has not been shown [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
SLLKSTLIVSLGTLFSRITGFVRDAIIASAFGAGLTADAFNVAFVIPNFFRRLFAEGAFNSAFVPVFTKA
KKKEKEARRAFANTVTTLLILSLLLVVLIGIFFAPFVISLLAPGFADETRSLAVSLTRIMFPYLLLISLA
AVFGGILNARKRFFIPSFSPILFNIGVILSLLFFDWNYGQYSLALAIGVLIGGVAQLLIQLPFLRKAGFL
LKPRFNFRDPGLKRFLKLFLPTTLGSSASQITLLINTALASFLEIGSVSALYYANRIYQLPLGIFGISLS
TVLLPKLSRHASEGNWNELRDLLNQGIRLSLLLTIPSSFGLLILSIPIVSLLFERGAFSEEDTVMTATIL
AAYGLGLIFYSLQKVLLRAFYARKDTRTPFINSVISVVLNALLSLLLIFPLGLVGIALATSAASMVSSVL
LYLMLNRRLKGILPFGVLKVLAKLVIASAIIGGVLYLIVSVSLGGVLVKNLLGLLAIGLIGLLVYFLGLA
LLKIEELNLLLR
>gnl|CDD|162494 TIGR01696, Phosphopentomutase_Phosphodeoxyribomutase., phosphopentomutase. This protein is involved in the purine and pyrimidine salvage pathway. It catalyzes the conversion of D-ribose 1-phosphate to D-ribose 5-phosphate and the conversion of 2-deoxy-D-ribose 1-phosphate to 2-deoxy-D-ribose 5-phosphate. The seed members of this protein are characterized deoB proteins from E.Coli(SP:P07651) and Bacillus (SP:P46353). This model matches pfam01676 for Metalloenzyme superfamily [Purines, pyrimidines, nucleosides, and nucleotides, Other]
RVFLIVMDSVGIGEAPDAADFGDEGAHTLGHIAEACAKLNLPNLTKLGLGKIHEPAGVDGNEEPIAYYAK
AHEASSGKDTMTGHWEIMGLPILFPFKVFPNGFPQELLQKLEERAGRKYLGNKPASGTVILDELGEEHMK
TGKLIVYTSADSVLQIAAHEETFPLEELYEICEIARELTTDPKYNIGRIIARPFVGEPGNFQRTGNRHDY
ALKPFAPTVLQKLKDEGHDVISIGKIADIYDGEGITKKVRTTSNMDGMDATIKEMKEDFTGISFTNLVDF
DALWGHRRDVAGYAAALELFDRRLPELFSLLREDDLLIITADHGNDPTWTGTDHTREYIPVLVYSPKVKP
GHSLGHRETFADIGATIADNFGTSDPEYGKS
>gnl|CDD|130758 TIGR01697, purine-nucleoside_phosphorylase, inosine/guanosine/xanthosine phosphorylase family. This model is a subset of the subfamily represented by pfam00896 (phosphorylase family 2). This model excludes the methylthioadenosine phosphorylases (MTAP, TIGR01684) which are believed toplay a specific role in the recycling of methionine from methylthioadenosine. In this subfamily is found three clades of purine phosphorylases based on a neighbor-joining tree using the MTAP family as an outgroup. The highest-branching clade (TIGR01698) consists of a group of sequences from both gram positive and gram negative bacteria which have been annotated as purine nucleotide phosphorylases but have not been further characterized as to substrate specificity. Of the two remaining clades, one is xanthosine phosphorylase (XAPA, TIGR01699), is limited to certain gamma proteobacteria and constitutes a special purine phosphorylase found in a specialized operon for xanthosine catabolism. The enzyme also acts on the same purines (inosine and guanosine) as the other characterized members of this subfamily, but is only induced when xanthosine must be degraded. The remaining and largest clade consists of purine nucleotide phosphorylases (PNPH, TIGR01700) from metazoa and bacteria which act primarily on guanosine and inosine (and do not act on adenosine). Sequences from Clostridium (GP:15025051) and Thermotoga (OMNI:TM1596) fall between these last two clades and are uncharacterized with respect to substrate range and operon
DVAIILGSGLGALADQVEDAVIIPYEKIPGFPVSTVVGHAGELVFGRLGGKPVVCMQGRFHYYEGYDMAT
VTFPVRVMKLLGVEILVVTNAAGGLNPDFKPGDLMIIKDHINLPGLNPLVGPNDDRFGTRFPDLSNAYDR
ELRKLAQDVAKELGFPLTEGVYVMVSGPSYETPAEIRMLRILGADAVGMSTVPEVIVARHCGIKVLAVSL
ITNMAAGITDVPLSHEEVLAAAAAAAERFISLLEDIIA
>gnl|CDD|130759 TIGR01698, Purine_nucleoside_phosphorylase, purine nucleotide phosphorylase. This clade of purine nucleotide phosphorylases has not been experimentally characterized but is assigned based on strong sequence homology. Closely related clades act on inosine and guanosine (PNPH, TIGR01700), and xanthosine, inosine and guanosine (XAPA, TIGR01699) neither of these will act on adenosine. A more distantly related clade (MTAP, TIGR01694) acts on methylthioadenosine
DMAIVLGSGWGGAVEALGEPVELPYAEIPGFPAPTVSGHAGELIRVRIGDGPVLVLGGRTHAYEGGDARA
VVHPVRTARATGAETLILTNAAGGLRQDWGPGTPVLISDHINLTARSPLIGPRFVDLTDAYSPRLRELAE
RVDPPLAEGVYAWFPGPHYETPAEIRMAGILGADLVGMSTVPETIAARFCGLEVLGVSLVTNLAAGITGT
PLSHAEVKAAGAAAGTRLAALLADIIK
>gnl|CDD|130760 TIGR01699, Purine_nucleoside_phosphorylase_2, xanthosine phosphorylase. This model represents a small clade of purine nucleotide phosphorylases found in certain gamma proteobacteria. The gene is part of an operon for the degradation of xanthosine and is induced by xanthosine. The enzyme is also capable of acting on inosine and guanosine (but not adenosine) in a manner similar to those other phosphorylases to which it is closely related (TIGR01698, TIGR01700)
RVAFILGSGLGALADQIENAVAISYEKLPGFPVSTVHGHAGELVLGHLQGVPVVCMKGRGHFYEGRGMTI
MTDAIRTFKLLGCELLFCTNAAGSLRPEVGAGSLVALKDHINTMPGTPMVGLNDDRFGERFFSLANAYDA
EYRALLQKVAKEEGFPLTEGVFVSYPGPNFETAAEIRMMQIIGGDVVGMSVVPEVISARHCDLKVVAVSA
ITNMAEGLSDVKLSHAQTLAAAELSKQNFINLICGFLR
>gnl|CDD|273764 TIGR01700, Purine_nucleoside_phosphorylase_1, purine nucleoside phosphorylase I, inosine and guanosine-specific. This model represents a family of bacterial and metazoan purine phosphorylases acting primarily on inosine and guanosine and not acting on adenosine. PNP-I refers to the nomenclature from Bacillus stearothermophilus where PHP-II refers to the nucleotidase acting on adenosine as the primary substrate.The bacterial enzymes (PUNA) are typified by the Bacilus PupG protein, which is involved in the metabolism of nucleosides as a carbon source.Several metazoan enzymes (PNPH) are well characterized including the human and bovine enzymes which have been crystallized [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
DIAIILGSGLGPLAEKVEDATIIDYSEIPHFPQSTVVGHAGNLVFGILGGKPVVAMQGRFHMYEGYDMAK
VTFPVRVMKLLGVETLVVTNAAGGINPEFKVGDLMLIRDHINLPGFNPLRGPNEERFGVRFPDMSDAYDR
DLRQKAHSIAKQLNIPLQEGVYVMLGGPSYETPAEVRLLRTLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKAAGILDYELSVHEEVMEAAKQAAEKLEKFVSLLIA
>gnl|CDD|273765 TIGR01701, Hypothetical_protein_Rv2900c/MT2968/Mb2924c., oxidoreductase alpha (molybdopterin) subunit. This model represents a well-defined clade of oxidoreductase alpha subunits most closely related to a group of formate dehydrogenases including the E. coli FdhH protein (TIGR01591). These alpha subunits contain a molybdopterin cofactor and generally associate with two other subunits which contain iron-sulfur clusters and cytochromes. The particular subunits with which this enzyme interacts and the substrate which is reduced is unknown at this time. In Ralstonia, the gene is associated with the cbb operon, but is not essential for CO2 fixation
DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVSPQTLAGLEFCENGAKAIAWETTP
RTIDPEFFAEHSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSLDPKQVAFY
TSGRTSNEAAYLYQLFARSLGSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAG
TNHPRMLKYLYAAKKRGAKIIAINPLRERGLERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGV
MKLLIEAEDAQPGSLIDHEFIANHTNGFDELRRHVLQLNWNDIERSSGLSQEEILEFAKLLANSRRVVFC
WAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGDRTMGITEKPEEEFLARLSQIYGF
TPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVATKLNRSHVLAKEEA
LILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVAWEILV
DTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAALCERKFPTPDGKANFIVIPLPEFRVPTGHEFELV
LVTLRSHDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQKRKFDNLRIVF
YDTPTGNAAAYYPEANPLLPLDHHDPQSKTPEYKTIPVRLEAS
>gnl|CDD|130763 TIGR01702, Carbon_monoxide_dehydrogenase, carbon-monoxide dehydrogenase, catalytic subunit. This model represents the carbon-monoxide dehydrogenase catalytic subunit. This protein is related to prismane (also called hybrid cluster protein), a complex whose activity is not yet fully described; the two share similar sets of ligands to unusual metal-containing clusters
SVDPAVKEMLEKAKDDGVETAFDRFEAQQPQCKFGLEGLCCRLCANGPCRISTTEGGPRGVCGADADTIV
ARNFLRMIAAGTAAYSHHAEHAARALKATAEGKTPYSIKDEAKLKWLAKKLGIDTEGDSNELAVEVAEIV
LSDFRKPREEKAELVEAFAPEKRKEKWEKLGILPGGIKAEVSDAVSKTHTNLDSDPVNLAVKALRLGIAT
GLTGLILATDLSDILFGTPQPVVSEANLGVMDPDYVNIVVNGHQPLLSEILCEAARDEDIQDEAKAAGAK
GINIVGICCTGQEVLMRQGHYVFVGLAGNNLSQELLIATGAIDAMVVDVNCTMPSIPAIAECYHTKIITV
DDNAKIPGADHIPYDPEKAEETAKTIIRMAIEAFKERKENQPVYIPQQKQKVVVGFSEEALVKALGGQNK
PLVDAIASGKIKGVVLVVGCSNLKNGGQDSSTVTLTKELIKRNILVLATGCSNGALEKAGLMTPEAAEEL
AGEGLKGVCKALGIPPVLHFGSCVDNGRAVDLATALAEDLGVDIPQLPLVASAPEWMEEKALADGTFAVS
LGLPTHVSPVPPVTGSELVTKLLTEDAEDLTGGKFIVEEDPQKAADKLEDAIEERRKKLGL
>gnl|CDD|130764 TIGR01703, Hydroxylamine_reductase, hydroxylamine reductase. This model represents a family of proteins containing an unusual 4Fe-2S-2O hydrid cluster. Earlier reports had proposed a 6Fe-6S prismane cluster. This subfamily is heterogeneous with respect to the presence or absence of a region of about 100 amino acids not far from the N-terminus of the protein. Members have been described as monomeric. The general function is unknown, although members from E. coli and several other species have hydroxylamine reductase activity. Members are found in various bacteria, in Archaea, and in several parasitic eukaryotes: Giardia intestinalis, Trichomonas vaginalis, and Entamoeba histolytica [Cellular processes, Detoxification, Energy metabolism, Amino acids and amines]
MFCYQCEQTARGTGCTVRGVCGKDPETANLQDLLVYVLKGISLWALQARKLGIDSEIDSFIPRALFSTLT
NVNFDEDRIVEYIEDAIKLREKLKKKCRLADSNSLLIQSFALNGDKSHVNDDVNSLRDLLLYGIKGIAAY
LYHARELGYDDEEIYAFLEEALASTLTNVFDADELIDLALEVGKMNLEAMKLLDKANTETYGLPEPTEVN
IGTTEGKAILVSGHDLKDLEELLEQTEGTGINVYTHGEMLPAHGYPELKKYPHLAGNYGGAWQDQQREFA
EFPGPILMTSNCIIPPRKSYKDRIFTTGIVGWPGVKHIENYDFSPVIEKALELPGFPKELEEGTITTGFG
HHTILALADKIVELVKEGKIRHFFLVGGCDGPNPERNYYTEFARKLPKDAIILTLACGKYRFNKLDLGDI
EGIPRLLDLGQCNDAYSAIEIALKLAEVFGCDVNELPLSIVLSWYEQKAIAILLALLYLGVKNIYIGPTL
PGFLTPNVFKILVDNFDLRLIGEPEDDLRAIL
>gnl|CDD|130765 TIGR01704, MTA/SAH-Nsdase, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase. This model represents the enzyme 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase which acts on its two substrates at the same active site. This enzyme is involved in the recycling of the components of S-adenosylmethionine after it has donated one of its two non-ribose sulfur ligands to an acceptor. In the case of 5-methylthioadenosine this represents the first step of the methionine salvage pathway in bacteria. This enzyme is widely distributed in bacteria, especially those that lack adenosylhomocysteinase (EC 3.3.1.1). One clade of bacteria including Agrobacterium, Mesorhizobium, Sinorhizobium and Brucella includes sequences annotated as MTA/SAH nucleotidase, but differs significantly in homology and has no independent experimental evidence. There are homologs of this enzyme in plants, some of which score between trusted and noise cutoffs here, but there is no experimental evidence to validate this function at this time [Central intermediary metabolism, Other, Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVI
INTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAV
RGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFL
AVAAKQSSLMVESLVQKL
>gnl|CDD|130766 TIGR01705, MTA/SAH-nuc-hyp, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase, putative. This model represents the enzyme 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase which acts on its two substrates at the same active site. This clade of sequences is sufficiently distinct from the characterized proteins, which form the seed of TIGR01704 as to cast some doubt on the accuracy of annotations based on sequence similarity alone. This enzyme is involved in the recycling of the components of S-adenosylmethionine after it has donated one of its two non-ribose sulfur ligands to an acceptor. In the case of 5'-methylthioadenosine this represents the first step of the methionine salvage pathway in bacteria. This enzyme is widely distributed in bacteria
MMANISHIADKDVLFVMAAQAEYGPHLQALFAPLMTGVGPVEAAIRVGAELAGLDAADALPDLVVSLGSA
GSRTLEQTEIYQAVSVSYRDIDASAFGFEKGATPFLDLPAEAALPFRIPDIAEARLSTGGAIISGAAYDA
IAADMVDMETFACLRACQLFDVPLIGLRGISDGAADLNHVDDWTAYLDIIDEKLADAVDRLCQAIEDGLI
AI
>gnl|CDD|273766 TIGR01706, Periplasmic_nitrate_reductase, periplasmic nitrate reductase, large subunit. This model represents the large subunit of a family of nitrate reductases found in proteobacteria which are localized to the periplasm. This subunit binds molybdopterin and contains a twin-arginine motif at the N-terminus. The protein associates with NapB, a soluble heme-containing protein and NapC, a membrane-bound cytochrome c. The periplasmic nitrate reductases are not involved in the assimilation of nitrogen, and are not directly involved in the formation of electrochemical gradients (i.e. respiration) either. Rather, the purpose of this enzyme is either dissimilatory (i.e. to dispose of excess reductive equivalents) or indirectly respiratory by virtue of the consumption of electrons derived from NADH via the proton translocating NADH dehydrogenase. The enzymes from Alicagenes eutrophus and Paracoccus pantotrophus have been characterized. In E. coli (as well as other organisms) this gene is part of a large nitrate reduction operon (napFDAGHBC) [Energy metabolism, Aerobic, Energy metabolism, Electron transport, Central intermediary metabolism, Nitrogen metabolism]
KISRRDFIKATAIASAASVAGLSLPAQAANMVGGQEETAIKWDKAPCRFCGTGCGVMVGVKDGRVVATQG
DPAAPVNRGLNCIKGYFLSKIMYGQDRLTQPLLRMKDGKYDKDGEFTPVSWDQAFDEMEEQFKRALKEKG
PTAIGMFGSGQWTIWEGYAALKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDFEAADAF
VLWGSNMAEMHPILWTRVTDRRLSHPKVKVVVLSTFTHRSFDLADIGIIFKPQTDLAILNYIANYIIQNN
AVNMDFVNKHTVFKTGATDIGYGLRPDHPLEKAAKNADDPAATSLSTFEEFKKFVAPYTLEKTSELSGVP
KAKLEQLAELYADPNRKVMSLWTMGFNQHTRGVWANNMVYNLHLLTGKIATPGNSPFSLTGQPSACGTAR
EVGTFSHRLPADMVVTNPKHREIAEKIWKIPAGTIPEKPGLHAVAQDRALKDGKLNFYWVQVNNNMQAGP
NINEERLPGYRNPDNFIVVSDAYPTVTALAADLILPSAMWVEKEGAYGNAERRTQVWHQQVLAPGEARSD
LWQLVEFSKRFKTEEVWPEELLAKKPEYRGKTLYDVLFANGEVDKFPLSEANAKSLNAESTAFGFYVQKG
LFEEYAKFGRGHGHDLAPFDTYHKVRGLRWPVVNGKETQWRYREGSDPYVKAGAGFQFYGNPDGKAVIFA
LPYEPPAERPDEEYPLWLVTGRVLEHWHSGSMTRRVPELYRAFPEALCFMHPEDAKALGLRRGDEVWVVS
RRGEVRSRVETRGRNKPPRGLVFVPWFDASQLINKVTLDATDPLSKQTDFKKCAVKIYKV
>gnl|CDD|273767 TIGR01707, Type_II_secretion_system_protein_I, type II secretion system protein I. This model represents GspI, one of two proteins highly conserved at their N-termini and described by pfam02501 but easily separable phylogenetically. The other is GspJ. Both GspI and GspJ are proteins of the type II secretion pathway, or main terminal branch of the general secretion pathway. This pathway carries proteins across the outer membrane. Note that proteins of type II secretion are cryptic in E. coli K-12 - present but not yet demonstrated to act on any target
GFTLLEVLVALAIFAAAALALISSVGGQTNAIGRLRDKTLALWIADNRLAELSLGVGPPALGRNSGKELI
AGREWLWRSQVHSTDDPTLLRVDITVATPSG
>gnl|CDD|130769 TIGR01708, Type_II_secretion_system_protein_H, type II secretion system protein H. This model represents GspH, protein H of the main terminal branch of the general secretion pathway, also called type II secretion. It transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
HRQSGFTLIELLVVLAIMGLVAAAAALSLVSHYGTKSLDQVAGRLAARLRLAQTSARATGRPVLLRLGSR
GIRFGERASLALPVDEVKMTDWTGQETVVADRQTVLTVLFLPDGRASPMDMTLQRKGRSVTVAVNWLGGL
RLW
>gnl|CDD|273768 TIGR01709, Type_II_secretion_system_protein_L, type II secretion system protein L. This model represents GspL, protein L of the main terminal branch of the general secretion pathway, also called type II secretion. It transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens [Protein fate, Protein and peptide secretion and trafficking]
LLLRLGSTAEEAIEWRVWSQGEGGITGRAALQALAPPDPAAAVVLLVPAEDVLLRSVPLPPGKAAQLRQA
LPFLLEEELAQDVEDLHFAVLPRDAEGATRVAVVDREWLQAWLDLLTEAGLAPERVVPDPLALPEPESGW
AAVALLTEWLVRGSAGQGLVASELWAQHLAALEPPAALLAYGELPAALGADPEPQALPGTELVALLAAPA
LFPPINLLTGPFAPRRSGRRQLARWRRALGAAAVLLVLSLVGAGLQAWQVARQLDQLRAQSAETYRQLFP
EAKKVVNPRTQFKAELSRLAAQGSGQGFLDLLAALATALGQLPGLQLQSLDFDGARGELRLKLEAPSDAD
LEQLRSRLARGFQVALGQAGAEGDSVSGQLTLRP
>gnl|CDD|130771 TIGR01710, Type_II_secretion_system_protein_G, type II secretion system protein G. This model represents GspG, protein G of the main terminal branch of the general secretion pathway, also called type II secretion. It transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
RGFTLLEIMVVLVILGLLAALVAPKLFSQADKAKAQVAKAQIKALKNALDMYRLDNGRYPTEEQGLAALV
TKPSGEPLPKNWHGGYLEKVPQDPWGNPYQYRDPGENGPYDLYSLGADGQPGGKGTDADIGNWD
>gnl|CDD|130772 TIGR01711, Type_II_secretion_system_protein_J, type II secretion system protein J. This model represents GspJ, one of two proteins highly conserved at their N-termini and described by pfam02501 but easily separable phylogenetically. The other is GspI. Both GspI and GspJ are proteins of the type II secretion pathway, or main terminal branch of the general secretion pathway. This pathway carries proteins across the outer membrane. Note that proteins of type II secretion are cryptic in E. coli K-12 - present but not yet demonstrated to act on any target
RGFTLLELLVAIAIFASLSLGAYQVLDSVMQSDEATRVQEARLRELQRAMGAMERDLTQMVERPVRDDGE
ASEQDLRGAFLSEGSDDQGVEFTRGGWRNPLGQQPRSRLQRVGWRLSGETLERRYWLYPDRAQGSKPRIQ
PVLDGVTALSWRFYDKGNWQGEWPTDNSLPLAVEVTLELRDYGKLVRVWLLG
>gnl|CDD|273769 TIGR01712, DNA_N-6-adenine-methyltransferase_M.T1, phage N-6-adenine-methyltransferase. This model is a fragment-mode model for a phage-borne DNA N-6-adenine-methyltransferase [Mobile and extrachromosomal element functions, Prophage functions, DNA metabolism, Restriction/modification]
YKGTNTPDAVRDLWSTPREVFAYLEGRYGKFDLDAAASEENAVCAKFYTQEDNALKRWWGKNKAVWLNPP
YSRPDIFVNKTAWFTEARQAAEVILIEADLSTVWWPEDIDGNEYIRSGRIAFISPETGKEKDGNNKGSVI
FIMREFKEGEVQQTHYIPITSLCASG
>gnl|CDD|273770 TIGR01713, Type_II_secretion_system_protein_C, type II secretion system protein C. This model represents GspC, protein C of the main terminal branch of the general secretion pathway, also called type II secretion. This system transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens [Protein fate, Protein and peptide secretion and trafficking]
LILTFILLVFISQQLGYILWNVSLPINFVPTIVVSKQISVNLANLQPSDLKLFELFGVFNEKSVSEVKTS
PVSVNAPVSPLSLKLTGIVASSDRIRSIAIIEEGSEQVSLGINESFEGYKAKIAKIEPDRVIFEYNGRYE
PLELKNTKGEKSNNSSEIVVSRRIIEELTKDPQKMFDYIRLSPVMKNDKLEGYRLNPGKDPSLFYKSGLQ
DGDIAVALNGLDLRDPEQAFQALQMLREETNLTLTVERDGQREDIYVRF
>gnl|CDD|130775 TIGR01714, hypothetical_phage_protein, phage replisome organizer, putative, N-terminal region. This model represents the N-terminal domain of a small family of phage proteins. The protein contains a region of low-complexity sequence that reflects DNA direct repeats able to function as an origin of phage replication. The region covered by this model is N-terminal to the low-complexity region [Mobile and extrachromosomal element functions, Prophage functions]
WIKLKVNFFDSKEIKLLEKMPEGDTHTIIWLKLLLLSLNDGGCIYLNELAPYNAEMLATMFNRNVGDIRI
TLQTLESLGLIEKKNNGDIFLENWEKHVGSDSASARRERKFRRNQKALE
>gnl|CDD|273771 TIGR01715, Gifsy-2_prophage_probable_minor_tail_protein, phage tail assembly protein T. This model represents a translation of the T gene in phage lambda and related phage. A translational frameshift from the upstream gene G into the frame of T produces a minor protein gpG-T, essential in tail assembly but not found in the mature virion [Mobile and extrachromosomal element functions, Prophage functions]
FRRPDWRAMLAEMSSTELGEWARFFRTNSFSDALLDAEFSTLKYAVSSLVTGPEMDASDFSLLTEPQTER
PDTDDMLMRKAAGISGGVRFGPDSE
>gnl|CDD|273772 TIGR01716, HTH-type_transcriptional_regulator_rgg, transcriptional activator, Rgg/GadR/MutR family, C-terminal domain. This model describes the whole, except for a 60 residue N-terminal helix-turn-helix DNA-binding domain (pfam01381) of the family of proteins related to the transcriptional regulator Rgg, also called RopB. Rgg is required for secretion of several proteins, including a cysteine proteinase associated with virulence. GadR is a positive regulator of a glutamate-dependent acid resistance mechanism. MutR is a transcriptional activator for mutacin biosynthesis genes in Streptococcus mutans. This family appears restricted to the low-GC Gram-positive bacteria, including at least eight members in Lactococcus lactis [Regulatory functions, DNA interactions]
YILNNYKESEKESFGEKIVEAFYSNDIVGLKSLLSKISETKETYNRLNKAVIKARLHTLDHSYILSEEEV
EFLTDYLFNIEEWTYYELYLFGNTMSILNSEDLEFLGKELLERLKRYRELNRYRRRVIQLLLNIAVLLIE
KNEFSYAQYFLEKLEKILDPEDDLYERILFNFLKGIILYKEGQKESGEEKIEQAIEIFDELGYPTLAAYY
QKLLEKFVKK
>gnl|CDD|273773 TIGR01717, AMP_nucleosidase., AMP nucleosidase. This model represents the AMP nucleosidase from proteobacteria but also including a sequence from Corynebacterium, a gram-positive organism. The species from E. coli has been most well studied
PAEAVDKLDALYEQSTAALRNALGNYIKSGELPDENYRKQGLFVYPQLTVTWDGSGTVDKTRAFGRVTHA
GSYTTTITRPDLFRSYLNEQLTLLYQDYGVHISVQPSQHEIPYPYVIGAGSELEADRAGSAGLARYFPTT
DLAQIGDEIADGDYIYHPGEFLPLAHFDAQRVDFSLARLRHYTGTPVEHFQPFVLFTNYTRYVDEFVRWG
CSQLLDPDSRYVALSLPGGNVITAETDAPEEAISDLLWKRHQMPAYHLITADGDGITLVNIGVGPSNAKT
ITDHLAVLRPHAWLMIGHCGGLRESQRIGDYVLAHAYLREDHVLDAVLPPDIPIPAIAEVQRALEDAVAE
VTGRPGEELKRRLRTGTVLTTDDRNWELRYSASALRLNLSRAIAVDMESATIAAQGYRFRVPYGTLLCVS
DKPLHGEIKLPGQANAFYEGAVSQHLQIGIRAIDLLRAEGDRLHSRKLRTFNEPPFR
>gnl|CDD|130779 TIGR01718, Uridine_phosphorylase, uridine phosphorylase. This model represents a family of bacterial and archaeal uridine phosphorylases unrelated to the mammalian enzymes of the same name. The E. coli, Salmonella and Klebsiella genes have been characterized. Sequences from Clostridium, Streptomyces, Treponema, Halobacterium and Pyrobaculum were included above trusted on the basis of sequence homology and a PAM-based neighbor-joining tree. A clade including second sequences from Halobacterium and Vibrio was somewhat more distantly related and may represent a slightly different substrate specificity - these were placed below the noise cutoff. More distantly related is a clade of archaeal sequences which as related to the DeoD family of inosine phosphorylases (TIGR00107) as they are to these uridine phosphorylases. This clade includes a characterized protein from Sulfolobus solfataricus which has been mis-named as a methylthioadenosine phosphorylase, but which acts on inosine and guanosine - it is unclear whether uridine has been evaluated as a substrate [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
VYHLGLTKNDIQTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIA
VEELAQLGARTFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESI
GVRHHVGVVASSDTFYPGQERDTYSGRVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAG
VIVNRTQQEIPNEETMKQTEEHAIKVAVEAVKRLL
>gnl|CDD|130780 TIGR01719, Uridine_phosphorylase_1, uridine phosphorylase. This model represents a clade of mainly eucaryotic uridine phosphorylases. Genes from human and mouse have been characterized. This enzyme is a member of the PHP/UDP subfamily (pfam01048) and is closely related to the bacterial uridine (TIGR01718) and inosine (TIGR00107) phosphorylase equivalogs. In addition to the eukaryotes, a gene from Mycobacterium leprae is included in this equivalog and may have resulted from lateral gene transfer [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLSCGRDYPNISERGD
RFAMYKVGPVLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACL
KPEYEQIVLGKRVIRPTQLDEALVQELLLCGAEGLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDK
MAYLRKLYALGVRNIEMESSMFAAMTSRAGFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRY
IKKKLSK
>gnl|CDD|273774 TIGR01720, Includes:_ATP-dependent, non-ribosomal peptide synthase domain TIGR01720. This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant
ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEKLAASPQPEISFNYLGQFDADSNDELFQPSSYSPGE
AISPESPRPYALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDF
SLKDLTQDELDEL
>gnl|CDD|130782 TIGR01721, AMN-like, AMP nucleosidase, putative. The sequences in the clade represented by this model are most closely related to the AMP nucleosidase found in TIGR01717. These sequences are found only in Chlamydia and Porphyromonas and differ sufficiently from the characterized AMP nucleosidase to put some doubt on assignment of this name
KSEQEIAEDMLERYTGSQLIDFEPYLLLTNFSYYLHVFAEHYGVPVVEGSMFSAAHAPAEGTSIIDFKLG
SPGAALIXDLCSFLPHPKAAIMLGMCGGLRSHYQVGDYFVPVASIRGEGTSDAYFPPEVPALANFVVQKA
ITSALENKGKDYHIGITHTTNIRFWEFNKKFRDKLYETKAQGVEMECATLFTAGYRRNLPXGALLLISDL
PLRPEGIKTKESDQLVTDTYTEEHILTGIEVLEILRERAASDHKKSSGLPHMEFGW
>gnl|CDD|130783 TIGR01722, Methylmalonate-semialdehyde_dehydrogenase, methylmalonic acid semialdehyde dehydrogenase. Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus [Energy metabolism, Amino acids and amines]
VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQ
ALLKEHRDEIAELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVC
AGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLL
EHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMA
ISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYK
VDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARR
FQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW
>gnl|CDD|130784 TIGR01723, 510-methenyltetrahydromethanopterin_hydrogenase, 5,10-methenyltetrahydromethanopterin hydrogenase. This model represents a clade of authenticated coenzyme N(5),N(10)-methenyltetrahydromethanopterin reductases. This enzyme does not use F420. This enzyme acts in methanogenesis and as such is restricted to methanogenic archaeal species. This clade is one of two clades in pfam03201 [Energy metabolism, Methanogenesis]
MKLAILGAGCYRTHAASGITNFSRACEVAEEVGKPEIALTHSSITYGAELKHLAGVDEVVVSDPVFDNEG
FTVIDDFDYEEVIEAHLEGNPEKIMPKIREKVNEVAKELPKPPKGAIHFTHPEDLGFEVTTDDREAVEDA
DFIITWLPKGDMQPDIIKKFIDDIPEGAIVTHACTIPTTKFYKIFEDKGREDLNVTSYHPGAVPEMKGQV
YIAEGYASEEAVNTLYELGQKARGNAFKLPAELLGPVCDMCSAVTAIVYAGLLSYRDAVTQILGAPADFA
QMMAKEALEQITALMEEVGIDKMEEALDPAALLGTADSMNFGPLAEILPTALEVLEKRKK
>gnl|CDD|130785 TIGR01724, hmd_rel, H2-forming N(5),N(10)-methenyltetrahydromethanopterin dehydrogenase-related protein. This model represents a sister clade to the authenticated coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase (HMD) of TIGR01723. Two members, designated HmdII and HmdIII, are found. Members are restricted to methanogens, but the function is unknown [Unknown function, Enzymes of unknown specificity]
MKVSVYGAGNQKLYTDELNLPEKFGGEPPYGGSRMAIEFAMAGHDVVLAEPNREFMSDDLWKKVEDAGVK
VVSDDKEAAKHGEIHVLFTPFGKGTFSIARTIIEHVPENAVICNTCTVSPVVLYYSLEKILRLKRTDVGI
SSMHPAAVPGTPQHGHYVIGGKPTAGKEMATEEQISKCVELAKSTGKKAYVVPADVTSAVADMGSLVTAV
ALAGVLDYYYVGTQIINAPKEMIEKQILMTLQTMASLVETSGVEGMAKAINPELLVKSARSMHLLDRQED
LDAALKIISDLDDDVMKWIEGAEINHTDLVAAQALTKELKTLIGDRAAEGTIRRSMRKLFE
>gnl|CDD|273775 TIGR01725, hypothetical_protein, phage protein, HK97 gp10 family. This model represents an uncharacterized, highly divergent bacteriophage family. The family includes gp10 from HK022 and HK97. It appears related to TIGR01635, a phage morphogenesis family believed to be involved in tail completion [Mobile and extrachromosomal element functions, Prophage functions]
FTGLDELLQKLEKLGKKVDKEKVRKALKAGANVIRAKLKSNAPVSKGKKHGSLRDSIVKQKDNGVLSVTV
GPGKTAWYARFLEFGTRYMPAQPFMRPAFKQNKPKVIKIMIEELEALIK
>gnl|CDD|130787 TIGR01726, Glutamine_transport_system_permease_protein_glnP., amine acid ABC transporter, permease protein, 3-TM region, His/Glu/Gln/Arg/opine family. This model represents one of several classes of multiple membrane spanning regions found immediately N-terminal to the domain described by pfam00528, binding-protein-dependent transport systems inner membrane component. The region covered by this model generally is predicted to contain three transmembrane helices. Substrate specificities attributed to members of this family include histidine, arginine, glutamine, glutamate, and (in Agrobacterium) the opines octopine and nopaline [Transport and binding proteins, Amino acids, peptides and amines]
NLPFLLKGLLLTLLLSVLSILLGLVLGLLLALLRLSGNRPLRWIATVYVELFRGTPLLVQLFFIYFGLPL
IGIRLSPLTAAVIALTLFYGAYLAEIFRG
>gnl|CDD|213647 TIGR01727, various_ABC-type_transport_systems, oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain. This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid [Transport and binding proteins, Amino acids, peptides and amines]
KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKE
PPALVEIAEGHRVACHL
>gnl|CDD|130789 TIGR01728, Putative_aliphatic_sulfonates-binding_protein, ABC transporter, substrate-binding protein, aliphatic sulfonates family. Members of this family are substrate-binding periplasmic proteins of ABC transporters. This subfamily includes SsuA, a member of a transporter operon needed to obtain sulfur from aliphatic sulfonates. Related proteins outside the scope of this model include taurine (NH2-CH2-CH2-S03H) binding proteins, the probable sulfate ester binding protein AtsR, and the probable aromatic sulfonate binding protein AsfC. All these families make sulfur available when Cys and sulfate levels are low. Please note that phylogenetic analysis by neighbor-joining suggests that a number of sequences belonging to this family have been excluded because of scoring lower than taurine-binding proteins [Transport and binding proteins, Other]
VRIGYQKNGHSALALAKEKGLLEKELGKTKVEWVEFPAGPPALEALGAGSLDFGYIGPGPALFAYAAGAD
IKAVGLVSDNKATAIVVIKGSPIRTVADLKGKRIAVPKGGSGHDLLLRALLKAGLSGDDVTILYLGPSDA
RAAFAAGQVDAWAIWEPWGSALVEEGGARVLANGEGIGLPGQPGFLVVRREFAEAHPEQVQRVLKVLVKA
RKWAEENPEESAKILAKELGLSQAVVEETVLNRRFLRVEVISDAVVDALQAMADFFYAAGLLKKKPDLKD
AVDRSFLK
>gnl|CDD|130790 TIGR01729, Taurine-binding_periplasmic_protein, taurine ABC transporter, periplasmic binding protein. This model identifies a cluster of ABC transporter periplasmic substrate binding proteins, apparently specific for taurine. Transport systems for taurine (NH2-CH2-CH2-SO3H), sulfonates, and sulfate esters import sulfur when sulfate levels are low. The most closely related proteins outside this family are putative aliphatic sulfonate binding proteins (TIGR01728)
VTVGYQTIVEPFKVAQADGAAAKEAGATIDWRKFDSGADISTALASGNVPIGVIGSSPLAAAASRGVPIE
LFWILDNIGKSEALVAREGSGIEKPEDLKGKNVAVPFVSTTHYSLLAALKHWKTDPREVNILNLKPPQIV
AAWQRGDIDAAYVWPPALSELLKSGKVISDSEQVGAWGAPTFDGWVVRKDFAEKNPEFVAAFTKVLADAY
ADYKANPDGWKADSPQVQKMAKLIGGDAEGVPQLLKGLSFPTADEQVSDKWLGGGAVKALEASAKFLKEQ
GKVDAVLDDYSPYVTSAYVK
>gnl|CDD|273776 TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane [Transport and binding proteins, Unknown substrate]
VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAAL
AQLAAAEAQLELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAP
FDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFI
DPRVDSGTGTVRVRATFPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSK
RPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGAKVKVV
>gnl|CDD|273777 TIGR01731, hemolysin/hemagglutinin-like_protein_HecA, adhesin HecA family 20-residue repeat (two copies). This model represents two copies of a 20-residue repeat found in Bordetella pertussis filamentous hemagglutinin family of adhesins. This family includes extremely long proteins from a number of plant and animal pathogens
GKISAGGALTLRAGSLDNRGGLLSSGGDLTLSAGSLDNRG
>gnl|CDD|273778 TIGR01732, tiny_TM_bacill, conserved hypothetical tiny transmembrane protein. This model represents a family of hypothetical proteins, half of which are 40 residues or less in length. Members are found only in spore-forming species. A Gly-rich variable region is followed by a strongly conserved, highly hydrophobic region, predicted to form a transmembrane helix, ending with an invariant Gly. The consensus for this stretch is FALLVVFILLIIV [Hypothetical proteins, Conserved]
GGGYGGGFALIVVLFILLVIVGAAFV
>gnl|CDD|273779 TIGR01733, non-ribosomal_peptide_synthetase, amino acid adenylation domain. This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -_ aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group
TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILED
AGARLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVV
THRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAE
HPVTVLNLTPSLLALLAAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTAT
LVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFA
GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV
>gnl|CDD|273780 TIGR01734, D-alanine--polyphosphoribitol_ligase_subunit_1, D-alanine--poly(phosphoribitol) ligase, subunit 1. This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -_ D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
KLIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGS
IKSGHAYIPVDTSIPSERIEMIIEAAGPELVIHTAELSIDAVGTQIITLSALEQAETSGGPVSFDHAVKG
DDNYYIIYTSGSTGNPKGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTL
HCLDKDITNNFKLLFEELPKTGLNVWVSTPSFVDMCLLDPNFNQENYPHLTHFLFCGEELPVKTAKALLE
RFPKATIYNTYGPTEATVAVTSVKITQEILDQYPRLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGP
SVSKGYLNNPEKTAEAFFSHEGQPAYRTGDAGTITDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSY
IESAVVVPKYNKDHKVEYLIAAIVPETEDFEKEFQLTKAIKKELKKSLPAYMIPRKFIYRDQLPLTANGK
IDRKALAEEVNG
>gnl|CDD|188163 TIGR01735, Phosphoribosylformylglycinamidine_synthase, phosphoribosylformylglycinamidine synthase, single chain form. This model represents a single-molecule form of phosphoribosylformylglycinamidine synthase, also called FGAM synthase, an enzyme of purine de novo biosynthesis. This form is found mostly in eukaryotes and Proteobacteria. In Bacillus subtilis PurL (FGAM synthase II) and PurQ (FGAM synthase I), homologous to different parts of this model, perform the equivalent function; the unrelated small protein PurS is also required and may be a third subunit [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
FLRGPSALSGFRLEKLLQKLQTKVPELTGVYAEFCYFVGWESALTADEEEKLQLLLLAGSVLEPPQSPLG
RGLLEVGPRLGTISPWSSKATSIARNCGLAKVDRIERGRRYYLSGAHPLSEEQEAQAAALLHDRMTESVL
PHEIEAFELFSVPEPLNLTTIDVLGGGRLALEKANQELGLALDEDEIDYLTKRFQELQRNPSDVELMMFA
QANSEHCRHKIFNADWIIDGKKQDKSLFQMIKSTHEANPENTVSAYKDNSSVIEGHKVGRLRPDPPTRPE
YRQHQEDLVHILMKVETHNHPTAIAPFPGASTGAGGEIRDEGATGRGAKPKAGLTGFCVSNLNIPGLEQP
WEDPFQKPERIASPLDIMIEAPLGAAAFNNEFGRPNLLGYFRTFELKASLPGGQVRGYHKPIMLAGGIGS
IDAEHIQKGEIEPGALLIVLGGPAMLIGLGGGAASSMVSGTNTADLDFASVQRGNPEMERRCQEVIDRCW
QLGEKNPIISIHDVGAGGLSNALPELIHDGGRGAVIDLRAVPLDDPGLSPLEIWCNESQERYVLLVRAEN
LEIFTAICERERCPFAVVGTATGDGRLTLVDDTPVRRNGQGDAPSHFPNNPVDLPLEVLLGKMPKMTRFV
QRKAPMLQPLDIPPGLDLHEALERVLRLPAVASKRFLITIGDRSVGGLVARDQMVGPWQTPLADVAVTAA
SFDTYTGEAMAIGERPPKALLDPKASARLAVGEAITNLAAALVGDLSDVKLSANWMAAAGHPGEDAALYD
AVKAVSELCPALGIAIPVGKDSLSMKTRWQDNGETKSVTAPGSLVISAFAPVPDVRKTVTPDLKHDKGDS
HLLLVDLGPGKNRLGGSALAQVFGQLGGDCPDLDDPERLKAFFAVMQGLVAEGLLLAYHDRSDGGLVTTL
LEMAFAGHCGLDVDLDALGDSLFAVLFNEELGAVIQVAKPDLAAVLELLRAAGLTALILGIGTPTGHPMI
RISVNGATLLSEKRSELRDIWEETSFQLQRLRDNPECAEEEFEGLRDRDGPGLKLPLTFDVNEDIAAPFI
NKGVKPKVAILREQGVNGDREMAAAFDRAGFEAWDVHMSDLLAGRVHLDEFRGLAACGGFSYGDVLGAGK
GWAKSILFNPRLRDQFQAFFKRPDTFSLGVCNGCQMLSNLLEWIPGTENWPHFVRNNSERFEARVASVRV
GESPSIMLRGMAGSRLPVAVAHGEGYAAFSSPELQAQADASGLAALRYIDDDGNPTEAYPLNPNGSPGGI
AGITSCDGRVTIMMPHPERVFRAWQNSWRPEDWDEDTPWLRLFRNARNWL
>gnl|CDD|273781 TIGR01736, FGAM_synth_II, phosphoribosylformylglycinamidine synthase II. Phosphoribosylformylglycinamidine synthase is a single, long polypeptide in most Proteobacteria and eukarotes. Three proteins are required in Bacillus subtilis and many other species. This is the longest of the three and is designated PurL, phosphoribosylformylglycinamidine synthase II, or FGAM synthase II [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
LSDEEMELIREILGREPNDTELAMFSAMWSEHCSYKSSKKLLKQFPTKGPNVIQGPGEDAGVVDIGDGYA
VVFKMESHNHPSAIEPYNGAATGVGGILRDILSMGARPIALLDSLRFGPLDDPKNRYLFEGVVAGISDYG
NRIGVPTVGGEVEFDESYNGNPLVNVMCVGLVRKDDIVTGKAKGPGNKLVLVGGKTGRDGIGGATFASEE
LSEEAEEEDRPAVQVGDPFTEKLLIEATLEAVDTGLVKGIKDLGAAGLTSASSEMAAKGGLGAEIYLDKV
PLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFEKYELPASVIGEVTDEGRIRLYYKGEVVADLPI
ELLADAPEYERPSEPPKYPEEEKEPEPPADLEDAFLKVLSSPNIASKEWVYRQYDHEVQTRTVVKPGEDA
AVLRIKETGKLGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLAAVGAEPLAAVDCLNFGNPERPEVYWQ
FVEAVKGLGDACRALGTPVVGGNVSLYNETNGVPIAPTPTIGMVGLVEDVEKLLTSNFKKEGDAIYLIGE
TKDELGGSEYLRVIHGIVSGQVPAVDLEEEKELADAVREAIRAGLVSAAHDVSRGGLAVALAEMAAASGI
GAEVDIDEIASARPDELLFSESNGRAIVAVPEEKAEEAVKSKGVPAKVIGKTGGDRLTIKTGDDTISVSV
KELRDAWEEALPEYM
>gnl|CDD|273782 TIGR01737, FGAM_synth_I, phosphoribosylformylglycinamidine synthase I. In some species, phosphoribosylformylglycinamidine synthase is composed of a single polypeptide chain. This model describes the PurQ protein of Bacillus subtilis (where PurL, PurQ, and PurS are required for phosphoribosylformylglycinamidine synthase activity) and functionally equivalent proteins from other bacteria and archaea [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
MKVAVIRFPGTNCDRDTVYALRLLGVDAEIVWYEDGSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQE
VREFAEKGVPVLGICNGFQILVEAGLLPGALLPNDSLRFICRWVYLRVENADTIFTKNYKKGEVIRIPIA
HGEGRYYADDETLARLESNDQVVFRYCDEDGDVAEEANPNGSVGNIAGIVNERGNVLGMMPHPERASEKL
LGGDDGLKLFESLVEWL
>gnl|CDD|273783 TIGR01738, Pimeloyl-_methyl_ester_esterase, pimelyl-[acyl-carrier protein] methyl ester esterase. This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
GQGNVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAPDPAIWL
GWSLGGLVALHIAATHPDRVRALVTVASSPCFSAREDWPEGIKPDVLTGFQQQLSDDYQRTIERFLALQT
LGTPTARQDARALKQTLLARPTPNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPML
DKLAPHSELYIFAKAAHAPFLSHAEAFCALLVAFK
>gnl|CDD|273784 TIGR01739, Probable_membrane_antigen_3, herpesvirus tegument protein/v-FGAM-synthase. This model describes a family of large proteins of herpesvirues. The protein is described variably as tegument protein or phosphoribosylformylglycinamidine synthase (FGAM-synthase). Most of the length of the protein shows homology to eukaryotic FGAM-synthase. Functional characterizations were not verified during construction of this model
RTLDFMYGPNLQGRPTTFSRELVDLLGTLGLTYPIRVEIGRHLTFILTHELKDIAKRHIELLYKFLCNKE
TLVTYLVIPQDERFENFEGSVGPPLVDPLPIPPDGLEQGIGYSSGGDRDLVAVAASVFAELDNVSIYPTA
VDTWTSWDSTNMMYDTRETIEVGTGFLHANANIQPPGNQLENLRFLSSWLPGVMPVASQLGLYYQTPALT
GEQDLPLSRKMSTAMLQAQASALRASGVPTCGGFIRLISKNKLSLPTPYTPTYNTSILDRLCHVTINTAD
EPPGQDIVALGQFEPSLLPDTPPLLYADSPLDVNKILTALALLTDDVKTPCIVGSIRPLGPCSVKEHLTA
LLPPCGAELDLSNLPDEVVAALARSSPANRVENEKMVKQYFLNVVCSVVFLTVKNTPHNTGTEGVTPLER
LKTACRMFGCPVKVLGKLVPLPGLHIVSDLFNPVPTYPTFDFTSFTPTSPLLPLGGPEPVSRTRPMFLDE
SLNWQTLNLRSTILKILSHPTVGSKEFIVRHIDRCGNGRVAQQQGVGPLDLPVSDYSLVLHNLSRPTDTT
EVTYSENAMDLILDPDSWLYSWENEVLENPALSCVCSALGEQTYKVQADPKRGATYAITEALLNLSLSPW
NTLEDVIITLSVTWSPTDHVYSLLKDALRACKDFCEELGVSFTVTSAASSPTQDSGSAPFMSIVFSASCP
VLLSAKKITPDLKSHGSHLIWLSLHPSYTLAGSIFEQILGLSFIRLPALSPVSLKKLLSALQTLVKEGVI
VSGHDVSDGGLVACVAEMALSGGKGVRITLPHGTDPLEFLCSETPGVVIEVDPSSMYAVLQFLRSEGLVF
QVIGRVGESGPSPTFSVVHNSTVLFQEPLSLLQGTWRSFSDEENTLLCPNLEPREMHVLDYGYNEMDFGG
VPKGLPLSPLRFFTCPDPRHQVAVLLLPGQSVPHGLLAALTNAGFDPRIVSITELKKTDFLDTFSGLIIG
GASGTLDSEVGARALAAALLRNQAFLRDLLTFLNRPDTFSLGFGELGCQLLLALNIVGYTQSSPFITVPT
EVQEPPRLEKNASGLYESRWLNFYIPETTKSVFLRPLRGSVLPCWAQGTHLGLYHPDDGVEEELENSGQI
ASTFHGNSPSSGLPATNYPRNPSGGSNVAGLCSADGRHLALLIDPSLSFFPWQWQHVPPNNPPLQVSPWK
LMFQRLHLWSLA
>gnl|CDD|273785 TIGR01740, Orotidine_5'-phosphate_decarboxylase, orotidine 5'-phosphate decarboxylase, subfamily 1. This model represents orotidine 5'-monophosphate decarboxylase, the PyrF protein of pyrimidine nucleotide biosynthesis. In many eukaryotes, the region hit by this model is part of a multifunctional protein [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKLNKLIFLDLKFADIPNTVKLQYE
SKIKLGADMVNVHGFAGSESVEAAKEAASEFGRRGLLAVTELTSMGSEEYGEDTMEKVVEYAKEAKEFGL
IGPVCSAEEAKEIRKATGDFLILTPGIRLDSKDADDQKRVVTLEEAKEAGADVIIVGRGIYAAEDPVEAA
KRIR
>gnl|CDD|130802 TIGR01741, staph_tand_hypo, conserved hypothetical protein. This model represents a tandem array of 10 proteins in Staphylococcus aureus and the C-terminal region of one protein each in Bacillus subtilis and Bacillus halodurans
MTFEEKLSDMYQEIANKINDMIPVEWEKVYLYAYVDDESGEVLFNYTTPESNQLIYYQDIPKHYNVSKDI
FKTSLRELRELFEELREEFRNENLEPWTSCEFDFTRSGELKVSFDYIDWIASEFDGYGRENYYMYKKFGI
LPEDEYEKEFVISYEGY
>gnl|CDD|273786 TIGR01742, SA_tandem_lipo, Staphylococcus tandem lipoproteins. Members of this family are predicted lipoproteins (mostly), found in Staphylococcus aureus in several different tandem clusters in pathogenicity islands. Members are also found, clustered, in Staphylococcus epidermidis
MGYAKKIALYISALILIISFVVGCGMFLKMDSKEEQIKKSFEKTLSMYPIKNLEDLYDKEGYRDGEFKKN
DKGTWYIYSSYVVQPKGELLKSDGMVLKLDRNTRTATGEYIVTTNDEKNATDSTYKSYPVKMVNNKIVLT
KDVKDPNLKKEIENFKFFIQYGNLKSLLNYNDGDVSYNPNVPSYSAKYKLSNDDPNVKQLKKRYNIPTNK
APKLLLKGSGDLKGSSVGYKKLEFYFSSPGKEQIIYKDSLTYNPI
>gnl|CDD|130804 TIGR01743, Pur_operon_repressor., pur operon repressor, Bacillus subtilis type. This model represents the puring operon repressor PurR of low-GC Gram-positive bacteria. This homodimeric repressor contains a large region homologous to phosphoribosyltransferases and is inhibited by 5-phosphoribosyl 1-pyrophosphate [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis, Regulatory functions, DNA interactions]
LRRSGRLVDLTNYLITNPNKLIPLNFFSERYESAKSSISEDIVIIKETFEKFGIGKLLTVPGAAGGVKYI
PKMSQAEAEEFVEELCQSLSEPERILPGGYLYLTDILGKPSILSKIGKILASVFAEREIDAVMTVATKGI
PLAYAVASVLNVPLVIVRKDSKVTEGSTVSINYVSGSSNRIQTMSLAKRSLKTGSKVLIIDDFMKAGGTI
NGMINLLDEFDAEVAGIGVLIDNEGVDEKLVDDYMSLLTLSNINEKEKSIEIENGNFL
>gnl|CDD|130805 TIGR01744, Xanthine_phosphoribosyltransferase, xanthine phosphoribosyltransferase. This model represent a xanthine-specific phosphoribosyltransferase of Bacillus subtilis and closely related proteins from other species, mostly from other Gram-positive bacteria. The adjacent gene is a xanthine transporter; B. subtilis can import xanthine for the purine salvage pathway or for catabolism to obtain nitrogen [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
MELLKQKIKEEGVVLPGGILKVDSFLNHQIDPKLMQEVGEEFARRFADDGITKIVTIEASGIAPAIMTGL
KLGVPVVFARKKKPLTLTDNLLTASVHSFTKQTTSTVAVSGEFLSDQDRVLIIDDFLANGQAAHGLVDIA
KQAGAKIAGIGIVIEKSFQNGRQELVELGYRVESLARIQSLEEGKVTFVQE
>gnl|CDD|130806 TIGR01745, Aspartate-semialdehyde_dehydrogenase, aspartate-semialdehyde dehydrogenase, gamma-proteobacterial [Amino acid biosynthesis, Aspartate family]
KNVGLVGWRGMVGSVLMQRMQEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDIDALKALDIIIT
CQGGDYTNEIYPKLRESGWQGYWIDAASSLRMKDDAVIILDPVNQDVITDGLNNGIRTFVGGNCTVSLML
MSLGGLFANDLVEWVSVATYQAASGGGARHMRELLTQMGHLYGHVEDELATPSSAILDIERKVTKLTRSG
ELPVDNFGVPLAGSLIPWIDKQLDNGQSREEWKGQAETNKILGTSSTIPVDGLCVRIGALRCHSQAFTIK
LKKDVSLETIEEIIRAHNPWVKVVPNDREITMRELTPAAVTGTLTIPVGRLRKLNMGPEYLSAFTVGDQL
LWGAAEPLRRMLRILA
>gnl|CDD|273787 TIGR01746, L-aminoadipate-semialdehyde_dehydrogenase, thioester reductase domain. This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold
TVLLTGATGFLGAYLLEELLRRSTRAKVICLVRADSEEHAMERLREALRSYRLWHENLAMERIEVVAGDL
SKPRLGLSDAEWERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVG
AAIDLSTGVTEDDATVTPYPGLAGGYTQSKWVAELLVREASDRGLPVTIVRPGRILGDSYTGAWNSSDIL
WRMVKGCLALGAYPQSPELTEDLTPVDFVARAIVALSSRPAASAGGIVFHVVNPNPVPLDEFLEWLERAG
YNLRLVSFDEWLQRLEDSDTAKRDSRRYPLLPLLHFTGDAFESDETDTRNLDSRSTAEALEGDGIREPSI
TAPLLHLYLQYLKEIGF
>gnl|CDD|130808 TIGR01747, Diaminopropionate_ammonia-lyase, diaminopropionate ammonia-lyase family. This small subfamily includes diaminopropionate ammonia-lyase from Salmonella typhimurium and a small number of close homologs, about 50 % identical in sequence. The enzyme is a pyridoxal phosphate-binding homodimer homologous to threonine dehydratase (threonine deaminase) [Energy metabolism, Other]
LFSQSQAKLALAFHKKIPGYRPTPLCALDHLANLLGLKKILVKDESKRFGLNAFKMLGGSYAIAQYLAEK
LHLDIETLSFEHLKNDAIGEKMGQATFATATDGNHGRGVAWAAQQLGQKAVVYMPKGSAQERVENILNLG
AECTITDMNYDDTVRLAMQMAQQHGWVVVQDTAWEGYEKIPTWIMQGYATLADEAVEQLREMGSVTPTHV
LLQAGVGSMAGGVLGYFVDVYSENNPHSIVVEPDKADCLYQSAVKKDGDIVNVGGDMATIMAGLACGEPN
PISWEILRNCTSQFISAQDSVAAKGMRVLGAPYGGDPRIISGESGAVGLGLLAAVMYHPQYQSLMEKLQL
DKDAVVLVISTEGDTDPDHYREIVWE
>gnl|CDD|130809 TIGR01748, L-rhamnose_isomerase, L-rhamnose isomerase. This enzyme interconverts L-rhamnose and L-rhamnulose. In some species, including E. coli, this is the first step in rhamnose catabolism. Sequential steps are catalyzed by rhamnulose kinase (rhaB), then rhamnulose-1-phosphate aldolase (rhaD) to yield glycerone phosphate and (S)-lactaldehyde. Characterization of this family is based on members in E. coli and Salmonella [Energy metabolism, Sugars]
IEQAYELAKQRYAAVGIDVEEALRQLDRLPISMHCWQGDDVSGFENPEGELTGGIQATGNYPGKARTPSE
LRADLEKAMSLIPGKHRLNLHAIYLETDEPVSRDEIKPEHFKNWVEWAKANGLGLDFNPTCFSHPLSADG
FTLSHPDDSIRQFWIDHCKASRRISEYFGKELGTPSVMNIWIPDGMKDIPVDRLTPRKRLLEALDEVFSE
KLNEAHHIDAVESKLFGLGAESYTVGSHEFYMGYATTRQKLLCLDAGHFHPTEVISNKISSAMLYVPQLL
LHVSRPVRWDSDHVVLLDDELQEIASEIVRNDLLDRVHIGLDFFDASINRIAAWVIGTRNMKKALLRALL
EPTAELKKLEAEGDYTARLALLEEQKSLPFGAVWEMYCERHGVPVGSEWLESVKAYEKEVLLKR
>gnl|CDD|130810 TIGR01749, 3-hydroxydecanoyl-_dehydratase, beta-hydroxyacyl-[acyl carrier protein] dehydratase FabA. This enzyme, FabA, shows overlapping substrate specificity with FabZ with regard to chain length in fatty acid biosynthesis. It is commonly designated 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.60) as if it were specific for that chain length, but its specificity is broader; it is active even in the initiation of fatty acid biosynthesis. This enzyme can also isomerize trans-2-decenoyl-ACP to cis-3-decenoyl-ACP to bypass reduction by FabI and instead allow biosynthesis of unsaturated fatty acids. FabA cannot elongate unsaturated fatty acids [Fatty acid and phospholipid metabolism, Biosynthesis]
KQNAYTREDLLACGRGELFGPGNAQLPAPPMLMIDRIVEISETGGKFGKGYVEAELDIRPDLWFFGCHFI
GDPVMPGCLGLDAMWQLVGFFLGWLGGPGRGRALGVGEVKFTGQVLPTAKKVTYRIHFKRVINRRLVMGI
ADGEVLVDGRLIYTASDLRVGLFTSTSAF
>gnl|CDD|130811 TIGR01750, 3-hydroxyacyl-_dehydratase_FabZ, beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ. This enzyme, FabZ, shows overlapping substrate specificity with FabA with regard to chain length in fatty acid biosynthesis. FabZ works preferentially on shorter chains and is often designated (3R)-hydroxymyristoyl-[acyl carrier protein] dehydratase, although its actual specificity is broader. Unlike FabA, FabZ does not function as an isomerase and cannot initiate unsaturated fatty acid biosynthesis. However, only FabZ can act during the elongation of unsaturated fatty acid chains [Fatty acid and phospholipid metabolism, Biosynthesis]
DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLA
ILSLGGEKGKGKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI
>gnl|CDD|188164 TIGR01751, crotonyl_CoA_reductase, crotonyl-CoA carboxylase/reductase. The enzyme represented by this model can convert crotonyl-CoA to butyryl-CoA (crotonyl-CoA reductase activity), but more importantly, in the presence of CO2, generates (2S)-ethylmalonyl-CoA. In serine cycle methylotrophic bacteria this enzyme is involved in the process of acetyl-CoA to glyoxylate. In other bacteria the enzyme is used to produce extender units for incorporation into polyketides such as tylosin from Streptomyces fradiae and coronatine from Pseudomonas syringae
ITVVPETMYAFAIREERDGDPRQAIQLEVVPVPELGPGEVLVAVMAAGVNYNNVWAALGEPVSTFAFLRK
YGKLDLPFHIIGSDASGVVWRVGPGVTRWKVGDEVVASCLQVDLTAPDGRDGDPMLSSEQRIWGYETNFG
SFAEFALVKDYQLMPKPKHLTWEEAACPGLTGATAYRQLVGWNPAAVKPGDNVLIWGAAGGLGSYATQLA
RAGGGNPVAVVSSPEKAEYCRSLGAEAVIDRNDFGHWGRLPDHNTQAPKEWTKSFKRFGKRIRELTGGED
PDIVFEHPGRATFPTSVYVCRRGGMVVICGGTTGYNHDYDNRYLWMRQKRIQGSHFANLREAYEANRLVA
KGRIDPTLSKTYPLEEIGQAHQDVHRNHHQGNVAVLVLAPRPGLGVFD
>gnl|CDD|273788 TIGR01752, Flavodoxin_1., flavodoxin, long chain. Flavodoxins are small redox-active proteins with a flavin mononucleotide (FMN) prosthetic group. They can act in nitrogen fixation by nitrogenase, in sulfite reduction, and light-dependent NADP+ reduction in during photosynthesis, among other roles. This model describes the long chain type, typical for nitrogen fixation but associated with pyruvate formate-lyase activation and cobalamin-dependent methionine synthase activity in E. coli [Energy metabolism, Electron transport]
KIGIFYGTDTGNTEGIAEKIQKELGEDDVDVFNIAKASKEDLNAYDKLILGTPTWGVGELQEDWEDFLPT
LEELDFTGKTVALFGLGDQEGYSETFCDGMGILYDKIKARGAKVVGFWPTDGYHFEASKAVRDGDKFVGL
ALDEDNQPDLTEERIEKWVEQIKPEFA
>gnl|CDD|273789 TIGR01753, Probable_flavodoxin-1, flavodoxin, short chain. Flavodoxins are small redox-active proteins with a flavin mononucleotide (FMN) prosthetic group. They can act in nitrogen fixation by nitrogenase, in sulfite reduction, and light-dependent NADP+ reduction in during photosynthesis, among other roles. This model describes the short chain type. Many of these are involved in sulfite reduction [Energy metabolism, Electron transport]
ILIVYASMTGNTEEMANIIAEGLKEAGAEVDLLEVADADAEDLLSYDAVLLGCSTWGDEDLEQDDFEPFF
EELEDIDLGGKKVALFGSGDWGYEFCEAVDDWEERLKEAGATIIAEGLKVDGDPEEEDLDKCREFAKDLA
>gnl|CDD|130815 TIGR01754, flav_RNR, ribonucleotide reductase-associated flavodoxin, putative. This model represents a family of proteins found immediately downstream of ribonucleotide reductase genes in Xyella fastidiosa and some Gram-positive bacteria. It appears to be a highly divergent flavodoxin of the short chain type, more like the flavodoxins of the sulfate-reducing genus Desulfovibrio than like the NifF flavodoxins associated with nitrogen fixation
MRILLAYLSLSGNTEEVAFMIQDYLQKDGHEVDILHRIGTLADAPLDPENYDLVFLGTWTWERGRTPDEM
KDFIAELGYKPSNVAIFGTGETQWGDDLYCGAVDRLAHFFGSSHPVLKIEQMPHGEQDGRAIYDWLEGVL
>gnl|CDD|130816 TIGR01755, NADPH_dehydrogenase_quinone, NAD(P)H:quinone oxidoreductase, type IV. This model represents a protein, WrbA, related to and slightly larger than flavodoxin. It was just shown, in E. coli and Archaeoglobus fulgidus (and previously for some eukaryotic homologs) to act as fourth type of NAD(P)H:quinone oxidoreductase. In E. coli, this protein was earlier reported to be produced during stationary phase, bind to the trp repressor, and make trp operon repression more efficient. WrbA does not interact with the trp operator by itself. Members are found in species in which homologs of the E. coli trp operon repressor TrpR (SP:P03032) are not detected [Energy metabolism, Electron transport]
VKVLVLYYSMYGHIETMARAVAEGAREVDGAEVVVKRVPETVPEEVAEKSHGKTDQTAPVATPQELADYD
AIIFGTPTRFGNMASQMRNFLDQTGGLWASGALVGKVGSVFTSTGTQHGGQESTILSTWTTLLHHGMIIV
PLPYAAQEQMGVDEVRGGSPYGATTIAGGDGSRQPSAEELDIARYQGRHVAGLAAKL
>gnl|CDD|130817 TIGR01756, putative_lactate_dehydrogenase_partial, lactate dehydrogenase. This model represents a family of protist lactate dehydrogenases which have aparrently evolved from a recent protist malate dehydrogenase ancestor. Lactate dehydrogenase converts the hydroxyl at C-2 of lactate to a carbonyl in the product, pyruvate. The preference of this enzyme for NAD or NADP has not been determined. A critical residue in malate dehydrogenase, arginine-91 (T. vaginalis numbering) has been mutated to a leucine, eliminating the positive charge which complemeted the carboxylate in malate which is absent in lactate. Several other more subtle changes are proposed to make the active site smaller to accomadate the less bulky lactate molecule
LSHWIANGDLYGNRPVCLHLLEIPPALNRLEALAMELEDCAFPNLAGTIVTTKLEEAFKDIDCAFLVASV
PLKPGEVRADLLTKNTPIFKATGEALSEYAKPTVKVLVIGNPVNTNCLVAMLHAPKLSAENFSSLCMLDH
NRAVSRIASKLKVPVDHIYHVVVWGNHAESMVADLTHAEFTKNGKHQKVFDELCRDYPEPDFFEVIAQRA
WKILEMRGFTSAASPVKASLQHMKAWLFGTRPGEVLSMGIPVPEGNPYGIKPGVIFSFPCTVDEDGKVHV
VENFELNPWLKTKLAQTEKDLFEERETALKALA
>gnl|CDD|130818 TIGR01757, Malate_dehydrogenase_1_chloroplastic, malate dehydrogenase, NADP-dependent. This model represents the NADP-dependent malate dehydrogenase found in plants, mosses and green algae and localized to the chloroplast. Malate dehydrogenase converts oxaloacetate into malate, a critical step in the C4 cycle which allows circumvention of the effects of photorespiration. Malate is subsequenctly transported from the chloroplast to the cytoplasm (and then to the bundle sheath cells in C4 plants). The plant and moss enzymes are light regulated via cysteine disulfide bonds. The enzyme from Sorghum has been crystallized
AAKQVQAGVATAEAAATKKCYGVFCLSYDLKNEDKSLTKSWKKTVNVAVSGAAGMISNHLLFMLASGEVF
GQDQPIALKLLGSERSKEALEGVAMELEDSLYPLLREVSIGIDPYEVFEDADWALLIGAKPRGPGMERAD
LLDINGQIFADQGKALNAVASKNCKVLVVGNPCNTNALIAMKNAPNIPRKNFHALTRLDENRAKCQLALK
SGKFYTSVSNVTIWGNHSTTQVPDFVNAKIGGRPAKEVIKDTKWLEEEFTPTVQKRGGALIKKWGRSSAA
STAVSIADAIKSLVVPTPEGDWFSTGVYTDGNPYGIAEGLVFSMPCRSKGDGDYELATDVSMDDFLRERI
RKSEDELLKEKECVAHLIGEGNAYCAVPEDTMLPGEN
>gnl|CDD|130819 TIGR01758, Malate_dehydrogenase_cytoplasmic, malate dehydrogenase, NAD-dependent. This model represents the NAD-dependent cytosolic malate dehydrogenase from eukaryotes. The enzyme from pig has been studied by X-ray crystallography
RVVVTGAAGQIGYALLPMIARGRMLGKDQPIILHLLDIPPAMKVLEGVVMELMDCAFPLLDGVVPTHDPA
VAFTDVDVAILVGAFPRKEGMERRDLLSKNVKIFKEQGRALDKLAKKDCKVLVVGNPANTNALVLSNYAP
SIPPKNFSALTRLDHNRALAQVAERAGVPVSDVKNVIIWGNHSSTQYPDVNHATVTKGGKQKPVREAIKD
DAYLDGEFITTVQQRGAAIIRARKLSSALSAAKAAVDQMHDWVLGTPEGTFVSMGVYSDGSPYGVPKGLI
FSFPVTCKNGEWKIVEGLCVDDSSRKKLALTAKELEEERDEALS
>gnl|CDD|130820 TIGR01759, Malate_dehydrogenase, malate dehydrogenase. This model represents a family of malate dehydrogenases in bacteria and eukaryotes which utilize either NAD or NADP depending on the species and context. MDH interconverts malate and oxaloacetate and is a part of the citric acid cycle as well as the C4 cycle in certain photosynthetic organisms
KKPVRVAVTGAAGQIGYSLLFRIASGELFGKDQPVVLHLLDIPPAMKALEGVAMELEDCAFPLLAGVVAT
TDPEEAFKDVDAALLVGAFPRKPGMERADLLSKNGKIFKEQGKALNKVAKKDVKVLVVGNPANTNALIAS
KNAPDIPPKNFSAMTRLDHNRAKYQLAAKAGVPVSDVKNVIIWGNHSNTQVPDFTHATVDGRPVKEVIKD
DKWLEGEFIPTVQQRGAAVIEARGASSAASAANAAIDHVRDWVTGTPEGDWVSMGVYSDGNPYGIPEGII
FSFPVTCKGDGEWEIVEGLPLDDFVRGKLDATEDELLEEKEEA
>gnl|CDD|273790 TIGR01760, COG5283:_Phage-related_tail_protein, phage tail tape measure protein, TP901 family, core region. This model represents a reasonably well conserved core region of a family of phage tail proteins. The member from phage TP901-1 was characterized as a tail length tape measure protein in that a shortened form of the protein leads to phage with proportionately shorter tails [Mobile and extrachromosomal element functions, Prophage functions]
SAALGGGLVAAVKAAIEFEDAMSGVRAVVDGSRTKEFEDLSNQARDLGDETPFSAAQIAGAMTALARAGI
SAKDLLGATPTALKLAAASDLTAEEAASILAKIMNAFGLTAKDSEKVADVLNYTANNSAATTRDMGDALQ
YAGPVAKSLGVSLEETAAATAALASAGIEGEIAGTALKAMLSRLAAPTGKAAKALKKLGIQTRDAKGNMK
GLLDVLKELQKLTKGMGTEQQAAKLKTIFGVEASSALATLLTAGSKLSLAKNAKSLANSNGSAKKEADKM
LDTLKGQLKLLQNAVENAFIELGEALLPALRELAQALTKLINAINGLAKGNPQLAVTLAAVAAAILALTA
>gnl|CDD|273791 TIGR01761, thiazolinyl-S-HMWP1_reductase, thiazolinyl imide reductase. This reductase is found associated with gene clusters for the biosynthesis of various non-ribosomal peptide derived natural products in which cysteine is cyclized to a thiazoline ring containing an imide double bond. Examples include yersiniabactin (irp3/YbtU, GP|21959262) and pyochelin (PchG, GP|4325022)
SPKQSVLVCGTRFGEMYLAAFMQAPEGLELAGLLAQGSERSRALAHALGVPLYTSPEELPDDIDIACVVV
RSTIVGGQGSQLARALLARGIHVLQEHPLHPDDISSLLRLAQRQGCRYWVNTFYPHLPAGRRFIRYARQL
CLRKTPPFVEATTSVQLLYSTLDILLRLLGGVGPAALECPGGDFSPFPCRRLQGVIAEVPLSLNLQNYLD
PADPDMHSLIMHRLLLGWPEGHLSLVASYGPVIWSPSLFVPDHQDENAHALYRRPAILRDPPGLTRLWYA
EPLSWRSVCETVWPEAVSWALAEFLAAEGPPVAAQNQHQLALSQLWQQIMRKTGNPEEVRRLTP
>gnl|CDD|130823 TIGR01762, syringomycin_biosynthesis_enzyme_2, chlorinating enzyme. This model represents a a group of highly homologous enzymes related to dioxygenases which chlorinate amino acid methyl groups. BarB1 and BarB2 are proposed to trichlorinate one of the methyl groups of a leucine residue in the biosynthesis of barbamide in the cyanobacterium Lyngbya majuscula. SyrB2 is proposed to chlorinate the methyl group of threonine in the biosynthesis of syringomycin in Pseudomonas syringae. CmaB is proposed to chlorinate the beta-methyl group of alloisoleucine in the process of ring closure in the biosynthesis of coronamic acid, a component of coronatine also in Pseudomonas syringae
FALTAEERQSFEKNGFIGPFTLYSPEEMKETWKRIRLRLLDRSAAPYQDLGGTNIANYDRHLDDDFLASH
ICRPEICHRVESILGPNVLCWRTEFFPKYPGDEGTDWHQADTFANASGKPQLVWPENEEFGGTITVWTAF
TDATIENGCMQFIPGTHNSMNYDETRRMTFEPDANNSVVKGGVRRGFFGYDYRQLQIDENWKPDEASAVP
MQMKAGQFIIFWSTLMHASYPNSGESQMRMGFASRYVPSFVHVYPDSDHIEEFGGRISLERYGAVQVIGD
ETPEYNRL
>gnl|CDD|273792 TIGR01763, Malate_dehydrogenase, malate dehydrogenase, NAD-dependent. This enzyme converts malate into oxaloacetate in the citric acid cycle. The critical residues which discriminate malate dehydrogenase from lactate dehydrogenase have been characterized, and have been used to set the cutoffs for this model. Sequences showing [aflimv][ap]R[rk]pgM[st] and [ltv][ilm]gGhgd were kept above trusted, while those in which the capitalized residues in the patterns were found to be Q, E and E were kept below the noise cutoff. Some sequences in the grey zone have been annotated as malate dehydrogenases, but none have been characterized. Phylogenetically, a clade of sequences from eukaryotes such as Toxoplasma and Plasmodium which include a characterized lactate dehydrogenase and show abiguous critical residue patterns appears to be more closely related to these bacterial sequences than other eukaryotic sequences. These are relatively long branch and have been excluded from the model. All other sequences falling below trusted appear to be phylogenetically outside of the clade including the trusted hits. The annotation of Botryococcus braunii as lactate dehydrogenase appears top be in error. This was initially annotated as MDH by Swiss-Prot and then changed. The rationale for either of these annotations is not traceable [Energy metabolism, TCA cycle]
RKKISVIGAGFVGATTAFRLAEKELADLVLLDVVEGIPQGKALDMYEASPVGGFDTKVTGTNNYADTANS
DIVVITAGLPRKPGMSREDLLSMNAGIVREVTGRIMEHSPNPIIVVVSNPLDAMTYVAWQKSGFPKERVI
GQAGVLDSARFRTFIAMELGVSVQDVTACVLGGHGDAMVPLVRYSTVAGIPVADLISAERIAEIVERTRK
GGGEIVNLLKQGSAYYAPAASVVEMVEAILKDRKRVLPCAAYLDGQYGIDGIYVGVPVILGKNGVEHIYE
LKLDQSELALLNKSAKIVDENCKML
>gnl|CDD|200128 TIGR01764, Probable_excisionase, DNA binding domain, excisionase family. An excisionase, or Xis protein, is a small protein that binds and promotes excisive recombination; it is not enzymatically active. This model represents a number of putative excisionases and related proteins from temperate phage, plasmids, and transposons, as well as DNA binding domains of other proteins, such as a DNA modification methylase. This model identifies mostly small proteins and N-terminal regions of large proteins, but some proteins appear to have two copies. This domain appears similar, in both sequence and predicted secondary structure (PSIPRED) to the MerR family of transcriptional regulators (pfam00376) [Unknown function, General]
YLTVEEAAEYLGVSKSTVYRLIEEGELPAYRVGRHYRIPREDVDEYLEQ
>gnl|CDD|130826 TIGR01765, COG0675:_Transposase_and_inactivated_derivatives, transposase, putative, N-terminal domain. This model represents the N-terminal region of a family of putative transposases found in the largest copy number in Thermoanaerobacter tengcongensis. The three homologs in Bacillus anthracis are each split into two ORFs and this model represents the upstream ORF [Mobile and extrachromosomal element functions, Transposon functions]
TIKAKLNFEDKEKEYLLDLIRAFSSAVNFVIKRLLEGKSHSELKKELQRLYYLNYREDAPLQAQSLIQGA
REL
>gnl|CDD|273793 TIGR01766, Putative_transposase_MJ0751, transposase, IS605 OrfB family, central region. This model represents a region of a sequence similarity between a family of putative transposases of Thermoanaerobacter tengcongensis, smaller related proteins from Bacillus anthracis, putative transposes described by pfam01385, and other proteins [Mobile and extrachromosomal element functions, Transposon functions]
ERNKVEDFLHKIVKQIVEYAKENNGTIVLEDLKNIREMVDKKSKYLRRKLHQWSFRKLISKIKYKAEEYG
IEVIEVNPAYTS
>gnl|CDD|130828 TIGR01767, 5-methylthioribose_kinase, S-methyl-5-thioribose kinase. This enzyme, S-methyl-5-thioribose kinase (MtnK) is involved in the methionine salvage pathway in certain bacteria
QEVGDGNLNLVFHVYDQEGDRAAIVKQALPYVRVVGESWPLTLDRARIESSALIRQGEHVPHLVPRIFHF
DTEMAVTVMEDLSHHKIARKGLIEGENYPHLARHIGEFLAKTLFYSSDYALEPKVKKALVAQFTNPELCD
ITERLVFTDPYFDHDTNDFEEELRPFVAKLRNDDSLKIEAAKLKHSFLASAETLLHGDLHSGSIFVSEHE
TKVIDPEFAFYGPIGFDIGQFIANLFLNALSRDGADQKGKRDAMREPLLEHVNQVWETFEETFSELWQKD
SLDMVYANIDGYLTDTLSHIWEDAIGFAGCELIRRTIGLAHVADLDTIVDFAKRIGCKRLALETGRAFIV
KRSEIKSIDEVIELFALLVQ
>gnl|CDD|273794 TIGR01768, Geranylgeranylglyceryl_phosphate_synthase, geranylgeranylglyceryl phosphate synthase family protein. This model represents a family of sequences including geranylgeranylglyceryl phosphate synthase which catalyzes the first committed step in the synthesis of ether-linked membrane lipids in archaea. The clade of bacterial sequences may have the same function or a closely related function. This model supercedes TIGR00265, which has been retired
RHFTLIDPDKTNPEEADEIAKAAAESGTDAILIGGSQGVTYEKLDTLIEALRRYGVPIILFPSNPTNVSR
DADALFFPSVLNSDDPYWIIGAQIEGAPKFKKIGEEIIPEGYIIVNPGGAAARVTKAKPIPYDKEDLAAY
AAMAEEMLGMPIFYLEAGSGAPEPVPPELVAEVKKVLDKARLFVGGGIRSVEKAREMAEAGADTVVTGNV
IEESVDKALETVE
>gnl|CDD|130830 TIGR01769, Geranylgeranylglyceryl_phosphate_synthase, phosphoglycerol geranylgeranyltransferase. This model represents geranylgeranylglyceryl phosphate synthase which catalyzes the first committed step in the synthesis of ether-linked membrane lipids in archaea. The active enzyme is reported to be a homopentamer in Methanobacterium thermoautotrophicum but is reported to be a homodimer in Thermoplasma acidophilum
HFTLIDPEKSDEIEKIAKNAKDAGTDAIMVGGSLGIVESNLDQTVKKIKKITNLPVILFPGNVNGLSRYA
DAVFFMSLLNSADTYFIVGAQILGAITILKLNLEVIPMAYLIVGPGGAVGYVGKAREIPYNKPEIAAAYC
LAAKYFGMKWVYLEAGSGASYPVNPETISLVKKASGIPLIVGGGIRSPEIAYEIVLAGADAIVTG
>gnl|CDD|273795 TIGR01770, NADH-quinone_oxidoreductase_subunit_N, proton-translocating NADH-quinone oxidoreductase, chain N. This model describes the 14th (based on E. coli) structural gene, N, of bacterial and chloroplast energy-transducing NADH (or NADPH) dehydrogenases. This model does not describe any subunit of the mitochondrial complex I (for which the subunit composition is very different), nor NADH dehydrogenases that are not coupled to ion transport. The Enzyme Commission designation 1.6.5.3, for NADH dehydrogenase (ubiquinone), is applied broadly, perhaps unfortunately, even if the quinone is menaquinone (Thermus, Mycobacterium) or plastoquinone (chloroplast). For chloroplast members, the name NADH-plastoquinone oxidoreductase is used for the complex and this protein is designated as subunit 2 or B. This model also includes a subunit of a related complex in the archaeal methanogen, Methanosarcina mazei, in which F420H2 replaces NADH and 2-hydroxyphenazine replaces the quinone [Energy metabolism, Electron transport]
LIAILPEIILLLGAFILLLYGLFYSRKKRNPLLLKNLSYIVLLSALVSLFLTLQYAAYLFTGFSFFIVDN
FALLIKLILLLSTLLTFFFALSYLSKEKINKFEFYILLLFALLGIFLLVSSNDLLSIYLGLELQSLCFYV
LAGLKRKSRFSTEAGLKYFILGAFSSGLLLFGISLIYGFTGSLNFEDLLLFLSNGMLNISLLLLGIVLIL
VGLLFKLSAVPFHMWVPDVYEGAPTPVTAFFSIVPKIAIFAVFLRLFLYILFGFSEAWQIFLAIIAFLSM
LIGNFGALAQKKVKRLLAYSSISHVGYILIGLLAGTLEGIKAVLFYIFIYALMSLGAFGVLSLLRSYKDE
WIEYISDFAGLFKTNPILAILILIFMFSLAGIPPLAGFFGKFYVFFALLKSGLYWLAVIAVLTSVIGAFY
YLRVVKVMYFDKPERRIPSNPQSKAQSLLLSISALFILFLGLFPSLIL
>gnl|CDD|273796 TIGR01771, L-lactate_dehydrogenase, L-lactate dehydrogenase. This model represents the NAD-dependent L-lactate dehydrogenases from bacteria and eukaryotes. This enzyme function as as the final step in anaerobic glycolysis. Although lactate dehydrogenases have in some cases been mistaken for malate dehydrogenases due to the similarity of these two substrates and the apparent ease with which evolution can toggle these activities, critical residues have been identified which can discriminate between the two activities. At the time of the creation of this model no hits above the trusted cutoff contained critical residues typical of malate dehydrogenases [Energy metabolism, Anaerobic, Energy metabolism, Glycolysis/gluconeogenesis]
IIGAGNVGSSTAFALLNQGIADEIVLIDINKDKAEGEAMDLQHAASFLPTPKKIRSGDYSDCKDADLVVI
TAGAPQKPGETRLELVGRNVRIMKSIVPEVVKSGFDGIFLVATNPVDILTYVAWKLSGFPKNRVIGSGTV
LDTARLRYLLAEKLGVDPQSVHAYIIGEHGDSEVPVWSSATIGGVPLLDYLKAKGTETDLDLEEIEKEVR
DAAYEIINRKGATYYGIGMAVARIVEAILHDENRVLPVSAYLDGEYGIKDVYIGVPAVLGRNGVEEIIEL
PLSDEEKEAFQKSAETLKK
>gnl|CDD|130833 TIGR01772, Malate_dehydrogenase_mitochondrial, malate dehydrogenase, NAD-dependent. This model represents the NAD-dependent malate dehydrogenase found in eukaryotes and certain gamma proteobacteria. The enzyme is involved in the citric acid cycle as well as the glyoxalate cycle. Several isoforms exidt in eukaryotes. In S. cereviseae, for example, there are cytoplasmic, mitochondrial and peroxisomal forms. Although malate dehydrogenases have in some cases been mistaken for lactate dehydrogenases due to the similarity of these two substrates and the apparent ease with which evolution can toggle these activities, critical residues have been identified which can discriminate between the two activities. At the time of the creation of this model no hits above the trusted cutoff contained critical residues typical of lactate dehydrogenases [Energy metabolism, TCA cycle]
KVAVLGAAGGIGQPLSLLLKLQPYVSELSLYDIAGAAGVAADLSHIPTAASVKGFSGEEGLENALKGADV
VVIPAGVPRKPGMTRDDLFNVNAGIVKDLVAAVAESCPKAMILVITNPVNSTVPIAAEVLKKKGVYDPNK
LFGVTTLDIVRANTFVAELKGKDPMEVNVPVIGGHSGETIIPLISQCPGKVLFTEDQLEALIHRIQNAGT
EVVKAKAGAGSATLSMAFAGARFVLSLVRGLKGEEGVVECAYVESDGVTEATFFATPLLLGKNGVEKRLG
IGKLSSFEEKMLNGALPELKKNIKKGEEFVAS
>gnl|CDD|273797 TIGR01773, GABA_permease, gamma-aminobutyrate permease. GABA permease (gabP) catalyzes the translocation of 4-aminobutyrate (GABA) across the plasma membrane, with homologues expressed in Gram-negative and Gram-positive organisms. This permease is a highly hydrophobic transmembrane protein consisting of 12 transmembrane domains with hydrophilic N- and C-terminal ends. Induced by nitrogen-limited culture conditions in both Escherichia coli and Bacillus subtilis, gabP is an energy dependent transport system stimulated by membrane potential and has been observed adjacent and distant from other GABA degradation proteins. GabP is highly homologous to amino acid permeases from B. subtilis, E. coli, as well as to other members of the amino acid permease family (pfam00324). A member of the APC (amine-polyamine-choline) transporter superfamily, GABA permease possesses a "consensus amphiphatic region" (CAR) found to be evolutionarily conserved within this transport family. This amphiphatic region is located between helix 8 and cytoplasmic loop 8-9, forming a potential channel domain and suggested to play a significant role in ligand recognition and translocation. Unique to GABA permeases, a conserved cysteine residue (CYS-300, E.coli) located at the beginning of the amphiphatic domain, has been determined to be critical for catalytic specificity [Transport and binding proteins, Amino acids, peptides and amines]
MNQSQSGLKLPNGLKTRHVTMLSIAGVIGAGLFVGSGSAIASAGPAALLAYLLAGLLVVFIMRMLGEMAV
ANPDTGSFSTYADDAIGRWAGFTIGWLYWWFWVLVIPLEAIAAAGILQYWFPDIPLWLFSLILTIVLTLT
NLYSVKSYGEFEFWFALIKVIAIIAFIILGAVAIFGFAPGSEVSGFSNLTGKGGFFPNGIGAVLLAILVT
MFSFMGTEIVTIAAAESSNPIKSITRATNSVIWRIIVFYLGSIFIVVALLPWNSPNLLEVGSYVAVLELL
GIPHAKLIMDFVVLTAVLSCLNSALYTTSRMLYSLAERGDAPRVFMKLNKKGVPVQAVLASTFFSFLTVV
VNYFAPDKVFLFLVNSSGAIALLVYLVIAVSQLRMRKKLKANGEAIKIRMWLYPWLTWLVIIFICGILVS
MLFIPSMRDEVLLTGLLTIIVLCSYLVFARRK
>gnl|CDD|273798 TIGR01774, Putative_formate_acetyltransferase_3, glycyl radical enzyme, PFL2/glycerol dehydratase family. This family previously was designated pyruvate formate-lyase, but it now appears that members include the B12-independent glycerol dehydratase. Therefore, the functional definition of the family is being broadened. This family includes the PflF and PflD proteins of E. coli, described as isoforms of pyruvate-formate lyase found in a limited number additional species. PFL catalyzes the reaction pyruvate + CoA -_ acetyl-CoA + formate, which is a step in the fermentation of glucose
MCMDRIEKLKKALSKPVARLSVERARLYTESMKQTEGEPMIIRRAKALAHVLENIPIQILDSELIVGNML
PNPRAAIIFPEGVGLWIIKELDSLPNRPTNRFAVSEEDKRVLREEIAPYWQRKTIEDFAFGLMTDEMKIL
YTTSIFVLTGEIAGISHVAVNYPYLLRRGLRWLLEESERRIRALEESGVYEGEKYSFYQAAKIVLEAVIN
HILRYAKLAEEMAASETGESRREELLKIAEICRKVAAEKPQTFWQAVQLVWLVQSILQQESNEQSISMGR
IDQYLYPFYKKDIGEGRIDRELAFEILASLWIKTNEIVPARSSSLEQYFAGQPTNQAVTIGGCDIYGNDA
VNELSYLMLEVTDRLRLRQPNLHVRINAGSPESFLKRLAEAIRSGCGNPALFNDEAVVPAFKNAGVDDRD
ALDYTTDGCVEIAPFGNSYTSSDAALINVAKVMEYALNEGVDLQFGYEFGAKTEKPKFLEDLLEKLREQI
SHYVKLVVEGSNVLDYANAEVKPTPLLSLCVEDCFEKGVDISRGGARYNFTGIQAVGIANLGDSLVAIKG
AVFEQGAYSMDDLVEALRKNFVGLTHEEKRHRLINQSPKYGNDDDAVDKYTAMVLEWYCEEVNRYRNPRG
GKFAAGCYPMSANVPFGFFTSATPDGRKAGEPLAPGVSPSTGMDREGPTAVINSVSKLSYENLPNGALLN
IKLSPATLEEEGDKQKLIEALRKSFMELKVMHIQFNIVKEDTLRKAQQEPEKYRWLVVRVAGYSAFFVEL
SRPVQDDIIRRTSHRL
>gnl|CDD|273799 TIGR01776, Lactoferrin-binding_protein_A, TonB-dependent lactoferrin and transferrin receptors. This family of TonB-dependent receptors are responsible for import of iron from the mammalian iron carriers lactoferrin and transferrin across the outer membrane. These receptors are found only in bacteria which can infect mammals such as Moraxella, Mannheimia, Neisseria, Actinobacillus, Pasteurella, Haemophilus and Histophilus species [Transport and binding proteins, Cations and iron carrying compounds, Transport and binding proteins, Porins]
MKMKKHVLNLSILALSLLFATLSFQTADADSAKDTANQAVYLDEITVTATKVAHRRSNEVTGLGKVVKTA
ETLSKEQVLGIRDLTRYDPGISVVEQGRGASSGYSIRGVDKNRVAVTVDGIPQIQSYTSQGSRSGTAGSG
AINEIEYENVRSVEISKGANSSEYGSGALGGSVAFRTKDASDIIKPGKHWGLQSKTAYSSKNRHFLQSLA
AAGKAGGFEGLVIYTKRRGKETKAHGDANKGVQSIDRLDAFEQKYDLRPPQGRSFIVENECASLDCAPCA
QYGYVYDNQLSDEEKAQVLASRYRHEQVSAKDYTGENRLLPNPLDYRSDSWLAKLGYHLNNRHYVGGVLE
DTKQRYDIRDMTEPAYLGLSDAVKGRLKNGGGIYLGDNYLEGLNFNAGPASFKGLRYARGKFFDERHTKR
RYGLEYRYKNEDYDRWLDTAKLSLDKQKIELRSRLQELHCSQYPKVDKNCRPSLDKPYSFYKNDRNHYKE
KHNVIQAEFDKSFDLGGGRHHLNLLLGYDKFKSQLSRHDYRRQNAVGTYESIRGDEPKQNPYKYRLGKAT
IVKNSLCRYSETNGYANCCEPRKIKGSNHYISLNDNFTIGKYVDLGLGGRYDKHNFKSTDRLVYSGTYRN
LSWNFGIVVKPTPFFSLSYRASTGFRVPSFYELYGERRGKASKKNVQQFLRTPDLKPEKSLNHEIGARFK
GDFGHLEVSYFRNRYKDMIAEAPETRTDNEAGQTYGYCDHNYHNAQNAVLKGINILGKLDLNGVASKLPD
GLYSTLAYNRIKVKEVKNRAGRLDVRSPLLDAIQPARYVVGLGYDHPSQKWGINLTLTYSKAKNPDELAG
TEYLGNGNVVKQTATKKLSRSWYTLDVTGYVNLKKNLTLRAGVYNLFNYRYTTWESVRQTASNAVNQHTG
VSNYNRYAAPGRNYSLSLEMKF
>gnl|CDD|273800 TIGR01777, Hypothetical_UPF0105_protein_Rv2216/MT2273/Mb2239., TIGR01777 family protein. This model represents a clade of proteins of unknown function including the E. coli yfcH protein [Hypothetical proteins, Conserved]
ILITGGTGFIGRALTQRLTKRGHEVTILTRSPPPGANTKWEGYKPWAGEDADSLEGADAVINLAGEPIAD
KRWTEERKQEIRDSRIDTTRLLVEAIAAAEQKPKVFISASAVGYYGPSEDREYTEEDSPAGDDFLAELCR
DWEEAAQAAEDLGTRVVLLRTGIVLGPKGGALAKMLLPFRLGLGGPLGSGRQWFSWIHIEDLVQLILFAL
ENASVSGPVNATAPEPVRNKEFAKALARALHRPAFFPVPAFVLRALLGEMAALLLKGQRVLPEKLLEAGF
QFQYPDLDEAL
>gnl|CDD|273801 TIGR01778, TonB-copper, TonB-dependent copper receptor. This model represents a family of proteobacterial TonB-dependent outer membrane receptor/transporters which bind and translocate copper ions. Two characterized members of this family exist, outer membrane protein C (OprC) from Pseudomonas aeruginosa and NosA from Pseudomonas stutzeri which is responsible for providing copper for the copper-containing N2O reducatse [Transport and binding proteins, Cations and iron carrying compounds, Transport and binding proteins, Porins]
VVTDPKQNRQPVPASDGADYLKTIPGFSAIRKGGSGGDPVFRGQFGSRLNIVTDGGFVLGACPNRMDPPT
SYISPESYDSVTVIKGPQTVEYGPGGSAGTVLFERQPERFDALELYGGASGLRGSNGRFDAYLDAAAGDK
SGYIRFIGNYSDSNDYKDGDGNVVPSSYDKWNGNLALGWTPDADTVVELSHGASSGEARYAGRGMDASQF
RNNSTGLKFAKSNVSDVLEKVEAQIYYNYADHIMDNFRLRTPPAAAMPMQSPVDRRTLGGRLSLTWNHDG
MDLVVGVDHQGNQHDARRYRGTVGADDNLQSPWWKDATFLNYGLFAELTWPFAENNRLKAGLRYDRASVE
DGRAHATPNDAMGALAKLTSTDARTDTLMSGFVRYEQDLWGNQGNFYAGLGRAVRFPDYWELFSAKNHNN
SADNAFDGIKPEKTHQLDFGTQYQGQALKAWVSLFYGVVNDYILFDYQHSAGADGTVATNVDARLMGGEA
GFSYQFDPHWKTGASLAYAWGHNETDDQALPQIPPLEARFTLTYEADRWSFGALWRVVAKQTRIATDSGN
VVGKDFDKSAGFGTLSLNGAYRPMPNLTLSMGVDNLFDKRYAEHLNKAGDAGFGFSANLQVNEPGRTLWA
KLDFEF
>gnl|CDD|273802 TIGR01779, Vitamin_B12_transporter_BtuB, TonB-dependent vitamin B12 receptor. This model represents the TonB-dependent outer membrane receptor found in gamma proteobacteria responsible for translocating the cobalt-containing vitamin B12 (cobalamin) [Transport and binding proteins, Other, Transport and binding proteins, Porins]
MQKSALAPALASLLTLCSALHANEAQPLDTVVVTANRFAQTASQTLAPVTIITRQDIERTQAKSLPELLR
RLPGVSIAQNGGRGQNTSLFLRGTESDHVLVLIDGIRFGSAAAGAADFQQLPVELVERIEYVRGPRSSLY
GSEAIGGVINIITRRRSGGQGTTLSAGLGSLDYQEYSIASGVAIGENGWYSVALGTESTKGINVRPGGPG
VYDPDRDGFRSDSLLLGGGHRFDESWSLFVNALRYENRNDYDNYSFGTRLYKEAEKGDQSFTGGRQRQSE
RDVSELTLSTGKSKDWDYAYSKGRYSSTSDTREQRNIQWQNDLLVGDGWVLAGGVDWQKDSIISSTADKE
DDRSNTAAFAQVLQQWGQQLLEASLRRDDNQQFGSHTTGSIAWGYQFIEELRFTASYGTAFKAPNLNQLY
YPSYGNPNLQPETSKSAELGFYGLFSGGKWSISGYRTKINDLIDYDSHPKGYPNNIGEARIKGVEATAEF
ATGGWTHQLSVDLLDAQNVNTGNTLPRRARQMYKWNADRAFEQFDWGASYQYVGKRYDDDYNTYPTQNVR
LGGYSLLDLRVSYYVTDSWTVQGRIANLFDKDYETAYGYPQAGRAYYLSIRYQF
>gnl|CDD|188167 TIGR01780, Succinate-semialdehyde_dehydrogenase_mitochondrial, succinate-semialdehyde dehydrogenase. Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 & G-242, C-293 & G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070) [Central intermediary metabolism, Other]
VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENG
KPLKEAKGEILYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGA
ALAAGCTVVVKPAEQTPLSALALARLAEQAGIPKGVLNVITGSRAKEVGNVLTTSPLVRKISFTGSTNVG
KILMKQSASTVKKVSMELGGNAPFIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKK
LAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAVEKGAKVVTGGKRHELGGNFFEPTVLSNVTA
DMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWRVAEALEYGMVGINTGLISNV
VAPFGGVKQSGLGREGSKYGIEEYLETK
>gnl|CDD|273803 TIGR01781, Trep_dent_lipo, Treponema denticola clustered lipoprotein. This model represents a family of six predicted lipoproteins from a region of about 20 tandemly arranged genes in the Treponema denticola genome. Two other neighboring genes share the lipoprotein signal peptide region but do not show more extensive homology. The function of this locus is unknown
MKKDKLKLIFILMLAVLLFSCKKEDKESGLREMRVEKFSKMEEKENEFLSKPEYNTHVKSPEQIKELSNK
ISGVSGKGESDKFVGTPLVKDDYDLVYIQALYTSTNIGKDNRIYYLDHADNVEVIKVERDKEFIYCKQKR
TAKNGKDLFYSIKYEWYKRAKKFVNTKYELEQELNIGVIDEKIIKEQVHGIVIESKEDPDKESLIKMFES
YMNKLDKNDKYHYTTKKYYVLDYVKGNFTNSGYDEYIVFFTNDSRKEEEEDGEHHPWKNNICDVACFIVE
GDKFIKVYNIYFRGSSSLYGSLNPRQMPYITNFGKQFSQGWVADFNQNGINEIYIYFPWKTGTVRIFMIE
FIDKDFVFKCIEILGDEFNNVDWHKKKINGNYYSIELRDDTYGIIKYKEIYQWNEDDDNYWL
>gnl|CDD|273804 TIGR01782, TonB-dependent_receptor, TonB-dependent receptor. This model represents a family of TonB-dependent outer-membrane receptors which are found mainly in Xanthomonas and Caulobacter. These appear to represent the expansion of a paralogous family in that the 22 X. axonopodis (21 in X. campestris) and 18 C. crescentus sequences are more closely related to each other than any of the many TonB-dependent receptors found in other species. In fact, the Crescentus and Xanthomonas sequences are inseparable on a phylogenetic tree using a PAM-weighted neighbor-joining method, indicating that one of the two genuses may have acquired this set of receptors from the other. The mechanism by which this family is shared between Xanthomonas, a gamma proteobacterial plant pathogen and Caulobacter, an alpha proteobacterial aquatic organism is unclear [Transport and binding proteins, Porins]
LDAVQVTGQRASLEKAIDAKRDADSVVDVISAEDIGKLPDVNVAEALQRVPGVSIERDQGEGRYVSVRGL
GPSYNRTTLNGRTIASTDSGGRAFSLDLLPSELVSGVEVYKTPTADMDEGGIGGTVDLRTRSPFDYDGRT
LSGSAQGGYNDLAGKDKPGPRGAASYSWTFGDGQFGVLLSASYQKRDFAEDNVETENWGTYTSADGGAQG
LYFPRGVRYRSYRNDRERKGVNGSLQWRPSDALELYLDTLYSKYDDDETRQQIEFRTLNGGSTVITSNQT
ATSGALVQGTVANLQILVEARYNEEKETTTSLTLGGEWTGDRWTLDGDLGYSKATRDRPDRVTRFFTAPT
PGYDFDYRGGPTLTLGTPADGDDASNYTNPANGELRRTQISYQKAEDSEDAAQLDATFDGPFTSLKFGVR
YRRRDKTNRGSRYRRSIIGATGASGLAGVPSDLAGAGLDGGLGGPLTGWDPADLDAFLNAARGDAAGGGT
YTYASTAPNTYTVTEDTTAAYAMANFDTGLRLRGNVGVRYERTDQTSDGWQSQPAANGTGSVLVPVSADR
DYTDVLPSLNLAYDLTDDLVLRFAASKTITRPDFGDLAANTSLSDDGTGGTVTVSGGNPDLKPYESDNLD
LSLEWYFGPGGLLSAAVFYKDIKNFIVTTTSTETNDGGGGLVVAGVLVSRPVNGGKAGKIRGVELGYQQT
FDFLPGPLSGFGVQANYTYVDSEADPSVDGVQRRKLPLPGLSKNTANATLYYEKGGFSARLSYNYRSDYL
LDVGGSNINRLDRYVDPRGQLDLSASYQVSDHLSLGLQASNLTNEPSRWYTGGKQRPREYVETGRTYMLG
LRYKF
>gnl|CDD|273805 TIGR01783, Ferrienterobactin_receptor, TonB-dependent siderophore receptor. This subfamily model encompasses a wide variety of TonB-dependent outer membrane siderophore receptors. It has no overlap with TonB receptors known to transport other substances, but is likely incomplete due to lack of characterizations. It is likely that genuine siderophore receptors will be identified which score below the noise cutoff to this model at which point the model should be updated [Transport and binding proteins, Cations and iron carrying compounds, Transport and binding proteins, Porins]
DIPQSVSVITRQELEDQQAGSLSEALQRVPGVVVGGSGGTTQFGNITIRGFGLEVDIDNVYLDGVPLLSR
GNLAIVDPAMVERVEVLRGPASLLYGGSAPGGVINIVTKRPQDEPKGSVTFGAGTRSGYRTAFDLGGPLG
ADGTFRGRLNGARQDGDSFYDGAGEETRLGATATDWQLDDRTLLRLGAYYQKERDRGGYGGLPASGGTSG
RDLSSDRYLGTSSNRNYDDREYLSYGLSLEYQFNDVWTGKQNLRYSYFDTDSNQVQASGYSSDGGLFGRS
LTVVNVKQDRVQIDAGLDGEFETGPIEHDLLLGVSYGQRTTNRFNNTGYPSDNIYSLTATSSARTDIGDS
PKDRALSSTTKALNGVALQRILLADKWTLTLGGRYDSVDVKSNNGVAGSTGKRDDSQFTPSLGVAYKPTD
DWSLYASYAESFKPGGYYPKGAGNSGDILEPEKGKNYELGVRYDLGDSLLATAALFRITKDNQLVQDPVN
GTFSVNAGKTRNRGVELEARGYLTPGLSLSAGYTYTDAEFTEDTNGDTQGNTVPFVPKHTASLWASYAPP
VGDNGLTLGGGVQYTGKAYVDGGNTGKVPSYTVVDLSVRYDLTKKKNLTLALNVNNLFDRDYYTSGYRWG
PSAYIYPGAPRTVGLSVSYDF
>gnl|CDD|273806 TIGR01784, Uncharacterized_protein_pSLT051, conserved hypothetical protein (putative transposase or invertase). Several lines of evidence suggest that members of this family (loaded as a fragment mode model to find part-length matches) are associated with transposition, inversion, or recombination. Members are found in small numbers of genomes, but in large copy numbers in many of those species, including over 30 full length and fragmentary members in Treponema denticola. The strongest similarities are usually within rather than between species. PSI-BLAST shows similarity to proteins designated as possible transposases, DNA invertases (resolvases), and recombinases. In the oral pathogenic spirochete Treponema denticola, full-length members are often found near transporters or other membrane proteins. This family includes members of the putative transposase family pfam04754
PHDFLFKQLFGDENEDFLIIFLNAVLGELLDIKTLELSSQSFVEENLEDKFSDLDILATDSEGLHYNIEH
QVAPDKDMAKRMLYYWSAMYQSQLKQGDKYVVLAPTVFINILPFDLFGDEERVHNIYLSEEEDSIFELTD
LQELHLLELPKLKAIIDERLLDVLDRWLLLLKGKDNQSVNLIFLQIPFIQKAEEEIKTLLLSSKELELYE
QREKYMTDAISAEEEGKEEGIEEGILEAKLETAKKLLKNGLTLEQVAEATGLSVEELEEI
>gnl|CDD|273807 TIGR01785, Heme/hemopexin_utilization_protein_C, TonB-dependent heme/hemoglobin receptor family protein. This model represents the TonB-dependent outer membrane heme/hemoglobin receptor/transporter found in bacteria which live in contact with animals (which contain hemoglobin or other heme-bearing globins) or legumes (which contain leghemoglobin). Some species having hits to this model such as Nostoc, Caulobacter and Chlorobium do not have an obvious source of hemoglobin-like proteins in their biological niche and so the possibility exists that they act on some other substance [Transport and binding proteins, Cations and iron carrying compounds, Transport and binding proteins, Porins]
LDTVTVTATRTRQVLSEAPASVSVISGEQIESKQANNLADALNTVPGVDVTGGGRPPGQSINIRGLQDNR
VLVVVDGARQNYQRGGAHNGSLFVDPELLKRIEIVKGPSSSLYGSGALGGVVAFRTKDAADLLRPGQLFG
GLAKLSYGSNNNSFGGSVAVAGRLDDNLDALVAATYRDGGNYRNGNKEEATNSAYVQKNLLAKLGWQLDD
AQRLEFSYFTTEGSLDEAQNSGPGTEYVLGSSSTLLASSTRDRSATLTYNWTPEDNPWLDATASLYYNRT
ENDNDRSARGVGREEGYQYTTYGATLQNTSRFDVASWSTLTYGVDWMKDKRRTESFDPNSVTTIVPNPPS
AKEYFFGLFLQDNIPLLDDRLTLSAGLRYDHYKLSPKTTADTEAVDRSYSRWSPSLGLSYKPVDWLTLYA
SYSQGFRAPSIDELYGTGDHPGTPGGYTFAPNPNLKPETSKTWELGANLSFDNLLLDNDQLQFKVAYFYN
DVKDFIDLTIGVTDNVTAGMNNITQYVNIDGARIRGIEASASYDAGLWATGLSYGYTIGKDQNTNQWLSN
IPPLKLVVTVGYRFPDRRLDLGAKAAYYERQSESPTTEDVAANGLLTTPGYTVVDLYATYQPNAVKGLTV
RFGVNNLTDRKYTPAQSVPGAGPGRNFKGSVKYQF
>gnl|CDD|273808 TIGR01786, hemoglobin-haptoglobin-binding_protein, TonB-dependent hemoglobin/transferrin/lactoferrin receptor family protein. This model represents a family of TonB-dependent outer membrane receptor/transporters acting on iron-containing proteins such as hemoglobin, transferrin and lactoferrin. Two subfamily models with a narrower scope are contained within this model, the heme/hemoglobin receptor family protein model (TIGR01785) and the transferrin/lactoferrin receptor family model (TIGR01776). Accessions which score above trusted to this model while not scoring above trusted to the more specific models are most likely to be hemoglobin transporters. Nearly all of the species containing trusted hits to this model have access to hemoglobin, transferrin or lactoferrin or related proteins in their biological niche [Transport and binding proteins, Cations and iron carrying compounds, Transport and binding proteins, Porins]
DTITVTATRTADPQRRDLSVTPASVSVISREQLKSQQVRNLRDLLRYEPGVSVVEGGRGGSQGINIRGLD
KNRVAVLVDGIRQNTSYGGQGSTFYAINSIDPELIKSIEIVKGASSSLYGSGALGGVVAFRTKDAADLLK
PGKDLGGLSKLGYSSANNRFTQSVAAAGRNDDVDALVQATYRRGHELKNGNKANIGNESKRSKPNPSDYK
SQSFLAKLGWQLNDAHRLGLSLEYTQTDYDEPEMTNTSYLTKPLGAPLLSSTVVLGDSKTRDRRTGLDYE
LNPDNSWLDTVKLALDKQYIQLYNYLNATSASDYPGVDKNGRYKDKYDYYTLGFDTNNKIEFSVHSLSLT
YGLDRFKDKVSTGDSRRNLPTAAYNLYGYEGENRPVKGSNFGLFLQDNIKLGDWLSLSAGLRYDHYKTDP
KADESKDYGAISKTYSRWSPSLGLTYKPTPWLTLYYSYSQGFRAPSFDELYGTGAHPGGGPYTFLPNPNL
KPETSKNWEIGINLHFDQLDFKVSYFRNDYKDFIDLGIGVTAKGNMAQVGSNTITNYVNIDNARIRGIEL
SGRYDLGSFFSGPDGWTTTLKYGYTKGKDSDTNPWLNAITPLKVVLGLGYDHPDEKWGVGLTLTFSGAKD
AVDAYATYYENGEAAKAGPLRTPSYTVVDLYGYYKPNKNLTLRFGVYNLLDRKYTTWESARQAGPLATGY
TAPGRNYKASVEYKF
>gnl|CDD|273809 TIGR01787, Lanosterol_synthase, squalene/oxidosqualene cyclases. This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol
TARRAVEFLLSLQAPDGYWWGELEGPLTLLAEYVLLCHIADTPLPGYREKIVRYLRHHQNEDGGWGLHIG
GKSTVFGTVLAYVALKILGMSPDDPAMVRARNFILKQGGAVASPVFTKFWLALLGVYPWEGVPPLPPEIM
LLPKWLPIHPSKSWCRCRMVYLPMSYCYGERLSAPIDPREELYVEDDSIRAQRNNVAKEDLYTPHSWLLR
ALYGLLNLFYHPFLRKALRKRALQWLYEHIAADGSIGPISKAMAMLALWFLDGPNSPAFQKHLQRIDDYL
WLQLDGMKMQGTGSQVWDTAFAIQALRESGDHRLPEFHPALVKAHEWLLLSQIPDNPPGDWKVYRHNLKP
GGWAFSFLNCGYPDVDDTAVVALKAVLLLQEDEHVKRDRLRDAVNWILGMQSSNGGFAAYDPDNTGEWLE
LLNPSEVFGDIMIDPPYVDVTARVIQALGAFGHRADEIRNVLERALEYLRREQRADGSWFGRWGVNYTYG
TGFVLSALAAAGRTYRNCPEVQKACDWLLSRQMPDGGWGEDCFSYEDPSYVGSGGSTPSQTGWALMALIA
AGEADSEAIERGVKYLLETQRPDGDWPQEYITGVGFPKNFYLKYTNYRNIFPLWALGRYRQ
>gnl|CDD|130848 TIGR01788, Glutamate_decarboxylase_alpha_GAD-alpha., glutamate decarboxylase. This model represents the pyridoxal phosphate-dependent glutamate (alpha) decarboxylase found in bacteria (low and hi-GC gram positive, proteobacteria and cyanobacteria), plants, fungi and at least one archaon (Methanosarcina). The product of the enzyme is gamma-aminobutyrate (GABA)
SAYGSRAVSTGIPKYRMPEEEMPPDAAYQLIHDELSLDGNPRLNLATFVTTWMEPEARKLMDETINKNMI
DKDEYPQTAEIENRCVNMLADLWHAPAKDAEAVGTSTIGSSEAIMLGGLAMKWRWRKRMEAAGKPTDKPN
LVMGSNVQVCWEKFARYFDVELREVPMDPGRYVIDPEQVVEAVDENTIGVVCILGTTYTGEYEDVKALND
ALDEYNAKTGWDIPIHVDAASGGFIAPFVYPDLEWDFRLPRVKSINVSGHKYGLVYPGVGWVIWRDEEAL
PEELIFHVNYLGGDEPTFTLNFSRPANQVIAQYYNFLRLGREGYRKIMQNSLDVARYLAEEIAKLGPFEI
ISDGSGIPLVAFKLKDDADPGYTLYDLSHRLRERGWIVPAYTLPKNAEDIVVMRIVVREGFSRDLAELLI
EDIEAALAYLE
>gnl|CDD|130849 TIGR01789, lycopene_cyclase, lycopene cyclase. This model represents a family of bacterial lycopene cyclases catalyzing the transformation of lycopene to carotene. These enzymes are found in a limited spectrum of alpha and gamma proteobacteria as well as Flavobacterium
DCIIVGGGLAGGLIALRLQRARPDFRIRVIEAGRTIGGNHTWSFFDSDLSDAQHAWLADLVQTDWPGYEV
RFPKYRRKLKTAYRSMTSTRFHEGLLQAFPEGVILGRKAVGLDADGVDLAPGTRINARSVIDCRGFKPSA
HLKGGFQVFLGREMRLQEPHGLENPIIMDATVDQLAGYRFVYVLPLGSHDLLIEDTYYADDPLLDRNALS
QRIDQYARANGWQNGTPVRHEQGVLPVLLGGDFSAYQDEVRIVAIAGLRAGLTHPTTGYSLPVAVENADA
LAAQPDLSSEQLAAFIDSRARRHWSKTGYYRLLNRMLFFAAKPEKRVRVFQRFYGLREGLIERFYAARSN
TFDKLRVLWGKPPVPIHSAL
>gnl|CDD|130850 TIGR01790, Uncharacterized_carotenoid_cyclase_DR_0801, lycopene cyclase family protein. This family includes lycopene beta and epsilion cyclases (which form beta and delta carotene, respectively) from bacteria and plants as well as the plant capsanthin/capsorubin and neoxanthin cyclases which appear to have evolved from the plant lycopene cyclases. The plant lycopene epsilon cyclases also transform neurosporene to alpha zeacarotene
DLAVIGGGPAGLAIALELARPGLRVQLIEPHPPIPGNHTYGVWDDDLSDLGLADCVEHVWPDVYEYRFPK
QPRKLGTAYGSVDSTRLHEELLQKCPEGGVLWLERKAIHAEADGVALSTVYCAGGQRIQARLVIDARGFG
PLVQYVRFPLNVGFQVAYGVEARLSRPPHGPSSMVIMDARVDQLAAPELKGYRPTFLYAMPLGSTRVFIE
ETSLADRPALPRDRLRQRILARLNAQGWQIKTIEEEEWGALPVGLPGPFLPQRVAAFGAAAGMVHPTTGY
SVARALSDAPGLAAAIAQALCQSSELATAAWDGLWPTERRRQRYFRLLGRMLFLALEPEERRRFFQRFFG
LPEELWERFLAARLSLPDLLRVLLRMFGQPPNPVRSAL
>gnl|CDD|130851 TIGR01791, Chorismate_mutase/prephenate_dehydratase_PheA., chorismate mutase, archaeal type. This model represents a clade of archaeal chorismate mutases. Chorismate mutase catalyzes the conversion of chorismate into prephenate which is subsequently converted into either phenylalanine or tyrosine. In Sulfolobus this gene is found as a fusion with prephenate dehydrogenase (although the non-TIGR annotation contains a typographical error indicating it as a dehydratase OMNI|NTL02SS0274) which is the next enzyme in the tyrosine biosynthesis pathway. The Archaeoglobus gene contains an N-terminal prephenate dehydrogenase domain and a C-terminal prephenate dehydratase domain followed by a regulatory amino acid-binding ACT domain. The Thermoplasma volcanium gene is adjacent to prephenate dehydratase [Amino acid biosynthesis, Aromatic amino acid family]
IEELRQEIEEIDKSILDLIEKRIKIARKIGEIKHNNGLPITDEEREERVIERLRNTARNLGLDVLKLKEI
FEILMSLSKEEQR
>gnl|CDD|273810 TIGR01792, Urease_subunit_alpha, urease, alpha subunit. This model describes the urease alpha subunit UreC (designated beta or B chain, UreB in Helicobacter species). Accessory proteins for incorporation of the nickel cofactor are usually found in addition to the urease alpha, beta, and gamma subunits. The trusted cutoff is set above the scores of many reported fragments and of a putative second urease alpha chain in Streptomyces coelicolor [Central intermediary metabolism, Nitrogen metabolism]
KMSREQYASLYGPTTGDKVRLGDTDLFVEVEKDLTTYGDESKFGGGKVLRDGMGQNATLTRNAGVLDLVI
TNALILDWTGIYKADIGIKNGRIVGIGKAGNPDTMDGVDMIVGASTEAISGEGKIVTAGGIDTHVHYISP
QQVQAALDNGITTLIGGGTGPADGTNATTCTPGPWYLHRMLQAADGLPINFGFTGKGSGSGPAALIEQIE
AGACGLKVHEDWGATPAAIDNALSVADEYDVQVAVHTDTLNESGFVEDTIAAFKGRTIHTYHTEGAGGGH
APDIIVVVGYNNILPSSTNPTLPYTVNTIDEHLDMLMVCHHLNPKIPEDVAFAESRIRKETIAAEDVLQD
MGAISMISSDSQAMGRIGEVVTRCWQTADKMKKQRGPLPGDSPGNDNNRVKRYVAKYTINPAITHGISDY
IGSIEVGKLADLVLWEPAFFGVKPDMVLKGGLIAWAIMGDPNASIPTPQPVLYRPMFGAYGRALQSTSIT
FVSQAAYDKGIKERLGLQKLLLPVHNTRSIGKADMKLNSATPKIEVDPQTYDVKVDGVLITVEPADELPL
TQRYFLF
>gnl|CDD|130853 TIGR01793, Citrate_synthase_mitochondrial, citrate (Si)-synthase, eukaryotic. This model includes both mitochondrial and peroxisomal forms of citrate synthase. Citrate synthase is the entry point to the TCA cycle from acetyl-CoA. Peroxisomal forms, such as SP:P08679 from yeast (recognized by the C-terminal targeting motif SKL) act in the glyoxylate cycle. Eukaryotic homologs excluded by the high trusted cutoff of this model include a Tetrahymena thermophila citrate synthase that doubles as a filament protein, a putative citrate synthase from Plasmodium falciparum (no TCA cycle), and a methylcitrate synthase from Aspergillus nidulans
DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIP
ECQKLLPKAKGGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFA
TAVMALQVESEFAKAYAKGIHKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSISIDDSKDYSANF
AHMLGYDSPSFQELMRLYLTIHSDHEGGNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLL
WLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAVLRKTDPRYICQREFALKHLPDDPLFKLVSNL
YKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRALGILSQLIWDRALGLPLERPK
SVSTEWL
>gnl|CDD|130854 TIGR01795, CM_mono_cladeE, monofunctional chorismate mutase, alpha proteobacterial type. This model represents a small clade of monofunctional (non-fused) chorismate mutases spanning alpha proteobacteria and two actinobacter gram positive species. The alpha proteobacterial members are trusted because the pathways of CM are evident and there is only one plausible CM in the genome. In S. coelicolor, however, there is another aparrent monofunctional CM [Amino acid biosynthesis, Aromatic amino acid family]
AVAELKALRQSIDNIDAAVIHMLAERFKCTSQVGVLKANAGLAPADPAREDYQIARLRRLAIDAGLDPEF
AEKFLNFIVTEVIKHHERIADAGG
>gnl|CDD|130855 TIGR01796, CM_mono_aroH, monofunctional chorismate mutase, gram positive type, clade 1. This model represents a family of monofunctional (non-fused) chorismate mutases from gram positive bacteria (Firmicutes) and cyanobacteria. Trusted members of the family are found in operons with other enzymes of the chorismate pathways, both up- and downstream of CM (Listeria, Bacillus, Oceanobacillus) or are the sole CM in the genome where the other members of the chorismate pathways are found elsewhere in the genome (Nostoc, Thermosynechococcus) [Amino acid biosynthesis, Aromatic amino acid family]
VRAVRGATTVERNEAEEIGEAVAELLTELMERNELTPEDLISVIFTVTEDLHADFPAAAARGLPGWTDVP
VMCAQEIPVEGSLPRCIRVLIHIESEKPRTGIHHVYLREAAKLRPDL
>gnl|CDD|130856 TIGR01797, Includes:_Prephenate_dehydratase, chorismate mutase domain of proteobacterial P-protein, clade 1. This model represents the chorismate mutase domain of the gamma and beta proteobacterial "P-protein" which contains an N-terminal chorismate mutase domain and a C-terminal prephenate dehydratase domain [Amino acid biosynthesis, Aromatic amino acid family]
LLALREKISAIDEKLLKLLAERRELAFEVGKSKLLSHRPVRDIERERDLLQRLITLGKAYHLDAHYITRL
FQLIIEDSVLTQQ
>gnl|CDD|273811 TIGR01798, Citrate_synthase, citrate synthase I (hexameric type). This model describes one of several distinct but closely homologous classes of citrate synthase, the protein that brings carbon (from acetyl-CoA) into the TCA cycle. This form, class I, is known to be hexameric and allosterically inhibited by NADH in Escherichia coli, Acinetobacter anitratum, Azotobacter vinelandii, Pseudomonas aeruginosa, etc. In most species with a class I citrate synthase, a dimeric class II isozyme is found. The class II enzyme may act primarily on propionyl-CoA to make 2-methylcitrate or be bifunctional, may be found among propionate utilization enzymes, and may be constitutive or induced by propionate. Some members of this model group as class I enzymes, and may be hexameric, but have shown regulatory properties more like class II enzymes [Energy metabolism, TCA cycle]
NKSVELPIYSGTLGPDVIDIRKLYKQTGLFTFDPGFTSTASCESKITFIDGDKGILLYRGYPIDQLAEKS
DYLEVCYLLLYGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGALSAFYHDALD
INDPRHREISAIRLIAKIPTLAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNPVLARAMD
RIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKK
VKDKNDPFRLMGFGHRVYKNYDPRAKVMRETCHEVLKELGLHDDPLFKLAMELEKIALNDPYFIERKLYP
NVDFYSGIILKAMGIPTSMFTVIFALARTVGWISHWSEMISDPGQKIGRPRQLYTGETQRDY
>gnl|CDD|130858 TIGR01799, Includes:_Prephenate_dehydrogenase, chorismate mutase domain of T-protein. This model represents the chorismate mutase domain of the gamma proteobacterial "T-protein" which consists of an N-terminal chorismate mutase domain and a C-terminal prephenate dehydrogenase domain [Amino acid biosynthesis, Aromatic amino acid family]
LEDLRGEIDGVDQELLHLLAKRLELVAQVGKVKHAAGLPIYAPEREAAMLAARREEAEKAGIAPDLIEDV
LRRFMRESYANEN
>gnl|CDD|130859 TIGR01800, Citrate_synthase, 2-methylcitrate synthase/citrate synthase II. Members of this family are dimeric enzymes with activity as 2-methylcitrate synthase, citrate synthase, or both. Many Gram-negative species have a hexameric citrate synthase, termed citrate synthase I (TIGR01798). Members of this family (TIGR01800) appear as a second citrate synthase isozyme but typically are associated with propionate metabolism and synthesize 2-methylcitrate from propionyl-CoA; citrate synthase activity may be incidental. A number of species, including Thermoplasma acidophilum, Pyrococcus furiosus, and the Antarctic bacterium DS2-3R have a bifunctional member of this family as the only citrate synthase isozyme
KGLEGVIAGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGL
PDEVIELIEALPAESHPMDVLRTAVSYLGALDPEKFGHTPEEARDIAIRLLAKLPTIVAYWYRIRHGGEI
IAPKDDDSIAGNFLYMLHGEEPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGAL
KGPLHGGANEAVMAMLDEIGDPDKAEAWIRKALENKERIMGFGHRVYKTYDPRAKILKEYAKKLSAKEGS
SKWYEIAERLEDVMEEEKGIYPNVDFFSASVYYMMGIPTDLFTPIFAMSRVTGWTAHIIEQVENNRLIRP
RADYVGPEERKYVPIEER
>gnl|CDD|130860 TIGR01801, CM_A, chorismate mutase domain of gram positive AroA protein. This model represents a small clade of chorismate mutase domains N-terminally fused to the first enzyme in the chorismate pathway, 2-dehydro-3-deoxyphosphoheptanoate aldolase (DAHP synthetase, AroA) which are found in some gram positive species and Deinococcus. Only in Deinococcus, where this domain is the sole CM domain in the genome can a trusted assignment of function be made. In the other species there is at least one other trusted CM domain present. The similarity between the Deinococcus gene and the others in this clade is sufficiently strong (~44% identity), that the whole clade can be trusted to be functional. The possibility exists, however, that in the gram positive species the fusion to the first enzyme in the pathway has evolved a separate, regulatory role [Amino acid biosynthesis, Aromatic amino acid family]
MSNQSLEDLRAEVDQLNRQILALISRRGEVVAQIGHAKSAQGPNHYDPAREEQMLNELIKINPGPFPTAT
IKGIFKEIFKASLALQESNDKKQLLVSRKVKP
>gnl|CDD|273812 TIGR01802, Chorismate_mutase_1_chloroplastic, monofunctional chorismate mutase, eukaryotic type. This model represents the plant and yeast (plastidic) chorismate mutase. These CM's are distinct from other forms by the presence of an extended regulatory domain [Amino acid biosynthesis, Aromatic amino acid family]
LTLENIRSQLIRQEDSIIFGLIERAQFAYNKKVYEPGAFGDMDNFDGSLLDYLLKETEKLHARVRRFKSP
DEHPFFPDDLPEPILPPLKYPKILHFAAPSVNVNSKIKNMYIEDIVPRISKKDGEDDGNYGSTATCDIEC
LQSLSRRIHFGKFVAEAKFQASPEKYEKLIKAQDKEGIMDMITDPAVEEKILKRLAMKARTYGQDPKVPE
ESGVKIDPILVVDIYKDWVIPLTKEVEVEYLLRRLD
>gnl|CDD|130862 TIGR01803, Salicylate_biosynthesis_protein_PchB, chorismate mutase related enzymes. This subfamily includes two enzymes which are variants on the mechanism of chorismate mutase and are likely to have evolved from an ancestral chorismate mutase enzyme. 4-amino-4-deoxy-chorismate mutase produces amino-deoxy-prephenate which is subsequently converted to para-dimethylamino-phenylalanine, a component of the natural product pristinamycin. Isochorismate-pyruvate lyase presumably catalyzes the same type of 2+2+2 cyclo-rearrangement as chorismate mutase, but acting on isochorismate, this results in two broken bonds instead of one broken and one made. The product of this reaction is salicylate (2-hydroxy-benzoate) which is also incorporated into various natural products
LADIREAIDRIDLALVQALGRRMDYVKRASEFKRSHEAAIPAPERVAAVLPNAARWAEENGLDPPFVEGL
FAQIIHWYIAEE
>gnl|CDD|200131 TIGR01804, Betaine_aldehyde_dehydrogenase, betaine-aldehyde dehydrogenase. Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171) [Cellular processes, Adaptations to atypical conditions]
FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLI
RERNEELAKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGI
GAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNH
PDVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGT
RVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPEN
VGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRV
ADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK
>gnl|CDD|130864 TIGR01805, Shikimate_5-dehydrogenase, monofunctional chorismate mutase, gram positive-type, clade 2. This model represents a clade of chorismate mutase proteins/domains from gram positive species. The sequence from Enterococcus is fused to the C-terminus of an aparrent acetyltransferase, and the seuence from Clostridium acetobutylicum (but not perfringens) is fused to the N-terminus of shikimate-5-dehydrogenase, another enzyme of the chorismate pathway. All the other members of this clade are mono-functional. Members of this clade from Streptococcus and Lactococcus have been found which represent the sole chorismate mutase domain in their respective genomes which also exhibit evidence of the enzymes of both the upstream and downstream branches of the chorismate pathways [Amino acid biosynthesis, Aromatic amino acid family]
LELIRKKIDEIDDKLVVLFEERMEVVKEIAAYKKKNGIPIFDSKREQEIIDKCTKNVENKEYRETIEEFF
RNIMDISKEVQ
>gnl|CDD|130865 TIGR01806, Monofunctional_chorismate_mutase, chorismate mutase, putative. This model represents a clade of probable chorismate mutases from alpha, beta and gamma proteobacteria as well as Mycobacterium tuberculosis and a clade of nematodes. Although the most likely function for the enzymes represented by this model is as a chorismate mutase, in no species are these enzymes the sole chorismate mutase in the genome. Also, in no case are these enzymes located in a region of the genome proximal to any other enzymes involved in chorismate pathways. Although the Pantoea enzyme has been shown to complement a CM-free mutant of E. coli, this was also shown to be the case with isochorismate-pyruvate lyase which only has a secondary (non-physiologically relevant) chorismate mutase activity. This enzyme is believed to be a homodimer and be localized to the periplasm [Amino acid biosynthesis, Aromatic amino acid family]
DQSPQLGQLVDAANERLQLADDVAGYKARNNLPIEDSPREEQVLDSLRAQAQSAGLDPDYVTRFFQAQIN
ANKAIQYRLVSDWLNPPSPPPQVPDLTDTRSAIDQLNTEMLSAI
>gnl|CDD|130866 TIGR01807, Includes:_Prephenate_dehydratase, chorismate mutase domain of proteobacterial P-protein, clade 2. This model represents one of two separate clades of the chorismate mutase domain of the gamma and beta and epsilon proteobacterial "P-protein" which contains an N-terminal chorismate mutase domain and a C-terminal prephenate dehydratase domain. It is also found in Aquifex aolicus [Amino acid biosynthesis, Aromatic amino acid family]
LEELRNKIDAIDDRILDLLSERATYAQAVGELKGSGASGASFYRPEREAQVIRRLQNLNKGPLDQEAIAR
IFREIM
>gnl|CDD|130867 TIGR01808, Hypothetical_protein_Rv0948c/MT0975/Mb0973c., monofunctional chorismate mutase, high GC gram positive type. This model represents the monofunctional chorismate mutase from high GC gram-positive bacteria and archaea. Trusted annotations from Corynebacterium and Pyrococcus are aparrently the sole chorismate mutase enzymes in their respective genomes. This is coupled with the presence in those genomes of the enzymes of the chorismate pathways both up- and downstream of chorismate mutase [Amino acid biosynthesis, Aromatic amino acid family]
EIDTLREEIDRLDAEILALVKRRAEISQAIGKARMASGGTRLVHSREMKVIERYSELGPEGKDLAIKLLR
VGRG
>gnl|CDD|273813 TIGR01809, Shik-DH-AROM, shikimate-5-dehydrogenase, fungal AROM-type. This model represents a clade of shikimate-5-dehydrogenases found in Corynebacterium, Mycobacteria and fungi. The fungal sequences are pentafunctional proteins known as AroM which contain the central five seven steps in the chorismate biosynthesis pathway. The Corynebacterium and Mycobacterial sequences represent the sole shikimate-5-dehydrogenases in species which otherwise have every enzyme of the chorismate biosynthesis pathway [Amino acid biosynthesis, Aromatic amino acid family]
GNKGPKKAFIIGKPIAHSRSPHLHNAGYEILGLPDKTYEFETCSAEELKEVLSGFGPQFGGASVTIPLKF
AILRFADEHTDRASLIGSVNTLLRTQNGIWKGDNTDWDGIAGALANIGKFEPLAGFRGLVIGAGGTSRAA
VYALASLGVTDITVINRNPDKLSRLVDLGVQVGVITRLEGDSGGLAIEKAAEVLVSTVPADVPADYVDLF
ATVPFLLLKRKSSEGIFLDAAYDPWPTPLVAIVSAAGWRVISGLQMLLHQGFAQFEQWTGMPAPREAMAC
AL
>gnl|CDD|273814 TIGR01810, Oxygen-dependent_choline_dehydrogenase, choline dehydrogenase. Choline dehydrogenase catalyzes the conversion of exogenously supplied choline into the intermediate glycine betaine aldehyde, as part of a two-step oxidative reaction leading to the formation of osmoprotectant betaine. This enzymatic system can be found in both gram-positive and gram-negative bacteria. As in Escherichia coli, Staphylococcus xylosus, and Sinorhizobium meliloti, this enzyme is found associated in a transciptionally co-induced gene cluster with betaine aldehyde dehydrogenase, the second catalytic enzyme in this reaction. Other gram-positive organisms have been shown to employ a different enzymatic system, utlizing a soluable choline oxidase or type III alcohol dehydrogenase instead of choline dehydrogenase. This enzyme is a member of the GMC oxidoreductase family (pfam00732 and pfam05199), sharing a common evoluntionary origin and enzymatic reaction with alcohol dehydrogenase. Outgrouping from this model, Caulobacter crescentus shares sequence homology with choline dehydrogenase, yet other genes participating in this enzymatic reaction have not currently been identified [Cellular processes, Adaptations to atypical conditions]
DYIIIGGGSAGSVLAGRLSEDVSNSVLVLEAGGSDYPWDLLIQMPAALAYPAGNKRYNWIYETEPEPHMN
NRRVGHARGKVLGGSSSINGMIYQRGNPMDYEKWAKPEGMESWDYADCLPYYKRLETTFGGEKPYRGHDG
PIKVRRGPADNPLFQAFIEAGVEAGYNKTPDVNGFRQEGFGPMDSTVHNGRRVSAARAYLHPAMKRPNLE
VQTRAFVTKINFEGNRATGVEFKKGGRKEHTEANKEVILSAGAINSPQLLQLSGIGDAEHLRELGIEPRI
HLPGVGENLQDHLEVYVQHACKQPVSLYPSLNWLKQPFIGAQWLFGRKGAGASNHFEGGGFVRSNDDVDY
PNIQYHFLPVAIRYDGTKAPKAHGFQVHVGPMYSNSRGHVKIKSKDPFEKPEIVFNYMSHEEDWREFREA
IRVTREILKQKALDPYRGGEISPGPEVQTDEEIDEFVRRHGETALHPCGTCKMGPASDEMSVVDPETRVH
GMEGLRVVDASIMPRITNGNLNAPVIMMGEKAADIIRGKKPL
>gnl|CDD|130870 TIGR01811, sdhA_Bsu, succinate dehydrogenase or fumarate reductase, flavoprotein subunit, Bacillus subtilis subgroup. This model represents the succinate dehydrogenase flavoprotein subunit as found in the low-GC Gram-positive bacteria and a few other lineages. This enzyme may act in a complete or partial TCA cycle, or act in the opposite direction as fumarate reductase. In some but not all species, succinate dehydrogenase and fumarate reductase may be encoded as separate isozymes [Energy metabolism, TCA cycle]
VIVVGTGLAGGMAAAKLAELGYHVKLFSYVDAPRRAHSIAAQGGINGAVNTKGDGDSPWRHFDDTVKGGD
FRARESPVKRLAVASPEIIDLMDAMGVPFAREYGGLLDTRSFGGVQVSRTAYARGQTGQQLLLALDSALR
RQIAAGLVEKYEGWEMLDIIVVDGNRARGIIARNLVTGEIETHSADAVILATGGYGNVFGKSTNAMNSNA
SAAWRAYEQGAYFANPEFIQIHPTAIPVDGTWQSKLRLMSESLRNDGRIWTPKEKNDNRDPNTIPEDKRD
YFLERRYPAFGNLVPRDIASRAIFQVCDAGKGVGPGENAVYLDFSDADERLGRKEIDAKYGNLFEMYEKF
TGDDPYKVPMRIFPAVHYTMGGLWVDYDQMTNIPGLFAAGECDFSQHGANRLGANSLLSAIADGYFALPF
TIPNYLGPELSSEDMPEDAPEFQAALAEEQERFDRLLKMRGDENPYYLHRELGEIMTENCGVSRNNEKLL
KTDEKIRELRERFWKNIDIPGTTKESNQVLEFARRVADYLELAELMCLDALNRNESCGAHFRPEFPTPDG
EAERNDEEFLKVTAWEFQGENDAPEFHYEELDFELVPPRKRDY
>gnl|CDD|273815 TIGR01812, Fumarate_reductase_flavoprotein_subunit, succinate dehydrogenase or fumarate reductase, flavoprotein subunitGram-negative/mitochondrial subgroup. This model represents the succinate dehydrogenase flavoprotein subunit as found in Gram-negative bacteria, mitochondria, and some Archaea. Mitochondrial forms interact with ubiquinone and are designated EC 1.3.5.1, but can be degraded to 1.3.99.1. Some isozymes in E. coli and other species run primarily in the opposite direction and are designated fumarate reductase [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]
DVVIVGAGLAGLRAAVEAAKAGLNTAVISKVYPTRSHTVAAQGGMAAALGNVDPDDSWEWHAYDTVKGSD
YLADQDAVEYMCQEAPKAILELEHWGVPFSRTPDGRIAQRPFGGHSKDRTCYAADKTGHALLHTLYEQCL
KLGVSFFNEYFALDLIHDDGRVRGVVAYDLKTGEIVFFRAKAVVLATGGYGRIYKTTTNAHINTGDGMAM
ALRAGVPLKDMEFVQFHPTGLYPSGILITEGCRGEGGYLVNKNGERFMERYAPEKMELAPRDVVSRAMWT
EIREGRGVGSPPGDYVYLDLRHLGEEKIEERLPQIRELAKYFAGVDPVKEPIPVRPTAHYSMGGIPTDYT
GRVICETIVKGLFAAGECACVSVHGANRLGGNSLLELVVFGRIAGEAAAEYAAKTGNPAADIEEEAVKAE
EALIDLLVESNGGERVAKIREELGDTMDDNVGIFRTEELLKKAVDEIEELRERYKNVRINDKSKVFNTDL
LEALELGNMLDLAEVVAAGALNRKESRGAHAREDYPERDDENWLKHTLAYYDNPGTPRLEYKPVTITKYE
PAERKY
>gnl|CDD|273816 TIGR01813, Fumarate_reductase_flavoprotein_subunit, flavocytochrome c. This model describes a family of redox proteins related to the succinate dehydrogenases and fumarate reductases of E. coli, mitochondria, and other well-characterized systems. A member of this family from Shewanella frigidimarina NCIMB400 is characterized as a water-soluble periplasmic protein with four heme groups, a non-covalently bound FAD, and essentially unidirectional fumarate reductase activity. At least seven distinct members of this family are found in Shewanella oneidensis, a species able to use a wide variety of pathways for respiraton [Energy metabolism, Electron transport]
DVVVVGSGFAGLSAALSAKKAGAANVVLLEKMPVIGGNSAIAAGGMNAAGTDQQKALGIEDSPELFIKDT
LKGGRGINDPELVRILAEESKDAVDWLQDGVGARLDDLIQLGGHSVPRAHRPTGGAASGAEIVQTLYKKA
KKEGIDTRLNSKVEDLIQDDQGSVVGVVVKGKGKGIYIKAAKAVVLATGGFGSNKEMIAKYDPTLKHLGS
TNQPGATGDGLLMAEKIGAALVDMDYIQAHPTASPDEGGFLISEAVRGYGAILVNKTGERFMNELATRDK
VSDAILAQPGKDAYLIFDDDVYKKAKMVDNYYRLGVAYKGDSLEELAKQFGIPAAALKQTIKDYNGYVAS
GKDTPFGRPMDMPTDLSKAPYYAIKVTPGVHHTMGGVKINTKAEVLDANGKPIPGLFAAGEVTGGVHGAN
RLGGNAIADCIVFGRIAGE
>gnl|CDD|130873 TIGR01814, kynureninase, kynureninase. This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen [Energy metabolism, Amino acids and amines]
ALELDEADPLRALRDEFHLPKIGDENAVIYLDGNSLGLMPKAARNALKEELDKWAKIAIRGHNTGKAPWF
TLDESLLKLRLVGAKEDEVVVMNTLTINLHLLLASFYKPTPKRYKILLEAKAFPSDHYAIESQLQLHGLT
VEESMVQIEPREEETLRLEDILDTIEKNGDDIAVILLSGVQYYTGQLFDMAAITRAAHAKGALVGFDLAH
AVGNVPLDLHDWGVDFACWCTYKYLNAGPGAGAFVHEKHAHTERPRLAGWWGHARPTRFKMDNTLGLIPC
GFRISNPPILSVAALRGSLDIFDQAGMEALRKKSLLLTDYLEELIKARCGGPPVLTIITPRDHAQRGCQL
SLTHPVPGKAVFQALIKRGVIGDKREPSVIRVAPVPLYNTFVDVYDAVNVLEEILD
>gnl|CDD|130874 TIGR01815, Includes:_Glutamine_amidotransferase, anthranilate synthase, alpha proteobacterial clade. This model represents a small clade of anthranilate synthases from alpha proteobacteria and Nostoc (a cyanobacterium). This enzyme is the first step in the pathway for the biosynthesis of tryprophan from chorismate [Amino acid biosynthesis, Aromatic amino acid family]
YQTRGGVTVTRRATALDPRTALDPVIDALDRRRGLLLSSGYEYPGRYRRWALGFVDPPVALSARGRTLRI
DALNERGQVLLPAIAEALRGLEALAGLEEAPSRVTASSASPPAPFPEEERSKQPSVFTVLRAVLDLFASP
EDPLLGLYGAFGYDLAFQFEPIRQRLERPDDQRDLVLYLPDELVVVDPYAGLARLVAYDFITAAGSTEGL
ECGGRDHPYRPDTNAPPGCDHAPGEYARLVESAKAAFRRGDLFEVVPGQTFAEPCEDAPSSVFRRLKAIN
PSPYEFFVNLGRGEYLVGASPEMFVRVAGRRVETCPISGTIARGADAIGDAAQILRLLNSAKDEAELTMC
TDVDRNDKSRVCEPGSVKVIGRRQIELYSRLIHTVDHVEGRLRSGMDALDAFLSHSWAVTVTGAPKRWAM
QFIEDTEQSPRRWYGGAFGRLGFNGGMNTGLTLRTIRMADGIAEVRAGATLLYDSDPDAEEAETRLKAAA
FRDAIRRAKAAGAAPTLPAAPRGGEGRRILLVDHEDSFVHTLANYLRQTGASVTTLRHSHAEAAFDERRP
DLVVLSPGPGRPADFDVAGTIDAALARGLPVFGVCLGLQGMVEAFGGALDVLPEPVHGKASRIRVLGPDA
LFAGLPERLTVGRYHSLFARRDRLPAELTVTAESADGLIMAIEHRRLPLAAVQFHPESIMTLDGGAGLAM
IGNVVDRLAAGALTDAA
>gnl|CDD|130875 TIGR01816, Succinate_dehydrogenase_flavoprotein_subunit, succinate dehydrogenase, flavoprotein subunit, E. coli/mitochondrial subgroup. Succinate dehydrogenase and fumarate reductase are homologous enzymes reversible in principle but favored under different circumstances. This model represents a narrowly defined clade of the succinate dehydrogenase flavoprotein subunit as found in mitochondria, in Rickettsia, in E. coli and other Proteobacteria, and in a few other lineages. However, this model excludes all known fumarate reductases. It also excludes putative succinate dehydrogenases that appear to diverged before the split between E. coli succinate dehydrogenase and fumarate reductase [Energy metabolism, TCA cycle]
LAKGGVNTACVTKLFPTRSHTVAAQGGISAALGNMEEDNWRWHMYDTVKGSDWLGDQDAIEYMCKQAPEA
VLELEHMGMPFSRTEDGKIYQRPFGGHTRDFGKGGAAERACAAADRTGHAILHTLYQQNLKADTSFFNEY
FALDLLMEDGECRGVIAYCLETGEIHRFRAKAVVLATGGYGRIYFSTTNAHTLTGDGTGMVTRAGLPLQD
MEFVQFHPTGIAGAGCLITEGCRGEGGILINANGERFMERYAPTAKDLASRDVVSRSMTLEIREGRGVGP
NKDHVYLDLDHLGPEVLEGRLPGISETARTFAGVDPVKDPIPVLPTVHYNMGGIPTNYHGQVLRDGNGND
QIVPGLYAAGEAACVSVHGANRLGTNSLLDLVVFGRAAGLSAAEYAKPGSDVKPMPPNAGEESVMRLDKL
RFATGGERVAALRLELQRSMQNHAGVFRTGEVLQKGVEKISALKERYKNVKINDKSKVWNTDLVEALELQ
NLLECAEATAVSAEARKESRGAHAREDFPERDDENWLKHTLSYVDINTGKVLLSYKPVIFKPLTVADFEP
KKRVY
>gnl|CDD|273817 TIGR01817, Nif-specific_regulatory_protein, Nif-specific regulatory protein. This model represents NifA, a DNA-binding regulatory protein for nitrogen fixation. The model produces scores between the trusted and noise cutoffs for a well-described NifA homolog in Aquifex aeolicus (which lacks nitrogenase), for transcriptional activators of alternative nitrogenases (VFe or FeFe instead of MoFe), and truncated forms [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, DNA interactions]
DLQLAALYEISKILSAPTRLEKTLANVLNVLSNDLGMRHGLITLSDSEGEPLLVAAIGWSEEGFAPIRYR
VGEGAIGQIVATGNSLVVPDVAAEPLFLDRLSLYDPGPVPFIGVPIKADSETIGVLAADRDFRSRERLEE
EVRFLEMVANLIGQTVRLHRLVAQRRERLIAEAVQLSKQLRDKAPEIARRRSGKEDGIIGKSPAMRQVVD
QARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFTGAIA
QRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGE
FRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNRENGRPLTITPSAIRVLMSCKWPGNVRELENC
LERTATLSRSGTITRSDFSCQSGQCLSPMLAKTCPHGHISIDPLAGTTPPHSPASAALPGEPGLSGPTLS
ERERLIAALEQAGWVQAKAARLLGMTPRQVGYALRKLNIEMKKL
>gnl|CDD|273818 TIGR01818, Nitrogen_assimilation_regulatory_protein, nitrogen regulation protein NR(I). This model represents NtrC, a DNA-binding response regulator that is phosphorylated by NtrB and interacts with sigma-54. NtrC usually controls the expression of glutamine synthase, GlnA, and may be called GlnL, GlnG, etc [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, DNA interactions, Signal transduction, Two-component systems]
VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQ
LPVIVMTAHSDLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVALPADAGEAEDSAELIGEA
PAMQEVFRAIGRLSRSDITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEK
GAFTGANTRRQGRFEQADGGTLFLDEIGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNL
EALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLARHFLALAARELDVEPKLLDPEALERLKQLRWP
GNVRQLENLCRWLTVMASGDEVLVSDLPAELALTGRPASAPDSDGQDSWDEALEAWAKQALSRGEQGLLD
RALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLKEL
>gnl|CDD|130878 TIGR01819, F420_cofD, 2-phospho-L-lactate transferase. This model represents LPPG:Fo 2-phospho-L-lactate transferase, which catalyses the fourth step in the biosynthesis of coenzyme F420, a flavin derivative found in methanogens, the Mycobacteria, and several other lineages. This enzyme is characterized so far in Methanococcus jannaschii but appears restricted to F420-containing species and is predicted to carry out the same function in these other species. The clade represented by this model is one of two major divisions of proteins in pfam01933 [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
TVLSGGTGTPKLLQGLKEVLPDAELTVVVNTGEDVWVSGLLVCPDLDTVLYTLGGGIDRERWWGIADDTF
HTHERLKELGVPEGLRLGDRDRATHIVRTQMLRAGHSLSEVTEALCDAFGIKARLLPMTDDEVSTYVETD
EGAMHFQEFWVRRRGEPPVEDVDFRGAEKASIAPKVLEAIRKEDNILIGPSNPITSIGPILSLPGIREAL
RDKKVVAVSPIVGNAPVSGPAGKLMAAVGVEVSAAGVAEHYGDFLDVFVVDEVDKADEDRFGCHVRRTDT
LMTTLEDTARLARAVVD
>gnl|CDD|273819 TIGR01820, Anthranilate_synthase_component_1, anthranilate synthase component I, archaeal clade. This model represents an archaeal clade of anthranilate synthase component I enzymes. This enzyme is responsible for the first step of tryptophan biosynthesis from chorismate. The Sulfolobus enzyme has been reported to be part of a gene cluster for Trp biosynthesis [Amino acid biosynthesis, Aromatic amino acid family]
PLELYKAIRADGDYAFLLESAEKPSKKARYSFIGWDPEFVVRINGKGKSVEGIPEDGDVVDKLRNAFPKL
KGINIPGEDRRFKGGLVGYIAYDAVRDYWEGIVDLKRKAEDWPPAEFFIYPNTIVYDHLEGKVYYVSTPE
PEAELERIVERAKRATDPGEAGVSFEGESLSDREEFEEAVEEAKEYIFAGDIFQVVLSREYEYRLDGDPF
ELYYNLREINPSPYMFLLKFGDRYLVGSSPETLVRVEGRTVETNPIAGTRPRGATPEEDERLAKELLSDE
KERAEHVMLVDLARNDVRKVSEPGSVKVPEFMYVEKYSHVQHIESTVIGTLKKDYDAFDALRATFPAGTL
SGAPKIRAMEIIDELEKEPRGVYGGGVGYFSWNGDADFAIAIRTAEIDKDKLRIQAGAGIVADSIPEREF
EETENKMKAVLKAIG
>gnl|CDD|273820 TIGR01821, 5-aminolevulinate_synthase, 5-aminolevulinic acid synthase. This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPDGAKDVTVWCSNDYLGMGQHPEVLQAMHE
TLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELN
HASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALT
YLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLP
PAIAAGATASIRHLKESQDLRRAHQENVKRLKNLLEALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNK
HGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGLPLS
>gnl|CDD|130881 TIGR01822, 2am3keto_CoA, glycine C-acetyltransferase. This model represents a narrowly defined clade of animal and bacterial (almost exclusively Proteobacterial) 2-amino-3-ketobutyrate--CoA ligase, now called glycine C-acetyltransferase. This enzyme can act in threonine catabolism. The closest homolog from Bacillus subtilis, and sequences like it, may be functionally equivalent but were not included in the model because of difficulty in finding reports of function [Energy metabolism, Amino acids and amines]
FYAQLAAELESIREAGLFKSERIITSPQGADIRVADGREVLNFCANNYLGLSSHPDLIQAAKDALDEHGF
GMSSVRFICGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVR
LCKAKRYRYANNDMADLEAQLKEARAAGARHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHA
TGFLGPTGRGSHELCGVMGRVDIITGTLGKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGA
SIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKPADHPIIPVMLYDAVLAQRFARRLLEEGIYVTG
FFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI
>gnl|CDD|273821 TIGR01823, para-aminobenzoate_synthase_predicted, aminodeoxychorismate synthase, fungal clade. This model represents the fungal clade of a para-aminobenzoate synthesis enzyme, aminodeoxychorismate synthase, which acts on chorismate in a pathway that yields PABA, a precursor of folate
QQQQRLHVLFIDSYDSFTYNVVRLLEQQTDISVHVTTVHSDTFQDQLLELLPLFDAIVVGPGPGNPNNAQ
DMGIISELWELANLDEVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFSVKSTRY
HSLYANPEGIDTLLPLCLTEDEEGIILMSAQTKKKPWFGVQYHPESCCSELGSGKLVSNFLKLAFINNVK
TGRWEKKKLNGSFSDISSRLDRTDDRDPIYKVKEKYPSGTTYVKQFEVSEDPKLTFEICNIIREPKFVMS
SSVITGRYSIIALPNSASQVFTHYGAMLKTTVHYWQDTEISYTRLKKCLSGVDSDLDKSQFWITLGKFME
NKKIDNPHREIPFIGGLVGILGYEIGSDLSTQYIACGRCNDDENSLVPDAKLVFINRSIVIDHKQGKLYV
QSLDNTFPVALEWSGELRDSFVRKKNIKQSLSWPFYLPEEIDFVITFPDKEDYAKAFKACQDYLHAGDSY
EMCLTTQTKVVPPAVISPDWEIYQRLRQRNPAPFSGFFRLKHIIFLSTSPEKFLEVGMDTHAKLRPIKGT
VKKGPQMNLEKARRILKTPKEMGENLMILDLIRNDLYELVPKNDVHVEELMSVEEHATVYQLVSVVKAHG
LTSASKKTRYSGIDVLKHSLPPGSMTGAPKKRSVQLLQDVEGGARGIYSGVTGYWDVNGNGDFSVNIRCA
FSYNGGTSWRIGAGGAVTVLSTPEGELEEMYNKLESNLQIFM
>gnl|CDD|130883 TIGR01824, Anthranilate_synthase_component_I-like_protein, aminodeoxychorismate synthase, component I, clade 2. This clade of sequences is more closely related to TrpE (anthranilate synthase, TIGR00564/TIGR01820/TIGR00565) than to the better characterized group of PabB enzymes (TIGR00553/TIGR01823). This clade includes one characterized enzyme from Lactococcus and the conserved function across the clade is supported by these pieces of evidence: 1) all genomes with a member in this clade also have a separate TrpE gene, 2) none of these genomes contain an aparrent PabB from any of the other PabB clades, 3) none of these sequences are found in a region of the genome in association with other Trp biosynthesis genes, 4) all of these genomes aparrently contain most if not all of the steps of the folate biosynthetic pathway (for which PABA is a precursor). Many of the sequences hit by this model are annotated as TrpE enzymes, however, we believe that all members of this clade are, in fact, PabB. The sequences from Bacillus halodurans and subtilus which score below the trusted cutoff for this model are also likely to be PabB enzymes, but are too closely related to TrpE to be separated at this time
GGRLGWLAYDVARRLEGIPDLGTSDGGWPVAADFRYEAAVARDHQRQIVALATVPAETEGEFATSSDQLP
AVAAATSLPSPDVGPLPVDLEASIDRAAYETGVRRIKDYIRAGDVFQANLSRRLTAPIAADVDPLQLFLA
LRAPNPAPYAIYLEEPGVDVASASPELFLAREGRVVQTRPIAGTRPRGATLAEDGALAAELLQHDKDRAE
HVMIVDLERNDLGRVCATGTVRVPELCAVESYSHVHHLVSRVTGRLREGAGLADLIRALFPGGSITGAPK
VRAMEIIDELEPQPRGPYTGSVGWIDADGNADLNILIRTLEGGGAQLHFRTGAGIVADSDPAGEWDETEA
KARAL
>gnl|CDD|130884 TIGR01825, 8-amino-7-oxononanoate_synthase_1, pyridoxal phosphate-dependent acyltransferase, putative. This model represents an enzyme subfamily related to three known enzymes; it appears closest to glycine C-acteyltransferase, shows no overlap with it in species distribution, and may share that function. The three closely related enzymes are glycine C-acetyltransferase (2-amino-3-ketobutyrate coenzyme A ligase), 5-aminolevulinic acid synthase, and 8-amino-7-oxononanoate synthase. All transfer the R-group (acetyl, succinyl, or 6-carboxyhexanoyl) from coenzyme A to an amino acid (Gly, Gly, Ala, respectively), with release of CO2 for the latter two reactions
LRQDLNGLKENGLYISIRVLESAQGPRVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAV
RTIAGTLRLHEELEEKLAKFKKTEAALVFQSGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKAT
KKIYKHADMDDLDRVLRENPSYGKKLIVTDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGEA
GRGTVHHFGLEDKVDIQVGTLSKAIGVVGGYAAGHKELIEYLKNRARPFLFSTAQPPAVVAALAAAVDEL
QRSPELMERLWDNTRFFKAGLGKLGYDTGGSETPITPVVIGDEKAAQEFSRRLFDEGIFAQSIVFPTVPR
GTARIRNIPTAEHTKDDLDQALDAYEKVGKELGLI
>gnl|CDD|211689 TIGR01826, Putative_gluconeogenesis_factor, conserved hypothetical protein, cofD-related. This model represents a subfamily of conserved hypothetical proteins that forms a sister group to the family of CofD, (TIGR01819), LPPG:Fo 2-phospho-L-lactate transferase, an enzyme of cytochrome F420 biosynthesis. Both this family and TIGR01819 are within the scope of the pfam01933 [Hypothetical proteins, Conserved]
VVAIGGGTGLSVLLRGLKELDSRITAIVTVADDGGSSGRLREELDVPPPGDLRNCLAALSDDPSLLSKLF
QYRFGGGGELSGHSLGNLMLAALSEISGSFLEAINLLSKILKVKGRVLPMSEHPVTLVAEFEDGREVRGE
SNIPKMGGKIDRVRLEPEDVPALREAVEAIREADLIILGPGSLYTSIIPNLLVPEIAEALRESKAPKVYV
CNLMTQPGETDGFSLEDHVDALHRHLGKPFIDTVLVNTEKVPLEVLRNYFEEGSEQVEHDAEGLQKLGIE
VIFEDLLRAENGTIRHDPQKLADALERILQ
>gnl|CDD|130886 TIGR01827, gatC_rel, Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative. This model represents a family small family related to GatC, the third subunit of an enzyme for completing the charging of tRNA(Gln) by amidating the Glu-tRNA(Gln). The few known archaea that contain a member of this family appear to produce Asn-tRNA(Asn) by an analogous amidotransferase reaction. This protein is proposed to substitute for GatC in the charging of both tRNAs
KILKEAEEILEEFSERLEDVDEEEETYYISDGSNKFREDEEPRCDPEFKKKMLENAPVSDDGYVVVERGH
WLR
>gnl|CDD|273822 TIGR01828, Pyruvate_phosphate_dikinase, pyruvate, phosphate dikinase. This model represents pyruvate,phosphate dikinase, also called pyruvate,orthophosphate dikinase. It is similar in sequence to other PEP-utilizing enzymes [Energy metabolism, Other]
KKRVYAFGEGNASMKNLLGGKGANLAEMTKLGLPVPPGFTITTEACNEYYANGKQFPKGLQEEIKEALTL
LEEKTGKKFGDTENPLLVSVRSGAAVSMPGMMDTILNLGLNDETVEGLAKLTGNARFAYDSYRRFIQMFG
DVVLGIPHELFEQILEAMKEEKGVKLDTDLTADDLKELIEKYKAIYREATGKPFPQDPKEQLELAIKAVF
DSWNNPRAIVYRRLNDIPEDWGTAVNIQSMVFGNMGETSGTGVAFTRNPSTGEKGLFGEFLINAQGEDVV
AGIRTPQPITAMEADMPDVYKELLDIAEKLEGHYRDMQDIEFTIERGKLYMLQTRNGKRTAKAAVRIAVD
MVKEGLITEEEAIMRVEPKSLDQLLHPRFDPSALKTVLAKGLPASPGAATGKIVFSAEDAVELAEKGKKV
ILVREETSPEDIEGMHVAEGILTARGGMTSHAAVVARGMGKCCVSGCEELKINEEAKTFTIGGRVFHEGD
IISIDGSTGEIYLGEIPLIEPSVSGDFETIMDWADKIRKLKVRANADTPEDALTARKFGAEGIGLCRTEH
MFFGAERIPAVRKMILADSEEERQKALNKLLPFQKEDFKGLFKAMEGLPVTIRLLDPPLHEFLPHTEELQ
KELAEDMGLTLAEILKRVEELHEVNPMLGHRGCRLGITYPEIYEMQVRAIMEAAVEVKKEGIDVHPEIMI
PLVGEKNELKILKDVLEEVAAEVFKEYGVTVPYEIGTMIEIPRAALTADKIAEEADFFSFGTNDLTQMTF
GFSRDDAGKFLPKYLEKGILEKDPFESLDQTGVGQLMRMAVEKGRQTRPNLKVGICGEHGGDPSSIEFCH
KIGLNYVSCSPYRVPI
>gnl|CDD|273823 TIGR01829, Acetoacetyl-CoA_reductase, acetoacetyl-CoA reductase. This model represent acetoacetyl-CoA reductase, a member of the family short-chain-alcohol dehydrogenases. Note that, despite the precision implied by the enzyme name, the reaction of EC 1.1.1.36 is defined more generally as (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH. Members of this family may act in the biosynthesis of poly-beta-hydroxybutyrate (e.g. Rhizobium meliloti) and related poly-beta-hydroxyalkanoates. Note that the member of this family from Azospirillum brasilense, designated NodG, appears to lack acetoacetyl-CoA reductase activity and to act instead in the production of nodulation factor. This family is downgraded to subfamily for this NodG. Other proteins designated NodG, as from Rhizobium, belong to related but distinct protein families
RIALVTGGMGGIGTAICQRLAKDGYRVAANCGPNEERAEAWLQEQGALGFDFRVVEGDVSSFESCKAAVA
KVEAELGPVDVLVNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGWGRIINISSVNG
QKGQFGQTNYSAAKAGMIGFTKALAQEGATKGVTVNTISPGYIATDMVMAMREDVLNSIVAQIPVKRLGR
PEEIAAAVAFLASEEAGYITGATLSINGGLYM
>gnl|CDD|273824 TIGR01830, 3-oxoacyl-_reductase_FabG, 3-oxoacyl-(acyl-carrier-protein) reductase. This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis [Fatty acid and phospholipid metabolism, Biosynthesis]
ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEI
EEELGTIDILVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLM
GNAGQANYAASKAGVIGFTKSLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRFGQPE
EVANAVAFLASDEASYITGQVIHVDGGMY
>gnl|CDD|273825 TIGR01831, fabG_rel, 3-oxoacyl-(acyl-carrier-protein) reductase, putative. This model represents a small, very well conserved family of proteins closely related to the FabG family, TIGR01830, and possibly equal in function. In all completed genomes with a member of this family, a FabG in TIGR01830 is also found [Fatty acid and phospholipid metabolism, Biosynthesis]
VLVTGASRGIGRAIANQLAADGFNIGVHYHSDAAGAQETLNAIVANGGNGRLLSFDVADRVACREVLEAD
IAQHGAYYGVVLNAGIARDAAFPALSEDDWDAVIHTNLDGFYNVIHPCIMPMIGARQGGRIITLASVSGV
MGNRGQVNYSAAKAGLIGATKALAIELAKRKITVNCIAPGLIDTGMIAMEESALKEALSMVPMKRMGQPE
EVAGLASFLMSDIAGYVTRQVISVNGGML
>gnl|CDD|188170 TIGR01832, 2-dehydro-3-deoxy-D-gluconate_5-dehydrogenase, 2-deoxy-D-gluconate 3-dehydrogenase. This model describes 2-deoxy-D-gluconate 3-dehydrogenase (also called 2-keto-3-deoxygluconate oxidoreductase), a member of the family of short-chain-alcohol dehydrogenases (pfam00106). This protein has been characterized in Erwinia chrysanthemi as an enzyme of pectin degradation [Energy metabolism, Biosynthesis and degradation of polysaccharides]
FSLEGKVALVTGANTGLGQGIAVGLAEAGADIVGAGRSEPSETQQQVEALGRRFLSLTADLSDIEAIKAL
VDSAVEEFGHIDILVNNAGIIRRADAEEFSEKDWDDVMNVNLKSVFFLTQAAAKHFLKQGRGGKIINIAS
MLSFQGGIRVPSYTASKHAVAGLTKLLANEWAAKGINVNAIAPGYMATNNTQALRADEDRNAAILERIPA
GRWGTPDDIGGPAVFLASSASDYVNGYTLAVDGGWLAR
>gnl|CDD|273826 TIGR01833, Hydroxymethylglutaryl-CoA_synthase, 3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade. Hydroxymethylglutaryl(HMG)-CoA synthase is the first step of isopentenyl pyrophosphate (IPP) biosynthesis via the mevalonate pathway. This pathway is found mainly in eukaryotes, but also in archaea and some bacteria. This model is specific for eukaryotes
WPKDVGILALEIYFPSQYVDQAELEKYDGVSAGKYTIGLGQTKMGFCTDREDINSLCLTVVSKLMERYNI
DYDQIGRLEVGTETIIDKSKSVKTVLMQLFEESGNTDVEGIDTTNACYGGTAALFNAINWIESSSWDGRY
ALVVAGDIAVYAKGNARPTGGAGAVAMLIGPNAPIVFERGLRGSHMQHAYDFYKPDLASEYPVVDGKLSI
QCYLSALDRCYKSYCKKIEKQWGKSGSDRKFTLDDFDYMIFHSPYCKLVQKSLARLLYNDFLRNPSSTDT
SLYEGLEALSGLKLEDTYTDRDLEKAFMKASKELFDKKTKPSLLVPTQVGNMYTASLYGCLASLLSSKSA
QELAGKRVGMFSYGSGLAASMFSLRVSQDASPGSALDKLIASLSDLKNRLDSRHCVAPEEFEETMELREQ
AHHKKNFTPQGSIDSLFPGTWYLERVDSKHRRSYARK
>gnl|CDD|273827 TIGR01834, Uncharacterized_protein_Alvin_0062, poly(R)-hydroxyalkanoic acid synthase, class III, PhaE subunit. This model represents the PhaE subunit of the heterodimeric class (class III) of polymerase for poly(R)-hydroxyalkanoic acids (PHAs), carbon and energy storage polymers of many bacteria. The most common PHA is polyhydroxybutyrate but about 150 different constituent hydroxyalkanoic acids (HAs) have been identified in various species. This model must be designated subfamily to indicate the heterogeneity of PHAs [Cellular processes, Adaptations to atypical conditions, Fatty acid and phospholipid metabolism, Biosynthesis]
QFWLESQRQYWDNWFDLMRHGKGGAGAQAPPPWMGSADQWFESLPQQALQQQQFYGELLKLQFEAWFSLW
PQFANGFAPGAVQGYLQLQTWIEQYEATTQALQGDMDGQGQCYIKELMRFWQLPLSGWQSSVSPLGPLPT
GDLHAWLDLNNLYGDQLYRKNLSSFLSMPALGYSREMQSQLQRLFRDWMEYQQAMADYQLLEADIGYKSF
AALMSDLLARAKSGKPVKTAKALYDLWVIAAEEAYAEVFASEENAKVHGKFINALMRLRIQQQEIVEALL
KMLNLPTRSELDEAHQRIQQLRREVKSLKKRLGELEANPG
>gnl|CDD|213655 TIGR01835, 3-hydroxy-3-methylglutaryl_CoA_synthase, 3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade. This clade of hydroxymethylglutaryl-CoA (HMG-CoA) synthases is found in a limited spectrum of mostly gram-positive bacteria which make isopentenyl pyrophosphate (IPP) via the mevalonate pathway. This pathway is found primarily in eukaryotes and archaea, but the bacterial homologs are distinct, having aparrently diverged after being laterally transferred from an early eukaryote. HMG-CoA synthase is the first step in the pathway and joins acetyl-CoA with acetoacetyl-CoA with the release of one molecule of CoA. The Borellia sequence may have resulted from a separate lateral transfer event
IGIDKISFFTPQNYLDMTALAEARGVDPEKFHIGIGQKKMAVPPIDEDIVTMAASAAKPILDRNDKQKID
MVIFGTESGIDQSKAAAVYVHGLLGLQPFCRSFELKQACYGATAALQMAKGHVALSPDRKVLVIASDIAK
YGLESPGEPTQGAGAVAMLVSADPKLLAINEDSVLYTDDIMDFWRPNYSTTALVDGQYSNEQYLNAFENA
WNDYAKRTGLSLADFAAFCFHVPFTKMGLKALRHILKKNYEDEDESVQNAYLESIIYNREVGNLYTGSLY
LGLASLLENAFEDTTGDKIGLFSYGSGAVAEFFSGTLVAGYRDHLKKERHLALLKNRTNLSYAEYEALFE
ETLPTDGDQPGEDRGFFRLAGINDHKRIY
>gnl|CDD|130895 TIGR01836, Poly-beta-hydroxybutyrate_polymerase, poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit. This model represents the PhaC subunit of a heterodimeric form of polyhydroxyalkanoic acid (PHA) synthase. Excepting the PhaC of Bacillus megaterium (which needs PhaR), all members require PhaE (TIGR01834) for activity and are designated class III. This enzyme builds ester polymers for carbon and energy storage that accumulate in inclusions, and both this enzyme and the depolymerase associate with the inclusions. Class III enzymes polymerize short-chain-length hydroxyalkanoates [Fatty acid and phospholipid metabolism, Biosynthesis]
LQKLIESLAQEYLDFTRKLKEGYENLTNEEDIEVGVTPKEVVYREDKVVLYRYTPVKDNTHKTPLLIVYA
LVNRPYMLDLQEDRSLVRGLLERGQDVYLIDWGYPDRADRYLTLDDYINGYIDKCVDYICRTSKLDQISL
LGICQGGTFSLCYAALYPDKIKNLVTMVTPVDFETPGNMLSNWARHVDIDLAVDTMGNIPGELLNLTFLM
LKPFSLGYQKYVNLVDILEDERKVENFLRMEKWIFDSPDQAGEAFRQFVKDFYQQNGLINGEVEIGGRKV
DLKNIKMPILNIYAERDHLVPPDASKALNDLVSSEDYTELSFPGGHIGIYVSGKAQKEVPPAIGKWLQAR
>gnl|CDD|130896 TIGR01837, to_the_polyhydroxyalkanoate_inclusion, poly(hydroxyalkanoate) granule-associated protein. This model describes a domain found in some proteins associated with polyhydroxyalkanoate (PHA) granules in a subset of species that have PHA inclusion granules. Included are two tandem proteins of Pseudomonas oleovorans, PhaI and PhaF, and their homologs in related species. PhaF proteins have a low-complexity C-terminal region with repeats similar to AAAKP [Fatty acid and phospholipid metabolism, Biosynthesis]
RVGESARKVWLAGIGALARVQEEGSKFFNRLVKEGELAEKRGQKRFDESVDAAREEVKTALEQTRDQVQR
NWDKLEKAFDERVEQALNRLNIPSREEIEALSAKIEQLAVQVEELRRA
>gnl|CDD|213656 TIGR01838, Poly-beta-hydroxybutyrate_polymerase, poly(R)-hydroxyalkanoic acid synthase, class I. This model represents the class I subfamily of poly(R)-hydroxyalkanoate synthases, which polymerizes hydroxyacyl-CoAs with three to five carbons in the hydroxyacyl backbone into aliphatic esters termed poly(R)-hydroxyalkanoic acids. These polymers accumulate as carbon and energy storage inclusions in many species and can amount to 90 percent of the dry weight of cell [Fatty acid and phospholipid metabolism, Biosynthesis]
LSAQPARLFEAQASYWQQQMQLWQKALLRSAGEDVEPFADPEPGDRRFASPAWSSHPFFDFLKQSYLLNS
SWLLELVDAVEGLDPKTRRRLEFFTRQLINAMAPSNFLATNPEALRLTVETQGESLVRGMENLAEDLERG
GGDLKIRQTDSSAFEVGRNLATTPGAVVFENELFQLIQYEPTTETVHKTPLLIVPPWINKYYILDLRPQN
SLVRWLVEQGHTVFVISWRNPDASQADKTFDDYIRDGVIAALEVVEAITGEKQVNCVGYCIGGTLLSTAL
AYLAARGDDKRIKSATFFTTLLDFSDPGELGVFVDEEIVAGIERQNGGGGYLDGRQMAVTFSLLRENDLI
WNYYVDNYLKGKSPVPFDLLFWNSDSTNLPGKMHNFYLRNLYLQNALTTGGLEVCGVRLDLSKVKVPVYI
IATREDHIAPWQSAYRGAALLGGPKTFVLGESGHIAGVVNPPSKNKYGHWTNAALPADPEVWLAGATEHP
GSWWPDWAAWLAGHSGKQVPARNPGNAKYPPLEPAPGRYVKV
>gnl|CDD|130898 TIGR01839, Poly3-hydroxyalkanoate_polymerase_1, poly(R)-hydroxyalkanoic acid synthase, class II. This model represents the class II subfamily of poly(R)-hydroxyalkanoate synthases, which polymerizes hydroxyacyl-CoAs, typically with six to fourteen carbons in the hydroxyacyl backbone into aliphatic esters termed poly(R)-hydroxyalkanoic acids. These polymers accumulate as carbon and energy storage inclusions in many species and can amount to 90 percent of the dry weight of cell [Fatty acid and phospholipid metabolism, Biosynthesis]
MSNKNNDGLQRQPAENMLGQNAIIGLRGKDLLSTARTVLRQALRQPLHSAKHLAAFGGQLGNVLLGDTSL
QPNPDDRRFNDPAWSNNPFYRRYLQAYLAWQKQLQDWIGESDLDPDDRARAQFLINLMTDAMAPSNSLSN
PLAVKELFNTGGKSLLDGVSHLLKDLVHNGGMPSQVNMDAFEVGKNLATTEGAVVFRNEVLELIQYKPIT
EQQHARPLLVVPPQINKFYIFDLSPEKSFVQYCLKNQLQVFIISWRNPDKAHREWGLSTYVDALKEAVDA
VRAITGSRDLNLLGACAGGLTCAALVGHLQALGQLRKVNSLTYLVSLLDSTMESPAALFADEQTLEAAKR
RSYQAGVLDGSEMAKVFAWMRPNDLIWNYWVNNYLLGNEPPAFDILYWNNDTTRLPAAFHGDLLDMFKSN
PLTRPDALEVCGTPIDLKKVKCDSFSVAGTNDHITPWDAVYRSALLLGGKRRFVLSNSGHIQSILNPPGN
PKARYMTNAKLSSDPRAWQEDAKRHEGSWWPHWLSWLGERSGELEKPPTRLGNAAYPPLEAAPGTYVHER
>gnl|CDD|273828 TIGR01840, poly3-hydroxybutyrate_depolymerase_A_precursor, esterase, PHB depolymerase family. This model describes a subfamily among lipases of the ab-hydrolase family. This subfamily includes bacterial depolymerases for poly(3-hydroxybutyrate) (PHB) and related polyhydroxyalkanoates (PHA), as well as acetyl xylan esterases, feruloyl esterases, and others from fungi [Fatty acid and phospholipid metabolism, Degradation]
MYVYVPAGLTGPRALVLALHGCGQTASAYVIDWGWKAAADRYGFVLVAPEQTSYNSSNNCWDWFFTHHRA
RGTGEVESLHQLIDAVKANYSIDPNRVYVTGLSAGGGMTAVLGCTYPDVFAGGASNAGLPYGEASSSISA
TPQMCTAATAASVCRLVRGMQSEYNGPTPIMSVVHGDADYTVLPGNADEIRDAMLKVYGETGTATASTSV
AG
>gnl|CDD|130900 TIGR01841, hypothetical_protein, phasin family protein. This model describes a family of small proteins found associated with inclusions in bacterial cells. Most associate with polyhydroxyalkanoate (PHA) inclusions, the most common of which consist of polyhydroxybutyrate (PHB). These are designated granule-associate proteins or phasins; the member from Rhodospirillum rubrum is an activator of polyhydroxybutyrate (PHB) degradation. However, the member from Magnetospirillum sp. AMB-1 is called a magnetic particle membrane-specific GTPase
AFEGVERLVKLQLQALRATLDESVAASQRLASAGDPQELIALQTEFAKPAAEKLLAYSRELYEIAAKSQA
EALKLLRDRFAEGSREAQ
>gnl|CDD|200134 TIGR01842, Proteases_secretion_ATP-binding_protein_PrtD, type I secretion system ABC transporter, PrtD family. Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion [Protein fate, Protein and peptide secretion and trafficking]
LAKVKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVL
VRIGEKLDGALNQPIFAASFSATLRRGSGDGLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLH
PWIGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFH
SKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGG
WKQFSGARQAYKRLNELLANYPSRDPAMPLPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAII
GPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENAD
PEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGE
QALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAKL
>gnl|CDD|130902 TIGR01843, Hemolysin_secretion_protein_D_plasmid, type I secretion membrane fusion protein, HlyD family. Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins [Protein fate, Protein and peptide secretion and trafficking]
SRFARLITWLIAGLVVIFFLWAYFAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQV
LVELDATDVEADAAELESQVLRLEAEVARLRAEADSQAAIEFPDDLLSAEDPAVPELIKGQQSLFESRKS
TLRAQLELILAQIKQLEAELAGLQAQLQALRQQLEVISEELEARRKLKEKGLVSRLELLELERERAEAQG
ELGRLEAELEVLKRQIDELQLERQQIEQTFREEVLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDG
TVQSLKVHTVGGVVQPGETLMEIVPEDDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRRYGILNGKVK
SISPDTFTDERGGGPYYRVRISIDQNTLGIGPKGLELSPGMPVTADIKTGERTVIEYLLKPITDSVQEAL
RER
>gnl|CDD|273829 TIGR01844, Proteases_secretion_protein_PrtF, type I secretion outer membrane protein, TolC family. Members of this model are outer membrane proteins from the TolC subfamily within the RND (Resistance-Nodulation-cell Division) efflux systems. These proteins, unlike the NodT subfamily, appear not to be lipoproteins. All are believed to participate in type I protein secretion, an ABC transporter system for protein secretion without cleavage of a signal sequence, although they may, like TolC, participate also in the efflux of smaller molecules as well. This family includes the well-documented examples TolC (E. coli), PrtF (Erwinia), and AprF (Pseudomonas aeruginosa) [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Porins]
AALTLLDAVLLALANNPELRAARAQRDAGEEQVAQARAALLPQLGLTANYGYSNTYPTESRGRNTDLNSG
SSTLTLSQPLFDGGSTWNAVRAAEAAALAARETLRATAQDLILRTAEAYMEVLRAQEILALAEANLAALK
EQLDLARARFDVGLGTRTDVLQAEARYASARAQLIQAQNNLDDAKAQLRRLVGQPELAPLAVPSFPAELP
EPLDQLLEIAEASNPLLLAAQAAVDAARYQVEQARAGHLPTLSLTASTGNSDTSSGGSGNSDSDTYSVGL
NVSIPLYQGGATSAQVRQAAHQLNQSRSTLESQKRTVRQQVRNAWSNLNAAAASVQAYEQQVASAQKALD
AYRQEYQVGTRTLLDVLNAEQELYQARQELANARYDYLQAQLNLLSATGTLNEADLLLQNAALSK
>gnl|CDD|273830 TIGR01845, Outer_membrane_protein_OprM, efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family. Members of this model comprise a subfamily of the Outer Membrane Factor (TCDB 1.B.17) porins. OMF proteins operate in conjunction with a primary transporter of the RND, MFS, ABC, or PET systems, and a MFP (membrane fusion protein) to tranport substrates across membranes. The complex thus formed allows transport (export) of various solutes (heavy metal cations; drugs, oligosaccharides, proteins, etc.) across the two envelopes of the Gram-negative bacterial cell envelope in a single energy-coupled step. Current data suggest that the OMF (and not the MFP) is largely responsible for the formation of both the trans-outer membrane and trans-periplasmic channels. The roles played by the MFP have yet to be determined [Cellular processes, Detoxification, Transport and binding proteins, Porins]
LAAALLLSGCAVGPDYARPETPLAAGYLESDPTFGGQGRLSAGVWPAVDWWTAFGDPQLNALIEEALADN
PDLQVAEARLRAARANLRAARADFFPSLGLSASATRQKSSEDASGTTSGGSLSNTSTLTLDVSYELDLFG
KVRRAVESALAQLEAAEADSQAARLTLSASIANAYVQLAALRAQLDVYHAALASRRKTLELTQKRYAAGV
AAASDVRQAEAAVASAEAELPSLDVQIAQARNALAALLGKGPSRGLAIARPLLLDQLPPDLPLSLPSDLL
RRRPDIRAAERRLAAANAQIGVAKAAFFPSITLSASIGLSASQLSRLFDGGSRFWSIGPALALPIFDGGS
LRAALDSAKATYDAAVAQYRQTVLTAFQEVADALVALQALARRLDAQRQAVEQAQEALSLAQTRYRAGLD
SYLTVLEAQRSLLTAQRSLATLQARRLSDSVALYKALGGG
>gnl|CDD|273831 TIGR01846, type_I_sec_HlyB, type I secretion system ABC transporter, HlyB family. Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion [Protein fate, Protein and peptide secretion and trafficking]
GLEALSLLAQVHNIAVTPSQLRHMLGHAGASLDDLEILLAAKQLGLKAKAVKVSIGRLNKLPLPALIDGE
GGWFVLGKLTANGVTIYDPPGDAPEVLSREVLEALWSGTVILLATRSVAGKALKFGFSWFIPAIIRYRKQ
FREVLLISLALQLFALVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRI
DVELGARLYRHLLGLPLGYFESRRVGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTL
TGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAY
VAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQD
FQQTGIALERLGDILNSPTEPRSAGLAALPELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVG
PSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPF
EHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEA
LIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG
>gnl|CDD|130906 TIGR01847, Bacteriocin_lactacin-F_subunit_LafA, bacteriocin-type signal sequence. Bacteriocins are bacterial peptide products toxic to closely related bacteria. This model represents the N-terminal region up to the GG cleavage motif. Processing to remove this bacteriocin leader peptide occurs together with export by an ABC transporter. Note: because this model is so small (15 amino acids), it may have many spurious high-scoring matches to unrelated proteins, even with fairly stringent cutoff scores. The most likely true positives are small proteins of Gram-positive bacteria, matching regions that start within the first 15 amino acids, and encoded near bacteriocin transport family proteins (TIGR01000, TIGR01193)
FKELSEKELAQIIGG
>gnl|CDD|130907 TIGR01848, Uncharacterized_protein_Alvin_0064, polyhydroxyalkanoate synthesis repressor PhaR. Poly-B-hydroxyalkanoates are lipidlike carbon/energy storage polymers found in granular inclusions. PhaR is a regulatory protein found in general near other proteins associated with polyhydroxyalkanoate (PHA) granule biosynthesis and utilization. It is found to be a DNA-binding homotetramer that is also capable of binding short chain hydroxyalkanoic acids and PHA granules. PhaR may regulate the expression of itself, of the phasins that coat granules, and of enzymes that direct carbon flux into polymers stored in granules. The C-terminal region is poorly conserved in this family and is not part of this model.//GO terms added 12/6/04 [SS] [Fatty acid and phospholipid metabolism, Biosynthesis, Regulatory functions, DNA interactions]
RIIKKYPNRRLYDTETSSYVTLEDIRDLVREGREFQVVDSKSGDDLTRSILLQIIAEEESGGEPVLSTDF
LTQIIRFYGGSMQSFVPQYLEASLEMFAKQQQKFREQ
>gnl|CDD|130908 TIGR01849, unnamed_protein_product, polyhydroxyalkanoate depolymerase, intracellular. This model represents an intracellular depolymerase for polyhydroxyalkanoate (PHA), a carbon and energy storing polyester that accumulates in granules in many bacterial species when carbon sources are abundant but other nutrients are limiting. This family is named for PHAs generally, rather than polyhydroxybutyrate (PHB) specificially as in Ralstonia eutropha H16, to avoid overcalling chemical specificity in other species. Note that this family lacks the classic GXSXG lipase motif and instead shows weak similarity to some [Fatty acid and phospholipid metabolism, Degradation]
LYQLHETIRNTNAPMRLAARAMASYFSWPPNPLADHPFARRMHAGLELFERFTRRYGKPEWGIDEVEVDG
KDVPIRERVVWDKPFCRLIHFKRQGFRAELPGPAVLIVAPMSGHYATLLRSTVEALLPDHDVYITDWVNA
RMVPLSAGKFDLEDYIDYLIEFIRFLGPDIHVIAVCQPAVPVLAAVALMAENEPPAQPRSMTLMGGPIDA
RASPTVVNELAREKPIEWFQHNVIMRVPFPYPGAGRLVYPGFLQLAGFISMNLDRHTKAHSDFFLHLVKG
DGQEADKHRIFYDEYLAVMDMTAEFYLQTIDVVFQQFLLPQGKFIVEGKRVDPGAITRVALLTVEGENDD
ISGLGQTKAALRLCTGIPEDMKRHHLQPGVGHYGVFSGSRFREEIYPLVREFIRRN
>gnl|CDD|273832 TIGR01850, N-acetyl-gamma-glutamyl-phosphate_reductase, N-acetyl-gamma-glutamyl-phosphate reductase, common form. This model represents the more common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and the gap architecture in a multiple sequence alignment. Bacterial members of this family tend to be found within Arg biosynthesis operons [Amino acid biosynthesis, Glutamate family]
IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSRESAGKPVSEVHPHLRGLVDLNLEPIDVEEILEDAD
VVFLALPHGVSAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIK
GARLIANPGCYPTATLLALAPLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHR
HTPEIEQELGRLAGGKVKVSFTPHLVPMTRGILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEGG
YPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVKGAAGQAVQNMNLMFGFDETTGLPFPPLYP
>gnl|CDD|273833 TIGR01851, N-acetyl-gamma-glutamyl-phosphate_reductase_2, N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form. This model represents the less common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment [Amino acid biosynthesis, Glutamate family]
APKVFIDGEAGTTGLQIRERLSGRDDIELLSIAPDRRKDAAERAKLLNAADVAILCLPDDAAREAVSLVD
NPNTCIIDASTAYRTADDWAYGFPELAPGQREKIRNSKRIANPGCYPTGFIALMRPLVEAGILPADFPIT
INAVSGYSGGGKAMIADYEQGSADNPSLQPFRIYGLALTHKHLPEMRVHSGLALPPIFTPAVGNFAQGMA
VTIPLHLQTLASKVSPADIHAALADYYQGEQFVRVAPLDDVETLDNTFLDPQGLNGTNRLDLFVFGSDDG
ERALLVARLDNLGKGASGAAVQNLNIMLGL
>gnl|CDD|188173 TIGR01852, Acyl---UDP-N-acetylglucosamine_O-acyltransferase, acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase. This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKY
KGEKTRLIIGDNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEV
GDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSREEITAIKR
AYRTLFRSGLPLREAAQQVAEEYEDNPEVKEILDFIRESKRGIC
>gnl|CDD|273834 TIGR01853, UDP-3-O-acylglucosamine_N-acyltransferase, UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD. This model describes LpxD, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
ELAERLGAELKGNGDIVITGVAPLEKAKANHITFLANPKYLKHLKSSQAGAVIVSPDDQGLPAKCAALVV
KDPYLAFAKVAELFDPPPKREAGIHPTAVVDPSAKIGDGVTIGPNVVIGAGVEIGENVIIGPGVVIGDDV
VIGDGSRIHPNVVIYERVQLGKNVIIHSGAVIGSDGFGYAHTANGGHVKIPQIGRVIIEDDVEIGANTTI
DRGAFDDTIIGEGTKIDNLVQIAHNCRIGENCIIVAQVGIAGSTKIGRNVIIGGQVGVAGHLEIGDNVTI
GAKSGVTKSIPPPGVYGGIPARPNKEWLRIAAKVKRLPELRKRI
>gnl|CDD|273835 TIGR01854, UDP-23-diacylglucosamine_hydrolase, UDP-2,3-diacylglucosamine diphosphatase. This model represents LpxH, UDP-2,3-diacylglucosamine hydrolase, and essential enzyme in E. coli that catalyzes the fourth step in lipid A biosynthesis. Note that Pseudomonas aeruginosa has both a member of this family that shares this function and a more distant homolog, designated LpxH2, that does not. Many species that produce lipid A lack an lpxH gene in this family; some of those species have an lpxH2 gene instead, although for which the function is unknown [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
TLFISDLHLSPERPDITALFLDFLREEARKADALYILGDLFEAWIGDDDPSTLARSVAQAIRQVSDQGVP
CYFMHGNRDFLIGKRFAREAGMTLLPDPSVIDLYGQKVLLMHGDTLCTDDTAYQAFRAKVHQPWLQRLFL
HLPLAVRVKLARKIRAESRADKQMKSQDIMDVNPAEVAAVMRRYGVDRLIHGHTHRPAIHPLQADGQPAT
RIVLGDWYRQGSILRVDADGA
>gnl|CDD|273836 TIGR01855, Imidazole_glycerol_phosphate_synthase_subunit_HisH, imidazole glycerol phosphate synthase, glutamine amidotransferase subunit. This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6 [Amino acid biosynthesis, Histidine family]
IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRL
GKPVLGICLGMQLLFERSEEGGGVPGLGLIKGNVVKLEARKVPHMGWNEVHPVKESPLLNGIDEGAYFYF
VHSYYAVCEEEAVLAYADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL
>gnl|CDD|273837 TIGR01856, Probable_histidinol-phosphatase, histidinol phosphate phosphatase, HisJ family. This model represents the histidinol phosphate phosphatase HisJ of Bacillus subtilis, and related proteins from a number of species within a larger family of phosphatases in the PHP hydrolase family. HisJ catalyzes the penultimate step of histidine biosynthesis but shows no homology to the functionally equivalent sequence in E. coli, a domain of the bifunctional HisB protein. Note, however, that many species have two members and that Clostridium perfringens, predicted not to make histidine, has five members of this family; this family is designated subfamily rather than equivalog to indicate that members may not all act as HisJ
RDSHSHSPFCAHGTDTLREVVQEAIQLGFEEICFTEHAPRPFYYPEEDFLKKEMLFLSLPEYFQEINQLK
QEYADKIKILIGLEVDYIPGFEEEIKDFLDSYNLDFVIGSVHHLGGIPIDFDIEEFDETLFSFQKNLEQA
QRDYFESQYDSIQNLFKPLVIGHLDLVKKFGPLTDVSSKSDEVRELLQRILKAVASYGKALEINTSGFRK
PLEEAYPSKELLNLAKELGIPLVLGSDAHGPGQVGLSYHKAKK
>gnl|CDD|130916 TIGR01857, FGAM-synthase, phosphoribosylformylglycinamidine synthase, clade II. This model represents a single-molecule form of phosphoribosylformylglycinamidine synthase, also called FGAM synthase, an enzyme of purine de novo biosynthesis. This model represents a second clade of these enzymes found in Clostridia, Bifidobacteria and Streptococcus species. This enzyme performs the fourth step in IMP biosynthesis (the precursor of all purines) from PRPP [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
KRVFVEKKAGFDVESQSLVKELRHNLGLSSLKDLRIVNVYDVFDLAEELFAPTVKTIFSEPVTDHVLDEL
SVQADLAKFFAVEFLPGQFDQRADSAQECILLLSESEDVTVNTAKLYILNGDLDDEELNKIKNYYINPVD
SREKDLTTGKALEEFSESPKEVETLTGFESYDAEDLAKFKAEQGLAMSLEDLKFIQDYFKSIGRNPTETE
IKVLDTYWSDHCRHTTFETELKHVTFSDSKFQKQLKKAYEDYLAMREELGRSEKPVTLMDMATIFAKYLR
KNGKLDDLEVSEEINACSVEIEVDVDGVKEPWLLMFKNETHNHPTEIEPFGGAATCIGGAIRDPLSGRSY
VYQAMRVTGAGDPTVPISETLKGKLPQRKITTTAAHGYSSYGNQIGLATGQVSEIYHPGYVAKRMEVGAV
VAATPKENVVREKPEPGDVIILLGGKTGRDGIGGATGSSKEHTVESLELCGAEVQKGNAPEERKIQRLFR
NGNVTRLIKKCNDFGAGGVSVAIGELADGLEIDLNKVPKKYEGLNGTELAISESQERMAVVVSPEDVDAF
LAYCNEENLEATVVATVTEKPRLVMNWNGKTIVDLSRRFLDTNGVRQVIDAKVVDKDVKLPEERQKTSAE
TLEEDWLKVLSDLNVASQKGLQERFDSSVGAGTVLMPLGGKYQLTPTEASVAKLPVLGGETHTASAIAWG
FNPYIAEWSPYHGAAYAVIESLAKLVAAGADYKKARLSFQEYFEKLDKDAERWGKPFAALLGAIKAQIDL
GLPAIGGKDSMSGTFEELTVPPTLISFAVTTANSRRVISPEFKAAGENIYLIPGQALEDGTIDFDLLKEN
FAQIEELIADHKVVSASAVKYGGVAESLAKMTFGNRIGAELNNPELEDLFTAQYGSFIFESPEELSIANV
EKIGQTTADFVLKVNGEKLDLEELESAWEGKLEEVFPSKFEDKKETVEVPAVASEKKVIKAKEKVEKPRV
VIPVFPGTNSEYDSAKAFEKEGAEVNLVIFRNLNEEALVESVETMVDEIDKSQILMLPGGFSAGDEPDGS
AKFIAAILRNPKVRVAIDSFLARDGLILGICNGFQALVKSGLLPYGNIEAANETSPTLTYNDINRHVSKI
VRTRIASTNSPWLSGVSVGDIHAIPVSHGEGRFVASDEVLAELRENGQIATQYVDFNGKPSMDSKYNPNG
SSLAIEGITSPDGRIFGKMGHSERYGDGLFKNIPGNKDQHLFASGVKYF
>gnl|CDD|130917 TIGR01858, Tagatose-16-bisphosphate_aldolase_agaY_TBPA., class II aldolase, tagatose bisphosphate family. This model describes tagatose-1,6-bisphosphate aldolases, and perhaps other closely related class II aldolases. This tetrameric, Zn2+-dependent enzyme is related to the class II fructose bisphosphate aldolase; fructose 1,6-bisphosphate and tagatose 1,6 bisphosphate differ only in chirality at C4
IVSTKYMLQDAQAGGYAVPAFNIHNLETIQAVVETAAEMRSPVILAGTPGTFKHAGTEYIVALCSAASTT
YNMPLALHLDHHESLDDIRQKVHAGVRSAMIDGSHFPFAQNVKLVKEVVDFCHRQDCSVEAELGRLGGVE
DDLSVDEEDALYTDPQEAKEFVEATGVDSLAVAIGTAHGLYKKTPKLDFDRLAEIREVVDVPLVLHGASD
VPDEDVRRTIELGICKVNVATELKIAFSGAVKAYFAENPQANDPRYYMRPGKDAMKKVVRNKINVCGSAG
RA
>gnl|CDD|130918 TIGR01859, Fructose-bisphosphate_aldolase, fructose-1,6-bisphosphate aldolase, class II, various bacterial and amitochondriate protist. This model represents of one of several subtypes of the class II fructose-1,6-bisphosphate aldolase, an enzyme of glycolysis. The subtypes are split into several models to allow separation of a family of tagatose bisphosphate aldolases. This form is found in Gram-positive bacteria, a variety of Gram-negative, and in amitochondriate protists. The class II enzymes share homology with tagatose bisphosphate aldolase but not with class I aldolase [Energy metabolism, Glycolysis/gluconeogenesis]
LVNGKEILQKAKKEGYAVGAFNFNNLEWTQAILEAAEEENSPVIIQVSEGAIKYMGGYKMAVAMVKTLIE
RMSIVPVALHLDHGSSYESCIKAIKAGFSSVMIDGSHLPFEENLALTKKVVEIAHAKGVSVEAELGTLGG
IEDGVDEKEAELADPDEAEQFVKETGVDYLAAAIGTSHGKYKGEPGLDFERLKEIKELTNIPLVLHGASG
IPEEQIKKAIKLGIAKINIDTDCRIAFTAAIRKVLTEKKDEYDPRKILGPAREAIKETVKEKMRLFGSAG
KA
>gnl|CDD|130919 TIGR01860, Nitrogenase_vanadium-iron_protein_alpha_chain, nitrogenase vanadium-iron protein, alpha chain. This model represents the alpha chain of the vanadium-containing component of the vanadium-iron nitrogenase compound I. The complex also includes a second alpha chain, two beta chains and two delta chains. Compount I interacts with compound II also known as the iron-protein which transfers electrons to compound I where the catalysis occurs [Central intermediary metabolism, Nitrogen fixation]
PLKLLECDEDIPERQKHVYIKEPGEDTTEFLPLSNIATIPGSLSERGCSYCGAKLVIGGVLKDTIQMIHG
PLGCAYDTWHTKRYPSDNGNFQLKYVWSSDMKESHVVFGGEKQLEKSIHEAFDEFPDIKRMIVYTTCPTA
LIGDDIKAVAKKVQKELPDVDIFTVECPGFAGVSQSKGHHVLNIGWINEKVGTLEPEITSEYTINVIGDY
NIQGDTQVLQKYWDKMGIQVIAHFTGNGTYDDLRCMHRAQLNVVNCARSAGYIANELKKRYGIPRLDVDT
WGFNYMAEALRKIGAFFGIEDKAEEVIAEEYAKYKPKLDWYKERLQGKKMCIWTGGPRLWHWTKALEDDL
GMQVVAMSSKFGHQEDFEKVIARGKEGTIYIDDGNELEFFEVLDLIKPDVIFTGPRVGELVKKLHIPYVN
GHGYHNGPYMGFEGAVNMARDMYNAIYSPLRHLAAVDIRDK
>gnl|CDD|130920 TIGR01861, Nitrogenase_iron-iron_protein_alpha_chain, nitrogenase iron-iron protein, alpha chain. This model represents the all-iron variant of the nitrogenase component I alpha chain. Molybdenum-iron and vanadium iron forms are also found. The complete complex contains two alpha chains, two beta chains and two delta chains. The component I associates with component II also known as the iron protein which serves to provide electrons for component I [Central intermediary metabolism, Nitrogen fixation]
MPYHEFECSKCIPERAMHAVIKGPGEDLTSCLPLGYLNTIPGTISERGCAYCGAKHVIGTPMKDVIHISH
GPVGCTYDTWQTKRYISDNDNFQLKYTFATDVKEKHVVFGAEKLLKQNIIEAFKAFPHIKRMTIYQTCAT
ALIGDDIAAIAKEVMEEMPDVDIFVCNSPGFAGPSQSGGHHKINIAWINQKVGTVEPEIKGKHVINYVGE
YNIQGDQEVMVDYFQRMGIQVLSTFTGNGSYDDLRGMHRAHLNVLECARSAEYICNELRKRYGIPRLDID
GFGFEPLAASLRKVAMFFGIEDEAQAIIDEETARWKPELDWYKERLKGKKVCLWPGGSKLWHWAHVIEEE
MGLKVVSVYSKFGHQGDMEKGVARCGEGALAIDDPNELEGLEAMEMLKPDIILTGKRPGEVSKKMRVPYL
NAHAYHNGPYKGFEGWVRFARDIYNAIYSPIHQLSGMDISKDEAPTDKGFRTRQMISDVNISDDVTTSEE
LRPYTGDYDSVTRLRGRTYPKLE
>gnl|CDD|273838 TIGR01862, Nitrogenase_molybdenum-iron_protein_alpha_chain, nitrogenase component I, alpha chain. This model represents the alpha chain of all three varieties (Mo-Fe, V-Fe, and Fe-Fe) of component I of nitrogenase [Central intermediary metabolism, Nitrogen fixation]
DRKKHIVVKDPGETQSEKLPIANTKTIPGLMTERGCAYAGAKGVIGGPIKDMIHISHGPVGCTYYTWGTK
RYPSDNENGVGAFLKYVFSTDMQESDIVFGGEKKLKKLIHEAFTEFPLIKAISVYATCPTGLIGDDIEAV
AKEVSKEIGKDVVAVNCPGFAGVSQSKGHHIANIAVINDKVGTREKEITTEYDVNIIGEYNIGGDAWVMR
IYLEEMGIQVVATFTGDGTYDEIRLMHKAKLNLVHCARSANYIANELEERYGIPWMKIDFFGFTYTAESL
RAIAAFFGIEKRAEEVIAEEKAKWKPELDYYKERLQGKRVCLYIGGSRLWHWIGSAEEDLGMEVVAVGYE
FAHEDDYEKTMKRMGEGTLLIDDPNELEFEEILEKLKPDIIFSGIKEKFVAQKLGVPYRQMHSYDNGPYH
GFEGFVNFARDMYNAIYNPCWKL
>gnl|CDD|273839 TIGR01863, CRISPR-associated_protein_CT1133_family, CRISPR-associated protein Cas8c/Csd1, subtype I-C/DVULG. CRISPR loci appear to be mobile elements with a wide host range. This model represents a protein that tends to be found near CRISPR repeats of the DVULG subtype of CRISPR/Cas locus. We designate this family Csd1 (CRISPR/Cas Subtype DVULG protein 1). The species range for this subtype, so far, is exclusively bacterial and mesophilic, although CRISPR loci in general are particularly common among archaea and thermophilic bacteria. In a few species (Xanthomonas axonopodis pv. citri str. 306 and Streptococcus mutans UA159), homology to this protein family is split across two tandem genes; the trusted cutoff to this family is set low enough to capture at least the longer of the two
LQALYEYYERKLLQDDALPIGFETKKIPFFIVLDEDGQFLRLEDLRKTDGKKLIPRTLLVPQRVGRTVGL
APNLLWDNADYVLGQGSFAKGEQERADECHAAFKELLRKVAEETEDPEGLKAILDFLSQPELVEDALEAI
EKSEEIDTPGANLAFRVDGEPEPVHERPAVRAWWARHLAEAESGPTGICLVTGREAPLARLHPKIKGVGA
QASGAKLVSFNNSAFESYGKEQGANAPVSYEAAFAYVTALNYLLEKDSRQRLQIGDATTVFWASDSSTLD
PLEEIFGDLLEDPPEDDPEPAARLAQLFALRIGKPTGGAWPLLADDTRFYVLGLSPNAGRLSVRYWRELT
VGELLENLERHFDDLEWEPRPKDDGPPSLWRILSATAGQGKSENVPPDLAGRLLRSILDGGPYPRSLLSA
ALMRIRADVAYREEWYKRLALLKACLNRQNRRGKKKKELPVALDPTNTNRAYLLGRLLAVLEKLQERALG
PGLNATIRDRYYGAASSTPAAVFPTLLRLAQHHLSKLGKNKPGRAVYLERELEEILELLDPPFPVTLSLP
LQGRFALGYYHQRAALFTKKEEET
>gnl|CDD|273840 TIGR01865, conserved_hypothetical_protein, CRISPR subtype II/NMENI RNA-guided endonuclease Cas9/Csn1. CRISPR loci appear to be mobile elements with a wide host range. This model represents a protein found only in CRISPR-containing species, near other CRISPR-associated proteins (cas), as part of the NMENI subtype of CRISPR/Cas locus. The species range so far for this protein is animal pathogens and commensals only
EYILGLDIGIASVGWAIVEDDYKVPAAKRLIDGGVRNFTGAELPKTGETAALDRRLARGARRRIRRRKHR
LLRLQELFSREGSLTDFDFFSRLENSFLVEEDKRNTIYHLRKAALENKLKPDELYLALLHIIKHRGHFLI
EGNDFDTANKETGALLSAVMINRYLEHEADLRTLKELILKKFPKKYKEIFSETFLRNQRGFYNGSIPRQL
LLEELEAIFRKQREYYPFIKLLTFRIPYYIGPLAEGKSEFAFVDKPASAENFIEKMTGKCTYLPEEKRAP
KHSLLAEKFTVLNELNNVRIIILEQGETKILSKEEKQELLDLLFKKKKLTYKKLRKLLGLSEDAIFKGLR
YEGLDNAEKAFNISLKTYHKLRKALGDKDLLDNPKNPKDLDEIVKILTLYKDREMIKKRLELYKDVLNEE
QVKKLVRLHFTGWGRLSLKALRGIRPLMEQGKRYDEAILELGGNRNFMQNINDSQLLPKINITKAKDEIL
NPVVKRALLQARKVVNELVKKYGPPDKIVIEMAREEQGTNFGKRNSKERYKKNEDKIKEFASALGKEILK
EEPTENSSKNILKLRLYYQQNGKCMYTGKEIDIDDLFDLSYYEIDHILPQSRSFDDSISNKVLVLASENQ
EKGDQTPYEAEIVKKDSAFWNKFEAYVLISKRKSDKLTRAERGGLSDDDKAGFIDRNLNDTRYITRVVAN
YLKDRFNFHLKKRKVKVVTLKGQLTSQLRKKWGLYKKREINNYHHAHDAYINAVSTNALVKKFSQLEPEF
RYKEYHNFDGRKKKKSATDKKVKFSNPMEFFKQKV
>gnl|CDD|273841 TIGR01866, CRISPR-associated_Csn2_family_protein, CRISPR type II-A/NMEMI-associated protein Csn2. CRISPR loci appear to be mobile elements with a wide host range. This model represents a protein found only in CRISPR-containing species, near other CRISPR-associated proteins (cas), as part of the NMENI subtype of CRISPR/Cas loci. The species range so far for this subtype is animal pathogens and commensals only. This protein is present in some but not all NMENI CRISPR/Cas loci
KLVYPGLEEPIEIEDGKVTVLVIENPKVYRKIILELYSQKNGDEGKIKLSDDDKEVDIEKNIDLITDVLN
IDINDKKILKKIYKKLEELITDEELRNKIIDLVAQLVELIEELLLELDLPLEVNDEIDLKSLLKAVGIKI
ETEYDNLLEKIISYLKILTELLKKKIFIFVNLRHYLTKEELEELYEYIKYTNIKVLLIENREINSLSQYE
FKYIIDEDLCEI
>gnl|CDD|273842 TIGR01868, hypothetical_protein, CRISPR-associated protein Cas5/CasD, subtype I-E/ECOLI. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This family is part of the ECOLI subtype CRISPR/Cas locus, and now characterized as part of the CASCADE complex of that system. It shares a small N-terminal homology region with members of several other CRISPR/Cas subtypes, and we view the families that share this region as being Cas5
SYLLLRLEGPLQAWGTVSRFGERDTLDFPTRSGLLGLLAAALGIRRDEPERLQELQDRLQFAVRVDREGV
VLRDFQTAGTGKRKRRTLLWGKPEGRGASYGATIVTRREYLGDASFTVALELPAAATPALDEIAAALRRP
VWPLYLGRKSCVPTRPLFLKEVVAATVQEALAAYPPDGNDRQREVEGPATHTILNDVDVRFDRKGRQFAT
RRIREI
>gnl|CDD|273843 TIGR01869, CRISPR_system_Cascade_subunit_CasC, CRISPR-associated protein Cas7/Cse4/CasC, subtype I-E/ECOLI. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This family is represented by CT1975 of Chlorobium tepidum and is part of the Ecoli subtype of CRISPR/Cas locis. It is designated Cse4, for CRISPR/Cas Subtype Ecoli protein 4
TFIQIHLLQSYPPSNLNRDDTGAPKTAVFGGKRRTRVSSQSLKRAWRLSAYYHEALAGHSGIRTRRLAQL
LAKRLQELGEDEDIAEFDAAKIAKGLKLASGKKVDKLLLLSAPETAPLAVLAEAWFDELAAAAEADAVAD
KALKKVLKALLDAARVNQGVDIALFGRMLASLPEGNVDAAVQVAHAITTHQVEVEVDFFTAVDDLQKAEE
SGSGHLGETEFSSGTFYRYANIDLDQLVENLGGDRELALQAVEAFTHALATVVPGAKQNSTAAFNPADLV
LIEFRDDQPLSLANAFEKAIKAKRGQLLPSVQALNGYLEKLANVY
>gnl|CDD|273844 TIGR01870, CRISPR_type_III-associated_protein_Csm2, CRISPR type III-A/MTUBE-associated protein Csm2. These proteins are found adjacent to a characteristic short, palidromic repeat cluster termed CRISPR, a probable mobile DNA element. This model represents the C-terminal domain of a minor family of CRISPR-associated protein from the Mtube subtype of CRISPR/Cas locus. The family is designated Csm2, for CRISPR/Cas Subtype Mtube Protein 2
LTTTQLRRFYDELRRIEEKIRRSEQKNEDITAELHMLKPKLAYAVGREGIREFEGFVELLEDLLDKIDKI
DNDDRRAFERFVKFFEAIVAYHKFYGG
>gnl|CDD|233610 TIGR01873, CRISPR-associated_endoribonuclease_Cas2, CRISPR-associated endoribonuclease Cas2, subtype I-E/ECOLI. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This model represents a minor branch of the Cas2 family of CRISPR-associated endonuclease, whereas most Cas2 proteins are modeled instead by TIGR01573. This form of Cas2 is characteristic for the Ecoli subtype of CRISPR/Cas locus
MLVVVTENVPPRLRGRLALWLLEVRAGVYVGDVSAKVRERIWEQLAQLCAEKGSVVMTWATNTETGFEFQ
TLGENRKEIVEIDGLRL
>gnl|CDD|273845 TIGR01874, CRISPR-associated_protein_Cas5, CRISPR-associated protein Cas5, subtype I-A/APERN. This model represents a minor family of CRISPR-associated (Cas) protein. These proteins are found adjacent to a characteristic short, palidromic repeat cluster termed CRISPR, a probable mobile DNA element. This family belongs to a set of several Cas proteins, one each for a number of different CRISPR/Cas subtypes, that share a region of N-terminal sequence similarity modeled by TIGR02593. The family is designated Cas5a, for CRISPR-associated protein Cas5, Apern subtype
VVAKLRWPFYSSKPESYQVAPSLPLPPPSTLIGALSYGKYLLGDTKGGKAGSPALKIVVKAAAKASNVFA
PGVKTEVVIRRVRMVLEELRNLRRGELKFRSDAMPRGYIYAPNQVVKVVYRAEMDKERLEKALWLIDRLG
DTECLVSVRDVEIGEAKEVKGKVKTSVKFPKV
>gnl|CDD|273846 TIGR01875, CRISPR-associated_protein_Cas7/Cst2/DevR, CRISPR-associated autoregulator DevR family. CRISPR is a term for Clustered Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR associated) proteins. This model represents one such family, represented by MJ0381 of Methanococcus jannaschii. This family includes the DevR protein of Myxococcus xanthus, a protein whose expression appears to regulated through a number of means, including both location and autorepression; DevR mutants are incapable of fruiting body development [Regulatory functions, DNA interactions, ]
VLVLTRTPVNNHSLNGGETIGNISSLKKVRVGDGRVVPYVSGEALKHALRVRLVEFELCELSKIYATIKF
SGEDVIKKAGSKLVEKELILKYIDADLFGFMYAEKGGTVRRTSPVKVSYAISITPFINERAQLDRDFGVR
SKISKQEEEGGQMPYETEYHSTLYQYSFFLDLDRIGVPESFEKVNYVLPDDERKKRVKALLKALPPLLGG
NIGANLTDFSPVFVLFSLVVRKSPKPL
>gnl|CDD|273847 TIGR01876, cas_Cas5d, CRISPR-associated protein Cas5, subtype I-C/DVULG. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This small Cas family is represented by CT1134 of Chlorobium tepidum. This family belongs to a set of several Cas protein families, one each for a number of different CRISPR/Cas subtypes, that share a region of N-terminal sequence similarity modeled by TIGR02593. This family represents the Dvulg subtype of CRISPR/Cas locus
LEVKGDYALFTRPETKGGVERVSYSVPTPQALRGIFEAIYWKPTIRWRIREIEVLNPIQWESVGVREVGI
ETARQLRAGLYLRDVAYRLKAHFEFNPPREDLRKDRNPGKHYAIFERSARKGGRRDPFLGCRECSGEVRL
VDDEANEPPPYYNGSETRNLGFMLHDFDYPKNLKEPPLPPAFFPAVMENGVIKFPDWESCEIV
>gnl|CDD|273848 TIGR01877, CRISPR-associated_endoribonuclease_Cas6_1, CRISPR-associated endoribonuclease Cas6. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This broadly distributed, highly divergent Cas family is now characterized as an endoribonuclease that generates guide RNAs for host defense against phage and other invaders. The family contains a C-terminal motif GXGXXXXXGXG, where the each X between two Gly is hydrophobic and the spacer XXXXX contains (usually) one Arg or Lys. The seed alignment for the current version of this model has gappy columns removed. Members of this protein family are found associated with several different CRISPR/cas system subtypes, and consequently we designate this family Cas6
ELHDKKKFKPFTFSVLFPKKREINKGIIEFKGPYSFYISSLDDELIESLYNGLLKLPEFKIGGLSFEVKE
IKVLEPPEITDEVTFKTLSPIVIRTKRKGKKKDYYLLPDDELFFESLKRNLIKKYNLFYGEEPELEEFEF
EPLKVKKVVLKPVRIKKKGIYGFAGEGVFRIKGDPEKLLKFAYYSGLGEKTSQGFGMVE
>gnl|CDD|273849 TIGR01878, Uncharacterized_protein_AF_1870, CRISPR type I-A/APERN-associated protein Csa5. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This model represents a minor family of Cas protein found in the (all archaeal) APERN subtype of CRISPR/Cas locus, so the family is designated Csa5, for CRISPR/Cas Subtype Protein 5
FFLYSESPTYVDRFGNALSKEAVEVALYEAQRILRSIREGADIDIEGKRYMEKEGKNRILVGYLPTDKEV
EDFLRDVREDIRYAKLAAALALAIPSR
>gnl|CDD|200138 TIGR01879, N-carbamoyl-L-amino_acid_hydrolase, amidase, hydantoinase/carbamoylase family. Enzymes in this subfamily hydrolize the amide bonds of compounds containing carbamoyl groups or hydantoin rings. These enzymes are members of the broader family of amidases represented by pfam01546
QRLWETLMWLGEVGADPAGGMTRLALSPEDREAQDLFKKRMRAAGLEVRFDEVGNLIGRKEGTEPPLEVV
LSGSHLDTVVNGGNFDGQLGVLAGIEVVDALKEAYVVPLHPIEVVAFTEEEGSRFPYGMWGSRNMVGLAN
PEDVRNICDAKGISFAEAMKACGPDLPNQPLRPRGDIKAYVELHIEQGPVLESNGQPIGVVNAIAGQRWY
KVTLNGESNHAGTTPMSLRRDPLVAASRIIHQVEEKAKRGDPTVGTVGKVEARPNGVNVIPGKVTFTLDL
RHTDAAVLRDFTQQLENDIKAISDERDIGIDIERWMDEPPVPCSEELVAALTELCERLGYNARVMVSGAG
HDAQILAPIVPIGMIFIPSINGISHNPAEWSNITDCAEGAKVLYLMVYQL
>gnl|CDD|273850 TIGR01880, Ac-peptdase-euk, N-acyl-L-amino-acid amidohydrolase. This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids
MSSSKWEEDIAVTRFREYLRINTVQPNPDYAACVDFLIKQADELGLARKTIEFVPGKPVVVLTWPGSNPE
LPSILLNSHTDVVPVFREHWTHPPFSAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHI
SFVPDEEIGGHDGMEKFAKTDEFKALNLGFALDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKLM
ENTAMEKLEKSVESIRRFRESQFQLLQSNPDLAIGDVTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSV
DFEEMENRLDEWCADAGEGVTYEFSQHSGKPLVTPHDDSNPWWVAFKDAVKEMGCTFKPEILPGSTDSRY
IRAAGVPALGFSPMNNTPVLLHDHNEFLNEAVFLRGIEIYQTLISALASV
>gnl|CDD|273851 TIGR01881, CRISPR_system_Cmr_subunit_Cmr5, CRISPR type III-B/RAMP module-associated protein Cmr5. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This model family, represented by TM1791.1 of Thermotoga maritima, is found in both archaeal and bacterial species as part of the 6-gene CRISPR RAMP module
EQERAKLAIKVVEEVEKSDKQFREKYRSRVRKLPSMILNNGLIPTLAFYLSKAENCTLNKFVSDETSYTK
YYAHILYWLKERELVDKFKNALKELMEKDYSDSRIATEEALRYLNWLKRLAEALLKE
>gnl|CDD|130937 TIGR01882, Peptidase_T, peptidase T. This model represents a tripeptide aminopeptidase known as Peptidase T, which has a substrate preference for hydrophobic peptides [Protein fate, Degradation of proteins, peptides, and glycopeptides]
KYEELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEKNGYVIATIPSNTDK
DVPTIGFLAHVDTADFNGENVNPQIIENYDGESIIQLGDLEFTLDPDQFPNLSGYKGQTLITTDGTTLLG
ADDKAGIAEIMTAADYLINHPEIKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYET
FSAAAAKITIQGNNVHPGTAKGKMINAAQIAIDLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHY
IIRDFEKENFQERKELMKRIVEKMNNEYGQDRIKLDMNDQYYNMAEKIEKVMEIVDIAKQAMENLGIEPK
ISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDVIVEIAKLNEEQA
>gnl|CDD|162579 TIGR01883, Uncharacterized_protein_YqjE, peptidase T-like protein. This model represents a clade of enzymes closely related to Peptidase T, an aminotripeptidase found in bacteria. This clade consists of gram positive bacteria of which several additionally contain a Peptidase T gene
RLKKYFLELIQIDSESGKEKAILTYLKKQITKLGIPVSLDEVPAEVSNDNNLIARLPGTVKFDTIFFCGH
MDTVPPGAGPEPVVEDGIFTSLGGTILGADDKAGVAAMLEAMDVLSTEETPHGTIEFIFTVKEELGLIGM
RLFDESKITAAYGYCLDAPGEVGNIQLAAPTQVKVDATIAGKDAHAGLVPEDGISAISVARMAIHAMRLG
RIDEETTANIGSFSGGVNTNIVQDEQLIVAEARSLSFRKAEAQVQTMRERFEQAAEKYGATLEEETRLIY
EGFKIHPQHPLMNIFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETISIEQLV
KLAELVIALAE
>gnl|CDD|273852 TIGR01884, cas_HTH, CRISPR locus-related DNA-binding protein. Most but not all examples of this family are associated with CRISPR loci, a combination of DNA repeats and characteristic proteins encoded near the repeat cluster. The C-terminal region of this protein is homologous to DNA-binding helix-turn-helix domains with predicted transcriptional regulatory activity [Regulatory functions, DNA interactions, ]
SYIATVGFDEKFIIRALMEIGIKEEGDLVILVKSPIVDGARRAVESLRAIISDLYGNLVEGTIKEIELKD
VPLALRQISDIIKEEPEPGVIINLSGGMRILILILLLLAILVKTVVFRVYYESEELISFIDLDLVPLLAG
LSREELKILEVLKATGEKSVKNIAKKLGKSLSTISRHLAELEKKGLVEQKGRKGKRYSLTKLG
>gnl|CDD|273853 TIGR01885, Ornithine_aminotransferase, ornithine aminotransferase. This model describes the final step in the biosynthesis of ornithine from glutamate via the non-acetylated pathway. Ornithine amino transferase takes L-glutamate 5-semialdehyde and makes it into ornithine, which is used in the urea cycle, as well as in the biosynthesis of arginine. This model includes low-GC bacteria and eukaryotic species. The genes from two species are annotated as putative acetylornithine aminotransferases - one from Porphyromonas gingivalis (OMNI|PG1271), and the other from Staphylococcus aureus (OMNI|SA0170). After homology searching using BLAST it was determined that these two sequences were most closely related to ornithine aminotransferases. This model's seed includes one characterized hit, from Bacillus subtilis (SP|P38021)
SEEAIERENKYGAHNYHPLPVVFSKAEGVHVWDVEGKRYLDFLSAYSAVNQGHCHPKIVKALTEQAQKLT
LSSRAFYNDVFGEFAEYVTKLFGYDKVLPMNTGAEAVETAIKLARKWGYKVKGIPENQAIIVSAKGNFHG
RTLGAISMSTDPDSRTNFGPYVPGFKKIPYNNLEALEEALEDHGPNVCAFIVEPIQGEAGVVVPDDGYLK
KVRELCTKHNVLLIADEIQTGLGRTGKLLCVDHENVKPDIVLLGKALSGGVYPVSAVLADDDVMLTIKPG
EHGSTYGGNPLACAVAVAALEVLEEEKLAENAEKLGEIFRDQLKKLPKPIITEVRGRGLLNAIVIDESKT
GRTAWDLCLKLKEKGLLAKPTHGNIIRLAPPLVITEEQLDEGLEIIKKVID
>gnl|CDD|130941 TIGR01886, Beta-Ala-Xaa_dipeptidase, dipeptidase PepV. This model represents a small clade of dipeptidase enzymes which are members of the larger M25 subfamily of metalloproteases. Two characterized enzymes are included in the seed. One, from Lactococcus lactis has been shown to act on a wide range of dipeptides, but not larger peptides. The enzyme from Lactobacillus delbrueckii was originally characterized as a Xaa-His dipeptidase, specifically a carnosinase (beta-Ala-His) by complementation of an E. coli mutant. Further study, including the crystallization of the enzyme, has shown it to also be a non-specific dipeptidase. This group also includes enzymes from Streptococcus and Enterococcus [Protein fate, Degradation of proteins, peptides, and glycopeptides]
TIDFKEEVEARKDALLEDLEELLRIDSSEDLENATEEYPFGPGPVDALTKFLSFAERDGFTTKNFDNYAG
HVEYGAGDERLGIIGHMDVVPAGEGWTRDPFEPEIDEGRIYARGASDDKGPSLAAYYAMKILKELGLPPS
KKIRFVVGTNEETGWVDMDYYFKHEETPDFGFSPDAEFPIINGEKGNFTLELSFKGDNKGDYVLDSFKAG
LAENMVPQVARAVISGPDAEALKAAYESFLADKASLDGSFEINDESATIVLIGKGAHGAAPQVGINSATF
LALFLNQYAFAGGAKNFIHFLAEVEHEDFYGEKLGIAFHDELMGDLAMNAGMFDFDHANKESKLLLNFRY
PQGTSPETMQKQVLDKFGGIVDVTYNGHFEEPHYVPGSDPLVQTLLKVYEKHTGKKGHEVIIGGGTYGRL
LERGVAYGAMFEGGPDVMHQANEFMMLDDLILAAAIYAEAIYELAK
>gnl|CDD|273854 TIGR01887, Beta-Ala-Xaa_dipeptidase, dipeptidase, putative. This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific
KDEILEDLKELIAIDSVEDLEKAKEGAPFGEGPRKALDKFLEIAKRDGFTTENVDNYAGYIEYGQGEEVL
GILGHLDVVPAGDGWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDE
ESGWKCIDYYFEHEEMPDIGFTPDAEFPIIYGEKGITTLEIKFKDDTEGDVVLESFKAGEAYNMVPDHAT
AVISGKKLTEVEQLKFVFFIAKELEGDFEVNDGTLTITLEGKSAHGSAPEKGINAATYLALFLAQLNLAG
GAKAFLQFLAEYLHEDHYGEKLGIKFHDDVSGDLTMNVGVIDYENAEAGLIGLNVRYPVGNDPDTMLKNE
LAKESGVVEVTLNGYLKPLYVPKDDPLVQTLMKVYEKQTGDEGEPVAIGGGTYARLMPNGVAFGALFPGE
EDTMHQANEYIMIDDLLLATAIYAEAI
>gnl|CDD|273855 TIGR01888, Hypothetical_protein_SSO1730, CRISPR type III-B/RAMP module-associated protein Cmr3. CRISPR is a term for Clustered Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR associated) proteins. This highly divergent family is found in at least ten different archaeal and bacterial species as part of the CRISPR RAMP modulue but is not a member of the RAMP superfamily itself. A typical example is TM1793 from Thermotoga maritima
ILIKPLDPLFFRSSRPFDAGNESVVSSIFPSPTTIAGAVRTALLEKNAGKSSRLLDIEREAKPYFPIYGP
FVVEKGKPFFPLPSDIGNAEKYFGVVDKALIERLGKAPLPPGKGSDSETTPGYLSESKLSKYLAGRISEL
HTPLQEEEIFKKEERIGIALDRERKVVKEGALYSQRFLRFKDDVGFIVWVEDPEAAKDLLPKRIVGLGGE
RRLAKLEVDEDNEDTFNPEILPETKYVKFYLLTPAIFIEGGVLSDLKGLLCEAKLVEVFNFGKRKRTVSG
WDYVEKKPKPTLRAVPPGSVYFFKAKEEGPLELLIKLGKFHKIGYGLAIIGEW
>gnl|CDD|130944 TIGR01889, Pleiotropic_Regulator_Of_Virulence, staphylococcal accessory regulator family. This model represents a family of transcriptional regulatory proteins in Staphylococcus aureus and Staphylococcus epidermidis. Some members contain two tandem copies of this region. This family is related to the MarR transcriptional regulator family described by pfam01047 [Regulatory functions, DNA interactions]
KDLLSLYLYIKSLKRYLKKEFNLSLEELLILYYLGKLENNEGKLTLKEIIKEILIKQSALVKIIKKLSKK
GYLSKERSEDDERKVIISINKEQRSKIESLISEIEQIIK
>gnl|CDD|273856 TIGR01890, Amino-acid_acetyltransferase, amino-acid N-acetyltransferase. This model represents a clade of amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the "acetylated" ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate [Amino acid biosynthesis, Glutamate family]
FVAWFREAAPYINAHRGKTFVVGLGGELVEGGNLGNIVADIALLHSLGVRLVLVHGARPQIERILAARGR
TPHYHRGLRVTDEASLEQAQQAAGTLRLAIEARLSMSLSNTPMAGSRLPVVSGNFVTARPIGVIEGVDYE
HTGVIRKIDTEGIRRQLDAGSIVLLSPLGHSPTGETFNLDMEDVATSVAISLKADKLIYFTLSPGISDPD
GTLAAELSPQEVESLAERLGSETTRRLLSAAVKACRGGVHRSHIVSYAEDGSLLQELFTRDGIGTSISKE
AFESIRQATIDDIGGIAALIRPLEEQGILVRRSREYLEREISEFSIIEHDGNIIGCAALYPYAEEDCGEM
ACLAVSPEYQDGGRGERLLAHIEDRARQMGISRLFVLTTRTGHWFRERGFQTASVDELPEARRKLYNYQR
NSKILMKRL
>gnl|CDD|273857 TIGR01891, p-aminobenzoyl-glutamate_hydrolase_subunit, amidohydrolase. This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site [Protein fate, Degradation of proteins, peptides, and glycopeptides]
LTDIRRHLHEHPELSFEEFKTSSLIAEALESLGIEVRRGVGGATGVVATIGGGKPGPVVALRADMDALPI
QEQTDLPYKSTNPGVMHACGHDLHTAILLGTAKLLKKLADLLEGTVRLIFQPAEEGGGGATKMIEDGVLD
DVDAILGLHPDPSIPAGTVGLRPGTIMAAADKFEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQIVSR
NVDPSRPAVVSVGIIEAGGAPNVIPDKASMSGTVRSLDPEVRDQIIDRIERIVEGAAAMYGAKVELNYDR
GLPAVTNDPALTQILKEVARHVVGPENVAEDPEVTMGSEDFAYYSQKVPGAFFFLGIGNEGTGLSHPLHH
PRFDIDEEALALG
>gnl|CDD|130947 TIGR01892, Acetylornithine_deacetylase, acetylornithine deacetylase (ArgE). This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes [Amino acid biosynthesis, Glutamate family]
EILTKLVAFDSTSFRPNVDLIDWAQAYLEALGFSVEVQPFPDGAEKSNLVAVIGPSGAGGLALSGHTDVV
PYDDAAWTRDPFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKM
IEAGAGRPRHAIIGEPTRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLL
REDLDEGFTPPYTTLNIGVIQGGKAVNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRDEPGFEV
QIEVVSTDPGVNTEPDAELVAFLEELSGNAPEVVSYGTEAPQFQELGAEAVVCGPGDIRQAHQPDEYVEI
EDLVRCRAVLARLV
>gnl|CDD|273858 TIGR01893, Cytosol_non-specific_dipeptidase, Xaa-His dipeptidase. This model represents a clade of dipeptidase enzymes, many of which are specific for carnosine (beta-alanyl-histidine). This enzymes is found broadly in bacteria and at least one archaeon (Methanosarcina). In most species there is only one sequence hitting this model, while Bacteroides thetaiotaomicron, Chlorobium tepidum and Clostridium perfringens have two each and Fusobacterium nucleatum has three. These may indicate that there is a broader substrate range than just carnosine in these (and other) species. 8/19/03 GO terms added [SS]
LKPSRVFKYFEEISKIPRPSKNEKEVSNFIVNWAKKLGLEVKQDEVGNVLIRKPATPGYENHPPIVLQGH
MDMVCEKNEDSLHDFEKDPIELIIDGDWLKARGTTLGADNGIGVAMGLAILEDNNLKHPPLELLFTVDEE
TGMDGALGLDENWLSGKILINIDSEEEGEFIVGCAGGRNVDITFPVKYEKFTKNEEGYQISLKGLKGGHS
GADIHKGRANANKLMARVLNELKENLNFRLSDIKGGSKRNAIPREAKALIAIDENDVKLLENLVKNFQSK
FKSEYSELEPNITIEVSKRENSVKVFSENTTDKLINALNGLPNGVQSVSDEEPGLVESSLNLGVVKTKEN
KVIFTFLIRSSVESDKDYVTEKIESIAKLAGARVEVSAGYPSWQPDPQSNLLDTARKVYSEMFGEDPEVK
VIHAGLECGIISSKIPDIDMISIGPNIYDPHSPNERVSISSVEKVWDFLVKVLERLK
>gnl|CDD|273859 TIGR01894, hypothetical_protein, CRISPR type III-B/RAMP module RAMP protein Cmr1. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This model represents the region of stongest conservation, the N-terminal half, of one such family, represented by TM1795 from Thermotoga maritima. This protein is the first of a set of six genes, mostly from the RAMP superfamily, that we designated the CRISPR-associated RAMP module
LEAITPIFGGGARGRKEEEVRSTSIKGLLRWWFRALIGSYFGNNLQKLKEAERLAEEIFGSTNRKSRFRL
EVEDEGVSENLGNVYLSKNKVGKRGEEQEKVILRDYNNTLRILLEGNDKKIIALINNPLLDKLSNFGGIG
ARSRRGFGSIEIKS
>gnl|CDD|273860 TIGR01895, conserved_hypothetical_protein, CRISPR-associated protein Cas5, subtype I-B/TNEAP. CRISPR is a term for Clustered Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR associated) proteins. This family is represented by TM1800 from Thermotoga maritima. It is related to TIGR01868 (CRISPR-associated protein, CT1976 family)
MKILRIKIKSWTASFRYPFFIYGYQPTYPLPPYSTIIGLLSAAVGEGNKDERFNYMSVVGDFEGVIVDLE
TFRKLSKKRKAFETSPIKVENLYNPNLNLYLKAEEHFLHEFEENFRKPRYYPLLGRSEDLVKIDEVKIIE
CEKKDLYPHDKYYGIPINIFTADYFGSYGIRMVYALVSDYLISTIPRKFERVKPYYVMIEAVVGEGEILF
DPEGD
>gnl|CDD|273861 TIGR01896, cas_AF1879, CRISPR-associated protein Cas4/Csa1, subtype I-A/APERN. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This model describes a particularly strongly conserved family found so only in the APERN subtype of CRISPR/Cas loci and represented by AF1879 from Archaeoglobus fulgidus. This family has four perfectly preserved Cys residues. This subfamily is found in a CRISPR/Cas locus we designate APERN, so the family is designated Csa1, for CRISPR/Cas Subtype Protein 1
LRRLHRSGAPDEVSEELRGWHWNEPPVKPPRYLGLSLSDVAYGYCPTGRDVYLKRVLGIRGEVRGLLVLG
QAIHEAFLKALEEVRKLIYSGYDMFSVLLRSFRAREFCAEALWKYGVEIYSAVMAYVFEKASFFSADSLV
FLVIPVAVEYNVDGSPLGLSDRLRVDALVGILPVVVEMKVGSYQERHELALAGYALAIEADLEVPVDYGL
LVYVNVNDGVEIKARLVYISDDLRTEFLERRDEAIRIIEYGSDPGLPPKCPPTCPFLEHCH
>gnl|CDD|273862 TIGR01897, hypothetical_protein, CRISPR-associated protein, MJ1666 family. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This model describes a Cas protein about 400 residues in length, found mostly in the Archaea but also in Aquifex
KKILIAPWGNPKNWKKVKYSFNGKEVESNSSLKAIVELLKPDETIIIVPDSLATVYSSNKERILKDSVEE
KLKEFSKNALGIENSDVIVLPGIGSFKNITFEGKPLDYFSYAYYHLLKILEKDKINEVYLDITHGINYMP
VLTLEAIRALLVYLAKEKEVKLELYNSDPYPKGVSKELRIHTIEHVREIESIVIRPLPLLSFVERKLLNK
YRNNPKNIGRKLLENFNIFISDIINATPLVFATAFPNGRDVELYLNDSILEFLRRIKIGGEEDLKPLVKR
ELYLGRDFKNLLKLYFHSLILEVLKKKGNSPKNEVKLEEIKKLAETFFDEEGISVIIEIIKNELDNIKNR
RKKAEELALIKTTEIYKVSGEGFEKRNFLAHAGFEYNVVEVKKEKDKIYVRYGKKIEKIE
>gnl|CDD|213662 TIGR01898, repair_system, CRISPR type III-B/RAMP module RAMP protein Cmr6. CRISPR is a term for Clustered Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR associated) proteins. This family, represented by TM1791 of Thermotoga maritima, is designated Cmr6 [sic], for CRISPR/Cas Ramp Module protein 6. This family is both closely related to and frequently encoded next to the TM1792 family of Cas proteins described by TIGR01867. The two proteins are fused in an example from Methanopyrus kandleri
FKLKTSSRLLVGLGNPHIYETGLTLDPIYGLPYIPGSAIKGVLRSATFEVLADEDKLSKGKVREELADKL
FGTQEREGELIFLDAYPIPDEDKSIFELDIINPHYQPYYQGEKPPGDWVNPIPIKFLTVKKGVTFQFVLE
FDNLGELLDKLQKLLKKALKEFGIGAKTSLGYGRFE
>gnl|CDD|273863 TIGR01899, cas_TM1807_csm5, CRISPR type III-A/MTUBE-associated RAMP protein Csm5. CRISPR is a term for Clustered Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR associated) proteins. Members of this cas gene family are found in the mtube subtype of CRISPR/cas locus and designated Csm5, for CRISPR/cas Subtype Mtube, protein 5
VTLEVLTPLHIGNGEELTMLDYYVEGNDRIIVLDFEKLILDILEKKDEISELIVMNRDYAGSNAELKEVL
EEVKLDPAKYRDYSSKIISGEPRREKKLTIKEFHKINGDPYIPGSSIKGAIRTALLWNYLKKNPDLLEIV
DDHLQKELRQYGRAFERKELKKNGISNTIPKDPVNDVFRALKVSDSRPLRTDRLIVHRIKLNYNGRPGIP
LYAECLDPGTTFSFNVKIDREELKRGLDRKKQFYAPSEGENKLEILKIACNHFKEEFLEFVLAKSNKAYE
EFRKLEKKLNNDNGDLEILHIGWGGGLRSKTIGILLDDEDGKDAQFRKVRKALGLGKKPLTNKLSLRFPK
TKRVINGKPMGWCKL
>gnl|CDD|273864 TIGR01900, dapE-gram_pos, succinyl-diaminopimelate desuccinylase. This model represents a clade of succinyl-diaminopimelate desuccinylases from actinobacteria (high-GC gram positives), delta-proteobacteria and aquificales and is based on the characterization of the enzyme from Corynebacterium glutamicum. This enzyme is involved in the biosynthesis of lysine, and is related to the enzyme acetylornithine deacetylase and other amidases and peptidases found within pfam01546. Other sequences included in the seed of this model were assessed to confirm that 1) the related genes DapC (succinyl-diaminopimelate transaminase) and DapD (2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase) are also found in the genome, 2) each is found only once in those genomes, 3) the lysine biosynthesis pathway is complete and 4) the direct (TIGR03540 or TIGR03542) or acetylated (GenProp0787) aminotransferase pathways are absent in thes genomes. Additionally, a number of the seed members are observed adjacent to either DapC or DapD (often as a divergon with a putative promoter site between them [Amino acid biosynthesis, Aspartate family]
LTEDLAELTAALVDIPSVSGDERALADAVESALRALPHLEVIRHGNSVVARTNLGRPSRVILAGHLDTVP
IADNLPSRVEGGRLYGRGAVDMKGGLAVMLALAATLDRTEPRHDLTLVFYEREEGPAEENGLGRLLREHP
EWLAGDLAVLLEPTDGKIEAGCQGTLRATVTFHGRRAHSARSWMGENAIHKAAPILARLAAYEPREVTVD
GLTYREGLNAVRIEGGVAGNVIPDECEVNVNYRFAPDRSLEQARAHVRELFEGDGAEVEVTDLSPGARPG
LDNPLAAELVAAVGGEVRAKYGWTDVARFSALGIPAVNFGPGDPALAHQDDEHVPVAQLTACAAILRRWL
S
>gnl|CDD|273865 TIGR01901, Heme/hemopexin-binding_protein, filamentous hemagglutinin family N-terminal domain. This model represents a conserved domain found near the N-terminus of a number of large, repetitive bacterial proteins, including many proteins of over 2500 amino acids. Members generally have a signal sequence, then an intervening region, then the region described by this model. Following this region, proteins typically have regions rich in repeats but may show no homology between the repeats of one member and the repeats of another. A number of the members of this family have been designated adhesins, filamentous haemagglutinins, heme/hemopexin-binding protein, etc
FNNWQQFNVGQGGTVTFNQPPAASNILNRVTGGSASQIQGLLQVNGKANVFLINPNGIIFGGGAQINVGG
LVASTTAIS
>gnl|CDD|130957 TIGR01902, putative_N-acetyllysine_deacetylase, N-acetyl-ornithine/N-acetyl-lysine deacetylase. This clade of mainly archaeal and related bacterial species contains two characterized enzymes, an deacetylase with specificity for both N-acetyl-ornithine and N-acetyl-lysine from Thermus, which is found within a lysine biosynthesis operon, and a fusion protein with acetyl-glutamate kinase (an enzyme of ornithine biosynthesis) from Lactobacillus. It is possible that all of the sequences within this clade have dual specificity, or that a mix of specificities have evolved within this clade
ELLKDLLEIYSPSGKEANAAKFLEEISKDLGLKLIIDDAGNFILGKGDGHKKILLAGHVDTVPGYIPVKI
EGGLLYGRGAVDAKGPLIAMIFATWLLNEKGIKVIVSGLVDEESSSKGAREVIDKNYPFYVIVGEPSGAE
GITLGYKGSLQLKIMCEGTPFHSSSAGNAAELLIDYSKKIIEVYKQPENYDKPSIVPTIIRFGESYNDTP
AKLELHFDLRYPPNNKPEEAIKEITDKFPICLEIVDETPPYKVSRNNPLVRAFVRAIRKQGMKPRLKKKT
GTSDMNILAPIWTVPMVAYGPGDSTLDHTPQEKISLAEYLIGIKTLMLAIEELWQK
>gnl|CDD|273866 TIGR01903, Hypothetical_protein., CRISPR type III-A/MTUBE-associated RAMP protein Csm4. CRISPR is a term for Clustered Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR associated) proteins. Members of this cas gene family are found in the mtube subtype of CRISPR/cas locus and designated Csm4, for CRISPR/cas Subtype Mtube, protein 4
LVKLKFKSSFHYGEILHSDTIFSAIINAYIKLYGRDEVDKLIEKFKDDSPFRISSLLPYIKNTYLVPKPL
HNALSDLNLLEKIPKDLKKISYIPIDELESWLDGEADEKKQLNNITKIKTEGNKGKPKVLIEEPKVSIDR
IEIKSNLYFVEDIFFKENFGLWFLADYSDESFEKLLEAALKLLEDFGLGGKRTTGYGLFNVEIEDNELEP
ENGEYYLTLSLFIPDDDELESDTELARYRLVKRRGFNIDGTKPKRQIRYFAEGSIFYLKFQGKVKDVSLI
LNGQESVYPYGFPITLP
>gnl|CDD|273867 TIGR01904, GSu_C4xC__C2xCH, Geobacter sulfurreducens CxxxxCH...CXXCH domain. This domain occurs from three to eight times in eight different proteins of Geobacter sulfurreducens. The final CXXCH motif matches ProSite motif PS00190, the cytochrome c family heme-binding site signature, suggesting
NAATGTCSNVYCHSSGQKASGAYPTTPAWGGTAATTGCNGCH
>gnl|CDD|213663 TIGR01905, paired_CXXCH_1, doubled CXXCH domain. This model represents a domain of about 41 amino acids that contains, among other motifs, two copies of the motif CXXCH associated with heme binding. Almost every member of this family has at least three copies of this domain (at least six copies of CXXCH) is predicted to be a high molecular weight c-type cytochrome. Members are found mostly in species of Shewanella, Geobacter, and Vibrio
HGPVAGGDCTSCHDPHGSPEPKLLKEDGPDLCLGCHDDAAL
>gnl|CDD|273868 TIGR01906, Uncharacterized_protein_aq_2036, integral membrane protein TIGR01906. This model represents a family of highly hydrophobic, uncharacterized predicted integral membrane proteins found almost entirely in low-GC Gram-positive bacteria, although a member is also found in the early-branching bacterium Aquifex aeolicus
LKTILLFIVIIFFIVSLSIILTINFSPKFHALEIQSNNDIPKRVGLEKEEILKDYSLMIKYLNNPKKEVL
KLPNFPFSDSGVFHFKDVKNLFSLLYLVSLAILLSFLLWIALTFKLRSLSLLIKSFIFLLLLPLIIGILI
LLNFEKAFTLFHKIFFNNDTWLFDPAKDPIINILPEKFFLHAFILIFILIEILFIIGGILYKKKLKK
>gnl|CDD|273869 TIGR01907, CRISPR_system_Cascade_subunit_CasE, CRISPR-associated protein Cas6/Cse3/CasE, subtype I-E/ECOLI. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This model family, represented by CT1974 from Chlorobium tepidum, is found in the Ecoli subtype of CRISPR/Cas regions and is designated Cse3 (CRISPR/Cas Subtype Ecoli protein 3). The representative of this family from Thermus thermophilus HB8 (TTHB192) has been crystallized and found to have a structure consisting of two domains with opposing parallel beta-sheets known as a beta-sheet platform. This structure is similar to those found in the Sex-lethal protein and poly(A)-binding protein. This structure is consistent with an RNA-binding function
MYLSRITLARADLKALWSRDLYQLHQWLWHLFPNRPDEARQFLFRVEKRNAPGGCHFLLLSAQPPLQAVA
FVIETKQVEPQLQVGVPLYFRLRANPTITINGKRKRMDAKGQIKRCRVPLIQQQEAIAWLQRKGQLSGFA
LVDPVHVIAYRQQQFSKGDGKSITFSSVDFSGMLTITDAPLFIQLLQQGIGKSKAFGCGLLSIKPL
>gnl|CDD|162595 TIGR01908, Uncharacterized_protein_aq_372, CRISPR-associated protein Cas8b1/Cst1, subtype I-B/TNEAP. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This (revised) model describes a conserved region from an otherwise highly divergent protein found in the Tneap subtype of CRISPR/Cas regions. This Cys-rich region features two motifs of CXXC
EDKNSPLCINCGERHAKKDTIFDTEIPLIGGLSGGVPNYFWNGKPKAPLCEICEFIVLSYFRGLTLLLKH
GKPPFLFVNSDTSAISLVSLNLLLNSKLKYKLPENILFELFTEVVLKSEEEKARENLSNIIFLEIFTNNN
EGMPKIYSFNISRRVARFLKNAARKDNFSGWSKIVYKGKRHSDKIKPEFIEKVLSNSVYYKLLNGESILK
YFIKNAKRSKYYDWNLLPYYLTEVNLLPKKALQFIKEVGDSISETIKEALWEIYLQGKKLAKRLRELEAE
NKIKSFAYKLLNAERIRDRLGFMDSLLRL
>gnl|CDD|213664 TIGR01909, Uncharacterized_protein_AF_0456, C_GCAxxG_C_C family probable redox protein. This model represents a putative redox-active protein of about 140 residues, with four perfectly conserved Cys residues. It includes a CGAXXG motif. Most members are found within one or two loci of transporter or oxidoreductase genes. A member from Geobacter sulfurreducens, located in a molybdenum transporter operon, has a TAT (twin-arginine translocation) signal sequence for Sec-independent transport across the plasma membrane, a hallmark of bound prosthetic groups such as FeS clusters
RNCAEAIFAALREEFNLDIPEEAVNMASGFGGGVAGSGHICGALTGAVMALGLYFGTEGDGEQVNNTYAL
CAELYEKFREKNGSPNCGDLNPKKDLVSKEQRRKCIEIVSTAAETLLEIL
>gnl|CDD|273870 TIGR01910, succinyl-diaminopimelate_desuccinylase, acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase. This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research [Protein fate, Degradation of proteins, peptides, and glycopeptides]
VELLKDLISIPSVNPPGGNEETIANYIKDLLREFGFSTDVIEITDDRLKVLGKVVVKEPGNGNEKSLIFN
GHYDVVPAGDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEE
SGEAGTLYLLQRGYFKDADGVLIPEPSGGDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLI
TELNELEEHIYARNSYGFIPGPITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKA
LSKSDGWLYENEPVVKWSGPNETPPDSRLVKALEAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYG
PGDLETAHQVNEYISIKNLVESTKV
>gnl|CDD|188182 TIGR01911, conserved_protein, HesB-like selenoprotein. This model represents a family of small proteins related to HesB and its close homologs, which are likely to be invovlved in iron-sulfur cluster assembly (See TIGR00049 and pfam01521). Several members are selenoproteins, with a TGA codon and Sec residue that aligns to the conserved Cys of the HesB domain. A variable Cys/Ser/Gly-rich C-terminal region is not included in the seed alignment and model [Unknown function, General]
MKKVVMSDEAYEEFLDFLKKNNQDNNVVRIYFEGFGUGGPKFGIAIAEPNENDELIYINDFTFYIDPNLI
DQFLGFNITLREENFGKGLKLE
>gnl|CDD|162597 TIGR01912, sec-independent_protein_translocase_protein_TatC, Twin arginine targeting (Tat) protein translocase TatC, Archaeal clade. This model represents the TatC translocase component of the Sec-independent protein translocation system. This system is responsible for translocation of folded proteins, often with bound cofactors across the periplasmic membrane. A related model (TIGR00945) represents the bacterial clade of this family. TatC is often found (in bacteria) in a gene cluster with the two other components of the system, TatA/E (TIGR01411) and TatB (TIGR01410). A model also exists for the Twin-arginine signal sequence (TIGR01409)
RLLIALATFRLILLLVALAIVTGSVLGWLTIFTPFIIAALRESILPLLAYHVIATLIAPSPFAALELRIK
SAFFIGLLLASPVLAYEAYRFIKPALKPHERRQVRLLGVIAVGLFAFGALFAYWVIFPLIFQILFEFASP
LGLSAIMDIRKYTSFALKLILSFGLAFETPVVLVFLTRLGVVSASTLVDYWRVIILVVLVFGAVITPDPD
VVSMILLAIPLIALYGLALVISKRVEK
>gnl|CDD|273871 TIGR01913, Uncharacterized_protein_UU154, phage recombination protein Bet. This model represents the phage recombination protein Bet from a number of phage, including phage lambda. All members of this family are found in phage genomes or in putative prophage regions of bacterial genomes [Mobile and extrachromosomal element functions, Prophage functions]
LLNANTVGEDSADPQELIGTIIKTYLKPGDASDAQFIMFLIVCQAYGLNPFTKEVYIVPMKNNGGPDRTI
IVGIEGFRKRAERTEQYDGFIDVERNDESCEIEGYVKIRNDPLCGGWAEVMGKDRRERFSVPFKAYDSGK
PKSTWQSMPKTMLRKCAEAQALREAFPEGFGGIYTEEEMG
>gnl|CDD|273872 TIGR01914, CRISPR-associated_protein_Cas8a2/Csa4, CRISPR-associated protein Cas8a2/Csa4, subtype I-A/APERN. CRISPR loci appear to be mobile elements with a wide host range. This model represents a protein that tends to be found near CRISPR repeats. The species range for this species, so far, is exclusively archaeal. It is found so far in only four different species, and includes two tandem genes in Pyrococcus furiosus DSM 3638. This subfamily is found in a CRISPR/Cas locus we designate APERN, so the family is designated Csa4, for CRISPR/Cas Subtype Protein 4
VCEFYTPGHNLILDTLIMYGIVESLARSGVVEGEVEPVGERYVIKVDADNCHLVSQELALRGLQEALEEV
LSGHEATGRARSSKEGNKILSNTRISAGANINNVNADILPKTLEKIHKNLEGKRLSKKGLVTVPLTLMPL
YGKYMTKSLGVKGGKPIKVCPLCYALAWIGFHYYSPYIKYQKGDETKVVILQPAPAEEVDMIELLLLKDL
ASKIMPYILRDFHFKISNELALLYHLLYTESLGETELVTESHFEVLSYTLEVSGNNQRVRDFGELDLGVL
MDFIAYLKARDFYSWPKFVDFLARRDPEISLQLTDAILNGDEEAFYTALRELKKSGVRYDPEQVDALAEI
LAER
>gnl|CDD|273873 TIGR01915, F420-dependent_NADP_reductase, NADPH-dependent F420 reductase. This model represents a subset of a parent family described by pfam03807. Unlike the parent family, members of this family are found only in species with evidence of coenzyme F420. All members of this family are believed to act as NADPH-dependent F420 reductase [Energy metabolism, Electron transport]
MKIAVLGGTGDQGKGLALRLAKAGNKIIIGSRDLEKAEEAAAKALEELGHGGSDIKVTGADNAEAAKRAD
VVILAVPWDHVLKTLESLRDELSGKLVISPVVPLASDGGKGARYLPPEEGSAAEQAAALLPETSRVVAAF
HNLSAVLLQDVDDEVDCDVLVCGDDEEAKEVVAELAGRIDGLRALDAGPLENAAIVESLTPLLINLNRRN
KLRDAGIRF
>gnl|CDD|273874 TIGR01916, Coenzyme_F420:L-glutamate_ligase, coenzyme F420-0:L-glutamate ligase. This model represents an enzyme of coenzyme F(420) biosynthesis, as catalyzed by MJ0768 of Methanococcus jannaschii and by the N-terminal half of FbiB of Mycobacterium bovis strain BCG. Note that only two glutamates are ligated in M. jannaschii, but five to six in the Mycobacterium lineage. In M. jannaschii, CofE catalyzes the GTP-dependent addition of two L-glutamates [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
IEVIAVEGLPLIREGDDLAELIAEAAPLEDGDVLVVASTVVSKAEGRIIRLEEITPSPEALEIAARTGKD
PRFVQAILDEAVEVVAVGTPFLITETRHGHVCANAGIDESNVGNGELLLLPEDPDASAEKIRRGLRELTG
VDVGVIITDTNGRPFREGQVGVAIGAAGLKVLRDWRGEKDLYGRELEVTEVAVADELAAAANLVMGEADE
GTPVVVIRGLNVADEGGGGARQLYRPEEEDVFR
>gnl|CDD|130972 TIGR01917, subunit_of_Protein_B_sticklandii, glycine reductase, selenoprotein B. Glycine reductase is a complex with two selenoprotein subunits, A and B. This model represents the glycine reductase selenoprotein B. Closely related to it, but excluded from this model, are selenoprotein B subunits of betaine reductase and sarcosine reductase. All contain selenocysteine incorporated during translation at a specific UGA codon
KVVHYINQFFAGIGGEEKADIAPFIAEELPPISQNLDKLIEEDAEIVATVVCGDSFFGENLEEAKAKVLE
MIKGANPDIFIAGPAFNAGRYGMAAGAITKAVQDELGIKAFTAMYEENPGADMFKKEVYVIPTADSAAGM
RKALPALAKFALKLAKGEEIGSPAEDGYFARGIRVNAFKDDRGAKRAVAMLVKKLKGEEFETEYPMPVFD
NVAPGPAIKDISKAKIAIVTSGGIVPKGNPDHIESSSASKYGKYDIDGFDDLSEADHETAHGGHDPTYAN
EDADRVIPVDVLRDLEKEGKIGELFKYFYSTTGNGTAVANSKQFAKEFSKELLAAGVDAVILTSTUGTCT
RCGATMVKEIERAGIPVVHICTVTPIALTVGANRIIPAIAIPHPLGDPALDAAEEKALRRKIVEKALKAL
ETEIEDQTVFE
>gnl|CDD|130973 TIGR01918, subunit_of_Protein_B_sticklandii, selenoprotein B, glycine/betaine/sarcosine/D-proline reductase family. This model represents selenoprotein B of glycine reductase, sarcosine reductase, betaine reductase, D-proline reductase, and perhaps others. This model is built in fragment mode to assist in recognizing fragmentary translations. All members are expected to contain an internal TGA codon, encoding selenocysteine, which may be misinterpreted as a stop codon
KVVHYLNQFFAGIGGEEKADYEPEIAEGQPPISQMLNKLLEEDAEVVHTVVCGDSFFGENLEEAVARVLE
MLKDKEPDIFIAGPAFNAGRYGVACGEICKVVQDKLNVPAVTSMYVENPGVDMFKKDVYVMITGDSAAGM
RKDLPAMAKFANKIAKGEEIGSPDEEGYFPRGKRVNHFREDRGSERAVDMLVKKLKGEEFQTEYPMPVFD
RVEPAAAIKDLSKAKIAVVTSGGIVPKDNPDRIESSSASKYGMYDITGLDRLEGGVYETAHGGFDPAYAN
ADPDRVVPVDVLRDYEKEGKIGELHEYFYSTVGNGTTVAESKQFAKEFVVELKQGGVDAVILTSTUGTCT
RCGATMVKEIERAGIPVVHMCTVIPIALTVGANRIVPTIAIPHPLGDPALSKAEEKKLRRKRVEKALKAL
ETEVEEQTVFE
>gnl|CDD|273875 TIGR01919, hisA-trpF, 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase/N-(5'phosphoribosyl)anthranilate isomerase. This model represents a bifunctional protein posessing both hisA (1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase) and trpF (N-(5'phosphoribosyl)anthranilate isomerase) activities. Thus, it is involved in both the histidine and tryptophan biosynthetic pathways. Enzymes with this property have been described only in the Actinobacteria (High-GC gram-positive). The enzyme is closely related to the monofunctional HisA proteins (TIGR00007) and in Actinobacteria, the classical monofunctional TrpF is generally absent
MPLILLPAVDVNGGAAVRLQQGAGGSKTYYGSLESAARWWEQGGAEWIHLVDLDAAFGGGNNEEMLEEVV
GLLDVVEELSGGRRDDSSLRAALTGGCARVNGGTAALENPWWAARVIREGGDIVAVGLDVLEIGEWHTLG
NRGWSDGGGDLEVLERLLDSGGCSRVVVTDSKKDGLLGGPNLLLLAVVAARTDAIVAASGGSSLLDDLRA
IKYLDEGGVSVAIGGKLLYARFFTLEAALAVEK
>gnl|CDD|273876 TIGR01920, Shikimate_kinase, shikimate kinase. This model represents the shikimate kinase (SK) gene found in archaea which is only distantly related to homoserine kinase (thrB) and not atr all to the bacterial SK enzyme. The SK from M. janaschii has been overexpressed in E. coli and characterized. SK catalyzes the fifth step of the biosynthesis of chorismate from D-erythrose-4-phosphate and phosphoenolpyruvate [Amino acid biosynthesis, Aromatic amino acid family]
AYGGGTILNAIATGLGGAFGIDLWVEAKVREGDEAGVSTYVRGNPRLIERILTAIRSKFGIVDGLEVEVE
SEIPAGSGLKSSSALVNALVEAVLKAKGVEIDDIDILRLGARLSKKAGLSVTGAFDDAAASYLGGIVITD
NRRMKILKRDKLEGCTAAVLVPKEGERRENVDLNRFRRISPVVEEAFNLALRGEYLKAMVLNGVAYATAL
GYPLEPASKALEAGAAAAGLSGKGPSYFALTEDPEEAAEALMEFGGDVIET
>gnl|CDD|273877 TIGR01921, Meso-diaminopimelate_D-dehydrogenase, diaminopimelate dehydrogenase. This model represents the diaminopimelate dehydrogenase enzyme which provides an alternate (shortcut) route of lysine buiosynthesis in Corynebacterium, Bacterioides, Porphyromonas and scattered other species. The enzyme from Corynebacterium glutamicum has been crystallized and characterized
MSKIRAAIVGYGNLGRSVEKAIQQQPDMELVGVFSRRGAETLDTETPVYAVADDEKHLDDVDVLILCMGS
ATDIPEQAPYFAQFANTVDSFDNHRDIPRHRQVMDAAAKAAGNVSVISTGWDPGMFSINRVYGEAVLPKG
QTYTFWGPGLSQGHSDAVRRIDGVKKAVQYTLPSEDALEKARRGEAPELTGKQTHKRQCFVVLKDGADHE
RVENEIRTMPDYFVGYETEVNFIDEATFDSEHTGMPHGGHVIRTGDSGGTFNQTVEFNLKLDRNPDFTAS
VLVAFARAAHRLKQAGQPGAFTVLEVPPYLLSPGDLDDLIARLV
>gnl|CDD|273878 TIGR01922, IMP_cyclohydrolase, IMP cyclohydrolase. This model represents IMP cyclohydrolase, the final step in the biosynthesis of inosine monophosphate (IMP) in archaea. In bacteria this step is catalyzed by a bifunctional enzyme (purH)
MYIGRFLVVGKLEDGTPFAAYRVSSRSFPNRRIEVREGAVAVVPEDPSEITENPYVTYNCIRIVDETAVV
SNGSHTDPIADKLESGVPPRDALVSVLLAMDYEKDEYNTPRIAAILDGETAYLGIVAADEVYVRVVKPKD
GEGYLLSVYGEEADEPSAINFKADTAEEAACDILPAAFEHPVCAAIARHDGDGWSLATR
>gnl|CDD|162605 TIGR01923, 2-succinylbenzoate--CoA_ligase, O-succinylbenzoate-CoA ligase. This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDL
DVQLLLTDSLLEEKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASA
VGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQLLEMIANERVTHISLVPTQLNR
LLDEGGHNENLRKILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETCSQVTTATPEMLHARPDVGRPLAGR
EIKIKVDNKEGHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGG
ENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKL
DELPYNASGKILRNQL
>gnl|CDD|273879 TIGR01924, Serine-protein_kinase_RsbW, serine-protein kinase RsbW. This model describes the anti-sigma B factor also known as serine-protein kinase RsbW. Sigma B controls the general stress regulon in B subtilis and is activated by cell stresses such as stationary phase and heat shock. RsbW binds to sigma B and prevents formation of the transcription complex at the promoter. RsbV (anti-anti-sigma factor) binds to RsbW to inhibit association with sigma B, however RsbW can phosphorylate RsbV, causing disassociation of the RsbV/RsbW complex. Low ATP level or environmental stress causes the dephosphorylation of RsbV
MRVHQDTIEMTVPAKPEYVGLIRLTLSGIASRAGYTYDDIEDLKIAVSEACTNAVKHAYKEGENGEIGIS
FHIYEDRLEIIVSDQGDSFDMDTFKQSLGPYDGSEPIDDLREGGLGLFLIETLMDEVEVYEDSGVTVAMT
KYLNREQVDNNVDIKATET
>gnl|CDD|130980 TIGR01925, Anti-sigma_F_factor, anti-sigma F factor. This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates spore development in B subtilis. SpoIIAB binds to sigma F, preventing formation of the transcription complex at the promoter. SpoIIAA (anti-anti-sigma F factor) binds to SpoIIAB to inhibit association with sigma F, however SpoIIAB can phosphorylate SpoIIAA, causing disassociation of the SpoIIAA/B complex. The SpoIIE phosphatase dephosphorylates SpoIIAA [Regulatory functions, Protein interactions, Cellular processes, Sporulation and germination]
MKNKMHLEFLAKSENESFARVTVASFIAQLDPTMEELTDIKTAVSEAVTNAIIHGYEENCEGVVYISATI
EDHEVYITVRDEGIGIENLEEAREPLYTSKPELERSGMGFTVMENFMDDVSVDSEKEKGTKIIMKKK
>gnl|CDD|130981 TIGR01926, peroxid_rel, uncharacterized peroxidase-related enzyme. This protein family with length of about 200 amino acids. One member, from Myxococcus xanthus, is a selenoprotein, with an otherwise conserved Cys replaced by Sec. This family is drawn narrowly enough to suggest that These proteins contain a domain described by TIGR00778, with a CxxCxxxHxxxxxxxG motif. Some members of that family are known to act as peroxidases or correlate with resistance to oxidative stress
SRLDVVDLAELTEEQKAYLAKIEEKTGFVPNVFRALAHDPEALRARTAYFNDLMLGEGGLSRAERELIAV
VVSRANGCVYCAAVHGAALRQLSGDPDLADAVAVNFRDADLSPRERAMLDFAVKLTATPAKVNEADFAAL
RAAGFSDLDILDLIHSVAFFNWANRLMLALGEPPNPE
>gnl|CDD|273880 TIGR01927, o-succinylbenzoate_synthase, o-succinylbenzoate synthase. This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are gamma proteobacteria and archaea. Many of the com-names of the proteins identified by the model are identified as O-succinylbenzoyl-CoA synthase in error [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
YRYQMPFDAPVVTRHGLLARREGLIVRLTDEGRTGWGEIAPLPGFGTETLAEALDFCRALIEEITRGDIE
AIDDQLPSVAFGFESALIELESGDELPPASNYYVALLPAGDPALLLLRSAKAEGFRTFKWKVGVGELARE
GMLVNLLLEALPDKAELRLDANGGLSPDEAQQFLKALDPNLRGRIAFLEEPLPDADEMSAFSEATGTAIA
LDESLWELPQLADEYGPGWRGALVIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAA
KLSPDPAAVGFTTALLRAQDLEAWPFS
>gnl|CDD|213667 TIGR01928, o-succinylbenzoate_synthase, o-succinylbenzoate synthase. This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are low GC gram positive bacteria and archaea. Also included in the seed and in the model are enzymes with the com-name of N-acylamino acid racemase (or the more general term, racemase / racemase family), which refers to the enzyme's industrial application as racemases, and not to its biological function as o-succinylbenzoic acid synthetase [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
YHVSEPFKSPFKTSKGTLNHRDCLIIELIDDKGNAGFGEVVAFQTPWYTHETIATVKHIIEDFFEPNINK
EFEHPSEALELVRSLKGTPMAKAGLEMALWDMYHKLPSFSLAYGQGKLRDKAPAGAVSGLANDEQMLKQI
ESLKATGYKRIKLKITPQIMHQLVKLRRLRFPQIPLVIDANESYDLQDFPRLKELDRYQLLYIEEPFKID
DISMLDELAKGTITPICLDESITSLDDARNLIELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIG
GMLETGISRAFNVALASLGGNDYPGDVSPSGYYFDQDIVAPSIR
>gnl|CDD|200143 TIGR01929, 14-Dihydroxy-2-naphthoyl-CoA_synthase, naphthoate synthase (dihydroxynaphthoic acid synthetase). This model represents an enzyme, naphthoate synthase (dihydroxynaphthoic acid synthetase), which is involved in the fifth step of the menaquinone biosynthesis pathway. Together with o-succinylbenzoate-CoA ligase (menE: TIGR01923), this enzyme takes 2-succinylbenzoate and converts it into 1,4-di-hydroxy-2-naphthoate. Included above the trusted cutoff are two enzymes from Arabadopsis thaliana and one from Staphylococcus aureus which are identified as putative enoyl-CoA hydratase/isomerases. These enzymes group with the naphthoate synthases when building a tree and when doing BLAST searches [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
FEDIRYEKSTDGIAKITINRPQVRNAFRPLTVKEIIQALDDAREDPDIGVVILTGAGDKAFCSGGDQKVR
GDYGYIDDSGVHRLNVLDVQRQIRTCPKPVIAMVNGYAIGGGHVLHMMCDLTIAAENARFGQTGPKVGSF
DGGYGSSYMARIVGQKKAREIWFLCRQYDAKQALDMGLVNTVVPLADLEKETVRWCREILQKSPMAIRML
KAALNADCDGQAGLQELAGNATMLFYMTEEGQEGRNAFLEKRQPDFSKF
>gnl|CDD|273881 TIGR01930, 3-ketoacyl-CoA_thiolase, acetyl-CoA acetyltransferases. This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation [Fatty acid and phospholipid metabolism, Other]
IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGL
PESVPAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVKPGNAELEDARL
KDLTDANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSS
DEGIRPNTTLEKLAKLKPAFDPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDP
EIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGA
RIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE
>gnl|CDD|273882 TIGR01931, Sulfite_reductase_flavoprotein_alpha-component, sulfite reductase [NADPH] flavoprotein, alpha-component. This model describes an NADPH-dependent sulfite reductase flavoprotein subunit. Most members of this family are found in Cys biosynthesis gene clusters. The closest homologs below the trusted cutoff are designated as subunits nitrate reductase
SPNSPLNQEQLDLLNRLLPTLTEAQLAWLSGYLWALANQTPAALSVAPNEAEEPAAQEKRVTILYGSQTG
NARRLAKRLAEKLEAAGFSVRLSSADDYKFKQLKKERLLLLVISTQGEGEPPEEAISLHKFLHSKKAPKL
ENLRYSVLGLGDSSYEFFCQTGKDFDKRLEELGGKRLLPRVDADLDYDANAAEWRAGVLTALNEQAKGGA
STPSASETSTPLQTSTSVYSKQNPFRAEVLENQKITGRNSKKDVRHIEIDLEGSGLHYEPGDALGVWYKN
DPALVKEILKLLNLDPDEKVTIGGKTIPLFEALITHFELTQNTKPLLKAYAELTGNKELKALIADNEKLK
AYIQNTPLIDLIRDYPADLDAEQLISLLRPLTPRLYSISSSQSEVGDEVHLTVGVVRYQAHGRARLGGAS
GFLAERLKEGDTVPVYIEPNDNFRLPEDPDTPIIMIGPGTGVAPFRAFMQERAEDGAKGKNWLFFGNPHF
TTDFLYQVEWQNYLKKGVLTKMDLAFSRDQAEKIYVQHRIREQGAELWQWLQEGAHIYVCGDAKKMAKDV
HQALLDIIAKEGHLDAEEAEEYLTDLRVEKRYQRDVY
>gnl|CDD|273883 TIGR01932, Protein_HflC, HflC protein. HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]
MRKIGIVVIVLLIVVLFQPFFIIKEGERGIITRFGKILKDNNHHVLVYEPGLHFKIPFIEHVKIFDAKIQ
TMDGRPDRIPTKEKKDIIIDTYIRWRIEDFKKYYLSTGGGTISAAEVLIKRKIDDRLRSEIGVLGLKEIV
RSSNDQLDTLVSKLALNRGGKINKIAMTITKGREILAREISQIANSQLKDIGIEVVDVRIKKINYSDELS
ESIYNRMRSEREQIARMHRSQGEEKAEEILGKAEYEVRKILSEAYRTARIIKGEGDAEAAKIYSDAYGKD
PEFYSFWRSLEAYEKSFKDNQDEKVLSTDSEFFQYMY
>gnl|CDD|130988 TIGR01933, Protein_HflK, HflK protein. HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]
IYTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYR
ITDPYKYLFSVENPEDSLRQATDSALRGVIGDSTMDDILTEGRSQIREDTKERLNEIIDNYDLGITVTDV
NFQSARPPEEVKEAFDDVIIAREDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRINRAKGDVA
RFTKLLAEYKKAPDVTRERLYLETMEKVLSNTRKVLLDDKKGNNLLYLPLD
>gnl|CDD|273884 TIGR01934, methylase_mitochondrial, ubiquinone/menaquinone biosynthesis methyltransferases. This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGV
DFSSEMLEVAKKKSELPLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLV
ILEFSKPANALLKKFYKFYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRS
LTFGVAAIHVGKK
>gnl|CDD|130990 TIGR01935, Regulator_of_ribonuclease_activity_A., RraA famliy. The E. coli member of this family has been characterized as a regulator of RNase E and its crystal structure has been analyzed. This model was initially classified as a "hypothetical equivalog" expressing the tentative hypothesis that all members might have the same function as the E. coli enzyme. Considering the second clade of enterobacterial sequences within this family, that appears to be less tenable. The function of these sequences outside of the narrow RraA equivalog model (TIGR02998) remains obscure. All of these were initially annotated as MenG, AKA S-adenosylmethionine: 2-demethylmenaquinone methyltransferase (EC 2.1.-.-). See the references characterizing this as a case of transitive annotation error in the case of the E. coli protein [Unknown function, General]
TPDLCDAYPDKVRVLEPMFRNFGGRAAFAGPIVTVKCFEDNSLVREVLEQPGAGRVLVVDGGGSLRCALL
GDNLAVLAEENGWEGVIVNGCVRDVAELAGMDLGVKALAAHPRKTEKRGAGEVDVPVTFAGVTFVPGDYL
YADEDGILVS
>gnl|CDD|273885 TIGR01936, Na+-translocating_NADH-quinone_reductase_subunit_A, NADH:ubiquinone oxidoreductase, Na(+)-translocating, A subunit. This model represents the NqrA subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump [Transport and binding proteins, Cations and iron carrying compounds]
ITIKKGLDLPLKGKPPEQGIAEKADPPTVAVDGRDFVGMRPKMKVRPGDKVKAGQPLFEDKKNPGVKFTS
PVSGEVVAINRGAKRVLLSVVIKKDGDGEFATFPTYDLQTLSAEQIKENLLESGLWTAIKQRPFDIVATP
DSSPRDIFITAADTRPLAPDPEVVLAEFSSAFVVGLDALAKLFTGKVHVCKKDRLSLPTQLLSNAEIHTF
SGPHPAGLPGTHIHFIAPIGNGKVVWTLNYQDVIAIGHLFLTGELLTERVIALAGPAVKKPRYVRTTKGA
NLSQLFPGELTSEGENRLISGSVLTGRKAKKEEAYLGRRDLQISVLPEGDVRELFGWLRPGLNKYSVTRT
YLSGLFKKRKEYNMDTNTNGGERAMIPIGIYERVMPLDIPPTLLLKALIAGDFDKAQRLGALEVDEEDFA
LCTFVDPSKYEYGSIVRESLDRIEKEG
>gnl|CDD|130992 TIGR01937, Na+-translocating_NADH-quinone_reductase_subunit_B, NADH:ubiquinone oxidoreductase, Na(+)-translocating, B subunit. This model represents the NqrB subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump [Transport and binding proteins, Cations and iron carrying compounds]
LKNFLNKLEPHFEKGGKYQKLTPVFDAVDTFLYEPGRTTSKPPHVRDAVDSKRWMILVVIALFPAMFFGM
YNVGLQAIVALSQPPQLMEAFWHISLFGSLGSFVSKEIGIGSKLLLGAKIFLPLLLVSYAVGGTWEVLFA
VVRKHEINEGFLVTGILFPLIVPPTIPLWMAALGIAFGVVVAKEVFGGTGRNILNPALVGRAFLFFAYPA
QMSGDQVWVGSNPMNSLGAGTAADGFSGATCLSQLASGGPSVKLQHNVTGPPASWMDAFLGNIPGSIGET
STLAILIGAALLILTGIASWRIMAGVMIGMIAMSWLFNAIGSWANAMFFIPWYWHLVLGGFAFGLVFMAT
DPVSSSFTKKGKWIYGAFIGFMAVLIRVVNPAYPEGMMLAILLANVFAPLIDYFVVQANIKRR
>gnl|CDD|273886 TIGR01938, Na+-translocating_NADH-quinone_reductase_subunit_C, NADH:ubiquinone oxidoreductase, Na(+)-translocating, C subunit. This model represents the NqrC subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump [Transport and binding proteins, Cations and iron carrying compounds]
KDSTSYTILVILVLSLVCSVLLAGVAVSLKPTQEENALLDKQKQILAAAGLLDPIVAKGKEVLALYAERI
ERRLLDLQTGTFTKAFEEENLDQREAFKDPQESIALLAFEDIAKIRRRANYTSVYLVKKDGGGITKVILP
IYGFGLWGPIYGFVALEEDGNTVLGITYYQQGETPGLGAEIENPEWQAQFVGKKLFDEQGQALALEVVKG
NGASAKAEHSVDGISGATLTSNGVQESFKFWLGPYGPFLAK
>gnl|CDD|130994 TIGR01939, Na+-translocating_NADH-quinone_reductase_subunit_D, NADH:ubiquinone oxidoreductase, Na(+)-translocating, D subunit. This model represents the NqrD subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump [Transport and binding proteins, Cations and iron carrying compounds]
TSNKSYKEYLLDPLWSNNPILLQILGICSALAVTTKLQTAIVMAIAVTFVTGFSNFFVSLLRNTIPNSIR
MIVQLVIIASLVIVVDQVLKAFAYDISKQLSVFVGLIITNCIVMGRAEAFAMANPPIPSFLDGIGNGLGY
GWVLVIIGFFRELFGSGTLLGIRVIPKLYYSGGWYQNNGLMLLAPSAFFLIGIVIWVVRIRKKDQQE
>gnl|CDD|130995 TIGR01940, Na+-translocating_NADH-quinone_reductase_subunit_E, NADH:ubiquinone oxidoreductase, Na(+)-translocating, E subunit. This model represents the NqrE subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump [Transport and binding proteins, Cations and iron carrying compounds]
EHYLSLFVKAVFVENMALSFFLGMCTFLAVSKKVSTAFGLGVAVTFVLTITVPINNLIYTYILKDGALSW
GGPAEVDLSFLELITFIGVIAALVQILEMVLERFSPSLYNALGIFLPLITVNCAIFGGVLFMVQREYNFG
ESVVYGFGSGLGWMLAIVALAGIREKLKYSDVPKGLQGLGITFITTGLMALAFMSFSGIQ
>gnl|CDD|130996 TIGR01941, Na+-translocating_NADH-quinone_reductase_subunit_F, NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit. This model represents the NqrF subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump [Transport and binding proteins, Cations and iron carrying compounds]
IILGIVMFTAIVLILVVVILFAKSKLVSSGDITIGINDDEEKSITVPAGGKLLNTLASNGIFISSACGGG
GTCGQCRVRVVEGGGEILPTELSHFSKREAKEGWRLSCQVKVKQDMSIEIPEEIFGVKKWECEVISNDNV
ATFIKELVLKLPDGESVPFKAGGYIQIEAPPHVVKYADFDIPPEYRGDWEKFNLFDLVSKVDEETVRAYS
MANYPAEKGIIKLNVRIATPPFINSDIPPGIMSSYIFSLKPGDKVTISGPFGEFFAKDTDAEMVFIGGGA
GMAPMRSHIFDQLKRLKSKRKISFWYGARSLREMFYQEDFDQLEAENPNFVWHVALSDPQPEDNWTGYTG
FIHNVLYENYLKDHDAPEDCEFYMCGPPMMNAAVIKMLEDLGVERENILLDDFGG
>gnl|CDD|130997 TIGR01942, pcnB, poly(A) polymerase. This model describes the pcnB family of poly(A) polymerases (also known as plasmid copy number protein). These enzymes sequentially add adenosine nucleotides to the 3' end of RNAs, targeting them for degradation by the cell. This was originally described for anti-sense RNAs, but was later demonstrated for mRNAs as well. Members of this family are as yet limited to the gamma- and beta-proteobacteria, with putative members in the Chlamydiacae and spirochetes. This family has homology to tRNA nucleotidyltransferase (cca)
VIPESEHNIPRQSFSAHALNVVERLKGAGYQAYIVGGAVRDLLLGIEPKDFDVVTSATPEEVRKLFRNSR
IVGRRFRLVHVSFGRQIIEVATFRSGHKSSVNAEGRILKDNVYGTLEEDAWRRDFTVNALYYDPSREVII
DYVGGMEDLKNRRLRLIGDPRSRYQEDPVRMLRALRFSVKLEFTIDESTARPIRESAPLLKGIPPARLFE
EILKLLFSGRSAALFRMLCGYQLLEPLFPSVAYALRESPKFESAFTVQALVNDTDFRVKRDKPVTPAFLY
AALLWPGLVFRVADAPDQGVMPYPAVFDAIRDFVEEQCAPISIPKRFSIPTREIWQMQLRLERRSGMRAR
KLLGHARFRAAYDLLLLREVCGRENAVLGEWWTPYQLASEEERTEMTRSAARHEGNRGRA
>gnl|CDD|130998 TIGR01943, Electron_transport_complex_protein_rnfA., electron transport complex, RnfABCDGE type, A subunit. The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the A subunit [Energy metabolism, Electron transport]
MSFFLIFLSAVFVNNFVLVKFLGLCPFLGVSKKLETAIGMGLAVTFVMTLASVISWLVYNFILDPLNLEF
LRTIVFILVIAALVQFVEMVVRKTSPDLYRALGIFLPLITTNCAVLGVALLNIQLDYNLLQSIVYAVGAG
LGFTLAMVIFAGIRERLDLSDVPKAFRGSPIALITAGLMSLAFMGFQGLV
>gnl|CDD|273887 TIGR01944, Electron_transport_complex_subunit_B, electron transport complex, RnfABCDGE type, B subunit. The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit [Energy metabolism, Electron transport]
MIIAAVAALSALGLALGAILGYAARRFPVEADPIVEEIDALLPQTQCGQCGYPGCRPYAEAIAEGEAINK
CPPGGEAVILALAELLGVEPIPQPLDADAGTIQPPMVALIDEDNCIGCTKCIQACPVDAIVGAAKAMHTV
IADECTGCDLCVEPCPTDCIEMIPV
>gnl|CDD|273888 TIGR01945, Electron_transport_complex_subunit_C, electron transport complex, RnfABCDGE type, C subunit. The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the C subunit [Energy metabolism, Electron transport]
LFTFKGGIHPPENKELSNDKPIEQLPLPQELIVPLSQHIGAPAEPIVKVGDKVLKGQKIAKADGFVSAPI
HAPTSGTVVAIEERVSPHASGLPVPAIVIEPDGEDEWIELEPIPDFENLSPEEILEKIRAAGIVGLGGAT
FPTHVKLNPPPEKKIETLIINGAECEPYLTCDDRLMRERAEEIIGGIRILLKILGVKKVVIGIEDNKPEA
IAALKKALGGYNIKVRVLPTKYPQGGEKQLIYALTGREVPSGGLPADIGVVVQNVGTAFAIYEAVVNGKP
LIERVVTVTGDAIRRPKNLWVLIGTPVSDILAFCGGFREKPERLIMGGPMMGLALPSLDVPVTKGTSGIL
ALDKEETPESPEKPCIRCGKCVQVCPMNLLPQQLNWLALADEFDEAEEHNLMDCIECGCCSYVCPSNIPL
VQYIRQAKAKLRAKK
>gnl|CDD|131001 TIGR01946, Electron_transport_complex_subunit_D, electron transport complex, RnfABCDGE type, D subunit. The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the A subunit [Energy metabolism, Electron transport]
SPHIRSGDSTRKIMRDVLIALLPGLAAQVYFFGWGTLIQIALAILTALILEAAILKLRKRSIKAFLKDGS
AILTGLLLAVAIPPLAPWWMIVIGTIFAIVLGKHLYGGLGQNIFNPAMVGYVFLLISFPVQMTTWPPPGK
LLSFVDSFSLIFSGNTSGIDGITTATPLDLFKTGLSLGTDLLPPKLPIFLGKSAGCGWEWSNLAFLLGGI
YLLYRKIITWHIPVSMLATLFVLSTITYLFSPFTHASPLFHLFSGGTMLGAFFIATDPVTAPTTNKGRII
FGAGIGVLVYLIRTFGGYPDGVAFAILLMNLCVPLIDYYTRPRTYGH
>gnl|CDD|273889 TIGR01947, Electron_transport_complex_subunit_G, electron transport complex, RnfABCDGE type, G subunit. The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the A subunit [Energy metabolism, Electron transport]
GLLLGLFAAVSAGLLALVNQFTKEQIAEAEAKQQLEALKQVLPQGLYDNDLLESTVPEVDEDLLGLGTIL
PVYGAKKGGQVVAYVLEVSAPGYSGPIQLLVGIDKDGTILGVRVLSHKETPGLGDKIELRISDWIEGFAG
KSLADPDDDHWAVKKDGGQFDQFTGATITPRAVVNAVKRALRYFKE
>gnl|CDD|162619 TIGR01948, Electron_transport_complex_subunit_E, electron transport complex, RnfABCDGE type, E subunit. The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the E subunit [Energy metabolism, Electron transport]
REEFKNGIWNNNPTLVQLLGLCPTLAVTTSAINGLGMGLATTFVLVGSNMVVSLVRKFIPKEVRIPVFIV
IIASFVTCVDMLMNAYTYDLYKSLGIFIPLIVVNCIILGRAEAFASKNGVLPSILDGLGMGLGFTLVLFV
LGGIREILGNGTLLDFGMFVITVFGKFSPALLAILPPGAFITLGFLIALKNYIDEK
>gnl|CDD|273890 TIGR01949, AroFGH_arch, predicted phospho-2-dehydro-3-deoxyheptonate aldolase. This model represents a clade of sequences related to fructose-bisphosphate aldolase (class I, included within pfam01791). The members of this clade appear to be phospho-2-dehydro-3-deoxyheptonate aldolases. This enzyme is the first step of the chorismate biosynthesis pathway. Evidence for this assignment is based on gene clustering and phylogenetic profiling. A group of species lack members of the three other types of phospho-2-dehydro-3-deoxyheptonate aldolase (represented by TIGR00034, TIGR01358 and TIGR01361), and also aparrently lack the well-known forms of step 2 (3-dehydroquinate synthase), but contain all other steps of the pathway: Desulfovibrio, Aquifex, Archaeoglobus, Halobacterium, Methanopyrus, Methanococcus and Methanobacterium. The clade of sequences represented here is limited strictly to this group of organisms. In Desulfovibrio, Aquifex, Archaeoglobus, Halobacterium and Methanosarcina the genes found by this model are clustered with other genes from the chorismate, phenylalanine, tyrosine and tryptophan biosynthesis pathways. In addition, these genes in Desulfovibrio, Archaeoglobus, Halobacterium, Methanosarcina and Methanopyrus are adjacent to a gene which hits pfam01959 which also has the property of having members only in those species which lack steps 1 and 2. Together these two genes appear to perform the synthesis of 3-dehydroquinate. It is presumed that the substrates and the chemical transformations involved are identical, but this has not yet been proven experimentally
LGKLVRLERIFNRESGRTVIVPMDHGVSNGPIKGLVDIRKTVNEVAEGGADAVLLHKGIVRRGHRGYGKD
VGLIIHLSASTSLSPDPNDKRIVTTVEDAIRMGADAVSIHVNVGSDTEWEQIRDLGMIAEICDDWGVPLL
AMMYPRGPHIDDRDPELVAHAARLGAELGADIVKTPYTGDIDSFRDVVKGCPAPVVVAGGPKTNSDREFL
QMIKDAMEAGAAGVAVGRNIFQHDDPVGITKAVCKIVHENADVEEALA
>gnl|CDD|131005 TIGR01950, HTH-type_transcriptional_activator_SoxR_homolog, redox-sensitive transcriptional activator SoxR. SoxR is a MerR-family homodimeric transcription factor with a 2Fe-2S cluster in each monomer. The motif CIGCGCxxxxxC is conserved. Oxidation of the iron-sulfur cluster activates SoxR. The physiological role in E. coli is response to oxidative stress. It is activated by superoxide, singlet oxygen, nitric oxide (NO), and hydrogen peroxide. In E. coli, SoxR increases expression of transcription factor SoxS; different downstream targets may exist in other species [Cellular processes, Detoxification, Regulatory functions, DNA interactions]
ELTVGELAKRSGVAVSALHFYESKGLITSIRNSGNQRRYKRDVLRRVAVIKAAQRVGIPLATIGEALAVL
PEGRTPTADDWARLSSQWREELDERIDQLNALRDQLDGCIGCGCLSLEDCPLRNPGDRLGEEGAGARLLE
DE
>gnl|CDD|273891 TIGR01951, nusB, transcription antitermination factor NusB. A transcription antitermination complex active in many bacteria was designated N-utilization substance (Nus) in E. coli because of its interaction with phage lambda protein N. This model represents NusB. Other components are NusA and NusG. NusE is, in fact, ribosomal protein S10 [Transcription, Transcription factors]
RRKARELALQALYQWELSGEDVDEIIEEFLEERELDEEDREYFRELVRGVLENQEEIDELISPHLEDWTL
ERLDPVDRAILRLAIYELLYRPDVPYKVVINEAVELAKKFGDEDSHKFVNGVLDKIAKE
>gnl|CDD|273892 TIGR01952, Probable_transcription_termination_protein_NusA, NusA family KH domain protein, archaeal. This model represents a family of archaeal proteins found in a single copy per genome. It contains two KH domains (pfam00013) and is most closely related to the central region bacterial NusA, a transcription termination factor named for its iteraction with phage lambda protein N in E. coli. The proteins required for antitermination by N include NusA, NusB, nusE (ribosomal protein S10), and nusG. This system, on the whole, appears not to be present in the Archaea
MRIKLSTEAIKYIALFEDMTGATVVDCLIDDRNRVVFVVKEGEMGAAIGKGGENVKRLEELIGKSIELIE
YSENLEEFVANKLAPAEVKNVTVSEFNGKKVAYVEVHPRDKGIAIGKGGKNIERAKELAKRHHDIDDVVV
V
>gnl|CDD|273893 TIGR01953, Transcription_elongation_protein_nusA., transcription termination factor NusA. This model describes NusA, or N utilization substance protein A, a bacterial transcription termination factor. It binds to RNA polymerase alpha subunit and promotes termination at certain RNA hairpin structures. It is named for the interaction in E. coli of phage lambda antitermination protein N with the N-utilization substance, consisting of NusA, NusB, NusE (ribosomal protein S10), and nusG. This model represents a region of NusA shared in all bacterial forms, and including an S1 (pfam00575) and a KH (pfam00013) RNA binding domains. Proteobacterial forms have an additional C-terminal region, not included in this model, with two repeats of 50-residue domain rich in acidic amino acids [Transcription, Transcription factors]
EFLAAIEALAKEKGISIETVIEAIEEALEQAYKKTFGQDENVEVNIDRKTGDINVYRRKEVVEEVEDPSL
EISLEDAREIDPDVQIGDEVKKEIPPENFGRIAAQTAKQVILQKIREAERERVYDEFSSKEGEIISGTVK
RVNRRGNLFVELGKTEGILPKKEQIPGEKFRIGDRIKAYVYEVRKTAKGPQIILSRTHPEFVKELLKLEV
PEIADGIIEIKKIAREPGYRTKIAVESNDENIDPVGACVGPKGSRIQAISKELNGEKIDIIEYSDDPAEF
IANALSPAKVISVEVLDEDKRSAEVVVPDDQLSLAIGKGGQNVRLASKLTGWNIDVKTESQ
>gnl|CDD|273894 TIGR01954, nusA_Cterm_rpt, transcription termination factor NusA, C-terminal duplication. NusA is a bacterial transcription termination factor. It is named for its interaction with phage lambda protein N, as part of the N utilization substance. Some members of the NusA family have a long C-terminal extension. This model represents an acidic 50-residue region found in two copies toward the C-terminus of most Proteobacterial NusA proteins, spaced about 26 residues apart. Analogous C-terminal extensions in some other bacterial lineages lack apparent homology but appear similarly acidic [Transcription, Transcription factors]
INEEIAQLLVEEGFTTVEDLAYVPIDELLSIEGFDEETAKELINRARNAL
>gnl|CDD|131010 TIGR01955, Transcriptional_activator_rfaH., transcription elongation factor/antiterminator RfaH. This model represents the transcription elongation factor/antiterminator, RfaH. This protein is most closely related to the transcriptional termination/antitermination protein NusG (TIGR00922) and contains the KOW motif (pfam00467). This protein appears to be limited to the gamma proteobacteria. In E. coli, this gene appears to control the expression of haemolysin, sex factor and lipopolysaccharide genes [Transcription, Transcription factors]
WYLLYCKPRQEQRAQEHLERQAVECYLPMITVEKIVRGKRQAVSEPLFPNYLFIEFDPEVDSWTTIRSTR
GVSRFVRFGGHPAPVPDDLIHQLRQYEPKDSVPPATTLPYKGDKVRITDGAFAGFEAIFLEPDGEKRSML
LLNMIGKQIKVSVPNTSVE
>gnl|CDD|273895 TIGR01956, NusG_myco, NusG family protein. This model represents a family of Mycoplasma proteins orthologous to the bacterial transcription termination/antitermination factor NusG. These sequences from Mycoplasma are notably diverged (long branches in a Neighbor-joining phylogenetic tree) from the bacterial species. And although NusA and ribosomal protein S10 (NusE) appear to be present, NusB may be absent in Mycoplasmas calling into question whether these species have a functional Nus system including this family as a member
QWYIATTINGNEDEVIENIKAKVRALGLENYISDFKILKEREIEEKVFEPKNGQAPRSMKNTATTKWETL
DETKYKKTKISEKNKYNGYIYIKMIMTEDAWFLIRNTENVTGLVGSSGKGAKPIPISADADKLKMLKGIS
ENTKKRVLVTNTAIVEMEENKFDEKCQYILKHKQVKPEAIAQVSESGEIIDEIVEEFQLVDNLSKFRVGN
FVKIVDGPFKGIVGKIKKIDQEKKKAIVEVEILGKSVDVDLNFKHLKL
>gnl|CDD|273896 TIGR01957, NADH-quinone_oxidoreductase_subunit_B, NADH-quinone oxidoreductase, B subunit. This model describes the B chain of complexes that resemble NADH-quinone oxidoreductases. The electron acceptor is a quinone, ubiquinone, in mitochondria and most bacteria, including Escherichia coli, where the recommended gene symbol is nuoB. The quinone is plastoquinone in Synechocystis (where the chain is designated K) and in chloroplast, where NADH may be replaced by NADPH. In the methanogenic archaeal genus Methanosarcina, NADH is replaced by F420H2 [Energy metabolism, Electron transport]
GVLLTTVDKLLNWGRSNSLWPLTFGLACCAIEMMATGASRYDLDRFGSEVFRASPRQADVMIVAGTVTKK
MAPALRRLYDQMPEPKWVISMGACANSGGMFHTSYSVVQGVDRIVPVDVYIPGCPPRPEALIYGLIKLQK
KIKRE
>gnl|CDD|131013 TIGR01958, NADH-quinone_oxidoreductase_subunit_E, NADH-quinone oxidoreductase, E subunit. This model describes the E chain of complexes that resemble NADH-quinone oxidoreductases. The electron acceptor is a quinone, ubiquinone, in mitochondria and most bacteria, including Escherichia coli, where the recommended gene symbol is nuoB. This model does not identify proteins from chloroplast and cyanobacteria [Energy metabolism, Electron transport]
LIEEIIAKYPDDQKRSAIMPALMIAQEQKGWVTPEAIAAVAEMLGIPPVWVYEVATFYSMFDTEPVGRYH
LQVCTNVPCALRGSEALLKYLENKLGIKPGETTPDGRFTLVEVECLGACGNAPVMMINDDYYEFLTPEKL
DELLERYE
>gnl|CDD|131014 TIGR01959, NADH-quinone_oxidoreductase_subunit_F, NADH-quinone oxidoreductase, F subunit. This model describes the F chain of complexes that resemble NADH-quinone oxidoreductases. The electron acceptor is a quinone, ubiquinone, in mitochondria and most bacteria, including Escherichia coli, where the recommended gene symbol is nuoF. This family does not have any members in chloroplast or cyanobacteria, where the quinone may be plastoquinone and NADH may be replaced by NADPH, nor in Methanosarcina, where NADH is replaced by F420H2 [Energy metabolism, Electron transport]
VLTTNLDNPESWTLEEYEKRGGYDALRKALEEMSPDDIIEEVKDSGLRGRGGAGFPTGLKWSFMPKDDSP
KPKYLVCNADESEPGTCKDRDLMEFDPHQLIEGMIIAAYAIGAHRGYIYIRGEFIKEAENLEAAIAEAYA
AGLLGKNILGSGFDFELFVHRGAGAYICGEETALLESLEGKRGQPRLKPPFPAVFGLYGKPTVINNVETL
ASVPAILRRGADWYRKLGKEKSPGTKLFSVSGHVNKPGNYELPLGTPLRELLEDYAGGMRGGWKLKAVIP
GGSSTPVLPAEQHLDAPMDYDSLAAAGSMLGTGAVIVMDESTCMVKAVRRLSEFYAHESCGQCTPCREGT
GWMVKILERIEEGEGTKEDIDLLLSVCKQIEGKTICALGDAAAWPVQSAIKHFRDEFEAHI
>gnl|CDD|131015 TIGR01960, ndhF3_CO2, NAD(P)H dehydrogenase, subunit NdhF3 family. This family represents a subfamily of NAD(P)H dehydrogenase subunit 5, or ndhF. It is restricted to two paralogs in each completed cyanobacterial genome, in which several subtypes of ndhF are found. Included in this family is NdhF3, shown to play a role in high-affinity CO2 uptake in Synechococcus sp. PCC7002. In all cases, neighboring genes include a paralog of ndhD but do include other NAD(P)H dehydrogenase subunits. Instead, genes related to C02 uptake tend to be found nearby
MLQSLLETSWLVPFYGLIGALLSLPWSPGITRQTGPRPAGYFNLLMTFVAFVHSLLALQAIWSQPPQYLV
WHWLQAAGLDLTFALEISSVSTGALVLITGLNLLAQIFALGYMEKDWGLARFFALLGLFEAGLGGLVLSD
SLFFSYVLLEILTLSTYLLIGFWFAQPLVVTGARDAFLTKRVGDLILLMGVVALSPLAGSWNYDDLAQWA
ATANVNPTTATLLGLALIAGPTGKCAQFPLHLWLDEAMEGPNPASILRNSVVVATGAWVLIKLQPVLTLS
PVALTALIAIGSVTAIGGSLIAIAQIDIKRALSYSVSAYMGLVFIAVGLGQGDLALLLLLTHAIAKALLF
MSIGSIIWNTVTQDLTELGGLWSRRPISGLSFVVGSAGLIAVPPLGSFWAWLKLADGLWATSPWLVGVLL
VVNLLTAFNLTRVFRLVFGGEAKPMTRRSPEVFWPMALPMVVLIGLVLHLPLILQQWSLLPDWAQINWAV
VALLIVSGLLGIGLGSFIYLGRAIPKPIRLPLRFVQDLLAYDFYTDKLYRATVVAAVASISRISAWFDRT
FVDGIVNLVGLVTLFGGEGLKYSVSGQSQFYLLTILLGVAILGAFI
>gnl|CDD|273897 TIGR01961, NADH-quinone_oxidoreductase_subunit_C, NADH (or F420H2) dehydrogenase, subunit C. This model describes the C subunit of the NADH dehydrogenase complex I in bacteria, as well as many instances of the corresponding mitochondrial subunit (NADH dehydrogenase subunit 9) and of the F420H2 dehydrogenase in Methanosarcina. Complex I contains subunits designated A-N. This C subunit often occurs as a fusion protein with the D subunit. This model excludes the NAD(P)H and plastoquinone-dependent form of chloroplasts and [Energy metabolism, Electron transport]
LVVWIKKEQLLEVLTFLKDPALGFELLTDVSGVDYPKEKRFEVVYHLLSIKKNRRIRLKVRLSEDDPVPS
LTSVFPTANWYERETYDMYGIVFDGHPDLRRILMPDDFEGHPLRKDYPLTG
>gnl|CDD|273898 TIGR01962, NADH-quinone_oxidoreductase_subunit_D, NADH dehydrogenase I, D subunit. This model recognizes specificially the D subunit of NADH dehydrogenase I complex. It excludes the related chain of NAD(P)H-quinone oxidoreductases from chloroplast and Synechocystis, where the quinone may be plastoquinone rather than ubiquinone. This subunit often appears as a C/D fusion [Energy metabolism, Electron transport]
EFMILNLGPQHPSTHGVLRLILELDGEYVVRADPHIGYLHRGTEKLAENRTYQQYIPYTDRLDYLSPFSN
ELAYCLAVEKLLGIEVPRRAQVIRVMLSELNRISSHLLFIGTHALDLGAMTPFLYAFREREKILDLFEAI
TGARMHSAYFRIGGVALDLPENWLEEIREFLEQFPKRLRDYETLLNENRIWKQRTQGVGVVSAKDALDWG
LTGPMLRGSGIDWDIRKSEPYEGYDEYDFDVPVGGNGDCYDRYLLRVLEMRESIKIIEQCLEKMPPGPIK
ADNPKLAPPPKERMLTSMEALIHHFKLVTEGFRVPAGEVYVPIESPKGELGFYIISDGGTKPYRLKIRAP
SFAHLQALEAMCVGHYLADLIAILGSIDPVMGEVDR
>gnl|CDD|211705 TIGR01963, D-beta-hydroxybutyrate_dehydrogenase, 3-hydroxybutyrate dehydrogenase. This model represents a subfamily of the short chain dehydrogenases. Characterized members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polmers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accumulate PHAs, including Oceanobacillus iheyensis and Bacillus subtilis. However, polymer formation is not required for there be a role for 3-hydroxybutyrate dehydrogenase; it may be members of this family have the same function in those species
GKTALVTGAASGIGLAIARALAAAGANVVVNDFGEEGAEAAAKVAGDAGGSVIYLPADVTKEDEIADMIA
AAAAEFGGLDILVNNAGIQHVAPIEEFPPEDWDRIIAVMLTSAFHTIRAALPHMKKQGWGRIINIASAHG
LVASPFKSAYVAAKHGLIGLTKVLALEVAEHGITVNAICPGYVRTPLVEKQIADQAKTRGIPEEQVIREV
MLKGQPTKRFVTVDEVAETALYLASDAAAQITGQAIVLDGGWTAQ
>gnl|CDD|213671 TIGR01964, chpXY, CO2 hydration protein. This small family of proteins includes paralogs ChpX and ChpY in Synechococcus sp. PCC7942 and other cyanobacteria, associated with distinct NAD(P)H dehydrogenase complexes. These proteins collectively enable light-dependent CO2 hydration and CO2 uptake; loss of both blocks growth at low CO2 concentrations [Energy metabolism, Photosynthesis]
RHPLRDYIQRLEAGQALLPDTPANLMEVVGILKSYGVPLDAYWRNLLYIAERQFLNLFPFFKYFNGETTM
PRLLHHWWHDRINYEYAEYCMRAMMWHGGGKLDEYLDSAEFKANADKAIRAKFKGNPLMQLLNKLFPEFL
LEQVRMLAYYSALGQFWEVMAPVFLELSDRYDEGEIKSIPDVVNHIVNGLFAIAGRPIYYHVYIDGETYD
ILPKSAGLTFLYETAVPYVEAVFYRGTPFRGTKSYNAQAGQIPPDQSDFHYGALFADPFPVGTAGIPPTL
LMQDMRHFLPPYLREYYQAHCRGEDDLLVQICITFQKSMFCVTTAAIQALAPYPLDTPNPQEQAANRAFF
EAWMDRFLTSRLENVQQ
>gnl|CDD|273899 TIGR01965, VCBS_repeat, VCBS repeat. This domain of about 100 residues is found multiple (up to 35) copies in long proteins from several species of Vibrio, Colwellia, Bradyrhizobium, and Shewanella (hence the name VCBS) and in smaller copy numbers in proteins from several other bacteria. The large protein size and repeat copy numbers, species distribution, and suggested activities of several member proteins suggests a role for this domain in adhesion
SGQLTISDADAGQAHFIAQTDAAGQYGTFSIDADGQWTYQADNSQTAVQALKAGETLTDTFTVTSADGTS
QTVTITITGANDAAVIGGADTGSVTEDST
>gnl|CDD|131021 TIGR01966, Ribonuclease_PH, ribonuclease PH. This bacterial enzyme, ribonuclease PH, performs the final 3'-trimming and modification of tRNA precursors. This model is restricted absolutely to bacteria. Related families outside the model include proteins described as probable exosome complex exonucleases (rRNA processing) and polyribonucleotide nucleotidyltransferases (mRNA degradation). The most divergent member within the family is RNase PH from Deinococcus radiodurans [Transcription, RNA processing]
RPDGRKPDQLRPVSITRDFLKHAEGSVLIEFGNTKVLCTASVEEKVPPFLRGSGEGWITAEYGMLPRATQ
TRNRRESAKGKQSGRTQEIQRLIGRALRAVVDLEALGERTIWIDCDVIQADGGTRTASITGAFVALADAI
SKLHKRGILKESPIRDFVAAVSVGIVDGEPVLDLDYEEDSAADVDMNVVMTGSGGFVEVQGTAEEGPFSR
DELNKLLDLAKKGIRELIELQKQALG
>gnl|CDD|273900 TIGR01967, ATP-dependent_RNA_helicase_HrpA, RNA helicase HrpA. This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB [Unknown function, Enzymes of unknown specificity]
LAEDLDHTMIRDRHRLRRRLHKLRKDHDQDRAIAALAKFRERIDAACDKVEARRQAVPEIRYPDNLPVSA
KREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLG
EKVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRP
DLKIIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYRPLVEEQEDDDLDQLEAILDAVDELFAEGPG
DILIFLPGEREIRDAAEILRKRNLRHTEILPLYARLSNKEQQRVFQPHSGRRIVLATNVAETSLTVPGIH
YVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRT
NLASVILQMLALRLGDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDEAEPQLTPIGRQLAQLPVDPRLA
RMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQALS
ANQFRNACRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKALLSGLLSQIGMKDEKHEY
DGARGRKFHIFPGSPLFKKPPKWVMAAELVETSKLYARLVAKIEPEWVEPVAGHLIKKNYFEPHWEKKRG
QVMAYEKVTLYGLTLVARRSVPYGPIDPADAREMFIRHALVEGEWQTRAAFFQANRALLEEVEELEHKAR
RRDILVDEQTLFDFYDGRLPEDINNARHFDSWWKKASRKQPDLLDFPKEVLFQRRANVISAAQFPDHWHK
GDLRLALSYHFEPGHGDDGVTVHIPLPLLNQLDTEDFDWLVPGLREEKVVALIKSLPKALRRNFVPAPDF
AKACLARLPPNQGPLTDALARELRRMTGERVNPEDWDWEQLPDHLQMNFRIVDDKGKVLAQGRDLALLKE
RLAGDVRAALSAVADVGIEKSGLTNWSFGPLPERMEQKTGNYKVTAYPALVDDGGSVAIKLFDTQAEAEA
AHRAGLRRLLLLQIPSPVKMLQGKLPNKAKLALYYNPLGRVEVLVDDILHAAVDRLIFENGGQVRTQADF
AALLAQVRAELAPEVERIAKQLEEILVLFGNIRKRLKGKIDPTQAKALSDIKAQLDKLVYQGFVRTTGPQ
RLSHLPRYLKAMELRLEKLRVDPGRDRERQAEISNVQEAYDARLAKLPHERRLPAALVEIRWMIEEYRVS
LFAQQLGTAYPISDKRILKYYRQ
>gnl|CDD|131023 TIGR01968, Septum_site-determining_protein_MinD, septum site-determining protein MinD. This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model [Cellular processes, Cell division]
ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYTLVDVVEGECRLQ
QALIKDKRLKNLYLLPASQTRDKDAVTPEQMKKLVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVV
TTPEVSAVRDADRVIGLLEAKGIEKIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVS
TNKGEPVVLNDKSRAGKAFENIARRILGEEVPFEDLTTQKKGFFARIKRFF
>gnl|CDD|131024 TIGR01969, Uncharacterized_ATP-binding_protein_MJ0169, cell division ATPase MinD, archaeal. This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown
RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPVTLHDVLAGEADIKDA
IYEGPFGVKVIPAGVSLEGLRKADPDKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNP
EISSITDALKTKIVAEKLGTAILGVVLNRVTRDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPV
VIYNPNSPAAQAFMELAAELAGIEYEPKEPKKEGFIAKVIR
>gnl|CDD|273901 TIGR01970, ATP-dependent_RNA_helicase_HrpB, ATP-dependent helicase HrpB. This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing [Unknown function, Enzymes of unknown specificity]
LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGGKIIMLEPRRLAARSAAQRLASQLG
EAVGQTVGYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQ
SSLREDLKILAMSATLDGERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQRLEDAVSRAVEHALASETG
SILVFLPGQAEIRRVQEQLAERLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEG
IRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQRLPAQDEPEIL
QADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAA
MLLSAHSTGLAALACDLAALLEERGLPRQGGADLMNRLHRLQQGRQGRGQRAQQLAKKLRRRLRFSQADS
GAIASHALGLLLALAFPDRIAKRRGQPGRYQLANGRGAVLSAEDALAREPWLVAADLGEGQGKTAARILL
AAPVDEALLRQVLPDLVVQVDQVDWDETKGRLVAERQLRIGQLVLKSEPLANPDPAQIAAALLNYVRQKG
LSALNWTEELRQWRARVACARSWDPEADWPDLSDEALLARLETWLEPYLAGVTSLSGLQELDLYDALKNL
LPWELQQALDALLPTHWPVPTGNFIAIRYSLDGPPLLAVRLQELFGLAESPRVAQGRVPLTLELLSPAQR
PLQVTRDLASFWAGAYREVKKEMKGRYPKHVWPDDPANAAPTKRTKPRG
>gnl|CDD|273902 TIGR01971, NADH-quinone_oxidoreductase_subunit_9, NADH-quinone oxidoreductase, chain I. This model represents the I subunit (one of 14: A-_N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes [Energy metabolism, Electron transport]
GLGLTLKYFFSKPVTVQYPEEKLYLPPRFRGRIVLTRDPNGEEKCIGCTLCAAVCPADAIRVVPAEGEDG
KRRLKFYEINFGRCIFCGLCEEACPTDAIVLTPEFELATYTRSDLVYGKEDL
>gnl|CDD|273903 TIGR01972, NADH-quinone_oxidoreductase_subunit_M, proton-translocating NADH-quinone oxidoreductase, chain M. This model describes the 13th (based on E. coli) structural gene, M, of bacterial NADH dehydrogenase I, as well as chain 4 of the corresponding mitochondrial complex I and of the chloroplast NAD(P)H dehydrogenase complex [Energy metabolism, Electron transport]
LSLLIFLPLIGALLILLLPSNKDGKARWIALVVALATLLLSLLLLFQFDPTGSGFQFTEDIPWIPALGIS
YHLGVDGISLLLVLLTALLTLLAILASWESIQKRVKEFYALLLLLEAGVIGVFLALDLFLFYVFWEAMLI
PMYLLIGVWGGPNRIYAAMKFFLYTLAGSLLMLLAILGLYFLGGGTFDLLELLNLPLPFGVQTWLFLAFF
IAFAVKVPLFPLHTWLPDAHVEAPTAGSVILAGVLLKMGTYGFLRFNLPLFPDASLYFAPVLAALGVIAI
IYGALIALAQTDIKRLIAYSSISHMGFVLLGIFSFNELGISGAVFQMISHGLITAALFLLVGVLYERAHT
RDIAKYGGLANKMPVLAAFFMLFAMASLGLPGTSGFVGEFLILLGSFKVNPVVAFLAALGIVLAAAYMLT
LYKRVFFGELSNPEVAEFPDLNGREIAVLAPLVVLILFLGLYPNPLLDLTEPSVNNLLSQV
>gnl|CDD|273904 TIGR01973, NADH-quinone_oxidoreductase_subunit_G, NADH-quinone oxidoreductase, chain G. This model represents the G subunit (one of 14: A-_N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria while translocating protons, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes related subunits from formate dehydrogenase complexes [Energy metabolism, Electron transport]
IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKIS
TNSEKVKKAREGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEM
TRCIHCTRCVRFANEVAGVEDLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPW
ELKSTPSICVHDSVGCNIRVDERNGEIMRILPRENDEINEEWLCDKGRFGYDGLNRQDRLTKPLLRNQEG
NLLEVSWAEALAIAAEKLKASSRIGGIAGPRSSLEELFALKKLVRKLGSENFDLRIRNYEFESADLRANY
LFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALIGIEKWNLTYPANTNLVFHPGLSP
KKLDDIASGAHSDIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIKVRRKEWNGLNILSSGAN
SVGLLDLGGESTGLDAALNLGAADALFLLGADLERALDKTARDALSKADAFIIYQGHHGTETAEKADVIL
PGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL
>gnl|CDD|273905 TIGR01974, NADH-quinone_oxidoreductase_subunit_L, proton-translocating NADH-quinone oxidoreductase, chain L. This model describes the 12th (based on E. coli) structural gene, L, of bacterial NADH dehydrogenase I, as well as chain 5 of the corresponding mitochondrial complex I and subunit 5 (or F) of the chloroplast NAD(P)H-plastoquinone dehydrogenase complex [Energy metabolism, Electron transport]
NLIFLIVFLPLIGFLIAGLFGRRIGERVSGIIGIGSVGLSAALSAFVFVDFFLNGEGEAFTQSLFPWISV
GGFQVDFGLRLDGLSLTMLVVVTGVGSLVHIYSIGYMAHDEGYSRFFAYLNLFTFSMLMLVLADNFLQLF
FGWEGVGLCSYLLIGFWYKKPSANNAAIKAFVVNRVGDFGLLLGIFLIFWYFGTLNFQEVFALAPGAFFS
ALTLICLLLFIGAMGKSAQLPLHTWLPDAMEGPTPVSALIHAATMVTAGVYLVARTSPLFELSPTALYLV
TIIGAITALFAATVALVQNDIKRILAYSTMSQLGYMFLALGVGAYAAAIFHLMTHAFFKALLFLGAGSVI
HAMHHEQDIRKMGGLRKKMPVTYITFLIGSLALIGFPGFAGFFSKDLILEAAFASGTHSFLFVAGLIGAF
LTAFYSFRLIFMVFHGKERHEADAHPHESPLVMLLPLIVLAVGSVFAGFFIVPLFEFLKGVLPTSAEPAL
EHHHVPALEIWSPTAVAILGILLAYLLYLGNPTLPAKIAQRHSGLYRLLLNKWYFDELYDKVFVKPYLFL
GKLLWKDPDDKIIDGFGPGIARLVGAISKRLRKSQTGYLRWYAASMVVG
>gnl|CDD|131030 TIGR01975, Isoaspartyl_dipeptidase, isoaspartyl dipeptidase IadA. The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases [Protein fate, Degradation of proteins, peptides, and glycopeptides]
FTLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPSTKDFVPNCVVVGLEGMIAVPGFIDQHVHIIGGGG
EGGPTTRTPELTLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPSRTITG
SVESDLLLIDKVIGVGEIAISDHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQPIYEL
VENTDVPITQFLPTHINRNVPLFEAGLEFAKKGGTIDLTSSIDPQFRKEGEVAPAEGIKKALEAGVPLEK
VTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVREAVKDGDVPLEKALRVITSNVAGVLNLTGKGEIS
PGNDADLVVLDPDLRIHSVIARGKLMVKDGKACVKGTFE
>gnl|CDD|273906 TIGR01976, am_tr_V_VC1184, cysteine desulfurase family protein, VC1184 subfamily. This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family (pfam00266). The most closely related characterized proteins are active as cysteine desulfurases, selenocysteine lyases, or both; some are involved in FeS cofactor biosynthesis and are designated NifS. An active site Cys residue present in those sequences, in motifs resembling GHHC or GSAC, is not found in this family. The function of members of this family is unknown, but seems unlike to be as an aminotransferase [Unknown function, Enzymes of unknown specificity]
FDVEAVRGQFPALADGDRVFFDNPAGTQIPQSVADAVSAALTRSNANRGGAYESSRRADQVVDDAREAVA
DLLNADPPEVVFGANATSLTFLLSRAISRRWGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDEA
TGELHPDDLASLLSPRTRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGAD
FLTCSAYKFFGPHMGILWGRPELLMNLPPYKLTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGESA
NGSRRERLVASFQAIDAYENRLAEYLLVGLSDLPGVTLYGVARLAARVPTVSFTVHGLPPQRVVRRLADQ
GIDAWAGHFYAVRLLRRLGLNDEGGVVRVGLAHYNTAEEVDRLLEAL
>gnl|CDD|131032 TIGR01977, am_tr_V_EF2568, cysteine desulfurase family protein. This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family. Related families contain members active as cysteine desulfurases, selenocysteine lyases, or both. The members of this family form a distinct clade and all are shorter at the N-terminus. The function of this subfamily is unknown [Unknown function, Enzymes of unknown specificity]
IYFDNAATTYPKPDEVYEAMADFYKNYGGSPGRGRYRLALRASREVEETRQLLAKLFNAPSSAHVVFTNN
ATTALNIALKGLLKEGDHVITTPMEHNSVARPLECLKEQIGVEITIVKCDNEGLISPERIKRAIKTNTKL
IVVSHASNVTGTILPIEEIGELAQENGIFFILDAAQTAGVIPIDMTELAIDMLAFTGHKGLLGPQGTGGL
YIREGIKLKPLKSGGTGSHSALIDQPSELPDRFESGTLNTPGIAGLNAGIKFIEKIGIANIAKKECMLTE
KLLNGLREINKVKIYGPADPANRVGVVSFTVEGIDSEEVADILDEKFDIATRTGLHCAPLAHKTIGTFAT
GTIRLSLGYFNTEEEIEKLLEALSEI
>gnl|CDD|273907 TIGR01978, Probable_ATP-dependent_transporter_SufC, FeS assembly ATPase SufC. SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKGQDLLELE
PDERARAGLFLAFQYPEEIPGVSNLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRS
VNEGFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYI
KPDYVHVLLDGRIVKSGDVELAKELEAKGYDWV
>gnl|CDD|131034 TIGR01979, Probable_cysteine_desulfurase, cysteine desulfurases, SufSfamily. This model represents a subfamily of NifS-related cysteine desulfurases involved in FeS cluster formation needed for nitrogen fixation among other vital functions. Many cysteine desulfurases are also active as selenocysteine lyase and/or cysteine sulfinate desulfinase. This subfamily is associated with the six-gene SUF system described in E. coli and Erwinia as an FeS cluster formation system during oxidative stress. The active site Cys is this subfamily resembles GHHC with one or both His conserved [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREK
VAKFINAASDEEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIP
LDDDGTLDLDDLEKLLTEKTKLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQAL
DCDFYVFSGHKMYGPTGIGVLYGKEELLEQMPPFLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIG
LGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRIYGPRDAEDRGGIISFNVEGVHPHDVGTILDE
EGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVRKFFG
>gnl|CDD|131035 TIGR01980, UPF0051_protein_slr0074, FeS assembly protein SufB. This protein, SufB, forms a cytosolic complex SufBCD. This complex enhances the cysteine desulfurase of SufSE. The system, together with SufA, is believed to act in iron-sulfur cluster formation during oxidative stress. Note that SufC belongs to the family of ABC transporter ATP binding proteins, so this protein, encoded by an adjacent gene, has often been annotated as a transporter component [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
TEYKYGFHDEDKYAYETEKGLTEEVVEEISEKKGEPDWMLDFRLRALELFEKMPMPTWGPDLSGIDYEDI
VYYSKPDKKKATSWDEVPDEIKDTFEKLGIPEAERKALAGVGAQYDSEVIYHNIKEDLEEKGVIFCDMDT
ALKEYPDLVKEYFMSVVPPSDNKFAALNGAVWSGGSFVYVPKGVRVDMPLQTYFRINSENTGQFEHTLII
ADEGASVHYIEGCSAPIYSTNSLHAAVVELIVKEDARVRYSTVQNWSKNVYNLVTKRALVEENGTMEWVS
GSIGSKITMKYPSSILKGEGAKTEFLSIAFAGKGQHLDTGAKMIHLAPNTSSTIISKSISKGGGKSTYRG
LVKIGPGAKGAKSHVQCDSLLIDDESASDTIPYIEIFNDTVDVEHEATVSKISEEQLFYLMSRGLSEEDA
RAMIVRGFVEPITKELPMEYAVELNRLI
>gnl|CDD|273908 TIGR01981, UPF0051_protein_Rv1462/MT1509, FeS assembly protein SufD. This protein, SufD, forms a cytosolic complex SufBCD. This complex enhances the cysteine desulfurase of SufSE. The system, together with SufA, is believed to act in iron-sulfur cluster formation during oxidative stress. SufB and SufD are homologous. Note that SufC belongs to the family of ABC transporter ATP binding proteins, so this protein, encoded by an adjacent gene, has often been annotated as a transporter component [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
TALFNSGLVLYIPKGVEAEEPIELRFIMGSENRVLAPRLLIVVEEGAKATVLERHDSGEGDAFLNGLVEI
NVGENASVEFIKVQFLSATSFHFSTVRITLERDARVRLSDVNLGGKLSRHDTDVDLNGEGSKAEIKGLYF
GDGSQHIDVHTNVIHNGPHTVSNILHRGVLDDRAHGVFNGNIDIPKGAQGTDARQSNRTLLLSDKARADT
KPELEIDADDVKASHGATVGQLDEEQLFYLRSRGIDEAEAKRLLIEGFFGEVIEEIPDESLKEEL
>gnl|CDD|273909 TIGR01982, Probable_protein_kinase_UbiB, 2-polyprenylphenol 6-hydroxylase. This model represents the enzyme (UbiB) which catalyzes the first hydroxylation step in the ubiquinone biosynthetic pathway in bacteria. It is believed that the reaction is 2-polyprenylphenol -_ 6-hydroxy-2-polyprenylphenol. This model finds hits primarily in the proteobacteria. The gene is also known as AarF in certain species [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
LRRLRRIIRVLIRYGFLALVESPIGPLSLRLLRRLLLPFSNRENRLMSRGERLRLALEELGPTFIKFGQT
LSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVD
GKEVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASEL
GENFKNDPGVYVPEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFH
ADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFE
QAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQKTLLTVEGVGRQLDPDLNMWKVAE
PFVKRWIRKRLGPKAKI
>gnl|CDD|273910 TIGR01983, Ubiquinone_biosynthesis_O-methyltransferase, ubiquinone biosynthesis O-methyltransferase. This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRKNFKNPLDGLRVLDVGCGGGLLSEPLARLGAN
VTGIDASEENIEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLK
PGGILFFSTINRTPKSYLLAIVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIK
NTWKLSKDTDVNYM
>gnl|CDD|273911 TIGR01984, 2-polyprenyl-6-methoxyphenol_hydroxylase, 2-polyprenyl-6-methoxyphenol 4-hydroxylase. This model represents the FAD-dependent monoxygenase responsible for the second hydroxylation step in the aerobic ubiquinone bioynthetic pathway. The scope of this model is limited to the proteobacteria. This family is closely related to the UbiF hydroxylase which catalyzes the final hydroxylation step. The enzyme has also been named VisB due to a mutant VISible light sensitive phenotype [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
DVIIVGGGLVGLSLALALSRLGKIKIALIEANSPSAAQPGFDARSLALSYGSKQILEKLGLWPKLAPFAT
PILDIHVSDQGHFGATHLRASEFGLPALGYVVELADLGQALLSRLALLTNIQLYCPARYKEIIRNQDYVR
VTLDNGQQLRAKLLIAADGANSKVRELLSIPTEEHDYNQTALIANIRHEQPHQGCAFERFTPHGPLALLP
LKDNYRSSLVWCLPSKQADTIANLPDAEFLAELQQAFGWRLGKITQVGERKTYPLKLRIAETHVHPRVVL
IGNAAQTLHPIAGQGFNLGLRDVETLAEVLIDARIDLGTYALLQEYLRRRQFDQFITIGLTDGLNRLFSN
HIPLLRALRNLGLLALENFPPLKKRLARQAMG
>gnl|CDD|131040 TIGR01985, kDa_protein, phasin. This model represents a family of granule-associate proteins (phasins) which are part of the polyhydroxyalkanoate synthesis machinery. This family is based on a pair of characterized genes from Methylobacterium extorquens. Members of the seed for this model all contain the rest of the components believed to be essential for this system (see the "polyhydroxyalkanoic acid synthesis" property in the GenPropDB). Members of this family score below trusted to another phasin model, TIGR01841 and together may represent a subfamily or broader equivalog
EVPAEFRDFAEKGVDQAKEAFAKFKGAAEETTKALEDAASTSSLTANEISSKTIEFMQANAEAAFDFTQK
LVGAKDPSEAFEIQSEFLRKQFEAFQAQAKEMGELAQKAATE
>gnl|CDD|273912 TIGR01986, Glutathione_synthetase, glutathione synthetase, eukaryotic. This model represents the eukaryotic glutathione synthetase, which shows little resemblance to the analogous enzyme of Gram-negative bacteria (TIGR01380). In the Kinetoplastida, trypanothione replaces glutathione, but can be made from glutathione; a sequence from Leishmania is not included in the seed, is highly divergent, and therefore scores between the trusted and noise cutoffs
LEELIQEANDWAIAHGVVMYPPSFEKEGPVNASVAPITLFPSPIPRACFDEAVQVQPVFNELYARISQDM
AFLHKTLSSTAKSDEFTGKLWDLYLKTLKSAQYKKQNFRLGLFRSDYMIDKKDGTEQLKQVEFNTISVSF
GGLSEKVSRLHSYLLRSNKYDPKGPIYNMVINTSGYGLAKGIAKAVESYKSPQSSSTTSDPIVLFIVQRN
ERNIFDQRVLELELLERFNIKSIRLTFADVNDKLSIDDDTGKLFVRDTGQEIAVVYYRTGYTPTDYPSQK
DWEARLLLEKSFAIKCPDIATQLAGSKKIQQELADPGVLERFLSDAEKKASLRKTFAGLYPLDDTKLGRE
GIKLALEKPSKFVLKPQREGGGNNVYGEDIPNFLKGLEEEEWDSYILMELIEPEPSENIILRDGKSYKEQ
IISELGIYGCYVRNDKTVVSNEQSGSLLRTKFNTSNEGGVAAGFAVLDSIYL
>gnl|CDD|131042 TIGR01987, Uncharacterized_protein_HI_0074, nucleotidyltransferase substrate binding protein, HI0074 family. The member of this family from Haemophilus influenzae, HI0074, has been shown by crystal structure to resemble nucleotidyltransferase substrate binding proteins. It forms a complex with HI0073, encoded by the adjacent gene and containing a nucleotidyltransferase nucleotide binding domain (pfam01909)
KFESFEQALMQLSDANWFDLTNDITIIDGAIQKFEFTFELAWKLMKRYLAQEGINDIGAYSPKDVLKEAF
RAGLIGDESLWIAMLDDRNITSHTYDQEKAREIYAQIRDYVPEFEFLLEQLRQ
>gnl|CDD|273913 TIGR01988, Ubiquinone_biosynthesis_monooxygenase_COQ6, Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family. This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
DIVIVGGGMVGLALALALARSGLKVALIEATPLPAPADPGFDNRVSALSAASIRLLEKLGVWDKIEPARA
QPIRDIHVSDGGSFGALRFDADEIGLEALGYVVENRVLQQALWERLQELPNVTLLCPARVVELPRHSDHV
ELTLDDGQQLRARLLVGADGANSKVRQLAGIPTTGWDYGQSAVVANVKHERPHQGTAWERFTPTGPLALL
PLPDNRSSLVWTLPPEEAERLLALSDEEFLAELQRAFGSRLGAITLVGERHAFPLSLTHAKRYVAPRLAL
IGDAAHTIHPLAGQGLNLGLRDVAALAEVLEDARRRGEDIGSLRVLQRYERRRRFDNAAMLGATDGLNRL
FSNDFPPLRLLRNLGLRLLNNLPPLKNFIARYAMG
>gnl|CDD|273914 TIGR01989, Ubiquinone_biosynthesis_monooxygenase_COQ6, ubiquinone biosynthesis monooxygenase COQ6. This model represents the monooxygenase responsible for the 4-hydroxylateion of the phenol ring in the aerobic biosynthesis of ubiquinone
FDVVIVGGGPVGLALAAALGNNPLTKDLKVLLLDAVDNPKLKSRNYEKPDGPYSNRVSSITPASISFFKK
IGAWDHIQSDRIQPFGRMQVWDGCSLALIRFDRDNGKEDMACIIENDNIQNSLYNRLQEYNGDNVKILNP
ARLISVTIPSKYPNDNSNWVHITLSDGQVLYTKLLIGADGSNSNVRKAANIDTTGWNYNQHAVVATLKLE
EATENDVAWQRFLPTGPIALLPLPDNNSTLVWSTSPEEALRLLSLPPEDFVDALNAAFDLGYSDHPYSYL
LDYAMEKLNEDIGFRTEGSKSCFQVPPRVIGVVDKSRAAFPLGLGHADEYVTKRVALVGDAAHRVHPLAG
QGVNLGFGDVASLVKALAEAVSVGADIGSISSLKPYERERYAKNVVLLGLVDKLHKLYATDFPPVVALRT
FGLNLTNYIGPLKNFIM
>gnl|CDD|213672 TIGR01990, bPGM, beta-phosphoglucomutase. This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-_ beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state [Energy metabolism, Biosynthesis and degradation of polysaccharides]
AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGKKYSEEEKEELAE
RKNDYYVELLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKG
KPDPEIFLAAAEGLGVSPSECIGIEDAQAGIEAIKAAGMFAVGVG
>gnl|CDD|273915 TIGR01991, HscA, Fe-S protein assembly chaperone HscA. The Heat Shock Cognate proteins HscA and HscB act together as chaperones. HscA resembles DnaK but belongs in a separate clade. The apparent function is to aid assembly of iron-sulfur cluster proteins. Homologs from Buchnera and Wolbachia are clearly in the same clade but are highly derived and score lower than some examples of DnaK [Protein fate, Protein folding and stabilization]
AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGVEVGKEALAAAAEDPKNTISSVKRLM
GRSIEDIKTFSILPYRFVDGPGEMVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYF
DDAQRQATKDAARLAGLNVLRLLNEPTAAAVAYGLDKASEGIYAVYDLGGGTFDVSILKLTKGVFEVLAT
GGDSALGGDDFDHALAKWILKQLGISADLNPEDQRLLLQAARAAKEALTDAESVEVDFTLDGKDFKGKLT
RDEFEALIQPLVQKTLSICRRALRDAGLSVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVV
ALGAAIQADLLAGNRIGNDLLLLDVTPLSLGIETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIH
VVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLLTVSAQEQSTGVEQSIQVKPSYGLSD
EEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDERAAIDAAMEALQKALQGD
DADAIKAAIEALEEATDNFAARRMDRGIRKALAGRSLDE
>gnl|CDD|273916 TIGR01992, phosphotransferase_system_trehalose_permease, PTS system, trehalose-specific IIBC component. This model represents the fused enzyme II B and C components of the trehalose-specific PTS sugar transporter system. Trehalose is converted to trehalose-6-phosphate in the process of translocation into the cell. These transporters lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). The exceptions to this rule are Staphylococci and Streptococci which contain their own A domain as a C-terminal fusion. This family is closely related to the sucrose transporting PTS IIBC enzymes and the B and C domains of each are described by subfamily-domain level TIGRFAMs models (TIGR00826 and TIGR00852, respectively). In E. coli, B. subtilis and P. fluorescens the presence of this gene is associated with the presence of trehalase which degrades T6P to glucose and glucose-6-P. Trehalose may also be transported (in Salmonella) via the mannose PTS or galactose permease systems, or (in Sinorhizobium, Thermococcus and Sulfolobus, for instance) by ABC transporters
RKDAKAILEAIGGKENIEAATHCVTRLRFVLKDPSKVDVKALEQIDLVKGSFTNAGQFQVVIGPGTVDKV
YAALIAETGIAEVSKEEVKKAAAKNMNPLQRLIKLLADIFIPILPAIITAGLLMGINNLLGAKGMSFGGQ
TLVEVYPQWAGIYNFINLIAETAFHFLPALIGWSAVKKFGGSPILGIVLGLMLVHPQLLNAYLYGQALAE
GNIPVWDLFGFFEIQKVGYQGQVLPALLAGYVLAVIEKWLRKRVPDAIQLLVVPPVSLLVTGFLAHAIIG
PIGRLIGNGITSGVTALFTSAAWLGGAIFGLLYAPLVITGLHHMFLAVDLQLIGSLGGTFLWPMIALSNI
AQGSAALGIIFMSRNEKEKGLSLTSAISAYLGVTEPAMFGVNLKYKFPFIAAMIGSGLAGLLSGLNGVLA
NSIGVGGLPGFISIQPQYWPVFAIGMAIAIVVPFVLTIFFSK
>gnl|CDD|273917 TIGR01993, Suppressor_of_disruption_of_TFIIS, pyrimidine 5'-nucleotidase. This family of proteins includes the SDT1/SSM1 gene from yeast which has been shown to code for a pyrimidine (UMP/CMP) 5'nucleotidase. The family spans plants, fungi and a small number of bacteria. These enzymes are members of the haloacid dehalogenase (HAD) superfamily of hydrolases, specifically the IA subfamily (variant 3, TIGR01509)
DVWFFDLDNTLYPHSAGIFLQIDRNITEFVAARLKLSPEEARVLRKDYYKEYGTTLAGLMILHEIDADEY
LRYVHGRLPYDKLKPDPELRNLLLRLPGRKIIFTNGDRAHARRALRRLGIEDCFDGIFCFDTANPDLLPK
PSPQAYEKALREAGVDPERAIFFDDSARNIAAGKALGMKTVLV
>gnl|CDD|273918 TIGR01994, Iron-sulfur_cluster_assembly_scaffold_protein_IscU, SUF system FeS assembly protein, NifU family. Three iron-sulfur cluster assembly systems are known so far. ISC is broadly distributed while NIF tends to be associated with nitrogenase in nitrogen-fixing bacteria. The most recently described is SUF, believed to be important to maintain the function during aerobic stress of enzymes with labile Fe-S clusters. It is fairly widely distributed. This family represents one of two different proteins proposed to act as a scaffold on which the Fe-S cluster is built and from which it is transferred [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
LDSLYRQVILDHYKNPRHRGKLEDATVQERGHNPTCGDEITLTVKLEGDRIEDIAFEGEGCSISQASASM
MTELIKGKTVEEALSLVEAFSEMIQGQETDEDEEKLGDAEALAGVAKFPARIKCATLAWKALERALA
>gnl|CDD|273919 TIGR01995, beta-glucosides_PTS_EIIBCA, PTS system, beta-glucoside-specific IIABC component. This model represents a family of PTS enzyme II proteins in which all three domains are found in the same polypeptide chain and which appear to have a broad specificity for beta-glucosides including salicin (beta-D-glucose-1-salicylate) and arbutin (Hydroquinone-O-beta-D-glucopyranoside). These are distinct from the closely related sucrose-specific and trehalose-specific PTS transporters
YQDLAKAIIENVGGKENIESVTHCATRLRFTLKDDAKADTEKLKKISGVITVVKSGGQYQVVIGNDVNDV
YQALMDVLGLDDQAEDDDSKGKKSILNKLIDLISGVFTPLLPALAGAGLLKAVLTLLTMTGLISADSQTY
QILNAMGDAVFYFLPILLAITAAKRFKVNPYLAAAIGAALLHPTLVAMVGSGKPVTFFGIPVTLMSYSSS
VIPVILAVWLMSYVEKFLKKVIPGALKNFLTPLLVMLITVPLTLLIIGPLGNYAGEGISSGILFLYEVSP
WLAGALLAALWPVLVMFGLHWAMIPIVINNIATQGFDPLILPASLAANFAQGGAALAVMLRTKNKKLKAL
AGSATISALFGITEPAIYGVNLPLKKPFYAAMIGGAVGGAIIGIGSVKAFTAFAPGLLGLPMFINPSDGA
NFISALIAIVISFVVSFVLTYFIGFKDQEDVVTQEAAALSKDESLYAPVAGEMLPLNEVPDEVFSSGAMG
KGIAILPTEGEVVAPVDGTVTAVFPTKHAIGIRSDNGIEILIHVGIDTVELNGEGFEILVKVGDHVKAGQ
LLLTFDLDKIKEAGYDPTTPVVVTNTKDFLDVIPTDKETVTAGDVLLRLI
>gnl|CDD|131051 TIGR01996, Includes:_Phosphotransferase_enzyme_IIB_component, PTS system, sucrose-specific IIBC component. This model represents the fused enzyme II B and C components of the sucrose-specific PTS sugar transporter system. Sucrose is converted to sucrose-6-phosphate in the process of translocation into the cell. Some of these transporters lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). The exceptions to this rule are Staphylococci, Streptococci, Lactococci, Lactobacilli, etc. which contain their own A domain as a C-terminal fusion. This family is closely related to the trehalose transporting PTS IIBC enzymes and the B and C domains of each are described by subfamily-domain level TIGRFAMs models (TIGR00826 and TIGR00852, respectively)
NYQQVAKEILELLGGKDNIVSVAHCATRLRLVLKDESKIDKKAIENLDGVKGTFFNSGQYQIIIGTGVVN
KVYDEIVKLTGLSESSTSEQKAEAAKKMNPFQRFARTLSDIFVPIIPAIVATGLLMGLNGMLTAFGLFGL
SGVSVAPIPEGLAEMINVFTSTAFAFLPILIGFSAAKRFGGNPYLGAVIGLIMVHPSLPNAYGVAAGTAT
GKAWNIFGLHIPVVGYQGTVLPVLVAVWILAKIEKFLRKVVPNALDLLLTPFLTLLITGFLTLLVIGPIG
RWVGDVLTDGLQWLYDLPGGLGGLLFGGLYSLIVITGIHHSFHAIETQLLANTKTGGNFLFPIASMANVA
QGGAALAVFFKTKDKKLKGLAIPSGLSALLGITEPAIFGVNLRYRKPFIAALIGGAIGGAYVVLFHVAAT
AYGLTGIPGFLSILPSGINLLHYIVGMLIAFAVAFIATLLL
>gnl|CDD|131052 TIGR01997, Protein_SufA, FeS assembly scaffold SufA. This model represents the SufA protein of the SUF system of iron-sulfur cluster biosynthesis. This system performs FeS biosynthesis even during oxidative stress and tends to be absent in obligate anaerobic and microaerophilic bacteria [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
AVITLTDAAAIHIRELVAKRPEAVGIRLGVKKTGCAGMEYVLDLVSEPKKDDDLIEHDGAKVFVAPEAVL
FILGTQVDFVRTTLRQGFKFNNPNATSACGCGESFEL
>gnl|CDD|273920 TIGR01998, N-acetylglucosamine_and_glucose_PTS, PTS system, N-acetylglucosamine-specific IIBC component. This model represents the combined B and C domains of the PTS transport system enzyme II specific for N-acetylglucosamine transport. Many of the genes in this family also include an A domain as part of the same polypeptide and thus should be given the name "PTS system, N-acetylglucosamine-specific IIABC component". This family is most closely related to the glucose-specific PTS enzymes [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
ILGYFQKLGRALMLPIATLPVAALLLRIGNATHGADLLVANFFIAAGGAIFDNLGLLFAIGVAIGMSKDN
DGAAALAGLVAYFVVTKVLSPPPLAAALGIKSEINMAFSAWKNVFVGILAGLIAGALYNRFSEIKLPEAL
SFFSGKRLVPIMAGFVGLVLAALLGYVWPTLYGGIVAFGESISGLGALGAGIYGFLNRLLIPTGLHHALN
SVFWFDVAGINDFGNFTGGGDLNRFKGIAGMFMAGFFPIMMFGLPAAALAMYHTARPERRKQVGGMLLSV
AFASFLTGVTEPLEFSFMFLAPVLYALHALLTGLSLFIAAMLHWTAGFSFSAGLIDYVLSFNNPTANQPL
MLLVQGLVFFALYYVVFRFAIRRFNLKTPGREDEDPEGATAAAVTSTGDSKMQLAKQYLAALGGHDNLVS
IDACITRLRLTLKDTSIVDEPALKALGARGVVKLGKHNLQVILGPLAEIVAGEMK
>gnl|CDD|188192 TIGR01999, Iron-sulfur_cluster_assembly_scaffold_protein_IscU, FeS cluster assembly scaffold IscU. This model represents IscU, a homolog of the N-terminal region of NifU, an Fe-S cluster assembly protein found mostly in nitrogen-fixing bacteria. IscU is considered part of the IscSUA-hscAB-fdx system of Fe-S assembly, whereas NifU is found in nitrogenase-containing (nitrogen-fixing) species. A NifU-type protein is also found in Helicobacter and Campylobacter. IscU and NifU are considered scaffold proteins on which Fe-S clusters are assembled before transfer to apoproteins. This model excludes true NifU proteins as in Klebsiella pneumoniae and Anabaena sp. as well as archaeal homologs. It includes largely proteobacterial and eukaryotic forms [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
YSEKVIDHYENPRNVGSLDKDDKNVGTGLVGAPACGDVMKLQIKVNDDGIIEDAKFKTFGCGSAIASSSL
ATELIKGKSLEEALKIKNTEIAKELSLPPVKLHCSLLAEDAIKAAIKDYKSKQE
>gnl|CDD|273921 TIGR02000, Nitrogen_fixation_protein_NifU, Fe-S cluster assembly protein NifU. Three different but partially homologous Fe-S cluster assembly systems have been described: Isc, Suf, and Nif. The latter is associated with donation of an Fe-S cluster to nitrogenase in a number of nitrogen-fixing species. NifU, described here, consists of an N-terminal domain (pfam01592) and a C-terminal domain (pfam01106). Homologs with an equivalent domain archictecture from Helicobacter and Campylobacter, however, are excluded from this model by a high trusted cutoff. The model, therefore, is specific for NifU involved in nitrogenase maturation. The related model TIGR01999 homologous to the N-terminus of this model describes IscU from the Isc system as in E. coli, Saccharomyces cerevisiae, and Homo sapiens [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]
MWDYTDKVKEHFYNPKNAGVVEDANAVGEVGSISCGDALRLMLKVDPESDKIVDAGFQTFGCGSAIASSS
ALTEMIKGLTLDEALKVSNQDIADYLGGLPPEKMHCSVMGQEALEAAIANYRGEPLEDDHDEGALVCKCF
GVDENMVRRAVIENDLTTLEEVTNYTKAGGGCGSCHEKIEDVLKEVLANKGATNPANAGGSKPTNKPNSG
QKRPLTNVQRIQLIQKVLEEVRPVLQADGGDVELYDVDGKIVYVVLTGACSGCSMSTMTLKGIQQRLRER
LGEFVVVEAV
>gnl|CDD|273922 TIGR02001, gcw_chp, conserved hypothetical protein, proteobacterial. This model represents a conserved hypothetical protein about 240 residues in length found so far in Proteobacteria including Shewanella oneidensis, Ralstonia solanacearum, and Colwellia psychrerythraea, usually as part of a paralogous family. The function is unknown
MKKSLLAALLTCALLASAAPLAQAMARQLGDAEVSGNVTLTSDYVFRGVSQTNSDPAIQGGLDYSHESGF
YAGVWASNVDFGAPDPTIEIDFYAGYKGELGDSLGYDVGLLYYSYPGASGSDYSYTELYGKISYLGSRLG
YSLAVNYDDDFGGSGADGGYYAFDADFTLKEGHTLSLHVGYSDGDADGAVDSYSDWSVGLSKPFLGLDLS
LAYSDTSLSGDCKAYSGNSYCDSRVVLSVSRSF
>gnl|CDD|273923 TIGR02002, PTS_system_glucose-specific_IIABC_component, PTS system, glucose-specific IIBC component. This model represents the combined B and C domains of the PTS transport system enzyme II specific for glucose transport. Many of the genes in this family also include an A domain as part of the same polypeptide and thus should be given the name "PTS system, glucose-specific IIABC component" while the B. subtilus enzyme also contains an enzyme III domain which appears to act independently of the enzyme II domains. This family is most closely related to the N-acetylglucosamine-specific PTS enzymes (TIGR01998) [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
FKKAFGQLQKIGKALMLPVAVLPVAGILLGFGNANQNNQVFSFLPFLHMEWIQLVSKVMEAAGGIIFANL
PLIFAIGVALGLAGNDGVAGLAALVGYLIMNKTMGVVAGLTLLLIASEIASFASVLGIPTLQTGVFGGII
IGAIAAYCYNRFYNIKLPEYLGFFAGKRFVPIITGLAAIVTGIVLSFIWPPVQDALNTFSHWAAYQNPVV
AFFIFGFIERSLIPFGLHHIFNAPFWFEFGSYTNEAGNLFRGDQPIFMAQLKDGVAFTAGGFLSGGFPFM
MFGLPAAALAIYHSAKPENKKLVGGLMISAALTSFLTGITEPLEFSFLFVAPILYVIHAILAGLSFPIMI
LLGVKIGTTFSGGAIDFILYGLLSNRSKAWLFIIVGIGYAIIYYFLFRFLIKKLNLKTPGREDATAEAKA
TGEPSELAFDVVAALGGKENITSLDACITRLRVSVADISKVDVAKLKKLGAAGVLVVGNNVQAIFGPKSD
TIKSEMHDIIRG
>gnl|CDD|131058 TIGR02003, PTS_system_glucose-specific_IIBC_component, PTS system, IIBC component. This model represents a family of fused B and C components of PTS enzyme II. This clade is a member of a larger family which contains enzyme II's specific for a variety of sugars including glucose (TIGR02002) and N-acetylglucosamine (TIGR01998). None of the members of this clade have been experimentally characterized. This clade includes sequences from Streptococcus and Enterococcus which also include a C-terminal A domain as well as Bacillus and Clostridium which do not. In nearly all cases, these species also contain an authentic glucose-specific PTS transporter [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
KIFRFDFWQKFGKALLVVIAVMPAAGLMISIGKLIGMIAGDSAALASIANIIADIGWAIITNLHILFALA
IGGSWAKDRAGGAFAAGLAFVLINRITGAFFGVNAAMLADPEAKISSFIAGDLIVKDYFTSVLEAPALNM
GVFVGIIAGFLGATAYNKYYNYDKLPEALAFFNGKRFVPFVVILRSIFTAIILSLLWPFIQSGINEFGMW
IAASKDSAPILAPFLYGTLERLLLPFGLHHMLTIPMNYTALGGTYEMLTGAAAGQKVAGQDPLWLAWITD
LNHLKANGDAKAYNDLLDNVTPARFKAGQMIGATAALMGIAFAMFRNVDADKKAKYKMMFISAAAAVFLT
GVTEPIEFLFMFAAMPLYIVYAITQGAAFALADLINLRVHAFGFIELITRTPMALKAGLGMDLINFVIVS
ILFAGIMFFIADFLIKKFHLATAGRAGNYDADIEDDRASEARGNQQADSGSLATKIIDLLGGAENIADVD
ACMTRLRVTVKDLAKVAAEADWKKADALGLIQKDKGVQAVYGPKADVLKSDIQDLLDA
>gnl|CDD|273924 TIGR02004, PTS_permease_for_glucose, PTS system, maltose and glucose-specific IIBC component. This model represents a family of PTS enzyme II fused B and C components including and most closely related to the MalX maltose and glucose-specific transporter of E. coli. A pair of paralogous genes from E. coli strain CFT073 score between trusted and noise and may have diverged sufficiently to have an altered substrate specificity [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
KATFWEFFQGLGKTFMLPVALLAFMGILLGLGSSFSSEAMIETIPFLGKPAFKIIFQWMSTIGLVAFAYL
PVMFAMAIPLGLAREEKGVAAFSGFVGYTAMNLAINFYLTQTGVLVDPEQLREAGQGMVFGIQSIDTGVL
GAVIVGLIVYKLHNRFYTVQMPDALAFFGGARFVPIISALVLAVVGLVIPLVWPLFALMIMAIGQLIQRS
GIFGPFLFGSGERLLLPIGLHHILVAMIRFTEAGGSAVVCGKEVSGALNIFYAELQCNLPISAVPSATAF
LSQGKMPTFLGGLPGAALAMYHCARPANRHKIKALLLSGVVACAVGGITEPLEFLFLFVAPLLYLVHAIL
TGLGFMVMALLGVVIGNTDGNLIDFLVFGVLQGTYTKWYLVPIVAAIWFVVYYFVFKTAITTFDLKTPGR
EKVLDAEEYTEQEVAYKKTGGYDAAAILAALGGQENIQSLDNCITRLRLVVADANKVDDAKLKQLGALGV
VKLDAHNVQVVIGTQVTTVKNQLEMIL
>gnl|CDD|273925 TIGR02005, PTS-IIBC-alpha, PTS system, alpha-glucoside-specific IIBC component. This model represents a family of fused PTS enzyme II B and C domains. A gene from Clostridium has been partially characterized as a maltose transporter, while genes from Fusobacterium and Klebsiella have been proposed to transport the five non-standard isomers of sucrose [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
MNAIQRFGGAMFVPVLLFAFAGIVVGFAILFKNPDIMGSLADQNTFWYKFWSVIEEGGWTVFRQMPLIFV
VGLPIGLAKKAQGRACLAALMGYLTFNYFINAILTQWGSSFGVNFTQGVGVGVSGLTSIAGIKTLDTSII
GAIIISGIITYIHNRFFDKRLPVFLGIFQGTTFVVTIAFFVMLPCAAITCLVWPKVQMGIGSLQAFLISS
GYIGVWLYTFLERILIPTGLHHFIYGPFIFGPAVVNHGIQAYWAQHLNEFAKSTKPLKELFPYGGFALHG
NSKVFGCLGIALAMYATAPPENRKKVAGLLIPATLTAVVVGITEPLEFTFLFIAPYLFVVHAVLAASMAT
VMYAFGVVGNMGGGLIDFIATNWLPLFKNHWGTYVTQIIIGLCFTAIYFLVFRFLILKFNIPTPGREDTE
EEVKLYSKADYKAKKGDSVESKRASSGNDKAAYFLQALGGKENIKDVTNCATRLRISVKDESKVLDDEVF
KKAGAHGVVRSGKAIQVIVGLSVPQVREAFEQLV
>gnl|CDD|131061 TIGR02006, Cysteine_desulfurase_IscS, cysteine desulfurase IscS. This model represents IscS, one of several cysteine desulfurases from a larger protein family designated (misleadingly, in this case) class V aminotransferases. IscS is one of at least 6 enzymes characteristic of the IscSUA-hscAB-fsx system of iron-sulfur cluster assembly. Scoring almost as well as proteobacterial sequences included in the model are mitochondrial cysteine desulfurases, apparently from an analogous system in eukaryotes. The sulfur, taken from cysteine, may be used in other systems as well, such as tRNA base modification and biosynthesis of other cofactors [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Protein synthesis, tRNA and rRNA base modification]
MKLPIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFT
SGATESNNLAIKGIAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIR
DDTILVSIMHVNNEIGVIQDIAAIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKG
IGALYVRRKPRVRLEALIHGGGHERGMRSGTLPTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIK
SIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGINDELAHSS
IRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWAAH
>gnl|CDD|131062 TIGR02007, 2Fe-2S_ferredoxin, ferredoxin, 2Fe-2S type, ISC system. This family consists of proteobacterial ferredoxins associated with and essential to the ISC system of 2Fe-2S cluster assembly. This family is closely related to (but excludes) eukaryotic (mitochondrial) adrenodoxins, which are ferredoxins involved in electron transfer to P450 cytochromes [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
PKIVFLPHEDLCPEGAVVEAKPGETILDVALDNGIEIEHACEKSCACTTCHCIVREGFDSLEEASEQEED
MLDKAWGLEPDSRLSCQAVVADEDLVVEIPKYTINHAREA
>gnl|CDD|273926 TIGR02008, Ferredoxin_root_R-B1, ferredoxin [2Fe-2S]. This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins
ATYKVTLVNPDGGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQM
EAGYVLTCVAYPTSDCTIETHKEEDLY
>gnl|CDD|213673 TIGR02009, Hypothetical_protein_Rv3400/MT3508/Mb3433., beta-phosphoglucomutase family hydrolase. This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509)
YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLEEIHQL
AERKNELYRELLRLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKN
GKPHPETFLLAAELLGVPPNECIVFEDALAGVQAARAAGMFAVAV
>gnl|CDD|273927 TIGR02010, Putative_HTH-type_transcriptional_regulator, iron-sulfur cluster assembly transcription factor IscR. This model describes IscR, an iron-sulfur binding transcription factor of the ISC iron-sulfur cluster assembly system [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Regulatory functions, DNA interactions]
MRLTTKGRYAVTAMLDLALNSETGPVTLADISERQGISLSYLEQLFAKLRKAGLVKSVRGPGGGYQLGRP
AEDISVADIIDAVDESVDATRCQGKGNCQHGTKCLTHDLWADLSKHIRDYLESISLADLVNQQNV
>gnl|CDD|213674 TIGR02011, Protein_yfhF., iron-sulfur cluster assembly protein IscA. This model represents the IscA component of the ISC system for iron-sulfur cluster assembly. The ISC system consists of IscRASU, HscAB and an Isc-specific ferredoxin. IscA previously was believed to act as a scaffold and now is seen as an iron donor protein. This clade is limited to the proteobacteria [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
ITLTDSAAARVNTFLANRGKGFGLRLGVKTSGCSGMAYVLEFVDEPTPDDIVFEDKGVKIVIDGKSLQYL
DGTQLDFVKEGLNEGFKFTNPNVKDECGCGESFHV
>gnl|CDD|162659 TIGR02012, Protein_RecA, protein RecA. This model describes orthologs of the recA protein. RecA promotes hybridization of homolgous regions of DNA. A segment of ssDNA can be hybridized to another ssDNA region, or to a dsDNA region. ATP is hydrolyzed in the process. Part of the SOS respones, it is regulated by LexA via autocatalytic cleavage [DNA metabolism, DNA replication, recombination, and repair]
DKQKALEAALAQIEKQFGKGSIMRLGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTT
LALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVD
SVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNA
LKFYASVRLDIRRIGTVKQGEEVVGNRTKVKVVKNKVAPPFREAEFDILYGEGISKLGEIIDLAVELDII
KKSGSWYSYGDEKLGQGRENAKAFLKENPELAQEIEKKVRE
>gnl|CDD|273928 TIGR02013, DNA-directed_RNA_polymerase_subunit_beta, DNA-directed RNA polymerase, beta subunit. This model describes orthologs of the beta subunit of Bacterial RNA polymerase. The core enzyme consists of two alpha chains, one beta chain, and one beta' subunit [Transcription, DNA-dependent RNA polymerase]
KKRIRIDFGKIPEVLEVPNLLEIQLDSYDWFLQQDTPPEKRKEEGLEEVFKSIFPIEDYTGNIELEYLSY
RLGEPKYSVEECKERGLTYSAPLKVKLRLINKEEDGTKEIKEQDVYMGDIPLMTDRGTFIINGAERVVVS
QLHRSPGVFFSSEKDTTKSGKVLFSARIIPYRGSWLEFETDKKDVLYVRIDRKRKLPATVLLRALGYTID
TLILNRLGSGEYIRNTLRKDPTNSEEEALVEIYRKLRPGEPPTVEAARSLLENLFFDPKRYDLGRVGRYK
LNKKLGLDVPESIGVLTKEDIIATIKYLIKLRNGKGEIDDIDHLGNRRIRSVGELLQNQFRVGLARMERI
VRERMSTQDTDTLTPQDLINAKPISAAIKEFFGSSQLSQFMDQTNPLAELTHKRRLSALGPGGLTRERAG
FEVRDVHPTHYGRICPIETPEGPNIGLINSLSTYARVNEYGFIETPYRKVKDGKVVVTDEIDYLTADEED
NYVIAQANAPLDENGRFVEDLVVARYRGEITLVSPDQVDYMDVSPKQVVSVAASLIPFLEHDDANRALMG
SNMQRQAVPLLRSEAPLVGTGMEAKVARDSGAVIVAKRGGVVEYVDAKRIVIRYDEDEEEPDGGIDIYRL
LKYQRSNQDTCINQRPIVSVGDRVEAGDVLADGPSTDLGELALGRNVLVAFMPWNGYNYEDAILISERLV
KDDVFTSIHIEEYEVEARDTKLGPEEITRDIPNVSEEALRNLDENGIVRIGAEVKAGDILVGKVTPKGET
ELTPEEKLLRAIFGEKARDVRDTSLRVPPGVEGTVIDVKVFSREQGDELPPGVNKLVKVYIAQKRKIQVG
DKMAGRHGNKGVVSKILPIEDMPFLEDGTPVDIVLNPLGVPSRMNIGQILETHLGWAGKRLGRKGVPIAT
PVFDGASEEEIKEYLEKAGLPRDGKVRLYDGRTGEQFDRPVTVGYMYMLKLHHLVDDKMHARSTGPYSLV
TQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVVGRTKAYEAIVKGENVPEPGIPESFN
VLIKELQSLGLDIEL
>gnl|CDD|131069 TIGR02014, chlorin_reductase_subunit, chlorophyllide reductase subunit Z. This model represents the Z subunit of the three-subunit enzyme, (bacterio)chlorophyllide reductase. This enzyme is responsible for the reduction of the chlorin B-ring and is closely related to the protochlorophyllide reductase complex which reduces the D-ring. Both of these complexes in turn are homologous to nitrogenase [Energy metabolism, Photosynthesis]
TIRDHDRAGGYWGAVYTFCALKGLQVVIDGPVGCENLPVTAVLHYTDALPPHELPIVVTGLGESEISSSG
TEAIMQRAIEKLDPGKPAVVVTGSIAEMIGGGVTPKGTSVRRFLPRTIDEDQWQGADRALAWLFSEFGDG
KRQKPARPQIAKPRVNIIGPTYGCFNMPSDLAEIRRLVEGIGAEVAHVYPLGSHLAEITKLKNADANIVM
YREFGRGLAEKLGKPYLQAPIGIESTTAFLRKLGRLLGLDPEPFIEREKRTTLKPVWDLWRSVTQDFFGT
ARFGIVASETYARGIRHVLEDELGLPCLFSLARKAGSKTDNNAVRKEIVQKQPLVLYGSMNEKIYLAEAD
AKSRFIPASFPGAIIRRATGTPFMGYSGATWLVQEVCNALFDTLFNILPITRRQDAAAATPSRMHDPLPW
DPEANAILDRIVEKAPVISRISAARELRDAAENLAASAGADTVTPDIV
>gnl|CDD|131070 TIGR02015, Chlorophyllide_reductase_52.5_kDa_chain, chlorophyllide reductase subunit Y. This model represents the Y subunit of the three-subunit enzyme, (bacterio)chlorophyllide reductase. This enzyme is responsible for the reduction of the chlorin B-ring and is closely related to the protochlorophyllide reductase complex which reduces the D-ring. Both of these complexes in turn are homologous to nitrogenase [Energy metabolism, Photosynthesis]
DYPVGPHDQPQSMCPAFGGLRVGLRMDRAATVLAGSACCVYGLTFVSHFYGARRSVGYVPFDSEQLVTGK
LFEDVRCSVHKLADPASYDAIVVINLCVPTASGVPLELLPKRINGVRVLGIDVPGFGVPTHAEAKDVLVS
AMLKYARREVSAGPVGEPKSGRDSKPTLVLLGEIFPVDAMVIGGVLQPIGVESGPTVPGRDWRELYAALD
SSAVAVLHPFYEATARLFEAAGVKIVGSAPVGANGTGEWLERIGEALDLDPDTVKTVAEEERQKIKGAIA
AEPIKGRVTVSGYEGSELLVVRLLLESGADVPYVGTAIPRTAWGAEDKRWLEMLGVEVKYRASLEDDMEA
VLEFEPDLAIGTTPLVQFAKEHGIPALYFTNLISARPLMGPAGAGSLLQVINGALENRERYGRMKEFFEG
VG
>gnl|CDD|273929 TIGR02016, Chlorophyllide_reductase_35.5_kDa_chain, chlorophyllide reductase iron protein subunit X. This model represents the X subunit of the three-subunit enzyme, (bacterio)chlorophyllide reductase. This enzyme is responsible for the reduction of the chlorin B-ring and is closely related to the protochlorophyllide reductase complex which reduces the D-ring. Both of these complexes in turn are homologous to nitrogenase. This subunit is homologous to the nitrogenase component II, or "iron" protein [Energy metabolism, Photosynthesis]
RIIAIYGKGGSGKSFTTTNLSHMMAEMGKRVLQLGCDPKHDSTSLLFGGISLPTIIEVATEKKLAGEEVK
VGDVCFKTTIMNGSGGVYGMELGGPEVGRGCGGRGIIHGFDLLEKLGFHDWDFDFVLMDFLGDVVCGGFA
TPLARSLAEEVIVIGSNDRQSLYVANNICNAVEYFRKLGGRVGLLGLVVNRDDGSGEAQAFAREVGIPVL
AAIPADEELRRKSLAYQIVGSHATPRFGKLFEELAGNVADAPPLRPRPLSPDALLALFETLPETRVVDLV
GATEEDLRGSNAAAKK
>gnl|CDD|131072 TIGR02017, hutG_amidohyd, N-formylglutamate amidohydrolase. In some species, histidine is converted to via urocanate and then formimino-L-glutamate to glutamate in four steps, where the fourth step is conversion of N-formimino-L-glutamate to L-glutamate and formamide. In others, that pathway from formimino-L-glutamate may differ, with the next enzyme being formiminoglutamate hydrolase (HutF) yielding N-formyl-L-glutamate. This model represents the enzyme N-formylglutamate deformylase, also called N-formylglutamate amidohydrolase, which then produces glutamate [Energy metabolism, Amino acids and amines]
DWLEVQRGNAPLLISIPHTGTDLPDAVESGLVSPWLALRDTDWHIHQLYDFARDLGATVVRTTYSRTVID
VNRDPDGVSLYPGQATTGLCPETTFDGEPLYRDGEAPSPAEIDDRRTQIFRPYHAALQAEIERLRAQHGY
AVLYDAHSIRSVIPRLFEGKLPDFNIGTNDGASCDPALTDAVEAVCAKATGYSHVLNGRFKGGWITRHYG
QPQNGVHAVQMELAQRGYMAEEAEPFAYRPDRAAPLRAVLKQLLQALLDWAAE
>gnl|CDD|188194 TIGR02018, Histidine_utilization_repressor, histidine utilization repressor, proteobacterial. This model represents a proteobacterial histidine utilization repressor. It is usually found clustered with the enzymes HutUHIG so that it can regulate its own expression as well. A number of species have several paralogs and may fine-tune the regulation according to levels of degradation intermediates such as urocanate. This family belongs to the larger GntR family of transcriptional regulators [Energy metabolism, Amino acids and amines, Regulatory functions, DNA interactions]
PLYQRIKQDILERIRSGEWPPGHRIPSEHELVAQYGCSRMTVNRALRELTDAGLLERRQGVGTFVAEPKA
QSALLEIRNIADEIVARGHRYRYELLELETRRATAEDAAALALPAGGKVFHSEIVHFENDVPFQLEDRLV
NAAAVPDYLKQDFTQTTPGAYLSQAAPLTEAEHRIEAISADPEEARLLAIDAGEPCLLIRRRTWSGAQVV
TRARLLYPGSRYRLVGRFTP
>gnl|CDD|131074 TIGR02019, Bacteriochlorophyll_synthase_23_kDa_chain, bacteriochlorophyll 4-vinyl reductase. This model represents the component of bacteriochlorophyll synthetase responsible for reduction of the B-ring pendant ethylene (4-vinyl) group. It appears that this step must precede the reduction of ring D, at least by the "dark" protochlorophyllide reductase enzymes BchN, BchB and BchL. This family appears to be present in photosynthetic bacteria except for the cyanobacterial clade. Cyanobacteria must use a non-orthologous gene to carry out this required step for the biosynthesis of both bacteriochlorophyll and chlorophyll [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
RIGPNSIIQTVPALEAAYGPGAADRALAAAGQGVLRPGPPSGMLPESQFSTLHRWLRDTLGETAAARLLR
ESGLATADYILANRIPPPAQRLIRALPAGLAARVLLTAIAKHAWTFAGSGKFRYVSGPPLSFEIARNPVV
AGESSDTPVCHWYAAVFERLLRRLVWPHVAVRETACCAKGAPRCRFEL
>gnl|CDD|131075 TIGR02020, 2-vinyl_bacteriochlorophillide_hydratase_putative, 2-vinyl bacteriochlorophyllide hydratase. This model represents the enzyme responsible for the first step in the modification of the ring A vinyl group of chlorophyllide a which (in part) distinguishes chlorophyll from bacteriochlorophyll. This enzyme is aparrently absent from cyanobacteria (which do not use bacteriochlorophyll) [Energy metabolism, Photosynthesis]
RYTPEQLAKRNASVWTTVQGILAPIQFLIFLGGLTLVTLYLFNLAGTDFYWATISILFKTLFLFTIFITG
AFFEKEVFGKYLFAKEFFWEDVGSMLAIFLHLLYFVMAFWMEYAEHVLMVEAYAAYLTYVINAAQFLVRL
RLEKN
>gnl|CDD|273930 TIGR02021, magnesium-protoporphyrin_O-methyltransferase, magnesium protoporphyrin O-methyltransferase. This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
QKEQVRHYFDGTAFQRWARIYGSGDPVSRVRQTVREGRAAMRRKLLDWLPKDPLKGKRVLDAGCGTGLLS
IELAKRGAIVKAVDISEQMVQMARNRAQGRDVAGNVEFEVNDLLSLCGEFDIVVCMDVLIHYPASDMAKA
LGHLASLTKERVIFTFAPKTAWLAFLKMIGELFPGSSRATSAYLHPMTDLERALGELGWKIVREGLVSTG
FYNSMLLEI
>gnl|CDD|273931 TIGR02022, hutF, formiminoglutamate deiminase. In some species, histidine utilization goes via urocanate to glutamate in four step, the last being removal of formamide. This model describes an alternate fourth step, formiminoglutamate hydrolase, which leads to N-formyl-L-glutamate. This product may be acted on by formylglutamate amidohydrolase (TIGR02017) and bypass glutamate as a product during its degradation. Alternatively, removal of formate (by EC 3.5.1.68) would yield glutamate [Energy metabolism, Amino acids and amines]
MHVYWAERALLPDGWAEGVRIAVADGRILAIETGVPAAPGDERLSGPLLPGLANLHSHAFQRAMAGLAEV
AGSGGDSFWTWRELMYRFADRLTPEQLQAIARQLYVEMLEAGFTRVGEFHYLHHAPDGTPYADPAEMAER
IAAAAADAGIGLTLLPVFYAHSGFGGAAPNPGQRRFIHDPERFARLVEVLRRTLAAQPGAVLGLAPHSLR
AVTPEQLAAVLQASDRQAPVHIHVAEQQKEVDDCLAWSGRRPVEWLLDHGPVDARWCLVHATHLTDEETK
LLAKSGAVAGLCPTTEANLGDGIFPAVDFAAAGGRFGIGSDSHVLIDVAEELRQLEYGQRLRDRARNVLA
AGPGPSVGRALYDAALLGGAQALGRATGGLRAGARADFLTLDGDHPRLAGALGDSLLDRWLFAGGKAAVR
DVWVGGRWVVRDGRHALREEIGRAFAKVLRALLA
>gnl|CDD|273932 TIGR02023, geranylgeranyl_bacteriochlorophyll_reductase, geranylgeranyl reductase. This model represents a group of geranylgeranyl reductases specific for the biosyntheses of bacteriochlorophyll and chlorophyll. It is unclear whether the processes of isoprenoid ligation to the chlorin ring and reduction of the geranylgeranyl chain to a phytyl chain are necessarily ordered the same way in all species [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
YDVAVIGGGPSGATAAETLARAGIETILLERALSNIKPCGGAIPPCLIEEFDIPDSLIDRRVTQMRMISP
SRVPIKVTIPSEDGYVGMVRREVFDSYLRERAQKAGAELIHGLFLKLERDRDGVTLTYRTPKKGAGGEKG
SVEADVVIGADGANSPVAKELGLPKNLPRVIAYQERIKLPDDKMAYYEELADVYYGGEVSPDFYGWVFPK
GDHIAVGTGTGTHGFDAKQLQANLRRRAGLDGGQTIRREAAPIPMKPRPRWDFGRAMLVGDAAGLVTPAS
GEGIYFAMKSGQMAAQAIAEYLQNGDATDLRHYERKFMKLYGTTFRVLRVLQMVYYRSDRRREVFVEMCR
DKDVQRLTFDSYMYKQMAPAPWLAQLKIAAKNIGSLVR
>gnl|CDD|131079 TIGR02024, FtcD, glutamate formiminotransferase. This model represents the tetrahydrofolate (THF) dependent glutamate formiminotransferase involved in the histidine utilization pathway. This enzyme interconverts L-glutamate and N-formimino-L-glutamate. The enzyme is bifunctional as it also catalyzes the cyclodeaminase reaction on N-formimino-THF, converting it to 5,10-methenyl-THF and releasing ammonia - part of the process of regenerating THF. This model covers enzymes from metazoa as well as gram-positive bacteria and archaea. In humans, deficiency of this enzyme results in a disease phenotype. The crystal structure of the enzyme has been studied in the context of the catalytic mechanism [Energy metabolism, Amino acids and amines]
MMKLVECVPNFSEGRNKEVIEKIVDAIIKTDNVKLLDVDMDPDHNRSVITFVGEPECVVNAALKLAKKAA
ELIDMRNHKGEHPRMGAADVIPFIPVRNVTMEECVELAKEFGKRLGEELGVPVYLYEEAATRPERQTLAA
IRKGQYEALFEKIKDPKWKPDFGPSEFNPKAGATATGARKFLIAFNVNLGTSNLEIAKKIAKAIRFQGGG
LRFVKAIGLYLEEKNLVQVSMNLTNYEKTPLYRVFELIKMEAQRYGVPVVGSELVGLVPLKALLDVAAYY
LRLDSFDPKQIIEYLLLE
>gnl|CDD|273933 TIGR02025, Magnesium-chelatase_subunit_H, magnesium chelatase, H subunit. This model represents the H subunit of the magnesium chelatase complex responsible for magnesium insertion into the protoporphyrin IX ring in the biosynthesis of both chlorophyll and bacteriochlorophyll. In chlorophyll-utilizing species, this gene is known as ChlH, while in bacteriochlorophyll-utilizing spoecies it is called BchH. Subunit H is the largest (~140kDa) of the three subunits (the others being BchD/ChlD and BchI/ChlI), and is known to bind protoporphyrin IX. Subunit H is homologous to the CobN subunit of cobaltochelatase and by anology with that enzyme, subunit H is believed to also bind the magnesium ion which is inserted into the ring. In conjunction with the hydrolysis of ATP by subunits I and D, a conformation change is believed to happen in subunit H causing the magnesium ion insertion into the distorted protoporphyrin ring [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
MRIVLIVGEEQYNAALSRAAANLNRELPLDIDLTIFVLSDLDEPEKRLEFEQAIQEADLFFGSMLFDEDQ
VDWLREVLSQIRNQEDTVVVFESMPELMKLTKLGSFAMGKPAEKSGMPKPVKKIADKSNGRGEDKLAGYM
KLLKIVPKLLKFIPGKAQDLRNWLLSYQYWLGGSPENVANMLRLLADKYFDGEIGGKIDPPVEYPDIGLY
HPDAKGFFETVKEYLAWYKKREGCRAPKAPRVGLLLLRKHLLTENQAHYDNLIRELEAAGLQVVPAFSGG
LDGRVAVEDFFMKDSPEAVKVDAVVSLTGFSLVGGPAGSDAAAAVEILKGLDVPYIVAIPLLFQTIESWT
ASDLGLGPLQVALLVAIPELDGAIAPVILGGLVGEAGDAIPVQERLERLAGRVKRWVRLRKKPNAEKKVA
IVLFNFPPGLGNVGTAAYLDVFESLYELLHRLKDEGYNVGELPESVEELREAVLEGNEEQYGSAKLNVAV
RIPVEQYERLYPRTERIEEQWGSAPGELLTDGDELHIGGAQFGNVFIGVQPSFGYEGDPMRLLFERDATP
HHQFAAFYRWLDRDFKADAVLHFGTHGSLEFMPGKQTGLTGECWPDRLLGDLPNFYIYAVNNPSEATIAK
RRGYATLISYLTPPLERAGLYKGLRELKELIAEYRELPNAERGYQIVEAIMKKAVDLNLDTDCPRPPDEP
FEDFVGRLYIYLTELENRLIPNGLHVLGEAPSAESLIDTLMEIASVDREELGSSSLPFLVTTGGRSYEEI
HRLSEKGDQAERESLEYLEFGLELMQNDDELNGLLRALEGEYIPPGPGGDLVRNPNVLPTGRNIHALDPY
RIPSPAAVKRGTRIADKLLAQHRAENGGNYPETIALVLWGTDNIKTKGESVAQALALMGAEPVPDALGRI
VRYELIPLEKLGRPRIDVVVTLSGIFRDLFVNQMELLDRAVKLAADADEPEEMNFVRKHALAQAAEMGID
VEEAAARIFSNAPGSYGSNVNDLVENSAWEDEGELADTFIRRKSFAYGRQGKGEQRPEILQSALKTVDRT
FQNIDSVEIGLTDIDHYFDSLGGLSKAVERQSGKTAPAVYVEDTTKDGKGQVRNLEELVRLEYRTKLLNP
KWYEGMLSHGYEGVREISQRVTNTMGWSATAGAVDNWVYQQATETYALDPEMRERLAQLNPNAFRNIVSR
LLEAHGRGYWEADPDKLEKLQELYEELEDRLEGV
>gnl|CDD|131081 TIGR02026, BchE, magnesium-protoporphyrin IX monomethyl ester anaerobic oxidative cyclase. This model represents the cobalamin-dependent oxidative cyclase, a radical SAM enzyme responsible for forming the distinctive E-ring of the chlorin ring system under anaerobic conditions. This step is essential in the biosynthesis of both bacteriochlorophyll and chlorophyll under anaerobic conditions (a separate enzyme, AcsF, acts under aerobic conditions). This model identifies two clades of sequences, one from photosynthetic, non-cyanobacterial bacteria and another including Synechocystis and several non-photosynthetic bacteria. The function of the Synechocystis gene is supported by gene clustering with other photosynthetic genes, so the purpose of the gene in the non-photosynthetic bacteria is uncertain. Note that homologs of this gene are not found in plants which rely solely on the aerobic cyclase
RILILNPNYHAGGAEIAGQWPPLWVAYIGGALLDAGYHDVTFLDAMTGPLTDEKLVERLRAHCPDLVLIT
AITPAIYIACETLKFARERLPNAIIVLGGIHPTFMFHQVLTEAPWIDFIVRGEGEETVVKLIAALENHNF
AEDRNKVDGIAFLRDQEIVETLAAPMIQDLDVYRPDWELVDWKKYIYYPLGVRVAVPNFARGCPFTCNFC
SQWKFWRRYRHRDPKKFVDEIEWLVRTHGVGFFILADEEPTINRKKFQEFCEEIIARNPISVTWGINTRV
TDIVRDADILHLYRRAGLVHISLGTEAAAQATLDHFRKGTTTSTNKEAIRLLRQHNILSEAQFITGFENE
TDETFEETYRQLLDWDPDQANWLMYTPWPFTSLFGELSDRVEVQDYTKYNFVTPIMKPTHMPRWEILLGV
KLNYIRFYMRKALWRYPFQPNKFSRRYMLGCLKAFLKAGVGRWFYDLGRRVLVGSKELIDFFFDERRVKN
GPQLAEF
>gnl|CDD|273934 TIGR02027, DNA-directed_RNA_polymerase_subunit_alpha, DNA-directed RNA polymerase, alpha subunit, bacterial and chloroplast-type. This family consists of the bacterial (and chloroplast) DNA-directed RNA polymerase alpha subunit, encoded by the rpoA gene. The RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. The amino terminal domain is involved in dimerizing and assembling the other RNA polymerase subunits into a transcriptionally active enzyme. The carboxy-terminal domain contains determinants for interaction with DNA and with transcriptional activator proteins [Transcription, DNA-dependent RNA polymerase]
YGKFVLEPLERGFGITLGNALRRVLLSSIPGAAITAVKIDGVLHEFSTIEGVKEDVTEIILNLKQLVVKS
EGDGERTMTLSKKGPGVVTAGDIKAPPGDVEIVNPDLVIATLTEPADLEIELRVERGRGYVPAEENREED
RPVGVIAVDAIFSPVLKVNYEVENTRVGQRTDYDKLILEIETNGSITPKDAIAEAAKILIEHLEPFVNLD
EEIEAFEEEQEEEEEELEDAKLLSIKIEELDLSVRSYNCLKRAGIHTLGELVSKSEEELLKIKNFGKKSL
TEIKEKLAELGLELGMD
>gnl|CDD|131083 TIGR02028, geranylgeranyl_reductase_partial, geranylgeranyl reductase. This model represents the reductase which acts reduces the geranylgeranyl group to the phytyl group in the side chain of chlorophyll. It is unclear whether the enzyme has a preference for acting before or after the attachment of the side chain to chlorophyllide a by chlorophyll synthase. This clade is restricted to plants and cyanobacteria to separate it from the homologues which act in the biosynthesis of bacteriochlorophyll [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
LRVAVVGGGPAGASAAETLASAGIQTFLLERKPDNAKPCGGAIPLCMVDEFALPRDIIDRRVTKMKMISP
SNIAVDIGRTLKEHEYIGMLRREVLDSFLRRRAADAGATLINGLVTKLSLPADADDPYTLHYISSDSGGP
SGTRCTLEVDAVIGADGANSRVAKEIDAGDYSYAIAFQERIRLPDEKMAYYDDLAEMYVGDDVSPDFYGW
VFPKCDHVAVGTGTVAAKPEIKRLQSGIRARAAGKVAGGRIIRVEAHPIPEHPRPRRVVGRVALVGDAAG
YVTKCSGEGIYFAAKSGRMCAEAIVEESRLGGAVTEEGDLAGYLRRWDKEYRPTYRVLDLLQRVFYRSNA
GREAFVEMCADEHVQKRTFDSYLYKRVAPAEPLGDLKLLWRTIGSLVR
>gnl|CDD|131084 TIGR02029, conserved_hypothetical_protein, magnesium-protoporphyrin IX monomethyl ester aerobic oxidative cyclase. This model respresents the oxidative cyclase responsible for forming the distinctive E-ring of the chlorin ring system under aerobic conditions. This enzyme is believed to utilize a binuclear iron center and molecular oxygen. There are two isoforms of this enzyme in some plants and cyanobacterai which are differentially regulated based on the levels of copper and oxygen. This step is essential in the biosynthesis of both bacteriochlorophyll and chlorophyll under aerobic conditions (a separate enzyme, BchE, acts under anaerobic conditions). This enzyme is found in plants, cyanobacteria and other photosynthetic bacteria [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
KKGTKTASQETLLTPRFYTTDFEEMANLDVSPVENEWDAMLAEMKADYNRHHFVRNEEFDQSWEHIDGEL
RQAFIEFLERSCTSEFSGFLLYKELSRRLKNRDPVVAELFQLMARDEARHAGFLNKALGDFGLALDLGFL
TKTRKYTFFRPKFIYYATYLSEKIGYWRYITIYRHLEENPENQFYPIFKYFESWCQDENRHGDAFAALMR
SQPQLLNNWKAKLWSRFFLLSVYSTMYLRDHQRPGFYEALGLDATDFDLQVFRNTNETSGRIFPMTLNTE
HPRFRRLLDRMAGYSEKISAIEASGGPKFIKLIRRLPLMAAIAWNFLMVYLIPPKDT
>gnl|CDD|131085 TIGR02030, Magnesium-chelatase_subunit_ChlI, magnesium chelatase ATPase subunit I. This model represents one of two ATPase subunits of the trimeric magnesium chelatase responsible for insertion of magnesium ion into protoporphyrin IX. This is an essential step in the biosynthesis of both chlorophyll and bacteriochlorophyll. This subunit is found in green plants, photosynthetic algae, cyanobacteria and other photosynthetic bacteria [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
FPFTAIVGQDEMKLALLLNVIDPKIGGVMVMGDRGTGKSTAVRALAALLPEIKAVAGCPFNSSPSDPEMM
CEEVRIRVDSQEPLSIIKKPVPVVDLPLGATEDRVCGTLDIERALTEGVKAFEPGLLARANRGILYIDEV
NLLEDHLVDVLLDVAASGWNVVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGLHAEIRTVRDVEL
RVEIVERRTEYDADPHAFCEKWQTEQEALQAKIVNAQNLLPQVTIPYDVLVKVAELCAELDVDGLRGELT
LNRAAKALAAFEGRTEVTVDDIRRVAVLALRHRLRKDPLESIDSGSRVERVVKEVLG
>gnl|CDD|273935 TIGR02031, Magnesium-chelatase_67_kDa_subunit, magnesium chelatase ATPase subunit D. This model represents one of two ATPase subunits of the trimeric magnesium chelatase responsible for insertion of magnesium ion into protoporphyrin IX. This is an essential step in the biosynthesis of both chlorophyll and bacteriochlorophyll. This subunit is found in green plants, photosynthetic algae, cyanobacteria and other photosynthetic bacteria. Unlike subunit I (TIGR02030), this subunit is not found in archaea [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
ERAKLALTLLAVDPSLGGVAIRARAGTGKTALARALAEILPPIMPFVELPLGVTEDRLIGGIDVEESLAG
GQRVTQPGLLDEAPRGVLYVDMANLLDDGLSNRLLQALDEGVVIVEREGISVVHPAKFALIATYDPAEGG
GGLPDHLLDRLALHVSLEDVASQDLRVEIVRRERCNEVFRMNDELELLRGQIEAARELLPQVTISAEQVK
ELVLTAASLGISGHRADLFAVRAAKAHAALHGRTEVTEEDLKLAVELVLLPRATRLPEPEPQPPPPPPPP
EPPEPEEEPDEPDQTDPDDGEETDQIPEELMFDAVEADLPDNILATLQTVQRRRGRAGGEQKSNHRGRPL
RSRLGKPGSGARVDLVATLRAAAPWQRLRREENPAGTRGLIVEASDIRIKRYRRKSGRLLIFVVDASGSA
AVARMSEAKGAVELLLGEAYVHRDQVSLIAFRGTAAEVLLPPSRSVEQAKRRLDVLPGGGGTPLAAGLAA
AFQTALQARSSGGTPTIVLITDGRGNIPLDGDPESIKADREQAAEEALALARKIREAGMPALVIDTAMRF
VSTGFAQKLARKMGAHYIYLPNATAASIA
>gnl|CDD|273936 TIGR02032, Uncharacterized_protein_MJ1520, geranylgeranyl reductase family. This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRYKPCGGALSPRALEELDLPGELIVNLVRGARFFS
PNGDSVEIPIETELAYVIDRDAFDEQLAERAQEAGAELRLGTRVLDVEIHDDRVVVIVRGSEGTVTAKIV
IGADGSRSIVAKKLGLKKEPREYGVAARAEVEMPDEEVDEDFVEVYIDRGIVPGGYGWVFPKGDGTANVG
VGSRSAEEGEDPKKYLKDFLARRPELKDAETVEVCGALIPIGRPDEKLVRGNVLLVGDAAGHVNPLTGEG
IYYAMRSGDIAAEVV
>gnl|CDD|273937 TIGR02033, putative_dihydropyrimidine, D-hydantoinase. This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme
LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTA
DDFFTGTKAAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEV
KEEGINSFKVFMAYKNLLMVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALS
RPPELEAEAVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDKPGFE
GAKYVCSPPLREPEDQDALWSALSSGALQTVGSDHCTFNFAQKKAIGKDDFTKIPNGGPGVEERMSLLFD
EGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPNRTTVISAETHHSNADYNPFEGF
KVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR
>gnl|CDD|213679 TIGR02034, Includes:_Sulfate_adenylyltransferase_subunit_1, sulfate adenylyltransferase, large subunit. Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase) [Central intermediary metabolism, Sulfur metabolism]
LRFLTCGSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTQGGEIDLALLVDGLQAEREQGITIDV
AYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAV
NKMDLVDYDEEVFENIKKDYLAFAEQLGFRDVTFIPLSALKGDNVVSRSESMPWYSGPTLLEILETVEVE
RDAQDLPLRFPVQYVNRPNLDFRGYAGTIASGSVHVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAV
TLTLDDEIDISRGDLLAAADSAPEVADQFAATLVWMAEEPLLPGRSYDLKLGTRKVRASVAAIKHKVDVN
TLEKGAAKSLELNEIGRVNLSLDEPIAFDPYAENRTTGAFILIDRLSNRTVGAGMI
>gnl|CDD|211710 TIGR02035, Probable_D-serine_dehydratase, D-serine ammonia-lyase. This family consists of D-serine ammonia-lyase (EC 4.3.1.18), a pyridoxal-phosphate enzyme that converts D-serine to pyruvate and NH3. This enzyme is also called D-serine dehydratase and D-serine deaminase and was previously designated EC 4.2.1.14. It is homologous to an enzyme that acts on threonine and may itself act weakly on threonine [Energy metabolism, Amino acids and amines]
LIAQYPLIKDLIALKEVTWFNPGTTSLAEGLPYVGLTAQDVADAEARLQRFAPYIAKVFPETAATGGIIE
SPLVEIPAMQKRLEKEYQQPIPGRLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSI
LAEPEFKQFFSRYSIAVGSTGNLGLSIGIISAALGFQVTVHMSADARQWKKDKLRSHGVTVVEYESDYGV
AVEEGRKAAQSDPNCYFIDDENSRTLFLGYAVAASRLKAQFDQQGIIVDAEHPLFVYLPCGVGGGPGGVA
FGLKLAFGDHVHCFFAEPTHSPCMLLGVYTGLHEQISVQDIGIDNLTAADGLAVGRPSGFVGRAMERLLD
GFYTVDDQTLYDLLGWLAQSEGIRLEPSALAGMAGPVRVCASEVSYRYMHGFSAEQLRNATHLVWATGGG
MVPEEEMNAYL
>gnl|CDD|131091 TIGR02036, HTH-type_transcriptional_regulator_DsdC, D-serine deaminase transcriptional activator. This family, part of the LysR family of transcriptional regulators, activates transcription of the gene for D-serine deaminase, dsdA. Trusted members of this family so far are found adjacent to dsdA and only in Gammaproteobacteria, including E. coli, Vibrio cholerae, and Colwellia psychrerythraea [Regulatory functions, DNA interactions]
RNRRLNSFQLSKMHTFEVAARHQSFSLAAEELSLTPSAISHRINQLEEELGIQLFVRSHRKVELTHEGKR
IYWALKSSLDTLNQEILDIKNQELSGTLTLYSRPSFAQCWLVPRIGDFTRRYPSISLTVLTGNENINFQG
AGIDVAIYFDDAPPAKLTCHFIMDETILPVCSPEYAQRHALTNTVINLCHCTLLHDNQAWSYDSGTDEWH
SWANHYAVNNLPTSSGIGFDRSDLAVIAAMNNAGVAMGRKSLVQKRLASGELVAPFGDMTVKCHQRYYVA
TLPNRQNPKIELFIIWLREQVK
>gnl|CDD|273938 TIGR02037, Probable_periplasmic_serine_protease_do/HhoA-like, periplasmic serine protease, Do/DeqQ family. This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]
PSFAPLVEKVAPAVVNISVEGTVKRRNRPPALPPFFRQFFGDDMPDFPRQQREQKVRGLGSGVIISADGY
VLTNNHVVDGADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGN
PFGLGQTVTSGIVSALGRSGLGIGDYENFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIG
FAIPSNMAKNVVDQLIEGGKVKRGWLGVTIQEVTSDLAKSLGLEKQRGALVAQVLPGSPAEKAGLKAGDV
ITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRKGKEKTITVTLGASPEEQASSSNPFLGLTVANLSPE
IRKELRLKGDVKGVVVTKVVSGSPAARAGLQPGDVILSVNQQPVSSVAELRKVLARAKKGGRVALLILRG
GATIFVTL
>gnl|CDD|273939 TIGR02038, Protease_degS_precursor., periplasmic serine pepetdase DegS. This family consists of the periplasmic serine protease DegS (HhoB), a shorter paralog of protease DO (HtrA, DegP) and DegQ (HhoA). It is found in E. coli and several other Proteobacteria of the gamma subdivision. It contains a trypsin domain and a single copy of PDZ domain (in contrast to DegP with two copies). A critical role of this DegS is to sense stress in the periplasm and partially degrade an inhibitor of sigma(E) [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]
LKKLGRSVLFGLIAAAMILLVTPSLRNKNLGNSLLQNRGNNTVEISFNKAVRRAAPAVVNIYNRSISQNS
LNQLSIQGLGSGVIMSKEGYILTNYHVIKKADQIVVALQDGRKFEAELVGSDPLTDLAVLKIEGDNLPTI
PVNLDRPPHVGDVVLAIGNPYNLGQTITQGIISATGRNGLSSVGRQNFIQTDAAINAGNSGGALINTNGE
LVGINTASFQKGGDEGGEGINFAIPIKLAHKIMGKIIRDGRVIRGYIGVSGEDINSVVAQGLGLPDLRGI
VITGVDPNGPAARAGILVRDVILKYDGKDVIGAEELMDRIAETRPGSKVMVTVLRQGKQLELPVTIDEKP
V
>gnl|CDD|131094 TIGR02039, Sulfate_adenylyltransferase_subunit_2, sulfate adenylyltransferase, small subunit. Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules [Central intermediary metabolism, Sulfur metabolism]
LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDH
MVAKYGLRLIVHSNEEGIADGINPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERI
FSFRNAFHQWDPKKQRPELWNLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQ
RDGMLIMVDDVRMPLAPGEVVKERMVRFRTLGCYPLTGAIESDAATVEEIIAETAAARTSERQGRAIDRD
QAASMEDKKREGYF
>gnl|CDD|273940 TIGR02040, transcriptional_regulator_AerR_aerR, transcriptional regulator PpsR. This model represents the transcriptional regulator PpsR which is strictly associated with photosynthetic proteobacteria and found in photosynthetic operons. PpsR has been reported to be a repressor. These proteins contain a Helix-Turn_Helix motif of the "fis" type (pfam02954) [Energy metabolism, Photosynthesis, Regulatory functions, DNA interactions]
LLATAADVTLLLDAEGVVREVAANPHHPSFEQLSEWEGRRWEEIVTAESVEKFELRLSEALRTGRGAVRV
ELNHIDPSSFELPMRFILVRLGADRGVLALGRDLRAVAELQQQLVAAQQAMERDYWTLREMETRYRVVLE
VSSDAVLLVDMSTGRIVEANSAAAALLGGVGQSLVGRAFPQEFEGRRREELMLTLRNVRATGSAAPVRIL
LRRSQKRLLVVVSVFRQDGESLFLCQLSPAGATQPVGDELSENLARLYHEAPDAIVFSDADGTIRGANEA
FLELTDSSSLEAVRGRTLDRWLGRGGVDLRVLLSNVRRTGQVRLYATTLTGEFGAQTEVEISAAWVDQGE
RPLIVLVIRDISRRLTMRDVPATGVLPRSARQLTELVGRSPLKDLVRETTDVVEQLCIEAALELTRDNRA
SAAEILGLSRQSLYVKLRRYGL
>gnl|CDD|273941 TIGR02041, Sulfite_reductase_hemoprotein_beta-component, sulfite reductase (NADPH) hemoprotein, beta-component. Sulfite reductase (NADPH) catalyzes a six electron reduction of sulfite to sulfide in prokaryotic organisms. It is a complex oligomeric enzyme composed of two different peptides with a subunit composition of alpha(8)-beta(4). The alpha component, encoded by cysJ, is a flavoprotein containing both FMN and FAD, while the beta component, encoded by cysI, is a siroheme, iron-sulfur protein. In Salmonella typhimurium and Escherichia coli, both the alpha and beta subunits of sulfite reductase are located in a unidirectional gene cluster along with phosphoadenosine phosphosulfate reductase, which catalyzes a two step reduction of PAPS to give free sulfite. In cyanobacteria and plant species, sulfite reductase ferredoxin (EC 1.8.7.1) catalyzes the reduction of sulfite to sulfide [Central intermediary metabolism, Sulfur metabolism]
ERIKEESNYLRGTILEDLADPLTGGFKGDNFQLIRFHGMYQQDDRDLRAERAEQKLEPRYAMMLRCRLPG
GVITPKQWLAIDKFAREYTNYGSIRLTNRQTFQFHGILKKNLKPVHQMLHSVGLDSLATAGDVNRNVLCT
SNPYESELHAEAYEWAKKISEHLLPRTRAYAEIWLDQEKVAGTEEVEPILGPTYLPRKFKTTVVIPPQND
VDVYANDLGFVAIAENGKLVGFNVLIGGGLSMEHGNKKTYPRLASEIGFIPPEHTLAVAEAVVTTQRDFG
NRTDRKNARTKYTIERMGLDTFKAEVERRAGIKFEPARPYEFTGRGDRIGWVKGIDGNWHLTLFIENGRI
LDYPDKPLKTGLLEIAKIHKGDFRITANQNLIIAGVPEGGKAKIEKLARQYGLINAVTALRENSMACVSF
PTCPLAMAEAERYLPDFIDKLDNIMAKHGLSDEEIVLRVTGCPNGCGRAMLAEIGLVGKAPGRYNLHLGG
NRIGTRIPRLYKENITEPEILAELDELIGRWAKERKPGEGFGDFLIRAGII
>gnl|CDD|131097 TIGR02042, Sulfite_reductase, ferredoxin-sulfite reductase. Distantly related to the iron-sulfur hemoprotein of sulfite reductase (NADPH) found in Proteobacteria and Eubacteria, sulfite reductase (ferredoxin) is a cyanobacterial and plant monomeric enzyme that also catalyzes the reduction of sulfite to sulfide [Central intermediary metabolism, Sulfur metabolism]
AKPQKRSKVEILKERSNFLREPLNEQLLEEATHFNEDAVQILKFHGSYQQDNRDNRGKGQEKDYQFMLRT
KNPGGYVPPQLYLTLDDLADEYGNGTLRATTRQTFQLHGILKKNLKTVISTIVKNLGSTLGACGDLNRNV
MAPPAPFRKRPEYEFAREYADNIADLLTPQSGAYYELWLDGEKVMSAEPDPEVVAARNDNSHGTNFADSP
EPLYGTQYLPRKFKIAVTVPGDNSIDLFTQDIGLVVVSNERGELEGFNIYVGGGMGRTHNKEETFARLAD
PLGYVPKEDIYYAVKAIVATQRDYGDRDDRRHARMKYLISDWGIEKFREVVEQYFGKKIAPVRELPEFEY
KDYLGWHEQGDGKWFLGLHIDSGRVKDDGNWQLKKALREIVEKYNLPVRLTPNQNIILYDIQPEWKRAIT
TVLAQRGVLQPEAIDPLNRYAMACPALPTCGLAITESERAIPGILKRIRALLEKVGLPDEHFVVRMTGCP
NGCARPYMAELGFVGSAPNSYQVWLGGSPNQTRLARPFIDKLKDGDLEKVLEPLFVHFKQSRQSGESFGD
FCDRVGFDALREFVESY
>gnl|CDD|131098 TIGR02043, transcriptional_regulator_MerR_family, Zn(II)-responsive transcriptional regulator. This model represents the zinc and cadmium (II) responsive transcriptional activator of the gamma proteobacterial zinc efflux system. This protein is a member of the MerR family of transcriptional activators (pfam00376) and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-Cys-X(8-9)-Cys, as well as a conserved and critical cysteine at the N-terminal end of the dimerization helix [Regulatory functions, DNA interactions]
MFQIGELAKLCGVTSDTLRFYEKNGLIKPAGRTDSGYRLYTDEDQKRLRFILKAKELGFTLDEIKELLSI
KLDATEHSCAEVKAIVDAKLELVDEKINELTKIRRSLKKLSDACCGHTNDASHCSILEALE
>gnl|CDD|131099 TIGR02044, HTH-type_transcriptional_regulator_CueR, Cu(I)-responsive transcriptional regulator. This model represents the copper-, silver- and gold- (I) responsive transcriptional activator of the gamma proteobacterial copper efflux system. This protein is a member of the MerR family of transcriptional activators (pfam00376) and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X7-Cys. This family also lacks a conserved cysteine at the N-terminal end of the dimerization helix which is required for the binding of divalent metals such as zinc; here it is replaced by a serine residue [Regulatory functions, DNA interactions]
MNIGQVAKLTGLSSKMIRYYEEKGLIPPPLRSEGGYRTYTQQHLDELRLISRARQVGFSLEECKELLNLW
NDPNRTSADVKARTLEKVAEIERKISELQSMRDQLEALAQACPGDDSPDCPIIENLS
>gnl|CDD|131100 TIGR02045, ADP-specific_phosphofructokinase, ADP-specific phosphofructokinase. Phosphofructokinase is a key enzyme of glycolysis. The phosphate group donor for different subtypes of phosphofructokinase can be ATP, ADP, or pyrophosphate. This family consists of ADP-dependent phosphofructokinases. Members are more similar to ADP-dependent glucokinases (excluded from this family) than to other phosphofructokinases [Energy metabolism, Glycolysis/gluconeogenesis]
GIFTAYNTNVDAIVYLNEEDVQKLVDEFGEDDIQDRMEEYPREINEPLDFVARLVHSLKTGKPAEVPLVN
EELHEWFDEHFKYDYERMGGQAGIISNLLGRLGLKKVIAYTPFLSKRQAEMFVATGNILYPVVENGKLVL
KPPGEAYREGDPSKVNRIFEFRKGTNFKLGGETIKVPRSGRFIVSSRPESLRIETKDQLRKFLPEIGEPV
DGAILSGYQGIKEEYSDGKTAKYYLERAKEDIELLKKNKDLKIHVEFASIQNREIRKKVVTNIFPHVDSV
GMDEAEIANVLSVLGYDELSDRIFRYNRIEDLILGAKILLDELNLEVVQVHTIYYIMYITHADNPLSEEE
LRRSLEFSTILAATRASLGNIENPDDAEAGLEVPYNERGDLEKLRFEEAKRKLRTKEYKAVLIPSRLVEN
PKSTVGLGDTISTGAFVSYLALLKQK
>gnl|CDD|131101 TIGR02046, Succinate_dehydrogenase_cytochrome_b558_subunit, succinate dehydrogenase (or fumarate reductase) cytochrome b subunit, b558 family. This family consists of the succinate dehydrogenase subunit C of Bacillus subtilis, designated cytochrome b-558, and related sequences that include a fumarate reductase subunit C. This subfamily is only weakly similar to the main group of succinate dehydrogenase cytochrome b subunits described by pfam01127, so that some members score above the gathering threshold and some do not [Energy metabolism, TCA cycle]
SSIGRKVVMALTGLVLLLFLVVHMVGNLFALFGAEAFNAAAHFLRSLPFRLWLERIILFVPFILHAVYAV
ILSIRNKRNARPYRYMHKGRPGVSWASRTMRVTGIIVLIFIGWHVLDFTIGAQMGEIFHMGVARHDGYDM
VVLTFSSPIMLSIYIVAMLALGFHLSHGLWSAAQTLGLNVTPRSQRIKTISNVVALVIFGGFSAVPLKFI
LGFV
>gnl|CDD|131102 TIGR02047, putative_regulatory_protein, Cd(II)/Pb(II)-responsive transcriptional regulator. This model represents the cadmium(II) and/or lead(II) responsive transcriptional activator of the proteobacterial metal efflux system. This protein is a member of the MerR family of transcriptional activators (pfam00376) and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X(6-9)-Cys, as well as a conserved and critical cysteine at the N-terminal end of the dimerization helix [Regulatory functions, DNA interactions]
MKIGELAQKTGVSVETIRFYEKQGLLPPPARTDNNYRVYTVGHVERLAFIRNCRTLDMSLAEIRQLLRYQ
DKPEKSCSDVNALLDEHISHVRARIIKLQALIEQLVDLRGRCNGLCTVEQCGVLQNL
>gnl|CDD|131103 TIGR02048, gshA_cyano, glutamate--cysteine ligase, cyanobacterial, putative. This family consists of proteins believed (see Copley SD, Dhillon JK, 2002) to be the glutamate--cysteine ligases of several cyanobacteria, which are known to make glutathione [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
LTKGFEVEIYTGKPTGEIVGLSDRIVRDLSGFVREPDSRNVEYTTPPLNSYDRLLCGLLRPRRQLRHYLS
QLGDYTLIPGSTLSLGGTDRFYRSDPQNPYHTYIEQTYGTQVVTASVHINIGIPDPEELMRACRLVRMEA
PLFLALSASSPFLDGQVTGYHSTRWQMFPKTPQEVPLFTSHAHFIEWTEEQLTLGTMQNVRHLWSAVRPN
GDRRPYDLNRLELRICDLVTDPISLLAITALLEARLLQLLADPDLDPLQQSQLTPEELLALADQNEISAA
VSSLDATLTHWRDGRAIAAREWIEELYQEVWLIAKYQGFSCFLPPLRKILREGNQAQQWLTQYEQGKTPQ
TIVQQAILQTEMEEAELAQDLCLPLS
>gnl|CDD|273942 TIGR02049, putative_gamma-glutamylcysteine_synthetase, glutamate--cysteine ligase, T. ferrooxidans family. This family consists of a rare family of glutamate--cysteine ligases, demonstrated first in Thiobacillus ferrooxidans and present in a few other Proteobacteria. It is the first of two enzymes for glutathione biosynthesis. It is also called gamma-glutamylcysteine synthetase [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
EIKILDLEKSIERWFRAQWQGHTPPFYSSVDLRNAGYKIAPVDTNLFPAGFNNLNPEFRPLAARAIQSYF
KRHCPGAKKVLIIPENHTRNKFYLENVARLEEILRLAGLEVRLGSLYNEVYTVLDLPYGTVLLLEPLLRD
DRRLTTDGFDPCVILLNNDLSAGIPDILKGIKQDILPPLHAGWHSRRKSNHFEAYQEVASEFAKLIGIDP
WLINPYFEKCDGIDFDDREGEDALATAVDQVLSKTQKKYEEYGIHTQPYVIVKADAGTYGMGIMTATSGE
EVLGLNRKERNKMAKVKEGLEVSEVIIQEGVYTFEMFNEAVAEPVVYMIGRTVTGGFYRVHTGRGVDENL
NAPGMHFVPLSFGSTVLPCSVVEPDAPANRLYLYGVVARLALLAAAVEIKSFH
>gnl|CDD|273943 TIGR02050, Hypothetical_protein_Rv0433/MT0448/Mb0441., carboxylate-amine ligase, YbdK family. This family represents a division of a larger family, the other branch of which is predicted to act as glutamate--cysteine ligase (the first of two enzymes in glutathione biosynthesis) in the cyanobacteria. Species containing this protein, however, are generally not believe to make glutathione, and the function is unknown
TLGVEEELLLVDPHTYDLAASASAVLIGACREKIGAGFKHELFESQVELATPVCTTLAEAAAQIRAVRAR
LVQAASDHGLRICGAGTHPFARWRRQEVADNPRYQRLLERYGYVARQQLVFGLHVHVGVPSPDDAVAVLN
RLLPWLPHLLALSASSPFWQGFDTGYASYRRNIFQAWPTAGLPPAFGSWDAFEAYFADLLETGVIDDDGD
LWWDIRPSPHFGTVEVRVADTCLNLEHAVAIAALIRALVEWLLREWPAPFPVPELDYWLLQENKWRAARY
GLDAEII
>gnl|CDD|131106 TIGR02051, Mercuric_resistance_operon_regulatory_protein, Hg(II)-responsive transcriptional regulator. This model represents the mercury (II) responsive transcriptional activator of the mer organomercurial resistance operon. This protein is a member of the MerR family of transcriptional activators (pfam00376) and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X(8)-Cys-Pro, as well as a conserved and critical cysteine at the N-terminal end of the dimerization helix [Cellular processes, Detoxification, Regulatory functions, DNA interactions]
TIGELAKAAGVNVETIRYYERKGLLPEPDRPEGGYRRYPEETVKRLRFIKRAQELGFSLEEIGGLLGLVD
GTHCREMYELASRKLKSVQAKMADLLRIERLLEELLEQCPANKGNTSCPIIESL
>gnl|CDD|131107 TIGR02052, periplasmic_mercuric_ion_binding_protein, mercuric transport protein periplasmic component. This model represents the periplasmic mercury (II) binding protein of the bacterial mercury detoxification system which passes mercuric ion to the MerT transporter for subsequent reduction to Hg(0) by the mercuric reductase MerA. MerP contains a distinctive GMTCXXC motif associated with metal binding. MerP is related to a larger family of metal binding proteins (pfam00403) [Cellular processes, Detoxification]
MKKLATLLALFVLTSLPAWAATQTVTLEVPGMTCVACPITVETALQKVDGVSKAEVTFKTKLAVVTFDDE
KTNVKALTEATTDAGYPSSLKQ
>gnl|CDD|273944 TIGR02053, Mercuric_reductase, mercury(II) reductase. This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH [Cellular processes, Detoxification]
YDLVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAAT
VAVDFGELLEGKREVVEELRHEKYEDVLSSYGVDYLRGRARFKDPKTVKVDLGREVRGAKRFLIATGARP
AIPPIPGLKEAGYLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEIS
AAVEEALAEEGIEVVTSAQVKAVSVRGGGKIITVEKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKL
DERGGILVDETLRTSNPGIYAAGDVTGGLQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVA
SVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALA
IRAGMTVDDLIDTLHPFPTMAEGLKLAAQTFYRDVSKLSCCAG
>gnl|CDD|131109 TIGR02054, HTH-type_transcriptional_regulator_MerD, mercuric resistence transcriptional repressor protein MerD. This model represents a transcriptional repressor protein of the MerR family (pfam00376) whose expression is regulated by the mercury-sensitive transcriptional activator, MerR. MerD has been shown to repress the transcription of the mer operon [Cellular processes, Detoxification]
MNAYTISRLAEDAGVSVHVVRDYLLRGLLHPVRRTTSGYGIFDDASLQRLRFVRAAFEAGIGLGELARLC
RALDAANGDDTAACLAVLRQLVEARREALAALEVQLAAMPTAAAQHSESA
>gnl|CDD|273945 TIGR02055, Phosphoadenosine_phosphosulfate_reductase, thioredoxin-dependent adenylylsulfate APS reductase. This model describes recently identified adenosine 5'-phosphosulfate (APS) reductase activity found in sulfate-assimilatory prokaryotes, thus separating it from the traditionally described phosphoadenosine 5'-phosphosulfate (PAPS) reductases found in bacteria and fungi. Homologous to PAPS reductase in enterobacteria, cyanobacteria, and yeast, APS reductase here clusters with, and demonstrates greater homology to plant APS reductase. Additionally, the presence of two conserved C-terminal motifs (CCXXRKXXPL & SXGCXXCT) distinguishes APS substrate specificity and serves as a FeS cluster [Central intermediary metabolism, Sulfur metabolism]
LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDILIDVLSPPPLTVEEQVKEYGLNLF
YRSVPHECCGIRKVEPLKRALAGVSAWITGLRRDQSPTRAQAPFLEIDEAFGLVKINPLADWTSEDVWEY
IADNELPYNPLHDRGYPSIGCEPCTRPVAPGEDPRAGRWWWEEAAKKECGL
>gnl|CDD|131111 TIGR02056, chlorophyll_synthase_33_kD_subunit, chlorophyll synthase, ChlG. This model represents the strictly cyanobacterial and plant-specific chlorophyll synthase ChlG. ChlG is the enzyme (esterase) which attaches the side chain moiety onto chlorophyllide a. Both geranylgeranyl and phytyl pyrophosphates are substrates to varying degrees in enzymes from different sources. Thus, ChlG may act as the final or penultimate step in chlorophyll biosynthesis (along with the geranylgeranyl reductase, ChlP) [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
QLLGIKGAAPGETNIWKIRLQLMKPITWIPLIWGVVCGAAASGNFHWSLEDVAKAALCMLLSGPCLTGYT
QTINDFYDRDIDAINEPYRPIPSGAISEPEVITQIVLLFIAGIAIAFILDLWAGHEFPNVFVLALFGSFI
AFIYSAPPLKLKQNGWLGNFALGASYIALPWWAGHALFGELNPDIAVLTLIYSIAGLGIAIVNDFKSVEG
DRALGLQSLPVAFGIETAAWICVGAIDIFQGLIAAYLLAIGENLYAAALVALIIPQITFQDKYFLKDPLK
NDVKYQASAQPFLVLGIFVAALALGH
>gnl|CDD|131112 TIGR02057, Phosphoadenosine_phosphosulfate_reductase, phosphoadenosine phosphosulfate reductase, thioredoxin dependent. Requiring thioredoxin as an electron donor, phosphoadenosine phosphosulfate reductase catalyzes the reduction of 3'-phosphoadenylylsulfate (PAPS) to sulfite and phospho-adenosine-phosphate (PAP). Found in enterobacteria, cyanobacteria, and yeast, PAPS reductase is related to a group of plant (TIGR00424) and bacterial (TIGR02055) enzymes preferring 5'-adenylylsulfate (APS) over PAPS as a substrate for reduction to sulfite [Central intermediary metabolism, Sulfur metabolism]
LDELNEQLEKLTPQEIIAWSIVTFPHGLVQTSAFGIQALVTLHLLSSISEPMIPVIFIDTLYHFPQTLTL
KDELTKKYYQTLNLYKYDGCESEADFEAKYGKLLWQKDIEKYDYIAKVEPMQRALKELNASAWFTGRRRD
QGSARANLPVIEIDEQNGILKVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRKVKEGEDE
RAGRWKGKLKTECGIH
>gnl|CDD|131113 TIGR02058, lin0512_fam, conserved hypothetical protein. This family consists of few members, broadly distributed. It occurs so far in several Firmicutes (twice in Oceanobacillus), one Cyanobacterium, one alpha Proteobacterium, and (with a long prefix) in plants. The function is unknown. The alignment includes a perfectly conserved motif GxGxDxHG near the N-terminus [Hypothetical proteins, Conserved]
KILFIEMGMGVDQHGQNITKAAMRAVRNAIASNSMPGIWESLPDSSLNEMIVEVKLAVPYDLDQLDEDKV
KAIIPYGTVTVEVEDGGMITSSGIALEEKNDKNDLMYIVNAAVEVG
>gnl|CDD|131114 TIGR02059, swm_rep_I, cyanobacterial long protein repeat. This domain appears in 29 copies in a large (_10000 amino protein in Synechococcus sp. WH8102 associated with a novel flagellar system, as one of three different repeats. Similar domains are found in two different large (<3500) proteins of Synechocystis PCC6803
ATDITNNSTKDLTAPVLLFGSTSTAVATNGNLLVLTFNEPLADITNHAPTRDQFAVTVNGAPNTVTSVSL
GGSNTTITLTLAQVVEDGDEVTLSYTKNSAN
>gnl|CDD|131115 TIGR02060, adenylylsulfate_reductase_beta_subunit, adenosine phosphosulphate reductase, beta subunit. During dissimilatory sulfate reduction and sulfur oxidation, adenylylsulfate (APS) reductase catalyzes reversibly the two-electron reduction of APS to sulfite and AMP. Found in several bacterial lineages and in Archaeoglobales, APS reductase is a heterodimer composed of an alpha subunit containing a noncovalently bound FAD, and a beta subunit containing two [4Fe-4S] clusters. Described by this model is the beta subunit of APS reductase, sharing common evolutionary origin with other iron-sulfur cluster-binding proteins [Central intermediary metabolism, Sulfur metabolism]
MPTFVYPTKCDGCKAGEKTACVYICPNDLMHLDTEIMKAYNIEPDMCWECYSCVKACPQGAIDVRGYADF
APLGGSCRPMRDEEKIMWTVKFRNGKVMRFKFPIRTTPWGSITPFEGVPEPSNEDSELLFNE
>gnl|CDD|273946 TIGR02061, adenylylsulfate_reductase_alpha_subunit, adenosine phosphosulphate reductase, alpha subunit. During dissimilatory sulfate reduction or sulfur oxidation, adenylylsulfate (APS) reductase catalyzes reversibly the two-electron reduction of APS to sulfite and AMP. Found in several bacterial lineages and in Archaeoglobales, APS reductase is a heterodimer composed of an alpha subunit containing a noncovalently bound FAD, and a beta subunit containing two [4Fe-4S] clusters. Described by this model is the alpha subunit of APS reductase, sharing common evolutionary origin with fumarate reductase/succinate dehydrogenase flavoproteins [Central intermediary metabolism, Sulfur metabolism]
DLLIVGGGMGGCGAAFEAVYWGDKKGLKIVLVEKANLERSGAVAQGLSAINTYLGTRFGENNAEDYVRYV
RTDLMGLVREDLIFDMARHVDDSVHLFEEWGLPLWIKPEDGKYVREGRWQIMIHGESYKPIVAEAAKNAL
GDIFERIFIVKLLLDKNTPNRIAGAVGFNVRANEVHVFKAKTVIVAAGGAVNVYRPRSVGEGAGRAWYAV
WNAGSTYTMCAQAGAEMTQMENRFVPARFKDGYGPVGAWFLLFKAKATNGKGEEYCATNRAMLKPYEGRG
YAKPHVIPTCLRNHMMLREMREGRGPIYMDTKEALQDPFATDKKQQKHLEEEAWEDFLDMTVGQANLWAA
TNVDPEERGSEIMPTEPYLMGSHSGCCGIWVSGPEDWVPEEYKVRAAKVYNRMTTVEGLFTCGDGVGASP
HKFSSGSFTEGRIAAKAAVRWILDHKDFKPEFDATAEELKKEIYRPMENYEVYKNASTAPVVNPNYINPK
QGLMRLQKCMDEYGGGVTTYYMTNEALLDTGLKLMAMLEEDLEKLAARDLHELLRAWELYHRLWTVEAHM
QHILFRKETRWPGYYYRADFLGLDDENWKCFVNSKYDPATGETTIEKKPYYQII
>gnl|CDD|131117 TIGR02062, Exoribonuclease_2, exoribonuclease II. This family consists of exoribonuclease II, the product of the rnb gene, as found in a number of gamma proteobacteria. In Escherichia coli, it is one of eight different exoribonucleases. It is involved in mRNA degradation and tRNA precursor end processing [Transcription, Degradation of RNA]
DNPLLAQLKQQLHSQTPRVEGVVKATEKGFGFLEVDAQKSYFIPPPQMKKVMHGDKIIAVIHSEKERESA
EPEELIEPFLTRFVGKVQGKDDKLAIVPDHPLLKDAIPCRAAKGLNHEFQEGDWAVAELRRHPLKGDRSF
YAELTQYITFADDHLAPWWVTLARHNLEREEPDGVADEMLLDGLVREDLTALDFVTIDSESTKDMDDALF
AEALPNGKLQLIVAIADPTAYIAEGSKLDKAAKIRGFTNYLPGFNIPMLPRELSDDLCSLRANEVRPVLA
CRITISKDGNIEDKIEFFAATIKSKAKLVYDQVSDWLENTSDWQPESEEIAQQVRLLHQFCQARIEWRHT
HALVFKDRPDYRFILSEKGEVLDIVAEPRRIANRIVEEAMIIANICAARFLRDKLGFGIYNTHAGFDPAN
AENVVALLKTNGLHVDAEELATLDGFCKLRRELDAQETGYLDSRIRRYQSFAEISTEPGPHFGLGLEAYA
TWTSPIRKYGDMINHRLLKAVIKGETATRPQEDITVQLAERRRLNRIAERDVADWLYARFLADKAAKNTR
FAAEIVDISRGGMRVRLLENGAIAFIPAAFLHANREELVCNQENGTVQIKGETVYKIGDVIDVVLTEVRM
ETRSIIARP
>gnl|CDD|273947 TIGR02063, Ribonuclease_R, ribonuclease R. This family consists of an exoribonuclease, ribonuclease R, also called VacB. It is one of the eight exoribonucleases reported in E. coli and is broadly distributed throughout the bacteria. In E. coli, double mutants of this protein and polynucleotide phosphorylase are not viable. Scoring between trusted and noise cutoffs to the model are shorter, divergent forms from the Chlamydiae, and divergent forms from the Campylobacterales (including Helicobacter pylori) and Leptospira interrogans [Transcription, Degradation of RNA]
SPLRELILEFLKSKKGKPISLKELAKAFHLKGADEKKALRKRLRALEDDGLVKKNRRGLYALPESLKLVK
GTVIAHRDGFGFLRPEDDDEDDIFIPPRQMNGAMHGDRVLVRITGKPDGGDRFEARVIKILERANDQIVG
TFYIENGIGFVIPDDKRIYLDIFIPPEQILGAEEGDKVLVEITKYPDRNRPAIGKVVEILGHADDPGIDI
LIIIRKHGIPYEFPEEVLDEAAKIPEEVPEEEIKGRKDLRDLPFVTIDGEDAKDFDDAVYVEKLKDGNYK
LGVAIADVSHYVREGSALDKEALKRGTSVYLPDRVIPMLPERLSNGICSLNPNEDRLTLSCEMEIDKKGR
VKKYEFYEAVINSHARLTYNQVNDIIEGKDALDKKEPPLKEMLKNLFELYKILRKKRKKRGAIDFDSKEA
KIILDENGKPIDIVPRERGDAHKLIEEFMIAANETVAEHLEKAKLPFIYRVHERPSEEKLQNLREFLKTL
GITLKGGTSDKPQPKDFQKLLEKVKGRPEEELINTVLLRSMQQAKYSPENIGHFGLALEYYTHFTSPIRR
YPDLIVHRLIKKALFGGENTTTEKEREYLEAKLEEIAEHSSKTERRADEAERDVNDWKKAEYMSEKIGEE
FEGVISGVTSFGLFVELENNTIEGLVHISTLKDDYYVFDEKGLALVGERTGKVFRLGDRVKVRVVKADLD
TGKIDFELV
>gnl|CDD|273948 TIGR02064, Sulfite_reductase_dissimilatory-type_subunit_alpha, sulfite reductase, dissimilatory-type alpha subunit. Dissimilatory sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide, as the terminal reaction in dissimilatory sulfate reduction. It remains unclear however, whether trithionate and thiosulfate serve as intermediate compounds to sulfide, or as end products of sulfite reduction. Sulfite reductase is a multisubunit enzyme composed of dimers of either alpha/beta or alpha/beta/gamma subunits, each containing a siroheme and iron sulfur cluster prosthetic center. Found in sulfate-reducing bacteria, these genes are commonly located in an unidirectional gene cluster. This model describes the alpha subunit of sulfite reductase [Central intermediary metabolism, Sulfur metabolism]
LDQLEKGPWPSFVSEIKKTAAYRADYQVPVDPEDLLGVLELSYDERKTHWKGGIVSVFGYGGGVIGRYSD
QGEKFPGVAEFHTVRVAQPSGKFYSTDYLRQLCDVWEKYGSGLTNFHGQTGDIVFLGTQTPQLQEIFEEL
TNLGTDLGGSGSNLRTPESCVGPARCEFACYDTLKACYELTMEYQDELHRPAFPYKFKFKFSGCPNDCVA
AIARSDFAVIGTWKDDIKVDQEAVKAYIAGWGKFDIENEVVNRCPTKAISWDGSKELSIDNRECVRCMHC
INKMPKALHPGDERGVTILIGGKAPILDGAQMGWVVVPFVEAEEPYDEIKELVEKIIDWWDEEGKNRERI
GETIKRLGLQKFLEVIGIEPDPQMVKEPRTNPYIFFKVEDEVPGGWDADIAE
>gnl|CDD|131120 TIGR02065, Exosome_complex_component_Rrp41, archaeal exosome-like complex exonuclease 1. This family contains the archaeal protein orthologous to the eukaryotic exosome protein Rrp41. It is somewhat more distantly related to the bacterial protein ribonuclease PH. An exosome-like complex has been demonstrated experimentally for the Archaea in Sulfolobus solfataricus, so members of this family are designated exosome complex exonuclease 1, after usage in SwissProt [Transcription, Degradation of RNA]
KLILEDGVRLDGRKPDELRPIKIEAGVLKNADGSAYLEFGGTKILAAVYGPREAHPRHLQLPDRAVLRVR
YHMAPFSTDERKRPGPSRREIEISKVIREALEPAILLEQFPRTVIDVFIEVLQADGGTRCAGLTAASLAL
ADAGIPMRDLVVGVAVGKVDGVVVLDLSEEEDMYGEADMPVAIMPKTGEITLLQLDGDLTPDEFRQALDL
AVEGIKRIYEIQREALKKKY
>gnl|CDD|131121 TIGR02066, Sulfite_reductase_dissimilatory-type_subunit_beta, sulfite reductase, dissimilatory-type beta subunit. Dissimilatory sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide, as the terminal reaction in dissimilatory sulfate reduction. It remains unclear however, whether trithionate and thiosulfate serve as intermediate compounds to sulfide, or as end products of sulfite reduction. Sulfite reductase is a multisubunit enzyme composed of dimers of either alpha/beta or alpha/beta/gamma subunits, each containing a siroheme and iron sulfur cluster prosthetic center. Found in sulfate-reducing bacteria, these genes are commonly located in an unidirectional gene cluster. This model describes the beta subunit of sulfite reductase [Central intermediary metabolism, Sulfur metabolism]
VVKKNYGKWKYHEVVKPGVIKHVAESGDVIYTVKAGTPRLLSVDTLRKLCDIADKYSDGYLRWTIRNNVE
FLVSDESKIQPLIDELEEVGFPVGGTGDAVKGNIVHTQGWLHCHIPAIDASGIVKAVMDELYEYFTDHKL
PAMVRISLSCCANMCGGVHASDIAIVGIHRKPPKINHEAVRNVCEIPSVVAACPTGALKPRRDGKNKSLE
VDVEKCIYCGNCYTMCPAMPIFDPENDGAAIWVGGKLSNARVMPELSKVVVPWIPNNPPRWPELVAYVKK
ILEAWKANAKKHERLIEWVERIGWERFFELVGLPFTQHHIDDWRIAPYFYSTFRASTQFKF
>gnl|CDD|273949 TIGR02067, his_9_HisN, histidinol-phosphatase, inositol monophosphatase family. This subfamily belongs to the inositol monophosphatase family (pfam00459). The members of this family consist of no more than one per species and are found only in species in which histidine is synthesized de novo but no histidinol phosphatase can be found in either of the two described families (TIGR01261, TIGR01856). In at least one species, the member of this family is found near known histidine biosynthesis genes. The role as histidinol-phosphatase wsa first proven in Corynebacterium glutamicum [Amino acid biosynthesis, Histidine family]
LLAFAEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEE
GDAERVWVLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSS
CANLSDAVLFTTSPDLLDDPGNRPAFERLRRAARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALI
PVIEEAGGCFTDWDGKPAPDGGGAVAAGNAMLHDEALEILN
>gnl|CDD|273950 TIGR02068, Cyanophycin_synthetase, cyanophycin synthetase. Cyanophycin is an insoluble storage polymer for carbon, nitrogen, and energy, found in most Cyanobacteria. The polymer has a backbone of L-aspartic acid, with most Asp side chain carboxyl groups attached to L-arginine. The polymer is made by this enzyme, cyanophycin synthetase, and degraded by cyanophycinase. Heterologously expressed cyanophycin synthetase in E. coli produces a closely related, water-soluble polymer with some Arg replaced by Lys. It is unclear whether enzymes that produce soluble cyanophycin-like polymers in vivo in non-Cyanobacterial species should be designated as cyanophycin synthetase itself or as a related enzyme. This model makes the designation as cyanophycin synthetase. Cyanophycin synthesis is analogous to polyhydroxyalkanoic acid (PHA) biosynthesis, except that PHA polymers lack nitrogen and may be made under nitrogen-limiting conditions [Cellular processes, Biosynthesis of natural products]
EILKIRTLRGPNYWSIRPVIEMRVDIEDLEDFPSNEIPGFYERLVEWLPSLIEHYCSPGVRGGFLQRLRE
GTYMGHILEHVALELQNLAGMPVGFGRTRETATPGVYNVVVEYSHEQVGRYAGRLAVDLVRSAIDDGPFD
LEQALQRLRDLVADASLGPSTAAIVDEAEKRGIPYMRLSAGSLVQLGYGSRQKRIQATETDRTSAIAVEI
ACDKDLTKEILSDAGVPVPEGTVVQSAEDAWEAAQDLGYPVVIKPYDGNHGRGVTINILTRDEIESAYEA
AVEESSGVIVERFITGRDHRLLVVGGKVVAVAERVPAHVIGDGVHTIEELIEQINTDPLRGDGHDKPLTK
IRLDSTARLELAKQGLTLDSVPAKGRIVYLRATANLSTGGVAIDRTDEIHPENAATAVRAAKIIGLDIAG
VDIVTEDISRPLRDTDGAIVEVNAAPGLRMHLAPSQGKPRNVARAIVDMLFPAEDDGRIPIVSVTGTNGK
TTTTRLVAHILKQTGKVVGMTTTDGVYIGKYLVEKGDNTGPASARRILMDPTVDAAVLETARGGILREGL
AFDRCDVGVVTNIAGDHLGIGDINTIEDLADVKRVVVEVVLPDGYAVLNADDPMVAAMAEKCKGKIAYFS
MDPNNPTVAAHIADGGRAVYYENGYIVIARGGDEVAIARIAAIPLTMGGRVAFQIENALAAVAAAWALGV
PIELIRAGIRTFDADAAQAPGRFNLFNLGGAHVLVDYGHNPAAIEAVGAAIRNWPARRRIGVIGGPGDRR
DEDLVEQGELLGGAFDQIILKEDDDVRGRPRGEAAALLRQGLRQSARKAAIEDILDETEAIAAALDDLRA
GDLVVIFPESVERAIKLILVRVWI
>gnl|CDD|131124 TIGR02069, cyanophycinase, cyanophycinase. This model describes both cytosolic and extracellular cyanophycinases. The former are part of a system in many Cyanobacteria and a few other species of generating and later utilizing a storage polymer for nitrogen, carbon, and energy, called cyanophycin. The latter are found in species such as Pseudomonas anguilliseptica that can use external cyanophycin. The polymer has a backbone of L-aspartic acid, with most Asp side chain carboxyl groups attached to L-arginine [Energy metabolism, Other]
LVIIGGAEDKVGDREILREFVSRAGGEDAIIVIITSASEEPREVGERYITIFSRLGVKEVKILDVRERED
ASDENAIALLSNATGIFFTGGDQLRITSLLGDTPLLDRLRKRVHEGIILGGTSAGAAVMSDTMIVGGDSE
ESPRKETVDMAPGLGLLPNVLIDQHFAQRGRLGRLLSAISQNPEVLGIGIDEDTAIVVEDDGSFRVIGQG
AVTIVDGRDITYTNVSEVKADEPLSIFNLRLHILPHGYKF
>gnl|CDD|273951 TIGR02070, mono_pep_trsgly, monofunctional biosynthetic peptidoglycan transglycosylase. This family is one of the transglycosylases involved in the late stages of peptidoglycan biosynthesis. Members tend to be small, about 240 amino acids in length, and consist almost entirely of a domain described by pfam00912 for transglycosylases. Species with this protein will have several other transglycosylases as well. All species with this protein are Proteobacteria that produce murein (peptidoglycan) [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
GYVIGCLVAGVLLFNLAVFAALASWRFVPPPSTAFMVAEKLALWGQGDPTCGIQHRWRPYDQISPNLKRA
VIASEDAKFVEHHGFDWEAIQDALEKNEKSGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLE
TWWSKQRILEVYLNSVEWGNGVFGAEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRK
ATWILKQMGYLGLP
>gnl|CDD|273952 TIGR02071, Includes:_Penicillin-insensitive_transglycosylase, penicillin-binding protein 1B. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
GFLLKLAFTAAVLLAFYGLYLDQQIRSRFDGKVWQLPAAVYARPLNLEPGMSLSKKELLIELDATQYRQV
SHVTLPGEYSVQNNSIEVIRRPFDFPDGAEPQRRARLTFNGNQLSKIENLDNNKEFGFFRLDPKLIAMLY
SPNGEQRLFVPRDQFPELLVDTLLATEDRDFYEHDGISLYSIGRAVWVNLTAGRTVQGGSTLTQQLVKNL
FLSNERSLWRKANEAYMALILDARYSKDRILELYLNEVYLGQSGDDAIHGFPLASQYYFGRPLGELSLDQ
VALLVGMVKGPSYYNPWRNPDRALERRNLVLRLLQEQKIIDDEEYDMLSARPLGVQKKGGIISRQPAFLQ
LVRRELRQKLGDKVKDLSGLRIFTTLDPVSQSAAEQAVQETIPALKKKKKLPDLEAAMVVTDRFTGEVRA
MVGGSDPQFAGFNRALQARRQIGSLVKPAVYLTALSQPDKYRLNTWIEDQPLSIKLSNGQVWSPQNYDRR
YSGTVMLYDALAHSLNIPTVNLGMKVGLPKVSQTWNKLGINKDEIPPVPSMLLGAINLTPYEVAQLYQTI
ASGGNRAPLSAVRSVLDEDGKVLYQSDPQAEQAVPSQAAYLTLYAMQQVVQRGTARSLGADFPSLSLAGK
TGTTNDNRDSWFAGIDGKEVTIIWLGRDDNGPTKLTGASGALQVYARYLSYQTPEPLLLVPPEGIDWFGV
DPQGNGGCKANCPGARRLPIWTGNPQALCQ
>gnl|CDD|273953 TIGR02072, Malonyl-_O-methyltransferase, malonyl-acyl carrier protein O-methyltransferase BioC. This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
SFNKAAKTYDRHAKIQREMAKRLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGM
LAQAKTKLSENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGT
LHELRQSFGQHGLRYLSLDELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGRTSRKQ
LKAFLERYEQEFQPDGLPLTYHVVYGIAKK
>gnl|CDD|273954 TIGR02073, Includes:_Penicillin-insensitive_transglycosylase, penicillin-binding protein 1C. This subfamily of the penicillin binding proteins includes the member from E. coli designated penicillin-binding protein 1C. Members have both transglycosylase and transpeptidase domains and are involved in forming cross-links in the late stages of peptidoglycan biosynthesis. All members of this subfamily are presumed to have the same basic function [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
PPPLLFHRPSSTVVLDRHGTLLRALLANDGQWRLPVPLEDISPKFLQALLLYEDKRFYWHPGVNPLALLR
AAWQNLTNGRRVSGGSTLTMQLARLLDPELSRTLTGKLRQMWRAIQLEARYSKREILEAYLNLAPYGGNL
EGLRAASLIYFGKEPSSLSLAEAALLAALPQAPSARRLDRLPKAAKAARDRLLDRMVEQGPDDSEQVALA
ALEPLPALPEPLPQLAPHFALKLLRARPEIASVIVSTLDADLQRRLEELARRYLSALRPRGISNLAILVV
DNRSGAVLAYVGSADFFDDSNSGQVDGVRAPRSPGSTLKPFLYALALDDGLLHPDSLLKDVPLRFGDYAP
ENFDKTFHGPVPAREALARSLNIPAVRLLERVGPPRFADFLRQAGLNLLKPKSDYYGLSLALGGAEITLQ
DLANLYAMLANQGLSGPLRFLQTDAKRPERERLLSPGAAWIVLDILKDRPRPDDTLPLSALPTRLPLAWK
TGTSYGFRDAWAAGVSGRYTIGVWVGNFDGKPNPGFFGAAAAAPLLFDILDALQASEASTLPRPLKEVPG
CLVLGNLPILPCPEQISTWFLPGGSPPTLSEPHKPVVILINEGIAACLPDKPEARQKLALFDVAAYFAQA
GLPKRKPLLERNASLIISPPLDGIYILRDPDGPKAALLLVLIAAGGASGLYWFLDGKLLGEALPKQSILW
WPPAPGFYRLSVVDDDGRIDTLVFFIE
>gnl|CDD|273955 TIGR02074, Includes:_Penicillin-insensitive_transglycosylase, penicillin-binding protein, 1A family. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
RREYVPIDDIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLEGGSTITQQLAKNLYLTNE
RTITRKIQEALLALKLEQKLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPK
APSAYNPFKNPERAKDRRNLVLSNMVENGYITAEEAEEAINEPIQLYLQTKKSEQYKAPYFVDYVIQELE
EEYGEELYTGGLKIYTTLDLDAQKAAEKVLNTGLRVAGRRDGDDLQAALVAIDPDTGAVRALVGGRDYGK
SQFNRATQAKRQPGSTFKPFVYAAALEKGLTPATIVNDEPITYNGNGPWSPKNYGGGYRGNVTLRQALAQ
SRNIPAVRLLQEVGLDKVVALAKRFGITSPLDPVLSLALGTVEVSPLEMASAYAVFANGGKYVEPHGIRK
IVDRDGKVIYENKPKTTQVISPATAYIMTDMLKGVVESGTGRSARLPGRPVAGKTGTTQNWRDAWFVGYT
PYYVTAVWVGYDDKKTLGKSGTGGGLAAPIWRDFMAEALKN
>gnl|CDD|213681 TIGR02075, Uridylate_kinase, uridylate kinase. This protein, also called UMP kinase, converts UMP to UDP by adding a phosphate from ATP. It is the first step in pyrimidine biosynthesis. GTP is an allosteric activator. In a large fraction of all bacterial genomes, the gene tends to be located immediately downstream of elongation factor Ts and upstream of ribosome recycling factor. A related protein family, believed to be equivalent in function and found in the archaea and in spirochetes, is described by a separate model, TIGR02076 [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
YKRVLLKLSGEALAGESQFGIDPDRLNRIANEIKELVKMGIEVGIVIGGGNIFRGVSAAELGIDRVSADY
MGMLATVINGLALRDALEKLGLKTRVLSAISMPQICESYIRRKAIKHLEKGKVVIFSGGTGNPFFTTDTA
AALRAIEINADVILKGTNVDGVYTADPKKNKDAKKYDTITYNEALKKNLKVMDLTAFALARDNNLPIVVF
NIDKPGALKKVILGKGIGTLVS
>gnl|CDD|273956 TIGR02076, Uridylate_kinase, uridylate kinase, putative. This family consists of the archaeal and spirochete proteins most closely related to bacterial uridylate kinases (TIGR02075), an enzyme involved in pyrimidine biosynthesis. Members are likely, but not known, to be functionally equivalent to their bacterial counterparts. However, substantial sequence differences suggest that regulatory mechanisms may be different; the bacterial form is allosterically regulated by GTP [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
IVISLGGSVLSPEIDAEFIKEFANILRKLSDEHKVGVVVGGGKTARRYIGVARELGASETFLDEIGIDAT
RLNAMLLIAALGDDAYPKVPENFEEALEAMSLGKIVVMGGTHPGHTTDAVAALLAEFSKADLLINATNVD
GVYDKDPKKDPDAKKFDKLTPEELVEIVGSSSVKAGSNEVVDPLAAKIIERSKIRTIVVNGRDPENLEKV
LKGEHVGTIIE
>gnl|CDD|200156 TIGR02077, Thr_operon_leader_peptide_Thr_operon_attenuator., thr operon leader peptide. This family consists of examples of the threonine biosynthesis (thr) operon leader peptide, also called the thr operon attenuator. The small gene for this peptide is often missed in genome annotation. It should be looked for in genomes of the proteobacteria, immediately upstream of genes for threonine biosynthesis, typically aspartokinase I/homoserine dehydrogenase, homoserine kinase, and threonine synthase. Transcription of the rest of the Thr operon is attenuated (mostly turned off) unless the ribosome pauses during a stretch of the leader sequence rich in both Ile (made from Thr) and in Thr itself because of the scarcity of those amino acids at the time. The leader peptide itself, once made, may have no role other than to be degraded. Similar systems exist for some other amino acid biosynthetic operons, such as Trp [Amino acid biosynthesis, Aspartate family]
MKRISLHITTTIITTTITTGNGAG
>gnl|CDD|131133 TIGR02078, AspKin_pair, Pyrococcus aspartate kinase subunit, putative. This family consists of proteins restricted to and found as paralogous pairs (typically close together) in species of Pyrococcus, a hyperthermophilic archaeal genus. Members are always found close to other genes of threonine biosynthesis and appear to represent the Pyrococcal form of aspartate kinase. Alignment to aspartokinase III from E. coli shows that 300 N-terminal and 20 C-terminal amino acids are homologous, but the form in Pyrococcus lacks ~ 100 amino acids in between [Amino acid biosynthesis, Aspartate family]
MIVVKFGGSSVRYAFEEALELVKSLSEEKRVIVVVSALKGITDCLIRYANTFDKSAALEIEEIYEEFAKE
LGVDLNILSPYLKELFNPPDLPKEALRDYILSLGERLSAVIFAEGINGKVVDPWDIFFAKGDFGNAFIDI
KKSKRNAKILYEVLESGKIPVIPGFYGNLNGYRVTLGRGGSDYSAVALGVLLNSKLVAIMSDVEGIFTAD
PKLVPSARLIPYLSYEEIKIAAKLGMKALQWKAADLAKEYKIPVLFGRTRDWRMGTLISNRSSGMPLMVY
KDGELLVVNVRREISYPVIEEGEFWKKYKVPKEDGIEIIRELHRKVV
>gnl|CDD|273957 TIGR02079, THD1, threonine dehydratase. This model represents threonine dehydratase, the first step in the pathway converting threonine into isoleucine. At least two other clades of biosynthetic threonine dehydratases have been characterized by models (TIGR01124 and TIGR01127). Those sequences described by this model are exclusively found in species containg the rest of the isoleucine pathway and which are generally lacking in members of the those other two clades of threonine dehydratases. Members of this clade are also often gene clustered with other elements of the isoleucine pathway [Amino acid biosynthesis, Pyruvate family]
QDIEAARKRLKEVVPHTPLQLNERLSEKYGANIYLKREDLQPVRSYKIRGAYNFLKQLSDAQLAKGVVCA
SAGNHAQGFAYACRHLGVHGTVFMPATTPKQKIDRVKIFGGEFIEIILVGDTFDQCAAAAREHVEDHGGT
FIPPFDDPRIIEGQGTVAAEILDQLPEKPDYVVVPVGGGGLISGLTTYLAGTSPKTKIIGVEPEGAPSMK
ASLEAGEVVTLDKIDNFVDGAAVKRVGDLNFKALKDVPDEVTLVPEGAVCTTILDLYNLEGIVAEPAGAL
SIAALERLGEEIKGKTVVCVVSGGNNDIERTEEIRERSLLYEGLKHYFIVRFPQRPGALREFLNDVLGPN
DDITRFEYTKKSNRETGPALIGIELNDKEDFAGLLERMAAADIHYEDINENDILYNLLI
>gnl|CDD|131135 TIGR02080, Cystathionine_gamma-synthase, O-succinylhomoserine (thiol)-lyase. This family consists of O-succinylhomoserine (thiol)-lyase, one of three different enzymes designated cystathionine gamma-synthase and involved in methionine biosynthesis. In all three cases, sulfur is added by transsulfuration from Cys to yield cystathionine rather than by a sulfhydrylation step that uses H2S directly and bypasses cystathionine [Amino acid biosynthesis, Aspartate family]
TRKQATIAVRSGLNSDTQYGCVVPPIYLSTTYNFTGFNEPRAYDYSRSGNPTRDLLQQALAELEGGAGAV
VTNTGMSAIHLVTTALLGPDDLLVAPHDCYGGTYRLLNALAKKGCFRVLFVDQGDEQALRAALAQKPKLV
LIETPSNPLLRVVDIAKICHLAKAVGAVVVVDNTFLSPALQNPLALGADLVLHSCTKYLNGHSDVIAGAV
IAKDPQVAEELAWWANNLGVTGGAFDSYLTLRGLRTLVARMRLQQRNAQAIVEYLQTQPLVKKIYYPGLP
DHPGHEIAARQQKGFGAMLSFELKGGEQTVRRFLGGLSLFTLAESLGGVESLIAHPATMTHAAMGPEARA
EAGISDTLLRLSVGLEDADDLIADLEQGLRAA
>gnl|CDD|273958 TIGR02081, conserved_hypothetical_protein, methionine biosynthesis protein MetW. This protein is found alongside MetX, of the enzyme that acylates homoserine as a first step toward methionine biosynthesis, in many species. It appears to act in methionine biosynthesis but is not fully characterized [Amino acid biosynthesis, Aspartate family]
RVDLESILNLIPPGSRVLDLGCGDGELLALLRDEKQVRGYGIEIDQDGVLACVARGVNVIQGDLDEGLEA
FPDKSFDYVILSQTLQATRNPEEILDEMLRVGRHAIVSFPNFGYWRVRWSILTKGRMPVTGELPYDWYNT
PNIHFCTIADFEDLCGELNLRILDRAAFDVDGRGGREVRWFPNLRGELAVYRVS
>gnl|CDD|273959 TIGR02082, Methionine_synthase, 5-methyltetrahydrofolate--homocysteine methyltransferase. This family represents 5-methyltetrahydrofolate--homocysteine methyltransferase (EC 2.1.1.13), one of at least three different enzymes able to convert homocysteine to methionine by transferring a methyl group on to the sulfur atom. It is also called the vitamin B12(or cobalamine)-dependent methionine synthase. Other methionine synthases include 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase (MetE, EC 2.1.1.14, the cobalamin-independent methionine synthase) and betaine-homocysteine methyltransferase [Amino acid biosynthesis, Aspartate family]
LNQRILVLDGAMGTQLQSANLTEADFRGAFADCHRELKGNNDILNLTKPEVIATIHRAYFEAGADIIETN
TFNSTTISQADYDLEDLIYDLNFKGAKLARAVADEFTLTPEKPRFVAGSMGPTNKTATLSPDVERPGFRN
VTYDELVDAYTEQAKGLLDGGVDLLLIETCFDTLNAKAALFAAETVFEEKGRELPIMISGTIVDTSGRTL
SGQTIEAFLTSLEHAGIDMIGLNCALGPDEMRPHLKHLSEHAEAYVSCHPNAGLPNAFGEYDLTPDELAK
ALADFAAEGGLNIVGGCCGTTPDHIRAIAEAVKNIKPRQRPVLYEPSRLSGLEAITIAQDSNFVNIGERT
NVAGSKKFRRLIIAEDYDEALDIAKQQVENGAQILDINVDYGMLDGVAAMKRFLNLLASEPDISTVPLML
DSSEWAVLEAGLKCIQGKCIVNSISLKDGEERFIETAKLIKEYGAAVVVMAFDEEGQARTADRKIEICKR
AYNILTEKVGFPPEDIIFDPNILTIATGIEEHRRYAINFIEAIRWIKEELPDAKISGGVSNVSFSFRGNP
AAREAMHSVFLYHAIRAGMDMGIVNAGKILPYDDIDPELRQVVEDLILNRRREATEPLLELAQLYEGTTT
KSSKEAQQAEWRNLPVEERLEYALVKGEREGIEEDLEEARKKLTRPLEIIEGPLMDGMKVVGDLFGSGKM
FLPQVVKSARVMKKAVAYLEPHMEKEKSEDSSKGKIVLATVKGDVHDIGKNIVGVVLSCNGYEVVDLGVM
VPIEKILEAAKDHNADVIGLSGLITPSLDEMKEVAEEMNRRGITIPLLIGGAATSKTHTAVKIAPIYKGP
VVYVLDASRAVTVMDTLMSAKRKDTENGRIKEEYDTAREKHGEQRSKRIAASEQAARKNVFAPDWSDDIE
PPAPPFWGTQIVEASDIAELRPYIDWTPFFLQWQLRGKYPKILGDEYEGLEAQKLFPDANEMLDKLSAEN
LLHARGVYGYFPAQSVGDDIEIYTDETVETHPIATVRYLFHFPRQQSGRYLCLADFIAPKASGIVDYIGA
FAVTAGFGAEELADKLEAQHDDYDYIMVKAIADRLAEAFAEYLHRRVRKELWGYAAEEPLSNEDLLKLRY
QGIRPAPGYPACPDHTEKATMFELLEPERIGVRLTESLAMHPEQSVSGLYFAHPEAKYFAV
>gnl|CDD|131138 TIGR02083, 3-isopropylmalate_dehydratase_large_subunit_1, 3-isopropylmalate dehydratase, large subunit. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are described by a separate model of subfamily (rather than equivalog) homology type (TIGR01343). This model along with TIGR00170 describe clades which consist only of LeuC sequences. Here, the genes from Pyrococcus furiosus, Clostridium acetobutylicum, Thermotoga maritima and others are gene clustered with related genes from the leucine biosynthesis pathway [Amino acid biosynthesis, Pyruvate family]
MTMAEKILAQHAGLESVEPGELILAKLDIVLGNDITTPLAIKAFKEYGGKKVFDPDRVALVPDHFTPNKD
IKSAEQCKMMREFAREQGIEKFFEIGNMGIEHALLPEEGIVKPGDLIIGADSHTCTYGALGAFATGVGST
DMAVGMATGKAWFRVPEAIKFVLKGKLKPWVTGKDLILHIIGIIGVDGALYKSMEFSGEGLKELSMDDRF
TIANMAIEAGAKTGIFPVDEITIEYEKGRGKREEKIYKADEDAKYVRVIEIDLSELEPQVAFPHLPENTK
DISEAGKEEIKIDQVVIGSCTNGRLEDLRLAAEILKGKTVAPDVRCIIIPGSQNVYLEAMKEGLLEIFIE
AGAVVSTPTCGPCLGGHMGILAEGERAISTTNRNFVGRMGHPKSEVYLASPAVAAASAIKGYIASPEEV
>gnl|CDD|131139 TIGR02084, 3-isopropylmalate_dehydratase_small_subunit, 3-isopropylmalate dehydratase, small subunit. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The members of the seed for this model are those sequences which are gene clustered with other genes involved in leucine biosynthesis and include some archaea [Amino acid biosynthesis, Pyruvate family]
GKVHKYGDNVDTDVIIPARYLNTSDPKELAKHCMEDLDKDFVKKVKEGDIIVAGENFGCGSSREHAPIAI
KASGISCVIAKSFARIFYRNAINIGLPIVESEEAVDEIEEGDEVEVDLEKGIIKNLTKGKEYKATPFPEF
LQKIMKAGGLLNYVKK
>gnl|CDD|131140 TIGR02085, 23S_rRNA_uracil747-C5-methyltransferase_RlmC, 23S rRNA (uracil-5-)-methyltransferase RumB. This family consists of RNA methyltransferases designated RumB, formerly YbjF. Members act on 23S rRNA U747 and the equivalent position in other proteobacterial species. This family is homologous to the other 23S rRNA methyltransferase RumA and to the tRNA methyltransferase TrmA [Protein synthesis, tRNA and rRNA base modification]
QCAFYIQGRCRSCQWLAQPYSEQLTNKQQHLKELLAPNATVVQWLAPVTSAEQAFRNKAKMVVSGSVERP
ILGILHRDGTPLDLCDCPLYPQSFQPVFAYLKNFIARAGLTPYNVAKKKGELKFILLTESENSGQLMLRF
VLRSETKLAQIRRALPWLIEQLPQLEVISVNIQPVHMAILEGEEEIFLTEQQALPERFNDVPLVIRPQSF
FQTNPKVAAQLYATARQWVREIPVTQMWDLFCGVGGFGLHCAGPDTQLTGIEIESEAIACAQQSAQMLGL
DNLSFAALDSAKFATAQMSAPELVLVNPPRRGIGKELCDYLSQMAPKFILYSSCNAQTMAKDIAELSGYQ
IERVQLFDMFPHTSHYEVLTLLVR
>gnl|CDD|273960 TIGR02086, 3-isopropylmalate_dehydratase_large_subunit_2, 3-isopropylmalate dehydratase, large subunit. This subfamily is a subset of the larger HacA family (Homoaconitate hydratase family, TIGR01343) and is most closely related to the 3-isopropylmalate dehydratase, large subunits which form TIGR00170. This subfamily includes the members of TIGR01343 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities
MTLAEKILSEKVGRPVCAGEIVEVEVDLAMTHDGTGPLAIKALRELGVARVWDPEKIVIAFDHNVPPPTV
EAAEMQKEIREFAKRHGIKNFDVGEGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMA
IALATGKTWIKVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLC
NMAVEMGAKAGIIEPDEETYEYLKKRRGLEFRILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVS
DVEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMI
CPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGSPNAEIYLASPATAAASAVEGYITDPED
>gnl|CDD|273961 TIGR02087, 3-isopropylmalate_dehydratase_small_subunit, 3-isopropylmalate dehydratase, small subunit. This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities
GRVWKFGDDIDTDEIIPGRYLRTTDPDELASHAMEGIDPEFAKKVRPGDVIVAGKNFGCGSSREQAALAL
KAAGIAAVIAESFARIFYRNAINIGLPLIEAKTEGIKDGDEVTVDLETGEIRVNGNEEYKGEPLPDFLLE
ILREGGLLEYLKKR
>gnl|CDD|273962 TIGR02088, 3-isopropylmalate_dehydrogenase, isopropylmalate/isohomocitrate dehydrogenases. This model represents a group of archaeal decarboxylating dehydrogenases which include the leucine biosynthesis enzyme 3-isopropylmalate dehydrogenase (LeuB, LEU3) and the methanogenic cofactor CoB biosynthesis enzyme isohomocitrate dehydrogenase (AksF). Both of these have been characterized in Methanococcus janaschii. Non-methanogenic archaea have only one hit to this model and presumably this is LeuB, although phylogenetic trees cannot establish which gene is which in the methanogens. The AksF gene is capable of acting on isohomocitrate, iso(homo)2-citrate and iso(homo)3-citrate in the successive elongation cycles of coenzyme B (7-mercaptoheptanoyl-threonine phosphate). This family is closely related to both the LeuB genes found in TIGR00169 and the mitochondrial eukaryotic isocitrate dehydratases found in TIGR00175. All of these are included within the broader subfamily model, pfam00180
VAVIPGDGIGPEVIEAAIRILNKLGLEIEFIEFEAGDEALKKYGSALPEDTLEEIRKADAILFGAVTTPA
NPGYKSVIVTLRKELDLYANVRPAKSLPGIPDLYPNGKDIVIVRENTEGLYAGFEFGFSDRAIAIRVITR
EGSERIARFAFNLAKERNRKVTCVHKANVLKGTDGLFREVCREIAKRYGVEYRDMYVDSAAMNLVKDPWR
FDVIVTTNMFGDILSDLASALAGSLGLAPSANIGDRKALFEPVHGSAPDIAGKGIANPTAAILSVAMMLD
YLGELEKGKLVWEAVEYYIIEGKKTPDLGGTAKTKEVGDEIA
>gnl|CDD|273963 TIGR02089, Probable_tartrate_dehydrogenase/decarboxylase, tartrate dehydrogenase. Tartrate dehydrogenase catalyzes the oxidation of both meso- and (+)-tartrate as well as a D-malate. These enzymes are closely related to the 3-isopropylmalate and isohomocitrate dehydrogenases found in TIGR00169 and TIGR02088, respectively [Energy metabolism, Other]
MKQYRIAAIPGDGIGKEVVAAALQVLEAAAKRHGGFSLHFTEFPWSCDYYKEHGKMMPEDGLEKLKKFDA
IFLGAVGWPALVPDHISLWGLLLKIRREFDQYANVRPAKLLPGVTSPLRNCGPGDFDFVVVRENSEGEYS
GVGGRIHRGTDEEVATQNAIFTRKGVERIMRFAFELAQKRRKHLTSATKSNGIRHSMPFWDEVFAEVAAE
YPDVEWDSYHIDALAARFVLKPETFDVIVASNLFGDILSDLGAALMGSLGVAPSANINPEGKFPSMFEPV
HGSAPDIAGKGIANPIGAIWTAAMMLEHLGEKEAGAKIMDAIERVTAAGILTPDVGGKATTSEVTEAVCN
AL
>gnl|CDD|273964 TIGR02090, Putative_R-citramalate_synthase_CimA, isopropylmalate/citramalate/homocitrate synthases. Methanogenic archaea contain three closely related homologs of the 2-isopropylmalate synthases (LeuA) represented by TIGR00973. Two of these in Methanococcus janaschii (MJ1392 - CimA; MJ0503 - AksA) have been characterized as catalyzing alternative reactions leaving the third (MJ1195) as the presumptive LeuA enzyme. CimA is citramalate (2-methylmalate) synthase which condenses acetyl-CoA with pyruvate. This enzyme is believed to be involved in the biosynthesis of isoleucine in methanogens and possibly other species lacking threonine dehydratase. AksA is a homocitrate synthase which also produces (homo)2-citrate and (homo)3-citrate in the biosynthesis of Coenzyme B which is restricted solely to methanogenic archaea. Methanogens, then should and aparrently do contain all three of these enzymes. Unfortunately, phylogenetic trees do not resolve into three unambiguous clades, making assignment of function to particular genes problematic. Other archaea which lack a threonine dehydratase (mainly Euryarchaeota) should contain both a CimA and a LeuA gene. This is true of, for example, archaeoglobus fulgidis, but not for the Pyrococci which have none in this clade, but one in TIGR00973 and one in TIGRT00977 which may fulfill these roles. Other species which have only one hit to this model and lack threonine dehydratase are very likely LeuA enzymes
VYIFDTTLRDGEQTPGVSLTVEQKVEIARKLDELGVDVIEAGFPIASEGEFEAIKKISQEGLNAEICSLA
RALKKDIDKAIDCGVDSIHTFIATSPIHLKYKLKKSRDEVLEKAVEAVEYAKEHGLIVEFSAEDATRTDI
DFLIKVFKRAEEAGADRINIADTVGVLTPQKMEELIKKLKENVKLPISVHCHNDFGLATANSIAGVKAGA
EQVHVTVNGIGERAGNAALEEVVMALKYLYGVKTKIKTEKLYETSRLVSELSGVKVPPNKAIVGENAFAH
ESGIHVDGVIENPLTYEPISPEVVGNKRRIILGKHSGRHAVEAKLKELGIKVTDEQLKEILKRIKEIGDK
GKRVTDADVKEIV
>gnl|CDD|273965 TIGR02091, Glucose-1-phosphate_adenylyltransferase, glucose-1-phosphate adenylyltransferase. This enzyme, glucose-1-phosphate adenylyltransferase, is also called ADP-glucose pyrophosphorylase. The plant form is an alpha2,beta2 heterodimer, allosterically regulated in plants. Both subunits are homologous and included in this model. In bacteria, both homomeric forms of GlgC and more active heterodimers of GlgC and GlgD have been described. This model describes the GlgC subunit only. This enzyme appears in variants of glycogen synthesis pathways that use ADP-glucose, rather than UDP-glucose as in animals [Energy metabolism, Biosynthesis and degradation of polysaccharides]
AMVLAGGRGSRLSPLTKRRAKPAVPFGGKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQRGWDFD
GFIDGFVTLLPAQQRESGTDWYQGTADAVYQNLDLIEDYDPEYVLILSGDHIYKMDYEKMLDYHIESGAD
VTIACIPVPRKEASRFGVMQVDEDGRIVDFEEKPANPPSIPGMPDFALASMGIYIFDKDVLKELLEEDAD
DPESSHDFGKDIIPRALEEGSVQAYLFSGYWRDVGTIDSFWEANMDLVSVVPPFDLYDRKWPIYTYNEFL
PPAKFVDSDAQVVDSLVSEGCIISGATVSHSVLGIRVRIGSGSTVEDSVIMGDVGIGRGAVIRNAIIDKN
VRIGEGVVIGN
>gnl|CDD|273966 TIGR02092, Glycogen_biosynthesis_protein_GlgD, glucose-1-phosphate adenylyltransferase, GlgD subunit. This family is GlgD, an apparent regulatory protein that appears in an alpha2/beta2 heterotetramer with GlgC (glucose-1-phosphate adenylyltransferase, TIGR02091) in a subset of bacteria that use GlgC for glycogen biosynthesis [Energy metabolism, Biosynthesis and degradation of polysaccharides]
NKMSAIINLTESSKNLSPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKNKERQSLFDHLGS
GREWDLHRKRDGLFVFPYNDRDDLSEGGKRYFSQNLEFLKRSTSEYTVVLNSHMVCNIDLKAVLKYHEET
GKDITVVYKKVKPADASEYDTILRFDESGKVKSIGQNLNPEEEENISLDIYIVSTDLLIELLYECIQRGK
LTSLEELIRENLKELNINAYEYTGYLANINSVKSYYKANMDLLDPQNFQSLFYSSQGPIYTKVKDEPPTY
YAENSKVENSLVANGCIIEGKVENSILSRGVHVGKDALIKNCIIMQRTVIGEGAHLENVIIDKDVVIEPN
VKIAGTSEQPLVISKGTVV
>gnl|CDD|273967 TIGR02093, Glycogen_phosphorylase, glycogen/starch/alpha-glucan phosphorylases. This family consists of phosphorylases. Members use phosphate to break alpha 1,4 linkages between pairs of glucose residues at the end of long glucose polymers, releasing alpha-D-glucose 1-phosphate. The nomenclature convention is to preface the name according to the natural substrate, as in glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, etc. Name differences among these substrates reflect differences in patterns of branching with alpha 1,6 linkages. Members include allosterically regulated and unregulated forms. A related family, TIGR02094, contains examples known to act well on particularly small alpha 1,4 glucans, as may be found after import from exogenous sources [Energy metabolism, Biosynthesis and degradation of polysaccharides]
ILYHLEYTYGKTIDDATPRDLYTALAKAVRDRLVDRWLETQEKYRDNNQKQVYYLSAEFLMGRLLGNNLL
NLGLYDEVKEALRELGLDLEEILEIENDAGLGNGGLGRLAACFLDSLATLGLPATGYGIRYEYGLFKQKI
VDGWQVELPDDWLRYGNPWEIRRPDRSYEVRFGGRVELQPDSDRLRPRWVPAETVLAIPYDVPVPGYRTD
TVNTLRLWSAEAPEEFDLDAFNAGDYYEAVEEKNRAENISRVLYPNDSTYEGKELRLKQQYFFVSASLQD
IIRRHLETHPDLSDFPKKVAIQLNDTHPALAIPELMRLLIDEEGMDWDEAWDITTKTFAYTNHTLLPEAL
EKWPVDLFQKLLPRHLEIIYEINRRFLAELAAKGPGDEAKIRRMSIIEEGQSKRVRMANLAIVGSHSVNG
VAALHTELLKEDLLKDFYELYPEKFNNKTNGITPRRWLRLANPGLSALLTETIGDDWLTDLDLLKKLEPY
ADDSEFLEEFRQVKQANKQRLAAYIKEHTGVEVDPNSIFDVQVKRLHEYKRQLLNVLHVIYLYNRIKEDP
PKDIVPRTVIFGGKAAPGYHMAKLIIKLINSVAEVVNNDPAVGDKLKVVFVPNYNVSLAELIIPAADLSE
QISTAGKEASGTGNMKFMLNGALTIGTLDGANVEIREEVGAENIFIFGLTVEEVEALREKGYNPREYYEA
DPELKRVLDLISSGTFSPGDPGLFRPLYDSLLNHGDPFFVLADFAAYVDAQERVDALYRDQLEWTKKSIL
NIANSGKFSSDRTIREYAKEIWHV
>gnl|CDD|273968 TIGR02094, Glycogen_phosphorylase, alpha-glucan phosphorylases. This family consists of known phosphorylases, and homologs believed to share the function of using inorganic phosphate to cleave an alpha 1,4 linkage between the terminal glucose residue and the rest of the polymer (maltodextrin, glycogen, etc.). The name of the glucose storage polymer substrate, and therefore the name of this enzyme, depends on the chain lengths and branching patterns. A number of the members of this family have been shown to operate on small maltodextrins, as may be obtained by utilization of exogenous sources. This family represents a distinct clade from the related family modeled by TIGR02093/pfam00343
VAYFSMEYGLHESLPIYSGGLGVLAGDHLKSASDLGLPLVAVGLLYKQGYFRQRLDEDGWQQEAYPNNDF
ESLPIEKVLDTDGKWLKISVRIRGRDVYAKVWRVQVGRVPLYLLDTNIPENSEDDRWITGRLYGGDKEMR
IAQEIVLGIGGVRALRALGIDPDVYHLNEGHAAFVTLERIRELIAQGLSFEEAWEAVRKSSLFTTHTPVP
AGHDVFPEDLMRKYFGDYAANLGLPREQLLALGRENPDDPEPFNMTVLALRLSRIANGVSKLHGEVSRKM
WQFLYPGYEEEEVPIGYVTNGVHNPTWVAPELRDLYERYLGENWRELLADEELWEAIDDIPDEELWEVHL
KLKARLIDYIRRRLRERWLRRGADAAILMATDRFLDPDVLTIGFARRFATYKRADLIFRDLERLARILNN
PERPVQIVFAGKAHPADGEGKEIIQRIVEFSKRPEFRGRIVFLENYDINLARYLVSGVDVWLNNPRRPLE
ASGTSGMKAAMNGVLNLSILDGWWGEGYDGDNGWAIGDGEEYDDEEEQDRLDAEALYDLLENEVIPLYYD
RDEKGIPADWVEMMKESIATIAPRFSTNRMVREYVDKFYLP
>gnl|CDD|273969 TIGR02095, Glycogen_synthase, glycogen/starch synthase, ADP-glucose type. This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate [Energy metabolism, Biosynthesis and degradation of polysaccharides]
MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVVELVDLSVGPRTL
YVKVFEGVVEGVPVYFIDNPSLFDRPGGIYGDDYPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTA
LVPALLKAVYRPNPIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLEFYGRVNFLKGGIVYADRVT
TVSPTYAREILTPEFGYGLDGVLKARSGKLRGILNGIDTEVWNPATDPYLKANYSADDLAGKAENKEALQ
EELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRV
IIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTVPIVRRTGGLADTVVDGDPEAESGTGFLFE
EYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSAKQYVELYRSL
>gnl|CDD|273970 TIGR02096, putative_cyclase, conserved hypothetical protein, steroid delta-isomerase-related. This family of proteins about 135 amino acids in length largely restricted to the Proteobacteria. This family and a delta5-3-ketosteroid isomerase from Pseudomonas testosteroni appear homologous, especially toward their respective N-termini. Members, therefore, probably are enzymes
TELAQHWIEAFNRGDMDAVLALLAEDVLYDDNQGGRVLGGKAQLARFLAPYRTAFPDLLVDVVVCRNDEG
VRVAAEWTVHGTYRTAFLGLPASGKTYSIRGVTFFVFDDGKIKRETTYYNLATFLRQLG
>gnl|CDD|131152 TIGR02097, Hypothetical_protein_yccV., hemimethylated DNA binding domain. This model describes the small protein from E. coli YccV and its homologs in other Proteobacteria. YccV is now described as a hemimethylated DNA binding protein. The model also describes a domain in longer eukaryotic proteins
AAKFRIGQVVRHKLFGYRGVVIDVDPEYSNTEEWLDAIPVEIRPLRDQPFYHVLAEDDEGLPYVAYVAEQ
NLLYDDSDEPIEHPQVDELFDGFDEGLQKPR
>gnl|CDD|131153 TIGR02098, Uncharacterized_protein_MJ0042, MJ0042 family finger-like domain. This domain contains a CXXCX(19)CXXC motif suggestive of both zinc fingers and thioredoxin, usually found at the N-terminus of prokaryotic proteins. One partially characterized gene, agmX, is among a large set in Myxococcus whose interruption affects adventurous gliding motility
MRIQCPNCKTSFRVVDSQLGANGGKVRCGKCGHVWYAR
>gnl|CDD|273971 TIGR02099, probable_transmembrane_protein, TIGR02099 family protein. This model describes a family of long proteins, over 1250 amino acids in length and present in the Proteobacteria. The degree of sequence similarity is low between sequences from different genera. Apparent membrane-spanning regions at the N-terminus and C-terminus suggest the protein is inserted into (or exported through) the membrane [Hypothetical proteins, Conserved]
RRLPRIAWSLFALILVLAALLVSLLRWLLPLADEYRPQIEQYLSSALGIPVAIGSLSGSWQRFGPTLELS
GVRIGDPDAGQLLILRVVVALDLWQSLLHRSPRLADLRVDGLALTLRRDDDGGWAVGGNPLTSNQPDGLL
LLLLRQLDRFSLRDSRISVLTPSGDRLTLEIPQLRWLNSGLRHRAEGRISLDDINHGSLQVRLDWQDDAG
LLDNGDFYAQADNLDLAPWLSRYMQDNTGLLRGQFSLRAWMSLSHGSVASGRVDLNPSQLAWSGANRTHT
LEVLQGNARWAPTAGGWQINAPSLRLDSDGEAWPLLVLAAAWQPRELRVRASRLDLEGLFPLLPLIAALS
PALNRWWQSLKPSGDLADVRLAGAPQDESLRFQASLEDLGWQPWELLPGANGLSGTIQGSAEGGELNLPT
QTAMLPYPEVFAAPLEIQQAGADLSWKQDGQGWTLALPKVQVANKDLGANGAFRLRFPGDAAPWMDLRAG
IADADAPAAWRYLPRSLMGEELADWLRTALQAGQVDNATLLYAGNLDDFPFPGNDGVFQAFVDLRNAVFA
FQPDWPALTDLDGDLLFENEGMSLDAAQGDLVGVPASQVTALIPDLGEEGLLVIADVQGEDGSAVLAYLA
ASPLKDSLGGTLAELQVGGPVAGKLKLDIPLAGGVETKVRGDVVLQNNALRIAPPMLELTQVSGKFEFDN
GGVSAKGLKARAFGQPLRLSFATEDKKKAFSVRLDANGDWTVKKLGQVLPEPLLPRLSGSAPWQGQVDID
LPDHGQTYQLLLNSDLVGLSLDLPAPLGKPADEARPLKLQVSGPLGARALRVSLGKLAAFAGRWLLGKAK
ALLAGALVLGRGRAAPPPPNGLHVRLRLPALDLDDWLALANRFDGPDDGPRQPSRSALFPAPQRVDLQTP
ELTAAGQTLHDLRLQAQPTAAGWAVTLDSREAKGTLTYPEAGAWAGQLKYLYYRLPALVALEATPEPEPD
SAADIDPQDIPALDLRIDDLWLGGQSIGALDLDARRQGSGLRLDNLQLASGEARLDGTGAWRGAGGASRT
TLSASLDGSNLGKLLDRFGLGPTVRNASFELNADLTWRGSPWSFQLATLSGNLKVDLGKGQFLDVSPGAA
RLLGLLSLDSLPRKLRLDFSDVFSKGFAFDSIRGTASLSDGVFRTDDIEMDGPAADIAIAGSTDLVTETV
DMEVVVVPELAASVPVAAAFALNPVVGLAVFAAQKVLGPPVAKISSVRYEVTGPWDDPQVTEVERQAKER
>gnl|CDD|131155 TIGR02100, Glycogen_operon_protein_GlgX_homolog, glycogen debranching enzyme GlgX. This family consists of the GlgX protein from the E. coli glycogen operon and probable equivalogs from other prokaryotic species. GlgX is not required for glycogen biosynthesis, but instead acts as a debranching enzyme for glycogen catabolism. This model distinguishes GlgX from pullanases and other related proteins that also operate on alpha-1,6-glycosidic linkages. In the wide band between the trusted and noise cutoffs are functionally similar enzymes, mostly from plants, that act similarly but usually are termed isoamylase [Energy metabolism, Biosynthesis and degradation of polysaccharides]
PGMPFPLGATWDGQGVNFALFSANAEKVELCLFDAQGEKEEARLPLPERTDDIWHGYLPGAQPGQLYGYR
VHGPYDPENGHRFNPNKLLLDPYAKALDGDLIWDDALFGYRIGHPDQDLSFDERDSAPGMPKAVVVDPDF
DWGGDEQRPRTPWEDTIIYEAHVKGFTQLHPDIPEELRGTYAGLAHPAMIDYLKKLGVTAVELLPVHAFI
DDRHLLEKGLRNYWGYNTLGFFAPEPRYLASGQVAEFKTMVRALHDAGIEVILDVVYNHTAEGNELGPTL
SFRGIDNASYYRLQPDDKRYYINDTGTGNTLNLSHPRVLQMVMDSLRYWVTEMHVDGFRFDLATTLGREL
YGFDMLSGFFTAIRQDPVLAQVKLIAEPWDIGPGGYQVGNFPPGWAEWNDRYRDDMRRFWRGDAGMIGEL
ANRLTGSSDLFEHNGRRPWASINFVTAHDGFTLRDLVSYNEKHNEANGENNRDGHNDNYSWNCGVEGPTD
DPAINALRRRQQRNLLATLLLSQGTPMLLAGDEFGRTQQGNNNAYCQDNEIGWVDWSLDEGDDELLAFTK
KLIALRKAHPVLRRERFFDGRNEADGLKDVTWLNADGEPMTEEDWENPETRLLCMVLSDMDPGGDPGADD
SLLLLLNAGPEPVPFKLPGGGGRWELVLDTADEEAPGIHLDAGQEAELPARSVLLLRR
>gnl|CDD|273972 TIGR02101, Invasin_IpaC, type III secretion target, IpaC/SipC family. This model represents a family of proteins associated with bacterial type III secretion systems, which are injection machines for virulence factors into host cell cytoplasm. Characterized members of this protein family are known to be secreted and are described as invasins, including IpaC from Shigella flexneri (SP:P18012) and SipC from Salmonella typhimurium (GB:AAA75170.1). Members may be referred to as invasins, pathogenicity island effectors, and cell invasion proteins [Cellular processes, Pathogenesis]
VLTSLLADDRRNLGAAAQLMHLANILKNTKQMSVKGEELEVRSLESAKQFDISGMSTNAVALLIALRVLM
SALNQADRKLSSKLSLLSFDATKSAAASMVREGKAALSSSIIGSATQVAITGVGAKLQAKGLFKQSGALK
KNLKPSNKLSAEAAQLKLQLNGQNAPKLVADSKRTGVAATKELGETTRHEIDPSNKALSAEHKAQLSQRV
ESLQDKIDLHQQTYEQNTLKAQAMQMIGDLIMRMSAVAGNISGASGQYAATQEEAEQQISQSSSRTASTA
SNETREASRKTKQLIQELLKILESINQSKNSAAAAIA
>gnl|CDD|273973 TIGR02102, alkaline_amylopullulanase, pullulanase, extracellular, Gram-positive. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (
IEENTLRIHYKNLPGESYENLGLWTWGDVEQPSENWPNGAIPFTDAKKDDYGYYVDVKLAEKQAKNISFL
INNTAGGNLDGDKHVELLSPKMNEVWIDEGYDEHSYIPLPAGTVRINYKRTDGNYDNWSLWFWGDVKSPS
TTDWPDGADFFAEGKYGAYIDIPLKEGANEIGFLILDKSKTGDAVKVQPADYSFTDLKNHNQIFVKDGDG
KVYTNPYYIDQVELKSAEQLSDESIVLSFTTLDGLDKEALLEQLKITDKEGNTVDITDVTIDTDKKTVTV
KGDFNLDKSPYTVSYNEVSVPTKQSWRLKDEMYAYDGKLGAQLHEDGTVTLKLWSPSADHVSVVLYDKDD
QDKVVGTVELKKGDRGVWEVQLTKENTGIDSLTGYYYHYEITRGGDKVLALDPYAKSLAAWNDATSDDQI
KVAKAAFVDPSSLGPQELDFAKIENFKKREDAIIYEAHVRDFTSDPAIAGDLTAQFGTFAAFVEKLDYLQ
DLGVTHIQLLPVLSYFFVNEFKNKERMLDYASSNTNYNWGYDPQNYFALSGMYSEDPKDPELRIAEFKNL
INEIHKRGMGVILDVVYNHTAKVYIFEDLEPNYYHFMDADGTPRTSFGGGRLGTTHEMSRRILVDSIKYL
VDEFKVDGFRFDMMGDHDAASIEIAYKEAKAINPNIIMIGEGWRTYAGDEGDPVQAADQDWMKYTETVGV
FSDDIRNELKSGFPNEGQPAFITGGARNVQGIFKNIKAQPHNFEADSPGDVVQYIAAHDNLTLHDVIAQS
IKKDPKVAENQEEIHRRIRLGNLMVLTSQGTAFIHSGQEYGRTKQFRNPDYRTPVSEDKVPNKSTLMTDV
DGNPFRYPYFIHDSYDSSDAINRFDWEKATDADAYPINNKTRDYTAGLIELRRSTDAFRLGSKALVDRKV
TLITIPGQNEIEEEDLVVAYQIVATNGDIYAVFVNADDKARTLTLGEDYAHLTVGEVVVDAEQAGVTGIA
EPKGVELTAEGLKLDPLTAAVVRVGGIEAPEKTPPPPEHEPQAPKPPTQDPDGSKPKDKVDPKDNKDPLT
PPGSDDENGETPKGNEEKKEEQPDKGANLPNTGTKNSNFILFGGLLVLLGTLGYLLKRKKQ
>gnl|CDD|273974 TIGR02103, pullulanase-like_protein_starch, alpha-1,6-glucosidases, pullulanase-type. Members of this protein family include secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants. Both enzymes hydrolyze alpha-1,6 glycosidic linkages. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family is closely homologous to, but architecturally different from, the Gram-positive pullulanases of Gram-positive bacteria (TIGR02102) [Energy metabolism, Biosynthesis and degradation of polysaccharides]
DLAGARAHWVDADTILWNVAENAPSVTLYYSPSAKLKFDSDGVFGGDRIKLTPSSGGLSQDLKMKFPHLA
SYKAFKLPADDANLRDLLKGQLVVVAYDANGILISATGVQTAGVLDALYAYAGPALSLGATLTDSGVTFR
LWAPTAQQVKLHIYSASKKVETTLPMTRDSTSGVWSAEGGSSWKGAYYRYEVTVYHPSTGKVETYLVTDP
YSVSLSANSEYSQVVDLNDPALKPEGWDALAMPKPQLASFADMVLYELHIRDFSANDESVPAELRGKYLA
FTAADSAGVQHLKKLADAGVTHLHLLPTFDIATVNEEKEKVADIQQPFSKLCELNPDSKSSEFAGYCDSG
SQLKQNDSKDNPEVQALNTLVRNLDSYNWGYDPFHYTVPEGSYATDPEGPARIKEFREMVQALNKTGLNV
VMDVVYNHTNASGPNDRSVLDKIVPGYYHRLNEDGGVENSTCCSNTATEHRMMAKLIVDSLVVWAKDYKV
DGFRFDLMGHHPKAQMLAAREAIKALTPEIYFYGEGWDFGEVANNRRFINATQLNLAGTGIGTFSDRLRD
AVRGGGPFDSGDALRQNQGFGSGLAVQPNAHHGLDAASKDGALHLADLTRLGMAGNLKDFVLTDHEGKVV
TGEELDYNGAPAGYAADPTETINYVSKHDNQTLWDAISYKAAAETPSAERVRMQAVSLSTVMLGQGIPFF
HAGSELLRSKSFDRDSYDSGDWFNRVDFSGQDNNWNVGLPRADKDGSNWPIIAPVLQDAAAKPDATDIKA
TTAFFLELLRIRSSSPLFRLDTAAEVMKRVDFRNTGPDQIPGLIVMSIDDGGIQAGASLDPRYDGIVVIF
NARPEEVTLSPDFAGTGLELHAVQQASGDESVAKSVYSAANGTFTVPAWTTAVFVLPR
>gnl|CDD|273975 TIGR02104, pulA_typeI, pullulanase, type I. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases
AFDDKFYYDGELGAVYTPEKTVFRVWAPTATEVELLLYKSGEDGEPYKVVKMKRGENGVWSAVLEGDLHG
YFYTYQVCINGKWRETVDPYAKAVTVNGKRGAVIDLEETNPEGWEKDHGPRLENPEDAIIYELHIRDFSI
HENSGVKNKGKYLGLTETGTKGPNGVSTGLDYLKELGVTHVQLLPVFDFAGVDEEDPNNAYNWGYDPLNY
NVPEGSYSTNPYDPATRIRELKQMIQALHENGIRVIMDVVYNHTYSREESPFEKTVPGYYYRYNEDGTLS
NGTGVGNDTASEREMMRKFIVDSVLYWVKEYNIDGFRFDLMGIHDIETMNEIRKALNKIDPNILLYGEGW
DLGTPLPPEQKATKANAYQMPGIAFFNDEFRDALKGSVFHLKKKGFVSGNPGTEEIVKKGILGSIELDAV
KPSALDPSQSINYVECHDNHTLWDKLSLANPDETEEQLKKRQKLATAILLLSQGIPFLHAGQEFMRTKQG
DENSYNSPDSINQLDWDRKATFKDDVNYIKGLIALRKAHPAFRLSSAEDIRKHLEFLPAEPSGVIAYRLK
DHANGDPWKDIIVIHNANPEPVDIQLPGDGTWNVVVDNKNAGSKP
>gnl|CDD|131160 TIGR02105, Yop_proteins_translocation_protein_F, type III secretion apparatus needle protein. Type III secretion systems translocate proteins, usually virulence factors, out across both inner and outer membranes of certain Gram-negative bacteria and further across the plasma membrane and into the cytoplasm of the host cell. This protein, termed YscF in Yersinia, and EscF, PscF, EprI, etc. in other systems, forms the needle of the injection apparatus [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
MDISAIAQQLKKPADDANQAVNDSLAALDLPNDPELMAELQFALNQYSAYYNIESTIVKMIKDLDSGILQ
KF
>gnl|CDD|211715 TIGR02106, putative_exported_protein, cyd operon protein YbgT. This model describes a very small (as short as 33 amino acids) protein of unknown function, essentially always found in an operon with CydAB, subunits of the cytochrome d terminal oxidase. It begins with an aromatic motif MWYFXW and appears to contain a membrane-spanning helix. This protein appears to be restricted to the Proteobacteria and exist in a single copy only. We suggest it may be a membrane subunit of the terminal oxidase. The family is named after the E. coli member YbgT (SP|P56100). This model excludes the apparently related protein YccB (SP|P24244) [Energy metabolism, Electron transport]
MWYFAWILGTLLACAFGVLNAMWLELREAR
>gnl|CDD|273976 TIGR02107, Coenzyme_PQQ_synthesis_protein_A, coenzyme PQQ precursor peptide PqqA. This model describes a very small protein, coenzyme PQQ biosynthesis protein A, which is smaller than 25 amino acids in many species. It is proposed to serve as a peptide precursor of coenzyme pyrrolo-quinoline-quinone (PQQ), with Glu and Tyr of a conserved motif Glu-Xxx-Xxx-Xxx-Tyr becoming part of the product [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
WKKPKFTEIRLGMEVTMYVSA
>gnl|CDD|273977 TIGR02108, Coenzyme_PQQ_synthesis_protein_B, coenzyme PQQ biosynthesis protein B. This model describes coenzyme PQQ biosynthesis protein B, a gene required for the biosynthesis of pyrrolo-quinoline-quinone (coenzyme PQQ). PQQ is required for some glucose dehydrogenases and alcohol dehydrogenases. Note that this gene appears to be required for PQQ in biosynthesis in Methylobacterium extorquens (under the name pqqG) and in Klebiella pneumoniae but that the equivalent pqqV in Acinetobacter calcoaceticus is not necessary for heterologous expression of PQQ biosynthesis in E. coli. Based on this latter finding, it is suggested (Goosen, et al. 1989) that PqqB might be a transporter or a PQQ-dependent enzyme rather than a PQQ biosynthesis enzyme [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
HIVVLGSAAGGGFPQWNCNCPNCRGARAGTIGAKARTQSSIAVSADGERWVLLNASPDIRQQIQATPALH
PQRGLRHTPIAGVVLTDGEIDHTTGLLTLREGQPFTLYATEMVLQDLSDNPIFNVLDHWNVRRQPIALNE
KFEFRIVARPGLEFTPFAVPGKAPLYSEHRAGDPHPGDTLGLKIEDGTTGKRLFYIPGCAEITDDLKARM
AGADLVFFDGTLWRDDEMIRAGVGTKTGRRMGHVSMSGEGGSLAVLADLEIARKVLIHINNTNPILDEDS
PERAEVEAAGWEVAYDGMEIVL
>gnl|CDD|162708 TIGR02109, Coenzyme_PQQ_synthesis_protein_E, coenzyme PQQ biosynthesis enzyme PqqE. This model describes coenzyme PQQ biosynthesis protein E, a prototypical peptide-cyclizing radical SAM enzyme. It links a Tyr to a Glu as the first step in the biosynthesis of pyrrolo-quinoline-quinone (coenzyme PQQ) from the precursor peptide PqqA. PQQ is required for some glucose dehydrogenases and alcohol dehydrogenases [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
PTVGPPLWLLAELTHRCPLQCPYCSNPLELARRKAELTTEEWTDVLTQAAELGVLQLHFSGGEPLARPDL
VELVAHARRLGLYTNLITSGVGLTEARLDALADAGLDHVQLSFQGVDEALADRIAGYKNAFEQKLAMARA
VKAAGLPLTLNFVIHRHNIDQIPEIIELAIELGADRVELATTQYYGWALLNRAALMPTRAQLEEATRIVE
EARERLKGGLVIDYVVPDYYAERPKACMGGWGRVFLNVTPAGKVLPCHAAEQIPGLSFPNVREHSLSEIW
YKSPAFNAYRGTDWMPEPCRSCERKERDFGGCRCQAFALTGDAANTDPVCSLSPLHDLILAARAEEAAGS
VPALVYRN
>gnl|CDD|273978 TIGR02110, Coenzyme_PQQ_synthesis_protein_F, coenzyme PQQ biosynthesis probable peptidase PqqF. In a subset of species that make coenzyme PQQ (pyrrolo-quinoline-quinone), this probable peptidase is found in the PQQ biosynthesis region and is thought to act as a protease on PqqA (TIGR02107), a probable peptide precursor of the coenzyme. PQQ is required for some glucose dehydrogenases and alcohol dehydrogenases [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
RRITLPNGLRVHLYHQPDAKRAAALLRVAAGSHDEPSAWPGLAHFLEHLLFLGGERFQGDDRLMPWVQRQ
GGQVNATTLERTTAFFFELPAAALAAGLARLCDMLARPLLTAEDQQREREVLEAEYIAWQNDADTLREAA
LLDALQAGHPLRRFHAGSRDSLALPNTAFQQALRDFHRRHYQAGNMQLWLQGPQSLDELEQLAARFGASL
AAGGECAQAPPAPLLRFDRLTLAGGSEPRLWLLFALAGLPATARDNVTLLCEFLQDEAPGGLLAQLRERG
LAESVAATWLYQDAGQALLALEFSARCISAAAAQQIEQLLTQWLGALAEQTWAEQLEHYAQLAQRRFQTL
ALSPLAQLRGRALGFALGCALPDALTDFLAALQDCPRTRLLTQQQIPGAPFAHSGLHAPVARLARAVVQA
RSVSLTLAASRCSAPKSPTRCAFLAALPSDKTERALALRWGFPSHPPEELALALQRQLRPLLADARHAGV
NGSWQATGASWQLLLNGPRSPMRAVFSVALALLALAAPMLAQPAANRASAPSIPIRQLLAALPERLLKSL
PAQQDDWLAARWGAATQLAQRVALQLSPGTADLARPTPLPARLGRGWVPLACDGGEQALLLFCPLPTADV
ASEAAWRLLAQLLEPPFFQRLRVELQLGYVVFCRYRRVADRDGLLFALQSPDASARELLQHIKRFLR
>gnl|CDD|131166 TIGR02111, Pyrroloquinoline-quinone_synthase, coenzyme PQQ biosynthesis protein C. This model describes the coenzyme PQQ (pyrrolo-quinoline-quinone) biosynthesis protein PqqC.In contrast to the broader model pfam05312, this model does not include related proteins likely to be functionally distinct from PqqC, such as homologs found in the Chlamydias [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
LSPEQFEAALRDIGARRYHDLHPFHALLHDGKLTRDQVQAWVLNRYYYQANIPLKDAAILARCPDPQLRR
IWRQRILDHDGDHEEDGGIERWLRLAEAVGLDREYVLSTRGVLPGTRFAVDAYVHFVREKSLLEAIASSL
TELFAPQIHSERVAGMLQHYDFIDDAALAYFRKRLTQAPRDVEFGLDYVLDHATTREKQEAALEALTFKC
DVLWAQLDALYFAYVAPGNVPPDAWVPGE
>gnl|CDD|131167 TIGR02112, Protein_ybgE., cyd operon protein YbgE. This model describes a small protein of unknown function, about 100 amino acids in length, essentially always found in an operon with CydAB, subunits of the cytochrome d terminal oxidase. It appears to be an integral membrane protein. It is found so far only in the Proteobacteria [Energy metabolism, Electron transport]
IASLYELMDKGLLRALSFILAFLLAGCVFWDPNRFAAAIGGFNAVLALLMIWAVCILWIHGVGFRPRSTL
WQLLFSPILGYIILIYLLIVFFA
>gnl|CDD|131168 TIGR02113, Probable_phosphopantothenoylcysteine_decarboxylase, phosphopantothenoylcysteine decarboxylase, streptococcal. In most bacteria, a single bifunctional protein catalyses phosphopantothenoylcysteine decarboxylase and phosphopantothenate--cysteine ligase activities, sequential steps in coenzyme A biosynthesis (see TIGR00521). These activities reside in separate proteins encoded by tandem genes in some bacterial lineages. This model describes proteins from the genera Streptococcus and Enterococcus homologous to the N-terminal region of TIGR00521, corresponding to phosphopantothenoylcysteine decarboxylase activity [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
KKILLAVTGSIAAYKAADLTSQLTKLGYDVTVLMTQAATQFITPLTLQVLSKNPVHLDVMDEHDPKVINH
IELAKKADLFLVAPASANTIAHLAHGFADNIVTSVALALPPETPKLIAPAMNTKMYQNPITQRNIKILKK
IGYQEIQPKESLLACGDYGRGALADLDDILQTIKEIL
>gnl|CDD|131169 TIGR02114, coaB_strep, phosphopantothenate--cysteine ligase, streptococcal. In most bacteria, a single bifunctional protein catalyses phosphopantothenoylcysteine decarboxylase and phosphopantothenate--cysteine ligase activities, sequential steps in coenzyme A biosynthesis (see TIGR00521). These activities reside in separate proteins encoded by tandem genes in some bacterial lineages. This model describes proteins from the genera Streptococcus and Enterococcus homologous to the C-terminal region of TIGR00521, corresponding to phosphopantothenate--cysteine ligase activity [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
KILVTSGGTSEPIDSVRSITNHSTGHLGKIITETFLSAGHEVTLVTTKRALKPEPHPNLSIREIETTKDL
LITLKELVQEHDILIHSMAVSDYTPVYMTDLEQVQASDNLNEFLSKQNHEAKISSTSEYQVLFLKKTPKV
ISLVKEWNPQIHLVGFKLLVNVTQEELVKVARASLIKNQADFILANDLTDISADQHKALLIEKNQVQTAQ
TKEEIAELLYEKVQKYD
>gnl|CDD|131170 TIGR02115, Protein_KdpF, K+-transporting ATPase, KdpF subunit. This model describes a very small integral membrane peptide KdpF, a subunit of the K(+)-translocating Kdp complex. It is found upstream of the KdpA subunit (TIGR00680). Because of its very small size and highly hydrophobic character, it is sometimes missed in genome annotation [Transport and binding proteins, Cations and iron carrying compounds]
IILLVLAVGLFIYLFYALLRPERF
>gnl|CDD|131171 TIGR02116, Hypothetical_protein_Rv3358/MT3466/Mb3393., toxin-antitoxin system, toxin component, Txe/YoeB family. The Axe-Txe pair in Enterococcus faecium and the homologous YefM-YoeB pair in Escherichia coli have been shown to act as an antitoxin-toxin pair. This model describes the toxin component. Nearly every example found is next to an identifiable antitoxin, as indicated by match to models TIGR01552 and/or pfam02604 [Cellular processes, Toxin production and resistance, Mobile and extrachromosomal element functions, Other]
FTPEAWEDYLKWQEADKKLKKKINELIKDVRRDPFKGKGKPEPLKGDLSGYWSRRITDEHRLVYRVLDDE
VLILAARYHY
>gnl|CDD|273979 TIGR02117, urease-associated_hypothetical_protein, conserved hypothetical protein. This conserved hypothetical protein of unknown function is found in several Proteobacteria. Its function is unknown and its genome context is not well-conserved. It is found amid urease genes in at least one species [Hypothetical proteins, Conserved]
FVAWLSLLLAGGTTFPRPVKATTGGQASPTEIYLLSNGIHTDIIAPVDDDNRDWFTVLPQLKIRDFHPEA
QWLEIGWGGKGFYLSTPTWADLKLQPVLRSLTADMSVLHVDGQPERYEAQSEVKRLLVSENQYNRLMDFI
SASFVRDAEGRVIPLPGGIYGDSDAFYAANGRYNALNTCNTWTAAALRSAGLRTGLWLPLPQGLRWSV
>gnl|CDD|131173 TIGR02118, TIGR02118, conserved hypothetical protein. This model represents a small family of proteins of unknown function, each about 105 amino acids in length. Conserved sites in the multiple alignment include a pair of aromatic residues, a histidine, and an aspartate [Hypothetical proteins, Conserved]
IKVSVLYEQPEDGAAFDHHYRDTHVPLAQKLPGLRRYAVDKIVSGLPGSSPYYGMCELYFDSIEDFQAAF
DSPEGKAAAADVANFADGAPTMQISEEVDL
>gnl|CDD|131174 TIGR02119, Sodium/pantothenate_symporter, sodium/pantothenate symporter. Pantothenate (vitamin B5) is a precursor of coenzyme A and is made from aspartate and 2-oxoisovalerate in most bacteria with completed genome sequences. However, some pathogens must import pantothenate. This model describes PanF, a sodium/pantothenate symporter, from a larger family of Sodium/substrate symporters (pfam00474). Several species that have this transporter appear to lack all enzymes of pantothenate biosynthesis, namely Haemophilus influenzae, Pasteurella multocida, Fusobacterium nucleatum, and Borrelia burgdorferi [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A, Transport and binding proteins, Other]
WEVVIPLIIYLVTVFLIAIYASKRVQSTDSFLNEYFLGGRSMGGFVLAMTLVATYGSASSFIGGPGIAYN
YGLGWVLLAMIQVPTGYFVLGVLGKKFAIISRKYNAITINDVLKARYNNKFLVWLSSISLLVFFFSAMVA
QFIGGARLIESLTGLSYLTALFIFSSSVLIYTTFGGFRAVALTDAIQGIVMFTGTTILLIAVIKAGGGVE
KIMEKLKDIDPNLITPFGGDGGLTKPFVASFWILVGIGVIGLPQTAVRCMSYKDSKAMHRAMIIGTIVVG
IIMLGMHLAGVLGRAVIPDLTVPDKVIPLLAIKVLPPILAGIFLAAPMAAIMSTVNSLLLQSSSTIIKDL
YLNYIPKEAKESKIKKISMCITLIIGLLVIIAAIKPPDLIIWLNLFAFGGLEAAFIWPIVLGLYWKRANA
TGALASMIVGVGSYITLESFKPKIFGLHNIVPSLVFALIAFIIGSLFGKKS
>gnl|CDD|273980 TIGR02120, Putative_general_secretion_pathway_protein_F, type II secretion system protein F. This membrane protein is a component of the terminal branch complex of the general secretion pathway (GSP), also known as the"Type II" secretion pathway. The GSP transports proteins (generally virulence-associated cell wall hydrolases) across the outer membrase of the bacterial cell. Transport across the inner membrane is often, but not exclusively handled by the Sec system. This model was constructed from the broader subfamily model, pfam00482 which includes components of pilin complexes (PilC) as well as other related genes. GspF is nearly always gene clustered with other GSP subunits. Some genes from Xylella and Xanthomonas strains score below the trusted cutoff due to excessive divergence from the family such that a sequence from Deinococcus which does not appear to be GspF scores higher [Protein fate, Protein and peptide secretion and trafficking]
FRYRALDAAGRAQKGTLEADSARAARLQLRERGLFPLDVDPVAAKGAGSGRKLGRRRLSRAELALFTRQL
ATLLGAGLPLEEALAALLEQAEKPRLKSVLAAIRSRVLEGKSLADALAQHPRDFPPLYRALVAAGEASGA
LDAVLERLADYLEERQALRSKITTALIYPAVLTVVAIGVVIFLLAYVVPKVVEQFAHMKQTLPLLTRALI
ALSDFLRSWGWALLAALAALVVLFRRLLRDPAFRLRFDRRLLRLPVIGRLVRGLNTARFARTLSILLSSG
VPLLRALQIARETLTNRALRAAVEDAAARVREGGSLSRALRATGLFPPLLVHMIASGEKSGQLETMLERA
ADNQEREFERRIATLTALLEPLLIVVMGGVVLFIVLAVLLPILQLNQLI
>gnl|CDD|273981 TIGR02121, Osmoregulated_proline_transporter, sodium/proline symporter. This family consists of the sodium/proline symporter (proline permease) from a number of Gram-negative and Gram-positive bacteria and from the archaeal genus Methanosarcina. Using the related pantothenate permease as an outgroup, candidate sequences from Bifidobacterium longum and several from archaea are found to be outside the clade defined by known proline permeases. These sequences, scoring between 570 and -40, define the range between trusted and noise cutoff scores [Transport and binding proteins, Amino acids, peptides and amines]
TEILITFGVYLIIMLLIGFYAYKKTTNLSDYVLGGRSLGPFVTALSAGASDMSGWLLMGLPGALYVTGLS
ELWIAIGLTIGAYINWKFVAPRLRVYTEAAHNSITLPDFFENRFNDKSRLLRIISALIILVFFTIYTSSG
LVAGGKLFESTFGLDYKTGLLIGALIIVIYTFFGGFLAVSWTDFVQGLLMFFALVLVPIVALFNLGGFGE
TLSAVAAINPHLLDMFKGASVIAIISLLAWGLGYFGQPHIIVRFMAIRSHKELPKARRIGMSWMILSLLG
AIAVGLTGIAYFNKNPHVELVDRETIFIVLSQILFHPWIAGILLAAILAAIMSTISSQLLVSSSALTEDF
YKAFFKREASQKELVMVGRLSVLVIAIIAIILAMNPNSSILNLVGYAWAGFGAAFGPVVLFSLYWKRMTR
NGALAGMIIGAVTVIVWISKLGGSFGLYEIVPGFIISSIVIVVVSKLTKAPPAAVQTVFEKAKKLVK
>gnl|CDD|273982 TIGR02122, 31_kDa_immunogenic_protein_precursor., TRAP transporter solute receptor, TAXI family. This family is one of at least three major families of extracytoplasmic solute receptor (ESR) for TRAP (Tripartite ATP-independent Periplasmic Transporter) transporters. The others are the DctP (TIGR00787) and SmoM (pfam03480) families. These transporters are secondary (driven by an ion gradient) but composed of three polypeptides, although in some species the 4-TM and 12-TM integral membrane proteins are fused. Substrates for this transporter family are not fully characterized but, besides C4 dicarboxylates, may include mannitol and other compounds [Transport and binding proteins, Unknown substrate]
MKKRLFLLGAALAIVGAALAACAGDGGEPTFVTIGTGGTGGVYYPIGGAIAQLINKKSGKLRVRVQSTGG
SVENVNLLEAGEADLAIVQSDVAYYAYEGDGEFEFEGPVEKLRALASLYPEYIQIVVRKDSGIKTVADLK
GKRVAVGAPGSGTELNARAVLKAAGLTYDDVKKVEYLGYAEAADALKDGKIDAAFYTAGTPTAAITELAT
SLDIRIVPISGEKVEKLREKYPFYRKGVIPAGTYPGQDEDVPTLAVPAALVTSSDVPEDLVYQITKAIFE
NLDELKDAHPAAQDIALETAIKGLPVPLHPGAEKYYKEVG
>gnl|CDD|273983 TIGR02123, conserved_inner_membrane_protein, TRAP transporter, 4TM/12TM fusion protein. In some species, the 12-transmembrane spanning and 4-transmembrane spanning components of tripartite ATP-independent periplasmic (TRAP)-type transporters are fused. This model describes such transporters, found in the Archaea and in Bacteria [Transport and binding proteins, Unknown substrate]
VAVLIFVLAIILSLFQLYTASFGTLSTTIFRALHLAFALPLIFLLYPATRKLKLDGVPWYDWLLALLALA
AALYLPLNYLDLLERRVGIPTTTDVVVGVLLILLVLEATRRTVGWALPILALVFLLYALFGPWLPGILRH
RGYSLEQLITHLYLTTEGIFGTPIQVSATYIFLFILFGAFLQKSGVGKFFIDLAFALAGKRRGGPAKVAV
ISSGLMGMISGSSVANVVTTGSFTIPLMKRAGYKPEFAGAVEAAASTGGQIMPPIMGAAAFIMAEFLGIP
YTEIIIAAIIPALLYFFGVFMQVHLEAKKQGLKGLSKEQLPSPKTVLKAGWYLLIPLVILIVMLLVGYSP
IRAAFYSIALTLIVSLVSFRKDTRMGLGEIFGALEDGARNAVPVAAACAGAGIIIGVVTLTGLGLKISND
LLDLAGGNLLLLLVLTMIASIILGMGLPTTANYIITATLAAPALIALGVPLIAAHMFVFYFGILADITPP
VALAAFAAAGIAGADPMKTGFEAFKLALAGYLVPFMFVYNPALLLQDSSTWLEILLAFITAIIGVLAIGA
ATSGYLLGALNLWERVLLIAAGFLLILPEWLSDLVGLAILALVFLLQLVTARRL
>gnl|CDD|273984 TIGR02124, Hydrogenase_expression/formation_protein_HypE, hydrogenase expression/formation protein HypE. This family contains HypE (or HupE), a protein required for expression of catalytically active hydrogenase in many systems. It appears to be an accessory protein involved in maturation rather than a regulatory protein involved in expression. HypE shows considerable homology to the thiamine-monophosphate kinase ThiL (TIGR01379) and other enzymes
MQQLIQELFLKAFGNEILAAMEDAAVLELSGGRLAFSTDSFVVDPLFFPGGDIGKLAVCGTVNDVAVSGA
KPLYLSCGFILEEGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIFINTTGIGVIPSGIPI
SAHNLQPGDKIIVSGTIGDHGAAILAVREGLGFETNLESDCAPLNGLVETLLNAGPAVHAMRDATRGGLA
AVLNEWAQASGVGIVIEEEKIPVKEEVKGACELLGLDPLYLANEGKLVLAVPPEAAEKVLEILKSHPYGK
DAAIIGEVVERKEGRVVLKTAYGGKRILDMPSGELLPRIC
>gnl|CDD|273985 TIGR02125, CytB-hydogenase, Ni/Fe-hydrogenase, b-type cytochrome subunit. This model describes a family of cytochrome b proteins which appear to be specific for nickel-iron hydrogenase complexes. Every genome which contains a member of this family posesses a Ni/Fe hydrogenase according to Genome Properties (GenProp0177), and most are gene clustered with other hydrogenase components. Some Ni/Fe hydrogenase-containing species lack a member of this family but contain other CytB homologs (pfam01292) which may substitute for it
YVFSAPVRIFHWVRALAIFVLIVTGFYIAYPFLSPPSGEAVHFLQGYIRFVHFAAGFVLIAVLLFRIYLA
FVGKDSRYERFSFRDPLNPKSWIQQLRWYLFLGKHPHKKGGYNPLQFVAYFGFIVLILFMILTGLALYYY
HNGLGGFLPSLFGWVEPLFGGLANVRSIHHLGMWAFVIFVPVHVYMAVREDIRSRDGVIDSMISGYRYHK
E
>gnl|CDD|273986 TIGR02126, Major_tail_protein., phage major tail protein, TP901-1 family. This family includes the members of pfam06199 but is broader. Characterized members are major tail proteins from various phage, including lactococcal temperate bacteriophage TP901-1 [Mobile and extrachromosomal element functions, Prophage functions]
AKAIKGKDILLLIRSLDGAKTSAALKPAGQTEGTISISAELIDITTKDGAGGWKGLLEGSGSIEAIISNG
DPFVDAIEDAKVNGKFFEIWEVDCREKVKEGDKYGAKYGPAYISSLEYAANHEDAVTYSISLEVNG
>gnl|CDD|273987 TIGR02127, Orotidine_5'-phosphate_decarboxylase, orotidine 5'-phosphate decarboxylase, subfamily 2. This model represents orotidine 5'-monophosphate decarboxylase, the PyrF protein of pyrimidine nucleotide biosynthesis. See TIGR01740 for a related but distinct subfamily of the same enzyme [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
FADRLNERILARRSPLCVGLDPRLELLPEWGLPSSAAGLQAFCLRIIDATAEYAAVVKPQVAFFERFGSE
GFKALEEVIAHARSLGLPVLADVKRGDIGSTASAYAKAWLGHLHADALTVSPYLGLDSLRPFLEYARANG
AGIFVLVKTSNPGGADLQDLRVSDGRTVYEEVAELAGELNESPGDCSSVGAVVGATSPGDLLRLRIEMPT
APFLVPGFGAQGAEAADLRGLFGADGSGLLINSSRGVLFAGPRSSALVAAG
>gnl|CDD|273988 TIGR02128, hypothetical_protein, bifunctional phosphoglucose/phosphomannose isomerase. This bifunctional isomerase is a member of the larger PGI superfamily and only distantly related to other glucose-6-phosphate isomerases. The family is limited to the archaea
WPEEFLEALDIVNIDEILKIYDEIVICGMGGSGIAGRIISILLLEKSFQGPVFVVKDYRLPRFVDGKTLL
IAVSYSGNTEETLSAVEEAKKKGAKVIAITSGGRLEEMAKERGLDVIKIPKGLQPRAAFPYLLTPLILML
IKPLGIDIEEAELLEGGLDTPKLKALAKRLAEEIYNRIPVIYSSSPTRPIAERWKNEINENAKSPAYYNI
LPELNHNEIEGLEDPYGLYEIVFMSDESDHSRCPKRVDITEKILGVVFISIYSRGNSLLARILSLIHLAG
YVSVKLAELRGVDPEPVPPIDKLKRRLS
>gnl|CDD|162719 TIGR02129, hisA_euk, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, eukaryotic type. This enzyme acts in the biosynthesis of histidine and has been characterized in S. cerevisiae and Arabidopsis where it complements the E. coli HisA gene. In eukaryotes the gene is known as HIS6. In bacteria, this gene is found in Fibrobacter succinogenes, presumably due to lateral gene transfer from plants in the rumen gut [Amino acid biosynthesis, Histidine family]
TKFRPCIDIHNGKVKQIVGGTLTSKKGSVLKTNFVSDKPSSYYAKLYKDDGVKGCHVIMLGPNNDDAAKE
ALHAYPGGLQVGGGINDTNAQEWLDEGASHVIVTSWLFTKGKFDLKRLKEIVSLVGKDRLIVDLSCRKTQ
DGRWIVAMNKWQTITDLELNAETLEELSKYCDEFLIHAADVEGLCKGIDEELVSKLGEWSPIPITYAGGA
KSIDDLDLVDELSKGKVDLTIGSALDIFGGNLVKFTDCVAWNK
>gnl|CDD|131185 TIGR02130, dapB_plant, dihydrodipicolinate reductase. This narrow family includes genes from Arabidopsis and Fibrobacter succinogenes (which probably recieved the gene from a plant via lateral gene transfer). The sequences are distantly related to the dihydrodipicolinate reductases from archaea. In Fibrobacter this gene is the only candidate DHPR in the genome [Amino acid biosynthesis, Aspartate family]
IQIMVNGCPGKMGKAVAEAADAAGLEIVPTSFGGEEEAENEAEVAGKEILLHGPSEREARIGEVFAKYPE
LICIDYTHPSAVNDNAAFYGKHGIPFVMGTTGGDREALAKLVADAKHPAVIAPNMAKQIVAFLAAIEFLA
EEFPGAFAGYKLEVMESHQASKADASGTAKAVIGCFQKLGFDYDMDDIEKIRDEKEQIERMGVPEEHLGG
HAFHLYHLDSADGTVHFEFQHNVCGRKIYAEGTVDAVLFLADKIIAAAEAKIFNMIDVLREGKMR
>gnl|CDD|131186 TIGR02131, PhaP_protein, polyhydroxyalkanoic acid inclusion protein PhaP. This model describes a protein found in polyhydroxyalkanoic acid (PHA) gene regions and incorporated into PHA inclusions in Bacillus cereus and Bacillus megaterium. The role of the protein may include amino acid storage (see McCool,G.J. and Cannon,M.C, 1999)
METKKYDTLIDAFWENWSKGLQLFADAGKQIEQLTLEALEQQQDALHKATEGLDALDKELKAELADFNNK
TTDNLKKLAGNALADQIEEWQDKTHEALAHLHELFFNPSKSSLSILKQAQEQFEETTKQFIEEQKKQREE
AQHQLDAFLEEFKSKQKEFAKKFEE
>gnl|CDD|131187 TIGR02132, PHA_synthase_subunit_PhaR, polyhydroxyalkanoic acid synthase, PhaR subunit. This model describes a protein, PhaR, localized to polyhydroxyalkanoic acid (PHA) inclusion granules in Bacillus cereus and related species. PhaR is required for PHA biosynthesis along with PhaC and may be a regulatory subunit
MEDQKVFDPFQAWKDAYDKTESFWGKAIGDNIKREEFSALMGNVLDLNLFYQKALNDTTGNYLEQVNVPT
KEDIANVASLVINLEEKVDLIEEFFDDKFDELEAQQEQAPALKKDVTKLKQDIKSLDKKLDKILELLEGQ
QKTQDELKETIQKQIKTQGEQLQAQLLEKQEALAAKLKAEAKEEAKPSN
>gnl|CDD|273989 TIGR02133, putative_ribose-5-phosphate_isomerase, ribose 5-phosphate isomerase. This family is a member of the RpiB/LacA/LacB subfamily (TIGR00689) but lies outside the RpiB equivalog (TIGR01120) which is also a member of that subfamily. Ribose 5-phosphate isomerase is an essential enzyme of the pentose phosphate pathway; a pathway that appears to be present in the actinobacteria. The only candidates for ribose 5-phosphate isomerase in the Actinobacteria are members of this family
MRVVLGHDHAGFEYKEALWLDLAAHEPEVCDVGVYDADDDDDYPCFCIAAAEAVARDAADLGIVIGGSGN
GEAIAANKVKGARAALAWDTASAGRARLHNNANVVGAGMRMHGLEEAFRLVFEFLGFEFDARSRHARRID
SISEYEGD
>gnl|CDD|131189 TIGR02134, transald_staph, transaldolase. This small family of proteins is a member of the transaldolase sybfamily represented by pfam00923. Coxiella and Staphylococcus lack members of the known transaldolase equivalog families and appear to require a transaldolase activity for completion of the pentose phosphate pathway [Energy metabolism, Pentose phosphate pathway]
LQKLNVKVFADGANLEEMVKFSTHPYVKGFTTNPSLMRKAGIVDYEAFAHEALAQITDLPISFEVFADDL
DEMEKEARYIASWGNNVNVKIPVTNTKGESTGPLIQKLSADGITLNVTALTTIEQVEKVCQSFTDGVPGI
VSVFAGRIADTGVDPEPHMREALEIVAQKPGVELLWASPRELFNIIQADRIGCDIITCAHDILAKLPLLG
KDLTQYSLETVQMFAKDAQSSGYSIL
>gnl|CDD|273990 TIGR02135, Uncharacterized_protein, phosphate transport system regulatory protein PhoU. This model describes PhoU, a regulatory protein of unknown mechanism for high-affinity phosphate ABC transporter systems. The protein consists of two copies of the domain described by pfam01895. Deletion of PhoU activates constitutive expression of the phosphate ABC transporter and allows phosphate transport, but causes a growth defect and so likely has some second function [Regulatory functions, Other, Transport and binding proteins, Anions]
KRFDEELKELREELLEMGGLVEEQLEDAVRALTEKDRELARKVIEDDDQINALEVKIEEKCLRLIALQQP
VAKDLRLIISIIKISSDLERIGDYAVNIAKRALRLKEEDAKPKHLEELEKMGKLALKMLKDALDAFLNKD
AELARQVAEMDERVDELYRQIFRELVTYMIEDPTNIEAALDVLLIARYLERIGDHATNIAERVIYIKTGK
IV
>gnl|CDD|273991 TIGR02136, ptsS_2, phosphate binding protein. Members of this family are phosphate-binding proteins. Most are found in phosphate ABC-transporter operons, but some are found in phosphate regulatory operons. This model separates members of the current family from the phosphate ABC transporter phosphate binding protein described by TIGRFAMs model TIGR00975 [Transport and binding proteins, Anions]
MKKRIFLLIGLAAALLAAAGCGGAIDSGIPDAKGSSTITIDGSTTVAPLAEAAAEEFQKIHPGVSVTVQG
AGSGTGIKALINGTVDIGNSSRPIKDEELQKDKQKGIKLIEHKVAVDGLAVVVNKKNVPVDDLTVEQLKK
IYSGEITNWKEVGGDLPNKPIVVVGRNAGSGTRDTFEEEVMGKAKIKPGKNEQESNGAVVSIVSSNPGAI
GYLGLGYVDDSVKTLKVNGVEPSKENIANGSYPLSRPLFMYVNGKPKKPELVAEFIDFVLSDDGGERIVE
ELGYVPL
>gnl|CDD|162723 TIGR02137, homoserine-kinase_isozyme, phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein. This protein is has been characterized as both a phosphoserine phosphatase and a phosphoserine:homoserine phosphotransferase. In Pseudomonas aeruginosa, where the characterization was done, a second phosphoserine phosphatase (SerB) and a second homoserine kinase (thrB) are found, but in Fibrobacter succinogenes neither are present. This enzyme is a member of the haloacid dehalogenase (HAD) superfamily, specifically part of subfamily IB by virtue of the presence of an alpha helical domain in between motifs I and II of the HAD domain. The closest homologs to this family are monofunctional phosphoserine phosphatases (TIGR00338)
MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPL
EGAVEFVDWLRERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAF
KSLYYRVIAAGDSYNDTTMLSEAHAGILFHAPENVIREFPQFPAVHTYEDLKREFLKASSRSL
>gnl|CDD|273992 TIGR02138, phosphate_transport_system_permease_protein_PstC, phosphate ABC transporter, permease protein PstC. The typical operon for the high affinity inorganic phosphate ABC transporter encodes an ATP-binding protein, a phosphate-binding protein, and two permease proteins. This family consists of one of the two permease proteins, PstC, which is homologous to PstA (TIGR00974). In the model bacterium Escherichia coli, this transport system is induced when the concentration of extrallular inorganic phosphate is low. A constitutive, lower affinity transporter operates otherwise [Transport and binding proteins, Anions]
EKIFKGLLLFSAVIIVLVLLLIVLFLLYEAIPAFEKNGILNFLTGTVWDPGSGPVQEQYGALPLIVGTLI
TSLIALLIAVPVGIGIAIFLSEIAPKRVRSVLKPVVELLAGIPSVVYGFWGLFVLVPFLKPHFQPFLGSN
LGLIPLFGGPILTAGIVLAIMILPTIASISRDALRAVPRSYKEASYALGATKWETIRRVILPAARSGIVG
AVVLGLGRALGETMAVTMVIGNVFPISPLSLFDPGTTITSLIANQFGEASGGSVHTSALFALGLVLFVIT
LLVNILARYIVRRRR
>gnl|CDD|131194 TIGR02139, permease_CysT, sulfate ABC transporter, permease protein CysT. This model represents CysT, one of two homologous, tandem permeases in the sulfate ABC transporter system; the other is CysW (TIGR02140). The sulfate transporter has been described in E. coli as transporting sulfate, thiosulfate, selenate, and selenite. Sulfate transporters may also transport molybdate ion if a specific molybdate transporter is not present [Transport and binding proteins, Anions]
VLPGFGLSLGVTLTYLSLIVLLPLAALFLKASQLGWAGFWQIITEPRVLAAYKLSFGTALIAALINAVFG
TLLAWVLVRYRFPGKRIVDALVDLPFALPTAVAGIALATLYSPNGWIGSFLAPLGIKIAFTPLGIVIALV
FVSLPFVVRTVQPVLEEIEKELEEAAASLGASRWQTFWRVILPALLPALLTGFALAFARAVGEYGSVIFI
AGNLPMKTEIAPLLIFQKLEQYDYAGATAIASVMLIISFVILLFINLLQWWALRY
>gnl|CDD|162725 TIGR02140, Sulfate_transport_system_permease_protein_CysW, sulfate ABC transporter, permease protein CysW. This model represents CysW, one of two homologous, tandem permeases in the sulfate ABC transporter system; the other is CysT (TIGR02139). The sulfate transporter has been described in E. coli as transporting sulfate, thiosulfate, selenate, and selenite. Sulfate transporters may also transport molybdate ion if a specific molybdate transporter is not present [Transport and binding proteins, Anions]
VRYLLISLALGLLFLLLLLPLALIFQEAFEKGFGVFFAAISDPDALSAIKLTLLVALIVVPLNTVFGVCA
AWVLTRFQFPGKRLLLTIIDLPFSVSPVVAGLIFVLLYGSQGWLGPWLEDLDIKIIFSLPGIVLATMFVT
CPFVARELIPVMEEQGTEQEEAALTLGASWWQTFWRVTLPNIKWGLLYGVILCNARAMGEFGAVSVVSGH
IRGKTNTLPLHVELLYNEYQSYAAFAAASLLALLALVTLVLKAILERRQGR
>gnl|CDD|273993 TIGR02141, modB_ABC, molybdate ABC transporter, permease protein. This model describes the permease protein, ModB, of the molybdate ABC transporter. This system has been characterized in E. coli, Staphylococcus carnosus, Rhodobacter capsulatus and Azotobacter vinlandii. Molybdate is chemically similar to sulfate, thiosulfate, and selenate. These related substrates, and sometimes molybdate itself, can be transported by the homologous sulfate receptor. Some apparent molybdenum transport operons include a permease related to this ModB, although less similar than some sulfate permease proteins and not included in this model [Transport and binding proteins, Anions]
WLSLKVAVIATLLLLPLGIPVAWLLARSRFRGKPLLEVLVTLPLVLPPTVLGFYLLIAFGPNGPIGKLLE
LFGISLVFTFTGAVLASVIVSFPLMVQPIRAAFEAVDPDLEEAARTLGASESQTFLKVTLPLAFPGLLAG
AVLSFARALGEFGATLMFAGNIPGETQTIPLAIYDAVESDYELAHQLSLVLLAISLIVLLLVELLNKR
>gnl|CDD|131197 TIGR02142, Molybdenum_import_ATP-binding_protein_ModC, molybdenum ABC transporter, ATP-binding protein. This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter [Transport and binding proteins, Anions]
LSARFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFL
PPEKRRIGYVFQEARLFPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRV
AIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV
AAAGPIAEVWASPDLPWLAREDQGSLIEGVVAEHDQHYGLTALRLGGGHLWVPENLGPTGARLRLRVPAR
DVSLALQKPEATSIRNILPARVVEIEDSDIGRVGVVLESGGKTLWARITRWARDELGIAPGTPVFAQIKA
VALR
>gnl|CDD|131198 TIGR02143, tRNA/tmRNA_uracil-C5-methyltransferase, tRNA (uracil(54)-C(5))-methyltransferase. This family consists exclusively of proteins believed to act as tRNA (uracil-5-)-methyltransferase. All members of far are proteobacterial. The seed alignment was taken directly from pfam05958 in Pfam 12.0, but higher cutoffs are used to select only functionally equivalent proteins. Homologous proteins excluded by the higher cutoff scores of this model include other uracil methyltransferases, such as RumA, active on rRNA [Protein synthesis, tRNA and rRNA base modification]
QYTAQLAEKVSRLKDLFAPFDAPEPEVFESPDKHYRMRAEFRIWHEGDDLYYAMFDQQTKSKIRVDQFPA
ASELINRLMPALIAALRQNPALRHKLFQVDFLTTLSGEALVSLLYHKQLDDEWRQAAEALKDIKLNVNLI
GRARKKKIVLDQDYVDETLPVAGREFIYRQVENSFTQPNAAVNIKMLEWACEVTQGSKGDLLELYCGNGN
FSLALAQNFRRVLATEIAKPSVNAAQYNIAANNIDNVQIIRMSAEEFTQAMNGVREFRRLKGIDLKSYNC
STIFVDPPRAGLDPDTCKLVQAYERILYISCNPETLKANLEQLSETHRVERFALFDQFPYTHHMECGVLL
ERK
>gnl|CDD|273994 TIGR02144, lysine_biosynthesis_enzyme, Lysine biosynthesis enzyme LysX. The family of proteins found in this equivalog include the characterized LysX from Thermus thermophilus, which is part of a well-organized lysine biosynthesis gene cluster. LysX is believed to carry out an ATP-dependent acylation of the amino group of alpha-aminoadipate in the prokaryotic version of the fungal AAA lysine biosynthesis pathway. No species having a sequence in this equivalog contains the elements of the more common diaminopimelate lysine biosythesis pathway, and none has been shown to be a lysine auxotroph. These sequences have mainly recieved the name of the related enzyme, "ribosomal protein S6 modification protein RimK". RimK has been characterized in E. coli, and acts by ATP-dependent condensation of S6 with glutamate residues
IAILYDIIRPDEKMLIEELEKLGLPYRVIYVPALPLPFGERPRALEDVDVAIIRCVSQSRALYSARLLEA
LGVPVINSSHAIEACGDKIFTYLKLAKAGVPTPRTYLAFDREAALKAAEALGYPVVLKPVIGSWGRLVAK
VRDRDEAEALLEHKEVLGGSQLKLFYIQEYINKPGRDIRVFVIGDEAIAAIYRYSNHWRTNTARGGKAEP
CPLDEEIEELAVKAAEAVGGGVVAIDIFESKERGLLVNEVNHVPEFKNSVRVTGVNVAGEILEYAVEVVK
>gnl|CDD|273995 TIGR02145, Fib_succ_major, Fibrobacter succinogenes major paralogous domain. This domain of about 175 to 200 amino acids is found, in from one to five copies, in over 50 proteins in Fibrobacter succinogenes S85, an obligate anaerobe of the rumen. Many members of this family have an apparent lipoprotein signal sequence. Conserved cysteine residues, suggestive of disulfide bond formation, are also consistent with an extracytoplasmic location for this domain. This domain can also be found in small numbers of proteins in Chlorobium tepidum and Bacteroides thetaiotaomicron [Cell envelope, Other]
TLVDSRDGQVYKTVKIGSQTWMAENLNYETEGSWCYEDDEENCAKYGRLYTWAAAMDSICPEGWHLPSTT
EWNTLFDAVGGKVNAGGKLKARSGWSKSGNGTDDYGFSALPAGYRFSDGEFSDDGEYAFFWSSDEENEDS
AYYMYLRYSSDGIFLIGEDKDDGLSVRCVKD
>gnl|CDD|162728 TIGR02146, Putative_homocitrate_synthase, homocitrate synthase. This model includes the yeast LYS21 gene which carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway. A related pathway is found in Thermus thermophilus. This enzyme is closely related to 2-isopropylmalate synthase (LeuA) and citramalate synthase (CimA), both of which are present in the euryarchaeota. Some archaea have a separate homocitrate synthase (AksA) which also synthesizes longer homocitrate analogs
IIDSTLREGEQFPGANFSTEQKIEIAKALDEFGIDYIEVTHPAASKQSRIDIEIIASLGLKANIVTHIRC
RLDDAKVAVELGVDGIDIFFGTSKLLRIAEHRSDAKSILESARETIEYAKSAGLEVRFSAEDTFRSELAD
LLSIYETVGVFGVDRVGIADTVGKAAPRQVYELIRTVVRVVPGVDIELHAHNDTGCAVANAYNAIEGGAT
IVDTTVLGIGERNGITPLGGILARLYYHTPMYVYKLGKLIELTRMVAGEVGVTIPFNNPITGELAFTHKA
GIHVKAILGNPRTYEFLPPEVFGRKRHILIARLTGKHAIKARKEKLGVKLIEEELKRVTAKIKS
>gnl|CDD|273996 TIGR02147, Fsuc_second, TIGR02147 family protein. This family consists of the 40 members of a paralogous protein family in the rumen anaerobe Fibrobacter succinogenes S85 and a smaller number in Bdellovibrio bacteriovorus HD100. Member proteins are about 270 residues long and appear to lack signal sequences and transmembrane helices. The only perfectly conserved residue is a glycine in an otherwise poorly conserved region, suggesting members are not enzymes. The family is not characterized [Hypothetical proteins, Conserved]
MKDIFEYTDYRKYLRDYYEERKKTDPAFSWRFFAEKAGFSSTSYLNDIIKGKKNLTKRMIPKFAEALGLD
EKEAAYFEAMVNFGQAKTDTEKQQFFEEMQALKPRPRLRVLAADQFEYYRHWYNSVIRELLGVMPFADDP
EELAKRCFPKISAEQVKESLDLLERLGLIKKNEDGFYKQTDKAVSTGDEVIPLAVRQYQKQMIDLAKEAL
DALPPSERDVSTVTFGISEEAYKEIVKKIQEFRKEVLAIATKDKEEDRVFQLNIQLFPLSK
>gnl|CDD|162730 TIGR02148, ORFveg106_random, fibro-slime domain. This model represents a conserved region of about 90 amino acids, shared in at least 4 distinct large putative proteins from the slime mold Dictyostelium discoideum and 10 proteins from the rumen bacterium Fibrobacter succinogenes, and in no other species so far. We propose here the name fibro-slime domain
YHNFHFCMKINAQFKYVGGQYFEFRGDDDVWVFINNKLVVDIGGQHPAVPGAVDLDTLGLKEGKTYPFDI
FYCERHTTGSNFRIRTSIQL
>gnl|CDD|273997 TIGR02149, glgA_Coryne, glycogen synthase, Corynebacterium family. This model describes Corynebacterium glutamicum GlgA and closely related proteins in several other species. This enzyme is required for glycogen biosynthesis and appears to replace the distantly related TIGR02095 family of ADP-glucose type glycogen synthase in Corynebacterium glutamicum, Mycobacterium tuberculosis, Bifidobacterium longum, and Streptomyces coelicolor [Energy metabolism, Biosynthesis and degradation of polysaccharides]
MKVTVLTREYPPNVYGGAGVHVEELTRELARLMDVDVRCFGDQRFDSEGLTVKGYRPWSELKEANKALGT
FSVDLAMANDPVDADVVHSHTWYTFLAGHLAKKLYDKPLVVTAHSLEPLRPWKEEQLGGGYKLSSWAEKT
AIEAADRVIAVSGGMREDILKYYPDLDPEKVHVIYNGIDTKEYKPDDGNVVLDRYGIDRSRPYILFVGRI
TRQKGVPHLLDAVHYIPKDVQVVLCAGAPDTPEVAEEVRQAVALLDRNRTGIIWINKMLPKEELVELLSN
AEVFVCPSIYEPLGIVNLEAMACGTPVVASATGGIPEVVVDGETGFLVPPDNSDADGFQAELAKAINILL
ADPELAKKMGIAGRKRAEEEFSWGSIAKKTVEMYRKVL
>gnl|CDD|273998 TIGR02150, Isopentenyl-diphosphate_Delta-isomerase_II, isopentenyl-diphosphate delta-isomerase, type 1. This model represents type 1 of two non-homologous families of the enzyme isopentenyl-diphosphate delta-isomerase (IPP isomerase). IPP is an essential building block for many compounds, including enzyme cofactors, sterols, and prenyl groups. This inzyme interconverts isopentenyl diphosphate and dimethylallyl diphosphate [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
VILVDENDNPIGTASKAEVHLQETPLHRAFSVFLFNEEGELLLQRRASSKITWPGVWTNSCCSHPLPGEL
EAAIRRLRHELGIPADDVPLTVLPRFSYRARDDAWGEHELCPVFFARANVDLNPNPEVAEYRWVSLEELK
EILAKPWAGFSPWFRIQA
>gnl|CDD|273999 TIGR02151, Isopentenyl-diphosphate_delta-isomerase, isopentenyl-diphosphate delta-isomerase, type 2. Isopentenyl-diphosphate delta-isomerase (IPP isomerase) interconverts isopentenyl diphosphate and dimethylallyl diphosphate. This model represents the type 2 enzyme. FMN, NADPH, and Mg2+ are required by this form, which lacks homology to the type 1 enzyme (TIGR02150). IPP is precursor to many compounds, including enzyme cofactors, sterols, and isoprenoids [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
ERKDEHIELCLKQNVEYGGSTGFDDITLIHNALPEINLDDIDLTTEFLGKRLKAPFYINAMTGGSEEAGK
INRNLARAARELGIPMGVGSQRAALKDPETADTFEVVREEAPNGPLIANIGAPQLVEGGPEEAQEAIDMI
EADALAIHLNVLQELVQPEGDRNFKGWLEKIAEICSQLSVPVIVKEVGFGISKEVAKLLADAGVSAIDVA
GAGGTSWAQVENYRAKGSNLASFFNDWGIPTAASLLEVRSDAPDAPIIASGGLRTGLDVAKAIALGADAV
GMARPFLKAALDEGEEAVIEEIELIIEELKVAMFLTGAKTIAELKKVPLVISG
>gnl|CDD|274000 TIGR02152, Putative_ribokinase, ribokinase. This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not [Energy metabolism, Sugars]
GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSN
GIDTEYVGTVKDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVL
EAAKIAKKHGVKVILNPAPAIKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKN
VIITLGSKGALLVSKDESKLIPAFKVKAVDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRK
GAQSSIPYLEEVE
>gnl|CDD|274001 TIGR02153, Glutamyl-tRNAGln_amidotransferase_subunit_D, glutamyl-tRNA(Gln) amidotransferase, subunit D. This peptide is found only in the Archaea. It is part of a heterodimer, with GatE (TIGR00134), that acts as an amidotransferase on misacylated Glu-tRNA(Gln) to produce Gln-tRNA(Gln). The analogous amidotransferase found in bacteria is the GatABC system, although GatABC homologs in the Archaea appear to act instead on Asp-tRNA(Asn) [Protein synthesis, tRNA aminoacylation]
VFEGVVMPSYELSDDDIIVLKLKNGYNIGFKISEIRNIEVLEEGSEPREVPPPAEIEKKPGLPKVSIIST
GGTIASRVDYETGAVYPAFTAEELARAVPELLEIANIKARAVFNILSENMKPEYWIKIAEAVAKALKEGA
DGVVVAHGTDTMAYTAAALSFMFETLPVPVVLVGAQRSSDRPSSDAALNLICAVRAATSPIAEVTVVMHG
ETSDTYCLVHRGVKVRKMHTSRRDAFQSINDIPIAKIDPDEGIEKLRIDYRRRGEKELELDDKFEEKVAL
VKFYPGISPEIIEFLVDKGYKGIVIEGTGLGHVSEDWIPSIKRATDDGVPVVMTSQCLYGRVNLNVYSTG
RELLKAGVIPCEDMLPEVAYVKLMWVLGQTDDLEEVRKMMRTNIAGEINERTLP
>gnl|CDD|131209 TIGR02154, PhoB, phosphate regulon transcriptional regulatory protein PhoB. PhoB is a DNA-binding response regulator protein acting with PhoR in a 2-component system responding to phosphate ion. PhoB acts as a positive regulator of gene expression for phosphate-related genes such as phoA, phoS, phoE and ugpAB as well as itself. It is often found proximal to genes for the high-affinity phosphate ABC transporter (pstSCAB; GenProp0190) and presumably regulates these as well [Regulatory functions, DNA interactions, Signal transduction, Two-component systems]
MTRRILVVEDEPAIRELIAYNLEKAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRR
RPETRAIPIIMLTARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVLRRIRPQLSDEVIEVGDLSLD
PVAHRVFRGGQPLSLGPTEFRLLHFFMTHPERVYSREQLLDRVWGRDVYVEERTVDVHIRRLRKALNPFG
LEDPVQTVRGAGYRFS
>gnl|CDD|131210 TIGR02155, Phenylacetate-coenzyme_A_ligase, phenylacetate-CoA ligase. Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in aromatic catabolism of phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Often located in a conserved gene cluster with enzymes involved in phenylacetic acid activation (paaG/H/I/J), phenylacetate-CoA ligase has been found among the proteobacteria as well as in gram positive prokaryotes. In the B-subclass proteobacterium Azoarcus evansii, phenylacetate-CoA ligase has been shown to be induced under aerobic and anaerobic growth conditions. It remains unclear however, whether this induction is due to the same enzyme or to another isoenzyme restricted to specific anaerobic growth conditions [Energy metabolism, Other]
ETASLDELRALQTQRLKWTVKHAYENVPHYRKAFDAAGVHPDDLQSLSDLAKFPFTQKHDLRDNYPFGLF
AVPREQVVRIHASSGTTGKPTVVGYTQNDIDTWSSVVARSIRAAGGRPGDLIHNAYGYGLFTGGLGAHYG
AEKLGCTVVPISGGQTEKQVQLIQDFKPDIIMVTPSYMLNLLEELKRMGIDPAQTSLQVGIFGAEPWTNA
MRKEIEARLGMKATDIYGLSEVIGPGVAMECVETQDGLHIWEDHFYPEIIDPHTGEVLPDGEEGELVFTT
LTKEALPVIRYRTRDLTRLLPGTARTMRRMDRITGRSDDMLIIRGVNVFPTQLEEVILKMDELSPHYQLE
LTRNGHMDELTLKVELKPESYTLRLHEQASLLAGEIQHTIKQEVGVSMDVHLVEPGSLPRSEGKARRVVD
LR
>gnl|CDD|131211 TIGR02156, PA_CoA_Oxy1, phenylacetate-CoA oxygenase, PaaG subunit. Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA [Energy metabolism, Other]
FQAKIDAGEKIEAKDWMPAAYRKTLIRQISQHAHSEIVGMLPEGNWITRAPTLKRKLILMAKVQDEAGHG
LYLYAAAETLGVSREELLDALLTGKAKYSSIFNYPTLTWADIGVIGWLVDGAAIMNQTPLCRCSYGPYSR
AMVRICKEESFHQRQGYEIMLTLARGTQEQRQMAQDALNRWWWPSLMMFGPHDADSPNSGQSTKWKIKRN
SNDELRQKFIDATVPQLESLGLTIPDPELKQNEERGHWVYGEIDWDEFKQVIKGNGPCNKERLATRRKAH
EEGAWVREA
>gnl|CDD|274002 TIGR02157, 12-phenylacetyl-CoA_epoxidase_subunit_B, phenylacetate-CoA oxygenase, PaaH subunit. Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA [Energy metabolism, Other]
WPLYEVFVRSKSGLPHQHVGSLHAPDEEMALMMARDNYTRREEGVSIWVVKASHIVASTPDEREEFFDPA
EDKVYRHPTFYGIPDRVWHM
>gnl|CDD|131213 TIGR02158, 12-phenylacetyl-CoA_epoxidase_subunit_C, phenylacetate-CoA oxygenase, PaaI subunit. Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA [Energy metabolism, Other]
LGDDALVLAQRGGEWCGHAPELEEDIALANIALDLLGHARMFLSLAGQLGGGDEDTLAFFRDEAEFRNLR
LTELPNGDFALTIARQFLYDAYKVLLLEALTQSRDVPLAAIAAKALKEARYHLQHAKTWLERLGLGTEES
HRRLQEALNELWPYTAELFEAGPIDEELAEAGIAVDPATLQAAWEKEVNAVLNEATLTLPQQTFYRSNGR
NGEHTEHLGPLLAEMQELQRSHPGAQW
>gnl|CDD|131214 TIGR02159, Putative_12-phenylacetyl-CoA_epoxidase_subunit_D, phenylacetate-CoA oxygenase, PaaJ subunit. Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA [Energy metabolism, Other]
VPDPEIPVVSVTDLGMVREVDVDGGGVVVKFTPTYSGCPALEVIRQDIRDAVRALGVEVVEVSTSLDPPW
TTDWITEDAREKLREYGIAPPAGHYVVGVSPEPPSVQCPRCGSADTTITSIFGPTACKALYRCRACKEPF
EYFKPI
>gnl|CDD|131215 TIGR02160, 12-phenylacetyl-CoA_epoxidase_subunit_E, phenylacetate-CoA oxygenase/reductase, PaaK subunit. Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA [Energy metabolism, Other]
FHRLTVAEVERLTADAVAISFEIPDELAEDYRFAPGQHLTLRREVDGEELRRSYSICSAPAPGEIRVAVK
KIPGGLFSTWANDEIRPGDTLEVMAPQGLFTPDLSTPHAGHYVAVAAGSGITPMLSIAETVLAAEPRSTF
TLVYGNRRTASVMFAEELADLKDKHPQRFHLAHVLSREPREAPLLSGRLDGERLAALLDSLIDVDRADEW
FLCGPQAMVDDAEQALTGLGVPAGRVHLELFYTDDEPGREVRHEVSGPEGDVSKVTVTLDGRSTETSSLS
RDESVLDAALRARPDLPFACKGGVCGTCRAKVLEGKVDMERNYALEPDEVDAGYVLTCQAYPLSDKLVVD
YD
>gnl|CDD|131216 TIGR02161, Cytochrome_c-type_protein_NapC, periplasmic nitrate (or nitrite) reductase c-type cytochrome, NapC/NirT family. Nearly every member of this subfamily is NapC, a predicted membrane-anchored four-heme c-type cytochrome that forms one component of the periplasmic nitrate reductase along with NapA, NapB, NapD, NapE, and NapF subunits. A single known exception at this time is NirT, which is instead a component of a nitrite reductase. This family excludes TorC subunits of trimethylamine N-oxide (TMAO) reductases
LLKRFWKWLRRPSRLALGTLLLGGFVGGIVFWGGFNTGLEATNTEEFCISCHEMRDNVYPEYRETIHYSN
RSGVRATCPDCHVPHEWTDKMARKVQASKEVWGHLFGTIDTREKFEAHRLELAEREWARMKANDSLECRN
CHNFEAMDFTRQKARAAKMHSRALTEGKTCIDCHKGIAHQLPDMS
>gnl|CDD|274003 TIGR02162, Cytochrome_c-type_protein_TorC, trimethylamine-N-oxide reductase c-type cytochrome TorC. This family includes consists of TorC, a pentahemic c-type cytochrome subunit of periplasmic reductases for trimethylamine-N-oxide (TMAO). The N-terminal half is closely related to tetrahemic NapC (or NirT) subunits of periplasmic nitrate (or nitrite) reductases; some species have both TMAO and nitrate reductase complexes
GKIWKAFTRPSAKWGLGVLVVIGFIAGAIGWNGFHYVVEKTSTTEFCISCHSMQNVYEEYKQTVHWQNTS
GVRAECADCHVPHDGTAKYARKLQASKDVFAEIRGTIDTPEKFEAHRLEMAEREWARMKANDSATCRTCH
SYEAMDFAKQSPEARKQMKQAANEDQSCIDCHKGIAHKLPDMASGSRGLFSKLEKAAQSLKPRKGETLYS
LRTIPAYLDKPEKAKADGRLLPASPVKVVKVTGDWVQVEITGWRKSKGFGRVIYEKFGKRIFVASLAKEA
TQSVTTLAKMVDPDTGLTWTQVSATAWMKKRDLTNDIKPVWAYAKSMYNGACSMCHVQPEPAHFDANTWI
GTLNGMKGFTNLDKEQERLVLRYLQMHASDFEPEGH
>gnl|CDD|274004 TIGR02163, Ferredoxin-type_protein_NapH_homolog, ferredoxin-type protein, NapH/MauN family. Most members of this family are the NapH protein, found next to NapG,in operons that encode the periplasmic nitrate reductase. Some species with this reductase lack NapC but accomplish electron transfer to NapAB in some other manner, likely to involve NapH, NapG, and/or some other protein. A few members of this protein are designated MauN and are found in methylamine utilization operons in species that appear to lack a periplasmic nitrate reductase
FLILRRLVQLSILGLFLLGPYAGVWILKGNLSSSRLLGTIPLSDPLITLQILLAGHSPPTNALIGALIIV
AFYALFGGRAFCSWVCPVNLVTDFAAWLRRKLGINKIIKLPRNLRYWVLVLFLLLSFLSGLLIWEWFNPV
GILHRGIIFGMGAGIWLILLVFLFDLLFSERGWCGHLCPLGAFYGLIGRKSLIKIAASDREKCTNCMDCF
NVCPEPQVLRMPLKKGGSTLVLSGDCTLCGRCIDVCHEDVLGFTT
>gnl|CDD|131219 TIGR02164, Trimethylamine-N-oxide_reductase_1, trimethylamine-N-oxide reductase TorA. This very narrowly defined family represents TorA, part of a family of related molybdoenzymes that include biotin sulfoxide reductases, dimethyl sulfoxide reductases, and at least two different subfamilies of trimethylamine-N-oxide reductases. A single enzyme from the larger family may have more than one activity. TorA typically is located in the periplasm, has a Tat (twin-arginine translocation)-dependent signal sequence, and is encoded in a torCAD operon
MSRRDFLKGIASSSAAVLGGPSLLTPLNALAAAAINEDEWKTTGSHWGAFRAKVKNGKVVEVKPFELDKY
PTEMINGIRGMVYNPSRVRYPMVRLDWLKKRHKSNTHQRGDNRFVRVTWDEALDLFYEELERVQKQYGPS
ALHAGQTGWRSTGQFHSCTSHMQRAVGMHGNYVKKIGDYSTGAGQTILPYVLGSTEVYAQGTSWPLILEN
SDTIVLWANDPVKNLQVGWNCETHESFAYLAQLKEKVAAGEINVISIDPVVTKTQAYLGCEHLYVNPQTD
VALMLALAHTLYSENLYDKKFIEGYCLGFEEFLPYVLGSKDGVAKTPEWAAKICGVEAEVIRDLARMLVK
GRTQLIFGWCIQRQQHGEQPYWMGAVLAAMIGQIGLPGGGISYGHHYSSIGVPSSGAAAPGAFPRNLDEG
QKPKFDNSDFKGYSSTIPVARWIDAILEPGKTIDHNGSKVTYPPIKMMIFSGCNPWHHHQDRNRMKQAFQ
KLETVVTIDVSWTATCRFSDIVLPACTQFERNDIDVYGSYSNRGIIAMQKLVDPLFDSRSDFEIFTELCR
RFGKEKEYTRNMDEMEWLKTLYNECKQANAGKFEMPDFAEFWKKGYVHFGDGEPWVRHADFREDPEINPL
GTPSGLIEIFSRKIAQYGYDDCKGHPMWFEKTERSHGGPGSDKHPFWLQSCHPDKRLHSQMCESEALRET
YAVQGREPVYINPVDAKARGIKDGDLVRVFNDRGQLLAGAVVSDNFPKGVVRIHEGAWYGPLGGEEVGAL
CTYGDPNTLTLDIGTSKLAQATSANTCLVEFEKYQGKVPKVTSFDGPIEVEI
>gnl|CDD|274005 TIGR02165, CRISPR-associated_protein_GSU0054_family, CRISPR-associated protein GSU0054/csb2, Dpsyc system. This model represents a CRISPR-associated protein from the Dpsyc subtype (a type I-C variant), named for Desulfotalea psychrophila LSv54. CRISPR systems confer resistance in prokaryotes to invasive DNA or RNA, including phage and plasmids. CRISPR-associated proteins typically are found near CRISPR repeats and other CRISPR-associated proteins, have low levels of sequence identify, have sequence relationships that suggest lateral transfer, and show some sequence similarity to DNA-active proteins such as helicases and repair proteins
MLVLEIRFLLGRYHGASDDGEPEWPPSPARLFQALVAAAARGRTGELSDEALAALKWLEALPPPAIRAPE
AVLGAPPVRYVPVNDADGPTSLKAPRVKKKIRPISVGVPSSDPVGYLWPDVPPDDLLATLERLAARIPYL
GRSTSLVRARVVELDDLPELLLVRPNWVPLPDGRAVRLRVPAPGRLDALIEAYEAKFQAKLKSDVFPVGP
PPPLPALRRITYLPPELAFTYPDRPWSLLRILRARATALTLRLTDAVTWCDALHRALISRWADPAPPIVT
GHGADRAGAKEPANRQHVAYLPLPSVGHRHADGHLLGSAVALFPPTGLDADERIWLRRALDGRALRLGGL
WRLPLVLLGDSPRSLDVQRWPAPRPARIWATVTPVVLPRRPKKRGHVFRDEFETEAAGQVRKALRRAGLP
EPSAIQPLAASLVAGAPRAYQFRVPRYLPRRQLYHVVISFPEPVRGPLALGAGRHLGLGLFAPE
>gnl|CDD|274006 TIGR02166, Putative_dimethyl_sulfoxide_reductase_chain_YnfE, anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family. Members of this family include known and probable dimethyl sulfoxide reductase (DMSO reductase) A chains. In E. coli, dmsA encodes the canonical anaerobic DMSO reductase A chain. The paralog ynfE, as part of ynfFGH expressed from a multicopy plasmid, could complement a dmsABC deletion, suggesting a similar function and some overlap in specificity, although YnfE could not substitute for DmsA in a mixed complex
ISRRHFLKTSAALGGLAAASGALSLPFSVNAAAEATPTGPDEKVVWSACTVNCGSRCPLRVHVKDGEITR
IETDNTGDDEYGNHQVRACLRGRSMRRRVYNPDRLKYPMKRVGKRGEGKFERISWDEATDTIADNLKRII
EKYGNEAIYVNYGTGTTGGTMSRSWPPTAVARLLNLCGGYLNQYGSYSTAQINEAMPYTYGISADGSSLD
DIENSKLVVMFGNNPAETRMSGGGQTYYFLQALEKSNARVIVIDPRYTDTVAGREDEWIPIRPGTDAALV
AAIAYVMISENLHDQAFLDRYCVGFDEKTLPASAPKNGSYKDYILGEGADGTPKTPEWASKITGIPADTI
IKLAREIGNAKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVGIKGGNNGAREGNYSLPFARMPELPN
PVKTSISCFLWTDAIDRGTEMTAIKDGVRGKDKLDSNIKFLWNYAGNCLINQHSDINRTHKILQDESKCE
MIVVIDNHMTSSAKYADILLPDTTTLEQNDFIEDSYASNMSYLIFMQKAIEPLFECKPIYDMLSEVAKRL
GVEAEFTEGRTQEEWLEHLYAQTRAADPALPSFAELRKQGIYKAKSAPGPFVAFEDFRRDPEANPLKTPS
GKIEIYSERLAQIAHTWELPEGDVITPLPEYVPTFEGPDDPLRKDFPLQLTGFHYKGRTHSTYGNVDWLR
EAAPQELWINPIDAQKRGITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQGAWYQPDKNGIDVGGCI
NTLTTQRPSPLAKGNPQHTNLVEVEKA
>gnl|CDD|274007 TIGR02167, cell_surface_protein_precursor, bacterial surface protein 26-residue repeat. This model describes a tandem peptide repeat sequence of 25 or 26 residues, found in predicted surface proteins (often lipoproteins) from Listeria monocytogenes, L. innocua, Enterococcus faecalis, Lactobacillus plantarum, Mycoplasma mycoides, Helicobacter hepaticus, and other species
MFSGCSSLTSLDLSNWDTSNVTNMSS
>gnl|CDD|274008 TIGR02168, Chromosome_partition_protein_Smc, chromosome segregation protein SMC, common bacterial type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSET
RKPLSLAEVELVFDNSDGLLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSI
IEQGKISEIIEAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAE
KAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE
EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK
EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ
QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR
LDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKK
AIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD
LDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKAL
AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL
EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL
EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR
SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK
IKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFP
KLFGGGEAELRLTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEV
DAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKGVSKIVSVDL
>gnl|CDD|274009 TIGR02169, chromosome_segregation_protein_related_ptotein, chromosome segregation protein SMC, primarily archaeal type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNG
QSGNEAYVTVTFKNDDGKFPDELEVVRRLKVTDDGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNVVL
QGDVTDFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA
ERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK
IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK
RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE
ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR
ELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVA
KEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIE
AARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRI
ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL
EEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE
QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA
QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQE
YEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELSGGTGELILENP
DDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKL
IREKAGEAQFIVVSLRSPMIEYADRAIGVTMRRNGESQVFGLKL
>gnl|CDD|274010 TIGR02170, Thymidylate_synthase_ThyX, thymidylate synthase, flavin-dependent. Two forms of microbial thymidylate synthase are known: ThyA (2.1.1.45) and ThyX (2.1.1.148). This model describes ThyX, a homotetrameric flavoprotein. Both enzymes convert dUMP to dTMP. Under oxygen-limiting conditions, thyX can complement a thyA mutation [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
FVKLIDYTPGPDALIVQAARVSYSSFEKDKPGTATDAGLIDYLLRHGHFSPLEHASFTFEVKGASRSVAA
QLTRHRIASYSVQSQRYVLLRNEAPEGERVVVPPSVNDTNLDEKPEEVVEKAYAEAEDHYRASYELYRKL
LEAGIAREDARFVLPNALYTHIVVTGNARSLMHFLDLRASNDAQWEIRELAEAMLDIVKEVAPWVFEAF
>gnl|CDD|274011 TIGR02171, Fb_sc_TIGR02171, Fibrobacter succinogenes paralogous family TIGR02171. This model describes a paralogous family of the rumen bacterium Fibrobacter succinogenes. Eleven members are found in Fibrobacter succinogenes S85, averaging over 900 amino acids in length. More than half are predicted lipoproteins. The function is unknown
IKFLVASLLVFGLWTSCSDSSSSECSNDPEDEEPSVDGFVYVKGKKSTTLGTDDISAKSNESPKMTVQLT
YDFYIGRHEVTCGEFNDLMKGETGFKVPCKEDKLPATNVTFYDAVLYANALSKSEGLDTVYTYTSANFDA
SGHCVNLEGLAFHPEVKGYRLPTEAEWIYVASQSWDPEKSWNSDNSSSEAHEVCTSPDNPGNVCDMAGNV
LEWVNDWLASFKDTTLTNYVGSSDPGSLGERVVKGGSYRNSPSAINLYTRGDVYPVTSSTKGDYVGFRLV
LGAIPDATWLDESGKVATSKIKSLATSSEIRELTGTYKAKLAFRNDVTGNLAYIDYTKGASRAVEIEDTI
SVYHPDISPDGKKVAFCTGIEGLPGKSSVYVRNLNASGSGLVKLPVENAAIPRWRVLENGDTVIVYVSDA
SNNKDDATFAAYSTWQVPFANGKFGTPKKLFDGAYHGGVSEDLNLAVSGARLLRAHVANEDVDNGKDDVW
YNGEQACNASLAKDGSKRTLFLDFGGSTGQAFVGQKYGVHERLLVADSKGKLVRAVAAPAGYTFDHTEWV
TGRSNLAVATLTNVNGAHKKIALINLSDSKVTELVEGDELWHPCLWVEQDNSSKYSLDLDLDSAGVYYDS
YAQFADFSLRYKMQLFWQFRDSIEVLALGSSRTLNAVYPTSIKSKFALNMGYSGGDIHASLYLLMNYAIP
HAKKLKYVVVELSLDFWWNTATEDTNAKYLLYPGFVYDENHNFWANGLPTPFVDAVKEGILYPSALRCDY
IIRGRFLLPTSCWGSWPVANFDATISDPGQQIINENMNSLKAFIDETAKKGVKVIGTIFPQSPGYKNTGS
FGRYGPRRSIAKKIIDSFKKMEKTYPHFILFDENKDGLHDYTDDMANNSDHLSDEGAKQFTYRLDSLLKK
LK
>gnl|CDD|162743 TIGR02172, Fb_sc_TIGR02172, Fibrobacter succinogenes paralogous family TIGR02172. This model describes a paralogous family of five proteins, likely to be enzymes, in the rumen bacterium Fibrobacter succinogenes S85. Members show homology to proteins described by pfam01636, a phosphotransferase enzyme family associated with resistance to aminoglycoside antibiotics
IDLSDWTQTGEGGNGESYTHKTGKWMLKLYNPGFDKETIKREFDASRKVFSLGIPTPHPFDLVEDGGRLG
LIYELIVGKRSFSRIISDNPSRLEEIAKIFAEMAKKLHSTKCDTSTFQSYKEKIRKFIEEKDFVPKDYKE
KARAFIKEVPDTSTCLHGDFQIGNLITSGKGTYWIDLGDFGYGNPLFDLGLLFMFCHYLDDDKLQAIFHM
NAEQLKAHWNIFAKAY
>gnl|CDD|274012 TIGR02173, cyt_kin_arch, cytidylate kinase, putative. Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017
MIITISGPPGSGKTTVAKILAEKLSLKLISAGDIFRELAAKMGLDLIEFLNYAEENPEIDKKIDRRIHEI
ALKEKNVVLESRLAGWIVREYADVKIWLKAPLEVRARRIAKREGKSLTVARSETIEREESEKRRYLKFYG
IDIDDLSIYDLVINTSNWDPNNVDIILDALD
>gnl|CDD|274013 TIGR02174, Putative_selT-like_protein_F28H7.4, selT/selW/selH selenoprotein domain. This model represents a domain found in both bacteria and animals, including animal proteins SelT, SelW, and SelH, all of which are selenoproteins. In a CXXC motif near the N-terminus of the domain, selenocysteine may replace the second Cys. Proteins with this domain may include an insert of about 70 amino acids. This model is broader than the current SelW model pfam05169 in Pfam
VEVEYCGSCGYKPRAAELKQALLEEFPDLEIEGENTPPTTGAFEVEVNGQLVWSKLEGGGFPEPEELKQL
IRD
>gnl|CDD|274014 TIGR02175, Pyruvate_synthase_subunit_PorC, 2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate family. A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins (H. pylori) used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes the gamma subunit. In Pyrococcus furious, enzymes active on pyruvate and 2-ketoisovalerate share a common gamma subunit
MIEIRFHGRGGQGAVTASQLLAEAAFLEGKYAQAFPEFGAERRGAPVRAFLRISDRPIRVHSQIYEPDYV
VVLDPTLLKTVNVTAGLKEDGILIVNTKKDPEELRKELKVYTVDATKIALVVLGRPIVNTPMLGAFAKVT
GLVSLESLEKAIEESFPGKLAEANAKAVERAYEEVKV
>gnl|CDD|131231 TIGR02176, pyruvate_flavodoxin/ferrodoxin_oxidoreductase, pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric. This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase
MKTMDGNTAAAHVAYAFSEVAAIYPITPSSTMGEYVDDWAAQGRKNIFGQTVKVVEMQSEAGAAGAVHGA
LQTGALTTTFTASQGLLLMIPNMYKIAGELLPCVFHVSARAIAAHALSIFGDHQDVMAARQTGFAMLASS
SVQEVMDLALVAHLATIEARVPFMHFFDGFRTSHEIQKIEVLDYEDMASLVNQELVAAFRKRSMNPEHPH
VRGTAQNPDIYFQGREAVNPYYLAVPGIVQKYMDKIAKLTGRSYHLFDYYGAPDAERVIIAMGSVAETIE
ETVDYLNAKGEKVGLLKVRLYRPFSAETFFAALPKSVKRIAVLDRTKEPGAAGEPLYLDVVSAFYEMGEA
MPVILGGRYGLGSKEFTPAMVKAVFDNLSGEAPKNHFTVGIEDDVTGTSLPVDEFFDTTPKGTIQAKFYG
LGSDGTVGANKNAIKIIGDNTDNYAQGYFSYDSKKSGGITISHLRFGEKPIRSTYLVTEADFVACHNPAY
LEMYDVLKGLKKGGTFLLNSPWAPEDLDKHLPNGVKRYIADKEIKFYTIDAVKIAQEVGLGGRINTIMQT
AFFKLAGVLPFEKAVDLLKKSIEKSYGKKGEKIVQKNIKAVDQAVESLHEVKVPAEWKDAPAEPKAIEGD
APEFVKNVVRPINAQEGDDLPVSAFPADGTFPLGTTAFEKRGVAINVPVWVPDNCIQCNQCAFVCPHAAI
RPKLADEEELENAPAGFKSLDAKGKELEGMKFRIQISPLDCTGCGNCVDICPAKEKALVMQPLAEQREAQ
VANWEFAINIPEKDNKLNIDTVKGSQFQRPLFEFSGACSGCGETPYVKLLTQLFGDRMVIANATGCSSIW
GASAPSTPYTTNEQGQGPAWSNSLFEDNAEFGYGMRLSMDKRRERLAELAAKALESDIASGDLKAALNGW
LAGKNDIEKSKERVAKLKKLLAGEKDDLLKEIYAVSDLFVKKSVWIIGGDGWAYDIGYGGLDHVLASGKD
VNVLVMDTEVYSNTGGQSSKATPTGAIAKFAAAGKRTSKKDLGMMAMTYGYVYVAQVSMGANMQQTLKAF
REAEAYDGPSIVIAYSPCINHGIKKGMGKSQAEQKTAVESGYWPLYRYNPRLAEQGKNPFQLDSKEPDSS
VAEFLNGEVRFASLKKSFPDDAERLFNKAAHEAKRRFKEYEHLAA
>gnl|CDD|274015 TIGR02177, 2-oxoacid_ferredoxin_oxidoreductase_beta_subunit, 2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family. A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes a subfamily of beta subunits, representing mostly pyruvate and 2-ketoisovalerate specific enzymes
PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANP
HLKVIVVGGDGDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPV
NPLLLAIALGYTFVARGFSGDVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDEEG
YDPIVREPEEFEEKAAAAIKKAMEWGDRIPIGIFYKNENKPTFEERLEKILPRYMSAPPAEQEIKPPIEK
PKELLEE
>gnl|CDD|131233 TIGR02178, Elongation_factor_P-like_protein, elongation factor P-like protein YeiP. This model represents the family of Escherichia coli protein YeiP, a close homolog of elongation factor P (TIGR00038) and probably itself a translation factor. Member of this family are found only in some Gammaproteobacteria, including E. coli and Vibrio cholerae [Protein synthesis, Translation factors]
KASEMKKGSIVEYNGKTLLIKDIQRSSPQGRGGNVRYKFRMYDVPTGSKVEERFKADDMLDTVELLRREA
SFSYKDGEEYVFMDEEDYTPYTFDKDAIEDELLFISEGLSGMYVQLIDGSPVALELPQHVVLEIVETPPE
IKGASASKRPKPAKLITGLVVQVPEYITTGERILINTTERAFMGRA
>gnl|CDD|131234 TIGR02179, Pyruvate_synthase_subunit_PorD, 2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family. A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes a subfamily of delta subunits, representing mostly pyruvate, 2-ketoisovalerate, and 2-oxoglutarate specific enzymes. The delta subunit is the smallest and resembles ferredoxins
IYEPGSSVANKTGDWRVFKPVVDKEKCIKCKNCWLYCPEGAIQEDEGGFVGIDYDYCKGCGICANVCPVK
AIEMVREE
>gnl|CDD|274016 TIGR02180, Uncharacterized_monothiol_glutaredoxin_F10D7.3, Glutaredoxin. Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses
VVVFSKSYCPYCKKAKEILAKLNVKPYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDL
LALYKNGKLAELL
>gnl|CDD|274017 TIGR02181, GRX_bact, Glutaredoxin, GrxC family. Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides [Energy metabolism, Electron transport]
VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVDGDPALRDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALD
REGKLDPLL
>gnl|CDD|274018 TIGR02182, Glutaredoxin-2_Grx2., Glutaredoxin, GrxB family. Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model includes the highly abundant E. coli GrxB (Grx2) glutaredoxin which is notably longer than either GrxA or GrxC. Unlike the other two E. coli glutaredoxins, GrxB appears to be unable to reduce ribonucleotide reductase, and may have more to do with resistance to redox stress [Energy metabolism, Electron transport]
KLYIYDHCPFCVRARMIFGLKNIPVEKHVLLNDDEETPIRMIGAKQVPILQKDDGRAMPESLDIVAYFDK
LDGEPLLTGKVSPEIEAWLRKVTGYANKLLLPRFAKSDLPEFATQSARKYFTDKKEASAGNFSALLNHTP
GLLEEINADLEELDKLIDGPNAVNGELSEDDILVFPLLRNLTLVAGINWPSRVADYLDNMSKKSKVPLL
>gnl|CDD|131238 TIGR02183, Glutaredoxin_1_Grx1., Glutaredoxin, GrxA family. Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model includes the E. coli glyutaredoxin GrxA which appears to have primary responsibility for the reduction of ribonucleotide reductase
FVVIFGRPGCPYCVRAKQLAEKLAIERADFEFRYIDIHAEGISKADLEKTVGKPVETVPQIFVDEKHVGG
CTDFEQLVKENFDIEA
>gnl|CDD|213689 TIGR02184, Myco_arth_vir_N, Mycoplasma virulence family signal region. This model represents the N-terminal region, including a probable signal sequence or signal anchor which in most instances has four consecutive Lys residues before the hydrophobic stretch, of a family of large, virulence-associated proteins in Mycoplasma arthritidis and smaller proteins in Mycoplasma capricolum
MIKAKKKKIKIATLAIVTALLVSLTIAGPIYYK
>gnl|CDD|274019 TIGR02185, membrane_protein_putative, putative ECF transporter S component, Trep_Strep family. This family consists of strongly hydrophobic proteins about 190 amino acids in length with a strongly basic motif near the C-terminus. If is found in rather few species, but in paralogous families of 12 members in the oral pathogenic spirochaete Treponema denticola and 2 in Streptococcus pneumoniae R6 [Transport and binding proteins, Unknown substrate]
LKIKDFIFIGLLTAIYFAIQFIVGMLTMTTGFFAHLFSPGITAFLVGIIFFLMVAKVPKRGVIFIFGILL
GLLFFLMGMYWPMIISSIIGGLLADIIASTGGYKNKRKVTIAYVLFFLLVAMGPILPIWLFKDEYIAFFA
ARGDSAEYIDQYIKYVSAIWAVIMIVLTAVAGIAGVLIGKKLLKKHFEK
>gnl|CDD|274020 TIGR02186, Hypothetical_transmembrane_protein, conserved hypothetical protein. This family consists of predicted transmembrane proteins of about 270 amino acids. Members are found, so far, only among the Alphaproteobacteria and only once in each genome
IRALLAAVLVLLLGAAATVAQAQNPAAERLEIGVSTEEIAITSNFRGADLTLFGALDNDDPTLLAQGAYD
IVVTLEGPRDDMVVRKKERVFGIWINTDSRTFLQVPESYSLASTRNIDDIASPDTARRMGIGVDNVRLVP
RVFGGYADNVPAFRNAFRRLRTQSGLYREDAGGVTFISPTLFRATLRLPANVPNGTHEVRAYLFRGGVFI
ARTELALEIVKTGLEQAVTTAAHQNPLIYGLLAVALAVVTGWGASILFRKD
>gnl|CDD|274021 TIGR02187, glutaredoxin-like_protein, Glutaredoxin-like domain protein. This family of archaeal proteins contains a C-terminal domain with homology to bacterial and eukaryotic glutaredoxins, including a CPYC motif. There is an N-terminal domain which has even more distant homology to glutaredoxins. The name "glutaredoxin" may be inappropriate in the sense of working in tandem with glutathione and glutathione reductase which may not be present in the archaea. The overall domain structure appears to be related to bacterial alkylhydroperoxide reductases, but the homology may be distant enough that the function of this family is wholly different
LSEEDREILKELFLKELKNPVEIVVFTDNDKEGCQYCKETEQLLEELSEVSPKLKLEIYDFDTPEDKEEA
EKYGVERVPTTIILEEGKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVF
VTPTCPYCPYAVLMAHKFALANDKILGEMIEANENPDLAEKYGVMSVPKIVINKGVEEFVGAYPEEQFLE
YILSA
>gnl|CDD|274022 TIGR02188, Acetyl-coenzyme_A_synthetase, acetate--CoA ligase. This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501
IANLEQYKELYEESIEDPDKFWAKLARELLDWFKPFTKVLDWSFPPFYKWFVGGELNVSYNCVDRHLEAR
PDKVAIIWEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIH
SVVFGGFSAEALADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVSVEHVLVVRRTGNPVVPW
VEGRDVWWHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGD
IFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGD
EWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATL
PFFGIEPAVVDEEGNPVEGPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDG
YIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRKE
LRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEELIEA
>gnl|CDD|274023 TIGR02189, glutaredoxin-like_protein, Glutaredoxin-like family. This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa
VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGK
LVGGLENVMALHISGSLVPMLKQAGALWL
>gnl|CDD|131245 TIGR02190, probable_peroxiredoxin/glutaredoxin_family_protein, Glutaredoxin-family domain. This C-terminal domain with homology to glutaredoxin is fused to an N-terminal peroxiredoxin-like domain
APQARKPESVVVFTKPGCPFCAKAKATLKEKGYDFEEIPLGNDARGRSLRAVTGATTVPQVFIGGKLIGG
SDELEAYLA
>gnl|CDD|274024 TIGR02191, Ribonuclease_3, ribonuclease III, bacterial. This family consists of bacterial examples of ribonuclease III. This enzyme cleaves double-stranded rRNA. It is involved in processing ribosomal RNA precursors. It is found even in minimal genones such as Mycoplasma genitalium and Buchnera aphidicola, and in some cases has been shown to be an essential gene. These bacterial proteins contain a double-stranded RNA binding motif (pfam00035) and a ribonuclease III domain (pfam00636). Eukaryotic homologs tend to be much longer proteins with additional domains, localized to the nucleus, and not included in this family [Transcription, RNA processing]
LEKRLGYKFKNPELLEQALTHRSYANEHHKDVKNNERLEFLGDAVLGLVVAEYLFKNFPDASEGELSRLR
AALVSEESLAEVARELGLGDFLLLGKGEEKSGGRRRDSILADAFEALIGAIYLDSGLEAARKFILKLLIP
RIDAIIKEETLKDYKTALQEWAQARGKPLPEYRLIKEEGPDHDKEFTVEVSVNGEPYGEGKGKSKKEAEQ
NAAKAALEKL
>gnl|CDD|131247 TIGR02192, Protein_HtrL, protein YibB. The protein from this rare, uncharacterized protein family is designated HtrL or YibB in E. coli, where its gene is found in a region of LPS core biosynthesis genes. Homologs are found in Shigella flexneri, Campylobacter jejuni, and Caenorhabditis elegans only. The htrL gene may represent an insertion to the LPS core biosynthesis region, rather than an LPS biosynthetic protein [Hypothetical proteins, Conserved]
VEREVTIVTAFLDIGRGDWDIYRRPLDTYHSYFETLATLENNMIIFTDESSKDFVVKTRTKLGLMDKTIV
IKKTLDDLPLYSAKKIINDELNYRTIADLDMKTNPESISPEYNIVVNLKTHFVHNAIMEGLFNSEHFVWL
DFGYGHAENHFPYSYKWQFALPEGKISLFKIKPYFDEVSSQDLKRLYRKNVALLSGGFIAGDKHAWGQFH
SIIHRKFKQLIYQNIVDDDQFTLLTLARNSFPNLNHIVLGDWFDAFRLFASDTLGPKVQM
>gnl|CDD|274025 TIGR02193, LIPOPOLYSACCHARIDE_HEPTOSYLTRANSFERASE-1, lipopolysaccharide heptosyltransferase I. This family consists of examples of ADP-heptose:LPS heptosyltransferase I, an enzyme of LPS inner core region biosynthesis. LPS, composed of lipid A, a core region, and O antigen, is found in the outer membrane of Gram-negative bacteria [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
RILIVKTSSLGDVIHTLPALTDIKRALPDVEIDWVVEEGFADIVRLHPAVDEVIPVALRRWRKTLFSAAT
WREIKALRALLRAERYDAVIDAQGLIKSALVARMARGPRHGFDWRSAREPLASLFYNKRVGISYQQHAVE
RNRKLFALALGYPPPIAETIDYGLARRAAVAFLGHALPAPYAVLLHATSRDDKTWPEERWRELARLLLAR
GLQIVLPWGNDAEKQRAERIAEALPGAVVLPKMSLAEVAALLAGADAVVGVDTGLTHLAAALDKPTVTLY
GATDPGRTGGYGKPNVALLGESGANPTPDEVLAALEELL
>gnl|CDD|131249 TIGR02194, Glutaredoxin-like_protein_NrdH, Glutaredoxin-like protein NrdH. NrdH-redoxin is a representative of a class of small redox proteins that contain a conserved CXXC motif and are characterized by a glutaredoxin-like amino acid sequence and thioredoxin-like activity profile. Unlike other the glutaredoxins to which it is most closely related, NrdH aparrently does not interact with glutathione/glutathione reductase, but rather with thioredoxin reductase to catalyze the reduction of ribonucleotide reductase
ITVYSKNNCVQCKMTKKALEEHGIAFEEINIDEQPEAIDYVKAQGFRQVPVIVADGDLSWSGFRPDKLKA
LA
>gnl|CDD|274026 TIGR02195, ADP-heptose--LPS_heptosyltransferase_2, lipopolysaccharide heptosyltransferase II. This family consists of examples of ADP-heptose:LPS heptosyltransferase II, an enzyme of LPS inner core region biosynthesis. LPS, composed of lipid A, a core region, and O antigen, is found in the outer membrane of Gram-negative bacteria [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
KILVIGPSWVGDMVMAQSLYRLLKKRYPQAVIDVLAPAWCRPLLERMPEIRQAIDMPLGHGALELTERRR
LGRSLREERYDQAIVLPNSLKSALIPFFAGIPHRTGWRGEMRYGLLNDVRALDKERLPLMVERYIALAYD
KGQDLPQPLPRPQLQVSPAEQAAALAKFGLDTERPIIAFCPGAEFGPAKRWPHEHYAELAKRLIDQGYQV
VLFGSAKDHPAGNEIEALLPGELRNLAGETSLDEAVDLIALAKAVVTNDSGLMHVAAALNRPLVALYGST
SPDFTPPLSEKAEVIRLNLECSPCFKRDCPYGHHQCLIDLSPEQVLEALNELLL
>gnl|CDD|274027 TIGR02196, Gene_56_protein, Glutaredoxin-like protein, YruB-family. This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system
KVKVYTTPWCPPCVKAKEYLTSKGVAFEEIDVEKDAAAREELLKVYGQRGVPVIVIGHKIVVGFDPEKLD
QLLN
>gnl|CDD|274028 TIGR02197, heptose_epim, ADP-L-glycero-D-manno-heptose-6-epimerase. This family consists of examples of ADP-L-glycero-D-mannoheptose-6-epimerase, an enzyme involved in biosynthesis of the inner core of lipopolysaccharide (LPS) for Gram-negative bacteria. This enzyme is homologous to UDP-glucose 4-epimerase (TIGR01179) and belongs to the NAD dependent epimerase/dehydratase family (pfam01370) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
IIVTGGAGFIGSNLVKALNERGITDILVVDNLRDGHKFLNLADLVIADYIDKEDFLDRLEKGAFGKIEAI
FHQGACSDTTETDGEYMMENNYQYSKRLLDWCAEKGIPFIYASSAATYGDGEAGFREGRELERPLNVYGY
SKFLFDQYVRRRVLPEALSAQVVGLRYFNVYGPREYHKGKMASVAFHLFNQIKAGGNVKLFKSSEGFKDG
EQLRDFVYVKDVVDVNLWLLENGVSGIFNLGTGRARSFNDLADAVFKALGKDEKIEYIPMPEALRGRYQY
FTQADITKLRAAGYYGPFTTLEEGVKDYVQWLLA
>gnl|CDD|274029 TIGR02198, Uncharacterized_sugar_kinase_BU060, rfaE bifunctional protein, domain I. RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in E. coli, and separate proteins in some other genome. The longer, N-terminal domain I (this family) is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (TIGR02199) adds ADP to yield ADP-D-glycero-D-manno-heptose [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
LIASFKGAKVLVVGDVMLDRYWYGKVSRISPEAPVPVVKVEREEDRLGGAANVARNIASLGARVFLVGVV
GDDEAGKRLEALLAEEGIDTSGLIRDKDRPTTTKTRVLARNQQLLRVDFEERDPINAELEARLLAAIREQ
LASADAVVLSDYAKGVLTPRVVQEVIAAARKHGKPVLVDPKGKDFSRYRGATLITPNRKEAEAAVGACDT
EAELVQAAEKLLEELDLEALLVTRSEKGMTLFTREGEPIHIPAQAREVYDVTGAGDTVIATLALALAAGA
SLEEACRLANAAAGVVVGKLGTATVSPAELANALQ
>gnl|CDD|131254 TIGR02199, rfaE_dom_II, rfaE bifunctional protein, domain II. RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in E. coli, and separate proteins in some other genome. Domain I (TIGR02198) is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
ALVARARARGKKIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKRLKGETRPINPEEDRAEV
LAALSSVDYVVIFDEDTPEELIGELKPDILVKGGDYKVETLVGAELVESYGGQVVLLPFVEGRSTTAIIE
KILK
>gnl|CDD|131255 TIGR02200, conserved_hypothetical_protein, Glutaredoxin-like protein. This family of glutaredoxin-like proteins is limited to the Actinobacteria and contains the conserved CxxC motif
TITVYGTTWCGYCAQLMRTLDKLGAAYEWVDIEEDEGAADRVVSVNNGNMTVPTVKFADGSFLTNPSAAQ
VKAKLQE
>gnl|CDD|131256 TIGR02201, lipopolysaccharide_glucosyltransferase_I, lipopolysaccharide heptosyltransferase III, putative. This family consists of examples of the putative ADP-heptose:LPS heptosyltransferase III, an enzyme of LPS inner core region biosynthesis. LPS, composed of lipid A, a core region, and O antigen, is found in the outer membrane of Gram-negative bacteria. This enzyme may be less widely distributed than heptosyltransferases I and II [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
RILLIKLRHHGDMLLTTPVISSLKKNYPDAKIDVLLYQETIPILSENPDINALYGLDRKKAKAGERKLAN
QFHLIKVLRANRYDLVVNLTDQWMVAILVKLLNARVKIGFDYPKRRSAFWRKSFTALAPLQGGNTLHTVE
QNLSVLTPLGLDSLVKQTRMSYPPADWKAMRALLDEAGVGQNYIVIQPTSRWFFKCWDNDRFSALIDALH
ARGYEVVLTSGPDKDELAMVNEIAQGCQTPRVTSLAGKLTLPQLAALIDHARLFIGVDSVPMHMAAALGT
PLVALFGPSKHIFWRPWSNNMIQFWAGDYGELPDPDQRDTNTRERYLSVIPAAAVIAAVDKLLP
>gnl|CDD|131257 TIGR02202, Ehrlichia_rpt, Ehrlichia chaffeensis immunodominant surface protein repeat. This model represents 77 residues of an 80 amino acid (240 nucleotide) tandem repeat, found in a variable number of copies in an immunodominant outer membrane protein of Ehrlichia chaffeensis, a tick-borne obligate intracellular pathogen
KEDDIVSQPSLEPFVAESEVSKVEQEETNPEVLIKDLQDVASHESGVSDQPAQVVTERENEIESHQGETE
KESGITE
>gnl|CDD|131258 TIGR02203, Lipid_A_export_ATP-binding/permease_protein_msbA., lipid A export permease/ATP-binding protein MsbA. This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGIC
SFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETL
TVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFG
GQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAM
IALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGTRAIERARGDVEFRNVTFRYPGRDRPALDS
ISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND
TIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPI
LILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGL
YAQLHNMQFRE
>gnl|CDD|131259 TIGR02204, system_ATPase_and_permease_component, ABC transporter, permease/ATP-binding protein. This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins
KRLRPLAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALV
LALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMAL
RNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTV
QAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQF
VFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPAR
PDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVP
QDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARA
ILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAE
LIAKGGLYARLARLQF
>gnl|CDD|274030 TIGR02205, Cell_division_protein_ZipA_homolog, cell division protein ZipA. This model represents the full length of bacterial cell division protein ZipA. The N-terminal hydrophobic stretch is an uncleaved signal-anchor sequence. This is followed by an unconserved, variable length, low complexity region, and then a conserved C-terminal region of about 140 amino acids (see pfam04354) that interacts with the tubulin-like cell division protein FtsZ [Cellular processes, Cell division]
DLRIILIIVGILAIAALLFHGLWTSRKEKSKYFDKAPLDRMKLKSDDPTSEEMVQPDNSPNTRVERGEHP
IPQPREQHLPSISELVAYQRDKSVDDEEASIPMQPTQQQYDMPQPNNVAQQTVEPRVAKSLPEASPQEEE
VGKNLEVTAPPKQKDKVIILNVAAKAESEFNGEKLVQAIEQTGLIFGDMNIFHRHLDLSGEGPVLFSMAN
MVKPGTFDMDNIAEFSTPGISFFMTLPSPGDPLQNFKLMLPTAQRLAEDLGGVVLDEQRNALTAQRIAHY
RDRI
>gnl|CDD|131261 TIGR02206, Uncharacterized_protein_TP_0381, conserved hypothetical integral membrane protein TIGR02206. This model represents a family of hydrophobic proteins with seven predicted transmembrane alpha helices. Members are found in Bacillus subtilis (ywaF), TP0381 from Treponema pallidum (TP0381), Streptococcus pyogenes, Rhodococcus erythropolis, etc
GPFILFSHSHFIILLIAVVLAVLLVFLGFRLTRLKAFRLFRAIILLGAVIGLMLWYVLLGGFTLDESLPL
HLCDIAIILAAIMLITKRRWFFQLTYFWGIGGSFQALLTPDLYPYGFPHVAFISFFIGHYFLLLAALYLI
LIFRERPTLRGLKVAVLFALILAIIALFVNRLLGANYGFLNKKPVTASILDLLGPWPVYITSLVTILVAI
WFLMYLPFRRSQ
>gnl|CDD|274031 TIGR02207, DDG_protein., lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase. This model represents a narrow clade of acyltransferases, nearly all of which transfer a lauroyl group to KDO2-lipid IV-A, a lipid A precursor; these proteins are termed lipid A biosynthesis lauroyl acyltransferase, HtrB. An exception is a closely related paralog of E. coli HtrB, LpxP, which acts in cold shock conditions by transferring a palmitoleoyl rather than lauroyl group to the lipid A precursor. Members of this family are homologous to the family of acyltransferases responsible for the next step in lipid A biosynthesis [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
PEFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAE
RERLLRENFESTGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFG
QQQPGIGVYRPHNNPLFDWIQTRGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFF
AVPDAATTTGTSILARLSKCAVVPFTPRRNEDGSGYRLKIDPPLDDFPGDDEIAAAARMNKIVEKMIMRA
PEQYMWLHRRFKTRPDEGESSLY
>gnl|CDD|274032 TIGR02208, lipid_A_msbB, lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase. This family consists of MsbB in E. coli and closely related proteins in other species. MsbB is homologous to HtrB (TIGR02207) and acts immediately after it in the biosynthesis of KDO-2 lipid A (also called Re LPS and Re endotoxin). These two enzymes act after creation of KDO-2 lipid IV-A by addition of the KDO sugars [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
YDRRFQKSFLHPKYWGTWLGVFALVLLAFMPAKLRDPIAKVLAKFVGPIAKKPRGRARINLSACFPEKSE
AERETIIDNNFATFVQVMLSQAELAIRSKAHLRRRVNLMGLEHIEAAQAAGKPVIFLVPHGWAIDYAGLR
LASQGLPMVTMFNNHKNPLFDWLWNRVRSRFGGHVYAREAGIKALLASLKRGESGYYLPDEDHGPEQSVF
VPFFATYKATLPVVGRLAKAGNAQVVPVFPGYNQVTGKFELTVRPAMATELSVDPEQEARAMNKEVEQFI
LPYPEQYMWILRLLKTRPDGEASIY
>gnl|CDD|131264 TIGR02209, Cell_division_protein_FtsL, cell division protein FtsL. This model represents FtsL, both forms similar to that in E. coli and similar to that in B. subtilis. FtsL is one of the later proteins active in cell division septum formation. FtsL is small, low in complexity, and highly divergent. The scope of this model is broader than that of the pfam04999.3 for FtsL, as this one includes FtsL from Bacillus subtilis and related species [Cellular processes, Cell division]
EKKLYVLLLLAILVSAISVVSAQHQTRQLNNELQKLQLEIDKLQKEWRDLQLEVAELSRHERIEKIAKKQ
LGMKLPDANIKVVVK
>gnl|CDD|274033 TIGR02210, Rod_shape-determining_protein_RodA, rod shape-determining protein RodA. This protein is a member of the FtsW/RodA/SpoVE family (pfam01098). It is found only in species with rod (or spiral) shapes. In many species, mutation of rodA has been shown to correlate with loss of the normal rod shape. Note that RodA homologs are found, scoring below the cutoffs for this model, in a number of both rod-shaped and coccoid bacteria, including four proteins in Bacillus anthracis, for example [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Cell division]
DWGLLLLVLLLVGIGLLVLYSASGGSLAPFALKQLVWFGIGLVLMIIVALIDYRFLRRLAYPLYVLGLLL
LVAVLLFGTTGKGAQRWIDLGFFRLQPSEFAKLALILMLAKYLSRRPLDKPPRLKDLLKALILILVPALL
ILKQPDLGTALVVLAIGLFVLFLAGLSWKLILGLLAAGAAAIPVIIWWFLLHDYQKQRILTFLDPESDPL
GAGYHIIQSKIAIGSGGLFGKGWLQGTQSQLEFLPEQHTDFIFSVLAEEFGFVGGLVLLLLYLLLILRGL
RIALNAKDRFGRLLAGGIALTFFFYVFVNIGMVIGLLPVVGIPLPLVSYGGSSLLTLMIGFGLLMSIHTH
RR
>gnl|CDD|131266 TIGR02211, LolD_lipo_ex, lipoprotein releasing system, ATP-binding protein. This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina [Protein fate, Protein and peptide secretion and trafficking]
LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLS
KLSSNERAKLRNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPS
ELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDR
VLEMKDGQLFN
>gnl|CDD|274034 TIGR02212, releasing_system_transmembrane_protein_lolC., lipoprotein releasing system, transmembrane protein, LolC/E family. This model describes the LolC protein, and its paralog LolE found in some species. These proteins are homologous to permease proteins of ABC transporters. In some species, two paralogs occur, designated LolC and LolE. In others, a single form is found and tends to be designated LolC [Protein fate, Protein and peptide secretion and trafficking]
PLSLFIALRYLRAKRRNRFVSFISLFSIIGIALGVAALIVVLSVMNGFERELLQRILGVIPHAIIESKQN
PIIDWQELLERILKNPGVKAAAPIVSGQALVQSAGKVSGVQVRGVDPSDEDKLSAISNNVKQGALKGFKP
GEYNIIIGEQLAEKLGVSVGDKITLISPESNVTPFGEIPRQKRFTVIGIFSTGGEVDGYLALMPLEDAQR
FLRYGDQVTGLRLKLDDPFQADALAQQVEPELGPELYVRDWTDQNGELFSAIQMEKNMMFLILSLIIAVA
AFNIVSTLVMAVKDKQGDIAILRTLGATPGQIMRIFIVQGLLIGVIGTLLGVILGVLLALNLTTIINFIE
WLIGVKFFNADIYFLDFLPSKLDPLDVLLIIVTALLLSLLATLYPAWRAAKLQPAEALRYE
>gnl|CDD|131268 TIGR02213, lolE_release, lipoprotein releasing system, transmembrane protein LolE. This protein is part of an unusual ABC transporter complex that releases lipoproteins from the periplasmic side of the bacterial inner membrane, rather than transport any substrate across the inner membrane. In some species, the permease-like transmembrane protein is represented by two paralogs, LolC and LolE, both in the LolCDE complex. This family consists of LolE, as found in E. coli and related species [Protein fate, Protein and peptide secretion and trafficking]
NLPLLIGWRFSRGKQRNPMVSLISKFSTIGIALGVAVLIVGLSAMNGFERELNQRILAVVPHAEIESVPP
PIHNWQNLEKRLQQNPQIKAAAPYVSFTGLVENGSKLKAVQVKGVEPQAEQKVSSIGNFVQEQAWNKFEK
GEGQLILGSGVAKELDVKVGDWVTLLIPQQNGDEKFAQPKRVRVQVTGILRLDGQLDHSYALLPLADAQQ
YLTYGDQVTGIALKLDDVFNARNLVRSMGNDYPQYVYMQSWISKFGYMYRDIQLIRTIMYLAMVLVIGVA
CFNIVSTLIMAVKDKQGDIAILRTLGANDGLIKRIFVWYGLQAGMKGSLIGIVLGVIVALNLTTFIQGIE
WVIGHQFLSGDIYFVDFLPSELHWLDVLMVLVTALALSLMASWYPASRAAKLQPAQVLSSH
>gnl|CDD|131269 TIGR02214, sporulation_specific_penicillin-binding_protein, stage V sporulation protein D. This model describes the spoVD subfamily of homologs of the cell division protein FtsI, a penicillin binding protein. This subfamily is restricted to Bacillus subtilis and related Gram-positive species with known or suspected endospore formation capability. In these species, the functional equivalent of FtsI is desginated PBP-2B, a paralog of spoVD [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]
RSIHILISFTALFLILILRLFYVQVFRGSFYKEMAEDQWTREIPIEAKRGRILDRNGNELAVSVSVDRVD
LDPATIRKNKEPKQREIANELARVLEMDKEKVFKRITKKNSPFVSAKLGRKIEKDKAEKVRNLKLNGVSV
SPDSKRYYPNGDFLSHVLGFTNSDGRGLEGLELYYDKELRGLPGVRVAEYDANSLELPYAQHAYVKPVDG
HDLVLTIDENIQYIIEREADKALRERKPKGVSIIVMNPKNGEILGMSNRPTYDPNDPRDKSPDTARRNRA
VSDAYEPGSTFKIITSSAAMEEGIVKESDKFYDDGSATVGGKKIKCWKPGGHGSQTFPEVVQNSCNPGFI
ELGMRLGAEKLNNYILAFGFGSKTGIDLPGEAAGILVPKKKVGPVDLATISFGQANTVTPIQLMTAVNAV
ANGGKLIQPHIMKEISDSQNNAVDQTFEPEVKRQVVSKETTQKLRLALETVVSKGSGKNAFIEGYRVGGK
TGTAQKVKPNGGYMEGEYIVSFVGFAPADDPAVAVLVVVDNPKGVQQFGGLVAAPVFGSVFNDILNYLGI
KPQMNQGEAPAAATNQVEAVAVPNLRGMKVDDAEKTLLHLGLDVATEGFGTRVVNQTPIPGEKVKEGTKV
VLYLGE
>gnl|CDD|274035 TIGR02215, conserved_hypothetical_protein, phage conserved hypothetical protein, phiE125 gp8 family. This model describes a family of proteins found exclusively in phage or in prophage regions of bacterial genomes, including the phage-like Rhodobacter capsulatus gene transfer agent, which packages DNA. Members of this family show some similarity to members of pfam05135, a putative DNA packaging protein family [Mobile and extrachromosomal element functions, Prophage functions]
MTMILETPPAAEPLTVADFKAHLRLGTEVEDAVLASLLRAARAAIEARTGKILISQTWRLTVDRWPRAGR
LVLPKGPVQAVTSVTLYDGGGQATVLDPAAFRLDRDSRPPRLRPAGAPLPGRATGGIEVDLVAGYGEAGG
DVPATLKQAVLTLAAHYYEYRGHVAALGDACMPFGVTSLIARYRRVRL
>gnl|CDD|274036 TIGR02216, GTA_orfg10.1_translated, phage conserved hypothetical protein. This model describes a family of proteins found exclusively in phage or in prophage regions of bacterial genomes, including the phage-like Rhodobacter capsulatus gene transfer agent, which packages DNA [Mobile and extrachromosomal element functions, Prophage functions]
PFPWPALMHAGLCGLRLSPEAFWRLTPAELFAMLGQGGGNAPMGRAALDALMRRFPDQ
>gnl|CDD|274037 TIGR02217, conserved_hypothetical_protein, TIGR02217 family protein. This model represents a family of conserved hypothetical proteins. It is usually (but not always) found in apparent phage-derived regions of bacterial chromosomes [Mobile and extrachromosomal element functions, Prophage functions]
AFHEIRFPLNVSLGSTGGPERRTDIVTLLSGLEQRNARWANARRRYDAGYGLRSNEDLEQVLAFFEARRG
SLFGFRFRDPADFSSAAPGAPINALDQVIGIGDGVLTKFQLRKTYGNGIAPYERVITKPVNGSVMIYVNG
VKAAEGEFSVDYATGIVTFPPGHPPPQDAIITAGFEFDVPVRFDTDYLEASICAFSAGDIPSIPLVEVKT
>gnl|CDD|274038 TIGR02218, conserved_hypothetical_protein, phage conserved hypothetical protein BR0599. This model describes a family of proteins found almost exclusively in phage or in prophage regions of bacterial genomes, including the phage-like Rhodobacter capsulatus gene transfer agent, which packages DNA. An apparent exception is Wolbachia pipientis wMel, a bacterial endosymbiont of the fruit fly, which has several candidate phage-related genes physically separate from obvious prophage regions [Mobile and extrachromosomal element functions, Prophage functions]
WYLTRADGVRMGFTDHDEDLTVDGVIFRAVSGFTASAAISASGLGQSNSEVEGALSSADIAEEDIEAGRY
DGADVEAFLVNWGDPEQRMLLWRGQIGKVTRSGGAFCAELRGLAAALERVPGRTYCRTCDAVLGDGRCKV
DLVRFRATGTVPQVIDGRVIRVTGLDGFADGWFSRGRLEWTGAGCDKRFATCRAKFNNLVNFRGFPHLPG
EDFVYAYPVETSPNDGGVL
>gnl|CDD|131274 TIGR02219, hypothetical_protein_CC_2775, putative phage cell wall peptidase, NlpC/P60 family. Members of this family show sequence similarity to members of the NlpC/P60 family described by pfam00877 and by Anantharaman and Aravind (). The NlpC/P60 family includes a number of characterized bacterial cell wall hydrolases. Members of this related family are all found in prophage regions of bacterial genomes [Mobile and extrachromosomal element functions, Prophage functions]
VLAEARSWIGTPYRHQASTLGVGCDCLGLVRGVWRALYGEEPEAPPPYAPDWAEAGGGETLAEAALRHLV
PVPCDAAQPGDVLVFRWRPGAAAKHAAIAASPTRFIHAYDGAAVVESALVPWWRRRLAGAFRFP
>gnl|CDD|274039 TIGR02220, hypothetical_protein_phage, phage conserved hypothetical protein, C-terminal domain. This model represents the conserved C-terminal domain of a family of proteins found exclusively in bacteriophage and in bacterial prophage regions. The functions of this domain and the proteins containing it are unknown [Mobile and extrachromosomal element functions, Prophage functions]
YKEIIEYLNEKAGKSFKHTTAKHKKLIKARWNEGYTLEDFKKVIDNKVSEWLGTEFEKYLRPKTLFGNKK
FDGYLNQ
>gnl|CDD|274040 TIGR02221, CRISPR-associated_protein_Csx1_2, CRISPR-associated protein, TM1812 family. CRISPR is a term for Clustered Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR associated) proteins. This family, represented by TM1812 of Thermotoga maritima, is found also in Vibrio vulnificus YJ016, Nitrosomonas europaea ATCC 19718, a large plasmid of Synechocystis sp. PCC 6803, and Fibrobacter succinogenes S85
TFISFLGVGDTNTDVQYKTAVYKFEGDSDTIETRFVQKALVEKLRPDKVIVVGTAGSMWDKLYEVGFDED
YWVLLGKKVGMSKVDNALLSELQLKLIEKLGDKVLKRLIPDAVSGSKEQWDLFMSLTNEVDHGDEIYLDI
THGFRFLPVVALAAIEYLRYVKNVKVEGVLYGALDMNSELGHSPIVDLKPMLEISDWVEGLGRFVTYGDS
YVLAKLLE
>gnl|CDD|131277 TIGR02222, Protein_CsaA, export-related chaperone protein CsaA. This model describes Bacillus subtilis CsaA, an export-related chaperone that interacts with the Sec system, and related proteins from a number of other bacteria and archaea. The crystal structure is known for the homodimer from Thermus thermophilus [Protein fate, Protein folding and stabilization, Protein fate, Protein and peptide secretion and trafficking]
YEDFEKLDLRVGRIVRAEPFPEARKPAYKLWVDFGTEIGVKQSSAQITKLYKPEDLIGRLVVAVVNFPPK
QIAGFLSEVLVLGVIDEQGRVVLLQPDRPVPNGTKIA
>gnl|CDD|274041 TIGR02223, Cell_division_protein_FtsN, cell division protein FtsN. FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis [Cellular processes, Cell division]
MAQRDYVRRGRGAPQKKKKNRRLVRATVLIAAILILLFIGGSSGLYLLTESKQANEPETLQPKNQTENGE
TAADLPPKPEERWSYIEELEAREVLINDPEEPSNGGGVEESAQLTAEQRQLLEQMQADMRAAEKVLATAP
SEQTVAVEARKQTAEKKPQKARTAEAQKTPVETEKIASKVKEAKQKQKALPKQTAETQSNSKPIETAPKA
DKADKTKPKPKEKAERAAALQCGAYANKEQAESVRAKLAFLGISSKITTTDGGKWYRVVSGPYKNKDDAE
KDLNKLKVAGVAGCIINE
>gnl|CDD|274042 TIGR02224, Tyrosine_recombinase_XerC, tyrosine recombinase XerC. The phage integrase family describes a number of recombinases with tyrosine active sites that transiently bind covalently to DNA. Many are associated with mobile DNA elements, including phage, transposons, and phase variation loci. This model represents XerC, one of two closely related chromosomal proteins along with XerD (TIGR02225). XerC and XerD are site-specific recombinases which help resolve chromosome dimers to monomers for cell division after DNA replication. In species with a large chromosome and homologs of XerC on other replicons, the chomosomal copy was preferred for building this model. This model does not detect all XerC, as some apparent XerC examples score in the gray zone between trusted (450) and noise (410) cutoffs, along with some XerD examples. XerC and XerD interact with cell division protein FtsK [DNA metabolism, DNA replication, recombination, and repair]
EAFLEYLRLERNYSPHTVRAYRRDLEAFLEFLEEEGGLASLAEVTAADLRSFLAELHARGLSRRSLARKL
SALRSFYRFLLRRGLIDANPAAGVRAPKQPKKLPKFLSEDEMEALLDAPEEDDEDWLALRDRAILELLYS
SGLRVSELVGLDLSDLDLDFGEVRVRGKGNKERIVPFGPYARDALQAYLEARRSPLLASEGQDALFLNRR
GGRLTPRGVQYRLQQLRAKAGLPKHVHPHALRHSFATHLLNNGADLRAVQELLGHASLSTTQIYTHVDFQ
HLAKVYDQAHPRAKK
>gnl|CDD|274043 TIGR02225, Tyrosine_recombinase_XerD, tyrosine recombinase XerD. The phage integrase family describes a number of recombinases with tyrosine active sites that transiently bind covalently to DNA. Many are associated with mobile DNA elements, including phage, transposons, and phase variation loci. This model represents XerD, one of two closely related chromosomal proteins along with XerC (TIGR02224). XerC and XerD are site-specific recombinases which help resolve chromosome dimers to monomers for cell division after DNA replication. In species with a large chromosome and with homologs of XerD on other replicons, the chomosomal copy was preferred for building this model. This model does not detect all XerD, as some apparent XerD examples score below the trusted and noise cutoff scores. XerC and XerD interact with cell division protein FtsK [DNA metabolism, DNA replication, recombination, and repair]
EQFLDYLWVERGLSQNTLEAYRRDLEKFLEFLEERGIDLEEVDRGDIVDFLAELKEAGLSARSIARALSA
LRSFYRFLLREGIREDDPSALIEPPKVARKLPKVLTVEEVEALLAAPDVDTPLGLRDRAMLELLYATGLR
VSELVGLRLEDVNLDEGFVRVRGKGNKERLVPLGEEAIEALERYLKEARPLLLKKKVKESDALFLNRRGG
PLSRQGVWKILKEYAKRAGIEKPISPHTLRHSFATHLLENGADLRVVQELLGHADISTTQIYTHVARERL
KEVHKKHHPRA
>gnl|CDD|131281 TIGR02226, hypothetical_protein-transmembrane_prediction, N-terminal double-transmembrane domain. This model represents a prokaryotic N-terminal region of about 80 amino acids. The predicted membrane topology by TMHMM puts the N-terminus outside and spans the membrane twice, with a cytosolic region of about 25 amino acids between the two transmembrane regions. Member proteins tend to be between 600 and 1000 amino acids in length [Hypothetical proteins, Domain]
MSFLNPALLAGLLAAVLPLLIHLLRRRPPRPVDFPALRFLREVPKRERSRSRLDQWWLLALRLLALAALA
IALARPLLNPSL
>gnl|CDD|274044 TIGR02227, Inactive_signal_peptidase_IA., signal peptidase I, bacterial type. This model represents signal peptidase I from most bacteria. Eukaryotic sequences are likely organellar. Several bacteria have multiple paralogs, but these represent isozymes of signal peptidase I. Virtually all known bacteria may be presumed to A related model finds a simlar protein in many archaea and a few bacteria, as well as a microsomal (endoplasmic reticulum) protein in eukaryotes [Protein fate, Protein and peptide secretion and trafficking]
FVFFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVEFRDG
KLYINGKKIDEPYLKPNGYLDTSEFNTPVKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYP
FD
>gnl|CDD|131283 TIGR02228, Signal_peptidase_I_W, signal peptidase I, archaeal type. This model represents signal peptidase I from most archaea, a subunit of the eukaryotic endoplasmic reticulum signal peptidase I complex, and an apparent signal peptidase I from a small number of bacteria. It is related to but does not overlap in hits with TIGR02227, the bacterial and mitochondrial signal peptidase I
KKISNVIYFILIILLVILLLYGLVSKASGPDPVVVVLSGSMEPTFNTGDLILVTGADPNDIQVGDVITYK
SPGFNTPVTHRVIEINNSGGELGFITKGDNNPAPDGEPVPSENVIGKYLGFTIPFAGYVLVFAPQAIGAA
ALLIIPGIGLISYLFITI
>gnl|CDD|131284 TIGR02229, hypothetical_protein, caa(3)-type oxidase, subunit IV. This model represents a small set of proteins with weak similarity to the sequences in pfam03626, which describes the cytochrome C oxidase subunit IV [Energy metabolism, Electron transport]
HPHISDTPTYLGVWLALVVLTAITIAASFFHLNLGTLAMVIALAIAVLKALLVALYFMHLKRAHALLRLA
SAVAFAILAILFVITHGDYASR
>gnl|CDD|131285 TIGR02230, H+-transporting_ATP_synthase_gene_1, F0F1-ATPase subunit, putative. This model represents a protein found encoded in F1F0-ATPase operons in several genomes, including Methanosarcina barkeri (archaeal) and Chlorobium tepidum (bacterial). It is a small protein (about 100 amino acids) with long hydrophic stretches and is presumed to be a subunit of the enzyme [Energy metabolism, ATP-proton motive force interconversion]
MNEREPEKLSAKDKPLEKRVGDKELRKLRARKNATRSIWEGLGMFGLIGWSVAIPTLLGVAVGIWLDRHY
PSPFSWTLTMLIVGVVIGCLNAWHWVSREN
>gnl|CDD|274045 TIGR02231, Hypothetical_protein_ZK1055.6b, conserved hypothetical protein. This family consists of proteins over 500 amino acids long in Caenorhabditis elegans and several bacteria (Pseudomonas aeruginosa, Nostoc sp. PCC 7120, Leptospira interrogans, etc.). The function is unknown
KISTVTVYPDRAEVTRSGKVDLPSGVNELVLKNLPLTLQDDSLRVSGEGLAVASLVTVSTWRERTSRPDP
ERLAELRKQIRELEAELRDLEDRGDALKALAKFLEDIREGLTEPIKDSAKRNEPDLKEWFQAFDFNGSEI
ERLLTEDREAERRIRELEKQLSELQNELNALLTGKSQRSHTVLVRLEAPEDAEAELNLTYQVGNASWTPS
YDARLDTGAPTVELTYLAEIRQSTGEDWSDIPLVLSTAQPSLGGRIPELGPLYADAPRPPVPMARGAASP
DLPRPDGTVVPQSRNLEPESLAEAPEVLSPAAEMTAEVEKGGLSVTFKIPGRVTIPSDGDAHKITIASFE
LPAALNYRAVPSLNSTAFLEASFKNTSDFPLLPGEVNIFRGNGFVGRSHLENVAPGERFELSLGVDEGIR
IERKVVKRQTDEGGLIGNTSRTEYAYRITLKNLRKEPERVQIEEQLPVSENEDIKVKLLSPTTPGYDEED
KKDGILEWKLTLKPGEKRDLKFKFKVEHPKDLTVV
>gnl|CDD|200169 TIGR02232, myxo_disulf_rpt, Myxococcus cysteine-rich repeat. This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus
APTCGDGIIEPGEECDDGNTTSGDGCSATCRLEEGFAC
>gnl|CDD|274046 TIGR02234, conserved_hypothetical_protein, trp region conserved hypothetical membrane protein. Members of this family are predicted transmembrane proteins with four membrane-spanning helices. Members are found in the Actinobacteria (Mycobacterium, Corynebacterium, Streptomyces), always associated with genes for tryptophan biosynthesis
RRSLAVALLLGALGAAVAWLSSRQGWAAGETFDVAGGDFPLTLKGADWSGVPAALALVGLAALVAVFAVR
SAGRRLVAGLLAVSAVGAGTIAASLLGVSDSTALDAKAAQASLDSSVTSQRLTHGAWPYVAVAAGALLLL
AGLLLLRYGRVWPAMRGGYERDGTPRPRRARARPDRPETDLEQAPGRVLWDALDEDEDPTDP
>gnl|CDD|131289 TIGR02235, menA_cyano-plnt, 1,4-dihydroxy-2-naphthoate phytyltransferase. This family of phytyltransferases, found in plants and cyanobacteria, are involved in the biosythesis of phylloquinone (Vitamin K1). Phylloquinone is a critical component of photosystem I. The closely related MenA enzyme from bacteria transfers a prenyl group (which only differs in the saturation of the isoprenyl groups) in the biosynthesis of menaquinone. Activity towards both substrates in certain organisms should be considered a possibility [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
LWLAAIKPPLYSVAVMPILVGTAVAWGQGGVFHLDRFALFLIAAILILAWINLTNDVFDSDTGIDRFKLH
SIVNLTGSRSLVFWLANFFLLIGLVGIAALSWRWQITVLALVGLCCFLGYLYQGPPFRLGYQGLGEPICW
LCFGPLAIAAALYAQSQSFSLIPWKASILVGLATTLILFCSHFHQVEDDLAHGKRSPVVRLGTKLAAKIV
PWVISLSYVVLLIAVIGGFLPWTTLLALASIPWAVKLIRLVRQNHNNPEQISNCKFIAVRFHFLSGILLT
LGLLL
>gnl|CDD|131290 TIGR02236, DNA_repair_and_recombination_protein_RadA, DNA repair and recombination protein RadA. This family consists exclusively of archaeal RadA protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239), and archaeal RadB (TIGR02237). This protein is involved in DNA repair and recombination. The member from Pyrococcus horikoshii contains an intein [DNA metabolism, DNA replication, recombination, and repair]
LEDLPGVGPATAEKLREAGYDTFEAIAVASPKELSEIAGISEGTAAKIIQAARKAADLGGFETADDVLER
RKTIGKITTGSKELDELLGGGIETQAITEVFGEFGSGKTQICHQLAVNVQLPEEKGGLGGKAVYIDTENT
FRPERIMQMAEARGLDPDEVLKNIYVARAYNSNHQMLLVEKAEDLIKELNNPVKLLIVDSLTSHFRAEYV
GRGALAERQQKLNKHLHDLLRLADLYNAAVVVTNQVMARPDAFFGDPTRPIGGHILGHAATFRVYLRKGK
GDKRIARLVDSPHLPEGEAVFRITEKGIED
>gnl|CDD|274047 TIGR02237, DNA_repair_and_recombination_protein_RadB, DNA repair and recombination protein RadB. This family consists exclusively of archaeal RadB protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239) and DMC1 (TIGR02238), and archaeal RadA (TIGR02236)
IDELLGGGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTEGLSPERFKQIAEDRPERALSN
FIVFEVFDFDEQGVAIQKTSKFIDRDSASLVVVDSFTALYRLELSDDRISRNRELARQLTLLLSLARKKN
LAVVITNQVYTDVNNGTLRPLGGHLLEHWSKVILRLEKFRGRRLATLEKHRSRPEGESVYFRITDDGIE
>gnl|CDD|131292 TIGR02238, Meiotic_recombination_protein_dmc1, meiotic recombinase Dmc1. This model describes DMC1, a subfamily of a larger family of DNA repair and recombination proteins. It is eukaryotic only and most closely related to eukaryotic RAD51. It also resembles archaeal RadA (TIGR02236) and RadB (TIGR02237) and bacterial RecA (TIGR02012). It has been characterized for human as a recombinase active only in meiosis
IDKLQAHGINAADIKKLKSAGICTVNGVIMTTRRALCKIKGLSEAKVDKIKEAASKIINPGFITAFEISQ
KRKKVLKITTGSQALDGILGGGIESMSITEVFGEFRCGKTQLSHTLCVTAQLPREMGGGNGKVAYIDTEG
TFRPDRIRAIAERFGVDPDAVLDNILYARAYTSEHQMELLDYLAAKFSEEPFRLLIVDSIMALFRVDFSG
RGELSERQQKLAQMLSRLNKISEEFNVAVFVTNQVQADPGATMTFIADPKKPIGGHVLAHASTTRILLRK
GRGEERVAKLYDSPDMPEAEASFQITEGGIADA
>gnl|CDD|274048 TIGR02239, DNA_repair_protein_RAD51, DNA repair protein RAD51. This eukaryotic sequence family consists of RAD51, a protein involved in DNA homologous recombination and repair. It is similar in sequence the exclusively meiotic recombinase DMC1 (TIGR02238), to archaeal families RadA (TIGR02236) and RadB (TIGR02237), and to bacterial RecA (TIGR02012)
IEKLEGNGITAADIKKLQEAGLHTVESVAYAPKKQLLEIKGISEAKADKILAEAAKLVPMGFTTATEFHQ
RRQEVIQLTTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLAVTCQLPIDQGGGEGKALYIDTEG
TFRPERLLAIAERYGLNPEDVLDNVAYARAYNTDHQLQLLQQAAAMMSESRFALLIVDSATALYRTDFSG
RGELSARQMHLARFLRSLQRLADEFGVAVVITNQVVAQVDGAGSMFAGDPKKPIGGNIMAHASTTRLSLR
KGRGEQRICKIYDSPCLPESEAMFAIYEDGIGDPKE
>gnl|CDD|131294 TIGR02240, Poly3-hydroxyalkanoate_depolymerase, poly(3-hydroxyalkanoate) depolymerase. This family consists of the polyhydroxyalkanoic acid (PHA) depolymerase of Pseudomonas oleovorans, Pseudomonas putida BM01, and related species. This enzyme is part of polyester storage and mobilization system as in many bacteria. However, species containing this enzyme are unusual in their capacity to produce aromatic polyesters when grown on carbon sources such as benzoic acid or phenylacetic acid [Energy metabolism, Other]
PFIFRTIDLDGQSIRTAVRPGKEGLTPLLIFNGIGANLELVFPFIEALDPDLEVIAFDVPGVGGSSTPRH
PYRFPGLAKLAARMLDYLDYGQVNAIGVSWGGALAQQFAHDYPERCKKLILAATAAGAVMVPGKPKVLMM
MASPRRYIQPSHGIHIAPDIYGGAFRRDPELAMAHASKVRSGGKLGYYWQLFAGLGWTSIHWLHKIQQPT
LVLAGDDDPIIPLINMRLLAWRIPNAELHIIDDGHLFLITRAEAVAPIIMKFLAEERQRAVMHPRP
>gnl|CDD|274049 TIGR02241, hypothetical_protein_SCD8A.25c, conserved hypothetical phage tail region protein. This family consists of uncharacterized proteins. All members so far represent bacterial genes found in apparent phage or otherwisely laterally transferred regions of the chromosome. Tentatively identified neighboring proteins tend to be phage tail region proteins. In some species, including Photorhabdus luminescens TTO1, several members of this family may be encoded near each other
EDPLVSFRFYVEIDGETVAGFSSVSGLQITMDVIEYREGGGNENERKLPGRTKYGPVTLKRGVTNDSDLW
QWANDSMLNDMGTRRKNASIRLYNEAGEPLMRWEVINAWPTKYGAPDLDANSNQVAVESIELVHEGLKRQ
>gnl|CDD|274050 TIGR02242, putative_secreted_protein, phage tail protein domain. This model describes a region of sequence similarity shared by a number of uncharacterized proteins in bacterial genomes, including Geobacter sulfurreducens PCA, Mesorhizobium loti, Streptomyces coelicolor A3(2), Gloeobacter violaceus PCC 7421, and Myxococcus xanthus. In all cases, the genomic region resembles a phage tail region, based on tentative identifications of neighboring genes. A region of this domain resembles a region of TIGR01634, another phage tail protein model [Mobile and extrachromosomal element functions, Prophage functions]
LDMLPAVYRRDEVGDFLHRFVSCLEEVTDPLLSDLDALPDYFDPETAPAPFLDFLAQWLGNPFDDELDVP
QLRRLVARAADIYRQRGTRLGLRELLRLYLGIEPRIVEPFASDTLVGEDEFGVRVLGPDP
>gnl|CDD|274051 TIGR02243, hypothetical_protein_SCD8A.17c, putative baseplate assembly protein. This family consists of a large, conserved hypothetical protein in phage tail-like regions of at least six bacterial genomes: Gloeobacter violaceus PCC 7421, Geobacter sulfurreducens PCA, Streptomyces coelicolor A3(2), Streptomyces avermitilis MA-4680, Mesorhizobium loti, and Myxococcus xanthus. The C-terminal region is identified by the broader model pfam04865 as related to baseplate protein J from phage P2, but that relationship is not observed directly [Mobile and extrachromosomal element functions, Prophage functions]
DLDDRRYADLVREALGRLPPRSPEWTDHNASDPGITLVELLAWVADQLIYRLNRVARENYLAFLRLVGIR
PRPGLPARTWVTLTLDAPPADEGMLPAGTEVATLRTDAAGTEAVVFVTIQDLLVLACREGAVTTARGDFV
RLDGLRVRVTDANTRAPQKLKSTAAFPEFGEAPAPGACLLLGTEPEEPARLFWLDIARGNRLAIELASAG
GTPVGATAVRPAATVLDLPLRWEAWTEDGWQPLSLLRVDEDGTGGFPRTGADGFTDPLTGADVDLDRPAT
APPPRFTVLEARLPRDGGAVAGEHVLATACRTLPARPGAPFYTRSPRIARLRANTIGGTVTVGATHSETV
SEEGLGSGAGLPGQRFTLPASPALAGAARVALLVQADLGVEEEWKERDDLADSGPDDRHYVLDAGTATIT
FGDGQNGRIPPTGAVIRAAYRVGGGRAGNLRAGTLWVLRASPPYIAAVVNPLPAGGGTDAETLAEARLRA
PLPLRAVDRAVTLRDYEALALARAGLEVARAAALPAWEGEAGTVRLVVAVQAVVDAEGRRVDPGAALLTA
VRDALERRRLIGVRLAVAPPRYVGVTVRARVGLAPDVRAVRVERRVRARLTRFLNPVGGGFDGKGWPFGR
PVYRGELVAALQAVPGVVFVAVVRLG
>gnl|CDD|274052 TIGR02244, Cytosolic_purine_5'-nucleotidase, HAD superfamily (subfamily IG) hydrolase, 5'-nucleotidase. This model includes a 5'-nucleotidase specific for purines (IMP and GMP). These enzymes are members of the Haloacid Dehalogenase (HAD) superfamily. HAD members are recognized by three short motifs {hhhhDxDx(T/V)}, {hhhh(T/S)}, and either {hhhh(D/E)(D/E)x(3-4)(G/N)} or {hhhh(G/N)(D/E)x(3-4)(D/E)} (where "h" stands for a hydrophobic residue). Crystal structures of many HAD enzymes has verified PSI-PRED predictions of secondary structural elements which show each of the "hhhh" sequences of the motifs as part of beta sheets. This subfamily of enzymes is part of "Subfamily I" of the HAD superfamily by virtue of a "cap" domain in between motifs 1 and 2. This subfamily's cap domain has a different predicted secondary structure than all other known HAD enzymes and thus has been designated "subfamily IG". This domain appears to consist of a mixed alpha/beta fold. A Pfam model (pfam05761) detects an identical range of sequences above the trusted cutoff, but does not model the N-terminal motif 1 region. A TIGRFAMs model (TIGR01993) represents a (putative) family of _pyrimidine_ 5'-nucleotidases which are also subfamily I HAD's, which should not be confused with the current model
VFVNRELNLEKIQVFGFDMDYTLAQYKSPELEALIYDLAKERLVKRFGYPEELLSFAYDPTFAIRGLVFD
KLKGNLLKLDRFGNILRGYHGLRPLSDKEVQEIYGNKYISRSNGDRYYLLDTLFSLPEACLIAQLVDYFD
DHPKGPLAFDYRQIYQDVRDALDWVHRKGSLKKKVMENPEKYVLRDPKLPLFLSKLKEHGKKLFLLTNSD
YDYTDKGMKYLLGPFLGEHDWRDYFDVVIVDARKPGFFTEGRPFRQVDVETGSLKWGEVDGLEPGKVYSG
GSLKQFHELLKWRGKEVLYFGDHIYGDLLRSKKKRGWRTAAIIPELEQEVGILTNSKSLREEL
>gnl|CDD|131299 TIGR02245, unnamed_protein_product, HAD-superfamily subfamily IIID hydrolase, TIGR02245. This family of sequences appears to belong to the Haloacid Dehalogenase (HAD) superfamily of enzymes by virtue of the presence of three catalytic domains, in this case: LLVLD(ILV)D(YH)T, I(VMG)IWS, and (DN)(VC)K(PA)Lx{15-17}T(IL)(MH)(FV)DD(IL)(GRS)(RK)N. Since this family has no large "cap" domain between motifs 1 and 2 or between 2 and 3, it is formally a "class III" HAD
KLLRRIEQYKIKLLNPPREGKKLLVLDIDYTLFDHRSPAETGEELMRPYLHEFLTSAYEDYDIVIWSATS
MKWIEIKMTELGVLTNPNYKITFLLDSTAMITVHTPRRGKFDVKPLGVIWALLPEFYSMKNTIMFDDLRR
NFLMNPKNGLKIRPFKKAHANRGTDQELLKLTQYLKTIAELEDFSSLDHKEWERY
>gnl|CDD|274053 TIGR02246, hypothetical_protein, conserved hypothetical protein. This family consists of uncharacterized proteins found in a number of genera and species, including Streptomyces, Xanthomonas, Oceanobacillus iheyensis, Caulobacter crescentus CB15, and Xylella fastidiosa. The function is unknown
DDERAIRALVARWEAAWAAGDAEAFADLFAPDGVFVTVPGQVRKGREAIRAAHEAFFAGPYKGTRVTGDV
IEVRFLGPDLAIVHTIQTITAPGKGRARPDAAVRLTFVAVKRDGRWRLAADHNTPVRP
>gnl|CDD|274054 TIGR02247, Hypothetical_protein_K09H11.1, epoxide hydrolase N-terminal domain-like phosphatase. This model represents a small clade of sequences including C. elegans and mammalian sequences as well as a small number of bacteria. In eukaryotes, this domain exists as an N-terminal fusion to the soluble epoxide hydrolase enzyme and has recently been shown to be an active phosphatase, although the nature of the biological substrate is unclear. These appear to be members of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases by general homology and the conservation of all of the recognized catalytic motifs (although the first motif is unusual in the replacement of the more common aspartate with glycine...). The variable domain is found in between motifs 1 and 2, indicating membership in subfamily I and phylogeny and prediction of the alpha helical nature of the variable domain (by PSI-PRED) indicate membership in subfamily IA
AIKAVIFDFGGVLLPSPGVMRRWETERGLPGLKDFIVTVNITGPDFNPWARTFERGELTAEAFDGLFRHE
YGLRLGHDVRIAPVFPLLYGENTKLRPSMMAAIKTLRAKGFKTACITNNFPTDHSAEEALLPGDIMALFD
AVVESCLEGLRKPDPRIYQLMLERLGVAPEECVFLDDLGSNLKPAAALGITTIKVSDEEQAIHDLEKATK
L
>gnl|CDD|131302 TIGR02248, DNA_mismatch_repair_protein_MutH, DNA mismatch repair endonuclease MutH. This family consists exclusively of MutH, an endonuclease in some Proteobacteria that is activated by MutS1 and MutL for methylation-directed mismatch repair [DNA metabolism, DNA replication, recombination, and repair]
PPQTEEQLLSQAQSLSGYTLGELADELGIPVPNNLKRDKGWVGMLLERALGATAGSKPEQDFSHLGVELK
TIPINSEGYPLETTFVCVAPLTNNSGVTWENSHVRHKLKRVLWIPIEGERHIPLRERRVGAPILWKPTAE
QERQLKQDWEELMDLIVLGKVEQITARHGEVLQLRPKAANSKAVTKGIGKNGEIIDTLPRGFYLRKEFTA
QLLNAFF
>gnl|CDD|131303 TIGR02249, Integrase/recombinase_E2_protein., integron integrase. Members of this family are integrases associated with integrons (and super-integrons), which are systems for incorporating and expressing cassettes of laterally transferred DNA. Incorporation occurs at an attI site. A super-integron, as in Vibrio sp., may include over 100 cassettes. This family belongs to the phage integrase family (pfam00589) that also includes recombinases XerC (TIGR02224) and XerD (TIGR02225), which are bacterial housekeeping proteins. Within this family of integron integrases, some are designated by class, e.g. IntI4, a class 4 integron integrase from Vibrio cholerae N16961 [DNA metabolism, DNA replication, recombination, and repair, Mobile and extrachromosomal element functions, Other]
FLDQVREHMRTRHYAKRTEEAYLHWIKRFIRFHNKRHPSTMGDTEVEAFLSDLAVDGKVAASTQNQALNA
LLFLYKEILKTPLSLMERFVRAKRPRKLPVVLTREEVRRLLEHLEGKYRLIAKLLYGSGMRLMECLRLRI
QDIDFDYGEIRIRQGKGGKDRTVTLPKELIPPLREQIELARAYHEADLAEGYGGVYLPHALARKYPNAPK
EWGWQYLFPSHRLSRDPESGVIRRHHINETTIQRAVRRAVERAGIEKPVTCHTLRHSFATHLLESGADIR
TVQELLGHSDVKTTQIYTHVLNRGASGVLSPLDRL
>gnl|CDD|131304 TIGR02250, FCP1_euk, FCP1-like phosphatase, phosphatase domain. This model represents the phosphatase domain of the humanRNA polymerase II subunit A C-terminal domain phosphatase (FCP1) and closely related phosphatases from eukaryotes including plants, fungi, and slime mold. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDDppphW). This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in the human NLI interacting factor-like phosphatases, and together both are detected by the pfam03031
LLREKKLHLVLDLDQTLIHTTKDPTLSEWEKYDIEEPNSETRRDLRKFNLGTMWYLTKLRPFLHEFLKEA
SKLYEMHVYTMGTRAYAQAIAKLIDPDGKYFGDRIISRDESGSPHTKSLLRLFPADESMVVIIDDREDVW
PWHKRNLIQIEPYNYF
>gnl|CDD|274055 TIGR02251, protein_phosphatase_putative, Dullard-like phosphatase domain. This model represents the putative phosphatase domain of a family of eukaryotic proteins including "Dullard", and the NLI interacting factor (NIF)-like phosphatases. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDNxPxxa) and aparrently lacking the last aspartate. This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in FCP1-like phosphatases (TIGR02250), and together both are detected by the pfam03031
KKTLVLDLDETLVHSTFKMPKVDADFKVPVLIDGKIIQVYVFKRPHVDEFLERVSKWYELVIFTASLEEY
ADPVLDILDRGGKVISRRLYRESCVFTNGKYVKDLSLVGKDLSKVIIIDNSPYSYSLQPDNAIPIKSWFS
DPNDTELLNLIPFLEGLRFEDD
>gnl|CDD|274056 TIGR02252, Rhythmically_expressed_gene_2_protein, REG-2-like, HAD superfamily (subfamily IA) hydrolase. This family of proteins includes uncharacterized sequences from eukaryotes, cyanobacteria and Leptospira as well as the DREG-2 protein from Drosophila melanogaster which has been identified as a rhythmically (diurnally) regulated gene. This family is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called 'capping domain', or the absence of such a domain. This family is a member of subfamily 1A in which the cap domain consists of a predicted alpha helical bundle found in between the first and second catalytic motifs. A distinctive feature of this family is a conserved tandem pair of tryptophan residues in the cap domain. The most divergent sequences included within the scope of this model are from plants and have "FW" at this position instead. Most likely, these sequences, like the vast majority of HAD sequences, represent phosphatase enzymes
KLITFDAVGTLLALKEPVGEVYCEIARKYGVEVSPDELEQAFRKAFKAMSEAFPNFGFSSGLTPQQWWQK
LVRDTFGRAGVPDPESFEKIFEELYSYFATPEPWQVYPDAIKLLKDLRERGLILGVISNFDSRLRGLLEA
LGLLEYFDFVVTSYEVGAEKPDPKIFQEALERAGISPEEALHIGDSLRNDYQGARAAGWRALL
>gnl|CDD|274057 TIGR02253, Uncharacterized_HAD-hydrolase_PYRAB05140, HAD superfamily (subfamily IA) hydrolase, TIGR02253. This family of sequences from archaea and metazoans includes the human uncharacterized protein CTE7. Pyrococcus species appear to have three different forms of this enzyme, so it is unclear whether all members of this family have the same function. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549)
MIKAIFFDLDDTLIDTSGLAEKARRNAIEVLIEAGLNVDFEEAYEELLKLIKEYGSNYPTHFDYLIRRLW
EEYNPKLVAAFVYAYHKLKFAYLRVYPGVRDTLMELRESGYRLGIITDGLPVKQWEKLERLGVRDFFDAV
ITSEEEGVEKPHPKIFYAALKRLGVKPEEAVMVGDRLDKDIKGAKNAGMKTVWINQGKSSKMEDDVYPYP
DYEISSLRELL
>gnl|CDD|162788 TIGR02254, hydrolase_haloacid_dehalogenase-like_family, noncanonical pyrimidine nucleotidase, YjjG family. This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549)
YKTLLFDLDDTILDFQAAEALALRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSA
LLKEYNTEADEALLNQKYLRFLEEGHQLLPGAFELMENLQQKFRLYIVTNGVRETQYKRLRKSGLFPFFD
DIFVSEDAGIQKPDKEIFNYALERMPKFSKEEVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIP
TYEIRSLEELYEIL
>gnl|CDD|131309 TIGR02256, Uncharacterized_protein_y4qB, integrative and conjugative element protein, VC0181 family. This uncharacterized protein is found in several Proteobacteria, among them Rhizobium sp. NGR234, Vibrio cholerae, Myxococcus xanthus, and E. coli strain ECOR31. In the latter, it is part of an integrative and conjugative element that is readily induced to excise and circularize
VVVAMLKSYRQWHDLSTETGGVLIGERRGAHAVITKISEPGSGDIRTRKRFSRDGEHHQSEVDEHFEVSG
GVDTYLGEWHTHPEDQPEPSWTDRRSWRTIIRSPEAMLLLIVGRKEAWIGQKTRRAILFER
>gnl|CDD|131310 TIGR02257, Aerobic_cobaltochelatase_subunit_CobN, cobaltochelatase, CobN subunit [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
MHRLLTLPGGIDDNNNVALLEQTPADIVFLSSADSDLALLAAAWKALPDDLPSLRLANLDNLQHPASVDL
YVDSTARKAKIIVVRLLGGRGYWSYGLEQLQAWAEERGRQLILLPGDDDPDLELNELSTVPLDLSDRLWK
YLREGGPENMGRFLDCLAALLTQDEAPVPPKAIPKAGYYDPGRGVWPLEKGPRVGILFYRSLLLAGDTAL
IEALIDALRQRGLNPVPIFVSSLKDPAVQAGLLDALKEEDPALIITTTGFASSNEQADNGETLWDSLGVP
VLQVISSNTSREVWEDSSRGLAPRDLAMHVVLPELDGRITTRAISFKGVSDVDPALESAITTYRPDPDRI
KWVADLAANWIKLQRKPNAERRIALVLANYPVRDGRIGNGVGLDTPASVVNILHALKEQGYDLGGGPIPS
NGDALIRLLIRGRTNDLESHDREPLDKLSLDEYLTFWDTLPLKAKQEIVLRWGEPSQDPDLEDKKGFPIN
GLRFGNIFVLIQPDRGYDIDPIADYHSPDLAPPHRYLAFYFWLRKVFGADAIVHVGKHGTLEWLPGKGVG
LSETCFPEIVLGPLPHIYPFIVNDPGEGAQAKRRTHAVILDHLTPPLTRAGLYGPLHDLERLLDEYYEAD
LLDRRRLDILERQILDLIQDLGLDSEIGVDRSDKPDSALERLDAYLCDLKESQIRDGLHIFGRAPDDLSD
APWRQSTEAEIAGLLAGLNGRYVSAGPSGAPTRGRPDVLPTGRNFYSVDLRGLPTPAAWDLGKKSAEQLI
ERYLQDHGDWPRSLALSVWGTATMRTGGEDIAQALALLGVRPVWDGASRRVIDLEVIPLSLLGRPRVDVT
LRISGLFRDAFPNLIALVDKAVQAVAQLDEPDELNPLAARTRAEGRASPRIFGSKPGAYGAGLQELISSG
DWETREDLAEAYLNWSSWAYGAGAEGIAAREALEQRLKEIQVVLHNQDNREHDLLDSDDYYQFQGGLSAA
VEQLSGQRPDIYHGDHSRPEKPKIRSLEEEINRVVRARVLNPKWIDGMKRHGYKGAFEFAATVDYLFAYD
ATTEAVPDWCYEAIYDAYLLDAEVRAFLIEHNPWALRDMAERLLEAINRGLWTPLRNSILDDLKALILEA
EA
>gnl|CDD|274058 TIGR02258, UPF0097_protein_AF_2157, 2'-5' RNA ligase. This protein family consists of bacterial and archaeal proteins with two tandem copies of Pfam domain pfam02834. Members for which activity has been measured perform a reversible, ATP-independent 2'-5'-ligation of what is presumably a non-phyiological substrate: half-tRNA splice intermediates from an intron-containing yeast tRNA. The physiological substrate(s) in prokaryotes may include small 2'-5'-link-containing oligonucleotides, perhaps with regulatory or biosynthetic roles [Transcription, RNA processing]
MRLFIAIDLPPEIREQLSRIQRKLKSPLDGIKWVPPENLHITLKFLGEVDEEQVEELEDALAKIAEPPFT
LKLEGIGVFGNPKRPRVLWAGVEQSEELTQLHADLERELAKLGFSKEERPFTPHITLARKKSGKPGVPEF
LQEFANEEFGSFHVDEFHLYSSTLTPGGPIYEPLARFQL
>gnl|CDD|131312 TIGR02259, A-subunit_of_benzoyl-CoA_reductase, benzoyl-CoA reductase, bcr type, subunit A. This model describes A, or gamma, subunit of the bcr type of benzoyl-CoA reductase, a 4-subunit enzyme. Many aromatic compounds are metabolized by way of benzoyl-CoA. This family shows strong sequence similarity to the 2-hydroxyglutaryl-CoA dehydratase alpha chain and to subunits of different types of benzoyl-CoA reductase (such as the bzd type)
MECFVGIDLGSTTTKAVLMDDKGEVIGRGITNSRSNYATAARVAKEEAFIDARFSLFRRALDKEEAGAEH
SAEFIAALERNFRLEQFIEQLDDLEETCHANLEAERFAAKAGAIQEALHEIFARLREEEAAKLFAPDAKR
KSDFFRDIAGSRFHQHAEAVARAMGIAFDHLLHAYDKSIIEVENRPPGADLNEKFRRAMARMLAEDSHAA
DGEAAFAAMIDAALEIDLEERYLVGTGYGRVRLPFPKEHIRSEILCHGLGAHLMYPGTRTVLDIGGQDTK
GIQIDDHGIVENFQMNDRCAAGCGRYLGYIADEMNMGLHELGPLAMKSSKPARINSTCTVFAGAELRDRL
ALGDKREDILAGLHRAIILRAISIISRSGGITDQFTFTGGVAKNEAAVKELRKLIKENYGEVQINIDPDS
IYTGALGASEFA
>gnl|CDD|131313 TIGR02260, B-subunit_of_benzoyl-CoA_reductase, benzoyl-CoA reductase, bcr type, subunit B. This model describes B, or beta, subunit of the bcr type of benzoyl-CoA reductase, a 4-subunit enzyme. Many aromatic compounds are metabolized by way of benzoyl-CoA
EAIKDASMAKQKEMIAAHYDRLAGAKERGEKVAATFVPGNLNELIMCFDMVNNLPETNAIQNGLRKQSGG
MIMDAEKAGHSEDVCTYVKADIGMMAKGNIAPNGKPLPAPDMLLLSYTGCFTFMKWFELLRHEYKCETIM
FQIPYLADGKITKDMIDFMVKQLKEDVIPKFEQISGVKFDIDRLREYLKKSAKAEDDHVWVLESAKHKPS
PIDAYFGGIYYIGPIFGAFRGTADAIEYYGFLRAEIEQRIAEGKGPITPDGDMGEEKYRLVVEGPPNWTN
FREFWKLFYDEGAVVVASSYTKVGGLYDQGFRHDPDDPLESLADYCLGCYTNNNLPMRVDLLEKYINEYE
ADGLLINSIKSCNSFSAGQLLMMREIEKRTGKPAAFIETDLVDPRYFSAANVKNRLESYFQMI
>gnl|CDD|131314 TIGR02261, D-subunit_of_benzoyl-CoA_reductase, benzoyl-CoA reductase, bcr type, subunit D. This model describes the D subunit of benzoyl-CoA reductase, a 4-subunit enzyme. Many aromatic compounds are metabolized by way of benzoyl-CoA. This family shows sequence similarity to the A subunit (TIGR02259) and to the 2-hydroxyglutaryl-CoA dehydratase alpha chain
TITAGIDIGTGAIKTVLFEVDGDKEECLAKRNDRIRQRDPFKLAEDAYDDLLEEAGLAAADVAYCATTGE
GESLAFHTGHFYSMTTHARGAIYLNPEARAVLDIGALHGRAIRMDERGKVEAYKMTSQCASGSGQFLENI
ARYLGIAQDEIGSLSQQADNPEKVSGICAVLAETDVINMVSRGISAPNILKGIHESMADRLAKLLKSLGA
LDGTVLCTGGLALDAGLLEALKDAIQEAKMAVAAENHPDAIYAGAIGAALWG
>gnl|CDD|274059 TIGR02262, benzoate-CoA_ligase, benzoate-CoA ligase family. Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases
EKYNAAEDLLDRNVVEGRGGKTAFIDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPI
AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVVGRPEAGEV
QLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAA
KLFFAYGLGNALTFPMSVGATTVLMGERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRL
RLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQD
VADGEPGELLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPF
EIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLP
KTATGKIQRFKLREG
>gnl|CDD|131316 TIGR02263, C-subunit_of_benzoyl-CoA_reductase, benzoyl-CoA reductase, subunit C. This model describes C subunit of benzoyl-CoA reductase, a 4-subunit enzyme. Many aromatic compounds are metabolized by way of benzoyl-CoA. This enzyme acts under anaerobic conditions
TADIIARCEALFEDLDFTAAREWKAADPGRIVIAFLPVYAPREIIHAAGGLPLGIFGGGDGLEVIHGDAF
YQSYICRIPRSTIELGLSGRLDFVDGMLFPSICDVIRNLSGMWKLMFPGKGARYFDLPHNFDDDLGGEFY
TAELNELCEGLEHLSGKKITDDAIRASIAVFNDNRKLIQALYGLRADEPWKVPSADLYLLLRAGLVIPVE
EHNQMLADYLAAARKQEAPIKDNCRVIICGMFCEQPPLNLIKSIELSGCYIVDDDFIIVHRFENNDVALA
GDPLQNLALAFLHDSISTAAKYDDDEADKGKYLLDQVRKNAAEGVIFAAPSFCDPALLERPMLAARCKEH
GIPQIAFKYAENSGQMQPIREQAGTFADSI
>gnl|CDD|131317 TIGR02264, gmx_para_CXXCG, Myxococcus xanthus double-CXXCG motif paralogous family. This family consists of at least 10 paralogous proteins from Myxococcus xanthus that lack detectable sequence similarity to any other protein family. An imperfectly conserved CXXCG motif, a probable binding site, appears twice in the multiple sequence alignment
RFYRVEADTASRYTGSLDAAHKWCLPGLAPCPVCGAGWGGAGLAYPCVDLSSLPERKLLEEPRPEPFEEF
SRLREQVRPLAPPGALLEPGTQFGPLVGKASGRFGDLALQAWSLLLIRIEALERLRAAGVRGLHGAPGDL
RFRGKNPPELLELQLLPHGRLHPDCLPPDREPPCPTCGSESNGLPDTYVLDAASLPVDVDLFRLRDFPTL
IVATERFVEAVKRLELDGVTFRELSVR
>gnl|CDD|131318 TIGR02265, Mxa_TIGR02265, Myxococcales-restricted protein, TIGR02265 family. This family consists of a set of at least 17 paralogous proteins in Myxococcus xanthus DK 1622. Members are about 200 amino acids in length. No other homologs are known; the function is unknown
LELLVFDDTVRGLFFRGLLDRVTPEAVERLRQAGLDLDRDLLPAYPLEQWLRLLRVAAELLAPQLPLEEA
FRALGERAVTGFRSTVVGRALLGLVRLLGPRRLLSRAPQGYRAAVNYGERRVVETGPTSGRLWMNRDFMP
PAYHEGVLHAALRAVGARDVRVRGRAFGGLDATYRLSWS
>gnl|CDD|274060 TIGR02266, gmx_TIGR02266, Myxococcus xanthus paralogous domain TIGR02266. This domain is related to Type IV pilus assembly protein PilZ (pfam07238). It is found in at least 12 copies in Myxococcus xanthus DK 1622
RVPARLKVDFRTDSEFLRDYSINLSKGGLFIRTRKPLAVGTRVELKLTLPGGERPVELKGVVAWVRPAAD
GGPPGMGVRFEDLDAESRARLQRVVS
>gnl|CDD|131320 TIGR02267, TIGR02267, DUSAM domain. This family consists of at least eight paralogs in Myxococcus xanthus and six in Stigmatella aurantiaca DW4/3-1, both members of Myxococcales order within the Deltaproteobacteria. The function is unknown. Some member proteins consist of two copies of the domain. This domain is hereby named DUSAM, DUplication in Stigmatella And Myxococcus
MAEHLDWDPIRELARRVLRLGEPLVLTDEVRALLLRTAREVAITPADVTQALADDVSALALLKEISRRIR
VGSRRLSRALTEAIRHRDAGDLDGARALLLDVLAVEVVPFYRELAQVQLEALD
>gnl|CDD|131321 TIGR02268, TIGR02268, Myxococcus xanthus paralogous family TIGR02268. This family consists of at least 8 paralogs in Myxococcus xanthus, a member of the Deltaproteobacteria. The function is unknown
MTAVLLLAGTAALAQPSATARWRRERRVEVLAASAGPPPEVRVAPGVSTTLLFDAPIVREGLLLEGLERF
RRLDVTETHLILVPSEALPEGERLPLTVRFADGAVPQRAVLELVTDPARVERQVEVRRHARTAASYQQEV
VELRARNQLLEEENARLRRQQPRPEGLAGLLLSGAIDKITGVAATWLDVRPHSENELVVRSALSYRSPGW
VAVAVNLENPPGAAPWQAGGAALTGLDGNELKELPVWQEGPLLPGGFSRVLVVAEPAPTAPPGPYTLELW
DEGRKRTLTLANVKF
>gnl|CDD|131322 TIGR02269, TIGR02269, Myxococcus xanthus paralogous lipoprotein family TIGR02269. This family consists of at least 9 paralogs in Myxococcus xanthus, a member of the Deltaproteobacteria. One appears truncated toward the N-terminus; the others are predicted lipoproteins. The function is unknown
ALVAWLLALVFTGCASTAPKSPHAWAEVPHGEECSCTREDRCVSLACAGGQCGLYVCEDVAGRVEPALGG
TARPPAAPGAGPHRRWGNVLGIRGGNGPVMVFPWRNAPPSEHRAPRLPLGPGRWVRHHLFPQAPELAKWF
ARRGVKIHDFTLVIPRHTHRRIHSGAGRGGAWNQAWRDFARRYPGASPEEIWRHAGELIFRFELTGPIVP
Y
>gnl|CDD|131323 TIGR02270, hypothetical_protein_GSU3180, conserved hypothetical protein. Members are found in Myxococcus xanthus (six members), Geobacter sulfurreducens, and Pseudomonas aeruginosa; a short protein homologous to the N-terminal region is found in Mesorhizobium loti. All sequence are from Proteobacteria. The function is unknown [Hypothetical proteins, Conserved]
IIWEILAQHLEEAAFLWRQWKRALVAPDYVLEDLAELEERLLAHVDGLVLAGKAATELLVSALAEADEPG
RVACAALALLAQEDALDLRSVLAVLQAGPEGLCAGIQAALGWLGGRQAEPWLEPLLAASEPPGRAIGLAA
LGAHRHDPGPALEAALTHEDALVRAAALRALGELPRRLSESTLRLYLRDSDPEVRFAALEAGLLAGSRLA
WGVCRRFQVLEGGPHRQRLLVLLAVAGGPDAQAWLRELLQAAATRREALRAVGLVGDVEAAPWCLEAMRE
PPWARLAGEAFSLITGMDVALEELAGERPEDVAPGPEDDDEDANVALDPEENLPLPDAERVAAWWAENAP
RFKPGVRYLRGKPLGQESLLDALREGSMRRRRAAALELARRTRGAPGFGVRAPTRRQRAE
>gnl|CDD|131324 TIGR02271, Stress_response_protein_YsnF, conserved domain. This model describes an uncharacterized domain, sometimes found in association with a PRC-barrel domain (pfam05239, which is also found in rRNA processing protein RimM and in a photosynthetic reaction center complex protein). This domain is found in proteins from Bacillus subtilis, Deinococcus radiodurans, Nostoc sp. PCC 7120, Myxococcus xanthus, and several other species. The function is not known
LKLRKEQLDVNKEWVQTGEVELGKEVSSEQKTVDIPVEHEEVVIERRPVTDNEASDDPIGDKEVIRVPVS
EEKVNVSKHRVVTEEVSVGKRDVEETEHIEETVKKEEPRINTEGN
>gnl|CDD|131325 TIGR02272, gentisate_12-dioxygenase, gentisate 1,2-dioxygenase. This family consists of gentisate 1,2-dioxygenases. This ring-opening enzyme acts in salicylate degradation that goes via gentisate rather than via catechol. It converts gentisate to maleylpyruvate. Some putative gentisate 1,2-dioxygenases are excluded by a relatively high trusted cutoff score because they are too closely related to known examples of 1-hydroxy-2-naphthoate dioxygenase. Therefore some homologs may be bona fide gentisate 1,2-dioxygenases even if they score below the given cutoffs
EREAFYSKISGQNLTPLWEVLHALVPAEPKSNCAPHHWNYQEIRPLLMEAGDLISAKEAERRVLVLENPG
LRGQSSITTSLYAGLQLILPGEVAPSHRHTQSALRFIVEGKGAFTAVDGERTTMHPGDFIITPSWTWHDH
GNPGDEPMIWLDGLDIPLVQLFDCSFAEGYPEDQQPVTRPEGDSLARYGHNMLPVRHKRSDRSSPIFNYP
YERSREALDDLTRTGEWDPWHGLKLRYVNPATGGYPMPTIGAFIQLLPKGFRTATYRSTDATVFCVVEGR
GQVRIGDAVFRFSPKDVFVVPSWHPVRFEASDDAVLFSFSDRPVQQKLGLFREAR
>gnl|CDD|274061 TIGR02273, Ribosome_maturation_factor_RimM, 16S rRNA processing protein RimM. This family consists of the bacterial protein RimM (YfjA, 21K), a 30S ribosomal subunit-binding protein implicated in 16S ribsomal RNA processing. It has been partially characterized in Escherichia coli, is found with other translation-associated genes such as trmD. It is broadly distributed among bacteria, including some minimal genomes such the aphid endosymbiont Buchnera aphidicola. The protein contains a PRC-barrel domain that it shares with other protein families (pfam05239) and a unique domain (pfam01782). This model describes the full-length protein. A member from Arabidopsis (plant) has additional N-terminal sequence likely to represent a chloroplast transit peptide [Transcription, RNA processing]
LLVVGKIGGPHGIKGEVKVKSFTDFPESLFDYGPWLILKGSKQWQTVKVARVRKQNNKLIVKFEGIDDRE
AAEALKGLELFVPREALPELEEDEYYWTDLIGLEVVTEEGEELGKVVEILETGANDVLVVRSKKGKKEVL
IPFVEEIVKEIDLEKKIITVDWPEG
>gnl|CDD|274062 TIGR02274, Probable_deoxycytidine_triphosphate_deaminase, deoxycytidine triphosphate deaminase. Members of this family include the Escherichia coli monofunctional deoxycytidine triphosphate deaminase (dCTP deaminase) and a Methanocaldococcus jannaschii bifunctional dCTP deaminase (3.5.4.13)/dUTP diphosphatase (EC 3.6.1.23), which has the EC number 3.5.4.30 for the overall operation [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
ILSDRDIKRWLEEGLLKIEPLDEEQLQPAGVDLRLGNEFRVFRNHTGAVIDPENPKEAVSYLFEVEEGEE
FVIPPGEFALATTLEYVKLPDDVVGFLEGRSSLARLGLFIHVTAGRIDPGFEGNITLELFNAGKLPVKLR
PGMRIAQLVFERLSSPAERPYNGRSGKYQGQRGVTPSRI
>gnl|CDD|274063 TIGR02275, Includes:_23-dihydroxybenzoate-AMP_ligase, 2,3-dihydroxybenzoate-AMP ligase. Proteins in this family belong to the AMP-binding enzyme family (pfam00501). Members activate 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate; many are involved in synthesis of siderophores such as enterobactin, vibriobactin, vulnibactin, etc. The most closely related proteine believed to differ in function activates salicylate rather than DHB [Transport and binding proteins, Cations and iron carrying compounds]
IEFTPWPEELAERYREKGYWQDKPLTDILRDQAARYPDAIAIICGNRQWSYRELDQRADNLAAGLTKLGI
KQGDTAVVQLPNIAEFYIVFFALLKLGVAPVLALFSHRKSELTAYASQIEPALYIIDRAHSLFDYDDFAR
QLQSKLPTLRNIIVAGQTGEAELFLWLESPAEPVKFPPTKSDEVAFFQLSGGSTGTPKLIPRTHNDYYYS
VRRSVEICWLTQQTRYLCALPAAHNYPLSSPGALGVFYAGGCVVLAPDPSPTDCFPLIERHKVTVTALVP
PAVALWMQAASKSRADLSSLKLLQVGGAKFSAAAARRVPAVFGCQLQQVFGMAEGLVNYTRLDDPAEIIF
TTQGRPMSPDDEVRVVDDHGNPVAPGETGMLLTRGPYTFRGYYKAPEHNAAAFDAEGFYYTGDLVRLTPE
GYIVVVGRAKDQINRGGEKIAAEEIENLLLAHPAVHDAALVSMPDELLGEKSCAFIVVRDPALKAAQLRR
FLRERGLAEYKLPDRVEFVDSLPLTAVGKVDKKALR
>gnl|CDD|213697 TIGR02276, surface_antigen_gene, 40-residue YVTN family beta-propeller repeat. This repeat of about 40 amino acids is found in up to 14 copies per protein. Archaea Methanosarcina mazei and Methanosarcina acetivorans each have over 10 genes that encode tandem copies of this repeat, which is also found in other species. PSIPRED predicts with high confidence that each 40-residue repeats contains four beta strands. This model overlaps somewhat with the NHL repeat (pfam01436) and also shows sequence similarity to the WD domain, G-beta repeat (pfam00400)
PDGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAVS
>gnl|CDD|274064 TIGR02277, Transcriptional_repressor_PaaX, phenylacetic acid degradation operon negative regulatory protein PaaX. This transcriptional regulator is always found in association with operons believed to be involved in the degradation of phenylacetic acid. The gene product has been shown to bind to the promoter sites and repress their transcription [Regulatory functions, DNA interactions]
SLIVTLYGDAIRPRGGAIWLGSLIEFLAGLGINERLVRTAVSRLVAQGWLQSERKGRRSFYSLTDKGRRR
FAAAAQRIYDPPAPAWDGKWRLLLLSGPEESLRDELRKELVWSGFGLLAPSLWVTPSPLPEQVETLLEKY
DISPAVHFRCEDAAGMGELKALAEKCWDLDEIADAYLAFIQKFGPLYVLLKNKAGELSPAAAFVARLLLV
HEYRRVVLRDPLLPEELLPADWPGDAARHLCARIYRTLAPPAERFLDSVGATENGPLPKAKELNFLRFGG
>gnl|CDD|131331 TIGR02278, PaaN-DH, phenylacetic acid degradation protein paaN. This enzyme is proposed to act in the ring-opening step of phenylacetic acid degradation which follows ligation of the acid with coenzyme A (by PaaF) and hydroxylation by a multicomponent non-heme iron hydroxylase complex (PaaGHIJK). Gene symbols have been standardized in. This enzyme is related to aldehyde dehydrogenases and has domains which are members of the pfam00171 and pfam01575 families. This family includes paaN genes from Pseudomonas, Sinorhizobium, Rhodopseudomonas, Escherichia, Deinococcus and Corynebacterium. Another homology family (TIGR02288) includes several other species
LQSYLSGEWRTGQGEGVPVRDASTGEVLARVTSEGLDVAAAVAWAREVGGPALRALTFHERARMLKALAQ
YLSERKEALYALAATTGATRRDNWVDIDGGIGTLFTYSSLGRRELPDANLIPEDEFEPLSKDGSFQGRHI
LTPKGGVAVQINAFNFPVWGLLEKFAPAFLAGVPTLAKPATPTAYVAEALVRTMVESGLLPEGSLQLICG
SAGDLLDHLDHRDVVAFTGSAATADRLRAHPNVLERGIRFNAEADSLNAAILGEDATPDEPEFDLFAQEI
VRELTIKAGQKCTAIRRVIVPKALLEAVLKALQARLAKVVLGDPREEGVDMGPLVSLEQRADVEAAVAAL
LAAGAEVRLGGPGRLDGAFFPPTLLLAEDPWAGAVHATEAFGPVATFFPYGDRAEAARLAARGGGSLVAT
LATSDPEEARQFILGLAPYHGRLHILNRDDAAESTGHGSPLPRLLHGGPGRAGGGEELGGLRSVKHYMQR
TAIQGSPWLLAALTGQWARGAEVPGAEVHPFRKPYEDLEIGDSLTTHRRTVTEADIALFAALSGDHFYAH
MDEIAARESFFGKRVAHGYFVLSAAAGLFVDPAPGPVLANYGLENLRFLEPVGPGDTIQVRLTVKRKTPR
DEKTYGVVEWAAEVVNQNGEPVATYDVLTLVAR
>gnl|CDD|188207 TIGR02279, 3-hydroxyadipyl-CoA_dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase PaaC. This 3-hydroxyacyl-CoA dehydrogenase is involved in the degradation of phenylacetic acid, presumably in steps following the opening of the phenyl ring. The sequences included in this model are all found in aparrent operons with other related genes such as paaA, paaB, paaD, paaE, paaF and paaN. Some genomes contain these other genes without an apparent paaC in the same operon - possibly in these cases a different dehydrogenase involved in fatty acid degradation may fill in the needed activity. This enzyme has domains which are members of the pfam02737 and pfam00725 families
ALTNVVTVAVIGAGAMGAGIAQVAASAGHQVLLYDIRAEALARAIAGIEARLNSLVTKGKLTAEECERTL
KRLIPVTDLHALADAGLVIEAIVENLEVKKALFAQLEELCPADTIIASNTSSLSITAIAAGLARPERVAG
LHFFNPAPVMALVEVVSGLATAAEVAEQLYETALAWGKQPVHCHSTPGFIVNRVARPYYAEALRALEEQV
AAPAVLDAALRDGAGFPMGPFELTDLIGHDVNFAVTCSVFNAFWQDRRFLPSLVQQELVIAGRLGRKSGL
GVYDYREEAEAVVPLEAVSDSFSPRVTVVGDIGAAAPLLARLEAAGIKVEKKSGMGVTQIGDALLALTDG
RTAQARAIELARPNLVLFDLVLDYSTGKRIAIAAAAVNPDSATRKAIYYLQQAGKKVLQIADYPGLLILR
TVAMLANEAADAVLQGVASAQDIDTAMRLGVNYPYGPLAWAAQLGWQRILRVLENLQHHYGEERYRPSSL
LRRRALLGSGYED
>gnl|CDD|274065 TIGR02280, 12-epoxyphenylacetyl-CoA_isomerase, phenylacetate degradation probable enoyl-CoA hydratase paaB. This family of proteins are found within apparent operons for the degradation of phenylacetic acid. These proteins contain the enoyl-CoA hydratase domain as detected by pfam00378. This activity is consistent with current hypotheses for the degradation pathway, which involve the ligation of phenylacetate with coenzyme A (paaF), hydroxylation (paaGHIJK), ring-opening (paaN) and degradation of the resulting fatty acid-like compound to a Krebs cycle intermediate (paaABCDE)
ILSHLEKGVATLTLNRPDKLNSFNAEMHAELAEALKRVERDDTARALLLTGAGRGFCAGQDLSDRNVTPG
PAPDLGMTVERFYNPLVRRLAALPKPVICAVNGVAAGAGANLALAGDIVIAARSAKFIQAFSKLGLIPDS
GGTWLLPRLVGRARAMGLALLGNKLSAEQAHEWGLIWQVVDDATLMDEAQALARHLATQPTRGLGLIKRA
IQAAETNSLDTQLDLERDLQREAGRSADYAEGVSAFLDKRSPQFTGK
>gnl|CDD|131334 TIGR02281, Uncharacterized_protein_RP867, clan AA aspartic protease, TIGR02281 family. This family consists of predicted aspartic proteases, typically from 180 to 230 amino acids in length, in MEROPS clan AA. This model describes the well-conserved 121-residue C-terminal region. The poorly conserved, variable length N-terminal region usually contains a predicted transmembrane helix. Sequences in the seed alignment and those scoring above the trusted cutoff are Proteobacterial; homologs scroing between trusted and noise are found in Pyrobaculum aerophilum str. IM2 (archaeal), Pirellula sp. (Planctomycetes), and Nostoc sp. PCC 7120 (Cyanobacteria) [Protein fate, Degradation of proteins, peptides, and glycopeptides]
SVQLAKDGDGHFYATGRVNGRNVRFLVDTGATSVALNEEDAQRLGLDLNRLGYTVTVSTANGQIKAARVT
LDRVAIGGIVVNDVDAMVAEGGALSESLLGMSFLNRLSRFTVRGGKLILRQ
>gnl|CDD|274066 TIGR02282, Membrane-bound_lytic_murein_transglycosylase_B, lytic murein transglycosylase B. This family consists of lytic murein transglycosylases (murein hydrolases) in the family of MltB, which is a membrane-bound lipoprotein in Escherichia coli. The N-terminal lipoprotein modification motif is conserved in about half the members of this family. The term Slt35 describes a naturally occurring soluble fragment of MltB. Members of this family never contain the putative peptidoglycan binding domain described by pfam01471, which is associated with several classes of bacterial cell wall lytic enzymes [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
QAFIDTLVAKHGFDRAQLEAILAQAKYNDEVIRLIDNPAESAKPWLEYRGIFITPKRIQDGVEFWKQHED
ALNRAEQRYGVPPEIIVAIIGVETNYGRNMGKYRVLDALTTLAFDYPRRATFFRGELGQFLLLAREEQLD
PLTLKGSYAGAMGYPQFMPSSYRQYAVDFDGDGHIDLWNSPDDAIGSVANYFHAHGWVRGDPVAVPATGA
APGDQLPNKFAKPHYSLSQLAAAGLIPQAPLGNEQKASLVDLDVGGGDQYWLGLPNFYAITRYNRSTFYA
MAVYQLSQAL
>gnl|CDD|274067 TIGR02283, Membrane-bound_lytic_murein_transglycosylase_B, lytic murein transglycosylase. Members of this family are closely related to the MltB family lytic murein transglycosylases described by TIGR02282 and are likewise all proteobacterial, although that family and this one form clearly distinct clades. Several species have one member of each family. Many members of this family (unlike the MltB family) contain an additional C-terminal domain, a putative peptidoglycan binding domain (pfam01471), not included in region described by this model. Many sequences appear to contain N-terminal lipoprotein attachment sites, as does E. coli MltB in TIGR02282 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
GFDAWLAQLRAEAAAKGISAATFDRAFAGIKEPDQSVLNLDRNQPEFTQTFWDYLSRRVSPRRIAIGRAM
LQRYAALLARIEKRYGVPAEILLAIWGMESDFGAYQGKFDVIRSLATLAYDGRRKDYFRTELIAALKILQ
RGDLTRAAMKGSWAGAMGQTQFLPSSYLNYAVDFDGDGRRDIWNSVPDALASTANYLVNGGWKRGEPWGY
EVQLPAGFDYALSGSQIKKPIAEWQRLGVTRVDGRPLPASAANAEASLLLPDGRKGPAFLVTPNFRVIKE
WNRSDYYALTIGLLADRIAG
>gnl|CDD|131337 TIGR02284, conserved_hypothetical_protein, conserved hypothetical protein. Members of this protein family are found mostly in the Proteobacteria, although one member is found in the the marine planctomycete Pirellula sp. strain 1. The function is unknown
TIHSLNDLIEISIDGKDGFEESAEEVKDPELATLFRRIAGEKSAIVSELQQVVASLGGKPEDHGSMVGSL
HQFWGKIRATLTPNDDYVVLEEAERGEDRAKKAYDETLADQDTPAAARDVALRQYPGVRACHDVIRALR
>gnl|CDD|131338 TIGR02285, conserved_hypothetical_protein, conserved hypothetical protein. Members of this family are found in several Proteobacteria, including Pseudomonas putida KT2440, Bdellovibrio bacteriovorus HD100 (three members), Aeromonas hydrophila, and Chromobacterium violaceum ATCC 12472. The function is unknown [Hypothetical proteins, Conserved]
GLLLLLAFAGAIPLAAKEAITWIVNDFPPFFIFSGPSKGRGVFDVILQEIRRALPQYEHRFVRVSFARSL
KELQGKGGVCTVNLLRTPEREKFLIFSDPTLRALPVGLVLRKELTAGVRDEQDGDVDLKKLLASKKKRLG
VIASRSYGQQIDDILSDSGYQHNTRIIGNAAMGNLFKMLEKGRVNYTLAYPPEKTYYEELNNGALPPLKF
LPVAGMPAHISVWVACPKTEWGRKVIADIDQALSELNVDPKYYKYFDRWLSPEMKEGY
>gnl|CDD|131339 TIGR02286, Acyl-coenzyme_A_thioesterase_PaaI, phenylacetic acid degradation protein PaaD. This member of the domain family TIGR00369 (which is, in turn, a member of the pfam03061 thioesterase superfamily) is nearly always found adjacent to other genes of the phenylacetic acid degradation pathway. Its function is currently unknown, but a role as a thioesterase is not inconsistent with the proposed overall pathway. Sequences scoring between trusted and noise include those from archaea and other species not known to catabolize phenylacetic acid and which are not adjacent to other genes potentially involved with such a pathway
AKALGIDILELGPGFARVAMTVRADMLNGHGTAHGGFLFSLADSAFAYACNSYGDAAVAAQCTIDFLRPG
RAGERLEAEAVEVSRGGRTGTYDVEVVNQEGELVALFRGTSRRL
>gnl|CDD|131340 TIGR02287, Phenylacetic_acid_degradation_protein_PaaY, phenylacetic acid degradation protein PaaY. Members of this family are located next to other genes organized into apparent operons for phenylacetic acid degradation. PaaY is located near the end of these gene clusters and often next to PaaX, a transcriptional regulator [Energy metabolism, Other]
CYQIDGLTPVVHPEAYVHPTAVLIGDVILGKRCYVGPLASLRGDFGRIVLKEGANIQDNCVMHGFPGQDT
VVEENGHVGHGAILHGCIVGRNALVGMNAVVMDGAVIGENSIVAASAFVKAGAEMPAQYLVVGSPAKVIR
ELSEQELAWKKQGTHEYQVLATRCKQTLHQCEPLREAEPGRPRMVDENVRPK
>gnl|CDD|131341 TIGR02288, putative_ring-opening_enzyme, phenylacetic acid degradation protein paaN. This enzyme is proposed to act in the ring-opening step of phenylacetic acid degradation which follows ligation of the acid with coenzyme A (by PaaF) and hydroxylation by a multicomponent non-heme iron hydroxylase complex (PaaGHIJK). Gene symbols have been standardized in. This enzyme is related to aldehyde dehydrogenases and has a domain which is a member of the pfam00171 family. This family includes sequences from Burkholderia, Bordetella, Streptomyces. Other PaaN enzymes are represented by a separate model, TIGR02278
AAQLFDRHRPTLEAAVQAIAARGYWSPFPESPKVYGETAQDDGQAAFEALFGQDFDLGQPGRSGWVGGER
SPYGVELGVTYPQCDGDALLDAAHAALPGWRDAGARARAGVCLEILQRLNARSFEIAHAVMHTTGQAFMM
AFQAGGPHAQDRGLEAVAYAYREMSRIPETAVWEKPQGKNDPLKLKKRFTIVPRGIALVIGCSTFPTWNT
YPGLFASLATGNPVLVKPHPGAILPLALTVQVAREVLGEAGFDPNLVTLAAFDPGHEAAQRLATDPAVRI
IDFTGSNAFGQWLEQNARQAQVYTEKAGVNTVIIESTDDYKAMLRNLAFSLSLYSGQMCTTTQAILVPRD
GIRTDQGRKSYDEVAADLATAIDGLLGDPARATAVLGAIQSPDTLARIAEARALGEVLLASTKIEHPEFP
GARVRTPLLLKCDAADEAAYMQERFGPIAFVVAVDDGAHAVELARRSVREKGAMTVGAYTTDPEVVDAVQ
EAAWDAAVALSLNLTGGVFVNQSAAFSDFHGTGGNPAANASLSDGAFVANRFRVVQRRRPA
>gnl|CDD|274068 TIGR02289, Oligoendopeptidase_F, oligoendopeptidase, M3 family. This family consists of probable oligoendopeptidases in the M3 family, related to lactococcal PepF and group B streptococcal PepB (TIGR00181) but in a distinct clade with considerable sequence differences. The likely substrate is small peptides and not whole proteins, as with PepF, but members are not characterized and the activity profile may differ. Several bacteria have both a member of this family and a member of the PepF family
IEELEKKFTELLEKFINSKEEQENWINEINDVRDDIEEMITLAYIRHSVDTDDEEFYKEEEHFQDEIKPL
LKRYNTKFDQKIIESPFREELEARFYKLLFKLIKCDLKLFSEENIPLLQKENKLSTKYTEIIANIKIDFE
GEEKTLSQLIPFLQDPNRSTRKKAWEARYEFFAEVEEELDRIYDELVKVRTKIAKNLGFSNYVDYGYKLK
NRTDYNAEDVYKYRESVLKYVVPLTTELRKRQQKRLGIEKLRPWDESFVFPDGNPKPFGDVDFIVEKAKK
MYKELSLEFDEFFNFMLENNLLDLVARKGKAGGGYCTYLPKYKAPFIFSNFNGTSGDIDVLTHEAGHAFH
VYESRKFLIPEYRWPTYEAAELHSMSMELLTWPWMKLFYTDEEDAKKYKFSHLSGALSFLPYGVIVDHFQ
HWVYENPNHTPEERKEKYRNLEKKYLPSRVYEDNDELEIGTFWLRQGHIFSVPFYYIEYTIAQIGALQIW
KRYKEDPEEALEDYKKLCSAGGSQSFLELYETAGLTFPFSEECIKEIVSFVEKLLEEID
>gnl|CDD|274069 TIGR02290, oligoendopeptidase_F, oligoendopeptidase, pepF/M3 family. The M3 family of metallopeptidases contains several distinct clades. Oligoendopeptidase F as characterized in Lactococcus, the functionally equivalent oligoendopeptidase B of group B Streptococcus, and closely related sequences are described by TIGR00181. The present family is quite similar but forms a distinct clade, and a number of species have one member of each. A greater sequence difference separates members of TIGR02289, probable oligoendopeptidases of the M3 family that probably should not be designated PepF
EWDLSDLYPGGSSPEFEEDLKKIKALADEFESLYQEKLTPLDAKGKEKLQNALKRYEALGELLSKVGAYA
SLLYSADTSDPEAKALLGELEALSSEIQQALLFFTLELMRLSDEVWAALLSDPDLAPYRFYLKELRKEAP
HTLSEEEEKLINALSLTGRAAWSRLYDELTGTLRIPVDGKDGEEETLSLEQALNLLRDPDAEVRKKAFKA
LLKAWEKNAPTLAAILNALAGDRLTEYRLRGYDHPLEPRLLYNRIDQETLDAMLEAIKENYPLFRRYYKL
KAKLLGKEKLDFYDLYAPLGDSSAKTYTFDEAKELVLEAFGKFSPEMADFAEKAFEEGWIDAEPRPGKRG
GAFCTGFPPSKEPRVLMNYDGSRRDVSTLAHELGHAYHSELAKDQPLLNARYPMTLAETASIFAEMLLFD
ALLKEAKTDEEKLSLLAEKLEDAIATLVRIHARFLFERRFHEARKEGELSADDICDLMLEAQKESYGDAL
DESELHPYMWAYKPHFYHAPFYNYPYTFGYLFVLGLYAKYREEGESFVPKYIALLRDTGSMTPEELVKKF
GFDLTSPDFWQKGIDVIEEKIDEFEEL
>gnl|CDD|274070 TIGR02291, conserved_protein_of_unknown_function, alpha-L-glutamate ligase-related protein. Members of this protein family contain a region of homology to the RimK family of alpha-L-glutamate ligases (TIGR00768), various members of which modify the Glu-Glu C-terminus of ribosomal protein S6, or tetrahydromethanopterin, or a form of coenzyme F420 derivative. Members of this family are found so far in various Vibrio and Pseudomonas species and some other gamma and beta Proteobacteria. The function is unknown
YTTPSKLRHKGIMGMNKRNADYILRYNKRSLYPLVDDKLKTKIIAQAAGITVPELYGVIHNQAEVKTIHN
IVKDHPDFVIKPAQGSGGKGILVITSRKDGRYRKPSGATINKEEIERHVSNILAGLYSLGGKNDVALIEY
RVKFDPCFDGFSYEGVPDIRIIVFKGYPVMAMMRLPTRASDGKANLHQGAVGVGIDLATGKTIRAVWFNQ
PITHHPDTGKDLSGLQVPHWERLLELAASCWELTGLGYMGVDMVLDKEEGPLVLELNARPGLAIQIANGA
GLLPRLKHIEARLETPAEYPKAIERVAYAQELFGVKP
>gnl|CDD|274071 TIGR02292, Hypothetical_protein_yecA., yecA family protein. This family resembles pfam03695 (version pfam03695.3), uncharacterised protein family UPF0149, but is broader in scope and includes additional proteins. It includes E. coli proteins YgfB and YecA. The function of this family of proteins is unknown. The crystal structure is known for the member from Haemophilus influenzae (Ygfb, HI0817) [Unknown function, General]
LDRLSDFLDALELDGECMNLEELDGFLTALLSGPEVLKPQEWLPLVWGGENQAAFDSEEQATRIIDLIVQ
HYNQIAAQLSDGPEKFPPLLPLDEDDGEEDQRGDDWANGFLLGIDLRPDDWATLMDDEETAELVDPIMDL
GGLYDEEENM
>gnl|CDD|131346 TIGR02293, conserved_protein_of_unknown_function, putative toxin-antitoxin system antitoxin component, TIGR02293 family. Proteins in this family are found almost exclusively in the Proteobacteria, but also in Gloeobacter violaceus PCC 7421, a cyanobacterium. This family was proposed by Makarova, et al. (2009) to be the antitoxin component of a new class of type 2 toxin-antitoxin system, or addiction module [Cellular processes, Other]
GWRVLGLPASRGTGLISRIERGLPIGALDRLAHLLAIGKAEIFKATGIPKATLQRRKMAHQRLSSEESDR
LARVARVWKAAVDVFGGDAEARQWLFRPVPGLGNRRPIDLLLTEAGAEIVEDLLGRLEYGVYA
>gnl|CDD|274072 TIGR02294, Nickel-binding_periplasmic_protein, nickel ABC transporter, nickel/metallophore periplasmic binding protein. Members of this family are periplasmic nickel-binding proteins of nickel ABC transporters. Most appear to be lipoproteins. This protein was previously (circa 2003) thought to mediate binding to nickel through water molecules, but is now thought to involve a chelating organic molecule, perhaps butane-1,2,4-tricarboxylate, acting as a metallophore [Transport and binding proteins, Cations and iron carrying compounds]
EKKENKQLTYAWPVDIGPMNPHVYNPNQMFAQSMVYEPLVRYTADGKIEPWLAKSWTVSEDGKTYTFKLR
DDVKFSDGTPFDAEAVKKNFDAVLQNSQRHSWLELSNQLDNVKALDKYTFELVLKEAYYPALQELAMPRP
YRFLSPSDFKNDTTKDGVKKPIGTGPWMLGESKQDEYAVFVRNENYWGEKPKLKKVTVKVIPDAETRALA
FESGEVDLIFGNEGSIDLDTFAQLKDDGDYQTALSQPMNTRMLLLNTGKNATSDLAVRQAINHAVNKQSI
AKNILYGTEKPADTLFAKNVPYADIDLKPYKYDVKKANALLDEAGWKLGKGKDVREKDGKPLELELYYDK
TSALQKSLAEYLQAEWRKIGIKLSLIGEEEDKIAARRRDGDFDMMFNYTWGAPYDPHSFISAMRAKGHGD
ESAQSGLANKDEIDKSIGDALASTDETERQELYKNILTTLHDEAVYIPISYISMTVVYRKDLEKVSFAPS
QYELPFNEIQ
>gnl|CDD|213698 TIGR02295, Substrate_Complex_Of_Homoprotocatechuate, 3,4-dihydroxyphenylacetate 2,3-dioxygenase. This enzyme catalyzes the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. 4-hydroxyphenylacetate arises from the degradation of tyrosine. The substrate, 3,4-dihydroxyphenylacetate (homoprotocatechuate) arises from the action of a hydroxylase on 4-hydroxyphenylacetate. The aromatic ring is opened by this dioxygenase exo to the 3,4-diol resulting in 2-hydroxy-5-carboxymethylmuconate semialdehyde. The enzyme from Bacillus brevis contains manganese
NILRTGHVELRVTDLDKSREFYVDLLGFRETESDKEYIYLRGIEEFQHHSLVLTKAPSAALSYIGFRVSK
EEDLDKAADFFQKLGHPVRLVRDGGQPEALRVEDPFGYPIEFYFEMEKVERLLRRYHRHRGVSPVRLDHF
NVFVPDVQRALRFYKEELGFRVTEYTEDDEGNLAAAWLHRKGGVHDIALTNGNGPRLHHIAYWVHDPLNI
IKACDILASAGLSDSIERGPGRHGVSNAFFLYLRDPDGHRIELYTGDYLTGDPDWPPIRWTLDDPQRQTL
WGHPAPPSWFTEAS
>gnl|CDD|131349 TIGR02296, HpaC, 4-hydroxyphenylacetate 3-monooxygenase, reductase component. This model identifies the reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase. This enzyme catalyzes the first step (hydroxylation at the 3-position) in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. 4-hydroxyphenylacetate arises from the degradation of tyrosine. These reductases catalyze the reduction of free flavins by NADPH. The flavin is then utilized by the large subunit of the monooxygenase
FRDAMASLAAAVNIITTNGIAGKCGITATAVCSVTDTPPTVMVCINRNSAMNPIFQENGKLCINVLAHEQ
QEMAEHFAGMTGLAMEERFAWHIWHEGPDGQPVLKGALAHLEGHIVDKHEIGTHTVFLVELKEIKVNGKR
HALVYFRRQFKFVD
>gnl|CDD|131350 TIGR02297, AraC-type_DNA-binding_domain-containing_protein, 4-hydroxyphenylacetate catabolism regulatory protein HpaA. This putative transcriptional regulator, which contains both the substrate-binding, dimerization domain (pfam02311) and the helix-turn-helix DNA-binding domain (pfam00165) of the AraC famil, is located proximal to genes of the 4-hydroxyphenylacetate catabolism pathway
EIPNIDIGKVYDGRYADSDVHYETFDNLALFFGRNMPVHFHDRYYQLHYLTEGSIALQLDEHEYSEYAPC
FFLTPPSVPHGFVTDLDADGHVLTVRQELVWQLLESLKGDIGDAFYPMCIELSPQEEAEQIAKLEYLFEL
LASEYRQHTDGRQTALQALAQLILIELLRLSKSNEKSTSPRNNELYLFNRFNFLIEENYKQHLRLPEYAD
RLGISESRLNDICRRFSALSPKRLIIERVMQEARRLLLFTQHSINQIAYDLGYKDPAYFARFFQKETGLS
PSAFRDR
>gnl|CDD|131351 TIGR02298, putative_34-dihydroxyphenylacetate_23-dioxygenase, 3,4-dihydroxyphenylacetate 2,3-dioxygenase. This enzyme catalyzes the ring-opening step in the degradation of 4-hydroxyphenylacetate
MGKLALAAKITHVPSMYLSELPGPLRGCRQGAIDGHKEISRRAKEMGVDTIVVFDTHWLVNSGYHINCND
QFSGSYTSHELPHFIQDLRYDYPGNPALGQLIADEAQEHGVKTLAHQVPSLGLEYGTLVPMRYMNEDGHF
KVVSIAAWCTVHDIEESRALGEAIRKAIEQSDGRVAVLASGSLSHRFWDNKDLAPEGMTTIASEFNRQVD
LRVLELWRERDYREFCAMLPDYAVKCNGEGGMHDTVMLFGALGWDDYDGEVEVITEYFPSSGTGQVNVVF
PV
>gnl|CDD|131352 TIGR02299, NAD-dependent_succinate_aldehyde_dehydrogenases, 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase. This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring
IGHFIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKRWAELKAAERKRYLHKIA
DLIEQHADEIAVLECLDCGQPLRQTRQQVIRAAENFRFFADKCEEAMDGRTYPVDTHLNYTVRVPVGPVG
LITPWNAPFMLSTWKIAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALV
AHPDVKAVSFTGETATGSIIMRNGADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTA
SSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPETEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERA
PTFRGEDLGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFKDEEEAIEKANDTRYGLAGYVWTNDVG
RAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNVALALGPHHIPKFGK
>gnl|CDD|131353 TIGR02300, Hypothetical_protein_SMc00332, TIGR02300 family protein. Members of this family are bacterial proteins with a conserved motif [KR]FYDLN, sometimes flanked by a pair of CXXC motifs, followed by a long region of low complexity sequence in which roughly half the residues are Asp and Glu, including multiple runs of five or more acidic residues. The function of members of this family is unknown
MAKPDLGTKRICPNTGSKFYDLNRRPAVSPYTGEQFPPEEALKSRRVRADDEKEAVAVKEVDPEIDEAAE
LVSLEEADEEVDPGAPTPAGGDDLAEDEDIADDDDDVTFLEDEEDDDIDDEDIIGVSGE
>gnl|CDD|131354 TIGR02301, Conserved_hypothetical_signal_peptide_protein, TIGR02301 family protein. Members of this uncharacterized protein family are found in a number of alphaProteobacteria, including root nodule bacteria, Brucella suis, Caulobacter crescentus, and Rhodopseudomonas palustris. Conserved residues include two well-separated cysteines, suggesting a disulfide bond. The function is unknown
RPFLAQPCLAALIAAPVPAAERAPAPYDQRLLRLAEILGSLHYLRNLCGSKGDDYWRSRMQALIDAETAD
EERRARMTAAFNRGYRSFASTYTRCTPAATKAEERYRKEGATLAREIASRY
>gnl|CDD|274073 TIGR02302, conserved_hypothetical_protein, TIGR02302 family protein. Members of this family are long (~850 residue) bacterial proteins from the alpha Proteobacteria. Each has 2-3 predicted transmembrane helices near the N-terminus and a long C-terminal region that includes stretches of Gln/Gly-rich low complexity sequence, predicted by TMHMM to be outside the membrane. In Bradyrhizobium japonicum, two tandem reading frames are together homologous the single members found in other species; the cutoffs scores are set low enough that the longer scores above the trusted cutoff and the shorter above the noise cutoff for this model
LDRAIGRATLAIAWERLWPHLLRVMSLVGLFLSLGWAGLFLALPFWLHIAGLVLFAALALVALIPAIRFR
WPSRDEALARLERNNGLKHRPATVQGDALATGDPFARALWREHQDRMAATIRGLKPGLPRPRLPIHDPWG
LRALVVLLLVAAFAYSGEERSGRIMDAFDWKPAMSPSTARIDAWVTPPVYTGRAPIFLTAASNKDLGTPG
SGPITVPQGSTLLVRSSGGDEETVLDIAAGGGVVEIKPDDAKAETAKPETPRSDAPKGTRNRHYRITKDG
TLRVAGSSAPWSFTATPDKPPAIAFAKEPQRQANGSLQLSYKLEDDYGVAEAEAEIVALPPAKAPGAKPL
YEAPQFKLVLPRRRTRVGVGQTSKDLSEHPYAGAEVTLTLVAKDAAGNQGHSEPFTIRLPERLFTKPLAR
AVAEQRRILALDANQNSQVYDALDALLLAPEETIPNAGHYLGLYTIRTRLERARTDDALRDVADNLWSLA
LGIEDGDLSDAERRLRAAQDALKDALERGASDEEIKQLTDKLRAAMQTYMRQLAQQLRNNPQQLARPLDP
NTKVLRQQDLQNMMDQIENLARSGDRDQAKQLLSQLQQMMNNLQMGQPGQGQQMGDQSGDMEQQMNKLGE
LMRKQQQLRDETFKLDQDQRRDRMRGQDGEQNFGDDMPQQDGQPNGQPNLHDRLRKLQQEEAKRGLGQSQ
GGLKGELGQLGQGLQNLGIQPGKGFDQADSAMGDAEGALGDGNGDGAVDSQGRALEALRQGAQDMMEAMQ
QGDGDGQGDGQGRQQSGANGRDPLGRPLRGRGLGFGLTVKIPGEIDVQRARRILEEIRRKLGDSLRPQIE
LDYLERLLKDY
>gnl|CDD|131356 TIGR02303, decarboxylase_divided_with_OB2865, 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit. This model represents one of two subunits/domains of the bifunctional isomerase/decarboxylase involved in 4-hydroxyphenylacetate degradation. In E. coli and some other species this enzyme is encoded by a single polypeptide containing both this domain and the closely related N-terminal domain (TIGR02305). In other species such as Pasteurella multocida these domains are found as two separate proteins (usually as tandem genes). Together, these domains carry out the decarboxylation of 5-oxopent-3-ene-1,2,5-tricarboxylic acid (OPET) to 2-hydroxy-2,4-diene-1,7-dioate (HHDD) and the subsequent isomerization to 2-oxohept-3-ene-1,7-dioate (OHED)
KLARILYKGRVHSVVYREGGLLTEDGRALPPEQVTWLPPFEPGTIFALGLNYADHASELGFSPPEEPLVF
LKGNNTLTGHKGVTYRPKDVRFMHYECELAVVVGKTAKNVKREDAMDYVLGYTIANDYAIRDYLENYYRP
NLRVKNRDTFTPIGPWIVDKEDVEDPMNLWLRTYVNGELTQEGNTSDMIFSVAELIEYLSEFMTLEPGDV
ILTGTPKGLSDVKPGDVVRLEIEGVGALENPIVSE
>gnl|CDD|274074 TIGR02304, conserved_hypothetical_protein, putative adenylate-forming enzyme. Members of this family form a distinct clade within a larger family of proteins that also includes coenzyme F390 synthetase, an enzyme known in Methanobacterium thermoautotrophicum and a few other methanogenic archaea. That enzyme adenylates coenzyme F420 to F390, a reversible process, during oxygen stress. Other informative homologies include domains of the non-ribosomal peptide synthetases involved in activation by adenylation. The family defined by this model is likely to be of an adenylate-forming enzyme related to but distinct from coenzyme F390 synthetase
IPLAILWRYFKTRYGLHFTDREALENWQAKQLEKFLQFVLSHSPWFQRYHTIPFNQWPMMDKALMMEHFD
ELNTAGLKKDEALDCAMRSEKTRDFKPCVGNISVGLSSGTSGRRGLFVVSPEEQQMWAGGILAKVLPDGL
FAKHRIAFFLRADNNLYQSVNNRWISLDFFDLLAPFQAHIKRLNQRKPSIIVAPPSVLRALALEVMEGEL
TIKPKKVISVAEVLEPQDRELIRNVFKNTVHQIYQATEGFLASTCRCGTLHLNEDLVHIEKQYLDEHKRF
VPIITDFTRTTQPIVRYRLNDILVESEQPCSCGSATMAIERIEGRQDDIFQLITRSGDEQTVFPDFIRRV
ILFTLPLIVEYRVLQTGSAQLELIADCELEMLEHCRSKALNALFTRQDIAVGQIIWSLFPQYVIVSFTKK
LKRIVRQVGR
>gnl|CDD|131358 TIGR02305, HpaG-N-term, 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit. This model represents one of two subunits/domains of the bifunctional isomerase/decarboxylase involved in 4-hydroxyphenylacetate degradation. In E. coli and some other species this enzyme is encoded by a single polypeptide containing both this domain and the closely related C-terminal domain (TIGR02303). In other species such as Pasteurella multocida these domains are found as two separate proteins (usually as tandem genes). Together, these domains carry out the decarboxylation of 5-oxopent-3-ene-1,2,5-tricarboxylic acid (OPET) to 2-hydroxy-2,4-diene-1,7-dioate (HHDD) and the subsequent isomerization to 2-oxohept-3-ene-1,7-dioate (OHED)
GTVFGVALNYREQLDRLQEAFQQAPYKAPPKTPVLYIKPRNTHNGCGQPIPLPAGVEKLRSGATLALVVG
RTACRVREEEALDYVAGYALVNDVSLPEDSYYRPAIKAKCRDGFCPIGPEVPLSAIGNPDELTIYTYING
KPAQSNNTSNLVRSAAQLISELSEFMTLNPGDVLLLGTPEARVEVGPGDRVRVEAEGLGELENPV
>gnl|CDD|274075 TIGR02306, hypothetical_protein_44RRORF209c, RNA ligase, DRB0094 family. The member of this family from Deinococcus radiodurans, a species that withstands and recovers from extensive radiation or dessication damage, is an apparent RNA ligase. It repairs RNA stand breaks in nicked DNA:RNA and RNA:RNA but not DNA:DNA duplexes. It has adenylyltransferase activity associated with the C-terminal domain. Related proteins also in this family are found in Streptomyces avermitilis MA-4680 and in bacteriophage 44RR2.8t. The phage example is unsurprising since one mechanism of host cell defense against phage is cleavage and inactivation of certain tRNA molecules. A fungal sequence from Neurospora crassa scores between trusted and noise cutofffs and may be similar in function
QLAVMREIADLQPHPNADALELATVGGWEVVVKKGEYRVGSDCVYFPEDSVLPTDAGLFRFLETRAKILD
GKMRARVKTVRLRGEISQGIALPTGALTDGELLGGQEMDKDIAEMLGITKWEPPQPGTMCGEGETFPIFI
PKTDEERCQNYFNRFKEGEKVAKTEKLHGTSITVAWVTDEERFLVLSKGVASRNLVLRENADNKYWKAVE
NYQIVDRAKAAELRMSVAIFGEVMGPGIQKNRYGFDKYRTVFAFRAFFDGEQRFLTDEDFQDLCLTLIVP
QLYEGPFDEFTVVKDMLGAETVSGIGLHIREGVVYKSVELRFAVDGRMVHFKAISNAYLLK
>gnl|CDD|274076 TIGR02307, RNA-editing_ligase_2_mitochondrial, RNA ligase, Rnl2 family. Members of this family ligate (seal breaks in) RNA. Members so far include phage proteins that can counteract a host defense of cleavage of specific tRNA molecules, trypanosome ligases involved in RNA editing, but no prokaryotic host proteins  [Mobile and extrachromosomal element functions, Prophage functions, Transcription, RNA processing]
FKKYTSLENHYRRIFAEKLYGLGLTEWVAREKIHGTNFSIIIERDFKVTCAKRTGIILPNEDFFGYHILI
KNYTASVKAIQDILETKAIIVVVSVQVFGELAGPGYQKPVVYSDKDFYAFDIKYTETSDDVTLVDDYMME
SFCNVPKLKYAPLLGRGTLDELLAFDVENFTTDHPALVDAGNYPLEGNTAEGYVVKHCRPGKWLRNGNRT
IIKCKNSKFSEKKNKAGKPILAKVVLSEAQNKLVALLLCYVTENRLNNVLSKIGTEPPKDFGMVMGLLAQ
DALKEFLRETPGITNTQADNRKLIKRSLVFMAQELLRPAWKDILD
>gnl|CDD|213699 TIGR02308, T4_RNA_ligase_1, RNA ligase, T4 RnlA family. Members of this family are phage proteins with ATP-dependent RNA ligase activity. Host defense to phage may include cleavage and inactivation of specific tRNA molecules; members of this family act to reverse this RNA damage. The enzyme is adenylated, transiently, on a Lys residue in a motif KXDGSL [Mobile and extrachromosomal element functions, Prophage functions, Transcription, RNA processing]
QELFNNLMNLCKDSQRKFFYKDDVTAMGTKYRIFSYNYASYSDWLLPDALECRGIMFEIDGEKPVRIASR
PMEKFFNLNENPFTMNIDLNDVDYVMDKEDGSLVSTYLDGGYILLKSKASIKSEQANRANGLLYSENHHD
LRERIADLAEDGFTFNFEYVAPSNRIVLAYQEPKLILLNVRHNETGEYVSYDDLYKDATLRPYLVERYEV
DSPRKWIDEVRNAEGIEGYVAVMKDGQMFKLKSDWYVALHSTKDSINNPEKLIYTIIEGATDDLRAMYAD
DEYSLRKIEAFEETYRSYLDRALFLVTECYNKHCGKDRKTYAIEAQGVAKGHGHRHLFGIIMSLYAGYDD
QEKVMDEIEQNFLKNYKKFIPAGY
>gnl|CDD|131362 TIGR02309, 4-hydroxyphenylacetate_3-monooxygenase, 4-hydroxyphenylacetate 3-monooxygenase, oxygenase component. This gene for this monooxygenase is found within apparent operons for the degradation of 4-hydroxyphenylacetic acid in Deinococcus, Thermus and Oceanobacillus. Phylogenetic trees support inclusion of the Bacillus halodurans sequence above trusted although the complete 4-hydroxyphenylacetic acid degradation pathway may not exist in that organism. Generally, this enzyme acts with the assistance of a small flavin reductase domain protein (HpaC) to provide the cycle the flavin reductant for the reaction. This family of sequences is a member of a larger subfamily of monooxygenases (pfam03241)
ARTGQEYIDALKTRPPNLYIKGERVEDPTTHPVFRGIVQSMAALYDLQHDPRYKEVLTYEEEGKRHGMSF
MIPKTKEDLKRRGEAYKLWADQNLGMMGRSPDYLNAVVMAYAASADYFGKSNSEFAENVRNYYEYLRDND
LALTHALTNPQVNRAKPPSEQPDPYIALGVVEQTDKGVIVRGARMTATFPIADEILIFPSTVLKAGAEKD
PYALAFAIPTNTPGLHFVCREALDGGDSPFDHPLSSRFEEMDALVIFDDVLVPWERIFILGDVELCNNAY
AATGAVNHMAHQVVALKIAKTEAFLGVAALMAEGIGADGFQHVQEKIAEIIVYLEAMKAFWTRAEEEAKE
NAYGLMTPDRGALDAARNLYPRLYPRLREILEQLGASGLITLPSEKDFKGPLGPFLEKFLQGANLEAKER
VALFRLAWDMTMSSFGARQELYERYFFGDPVRMYQALYNVYDKEPYKARIREFLKES
>gnl|CDD|213700 TIGR02310, HpaB-2, 4-hydroxyphenylacetate 3-monooxygenase, oxygenase component. This gene for this monooxygenase is found within apparent operons for the degradation of 4-hydroxyphenylacetic acid in Shigella, Photorhabdus and Pasteurella. The family represented by this model is narrowly limited to gammaproteobacteria to exclude other aromatic hydroxylases involved in various secondary metabolic pathways. Generally, this enzyme acts with the assistance of a small flavin reductase domain protein (HpaC) to provide the cycle the flavin reductant for the reaction. This family of sequences is a member of a larger subfamily of monooxygenases (pfam03241)
KPEDFRAEKNRPFTGEEYLASLRDGREIYIYGERVKDVTTHPAFRNAAASVAKLYDALHDPATKDELCWE
TDTGNGGYTHKFFRYARSADELRQQRDAIAEWSRLSYGWMGRTPDYKAAFGSALGANPGFYGKFEDNARN
WYKRIQESCLYFNHAIVNPPIDRNKPIDQVKDVYIKIEEERDDGIVVSGAKVVATNSALTHYNFIGFGSA
QIIGDNDDFALMFIAPMDAEGVKLICRHSYELVAGATGSPFDYPLSSRFDENDAILVMDSVFIPWENVLI
YRDFERCRTWAQYGGFARLFPMQACTRLAVKLDFITGLLHKALQCTGVLEFRGVQAQMGEVVAWRNLFWT
LTDAMAGSAYQWKNGAQLPSAQALQTYRVMAPMAYHTIKKIIEQTVTSGLIYLPSHIRDLNNPQIDQYLE
KYVRGSNGMEHRERIKILKLLWDAIGSEFGGRHELYEINYAGSQDEIRLQVLRQATGSGTMQRMFDMVDK
CLADYDENGWTVPHLHNSEDINILDNLNR
>gnl|CDD|131364 TIGR02311, 24-dihydroxyhept-2-ene-17-dioic_acid_aldolase, 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase. This model represents the aldolase which performs the final step unique to the 4-hydroxyphenylacetic acid catabolism pathway in which 2,4-dihydroxyhept-2-ene-1,7-dioic acid is split into pyruvate and succinate-semialdehyde. The gene for enzyme is generally found adjacent to other genes for this pathway organized into an operon
NQFKQALKEGQPQIGLWLGLADPYAAEICAGAGFDWLLIDGEHAPNDVRTILSQLQALAPYPSSPVVRPA
IGDPVLIKQLLDIGAQTLLVPMIETAEQAEAAVAATRYPPMGIRGVGSALARASRWNRIPDYLQQADEEI
CVLLQVETREALDNLEEIAAVEGVDGVFIGPADLAASMGHLGNPSHPEVQAAIDDAIERIKAAGKAAGIL
TADPKLARQYLKLGALFVAVGVDTTLLARGAEALAARFK
>gnl|CDD|131365 TIGR02312, 2-keto-4-pentenoate_hydratase, 2-oxo-hepta-3-ene-1,7-dioic acid hydratase. This model represents the enzyme which hydrates the double bond of 2-oxo-hepta-3-ene-1,7-dioic acid to form 4-hydroxy-2-oxo-heptane-1,7-dioic acid in the catabolism of 4-hydroxyphenylacetic acid. The gene for this enzyme is generally found adjacent to other genes of this pathway in an apparent operon
MLTDALIQEAAAELYEAEKTRVQISQFSLRYPEITIEDAYRIQRAWVAMKIAEGRRVIGHKIGLTSRAMQ
QASNIDEPDYGVLLDDMFFEDGSTIPADRFIQPRVEVELAFVLKKDLEGPNVTIFDVLNATDYVVPALEI
IDARIERVDPETGATRKVFDTISDNAANAGIVLGGRPVRPDALDLRWVGAILYRNGVVEETGLAAGVLNH
PANGVAWLANKLAPWGETLEAGQVVLAGSFTRPVAARSGDTFHADYGPLGTISVRFV
>gnl|CDD|131366 TIGR02313, dihydrodipicolinate_synthase, 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase. This model represents a subset of the DapA (dihydrodipicolinate synthase) family which has apparently evolved a separate function. The product of DapA, dihydrodipicolinate, results from the non-enzymatic cyclization and dehydration of 6-amino-2,4-dihydroxyhept-2-ene-1,7-dioic acid, which is different from the substrate of this reaction only in the presence of the amino group. In the absence of this amino group, and running the reaction in the opposite direction, the reaction corresponds to the HpaI aldolase component of the 4-hydroxyphenylacetic acid catabolism pathway (see TIGR02311). At present, this variant of DapA is found only in Oceanobacillus iheyensis HTE831 and Thermus thermophilus HB27. In both of these cases, one or more other DapA genes can be found and the one identified by this model is part of an operon for 4-hydroxyphenylacetic acid catabolism
FRGSIAPLITPFKRNGDIDEEALRELIEFQIEGGSHAISVGGTSGEPGSLTLEERKQAIENAIDQIAGRI
PFAPGTGALNHDETLELTKFAEEAGADAAMVIVPYYNKPNQEALYDHFAEVADAVPDFPIIIYNIPGRAA
QEIAPKTMARLRKDCPNIVGAKESNKDFEHLNHLFLEAGRDFLLFCGIELLCLPMLAIGAAGSIAATANV
EPKEVAELCEAAEAGDIKGAQDLHFELLEANDAIFKDTNPAPLKAALGMMGLIEKELRPPLGLPSDALEE
EIRDMAEKYGKIEK
>gnl|CDD|131367 TIGR02314, Methionine_import_ATP-binding_protein_MetN, D-methionine ABC transporter, ATP-binding protein. Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria
MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLT
TLSNSELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSN
LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDC
VAVISNGELIEQGTVSEIFSHPKTPLAQKFIRSTLHLSIPEDYQERLQATPFADSVPMVRLEFTGQTVDA
PLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGTQQDTQAAIAYLQEHNVKVEVLGYV
>gnl|CDD|131368 TIGR02315, Phosphonates_import_ATP-binding_protein_PhnC, phosphonate ABC transporter, ATP-binding protein. Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates [Transport and binding proteins, Anions]
MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLR
GKKLRKLRRRIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAY
QRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAK
KYADRIVGLKAGEIVFDGAPSELDDEVLRHIYG
>gnl|CDD|131369 TIGR02316, Propionate--CoA_ligase, propionate--CoA ligase. This family contains one of three readily separable clades of proteins in the group of acetate and propionate--CoA ligases. Characterized members of this family act on propionate. From propionyl-CoA, there is a cyclic degradation pathway: it is ligated by PrpC to the TCA cycle intermediate oxaloacetate, acted upon further by PrpD and an aconitase, then cleaved by PrpB to pyruvate and the TCA cycle intermediate succinate
MRYEEFYQRSIEQPEAFWAEQARRIDWQTPPQRILDYSNPPFARWFAGGRTNLCHNALDRHLDERGEQLA
LVTVSSETGQERTLTYRQLHREVNVFASALRALGVGRGDRVLIYMPMIAEAVFAMLACARIGAIHSVVFG
GFASHSLALRIDDATPKLIVSADAGMRGGKVIPYKPLLDAAIAEAQHPPPHVLLVDRGLAPMRLIPGRDV
DYAALRTQHEDAQVPVEWLESNEPSYILYTSGTTGKPKGVQRDVGGYAVALALSMWAIFGIRAGQVMFSA
SDVGWVVGHSYIVYAPLLAGAATVLYEGLPTNPDPGVWWSIVERYGVRTMFSAPTAIRVLKKQDAAWLRK
HDLSSLHWLFLAGEPLDEPTAHWITDGLGKPVIDNYWQTETGWPVLAIMPGLDLKPVKLGSPGLPMYGYH
LRVLDEATGRPCGPNEKGVLTVVPPLPPGCLSTVWGDDARFLKTYWSHFKRPLYSSFDWGIRDEDGYTFI
LGRTDDVINVAGHRLGTREIEESVSSHPSVAEVAVVGVHDELKGQVAVVFAILKESDSAGDAHDPHAVET
GMMDCVVRQLGAVARPARVYFVAALPKTRSGKLLRRSIQALAEGRDPGDLTTIDDPGALEQVRRAMER
>gnl|CDD|131370 TIGR02317, Methylisocitrate_lyase, methylisocitrate lyase. Members of this family are methylisocitrate lyase, also called (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase. This enzyme acts in propionate metabolism. It cleaves a carbon-carbon bond to convert 2-methylisocitrate to pyruvate plus succinate. Some members of this family have been annotated, incorrectly it seems, as the related protein carboxyphosphoenolpyruvate phosphomutase, which is involved in synthesizing the antibiotic bialaphos in Streptomyces hygroscopicus
PGKAFRAALAKEDILQIPGAINAMAALLAERAGFEAIYLSGAAVAASLGLPDLGITTLDEVAEDARRITR
VTDLPLLVDADTGFGEAFNVARTVREMEDAGAAAVHIEDQVLPKRCGHLPGKELVSREEMVDKIAAAVDA
KRDEDFVIIARTDARAVEGLDAAIERAKAYVEAGADMIFPEALTSLEEFRQFAKAVKVPLLANMTEFGKT
PLFTADELREAGYKMVIYPVTAFRAMNKAAEAVYNEIKEHGTQKGSLDDMQTRKELYELIGYYDYEKKDD
SIFKR
>gnl|CDD|131371 TIGR02318, phosphono_phnM, phosphonate metabolism protein PhnM. This family consists of proteins from in the PhnM family. PhnM is a a protein associated with phosphonate utilization in a number of bacterial species. In Pseudomonas stutzeri WM88, a protein that is part of a system for the oxidation of phosphites (another form of reduced phosphorous compound) scores between trusted and noise cutoffs [Energy metabolism, Other]
VLSNARLVLEDEVVEGSVVIEDGAIADIGEGPVALAEAIDGEGDLLLPGLIDLHTDNLERHMSPRPGVDW
PIDAAIVEHDKQLAAAGITTVFDALALGDTESGGRRPDNLRRMIDAISEARDRGLLRADHRLHLRCELPN
EEVLPELEELIDDPRVDLISLMDHTPGQRQFRDLEKYREYYRGKRGLSDDEFDEIVEERIARRAEYGLAN
RSEIAALARARGIPLASHDDDTPEHVAEAHDLGVTISEFPTTLEAAKEARSLGMQILMGAPNIVRGGSHS
GNLSARELAHEGLLDVLASDYVPASLLLAAFQLADDVEGIPLPQAVKMVTKNPARAVGLSDRGSIAPGKR
ADLVRVHRVDGVPRIRAVWRAGRRVY
>gnl|CDD|131372 TIGR02319, Carboxyvinyl-carboxyphosphonate_phosphorylmutase, carboxyvinyl-carboxyphosphonate phosphorylmutase. This family consists of carboxyvinyl-carboxyphosphonate phosphorylmutase (CPEP phosphonomutase), an unusual enzyme involved in the biosynthesis of the antibiotic bialaphos. So far, it is known only in that pathway and only in Streptomyces hygroscopicus. Some related proteins annotated as being functionally equivalent are likely misannotated examples of methylisocitrate lyase, an enzyme of priopionate utilization
AVTKARTFRELMNAPEILVVPSAYDALSAKVIQQAGFPAVHMTGSGTSASMLGLPDLGFTSVSEQAINAK
NIVLAVDVPVIMDADAGYGNAMSVWRATREFERVGIVGYHLEDQVNPKRCGHLEGKRLISTEEMTGKIEA
AVEAREDEDFTIIARTDARESFGLDEAIRRSREYVAAGADCIFLEAMLDVEEMKRVRDEIDAPLLANMVE
GGKTPWLTTKELESIGYNLAIYPLSGWMAAASVLRKLFTELREAGTTQKFWDDMGLKMSFAELFEVFEYS
KISELEARFVRDQD
>gnl|CDD|274077 TIGR02320, Phosphoenolpyruvate_phosphomutase, phosphoenolpyruvate mutase. This family consists of examples of phosphoenolpyruvate phosphomutase, an enzyme that creates a C-P bond as the first step in the biosynthesis of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for phosphonopyruvate decarboxylase (aepY). Since the PEP phosphomutase reaction favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP). A closely related enzyme, phosphonopyruvate hydrolase from Variovorax sp. Pal2, is excluded from this model
LRQLLHSKPLERLMEAHNGLSALIAEEARVEVGDSLGFDGIWSSSLTDSTSRGVPDIEEASWTQRLDVVE
FMFDVTTKPIILDGDTGGNFEHFRRLVRKLERRGVSAVCIEDKLGLKKNSLFGNDVAQPQASVEEFCGKI
RAGKDAQTTEDFMIIARVESLILGKGMEDALKRAEAYAEAGADGIMIHSRKKDPDEILEFARRFRNHYPR
TPLVIVPTSYYTTPTDEFRDAGISVVIYANHLLRAAYAAMQQVAERILEHGRLVEVEDKCAPIKEIFRLI
PGTE
>gnl|CDD|131374 TIGR02321, phosphoenolpyruvate_phosphomutase, phosphonopyruvate hydrolase. This family consists of phosphonopyruvate hydrolase, an enzyme closely related to phosphoenolpyruvate phosphomutase. It cleaves the direct C-P bond of phosphonopyruvate. The characterized example is from Variovorax sp. Pal2
MTKNQALRAALDSGRLFTAMAAHNPLVAKLAEQAGFGGIWGSGFELSASYAVPDANILSMSTHLEMMRAI
ASTVSIPLIADIDTGFGNAVNVHYVVPQYEAAGASAIVMEDKTFPKDTSLRTDGRQELVRIEEFQGKIAA
ATAARADRDFVVIARVEALIAGLGQQEAVRRGQAYEEAGADAILIHSRQKTPDEILAFVKSWPGKVPLVL
VPTAYPQLTEADIAALSKVGIVIYGNHAIRAAVGAVREVFARIRRDGGIREVDAALPSVKEIIELQGDER
MRAVEARYLK
>gnl|CDD|274078 TIGR02322, Ribose_15-bisphosphate_phosphokinase_PhnN, phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN. Members of this family resemble PhnN of phosphonate utilization operons, where different such operons confer the ability to use somewhat different profiles of C-P bond-containing compounds (see), including phosphites as well as phosphonates. PhnN in E. coli shows considerable homology to guanylate kinases (EC 2.7.4.8), and has actually been shown to act as a ribose 1,5-bisphosphokinase (PRPP forming). This suggests an analogous kinase reaction for phosphonate metabolism, converting 5-phosphoalpha-1-(methylphosphono)ribose to methylphosphono-PRPP [Central intermediary metabolism, Phosphorus compounds]
GRLIYVVGPSGAGKDTLLDYARARLAGDPRVHFVRRVITRPASAGGENHIALSTEEFDHREDGGAFALSW
QAHGLSYGIPIEIDQWLEAGDVVVVNGSRAVLPEARQRYPNLLVVNITASPDVLAQRLAARGRESREEIE
ERLARSARFAAAPADVTTIDNSGSLEVAGETLLRLLRKE
>gnl|CDD|188208 TIGR02323, phosphonates_transport_ATP-binding_protein_phnK, phosphonate C-P lyase system protein PhnK. Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se [Central intermediary metabolism, Phosphorus compounds]
KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAEL
ELYQLSEAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPT
RIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLG
VARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSIL
>gnl|CDD|131377 TIGR02324, phosphonate_uptake_transporter_ATP-binding_protein, phosphonate C-P lyase system protein PhnL. Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se
LLEVEDLSKTFTLHQQGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHE
GAWVDLAQASPREVLEVRRKTIGYVSQFLRVIPRVSALEVVAEPLLERGVPREAARARARELLARLNIPE
RLWHLPPATFSGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKARGAALIGIFHDEE
VRELVADRVMDVTP
>gnl|CDD|131378 TIGR02325, Probable_transcriptional_regulator_PhnF, phosphonates metabolism transcriptional regulator PhnF. All members of the seed alignment for this family are predicted helix-turn-helix transcriptional regulatory proteins of the broader gntR and are found associated with genes for the import and degradation of phosphonates and/or related compounds (e.g. phosphonites) with a direct C-P bond [Transport and binding proteins, Anions, Regulatory functions, DNA interactions]
IERTSGVALWRQIADKIEQEIAAGHLRAGDYLPAEMQLAERFGVNRHTVRRAIAALVERGLLRAEQGRGT
FVAARRIDYPLSARTRFSQNLADQGREPTGELLLSDLEPASAELADALGLTVGAPLVRLETLRKADGRPL
CRATTWFPAARFPGIGQAYAASGSITDALREQGVADYRRSSTRISARHADAKDCARLELPPGRPLLVVQA
LNHDGEGRPVQYSVSRFRADRVEFTMEN
>gnl|CDD|131379 TIGR02326, 2-aminoethylphosphonate--pyruvate_aminotransferase, 2-aminoethylphosphonate--pyruvate transaminase. Members of this family are 2-aminoethylphosphonate--pyruvate transaminase. This enzyme acts on the most common type of naturally occurring phosphonate. It interconverts 2-aminoethylphosphonate plus pyruvate with 2-phosphonoacetaldehyde plus alanine. The enzyme phosphonoacetaldehyde hydrolase (EC 3.11.1.1), usually encoded by an adjacent gene, then cleaves the C-P bond of phosphonoacetaldehyde, adding water to yield acetaldehyde plus inorganic phosphate. Species with this pathway generally have an identified phosphonate ABC transporter but do not also have the multisubunit C-P lysase complex as found in Escherichia coli [Central intermediary metabolism, Phosphorus compounds]
ERNYLLLTPGPLTTSRTVKEAMLFDWCTWDSDYNIVVEQIRQQLLALATAEEGYTSVLLQGSGTFAVEAV
IGSAVPKDGKLLVVINGAYGARIVQIAEYLGIPHHVVDTGEVEPPDVVEVEAILAADPAITHIALVHCET
TTGILNPIEAVAKLAHRHGKVTIVDAMSSFGGIPIDIAELHIDYLISSANKCIQGVPGFGFVIARQAELA
ACKGNARSLSLDLYDQWRCMEDNHGKWRFTSPTHVVHAFAQALLELEKEGGVAARHQRYQQNQKTLVAGM
RALGFEPLLDDEIQSPIITSFYSPEDPDYRFADFYQRLKEQGFVIYPGKVSQVDCFRIGNIGEVDAADIT
RLLTAIGKAMYWT
>gnl|CDD|131380 TIGR02327, conserved_hypothetical_protein, conserved hypothetical integral membrane protein. Members of this protein family are small, typically about 80 residues in length, and are highly hydrophobic. The gene is found so far only in a subset of the Firmicutes in association with genes of the ATP synthase F1 complex or NADH-quinone oxidoreductase. This family includes ywzB from Bacillus subtilis; pfam06612 describes the same family as Protein of unknown function DUF1146
IVAIVSHLLFIGISYWALQVIDWEKFIKPQNVGQLRVLVVLIAIALGYTVSHFFLELIQLSQSLFFEF
>gnl|CDD|131381 TIGR02328, TIGR02328, conserved hypothetical protein. Members of this protein are found in a small number of taxonomically well separated species, yet are strongly conserved, suggesting lateral gene transfer. Members are found in Treponema denticola, Clostridium acetobutylicum, and several of the Firmicutes. The function of this protein is unknown [Hypothetical proteins, Conserved]
MRLWHQSLITKLPRQQLLGQHRECCALRGNGWGKKHSTVDYVFCYSPYKLFAYHLLVMEEMATRGYHVSK
QWLDPNYRGQNCPNYDLLEEIKLTTPIYPEHNDDYLNECLANLRAKGIIL
>gnl|CDD|274079 TIGR02329, Propionate_catabolism_operon_regulatory_protein, propionate catabolism operon regulatory protein PrpR. At least five distinct pathways exists for the catabolism of propionate by way of propionyl-CoA. Members of this family represent the transcriptional regulatory protein PrpR, whose gene is found in most cases divergently transcribed from an operon for the methylcitric acid cycle of propionate catabolism. 2-methylcitric acid, a catabolite by this pathway, is a coactivator of PrpR [Regulatory functions, DNA interactions]
NADKPVIWTVSVSRLFDLFRDIAPEFDHRANITPIQLGFEDAVREIRQRLGAERCDVVVAGGSNGAYLKS
RLSLPVIVIKPTGFDVMQALARARRIASSIGVVTHQDTPPALRRFQAAFNLDIVQRSYVTEEDARSCVND
LRARGIGAVVGAGLITDLAEQAGLHGVFLYSADSVRQAFDDALDVARATRLRQAATLRSATRNQLRTRYR
LDDLLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLE
AELFGYEEGAFTGARRGGRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVR
VVAATHCALTTAVQQGRFRRDLFYRLSILRIALPPLRERPGDILPLAAEYLVQAAAALRLPDSEAAAQVL
AGVADPLQRYPWPGNVRELRNLVERLALELSAMPAGALTPDVLRALAPELAEASGKGKTSALSLRERSRV
EALAVRAALERFGGDRDAAAKALGISRTTLWRRLKA
>gnl|CDD|131383 TIGR02330, 2-methylcitrate_dehydratase, 2-methylcitrate dehydratase. Members of this family are bacterial proteins known or predicted to act as 2-methylcitrate dehydratase, an enzyme involved in the methylcitrate cycle of propionate catabolism. A related clade of archaeal proteins that may or may not be functionally equivalent is reserved for a future model and is excluded from this family. The PrpD enzyme of E. coli is responsible for the minor aconitase activity (AcnC) not accounted for by AcnA and AcnB
DAELVDIADYVLNYEISSKEAYDTARYCLMDTLGCGLLALEYPACTKLLGPVVPGTVVPNGARVPGTSFQ
LDPVKAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKRIASGKAPLTVKQVLEAMIKAH
EIQGVIALENSFNRVGLDHVLLVKVASTAVVAKMLGGTREEILNALSHAWVDGQSLRTYRHAPNTGSRKS
WAAGDATSRGVRLALKALTGEMGYPSALSAPVWGFYDVLFKGQSFRFPRPYGSYVMENVLFKISFPAEFH
AQTAVEAAVKLHPEVKARLDEIERITITTHESAIRIIDKVGPLNNPADRDHCIQYMVAIPLLFGRLTAED
YEDAVAQDPRIDALREKMNVVEDPRYTRDYLDPDKRSIANAVQVFFKDGTRTEEVEVEYPIGHRRRRDEG
IPKLVDKFKANLARQFPSKQQQRILEVCLDQARLEQTPVNEFLDLFAI
>gnl|CDD|131384 TIGR02331, surface_protein_R28, Rib/alpha/Esp surface antigen repeat. Sequences in this family are tandem repeats of about 79 amino acids, present in up to 14 copies in a protein and highly identical, even at the DNA level, within each protein. Sequences with these repeats are found in the Rib and alpha surface antigens of group B Streptococcus, Esp of Enterococcus faecalis, and related proteins of Lactobacillus. The repeat lacks Cys residues. Most members of this protein family also have the cell wall anchor motif LPXTG shared by many staphyloccal and streptococcal surface antigens
GETVEVGGTPDASDSITNLVDLPDGTTYVWKTVNTPDTNTPGDKPAVVVVTYPDGTKDTVPVTVHVTPPR
TDADKYDPAG
>gnl|CDD|131385 TIGR02332, putative_4-hydroxyphenylacetate_permease, 4-hydroxyphenylacetate permease. This protein is a part of the Major Facilitator Superfamily (pfam07690). Member of this family are found in a number of proteobacterial genomes, but only in the context of having genes for 4-hydroxyphenylacetate (4-HPA) degradation. The protein is characterized by Prieto, et al. (as 4-hydroxyphenylacetate permease in E. coli, where 3-HPA and 3,4-dihydroxyphenylacetate are shown to competitively inhibit 4-HPA transport and therefore also interact specificially
VIKKLFRRLIIFLFILFIFSFLDRINIGFAGLTMGKDLGLSATMFGLAATLFYAAYVICGIPSNIMLAII
GARRWIAGIMVLWGIASTATMFATGPESLYLLRILVGIAEAGFLPGILLYLTFWFPAYFRARANALFMIA
MPVTMALGLILSGYILALDGLMALKGWQWLFLLEGFPSVILGVMTWFWLDDSPDKAKWLDEEDKKALKEM
IDNDQLTLEQPEGAFAHAAMPQRSMLREIFTPAIMLYTLAYFCLTNTLSAINIWTPQILQSFNQGSSNIM
IGLLAAIPQFCTIFGMIWWSRHSDRLKERKHHTALPYLFAAAGWLLASATDHNLIQLLGIIMASMGSFSA
MAIFWTTPDQSISLQARAIAIAVINATGNIGSALSPFLIGILKDATGSFNSGLWFVAALLVI
>gnl|CDD|131386 TIGR02333, 2-methyl_citrate_dehydratase_Fe-S_dependent_AcnD, 2-methylisocitrate dehydratase, Fe/S-dependent. Members of this family appear in an operon for the degradation of propionyl-CoA via 2-methylcitrate. This family is homologous to aconitases A and B and appears to act the part as 2-methylisocitrate dehydratase, the enzyme after PrpD and before PrpB. In Escherichia coli, which lacks a member of this family, 2-methylisocitrate dehydratase activity was traced to aconitase B (TIGR00117) ()
NTLYRKPLPGTDLDYFDTRAAVEAIKPGAYDKLPYTSRILAENLVRRCDPETLSASLLQIIERKRDLDFP
WYPARVVCHDILGQTALVDLAGLRDAIAEKGGDPAQVNPVVPTQLIVDHSLAVEYGGFDPDAFEKNRAIE
DRRNEDRFHFINWTKTAFKNVDVIPAGNGIMHQINLEKMSPVIQVKNGVAFPDTCVGTDSHTPHVDALGV
IAIGVGGLEAETVMLGRASMMRLPDIVGVELTGKRQPGITATDIVLALTEFLRKERVVSAYLEFFGEGAR
ALTIGDRATISNMTPEYGATAAMFYIDEQTIDYLKLTGREPEQVKLVETYAKAAGLWADSLKHAVYERVL
EFDLSSVVRNMAGPSNPHARVPTSDLAARGIAGPAEEQPEGLMPDGAVIIAAITSCTNTSNPRNVVAAGL
LARNANQLGLKRKPWVKTSFAPGSKVAQLYLEEAGLLPELEQLGFGIVAFACTTCNGMSGALDPVIQQEI
IDRDLYATAVLSGNRNFDGRIHPYAKQAFLASPPLVVAYAIAGTIRFDIEKDVLGVDADGKPIRLKDIWP
SDEEIDAVVAAAVKPEQFRKVYIPMFDLDDTQSAVSPLYDWRPMSTYIRRPPYWEGALAGERTLKGMRPL
AILGDNITTDHLSPSNAILADSAAGEYLAKMGLPEEDFNSYATHRGDHLTAQRATFANPKLFNEMVKNDG
SVKQGSLARIEPEGKVTRMWEAIETYMNRKQPLIIIAGADYGQGSSRDWAAKGVRLAGVEAIVAEGFERI
HRTNLVGMGVLPLEFKPGTNRHTLGLDGTETFDVVGEITPRADLTLVVTRKNGEKLEVPVTCRLDTAEEV
SVYEAGGVLQRFAQDFLE
>gnl|CDD|131387 TIGR02334, conserved_hypothetical_protein, probable AcnD-accessory protein PrpF. The 2-methylcitrate cycle is one of at least five degradation pathways for propionate via propionyl-CoA. Degradation of propionate toward pyruvate consumes oxaloacetate and releases succinate. Oxidation of succinate back into oxaloacetate by the TCA cycle makes the 2-methylcitrate pathway a cycle. This family consists of PrpF, an incompletely characterized protein that appears to be an essential accessory protein for the Fe/S-dependent 2-methylisocitrate dehydratase AcnD (TIGR02333). This protein is related to but distinct from FldA (part of pfam04303), a putative fluorene degradation protein of Sphingomonas sp. LB126 [Energy metabolism, Fermentation]
MPQIRIPATYLRGGTSKGVFFRLEDLPEAARVPGEARDKLLLRVIGSPDPYGKQIDGMGGATSSTSKCVI
LSKSSRPGHDVDYLFGQVSIDKPFVDWSGNCGNLSAAVGAFAIHAGLVDPARIPEDGICTVRIWQANIGK
TIIAHVPISGGQVQETGDFELDGVTFPAAEVQLEFLDPADDGEGAMFPTGNLVDDLEVPGVGTFKATLIN
AGIPTVFVNAEDLGYTGTELQDAINGDPAALAMFETIRAYGALRMGLISDLEEAATRQHTPKVAFVAPPA
DYTASSGKLVNAAEIDLLVRALSMGKLHHAMMGTAAVAIGTAAAVPGTLVNLAAGGGERSAVRFGHPSGT
LRVGAEASQVNGQWTVTKAIMSRSARVLMEGWVRVPADVF
>gnl|CDD|131388 TIGR02335, phosphonoacetate_hydrolase, phosphonoacetate hydrolase. This family consists of examples of phosphonoacetate hydrolase, an enzyme specific for the cleavage of the C-P bond in phosphonoacetate. Phosphonates are organic compounds with a direct C-P bond that is far less labile that the C-O-P bonds of phosphate attachment sites. Phosphonates may be degraded for phosphorus and energy by broad spectrum C-P lyase encoded by large operon or by specific enzymes for some of the more common phosphonates in nature. This family represents an enzyme from the latter category. It may be found encoded near genes for phosphonate transport and for pther specific phosphonatases
ISVNGRSYALPQRPTVVICVDGCDPEYINRGIADGVAPFIAELTGFGTVLTADCVVPSFTNPNNLSIVTG
APPAVHGICGNYYLDQDTGEEIMMTDAKYLRAPTILGEMSKAGVLTAVVTAKDKLRKVLGHQLKGICFSS
EKADQVNLEEHGVENILALVGRPRPDVYSADLSLFVLDAGLSLLTNERPDLMYLSTSDYVQHKHAPGEPE
SNAFYAAMDSRFKRYHEQGAIVAITADHGMNAKTDAIGRPNILFLQDLLDAQFGAGRARVICPITDPFVR
HHGALGSFVRVYLRDPVDIRAMMDFAAGIAGVEAVLTRSQACQRFELPEDREGDFVVLGERLTVLGSRAD
KHDLSGLGDHPLRSHGGVSEQKVPFILSRPLVRDYRERAAPGRLRNFDIFDFALNGVA
>gnl|CDD|213701 TIGR02336, hypothetical_protein_BL1641, 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase. Members of this family are found in phylogenetically diverse bacteria, including Clostridium perfringens (in the Firmicutes), Bifidobacterium longum and Propionibacterium acnes (in the Actinobacteria), and Vibrio vulnificus (in the Proteobacteria), most of which occur as mammalian pathogens or commensals. The nominal activity, 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase (EC 2.4.1.211), varies somewhat from instance to instance in relative rates for closely related substrates [Energy metabolism, Biosynthesis and degradation of polysaccharides]
TSKGRFTLPSEENFAEKTKELAERWGADALRDSDGTHLDEAVLALGKKIYSAYFPVRADQEWATLHMDEL
PQVYLMSFPVLAESDRVDIPLLDGYFKEQLEPDRDADPKKWWEVVDRTTGEVVDPSKWTFDAQEDTVHVE
DAIPYHEYTVSFLAYIIWDPVEMYNHLTNDWGDKEHEIPFDIYHPATRKHVFDTFEQWLKDSPQTDVVRF
TTFFYQFTLLFDEKRREKVVDWFGYACTVSPRALEDFEAKYGYKLRPEDFVDAGYYNSTWRVPRKQYRDW
IDFLSGFVRENAKELVDMSHAAGKEAMMFLGDQWIGTEPYKDGFDEIGLDAVVGSVGDGTTTRMIADIPG
VKYTEGRFLPYFFPDVFYEGNDPVIEGLDNWRKARRAILRSPLDRIGYGGYLSLAAKFPKFVDTVTHIAN
EFREIHDRTGGVAAEGLPLKVAVLNSWGKMRSWMAFQVAHALPYKQTYSYYGILECLSGMPVEVEFISFD
DILEHGIDSDIDVIINGGDADTAWSGGDVWTNPKLVETVRAWVRGGGGFVGVGEPSAAPQNGRFFQLADV
IGVDKERYQTLSVDKYFPPVVPHHFITADIPVDGIDFGEPVLNVYPVNENVTVLRADGGQVQLATNDYGK
GRGVYISGLPYSAENARLLERVLFWASHNEDKYAAWSSSNPECEVAHFPEQGKYCVINNTDEPQKTTVTL
ADGTTEDFTLPPSEIRWRE
>gnl|CDD|188209 TIGR02337, Homoprotocatechuate_degradative_operon_repressor., homoprotocatechuate degradation operon regulator, HpaR. This Helix-Turn-Helix transcriptional regulator is a member of the MarR family (pfam01047) and is found in association with operons for the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate
SLPLALLQAREAAMSFFRPILAQHGLTEQQWRILRILAEQGSMEFTQLANQACILRPSLTGILARLERDG
LVTRLKASNDQRRVYISLTPKGQALYASLSPQIEEIYAAIEERLGEEK
>gnl|CDD|131391 TIGR02338, Prefoldin_subunit_beta, prefoldin, beta subunit, archaeal. Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and is found (usually) in bacteria and organelles of bacterial origin. The group II chaperonin system, called the thermosome in Archaea and TRiC or CCT in the Eukaryota, is structurally similar but only distantly related. Prefoldin, also called GimC, is a complex in Archaea and Eukaryota, that works with group II chaperonins. Members of this protein family are the archaeal clade of the beta class of prefoldin subunit. Closely related, but outside the scope of this family are the eukaryotic beta-class prefoldin subunits, Gim-1,3,4 and 6. The alpha class prefoldin subunits are more distantly related
IPPQVQNQLAQLQQLQQQLQAVATQKQQVEAQLKEAEKALEELERLPDDTPVYKSVGNLLVKTDKEEAIQ
ELKEKKETLELRVKTLQRQEERLREQLKELQEKIQEALAP
>gnl|CDD|274080 TIGR02339, Thermosome_subunit_alpha, thermosome, various subunits, archaeal. Thermosome is the name given to the archaeal rather than eukaryotic form of the group II chaperonin (counterpart to the group I chaperonin, GroEL/GroES, in bacterial), a torroidal, ATP-dependent molecular chaperone that assists in the folding or refolding of nascent or denatured proteins. Various homologous subunits, one to five per archaeal genome, may be designated alpha, beta, etc., but phylogenetic analysis does not show distinct alpha subunit and beta subunit lineages traceable to ancient paralogs [Protein fate, Protein folding and stabilization]
PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHP
AAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKIS
PEDRDLLKKIAYTSLTSKASAEVAKDKLADLVVEAVKQVAELRGDGKYYVDLDNIKIVKKKGGSIEDTEL
VEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIAS
AGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEITESDLGYAELVEERKV
GEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIELALRLRSY
ARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLELGVI
EPLRVKEQAIKSATEAATMILRIDDVIAA
>gnl|CDD|274081 TIGR02340, T-complex_protein_1_subunit_alpha, T-complex protein 1, alpha subunit. Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes
LFLGGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKI
LVELAQLQDREVGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKENLSVSVDELG
REALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVKTTNENGETKYPIKAINILKAHGKSARESMLVKGY
ALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGAN
VVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTLADLEGEETFEASYLGFADEVVQE
RIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVEAALSIYLE
NFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQLKPEKKHLKWYGLDLVNGK
IRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQSKG
>gnl|CDD|274082 TIGR02341, T-complex_protein_1_subunit_beta, T-complex protein 1, beta subunit. Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes
QIFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSSDASIMVTNDGATILKSIGVDNP
AAKVLVDMSKVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNG
SDEVKFRQDLMNIARTTLSSKILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFL
LDKKIGVNQPKRIENAKILIANTGMDTDKVKIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINC
FINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKL
LKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTP
GKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMRQLGITESYKV
KRAVVSSAAEAAEVILRVDNIIKAAPRKR
>gnl|CDD|274083 TIGR02342, T-complex_protein_1_subunit_delta, T-complex protein 1, delta subunit. Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT delta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes
FQDKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVE
LSKAQDIEAGDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQL
LKSATTSLSSKVVSQYSSLLAPLAVDAVLKVIDPENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKA
SKSAGGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQ
KSILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDHFTADKLGSAELVEEVDSDGGK
IIKITGIQNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEIEIARRLSKYART
MKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEEHVLQPL
LVTTSAITLASETVRSILKIDDIVFTR
>gnl|CDD|274084 TIGR02343, T-complex_protein_1_subunit_epsilon, T-complex protein 1, epsilon subunit. Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT epsilon chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes
ILAFDEYGRPFIIIKDQDNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGA
TILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAV
EHLEEISDEISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIAVDAVLNVADMERRDVDFDLIKVEGKV
GGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKF
KEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQELSKDKLGK
AGLVREISFGTTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAA
EISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNLGVDCLG
YGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISPG
>gnl|CDD|274085 TIGR02344, T-complex_protein_1_subunit_gamma, T-complex protein 1, gamma subunit. Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes
PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHP
AAKSMIELSRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVD
VNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQRDENGRKEIDIKRYAKVEKIPGGDIEDSCVL
KGVMINKDVTHPKMRRYIENPRIVLLDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAV
KPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRPEELRESDVGTGCGLFEVKKI
GDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVPGGGATEMAVSVALTEK
SKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETGKIVDMKEKGI
WEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK
>gnl|CDD|274086 TIGR02345, T-complex_protein_1_subunit_eta, T-complex protein 1, eta subunit. Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes
RPTIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIV
HPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVT
IDEEKGEQRELLEKCAATALSSKLISHNKEFFSKMIVDAVLSLDRDDLDLKLIGIKKVQGGALEDSQLVN
GVAFKKTFSYAGFEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIV
ESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVLGTCALFEERQ
IGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRD
YSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFV
WEPALVKINALKAAFEAACTILSVDETITNPKS
>gnl|CDD|274087 TIGR02346, T-complex_protein_1_subunit_theta, T-complex protein 1, theta subunit. Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes
GIASLLKEGYRHFSGLEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQ
HPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVW
EVKDLRDKDELIKALKASISSKQYGNEDFLAQLVAQACSTVLPKNPQNFNVDNIRVCKILGGSLSNSEVL
KGMVFNREAEGSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGV
NVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGD
KVTVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELASRLTKYGE
KLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGVKDASEAGIY
DMLATKKWAIKLATEAAVTVLRVDQIIMAKPAGGPKPPQGK
>gnl|CDD|274088 TIGR02347, T-complex_protein_1_subunit_zeta, T-complex protein 1, zeta subunit. Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes
SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHP
TASMIARAATAQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKE
DEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGL
VLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKK
VCGKSPDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNSVEDLTPECLGWAGL
VYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFEIAAY
RHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDP
EIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK
>gnl|CDD|274089 TIGR02348, 60_kDa_chaperonin, chaperonin GroL. This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118 [Protein fate, Protein folding and stabilization]
AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQ
LVKEVASKTNDVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKK
EIAQVATISANNDEEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKME
VELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFG
DRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKKVTVDKDNTTIVEGAGDKAAIKARVAQIKAQ
IEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNATRAAVEEGIVPGGGVALLRA
AAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAATGEYEDLVEAG
IIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE
>gnl|CDD|274090 TIGR02349, Chaperone_protein_DnaJ, chaperone protein DnaJ. This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family
DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFN
GGGGGGGGGFNGFDIGFFGDFGDIFGDFFGGGGGSGRRRRSGPRRGEDLRYDLELTFEEAVFGVEKEIEI
PRKESCETCHGTGAKPGTDPKTCPTCGGTGQVRRQQGTPFGFFQQQQTCPTCGGEGKIIKEPCSTCKGKG
RVKERKTITVKIPAGVDTGQRLRVSGKGNAGENGGPNGDLYVVIRVKPHKIFERDGNDLYIEVPISFTQA
ILGGEIEVPTLDGDVKLKIPAGTQSGTVFRLKGKGVPRLRGNGRGDLLVTVKVETPKNLSKEQKELLEEL
AEAS
>gnl|CDD|274091 TIGR02350, Chaperone_protein_DnaK, chaperone protein DnaK. Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE chaperone system. All members of the seed alignment were taken from completely sequenced bacterial or archaeal genomes and (except for Mycoplasma sequence) found clustered with other genes of this systems. This model excludes DnaK homologs that are not DnaK itself, such as the heat shock cognate protein HscA (TIGR01991). However, it is not designed to distinguish among DnaK paralogs in eukaryotes. Note that a number of dnaK genes have shadow ORFs in the same reverse (relative to dnaK) reading frame, a few of which have been assigned glutamate dehydrogenase activity. The significance of this observation is unclear; lengths of such shadow ORFs are highly variable as if the presumptive protein product is not conserved [Protein fate, Protein folding and stabilization]
KIIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGERLVGQPAKRQAVTNPENTIYSIKRF
MGRRFDEVTEEAKRVPYKVVGDGGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAY
FNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVL
STAGDTHLGGDDFDQRIIDWLADEFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITAD
ASGPKHLEMTLTRAKFEELTADLVERTKEPVRQALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFFGK
EPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTA
ADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVSAKDKGTGKEQSI
TITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEKIEKAV
AELKEALKGEDVEEIKAKTEELQQALQKLAEAMYQ
>gnl|CDD|131404 TIGR02351, ThiH_protein, thiazole biosynthesis protein ThiH. Members this protein family are the ThiH protein of thiamine biosynthesis, a homolog of the BioB protein of biotin biosynthesis. Genes for the this protein generally are found in operons with other thiamin biosynthesis genes [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
TFKDEIEDILWEEVSYDIYSFTAADVERALNKRHLSLEDFLALLSPAAEPYLEEMAQKAKKLTRKRFGNT
ISLFTPLYLSNYCSNKCVYCGFSMSNKIKRKKLNEEEIEREIEAIKKSGFKEILLVTGESEKAAGVEYIA
EAIKLAREYFSSLAIEVQPLNEEEYKKLVEAGLDGVTVYQETYNEKKYKKHHLAGKKKDFRYRLNTPERA
AKAGMRKIGIGALLGLDDWRTDAFFTAYHLRYLQKKYWKTEISISVPRLRPCTNGLKPKVIVTDRELVQI
ICAYRLFDPFVEISLSTRESKKFRDNVIPLGITKMSAGSSTEPGGYSSEKKGLEQFEISDERSVAEVEED
LRSKGLQPVWKDWDYF
>gnl|CDD|274092 TIGR02352, Glycine_oxidase, glycine oxidase ThiO. This family consists of the homotetrameric, FAD-dependent glycine oxidase ThiO, from species such as Bacillus subtilis that use glycine in thiamine biosynthesis. In general, members of this family will not be found in species such as E. coli that instead use tyrosine and the ThiH protein [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
WELAKRGHSVTLFDRDPMGGGASWAAAGMLAPHAECEYAEDPLFDLALESLRLYPEWLEALKELTGLDTG
YHQCGTLVVAFDEDDVEHLRQLADLQSATGMEVEWLSGRALRRLEPYLSGGIRGAVFYPDDAHVDPRALL
KALEKALEKLGVEIIEHTEVQHIEIRGEKVTAIVTPSGDVQADQVVLAAGAWAGELLPLPLRPVRGQPLR
LEAPAVPLLNRPLRAVVYGRRVYIVPRRDGRLVVGATMEESGFDTTPTLGGIKELLRDAYTILPALKEAR
LLETWAGLRPGTPDNLPYIGEHPEDRRLLIATGHYRNGILLAPATAEVIADLILGKE
>gnl|CDD|274093 TIGR02353, NON-RIBOSOMAL_PEPTIDE_SYNTHETASE, non-ribosomal peptide synthetase terminal domain of unknown function. This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size
VCQTLQLIPIVTLSGLQWLAPLLGYNWLYEALDDVSWLYLRAVALVFAVPVGRLGFAIAAKWLLVGRWKP
GTYPIWGSTYLRFWTVKRLVDAAPTVLLSGSPLYSLYLRALGAKIGKGVDIGSLPPVCTDLLTIGAGTIV
RKEVMLLGYRAERGRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIPDGERWHGSPA
QKTGADYRKVQPARPYTVRRRLYVAGALFVVFVLLPPLAFLFAIPVAITFDEIDWTLGPDMVGFILALVL
TFVALAGFIAYTVLLLAAVRLLLNLVLKPGRYYVHSGFYYQAWTVQQLMDNSRVLLFPLYASSYIPHWYR
ALGAKIGKVAEISSAQHEVPDLTDIGEETFIADGLLMGNARLSGGWFRLGRTRIGRRSFLGNSGYYPPGA
KTGDNVLLGVLSMTPKDGKVREGVGWLGSPPFELPRRVNRDDELEALTFEPDPRRRLARKNVENLRIILP
FLLVQWAMLFALVVLDLQALDDYTEWGAVALLAALILMAVGVGAFLILVERKWLVFGRLKPQEHPLWSPF
VWLHELHWKLYESVAVPNFLRPFRGTPFLPAILRLLGVKIGRGVYIDGTDLTERDLVTIGDDSTLNEGSV
IQTHLFEDRVMKSDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKGEEVPAHTRWRGNPA
>gnl|CDD|162819 TIGR02354, molybdopterin_biosynthesis_protein_moeB, thiamine biosynthesis protein ThiF, family 2. Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with one the E. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the divergent clade of putative ThiF proteins such found in Campylobacter [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
EEFRRALVARHTPKIVQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQ
VGEPKTEALKENISEINPYTEIEAYDEKITEENIDKFFKDADIVCEAFDNAEAKAMLVNAVLEKYKDKYL
IAASGLAGYDDANSIKTRKISKHFYLCGDGKSDAKQGLGLMAPRVQICAAHQANLVLELI
>gnl|CDD|131408 TIGR02355, Molybdopterin-synthase_adenylyltransferase, molybdopterin synthase sulfurylase MoeB. This model describes the molybdopterin biosynthesis protein MoeB in E. coli and related species. The enzyme covalently modifies the molybdopterin synthase MoaD by sulfurylation. This enzyme is closely related to ThiF, a thiamine biosynthesis enzyme that modifies ThiS by an analogous adenylation. Both MoeB and ThiF belong to the HesA/MoeB/ThiF family (pfam00899) [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
EMLRYNRQIILRGFDFDGQEALKASRVLIVGLGGLGCAASQYLAAAGVGNLTLLDFDTVSLSNLQRQVLH
SDANIGQPKVESAKDALTQINPHIAINPINAKLDDAELAALIAEHDIVVDCTDNVEVRNQLNRQCFAAKV
PLVSGAAIRMEGQVSVFTYQDGEPCYRCLSRLFGENALSCVEAGVMAPVVGVVGSLQAMEAIKVLAGIGK
PLSGKILMIDAMTMSFREMKLPKNPTCPVC
>gnl|CDD|274094 TIGR02356, molybdopterin_biosynthesis_protein_moeB, thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily. Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEE
DVGRPKVEVAAQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLI
SAAVVGFGGQLMVFDPGGEGPCLRCLFPDIADTGPSCATAGVIGPVVGVIGSLQALEALKLL
>gnl|CDD|274095 TIGR02357, conserved_hypothetical_protein, energy-coupled thiamine transporter ThiT. Members of this protein family have been assigned as thiamine transporters by a phylogenomic analysis of families of genes regulated by the THI element, a broadly conserved RNA secondary structure element through which thiamine pyrophosphate (TPP) levels can regulate transcription of many genes related to thiamine transport, salvage, and de novo biosynthesis. Species with this protein always lack the ThiBPQ ABC transporter. In some species (e.g. Steptococcus mutans and Streptoccus pyogenes), yuaJ is the only THI-regulated gene. Evidence from Bacillus cereus indicated thiamine uptake is coupled to proton translocation. However, a more recent comprehensive study of energy-coupled factor (ECF) transport suggests this protein is the S (subtrate capture) component of an ECF system, meaning it is energized by ATP. Previously YuaJ, but renamed ThiT [Transport and binding proteins, Other]
LRLLIEIAIMAALAMILSMIPLTVYPQGGGSVSFAMIPIVLISFRRGLKAGLVAGLIWGLLKIILGHAYI
LHPVQVFLEYILAFMALGLAGLFRQKTKKRALAPVILGTLVASLLRYFFHFIAGVIFWGSYAPKGMSAWL
YSLIYNGSSALVEALICAIVLILLVKKAPQLFI
>gnl|CDD|274096 TIGR02358, purine-cytosine_transport_protein, putative hydroxymethylpyrimidine transporter CytX. On the basis of a phylogenomic study of thiamine biosythetic, salvage, and transporter genes and a highly conserved RNA element THI, this protein family has been identified as a probable transporter of hydroxymethylpyrimidine (HMP), the phosphorylated (by ThiD) form of which gets joined (by ThiE) to hydroxyethylthiazole phosphate to make thiamine phosphate [Transport and binding proteins, Nucleosides, purines and pyrimidines, Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
RSLFLIWFGAAISIAEIQTGALLAPLGLTRGLLAILLGHLVGVLLLSAAGVIGADTGLSAMGSLKLSLGS
KGSVLPSLLNLLQLVGWTAVMIIVGAKAASLLGGRLFGEESPMLWILIVGILVTLWLLSGPLAFVWLNNW
SVWLLLIATLWLLVVVFSKADLSELWNRAGDMSFAVAVELVIAMPLSWLPLIADYTRFARNPRHVFLGTV
LGYFIGSCWMYFLGLAVTLATGQTDIISILAGAGLGIPALLIILLSTVTTTFMDIYSAAISTGNLLPRLK
VKHLAIGVGVLGTLIALLFPVDKYENFLLLIGSVFAPLYAVVFVDFFVVKRRRLSGYLNFQALVSWIIGF
ILYHALIAAGAPELKWLLGATIPAVLLAGVIYGLLS
>gnl|CDD|131412 TIGR02359, conserved_hypothetical_protein, energy coupling factor transporter S component ThiW. Levels of thiamine pyrophosphate (TPP) or thiamine regulate transcription or translation of a number of thiamine biosynthesis, salvage, or transport genes in a wide range of prokaryotes. The mechanism involves direct binding, with no protein involved,to a structural element called THI found in the untranslated upstream region of thiamine metabolism gene operons. This element is called a riboswitch and is seen also for other metabolites such as FMN and glycine. This protein family consists of proteins identified in operons controlled by the THI riboswitch and designated ThiW. The hydrophobic nature of this protein and reconstructed metabolic background suggests that this protein acts in transport of a thiazole precursor of thiamine [Transport and binding proteins, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
IRRLTLLALLIAIGVVLSQLIRIPVGPTKAAPVQHFVNVIAGVLLGPWYALAVAFIIGLLRNTLGLGTVL
AFPGGMPGALLAGLLYRFGRKHYWASLGEILGTGIIGSLLAYPVAAWLLGSSENFALFPITLGFIVSTLI
GSVIGWFVLVALKRTGVFRL
>gnl|CDD|131413 TIGR02360, p-hydroxybenzoate_hydroxylase, 4-hydroxybenzoate 3-monooxygenase. Members of this family are the enzyme 4-hydroxybenzoate 3-monooxygenase, also called p-hydroxybenzoate hydroxylase. It converts 4-hydroxybenzoate + NADPH + molecular oxygen to protocatechuate + NADPH + water. It contains monooxygenase (pfam01360) and FAD binding (pfam01494) domains. Pathways that contain this enzyme include the protocatechuate 4,5-degradation pathway [Energy metabolism, Other]
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQSRDYVLGRIRAGVLEQGTVDLLREAGVDERMDREGL
VHEGTEIAFDGQRFRIDLKALTGGKTVMVYGQTEVTRDLMEAREAAGLTTVYDADDVRLHDLAGDRPYVT
FERDGERHRLDCDFIAGCDGFHGVSRASIPAEVLKEFERVYPFGWLGILSETPPVSHELIYSNHERGFAL
CSMRSATRSRYYVQVPLTDKVEDWSDDRFWAELKRRLPSEAAERLVTGPSIEKSIAPLRSFVCEPMQYGR
LFLAGDAAHIVPPTGAKGLNLAASDVHYLYEALLEHYQEGSSAGIEGYSARALARVWKAERFSWWMTSLL
HRFPDTDAFDQRIQQAELEYLLGSEAAQATLAENYVGLPY
>gnl|CDD|274097 TIGR02361, Dihydroxyacetone_kinase_1, dihydroxyacetone kinase, ATP-dependent. This family consists of examples of the form of dihydroxyacetone kinase (also called glycerone kinase) that uses ATP (2.7.1.29) as the phosphate donor, rather than a phosphoprotein as in E. coli. This form is composed of a single chain with separable domains homologous to the K and L subunits of the E. coli enzyme, and is found in yeasts and other eukaryotes and in some bacteria, including Citrobacter freundii. The member from tomato has been shown to phosphorylate dihydroxyacetone, 3,4-dihydroxy-2-butanone, and some other aldoses and ketoses ()
KHFVNDPEHLVDDALKGLVAANPGLQLLESRKVVYRRDLNKDKVSLISGGGSGHEPAHAGFVGKGMLTAA
VAGDVFASPSTKQILAAIRAVVGSEAGTLLIVKNYTGDRLNFGLAAEKAKAEGYNVEMVIVGDDVSVGRK
KGGLVGRRGLAGTVLVHKIAGAAAARGLSLAEVAKVAQAAADNLVTIGASLDHCHVPGETEAEPELKEDE
MELGMGIHNEPGAKRISPIPSSDLVVQLMLKKLLDETDKRSYVKFNEGDEVVLLVNNLGGVSNLELGIIA
DEVVEQLALHYNIIPVRIYSGTFMTSLNGPGFSITLLNATEAGKSILDLLDAPTEAPGWPVAAYSSKPWR
EKREVVSSSAPELIEETAVRSYDPQLVAAILESGCAALLELEPHLTKLDTKAGDGDCGSTLARGAEAILE
LLKSKKLPLNDPATLLAQISDVVEGVMGGTSGALYSIFFSAAAQSLKQNASKKEEITPEAWAAALKTALD
ALYKYTGARPGDRTMIDALQPFVEALEAGKSNLNAAVKAAEAGAEATKKMKAKAGRASYVSSEALEGVPD
PGAVGLAAWLRGLA
>gnl|CDD|213706 TIGR02362, putative_dihydroxyacetone_kinase, probable dihydroxyacetone kinase DhaK1b subunit. Two types of dihydroxyacetone kinase (glycerone kinase) are described. In yeast and a few bacteria, e.g. Citrobacter freundii, the enzyme is a single chain that uses ATP as phosphoryl donor and is designated EC 2.7.1.29. By contract, E. coli and many other bacterial species have a multisubunit form with a phosphoprotein donor related to PTS transport proteins. This family represents a protein, unique to the Firmicutes (low GC Gram-positives), that appears to be a divergent second copy of the K subunit of that complex; its gene is always found in operons with the other three proteins of the complex
KIINEPQNAVSQAIQGIQWAYPNLVQVPDLPGIYDSNFDDQQIPIISGGGSGHEPAHWGYVGEGMLSAAI
MGDVFVPPTAQDILEAIRQVDRGKGVFVIIKNFEADLSEFSQAIQQARQEGRQIKYIIVHDDISVEHESF
KQRRRGVAGTILVHKILGAAAAEGASLDELEHIAAALVTNIATIGVAAKSARIPGQSTPSFDLEEGEIYY
GIGIHGEPGYRTEPFVSSEHLAVELVNKLKLKFRWQADDHYAVLVNNLGGTTPMEQMVFNNDVHELLALE
ALHLPFIKVGTFLTSLDMHGLSLTLLRLKDPQWLDYLNAPVDAAAW
>gnl|CDD|274098 TIGR02363, dhaK1, dihydroxyacetone kinase, DhaK subunit. Two types of dihydroxyacetone kinase (glycerone kinase) are described. In yeast and a few bacteria, e.g. Citrobacter freundii, the enzyme is a single chain that uses ATP as phosphoryl donor and is designated EC 2.7.1.29. By contract, E. coli and many other bacterial species have a multisubunit form (EC 2.7.1.-) with a phosphoprotein donor related to PTS transport proteins. This family represents the DhaK subunit of the latter type of dihydroxyacetone kinase, but it specifically excludes the DhaK paralog DhaK2 (TIGR02362) found in the same operon as DhaK and DhaK in the Firmicutes
MKKLINDPEDVVAEMLDGLVKAHPELVTLVADTRVIVRKDKKVNGKVALVSGGGSGHEPAHAGFVGYGML
DAAVPGEVFTSPTPDQILEAIKAVDQGAGVLLIVKNYTGDVMNFEMAAELAEDEGIKVATVVVDDDIAVE
DSLYTAGRRGVAGTVFVHKIAGAAAEKGASLDELKSLGEKVNPNTKSIGVALTACTVPAVGKPGFDLADD
EMEIGVGIHGEPGIRREKMKSSDEIADELLDKLLDDLGLQSGDRVIVLVNGMGATPLMELYIFYNDVQRL
LEQRGVNVARTLVGNYMTSLDMAGFSLTLLKLDDELLELWDAPVTTIAL
>gnl|CDD|131417 TIGR02364, dha_pts, dihydroxyacetone kinase, phosphotransfer subunit. In E. coli and many other bacteria, unlike the yeasts and a few bacteria such as Citrobacter freundii, the dihydroxyacetone kinase (also called glycerone kinase) transfers a phosphate from a phosphoprotein rather than from ATP and contains multiple subunits. This protein, which resembles proteins of PTS transport systems, is found with its gene adjacent to
VGIVLVSHSKKIAEGIKELIKQMAGDDVTIISAGGTDDGRLGTSPDKIIEAIEKADNEADGVLIFYDLGS
AVMNAEMAVELLEDEDRDKVHLVDAPLVEGAFAAAVEAQVGASIEQVLAEALQAK
>gnl|CDD|274099 TIGR02365, dha_L_ycgS, dihydroxyacetone kinase, phosphoprotein-dependent, L subunit. Two types of dihydroxyacetone kinase (glycerone kinase) are described. In yeast and a few bacteria, e.g. Citrobacter freundii, the enzyme is a single chain that uses ATP as phosphoryl donor and is designated EC 2.7.1.29. By contract, E. coli and many other bacterial species have a multisubunit form (EC 2.7.1.-) with a phosphoprotein donor related to PTS transport proteins. This family represents the subunit homologous to the E. coli YcgS subunit
ILNWLKNCGDLIIENKEYLTELDRAIGDGDHGINMARGFSEVKEKLDAFKDKTIGEILKNTGMTLISKVG
GASGPLYGTAFLKASKALKDDEILDAEDLAEILQAGLEGIQSRGKATPGEKTMVDVWAPVVEALRKAADE
PDALAAAREAAEQGAEATKDMQATKGRASYLGERSIGHIDPGATSSYYLFQALA
>gnl|CDD|274100 TIGR02366, conserved_hypothetical_protein, probable dihydroxyacetone kinase regulator. The seed alignment for this family was built from a set of closely related uncharacterized proteins associated with operons for the type of bacterial dihydroxyacetone kinase that transfers PEP-derived phosphate from a phosphoprotein, as in phosphotransferase system transport, rather than from ATP. Members have a TetR transcriptional regulator domain (pfam00440) at the N-terminus and sequence homology throughout
SIITKKKIAKAFKDLMEVQAFHKISVSDIMQTAQIRRQTFYNHFQDKYELLSWIFETELKEQVIDNLDYI
SWQNILDLLLRYFDENQTFYQKAFVIDGQNDFTHYFLEHCENLLDKLIDDYSKSSDSQWSDLEKSFICSF
YSAGAVGAITKWIVINCPSDPKLYSQHIKNLILTQI
>gnl|CDD|188213 TIGR02367, lysyl-tRNA_synthetase_class_II, pyrrolysyl-tRNA synthetase, C-terminal region. PylS is the enzyme responsible for charging the pyrrolysine tRNA, PylT, by ligating a free molecule of pyrrolysine. Pyrrolysine is encoded at an in-frame UAG (amber) at least in several corrinoid-dependent methyltransferases of the archaeal genera Methanosarcina and Methanococcoides, such as trimethylamine methyltransferase. This protein occurs as a fusion protein in Methanosarcina but as split genes in Desulfitobacterium hafniense and other bacteria [Protein synthesis, tRNA aminoacylation]
FKGLEHELISRRKRDLEQLRTEKRRPALGKLERELAKALVDRGFVQVKTPIIIPKEYLEKMTIDEDHPLF
SQVFWVDENKCLRPMLAPNLYNYLRKLDRLWPKPIRIFEIGPCYRKESQGSQHLNEFTMLNLCEMGSPLE
CRRERLEDLARWVLEHLGIREFELVTDSSVVYGDTVDVMHGDLELSSGAVGPHFLDREWGIVKPWVGAGF
GLERLLMVRHGTQNVRSMARSLSYLDGVRLNI
>gnl|CDD|131421 TIGR02368, Dimethylamine_methyltransferase_MtbB1, dimethylamine:corrinoid methyltransferase. This family consists of dimethylamine methyltransferases from the genus Methanosarcina. It is found in three nearly identical copies in each of M. acetivorans, M. barkeri, and M. Mazei. It is one of a suite of three non-homologous enzymes with a critical UAG-encoded pyrrolysine residue in these species (along with trimethylamine methyltransferase and monomethylamine methyltransferase). It demethylates dimethylamine, leaving monomethylamine, and methylates the prosthetic group of the small corrinoid protein MtbC. The methyl group is then transferred by methylcorrinoid:coenzyme M methyltransferase to coenzyme M. Note that the pyrrolysine residue is variously translated as K or X, or as a stop codon that truncates the sequence
MATEYALRMGDGKRVFLTKEKILEEIEAGTANAADLGEIPDLSADEMNKLAEILMMPGKAVSVEQGMEVP
VTHDIGTIRLDGDQGNSGVGIPSSRLVGCMTHERAFGADTMELGHIDYSFKPVKPVVSNECQAMEVCQQN
MIIPLFYGAMPNMGLYYTPDGPFENPGDLMKAFKIQEAWESMEHAAEHLTRDTVWVMQKLFASGADGVNF
DTTAAAGDADMYGTLHAIEALRKEFPEMYIEAGMAGEMVLGMHGNLQYDGVTLAGLWPHQQAPLVAKAGA
NVFGPVVNTNTSKTSAWNLARAVTFIKEAVKASPIPCHVDMGMGVGGIPMLETPPVDAVTRASKAMVEVA
GVDGIOIGVGDPLGMPISHIMASGMTGIRAAGDLVARMQFSKNMRIGEAKEYVAKKLNVDIMDLADEHVM
RELREELDIGVITSVPGAAKGIAAKMNIEKLLGIKINSCELFRKQT
>gnl|CDD|131422 TIGR02369, Trimethylamine_methyltransferase_MttB1, trimethylamine:corrinoid methyltransferase. This model represents a distinct subfamily of pfam06253. All members here are trimethylamine:corrinoid methyltransferases that contain a critical pyrrolysine residue incorporated during translation via a special tRNA for a TAG (amber) codon. Known members so far are from the genus Methanosarcina. It is one of a suite of three non-homologous enzymes with a critical UAG-encoded pyrrolysine residue in these species (along with dimethylamine methyltransferase and monomethylamine methyltransferase). It demethylates trimethylamine, leaving dimethylamine, and methylates the prosthetic group of its small cognate corrinoid protein, MttC. The methyl group is then transferred by methylcorrinoid:coenzyme M methyltransferase to coenzyme M. Note that the pyrrolysine residue is variously translated as K or X, or as a stop codon that truncates the sequence
KNNAVAGFNALNGVELNLFTIDELKAIHYATMDVLMNPGVQVSDPEARQIFKENGCEVDEKTNVVKIPEY
LVRRALQLAPSRFVLWGRDKKFNTVQEAGGKVHWTCFGTGVKMCKYQDGKYVTVDSVEQDIADIAKLCDW
AENIDYFSLPVSARDIAGKGAQDVHETLTPIANTAKHYHHIDPVGENVEYYRDIVKAYYGGDEEEARKKP
IFSMLLCPTSPLELSVNACQVIIKGARFGMPVNVLSMAMSGGSSPVYLAGTLVTHNAEVLAGITLAQLTV
PGAKVWYGSSTTTFDLKKGTAPVGSPELGLISAAVAKLAQFYGLPAFVAGTOADAKIPDNQAGHEKTMTC
FLPALAGANTIYGAGMLELGMTFSMEQLVIDNDIIKMTKKALQGIEVNEETLAVDSIQKVGIGNNFLALK
QTRLLVNYPSDPMLIDRRMFGDWAAAGSKDLAAAAHDKVTDVLKHHEVKPIDADILKDMQAIVDRADKA
>gnl|CDD|131423 TIGR02370, Monomethylamine_corrinoid_protein_1, methyltransferase cognate corrinoid proteins, Methanosarcina family. This model describes a subfamily of the B12 binding domain (pfam02607, pfam02310) proteins. Members of the seed alignment include corrinoid proteins specific to four different, mutally non-homologous enzymes of the genus Methanosarcina. Three of the four cognate enzymes (trimethylamine, dimethylamine, and monomethylamine methyltransferases) all have the unusual, ribosomally incorporated amino acid pyrrolysine at the active site. All act in systems in which a methyl group is transferred to the corrinoid protein to create methylcobalamin, from which the methyl group is later transferred elsewhere
KLAKAIFEGEEDDVVEGAQKALDAGIDPIELIEKGLMAGMGVVGKLFEDGELFLPHVMMSADAMLAGIKV
LTPEMEKAVETEVLGKVVCGVAEGDVHDIGKNIVVTMLRANGFDVIDLGRDVPIDTVVEKVKKEKPLMLT
GSALMTTTMYGQKDINDKLKEEGYRDSVKFMVGGAPVTQDWADKIGADVYGENASDA
>gnl|CDD|131424 TIGR02371, Alanine_Dehydrogenase_Dimer_WBOUND_NAD_ARCHAEAL, alanine dehydrogenase, Archaeoglobus fulgidus type. This enzyme, a homolog of bacterial ornithine cyclodeaminases and marsupial mu-crystallins, is a homodimeric, NAD-dependent alanine dehydrogenase found in Archaeoglobus fulgidus and several other Archaea. For a number of close homologs, scoring between trusted and noise cutoffs, it is not clear at present what is the enzymatic activity
ETLVLTQEEVESLLNMDDCMKAVEGAFRQEALGKVQMPPKMYLFFRRYNGDLRVMPAYLEELEMAGVKCV
NVHPGNPDRHLPTVMALIILVSPETGFPIALMDGTYITDMRTGAAGGVAAKYLARKDSSVLGIIGAGRQA
WTQLEALSRVFDLEEVSVYCRTPSTREKFALRASDYEVPVRAATDPREAVEGCDILVTTTPSRKPVVKAD
WVSEGTHINAIGADAPGKQELDPEILKNAKIFVDDLEQATHSGEINVPISKGIIRVDDLHASLGEVITGL
KEGRTSPEEITIFDSTGLAIQDVATAWMVYERAVAGEVGLEVDLF
>gnl|CDD|131425 TIGR02372, 4-coumarate--CoA_ligase, 4-coumarate--CoA ligase, photoactive yellow protein activation family. This model represents the 4-coumarate--CoA ligase associated with biosynthesis of the 4-hydroxy cinnamyl (also called 4-coumaroyl) chromophore covalently linked to a Cys residue in photoactive yellow protein of Rhodobacter spp. and Ectothiorhodospira halophila. This enzyme is designated 6.2.1.12 and therefore joins a number of plant enzymes linked to lignin biosynthesis and given similar names
QVLDAEAVGRLLVSLIAAEQQEGRVQHHQMPEARLLTADLRIDEETLGLDSLLRLSLVTAVAGFFHLSDT
GTEDYLLVRRRIGEWVDLIAHHSTPTARFTFATSGSTGTPKPVTHSWAALLSEAQAIAKILGERPPPVRR
VISCVPAHHLYGFLFSCLLPSRRGLEAKQLAAAPASGIMRHARPGDLIVGTPFIWEQLADLDYRLPGVVG
VSSGAPSTAATWRCLLAAGLARLLEVYGATETGGIGLREAPDDPFRLLPDLACFADTLSSAGLARRLDLQ
DRLAWDKDGGFTILGRKDEILQVGGVNVSPGHVRDILERNPRVRAAAVRLDGRRLKAFIVVAEDADEAEL
EIELRATAARHLPAPARPDRFRFGTELPRTGAGKLA
>gnl|CDD|131426 TIGR02373, Photoactive_yellow_protein, photoactive yellow protein. Members of this family are photoactive yellow protein, a cytosolic, 14-kDa light-sensing protein which has a 4-hydroxycinnamyl (p-coumaric acid) chromophore covalently linked to a Cys residue. The enzyme 4-coumarate--CoA ligase as described by TIGR02372 is required for its biosynthesis. The modified Cys is in a PAS (pfam00989) domain, frequently found in signal transducing proteins. Members are known in alpha and gamma Proteobacteria that include Rhodobacter capsulatus, Halorhodospira halophila, Rhodospirillum centenum, etc
ETIDFGTEDIENTLAGMGDAQFDALPFGAIQLDGSGVILRYNAAEGRITGRDPERVIGRNFFKEVAPCTD
IPEFSGRFMEGVASGTLNAMFDYVFDYQMAPVKVKIHMKNAGVGDSYWIFVKRV
>gnl|CDD|162827 TIGR02374, Nitrite_reductase_NADH_large_subunit, nitrite reductase [NAD(P)H], large subunit [Central intermediary metabolism, Nitrogen metabolism]
LVLVGNGMAGHRCIEEVLKLNRHMFEITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKHGIT
LYTGETVIQIDTDQKQVITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRF
KKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVG
ATKADRIRFKDGSSLEADLIVMAAGIRPNDELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRV
YGLVAPLYEQAKVLADHICGVECEEYEGSDLSAKLKLLGVDVWSAGDAQETERTTSIKIYDEQKGIYKKL
VLSDDKLLGAVLFGDTSDYGRLLDMVLKQADISEDPAIIKPQISGPEAGGPGVEAMPDSEQICSCNTVTK
GAIIDAIHTGSCTTVEELKACTKAGTSCGGCKPLVEQLLRAELNSQYTASTPALCECTDFSRDELFEEIQ
ARGFTTFAEVMNQLGWKTKNGCSTCKPAVQYYLAMLYPGFILDEEATSLSNDHFLANIQKDGTYSVIPRM
YGGRTNPEQLRTIANIAEAYSIPYVKITGGQRLDLFGAKKDDLPNIWKDLKMPGYEHAYGKALRTVKTCV
GSQWCRYGNQDSVQLAIQLERRYEGLRTPHKIKIGVSGCERECAEAAGKDVGVIATEKGWNLYVGGNGGT
HPRHGDLLAVDEDEETLIGYIDRFLQYYRETADYLERTAPWLERLGIDHVREVLFEDDLRAELEESMQRD
LSLIKCPWKETLEDK
>gnl|CDD|131428 TIGR02375, pseudoazurin, pseudoazurin. Pseudoazurin, also called cupredoxin, is a small, blue periplasmic protein with a single bound copper atom. Pseudoazurin is related plastocyanins. Several examples of pseudoazurin are encoded by a neighboring gene for, or have been shown to transfer electrons to, copper-containing nitrite reductases (TIGR02376) of the same species [Energy metabolism, Electron transport]
MLNKGAEGAMVFEPAYIRAAPGDTVTFVPTDKGHNVETIKGMIPEGAEAFKSKINEEYTVTLTKEGVYGV
KCTPHYGMGMVGLIQVGDPPANLEAAKSAKHPKKAQERLDKIFAQV
>gnl|CDD|131429 TIGR02376, Copper-containing_nitrite_reductase, nitrite reductase, copper-containing. This family consists of copper-type nitrite reductase. It reduces nitrite to nitric oxide, the first step in denitrification [Central intermediary metabolism, Nitrogen metabolism]
LPRVKVDLVAPPFVHVHDQIDRSGPKVVEVTMTIEEKKMVIDDGVTYQAMTFDGSVPGPLIRVHEGDYVE
LTLINPPTNTMPHNVDFHAATGALGGAALTQVNPGETATLRFKATRPGAFVYHCAPPGMVPWHVVSGMNG
AIMVLPREGLPEYDKEYYIGESDLYTPKDEGEGGAYEDDVAAMRTLTPTHVVFNGAVGALTGDNALTAGV
GERVLFVHSQPNRDSRPHLIGGHGDYVWVTGKFANPPNRDVETWFIPGGSAAAALYTFEQPGVYAYVDHN
LIEAFEKGAAAQVKVEGAWNPDLMTQVVAPT
>gnl|CDD|131430 TIGR02377, putative_Rieske-like_ferredoxin_MocE, Rieske [2Fe-2S] domain protein, MocE subfamily. This model describes a subfamily of the Rieske-like [2Fe-2S] family of ferredoxins that includes MocE, part of the rhizopine (3-O-methyl-scyllo-inosamine) catabolic cluster in Rhizobium. Members of this family are related to, yet distinct from, the small subunit of nitrite reductase [NAD(P)H]
NWVKACDADDIGREDVARFDHGGRTFAIYRTPDDQYYATDGLCTHEYAHLADGLVMDTTVECPKHAGCFD
YRTGEALNPPVCVNLKTYPVKVVDGAVYVDI
>gnl|CDD|131431 TIGR02378, Assimilatory_nitrite_reductase_small_subunit, nitrite reductase [NAD(P)H], small subunit. This model describes NirD, the small subunit of nitrite reductase [NAD(P)H] (the assimilatory nitrite reductase), which associates with NirB, the large subunit (TIGR02374). In a few bacteria such as Klebsiella pneumoniae and in Fungi, the two regions are fused [Central intermediary metabolism, Nitrogen metabolism]
TWQDICAIDDIPEETGVCVLLGDTQIAIFRVPGDQVFAIQNMCPHKRAFVLSRGIVGDAQGELWVACPLH
KRNFRLEDGRCLEDDSGSVRTYEVRVEDGRVYVAL
>gnl|CDD|131432 TIGR02379, dTDP-4-amino-46-dideoxygalactose_transaminase, TDP-4-keto-6-deoxy-D-glucose transaminase. This family consists of TDP-4-keto-6-deoxy-D-glucose transaminases, the WecE (formerly RffA) protein of enterobacterial common antigen (ECA) biosynthesis, from enterobacteria. It also includes closely matching sequence from species not expected to make ECA, but which contain other genes for the biosynthesis of TDP-4-keto-6-deoxy-D-Glc, an intermediate in the biosynthesis of other compounds as well and the substrate of WecA. This family belongs to the DegT/DnrJ/EryC1/StrS aminotransferase family (pfam01041) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
MIPFNKPPVTGTELDYIQEAISSGKLSGDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQP
GDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMA
LANKHNLFVIEDAAQGVMSTYKGRALGSIGHIGTFSFHETKNYTSGGEGGALLINDQAFIERAEIIREKG
TNRSQFFRGEVDKYTWRDIGSSYLPSELQAAYLWAQLEQADRINQQRLALWQNYYDALAPLEEKGIIELP
SIPDGCQHNAHMFYIKLRDIDDRSELINFLKEQEIMAVFHYIPLHSSPAGRHFGRFHGEDIYTTKESERL
VRLPLFYGLSPEDQRRVIATLCDYLS
>gnl|CDD|131433 TIGR02380, ECA_wecA, undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphatetransferase. Members of this family are the WecA enzyme of enterobacterial common antigen biosynthesis, undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphatetransferase. This family represents one narrow clade, and closely related sequences outside this clade may represent enzymes that catalyze the same specific reaction, but in the context of different pathways. A His-rich motif in a cytosolic loop of this integral membrane protein, shown critical to enzymatic activity for WecA is variously present or absent in the clade that includes Bacillus subtilis TagO teichoic acid biosynthesis enzyme, which may catalyze the same reaction as WecA [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
FLELIVIFLSSFAFLFLMRKVAKIVGLVDKPNARKRHQGFIPLVGGISIFLTLCIYLFLHPALIPHYSLY
LFCATILVVIGIIDDRFDISVKIRLAIQAAVSIVMIQFGNIYLHSLGNIFGPKELTLGLFGYIITIFAVI
GAINAFNMIDGIDGLLGGLSCVSFAALGYLFWLDGQVELAYWCFALIVAILPYLMLNLGIPLGRKFKVFM
GDAGSTFIGFTVIWLLLLATQGESSPSMRPVTALWLIALPLMDMAAIMLRRIRKGDSPFKPDRQHLHHIL
QRLGLTSRQSLFVICGFAALFAAIGIWSEVNNVSEWVMLVSFFALFFVYFYLISHIWKITRLVHRF
>gnl|CDD|131434 TIGR02381, Cold_shock-like_protein_CspD, cold shock domain protein CspD. This model represents what appears to be a phylogenetically distinct clade, containing E. coli CspD (SP|P24245) and related proteobacterial proteins within the larger family of cold shock domain proteins described by pfam00313. The gene symbol cspD may have been used idependently for other subfamilies of cold shock domain proteins, such as for B. subtilis CspD. These proteins typically are shorter than 70 amino acids. In E. coli, CspD is a stress response protein induced in stationary phase. This homodimer binds single-stranded DNA and appears to inhibit DNA replication [DNA metabolism, DNA replication, recombination, and repair, Cellular processes, Adaptations to atypical conditions]
MAIGIVKWFNNAKGFGFICPEGVDGDIFAHYSTIQMDGYRTLKAGQKVQFEVVQGPKGAHATHIVPIE
>gnl|CDD|131435 TIGR02382, dTDP-fucosamine_acetyltransferase, TDP-D-fucosamine acetyltransferase. This model represents the WecD protein (Formerly RffC) for the biosynthesis of enterobacterial common antigen (ECA), an outer leaflet, outer membrane glycolipid with a trisaccharide repeat unit. WecD is a member of the GNAT family of acetytransferases (pfam00583) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
VQAKIAASNLGLLDALQQLGFSLVEGEVDLSLPVNNTENATSDPGARVATETDIPALRQLASAAFALSRF
RAPWYAPDDSGRFYAQWVENAVRGTFDHQCLILRDASGDPRGYVTLRELNDTDARIGLLAVFPGAQSRGI
GAELMQTALNWCYARGLTRLRVATQMGNTAALRLYIRSGANIESTAYWLYR
>gnl|CDD|274101 TIGR02383, RNA-binding_protein_Hfq, RNA chaperone Hfq. This model represents the RNA-binding pleiotropic regulator Hfq, a small, Sm-like protein of bacteria. It helps pair regulatory noncoding RNAs with complementary mRNA target regions. It enhances the elongation of poly(A) tails on mRNA. It appears also to protect RNase E recognition sites (A/U-rich sequences with adjacent stem-loop structures) from cleavage. Being pleiotropic, it differs in some of its activities in different species. Hfq binds the non-coding regulatory RNA DsrA (see Rfam RF00014) in the few species known to have it: Escherichia coli, Shigella flexneri, Salmonella spp. In Azorhizobium caulinodans, an hfq mutant is unable to express nifA, and Hfq is called NrfA, for nif regulatory factor (see . The name hfq reflects phenomenology as a host factor for phage Q-beta RNA replication [Regulatory functions, Other]
QNLQDQFLNQLRKERIPVTVFLVNGVQLKGVIESFDNFTVLLESQGKQQLIYKHAISTISP
>gnl|CDD|274102 TIGR02384, Putative_antitoxin_RelB, addiction module antitoxin, RelB/DinJ family. Plasmids may be maintained stably in bacterial populations through the action of addiction modules, in which a toxin and antidote are encoded in a cassette on the plasmid. In any daughter cell that lacks the plasmid, the toxin persists and is lethal after the antidote protein is depleted. Toxin/antitoxin pairs are also found on main chromosomes, and likely represent selfish DNA. Sequences in the seed for this alignment all were found adjacent to toxin genes. The resulting model appears to describe a narrower set of proteins than pfam04221, although many in the scope of this model are not obviously paired with toxin proteins. Several toxin/antitoxin pairs may occur in a single species [Cellular processes, Toxin production and resistance, Mobile and extrachromosomal element functions, Other]
MATATISIRIDEELKKEAYAVFEELGLTPSTAIRMFLKQVIREQGLPFDLRLPNDETLAAIEEIKELRKL
ENKFKSVKDLLDDL
>gnl|CDD|211740 TIGR02385, Hypothetical_relE_protein., addiction module toxin, RelE/StbE family. Plasmids may be maintained stably in bacterial populations through the action of addiction modules, in which a toxin and antidote are encoded in a cassette on the plasmid. In any daughter cell that lacks the plasmid, the toxin persists and is lethal after the antidote protein is depleted. Toxin/antitoxin pairs are also found on main chromosomes, and likely represent selfish DNA. Sequences in the seed for this alignment all are found adjacent to RelB/DinJ family antitoxin genes (TIGR02384), as are most genes found by the resulting model. StbE from Morganella morganii plasmid R485 shows typical behaviour for an addiction module toxin. It cannot be cloned without its partner (the antitoxin), whereas its partner cannot confer plasmid stability without StbE [Cellular processes, Toxin production and resistance, Mobile and extrachromosomal element functions, Other]
KIVYTEQFKKDLKKIKKYIRKDLPKLLEVIELLINGKPLERRYRDHPLTGSWKGTRECHIEPDYLLVYQV
EDEVVIRLVRVGSHSQLF
>gnl|CDD|274103 TIGR02386, DNA-directed_RNA_polymerase_subunit_beta', DNA-directed RNA polymerase, beta' subunit, predominant form. Bacteria have a single DNA-directed RNA polymerase, with required subunits that include alpha, beta, and beta-prime. This model describes the predominant architecture of the beta-prime subunit in most bacteria. This model excludes from among the bacterial mostly sequences from the cyanobacteria, where RpoC is replaced by two tandem genes homologous to it but also encoding an additional domain [Transcription, DNA-dependent RNA polymerase]
AIKISIASPDTIRNWSYGEVKKPETINYRTLKPEKDGLFCEKIFGPTKDWECYCGKYKKIRYKGVVCERC
GVEVTESKVRRERMGHIELAAPVAHIWYFKGLPSRIGLLLDITAKELESVLYFENYVVLDPGDTKLDKKE
VLDETEYREVLKRYGDGFRAGMGAEAIKELLEKIDLDKEIEELKIQLRESKSDQKRKKLLKRLEIVEAFK
DSGNRPEWMVLDVIPVIPPELRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLLELGAPEIIVRNEKRM
LQEAVDALFDNGRRGKPVVGKNNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKMYQCGL
PKKMALELFKPFIIKRLIDRELAANIKSAKKMIEQEDPEVWDVLEDVIKEHPVLLNRAPTLHRLGIQAFE
PVLVEGKAIRLHPLVCTAFNADFDGDQMAVHVPLSPEAQAEARALMLASNNILNPKDGKPIVTPSQDMVL
GLYYLTTEKPGAKGEGKIFSNVDEAIRAYDNGKVHLHALIGVRTSGEILETTVGRVIFNEILPEGFPYIN
DNEPLSKKEISSLIDLLYEVHGIEETAEMLDKIKALGFKYATKSGTTISASDIVVPDEKYEILKEADKEV
AKIQKFYNKGLITDEERYRKVVSIWSETKDKVTDAMMKLLKKDTYKFNPIFMMADSGARGNISQFRQLAG
MRGLMAKPSGDIIELPIKSSFREGLTVLEYFISTHGARKGLADTALKTADSGYLTRRLVDVAQDVVVREE
DCGTEEGIEVEAIVEGKDEIIESLKDRIVGRYSAEDVYDPDTGKLIAEANTLITEEIAEKIENSGIEKVK
VRSVLTCESEHGVCQKCYGRDLATGKLVEIGEAVGVIAAQSIGEPGTQLTMRTFHTGGVAGASGDITQGL
PRVKELFEARTPKDKAVIAEVDGTVEIIEDIVKNKRVVVIKDENDEEKKYTIPFGAQLRVKDGDSVSAGD
KLTEGSIDPHDLLRIKGIQAVQEYLVKEVQKVYRLQGVEINDKHIEVIVRQMLRKVRITDSGDSNLLPGE
LIDIHEFNEENRKLLEQGKKPASAIPQLLGITKASLNTESFLSAASFQETTKVLTDAAIKGKVDYLLGLK
ENVIIGNLIPAGTGLKTYKE
>gnl|CDD|131440 TIGR02387, DNA-directed_RNA_polymerase_subunit_gamma, DNA-directed RNA polymerase, gamma subunit. The RNA polymerase gamma subunit, encoded by the rpoC1 gene, is found in cyanobacteria and corresponds to the N-terminal region the beta' subunit, encoded by rpoC, in other bacteria. The equivalent subunit in plastids and chloroplasts is designated beta', while the product of the rpoC2 gene is designated beta''
RFDYVKITIASPERVMEWGQRTLPNGQVVGEVTKPETINYRTLKPEMDGLFCEKIFGPSKDWECHCGKYK
RVRHRGIVCERCGVEVTESRVRRHRMGYIKLAAPVTHVWYLKGIPSYVSILLDMPLRDVEQIVYFNAYVV
LNPGNAKNLKYKQLLTEDQWLEIEDQIYAEDSELENEEVVGIGAEALKQLLADLNLEEVAEQLREEINGS
KGQKRAKLIKRLRVIDNFIATSSRPEWMVLDVIPVIPPDLRPMVQLDGGRFATSDLNDLYRRVINRNNRL
ARLQEILAPEIIVRNEKRMLQEAVDALIDNGRRGRTVVGANNRPLKSLSDIIEGKQGRFRQNLLGKRVDY
SGRSVIVVGPKLKMHQCGLPKEMAIELFQPFVIHRLIRQGIVNNIKAAKKLIQRADDEIWSVLQEVITGH
PVMLNRAPTLHRLGIQAFEPILVDGRAIQLHPLVCPAFNADFDGDQMAVHVPLSLEAQTEARLLMLASNN
VLSPATGEPIVTPSQDMVLGCYYLTALNPGAEKGRGRYFSSLEDAIHAYEDGRIDLHDWIWVRFNGEVET
NDPLDEPIKSEDLSDGTRIEQWTYRRDRFDEDGALISQYILTTTGRIIMNHTIIEALVA
>gnl|CDD|274104 TIGR02388, DNA-directed_RNA_polymerase_subunit_beta', DNA-directed RNA polymerase, beta'' subunit. The family consists of the product of the rpoC2 gene, a subunit of DNA-directed RNA polymerase of cyanobacteria and chloroplasts. RpoC2 corresponds largely to the C-terminal region of the RpoC (the beta' subunit) of other bacteria. Members of this family are designated beta'' in chloroplasts/plastids, and beta' (confusingly) in Cyanobacteria, where RpoC1 is called beta' in chloroplasts/plastids and gamma in Cyanobacteria. We prefer to name this family beta'', after its organellar members, to emphasize that this RpoC1 and RpoC2 together replace RpoC in other bacteria [Transcription, DNA-dependent RNA polymerase]
IFKNRVVDKKALKNLISWAYKTYGTARTAAMADKLKDLGFRYATRAGVSISVDDLKVPPAKQDLLEAAEK
EIRATEERYRRGEITEVERFQKVIDTWNGTNEELKDEVVNNFRQTDPLNSVYMMAFSGARGNMSQVRQLV
GMRGLMANPQGEIIDLPIKTNFREGLTVTEYVISSYGARKGLVDTALRTADSGYLTRRLVDVSQDVIVRE
EDCGTERSIVVRAMTEGDKKISLGDRLLGRLVAEDVLHPEGEVIVPKNTAIDPDLAKTIETAGISEVVVR
SPLTCEAARSVCRKCYGWSLAHAHLVDLGEAVGIIAAQSIGEPGTQLTMRTFHTGGVFTGEVARQVRSKI
DGTVEFGKKLRTRGYRTRHGEDAKQVEVAGLLIIKPTGSITNKAQEIEVTQGSLLFVEDGQTVDAGQLLA
EIALGAVRKSTEKATKDVASDLAGEVKFDKVVPEEKTDRQGNTTRIAQRGGLIWVLSGEVYNLPPGAEPV
VKNGDRVEQGTVLAETKLSTEHGGVVRLPESVGDSREVEIITASVLLDQAKVIEESSQGRELYHIETADG
QRFRLKAAPGTKVQNGQVVAELIDDRYRTTTGGLLKYAGVEVAKKGKAKQGYEVSQGGTLLWIPEETHEI
NKDISLLMVEDGQYVEAGTEVVKDIFCQNSGIVEVTQKNDILREIIVKPGEFHEVDDPEAVSTEEGTLLQ
PGEEVLPGVVVDELSQVQYLETPEGPGLLLRPVEEYTVPDEPEVPSQSSVSQEKGRSIALRAVQRLPYKD
GERVKSVEGVELLRTQLVLEIFDEGPQLAADIELIQDEEDKDIQRLQLVILESLVLRRDIASDSTQGSTH
TSLLVKDGDLIKPGAVIARTQILCKEAGVVQGIDSGGESIRRLLVERNSDRLKVNIKAKPVVKTGDLVVA
GDELAKGVKAEESGEIEEVASDYVILRIGRPYRVSPGAVLHIEDGDLVQRGDNLALLVFERAKTGDIVQG
LPRIEELLEARKPKEACILAKRPGVVQVKYGTDDESVSIKVIERDGTISEYPLLPGQNIMVSDGQQVTGG
EPLTDGPINPHDILDVFFSYYKDQDGLYEAAQESLQKVQRFLVNEVQNVYQSQGVDISDKHIEVIVRQMT
SKVRIDDAGDTTLLPGELVELRQVEQVNEAMAITGGAPAQYTPVLLGITKASLNTDSFISAASFQETTRV
LTEAAIEGKSDWLRGLKENVIIGRLIPAGTGFSSYEE
>gnl|CDD|274105 TIGR02389, DNA-directed_RNA_polymerase_subunit_A'', DNA-directed RNA polymerase, subunit A''. This family consists of the archaeal A'' subunit of the DNA-directed RNA polymerase. The example from Methanocaldococcus jannaschii contains an intein [Transcription, DNA-dependent RNA polymerase]
VLPEKLLKELEETVKKREISDKEELDEIIKRVEEEYLRSLIDPGEAVGIVAAQSIGEPGTQMTMRTFHYA
GVAELNVTLGLPRLIEIVDARKTPSTPSMTIYLEDEYEKDREKAEEVAKKIEATKLEDVAKDISIDLADM
TVIIELDEEQLKERGITVDDVEKAIKKAKLGKVIEIDMDNNTITIKPGNPSLKELRKLKEKIKNLHIKGI
KGIKRVVIRKEGDEYVIYTEGSNLKEVLKLEGVDKTRTTTNDIHEIAEVLGIEAARNAIIEEIKRTLEEQ
GLDVDIRHLMLVADLMTWDGEVRQIGRHGISGEKASVLARAAFEVTVKHLLDAAIRGEVDELKGVIENII
VGQPIPLGTGDVDLVMD
>gnl|CDD|274106 TIGR02390, DNA-directed_RNA_polymerase_subunit_A', DNA-directed RNA polymerase subunit A'. This family consists of the archaeal A' subunit of the DNA-directed RNA polymerase. The example from Methanocaldococcus jannaschii contains an intein
PKKIGSIKFGLLSPEEIRKMSVVEVVTADTYDDDGYPIEGGLMDPRLGVIEPGLRCKTCGGKVGECPGHF
GHIELARPVVHVGFAKEIYKILRATCRKCGRITLTEEEIEQYLEKINKLKEEGGDLASTLIEKIVKEAAK
RMKCPHCGEEQKKIKFEKPTYFYEEGKEGDVKLTPSEIRERLEKIPDEDAELLGINPKVARPEWMVLTVL
PVPPVTVRPSITLETGERSEDDLTHKLVDIIRINQRLKENIEAGAPQLIIEDLWELLQYHVATYFDNELP
GIPPARHRSGRPLKTLAQRLKGKEGRFRGNLSGKRVNFSARTVISPDPNISINEVGVPEQIAKELTVPER
VTPWNIDELREYVLNGPDSWPGANYVIRPDGRRIKIRDENKEELAERLEPGWVVERHLIDGDIVLFNRQP
SLHRMSMMGHKVKVLPGKTFRLNLAVCPPYNADFDGDEMNLHVPQTEEARAEARELMLVEEHILTPRYGG
PIIGGIHDYISGAYLLTHKSTLFTKEEVQTILGVAGYFGDPPEPAIEKPKEYWTGKQIFSAFLPEDLNFE
GRAKICSGSDACKKEECPHDAYVVIKNGKLLKGVIDKKAIGAEKGKILHRIVREYGPEAARRFLDSVTRL
FIRFITLRGFTTGIDDIDIPKEAKEEIEELIEKAEKRVDNLIERYRNGELEPLPGRTVEETLEMKIMEVL
GKARDEAGEVAEKYLDPENHAVIMARTGARGSLLNITQMAAMVGQQSVRGGRIRRGYRNRTLPHFKKGDI
GAKARGFVRSSFKKGLDPTEYFFHAAGGREGLVDTAVRTSQSGYMQRRLINALQDLYVEYDGTVRDTRGN
LIQFKYGEDGVDPMKSDHGKPVDVKKIF
>gnl|CDD|162834 TIGR02391, conserved_hypothetical_protein, TIGR02391 family protein. This family consists of a relatively rare (~ 8 occurrences per 200 genomes) prokaryotic protein family. Genes for members are appear to be associated variously with phage and plasmid regions, restriction system loci, transposons, and housekeeping genes. The function is unknown [Hypothetical proteins, Domain]
LHPKVLGFCREELLLGNYFHAVFEAVKIVEEKIRELTGDSLDGVELIDQAFSSKNNPKVGGNLLQTEAEQ
GEQEGLSNLLAGAITGFRNPVAHAPRYFIDPNIFDAADALQLASLASRLLDRAKQ
>gnl|CDD|274107 TIGR02392, RNA_polymerase_sigma_factor_RpoH, alternative sigma factor RpoH. A sigma factor is a DNA-binding protein protein that binds to the DNA-directed RNA polymerase core to produce the holoenzyme capable of initiating transcription at specific sites. Different sigma factors act in vegetative growth, heat shock, extracytoplasmic functions (ECF), etc. This model represents the clade of sigma factors called RpoH and further restricted to the Proteobacteria. This protein may be called sigma-32, sigma factor H, heat shock sigma factor, and alternative sigma factor RpoH. Note that in some species the single locus rpoH may be replaced by two or more differentially regulated stress response sigma factors [Cellular processes, Adaptations to atypical conditions, Transcription, Transcription factors]
GSLDAYIRAVNRIPMLTPEEEYQLAKRLREHGDLDAAKKLVLSHLRFVVKIARGYRGYGLPQADLIQEGN
IGLMKAVKRFDPERGVRLVSFAVHWIKAEIHEYILRNWRLVKVATTKAQRKLFFNLRKMKKRLQGWLNPE
EVEAIAEELGVSEREVREMESRLSGQDMSLNASIDDDEDDGGAPIAYLVDKRSDPEDTLEEEQWEELQRQ
ALANALGSLDARSRRIIEARWLDDDKLTLQELAAEYGVSAERIRQIEKNAMKKLKAALAA
>gnl|CDD|274108 TIGR02393, RNA_polymerase_sigma_factor_RpoD, RNA polymerase sigma factor RpoD, C-terminal domain. This model represents the well-conserved C-terminal region of the major, essential sigma factor of most bacteria. Members of this clade show considerable variability in domain architecture and molecular weight, as well as in nomenclature: RpoD in E. coli and other Proteobacteria, SigA in Bacillus subtilis and many other Gram-positive bacteria, HrdB in Streptomyces, MysA in Mycobacterium smegmatis, etc [Transcription, Transcription factors]
AKKKLVESNLRLVVSIAKKYTNRGLSFLDLIQEGNIGLMKAVEKFDYRKGYKFSTYATWWIRQAITRAIA
DQARTIRIPVHMVETINKLIKAERQLTQELGREPTDEELAERMGMPAEKVREIKKIAQEPISLETPIGEE
EDSFLGDFIEDESIESPDDAAAKELLREQLDEVLETLTERERKVLRMRYGLLDGRPHTLEEVGKEFNVTR
ERIRQIESKALRKLRHPSRSKKLKDFLD
>gnl|CDD|131447 TIGR02394, RNA_polymerase_sigma_factor_RpoS, RNA polymerase sigma factor RpoS. A sigma factor is a DNA-binding protein protein that binds to the DNA-directed RNA polymerase core to produce the holoenzyme capable of initiating transcription at specific sites. Different sigma factors act in vegetative growth, heat shock, extracytoplasmic functions (ECF), etc. This model represents the clade of sigma factors called RpoS (also called sigma-38, KatF, etc.), found only in Proteobacteria. This sigma factor is induced in stationary phase (in response to the stress of nutrient limitation) and becomes the second prinicipal sigma factor at that time. RpoS is a member of the larger Sigma-70 subfamily (TIGR02937) and most closely related to RpoD (TIGR02393) [Cellular processes, Adaptations to atypical conditions, Transcription, Transcription factors]
EFKKAETETRVADVTQLYLREIGFKPLLTAEEEIAYARRALAGDFEARKVMIESNLRLVVSIAKHYVNRG
LPLLDLIEEGNLGLMHAVEKFDPERGFRFSTYATWWIRQTIERAIMNQARTIRLPVHVIKELNVYLRAAR
QLEKKLGREPSVEEIAELLDKPVEDVSRVLALNERITSLDAPLDDDSSKSLLDTIADEQSIDPESLVQND
DLKQLIEAWLAELNERQREVLARRFGLLGYEPATLEEVAAEVGLTRERVRQIQVEALKKLRRILERDGVD
REALF
>gnl|CDD|274109 TIGR02395, RNA_polymerase_sigma-54_factor, RNA polymerase sigma-54 factor. A sigma factor is a DNA-binding protein protein that binds to the DNA-directed RNA polymerase core to produce the holoenzyme capable of initiating transcription at specific sites. Different sigma factors act in vegetative growth, heat shock, extracytoplasmic functions (ECF), etc. This model represents the clade of sigma factors called sigma-54, or RpoN (unrelated to sigma 70-type factors such as RpoD/SigA). RpoN is responsible for enhancer-dependent transcription, and its presence characteristically is associated with varied panels of activators, most of which are enhancer-binding proteins (but see Brahmachary, et al., ). RpoN may be responsible for transcription of nitrogen fixation genes, flagellins, pilins, etc., and synonyms for the gene symbol rpoN, such as ntrA, reflect these observations [Transcription, Transcription factors]
QSQKLALTQQLQQSIQLLQLSTAELEKYIQQAALENPLLEIRASSAEAFSDSLSSKKSVDASEDEMYTNQ
QSPATESLFEHLLEQLDLLFFTERDRKIALYIIDNLDEDGYLEIDLEEIADELEVSEEEVEKVLELIQRL
DPAGVGARDLQECLLLQLERLDIDDTELAYNILLEHLELLAEKDFRRLAKKLGLSEEELKEALDLIKSLS
PKPGKEFADPEEVEYVIPDVIVTKKNGEWVVELNGRSLPELRINEEYFKLLKDAEKEAADQYLKQKLKEA
RWLIKALEQREETLLKVAEAIVEHQKDFFLGGPAALKPLTLREVAEELGLHESTISRAINNKYLQTPRGV
FELKYFFSRGVSTDSAEGEVSSTAIKALIKELIAAEDKRKPLSDQKIAELLKEKGIKIARRTVAKYREEL
GIPSSSKRK
>gnl|CDD|274110 TIGR02396, conserved_hypothetical_protein, rpsU-divergently transcribed protein. This uncharacterized protein is found in a number of Alphaproteobacteria and, with N-terminal regions long enough to be transit peptides, in eukaryotes. This phylogeny suggests mitochondrial derivation. In several Alphaproteobacteria, the gene for this protein is encoded divergently from rpsU, the gene for ribosomal protein S21. S21 is unusual in being encoded outside the usual long ribosomal protein operons, but rather in contexts that suggest regulation of the initiation of protein translation [Unknown function, General]
KAKLLDAALEHVPFLGWTDEALLLAARDLGYSDSLPGLLPPEGAADLIEFFEDYCDTALLEALKSSDLEG
LKVREKIELAVWIRLKMVIPIIQHLPQALAFLAQPQNLALSLRLLAELSDAIWYLAGDKSTDFNWYTKRA
ILSGVYSSTELFMIQDKSEGFEDTWSFLDSRIKNAVKLQKIKARL
>gnl|CDD|274111 TIGR02397, DNA_polymerase_III_subunit_gamma, DNA polymerase III, subunit gamma and tau. This model represents the well-conserved first ~ 365 amino acids of the translation of the dnaX gene. The full-length product of the dnaX gene in the model bacterium E. coli is the DNA polymerase III tau subunit. A translational frameshift leads to early termination and a truncated protein subunit gamma, about 1/3 shorter than tau and present in roughly equal amounts. This frameshift mechanism is not necessarily universal for species with DNA polymerase III but appears conserved in the exterme thermophile Thermus thermophilis [DNA metabolism, DNA replication, recombination, and repair]
YQVLARKYRPQTFEDVIGQEHIVQTLKNAIKNGRIAHAYLFSGPRGTGKTSIARIFAKALNCQNGPDGEP
CNECESCKEINSGSSLDVIEIDAASNNGVDDIREILDNVKYAPSSGKYKVYIIDEVHMLSKSAFNALLKT
LEEPPEHVVFILATTEPHKIPATILSRCQRFDFKRIPLEDIVERLKKILDKEGIKIEDEALELIARAADG
SLRDALSLLDQLISFGNGKITYEDVNELLGLVDDEKLIELLEAILNKDTAEALKILDEILESGVDPEKFL
EDLIEILRDLLLIKKTPSNLLAVLESEQEFLKELALKLSLEFLLRLLDILLEALKDLRFSNDPRIWLEMT
LLRLL
>gnl|CDD|131451 TIGR02398, Glucosylglycerol-phosphate_synthase, glucosylglycerol-phosphate synthase. Glucosylglycerol-phosphate synthase catalyzes the key step in the biosynthesis of the osmolyte glucosylglycerol. It is known in several cyanobacteria and in Pseudomonas anguilliseptica. The enzyme is closely related to the alpha,alpha-trehalose-phosphate synthase, likewise involved in osmolyte biosynthesis, of E. coli and many other bacteria. A close homolog from Xanthomonas campestris is excluded from this model and scores between trusted and noise
LYHRLPYDEFRGADGKLQRRDPTSPNGIIPTLLSFFGDGRAGTWVAWAEHDENSGETFDSHMTVPAEYKL
TAARIPLSKEQVDIFYHITSKEAFWPILHTFPERFQFREDDWQVFLKVNRAFAEAACLEAAEGATVWVHD
YNLWLVPGYIRQLRPDLKIAFFHHTPFPSADVFNILPWREQIIGSLLCCDYIGFHIPRYVENFVDAARGL
MPLQTVSRQNVDPRFITVGTALGEERMTTALDTGNRVVKLGAHPVGTDPERIRSALAAASIREMMERIRS
ELAGVKLILSAERVDYTKGILEKLNAYERLLERRPELLGKVTLVTACVPAASGMTIYDELQGQIEQAVGR
INGRFARIGWTPLQFFTRSLPYEEVSAWFAMADVMWITPLRDGLNLVAKEYVAAQGLLDGVLVLSEFAGA
AVELKGALLTNPYDPVRMDETIYVALAMPKAEQQARMREMFDAVNYYDVQRWADEFLAAVSPQAQLG
>gnl|CDD|131452 TIGR02399, Glucosylglycerol-phosphate_phosphatase, glucosylglycerol 3-phosphatase. Proteins in this family are glucosylglycerol-phosphate phosphatase, with the gene symbol stpA (Salt Tolerance Protein A). A motif characteristic of acid phosphatases is found, but otherwise this family shows little sequence similarity to other phosphatases. This enzyme acts on the glucosylglycerol phosphate, product of glucosylglycerol phosphate synthase and immediate precursor of the osmoprotectant glucosylglycerol
EIIINTENLLIVQDLDGVCIPLVKDPLTRKLDSKYVFAVKNLEKEFYVLTNGEHEGPRGVNRIVERSLGD
IDQPKEKGLYLPGLAAGGVQYQDNNGNISHPGVSKEEVDFLAAVPDLMRPSLEQIVKKIFPNLVQEEIQT
HASKSVLDTRFSPTINLNSLFDLVKDDSEIRKILQKSFEDLMNELMYKAKTQGLENSFFLHIAPNLGSDN
GNEIIKLASKGDIGTTDIQFMLKGAVKEAGVLFLLNKFIYDSTGIAPLGRNFNFRDAPKSHQELLNLCKK
HIKPEDMPLIIGVGDTVTSQKIPNTNGYSRGGSDRSFLELIQLLGQEFNSNNKVVFVDSSSGEVYRPSLK
IEGLKGISDDEDPLKFDVIFPNGPKEYVAWFIKFAKRRS
>gnl|CDD|274112 TIGR02400, Alphaalpha-trehalose-phosphate_synthase, alpha,alpha-trehalose-phosphate synthase [UDP-forming]. This enzyme catalyzes the key, penultimate step in biosynthesis of trehalose, a compatible solute made as an osmoprotectant in some species in all three domains of life. The gene symbol OtsA stands for osmotically regulated trehalose synthesis A. Trehalose helps protect against both osmotic and thermal stresses, and is made from two glucose subunits. This model excludes glucosylglycerol-phosphate synthase, an enzyme of an analogous osmoprotectant system in many cyanobacterial strains. This model does not identify archaeal examples, as they are more divergent than glucosylglycerol-phosphate synthase. Sequences that score in the gray zone between the trusted and noise cutoffs include a number of yeast multidomain proteins in which the N-terminal domain may be functionally equivalent to this family. The gray zone also includes the OtsA of Cornyebacterium glutamicum (and related species), shown to be responsible for synthesis of only trace amounts of trehalose while the majority is synthesized by the TreYZ pathway; the significance of OtsA in this species is unclear (see Wolf, et al., ) [Cellular processes, Adaptations to atypical conditions]
RLIVVSNRLPVPITRGGLEPSAGGLAVALLGALKATGGVWFGWSGKTVEEDEGEPFLRTELEGKITLAPV
FLSEEDVDGYYNGFSNSTLWPLFHYRPDLIRYDRKAWEAYRRVNRLFAEALAPLLQPGDIVWVHDYHLML
LPAMLRELGVQNKIGFFLHIPFPSSEIYRTLPWRRELLEGLLAYDLVGFQTYDDARNFLSAVSRELGLET
LPNGVESGGRTVRVGAFPIGIDVDRFAEQAKKPSVQKRIAELRESLKGRKLIIGVDRLDYSKGLPERLLA
FERFLEEHPEWRGKVVLVQIAVPSRGDVPEYQQLRRQVEELVGRINGRFGTLDWTPIRYLNRSYDREELM
ALYRAADVGLVTPLRDGMNLVAKEYVAAQDPKDGVLILSEFAGAAQELNGALLVNPYDIDGMADAIARAL
TMPLEEREERHRAMMDKLRKNDVQRWREDFLSDLNS
>gnl|CDD|274113 TIGR02401, Putative_maltooligosyl_trehalose_synthase, malto-oligosyltrehalose synthase. This enzyme, formally named (1-_4)-alpha-D-glucan 1-alpha-D-glucosylmutase, is the TreY enzyme of the TreYZ pathway of trehalose biosynthesis, an alternative to the OtsAB pathway. Trehalose may be incorporated into more complex compounds but is best known as compatible solute. It is one of the most effective osmoprotectants, and unlike the various betaines does not require nitrogen for its synthesis [Energy metabolism, Biosynthesis and degradation of polysaccharides]
PTATYRLQLRAGFTFDDAAALLPYLKSLGVSHLYLSPILTAVPGSTHGYDVVDHSEINPELGGEEGLRRL
SEAARARGLGLIVDIVPNHMAVHLEQNPWWWDVLKNGPSSAYAEYFDIDWDPLGGDGKLLLPILGDQYGA
VLDRGEIKLRFDGDGTLALRYYDHRLPLAPGTLPELEVLEDVPGDGDALKKLLERQHYRLTWWRVAAGEI
NYRRFFDINDLAGVRVEDPAVFDATHRLVLELVAEGLVDGLRIDHIDGLADPEGYLRRLRELVGPARYLV
VEKILAPGEHLPADWPVDGTTGYDFLNEVNGVLVDAAGEEPLTALYRNFTGRPQDIEETLRRAKRLVLRH
LLASEIRRLARLLARLAELDPAARDFTPEALRQALRELLACFPVYRTYLPGGAEIIADAQALAEAIARAR
KEGPPADPGALDFLQDLLLGDDGAPHREFRRRFQQLSGPVMAKGVEDTAFYRYNRLLSLNEVGGDPGRFG
VSIADFHARNAERARRWPRSMTTTSTHDTKRGEDVRARISVLSEIPQEWAEALNRWRALNPGAPDPSDEY
MLYQTLLGAWPIDLNADDALRERIQAYALKALREAKLHTSWTNPNEAYETAVADFVDAVLDPPAGSLFLT
DFVAREKKLIPAGLQNSLSQTLLKLTAPGVPDIYQGTEFWDLSLVDPDNRRPVDYAARRAALLQLTTPNW
SELELWLLDGLVKLAVTAAALQLRREHPELFGQGDYQPLEAGGPGAAHVIAFARGTDRQAAIVVVTRLSL
RLIQTGLPPNGFWRDTALTLPAGAWRDILTGETLSPGAVPLAELFGRFPVALLVR
>gnl|CDD|274114 TIGR02402, Malto-oligosyltrehalose_trehalohydrolase, malto-oligosyltrehalose trehalohydrolase. Members of this family are the trehalose biosynthetic enzyme malto-oligosyltrehalose trehalohydrolase, formally known as 4-alpha-D-{(1-_4)-alpha-D-glucano}trehalose trehalohydrolase (EC 3.2.1.141). It is the TreZ protein of the TreYZ pathway for trehalose biosynthesis, and alternative to the OtsAB system [Energy metabolism, Biosynthesis and degradation of polysaccharides]
VRFRLWAPTAASVKLRLNGALHAMQRNGDGWFEATVPPVGPGTRYGYVLDDGTPVPDPASRRQPDGVHGP
SQVVDPDRYAWQDTGWRGRPLEEAVIYELHVGTFTPEGTFDAAIEKLPYLADLGITAIELMPVAQFPGTR
GWGYDGVLPYAPHEAYGGPDDLKALVDAAHGLGLGVLLDVVYNHFGPEGNYLPRFAPYFTDRYSTPWGAA
INFDGPGSDEVRRYIIDNALYWLREYHFDGLRLDAVHAIADTSAKHFLEELARAVRELAADLRPVHLIAE
SDLNDPSLLTPRADGGYGLDAQWNDDFHHALHVLLTGERQGYYADFADPLAALAKALAEGFVYDGEYSPF
RGRPHGRPSGDLPPHRFVVFIQNHDQVGNRAQGERLSQLLSPGSLKLAAALTLLSPYIPLLFMGEEYGAT
TPFQFFTDHPDPELAEAVREGRKKEFARFGWDPEDVPDPQDPETFLRSKLDWAEAESGEHARWLAFYRDL
LALRRELPVPLLPGARALEVTVDETPGWVAVRWRFGRGELELAANLSTSPVAVP
>gnl|CDD|274115 TIGR02403, Trehalose-6-phosphate_hydrolase, alpha,alpha-phosphotrehalase. Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor
WWQKKVIYQIYPKSFYDSTGDGTGDLRGIIEKLDYLKKLGVDYIWLNPFYVSPQKDNGYDVSDYYAINPL
FGTMADFEELVSEAKKRNIKIMLDMVFNHTSTEHEWFKKALAGDSPYRDFYIWRDPKGKPPTNWQSKFGG
SAWEYFGDTGQYYLHLFDKTQADLNWENPEVREELKDVVNFWRDKGVDGFRLDVINLISKDQFFEDDEIG
DGRRFYTDGPRVHEYLQEMNQEVFGDNDSVTVGEMSSTTIENCIRYSNPENKELSMVFTFHHLKVDYPNG
EKWTLAKFDFAKLKEIFSTWQTGMQAGGGWNALFWNNHDQPRAVSRFGDDGEYRVESAKMLAAAIHLLRG
TPYIYQGEEIGMTNPKFTNIEDYRDVESLNAYDILLKKGKSEEEALAILKQKSRDNSRTPMQWNNEKNAG
FTTGKPWLGVATNYKEINVEKALADDNSIFYFYQKLIALRKSEPVITDGDYQFLLPDDPSVWAYTRTYKN
QKLLVINNFYGEEKTIELPLDLLSGKILLSNYEEAEKDAKLELKPYEAIVLLI
>gnl|CDD|274116 TIGR02404, Trehalose_operon_transcriptional_repressor, trehalose operon repressor, B. subtilis-type. This family consists of repressors of the GntR family typically associated with trehalose utilization operons. Trehalose is imported as trehalose-6-phosphate and then hydrolyzed by alpha,alpha-phosphotrehalase to glucose and glucose-6-P. This family includes repressors mostly from Gram-positive lineages and does not include the TreR from E. coli [Regulatory functions, DNA interactions]
KYEQIYQDLEQKITKGQYKEGDYLPSEHELMDQYGASRETVRKALNLLTERGYIQKIQGKGSIVLNRKQI
EFPISGITSFKELNETLGLDSKTEVVELDKEDPLPETLAQLTGLEEGSLIWRIKRVRVIDGEAVILDIDY
LLKELVPGLTKEIAEDSIYQYLENELGLAISYAQKEITVEPCTDEDKKLLDLDGDDHVVVVKSKTFLEDT
RQFQYTESRHRLDKFKFVDFARR
>gnl|CDD|131458 TIGR02405, HTH-type_transcriptional_regulator_TreR, trehalose operon repressor, proteobacterial. This family consists of repressors of the LacI family typically associated with trehalose utilization operons. Trehalose is imported as trehalose-6-phosphate and then hydrolyzed by alpha,alpha-phosphotrehalase to glucose and glucose-6-P. This family includes repressors mostly from Gammaproteobacteria and does not include the GntR family TreR of Bacillus subtilis [Regulatory functions, DNA interactions]
KLTIKDIARLAGVGKSTVSRVLNNEPKVSIETRERVEQVIQQSGFVPSKSARAMRGGSDKVVAVIVSRLD
SPSENLAVSGMLPVFYTAGYDPIIMESQFSPQLTNEHLSVLQKRNVDGVILFGFTGCDEEILESWNHKAV
VIARDTGGFSSVCYDDYGAIELLMANLYQQGHRHISFLGVDPSDKTTGLMRHNAYLAYCESANLEPIYQT
GQLSHESGYVLTDKVLKPETTALVCATDTLALGAAKYLQELDRSDVQVSSVGNTPLLSFLFPNTVSIDPG
YYEAGKAAASQLIKQLAGCHEVQHLIIPAML
>gnl|CDD|131459 TIGR02406, L-24-diaminobutyric_acid_acetyltransferase, diaminobutyrate acetyltransferase. This enzyme family is the EctA of ectoine biosynthesis. Ectoine is a compatible solute, analagous to trehalose, betaines, etc., found often in halotolerant organisms. EctA is L-2,4-diaminobutyric acid acetyltransferase, also called DABA acetyltransferase [Cellular processes, Adaptations to atypical conditions]
FRPPRIEDGAGIWELVKDCPPLDLNSSYAYLLLCTDFADTSIVAESEGGEIVGFVSGYLRPDRPDVLFVW
QVAVDPRARGKGLARRLLEALLERVACERVRHLETTITPDNQASRALFKALARRRGVHLIEEPFFDGELF
PGGAHDDEWLLRIGPFT
>gnl|CDD|274117 TIGR02407, Diaminobutyrate--2-oxoglutarate_transaminase, diaminobutyrate--2-oxoglutarate aminotransferase. Members of this family of class III pyridoxal-phosphate-dependent aminotransferases are diaminobutyrate--2-oxoglutarate aminotransferase (EC 2.6.1.76) that catalyze the first step in ectoine biosynthesis from L-aspartate beta-semialdehyde. This family is readily separated phylogenetically from enzymes with the same substrate and product but involved in other process such as siderophore (SP|Q9Z3R2) or 1,3-diaminopropane (SP|P44951) biosynthesis. The family TIGR00709 previously included both groups but has now been revised to exclude the ectoine biosynthesis proteins of this family. Ectoine is a compatible solute particularly effective in conferring salt tolerance [Cellular processes, Adaptations to atypical conditions]
DIFEELESEVRSYCRSFPTVFEKAKGSTLWDEDGKEYIDFFAGAGALNYGHNNPKLKQALIDYLADDGII
HSLDMATEAKREFLETFNEIILKPRGLDYKVQFPGPTGTNAVESALKLARKVTGRSNVVSFTNAFHGMTL
GSLSVTGNRFKRQGAGVPLSNVSRMPYDGYLGGDVDTIAYFEKLLEDSSSGVDLPAAVILETVQGEGGIN
VASDEWLQRLEKLCRRHDILLIVDDIQAGCGRTGTFFSFEPAGIEPDIVCLSKSISGYGLPLALTLIKPE
LDVWKPGEHNGTFRGNNLAFVTATAALEYYWSDDAFEKAVQRKSEIIQERLDRIVAEYPELIKQVRGRGL
MQGIECGDGDLAGKIAKAAFENGLIIETSGPNDEVIKLLPPLTIDEETLQQGLDILEQAVEE
>gnl|CDD|131461 TIGR02408, putative_L-proline_4-hydroxylase, ectoine hydroxylase. Both ectoine and hydroxyectoine are compatible solvents that serve as protectants against osmotic and thermal stresses. A number of genomes synthesize ectoine. This enzyme allows conversion of ectoine to hydroxyectoine, which may be more effective for some purposes, and is found in a subset of ectoine-producing organisms
PRQDPVVWGEGKAAGPLSAKQLQSYERDGFLLLENLFSDDEVAALLAEVERMTRDPAIVRDEEAITEPGS
NAVRSIFEVHVLSPILARLVRDPRVANAARQILGSDVYVHQSRINMKPGFKGTGFYWHSDFETWHAEDGM
PSMRAVSCSIALTDNNETNGPLMLVPGSHRTFISCVGETPRDNYKQSLKKQEYGVPDPVSLTKLADQGGI
STFTGKAGSAVWFDCNTMHGSGSNITPWPRSNVFMVFNSVENALNEPFAAPNRRPEHIAARQFKPVR
>gnl|CDD|274118 TIGR02409, Probable_gamma-butyrobetaine_dioxygenase, gamma-butyrobetaine hydroxylase. Members of this protein family are gamma-butyrobetaine hydroxylase, both bacterial and eukarytotic. This enzyme catalyzes the last step in the conversion of lysine to carnitine. Carnitine can serve as a compatible solvent in bacteria and also participates in fatty acid metabolism
LVQILWQDGKESRFPAVWLRDNCPCPDCYLDSNGARKLLVLDIPVEIGIKKLIIDDKGNLVVIFWPDGHL
SEFPADWLKKRCYDKQELRERELFFPEKQRWGKATSELSLPTLDFEAVMRDDSVLLDWLSAVRDVGIVVL
TGAPTKPGAVSKLGKRIGFIRETNYGHLFEVRDKADANNLAYTNGGLPFHTDNPYRDHPPGLQLLHCLES
TVEGGDSEFVDGFAVAEALRKENPEAFRILSSTPVEFRDIGDDYCDLRSKHPVIELDDDGEVVKIRFNNA
SRDTIFDVPVERVQDFYAAYRRFVELIESPRFKFTFKLEPGDLILFDNTRLLHARDAFSATEGKRHLQGC
YADWDGLLSRLRALRQ
>gnl|CDD|274119 TIGR02410, Trimethyllysine_dioxygenase_mitochondrial, trimethyllysine dioxygenase. Members of this family with known function act as trimethyllysine dioxygenase, an enzyme in the pathway for carnitine biosynthesis from lysine. This enzyme is homologous to gamma-butyrobetaine,2-oxoglutarate dioxygenase, which catalyzes the last step in carnitine biosynthesis. Members of this family appear to be eukaryotic only
IFHNVWLRDNCTCQECYHLATHQRLLNSFDITSLSEDIKPATVIIDEDTLRVTWPDGHVSKFKEDWLIRH
SYEPKKEKNVKALILPNRKIYWLAEFNELKDPSVHFKTTYDHTDSTLKSFSKNIYKYGFTFVDNVPVTPE
ATEKLCERISIIRPTHYGGFWDFTSDLSKNDTAYTSLAIDMHTDGTYWDETPGLQLFHCLTHDGTGGETV
LVDGFYCAEQLRKEAPEDFELLTKVPIPHHYSGESDSVFIHPDYPQPVLTLDPSTGELTQIRWNNSDRAV
MDCLNWSSPYDVPKFYKAIRRFNKIITDPDNEIEFKLRPGTVLIFDNWRVLHSRTSFTGYRRMCGCYLTR
DDFLARARLLLF
>gnl|CDD|274120 TIGR02411, Leukotriene_A-4_hydrolase_homolog, leukotriene A-4 hydrolase/aminopeptidase. Members of this family represent a distinctive subset within the zinc metallopeptidase family M1 (pfam01433). The majority of the members of pfam01433 are aminopeptidases, but the sequences in this family for which the function is known are leukotriene A-4 hydrolase. A dual epoxide hydrolase and aminopeptidase activity at the same active site is indicated. The physiological substrate for aminopeptidase activity is not known
DPSSLSNYKDFRTSHTDLNLSVDFTKRKLSGSVTFTLKSLTDNLNKLVLDTSYLDIQKVTINGLPADFAI
GERKEPLGSPLTISLPIATSKNDEFVLNISFSTTPKCTALQWLNPEQTSGKKHPYLFSQCQAIHARSLFP
CQDTPSVKSTYTAEVESPLPVLMSGIRDGETSNDPGKYLFKQKVPIPAYLIAIASGDLASAPIGPRSTVY
SEPEQLEKCQYEFENDTEKFIKTAEDLIFPYEWGQYDLLVLPPSFPYGGMENPNLTFATPTLIAGDRSNV
DVIAHELAHSWSGNLVTNCSWEHFWLNEGWTVYLERRIIGRLYGEKTRHFSALIGWGDLQESVKTLGETP
EFTKLVVDLKDNDPDDAFSSVPYEKGFNFLFYLEQLLGGPAEFDPFLRHYFKKFAYKSLDTYQFKDALYE
YFKDKKKVDKLDAVDWETWLYSPGMPPVKPNFDTTLADECYALADRWVDAAKADDLSSFNAKDIKDFSSH
QLVLFLETLTERGGDWALPEGHIKRLGDIYNFAASKNAEVRFRWFRLAIQAKLEDEYPLLADWLGTVGRM
KFVRPGYRLLNAFVDRDLAIRTFEKFKDSYHPICAMLVKKDL
>gnl|CDD|274121 TIGR02412, Aminopeptidase_N, aminopeptidase N, Streptomyces lividans type. This family is a subset of the members of the zinc metallopeptidase family M1 (pfam01433), with a single member characterized in Streptomyces lividans 66 and designated aminopeptidase N. The spectrum of activity may differ somewhat from the aminopeptidase N clade of E. coli and most other Proteobacteria, well separated phylogenetically within the M1 family. The M1 family also includes leukotriene A-4 hydrolase/aminopeptidase (with a bifunctional active site)
NLTREEARLRASLITVEHYEIALDLTGADEFFATRCVSTNTVRLSEPGADTFLDLLAAQIESVTLNGILD
VAPVYDGSRIPLPGLLTGENTLRVEATRAYTNTGEGLHRFVDPVDGEVYLYTQFEPADARRVFAVFDQPD
LKANFKFSVKAPEDWTVISNSRETDVTPEPADRRWEFPETPKLSTYLTAVAAGPYHSVQDESRSYPLGIY
ARRSLAQYLDADAIFTITRQGLAFFHRKFGYPYPFKKYDQIFVPEFNAGAMENAGCVTFAENFLHRAEAT
RAEKENRAGVILHEMAHMWFGDLVTMRWWNDLWLNESFAEYMGTLASAEATEYTDAWTTFAAQGKQWAYE
ADQLPTTHPIVADVADLADALSNFDGITYAKGASVLKQLVAWVGEEAFFAGVNAYFKRHAFGNATLDDLI
DSLAKASGRDLSAWSDAWLETAGVNTLTPEITTDGGVVSALYPESSGPPRPHRIAIGLYDLDRDDLRRTT
LVPLTISGERTAVPQLVGKRAPALVLLNDDDLTYAKVRLDPTSFDTVLAALSKLPDPLSRAVVWASLWDS
VRDGELSPDDYLSTVFAHVPSETDYAVVQQVLSQLLRAVAAQYAPIADRPALLAVAALACRSLRRAMESG
PDFQLRWLRALALTATDPDSLRRLLSLLDGKIKGLALDPDLRWRIIARLAALGFIDADDIAAELERDNTA
SGEEHAAAARAARPDAAAKREAWQKLVTTDALPNSKQRAIIEGFWQPEQALLLAAYAERYFANLADIWKR
RGPAIAQAISRGLFPATAVNYDTLATADKWLRSQADASPGLRRTLLERRDAAERALRAREA
>gnl|CDD|131466 TIGR02413, Uncharacterized_protein_YrzI, Bacillus tandem small hypothetical protein. Members of this family are very small proteins, about 47 residues each, in the genus Bacillus. Single members are found in Bacillus subtilis and Bacillus halodurans, but arrays of six in tandem in Bacillus cereus and Bacillus anthracis. An EIxxE motif present in most members of this family resembles cleavage sites by the germination protease GPR in a number small, acid-soluble spore proteins (SASP). A role in sporulation is possible
MTFNLFFLTITIQKRKLSEAEIEREQQIEKIMDEVKERQSLYYSHL
>gnl|CDD|274122 TIGR02414, Aminopeptidase_N, aminopeptidase N, Escherichia coli type. The M1 family of zinc metallopeptidases contains a number of distinct, well-separated clades of proteins with aminopeptidase activity. Several are designated aminopeptidase N, EC 3.4.11.2, after the Escherichia coli enzyme, suggesting a similar activity profile (see SP|P04825 for a description of catalytic activity). This family consists of all aminopeptidases closely related to E. coli PepN and presumed to have similar (not identical) function. Nearly all are found in Proteobacteria, but members are found also in Cyanobacteria, plants, and apicomplexan parasites. This family differs greatly in sequence from the family of aminopeptidases typified by Streptomyces lividans PepN (TIGR02412), from the membrane bound aminopeptidase N family in animals, etc [Protein fate, Degradation of proteins, peptides, and glycopeptides]
DYKPPPFLIEKTHLDFDLHEEETVVRARLTVRRNPDGNGAPLVLDGEELKLLSIAIDGKPLAAGDYQLDD
ETLTIASVPESFTLEIETEIHPEENTSLEGLYKSGGNFCTQCEAEGFRRITYFPDRPDVMSRYTVTITAD
KKKYPVLLSNGNKIASGELPDGRHWAEWEDPFPKPSYLFALVAGDLDVLEDTFTTKSGREVALRVYVEEG
NKDKCDHAMESLKKAMKWDEEVFGLEYDLDIFMIVAVDDFNMGAMENKGLNIFNSKYVLADPETATDADY
ERIESVIAHEYFHNWTGNRVTCRDWFQLSLKEGLTVFRDQEFSADMTSRAVKRIEDVRLLRAHQFPEDAG
PMAHPVRPESYVEINNFYTATVYEKGAEVIRMLHTLLGEEGFRKGMDLYFSRHDGQAVTCEDFVAAMEDA
SGRDLNQFRRWYSQAGTPVLEVKENYDAAKKTYTLTVRQSTPPTPGQTEKKPLHIPIAVGLLGPNGRKLM
LSLDGERDTTRVLELTEAEQTFVFEGIAEKPVPSLLRGFSAPVNLEYPYSDEDLLLLLAHDSDPFNRWEA
GQRLARRVILANIARAQGGEELPVDPAFIDALGKLLNDPHLDAAFKALLLALPSEAYLAELMENIDPDAL
HAAREFLRAAIARQLADDLLRLYDALQENGPYSVDPAAAGRRALRNACLSYLSAADDAEIRNLALEQFKS
ADNMTDRLAALSALVHFESDFRERALAAFYQKWKDDPLVMDKWFALQATSPRPDTLERVKALLQHPAFDL
KNPNRVRALIGAFANNNLVRFHDISGSGYRFLADQIIAIDRFNPQVAARLLEPLTRWRKLDPKRQELMKA
ALERIAAEENLSKDVREVVSKAL
>gnl|CDD|131468 TIGR02415, Diacetyl_reductase, acetoin reductases. One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase () [Energy metabolism, Fermentation]
KVALVTGGAQGIGKGIAERLAKDGFAVAVADLNEETAKETAKEINQAGGKAVAYKLDVSDKDQVFSAIDQ
AAEKFGGFDVMVNNAGVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHGGKIINAASIAG
HEGNPILSAYSSTKFAVRGLTQTAAQELAPKGITVNAYCPGIVKTPMWEEIDEETSEIAGKPIGEGFEEF
SSEIALGRPSEPEDVAGLVSFLASEDSDYITGQSILVDGGMVYN
>gnl|CDD|131469 TIGR02416, Carbon_monoxide_dehydrogenase_large_chain, carbon-monoxide dehydrogenase, large subunit. This model represents the large subunits of group of carbon-monoxide dehydrogenases that include molybdenum as part of the enzymatic cofactor. There are various forms of carbon-monoxide dehydrogenase; Salicibacter pomeroyi DSS-3, for example, has two forms. Note that, at least in some species, the active site Cys is modified with a selenium attached to (rather than replacing) the sulfur atom. This is termed selanylcysteine, and created post-translationally, in contrast to selenocysteine incorporation during translation as for many other selenoproteins [Energy metabolism, Other]
EDIRFIQGKGNYVDDVKLPGMLHGDIVRSPHAHARIKSIDTSAAKALPGVFAVLTAADLKPLNLHWMPTL
AGDVQAVLADEKVLFQNQEVAFVVAKDRYVAADAIELVEVDYEPLPVVIDPFKALEPDAPVLREDLKGKT
TGAHGARKHHNHIFRWEIGDKAATDAVFAKAEVVVKQMMTYPRVHPSPLETCGCVASMDPIKGELTLWGT
FQAPHVIRTVVSLISGLPEHKIRVISPDIGGGFGNKVGIYPGYVCAIVASIVLGVPVKWVEDRMENLSTT
SFARDYHMTGELAATKDGKILAMRCNVLADHGAFDACADPSKWPAGFFNICTGSYDIPVAHCAVDGVYTN
KAPGGVAYRCSFRVTEAVYAIERAVDTLAQRLEMDSADLRIKNFIQPEQFPYTAPLGWEYDSGDYPLAMK
KAMDTVDYHQLRAEQAAKRKRGETRELMGIGISFFTEIVGAGPSKNCDILGVGMFDSCEIRIHPTGSAIA
RMGTKSQGQGHETTYAQIIATELGIPAEDIMVEEGDTDTAPYGLGTYGSRSTPVAGAATALAARKIKAKA
QMIAAHMLEVHEGDLEWDVDRFRVKGDPSKFKTMADIAWAAYNSPPPGLEPGLEAVNYYDPPNMTYPFGA
YFCVVDIDVDTGVAKVRRFYALDDCGTRINPMIIEGQIHGGLTEGFAVAMGQEIRFDEQGNVLGASLMDY
FLPTAVETPHWETDHTVTPSPHHPIGAKGVGESPHVGSVPCFSNAVVDAYAFLGVGHIDMPHTAWRVWKV
>gnl|CDD|131470 TIGR02417, Fructose_repressor_Catabolite_repressor/activator., D-fructose-responsive transcription factor. Members of this family belong the lacI helix-turn-helix family (pfam00356) of DNA-binding transcriptional regulators. All members are from the proteobacteria. Characterized members act as positive and negative transcriptional regulators of fructose and sucrose transport and metabolism. Sucrose is a disaccharide composed of fructose and glucose; D-fructose-1-phosphate rather than an intact sucrose moiety has been shown to act as the inducer [Regulatory functions, DNA interactions]
TLSDIAKLAGVSKTTASYVINGKAKEYRISQETVERVMAVVREQGYQPNIHAASLRAGRSRTIGLVIPDL
ENYSYARIAKELEQQCREAGYQLLIACSDDNPDQEKVVIENLLARQVDALIVASCMPPEDAYYQKLQNEG
LPVVALDRSLDDEHFCSVISDDVDAAAELIERLLSQHADEFWYLGAQPELSVSRDRLAGFRQALKQATLE
VEWVYGGNYSRESGYQMFAKLCARLGRLPQALFTTSYTLLEGVLDYMLERPLLDSQLHLATFGDNYLLDF
LPLPINSVAQQHRQLAWHALELALAAIDGKKPEPGQRYIPRTLQIRH
>gnl|CDD|131471 TIGR02418, Acetolactate_synthase_catabolic, acetolactate synthase, catabolic. Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family [Energy metabolism, Fermentation]
GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSG
PGCSNLVTGLATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAF
RAAESGKPGAAFVSLPQDVVDSPVSVKAIPASYAPKLGAAPDDAIDEVAEAIQNAKLPVLLLGLRASSPE
TTEAVRRLLKKTQLPVVETFQGAGAVSRELEDHFFGRVGLFRNQPGDRLLKQADLVITIGYDPIEYEPRN
WNSENDATIVHIDVEPAQIDNNYQPDLELVGDIASTLDLLAERIPGYELPPDALAILEDLKQQREALDRV
PATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARYFRSYRARHLLISNGMQTLGVALPWAIGA
ALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQEEMKYQRSSGVDFGPIDFV
KYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVDYSDNPKLMS
>gnl|CDD|274123 TIGR02419, kDa_protein_in_gpA_5'region, phage/conjugal plasmid C-4 type zinc finger protein, TraR family. Members of this family are putative C4-type zinc finger proteins found almost exclusively in prophage regions, actual phage, or conjugal transfer regions of the Proteobactia. This small protein (about 70 amino acids) appears homologous to but is smaller than DksA (DnaK suppressor protein), found to be critical for regulating transcription of ribosomal RNA [Mobile and extrachromosomal element functions, Prophage functions]
DEFDRAQELEEELLERALAAARAKKVIGPSLRECEDCGEPIPEARREALPGVTRCVSCQEILE
>gnl|CDD|274124 TIGR02420, RNA_polymerase-binding_transcription_factor_DksA, RNA polymerase-binding protein DksA. The model that is the basis for this family describes a small, pleiotropic protein, DksA (DnaK suppressor A), originally named as a multicopy suppressor of temperature sensitivity of dnaKJ mutants. DksA mutants are defective in quorum sensing, virulence, etc. DksA is now understood to bind RNA polymerase directly and modulate its response to small molecules to control the level of transcription of rRNA. Nearly all members of this family are in the Proteobacteria. Whether the closest homologs outside the Proteobacteria function equivalently is unknown. The low value set for the noise cutoff allows identification of possible DksA proteins from outside the proteobacteria. TIGR02419 describes a closely related family of short sequences usually found in prophage regions of proteobacterial genomes or in known phage [Transcription, Transcription factors, Regulatory functions, Small molecule interactions]
MSEAQLEHFRKILLRWKQELLEEADKTLEHLQEESENFPDPADRATQEEERALELRTRDRERKLIKKIDE
ALKRIEDGEYGYCEECGEEIGLRRLEARPTATLCIDCKTL
>gnl|CDD|274125 TIGR02421, conserved_hypothetical_protein, conserved hypothetical protein. Members of this family include a possible metal-binding motif HEXXXH and, nearby, a perfectly conserved motif QEGLA. All members belong to the Proteobacteria, including Agrobacterium tumefaciens and several species of Vibrio and Pseudomonas, and are found in only one copy per chromosome (Vibrio vulnificus, with two chromosomes, has two). The function is unknown
RDRQLQTLVRLLDALKWVTPTNEPFLQSRFRDNPFSYQPEFQYRPLPFDVAETKRELYSLPIDIIRDPPL
GQLYREKQDEYDLVIDLLESIGTATFLYNSLRLYGAPSDALIGNAPFLLELDARAMEEEEQAPVSATEAA
EILQQRLEDYFGEETIRVTLSDDLPAGAMVSGDKLKLNSDAMFSERDLEALIHHEIGVHLLTTLNGRAQP
LRLLSIGLPGYTATQEGLAILAEYLAGSMTPERLRTLALRVVAVDMMLKGADFIQVFRYLTEQYGFDAAQ
AFSITQRVFRGGGFTKDALYLRGFVEVLNHIRQGGELLDLLFVGKTALEDFPVIRELVERGLLVPPKYLP
PFLSKPSALEPLLKFS
>gnl|CDD|131475 TIGR02422, Protocatechuate_34-dioxygenase_beta_chain, protocatechuate 3,4-dioxygenase, beta subunit. This model represents the beta chain of protocatechuate 3,4-dioxygenase. The most closely related family outside this family is that of the alpha chain (TIGR02423), typically encoded in an adjacent locus. This enzyme acts in the degradation of aromatic compounds by way of p-hydroxybenzoate to succinate and acetyl-CoA [Energy metabolism, Other]
HPPALTPDYKTSVLRSPKNALISIPQSLSELTGPVFGHDDLGPIDNDLTLAHGGEPIGERIIVHGRVLDE
DGRPVPNTLVEVWQANAAGRYRHKNDQYLAPLDPNFGGVGRTLTDSDGYYRFRTIKPGPYPWGNHHNAWR
PAHIHFSLFGTSFAQRLITQMYFEGDPLIAYDPIVNSIPDEAARERLIATLDLDNTIPMDALGYRFDIVL
RGRRATPFEN
>gnl|CDD|274126 TIGR02423, Protocatechuate_34-dioxygenase_alpha_chain, protocatechuate 3,4-dioxygenase, alpha subunit. This model represents the alpha chain of protocatechuate 3,4-dioxygenase. The most closely related family outside this family is that of the beta chain (TIGR02422), typically encoded in an adjacent locus. This enzyme acts in the degradation of aromatic compounds by way of p-hydroxybenzoate to succinate and acetyl-CoA [Energy metabolism, Other]
TPSQTVGPYVHIGLTPEQAGTFTQEFGNNLVTPDADGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRY
NSPADLRAPATDPGFRGWGRTGTDESGEFTFETVKPGAVPDRDGVLQAPHINVSVFARGINRRLYTRLYF
DDEAAANASDPVLALVPAERRATLIAKRERDGKVAYRFDIRLQGEGETVFFDV
>gnl|CDD|274127 TIGR02424, TF_pcaQ, pca operon transcription factor PcaQ. Members of this family are LysR-family transcription factors associated with operons for catabolism of protocatechuate. Members occur only in Proteobacteria [Energy metabolism, Other, Regulatory functions, DNA interactions]
TRIKFRHLQCFVEVARQGSVKRAAEALHITQPAVSKTLRELEEILGTPLFERDRRGIRLTRYGELFLRHA
GASLAALRQGVASLSQLGEGEGPTVRIGALPTVAARLMPEVVKRFLARAPRLRVRIMTGPNAYLLDQLRV
GALDLVVGRLGAPETMQGLSFEHLYNEPVVFVVRAGHPLLAAPSLPVASLADYPVLLPPEGSAIRPLAER
LFIACGIPPPPQRIETVSGSFGRRYVQESDAIWIISRGVVALDLADGTLVELPFDTRETGGPVGLCTRPD
TQLSRAAQLFVDALRSAAAA
>gnl|CDD|131478 TIGR02425, putative_gamma-carboxymuconolactone_decarboxylase, 4-carboxymuconolactone decarboxylase. Members of this family are 4-carboxymuconolactone decarboxylase, which catalyzes the third step in the catabolism of protocatechuate (and therefore the fourth step in the catabolism of para-hydroxybenzoate, of 3-hydroxybenzoate, of vanillate, etc.). Most members of this family are encoded within protocatechuate catabolism operons. This protein is sometimes found as a fusion protein with other enzymes of the pathway, as in Rhodococcus opacus, Streptomyces avermitilis, and Caulobacter crescentus [Energy metabolism, Other]
EQERYEQGMQVRRAVLGDAHVDRALAATTDFDQPFQELITEYAWGTVWTRPGLTKRERSLVTIALLAALG
RDEELAMHVRATANTGVTEDDIKEVLLHVAIYAGVPAANHAFALAKEALAEMA
>gnl|CDD|274128 TIGR02426, 3-carboxy-ciscis-muconate_cycloisomerase, 3-carboxy-cis,cis-muconate cycloisomerase. Members of this family are 3-carboxy-cis,cis-muconate cycloisomerase, the enzyme the catalyzes the second step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate [Energy metabolism, Other]
LLDGLFGDPAALELFSDRAFLRAMLDFEAALARAQADAGLIPAEAAAAIEAACAAAAPDLEALAHAAATA
GNPVIPLVKALRKAVAGEAARYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTP
MTGRTLLQQAVPTTFGLKAAGWLAAVLRARDRLAALRTRALPLQFGGAAGTLAALGTRGGAVAAALAARL
GLPLPALPWHTQRDRIAEFGSALALVAGALGKIAGDIALLSQTEVGEVFEAGGGGSSAMPHKRNPVGAAL
LAAAARRVPGLAATLHAALPQEHERSLGGWHAEWETLPELVRLTGGALRQAQVLAEGL
>gnl|CDD|131480 TIGR02427, b-ketoadipate_enol-lactone_hydrolase, 3-oxoadipate enol-lactonase. Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate [Energy metabolism, Other]
RLHYRLDGAADGAPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVL
ALLDHLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAAKIGTPESWNARIAAVRAEGLAALADA
VLERWFTPGFREAHPARLDLYRNMLVRQPPDGYAGCCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPE
LVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAALRDFLR
>gnl|CDD|188219 TIGR02428, 3-oxoadipate_CoA-transferase_subunit_B, 3-oxoacid CoA-transferase, B subunit. Various members of this family are characterized as the B subunits of succinyl-CoA:3-ketoacid-CoA transferase (EC 2.8.3.5), beta-ketoadipate:succinyl-CoA transferase (EC 2.8.3.6), acetyl-CoA:acetoacetate CoA transferase (EC 2.8.3.8), and butyrate-acetoacetate CoA-transferase (EC 2.8.3.9). This represents a very distinct clade with strong sequence conservation within the larger family defined by pfam01144. The A subunit represents a different clade in pfam01144
WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQ
PVTLLPGASYFDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAKRVIVA
MEHTTKDGESKILKECTLPLTGAKCVDRIVTELAVFEVTDGGLILRELAPGVTVEELQAKTEADLII
>gnl|CDD|131482 TIGR02429, 3-oxoadipate_CoA-transferase_subunit_A, 3-oxoacid CoA-transferase, A subunit. Various members of this family are characterized as the A subunits of succinyl-CoA:3-ketoacid-CoA transferase (EC 2.8.3.5), beta-ketoadipate:succinyl-CoA transferase (EC 2.8.3.6), acetyl-CoA:acetoacetate CoA transferase (EC 2.8.3.8), and butyrate-acetoacetate CoA-transferase (EC 2.8.3.9). This represents a very distinct clade with strong sequence conservation within the larger family defined by pfam01144. The B subunit represents a different clade in pfam01144, described by TIGR02428. The two are found in general as tandem genes and occasionally as a fusion
MINKTIESAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQ
VRKLICSFPRQSDSYVFDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEGKETREFD
GKGYVLEYPLPADFALIKAHKADRWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPG
IFVQRVVEVRDA
>gnl|CDD|131483 TIGR02430, Probable_beta-ketoadipyl-CoA_thiolase., 3-oxoadipyl-CoA thiolase. Members of this family are designated beta-ketoadipyl CoA thiolase, an enzyme that acts at the end of pathways for the degradation of protocatechuate (from benzoate and related compounds) and of phenylacetic acid
REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNPQLDWAAIDDVIYGCANQAGEDNRNVARMA
ALLAGLPVSVPGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRSAKIE
DTTIGWRFINPLMKALYGVDSMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIP
QKKGEPTVVDQDEHPRPETTLEGLAKLKPVVRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRAR
ILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIELNEAFAAQALAVLRELGLADDDARVNPNGG
AIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIERV
>gnl|CDD|131484 TIGR02431, p-hydroxybenzoate_hydroxylase_transcriptional, beta-ketoadipate pathway transcriptional regulators, PcaR/PcaU/PobR family. Member of this family are IclR-type transcriptional regulators with similar DNA binding sites, able to bind at least three different metabolites related to protocatechuate metabolism. Beta-ketoadipate is the inducer for PcaR, p-hydroxybenzoate for PobR, and protocatechuate for PcaU [Regulatory functions, DNA interactions]
SRDFVASLARGLAVIEAFGAERPRLTLTDVAEATGLTRAAARRFLLTLVELGYVTSDGRLFWLTPRVLRL
GYAYLSSAPLPKVAQPLLERLSAQTHESCSVAVLDGDEIVYVARSPTHRIMSVGLSVGTRLPAYCTSMGR
VLLAGLDDEELDEYLARSTLQALTPRTITDRDALLAELLAVRAQGYALVDQELELGLRSIAVPIRNARGQ
VVAALNVSTHAARTTPEELVERILPLLLEAARELRQLL
>gnl|CDD|274129 TIGR02432, tRNAIle-lysidine_synthase, tRNA(Ile)-lysidine synthetase, N-terminal domain. The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family (pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer) [Protein synthesis, tRNA and rRNA base modification]
RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEIKKVDVKA
LAKGKKKNLEEAAREARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRILGS
GIQIIRPLLGISKSEIEEYLKENGLPWFEDETNQDDKYLRNRIRHELLP
>gnl|CDD|274130 TIGR02433, tRNAIle-lysidine_synthase, tRNA(Ile)-lysidine synthetase, C-terminal domain. TIGRFAMs model TIGR02432 describes the family of the N-terminal domain of tRNA(Ile)-lysidine synthetase. This family (TIGR02433) describes a small C-terminal domain of about 50 residues present in about half the members of family TIGR02432,and in no other protein. Characterized examples of tRNA(Ile)-lysidine synthetase from E. coli and Bacillus subtilis both contain this domain [Protein synthesis, tRNA and rRNA base modification]
LTVRFRQGGDRIKLLGRKGSKKLKKLFIDAKVPPWLRDRIPLLFYGD
>gnl|CDD|131487 TIGR02434, Precorrin-6A_synthase, precorrin-6A synthase (deacetylating). In the aerobic cobalamin biosythesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A. The first of the four steps is carried out by EC 1.14.13.83, precorrin-3B synthase (CobG), yielding precorrin-3B as the product. This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; EC 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5 and precorrin-6A, respectively. This model identifies CobF in High GC gram positive, alphaproteobacteria and pseudomonas-related species
RTILLIGIGAGDPEQLTLQAVDALNHADVFFVLDKGEQKSDLVALRREICARYVTAPGYRIVEVDDPERD
AGADDYRAAVDDWHAQRADIWAQAIAEELGDDGTGAFLVWGDPSLYDSTLRILERLRALGGVPFDYEVIP
GITSVQALTARHRIPLNRIGEPVQITTGRRLAEGGFPEGDTVVVMLDGEQAFQRVDPEDIDIYWGAYLGT
PDEILISGPLAEVGPRIAELRAQARARHGWIMDTYLLRR
>gnl|CDD|274131 TIGR02435, Precorrin-3B_synthase, precorrin-3B synthase. An iron-sulfur protein. An oxygen atom from dioxygen is incorporated into the macrocycle at C-20. In the aerobic cobalamin biosythesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A. The first of the four steps is carried out by EC 1.14.13.83, precorrin-3B synthase (CobG), yielding precorrin-3B as the product. This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; EC 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5 and precorrin-6A, respectively [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
RRGACPGLLRPMQAGDGLLVRVRLPGGRLTPAQAIGLADLAERLGNGIIEVTARGNLQLRGLTADHDALS
QALLAAGLGAAGAAADDIRNIEVSPLAGIDPGEIADTRPLAAELRAALENERALLELPPKFSVAIDGGGR
LVLLGDTADVRLQALTTGAGVAWVVSLAGISTSARSLVTVAPDAAVPVAVALLRVFVELGGAARGRDLDD
AFLFALALELVEDSRPLIPDAAEGEAPRPAVDAAAPLGLHPQGDAGVTLGAGLALGQLTAAQLRGLAQLA
QALGDGDLRLTPWRALLVLGLPPERADAAQRALAALGLVTSASDPRARIIACTGAPGCASALADTRADAE
ALAAYCEPTAPITVHLSGCAKGCAHPGPAAITLVAAGAGY
>gnl|CDD|274132 TIGR02436, S23_ribosomal_protein, four helix bundle protein. This family describes a protein of unknown function whose structure is a bundle of four long alpha helices. Some of the first members of this family were found encoded in the (atypically large) intervening sequence (IVS) of Leptospira 23S RNA, a region often present in the rRNA gene and removed during rRNA processing without re-ligation. However, this location is not conserved, and naming this protein as a 23S RNA protein is both confusing and inaccurate
VWQKAMDLALEIYKLTKTFPKEELYGLTSQIRRAATSIPANIAEGYGRRSKKDFIRFLSIALGSLAETET
QLELAKDLGYIDEEQYEELLEELEEIIKMLNGLIKSLK
>gnl|CDD|131490 TIGR02437, FadB, fatty oxidation complex, alpha subunit FadB. Members represent alpha subunit of multifunctional enzyme complex of the fatty acid degradation cycle. Activities include: enoyl-CoA hydratase (EC 4.2.1.17), dodecenoyl-CoA delta-isomerase activity (EC 5.3.3.8), 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35), 3-hydroxybutyryl-CoA epimerase (EC 5.1.2.3). A representative is E. coli FadB (SP:P21177). This model excludes the FadJ family represented by SP:P77399 [Fatty acid and phospholipid metabolism, Degradation]
MIYQGKTIQVTALEDGIAELKFDAPGSVNKFDRATLASLDQALDAIKAQSSLKGVILTSGKDAFIVGADI
TEFLGLFALPDAELIQWLLFANSIFNKLEDLPVPTVAAINGIALGGGCECVLATDFRIADDTAKIGLPET
KLGIMPGFGGTVRLPRVIGADNALEWIASGKENRAEDALKVGAVDAVVTADKLGAAALQLLKDAINGKLD
WKAKRQPKLEPLKLSKIEAMMSFTTAKGMVAQVAGPHYPAPMTAVKTIEKAARFGRDKALEIEAKGFVKL
AKTSEAKALIGLFLNDQYVKGKAKKADKIAKDVKQAAVLGAGIMGGGIAYQSASKGTPIVMKDINQHSLD
LGLTEAAKLLNKQVERGRITPAKMAGVLNGITPTLSYAGFDNVDIVVEAVVENPKVKAAVLAEVEQHVRE
DAILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEVIRGEKSSDETIATVVAYASKMGKTPIV
VNDCPGFFVNRVLFPYFGGFSKLLRDGADFVRIDKVMEKQFGWPMGPAYLLDVVGIDTGHHAQAVMAEGF
PDRMGKDGRDAIDALFEAKRLGQKNGKGFYAYEADKKGKPKKLVDSSVLELLKPVVYEQRDFDDEEIIAR
MMIPMINETVRCLEEGIVATAAEADMGLVYGLGFPPFRGGAFRYLDSIGVANFVALADQYAELGALYQVT
AKLREMAKNGQSFY
>gnl|CDD|274133 TIGR02438, catechol_12-dioxygenase, catechol 1,2-dioxygenase, Actinobacterial. Members of this family are catechol 1,2-dioxygenases of the Actinobacteria. They are more closely related to actinobacterial chlorocatechol 1,2-dioxygenases than to proteobacterial catechol 1,2-dioxygenases, and so are built in this separate model. The member from Rhodococcus rhodochrous NCIMB 13259 (GB|AAC33003.1) is described as a homodimer with bound Fe, similarly active on catechol, 3-methylcatechol and 4-methylcatechol
MTTTETAPTAAASGNAATDKFKAERVSADTSKERVAAIARDVLGAINETILKHKVTYDEYNVLKQWLIDV
GEDGEWPLFLDVFVEHSVEEVAYSHRHGTKGSIEGPYYVPNSPELPSKCTMPMREQDEAGTPLVFSGQVT
DLDGNGLAGAKVELWHADDDGFYSQFAPGIPEWNLRGTIIADDEGRFEITTMQPAPYQIPTDGPTGKFIA
AAGGHPWRPAHLHLKVSAPGHELITTQLYFKGGEHVEDDVASAVKPELILDPKPGADGVNEVTYNFVLDP
E
>gnl|CDD|274134 TIGR02439, Catechol_12-dioxygenase_1, catechol 1,2-dioxygenase, proteobacterial. Members of this family known so far are catechol 1,2-dioxygenases of the Proteobacteria. They are distinct from catechol 1,2-dioxygenases and chlorocatechol 1,2-dioxygenases of the Actinobacteria, which are quite similar to each other and resolved by separate models. This enzyme catalyzes intradiol cleavage in which catechol + O2 becomes cis,cis-muconate. Catechol is an intermediate in the catabolism of many different aromatic compounds, as is the alternative intermediate protocatechuate. In Acinetobacter lwoffii, two isozymes are present with abilities, differing somewhat, to act on catechol analogs 3-methylcatechol, 4-methylcatechol, 4-methoxycatechol, and 4-chlorocatechol [Energy metabolism, Other]
NTKEIQAFLKQVAGLDQKGGNARIKQIIHRVLSDLFRAIEDLDITPDEFWSAVDYLNRLGQANEAGLLAA
GLGFEHFLDLRADAADAAAGITGGTPRTIEGPLYVAGAPESQGFARMDDGSESDKGETLILHGTVTDTEG
KPIAGAKVEVWHANSKGNYSHFDKSQSEFNLRRTIITDANGKYRARSIVPSGYGCPPQGPTQQLLNLLGR
HGNRPAHVHFFVSAPGYRKLTTQINIEGDPYLWDDFAFATRDGLVAEATFVEDAAAAQRRGVEGPFAEIT
FDFEL
>gnl|CDD|131493 TIGR02440, FadJ, fatty oxidation complex, alpha subunit FadJ. Members represent alpha subunit of multifunctional enzyme complex of the fatty acid degradation cycle. Plays a minor role in aerobic beta-oxidation of fatty acids. FadJI complex is necessary for anaerobic growth on short-chain acids with nitrate as an electron acceptor. Activities include: enoyl-CoA hydratase (EC 4.2.1.17),3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35), 3-hydroxybutyryl-CoA epimerase (EC 5.1.2.3). A representative is E. coli FadJ (aka YfcX) (SP:P77399). This model excludes the FadB of TIGR02437 equivalog model [Fatty acid and phospholipid metabolism, Degradation]
AFTLTVREDGIAILTIDVPGEKMNTLKAEFADQVSEILSQLKRDKSIRGLVLVSGKPDNFIAGADISMLA
ACQTAGEAKALAQQGQVLFAELEALPIPVVAAIHGACLGGGLELALACHSRVCSDDDKTVLGLPEVQLGL
LPGSGGTQRLPRLIGVSTALDMILTGKQLRAKQALKLGLVDDVVPQSILLDTAVEMALKGKPIRKPLSLQ
ERLLEGTPLGRALLFDQAAKKTAKKTQGNYPAAERILDVVRQGLAQGMQKGLDAEARAFGELVMTPESAA
LRSIFFATTEMKKETGSDATPAKIKKVGILGGGLMGGGIASVTATKAGIPVRIKDINPQGINNALKYAWK
LLDKGVKRRHMTPAERDNQMALITGTTDYRGFKDVDIVIEAVFEDLALKHQMVKDIEQECAAHTIFASNT
SSLPIGQIAAAASRPENVIGLHYFSPVEKMPLVEVIPHAGTSEQTIATTVALAKKQGKTPIVVADKAGFY
VNRILAPYMNEAARLLLEGEPVEHIDKALVKFGFPVGPITLLDEVGIDVGAKISPILEAELGERFKAPAV
FDKLLSDDRKGRKNGKGFYLYGAATKKKAVDESVYGLLGIKPGVDKEASAVAERCVMLMLNEAVRCLDEG
VIRSPRDGDIGAIFGIGFPPFLGGPFRYIDTLGADNVVKILERLQTQYGDRFTPCQRLVAMAAEKQSFY
>gnl|CDD|131494 TIGR02441, fa_ox_alpha_mit, fatty acid oxidation complex, alpha subunit, mitochondrial. Members represent alpha subunit of mitochondrial multifunctional fatty acid degradation enzyme complex. Subunit activities include: enoyl-CoA hydratase (EC 4.2.1.17) & 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35). Some characterization in human (SP:P40939), pig (SP:Q29554), and rat (SP:Q64428). The beta subunit has activity: acetyl-CoA C-acyltransferase (EC 2.3.1.16)
RLFSTSAALMARTHRHYEVKGDVAVVKIDSPNSKVNTLSKELFAEFKEVMNELWTNEAIKSAVLISGKPG
SFVAGADIQMIAACKTAQEVTQLSQEGQEMFERIEKSQKPIVAAISGSCLGGGLELALACHYRIATKDRK
TLLGLPEVMLGLLPGAGGTQRLPKLTGVPAALDMMLTGKKIRADRAKKMGIVDQLVDPLGPGLKPAEENT
IEYLEEVAVKFAQGLANGKLSINRDKGLVHKITQYVMTNPFVRQQVYKTAEDKVMKQTKGLYPAPLKILD
VVRTGYDQGPDAGYEAESKAFGELSMTFESKALIGLFHGQTDCKKNKFGKPQRPVKTLAVLGAGLMGAGI
AQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDSILSNLTPTLDYSGFKNADMVIE
AVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDG
TSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGVDPKKLDKLTTKFGFPVGAAT
LADEVGVDVAEHVAEDLGKAFGERFGGGSAELLSELVKAGFLGRKSGKGIFIYQEGKKGSKKVNSDADEI
LAQYKLPPKAEVSSPEDIQIRLVSRFVNEAVLCLEEGILASPSEGDIGAVFGLGFPPFLGGPFRFVDLYG
ADKLVDKMEKYAAAYGVQFTPCQLLLDHAKSPGKKFY
>gnl|CDD|274135 TIGR02442, Uncharacterized_protein_Rv2850c/MT2916, cobaltochelatase subunit. Cobaltochelatase is responsible for the insertion of cobalt into the corrin ring of coenzyme B12 during its biosynthesis. Two versions have been well described. CbiK/CbiX is a monomeric, anaerobic version which acts early in the biosynthesis (pfam06180). CobNST is a trimeric, ATP-dependent, aerobic version which acts late in the biosynthesis (TIGR02257/TIGR01650/TIGR01651). A number of genomes (actinobacteria, cyanobacteria, betaproteobacteria and pseudomonads) which apparently biosynthesize B12, encode a cobN gene but are demonstrably lacking cobS and cobT. These genomes do, however contain a homolog (modelled here) of the magnesium chelatase subunits BchI/BchD family. Aside from the cyanobacteria (which have a separate magnesium chelatase trimer), these species do not make chlorins, so do not have any use for a magnesium chelatase. Furthermore, in nearly all cases the members of this family are proximal to either CobN itself or other genes involved in cobalt transport or B12 biosynthesis
FPFTAIVGQEDLKLALLLNAVDPRIGGVLIRGEKGTAKSTAARGLAALLPPIDVVAGCPFSCDPDDPEEW
CEECRRKYRPSEQRPVPFVNLPLGATEDRVVGSLDIERALREGEKAFQPGLLAEAHRGILYIDEVNLLDD
HLVDVLLDAAAMGVNRVEREGLSVSHPARFVLIGTMNPEEGDLRPQLLDRFGLCVDVAAPRDPEERVEII
RRRLAFDADPEAFAARWAAEQEELRNRIARARSLLPSVRISDSLIRFISELCIEFGVDGHRADIVMARAA
RALAALDGRRRVTAEDVREAAELVLPHRRRRKPFEQPQGKDEKDLEEKPEEPGPDPEKPDEGEDDAEQSG
PRGHPTPGNDDEKEPDPQEEADGQGSSTDPAGDIFRIRVLAPPQARARGASGRRSRTRSDSRGRYVRARR
NRGPPDDLAVDATLRAAAPHQRARPGAVAVEPEDLREKIRAGRAGNLVIFVVDASGSMAARGRMAAAKGA
VLSLLRDAYQKRDKVALITFRGEEAEVLLPPTSSVELAARRLEELPTGGRTPLAAGLLKAAEVLSNELLR
DDDGRPLLVVITDGRANVADGGEPPTDDARTIAAKLAARGILFVVIDTESGFVRLGLAEDLARALGGEYV
RLD
>gnl|CDD|131496 TIGR02443, Hypothetical_protein_yheV., conserved hypothetical metal-binding protein. Members of this family are small proteins, about 70 residues in length, with a basic triplet near the N-terminus and a probable metal-binding motif CPXCX(18)CXXC. Members are found in various Proteobacteria
KIKKRFIAGAVCPACSAQDTLAMWKENNIELVECVECGYQEQQKDQSVSVHERANEQVI
>gnl|CDD|274136 TIGR02444, conserved_hypothetical_protein, TIGR02444 family protein. Members of this family are bacterial hypothetical proteins, about 160 amino acids in length, found in various Proteobacteria, including members of the genera Pseudomonas and Vibrio. The C-terminal region is poorly conserved and is not included in the model [Hypothetical proteins, Conserved]
LEALWDFSLDYYARPGVAEACLALQDNFGGNVNLLLLFLWLAERGLAFDEQEIAQVQACAGTWSEDVVRP
LRAVRRQLKQHLPDTPEEINAALRAAVKALELQGEKLLQSDLEALI
>gnl|CDD|131498 TIGR02445, 3-ketoacyl-CoA_thiolase, fatty oxidation complex, beta subunit FadA. This subunit of the FadBA complex has acetyl-CoA C-acyltransferase (EC 2.3.1.16) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit. This protein is almost always located adjacent to FadB (TIGR02437). The FadBA complex is the major complex active for beta-oxidation of fatty acids in E. coli [Fatty acid and phospholipid metabolism, Degradation]
DVVIVDFGRTPMGRSKGGAFRNTRAEDLSAHLMSKLLARNPKVDPAEVEDIYWGCVQQTLEQGFNIARNA
ALLAQIPHTSAAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMMHGVDFHPGMSLHVAK
AAGMMGLTAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRP
ETTVESLAALRPAFDPKNGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGY
GPVPATQKALKRAGLSISDIDVFELNEAFAAQALPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGARI
STTLLNLMEQKDATFGLATMCIGLGQGIATVFERV
>gnl|CDD|131499 TIGR02446, 3-ketoacyl-CoA_thiolase, fatty oxidation complex, beta subunit FadI. This subunit of the FadJI complex has acetyl-CoA C-acyltransferase (EC 2.3.1.16) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit, and YfcY. This protein is almost always located adjacent to FadJ (TIGR02440). The FadJI complex is needed for anaerobic beta-oxidation of short-chain fatty acids in E. coli [Fatty acid and phospholipid metabolism, Degradation]
VKTRQGERIAIVAGLRTPFARQATAFHGIPAVDLGKMVVSELLARSEIDPKLIEQLVFGQVVQMPEAPNI
AREIVLGTGMNVHTDAYSVTRACATSFQSAVNVAESIMAGAIDIGIAGGADSSSVLPIGVSKKLAASLVD
LNKARTLGQKLKVFSRLGLKDLMPVPPAVAEYSTGLSMGQTAEQMAKTYGITRAEQDALAHRSHTLASQA
WRDGKLAGEVMTAFPPPYKQWIAEDNNIRHNSTLAGYAKLRPAFDRKHGSVTAANSTPLTDGAAAVILMR
EGRAKELGMEPLGYIRSYAFTAIDVWQDMLMGPSYATPLALQRAGLALSDLTLIDMHEAFAAQTLANVQM
FASDKFAQENLGRSKAMGEIDMSKFNVLGGSIAYGHPFAATGARMITQTLRELKRRGGGLGLNTACAAGG
LGAAMILEVE
>gnl|CDD|131500 TIGR02447, conserved_hypothetical_protein, thioesterase domain, putative. This family consists of a broadly distributed uncharacterized domain found often as a standalone protein. The member from Shewanella oneidensis, PDB|1T82_A (Forouhar, et al., unpublished) is described from crystallography work as a putative thioesterase. About half of the members of this family are fused to an Acetyltransf_1 domain (pfam00583). The function of this protein is unknown
YLHSAIPLSEAMGIAVSSYTGGELRLSAPLAANINHHGTMFGGSLYTLATLSGWGLLWLRLQELGIDGDI
VIADSHIRYLAPVTGDPVANCEAPDLESWEAFLATLQRGGKARVKLEAQISSDGKLAATFSGEYVALP
>gnl|CDD|274137 TIGR02448, conserved_hypothetical_protein, conserverd hypothetical protein. This family consists of small hypothetical proteins, about 100 amino acids in length. The family includes five members (three in tandem) in Pseudomonas aeruginosa PAO1, and also in Pseudomonas putida KT2440, four in Pseudomonas syringae DC3000, and single members in several other Proteobacteria. The function is unknown
MRRKLLLAAALLLSLAMGAAAASFDATTRAVAASGAVTSDSTSSFRDDKLVIAARDDAASFVASDGAIRG
ARLEAALRQLRSDNPALQASDMELAQAILAQ
>gnl|CDD|131502 TIGR02449, conserved_hypothetical_protein, TIGR02449 family protein. Members of this family are small proteins, typically 73 amino acids in length, with single copies in each of several Proteobacteria, including Xylella fastidiosa, Pseudomonas aeruginosa, and Xanthomonas campestris. The function is unknown
ELQALAAQVEHLLEYLERLKSENRLLRAQEKTWREERAQLLEKNEQARQKVEAMITRLKALEQHT
>gnl|CDD|131503 TIGR02450, hypothetical_protein, tryptophan-rich conserved hypothetical protein. Members of this family are small hypothetical proteins of 60 to 100 residues from Cyanobacteria and some Proteobacteria. Prochlorococcus marinus strains have two members, other species one only. Interestingly, of the eight most conserved residues, four are aromatic and three are invariant tryptophans. It appears all species that encode this protein can synthesize tryptophan de novo
LGSKWTSATPINGERHFVVVNYGDEGGQVWVEMVSVVDVKISFRVNWQDLKDPDLWRPGWK
>gnl|CDD|131504 TIGR02451, Anti-sigma-E_factor_ChrR, anti-sigma factor, putative, ChrR family. The member of this family from Rhodobacter sphaeroides has been shown both to form a complex with sigma(E) and to negatively regulate tetrapyrrole biosynthesis. This protein likely contains (at least) two distinct functional domains; several smaller homologs (excluded by the model) show homology only to the C-terminal, including a motif PxHxHxGxE [Regulatory functions, Other]
HHPSDELLLAYAAGTLDSASSLVVATHLALCPECRARIAAFEALGGSLLEDLEPSALWPGMLDNVMALLD
QQEESEPYIESTVRLPRADIRIRLPEVLRDYVGGPWRWRGPGGRVSRVTLPIDDGNARVRLLYIEAGQSI
PQHTHKGFELTLVLHGAFSDETGVYGVGDFEEADGSVQHQPRTVSGGDCLCLAVLDAPLRFTGGFARLLQ
PFFKG
>gnl|CDD|131505 TIGR02452, conserved_hypothetical_protein, TIGR02452 family protein. Members of this uncharacterized protein family are found in Streptomyces, Nostoc sp. PCC 7120, Clostridium acetobutylicum, Lactobacillus johnsonii NCC 533, Deinococcus radiodurans, and Pirellula sp. for a broad but sparse phylogenetic distibution that at least suggests lateral gene transfer
TIAQNTLNILNAGKYIDDDTEKVDIATFTDRAIQGTKLYDPQEEEVLFLYPAHHRTELKVVNESTLHAAV
RLKESYFAGKVALLNFASAKNPGGGFLNGAQAQEESLCRASALYPCLIKFNEYYEFHRHQRSPLYSDRAI
YSPNVPVFRNDDGDLLNEPFLASFITSPAPNARPVARLYPISYEEIPMTLKNRMYKVLNIAEDQNIDALV
LGAWGCGVFGNDPAEVAKIFHDLLSPGGIFKGRIKEVVFAILDRHGQSTNTQIFRR
>gnl|CDD|274138 TIGR02453, conserved_hypothetical_protein, TIGR02453 family protein. Members of this family are widely (though sparsely) distributed bacterial proteins about 230 residues in length. All members have a motif RxxRDxRFxxx[DN]KxxY. The function of this protein family is unknown. In several fungi, this model identifies a conserved region of a longer protein. Therefore, it may be incorrect to speculate that all members share a common function
FTPEALAFLKALAANNNREWFEENRDRYEQELRQPFEDLIEQLIARLAKISPELRGDAKKGSLFRIYRDV
RFSKDKTPYKTHLGALISHKGKDLEAPGFYIHLQPDGCFAGGGLWGPEAETLAAIRAAIAENPDGWRAAV
AALKFLRGFGLSGEKLKRAPKGFDKDHPLIDWLRRKDFVVWKKLPDEELTGNDLVERIADAFERLRPLMD
YLNAAIE
>gnl|CDD|274139 TIGR02454, Uncharacterized_protein_MJ1089, cobalt ECF transporter T component CbiQ. This model represents the CbiQ component of the cobalt-specific ECF-type. CbiQ is now recognized as the T component of energy-coupling factor (ECF)-type transporters. The S component confers specificity (CbiM-N for cobalt systems), which CbiO is the ABC-family ATPase. In general, proteins found by this model reside next to the other putative subunits of the complex, identified as CbiN, CbiO, or CbiM. Note that the designation of cobalt transporter has been spread excessively among ECF system transporters with many other specificities [Transport and binding proteins, Cations and iron carrying compounds]
LDPRVKLISALALLVLAVLLPNPIALLILAIFALLLVGLAGIPLRILLKRLAVPIGFLLVGLLLLLFSNG
TPGEPLLVLGPLLSITREGLVYALTLALRSLTSLSAVYLLALTTPFPELLSALRRLGVPPLLVEILLLTY
RYLFVLLEELRRMLLAQRSRLGYRSLMRGWRSLGALAGALFIRSLERAERVYLAMESR
>gnl|CDD|131508 TIGR02455, trehalose_synthase_putative, trehalose synthase, Pseudomonas stutzeri type. Trehalose synthase catalyzes a one-step conversion of maltose to trehalose. This is an alternative to the OtsAB and TreYZ pathways. This family includes a characterized example from Pseudomonas stutzeri plus very closely related sequences from other Pseudomonads. Cutoff scores are set to find a more distantly related sequence from Desulfovibrio vulgaris, likely to be functionally equivalent, between trusted and noise limits [Energy metabolism, Biosynthesis and degradation of polysaccharides, Cellular processes, Adaptations to atypical conditions]
MSIPDNSYIEWLEDQAMLHAAQDRARHYAGQARLWQQPYAEAQPRDASAIASVWFTAYPAAIIAPEGCSV
LEALADDALWKALSEIGVQGIHNGPIKLSGGIRGREFTPSIDGNFDRISFDIDPLLGSEEELIQLSRMAA
AHNAITIDDIIPAHTGKGADFRLAELAHGDYPGLYHMVEIREEDWALLPEVPAGRDAVNLLPAQCDELKA
KHYIVGQLQRVIFFEPGIKDTDWSATGEITGVDGKTRRWVYLHYFKEGQPSLNWLDPTFAAQQLIIGDAL
HAIDCLGARGLRLDANGFLGVERRAEGTAWSEGHPLSLTGNQLIAGAIRKAGGFSFQELNLTIDDIAAMS
HGGADLSYDFITRPAYHHALLTGDTEFLRLMLKEMHAFGIDPASLIHALQNHDELTLELVHFWTLHAHDH
YHYKGQTLPGGHLREHIREEIYERLSGEHAPYNLKFVTNGIACTTASLIAAALGIRDLDAIGPADIELIK
KLHILLVMFNAMQPGVFALSGWDLVGALPLAAEAVAELMGDGDTRWIHRGGYDLADLAPEAEASAEGLPK
ARALYGSLAEQLDEPDSFACKLKKILAVRQAYDIAASKQILIPDVQAPGLLVMVHELPAGKGIQITALNF
GADAIAEEICLPGFAPGPVVDIIHESVEGDLTDDCELMINLDPYEALALRIVNAAGHV
>gnl|CDD|274140 TIGR02456, Trehalose_synthase, trehalose synthase. Trehalose synthase interconverts maltose and alpha, alpha-trehalose by transglucosylation. This is one of at least three mechanisms for biosynthesis of trehalose, an important and widespread compatible solute. However, it is not driven by phosphate activation of sugars and its physiological role may tend toward trehalose degradation. This view is accentuated by numerous examples of fusion to a probable maltokinase domain. The sequence region described by this model is found both as the whole of a trehalose synthase and as the N-terminal region of a larger fusion protein that includes trehalose synthase activity. Several of these fused trehalose synthases have a domain homologous to proteins with maltokinase activity from Actinoplanes missouriensis and Streptomyces coelicolor () [Energy metabolism, Biosynthesis and degradation of polysaccharides]
LWYKDAVFYEVHVRSFFDSNGDGIGDFPGLTSKLDYLKWLGVDALWLLPFFQSPLRDDGYDVSDYRAILP
EFGTIDDFKDFVDEAHARGMRVIIDLVLNHTSDQHPWFQEARSNPDGPYRDFYVWSDTDEKYKDTRIIFV
DTEKSNWTFDPVAKQYYWHRFFSHQPDLNYDNPAVHDAVHDVMRFWLDLGVDGFRLDAVPYLYEREGTSC
ENLPETHEFLKRLRKMVDREYPGRMLLAEANQWPEEVVAYFGDEGDPECHMAFNFPVMPRIFMALRREDR
SPIIDILKETPDIPDSCQWCIFLRNHDELTLEMVTDEERDFMYAAYAPDPRMRINLGIRRRLAPLLDNDR
RRIELLTALLLSLPGSPILYYGDEIGMGDNIWLGDRNGVRTPMQWSPDRNAGFSSADPGQLFLPPVQDPV
YGYQQVNVEAQLRDPSSLLHWTRRVLHVRKAHPAFGRGSLTFLPTGNRRVLAFLREYEGERVLCVFNFSR
NPQAVELDLSEFAGRVPVELIGGAPFPPVGGDGYLLTLGPHGFYWFRLE
>gnl|CDD|274141 TIGR02457, trehalose_synthase, trehalose synthase-fused probable maltokinase. Three pathways for the biosynthesis of trehalose, an osmoprotectant that in some species is also a precursor of certain cell wall glycolipids. Trehalose synthase, TreS, can interconvert maltose and trehalose, but while the equilibrium may favor trehalose, physiological concentrations of trehalose may be much greater than that of maltose and TreS may act largely in its degradation. This model describes a domain found only as a C-terminal fusion to TreS proteins. The most closely related proteins outside this family, Pep2 of Streptomyces coelicolor and Mak1 of Actinoplanes missouriensis, have known maltokinase activity. We suggest this domain acts as a maltokinase and helps drive conversion of trehalose to maltose [Energy metabolism, Biosynthesis and degradation of polysaccharides]
ALPELETLVLREGSWWETLALPSLDTLEEDVLPAYLKRRRWFAGKARPIISVRLTDTVPLPGDEPFPIAE
LEVAYDDGPPERYQLPVAFLWVEETPRALAEQLALARVRRGAEEGTLTDAFADEPFRRALLAALLAGRRL
PGAGGSLIGRLEFEATPRLASLAIMEPPEVRLLSAEQSNSSLVVGDRVVLKLYRKVEPGINPEIEMGRYL
TAAGYANIPPLLGSVERVGGDQAPHTLGLLQGYVQNQGDAWRWTLGHLKRYIEEQLSPCANGALAPTLIG
AGYLEFAGLLGRRLAELHLALAAGGEDPAFAPEPISTLYQRSWYQDMRAQAERALQLLAQSRDGLPAAAR
ALADRLLAQRKELAAHLRPLVKREIDGLKIRIHGDFHLGQVLVVQDDAVLIDFEGEPARPLAERRAKRSP
LRDVAGMLRSFDYAAAVALRRAAAAGAPEDRPALEAWAEQFRYRAGQAFLAAYREAMDASPLVPTEPRDA
EALLRLFLLEKAAYELCYELANRPEWLPVPLNGLLRLL
>gnl|CDD|274142 TIGR02458, conserved_hypothetical_protein, cobalt transporter subunit CbtA (proposed). This model represents a family of proteins which have been proposed to act as cobalt transporters acting in concert with vitamin B12 biosynthesis systems. Evidence for this assignment includes 1) prediction of five trans-membrane segments, 2) positional gene linkage with known B12 biosynthesis genes, 3) upstream proximity of B12 transcriptional regulatory sites, 4) the absence of other known cobalt import systems and 5) the obligate co-localization with a small protein (CbtB) having a single additional trans-membrane segment and a C-terminal histidine-rich motif likely to be a metal-binding site
ILFAALFAGLLAGLLATLLQALFTVPLILQAETYETAELAALSHEHAEAASAVPAHPHAEEAWAPADGFQ
RTAFTVVANLVTGVGYALVLVALMSLAGRAITWRQGLLWGLAGFAAFHLAPGLGLPPELPGMPAADLTAR
QIWWIATVAATGIGLYLIAFRGNLWAKLLALVLIVAPHLIGAPQPESFASPVPEALAAQFAVAALATNLV
FWAVIGLAAGWFWQR
>gnl|CDD|131512 TIGR02459, conserved_hypothetical_protein, cobalt transporter subunit CbtB (proposed). This model represents a family of proteins which have been proposed to act as cobalt transporters acting in concert with vitamin B12 biosynthesis systems. Evidence for this assignment includes 1) prediction of a single trans-membrane segment and a C-terminal histidine-rich motif likely to be a metal-binding site, 2) positional gene linkage with known B12 biosynthesis genes, 3) upstream proximity of B12 transcriptional regulatory sites, 4) the absence of other known cobalt import systems and 5) the obligate co-localization with a protein (CbtA) predicted to have five additional trans-membrane segments
MSTNSLTSSAASSVSAARLAAALVAALLGLFLVYFVGFSHIDAVHNAAHDTRHSAAFPCH
>gnl|CDD|162866 TIGR02460, Mannosyl-3-phosphoglycerate_synthase, mannosyl-3-phosphoglycerate synthase. This family consists of examples of mannosyl-3-phosphoglycerate synthase (MPGS), which together mannosyl-3-phosphoglycerate phosphatase (MPGP) comprises a two-step pathway for mannosylglycerate biosynthesis. Mannosylglycerate is a compatible solute that tends to be restricted to extreme thermophiles of archaea and bacteria. Note that in Rhodothermus marinus, this pathway is one of two; the other is condensation of GDP-mannose with D-glycerate by mannosylglycerate synthase
LLEAPNYTERFGAVRIHEVQRVLELDSGTPKSPIYTLSNIDREELYDLLGKTAIVVPVKNEKLHLLEGVL
SGIPHECPIIVVSNSKREPPDRFKMEVDLIRHFSNLTHRKIIIIHQKDPALAEALKEVGYTSILGENGLV
RSGKGEGMLLGLLLAAAIGAEYVGFVDADNYFPGAVNEYVKIYAAGFLMATSPYSMVRIHWRYKPKLTKG
TLYFRKWGRVSEITNHYLNLLISEHTGFETDIIKTGNAGEHALTMKLAEILPFSSGYAVEPYELVYILER
FGGWLPVEEKDVFDQGIEIFQIETLNPHFHEEKGDEHIAEMLLLSLATIYHSKLATEEVRKRILDDLRDL
GILGENEEPPKPLVYRPIKEIPIKEFADFVE
>gnl|CDD|131514 TIGR02461, Mannosyl-3-phosphoglycerate_phosphatase, mannosyl-3-phosphoglycerate phosphatase. Members of this family are mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70). It acts sequentially after mannosyl-3-phosphoglycerate synthase (EC 2.4.1.217) in a two-step pathway of biosynthesis of the compatible solute mannosylglycerate, a typical osmolyte of thermophiles
VIFTDLDGTLLDPGYEPGPAREALEELKDLGFPIVFVSSKTRAEQEYYREELGVEPPFIVENGGAIYIPR
GYFPFPVGAGREVGNYEVIELGKPYAKIRAALKEAENEAGIKGYGDSTAEEVARLTGLPREAARLAKRRE
YSETIFLWSREGWEAVLVTARARGLEYTHGGRFYTVHGGSDKGKAIKRLLDLYKLRPGAIESVGLGDSEN
DFPMFEAVDLAFLVG
>gnl|CDD|274143 TIGR02462, Pyranose_2-oxidase, pyranose oxidase. Pyranose oxidase (also called glucose 2-oxidase) converts D-glucose and molecular oxygen to 2-dehydro-D-glucose and hydrogen peroxide. Peroxide production is believed to be important to the wood rot fungi in which this enzyme is found for lignin degradation
YDVFIAGSGPIGCTYARLCVDAGLKVAMVEIGAADSFTKIVPGAHKKNEIEYQKDIDKFVNVIKGALQSV
SIPVSNLVIPTLDPTAWSASLDSFFVSNGKNPEQDPFRNLSGEAVTRGVGGMSTHWTCATPRFHREERPK
LSDDAAEDDAEWDRLYTKAKSLIGTSTDQFDESIRHNLVLRKLQDEYKGQRDFQPLPLACHRRTDPTYVE
WHSADTVLDLQPNDDAPRERFTLLTNHRCTKLVRNHYNESEVEAALVRDLLSGDSDEEIKADSYVLACGA
VHTAQILVNSGIGQLGRPDPTNPPPLLPSLGRYITEQSMTFCQIVLSTSLVDSVRSDPWGLDWWKEKVAN
HMMKHPEDPLPIPFRDPEPQVTIPFTEEHPWHVQIHRDAFSYGAVGPSIDSRVIVDLRFFGRTEPKEENK
LVFQDKVTDAYNMPQPTFDFRFSAADSKRARRMMTDMCNVAAKIGGYLPGSLPQFMEPGLALHLAGTTRI
GFDEQKTVANTDSKVHNFKNLYVGGNGNIPTAFAANPTLTSMCYAIKSAEYIINNFG
>gnl|CDD|131516 TIGR02463, Putative_mannosyl-3-phosphoglycerate_phosphatase, mannosyl-3-phosphoglycerate phosphatase-related protein. This family consists of members of the HAD superfamily, subfamily IIB. All members are closely related to mannosyl-3-phosphoglycerate phosphatase, the second enzyme in a two-step pathway for biosynthesis of mannosylglycerate, a compatible solute present in some thermophiles and in Dehalococcoides ethenogenes. However, members of this family are separable in a neighbor-joining tree constructed from a multiple sequence alignment and are found only in mesophiles that lack the companion mannosyl-3-phosphoglycerate synthase (TIGR02460). Members of this family are like to act on a compound related to yet distinct from mannosyl-3-phosphoglycerate [Unknown function, General]
WVFSDLDGTLLDSHSYDWQPAAPWLTRLQEAGIPVILCTSKTAAEVEYLQKALGLTGDPYIAENGAAIHL
EELWREEPGYPRIILGISYGIIRLVLETLSEELHFKFTPFDDLSDAEIAELTGLSGSQAALAQDREASVP
LLWRDSDSRMPRFTALLADLGLAIVQGNRFSHVLGASSSKGKAANWLKATYNQPDVKTLGLGDGPNDLPL
LEVADYAVVIK
>gnl|CDD|274144 TIGR02464, Swarming_motility_protein_YbiA, conserved hypothetical protein, ribA/ribD-fused. This model describes a sequence region that occurs in at least three different polypeptide contexts. It is found fused to GTP cyclohydrolase II, the RibA of riboflavin biosynthesis (TIGR00505), as in Vibrio vulnificus. It is found fused to riboflavin biosynthesis protein RibD (TIGR00326) in rice and Arabidopsis. It occurs as a standalone protein in a number of bacterial species in varied contexts, including single gene operons and bacteriophage genomes. The member from E. coli currently is named YbiA. The function(s) of members of this family is unknown
ILFYGTWDTYGCFSNFYPSPFTVDGVTFPTSEHYYMAQKARLFGDEEIAEEILEAKTPEEAKRLGRKVRG
FLEKQWDQVKYEVMRRALLAKFSTHADLREILLSTGGKKLVEASPNDKIWGIGLDAQDARIPRNWKGKNL
LGKLLMEVREELR
>gnl|CDD|131518 TIGR02465, 12-dioxygenase_From_Rhodococcus_Opacus, chlorocatechol 1,2-dioxygenase. Members of this protein family are chlorocatechol 1,2-dioxygenase. This protein is closely related to catechol 1,2-dioxygenase, TIGR02439, EC 1.13.11.1. Note that annotated database entries have appeared for the present protein family with the EC number that refers to that of family TIGR02439. This protein acts in pathways of the biodegradation of chlorinated aromatic compounds
NNRVKEVVDDIVEAVRDVLVRHEVTFDEYRTGVQYLMKVAEAGETPLLLDVFFNSTIDEIENRKSRGSTS
AIQGPYFLEGAPLVEGTLKTYDTDDHKPLLIRGTVRDLSGTPVAGAVIDVWHSTPDGKYSGFHDNIPDDY
YRGKLVTAADGSYEVRTTMPVPYQIPDAGPTGALLETMGRHSWRPAHVHYKVRADGYRPLTTQAYFEGGP
YIDDDCCNGVKSELITPEVIEGGVRVMEFNFVLEPA
>gnl|CDD|274145 TIGR02466, hypothetical_protein_predicted_by_Glimmer/Critica, conserved hypothetical protein. This family consists of uncharacterized proteins in Caulobacter crescentus CB15, Bdellovibrio bacteriovorus HD100, Synechococcus sp. WH 8102, Silicibacter pomeroyi DSS-3, and Hyphomonas neptunium ATCC 15444. The context of nearby genes differs substantially between members and does point to any specific biological role [Hypothetical proteins, Conserved]
RSLFPTPVYQADLTEGPADLNKALDQSLYSIAEDDEAGQEWSNRNGLGGYTSYASLLDLPHRFPEFAELV
QQLDKHVAKFARDLEGDNDGLELRIQKAWVNILPQGGTHSPHLHPGSVISGTYYVQTPENCGAIKFEDPR
LDDMMAAPMRIPNAKRAVQRFVYVPPQEGRVLLFESWLRHEVPPNESEEERISVSFNYAWV
>gnl|CDD|274146 TIGR02467, Probable_cobalt-precorrin-7_C5-methyltransferase, precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit. This model recognizes the CbiE methylase which is responsible, in part (along with CbiT), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiT subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL
VVGIGPGGPELLTPAAIEAIRKADLVVGGERHLELLAELIGEKREIILTYKDLDELLEFIAATRKEKRVV
VLASGDPLFYGIGRTLAERLGKERLEIIPGISSVQYAFARLGLPWQDAVVISLHGRELDELLLALLRGHR
KVAVLTDPRNGPAEIARELIELGIGGSYELTVGENLGYEDERITEGTLEEIAAAQFDFSPLLVV
>gnl|CDD|274147 TIGR02468, Probable_sucrose-phosphate_synthase, sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant. Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein
MAGNDWINSYLEAILDVGPGLDDAKSSALLLLRERGRFSPTRYFVEEVITGFDETDLHRTWVKAVATRSP
QERNTRLENMCWRIWNLARKKKQLEWEEAQRLAKRRLERERGRREATADMSEDLSEGEKGDVAGDISVAG
GEPSTKGRLPRISSNLEMETWSDQQKEKKLYIVLISLHGLVRGENMELGRDSDTGGQVKYVVELARALGS
MPGVYRVDLLTRQVSSPDVDWSYGEPTEMLTPRSSENDGDEMGESSGAYIIRIPFGPRDKYIPKEELWPY
IPEFVDGALSHIVNMSKVLGEQIGSGHPVWPYVIHGHYADAGDSAALLSGALNVPMVLTGHSLGRDKLEQ
LLKQGRMSKEEINSTYKIMRRIEAEELSLDASEIVITSTRQEIEEQWGLYDGFDVILERKLRARARRGVS
CYGRFMPRMAVIPPGMEFSHIVPHDGDMDGETEGNEEHPAKPDPPIWSEIMRFFTNPRKPMILALARPDP
KKNITTLVKAFGECRPLRELANLTLIMGNRDDIDEMSSGSSSVLTSVLKLIDKYDLYGQVAYPKHHKQSD
VPDIYRLAAKTKGVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADA
LLKLVADKQLWAECRQNGLKNIHLFSWPEHCKTYLSRIASCRPRHPQWQRDTDDGEEASEDESPGDSLRD
IQDISLNLSVDGDKESNNGSSNVEGSGPPADRVAKIENAVRSWSKSPKGSSAKAQQGSGAGKYPALRRRK
RLFVIAVDCYDDKDLLQIIKNIFEAVRKERMEGSSGFILSTSMTISEIQSFLKSGGLNPTDFDALICNSG
SELYYPSLNGSEEGKLVADQDYHSHIEYRWGGEGLRKTLVKWAASINEKKGENEEQIVEEDEESSTDHCY
AFKVKDPSKVPPVKELRKLLRIQGLRCHAVYCRNGTRLNVIPLLASRSQALRYLFVRWGIELANMAVFVG
ESGDTDYEGLLGGLHKTVILKGVVSRGSEQLHANRSYPLDDVVPLDSPNIVQATGGSSSDDISDALKKLS
>gnl|CDD|274148 TIGR02469, CbiT, precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit. This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
GMTKREVRALTLAKLRLRPGDVLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGVSN
IVIVEGDAPEAPEALLPDPDAVFVGGSGGLLQEILEAVERRLRPGGRIVLNAIT
>gnl|CDD|274149 TIGR02470, Sucrose_synthase_1, sucrose synthase. This model represents sucrose synthase, an enzyme that, despite its name, generally uses rather produces sucrose. Sucrose plus UDP (or ADP) becomes D-fructose plus UDP-glucose (or ADP-glucose), which is then available for cell wall (or starch) biosynthesis. The enzyme is homologous to sucrose phosphate synthase, which catalyzes the penultimate step in sucrose synthesis. Sucrose synthase is found, so far, exclusively in plants and cyanobacteria [Energy metabolism, Biosynthesis and degradation of polysaccharides]
RAELRQLLSRYVSQGKRYLLRHQLLDEFEQYCSDADKEKKLSESPLGKLIFSTQEAIVLPPWVALAVRPR
IGVWEYVRVNVEELSVEELTISEYLDFKEQLVNGHANDPNVLELDFEPFNASFPRPSDSKSIGNGVQFLN
RHLSSKLFQDPESMEPLLNFLRVHNYNGIQLMINDRIQSVSHLQSQLRKAEEFLSALPPDTPYSEFEFEL
QELGFEPGWGDTAQRVLETLHLLDDLLEAPDPSVLEAFLGRIPMVFNVVILSPHGYFGQENVLGLPDTGG
QVVYILDQVRALENEMLQRIKLQGLEITPKILIVTRLIPDAEGTTCNQRLEKVYGTEHAWILRVPFRTEN
GIILRNWISRFEIWPYLETFAEDAEKEILAELQGKPDLIIGNYSDGNLVASLLARKLGVTQCTIAHALEK
TKYPDSDIYWQEFEDKYHFSCQFTADLIAMNAADFIITSTYQEIAGTKDSVGQYESHQAFTMPGLYRVVH
GIDVFDPKFNIVSPGADESIYFPYSDKEKRLTNLHPEIEELLFSLEDNDEHYGYLKDPNKPIIFSMARLD
RVKNLTGLVECYGRSPKLRELVNLVVVAGKLDAKESKDREEQAEIEKMHNLIDQYQLHGQIRWIGAQLNR
VRNGELYRYIADTKGIFVQPALYEAFGLTVLEAMTCGLPTFATRFGGPLEIIQDGVSGFHIDPYHGEEAA
EKIVDFFEKCDEDPSYWQKISQGGLQRIYEKYTWKIYSERLLTLAGIYGFWKFVSKLEREETRRYLEMFY
HLKYRPLAEAVPLA
>gnl|CDD|131524 TIGR02471, putative_sucrose-phosphate_synthase, sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial. Sucrose phosphate synthase (SPS) and sucrose phosphate phosphatase (SPP) are the last two enzymes of sucrose biosynthesis. In cyanobacteria and plants, the C-terminal region of most or all versions of SPS has a domain homologous to the known SPP. This domain may serve a binding or regulatory rather than catalytic function. Sequences in this family are bacterial C-terminal regions found in all but two of the putative bacterial sucrose phosphate synthases described by TIGR02472
LIITDLDNTLLGDDEGLASFVELLRGSGDAVGFGIATGRSVESAKSRYAKLNLPSPDVLIARVGTEIYYG
PELQPDRFWQKHIDHDWRRQAVVEALADIPGLTLQDDQEQGPFKISYLLDPEGEPILPQIRQRLRQQSQA
AKVILSCGWFLDVLPLRASKGLALRYLSYRWGLPLEQILVAGDSGNDEEMLRGLTLGVVVGNHDPELEGL
RHQQRIYFANNPHAFGILEGINHYDF
>gnl|CDD|131525 TIGR02472, putative_sucrose-phosphate_synthase, sucrose-phosphate synthase, putative, glycosyltransferase domain. This family consists of the N-terminal regions, or in some cases the entirety, of bacterial proteins closely related to plant sucrose-phosphate synthases (SPS). The C-terminal domain (TIGR02471), found with most members of this family, resembles both bona fide plant sucrose-phosphate phosphatases (SPP) and the SPP-like domain of plant SPS. At least two members of this family lack the SPP-like domain, which may have binding or regulatory rather than enzymatic activity by analogy to plant SPS. This enzyme produces sucrose 6-phosphate and UDP from UDP-glucose and D-fructose 6-phosphate, and may be encoded near the gene for fructokinase
LYLLLLSLHGLIRGHDLELGRDADTGGQTKYVLELARALARRSEVEQVDLVTRLIKDAKVSPDYAQPIER
IAPGARIVRLPFGPRRYLRKELLWPYLDELADNLLQHLRQQGHLPDLIHAHYADAGYVGARLSRLLGVPL
IFTGHSLGREKRRRLLAAGLKPQQIEKQYNISRRIEAEEETLAHASLVITSTHQEIEEQYALYDSYQPER
MQVIPPGVDLSRFYPPQSSEETSEIDNLLAPFLKDPEKPPILAISRPDRRKNIPSLVEAYGRSPKLQEMA
NLVLVLGCRDDIRKMESQQREVLQKVLLLIDRYDLYGKVAYPKHHRPDDVPELYRLAARSRGIFVNPALT
EPFGLTLLEAAACGLPIVATDDGGPRDIIANCRNGLLVDVLDLEAIASALEDALSDSSQWQLWSRNGIEG
VRRHYSWDAHVEKYLRILQ
>gnl|CDD|131526 TIGR02473, conserved_hypothetical_protein, flagellar export protein FliJ. Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems
EFRLQKLLDLREKEEEQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSALELSNYQRFI
RQLDQRIQQQQQELALLQQEVEAKRERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQRFR
R
>gnl|CDD|274150 TIGR02474, pectate_lyase, pectate lyase, PelA/Pel-15E family. Members of this family are isozymes of pectate lyase (EC 4.2.2.2), also called polygalacturonic transeliminase and alpha-1,4-D-endopolygalacturonic acid lyase [Energy metabolism, Biosynthesis and degradation of polysaccharides]
QQPNGGWPKNLDRLRLYTRHYTGEEYASVKNGGGGNESGTIDNGATVTEIRYLAQVYQQEKNAKYRDAAR
KGIEYLLKAQYPNGGWPQFYPLKGGYSDAITYNDNAMVNVLTLLDDIANGKDPFDVFPDSTRTRAKTAVT
KGIECILKTQVVQNGKLTVWCQQHDALTLQPKKARAYELPSLSSSESVGILLFLMTQPNPSAEIKEAIRA
GVAWFDTSRIRGYAYVKSDAAYPLVPEPGAKVLWARFYDLDTNRPFFSDRDGVIHDDIMEISQERRTGYA
WYGTSGQKLL
>gnl|CDD|274151 TIGR02475, Probable_cobalamine_biosynthesis_protein, cobalamin biosynthesis protein CobW. The family of proteins identified by this model is generally found proximal to the trimeric cobaltochelatase subunit CobN which is essential for vitamin B12 (cobalamin) biosynthesis. The protein contains an P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. A broader CobW family is delineated by two Pfam models which identify the N- and C-terminal domains (pfam02492 and pfam07683) [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
LAKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEGCSEENIVELANGC
ICCTVADDFIPTMTKLLARRQRPDHILIETSGLALPKPLVQAFQWPEIRSRVTVDGVVTVVDGPAVAAGR
FAADPDALDAQRAADDNLDHETPLEELFEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAVKIVE
ASHGEVDARVLLGLGAAAEDDLDNRPSHHDFEGGEEHDHDEFDSVVVDLGEVADPAALRQRLERLAEEHD
VLRIKGFAAVPGKPMRLLVQGVGQRVDSYYDRPWQAAETRQTRLVVIGLHDLDQAAIRAAL
>gnl|CDD|162875 TIGR02476, BluB, 5,6-dimethylbenzimidazole synthase. A previously published hypothesis that BluB, involved in cobalamin biosynthesis, is EC 1.16.8.1 (cob(II)yrinic acid a,c-diamide reductase) is now contradicted by newer work ascribing a role in 5,6-dimethylbenzimidazole (DMB) biosynthesis. The BluB protein is related to the nitroreductase family (pfam0881) [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
FSDAERAAVYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFT
RANQAAAAIYDGERASQYHRLKLEGIREAPVQLAVFCDDARGEGHGLGRHTMPEMLRYSVACAIQNLWLA
ARAEGLGVGWVSILDPDAVRRLLGVPEGWRLVAYLCLGWPDAFYDEPELERAGWQERRPLEWRRY
>gnl|CDD|131530 TIGR02477, PFKA_PPi, diphosphate--fructose-6-phosphate 1-phosphotransferase. Diphosphate--fructose-6-phosphate 1-phosphotransferase catalyzes the addition of phosphate from diphosphate (PPi) to fructose 6-phosphate to give fructose 1,6-bisphosphate (EC 2.7.1.90). The enzyme is also known as pyrophosphate-dependent phosphofructokinase. The usage of PPi-dependent enzymes in glycolysis presumably frees up ATP for other processes. TIGR02482 represents the ATP-dependent 6-phosphofructokinase enzyme contained within pfam00365: Phosphofructokinase. This model hits primarily bacterial, plant alpha, and plant beta sequences [Energy metabolism, Glycolysis/gluconeogenesis]
LQQSRLQYVPKLPKVLQGDTANISLEDGEPTAAVADQEELKELFPNTYGLPIITFEPGEASPDEHQPLKI
GVILSGGQAPGGHNVISGLFDALKKLNPNSKLYGFIGGPLGLLDNNYVELTKELIDTYRNTGGFDIIGSG
RTKIETEEQFAKALTTAKKLKLDGLVIIGGDDSNTNAALLAEYFAKHGLKTQVIGVPKTIDGDLKNQFIE
TSFGFDTACKIYSELIGNICRDALSAKKYWHFIRLMGRSASHIALECALQTHPNVCIIGEEVAAKKMTLS
QLTDYIADVIVKRAAKGKNFGVILIPEGLIEFIPEVQALIKELNNLLAQNVLEEGRKDNVQSKLSPSSKA
LFESLPEFIRHQLLLDRDPHGNVQVSQIETEKLLIELVQTELNKRKKEGEYKGKFSAVSHFFGYEGRCAF
PSNFDSDYCYALGYTAAILLANGLTGYMSTIKNLTNPAEEWIAGGVPLTMMMNMERRHGEMKPVIKKALV
DLEGKPFKKFASNRDKWALEDLYVFPGPIQYFGPEEVCDQPTLTLLLEQ
>gnl|CDD|274152 TIGR02478, ATP-dependent_6-phosphofructokinase, 6-phosphofructokinase, eukaryotic type. Members of this family are eukaryotic (with one exception) ATP-dependent 6-phosphofructokinases (EC 2.7.1.11) in which two tandem copies of the phosphofructokinase are found. Members are found, often including several isozymes, in animals and fungi and in the bacterium Propionibacterium acnes KPA171202 (a human skin commensal)
KRIAVLTSGGDAQGMNAAVRAVVRMAIYVGCRVYAIREGYQGLVDGGDNIEEAQWEDVRGILSLGGTIIG
TARCKEFRERPGRLKAARNLVSNGIDALVVIGGDGSLTGADLFREEWPSLLEELVDTGKITAEQAEEHRH
LTIVGLVGSIDNDMCGTDMTIGADSALHRICEAIDAISSTAQSHQRAFVVEVMGRHCGYLALMAAIATGA
DYVFIPERPPEEGWEDQLCHKLKRNRKAGKRKTIVIVAEGAIDRDLNPITSEDVKDVLVERLGLDTRITV
LGHVQRGGAPSAFDRILATRQGVEAVLAVLESTPETPSPVISLRGNKIVRKPLVEAVAQTKTVAKAIEEK
DFDEAMRLRGREFAENLETFLFLSIPDDDKKLVPSEASRLRIAIIHVGAPAGGMNAATRSAVRYALARGH
TVIAIHNGFSGLARHDVRELTWSDVEGWVGEGGSELGTNRSLPGDDLGTIAYYFQQHKIDGLIIIGGFEA
FEALYQLDAAREKYPAFRIPMVVIPATISNNVPGTEYSLGSDTALNEITEYCDNIKQSASASKRRVFVVE
TMGGYSGYLATMAGLATGADAAYIPEEGISLKDLQEDIEHLKETFAEGRAGKLILRNEKASKVYTTDFIA
RIISEEGKGRFDARTAVLGHMQQGGSPSPFDRVRATRLAIRAVDFIEEKIKANKHADKLSADDTSAVVIG
IRGSNVLFTPVKQLLANETDFEHRRPKNQWWLQLRPLVRILAGRDS
>gnl|CDD|274153 TIGR02479, RNA_polymerase_sigma_factor_WhiG, RNA polymerase sigma factor, FliA/WhiG family. Most members of this family are the flagellar operon sigma factor FliA, controlling transcription of bacterial flagellar genes by RNA polymerase. An exception is the sigma factor WhiG in the genus Streptomyces, involved in the production of sporulating aerial mycelium
LIRRYLPLVKRIAGRLSVGLPSSVELDDLIQAGMFGLLDAIERYDPSRGAKFETYAVQRIRGAMLDELRR
LDWVPRSLRQKARKLERAIRELEARLGREPTEEEIAEELGMDLKEYRQALNEINALSLVSLDELLESGDD
GGSLIDRIEDDKSEDPEEELEREELREALAEAIESLSEREQLVLSLYYYEELNLKEIGEVLGLTESRVSQ
IHSQALKKLRAKLS
>gnl|CDD|131533 TIGR02480, Flagellar_motor_switch_protein_FliN, flagellar motor switch protein FliN. Proteins that consist largely of the domain described by this model for this protein family can be designated flagellar motor switch protein FliN. Longer proteins in which this region is a C-terminal domain typically are designated FliY. More distantly related sequences, outside the scope of this family, are associated with type III secretion and include the surface presentation of antigens protein SpaO required or invasion of host cells by Salmonella enterica [Cellular processes, Chemotaxis and motility]
NIDLILDIPVELTVELGRTRITLGDLLKLGEGSVIELDKLAGEPLDILVNGRLIARGEVVVVEDKFGIRI
TEIVDSS
>gnl|CDD|274154 TIGR02481, hemeryth_dom, hemerythrin-like metal-binding domain. This model describes both members of the hemerythrin (TIGR00058) family of marine invertebrates and a broader collection of bacterial and archaeal homologs. Many of the latter group are multidomain proteins with signal-transducing domains such as the GGDEF diguanylate cyclase domain (TIGR00254, pfam00990) and methyl-accepting chemotaxis protein signaling domain (pfam00015). Most hemerythrins are oxygen-carriers with a bound non-heme iron, but at least one example is a cadmium-binding protein, apparently with a role in sequestering toxic metals rather than in binding oxygen. Patterns of conserved residues suggest that all prokaryotic instances of this domain bind iron or another heavy metal, but the exact function is unknown. Not surprisingly, the prokaryote with the most instances of this domain is Magnetococcus sp. MC-1, a magnetotactic bacterium
KWDDSLSTGIEEIDAQHKELFELINELYDALSAGRGKDELKEILKELIDYTENHFADEERLMEAYGYPDL
EEHKKEHEKFVKKIEELQEAVAEGADESLAEELLDFLKDWLVNHILKEDKKYAPYL
>gnl|CDD|213713 TIGR02482, ATP-dependent_6-phosphofructokinase, 6-phosphofructokinase. 6-phosphofructokinase (EC 2.7.1.11) catalyzes the addition of phosphate from ATP to fructose 6-phosphate to give fructose 1,6-bisphosphate. This represents a key control step in glycolysis. This model hits bacterial ATP-dependent 6-phosphofructokinases which lack a beta-hairpin loop present in TIGR02483 family members. TIGR02483 contains members that are ATP-dependent as well as members that are pyrophosphate-dependent. TIGR02477 represents the pyrophosphate-dependent phosphofructokinase, diphosphate--fructose-6-phosphate 1-phosphotransferase (EC 2.7.1.90) [Energy metabolism, Glycolysis/gluconeogenesis]
KIGILTSGGDAPGMNAAIRAVVRTAIYHGFEVYGIRRGYKGLINGKIEPLESKNVSGIIHRGGTILGTAR
CPEFKTEEVREKAVENLKKLGIEGLVVIGGDGSYTGAQKLYEEGGIPVIGLPGTIDNDIPGTDYTIGFDT
ALNTIIDAVDKIRDTATSHERAFVIEVMGRHAGDLALYAGIATGAEIIIIPEFDYDIDELIQRLKEQHEA
GKKHSIIIVAEGNIVGSAKEVAKKIEEKTGIETRVTVLGHTQRGGSPSAFDRVLASRLGAKAVELLLEGK
GGVMIGIQNNKIVTHPIEEAL
>gnl|CDD|274155 TIGR02483, ATP-dependent_6-phosphofructokinase_1, phosphofructokinase. Members of this family that are characterized, save one, are phosphofructokinases dependent on pyrophosphate (EC 2.7.1.90) rather than ATP (EC 2.7.1.11). The exception is one of three phosphofructokinases from Streptomyces coelicolor. Family members are both bacterial and archaeal [Energy metabolism, Glycolysis/gluconeogenesis]
RIGVLTGGGDCPGLNAVIRGVVRRAIAEYGWEVIGIRDGWRGLLEGDTVPLLDLEDVRGILPRGGTILGS
SRTNPFKYEEDGDDKIVANLKELGLDALIAIGGDGTLGIARRLADKGLPVVGVPKTIDNDLEATDYTFGF
DTAVEIATEALDRLHTTAESHHRVMVVEVMGRHAGWIALHSGIAGGADVILIPEIPFDIDSVCEKVRERF
ARGKRFAIVVVAEGAKPKGGEMVVQEGVKDAFGHVRLGGIGNWLAEEIERRTGIETRATVLGHLQRGGSP
SAFDRVLATRFGVAAVDLVHEGQFGHMVALRGTDIVYVPIAEAV
>gnl|CDD|274156 TIGR02484, conserved_hypothetical_protein, CitB domain protein. This model identifies proteins of two distinct names which may or may not have two distinct functions. CitB has been identified in salmonella and E. coli as the signal transduction component of a two-component system for citrate in which CitA acts as a citrate transporter. CobZ is essential for cobalamin biosynthesis (by knockout of the R. capsulatus gene) and is complemented by the characterized precorrin 3B synthase CobG. The enzyme has been shown to contain flavin, heme and Fe-S cluster cofactors and is believed to require dioxygen as a substrate. This model identifies the C-terminal domain of the R. capsulatus CobZ, which, in most other species exists as a separate gene adjacent to CobZ
PAPDPFAEAKRVLNLCNSCGYCTGLCAVFPAAQGRPDLTRGDLRHLAHLCHDCQSCWHDCQYAPPHAFAI
NLPATLADVRRASYAEHLWPPTLGRASSLAAQALFALCCVLPPLLLLTLQPLERLFAAHAGPGAFYAVIP
WPVMAGAAGATMGWAALALALRLARFWRAIAGGGPVPVDARALRAALVDILTLRNLGGGGAGCEDRAGRP
SHRRRILHHLLAGGFGLTFLSTVAAFVYHHLLGQPAPYPLLSLPVILGLVGGVAMLAGAAGLSGLEARAD
PEPLKTPAMLRSDRFLLGQLALLAGTGLALLALRDTPAMGLLLALHLGAVAGAFLGLPFSKLSHGGWRAA
ALLRAALDRARSKTASGPERAG
>gnl|CDD|274157 TIGR02485, conserved_hypothetical_protein, precorrin 3B synthase CobZ. CobZ is essential for cobalamin biosynthesis (by knockout of the R. capsulatus gene) and is complemented by the characterized precorrin 3B synthase CobG. The enzyme has been shown to contain flavin, heme and Fe-S cluster cofactors and is believed to require dioxygen as a substrate. This model identifies the N-terminal portion of the R. capsulatus gene which, in other species exists as a separate protein. The C-terminal portion is homologous to the 2-component signal transduction system protein CitB (TIGR02484) [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
VIGGGLAGLCAAIEARRAGASVLLLEAAPRARRGGNARHGRNIRVAHDIPTDFQRDSYPAEEFERDLAPV
TGGRTNESLSRLGIGRGSRDLRWAFAHGVHLQPWAAGNLPYSRRTAFLRGGGKALTNALYSSAERLGVEI
RYGIAVDRIPPEAFGPAHDGPLTAVGTHRITTQSLVLAAGGLGANRDWLRKTHGPRADGIANRGTPYQLG
GLLLQLLAEGAQAIGDPTDGHVVAVDARAPFHDGGIVTRIDGMQLGIVVGRDGRRFADEGAIRGPERYAV
WGRQLASRPGQRAYILLDADAAKRLPPMACPPLSADTLEELAGLLGIDPGGLAETLDRPNAAPRTGARMI
LVVPFHAYPMIPGITFTRYGLVVDATARVRLNDAVAPRNLFAAGTNMAGNVLGQGYLAGAGLTIAAVFGR
IAGRAAARLAPK
>gnl|CDD|274158 TIGR02486, putative_reductive_dehalogenase_partial, reductive dehalogenase. This model represents a family of corrin and 8-iron Fe-S cluster-containing reductive dehalogenases found primarily in halorespiring microorganisms such as dehalococcoides ethenogenes which contains as many as 17 enzymes of this type with varying substrate ranges. One example of a characterized species is the tetrachloroethene reductive dehalogenase (1.97.1.8) which also acts on trichloroethene converting it to dichloroethene
KWEGTPEENSRMVRAAARFLGADDVGIAELDDNWVFKLFYEHSTDPMDGPTSTTENKDIEKKYVFEDVDE
EYTTTEPDTKLVIPNKPKYVIVATIEMDYETYLRSPGSSIIASAASFKAYSRFGYVAVRLQQFIRNLGYN
AVPSGNGNGLGSSVAFAVLAGLGEHGRMGQAIISPEYGPRVRIAKVILTDLPLVPTKPIDAGMAKFCETC
GKCADECPSGAISKGGEPTWDPEDSNGDPPGENNPGLKWQYDGWRCLLFRCYNEGGGGCGVCQAVCPFNK
KPNSWIHDVVRSTVSTTSVFNSFFTNMDKAFGYG
>gnl|CDD|274159 TIGR02487, Anaerobic_Ribonucleoside-triphosphate_reductase, anaerobic ribonucleoside-triphosphate reductase. This model represents the oxygen-sensitive (anaerobic, class III) ribonucleotide reductase. The mechanism of the enzyme involves a glycine-centered radical, a C-terminal zinc binding site, and a set of conserved active site cysteines and asparagines. This enzyme requires an activating component, NrdG, a radical-SAM domain containing enzyme (TIGR02491). Together the two form an alpha-2/beta-2 heterodimer [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
NENANMDSPTPSTQRKLIASEVSKDYALLHLLPKDIARAHLNGDIHIHDLDYALTLTTNCCLHDLRNLLK
YGFRTGNIVSKPPKHIDVALNHIVNILQSLQNEQYGGQSFPEFDTLLAPYIEKTNLKHRKVLQQLQLLLF
EATEYAARRTFTDVTQAMQGPEYNPNTLHSAGGQTPFESIGYGTETSKEGRMIAKALLDVRMEGDGKGEP
FIFPKIIFKVREGFNWDEPDPYDLFELAFECAAKRGYPYFLNLDPEDNVKEDVRYPMGCRTFLSPNENGD
GEESYIGRGNIGVTSINLPRIAYKSRGDEEEFFEELDEYLEIAKEALEIRREYLKKMLAKDLPPMYSQGG
WDGGNLLDESVEEILKSGTNSIGFIGLNEALVALTGKHLHEEEEARELAIRILEFIRDKADEFKKETGLN
YSVYATPAESLCGRFAKKDREEFGEIPGVTDKPYYTNSFHVPVYEDVNLGEKIDIEAPFHPLTNGGHITY
IELDEAIPDPEALKDITKKAMKNGIGYFGINPPVDVCEDCGYTGEGLNDKCPKCGSHDIEVISRITGYLG
PVENWNDGKQAEFKDRKKH
>gnl|CDD|131541 TIGR02488, Flagellar_basal-body_rod_protein_FlgG, flagellar basal-body rod protein FlgG, Gram-negative bacteria. This family consists of the FlgG protein of the flagellar apparatus in the Proteobacteria and spirochetes [Cellular processes, Chemotaxis and motility]
ALWTAATGMNAQQTNMDVISNNLANVNTTGFKKDRAEFEDLLYQTERQPGAQSSEQQTILPVGVQVGLGV
RVVATQKLFTQGSLQNTGNDLDLAIEGEGFFQVLMPDGTTAYTRDGAFKINAEGQLVTSNGYPLQPEITI
PENATSITVGSDGEVSVRQGGQTEPQEVGQITLATFINPAGLEAVGENLFRETPASGPPQIGTPGLDGFG
KLRQGFLEASNVNVVQEMVDMITAQRAYEMNSKAIQASDQMLQTVSQLL
>gnl|CDD|131542 TIGR02489, flagellar_hook_subunit_protein, flagellar hook protein FlgE, epsilon proteobacterial. Members of this family are flagellar hook proteins, designated FlgE, as found in the epsilon subdivision of the Proteobacteria (Helicobacter, Wolinella, and Campylobacter). These proteins differ significantly in architecture from proteins designated FlgE in other lineages; the N-terminal and C-terminal domains are homologous, but members of this family only contain a large central domain that is surface-exposed and variable between strains
MLRSLWSGVSGMQAHQVALDVEGNNIANVNTTGFKYSRADFGDMLSQTVKIATSPYDGLGGQNDLSIGLG
VSISSTTKIFSQGSVQTTNSKTDVAINGDGFFIVSDDGGLTNYYTRDGAFKFDAYGNFVNNSGYIVQGWN
RPLEAAESGTMSDWDDQTVDSTRPPQNIFIDPGMVIPAAATTEVALKANLNAGLNIDTSSNLYALDSTHQ
TAADGTTAFYDSSGEVTQKGEDAGVLFNASGTALNLREGQGIWVSYADAKYSTNKVVVSAFDTITLNGVR
IQFANISNIDGVSSYVAAQNAINDTRDGTGVRAVKSAGQLRFVNDNSDDGTDNMKNINITVSGAGELWNF
TFNQNTITAFRYIYTSNDDADSTARTFRTTEDLRALLQRDANYIKYDGSGYFASTDVNAAVKVTINANGM
FEISNADDNDTEPKNLSLNVTSYSNKNVTTNVLFKAIMKALNTGPLTEGGSIKESEQLKLAAHSAGLDIV
DSLGSKHTLEVQFVKQGGNEWSFIIRVPEPAEFNGGSGEGPNIFEGGRARFNNDGSLAGMNPPTIQFSPK
NGAAPPQRIKLSFGTSGTFDGLTSSDKASTTTGIAQNGYQSGNLKDIRFDSNGNLLGEFSNGKTFALAQV
AMASFANNSGLQAEGGNLFSQTANSGEPVVGEAGTGGRGEMSTSALEMSNVDLSRSLTQLIVVQRGFQAN
SKTVTTSDQILNTLLQLKQ
>gnl|CDD|274160 TIGR02490, flgF, flagellar basal-body rod protein FlgF. Members of this protein are FlgF, one of several homologous flagellar basal-body rod proteins in bacteria [Cellular processes, Chemotaxis and motility]
IVLPPDGDITIGADGTISQDGEEVGRLGLVNFDNPNQLQREGDGLFRATGGGPAPADSNVRVVQGYLEGS
NVNAVSEMVDMIEAQRAYE
>gnl|CDD|274161 TIGR02491, Anaerobic_ribonucleoside-triphosphate_reductase, anaerobic ribonucleoside-triphosphate reductase activating protein. This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]
NYMNIKPDDIVNGEGIRVSLFVAGCKHHCEGCFNKETWNFNGGKEFTEALEKEIIRDLNDNPLIDGLTLS
GGDPLYPRNVEELIELVKKIKAEFPEKDIWLWTGYTWEEILEDEKHLEVLKYIDVLVDGKFELSKKDLKL
KFRGSSNQRIIDLK
>gnl|CDD|274162 TIGR02492, flgK_ends, flagellar hook-associated protein FlgK. The flagellar hook-associated protein FlgK of bacterial flagella has conserved N- and C-terminal domains. The central region is highly variable in length and sequence, and often contains substantial runs of low-complexity sequence. This model is built from an alignment of FlgK sequences with the central region excised. Note that several other proteins of the flagellar apparatus also are homologous in the N- and C-terminal regions to FlgK, but are excluded from this model [Cellular processes, Chemotaxis and motility]
SLLNIAKSGLSASQIALSVTSNNIANANTPGYSRQRAVLTAVPAGGQGGKQIGTGVKVTSIRRIQDQFLD
NQYRRANSSAGYADSRASGLSKIEQIFNDLDGSGLGTYLNNFFNALQELAKNPDSEALRQAVLESAQALA
NSFNQTSNELQDLRKGINAEIKSAVTEINSLLKQIASLNKEIKQVEASGQDANDLLDQRDLLLKELSQLI
GISVSENENGTVNVYTGSGQVLVDGATVTGSSTSPLTADTTGGKVGGDGVYLPSGSSKVTISSDLQGGKL
GGLLDLRDGVLPDLQSQLDQLAKTLADEFNEVHQSGADLTGSA
>gnl|CDD|131546 TIGR02493, PFLA, pyruvate formate-lyase 1-activating enzyme. An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair]
RIHSTESMGTVDGPGIRFVVFMQGCPLRCQYCHNPDTWDLKGGTEVTPEELIKEVGSYKDFFKASGGGVT
FSGGEPLLQPEFLSELFKACKELGIHTCLDTSGFLGGCTEAADELLEYTDLVLLDIKHFNPEKYKKLTGV
SLQPTLDFAKYLAKRNKPIWIRYVLVPGYTDSEEDIEALAEFVKTLPNVERVEVLPYHQLGVYKWEALGI
EYPLEGVKPPNKEQLERAAEIFKEY
>gnl|CDD|274163 TIGR02494, PFLE_PFLC, glycyl-radical enzyme activating protein. This subset of the radical-SAM family (pfam04055) includes a number of probable activating proteins acting on different enzymes all requiring an amino-acid-centered radical. The closest relatives to this family are the pyruvate-formate lyase activating enzyme (PflA, 1.97.1.4, TIGR02493) and the anaerobic ribonucleotide reductase activating enzyme (TIGR02491). Included within this subfamily are activators of hydroxyphenyl acetate decarboxylase (HdpA), benzylsuccinate synthase (BssD), gycerol dehydratase (DhaB2) as well as enzymes annotated in E. coli as activators of different isozymes of pyruvate-formate lyase (PFLC and PFLE) however, these appear to lack characterization and may activate enzymes with distinctive functions. Most of the sequence-level variability between these forms is concentrated within an N-terminal domain which follows a conserved group of three cysteines and contains a variable pattern of 0 to 8 additional cysteines
IFNIQRYSVHDGPGIRTTVFLKGCPLRCKWCSNPESQRKSPELLFKENRCLGCGKCVEVCPAGTARLSEL
ADGRNRIIIRREKCTHCGKCTEACPSGALSIVGEEMTVEEVMRVVLRDSIFYRNSGGGVTLSGGEPLLQP
EFALALLQACHERGIHTAVETSGFTPWETIEKVLPYVDLFLFDIKHLDDERHKEVTGVDNEPILENLEAL
AAAGKNVVIRIPVIPGFNDSEENIEAIAAFLRKLEPGVDEIDLLPYHRLGENKYRQLGREYPDSEIPDPA
EEQLLELKEIFESKG
>gnl|CDD|274164 TIGR02495, RADICAL-ACTIVATING_ENZYME, anaerobic ribonucleoside-triphosphate reductase activating protein. This enzyme is a member of the radical-SAM family (pfam04055). It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487) and presumably fulfills the identical function as NrdG, which utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in NrdD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]
RIAGLVPFSTVDYPGKLAFTIFLQGCNLKCPYCHNPLLIPRRGSGEIEVEELLEFLRRRRGLLDGVVITG
GEPTLQAGLPDFLREVRELGFEVKLDTNGSNPRRLEELLEEGLVDYVAMDVKAPPEKYGELYGLEKNGAA
KNILKSLEILLESGIPFELRTTVVRGFLTEEDLAEIATRIKENGTYVLQPFR
>gnl|CDD|131549 TIGR02497, hypothetical_protein_CV_2587, type III secretion apparatus protein, YscI/HrpB, C-terminal domain. This model represents the conserved C-terminal domain of a protein conserved in across species in the bacterial type III secretion apparatus. This protein is designated YscI (Yop proteins translocation protein I) in Yersinia and HrpB (hypersensitivity response and pathogenicity protein B) in plant pathogens such as Pseudomonas syringae [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
PEDLLQMQRALMQATVQVDLTAKVAGAMSQAVNKLVNMQ
>gnl|CDD|131550 TIGR02498, probable_type_III_secretion_apparatus, type III secretion system protein, SsaH family. This family describes a small protein, always smaller than 100 amino acids, encoded in pathogenicity islands for bacterial type III secretion systems in various strains of Yersinia, Salmonella, and enteropathogenic E. coli, as well as Chromobacterium violaceum and Citrobacter rodentium. Although strictly associated with type III secretion systems, this protein seems not yet to have been characterized as part of the apparatus or as an effector protein [Cellular processes, Pathogenesis]
LDTDANKLVVEAALAAVNHSLPKEAHSILNALPQIIPDKKDRLVCEAILLFGLNHKNDAVKLLENMDDEE
AQLLRSLVN
>gnl|CDD|274165 TIGR02499, translocation_protein, type III secretion apparatus protein, HrpE/YscL family. This model is related to pfam06188, but is broader. pfam06188 describes HrpE-like proteins, components of bacterial type III secretion systems primarily in bacteria that infect plants. This model includes also the homologous proteins of animal pathogens, such as YscL of Yersinia pestis. This model excludes the related protein FliH of the bacterial flagellar apparatus (see pfam02108) [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
APVLRAEDLAALAQAQAILAAARQRAEAILADAEEEAEASRQLGYEQGLEQFWQEAAAQLAEWQQEAEQL
EASLEERLAELVLQALEQILGEYDEPERLVRLLRQLLRAVANQGRLTLRVHPEQLDEVREALAERLALEP
WELEPDASLAPGACVLETESGVVDLS
>gnl|CDD|274166 TIGR02500, Yop_proteins_translocation_protein_D, type III secretion apparatus protein, YscD/HrpQ family. This family represents a conserved protein of bacterial type III secretion systems. Gene symbols are variable from species to species. Members are designated YscD in Yersinia, HrpQ in Pseudomonas syringae, and EscD in enteropathogenic Escherichia coli. In the Chlamydiae, this model describes the C-terminal 400 residues of a longer protein [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
WKLRVLSGPHRGAELPLPEGNLVLGTDAADCDIVLSDGGIAAVHVSLHVRLEGVTLAGAVEPAWEEGGVL
PDEEGTPLPSGTPLLVAGVAFALGEVDDALPDTEVTPRQSAEPAPPPRRARTSLPLLLLALFLLLSGATA
SGLWPSVAAPPVTDPPADVAAQLAEAGLHAVRAEWRERGNLLLSGLVADSTQKLPLALWLKSLGIRYRLE
VICDDELRREVRDVLSLMGYHDAEVSVGPEPGGLLISGYVADGKQWLKVADLLRAIVPLAGWRIVRVASD
VIAQLASLLSDAGLLGVVTVTESGREIALSGQLDSEKRSRLQELLAAFKQRDGVIPDVVLQNIPAADGTS
DELPFPVVSISGSGPNPYVVLADGQRLFVGARLPGGYRIVAISPDGLTLEKGGRLIRIPL
>gnl|CDD|274167 TIGR02501, Putative_Yop_proteins_translocation_protein_E, type III secretion system protein, YseE family. Members of this family are found exclusively in type III secretion appparatus gene clusters in bacteria. Those bacteria with a protein from this family tend to target animal cells, as does Yersinia pestis. This protein is small (about 70 amino acids) and not well characterized [Cellular processes, Pathogenesis]
MTQLEDRLSHADTAARAIIEQLEAALAELKEQLSRGGDPQQYQEWQLLADAIEAAIKIIEILTGRYH
>gnl|CDD|131554 TIGR02502, Yop_proteins_translocation_protein_X, type III secretion protein, YscX family. Members of this family are encoded within bacterial type III secretion gene clusters. Among all species with type III secretion, those with this protein are found among those that target animal rather than plant cells. The member of this family in Yersinia was shown by mutation to be required for type III secretion of Yops effector proteins and therefore is believe to be part of the secretion machinery [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
MSRVSALHIGIEALTAISHEEVDTDLPERYALLPDGQPVETHLERLYPARQSDQYLLAFAKPQLNFHGLL
RPEDYRQALDNLQQLLQESGSANLQAAAELLQSTQLDERLLQMALNLLHKV
>gnl|CDD|131555 TIGR02503, Chaperone_protein_sycN., type III secretion chaperone SycN. Members of this protein family are part of the machinery of bacterial type III secretion in a number of bacteria that target animal cells. In the well-studied system from Yersinia, a complex of this protein (SycN) and YscB (pfam07329) acts as a chaperone for the export of YopN (). YopN then acts to control effector protein secretion, in response to calcium levels, so that secretion occurs only after contact with the targeted eukaryotic cell [Protein fate, Protein folding and stabilization, Cellular processes, Pathogenesis]
IDRALAQFCQDLGLPTPAPLPRLAQLSMEQSGRLYVEQHDGTLLLWLARSLEWHQAEEALKRALTLCHAQ
RGGALPLRAGLLGEQQLVLCTRLDGRSLTAPTLHQAFVQLLRLLDEVTA
>gnl|CDD|274168 TIGR02504, ribonucleotide_reductase, ribonucleoside-diphosphate reductase, adenosylcobalamin-dependent. This model represents a group of adenosylcobalamin(B12)-dependent ribonucleotide reductases (Class II RNRs) related to the characterized species from Pyrococcus, Thermoplasma, Corynebacterium, and Deinococcus. RNR's are responsible for the conversion of the ribose sugar of RNA into the deoxyribose sugar of DNA. This is the rate-limiting step of DNA biosynthesis. This model identifies genes in a wide range of deeply branching bacteria. All are structurally related to the class I (non-heme iron dependent) RNRs. In most species this gene is known as NrdJ, while in mycobacteria it is called NrdZ [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
VLAARYLLKDEDGNIIESPEDLFRRVARALAAAEDKYNSPVWKQWYERFYDLMVNLGFIPNSPTLMNAGG
TRLGQLSACFVLPVEDSMEDIFEALKEAALIFKRGGGVGYNFSTLRPKGDLVSGTGGVASGPVSFMRVFD
SAAGVVKQGGTRRGAQMGILDVWHPDIEEFIEAKAKEGKLQNFNISVGVTDEFMEAVENDEEYELRNPRT
GEYKEVDARELWDKIVESAWKSAEPGVLFIDTINKWHTCPYGGRINATNPCGEQPLLPYESCNLGSINLA
KFVKNDFGDEASFDFERLREVVRLATRFLDNVIDINVFPLPEIAENTKKTRRIGLGIMGLADLLIKLGIP
YDSEEARELAEEVMEFIADAAYRASAELAKERGAFPLYDASKYPMGRAMGARIPSALPAEIREAIRKYGI
RNAQLTTIAPTGTISLIAGTSSGIEPVFALVYFRNVTVGGELLEVNPLVELALRELGYYSDEIVKYVDEK
GTVEGAPGPEELPKVFVTAMDISPEDHVLMQAAIQPWVDSSISKTINMPSDATVEDVKAVYLEAWKLGLK
GITVYRDGSRSSQVL
>gnl|CDD|274169 TIGR02505, RTPR, ribonucleoside-triphosphate reductase, adenosylcobalamin-dependent. This model represents a group of adenosylcobalamin(B12)-dependent ribonucleotide reductases (RNR) related to the characterized species from Lactococcus leichmannii. RNR's are responsible for the conversion of the ribose sugar of RNA into the deoxyribose sugar of DNA. This is the rate-limiting step of DNA biosynthesis. Thus model identifies NrdJ enzymes only in cyanobacteria, lactococcus and certain bacteriophage. A separate model (TIGR02504) identifies a larger group of divergent B12-dependent RNR's [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
MTSVKPHWGKTALVTYKRTYARWLPEKGRSENWDETVERVVSGNRNLWPRLQDRPLLELQQSLTEEAERL
YRLIYELKALPSGRNLWIGGTDYQRRTEDSLFNCWFTAIRPQKPFSFLFDLLMKGCGVGFSVARSNISQI
PRVDQEIKVQLVVDETSESYDASVEVGAVSKNEDVQDVDLPDTREGWVLANALLIDLHFAQTNADRKQKL
VLDLSDIRPAGAELKGFGGTASGPVPLAKMLTDVAEILSNKAGGRLTAVDAADICNLIGKAVVAGNVRRS
AEMALFSNDDPEFESFKQAKEKLMHHRWASNNSVAVDSAFSGLARSAADILENGEPGQVNLDLSKSEGRI
VNGRYQAGEDGDVEGTNPCGEILLANGEPCNLFEVNLLAFEEDGWGLQRAFALAARYAKRVTFSPYDDEI
SREIIQKNRRIGVSMSGIQDFLLLRGGTGFKDDFDPETHEAIKVRVYDKRAAKFLDRMYKIVVKAAQDYS
KELGCPEPIKHTTVKPSGTISKLAGASEGIHPPYGAYLIRRITFSKSDPLAPALKACGYTVEADQYDKNE
QGRLPPCKTTLVEFPIKAVGADNPNIAEVGINTVSAAAQFAFYAFLQTYWSDNNVSCTITFDPSEGEQVE
SALRQYRDNSEGYFSTKSTSLLPAFGGSFPQLPKEPIDKETYEKRSAEITGNVEEVFSQLNSDIKDLEDV
DQEDCANGACPIK
>gnl|CDD|274170 TIGR02506, Ribonucleoside-diphosphate_reductase_large_subunit, ribonucleoside-diphosphate reductase, alpha subunit. This model represents the alpha (large) chain of the class I ribonucleotide reductase (RNR). RNR's are responsible for the conversion of the ribose sugar of RNA into the deoxyribose sugar of DNA. This is the rate-limiting step of DNA biosynthesis. Class I RNR's generate the required radical (on tyrosine) via a "non-heme" iron cofactor which resides in the beta (small) subunit. The alpha subunit contains the catalytic and allosteric regulatory sites. The mechanism of this enzyme requires molecular oxygen. E. Coli contains two versions of this enzyme which are regulated independently (NrdAB and NrdEF, where NrdA and NrdE are the large chains). Most organisms contain only one, but the application of the gene symbols NrdA and NrdE are somewhat arbitrary. This model identifies RNR's in diverse clades of bacteria, eukaryotes as well as numerous DNA viruses and phage [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
YMGLKELYNRYLLRNAATGAIYESPQEAYMRVAMGLASLEPKDTRLADAIRFYDLLSRLKISPATPTLFN
AGTPRGQLSSCFLLDVTDDTLESIYKAIDDVAQLSKHGGGIGLNLTKLRAIGSPIRGTNNASKGIIPFLK
LLDSSVEAVNQGGKRPGAAAVYLEVWHPDIEEFLDLKKNNGDERRRCDNLFYGLWIPDLFMKRVEEDKDW
YLFSPYDVPGLYGLYGEEFEEEYERLEKDVEARKKIRKVSARDLMKDILRTRVETGRPYILFKDAVNKHN
PFKTGGGAIKMSNLCTEITQPTDDSHKGETAVCNLASVNLANFVMEDKFDFSELEDAVRIAVRFLDNVID
LQNYPTAPAAKSNQRRRSIGIGVMGLHDVLAKLGLPYDSEEARDLNDRIFEAIYYYAIKASAELAKEKGP
FPGFSGSKYAKGWLHPDTWEKTIDPKTSMAPTEEDWEALRERIKEYGLRNSQLTALMPTASSSQLTGVTE
SIEPVFSNIFTKKTLSGEFLIPNKYLMKELEELGLWDADRRGDIVENVGSPQPIAAIPETLKYKYKTAYE
LDQEALIDMAADRQKFVDQSISLNLFLTEEVTAKDLLKLLLLAWKKGLKTMYYCRSR
>gnl|CDD|131559 TIGR02507, MtrF, tetrahydromethanopterin S-methyltransferase, F subunit. This small protein (MtrF) is one of eight subunits of the N5-methyltetrahydromethanopterin: coenzyme M methyltransferase in methanogenic archaea. This methyltranferase is membrane-associated enzyme complex that uses methy-transfer reaction to drive sodium-ion pump. Archaea domain, have evolved energy-yielding pathways marked by one-carbon biochemistry featuring novel cofactors and enzymes. This transferase is involved in the transfer of 'methyl' group from N5-methyltetrahydromethanopterin to coenzyme M. In an accompanying reaction, methane is produced by two-electron reduction of the methyl moiety in methyl-coenzyme M by another enzyme methyl-coenzyme M reductase
GIPTVAEPDIESIKSLVEAIDYRVQLITRDIGLASGVQTTTITGLAYGFLFAVLLVAVPIAMKFL
>gnl|CDD|131560 TIGR02508, Putative_Yop_proteins_translocation_protein_G, type III secretion protein, YscG family. YscG is a molecular chaperone for YscE, where both are part of the type III secretion system that in Yersinia is designated Ysc (Yersinia secretion). The secretion system delivers effector proteins, designate Yops (Yersinia outer proteins) in Yersinia. This family consists of YscG of Yersinia, and functionally equivalent type III secretion machinery protein in other species: AscG in Aeromonas, LscG in Photorhabdus luminescens, etc [Protein fate, Protein folding and stabilization, Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
KRELKVLLAEIALIGTGHHCHQEANTIADWLHLKGESEEAVQLIRLSSLMNRGDYQSALQLGNKLCYPDL
EPWLALCEWRLGLGSALESRLNRLAASGDPRLQTFVAGMREQIKT
>gnl|CDD|131561 TIGR02509, Yop_proteins_translocation_protein, type III secretion effector, YopR family. Members of this family are type III secretion system effectors, named differently in different species and designated YopR (Yersinia outer protein R), encoded by the YscH (Yersinia secretion H) gene. This Yops protein is unusual in that it is released to extracellularly rather than injected directly into the target cell as are most Yops [Cellular processes, Pathogenesis]
LENKLAISDPATQRELLWQQYQQGKPAAGTADLVPELLSPVKERLLGRFGGQQLPVVPPIDRLELRAMLR
QFDPLGRQQEAALLQLLGKLKSLPQVGMEYLSDLARRELMTLIPKNGMVDNLMRNSHKLDL
>gnl|CDD|188230 TIGR02510, NrdE-prime, ribonucleoside-diphosphate reductase, alpha chain. This model represents a small clade of ribonucleoside-diphosphate reductase, alpha chains which are sufficiently divergent from the usual Class I RNR alpha chains (NrdE or NrdA, TIGR02506) as to warrant their own model. The genes from Thermus thermophilus, Dichelobacter and Salinibacter are adjacent to the usual RNR beta chain [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
EIPEWYNTQGRSMFRRGYLLKGETVEGRVREIASTAEKLDIRPGFEERFFEYLARGKYSLATPVWANTGL
DRGLPISCAGSYVGDSVLDILEGQAEVGMMAKNGGGTSSYLGDIRPRGADISTNGTSNGADGFAPLFDNF
INVKTQGATRRGEWAGYVDFEHPDFEEWLGIQLENPASQHVGWGVEVGDDWYEKMIAGDPEKRARWAKLM
YSRARTGIPYMWFRWNANELAPQVIKNSGIPIRASNLCTEIALPSDDMESFVCCLSSLNVLHYDEWKDTD
AVETLVRFLDSVCSEFIAKAKGLSYMHRAVRFAERARAIGLGTLGWHSYLQSNRIPFESGEAHILNAEIY
KTIKERAEEASRELAERYGEPEVCEGTGRRNATLIAIAPTKSSAFILGQVSPSIEPLVSNYFIQDSNKGD
VVRKNPVLAKVLKEKGTDQELVWDIITYHNGSVQHLDFLTDEEKSVFKTFYEISQMAIIRLAAARQKHID
QAQSLNLFISPDEKPSVDANVLRAFAWDPGLKSLYYQRSERGAQASSRDLLDCLACEG
>gnl|CDD|131563 TIGR02511, Protein_tyeA., type III secretion effector delivery regulator, TyeA family. Members of this family include both small proteins, about 90 amino acids, in which this model covers the whole, and longer proteins of about 360 residues which match in the C-terminal region. The longer proteins (HrpJ) have N-terminal regions that match pfam07201. Members of this family belong to bacterial type III secretion systems, and include TyeA from the well-studied Yersinia systems. TyeA appears involved in calcium-responsive regulation of the delivery of type III effectors
YDAQGLLGDLLALVEERWLGPDWIEQLANALGLPELEHRVAFLQGLKRLLRLLPIALFSDEEQRQNLLQA
LQEAIDEAI
>gnl|CDD|274171 TIGR02512, Periplasmic_hydrogenase_large_subunit [FeFe] hydrogenase, group A. This model describes iron-only hydrogenases of anaerobic and microaerophilic bacteria and protozoa. This model is narrower, and covers a longer stretch of sequence, than pfam02906. This family represents a division among families that belong to pfam02906, which also includes proteins such as nuclear prelamin A recognition factor in animals. Note that this family shows some heterogeneity in terms of periplasmic, cytosolic, or hydrogenosome location, NAD or NADP dependence, and overal protein protein length
SIVRDMSKCIGCGRCVRACTNVQIVGALGFLNRGGKTEVAPKFGRLLDESNCIGCGQCSLVCPVGAITEK
DHVDRVLKALADPKKVVVVQIAPAVRVALGEEFGMPIGTDVTGKMVAALRKLGFDYVFDTNFAADLTIME
EGTELLERLKNGGKLPMFTSCCPGWVNYAEKYYPELLPNLSSCKSPQQMLGAVIKTYWAKKMGIDPEDVY
VVSIMPCTAKKDEAQRPELKSDGYRDVDAVLTTRELARMIKEAGIDFAKLPDSQFDSPFGEYSGAGAIFG
ATGGVMEAALRTAYEIVTGKELELIEFKAVRGLDGVKEATVDIGGTKVKVAVAHGLGNARKLLDDVKAGE
ADYHFIEVMACPGGCVNGGGQPKV
>gnl|CDD|131565 TIGR02513, Chaperone_protein_YscB, type III secretion system chaperone, YscB family. Members of this family include YscB of Yersinia and functionally equivalent (but differently named) proteins from type III secretion systems of other pathogens that affect animal cells. YscB acts, along with SycN (TIGR02503), as a chaperone for YopN, a key part of a complex that regulates type III secretion so it responds to contact with the eukaryotic target cell
QNLLKNLAARLGQGPFVADRQGVYHLTIDQHLVMLAQHGSELVLETPLDARMLRPGDNQNVTLLRSLMQQ
VLAWARRYPQALVLDADGQLILEARLRLDELDTHGLEEVLAQQVALLEHLMPQLEPFSVNHTASRVVWN
>gnl|CDD|274172 TIGR02514, Yop_proteins_translocation_protein_P., type III secretion system needle length determinant. Members of this family include YscP of the Yersinia type III secretion system and equivalent proteins in other animal pathogen bacterial type III secretion systems. The model describes the conserved C-terminal region. N-terminal regions are poorly conserved and variable in length with some low-complexity sequence
TPGDLILARMEATEPPHPSRDLNQLISRLVVRIYVELPSASRPAELRLTLPQLGGLEIRIARDSGGLQVE
ILASPASSQLLQQARQELLERLQRLYPGQPVRLDLSQQADSEQGSRQRRSVYEEWQAEA
>gnl|CDD|274173 TIGR02515, Putative_DNA_transport_protein_HofQ, type IV pilus secretin (or competence protein) PilQ. A number of proteins homologous to PilQ are involved in type IV pilus formation, competence for transformation, type III secretion, and type II secretion (also called the main terminal branch of the general secretion pathway). Members of this family include PilQ itself, which is a component of the type IV pilus structure, from a number of species. In Haemophilus influenzae, the member of this family is associated with competence for transformation with exogenous DNA rather than with formation of a type IV pilus; the surface structure required for competence may be considered an unusual, incomplete type IV pilus structure [Cell envelope, Surface structures]
GEKISLNFQDIPVRTVLQVIAEFTGLNIVVSDSVQGNITLRLKNVPWDQALDIVLKSKGLDKRRDGNIIY
IAPLDELAAQEKDELEAKKQIENLEPLQTELIQLNYAKASDIAKVLTGVTGGSGGLLSPRGSVTVDPRTN
TLIVTDTPENLARIRKLIAELDIPVRQVLIEARIVEATDSFSRELGVRWGITDKNGNGNGTAGGIGGNNG
TTATGAGGTGNPPFGDNLNVNLATATTAAGISFALGKIGSGRLLDLELSALESEGKGEIISSPRVLTANN
KEAKIEQGTEIPYQQTSSSGATSVEFKEAVLSLEVTPQITPDGRIIMDLLVSKDSPGVVAQAGGGVPAID
KQEINTQVLVKNGETVVIGGIYEQTQTNSEDKVPLLGDIPVLGNLFKKTGKSDEKSELLIFITPRIVN
>gnl|CDD|274174 TIGR02516, type_III_yscC, type III secretion outer membrane pore, YscC/HrcC family. A number of proteins homologous to the type IV pilus secretin PilQ (TIGR02515) are involved in type IV pilus formation, competence for transformation, type III secretion, and type II secretion (also called the main terminal branch of the general secretion pathway). The clade described by this model contains the outer membrane pore proteins of bacterial type III secretion systems, typified by YscC for animal pathogens and HrcC for plant pathogens [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
EYFYVAKQESLRALLADFAANYGIPVVVSSKVNKKVTGKFEDDNPEKFLQRLALLYGLTWYYDGNALYIY
PNSEIARAVISPRPLSANELKKALRRSGLYDPRFPWRGDPEEGTVYVSGPPAYIDLVRNAATALEKQDQG
RAGNRQVVKVFPLKYASASDRTYNYRDQKVTIPGVATILRRLLSGGRQGAGGGRASASPKISADPRTNAV
LIRDRPERMAIYEQLIQQLDVPPRLIEISAWIIDIDASDLSQLGVDWQATLGAGDRQTGFNVSAGAGLGA
TGSSIVTSDGDYFMARVNALEQTGKAKIVSRPSVLTLENVQAVLDNNRTFYVKVSGERVADLESVTAGTS
LRVTPRVIGDEGAQRQIKLNVDIEDGQQKTDGTSTVDALPEIKRTEINTQARVGHGQSLLIGGYYRDESA
DSVDGIPLLGDIPLLGNLFRSTSKEKSRVVRLFLITPKIVRD
>gnl|CDD|274175 TIGR02517, Putative_type_II_secretion_system_protein_D, type II secretion system protein D. In Gram-negative bacteria, proteins that have first crossed the inner member by Sec-dependent protein transport can be exported across the outer membrane by type II secretion, also called the main terminal branch of the general secretion pathway. Members of this family are general secretion pathway protein D. In Yersinia enterocolitica, a second member of this family is part of a novel second type II secretion system specifically associated with virulence (See). This family is closely homologous to the type IV pilus outer membrane secretin PilQ (TIGR02515) and to the type III secretion system pore YscC/HrcC (TIGR02516) [Protein fate, Protein and peptide secretion and trafficking]
LNFVDADISTVVKAISDLTGKNFIIDPRVKGKITIISPRPVTEDEAYQLFLSALRAQGFAVVPEGNGYKI
VVPRAAAKLSPGPIEDGPAPGVGGDQFVTRVFPLRNISASELVPVLRPLVSPNGDVAAYPPTNTIVVTDY
ASNINRVARIIQQLDVDGAGSVEVIPLKNASAVDIADVLNKLLGEGGKTDGGGKLSVIAPDRRNNILIRA
GSPEALERIKKLISQLDVPASEGGNVRVYYLRNADAEELAKTLQGVFGGGGNEPGSSSSPGLGGAVNPGG
SQSAQAASSASGGSVSGSADKATNSLIITASPQDYKNIRAVIKQLDVRRAQVLVEAIIVEVSLDDALELG
VQWLIAGTGGGVNFSTGSPNSGSLLGASASAISLGSAGIGLLVTSSSTTSGVGGTGGGPNLGVLLNALKQ
DTGFNVLSTPSLLTLDNQEAEINVGQEVPVLTGSYNTGTGGTNANPFNTYQRKDVGIKLKVTPQINEGGT
VRLEIYQEVSSVAPTTVGSAASGPTFNKREIKTVVLVDNGDTVVLGGLIQDKTSESVTKVPLLGDIPVLG
WLFRSTTTERTKTNLMVFITPRIIRDPEDARALT
>gnl|CDD|131570 TIGR02518, Acetaldehyde_dehydrogenase_acetylating, acetaldehyde dehydrogenase (acetylating)
DKDLYSIQQVRNLIRSAKVAQKKLANMTQEQIDKIVKAIVDAAYENAVKLAKMANEETGFGKWEDKVIKN
VFAATIVYDSIKDMKTIGILSEDKEKKVIEIAVPVGVVAGLIPSTNPTSTAIYKTLISIKARNAIVFSPH
PNAKKCIIETVKLMRKAAEEAGAPEGAIGCITVPTIEGTNELMKNKDTSLILATGGEAMVKAAYSSGTPA
IGVGPGNGPAYIERTANVKKAVRDIIDSKTFDNGTICASEQSIIVEECNKDAVVEELKKQGGYFLTAEEA
EKLGKFILRPNGTMNPQIVGKSPQVIANLAGLTVPEDAKVLIGEQNGVGNKNPYSREKLTTILAFYTEEN
WHEACELSIELLQNEGAGHTLIIHSENKDIVREFALKKPVSRMLVNTGGSLGGIGATTNLVPAFTLGCGA
VGGSSTSDNITPENLINIRRVAYGVRELEDIRKEDNTFNCIKTASNLDGVDNEELILSLVNKIIAELK
>gnl|CDD|274176 TIGR02519, related_to_type_II_protein_secretion_protein, pilus (MSHA type) biogenesis protein MshL. Members of this family are predicted secretins, that is, outer membrane pore proteins associated with delivery of proteins from periplasm to the outside of the cell. Related families include GspD of type II secretion (TIGR02517), the YscC/HrcC family from type III secretion (TIGR02516), and the PilQ secretin of type IV pilus formation (TIGR02515). Members of this family are found in gene clusters associated with MSHA (mannose-sensitive hemagglutinin) and related pili, and appear to be the secretin of this pilus system [Cell envelope, Surface structures]
YIINPEAGLLTVTATPAQIRRVEEYLESLQERIHRQVLIEAKILEVTLSDNHQQGIDWSNFNGSGLARYK
ALGAANSNDSSGNQFSSGLGFLDNIGLPTGVNSGFGFDSIINFLATFGDTKVLSNPKVMALNNQPAVISV
GDNIRYVTEESSTGTTGGTTSTASSDTRVDSVFSGIVLGVTPQISDDGKVILNVHPSISEVKPQSIDLNP
VGNGAEVALPEISVKEMSSVLRVKDGDTVVLGGLIDKKKSNTKTGLPFLGDIPGLGYLFGYKSKSKKKTE
LVIIIRPSVV
>gnl|CDD|274177 TIGR02520, putative_Type_IV_pilus_protein, type IVB pilus formation outer membrane protein, R64 PilN family. Several related protein families encode outer membrane pore proteins for type II secretion, type III secretion, and type IV pilus formation. This protein family appears to encode a secretin for pilus formation, although it is quite different from PilQ. Members include the PilN lipoprotein of the plasmid R64 thin pilus, a type IV pilus. Scoring between the trusted and noise cutoffs are examples of bundle-forming pilus B (bfpB) [Cell envelope, Surface structures, Protein fate, Protein and peptide secretion and trafficking]
VVWVDGPWVSTRPIRVKAAQQLKLPPCSLTLIIASSLSLSEVAQRITRSCGVPVVIAPDAMSALSGSSSQ
GGVGAARAIPAVLPRPDEGGRPPLPSGLGATSTQSEGPGGTAGLITDISWEGEPLGGLLDQVTSRLGLSW
KYENGAVRIFYTDTRTFQVKALPGDTALNSSVTSTSSSTAGSGSSSSGGSGNSGSTQSTAVKLESSVHND
IQQSIKSMLSSSGSWHLSGSTGSLVVTDVPEVLDRVASYIDSQNRRLTRQVLLNVKVLSVQFKGSDQTGV
DWSLVYKSLSRFGLSLANAGTSTAATAGSSAGINVVDGPFAGTTALIRALSTQGKVSVVTSPSVTTLNLQ
PAPFQIATQTGYLASQSTTVTANVGSSTDLEPGTITTGFNMTLLPDIRDDGDILLQFNISHSDLAQLRKF
TSKDGGTKVQTPDTDVRNFSQRVNLKSGQTLVLSGYESRNDTADREGVGDPDVTVLGGGRSSERDHVVLV
ILVTPVV
>gnl|CDD|131573 TIGR02521, Uncharacterized_protein_HI_0366, type IV pilus biogenesis/stability protein PilW. Members of this family are designated PilF and PilW. This outer membrane protein is required both for pilus stability and for pilus function such as adherence to human cells. Members of this family contain copies of the TPR (tetratricopeptide repeat) domain
LALVFLLALTGCVTTPDVPRSSRTTDRNKAAKIRVQLALGYLEQGDLEVAKENLDKALEHDPDDYLAYLA
LALYYQQLGELEKAEDSFRRALTLNPNNGDVLNNYGTFLCQQGKYEQAMQQFEQAIEDPLYPQPARSLEN
AGLCALKAGDFDKAEKYLTRALQIDPQRPESLLELAELYYLRGQYKDARAYLERYQQTYNQTAESLWLGI
RIARALGDVAAAQRYGAQLQKLFP
>gnl|CDD|274178 TIGR02522, Uncharacterized_lipoprotein_y4xK, pilus (Caulobacter type) biogenesis lipoprotein CpaD. This family consists of a pilus biogenesis protein, CpaD, from Caulobacter, and homologs in other bacteria, including three in the root nodule bacterium Bradyrhizobium japonicum. The molecular function is not known [Cell envelope, Surface structures]
RVLLLAATALLAGCASTDIIDVGALPDDYRQRHPIAVQESSVSIDLLVAPGDRGLSASQQDQLLGFLKDW
GRASAQTLTLIIPSAAAEAMAGEIRRVLAASGVGARNVKVMYRATASGDTGPIRVSYVAYVAQTTKCGIW
PEDLLMTKLNEAYGNFGCATQNNLAAQIANPRDLLGPRAMTPADGERRDIVIDRYRKG
>gnl|CDD|131575 TIGR02523, probable_type-4_fimbrial_biogenesis_protein, type IV pilus modification protein PilV. Pilus systems categorized as type IV pilins differ greatly from one another, with some showing greater similarty to type II or type III secretion systems than to each other. Members of this protein family represent the PilV protein of type IV pilus systems as found in Pseudomonas aeruginosa PAO1, Pseudomonas syringae DC3000, Neisseria meningitidis MC58, Xylella fastidiosa 9a5c, etc [Cell envelope, Surface structures, Protein fate, Protein modification and repair]
QAGFSMIEVLVALLVLAIGVLGMAALQLKAVRYTRSASTRTIASMLAYNLLDRMRANPTALGDGNYNTYT
GYAGTKASAVAGDCATSSCTTANAAANADLKRWLSEVKNALPGGRGSICVDSNCDNGANGEVTVKIAWV
>gnl|CDD|131576 TIGR02524, ATP-binding_protein, Dot/Icm secretion system ATPase DotB. Members of this protein family are the DotB component of Dot/Icm secretion systems, as found in obligate intracellular pathogens Legionella pneumophila and Coxiella burnetii. While this system resembles type IV secretion systems and has been called a form of type IV, the liturature now seems to favor calling this the Dot/Icm system. This family is most closely related to TraJ proteins of plasmid transfer, rather than to proteins of other type IV secretion systems
FEPKFIDDLLEHAERLGASDITIQTGEAIFAEVYGRLLKITNRELSNAELGDLINAIYGPNATTQILRGE
DIDTHYEFRPNRGERFRYRINATACHVDGHDAIQITIRAIPAEPPKLSKLDLPAAIIDAIAPQEGIVFIT
GATGSGKSTLLAAIIRELAEAPDSHRKILTYEAPIEFVYDEIETISASVCQSEIPRHLNNFAAGVRNALR
RKPHAILVGEARDAETISAALEAALTGHPVYTTLHSSGVAETIRRLVGSFPAEERIGRTIDIIETIRLCI
WQKLVPSVDEKRVALREFLVFDEEIRDILLDGDPEEITAATRKLVAEHGQLMQVDAEAKFEGGIISERLY
KIIIAGAE
>gnl|CDD|131577 TIGR02525, type_IV_pilus_biogenesis_protein, plasmid transfer ATPase TraJ. Members of this protein family are predicted ATPases associated with plasmid transfer loci in bacteria. This family is most similar to the DotB ATPase of a type-IV secretion-like system of obligate intracellular pathogens Legionella pneumophila and Coxiella burnetii (TIGR02524) [Mobile and extrachromosomal element functions, Plasmid functions]
FNFGPGLTADTLRRFFVHCSRHEVSDIHLQGGSPIVVERHGRQVPASSFPLDNLELERLVDEVFGPEIKP
TVKSGAPVDRAIQLRGDENGRYGLGRGERVRFRCNFIQATIGKLETAISLTLRVIPSDIPDLKQMGIEPD
LFNSLLPAAGLGLICGETGSGKSTLAASIYQHCGETYPDRKIVTYEDPIEYILGSPDDLLPPAQSQIGRD
VDSFANGIRLALRRAPKIIGVGEIRDLETFQAAVLAGQSGHFCLGTLHVKSPGEAISRCLQMYPPEMREA
AAFDLLSILQYIIVQRLLRTTDGKRQAVREYIVFDDSLRRKLYDVDYSKWGRYIDDILRAEQRRIADQAW
AMHQEGRIDEREAAEVIGAMEF
>gnl|CDD|131578 TIGR02526, putative_ethanolamine_utilization_protein, PduT-like ethanolamine utilization protein. This gene shows up in ethanolamine utilization operons in which a proteinaceous coat organelle is also encoded. It is closely related to the PduT protein in propane-diol operons with the same structure
MKKSLGILEFRSISKGIEMSDVFLKAAFVEVFTLRPICPGKFLIILQGDSGEVKEAIQDAKEEAGKFLVS
SYIIHSAHEDILAALKNKYSHKKVEVDAIGIMEISQVGSGLNALDEALKKSAIHLVKLTLGAGIGGKFVA
IFTGEVSSVEEGMRILQETAEPKKIIHHTVIPSPDELLKRNL
>gnl|CDD|274179 TIGR02527, hypothetical_protein_lpp0510, Dot/Icm secretion system protein IcmQ. Members of this protein family are the IcmQ component of Dot/Icm secretion systems, as found in obligate intracellular pathogens Legionella pneumophila and Coxiella burnetii. While this system resembles type IV secretion systems and has been called a form of type IV, the literature now seems to favor calling this the Dot/Icm system. This protein was shown to be essential for translocation ()
TILKALNDAIEKGPWDKSNFLRVIGKKLIAIRDRFLKRIGAASQADLEAESHLANTIALTSGQQEIYVSL
YSSDGSNLQSWEKIVGSLPRQMISRPIYADEEDIKAILKTKENKQNEAYVAIYISQSDILHLSADKAPVD
KLGKPLLTLKDKSISLENISRFVHVSGVYRYSNGRLIKN
>gnl|CDD|131580 TIGR02528, Ethanolamine_utilization_protein_EutP, ethanolamine utilization protein, EutP. This protein is found within operons which code for polyhedral organelles containing the enzyme ethanolamine ammonia lyase. The function of this gene is unknown, although the presence of an N-terminal GxxGxGK motif implies a GTP-binding site [Energy metabolism, Amino acids and amines]
KRIMFIGSVGCGKTTLTQALQGEEILYKKTQAVEYNDGAIDTPGEYVENRRLYSALIVTAADADVIALVQ
SATDPESRFPPGFASIFVKPVIGLVTKIDLAEADVDIERAKELLETAGAEPIFEISSVDEQGLEALVDYL
NS
>gnl|CDD|274180 TIGR02529, ethanolamine_utilization_protein_eutJ, ethanolamine utilization protein EutJ family protein
GVDLGTANIVIVVLDEDGQPVAGVMQFADVVRDGIVVDFLGAVEIVRRLKDTLEQKLGIELTHAATAIPP
GTIEGDPKVIVNVIESAGIEVLHVLDEPTAAAAVLQIKNGAVVDVGGGTTGISIFKKGKVIYSADEPTGG
THMSLVLAGAYGISFEEAEEYKRGQKGESEIFPVVKPVYQKMASIVKRHIEGQGVEDLYLVGGACSFSGF
ADVFEKQLGLNVIKPQHPLYVTPLGIAMS
>gnl|CDD|274181 TIGR02530, conserved_hypothetical_protein, flagellar operon protein. Members of this family are found in a subset of bacterial flagellar operons, generally between genes designated flgD and flgE, in species as diverse as Bacillus halodurans and various other Firmicutes, Geobacter sulfurreducens, and Bdellovibrio bacteriovorus. The specific molecular function is unknown [Cellular processes, Chemotaxis and motility]
SFKDVLQEEIQLAELKLSKHALERMRERNISINPDDWKKLLEAVEEAESKGVKDSLILMNDAALVVSLKN
RTVITAMDKDELKNNVFTNIDGTVII
>gnl|CDD|188231 TIGR02531, conserved_hypothetical_protein, TrpR-related protein YerC/YecD. This model represents a protein subfamily found mostly in the Firmicutes (Bacillus and allies). This family is similar in sequence to the trp operon repressor TrpR described by TIGR01321, and represents a distinct clade within the broader family described by pfam01371. At least one species, Xylella fastidiosa, in the Proteobacteria, has a member of both this family and TIGR01321. Several genomes with a member of this family do not synthesize tryptophan, and members of this family should not be considered trp operon repressors without new evidence [Unknown function, General]
RGELLDELFDAILTLKNREECYRFFDDICTINEIQSLAQRLQVAKMLKQGKTYSDIEAETGASTATISRV
KRCLNYGNDGYNIVLER
>gnl|CDD|274182 TIGR02532, Type_II_secretion_system_protein_J, prepilin-type N-terminal cleavage/methylation domain. This model describes many but not all examples of the N-terminal region of bacterial proteins that resemble type IV pilins at their N-terminus, with a cleavage site G^FxxxE followed by a hydrophobic stretch. The new N-terminal residue, usually Phe, is methylated. Separate domains of the prepilin peptidase appear responsible for cleavage and methylation. Proteins with this N-terminal region include type IV pilins and other components of pilus biogenesis, competence proteins, and type II secretion proteins. Typically several proteins in a single operon have this N-terminal domain. The N-terminal cleavage and methylation site is described by PROSITE motif PS00409 as [KRHEQSTAG]-G-[FYLIVM]-[ST]-[LT]-[LIVP]-E-[LIVMFWSTAG](14) [Cell envelope, Surface structures, Protein fate, Protein and peptide secretion and trafficking]
QRGFTLIELLVVLAILGILALIAL
>gnl|CDD|131585 TIGR02533, Type_II_secretion_system_protein_E, type II secretion system protein E. This family describes GspE, the E protein of the type II secretion system, also called the main terminal branch of the general secretion pathway. This model separates GspE from the PilB protein of type IV pilin biosynthesis [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
VRRLPIGFAKQSRVLPLSEHDGTLVVAVSDPLDLAALDEVRRLFGAPVQLIIATASEIDDAINSVYARTG
SAAAQIVEEIEGEDDLSALELDEPKIEDLLDLEDDAPVIRLVNSLLSRAVKERASDIHIEPFEKALVVRF
RVDGVLRDVLSPPKKLHAALVSRVKIMAKLNIAEKRLPQDGRISLRVGGRDIDIRVSTVPTSHGERVVMR
LLDKTAVRLDLETLGMSPELLSRFERLIRRPHGIILVTGPTGSGKTTTLYAALSRLNTPERNILTVEDPV
EYQIEGIGQIQVNPKIGLTFAAGLRAILRQDPDIIMVGEIRDLETAQIAIQASLTGHLVLSTLHTNDAAG
AVTRLIDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEATPEEIALFGISPEGPINLYRPVGCPHCNH
TGYLGRTGIYELLIVDDDLRSLIHSRADEGEIKEIARAAGMRTLRDDGLRKVLAGITTIEEVLRVT
>gnl|CDD|162905 TIGR02534, Muconate_cycloisomerase_1-2, muconate and chloromuconate cycloisomerases. This model encompasses muconate cycloisomerase (EC 5.5.1.1) and chloromuconate cycloisomerase (EC 5.5.1.7), enzymes that often overlap in specificity. It excludes more distantly related proteins such as mandelate racemase (5.1.2.2)
IQSVETILVDVPTIRPHKLATTTMTEQTLVLVRIRTEDGVIGYGEGTTIGGLWWGGESPETIKANIDTYL
APVLVGRDATEIAAIMADLEKVVAGNRFAKAAVDTALHDAQARRLGVPVSELLGGRVRDSVDVTWTLASG
DTDRDIAEAEERIEEKRHRSFKLKIGARDPADDVAHVVAIAKALGDRASVRVDVNAAWDERTALHYLPQL
ADAGVELIEQPTPAENREALARLTRRFNVPIMADESVTGPADALAIAKASAADVFALKTTKSGGLLESKK
IAAIAEAAGIALYGGTMLEGPIGTIASAHFFATFPALSFGTELFGPLLLKDEILTEPLQYEDFQLHLPQG
PGLGVEVDEDKVNFYRRD
>gnl|CDD|274183 TIGR02535, hyp_Hser_kinase, proposed homoserine kinase. The genes in this family are largely adjacent to genes involved in the biosynthesis of threonine (aspartate kinase, homoserine dehydrogenase and threonine synthase) in genomes which are lacking any other known homoserine kinase, and in which the presence of a homoserine kinase would indicate a complete pathway for the biosynthesis of threonine. These genes are a member of the (now subfamily, formerly equivalog) TIGR00306 model describing the archaeal form of 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. All of these are members of a superfamily (pfam01676) of metalloenzyme also including phosphopentomutase alkaline phosphatases and sulfatases. The proposal that this family encodes a kinase is based on analogy to phosphomutases which are intramolecular phosphotransferases. A mutase active site could evolve to bring together homoserine and a phosphate donor such as phosphoenolpyruvate resulting in a kinase activity
MKYIILIGDGMADWPLKELGGKTPLEVANTPNMDKLAKRGRCGLLRTVPEGFEPGSDVANMSLLGYDPRK
YYTGRAPLEAASIGVDLAPDDVAFRCNLVTVEDGIMKDYSAGHISTEEAATLIEALNKELGNERVRFYPG
VSYRNLLVIKGGGDRAELRTTPPHDITGKEVSKYLPSGEGAPILNDLILKSAEILKNHPVNLKRKSEGKL
PANMIWLWGQGGTPKMPTFEERYGLRGAMISAVDLLKGLGIYAGLEVIEVEGATGYLDTNYEGKVRAALE
ALETYDFVVIHVEAPDEAGHEGDLEAKIKAIELIDRRVVGPLLEALSDRDEPFRILVLPDHPTPIELKTH
TAEPVPFLLYGSGIESDSVKTFDEKSARRGGYGFVKGCELMDIFLK
>gnl|CDD|274184 TIGR02536, putative_ethanolamine_utilization_protein, ethanolamine utilization protein. This family of proteins is found in operons for the polyhedral organelle-based degradation of ethanolamine. This family is not found in proteobacterial species which otherwise have the same suite of genes in the eut operon. Proteobacteria have two genes that are not found in non-proteobacteria which may complement this genes function, a phosphotransacetylase (pfam01515) and the EutJ protein (TIGR02529) of unknown function
MDELIKRITEEICTSQQLEEKKYIVALGDSKHAIPEEMLKEFDVSWVTSEQKLADILLVSRLSIKELNNI
SHGQETNEKEKFIIAFLLEGKPIYILKPGIEYSKYENTAPYALKQKFQEYEEKLQSFGIEFIDSENYITF
ESKKEEVYGCQKQLRSLSENKKKLITEKDLKKLTKNGVSEIILSKKSILTPLAKDYAKEKNINIKLS
>gnl|CDD|274185 TIGR02537, Uncharacterized_protein, archaeal flagellin N-terminal-like domain. This model describes a hydrophobic N-terminal sequence of archaeal flagellins and other archaeal proteins. The sequence is directly analogous to bacterial sequences recognized by TIGR02532, which has cleavage motif resembling G^FxxxE followed by strongly hydrophobic sequence. Such sequences are the recognized for cleavage and methylation, and include pilins and other pilus components and competence and type II secretion secretion proteins. In the present family, the E is not conversed and sequence differs enough that there is no overlap between this family and TIGR02532
RKGISPIIGTIILIAITIVLAGAA
>gnl|CDD|274186 TIGR02538, Type_IV_pilus_assembly_protein_PilF, type IV-A pilus assembly ATPase PilB. This model describes a protein of type IV pilus biogenesis designated PilB in Pseudomonas aeruginosa but PilF in Neisseria gonorrhoeae; the more common usage, reflected here, is PilB. This protein is an ATPase involved in protein export for pilin assembly and is closely related to GspE (TIGR02533) of type II secretion, also called the main terminal branch of the general secretion pathway. Note that type IV pilus systems are often divided into type IV-A and IV-B, with the latter group including bundle-forming pilus, mannose-sensitive hemagglutinin, etc. Members of this family are found in type IV-A systems [Cell envelope, Surface structures, Protein fate, Protein and peptide secretion and trafficking]
GLGRILVKAGLLTETQAQAALEEAQASGQPLVQYLIQNGLLDPKQLAEFLSREFGVPLLDLNAFDPDALP
VQLVSEELIQKHQALPLFKRGNTLFVAVSDPTNISALDDIRFATGLNVEVVIVEEDKLSALIEKYYGGSD
SLAKELGDEDIGDLEELDVDAIDDEGPDDIEQDAVDDDAPIVKFVNKILLDAIRKGASDIHFEPYEKSYR
VRFRIDGILHEVAQPPLALANRIAARIKVMSRLDIAEKRIPQDGRIKLKLSKSKAIDFRVSTLPTLFGEK
VVLRILDSSAAQLDIDKLGFEPDQKALFLEAIHKPQGMVLVTGPTGSGKTVSLYTALNILNTEEVNISTA
EDPVEINLPGINQVNVNPKIGLTFAAALRSFLRQDPDIIMVGEIRDLETAEIAIKAAQTGHLVLSTLHTN
DAPETLARLVNMGIAPFNIASSVNLIMAQRLARRLCSHCKAPEEVPAEALLELGFTQEDLADLKLYGPVG
CDECSNTGYKGRVGIYEVMPMSEEIAELILKGGNALQIAELAQKEGMRTLRRSGLLKVKQGVTSLEEVLR
VTVD
>gnl|CDD|274187 TIGR02539, O-phospho-L-seryl-tRNA:Cys-tRNA_synthase, O-phospho-L-seryl-tRNA:Cys-tRNA synthase. Aminoacylation of tRNA(Cys) with Cys, and cysteine biosynthesis in the process, happens in Methanocaldococcus jannaschii and several other archaea by misacylation of tRNA(Cys) with O-phosphoserine (Sep), followed by modification of the phosphoserine to cysteine. In some species, direct tRNA-cys aminoacylation also occurs but this pathway is required for Cys biosynthesis. Members of this protein catalyze the second step in this two step pathway, using pyridoxal phosphate and a sulfur donor to synthesize Cys from Sep while attached to the tRNA
TRSLTREFINLNPIQRGGVLPKEARKALYEFGDGYSVCDYCHGRLDEVTKPPIKDFLEDLAEFLGMDCAR
PTHGAREGKFAVMHALCKEGDYVVLDGNAHYTSYVAAERAGLNVAEVPETGHPEYKVNPEGYKEVIDEVE
DEGKPVGLALLTHVDGEYGNLNDAKKVAKICREKGVPLLLNCAYTVGRMPVNGKEVKADFIVGSGHKSMA
ASAPCGVLAMSEEWEDKVLRTSRKFPVKEVEMLGCTSRGAPIVTLMASFPHVVERVKRWDEEVKKTRYFV
DELEDIGFKQLGIKPKEHDLVKFETPVFHEIAKKHKRRGFFLYEELKKRGIGGIRAGQTKEIKMSVYGLT
WEQVEYVVDAFKEIVEEYK
>gnl|CDD|131592 TIGR02540, Glutathione_peroxidase_7, putative glutathione peroxidase Gpx7. This model represents one of several families of known and probable glutathione peroxidases. This family is restricted to animals and designated GPX7
DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESE
PDSSKEIESFARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEE
PVEEIRPEITALV
>gnl|CDD|274188 TIGR02541, Peptidoglycan_hydrolase_FlgJ, flagellar rod assembly protein/muramidase FlgJ. The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring
LAHDAQSLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATPKDGLFDSQQTRFYTQMLDQQMAQ
QLSANGGIGLADMIVAQLTKGQGNEPSEGAARGAAPSPLVYRPRLDPKPRRIVKALIESVELSRPRGRSH
AESVPGHPKSFVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQG
KVVTTMTTEYVDGVAQKLTAKFRSYSSYEEAFSDYARLLNNNPRYEAVLQQRSAESFARGLQRAGYATDP
RYARKLLQVIQSLA
>gnl|CDD|211749 TIGR02542, T_forsyth_147, TANFOR domain. The longest predicted protein in Tannerella forsythia (Bacteroides forsythus) ATCC 43037 is over 3000 residues long and lacks homology to other known proteins. Immediately after the signal sequence are four tandem repeats, approximately 147 residues long. This model describes that repeat, plus homologous single copy N-terminal domains in other large bacterial proteins. We designate this region the TANFOR domain. Many proteins with this domain also have fibronectin type III domains
NAIVNQTVQVLPPYTNKLSDYFESPGKIQSVITVTQYPDNDALLYVHGTLEQVDGNIRIGSGQTPASVRI
QGTPSGNNVIFPPYTLTYNELRQIFREPMVYQGITREQVQRDGLPEGSYRICFRLFNATQFEEISRSCSA
PFRIE
>gnl|CDD|274189 TIGR02543, fibronectin_type_III_domain_protein, Listeria/Bacterioides repeat. This model describes a conserved core region, about 43 residues in length, of at least two families of tandem repeats. These include 78-residue repeats from 2 to 15 in number, in some proteins of Bacteroides forsythus ATCC 43037, and 70-residue repeats in families of internalins of Listeria species. Single copies are found in proteins of Fibrobacter succinogenes, Geobacter sulfurreducens, and a few bacteria [Unknown function, General]
PTKTGYTFVGWTGDSTGTPVKNFTIPSGSTGDLTLYAKWTPNT
>gnl|CDD|274190 TIGR02544, YOP_proteins_translocation_lipoprotein, type III secretion apparatus lipoprotein, YscJ/HrcJ family. All members of this protein family are predicted lipoproteins with a conserved Cys near the N-terminus for cleavage and modification, and are part of known or predicted type III secretion systems. Members are found in both plant and animal pathogens, including the obligately intracellular chlamydial species and (non-pathogenic) root nodule bacteria. The most closely related proteins outside this family are examples of the flagellar M-ring protein FliF [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
LRRKLLLLLLLLLLTGCKVDLLYSGLSEREANEMLAVLMRHGIDAEKEGSGKGGYTISVEESDFARAVEL
LRQYGLPRQRFVNLGELFPKDGLVSSPQEERARYLYAIEQRLEQTLSQIDGVISARVHVVLPENDNNGRP
KKPSSASVFIKYRPGLNLDALIPKIKRLVANSIPGLDYDNVSVVLVPAEERQS
>gnl|CDD|274191 TIGR02546, III_secr_ATP, type III secretion apparatus H+-transporting two-sector ATPase [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
QPVRVRGRVTEVSGTLLKAVLPGARVGELCLIRRRDPSQLLAEVVGFTGDEALLSPLGELHGISPGSEVI
PTGRPLSIRVGEALLGRVLDGFGRPLDGKGELPAGEIETRPLDADPPPPMSRQPIDQPLPTGVRAIDGLL
TCGEGQRIGIFAGAGVGKSTLLGMIARGASADVNVIALIGERGREVREFIEHHLGEEGRKRSVLVVSTSD
RPSLERLKAAYTATAIAEYFRDQGKRVLLMMDSLTRFARALREIGLAAGEPPARGGYPPSVFSSLPRLLE
RAGNGEKGSITALYTVLVEGDDMNDPIADEVRSILDGHIVLSRALAERNHYPAIDVLASLSRVMSQVVST
EHRRAAGKLRRLLATYKEVELLIRLGEYQPGSDPETDDAIDKIDAIRAFLRQSTDEYSPYEETLEQLHAL
VA
>gnl|CDD|274192 TIGR02547, CRISPR_system_Cascade_subunit_CasA, CRISPR type I-E/ECOLI-associated protein CasA/Cse1. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This model family, represented by CT1972 from Chlorobium tepidum, is found in Ecoli subtype CRISPR/Cas regions of many bacteria, most of which are mesophiles, and not in Archaea. It is designated Cse1
NLLDEPWIPVRDKDGGAVEVLLLQDLLRSDRVVDLAGPRPDQELAALRLLLAILQRALAPKDTEDWKEIW
RDGLPADKLRKYLNPWRDRFDLFHPTPPFMQDADLLAKDKTPVAKLLAETPGANNILFNKDHFVKRGLPE
ATCGHCAALALFSLQLNAPSFGGGYRVGLRGGGPVTTLVLGQGSYEGGTLWETLLLNLVPQEEPDPDPTD
PQGFDWPPPERVSEQPGEVIPPLPVGPLRGLTWMPRRIRLLDPDGGNVLLGGVRTKNYGLTYGGLWPHPL
DPYLWTVKKGEGEPKSVKLQPERLLWRDLDSLLLTEDSQNAAEQPALLAELFGQAELVSNKVRLWLFGLD
YDNNKARIWYIARDPLPFNSGELQLWPRLAIAVGAAVQILEILRNALKNAVFALAEAAKGKDFKGAGVSF
WLEAETRFWRLAESLFPDLLYWRQADDADEALAAWGTALLLLATDVFDEAVARYPYRPIDAIRARAAARK
DLYKSLRELKAQ
>gnl|CDD|274193 TIGR02548, CRISPR_system_Cascade_subunit_CasB, CRISPR type I-E/ECOLI-associated protein CasB/Cse2. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This model family is found in Ecoli subtype CRISPR/Cas regions of many bacteria, most of which are mesophiles, and not in Archaea. It was designated Cse2 originally, and renamed CasB based on its characterization in the CASCADE complex
LYEALERLDEGDPGARAALRAGLRRCAGPDPLLLSFVFPRLLKGDQWETPERRAPYLVAALAAAAGQSLK
VGSHTPGISLARALAEKGRSLASNASERRFRALLEADARDELLRRLRRLLSLLKSLAISVDYAQLARDLL
RWNDPSQRVRRRWARDYYRA
>gnl|CDD|274194 TIGR02549, CRISPR-associated_protein_Csx1_1, CRISPR-associated DxTHG motif protein. This model describes a short region highly conserved between two otherwise substantially different CRISPR-associated (cas) proteins, TIGR02221 and TIGR01987. This region includes the motif [VIL]-D-x-[ST]-H-[GS]
EIILDVTHGFNFMPLLAYEAV
>gnl|CDD|274195 TIGR02550, Flagellar_hook-associated_protein_3, flagellar hook-associated protein 3. This protein family consists of flagellar hook-associated proteins designated FlgL (or HAP3) encoded in bacterial flagellar operons. A N-terminal region of about 150 residues and a C-terminal region of about 85 residues are conserved. Members show considerable length heterogeneity between these two well-conserved terminal regions; the seed alignment 486 columns, 393 of which are represented in the model, while members of this family are from 287 to over 500 residues in length. This model distinguishes FlgL from the flagellin gene product FliC [Cellular processes, Chemotaxis and motility]
RVSTNMLYNNSLNSITNNQSRLAKLQQQLSSGKRINKPSDDPVAAAQALNLNQELAQLEQYQKNIDDAKN
WLSQTETALSSVGDVLQRARELAVQAANGTLSDDDRKAIAKEIKQLLDQLVNLANTKDGNGRYIFSGTKT
DTPPFSEDEGGEVTYNGDGGQRKVQVASNRSMPIGHPGDKVFMSIPNNDKSVFSTGDDLIDALKKLEDAL
SSGDAKAALSASLNDLDKALDNVLSARAEVGARLNRLENLNSRLSEQKLQLTEQLSDLEDVDLAEAISDL
NMQQAALQAALKTFAKIQQLSLFDYL
>gnl|CDD|274196 TIGR02551, translocation_protein_Q, type III secretion system apparatus protein YscQ/HrcQ. Genes in this family are found in type III secretion operons. The gene (YscQ) in Yersinia is essential for YOPs secretion, while SpaO in Shigella is involved in the Surface Presentation of Antigens apparatus found on the virulence plasmid, and HrcQ is involved in the Harpin secretory system in organisms like Pseudomonas syringae [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
ALAELPVSSGVWLALALAGQTLSLWLRGAELQLWLAPALATAAFASLPLELLLALLLAALAPAGLLLTEL
VALGESPASLPAPQLSPLALRLGLTLEGLDGPEPVLLLATLALWLTWVAAALLAALPARPTVLLKALPLP
VRLEIGSSRLALDELRSLEVGDVLLLDNPSAARAGLGALLLWGPPWARVLLADDRLELIDGITADNLDLS
DLTDTESPDEPAAPTPEVDLDQLPVTLEFELGRLTLTLAELAALQPGSVLELNVPVDGPVRLRANGRLLG
RGELVDVGGRLGVRILEL
>gnl|CDD|274197 TIGR02552, Low_calcium_response_locus_protein_H, type III secretion low calcium response chaperone LcrH/SycD. Genes in this family are found in type III secretion operons. LcrH, from Yersinia is believed to have a regulatory function in the low-calcium response of the secretion system. The same protein is also known as SycD (SYC = Specific Yop Chaperone) for its chaperone role. In Pseudomonas, where the homolog is known as PcrH, the chaperone role has been demonstrated and the regulatory role appears to be absent. ScyD/LcrH contains three central tetratricopeptide-like repeats that are predicted to fold into an all-alpha-helical array
SGGATLKDLLGLDSEQLEQIYALAYNLYQQGRYDEALKLFQLLAAYDPYNSRYWLGLAACCQMLKEYEEA
IDAYALAAALDPDDPRPYFHAAECLLALGEPESALKALDLAIEICGENPEYSELKERAEAMLESL
>gnl|CDD|274198 TIGR02553, pathogenicity_island_1_effector_protein, type III effector protein IpaD/SipD/SspD. These proteins are found within type III secretion operons and have been shown to be secreted by that system
PSDAGARAMTDDDLRAAGVDRRVLEQALGKAIDEFQSLRLPPPISDERIDGRTVDGRRANLTLFDDARSG
VRGSAEQQRNLLSRLDAPTEALGGTLPMAGDEGGIQDDPIWDMLSDVIGKIGDSYLGVYENVVEGYTDFY
QAFSDILSKMQDWISPGKDGNNVKLDVGKLKALLQQLIDHLPNKKNVLFPAQDGGMQLPKEADARRWRKE
LGLPVSCLQISDSGYVVTVDPTPLIKMRDDLPPLGTGTELEWDNAKYQAWQSGFKAQEENIKNTLQTLTQ
KYSNANSLFDNLVKVLSSTISSLLETAKSFLQI
>gnl|CDD|131605 TIGR02554, type_III_secretion_system_protein_BsaM, type III secretion system protein PrgH/EprH. In Samonella, this gene is part of a four-gene operon PrgHIJK and in general is found in type III secretion operons. PrgH has been shown to be required for secretion, as well as being a structural component of the needle complex [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
DSGLEALQVRLLNSPLFGCEFALPSGETLFCVGEQVALDAPGEHPERPADSLFIPLRAGGVNFELRFDAA
SGDFELDFLSADGCESQRAAFNTPCRVGDLAFALRPQREPWSEEVMHYAEHAPSRAAPAAEPGAPGSRFA
LALGALLVAGVALAGLAWWQNSGQRQLAELNGLLGGAPVRFAVLPGRDGRIYVAAASQRDAEWARQALLR
AALPEKIEVAVIGAERQRVSRWLDEAGPQLAFYRLRLDAPRHPELWLSRQRNAAPAAARARLIGELRRLM
PYARDVRIIDADDGAAEQQAENGLDKQALPYRRLARRGGVTFVIAGALDDEELARARQFVDSYYRKWGGR
YVQFAIELKDDWLKGKSFRYGGDGYVKLDHGHWYFPQPL
>gnl|CDD|131606 TIGR02555, MxiK_protein., type III secretion apparatus protein OrgA/MxiK. This gene is found in type III secretion operons and has been shown to be essential for the invasion phenotype in Salmonella and a component of the secretion apparatus. The protein is known as OrgA in Salmonella due to its oxygen-dependent expression pattern in which low-oxygen levels up-regulate the gene. In Shigella the ghene is called MxiK and has been shown to be sessential for the proper assembly of the secretion needle complex
LMRIIYDPLSYIHPSRLNLPGELLENPAARSIANEWIINHYRLSCDEDFALRGSPTAMFVDNWNLLPQIA
YLIGCQRLRARLAERGRFINLPDWVQSFLAMPLEKSEKAACLGIPDPAAIIAWGFACLLAWLENLPRALY
QRLNLLFPDFLEGLLTPLPRALTLLSPSAFQYAKNHPTLIPASCL
>gnl|CDD|274199 TIGR02556, hypothetical_protein_MM_0564, CRISPR-associated protein, TM1802 family. This minor cas protein is found in CRISPR/cas regions of at least five prokaryotic genomes: Methanosarcina mazei, Sulfurihydrogenibium azorense, Thermotoga maritima, Carboxydothermus hydrogenoformans, and Dictyoglomus thermophilum, the first of which is archaeal while the rest are bacterial
MLENIKNIGKIVRTTSAEDFVSNLVEYDESGNYKFIVIMNFSLDSVFINIYSREFKKQVLEEKVFLYRAK
GSNPQDRVTPTYKICSAKAGNGSSIVKLFDVLLGGTLKNLLKEVKDKLFKNKEKVRYCLDLSKIGNGELT
PPIDGKFLKEIENLWKIFEEKLGLKKKKISGTCHLCGERSDITYDSFVYKFYTTDKPGFSSDKGFSKNFS
ICRDCYKDVIYGRKFIQENLSTRFGGNDLWIIPGLFFNGKELKESWIRISREFKKSTFLSFERRIERELD
EINEFEEIKDGGTVDFLFYEKEKSAEKIKLYIKDVHPSRVSKIRESIKKVESIFGEENNWFLGNFDILFL
FPIRRDKIFNYKKMLDLYEDIFLEGKIDKDLLLDYFVSKIKVDFFEGYNTKMVANTDMGFIVKLGLLLKL
FEKLNLITGGDSMPKFEDDKDFFEYISKFFDSPEKKALFLLGYLIGELLYEQISGRDLSAKKKNLNKLKG
LKISAKDLIGLLNEVFEKLDQYGIRGKGEKELSVETSKMLLHAGSWKLSEDEIVYYFVSGMALNT
>gnl|CDD|274200 TIGR02557, HRP-associated_protein, type III secretion protein HpaP. This family of genes is always found in type III secretion operons, althought its function in the processes of secretion and virulence is unclear. Hpa stands for Hrp-associated gene, where Hrp stands for hypersensitivity response and virulence
IIQGARLARPAPADPARPARRRTPLAQLRRRDALAYAPPPRPEPPPPCDEDRPEPRADTRASDPPPEAPT
DADPAQPPDDPDASAHTAAIASGAAGARVVRVCSERQRGERMTEHLAREIAAFCASQAIRSAGCWEASLD
LDPKLLPETTLHLRLSPFTLSLRFETPDPRTRHLLSTHRDTLEARLHALLGQQRDIELEVW
>gnl|CDD|131609 TIGR02558, hypothetical_protein_BPSS1398, type III secretion protein HrpB2. This family of genes is found in type III secretion operons in a narrow group of species including Xanthomonas, Burkholderia and Ralstonia
VPRTALQLSLTPATNPTAANPPAELAERFQALMRKAPMEPPAAPHSAGPSAISRLVAAQDAEVRASVDDV
AAVERRAPMMSLEEINVETMRLTYEAAATQLDMEAKMSVVNSGKNAIQTLMKNQ
>gnl|CDD|131610 TIGR02559, putative_type_III_secretion_protein, type III secretion protein HrpB7. This family of genes is found in type III secretion operons in a narrow range of species including Xanthomonas, Burkholderia and Ralstonia
RRASAWRTLLERKTRRDARLRAELAERRAALQSADRELAEKVSQAEAKADRLHRHAARIDDLATGTASFT
IDAYLQCRAYRDVLEAHLGAAEQAEAAARAALQALAAALAAKKREIARLDAQIDVCRERAERLRRAGEAA
REEALEEEAEEAALGRRL
>gnl|CDD|131611 TIGR02560, putative_type_III_secretion_protein, type III secretion protein HrpB4. This family of genes are always found in type III secretion operons in a limited number of species including Burkholderia, Xanthomonas and Ralstonia
DNTPIQAAAACLQRYTANLARLAEWLHASWVAAWLGPAAASGHAAAPRAACSRVIQAWLGWSGPSLSALL
ERANRLAVLPPALLLRVLRMRALFSRRTAVRRCIDRARLSRLEAWVGPALVAALAAVRQNASAGLPVPLA
PRDADQLAWEGWRLLQADGVWPPPSVIRLMRLALPALATAQVLALAADGASEAFLAALPSLMPEASWLFG
>gnl|CDD|131612 TIGR02561, putative_type_III_secretion_protein, type III secretion protein HrpB1/HrpK. This gene is found within type III secretion operons in a limited range of species including Xanthomonas, Ralstonia and Burkholderia
EYIQCSNRLLGGLIEVLMYALRSADPYDAQAMLDALRVLRPNLKELDMFDGWLLIARGNYDEAARILREL
LSSAGAPPYGKALLALCLNAKGDAEWHVHADEVLARDADADAVALVRALLGAQQPPASVAEAAAEVAETA
DMAAFHTSQYLRA
>gnl|CDD|274201 TIGR02562, conserved_hypothetical_protein, CRISPR-associated helicase Cas3, subtype I-F/YPEST. The helicase in many CRISPR-associated (cas) gene clusters is designated Cas3, and most Cas3 proteins are described by model TIGR01587. Members of this family are considerably larger, show a number of motifs in common with TIGR01587 sequences, and replace Cas3 in some CRISPR/cas loci in a number of Proteobacteria, including Yersinia pestis, Chromobacterium violaceum, Erwinia carotovora subsp. atroseptica SCRI1043, Photorhabdus luminescens subsp. laumondii TTO1, Legionella pneumophila, etc
MNILLISQCEKRALTETRRILDQFAERTGDRVWQTPITQEGLKTLRKLLRKTARRNTAVACYWIFGMNRS
ELLWIVGDKRRFNHQGAVPTNSTQRDILRALDENEWVSAESISLLAGLAGLLHDIGKASVHFQNKLSPEM
NGPKIADDYRHEWVSLRLFQAFVECQTDNGWLWRLAWKNLDDGTDKFTTLDSQEIEDGLDNHFSPFAALP
PLAAVDYWLVTSHHRLPVEEALKNDPLALPHYENHARTLVPSLEQIWNPAVWVSGHPTPQAFWQFPCGGP
LQDAIWKKHQARMAKLALLIPKLKTDQLLYWKFLALHSRLALMLADHHYSAQQYSLQWQELNVALFANTK
LKNIDQDKKAKLQKQPLDEHLIGVGQRALRIARMLPDLSRELPAIQTHKYFCQRSAHPRFRWQNKAFNLA
QKLRQKSPEQGAFGVNMASTGCGKTLANARAMYALRDDKQGARFAIALGLRSLTLQTGHALKTRLNLSDD
DLAVLIGGTAVQTLFDLSKEKIEQVDEDGSESAPIFLAEGQDCNLPDWDGPLDTIELLGRLSLDDKEKTL
LAAPVLVCTIDHLIPATESHRGGHHIAPMLRLMSSDLILDEPDDYEPEDLPALLRLVQLAGLLGSRVLLS
SATLPPALVKTLFRAYEAGRQMYQALYGQPKKPLNICCAWVDEPQVWQADCNQKSEFIQRHQDFLRDRAV
QLAKKPVRRLAELLSLSSLPRENESTYLALAQSLLEGALRLHQAHAQTDPKSEKKVSVGLIRVANIDPLI
RLAQFLYALLAEEKYQIHLCCYHAQDPLLLRSYIERRLDQLLTRHKPEQLFQDDEIIDLMQNSPALNHLF
IVLATPVEEVGRDHDYDWAIADPSSMRSIIQLAGRVNRHRLEKVQQPNIVILQWNYRYLERRDIQRRPVY
IRPGFETYRVSRLSTHDLDQLLELLPYDHISALPRIARLRFLQPGTLFADLEHEQIKDFLNGYFADQGLQ
LASRWDRKAAILTANLYRITPFRESNYQEEYMFELAESDEVDKQVFGFLEKATKNLKYRKYGLVWEDVKL
EEAAGKSPWWLASTLQQLKDLAEELNIALEEGCRTFGCVSLPYNRDEVPTWHYHPGLGVF
>gnl|CDD|274202 TIGR02563, conserved_hypothetical_protein, CRISPR-associated endoribonuclease Cas6/Csy4, subtype I-F/YPEST. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family, typified by YPO2462 of Yersinia pestis, is a CRISPR-associated (Cas) family strictly associated with the Ypest subtype of CRISPR/Cas locus. This family is designated Csy4, for CRISPR/Cas Subtype Ypest protein 4
HYLDITLLPDAEFSNEVLMNACYKKLHRALADYETRRIGVSFPLYGYQETLGRQLRLHGTAEDLDKLHSR
RWLSGLSDYASISEISTVPADCVKRRTVRRKQTKSSAARLRRRLERRQGINDEEARPRAPDKTTQRANLP
YLSLKSASSGQRFRLFIEQGERAPESVTGKFNAYGLSNTATVPWF
>gnl|CDD|274203 TIGR02564, conserved_hypothetical_protein, CRISPR type I-F/YPEST-associated protein Csy1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family, typified by YPO2465 of Yersinia pestis, is a CRISPR-associated (Cas) family strictly associated with the Ypest subtype of CRISPR/Cas locus. This family is designated Csy1, for CRISPR/Cas Subtype Ypest protein 1
AKYRPDIWLTDAARRAGQLKLGTHISKGIHSDSRGSNVFNFEQKFVDHDYVGSHTLANNALDVVGNAAAL
DLVKLLQWEHEGGSLRALLWAGDPRLLRCFADDPELSEQWQTTFQTILTANRNPASHKLAKQLYWPLPPT
SDNRDNYHLLSPLYSSSLTHAFYQRIEAIRFSEENKNARQARRKSVWHQKRYADYLDLAVQKLGGTKPQN
ISQLNSSRKGRSYLLPSLPPVWKNIDKPPIKFSSILESRFFSKSLARRTLDQLKILLLVVKPKENNYDIR
NMRLAALDQIIEQLLSIVAEIQNLPAGWSKDCDLKRAEQYWLDPKRADLDEVFKAEREKGDWDQEVEKDF
ARWLNKRLQHDRLEFGDVEHHEWRREMLFKIRER
>gnl|CDD|274204 TIGR02565, conserved_hypothetical_protein, CRISPR type I-F/YPEST-associated protein Csy2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family, typified by YPO2464 of Yersinia pestis, is a CRISPR-associated (Cas) family strictly associated with the Ypest subtype of CRISPR/Cas locus. This family is designated Csy2, for CRISPR/Cas Subtype Ypest protein 2
LIVLPRIRVQNANAISGPLTYGFPALTAFTGFMHALSRKLGASHGLTLHGVGVACHGQQLHTYGSAQRWD
RVFILTRNPVTKNGKTAAIIEEGRCHLTVSLVIGVSGSDIAPTDDALQALLEHLKQLLKQQRLAGGTVIE
FIERVQVQTLPENEDEAATRRLLPGFALLDRQDLLAEHTQRLQQTNPQATALDAWLDFAALKHIPERAFS
DETNWWTYSVKKGRGWLVPIPVGYQAISPLYAPGQVDNARDPHYPFQFVEALYSLGEWVFPHRIVDIDQL
LWWTYYDAQNDLYLCR
>gnl|CDD|274205 TIGR02566, conserved_hypothetical_protein, CRISPR type I-F/YPEST-associated protein Csy3. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family, typified by YPO2463 of Yersinia pestis, is a CRISPR-associated (Cas) family strictly associated with the Ypest subtype of CRISPR/Cas locus. This family is designated Csy3, for CRISPR/Cas Subtype Ypest protein 3
KLPSVLSFERKLDPSDAIFFAGNWDGKDEWTPLPIREKAVRGTISNRLKKYKYDTQIDDPAKLDAEIQKA
NLQRVDVAALPYDADTLKLSFTLKVLASLAKPSKCNDAEYKQTLLQTVKLYIEEQGFEELARRYAENIAN
GRWLWRNRVGAESIEIRVTWPWEDEKAIWPFDAIRFNLRGFAQPSKDLDALAKLIAQGLSGENGFAILEV
TAYVRLGTGQEVYPSQELVLDKSKGGKKSKILYAVDQDGESIAALHSQKIGNAIRTIDTWYPDADENGPI
AIEPYGAVTELGKAYRQPKTKKDDFYTLFDNWVLKEQLPAVEQQHFVMAVLIRGGVFGEKG
>gnl|CDD|131618 TIGR02567, Exoenzyme_S_synthesis_protein_B, type III secretion system chaperone YscW. This family of proteins is found within type III secretion operons. The protein has been characterized as a chaperone for the outer membrane pore component YscC (TIGR02516). YscW is a lipoprotein which is itself localized to the outer membrane and, it is believed, facilitates the oligomerization and localization of YscC
LLILLLLLTGCASQPFPVQSQANVYGWVSMEYHLPRSAYIEVSMCQVVEGKVLTVAEQHYRGVQLPVQYS
FLLNPIQAGKGELYLRGKLSWQGQRAVQAEAQQIFRAGQKVVLRLFPIECYPNC
>gnl|CDD|274206 TIGR02568, type_III_secretion_system_protein, type III secretion regulator YopN/LcrE/InvE/MxiC. This protein is found in type III secretion operons and, in Yersinia is localized to the cell surface and is involved in the Low-Calicium Response (LCR), possibly by sensing the calcium concentration. In Salmonella, the gene is known as InvE and is believed to perform an essential role in the secretion process and interacts with the proteins SipBCD and SicA.//Altered name to reflect regulatory role. Added GO and role IDs . Negative regulation of type III secretion in Y pestis is mediated in part by a multiprotein complex that has been proposed to act as a physical impediment to type III secretion by blocking the entrance to the secretion apparatus prior to contact with mammalian cells. This complex is composed of YopN, its heterodimeric secretion chaperone SycN-YscB, and TyeA. 3[SS 6/3/05] [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
QGESLQSVSDASQSLADAAEELRFAELEAARKALQSRKVALEEKAELLSEYLERVPDTDADQKLKELRAE
LSGQAAGLEQLLALARGAFPDPSDQYLALRAALQRLELDPAERKALEEAAQALLELEDGPTIRAGINTAL
AAAAFADQLDLKASALRDLYRQAVSDQSSLVQLLSDLIERYGAQRFDIVLDFLIRALAADLSAQGPSTDS
AQLQVLMSDLTQLRHLLTALDQCESLLQRL
>gnl|CDD|131620 TIGR02569, conserved_hypothetical_protein, TIGR02569 family protein. This protein family is found, so far, only in Actinobacteria, including as least five species of Mycobacterium, three of Corynebacterium, and Nocardia farcinica, always in a single copy per genome. The function is unknown [Hypothetical proteins, Conserved]
EQLPEHVRDAFGLAGAPPIQLGAAWDGGWRVGNVVFSMVADPARSAWSARVRETLFPDGVRVVRPVRSTD
GRYVVAGWRADTFVAGTPEPRVDETVVAALRLHEALGDLERPGPAAPWAEIDVFVAADRAAWEERPLQSV
PPGVPTAPPAADPQRSIDLINQIAGLLKPIKSPNQVVHADMYATTLYAGTQPPGVTDLVPVWRPAGWTAA
VAIVDALLWGAVDEGIIERFSHLPEWPQLLLRALMFRLAVYALHPRSTANAFPNLAHVAATV
>gnl|CDD|274207 TIGR02570, CRISPR-associated_protein_Csb1, CRISPR-associated protein GSU0053/csb1, Dpsyc system. Members of this family are found in association with CRISPR repeats and other CRISPR-associated (cas) genes in the genomes of Geobacter sulfurreducens PCA and Desulfotalea psychrophila LSv54 (both Desulfobacterales from the Deltaproteobacteria), Gemmata obscuriglobus (Planctomycete), and Actinomyces naeslundii MG1 (Actinobacteria). This CRISPR/Cas type is designated Dpsych
AAISIREPLMPLEGADGVLFPATFAPTGFPGVAIDKGPDGGKACLIDSVGSQANRIEAVLADTGNNNWYA
PLLPQIVVLVGDKETNSVELGHRAGDAIIRCSELQGELKAAFNDDASRPLVLASNATALLKIAPTSLLFG
VWDSKDTGQAKLPRLVTSEIRAYDVRPLTRGA
>gnl|CDD|131622 TIGR02571, putative_dCMP_deaminase, ComE operon protein 2. This protein is found in the ComE operon for "late competence" as characterized in B. subtilis. Proteins in this family contain homology to a cytidine/deoxycytidine deaminase domain family (pfam00383), and may carry out this activity
ERIKWDQYFMAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGCYVVDGHCVRTIHA
EMNALLQCAKFGVSTEGAEIYVTHFPCLQCTKSIIQAGIKKIYYAQDYHNHPYAIELFEQAGVELKKVPF
DPSYLAQYNTQ
>gnl|CDD|131623 TIGR02572, Low_calcium_response_locus_protein_R., type III secretion system regulator LcrR. This protein is found in type III secretion operons and has been characterized in Yersinia as a regulator of the Low-Calcium Respone (LCR) [Protein fate, Protein and peptide secretion and trafficking]
MADPLIPWFEETGLEVTPHCLQKSPIQLGWRVEVDGCELAWRVEEERVWIVLLRRVSQRRGLANPFAALY
LLAEAAIALLGPDWRLYGNVDVLAGSPLSSQRLARFYRRWTGASEDQQGWFELEASDVITLKKMKKRQK
>gnl|CDD|131624 TIGR02573, Low_calcium_response_locus_protein_G., type III secretion protein LcrG. This protein is found in type III secretion operons, along with LcrR, H and V. Also known as PcrG in Pseudomonas, the protein is believed to make a 1:1 complex with PcrV (LcrV). Mutants of LcrG cause premature secretion of effector proteins into the medium
EDPFTKTLQAAELAIRDSDERNDLLQEMWQGLGLGPVAGEVLFGGLNAELMQHAEQELLEEVQRRRSQQP
QQGEQGKRPRRPTMMRGMII
>gnl|CDD|131625 TIGR02574, hypothetical_protein, putative addiction module component, TIGR02574 family. Members of this family are bacterial proteins, typically are about 75 amino acids long, always found as part of a pair (at least) of two small genes. The other in the pair always belongs to a subfamily of the larger family pfam05016 (although not necessarily scoring above the designated cutoff), which contains plasmid stabilization proteins. It is likely that this protein and its pfam05016 member partner comprise some form of addiction module, although these gene pairs usually are found on the bacterial main chromosome [Mobile and extrachromosomal element functions, Other]
LALSPDERIQLVEDIWDSIAAEAKHLILTEAQKAELDRRLADYKADPSKASPWEEVRARIRKR
>gnl|CDD|274208 TIGR02577, thermophile-specific_DNA_repair_system, CRISPR-associated protein Cas10/Cmr2, subtype III-B. This model represent a Crm2 family of the CRISPR-associated RAMP module, a set of six genes recurring found together in prokaryotic genomes. This gene cluster is found only in species with CRISPR repeats, usually near the repeats themselves. Because most of the six (but not this family) contain RAMP domains, and because its appearance in a genome appears to depend on other CRISPR-associated Cas genes, the set is designated the CRISPR RAMP module. This protein, typified by TM1794 from Thermotoga maritima, is designated Crm2, for CRISPR RAMP Module protein 2
TLVVITIGPVQEFIAKARKLRDLWAGSYLLSYLIWKAIEFLVEKFGPDHVIFPSLRGNPFFDLKLANKNE
LEFRVKGSEEYAELPNLFLAILPAKDEKILEKLQETIRIKIKDELAELLKKAVKDLIEGPAVITDLEEGL
KQKEEALKKELEKYADKRLSAPSLLEKEEVYKDVKNGNVGTGLNNVSKYLSFEESVLKLSEKFLRKELIR
IYPKLRESLDAIGLTKRFSERCEKCLELPGIKCLLCGENLAIAGVKRKLLELKDLKALLQEEERLCPLCL
IKRQLPFIERISPGYSKDLLFPSISEVAESEKEVLLLVDGELDVDKEYLESLRKKERKNPRPYYAILKAD
GDRMGKLLRGEIRPEEKERIHPKKVKNLTTPAAHVAFSRALAEFSLKAVKIVVNEHYGELVYAGGDDVLA
LLPVDTALDVAKELRKEFRESLEKSLGGERGPTMSAGLLIVHHKEPLYDALELARRLLKRAKE
>gnl|CDD|274209 TIGR02578, CRISPR-associated_protein_Cas10/Csm1, CRISPR-associated protein Cas10/Csm1, subtype III-A/MTUBE. The family is designated Csm2, for CRISPR/Cas Subtype Mtube Protein 2. A typical example is TM1811 from Thermotoga maritima. CRISPR are Clustered Regularly Interspaced Short Palindromic Repeats. This protein family belongs to a conserved gene cluster regularly found near CRISPR repeats
LAVAALLHDIGKVIRRAGDCYNEDLKHDKTGYEFIHEFFKNALLEVLDKKADDLLKNLVKSHHEEDYLDD
LIARAERLASGLEIIDRLEAGDDREEEELGNEEEPLVSPFPKIPLGNSLRNAGGFKPKYPLKSLNRAVPP
ENDNKASQENYKRLMEKFLGDLEKLKPSYPDKIELLLTLFEKLWSFVPAATNGGSKPDVSLYDHLKLTAA
IASALYRYLKENNTKDDALAKLDSAIDEDWNGEKFLLVSGDLSGIQDFIFRITSKGALKSLRGRSFYIEL
LQEYIALYILEELNLTRTNILFDGGGHFYLLLPNTEEARLEKLRERIEEELLKEFRGEMLTLGIASDAFS
ENDLRNFATKRKKLHEKLERAKKRRFSELLSTAGNPKSGFYSFGNNTCDICGRAASAREIEDLALCDLCA
EEYNLGEALRADRSFVILDEAGIPKLDFEKYIVLFAREADDAKKLEQLSQEGYLIYEYSRDHINAYRGIA
YGLQITDKPIPDDESAFKPVSEKGLGEEGHKKLGVLKMDVDNLGEIFASGLKRPTRISRLATLSRQLELF
FKLYLLHLAEDKRNKRNLYVVYSGGDDLFLIGPWNAVLELASDIREYFEKFTCRDKITISAGVVVVSPKY
PVYRAARIAEELLEAAKE
>gnl|CDD|131628 TIGR02579, Uncharacterized_protein_AF_1864, CRISPR-associated protein, Csx3 family. Members of this family are found encoded in CRISPR-associated (cas) gene clusters, near CRISPR repeats, in the genomes of several different thermophiles: Archaeoglobus fulgidus (archaeal), Aquifex aeolicus (Aquificae), Dictyoglomus thermophilum (Dictyoglomi), and a thermophilic Synechococcus (Cyanobacteria). It is not yet assigned to a specific CRISPR/cas subtype (hence the x designation csx3)
FTLIEFELERPLVPEDLKQLQPPAGVNTRKGVVLSGRGPIWLYGFLVHFYHPTPFVAVYDPRLGAVVVSS
HSPEVRVGDVIDW
>gnl|CDD|274210 TIGR02580, putative_CRISPR-associated_protein, CRISPR type III-B/RAMP module RAMP protein Cmr4. This model represents a CRISPR-associated protein from the family that includes TM1792 of Thermotoga maritima. This family is part of the broad RAMP superfamily (pfam03787) collection of CRISPR-associated proteins. It is the fourth of a recurring set of six proteins, four of are in the RAMP superfamily, that we designate the CRISPR RAMP module
YLVLLYALTPIHVGAGQSGIGVVDLPIQRERHTGYPIIYGSSLKGALRSYFIRQISRDKDESKVECVFGN
PKEEAEESAGKVVFSDARLLAYPVRSFDGVFAYVTSPYLLERFERDLEAAGVLIGSLELEENEKALLFSG
IKEGKVLLEEIKLEAILNEAPGVRELWLAIKTFKELVPLLENRLVVVSDNLFRDLVNSALERVPRIRLNQ
ETKTVEEGGLWYEEYIPAGTIFYGLINVDDELNKKESNKEEIFKEFSKIINNGKVIQIGGKETVGKGLVR
>gnl|CDD|274211 TIGR02581, putative_CRISPR-associated_protein, CRISPR-associated RAMP protein, SSO1426 family. Members of this CRISPR-associated (cas) gene family are found in the RAMP-2 subtype of CRISPR/cas locus and designated TM1809 family
KSQTKISGILENQTPLRIGYGKSQEPTGPDDPVIKDANGRPIIPGSSFKGALRSLAERYLKRRNLITCSW
NDPDYWVCDPDDNKCTSCNGKENYIEDALETFWNKTCLPCILFGSPWLASRVYILDAVAEEPSDQQRTMV
AIDRDFGTALPGHLYDFEYVEPGSVFNFSIFLENLNEEWEIGALLTVLKTLITGGIFIGGKKSRGFGLVK
LTSGEIE
>gnl|CDD|274212 TIGR02582, CRISPR_type_III-associated_RAMP_protein_Csm3, CRISPR type III-A/MTUBE-associated RAMP protein Csm3. Members of this CRISPR-associated (cas) gene family are found in the mtube subtype of CRISPR/cas locus and designated Csm3, for CRISPR/cas Subtype Mtube, protein 3
KGKIIITGTIEVLTGLHIGGSKEELKIGGTDSPVIRDPLTDLPYIPGSSLKGKIRSLLERSLGAVSNKGK
YRYHNCDPGECEVCRLFGSAPENDEESIKGPTRLIVRDAFLTEDTKEELARNDTDLPYTEIKFENAIDRI
TSKANPRQIERVPAGAKFKFEIIYSVYEGDEEEEDFKNILEGLKLLEDDYLGGSGSRGYGKVKF
>gnl|CDD|274213 TIGR02583, putative_CRISPR-associated_regulatory_protein_Csa2, CRISPR-associated protein Cas7/Csa2, subtype I-A/APERN. CRISPR is a term for Clustered Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR associated) proteins. This model represents one such family, typified by MJ0381 of Methanococcus jannaschii. This archaeal clade is a member of the DevR family (TIGR01875) which includes the DevR protein of Myxococcus xanthus, a protein whose expression appears to regulated through a number of means, including both location and autorepression; DevR mutants are incapable of fruiting body development. This subfamily is found in a CRISPR/Cas locus we designate APERN, so the family is designated Csa2, for CRISPR/Cas Subtype Protein 2
YVSVSGRVLVNVEALNGVESAGNYTKHRRAPVVVKTDNGYTVYYVPAISGESLAHWYQVYLVEIAKKLGL
PVNELCKRGIFLKFGNGDTLKKKGSGEPKDPNDAEVEVIKKDVVEDVGGFLYAEKAPVKRTSLIKFSYMI
PVLRGDEEVAQAEAQFHVRHNRVDPSEKGASKEGTGQMIFNVEYSSALYGFSFELDLDLIGVPQFLPEKE
GGEEEDERERKRRIEAALKALLPLLSGNFGAKRARFLPVMKVEELVVAVSEKPFPVPPIHGGYIDYTEKR
LSKAK
>gnl|CDD|274214 TIGR02584, hypothetical_protein_NE0113, CRISPR-associated protein, NE0113 family. Members of this minor CRISPR-associated (Cas) protein family are found in cas gene clusters in Vibrio vulnificus YJ016, Nitrosomonas europaea ATCC 19718, Mannheimia succiniciproducens MBEL55E, and Verrucomicrobium spinosum
ILLCVIGMSPQIITETIYALAQESPPVVPEEIHVITTSDGKRDIQQQLLTPDEAWQGVLAKLRHDYFQGP
RPPFDELRIYLIPTGQRKPLADIRTPADNEAAANFIVQTVAPLCAAQDHQLHASIAGGRKTMGFYLGYAL
SLFGREQDRLSHVLVSEPFENIRGFYYPPRKGPILEIRTRDGPPAPADTSEAVVELAELPFVRLRHKLP
>gnl|CDD|274215 TIGR02585, conserved_protein, CRISPR-associated protein Cas7/Cst2/DevR, subtype I-B/TNEAP. CRISPR is a term for Clustered Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR associated) proteins. This clade is a member of the DevR family (TIGR01875) and includes the DevR protein of Myxococcus xanthus, a protein whose expression appears to be regulated through a number of means, including both location and autorepression; DevR mutants are incapable of fruiting body development
LTLVFVNMLNNYDEGIGNIVTLKKLLRNDGEVYPYVSRQAIRYALRDTLKEGGWELSETPVKGDGTEKQF
NTEGNPIKYIDDDLFGYMRTKKKATNKRTSPVRITPAISLEPFQGDVDFGANSPLANRARQEAKPNPFET
EIHSTLYKYSFLVDLDRVGKFEVDELLCLKIENVGGIDEKELPNEERKKRAKALLEAIGNLHGGAKQARR
LEDLSPKFVVLGVLNIKIPVFLNVLKVEEEYLEGEVIIDVELIVTALEDFSEKVEDEVHIGLLKGFFEEN
EEEAIELKPDGGVESIIVIFDKVKKAVEKI
>gnl|CDD|131635 TIGR02586, CRISPR-associated_protein_Cas5, CRISPR-associated protein Cas5/DevS, subtype MYXAN. This model represents DevS of Myxococcus xanthus and related proteins of Leptospira interrogans and Gemmata obscuriglobus. This protein is encoded in a cluster of CRISPR-associated (cas) genes, and in the special case of Myxococcus xanthus has taken on a role in the control of fruiting body development. CRISPRs are clustered, regularly interspaced short palidromic repeats. This protein family is related to models TIGR01868, TIGR01895, and TIGR01876
IALELEIPIACFRKGQARELQDSEPLPPPATCIGALLSLCGEQDDERKFFRGCEMCAAVADANPISARLR
TFRRMKNLGDAGGDDENAAPDQQELVIDARGIVACDGLEAPDSGEELADPMKRALREPEKIIRAGGLSLG
ESSFLIDDARLFEEGDPPAGCRAFLIADMGASLDLPVWIDHIGPRGTR
>gnl|CDD|131636 TIGR02587, TIGR02587, putative integral membrane protein TIGR02587. Members of this family are found in Nostoc sp. PCC 7120, Agrobacterium tumefaciens, Sinorhizobium meliloti, and Gloeobacter violaceus in a conserved two-gene neighborhood. This family, as defined, includes some members of COG4711 but is narrower and strictly bacterial. Members appear to span the membrane seven times [Cell envelope, Other]
RRFINGLVRGTAGALLFAIPLLMTMEVWWLGSLAKPRRLVLLIALMFPVLFLLNYTEGFRKRKRVREAVI
DTVEAMAIGFVCSAAMLWLFGIITPETSLKEIVGKVAFQGVPFSLGAALARQQLGDTNQNNSLSEGKQNS
EYGYLAELFAMLVGALFLSFNIAPTEEVPLIAYKISPPHIFALILASLVIMHAFVYQLGFRGQHKRRQGK
GIFQRFLRETTIGYLVSLLASAYMLWTFQRVDFADWSMWLEATVVLGLPATIGAAAARLIL
>gnl|CDD|131637 TIGR02588, TIGR02588, TIGR02588 family protein. The function of this protein is unknown. It is always found as part of a two-gene operon with TIGR02587, a protein that appears to span the membrane seven times. It is found in Nostoc sp. PCC 7120, Agrobacterium tumefaciens, Sinorhizobium meliloti, and Gloeobacter violaceus, so far, all of which are bacterial [Hypothetical proteins, Conserved]
SLAEWVTFGISTLILAAMFGLVAYDWLRYSNKAAVLEVAPAEVERMQTGQYYVPFAIHNLGGTTAAAVNI
RGELRQAGAVVENAEVTIDYLASGSKENGTLIFRSDPRNGQLRLRVAGYKEP
>gnl|CDD|274216 TIGR02589, conserved_hypothetical_protein, CRISPR-associated protein Cas7/Csd2, subtype I-C/DVULG. This model represents one of two closely related CRISPR-associated proteins that belong to the larger family of TIGR01595. Members are the Csd2 protein of the Dvulg subtype of CRISPR/cas system. CRISPR stands for Clustered Regularly Interspaced Short Palindromic Repeats. The related model is TIGR02590, the Csh2 protein of the Hmari CRISPR subtype
RIDFVVLFDVKNGNPNGDPDAGNMPRIDAETGHGLVTDVSLKRKIRNRVLLMGGQDIFVQEKARLNDTIK
SLYKRLDIKLETAKKRNKKGRGKEVEEFRKWMCANWFDVRAFGAVMATKGNAGQVRGPVQITFARSIDPV
VIQEHSITRMAVTTEEEAEKQKGDSRTMGRKHTVDYGLYVAHGFISAQLAEKTGFSDEDLELIKQALVNM
FENDRSAARGSMSVRKVYWFKHSSKLGNAPAAKLFDLLSVSRKDDSDSPARYFIDYNVEVDAAYLPKGLE
VEEL
>gnl|CDD|274217 TIGR02590, hypothetical_protein_MM_0563, CRISPR-associated protein Cas7/Csh2, subtype I-B/HMARI. This model represents one of two closely related CRISPR-associated proteins that belong to the larger family of TIGR01595. Members are the Csh2 protein of the Hmari subtype of CRISPR/cas system. CRISPR stands for Clustered Regularly Interspaced Short Palindromic Repeats. The related model is TIGR02589, the Csd3 protein of the Dvulg CRISPR subtype
RSEILFLYDAVDANPNGDPLSANRPRIDEQTQQLIVTDVRLKRYVRDQLDDDGHGVLIRTVQEEEDRLKS
VDYDSYDVDDDEEVKEFREDVFGEYLRKSIDVRLFGAVISVDKDDVLPDHITGPVQFSPGKSMHAVNENE
EQGTSAIATQEGKEQGGFDDDHRIPYALIRFYGVVNENGAKDTGLTEEDVERLDTLCWRGIKNTISRSKV
GQEPRLLCRVEYKEESFHLGELDYDVRVDEEAEDEELRDISDLALDIDDLVDRLDGAKAQIERIRVVASD
VLKFTH
>gnl|CDD|188234 TIGR02591, cas_Csh1, CRISPR-associated protein Cas8b/Csh1, subtype I-B/HMARI. This domain is found in the C-terminal 2/3 of a family of CRISPR associated proteins of the Hmari subtype. Except for the two sequences from halophilic archaea this domain contains a pair of CXXC motifs
VGTTSDPYKFYTTDKPGYSPGLEKKNAWKNYPICEDCYKDVLIGRKFIEECLDRRFGGNTYKLPIIPGTI
FPKVAQDLYKEEIKKIYEFRKNDFLQEKFYTEEAGYEIELDEDLEENKIGYYLRYDFLFYSKEKQAEKIT
LYIKDVEPSRVEKILELEKKVLNVSKEDFGELKENWFFGQVYAFLLDNDFFEDDEFLNLLDAIFRGGPLD
KDTLFTEFLKKIKDEFFGGDSINNLIVASQNMRLLLLAREALLLLLSLDKYLELLTSEAEVEGEVKDTKL
EDIFEYVKESFLDPQKRALFLLGVLVGELISLQKSKRNKSKPLVNKLKGLKITKKTIENLLNEVREKLTQ
YGRQSEGGSKRYTSTSELLDRLIESWKLSEDENVFYFVSGMAY
>gnl|CDD|131641 TIGR02592, hypothetical_protein_CTC_01466, CRISPR-associated protein Cas5, subtype I-B/HMARI. This is a CRISPR-associated protein unique to the hmari subtype of cas genes and CRISPR repeat, which is the only subtype present in Haloarcula marismortui ATCC 43049. The hmari type, though uncommon, is also found in the Aquificae, Thermotogae, Firmicutes, and Dictyoglomi
DCLVFSVSGPYAFFRKPYTTTSYFTYGNVHRTALLGLIGAVLGYGKEEIYDEFYEKLKKIAIQVVPPLRK
LYIDKKIVSTKADVGYASKELGGRLIVNEQWLENPAYRIFVSWDDEVPKELKDRLENFKFIYTPYLGVSE
HIANITYVGYLEAEEKLDDTNSVDSIVPNDVYEIQLESKNFNDIKEIIKKSSSKIREFKYEEMLPYAFEE
DTNPYKVETFIYTNSADTKVYKVGEKNIFFF
>gnl|CDD|274218 TIGR02593, CRISPR-associated_protein_Cas5, CRISPR-associated protein Cas5, N-terminal domain. This model represents a shared N-terminal domain, about 43 amino acids in length, common to a number of related protein families each of which is associated with a distinct subtype of CRISPR/cas system, where CRISPR is an acronym for Clustered Regularly Interspaced Short Palindromic Repeat and Cas is an abbreviation for CRISPR-associated. Members of this family are widely distributed enough that we designated the family Cas5. Homology appears remote, or absent, between the more C-terminal regions different subfamilies of these proteins, which typically are 210 to 265 amino acids in total length. Cas5 proteins of six different CRISPR/cas subtypes so far defined are described by respective full-length models TIGR01868, TIGR01876, TIGR01895, TIGR01874, TIGR02586, and TIGR02592. The best characterized protein in this family is DevS or Myxococcus xanthus, a Cas protein that appears to participate in a species-specific developmental pathway
LLLRLRGPLASFRKPETFGERPTYPVPPPSALLGLLGAALGK
>gnl|CDD|131643 TIGR02594, hypothetical_protein, TIGR02594 family protein. Members of this protein family known so far are restricted to the bacteria, and for the most to the proteobacteria. The function is unknown
GWVKEARKYIGVKEIKGGKNNPRIVEYNKVRTDDETPWCGSFVNMCLEKTGRKGTGNSAMARSWARYGTK
LSKPAYGCIAVKRRGGGGHVGFVVGKDKQTGTIIVLGGNQGDRVREALYSRSRIVAYRW
>gnl|CDD|131644 TIGR02595, conserved_hypothetical_protein, PEP-CTERM protein-sorting domain. This model describes a 25-residue domain that includes a near-invariant Pro-Glu-Pro (PEP) motif, a thirteen residue strongly hydrophobic sequence likely to span the membrane, and a five-residue strongly basic motif that often contains four Arg residues. In nearly every case, this motif is found within nine residues, and usually within five residues, of the extreme C-terminus of the protein. Proteins with this motif typically have signal sequences at the N-terminus. This region appears many times per genome or not at all, and co-occurs in genomes with a proposed protein-sorting integral membrane protein we designate exosortase (see TIGR02602). PEP-CTERM proteins frequently are poorly conserved, Ser/Thr-rich proteins and may become extensively modified proteinaceous constituents of extracellular material in bacterial biofilms [Cell envelope, Surface structures]
VPEPSTLLLLLLGLGFLLLRRRRK
>gnl|CDD|274219 TIGR02596, TIGR02596, Verru_Chthon cassette protein D. This model describes a nearly twenty member protein family in Verrucomicrobium spinosum and a somewhat smaller paralogous family in Chthoniobacter flavus. All members share a type IV pilin-like N-terminal leader sequence (TIGR02532). These proteins occur in the four-gene Verru_Chthon cassette, in which two other genes likewise encode a cleavage/methylation domain. Most of these cassettes occur next to an unusually large PEP-CTERM protein with an autotransporter domain [Cell envelope, Surface structures]
FTLVELLVVIAIAALLMALSTPVVNQVLAAQQLGSSATRLANELAAAAQLAVRENRPVEVRFLRRADDAG
PGALGYRGWQLMVPEPTTIGKWRPIGEVQLLEASVIMLEDPTYSTLLSRDSPVDLKLADAVPDSATTPPT
FAFKPDGGTNLPRGDTDGKWCLTLALEKDVADPTALPPNYRTLVVDPVTGAVVLY
>gnl|CDD|274220 TIGR02597, TIGR02597, TIGR02597 family protein. This model describes a paralogous family with at least ten members in Verrucomicrobium spinosum. Two additional predicted proteins match more weakly and score between the trusted and noise cutoffs, while a third contains a point mutation. Eleven of the thirteen genes are found in a single tandem array
ATWVEGISLFAQVFSDPVGFNKFEAPGNSDTRVSAPFHRPPEFRGTVTSVSGNGVVTVLGTPNWASNQFV
YAAGTQPNHFYVRVTSGSRAGMYYTITANTTATLTIDLSGDNIDGGVQPGDTFKIIPYWTLSTIFPGQQG
IHTSTSHSIPGRTTEVLIPDTGSPGIDLAPVDSYYYYDGSSGAGPGWRKSGDAAAITFNDTVLLPDSHLI
IRHNSASPTTTVVTSGTVPLTKLATPLLTLAATTDQDNAVALPFPIPLTLAQLSLVESGAFKPSPTHSIT
TGDLLLVYDNTVAGINKAASASYYYYTGSMGGGPGWRDSGGGATTIANSDVVLSPSSGFVIRKKAGNVPQ
TKLWTVRPPYP
>gnl|CDD|131647 TIGR02598, TIGR02598, Verru_Chthon cassette protein B. This family consists sets of paralogous family of proteins in the Verrucomicrobium spinosum and Chthoniobacter flavus. All members contain the prepilin-type N-terminal cleavage/methylation domain (TIGR02532) at the N-terminus. The mature protein would be about 150 amino acids long. These proteins occur in the four-gene Verru_Chthon cassette, in which two other genes likewise encode a cleavage/methylation domain. Most of these cassettes occur next to an unusually large PEP-CTERM protein with an autotransporter domain [Cell envelope, Surface structures]
GFSLVEVVLAVGIAATVLLTLIGLLPTGLDTLRQSSNKQAEARILQSISGDYQMRDWGEWTSSQNLADKT
YYFDQQGTEVKSVDDVDRIYTARAKVDNTPPLLGGDDSATNPYLRQLMIKVTDSSNRTAAFSDPGRYRER
ATTVAQMEQTP
>gnl|CDD|274221 TIGR02599, TIGR02599, Verru_Chthon cassette protein C. This family consists sets of paralogous family of proteins in the Verrucomicrobium spinosum and Chthoniobacter flavus. All members contain the prepilin-type N-terminal cleavage/methylation domain (TIGR02532) at the N-terminus. The mature protein would be about 350 amino acids long. These proteins occur in the four-gene Verru_Chthon cassette, in which two other genes likewise encode a cleavage/methylation domain. Most of these cassettes occur next to an unusually large PEP-CTERM protein with an autotransporter domain [Cell envelope, Surface structures]
MTVLAILMLVLAQVLSQTQNTWRRATARVEQFREARAAFEAISRNLSQATLNAYWDYKYNAGDTPTVPAT
GYERQSELHFVSGPASTLLGTGAGAEPGHAVFFQAPLGFTEQAGTEGLDNLLNAWGYYVEYGTDLPRRPA
FLAGSSPPVPERYRFRLMEYRQPAERLRLYDLTAFGLNTQTSRAQALQWFQTALAANSRPHPVAENIIAL
VISPKVPGTGPTSSPGVTPTGVWLAPAYAYDSRDVQWNGANGLAESSRHQLPPVVRLTLVAIDESSAARL
ADTAGGAAAPELGLVTAGKFTDASKYEADLEALETTLVALKLNFRVFSTTVSLRGAKWS
>gnl|CDD|274222 TIGR02600, Verru_Chthon_A, Verru_Chthon cassette protein A. In Verrucomicrobium spinosum and Chthoniobacter flavus, a four-gene operon that includes proteins with an N-terminal signal sequence for cleavage and methylation recurs many times. Each operon is likely to encode a membrane complex, the function of which is unknown. This model represents a long protein from this putative membrame complex, with members averaging about 1300 amino acids. The N-terminal region includes an apparent signal sequence. The function is unknown. Most cassettes are adjacent to an unusually large protein with both an outer membrane autotransporter region and PEP-CTERM putative protein-sorting motif [Cell envelope, Surface structures]
MALIMVLIILALITILVLGFLSMVRTETRSSSSHASRSDARTLSDMAVNIVIGQIRQATTDLGKTWASQP
GAIRVYGTTGGTSNRAYKLYSSDQMVVGAAFATALALESDVPATWDAPKALYTDLNEPVATLADNGTRGH
VPTDEPGMDTPAYPASTGGYPVKGAVKGTSGTVAPPGTDATSPRLPMPVRWLYVLQDGTLDVPDGPAGGV
AFFGALANTANNPIVGRIAFWTDDESSKVNINTASEGTFWDVPRAVTVRERNFANYEPAQNEFQRFPGHP
ATTCLSAVFTPFDPLLPPSTASAATLQNIYDLAPRVNAGGSRDGTDTVTGSIGPPDKDADRLYASVDEFF
FDTSEDRTRRRDSSAGSPPGDAEVLEKARFFLTAYSRAPETTLFNEPRISLWPIQAEKAARNAKDKLIAF
CATLGNKPYYFQRAKKFKNSDTSPGQSQSPNLDLAKALARNQELLNSYLQRLTAWPIPGFGTGSFQAKYG
VGNRNQILTEMFDLTRWSVNSASTYGTPTYTYVPPRASSGSSAELIGESSALPVVPGGDTKGFGRFFTVS
EAGLVFMPTEVNPNPDTSLAVGTKRMRAYLILEPFCPITGMPAWSPNFRYRITGLNTWQINTTGMGFPAA
GGNNSLPPLGVSTGGEIHLTALTGLDAIDLAKSAGGMVAVPLAGGSGDELNNYPFVSAFITVGSTATTFT
FDGGNITIEILAGEYAAAYPKALTLMQNARPTTPVPTEAWVPTVNLRLPRALNAEYANTQVATQLQARPE
SVANNPRRELIAPGDTVRSVTVDPAGPAKGDLRSIAVLRDVPADYYVPHPERDPGAIEEAHSLRPGTKTA
TGQFGRINGPYVGYSLSGADGGTLAWNTAGADYNTLLRPVFYRRTCSPAGPAGLNGAYNSTGRPEGDWDN
GIGRTEDGPYINKPDEGNTVYGGFNRSYGLGYFSRGGFGSEPAGITYSPNRQISSAVAFGSLPTGIEPGR
AGPGGVPWQTLLFCPNPHSGTTLAGLEPGFTVPPDHALLDLFWMPVVEPYAISEPFSTAGKINMNYQILP
FTHIKRATGLHAVLKSVLPTAIPLSGVGNYNFTTETGYKYTANSYRAEWTADNIYNRTLAGFEKRFDQGD
IFRSASEICEIFLVPKTNVDADGLPTGSPTYETMESWWNSHELTGDNVRESPYNQIYPRLTTRSNVFTVH
FRVQSLKKARSTDADEWDEDRDLVTSEYRGSTLLERYIDPNDPELPNLEYGTLDPAASLDTYYRFRIIER
KRFAP
>gnl|CDD|274223 TIGR02601, outer_membrane_autotransporter, autotransporter-associated beta strand repeat. This model represent a core 32-residue region of a class of bacterial protein repeat found in one to 30 copies per protein. Most proteins with a copy of this repeat have domains associated with membrane autotransporters (pfam03797, TIGR01414). The repeats occur with a periodicity of 60 to 100 residues. A pattern of sequence conservation is that every second residue is well-conserved across most of the domain. pfam05594 is based on a longer, much more poorly conserved multiple sequence alignment and hits some of the same proteins as this model with some overlap between the hit regions of the two models. It describes these repeats as likely to have a beta-helical structure [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
GLTKTGAGTLTLSGANTYTGGTTVNAGTLQVG
>gnl|CDD|131651 TIGR02602, conserved_hypothetical_protein, exosortase. This family is designated exosortase, and it is the predicted protein-sorting transpeptidase for the PEP-CTERM protein-sorting signal of many biofilm-producing Gram-negative bacteria. This system is analogous to the sortase/LPXTG system found mostly in Gram-positive bacteria. Members of this family are integral membrane proteins with eight predicted transmembrane helices in common, and with a triad of invariant residues that matches the catalytic triad of sortases. Some members of this family have long trailing sequences past the region described by this model, which in other species is a separate protein EpsI. This model does not include the region of the first predicted transmembrane region. The only partially characterized member is EpsH of Methylobacillus sp. 12S, part of a locus associated with biosynthesis of the exopolysaccharide methanolan but itself not involved in polysaccharide biosynthesis [Protein fate, Protein and peptide secretion and trafficking]
VSIWWRSDTYSHGYLIIPFVAYLAWSKRERLSELPSRPSSLGLALLVLGLAAYLLASVLSVTWMASLSLV
ALLAGSVLALFGFRAFRLLLFPLLLLLFAIPPPGYYAILTIPLQHLTAFAAVGLLDATGIPVYVEGNVIH
LPSGTLEVVEACSGLRSLFTSLALGTLFAYLNLRSLWRRAIFLSVAILIAVAANILRVSILIVAGHQTGM
DLASGWAHDVLGWVLFAVSMFLLFSIGGMLM
>gnl|CDD|274224 TIGR02603, CxxCH_TIGR02603, putative heme-binding domain, Pirellula/Verrucomicrobium type. This model represents a domain limited to very few species but expanded into large paralogous families in some species that conain it. We find it in over 20 copies each in Pirellula sp. strain 1 (phylum Planctomycetes) and Verrucomicrobium spinosum DSM 4136 (phylum Verrucomicrobia), and no matches above trusted cutoff an any other species so far. This domain, about 140 amino acids long, contains an absolutely conserved motif CxxCH, the cytochrome c family heme-binding site signature (PS00190)
GDAARGKAVFAKVCYLCHRIGGQGVDFGPNLTTVGTKGKEYLLEAILDPSRTVAPGFETYRVTTKDGRIL
AGLVASETADPLTIKMPGGVEQVVPREEIKKRKHLPVSLMPEGLEMGLSDQDLADLVAYLKSL
>gnl|CDD|274225 TIGR02604, Piru_Ver_Nterm, putative membrane-bound dehydrogenase domain. All proteins that score above the trusted cutoff score of 45 to this model are large proteins of either Pirellula sp. 1 or Verrucomicrobium spinosum. These proteins all contain, in addition to this domain, several hundred residues of highly variable sequence, and then a well-conserved C-terminal domain (TIGR02603) that features a putative cytochrome c-type heme binding motif CXXCH. The membrane-bound L-sorbosone dehydrogenase from Acetobacter liquefaciens (Gluconacetobacter liquefaciens) (SP|Q44091) is homologous to this domain but lacks additional sequence regions shared by members of this family and belongs to a different clade of the larger family of homologs. It and its closely related homologs are excluded from the this model by scoring between the trusted (45) and noise (18) cutoffs
GLKVTLFAAEPLVRNPIAVCFDEDGRLWVAEMITYSRTRGRDMPLGDRILVLEDTDGDGKYDKSTVFAEE
VQMLTGLAVAVGGVYVATPPHILRLRDKDGDGKAEDKREVLLSGFNGQAASHHHSLNGLKWGPDGRLYFN
CGNTLASKVTTPGRSDESRQGIGGFLFRMNPDGGRLRIVAGGFQNPYGHSVDSWGDVFFCDNDDPPACRV
TDVAEGGRNGYQSRSGRRYWLADRGADQEVPTAKWRQDDRGTVGVGDVAGTGTAPTGITFYRGGALPKEY
RGLLLTADAGGQLINRYRLEPKGASFKGERPEFLKSDDTWFRPVNVTTGPDGAIYVADWYDRGIEHHNDD
LNDGSNSGRIYRITPKG
>gnl|CDD|274226 TIGR02605, CxxC_CxxC_SSSS, putative regulatory protein, FmdB family. This model represents a region of about 50 amino acids found in a number of small proteins in a wide range of bacteria. The region begins usually with the initiator Met and contains two CxxC motifs separated by 17 amino acids. One member of this family is has been noted as a putative regulatory protein, designated FmdB (SP:Q50229, ). Most members of this family have a C-terminal region containing highly degenerate sequence, such as SSTSESTKSSGSSGSSGSSESKASGSTEKSTSSTTAAAAV in Mycobacterium tuberculosis and VAVGGSAPAPSPAPRAGGGGGGCCGGGCCG in Streptomyces avermitilis. These low complexity regions, which are not included in the model, resemble low-complexity C-terminal regions of some heterocycle-containing bacteriocin precursors [Regulatory functions, DNA interactions]
MPIYEYRCTACGHRFEVLQKMSDDPLATCPACGGTKLRRLLSAAGFALKGSG
>gnl|CDD|274227 TIGR02606, Antitoxin_ParD, putative addiction module antidote protein, CC2985 family. This bacterial protein family has a very similar seed alignment to that of pfam03693 but is a more stringent model with higher cutoff scores. Proteins that score above the trusted cutoff to this model almost invariably are found adjacent to a ParE family protein (pfam05016), where ParE is the killing partner of an addiction module for plasmid stabilization. Members of this family, therefore, are putative addiction module antidote proteins. Some are encoded on plasmids or in prophage regions, but others appear chromosomal. A genome may contain several identical copies, such as the four in Magnetococcus sp. MC-1. This family is named for one member, CC2985 of Caulobacter crescentus CB15 [Cellular processes, Other, Mobile and extrachromosomal element functions, Plasmid functions]
MTSVSLGEHLESFIRSQVQSGRYGSASEVIRAALRLLEERETKLQALRDAIEEGEQSGEAGRSLDDVLS
>gnl|CDD|274228 TIGR02607, Virulence-associated_protein_I, addiction module antidote protein, HigA family. Members of this family form a distinct clade within the larger family HTH_3 of helix-turn-helix proteins, described by pfam01381. Members of this clade are strictly bacterial and nearly always shorter than 110 amino acids. This family includes the characterized member HigA, without which the killer protein HigB cannot be cloned. The hig (host inhibition of growth) system is noted to be unusual in that killer protein is uncoded by the upstream member of the gene pair [Regulatory functions, DNA interactions, Regulatory functions, Protein interactions, Mobile and extrachromosomal element functions, Other]
NPAHPGEILLEEFLEPLGLSVRALAKALGVSRSTLSRIVNGRAAITADMALRLAKALGTSPEFWLNLQNA
YDLWIAEQ
>gnl|CDD|274229 TIGR02608, hypothetical_protein, delta-60 repeat domain. This domain occurs in tandem repeats, as many as 13, in proteins from Bdellovibrio bacteriovorus, Azotobacter vinelandii, Geobacter sulfurreducens, Pirellula sp. 1, Myxococcus xanthus, and others, many of which are Deltaproteobacteria. The periodicity of the repeat ranges from about 57 to 61 amino acids, and a core region of about 54 is represented by this model and seed alignment
DRAYAVAVQSDGKILVAGYVDNSGNNDFVLARLNADGSLDTTFGTGGKVTFDLG
>gnl|CDD|274230 TIGR02609, hypothetical_protein_XAC1195, putative addiction module antidote. Members of this protein family are putative addiction module antidote proteins that appear recurringly in two-gene operons with members of the Doc (death-on-curing) family TIGR01550. Members of this family contain a SpoVT/AbrB-like domain (pfam04014). Note that the gene pairs with a member of this family tend to be found on bacterial chromosomes, not on plasmids [Mobile and extrachromosomal element functions, Other]
RKIRKVGNSLVVTLPKEVLESLGLKEGDTLYVDEEEGGLKLKRFDEGKELEKKMQMAVERAMSKYDEALK
ELAD
>gnl|CDD|131659 TIGR02610, conserved_hypothetical_protein, putative polyhydroxyalkanoic acid system protein. All members of this family are encoded by genes polyhydroxyalkanoic acid (PHA) biosynthesis and utilization genes, including proteins at found at the surface of PHA granules. Examples so far are found in the Pseudomonales, Xanthomonadales, and Vibrionales, all of which belong to the Gammaproteobacteria
MSSISVERDHSLGPAAARAKAEDLARKLTDRYGLASHWEGDTLRIARSGVDGAVHLGPQSIRVTAELGML
LSAMSGTIKSEIERALDKALA
>gnl|CDD|131660 TIGR02611, Putative_membrane_protein, TIGR02611 family protein. Members of this family are Actinobacterial putative proteins of about 150 amino acids in length with three apparent transmembrane helix and an unusual motif with consensus sequence PGPGW [Hypothetical proteins, Conserved]
VEDALERLQDEHVHAKRRAYGFVVRPLVLVVGWVVLIVGIITIPLPGPGWLTIFIGLAILSLEFVWAQRL
LRWGVRKYDEFFAWYADQHVRVRNLLLGSLIVVIWAVLAGTYLWMWGLGMP
>gnl|CDD|274231 TIGR02612, transcriptional_regulator, mobile mystery protein A. Members of this protein family are found in mobization-related contexts more often than not, including within a CRISPR-associated gene region in Geobacter sulfurreducens PCA, and on plasmids in Agrobacterium tumefaciens and Coxiella burnetii, always together with mobile mystery protein B, a member of the Fic protein family (pfam02661). This protein is encoded by the upstream member of the gene pair and belongs to a family of helix-turn-helix DNA binding proteins (pfam01381) [Unknown function, General]
SLKLARKQLDQRLVALAGAGAIQTPKEGWVRAIRKALGMSGAQLAGRLGVTPQRVEALEKSELSGTVTLK
TLRAAAEALDCTFVYAFVPKTSLEATIRAQARKVAKEIVARVAHTMALEDQATSKNRTEAEVERLTSELL
REMPRDLWSE
>gnl|CDD|131662 TIGR02613, cell_filamentation_protein, mobile mystery protein B. Members of this protein family, which we designate mobile mystery protein B, are found in mobization-related contexts more often than not, including within a CRISPR-associated gene region in Geobacter sulfurreducens PCA, and on plasmids in Agrobacterium tumefaciens and Coxiella burnetii, always together with mobile mystery protein A (TIGR02612), a member of the family of helix-turn-helix DNA binding proteins (pfam01381). This protein is encoded by the downstream member of the gene pair and belongs to the Fic protein family (pfam02661), where Fic (filamentation induced by cAMP) is a regulator of cell division. The characteristics of having a two-gene operon in a varied context and often on plasmids, with one member affecting cell division and the other able to bind DNA, suggests similarity to addiction modules
ATPLDPEELEGLLPGHITTRGELDEFEQANIAEGILWAEGRRRKKKDILSETFLRRLHRRMFGDVWRWAG
DFRTTQKNIGVSPLQIPSELAILLDDVRYWLQNGTFSPDEIAIRFHHRLVAIHPFPNGNGRHARLATDLL
LEQQGYSPFTWGSGSLALVGDLRKEYIAALKAADRHDYGPLLEFAR
>gnl|CDD|274232 TIGR02614, Putative_lipid_II_flippase_FtsW, cell division protein FtsW. This family consists of FtsW, an integral membrane protein with ten transmembrane segments. In general, it is one of two paralogs involved in peptidoglycan biosynthesis, the other being RodA, and is essential for cell division. All members of the seed alignment for this model are encoded in operons for the biosynthesis of UDP-N-acetylmuramoyl-pentapeptide, a precursor of murein (peptidoglycan). The FtsW designation is not used in endospore-forming bacterial (e.g. Bacillus subtilis), where the member of this family is designated SpoVE and three or more RodA/FtsW/SpoVE family paralogs are present. SpoVE acts in spore cortex formation and is dispensible for growth. Biological rolls for FtsW in cell division include recruitment of penicillin-binding protein 3 to the division site [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Cell division]
DRLLLFVVLLLLGIGLVMVYSASAAVALRLGGNPFYFLKRQLFYALLGLILMFVASRLPLRFWRKLSVPI
LLIAIVLLVLVLIPGIGKEVNGARRWIGLGGFSIQPSEFAKLALIIYLAWYLARKQKEVKSFLKFLPPLA
VLGLLVGLLLLLQPDFGTTVVIFFITLGMLFLAGAPLRYFALLLLLGLLGGAILIVSSPYRMRRILSFLD
PWADPFGSGYQLTQSLIALGSGGLFGVGLGNSVQKLFYLPEAHTDFIFAVIGEELGFIGVLIVILLFAFL
VWRGLRIALRAEDLFGRYLAAGITIWIGLQAFINIGVVLGLLPTKGLTLPFISYGGSSLVATMIAIGLLL
NISRER
>gnl|CDD|131664 TIGR02615, Stage_V_sporulation_protein_E, stage V sporulation protein E. This model represents an exception within the members of the FtsW model TIGR02614. This exception occurs only in endospore-forming genera such as Bacillus, Geobacillus, and Oceanobacillus. Like FtsW, members are found in a peptidoglycan operon context, but in these genera they part of a larger set of paralogs (not just the pair FtsW and RodA) and are required specifically for sporulation, not for viability [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]
DYLLLIVIMLLVAIGVVMVYSASAYWAEYKFNDSFYFLKRQLLWAILGVFAMFFTMNIDYHTWKRWAKML
MVICFVLLLLVLIPGVGMERNGARRWIGVGAFSIQPSEIAKYALIIYLAKSLSEKQEYITSFRKGVIPYL
LLAGFAFGLIMLQPNLSTATVIVMVCFIMLFVAGARLSHFIALVGIGISGGVALILSAPFRIGRILSFLN
PWEDPLGSGYQIIQSLYALGSGGLFGVGLGQSRQKCFYLPEPHNDFIFAIIGEELGLIGGTFIILLFVIL
LWRGIRIALKAPDLFGTLLAVGITSMIGIQAMINIAVVTGSIPVTGVTLPFISYGGSSLTLMMMAVGILL
NISR
>gnl|CDD|274233 TIGR02616, Tryptophanase_leader_peptide., tryptophanase leader peptide. Members of this family are the apparent leader peptides of tryptophanase operons in Esherichia coli, Vibrio cholerae, Photobacterium profundum, Haemophilus influenzae type b, and related species. All members of the seed alignment are examples ORFs upstream of tryptophanase, with a start codon, a conserved single Trp residue, and several other conserved residues. It is suggested (Konan KV and Yanofsky C) that the nascent peptide interacts with the ribosome once (if) the ribosome reaches the stop codon. Note that this model describes a much broader set (and shorter protein region) than pfam08053 [Energy metabolism, Amino acids and amines, Transcription, Other]
LIHICNLSKWFNIDHRISFFFP
>gnl|CDD|131666 TIGR02617, tnaA_trp_ase, tryptophanase, leader peptide-associated. Members of this family belong to the beta-eliminating lyase family (pfam01212) and act as tryptophanase (L-tryptophan indole-lyase). The tryptophanases of this family, as a rule, are found with a tryptophanase leader peptide (TnaC) encoded upstream. Both tryptophanases (4.1.99.1) and tyrosine phenol-lyases (EC 4.1.99.2) are found between trusted and noise cutoffs, but this model captures nearly all tryptophanases for which the leader peptide gene tnaC can be found upstream [Energy metabolism, Amino acids and amines]
KHLPEPFRIRVIEPVKRTTRAYREKAIIKAGMNPFLLDSEDVFIDLLTDSGTGAVTQSMQAAMMRGDEAY
SGSRSYYALAESVKNIFGYQYTIPTHQGRGAEQIYIPVLIKKREQEKGLDRSKMVAFSNYFFDTTQGHSQ
INGCTARNVYTKEAFDTGVRYDFKGNFDLEGLERGIEEVGPNNVPYIVATITCNSAGGQPVSLANLKAVY
EIAKKYDIPVVMDSARFAENAYFIKQREAEYKNWSIEQITRETYKYADMLAMSAKKDAMVPMGGLLCFKD
DSFFDVYTECRTLCVVQEGFPTYGGLEGGAMERLAVGLYDGMNLDWLAYRINQVQYLVNGLEEIGVVCQQ
AGGHAAFVDAGKLLPHIPADQFPAHALACELYKVAGIRAVEIGSLLLGRDPKTGKQLPCPAELLRLTIPR
ATYTQTHMDFIIEAFKHVKENAPNIKGLTFTYEPKVLRHFTARLKEV
>gnl|CDD|131667 TIGR02618, Tyrosine_phenol-lyase, tyrosine phenol-lyase. This model describes a group of tyrosine phenol-lyase (4.1.99.2) (beta-tyrosinase), a pyridoxal-phosphate enzyme closely related to tryptophanase (4.1.99.1) (see model TIGR02617). Both belong to the beta-eliminating lyase family (pfam01212) [Energy metabolism, Amino acids and amines]
AEPYKIKAVEPISMTTREEREKKMQEAGYNTFLLNSEDVYIDLLTDSGTNAMSDKQWAGLMMGDEAYAGS
RNFYHLERTVRELYGFKYVVPTHQGRGAENLLSQIAIKPGDYVPGNMYFTTTRYHQEKNGATFVDIIIDE
AHDAQLNIPFKGNVDLKKLQKLIDEVGADKIPYICLAVTVNLAGGQPVSMANMREVRELCEAHGIKVFYD
ATRCVENAYFIKEREQGYEDKSIAEILKEMMSYADGCTMSGKKDCLVNIGGFLCMNDDEMFQSAKELVVV
FEGMPSYGGLAGRDMEAMAIGIREAVDYEYIEHRVKQVRYLGDKLKAAGVPIVEPVGGHAVFLDARRFLP
HIPQDQFPAQSLAASIYVETGVRSMERGIVSAGRNNVTGEHHRPKLELVRLTIPRRVYTYAHMDVVADGI
IKLYKHRDDIRGLKMVYEPKQLRFFTARFE
>gnl|CDD|274234 TIGR02619, Uncharacterized_protein_conserved_in_archaea, putative CRISPR-associated protein, APE2256 family. This model represents a conserved domain of about 150 amino acids found in at least five archaeal species and three bacterial species, exclusively in species with CRISPR (Clustered Regularly Interspaced Short Palidromic Repeats). In six of eight species, the member of this family is in the vicinity of a CRISPR/Cas locus
ALVKLVVEDPERCSAELNTVLKAARRSDRLFSGDDKAILYHSDTAQGRFCASILKRFLERELRARQCVAQ
VKVAEGPGRDFYGGLSKLAREAKTDVYVARREGNVVYIAATGGFKPESTFLVLAGSLAGALPVFYIHESF
NDLVMLPMV
>gnl|CDD|200203 TIGR02620, hypothetical_protein, putative CRISPR-associated protein, VVA1548 family. This model represents a conserved domain of about 95 amino acids exclusively in species with CRISPR (Clustered Regularly Interspaced Short Palidromic Repeats). In all bacterial species with members so far (Vibrio vulnificus YJ016, Mannheimia succiniciproducens MBEL55E, and Nitrosomonas europaea ATCC 19718) and but not in the archaeon Methanothermobacter thermautotrophicus str. Delta H, the gene for this protein is in the midst of a cluster of Cas protein gene near CRISPR repeats
WLICRHSGAQEWLSQQGIHIDHVVDHLDLIDISQGDKVIGDLPVSLAADLCKKGARYFELSLDIPHSVRG
TELEAEYLKACDAQLEETEVHIG
>gnl|CDD|274235 TIGR02621, CRISPR-associated_helicase_Cas3, CRISPR-associated helicase Cas3, subtype Dpsyc. This model describes a CRISPR-associated putative DEAH-box helicase, or Cas3, of a subtype found in Actinomyces naeslundii MG1, Geobacter sulfurreducens PCA, Gemmata obscuriglobus UQM 2246, and Desulfotalea psychrophila. This protein includes both DEAH and HD motifs
LDFTDLFRELTGHSPFPWQVRLAERFVAGEPPESCSVPTGLGKTAVIAGWLYALTQDAEQVRRRKVPRRL
VYVVDRRTVVDQSTREAEKIQEALGEAPERSAVRHVLESLRSAFAIPAAAEPLAVSTLRGGFADNDEWTR
DPSRPAVIVGTVDMIGSRLLFRGYGCSPKSRPIHAALLGQDALIVLDEAHLSPAFQETLFVIRSEQQRLE
DFCPLRVVELTATPRTDTPDTLTTLRQEDYKHPTPGKRLDAKKECRLDPQLDEKRLHRDVVPLDLHRKDS
GEAILVFCNTVDTVKKVVAKLPKQARKLEELTGTVRGMERDMLARRSEIFVRFLPPYRTGSEGRPQQGTV
YVVATSTGEVGADLDFDHLVTDLCPFESLVQRFGRVNRFGERPDGSITIVHSTTGKDPDFDGAADIDVEL
IDTLTTLGQLVGRNKRAALGDLDGKERQEAFTPPPVIIPPSDFLFDLWALTSRRQKLPGDPPVHPWLHGP
SEWRPDTHVVWREEVGDLAGCPPEDLLEDYPLKPPELLRDAWSRVFNDLQKLAKRAVKTPVWVIIDDTSV
EVSVLEALVDRGDLVPGQCTVLLPPDGGGLDNGMLDYSGQHVMPVSKDLADLWTGTDRRTSRRRCRIWDD
LGPYSGMREERTLIDVPPDWQEIEEELGADTGHPWWRWYLVEAATEDPDGSKDDADEVTLCGHLDRVGER
AKQWVRALGLGELLVEAVVTAARHHDLGKDDPRFQTALGARVYPPLSLAKSGRRYWNIAMSMYGHPSGWR
HEAASADRLPEFLELSEELADLVLHLVATHHGRFRPHFPEPEHFDAPRHQDPNAASWSEVPSRFHRLNRK
YGRWGLAYLEALLRLADWDASQ
>gnl|CDD|274236 TIGR02622, CDP-glucose_46-dehydratase, CDP-glucose 4,6-dehydratase. Members of this protein family are CDP-glucose 4,6-dehydratase from a variety of Gram-negative and Gram-positive bacteria. Members typically are encoded next to a gene that encodes a glucose-1-phosphate cytidylyltransferase, which produces the substrate, CDP-D-glucose, used by this enzyme to produce CDP-4-keto-6-deoxyglucose [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
FWQGKKVLVTGHTGFKGSWLSLWLLELGAEVYGYSLDPPTSPNLFELLNLAKKIEDHFGDIRDAAKLRKA
IAEFKPEIVFHLAAQPLVRKSYADPLETFETNVMGTVNLLEAIRAIGSVKAVVNVTSDKCYRNDEWVWGY
RETDPLGGHDPYSSSKACAELVIASYRSSFFGVANFHGIKIASARAGNVIGGGDWAEDRLIPDVIRAFSS
NKIVIIRNPDATRPWQHVLEPLSGYLLLAEKLFTGQAEFAGAWNFGPRASDNARVVELVVDALEFWWGDD
AEWEDDSDLNHPHEARLLKLDSSKARTLLGWHPRWGLEEAVSRTVDWYKAWLRGEDMLQLTLEQIKAYM
>gnl|CDD|131672 TIGR02623, Glucose-1-phosphate_cytidylyltransferase, glucose-1-phosphate cytidylyltransferase. Members of this family are the enzyme glucose-1-phosphate cytidylyltransferase, also called CDP-glucose pyrophosphorylase, the product of the rfbF gene [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHM
SDVTFHMADNTMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYLDDEAFCFTYGDGVADIDIKALIAF
HRKHGKKATVTAVQPPGRFGALDLEGEQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPL
ETLAQRGELSAYEHSGFWQPMDTLRDKNYLEELWESGRAPWKVW
>gnl|CDD|131673 TIGR02624, Rhamnulose-1-phosphate_aldolase, rhamnulose-1-phosphate aldolase. Members of this family are the enzyme RhaD, rhamnulose-1-phosphate aldolase
MQDILDSPFVQEMIKTTSDLWRLGWDERNGGNISLRLDEEEVAPYLDFHQVPRKIPLKFPAPELANKYFL
VTGSGKFFRNVEENPAENLGILRVSEDGASVHLLWGLTDGGVPTSELPAHFMSHIARLKVDPENRVIMHC
HATNLIAMTFTHELDEAVFTRTLWQMCTECLVVFPDGVGIIPWMVPGTNEIGEATAEKMKEHRLVLWPHH
GIFGAGPSLDETFGLIETAEKSAEVYTKVYSQGGVKQTISDEQLIALAKRFGVTPKAGYL
>gnl|CDD|131674 TIGR02625, L-rhamnose_mutarotase, L-rhamnose mutarotase. Members of this protein family are rhamnose mutarotase from Escherichia coli, previously designated YiiL as an uncharacterized protein, and close homologs also associated with rhamnose dissimilation operons in other bacterial genomes. Mutarotase is a term for an epimerase that changes optical activity. This enzyme was shown experimentally to interconvert alpha and beta stereoisomers of the pyranose form of L-rhamnose. The crystal structure of this small (104 amino acid) protein shows a locally asymmetric dimer with active site residues of His, Tyr, and Trp [Energy metabolism, Sugars]
RKAFVMYVNPDAHEEYQKRHNEIWPELKEVLKSHGAHNYSIFLDKQRNLLFAYVEIEDEERWNAIAETDI
CQKWWKYMADVMPSNPDNSPVSTDLQEVFYLD
>gnl|CDD|274237 TIGR02627, rhamnulo_kin, rhamnulokinase. This model describes rhamnulokinase, an enzyme that catalyzes the second step in rhamnose catabolism
VAVDLGASSGRVMLASYENECQKLTLEEIHRFKNGLVSQNGHECWDIDALEQEIRLGLNKVDAEGIAPDS
IGIDTWGVDFVLLDQNGQRVGDPVSYRDSRTDGVMAQVQSELGKEAIYQRTGIQFLPFNTLYQLRALTEQ
QPDLLEKVAHFLLIPDYLNYRLTGKKVWEYTNATTTQLVNINTDDWDEDLLAYLGVPAAWFGRPTHPGNV
IGLWECPQGNQIPVVAVATHDTASAVVAAPLQGENAAYLSSGTWSLMGFESQTPITNEQALAANITNEGG
ADGRYRVLKNIMGLWLLQRVCRERDINDLPALIEQAQALPAFKSIINPNDDRFINPENMCEEIQAYCRET
NQPIPESDAELARCIFDSLALLYRQVLLELAELRGKPISQLHIVGGGSQNAFLNQLCADACGIRVIAGPV
EASTLGNIGVQLMALDEINDMAAFRQIVSNNFPL
>gnl|CDD|131676 TIGR02628, fuculo_kin_coli, L-fuculokinase. Members of this family are L-fuculokinase, from the clade that includes the L-fuculokinase of Escherichia coli. This enzyme catalyzes the second step in fucose catabolism. This family belongs to FGGY family of carbohydrate kinases (pfam02782, pfam00370). It is encoded by the kinase (K) gene of the fucose (fuc) operon [Energy metabolism, Sugars]
EVILVLDCGATNLRAIAINRQGKIVASASTPNATKQAIENNDYHIWDLEAIWQKLADCCQQINSELTEKH
IRGIAVTTFGVDGAPFDKQGNQLYPIISWKCPRTAPVMDNIERLLDAQRLYAINGIGAYSFNTLYKLVWL
KEHHPQLFERMHKFVFISSMITHRLTGEFTTDITMAGTSMMTDLTQRNWSPQILQALGLSRRLFPPLVEA
GEQIGTLQNSAAAMLGLPVGVPVISAGHDTQFALFGSGAEQNQPVLSSGTWEILMARSQQVDTSLLSQYA
GSTCELDSQAGLYNPAMQWLASGVLEWVRKLFFTAETPSDHYYQMMIEEARLIANGADGVVNFQCDLLSC
GQGGIQGLTLNTTRGHIYRAALEGLTAQLKRNLQMLEQIGQFKASELLLVGGGSKNTLWNQIRANMLDIP
VKVVDDAETTVAGAAMFGFYGVGEYNSPEEAQAQMHPQYRYFYPQ
>gnl|CDD|131677 TIGR02629, Probable_sugar_isomerase_mlr5709, L-rhamnose catabolism isomerase, Pseudomonas stutzeri subtype. Members of this family are isomerases in the pathway of L-rhamnose catabolism as found in Pseudomonas stutzeri and in a number of the Rhizobiales. This family differs from the L-rhamnose isomerases of Escherichia coli (see TIGR01748). This enzyme catalyzes the isomerization step in rhamnose catabolism. Genetic evidence in Rhizobium leguminosarum bv. trifolii suggests phosphorylation occurs first, then isomerization of the the phosphorylated sugar, but characterization of the recombinant enzyme from Pseudomonas stutzeri does show L-rhamnose isomerase activity. The name given is deliberately vague because the relative order of phosphorylation and isomerization is unclear [Energy metabolism, Sugars]
VVARENARRASALKRDYESLGARLARRGIDIDAVTAKVEKFFVAVPSWGVGTGGTRFARFPGTGEPRGIF
DKLEDCAVIQQLTRATPNVSLHIPWDKADPKELKARGSALGLGFDAMNSNTFSDAPGQAHSYKFGSLSHT
DAATRRQAVEHNLECIEIGKALGSKALTVWIGDGSNFPGQSNFTRAFERYLDAMKAVYAGLPDDWKLFTE
HKMYEPAFYSTVVQDWGTNYLIAQELGPKAFCLVDLGHHAPNVNIEMIVARLIQFKKLGGFHFNDSKYGD
DDLDAGSIDPYRLFLVFNELVDAEARGAKGFDPAHMLDQSHNVTDPIESLMNSANEVRRAYAQALLVDRK
ALSGYQEDNDALMATETLKRAYRTDVEPILAEARLRTGGAIDPVATYRASGYRARVAAERPA
>gnl|CDD|274238 TIGR02630, Xylose_isomerase, xylose isomerase. Members of this family are the enzyme xylose isomerase (5.3.1.5), which interconverts D-xylose and D-xylulose [Energy metabolism, Sugars]
FFPGIPKIQYEGPDSKNPLAFKYYNPEEVIGGKTMKDHLRFAVAYWHTFCGDGGDPFGDGTADRPWDGGT
DPMDKAKAKVDAAFEFFEKLGVPYYCFHDRDIAPEGASLRETNANLDEIVDLIKEKQKETGVKLLWGTAN
LFSHPRYMHGAATSPDADVFAYAAAQVKKALEVTKKLGGENYVFWGGREGYETLLNTDMKRELDHLARFL
HMAVDYAKKIGFKGQFLIEPKPKEPTKHQYDFDAATVYAFLKKYGLDKDFKLNIEANHATLAGHTFEHEL
RVARDNGLLGSIDANQGDLLLGWDTDQFPTDVYETTLAMYEVLKNGGFTTGGLNFDAKVRRESFDPEDLF
IAHIAGMDTFARGLKVAAKLLEDGFLDKFVAERYSSFNSGIGADIEAGKTDLEDLEKYALEKGDDPENKS
GRQEYLESLINRYL
>gnl|CDD|131679 TIGR02631, Xylose_isomerase, xylose isomerase, Arthrobacter type. This model describes a D-xylose isomerase that is also active as a D-glucose isomerase. It is tetrameric and dependent on a divalent cation Mg2+, Co2+ or Mn2+ as characterized in Arthrobacter. Members of this family differ substantially from the D-xylose isomerases of family TIGR02630
YQPTPEDRFTFGLWTVGWVGRDPFGDATRTALDPVEAVHKLAELGAYGVTFHDDDLIPFGAPPQERDQIV
RRFKKALDETGLKVPMVTTNLFSHPVFKDGGFTSNDRSVRRYALRKVLRNMDLGAELGAETYVVWGGREG
AEYDGAKDVRAALDRMREALNLLAAYAEDQGYGLRFALEPKPNEPRGDILLPTVGHALAFIETLERPELF
GLNPETGHEQMAGLNFTHGIAQALWAGKLFHIDLNGQRGIKFDQDLRFGHGDLKAAFFLVDLLESGGYQG
PRHFDYKPSRTEDYDGVWASAKGCMRMYLILKERAEAFRADPEVQEALAASYVDELAAPTLNGGYADLLA
DRSAFAEFDAEAAAARGYAFERLDQLAIEHLL
>gnl|CDD|131680 TIGR02632, conserved_hypothetical_protein, rhamnulose-1-phosphate aldolase/alcohol dehydrogenase
LAELVYRSNLLGADRRITNYGGGNTSAKTTETDPLTGGEVEVMWVKGSGGDLGTMTAANFAGLRLDKLRP
LKERYPGVETEDEMVAYLPHCLFNLNGRAPSIDTPLHAFVPFKHVDHMHPDAIIALACAENGRELTEEIF
GDEVVWVPWRRPGFQLGLDIAAQVDANPQAKGVVLEGHGLVVWGDTAKECYERTLSIINEAEQFIEEKRG
GEAPFGGAAYAALPKEERRALLAAIMPVLRGAISHQRRMIGTFDDSDPVLEFVNSKEAPRLAALGTSCPD
HFLRTKIRPLFIDWVPDAPDLEGLVAALLNGLAAYREDYARYYERHRRPDSPTMRDPNPRVLLIPGVGMI
SFGKDKETARVAREFYVNAINVMRGAEAVSEYVSLPEQEAFDIEYWPLEEAKLRRMPKEKTLARRVAFVT
GGAGGIGRETARRLAAEGAHVVLADLNLEAAEAVAAEINGQFGAGRAVALKMDVTDEQAVKAAFADVALA
YGGVDIVVNNAGIATSSPFEETTLQEWQLNLDILATGYFLVAREAFRQMREQGLGGNIVFIASKNAVYAG
KNASAYSAAKAAEAHLARCLAAEGGTYGIRVNTVNPDAVLQGSGIWDGEWREERAAAYGIPADELEEHYA
KRTLLKRHIFPADIAEAVFFLASSKSEKTTGCIITVDGGVPAAFLR
>gnl|CDD|131681 TIGR02633, Xylose_import_ATP-binding_protein_XylG, D-xylose ABC transporter, ATP-binding protein. Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005) [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKAS
NIRDTERAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVG
DYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDT
ICVIRDGQHVATKDMSTMSEDDIITMMVGREITSLYPHEPHEIGDVILEARNLTCWDVINPHRKRVDDVS
FSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGI
VPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLT
NPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHAL
TQEQVLAAAL
>gnl|CDD|188237 TIGR02634, D-xylose-binding_periplasmic_protein, D-xylose ABC transporter, substrate-binding protein. Members of this family are periplasmic (when in Gram-negative bacteria) binding proteins for D-xylose import by a high-affinity ATP-binding cassette (ABC) transporter [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
IGMSIDDLRLERWQKDRDIFVAKAESLGAKVFVQSANGNEAKQISQIENLINRGVDVLVIIPYNGEVLSN
AVQEAKDEGIKVLAYDRLINDADIDFYLSFDNEKVGEMQAKAVLAAAPKGNYFLMGGSPTDNNAKLLRGG
QMKVLQPAIDSGDIKIVGDQWVDGWLPENALKIMENALTANDNKIDAVVASNDATAGGAIQALSAQGLSG
KVPISGQDADLAAIKRVADGTQTMTVYKPITLLANKAAEIAVELGNGEKPGADTTLNNGLKKVPARLLTP
IPVTKDNIKTVVKDGFHTKETL
>gnl|CDD|274239 TIGR02635, putative_xylose_isomerase, L-rhamnose isomerase, Streptomyces subtype. This clade of sequences is closely related to the L-rhamnose isomerases found in Pseudomonas stutzeri and in a number of the Rhizobiales (TIGR02629). The genes of the family represented here are found in similar genomic contexts which contain genes apparently involved in rhamnose catabolism such as rhamnulose-1-phosphate aldolase (TIGR02632), sugar kinases, and sugar transporters [Energy metabolism, Sugars]
LEEVEKKLKALKIETPSWAYGNSGTRFKVFHQEGAARNVFEKIEDAALVHRLTGICPTVALHIPWDRVED
YEELARYAEELGLKIGAINPNLFQDDDYKFGSLTHPDKRIRRKAIDHLLECVDIAKKTGSKDISLWLADG
TNYPGQDDFRSRKDRLEESLAEVYEHLGADMRLLIEYKFFEPAFYHTDIPDWGTAYALSEKLGERALVLV
DTGHHAQGTNIEFIVATLLDEKKLGGFHFNSRKYADDDLTVGAINPYELFLIFKEIVRAGRDPEDSASDV
ALMLDQCHNLEPKIPAMIRSVLNVQELFAKALLVDRDALRKAQENGDVLEAEAVLMDAFETDVRPLLAEV
REEMGLPEDPLKAYRESGYMEKIAAERR
>gnl|CDD|274240 TIGR02636, Aldose_1-epimerase_Mutarotase., galactose mutarotase. Members of this protein family act as galactose mutarotase (D-galactose 1-epimerase) and participate in the Leloir pathway for galactose/glucose interconversion. All members of the seed alignment for this model are found in gene clusters with other enzymes of the Leloir pathway. This enzyme family belongs to the aldose 1-epimerase family, described by pfam01263. However, the enzyme described as aldose 1-epimerase itself (EC 5.1.3.3) is called broadly specific for D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose. The restricted genome context for genes in this family suggests members should act primarily on D-galactose
GQPAQLITLTNKNGMTISFMDIGATWLSCQVPLAGELREVLLGFASAEEYLKQDAYLGATVGRYANRIAN
GSFEIDGKTYQLSINQGPNCLHGGPEGFDKRRWTIETLEQAEVQVKFSLESPDGDQGFPGNLTVSVTYTL
TDDNELKIDYEATTDKATPFNLTNHVYFNLDGADAGSDVLNHELQLNADRYLPLDEEGIPLGQLKPVDGT
SFDFRKEKAIGQDFLANDQQQLAKGYDHAFLLNGERLDGKEAARLTSPDEDLSLEVFTNQPALQIYTGNF
LAGTPNRGGKKYVDHAGIALETQFLPDSPNHPEWGDISCILSPGQEYQHQTRYQFI
>gnl|CDD|131685 TIGR02637, putative_secreted_solute-binding_lipoprotein, rhamnose ABC transporter, rhamnose-binding protein. This sugar-binding component of ABC transporter complexes is found in rhamnose catabolism operon contexts. Mutation of this gene in Rhizobium leguminosarum abolishes rhamnose transport and prevents growth on rhamnose as a carbon source
IGLVVKSLGNPFFEAANKGAEEAAKELGSVYIIYTGPTGTTAEGQIEVVNSLIAQKVDAIAISANDPDAL
VPALKKAMKRGIKVVTWDSGVAPEGRNLFLNQASADLIGRTQVQLAAEQIGNGGEIAILSAASTATNQNA
WIEIMKKELKDPKYPKVKLVATVYGDDDAQKSYQEAQGLLKSYPNLKGIIAPTTVGIKAAAQAVSDAKLI
GKVKLTGLGLPSEMAKYVKNGTVKAFALWNPIDLGYSAAYTAYRLSSGEITGKPGETFKAGRMGEYTIGD
NGVAALGPPFVFDADNIDQFSK
>gnl|CDD|131686 TIGR02638, Lactaldehyde_reductase_Propanediol_oxidoreductase., lactaldehyde reductase. This clade of genes encoding iron-containing alcohol dehydrogenase (pfam00465) proteins is generally found in apparent operons for the catabolism of rhamnose or fucose. Catabolism of both of these monosaccharides results in lactaldehyde which is reduced by this enzyme to 1,2 propanediol. This protein is alternatively known by the name 1,2 propanediol oxidoreductase. This enzyme is active under anaerobic conditions in E. coli while being inactivated by reactive oxygen species under aerobic conditions. Under aerobic conditions the lactaldehyde product of rhamnose and fucose catabolism is believed to be oxidized to lactate by a separate enzyme, lactaldehyde dehydrogenase [Energy metabolism, Sugars]
SNRLILNETSYFGAGAIEDIVDEVKRRGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNP
TITVVKAGVAAFKASGADYLIAIGGGSPIDTAKAIGIISNNPEFADVRSLEGVAPTKKPGVPIIAIPTTA
GTAAEVTINYVITDEENKRKFVCVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWE
LTDMLHLKAIEIIARWLRSAVEGGKDLEAREQMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVA
NAILLPHVMEFNAEFTGEKYREIAKAMGVKTEGMSDEEARDAAVEAVKTLSKRVGIPEGLSELGVKEEDI
PALAEAALADVCTGGNPRETTVEEIEELY
>gnl|CDD|274241 TIGR02639, ATP-dependent_Clp_protease_subunit, ATP-dependent Clp protease ATP-binding subunit clpA [Protein fate, Degradation of proteins, peptides, and glycopeptides]
ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIEILEECGGDVELLRKRLEDYLEENLPVIPE
DIDEEPEQTVGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGI
SKDDGKDQLGEEAGKEEEKGQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGE
PGVGKTAIVEGLALRIAEGKVPERLKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFID
EIHTIVGAGATSGGSMDASNLLKPALSSGKIRCIGSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETV
KILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVIDEAGAAFRLRPKAKKKANVNVKD
IENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVG
PTGVGKTELAKQLAEELGVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDE
IEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFGGENRESKSLKAIKKL
FSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLA
RVIQEEIKKPLSDEILFGKLKKGGSVKISL
>gnl|CDD|131688 TIGR02640, Gas_vesicle_protein_GvpN, gas vesicle protein GvpN. Members of this family are the GvpN protein associated with the production of gas vesicles produced in some prokaryotes to give cells buoyancy. This family belongs to a larger family of ATPases (pfam07728) [Cellular processes, Other]
FIETDAVKRVTSRALRYLKSGYPVHLRGPAGTGKTTLAMHVARKRDRPVMLINGDAELTTSDLVGSYAGY
TRKKVHDQFIHNVVKLEDIVRQNWVDNRLTLAVREGFTLVYDEFTRSKPETNNVLLSVFEEGVLELPGKR
GTSRYVDVHPEFRVIFTSNPVEYAGVHETQDALLDRLITIFMDYPDIDTETAILRAKTDVAEDSAATIVR
LVREFRASGDEITSGLRASLMIAEVATQQDIPVDVDDEDFVDLCIDILASRV
>gnl|CDD|274242 TIGR02641, Gas_vesicle_protein_C, gas vesicle protein GvpC repeat. This model describes a 33-amino acid repeated domain in bacterial versions of the gas vesicle protein GvpC, a structural protein less abundant than GvpA [Cellular processes, Other]
VQQLQQETQEFLAQTAQERQAQAKAQAQQLHQF
>gnl|CDD|274243 TIGR02642, hypothetical_protein_YPTB1803, uncharacterized phage protein. This uncharacterized protein is found in prophage regions of Shewanella oneidensis MR-1, Vibrio vulnificus YJ016, Yersinia pseudotuberculosis IP 32953, and Aeromonas hydrophila ATCC7966. It appears to have regions of sequence similarity to phage lambda antitermination protein Q [Mobile and extrachromosomal element functions, Prophage functions]
MTKSIEMLTILSSPRGMSIEERTAKRGPNVLTKEQLLGAIALAQRDNPIGIAILMAKYMRDAYAIQKLYA
HICEQLLPLITPNAAEAASYLAVNEVLNSCKCPRCRGTGLIQRRQRECDTCAGTGRFRPTVEDLLKSFGV
DSGAAIVLKDNWPQVVTSVRAQVDALRRHESDAARVVERRIRLEFE
>gnl|CDD|131691 TIGR02643, Thymidine_phosphorylase, thymidine phosphorylase. Thymidine phosphorylase (alternate name: pyrimidine phosphorylase), EC 2.4.2.4, is the designation for the enzyme of E. coli and other Proteobacteria involved in (deoxy)nucleotide degradation. It often occurs in an operon with a deoxyribose-phosphate aldolase, phosphopentomutase and a purine nucleoside phosphorylase. In many other lineages, the corresponding enzyme is designated pyrimidine-nucleoside phosphorylase (EC 2.4.2.2); the naming convention imposed by this model represents standard literature practice [Purines, pyrimidines, nucleosides, and nucleotides, Other]
FLPQEIIRKKRDGHSLSDAEIAQFINGITDGSVSEGQIAAFAMAVFFNGMNRDERVALTLAMRDSGDVLD
WRSLDLNGPVVDKHSTGGVGDVVSLMLGPIVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYDIFPDPAL
FRRVVKDVGVAIIGQTADLAPADKRFYATRDVTATVESIPLITASILSKKLAAGLDALVMDVKVGNGAFM
PTYEESEELARSLVDVANGAGVRTTALITDMNQPLASAAGNAVEVRNAVDFLTGEKRNPRLEDVTMALAA
EMLVSGGLAADEAEARAKLQAVLDSGRAAERFARMVAALGGPADFVENPERYLATAPLIKPVYADREGYV
SEMDTRALGMAVVALGGGRRKADDTIDYSVGLTDLLPLGDRVEKGEPLAVVHAADESDAEEAAKRVKAAY
RIADEAPESTPVVYRRI
>gnl|CDD|274244 TIGR02644, Thymidine_phosphorylase, pyrimidine-nucleoside phosphorylase. In general, members of this protein family are designated pyrimidine-nucleoside phosphorylase, enzyme family EC 2.4.2.2, as in Bacillus subtilis, and more narrowly as the enzyme family EC 2.4.2.4, thymidine phosphorylase (alternate name: pyrimidine phosphorylase), as in Escherichia coli. The set of proteins encompassed by this model is designated subfamily rather than equivalog for this reason; the protein name from this model should be used when TIGR02643 does not score above trusted cutoff [Purines, pyrimidines, nucleosides, and nucleotides, Other]
AVDIIRKKRDGKKLSDEEINFFINGYTNGEIPDYQMSALLMAIYFNGMTDEETAYLTKAMIDSGEVLDLS
SLPGPKVDKHSTGGVGDKVSLVLGPIVAACGVKVAKMSGRGLGHTGGTIDKLESIPGFRTELSEAEFIEI
VNKVGLAIIGQTKDLAPADKKLYALRDVTGTVDSIPLIASSIMSKKLAAGADAIVLDVKVGSGAFMKTLE
DAKELAKLMVEIGKGAGRKTSALLTDMNQPLGRAIGNALEVKEAVEFLKGEGPADLKELTLALAAEMLLL
AGIAKTEKEARALAEDVLESGKALEKFRRFVEAQGGDPDVIKNLDKLPKAKYKEEVKAEKSGYISEIDAE
ELGLAAVDLGAGRARKEDKIDHEAGIYLHKKTGDRVKKGDPLATLYSSDPISLEA
>gnl|CDD|274245 TIGR02645, AMP_phosphorylase, putative thymidine phosphorylase. Members of this family are closely related to characterized examples of thymidine phosphorylase (EC 2.4.2.4) and pyrimidine nucleoside phosphorylase (RC 2.4.2.2). Most examples are found in the archaea, but other examples in Legionella pneumophila str. Paris and Rhodopseudomonas palustris CGA009
LKVRPLNIDTGQEHVLINSPDLRAEGFTPQDRVEVRIGGKSLIAILVGSDTLVEMGEIGLSVSAVETFMA
REGDIVTVTPAEAPESLRAIRKKIDGAKLDQHEIASIVGDIVDERLSDVEISAFLTASAINGMTMDEIEA
LTIAMADTGEMLEWDREPIMDKHSIGGVPGNKTSLIVVPIVAAAGLLIPKTSSRAITSAAGTADTMEVLT
RVALSAEEIKRIVEKVGGCLVWGGALNLAPADDVLIRVERPLSIDPRAQMLASIMSKKIAAGSTHVLIDI
PVGPGAKVRSLQEAERLARLFIELGDRLGVRVECAITYGSQPIGRGIGPALEAKEALAVLERSPAAPFSL
REKSLLLAGILLEMGGAAPRGAGKELARELLDSGKALEKMKEIIEAQGGDPNKSDDIEAGIYTADIHAET
DGYVTEIDNKHITRIARLAGAPNDKGAGVELHVKVGDQVKKGDPLYTIYAESEGELDYAIALARRLNPIK
VEG
>gnl|CDD|131694 TIGR02646, Hypothetical_protein_SMc04429, TIGR02646 family protein. Members of this uncharacterized protein family are found exclusively in bacteria. Neighboring genes in various genomes are also uncharacterized or may annotated as similar to restriction system proteins [Hypothetical proteins, Conserved]
APSWPDLQNDHKDEVHNQLLQLQGGLCAYCEREIELLGSHIEHFRPKGAYPPLTLDWSNLFGSCHRESKQ
GNPLHCGRFKDNSCGSNNFDELIDPLADDCEQLFTYLLTGKIEPRESRAPTDVEKAKETIEVLNLNAKRL
TRRR
>gnl|CDD|131695 TIGR02647, protein_inhibitor_Id-2-related_protein, TIGR02647 family protein. Members of this family are found, so far, only in the Gammaproteobacteria. The function is unknown. The location on the chromosome usually is not far from housekeeping genes rather than in what is clearly, say, a prophage region. Some members have been annotated in public databases as DNA-binding protein inhibitor Id-2-related protein, putative transcriptional regulator, or hypothetical DNA binding protein [Hypothetical proteins, Conserved]
MKYTPELIAELELLALFNLSSTQEGIKVHSTASPAAVAAAARLHEKGLTTQPDGGYLTSLGLEAAEHAQK
LLTILSA
>gnl|CDD|131696 TIGR02648, DNA_replication_terminus_site-binding_protein, DNA replication terminus site-binding protein. Members of this protein family are found on the main chromosomes of a number of the Gammaproteobacteria; this model excludes related plasmid proteins, which score between trusted and noise cutoffs. This protein, DNA replication terminus site-binding protein, binds specific DNA sites near the replication terminus to arrest the DNA replication fork [DNA metabolism, DNA replication, recombination, and repair]
LNTCFQQLEQKLAQLAQQLEQYKLLAARVFSLPEVEKGTEHNPIERIEVNQHLGNDARSLGLRHFQRLFI
HHQSENRSSKAAVRLPGVLCFSVNNLQYAAAVSLIQEINKLKAELEHIVTVESGLPTEQRFEFVHSHLHG
LITLNAYRTLTPLHNPASVRFGWANKHIIKNVTRDEILAQLEKSLNSGRAVAPYTREQWQELVEREIQDI
AALPEDAVLKIKRPVKVQPIARVWYAEQQKQVQHACPTPLIALCQRDNGAGVPKIGELLNYDADNIKHRY
KPKAKPLRLIIPRLHLYVED
>gnl|CDD|131697 TIGR02649, Ribonuclease_BN, ribonuclease BN. Members of this protein family are ribonuclease BN of Escherichia coli K-12 and closely related proteins believed to be equivalent in function. Note that E. coli appears to lack RNase Z per se, and this protein of E. coli appears orthologous to (but not functionally equivalent to) RNase Z of Bacillus subtilis and various other species. Meanwhile, the yihY gene product of E. coli previously was incorrectly identified as RNase BN [Transcription, RNA processing]
LIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFG
LPGLLCSRSMSGIIQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEILDDGLRKVTAYPLEHP
LECYGYRIEEHDKPGALNAQALKAAGVPPGPLFQELKAGKTITLEDGRQINGADYLAAPVPGKALAIFGD
TGPCDAALDLAKGVDVMVHEATLDITMEAKANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQH
LLRECRSIFPATELANDFTVFNV
>gnl|CDD|188239 TIGR02650, RNase_Z_T_toga, ribonuclease Z, Thermotoga type. Members of this protein family are ribonuclease Z as found in the genus Thermotoga, where the enzyme cleaves after the CCA, in contrast to the activities characterized for other enzymes also designated ribonuclease Z. In other systems, cleavage occurs 5-prime to the location of the CCA sequence, and CCA is added subsequently. A species may lack ribonuclease Z if all tRNA genes encode the CCA sequence, or if the CCA is exposed by exonuclease activity rather than endonuclease activity. Note that members of this sequence family differ considerably from the majority of RNase Z sequences [Transcription, RNA processing]
NIIGFSKALFSTWIYYSPERILFDAGEGVSTTLGSKVYAFKYVFLTHGHVDHIAGLWGVVNIRNNGMGDR
EKPLDVFYPEGNRAVEEYTEFIKKANPDLRFSFNVHPLEEGDRVFLRDAGGFKRYVQPFRTKHVASEVSF
GYHIFEVRRKLKEEFQGLDSKEIARLVKEKGRDFVTEEYHKKILTISGDSLALDPEEIEGTELLIHECTF
LDARDRRYKNHAAIDEVMESVKAAGVKKVILYHISTRYIRQIKSVIKKYREELPDVEILYMDPRKVF
>gnl|CDD|274246 TIGR02651, Ribonuclease_Z, ribonuclease Z. Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN [Transcription, RNA processing]
EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPG
LLSTMSFQGRKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGLVFEDDGFKVEAFPLDHSIP
SLGYRFEEKDRPGKFDREKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTR
PCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEELLEE
AKKIFPNTYIAEDFMEIEI
>gnl|CDD|131700 TIGR02652, hypothetical_protein, TIGR02652 family protein. Members of this family of conserved hypothetical proteins are found, so far, only in the Cyanobacteria. Members are about 170 amino acids long and share a motif CxxCx(14)CxxH near the amino end [Hypothetical proteins, Conserved]
AQYPIFGPEIRCPHCRQNIPALTLTDTYLCNRHGAFEADPETGELVHLQSGRRWRLWEGQWYRQHTHPDG
IRFEIHEALDRLFTQGYRATRVIIAERYRELLRSYLERSTGLGAAACSEHRLYGLPVEFSPAAKQDPRWA
VINFELEKEPGAPLRYPYFRLFD
>gnl|CDD|131701 TIGR02653, putative_ATP-dependent_Lon_protease, conserved hypothetical protein. This model describes a protein family of unknown function, about 690 residues in length, in which some members show C-terminal sequence similarity to pfam05362, which is the Lon protease C-terminal proteolytic domain, from MEROPS family S16. However, the annotated catalytic sites of E. coli Lon protease are not conserved in members of this family. Members have a motif GP[RK][GS]TGKS, similar to the ATP-binding P-loop motif GxxGxGK[ST] [Hypothetical proteins, Conserved]
SDDLDAKLNQHFSGRVVRKDLTKQLKVGANVPVYVLEYLLGMYCASDDEEVVEQGLQNVKNILAENYVRP
DEAEKVKSLIRERGRYTIIDKVSVKLNQKKDVYEAELSNLGIKDALIPERYVRDYDKLLTGGIWCMITVR
YFFEEGQKTSPFSIMSLKPIQMPNMDMNEVFEGRRHFTSDEWIDVLLRSVGMEPTNLERRTKWHLLTRLI
PLVENNYNLCELGPRGTGKSHVYKECSPNSILMSGGQTTVANLFYNMSTRQIGLVGMWDVVAFDEVAGIE
FKDKDGVQIMKDYMASGSFARGKESIEGKASIVFVGNINQSVETLVKTSHLFAPFPEAMRIDTAFFDRFH
YYIPGWEIPKMRPEYFTNRYGFIVDYLAEYMREMRKRSFADAIDRFFKLGNNLNQRDVIAVRKTVSGLLK
LLYPDGEYTKDDVRECLTYAMEGRRRVKEQLKKLGGFEFFDVNFSYIDNESLEEFFVSVPEQGGSKLIPA
GPPKPGVVYAVTQNESGKVGLYRFEVQVSAGSGKHSVSGLGSNTTAKESIRVAFDYFKGNLVRISASAKF
SEHDYHLHVVDLHNTGPSTEASLAALIALCSALLKRPVQEQMVILGSMTIGGVINPVQDLAGSLQLAMDS
GAKRVLIPMSSARDIPTVPAELFSKFQISFYSDPVDAVYKALGLN
>gnl|CDD|211759 TIGR02654, Circadian_clock_protein_KaiB, circadian clock protein KaiB. Members of this protein family are the circadian clock protein KaiB of Cyanobacteria, encoded in the circadian clock gene cluster kaiABC. KaiB has homologs of unknown function in some Archaea and Proteobacteria, and has paralogs of unknown function in some Cyanobacteria. KaiB forms homodimers, homotetramers, and multimeric complexes with KaiA and/or KaiC [Cellular processes, Other]
RKTYVLKLYVAGNTPNSVRALKTLKNILETEFQGVYALKVIDVLKNPQLAEEDKILATPTLSKILPPPVR
KIIGDLSDRERVLIGLD
>gnl|CDD|131703 TIGR02655, Circadian_clock_protein_kinase_KaiC, circadian clock protein KaiC. Members of this family are the circadian clock protein KaiC, part of the kaiABC operon that controls circadian rhythm. It may be universal in Cyanobacteria. Each member has two copies of the KaiC domain (pfam06745), which is also found in other proteins. KaiC performs autophosphorylation and acts as its own transcriptional repressor [Cellular processes, Other]
AKIRTMIEGFDDISHGGLPIGRSTLVSGTSGTGKTLFSIQFLYNGIIHFDEPGVFVTFEESPQDIIKNAR
SFGWDLQKLVDEGKLFILDASPDPEGQDVVGGFDLSALIERINYAIRKYKAKRVSIDSVTAVFQQYDAVS
VVRREIFRLVARLKQIGVTTVMTTERIEEYGPIARYGVEEFVSDNVVILRNVLEGERRRRTLEILKLRGT
SHMKGEYPFTITDHGINIFPLGAMRLTQRSSNVRVSSGVVRLDEMCGGGFFKDSIILATGATGTGKTLLV
SKFLENACANKERAILFAYEESRAQLLRNAYSWGIDFEEMEQQGLLKIICAYPESAGLEDHLQIIKSEIA
DFKPARIAIDSLSALARGVSNNAFRQFVIGVTGYAKQEEITGFFTNTSDQFMGSHSITDSHISTITDTIL
MLQYVEIRGEMSRAINVFKMRGSWHDKGIREFMISDKGPEIKDSFRNFERIISGSPTRVTVDEK
>gnl|CDD|274247 TIGR02656, Plastocyanin_chloroplastic, plastocyanin. Members of this family are plastocyanin, a blue copper protein related to pseudoazurin, halocyanin, amicyanin, etc. This protein, located in the thylakoid luman, performs electron transport to photosystem I in Cyanobacteria and chloroplasts [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]
VTVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESY
EVTFSTPGTYTFYCEPHRGAGMVGKITVE
>gnl|CDD|131705 TIGR02657, amicyanin, amicyanin. Members of this family are amicyanin, a type I blue copper protein that accepts electrons from the tryptophan tryptophylquinone (TTQ) cofactor of the methylamine dehydrogenase light chain and then transfers them to the heme group of cytochrome c-551i. Amicyanin, methylamine dehydrogenase, and cytochrome c-551i are periplasmic and form a complex. This system has been studied primarily in Paracoccus denitrificans and Methylobacterium extorquens. Related type I blue copper proteins include plastocyanin, pseudoazurin, halocyanin, etc [Energy metabolism, Electron transport]
VDIAKMKYETPELHVKVGDTVTWINREAMPHNVHFVAGVLGEAALKGPMMKKEQAYSLTFTEAGTYDYHC
TPHPFMRGKVVVE
>gnl|CDD|131706 TIGR02658, Methylamine_dehydrogenase_heavy_chain, methylamine dehydrogenase (amicyanin) heavy chain. This family consists of the heavy chain of methylamine dehydrogenase light chain, a periplasmic enzyme. The enzyme contains a tryptophan tryptophylquinone (TTQ) prothetic group derived from two Trp residues in the light subunity. The enzyme forms a complex with the type I blue copper protein amicyanin and a cytochrome. Electron transfer procedes from TQQ to the copper and then to the heme group of the cytochrome [Energy metabolism, Amino acids and amines]
EPRILEAPASDARRVYVLDPGHFAATTQVYTIDGEAGRVLGMTDGGFLPNPVVASDGSFFAHASTVYSRI
ARGKRTDYVEVIDPQTHLPIADIELPEGPRFLVGTYPWMTSLTPDNKTLLFYQFSPSPAVGVVDLEGKAF
VRMMDVPDCYHIFPTANDTFFMHCRDGSLAKVGYGTKGNPKIKPTEVFHPEDEYLINHPAYSNKSGRLVW
PTYTGKIFQIDLSSGDAKFLPAIEAFTEAEKADGWRPGGWQQVAYHRARDRIYLLADQRAKWTHKTASRF
LFVVDAKTGKRLRKIELGHEIDSINVSQDAKPLLYALSTGDKTLYIFDAETGKELSSVNQLGRGPQVITT
AD
>gnl|CDD|131707 TIGR02659, Methylamine_dehydrogenase_light_chain, methylamine dehydrogenase (amicyanin) light chain. This family consists of the light chain of methylamine dehydrogenase light chain, a periplasmic enzyme. This subunit contains a tryptophan tryptophylquinone (TTQ) prothetic group derived from Trp-114 and Trp-165 of the precursor, numbered according to the sequence from Paracoccus denitrificans. The enzyme forms a complex with the type I blue copper protein amicyanin and cytochrome. Electron transfer procedes from TQQ to the copper and then to the heme group of the cytochrome [Energy metabolism, Amino acids and amines]
MLGNFRFDDMVEKLSRRVAGKTSRRGFIGRLGTALAGSALVPLLPVDRRGRVSRANAATTGNDPRAKWKP
QDNDIQACDYWRHCSIDGNICDCSGGSLTSCPPGTKLATSSWVASCYNPTDGQSYLIAYRDCCGYNVSGR
CPCLNTEGELPVYRPEFANDIIWCFGAEDDAMTYHCTISPIVGKAS
>gnl|CDD|274248 TIGR02660, Homocitrate_synthase, homocitrate synthase NifV. This family consists of the NifV clade of homocitrate synthases, most of which are found in operons for nitrogen fixation. Members are closely homologous to enzymes that include 2-isopropylmalate synthase, (R)-citramalate synthase, and homocitrate synthases associated with other processes. The homocitrate made by this enzyme becomes a part of the iron-molybdenum cofactor of nitrogenase [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]
PVIINDTTLRDGEQAPGVAFTAAEKLAIARALDEAGVDELEVGIPAMGEEERAVIRAIVALGLPARLMAW
CRARDADIEAAARCGVDAVHISIPVSDLQIEAKLRKDRAWVLERLARLVSFARDRGLFVSVGGEDASRAD
PDFLVELAEVAAEAGADRFRFADTVGILDPFSTYELVRALRQAVDLPLEMHAHNDLGMATANTLAAVRAG
ATHVNTTVNGLGERAGNAALEEVAMALKRLLGRDTGIDTSRLPALSQLVARASGRPIPPQKPVVGESVFT
HESGIHVDGLLKDPRTYEPFDPELVGRSRRIVIGKHSGRAALINALAQLGIPLSEEEAAALLPAVRAFAT
RLKRPLSDAELIALY
>gnl|CDD|131709 TIGR02661, Methylamine_utilization_protein_MauD, methylamine dehydrogenase accessory protein MauD. This protein, MauD, appears critical to proper formation of the small subunit of methylamine dehydrogenase, which has both an unusual tryptophan tryptophylquinone cofactor and multiple disulfide bonds. MauD shares sequence similarity, including a CPxC motif, with a number of thiol:disulfide interchange proteins. In MauD mutants, the small subunit apparently does not form properly and is rapidly degraded [Protein fate, Protein folding and stabilization, Energy metabolism, Amino acids and amines]
FLIASNVLLWLAFLGLAVLMLGLIRQVGLLHERSSPMGAMITDHGPDVGDAAPIFNLPDFDGEPVRIGGS
IAPGRPTLLMFTAPSCPVCDKLFPIIKSIARAEETDVVMISDGTPAEHRRFLKDHELGGERYVVSAEIGM
AFQVGKIPYGVLLDQDGKIRAKGLTNTREHLESLLEADREGFASLQQYM
>gnl|CDD|131710 TIGR02662, ADP-ribosyl-_glycohydrolase, ADP-ribosyl-[dinitrogen reductase] hydrolase. Members of this family are the enzyme ADP-ribosyl-[dinitrogen reductase] hydrolase (EC 3.2.2.24), better known as Dinitrogenase Reductase Activating Glycohydrolase, DRAG. This enzyme reverses a regulatory inactivation of dinitrogen reductase caused by the action of NAD(+)--dinitrogen-reductase ADP-D-ribosyltransferase (EC 2.4.2.37) (DRAT). This enzyme is restricted to nitrogen-fixing bacteria and belongs to the larger family of ADP-ribosylglycohydrolases described by pfam03747 [Central intermediary metabolism, Nitrogen fixation]
IRSRALGAYLGLAVGDALGATVEFMTKGEIAAQYGVHRHITGGGWLRLKPGQVTDDTEMSLALGRAILAA
GEWDVTRIAEEFAVWLKSKPVDVGNTCRRGIRRFMLHGTLSAPESEWDAGNGAAMRNLPAALATLGDDAA
FERWSVEQAHITHNHPLSDAATLTLGRMVHRLVLGGSVRDVRREANRLIAKHRTFKFEPYRGLSTAYIVD
TMQTVLHYYFQTDSFESCLIETVNQGGDADTTGAIAGMLAGATYGVEGIPPRWLKKLDRKVYREICAQVD
ALLARAP
>gnl|CDD|131711 TIGR02663, Protein_NifX, nitrogen fixation protein NifX. Members of this family are NifX proteins encoded within operons for nitrogen fixation in a number of bacteria. NifX, NafY, and the C-terminal region of NifB all belong to the pfam02579 and are involved in MoFe cofactor biosynthesis. NifX is a nitrogenase accessory protein with a role in expression of the MoFe cofactor [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]
MKVAFATQDLENLNAHFGSAKQFAIYDVTAEGARFVEAIQFDGASDEDGEEDKIAPKIEALKDCAILYCL
AIGGPAAAKVVAAKIHPIKVNEPESISELLERLQKMLKGNPPPWLRKAL
>gnl|CDD|131712 TIGR02664, conserved_hypothetical_protein, conserved hypothetical protein. Most members of this protein family are found in the Cyanobacteria, and these mostly near nitrate reductase genes and molybdopterin biosynthesis genes. We note that molybdopterin guanine dinucleotide is a cofactor for nitrate reductase. This protein is sometimes annotated as nitrate reductase-associated protein. Its function is unknown
LFEFEQDFSESLRCIPMIVRYKLDLCGVKLKLEHWQQLTQAEREELVRLPCDTAEVIDPYREYLRDLLRT
HADTPPSDLPPDEHAAWQSVSALPDAIVAQAGEVGLVALTASQWATLTPLQRFALTKLSRSGHENHNFPP
ALAEF
>gnl|CDD|274249 TIGR02665, Molybdenum_cofactor_guanylyltransferase, molybdenum cofactor guanylyltransferase, proteobacterial. In many molybdopterin-containing enzymes, including nitrate reductase and dimethylsulfoxide reductase, the cofactor is molybdopterin-guanine dinucleotide. The family described here contains MobA, molybdenum cofactor guanylyltransferase, from the Proteobacteria only. MobA can reconstitute molybdopterin-guanine dinucleotide biosynthesis without the product of the neighboring gene MobB. The probable MobA proteins of other lineages differ sufficiently that they are not included in scope of this family [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
ISGVILAGGRARRMGGRDKGLVELGGKPLIEHVLARLRPQVSDLAISANRNPERYAQAGFGLPVVPDALA
DFPGPLAGILAGLRWAGTDWVLTVPCDTPFLPEDLVARLAAALEASDADIAVAHDGGRWHPVFALWPVAL
APDLEAFLAAGERRVRRFYARHGAVAVDFSDSPDAFANLNTPEDLA
>gnl|CDD|274250 TIGR02666, Cyclic_pyranopterin_monophosphate_synthase, molybdenum cofactor biosynthesis protein A, bacterial. The model for this family describes molybdenum cofactor biosynthesis protein A, or MoaA, as found in bacteria. It does not include the family of probable functional equivalent proteins from the archaea. MoaA works together with MoaC to synthesize precursor Z from guanine [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEP
LLRKDLVELVARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGRLEQ
VLAGIDAALAAGLEPVKLNTVVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSADEI
LERLEQAFGPLEPVPSPRGNGPAPAYRWRLPGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADD
GVDLRPLLRGGASDALLEAIIQAILQKKPEGHSFLRFTSPANKRRKRAMSQIGG
>gnl|CDD|131715 TIGR02667, Molybdenum_cofactor_biosynthesis_protein_B., molybdenum cofactor biosynthesis protein B, proteobacterial. This model represents the MoaB protein molybdopterin biosynthesis regions in Proteobacteria. This crystallized but incompletely characterized protein is thought to be involved in, though not required for, early steps in molybdopterin biosynthesis. It may bind a molybdopterin precursor. A distinctive conserved motif PCN near the C-terminus helps distinguish this clade from other homologs, including sets of proteins designated MogA [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
PFIPLRIAILTVSDTRTEEDDTSGQYLVERLTEAGHRLADRAIVKDDIYQIRAQVSAWIADPDVQVILIT
GGTGFTGRDVTPEALEPLFDKTVEGFGELFRQLSYEEIGTSTIQSRALAGLANGTFVFCLPGSTGACRTA
WDKIIAAQLDARHRPCNFVEHLP
>gnl|CDD|274251 TIGR02668, moaA_archaeal, probable molybdenum cofactor biosynthesis protein A, archaeal. This model describes an archaeal family related, and predicted to be functionally equivalent, to molybdenum cofactor biosynthesis protein A (MoaA) of bacteria (see TIGR02666) [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
LYDRFGRPVTSLRISVTDRCNLSCFYCHMEGEDRSGGNELSPEEIERIVRVASEFGVRKVKITGGEPLLR
KDLIEIIRRIKDYGIKDVSMTTNGILLEKLAKKLKEAGLDRVNVSLDTLDPEKYKKITGRGALDRVIEGI
ESAVDAGLTPVKLNMVVLKGINDNEIPDMVEFAAEGGAILQLIELMPPGEGEKEFKKYHEDIDPIEEELE
KMADRVRTRRMHNRPKYFIPGGVEVEVVKPMDNPVFCAHCTRLRLTSDGKLKTCLLRDDNLVDILDALRN
GEDDELREAFREAVARREPYFK
>gnl|CDD|274252 TIGR02669, stage_II_sporulation_protein_D, SpoIID/LytB domain. This model describes a domain found typically in two or three proteins per genome in Cyanobacteria and Firmicutes, and sporadically in other genomes. One member is SpoIID of Bacillus subtilis. Another in B. subtilis is the C-terminal half of LytB, encoded immediately upstream of an amidase, the autolysin LytC, to which its N-terminus is homologous. Gene neighborhoods are not well conserved for members of this family, as many, such as SpoIID, are monocistronic. One early modelling-based study suggests a DNA-binding role for SpoIID, but the function of this domain is unknown [Unknown function, General]
LAINELPLEDYLKGVVPAEMPASWPMEALKAQAVAARTYALRNLKRFAGDGYDLCADTQCQVYRGVEEET
PRTEQAVEATAGQVLTYNGQLINAVYHSSSGGYTENSEDVWGKDLPYLKSVPDPYQNAAPWSWSLPLKSV
ELFLRFLGVAVGGLYPSKILKRRNSGRVIKLKIRGSGGSVKLIGIGFRRKLGLKSGKDITGRKFRELLGL
NSTNFSVKSRGNAILFTGKGYGHGVGMSQWGANGLAKLGKDYREILKHYYPGTELSR
>gnl|CDD|274253 TIGR02670, Hypothetical_protein_FN1182, CRISPR-associated protein Cas8a1/Csx8, subtype I. In three genomes so far, a member of this protein appears in the midst of a CRISPR-associated (cas) gene operon, immediately upstream of a member of family TIGR01875 (CRISPR-associated autoregulator, DevR family). The genomes so far are Nocardia farcinica IFM10152, Clostridium perfringens SM101, and Clostridium tetani E88
FDTALEASDWRYSATIVGLIYYFKELEKKYEIKKITIYEIEDDYLLYNSEDINEENYLDFVEKFYSDTLH
HKKVENILKHKEFTEEIIKSINEKLSANTVMKKVFGKIKFDGTNKDEILDLIDKNRHSLIKETFRRKKDL
YDNYCNTNRLFEDDNSPCRLKGYCFDPGKKGKSTGYNFVSSTFDYFDDKIFDFIPFAFTGSFEAFFINDN
LDIEILKKSNKAIKEKKNEETEGENNSVPLRKTLFNILQEKVDYIKYDVEVILKNRDKEYFETWYLRNES
IKIFKESDIEDYKKLDFRIKITDKYYFNLLDEVFSAILNLSLLDNSIEYLLKDKNSYSYAINELIKINQL
IRNGGKEMDENLKKAKACAKAVVKKFIKENNKLASYKQKLLSSVVFKDHDRICDILLQLSVYSGVYFSFA
YDLIEDFEQNKDLAYTFINAL
>gnl|CDD|131719 TIGR02671, hypothetical_protein_conserved, CRISPR-associated protein Cas8a2/Csx9, subtype I-A/APERN. Members of this family, so far, are archaeal proteins found in CRISPR-associated (cas) gene regions. So far, this rare cas protein is found in only three genomes: Pyrococcus horikoshii shinkaj OT3, Pyrococcus abyssi GE5, and Thermococcus kodakarensis KOD1. In each case it is found immediately upstream of cas3 in loci that resemble the Apern type but lack Csa1 and Csa4 genes
MSWVVMDAGLEPDPEELADALEGALDSLKSRAMINTSKIGRNDRNSFDRVLSAWFGRSAPETYGELFELV
INETIKLLRSGKIDPAKSLSTIKTDKNGTYLGQAYNGEQAILPAIIKQPEYYEFQSEFLKPTTGQKAQIR
MDPLWFSFMALGFFTSFAGFIRGKYYLMTKPGIEVFWPYEVEEIIEDGILPLTDAGASGRISLDTEELYE
MKLAMKLAEEGRKVIEEVYPVTLHVISLEGQVYTELKTLQLNLKELSNYLAEYVKKIENYRVGGVDLLVE
LKEGGATVEKYPLWALVDIAEKELWKGVSGDREMLAYIFVKDLYRAINSGRKELIEDSIFRLFRQGRALL
EGSGRASGEFRKVMRTFMWEEHLEVLL
>gnl|CDD|131720 TIGR02672, hypothetical_protein_SERP2456, CRISPR type III-A/MTUBE-associated protein Csm6. Members of this family as found in CRISPR-associated (cas) gene regions in Streptococcus thermophilus CNRZ1066, Staphylococcus epidermidis RP62A, and Mycobacterium tuberculosis (strains CDC1551 and H37Rv), as part of Mtube-type CRISPR/Cas systems. CRISPR is a widespread form of direct repeat found in archaea and bacteria, with distinctive subtypes each of which has a characteristic sporadic distribution
ITRLAPNTEVEIIIYTNPSVHRFDLFVPVFRNHLVILSAEYPDREIILNTSSGTPQMQSALVAINVFGIP
NTKAVQVSTPARASNKDIESPNAYDLEEMWDANDDNQPGAPNRCFEANSAAFGAALERANLKQLIVSYDY
SAALTIAADSRLFDNVKNLIRGKLHRSRLEHKVAPKFFKITAFTYDDANKKVLEYYLALALLAKREQWAE
FLISAKSAAEFVLRAAIAKHLPELIYLDDGMPRLNREDKLEREPKIRCALKHPPKSFNVEWYLYLKDWLA
ILRQFEPDSQLALEVNGRFESNGVRNTAAHELVSISEDRNKNITKDGGLLPEQLLKLLARETGIDLTLYN
YLNDENKEQIDM
>gnl|CDD|131721 TIGR02673, cell_division_ATP-binding_protein_FtsE, cell division ATP-binding protein FtsE. This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein [Cellular processes, Cell division]
MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLR
GRQLPLLRRRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSG
GEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIIL
DDGR
>gnl|CDD|131722 TIGR02674, cas_cyan_RAMP_2, CRISPR-associated RAMP protein, Csx10 family. CRISPR is a widespread repeat family in prokaryotes. At least 45 different protein families occur in prokaryotes only when these repeats are present. This family, a minor CRISPR-associated protein family, seems largely restricted to the Cyanobacteria. It belongs to the RAMP superfamily (pfam03787)
MNIIELTITALSPLAIGRQKPGGSIGEAYPYIPGSVLRGAAAAMLLRQGRGIVAVAARGEDAARLFFDGR
TRYFNYAYPVLPATASSSKTNPGFRSEFHGVFDTLIDDFALEVLDAVNDPAETVGFGGRVEDSQGFYSID
DSNERYCSPARRIRLLTRVGINRYRATAVDQILYSYEALNEVTVGPDEKVSGQVFAGWIYVDKDDLAELL
SSLLNHIYRLGGSVSRGYGRVTVAADEPQNIPDIWERIPKFNQPLDARWQDWVTLFGDTLVPDPNTGQYF
TWDLRSALILLESVEIEMLQPIAGEEDQSLELVRAVSRYDYVGGWNRAWGLPKPVELATAGGSVFVFRTR
TSPIWIQTLAGLEWDGIGERRAEGFGQLEVCWQFHQEFIENPV
>gnl|CDD|131723 TIGR02675, Mu-like_prophage_FluMu_protein_gp42, tape measure domain. Proteins containing this domain are strictly bacterial, including bacteriophage and prophage regions of bacterial genomes. Most members are 800 to 1800 amino acids long, making them among the longest predicted proteins of their respective phage genomes, where they are encoded in tail protein regions. This roughly 80-residue domain described here usually begins between residue 100 and 250. Many members are known or predicted to act as phage tail tape measure proteins, a minor tail component that regulates tail length
INDAGAASGASAEEADGALIQLSQMLASGKLRGEEINSLLEALPGALQALAKAMGVTRGELRKMLSDGKL
TADVI
>gnl|CDD|131724 TIGR02677, conserved_hypothetical_protein, TIGR02677 family protein. Members of this protein belong to a conserved gene four-gene neighborhood found sporadically in a phylogenetically broad range of bacteria: Nocardia farcinica, Symbiobacterium thermophilum, and Streptomyces avermitilis (Actinobacteria), Geobacillus kaustophilus (Firmicutes), Azoarcus sp. EbN1 and Ralstonia solanacearum (Betaproteobacteria) [Hypothetical proteins, Conserved]
EAFRHISAENADLYRAIMRSFYAAKERFRTYLRPDDVLAFLRQYLPVADLTELQQALDQLVKWGNLTAIP
ETSRVRTIEEFRRKRFLYQLSRIGEAAEAALRTLEQALGSRGALQTAALDDIVQRLRELLALIDQPRPDA
REVHRTLRELYGSFESLADNAQAFMADLQRHRPLEVADYEAFLAYKDRLIAYLQDFIVRLVDRSEQIAQL
LRVLAESGVDLLLTAAVVREAQDPAPADAEDPSAPDFERWRERWLGLRDWFLGRFGRQPQAEVLRERARA
AIPRLLRVVARLNERRLGRSSRSQDFRDLARWFAECPSDEDAHRLWRVAFGLTPARHLRLDAPDATPPAD
KDPWEEAPPEWVTPRLRVYGEQEPRGRPEKVRDRTEERAELALRARAERARAAQALAELVTDGPVRLSDL
GALDPRVFQLLLGLLGKALTAQGPADGRVAVTTGDGNWSVVLEVLADGPTAELRTADGTFTGPDYLIHIT
KRGG
>gnl|CDD|274254 TIGR02678, hypothetical_protein, TIGR02678 family protein. Members of this protein belong to a conserved gene four-gene neighborhood found sporadically in a phylogenetically broad range of bacteria: Nocardia farcinica, Symbiobacterium thermophilum, and Streptomyces avermitilis (Actinobacteria), Geobacillus kaustophilus (Firmicutes), Azoarcus sp. EbN1 and Ralstonia solanacearum (Betaproteobacteria) [Hypothetical proteins, Conserved]
ALRALLDRPLITQADEPELFRLVRRREDELKAWFDEETGWRLLVERGVARLEKIPAQPEFASGRLPLFSR
RRYVLLCLALAFLERLVPQITLGFLASRVLQRIAAPALYAGELRFDLARRSERRALVAVLKLLEELGVLR
RVDGDEESFVASTEGEVLYEVTRRALRLLLAAPRGPSAVAVPADHDERLAPLTAEEAPGTDARRWRALRH
RLVRRLFDDPVVYRALLANDELAYLTNQRGALTRRIAEITGFLTERRAEGVLLVDPDDPATDVRFPDTGT
TAHVILLLAERLQERSGRWPADADTLGELEAELADERTRHGPGWGKAYRDPSAEAELVTVALSELLRLGL
ARRPDRFDRIWLLPAAARYRGRYPT
>gnl|CDD|274255 TIGR02679, conserved_hypothetical_protein, TIGR02679 family protein. Members of this protein belong to a conserved gene four-gene neighborhood found sporadically in a phylogenetically broad range of bacteria: Nocardia farcinica, Symbiobacterium thermophilum, and Streptomyces avermitilis (Actinobacteria), Geobacillus kaustophilus (Firmicutes), Azoarcus sp. EbN1 and Ralstonia solanacearum (Betaproteobacteria) [Hypothetical proteins, Conserved]
GRLRGRVRLQSLSAEQREALAALLGRDSRRDRSMSVPLADLDAALTRAGFGRGLREALEHLDGPIMDRAE
ERAAAASEWARLFARGRALPPLAELRAWLARVVAGGFVRRLYGADTEAAAALLRDVGAALARLPVSREPL
LVLAAQVLAGDAHALDAGTPVAALVLSALRARAAGQWAVLAHERTRELWARAGLLVDELSSTVLALNLPG
ATEGPAHPVASAASEAGTAAYLTLRQLLRSPGAWTAAGTPGRVYVVENPNVLAIALDRLGPRCAPLVCTD
GQPNAAQIKLLDLLAAAGARLYYHGDFDWPGLRIANGLIRRYGARPWRFSAADYRAAVVGPPHTPRPLAD
RAAVASWDPPLAPAMARHGIAIYEEALADVLLEDL
>gnl|CDD|274256 TIGR02680, conserved_hypothetical_protein, TIGR02680 family protein. Members of this protein family belong to a conserved gene four-gene neighborhood found sporadically in a phylogenetically broad range of bacteria: Nocardia farcinica, Symbiobacterium thermophilum, and Streptomyces avermitilis (Actinobacteria), Geobacillus kaustophilus (Firmicutes), Azoarcus sp. EbN1 and Ralstonia solanacearum (Betaproteobacteria). Proteins in this family average over 1400 amino acids in length [Hypothetical proteins, Conserved]
RWRPHRAGLVNLWYYDEQEFWFRDGRLLLRGNNGAGKSKVLELLLPFLLDGKLRPSRLEPDGDSRKRMAW
NLLLGGVNHDERVGYLWLEFGRVEDDGNEHYLTIGAGLRASASRGTADAWFFTTDARRIGYDLWLLSPAG
IPLTRDRLKEALGDGGEVFDTATDYRRAVDEELFGFLGEERYAALLDLLIQLRQPQLSKKPDEGVLSDAL
TEALPPLDDDELTDVADALEQLDEYRDELERLEALERALRNFLQRYRRYARTMLRRRATRLRSAQTQYDQ
LSRDLGRARDELETAREEERELDARTEALEREADALRTRLEALQGSPAYQDAEELERARADAEALQAAAA
DARQAIREAESRLEEERRRLDEEAGRLDDAERELRAAREQLARAAERAGLSPAHTAEPDAALAAQELQEL
GALDARRQDADRVIAQRSEQVALLRRRDDVADRAEATHAAARARRDELDEEAEQAAARAELADEAVHREG
ARLAWVDAWQAQLRELTILAVDDQPGALADLDSWDALLQGEAPVRVAVYSAVQPLADELTRERAALRLAE
EVLEEERDALRTERERLEQGTDRDPPPPHTRAALRRAGRAGAPLWQLVDFADDVPADVRAGLEAALEAAG
LLDAWVTADGTLQDPDGAVLLHPATVAPGETLADVLRPWLDPPVSAERQPEVDPAAVTRVLEGIACGTAD
AGAAHTWIDVDGRFRLGVLRGAWAKPAAEYIGAAARERARLRRIAELDARLAAVDDELAELARELRALGA
RQRALADELAGAPSDRSLRAAHRRAAEAERQAESAERELARAARKAAAAAAAWKQARRELERDAADLDLP
TDPDALEAVGLALKRFGDHLHTLEVAVRELRHAATRAAEQRARAARAESDAREAAEDAAEARAEAEEASL
RLRTLEESVGAMVDEIRARLAETRAALASGGRELPRLAEALATAEEARGRAEEKRAEADATLDERAEARD
HAIGQLREFALTGLLEDALPDTEVPELDAKWTIEAALKVARRTEAALLQVADDDEALDRAANRISEEYLE
LRRTLAALGDDAQMEPADDGLVVSLVYQGRPVTPAGLLARLEQEIAQRRELLTARERELLENHLQGEIAR
HLQSLILAAERQVAAMNTELAKRPTSTGVRLRLQWKLLPEGTDGAPTGLALRRLLRTDPDLWTEEDREAV
GEFLQQRIERARELDDAGSLLEHLAEALDYRRWHRFTVYYERWQDGQWRPLTHRFGPASGGERALALYVP
LFAAASSHYTQEAYPHAPRLILLDEAFAGVDDNARAHLFGLLRALDLDFVMTSEREWGCYPEVPGLAICQ
LLRPDGVDAVTVSRWTWNGRVRR
>gnl|CDD|131728 TIGR02681, Uncharacterized_protein_HI_1412, phage regulatory protein, rha family. Members of this protein family are found in temperate phage and bacterial prophage regions. Members include the product of the rha gene of the lambdoid phage phi-80, a late operon gene. The presence of this gene interferes with infection of bacterial strains that lack integration host factor (IHF), which regulates the rha gene. It is suggested that pRha is a phage regulatory protein [Mobile and extrachromosomal element functions, Prophage functions]
VFPKVFTKRNQVVTDSLTMAQMFGKRHDNVIRDIKVLLIEANETEFGQLNFEETQYQDEQNKKQPMFNLT
EDGFTIVAMGYTTPKAMKMKEKFIKEFNEMKEHLQKVQ
>gnl|CDD|274257 TIGR02682, hypothetical_protein_MM_3356, CRISPR-associated protein, Csx11 family. Members of this uncommon, sporadically distributed protein family are large (_900 amino acids) and strictly associated, so far, with CRISPR-associated (Cas) gene clusters. Nearby Cas genes always include members of the RAMP superfamily and the six-gene CRISPR-associated RAMP module. Species in which it is found, so far, include three archaea (Methanosarcina mazei, M. barkeri and Methanobacterium thermoautotrophicum) and two bacteria (Thermodesulfovibrio yellowstonii DSM 11347 and Sulfurihydrogenibium azorense)
SGLKRIKNNKDEILLAEIGAYLHLWGKLSPSFINSNSIDKQPNFEYFNENNDCWKSALKNSKIDFRLEVN
SKEFETWDNFIKKWRGHTKKNDLQGLCQILYGASGSLNGGDKKGSPREKVKKQPKEYTWISNAFGYYKEK
IILLRESKNIENLRIQLINNKVQSINGNSHISFEDLRELRKELKELFSGLLGDTRRPINDVSLWDQAYMT
ASLFKSLLVDYILINQIPDRQEVKWRILGIQYNKIGLIEKGFKIASIEWYKQQLKEIDDKLKKLLEVEYP
LGNEIYRDDTGIYFIVPELDKNEDNNLAVLVDDLKLLEEEIINEFEEKITGEVCSVILLTKASRGLMNLS
DLVEPAIENFLYVKTDNKITQKDMQNVNNTSEGIGICPLCRLRLIYDKQKNNSKTRCKTCDERIHHRAKK
WLEKIEKETIWIDEVADKNDRIALISLRFDLKKWLNKDSSSLTEKIIKEPNKEIELLQFLFRKNPSPARL
RRIWETTENFFEEILIEIIDEIPNYRRKRIVFELPYIEGIKDLKEELEGDGLLFWALPSINIDKTDIYLV
SVIHDFIGKFATKDSLKRLNENNLEEEDENNFEDKKIKLKKYEDKENRNTISNLCSLQKSEIKNFVLYYP
YIPITDTPVGFMVIIPAEDALKIIDLIMEKYNKEFKKVYGKLPLHLGIIIAKRKTPLYILLDALRKMLRD
VNNKKKTYQDKWKSCEKYHENYNNYAKPEELCNSTQKYYSIYWDNGDKTTLDFWDPYIRPNENWKKTGSF
FDNEVDDRYIVHVPNLKDNDCLDINTSRFDIFFLKSASDRRAFQLKSNRPYELEEIWDFKDLWDTFSDNL
SNAQIHKLVNIFYDKIEEWKKDEDPNLASSFVNFVELDLANIFGLKEKNDRDKELFNKLNSANIKLLLDI
FELWSKAL
>gnl|CDD|162974 TIGR02683, Uncharacterized_protein_HI_1419, putative addiction module killer protein. Members of this strictly bacterial protein family are small, at roughly 100 amino acids. The gene is almost invariably the upstream member of a gene pair, where the downstream member is a predicted DNA-binding protein from a clade within Pfam helix-turn-helix family pfam01381. These gene pairs, when found on the bacterial chromosome, often are located with prophage regions, but also in both integrated plasmid regions and near housekeeping genes. Analysis suggests that the gene pair may serve as an addiction module
YTIDRTDTFDKWLDGLKDPRAKARILARIDRLALGNFGDVKPVGEGVSELRIDFGPGYRVYFTQRGKVII
LLLCGGDKSTQQKDIKRAKELAKDL
>gnl|CDD|188241 TIGR02684, conserved_hypothetical_protein, probable addiction module antidote protein. Members of this strictly bacterial protein family are small, at roughly 100 amino acids. The gene is almost invariably the downstream member of a gene pair. It is a predicted DNA-binding protein from a clade within Pfam helix-turn-helix family pfam01381. These gene pairs, when found on the bacterial chromosome, are located often with prophage regions, but also both in integrated plasmid regions and in housekeeping gene regions. Analysis suggests that the gene pair may serve as an addiction module [Mobile and extrachromosomal element functions, Other]
KLAEFDPAEYLKTEEAIAEYLAQAFEDGDPAYIAHALGYIARARGMTQLAKKTGLSRESLYKALSGKGNP
TFDTILKVTKALGLKLTAK
>gnl|CDD|131732 TIGR02685, Pteridine_reductase_1, pteridine reductase. Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family
APAAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTLAAELNARRPNSAVTCQADLSNSATLFSR
CEAIIDACFRAFGRCDVLVNNASAFYPTPLLRGDAGEGVGDKKSLEVQVAELFGSNAIAPYFLIKAFAQR
QAGTRAEQRSTNLSIVNLCDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSLLPD
AMPFEVQEDYRRKVPLGQREASAEQIADVVIFLVSPKAKYITGTCIKVDGGLSLTRA
>gnl|CDD|274258 TIGR02686, Multifunctional_conjugation_protein_TraI, conjugative relaxase domain, TrwC/TraI family. This domain is in the N-terminal (relaxase) region of TrwC, a relaxase-helicase that acts in plasmid R388 conjugation. The relaxase domain has DNA cleavage and strand transfer activities. Plasmid transfer protein TraI is also a member of this domain family. Members of this family on bacterial chromosomes typically are found near other genes typical of conjugative plasmids and appear to mark integrated plasmids [Mobile and extrachromosomal element functions, Plasmid functions]
AADYYTDGDNYYLKDSDAGRWLGKGAQELGLSGEVEKKQFEALLEGRLPDGTRLGRIEDRQSKHRPGFDL
TFSAPKSVSILALVGGDPRLIDAHDEAVKFTLEQLEKEAAAARVTQDGEIEFEKTGNLVIALFRHDTSRA
NDPQLHTHAVVANMTRRSDGKWRSLSSDKKGKHGFIEEIYKNQIYLGLLYRAKLANELKELGYQTRVYGK
HGNFEIDGVPEEVIEAFSKRRQQIEEWVAERGWSLAKSRDTAALDTRKKKTVHDREALREEWQQTAKELG
FDP
>gnl|CDD|274259 TIGR02687, conserved_hypothetical_protein, TIGR02687 family protein. Members of this family are uncharacterized proteins sporadically distributed in bacteria and archaea, about 880 amino acids in length. This protein is repeatedly found upstream of another uncharacterized protein of about 470 amino acids in length, modeled by TIGR02688
QRFIPALLKDFAKHRIVFWYDPDGEFLEEIDHLLLENVIKLHLTDNNYLEVKKLLEIKDPEQNFLLYRPD
KEPAHETNWLLDIQLYSSEFRADRISIILSELEIDGLELRDHFQAREKFFGAKERVQALKKLVTKDDREK
ELDLKMLAVFSGSEAPEFKQIVRDLLLKSVDDGENPIWENISRFGLEGNFWELTEQDFGYSAENPTLRDL
FLSLLITDMKRYSDGQLSEYLQYVVRLEAEALVFLKRWRDSRRDSETFEKLSKDIAEELNLEGALDKRDV
QKLLEAETFDTIDQAIIVHLVKFLLAPVDSSGEEAYLSWIDTRRTKHWFSEYEAIYDALEYAAKLFNLSL
RYYDGFKAADAAELFKAYAEELYQFDQLYRKFYYYADKVQEGAILLKSLRDQVEDLYTNWYLGKLGLKWS
KVIESELKRQWKIAGVPSQKDFYKQHVNPILQKDDRKKVFVIISDALRYEAAEELFEQLNKETRFIAELS
SQLGVLPSYTQLGMAALLPHNALAYRDNSGREVLVDGQSSSGLENRNKILQSKKYDGLAFKADDLMRYKR
DEGRELIRDKRVIYIYHNKIDATGDKQSSEENVFEAVEETIVELKKLVKYLINRLNGTNIIVTADHGFLY
QRDPLENADKSDLDAFPESIIKTTKRFILGQGLSPENSLWKGHSAGTAGILDHGPLEFYVPKGILRFHLQ
GGGARFVHGGASPQEIVIPVLTVNHRRNEKAIDKKKHRKVEVSVLNDRKKVVTSKFKVKIFQTEPVTDKM
KPRTLKISLWDIAEKLVSDEKIITFDSESDEPEERQRNVMLTLGNNLENKTYEYWLILEDAAEITDIARI
PFEI
>gnl|CDD|131735 TIGR02688, hypothetical_protein_GSU2105, TIGR02688 family protein. Members of this family are uncharacterized proteins sporadically distributed in bacteria and archaea, about 470 amino acids in length. Several members of this family appear in public databases with annotation as ATP-dependent protease La, despite the lack of similarity to families TIGR00763 (ATP-dependent protease La) or pfam02190 (ATP-dependent protease La (LON) domain). This protein is repeatedly found downstream of another uncharacterized protein of about 880 amino acids in length, described by model TIGR02687 [Hypothetical proteins, Conserved]
VRRVFPGLVVRKDLVYGVKVGANVPSYVLEYLLGKYCATDGELIEEGIQKVRSILAKNYVRPNEAQIIKH
RLVETGVYTVIDKVQVQVDIKKDIYRAEISNLGIKPAEIPSDLVERYPKLLAGGMWGIITLEYEPEEDEG
RPSPVIISSFKPIQASEVDLDYYKEGRKEFTLEEWIDVLIRSIGYEPEGFEARQKLLLLARLLPLVEPNY
NLIELGPKGTGKSYIYNNLSPYVILISGGTITVAKLFYNISTRQIGLVGRWDVVAFDEVATLKFAKPKEL
IGILKNYMESGSFTRGDETKSSDASFVFLGNVPLTSEHMVKNSDLFSPLPEFMRDSAFLDRIHGYLPGWE
IPKIRKEMFSNGYGFVVDYFAEALRELREREYADIVDRHFSLSPNLNTRDVIAVKKTFSGLMKILFPHGT
ITKEEFTECLEPALEGRQRVKDQLHKIDP
>gnl|CDD|131736 TIGR02689, arsenate_reductase, arsenate reductase, glutathione/glutaredoxin type. Members of this protein family represent a novel form of arsenate reductase, using glutathione and glutaredoxin rather than thioredoxin for reducing equivalents as do some homologous arsenate reductases. An example of this type is Synechocystis sp. strain PCC 6803 slr0946, and of latter type (excluded from this model) is Staphylococcus aureus plasmid pI258 ArsC. Both are among the subset of arsenate reductases that belong the the low-molecular-weight protein-tyrosine phosphatase superfamily [Cellular processes, Detoxification]
KKVMFVCKRNSCRSQMAEGFAKTLGAGKIAVTSCGLESSRVHPTAIAVMEEVGIDISGQTSKPLENFNAE
DYDVVISLCGCGVNLPEAWVTREIFEDWQLEDPDGQSLEVFRRVRDEIKERVENLI
>gnl|CDD|274260 TIGR02690, arsenical_resistance_protein_ArsH_putative, arsenical resistance protein ArsH. Members of this protein family occur in arsenate resistance operons that include at least two different types of arsenate reductase. ArsH is not required for arsenate resistance in some systems. This family belongs to the larger family of NADPH-dependent FMN reductases (pfam03358). The function of ArsH is not known [Cellular processes, Detoxification]
MPAQDLHGIDEPALRPLFSATHKPHIPRILLLYGSLRERSYSRLLAEEAARLLGCEGRETRIFDPPGLPL
PDAAHADHPKVRELRQLSEWSEGQVWCSPERHGAITGSQKDQIDWIPLSVGPVRPTQGKTLAVMQVSGGS
QSFNAVNILRRLGRWMRMPTIPNQSSVAKAFDEFDEAGRMKPSDYYDRVVDVMEELTKFTLLTRAYLDYL
VDRYSERKE
>gnl|CDD|131738 TIGR02691, Protein_ArsC, arsenate reductase (thioredoxin). This family describes the well-studied thioredoxin-dependent arsenate reductase of Staphylococcus aureaus plasmid pI258 and other mechanistically similar arsenate reductases. The mechanism involves an intramolecular disulfide bond cascade, and aligned members of this family have four absolutely conserved Cys residues. This group of arsenate reductases belongs to the low-molecular weight protein-tyrosine phosphatase family (pfam01451), as does a group of glutathione/glutaredoxin type arsenate reductases (TIGR02689). At least two other, non-homologous groups of arsenate reductases involved in arsenical resistance are also known. This enzyme reduces arsenate to arsenite, which may be more toxic but which is more easily exported [Cellular processes, Detoxification]
IYFLCTGNSCRSQMAEGWGKKYLGDEWEVYSAGIEAHGLNPNAVKAMKEVGIDISNQTSDLIDLDILNKA
DLVVTLCGDARDKCPATPPHVKREHWGLDDPARAEGTEEEKWAVFRRVRDEIKERVKDF
>gnl|CDD|131739 TIGR02692, putative_tRNA_nucleotidyltransferase, tRNA adenylyltransferase. The enzyme tRNA adenylyltransferase, also called tRNA-nucleotidyltransferase and CCA-adding enzyme, can add or repair the required CCA triplet at the 3'-end of tRNA molecules. Genes encoding tRNA include the CCA tail in some but not all bacteria, and this enzyme may be required for viability. Members of this family represent a distinct clade within the larger family pfam01743 (tRNA nucleotidyltransferase/poly(A) polymerase family protein). The example from Streptomyces coelicolor was shown to act as a CCA-adding enzyme and not as a poly(A) polymerase [Protein synthesis, tRNA and rRNA base modification]
LLARAAVALGELSPLLAPLAAAFAAAGHELYLVGGSVRDALLGRLGHDLDFTTDARPEETLAILRPWADA
VWDTGIAFGTVGAEKDGQQIEITTFRSDSYDGTSRKPEVTFGDTLEGDLIRRDFTVNAMAVRIPADGSLE
FHDPVGGLDDLLAKVLDTPATPEQSFGDDPLRMLRAARFVSQLGFEVAPRVRAAMTEMADQIERISAERV
RVELDKLLLGDHPRAGIDLMVETGLADRVLPEIPALRLEIDEHHQHKDVYEHSLTVLRQAIDLEDDGPDL
VLRWAALLHDIGKPATRRFEPDGRVSFHHHEVVGAKMVRKRMRALKYSKQMVEDVSRLVELHLRFHGYGD
GQWTDSAVRRYVRDAGPLLPRLHKLVRADCTTRNKRKAARLQAAYDDLEERIAELAAQEDLARVRPDLDG
NEIMEILGIKPGPEVGQAWKYLKELRLERGPLEREEAIAELLAWWK
>gnl|CDD|274261 TIGR02693, Arsenite_oxidase_subunit_AioA, arsenite oxidase, large subunit. This model represents the large subunit of an arsenite oxidase complex. The small subunit is a Rieske protein. Homologs to both large and small subunits that score in the gray zone between the set trusted and noise bit score cutoffs for the respective models are found in Aeropyrum pernix K1 and in Sulfolobus tokodaii str. 7. This enzyme acts in energy metabolim by arsenite oxidation, rather than detoxification by reduction of arsenate to arsenite prior to export [Energy metabolism, Electron transport]
RLPIPPANAKKHNVTCHFCIVGCGYHVYTWPINKEGGTDPQQNAFGLDLSEQQQPESDAWYTPSMYNVVK
QRDGRDVNVVIKPDKECVVNSGLGSVRGGRMAETSFSEDRNTQDRLTYPLVWRGDQMQPTSWDDALDLVA
RLTKKIVDEKGEDDIIVSAFDHGGAGGGFENTWGTGKLYFEAMKVKNIRIHNRPAYNSEVHGTREMGVGE
LNNCYEDAELADTIVAVGTNAYETQTNYFLNHWLPNLRGETLGKKKQLFPGEPHEPGRIIIVDPRRTVSV
NAAEQTAADRVLHLAINSGTDLALFNALFTYVADKGWVDRDFIDKSGHLSSFEDAVKGCRMSIAEAARIT
GVSAAQIIKAAEWIGKPKAGGKRRRTMFGYEKGIIWGNDNYRTNGALVNLALATGNIGRPGTGCVRLGGH
QEGYVRPPDAHVGGPAAYVDQLLIGGKGGVHHIWGCDHYKTTLNAQEFRRVYKKRTDMVKDAMSAAPYGD
REEMVNAIVDAINQGGLFAVNVDIYPTKIGEAAHLILPAATSGEMNLTSMNGERRMRLTEKFMDPPGQAM
PDCLIAARLANTMERVYTAEGKVEYAKQFKGFDWKTEEDAFMDGYNKNRDNTVEDEAAHGGENYKFVTYE
LLSAMGTNGFQEPATRFTDGKIEGTQRLYTDGVFSTDDGKARFMDAPWRGLPAPGKQQQKDKHKFWINNG
RANVVWQSAYHDQENDFVMDRFPLPYIEMNPEDAAELGLKEGDLVEVYNDAGATQAMAYPTPTAKPGETF
MLFGFPTGVQGNVTTAGTDELIIPNYKGTWGNIRKI
>gnl|CDD|131741 TIGR02694, Arsenite_oxidase_subunit_AioB, arsenite oxidase, small subunit. This model represents the small subunit of an arsenite oxidase complex. It is a Rieske protein and appears to rely on the Tat (twin-arginine translocation) system to cross the membrane. Although this enzyme could run in the direction of arsenate reduction to arsenite in principle, the relevant biological function is arsenite oxidation for energy metabolism, not arsenic resistance. Homologs to both large (TIGR02693) and small subunits that score in the gray zone between the set trusted and noise bit score cutoffs for the respective models are found in Aeropyrum pernix K1 and in Sulfolobus tokodaii str. 7 [Energy metabolism, Electron transport]
GLEYPANRVANISELKLNEPLDFNYPDASSPGVLLKLGTPVEGGVGPDGDIVAFSTLCTHMGCPVSYSAD
NKTFNCPCHFSVFDPEKGGQQVWGQATQNLPQIVLRVADNGDIFAEGVDGLIYGRLSNV
>gnl|CDD|131742 TIGR02695, Outer_membrane_protein_H.8, azurin. Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see pfam00127). It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The most closely related copper-binding proteins to this family are auracyanins, as in Chloroflexus aurantiacus, which have similar redox activities [Energy metabolism, Electron transport]
CEVTVESNDNMQFNTKSISVPKSCKEFTVNLKHTGKLPKAVMGHNWVLAKSADMQAVAKDGMGAGADNNY
VKPGDARVIAHTKVIGGGEKTSVTFDVSKLSAGEDYTFFCSFPGHWAMMRGTVTL
>gnl|CDD|131743 TIGR02696, polyribonucleotide_nucleotidyltransferase, guanosine pentaphosphate synthetase I/polynucleotide phosphorylase. Sohlberg, et al. present characterization of two proteins from Streptomyces coelicolor. The protein in this family was shown to have poly(A) polymerase activity and may be responsible for polyadenylating RNA in this species. Reference 2 showed that a nearly identical plasmid-encoded protein from Streptomyces antibioticus is a bifunctional enzyme that acts also as a guanosine pentaphosphate synthetase
GVTFAEAVIDNGRFGTRTIRFETGRLARQAAGSVVAYLDDETMLLSATTASKQPKDQFDFFPLTVDVEER
MYAAGRIPGSFFRREGRPSTDAILTCRLIDRPLRPSFVKGLRNEVQVVVTVLSLNPDHLYDVVAINAASA
STQLAGLPFSGPIGGVRVALIDGQWVAFPTHEQLEGAVFDMVVAGRVLENGDVAIMMVEAEATEKTWDLV
KGGAEAPTEEVVAEGLEAAKPFIKVLCRAQADLAEKAAKPTGEFPLFPDYQDDVYEAVEGAVKDELSAAL
TIAGKQEREEALDEVKALVAAKLAEQFEGREKEISAAYRAVTKKLVRERVLTEGVRIDGRGVTDIRPLDA
EVQVIPRVHGSALFERGETQILGVTTLNMLKMEQQIDSLSPETSKRYMHHYNFPPYSTGETGRVGSPKRR
EIGHGALAERALVPVLPSREEFPYAIRQVSEALGSNGSTSMGSVCASTLSLLNAGVPLKAPVAGIAMGLI
SDEVDGETRYVALTDILGAEDAFGDMDFKVAGTSEFVTALQLDTKLDGIPASVLASALKQARDARLAILD
VMAEAIDTPDEMSPYAPRIITVKIPVDKIGEVIGPKGKMINQIQDETGAEISIEDDGTVYIGAADGPSAE
AARAMINAIANPTMPEVGERFLGTVVKTTAFGAFVSLLPGKDGLLHISQIRKLAGGKRVENVEDVLSVGQ
KIQVEIADIDDRGKLSLVP
>gnl|CDD|131744 TIGR02697, hypothetical_protein_WD_0725, Wolbachia palindromic element (WPE) domain. This domain conceptually resembles TIGR01045, the Rickettsial palindromic element (RPE) domain. In both cases, a protein-coding palindromic element spreads through a genome, inserting usually in protein-coding regions. The additional protein coding sequence is thought to allow function of the host protein because of location in surface-exposed regions of the protein structure. Note that this model appears to work better in fragment mode [Mobile and extrachromosomal element functions, Other]
VIPVPRHWDPENLIANERIRQLYNKNWIPVSATGMT
>gnl|CDD|131745 TIGR02698, Uncharacterized_16.5_kDa_protein_in_ptsI_3'region, copper transport repressor, CopY/TcrY family. This family includes metal-fist type transcriptional repressors of copper transport systems such as copYZAB of Enterococcus hirae and tcrYAZB (transferble copper resistance) of an Enterocuccus faecium plasmid. High levels of copper can displace zinc and prevent binding by the repressor, activating efflux by copper resistance transporters. The most closely related proteins excluded by this model are antibiotic resistance regulators including the methicillin resistance regulatory protein MecI [Transport and binding proteins, Cations and iron carrying compounds, Regulatory functions, DNA interactions]
SISDAEWEVMRVVWTLGETTSRDIIRILAEKKDWSDSTIKTLLGRLVDKGCLTTEKEGRKFIYTALVSED
EAVENAAQELFSRICSRKVGAVIADLIEESPLSQTDIEKLEKLLSEKKSTAVEEVPCNCI
>gnl|CDD|131746 TIGR02699, Uncharacterized_protein_MJ0730, archaeoflavoprotein AfpA. The prototypical member of this archaeal protein family is AF1518 from Archaeoglobus fulgidus. This homodimer with two non-covalently bound FMN cofactors can receive electrons from ferredoxin, but not from a number of other electron donors such as NADH or rubredoxin. It can then donate electrons to various reductases [Energy metabolism, Electron transport]
RIAWGITGSGDKLPETYSIMKDVKNRYGDEIDVFLSKAGEQVVKWYKLWDKLENDFPNFRVEINANSPFL
AGQLQMGKYDFLLIAPATANTVAKIAYGIADTLVTNAVIQAAKAKVPVYIMPSDYKEGTVKTALPSGRKL
ELRMRKVDVENVEKLAQMEGIEILTKPEDIYKIF
>gnl|CDD|131747 TIGR02700, Uncharacterized_protein_MJ0208, archaeoflavoprotein, MJ0208 family. This model describes one of two paralogous families of archaealflavoprotein. The other, described by TIGR02699 and typified by the partially characterized AF1518 of Archaeoglobus fulgidus, is a homodimeric FMN-containing flavoprotein that accepts electrons from ferredoxin and can transfer them to various oxidoreductases. The function of this protein family is unknown [Unknown function, General]
RIGWGITGAGHLLVESFQVMKELKREIEELRVSTFVSRAGEEVVRMYGLWDDLREISPGGYYEEVFTESE
EGASSPIIGRFALGKYDLLIVSPATANTVAKIAHGIADSLVTNAVAQAGKGDVPVWVVPVDYEEGIIRTI
TPYMIDRKRCKGCGICVDACPRSAIDMVDGKAFIRLLKCVGCGKCKEACPYNAIHGGLEYEMRVRSVDAE
NVRKLERLEGIEVLRHPEEILERF
>gnl|CDD|274262 TIGR02701, carboxysome_structural_polypeptide, carboxysome shell carbonic anhydrase. This model describes a carboxysome shell protein that proves to be a novel class, designated epsilon, of carbonic anhydrase. It tends to be encoded near genes for RuBisCo and for other carboxysome shell proteins [Central intermediary metabolism, One-carbon metabolism]
HPLTDEEANERLGRYEDSVKGRFDRIIPFLKEIAALQHELDFVERAQRLAQSSLGFTLPEELLEDAWISG
LDMKALFGYCVFQSFTAMSEQFSRKDPLEGQRSAEAISFLLDCGFHAVDISPCADGRLKGLLPYILRLPL
DAVRYRKAYAGAMFDVEADVARWIKTELRRYREGVPNSADEPTRYLKIAVYHFSSSDPTHQGCAAHGSND
RAAAEAALTRLMEFREAIENSFCCGASVDILLIGVDTDTDAIRVHIPDADGFVNLYRYVDNTVLYAETLG
LTADEARQHIAEAIDAANRSDGWAKGNGVPSEGMRRLIAQLLINNLSQIDYVVNRHGGRYPDIGHAERFI
SVGDGFDEVQLRNLAYFAHLDTVEEGAPDVDVGIKIFTGLNVSRGLPIPVAVHFRYDGRVPGSRERAVVK
ARRVKAAIEERYSELDEQGLLQCRLTVQDR
>gnl|CDD|131749 TIGR02702, transcriptional_regulator, iron-sulfur cluster biosynthesis transcriptional regulator SufR. All members of this cyanobacterial protein family are the transcriptional regulator SufR and regulate the SUF system, which makes possible iron-sulfur cluster biosynthesis despite exposure to oxygen. In all cases, the sufR gene is encoded near SUF system genes but in the opposite direction. This DNA-binding protein belongs to the the DeoR family of helix-loop-helix proteins. All members also have a probable metal-binding motif C-X(12)-C-X(13)-C-X(14)-C near the C-terminus [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Regulatory functions, DNA interactions]
STKEDILSYLLKQGQATAAALAEALAISPQAVRRHLKDLETEGLIEYEAVVQGMGRPQYHYQLSRQGREQ
FPQRHGRFAVSLLDSLAETLGPEQFEAVLQKQWQRKAEAYRRQLGQGSLAERLAQLVALRQQEGFMAEVH
PVSDEQKEAFILTEYNCAIASVAESFPTVCGHELEMFAATLPDCAVERTHWLIDGEHRCGYLI
>gnl|CDD|131750 TIGR02703, unidentified_carboxysome_polypeptide, carboxysome peptide A. This model distinguishes one of two closely related paralogs encoded by nearby genes in the carboxysome operons of a number of cyanobacteria and chemoautotrophic bacteria. More distantly related proteins, also belonging to pfam03319, participate in other types of shell such as the ethanolamine degradation organelle [Central intermediary metabolism, One-carbon metabolism]
MKIMQVEKTLVSTNRIADMGHKPLLVVWEKPGGARQVAVDAIGCKPGDWVLCVGSSAAREAAGSKSYPSD
LTIVGIIDHWE
>gnl|CDD|131751 TIGR02704, carboxysome_peptide_B, carboxysome peptide B. This model distinguishes one of two closely related paralogs encoded by nearby genes in the carboxysome operons of a number of cyanobacteria and chemoautotrophic bacteria. More distantly related proteins, also belonging to pfam03319, participate in other types of shell such as the ethanolamine degradation organelle [Central intermediary metabolism, One-carbon metabolism]
MEIMRVMSDLVCTRRIPGLKNASLRVLRDAKGKISVAVDPVGAPEGKWVFTASGSAARFACPDPSILTDL
TIGGIIDHWT
>gnl|CDD|131752 TIGR02705, conserved_hypothetical_protein, nucleoside triphosphatase YtkD. The functional assignment to the proteins of this family is contentious, with papers disagreeing in both interpretation and enzyme assay results. This protein belongs to the nudix family and shares some sequence identity with E. coli MutT but appears not to be functionally interchangeable with it [DNA metabolism, DNA replication, recombination, and repair]
VKFIDYYGNKVTLAFEKEPFSPNPNHVLVIPRYKDQWLLTEHKRRGLEFPGGKVEPGETSKEAAIREVME
ETGAIVKELHYIGQYEVEGESTDFVKDVYFAEVSALESKDDYLETKGPVLLQEIPDIIKADPRFSFIMKD
DVLLKCLERAKHIGFY
>gnl|CDD|162980 TIGR02706, Phosphate_butyryltransferase, phosphate butyryltransferase. Members of this family are phosphate butyryltransferase, also called phosphotransbutyrylase. In general, this enzyme is found in butyrate-producing anaerobic bacteria, encoded next to the gene for butyrate kinase. Together, these two enzymes represent what may be the less common of two pathways for butyrate production from butyryl-CoA. The alternative is transfer of the CoA group to acetate by butyryl-CoA:acetate CoA transferase. Cutoffs for this model are set such that the homolog from Thermotoga maritima, whose activity on butyryl-CoA is only 30 % of its activity with acetyl-CoA, scores in the zone between trusted and noice cutoffs [Energy metabolism, Fermentation]
FEELIEKVKECPMKTVAVAVAQDEPVLEAVKEAKEHGIARAILVGDEEKINEIAKKIGMNLDDVEIVNAP
SPKKAALLAVRLVSTGKADMLMKGLVDTATFLRSVLNKEVGLRTGKVLSHVAVFEVPGFDRLLFLTDAAF
NTYPELKDKVQIINNAVKVAHAIGIDVPKVAPLAAVEVVNPKMPATVDAAALAKMSDRGQIKGCIVDGPL
ALDNAISEEAAKHKGIEGEVAGKADILLVPDIEAGNVLYKTLTYFAKSKNGGILVGTKAPVVLTSRADSF
ETKLNSIALAALVA
>gnl|CDD|162981 TIGR02707, Probable_butyrate_kinase, butyrate kinase. This model represents an enzyme family in which members are designated either butryate kinase or branched-chain carboxylic acid kinase. The EC designation 2.7.2.7 describes an enzyme with relatively broad specificity; gene products whose context suggests a role in metabolism of aliphatic amino acids are likely to act as branched-chain carboxylic acid kinase. The gene typically found adjacent, ptb (phosphate butyryltransferase), likewise encodes an enzyme that may have a broad specificity that includes a role in aliphatic amino acid cabolism [Energy metabolism, Fermentation]
KILVINPGSTSTKLAVFEDERPLFEETLRHSVEELGRFKNVIDQFEFRKQVILQFLEEHGISISKLDAVV
GRGGLLKPIPGGTYLVNEAMLEDLKSGKRGEHASNLGAIIANELADELNIPAYIVDPVVVDEMEDVARIS
GLPEIERKSIFHALNQKAVARRIAKELGKRYEEMNLIVAHMGGGISVAAHRKGRVIDVNNALDGEGPFSP
ERSGTLPLGDLVDLCYSGKYTKEEMKKKIVGNGGLVAYLGTNDAREVEKRIEAGDEKAKLILDAMAYQIA
KEIGKMAVVLKGKVDAIVLTGGLAYSKYFVSEIIKRVSFIAPVLVYPGEDEMEALAEGALRVLRGEEKPK
N
>gnl|CDD|131755 TIGR02708, lactate_oxidase, L-lactate oxidase. Members of this protein oxidize L-lactate to pyruvate, reducing molecular oxygen to hydrogen peroxide. The enzyme is known in Aerococcus viridans, Streptococcus iniae, and some strains of Streptococcus pyogenes where it appears to contribute to virulence [Energy metabolism, Other]
EYKTSSAEGYVDFINTYDLEEMAQQVIPKGAFGYIASGAGDTFTLRENIRAFNHKLIVPHLLQDVENPST
EIEFLGHKLKSPFIMAPVAAHKLANEQGEVATARGVSEFGSIYTTSSYSTADLPEISEALNGTPHWFQFY
MSKDDGINRDIMDRVKADGAKAIVLTADATVGGNREVDVRNGFVFPVGMPIVQEYLPTGAGKSMDNVYKS
AKQKLSPRDIEEIAGYSGLPVYVKGPQCPEDADRALKAGASGIWVTNHGGRQLDGGPAAFDSLQEVAEAV
DKRVPIVFDSGVRRGQHVFKALASGADLVALGRPVIYGLALGGSQGARQVFEYLNKELKRVMQLTGTQTI
EDVKGFDLRHNPYGYEY
>gnl|CDD|131756 TIGR02709, branched-chain_phosphotransacylase, branched-chain phosphotransacylase. This model distinguishes branched-chain phosphotransacylases like that of Enterococcus faecalis from closely related subfamilies of phosphate butyryltransferase (EC 2.3.1.19) (TIGR02706) and phosphate acetyltransferase (EC 2.3.1.8) (TIGR00651). Members of this family and of TIGR02706 show considerable crossreactivity, and the occurrence of a member of either family near an apparent leucine dehydrogenase will suggest activity on branched chain-acyl-CoA compounds [Energy metabolism, Amino acids and amines]
ITVSIAGGSQPEILQLVKKALKEAEQPLQFIVFDTNENLDTENLWKYVHCSDEAAVAQEAVSLVATGQAQ
ILLKGIIQTHTLLKEMLKSEHQLKNKPILSHVAMVELPAGKTFLLTDCAMNIAPTQATLIEIVENAKEVA
QKLGLHHPKIALLSAAENFNPKMPSSVLAKEVTAHFNDQQEATVFGPLSLDLATSEEAVAHKRYSGPIMG
DADILVVPTIDVGNCLYKSLTLFGHAKVGGTIVGTKVPVVLTSRSDSTESKFHSLRFAMRQ
>gnl|CDD|274263 TIGR02710, conserved_hypothetical_protein, CRISPR-associated protein, TIGR02710 family. Members of this family are found, exclusively in the vicinity of CRISPR repeats and other CRISPR-associated (cas) genes, in Methanothermobacter thermautotrophicus (Archaea), Thermus thermophilus (Deinococcus-Thermus), Chloroflexus aurantiacus (Chloroflexi), and Thermomicrobium roseum (Thermomicrobia)
HPLAQAIAEKRPDKVVFLGSKKTVEFIAEEAEAQGKDPPEYKTIELEDIDQLYRGYQELFEAFEDLMRYG
DQEILADLTGGTKPMTAGLVLAAILYGELSVYTGFRDRQGRVIPGTERLIEPSDPYNVEGNTEQGYARRA
INAFDYLFAHARLETLLRRLLSAVNHTFYEAMIKLTRAYLHWDRFEHEEALDYLNDPLPERLALYQVTSH
DELEDVIKRNASILPEIIGSRNGRREAKRRPFLPLLGDLLANAERRATQGRYDDAAARLYRALELIVQIR
LEERGKYGLDTDSINPDGLPESTRAALKLDGKKSHLALKNAYDLLECEGDDAGRLFGEDNRILQLLQIRN
HSILAHGFRPVTEEQYREFYDKVLELARMI
>gnl|CDD|131758 TIGR02711, Cation/acetate_symporter_ActP, cation/acetate symporter ActP. Members of this family belong to the Sodium:solute symporter family. Both members of this family and other close homologs tend to be encoded next to a member of pfam04341, a set of uncharacterized membrane proteins. The characterized member from E. coli is encoded near and cotranscribed with the acetyl coenzyme A synthetase (acs) gene. Proximity to an acs gene was used as one criterion for determining the trusted cutoff for this model. Closely related proteins may differ in function and are excluded by the high cutoffs of this model; members of the family of phenylacetic acid transporter PhaJ can score as high as 1011 bits [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
KRVLLLLLATLPFLAWAADAISGAVERQPLNIQAIIMFLLFVGFTLYITYWASKKTRSRSDYYTAGGNIT
GFQNGLAIAGDYMSAASFLGISALVYTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRL
KQRPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHVAVVLVGILMVMYVLFGGMLATTWVQIIK
AVLLLFGATFMAFMVMKSVGFSFNTLFKEAMAVHPKGVAIMSPGGLVSDPISALSLGLGLMFGTAGLPHI
LMRFFTVSDAKEARKSVFYATGFMGYFYILTFIIGFGAILLVSANPEFKDATGALIGGNNMAAVHLANAV
GGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVIKKGKATERDELRVSKITVLILGVIAIGLG
ILFENQNIAFMVGLAFSIAASCNFPIILLSMYWSKLTTRGAMIGGWLGLITAVVLMILGPTIWVQILGHE
KPIYPYEYPALFSMIVAFIGIWFFSITDNSETGAQERELFRAQFIRSQTGLGASQGRAH
>gnl|CDD|274264 TIGR02712, Includes:_Allophanate_hydrolase, urea carboxylase. Members of this family are ATP-dependent urea carboxylase, including characterized members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae. The allophanate hydrolase domain of the yeast enzyme is not included in this model and is represented by an adjacent gene in Oleomonas sagaranensis. The fusion of urea carboxylase and allophanate hydrolase is designated urea amidolyase. The enzyme from Oleomonas sagaranensis was shown to be highly active on acetamide and formamide as well as urea [Central intermediary metabolism, Nitrogen metabolism]
FDTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAK
KTGAQAIHPGYGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPGTGLLSSLD
EALEAAKEIGYPVMLKSTAGGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQ
IFGDGKGKVVALGERDCSLQRRNQKVVEETPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEAR
DEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELPDFASLNISLTPRGAAIEARVYAENPAKNFQ
PSPGLLTDVQFPDDVRVDTWVETGTEVSPEYDPMLAKIIVHGSDREDAILKLHQALAETRVYGIETNLDY
LRSILSSETFRSAQVSTRTLNSFVYTPPAIEVLSPGAQTTVQDYPGRTGYWDVGVPPSGPMDSYSFRLAN
RIVGNDEGAAGLEITLTGPTLRFHSDAVIAITGAPAPATLDGQPVPQWKPITVKAGSTLSIGKIAGSGCR
TYLAIRGGIDVPDYLGSRSTFTLGQFGGHAGRALKTGDVLHIGEPELHEASIPAPIPAAPIPPYGSEWRI
GVLYGPHGAPDFFTEEDIEEFFSAEWKVHYNSNRTGVRLIGPKPKWARSDGGEAGLHPSNIHDNVYAIGA
IDFTGDMPVILGPDGPSLGGFVCPAVVAEAELWKVGQLKPGDTVRFVPISEDSARALKDAQDVAISNLDS
LSLLSLPDSLALPSYEDPGVLARVPADGDSPKVVYRQAGDRYLLVEYGENVLDIALRYRIHLLMEALQKA
KLPGIIDLTPGIRSLQIHYDPRVISQSELLEVLVAIEEQLPAAEDLQVPSRIVHLPLSWEDPATLLAVER
YMETVRSDAPWCPSNIEFIRRVNGLSSRDDVRDTVFDASYLVLGLGDVYLGAPVATPLDPRHRLLTTKYN
PARTWTPENAVGIGGAYMCIYGMEGPGGYQLVGRTIQIWNRYRLGGAFQDGPWLLRFFDQIRFYPVSEEE
LLELREEFDNGRFKVRVEETVFDLAEYQRFLADNADSIEAFKERQQGAFEAERARWIASGNADLAEEVTE
APEEEADLPEGAEQVESEYAGNFWKVLVEVGDRVEAGQPLVILEAMKMEMPVSAPVAGKVTKILCQPGDM
VDAGDIVAVLE
>gnl|CDD|274265 TIGR02713, Allophanate_hydrolase, allophanate hydrolase. Allophanate hydrolase catalyzes the second reaction in an ATP-dependent two-step degradation of urea to ammonia and C02, following the action of the biotin-containing urea carboxylase. The yeast enzyme, a fusion of allophanate hydrolase to urea carboxylase, is designated urea amidolyase [Central intermediary metabolism, Nitrogen metabolism]
DEAWISLLSEEDLLAQAAALDARDARPERLPLYGVPFAVKDNIDVAGLPTTAACPAFAYTPEEDATVVAL
LRAAGAIVVGKTNLDQFATGLVGTRSPYGAVRNAFDPAYISGGSSSGSAVAVARGLVPFALGTDTAGSGR
VPAALNNIVGLKPTKGLVSTTGVVPACRSLDCVSIFALTVADAEQVLRIAAAPDARDPYSRPLPAAALRR
FPPPPRVGVPRAAQLEFFGDSQAEAAFAAAVERLEALGVEVVEIDFAPFLETAALLYEGPWVAERYAAVG
EFVEAQPDALDPVVRGIITSATRFSAADAFAAQYRLAALRRKAEALLAGVDVLLVPTAPTHPTIEEVLAD
PVGLNSRLGTYTNFVNLLDLCAVAVPAGFRSDGLPFGVTLIGPAFHDAALASLGRRLQAASALPLGATGE
SLPAALAEAATAAPRVVRLAVVGAHLSGMPLNWQLTERGARLLRTTRTAPDYRLYALAGTPPPKPGLVRV
APGGGAAIEVEVWELPAEAFGRFVAAIPAPLGIGTVTLADGSWVKGFICEPAALEGARDITAFGGWRAYL
A
>gnl|CDD|274266 TIGR02714, Cyanuric_acid_amidohydrolase, ring-opening amidohydrolases. Members of this family are are ring-opening amidohydrolases, including cyanuric acid amidohydrolase (EC 3.5.2.15) (AtzD and TrzD) and barbiturase. Note that barbiturase does not act as defined for EC 3.5.2.1 (barbiturate + water = malonate + urea) but rather catalyzes the ring-opening of barbituric acid to ureidomalonic acid (see Soong, et al., )
IDVFRVPCHSPGDTSGLAKLIDTGVVAAADVVAVMGKTEGNGCVNDYTREYATAAFAACLSRKLQLSPHE
VEERVAFVMSGGTEGVLSPHHTIFARRPADDAHTKPAGKRLTVGIAFTRDFLPEEIGRHAQITETAGAVK
RAMRDAGIADIDDVHFVQVKCPLLTPAKIADARSRGCTVVTEDTYESMGYSRGASALGIALALGEVPSSM
LVDESVLNDWSLSSSVASASAGIELEHNVIIVIGNSRQAGGELVIGHGVMKDAIDAASVRRAIRDLGIRS
DDRPHSDELDRIVNVFAKAEASPDGVVRGRRHTMLDDSDINSTRHARAVVGAVIASVVGDPMVYVSGGAE
HQGPAGGGPVAVIARA
>gnl|CDD|274267 TIGR02715, Glu-tRNAGln_amidotransferase_A_subunit, amidohydrolase, AtzE family. Members of this protein family are aminohydrolases related to, but distinct from, glutamyl-tRNA(Gln) amidotransferase subunit A. The best characterized member is the biuret hydrolase of Pseudomonas sp. ADP, which hydrolyzes ammonia from the three-nitrogen compound biuret to yield allophanate. Allophanate is also an intermediate in urea degradation by the urea carboxylase/allophanate hydrolase pathway, an alternative to urease [Unknown function, Enzymes of unknown specificity]
SIVEIAGAIRSGRVSARAVAEATLARINQADGGLNAFTAVTAERALADAARIDADLAAGSPLGPLAGVPF
AVKNLFDVAGLTTLAGAKINRDLAPAKRDATLVQRLSAAGAVLVGALNMDEFAYGFTTENAHYGPTRNPH
DLTRIAGGSSGGSAAAVAAGLVPFSLGSDTNGSIRVPASLCGVFGLKPTYGRLSRQGVFPFVASLDHVGP
FARSVEDLALAYDVMQGPDPQDPFCTDRPAEPTVPLLPAGISGLRIAVLGGWFQQNADPEALAAVGRVAK
ALGATTIVELPDAERARAAAFVITASEGGNLHLDALRTRPQDFDPATRDRLLAGALLPASWYAQAQRFRH
WFRDAIRELFQRVDVLIAPATPCSAPLIGQETMIIDGVPVPVRANLGIFTQPISFAGLPVLAAPLPRPGR
LPIGVQLIAAPWREDLCLRAAAVLERQGVVAA
>gnl|CDD|131763 TIGR02716, C-20_methyltransferase, C-20 methyltransferase BchU. Members of this protein family are the S-adenosylmethionine-depenedent C-20 methyltransferase BchU, part of the pathway of bacteriochlorophyll c production in photosynthetic green sulfur bacteria. The position modified by this enzyme represents the difference between bacteriochlorophylls c and d; strains lacking this protein can only produced bacteriochlorophyll d [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
LIEFSCMKAAIELDLFSHMAEGPKDLATLAADTGSVPPRLEMLLETLRQMRVINLEDGKWSLTEFADYMF
SPTPKEPNLHQTPVAKAMAFLADDFYMGLSQAVRGQKNFKGQVPYPPVTREDNLYFEEIHRSNAKFAIQL
LLEEAKLDGVKKMIDVGGGIGDISAAMLKHFPELDSTILNLPGAIDLVNENAAEKGVADRMRGIAVDIYK
ESYPEADAVLFCRILYSANEQLSTIMCKKAFDAMRSGGRLLILDMVIDDPENPNFDYLSHYILGAGMPFS
VLGFKEQARYKEILESLGYKDVTMVR
>gnl|CDD|131764 TIGR02717, Uncharacterized_protein_MJ0590, acetyl coenzyme A synthetase (ADP forming), alpha domain. Although technically reversible, it is believed that this group of ADP-dependent acetyl-CoA synthetases (ACS) act in the direction of acetate and ATP production in the organisms in which it has been characterized. In most species this protein exists as a fused alpha-beta domain polypeptide. In Pyrococcus and related species, however the domains exist as separate polypeptides. This model represents the alpha (N-terminal) domain. In Pyrococcus and related species there appears to have been the development of a paralogous family such that four other proteins are close relatives. In reference, one of these (along with its beta-domain partner) was characterized as ACS-II showing specificity for phenylacetyl-CoA. This model has been constructed to exclude these non-ACS-I paralogs. This may result in new, authentic ACS-I sequences falling below the trusted cutoff
LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVI
VVPAKYVPQVVEECGEKGVKGAVVITAGFKEVGEEGAELEQELVEIARKYGMRLLGPNCLGIINTHIKLN
ATFAPTMPKKGGIAFISQSGALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLY
LEGIKDGRKFLKTAREISKKKPIVVLKSGTSEAGAKAASSHTGALAGSDEAYDAAFKQAGVIRADSIEEL
FDLARLLSNQPLPKGNRVAIITNAGGPGVIATDACEENGLELAELSEATKNKLRNILPPEASIKNPVDVL
GDATPERYAKALKTVAEDENVDGVVVVLTPTAMTDPEEVAKGIIEGAKKSNEKPVVAGFMGGKSVDPAKR
ILEENGIPNYTFPERAVKALSALYRYA
>gnl|CDD|131765 TIGR02718, Probable_transporter., siderophore transporter, RhtX/FptX family. RhtX from Sinorhizobium meliloti 2011 and FptX from Pseudomonas aeruginosa appear to be single polypeptide transporters, from the major facilitator family (see pfam07690) for import of siderophores as a means to import iron. This function was suggested by proximity to siderophore biosynthesis genes and then confirmed by study of knockout and heterologous expression phenotypes [Transport and binding proteins, Cations and iron carrying compounds]
RLVITLGLLYLSQGIPIGLAMDALPTLLREDGAPLTALAFLPLVGLPWVVKFLWAPLVDNWWSWRLGRRR
SWVLPMQCLVSACLASLALVGPDVAGAGWAVGLLACASLASATQDIATDGMAAEHFNGRTLAKGNAVQIA
GVMIGFFGGGAGTLVLFGKFGQRPAFLLVACVPLASLVCVLWLKDRAVASPEAPLARRASLFRFFRRPLA
WSLLALALLSAMTAVSGFGLSKLYLVDAGWPLEWIGRLGMAGGAVTVLLGCGGGAWLVRRAGLWRTFILG
VGLAGSLALLWFAQAAFWLAPGIAVAWSCSAFGSLITGITSVAIYTAFMRFAGDGDQAGTDVTAVQSTRD
LGELIASSIAGYLTDRFGYAGGFLSGTVLAVLAILLAVRL
>gnl|CDD|131766 TIGR02719, transcriptional_regulator_PadR_family, poly-beta-hydroxybutyrate-responsive repressor. Members of this family are transcriptional regulatory proteins found in the vicinity of poly-beta-hydroxybutyrate (PHB) operons in several species of Bacillus. This protein appears to have repressor activity modulated by PHB itself. This protein belongs to the larger PadR family (see pfam03551) [Regulatory functions, DNA interactions]
NEKDNRESLENNLAKQINGAPKNFLVPFLLLCLKDWNLHGYKLIQMLMDFGFSSVDQGNVYRTLRKLEKD
NLISSQWDTSAEGPAKRIYSLTDAGEQYLSMCANSFEHYQNMLDSFFHLYTDAFFPFSSSPEKDEKDS
>gnl|CDD|213733 TIGR02720, Pyruvate_oxidase, pyruvate oxidase. Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name [Energy metabolism, Aerobic]
ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGS
AGPGATHLLNGLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDE
AIRRAYAHNGVAVVTIPVDFGWQEIPDNDYYASSVSYQTPLLPAPDVEAVTRAVQTLKAAERPVIYYGIG
ARKAGEELEALSEKLKIPLISTGLAKGIIEDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYPFAEV
SKAFKNTKYFIQIDIDPAKLGKRHHTDIAVLADAKKALAAILAQVEPRESTPWWQANVANVKNWRAYLAS
LEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKNKWITSNLFATMGVGVPGAIAA
KLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTNQPLIGVDFNDADFA
KIAEGVGAVGFRVNKIEQLPAVFEQAKAIKQGKPVLIDAKITGDRPLPVEKLRLDPALSSAADIEAFKEK
YEAQELKPLSTYLKQ
>gnl|CDD|274268 TIGR02721, Thiamine_kinase, thiamine kinase. Members of this family are the ycfN gene product of Escherichia coli, now identified as the salvage enzyme thiamine kinase (thiK), and additional proteobacterial homologs taken to be orthologs with equivalent function [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
VQTLSGGLTNRSWRIEHPGISFVWRPQSPVCKALGVDRQREYQILQALSALGLAPKPILVNEHWLLVEWL
EGEVITLDQFVALDLLLELAALLHQLHSQPRFGYPLSLKARIAHYWLQIDPARRTPEWLRLYKQFRSAPE
PAPLPLAPLHMDVHAYNLVVTPQGLKLIDWEYASDGDIALELAAIIRANDEEQQQDFVQRYCQRRRIYSI
SVLWRQVKAWQPWVDYMAALWFELRWQQTGDPQFLELAQELRHRLC
>gnl|CDD|274269 TIGR02722, Penicillin-binding_protein_activator_LpoB, uncharacterized proteobacterial lipoprotein. Members of this protein family are restricted to the Proteobacteria, and all are predicted lipoproteins. In genomes that contain the thiK gene for the salvage enzyme thiamin kinase, the member of this family is encoded nearby [Cell envelope, Other]
KKYKIIFVALLALLLSGCVSQRAYTDPTDPDVEPVTPGFSSTDLEPIANTMPQSMLSSPAVAQITPGTRP
ILLVDSIKNDTNEHIDTESLTDKIRTALLQSGKFVLTDAQALDRMREQLGYQAESGLVNQSTAIKKGRLV
GADYSLYGKISSIVKSDGSRKLVYYKFTMQLMDLKTGLIVWSDEKPIRK
>gnl|CDD|131770 TIGR02723, alpha_subunit_of_phenylphosphate_carboxylase, phenylphosphate carboxylase, alpha subunit. Members of this protein family are the alpha subunit of phenylphosphate carboxylase. Phenol (methyl-benzene) is converted to phenylphosphate, then para-carboxylated by this four-subunit enzyme, with the release of phosphate, to 4-hydroxybenzoate. The enzyme contains neither biotin nor thiamin pyrophosphate. This alpha subunit is homologous to the beta subunit and, more broadly, to UbiD family decarboxylases [Energy metabolism, Anaerobic]
MAKISAPKNNREFIEACVKSGDAVRIRQEVDWDNEAGAIVRRACELAEAAPFMENIKDYPGFSYFGAPLS
TYRRMAISLGMDPASTLPQIGAEYLKRTNSEPIAPVIIDKRDAPCKENILLGADVDLTKLPVPLVHDGDG
GRYVGTWHAVITKHPVRGDVNWGMYRQMMWDGRTMSGAVFPFSDLGKALTDYYLPRGEGCPFATAIGLSP
LAAMAACAPSPIPEPELCGMLAGEAVRLVKCETNDLEVPADAEIIIEGMILPDYKVEEGPFGEYTGYRTS
PRDFRVTFRVDAITYRNNATMTISNMGVPQDEGQLLRSFSLGLELEKLLKSQGIPVTGVYMHPRSTHHMM
IVGVKPTYAGIAMQIAQLAFGSKLGPWFHMVMVVDDQTDIFNWDEVYHAFCTRCNPERGIHVFKNTTGTA
LYPHATPHDRKYSIGSQVLFDCLWPVDWDKTNDVPSLVSFKKVYPKDIQDKVTNNWTDYGFKPVK
>gnl|CDD|131771 TIGR02724, beta_subunit_of_phenylphosphate_carboxylase, phenylphosphate carboxylase, beta subunit. Members of this protein family are the beta subunit of phenylphosphate carboxylase. Phenol (methyl-benzene) is converted to phenylphosphate, then para-carboxylated by this four-subunit enzyme, with the release of phosphate, to 4-hydroxybenzoate. The enzyme contains neither biotin nor thiamin pyrophosphate. This beta subunit is homologous to the alpha subunit and, more broadly, to UbiD family decarboxylases
MDLRYFINQCAEAHELKRITTEVDWNLEISHVSKLTEEKKGPALLFESIKGYDTPVFTGAFATTKRLAIM
LGLPHHLSLCESAQQWMKKTITSEGLIKAKEVKDGPVLENVLSGDKVDLNMFPVPKFFPLDGGRYIGTMV
SVVLRDPETGEVNLGTYRMQMLDDKRCGVQILPGKRGERIMKKYAKLGKKMPAAAIIGCDPLIFMAGTLM
HKGASDFDITGTVRGQQAEFLMAPLTGLPVPAGAEIVLEGEIDPNAFLPEGPFAEYTGYYTDELHKPIPK
PVLEVQQILHRNNPILWATGQGRPVTDVHMLLAFTRTATLWTELEQMRIPGIQSVCVLPESTGRFWSVVS
LKQAYPGHSRQVADAVIASNTGSYGMKGIITVDEDIAADDLQRVFWALSCRYDPARGTELIKRGRSTPLD
PALDPDGDKLTTSRILMDACIPYEWKQKPVEARMDEEMLAKIRARWHEYGID
>gnl|CDD|131772 TIGR02725, Phenylphosphate_carboxylase_delta_subunit, phenylphosphate carboxylase, gamma subunit. Members of this protein family are the gamma subunit of phenylphosphate carboxylase. Phenol (methyl-benzene) is converted to phenylphosphate, then para-carboxylated by this four-subunit enzyme, with the release of phosphate, to 4-hydroxybenzoate. The enzyme contains neither biotin nor thiamin pyrophosphate. The gamma subunit has no known homologs
MNQWEVFVMDLAELPEGKELELSVRTLNPGLKKYTYQRVKAELSNALDKFPDQLQVRFGRGQLCPQQFSI
RIIEQVQRMPAKYL
>gnl|CDD|131773 TIGR02726, Phenylphosphate_carboxylase_gamma_subunit, phenylphosphate carboxylase, delta subunit. Members of this protein family are the alpha subunit of phenylphosphate carboxylase. Phenol (methyl-benzene) is converted to phenylphosphate, then para-carboxylated by this four-subunit enzyme, with the release of phosphate, to 4-hydroxybenzoate. The enzyme contains neither biotin nor thiamin pyrophosphate. This delta subunit belongs to HAD family hydrolases [Energy metabolism, Anaerobic]
MEQAKNIKLVILDVDGVMTDGRIVINDEGIESRNFDIKDGMGVIVLQLCGIDVAIITSKKSGAVRHRAEE
LKIKRFHEGIKKKTEPYAQMLEEMNISDAEVCYVGDDLVDLSMMKRVGLAVAVGDAVADVKEAAAYVTTA
RGGHGAVREVAELILKAQGKWDAMLAKIH
>gnl|CDD|274270 TIGR02727, Uncharacterized_protein_YqgN, 5,10-methenyltetrahydrofolate synthetase. This enzyme, 5,10-methenyltetrahydrofolate synthetase, is also called 5-formyltetrahydrofolate cycloligase. Function of bacterial proteins in this family was inferred originally from the known activity of eukaryotic homologs. Recently, activity was shown explicitly for the member from Mycoplasma pneumonia. Members of this family from alpha- and gamma-proteobacteria, designated ygfA, are often found in an operon with 6S structural RNA, and show a similar pattern of high expression during stationary phase. The function may be to deplete folate to slow 1-carbon biosynthetic metabolism [Central intermediary metabolism, One-carbon metabolism]
KKELRKKLLEARKALSSEERKAASSAIAKRLLALIEWKNAKTIALYLPLRGEVDTRPLIEQLLKEGKRVA
LPKVDPDGKEMLFFRIWSPEQLLTKGPFGILEPVGDLEEPVPPDEIDLIIVPGVAFDRRGYRLGYGGGYY
DRFLARLKGITIGLAFDFQLVDELPREPHDVPVDAIITE
>gnl|CDD|131775 TIGR02728, Spore_coat_protein_GerQ, spore coat protein GerQ. Members of this protein family are the spore coat protein GerQ of endospore-forming Firmicutes (low GC Gram-positive bacteria). This protein is cross-linked by a spore coat-associated transglutaminase [Cellular processes, Sporulation and germination]
LPVEQSYIENILRMNRGKTATVYMTFENSPEWAARVFRGQIENAGRDHIVISDPQSGMRYLLLMVYLDYL
TFDEEIRYPYPY
>gnl|CDD|274271 TIGR02729, Obg_CgtA, Obg family GTPase CgtA. This model describes a univeral, mostly one-gene-per-genome GTP-binding protein that associates with ribosomal subunits and appears to play a role in ribosomal RNA maturation. This GTPase, related to the nucleolar protein Obg, is designated CgtA in bacteria. Mutations in this gene are pleiotropic, but it appears that effects on cellular functions such as chromosome partition may be secondary to the effect on ribosome structure. Recent work done in Vibrio cholerae shows an essential role in the stringent response, in which RelA-dependent ability to synthesize the alarmone ppGpp is required for deletion of this GTPase to be lethal [Protein synthesis, Other]
FVDEAKIFVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGSVILEADENLNTLLDFRYQRHFKAENGEN
GMGKNRTGKSGEDLVIKVPVGTVVYDADTGELLADLTEPGQRFLVAKGGRGGLGNAHFKSSTNRAPRFAT
PGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIA
DIPGLIEGASEGAGLGHRFLKHIERTRVLLHLIDISPEDGSDPVEDYEIIRNELKKYSPELAEKPRIVVL
NKIDLLDEEELEELLKELKKELGKPVFPISALTGEGLDELLDALAELL
>gnl|CDD|131777 TIGR02730, Carotenoid_isomerase, carotene isomerase. Members of this family, including sll0033 (crtH) of Synechocystis sp. PCC 6803, catalyze a cis-trans isomerization of carotenes to the all-trans lycopene, a reaction that can also occur non-enzymatically in light through photoisomerization [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
YDAIVIGSGIGGLVTATQLAVKGAKVLVLERYLIPGGSAGYFEREGYRFDVGASMIFGFGDKGTTNLLTR
ALAAVGRKLETIPDPVQIHYHLPNGLNVKVHREYDDFIQELVAKFPHEKEGIRRFYDECWQVFNCLNSME
LLSLEEPRYLFRVFFKHPLACLGLAKYLPQNAGDIARRYIRDPGLLKFIDIECFCWSVVPADQTPMINAG
MVFSDRHYGGINYPKGGVGQIAESLVKGLEKHGGQIRYRARVTKIILENGKAVGVKLADGEKIYAKRIVS
NATRWDTFGKLLKAENLPKKEKNWQRNYVKSPSFLSLHLGVKADVLPPGTECHHILLEDWTNLEKPQGTI
FVSIPTLLDPSLAPEGHHIIHTFTPSSMEDWQGLSPKDYEAKKEADAERIIDRLEKIFPGLDSAIDYKEV
GTPRTHRRFLGRDSGTYGPIPRRTLPGLLPMPFNRTAIPGLYCVGDSCFPGQGLNAVAFSGFACAHRVAA
DLG
>gnl|CDD|131778 TIGR02731, Phytoene_dehydrogenase_chloroplastic/chromoplastic, phytoene desaturase. Plants and cyanobacteria (and, supposedly, Chlorobium tepidum) have a conserved pathway from two molecules geranylgeranyl-PP to one of all-trans-lycopene. Members of this family are the enzyme pytoene desaturase (also called phytoene dehydrogenase). This model does not include the region of the chloroplast transit peptide in plants. A closely related family, excluded by this model, is zeta-carotene desaturase, another enzyme in the same pathway [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
RVAIAGAGLAGLSCAKYLADAGHTPIVLEARDVLGGKVAAWKDEDGDWYETGLHIFFGAYPNMLQLLKEL
NIEDRLQWKSHSMIFNQPDKPGTFSRFDFPDIPAPFNGVAAILRNNDMLTWPEKIKFAIGLLPAIVRGQK
YVEEQDKYTVTEWLRKQGVPERVNDEVFIAMSKALNFINPDELSMTVVLTALNRFLQERHGSKMAFLDGA
PPERLCQPIVDYITSRGGEVRLNSRLKEIVLNEDGSVKHFVLADGEGQRRFEVTADAYVSAMPVDIFKLL
LPQPWKQMPFFQKLNGLEGVPVINVHIWFDRKLTTVDHLLFSRSPLLSVYADMSETCKEYADPDKSMLEL
VFAPAADWIGRSDEEIIDATMAELAKLFPNHIKADSPAKILKYKVVKTPRSVYKTTPGRQQYRPHQKTPI
PNFFLAGDYTKQKYLASMEGAVLSGKLCAQAIV
>gnl|CDD|131779 TIGR02732, Zeta-carotene_desaturase, 9,9'-di-cis-zeta-carotene desaturase. Carotene 7,8-desaturase, also called zeta-carotene desaturase, catalyzes multiple steps in the pathway from geranylgeranyl-PP to all-trans-lycopene in plants and cyanobacteria. A similar enzyme and pathway is found in the green sulfur bacterium Chlorobium tepidum
KVAIVGAGLAGLSTAVELVDAGHEVDIYESRSFIGGKVGSWVDGDGNHIEMGLHVFFGCYANLFRLMKKV
GAEDNLLLKEHTHTFVNKGGDIGELDFRFATGAPFNGLKAFFTTSQLKWVDKLRNALALGTSPIVRGLVD
YDGAMKTIRDLDKISFAEWFLSHGGSLGSIKRMWDPIAYALGFIDCENISARCMLTIFMLFAAKTEASKL
RMLKGSPDKYLTKPILEYIEARGGKFHLRHKVREIKYEKSSDGSTRVTGLIMSKPEGKKVIKADAYVAAC
DVPGIKRLLPQEWRQFEEFDNIYKLDAVPVATVQLRYDGWVTELQDLAKRKQLKRAAGLDNLLYTADADF
SCFADLALTSPDDYYKEGQGSLLQCVLTPGDPWMPESNEEIAKRVDKQVRALFPSSKNLKLTWSSVVKLA
QSLYREAPGMDPFRPDQKTPISNFFLAGSYTQQDYIDSMEGATLSGRQAAAAIL
>gnl|CDD|274272 TIGR02733, similar_to_to_phytoene_dehydrogenase, C-3',4' desaturase CrtD. Members of this family are slr1293, a carotenoid biosynthesis protein which was shown to be the C-3',4' desaturase (CrtD) of myxoxanthophyll biosynthesis in Synechocystis sp. strain PCC 6803, and close homologs (presumed to be functionally equivalent) from other cyanobacteria, where myxoxanthophyll biosynthesis is either known or expected. This enzyme can act on neurosporene and so presumably catalyzes the first step that is committed to myxoxanthophyll [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
ETSVVVIGAGIAGLTAAALLAKRGYRVTLLEQHAQPGGCAGTFRRRGFTFDVGATQVAGLEPGGIHARIF
RELGIPLPEAKILDPACAVDLPDGSEPIPLWHDPDRWQKERERQFPGSERFWQLCSQLHQSNWRFAGRDP
VLPPRNYWDLLQLVSALRPDTLLTGPLSLLTVADLLRLCGLGDDRRLRRFLDLQLKLYSQEDADETAALY
GATVLQMAQAPHGLWHLHGSMQTLSDRLVEALKRDGGNLLTGQRVTAIHTKGGRAGWVVVVDSRKQEDLN
VKADDVVANLPPQSLLELLGPLGLPPGYRKRLKKLPEPSGAFVFYLGVKRAALPVDCPPHLQFLSDHQGS
LFVSISQEGDGRAPQGEATLIASSFTDTNDWSSLDEEDYTAKKKQYTQTIIERLGHYFDLLEENWVHVEL
ATPRTFERWTGRPQGIVGGLGQRPSTFGPFGLSSRTPVKGLWLCGDSIHPGEGTAGVSYSALMVVRQILA
SK
>gnl|CDD|274273 TIGR02734, Phytoene_desaturase_lycopene-forming, phytoene desaturase. Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLEDDGFRFDTGPTVITMPEALEELFALAGRD
LADYVELVPLDPFYRLCWEDGSQLDVDNDQEELEAQIARFNPGDVAGYRRFLDYAERVYREGYRKLGYVP
FLSPRDLLRADAPQLLALLAWRSLYSKVARFFSDERLRQAFSFHALFLGGNPFRTPSIYALISALEREWG
VWFPRGGTGALVAAMAKLAEDLGGELRLNAEVIRIETEGGRATAVHLADGERLDADAVVSNADLHHTYRR
LLPNHPRRRYPAARLSRKRPSPSLFVLYFGLLGVDGHWPQLAHHTLCFGPRYKELFDEIFRKGRLAEDPS
LYLHRPTVTDPSLAPPGCESLYVLAPVPHLGTADVDWSVEGPRYRDRILAYLEERAIPGLRDRIVVERTF
TPADFRDRYNAWLGSAFSLEHTLTQSAWFRPHNRDRKIDNLYLVGAGTHPGAGVPGVLGSAKATAKLMLG
DLAPG
>gnl|CDD|131782 TIGR02735, purC_vibrio, phosphoribosylaminoimidazole-succinocarboxamide synthase, Vibrio type. Members of this protein family appear to represent a novel form of phosphoribosylaminoimidazole-succinocarboxamide synthase (SAICAR synthetase), significantly different in sequence and gap pattern from a form (see TIGR00081) shared by a broad range of bacteria and eukaryotes. Members of this family are found within the gammaproteobacteria in the genera Vibrio, Shewanella, and Colwellia, and also (reported as a fragment) in the primitive eukarote Guillardia theta [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
SLADQVLAVNDDLPIRTDEPVHSGKVRSVYWLTEEDSRRLIEEKGYPVAHDAPLAIMVISDRISAFDCIW
HAEGGLNGVPGKGAALNAISNHWFKLFAEAGLAESHILDIPHPFVWIVQKAKPVKIEAICRQYITGSMWR
AYAKGERVFCGIDLPEGLAKDQRLPELLITPSTKGILEGIPGVPAIDDVNITRADIERNWSAFNFEQPED
IDHYERLLREGFAVISDRLSKLGQLFVDTKFEFGYVTDVEGTRKLIYMDEVGTPDSSRIWDAGAYAQGKI
VENSKEGFRQALLNWFPDPDILLNKDRMVERAALARDNALPQEMLMDVSETYLGIAEKITGSSITLSENP
KAEIKAILSVEYGLV
>gnl|CDD|131783 TIGR02736, cb-type_cytochrome_C_oxidase_subunit_IV, cytochrome c oxidase, cbb3-type, CcoQ subunit, epsilon-Proteobacterial. Members of this protein family are restricted to the epsilon branch of the Proteobacteria. All members are found in operons containing the other three structural subunits of the cbb3 type of cytochrome c oxidase. These small proteins show remote sequence similarity to the CcoQ subunit in other cytochrome c oxidase systems, so this family is assumed to represent the epsilonproteobacterial variant of CcoQ [Energy metabolism, Electron transport]
GYAYFAFTLLLVIFLYAYIYHLYRSQKKGERDYEKYANLALNDDLDDSLIEPRRKK
>gnl|CDD|131784 TIGR02737, Protein_CtaG, cytochrome c oxidase assembly factor CtaG. Members of this family are the CtaG protein required for assembly of active cytochrome c oxidase of the caa3 type, as in Bacillus subtilis
LLQIFGFRALWSPYFLIILAMVGFLYFLITGPWRRRFGNSDKVTIKQKIYFLTGLLLLYIVKGSPIDLLG
HIMFTAHMVQMAVLYLIVPPLFILGIPAWLWEKIFERPFVEQVLKFFTKPLIALLLFNGLFSLYHVPFVF
DTVKQSPILHTLITFLLFVAAFLMWWPLLAPIPELQKLSDLKKIGYIFANGILLTPACALIIFAPAPLYA
TYTDPAAWAEAMALCVPAGTLVPLSLTGPEMFTSLPTVMDQQLGGVLMKIMQEIVYGTTLGYIFFQWLKK
E
>gnl|CDD|131785 TIGR02738, hypothetical_protein, type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB. This protein is part of a large group of proteins involved in conjugative transfer of plasmid DNA, specifically the F-type system. This protein has been predicted to contain a thioredoxin fold, contains a conserved pair of cysteines and has been shown to function as a thiol disulfide isomerase by complementation of an Ecoli DsbA defect. The protein is believed to be involved in pilin assembly. The protein is closely related to TraF (TIGR02739) which is somewhat longer, lacks the cysteine motif and is apparently not functional as a disulfide bond isomerase
MLRKLLIVLLLLAGLAQASTLDEITNLWAPPQGLTAATDNAPQGRHANQDDYALVFFYQSTCPYCHQFAP
VLKRFSQQFGLPVYAFSLDGQGLTGFPDPLPATPEVMQTFFPNPRPVVTPATFLVNVNTRKAYPVLQGAV
DEAELANRMDEIL
>gnl|CDD|274274 TIGR02739, pilus_assembly_protein_TraF, type-F conjugative transfer system pilin assembly protein TraF. This protein is part of a large group of proteins involved in conjugative transfer of plasmid DNA, specifically the F-type system. This protein has been predicted to contain a thioredoxin fold and has been shown to be localized to the periplasm. Unlike the related protein TrbB (TIGR02738), TraF does not contain a conserved pair of cysteines and has been shown not to function as a thiol disulfide isomerase by complementation of an Ecoli DsbA defect. The protein is believed to be involved in pilin assembly. Even more closely related than TrbB is a clade of genes (TIGR02740) which do contain the CXXC motif, but it is unclear whether these genes are involved in type-F conjugation systems per se
NFRLLPLLVSGLLVSLHPDPLNEKPEGWQWYNEPKEEKEEKKPKPVPLQPSQEPPPLSPTEQMKLLRQET
KEALNQAILNPSVENFARYMRLQRFWTKQSSQFSMTWQKALLAHPELDYTLTHPTSNAARQVYLQLEKEQ
KEKAIQQLSQSYGLFFFYRGKSPISQKMAPVIQAFAKEYGISVIPISVDGTLIPGLPNSRSDSGQAQHLG
VKYFPALYLVNPKSQKMSPLAYGFISQDELKERILNVLTQFKRPDY
>gnl|CDD|274275 TIGR02740, putative_pilus_assembly_and_synthesis_protein, TraF-like protein. This protein is related to the F-type conjugation system pilus assembly proteins TraF (TIGR02739)and TrbB (TIGR02738) both of which exhibit a thioredoxin fold. The protein represented by this model has the same length and architecture as TraF, but lacks the CXXC-motif found in TrbB and believed to be responsible for the disulfide isomerase activity of that protein
LPLLALAVVVILSLAASAAHAQESDTPFVSGQAFYKDEKRGWFWYEDPPPKEEEEPLEPAPPAPPAQQPA
REELAPFSVAWLRENLPELRDKAIDNPTPENVRAYLEAQRIMLDKASRFADVSQRVIWTDPILDETLRRP
VSTLALDAHDTTAKKQKDRVMKDLAKKSGLFFFFKSDCPYCHQQAPILQAFEDRYGIEVLPVSVDGGPLP
GFPNARPDAGQAQQLKIRTVPAVFLADPDPNQFTPIGFGVMSADELVDRILLAAHPAGLIS
>gnl|CDD|131788 TIGR02741, conjugative_transfer_fimbrial_synthesis_protein, type-F conjugative transfer system pilin chaperone TraQ. This protein makes a specific interaction with the pilin (TraA) protein to aid its transfer through the inner membrane during the process of F-type conjugative pilus assembly
MRKFRFSLPEFDITGLWVFSLGIWFHIVSRLVYRKPWMAFFLAELIAVILVLWGAYRVLDAWIARVSREE
RDALEARQEA
>gnl|CDD|131789 TIGR02742, putative_conjugative_transfer_protein_TrbC, type-F conjugative transfer system pilin assembly protein TrbC. This protein is an essential component of the F-type conjugative pilus assembly system for the transfer of plasmid DNA. The N-terminal portion of these proteins are heterogeneous and are not covered by this model
VMVFVSFSMPEPLLKQLLDQAEALGAPLVIRGLLDNGFKATATRIQSLIKDGGKSGVQIDPQWFKQFDIT
AVPAFVVVKDGLACLPEQPCPESDYDVVYGNVSLKGALEKMAQDGDSPQIVAQQLLERIK
>gnl|CDD|274276 TIGR02743, hypothetical_protein, type-F conjugative transfer system protein TraW. This protein is an essential component of the F-type conjugative transfer sytem for plasmid DNA transfer and has been shown to be localized to the periplasm
MTILLLILLLLLFVSSVEAKNLGVYGQTFPIAEPDMLEVIEQRLKRLEQSGELKAMQQRFQSRVLEHVKR
PPPVPGLGTTETPKTWYFDPSITLAQDILDEKGQVLAKKGTRINPLDRVSLSKTLLFFDADDPEQLAWAQ
QQLPSCPNVKWILTGGSVNELEKRLDSRIYFDQHGKLTQKFGIKHVPARVSQEGLRLRIQEI
>gnl|CDD|274277 TIGR02744, type-F_conjugative_transfer_system_protein_TrbI, type-F conjugative transfer system protein TrbI. This protein is an essential component of the F-type conjugative transfer sytem for plasmid DNA transfer and has been shown to be localized to the periplasm
RRLHPLWMIPGCLAMVVLSALVSYGIVRLNSPVTVAFDMKQTLDAFFDSASQKKLSEAQQKALLGRFNAL
LEAELQAWQAQHHAIILVSPAVVSGAVDITDEIQTAIAERMR
>gnl|CDD|274278 TIGR02745, iron-sulfur_cluster-binding_protein, cytochrome c oxidase accessory protein FixG. Member of this ferredoxin-like protein family are found exclusively in species with an operon encoding the cbb3 type of cytochrome c oxidase (cco-cbb3), and near the cco-cbb3 operon in about half the cases. The cco-cbb3 is found in a variety of proteobacteria and almost nowhere else, and is associated with oxygen use under microaerobic conditions. Some (but not all) of these proteobacteria are also nitrogen-fixing, hence the gene symbol fixG. FixG was shown essential for functional cco-cbb3 expression in Bradyrhizobium japonicum
FRKLRYVIGAVLLLIFLITPWIRWNGNQAVLLDFAHRQFHFFGITFWPQEFYLLAGLLIIAALGLFFITT
LAGRVWCGYACPQTVWTDLFDWIERKIEGDRNKRMKLDKAPWTFDKVWKKTLKHLLWLVISLVTGGTFIF
YFVPAPDLFAYLFTGPADHPAYFWVLFFTAATYIFDGWMREQFCIYMCPYARIQSVMFDKDTLIVVYDEK
RGEPRGPRKGKKDPKAPGPLGDCIDCNLCVQVCPTGIDIRDGLQLECINCGLCIDACDDVMEKMGKPKGL
ISYTSEAALEGRKKVRLLRPRTIGYAAVLAIVIGLLAIALSTREPMDLNVLRDRNLLYVRNSDGVVENTY
TLKILNKTEQPHEYYLSVLGLPGIKIEGPGAPIHVKAGEKVKLPVFLRTPPDALKSGITSIEIRAYAEDD
SEGIRVERESVFVG
>gnl|CDD|274279 TIGR02746, hypothetical_protein, type-IV secretion system protein TraC. The protein family described here is common among the F, P and I-like type IV secretion systems. Gene symbols include TraC (F-type), TrbE/VirB4 (P-type) and TraU (I-type). The protein conyains the Walker A and B motifs and so is a putative nucleotide triphosphatase
WLPYRAYDEESGIFMNRHSMGFGLELTPLSGADESLVESLSSLLRTDLPEGTDIQVLLWGSPQIGPFLDR
NEEQFSQNGGILEKLARNRVKYYLNAAQKGFFKNSGVTLRDFRLFLSVSIPFKSPNEDVIQELRSLRERI
ESTLRSAGFGCRRVDAEDLLSLVREMLNPDPDSIHPWPISYDPNQLLRDQIVDPDTDLEVHEGGLEVDHE
DNQGEVKTRIRVFSIKRFPEEFTLWQTGNLIGDLLNPSLQITCPFLLSFTVRVEDQVKKKAKATAKAKDL
NKQAKSSMAKWVPSLEKKLKEIKYLREAIASGGDSLVSMYYNVLLFTNPDNLRRDVEAAKSSFRKNGFDL
AEDKRIQLQAFLAALPFNPTEGLFEDLKKAGRVRTLSSANAVNLLPLIADWKGTKGSGLLLPTRRGQLSA
FDPFDSDSTNYNIAVVGGSGAGKSFFMQELIVDNLSRGGKVWVIDVGRSYKKLCEMLGGTYIEFSPESNI
CLNPFTGNNVTEIDDEIDQITALIALMASPEGGLSDEQRSTLEEAILAAWKEYGNEATITDVQDALQQLE
DDENDPRIKDLGKMLNPYTSHGVYGRYFNGPNNLDFSNRFVVLELEELEDRPDLQAVVLFSLMVRITGEM
YLTPRKRRKICIIDEAWSLLDGANPQAADFIETGYRRARKYGGAFITITQGIEDFYSSPEARAAYANSDW
KIILRQSAESIAKLKAENPFTFSPFEKRLIKSLRTAKGAFSELLIRSGEGSSVHRLFVDPFSRVLFSTDG
PEFEEVEELREQGLSLEEAIEQLAQKH
>gnl|CDD|274280 TIGR02747, conjugative_transfer:_assembly, type IV conjugative transfer system lipoprotein TraV. The TraV protein is a component of conjugative type IV secretion systems. TraV is an outer membrane lipoprotein and is believed to interact with the secretin TraK. The alignment contains three conserved cysteines in the N-terminal half
MRIRFLLLIACVAFLTGCSAGCNSNFSCEGTGGWGTCATMDQVNDDKRTLKAQNEARKLLHGEFSARGVL
PNIHPQTAPQKTLASGAALQPTPAFQPLVRRNRPGQPLRTQERVAKLWIAPYIDPEGNYHDPGDVYSIIK
PGQW
>gnl|CDD|131795 TIGR02748, Heptaprenyl_diphosphate_synthase_component_2, heptaprenyl diphosphate synthase component II. Members of this family are component II of the heterodimeric heptaprenyl diphosphate synthase. The trusted cutoff was set such that all members identified are encoded near to a recognizable gene for component I (in pfam07307). This enzyme acts in menaquinone-7 isoprenoid side chain biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
KLADIYSFLQKDIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAV
ALELIHMASLVHDDVIDDADLRRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVE
VCRGEIEQIKDKYNFDQNLRTYLRRIKRKTALLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITD
DILDFVGTEEELGKPAGGDLLQGNVTLPVLYAMEDPFLKKRIEQVLEETTAEEMEPLIEEVKKSDAIEYA
YAVSDRYLKKALELLDGLPDGRAKKPLQEIAKYIGKRKY
>gnl|CDD|131796 TIGR02749, Prenyl_transferase, solanesyl diphosphate synthase. Members of this family all are from cyanobacteria or plastid-containing eukaryotes. A member from Arabidopsis (where both plastoquinone and ubiquinone contain the C(45) prenyl moiety) was characterized by heterologous expression as a solanesyl diphosphate synthase [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
ASATSLFAPVEDDLYLLTDNLKSLVGARHPILYAAAEHLFSAGGKRLRPAIVLLVSRATAEQQELTPRHR
RLAEITEMIHTASLVHDDVIDESDTRRGIETVHSLFGTRVAVLAGDFLFAQASWYLANLENLEVVKLISK
VITDFAEGEIKQGLNQFDSDLSLEDYLEKSFYKTASLVAASSKAAAVLSDVPSQVANDLYEYGKHLGLAF
QVVDDILDFTGSTEQLGKPAGSDLMKGNLTAPVLFALEEEPKLSELIEREFSQKGDLEQALSLVRKSGGI
KKARELAKEQAQLALQSLSFLPPSPPREALKELVHFVLSRLY
>gnl|CDD|274281 TIGR02750, hypothetical_protein, type-F conjugative transfer system mating-pair stabilization protein TraN. TraN is a large cysteine-rich outer membrane protein involved in the mating-pair stabilization (adhesin) component of the F-type conjugative plamid transfer system. TraN is believed to interact with the core type IV secretion system apparatus through the TraV protein
WVLLFLLLASGLAAADQNQDYQDGVNWAKQAADQALDNIKGFCPDAACPGYTANPPQTGYYPQEDTGLNS
QKTAAIANNDTAKAVQENFNNGRPDLNPNTPAMQKALLIQENADAITHGQSNDYVDCNKGSQCTIEEIEK
QCESSLTLNMVTCTKTLVVTVDSEKTASYSLTVSYTRSGVICVRPVTVTTAGLTNCAPGDVPYTWIEWNR
PAFPIRLGAPCEGISVTVTNHGQPLYWTKQWPTCTNTTLLVATINCGNGRTTVPLALTVTVHSKEYISDE
YWDNQCEPIQSKCFITSEQCTEPNQTRVIGGVPTSLPCWKYRLTYQCGSAQSDTCATLVNQGCEQTASTC
SKSQAGVCVEYKQTYSCPEKTCSDTQLICGEDSFCLDGDCYKHTPEQSDDFGEAVSSLAALAEAAKDLGD
PPLIFTGKAMECKKKPLGFSDCCKDSGWGQDIGLAKCSDAEKALGKAKENKLTVYLGEYCAKKVLGVCLR
KKRSYCVFDSKLARIVQEQGRGGQLGIGFGSAKHPDCRGITPEELQQINFESIDFSPFYEDLHNNQKLPD
NDEITQRLQSAI
>gnl|CDD|131798 TIGR02751, Uncharacterized_protein_conserved_in_archaea, phosphoenolpyruvate carboxylase, archaeal type. This family is the archaeal-type phosphoenolpyruvate carboxylase, although not every host species is archaeal. These sequences bear little resemblance to the bacterial/eukaryotic type. The members from Sulfolobus solfataricus and Methanothermobacter thermautotrophicus were verified experimentally, while the activity is known to be present in a number of other archaea [Energy metabolism, Other]
IPRTMSTQHPDNAKIPFWASSKVISGEDEVEEAYEAYSHLGCDEYMWDFEGKEVDTHVVRKLLSRYYDFF
KEHILGKDIFLTYRVPNPAIEGAEAKLLLETLESIPRNYDVAREFYDERIAPIFEVILPMTTSADEILNV
HQYYEKAVAGKQSIELYDEVTVKEWLGEFKPKKIRVIPLIEDKDSLLNADEIVKEYAEAHEPEYMRVFLA
RSDPALNYGMIAAVLSNKYALSRLYELSEETGISIYPIIGAGSLPFRGHLSPENIERVLDEYPGVYTFTV
QSAFKYDYPREEVVAAIRRINEKLPNAPPILIDEEEEIIVEIIEIYAKRYQKIIEKLAPTINRIASYIPK
RRDRKLHVGLFGYSRSVGGVSLPRAIKFTGALYSIGLPPELIGIGSLSELDEDDLEVIKELYPNLRSDLS
FAARYLNPESADSLKDIVKLSEETEDMIVIDVKYDEDEPGIKYNLVYTLEEHLLYTGLIGKAFKEEVFQA
VRSLILEMALIRKFLG
>gnl|CDD|131799 TIGR02752, Demethylmenaquinone_methyltransferase, demethylmenaquinone methyltransferase. MenG is a generic term for a methyltransferase that catalyzes the last step in menaquinone biosynthesis; the exact enzymatic activity differs for different MenG because the menaquinone differ in their prenoid side chains in different species. Members of this MenG protein family are 2-heptaprenyl-1,4-naphthoquinone methyltransferase, and are found together in operons with the two subunits of the heptaprenyl diphosphate synthase in Bacillus subtilis and related species [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
ESKEERVHKVFEKIYKKYDRMNSVISFQRHKKWRKDTMKRMNVQAGTSALDVCCGTADWSIALAEAVGPE
GHVIGLDFSENMLSVGRQKVKDAGLHNVELVHGNAMELPFDDNSFDYVTIGFGLRNVPDYMQVLREMYRV
VKPGGKVVCLETSQPTIPGFKQLYFFYFKYIMPLFGKLFAKSYKEYSWLQESTRDFPGMDELAEMFQEAG
FKDVEVKSYTGGVAAMHMGFK
>gnl|CDD|131800 TIGR02753, Superoxide_dismutase, superoxide dismutase, Ni. This superoxide dismutase uses nickel, rather than iron, manganese, copper, or zinc. Its gene is always accompanied by a gene for a required protease
MLYDLIASLLKKLPFPVVMAHCDGPCGVYDPASARISAEAVLAMTKKLNALKPPSSLDADYQNTFSRFVA
VKEEQAIETKKEISVLWTDYFKPPHLEQFPELHELVWKAAKACSAAKVNIDKAAAQELLQYVEKIHEIFW
ETKKR
>gnl|CDD|274282 TIGR02754, putative_signal_peptidase, nickel-type superoxide dismutase maturation protease. Members of this protein family are apparent proteases encoded adjacent to the genes for a nickel-type superoxide dismutase. This family belongs to the same larger family (see pfam00717) as signal peptidase I, an unusual serine protease suggested to have a Ser/Lys catalytic dyad [Cellular processes, Detoxification, Protein fate, Protein modification and repair]
AKVTGVSMSPTLPPGDRIIVVPWLKIFRVPPIGNVVVVRHPLQPYGLIIKRLAAVDDNGLFLLGDNPKAS
TDSRQLGPVPRSLLLGKVLW
>gnl|CDD|131802 TIGR02755, TraX_protein, type-F conjugative transfer system pilin acetylase TraX. TraX is responsible for the acetylation of the F-pilin TraA during conjugative plasmid transfer. The purpose of this acetylation is unclear, but the reported transcriptional regulation of TraX may indicate that it is involved in the process of pilu extension/retraction
VLNWSPGQRDVIKTVALVLMVGDHINTIFQLDQEWLFLAGRGAFPLFALVWGLNLSRHTHIRQHAINRLW
GWALIAQPGYWLAGFPWYEGNILFAFAVVAQVLLWCESRTARNGAAAFLLLMGWTPLSGTSYGIAGLLML
AGALRLYRVRDTEERLALFACLLLLVPALNLRTSDAAAVAGLILTLLTVGLVSATGKSRPRFWPGDFFPP
FYACHLAFLGFLVR
>gnl|CDD|274283 TIGR02756, hypothetical_protein, type-F conjugative transfer system secretin TraK. The TraK protein is predicted to interact with the TraV and TraB proteins as part of the scaffold which extends from the inner membrane, through the periplasm to the cell envelope and through which the F-type conjugative pilus passes. TraK is homologous to the P-type IV secretion system protein TrbG, the Ti-type protein VirB9 and the I-type TraN protein. The protein is related to the secretin family especially the HrcC subgroup of the type III secretion system. The protein is hypothesized to oligomerize to form a ring structure akin to other secretins
AGILFLGLVSATASGTLGAVTVTFANGEDIAIALSSTDPNRLVVEGDRITAVSFPENGMLVSKGTEDDTT
GSVVVKPVAKKPFTFYLTTEKGLHFSVRIVPRAIAGKTIELVSLRGTGEEAGVWETAAPYTQSYESVLVA
VIRALRGGTLPAGFYQIPVTPEALQLPAGLSVRPDAVWTGNHLKGERFELENKTNSPLELTESWFWQPGT
RAVALSKPQLAPGETADLYRIR
>gnl|CDD|274284 TIGR02757, conserved_hypothetical_protein, TIGR02757 family protein. Members of this uncharacterized protein family are found sporadically, so far only among spirochetes, epsilon and delta proteobacteria, and Bacteroides. The function is unknown and its gene neighborhoods show little conservation [Hypothetical proteins, Conserved]
FIPPDPLQFPHRYKDKEDIEISGLICALFSYGNRKAILKSLDKLDFSLLGNSPYAYLLSSTWAQLKNAGF
KTFYYRFQNEKDIQAIFKTLYRIYESHGSLEELFYAAYYKGPPIERLSSFRKHIIKLNSYNNTIADPSGG
SPLKRLNMFLRWMIRKDEVDLGIWESFKPSDLILPLDTHVFRIAKKLKLLKRKSYDLKAAIEITEALREL
NPEDPIKYDFALFRLGQNK
>gnl|CDD|131805 TIGR02758, putative_conjugative_transfer_protein_TraA, type IV conjugative transfer system pilin TraA. TraA is the single structural subunit of the pilus found in type IV conjugative transfer systems. This family is generally found in gammaproteobacteria. The pilins show considerable heterogeneity among the different conjugative plasmit types. All of them however contain an N-terminal part which is cleaved off by a leader peptidase (LepB, or similar) to result in a 68-78 amino acid product. Pilins may be further processed by acetylation (in F-like systems by the TraX protein) or by cyclization (in P-like systems by the TraF protein)
NTRMALLLGVTAIAALSALAAFQPALAADLFAGGKATVKATAGKDSSVEMAMILAGLLVAAVMGFMTKNW
FAALGGFAGGSIFWNVGMALVGL
>gnl|CDD|131806 TIGR02759, putative_conjugative_transfer_protein_TraD, type IV conjugative transfer system coupling protein TraD. The TraD protein performs an essential coupling function in conjugative type IV secretion systems. This protein sits at the inner membrane in contact with the assembled pilus and its scaffold as well as the relaxosome-plasmid DNA complex (through TraM)
FTRGGQITFHNIRMFFQVTKTLFYWMFILFIILTGLILWFMASVNTFLGNIYYWEAQLFTLVGHIKTQEV
FTPWFGKTYTTYQAQILTNPYVIRAYDQLWQALQKSALAALAISLVVFLLFMFFFIKRGEQQSKDHFIRG
SQLSSPKELIKKLKKSRRASDIKIGGLPLIKFGSETQHILIHGTTGSGKSVAIRKLLRWIRQRGDRAIIY
DKGCTFTSRFYDPSQDVILNPFDERCANWDVWRECKDKTDFENMAEALIPMHGDGDPFWVDSARTIFTST
AYKMRNDPKRSTSKLLDLLLTSELEELRDYLKGTESASLVSDKIEKTAISIKSVLATYLKSLRFLEGLDR
KGREPFSIRDWILNEQKNGWLFISSNAQQHASLKPLISMWLSIASRGLLSLPPNDDRRIWFIMDELPSLH
KLPDLDETIAEVRKFGGCYVLGIQSFAQLEKIYGQNGAATLFDLLNTRFFFRSPSAKMAKIVSDDLGEQE
IEESKENYSYGANSVRDGVSLGSQTITRPLVSYSDIQFLDDLQCYVRLPGNYPITKLKLKYDERPKICPP
FIPRDI
>gnl|CDD|274285 TIGR02760, conjugative_transfer_relaxase_protein_TraI, conjugative transfer relaxase protein TraI. This protein is a component of the relaxosome complex. In the process of conjugative plasmid transfer the realaxosome binds to the plasmid at the oriT (origin of transfer) site. The relaxase protein TraI mediates the single-strand nicking and ATP-dependent unwinding (relaxation, helicase activity) of the plasmid molecule. These two activities reside in separate domains of the protein
MMSISPLRSAGDAAAYYLDEDNYYLKDSKSLNNTRWLGKGAEQLGLLGKPVEKEQFEALLSGTLPDGTQL
GRIDKGGIHHRPGFDLTFSAPKSVSILALVGGDKRLIEAHDKAVKIAVSEMEKDAAQARQTVDGKTEFIN
TRNLVFAMFRHKTSRENDPQLHTHAVVQNMTHDSDGKWRSLASDMKGQKGVIEGFRERIYNHQIYYGLLY
RSKLAKKVEELGYQTASVGKGQFEIQGVPEQVLTAFSKRRQQIDELVDEKGWSSAKARDIAALDTRKDKT
YIDDETLMEKWQQECKDMGFDPHALVASSYKPENIVARFYGPSQIDAQHAVEVAIAHLSQYSTQFEYEKL
IEEAAKYFTAGNKIIDEIDIKKAIDELIANGQLIPLFTQKGLFTTQTMLTNEKELIARTEGGKGALRVIV
SKQKLSEFALSPSNKDAVSTLFTSTKRFIIINGFGGTGSTEIAQLLLHLASEQGYEIQIITAGSLSAQEL
RQKIPRLASTFITWVKNLFNDDQDHTVQGLLDKSSPFSNKDIFVVDEANKLSNNELLKLIDKAEQHNSKL
ILLNDSAQRQGMSAGSAIDLLKEGGVTTYAWVDTKQQKASVEISEAVDKLRVDYIASAWLDLTPDRQNSQ
VLATTHREQQDLTQIIRNALKQEGQLSRQEVTVPTLKPVNLTGIQRRNAAHYKQGMVIRFWQKGKIPHDD
YVVTNVNKHNNTLTLKDAQGKTQKFKPSSLKDLERPFSVYRPEQLEVAAGERLQVTGNHFHSRVRNGELL
TVSSINNEGITLITEDGQTLHLPHGALEDAHLDYGYVLTPYHTQPDDAKVFLGVKQYALSKALLNSLNRS
ASRVDLFTDLDEKAQRYLEKTRGIPSAIVVVDQKQHLPDAVTTNNTDKSLEMDISDTLHALEAKAKDGKN
SIALQYALEKVSEKEAAFKQKELVTEAYVFAFEETGFAIKAAEIAAALKNRPKLYRLLSAEYGDGTRWTT
RAALRTETSILLHILPGKETVTPLATRAQVFLNLELLERLTHGQKQAIHLIISTKDRFVAVQGLAGVGKT
TMLESRYKPVLQAFESEQLQVIGLAPTHEAVGELKSAGVQAQTLDSFLTDISLYRNSGGDFRNTLFILDE
SSMVSNFQLTHATELVQKSGSRAVSLGDIAQLQSLAAGKPFELAITFDIIDTAIMKEIVRQNNSAELKAA
HNSLDKRSNPKALELLKNQNPLQHELMQNAAMPEIASDEQGLQKHDLAKLAVNTEKPKKAQPDATVTLYR
EIVKDYLSRTPEFRENTLIIAHTNNDRTGIYPFIREGLIKQKELSKQQVTVPRLRSVNISSPELKTMMPF
EKGAVLRLKKDAYLTIADIDREHGKLTVADIKTGSERDILPRQLDHTFTSLYSDSELPLAKGDKIRLRAT
DKNRGIKANEVYTVTQVVNGLSVQLSKVKNSLSLKPIQAKDKHWDYAYTRTADSAQGATYTFVIALIKGR
LALTNYRSAYIDLTRASHHVELYTDNKEGTVKSWKQREANKTSAVETEEDYRPKQSTQFNNRAQPHEEPK
YQQKNGPLKIQSAAEIINEALPAYTESLAKTLLGEPNTQKSRRDRYTFGAKGGLKVSLTGKYRGLWHDFS
TGEKGTLIQLIEAKKGLSFKEALNQAASLLGIPQHYQLSINIKAPQLSNTEPQKLNQLEKRAKSLFQGSQ
ELKGTLAEKYLKQHRGLASIDNDDIRFHPTVYSSDKKNKHPALIAAARNEKGEITGIQITYLDKDDANKD
KDMDNNKRVKGSISGQFVVINKGMQGDRSYIAEGIETGLSIALANPKATVVIAVGGKNNLSPIIPKFIPK
NVVIVLDNDGEEAKSQRAIEKIINKFKQDNISARIVFPDDWNDIGEEELQKQLMRAISSIEDKDIEIPKA
IADFESVLKMPNSDIISIIDNARTEREKSDLEQIVANEHKSQQALERDLNKEFTPDKRTTKLRSDREMER
>gnl|CDD|163004 TIGR02761, plasmid-like_conjugative_transfer_protein_TraE, type IV conjugative transfer system protein TraE. TraE is a component of type IV secretion systems involved in conjugative transfer of plasmid DNA. The function of the TraE protein is unknown
MKFEQFKSELEGLSKRRNLLFVLVSGVLAVNVLLSIVLIVALKKTRTVVVPPTISQAFTVSAASADATYL
ELMGLYFIQLRLNVTPESADAQHNALLGYVEPQNYGQIKSRLAKEAEEIKKANASSVFYPKSVEWNPQEG
TVKVRGHLKRFVGGRLLSDERKTYLLRFSYSGGRLVLDDFK
>gnl|CDD|274286 TIGR02762, Hypothetical_protein., type IV conjugative transfer system protein TraL. This protein is part of the type IV secretion system for conjugative plasmid transfer. The function of the TraL protein is unknown [Cellular processes, Conjugation]
LVYKIPKYLDEQPRILGWPLDEFLPGATLFGVGILSGKALIGLILGAAVMLIWKLRRLKGGEGPNFLLHL
FYWYLPASLNTLRATPPSHKRIWL
>gnl|CDD|131810 TIGR02763, Internal_scaffolding_protein_VP3, chlamydiaphage internal scaffolding protein. Members of this protein family are encoded by genes in chlamydiaphage such as Chp2, viruses with around eight genes that infect obligately intracellular bacterial pathogens of the genus Chlamydia. This protein, initially designated VP3 (as if a structural protein of mature viral particles), is displaced from procapsids as DNA is packaged, and therefore is described as a scafolding protein [Mobile and extrachromosomal element functions, Prophage functions]
IEKIVAKANAPSVLHAFETRSPEYGECPSPLDYQEALNIVIEGEEAFDSLPAKVRENFGNDPEEMLSWLE
DEANYDEVEALGLLDPETKIRAIMMRIKVQIKKSKLQKDQKEEV
>gnl|CDD|274287 TIGR02764, Probable_polysaccharide_deacetylase_PdaB, polysaccharide deacetylase family sporulation protein PdaB. This model describes the YbaN protein family, also called PdaB and SpoVIE, of Gram-positive bacteria. Although ybaN null mutants have only a mild sporulation defect, ybaN/ytrI double mutants show drastically reducted sporulation efficiencies. This synthetic defect suggests the role of this sigmaE-controlled gene in sporulation had been masked by functional redundancy. Members of this family are homologous to a characterized polysaccharide deacetylase; the exact function this protein family is unknown [Cellular processes, Sporulation and germination]
VDTSDKKIALTFDISWGNDYTEPILDTLKEYDVKATFFLSGSWAERHPELVKEIVKDGHEIGSHGYRHKN
YTTLEDEKIKKDLLRAQEIIEKLTGKKPTLFRPPSGAFNKAVLKAAESLGYTVVHWSVDSNDWKNPGVES
IVDRVVKNTKPGDIILLHASDSAKQTVKALPTIIKKLKEKGYEFVTISELI
>gnl|CDD|274288 TIGR02765, deoxyribodipyrimidine_photolyase, cryptochrome, DASH family. Photolyases and cryptochromes are related flavoproteins. Photolyases harness the energy of blue light to repair DNA damage by removing pyrimidine dimers. Cryptochromes do not repair DNA and are presumed to act instead in some other (possibly unknown) process such as entraining circadian rhythms. This model describes the cryptochrome DASH subfamily, one of at least five major subfamilies, which is found in plants, animals, marine bacteria, etc. Members of this family bind both folate and FAD. They may show weak photolyase activity in vitro but have not been shown to affect DNA repair in vivo. Rather, DASH family cryptochromes have been shown to bind RNA (Vibrio cholerae VC1814), or DNA, and seem likely to act in light-responsive regulatory processes [Cellular processes, Adaptations to atypical conditions]
KVVLYWFRNDLRVHDNPALYKASSSSDTLIPLYCFDPRQFKLTHFFGFPKTGPARGKFLLESLKDLRTSL
RKLGSDLLVRSGKPEDVLPELIKELGVRTVFLHQEVGSEEKSVERLLQQALARLGIHVEQHWGSTLYHED
DLPFDLEDLPDVFTQFRKQVEAKCSIRPPLPAPEKLPPLPSVDDPGWIPTLEDLGEESSEVDRGLPFVGG
ETAGLARLKEYFWSKDLKSYKETRNGMLGPDYSTKFSPWLALGCVSPRQIYEELQRYETERGANDSTYWV
IFELLWRDYFRFYALKYGNRLFRFGGLRGKHPKWSFDAKRFEQWKTGTTGYPLVDANMRELNATGFMSNR
GRQNVASFLVKDLGLDWRYGAEWFETQLVDYDVCSNWGNWQYLAGVGNDPRGSRQFNIEKQAQDYDPDGE
YVATWVPEL
>gnl|CDD|131813 TIGR02766, crypt_chrom_pln, cryptochrome, plant family. At least five major families of cryptochomes and photolyases share FAD cofactor binding, sequence homology, and the ability to react to short wavelengths of visible light. Photolysases are responsible for light-dependent DNA repair by removal of two types of uv-induced DNA dimerizations. Cryptochromes have other functions, often regulatory and often largely unknown, which may include circadian clock entrainment and control of development. Members of this subfamily are known so far only in plants; they may show some photolyase activity in vitro but appear mostly to be regulatory proteins that respond to blue light
IVWFRRDLRVEDNPALAAAARAGPVIPVFVWAPEEEGQYYPGRVSRWWLKQSLAHLDQSLRSLGTCLVTI
RSTDTVAALLDCVRSTGATRLFFNHLYDPVSLVRDHRAKEVLTAQGISVQSFNADLLYEPWEVYDELGRP
FTMFAAFWERCLSMPYDPESPLLPPKKIISGDVSKCSADDLGFEDDSEKGSNALLARAWSPGWSNADKAL
TEFINGPLLEYSKNRKKADSATTSLLSPYLHFGEVSVRKVFHLVRMKQIAWANEGNSAGEESVNLFLRSI
GLREYSRYISFNHPFSHEKPLLGHLKFFPWAVDENYFKAWRQGRTGYPLVDAGMRELWATGWLHDRIRVV
VSSFFVKVLQLPWRWGMKYFWDTLLDADLESDALGWQYISGSLPDGRELDRIDNPQLEGYKFDPNGEYVR
RWLPELARLPTEWIHHPWDAPESVLQAAGVELGSNYPLPIVGLDEARARLHEALS
>gnl|CDD|131814 TIGR02767, Conjugal_transfer_protein_TraG, Ti-type conjugative transfer system protein TraG. This protein is found in the Agrobacterium tumefaciens Ti plasmid tra region responsible for conjugative transfer of the entire plasmid among Agrobacterium strains. The protein is distantly related to the F-type conjugation system TraG protein. Both of these systems are examples of type IV secretion systems
RLLLIILPIAIMLAAMFATSGMEQRLAAGTSPQAKYWLGRAGPLLVLIAAVAIGLIGLFAANLHARKAAG
LSSLAGFGVVATIATLREVIRLNPYVASSVPTWQSALAFADPVTVIGASIGFISGMFALRISSTTAPKVI
RAKRGVFGDADWMKIQEAAKLFPERGGIVIGERYRVDRDSVAAMPFRPDDRQTWGAGGKAPLLTFDGDFG
STHMIFFAGSGGFKTTSVVVPTALKYGGPLVCLDPSTEVAPMVCEHRRQAGNRKVIVLDPTAGGVGFNVL
DWIGRHGNTKEEDIVGVATWLLTDNPRTESSRDDYFRAQAHNLLTALLAHVCLSGEYETEDRNLRRLRAI
LSEPEPKVRARLRKIQEGSESDFIRENVGVFVNMTPQTFSGVYATASKDTQWLSLPNYAGLVCGNSFSSS
DIADGKTDVFINLPASILESYPGIGRVIIGSLLNAMYNADGNVKGRTLFLLDEVDLLGYMRILEEARDRG
RKYGISLMLIYQSLGQLREHFGRDGASSWFESCSFISYAAIKDLDTADYISKRCGDMTVEVDGTNRSTGM
SGSSRSRNKNLQRRPLILPHEILQEMRSDEQIIFTQGNPPLRCGRAIYFRRKDMKACAGENRF
>gnl|CDD|274289 TIGR02768, conjugal_transfer_protein_TraA, Ti-type conjugative transfer relaxase TraA. This protein contains domains distinctive of a single strand exonuclease (N-terminus, MobA/MobL, pfam03389) as well as a helicase domain (central region, homologous to the corresponding region of the F-type relaxase TraI, TIGR02760). This protein likely fills the same role as TraI(F), nicking (at the oriT site) and unwinding the coiled plasmid prior to conjugative transfer
MAIYHLSASIISRSSGRSAVAAAAYRSAARLVDERIGRVFDFTRKDGVAHSEIVLPDGAPDSFLERAALW
NAVEAAEKRKDAQLAREFEIALPRELNLEQNIELARRFVRDHFVEKGMVADWAIHDDGDGNPHAHLLTTT
RPLEENGFGAKKVRVLGEDGQPYEFWAGSKEDLDYWREQWAELANEHLAEAGLDLRIDHRSYAEQGIDLI
PTKHIGVHAKAMERRGEAAERLPENLAIRQENAERILDNPELVLDLLTTEQSVFTRRDIARLLHRYIDDP
QQFQQLMARVLASPQLVALGDPGTGKEPARFSTREMIRLEAQMARSAEALSQSQGHGVSPPIVDAAIDQH
YRLSEEQYEAVRHVTGSGDIAVVVGRAGTGKSTMLKAAREAWEAAGYRVIGAALSGKAAEGLQAESGIES
RTLASLEYAWANGRDLLSDKDVLVIDEAGMVGSRQMARVLKEAEEAGAKVVLVGDPEQLQPIEAGAAFRA
IAERIGYAELETIRRQREAWARQASLELARGDVEKALAAYRDHGHITIHDTREEAIEQVVADWKQDLREA
NPAGSQIMLAHTRKDVRALNEAAREALIERGELGESILFQTARGERKFAAGDRIVFLENNRDLGVKNGML
GTVEEIEDGRLVVQLDSGELVIIPQAEYDALDHGYATTIHKSQGVTVDRAFVLASKSMDRHLAYVAMTRH
RESVQLYAGKEDFTDRGALVKTLSRSSTKDTTLDYPHDFAIRRG
>gnl|CDD|131816 TIGR02769, Nickel_import_ATP-binding_protein_NikE, nickel import ATP-binding protein NikE. This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase [Transport and binding proteins, Cations and iron carrying compounds]
SLLEVRDVTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSF
RGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLR
SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHD
LRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNLQSAVLPEHPVRRSITT
>gnl|CDD|131817 TIGR02770, Nickel_import_ATP-binding_protein_NikD, nickel import ATP-binding protein NikD. This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous [Transport and binding proteins, Cations and iron carrying compounds]
LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQN
PRTAFNPLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALAL
LLEPPFLIADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTV
KEIFYNPKHETTRKLLSAHL
>gnl|CDD|131818 TIGR02771, Conjugal_transfer_protein_TraF, conjugative transfer signal peptidase TraF. This protein is found in apparent operons encoding elements of conjugative transfer systems. This family is homologous to a broader family of signal (leader) peptidases such as lepB. This family is present in both Ti-type and I-type conjugative systems
LVIFVLGIAGLALSGLTILGLYCVGARINTTKSLPLGLYWTTSSKPVERGDYVVFCPPDNPQFEEARERG
YLREGLCPGGFGPLLKRVLGLPGDRVTVRADVVAINGQLLPYSKPLATDSSGRPLPPFPEGVIPPGFFVV
HDTSPTSFDSRYFGPISREQVIGRVKPLFTW
>gnl|CDD|274290 TIGR02772, conserved_hypothetical_protein, Ku protein, prokaryotic. Members of this protein family are Ku proteins of non-homologous end joining (NHEJ) DNA repair in bacteria and in at least one member of the archaea (Archaeoglobus fulgidus). Most members are encoded by a gene adjacent to the gene for the DNA ligase that completes the repair. The NHEJ system is broadly but rather sparsely distributed, being present in about one fifth of the first 250 completed prokarytotic genomes. A few species (e.g. Archaeoglobus fulgidus and Bradyrhizobium japonicum) have multiple copies that appear to represent recent paralogous family expansion [DNA metabolism, DNA replication, recombination, and repair]
ARAIWKGAISFGLVNCPVKLYPATESEDISFHQLHREDGNRVRYQKVCSETGKEVEREEIVKGYEYDKGK
YVIIEDEDIESLPPESTKTIEIEAFVDADEIDPIYFDTPYYLAPDKGGEKAYALLREALEDTGKVGIAKV
VLRGRERLAALRPVGKGLVLTTLRYPDEVRSPDEFFGPIKDVEVDPEELELAGQLIDKMTGKFDPEDYHD
EYREALLELVDAKLEGGKPPKAEEPAAPAPGNVVDLMDALKASLRAAK
>gnl|CDD|213736 TIGR02773, ATP-dependent_helicase/deoxyribonuclease_subunit_B, helicase-exonuclease AddAB, AddB subunit. DNA repair is accomplished by several different systems in prokaryotes. Recombinational repair of double-stranded DNA breaks involves the RecBCD pathway in some lineages, and AddAB (also called RexAB) in other. The AddA protein is conserved between the firmicutes and the alphaproteobacteria, while the partner protein is not. Nevertheless, the partner is designated AddB in both systems. This model describes the AddB protein as found Bacillus subtilis and related species. Although the RexB protein of Streptococcus and Lactococcus is considered to be orthologous, functionally equivalent, and merely named differently, all members of this protein family have a P-loop nucleotide binding motif GxxGxGK[ST] at the N-terminus, unlike RexB proteins, and a CxxCxxxxxC motif at the C-terminus, both of which may be relevant to function [DNA metabolism, DNA replication, recombination, and repair]
MGLRFIYGRSGTGKTTFIINEIKQKIKRNPFGKPIILLVPDQMTFQMEYALLNDIELNGMLRAQVLSFSR
LAWRVLQETGGLTRTFLTSTGKQMLIRKLIEEHKDELKVYQKASRKKGFTAQLSEMITEFKRYEVTPEDL
RRMAESITDSEYLKEKLEDLSIIYQQFEERLADQYLDSEDYLTLLAEKIPQSEDIKGAEIYIDGFHSFTP
QEYSVIEALMKKAKKVTVSLTLDKPSKREPDELSLFRATSKTYYRLKQLAKELGIDVEEPIFLNTERPTK
NKELAHLEKQFDARPAIAYAEKQESLSIFQANNRRAEVEGVAREILRLVRDKGYRYKDIAILTRDPEDYK
DLVKAVFSDYEIPYFIDKKRSMLNHPLIEFIRSSLDVIQGNWRYEAVFRYLKTGLLFPLNEPFIDVRELI
DQLENYVLAYGIKGKKRWWKEDWFQYRRFRGLDDDFAQTDEEIEMQEMLNDTRDWIVPPLFTFEKRMKKA
KTVKEFAEALYEFLEELDLPDKLEKERQRAEDDGRIEEAREHEQAWDAVIQLLDEFVEVLGNEEMDLNLF
QEVIDIGLEQLEFSLIPPALDQVFVGTMDRSKMYNTKCIFLLGANDGVLPARPKENGILSDEDRELLEQI
GVELSSTSREKLLDEQFLVYTAFTSASDRLKVSYPLADAEGKSLRPSIIIHRLEELFPKLKESLLLNEPE
QVSDEEQLSYVSNKLPTLSELTSQLRKWKRGYPISDVWWDVYNWYREEDKWKQGLEYVLSGLFYDNETKQ
LQESKAKQLYGERIQASVSRLETYNACPFAHFAQYGLKLKERKIYKLEAPDLGQLFHEALKEISDELKEE
KLDWSDLTKEQCRLFANDAVENLAPKLQHEILLSSNRYRYVQKKLKRIVTRAVGVLSEQAKRSGFVPVGL
ELGFGFGKNPLPPLKLQLKNGEELELRGRIDRVDKAEKEDETYLRIIDYKSSSKGLDLTEVYYGLALQML
TYLDIVLTNSAKWLGNQATPAGVLYFHIHDPMIQAKGDLTEEEIEQEIFKEYKMKGLLLSDQEVVRLMDT
TLEEGSSNIIPASLKKDGSLGSRSKAATEEEFELLRKHVRRKFQEAGENITDGRVSIEPYKMKKQTPCQY
CNFSSVCQFDTSLEENEYRHLEAEKDETILEWINEEVGGN
>gnl|CDD|274291 TIGR02774, putative_ATP-dependent_exonuclease_subunit_B, ATP-dependent nuclease subunit B. DNA repair is accomplished by several different systems in prokaryotes. Recombinational repair of double-stranded DNA breaks involves the RecBCD pathway in some lineages, and AddAB (also called RecAB) in other. The AddA protein is conserved between the firmicutes and the alphaproteobacteria, while the partner protein is not. The partner may be designated AddB, as in Bacillus and in alphaproteobacteria, or RexB as in Streptococcus and Lactococcus. Note, however, that RexB proteins lack an N-terminal GxxGxGK[ST] ATP-binding motif found in Bacillus subtilis and related species, and this difference may be important; this model represents specifically RexB proteins as found in Streptococcus and Lactococcus [DNA metabolism, DNA replication, recombination, and repair]
KLLYTDIRTSLTEILVNEAEEAAAAGKRVFYIAPNSLSFEKERAVLEYLPQQASFSITVTRFAQMARYFV
LNDLPAKTTLDDIGLAMIFYRALAQLEPGDLKVYGRLKQDPQFIQQLVELYKELQKSQLSILDLENLTSP
DKREDLLAIFEKVTAYLNQGQYAQQSKLAHFIEAIESGKLDSDLKNTVLVIDGFTRFSAEEEALVSLLHG
KGVEIIIGAYASQKAYKSSFSEGNLYQASVKFLHDLAQKYQTKAEFISSTHESKDSFDKLSRLLEASHDF
SELALDLDDKDKDNLTIWSCLTQKEEVEHVARSIRQKLYEGYRYKDILVLLGDVDSYQLQLGKIFDQYDI
PFYLGKAEPMAHHPLVQFIESLERIKRYRFRAEDVLNLLKTGLYGDFSQSDIDAFEQYIRYADIKGLPKF
QKTFTKNHHGKFDLDRLNVLRQRILAPLEELFKSRKQLGEKLLNKFSVFLKEIALTKNLQDLATTLSEVE
QEKQEEVWKTFTDILEQFATIFGQEKLSLDDFLALLHSGMSLSQYRTVPATVDVVTVKSYDLIEPHTAPF
VYAIGLTQSNFPKISQNSSLLTDEERQNLNDATEEGGHFDIASQENLKKNHYTMLSLFNSATKELVLSAP
QLFNESEDKESPYLQELIDFGVPLREKGMNSLGEDKEDIGNYKALLSRVVAYNQQGEMEMTKQDLTFWSV
LVRYLRKKLDQQGLEIPTITDSLSTKTLSKDVLQALYPADQPLKLSASALTTFYNNQYSYFLRYVLGLEE
EESIHPDARHHGNYLHRIFERLMKLPGEESFDQKLNQAINETSQEREFEALYQEDAEARYTLEILLDIAR
STAPILRHNSAIQVIKEEENFGGKDNFQLQIDNGRSIFVRGIIDRIDRLSDGGSLGVVDYKSSATQFDIP
HFYNGLSPQLPTYLAALKRIAPHEGEQPIFGAMYLHMQEPVQDLMAVKNLDDAVVEASKALKYQGLFSEK
EKSHLAEGYNKNKANLYSDEELQLLLDYNKYLYKKAAETILSGRFAINPYTEDGRSVQGDQLKAITGFEA
DRHMGQARRLEKLPAKEKKELFLTLM
>gnl|CDD|274292 TIGR02775, probable_conjugal_transfer_protein_TrbG, P-type conjugative transfer protein TrbG. The TrbG protein is found in the trb locus of Agrobacterium Ti plasmids where it is involved in the type IV secretion system for plasmid conjugative transfer. TrbG is a homolog of the F-type TraK protein (which is believed to be an outer membrane pore-forming secretin, TIGR02756) as well as the vir system VirB9 protein [Cellular processes, Conjugation]
GAVVYPYGAALPSIVCAPLQVCDIALQPGEQLNNILAGDTVRWKVEPTLSGSGDNARTHVIVKPSDVGLE
TSLVITTNRRTYHLKLKSREKKYMPSVGFDYPEDAKAALASINAKAEAAAPPGTGLPLEQLSFRYSVSGS
APWRPVRVYDDGEKTYIEFPRSINQGELPPLFVVGPDGRNELVNYRVKGDYYIVDRLFKAAVLRLG
>gnl|CDD|274293 TIGR02776, ATP-dependent_DNA_ligase, DNA ligase D. Members of this protein family are DNA ligases involved in the repair of DNA double-stranded breaks by non-homologous end joining (NHEJ). The system of the bacterial Ku protein (TIGR02772) plus this DNA ligase is seen in about 20 % of bacterial genomes to date and at least one archaeon (Archeoglobus fulgidus). This model describes a central and a C-terminal domain. These two domains may be permuted, as in genus Mycobacterium, or divided into tandem ORFs, and therefore not be identified by this model. An additional N-terminal 3'-phosphoesterase (PE) domain present in some but not all examples of this ligase is not included in the seed alignment for this model; it only represents the central ATP-dependent ligase domain and the C-terminal polymerase domain. Most examples of genes for this ligase are adjacent to the gene for Ku [DNA metabolism, DNA replication, recombination, and repair]
TRNGHDWTKRFPEIVKALALLKLLPAWIDGEIVVLDERGRADFAALQNALSAGASRPLTYYAFDLLFLSG
EDLRDLPLEERKKRLKQLLKAQDEPAIRYSDHFESDGDALLESACRLGLEGVVSKRLDSPYRSGRSKDWL
KLKCRRRQEFVITGYTPPNRRFGALLVGVYEGGQLVYAGKVGTGFGADTLKTLLARLKALGAKASPFSGP
AGAKTRGVHWVRPSLVAEVEYAGITRDGILREASFKGLREDKPAEEVTLETPQRHAAAKRKRSAALVAGV
RITHPDKVLWPKEGITKLDLAVYYAEVGDWMLPFLKGRPLSLIRCPDGIGGECFFQKHAPDYAPPFVASF
KDGDEKEYLVCNDAEGLLWLAQQGALEFHIWGQTIDSLDKPDRIVFDLDPPPGVAFKLAVEAAQLMKQLL
DELGLVSFVKTSGGKGLHVVVPLRPNTFTWDETKLFAKAIAEYLARQFPERFTTEMGKKNRVGRIFIDYL
RNARGKTTVAPYSPRAREGGPVSTPLTWDELASLDLSPAQFTITNVPERLRESGDPWADYAD
>gnl|CDD|131824 TIGR02777, LigD_PE_dom, DNA ligase D, 3'-phosphoesterase domain. Most sequences in this family are the 3'-phosphoesterase domain of a multidomain, multifunctional DNA ligase, LigD, involved, along with bacterial Ku protein, in non-homologous end joining, the less common of two general mechanisms of repairing double-stranded breaks in DNA sequences. LigD is variable in architecture, as it lacks this domain in Bacillus subtilis, is permuted in Mycobacterium tuberculosis, and occasionally is encoded by tandem ORFs rather than as a multifuntional protein. In a few species (Dehalococcoides ethenogenes and the archaeal genus Methanosarcina), sequences corresponding to the ligase and polymerase domains of LigD are not found, and the role of this protein is unclear [DNA metabolism, DNA replication, recombination, and repair]
LEEYRRKRDFNKTPEPSGTAARPSGNQAIFVVQKHHASRLHYDFRLELDGVLKSWAVPKGPSLDPADKRL
AVHVEDHPLDYADFEGTIPKGEYGAGTVIVWDRGTWEPEGDPDKALKKGHLKFELHGEKLKGGWALVRTK
RPGEKENWLLIKEDDA
>gnl|CDD|274294 TIGR02778, ligD_pol, DNA ligase D, polymerase domain. DNA repair of double-stranded breaks by non-homologous end joining (NHEJ) is accomplished by a two-protein system that is present in a minority of prokaryotes. One component is the Ku protein (see TIGR02772), which binds DNA ends. The other is a DNA ligase, a protein that is a multidomain polypeptide in most of those bacteria that have NHEJ, a permuted polypeptide in Mycobacterium tuberculosis and a few other species, and the product of tandem genes in some other bacteria. This model represents the polymerase domain
VRITNPDKVLWPAEGITKLDLADYYAAVAPFMLPHLRGRPLSLLRCPDGIGGECFFQKHLPQGAPPFVVS
AEVEESDGETYLVINDAEGLLWLVQQGALEFHIWGARIDAPEKPDRIVFDLDPGPGVAWKLVVEAAQLIR
ELLDELGLESFVKTSGGKGLHVYVPLRPTLSWDEVKDFAKALAQALAQQMPDRFTAEMSKKNRVGKIFVD
YLRNARGKTTVAPYSLRAREGATVSTPLTWDELDS
>gnl|CDD|274295 TIGR02779, NHEJ_ligase_lig, DNA ligase D, ligase domain. DNA repair of double-stranded breaks by non-homologous end joining (NHEJ) is accomplished by a two-protein system that is present in a minority of prokaryotes. One component is the Ku protein (see TIGR02772), which binds DNA ends. The other is a DNA ligase, a protein that is a multidomain polypeptide in most of those bacteria that have NHEJ, a permuted polypeptide in Mycobacterium tuberculosis and a few other species, and the product of tandem genes in some other bacteria. This model represents the ligase domain
LATLVTTPPTGDDWRYEVKYDGYRCLARIEGGKVRLISRNGHDWTEKFPILAAALAALPILPAVLDGEIV
VLDESGRSDFSALQNRLRAGRDRPATYYAFDLLYLDGEDLRDLPLSERKKLLEELLKAIKGPLAPDRYSV
HFEGDGQALLEAACRLGLEGVVAKRRDSPYRSGRSADWLKLKCRRRQEFVIGGYTPPNGSRSGFGALLLG
VYEGGGLRYVGRVGTGFSEAELATIKERLKPLESKPDKPGAREKRGVHWVKPELVAEVEFAGWTRDGRLR
QASFVGLREDKPASEVTR
>gnl|CDD|131827 TIGR02780, TrbJ_protein, P-type conjugative transfer protein TrbJ. The TrbJ protein is found in the trb locus of Agrobacterium Ti plasmids where it is involved in the type IV secretion system for plasmid conjugative transfer. TrbJ is a homolog of the F-type TraE protein (which is believed to be an inner membrane pore-forming protein, TIGR02761) as well as the vir system VirB5 protein
RPLEAKAALLLAASVALLPAPAGAPVTCINCANFSQQILTAAESVEQLNNQIQQLQNQIQRYENQLKNTM
SLPANIWNRLESSLQKLTNIISQAQALAYDIANLDDIFSQLYQGYDSYAASSGSDRQNMSDAYARWAQTT
RDTAEDALSMAGLQTGNLAEDNATLDQLQSLSQSASGQLQALQAGNQLAAQQSKQLQKLRALLAAQIQAQ
STYMASEQAREDVTQQQRRQFLARRGTYTPGLVTGW
>gnl|CDD|274296 TIGR02781, Protein_virB9, P-type conjugative transfer protein VirB9. The VirB9 protein is found in the vir locus of Agrobacterium Ti plasmids where it is involved in a type IV secretion system . VirB9 is a homolog of the F-type conjugative transfer system TraK protein (which is believed to be an outer membrane pore-forming secretin, TIGR02756) as well as the Ti system TrbG protein [Cellular processes, Conjugation]
KLLIALLLLTLAIPAYALNTPRGSSYDSRIRTVVYNPDDVVRVVTSYGYSTTIEFADDETIKTVAVGDSK
AWEVTPNGNKLFIKPTEKDWKTNMTVVTNKRSYVFDLTSRDGLDSEVQDLAYSVRFRYPAEEAEADADLA
KLAEAKQSQPIANGLGPEDVNWNYTFSGSASIAPIEAFDDGRFTYFKFPNNKEIPAIFIVDEDGKESLVN
YRVEGNYVVVQGVAKKLVLRYGDKVVGVFNTAF
>gnl|CDD|274297 TIGR02782, conjugal_transfer_protein, P-type conjugative transfer ATPase TrbB. The TrbB protein is found in the trb locus of Agrobacterium Ti plasmids where it is involved in the type IV secretion system for plasmid conjugative transfer. TrbB is a homolog of the vir system VirB11 ATPase, and the Flp pilus sytem ATPase TadA [Cellular processes, Conjugation]
MLRRALGPEIAAALDDPGVVEIMLNPDGRLWVERLGSGMSPLGEMSPADAQRIIGLVADYLGTEVDRDKP
IVEGELPLDGSRFEGLIPPVVAAPSFAIRKKAVAVFTLDDYVEAGIMTAAQRDVLREAVLARKNILVVGG
TGSGKTTLANALLAEIAKNDPTDRVVIIEDTRELQCAAPNVVQLRTSDDAISMTRLLKATLRLRPDRIIV
GEVRGGEALDLLKAWNTGHPGGIATIHANNAKAALDRLEQLIQEVSVTPMQTLIAEAVDLVIFIARTPAG
RRVQEIAKVKGFDDGNYIT
>gnl|CDD|131830 TIGR02783, probable_conjugal_transfer_protein_TrbL, P-type conjugative transfer protein TrbL. The TrbL protein is found in the trb locus of Agrobacterium Ti plasmids where it is involved in the type IV secretion system for plasmid conjugative transfer. TrbL is a homolog of the F-type TraG protein (which is believed to be a mating pair stabilization pore-forming protein, pfam07916) as well as the vir system VirB6 protein [Cellular processes, Conjugation]
AQNVGVLDQLLSLFHTAADIWEGRILIAALDLFWLLAVIEIVWLGLRLALRKADLEDLLAELVKKILVIG
FFLFILTNATAWIGAIINSLAQIGAGALGSSTSLSPGNIFDNGLDIASKVLDSASQIFSPIDLIVVLLGA
LVIVLVFAFIAVEFVVTLVEAYLVLNAGVILLGFGGSRWTRDFAWNYLKYALSVGVKLFVLTLIAGIGSS
FFAQFHTALPAGTIGIQALLVVVGASVVILGLVKTIPPIAASLVSGASVMGAGGAVAAAAAVAGVAAAGG
AALGAGASSAMAGASGAA
>gnl|CDD|274298 TIGR02784, ATP-dependent_nuclease_subunit_A, double-strand break repair helicase AddA, alphaproteobacterial type. AddAB, also called RexAB, substitutes for RecBCD in several bacterial lineages. These DNA recombination proteins act before synapse and are particularly important for DNA repair of double-stranded breaks by homologous recombination. The term AddAB is used broadly, with AddA homologous between the alphaproteobacteria (as modeled here) and the Firmicutes, while the partner AddB proteins show no strong homology across the two groups of species [DNA metabolism, DNA replication, recombination, and repair]
ARQAQAADPAASAWVSANAGSGKTHVLTQRVIRLLLAGTEPSKILCLTYTKAAAAEMQNRVFKRLGEWAV
LDDADLRARLEALEGKRPDAAKLAEARRLFARALETPGGLKIQTIHAFCEALLHQFPLEANVAGHFSVID
DRAAATLLEEARRALLAGPAAPDDALADALATVLEAAGETGLEALLAEIVARRDALMAFLDEAGGEGAEA
RLRRALGLAPGDTAEDLLEAVWPLPGLPRLALALIAALLKSGGGSKDAAAALSQLREAAAEPDPVARLDL
LLGAFLTSKGEPKSASFVIKKAIQKSLPDLAEALEDAASRVEALRERLRALRMAQRTLAALRLAARLLQR
YARLKKARGLLDFNDLIERTVALLARPGAGAWVHYKLDRGIDHILVDEAQDTSPEQWDIIQALAEEFFSG
EGARSGVERTIFAVGDEKQSIYSFQGADPERFAEERREFSRKVRAVGRKFEDLSLNYSFRSTPDVLAAVD
LVFADPENARGLSADSDAPVHEAFRDDLPGRVDLWDLISKEEGEEPEDWTDPVDELGERAPEVRLAERIA
AEIRAWLDRGTPIPGRGRAVRPGDILVLVRKRDAFFSALIRALKRRGIPVAGADRLKLTSHIAVKDLMAL
GRFVLQPEDDLSLAALLKSPLFGLDEDDLFRLAAGRSGGSLWAALRRREAEFAATLAVLRDWLSLADFLT
PFEFYARLLGRDGGRRKLLARLGAEAEDILDEFLSQALAYERTGLPGLQAFLSWLEADDPEIKREMDQAR
DEVRVMTVHGAKGLEAPVVFLVDTGSKPFASQRAPLLLATGGSGGKAPLWRPASAFDPSLSAAARERLKE
RAEDEYRRLLYVAMTRAEDRLIVCGYRGKRESPKDSWHALVKRALAAAGIAWQEPHPAQGKAEWRLRFTR
RDWDPVGLPVEAAQTDTLEALPDWLRAPAPAEPALPRPLAPSGLGGAIDSALPGEAVRSSLGTQAPAFAL
LRGTLLHRLLQHLPDLPPEEREDAARRYLARSAADWPEAEREALLAAVLAVLDDPRLAPVFAPGSRAEVA
IMGTLKEGGQQLAVSGQIDRLAVDRDRVLIVDYKTNRPVPATAEEVPPAYLRQLALYRALLRPLYPGRAV
EAALLWTEAPKLMPL
>gnl|CDD|274299 TIGR02785, ATP-dependent_helicase/nuclease_subunit_A, helicase-exonuclease AddAB, AddA subunit, Firmicutes type. AddAB, also called RexAB, substitutes for RecBCD in several bacterial lineages. These DNA recombination proteins act before synapse and are particularly important for DNA repair of double-stranded breaks by homologous recombination. The term AddAB is used broadly, with AddA homologous between the Firmicutes (as modeled here) and the alphaproteobacteria, while the partner AddB proteins show no strong homology across the two groups of species [DNA metabolism, DNA replication, recombination, and repair]
QWTDEQWQAIYTRGQDILVSASAGSGKTAVLVERIIRKITRGVDVDRLLVVTFTNAAAREMKERIAEALE
KELVQEPNSKHLRRQLALLNTANISTLHSFCLKVIRKHYYLLDLDPSFRILTDTEQLLLIKEVLDDVFEE
EYYKEDKEAFFELVDNFSGDRSDDGLRDLILQLYDFSRSTPNPEKWLNNLAEAYEVKEKFTIESLKLQQQ
IKELLKNELEGLQEKLQRALELFMAEDGLAPRLENFQLDLQNIDELIQESLAQADWNELRKAVAAFKFKN
LKAAKGDEEDADLLEEADKLREEAKKQLEKLKTDYFTRSEEDHLRIMQEMKPVVKTLVQLVKDFIERFGA
EKREKNILDFSDLEHYALQILTNENESPSEAAEFYREKFHEVLVDEYQDTNLVQESILQLVKRGPEEEGN
LFMVGDVKQSIYRFRQADPLLFLEKYHRFAQEGEEHGKRIDLAENFRSRAEVLDTTNFLFKQLMDEEVGE
IDYDEEAQLKFGAAKYPENPDNKTEELLYEKLLIEEAEEEEIDEEAEILDKAQQEATMVAERIKALIKEG
FKVYDKKTGTYRPVTYRDIVILTRSRGWNLQIMEEFKKYGIPVFANDAENYFQTTEVRVMLSLLRVIDNP
YQDIPLVAVLRSPIVGFDENELALIRLENKDSSYYEAVKDYVKAGLIEDELYEKLNTFLDSLQKWREFAR
THSVSELIWKIYNDTGYYDYVGGLPGGKQRQANLYALYERARQYESTSFKGLFQFIRFIERMQERQKDLA
SAVAVGEAENAVRLMTIHKSKGLEFPVVFVLGMGKQFNKQDLNSSYLLDRQLGLGIKYIDPQERLSYPSL
PKVAIKQKMKRELLSEEMRVLYVALTRAKEKLILVGSVKDEKKELKKWLAALAQSDWLLPENDRLQARNY
LDWIGPALARHRDIKLLGDDAGVSIHDELTKDPANFAVEVIDSYDLLAEELEERMDEKSEQLEALADKNQ
STGDKEFREKLREQLSYDYPHQAATETPAKQSVSEIKRIFEDEDEGSERAPVKQSRGKSISLERPKFLTK
TKGLTAAEIGTATHLVMQHIDLSKDPSEEELQQTIDRLVKKELLTEEQAEKIDIDKIVAFFDTPLGKQIL
KAKEVLRREPFFSMLISAEIYFDAHDEADEEDILVQGIIDGYYETEDGLYLFDYKTDHVEGHGFEGAINQ
LKERYRGQLQLYEKALEEIYKKKVKGKYLYLLDGDHVIDV
>gnl|CDD|274300 TIGR02786, conserved_hypothetical_protein, double-strand break repair protein AddB, alphaproteobacterial type. AddAB is a system well described in the Firmicutes as a replacement for RecBCD in many prokaryotes for the repair of double stranded break DNA damage. More recently, a distantly related gene pair conserved in many alphaproteobacteria was shown also to function in double-stranded break repair in Rhizobium etli. This family consists of AddB proteins of the alphaproteobacteial type [DNA metabolism, DNA replication, recombination, and repair]
RVFSIPPGRPFLDALAEGLLKGRLVAGFEADGDDPLALADATIYVPTRRAARALREAFVDVLDGRAALLP
RIRPLGDVDEDEALFAAEGPAILDLPPAISPLERLLELARLIRAWRDKLVEDVLAPAGPADAIWLARDLA
DLMDEMETEGVDWSKLDDLAEGDLARHWQVTLKFLEIVTRAWPKRLAELGRSNPAARRNRLLRALAARWA
TNPPEGPVIAAGSTGSIPATADLLAVVARLPQGAVVLPGLDLDMDEEAWQALGPAGTDPPSVFGHPQYGL
KRLLDRLGVSRKEVREWGPADRGLRKRERLVSEALRPAETTDRWGSQREQPAEAGIAEAFANLSLIEAAN
EREEALAIALALREAVEDPGKTAALVTPDRALARRVAAELKRFGIDADDSAGRPLSLTPPAVLLRLLAEA
VFAPLDPVALLSLLKHPLVRLGEERDDWRAAAELLELVALRGGTPRAGILALPAFFERRLLALGDDPEVP
AWHSALPEQSIEAARPLCELLEIAIEPLESLAGRREELDAELAEATVELMEALSRDEEGWLAALYEGEAG
HKLASLFAELLSSAHGLDFDARDWPDVLQALMATEAVRPRDGGHPRIFIWGALEARLQTADLVVIGGLNE
GVWPPAPRNDPFLSRPMRHELGLPPPERRIGLSAHDFQQALGAKEVVLTRAARSGGAPAVPSRWLQRLEA
LAGADVLEEMRRRGERYLHWARALDEPQDVAPATRPAPRPPVADRPRHFSVTEIETLRRDPYAIYARHIL
KLRPLDPLDRDPEAADRGTLIHDILERFVREYPDPLPADAADALRKIGRAEFASLNLPPTAEALWWPRFA
RAADWFADWERARRLDVRRIFAEARGRKELVGERGFTLSGRADRIDRTPDGSAAILDYKTGAPPSGKQVR
AGLSPQLALEAALLMRGAFKDIGAPTPANLYYVRLGGNGPVGEESILSEKGKGGKEPQDAPDLAEEAWER
LIQLIRAYDDPDQGYTSRALPFGKKEYYGDYDHLARVDEWS
>gnl|CDD|131834 TIGR02787, Transcriptional_regulator, GTP-sensing transcriptional pleiotropic repressor CodY. This model represents the full length of CodY, a pleiotropic repressor in Bacillus subtilis and other Firmicutes (low-GC Gram-positive bacteria) that responds to intracellular levels of GTP and branched chain amino acids. The C-terminal helix-turn-helix DNA-binding region is modeled by pfam08222 in Pfam [Regulatory functions, DNA interactions]
LLEKTRRINSILQKSAQTELPFNEMAEVLADVIDCNAYVISRKGRLLGYSLTYKTNNDRVEQFFQDRKFP
EEYNSALMMIYDTEANIPVDSELTVFPEESRDLFPKGLTTIVPIYGGGERLGTLILARSDKEFNDDDLVL
AEYAATVVGMELLRAQAEEIEEEARKKAAVQMAINTLSYSELEAVEHIFEELDGNEGLLVASKIADRVGI
TRSVIVNALRKLESAGVIESRSLGMKGTYIKVLNDKLIEEL
>gnl|CDD|274301 TIGR02788, conjugal_transfer_protein, P-type DNA transfer ATPase VirB11. The VirB11 protein is found in the vir locus of Agrobacterium Ti plasmids where it is involved in the type IV secretion system for DNA transfer. VirB11 is believed to be an ATPase. VirB11 is a homolog of the P-like conjugation system TrbB protein and the Flp pilus sytem protein TadA
FLDDEDVTEICINRPGEVWVEGPGGWQRFDVPDLTFSHLMRLARAIASFSKQSISEENPILSATLPGGER
VQIVIPPACENDTVSITIRKPSLVDFSLDDYEEKGFFDTVRAQSGTLSDNDEQLLELLDAGDIKEFLRLA
IASRKNIIISGGTGSGKTTFLKSLVDEIPKDERIITIEDTREIFLPHPNYVHLFYSKGGQGLAKVTPKDL
LQSCLRMRPDRIILGELRGDEAFDFIRAVNTGHPGSITTLHAGSPEEAFEQLALMVKSSQAGLGLDFAYI
VKLVREVIDIVVQINRRGGGRKITEVYF
>gnl|CDD|131836 TIGR02789, Nickel_transport_system_permease_protein_NikB, nickel ABC transporter, permease subunit NikB. This family consists of the NikB family of nickel ABC transporter permeases. Operons that contain this protein also contain a homologous permease subunit NikC. Nickel is used in cells as part of urease or certain hydrogenases or superoxide dismutases [Transport and binding proteins, Cations and iron carrying compounds]
MLNYILRRLLLLIPVVLAASLLAFILIHLGPSDPAEDYLRLSHIPPTDEAIADMRHSLGLDQPLYVQYFH
WLWNALHLDFGISYISDRPVLDEIARSLPATLELAGFALVIVVLVSVPLGILAARYRDRLPDHAVRFIIF
LGVSIPNFWLAFLLVWGFSVYLNLLPTNGAGTWQHLVLPAVTLALMSVSIYARLLRASMLDNMQERYVTY
ARVRGIKERWVIRRHILRNAILPMITALGMHIGELLGGTFVIENIFSWPGVGRYAISAIFNRDYPVIQCY
TLLMGLLFVFCNLIVDLFQALLDPRIRRKEGVHA
>gnl|CDD|131837 TIGR02790, Nickel_transport_system_permease_protein_nikC., nickel ABC transporter, permease subunit NikC. This family consists of the NikC family of nickel ABC transporter permeases. Operons that contain this protein also contain a homologous permease subunit NikB. Nickel is used in cells as part of urease or certain hydrogenases or superoxide dismutases [Transport and binding proteins, Cations and iron carrying compounds]
VVSALLIIAVLFLLAIFAPWIAPHDPLAQNLPMRLLGPSMEYWLGTDHLGRCIFSRLIFGARVSLGSALL
VLGLVLTIGLLIGGLAGYIGGRVDEAIMRVCDVFLSFPTIILSLAIVGILGPGLENVIIAIVLVHWAWYA
RMVRGMVVSLKQREFVLAARTSGASHWQIIRRHILPNILSPIIVLATLDIGHVILHIAGLSFLGLGIQPP
TPEWGAMLSEAKQYIWTQPLLMIYPGLAILISVMAFNLLGDALRDHLG
>gnl|CDD|274302 TIGR02791, conjugal_transfer_protein, P-type DNA transfer protein VirB5. The VirB5 protein is involved in the type IV DNA secretion systems typified by the Agrobacterium Ti plasmid vir system where it interacts with several other proteins essential for proper pilus formation. VirB5 is homologous to the IncN (N-type) conjugation system protein TraC as well as the P-type protein TrbJ and the F-type protein TraE
MKKHAISCALTAALAAASAAVAGIPVTDPASIANALAQAIEQMAALKTQYEQLSEQIEQYKQQYGSLTGN
RGMGDLLNDPALRRYLPFDWAAIYEGVLSGGYTGVMGDWASIYSTGRVYDSCTRYAANSDRASCEAKAVK
MAAADKALAERAYDAATKRLSNIEQLRQKINEAGDPKAIADLQARIQVEQAMIQNEQTRLQNLQMLQEAQ
DKLQNQRRAE
>gnl|CDD|131839 TIGR02792, Protocatechuate_45-dioxygenase_alpha_chain, protocatechuate 4,5-dioxygenase, alpha subunit. Protocatechuate (PCA) 4,5-dioxygenase is the first enzyme in the PCA 4,5-cleavage pathway that is an alternative to PCA 3,4-cleavage and PCA 2,3 cleavage pathways. PCA is an intermediate in the breakdown of lignin (hence the gene symbol ligA) and other compounds. Members of this family are the alpha chain of PCA 4,5-dioxygenase, or the equivalent domain of a fusion protein [Energy metabolism, Aerobic]
YDDVPGTRIFDAQQARKGYNLNQFCMSLMKAENRERFKADESAYLDEWNLTPAQKQAVLARDLNACIDEG
GNIYFLAKIGATDGKSFQQMAGSMTGMTEEEYRQMMIGGGRSPEGNR
>gnl|CDD|131840 TIGR02793, Putative_nickel-responsive_regulator, nickel-responsive transcriptional regulator NikR. Three members of the seed for this model, from Escherichia coli, Pseudomonas putida, and Brucella melitensis, are found associated with a nickel ABC transporter operon that acts to import nickel for use as a cofactor in urease or hydrogenase. These proteins, with characterized nickel-binding and DNA-binding domains, act as nickel-responsive transcriptional regulators. In the larger family of full-length homologs, most others both lack proximity to the nickel ABC transporter operon and form a separate clade. Several of the homologs not within the scope of this model, but rather scoring between the trusted and noise cutoffs, have been shown to bind nickel, copper, or both, and to regulate genes in response to nickel [Regulatory functions, DNA interactions]
QRVTITLDDDLLETLDRLIARRGYQNRSEAIRDLLRSGLQQEAAEQHGTACVAVLSYTYDHSKRDLPRRL
TQTQHHHHDLSVATLHVHLDHDDCLEVSVLKGDMGDVQHFADHVIAERGVRHGHLQVLP
>gnl|CDD|274303 TIGR02794, Protein_TolA, TolA protein. TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
RRAFLLSLLLHILLLGLLILGSLYHSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQ
KKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEA
ERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAA
AKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQNLYDDP
SFRGKTCRLRIRLAPDGTLLSVTKSSGDPALCQAALAAVAKAAKLPMPPSDPVYEEFKNINLTFKP
>gnl|CDD|188247 TIGR02795, Uncharacterized_protein_in_oprL_3'region, tol-pal system protein YbgF. Members of this protein family are the product of one of seven genes regularly clustered in operons to encode the proteins of the tol-pal system, which is critical for maintaining the integrity of the bacterial outer membrane. The gene for this periplasmic protein has been designated orf2 and ybgF. All members of the seed alignment were from unique tol-pal gene regions from completed bacterial genomes. The architecture of this protein is a signal sequence, a low-complexity region usually rich in Asn and Gln, a well-conserved region with tandem repeats that resemble the tetratricopeptide (TPR) repeat, involved in protein-protein interaction
EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYAPNAHYWLGEAYYAQGDYADAAKAFLAVVKKYPKS
PKAPDALLKLGMSLQELGDKEKAKATLQQVIKRYPGSSAAKLAQKRL
>gnl|CDD|131843 TIGR02796, Protein_TolQ, TolQ protein. TolQ is one of the essential components of the Tol-Pal system. Together with TolR, it harnesses protonmotive force to energize TolA, which spans the periplasm to reach the complex of TolB and Pal at the outer member. The tol-pal system proves to be important for maintaining outer membrane integrity. Gene pairs similar to the TolQ and TolR gene pair often number several per genome, but this model describes specificially TolQ per se, as found in tol-pal operons. A close homolog, excluded from this model, is ExbB of the ExbB/ExbD/TonB protein complex, which powers transport of siderophores and vitamin B12 across the bacterial outer membrane. The Tol-Pal system is exploited by colicin and filamentous phage DNA to enter the cell. It is also implicated in pathogenesis in several bacterial species [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
SILDLFLQASFVVKLVMLILLLASIISWAIIFQKFFIFRRARREAEEFEDRFWSGGDLEKLYNSLSNNKP
TSGLESIFCAGFKEFSRLKSKGELDPGVVIERIDRAMRVALNRESEKLESGLPFLATIGSTSPFIGLFGT
VWGIMHSFQAIGGSKNQATLAVVAPGIAEALIATAIGLFAAIPAVIAYNKLSTQVNKIEQRYENFADEFS
TILQR
>gnl|CDD|131844 TIGR02797, Biopolymer_transport_protein_ExbB, tonB-system energizer ExbB. This model describes ExbB proteins, part of the MotA/TolQ/ExbB protein family. The paired proteins MotA and MotB, TolQ and TolR, and ExbB and ExbD harness the proton-motive force to drive the flagellar motor, energize the Tol-Pal system, or energize TonB, respectively. Tol-Pal and TonB are both active at the outer membrane. Genomes may have many different TonB-dependent receptors, of which many of those characterized are involved in siderophore transport across the outer membrane [Transport and binding proteins, Cations and iron carrying compounds]
SPWGMFLAADIVVKAVMIGLALASVVTWTIWIAKSVELAGARRRLKRALKALGEARTLAEAQEALGDRGG
PAAALVRAAEEEMELSAAGLSDGEGIKERVASRLERIEAAAGRRMSRGTGVLATIGATAPFVGLFGTVWG
IMNSFIGISKSQTTNLAVVAPGIAEALLATAIGLVAAIPAVVIYNVFARSIAGYRALLADASAGVERLVS
R
>gnl|CDD|131845 TIGR02798, oxalocitramalate_aldolase, 4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase. Members of this protein family 4-carboxy-4-hydroxy-2-oxoadipate aldolase, also called 4-oxalocitramalate aldolase. This enzyme of the protocatechuate 4,5-cleavage pathway converts its substrate to pyruvate plus oxaloacetate. Protocatechuate is an intermediate in many pathways for degrading aromatic compounds, including lignin, fluorene, etc. Hara, et al. showed the LigK gene was not only a 4-carboxy-4-hydroxy-2-oxoadipate aldolase but also the enzyme of the following step, oxaloacetate decarboxylase
GIVVRNIERADLAAVDGLAAFGVATVHEAMGRVGLLAPYMRPIYTGARVCGTAVTVLLQPGDNWMMHVAA
EQIQEGDVVVAACTAECEDGYFGDLLATSFQARGCRGLIIDAGVRDVRDLTEMNFPVWSKAIHAKGTVKA
TLGSVNIPVVCANALVNPGDVVVADDDGVVVVPRANAGAVLDAAQAREANEEAKRVKLASGVLGLDMYKM
REPLEKAGLKYV
>gnl|CDD|274304 TIGR02799, Acyl-CoA_thioesterase_YbgC, tol-pal system-associated acyl-CoA thioesterase. The tol-pal system consists of five critical genes. Inner membrane proteins TolQ and TolR convert protomotive force to energy that is transduced through TolA to an outer membrane complex of TolB and Pal. The system is known to be required to maintain outer membrane integrity. In a system with several homologous parts, ExbB and ExbD transduces energy through TonB to a variety of outer membrane proteins, many of which are siderophore receptors. The tol-pal system therefore may also be involved in transport. This family consists of a protein nearly always found in operons with the genes of the tol-pal system. The significance of this thioesterase to the tol-pal system is unclear, but either of two observations may be relevant. First, Pal, or peptidoglycan-associated lipoprotein, has a conserved N-terminal cleavage and acylation that makes it a lipoprotein. Second, the tol-pal system is implicated not only in the import of certain organics but also in the maintenance of outer membrane integrity (by an unknown mechanism)
FRWPIRVYYEDTDAGGVVYHANYLRFMERARTEWLRALGFEQSALLEETGLVFVVRSMELDYLKPARLDD
LLTVTTRVVELKGASLVFAQEVRRGDTLLCEATVEVACVDASDMRPRRLPAELRAA
>gnl|CDD|274305 TIGR02800, Protein_TolB, tol-pal system beta propeller repeat protein TolB. Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The {beta}-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. E. coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggest that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi, Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
LAVSTPAAADLTIEITKGGASALPIAVAPFSNDGGGSPDANLGESIAEVIANDLKRSGLFSPVDKAGLPS
NPIAESQVNPAAWQALGADALVVGSVTPNGNGRYTVRFRLYDVVSGQLQLLGKQYTVTASQLRRVAHRIA
DAIYEKLTGERGAFSTRIAYVSKSGKSRRYELQVADYDGANPQTITRSREPILSPAWSPDGQKLAYVSFE
SGKPEIYVQDLATGQREKVASFPGMNGAPAFSPDGSKLAVSLSKDGNPDIYVMDLDGKQLTRLTNGPGID
TEPSWSPDGKSIAFTSDRGGSPQIYMMDADGGEVRRLTFRGGYNASPSWSPDGDLIAFVHREGGGFNIAV
MDLDGGGERVLTDTGLDESPSFAPNGRMILYATTRGGRGVLGLVSTDGRFRARLPLGNGDVREPAWS
>gnl|CDD|274306 TIGR02801, Protein_TolR, TolR protein. The model describes the inner membrane protein TolR, part of the TolR/TolQ complex that transduces energy from the proton-motive force, through TolA, to an outer membrane complex made up of TolB and Pal (peptidoglycan-associated lipoprotein). The complex is required to maintain outer membrane integrity, and defects may cause a defect in the import of some organic compounds in addition to the resulting morphologic. While several gene pairs homologous to talR and tolQ may be found in a single genome, but the scope of this model is set to favor finding only bone fide TolR, supported by operon structure as well as by score [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
LMSEINVVPYVDVMLVLLIIFMVTAPLLTQGVKVDLPKSSAKPLQSKDKKPITVSVDADGKIYLNDNKID
KDEQLDADELLAEIAAALAANPDTPVLIRADKTVPYGEVIKVMALLKQAGIEKVGLITE
>gnl|CDD|274307 TIGR02802, Peptidoglycan-associated_lipoprotein, peptidoglycan-associated lipoprotein. Members of this protein are Pal (also called OprL), the Peptidoglycan-Associated Lipoprotein of the Tol-Pal system. The system appears to be involved both in the maintenance of outer membrane integrity and in the import of certain organic molecules as nutrients. Members of this family contain a hydrodrophobic lipoprotein signal sequence, a conserved N-terminal cleavage and modification site, a poorly conserved low-complexity region, together comprising about 65 amino acids, and a well-conserved C-terminal domain. The seed alignment for this model includes only the conserved C-terminal domain
RVYFDFDSSDLKSEAQATLDAHAQYLKKNPSVRVTIEGHTDERGTREYNLALGERRANAVKDYLQSKGVS
ASQIETVSYGKEKPAALGHDEAAWAKNRRAVLVY
>gnl|CDD|131850 TIGR02803, Biopolymer_transport_protein_ExbD, TonB system transport protein ExbD, group 1. Members of this family are Gram-negative bacterial inner membrane proteins, generally designated ExbD, related to the TolR family modeled by TIGRFAMs TIGR02801. Members always are encoded next to a protein designated ExbB (TIGR02797), related to the TolQ family modeled by TIGRFAMs TIGR02796. ExbD and ExbB together form a proton channel through which they can harness the proton-motive force to energize TonB, which in turn energizes TonB-dependent receptors in the outer membrane. TonB-dependent receptors with known specificity tend to import siderophores or vitamin B12. A TonB system and Tol-Pal system often will co-exist in a single bacterial genome
NHEINVTPFIDVMLVLLIIFMVAAPLATVDVKVDLPASTAAPQPRPEKPVYVSVKADLSLFVGNDPVARE
TLGTALDALTEGDKDTTIFFRADKTVDYGDLMKVMNLLRQAGYLKIGLVGLE
>gnl|CDD|131851 TIGR02804, Biopolymer_transport_protein_ExbD, TonB system transport protein ExbD, group 2. Members of this family are Gram-negative bacterial inner membrane proteins, generally designated ExbD, related to the TolR family modeled by TIGRFAMs TIGR02801. Members always are encoded next to a protein designated ExbB (TIGR02797), related to the TolQ family modeled by TIGRFAMs TIGR02796. ExbD and ExbB together form a proton channel through which they can harness the proton-motive force to energize TonB, which in turn energizes TonB-dependent receptors in the outer membrane. TonB-dependent receptors with known specificity tend to import siderophores or vitamin B12. A TonB system and Tol-Pal system often will co-exist in a single bacterial genome
FEGLNIVPFIDIMLVLLAIVLIISTFIAQGKIQVNLPKASTAVAFKSDELKLLITITADNQLYFNDKPIS
LEELEAEIAQLNKDQKVTLKSDKEAKFQDFVTITDMLKAKEHENVQIVSMK
>gnl|CDD|131852 TIGR02805, Biopolymer_transport_protein_ExbB, tonB-system energizer ExbB, group 2. Members of this protein family appear to be the ExbB protein of an ExbBD proton-transporting membrane complex that, by means of TonB, energizes transport by TonB-dependent receptors. Note that this family represents one of at least two distinct groups TolQ homologs designated ExbB - see also TIGR02797. Each group associates with a distinct group of ExbD proteins, and a single species may have two ExbB/ExbD/TonB systems [Transport and binding proteins, Cations and iron carrying compounds]
DFLKQYSDYFIFGILGLMSIIALAMVIERYLFLRKISVAHYSTIHQLDIDLNRNLTVISIIGSNAPYIGL
LGTVIGIMVTFYQMGHGGGIDPSVIMLGLSLALKATALGLLVAIPSLVFYNALLRKVEVNRLAWKVLS
>gnl|CDD|131853 TIGR02806, Contains:_Clostripain_light_chain, clostripain. Clostripain is a cysteine protease characterized from Clostridium histolyticum, and also known from Clostridium perfringens. It is a heterodimer processed from a single precursor polypeptide, specific for Arg-|-Xaa peptide bonds. The older term alpha-clostripain refers to the most active, most reduced form, rather than to the product of one of several different genes. Clostripain belongs to the peptidase family C11, or clostripain family (see pfam03415) [Protein fate, Degradation of proteins, peptides, and glycopeptides, Cellular processes, Pathogenesis]
KLTIMVYADADNNLEESILNDIEEMKEGYKDNPNLNIIALVDRIPGYSNDEKVLGEDFEDTRLYKIEENK
AERIDGKNEFPEISTTSKYEANMGDAETLKKFIDFCKKNYEADKYMLIMANHGGGAKDDKDRAPRLNKAI
CWDDSNLDKNGEADCLYMGEISDHLTEDESVDLLAFDACLMGNAEVAYQYRPGNGGFEADTLVASAPVVW
GFGFKYDKIFDRIKAGGGDNGEDDLTLGGKEKIFDPATITNEELGALFVEEQRDSTHACGRTDQHLSCYD
LKKAEKVKKAIDALARNLSKENKKDAIEKLRGSGIHADLMHYFDEYDEGEWIEYPYFDLYDLCEKINKSD
EFNEKTKDLAKNAMKKLDELILYSFADKDFKGFKEGKNGISIFLPDGDKKYSDQYSGQAIPHWAIQRWYN
PIDTNAYGLNPGYGKLAWCKDGLDPEINKVGNWFELLDSWFDKDNDSLGGVNHYQW
>gnl|CDD|274308 TIGR02807, hypothetical_protein_LA_3189, CRISPR-associated protein Cas6, subtype MYXAN. Members of this protein family resemble the Cas6 proteins described by TIGR01877 in having a C-terminal motif GXGXXXXXGXG, where the single X of each GXG is hydrophobic and the spacer XXXXX has at least one Lys or Arg. Examples are found in cas gene operons of CRISPR regions in Anabaena variabilis ATCC 29413, Leptospira interrogans, Gemmata obscuriglobus UQM 2246, and twice in Myxococcus xanthus DK 1622. Oddly, an orphan member is found in Thiobacillus denitrificans ATCC 25259, whose genome does not seem to contain other evidence of CRISPR repeats or cas genes
PPVIDLLFPVRGGTVPADHAYMLFSALCGVLPALHERDDLGIQTLRGVPDNSGVLNLTRRSRLRIRIPVE
QVPLVLPLAGKSLDIGGHRLRLGAPSIRALQPASSLFARIVTFKHAEEPAAFLAVARRQLEALGIQARPI
LGRRRTVRIAGFTVVGFALELHGLSAEDSLRLQEQGLGGRRKMGCGLFLP
>gnl|CDD|131855 TIGR02808, hypothetical_protein_VF_1902, TIGR02808 family protein. This very small protein (about 46 amino acids) consists largely of a single predicted membrane-spanning region. It is found in Photobacterium profundum SS9 and in three species of Vibrio, always near periplasmic nitrate reductase genes, but far from the periplasmic nitrate reductase genes in Aeromonas hydrophila ATCC7966 [Hypothetical proteins, Conserved]
MSTLESTIWHVLGYGAMPFIILSGFVAVAVTSILLLNAFGDK
>gnl|CDD|131856 TIGR02809, phasin_3, phasin family protein. Members of this protein family are encoded in polyhydroxyalkanoic acid storage system regions in Vibrio, Photobacterium profundum SS9, Acinetobacter sp., Aeromonas hydrophila, and several species of Vibrio. Members appear distantly related to the phasin family proteins modeled by TIGR01841 and TIGR01985
EVFKTFSEQTEKFAAPYTKFNKLLAKNVEQLTELQLAAARTYSELGLNQLKAAGEVKDAQSLAAFNTQQL
ETLSKLSQQMMDDSKKLNTLAQQFKDDVEALAAENIKKVT
>gnl|CDD|274309 TIGR02810, Putative_tagatose_6-phosphate_kinase_gatZ, D-tagatose-bisphosphate aldolase, class II, non-catalytic subunit. Aldolases specific for D-tagatose-bisphosphate occur in distinct pathways in Escherichia coli and other bacteria, one for the degradation of galactitol (formerly dulcitol) and one for degradation of N-acetyl-galactosamine and D-galactosamine. This family represents a protein of both systems that behaves as a non-catalytic subunit of D-tagatose-bisphosphate aldolase, required both for full activity and for good stability of the aldolase. Note that members of this protein family appear in public databases annotated as putative tagatose 6-phosphate kinases, possibly in error [Energy metabolism, Sugars]
LELARRHKAGEPRGIYSVCSAHPLVLEAALRRARASGTPVLIEATSNQVNQFGGYTGMTPADFRDFVYTI
ADRIGFPRERLILGGDHLGPNPWQHLPAEEAMEKAAALVDAYVEAGFTKIHLDASMSCAGDPAPLPDATI
AERAARLCAVAESAATEEQGETKPVYVIGTEVPVPGGALETLQTLAVTTPEAARETLEAHRKAFAQRGLD
DAWPRVIALVVQPGVEFDHSNVIDYQPERAQALSQVIETTPGLVFEAHSTDYQTPAALRALVRDHFAILK
VGPALTFALREALFALAQIEDELIPAEARSHLREVIEQVMLAEPGYWQKYYHGDDAEQRLDRHYSYSDRI
RYYWPHPRIAAAVETLMANLDGQPIPLTLLSQYLPDQYAAVRAGELAPKPRELIIDKIRDVLADYAAACG
>gnl|CDD|274310 TIGR02811, formate_dehydrogenase_accessory_protein_FdhX, formate dehydrogenase region TAT target. Members of this uncharacterized protein family are all small, extending 70 or fewer residues from their respective likely start codons. All have the twin-arginine-dependent tranport (TAT) signal sequence at the N-terminus and a conserved 20-residue C-terminal region that includes the motif Y-[HRK]-X-[TS]-X-H-[IV]-X-X-[YF]-Y. The TAT signal sequence suggests a bound cofactor. All members are encoded near genes for subunits of formate dehydrogenase, and may themselves be a subunit or accessory protein [Unknown function, General]
MSDDQKADPSRRDLLKGLGVGAAAGAVAAATGRVASASVDSEPSEPEKKKKGYRETQHIRDYYRTL
>gnl|CDD|163028 TIGR02812, Fatty_acid_metabolism_regulator_protein, fatty acid metabolism transcriptional regulator FadR. Members of this family are FadR, a transcriptional regulator of fatty acid metabolism, including both biosynthesis and beta-oxidation. It is found exclusively in a subset of Gammaproteobacteria, with strictly one copy per genome. It has an N-terminal DNA-binding domain and a less well conserved C-terminal long chain acyl-CoA-binding domain. FadR from this family heterologously expressed in Escherichia coli show differences in regulatory response and fatty acid binding profiles. The family is nevertheless designated equivalog, as all member proteins have at least nominally the same function [Fatty acid and phospholipid metabolism, Biosynthesis, Fatty acid and phospholipid metabolism, Degradation, Regulatory functions, DNA interactions]
VIKAKSPAGFAEEYIVESIWNNRFPPGSILPAERELSELIGVTRTTLREVLQRLARDGWLTIQHGKPTKV
NNFWETSGLNILETLIRLDGESVPSLIDNLLSARTNISAIYIRYAFKNNPEKALEVLANANELEDTAEAF
TEFDYQLFRGLAFASGNPIYGLILNGLKGLYTRIGRYYFANPEARELALQFYKELQALCKAGNHDEVPDC
IRQYGIESGEIWHQMQDELPQDLSE
>gnl|CDD|274311 TIGR02813, omega-3_polyunsaturated_fatty_acid_synthase_PfaA, polyketide-type polyunsaturated fatty acid synthase PfaA. Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD
NKRLKDMPIAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYDSDKSEADKSYCKRGGFL
PEVDFNPMEFGLPPNILELTDISQLLSLVVAKEVLNDAGLPDGYDRDKIGITLGVGGGQKQSSSLNARLQ
YPVLKKVFKASGVEDEDSEMLIKKFQDQYIHWEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSL
AAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKR
LEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDV
AEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKLDIEN
SPFYLNTETRPWMQREDGTPRRAGISSFGFGGTNFHMVLEEYSPKHQRDDQYRQRAVAQTLLFTAANEKA
LVSSLKDWKNKLSAKADDQPYAFNALAVENTLRTIAVALARLGFVAKNADELITMLEQAITQLEAKSCEE
WQLPSGISYRKSALVVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGKGALSPVLY
PIPVFNDESRKAQEEALTNTQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDY
MMLAFSRGQAMAAPTGEADIGFMYAVILAVVGSPTVIANCIKDFEGVSIANYNSPTQLVIAGVSTQIQIA
AKALKEKGFKAIPLPVSGAFHTPLVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKN
HMLQSVHFSEQLEAMYAAGARVFVEFGPKNILQKLVENTLKDKENELCAISINPNPKGDSDMQLRQAAVQ
LAVLGLELTEIDPYQAEKRPPAATSPMNIKLNAANYISPATRKKMDDSLNDGWTIKQATSVPQVVEKIVE
KIVEKERIVEVERIVYLTADVKVFDGSVADGTVANGQAPAQVAVNTADQANSIERSLSAFFDAQQQAANL
HQQFLAIPQQYGDTFDALMSEQAKMASLGIAIPESLQRSMELFHQHQAETLKVHEQYLNLQTDSNIVKLS
PLATQAPVIKSVVTQAPVVQVTISVAPAAPVLPAVVSPPVVSAAPAQSVATAVAMAPVAEVPIAVPVQQS
VDYMPSVAQAAAPQASVNDSAIQQVMMEVVAEKTGYPTEMLELEMDMEADLGIDSIKRVEILGSVQEIIN
DLPELNPEDLAELRTLGEIVNYMQSKVSAAVASAPVNTAVSSTDLIQIQNVMLEVVADKTGYPTEMLELE
MDMEADLGIDSIKRVEILGTVQDTLPDLPELSPEDLAECRTLGEIVSYMQSKVPVASAAVAAIAPNATAN
ASAAIDLDYIQSTMMTVVADKTGYPTEMLELEMDMEADLGIDSIKRVEILGTVQDTLPDLPELNPEDLAE
CRTLGEIVSYMQSKVPVAPIAVVANAQAAPAIVASAVSSAPAIDLDYIQSTMMTVVADKTGYPTEMLELA
MDMEADLGIDSIKRVEILGTVQDTLPDLPELNPEDLAECRTLGEIVSYMQSKVPPVADVTVETSTLAAES
APAIDLNDYIQSTMMTVVADKTGYPTEMLELAMDMEADLGIDSIKRVEILGTVQDQLPDLPELNPEDLAE
CRTLGEIVAYMQSKVSPTDATDPKVATTVPAAVEAIARTVETAVNLPPHSEVELKKLPAVNKLVQDVTGE
GKQSGANALVIDDDGHNAGVLAEKLIAAGWQVAVVRSPWVVSHSASPLASAIASVTLGTIDDTSIEAVIK
DIEEKTAQIDGFIHLQPQHKSVADKVDAIELPEAAKQSLMLAFLFAKLLNVKLATNARASFVTVSRIDGG
FGYSNGDADSGTQQVKAELNQAALAGLTKTLNHEWNAVFCRALDLAPKLDADKAATAVNDELLDIDGSIV
EVGHDTDNLSNGSRLTLSAVVTDTAIAKGSNAALNSDDVFLVTGGAKGVTFECALELAKQCQAHFILAGR
SSFDDNEPSWAQGKDENELKKAAIQHLQASGEKPTPKKVDALVRPVLSSLEIAQALAAFKAAGASAEYAS
ADVTNSVSVAATVQPLNKTLQITGIIHGAGVLADKHIQDKTLEEFNAVYGTKVDGLLSLLAALNAENIKL
LALFSSAAGFYGNTGQSDYAMSNDILNKAALQLKALNPSAKVMSFNWGPWDGGMVNPALKKMFNDRGVYV
IPLDAGAELFVSQLLSDTGAQLLVGTDMQGNDTAEDASVKKPQVSRLTARVPQPMAIRVMRTLDPKNMTF
IADHCIGGDKVLPTVCAIAWMREAAMVALGAFVGVADYKLLKGVIFDGSEATEYIDMILQLELTPLVVDT
KISTTNEQALISFHYRPQYTAVLVAERKEAPTAELFLPEALPELLPETVLSSIEEAGALYSNGTLFHGPR
LQGIKAVLAFDDQGLLAKCQLPAVASLDCGEFPPSPLNSGSQPFAEDILLQAMLVWARLKYGAASLPSSI
GEFVSYRPVSLGEKFYLKLDVVKSSGRSLVANIELYHQDGRLSSEMKSAKVTISKNLNDAFL
>gnl|CDD|274312 TIGR02814, omega-3_polyunsaturated_fatty_acid_synthase_PfaD, PfaD family protein. The protein PfaD is part of four gene locus, similar to polyketide biosynthesis systems, responsible for omega-3 polyunsaturated fatty acid biosynthesis in several high pressure and/or cold-adapted bacteria. Several other members of the seed alignment for this model are found in loci presumed to act in polyketide biosyntheses per se
LTAESLGSAAFREDYGVRYAYVAGAMANGIASAELVIAMGRAGILGFFGAGGLPLEEVEQAIHRIQQALP
GGPAYGVNLIHSPSDPALEWGLVDLLLRHGVRIVEASAFMQLTPALVRYRAKGLHRDADGRVVIRNRLIA
KVSRPEVAEAFMSPAPAHILQKLLAEGRITREEAELARRVPVADDICVEADSGGHTDNRPLVVLLPAIIR
LRDTLMRRYGYRKPIRVGAAGGIGTPEAAAAAFMLGADFIVTGSVNQCTVEAGTSDNVKKLLAKADVQDT
AYAPAGDMFELGVKLQVLKRGTLFPARANKLYELYRRYDSLEALPAATRAQLEKKYFKRSLDDVWEETRA
YYIGRHDPAEIERAERDPKHKMALVFRWYFGHSSRWANTGEEERRVDYQIWCGPAIGAFNQWVKGTYLED
WRNRHVDQIAKHLMRGAAFLLRLR
>gnl|CDD|131862 TIGR02815, agaS_fam, putative sugar isomerase, AgaS family. Some members of this protein family are found in regions associated with N-acetyl-galactosamine and galactosamine untilization and are suggested to be isomerases
NATHTAREIRQQPALWRRLLTIIQALRPALNAFLEPLLARENLRIVLTGAGTSAFIGDALAPWLASHTGL
NVSAVPTTDLVSNPRQYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAI
NRSNAFALLMPAESNDRSFAMTSSFSCMTLATLAVLGPETIESQTEERFADAALCILESGQWDFSEGVLG
YAPWERIVYLGSGGLQGLARESALKVLELTAGKVMAFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQ
YDLDLLAELRRDNQAGRVVAISAESSDIVAAGDHFILPPSRHFIDVELAFPYLIFAQTLAFEQSLALGNT
PDNPCPTGEVNRVVQGVTIHPF
>gnl|CDD|131863 TIGR02816, omega-3_polyunsaturated_fatty_acid_synthase_PfaB, PfaB family protein. The protein PfaB is part of four gene locus, similar to polyketide biosynthesis systems, responsible for omega-3 polyunsaturated fatty acid biosynthesis in several high pressure and/or cold-adapted bacteria. The fairly permissive trusted cutoff set for this model allows detection of homologs encoded near homologs to other proteins of the locus: PfaA, PfaC, and/or PfaD. The likely role in every case is either polyunsaturated fatty acid or polyketide biosynthesis
SHYWFSEFHKARVAAINFNANGDQASSLVLTQASGLLAAKSLLNAQRLFFILPGLNEIEISAQIEQLKQQ
LADLPVTEVNDLSLECNAALIAIMTDNLANADKDTSRDAKPAISLPQAVIQAASVSAAKQEISAINDALP
ALFAEKSNATSTNKGLIHYKTPAGSCFSLAPLGSNNDNAKAGLAFVYPGVGTVYADMFNDFHQYFPALFA
KLEREGDLKAMLQAEDIYGEDPKHAAEMSLGDLAIAGVGSSYLLTQLLCDEFAIKPDFALGYSKGEASMW
ASLGVWKNPHALIEKTQTDPIFTSAISGKLTAVREAWQLDDTAAEIQWNSFVVRCEAAPIEALLKDFPHA
YLAIIQGDTCVIAGCEAQCKALLAALGKRGIAANRVTAMHTQPALQEHQNVMDFYLQPLCAELPMDIKFI
SAADLLAKNQNSEQAIDSQSIANSIADTFCQTLDFTALIHHAQEQGAKLFVEIGADRQNCTLIDKINKQD
GASSEQHQPCCTVAANAKGGEDITSLIKAIAQLISHQIPLSLQPFIDG
>gnl|CDD|274313 TIGR02817, Putative_oxidoreductase_transmembrane_protein, zinc-binding alcohol dehydrogenase family protein. Members of this model form a distinct subset of the larger family of oxidoreductases that includes zinc-binding alcohol dehydrogenases and NADPH:quinone reductases (pfam00107). While some current members of this family carry designations as putative alginate lyase, it seems no sequence with a direct characterization as such is detected by this model [Energy metabolism, Fermentation]
KAVGYKKPLPITDPDALVDIDLPKPKPGGRDLLVEVKAISVNPVDTKVRARMAPEAGQPKILGWDAAGVV
VAVGDEVTLFKPGDEVWYAGDIDRPGSNAEFHLVDERIVGHKPKSLSFAEAAALPLTSITAWELLFDRLG
INDPVAGDKRALLIIGGAGGVGSILIQLARQLTGLTVIATASRPESQEWVLELGAHHVIDHSKPLKAQLE
KLGLEAVSYVFSLTHTDQHFKEIVELLAPQGRFALIDDPAELDISPFKRKSISLHWEFMFTRSMFQTADM
IEQHHLLNRVARLVDAGKIRTTLAETFGTINAANLKRAHALIESGKARGKIVLEGF
>gnl|CDD|131865 TIGR02818, S-hydroxymethylglutathione_dehydrogenase, S-(hydroxymethyl)glutathione dehydrogenase/class III alcohol dehydrogenase. The members of this protein family show dual function. First, they remove formaldehyde, a toxic metabolite, by acting as S-(hydroxymethyl)glutathione dehydrogenase (1.1.1.284). S-(hydroxymethyl)glutathione can form spontaneously from formaldehyde and glutathione, and so this enzyme previously was designated glutathione-dependent formaldehyde dehydrogenase. These same proteins are also designated alcohol dehydrogenase (EC 1.1.1.1) of class III, for activities that do not require glutathione; they tend to show poor activity for ethanol among their various substrate alcohols [Cellular processes, Detoxification, Energy metabolism, Fermentation]
KSRAAVAWAAGQPLKIEEVDVEMPQKGEVLVRIVATGVCHTDAFTLSGADPEGVFPVILGHEGAGIVEAV
GEGVTSVKVGDHVIPLYTAECGECKFCLSGKTNLCVAVRETQGKGLMPDGTSRFSKDGQPIYHYMGCSTF
SEYTVVPEISLAKINPAAPLEEVCLLGCGVTTGIGAVLNTAKVEEGDTVAVFGLGGIGLSVIQGARMAKA
SRIIAIDINPAKFELAKKLGATDCVNPNDYDKPIQEVIVEITDGGVDYSFECIGNVNVMRAALECCHKGW
GESIIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKGRTELPGIVEQYMKGEIALDDFVTHTMPLEDIN
EAFDLMHEGKSIRTVIHY
>gnl|CDD|274314 TIGR02819, formaldehyde_dehydrogenase_glutathione-independent, formaldehyde dehydrogenase, glutathione-independent. Members of this family represent a distinct clade within the larger family of zinc-dependent dehydrogenases of medium chain alcohols, a family that also includes the so-called glutathione-dependent formaldehyde dehydrogenase. Members of this protein family have a tightly bound NAD that can act as a true cofactor, rather than a cosubstrate in dehydrogenase reactions, in dismutase reactions for some aldehydes. The name given to this family, however, is formaldehyde dehydrogenase, glutathione-independent [Central intermediary metabolism, One-carbon metabolism]
SGNRGVVYLGPGKVEVQDIDYPKLELPDGRKCEHGVILKVVTTNICGSDQHMVRGRTTAPTGLVLGHEIT
GEVIEKGRDVEFIKIGDIVSVPFNIACGRCRNCKEGHTGVCLNVNPARAGAAYGYVDMGGWVGGQSEYVM
VPYADFNLLKFPDRDQALEKIRDLTMLSDIFPTGYHGAVTAGVGPGSTVYIAGAGPVGLAAAASAQLLGA
AVVIVGDLNPARLAQARSFGCETVDLSKDATLPEQIEQILGEPEVDCAVDCVGFEARGHGHDGKKEAPAT
VLNSLMEVTRVGGAIGIPGLYVTEDPGAVDAAAKTGSLSIRFGLGWAKSHSFHTGQTPVMKYNRNLMQAI
LHDRVQIAKAVNVTVISLDDAPEGYAEFDAGAAKKFVIDPHGT
>gnl|CDD|131867 TIGR02820, formald_GSH, S-(hydroxymethyl)glutathione synthase. The formation of S-(hydroxymethyl)glutathione synthase from glutathione and formaldehyde occurs naturally, but this enzyme speeds its formation in some species as part of a pathway of formaldehyde detoxification [Cellular processes, Detoxification, Central intermediary metabolism, One-carbon metabolism]
KLHPAIDNGIKPASTSFAGGTLKCLCTSNKVTVKIKGQSAHNHACGCSKCWKPEGAIFSVVAVVPRDNVT
VTANGDKLKVVDASATIQRHACKGCGTHMYGRIENKDHPFYGLDFIHTELSAEDGWSAPGFAAFVSSIIE
TGTDPERMDGIRARLRELGLEPYDCLSPALMDAIATHVAKQK
>gnl|CDD|131868 TIGR02821, S-formylglutathione_hydrolase, S-formylglutathione hydrolase. This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well [Cellular processes, Detoxification]
ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAE
HGLALVAPDTSPRGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQ
GITGHSMGGHGALVIALKNPDRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADGGR
HSTILIDQGTADQFLDEQLRPDAFEQACRAAGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL
>gnl|CDD|131869 TIGR02822, putative_alcohol_dehydrogenase, zinc-binding alcohol dehydrogenase family protein. Members of this model form a distinct subset of the larger family of oxidoreductases that includes zinc-binding alcohol dehydrogenases and NADPH:quinone reductases (pfam00107). The gene neighborhood of members of this family is not conserved and it appears that no members are characterized. The sequence of the family includes 6 invariant cysteine residues and one invariant histidine. It appears that no member is characterized [Energy metabolism, Fermentation]
AWEVERPGPIEDGPLRFVERPVPRPGPGELLVRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAG
RGADAGGFAVGDRVGIAWLRRTCGVCRYCRRGAENLCPASRYTGWDTDGGYAEYTTVPAAFAYRLPTGYD
DVELAPLLCAGIIGYRALLRASLPPGGRLGLYGFGGSAHLTAQVALAQGATVHVMTRGAAARRLALALGA
ASAGGAYDTPPEPLDAAILFAPAGGLVPPALEALDRGGVLAVAGIHLTDTPPLNYQRHLFYERQIRSVTS
NTRADAREFLELAAQHGVRVTTHTYPLSEADRALRDLKAGRFDGAAVLV
>gnl|CDD|274315 TIGR02823, oxido_YhdH, putative quinone oxidoreductase, YhdH/YhfP family. This model represents a subfamily of pfam00107 as defined by Pfam, a superfamily in which some members are zinc-binding medium-chain alcohol dehydrogenases while others are quinone oxidoreductases with no bound zinc. This subfamily includes proteins studied crystallographically for insight into function: YhdH from Escherichia coli and YhfP from Bacillus subtilis. Members bind NADPH or NAD, but not zinc [Unknown function, Enzymes of unknown specificity]
KALVVEKEDGKVSAQVETLDLSDLPEGDVLIKVAYSSLNYKDALAITGKGGVVRSYPMIPGIDAAGTVVS
SEDPRFREGDEVIVTGYGLGVSHDGGYSQYARVPADWLVPLPEGLSLREAMALGTAGFTAALSVMALERN
GLTPEDGPVLVTGATGGVGSLAVAILSKLGYEVVASTGKAEEEDYLKELGASEVIDREDLSPPGKPLEKE
RWAGAVDTVGGHTLANVLAQLKYGGAVAACGLAGGPDLPTTVLPFILRGVSLLGIDSVYCPMALREAAWQ
RLATDLKPRNLESITREITLEELPEALEQILAGQHRGRTVVDV
>gnl|CDD|274316 TIGR02824, quinone_oxidoreductase, putative NAD(P)H quinone oxidoreductase, PIG3 family. Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam pfam00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized [Unknown function, Enzymes of unknown specificity]
MKAIEITEPGGPEVLVLVEVPLPVPKAGEVLIRVAAAGVNRPDLLQRAGKYPPPPGASDILGLEVAGEVV
AVGEGVSRWKVGDRVCALVAGGGYAEYVAVPAGQVLPVPEGLSLVEAAALPETFFTVWSNLFQRGGLKAG
ETVLIHGGASGIGTTAIQLAKAFGARVFTTAGSDEKCAACEALGADIAINYREEDFVEVVKAETGGKGVD
VILDIVGGSYLNRNIKALALDGRIVQIGFQGGRKAELDLGPLLAKRLTITGSTLRARPVAEKAAIAAELR
EHVWPLLASGRVRPVIDKVFPLEDAAQAHALMESGDHIGKIVLTV
>gnl|CDD|131872 TIGR02825, Prostaglandin_reductase_1, leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase. Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase
AKTWTLKKHFVGYPTDSDFELKTVELPPLNNGEVLLEALFLSVDPYMRVAAKRLKEGDTMMGQQVARVVE
SKNVALPKGTIVLASPGWTSHSISDGKDLEKLLTEWPDTLPLSLALGTVGMPGLTAYFGLLEICGVKGGE
TVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKVAYLKKLGFDVAFNYKTVKSLEETLKKASPDGYDC
YFDNVGGEFSNTVIGQMKKFGRIAICGAISTYNRTGPLPPGPPPEIVIYQELRMEGFIVNRWQGEVRQKA
LKELLKWVLEGKIQYKEYVIEGFENMPAAFMGMLKGENLGKTIVK
>gnl|CDD|274317 TIGR02826, hypothetical_protein, anaerobic ribonucleoside-triphosphate reductase activating protein. Members of this family represent a set of radical SAM enzymes related to, yet architecturally different from, the activating protein for the glycine radical-containing, oxygen-sensitive ribonucleoside-triphosphate reductase (RNR) as described in model TIGR02491. Members of this family are found paired with members of a similarly divergent set of anaerobic ribonucleoside-triphosphate reductases. Identification of this protein as an RNR activitating protein is partly from pairing with a candidate RNR. It is further supported by our finding that upstream of these operons are examples of a conserved regulatory element (described Rodionov and Gelfand) that is found in nearly all bacteria and that occurs specifically upstream of operons for all three classes of RNR genes [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
KYVNEDIVFQEVPDEVSLAFYISGCPLGCPGCHSPELWHEDEGTPLTPEVLAQLLDKYRSLITCVLFLGG
EWEPEALLSLLKYVKEHAGLKVCLYTGREPKDPLELVQHLDYLKTGPWIETLGGLDSPTTNQRFYDIRTG
EKMNHLF
>gnl|CDD|274318 TIGR02827, conserved_hypothetical_protein, anaerobic ribonucleoside-triphosphate reductase. Members of this family belong to the class III anaerobic ribonucleoside-triphosphate reductases (RNR). These glycine-radical-containing enzymes are oxygen-sensitive and operate under anaerobic conditions. The genes for this family are pair with genes for an acitivating protein that creates a glycine radical. Members of this family, though related, fall outside the scope of TIGR02487, a functionally equivalent protein set; no genome has members in both familes. Identification as RNR is supported by gene pairing with the activating protein, lack of other anaerobic RNR, and presence of an upstream regulatory element strongly conserved upstream of most RNR operons [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
LQEDQLGDKLDFTEDYCHARNAAIGSKIDANANVRVKNIATLEIEISKDHFIQINRYLVWDKIKEMFGKE
LADEYLRQIEHHEIYVHDETSLKPYCASITMYPILEKGLPFIGGESKAPKHLSSFCGHFINFVFAVSSQF
AGAVATPEFLMYFDYFARKDYGEDYLKTHKLDWYIENHFQQVVYSLNQPAAARGYQSVFWNISYYDKNYF
KSLFGGFVFPDGSLPHWEDVIALQKHFMEWFNQEREKAVLTFPVLTAALLYEDGKCRDEDFARFIAQINA
KGNSFFWYMSDSADSLASCCRLRNEIQDNTFSYSLGAGGVATGSINVITINLNRLVQESGDDREKYLQIL
RHRVDLIHKYQAAYRELMKEYLSEGLLPLYDAGFILLDRQYLTIGINGMVEAAEFMGLTVKYNEEYKVFV
QNVLDVIREANEKAYHEYGFMFNTEFVPAENLGVKNAKWDKLDGYFVPRDCYNSYFYPVEDNSTNVLDKF
RLHGKEWIEKLDGGSALHLNLDESLSEEEYRNLVRVAADTGCNYFCFNIKITVCNECHHIDKRTLERCPV
CGSANVDYYTRVIGYLKRVSAFSKARQIEAPKRQY
>gnl|CDD|131875 TIGR02828, conserved_hypothetical_protein, putative membrane fusion protein. Members of this family show similarity to the members of TIGR00999, the membrane fusion protein (MFP) cluster 2 family, which is linked to RND transport systems [Transport and binding proteins, Unknown substrate]
SGIVFYQTDGLEEVLTPENVAGLGPEKFSTLPYPDTRVDGPVEEGQPLFKIVDNLSLMLLVISADSLSES
LLEGQEVELQVSGRDLELTARVVRLAAGGPDLLVHLEAPIPSYPDALRLRKMRVSIKLKEYEGIILPVSA
IDVEQGKTGVWILKNGGYVFVPVRVLGSTADEVAVEGDKPPDAQLLTK
>gnl|CDD|213743 TIGR02829, Stage_III_sporulation_protein_AE, stage III sporulation protein AE. A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This protein, a member of this panel, is found in a spore formation operon and is designated stage III sporulation protein AE [Cellular processes, Sporulation and germination]
MKKLIFILLLILILFLCFVVPVQASGVDESSRIDNSLEIEQIYDFWSNLKTEYGILFLPESQKYSLMEFL
RGEKPFSVKKIGEALLSYLFHELLSNGKLLGTLIILAIICALLQNLQNAFSSESVSQIAYFACYMVLIII
ALKSFHVAMSYAKEAIESMVDFMLALLPLLLALLASSGGVTSAAFFDPVILFSINTTGKVITNIVIPLIL
LSFVLSIVNNISDEYKIDKLSKFLKQISIGSQGVFLTIFLGVITIQGITAAVADGVTVKTAKFAVGNFVP
VVGKMLTDAVDTVAGASLLLKNAIGTLGLIILIVIVAFPAIKILSLAFIYKFAAAVLEPLGDKRIVSCLS
SVGNALILIFSCLASVSLMFFIMITIIIAAG
>gnl|CDD|274319 TIGR02830, Stage_III_sporulation_protein_AG, stage III sporulation protein AG. CC A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This protein, a member of this panel, is found in a spore formation operon and is designated stage III sporulation protein AG [Cellular processes, Sporulation and germination]
KKLTYLLVLLLIGLLLLIVSSFFSSSEDIEESDTPNNEKTEPEFVQGEVQKEDEISDYEKQYENELKEIL
EKIEGVGDVTVMVNLDSSEEKVYAKNTSKGQQTTEETDKEGGKRSVEDESDGEEVVIIRNGDQETPVVLK
TEKPEIRGVLVVAEGAENPQIKYRIVEAVSRVLDVPAHKVSVLPKK
>gnl|CDD|131878 TIGR02831, Stage_II_sporulation_protein_M, stage II sporulation protein M. A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This predicted integral membrane protein is designated stage II sporulation protein M [Cellular processes, Sporulation and germination]
EGLMEHLKENFWLYIFVLLLFLVGIVFGAYTVNSMSIVQKNDLYFYLSNFFGQLSGGNSASYGDIFRQSL
FNNIKYVGLMWILGLSIIGLPIILILDFLKGFVVGFTVGFLVNQLGMKGVLLAFLGVLPQNLIIIPGILI
ASVIAISFSLGLLRSGFNKRINEGLSQAFIRYSLSFLCIAVLIALGSLIEAYVSPNLMRL
>gnl|CDD|131879 TIGR02832, conserved_hypothetical_protein, sporulation protein YunB. A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. Mutation of this sigma E-regulated gene, designated yunB, has been shown to cause a sporulation defect [Cellular processes, Sporulation and germination]
LPFRRILLISLILFILLLLQFLWIVDSLIKPTLLAVAEVEMNRIATETINKAVTDEVEQGFDYNDLIEIE
TDENGKITLIQANTLLLNKLASNITLRVQEKLNELGETGVKIPLGRLTGNSLLSNVGPKIPVRFAPIGDV
ETDFKQEFEPAGINQTRHQIYVEIEVTMRVIIPLTTKEVKVKQELPIAETIIVGEVPQSYGGGS
>gnl|CDD|131880 TIGR02833, Stage_III_sporulation_protein_AB, stage III sporulation protein AB. A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This protein, a member of this panel, is designated stage III sporulation protein AB [Cellular processes, Sporulation and germination]
KLLGALLIVLSSTWIGFLYANRFKERPRQLRQLINALQSLEAEIVYGHTPLPEAFKKIALKSPKPVNLLF
ESASERLKEGEGLTVYEAWKKALNEVWKQTALQKSEKEILLQFGKTLGESDREGQQKHINLTLEHLERQL
TEAEDEQKKNEKMYRYLGVLVGLMIVLLLL
>gnl|CDD|274320 TIGR02834, Uncharacterized_protein_YtxC, putative sporulation protein YtxC. This uncharacterized protein is part of a panel of proteins conserved in all known endospore-forming Firmicutes (low-GC Gram-positive bacteria), including Carboxydothermus hydrogenoformans, and nowhere else [Cellular processes, Sporulation and germination]
IEIHFEEDKEIEELLESLFRRLRKEGLEVGVGESIEGGSHFIEIYVAEENFDSKFKNKFRKHIASILADI
IVEHKEDELILKIIEESYYFTDQEEIEQILAIANSILTGERKDDPSEIYKMNRKNEILDEINEFLEENDE
INIEGFVTFRLKPYVEELRDIVEKAIDEYLMEKEYQEFIKLLRYFVEIQDSRLEIVHIVVDGGSFRLYDE
NGRDLSSEELVELIDEVFESGLYIEDILISPLISLAPEKIKIHTDDPDHNKIILTIQNVFQERVEV
>gnl|CDD|131882 TIGR02835, RNA_polymerase_sigma-35_factor, RNA polymerase sigma-E factor. Members of this family comprise the Firmicutes lineage endospore formation-specific sigma factor SigE, also called SpoIIGB and sigma-29. As characterized in Bacillus subtilis, this protein is synthesized as a precursor, specifically in the mother cell compartment, and must cleaved by the SpoIIGA protein to be made active [Transcription, Transcription factors, Cellular processes, Sporulation and germination]
FKLTRVLRKLLAKLLIRPREIYYIGGSEALPPPLTGEEEEALLQKLTQGDESAKSTLIERNLRLVVYIAR
KFENTGIGIEDLVSIGTIGLIKAVNTFNPSKKIKLATYASRCIENEILMYLRRNNKTRSEVSFDEPLNVD
WDGNELLLSDVLGTDSDIVYKYLEEEVDRELLRKALAKLNDREKKIMELRFGLVGGTEKTQKEVADMLGI
SQSYISRLEKRILKRLKKEINRME
>gnl|CDD|131883 TIGR02836, Stage_IV_sporulation_protein_A, stage IV sporulation protein A. A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This protein, a member of this panel, is designated stage IV sporulation protein A. It acts in the mother cell compartment and plays a role in spore coat morphogenesis [Cellular processes, Sporulation and germination]
MEKVDIYKDIAERTQGDIYIGVVGPVRTGKSTFIKKFMELLVLPNISNEYDKERAQDELPQSAAGKTIMT
TEPKFVPNEAVEININEGTKFKVRLVDCVGYTVKGALGYMEEDKPRMVSTPWYDYEIPFEEAAEIGTRKV
IQEHSTIGVVVTTDGTITDIPREDYVEAEERVIEELKELNKPFIILLNSTHPYHPETEALRQELEEKYDV
PVLAMDVESMRESDILSVLEEVLYEFPILEINIDLPSWVEVLDENHWLKENFQSSVKETVKDVYRLRDVD
NVVGQLKENEFIESVGLAGIEMGEGVAEIDLYAKEGLFYKILKEVSGVEIRGEDHLMELMKDLAHAKTEY
DKISDALKMVKETGYGVVAPALEEMKLEEPEIVRQGNRFGVRLKASAPSIHIIKADIETEITPIIGTEKQ
SEELVKYLLEQFEDDPLKIWESNIFGKSLSDLVKEGIQNKLSLMPENAQVKLQETLEKIINEGGGGLICI
IL
>gnl|CDD|131884 TIGR02837, Stage_II_sporulation_protein_R, stage II sporulation protein R. A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This protein, a member of this panel, is designated stage II sporulation protein R [Cellular processes, Sporulation and germination]
KKIIIVLLLAVLGLGFIVGSVLLAAAARANDQEVISEKLIRFHVLANSDSDEDQALKLKVRDAVLKEIRP
WLSGLKSLEEARRVIRENLPEIERIAESVIKAEGADYKVRVELGKYSFPTKLYGNIVLPAGEYEALRILI
GEGAGANWWCVVFPPLCFTDRTVGVAVE
>gnl|CDD|131885 TIGR02838, stage_V_sporulation_protein_AC, stage V sporulation protein AC. This model describes stage V sporulation protein AC, a paralog of stage V sporulation protein AE. Both are proteins found to present in a species if and only if that species is one of the Firmicutes capable of endospore formation, as of the time of the publication of the genome of Carboxydothermus hydrogenoformans. Mutants in spoVAC have a stage V sproulation defect [Cellular processes, Sporulation and germination]
QEYQNLVKKYEPKPPYLKNCVMAFLVGGLICLIGQLISDFYLRYFQFSEKTAGSPTSATLIFISALLTGL
GVYDKIAQFAGAGSIVPITGFANAMASPALEHKTEGLVLGVGANMFTLAGPVIVYGVSTAYIVGIIRYLL
R
>gnl|CDD|131886 TIGR02839, stage_V_sporulation_protein_AE, stage V sporulation protein AE. This model describes stage V sporulation protein AE, a paralog of stage V sporulation protein AC. Both are proteins found to present in a species if and only if that species is one of the Firmicutes capable of endospore formation, as of the time of the publication of the genome of Carboxydothermus hydrogenoformans. Mutants in spoVAE have a stage V sproulation defect [Cellular processes, Sporulation and germination]
YILAFLVGGAICVIGQLLLDKTKLTPAHILVTFVTVGAILDGFGLYDKLIEFAGAGATVPLTGFGHSLAH
GAIEEVEKKGLIGIFTGGFEGTSAGISAAILFGYLMALIFKPKG
>gnl|CDD|274321 TIGR02840, conserved_hypothetical_protein, putative sporulation protein YtaF. This protein family was identified, at the time of the publication of the Carboxydothermus hydrogenoformans genome, as having a phylogenetic profile that exactly matches the subset of the Firmicutes capable of forming endospores. The species include Bacillus anthracis, Clostridium tetani, Thermoanaerobacter tengcongensis, Geobacillus kaustophilus, etc. This protein, previously named YtaF, is therefore a putative sporulation protein [Cellular processes, Sporulation and germination]
LSLLLLAFAVSLDSFGVGIAYGLRKIKIPFLSNLIIAVISGLFIFISMLLGKFLAKFLPPKVTEILGAFI
LIAIGIWIIYNAFRPKKEVKDRSSEPDSTKELKSFGFVIQILRNPEVADLDKSGNISGKEALLLGIALSL
DAFGAGIGASLLGLNPLATSILVAVMSFIFVSLGLFLGKKISKKSIIGKFSFLSGILLILLGVWRL
>gnl|CDD|131888 TIGR02841, Uncharacterized_protein_YyaC, putative sporulation protein YyaC. A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This protein, also called YyaC, is a member of that panel and is otherwise uncharacterized. The second round of PSI-BLAST shows many similarities to the germination protease GPR, which is found in exactly the same set of organisms and has a known role in the sporulation/germination process [Cellular processes, Sporulation and germination]
REIVLLCIGTDRSTGDALGPLVGMKLKFLLLNNFHVFGTLEEPVHAKNLEEKLKIIKKKHPNPFIIAIDA
CLGRTKSVGHITIGKGPLKPGAAVNKDLPPVGDLSITGIVNVSGFMEFMVLQNTRLSTVMKMADVISAGL
>gnl|CDD|131889 TIGR02842, Cytochrome_bo3_ubiquinol_oxidase_subunit_3, cytochrome o ubiquinol oxidase, subunit III. Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant [Energy metabolism, Electron transport]
TIFGFWLYLMSDCILFATLFATYAVLSNNTAGGPSGKEIFDLPFVLVETFLLLLSSITFGFAMLAMNKKN
KKMVILWLAITFLLGLGFIGMEIYEFYHLIAEGNGPDRSAFLSAFFTLVGTHGLHVTSGLIWIIVMIIQV
YKYGLTKINRRRLACLSLFWHFLDIVWICVFTFVYLLGVL
>gnl|CDD|131890 TIGR02843, Cytochrome_bo3_ubiquinol_oxidase_subunit_1, cytochrome o ubiquinol oxidase, subunit I. Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant [Energy metabolism, Electron transport]
FGKLTLDAIPYHEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLR
GFADAIMMRTQQALASGGSAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFL
NSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVT
IIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWA
WGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIA
TMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFH
NVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNPEW
HPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDR
DAFWDMKKKGVAYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFD
DDVDYYVPAEEVKKIE
>gnl|CDD|131891 TIGR02844, Stage_III_sporulation_protein_D, sporulation transcriptional regulator SpoIIID. Members of this protein are the transcriptional regulator SpoIIID, or stage III sporulation protein D. It is present in genomes if and only if the species is capable of endospore formation as occurs in the model species Bacillus subtilis. SpoIIID is a DNA binding protein that, in B. subtilis, downregulates many genes but also turns on ten genes [Regulatory functions, DNA interactions, Cellular processes, Sporulation and germination]
KDYIEERVLEIGKYIVETKATVRETAKVFGVSKSTVHKDVTERLPEINPDLAEEVKEVLDLNKAERHIRG
GKATKLKYKK
>gnl|CDD|188254 TIGR02845, Stage_V_sporulation_protein_AD, stage V sporulation protein AD. Bacillus and Clostridium species contain about 10 % dipicolinic acid (pyridine-2,6-dicarboxylic acid) by weight. This protein family, SpoVAD, belongs to the spoVA operon that is suggested to act in the transport of dipicolinic acid (DPA) from the mother cell, where DPA is synthesized, to the forespore, a process essential to sporulation. Members of this protein family are found, so far, in exactly those species believed capable of endospore formation [Cellular processes, Sporulation and germination]
KQTWVFENPPVIVSAGTAVGPKEGDGPLGSYFDKIYDDLYCGEDSWEKAERQLMEDAVNLALQKANLTKD
DVDLFLAGDLLNQIITANFVARDLGIPFLGLYGACSTSMETLALGAMLVDGGFADRVLAATSSHYATAER
QFRYPTEYGVQKPPTAQWTVTGAGAVLLSSTGGGPRITSATIGKVVDLGITDPLDMGAAMAPAAADTIEQ
HFKDTGRTVDDYDLIVTGDLSRVGSEILRDLLKERGYDVGEKYDDCGLMIYRPDQQVFAGGSGCACSAVV
TYGHILKQLRRGKLKKVLVVATGALLSPTTIQQKESIPTIAHAVSIE
>gnl|CDD|131893 TIGR02846, RNA_polymerase_sigma_subunits_sigma70/sigma32, RNA polymerase sigma-K factor. The sporulation-specific transcription factor sigma-K (also called sigma-27) is expressed in the mother cell compartment of endospore-forming bacteria such as Bacillus subtilis. Like its close homolog sigma-E (sigma-29) (see TIGR02835), also specific to the mother cell compartment, it must be activated by a proteolytic cleavage. Note that in Bacillus subtilis (and apparently also Clostridium tetani), but not in other endospore forming species such as Bacillus anthracis, the sigK gene is generated by a non-germline (mother cell only) chromosomal rearrangement that recombines coding regions for the N-terminal and C-terminal regions of sigma-K [Transcription, Transcription factors, Cellular processes, Sporulation and germination]
VLGALLTLIVKSLLFLVGYVTNNGSFPQPLSEEEEKKYLDRLKEGDEEARNVLIERNLRLVAHIVKKFSN
TGEDVDDLISIGTIGLIKAIDSFDPDKGTRLATYAARCIENEILMHLRALKKTKGEVSLQDPIGVDKEGN
EISLIDILGSDGDSVIEQVELNLEIKKLYKKLSVLDGREREVIEMRYGLGDGRRKTQREIAKILGISRSY
VSRIEKRALMKLYKELY
>gnl|CDD|131894 TIGR02847, Cytochrome_bo3_ubiquinol_oxidase_subunit_4, cytochrome o ubiquinol oxidase subunit IV. Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant [Energy metabolism, Electron transport]
HGSLKSYLIGFVLSVILTAIPFGLVMSGTLSKGLTLVIIIVLAVVQILVHLVFFLHLNTSSEQRWNLISL
LFTILIIFILIGGSIWIMHNLNHNMM
>gnl|CDD|131895 TIGR02848, Stage_III_sporulation_protein_AC, stage III sporulation protein AC. Members of this protein family are designated SpoIIIAC, part of the spoIIIA operon of sporulation genes whose mutant phenotype is linked to sporulation stage III. Members of this family are encoded by the genome of a species if and only if that species is capable of endospore formation, as in Bacillus subtilis. The molecular function of this small, probable integral membrane protein is unknown [Cellular processes, Sporulation and germination]
LDISLIFKIAGVGILVAVIHTILKQSGKEEQAQMVTLAGIVVVLFMVITLINDLFNKIKTVFLL
>gnl|CDD|131896 TIGR02849, Stage_III_sporulation_protein_AD, stage III sporulation protein AD. Members of this family are the uncharacterized protein SpoIIIAD, part of the spoIIIA operon that acts at sporulation stage III as part of a cascade of events leading to endospore formation. Note that the start sites of members of this family as annotated tend to be variable; quite a few members have apparent homologous protein-coding regions continuing upstream of the first available start codon. The length of the alignment and the scoring cutoff thresholds for the model have been set to try to detect all valid members of the family, even if annotation of the start site begins too far downstream [Cellular processes, Sporulation and germination]
IAVFLSLIAGIVIFLFVMPKINAVVEVIQSLARKAGLDSLYLATVLKIIGIAYIAEFGSQICKDAGEKAI
ASKIELAGKILILLLAVPIITGVLEAILSIL
>gnl|CDD|131897 TIGR02850, RNA_polymerase_sigma-G_factor, RNA polymerase sigma-G factor. Members of this family comprise the Firmicutes lineage endospore formation-specific sigma factor SigG. It is also desginated stage III sporulation protein G (SpoIIIG). This protein is rather closely related to sigma-F (SpoIIAC), another sporulation sigma factor [Transcription, Transcription factors, Cellular processes, Sporulation and germination]
NKVEICGVNTSKLPVLKNQEMRELFIRMQSGDTTAREKLINGNLRLVLSVIQRFNNRGEYVDDLFQVGCI
GLMKSIDNFDLSQNVKFSTYAVPMIIGEIRRYLRDNNPIRVSRSLRDIAYKALQVRDKLISENSKEPTVS
EIAKELKVPQEEVVFALDAIQDPVSLFEPIYNDGGDPIYVMDQISDEKNKDSQWLEGIALKEAMKRLNER
EKMILNMRFFEGKTQMEVAEEIGISQAQVSRLEKAALKHMRKYV
>gnl|CDD|131898 TIGR02851, stage_V_sporulation_protein_T, stage V sporulation protein T. Members of this protein family are the stage V sporulation protein T (SpoVT), a protein of the sporulation/germination program in Bacillus subtilis and related species. The amino-terminal 50 amino acids are nearly perfectly conserved across all endospore-forming bacteria. SpoVT is a DNA-binding transcriptional regulator related to AbrB (See pfam04014) [Regulatory functions, DNA interactions, Cellular processes, Sporulation and germination]
KATGIVRRIDDLGRVVIPKEIRRTLRIREGDPLEIFTDREGEVILKKYSPIGELGDFAKEYAESLYQSLG
HIVLITDRDTVIAVAGVSKKEYLNKPISDELEDTMEERKTVILSDTKDGPIEIIDGQEFEYTSQVIAPII
AEGDPIGAVIIFSKEPGEKLGEVEQKAAETAAAFLGKQME
>gnl|CDD|188255 TIGR02852, Dipicolinate_synthase_subunit_B, dipicolinic acid synthetase, B subunit. Members of this family represent the B subunit of dipicolinic acid synthetase, an enzyme that synthesizes a small molecule that appears to confer heat stability to bacterial endospores such as those of Bacillus subtilis. The A and B subunits are together in what was originally designated the spoVF locus for stage V of endospore formation [Cellular processes, Sporulation and germination]
KRIGFGLTGSHCTLEAVMPQLEKLIAEGAEVRPIVSYTVQSTNTRFGEGAEWIKKIEEITGFKAINTIVE
AEPFGPKIPLDCMVIAPLTGNSMSKFANAMTDSPVLMAAKATLRNGKPVVLAISTNDALGLNAVNLMRLL
ATKNIYFVPFGQDDPFKKPNSLVAKMDYLEPTIEEALQGKQLQPVLV
>gnl|CDD|131900 TIGR02853, dipicolinate_synthase_subunit_A, dipicolinic acid synthetase, A subunit. This predicted Rossman fold-containing protein is the A subunit of dipicolinic acid synthetase as found in most, though not all, endospore-forming low-GC Gram-positive bacteria; it is absent in Clostridium. The B subunit is represented by TIGR02852. This protein is also known as SpoVFA [Cellular processes, Sporulation and germination]
GIHIAVIGGDARQLELIRKLEELDAKISLIGFDQLEDGFTGAVKCELLELDLTTLDVVILPVPGTSHDGK
VATVFSNEKVVLTPELLESTKGHCTIYVGISNPYLEQLAADAGVKLIELFERDDVAIYNSIPTAEGAIMM
AIEHTDFTIHGSNVMVLGFGRTGMTIARTFSALGARVFVGARSSADLARITEMGLIPFPLNKLEEKVAEI
DIVINTIPALVLTADVLSKLPKHAVIIDLASKPGGTDFEYAKKRGIKALLAPGLPGIVAPKTAGKILANV
LSELLLE
>gnl|CDD|131901 TIGR02854, spore_II_GA, sigma-E processing peptidase SpoIIGA. Members of this protein family are the stage II sporulation protein SpoIIGA. This protein acts as an activating protease for Sigma-E, one of several specialized sigma factors of the sporulation process in Bacillus subtilis and related endospore-forming bacteria [Cellular processes, Sporulation and germination]
MTVYLDVVFLENFIIDYFLLYLTARTLKDKVSQWRLLLAALIGSLYVLFMFTPKASFFTSPIAKLLYSFL
IIFIAFGPKSLRFFLKLLFLFYFVSFATGGGLFALHFFLATNEPALFNAFIGDGVSWKFILIGFPILYYF
VKRRMDAIRDRAILDKQIYELEICLDGKKVTIKGFLDTGNQLRDPLTKLPVIVVEYDSLKSILPDDLDEF
LLSGKMILDPERWQSRIRLIPFRGVGGGSGFLLGIKPDRVKIRYEGEWIEVKDVLIGLSDGKLSSEGDYQ
ALLSPGII
>gnl|CDD|274322 TIGR02855, Sporulation-specific_protease_YabG, sporulation peptidase YabG. Members of this family are the protein YabG, demonstrated for Bacillus subtilis to be an endopeptidase able to release N-terminal peptides from a number of sporulation proteins, including CotT, CotF, and SpoIVA. It appears to be expressed under control of sigma-K [Cellular processes, Sporulation and germination]
KIGDIVARKSYGCDILFRIIDIIENKGGDIAILHGEEMRLIADAPLDDLELVDESERKKRKKRFKERMET
SYRLFRQDYKLMKEKKEYRATGGYKNNQLYFGMPGRVLHIDGDPEYLRKCLKLYKKIGVPVVGIHCKEKE
MPEKVLDLIEEVRPDILVITGHDAYSKNKGNYMDLNAYRHSKYFVETVREARKYVPSLDQLVIFAGACQS
HFESLIRAGANFASSPSRVNIHALDPVYIVEKISFTPFMERVNIWEVLRNTITGEKGLGGIETRGKLREG
MPK
>gnl|CDD|131903 TIGR02856, Uncharacterized_protein_YqfC, sporulation protein YqfC. This small protein, designated YqfC in Bacillus subtilis, is both restricted to and universal in sporulating species of the Firmcutes, such as Bacillus subtilis and Clostridium perfringens. It is part of the sigma(E)-controlled regulon, and its mutation leads to a sporulation defect [Cellular processes, Sporulation and germination]
MKEWLAEKLDLPGDIILDLPRITLIGNEHIYIENHRGLVVFSPEEVKLNSTNGKITIEGKNFVIKFILPE
EILLEGKIKSVRYEE
>gnl|CDD|274323 TIGR02857, transport_ATP-binding_protein, thiol reductant ABC exporter, CydD subunit. The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAAR
AAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVF
PQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIR
RSSEEYRERTMRVLRIAFLSSAVLELFATLSVALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQL
GAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGER
VALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR
PDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD
AETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL
>gnl|CDD|274324 TIGR02858, Stage_III_sporulation_protein_AA, stage III sporulation protein AA. Members of this protein are the stage III sporulation protein AA, encoded by one of several genes in the spoIIIA locus. It seems that this protein is found in a species if and only if that species is capable of endospore formation [Cellular processes, Sporulation and germination]
EEIRIRVGRPLELVFDGEEVFVTDYIPTVEDVNYILQLISNYSLYAFEEELKQGYITIEGGHRVGLAGRC
VTENGKVKTIKNVSSLNIRIAREKLGAADKLLPYLVRNNRVLNTLIISPPQCGKTTLLRDLARILSTGIS
QLGLRGKKVGIVDERSEIAGCVNGVPQHDVGIRTDVLDGCPKAEGMMMLIRSMSPDVIVVDEIGREEDVE
ALLEALHAGVSIIATAHGRDVEDLYKRPVFKELIENEAFERYVVLSRRKGPGTVEAVYDS
>gnl|CDD|131906 TIGR02859, RNA_polymerase_sigma-H_factor, RNA polymerase sigma-H factor. Members of this protein family are RNA polymerase sigma-H factor for sporulation in endospore-forming bacteria. This protein is also called Sigma-30 and SigH. Although rather close homologs in Listeria score well against this model, Listeria does not form spores and the role of the related sigma factor in that genus is in doubt [Transcription, Transcription factors, Cellular processes, Sporulation and germination]
FKQLEDEEIVELARQGNTHALEYLINKYKNFVRAKARSYFLIGADKEDIIQEGMIGLYKAIRDFRPDKLS
SFKAFAELCVTRQIITAIKTATRQKHIPLNSYVSLNKPIYDEESDRTLLDVISGAKVTDPEELIISQEEY
GDIESKMNELLSDLEWKVLQSYLDGKSYQEIACDLNRHVKSIDNALQRVKRKLEKYLE
>gnl|CDD|274325 TIGR02860, stage_IV_sporulation_protein_B, stage IV sporulation protein B. SpoIVB, the stage IV sporulation protein B of endospore-forming bacteria such as Bacillus subtilis, is a serine proteinase, expressed in the spore (rather than mother cell) compartment, that participates in a proteolytic activation cascade for Sigma-K. It appears to be universal among endospore-forming bacteria and occurs nowhere else [Cellular processes, Sporulation and germination]
KEKIRIVIGVLLFVLLVSVGSSPPLRQFVSTPDQVFIFEGQNHSINLKFPFSKTTLYSNASKTGEAELVV
KLFGLIPIKSISVKVLPDIKVIPGGQSIGVKLNTKGVLVVGFSDIETEKGKIHSPGEEAGIQIGDRILKI
NGEKIKNMDDLANLINKAGGEKLTLTIERGGKIIETVIKPVKDKEEGRYRIGLYIRDSAAGIGTLTFYDP
KTKKYGALGHVITDIDTGKPISVENGQIVNSSITSIEKGRRGNPGEKLGIFSEEKKIIGNIKKNTPFGIF
GKLNQEIKNPLYNKPMPVALRDEVKEGPAKILTVIDGEKVEKFDIEIVKLVPQNSPATKGMVIKITDPRL
LEKTGGIVQGMSGSPIIQNGKVIGAVTHVFVNDPTSGYGVYIEWMLKEAGIL
>gnl|CDD|274326 TIGR02861, Hypothetical_protein_CA_C1663, small acid-soluble spore protein, H-type. This model is derived from pfam08141 but has been expanded to include in the seed corresponding proteins from three species of Clostridium. Members of this family should occur only in endospore-forming bacteria, typically with two members per genome, but may be absent from the genomes of some endospore-forming bacteria. SspH (previously designated YfjU) was shown to be expressed specifically in spores of Bacillus subtilis [Cellular processes, Sporulation and germination]
MDVQRAKEIAASPEMINVTYKGVPVYIEHVDEQSGTARVYSLDNPGKEQDVPVNDLEE
>gnl|CDD|163046 TIGR02862, Sigma-K_factor-processing_regulatory_protein_BofA, pro-sigmaK processing inhibitor BofA. Members of this protein family are found only in endospore-forming bacteria, such as Bacillus subtilis and Clostridium tetani. Among such bacteria, it appears only Symbiobacterium thermophilum lacks a member of this family. The protein, designated BofA, is an integral membrane protein that regulates the proteolytic activation of the RNA polymerase sigma factor K [Cellular processes, Sporulation and germination]
ELIISIILGLVILLLIVGAPVKPLRLIGKAAINLIIGALLLFIVNVFGGAFGIHIPINLVTATIAGFLGL
PGIALLVAIKLFI
>gnl|CDD|131910 TIGR02863, putative_small_acid-soluble_spore_protein, small, acid-soluble spore protein, SspJ [Cellular processes, Sporulation and germination]
MGIFFNKDKGKKSEKDKNAIQGALEDAGQALKDDPLQEAVNKKKNNR
>gnl|CDD|274327 TIGR02864, Small_acid-soluble_spore_protein_O, small, acid-soluble spore protein O. This model represents a minor (low-abundance) spore protein, designated SspO. It is found in a very limited subset of the already small group of endospore-forming bacteria, but these species include Oceanobacillus iheyensis, Geobacillus kaustophilus, Bacillus subtilis, B. halodurans, and B. cereus. This protein was previously called CotK [Cellular processes, Sporulation and germination]
MVKKKANHRINGMNAAKAQGKGAGQFDEEFANEPLTAAERQNNKKRKKNQ
>gnl|CDD|274328 TIGR02865, Stage_II_sporulation_protein_E, stage II sporulation protein E. Stage II sporulation protein E (SpoIIE) is a multiple membrane spanning protein with two separable functions. It plays a role in the switch to polar cell division during sporulation. By means of it protein phosphatase activity, located in the C-terminal region, it activates sigma-F. All proteins that score above the trusted cutoff to this model are found in endospore-forming Gram-positive bacteria. Surprisingly, a sequence from the Cyanobacterium-like (and presumably non-spore-forming) photosynthesizer Heliobacillus mobilis is homologous, and scores between the trusted and noise cutoffs [Cellular processes, Sporulation and germination]
IIFFVIAFLLGRAVIVSPMAPFGIAFLAAVLLAKKGGDKAFFSALGVLLGAISIQPKHSLKYLLLVAVII
LLSYVLKNLTDKKKTVVPPIVVFLEAAVYAIFGYLQNKLVTPLDFILSIVEASLSFVLYYIFNYSIPCLK
NGRTKHLLTNEEIVSLIILIASVLTGLRGLSIWGLSLENIIARLAVLLISYIGGSGAGAAGGVVIGVILG
LANNANLYQIGVFGFAGLLGGIFKELGKIGTGIGYLVGFLILAFYTQGSVAFSLALYEALIATLLFLLIP
NKIYKKLERYLDGERKQPDLQEDYMRKVREIAAEKLEEFSEVFRELSNTFVEALASNEKLTMKRKSSYLL
ENLAERVCQSCNMKHRCWKREFDYTYSAMEELIENLEEKKDPNSKLPDEFERKCIKRKELINTTEDILNN
YIINEMWRKRLEEGRRLVAEQLKGVAESVEDIAKEINLEIVFHQLLEEKIIRALNKNGIPYEDVLAYNTE
GGNIDVELTIAACGGRGECEKKIAPIISEVTGELMCVKDERCSIDPKGRCHLTFEETPKYHVSTGVARAA
KDGELVSGDSYSFGKLSAGKYAVAISDGMGSGPEAAQESSACVRLLEKFLESGFDREVAIKTVNSILSLR
STDEKFSTLDLSVIDLYTGQAEFVKVGAVPSFIKRGAKVEVIRSSNLPIGILDEVDVELVRKKLKNGDLI
VMVSDGVLEGEKEVEGKVLWLVRKLKETNTNDPEEIAEYLLEKAKELRSGKIKDDMTVIVAKVY
>gnl|CDD|274329 TIGR02866, Heme-copper_oxidase_subunit_2, cytochrome c oxidase, subunit II. Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions [Energy metabolism, Electron transport]
PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVG
LFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESGFTTVNELVLPAGTPVELQVTSKDVIHSFWV
PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE
>gnl|CDD|274330 TIGR02867, Stage_II_sporulation_protein_P, stage II sporulation protein P. Stage II sporulation protein P is a protein of the endospore formation program in a number of lineages in the Firmicutes (low-GC Gram-positive bacteria). It is expressed in the mother cell compartment, under control of Sigma-E. SpoIIP, along with SpoIIM and SpoIID, is one of three major proteins involved in engulfment of the forespore by the mother cell. This protein family is named for the single member in Bacillus subtilis, although most sporulating bacteria have two members [Cellular processes, Sporulation and germination]
VFIYHTHSTESYLPELPGVTDPNAATHSEGNITKVGDRLAKELEEKGIGVIHDKTVHDGLNYEQSYDRSR
ETVKKALKENKDLKYIIDLHRDSVRRKKTTVNINGESVAKVMFVIGKNNPHFEKNLQLANKLHAKLEKKY
PGLSRGIFYKDYGNGVYNQDLSPNAILIEVGGVDNTLEEAKRSADYLAEAIAEYLN
>gnl|CDD|274331 TIGR02868, ABC_transporter_ATP-binding_protein, thiol reductant ABC exporter, CydC subunit. The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex
LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPPVLYLSVAAVAVRAFGIGRAVFR
YLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVV
GAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASG
ALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLP
LAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPV
LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHL
FDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADA
PILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL
>gnl|CDD|213747 TIGR02869, Spore_cortex-lytic_enzyme, spore cortex-lytic enzyme. Members of this protein family are the spore cortex-lytic enzyme SleB from Bacillus subtilis and other Gram-positive, endospore-forming bacterial species. This protein is stored in an inactive form in the spore and activated during germination [Cellular processes, Sporulation and germination]
FAVQTYQRGATGSDVIEIQRRLKYWGYYNGKVDGVFGWGTYWAVRNFQSKNGLTVDGIVGPKTKAALGIA
TTQASSANSGNGYSQNDIQLLARLVNGEARGEPYEGQVAVAAVILNRVRDPRFPNTIAGVIYQPGAFTAV
ADGQIWLTPTETSKKAALDALNGWDPSGGALYYFNPATATSSWIWTRPIIKRIGKHIFCK
>gnl|CDD|274332 TIGR02870, Stage_II_sporulation_protein_D, stage II sporulation protein D. Stage II sporulation protein D (SpoIID) is a protein of the endospore formation program in a number of lineages in the Firmicutes (low-GC Gram-positive bacteria). It is expressed in the mother cell compartment, under control of Sigma-E. SpoIID, along with SpoIIM and SpoIIP, is one of three major proteins involved in engulfment of the forespore by the mother cell [Cellular processes, Sporulation and germination]
KRLIIMVLILIAIIILLPAIIVAGFGDPQNVTEENEKLAPVEKKPEKGVTNLKEEEVAIKVYRSNEDKIE
KVPLEEYVKGVVASEMPAEFEIEALKAQAVAARTFAVRRMLQFGGTGCGDHPGGDVCTDTTHCQAYQSKE
ELKKKWGKDYDEYWSKISQAVASTKGKVLTYNGELIDPVYFSTSGGKTENAEDVWGEDVPYLKSVTSPWE
EQSPKYKTETVMSISEFVDKLKSSLPNLKLQNAASVGVKILARTAGGRVKTIKIGGVTLKGREIRERLGL
NSTDFTWKVQGDKIVITTIGYGHGVGMSQYGANAMAKEGKTYDEILKHYYQGVEIEEI
>gnl|CDD|274333 TIGR02871, conserved_hypothetical_protein, sporulation integral membrane protein YlbJ. Members of this protein family are found exclusively in Firmicutes (low-GC Gram-positive bacterial) and are known from studies in Bacillus subtilis to be part of the sigma-E regulon. Mutation leads to a sporulation defect, confirming that members of this protein family, YlbJ, are sporulation proteins. This protein appears to be universal among endospore-forming bacteria, but is encoded by a pair ORFs distant from eash other in Symbiobacterium thermophilum IAM14863 [Cellular processes, Sporulation and germination]
NIILASLLTLLILSFILNPKASIEASKSGAKLWFYSVFPSLFPFFIISELLINLGGVHFYGKLLEPILRP
PFRVPGVGSFALVMGFLSGYPLGAKYSADLYEEKLITFEEAERLLNFANNSGPLFIIGAVGTSMLNNPTL
GYILLISHYLSCITMGLILRFYKRRKRKILSKKKKTFHIIRLKSKFPIGKTLKEAIENAVKTILLVGGFV
ILFSVVISLLKNSFIFKLILKPLLSLFNLPEQLIIGFFLGILEITNGSKMISESSISLLQKVILISFLLS
FGGISIIAQVASFISKTKISYKPYFIAKLLQGVIASIISYLLYKILYLKNAIGTFTAINSAILNPSNLLQ
IIGFLLLLFLLF
>gnl|CDD|274334 TIGR02872, UPF0118_membrane_protein_YtvI, sporulation integral membrane protein YtvI. Three lines of evidence show this protein to be involved in sporulation. First, it is under control of a sporulation-specific sigma factor, sigma-E. Second, mutation leads to a sporulation defect. Third, it if found in exactly those genomes whose bacteria are capable of sporulation, except for being absent in Clostridium acetobutylicum ATCC824. This protein has extensive hydrophobic regions and is likely an integral membrane protein [Cellular processes, Sporulation and germination]
RLILLIGLIAIFVLAIYFALPYSLPFVIALILALILEPMVRFLEKKLKLPRALAVFIVLLIFLGIIGGLL
YILVTELVTETIALAKNLPQYLNNINDHILPLIDDLESYYGSLPPGQQYTIVNNIQTLLEKLLNYVVSFA
TNLITSIPSFIASIPNFLIVLLFTLIATFFISKDLPRLKSKLFSILPERTSQKLKNIFSELKKAAFGFLK
AQLILVLITFVIVLIGLLIIGVDYALTLALIIGIVDILPILGPGAVLVPWALYLFITGNYAMGIGLLILY
LVVLILRQILEPKVVSSSIGLHPLATLISMYIGLKLFGFLGLIFGPVIVVLFKALIEAGII
>gnl|CDD|131920 TIGR02873, Uncharacterized_protein_YlxY, probable sporulation protein, polysaccharide deacetylase family. Members of this protein family are most closely related to TIGR02764, a subset of polysaccharide deacetylase family proteins found in a species if and only if the species forms endospores like those of Bacillus subtilis or Clostridium tetani. This family is likewise restricted to spore-formers, but is not universal among them in having sequences with full-length matches to the model [Energy metabolism, Biosynthesis and degradation of polysaccharides, Cellular processes, Sporulation and germination]
DELYEEIEQKAKEYEEEPQNAYIDKVWKATPGYNGRQVDVEASYNKMKQEGRFDEKLLVFDEVSPSVHLD
DLPPSPIYRGHPEKPMVALLINVAWGNEYLPEILQILKKHDVKATFFLEGKWVKENSQLAKMIVEQGHEI
GNHAYNHPDMATLSKEEIYDQINQTNEIIEATIGVTPKWFAPPSGSFNDNVVQIAADLQMGTIMWTVDTI
DWKNPSPSVMVNRVLSKIHPGAMVLMHPTASSTEGLEEMITIIKEKGYKIGTITELLD
>gnl|CDD|131921 TIGR02874, conserved_hypothetical_protein, sporulation protein YtfJ. Members of this protein family, exemplified by YtfJ of Bacillus subtilis, are encoded by bacterial genomes if and only if the species is capable of endospore formation. YtfJ was confirmed in spores of Bacillus subtilis; it appears to be expressed in the forespore under control of SigF (see) [Cellular processes, Sporulation and germination]
NHPIENLMKTTMENIKEMIDVNTIVGDPVETPDGSVIIPISKVSFGFAAGGSEFSSSEGSKKSQQKYPFG
GGSGAGVSVKPVAFLVIGSDQIRLLPVDQNTLYEKLIDLAPQLLEMIKNLFSKNK
>gnl|CDD|131922 TIGR02875, stage_0_sporulation_protein_A, sporulation transcription factor Spo0A. Spo0A, the stage 0 sporulation protein A, is a transcription factor critical for the initiation of sporulation. It contains a response regulator receiver domain (pfam00072). In Bacillus subtilis, it works together with response regulator Spo0F and the phosphotransferase Spo0B, both of which are missing from at least some sporulating species and thus not part of the endospore forming bacteria minimal gene set. Spo0A, however, is universal among endospore-forming species [Cellular processes, Sporulation and germination]
HKIRIVIADDNKEFCNLLKEYLAAQPDMEVVGVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKL
NEIELSARPRVIMLSAFGQEKITQRAVALGADYYVLKPFDLEILAARIRQLAWGTNADILADSPTVPPAS
HAAKTKDLEAEITNIIHEIGVPAHIKGYMYLRDAILMVLKDMELLGAVTKELYPAIAKKYNTTASRVERA
IRHAIEVAWSRGNIEPINKLFGYTIEGEKGKPTNSEFIAMVADKLRLGSKAS
>gnl|CDD|274335 TIGR02876, stage_IV_sporulation_protein, sporulation protein YqfD. YqfD is part of the sigma-E regulon in the sporulation program of endospore-forming Gram-positive bacteria. Mutation results in a sporulation defect in Bacillus subtilis. Members are found in all currently known endospore-forming bacteria, including the genera Bacillus, Symbiobacterium, Carboxydothermus, Clostridium, and Thermoanaerobacter [Cellular processes, Sporulation and germination]
LVKYLLGYVRVEVQGGDIERFLNLCWRNGILVWDVKKINAETLTFKVSLKDFKKLKPIARKTGCKVKIIA
RKGLPFLFKRLRKRPGILIGILLFLAIVYFLSNFIWKIDITGVKGETPYEIRKQLKEMGIKPGVWKFSVD
VYKLERKLLDRVPEIMWAGVRVRGTTLVIKVVEKQEPKPVLKKAEPRNIVAKKDGVIKRVYVTSGEPVVK
KGDVVKKGDLLISGILGKEGKTYTVHAEGEVFARTWYEKTVEVPLKTQREVRTGKKIVRYYLNIGGKKIY
LKKPPKEFAKYDVEEKTKKFGLWRWSLPIEIVKETYYEVKEKVEKVTKEEAIEKAKEKAEKELKKELDPN
AKIVSDKILSERVEGGKVKVTVHVEVEEDIAV
>gnl|CDD|274336 TIGR02877, Stress_response_UPF0229_protein_YhbH, sporulation protein YhbH. This protein family, typified by YhbH in Bacillus subtilis, is found in nearly every endospore-forming bacterium and in no other genome (but note that the trusted cutoff score is set high to exclude a single high-scoring sequence from Nitrosococcus oceani ATCC 19707, which is classified in the Gammaproteobacteria). The gene in Bacillus subtilis was shown to be in the regulon of the sporulation sigma factor, sigma-E, and its mutation was shown to create a sporulation defect [Cellular processes, Sporulation and germination]
FRISREDWSLHRKGGEDQERHQEKVEEAIKDNLPDIVSEESIIMSDGKKKIKVPIRGLKEYRFRYDWNKQ
KRVGQGDGNEKVGDVIGRERAGGEGGGGKGAGDQEGEDYYETEVTLEELFELLFEDLELPNLKKKKFDEI
TTDSFKFKDVRKKGLMPNLDKKRTVIEALKRNQLRGRPELYPITKEDLRYKTWKENEKPESNAVVIAMMD
TSGSMGQFKKYIARSFFFWMVKFLRTKYENVEICFISHHTEAKEVTEEEFFHKGESGGTYCSSGYKKALE
IIDERYNPARYNIYAFHFSDGDNLTSDNERAVKLVRKLLEVCNLFGYGEIMPYGYSNTLKNKFKNEIKDP
NFVPLIIRDKEDLYPALKKFL
>gnl|CDD|131925 TIGR02878, Uncharacterized_protein_YpjB, sporulation protein YpjB. Members of this protein, YpjB, family are restricted to a subset of endospore-forming bacteria, including Bacillus species but not CLostridium or some others. In Bacillus subtilis, ypjB was found to be part of the sigma-E regulon, where sigma-E is a sporulation sigma factor that regulates expression in the mother cell compartment. Null mutants of ypjB show a sporulation defect. This protein family is not, however, a part of the endospore formation minimal gene set [Cellular processes, Sporulation and germination]
SWEELNDLSDQVLQLTKQARYEEAKQVLEYFSKQFVSAGKEKDPMLTMDQLRTITLTYERAVQALTATDM
SDDEKIRAVTAFRLAVDAIVSRSQPLWGSLEKPVMEAFTELEKAAQKEDSQAFQEKLNEFLSLYDLIYPS
LTIDVPEDQVQRVDSHLSYLENFRFQQRSEDEKEEQLSLMRGDLKALFDGVKEDEADPSLLWVMISTGGI
IVATLTYVGWRKYKGEKEKVKAR
>gnl|CDD|200217 TIGR02880, Protein_CbxX_chromosomal, probable Rubsico expression protein CbbX. Proteins in this family are now designated CbbX. Some previously were CfxQ (carbon fixation Q). Its gene is often found immmediately downstream of the Rubisco large and small chain genes, and it is suggested to be necessary for Rubisco expression. CbbX has been shown to be necessary for photoautotrophic growth. This protein belongs to the larger family of pfam00004, ATPase family Associated with various cellular Activities. Within that larger family, members of this family are most closely related to the stage V sporulation protein K, or SpoVK, in endospore-forming bacteria such as Bacillus subtilis
SVDLRAEYEGSGITEVLDQLDRELIGLKPVKTRIREIAALLLVERARQKLGLASAAPTLHMSFTGNPGTG
KTTVALRMAQILHRLGYVRKGHLVSVTRDDLVGQYIGHTAPKTKEVLKRAMGGVLFIDEAYYLYRPDNER
DYGQEAIEILLQVMENNRDDLVVILAGYKDRMDSFFESNPGFSSRVAHHIDFPDYSDEELLEIAGLMLDE
QQYRFTAEAETAFADYIALRRTQPHFANARSIRNALDRARLRQANRLFTASDGVLDKSDLSTIAPEDILA
SRVF
>gnl|CDD|163057 TIGR02881, Stage_V_sporulation_protein_K, stage V sporulation protein K. Members of this protein family are the stage V sporulation protein K (SpoVK), a close homolog of the Rubisco expression protein CbbX (TIGR02880) and a members of the ATPase family associated with various cellular activities (pfam00004). Members are strictly limited to bacterial endospore-forming species, but are not universal in this group and are missing from the Clostridium group [Cellular processes, Sporulation and germination]
VERELSRMVGLDEVKALIKEIYAWIQINEKRKEEGLKTSKQVLHMIFKGNPGTGKTTVARILGKLFKEMN
VLSKGHLIEVERADLVGEYIGHTAQKTREVIKKALGGVLFIDEAYSLARGGEKDFGKEAIDTLVKGMEDN
RNEFVLILAGYSDEMDYFLSLNPGLRSRFPISIDFPDYTVEELMEIAERMVKEREYKLTEEAKWKLREHL
YKVDQLSSREFSNARYVRNIIEKAIRRQAVRLLDKSDYSKEDLMLLKKEDL
>gnl|CDD|131928 TIGR02882, cytochrome_aa3_quinol_oxidase_subunit_I, cytochrome aa3 quinol oxidase, subunit I. This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site [Energy metabolism, Electron transport]
PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGI
DALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFW
LFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRA
PGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEV
YIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAI
PTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITG
VVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYSPSDGWFPLNL
ISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPWNGRTLEWATASPPPKYNFAVTPDVNDYDAFWDMK
KHGYRHYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYH
IPAAEIAETEARL
>gnl|CDD|274337 TIGR02883, spore_cwlD, N-acetylmuramoyl-L-alanine amidase CwlD. Members of this protein family are the CwlD family of N-acetylmuramoyl-L-alanine amidase. This family has been called the germination-specific N-acetylmuramoyl-L-alanine amidase. CwlD is required, along with the putative deactylase PdaA, to make muramic delta-lactam, a novel peptidoglycan constituent found only in spores. CwlD mutants show a germination defect [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]
KIIVIDPGHGGIDGGAVGKDGTLEKDITLEIALKLKDYLQEQGALVVMTREDDSDLASEGTKGYSRRKIE
DLRKRVKLINESEADLFISIHLNAFPSSKYSGAQTFYYGNSEENKRLAKFIQDELRRNLDNTNRRAKKIN
DYYLLRNAEVPGVIVECGFLSNPEEAELLKDEDYQQKIAAAIYKGVLRY
>gnl|CDD|131930 TIGR02884, spore_pdaA, delta-lactam-biosynthetic de-N-acetylase. Muramic delta-lactam is an unusual constituent of peptidoglycan, found only in bacterial spores in the peptidoglycan wall, or spore cortex. The proteins in this family are PdaA (yfjS), a member of a larger family of polysaccharide deacetylases, and are specificially involved in delta-lactam biosynthesis. PdaA acts immediately after CwlD, an N-acetylmuramoyl-L-alanine amidase and performs a de-N-acetylation. PdaA may also perform the following transpeptidation for lactam ring formation, as heterologous expression in E. coli of CwlD and PdaA together is sufficient for delta-lactam production [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]
NWGYKRKKNHTPPDAGKEYTELLKKYNAYYLGDTSKKVIYLTFDNGYENGYTPKILDVLKEKKVPAAFFV
TGHYIKTQPDLIKRMVDEGHIVGNHSVHHPSLTAVNDEKFKEELTGVEEEFKKVTGQKEMKYFRPPRGVF
SERTLAYTKELGYYTVFWSLAFKDWKVDEQPGWQYAYKQIMKKIHPGAILLLHAVSKDNAEALDKIIKDL
KEQGYTFKSLDDLM
>gnl|CDD|131931 TIGR02885, RNA_polymerase_sigma-F_factor, RNA polymerase sigma-F factor. Members of this protein family are the RNA polymerase sigma factor F. Sigma-F is specifically and universally a component of the Firmicutes lineage endospore formation program, and is expressed in the forespore to turn on expression of dozens of genes. It is closely homologous to sigma-G, which is also expressed in the forespore [Transcription, Transcription factors, Cellular processes, Sporulation and germination]
LIKLAQNGDKEARDKLIECNLRLVWSIVKRFLNRGYEPEDLFQIGCIGLVKAIDKFDLSYDVKFSTYAVP
MIMGEIKRFLRDDGIIKVSRSLKELARKIRYMKEELSKELGREPTINELAEALGVSPEEIVMALESARSP
QSLYDTVHQDDGDPIYLLDQIADKGSEDSDWLEKIALKEAISKLDERERQIIMLRYFKDKTQTEVANMLG
ISQVQVSRLEKKVLKKMKEKL
>gnl|CDD|131932 TIGR02886, Anti-sigma_F_factor_antagonist, anti-sigma F factor antagonist. The anti-sigma F factor antagonist, also called stage II sporulation protein AA, is a protein universal among endospore-forming bacteria, all of which belong to the Firmcutes [Regulatory functions, Protein interactions, Cellular processes, Sporulation and germination]
IEFEVKGDVLIVRLSGELDHHTAERVRRKIDDAIERRPIKHLILNLKNVTFMDSSGLGVILGRYKKIKNE
GGEVIVCNVSPAVKRLFELSGLFKIIRIYESEEEAL
>gnl|CDD|274338 TIGR02887, Spore_germination_protein_B3, germination protein, Ger(x)C family. Members of this protein family are restricted to endospore-forming members of the Firmicutes lineage of bacteria, including the genera Bacillus, Clostridium, Thermoanaerobacter, Carboxydothermus, etc. Members are nearly all predicted lipoproteins and belong to probable transport operons, some of which have been characterized as crucial to germination in response to alanine. Members typically have been gene symbols gerKC, gerAC, gerYC, etc [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Sporulation and germination]
KKLKILLLLLALLLLTGCWDSREIEDLALVQGIGIDKGEDGKYKLTYQFVNPSKLGSGGGGSPSYKVVSG
TGKTIREAIRDINLKSSRPLFFGHLRVIVFGEKLARDGIEEVLDFLIRDPEIRRTIYIAVTDGKAEELLK
TKPQLEELPGFYLLDLIENSERSSSIIPPVTLNDFLSKLLSEGRDPILPLIKIKKNKKGVKLDGAALFKN
DKLVGKLSEEETRGLNWLTGKVKGGVLTVKLPSDGDFITLEILKSKTKIKIKVKGGKPHFKIHIKLEGRI
TESQDPKENLEKPKNLKKIEKEAEKEIEKEIEQLIKKLQKYKIDPLGLGDELYRKHPKLWKKVKKNWDEI
FKNVDIDVNVDVTIRRSGLTR
>gnl|CDD|274339 TIGR02888, conserved_hypothetical_protein, sporulation protein, YlmC/YmxH family. Members of this family belong to the broader family of PRC-barrel domain proteins (see pfam05239), but are found only in endospore-forming bacteria of the Firmicutes lineage. Most such species have exactly two members of this family and all have at least one; the function is unknown. One of two members from Bacillus subtilis, YmxH, is strongly induced by the mother cell-specific sigma-E factor [Cellular processes, Sporulation and germination]
RLSDLRGKEIINVNDGERLGVIGNIDLEIDEEDGRILSLIIPGKGKKFGLFSKGEEIEIPWDAIKKIGSD
VILVDV
>gnl|CDD|131935 TIGR02889, Sporulation_protein_YpeB, germination protein YpeB. Members of this family are YpeB, a protein usually encoded with the putative spore-cortex-lytic enzyme SleB and required, together with SleB, for normal germination. This family is retricted to endospore-forming species in the Firmicutes lineage of bacteria, and found in all such species to date except Clostridium perfringens. The matching phenotypes of mutants in SleB (called a lytic transglycosylase) and YpeB suggests that YpeB is necessary to allow SleB to function [Cellular processes, Sporulation and germination]
RTILTAAVSIAVVGLGAWGYLQTQEKNDLRNYLQAQYQRAFYELTYHVEQIEAQLGKTLAMGSQRQNTPV
LADVWRHASAANESLSQLPLTQESLEKTSKFLSQVGDFTYTLSVKDAEGKSLSDKEYKTLTTLYNQAVKL
ENQLRKVQNIVMQGGVRWGEIRKLYSGDEAQMPEAILNDFKDVEKNVTQFPTLIYDGPFSDSVINLTPKG
LKGKEISKEEAKQIARDFLGDNAATRIEVVDSGKNGGIPTYSFEVKDPGRKARIYMNVSKKGGHPLWFLD
NRPVSKPKISLNEAVNKAKKFLEKIGFKDMEPTESDKYDNVGVISYVYVQNDVRVYPDQIKVKVALDDGD
VVGFDARQYLTSHRKRTLPKPKLTEEEARSKVNKHLKILSTRLAVIPNETNQEVLTYEFLGTYLGETFLV
YINAETGYEEKILQL
>gnl|CDD|274340 TIGR02890, conserved_hypothetical_protein, regulatory protein, yteA family. Members of this predicted regulatory protein are found only in endospore-forming members of the Firmicutes group of bacteria, and in nearly every such species; Clostridium perfringens seems to be an exception. The member from Bacillus subtilis, the model system for the study of the sporulation program, has been designated both yteA and yzwB. Some (but not all) members of this family show a strong sequence match to Pfam family pfam01258 the C4-type zinc finger protein, DksA/TraR family, but only one of the four key Cys residues is conserved. All members of this protein family share an additional C-terminal domain. Smaller proteins from the proteobacteria with just the N-terminal domain, including DksA and DksA2 are RNA polymerase-binding regulatory proteins even if the Zn-binding site is not conserved [Unknown function, General]
QQLAELKNMLLQEKKELEQRLKQMNKEDGIASQRESTGELSQYDNHPADLATELYEREKDIALREHEERE
LREIEHALQKIENGTYGICEVCGKPIPYERLEAIPTATTCVECQNRKEVKNDRPVEEDVLSPPFGKFNFD
DKGRTAFDAEDAWQEVARF
>gnl|CDD|213748 TIGR02891, Probable_cytochrome_c_oxidase_subunit_1-beta, cytochrome c oxidase, subunit I. This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115 [Energy metabolism, Electron transport]
LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPILAG
FGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWL
LGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGT
HFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVW
AHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVML
ASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPM
HLLGLLGMPRRYYTYPPQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTT
SSPPPAHNF
>gnl|CDD|274341 TIGR02892, conserved_hypothetical_protein, sporulation protein YabP. Members of this protein family are the YabP protein of the bacterial sporulation program, as found in Bacillus subtilis, Clostridium tetani, and other spore-forming members of the Firmicutes. In Bacillus subtilis, a yabP single mutant appears to sporulate and germinate normally (), but is in an operon with yabQ (essential for formation of the spore cortex), it near-universal among endospore-forming bacteria, and is found nowhere else. It is likely, therefore, that YabP does have a function in sporulation or germination, one that is either unappreciated or partially redundant with that of another protein [Cellular processes, Sporulation and germination]
HSVSIENRKRLSITGVKEVISFDDEEILLETVMGFLTIKGQELKMNKLDVENGQVIIKGFISELTYSEGN
GSKEKGKGFFSRLFR
>gnl|CDD|131939 TIGR02893, Spore_protein_YabQ, spore cortex biosynthesis protein YabQ. YabQ, a protein predicted to span the membrane several times, is found in exactly those genomes whose species perform sporulation in the style of Bacillus subtilis, Clostridium tetani, and others of the Firmicutes. Mutation of this sigma(E)-dependent gene blocks development of the spore cortex. The length of the C-terminal region, including some hydrophobic regions, is rather variable between members [Cellular processes, Sporulation and germination]
SITIQFYTMISMVLSGIILGALFDTYRRFRKRQRLNKILVFIEDILFWIVQALIVFYFLLYVNEGEIRFY
VFLALLCGLAIYQALLSKYYVRILEKVITIVVKVLRFLFKLIKKLVVSPIIWILKLLIRL
>gnl|CDD|274342 TIGR02894, DNA_bind_RsfA, transcription factor, RsfA family. In a subset of endospore-forming members of the Firmcutes, members of this protein family are found, several to a genome. Two very strongly conserved sequences regions are separated by a highly variable linker region. Much of the linker region was excised from the seed alignment for this model. A characterized member is the prespore-specific transcription RsfA from Bacillus subtilis, previously called YwfN, which is controlled by sigma factor F and seems to fine-tune expression of some genes in the sigma-F regulon. A paralog in Bacillus subtilis is designated YlbO [Regulatory functions, DNA interactions, Cellular processes, Sporulation and germination]
KTRQDAWTDEEDLLLAETVLRHIREGSTQLSAFEEVGRALNRTAAACGFRWNAYVRKQYEEAIELAKKQR
KEKKRAPGSLTLQDVISFLQNLKTTNPSDQALQKENERLKNELESLQKRNEELEKELEKLRQRLSTIEED
YQTLIDIMDRARKLAVVEDDE
>gnl|CDD|131941 TIGR02895, RNA_polymerase_sigma_factor, RNA polymerase sigma-I factor. Members of this sigma factor protein family are strictly limited to endospore-forming species in the Firmicutes lineage of bacteria, but are not universally present among such species. Sigma-I was shown to be induced by heat shock () in Bacillus subtilis and is suggested by its phylogenetic profile to be connected to the program of sporulation () [Transcription, Transcription factors, Cellular processes, Sporulation and germination]
VQPIQPGNEEREELIRQYKPFIAKIVSSVCGRYIDTKSDDELSIGLIAFNEAIESYDSNKGKSFLSFAKL
IIKRRLIDYIRKNQKYQNLLYLDEDYDENPLEFNKSMEEYRNEIENENRRLEILEYKKLLKQFGIEFVEL
VKVSPKHRDTRKKAIKIAKVIVENEELLEYLIRKKKLPIKEIEERVRISRKTIERYRKYIIALVIILSGD
YTYLKEYI
>gnl|CDD|131942 TIGR02896, Stage_III_sporulation_protein_AF, stage III sporulation protein AF. This family represents the stage III sporulation protein AF of the bacterial endospore formation program, which exists in some but not all members of the Firmicutes (formerly called low-GC Gram-positives). The C-terminal region of this protein is poorly conserved, so only the N-terminal region, which includes two predicted transmembrane domains, is included in the seed alignment [Cellular processes, Sporulation and germination]
EFLKEWVTNIIVLILLATILEMLLPNSSLKKYVKFVVGLILMVVILNPIIKLLTTDPNIDIYVFKASELS
VKNQIEEQKKKIQAKTRAYILEEMAVQLEKQVEKEL
>gnl|CDD|131943 TIGR02897, AA3-600_quinol_oxidase_subunit_III, cytochrome aa3 quinol oxidase, subunit III. This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site [Energy metabolism, Electron transport]
EYRSEQGRLNILGFWIFLGAEIALFATLFATYLVLQHGGDYAGKMPAELFELPLVLIMTFLLLFSSFTCG
IAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEFAHYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGI
VWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIGMV
>gnl|CDD|131944 TIGR02898, Uncharacterized_lipoprotein_YlaJ, sporulation lipoprotein, YhcN/YlaJ family. YhcN and YlaJ are predicted lipoproteins that have been detected as spore proteins but not vegetative proteins in Bacillus subtilis. Both appear to be expressed under control of the RNA polymerase sigma-G factor. The YlaJ-like members of this family have a low-complexity, strongly acidic 40-residue C-terminal domain that is not included in the seed alignment for this model. A portion of the low-complexity region between the lipoprotein signal sequence and the main conserved region of the protein family was also excised from the seed alignment [Cellular processes, Sporulation and germination]
ILFIILLLLLVLTGCTNAQKKNPPNNNVGETNVMSKNNNGMNTTNDTNDGDLYDVADEIASEAAKVKGVK
DATVVITGNYAYVGVDLTNGLEGSVTDELKEKVAETVKSTDNRIANVYVSADPDTVERIRRYGKGIKEGR
PVEGFLDELAEIVRRVFP
>gnl|CDD|131945 TIGR02899, hypothetical_conserved_protein, spore coat assembly protein SafA. SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria [Cellular processes, Sporulation and germination]
VQKGDTLWKIAKKYGVDFDELIQANPQLSNPNLIYPGMKIKIPS
>gnl|CDD|274343 TIGR02900, Stage_V_sporulation_protein_B, stage V sporulation protein B. SpoVB is the stage V sporulation protein B of the bacterial endopore formation program in Bacillus subtilis and various other Firmcutes. It is nearly universal among endospore-formers. Paralogs with rather high sequence similarity to SpoVB exist, including YkvU in B. subtilis and a number of proteins in the genus Clostridium [Cellular processes, Sporulation and germination]
FLKGTFILTIANLITRILGFIFRIVLSRILGAEGVGLYGMAMPIYFLFITLTTGGLPVAISKFVAEASAK
NDRKNIKKILKVSLIFTLIWSLIVTAIVFLLSPFIASTLLKDERSLYSLLVICPAMPFIALSSVLKGYFQ
GISNMKPPAYIQVIEQIVRISVVALLISAFLPYGLEYAVAGAYLSLVLGELVSLLYLYFFFKRKKSFSIR
FPFFDYKSEGKALLFDLFSVSLPLTLSRFIGSLLYFLETLLVPQRLVIAGVTYREATSLYGKLSGMAMPL
LTFPAVITSSLSTALVPDISEAMAKKNYSSIEKRINQAIKISLLLGLITTVILLVIPDELGALFYGRPDA
GNFIRVLAPSFPFLYFSAPLQSILQGLGKQKVALRNSLIGAIVKIILLFVLTSIPSINIYGYAITFIITS
VLVTILNLAEIKKNIRITIDLSDFLIFALLGILVYLGLSLLKYIIFNPNILINLLLIIILGFSLYILL
>gnl|CDD|200218 TIGR02901, cytochrome_aa3_quinol_oxidase_subunit_IV, cytochrome aa3 quinol oxidase, subunit IV. This family (QoxD) encodes subunit IV of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site [Energy metabolism, Electron transport]
MRELFPWKHVMGFILSLILTLLALWVAFYSDLSLVVGLTIIIVFAFIQASLQLIVFMHINEGNDGKVQIY
NIGYAAFIALVTVFGSLWVMIWGY
>gnl|CDD|131948 TIGR02902, Lon_protease_2, ATP-dependent protease LonB. Members of this protein are LonB, a paralog of the ATP-dependent protease La (LonA, TIGR00763). LonB proteins are found strictly, and almost universally, in endospore-forming bacteria. This protease was shown, in Bacillus subtilis, to be expressed specifically in the forespore, during sporulation, under control of sigma(F). The lonB gene, despite location immediately upstream of lonA, was shown to be monocistronic. LonB appears able to act on sigma(H) for post-translation control, but lonB mutation did not produce an obvious sporulation defect under the conditions tested. Note that additional paralogs of LonA and LonB occur in the Clostridium lineage and this model selects only one per species as the protein that corresponds to LonB in B. subtilis [Protein fate, Degradation of proteins, peptides, and glycopeptides, Cellular processes, Sporulation and germination]
GIFAIVQIIFLIIIGLYFFNALKNQQTNKITIDKESKKELEKLNKMRAIRLTEPLSEKTRPKSFDEIIGQ
EEGIKALKAALCGPNPQHVIIYGPPGVGKTAAARLVLEEAKKNPASPFKEGAAFVEIDATTARFDERGIA
DPLIGSVHDPIYQGAGPLGIAGIPQPKPGAVTRAHGGVLFIDEIGELHPVQMNKLLKVLEDRKVFLDSAY
YNSENPNIPSHIHDIFQNGLPADFRLIGATTRNPEEIPPALRSRCVEIFFRPLLDEEIKEIAKNAAEKIG
INLEKHALELIVKYASNGREAVNIVQLAAGIALGEGRKRILAEDIEWVAENGNYHPKPEIKLSSEPQIGR
VNGLAVYGPNSGAVLEVEATAERAENLPGSINVTGIIEEEEIGGSGKSVRRKSSARGSVENVLAVLRSVF
GINPQNYDIHINFPGGIPVDGPSAGVAIAVAIYSAIFKCPIDNKVAMTGEISLNGLVKPVGGVPSKIEAA
KKAGAKKVIIPYENWQESFGSISGINVIPVKNIDEALNYAL
>gnl|CDD|274344 TIGR02903, Lon-like_ATP-dependent_protease, ATP-dependent protease, Lon family. Members of this protein family resemble the widely distributed ATP-dependent protease La, also called Lon and LonA. It resembles even more closely LonB, which is a LonA paralog found in genomes if and only if the species is capable of endospore formation (as in Bacillus subtilis, Clostridium tetani, and select other members of the Firmicutes) and expressed specifically in the forespore compartment. Members of this family are restricted to a subset of spore-forming species, and are very likely to participate in the program of endospore formation. We propose the designation LonC [Protein fate, Degradation of proteins, peptides, and glycopeptides, Cellular processes, Sporulation and germination]
RLEVQVNALYNVLKNVLGPKRLRVKAIKYKALGLIKSEKVEEKVLALQKIVYEDPGLDTVPDPRELPEIL
EDTEDHIADILARRTVENRIERKVETRMQERQNKYLEEIRLQVLKEEKGPENSSTLKKLERLEKLEKKKL
HKSAQSLLRPRAFSEIVGQERAIKALLAKVASPFPQHIILYGPPGVGKTTAARLALEEAKKLKHTPFAED
APFVEVDGTTLRWDPREVTNPLLGSVHDPIYQGARRDLAETGVPEPKTGLVTDAHGGVLFIDEIGELDPL
LQNKLLKVLEDKRVEFSSSYYDPDDPNVPKYIKKLFEEGAPADFVLIGATTRDPEEINPALRSRCAEVFF
EPLTPEDIALIVLNAAEKINVHLAAGVEELIARYTIEGRKAVNILADVYGYALYRAAEAGKENDKVTITQ
DDVYEVIQISRLSPYEKRKASPTYEVGHVFGLGVSGFVGSVLEIEAVAFEAKEPGKGTVRFNDTAGSMAK
DSVFNAASVIRKITGKDLSNYDIHVNVIGGGRIDGPSAGAAITLCMISAILGKPIRQDVAITGEISLRGK
IKPVGGIFEKIYGAKQAGIKTVVIPEENLKDVPQGLPGIEVKFVSTIEELMRIVF
>gnl|CDD|274345 TIGR02904, hypothetical_conserved_protein, spore coat protein YsxE. Members of this family are homologs of the Bacillus subtilis spore coat protein CotS. Members of this family, designated YsxE, are found only in the family Bacillaceae, from among the endospore-forming members of the Firmicutes branch of the Bacteria. As a rule, the ysxE gene is found immediately downstream of spoVID, a gene necessary for spore coat assembly. The protein has been shown to be part of the spore coat [Cellular processes, Sporulation and germination]
YEAVLEHYGLQPEEMEQVTGKLFKVYTDQGVFALKKLYADRNTIESFVSQIQVLSEKGFSRIVPVYPTKD
GSYYLFHGHFLYYLMPWLDIERNEERNYQHESMFQELALLHRKTVKTERVTEEELKKHYERTLSRWENIP
EGLEEFIVEAEAKWYMSPFELQACTYYHEVMQAAEFAQNKLEDWHEATKEKESWRTVLVHGKLSLSHFLY
DETRGGYFINFEKASFASPLTDLAAFFRRSFGTYPQPIDEMFEWFYTYEKTLPLTDEEIHLLTSYLAYPG
PFIRVIQNYTKQRNEKNELEQVRRLQRQF
>gnl|CDD|131951 TIGR02905, conserved_hypothetical_protein, spore coat protein YutH. Members of this family are homologs of the Bacillus subtilis spore coat protein CotS. Members of this family, designated YutH, are found only in the family Bacillaceae from among the endospore-forming members of the Firmicutes branch of the Bacteria [Cellular processes, Sporulation and germination]
ERNLYDQFGLYCDERFRVGRYEAFRANNQAYLIVPVDGLEEEELAELMAMSDYLQQAGDETVLELVKTKF
GQSSALIDGVSYYLFKAPEFNERRGVDLGRELATFHKRGRQYPRPIWKKSRIGQWKELWAKRLDQLEDWW
QSLLAQGPQTLFDEQFLETFPYYLGLTENAIQYAADTELDDEPGLADSGTICHERFGETTWLERGGLIKP
PTEWVYDHPARDLAEWIRERYMGEIRQNQRAIASFLQEYEQAAPLTPFSWRLMYARLLFPLHYFETIENY
YIAQLEHERREYEKQLQRLLDRETSHEQFLGEF
>gnl|CDD|131952 TIGR02906, Spore_coat_protein_S, spore coat protein, CotS family. Members of this family include the spore coat proteins CotS and YtaA from Bacillus subtilis and, from other endospore-forming bacteria, homologs that are more closely related to these two than to the spore coat proteins YutH and YsxE. The CotS family is more broadly distributed than YutH or YsxE, but still is not universal among spore-formers [Cellular processes, Sporulation and germination]
IDVKSIKPLRNVYKVETDSGNKCLKKINYPPERLLFILGAQEHLRKNGFNIPKILKTKDGELYVKYNGDL
YVLTEWIEGRECDFNNPIDLKKAAKGLALFHHASKGYVPPDGSKIRSKLGKWPKQFEKRLKELERFKKIA
LEKKYKDEFDKLYLKEVDYFLERGKKALELLNKSKYYDLCKEAKKIRGFCHQDYAYHNILLKDNEVYVID
FDYCTIDLPVRDLRKLIIKLMKKNGVWDLEKAKEIIEAYSSINPLSKEEKEVLYIDLAFPHKFWKIGKQY
YYKRKIWSEEKFLKKLEKIIEEEESKQEFLKEF
>gnl|CDD|274346 TIGR02907, Stage_VI_sporulation_protein_D, stage VI sporulation protein D. SpoVID, the stage VI sporulation protein D, is restricted to endospore-forming members of the bacteria, all of which are found among the Firmicutes. It is widely distributed but not quite universal in this group. Between well-conserved N-terminal and C-terminal domains is a poorly conserved, low-complexity region of variable length, rich enough in glutamic acid to cause spurious BLAST search results unless a filter is used. The seed alignment for this model was trimmed, in effect, by choosing member sequences in which these regions are relatively short. SpoVID is involved in spore coat assembly by the mother cell compartment late in the process of sporulation [Cellular processes, Sporulation and germination]
LTFSLEESVWFEKGQEVEEILGISLDPEISIDEYDDYVTIRGALELQGEYQRVPGTEVEDEPLSFDELSS
KRYIEKIEEREDGVYELSHTFPIEISIPPNRVDNIDDVYVQIESFDYELLENGCLQLTADISISGIQQEN
NLDAEPAREDEEEEESFSAEFEHPAQEETAGEEERTDEPKVEHEAHEQHEQPADDDPDEWKISASEPFQL
ESEVEASPEEENYEEYEDETELEVEDEEKALDEQTEDPQQEDALAGDAKKALEEEEEKGERPENATYLTK
LFRKAEEEQFTKLRMCIVQEGDTIETIAERYEISVSQLIRHNQLEDFEVNEGQILYIP
>gnl|CDD|131954 TIGR02908, Cytochrome_c_oxidase_subunit_4B, cytochrome c oxidase, subunit IVB. This model represents a small clade of cytochrome oxidase subunit IV's found in the Bacilli [Energy metabolism, Electron transport]
MTDNMSTGKINSDLEFQKAKNAEEMKKQIVTFALMIFLTLIAFFAVMLDEIDKWFVIPFILLLAAVQVAF
QLYYFMHMKDKGHEVPAQFIYGGVFVTMLVVLAFTTITWW
>gnl|CDD|131955 TIGR02909, conserved_hypothetical_protein, uncharacterized protein, YkwD family. Members of this protein family represent a subset of those belonging to pfam00188 (SCP-like extracellular protein). Based on currently cuttoffs for this model, all member proteins are found in Bacteria capable of endospore formation. Members include a named but uncharacterized protein, YkwD of Bacillus subtilis. Only the C-terminal region is well-conserved and is included in the seed alignment for this model. Three members of this family have an N-terminal domain homologous to the spore coat assembly protein SafA
LTAEEKRVVELVNAERAKNGLKPLKADPELSKVARLKSEDMRDKNYFSHTSPTYGSPFDMMKKFGISYRM
AGENIAYGNSTVEAVHNAWMNSPGHRANILNPNYTEIGVGYVEGGSGGIYWTQMFIG
>gnl|CDD|131956 TIGR02910, anaerobic_sulfite_reductase_subunit_A, sulfite reductase, subunit A. Members of this protein family include the A subunit, one of three subunits, of the anaerobic sulfite reductase of Salmonella, and close homologs from various Clostridum species, where the three-gene neighborhood is preserved. Two such gene clusters are found in Clostridium perfringens, but it may be that these sets of genes correspond to the distinct assimilatory and dissimilatory forms as seen in Clostridium pasteurianum. Note that any one of these enzymes may have secondary substates such as NH2OH, SeO3(2-), and SO3(2-). Heterologous expression of the anaerobic sulfite reductase of Salmonella confers on Escherichia coli the ability to produce hydrogen sulfide gas from sulfite [Central intermediary metabolism, Sulfur metabolism]
MGFKITPEEFNLLLQKLNKDYKVYAPKALFGKGTFSDTDNIRYQEISGVEEIEFHEKSHFSPKEIILPIT
ETLFYFTEDTVQEAETDKKNIIIFLRSCDINAVKRLDYIYLKNGNEDYYYKRLREKVKFVLIECEESFEN
CFCVSMGTNKTDCYSAAVRFSEEGVLVDIKDEFIEAAFKEVGEELEVEPSFVSENKEKVKIPDKIRDKIF
RSDFWDEYDSRCIACGRCNTVCPTCTCFSMQDVFYKDNPKAGERRRVWASCMVDGFTNMAGGHGFREKKG
QRMRFKVMHKVNDYKKRNGYHMCVGCGRCDDICPEYISFSNCINKLTAAVREVN
>gnl|CDD|131957 TIGR02911, Anaerobic_sulfite_reductase_subunit_B, sulfite reductase, subunit B. Members of this protein family include the B subunit, one of three subunits, of the anaerobic sulfite reductase of Salmonella, and close homologs from various Clostridum species, where the three-gene neighborhood is preserved. Two such gene clusters are found in Clostridium perfringens, but it may be that these sets of genes correspond to the distinct assimilatory and dissimilatory forms as seen in Clostridium pasteurianum [Central intermediary metabolism, Sulfur metabolism]
NSYLPFKSEILEIIKHTDIEYTFRMSYDGPVKPGQFFEVSLPKYGEAPISVSGIGEGYIDLTIRRVGKVT
DEVFTLKEGDNLFLRGPYGNGFDVDNYKHKELVVVAGGTGVAPVKGVVEYFVKNPKEIKSLNLILGFKTP
DDILFKEDIAEWKGNINLTLTLDEAEEDYKGNIGLVTKYIPELTLKDIEEVQAIVVGPPIMMKFTVQELL
KKGIKEENIWVSYERKMCCGVGKCGHCKIDDVYVCLDGPVFNYTKAKRLID
>gnl|CDD|131958 TIGR02912, Anaerobic_sulfite_reductase_subunit_C, sulfite reductase, subunit C. Members of this protein family include the C subunit, one of three subunits, of the anaerobic sulfite reductase of Salmonella, and close homologs from various Clostridum species, where the three-gene neighborhood is preserved. Two such gene clusters are found in Clostridium perfringens, but it may be that these sets of genes correspond to the distinct assimilatory and dissimilatory forms as seen in Clostridium pasteurianum. Note that any one of these enzymes may have secondary substates such as NH2OH, SeO3(2-), and SO3(2-). Heterologous expression of the anaerobic sulfite reductase of Salmonella confers on Escherichia coli the ability to produce hydrogen sulfide gas from sulfite [Central intermediary metabolism, Sulfur metabolism]
DINTKALKKNAFRVTKVRGKTAIRVRVPGGILPAKYLSVLQNIAETYGNGKVHITTRQGFEIPGIRFEDI
DEVNKALQPIIEGLEINQEDVQKGYSASGTRNITACIGNRVCPFANYDTTKFAKRIEKAVFPNDYHVKIA
LTGCPNDCAKARMHDFGIIGMTEPQYDADRCIGCGACVKVCKKKAVGALSFENYKVVRDHSKCIGCGECV
LKCPTGAWTRSEEKYYKLRLMGRTGKKNPRLGEDFIKWVDEDSIVKIILNTYDYITEYIDKNAPGGKEHI
GYIVDRTGYQEFKKWALKDVQLNPKAEVAENIYW
>gnl|CDD|131959 TIGR02913, hypothetical_protein, probable extracellular repeat, HAF family. The model for this family detects a homology domain of about 40 amino acids. Member proteins always have a least two tandem copies and as many as seven. The spacing between repeats as defined here usually is four residues exactly. This repeat is named for a tripeptide motif HAF found in most members. Some members proteins are found in species with no outer membrane (archaea and Gram-positive bacteria) while others have C-terminal autotransporter domains that suggest that the repeat region is transported across the outer membrane. This domain seems likely to be an extracellular protein repeat
ATGINNDGQVVGYSTTANGETHAFLYSDGTMIDLGTLGG
>gnl|CDD|274347 TIGR02914, hypothetical_protein, EpsI family protein. In Methylobacillus sp strain 12S, EpsI is encoded immediately downstream of the multiple-membrane-spanning putative transporter EpsH, and is predicted to be a periplasmic protein involved in, but not required for, expression of the exopolysaccharide methanolan. In a number of other species, protein homologous to EpsI is encoded either next to EpsH or, more often, combined in a fused gene. We have proposed renaming EpsH, or the EpsHI fusion protein, to exosortase, based on its phylogenetic association with the PEP-CTERM proposed protein targeting signal [Transport and binding proteins, Unknown substrate]
EASFPKAFGGWRGASAPLEDWVPDFLGADDYLSRTYRNRDGRVVGLYIAYYRDQRQGGELHSPENCLPGS
GWAWLSSAKRTLSLGGGPIPVRRLVLASGGRRELVWYWYWVGGRTTASDYAAKLALLLDRLTGGRPDGAL
VRVSTPVADDSIEAARAVLRDFLREMAPVLPGFL
>gnl|CDD|274348 TIGR02915, Two_Component_Transcriptional_Regulator_Fis_family, PEP-CTERM-box response regulator transcription factor. Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158) [Regulatory functions, DNA interactions]
LLIVEDDLGLQKQLKWSFADYELAVAADRESAIALVRRHEPAVVTLDLGLPPDADGASEGLAALQQILAI
APDTKVIVITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGTALRG
LITSSPGMQKICRTIEKIAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESEL
FGYEKGAFTGAVKQTLGKIEYAHGGTLFLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCA
TNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDGDAVLLANAFLERFARELKRKTKGFTDDALRALE
AHAWPGNVRELENKVKRAVIMAEGNQITAEDLGLDARERAETPLEVNLREVRERAEREAVRKAIARVDGN
IARAAELLGITRPTLYDLMKKHGIK
>gnl|CDD|274349 TIGR02916, sensor_histidine_kinase, putative PEP-CTERM system histidine kinase. Members of this protein family have a novel N-terminal domain, a single predicted membrane-spanning helix, and a predicted cystosolic histidine kinase domain. We designate this protein PrsK, and its companion DNA-binding response regulator protein (TIGR02915) PrsR. These predicted signal-transducing proteins appear to enable enhancer-dependent transcriptional activation. The prsK gene is often associated with exopolysaccharide biosynthesis genes [Protein fate, Protein and peptide secretion and trafficking, Signal transduction, Two-component systems]
LGYGAAAVAYLFLSLLLVTAWRQRLAGGLLLLAAALSAVWALASAALVYMDYPWPLLVLVLEVFRDAAWL
AFLLTLLRRPATSGKPFNQRPKLLQRLAAPLVFGLLCLQAFLVMPDLAPEDLLFALWSRNYFLLGFLLLA
VIGLVLVEQLYRNAPLESRWAIKFLCLGLGALFVFDFYLYADALLFRRLDTDVWPARGLVAALVVPLIAV
SAARNPDWSVRIAVSREMAFHSATLLGAGLYLLAMAGAGYYLRYFGGEWGDAFQLAFLFAAGLLLAVLLF
SGTLRARLRVFISKHFFRYKYDYREEWLRFTQTLSEARSSDDLGERVIRALAQLVESPGGVLWLKSGNDG
LYRPAARWNQPLAQAFEPSDSAFCQFLQESGWIINLEEARSEPDHYSGLVLPEWLREIPNAWLIVPLISG
EELVGFVVLARPRTAGEFNWEVRDLLKTAGRQAASYLAQMEASEALAEARQFEAFNRMSAFVVHDLKNLV
AQLSLLLRNAERHKDNPEFQDDMLETVENAVNRMKKLLAQLRSKGLEEEKLCVDLVDLLRRAIASKRAQG
PRPEVSIDTDLSVRADRERLERVLGHLVQNALEATPGEGRVAIRVERECGAARIEIEDSGCGMSPAFIRE
RLFKPFDTTKGAGMGIGVYECRQYVEEIGGRIEVESTPGQGTIFTLVLP
>gnl|CDD|274350 TIGR02917, TPR_domain_protein, putative PEP-CTERM system TPR-repeat lipoprotein. This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator
FIKITALLCIALALSACGDQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFLLGKIYLALG
DYAAAEKELRKALSLGYPKNQVLPLLARAYLLQGKFQQVLDELPGKTLLDDEGAAELLALRGLAYLGLGQ
LELAQKSYEQALAIDPRSLYAKLGLAQLALAENRFDEARALIDEVLTADPGNVDALLLKGDLLLSLGNIE
LALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDFQKKNYEDA
RETLQDALKSAPEYLPALLLAGASEYQLGNLEQAYQYLNQILKYAPNSHQARRLLASIQLRLGRVDEAIA
TLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADL
ETAAQLDPELGRADLLLILSYLRSGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEK
ALSIEPDFFPAAANLARIDIQEGNPDDAIQRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLEKAA
ELNPQEIEPALALAQYYLGKGQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLAL
QPDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLLAAKRTESAKKIAKSLQKQHP
KAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSSQNAIKLHRALLASGNTAEAVKTLEAWLKTHPNDA
VLRTALAELYLAQKDYDKAIKHYQTVVKKAPDNAVVLNNLAWLYLELKDPRALEYAERALKLAPNIPAIL
DTLGWLLVEKGEADRALPLLRKAVNIAPEAAAIRYHLALALLATGRKAEARKELDKLLN
>gnl|CDD|131964 TIGR02918, lipopolysaccharide_biosynthesis_protein, accessory Sec system glycosylation protein GtfA. Members of this protein family are found only in Gram-positive bacteria of the Firmicutes lineage, including several species of Staphylococcus, Streptococcus, and Lactobacillus. Members are associated with glycosylation of serine-rich glycoproteins exported by the accessory Sec system [Protein fate, Protein modification and repair]
MTIYNINFGIGWASSGVEYAQAYRAQLFRKLNIEAKFIFLDFIQNENIQTLTANIGFKDDEIIWLYQYFT
DIKIAPTTYTVDDLEKELGLEITRREKNGKVLRLFFNNQSNFVTCYLKNENKDIVDRAEYVSNGKLIRKD
FYSYTRYFSEYYAPADNKAKLYQRTFYNEDGSIAYDEYIDGKESVFVFKDKILYSKQEFIAYFLKQLNLT
KSDIVILDRSTGIGQAVLENKGPAKLGVVVHAEHYSENATNETYILWNNYYEYQFSNADYIDFFITATDI
QNQILQEQFKKYTNIEPKIYTIPVGSLDSLQYPEQERKPFSIITASRLAKEKHIDWLVKAVVKAKKSLPE
LTFDIYGEGGEKSKLRKIIAENQAEDYIQLKGHRNLSEIYKDYELYLSASTSEGFGLTLMEAIGSGLGMI
GFDVNYGNPTFIEDGQNGYLIPIDEEEDDEDQIITALAEKIVEYFNENDLDAMHEYSYQIAEGFLTKEII
EKWKKLVEEV
>gnl|CDD|274351 TIGR02919, conserved_hypothetical_protein, accessory Sec system glycosyltransferase GtfB. Members of this protein family are found only in Gram-positive bacteria of the Firmicutes lineage, including several species of Staphylococcus, Streptococcus, and Lactobacillus [Protein fate, Protein modification and repair]
MINLFDNFDQESIDLYRSLKFAGLKNPTIVINDDGFLPDDVLSPYRFFTGYEDTNGKPLYFNEVPVPDFW
EIKGNNNSAEIYDLGEKRGKIFYKENYKTRIVKEVEWLDKNGRLRYVDHYNKFGFCFAQTVYDANGKAIL
KRYFDKDGKEVIVENFVTGDIILNWENKSYFFASKVEFVTFYLSQLEINLSHIFINSLSTPFLVSYGLPE
DGSDVLFWQEPITDDIPGNMKLLLDNETRNKKIIIPNKNEYEKIKELLDNEYQEQISQLGYLYPFKKDNK
YRKQALILTNSDQIEHLEEIVQALPDYHFHIAALTEMSSKLMSLDKYDNVKLYPNITTQKIQELYQTCDI
YLDINHGNEILNAVRRAFEYNLLILGFEETAHNRDFIASENIFEHNEVDQLISKLKDLLNDPNQFRELLE
QQREHANDISKEQFKEVL
>gnl|CDD|131966 TIGR02920, preprotein_translocase_SecY_family_protein, accessory Sec system translocase SecY2. Members of this family are restricted to the Firmicutes lineage (low-GC Gram-positive bacteria) and appear to be paralogous to, and much more divergent than, the preprotein translocase SecY. Members include the SecY2 protein of the accessory Sec system in Streptococcus gordonii, involved in export of the highly glycosylated platelet-binding protein GspB [Protein fate, Protein and peptide secretion and trafficking]
IIYKKILFTCFILIIYVLGSYIPIPFVEVSKQDMEGVKNSFFKIAIANTGGNLTTLSIFSLGLGPWMTSM
IILQLFSFTKSDGFDAQSPKEQQYRERFLTLIIAIIQGLAIIHSFTNKNGLSDFNMLLATLILVTGTCLL
VWLADLNAKYGIGGSMPIVLVSMLKNIPSNVFELFQMSYIWLIALLILLTLVALFLLAFIERAEYRIPVN
DISLHNRSNLMSYLPIKLNPAGGMMYMYVMSLLMLPQYIIILLGRIFPNSSLINNWVFQFSFSSPVGILI
YLILQMLLSYFFTFVNINPKEISKSFRKSGNYIPGIAPGKDTQRYLNRLARRFCWFGGVFNAFQLGIPLY
FALFVPHLLTEAYIPGQFMMITGMSFNIADEIRTILYFDRYKPLL
>gnl|CDD|131967 TIGR02921, PEP_integral, PEP-CTERM family integral membrane protein. Members of this protein family, found in eighteen genera so far, have a PEP-CTERM sequence at the carboxyl-terminus (see model TIGR02595), but are unusual among PEP-CTERM proteins in having multiple predicted transmembrane segments. The function is unknown. It is proposed that an exosortase (see TIGR02602), recognizes and cleaves PEP-CTERM proteins in a manner analogous to the cleavage of LPXTG proteins by sortase (see Haft, et al., 2006). In at least six species, a gene encoding what appears to be a dedicated (single target) exosortase is adjacent. In that subset, the PEP-CTERM motif takes the form VPEPxxWxL
LKGFLAACCEGIFWFWNLTFASLTGLGILPFFGLPAILAAAIGDHPIEFALALILLIAIPAICIGIGGTC
FLKNPTALIKLFYGVEAPIFFICLLRLFLIRELNPASSHILINIGIAIAAFAACLFGGVASRFKIGLQWL
QLLAAMLMLLFGIYAAALLAFFAIPAAAGFFELLEEIEFEHLGDIFNYILFHTAFICGLFIISMWLIVLA
FSATLFIALPFALTALYIHEFAKELKAAAAEHGNAKAFAGAAAIIAAFALLFASLNQQPQQEAFELLAFA
DKNDQDGETIISIPREEHDAIRKGLINAYLAPYRYLSSREENGAIFAAYLGAFDGADHSAADGLQAIFNF
LASPFLYDGAYFDEDKAKAAKLYAAFFDQPIEKAEKEAILHAIQATFDEGEPKAGLLDILEKKVLIANMA
ITVEEHGDNADIEIVETLENQTPENHEVFFHFSLPEEAAITGLWLGDDAKDDDKFAFALAPRGAAQKVYN
DEVQQERPIDPALLEQVGPRHYRLRAFPIPPRRANYNNNMGLIEGQDPEPDEMNLTFEYKTLGNDKGAWA
LPDLGEKRNAFWSDQTKRILNDKEIGFEEDAWLEEFAPASAAAPPALHDASLDAGQKILAKPLSGADAQW
DIPKNTQPVAILIDGSRSMGEHAGELTQALKQLKQHDFADEDFLCNDACLSISAPPGADPTRLDNLQQFQ
PEKVAFYGDILPMEMLAAFNNLKGDQAYDAVLLLSDAGSYELEKNFKLKAAQMAPLWLVHLGETLAGAYH
DGIIDLLKDSGGGVALDIAEAIAAHQFAQKRALDDGLFAVTNGYAWYAEAGADADAALSNAKQEADFFPA
IAARQLIEGLAKQIDLDDLKSLDAIHAIAKAEHIVSDYSSMIVLVEDEQKKALEEAEAAADRFDREVENG
KENFSAPMDMFKASPVPEPEEGILLGLAAIALGFAIFAKKRR
>gnl|CDD|131968 TIGR02922, protein_of_unknown_function_DUF2375, TIGR02922 family protein. Two members of this family are found in Colwellia psychrerythraea 34H and one each in various other species of Colwellia and Shewanella. One member from C. psychrerythraea is of special interest because it is preceded by the same cis-regulatory site as a number of genes that have the PEP-CTERM domain described by TIGR02595 [Hypothetical proteins, Conserved]
MCEAKAKVTVIYYCAPELLLMHNLQSFPVNESGRVMIPQEFKRGKSIIAVCEGEITILNSVGDRVVS
>gnl|CDD|274352 TIGR02923, V-type_ATP_synthase_subunit_C, ATP synthase A1, C subunit. The A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The C subunit is part of the hydrophilic A1 "stalk" complex (AhaABCDEFG), which is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex
KYSPYAYPNARVRAMESRLLKEEDFNELLEMRGTDEIVRFLEETDYKKELDELGSKSYGVDLIEHALDAN
LAKTYEKLFRISPGASRDLIRLYLKKWDVWNIKTLIRAKYANASAEEVEDLLIPAGEFLEKRIKELAEAK
TIEEIVEALEGTPYYGPLQEALAGNGDLSPIENELDRMYYEKLLKYVGSPSDDETKLFTEFIKTEVDIRN
LKTLLRLKAAGLSPDEIMPYTIPGGYELDEEKLAPLAHIESIDEVVSALDGTKYGEDISEVLSEEEKSVA
VFERALDEYLIKMATKLSLRYPLSVGPVLGYILKKEREVRNLRAIARGKEEGLPPEEIKEQLV
>gnl|CDD|274353 TIGR02924, Isocitrate/isopropylmalate_dehydrogenase_LeuB, isocitrate dehydrogenase. This family of mainly alphaproteobacterial enzymes is a member of the isocitrate/isopropylmalate dehydrogenase superfamily described by pfam00180. Every member of the seed of this model appears to have a TCA cycle lacking only a determined isocitrate dehydrogenase. The precise identity of the cofactor (NADH -- 1.1.1.41 vs. NADPH -- 1.1.1.42) is unclear [Energy metabolism, TCA cycle]
IPITVAYGDGIGPEIMEAVLLILKEAEAPIDIETIEIGEKVYKKGWPSGISPSSWESIRRTKVLLKAPIT
TPQGGGHKSLNVTLRKTLGLYANIRPCVSYHPFIETKSPNLNIVIVRENEEDLYTGIEYRQTPDTYECTK
LITRSGSEKICRYAFEYARKHNRKKVTCLTKDNIMKMTDGIFHKIFDKIAAEYPDIESEHYIVDIGMARL
ATNPENFDVIVTPNLYGDILSDVAAEISGSVGLAGSANIGEEYAMFEAVHGSAPDIAGQNIANPSGLLNA
AIQMLVHIGQSDIAQLIYNAWLKTLEDGVHTADIYNEKTSKQKVGTKEFAEAVTANLGKKPETLPKALYS
NSFHESHINYSREQSYKVKVLVGVDIFIKWDGSSDANQLATLLQKISNDDIKLKLISNKGLKIWPNETPV
TSYSDQWCCRFIAKTNKIISNTDINNLLNRLEQKKIDVVKMEKLYLFDGVAGF
>gnl|CDD|131971 TIGR02925, hypothetical_protein_Nmul_A0241, peptidyl-prolyl cis-trans isomerase, EpsD family. Members of this family belong to the peptidyl-prolyl cis-trans isomerase family and are found in loci associated with exopolysaccharide biosynthesis. All members are encoded near a homolog of EpsH, as detected by TIGR02602
ITSLFFVLLVGILAGCGEKEAQESASQVAAKVNGVEISVHQLNYALQRTPNPGASSDAARARRQVLDRLV
DQELVVGKALEEKLDRSPDVVMALEAAKREILARAYLRQLAGAQSKPSPEEAKSYFQEHPQLFAERKLYN
LQEIALPPDMELLDELRAMVENGKPLEDILAWLKAKNVPFNASSAARPAEQLPAEILAVLAKLKPGAPLV
VQGPNNVLILVLADAQPAPVTL
>gnl|CDD|131972 TIGR02926, Uncharacterized_protein_AF_1158, ATP synthase archaeal, H subunit. he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes
LEEIKKAEEDAEELIEEAEEERKQRIAEAREEARELLEEAEEEASKLGEEIIKEAEEEIEKEAEKIREEG
EKEIEAMKSKAKEKI
>gnl|CDD|200219 TIGR02927, putative_dihydrolipoamide_acyltransferase, 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase. This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817)
MAESVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVG
GVLAIIGEPGEAGSEPAPAAPEPEAAPEPEAPAPAPTPAAEAPAPAAPQAGGSGEATEVKMPELGESVTE
GTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAPAEP
AEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSGDSGPYVTPLVRKLAKDKG
VDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAAAAKPAEPDTAKLRGTTQKMNRI
RQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNA
SYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFT
ITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRF
LTTIKKRLEEGDFEGDLGL
>gnl|CDD|274354 TIGR02928, ORC1-type_DNA_replication_protein, orc1/cdc6 family replication initiation protein. Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other [DNA metabolism, DNA replication, recombination, and repair]
IFRNRDLLEPDYVPDRIVHRDEQIEELAKALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKELEEAAED
RDVRVVTVYVNCQILDTLYQVLVELANQLRGSGEEVPTTGLSTSEVFRRLYKELNERGDSLIIVLDEIDY
LVGDDDDLLYQLSRARSNGDLDNAKVGVIGISNDLKFRENLDPRVKSSLCEEEIIFPPYDAEELRDILEN
RAEKAFYDGVLDDGVIPLCAALAAQEHGDARKAIDLLRVAGEIAEREGAERVTEDHVEKAQEKIEKDRLL
ELIRGLPTHSKLVLLAIANLAANDEDPFRTGEVYEVYKEVCEDIGVDPLTQRRISDLLNELDMLGLVEAE
ERNKGRGGRTREYSL
>gnl|CDD|131975 TIGR02929, Nitrogenase_iron-iron_protein_delta_chain, Fe-only nitrogenase, delta subunit. Nitrogenase, also called dinitrogenase, is the enzyme of biological nitrogen fixation. The most wide-spread and most efficient nitrogenase contains a molybdenum cofactor. This protein family, AnfG, represents the delta subunit of the Fe-only alternative nitrogenase. It is homologous to VnfG, the delta subunit of the V-containing (vanadium) nitrogenase [Central intermediary metabolism, Nitrogen fixation]
KMDQLEDYIMKHCLWQFNSRGWDREIQNEGILMKTRQILCGENAREDTSADRCYWVDAVTLAGAYKRRFP
WLEDMTKDEIKTLMQALHEKMDHLTIKGSLNLELTKEHY
>gnl|CDD|131976 TIGR02930, vanadium_dinitrogenase_delta_subunit, V-containing nitrogenase, delta subunit. Nitrogenase is the enzyme of biological nitrogen fixation. The most wide-spread and most efficient nitrogenase contains a molybdenum cofactor. This protein family, VnfG, represents the delta subunit of the V-containing (vanadium) alternative nitrogenase. It is homologous to AnfG, the delta subunit of the Fe-only nitrogenase [Central intermediary metabolism, Nitrogen fixation]
KVEQITAYIQERCLWQFFSRTWDREENIEGVMTMAGKLLNGEKINLETPMDKLFYADAKNLASDIKERFP
WISELDKDQILELVESVKKRLVEITITRSLNGELNHSLY
>gnl|CDD|131977 TIGR02931, Nitrogenase_iron-iron_protein_beta_chain, Fe-only nitrogenase, beta subunit. Nitrogenase is the enzyme of biological nitrogen fixation. The most wide-spread and most efficient nitrogenase contains a molybdenum cofactor. This protein family, AnfK, represents the beta subunit of the iron-only alternative nitrogenase. It is homologous to NifK and VnfK, of the molybdenum-containing and the vanadium (V)-containing types, respectively [Central intermediary metabolism, Nitrogen fixation]
TCEVKEKAREGTINPIFTCQPAGAQFASIGIKDCIGIVHGGQGCVMFVRLLISQHMKESFEIASSSLHED
GAVFGALDRVEEAVDVLLTRYPDVKVVPIITTCSTEIIGDDVDGLISKLNEELLKEKFPDREVHLIPIHT
PSFVGSMITGYDVAVHDFVKHFAKKDKPNDKINLITGWVNPGDVKELKHLLEEMDIEANVLFEIESFDSP
LMPDKSAVSHGSTTIEDLTDTANAKGTIALNRYEGMKAADYLQKKFDVPAIIGPTPIGIRNTDTFLQNLK
KMTGKPIPESLVKERGIAIDAIADLTHMFLADKRVAIYGNPDLVIGLAEFCLDLEMKPVLLLLGDDNSGY
VDDPRIKALQENVDYDMEIVTNADFWELESRIKNQGLELDLILGHSKGRFISIDYNIPMVRVGFPTYDRA
GMYRHPVVGYGGAIWLAEQMANTLFADMEAKKNKEWILNVW
>gnl|CDD|131978 TIGR02932, Nitrogenase_vanadium-iron_protein_beta_chain, V-containing nitrogenase, beta subunit. Nitrogenase is the enzyme of biological nitrogen fixation. The most wide-spread and most efficient nitrogenase contains a molybdenum cofactor. This protein family, VnfK, represents the beta subunit of the vanadium (V)-containing alternative nitrogenase. It is homologous to NifK and AnfK, of the molybdenum-containing and the iron (Fe)-only types, respectively [Central intermediary metabolism, Nitrogen fixation]
VSPKEREGVINPMYDCQPAGAQYAGIGVKDCIPLVHGGQGCTMFVRLLFAQHFKENFDIASTSLHEESAV
FGGAKRIEEGVLTLARRYPNLRVIPIITTCSTETIGDDIEGSIRKVNRALKKEFPDRKIKLVPVHTPSFK
GSQVTGYAECVKSVIKTIAAKKGEPSGKLNVFPGWVNPGDVVLLKHYFSEMGVDANILMDTEDFDSPMLP
DKSIFTHGRTTVEDIADSANAIATLALAKYEGGNTAEFLQETFDVPSILVPTPYGIKNTDAMLKNISELT
GKPIPESLVRERGIALDALADLAHMFFANKKVAIFGHPDLVIGLAEFCLEVELEPVLLLLGDDNSKYKKD
PRIEELKNKANFDIEVVWNADLWELEKRIKAKLDIDLIMGHSKGRYVAIDANIPMVRVGFPTFDRAGLYR
KPVIGYRGAMWLGEMIANAMFAHMEYKHDREWILNTW
>gnl|CDD|131979 TIGR02933, Putative_peptidyl-prolyl_cis-trans_isomerase_NifM, nitrogen fixation protein NifM. Members of this protein family, found in a subset of nitrogen-fixing bacteria, are the nitrogen fixation protein NifM. NifM, homologous to peptidyl-prolyl cis-trans isomerases, appears to be an accessory protein for NifH, the Fe protein, also called component II or dinitrogenase reductase, of nitrogenase [Central intermediary metabolism, Nitrogen fixation]
RYSRWKLAHEMWNCAPGELSPDQLQQFDQAWQRQRHIEQAVVRAADEIGVVIPPSLLEEAPQALAQALDE
QALDAAERRAMLAHHLRLEAQLACVCAQAPQPDDADVEAWYRRHAEQFKRPEQRLTRHLLLTVNEDDREA
VRTRILAILRRLRGKPAAFAEQAMRHSHCPTAMEGGLLGWVSRGLLYPQLDAALFQLAEGELSPPIESEI
GWHLLLCEAIRPARPLTLEEALPRARDRLQLRQQKAYQRQWLVQLI
>gnl|CDD|274355 TIGR02934, hypothetical_protein_WS1400, probable nitrogen fixation protein FixT. This largely uncharacterized protein family is assigned a role in nitrogen fixation by two criteria. First, its gene occurs, generally, among genes essential for expression of active nitrogenase. Second, its phylogenetic profile closely matches that of nitrogen-fixing bacteria. However, mutational studies in Klebsiella pneumoniae failed to demonstrate any phenotype for deletion or overexpression of the protein
MKVMIRRNRAGGLSAYVPKKDLEEVIVAVEIKEELWGGWVTLANGWRLELPEIPSETRLPITVEAKKL
>gnl|CDD|131981 TIGR02935, UPF0460_protein_in_nifX_3'region, probable nitrogen fixation protein. Members of this protein family, called DUF269 by pfam03270, are strictly limited to nitrogen-fixing species, although not universal among them. The gene typically is found next to the nifX gene (see TIGRFAMs model TIGR02663) [Central intermediary metabolism, Nitrogen fixation]
ESPFVKELVRQIRAQDTYGAWEGKSDAELLAPYIVTKEERREIPIIGDPDPETLWRIELFYNAVALAIEK
RTGLMASPMMKLHHEGFGRVLLIAGRLVVVNKTMRDVHRFGFDSLEKLAEEGDKLVSEAIAAIEKYPDVA
>gnl|CDD|274356 TIGR02936, fdxN_nitrog, ferredoxin III, nif-specific. Members of this family are homodimeric ferredoxins from nitrogen fixation regions of many nitrogen-fixing bacteria. As characterized in Rhodobacter capsulatus, these proteins are homodimeric, with two 4Fe-4S clusters bound per monomer. Although nif-specific, this protein family is not usiveral, as other nitrogenase systems may substitute flavodoxins, or different types of ferredoxin [Central intermediary metabolism, Nitrogen fixation]
TGLTRGGSEWTPQFVTSIDQEKCIGCGRCYKVCGRDVLTLKGINEEGELVASDDDDDEIERKVMVVANPG
NCIGCGACARVCPKKCQTHAP
>gnl|CDD|274357 TIGR02937, RNA_polymerase_sigma_factor, RNA polymerase sigma factor, sigma-70 family. This model encompasses all varieties of the sigma-70 type sigma factors including the ECF subfamily. A number of sigma factors have names with a different number than 70 (i.e. sigma-38), but in fact, all except for the Sigma-54 family (TIGR02395) are included within this family. Several Pfam models hit segments of these sequences including Sigma-70 region 2 (pfam04542) and Sigma-70, region 4 (pfam04545), but not always above their respective trusted cutoffs
EAFEELYERYLPLVYRYARRYLGDDADAEDLVQEAFLKLLEALDRFDPEGSFKAWLFRIARNLILDYLRR
KRRLRRELDLLEELLDSDPSPEEELEQEEEREALREALEKLPEREREVLVLRYLEGLSYKEIAEILGISV
GTVKRRLKRARKKLRELL
>gnl|CDD|131984 TIGR02938, Nitrogen_fixation_regulatory_protein, nitrogen fixation negative regulator NifL. NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]
LPPEAYRQTVDQAPLAISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLA
EQKPWAGKLLNRRKDGELYLAELTVAPVLNEAGETTHFLGMHRDITELHRLEQVVANQKLLIESVVDAAP
VAFVLLDPTGRVILDNQEYKKLATDLRVKEPAHTVLDLLREAWREALAENWPQQLAFSNREARFDRGGGR
PARWLSCTGSVIGMESDCADSFFCAAEQPYLLLTIADISNLREEQERARLSALQALMAEEERLEAIRETL
SAAIHRLQGPMNLISAAISVLQRRGDDAGNPASAAMLQQALSAGREHMEALRQVIPQSPQEIVVPVNLNQ
ILRDVITLSTPRLLAAGIVVDWQPAATLPAILGRELQLRSLFKALVDNAIEAMNIKGWKRRELSITTALN
GDLIVVSILDSGPGIPQDLRYKVFEPFFTTKGGSRKHIGMGLSVAQEIVADHGGIIDLDDDYSEGCRIIV
EFRV
>gnl|CDD|131985 TIGR02939, Sigma_factor_ECF_subfamily, RNA polymerase sigma factor RpoE. A sigma factor is a DNA-binding protein protein that binds to the DNA-directed RNA polymerase core to produce the holoenzyme capable of initiating transcription at specific sites. Different sigma factors act in vegetative growth, heat shock, extracytoplasmic functions (ECF), etc. This model represents the clade of sigma factors called RpoE. This protein may be called sigma-24, sigma-E factor, sigma-H factor, fecI-like sigma factor or alternative sigma factor AlgU
MSPQELDLELVERVQRGEKQAFDLLVRKYQHKVVALVGRYVRDSSEVEDVAQEAFVKAYRALSSFRGDSA
FYTWLYRIAVNTAKNHLVAQGRRPPTSDVEIEDAEHFEGADRLREIDTPERLLLSRELEQTVMRAVEALP
EDLRTAITLRELEGLSYEDIARIMDCPVGTVRSRIFRAREAIAIRLRPLL
>gnl|CDD|274358 TIGR02940, conserved_hypothetical_protein, Fe-only nitrogenase accessory protein AnfO. Members of this protein family, called Anf1 in Rhodobacter capsulatus and AnfO in Azotobacter vinelandii, are found only in species with the Fe-only nitrogenase and are encoded immediately downstream of the structural genes in the above named species
KIAVFVDDEGQISSIFDPGFILLYEGSGGEWKLLKDIENAVCPAKGLAAVRAAVADMVKQLDDCRVFLAS
EVRGIAYSLLQEMGFQVWLSEGPVLDQLDSVAKKELERAKEAAKEARAERSSGRRGSDRFDIKEVLVGDV
NKGDFRLDLEAILADDPRLNSRKILIPVLKGKPFRQLDILCDHIPRWFDRELRALGLRAEIMEDRGNGVA
LRVT
>gnl|CDD|131987 TIGR02941, RNA_polymerase_general_stress_sigma_factor_sigma_B, RNA polymerase sigma-B factor. This sigma factor is restricted to certain lineages of the order Bacillales including Staphylococcus, Listeria, and Bacillus
MEIQSQPTNLTKEDVIQWIAEFQQNQNGEAQEKLVDHYQNLVYSIAYKYSKGGPMHEDLVQVGMLGLLGA
IRRYDYSIGNAFEPFAIPTIIGEIKRYLRDKTWSVHVPRRIKELGPKIKKAIDELTDHLQRSPKIIEIAD
HLGLSEEEVLEIMEMGQSYRALSVDDVIEADSDGSTVARLDSVGEVEDGYDQTERRMVLEKILPILSERE
KSIIHCTFEENLSQKETGERLGISQMHVSRLQRQAISKLKEAAFL
>gnl|CDD|274359 TIGR02943, RNA_polymerase_sigma-24_subunit_RpoE, RNA polymerase sigma-70 factor, TIGR02943 family. This group of sigma factors are members of the sigma-70 family (TIGR02937). They and appear by homology, tree building, bidirectional best hits and one-to-a-genome distribution, to represent a conserved family
PDHDPQELEQLRRDLLRFARLQLRDRDLAEDAVQETLLAALSHRDSFAGRSALKTWLFAILKNKIIDALR
AKGREVKVSDLDDELDDEAFNALFTQNGHWAQHGQPQHWNTPEKQLENKEFWEVFEACLYHLPEQTARVF
MMREVLGFESDEICQELEISTSNCHVLLYRARLSLRACLSINWFGEEN
>gnl|CDD|131989 TIGR02944, conserved_hypothetical_protein, FeS assembly SUF system regulator, gammaproteobacterial. The SUF system is an oxygen-resistant iron-sulfur cluster assembly system found in both aerobes and facultative anaerobes. Its presence appears to be a marker of oxygen tolerance; strict anaerobes and microaerophiles tend to have different FeS cluster biosynthesis systems. Members of this protein family belong to the rrf2 family of transcriptional regulators and are found, typically, as the first gene of a SUF operon. It is found only in a subset of genomes that encode the SUF system, including the genus Xanthomonas. The conserved location suggests an autoregulatory role [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Regulatory functions, DNA interactions]
MLKISKLTDYATLVLTTLAQNDSQPYSAAEIAEQTGLNAPTVSKILKQLSLAGIVTSKRGVEGGYTLARA
PRDITVADIVKAVEGPVALTECSDDQKKCSLGNSCGVRSNWKVINSQVLDLLSSVSLADM
>gnl|CDD|131990 TIGR02945, SUF_assoc, FeS assembly SUF system protein. Members of this family belong to the broader pfam01883, or Domain of Unknown Function DUF59. Many members of DUF59 are candidate ring hydroxylating complex subunits. However, members of the narrower family defined here all are found in genomes that carry the FeS assembly SUF system. For 70 % of these species, the member of this protein family is found as part of the SUF locus, usually immediately downstream of the sufS gene [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
RLKDAVIEALKTVYDPEIPVNIYELGLIYDIDVDDDGHVDIQMTLTAPNCPVAGSMPGEVENAVRAVPGV
GSVTVELVWDPPWTPERMSEEARLELGMF
>gnl|CDD|274360 TIGR02946, Putative_diacyglycerol_O-acyltransferase_Mb3115, acyltransferase, WS/DGAT/MGAT. This bacteria-specific protein family includes a characterized, homodimeric, broad specificity acyltransferase from Acinetobacter sp. strain ADP1, active as wax ester synthase, as acyl coenzyme A:diacylglycerol acyltransferase, and as acyl-CoA:monoacylglycerol acyltransferase [Unknown function, Enzymes of unknown specificity]
LSPVDAAFLRLETPTRPMHIGALAVFEGPLSFEALRALLESRLPLAPRFRQRLREVPLGLGHPYWVEDPD
FDLDYHVRRVALPAPGTRRELLELVGRLMSTPLDRSRPLWEMHLIEGLAGGRFAVLTKVHHALADGVAGL
RLLARLLDDDPDPPPLPAPPPPPQPSTRGLLSGALSGLPSALLRRVASTAPGVVRAAGRAVEGVARSARP
ALPFTAPPTPLNGPISRKRRFAAQSLPLADVKAVAKAFGVTINDVVLAAVAGALRRYLEERGELPDDPLV
AMVPVSLRPMEDDSEGGNQVSAVLVPLPTGIADPVERLSAIHASMTRAKESGQAMGANALLALSGLLPAP
LLRLALRALARKAQRLFNLVISNVPGPREPLYLAGAKLDELYPLSPLLDGQGLNITVTSYNGQLDFGLLA
DRDAVPDPQELADALEAALEELEAAA
>gnl|CDD|131992 TIGR02947, putative_RNA_polymerase_sigma_factor, RNA polymerase sigma-70 factor, TIGR02947 family. This group of sigma factors are members of the sigma-70 family (TIGR02937). They and appear by homology, tree building, bidirectional best hits and (with the exception of a paralog in Thermobifida fusca YX) one-to-a-genome distribution, to represent a conserved family. This family is restricted to the Actinobacteria and each gene examined is followed by an anti-sigma factor in an apparent operon
VAEETKTQRAQRFERDALEYLDQLYGAALRMTRNPADAEDLVQEAYAKAFSSFHQFKPGTNLKAWLYRIL
TNTYINSYRKAQRRPQQSDDDDIEDWQLAKAASHTSNGLRSAELEALDGLPDQDIKDALQGLPEEFRQAV
YLADVEGFAYKEIAEIMGTPIGTVMSRLHRGRKQLRKQLVDVAGERGFGPRAG
>gnl|CDD|131993 TIGR02948, RNA_polymerase_ECF-type_sigma_factor_sigma-W, RNA polymerase sigma-W factor. This sigma factor is restricted to certain lineages of the order Bacillales
MDSIIKKRIKEVRKGDENAFADLVDLYKDKIYQLCYRMLGNVHEAEDVAQEAFIRAYTNIDTYDIQRKFS
TWLYRIATNLTIDRLRKRKPDFYLDDEVQGTDGLTMESQLAADEAPPEDQVISLELRDTIQQEIQALPPK
YRMVIVLKYMEDLSLKEISEILDLPVGTVKTRIHRGREALRKQLRHL
>gnl|CDD|188261 TIGR02949, putative_anti-sigma_factor, anti-sigma factor, TIGR02949 family. This group of anti-sigma factors are associated in an apparent operon with a family of sigma-70 family sigma factors (TIGR02947). They and appear by homology, tree building, bidirectional best hits and one-to-a-genome distribution, to represent a conserved family. This family is restricted to the Actinobacteria [Transcription, Transcription factors]
QDASGKTDCAEVIDHLYEFLDGECTEDDAERLRRHLAACPECLREYDLEQAVRKLLKRCCRTEAAPEELR
ARLLGRIHVIRRWE
>gnl|CDD|274361 TIGR02950, RNA_polymerase_ECF-type_sigma_factor, RNA polymerase sigma factor, SigM family. This family of RNA polymerase sigma factors is a member of the Sigma-70 subfamily (TIGR02937) and is restricted to certain lineages of the order Bacillales. This family encompasses at least two distinct sigma factors as two proteins are found in each of B. anthracis, B. subtilis subsp. subtilis str. 168, and B. lichiniformis (although these are not apparently the same two in each). One of these is designated as SigM in B. subtilis (Swiss_Prot: SIGM_BACSU) and is activated by various stressors
YREYMHDVFRYLYRLTKDKHLAEDLLQETFLKAYIHLHSFKDSSIKPWLFRIARNAFIDWYRKDKKIQTI
DDDAIGDLEQHPVESPEHHLLIKIEQEEITHHLSRLPENYRTVLILREFKEFSYKEIAELLNLSLAKVKS
NLFRARKELKKLLE
>gnl|CDD|131996 TIGR02951, anaerobic_dimethyl_sulfoxide_reductase_subunit_B, DMSO reductase, iron-sulfur subunit. This family consists of the iron-sulfur subunit, or chain B, of an enzyme called the anaerobic dimethyl sulfoxide reductase. Chains A and B are catalytic, while chain C is a membrane anchor
QYGFYVDQTRCSGCKTCQIACKDKNDLEVGVLFRRVYEYEGGGWTEEGEGFHPDVFAYYISISCNHCADP
ACVKNCPTGAMYKREEDGLVLVDQDKCIGCRYCVWACPYGAPQYDPQQGVMGKCDGCYDRVEKGLRPACV
DACPMRALDFGPIDELRAKYG
>gnl|CDD|131997 TIGR02952, RNA_polymerase_sigma-70_factor_ECF_subfamily, RNA polymerase sigma-70 factor, TIGR02952 family. This group of sigma factors are members of the sigma-70 family (TIGR02937). They and appear by homology, tree building, bidirectional best hits and one-to-a-genome distribution, to represent a conserved family. This family is found in a limited number of Gram-positive bacterial lineages
LLERAQDREEDAFARIYETYSDRVYRYIYYRVGCKYTAEDLTSEVFERVLRKIDSFKEQKNSFEAWLFTI
ARNVVNDYFRGSKRHPLFSLDVFKELLSNEPNPEEAILKEEANEKLLKALKILTPKQQHVIALRFGQNLP
IAEVARILGKTEGAVKILQFRAIKKLARQM
>gnl|CDD|131998 TIGR02953, conserved_hypothetical_protein, pentapeptide MXKDX repeat protein. Members of this protein family are small bacterial proteins, each with an N-terminal signal sequence followed by up to 11 imperfect repeats of a pentapeptide. The pentapeptide repeat usually follows the form Met-Xaa-Lys-Asp-Xaa
KRIVAAISAAAFLSLAPAALAQDAMKKDTMKKDAMGKDAMAKDAMSKDAMKKDAMKKDAMKKDGMKKDAM
KKDAM
>gnl|CDD|213752 TIGR02954, RNA_polymerase_ECF-type_sigma_factor, RNA polymerase sigma-70 factor, TIGR02954 family. This group of sigma factors are members of the sigma-70 family (TIGR02937). They and appear by homology, tree building, bidirectional best hits and one-to-a-genome distribution, to represent a conserved family. This family is found in certain Bacillus and Clostridium species
MNDEELVKKAKRGNKPAFESLIKKHKEKLYKTAFIYVKNEHDALDVIQETVYKAYLSIDKLKHPKYFNTW
LTRILINECIDLLKKKKKVIPFDPNTSIEKGECETHADSRLDLYKAIDTLNDKYQTAIILRYYHDLTIKE
IAEVMNKPEGTVKTYLHRALKKLKKRLEE
>gnl|CDD|132000 TIGR02955, periplasmic_protein_TorT, TMAO reductase system periplasmic protein TorT. Members of this family are the periplasmic protein TorT which, together with the the TorS/TorR histidine kinase/response regulator system, regulates expression of the torCAD operon for trimethylamine N-oxide reductase (TMAO reductase). It appears to bind an inducer for TMAO reductase, and shows homology to a periplasmic D-ribose binding protein
KLCALYPHLKDSYWLSINYGMVEQAKHLGVELKVLEAGGYPNLDKQLAQIEQCKSWGADAILLGTVSPEA
LNHDLAQLTKSIPVFALVNQIDSNQVKGRVGVDWYQMGYQAGEYLAQRHPKGSGPTTLAWLPGPKNRGGT
KPVTQGFRAALEGSDVEISAILWADNDKELQRNLLQDLLKKHPDIDYLVGSAVAAEAAISELRSLHMTQQ
IKLVSTYLSHGVYRGLKRGKVLFAPTDQMVLQGKLAIDQAVRYLEGKPVSFDQAPKIEALTPQHLPREVI
EDSLSPAEFRPVYQV
>gnl|CDD|274362 TIGR02956, sensor_protein_TorS, TMAO reductase sytem sensor TorS. This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072) [Signal transduction, Two-component systems]
SIGRKLLLAFSVMAALLLLSVVIGVLGLSLVAKTERTVTQSALPAMIEARQLSELSNQIIFSVQLLSNVD
DERQRQAIGKKLTLQSETLLHSLKALGELPFNEDLLARLEVLVKDIIDTLAQLGLSVGERITLQAQLQQL
SRELSEAAQEISELSQSQVANASTIALANVSGIYDLIESGKNDQVYQALDDLIEVDLDLAERLNELRLLA
LRVLNTIDDTKTSQDLAHINQLDEEFNRLVMILSRRVQSIEDPTRSNQLKDLLVTLNKTPKLFKLLRQLS
QILQKQQRLQQANLEQFTQLNTTVSQLVNAQNQRTEAAVSDLLMTLSVAQFGLLITGMLGLVILVFIMWR
VVYRSVILRLNQHTQALLRLALGDLDISLDARGDDELAHMGRAIEAFRDTAAHNLKLQADERQVAQELQE
HKESLEQLVAQRTQELAETNERLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLG
DTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQ
LRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSSLLFEVEDTGCGIAEEEQAT
LFDAFTQADGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTVIDL
PPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRA
IYGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGGKSNTEAPVLSASPSFD
SASVIENAQADDIPESNQASEFLLDEEQLQQDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQ
IKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKTGALELSDIDEIKQAWQASKTALDQW
>gnl|CDD|132002 TIGR02957, putative_sigma_factor, RNA polymerase sigma-70 factor, TIGR02957 family. This group of sigma factors are members of the sigma-70 family (TIGR02937). They and appear by homology, tree building and bidirectional best hits, to represent a conserved family. This family is found in a limited number of bacterial lineages. This family includes apparent paralogous expansion in Streptomyces coelicolor A3(2), and multiple copies in Mycobacterium smegmatis MC2, Streptomyces avermitilis MA-4680 and Nocardia farcinica IFM10152
EEFEALRPLLFSLAYRMLGSVADAEDIVQETFLRWQEADRAQIENPKAYLTKVVTRRCIDVLRSARARRE
VYVGPWLPEPLLTTSADPAESVELAESLSMAYLLLLERLSPLERAVFVLREVFDYPYEEIASIVGKSEAN
CRQLVSRARRHLDARRPRFEVSREESRQLLERFVEAAQTGDLDGLLELLAEDVVLYGDGGGKVRAALRPI
YGADRVARFFFGLVRRLGPGGRVDPVDVNGQPAVLVRIDGKLAYVVTFAIEGGGIQNIYIVRNPEKLAHI
G
>gnl|CDD|132004 TIGR02959, RNA_polymerase_sigma_factor_SigZ, RNA polymerase sigma factor, SigZ family. This family of RNA polymerase sigma factors is a member of the Sigma-70 subfamily (TIGR02937). One of these is designated as SigZ in B. subtilis (Swiss_Prot: SIGZ_BACSU). Interestingly, this group has a very sporatic distribution, B. subtilis, for instance, being the only sequenced strain of Bacilli with a member. Dechloromonas aromatica RCB appears to have two of these sigma factors. A member appears on a plasmid found in Photobacterium profundum SS9 and Vibrio fischeri ES114 (where a second one is chromosomally encoded)
WDEFRSELKAFIKSRVSDASDVEDLLQEVFIKIHRNLPSLKDGQKIQSWLYQIARNTIIDFYRSKSRSVE
LPESLLAADSAREETFVKELSQCIPPMIKELPDEYREAIRLTELEGLSQQEIAEKLGLSLSGAKSRVQRG
RKKLKELLETCCHFEFDRVGNLIDYEPKGT
>gnl|CDD|132005 TIGR02960, probable_RNA_polymerase_sigma_subunit, RNA polymerase sigma-70 factor, TIGR02960 family. This group of sigma factors are members of the sigma-70 family (TIGR02937). They and appear by homology, tree building, bidirectional best hits and one-to-a-genome distribution, to represent a conserved family
SVDGAAFTALAEPHRRELLAHCYRMLGSLHEAEDLVQETLLRAWRARDRFEGRSSVRTWLYRIATNACLD
ALEARQRRPRPVGLGAPSADGTAAASEAAEVTWLEPLPDLTLDLDDPAAADPSVAAGSRESVRLAFVAAI
QYLPPRQRAVLLLRDVLGWRAAETAELLGTSTASVNSALQRARATLDEVGPSARDDQLAQPPSPEEQDLL
ERYIAAFESYDLDALTALLHEDAIWEMPPYTLWYQGRPAIVGFIHTVCPGEGAAGMRLLPTIANGQPAAA
MYMRRPDAERHTAFQLHVLEIRGGRITHVTAFLDGPSLFAAFGL
>gnl|CDD|274363 TIGR02961, Probable_allantoicase, allantoicase. Members of this family are the enzyme allantoicase (EC 3.5.3.4), also called allantoate amidinohydrolase. This enzyme hydrolyzes allantoate to (S)-ureidoglycolate and urea; it can also degrade (R)-ureidoglycolate to glyoxylate and urea. Allantoinase (EC 3.5.2.5) hydrolyzes (S)-allantoin (a xanthine metabolite, via urate) to allantoate. Allantoate can then be degraded either by this enzyme, allantoicase, or by allantoate deiminase (EC 3.5.3.9). Members of the seed alignment for this model were taken from BRENDA. Proteins in this family contain two copies of the allantoicase repeat (pfam03561). A different but similarly named enzyme, allantoate amidohydrolase (EC 3.5.3.9), simultaneously breaks down the urea to ammonia and carbon dioxide [Purines, pyrimidines, nucleosides, and nucleotides, Other, Energy metabolism, Other]
QLVNLADRRLGGKVLFASDEFFAPAENLLKPEAPEFKPGVFDEFGKWMDGWETRRKRGAGHDWCIVRLGV
PGVIHGVDIDTSFFTGNYPPAVSIEACLSPEPSPEILLDSTEWVELLPRTELGPSQHHYFEVSSKQRFTH
IRLNIYPDGGIARLRVYGIVVPDWSLLDADETVDLAALENGGVVVACSDAHFGHPDNLIGPGRGRNMGDG
WETARRRDPGNDWAIVRLGAPGEIERIEVDTAHFKGNYPDSCSLQAADLEGGEDEQLITQSMFWVELLPR
TKLGPDTEHVFESSLAASGPVTHVRLNIIPDGGVSRLRLWGR
>gnl|CDD|274364 TIGR02962, Probable_5-hydroxyisourate_hydrolase_R09H10.3, hydroxyisourate hydrolase. Members of this family, hydroxyisourate hydrolase, represent a distinct clade of transthyretin-related proteins. Bacterial members typically are encoded next to ureidoglycolate hydrolase and often near either xanthine dehydrogenase or xanthine/uracil permease genes and have been demonstrated to have hydroxyisourate hydrolase activity. In eukaryotes, a clade separate from the transthyretins (a family of thyroid-hormone binding proteins) has also been shown to have HIU hydrolase activity in urate catabolizing organisms. Transthyretin, then, would appear to be the recently diverged paralog of the more ancient HIUH family [Purines, pyrimidines, nucleosides, and nucleotides, Other]
SPLSTHVLDTTSGKPAAGVPVTLYRLDGGGWTPLATGVTNADGRCDGPLPEGEDLAPGIYKLRFDTGDYF
AARGVESFYPEVEVVFTIADPGQHYHVPLLLSPYGYSTYRGS
>gnl|CDD|274365 TIGR02963, Includes:_Xanthine_dehydrogenase, xanthine dehydrogenase, small subunit. Members of this protein family are the small subunit (or, in eukaryotes, the N-terminal domain) of xanthine dehydrogenase, an enzyme of purine catabolism via urate. The small subunit contains both an FAD and a 2Fe-2S cofactor. Aldehyde oxidase (retinal oxidase) appears to have arisen as a neofunctionalization among xanthine dehydrogenases in eukaryotes and [Purines, pyrimidines, nucleosides, and nucleotides, Other]
IRFFLNGETVTLSDVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVGELVDGGKLRYRSVNACIQF
LPSLDGKAVVTVEDLRQPDGRLHPVQQAMVECHGSQCGFCTPGFVMSLYALYKNSPAPSRADIEDALQGN
LCRCTGYRPILDAAEAAFDYPCSDPLDADRAPIIERLRALRAGETVELNFGGERFIAPTTLDDLAALKAA
HPDARIVAGSTDVGLWVTKQMRDLPDVIYVGQVAELKRIEETDDGIEIGAAVTLTDAYAALAKRYPELGE
LLRRFASLQIRNAGTLGGNIANGSPIGDSPPALIALGARLTLRKGEGRRTLPLEDFFIDYGKTDRQPGEF
VEALHVPRPTPGERFRAYKISKRFDDDISAVCAAFNLELDGGVVAEIRIAFGGMAATPKRAAATEAALLG
KPWNEATVEAAMAALAGDFTPLSDMRASAEYRLLTAKNLLRRFFLET
>gnl|CDD|274366 TIGR02964, conserved_hypothetical_protein, xanthine dehydrogenase accessory protein XdhC. Members of this protein family are the accessory protein XdhC for insertion of the molybdenum cofactor into the xanthine dehydrogenase large chain, XdhB, in bacteria. This protein is not part of the mature xanthine dehydrogenase. Xanthine dehydrogenase is an enzyme for purine catabolism, from other purines to xanthine to urate to further breakdown products [Protein fate, Protein folding and stabilization, Purines, pyrimidines, nucleosides, and nucleotides, Other]
VLVTVAEVRGSAPREAGAKMLVTRDGTFGTIGGGHLEYKAIEIARAMLAGGAAAPRLERFPLGPELGQCC
GGAVTLLFEPLDAADLDWLEWLTETEAPPAPHVVLFGAGHVGRALVRALAPLPCRVTWVDSREEEFPEDI
PDGVAPLVTDEPEAEVAEAPPGSYFLVLTHDHALDLELCHAILRRGDFAYFGLIGSKTKRARFEHRLRAR
GVDPAQIARMTCPIGLAGVKGKAPAVIAVSVAAELL
>gnl|CDD|274367 TIGR02965, xanthine_dehydrogenase, xanthine dehydrogenase, molybdopterin binding subunit. Members of the protein family are the molybdopterin-containing large subunit (or, in, eukaryotes, the molybdopterin-binding domain) of xanthine dehydrogenase, and enzyme that reduces the purine pool by catabolizing xanthine to urate. This model is based primarily on bacterial sequences; it does not manage to include all eukaryotic xanthine dehydrogenases and thereby discriminate them from the closely related enzyme aldehyde dehydrogenase [Purines, pyrimidines, nucleosides, and nucleotides, Other]
VGTSLKHESAHKHVAGTAVYIDDIPEPAGTLHAALGLSTRAHARITSMDLSAVRAAPGVVDVLTAADIPG
ENDISPIIHDDPLLADGKVEFVGQPIFAVVATSRDAARRAARLAKIEYEELPAVLDIEEALAAGSRLVTP
PLTLERGDAAAALAAAPHRLSGTMRIGGQEHFYLEGQIALAVPGEDGGMHVWSSTQHPSEVQHLVAHVLG
VPSHAVTVEVRRMGGGFGGKETQANLFACLAAVAARKTGRPVKLRPDRDDDMMITGKRHDFRVDYDVGFD
DEGRILGVDIDMAARCGFSADLSGPVTDRALFHADNAYFLPDVTITSHPLKTNTQSNTAFRGFGGPQGMV
AIERIMDEVARALGKDPLEVRKRNFYGKDERNVTPYHQTVEDNIIHEIIEELEASSDYAARRAAIRAFNA
TSPVLKKGIALTPVKFGISFTVTHLNQAGALVHVYTDGSIHLNHGGTEMGQGLNTKVAQVVAEEFQVDID
RVKITATDTGKVPNTSATAASSGSDLNGMAAQDAARQIKERLVEFAAEKWQVPEEDVRFAPNHVRVGEQR
VPFAELVQQAYFARVQLSSTGFYKTPKIHWDRAKGRGRPFYYFAYGAACSEVSVDTLTGEYKVLRADILH
DVGRSLNPAIDIGQIEGGFVQGMGWLTTEELVWDEKGRLRTHAPSTYKIPAASDRPKDFNVRLFEWGENR
EDTIHRSKAVGEPPLMLGISVLFAISDAVASVADYRVCPRLDAPATPERVLMAVEALR
>gnl|CDD|274368 TIGR02966, Phosphate_regulon_sensor_protein_PhoR, phosphate regulon sensor kinase PhoR. Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154) [Signal transduction, Two-component systems]
LSALLSRFRAAAQALPDAVVVLDEEGQIEWCNPAAERLLGLRWPDDLGQRITNLIRHPEFVEYLAAGRFS
EPLELPSPINSERVLEIRIAPYGEEQKLLVARDVTRLRRLEQMRRDFVANVSHELRTPLTVLRGYLETLA
DGPDEDPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKN
HQITFEIDGGVDVLGDEDELRSAFSNLVSNAIKYTPEGGTITVRWRRDGGGAEFSVTDTGIGIAPEHLPR
LTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFIF
>gnl|CDD|132012 TIGR02967, guanine_deaminase, guanine deaminase. This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model [Purines, pyrimidines, nucleosides, and nucleotides, Other]
LEYFEDGLLVVENGRIVAVGDYAELKETLPAGVEIDDYRGHLIMPGFIDTHIHYPQTEMIASYGEQLLEW
LEKYTFPTEARFADPDHAEEVAEFFLDELLRNGTTTALVFATVHPESVDALFEAALKRGMRMIAGKVLMD
RNAPDYLRDTAESSYDESKALIERWHGKGRLLYAVTPRFAPTSSPEQLAAAGELAKEYPDVYVQTHLSEN
KDEIAWVKELFPEAKDYLDVYDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGLFN
LKKALEHGVRVGLGTDVGGGTSFSMLQTLREAYKVSQLQGARLSPFEAFYLATLGGARALDLDDRIGNFE
PGKEADFVVLDPAATPLLALRFEGADTLEDKLFKLMYLGDDRNVAETYVAG
>gnl|CDD|274369 TIGR02968, succ_dehyd_anc, succinate dehydrogenase, hydrophobic membrane anchor protein. In E. coli and many other bacteria, two small, hydrophobic, mutually homologous subunits of succinate dehydrogenase, a TCA cycle enzyme, are SdhC and SdhD. This family is the SdhD, the hydrophobic membrane anchor protein. SdhC is apocytochrome b558, which also plays a role in anchoring the complex [Energy metabolism, TCA cycle]
ARSGLRDWLLQRVTAVVLALYTIFLIGFLLALPGLTYEAWRALFAHPWMKIFTLLALLALLYHAWIGMRV
VLEDYVKPEGLRLVLQVLIILFLVAYLIWGAFILW
>gnl|CDD|132014 TIGR02969, Aldehyde_oxidase_1, aldehyde oxidase. Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, closely related to xanthine dehydrogenase/oxidase
PELLFYVNGRKVVEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPSTKSIRHHPVNAC
LTPICSLYGAAVTTVEGIGSTRTRLHPVQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDAL
GGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCCLDQGINGLPEFEEGDETSPELFSEEEFLPLDPTQ
ELIFPPELMRMAEKQPQRTRVFYSERMMWISPVTLKELLEAKFKYPQAPVVMGNTSVGPEVKFKGVFHPV
IISPDRIEELSVVNHTGDGLTLGAGLSLAQVKDILADVVQKLPEETTQTYRALLKHLGTLAGSQIRNMAS
LGGHIISRHLDSDLNPLLAVGNCTLNLLSKEGKRQIPLSEQFLSKCPDADLKPQEILVSVNIPYSRKWEF
VSAFRQAQRQQNALAIVNSGMRVFFGEGDGIIRELSISYGGVGPTTICAKNSCQKLIGRPWNEEMLDTAC
RLILDEVSLAGSAPGGKVEFKRTLIISFLFKFYLEVSQILKRMDPGHYPSLADKYESALEDLHSKHHWST
LKHQNVDSMQLPQDPIGHPIMHLSGVKHATGEAIYCDDMPAVDQELFLTFVTSSRAHAKIVSIDLSEALS
LPGVVDIITAEHLQDANTFGTEKLLATDKVHCVGQLVCAVIADSEVQAKQAAKHVKIVYRDLEPLILTIE
EAIQHKSFFEPERKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFP
KYIQDIVAATLKLPVNKVMCHVRRVGGAFGGKVGKTSIMAAITAFAANKHGRAVRCTLERGEDMLITGGR
HPYLGKYKAGFMNDGRIVALDVEHYSNGGSSLDESLWVIEMGLLKMDNAYKFPNLRCRGWACRTNLPSNT
AFRGFGFPQAGLITEACITEVAAKCGLSPEKVRTINMYKEIDQTPYKQEINAKNLFQCWRECMAKSSYSE
RKVAVEKFNAENYWKKRGLAVIPLKFPVGLGSVAMGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQV
VSRELKMPMSNVHLRGTSTETVPNTNASGGSVVADLNGLAVKDACQTLLKRLEPIISKNPQGTWKDWAQT
AFDQSISLSAVGYFRGYESNINWEKGEGHPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGHSINPA
LDIGQVEGAFIQGMGLYTIEELSYSPQGILYSRGPNQYKIPAICDIPTELHISFLPPSEHSNTLYSSKGL
GESGVFLGCSVFFAIHDAVRAARQERGLSGPWKLTSPLTPEKIRMACEDKFTKMIPRDEPGSYVPWNVPV
>gnl|CDD|274370 TIGR02970, Succinate_dehydrogenase_cytochrome_b556_subunit, succinate dehydrogenase, cytochrome b556 subunit. In E. coli and many other bacteria, two small, hydrophobic, mutually homologous subunits of succinate dehydrogenase, a TCA cycle enzyme, are SdhC and SdhD. This family is the SdhC, the cytochrome b subunit, called b556 in bacteria and b560 in mitochondria. SdhD (see TIGR02968) is called the hydrophobic membrane anchor subunit, although both SdhC and SdhD participate in anchoring the complex. In some bacteria, this cytochrome b subunit is replaced my a member of the cytochrome b558 family (see TIGR02046) [Energy metabolism, TCA cycle]
KQRPLSPHLQIYRFPITAILSILHRITGVLLFFGLPFLLWWLSLSLSSPESFATVHALLSSPLGKLILWG
LLWALLYHLLAGIRHLLWDLGYGLELKSARISAWVVLVLSLVLTILAGIW
>gnl|CDD|213754 TIGR02971, devB-like_secretion_protein, ABC exporter membrane fusion protein, DevB family. Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. DevB from Anabaena sp. strain PCC 7120 is partially characterized as a membrane fusion protein of the DevBCA ABC exporter, probably a glycolipid exporter, required for heterocyst formation. Most Cyanobacteria have one member only, but Nostoc sp. PCC 7120 has seven members
VTALGRLEPEGEVVAVAAPSSGGTDRIKKLLVAEGDRVQAGQVLAELDSRPERTAELDVARTQLDEAKAR
LAQVRAGAKKGEIAAQRAARAAAKLFKDVAAQQATLNRLEAELETAQREVDRYRSLFRDGAVSASDLDSK
ALKLRTAEEELEEALASRSEQIDGARAALASLAEEVRETDVDLAQAEVKSALEAVQQAEALLELTYVKAP
IDGRVLKIHAREGEVIGSEGILEMGDTSQMYAVAEVYETDINRVRVGQRATITSTALSGPLRGTVRRIGS
LIAKNDVLSTDPAADADARVVEVKIRLDPASSERVGRLTNLQVDVAI
>gnl|CDD|132017 TIGR02972, TMAO_torE, trimethylamine N-oxide reductase system, TorE protein. Members of this small, apparent transmembrane protein are designated TorE and occur in operons for the trimethylamine N-oxide (TMAO) reductase system. Members are closely related to the NapE protein of the related periplasmic nitrate reductase system. It may be that TorE is an integral membrane subunit of a complex with the reductase TorA [Energy metabolism, Anaerobic]
SDESKRSNELKALGFIIVVLFPILSVAGIGGYGFIIWMIQAFGGVPG
>gnl|CDD|132018 TIGR02973, periplasmic_nitrate_reductase_protein_NapE, periplasmic nitrate reductase, NapE protein. NapE, homologous to TorE (TIGR02972), is a membrane protein of unknown function that is part of the periplasmic nitrate reductase system; it may be part of the enzyme complex. The periplasmic nitrate reductase allows for nitrate respiration in anaerobic conditions [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]
KRMELNTFLFLAAVIWPVLSVITVGGYGFAVWMYQILAGPPG
>gnl|CDD|274371 TIGR02974, psp_operon_transcriptional_activator, psp operon transcriptional activator PspF. Members of this protein family are PspF, the sigma-54-dependent transcriptional activator of the phage shock protein (psp) operon, in Escherichia coli and numerous other species. The psp operon is induced by a number of stress conditions, including heat shock, ethanol, and filamentous phage infection. Changed com_name to adhere to TIGR role notes conventions. 09/15/06 - DMH [Regulatory functions, DNA interactions]
LIGESNAFLEVLEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSEL
FGHEAGAFTGAQKRHQGRFERADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCA
TNADLPALAAEGRFRADLLDRLAFDVITLPPLRERQEDIMLLAEHFAIRMARELGLPLFPGFTPQAREQL
LEYHWPGNVRELKNVVERSVYRHGLEEAPIDEIIIDPFASPWRPKQAAPAVDEVNSTPTDLPSPSSIAAA
FPLDLKQAQQDYEIELLQQALAEAQFNQRKAAELLGLTYHQLRGLLRKH
>gnl|CDD|132020 TIGR02975, putative_membrane_protein, phage shock protein G. This protein previously was designated yjbO in E. coli. It is found only in genomes that have the phage shock operon (psp), but only rarely is encoded near other psp genes. The psp regulon is upregulated in response to a number of stress conditions, including ethanol, expression of the filamentous phage secretin protein IV and other secretins, and heat shock [Cellular processes, Adaptations to atypical conditions]
LELIFVLGFFVMLMVTGISLLGVLAALGVAVLFMALGGMFALMIKLLPWLILAVVVVWFIKSVR
>gnl|CDD|132021 TIGR02976, Phage_shock_protein_B., phage shock protein B. This model describes the PspB protein of the psp (phage shock protein) operon, as found in Escherichia coli and many related species. Expression of a phage protein called secretin protein IV, and a number of other stresses including ethanol, heat shock, and defects in protein secretion trigger sigma-54-dependent expression of the phage shock regulon. PspB is both a regulator and an effector protein of the phage shock response [Cellular processes, Adaptations to atypical conditions]
MSIFFLAIPLIIFVIFVAPLWLILHYRSKRKTAASLSTDDQALLQELYAKADRLEERIDTLERILDAEHP
NWRRR
>gnl|CDD|274372 TIGR02977, phage_shock_protein_A, phage shock protein A. Members of this family are the phage shock protein PspA, from the phage shock operon. This is a narrower family than the set of PspA and its homologs, sometimes several in a genome, as described by pfam04012. PspA appears to maintain the protonmotive force under stress conditions that include overexpression of certain phage secretins, heat shock, ethanol, and protein export defects [Cellular processes, Adaptations to atypical conditions]
MGIFSRFADIVNSNLNALLDKAEDPEKMIRLIIQEMEDTLVEVRTASARTIADKKELERRVSRLEAQVAD
WQDKAELALSKGREDLARAALIEKQKAQELAEALERELAAVEETLAKLQEDIAKLQAKLAEARARQKALA
IRHQAASSRLDVRRQLDSGRSDEAMARFEQYERRVDELEAQAESYDLGRKPSLEDEFAELEADDEIEREL
AALKAKMKK
>gnl|CDD|132023 TIGR02978, Phage_shock_protein_C., phage shock protein C. All members of this protein family are the phage shock protein PspC. These proteins contain a PspC domain, as do other members of the larger family of proteins described by pfam04024. The phage shock regulon is restricted to the Proteobacteria and somewhat sparsely distributed there. It is expressed, under positive control of a sigma-54-dependent transcription factor, PspF, which binds and is modulated by PspA. Stresses that induce the psp regulon include phage secretin overexpression, ethanol, heat shock, and protein export defects [Cellular processes, Adaptations to atypical conditions]
RRELYRDPQNGKIAGVCAGLADYFGVEVWLVRILVVSALLFGGGFFVLVAYIALWLLLDKKPINLYEDDD
VKSKPWQAGQSPRQALREVKREFRDLERRLRNMERYVTSDTFRLRREFRNL
>gnl|CDD|132024 TIGR02979, phageshock_pspD, phage shock protein PspD. Members of this family are phage shock protein PspD, found in a minority of bacteria that carry the defining genes of the phage shock regulon (pspA, pspB, pspC, and pspF). It is found in Escherichia coli, Yersinia pestis, and closely related species, where it is part of the phage shock operon. It is known to be expressed but its function is unknown [Cellular processes, Adaptations to atypical conditions]
KPGFKLAGKLVLLTALRYGPAGVAGWAMKSVARRPLKMLLAIALEPMLKRAANKVASRY
>gnl|CDD|274373 TIGR02980, SigBFG, RNA polymerase sigma-70 factor, sigma-B/F/G subfamily. This group of similar sigma-70 factors includes clades found in Bacilli (including the sporulation factors SigF:TIGR02885 and SigG:TIGR02850 as well as SigB:TIGR02941), and the high GC gram positive bacteria (Actinobacteria) where a variable number of them are found depending on the lineage
DKEAREKLVELNLPLVRSIARRFRNRGEPHEDLVQVGTIGLVKAIDRFDPSYGVKFSTFAVPTIMGEIKR
FFRDDTWAVRVPRRLKELGVKINKATEELTQRLGRSPTIAEIAERLGVSEEEVVEALEAGNAYQALSLDA
SIEDDDGDPIALLDTLGDEDDALETVEDRLALKPLLAALPERERRILLLRFFEDKTQSEIAERLGISQMH
VSRLLRRALKKLREQLL
>gnl|CDD|132026 TIGR02981, phageshock_pspE, phage shock operon rhodanese PspE. Members of this very narrowly defined protein family are proteins active as rhodanese (EC 2.8.1.1) and found in the extended variants of the phage shock protein (psp operon) in Escherichia coli and a few closely related species. Note that the designation phage shock protein PspE has been applied, incorrectly, in many instances where the genome lacks the phage shock regulon entirely
KKGIFALALFFALPLFAAEHWIDVRIPEQYQQEHIQGAINIPLKEIKEHIATAVPDKNDTVKLYCNAGRQ
SGMAKDILLDMGYTHAENAGGIKDIAMPKVK
>gnl|CDD|274374 TIGR02982, heterocyst_DevA, ABC exporter ATP-binding subunit, DevA family. Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts
VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELH
GASKKQLVQLRRRIGYIFQAHNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLGDHLNYYPH
NLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADR
ILQMEDGKLL
>gnl|CDD|132028 TIGR02983, putative_RNA_polymerase_ECF-subfamily_sigma_factor, RNA polymerase sigma-70 factor, sigma-E family. This group of similar sigma-70 factors includes the sigE factor from Streptomyces coelicolor. The family appears to include a paralagous expansion in the Streptomycetes lineage, while related Actinomycetales have at most two representatives
RSATEEEFTAFVAARYPRLLRTAYLLTGDPHEAEDLVQEALVRTYVRWDRIRDPDAPDAYVRRVLVNLAR
SRWRRRRLLELPTRELPDAAAPDPAPDVALRAALARALRRLPARQRAVVVLRYYEDLSEAQVAEALGISV
GTVKSRLSRALARLRELLEEPT
>gnl|CDD|274375 TIGR02984, Sig-70_plancto1, RNA polymerase sigma-70 factor, Planctomycetaceae-specific subfamily 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are apparently found only in the Planctomycetaceae family including the genuses Gemmata and Pirellula (in which seven sequences are found)
ARGGDREALGELLDRYRNYLRLLARVQLDPRLRRRVDPSDLVQETLLEAHRRFDQFRGKTEGEFAGWLRG
ILSNVLADALRRHLGAQKRDIRREQSLDAGGRLDESSVRLEAQLAADGPSPSQVAARRESAVRLAQALAK
LPEDYREVILLRHLEGLSFAEVAERMDRSEGAVSMLWVRGLARLRQILE
>gnl|CDD|274376 TIGR02985, Sig70_bacteroi1, RNA polymerase sigma-70 factor, Bacteroides expansion family 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found primarily in the genus Bacteroides. This family appears to have resulted from a lineage-specific expansion as B. thetaiotaomicron VPI-5482, Bacteroides forsythus ATCC 43037, Bacteroides fragilis YCH46 and Bacteroides fragilis NCTC 9343 contain 25, 12, 24 and 23 members, respectively. There are currentlyonly two known members of this family outside of the Bacteroides, in Rhodopseudomonas and Bradyrhizobium
EAFEQLYRRYYPKLCAFARRYVKDEEDAEDIVQDVFLKLWENRETLEISESIKAYLFTIVKNRCLNYLRH
KQVEEKYQEELAEIEERELSEADPEEELEAKELEEIIEEAIEKLPEQCREIFILSRFEGLSNKEIAEELG
ISVKTVEYHITKALKFLRKEL
>gnl|CDD|132031 TIGR02986, restriction_endonuclease, type II restriction endonuclease, Alw26I/Eco31I/Esp3I family. Members of this family are type II restriction endonucleases of the Alw26I/Eco31I/Esp3I family. Characterized specificities of three members are GGTCTC, CGTCTC, and the shared subsequence GTCTC [DNA metabolism, Restriction/modification]
HPKFIEYMRFIIQHPNYIGMPNAGGEDGRISWQVSSKKTTGFYTYYQARRAWWEQKADELGIPSIENGRY
SKAARLIHPTGVKPCQTCGKTMSLGYSYPNHNFAKRLKKTFPDETFKDQLIEDIYDILKSLVSENNQEAY
FLLPFPERRKDFKRLPDLEEWIQCLISVYIPGEIKMLSPGAMANPPDRFDGFHSYNRCCRSTADPGRSDE
NLKSYTKDRRAFEYWSDGNWAAADQLMGKAGFNRCSIPECCKHPEKISADHIGPISLGFVHDPRFQPLCS
SCNSAKNDRLTLSDVKTLIEYENRTGESVASWQCRAIWDSIKHDVSNDDTLKRLSNILRSNQDTYMRILW
YILSNGGAEFLATLLKPEYAEYNYTFEGLDIGTLFGEIVSKTPRNTKRADSEAARRVRIAFESLKDYNSK
ENRN
>gnl|CDD|274377 TIGR02987, m6_adenine_and_m5_cytosine_DNA_methyltransferase, type II restriction m6 adenine DNA methyltransferase, Alw26I/Eco31I/Esp3I family. Members of this family are the m6-adenine DNA methyltransferase protein, or domain of a fusion protein that also carries m5 cytosine methyltransferase activity, of type II restriction systems of the Alw26I/Eco31I/Esp3I family. A methyltransferase of this family is alway accompanied by a type II restriction endonuclease from the Alw26I/Eco31I/Esp3I family (TIGR02986) and by an adenine-specific modification methyltransferase. Members of this family are unusual in that regions of similarity to homologs outside this family are circularly permuted [DNA metabolism, Restriction/modification]
KAYGTFFTPPDIAKAMVANLVNEIGKNDKSTKTKIIDPCCGDGRLIAALLKKNEEINYFKEVELNIYFAD
IDKTLLKRAKKLLGEFALLEINVINFNSLSYVLLNIESYLDLFDIVITNPPYGRLKPDKKELTNIETLEY
EKYIDFLKEFDDLLSRVLPYSDPIRKYAGVGTEYSRVFEEISLEIANKNGYVSIISPASWLGDKTGENLR
EYIFNNRLINCIQYFQEEAKLFSGVNQATSIIHLNSGSKSKKIELIFYDKSLSEKGDNITYVDLNIIKSM
NLSIPIPQGSNHLLTILKLLKKLPTLSSLEKIINLRGELDLTGQKDLLSKLGTGYPLIRGKHVGRFNLKN
ESSSEDIFKKFIKNSKKSRHIRMKRIVWRQCSYMKQKRRLIFCIVPPNYILGNSCNYISVKDNNEIEDLY
ALLGIINSAIFEWQFRLFNSNNHVSNYEIDNFPIPKNEKWTNLIMLSQLVEKYIKNEDSKLLEKIEASVA
KAYGLAIEDEDSLLLFDKIELEEKESILKYAKHY
>gnl|CDD|274378 TIGR02988, YaaA_near_RecF, S4 domain protein YaaA. This small protein has a single S4 domain (pfam01479), as do bacterial ribosomal protein S4, some pseudouridine synthases, tyrosyl-tRNA synthetases. The S4 domain may bind RNA. Members of this protein family are found almost exclusively in the Firmicutes, and almost invariably just a few nucleotides upstream of the gene for the DNA replication and repair protein RecF. The few members of this family that are not near recF are found instead near dnaA and/or dnaN, the usual neighbors of recF, near the origin of replication. The conserved location suggests a possible role in replication in the Firmicutes lineage [DNA metabolism, DNA replication, recombination, and repair]
EIKIFTEYITLGQLLKELGIIDSGGQAKWFLQENEVLVNGELENRRGKKLYPGDVIEIP
>gnl|CDD|274379 TIGR02989, Sig-70_gvs1, RNA polymerase sigma-70 factor, Rhodopirellula/Verrucomicrobium family. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are abundantly found in the species Rhodopirellula baltica (11), and Verrucomicrobium spinosum (16) and to a lesser extent in Gemmata obscuriglobus (2)
KAFVRLLTRHERALRAFVRSLVADRDDVDDVLQETFVVAWRKFDQFDPGTNFVAWARGIARNKVLNYRRK
LGRDRLVFDDDLLEALAAEAEPTEAERLSDDRQALEGCLEKLPERQRELLDLRYQRGQKATALAEQTGRT
VNAVYKALQRIRVSLRECV
>gnl|CDD|132035 TIGR02990, ectoine_eutA, ectoine utilization protein EutA. Members of this protein family are EutA, a predicted arylmalonate decarboxylase found in a conserved ectoine utilization operon of species that include Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti and Silicibacter pomeroyi. It is missing from two other species with the other ectoine transport and utilization genes: Pseudomonas putida and Agrobacterium tumefaciens
LDDRPLDKRIGLVILATDHTSERDFARMVASDRIGVYVNRIPYANPTTPENLRKMQPRLTEAAALILPDE
ELDVVAYSCTSASVVIGDDEVTRAINAAKPGTPVVTPSSAAVDGLAALGVRRISLLTPYTPETSRPMAQY
FAVRGFEIVNFTCLGLTDDREMARISPDCIVEAALAAFDPDADALFLSCTALRAATCAQRIEQAIGKPVV
TSNQATAWRCLRLCGDPDMRPGYGRLMHL
>gnl|CDD|132036 TIGR02991, ectoine_eutB, ectoine utilization protein EutB. Members of this protein family are EutB, a predicted arylmalonate decarboxylase found in a conserved ectoine utilization operon of species that include Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. Members of this family resemble threonine dehydratases
VTLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGV
VAASTGNHGRALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLT
MLPPFDHPDIVAGQGTLGLEVVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKA
SLQAGRPVLVAELPTLADSLGGGIGLDNRVTFAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGA
VGIAALLAGKIKNPGPCAVIVSGRNIDMDLHKRIIDG
>gnl|CDD|132037 TIGR02992, ectoine_eutC, ectoine utilization protein EutC. Members of this protein family are EutA, a predicted arylmalonate decarboxylase found in a conserved ectoine utilization operon of species that include Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. This family belongs to the ornithine cyclodeaminase/mu-crystallin family (pfam02423)
ILILTEAELRECVPLDLDAIDCVENAFAALATGKVVMPPILRLDIPEHNGEVDVKTAYVPGLDGFAIKVS
PGFFDNPKLGLPSLNGMMVLLSSRTGLLQALLLDNGYLTDVRTAAAGAVAARHLAREDSSVVAIFGAGMQ
ARLQLEALTLVRDIRSARIWARDSAKAEALALQLSSLLGIDVTAATDPRAAMSGADIIVTTTPSETPILH
AEWLEPGQHVTAMGSDAEHKNEIDPAVIAKADHYVADRLSQTATLGELHHAIAAGLAAALQVFAELGQVI
AGDRPGRRSPDDITIADLTGTGVQDTAIANLAFSRAIATGAGLTFE
>gnl|CDD|274380 TIGR02993, ectoine_eutD, ectoine utilization protein EutD. Members of this family are putative peptidases or hydrolases similar to Xaa-Pro aminopeptidase (pfam00557). They belong to ectoine utilization operons, as found in Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. The exact function is unknown
VVNLPFTREEYAARLAKTRAEMEARGIDLLIVTDPSNMAWLTGYDGWSFYVHQCVLLPPEGEPIWYGRGQ
DANGAKRTAFMDHDNIVGYPDHYVQSTERHPMDYLSEILQDRGWDSLTIGVEMDNYYFSAAAFASLQKHL
PNARFVDATALVNWQRAVKSETEISYMRVAARIVEKMHQRIFERIEPGMRKCDLVADIYDAGIRGVDGFG
GDYPAIVPLLPSGADASAPHLTWDDSPMKVGEGTFFEIAGCYKRYHCPLSRTVFLGKPTQAFLDAEKAVL
EGMEAGLEAAKPGNTCEDIANAFFAVLKKYGIHKDSRTGYPIGLSYPPDWGERTMSLRPGDNTVLKPGMT
FHFMTGLWMEDWGLEITESILITETGVECLSSVPRKLFVKD
>gnl|CDD|132039 TIGR02994, ectoine_eutE, ectoine utilization protein EutE. Members of this family, part of the succinylglutamate desuccinylase / aspartoacylase family (pfam04952), belong to ectoine utilization operons, as found in Sinorhizobium meliloti 1021 (where it the operon is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida
RPSPISPTVDFDRDGVQHGFLRLPYSRDDSAWGSVMIPITVIKNGIGPTALLTGGNHGDEYEGPIALFEL
ARTLDAEDVSGRIIIVPAMNYPAFRAGTRTSPIDRGNLNRSFPGRPDGTVTEKIADYFQRHLLPLADIVL
DFHSGGKTLDFVPFAAAHILPDKAQEAKCFDAVAAFAAPYSMKMLEIDSVGMYDTAAEEMGKVFVTTELG
GGGTASARTIKIAKRGVRNVLRHAGILKGELEIAPTIWLDMPSDDCFIFAEDDGLIEFMIDLGDPVSKGD
VIARVYPVGRTGVAPVEYRAKRDGLLAARHFPGLIKSGDCIAVLA
>gnl|CDD|132040 TIGR02995, ectoine_ehuB, ectoine/hydroxyectoine ABC transporter solute-binding protein. Members of this family are the extracellular solute-binding proteins of ABC transporters that closely resemble amino acid transporters. The member from Sinorhizobium meliloti is involved in ectoine uptake, both for osmoprotection and for catabolism. All other members of the seed alignment are found associated with ectoine catabolic genes [Transport and binding proteins, Amino acids, peptides and amines]
MAMAAGLTALMAIAAATPAAADANTLEELKEQGFARIAIANEPPFTYVGADGKVSGAAPDVARAIFKRLG
IADVNASITEYGALIPGLQAGRFDAIAAGLFIKPERCKQVAFTQPILCDAEALLVKKGNPKGLKSYKDIA
KNPDAKIAAPGGGTEEKLAREAGVKREQIIVVPDGQSGLKMVQDGRADAYSLTVLTINDLASKAGDPNVE
VLAPFKDAPVRYYGGAAFRPEDKELRDAFNVELAKLKESGEFAKIIAPYGFSAKAAMSKTRAKLC
>gnl|CDD|274381 TIGR02996, rpt_mate_G_obs, repeat-companion domain TIGR02996. This model describes an abundant paralogous domain of Gemmata obscuriglobus UQM 2246, a member of the Planctomycetes. The domain also occurs, although rarely, in Myxococcus xanthus DK 1622 and related species. Most member proteins have extensive repeats similar to the leucine-rich repeat, or another repeat class or region of low-complexity sequence. This domain is not repeated, and in Gemmata is usually found at the protein N-terminus
DEEALLRAILAHPDDDTPRLVYADWLDEHGDPARAEFIRLQC
>gnl|CDD|274382 TIGR02997, RNA_polymerase_sigma_subunit_sigma70/sigma32, RNA polymerase sigma factor, cyanobacterial RpoD-like family. This family includes a number of closely related sigma-70 (TIGR02937) factors in the cyanobacteria. All appear most closely related to the essential sigma-70 factor RpoD, and some score above trusted to the RpoD C-terminal domain model (TIGR02393)
DLVRLYLQEIGRVPLLTPEEEIELARQVQQMMVLEELREELEEQLGREPSKEEWAAAAGLSEAELRQRLR
QGQRAKEKMIKANLRLVVSVAKKYQNRGLELLDLIQEGSLGLERAVEKFDPTRGYKFSTYAYWWIRQGIT
RAIANQSRTIRLPIHITEKLNKIKKVQRELSQKLGRTPSEAEIAEALELEPEQVRELLQRARQPVSLDAP
VGDEEDTELGDLLEDDGESPEEQVERESLRQDLESLLAELTPRERQVLRLRFGLDGGEPLTLAEIGRRLN
LSRERVRQIEAKALRKLR
>gnl|CDD|132043 TIGR02998, Regulator_of_ribonuclease_activity_A, regulator of ribonuclease activity A. This family includes a number of closely related sequences from certain enterobacteria. The E. coli member of this family has been characterized as a regulator of RNase E and its crystal structure has been analyzed. The broader subfamily which includes this equivalog, TIGR01935, was initially classified as a "hypothetical equivalog" with the name "regulator of ribonuclease activity A" based on the same evidence for this model. It now appears that, considering the second group of enterobacterial sequences within TIGR01935, the functional assignment is unsupported. THIS PROTEIN IS _NOT_ MenG, AKA S-adenosylmethionine: 2-demethylmenaquinone methyltransferase (EC 2.1.-.-). See the references characterizing this as a case of transitive annotation error [Transcription, Degradation of RNA, Regulatory functions, Protein interactions]
MQYDTSELCDFYADLVDVVEPIFSNFGGRSSFGGKVVTVKCFEHNGLINELLEQNGTGRVLVIDGGGSTR
RALIDAELAQLAANNGWEGIVVYGAVRQVDALEELDIGIQALAAIPVGADEQGIGESDIAVNFAGVTFFP
DDYIYADNTGIILSPEPLEIE
>gnl|CDD|132044 TIGR02999, Sig-70_X6, RNA polymerase sigma factor, TIGR02999 family. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found in a variety of species including Rhodopirellula baltica which encodes a paralogous group of five
SAPVTELLQQWQNGDAAARDQLFPQLYQELRRIARRQLRRERSGQTLQTTALVHEAYLRLSDQDEQKWDD
RAHFFAAAAKAMRRILVDHARRRRAQKRGGGAVRVPLDEVLPDAEADLDEELLDLDDALDKLAQVDPRQA
EVVELRFFAGLTVEEIAELLGVSVRTVERDWRFARAWLADELS
>gnl|CDD|274383 TIGR03000, plancto_dom_1, Planctomycetes uncharacterized domain TIGR03000. Domains described by this model are found, so far, only in the Planctomycetes (Pirellula sp. strain 1 and Gemmata obscuriglobus), in up to six proteins per genome, and may be duplicated within a protein. The function is unknown
ARATVTVILPADAKLSVDGIETNGTGTVRTFRTPPLPAGQEFRYEVRAEYDRDGRTVTVTRTVVVRAGET
VTVDF
>gnl|CDD|188267 TIGR03001, Sig-70_gmx1, RNA polymerase sigma-70 factor, Myxococcales family 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found in multiple copies in the order Myxococcales. This model supercedes TIGR02233, which has now been retired
FLRHLAARLPEAGDPALLLGQLHAADLYLACACAQGEPAALAALERHVLSKVPARLAGLRPPTAFVDEVL
QRLRQRLLVPRAEAPPRIAEYSGRGPLLSWVRIVATRIALELQAQERRHSPVEEPTELAALPAPGSDPEL
DLLRERYRQDFRQALREALAALSERERHLLRLHFVDGLSMDRIGAMYQVHRSTVSRWVAQARERLLERTR
RRLAERLKLSSPELESLLGLVRSRLDVSLSRLLE
>gnl|CDD|274384 TIGR03002, outer_YhbN_LptA, lipopolysaccharide transport periplasmic protein LptA. Members of this protein family include LptA (previously called YhbN). It was shown to be an essential protein in E. coli, implicated in cell envelope integrity, and to play a role in the delivery of LPS to the outer leaflet of the outer membrane. It works with LptB (formerly yhbG), a homolog of ABC transporter ATP-binding proteins, encoded by an adjacent gene. Numerous homologs in other Proteobacteria are found in a conserved location near lipopolysaccharide inner core biosynthesis genes. This family is related to organic solvent tolerance protein (OstA), though distantly [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
ALTSDREQPIHIEADSQTLDDKKGVVTFTGNVVITQGTLKIRADKVVVTRNDAGGIEKATATGKPATFRQ
KLDNGKEIEGQANRIEYDPAKDEVVLTGNARLKQGGNEISGDVITYDTKKQKVIAKGDGGKTGRVTTIIQ
PK
>gnl|CDD|132048 TIGR03003, ectoine_ehuD, ectoine/hydroxyectoine ABC transporter, permease protein EhuD. Members of this family are presumed to act as permease subunits of ectoine ABC transporters. Operons containing this gene also contain the other genes of the ABC transporter and typically are found next to either ectoine utilization or ectoine biosynthesis operons
WDWEFVRQILPTLIEGLKITILATALGFAIAAVLGLVFAILRRSAPTPISWPTSFVVEFIRGTPLLVQLY
FLYYVLPDIGIRLPALVAGVLGLGLHYATYAAEVYRAGIEAVPRGQWEAATALNLTARQTYRHIILPQAI
PPIIPALGNYLVAMFKETPVLSAITVLELMNQAKSIGNSTFRYLEPMTLVGVFFLILSIISVFFLRRLEA
RL
>gnl|CDD|132049 TIGR03004, ectoine_ehuC, ectoine/hydroxyectoine ABC transporter, permease protein EhuC. Members of this family are presumed to act as permease subunits of ectoine ABC transporters. Operons containing this gene also contain the other genes of the ABC transporter and typically are found next to either ectoine utilization or ectoine biosynthesis operons. Permease subunits EhuC and EhuD are homologous
TAYLPLLLQGAWVTMQITLAGSVLATVLAFFAGLGRVSGGPILRTVALCYIEVFRGTSLLVQLFWFYFVL
PLIGLSLDPVTTGVMVLGLHAGAYGAEIVRGALSSVSVQQLEACRALNFTRFQTLRRISLPQALVEMMPA
FGNLAIELLKLTSLVSLISLADLTFAAQSIRNLTLDTLSIFAITLLCYFVMALIIMLIMRVLERVVRRGN
VFPR
>gnl|CDD|132050 TIGR03005, ectoine_ehuA, ectoine/hydroxyectoine ABC transporter, ATP-binding protein. Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins
VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGR
NGPLVPADEKHLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKA
DHMPAQLSGGQQQRVAIARALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFA
REFADRVCFFDKGRIVEQGKPDEIFRQPKEERTREFLSKVIA
>gnl|CDD|274385 TIGR03006, pepcterm_polyde, polysaccharide deacetylase family protein, PEP-CTERM locus subfamily. Members of this protein family belong to the family of polysaccharide deacetylases (pfam01522). All are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria, and are found near the epsH homolog that is the putative exosortase gene. The highest scoring homologs below the trusted cutoff for this model are found in several species of Methanosarcina, an archaeal genus [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
NALTIDVEDYFQVSAFAPHIPRDEWDSLPCRVERNTDRILDLLDRHGVKATFFTLGWVAERYPELVRRIV
DAGHELASHGYGHERVTTQTPEAFRADIRRSKALLEDLSGQAVRGYRAPSFSIGKKNLWALDVLAEAGYR
YSSSIYPIRHDHYGMPDAPRFPFRPDNGRLLEIPVTTVRLGGRNLPAGGGGYFRLLPYALSRWALRRVNG
REGRPAIFYFHPWEIDPEQPRIAGASMKSRFRHYLNLDRMEGRLRRLLGDFRWGRMDRVFL
>gnl|CDD|274386 TIGR03007, pepcterm_ChnLen, polysaccharide chain length determinant protein, PEP-CTERM locus subfamily. Members of this protein family belong to the family of polysaccharide chain length determinant proteins (pfam02706). All are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria, and are found near the epsH homolog that is the putative exosortase gene [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
EQLLSYLKGIWRRRWLFVAVAWVVMIVGWGVVYFLPDRYEASARVYVDTQSVLRPLLKGIAVTPNVDQKI
RIMSRTLLSRPNLEKVIRMLDLDLGAKSPAQLEALITKLRKNISISLAGRDNLFTISYEDKDPELAKDVV
QTLLTIFVEETLGSKRQDSDSAQRFIDEQIKTYEKKLEAAENRLKAFKQENGGILPDQEGDYYSEISEAQ
EELEAARLELNEAIAQRDALKRQLGGEEPVLLAGSSVANSELDGRIEALEKQLDALRLRYTDKHPDVIAT
KREIAQLEEQKEEEGSAKNGGPERGEIANPVYQQLQIELAEAEAEIASLEARVAELTARIERLESLLRTI
PEVEAELTQLNRDYEVNKSNYEQLLTRRESAEVSKQMEVQDKAVSFRIIDPPIVPSKPSGPNRPLLMLAG
LLGGLGAGIGLAFLLSQLRPTVRSVRDLRELTGLPVLGVIPMIATPEERRRRRRRLAAFLASAGLLIAVY
GALMAMEL
>gnl|CDD|163100 TIGR03008, pepcterm_CAAX, CAAX prenyl protease-related protein. The CAAX prenyl protease, in eukaryotes, catalyzes three covalent modifications, including cleavage and acylation, at the C-terminus of certain proteins in a process connected to protein sorting. This family describes a bacterial protein family homologous to one domain of the CAAX-processing enzyme. Members of this protein family are found in genomes that carry a predicted protein sorting system, PEP-CTERM/exosortase, usually in the vicinity of the EpsH homolog that is the hallmark of the system. The function of this protein is unknown, but it may relate to protein motification [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
IAARILPFAVYMLFILLEEVLRQLPTQGVILFDPGWFLYPVKAAIVGAVLAVFRKRCLELHLRDLRPRHL
LFSAAVGVAVFVLWVNLDWLLPFQGEPAGFDPSQIGNAGLTRWVLIAFRLAGATLVVPVMEELFWRSFLL
RYLQQSDFESVPGGRFHWPSFLAVTLLFGLEHHLIVAGLIAGLAYNLLLLRTGSIMACILAHAVTNGLLG
LWVLLTGAWSFW
>gnl|CDD|274387 TIGR03009, plancto_dom_2, Planctomycetes uncharacterized domain TIGR03009. Domains described by this model are found, so far, only in the Planctomycetes (Pirellula sp. strain 1 and Gemmata obscuriglobus), in up to four proteins per genome. The function is unknown [Hypothetical proteins, Conserved]
LDQHLAAWEKKMAGVVNLRCDVKLTRTDSVSQKATAYSGQVLCMKPNFAVVRLNNAADKTQTDYEAWICN
GTAVYEYSGLAKTVTEFELPPAGQGADNLPLDFLAGMKAKDVKERFDVQLHKTDENYIYLAIKPRLGKDQ
AEFKHLRLALYGPGPATAAVAYLPAQVFNLKPNDDTEVWKFTNPKVDSPGVSPKHFQYVEIKEQGWKVFR
>gnl|CDD|200229 TIGR03010, sulf_tusC_dsrF, sulfur relay protein TusC/DsrF. The three proteins TusB, TusC, and TusD form a heterohexamer responsible for a sulfur relay reaction. In large numbers of proteobacterial species, this complex acts on a Cys-derived persulfide moiety, delivered by the cysteine desulfurase IscS to TusA, then to TusBCD. The activated sulfur group is then transferred to TusE (DsrC), then by MnmA (TrmU) for modification of an anticodon nucleotide in tRNAs for Glu, Lys, and Gln. The sulfur relay complex TusBCD is also found, under the designation DsrEFH, in phototrophic and chemotrophic sulfur bacteria, such as Chromatium vinosum. In these organisms, it seems the primary purpose is related to sulfur flux, such as oxidation from sulfide to molecular sulfur to sulfate [Protein synthesis, tRNA and rRNA base modification]
KLAFVFRQAPHGTASGREGLDALLAASAFDEDIGVFFIDDGVLQLLKNQQPELILQKDYIATFKALPLYD
IEELYVCAESLAERGLSEDDLILDVEVLDRSALRAKLDRYDVVLTF
>gnl|CDD|274388 TIGR03011, sulf_tusB_dsrH, sulfur relay protein TusB/DsrH. The three proteins TusB, TusC, and TusD form a heterohexamer responsible for a sulfur relay reaction. In large numbers of proteobacterial species, this complex acts on a Cys-derived persulfide moiety, delivered by the cysteine desulfurase IscS to TusA, then to TusBCD. The activated sulfur group is then transferred to TusE (DsrC), then by MnmA (TrmU) for modification of an anticodon nucleotide in tRNAs for Glu, Lys, and Gln. The sulfur relay complex TusBCD is also found, under the designation DsrEFH, in phototrophic and chemotrophic sulfur bacteria, such as Chromatium vinosum. In these organisms, it seems the primary purpose is related to sulfur flux, such as oxidation from sulfide to molecular sulfur to sulfate [Protein synthesis, tRNA and rRNA base modification]
HTVKKSPFEDNDLELCLRLLGPGDAILLLQDGVYAALEGNRYLSALLKAGVKVYALKEDLEARGLTDRLS
DGVNVIDYTGFVELTEKHDKVITW
>gnl|CDD|274389 TIGR03012, sulf_tusD_dsrE, sulfur relay protein TusD/DsrE. The three proteins TusB, TusC, and TusD form a heterohexamer responsible for a sulfur relay reaction. In large numbers of proteobacterial species, this complex acts on a Cys-derived persulfide moiety, delivered by the cysteine desulfurase IscS to TusA, then to TusBCD. The activated sulfur group is then transferred to TusE (DsrC), then by MnmA (TrmU) for modification of an anticodon nucleotide in tRNAs for Glu, Lys, and Gln. The sulfur relay complex TusBCD is also found, under the designation DsrEFH, in phototrophic and chemotrophic sulfur bacteria, such as Chromatium vinosum. In these organisms, it seems the primary purpose is related to sulfur flux, such as oxidation from sulfide to molecular sulfur to sulfate [Protein synthesis, tRNA and rRNA base modification]
KYTLLVTGPPYGTQAASSAYQFAQALLAKGHEISRVFFYQDGVLNANNLVSPASDEFDLVAAWQQLAQEH
QVDLVVCVAAALRRGVVDEEEASRLQISHGNLAPGFELSGLGELAEAALTADRLVQF
>gnl|CDD|274390 TIGR03013, EpsB_2, sugar transferase, PEP-CTERM system associated. Members of this protein family belong to the family of bacterial sugar transferases (pfam02397). Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria (notable exceptions appear to include Magnetococcus sp. MC-1 and Myxococcus xanthus DK 1622). These genes are generally found near one or more of the PrsK, PrsR or PrsT genes that have been related to the PEP-CTERM system by phylogenetic profiling methods. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species. These proteins are homologs of the EpsB protein found in Methylobacillus sp. strain 12S, which is also associated with a PEP-CTERM system, but of a distinct type. A name which appears attached to a number of genes (by transitive annotation) in this family is "undecaprenyl-phosphate galactose phosphotransferase", which comes from relatively distant characterized enterobacterial homologs, and is considerably more specific than warranted from the currently available evidence
AELVVLVLALYLAVLLRFFYQIGMFSLLSLVPLAQLVTFALVVIISAIALGLYNVDLREDFRGIIARLAI
SLLVSFLALSFIFYFYPEFYLGRGLLALAIVLAGSLVLLSRLFFLKILGLQGLKRRILVLGTGPRAREIA
RLRRSSDRRGHEIVGFVPLPDEPAYVPSEHVIENGDGLVEYVLRHRIDEIVIALDERRGSLPVDELLECK
LSGIEVVDAPSFFERETGKIAIDLIYPSWLIFSNGFRNSSLRRITKRSFDVVASLILLILTLPVMLFTAL
AIKLESGGPVLYRQERVGLNGRPFNLIKFRSMRADAEKNGAVWAQKDDPRVTRVGRFLRKTRIDELPQIF
NVLRGDMSFVGPRPERPEFVEKLSEEIPYYNERHRVKPGITGWAQIKYPYGASVADAKEKLRYDLYYIKN
MSLLLDLIILIQTFEVVLFGKG
>gnl|CDD|132059 TIGR03014, Hypothetical_protein., exopolysaccharide biosynthesis operon protein EpsL. The epsL gene is described as a component of the methanolan exopolysaccharide biosynthesis operon in Methylobacillus sp strain 12S, although no other information regarding its possible function is suggested. Homologs of this gene are found in several other exopolysaccharide operons in a small number of species. These operons contain a subset of the methanolan operon genes by homology and synteny, including the epsH gene which is proposed to act as an "exosortase" directing proteins with a C-terminal tag (PEP-CTERM) to the exopolysaccharide layer. Each of the genomes in which these genes and epsL are found also encode genes with these C-terminal tags
CADEGDTLSFTASLTYTYDDNLFRLDSSESSQALTGSSDRSDQINVTTAGVSVNKRYSRQRFKVDARLSK
HRYQNYDFLDFDGRNYIAAWDWSLTPRLHGNLGFDHKEALNNFANFQGLGTMTSLNTRTLRRYLFDADWE
LHGRWRVLGGVAHSEMTNSALTQRDFDYKEDSVEAGIRYVSPSGSSLSYRLRNTEGEYPNRPLSETLFDS
DYDQTEHELRFDWAVTGKSKLQGSIGYVDREHDHLSQRDFSGVIGRLNADWMVTGKTSLNAAISRELANY
QTVTSSYYRNRGTSIGPTWQATSKIAVRGRLDYEERDFEGDPLVGPPARSDRTRSGSLSLDWSPVRAVRI
SAAFQREKRDSNSDGFDFDSNSVSVSATLTF
>gnl|CDD|132060 TIGR03015, pepcterm_ATPase, putative secretion ATPase, PEP-CTERM locus subfamily. Members of this protein are marked as probable ATPases by the nucleotide binding P-loop motif GXXGXGKTT, a motif DEAQ similar to the DEAD/H box of helicases, and extensive homology to ATPases of MSHA-type pilus systems and to GspA proteins associated with type II protein secretion systems [Protein fate, Protein and peptide secretion and trafficking]
MYEAFFGFTTKPFQLLPDPDFFYPSKGHKRAMAYLEYGLSQREGFILITGEVGAGKTTLIRNLLKRLDQE
RVVAAKLVNTRVDAEDLLRMVAADFGLETEGRDKAALLRELEDFLIEQFAAGKRALLVVDEAQNLTPELL
EELRMLSNFQTDNAKLLQIFLVGQPEFRETLQSPQLQQLRQRIIASCHLGPLDREETREYIEHRLERAGN
RDAPVFSEGAFDAIHRFSRGIPRLINILCDRLLLSAFLEEKREIGGEEVREVIAEIDFE
>gnl|CDD|274391 TIGR03016, hypothetical_protein, uncharacterized protein, PEP-CTERM system associated. Members of this protein family are found predominantly in exopolysaccharide biosynthesis operons marked by the presence of the EpsH-family putative exosortase and presence in the genome of the PEP-CTERM protein sorting signal. Members of this family may be distantly related to the EpsL family modeled in TIGR03014
AAEWVFQPSLGLRETYTDNVDLTAGGKRGDFITQVTPGLDALYDGRRLKLSLDYTLDYVMYAQNSESDDT
YHRLNADGTAELVEDFLFVDGSATISQVSISDFGGQEDNESVTGNRTDQNIFSASPYVVFRLGPRASLQA
RYRYSWVRYEDNIGQSSGSDTFLGSLNSGTRFQRLGWSLDYSKRTHDGFADLNYTLTERIRGTLTYSLTP
QFRLEGTAGSDSNRYASITGWNYSYSEDSTTFARQSGRVSAGGAVRQLYDAGDLFTRIWNPDLRHTFGRL
LLTLGLGRDYTDDFVSNRAFLRKRLSASVALNGARNTLTLRGSYRERESLSTDNRDDSLSNTTRQTGGSV
LLTHRLSPRLTANLGLTYERNEGSGTNDQETDRTSVSAGLSYQLGENTTGSLTYRYQERDSNFEATDYTE
NRLMAEVTMTF
>gnl|CDD|132062 TIGR03017, Lipopolysaccharide_biosynthesis., chain length determinant protein EpsF. Sequences in this family of proteins are members of the chain length determinant family (pfam02706) which includes the wzc protein from E.coli. This family of proteins are homologous to the EpsF protein of the methanolan biosynthesis operon of Methylobacillus species strain 12S. The distribution of this protein appears to be restricted to a subset of exopolysaccharide operons containing a syntenic grouping of genes including a variant of the EpsH exosortase protein. Exosortase has been proposed to be involved in the targetting and processing of proteins containing the PEP-CTERM domain to the exopolysaccharide layer
MNLIQFLLILKARYWIVLFTLLITVTTTAVVSLLLPKEYTATTSVVLDYKGPDPVTGMVLPGQMSPGYMA
TQVDIINSDRVAKKVVDKLKLDENPAVKEKFEEATGGQGSLKEWLADLLLKKLEVKPSRESSVISIEFSG
VDPRFAATVANAFAQAYIDTNIELKVEPAQKAALWFVQQIAALREDLARAQSKLSAYQQEKGIVSSDERL
DVERARLNELSAQLVAAQAQVMDASSKEGGSSGKDALPEVIANPIIQNLKTDIARAESKLAELSQRLGPN
HPQYKRAQAEINSLKSQLNAEIKKVTSSVGTNSRILKQREAELREALENQKAKVLELNRQRDEMSVLQRD
VENAQRAYDAAMQRYTQTRIEAQSNQTDISILNPAVPPLEPSSPRLLLNLVLSIFLGMLLGIGFAFLAEL
MDRRVRSADDIIEALDVPVLATIG
>gnl|CDD|274392 TIGR03018, pepcterm_TyrKin, exopolysaccharide/PEP-CTERM locus tyrosine autokinase. Members of this protein family are related to a known protein-tyrosine autokinase and to numerous homologs from exopolysaccharide biosynthesis region proteins, many of which are designated as chain length determinants. Most members of this family contain a short region, immediately C-terminal to the region modeled here, with an abundance of Tyr residues. These C-terminal tyrosine residues are likely to be autophosphorylation sites. Some members of this family are fusion proteins
LITPNSPRSRIAEEFRKIKRPLLANAFSAATKKNNNLIMVTSSLPGEGKSFTAINLAISLAQEYDKTVLL
IDADLRRPSLHRTLGLEAEPGLSDCLLDPVLDLADVLVPTNIGRLSLLPAGRRHPNPTELLASQRMRSLL
HELARRYPDRIIIIDTPPLLVFSEARALARLVGQIVLVVEEGRTTQEAVKEALSALESCKVLGVVLN
>gnl|CDD|132064 TIGR03019, pepcterm_femAB, FemAB-related protein, PEP-CTERM system-associated. Members of this protein family are found always as part of extended exopolysaccharide biosynthesis loci in bacteria. In nearly every case, these loci contain determinants for the processing of the PEP-CTERM proposed C-terminal protein sorting signal. This family shows remote, local sequence similarity to the FemAB protein family (see pfam02388), whose members [Unknown function, General]
ARWDAFVEAHPEATFFHRAGWQRVIESAFGHPTYFLYAERDGRIVGVLPLAEIRSRLFGNFLVSLPFCVY
GGIAADSAEVAQALEAEAQGLADRLGVGHLELRHLTPRHSGWPAKDLYVTFRKAIPADPEANWLAIPRKQ
RAMVRKGIKAGLTVTVDGDLDRFYDVYAENMRDLGTPVFSRRYFRLLKDVFGEDCEVLTVRLGDGVVASA
VLSFYFRDEVLPYYAGGLREARDVAANDLMYWELMRRACERGLRVFDFGRSKRGTGPFKFKKNWGFEPQP
LHYEYLLYEGREVPDLNPLNPKYRLFIALWRRLPVALANALGPHIVRNLG
>gnl|CDD|274393 TIGR03020, Transcriptional_regulator_LuxR_family., transcriptional regulator EpsA. Proteins in this family include a C-terminal LuxR transcriptional regulator domain (pfam00196). These proteins are positioned proximal to either EpsH-containing exopolysaccharide biosynthesis operons of the Methylobacillus type, or the associated PEP-CTERM-containing genes
LTDDEAGHLFRILDASLRIRRRHQFFSWLQGEVQSLLPHEILLCGWADFEGGNVLHERFSPLRYVRDAQY
SRAIHPPDGLLHRLTNAWGAGKRQPRLVCALTLDDDGWLRFSVNLLLLNLKNIAFHGLSDVDGRHDCLYS
FSRSSVPLDARHAYFLELLLPYLDSALRRVLFLPNQHRTRPLGERHSAGLITAREAEILAWVRDGKTNEE
IAAILGISSLTVKNHLQHIFKKLDVRNRAQAVAKAIA
>gnl|CDD|274394 TIGR03021, pilP_fam, type IV pilus biogenesis protein PilP. Members of this protein family are found in type IV pilus biogenesis loci and include proteins designated PilP [Cell envelope, Surface structures]
NTTVGQLEQLQSETALLEAQLARAKAQNELEEAERGGQNAGPGMPFTSGVPPMAPTIANPTPGVAKALPR
VVEIFGRGGRLTATLRLPGGREVDVKVGDSLPGGYKVKSITLDGVVLS
>gnl|CDD|274395 TIGR03022, WbaP_sugtrans, Undecaprenyl-phosphate galactose phosphotransferase, WbaP. The WbaP (formerly RfbP) protein has been characterized as the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. This model includes the enterobacterial enzymes, where the function is presumed to be identical to the S. typhimurium enzyme as well as a somewhat broader group which are likely to catalyze the same or highly similar reactions based on a phylogenetic tree-building analysis of the broader sugar transferase family. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. The most likely heterogeneity would be in the precise nature of the sugar molecule transferred
LFLGDIAALVFAIYLALLLRYLFGDSSLIWFLLLRSLPVGLFFVAYRAHYGLYPGTGMSPWEELRRLTLA
TFALFLFILALAFFTKVSEPYSRLVFLLAWGLALVLVPLARILVRKLLSRRGWWGRPAVIIGAGQNAAIL
YRALQSNPQLGLRPLAVVDTDPAASGRLLTGLPVVGADDALRLYARTRYAYVIVAMPGTQAEDMARLVRK
LGALHFRNVLIVPSLFGLPNLWISPRFIGGVLGLRVRNNLLLPSARLIKRTLDLVLSLLALPLLLPLLLV
IALLIRLDSKGPAFYKQERVGRNGKLFKCYKFRTMVMNSDQVLEELLAADPELRAEWEEYHKLRNDPRIT
RIGKFLRKTSLDELPQLWNVLKGDMSLVGPRPYLTSELSRYGEALELYLRVRPGITGLWQVSGRNETTYD
ERVYLDVWYIKNWSLWLDIVILAKTIKVVLRRKGAY
>gnl|CDD|274396 TIGR03023, Sugar_transferase., Undecaprenyl-phosphate glucose phosphotransferase. This family of proteins encompasses the E. coli WcaJ protein involved in colanic acid biosynthesis, the Methylobacillus EpsB protein involved in methanolan biosynthesis, as well as the GumD protein involved in the biosynthesis of xanthan. All of these are closely related to the well-characterized WbaP (formerly RfbP) protein, which is the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose (NOTE: not glucose) to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. Colanic acid biosynthesis utilizes a glucose-undecaprenyl carrier, knockout of EpsB abolishes incorporation of UDP-glucose into the lipid phase, and the C-terminal portion of GumD has been shown to be responsible for the glucosyl-1-transferase activity
LLDLLLIALALLLAYLLRFGSRGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAW
TLTFLILALLAFLLKTGTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGR
RLAERLARNPELGYRVVGFFDDRPDARTSVRGVPVLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELL
DALRDLTVDVRLVPDLFDFALLRSRIEEIGGLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLL
LIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVHAEGDGVTQATRNDPRVTRVGAFLRRTSLDEL
PQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWAQVNGLRGETDTLEKMEKRVEYD
LYYIENWSLWLDLKIILLTVFKGFVGKNAY
>gnl|CDD|274397 TIGR03024, hypothetical_protein, PEF-CTERM protein sorting domain. This domain, distantly related to the PEP-Cterm domain described in model TIGR02595, is found in Methanosarcina mazei in four different proteins, as well as in other archaea such as Methanococcoides burtonii. Several proteins with this domain have their genes only a short distance from archaeosortase C, a proposed integral membrane transpeptidase. This family should exclude members of the PEFG-CTERM domain family (TIGR04296), specific to the Thaumarchaeota
VPEFSTIALPIIALLAIIVILRRRK
>gnl|CDD|274398 TIGR03025, EPS_sugtrans, exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase. Members of this family are generally found near other genes involved in the biosynthesis of a variety of exopolysaccharides. These proteins consist of two fused domains, an N-terminal hydrophobic domain of generally low conservation and a highly conserved C-terminal sugar transferase domain (pfam02397). Characterized and partially characterized members of this subfamily include Salmonella WbaP (originally RfbP), E. coli WcaJ, Methylobacillus EpsB, Xanthomonas GumD, Vibrio CpsA, Erwinia AmsG, Group B Streptococcus CpsE (originally CpsD), and Streptococcus suis Cps2E. Each of these is believed to act in transferring the sugar from, for instance, UDP-glucose or UDP-galactose, to a lipid carrier such as undecaprenyl phosphate as the first (priming) step in the synthesis of an oligosaccharide "block". This function is encoded in the C-terminal domain. The liposaccharide is believed to be subsequently transferred through a "flippase" function from the cytoplasmic to the periplasmic face of the inner membrane by the N-terminal domain. Certain closely related transferase enzymes, such as Sinorhizobium ExoY and Lactococcus EpsD, lack the N-terminal domain and are not found by this model
LADLLALVLAFLLAFLLLGLGLLPPPDFYSLLLLLLLLLFLILFALSGLYRSWRGRSLLEELARVLLAWL
VAFLLLLALAFLFKSFDFSRLVLLLWFVLALVLLLLWRLLLRRLLRRLRKRGKNLRRVLIVGTGEAAERL
ARALRRNPALGYRVVGFVDDRPSDRVEVAGLPVLGKLDDLVELVRAHRVDEVIIALPLSEEARILRLLLQ
LEDLGVDVYLVPDLFELLLLRLRVEELGGVPLLSLSNFPLSGLNRALKRLFDIVLSLLALLLLSPLMLAI
ALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRVDAEEGGGPVQATKNDPRITRVGRFLRRTSLDELP
QLFNVLKGDMSLVGPRPERPAEVEKYEQEIPGYMLRHKVKPGITGWAQVSGRGETSTMEERVEYDLYYIE
NWSLWLDLKILLKTVKVVLTGKGAY
>gnl|CDD|274399 TIGR03026, NDP-sugDHase, nucleotide sugar dehydrogenase. Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively
MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDY
EEAIRDADVIIICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGL
KLGEDFYLAYNPEFLREGNAVHDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAEN
TFRAVKIAFANELARICEALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN
PELIEAAREINDSQPDYVVEKIKDLLGPLKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAY
DPLVPEEEVKGLPSIDDLEEALKGADALVILTDHSEFKDLDLEKIKDLMKGKVVVDTRN
>gnl|CDD|132072 TIGR03027, pepcterm_export, putative polysaccharide export protein, PEP-CTERM sytem-associated. This protein family belongs to the larger set of polysaccharide biosynthesis/export proteins described by pfam02563. Members of this family are variable in either containing of lacking a 78-residue insert, but appear to fall within a single clade, nevertheless, where the regions in which the gene is found encode components of the PEP-CTERM/EpsH proposed exosortase protein sorting system [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
YVIGPGDSLNINVWRNPELSGSVPVRPDGKITTPLVGDLVASGKTPTQLARDIEEKLAKYVRNPVVTVIV
TGFIGPFSEQIRVVGAAANPQALPYREGMTLLDVMIAVGGLTDFADGNRAVIVRTVDGEQKQISVRLKDL
IKDGDVTANVELKPGDVLIIPESWF
>gnl|CDD|132073 TIGR03028, EpsE, polysaccharide export protein EpsE. Sequences in this family of proteins are members of a polysaccharide export protein family (pfam02563) which includes the wza protein from E.coli. This family of proteins are homologous to the EpsE protein of the methanolan biosynthesis operon of Methylobacillus species strain 12S. The distribution of this protein appears to be restricted to a subset of exopolysaccharide operons containing a syntenic grouping of genes including a variant of the EpsH exosortase protein. Exosortase has been proposed to be involved in the targetting and processing of proteins containing the PEP-CTERM domain to the exopolysaccharide layer
DYRLGPGDVLRITVFQQPDLTTDTRVSESGSITFPLIGEVKLGGETPAAAERKIASRLSKGGFVKQPQVT
INVLQYRGQQVSVLGQVNRPGRYPLETAGRVSDVLALAGGVTPDGADVITLVREREGKIFRKQIDFPALF
NPGGDNENILVAGGDIIYVDRAPVFYIYGEVQRPGAYRLERNMTVMQALAQGGGLTPRGTERGIRVMRRD
DKGAVEEVSGELGDLVQPDDVIYVRESLF
>gnl|CDD|132074 TIGR03029, EpsG, chain length determinant protein tyrosine kinase EpsG. The proteins in this family are homologs of the EpsG protein found in Methylobacillus strain 12S and are generally found in operons with other Eps homologs. The protein is believed to function as the protein tyrosine kinase component of the chain length regulator (along with the transmembrane component EpsF)
NDANIGKVLLDAGKLSEDEAERILRLQKQENIRFGEAALRLGLINEDDIRQALSRQFEYPYLPPNDGSFS
PDLIAAYQPFSPQVEALRALRSQLMLRWFSEGRKALAVVSAKSGEGCSYIAANLAIVFSQLGEKTLLIDA
NLRDPVQHRNFKLSEQRGLSDILAGRSDLEVITHIPALENLSVLPAGAIPPNPQELLARPAFTDLLNKVM
GDYDVVIVDTPSAEHSSDAQIVATRARGTLIVSRVNETRLHELTSLKEHLSGVGVRVVGAVLNQ
>gnl|CDD|274400 TIGR03030, Cellulose_synthase_UDP-forming, cellulose synthase catalytic subunit (UDP-forming). Cellulose synthase catalyzes the beta-1,4 polymerization of glucose residues in the formation of cellulose. In bacteria, the substrate is UDP-glucose. The synthase consists of two subunits (or domains in the frequent cases where it is encoded as a single polypeptide), the catalytic domain modelled here and the regulatory domain (pfam03170). The regulatory domain binds the allosteric activator cyclic di-GMP. The protein is membrane-associated and probably assembles into multimers such that the individual cellulose strands can self-assemble into multi-strand fibrils
GPPALFKGLLFIIAVAGLLALLALITAPVTLETQLIIAGSAFLLLLILKRFNGKRPRLLLLVLSVFISLR
YLWWRLTETLPFDNTLNFIFGTLLLLAELYSITILLLGYFQTVRPLDRTPVPLPLDPEEWPTVDVFIPTY
NEDLEIVATTVLAAKNMDYPADKFRVWILDDGGTDQKRNDPDPEQAEAAQRREELKEFCRKLGVNYITRP
RNVHAKAGNINNALKHTDGELILIFDADHVPTRDFLQRTVGWFVEDPKLFLVQTPHFFVSPDPIERNLGT
FRRMPNENELFYGLIQDGNDFWNAAFFCGSAAVLRREALDEIGGIAGETVTEDAETALKLHRRGWNSAYL
DRPLIAGLAPETLSGHIGQRIRWAQGMMQIFRLDNPLLKRGLSFPQRLCYLNAMLFWFFPLPRVIFLTAP
LAYLFFGLNIFVASALEILAYALPHMLHSLLTNSYLFGRVRWPFWSEVYETVLAVYLLPPVLVTLLNPKK
PKFNVTPKGELLDEDYFSPLSRPYLILFALILAGLAFGLYRIYGYPIERGVLLVVLGWNLLNLILLGAAL
AVVAERRQRRSSPRIPCKIPAEVQRDGGRWVEATVEDASVGGLGIKINAQGAPGPQLGAGVLVQIRPKRN
GLPALKPARVRGAGGVMIGLEFSPLNVQQVREIVDLVFARSDRWVALWEERRRPDGPLRGLADFLKIALR
GLFRSARDLVRAP
>gnl|CDD|274401 TIGR03031, cas_csx12, CRISPR system subtype II-B RNA-guided endonuclease Cas9/Csx12. Members of this family of CRISPR-associated (cas) protein are found, so far, in CRISPR/cas loci in Wolinella succinogenes DSM 1740, Legionella pneumophila str. Paris, and Francisella tularensis, where the last probably is an example of a degenerate CRISPR locus, having neither repeats nor a functional Cas1. The characteristic repeat length is 37 base pairs and period is about 72. One region of this large protein shows sequence similarity to pfam01844, HNH endonuclease
PIGIDLGGKNTGVFSSHLEAFAELPNLDNTKYSVILIDHNSFQLSQAQRRATRHRVRNKKRNQLVKRLFL
LLFQEILSLDLDAKEETAICHLFNNRGYTYVDTDLDEYIKDATEINLLKELLPFKLRSISEDNFIDWFLQ
KIQSSADYLANYSEEFRKILVSKTEEKKDDKELKNAVKDKYNIKEFLTGATINDEILGTFDKNEVEGHRH
RKVYFEEIKSDITKNNQLDSIKKKSNLPSVCLSNLLGNLSNLQLKNLRRYFNDKIHKKPDQWDEQKFGNE
FLRMLKNWRHLKGDQESLAVRNLIQQLKQKQDYISILEKTPPEITIPPYEDRNNRGMEKCQSLLLNPEKL
DNLYPNWRNLIPGIIDAHPFLEKDLEHTKLRDRKRIISSSKQDYKRDSYILQRYLDLNKKIDKFKLKKQL
SFLGQGKKLPENLIETLKEMETNFNSSLVSVLIQIASYYNKEREDAAQGIWIKLDKYNNTGRFDDNFSLL
ELCNHNPPRKQKQLPNLVAGILQVSSEDFINNKDEWFWNAHKVGRTKLKSYCKEIEEARKNSGNTFKIDI
EEALSKDPEHLTSNEKALLKLIQTIPDISQKIQSHLGHNDKQALIFNNPFSLAQLYTILETKRDGFHKTC
VACTAENYWRSQKTEIDPEDNKDNIILIAYAQRLPADSVRPFDGVLARMMQRLAYEIAMAKWEQIKHIPD
AKSLLIPIILEQNAFEFEESLKKIKGSSSDDRRKKTLEQAIEKQEIQWKDKFQRIKNFSMGICPYKGASI
GGQGEIDHIYPRSHSKKHYGTIFNSEVNLIYV
>gnl|CDD|274402 TIGR03032, conserved_hypothetical_protein, TIGR03032 family protein. This protein family is uncharacterized. A number of motifs are conserved perfectly among all member sequences. The function of this protein is unknown [Hypothetical proteins, Conserved]
LSFRASGQFAQWLAELKLSLAVTTYQAGKLFFIGLQPNGELDVFERTFPRPMGLAVSPQSLTLGTRYQLW
RFANVDNLLPAGQTHPGYDRLYVPRASYVTGDIDAHDLALGAGRLLFVNTLFSCLATVSPDYSFVPLWKP
PFISKLAPEDRCHLNGMALDDGEPRYVTALSQSDVADGWREGRRDGGCVIDIPSGEVVASGLSMPHSPRW
YQGKLWLLNSGRGELGYVDPQAGKFQPVAFLPGFTRGLAFAGDFAFVGLSKLRESRVFGGLPIEERLDAL
GCGVAVIDLNSGDVVHWLRFEGVIEEIYDVAVLPGVRRPEALGPDDDEIRRLINV
>gnl|CDD|200235 TIGR03033, hypothetical_protein, putative phage-type endonuclease. Members of this protein family are found often in phage genomes and in prokaryotic genomes in uncharacterized regions that resemble integrated prophage regions
DLVQRTEEWHAWRKGGITASDIAAIMGLNPYKTPEELWKEKTGFVEPEDMNEAMYHGVKLEPEAREAFRD
KYGIMAEPFCLEHDEYPWMAASLDGLVADDKQILEIKCPSERVSKLWVSELSGEVPAYYQAQVQWQLYVS
GSQAAYFAVYLGG
>gnl|CDD|132079 TIGR03034, TIGR03034, conserved hypothetical protein. Members of this protein family have been found in several species of gammaproteobacteria, including Yersinia pestis and Y. pseudotuberculosis, Xylella fastidiosa, and Escherichia coli UTI89. As many as five members can be found in a single genome. The function is unknown [Hypothetical proteins, Conserved]
SLNFPCTLFKTISRMDDYSADDMKCGDLTEQQLKSDFGLSDISAKVDPYTLIKYHFPGPGSINVAFFAKS
SSKKISQRECVRILFNEFRHLARMFSFFGQYKSLIEKLIEHFQYGNGTPFRDLLLDLAFKEQILNDYSEN
SSIRIIKSVLENGINWTPGTYPSEIKQSIKTKLLSSRLPKFNRFQDSFNGLGITVHDISATKITIKSLQI
YADGYSATVHYVAQDHFGLDDTDIKNKTYSKFRFFRIWFVLQRWKDFAFKPFMTNMEATIEITG
>gnl|CDD|132080 TIGR03035, trp_arylform, arylformamidase. One of several pathways of tryptophan degradation is as follows: tryptophan 2,3-dioxygenase (1.13.11.11) uses 02 to convert Trp to L-formylkynurenine. Arylformamidase (3.5.1.9) hydrolyzes the product to L-kynurenine and formate. Kynureninase (3.7.1.3) hydrolyzes L-kynurenine to anthranilate plus alanine. Members of the seed alignment for this model are bacterial predicted metal-dependent hydrolases. All are supported as arylformamidase (3.5.1.9) by an operon structure in which kynureninase and/or tryptophan 2,3-dioxygenase genes are adjacent. The members from Bacillus cereus, Pseudomonas aeruginosa and Ralstonia metallidurans were characterized. An example from Pseudomonas fluorescens is given the gene symbol qbsH instead of kynB because of its role in quinolobactin biosynthesis, which begins with tryptophan. All members of this family should be arylformamidase (3.5.1.9) [Energy metabolism, Amino acids and amines]
RWWDISPPLNNNTPTWPGDTPFSQEWAWSKEETCPVNVGRITLSPHTGAHADAPLHYRNDGAPIGDVPLD
VYLGPCRVIHCLGAGPLIDPEHLRSALLELPPRVLLRTYEPAPANAWPDDFPAVAPDTIELLAERGVRLI
GIDTPSLDPQDSKTLDAHHALFRHGMAILENVVLDDVAEGDYELIALPLKFTDADASPVRAVLRAL
>gnl|CDD|188272 TIGR03036, trp_2_3_diox, tryptophan 2,3-dioxygenase. Members of this family are tryptophan 2,3-dioxygenase, as confirmed by several experimental characterizations, and by conserved operon structure for many of the other members. This enzyme represents the first of a two-step degradation to L-kynurenine, and a three-step pathway (via kynurenine) to anthranilate plus alanine [Energy metabolism, Amino acids and amines]
DFSGSMSYGDYLQLDTLLSAQHPLSDDHDEMLFIVQHQTSELWMKLILHELRAARRAIRADDLPPAFKML
ARVSRIQEQLNQAWDVLATMTPAEYSAFRDALGQSSGFQSYQYREIEFLLGNKNAAMLRPHEHDPELHAE
LEAALHAPSLYDEVLRLLARRGFPIPAEVLERDWTQPYEPNPSVEAAWLEVYRDPDTYWELYELAEKLVD
LEDLFRQWRFRHLTTVERIIGFKRGTGGSSGVAYLKKMLDVVLFPELWTVRTEL
>gnl|CDD|132082 TIGR03037, anthran_nbaC, 3-hydroxyanthranilate 3,4-dioxygenase. Members of this protein family, from both bacteria and eukaryotes, are the enzyme 3-hydroxyanthranilate 3,4-dioxygenase. This enzyme acts on the tryptophan metabolite 3-hydroxyanthranilate and produces 2-amino-3-carboxymuconate semialdehyde, which can rearrange spontaneously to quinolinic acid and feed into nicotinamide biosynthesis, or undergo further enzymatic degradation
FNFKKWIDEHKHLLKPPVGNQQIWQDSEFMVTVVGGPNARTDFHDDPGEEFFYQLKGEMYLKVTEEGKRE
DVPIREGDIFLLPPHVPHSPQRPAGSIGLVIERKRPQGELDGFQWFCPQCGHKLHRAEVQLENIVTDLPP
VFEHFYSNEDARTCKNCGH
>gnl|CDD|274403 TIGR03038, Photosystem_II_reaction_center_protein_M, photosystem II reaction center protein PsbM. Members of this protein family are the photosystem II reaction center M protein, product of the psbM gene, in Cyanobacteria and their derived organelles in plants. This model resembles pfam05151 but has cutoffs set to avoid false-positive matches to similar (not necessarily homologous) sequences in species that are not photosynthetic [Energy metabolism, Photosynthesis]
MEVNILGFIATALFILVPTVFLLILYIQTASRE
>gnl|CDD|163117 TIGR03039, PS_II_CP47, photosystem II chlorophyll-binding protein CP47 [Energy metabolism, Photosynthesis]
MGLPWYRVHTVVINDPGRLIAVHLMHTALVAGWAGSMALYELAIFDPSDPVLNPMWRQGMYVLPFMARLG
VTGSWGGWSITGETGVDPGFWSFEGVAAAHIVLSGLLFLAACWHWVYWDLELFRDPRTGEPALDLPKIFG
IHLFLSGLLCFGFGAFHLSGLFGPGMWVSDPYGLTGHVQPVAPEWGADGFNPFNPGGIVAHHIAAGIVGI
IGGLFHITVRPPERLYKALRMGNIETVLASSLAAVFFAAFVVAGTMWYGSATTPVELFGPTRYQWDQGYF
RQEINRRVQAAVASGASLEEAWSAIPEKLAFYDYVGNSPAKGGLFRTGPMNNGDGIATGWLGHIVFKDKE
GRELRVRRLPNFFENFPVILTDSNGVVRADIPFRRAESKYSFEQTGVTVSFYGGDLNGQTFTDPAQVKSY
ARKAQLGEAFEFDTETLNSDGVFRTSPRGWFTFAHAVFALLFFFGHIWHGARTLFRDVFAGIDPDLGEQV
EFGVFQKLGDPTTR
>gnl|CDD|213761 TIGR03041, PS_antenn_a_b, chlorophyll a/b binding light-harvesting protein. This model represents a family of proteins from the Cyanobacteria, closely homologous to and yet distinct from PbsC, a chlorophyll a antenna protein of photosystem II. Members are not univerally present in Cyanobacteria, while the family has several members per genome in Prochlorococcus marinus, with seven members in a strain adapted to low light conditions. These antenna proteins may deliver light energy to photosystem I and/or photosystem II [Energy metabolism, Photosynthesis]
WWAGNARVTNRSGRFIAAHVAHAGLIAFWAGAFTLFELARYDPSIPMGHQGLILLPHLATLGIGFDEAGV
WTDTYPVFVIAILHLISSAVLGAGGLLHSLLFPGDLAESEVPRARKFKLEWDDPDKLTFILGHHLIFLGL
GAILFVEWARWHGIYDPAIGAVRQVEYNLNLAMIWNHQFDFLAIDSLEDVMGGHAFLAFLLITGGAWHIA
TKPFGEYTKFKGKGLLSAEAVLSYSLAGIAWMAIVAAFWCAVNTTVYPVEFYGEPLQLKFGISPYFIDTV
DLPGGAHTSRAWLANVHFYLGFFFLQGHLWHALRAMGFDFK
>gnl|CDD|274404 TIGR03042, hypothetical_protein, photosystem II protein PsbQ. This protein through the member sll1638 from Synechocystis sp. PCC 6803, was shown to be part of the cyanobacteria photosystem II. It is homologous to (but quite diverged from) the chloroplast PsbQ protein, called oxygen-evolving enhancer protein 3 (OEE3). We designate this cyanobacteria protein PsbQ by homology [Energy metabolism, Photosynthesis]
LRRLASFLLVLLLTFLVSCSGPAAAVPATYSPAQLAQIQRQAEGIEAAKDRLPELASLVAKGDWVFTRNL
IHGPMGEVRREMTYLNQSLLPKDQKEALALAKELKDDLEKLDEAARLQDGPQAQKAYQEAAADFDAYLDL
LP
>gnl|CDD|274405 TIGR03043, Photosystem_II_reaction_center_protein_Z, photosystem II core protein PsbZ. PsbZ is a core protein of photosystem II in thylakoid-containing Cyanobacteria and plant chloroplasts. The original Chlamydomonas gene symbol, ycf9, is a synonym. PsbZ controls the interaction of the reaction center core with the light-harvesting antenna [Energy metabolism, Photosynthesis]
IFQLAVLALVLLSFVLVVGVPVALASPGGWERSKNLIFSGAGLWFGLVLLVGVLNSFV
>gnl|CDD|274406 TIGR03044, possible_photosystem_II_Psb27_protein, photosystem II protein Psb27. Members of this family are the Psb27 protein of the cyanobacterial photosynthetic supracomplex, photosystem II. Although most protein components of both cyanobacterial and chloroplast versions of photosystem II are closely related and described together by single models, this family is strictly bacterial. Some uncharacterized proteins with highly divergent sequences, from Arabidopsis, score between trusted and noise cutoffs for this model but are not at this time assigned as functionally equivalent photosystem II proteins [Energy metabolism, Photosynthesis]
KRLFSRLSRAALALVLGLCLLLTACSGAAKTRLTGDYVEDTLAVIQTLREAIDLPDDDPNKSEAQAEARQ
LINDYISRYRRRPRVNGLSSFTTMQTALNSLAGHYKSYANRPLPEKLKERLEKELKKAEKALLRG
>gnl|CDD|274407 TIGR03045, Cytochrome_c-550, cytochrome c-550. Members of this protein family are cytochrome c-550, the PsbV extrinsic protein of photosystem II, from both Cyanobacteria and chloroplasts. A paralog to this protein, PsbV2, is found in some species in addition to PsbV itself [Energy metabolism, Photosynthesis]
LRRSIWGLLALLLLLIQLNVGPAQAAELDEETRTVPLNSTGETVTLTEEQVKRGKRLFNTACGTCHVGGI
TKTNPNVGLDPEALALATPPRDNVEALVDYMKNPTSYDGEESIAELHPSIRSADIFPKMRNLTDEDLRLI
AGHILVQPKVVGEKWGGGK
>gnl|CDD|274408 TIGR03046, hypothetical_protein_TeryDRAFT_3222, photosystem II cytochrome PsbV2. Members of this protein family are PsbV2, a protein closely related cytochrome c-550 (PsbV), a protein important to the water-splitting and oxygen-evolving activity of photosystem II. Mutant studies in Thermosynechococcus elongatus showed PsbV2 can partially replace PsbV, from which it appears to have arisen first by duplication, then by intergenic recombination with a different gene [Energy metabolism, Photosynthesis]
IWFWLGILILVWLILASPAAARVDPYVIQYLRVTGPVELPLDARGETKTFTPEQLTDGKNLFESNCLNCH
VGGSTLPNPNVSLSLKDLKGATPPRDTIQSLVAYQRDPRSYDGSEESYGCRPVPEDWMDDEELENLAAFI
LRAAQVAPGWGVESF
>gnl|CDD|274409 TIGR03047, Photosystem_II_reaction_center_Psb28_protein, photosystem II reaction center protein Psb28. Members of this protein family are the Psb28 protein of photosystem II. Two different protein families, apparently without homology between them, have been designated PsbW. Cyanobacterial proteins previously designated PsbW are members of the family described here. However, while members of the plant PsbW family are not found (so far) in Cyanobacteria, members of the present family do occur in plants. We therefore support the alternative designation that has emerged for this protein family, Psp28, rather than PsbW [Energy metabolism, Photosynthesis]
IQFFRGIDEEVIPDVRLTRSRDGGTGTALFRFENPKALDKFNSFGEITGMYLIDEEGEISTREVKAKFVN
GKPKALEAVYIMKSEDEWDRFMRFMERYAEANGLGYSK
>gnl|CDD|132092 TIGR03048, Photosystem_I_iron-sulfur_center, photosystem I iron-sulfur protein PsaC. Members of this family are PsaC, an essential component of photosystem I (PS-I) reaction center in Cyanobacteria and chloroplasts. This small protein, about 80 amino acids in length, contains two copies of the ferredoxin-like 4Fe-4S binding site (pfam00037) and therefore eight conserved Cys residues. This protein is also called photosystem I subunit VII [Energy metabolism, Photosynthesis]
AHSVKIYDTCIGCTQCVRACPTDVLEMVPWDGCKAGQIASAPRTEDCVGCKRCESACPTDFLSVRVYLGA
ETTRSMGLAY
>gnl|CDD|274410 TIGR03049, Photosystem_I_reaction_center_subunit_PsaK, photosystem I reaction center subunit PsaK. Members of this protein family are the PsaK of the photosystem I reaction center. Photosystems I and II occur together in the same sets of organisms. Photosystem I uses light energy to transfer electrons from plastocyanin to ferredoxin, while photosystem II uses light energy to split water and releases molecular oxygen [Energy metabolism, Photosynthesis]
LLAAVPATLTWSPKVAIIMILCNVLAIVIGRYAIQYPGVGPKLPLSAFFGGFGLPELLATTSFGHILGAG
AILGLANLGVL
>gnl|CDD|188274 TIGR03050, PS_I_psaK_plant, photosystem I reaction center PsaK, plant form. This protein family is based on a model that separates the photosystem I PsaK subunit of chloroplasts from chloroplast PsaG protein and from Cyanobacterial PsaK, both of which show sequence similarity
FIGSSTNLIMVTSTTLMLFAGRFGLAPSANRKATAGLKLEARDSGLQTGDPAGFTLADTLACGAVGHIIG
VGIVLGLKNIGAL
>gnl|CDD|132095 TIGR03051, PS_I_psaG_plant, photosystem I reaction center subunit V, chloroplast
VISGSTGLFLALGRFVFLNFQRRNVAKQVPEQNGPKTTGATDFDALQYASLLKSNDPAGFNLVDVLAWGA
LGHIVAVFILATANNGYD
>gnl|CDD|132096 TIGR03052, Photosystem_I_reaction_center_subunit_VIII, photosystem I reaction center subunit VIII. Members of this protein family are PsaI, subunit VIII of the photosystem I reaction center. This protein is found in both the Cyanobacteria and the chloroplasts of plants, but is absent from non-oxygenic photosynthetic bacteria such as Rhodobacter sphaeroides. Species that contain photosystem I also contain photosystem II, which splits water and releases molecular oxygen [Energy metabolism, Photosynthesis]
AWLPSIFVPLVGLVFPAVFMALLFRYIEADD
>gnl|CDD|274411 TIGR03053, Photosystem_I_reaction_center_subunit_XII, photosystem I reaction center subunit XII. Members of this protein family are PsaM, which is subunit XII of the photosystem I reaction center. This protein is found in both the Cyanobacteria and the chloroplasts of plants, but is absent from non-oxygenic photosynthetic bacteria such as Rhodobacter sphaeroides. Species that contain photosystem I also contain photosystem II, which splits water and releases molecular oxygen. The seed alignment for this model includes sequences from pfam07465 and additional sequences, as from Prochlorococcus [Energy metabolism, Photosynthesis]
ISDSQIFIALVIALIAGILALRLGKELYR
>gnl|CDD|213764 TIGR03054, photo_alph_chp1, putative photosynthetic complex assembly protein. In twenty or so anoxygenic photosynthetic alpha-Proteobacteria known so far, a gene for a member of this protein family is present and is found in the vicinity of puhA, which encodes a component of the photosynthetic reaction center, and other genes associated with photosynthesis. This protein family is suggested, consequently, as a probable assembly factor for the photosynthetic reaction center, but its seems its actual function has not yet been demonstrated [Energy metabolism, Photosynthesis]
KGLLIAMLGLVLLTFALVAFAVLTGVGHSGLPAPAAVVASLWLVFEDRPDGAVAVVETPDGRLVAILEPG
QNGFVRVMLRGLARARARAGVAAEPPFRLTRYDNGRLTLTDPATGWSIELNAFGADNAAAFERLL
>gnl|CDD|188275 TIGR03055, photo_alph_chp2, putative photosynthetic complex assembly protein 2. This uncharacterized protein family was identified, by the method of partial phylogenetic profiling, as having a matching phylogenetic distribution to that of the photosynthetic reaction center of the alpha-proteobacterial type. It is nearly always encoded near other photosynthesis-related genes, including puhA [Energy metabolism, Photosynthesis]
VPALYAIFVWWFSTGAVLWLLDSLGRSTHLRSVVAGLPMLTGGLWGLSATADDTSVGGAYVAFTCAIFVW
GWQELSFLSGWVTGPRADPCPPGARGFERFLRALGTILWHEICLLACGILVLVLTWGAENQVGLWTFVVL
WVMRVSAKLNLFLGVPNLNAEFLPDHLAHLKSYFRRKPMNALFPISVTLLTAALVVMIERALDAATAPHE
VVGFALLATLTALAVLEHWFMVLPLPDAKLWSWML
>gnl|CDD|132100 TIGR03056, bchO_mg_che_rel, putative magnesium chelatase accessory protein. Members of this family belong to the alpha/beta fold family hydrolases (pfam00561). Members are found in bacterial genomes if and only if they encoded for anoxygenic photosynthetic systems similar to that of Rhodobacter capsulatus and other alpha-Proteobacteria. Members often are encoded in the same operon as subunits of the protoporphyrin IX magnesium chelatase, and were once designated BchO. No literature supports a role as an actual subunit of magnesium chelatase, but an accessory role is possible, as suggested by placement by its probable hydrolase activity [Energy metabolism, Photosynthesis]
TWPHRDCSRRVTVGPFHWHVQDMGPTAGPLLLLLHGTGASTHSWRDLMPPLARSFRVVAPDLPGHGFTRA
PFRFRFTLPSMAEDLSALCAAEGLSPDGVIGHSAGAAIALRLALDGPVTPRMVVGINAALMPFEGMAGTL
FPYMARVLACNPFTPPMMSRGAADQQRVERLIRDTGSLLDKAGMTYYGRLIRSPAHVDGALSMMAQWDLA
PLNRDLPRITIPLHLIAGEEDKAVPPDESKRAATRVPTATLHVVPGGGHLVHEEQADGVVGLILQAAE
>gnl|CDD|274412 TIGR03057, hypothetical_protein_lp_1332, X-X-X-Leu-X-X-Gly heptad repeats. This model represents a 28-column alignment, comprising four tandem sets of seven residues each, in which the fourth residue tends to be Leu and the seventh tends to be Gly in each set. This heptad periodicity, corresponding to two turns of an alpha helix, suggests alpha-helical structure; in many proteins this 28-region model hits many times in tandem. Arrangement of these sequences on a helical wheel would show a strict alternation of Leu and Gly residues on one side of the helix, that is, an extremely bulky side chain alternating with the virtual absence of one. This suggests an extended zippering of one alpha helix to another, analogous to the shorter leucine zippers found in many dimerizing transcription factors. Proteins in which these heptad repeats occur often have higher order repeats of a unit comprised of several heptads
SGQLADGAGQLASGAGQLASGANQLADG
>gnl|CDD|132102 TIGR03058, rpt_csmH, chlorosome envelope protein H repeat. CsmH, as studied in Chlorobium tepidum, is one of at least ten surface-exposed proteins of the chloroplast, a bacteriochlorophyll-rich structure with a lipid-protein envelope. CsmH contain typically three copies of a repeated sequence, represented by this model [Energy metabolism, Photosynthesis]
EPVQGVISTVSSATGQLVEGVTTTINS
>gnl|CDD|132103 TIGR03059, chloroplast_putative_16_kDa_membrane_protein, photosystem I protein PsaO. Members of this family are the PsaO protein of photosystem I. This protein is found in chloroplasts but not in Cyanobacteria
APVAAIGFVGWVLPTVLNVPLYGGKSLTGLFASSIGENLAHFPAPPALDDPFWLLLFTWHSGLFLVMTFG
QIGWQGRKNGYY
>gnl|CDD|213765 TIGR03060, PS_II_psb29, photosystem II biogenesis protein Psp29. Psp29, originally designated sll1414 in Synechocystis 6803, is found universally in Cyanobacteria and in Arabidopsis. It was isolated and partially sequenced from purified photosystem II (PS II) in Synechocystis. While its function is unknown, mutant studies show an impairment in photosystem II biogenesis and/or stability, rather than in PS II core function [Energy metabolism, Photosynthesis]
MTERRTVSDSKRAFHAAFPRVIPPLYRRVVDELLVELHLLSHQSDFKYDPLFALGLVTVFDRFMEGYRPE
EHLDALFDALCNSNGFDPEQLREDAKQLLEQAKGKGLDEILSWLTQANLSNGGGDTLQGIAGRHKFKYSR
LFAIGLYSLLEEAAPDKDIDEEDLNEILKELSEALGLSYDRVEKDLDLYKSNLEKMKQALELMEETLEAE
RRKR
>gnl|CDD|274413 TIGR03061, hypothetical_protein_lp_1332, YhgE/Pip N-terminal domain. This family contains the N-terminal domain of a family of multiple membrane-spanning proteins of Gram-positive bacteria. One member was shown to be a host protein essential for phage infection, so many members of this family are called "phage infection protein". A separate model, TIGR03062, represents the conserved C-terminal domain. The domains are separated by regions highly variable in both length and sequence, often containing extended heptad repeats as described in model TIGR03057
SELKRLRKNKLLRIALIAIMLIPLLYGGLFLWAFWDPYGNLDNLPVAVVNEDKGATYDGKTLNAGDDLVK
ELKKNDDLDWHFVSAKEAEKGLADGKYYMVITIPEDFSENATSLLDDQPKKAQLIYKTNDANNYIASQIA
ESAAEKVKTSVSKSITETYAETIF
>gnl|CDD|274414 TIGR03062, hypothetical_protein_lp_1332, YhgE/Pip C-terminal domain. This family contains the C-terminal domain of a family of multiple membrane-spanning proteins of Gram-positive bacteria. One member was shown to be a host protein essential for phage infection, so many members of this family are called "phage infection protein". A separate model, TIGR03061, represents the conserved N-terminal domain. The domains are separated by regions highly variable in both length and sequence, often containing extended heptad repeats as described in model TIGR03057
AKMVAEPVKLKHSDYDDVPNYGTGLAPYFLSLALFVGALVLNLIFPPLSRRALPKSARSWRIALAKLLPG
GLIGVIQAIILYGVLILALGLDPAHPPATFGFAILTSLTFMAIIQFLVALFGSVGRFLALVLLVLQLGSS
GGTFPIELLPAFFQAIHPFLPMTYSVNGLRQLISGGDDSTLWQAVAVLLLILVIFLALSLLSARRKRR
>gnl|CDD|213766 TIGR03063, conserved_hypothetical_protein, sortase B cell surface sorting signal. Two different classes of sorting signal, both analogous to the sortase A signal LPXTG, may be recognized by the sortase SrtB. These are given as NXZTN and NPKXZ. Proteins sorted by this class of sortase are less common than the sortase A and LPXTG system. This model describes a number of cell surface protein C-terminal regions from Gram-positive bacteria that appear to be sortase B (SrtB) sorting signals
NPKTGDSAQIGLYAVLFLGSGLFLIRKRK
>gnl|CDD|211782 TIGR03064, sortase_srtB, sortase, SrtB family. Members of this transpeptidase family are, in most cases, designated sortase B, product of the srtB gene. This protein shows only distant similarity to the sortase A family, for which there may be several members in a single bacterial genome. Typical SrtB substrate motifs include NAKTN, NPKSS, etc, and otherwise resemble the LPXTG sorting signals recognized by sortase A proteins [Cell envelope, Other, Protein fate, Protein and peptide secretion and trafficking]
FLKKSITLLFLIVFFYSLYKLGQIFYDYYTNRQVLAEAQQVYKKSMAKQSEEGEVRKQFEDLLAINSDIV
GWITVPGTHIDYPVVQGKDNDYYLNKNYEGEESRAGSIFMDYRNKVDFEDRNTILYGHHMADNSMFGDLK
KFLKQDFFNKHKYFYYETKERKYDVEIFSVYQTTTDFYYIETDFDNDDDYEDFLKEIKEKSVQKRDVKVT
VNDKIITLSTCDYELTTGRIVV
>gnl|CDD|132109 TIGR03065, srtB_sig_QVPTGV, sortase B signal domain, QVPTGV class. This model represents a boutique (unusual) sorting signal, recognized by a member of the sortase SrtB family rather than by the housekeeping sortase, SrtA
EVPTGVAGTLAPFAALGIVAIGGAIYFTKKKK
>gnl|CDD|132110 TIGR03066, Gem_osc_para_1, Gemmata obscuriglobus paralogous family TIGR03066. This model represents an uncharacterized paralogous family in Gemmata obscuriglobus UQM 2246, a member of the Planctomycetes. This family shows sequence similarity to TIGR03067, which is also found in Gemmata obscuriglobus as well as in a few other species [Hypothetical proteins, Conserved]
VALALAGGGRADDKDEKIDAKKLVGKWETSKTKDDVVIEFAKDGKLVVTIGEKGKEVKADGTYKLDGNKL
TLTLKAGGKEKKETLTVKKLTDDELVGKDPDGKKDTLKRVK
>gnl|CDD|274415 TIGR03067, Planc_TIGR03067, Planctomycetes uncharacterized domain TIGR03067. This domain occurs in several species, mostly from the Planctomycetes division of the bacteria. It is expanded into a paralogous family of at least twenty-five members in Gemmata obscuriglobus UQM 2246. This family appears related to TIGR03066, which also is expanded into a large paralogous family in Gemmata obscuriglobus [Unknown function, General]
KDELEKLQGTWKVVAAEKDGKAVPPPEVDALTVTFKGDKLTLKVGEGDPRVATIVLDPAANPKTIDLVQP
DGPEKGKPCKGIYKLEGDTLTVCFSGGGDKPRPTEFD
>gnl|CDD|132112 TIGR03068, srtB_sig_NPQTN, sortase B signal domain, NPQTN class. This model represents one of the boutique (rare) sortase signals, recognized by sortase B (SrtB) rather than by the housekeeping-type SrtA class sortase. This sequence, beginning NPQTN, shows little similarity to several other SrtB substrates
NPQTNAGTPAYIYAIPVASLALLIAITLFVRKK
>gnl|CDD|132113 TIGR03069, RNA-binding_S4_domain-containing_protein, photosystem II S4 domain protein. Members of this protein family are about 265 residues long and each contains an S4 RNA-binding domain of about 48 residues. The member from the Cyanobacterium, Synechocystis sp. PCC 6803, was detected as a novel polypeptide in a highly purified preparation of active photosystem II (Kashino, et al., 2002). The phylogenetic distribution, including Cyanobacteria and Arabidopsis, supports a role in photosystem II, although the high bit score cutoffs for this model reflect similar sequences in non-photosynthetic organisms such as Carboxydothermus hydrogenoformans, a Gram-positive bacterium [Energy metabolism, Photosynthesis]
LPREELLKGANYPEELERLLDLAEQALRTWEPVWSDFLSAPLQEEILKRFSNLTDLKWLAWGGYPQAERQ
RIACARSDNPLDPDIIPIQGLLIEGNFLFDPASHEDFRGALLGTGIVREKIGDIWVLGDRGAQALCTPEL
AEFLQEKLGQVRDVEVKCKAIPLEELQIPAPRTPKELTTVEASLRIDAIASAGFGLSRSKIVDQIKAGRL
RLNWKTVTQPSRELKVGDRLQLRGKGRLEILELEITKKERWRVELLR
>gnl|CDD|213767 TIGR03070, couple_hipB, transcriptional regulator, y4mF family. Members of this family belong to a clade of helix-turn-helix DNA-binding proteins, among the larger family pfam01381 (HTH_3; Helix-turn-helix). Members are similar in sequence to the HipB protein of E. coli. Genes for members of the seed alignment for this protein family were found to be closely linked to genes encoding proteins related to HipA. The HibBA operon appears to have some features in common with toxin-antitoxin post-segregational killing systems [Regulatory functions, DNA interactions]
KQIGILVRARRKALGLTQADLADLAGVGLRFIRDLENGKPTVRLDKVLRVLDALGLEL
>gnl|CDD|274416 TIGR03071, couple_hipA, HipA N-terminal domain. Although Pfam models pfam07805 and pfam07804 currently are called HipA-like N-terminal domain and HipA-like C-terminal domain, respectively, those models hit the central and C-terminal regions of E. coli HipA but not the N-terminal region. This model hits the N-terminal region of HipA and its homologs, and also identifies proteins that lack match regions for pfam07804 and pfam07805
QLVVWLNGERAGILTEDEGGKLSFRYDDDYLGSPSAPPLSLSLPLQAEEFRSGVVPPFFDGLLPEGEILS
RLARRFQISSRDPFGLLLAIGGDCAGAVQIL
>gnl|CDD|213768 TIGR03072, release_prfH, putative peptide chain release factor H. Members of this protein family are bacterial proteins homologous to peptide chain release factors 1 (RF-1, product of the prfA gene), and 2 (RF-2, product of the prfB gene). The member from Escherichia coli K-12, designated prfH, appears to be a pseudogene. This class I release factor is always found as the downstream gene of a two-gene operon [Protein synthesis, Translation factors]
ILLQLSSAQGPAECCLAVAKALERLTREAAARGVRVEVLEQEPGEVPGTLRSALVSLDGEAAAALADRWE
GTLLWICPSPYRPHHRRKNWFIGVQRFSASEEATEDEIRFETLRSSGPGGQHVNKTESAVRATHLASGIS
VKVQSERSQHANKRLATLLLAVRLADLQQEQAAALRAERRTAHHQIERGNPVRVFKGELF
>gnl|CDD|274417 TIGR03073, release_rtcB, release factor H-coupled RctB family protein. Members of this family are related to RctB. RctB a protein of known structure but unknown function that often is encoded near RNA cyclase and therefore is suggested to be a tRNA or mRNA processing enzyme. This family of RctB-like proteins in encoded upstream of, and apparently is translationally coupled to, the putative peptide chain release factor RF-H (TIGR03072), product of the prfH gene. Note that a large deletion at the junction between this gene and the prfH gene in Escherichia coli K-12 marks both as probable pseudogenes [Protein synthesis, Other]
VSLIASDNTWIEGSAIQQLQTTAQLPGMRRVVGMPDLHPGRGYPIGAAFFSVGRFYPALVGNDIGCGMAL
WQTGLLARKYNLDKLEKRLGNLDLPLDEQWDEENTALAPALHGFRSSLGTIGGGNHFAELQQVDQIYDAD
ALATLGLDAKQLLLLVHSGSRGLGQAILREHVDYFGHNGLPEGSPAAAAYLAQHDDALRFAKANRQLIAR
RILQRLRAKGDPLLDVNHNLVSPATIEGEDGWLHRKGATPADQGPVVIPGSRGDYSYLVQPVPSEESLFS
LAHGAGRKWMRSECKDRLAARFSVDQLRRTRLGSRVICEDRQLIYEEAPEAYKSIDSVVGALLQAGLIKV
VARLKP
>gnl|CDD|274418 TIGR03074, PQQ_membr_DH, membrane-bound PQQ-dependent dehydrogenase, glucose/quinate/shikimate family. This protein family has a phylogenetic distribution very similar to that coenzyme PQQ biosynthesis enzymes, as shown by partial phylogenetic profiling. Members of this family have several predicted transmembrane helices in the N-terminal region, and include the quinoprotein glucose dehydrogenase (EC 1.1.5.2) of Escherichia coli and the quinate/shikimate dehydrogenase of Acinetobacter sp. ADP1 (EC 1.1.99.25). Sequences closely related except for the absense of the N-terminal hydrophobic region, scoring in the gray zone between the trusted and noise cutoffs, include PQQ-dependent glycerol (EC 1.1.99.22) and and other polyol (sugar alcohol) dehydrogenases
WLVALGGSWYYLLAGLALLLSAWLLFRRRPAGLWLYAALLLGTLIWALWEVGLDFWPLIPRLGLIAVLGL
WLLLPWVRRPRSVGPARRGAGALAGVLAVAVLAALASMFTDPHPIVGALDTEVPATAAAAPAVPAGDWAA
YGRTQAGQRYSPLDQINPDNVGNLKVAWTYHTGDLKTPDDPGEATFQATPLKVGDTLYLCTPHNKVIALD
AATGKEKWKFDPKLKTEADRQHQTCRGVSYYDAPAAAAGPAGPAAPADCARRIILPTSDARLIALDADTG
KLCEDFGNNGTVDLTAGMGPTPPGYYYPTSPPLVAGTTVVIGGRVADNYSTDEPSGVIRAFDVNTGALVW
AWDPGNPDPTAPPAPGETYTRNSPNSWSVASYDEKLGLVYLPMGNQTPDQWGGDRTPADEKYSSSLVALD
ATTGKERWVFQTVHHDLWDMDVPAQPSLVDLPKADGTTVPALVAPTKQGQIYVLDRRTGEPIVPVEEVPV
PQGAVPGERYSPTQPFSVLTFGPPTLTESDMWGATPFDQLACRIQFKSLRYEGLYTPPSEQGSLVFPGNL
GGFNWGGVAVDPTRQVMFVNPMRLPFVSQLVPRAPGDEAPSGAKGKGTEMGLNPNKGTPYAVNMNPFLSP
LGIPCQAPPWGYMAAIDLKTGKVVWQHPNGTVRDTGPMGIPMPLPIPIGVPTLGGPLATAGGLVFIGATQ
DNYLRAYDLSTGKELWEARLPAGGQATPMTYMGKDGKQYVVIVAGGHGSSGTKRGDYVIAYALP
>gnl|CDD|274419 TIGR03075, PQQ_enz_alc_DH, PQQ-dependent dehydrogenase, methanol/ethanol family. This protein family has a phylogenetic distribution very similar to that coenzyme PQQ biosynthesis enzymes, as shown by partial phylogenetic profiling. Genes in this family often are found adjacent to the PQQ biosynthesis genes themselves. An unusual, strained disulfide bond between adjacent Cys residues contributes to PQQ-binding, as does a Trp residue that is part of a PQQ enzyme repeat (see pfam01011). Characterized members include the dehydrogenase subunit of a membrane-anchored, three subunit alcohol (ethanol) dehydrogenase of Gluconobacter suboxydans, a homodimeric ethanol dehydrogenase in Pseudomonas aeruginosa, and the large subunit of an alpha2/beta2 heterotetrameric methanol dehydrogenase in Methylobacterium extorquens
AAAAAVTNEDLLNDAKDPSDWLTYGGGYAGQRYSPLDQINTDNVKKLQPAWTFSLGKQRGQESQPLVVDG
VMYVTTSYSRVYALDAKTGKILWKYDPKLPDDIIPVMCCDVVNRGAALYDGKVFFGTLDARLVALDAKTG
KVVWSKKNGDYKKGYTITAAPLVVKGKVITGISGGEFGVRGYVTAYDAKTGKLVWRRYTVPGDMGYLKKT
GKPVGGDPGAKTWPGDAWKTGGGATWGTGSYDPETNLIYFGTGNPAPWNSHLRPGDNLYTSSIVARDPDT
GKIKWHYQTTPHDEWDYDGVNEMILFDLKKDGKPRKLLAHADRNGFFYVLDRTNGKLLSAEPFVDKVNWA
TGVDLKTGRPIEVPEARSTDGKKGKPVEVCPGFLGGKNWQPMAYSPKTGLFYVPANHVCMDYWPEKVSYK
KGAAYLGAGFTIKPPPDDHIGSLIAWDPITGKIVWEHKEDFPLWGGVLATAGDLVFTGTLEGYFKAFDAK
TGEELWKFKTGSGIVGPPVTYEQDGKQYVAVLSGWGG
>gnl|CDD|213771 TIGR03076, near_not_gcvH, Chlamydial GcvH-like protein upstream region protein. The H protein (GcvH) of the glycine cleavage system shuttles the methylamine group of glycine from the P protein to the T protein. Most Chlamydia but lack the P and T proteins, and have a single homolog of GcvH that appears deeply split from canonical GcvH in molecular phylogenetic trees. The protein family modeled here is observed so far only in the Chlamydiae, always as part of a two-gene operon, upstream of the homolog of GcvH. Its function is unknown [Unknown function, General]
LAFFYKHQKKFIGLVIAGVCVSGIGVGWGRTFKKTSKFGSNKTVFKTPSGKKYSEKEFFALKRFFSNEAY
PFTGNPKAWNFLNEGLLTERFLTNKLGEKLFLKVYKSGFPAFDKEKSYQGYRRFDAPFISSEEVWKSSAP
QLRDALHIFQQIENPVSPEGFAARVRLFLEEKKFPHYVLRQMLEYRRQMFNLPVDGSLAQGKDLRLFGYR
NIKDWFGDAYVSAAVEALLRFIDEQKKNIAMPSLKEAQQDFYDKAKQAFTKLSKHAEFNLTFDQFVSSYF
SFMGVSESEFFNMYREILLCKRALLALEGAVAFDFYPLQKFFSMGKDSVSVEMFHLPEEYVFKDKEDLEA
FEVYLSLVAAPSSDILDVPTKLLPIETIKAKEPRLVGRRFSVCYKRVKLQDLEKYVPMVEVYQWQQNPEN
FQEILQQFPELETCSSLKDFQNLKPALVEKIHSFTRKEILRADPGRILSELAQQEQKSEEVFLSAGKDSL
LPGIQDGVRLAKVLLQNEVLDYYSQDDEYYYTIIVKNRFETEEVLPYREVLRKGLAKVLLESHKAEERIT
RVLAALQERYPNEEGKDLWQRRLWRFVESHRSGRFSQGDLSWGLEKSVKTFSRGDQGVPQEFEEMLSMKE
GQVSDVLFDPDEGPFYYTCLSHTYCDYPVSVDKLFLAKNHLNEELLGSYLEEFIQN
>gnl|CDD|132121 TIGR03077, Glycine_cleavage_system_H_protein, glycine cleavage protein H-like protein, Chlamydial. The H protein (GcvH) of the glycine cleavage system shuttles the methylamine group of glycine from the P protein to the T protein. Most Chlamydia but lack the P and T proteins, and have a single homolog of GcvH that appears deeply split from canonical GcvH in molecular phylogenetic trees. The protein family modeled here is observed the Chlamydial GcvH homolog, so far always seen as part of a two-gene operon, downstream of a member of the uncharacterized protein family TIGR03076. The function of this protein is unknown
WYSDYHVWILPIHSQVVRLGLTSRMQENLGNILHIDLPSVGSSCKEGEVLVILESSKSAIEVLSPVSGEV
IEVNIALEDDTQPINHSPESEGWFVVVQLDEDFDGENLSL
>gnl|CDD|274420 TIGR03078, ammonia_monooxygenase_3_subunit_C, methane monooxygenase/ammonia monooxygenase, subunit C. Both ammonia oxidizers such as Nitrosomonas europaea and methanotrophs (obligate methane oxidizers) such as Methylococcus capsulatus each can grow only on their own characteristic substrate. However, both groups have the ability to oxidize both substrates, and so the relevant enzymes must be named here according to their ability to oxidze both. The protein family represented here reflects subunit C of both the particulate methane monooxygenase of methylotrophs and the ammonia monooxygenase of nitrifying bacteria
SEWFDSKWYKLGLAPILAFAIFWRWYQRTYAYSHGMDSMEPEFETYWMGLWRVEMVVEALAALILWGWLW
KTRDTKEQLAALTPKEELKRYFYFLMWLGVYGFAVYWGASFFTEQDASWHQVIIRDTSFTPSHIIEFYGS
FPIYIIMGIASFIYAKTRLPLYAKGWSFPLLMLVAGPLMILPNVGLNEWGHAFWFMEELFSAPLHWGFVI
LAWAALFVGGIALQVITRFSN
>gnl|CDD|132123 TIGR03079, ammonia_monooxygenase_subunit_B, methane monooxygenase/ammonia monooxygenase, subunit B. Both ammonia oxidizers such as Nitrosomonas europaea and methanotrophs (obligate methane oxidizers) such as Methylococcus capsulatus each can grow only on their own characteristic substrate. However, both groups have the ability to oxidize both substrates, and so the relevant enzymes must be named here according to their ability to oxidze both. The protein family represented here reflects subunit B of both the particulate methane monooxygenase of methylotrophs and the ammonia monooxygenase of nitrifying bacteria
YGVAALAATVVLDVSTVAAHGERSQEPFLRMRTIQWYDMKWGPDTTKVNETATITGKFHLAEDWPRAVEK
PHVSFFNVGSPSPVFVRLSTKVNGMPVFISGPLEIGRDYEFEVTLQARIPGRHHMHAMLNVKDAGPIAGP
GKWMNITGSWDDFTNPIKDLTGNTIDLETFNTGNGIFWHLSWMVLGIFWIGWFAARPMFLPRSRVLLAYG
DNLLLDPMDKKLTIGVAILTLAIVWGGYRYTEDKHPYTVPIQAGLSKVASLPVAPNPVSINVTKANYDVP
GRALRVTMEITNNGDQVISIGEFTTAGIRFMNANGVRVLDPDYPRELLAEGLEVDDQSAIAPGETVEVKM
EAKDALWEVQRLMALLGDPESRFGGLLMFWDPEGNRIINSIAGPVIPVF
>gnl|CDD|132124 TIGR03080, ammonia_monooxygeanse_subunit_A, methane monooxygenase/ammonia monooxygenase, subunit A. Both ammonia oxidizers such as Nitrosomonas europaea and methanotrophs (obligate methane oxidizers) such as Methylococcus capsulatus each can grow only on their own characteristic substrate. However, both groups have the ability to oxidize both substrates, and so the relevant enzymes must be named here according to their ability to oxidze both. The protein family represented here reflects subunit A of both the particulate methane monooxygenase of methylotrophs and the ammonia monooxygenase of nitrifying bacteria
SEILKAAKMPPEAAKMSRTIDAVYFPILFMLLVGTYHMHFMLLAGDWDFWVDWKDRQFWPVVTPIVGIAY
CAAIMYYLWVNYRLPFGATLCTVCLLAGEWLTRYWGFYWWSHYPINFVWPTIMLPGALMLDAMMALTRSW
LVTALVGGGFFGLLFYPGNWPIFGPTHLPAVVEGVLLSLADYMGYLYVRTGTPEYVRMIEQGSLRTFGGH
TTVIAAFFAAFVSMLMFFVWWYVGKWYCTAFHI
>gnl|CDD|213772 TIGR03081, Methylmalonyl-CoA_epimerase_mitochondrial, methylmalonyl-CoA epimerase. Members of this protein family are the enzyme methylmalonyl-CoA epimerase (EC 5.1.99.1), also called methylmalonyl-CoA racemase. This enzyme converts (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, which is then a substrate for methylmalonyl-CoA mutase (TIGR00642). It is known in bacteria, archaea, and as a mitochondrial protein in animals. It is closely related to lactoylglutathione lyase (TIGR00068), which is also called glyoxylase I, and is also a homodimer
RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIALGNTKVELLEPLGEDSPIAKFLEKNG
GGIHHIAIEVDDIEAALETLKEKGVRLIDEEPRIGAHGKPVAFLHPKSTGGVLIELEQ
>gnl|CDD|274421 TIGR03082, Gneg_AbrB_dup, membrane protein AbrB duplication. The model describes a hydrophobic sequence region that is duplicated to form the AbrB protein of Escherichia coli (not to be confused with a Bacillus subtilis protein with the same gene symbol). In some species, notably the Cyanobacteria and Thermus thermophilus, proteins consist of a single copy rather than two copies. The member from Pseudomonas putida, PP_1415, was suggested to be an ammonia monooxygenase characteristic of heterotrophic nitrifiers, based on an experimental indication of such activity in the organism and a glimmer of local sequence similarity between parts of P. putida protein and an instance of the AmoA protein from Nitrosomonas europaea (; we do not believe the sequence similarity to be meaningful. The member from E. coli (b0715, ybgN) appears to be the largely uncharacterized AbrB (aidB regulator) protein of E. coli cited in Volkert, et al. (PMID 8002588), although we did not manage to trace the origin of association of the article to the sequence
LLLLLVGVAGGLLLSLLGLPAAWLLGPLLAGAVLSLAGGLEITLPPWLLALAQVVIGILIGSRFTREVLA
ELKRLWPAALLSTVLLLALSALLAWLLARLTGVDPLTAFLATSPGGASEMAALAAELGADVAFVAAMQTL
RLLFVVLVVPLIARLL
>gnl|CDD|274422 TIGR03083, TIGR03083, uncharacterized Actinobacterial protein TIGR03083. This protein family pulls together several groups of proteins, each very different from the others. They share in common three conserved regions. The first is a region of about 38 amino acids, nearly always at the N-terminus of a protein. This region has a bulky hydrophobic residue, usually Trp, at position 29, and a His residue at position 37 that is invariant, so far, in over 150 instances. The second conserved region has a motif [DE]xxxHxxD. The third conserved region contains a hydrophobic patch and a well-conserved Arg residue. Most examples are found in the Actinobacteria, including the genera Mycobacterium, Corynebacterium, Streptomyces, Nocardia, Frankia, etc. The pattern of near-invariant residues against a backdrop of extreme sequence divergence suggests enzymatic activity and conservation of active site residues
LARAERAALAALLAALDPDQWAAPTPCPGWTVRDLLAHLAGRERAAAAVVAGLITVRADSDRARERAIEE
LAALPPAALLAWFRAGAARLLDALAALDPDAWGPPPRPAGGALARRLMEVWVHGWDLARALGRPDRLPRA
LAERALDELLATLPRVARLGGRAPPAAVVLAPTGGTWTFGPGGPAVTVTGPAEDLLLLLTGR
>gnl|CDD|274423 TIGR03084, conserved_hypothetical_protein, TIGR03084 family protein. This family, like pfam07398, belongs to the larger set of probable enzymes modeled by TIGRFAMs family TIGR03083. Members are found primarily in the Actinobacteria (Mycobacterium, Streptomyces, etc.). The family is uncharacterized [Hypothetical proteins, Conserved]
MAVLADLLAESEALDRLVAALSEAQWARPTPAPGWTIADQIAHLAFFDEAAVLAATDPAAFRALVAPAMA
DPDGFVDAAAPELATLSPAELLARWRAGRAALAEALRAAPPGARVPWFGPPMSAASMATARLMETWAHGQ
DVADALGVTREPTDRLRHIAHLGVRTRDFAFRIHGLTPPAEPFRVELTAPSGEVWTWGPEDAAQRVTGPA
EDFCLLVTQRRHRDDTDLVAVGADAERWLEIAQAFAGPPGEGR
>gnl|CDD|132129 TIGR03085, TIGR03085, TIGR03085 family protein. This family, like pfam07398 and TIGRFAMs family TIGR03084, belongs to the larger set of probable enzymes defined in family TIGR03083. Members are found primarily in the Actinobacteria (Mycobacterium, Streptomyces, etc.). The family is uncharacterized [Hypothetical proteins, Conserved]
AQSERAALAETLLAKGPDAPTLCGGWTTRDLAAHLVIRERRPDAALGMFLPGLADAVAEVRAKRLAQPFE
ELVARIRAGPPALSPFRILDSVANLIEHFVHHEDVRRAQPDWGPRELPPEHRDALWDALRKMARLLLRRS
PCGVVLERPDGRLVVADRGGVPVVTVTGEPGELLLWAFGRDNVARVDVSGDPEAVAALH
>gnl|CDD|274424 TIGR03086, TIGR03086, TIGR03086 family protein. This family, like pfam07398 and TIGRFAMs family TIGR030834, belongs to the larger set of probable enzymes defined in family TIGR03083. Members are found primarily in the Actinobacteria (Mycobacterium, Streptomyces, etc.). The family is uncharacterized
ADEALAVLAALVRAVRADQLSRPTPCAGWDVRDLLNHLVGSAEAFAAVKEAGGDGWAGPPADDPWLGDDP
VAAYAAAADRARAAWADPAALDATVSLPGGEVPARAALAVHLTELVVHGWDLARATGRDYRLDPALAEFA
LALAEAVGDPPLRPPGLFAPPVPVPADAPALDRLLALLGR
>gnl|CDD|274425 TIGR03087, stp1, sugar transferase, PEP-CTERM/EpsH1 system associated. Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate
ILYLVHRIPFPPNKGDKIRSFHLLRHLAQRHRVHLGTFVDDPEDWQYAADLRPLCEELCLVPLDPRVARL
RSLSGLLTGEPLTLPYYRDRRLQRWVNALLAAEPVDAIVVFSSAMAQYVTHHVRGIPRIIDFVDVDSDKW
AQYARTKRWPLSWIYQREGRLLLAYERRIAALFDAATFVSEAEAELFRRLAPEAAVRIDAFPNGVDADFF
SPDRDYPNPYPPGKRVLVFTGAMDYWPNIDAVSWFAERVFPAVRAARPAAQFYIVGAKPSDAVQALAALP
GVTVTGSVADVRPYLAHAAAAVAPLRIARGIQNKVLEAMAMGRPVVASPEAAEGIDALAEAELLVAADPA
EFAAAILAVLANPAEAEGAGQAGRRRVLSHYAWPRNLARLDALLEQP
>gnl|CDD|132132 TIGR03088, stp2, sugar transferase, PEP-CTERM/EpsH1 system associated. Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate
RPLIVHVVYRFDVGGLENGLVNLINHLPADRYRHAVVALTEVSAFRKRIQRPDVAFYALHKQPGKDVAVY
PQLYRLLRQLRPDIVHTRNLAALEAQLPAALAGVPARIHGEHGRDVFDLDGSNWKYRWLRRLYRPLIHHY
VAVSRDLEDWLRGPVKVPPAKIHQIYNGVDTERFHPSRGDRSPILPPDFFADESVVVGTVGRLQAVKDQP
TLVRAFALLVRQLPEGAERLRLVIVGDGPARGACEQMVRAAGLAHLVWLPGERDDVPALMQALDLFVLPS
LAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGR
ARAEQQFSINAMVAAYAGLYDQLL
>gnl|CDD|274426 TIGR03089, conserved_hypothetical_protein, TIGR03089 family protein. This protein family is found, so far, only in the Actinobacteria (Streptomyces, Mycobacterium, Corynebacterium, Nocardia, Propionibacterium, etc.) and never more than one to a genome. Members show twilight-level sequence similarity to family of AMP-binding enzymes described by pfam00501
LLSPLLAADPASPRLTFYDDATGERVELSAATLANWVAKTANLLQDELDAEPGSRVALDLPAHWQTAVWL
LAAWSTGVEVVLAGDPDADVVVTGPDRLAAAAGSGEVVALSLDPLGRRVAEELPPGVIDFAPEVRVHGDQ
FAPYEQPDPTDPALVAGGGEWTGAELVSAARAAAGLPPGDRVLSLAWTDLEDFLATLLAPLAAGGSLVLV
THPDPARLDQIAEAERVT
>gnl|CDD|163133 TIGR03090, SASP_tlp, small, acid-soluble spore protein tlp. This protein family is restricted to a subset of endospore-forming bacteria such as Bacillus subtilis, all of which are in the Firmicutes (low-GC Gram-positive) lineage. Although previously designated tlp (thioredoxin-like protein), the B. subtilis protein was shown to be a minor small acid-soluble spore protein SASP, unique to spores. The motif E[VIL]XDE near the C-terminus probably represents at a germination protease cleavage site [Cellular processes, Sporulation and germination]
AKPDDRSDNVEKLQQMIDNTIENMEEANEYIEAHAELSEEEKQRIEEKNERREQSIDGFRSEIKDEARAR
>gnl|CDD|274427 TIGR03091, SASP_sspK, small, acid-soluble spore protein K. This protein family is restricted to a subset of endospore-forming bacteria such as Bacillus subtilis, all of which are in the Firmicutes (low-GC Gram-positive) lineage. It is a minor SASP (small, acid-soluble spore protein) designated SspK [Cellular processes, Sporulation and germination]
FDGEPKAKDEHASKRPDGTINTHPQERMRASN
>gnl|CDD|132136 TIGR03092, SASP_sspI, small, acid-soluble spore protein I. This protein family is restricted to a subset of endospore-forming bacteria such as Bacillus subtilis, all of which are in the Firmicutes (low-GC Gram-positive) lineage. It is a minor SASP (small, acid-soluble spore protein) designated SspI. The gene in Bacillus subtilis previously was designated ysfA [Cellular processes, Sporulation and germination]
NLRRAILANISNNTKEQLEATIVDAIQSGEEKMLPGLGVLFEAIWKHANEQEKDEMLETLEQGVK
>gnl|CDD|132137 TIGR03093, SASP_sspL, small, acid-soluble spore protein L. This protein family is restricted to a subset of endospore-forming bacteria such as Bacillus subtilis, all of which are in the Firmicutes (low-GC Gram-positive) lineage. It is a minor SASP (small, acid-soluble spore protein) designated SspL [Cellular processes, Sporulation and germination]
KGRLTGGVNPQGDSEDNAHQDPKSELENRAKKSNTK
>gnl|CDD|132138 TIGR03094, sulfo_cyanin, sulfocyanin. Members of this family are blue-copper redox proteins designated sulfocyanin, from the archaeal genera Sulfolobus, Ferroplasma, and Picrophilus. The most closely related proteins characterized as functionally different are the rustacyanins [Energy metabolism, Electron transport]
AQSAAFAVLVGAIVLIAAVGVTVYLYHPMNTLSSDTSAVSTGTSTTSKIYIPYNSSNKTVFLTLVVWGSG
NAYPFNFNGTSYGAMTIYLPAGWNVYVTFTNYESLPHNLKLLPNSTQTPRGPIWAHTGKIINSTGATTSI
YYGNGISSGHSRSGWWNDTSAGKYWLVCGITGHAESGMWAVVIVSSNVTTPYYTI
>gnl|CDD|132139 TIGR03095, rusti_cyanin, rusticyanin. Rusticyanin is a blue copper protein, described in an obligate acidophilic chemolithoautroph, Acidithiobacillus ferrooxidans, as an electron transfer protein. It can constitute up to 5 percent of protein in cells grown on Fe(II) and is thought to be part of an electron chain for Fe(II) oxidation, with two c-type cytochromes, an aa3-type cytochrome oxidase, and 02 as terminal electron acceptor. It is rather closely related to sulfocyanin (TIGR03094) [Energy metabolism, Electron transport]
QLKSLNETDPGVQVSVSGSTIYYNNSTTLVVAAGPMPGPSMYSFEIHDLKNPTIVIPEGVTVHFTVINTD
TDSGHNFDISKRGPPYPYMPGMDGLGFVAGTGFLPPPKSGKFGYTDFTYHFSTAGTYWYLCTYPGHAENG
MYGKIVVK
>gnl|CDD|132140 TIGR03096, nitroso_cyanin, nitrosocyanin. Nitrosocyanin, as described from the obligate chemolithoautotroph Nitrosomonas europaea, is a red copper protein of unknown function with sequence similarity to a number of blue copper redox proteins [Energy metabolism, Electron transport]
KITKAMFAGFALGLLLMGTAQAAEQSFTVVINAYDTTIPELNVEGVTVKNIRAFNVLNEPEALVVKKGTP
VKVTVENKSPISEGFSIDAYGISEVIKAGETKTISFKADKAGAFTIWCQLHPKNIHLPGSLNVVE
>gnl|CDD|132141 TIGR03097, PEP_O_lig_1, probable O-glycosylation ligase, exosortase A-associated. These proteins are members of the O-antigen polymerase (wzy) family described by pfam04932. This group is associated with genomes and ususally genomic contexts containing elements of the exosortase/PEP-CTERM protein export system, specificially the type 1 variety of this system described by the Genome Property, GenProp0652
RDLLITLVIVGSLPMAFRRPWVGVLVWTWLSIMNPHRLTWGFAYDAPFAALVAGVTLAGLLFSKERKSIP
WTPEVIFLLLLTIWMTVTTFFAFDPDVAFVQWDKVMKIFLMVLVTLMLISDRQRLHWLLWVIVLSLGFYG
AKGGLFTLLTGGNFRVWGPPGSFIADNNHLALALIMTLPLLRYLHLQLARPWQRHLLAVTMLLTVISVLG
SYSRGALLALVAMGAVLFWRSRRKGLMSLLGAVVLLLGLAMMPEEWWDRMNTIQTYEEDASAMGRINAWL
LAWNLAKDRPLVGGGFEYQDEFRFSTYAPVPTNVHAAHSIYFQVLGEHGFVGLALFLGLLALTLLRAGWL
KRHARGIPELKWAVDLAAMLQVSLVGYAVGGAFLGLAYFDLPYHLMVLLVLL
>gnl|CDD|211788 TIGR03098, ligase_PEP_1, acyl-CoA ligase (AMP-forming), exosortase A-associated. This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present
LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGA
ALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSSERLDLLHPALPGCHDLRTLIIVGDPAHASEGHPGE
EPASWPKLLALGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAV
LPLSFDYGFNQLTTAFYVGATVVLHDYLLPRDVLKALEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRY
LTNSGGAMPRATLSRLRSFLPNARLFLMYGLTEAFRSTYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSE
CAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELHLPELAVWSGDTVRRDEEGFLYFVGRRDE
MIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYM
VPALIHVRQALPRNANGKIDRKALAKE
>gnl|CDD|132143 TIGR03099, dCO2ase_PEP1, pyridoxal-dependent decarboxylase, exosortase A system-associated. The sequences in this family contain the pyridoxal binding domain (pfam02784) and C-terminal sheet domain (pfam00278) of a family of Pyridoxal-dependent decarboxylases. Characterized enzymes in this family decarboxylate substrates such as ornithine, diaminopimelate and arginine. The genes of the family modeled here, with the exception of those observed in certain Burkholderia species, are all found in the context of exopolysaccharide biosynthesis loci containing the exosortase/PEP-CTERM protein sorting system. More specifically, these are characteristic of the type 1 exosortase system represented by the Genome Property GenProp0652. The substrate of these enzymes may be a precursor of the carrier or linker which is hypothesized to release the PEP-CTERM protein from the exosortase enzyme. These enzymes are apparently most closely related to the diaminopimelate decarboxylase modeled by TIGR01048 which may suggest a similarity (or identity) of substrate
FTIKNGCLCVGGIPLTELAARAGGTPFYAYDRGLVSERVAALRKALPEELAIHYAVKANPMPALLAHMAP
LVDGFDVASAGELAVALDTGYDPGCISFAGPGKTDAELRRALAAGVLINVESLRELNRLAALSEALGLRA
RVAVRVNPDFELKGSGMKMGGGAKQFGIDAEQVPAALAFIKAADLDFQGFHIFAGSQNLNAEAIIEAQAK
TLALALRLAESAPAPVRVINIGGGFGIPYFPGNPPLDLAPVGAALAALFARLRDALPEVEILLELGRYLV
GEAGIYVCRVIDRKISRGETFLVTDGGLHHHLSASGNFGQVIRRNYPVVIGNRIGGAVREIASIVGPLCT
PLDLLAEKGTLPVAEPGDLVVIFQSGAYGASASPLAFLGHPEAVELLV
>gnl|CDD|132144 TIGR03100, hydr1_PEP, exosortase A system-associated hydrolase 1. This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 2, TIGR03101) of the same superfamily
TERALTFSCEGETLVGVLHIPGASHTTGVLIVVGGPQYRVGSHRQFVLLARRLAEAGFPVLRFDYRGMGD
SEGENLGFEGIDADIAAAIDAFREAAPHLRRIVAWGLCDAASAALLYAPADLRVAGLVLLNPWVRTEAAQ
AASRIRHYYLGQLLSADFWRKLLSGEVNLGSSLRGLGDALLKARQKGDEVAHGGLAERMKAGLERFQGPV
LFILSGNDLTAQEFADSVLGEPAWRGALEDPGIERVEIDGADHTFSDRVWREWVAARTTEWLRR
>gnl|CDD|274428 TIGR03101, hydr2_PEP, exosortase A system-associated hydrolase 2. This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily
HPFFLDAPHGFRFCLYHPPVAVGPRGVVIYLPPFAEEMNKSRRMVALQARAFAAGGFGVLQIDLYGCGDS
AGDFAAARWDVWKEDVAAAYRWLIEQGHPPVTLWGLRLGALLALDAANPLAAKCNRLVLWQPVVSGKQQL
QQFLRLRLVARRLGGESAEASNSLRERLLAGEDVEIAGYELAPALASDLDQRQLAPAVPKNCPVHWFEVR
PEEGATLSPVFSRLGEQWVQSGVEVTVDLVPGPAFWQTQEIEEAPELIARTTALWS
>gnl|CDD|274429 TIGR03102, halo_cynanin, halocyanin domain. Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronobacterium pharaonis. This model represents a domain duplicated in some halocyanins, while appearing once in others. This domain includes the characteristic copper ligand residues. This family does not include plastocyanins, and does not include certain divergent paralogs of halocyanin
YDGFLDDVSNYDGSIVDRTGQDEVTVDVGAEANGGGFAFDPPAIRVDPGTTVVWEWTGEGGGHNVVSDGD
GDLDESERVSEEGTTYEHTFEEPGIYLYVCVPHEALGMKGAVVVE
>gnl|CDD|132147 TIGR03103, trio_acet_GNAT, GNAT-family acetyltransferase TIGR03103. Members of this protein family belong to the GNAT family of acetyltransferases. Each is part of a conserved three-gene cassette sparsely distributed across at least twenty different species known so far, including alpha, beta, and gamma Proteobacteria, Mycobacterium, and Prosthecochloris, which is a member of the Chlorobi. The other two members of the cassette are a probable protease and an asparagine synthetase family protein
MPKEVVIDCGWGRLLFGQTFSDPQELAEALREEGPGRRDIALYVRDPHVVLALAPQELFLDPSHTYRLWL
TQYRPAARTPRGFTVRRLRGPADVDAINRLYAARGMVPVRVDFVLDHRHSRAITYLVAEDEASGAIIGTV
MGVDHRKAFNDPEHGSSLWCLAVDPQAAHPGVGEALVRALAEHFQSRGCAYMDLSVMHDNEQAIALYEKL
GFRRIPVFALKRKNAINERLFSGPAPEADLNPYARIIVDEARRRGIEVEVLDAEGGLFRLSLGGRSIRCR
ESLSELTSAVAMSLCDDKRLTRRLVSEAGLQVPEQQLAGNGEAVEAFLAEHGAVVVKPVRGEQGKGISVD
VRTPDDLEAAIAKARQFCDRVLLERYVPGEDLRLVVIDFEVVAAAVRRPPEVIGDGRSSIRDLIEKQSRR
RAAATGGESRIPLDAETERCLAEAGLDLDDVLPEGQRLRVRRTANLHTGGTIHDVTEQLHPDLREAAERA
ARALDIPVVGIDFLVPDVTGPDYVIIEANERPGLANHEPQPTAERFIDLLFPGTRPA
>gnl|CDD|274430 TIGR03104, trio_amidotrans, asparagine synthase family amidotransferase. Members of this protein family are closely related to several isoforms of asparagine synthetase (glutamine amidotransferase) and typically have been given this name in genome annotation to date. Each is part of a conserved three-gene cassette sparsely distributed across at least twenty different species known so far, including alpha, beta, and gamma Proteobacteria, Mycobacterium, and Prosthecochloris, which is a member of the Chlorobi. The other two members of the cassette are a probable protease and a member of the GNAT family of acetyltransferases
MCGICGEIRFDGQAPDVAAVVRMLAVLAPRGPDAGGVHAQGPVALGHRRLKIIDLSEASQQPMVDAELGL
ALVFNGCIYNYRELRAELEALGYRFFSDGDTEVILKAYHAWGRDCVSRFNGMFAFAIWERDSGRLLLARD
RLGIKPLYYAEDAGRLRFASSLPALLAAGGVDTDIDPVALHHYLTFHAVVPAPHTILKGVRKLPPATWMT
VEPDGSRTQRSYWSLDAGRPADDAARTEADWQDAILEALRLAVKRRLVADVPVGVLLSGGLDSSLIVGLL
AEAGVDGLRTFSIGFEDVGGEKGDEFEYSDIIAERFHTRHHKIRIPNHRVLPALPEAVAAMSEPMVSHDC
VAFYLLSEEVSKHVKVVQSGQGADEVFGGYHWYPPLAAGAGDPVAAYRRAFFDRDHAEYLEMVGPRFHAE
DVSGEFVADHFARPGADTAVDQALRLDTTVMLVDDPVKRVDNMTMAWGLEARVPFLDHELVELAARIPPE
LKLADGGKGVLKEAARGVIPSEVIDRPKGYFPVPALKYLRGPFLEWVRDALTSPAARERGLFQRAYVDRL
LADPDGHLTPLRGSKLWQLALLELWLQRH
>gnl|CDD|274431 TIGR03105, gln_synth_III, glutamine synthetase, type III. This family consists of the type III isozyme of glutamine synthetase, originally described in Rhizobium meliloti, where types I and II also occur
LQALARDKGIKYFLASFVDLHGVQKAKLVPAEAIDHMATGGAGFAGFAAWGLGQSPADPDLMAIPDLDSL
TQLPWQPGVAWVAADLHVNGKPYPQAPRVVLKRQLAEAAELGLTLNTGVECEFFLLRRDEDGSLSIADRA
DTLAKPCYDQRGLMRRYDVLTEISDAMNALGWDPYQNDHEDANGQFEMNFTYADALTTADRHAFFRYMVK
EIAEKHGMRATFMPKPFADLTGNGCHFHLSLWDEDGRNLFADDSDPNGLGLSKLAYHFIGGILHHAPALC
AVLAPTVNSYKRLNAPRTTSGATWAPNFISYGGNNRTHMVRIPDPGRFELRLADGAANPYLAQAAILAAG
LDGIERKLDPGPPRDINLYAEELAARGVETLPQNLLEALRALEADPLLAEALGAEFVDEFLKLKRQEWEE
YHRHVSDWEIDRYLD
>gnl|CDD|132150 TIGR03106, trio_M42_hydro, hydrolase, peptidase M42 family. This model describes a subfamily of MEROPS peptidase family M42, a glutamyl aminopeptidase family that also includes the cellulase CelM from Clostridium thermocellum and deblocking aminopeptidases that can remove acylated amino acids. Members of this family occur in a three gene cassette with an amidotransferase (TIGR03104)in the asparagine synthase (glutamine-hydrolyzing) family, and a probable acetyltransferase (TIGR03103) in the GNAT family
DTDYLTETLLALLAIPSPTGFTDAVVRYVAERLEDLGIEYELTRRGAIRATLPGREATPARAVVTHLDTL
GAMVRELKDNGRLELVPIGHWSARFAEGARVTIFTDSGEFRGTILPLKASGHAFNEEIDSQPTGWDHVEV
RVDARASCRADLVRLGISVGDFVAFDPQPEFLANGFIVSRHLDDKAGVAALLAALKAIVEHKVPLPVDVH
PLFTITEEVGSGASHALPPDVAELVSVDNGTVAPGQNSSEHGVTIAMADSSGPFDYHLTRKLIRLCQDHG
IPHRRDVFRYYRSDAASAVEAGHDIRTALVTFGLDASHGYERTHIDALEALANLLVAYAQSPP
>gnl|CDD|132151 TIGR03107, Glutamyl_aminopeptidase, glutamyl aminopeptidase. This model represents the M42.001 clade within MEROPS family M42. M42 includes glutamyl aminopeptidase as in the present model, deblocking aminopeptidases as from Pyrococcus horikoshii and related species, and endo-1,4-beta-glucanase (cellulase M) as from Clostridium thermocellum. The current family includes [Protein fate, Degradation of proteins, peptides, and glycopeptides]
FNKIKEVTELQGTSGFEHPIRDYLRQDITPLVDQVETDGLGGIFGIKESQVENAPRVMVAAHMDEVGFMV
SQIKPDGTFRVVELGGWNPLVVSSQRFTLFTRKGKKYPVISGSVPPHLLRGSSGGPQLPAVSDILFDGGF
TNKDEAWSFGVRPGDVIVPQTETILTANGKNVISKAWDNRYGVLMILELLESLKDQELPNTLIAGANVQE
EVGLRGAHVSTTKFNPDIFFAVDCSPAGDIYGDQGGKLGEGTLLRFFDPGHIMLPRMKDFLLTTAEEAGI
KYQYYVAKGGTDAGAAHLKNSGVPSTTIGVCARYIHSHQTLYSIDDFLAAQAFLQAIVKKLDRSTVDTIK
>gnl|CDD|132152 TIGR03108, eps_aminotran_1, exosortase A system-associated amidotransferase 1. The predicted protein-sorting transpeptidase that we call exosortase (see TIGR02602) has distinct subclasses that associated with different types of exopolysaccharide production loci. This model represents a distinct clade among a set of amidotransferases largely annotated (not necessarily accurately) as glutatime-hydrolyzing asparagine synthases. Members of this clade are essentially restricted to the characteristic exopolysaccharide (EPS) regions that contain the exosortase 1 genome (xrtA), in genomes that also have numbers of PEP-CTERM domain (TIGR02595) proteins
MCGITGIFDLTGQRPIDRDLLRRMNDAQAHRGPDGGGVHVEPGIGLGHRRLSIIDLSGGQQPLFNEDGSV
VVVFNGEIYNFQELVAELQALGHVFRTRSDTEVIVHAWEEWGEACVERFRGMFAFALWDRNQETLFLARD
RLGIKPLYYALLADGWFIFGSELKALTAHPSLPRELDPLAVEDYFAYGYVPDPRTIFKGVKKLEPGHTLT
LRRGAPPARPRCYWDVSFAPAAPLSEADALAELIERLREAVRSRMVADVPLGAFLSGGVDSSAVVALMAG
LSDTPVNTCSIAFDDPAFDESAYARQVAERYGTNHRVETVDPDDFSLVDRLAGLYDEPFADSSALPTYRV
CELARKRVTVALSGDGGDELFAGYRRYRWHMAEERVRGILPLGLRRPLFGTLGRLYPKADWAPRMLRAKT
TFQALARDPLEGYFHSVSVLDNALRRQLFSPDFRRELQGYRAIEVLRRHAARAPTDDALSLAQYLDLKTY
LPGDILTKVDRASMAHGLEVRVPLLDHRLVEWAAGLPPDLKLRGGEGKYLLKKAMRPYLPDDVLYRPKMG
FSVPLAAWFRGPLRERVRTLVLGETLAETGLFDPAFIRKLVDQHQSGRRDYSAPLWSLLMFEAFLRQA
>gnl|CDD|274432 TIGR03109, exosortase_1, exosortase A. The predicted protein-sorting transpeptidase that we call exosortase (see TIGR02602) has distinct subclasses that associated with different types of exopolysaccharide production loci. We designate this, the most common type so far, exosortase 1. We propose the gene symbol xrtA, analogous to srtA for the most common type of sortase in Gram-positive bacteria
KAWRRALVLLLLVLLAIILAYLPTWLSMVEIWARSDTYAHGYLIPPISLWLVWRKREELLKLAPQPSPLA
LLLLAAAGLAWLLAEAASVSLLAQLSLVALLVFSVIALLGPRVARALAFPLAYLLFAVPVGDFLIPPLQD
ITAFFTVALLSATGIPVYREGLFIHIPSGTFEVAEACSGLRYLIASLAIGALYAYLNYRSIKRRLLFFLV
SIIVPILANWLRAYGIIMIGHYSGMELALGFDHLVYGWIFFGVVMALLFWIGGRWRE
>gnl|CDD|188282 TIGR03110, exosort_Gpos, exosortase family protein XrtG. Members of this protein family are found in a modest number of non-pathogenic Gram-positive bacteria, including three species of Lactococcus and three paralogs in Clostridium acetobutylicum. This protein appears related to the conserved core region of a family of proposed transpeptidases, exosortase (previously EpsH), thought to act on PEP-CTERM proteins. Members of the seed alignment include all exosortase proposed active site residues. However, in contrast to canonical exosortase (TIGR02602) and archaeal (TIGR03762), and cyanobacterial (TIGR03763) variants, this family has not yet been matched to a cognate PEP-CTERM-like sorting signal. This protein is assigned the gene symbol XrtG (eXosoRTase family protein of Gram-positives)
VLICLLIIAWIYLLSVLKRAKLDFFYFIVGSVGLFFILTFFFRNYLVWFLSRCVSTVLGLIGDLTGYFSS
FIDNNLISIETKGGLISIFIDYECSGVIETLAFTSLLWFYPFYQRLEKIFYTIFGDLWIFLANILRISLI
IVIVKYFGVSSFYIAHTVLGRIIFYVLVIILYYNVFTKSQLKRQNVG
>gnl|CDD|132155 TIGR03111, glyc2_xrt_Gpos1, putative glycosyltransferase, exosortase G-associated. Members of this protein family are probable glycosyltransferases of family 2, whose genes are near those for the exosortase homolog XrtG (TIGR03110), which is restricted to Gram-positive bacteria. Other genes in the conserved gene neighborhood include a 6-pyruvoyl tetrahydropterin synthase homolog (TIGR03112) and an uncharacterized intergral membrane protein (TIGR03766)
QKLIIQLGFWIAWLLIPIIVEIIPAVGGFIILLRKYRHKKRLKFIGKLPDITIIIPVYNSEDTLFNCIES
IYNQTYPIELIDIILANNQSTDDSFQVFCRAQNEFPGLSLRYMNSDQGKAKALNAAIYNSIGKYIIHIDS
DGKLHKDAIKNMVTRFENNPDIHAMTGVILTDKELIEKTKGRFLKLIRRCEYFEYAQAFLAGRNFESQVN
SLFTLSGAFSAFRRETILKTQLYNSETVGEDTDMTFQIRELLDGKVYLCENAIFYVDPIDGLNKLYTQRQ
RWQRGELEVSHMFFESANKSIKGFFSNFMVRRIMYDHTFAFPRMIWYFAMIFLIFLGYPVKLVVGSNLLI
YILYVLSSFLNFINVKIFLKEYKEIRDYYKKKWYIIFLLPIYNFVVFWIRVIGIINAMTTQASWKTRTFT
DEWEAFLVVLKRDFSLIFK
>gnl|CDD|132156 TIGR03112, 6_pyr_pter_rel, 6-pyruvoyl tetrahydropterin synthase-related domain. Members of this family are small proteins, or small domains of larger proteins, that occur in certain Firmicutes in the same regions as members of families TIGR03110 and TIGR03111. Members of TIGR03110 resemble exosortase, a proposed protein sorting transpeptidase (see TIGR02602). TIGR03111 represents a small clade among the group 2 glycosyltransferases. Members of the current protein family resemble eukaryotic known and prokaryotic predicted 6-pyruvoyl tetrahydropterin synthases
YKFKFYLNASHSIIINGVRGNKHPHTWEITIFVIKKEDKFILFNDVEKKVEKYLKPYQNKYLNDLEPFDK
INPTLENIGDYFFDEIKKLLKEKGWKLHSIEISETPTRTYVVN
>gnl|CDD|274433 TIGR03113, exosortase_2, exosortase B. The predicted protein-sorting transpeptidase that we call exosortase (see TIGR02602) has distinct subclasses that associated with different types of exopolysaccharide production loci. We designate this relatively uncommon proteobacterial type to be type 2. We propose the gene symbol xrtB. Most species encountered so far with xrtB also contain xrtA (TIGR03109)
WWPILLGLLVLYLPTYWDLAHGLWNSEEQAHGPIVLIVALWLIWQQRHAVFHDEEVTPTRPATGWALLIF
GLLLYVLGRSQDILLFEIGSQIPVIAGLLLITRGWRALRALWFPLFFLLFMIPLPGFVVDALTLPMKQAV
SYVAEQILYWAGYPIARSGVILQVGQYQLLVADACAGLHTLFSLEAMGLLYLNLVRHDSIARNVILAIAI
IPISFTANVVRVMVLTLVTYHFGDEAGQGFLHGFAGMVLFVSALLLIIGVDSLLQYAV
>gnl|CDD|274434 TIGR03114, cas8u_csf1, CRISPR type AFERR-associated protein Csf1. Members of this family show up near CRISPR repeats in Acidithiobacillus ferrooxidans ATCC 23270, Azoarcus sp. EbN1, and Rhodoferax ferrireducens DSM 15236. In the latter two species, the CRISPR/cas locus is found on a plasmid. This family is one of several characteristic of a type of CRISPR-associated (cas) gene cluster we designate Aferr after A. ferrooxidans, where it is both chromosomal and the only type of cas gene cluster found. The gene is designated csf1 (CRISPR/cas Subtype as in A. ferrooxidans protein 1), as it lies closest to the repeats
CGKNIWVGDRYTKFSVGPSFMDVADLAARGGGMVCGHCTALMSKDMLQAYAKSIFSEGGVFPFASNVDVA
RGLLNPPEPPFVALYATRKSQHMAWRAPVNLSRDLMYVRVGDRDLKIRRPVLLSAVQACQTLGSFMGIKP
IAKSLAHPPARLERDLKDPAHGLLRPKGPEKTLAEAPAYPEAYQLLQSLTVGETWALRFLLS
>gnl|CDD|274435 TIGR03115, cas7_csf2, CRISPR type IV/AFERR-associated protein Csf2. Members of this family show up near CRISPR repeats in Acidithiobacillus ferrooxidans ATCC 23270, Azoarcus sp. EbN1, and Rhodoferax ferrireducens DSM 15236. In the latter two species, the CRISPR/cas locus is found on a plasmid. This family is one of several characteristic of a type of CRISPR-associated (cas) gene cluster we designate Aferr after A. ferrooxidans, where it is both chromosomal and the only type of cas gene cluster found. The gene is designated csf2 (CRISPR/cas Subtype as in A. ferrooxidans protein 2), as it lies second closest to the repeats
ISGFIRLTAPLHIAAPGSMRFDGKTVYGGKTVGVPCTGITREVLFNEAGEAKHIPYIAANNIRGRLRRHA
ARIIMEALRLRGQKVSLALYNVLQCGAVTGNPDGKDMTLGEYRQARDDPYFGLFGGGPKMMRSRCLEVED
ALPVHADTTALLPSMAHPHAHRAAPGDHFTEVWGIRRNDDLRRLVNIDQAAEVVQNFEAEFAARQQAILN
EVDREQKGSSKTSGKDSEKLKTNDLKTYSAVEFIIPGTLLYFSILMKDAITDAQAGLLLLALDSLANTEA
LGGYGRNGFGRFTAAILLTSDGDEHQDAFHDGRLNGEDPLTAHTLPAWHAASQKIDATALANLI
>gnl|CDD|132160 TIGR03116, cas5_csf3, CRISPR type IV/AFERR-associated protein Csf3. Members of this family show up near CRISPR repeats in Acidithiobacillus ferrooxidans ATCC 23270, Azoarcus sp. EbN1, and Rhodoferax ferrireducens DSM 15236. In the latter two species, the CRISPR/cas locus is found on a plasmid. This family is one of several characteristic of a type of CRISPR-associated (cas) gene cluster we designate Aferr after A. ferrooxidans, where it is both chromosomal and the only type of cas gene cluster found. The gene is designated csf3 (CRISPR/cas Subtype as in A. ferrooxidans protein 3), as it lies third closest to the repeats
PLEIRFRLATPMVHSDYPFHFDALMAYAVSRDALMNASADPWGDARDLSEDLPLGKEEEGDSWVWKASRL
EVLAFLPYPKRYETAKTLPFTDPSRFIGDDLDRGLWQARGKVNPETFRIDTNRGQQKNYQMYYTTENAQE
LAAWCIGDEEALEFLLSQITHIGKGTRNGHGRISNAEIRDDEEAADRWKKRWLPKDMPGADYAPIMGRLR
QPYW
>gnl|CDD|274436 TIGR03117, cas_csf4, CRISPR type AFERR-associated DEAD/DEAH-box helicase Csf4. Members of this family show up near CRISPR repeats in Acidithiobacillus ferrooxidans ATCC 23270, Azoarcus sp. EbN1, and Rhodoferax ferrireducens DSM 15236. In the latter two species, the CRISPR/cas locus is found on a plasmid. This family is one of several characteristic of a type of CRISPR-associated (cas) gene cluster we designate Aferr after A. ferrooxidans, where it is both chromosomal and the only type of cas gene cluster found. The gene is designated csf4 (CRISPR/cas Subtype as in A. ferrooxidans protein 1), as it lies farthest (fourth closest) from the repeats in the A. ferrooxidans genome
EQALFYLNCLTSLRQKRIGMLEASTGVGKTLAMIMAALTMLKERPDQKIAIAVPTLALMGQLWSELERLT
AEGLAGPVQAGFFPGSQEFVSPGALQELLDQSGYDKDPAVQLWIGQGGPLIHEAALIRCMSDAPTKMHWM
THDLKAVATLLNRQDDVTLAIREDDEDKRLVESREYEAEARRCRILFCTHAMLGLAFRDKWGLLPQPDIL
IVDEAHLFEQNISRVYSNALSLRRLHLYVEKRHTGAGKGIVSAAVAAVSHCIQRLRALDVFGDGQTLCLD
AGNKELETLFADLDAALDACSVGRNRDENKKALSVVKDVKKARFILDNAITAIQGKASAVLQFSPDRRFP
SLIVGREDLGKVMGGLWKDVTHGAIIVSATLYLPDRFGQMSCDYLKRVLSLPLSRLDTPSPIVAPWVRNA
IPHLHVPNAKARFLRPVGKDEQGDANLQEAERTWLENVSLSTAAILRKAQGGTLVLTTAFSHISAIGQLV
ELGIPAEIVIQSEKNRLASAEQQFLALYANGIQPVLIAAGGAWTGIDLTHKPVSPDKDNLLTDLIITCAP
FGLNRSLSMLKRIRKTSVRPWEIINESLMMLRQGLGRLVRHPDMPQNRRIHMLDGRIHWPYMESWQESVK
TILDGY
>gnl|CDD|132162 TIGR03118, PEPCTERM_chp_1, TIGR03118 family protein. This model describes and uncharacterized conserved hypothetical protein. Members are found with the C-terminal putative exosortase interaction domain, PEP-CTERM, in Nitrosospira multiformis, Rhodoferax ferrireducens, Solibacter usitatus Ellin6076, and Acidobacteria bacterium Ellin345. It is found without the PEP-CTERM domain in several other species, including Burkholderia ambifaria, Gloeobacter violaceus PCC 7421, and three copies in the Acanthamoeba polyphaga mimivirus [Hypothetical proteins, Conserved]
YTQRNLVTNSPAHAAQIVDPGLRNAWGLSYRPGGPFWVANTGTGTATLYVGNPDTQPLVQDPLVVVIPAP
PPLAAEGTPTGQVFNGSDTFVVSGEGITGPSRFLFVTEDGTLSGWAPALGTTRMTRAEIVVDASQQGNVY
KGLAVGPTGGGDYLYAANFRQGRIDVFKGSFRPPPLPGSFIDPALPAGYAPFNVQNLGGTLYVTYAQQDA
DRNDEVAGAGLGYVNVFTLNGQLLRRVASSGRLNAPWGLAIAPESFGSLSGALLVGNFGDGTINAYDPQS
GAQLGQLLDPDNHPVKVDGLWSLTFGNGVSGGSANYLYFTAGPDDEQHGLFGVLTA
>gnl|CDD|132163 TIGR03119, one_C_fhcD, formylmethanofuran--tetrahydromethanopterin N-formyltransferase. Members of this protein family are the FhcD protein of tetrahydromethanopterin (H4MPT)-dependent C-1 carrier metabolism. In the archaea, FhcD is designated formylmethanofuran--tetrahydromethanopterin N-formyltransferase, while in bacteria it is commonly designated as formyltransferase/hydrolase complex subunit D. FhcD is essential for one-carbon metabolism in at least three groups of prokaryotes: methanogenic archaea, sulfate-reducing archaea, and methylotrophic bacteria [Central intermediary metabolism, One-carbon metabolism]
IEDTFAEAFDMKAARVLITAATYRWAMEAATEATGFATSVIMCPAEAGIEKELSPAETPDGRPGVSILIF
HMSKKGLEKQLLERIGQCVLTAPTTAVFNGLPEAEEKIPLGFKLRFFGDGYQISKELDGRRYWRIPVMDG
EFLCEDDFGITKGVAGGNFFIMAETQPSALAAAEAAVDAIREVPGVITPFPGGIVASGSKVGSKYKFLPA
STNDAYCPTLKDQVESELPEGVNAVYEIVIDGLNEAAIAEAMRVGILAATEIPGVVKITAGNYGGKLGPH
HIHLREL
>gnl|CDD|274437 TIGR03120, one_C_mch, methenyltetrahydromethanopterin cyclohydrolase. Members of this protein family are the enzyme methenyltetrahydromethanopterin cyclohydrolase, a key enzyme for tetrahydromethanopterin (H4MPT)-linked C1 transfer metabolism [Central intermediary metabolism, One-carbon metabolism]
SVNENALPIVESMIRNAEKLRVEVAKLENGATVIDCGVNVPGSLEAGLLFAEVCLGGLAEVTIVPFPIDG
LKWPAVQVTTDHPVIACLGSQKAGWQVKVGKYFAMGSGPARALALKPKETYEEIGYEDDSDVAVIVLESD
KLPDEEVAEYIADECGVDPENLTLLVAPTASLVGSIQISARVVETALHKLEELGFDVTKIVSAAGTAPIP
PVKPDFIQAMGRTNDAILYGGRVYLYVKADDEDLEELAEKLPSSASDDYGKPFAEIFKEANYDFYKIDPG
LFSPAEVTVNDLKTGKTYHAGELNPEVLKKSFG
>gnl|CDD|274438 TIGR03121, one_C_dehyd_A, formylmethanofuran dehydrogenase subunit A. Members of this largely archaeal protein family are subunit A of the formylmethanofuran dehydrogenase. Nomenclature in some bacteria may reflect inclusion of the formyltransferase described by TIGR03119 as part of the complex, and therefore call this protein formyltransferase/hydrolase complex Fhc subunit A. Note that this model does not distinguish tungsten (FwdA) from molybdenum-containing (FmdA) forms of this enzyme; a single gene from this family is expressed constitutively in Methanobacterium thermoautotrophicum, which has both tungsten and molybdenum forms and may work interchangeably
EILIKNGTVYDPANGIDGEVMDIFIRDGKIVEPVSGGTKPAKVIDASGKLVMAGGVDSHTHIAGPKVNVG
RLLRPEDHRRDPEPRTGLTRAGSGFSVPSTYATGYRYARMGYTTVFEAAVPPLNARHTHEEFADTPILDK
GGYTLLGNNWFLLEYLKDGEPEKAAAYVAWLLKATKGYGIKVVNPGGVEAWGWGENVLSLDDPVPYFGIT
PREIIKGLARANEELGLPHSIHVHCNNLGVPGNYETTLDTLDAAEGVKPNRNQVLHLTHVQFHSYGGTSW
RDFESGAEKIADYVNANPNVTIDVGQVTFGETTTMTADGPMEYDLHKLTGLKWANKDVELETGSGVVPFK
YSPKNPVHALQWAIGLELFLLIKDPWRVFLTTDHPNGGPFTRYPRIIALLMSRKYREDMLSTVHPWAAAR
STLGGIDREYSLYEIAIMTRAGPAKLLGLTDRGHLGVGADADIAVYDINPDDVDTDYADVEKAFSTALYV
FKDGEIVVKDGEIVETPWGRTYWVDAKVPEEMDKEIEPDLRDKFRRYYTVGLDNYAVPDEYIPKPT
>gnl|CDD|274439 TIGR03122, one_C_dehyd_C, formylmethanofuran dehydrogenase subunit C. Members of this largely archaeal protein family are subunit C of the formylmethanofuran dehydrogenase. Nomenclature in some bacteria may reflect inclusion of the formyltransferase described by TIGR03119 as part of the complex, and therefore call this protein formyltransferase/hydrolase complex Fhc subunit C. Note that this model does not distinguish tungsten (FwdC) from molybdenum-containing (FmdC) forms of this enzyme
LTLTPKKEPSVPLEADPILPDNLAGKSAEEIEALELWYGNKTVPLGDLFDVEGDGKPDETRLVIDGDMSR
VKRIGENMSAGEIVVEGDVGMHVGAEMKGGKIVVNGNADSWAGCEMKGGEIIIKGNAGDYVGSAYRGEWR
GMSGGKIIVEGNAGDYLGERMRGGEILIKGNAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRGTIVVGGKV
DELLPTFKFEGLHELPFLLKSAFTQAIGTFHKFTGDYANKGKGELYI
>gnl|CDD|163144 TIGR03123, one_C_unchar_1, probable H4MPT-linked C1 transfer pathway protein. This protein family was identified, by the method of partial phylogenetic profiling, as related to the use of tetrahydromethanopterin (H4MPT) as a C-1 carrier. Characteristic markers of the H4MPT-linked C1 transfer pathway include formylmethanofuran dehydrogenase subunits, methenyltetrahydromethanopterin cyclohydrolase, etc. Tetrahydromethanopterin, a tetrahydrofolate analog, occurs in methanogenic archaea, bacterial methanotrophs, planctomycetes, and a few other lineages [Central intermediary metabolism, One-carbon metabolism]
LGIDIGGANTKAAELDEDGRIKEVHQLYCPLWKGNDKLAETLKEISQDLSSADNVAVTMTGELADCFEDK
AEGVEFILAAVESAFGSPVSVFASDGGFVSAEEALTNPLDVAAANWLATAQLIAKRIPECLFVDMGSTTT
DIIPIIDGEVAAKGKTDLERLKTGELVYTGVLRTPISALAREVPLEGEWTRVSSEYFAITADVYRLLGEI
TEEDYTCDTPDGKGKSIEECMRRLARMVCADLEELGEEDVRNLAKYYYEAQLEQLTEAIEEVLERYGLKT
VVAAGAGEFLAKEAAARLGRECIDVDERLGKEVSTAAP
>gnl|CDD|163145 TIGR03124, citrate_citX, holo-ACP synthase CitX. Members of this protein family are the CitX protein, or CitX domain of the CitXG bifunctional protein, of the citrate lyase system. CitX transfers the prosthetic group 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA to the citrate lyase gamma chain, an acyl carrier protein. This enzyme may be designated holo-ACP synthase, holo-citrate lyase synthase, or apo-citrate lyase phosphoribosyl-dephospho-CoA transferase. In a few genera, including Haemophilus, this protein occurs as a fusion protein with CitG (2.7.8.25), an enzyme involved in prosthetic group biosynthesis. This CitX family is easily separated from the holo-ACP synthases of other enzyme systems [Energy metabolism, Fermentation, Protein fate, Protein modification and repair]
VSLEELLAAREQRVARQQELLKKYPLTLLSLTLNIPGPIKNNELLRRVFDIGIKAIEALLAKNGWTILVQ
QALNEATGPEAFLVVDAPALELKRLMIKLEESHPLGRLWDIDVLDADGKSLSRTDLGLPPRKCLLCEEDA
KICARSRRHSLEELQNKIEEKIHKY
>gnl|CDD|132169 TIGR03125, citrate_citG, triphosphoribosyl-dephospho-CoA synthase CitG. Triphosphoribosyl-dephospho-CoA is transferred to, and becomes the prosthetic group of, the respective acyl carrier protein subunits of both citrate lyase and malonate decarboxylase. Members of this protein family are triphosphoribosyl-dephospho-CoA synthases specifically from citrate lyase systems. This protein sometimes occurs as a fusion protein with CitX, the phosphoribosyl-dephospho-CoA transferase [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Energy metabolism, Fermentation]
KEIANLAYKALLYEVSLTPKPGLVDPINNGAHKDMDLYTFIDSALALSPYFSKFIEAGMEYAALPPEQLL
SQLRPLGLAAEKAMFQATNGVNTHKGAIFSLGLLCAAIGRLLARGPPLDLKLICSLVATMCQGLVDNELE
NLNNKKPLTAGERLFQQYGLTGARGEAESGYPTVMQHALPALQELTKQLDTEQRLLDTLLYLMANNEDTN
LVHRGGIEGLKFVQQEAQKLLQKGGSRTEALTAALRELDQEFIERNLSPGGSADLLALTIFLAFL
>gnl|CDD|132170 TIGR03126, one_C_fae, formaldehyde-activating enzyme. This family consists of formaldehyde-activating enzyme, or the corresponding domain of longer, bifunctional proteins. It links formaldehyde to the C1 carrier tetrahydromethanopterin (H4MPT), an analog of tetrahydrofolate, and is common among species with H4MPT. The ribulose monophosphate (RuMP) pathway, which removes the toxic metabolite formaldehyde by assimilation, runs in the opposite direction in some species to produce ribulose 5-phosphate for nucleotide biosynthesis, leaving formaldehyde as an additional metabolite. In these species, formaldehyde activating enzyme may occur as a fusion protein with D-arabino 3-hexulose 6-phosphate formaldehyde lyase from the RuMP pathway
YRIGEALIGEGNEVAHIDLIIGPKGGPVGTAFANALANLSAGHTPLLAVLRPNLPTKPATLIVPKVTIKN
MAQAVQMFGPAQAAVAKAVADSVEEGIIPKDEADDLVIIVSVFIHPEAKDDRKIYKYNYEATKLAIKRAM
EGEPSVDEVLAKKDSATHPF
>gnl|CDD|132171 TIGR03127, RuMP_HxlB, 6-phospho 3-hexuloisomerase. Members of this protein family are 6-phospho 3-hexuloisomerase (PHI), or the PHI domain of a fusion protein. This enzyme is part of the ribulose monophosphate (RuMP) pathway, which in one direction removes the toxic metabolite formaldehyde by assimilation into fructose-6-phosphate. In the other direction, in species lacking a complete pentose phosphate pathway, the RuMP pathway yields ribulose-5-phosphate, necessary for nucleotide biosynthesis, at the cost of also yielding formaldehyde. These latter species tend usually have a formaldehyde-activating enzyme to attach formaldehyde to the C1 carrier tetrahydromethanopterin
AKLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSI
KKGDLLIAISGSGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGNYKSIQP
LGSLFEQSLLLFLDAVILKLMKKKGLDEEEMKKRHANLE
>gnl|CDD|132172 TIGR03128, RuMP_HxlA, 3-hexulose-6-phosphate synthase. Members of this protein family are 3-hexulose-6-phosphate synthase (HPS), or the HPS domain of a fusion protein. This enzyme is part of the ribulose monophosphate (RuMP) pathway, which in one direction removes the toxic metabolite formaldehyde by assimilation into fructose-6-phosphate. In the other direction, in species lacking a complete pentose phosphate pathway, the RuMP pathway yields ribulose-5-phosphate, necessary for nucleotide biosynthesis, at the cost of also yielding formaldehyde. These latter species tend usually have a formaldehyde-activating enzyme to attach formaldehyde to the C1 carrier tetrahydromethanopterin. In these species, the enzyme is viewed as a lyase rather than a synthase and is called D-arabino 3-hexulose 6-phosphate formaldehyde lyase. Note that there is some overlap in specificity with the Escherichia coli enzyme 3-keto-L-gulonate 6-phosphate decarboxylase
KLQLALDLLDIEEALELAEKVADYVDIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAE
QAFAAGADIVTVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKRAKELKELGADYIGVHTGLDEQA
KGQNPFEDLQTILKLVKEARVAVAGGINLDTIPDVIKLGPDIVIVGGAITKAADPAEAARQIRKLI
>gnl|CDD|132173 TIGR03129, one_C_dehyd_B, formylmethanofuran dehydrogenase subunit B. Members of this largely archaeal protein family are subunit B of the formylmethanofuran dehydrogenase. Nomenclature in some bacteria may reflect inclusion of the formyltransferase described by TIGR03119 as part of the complex, and therefore call this protein formyltransferase/hydrolase complex Fhc subunit C. Note that this model does not distinguish tungsten (FwdB) from molybdenum-containing (FmdB) forms of this enzyme
NVVCPFCGCLCDDIEVEVEGNKIVKVENACRIGAAKFKEAEESHRITRPMIRKNGDGKEVSYEEAIEKAA
EILKNAKRPLIYGWSSTSCEAQRAGLELAEKLGAVIDNTASVCHGPSLLALQEVGWPSCTLGEVKNRADV
IIYWGTNPMHAHPRHMSRYSVFPRGFFTQRGREDRTVIVVDPRKTDTAKLADYHLQIKPGSDYELISALR
AVLRGKEPQPEEVAGIPKEKILELAEILKNAKFGVIFFGLGLTSSLGKHRNVEIAIELVKDLNKYTKFTI
IPMRGHYNVAGFNQVLTWETGYPFGVDFSRGYPRYNPGETTTVDLLKRKEVDAALIIGSDPGAHFPQDAV
KHLAEIPVIVIDPHPTPTTEIADVVIPVAIDGIEAGGTAYRMDNVPIRLRKVIESPEPSDEEILKKILER
V
>gnl|CDD|188283 TIGR03130, malonate_delta, malonate decarboxylase acyl carrier protein. Members of this protein family are the acyl carrier protein, also called the delta subunit, of malonate decarboxylase. This subunit has the same covalently bound prosthetic group, derived from and similar to coenzyme A, as does citrate lyase, although this protein and the acyl carrier protein of citrate lyase do not show significant sequence similarity. Both malonyl and acetyl groups are transferred to the prosthetic group for catalysis
ETLTFEFPAQAPARGKAPALVGVVGSGDLEVLVEPGALGGKTEVQIVTSVDGFDAVWQAVLERFFARYPL
AGLQIEINDFGATPAVVSLRLRQALEEL
>gnl|CDD|132175 TIGR03131, malonate_mdcH, malonate decarboxylase, epsilon subunit. Members of this protein family are the epsilon subunit of malonate decarboxylase. This subunit has malonyl-CoA/dephospho-CoA acyltransferase activity. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. The epsilon subunit is closely related to the malonyl CoA-acyl carrier protein (ACP) transacylase family described by TIGR00128, but acts on an ACP subunit of malonate decarboxylase that has an unusual coenzyme A derivative as its prothetic group
IALLFPGQGSQRAGMLAELPDHPAVAAVLAEASDVLGIDPRELDDAEALASTRSAQLCILAAGVAAWRAL
LALLPRPSAVAGYSVGEYAAAVVAGVLTFDDALRLVALRAALMDQAVPGGYGMLAVLGLDLAAVEALIAK
HGVYLAIINAPDQVVIAGSRAALRAVAELARAAGASRAKRLAVRVPSHTPLLAKAAEQFAEALAEIPLAA
PRLPYLSGIDARLVRDAAQIRDDLARQIATPVDWHDCMQAAYERGARLVIELGPGDVLTKLANEAFPELP
ARSADDFRSLDGLLA
>gnl|CDD|274440 TIGR03132, malonate_mdcB, triphosphoribosyl-dephospho-CoA synthase MdcB. This protein acts in cofactor biosynthesis, preparing the coenzyme A derivative that becomes attached to the malonate decarboxylase acyl carrier protein (or delta subunit). The closely related protein CitG of citrate lyase produces the same molecule, but the two families are nonetheless readily separated [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
AQRIADLAVQALYDEVALTPKPGLVDPRDSGAHTDMDLALFLRSAFALRPYFAAMAEAGARHAAFAQALR
ERLRALGREAEAAMLAATGGVNTHRGAIFALGLLCAAAAKLAAQRAALTAIALCAGVIARWGDRLQREPR
DADSHGQRVRRRYGVGGAREEAAQGFPAVREVGLPALRAARAAGHDEEAARLHALLALMAALDDTNVLHR
GGPDGLAFAQTGAREFLAAGGVLTSDGRRALHALDQDFVARRLSPGGSADLLAATLFLDSLE
>gnl|CDD|188285 TIGR03133, malonate_beta, biotin-independent malonate decarboxylase, beta subunit. Members of this protein family are the beta subunit of malonate decarboxylase. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. In the malonate decarboxylase complex, the beta subunit appears to act as a malonyl-CoA decarboxylase
RSFYEANARERARGLLDAGSFRELLGPFDRVISPHLALLGIVPQFDDGVVVGRGTIDGKPVVVIAQEGRF
QGGSVGEVHGAKIVGALRLAIEDNRKGQPTAVVLLLETGGVRLQEANAGLIAIAEIMRAILDARAAVPVI
GVIGGRVGCFGGMGIAAGLCSYLIMTEEGRLGLSGPEVIEQEAGVEEFDSRDRALVWRTTGGKHRFLSGD
ADVLVEDDVDAFRAAVIALLALGLPAAPRSDLAALYAEQLRLALRLARQGDCRDARDVWQALGA
>gnl|CDD|274441 TIGR03134, malonate_gamma, biotin-independent malonate decarboxylase, gamma subunit. Members of this protein family are the gamma subunit of malonate decarboxylase. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. In the malonate decarboxylase complex, the beta subunit appears to act as a malonyl-CoA decarboxylase, while the gamma subunit appears either to mediate subunit interaction or to act as a co-decarboxylase with the beta subunit. The beta and gamma subunits exhibit some local sequence similarity
RGRDWLAALFPNGHEVAGDPGVLVGSAELAGGKVTVIGVVPDAEVGLDEGLALAQAVLDVIEADPKRPIV
VLVDTPSQAYGRREELLGINQALAHLAKALALARLAGHPVIGLVYGRAISGAFLAHGLQADRIIALPGAM
VHVMDLESMARVTKRSVEELEALAKSSPVFAPGIENFVKLGGVHALLDVADADAPAAQIAAVRAALAAAI
QDGRRDLGAERGGRKAAAEVRERVRAQW
>gnl|CDD|274442 TIGR03135, Phosphoribosyl-dephospho-CoA_transferase, malonate decarboxylase holo-[acyl-carrier-protein] synthase. Malonate decarboxylase, like citrate lyase, has a unique acyl carrier protein subunit with a prosthetic group derived from, and distinct from, coenzyme A. Members of this protein family are the phosphoribosyl-dephospho-CoA transferase specific to the malonate decarboxylase system. This enzyme can also be designated holo-ACP synthase (2.7.7.61). The corresponding component of the citrate lyase system, CitX, shows little or no sequence similarity to this family [Energy metabolism, Other]
RRHDLVWLDPAAWLASLPLPAAQPAWADWLAAGRPVVVRRQAPDDAGQVALGLRLPGAARKQRLALWVAA
DAIARVVSPPALADVLPAAPLAWQPALRALDAALDALGVPWGVYGSAGWQLLTGLPYLHASSDLDLLLRA
PSPLSLARALALLQALEALAPCRIDGELVTPDGAAVAWRELAADAARVLLKTADGVRLVKRP
>gnl|CDD|188287 TIGR03136, decarboxylase_subunit_of_malonate_decarboxylase, Na+-transporting malonate decarboxylase, carboxybiotin decarboxylase subunit. Malonate decarboxylase can be a soluble enzyme, or a sodium ion-translocating with additional membrane-bound components. Members of this protein family are integral membrane proteins required to couple decarboxylation to sodium ion export. This family belongs to a broader family, TIGR01109 of sodium ion-translocating decarboxylase beta subunits [Transport and binding proteins, Cations and iron carrying compounds]
EQLFTVFPGIGTLFVQDPVISIARLALIGLGFFLAYLGFKRTLEPLIMVPMGLGMMAVNAGVMFLEAGQV
GTLHLDPLVSEPSVLVNIMQINFLQPVYNFTFSNSLVACMLFFGIGTMSDISFILARPWASITVALFAEM
GTFATLVIGYYCGLTPGEAAAVGTIGGADGPMVLFASLMLAKDLFVPISIIAYLYLSLTYAGYPYLVKLL
VPKKYRGLEVEMDFPDVSQRAKFVFTVVAAGLLCLLLPVASPLILSFFLGVAIKEAQIEPYQNLLEKTVT
YGSTLFLGLVLGVLCEASTLLDPRVALLLVLGITALLISGLGGILGGWFVYWFSKGKFNPVIGIAGVSCM
PTTAKIAQKIAFEANPYAMIMPLAMGAGICGVIVSAIAVGVFASTIGLV
>gnl|CDD|211789 TIGR03137, AhpC, peroxiredoxin. This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one subunit of a two-subunit complex with subunit F(TIGR03140). Usually these are found as an apparent operon. The gene has been characterized in Bacteroides fragilis, where it is important in oxidative stress defense. This gene contains two invariant cysteine residues, one near the N-terminus and one near the C-terminus, each followed immediately by a proline residue [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions]
MSLINTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYS
VSTDTHFVHKAWHDTSEAIGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNG
IGRDASELLRKIKAAQYVAAHPGEVCPAKWKEGAETLKPSLDLVGKI
>gnl|CDD|274443 TIGR03138, QueF, 7-cyano-7-deazaguanine reductase. This enzyme catalyzes the 4-electron reduction of the cyano group of 7-cyano-7-deazaguanine (preQ0) to an amine. Although related to a large family of GTP cyclohydrolases (pfam01227), the relationship is structural and not germane to the catalytic mechanism. This mode represents the longer, gram-negative version of the enzyme as found in E. coli. The enzymatic step represents the first point at which the biosynthesis of queuosine in bacteria and eukaryotes is distinguished from the biosynthesis of archaeosine in archaea [Transcription, RNA processing]
MTLEHSPLGKSTEYPDEYDPSLLFPIPRSLNRDELGLDADKLPFVGVDIWNAYELSWLNAKGKPQVAIGE
FRIPATSPNLIESKSFKLYLNSFNQTRFDSWEEVRQTLEKDLSAAAGAEVSVELFPLDEFAELPIAAPDG
ICIDDLDIEIDNYQPDPSLLKTDQSDEEVEETLYSHLLKSNCPVTGQPDWGSVQIRYRGKKIDREALLRY
LISFRQHNEFHEQCVERIFADIMRFCQPEKLTVYARYTRRGGLDINPYRSNDEAATPDNIRLARQ
>gnl|CDD|213775 TIGR03139, QueF-II, 7-cyano-7-deazaguanine reductase. This enzyme catalyzes the 4-electron reduction of the cyano group of 7-cyano-7-deazaguanine (proQ1) to an amine. Although related to a large family of GTP cyclohydrolases (pfam01227), the relationship is structural and not germane to the catalytic mechanism. This mode represents the shorter, gram-positive version of the enzyme as found in B. subtilis. The enzymatic step represents the first point at which the biosynthesis of queuosine in bacteria and eukaryotes is distinguished from the biosynthesis of archaeosine in archaea
PSKELLEAFPNPYPDRDYTIEFVCPEFTSLCPKTGQPDFATIVISYIPDQRCVELKSLKLYLFSFRNHGI
FHEDVTNTILDDLVALLDPRYLEVIGDFTPRGGIKTIVFVEYGKP
>gnl|CDD|274444 TIGR03140, AhpF, alkyl hydroperoxide reductase subunit F. This enzyme is the partner of the peroxiredoxin (alkyl hydroperoxide reductase) AhpC which contains the peroxide-reactive cysteine. AhpF contains the reductant (NAD(P)H) binding domain (pfam00070) and presumably acts to resolve the disulfide which forms after oxidation of the active site cysteine in AphC. This proteins contains two paired conserved cysteine motifs, CxxCP and CxHCDGP [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions]
MLDQSLLAQLKSYLASLENPVTLVLSAGSHEKSKELLELLDEIASLSDKISLTQNTADTLRKPSFTILRD
GADTGIRFAGIPGGHEFTSLVLAILQVGGHGPKLDEGIIDRIRRLNGPLHFETYVSLTCQNCPDVVQALN
QMALLNPNISHTMIDGALFQDEVEALGIQGVPAVFLNGEEFHNGRMDLAELLEKLEETAGVEAASALEQL
DPYDVLVVGGGPAGAAAAIYAARKGLRTAMVAERIGGQVKDTVGIENLISVPYTTGSQLAANLEEHIKQY
PIDLMENQRAKKIETEDGLIVVTLESGEVLKAKSVIVATGARWRKLGVPGEKEYIGKGVAYCPHCDGPFF
KGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFADELKADKVLQDKLKSLPNVDILTSAQTTEIVGDGDK
VTGIRYQDRNSGEEKQLDLDGVFVQIGLVPNTEWLKDAVELNRRGEIVIDERGRTSVPGIFAAGDVTTVP
YKQIIIAMGEGAKAALSAFDYLIRQ
>gnl|CDD|274445 TIGR03141, cytochro_ccmD, heme exporter protein CcmD. The model for this protein family describes a small, hydrophobic, and only moderately well-conserved protein, tricky to identify accurately for all of these reasons. However, members are found as part of large operons involved in heme export across the inner membrane for assembly of c-type cytochromes in a large number of bacteria. The gray zone between the trusted cutoff (13.0) and noise cutoff (4.75) includes both low-scoring examples and false-positive matches to hydrophobic domains of longer proteins
MGGYAFYVWLAYGITFLVLAILILWSLLDRRRLLRELRRLQAREA
>gnl|CDD|274446 TIGR03142, cytochro_ccmI, cytochrome c-type biogenesis protein CcmI. This TPR repeat-containing protein is the CcmI protein (also called CycH) of c-type cytochrome biogenesis. CcmI is thought to act as an apo-cytochrome c chaperone. This model describes the N-terminal region of the protein, Members of this protein family [Protein fate, Protein folding and stabilization, Energy metabolism, Electron transport]
LFWIVAALLTLVALLFLLLPLLRRRRAAATVDRDELNLAVYRDRLAELERDLAEGLLDEAEAEAARAELQ
RRLLADIPAAETAAARQAKRSGRLAALVVVLLLPVLALGLYLKLGAP
>gnl|CDD|132187 TIGR03143, AhpF_homolog, putative alkyl hydroperoxide reductase F subunit. This family of thioredoxin reductase homologs is found adjacent to alkylhydroperoxide reductase C subunit predominantly in cases where there is only one C subunit in the genome and that genome is lacking the F subunit partner (also a thioredcxin reductase homolog) that is usually found (TIGR03140)
MEEIYDLIIIGGGPAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPGILNTTGPELMQEMRQQA
QDFGVKFLQAEVLDVDFDGDIKTIKTARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEF
FTGMDVFVIGGGFAAAEEAVFLTRYASKVTVIVREPDFTCAKLIAEKVKNHPKIEVKFNTELKEATGDDG
LRYAKFVNNVTGEITEYKAPKDAGTFGVFVFVGYAPSSELFKGVVELDKRGYIPTNEDMETNVPGVYAAG
DLRPKELRQVVTAVADGAIAATSAERYVKELKEKLGIAEEYEEEEAKEASEASAAETTPAATTKKGSLLD
DSLRQQLVGIFGRLENPVTLLLFLDGSNEKSAELQSFLGEFASLSEKLNSEAVNRGEEPESETLPKITKL
PTVALLDDDGNYTGLKFHGVPSGHELNSFILALYNAAGPGQPLGEELLEKIKKITKPVNIKIGVSLSCTL
CPDVVLAAQRIASLNPNVEAEMIDVSHFPDLKDEYGIMSVPAIVVDDQQVYFGKKTIEEMLELIG
>gnl|CDD|274447 TIGR03144, cytochrome_c_biogenesis_protein_chloroplast, cytochrome c-type biogenesis protein CcsB. Members of this protein family represent one of two essential proteins of system II for c-type cytochrome biogenesis. Additional proteins tend to be part of the system but can be replaced by chemical reductants such as dithiothreitol. This protein is designated CcsB in Bordetella pertussis and some other bacteria, resC in Bacillus (where there is additional N-terminal sequence), and CcsA in chloroplast. We use the CcsB designation here. Member sequences show regions of strong sequence conservation and variable-length, poorly conserved regions in between; sparsely filled columns were removed from the seed alignment prior to model construction [Energy metabolism, Electron transport, Protein fate, Protein modification and repair]
LMILGFILITGLLVLRWIESGHFPLSNLYESLLFLSWSLSLIYLILERKYKLRLLGAFVAPLALLILGFA
TLVLPVEMQQSTPLVPALQSNWLMMHVSVMILSYAALLVGSLLSIAYLVKTRKPKKKLKGSSSSFLGKNS
RRLPLLETLDNLSYRTIAIGFPLLTIGIISGAVWANEAWGSYWSWDPKETWALITWLIYAAYLHARLTKG
WRGKKAAWLASIGFFVVWFCYLGVNLLGSGLHSYG
>gnl|CDD|274448 TIGR03145, cyt_nit_nrfE, cytochrome c nitrate reductase biogenesis protein NrfE. Members of this protein family closely resemble the CcmF protein of the CcmABCDEFGH system, or system I, for c-type cytochrome biogenesis (GenProp0678). Members are found, as a rule, next to closely related paralogs of CcmG and CcmH and always located near other genes associated with the cytochrome c nitrite reductase enzyme complex. As a rule, members are found in species that also encode bona fide members of the CcmF, CcmG, and CcmH families
MIPELGFIALLLATVSAFLLALLPLFGLIKKNPYLIGFAWPLSYLFAIFLTIALGLLAYSFAVDDFSVVY
VAQHSNSQLPLFFKVAAVWGGHEGSMLFWLFALALWGAAFAFFSRKKDPAFSARVLAILGLICLGFALFI
LFTSNPFERLFPIPPEGRDLNPMLQDIGLIFHPPLLYLGYVGFAVNFAMALAALISGHLDAAVARWSRPW
VLLSWVFLTGGIMLGSWWAYYELGWGGWWFWDPVENASLMPWLLGTALLHSLIVTEKRGIFSYWTLLLSL
FAFSLSLLGTFIVRSGVLTSVHAFAVDPTRGIALLLLFFLLTASALTLFALKANLRQSAVRFGLFSKEGA
LLLGNVLLTVATVSVLLGTFYPMIFQALGWGSISVGAPYFNSIFVPLAFLLMALMGLAPLLRWQNLAKTL
FIQRMWLLLPALILAYIGIWLSLQANSGLRFNLFALVLLSLAIWLILSTLWAPWRQRTLKLRQLGMVLAH
LGVAICAIGAIMVSYFGSEIGVRLAPQQQQPLGGYEFRYQGFENVIGPNYTAEQANFSVTKNGKILAEIK
PERRYYDVRTMNMSEVGIDWGFLGDIYIVMGDKLGDGEYAFRLHYKPLVRWLWL
>gnl|CDD|132190 TIGR03146, cyt_nit_nrfB, cytochrome c nitrite reductase, pentaheme subunit. Members of this protein family contain five copies of the CXXCH heme-binding motif, and are the NrfB component of the multisubunit enzyme, cytochrome c nitrite reductase [Energy metabolism, Electron transport]
RHQVELIRDPDYACLQCHKDEKETLHGSHGSEINPNTGRPVTCVNCHGNISPDHREGAKDVMRFSGAQGS
EKVPMDESTVLEQNSVCMSCHQPEDLREAFWTHDVHAKKLTCASCHTLHPAKDKMKGIDRKQRIKMCVDC
HSDQR
>gnl|CDD|274449 TIGR03147, cyt_nit_nrfF, cytochrome c nitrite reductase, accessory protein NrfF [Energy metabolism, Electron transport]
KKFLALLLFLISFSARAQMVDTYQFHNPEQRTRAVALAKSLRCPQCQNQNLVESNSPIAYDLRHEVYSMV
DEGKSNQQIIDFMTSRFGDFVRYNPPFKWQTLLLWLLPVVLLLLAAVILWRVRRRR
>gnl|CDD|274450 TIGR03148, cyt_nit_nrfD, cytochrome c nitrite reductase, NrfD subunit. Members of this protein family are NrfD, a highly hydrophobic protein encoded in the nrf operon, which encodes cytochrome c nitrite reductase. This multiple heme-containing enzyme can reduce nitrite to ammonia. Members belong to a broader Pfam protein family, pfam03916, which also contains an NrfD-related subunit of polysulphide reductase [Energy metabolism, Electron transport]
SAFHFDSLVWDWPIAIYLFLLGISAGAVMLAILLKRKVPEEKPSDNWIIRATAILAPFGIIIGLTILIFH
LTKPWTFWKLMFFYNFTSVMSMGVMLFQVYMAVLLLWLAIIFKKEVAALLNRYLPILDFVLKLIAIAERF
ENSIEIFLLVLAVLLGAYTGFLLSALKSYPMLNNPVLPALFLFSGTSSGIAACLLAILLGGKESGHSPEV
HFIHKFETPVVLFELFLLVAFFVGLYFGGGQKTVALQNALLGGFWGSWFWIGVIGIGILIPLLLNLFAND
SLKHNKGFIILVSVLSLIGVLCLRFFILYAGQMTVA
>gnl|CDD|274451 TIGR03149, cyt_nit_nrfC, cytochrome c nitrite reductase, Fe-S protein. Members of this protein family are the Fe-S protein, NrfC, of a cytochrome c nitrite reductase system for which the pentaheme cytochrome c protein, NrfB (family TIGR03146) is an unambiguous marker. Members of this protein family show similarity to other ferredoxin-like proteins, including a subunit of a polysulfide reductase [Energy metabolism, Electron transport]
SCSRRNFLAGVGALILTTGTAGTSVVSLAKEDKDKTKRYGMVHDETACIGCTACMDACREVNKVPEGVSR
LEIIRSEPYGEFPDVEYRFFRKSCQHCDNAPCVAVCPTGASFKDEETGIVDVHKDLCVGCQYCIAACPYR
VRFIHPVTKSADKCNFCRDTNLAEGKLPACVESCPTKALTFGDLNDPNSEVSQKLKQKPVYRTKVELGTK
PKLYKIPFKKGEVRR
>gnl|CDD|274452 TIGR03150, fabF, beta-ketoacyl-acyl-carrier-protein synthase II. 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model [Fatty acid and phospholipid metabolism, Biosynthesis]
RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDR
FIQYALAAAKEAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMA
AGQISIRYGAKGPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRN
DDPEKASRPFDKDRDGFVMGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARA
MRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIF
TVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGTNASLVFK
>gnl|CDD|132195 TIGR03151, enACPred_II, putative enoyl-[acyl-carrier-protein] reductase II. This oxidoreductase of the 2-nitropropane dioxygenase family (pfam03060) is commonly found in apparent operons with genes involved in fatty acid biosynthesis. Furthermore, this genomic context generally includes the fabG 3-oxoacyl-[ACP] reductase and lacks the fabI enoyl-[ACP] reductase
KTRLCDLLGIEYPIFQGGMAWVATGSLAAAVSNAGGLGIIGAGNAPPDVVRKEIRKVKELTDKPFGVNIM
LLSPFVDELVDLVIEEKVPVVTTGAGNPGKYIPRLKENGVKVIPVVASVALAKRMEKAGADAVIAEGMES
GGHIGELTTMALVPQVVDAVSIPVIAAGGIADGRGMAAAFALGAEAVQMGTRFLCAKECNVHPNYKEKVL
KAKDRDTVVTGASTGHPVRVLKNKLTRKYQELEKEGASPEEFEKLGAGALRRAVVEGDVENGSVMAGQIA
GLIKEIKPAKEIIEDIMSEAKEVIKRL
>gnl|CDD|200248 TIGR03152, cyto_c552_HCOOH, formate-dependent cytochrome c nitrite reductase, c552 subunit. Members of this protein family are cytochrome c552, a component of cytochrome c nitrite reductase, which is known more formally as nitrite reductase (cytochrome; ammonia-forming) (EC 1.7.2.2). Nitrate can be reduced by several enzymes. EC 1.7.2.2 reduces nitrite all the way to ammonia, rather than to ammonium hydroxide (nitrite reductase (NAD(P)H), EC 1.7.1.4) or nitric oxide (nitrite reductase (NO-forming), EC 1.7.2.1). Some examples of EC 1.7.2.2 occur in a seven gene system that enables formate-dependent nitrite reduction, but is also found in simpler contexts. Members of this protein family, however, belong to the formate-dependent system [Energy metabolism, Electron transport]
VEAANEKFAAKHPDQYDSWKATSESTEIEDALEEDPRLVILWAGYAFAKDYNKPRGHIYAVTDVRETLRT
GAPKDANDGPQPMACWSCKSPDVPRLIAEWGEDGYFSGKWARGGAEIVNSIGCADCHDTTSKEFAEGKPA
LRLARPHVERAMEAIGKPFEDADRFDQQAAVCGQCHVEYYFDGKTKAVKFPWDKGTDVDSMEKYYDEIGF
KDWTHSLSKAPMLKAQHPDYETWSAGIHGKNGVTCIDCHMPKVQNADGKVYTDHKIGNPFDRFDDTCANC
HTQSKATLQKVVAERKAQVKEMKLRLEDQIVKAHFEAKAAWDAGATEEEMKPILMDIRHAQWRWDYAIAS
HGVHMHAPEVALRVLGTALDKAADARAKLARLLAKKGITTPIQIPDISTKEKAQKAVGIDMEKERAEKEE
FLKTVVPQWEKQARERGLL
>gnl|CDD|274453 TIGR03153, cytochr_NrfH, cytochrome c nitrite reductase, small subunit. Members of this protein family are NrfH, a tetraheme cytochrome c. NrfH is the cytochrome c nitrite reductase small subunit, and forms a heterodimer with NrfA, the catalytic subunit. While NrfA can act as a monomer, NrfH can bind to and anchor NrfA in the membrane and enables electron transfer to NrfA from quinones [Energy metabolism, Electron transport]
LVILGVALGVGAYAFYGAKGLSYLSDDPEACANCHVMNPQYATWQHSSHHNVATCNDCHLPHNFVAKYIW
KAIDGWRHSVAFTFGTYPDVIRISEHSKKVVQENCIRCHADLVTELVPNHDDERNCWDCHRDVGH
>gnl|CDD|132198 TIGR03154, sulfolob_CbsA, cytochrome b558/566, subunit A. Members of this protein family are CbsA, one subunit of a highly glycosylated, heterodimeric, mono-heme cytochrome b558/566, found in Sulfolobus acidocaldarius and several other members of the Sulfolobales, a branch of the Crenarchaeota
SLKIKSKITIGVLLIIFLLSIIFTLENVPMAQTSPQIPVYKVVGSADLSNPGSASYWSQIPWINISLTAN
IPMAPTSGLTHYLLVKAAWNGSWIFILEEWYAPEPAFGAWSAAAAGIYPPASGPGLFRQIMLTPGTTYTI
EKNYTNYVSIVNGKEEQGRLVLNYSGILLPAPNNTQITVLSNGTIILWHSPRPVEDLLYSDGMFYGYYTN
STWYYPDRAAIMWYMGSVIPPTKDGMNIGGKYPGQQFDGVTFKDAGGSLAQPGGAANIWMWVSGATWNNS
TYDPAFKVNLWQNESLTGLPYVDPGNHGFAVPLYTNNTNMYEVDTAGIWYTPVASEGLNGSLFFIWTGAT
YENGYWTVEFARPLAVPLDYAPWMPNITVGKTYYVAFAVWQGKLGETLFDKSITSSFLTLELVTTPPTPP
TSTTTSTSPSTTTSSAIPSTTLYVTIIGVVIAIVALVILYVVFRR
>gnl|CDD|274454 TIGR03155, sulfolob_CbsB, cytochrome b558/566, subunit B. Members of this protein family are CbsB, one subunit of a highly glycosylated, heterodimeric, mono-heme cytochrome b558/566, found in Sulfolobus acidocaldarius and several other members of the Sulfolobales, a branch of the Crenarchaeota
LEKNLKYFLIILGISSFLQFMFKEAFMFPSILPLNIPAEMILLRIGNVSFYIFFISLLLVSLLLSNKYKA
LLPLTIVLIISPFLALIPNYVSSTYYYSIEIFIIIVGIMALIEATVKSSVKSVLLIPTGILVGLGLIASI
FLNFFHTALFISYLDFYLISAIGYLVYTVFWRKIKSKRSYIAIIVGLLSMIPFIFFAHEIITNRYLEILM
NMILPSTLGITLYNPYHITLLVYALGLSTMGIVSSIIKGNSSAGIGYFMLISTVFLGIDGYLLLIYMLVP
IIGFVLITYNEMRKERIIDIIS
>gnl|CDD|274455 TIGR03156, GTP_HflX, GTP-binding protein HflX. This protein family is one of a number of homologous small, well-conserved GTP-binding proteins with pleiotropic effects. Bacterial members are designated HflX, following the naming convention in Escherichia coli where HflX is encoded immediately downstream of the RNA chaperone Hfq, and immediately upstream of HflKC, a membrane-associated protease pair with an important housekeeping function. Over large numbers of other bacterial genomes, the pairing with hfq is more significant than with hflK and hlfC. The gene from Homo sapiens in this family has been named PGPL (pseudoautosomal GTP-binding protein-like) [Unknown function, General]
RAILVGVDLGNEDDEEESLEELAELAETAGAEVVGTVTQKRSRPDPATYIGKGKVEEIAELVEELEADLV
IFDHELSPSQERNLEKALGCRVIDRTGLILDIFAQRARTHEGKLQVELAQLKYLLPRLVGGWTHLSRQGG
GIGTRGPGETQLETDRRLIRERIAQLKKELEKVEKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALT
GADVYAADQLFATLDPTTRRLDLPDGGEVLLTDTVGFIRDLPHELVAAFRATLEEVREADLLLHVVDASD
PDREEQIEAVEKVLEELGAEDIPQLLVYNKIDLLDEPRIERLEEGYPEAVFVSAKTGEGLDLLLEAIAER
L
>gnl|CDD|274456 TIGR03157, cas_Csc2, CRISPR type I-D/CYANO-associated protein Csc2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. This family is designated Csc2 for CRISPR/Cas Subtype Cyano protein 2, as it is often the second gene upstream of the core cas genes, cas3-cas4-cas1-cas2
PKGRYVTLLVLRETESEALFRTEGEPENSSLVRAGDEGKTEISPLIMFKRKQSAPERRLGRELLRDYELL
IYGKSDPSNCSLNVNGMCRECPDCALYGFAAADGDGSVKSRVMYDTAFSITPASKSVEERTQNAPGEDGT
KTSFIGTRTSSINEPDFIKPGTLFPCVVTLKDVTPAEFLYVVNNIARTARYGANTTRFGRVRNRILGVFL
SPYEGPSNLELTQATYDQFASGKGLDLPDPLNVDQVNAAVREAIKNLSKEGRIVTFDLLGDEVVKLLTDV
KN
>gnl|CDD|274457 TIGR03158, cas3_cyano, CRISPR-associated helicase Cas3, subtype CYANO. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. It contains helicase motifs and appears to represent the Cas3 protein of the Cyano subtype of CRISPR/Cas system
HQVATFEALQSKDADIIFNTAPTGAGKTLAWLTPLLHGENDTIALYPTNALIEDQTEAIKEFVDVFKPER
DVNLLHVSKATLKDIKEYANDKVGSSKGEKLYNLLRNPIGTSTPIILLTNPDIFVYLTRFAYIDRGDIAA
GFYTKFSTVIFDEFHLYDAKQLVGMLFLLAYMQLIRFFECRRKFVFLSATPDPALILRLQNAKQAGVKIA
PIDGEKYQFPDNPELEADNKTQSFRPVLPPVELELIPAPDFKEEELSELAEEVIERFRQLPGERGAIILD
SLDEVNRLSDLLQQQGLGDDIGRITGFAPKKDRERAMQFDILLGTSTVDVGVDFKRDWLIFSARDAAAFW
QRLGRLG
>gnl|CDD|274458 TIGR03159, cas_Csc1, CRISPR type I-D/CYANO-associated protein Csc1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. This family is designated Csc1 for CRISPR/Cas Subtype Cyano protein 1, as it is often the first gene upstream of the core cas genes, cas3-cas4-cas1-cas2
LTLHSPVFFASRESGRLYETEPYIGNTALDYALGYILGEYVDLHGQATQRPTYEEDLAPFNDLGIYVTPA
NPIKNNTFYWSYMTNARRATMLQINYYGRQLNPPTGVASKNYPNFGRAKEIAPGNKFYFYVFTDQGEEKL
PVYIRLGKKRSKAKVTVKEVPVERKSGVYVLNHPLNPLDLKNIPNLDFNVVNMPPYPLINNGQFEGDYWQ
IDPVTNVVMPAGYKF
>gnl|CDD|274459 TIGR03160, cobT_DBIPRT, nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase. Members of this family are nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase, an enzyme of cobalamin biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
DAEARAAAQARQDSLTKPPGSLGRLEELAVQLAGIQGTVPPRIDRPAVVVFAGDHGVAAEGVSAFPQEVT
AQMVENFLAGGAAINVLARQAGADLRVVDVGVDHDLPEHPGLINRKVRRGTANIAQGPAMTREEAEAALE
AGIEAADEAIDSGADLLGTGEMGIGNTTPAAALLAALTGLPPEEVVGRGTGLDDEGLARKVAVIRRALER
HRPNAGDPLDVLAKVGGFEIAAMAGAILGAAARRIPVLVDGFISTAAALVAVRLAPGVRDYLIASHRSAE
PGHRAVLEALGLEPLLDLGMRLGEGTGAALALPLVRAAAAILNEMATFAEAGV
>gnl|CDD|274460 TIGR03161, ribazole_CobZ, alpha-ribazole phosphatase CobZ. Sequences in the seed alignment were the experimentally characterized CobZ of the methanogenic archaeon Methanosarcina mazei, and other archaeal proteins found similarly next to or very near to other cobalamin biosynthesis genes. CobZ replaces the alpha-ribazole-phosphate phosphatase (EC 3.1.3.73) called CobC in analogous bacterial pathways for cobalamin biosynthesis under anaerobic conditions [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
ILLLLESRGVTLEGMVELGMELYVGEPKEEARERLRSELERYLEDPNVAALLIAALLLDEHFEAGAIPGL
SSELRGDPVNLVADELLGAALAEYIGGFKALFNFKWYDEKKPGILAELPPFLDDAVSGLIAGCMTRLFE
>gnl|CDD|274461 TIGR03162, Adenosylcobalamin/alpha-ribazole_phosphatase, alpha-ribazole phosphatase. Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
LYLIRHGETDVNAGLCYGQTDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAERRGLPI
IKDDRLREMDFGDWEGRSWDEIPEAYPELDAWAADWQHARPPGGESFADFYQRVSEFLEELLKAHEGDNV
LIVTHGGVIRALLAHLLGLPLEQWWSFAVEYGSITLI
>gnl|CDD|132208 TIGR03164, UHCUDC, OHCU decarboxylase. Previously thought to only proceed spontaneously, the decarboxylation of 2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) has been recently been shown to be catalyzed by this enzyme in Mus musculus. Homologs of this enzyme are found adjacent to and fused with uricase in a number of prokaryotes and are represented by this model
MDKADFVAALGDIFEHSPWIAERAWAQRPFDSIEDLHAAMVGAVRAASPEQQLALIRAHPDLAGKLAVAG
ELTAESTSEQASAGLDQLSQEEFARFTRLNNAYRARFGFPFIMAVKGKTKQSILAAFEARLNNDRETEFA
RALREIERIARFRLRDL
>gnl|CDD|274462 TIGR03165, F1F0_chp_2, F1/F0 ATPase, Methanosarcina type, subunit 2. Members of this protein family are uncharacterized, highly hydrophobic proteins encoded in the middle of apparent F1/F0 ATPase operons. We note, however, that this protein is both broadly and sparsely distributed. It is found in about only about two percent of microbial genomes sequenced, with the first ten examples found coming from the Euryarchaeota, Chlorobia, Betaproteobacteria, Deltaproteobacteria, and Planctomycetes. In most of these species, surrounding operon appears to represent a second F1/F0 ATPase system, and the member proteins belong to subfamilies with the same phylogenetic distribution as the current protein family
MTLLLALLAGFLLGAFFFGGLWWTVRKGLASRRPALLFLGSLLLRTAIVLAGFYLLARGGWRRLLAALAG
FFAARVLAVRLTR
>gnl|CDD|132210 TIGR03166, alt_F1F0_F1_eps, alternate F1F0 ATPase, F1 subunit epsilon. A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 epsilon subunit of this apparent second ATP synthase
RLKILTPFRVFLDKLPVTRIVAETESGSFGLLPGHVDCVAALVPGILIYETADGGEHYVAVDQGILVKRG
ADVEVSVRNAVGGTELEELEEAVRQEFLTLDEQERSARSAMARLESDFIRRL
>gnl|CDD|274463 TIGR03167, tRNA_sel_U_synt, tRNA 2-selenouridine synthase. The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene [Protein synthesis, tRNA and rRNA base modification]
AFDPLIDVRSPAEFAEGHLPGAINLPLLNDEERAEVGTLYKQVGPFAAIKLGLALVSPNLAAHVEQWRAF
ADGPPQPLLYCWRGGMRSGSLAWLLAQIGFRVPRLEGGYKAYRRFVIDQLEELPQPFPLIVLGGMTGSGK
TELLHALANAGAQVLDLEGLANHRGSSFGALGLGPQPSQKRFENALAEALRRLDPGRPIFVEDESRRIGR
VALPDALFEAMRAAPLVELEASLEERVERLVEEYAGFEEDPEFLAAALERIRKRLGGERYQQLLALLEAG
DHREWIRALLEDYYDPMYAYQLAKKAERVSF
>gnl|CDD|274464 TIGR03168, 1-PFK, hexose kinase, 1-phosphofructokinase family. This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases
IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALL
AEEGIKNDFVEVKGETRINVKIKESSGEETELNEPGPEISEEELEQLLEKLRELLASGDIVVISGSLPPG
VPPDFYAQLIAIARKKGAKVILDTSGEALREALAAKPFLIKPNHEELEELFGRELKTLEEIIEAARELLD
RGAENVLVSLGADGALLVTKEGALKATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSA
AAFSPGTGLPDPEDVEELLDQVT
>gnl|CDD|274465 TIGR03169, selenide_water_dikinase_putative, pyridine nucleotide-disulfide oxidoreductase family protein. Members of this protein family include N-terminal sequence regions of (probable) bifunctional proteins whose C-terminal sequences are SelD, or selenide,water dikinase, the selenium donor protein necessary for selenium incorporation into protein (as selenocysteine), tRNA (as 2-selenouridine), or both. However, some members of this family occur in species that do not show selenium incorporation, and the function of this protein family is unknown
DLVLIGGGHSHALVLRMWGMKPLPGVRLTLINPGPTTPYSGMLPGHVAGHYTRDELHIDLVRLARFAGAR
LILDRAIGLDLAAKQVICAGRPPIAYDVLSIDIGSTPALPDVPGFAEHAIPAKPLGQFAQRWQRFLERAK
PQQPPRIAVIGGGAAGVELALAMAHRLRQLGRNAEVTLIDRGNVLLPGHNARVRRRLERALQERGVTLHL
GATVAEVTADAVRLEDGQTLPADFTFWATGARPPGWLAESGLALDEDGFIRVGPTLQSLSHPDIFAAGDC
AHLVHAPRPKAGVFAVRQAPVLAENLRAALTGGPLRPYRPQSDYLKLISTGDKSAVASRGGLAFSGAWLW
RWKDRIDRKFMDKF
>gnl|CDD|274466 TIGR03170, flgA_cterm, flagella basal body P-ring formation protein FlgA. This model describes a conserved C-terminal region of the flagellar basal body P-ring formation protein FlgA. This sequence region contains a SAF domain, now described by pfam08666 [Cellular processes, Chemotaxis and motility]
VVVAKRPLKRGEVITPEDLKLERGDLARLPGGVLTDPDEVVGKVAKRPLRAGQPLTANMLRPPWLVKRGD
TVTVIARGGGLSITTEGKALEDGAVGDQIRVRNLSSGKIISGIVTAPGTVEV
>gnl|CDD|132215 TIGR03171, putative_Rieske_protein, Rieske iron-sulfur protein SoxL2. This iron-sulfur protein is found in a contiguous genomic region with subunits of cytochrome b558/566 in several archaeal species, and appears to be part of a cytochrome bc1-analogous system
IKFRLNKDEKPILSYSDLYFIRKLLAKMRDPKTKFDSREFVNKGEDYLFNYVNKNVGGVDEGRRKFLKGL
IFGIAAAAVVGIIPGLRVLVPPTVAAASGFPKSLLVDSSGNPIKASSIPVNSPIITIFEYPMTGEPNFLL
NLGDSSGKPVEIPPTKVVVPQTGKTYTFPGGVGPNKSIVAYSAICQHLGCTPPYIHFYPPNYVNPSQLTA
PEPDQLTAQALLAAKQANVPALIHCDCHGSTYDPYHGAAVLTGPTVRPLPAVILEWDSSTDYLYAIGSIG
VAVYPEGSNGVPSQDPTSDLDSSFGSSVGTKTTVQETENPF
>gnl|CDD|274467 TIGR03172, Uncharacterized_protein_YqeC, probable selenium-dependent hydroxylase accessory protein YqeC. This uncharacterized protein family includes YqeC from Escherichia coli. A phylogenetic profiling analysis shows correlation with SelD, the selenium donor protein, even in species where SelD contributes to neither selenocysteine nor selenouridine biosynthesis. Instead, this family, and families TIGR03309 and TIGR03310 appear to mark selenium-dependent molybdenum hydroxylase maturation systems [Unknown function, General]
IISIVGAGGKTTLMFALARELRKEGKPVLVTTTTHIFPPPAEYFVLYEPDAAAITAALKQPGLVCAGSPA
GNKGKLTGFSPEVLDALADIADYVLIEADGAKRLPLKAPADHEPVIPKQTTHVIGVAGLSALGRPIDEVF
CHRPELFAAILGKSPGDPLTPEDIAALIAHPKGGFKNVPPEARFIILLNQADTEERIQAAEEIAKLLARR
>gnl|CDD|274468 TIGR03173, pbuX, xanthine permease. All the seed members of this model are observed adjacent to genes for either xanthine phosphoribosyltransferase (for the conversion of xanthine to guanine, GenProp0696) or genes for the conversion of xanthine to urate and its concomitant catabolism (GenProp0640, GenProp0688, GenProp0686 and GenProp0687). A number of sequences scoring higher than trusted to this model are found in different genomic contexts, and the possibility exist that these transport related compounds in addition to or instead of xanthine itself. The outgroup to this family are sequences which are characterized as uracil permeases or are adjacent to established uracil phosphoribosyltransferases
GLQHVLAMYAGAVAVPLIVGGALGLSAEQTAYLISADLFACGIATLIQTLGIGPFGIRLPVVQGVSFAAV
GPMIAIGAGDGLGAIFGAVIVAGLFVILLAPFFSKLVRFFPPVVTGTVITLIGLSLMPVAINWAAGGAGA
PDFGSPQNLGLALLTLVIILLLNRFGKGFLRSIAVLIGLVVGTIVAAALGMVDFSGVAEAPWFALPTPFH
FGAPTFDLVAILTMIIVYLVSMVETTGDFLALGEITGRKITEKDLAGGLRADGLGSALGGLFNTFPYTSF
SQNVGLVQLTGVKSRYVVAAAGVILVLLGLFPKLAALVASIPQPVLGGAGLVMFGMVAASGIRILSKVDF
DRRRNLLIVAVSLGLGLGPTVVPEFFSQLPAWAQTLFSSGIAVGAISAILLNLLFN
>gnl|CDD|274469 TIGR03174, cas_Csc3, CRISPR type I-D/CYANO-associated protein Csc3/Cas10d. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. This family is designated Csc3 for CRISPR/Cas Subtype Cyano protein 3, as it is often the third gene upstream of the core cas genes, cas3-cas4-cas1-cas2
KGDQSLANHILNGLLTLWNLERRLQQLDFPVRLNVKERRLVIAGFTLHDYHKHCHADDMPNDEFDLNIQE
IIPIILALGKRLGLDEFWAPETPEDWRDYIAEISFLAQNVHGKQHTNLNHSTAGYNFTLKERTLRPLRHL
LLLADSAASLSSPHDAVSSTMKDRLRFLLNRGGFELRYHHLRETTGVLSNVVHNAVLETVQKLDYKPLLF
FAQGVIYLAPQDTEIPETNEIKQIVVQGISQELGKKISASHVGFKRDGKGLKSSEETSFFYAGAGIVRIA
PQAISVKVNNAKSSATDKRTESLELLDADLEKKYEVADLRIDRLAELGGLVQKSIFVETVNRIEDIRKKD
KKLLPEPFIPLTRKVAEFWNLTAFVLKDLELQSVVEMPEENQVQGNSGGVWYYWYAIAAHYLDRHPGIES
VTWDIQEVIEYLQGLGDRLASQSAEEEGYFAAHLSPTRQIFLDYLDEYLSIQGWELHQTFIAELNNYNAY
AKTKRGKQPICSLSSGEFPSEEQMDSVVLFLPQQYSNKNPLGGSQIKRGISSIWSIEMLLRQIFWSVRSG
KFEDGQPIYFYLYPDYVFTPQTVEAISELVNGIASVRFDGDVRKHWVNLAMDFSLESLPWQSVDAFLLNE
EVERGTNAQLKLSYPFDQNLTFLFVVYFTTRDNTDTEAWFFPSFLALLLPYLLGVKVVASESPIPLMRSG
QEFRESVHLDGAPHFWVLLGIPDRLRLEDITPALNKLLAIYTLHLAIRSSPPKANWQDFPKTLQTFRTDP
LPVFALLKQGVRRQDRERPYISEVTEYAYHFYPCWDFYELFSQGNIVLTEKLENSLLTKRLVELYRRFYR
VALSKNPKPHAVLKPFREAVEAILSKPGSQWDEEDLVLQVSGRLQKMIDRQEVYTGDSVAYETRQLQELE
AIQIFATYFVDEIFYEMAKGDRAILKRQRNNLADGFAEFTYRL
>gnl|CDD|274470 TIGR03175, AllD, ureidoglycolate dehydrogenase. This enzyme converts ureidoglycolate to oxalureate in the non-urea-forming catabolism of allantoin (GenProp0687). The pathway has been characterized in E. coli and is observed in the genomes of Entercoccus faecalis and Bacillus licheniformis
MKVSRETLHQLIKQKLEKAGLKREHAAEVADVLTFADARGIHSHGAVRVEYYAERIAKGGITREPEFRFE
KTGPCTAIFHGDNGAGQVAAKMAMEHAIELAKESGVAVVGISRMSHSGALSYFVKQAAEQGMVALSMCQS
DPMVVPFGGTEIYFGTNPIAFAAPSAGDEIITFDMATTVQAWGKVLDARSRNESIPDTWAVDKNGAPTTD
PFAVHALLPIAGPKGYGLMMMVDVLSGSLLGLPFGRHVSSMYADLTAGRNLGQLHLVINPAFFTDSELFK
QHISQMMEELNAVPPAEGFQQVYYPGEDGDLKQQKADSEGIEIVDDIYQYLVSDAVHYDSYEGKNPFAQ
>gnl|CDD|274471 TIGR03176, AllC, allantoate amidohydrolase. This enzyme catalyzes the breakdown of allantoate, first to ureidoglycine by hydrolysis and then decarboxylation of one of the two equivalent ureido groups. Ureidoglycine then spontaneously exchanges ammonia for water resulting in ureidoglycolate. This enzyme is an alternative to allantoicase (3.5.3.4) which releases urea [Central intermediary metabolism, Nitrogen metabolism]
MIKHFRQAIEELSSFGADPAGGMTRLLYSPEWLAAQQQFKKRMAESGLETRFDDVGNLYGRLVGTEFPEE
TILTGSHIDTVVNGGNLDGQFGALAAWLAVDYLKEKYGAPLRTVEVLSMAEEEGSRFPYVFWGSKNIFGL
AKPEDVRTIEDAKGIKFVDAMHACGFDLRKAPTVRDDIKAFVELHIEQGCVLESEGQSIGVVNAIVGQRR
YTVNLKGEANHAGTTPMSYRRDTVYAFSRICTQSIERAKEIGDPLVLTFGKVEPVPNTVNVVPGETTFTI
DCRHTDAAVLRNFTKELENDMKAIADEMDITIDIDLWMDEAPVPMNKEIVAIIEQLAKAEKLNYRLMHSG
AGHDAQIFAPRVPTAMIFVPSIGGISHNPAERTNIEDLVEGVKTLADMLYELAYKK
>gnl|CDD|274472 TIGR03177, pilus_cpaB, Flp pilus assembly protein CpaB. Members of this protein family are the CpaB protein of Flp-type pilus assembly. Similar proteins include the FlgA protein of bacterial flagellum biosynthesis
VLAIALVLGGLAALLARRWLSPQQPVAAVAEKVPTVPVVVAARDLPAGTPITAEDLRWVLWPEASVPAGA
FDDIAQLVGRVVRRPLEAGEPILAAKLAPPGASGGLAALIPPGMRAVAIRVDEVTGVGGFILPGDRVDVL
LTRRDDGSRPNDRAVSKTVLQNIRVLAVDQTTQEGEDGKPKVVRTVTLEVTPEQAEKLALARQVGTLSLA
LRNAADTDEPEATAVLAATLSLAPQVAKAVDVAAARRAAVEVIRGGQVSEV
>gnl|CDD|163175 TIGR03178, allantoinase, allantoinase. This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases
DLIIRGGRVILPNGEREADVGVKGGKIAAIGPDILGPAAKIIDAGGLVVFPGVVDTHVHINEPGRTEWEG
FETGTRAAAAGGITTYIDMPLNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYNLDDLRELDEAGV
VGFKAFLSPSGDDEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRP
VFAEVEAIRRTLALAKVTGCRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGTLAK
CAPPIRDLANQEGLWEALLNGLIDCVVSDHSPCTPDLKRAGDFFKAWGGIAGLQSTLDVMFDEAVQKRGL
PLEDIARLMATNPAKRFGLAQKGRIAPGKDADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRAT
YLRGQCIYDDEQFIGAPKGQLLL
>gnl|CDD|188295 TIGR03180, UraD_2, OHCU decarboxylase. Previously thought to only proceed spontaneously, the decarboxylation of 2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) has been recently been shown to be catalyzed by this enzyme in Mus musculus. Homologs of this enzyme are found adjacent to and fused with uricase in a number of prokaryotes and are represented by this model. This model is a separate (but related) clade from that represented by TIGR3164. This model places a second homolog in streptomyces species which (are not in the vicinity of other urate catabolism associated genes) below the trusted cutoff
FNSLSKDEASATLAPCCAIPAWAETLVAARPFASREALLAAADQAMANLSEDDLNEALAGHPRIGEKPAG
QAAHAATSRREQAGVDGADEETRAALLEGNAAYEEKFGRIFLIRAAGRSAEEMLDALQARLQNDPEEELR
IAAEQLREITRLRLSRLI
>gnl|CDD|213783 TIGR03181, PDH_E1_alph_x, pyruvate dehydrogenase E1 component, alpha subunit. Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc [Energy metabolism, Pyruvate dehydrogenase]
ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSAL
ALRKDDWVFPSYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKL
RGEDNVAVTYFGDGGTSEGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPG
VQVDGNDVLAVYAVTKEAVERARSGGGPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKDPILRLRK
YLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPPVDDIFDHVYAELPPELEEQRAEL
>gnl|CDD|274473 TIGR03182, Pyruvate_dehydrogenase_E1_component_subunit_alpha, pyruvate dehydrogenase E1 component, alpha subunit. Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc [Energy metabolism, Pyruvate dehydrogenase]
KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALAR
GVPPKEVMAELTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFG
DGAANQGQFYESFNMAALWKLPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVR
EAAKEAVERARSGKGPILLEMKTYRFRGHSMSDPAKYRSKEEVEEWRKRDPIEKLKARLIEQGIASEEEL
KEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA
>gnl|CDD|163177 TIGR03183, DNA_S_dndC, putative sulfurtransferase DndC. Members of this protein family are the DndC protein from the dnd (degradation during electrophoresis) operon. The dnd phenotype reflects a sulfur-containing modification to DNA. This operon is sparsely and sporadically distributed among bactera; among the first eight examples are members from the Actinobacteria, Firmicutes, Gammaproteobacteria, Cyanobacteria. DndC is suggested to be a sulfurtransferase [DNA metabolism, Restriction/modification]
LIEEIQELYLSDDIPWVVGYSGGKDSTAVLQLIWNALAALPAEQRTKKIHVISTDTLVENPIVAAWVNAS
LERMQEAAQDQGLPIEPHRLTPEIKDTFWVNLIGKGYPAPRQKFRWCTDRLKISPSNTFIRDVVAANGEV
ILVLGTRKAESQARAAVMEKHESGSLRDRLSRNSSLPNSWVYSPIEDWSNDDVWMYLLQVPNPWGIDNKD
LFGMYQGATADGECPLVVDTSTPSCGDSRFGCWVCTMVSEDKSMNAMIQNDSEKEWMKPLLDFRNKLDGI
ENDRDKRDFRRMNGRVQLHEDKKDGKTDAELIPGPYLQSYREQWLKELLEAQLTIRNLAPEEVRDIELIS
LEELREIRRIWLEEKHEWEDSLPKIYQEVTGEDFPGWPGADHPLLGSDEIDVLEEICAGDGLHYELVRKL
LSTERQYRGMSRRAGLFDELEQVLKKS
>gnl|CDD|274474 TIGR03184, putative_phosphoribosylaminoimidazole, DNA sulfur modification protein DndE. This model describes the DndE protein encoded by an operon associated with a sulfur-containing modification to DNA. The operon is sporadically distributed in bacteria, much like some restriction enzyme operons. DndE is a putative carboxylase homologous to NCAIR synthetases [DNA metabolism, Restriction/modification]
IRLSQTAKDQLRRLKRRTGLTPWNILCRWAFCLSLEEGSTPGVADIKLDGGLEIDWYTFAGEYGDIYLAL
LKQRCVADGPELDDESLAKALNLHVHRGIGYLSGR
>gnl|CDD|274475 TIGR03185, DNA_S_dndD, DNA sulfur modification protein DndD. This model describes the DndB protein encoded by an operon associated with a sulfur-containing modification to DNA. The operon is sporadically distributed in bacteria, much like some restriction enzyme operons. DndD is described as a putative ATPase. The small number of examples known so far include species from among the Firmicutes, Actinomycetes, Proteobacteria, and Cyanobacteria [DNA metabolism, Restriction/modification]
MIILQLTLENFGPYRGRQTFDLSPSSPKPIILIGGLNGAGKTTLLDAIQLALYGKRALCSGRGNKSYEQY
LRGLINRQAGKTNPASITLTFSVVEGGKRHEYTLVRSWHINNKDVKEKLTVYKDDEEDDSLNDIWDEFIN
ELLPLELADLFFFDGEKIEALANPDRLASLLKEAIEVLLGLDLIDRLAGDLTNVLRRRKKSELPSSILSE
IEALEAELKEQSEKYEDLAQEIAHLRNELEEAQRSLESLEKKFRSEGGDLFEEREQLERQLKEIEAARKA
NRAQLRELAADPLPLLLIPNLLDSTKAQLQKEEQSQQNQLTQEELEERDKELLESLPKLALPAEHVKEIA
AELAEIDKPATTDSEIPHRLSGSELTQLEVLIQQVKRELQDAKSQLLKELRELEEELAEVDKKISTIPSE
EQIAQLLEELGEAQNELFRSEAEIEELLRQLETLKEAIEALRKTLDEKTKQKINAFELERAITIADKAKK
TLKEFREKLLERKLQQLEEEITKSFKKLMRKHNLISRLKIDPETFAVSLYDNNGKHIDKERLSAGERQIL
AIALLWGLAKVSGRRLPVIIDTPLGRLDSSHRENLVVNYFPKASHQVLLLSTDEEVDEKHYNLLKPNISH
EYLLEFDDEARTSVVTEGYF
>gnl|CDD|132230 TIGR03186, alpha-ketobutyrate_dehydrogenase_E1, alpha-ketoglutarate dehydrogenase. Several bacterial species have a paralog to homodimeric form of the pyruvate dehydrogenase E1 component (see model TIGR00759), often encoded next to L-methionine gamma-lyase gene (mdeA). The member from a strain of Pseudomonas putida was shown to act on alpha-ketobutyrate, which is produced by MdeA.This model serves as an exception model to TIGR00759, as other proteins hitting TIGR00759 should be identified as the pyruvate dehydrogenase E1 component
RRHDDTDPQETAEWLDALDGVVAHAGAERAQYLLAQLAAHAARLGLAPPAAGATPYVNTIAVDQEPPYPG
DLQLEERLAAILRWNALAMVVRANRAYGELGGHIASYASAADLFEVGFNHFFRAAGDASGGDLVYFQPHS
APGVYARAFLEGFLSDAQLAHYRQEIAGPGLCSYPHPWLMPDFWQFPTGSMGIGPINAIYQARFMRYLQN
RGLARTEGRKVWGFFGDGEMDEPESIGALSLAARERLDNLVFVINCNLQRLDGPVRGNGRIIDELESQFA
GAGWNVIKVLWGSDWDALFARDATGALARAFAHTVDGQFQTFSANDGAYNRARFFGQDPALAALVAHLSD
EDIDRLRRGGHDARKLYAAYDRAVRHEGRPTVILAKTMKGFGMGAIGQGRMTTHQQKKLDVEALLAFRDR
FRLPLSDADVEQLKFYKPDEDSAEMRYLHARRAALGGYLPRRRTAATHALAVPALPSWGRFALDAEGKEM
STTMAIVRMLGALLKDAELGPRIVPIVADEARTFGMANLFRQVGIYSPLGQRYEPEDLGSMLYYREDTDG
QILEEGISEAGAISSWIAAATSYSVHDLPMLPFYIYYSMFGFQRIGDLIWAAADQRARGFLIGATSGKTT
LGGEGLQHQDGTSHLAASTVPNCRAWDPAFAYEVAVIVDEGMREMLERQRDEFYYLTVTNENYAQPSLPE
DRLDAVRRGILKGMYPLDPAALAAARVQLLGSGAILGEVQAAARLLRDDWGIDAAVWSVTSFTELARDGR
AAERAQRLGDAERPPSPHVAQALGATQGPVIAATDYVRAVPELIRAYVPRRYVTLGTDGFGRSDTRAALR
AFFEVDRASIVIAALQALADDGLVARDVVRQAIARYGKAATSRAPPWER
>gnl|CDD|274476 TIGR03187, hypothetical_protein, DGQHR domain. This highly divergent, uncharacterized domain has several absolutely conserved residues, including a QR pair and FxxxN motif. Its most striking feature, however, is a near invariant pentapeptide motif DGQHR. Several different subfamilies occur specifically as a part of DNA phosphorothioation systems, previously called DND (DNA instability during electrophoresis), while others (e.g. CPS_2936) occur in other contexts suggestive of lateral gene transfer (sporadic distribution of helicase-containing cassettes). The region described by this model is about 280 amino acids in length; additional sequences show local sequence similarity
AIRGVQGGREFYVFMVPAEVLAKIFYFDRRDEPTLLGYQRPLNKSRIKEIARYIENPDAYFPPAITLSID
GSVEFEPDEGKGRGVGTLEIPMDASAWIVDGQHRLAAIEDALKESPELAETIPVVFFIDLGLEEQQQIFA
DINLNAPKPKSLLYDLYDHRDPLARLARELNEDPSSPLFGGIVRLEKSTLSANSIKLITLSALVDAVLRL
LGKPAGVKDENDEEIAQILNNFWTAVAEVFPEAWLKVPRKEDSILTHGVGIQALGLLGRELL
>gnl|CDD|274477 TIGR03188, Phosphoribosyl-ATP_pyrophosphatase, phosphoribosyl-ATP pyrophosphohydrolase. This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, catalyses the second step in the histidine biosynthesis pathway. It often occurs as a fusion protein. This model a somewhat narrower scope than pfam01503, as some paralogs that appear to be functionally distinct are excluded from this model [Amino acid biosynthesis, Histidine family]
LEELEATIAERKAADPEGSYTARLFAKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLL
AAQGVSLEDVLAEL
>gnl|CDD|132233 TIGR03189, Cyclohexa-15-dienecarbonyl-CoA_hydratase, cyclohexa-1,5-dienecarbonyl-CoA hydratase. This enzyme, cyclohexa-1,5-dienecarbonyl-CoA hydratase, also called dienoyl-CoA hydratase, acts on the product of benzoyl-CoA reductase (EC 1.3.99.15). Benzoyl-CoA is a common intermediate in the degradation of many aromatic compounds, and this enzyme is part of an anaerobic pathway for dearomatization and degradation
LKVWLERDGKLLRLRLARPKANIVDAAMIAALSAALGEHLEDSALRAVLLDAEGPHFSFGASVAEHMPDQ
CAAMLASLHKLVIAMLDSPVPILVAVRGQCLGGGLEVAAAGNLMFAAPDAKLGQPEIVLGVFAPAASCLL
PERMGRVAAEDLLYSGRSIDGAEGARIGLANAVAEDPENAALAWFDEHPAKLSASSLRFAVRAARLGMNE
RVKAKIAEVEALYLEELMATHDAVEGLNAFLEKRPALWEDR
>gnl|CDD|132234 TIGR03190, benz_CoA_bzdN, benzoyl-CoA reductase, bzd-type, N subunit. Members of this family are the N subunit of one of two related types of four-subunit ATP-dependent benzoyl-CoA reductase. This enzyme system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for a number of different aromatic compounds, such as phenol and toluene
DGLFDQFKTWYEKRHDYARDWKARTGGQVVATMCTYTPEELLIAAGMLPVRVLGAHEPQNVTEPHIFGMF
CPFCRDSLAQGLLGRFDYAEGVTLTQSCIQYRQTFGSWRQHVPTVKWDYYVPMPNEVQSPHARKAHYAEV
QRFRVFLQTLTGKEITDDMLRDALAVCDENRRLLRELFDYRKEADPKVTGVEALYASLTAQFIDKREHNE
MLKKVLAALPSRKVERKTGARFMTIGSENDDIAFMAMVESVGATIVIDDQCSGTRYFWNASKPEDDVIKA
IAERYCDRPACPTKDYPVHTRYDHVLGLAKEYNVQGAIFLQQKFCDPHEGDYPDLKRHLEANGIPTLFLE
FDITNPIGPFRIRIEAFLETLSEEELF
>gnl|CDD|132235 TIGR03191, benz_CoA_bzdO, benzoyl-CoA reductase, bzd-type, O subunit. Members of this family are the O subunit of one of two related types of four-subunit ATP-dependent benzoyl-CoA reductase. This enzyme system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for a number of different aromatic compounds, such as phenol and toluene
YPTEPLKLWGKAKQLREQYYQNFARAKDKGGIRWSAAAWAFDAIPAGLGDDVYPLTGEPYAAAVAHDRKF
AKECLDAAEAYGFARDLCSYMRIYWGGMHLDEYAFGGEFPKPDFIFQTQICCSHAKWYQHVAKEEKIPDF
YLDVGVGAYKDLTDARLDYVANQLHDGIEFVEKASGRKCDDELFIKAIKNEMRSTARWADICALNKAKPA
PLDEKTMYSLYVLAILHKSSQWCADFMDELYEEVKDRVARGIAAVPNERCRLMSDTQPPWPFLKIFRYLE
TYGAVSIGSLYTFALEGIWEDKEDGSWGARTLPWEKGIEINDRATALRLYADWNLSKPLWQHFFDPRIKS
EMMLNIARDWNVDGCMLHLNRGCEGLSIGIMENRLAIAKAGIPIMTFEGNMGDEREFDEVRTQARVDAFM
EQLGLRRLAA
>gnl|CDD|132236 TIGR03192, benz_CoA_bzdQ, benzoyl-CoA reductase, bzd-type, Q subunit. Members of this family are the Q subunit of one of two related types of four-subunit ATP-dependent benzoyl-CoA reductase. This enzyme system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for a number of different aromatic compounds, such as phenol and toluene
AAAAAAPEKKEFWRWQENTVFDENKDWKDAKIITCGIDVGSVSSQAVLVCDGELYGYNSMRTGNNSPDSA
KNALQGIMDKIGMKLEDINYVVGTGYGRVNVPFAHKAITEIACHARGANYMGGNAVRTILDMGGQDCKAI
HCDEKGKVTNFLMNDKCAAGTGRGMEVISDLMQIPIADLGPRSFDVETEPEAVSSICVVFAKSEALGLLK
AGYTKNMVIAAYCQAMAERVVSLLERIGVEEGFFITGGIAKNPGVVKRIERILGIKAVDTKIDSQIAGAL
GAALFGYTLMQKQ
>gnl|CDD|132237 TIGR03193, 4-hydroxybenzoyl-CoA_reductase_subunit_gamma, 4-hydroxybenzoyl-CoA reductase, gamma subunit. 4-hydroxybenzoyl-CoA reductase converts 4-hydroxybenzoyl-CoA to benzoyl-CoA, a common intermediate in the degradation of aromatic compounds. This protein family represents the gamma chain of this three-subunit enzyme
LLRLTVNGRWREDAVADNMLLVDYLRDTVGLTGTKQGCDGGECGACTVLVDGRPRLACSTLAHRVAGRKV
ETVEGLATNGRLSRLQQAFHERLGTQCGFCTPGMIMAAEALLRRNPSPSRDEIRAALAGNLCRCTGYVKI
IESVEAAA
>gnl|CDD|132238 TIGR03194, 4-hydroxybenzoyl-CoA_reductase_subunit_alpha, 4-hydroxybenzoyl-CoA reductase, alpha subunit. This model represents the largest chain, alpha, of the enzyme 4-hydroxybenzoyl-CoA reductase. In species capable of degrading various aromatic compounds by way of benzoyl-CoA, this enzyme can convert 4-hydroxybenzoyl-CoA to benzoyl-CoA
VPLVDGVEKVTGKAKYTADLAAPGALVGRILRSPHAHARILAIDTSEAEALPGVIAVVTGADCPVPYGVL
PIAENEYPLARDKVRYRGDPVAAVAAVDEVTAEKALALIKVEYEELPAYMDPKAAMKAGAILLHDNKPGN
IEREVHNEFGDVAAAFAEADLIREKTFTCAEVNHAHMEPNATLAEYDPVRGMLTLNSVTQVPYYVHLKLA
RCLQMDSARIRVIKPFLGGGFGARVEPLNFEIIAGLLARKAKGTVRLLQTREETFITHRGRPQTYVKMKI
GLKKDGKITACAAEVVQRGGAYAGYGIVTILYAGALLHGLYDIPAVKYDGYRVYTNTPPCGAMRGHGTVD
TRAAFESLLDEMAAELGIDPFAIRRRNLLQAPTVTMNDLRVMSYGLPECLEKVEQASGWEERKGRLPKGR
GLGIACSHFVSGSAKPIHFTGEPHATVALKLDFDGGITLLTGAADIGQGSSTIASQVAAEVLGVRLSRIR
VISADSALTPKDNGSYSSRVTFMVGNAAIDAAEELKGVLVAAAAKKLDAREEDIECAGEMFFVSGSADPG
LSFQEVVKAALVDSGTITVKGTYTCPPEFQGGKKRGGAVGSTMGFSYAAQVVEVSVDEETGKVTVHKVWV
AVDCGKAINPLAVEGQVQGAVWMGMGQALSEETVYDNGRMKHASLLDYRVPTIVESPDIEVIIVESMDPN
GPFGAKEASEGALAGFLPAIHNAVYDAVGVRATDLPLTPDRVTEAL
>gnl|CDD|132239 TIGR03195, 4-hydroxybenzoyl-CoA_reductase_subunit_beta, 4-hydroxybenzoyl-CoA reductase, beta subunit. This model represents the second largest chain, beta, of the enzyme 4-hydroxybenzoyl-CoA reductase. In species capable of degrading various aromatic compounds by way of benzoyl-CoA, this enzyme can convert 4-hydroxybenzoyl-CoA to benzoyl-CoA
ALTDFRTLRPASLADAVAALAAHPAARPLAGGTDLLPNLRRGLGQPETLVDLTGIDEIAQLSTLADGLRI
GAGVTLAALAEDALVRTRWPALAQAARAVAGPTHRAAATLGGNLCLDTRCIYYNQSEWWRSGNGYCLKYR
GDKCHVAPKSDRCYAAFSGDVAPALLVLDAEAEIVGPAGVRRVPLAELYVEDGAAHLTLEPGEVLAAVRV
PPTGGWTSAYSKVRVRGAIDFPLAGVAVALQRDGDRIAGLRVALTGTNSRPLMVPGTDALAGRPLDDAAA
EEIARLVRKTSQPMRTTLMGVKYRRRVLLAIARRLVDQLWN
>gnl|CDD|132240 TIGR03196, pucD, xanthine dehydrogenase D subunit. This gene has been characterized in B. subtilis as the molybdopterin binding-subunit of xanthine dehydrogenase (pucD), acting in conjunction with pucC, the FAD-binding subunit and pucE, the FeS-binding subunit. The more common XDH complex (GenProp0640) includes the xdhB gene which is related to pucD. It appears that most of the relatives of pucD outside of this narrow clade are involved in other processes as they are found in unrelated genomic contexts, contain the more common XDH complex and/or do not appear to process purines to allantoin
LGIGKPSRVRPDGPDKVTGEFKYMGDLRFPGMLHAKTLRSAHAHAEIRRVCTDAAEKLEGVQAMVTAADV
PGLARFGIIIADQPVFAADEIRYAGDAIAAVAAEDEEIAEAALAAIEVDYEELAPMDDPDKALQPDAEPL
HEAGNILHEAEFRHGDPDEGFAAGDTVFEDQYELGMQDHAFLAPEAALAMPAADGGFDLRAATQHGHKDR
EQIAACFDIPEEKIRITLAGMGGAFGGKDDLNIQIHAALLALASGLPVKIAQDRKESFLGGIHRHPAKIT
FKHGADADGNLLAHDAKIVADGGAYASLGPAVLAFAVEHAAGPYRIPNAHLEGISVFTNNGPAGAFRGFG
GNQITFAHEAHLDRLADALGIDPLDLRRKNARKPGDLGPLEHRIAAPDGAAEVIEAIASRPLPKAPILKK
ANRAVTALPGGRPAAAECGRLQRGTGAAIAMHGGGFGEGMDDAAVAGARLELAEDGTVKIRAHFACAECG
QGFLAAAEQIAMEELGCAAEDISIAIADTAKGPKAGSSSASRGTSMSGGAIQGACAAFAAQLKARAAETA
GLPAEVVEAPAENLIPGAAEIVGDKNEAALRVPLAEAAADGPIAAETAFHDFPTSALDADVGQGDGHFAF
AAAAAAAEVDVDLDLGDVKLIDCAHAIAAGPVLNPLALRGQIEGGAAMALGLALMEEAKMTDGRVAAENF
DDYLIPGIADVPDLDFIAIEDLMKDAPYGPKGVGEAGTCAATPAIIAAIHDAVGCDINKLPIRPEDLL
>gnl|CDD|274478 TIGR03197, MnmC_Cterm, tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain. In Escherichia coli, the protein previously designated YfcK is now identified as the bifunctional enzyme MnmC. It acts, following the action of the heterotetramer of GidA and MnmE, in the modification of U-34 of certain tRNA to 5-methylaminomethyl-2-thiouridine (mnm5s2U). In other bacterial, the corresponding proteins are usually but always found as a single polypeptide chain, but occasionally as the product of tandem genes. This model represents the C-terminal region of the multifunctional protein [Protein synthesis, tRNA and rRNA base modification]
TAYSLARRGWQVTLYEQDEAPAQGASGNPQGALYPLLSADDNPLSRFFLAAFLYARRFYRQLAEAGFPFD
HEWCGVLQLAYDEKEAERLQKLLEQLGFPEELARWVDAEQASQLAGIPLPYGGLFFPQGGWLSPPQLCRA
LLAHAGIRLTLHFNTEITSLERDGEGWQLLDANGEVIAASVVVLANGAQAPQLAQTAHLPLRPVRGQVSH
LPATEALSALKTVLCYDGYLTPANNGEHCIGASYDRNDDDLALREADHAENLERLAECLPALAWASEVDI
SALQGRVGVRCASPDHLPLVGAVPDFEAIKEAYAELAKDKNRPIAEPAPYYPGLYVLGGLGSRGLTSAPL
AAEILAAQICGEPLPLERDLLHALHPARFLI
>gnl|CDD|132242 TIGR03198, pucE, xanthine dehydrogenase E subunit. This gene has been characterized in B. subtilis as the Iron-sulfur cluster binding-subunit of xanthine dehydrogenase (pucE), acting in conjunction with pucC, the FAD-binding subunit and pucD, the molybdopterin binding subunit. The more common XDH complex (GenProp0640) includes the xdhA gene as the Fe-S cluster binding component
KEQFRFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGH
EITTIEGIAENELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRETPQPSDEDMEEGLSGNLCRCTGYGG
IIRSACRIRRG
>gnl|CDD|274479 TIGR03199, pucC, xanthine dehydrogenase C subunit. This gene has been characterized in B. subtilis as the FAD binding-subunit of xanthine dehydrogenase (pucC), acting in conjunction with pucD, the molybdopterin-binding subunit and pucE, the FeS-binding subunit
PAALDEAWSLLEKAPDSTFVSGSTLLQLQWEKGTLPMKQHLVSLEGIDELKGISTSDTHVSIGALTTLNE
CRKNPLIKRALPCFVDAASAIAAPGVRNRATIGGNIASGIGDFIPALLVLGAELIVYQKELIRLPLGAWL
SEEDFKPTAIVTRVIIGPRAETGEFVFYHKVGRRETFTGSLVVVAGRFLLDGSQTIKEIRLAVGGADITP
RRLLDSEAKLMAPPWDPHLLAELYKTIIQELPFSSDPFATAAYRKKVAANVIVS
>gnl|CDD|132244 TIGR03200, 6-oxocyclohex-1-ene-1-carbonyl-CoA_hydratase, 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase. Members of this protein family are 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase, a ring-hydrolyzing enzyme in the anaerobic metabolism of aromatic enzymes by way of benzoyl-CoA, as seen in Thauera aromatica, Geobacter metallireducens, and Azoarcus sp. Note that Rhodopseudomonas palustris uses a different pathway to perform a similar degradation of benzoyl-CoA to 3-hydroxpimelyl-CoA
LNDHNLVGEHPETVCPGVLYEKRPAKRPDGNVVPGLYNAWIILDNPKQYNSYTTDMVKAIILAFRRASSD
RDVVAVVFTAVGDKAFCTGGNTKEYAEYYAGNPQEYRQYMRLFNDMVSAILGCDKPVICRVNGMRIGGGQ
EIGMAADFTIAQDLANFGQAGPKHGSAPIGGATDFLPLMIGCEQAMVSGTLCEPWSAHKAKRLGIIMDVV
PALKVDGKFVANPLVVTDRYLDEFGRIVHGEFKAGDELKAGKELIKQGTIDLSLLDEAVEALCAKLLNTF
PECLTKSIEELRKPKLFAWNQNKENSRAWLALNMMNEARTGFRAFNEGKKETGREIDFVKLRQALAKGHP
WTPELIESLM
>gnl|CDD|132245 TIGR03201, 6-hydroxycylohex-1-en-1-carbonyl-CoA_dehydrogenase, 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase. Members of this protein family are 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase, an enzyme in the anaerobic metabolism of aromatic enzymes by way of benzoyl-CoA, as seen in Thauera aromatica, Geobacter metallireducens, and Azoarcus sp. The experimentally characterized form from T. aromatica uses only NAD+, not NADP+. Note that Rhodopseudomonas palustris uses a different pathway to perform a similar degradation of benzoyl-CoA to 3-hydroxpimelyl-CoA
RWMMTEPGKPMVKTRVEIPELGAGDVVVKVAGCGVCHTDLSYYYMGVRTNHALPLALGHEISGRVIQAGA
GAASWIGKAVIVPAVIPCGECELCKTGRGTICRAQKMPGNDMQGGFASHIVVPAKGLCVVDEARLAAAGL
PLEHVSVVADAVTTPYQAAVQAGLKKGDLVIVIGAGGVGGYMVQTAKAMGAAVVAIDIDPEKLEMMKGFG
ADLTLNPKDKSAREVKKLIKAFAKARGLRSTGWKIFECSGSKPGQESALSLLSHGGTLVVVGYTMAKTEY
RLSNLMAFHARALGNWGCPPDRYPAALDLVLDGKIQLGPFVERRPLDQIEHVFAAAHHHKLKRRAILTP
>gnl|CDD|132246 TIGR03202, pucB, xanthine dehydrogenase accessory protein pucB. In Bacillus subtilis the expression of this protein, located in an operon with the structural subunits of xanthine dehydrogenase, has been found to be essential for XDH activity. Some members of this family appear to have a distant relationship to the MobA protein involved in molybdopterin biosynthesis, although this may be coincidental
IVAIYLAAGQSRRMGENKLALPLGETTLGSASLKTALSSRLSKVIVVIGEKYAHLSWLDPYLLADERIML
VCCRDACEGQAHSLKCGLRKAEAMGADAVVILLADQPFLTADVINALLALAKRRPDDYVAASFKGKPRPP
ILFSKSLFPKLKALKGDEGARALLRKDKSGLALPVADASAFFDIDTKEDY
>gnl|CDD|132247 TIGR03203, pimD_small, pimeloyl-CoA dehydrogenase, small subunit. Members of this protein family are the PimD proteins of species such as Rhodopseudomonas palustris, Bradyrhizobium japonicum. The pimFABCDE operon encodes proteins for the metabolism of straight chain dicarboxylates of seven to fourteen carbons. Especially relevant is pimeloyl-CoA, basis of the gene symbol, as it is a catabolite of benzoyl-CoA degradation, which occurs in Rhodopseudomonas palustris
DFDLSEEQRLLKESVEGLLKTSYDFDSRKKYQKEKGGWSKAVWGKLAEQGLLGLPFSEADGGFGAGSVET
MIVMEALGKALVLEPYLATVVIGGGFLRHAGSAAQKAAHLPGIIDGSKTFAFAQLEKNSRYDLGDVSTTA
KKTGDGWVIDGEKFVVLNGETADTLIVTARTKGARRDRTGIGVFLVPAGAKGVTIKGYPTQDGLHAADIT
FTGVVVGADAAIGDPENALPLIERVVDDARAALCAEAVGLMDESLKTTVEYIKTRKQFGVPIGSFQVLQH
RAADMFVAVEQARSMAMFATMASDFDDAKERANAIAAAKVQIGKSLKFVGQQSIQLHGGIGMTMEAKIGH
YFKRLTMIEHTFGDTDFHLSRVSAAGGL
>gnl|CDD|132248 TIGR03204, pimC_large, pimeloyl-CoA dehydrogenase, large subunit. Members of this protein family are the PimC proteins of species such as Rhodopseudomonas palustris and Bradyrhizobium japonicum. The pimFABCDE operon encodes proteins for the metabolism of straight chain dicarboxylates of seven to fourteen carbons. Especially relevant is pimeloyl-CoA, basis of the gene symbol, as it is a catabolite of benzoyl-CoA degradation, which occurs in Rhodopseudomonas palustris
DLAFSKEEQAFRDEVRSFFKDNVPADTRQKLVEGRHLTKDEMVTWWRILNKKGWGVSHWPKQYGGTGWTS
VQHYIFNEELQSAPAPQPLAFGVSMVGPVIYTFGNEEQKKRFLPRIANVDDWWCQGFSEPGSGSDLASLK
TKAEKKGDKWIINGQKTWTTLAQHADWIFCLCRTDPTAKKQMGISFILVDMKSKGITVRPIQTIDGGVEV
NEVFFDDVEVPYENLVGEENKGWDYAKFLLGNERTGIARVGVSKERIRRIKDLAAKVESGGKPVIEDAKF
REKLAAVEIELKALELTQLRVVADEGKHGKGKPNPASSVLKIKGSEIQQATTELLMEVIGPFAAPYDVHG
DDGSNEAMDWTAQIAPSYFNNRKVSIYGGSNEIQRNIIAKAVLGL
>gnl|CDD|132249 TIGR03205, pimA, dicarboxylate--CoA ligase PimA. PimA, a member of a large family of acyl-CoA ligases, is found in a characteristic operon pimFABCDE for the metabolism of pimelate and related compounds. It is found, so far, in Bradyrhizobium japonicum and several strains of Rhodopseudomonas palustris. PimA from R. palustris was shown to be active as a CoA ligase for C(7) to C(14) dicarboxylates and fatty acids
THPGEQFYPEGVRWDATIARGTLPDLLSKAAADYGPRPALEFRDRPITYTELEAMAETAAAALLRAGYGK
DASVALYLGNTPDHPINFFGALKAGARVVHLSPLDGERALSHKLSDSGARLLITSDLAALLPMALKFLEK
GLLDRLIVCEDDNWGKVGTPQAPIPADPRIVTYADFVKGAAAPAEWPAVTPDDVALLQYTGGTTGLPKGA
MLTHGNLTSAVSIYDVWGKPSRATRGDVERVICVLPLFHIYALTVILLRSLRRGDLISLHQRFDVAAVFR
DIEEKRATVFPGVPTMWIALANDPSLEKRDLSSLATIGSGGAPLPVEVANFFERKTGLKLKSGWGMTETC
SPGTGHPPEGPDKPGSIGLMLPGIELDVVSLDDPTKVLPPGEVGELRIRGPNVTRGYWNRPEESAEAFVG
DRFLTGDIGYMDTDGYFFLVDRKKDMIISGGFNVYPQMIEQAIYEHPGVQEVIVIGIPDQYRGEAAKAFV
KLRPGAKPFSLDELRAFLAGKLGKHELPVAVEFVDELPRTPVGKLSRHELR
>gnl|CDD|132250 TIGR03206, benzo_BadH, 2-hydroxycyclohexanecarboxyl-CoA dehydrogenase. Members of this protein family are the enzyme 2-hydroxycyclohexanecarboxyl-CoA dehydrogenase. The enzymatic properties were confirmed experimentally in Rhodopseudomonas palustris; the enzyme is homotetrameric, and not sensitive to oxygen. This enzyme is part of proposed pathway for degradation of benzoyl-CoA to 3-hydroxypimeloyl-CoA that differs from the analogous in Thauera aromatica. It also may occur in degradation of the non-aromatic compound cyclohexane-1-carboxylate
LKDKTAIVTGGGGGIGGATCRRFAEEGAKVAVFDLNREAAEKVAADIRAKGGNAQAFACDITDRDSVDTA
VAAAEQALGPVDVLVNNAGWDKFGPFTKTEPPLWERLIAINLTGALHMHHAVLPGMVERGAGRIVNIASD
AARVGSSGEAVYAACKGGLVAFSKTMAREHARHGITVNVVCPGPTDTALLDDICGGAENPEKLREAFTRA
IPLGRLGQPDDLPGAILFFSSDDASFITGQVLSVSGGLTM
>gnl|CDD|132251 TIGR03207, cyc_hxne_CoA_dh, cyclohexanecarboxyl-CoA dehydrogenase. Cyclohex-1-ene-1carboxyl-CoA is an intermediate in the anaerobic degradation of benzoyl-CoA derived from varioius aromatic compounds, in Rhodopseudomonas palustris but not Thauera aromatica. The aliphatic compound cyclohexanecarboxylate, can be converted to the same intermediate in two steps. The first step is its ligation to coenzyme A. The second is the action of this enzyme, cyclohexanecarboxyl-CoA dehydrogenase
LNEDLQALADTARRFARERIAPGFKERDKTRVLDRELMRDMGEMGFIGPELPEEHGGLGMGCLAAGVIHE
QIARADLSMSYVNLLASLNGQILAQHARPEIAKPWLGQLIAGEALFAIALTEPRGGSDAARLRLRAERDG
DDYVLNGEKTSISAADQADAAVVFARTGSEAEGARGISAFLVPMDLPGITRNRFDCHGQRAIGRGSIFFE
NVRVPADHMLGNEGQGFVQVMQGFDFSRALIGLQVLAVARAALDETWRYVAERQAFGKPLSAFQGVSHPL
ADAETQVEAARLLCLQTLWLKDHGLPHTSEAAMCKWWAPKLAYDVIHQCLLTHGHGGYDRGDMEQRLRDV
LGFQIGDGTAQIMKTIIARHRA
>gnl|CDD|132252 TIGR03208, cyc_hxne_CoA_lg, cyclohexanecarboxylate-CoA ligase. Members of this protein family are cyclohexanecarboxylate-CoA ligase. This enzyme prepares the aliphatic ring compound, cyclohexanecarboxylate, for dehydrogenation and then degradation by a pathway also used in benzoyl-CoA degradation in Rhodopseudomonas palustris
FDAVLLAPRRAASKAAGLWRDRTINDHFDAAVANCPDKPALTAYRDGHGAVRRFSYRELDCRVDRIAVGL
ARLGVGRGDVVSFQLPNRWEFTALYLACARIGAVLNPLMPIFRERELSFMLNHADSKVFVVPSVFRGFDH
AAMARELQSKLPALRQVVVIDGDGDDSFDRVLMTPERDDTPDAAAILAGPRPSPDDVTQLIYTSGTTGEP
KGVMHTANTLFSNIHPYAERLELGGGDVILMASPMAHQTGFMYGLMMPLILNATAVLQDIWNPARAAELI
RETGVTFTMASTPFLTDLCRAVKESGAPVPSLFTFLCAGAPIPGILVERAWELLGALIVSAWGMTENGAV
TVTEPDDALEKASTTDGRPLPGVEVKVIDANGAKLSQGETGRLLVRGCSNFGGYLKRPHLNSTDAEGWFD
TGDLAFQDAEGYIRINGRSKDVIIRGGENIPVVEIENLLYQHPAVAQVAIVAYPDERLGERACAVVVPKP
GCTLDFAAMVAFLKAQKVALQYIPERLEVVDALPATPAGKIQKFRLRE
>gnl|CDD|132253 TIGR03209, P-21_partial, clostridium toxin-associated regulator BotR. Clostridium botulinum neurotoxin production is regulated by a regulatory sigma-70 protein, BotR transcription regulator. Similarly, tetanus toxin production of Clostridium tetani is regulated by TetR which is a very close relative of BotR. Both BotR and TetR are members of the TIGR02937 subfamily of sigma-70 RNA polymerase sigma factors. Functional complementation experiments have been done for botR and tetR in highly transformable strain of Clostridium perfringens host cells to assess functional interchangeability of sigma factors and it has been confirmed that they are interchangeable in vivo
FEEIYMNFKNTIDIFTRKYNLYYDYNDILYHLWIILKKIDLNKFNTENDLEKYISTSLKRYCLDICNKKN
RDKKIIYNSEITDIKLSLINVYSSNDLEFEFNDLISILPNKQKKIIYMKFFEDMKEIDIAKKLHISRQSV
YK
>gnl|CDD|132254 TIGR03210, badI, 2-ketocyclohexanecarboxyl-CoA hydrolase. Members of this protein family are 2-ketocyclohexanecarboxyl-CoA hydrolase, a ring-opening enzyme that acts in catabolism of molecules such as benzoyl-CoA and cyclohexane carboxylate. It converts -ketocyclohexanecarboxyl-CoA to pimelyl-CoA. It is not sensitive to oxygen
YEDILYEKRNGIAWIMINRPAKMNAFRGQTCDELIHALKDAGYDRQIGVIVLAGAGDKAFCTGGDQSTHD
GGYDGRGTIGLPMEELHSAIRDVPKPVIARVQGYAIGGGNVLVTICDLTIASEKAQFGQVGPKVGSVDPG
YGTALLARVVGEKKAREIWYLCRRYTAQEALAMGLVNAVVPHDQLDAEVQKWCDEIVEKSPTAIAIAKRS
FNMDTAHQRGIAGMGMYALKLYYDTAESREGVKAFQEKRKPEFRKY
>gnl|CDD|274480 TIGR03211, catechol_2_3, catechol 2,3 dioxygenase. Members of this family all are enzymes active as catechol 2,3 dioxygenase (1.13.11.2), although some members have highly significant activity on catechol derivatives such as 3-methylcatechol, 3-chlorocatechol, and 4-chlorocatechol (see Mars, et al.). This enzyme is also called metapyrocatechase, as it performs a meta-cleavage (an extradiol ring cleavage), in contrast to the ortho-cleavage (intradiol ring cleavage)performed by catechol 1,2-dioxygenase (EC 1.13.11.1), also called pyrocatechase [Energy metabolism, Other]
GVMRLGHVELRVLDLEESLKHYTDVLGLEETGRDGQRVYLKAWDEWDHYSVILTEADTAGLDHMAFKVES
EADLERLVKRLEAYGVGTGWIPAGELPGVGRRVRFTLPSGHTMELYAEKEYVGELVGGLNPDPWPDPLRG
VGARRLDHCLLYGEDVAENTRFFTEVLGFRLTEQVVLGDGKEMAAAWLSVSNKAHDIAFVGDPEPGKLHH
VSFFLDSWEDVLKAADVMSKNDVSIDIGPTRHGITRGQTIYFFDPSGNRNETFAGGYLAYPDWPPITWTE
DELGRGIFYHGRVLNESFHTVGT
>gnl|CDD|211797 TIGR03212, uraD_N-term-dom, putative urate catabolism protein. This model represents a protein that is predominantly found just upstream of the UraD protein (OHCU decarboxylase) and in a number of instances as a N-terminal fusion with it. UraD itself catalyzes the last step in the catabolism of urate to allantoate. The function of this protein is presently unknown. It shows homology with the pfam01522 polysaccharide deacetylase domain family
YPRDLIGYGRNPPDARWPGGARIAVQFVLNYEEGGENCVLHGDAASEAFLSEIVGAAPWPGQRHMSMESL
YEYGSRAGFWRLLRLFTERGLPLTVFGVAMALARNPEAVAAMKEAGWEIASHGLRWIDYQDMDEAQEREH
IAEAIRLHTEVTGERPLGWYTGRTSPNTRRLVAEEGGFLYDSDSYADDLPYWDDGAGRPQLIVPYTLDAN
DMRFATPQGFNTGEQFFTYLKDAFDVLYAEGEGAPKMMSIGLHCRLVGRPGRIAALQRFLDYVQSHDKVW
VARRIDIARHWHATHPY
>gnl|CDD|132257 TIGR03213, Biphenyl-23-diol_12-dioxygenase_1, 2,3-dihydroxybiphenyl 1,2-dioxygenase. Members of this protein family all have activity as 2,3-dihydroxybiphenyl 1,2-dioxygenase, the third enzyme of a pathway for biphenyl degradation. Many of the extradiol ring-cleaving dioxygenases, to which these proteins belong, act on a range of related substrates. Note that some members of this family may be found operons for toluene or naphthalene degradation, where other activities of the same enzyme may be more significant; the trusted cutoff for this model is set relatively high to exclude most such instances [Energy metabolism, Other]
VRGLGYLGIGVSDVDAWREFATEVLGMMVASEGENDALYLRLDSRAHRIAVHPGESDDLAYAGWEVADEA
GLDQVKEKLEKAGVAVTVASAAEARERGVLGLIKFTDPGGNPLEIYYGAVEDFEKPFVSPRAVSGFVTGD
QGLGHIVLRVPDVDAALAFYTEVLGFQLSDVIDLPAGPGVTVRPYFLHCNERHHSLAFAAGPSEKRLNHL
MLEVDTLDDVGLALDRVDADGIVASTLGRHTNDHMVSFYVATPSGWLVEYGWGARVVERSYSVVEYDADS
IWGHKN
>gnl|CDD|200251 TIGR03214, ura-cupin, putative allantoin catabolism protein. This model represents a protein containing a tandem arrangement of cupin domains (N-terminal part of pfam07883 and C-terminal more distantly related to pfam00190). This protein is found in the vicinity of genes involved in the catabolism of allantoin, a breakdown product of urate and sometimes of urate iteslf. The distribution of pathway components in the genomes in which this family is observed suggests that the function is linked to the allantoate catabolism to glyoxylate pathway (GenProp0686) since it is sometimes found in genomes lacking any elements of the xanthine-to-allantoin pathways (e.g. in Enterococcus faecalis)
QKQLLTTRAIFTGNYAVITPDGLVSNIVPGFENTDIWILARPKLGFSATFVQYIVEVHPGGGATTGFGGE
GIETFLFVIDGEVNVSLGGETHELEEGGYAYLPPGSKWTLENAQDEDARFFLYKKRYQPVEGLHAPEAVV
GNERDIEPEAYEGMDDVWATTLLPKELAFDMNVHILSFEPGASHPYIETHVMEHGLYVLEGKGVYNLDND
WVPVEAGDYIWMGAYCPQACYAVGRGPFRYLLYKDVNRHPKL
>gnl|CDD|132259 TIGR03215, ac_ald_DH_ac, acetaldehyde dehydrogenase (acetylating). Members of this protein family are acetaldehyde dehydrogenase (acetylating), EC 1.2.1.10. This enzyme oxidizes acetaldehyde, using NAD(+), and attaches coenzyme A (CoA), yielding acetyl-CoA. It occurs as a late step in the meta-cleavage pathways of a variety of compounds, including catechol, biphenyl, toluene, salicylate, etc
KVKVAIIGSGNIGTDLMYKLLRSEHLEMVAMVGIDPESDGLARARELGVKTSAEGVDGLLANPDIDIVFD
ATSAKAHARHARLLAELGKIVIDLTPAAIGPYVVPAVNLDEHLDAPNVNMVTCGGQATIPIVAAISRVAP
VHYAEIVASIASRSAGPGTRANIDEFTETTSRALEQVGGAKKGKAIIILNPAEPPLMMRDTIYCLVEDPD
EDAIEASVEEMVAEVQKYVPGYRLKQEPQFDGLRVSVFLEVEGAGDYLPKYAGNLDIMTAAALAVAEMFA
QQLLG
>gnl|CDD|132260 TIGR03216, 2-hydroxymuconic_semialdehyde_dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase. Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation [Energy metabolism, Other]
IRNFINGAFVESGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAALKGPWGKMTVAERADLLYAVAD
EIERRFDDFLAAEVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTECFEMATPDGKGALNYAVRKPL
GVVGVISPWNLPLLLMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPDSA
GEFLTRHPGVDAITFTGETRTGSAIMKAAADGVKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTG
QVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDPATNMGPLISAEHRDKVLSYYALAVEEGATVVT
GGGVPDFGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFDSEEEVIALANDTPYGLAASVWTE
DLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNVCIKL
>gnl|CDD|274481 TIGR03217, 4-hydroxy-2-oxovalerate_aldolase, 4-hydroxy-2-oxovalerate aldolase. Members of this protein family are 4-hydroxy-2-oxovalerate aldolase, also called 4-hydroxy-2-ketovalerate aldolase and 2-oxo-4-hydroxypentanoate aldolase. This enzyme, part of the pathway for the meta-cleavage of catechol, produces pyruvate and acetaldehyde. Acetaldehyde is then converted by acetaldehyde dehydrogenase (acylating) (DmpF; EC 1.2.1.10) to acetyl-CoA. The two enzymes are tightly associated [Energy metabolism, Other]
KKLYITDVTLRDGMHAIRHQFTIEQVRAIAAALDEAGVDAIEVTHGDGLGGSSFNYGFSAHTDLEYIEAA
ADVVKRAKVAVLLLPGIGTVHDLKAAYDAGARTVRVATHCTEADVSEQHIGMARELGMDTVGFLMMSHMT
PPEKLAEQAKLMESYGADCVYIVDSAGAMLPDDVRDRVRALKAVLKPETQVGFHAHHNLSLAVANSIAAI
EAGATRIDASLRGLGAGAGNAPLEVFVAVLDRLGWNTGCDLFKLMDAAEDIVRPLMDRPVRVDRETLTLG
YAGVYSSFLLHAERAAAKYGVDARDILVELGRRKMVGGQEDMIVDVALDLAKA
>gnl|CDD|132262 TIGR03218, 4-oxalocrotonate_decarboxylase, 4-oxalocrotonate decarboxylase. Members of this protein family are 4-oxalocrotonate decarboxylase. Note that this protein, as characterized (indirectly) in Pseudomonas sp. strain CF600, was inactive except when coexpressed with DmpE, 2-oxopent-4-enoate hydratase, a homologous protein from the same operon. Both of these enzymes are active in the degradation of catechol, a common intermediate in the degradation of aromatic compounds such as benzoate, toluene, phenol, dimethylphenol (dmp), salicylate, etc [Energy metabolism, Other]
MNMTLNREQIEALAEHLENAELQAHDIPKITDEYPDMDWADAYAIQWEIRRRKEARGAKIVGLKAGLTSW
AKMKQMGVETPVFGFLVDYFSVPDGGEIKTSELIHPKVEAEIAFVTKAPLKGPGCHIGDVLAATDFVMPA
VEVIDSRYRDFKFDLKSVIADNTSSARFVTGGRAANVEDLDLRTLGVVMEKNGEVVAMGAGAAVLGHPAA
AVAMLANHLAERGEEIPAGSFIMSGGITEAVAVAPGDSVTVRYQGLGSVSMRF
>gnl|CDD|274482 TIGR03219, Salicylate_hydroxylase, salicylate 1-monooxygenase. Members of this protein family are salicylate 1-monooxygenase, also called salicylate hydroxylase. This enzyme converts salicylate to catechol, which is a common intermediate in the degradation of a number of aromatic compounds (phenol, toluene, benzoate, etc.). The gene for this protein may occur in catechol degradation genes, such as those of the meta-cleavage pathway
LRVAIIGGGIAGVALALNLCKHSHLNVQLFEAAPAFGEVGAGVSFGANAVRAIVGLGLGEAYTQVADSTP
APWQDIWFEWRNGSDASYLGATIAPGVGQSSVHRADFLDALLKHLPEGIASFGKRATQIEEQAEEVQVLF
TDGTEYRCDLLIGADGIKSALRDYVLQGQGQAPVRPRFSGTCAYRGLVDSLQLREAYRAAGLDEHLVDVP
QMYLGLDGHILTFPVRQGRLINVVAFISDRSQPKPTWPSDTPWVREATQREMLDAFAGWGDAARALLECI
PAPTLWALHDLAELPGYVHGRVALIGDAAHAMLPHQGAGAGQGLEDAYFLARLLGDTELEAGDLPALLEA
YDDVRRPRACRVQRTSREAGELYELRDPAVGADEELLGAHLATRFDWLWNHDLDQDLAEARAAL
>gnl|CDD|132264 TIGR03220, 2-hydroxypenta-24-dienoate_hydratase, 2-oxopent-4-enoate hydratase. Members of this protein family are 2-oxopent-4-enoate hydratase, which is also called 2-hydroxypent-2,4-dienoate hydratase. It is closely related to another gene found in the same operon, 4-oxalocrotonate decarboxylase, with which it interacts closely
LITQLGDELYQALVTRTPVAPLTSRGPDISIEDAYRIQQRMIARRLAAGERIIGKKIGVTSKAVMNMLGV
YQPDFGYLLDGMVYNEGEPIPTDTLIQPKAEGEIAFVLKKDLMGPGVTAADVLAATECVMPCFEIVDSRI
RDWKIKIQDTVADNASCGVFVLGDTRVDPRKLDLALCGMVLEKNGEIVSTGAGAAALGSPVNAVAWLANT
LGRLGIPLKAGEVILSGSLAALVPVKAGDNLRVSIGGIGSCSVRF
>gnl|CDD|213786 TIGR03221, muco_delta, muconolactone delta-isomerase. Members of this protein family are muconolactone delta-isomerase (EC 5.3.3.4), the CatC protein of the ortho cleavage pathway for metabolizing aromatic compounds by way of catechol [Energy metabolism, Other]
LFHVRMDVNLPVDMPAEKAAAIKAREKAYAQELQREGKWRHLWRVAGEYANYSIFDVESNDELHTLLSGL
PLFPYMDIEVTPLARHPSSI
>gnl|CDD|213787 TIGR03222, benzo_boxC, benzoyl-CoA-dihydrodiol lyase. In the presence of O2, the benzoyl-CoA oxygenase/reductase BoxBA BoxAB converts benzoyl-CoA to 2,3-dihydro-2,3-dihydroxybenzoyl-CoA. Members of this family, BoxC, homologous to enoyl-CoA hydratases/isomerases, hydrolyze this compound to 3,4-dehydroadipyl-CoA semialdehyde + HCOOH
VDFRTEPSQYRHWKLTFDGPVATLTMDVDEDGGLRPGYKLKLNSYDLGVDIELHDAVQRIRFEHPEVRTV
VMTSGKDRVFCSGANIFMLGLSTHAWKVNFCKFTNETRNGIEDSSRHSGLKFLAAVNGTCAGGGYELALA
CDEIMLVDDRSSSVSLPEVPLLGVLPGTGGLTRVTDKRRVRRDHADIFCTIEEGVRGKRAKEWRLVDEVV
KPSQFDAAIAERAAELAAQSDRPADAKGVQLTPLERTIDEDGVRYPTVDVAIDRAARTATITLKGPKAAQ
PADIAAIVAQGANWWPLKLARELDDAILHLRTNELDIGLWVFRTQGDAELVLAADALLEAHKDHWFVRET
IGYLRRTLARLDVSSRSLFALIEPGSCFAGTLAELAFAADRSYMLAFPDNNDPEPAITLSELNFGLYPMV
NGLSRLATRFYAEPAPVAAVRDKIGQALDAEEAERLGLVTAAPDDIDWEDEIRIALEERASFSPDALTGL
EANLRFAGPETMETRIFGRLTAWQNWIFNRPNAVGENGALKVYGSGKKAQFDMERV
>gnl|CDD|274483 TIGR03223, Phn_opern_protn, putative phosphonate metabolism protein. This family of proteins is observed in the vicinity of other caharacterized genes involved in the catabolism of phosphonates via the3 C-P lyase system (GenProp0232), its function is unknown. These proteins are members of the somewhat broader pfam06299 model "Protein of unknown function (DUF1045)" which contains proteins found in a different genomic context as well
MRYAIYYAPPRGSPLWRAGCRWLGRDAETGEELPHPPVPGFLAPDLAALTAAPRRYGFHATLKAPFRLAP
GVTEAELLAAVAAFAATRAPFALPPLRVALLGGFLALRPAAPCPALQALAAACVRELDPFRAPLTEAELA
RRRPDQLTPRQRALLERWGYPYVLEEFRFHMTLTGRLDEEERAAVLARLEARFAPLLADPLAVDGLALFV
EPEPGAPFRLIARVALAG
>gnl|CDD|132268 TIGR03224, benzo_boxA, benzoyl-CoA oxygenase/reductase, BoxA protein. Members of this protein family are BoxA, the A component of the BoxAB benzoyl-CoA oxygenase/reductase. This oxygen-requiring enzyme acts in an aerobic pathway of benzoate catabolism via coenzyme A ligation. BoxA is a homodimeric iron-sulphur-flavoprotein and acts as an NADPH-dependent reductase for BoxB [Energy metabolism, Other]
IIKQHLIDPEICIRCNTCEETCPIDAITHDDRNYVVKADVCNGCMACVSPCPTGAIDNWRTMLRAKAYSL
EEQLTWDELPEEVTLPEAAAEPAAAAGQDDEEPSRGSKSSGVQEVEAAQHGSTRAPWSAAHPYVNLYGVK
APITATVVGNYRLTDEDASSDIHHIVLDFGSHPFPVLEGQSIGILPPGTDASGKPHYARMYSVASPRNGE
RPGYNNLALTVKRVTTDHQGNAVRGVASNYLCDLKKGDKVQVIGPFGSTFLMPNHPESSIMMICTGTGSA
PMRAMTERRRRRRDHGEGGKLMLFFGARTKEELPYFGPLQKLPKDFIDINFAFSRTPEQPKRYVQDAIRE
RAADVAALLKDPNTYIYICGLKGMEEGVLDAFRDVCATNGLSWETLEPRLRAEGRLHLETY
>gnl|CDD|200253 TIGR03225, benzo_boxB, benzoyl-CoA oxygenase, B subunit. Members of this protein family are BoxB, the B subunit of benzoyl-CoA oxygenase. This oxygen-requiring enzyme acts in an aerobic pathway of benzoate catabolism via coenzyme A ligation [Energy metabolism, Other]
INYSEKIPNNVNLSEDKTLQRALEQWQPGYIDWWKDMGPEGFQNSDVYLRTAVSVDPKGWAKFGHVKMPD
YRWGIFLAPQEENRKIPFGEHKGEPAWQEVPGEYRSMLRRLIVTQGDTEPASVEQQRHLGLTAPSLYDLR
NLFQVNVEEGRHLWAMVYLLHKYFGRDGREEAEALLERRSGDADNPRILGAFNEKTPDWLSFFMFTYFTD
RDGKMQLASLAESGFDPLSRTCRFMLTEEAHHMFVGESGVGRVIQRTCQVMKELGTDDPYRIRALGVIDL
PTIQKYLNFHYSVTSDLFGAEVSSNAATAYNAGLKGRYEETKIGDDHQLQNATYPVLDVIDGKIVTREVP
ALTALNERLRDDYIKDVQAGVDRWNKIIEKHGIDFRLTLPHKAFNRKIGEFADTHVSPDGRLISEAEWAA
RKDEWLPTESDRDYVHSLMGPCVEPGKFANWIAPPAVGINNQPGDFEYVRF
>gnl|CDD|274484 TIGR03226, PhnU, 2-aminoethylphosphonate ABC transporter, permease protein. This ABC transporter permease (membrane-spanning) component is found in a region of the salmonella typhimurium LT2 genome responsible for the catabolism of 2-aminoethylphosphonate via the phnWX pathway (GenProp0238)
AMAAAHDAAARPAENLAPALILALAALVLAPLFFYPLALIAELALLDAHGNLSLAAFRQFFASHDFIDAL
GNTLQIAFAAAGGALVLGSLLAAILFFIPFPGAQLVGRFIDLFIAFPSFLIAFAFIFIYGSAGLLNGALM
AAFAFDAPPLDFLFGAGGVILAEITFFTPFVMRPLLAGFAQIDKRLLEAASILGAHGLMLARQVIFPAAL
PAIAAGGILCFLLTLNEFGILLFIGAAGLITLPMAIYSKAILDIDLPAAAAGALIMIALSLALFALYRLA
AARAGEGG
>gnl|CDD|132271 TIGR03227, PhnS, 2-aminoethylphosphonate ABC transporter, periplasmic 2-aminoethylphosphonate binding protein. This ABC transporter periplasmic substrate binding protein component is found in a region of the salmonella typhimurium LT2 genome responsible for the catabolism of 2-aminoethylphosphonate via the phnWX pathway (GenProp0238). The protein contains a match to pfam01547 for the "Bacterial extracellular solute-binding protein" domain
MKLSNFALGGALRRFALAAGAAALLQGAAAPAQAAAVVLVYSADGLEDGDNSLYQDQFDAFEKAEGIKVN
IVEAGGGEVVERAAKEKGNPKADVIVTAPPFIQQAAAEGLLANFNSDAAKAIPAIAKAADGLWAPFVKNY
FSFAINPKLLKSAPASFADLLDADFKGKLAYSNPAQAADGMAVIILAFALFGSEDAAFAYLAKLEANNKF
HSAGTGKLNALLNKGEIAVANGDLQMDLADAEHGGLNIKIFFPAADAGEPPSAFAIPYAIGLVKGAPNQD
AGKKLIDFLLSADAQAKVPDLSFGIPGRSDVPLSDEHGEAAKAAIAGVKLIPPDWDAVAAKKPADIERWH
KEVIGDSGKQTEVTEPE
>gnl|CDD|132272 TIGR03228, anthran_1_2_A, anthranilate 1,2-dioxygenase, large subunit. Anthranilate (2-aminobenzoate) is an intermediate of tryptophan (Trp) biosynthesis and degradation. Members of this family are the large subunit of anthranilate 1,2-dioxygenase, which acts in Trp degradation by converting anthranilate to catechol. Closely related paralogs typically are the benzoate 1,2-dioxygenase large subunit, among the larger set of ring-hydroxylating dioxygenases [Energy metabolism, Amino acids and amines]
VGGCLDFRPNDGVFRIARDMFTEPELFDLEMELIFEKNWIYACHESELPNNHDFVTVRAGRQPMIVTRDG
KGELHALVNACQHRGATLTRVGKGNQSTFTCPFHAWCYKSDGRLVKVKAPGEYCEGFDKATRGLKKARIA
SYRGFVFVSLDVAATDSLEDFLGDARVFLDMMVAQSPTGELEVLPGKSAYTYAGNWKLQNENGLDGYHVS
TVHYNYVATVQHRQQVNAAKGGELATLDYSKLGAGDAETDDGWFSFKNGHSVLFSEMPNPAVRPGYASVM
PRLVAEFGQARAEWMMHRLRNLNLYPSLFFMDQISSQLRIIRPVAWNKTEIISQCIGVKGESDADRENRI
RQFEDFFNVSGMGTPDDLVEFREAQRGFQGRLERWSDISRGYHQWTYGPTQNSQDLGIEPVITGTEITHE
GLYVNQHGQWQRFLLDGL
>gnl|CDD|132273 TIGR03229, benzo_1_2_benA, benzoate 1,2-dioxygenase, large subunit. Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to the larger family of aromatic ring-hydroxylating dioxygenases. Members of this family all act on benzoate, but may have additional activities on various benozate analogs. This model describes the large subunit. Between the trusted and noise cutoffs are similar enzymes, likely to act on benzoate but perhaps best identified according to some other activity, such as 2-chlorobenzoate 1,2-dioxygenase (1.14.12.13) [Energy metabolism, Other]
LDRLLEDDPEKGIFRCKREMFTDPELFDLEMKHIFEGNWIYLAHESQIPNNNDYYTTYMGRQPIFIARNK
DGELNAFINACSHRGAMLCRHKRGNKTTYTCPFHGWTFNNSGKLLKVKDPEDAGYPECFNKDGSHDLKKV
ARFESYRGFLFGSLNPDVLPLEEHLGETAKIIDMIVDQSPDGLEVLRGSSTYTYEGNWKLQAENGADGYH
VSAVHWNYAATTNQRKQREAGDEIKAMSAGTWGKQGGGSYSFEHGHMLLWTRWGNPEDRPLYERRDELAE
KFGEAKADWMIENSRNLCLYPNVYLMDQFSSQIRVFRPISVDKTEVTIYCIAPKGESAEARAKRIRQYED
FFNASGMATPDDLEEFRACQKGYNGTGLEWNDMSRGAKHWIEGPDEAAKEIGLNPVLSGVRTEDEGLYVV
QHHYWLDLMKRAV
>gnl|CDD|132274 TIGR03230, Lipoprotein_lipase, lipoprotein lipase. Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a eukaryotic triacylglycerol lipase active in plasma and similar to pancreatic and hepatic triacylglycerol lipases (EC 3.1.1.3). It is also called clearing factor. It cleaves chylomicron and VLDL triacylglycerols; it also has phospholipase A-1 activity
DFTDIESKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYER
EPSANVIVVDWLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLT
KHKVNRITGLDPAGPTFEYADAPSTLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPG
CDIQETLLVIAEKGLGNMDQLVKCSHERSIHLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNK
LGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGKTSLSHTDQPMKISLYGTHGEKENIPFTLPE
VSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISWSDWWSSPGFHIRKLRIKSGETQSKVIFSAKEGEFS
YLQRGGEAAVFVKCKEKSLSRK
>gnl|CDD|132275 TIGR03231, anthran_1_2_B, anthranilate 1,2-dioxygenase, small subunit. Anthranilate (2-aminobenzoate) is an intermediate of tryptophan (Trp) biosynthesis and degradation. Members of this family are the small subunit of anthranilate 1,2-dioxygenase, which acts in Trp degradation by converting anthranilate to catechol. Closely related paralogs typically are the benzoate 1,2-dioxygenase small subunit, among the larger set of ring-hydroxylating dioxygenases [Energy metabolism, Amino acids and amines]
VEQFLYRKAELCDAQDWDAYLDLFDEDSEFHLPQWISEHNYTRDPKRELSLIYYEDRSGLEDRVFRIRTG
KAASTTPMPRTLHNIHNVRIAELEDGLLRVRVNWRTLFNRLGLEGCFYGHATYVLKPTGDSWLIRRKHSV
LLNDKIDSVLDFYHL
>gnl|CDD|132276 TIGR03232, benzo_1_2_benB, benzoate 1,2-dioxygenase, small subunit. Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to the larger family of aromatic ring-hydroxylating dioxygenases. Members of this family should all act on benzoate, but several have additional known activities on various benozate analogs. Some members actually may be named more suitably according to such alternate an activity, such as 2-chlorobenzoate 1,2-dioxygenase (1.14.12.13)
IQAFLYREARLLDDEQWDDWLECYRADASFWMPAWDDDDQLTEDPQSEISLIYYPNRQGLEDRVFRIKTE
RSSATVPDTRTSHNISNVEIEEQDGDVITVRFNWHTLSFRYKTTDSYFGMSRYTIDFSGESPKIKSKYVV
LKNDYINQVIDIYHI
>gnl|CDD|163189 TIGR03233, DNA_S_dndB, DNA sulfur modification protein DndB. This model describes the DndB protein encoded by an operon associated with a sulfur-containing modification to DNA. The operon is sporadically distributed in bacteria, much like some restriction enzyme operons. DndB is described as a putative ATPase [DNA metabolism, Restriction/modification]
GFSYTFPAIRGMQAGREYYISMCPLRLIPKIFLFDEEELPPELRAQRILNEERIPEIANYILENRDSYVF
SALTASIDGDIEFEPVGEDGSAQRLGTLRIDMDAKFLINDGQHRRAAIEEALKEDPELGDETIAVVFFHD
RGLERSQQMFADLNRHAVRPSSSLSILYDHRDDLALLTKEIIERSEIFKKLVEMEKSNLSKRSRKLFTLS
ALYKANKYLLGKRGKDNITEAIQFAFEFWEAVCSNMPEWQLVREKRLSAGELRRDFIHAHGIALHALGLV
GKDLLRNFPKNWKSKLKGLRDIDWSRSNSIDWEGRAMINGRISKTRSSVTLTANQIKKHLGLPLTPEEQL
IEDAF
>gnl|CDD|163190 TIGR03234, OH-pyruv-isom, hydroxypyruvate isomerase. This enzyme interconverts tartronate semi-aldehyde (TSA, aka 2-hydroxy 3-oxopropionate) and hydroxypyruvate. The E. coli enzyme has been characterized and found to be specific for TSA, contain no cofactors, and have a rather high Km for hydroxypyruvate of 12.5 mM. The gene is ofter found in association with glyoxalate carboligase (which produces TSA), but has been shown to have no effect on growth on glyoxalate when knocked out. This is consistent with the fact that the gene for tartronate semialdehyde reductase (glxR) is also associated and may have primary responsibility for the catabolism of TSA
PRFAANLSMLFTELPFLERFAAAAQAGFTGVEYLFPYDWDAEALKARLAAAGLEQVLFNLPAGDWAAGER
GIACLPGREEEFREGVALAIAYARALGCPQVNCLAGKRPAGVSPEEARATLVENLRYAADALDRIGLTLL
IEPINSFDMPGFFLTTTEQALAVIDDVGRENLKLQYDLYHMQRMGGDLARTLAAYAAHIGHVQIADNPGR
HEPGTGEINYRFLFAVLDRLGYDGWVGLEYKPLTDTEASLGWLK
>gnl|CDD|163191 TIGR03235, DNA_S_dndA, cysteine desulfurase DndA. This model describes DndA, a protein related to IscS and part of a larger family of cysteine desulfurases. It is encoded, typically, divergently from a conserved, sparsely distributed operon for sulfur modification of DNA. This modification system is designated dnd, after the phenotype of DNA degradation during electrophoresis. The system is sporadically distributed in bacteria, much like some restriction enzyme operons. DndB is described as a putative ATPase [DNA metabolism, Restriction/modification]
YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRTHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATE
SNNLAILGLARAGEQKGKKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTL
LVSIMHVNNETGSIQPIREIAEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGAL
VIRKRGKPKAPLKPIMFGGGQERGLRPGTLPVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDALQTL
GVKLNGDPAETIPHILNFSIDGVNSEALIVNLRADAAVSTGSACSSSKYEPSHVLQAMGLDTDRARGAIR
FSW
>gnl|CDD|274485 TIGR03236, dnd_assoc_1, DNA phosphorothioation-dependent restriction protein DptG. A DNA sulfur modification (phosphorothioation) system, dnd (degradation during electrophoresis), is sparsely and sporadically distributed among the bacteria. This protein is one member of a three-gene restriction enzyme cassette that depends on DNA phosphorothioation [DNA metabolism, Restriction/modification]
YFFGQNNSLFPISPELFNFKAAPESKEKNNQKYGQFMRDILVGGIDISSVPVNELNFLEKESEDEFTSLI
LSKLDVSSKDASIQYLPFLAELFQKDLKFLSESPDYFLKNFSLLTQLYSFLYVCQLAMNFEQWDVAEPTS
TPLYFILDWESASKERKAVDSLGFRRLKEYAPNLFPHLHTMSQLNHCDEVESKNKPLWMTFTEIKELMDS
KGEDLSQRLVNFIEEWYSTIETWKDSSTPKEVSKDLPSAFRTLFNCLQEGMLTGSNEKVVKNIEDLGVNV
FIQNRGRIGAVLNMNQDYLLLLTNLAVGEREKLPLNRLIEEFSKRGVAFDRQSQQMLIEFYERHGNLERM
SDSGDAVYVRKTL
>gnl|CDD|132281 TIGR03237, dnd_assoc_2, DNA phosphorothioation-dependent restriction protein DptH. A DNA sulfur modification (phosphorothioation) system, dnd (degradation during electrophoresis), is sparsely and sporadically distributed among the bacteria. This protein is one member of a three-gene restriction enzyme cassette that depends on DNA phosphorothioation [DNA metabolism, Restriction/modification]
EKQFENFLVEHLGDWKAESLKAGDRFQFQSDDVEDVDNLVEALQEQEDVSVFVYKHELGSIEIQNIQLVI
AYTNENVTPNYLATLRDQVGEQKSVWKETALLSIHNSQLDTIQNSTSDLAQDGMPWHPNSIVKLLRQEID
SSMLDKTASICLLDMIKQEQAHDQVTFFGFEELYSTIADGDLEFQELGLFKDKELAGWKGNQIKERLGEN
RELSDKLDFITYHFPRELHDGLGTEEFEKKFTKEGFSDLKREDWKEMGFAEVFTELQKKASINLEGLTVK
EGYLHLWDKPKKETAAGERKRHLVLFNPECQETFHLNLAFSIQSLSNSYVKIQPTKKMKNVEVSVKPGGI
NLNAVITTGFGNQPTFFRLRYKHDDKSELVEFFILVLPIEPFVLDAFKTTYLIAPNKQLLELQHDDQELS
FGQGYNTSITLYENNATVDCNELGILDQPEAYNESDEMRFIIRLTETILPLILEGELPESTLSLPLLLDN
GRRIWKFKDEYQGDYEWSKNRVRFGNREFYLSPERKNLLDWEYEWIESGFRCAVVESDVLVPEDLSISDE
LREAYSRFLTYLKHKKGLPSLCGWGDELVKLAEEYVETYIAEIKSFEEGHELGKRGKDLFKLGTARGNNV
IYFTPFHPLMLAYQLKLNNLLSNDKDATSFKELPNVTLQRLKPDGLVPYIYDERDQLSYPDNQNENLFWM
DFVPVNQSSVDYLAKLVEDKIQQFTGHFGYLFSEYSRAPLQINSVNNENNHETFRGLVNYMLERIEGLKA
IHVNLYDEEGQDTAFDNFARMASYDDFKTKFNLNKGAAQQEPDDILDFLRTRLTYSKFKKEKGEEQKYAH
ISFFKNNAQVRAADQSMDEMLSGVACDGLYTGESSMKSNENYKTGFGLKGYDVEDEPLLKQTTYYFNELC
PNLHNNNTYREGEAIFLRVTSADKKLLEESYKSSYWVTIVDPKVTLEFFNDEQNLVLIHYSDQYTSSSRY
DAITVTKQSQLYHFVLEENVESTIKEFNAFNGEWLLRVVGSKDHESREKLGIISAYKFVLAYFEHSDILW
VPLSLAEVIRVAGNVGLKMADSDFSRHNLGFKNGVISDDLLFIGFKDLMMHLLPVEVKIGARKNLEKARK
QVKELKKYIEDLLGQNSLAGRLYRGLFARQVLSQANKYFLYKVWKEGYFESNNKVVEKWLKGQYELANLI
EYPAGEAILSFQRDAYHRSAKLDVEGILLVNLPEFDLYSGVIQPMEDLKNWLQETELDFIKEEYIL
>gnl|CDD|132282 TIGR03238, dnd_assoc_3, DNA phosphorothioation-dependent restriction protein DptF. A DNA sulfur modification (phosphorothioation) system, dnd (degradation during electrophoresis), is sparsely and sporadically distributed among the bacteria. This protein is one member of a three-gene restriction enzyme cassette that depends on DNA phosphorothioation [DNA metabolism, Restriction/modification]
FSQFKKYLYVKRKIQTDLERILVKFNKELPSSSLLFLCGSSGDGKSEILAENKRKFSEGYEFFLDATHSF
SPNKNAMETLDEIFDGFNQSNKPLIVGINMGMLHNFQEFGYTALNKFKDSIGLFSSSVTTCDHFDFISFE
DYPKFELTEEGPQSTFFLKLLNKITAKEEGNPFYLAYQEDVNKKVRTMVQENYEFLQEPYVQKQIVNLLI
QTRLKFDQFISARAFLDFIADLIAGPSLLFDNLFSKERSELLKFLHELDPVHRRTSKIDQFIIDLSLNLP
DQEFNEFKTVLNRLGCVTSNKGRSWLRPFYVLRITYLTNEYHVKFSQDFEDQTYEKYINVYQLHKLFDFN
SGNKKEIKVFYNETLKDALYKWNNRGSPQLDKGYIYLNEPNGFRLAQFLNIKPDIKHLKFSPNNILESFK
ASIKVADHNGILLPIDYQLLCLLTRVCHGYRPNKHDKNTVVKLTEFVEKITKFAEKKSELHFPNDSRFYK
LTRDDDDEFVFERE
>gnl|CDD|132283 TIGR03239, GarL, 2-dehydro-3-deoxyglucarate aldolase. In E. coli this enzyme (GarL) 2-dehydro-3-deoxyglucarate aldolase acts in the catabolism of several sugars including D-galactarate, D-glucarate and L-idarate. In fact, 5-dehydro-4-deoxy-D-glucarate aldolase is a synonym for this enzyme as it is unclear in the literature whether the enzyme acts on only one of these or, as seems likely, has no preference. (Despite the apparent large difference in substrate stucture indicated by their names, 2-DH-3DO- and 5-DH-4DO-glucarate differ only by the chirality of most central hydroxyl-bearing carbon and is alternately named 2-DH-3DO-galactarate.) The reported product of D-galactarate dehydratase (4.2.1.42) is the 5DH-4DO-glucarate isomer and this enzyme is found proximal to the aldolase in many genomes (GenProp0714) where no epimerase is known. Similarly, the product of D-glucarate dehydratase (4.2.1.40) is again the 5-DH-4DO isomer, so the provenance of the 2-DH-3DO-glucarate isomer for which this enzyme is named is unclear
NRFRQDLLARETLIGCWSALGNPITTEVLGLAGFDWLLLDGEHAPNDVLTFIPQLMALKGSASAPVVRPP
WNEPVIIKRLLDIGFYNFLIPFVESAEEAERAVAATRYPPEGIRGVSVSHRSNRYGTVPDYFATINDNIT
VLVQIESQKGVDNVDEIAAVDGVDGIFVGPSDLAAALGHLGNPNHPDVQKAIRHIFDRAAAHGKPCGILA
PVEADARRYLEWGATFVAVGSDLGVFRSATQALRDKFKK
>gnl|CDD|274486 TIGR03240, arg_catab_astD, succinylglutamate-semialdehyde dehydrogenase. Members of this protein family are succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71), the fourth enzyme in the arginine succinyltransferase (AST) pathway for arginine catabolism [Energy metabolism, Amino acids and amines]
LFIDGKWRAGQGESFASRNPATQEVLWQGAAASADQVEAAVAAARAAFPAWARLSLEERIAVVQRFAALL
EERKEALARVIARETGKPLWETRTEVASMIGKVAISIKAYHERTGESENPMPDGRAVLRHRPHGVVAVFG
PYNFPGHLPNGHIVPALIAGNTVVFKPSELTPWVAEETVKLWEKAGLPAGVLNLVQGARETGVALAAHPQ
IDGLLFTGSSNTGTLLHRQFGGRPEKILALEMGGNNPLIVDEVADIDAAVHHIIQSAFISAGQRCTCARR
LLVPDGAQGDAFLARLVEVAERLTVGAWDAEPQPFMGAVISLRAAQRLLAAQAKLLALGGKSLLEMRQLD
PGAAFLTPGIIDVTGVAELPDEEHFGPLLQVIRYTDFDEAIAIANNTRFGLSAGLLSDDRELYDRFLLEI
RAGIVNWNKPLTGASSAAPFGGIGASGNHRPSAYYAADYCAYPVASLEADSLTLPATLSPGLKF
>gnl|CDD|132285 TIGR03241, arg_catab_astB, succinylarginine dihydrolase. Members of this family are succinylarginine dihydrolase (EC 3.5.3.23), the second of five enzymes in the arginine succinyltransferase (AST) pathway [Energy metabolism, Amino acids and amines]
AYEVNFDGLVGPTHHYAGLSFGNVASTSNRNQVSNPRLAAKQGLLKMKALADLGFKQGVLPPQERPDIPV
LRRLGFSGSDEQVLAKAARQAPVLLSAVSSASSMWTANAATVSPSADTADGRVHFTVANLNNKFHRSIEH
PTTTRLLKAIFNDERYFAHHDALPQVALFGDEGAANHNRLGGEYGSPGVQFFVYGRSAFGRGPRPKRYPA
RQTLEASQAVARLHGLNPAQVVFAQQNPDVIDQGVFHNDVIAVSNRNVLFHHQQAFLNQSQVLDELRAKL
AGLGQQFVAIEVPDAEVSVADAVSSYLFNSQLLSREDGKMMLVVPEECRENAAVWAYLNELVAGGGPIDE
VRVFDLRESMRNGGGPACLRLRVVLNDAELAAVNPAVMMNDALFATLNAWVDRHYRDRLSAADLADPQLL
IECRTALDELTQILNLGSVYPFQ
>gnl|CDD|132286 TIGR03242, arg_catab_astE, succinylglutamate desuccinylase. Members of this protein family are succinylglutamate desuccinylase, the fifth and final enzyme of the arginine succinyltransferase (AST) pathway for arginine catabolism. This model excludes the related protein aspartoacylase [Energy metabolism, Amino acids and amines]
DFLALTLTGKKPHVTQGETNNVRWRWLGEGVLELTPHAPPQKSLVISAGIHGNETAPIEILEQLLGDIAA
GKLPLRVRLLVILGNPPAMRTGKRYLHDDLNRMFGGRYQQLAPSFETCRAAELEQCVEDFFSQGGRSVAR
WHYDLHTAIRGSLHEQFALLPYQGRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLEL
GKALPFGQNDLSQFAAITSALRALISDEAIPARRTDPLRLFRVVSSITKHSDSFELHVASDTLNFTPFPK
GTLLATDGNERYRVTHEGERILFPNPNVANGLRAGLMLV
>gnl|CDD|274487 TIGR03243, arg_catab_AOST, arginine and ornithine succinyltransferase subunits. In many bacteria, the sole member of this protein family is arginine N-succinyltransferase (EC 2.3.1.109), the AstA protein of the arginine succinyltransferase (ast) pathway. However, in Pseudomonas aeruginosa and several other species, a tandem gene pair encodes alpha and beta subunits of a heterodimer that is designated arginine and ornithine succinyltransferase (AOST)
IVRPVRTSDLDALMQLARESGIGLTSLPADRAALGSRIARSEKSFAGESTRGEEGYLFVLEDTETGTVAG
VSAIEAAVGLDEPFYNYRVGTLVHASRELGVYNKIPTLTLSNDLTGSSELCTLFLDPDYRKGGNGRLLSR
SRFLFIAAFRERFGDKIIAEMRGVSDEQGRSPFWEALGRHFFSMDFAQADYLSGIGSKTFIAELMPKYPI
YVPLLPEEAQDVIGQVHPDTRPARAMLESEGFRYQGYVDIFDAGPTLEAEVDDIRAVRESRRVPVKVGES
APGDGTPYLVCNGRLADFRAVLAPLSADAGTLILSADAADALGVSEGDTVRVVPL
>gnl|CDD|274488 TIGR03244, arg_catab_AstA, arginine N-succinyltransferase. In many bacteria, the arginine succinyltransferase (ast) pathway operon consists of five genes, including this protein, arginine N-succinyltransferase (EC 2.3.1.109). In a few species, such as Pseudomonas aeruginosa, the member of this family is encoded adjacent to a paralog, and the two polypeptides form a heterodimeric enzyme, active on both arginine and ornithine. In such species, this polypeptide may be treated as the beta subunit of an enzyme that may be named either arginine N-succinyltransferase (AST) or arginine and orthithine N-succinyltransferase (AOST) [Energy metabolism, Amino acids and amines]
IVRPVETSDLDALYQLAQSTGIGLTSLPANEDLLSARIERAEKTFSGELTRAEQGYLFVLEDTETGTVAG
VSAIEAAVGLEEPFYNYRVGTVVHASKELGIYKALETLFLSNDLTGYSELCTLFLDPDYRKGGNGRLLSK
SRFLFIAQFRERFSKKIIAEMRGVSDEQGRSPFWNALGRHFFSMDFSQADYLSGIGQKAFIAELMPKFPI
YVDLLSAEAQDVIGRVHEDTRPALAMLESEGFRYQGYVDIFDAGPTLEAEVADIRAVRESRLVPVAVGEP
AARDNGPPYIVANTSLSDFRATLAPSDLDAGELVLTAAQADALRVSAGDLVRIVPL
>gnl|CDD|274489 TIGR03245, arg_AOST_alph, arginine/ornithine succinyltransferase, alpha subunit. In some bacteria, including Pseudomonas aeruginosa, the astB gene (arginine N-succinyltransferase) is replaced by tandem paralogs that form a heterodimer. This heterodimer from P. aeruginosa is characterized as arginine and ornithine N-2 succinyltransferase (AOST). Members of this protein family represent the less widespread paralog, designated AruI, or arginine/ornithine succinyltransferase, alpha subunit
IVRPSRFADLPAIERLANESAIGVTSLPADRAKLGEKIAQSERSFAAEVSFVGEERYLFVLEDTETGKLL
GTSSIVASAGYGEPFYSYRNDTLIHASRELKVNNKIHVLYMCHELTGSSLLCSFYVDPRLRKTEAAELLS
RARLLFMAAHRERFQSRIIVEIQGVQDDNGDSPFWDAIGRHFFDLDFATAEYYSGIKSKTFIAELMPPYP
IYVPLLPDDAQDAIGQPHPHARDNCQILNREGFEMDRYIDIFDGGPTLTADLDRLTTVKSSRTKPVKISA
NQTGGTQYLVCNGLLEDFRATLADVTDVDGDLLRLKRDAAEALGVSEGDNVRFAPL
>gnl|CDD|274490 TIGR03246, arg_catab_astC, succinylornithine transaminase family. Members of the seed alignment for this protein family are the enzyme succinylornithine transaminase (EC 2.6.1.81), which catalyzes the third of five steps in arginine succinyltransferase (AST) pathway, an ammonia-releasing pathway of arginine degradation. All seed alignment sequences are found within arginine succinyltransferase operons, and all proteins that score above 820.0 bits should function as succinylornithine transaminase. However, a number of sequences extremely closely related in sequence, found in different genomic contexts, are likely to act in different biological processes and may act on different substrates. This model is desigated subfamily rather than equivalog, pending further consideration, for this reason [Energy metabolism, Amino acids and amines]
VTRQDFDEVMVPVYAPAPFIPVRGEGSRVWDQQGKEYIDFAGGIAVNALGHAHPELVKALIEQAQKLWHI
GNGYTNEPVLRLAKKLVDATFADRVFFCNSGAEANEAALKLARKYALDRHGAHKSEIVAFKNSFHGRTLF
TVSVGGQPKYSQDFAPLPGGIKHAPYNDLAAAKALIDDKTCAVIVEPIQGEGGVVPADPAFLKGLRELCD
RHNALLIFDEVQTGVGRTGELYAYMHYGVTPDILTTAKALGGGFPIGAMLTTTEIAAVLTVGTHGTTYGG
NPLACAVAGKVLDLVNTPEVLAGVKQRHDWFVDRLEKINARYNVFSEIRGKGLLIGCVLTAAYAGKAKQI
VNAAAEEGVMALIAGPNVVRFAPSLVISDEDIDEGLARFERAVEQFV
>gnl|CDD|211799 TIGR03247, glucar-dehydr, glucarate dehydratase. Glucarate dehydratase converts D-glucarate (and L-idarate, a stereoisomer) to 5-dehydro-4-deoxyglucarate which is subsequently acted on by GarL, tartronate semialdehyde reductase and glycerate kinase (GenProp0716). The E. coli enzyme has been well-characterized
ATTPVVTEMRVIPVAGHDSMLLNLSGAHAPFFTRNIVILTDSSGNTGVGEVPGGEKIRATLEDARPLVVG
KPLGEYQNVLNDVRATFADRDAGGRGLQTFDLRTTIHAVTAIESALLDLLGQHLGVPVAALLGEGQQRDE
VEMLGYLFFIGDRKRTSLPYRSGPQDDDDWFRLRHEEALTPEAVVRLAEAAYDRYGFRDFKLKGGVLRGE
EEIEAVTALAKRFPQARITLDPNGAWSLDEAIALCKDLKGVLAYAEDPCGAEQGYSGREVMAEFRRATGL
PTATNMIATDWRQMGHALQLQAVDIPLADPHFWTMQGSVRVAQMCHDWGLTWGSHSNNHFDISLAMFTHV
AAAAPGKITAIDTHWIWQDGQRLTKEPLEIKGGKIQVPDKPGLGVEIDMDAVDAAHELYQKHGLGARDDA
IAMQYLIPGWTFDNKRPCLVR
>gnl|CDD|274491 TIGR03248, galactar-dH20, galactarate dehydratase. Galactarate dehydratase converts D-galactarate to 5-dehydro-4-deoxyglucarate which is subsequently acted on by GarL, tartronate semialdehyde reductase and glycerate kinase (GenProp0714)
LYIRVHPQDNVAIVVNDGGLPAGTVFPDGLTLIEHIPQGHKVALVDLAKGDAIIRYGETIGYALQDIPRG
SWVRESLVTMPTAPPLEDLPLATRVPAKLPPLEGYTFEGYRNADGSVGTKNILGITTSVQCVAGVLDHAV
KRIKAELLPRYPNVDDVVALTHSYGCGVAINAPDAIVPIRTLRNIALNPNFGGEAMVVGLGCEKLQPERL
LPEELSPGLGDANIYRLQDERHGFAAMIEAIMEMAEERLAKLNRRRRETVPASELVVGLQCGGSDAFSGV
TANPAVGFAADLLVRAGATVMFSEVTEVRDAIHLLTPRAETAEVAKALIREMKWYDRYLARGQADRSANT
TPGNKKGGLSNIVEKALGSIVKSGSSPIVGVLSPGEKVTKKGLIYAATPASDFVCGTLQLASGMNLHVFT
TGRGTPYGLAMVPVIKVSTRTELAERWHDLIDIDAGRIATGEATIEDVGWELFHLILDVASGRKKTWAEK
WGLHNDLALFNPAPVT
>gnl|CDD|132293 TIGR03249, KdgD, 5-dehydro-4-deoxyglucarate dehydratase. 5-dehydro-4-deoxyglucarate dehydratase not only catalyzes the dehydration of the substrate (diol to ketone + water), but causes the decarboxylation of the intermediate product to yield 2-oxoglutarate semialdehyde (2,5-dioxopentanoate). The gene for the enzyme is usually observed in the vicinity of transporters and dehydratases handling D-galactarate and D-gluconate as well as aldehyde dehydrogenases which convert the product to alpha-ketoglutarate
MKRKAGSGLLSFPVTPFDADGSFDEAAYRENIEWLLGYGLEALFAAGGTGEFFSLTPAEYEQVVEIAVST
AKGKVPVYTGVGGNTSDAIEIARLAEKAGADGYLLLPPYLINGEQEGLYAHVEAVCESTDLGVIVYQRDN
AVLNADTLERLADRCPNLVGFKDGIGDMEQMIEITQRLGDRLGYLGGMPTAEVTAPAYLPLGVTSYSSAI
FNFIPHIARAFYEALRRGDHATVGEIYKEFILPINEIRNRKKGYAVSIIKAGMEIVGLPAGPVRPPLTDL
TKEEYAQLEVILKKAG
>gnl|CDD|132294 TIGR03250, PhnAcAld_DH, putative phosphonoacetaldehyde dehydrogenase. This family of genes are members of the pfam00171 NAD-dependent aldehyde dehydrogenase family. These genes are observed in Ralstonia eutropha JMP134, Sinorhizobium meliloti 1021, Burkholderia mallei ATCC 23344, Burkholderia thailandensis E264, Burkholderia cenocepacia AU 1054, Burkholderia pseudomallei K96243 and 1710b, Burkholderia xenovorans LB400, Burkholderia sp. 383 and Polaromonas sp. JS666 in close proximity to the PhnW gene (TIGR02326) encoding 2-aminoethyl phosphonate aminotransferase (which generates phosphonoacetaldehyde) and PhnA (TIGR02335) encoding phosphonoacetate hydrolase (not to be confused with the alkylphosphonate utilization operon protein PhnA modeled by TIGR00686). Additionally, transporters believed to be specific for 2-aminoethyl phosphonate are often present. PhnW is, in other organisms, coupled with PhnX (TIGR01422) for the degradation of phosphonoacetaldehyde (GenProp0238), but PhnX is apparently absent in each of the organisms containing this aldehyde reductase. PhnA, characterized in a strain of Pseudomonas fluorescens that has not het been genome sequenced, is only rarely found outside of the PhnW and aldehyde dehydrogenase context. For instance in Rhodopseudomonas and Bordetella bronchiseptica, where it is adjacent to transporters presumably specific for the import of phosphonoacetate. It seems reasonably certain then, that this enzyme catalyzes the NAD-dependent oxidation of phosphonoacetaldehyde to phosphonoacetate, bridging the metabolic gap between PhnW and PhnA. We propose the name phosphonoacetaldehyde dehydrogenase and the gene symbol PhnY for this enzyme
IRAEALRIAGEKVSRDRVIEVRYPYNGTVVGTVPKASVDDVRRAFAIAAAYRPTLTRYERSAILDRAAAL
LAARKEEISDLITLESGLSKKDSLYEVGRVADVLTFAAAEALRDDGQIFSCDLTPHGKARKVFTQREPLL
GVISAITPFNHPMNQVAHKIAPAIATNNRMVVKPSEKTPLSALYLADILYEAGLPPQMLQVVTGDPREIA
DELITNPHVDLVTFTGGVAIGKYIAARAGYRRQVLELGGNDPLIVMEDADLDRAADLAVKGSYKNSGQRC
TAVKRMLVQESVADRFTELLVEKTRAWRYGDPMDPSVDMGTVIDEAAAILFEARVNEAIAQGARLLLGNV
RDGALYAPTVLDRVDPSMTLVREETFGPVSPVIRFCDIDDAIRISNSTAYGLSSGVCTNRLDYITRFIAE
LQVGTVNVWEVPGYRLELTPFGGIKDSGLGYKEGVQEAMKSFTNLKTYSLPW
>gnl|CDD|274492 TIGR03251, LAT_fam, L-lysine 6-transaminase. Characterized members of this protein family are L-lysine 6-transaminase, also called lysine epsilon-aminotransferase (LAT). The immediate product of the reaction of this enzyme on lysine, 2-aminoadipate 6-semialdehyde, becomes 1-piperideine 6-carboxylate, or P6C. This product may be converted subsequently to pipecolate or alpha-aminoadipate, lysine catabolites that may be precursors of certain seconary metabolites
PDRVHEVLSRHMLTDGFDLVLDLDRSRGSVLVDARDGRRYLDMFSFFASSALGMNHPALVDDLAFRARLG
QAALNKPSNSDVYTVAMARFVDTFARVLGDPALPHLFFIEGGALAVENALKTAFDWKSRHNQARGIDPAL
GTQVLHLRQAFHGRSGYTLSLTNTDPRKTARFPKFDWPRIDNPKLRFPLDAPALDAVIALEAEALRQARA
AFAERPHDIACFIAEPIQGEGGDNHFRPEFLAAMRALCDEHDALLIFDEVQTGVGLTGTAWAYQQLGVAP
DIVAFGKKTQVCGIMAGRRVDEVADNVFAVPSRLNSTWGGNLVDMVRATRILEIIEEERLVDRARVQGAH
LLARLHELAAEFPHLVSNPRGRGLMCAFDLPSTADRDELIRQLYREGVLVLGCGERSIRFRPPLTVSREE
IDAAIDAIRRA
>gnl|CDD|132296 TIGR03252, TIGR03252, uncharacterized HhH-GPD family protein. This model describes a small, well-conserved bacterial protein family. Its sequence largely consists of a domain, HhH-GPD, found in a variety of related base excision DNA repair enzymes (see pfam00730) [DNA metabolism, DNA replication, recombination, and repair]
TLHLAQDPEADELLSSDPFALLTGMLLDQQVPMERAFAGPHKIARRMGSLDAEDIAKYDPQAFVALFSER
PAVHRFPGSMAKRVQALAQYVVDTYDGDATAVWTEGDPDGKELLRRLKALPGFGKQKAKIFLALLGKQLG
VTPEGWREAAGPYGEPGSFRSVADITDPESLTQVRAH
>gnl|CDD|211800 TIGR03253, Formyl-CoA:oxalate_CoA-transferase, formyl-CoA transferase. This enzyme, formyl-CoA transferase, transfers coenzyme A from formyl-CoA to oxalate. It forms a pathway, together with oxalyl-CoA decarboxylase, for oxalate degradation; decarboxylation by the latter gene regenerates formyl-CoA. The two enzymes typically are encoded by a two-gene operon [Cellular processes, Detoxification]
TKPLDGIKVLDFTHVQSGPSCTQMLAWLGADVIKIERPGVGDITRGQLRDIPDVDSLYFTMLNCNKRSIT
LNTKTPEGKEVLEELIKKADVMVENFGPGALDRMGFTWEYIQEINPRLILASIKGFGEGSPYENVKAYEN
VAQAAGGAASTTGFWDGPPLVSGAALGDSNTGMHLMIGILAALYQREHTGRGQRVTVAMQDAVLNLCRVK
LRDQQRLDRLGPLAEYPQYPNGAFGDAVPRGGNAGGGGQPGWILKCKGWETDPNAYVYFTIQANNWEQIC
DMIGKPEWITDPAYATPEARQPKLNDIFAFIETYTATKDKFEVTEWLNQYGIPCGPVLSMKEIAEDPSLR
AVGTVVEVDQPIRGKYLTVGAPFKLSDFPPDIKRAPLLGEHTDEVLKELGYDDDEIAELKASGVI
>gnl|CDD|132298 TIGR03254, oxalate_oxc, oxalyl-CoA decarboxylase. In a number of bacteria, including Oxalobacter formigenes from the human gut, a two-gene operon of oxc (oxalyl-CoA decarboxylase) and frc (formyl-CoA transferase) encodes a system for degrading and therefore detoxifying oxalate. Members of this family are the thiamine pyrophosphate (TPP)-containing enzyme oxalyl-CoA decarboxylase [Cellular processes, Detoxification]
ALTDGFHLVIDALKLNGINTIYGVVGIPVTDLARLAQAKGMRYIGFRHEQSAGYAAAAAGFLTQKPGVCL
TVSAPGFLNGLTALANATTNCFPMIMISGSSERHIVDLQQGDYEEMDQLAAAKPFAKAAYRVLRAEDIGI
GIARAIRTAVSGRPGGVYLDLPAAVLGQTMEAEKAKKTLVKVVDPAPKQLPSPDSVDRAVELLKDAKRPL
ILLGKGAAYAQADEEIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSFALAEADVVMLVGARLNWLL
SHGKGKLWGEDAKFIQVDIEPTEMDSNRPIAAPVVGDIGSVVQALLSAAKNGGVKPPADWRNAIKTKSEK
NVAKMAERLSASESPMNYHGALEAIRDVLKDNPDIYLVNEGANTLDLARNVIDMYKPRHRLDVGTWGVMG
IGMGYAIAAAVETGKPVVALEGDSAFGFSGMEVETICRYNLPVCVVIFNNGGIYRGDDVNVVGADPAPTV
LVHGARYDKMMKAFGGVGYNVTTPDELKAALNEALASGKPTLINAVIDPSAGTESGHIGNLNPK
>gnl|CDD|132299 TIGR03255, PhnV, 2-aminoethylphosphonate ABC transport system, membrane component PhnV. This membrane component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate
LIWSDAASRVAGRAAAAVLAAAACCVFFFLPLAVIALSSLAGHWNGTILPAGFSLNHFVEALGGAAFDAL
AASLEIGFCAAAFALACGLGAALALALEGRKRQGVGALLDALFMLPNAIPSVSLGLAILIAFHAGPLDLN
GSLAIVLFAHFALILAFCFRCAAAALAPELADIEEAAASLGAPPAMRLRHVLLPLLMPAIMAALALGFAL
SLGELGATLMIYPPGFATLPIAIFGATDRGNIADAAALSILLLAASLLALIAIAAIAKRLGQ
>gnl|CDD|132300 TIGR03256, Methyl-coenzyme_M_reductase_subunit_alpha, methyl-coenzyme M reductase, alpha subunit. Members of this protein family are the alpha subunit of methyl coenzyme M reductase, also called coenzyme-B sulfoethylthiotransferase (EC 2.8.4.1). This enzyme, with alpha, beta, and gamma subunits, catalyzes the last step in methanogenesis. Several methanogens have encode two such enzymes, designated I and II; this model does not separate the isozymes [Energy metabolism, Methanogenesis]
DKLFKKALKKKFEESPEEKKTTFYTLGGWKQSERKKEFVEAGKEIAEKRGIPFYNPDIGTPLGQRVLMPY
QVSGTDTFVEGDDLHFVNNAAMQQMWDDIRRTVIVGLDHAHRVLEKRLGKEVTPETINHYLETLNHAMPG
AAVVQEHMVETHPALVADCYVKVFTGDDELADEIDKQFLIDINKQFPEEQAEQLKAAIGKTIWQAVRIPT
IVSRTCDGATTSRWAAMQIGMSFISAYKQAAGEAAVADFAFAAKHAEVIHMGEMLPARRARGENEPGGVP
FGHLADIVQTSRVNYEDPAKVALEVVAAGAMLYDQIWLGSYMSGGVGFTQYATAAYTDNILDDFTYYGKE
YVEDKYGGLAEAPASMDVVKDVATEVTLYGLEQYEEYPTALEDHFGGSQRAAVLAAAAGCSTAFATGNAQ
AGLSGWYLSMYLHKEAHGRLGFYGYDLQDQCGAANVLSIRGDEGLPLELRGPNYPNYAMNVGHQGEYAGI
VQAAHAARGDAFTVNPLVKVAFADDNLPFDFTEPRGEFAKGALREFEPAGERDLIIPA
>gnl|CDD|132301 TIGR03257, Methyl-coenzyme_M_reductase_subunit_beta, methyl-coenzyme M reductase, beta subunit. Members of this protein family are the beta subunit of methyl coenzyme M reductase, also called coenzyme-B sulfoethylthiotransferase (EC 2.8.4.1). This enzyme, with alpha, beta, and gamma subunits, catalyzes the last step in methanogenesis. Several methanogens have encode two such enzymes, designated I and II; this model does not separate the isozymes [Energy metabolism, Methanogenesis]
EDKVDLYDDRGNLVEENVPIEALSPLRNAAIQSIIMDIKRTVAVNLAGIEGALASGKMGGKGCQIPGRGL
NYDVIGNAEAIAEKVKKLVQVDEGDDTNVILVKGGKSLLIQVPSSRLIAAAEYSVATLVTAAAVTQTIID
MFGIDPYDAPIVKSAVWGSYPQTMDYMGGNIAGILSIPQKLEGLGYALRNIMVNHVVAITNKNAMNASAL
SSILEQTAMFEMGDAVGMFERHHLLGLAYQGLNADNLLYDLVKANGKDGTVGSVVESVVERAIEDGVISV
DKTAPSGYNFYKANDVPKWNAYAAAGLVAATLVNCGAARAAQNVSSTILYFNDILEKETGLPGVDYGRVE
GTAVGFSFFSHSIYGGGGPGIFNGNHVVTRHSKGFAIPCVCAAMALDAGTQMFSPESTSGLIGDVFSAID
EFREPLKYVAEVL
>gnl|CDD|132302 TIGR03258, PhnT, 2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT. This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate
GACGGIRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGLTGRIAIADRD
LTHAPPHKRGLALLFQNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSG
GMQQRIAIARAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEELPELTILCVTHDQDDALTLADKAG
IMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPAIALGITEAPGLVDVSCGGAVIFAFGDGRHDGRD
KLACIRPEHLALTPRPAGEGRFHATIASVEWHGAALHLLCDLDAACDEPMLVTMLRGRGPAPERGAKLAL
DCEADDAVLIEP
>gnl|CDD|132303 TIGR03259, Methyl-coenzyme_M_reductase_subunit_gamma, methyl-coenzyme M reductase, gamma subunit. Members of this protein family are the gamma subunit of methyl coenzyme M reductase, also called coenzyme-B sulfoethylthiotransferase (EC 2.8.4.1). This enzyme, with alpha, beta, and gamma subunits, catalyzes the last step in methanogenesis. Several methanogens have encode two such enzymes, designated I and II; this model does not separate the isozymes [Energy metabolism, Methanogenesis]
QYYPGATKVAENRRKHMNPEYELEKLREISDEDLVKVLGHRAPGEDYPSVHPPLEEMDEPEDSVREMVEP
IPGAKAGDRVRYIQFADSMYNAPAQPYDRSRFYMIRFRGVDPGTLSGRQIVEARERDLEQISKELVETEL
FDPATTGVRGATVHGHSLRLDEDGVMFDMLQRYRFDEETGHIIMVKDQVGRPLDEPVDLGEPLSEEELKK
ITTIYRVDNVAMRDDAEVVEVVHRIHDQRTKGGF
>gnl|CDD|274493 TIGR03260, met_CoM_red_D, methyl-coenzyme M reductase operon protein D. Members of this protein family are protein D, a non-structural protein, of the operon for methyl coenzyme M reductase, also called coenzyme-B sulfoethylthiotransferase (EC 2.8.4.1). That enzyme, with alpha, beta, and gamma subunits, catalyzes the last step in methanogenesis; it has several modified sites, so accessory proteins are expected. Several methanogens have encode two such enzymes, designated I and II; this model does not separate the isozymes. Proteins in this family are expressed at much lower levels than the methyl-coenzyme M reductase itself and associate and have been shown to form at least transient associations. The precise function is unknown [Energy metabolism, Methanogenesis]
DVEIFPHRLLKAETTEKLLNKLYDLDGILRVVIHGQRLPKKVPYGPARGLPVNHPDRKTIRVKGEDVELR
VQVGRIILELEDEDIVEEIEEICKEMLPFGYEVRVGKFLRTKPTVTDYIKYGEDGDKIDERLLGLVDPRA
KLSESVTIIK
>gnl|CDD|274494 TIGR03261, phnS2, putative 2-aminoethylphosphonate ABC transporter, periplasmic 2-aminoethylphosphonate-binding protein. This ABC transporter extracellular solute-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely [Transport and binding proteins, Amino acids, peptides and amines]
SVVAGFIMTSLFFSACNSKANTELTVYTAIEDELIAKYKDAFEKVNPDIKINWVRDSTGIITAKLLAEKN
NPQADVVWGLAASSLALLDKEGMLKPYKPKGLDALNPKFRDAKNPPHWVGMDAWMAAICFNTVEAKKKGL
PKPTSWEDLTKPEYKGHIVMPNPASSGTGFLDVSAWLQMMGEDKGWDYMDKLHKNIAVYTHSGSKPCKLA
GMGEFPIGISMAYRALKEKKKGAPIDVVFPKEGLGWDIEATAIIKGSKNNDAAKKLVDWSISDEAMELYA
KNYAVVATPGVAKPDAGFPKNVEDLLIKNDFVWAAANRDKILEEWSKRYGAKAE
>gnl|CDD|274495 TIGR03262, PhnU2, putative 2-aminoethylphosphonate ABC transporter, permease protein [Transport and binding proteins, Amino acids, peptides and amines]
LIARLLLAGMILALLLFLLLPLLALLTKSVYDSDGDFIGLANFAEYFATPGLLQSLGNSLTVSAIVTAIV
VPLAFAFAYALTRSRIPGKGAFRLVALLPLLAPSLLPAISLIYLFGNQGLLKGLLGGFSIYGFWGIVIGE
VFYTFPHALMILVTALSLADGRLYEAARAMGASPWRTFFTVTLPGAKYGLISAAFVVFTLVITDFGVPKV
IGGDYNVLATDIYKQVIGQQNFPMGAVVGVLLLLPALLAFGIDRAIQRRQRAQLSSRSVPYQPKPNRVRD
AACLVYCAIISAALLAVVGMAVYASLVKFWPYNLSLTLKHYNFDLMDGGGWEAYKNSLRLAATTALIGTI
LVFGGAYLIEKTRGFGLLRGVLRFLAILPMAVPGLVLGLGYIFFFNAPTNPLNGLYGTMALLVLCTVVHF
YTVSHLTAVTALKQIDSEFEAVSASLKVPFYKTFLRVTLPVCLPAILDIARYLFVNSMTTVSAVVFLYSP
DTKLASVAILNMDDAGDIAPAAAMATLIVLTSAVAKLLFALASRRLLRRTQAWRKR
>gnl|CDD|213788 TIGR03263, Guanylate_kinase, guanylate kinase. Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
LLIVISGPSGAGKSTLVKALLEEDPNLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAE
VHGNYYGTPKSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVI
ERRLAKAKKEIAHADEFDYVIVNDDLEKAVEELKSIILA
>gnl|CDD|132308 TIGR03264, met_CoM_red_C, methyl-coenzyme M reductase I operon protein C. Members of this protein family are protein C, a non-structural protein, of the operon for methyl coenzyme M reductase, also called coenzyme-B sulfoethylthiotransferase (EC 2.8.4.1). That enzyme, with alpha, beta, and gamma subunits, catalyzes the last step in methanogenesis; it has several modified sites, so accessory proteins are expected. Several methanogens have encode two such enzymes, designated I and II; this protein occurs only operons of type I. The precise function is unknown [Energy metabolism, Methanogenesis]
GRETQVVDCRETMGMGEGGGLAQRGTFAECGRNDVVAVAMSPGRRHITKPVCEITYALREAGIQTSVLVL
NAGSGIPPDAPRGGGGSTFGLTPEEIEQINRHKLAVIHLGNVKSHIIYKARLILKHVDIPAIIVCQAPVD
FEDFAKIGVKTRAVMPLEPKTKGTVVEIVTGVIRGESCPQEKIDEIIRKVKTHL
>gnl|CDD|274496 TIGR03265, PhnT2, putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein. This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely [Transport and binding proteins, Amino acids, peptides and amines]
SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITR
LPPQKRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQ
QRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNH
GVIEQVGTPQEIYRHPATPFVADFVGEVNWLPGTRGGGSRARVGGLTLACAPGLAQPGASVRLAVRPEDI
RVSPAGNAANLLLARVEDMEFLGAFYRLRLRLEGLPGQALVADVSASEVERLGIRAGQPIWIELPAERLR
AFA
>gnl|CDD|132310 TIGR03266, methan_mark_1, putative methanogenesis marker protein 1. Members of this protein family represent a distinct clade among the larger set of proteins that belong to families TIGR00702 and pfam02624. Proteins from this clade are found in genome sequence if and only if the species sequenced is one of the methanogens. All methanogens belong to the archaea; some but not all of those sequenced are hyperthermophiles. This protein family was detected by the method of partial phylogenetic profiling (see Haft, et al., 2006)
TQRAYSPEETLEKIKDLIKKIGVTRIADITHLDRIGIPVFSSIRPSAADGAISIYAGKGATEIQARVSAI
MEAFERYSAERPGNNANILGAREPCNPLNPESLILPQPYYPTSPLEWVEGYDLTNNEEVYVPANAVFHPY
DSPGQGKLFRSNTNGLASGNVLEEAIFHGLLEVIERDAWSLAEASRNLGPEINVTAENGYLYELLEKFKD
AGVDVKLRDLTSDTGIPTVAAVSDDLKLKDPALLVMGVGSHLDPEIAVLRALTEVAQSRATQIHGAREDT
DREEFIRKVGYDRMKRLNRHWFEPEETINIDDMPDLSTRSFKEDIEIILEKLKEAGLDKVIVVDLTREEV
GVPVVRVIIPGMELYTIDRDRVGNRI
>gnl|CDD|132311 TIGR03267, methan_mark_2, putative methanogenesis marker protein 2. A single member of this protein family is found in each of the first ten complete genome sequences of archaeal methanogens, and nowhere else. Sequence similarity to various bacterial proteins is reflected in Pfam models pfam00586 and pfam02769, AIR synthase related protein N-terminal and C-terminal domains, respectively. The functions of proteins in this family are unknown, but their role is likely one essential to methanogenesis [Energy metabolism, Methanogenesis]
NLRELARELRSFEGVTRKHPIKDVVEILEPLDVTYEGNVIVDFGDDAAAIKIGGDDILLLAADGIWGKLL
DADPWWAGYCAVLVNVNDIAAMGGKPVGMVNVLSINDVDVCREVLEGMREGAWKFGVPVVGGHTHPDTPY
NALDVAIVGIAKEDCIIRSDTAKPGDLIIFAIDLDGRPYPSFPLNWDTTTMKSPDYLRAQMDAVVEIAER
KLVKAGKDISNPGLIGTLGMLLEASRVGAEVDLESIPKPEDVDMVTWLKMYPGSGFVLTADPENVREIVR
VLEDAGLTASVIGEVIEDGKLYVSDGDESAVVFDFRKDRITGV
>gnl|CDD|132312 TIGR03268, methan_mark_3, putative methanogenesis marker protein 3. A single member of this protein family is found in each of the first ten complete genome sequences of archaeal methanogens, and nowhere else. This protein family was detected by the method of partial phylogenetic profiling (see Haft, et al., 2006). The functions of proteins in this family are unknown, but their role is likely one essential to methanogenesis [Energy metabolism, Methanogenesis]
VKVNGEEVTVPDGSTVRDALKASDAPYIEGATIGIIKGVQELERETKEYLIKTTKGEVVIELTPNTEAGK
FWSEIYKELEGKQIRWTTPQEVAFGPFPSDLEPSREPSEYERWDVILSLSGFDPDETHIIFSKKRHAAEY
GVPDENGIIARVVGGKRVIDRLSDGDQIISIEPVIERKEIVDSATTTDLSTVLEDGDRIFTYVEVELDPN
APVSVEHFLALMEDGTFRVDYRTSTFISDDSLRGLDKPEENIEKRRRGAVTVRNSGVGEGRVYIYREDRP
SSLSHNVVGHVTRGIELIDIAQEGDRLSVETEPPRIDLVGLTQEEAEELLEELGIELEKEGVDGDDAVVV
KQEPPYTLDVLKEGKVKVEGVPKDKVIEIELYDDNAPRSVWYFRKFTGLKTKPVGRLPVHFAFKEMIMFK
GNKELAKGLIPENTPEDKVEAGVIGVTNQACKHVGMIGVRLEDSDEFGPTGEPFSGTNIIGRVVEGMERL
KGLKEGDTVYVRE
>gnl|CDD|132313 TIGR03269, met_CoM_red_A2, methyl coenzyme M reductase system, component A2. The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2 [Energy metabolism, Methanogenesis]
IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEKCG
YVERPSKVGEPCPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGY
EGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNA
LEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPII
KVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWV
DMTKPGPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAEEI
LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDF
VLDVCDRAALMRDGKIVKIGDPEEIVEELT
>gnl|CDD|274497 TIGR03270, methan_mark_4, putative methanogen marker protein 4. Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely linked to it. Some members have been suggested to be a methyltransferase, based on the proximity of its gene to genes of the multi-subunit complex, N5-methyl-tetrahydromethanopterin--coenzyme M methyltransferase. That context is not conserved, however. The family shows similarity to various phosphate acyltranferases [Energy metabolism, Methanogenesis]
VELEDPEEELIDDLVNGRLDAAVRGSLSSSNTIRELKKALGKIYRASILETADGRIFLLAPVGIDEGWTI
SDKVKIIELASEFLRRLGREPKVAVLSGGRLGDVGRSPEVDRSIADGELIARLLKDGMEIEHYGILIEEA
LKDGSNVIIAPDGISGNLIFRSLALVGGGRSYGAPVLNDEGVFVDTSRSQTAEGYYNALKLA
>gnl|CDD|132315 TIGR03271, methan_mark_5, putative methanogenesis marker protein 5. Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it [Energy metabolism, Methanogenesis]
KVFIYPPNSLILSDLVERFGHEPLVLQKEIKKRVTTPEIDSPPLNITPEDPKKGLKYAAVEVPSGVRGRM
SLFGPLIEEAEAAIIVREAPFAFGCMGCARTNELTVFLVRRKDIPILELDYPTSEEEGIIFVRKINDFLD
SL
>gnl|CDD|274498 TIGR03272, methan_mark_6, putative methanogenesis marker protein 6. Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it [Energy metabolism, Methanogenesis]
IVLIPSAKVSPKELVQKLYELELPVTIKETCFGAIITGPEEEVMKVAERIRELDPNHIFVKDRGFPPGDP
RRCRANRGGGPRPGFHQLEAEVELLDRIGEALEKLEKPKEVEVEEPEKISVDEFKKIIEEEL
>gnl|CDD|132317 TIGR03274, methan_mark_7, putative methanogenesis marker protein 7. Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it
YETVTYTGGVHKHDEIKELIEDLGGFIIQKHMMQLEVVLTLAVPKEDVDIIKEKAKELLGEIKEAPLAGT
EIAVVSPSLARHHLPHAACDIAEYLRRYGAKTNMIGLARGAGRRIAQLSDEERRLIEEHDLAIFVFGNFE
DCIKKKMPLFRDIDIPVVVTGGPEKIDLMDIPGADAYVGGLGRIPHRLRRGEEIRALDKLVEVVSKIIDE
RRRELAKDPLIVPPARVKDEIERQVPAIKEVTSPMPIVLQLDGVRVKLPYDEYAEEIAEVEVEGYRLGDI
ADIRRSKMKDYILVKIKPKSEV
>gnl|CDD|132318 TIGR03275, methan_mark_8, putative methanogenesis marker protein 8. Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it
HVMEALGKTRVVVKNGKVVEVGEPLIEYCPLFAKYRGIEEITPEAIRKNIEFRIDDFGMFTKNRRLESSD
RFVGFGASEILMTALKSGFIDAAVIVCDGAGTVITTNPALVQGLGGRISGLIETSPIPEVIEKIEDEGGI
VLDPDTATIDQIKGVEKAIELGYKKIAVTVADAEDAKAIRELESESGIDIIIFAVHTTGIDREDAEEVVQ
YADIVTSCASKNIREIAKPRALLQVGSAVPVYALTDKGKELLLERAKDI
>gnl|CDD|132319 TIGR03276, Phn-HD, phosphonate degradation operons associated HDIG domain protein. This small clade of proteins are found adjacent to other genes implicated in the catabolism of phosphonates. They are members of the TIGR00277 domain family and contain a series of five invariant histidines (the domain in general has only four)
KQTLDEIFALFDEHGARQYGGEAVSQLEHALQCAQLAEAAGADDELIVAAFLHDIGHLLADEGATPMGRG
GDDHHEELAADYLRELFSPSVTEPIRLHVQAKRYLCAVDPAYAESLSPASRRSLELQGGPFTAAEADAFE
RDPHAADAIRLRRWDDLAKDPGVPTPDLDHFMPLAERHL
>gnl|CDD|132320 TIGR03277, methan_mark_9, putative methanogenesis marker domain 9. A gene for a protein that contains a copy of this domain, to date, is found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it. A 69-amino acid core region of this 110-amino acid domain contains eight invariant Cys residues, including two copies of a motif [WFY]CCxxKPC. These motifs could be consistent with predicted metal-binding transcription factor as was suggested for the COG4008 family. Some members of this family have an additional N-terminal domain of about 250 amino acids from the nifR3 family of predicted TIM-barrel proteins
GWYNAPSHVCRGGDIRGLAFCCPPVKPCPIHPKLAELGLSPQEFVRIKEEFAKGTPLGQGENTCFGSLVW
CCKITKPCPLRDSALQRIGMSPEEYMELKKKLAEELLKK
>gnl|CDD|132321 TIGR03278, methan_mark_10, methanogenesis marker radical SAM protein. Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. It is a radical SAM enzyme by homology. The exact function is unknown, but likely is linked to methanogenesis. In most genomes, the member of this family is encoded by a gene next to, and divergently transcribed from, the methyl coenzyme M reductase operon
VGGRPGIDCRGFCRYCYFKKVDDEQPFGCKNCPPGTKGCDYCTRSVWEINGDFIPPQVVLGEVQTSLGFR
TGRDTKVTISGGGDVSCYPELEELTKGLSDLGLPIHLGYTSGKGFDDPEIAEFLIDNGVREVSFTVFATD
PELRREWMKDPTPEASLQCLRRFCESCEVHAASVIIPGVNDGDVLWKTCADLESWGAKALILMRFANTEE
QGLILGNAPIIPGIKPHTVSEFKNIVRETHKEFPIRVTGTPLCDPETGAPFALAKEPNEYLEILPPVEKE
ATIITGRVAAPFIREIFRALGGGDLVNVVPVKKDIACLITEDDLEELDLSEVKETVIIPGRAFVHDMVAE
EILKRDGVDRIVVRGPDRLTADGEMSGGMTREEVLEFELEAFRELINLINFLGE
>gnl|CDD|132322 TIGR03279, cyano_FeS_chp, putative radical SAM enzyme, TIGR03279 family. Members of this protein family are predicted radical SAM enzymes of unknown function, apparently restricted to and universal across the Cyanobacteria. The high trusted cutoff score for this model, 700 bits, excludes homologs from other lineages. This exclusion seems justified because a significant number of sequence positions are simultaneously unique to and invariant across the Cyanobacteria, suggesting a specialized, conserved function, perhaps related to photosynthesis. A distantly related protein family, TIGR03278, in universal in and restricted to archaeal methanogens, and may be linked to methanogenesis
LISAVLPGSIAEELGFEPGDALVSINGVAPRDLIDYQFLCADEELELEVLDANGESHQIEIEKDLDEDLG
LEFTTALFDGLIQCNNRCPFCFIDQQPPGKRESLYLKDDDYRLSFLYGSYLTLTNLPPAEWQRIEQLRLS
PLYVSVHATEPSLRARLLKNPRAGLILEQLKWFQERRLQLHAQVVVCPGINDGKHLERTLRDLAQFHDGD
WPTVLSVAVVPVGLTRFRPEEDELTPVTPECARRVIAQVEALQTQFQRQLGSRFAWLADEWYLIAGEPLP
PRAHYEDYPQLENGVGSIRSFLEEFDRQAEHLPKKIAPARRLSWVVGNAVEQAFEPLVERLNAVEGLELD
LHGLASDYWGQEITVTGLLTGQDLIAGLKGKDLGDGLLLPSVMLKHGELVFLDDLTVEEVAEALGTPIRV
VAGGADLLEHAIT
>gnl|CDD|213789 TIGR03280, methan_mark_11, methanogenesis imperfect marker protein 11. The first twenty-nine completed genomes with a member of this protein family include twenty-eight archaeal methanogens and one other related archaeon, Ferroglobus placidus DSM 10642. The exact function is unknown, but the protein likely belongs to a system usually tightly linked to methanogenesis
PYRKILAVVDETRELVELIEYHPCPSGSEWVIYQYQRTSPLILKARREGNKHRFLLKTGKADLDLEPSVS
AAGIEEVIVEGDEVRIVYAGLAGAGVGAALCRGSAEGVLRVEIDEKGGGSKLGRATVVTPRLEKVLIGID
DTDTPEEGATWTLAHNIARELEDEKGGFYLDHTTVQLYPGNPNKTQNCVSVVLEFAVYPEYKEKLAREFK
KLLKEYTLSDETAMAVYDGLFPPKELKEYGNKAKREMVSIEEAERVAERNNIEIIEVTGGRGIIGALAAL
GLYDRPEEAAKV
>gnl|CDD|132324 TIGR03281, methan_mark_12, putative methanogenesis marker protein 12. Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it [Energy metabolism, Methanogenesis]
FVGIDHGTTGIRFAIIDGEKEPVFKLPRTELSEKEILESDELEDRVALEEIDLIALTYSMGDGISKITPI
ERVKNRGLQSIEGAGKKTGGGTRVYDEIKESGIPAVLIPGLHRGSPCLDPRFRAVYSHIASPEKVSIAYN
AYCLTGFKDFIVSDISSNTVTLLIKDGKIIGGFDACVGAPGVLHGPLDLEAIRNIDAGKKTANEAFSHAG
AVKIACADKGVENAKEEILNNYNGDEPGRLALDSLAMSVAMEIASLGLLDCKEAGVVLAGSGGTLREPIN
FSGKIKRVLSCKVLVLDSESAAIGLALIAEDIFSGKREILGIDVDY
>gnl|CDD|274499 TIGR03282, methan_mark_13, putative methanogenesis marker 13 metalloprotein. Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it. This metal cluster-binding family is related to nitrogenase structural protein NifD and accessory protein NifE, among others [Energy metabolism, Methanogenesis]
HPRPSPIAAALYTLRDLEVDVIILHGPSGCCFRTARLLEEDGVRVFTTGMDENDFVFGASEKLVKVIRYA
EEKFKPELIGVVGTCASMIIGEDLKEAVDEADVDAEVIAVEVHAGFGDNTEGVIATLESAAEAGIIDEDE
VERQKELLKKATEVEKKRGMAKREYIEPSYGDDKHKVAKRLVDLIQEGKKVLAILNAKKETAYLFADPLL
ALNKLGPDNPPVNIANLDPNIGLPKVRRDAEVILSDFDATGLEYDYITGGLDEYPVTGEKAAEIIEDEDP
DFAVITGVPHAVPIEELDGIECIAVTDGPRQVAPLKELGYDYVVVELDAHARTLGVRSIVESEFGETLRS
LL
>gnl|CDD|132326 TIGR03283, thy_syn_methano, thymidylate synthase, methanogen type. Thymidylate synthase makes dTMP for DNA synthesis, and is among the most widely distributed of all enzymes. Members of this protein family are encoded within a completed genome sequence if and only if that species is one of the methanogenenic archaea. In these species, tetrahydromethanopterin replaces tetrahydrofolate, The member from Methanobacterium thermoautotrophicum was shown to behave as a thymidylate synthase based on similar side reactions (the exchange of a characteristic proton with water), although the full reaction was not reconstituted. Partial sequence data showed no similarity to known thymidylate synthases simply because the region sequenced was from a distinctive N-terminal region not found in other thymidylate synthases. Members of this protein family appear, therefore, to a novel, tetrahydromethanopterin-dependent thymidylate synthase [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
LVIRKRSIAQAWRELVTKIMVEGEVVEDERGSLTKEVRNLIIHIENPGPEKIPEGYPLDEEKLEEYEKQL
LDPERQGFVYTYGNRLRRYFGIDQIDYIIERLNQSPNSRRAIAITWDPPQDIKVDEVPCLQLVQFLIRDN
KLYLTAFFRSNDVGGAWVANAIGLRRLQEYVAEKVGVEPGTLTTHAISAHIYERDFDEL
>gnl|CDD|213790 TIGR03284, thym_sym, thymidylate synthase. Members of this protein family are thymidylate synthase, an enzyme that produces dTMP from dUMP. In prokaryotes, its gene usually is found close to that for dihydrofolate reductase, and in some systems the two enzymes are found as a fusion protein. This model excludes a set of related proteins (TIGR03283) that appears to replace this family in archaeal methanogens, where tetrahydrofolate is replaced by tetrahydromethanopterin [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
QYLDLLRDILENGHQKGDRTGTGTISVFGYQMRFDLSKGFPLLTTKKVPFRLIASELLWFLKGDTNIRYL
LDHNVNIWDEWAFERWVKSDDYNGPDMTDFGHRAQDDPEEDDEFADKYGDLGPVYGKQWRSWATPDGETI
DQIKNVIEMIKTNPDSRRLIVSAWNPEDVPTMALPPCHTLFQFYVADGKLSCQLYQRSADVFLGVPFNIA
SYALLTHLIAQETGLEVGEFVHTLGDAHLYSNHLEQAKLQLTREPRPLPTLKLNPDKKDIFDFEYEDIEI
EGYDPHPAIKAPVAV
>gnl|CDD|274500 TIGR03285, methan_mark_14, putative methanogenesis marker protein 14. Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it [Energy metabolism, Methanogenesis]
YYIVASVELGNTTTKCILTATNLKTGKTYLLNKCVRMTRDVRPPRSGEEVFGKTVWGVELTRESVAELVK
DTLKESLKKAGLDIDDLDFVVRSTGVTAGFASPEEVGEMIKALADGCLKAGVPPSKMTPAMSKENIPEPL
RKYSFLDKVIFDGAVAGVAPPTGKEVVANEMEGELVTAGIKVGSKSTDVDFRNPCISIDFGTTLAGRITN
DDLPYAKTIGNFCGLAGAIPDAIIRGCGVIDERMGAALDLANKQNPPQFNEKKAREHAERIHEYIDIRKV
PANRDRFGTVPVDPKAAKKAGTTLIGCDVGENGSDLTKLTEIGREIYESEGIPTLFAVLDDVMALIAKRL
IEQASKLGLIQEKTTLGITGRAGITGYKPELILEYLKNSFLWDKEENVVFVDDGLALGAAVMARCMNSLG
TPQNPLGGRRGGGCILGQRIKLQKK
>gnl|CDD|132329 TIGR03286, methan_mark_15, putative methanogenesis marker protein 15. Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it. Related proteins include the BadF/BadG/BcrA/BcrD ATPase family (pfam01869), which includes an activator for (R)-2-hydroxyglutaryl-CoA dehydratase [Energy metabolism, Methanogenesis]
VKIAQLSCGTEYSGVQPEIEKAAEKVGAEIIFPEVDLDYIDEACRDFGLTVKSGDLKLMIARAMALVEGY
TEADAVFIATCFRCAEGALVRNEVRRYIQENTNLPVVSYSFTERTTAGELLTRMEALTTIVRRKSLLARE
RQEGLTLGIDSGSTTTKAVVMEDNEVIGTGWVPTTKVIESAEEAVERALEEAGVSLEDVEAIGTTGYGRF
TIGEHFGADLIQEELTVNSKGAVYLADKQEGPATVIDIGGMDNKAISVWDGIPDNFTMGGICAGASGRFL
EMTAKRLGVDITELGKLALKGMPEKVRMNSYCIVFGIQDLVTALAEGASPEDVAAAACHSVAEQVYEQQL
QEIDVREPVILVGGTSLIEGLVKALGDLLGIEVVVPEYSQYIGAVGAALLASGF
>gnl|CDD|274501 TIGR03287, methan_mark_16, putative methanogenesis marker 16 metalloprotein. Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it. This protein is a predicted to bind FeS clusters, based on the presence of two copies of the Fer4 domain (pfam00037), with each copy having four Cys residues invariant across all members [Energy metabolism, Methanogenesis]
VLTADELKDRIRNGEEDTVEDVDVVTCATCGIMSGTYAVFSFPVSEPGSFRRAEEVYLNGIPAVVGPCPN
ERLGLVDLIVYGTAHSDDRYGGGFLFRDLVEGKEVEVKVTSDEGKEYEATITLDELPTARLFGTRMAFKN
YSAITNPGERPVKTIFHALPLEGTFGEASFSGCGELNPLENDPKLETIRPGTRVLLNGAEGIITGKGTRS
SPEKPNLTLHADLKDMDPHYMGGFRTSAGPEIINTVAVPIPVLSEEVLENLKVLDSDIPLPVVDISDRTP
IAEITYADVWDNTDVRPKYNPERCENCDPCLVEEACPVPAIKKDGTLNTEDCFGCGYCAEICPGGAFEVN
LGSVRVEGRKIPITCRQSDRKRAKKLAEELKEAIERGEFKI
>gnl|CDD|132331 TIGR03288, CoB_CoM_SS_B, CoB--CoM heterodisulfide reductase, subunit B. Members of this protein family are subunit B of the CoB--CoM heterodisulfide reductase, or simply heterodisulfide reductase, found in methanogenic archaea. Some archaea species have two copies, HdrB1 and HdrB2
KYAFFLGCIMPNRYPGIEKATRLTMEKLGIELLDMPGASCCPAPGVFGSFDLKTWLTLAARNLVIAEEMG
KDILTVCNGCYGSLFEANHLLKENPELRDKVNEKLAEIGREYKGTINVRHLAEFLYKDIGVDKIKEKVTK
PLNLNVAVHYGCHLLKPSDERHLGSPERPKILDELVEATGAKSVDYKDKMMCCGAGGGVRSRDLDVALDM
TKEKLENMKEAGADCIVNVCPFCHLQFDRGQIEIKEKFGEEYNIPVLHYSQLLGLAMGMSPEDLALDLHA
IDCDEFLQKL
>gnl|CDD|274502 TIGR03289, frhB, coenzyme F420 hydrogenase, subunit beta. This model represents that clade of F420-dependent hydrogenases (FRH) beta subunits found exclusively and universally in methanogenic archaea. The N- and C-terminal domains of this protein are modelled by pfam04422 and pfam04423 respectively
LGTYKEIVSARSTDREVLKKAQDGGIVTGLLIYALEEGIIDGAIVAGPGEEPWKPEPMVATTPEEILAAA
GTKYTVCPNVSVLKEAVREYGLEKIGTVGTPCQVMGLRKMQTYPVGVRFVADKIALLIGIYCMENFPYTS
LKTFICEKCGVTMELVEKMDIGKGKFWVYTQDGEVGTIPLKETHGYEQAGCHVCKDYVAELADISTGSVG
SPDGWSTVIIRTDKGESIFNKAVEAGIFETKPIEEVKPGLGLLEKLATQKKEKNQKEIEHRKEMG
>gnl|CDD|132333 TIGR03290, CoB_CoM_SS_C, CoB--CoM heterodisulfide reductase, subunit C. The last step in methanogenesis leaves two coenzymes of methanogenesis, CoM and CoB, linked by a disulfide bond. Members of this protein family are the C subunit of the enzyme that reduces the heterodisulfide to CoB-SH and CoM-SH. Similar enzyme complex subunits are found in various other species, but likely act on a different substrate
VKACYQCGTCTGSCPSGRRTSYRTRLIIRKALLGLKDEVISDDDLWMCTTCYTCQERCPRDVKITDIIKA
LRNLAAKKGFMAKAHRKTASFVLKTGHAVPINDEIKELRKELGLDEIPPTTHKYPEALEEVQKLIKALEF
DELI
>gnl|CDD|274503 TIGR03291, methan_mark_17, putative methanogenesis marker protein 17. Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it [Energy metabolism, Methanogenesis]
VVECYDKVGAELYRKIIRTALTDLKLARAIIRVRFFLDPEEPLFIAAVITRKVSRPITLRDMAEVEEDDK
EGGLKLSIADETYLPDLLRKLWSSYGKDRVSQPDRFEITIETPIDEASEGIEDLEVADPRKDLKKKVYDF
MFRVFPEGFRVKRNAYEDNRFVFVASEETLEDEWIDEAFELIDEL
>gnl|CDD|274504 TIGR03292, PhnH_redo, phosphonate C-P lyase system protein PhnH. PhnH is a component of the C-P lyase system (GenProp0232) for the catabolism of phosphonate compounds. The specific function of this component is unknown. This model is based on pfam05845.2, and has been broadened to include sequences missed by that model which are clearly true positive hits based on genome context
RTFRALLDAMSRPGTIRQLPSAASPPLPLSPATAAVLLTLLDHETPVWLAADDAALRAWLRFHTGAPVTA
DPEEADFAVIDDGSALPDLSRFALGTLEYPERSATLIIEVPSLASGPPLTLTGPGIATERTVAPSGLPDA
FWDERQENRAAFPLGVDLILTDGERVLGLPRTTR
>gnl|CDD|274505 TIGR03293, PhnG_redo, phosphonate C-P lyase system protein PhnG. PhnH is a component of the C-P lyase system (GenProp0232) for the catabolism of phosphonate compounds. The specific function of this component is unknown. This model is based on pfam06754.2, and has been broadened to include sequences missed by that model which are clearly true positive hits based on genome context
TMTRQRWLEILAHAPLEELEALANRVAPSPQYSVLRAPETGLVMLRGRDGGTGEPFNLGEITVTRAAVRL
NDGTEGYAYVLGRDKRHAELLAVLDALLQAPLLHDELIADLIAPLAQRLAERRARRQAEAAATRVDFFTM
VRGE
>gnl|CDD|132337 TIGR03294, FrhG, coenzyme F420 hydrogenase, subunit gamma. This model represents that clade of F420-dependent hydrogenases (FRH) beta subunits found exclusively and universally in methanogenic archaea. This protein contains two 4Fe-4S cluster binding domains (pfam00037) and scores above the trusted cutoff to model pfam01058 for the "NADH ubiquinone oxidoreductase, 20 Kd subunit" family
KITVGYVHLSGCTGCLVSLTDNYEGLLDILDNIADLVYCQTLADAREIPEMDVALVEGSVCLQDEHSLEE
IKELREKAKVVVALGACAATGNFTRYSRGGQQAQPQHESFVPITDVIDVDLAIPGCPPSPEAIRNVCVAL
LNGDMEYLQPLAALAEEGTEACGCDLMTKVVNQGLCMGCGTCAAACPTRAIEMEDGRPNVNRDRCIKCGA
CYVQCPRAFWPEYENIKE
>gnl|CDD|274506 TIGR03295, frhA, coenzyme F420 hydrogenase, subunit alpha. This model represents that clade of F420-dependent hydrogenases (FRH) beta subunits found exclusively and universally in methanogenic archaea. This protein is a member of the Nickel-dependent hydrogenase superfamily represented by Pfam model, pfam00374
LSKRIEISPTTRHEGHAKLVLEVDDEGIVEKGRYLSITPVRGFEKMLVGKAAEFAPIAVSRICGICPIAH
TLASVEAIEDSIDIEVPKDGLLLRELTGAANRLHSHALHHFLIAPDFIPENLMAEAIKRIQEMRKNGQYV
VDIVGGEGIHPPNIRIGGMADNITELAKSRLYYRLKQYEPLAIEHVELMIGLIEDWETEKGIPEKLGVHD
QPYIATHQTYGDRTKIDLDRVTEVMPYSWYDDPEIAKQACTTIPLYDGRPVEVGPRARMVKFQNFKEKGA
MAIHIARALENKTALYRAIEILDELDTNGKVRADEDERGDGKLGIGAHEAPRGLDVHMARVEDGKIQFYS
ALVPTTWNIPTMGKATEGFHHQYAEHVMRAYDPCVSCATHVIVVDEEDKSIIAQKMVQ
>gnl|CDD|274507 TIGR03296, hypothetical_protein, M6 family metalloprotease domain. This model describes a metalloproteinase domain, with a characteristic HExxH motif. Examples of this domain are found in proteins in the family of immune inhibitor A, which cleaves antibacterial peptides, and in other, only distantly related proteases. This model is built to be broader and more inclusive than pfam05547
MVLVDFSDYPFPQQHYEDLLFGTPNGGNLGSVRDYYEEQSGGKYTVTGDVVGWYRMPHPAAYYGANNDAT
SDAGARDLVKEALAAALAQYDDFDRYDLNGDGNFDEPDLNVVHAGAGGEAGGGALGDAIWSHRWYLNGTV
VRIDGTTIGGYSWVGDYTIQPEDGGIGVFAHELGHDLGLPDLYDTQYDGGGEPVGYWSLMSSGSWAGKIG
DTPPPMSAWLKWRLGWLDPVVVDSVTGTTPVARSGGVKVLKLTVSKNPNEYLLLENRPKKGYDRALPAEG
LLIYY
>gnl|CDD|274508 TIGR03297, Ppyr-DeCO2ase, phosphonopyruvate decarboxylase. This family consists of examples of phosphonopyruvate an decarboxylase enzyme that produces phosphonoacetaldehyde (Pald), the second step in the biosynthesis phosphonate-containing compounds. Since the preceding enzymate step, PEP phosphomutase (AepX, TIGR02320) favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Pald is a precursor of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for AepX. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP)
GFDFFSGVPDSLLKPFCNYITDNNRDLRHVIAANEGAAVGLAAGAYLATGKRAAVYMQNSGLGNAVNPLT
SLADTEVYDIPLLLIVGWRGEPGVHDEPQHVKQGRITLSLLDALEIPWEVLSTDNDEALAQIERALAHAL
ATSRPYALVVRKGTFASYKLKGGPANPYATLMTREEAIAAILDHLPDNTVIVSTTGKTSRELYELRDRIG
QGHARDFLTVGSMGHASQIALGLALARPDQRVVCLDGDGAALMHMGGLATIGTQGPANLIHVLFNNGAHD
SVGGQPTVSQHLDFAQIAKACGYAKVYEVSTLEELETALTAASSANGPRLIEVKVRPGSRADLGRPTTSP
PENKRRFMRFL
>gnl|CDD|274509 TIGR03298, argP, transcriptional regulator, ArgP family. ArgP used to be known as IciA. ArgP is a positive regulator of argK. It is a negative autoregulator in presence of arginine. It competes with DnaA for oriC iteron (13-mer) binding. It activates dnaA and nrd transcription. It has been demonstrated to be part of the pho regulon (). ArgP mutants convey canavanine (an L-arginine structural homolog) sensitivity [Cellular processes, Toxin production and resistance, DNA metabolism, DNA replication, recombination, and repair, Regulatory functions, DNA interactions]
LDYRQLAALAAVVEEGSFERAAAALSVTPSAVSQRIKALEERLGQPLLVRTQPCRATEAGQRLLRHARQV
RLLEAELLAELPGLAPGAPTRLTIAVNADSLATWFLPALAPVLAREGVLLDLVVEDQDHTAELLRSGEVL
GAVTTEAKPVPGCRVVPLGAMRYLAVASPAFAARYFPDGVTAAALARAPVIVFNRKDDLQDRFLRRLFGL
PVSPPRHYVPSSEGFVDAARAGLGWGMVPELQAEPHLAAGRLVELAPGRALDVPLYWHHWRLESRLLERL
TDAVVAAARRAL
>gnl|CDD|274510 TIGR03299, LGT_TIGR03299, phage/plasmid-like protein TIGR03299. Members of this uncharacterized protein family are found in various Mycobacterium phage genomes, in Streptomyces coelicolor plasmid SCP1, and in bacterial genomes near various markers that suggest lateral gene transfer. The function is unknown [Mobile and extrachromosomal element functions, Other]
ETMAYVREPAWHGLGNHLPGRQPVEDWARAAGLDWRIEEVPVLYVWAGDGLIRPVPDQKALVRSDTGAPL
SVVSDRYQVVQPQEVLEFYEDLLGDGDFVLETAGVLKGGRKLWALARTPQTITVKGDDPVRPYLLLATAH
DGTLATTAQFTSVRVVCANTLAAALGRAGGTVVKVRHTAKFDARLDEAKQALGIVVKQFDQFAAEAKRLA
ERRVSDRQFAAFLDDVLPVPDASDRDRTNNEKARDTVTRLFAGAARLEPVRGTAWGLLQAITEYVDHVRR
VRDADSRLDSAWFGSGASLKQRALREALL
>gnl|CDD|274511 TIGR03300, assembly_YfgL, outer membrane assembly lipoprotein YfgL. Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ [Protein fate, Protein and peptide secretion and trafficking]
KRLALVLACAALLSGCSWFSSEDDEPQPAELPEFQPTVKVDQVWSASVGDGVGHYYLRLQPAVAGGKVYA
ADADGTVAALDAETGKRLWRVDLDERLSGGVGADGGLVFVGTEKGEVIALDAEDGKELWRAKLSSEVLSP
PLVANGLVVVRTNDGRLTALDAATGERLWTYSRVTPPLTLRGSASPVIADGGVLVGFAGGKLVALDLQTG
QPLWEQRVALPKGRTELERLVDVDGDPVVDGGQVYAVSYQGRVAALDLRSGRVLWKRDASSYQGPAVDDN
RLYVTDADGVVVALDRRSGSELWKNDELKYRQLTAPAVLGGYLVVGDFEGYLHWLDRDDGSFVARLKTDG
SGIASPPVVVGDGLLVQTRDGDLYAFR
>gnl|CDD|274512 TIGR03301, PhnW-AepZ, 2-aminoethylphosphonate aminotransferase. This family includes a number of 2-aminoethylphosphonate aminotransferases, some of which are indicated to operate in the catabolism of 2-aminoethylphosphonate (AEP) and others which are involved in the biosynthesis of the same compound. The catabolic enzyme (PhnW) is known to use pyruvate:alanine as the transfer partner and is modeled by the equivalog-level model (TIGR02326). The PhnW family is apparently a branch of a larger tree including genes (AepZ) adjacent to others responsible for the biosynthesis of phosphonoacetaldehyde. The identity of the transfer partner is unknown for these enzymes and considering the reversed flux compared to PhnW, it may very well be different
ILLTPGPLSTSATVRDAMLVDWCHWDSEFNDVTDQVRDRLLALAGGDDNHTCVLLQGSGTFAVEATIGSL
VPRDGKLLVLINGAYGERLAKICEYLGIPHTDLNFSEYEPPDLNRIEEALAADPDITHVATVHHETTTGI
LNPLEAIAKVARSHGAVLIVDAMSSFGAIPIDIEELDVDALIASANKCLEGVPGFGFVIARRDLLEASAG
NARSLYLDLYDQWAYMEKTGKWRFTPPTHTVYAFAQALEELEAEGGVPARIARYRRNRELLVDGLRALGF
QPLLPERWQSPIIVSFLYPDDPDFDFDDFYQELKERGFVIYPGKLTLADTFRIGTIGEIDAADIERLLEA
IKDAL
>gnl|CDD|274513 TIGR03302, OM_YfiO, outer membrane assembly lipoprotein YfiO. Members of this protein family include YfiO, a near-essential protein of the outer membrane, part of a complex involved in protein insertion into the bacterial outer membrane. Many proteins in this family are annotated as ComL, based on the involvement of this protein in natural transformation with exogenous DNA in Neisseria gonorrhoeae. This protein family shows sequence similarity to, but is distinct from, the tol-pal system protein YbgF (TIGR02795) [Protein fate, Protein and peptide secretion and trafficking]
LLLLILLLALLLLLAGCSSKKKKEADPVEEWPAEELYEEAKEALDSGDYTEAIKYFEALESRYPFSPYAE
QAQLDLAYAYYKSGDYAEAIAAADRFIRLHPNHPDADYAYYLRGLSNYNQIDRVDRDQTAAREAFEAFQE
LIRRYPNSEYAPDAKKRMDYLRNRLAGKELYVARFYLKRGAYVAAINRFQTVVENYPDTPATEEALARLV
EAYLKLGLTDLAQDAAAVLGANYPD
>gnl|CDD|274514 TIGR03303, OM_YaeT, outer membrane protein assembly complex, YaeT protein. Members of this protein family are the YaeT protein of the YaeT/YfiO complex for assembling proteins into the outer membrane of Gram-negative bacteria. This protein is similar in sequence and function to a non-essential paralog, YtfM, that is also in the Omp85 family. Members of this family typically have five tandem copies of the surface antigen variable number repeat (pfam07244), followed by an outer membrane beta-barrel domain (pfam01103), while the YtfM family typically has a single pfam07244 repeat [Protein fate, Protein and peptide secretion and trafficking]
FVVKDIRVEGLQRVSEGTVLNYLPVKVGDTISDEKIDEAIKALYATGYFEDVKIEREGGVLVIKVKERPI
INSIVFSGNKEIKKDQLKKALVGIKKGEIFNRAKLEKDEKALKEFYRSRGKYNAKVEAKVTPLPRNRVDL
EFNIKEGKKAKIKKINFVGNKAFSDSELRDVFALKESNFWSWFTGDDKYSKQKLEADLELLRSFYLNRGY
LDFKVESTQVSITPDKKGVYITYNIKEGEQYKFGEVTIEGDLIGPDEELKKLLKIKKGEVFNRSKVTKIV
KAIKDLLGEKGYAFANVNPRPQINDENKTVDLTFKVDPGKRVYVRRINISGNTRTRDEVIRRELRQLEGD
WYSLSKIKRSKRRLERLGYFETVNIETVPVGSPDQVDLNVKVKEQPTGSISFGVGYGSSSGLSFNASISE
RNFLGTGNRLSLSANKSSLSTSYSLSFTDPYFTDDGVSLGFSIFYSETDRNYKNFSDYKTKTYGGSINLG
YPITEYLRVSLGYGYEQNKIKDDSDSDSSASYFIKEQGGKFIDSSLSYGWSYDTLDSGYFPTKGSIQRLS
QEFAGPGGDLKYYKLTYDSEYYIPLSKEDDWVLSLRGRLGYGNGYGGKDLPFYERFYAGGIGSVRGFESN
GIGPRDINDSGDSIGGNAMATANVELIFPLPFLPEDNGLRGSVFFDAGNVWGTDQKKEGDYSDDSSLRAS
VGVGLRWISPMGPLRFSYAKPLKKKKGDKTQSFQFSIGTTF
>gnl|CDD|274515 TIGR03304, OMP85_target, outer membrane insertion C-terminal signal. This hidden Markov model detects a 10-residue targeting sequence common to beta-barrel outer membrane proteins (OMP) that rely on Omp85-like proteins for insertion into the outer membrane. Hits should be trusted if they include the last amino acid of a protein sequence that occurs in Gram-negative bacteria. It has been noted that Omp85 target sequences differ somewhat by species, while this model works generally for most Proteobacteria
TFYLGVRYRF
>gnl|CDD|132348 TIGR03305, alt_F1F0_F1_bet, alternate F1F0 ATPase, F1 subunit beta. A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase
GHVVAVRGSIVDVRFDGELPAIHSVLRAGREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGP
LKAPVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGK
AGLFGGAGVGKTVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPG
ARFRVGHTALTMAEYFRDDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIA
TTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERH
YDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLERFLTQPFFTTEQFTGMKGKTVSLEDA
LDGCERILNDEFQDYPERDLYMIGKIDEA
>gnl|CDD|132349 TIGR03306, altF1_A, alternate F1F0 ATPase, F0 subunit A. A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F0 subunit A of this apparent second ATP synthase
ISPDELIYWQYGFVKINATIAFTWLLMLLLVIGSWLITRRLSTGLERSRWQNLLEVLVTGIQEQISDVGL
AKPRKYLPFLGTLFLFIAVANLLSVIPGYEPPTGSLSTTAALALCVFVAVPLFGIAERGLSGYLKSYLKP
TPFMLPFNIIGELSRTLALAVRLFGNMMSGSMILAILLSISPLIFPVLMQVLGLLTGMVQAYIFSVLATV
YIAAATR
>gnl|CDD|163212 TIGR03307, PhnP, phosphonate metabolism protein PhnP. This family of proteins found in operons encoding phosphonate C-P lyase systems as is observed in E. coli and is a member of the metallo-beta-lactamase superfamily (pfam00753). As defined by this model, all instances of this protein are associated with the C-P lyase, but not all genomes containing the C-P lyase system contain phnP
AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHV
QGLFPLRWGVGEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLL
ETDGQRVAYLTDTAGLPPDTEAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTH
ISHQLDAWLMENPDLPSGVAVGYDGQTL
>gnl|CDD|132351 TIGR03308, phn_thr-fam, phosphonate metabolism protein, transferase hexapeptide repeat family. This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein
MPVLLSPEPTLHPTAELTESKLGRYTEIGERTRLREVALGDYSYVMRDCDIIYTTIGKFCSIAAMVRINA
TNHPMERPTLHHFTYRAAMYFDDASDDADFFAWRRAKRVTIGHDVWIGHGAVILPGVTIGNGAVIAAGAV
VTKDVAPYTIVAGVPAKLIRRRFPPEIAARIEALAWWDWDHETLREALPDFRDLPAEAFLDKYE
>gnl|CDD|132352 TIGR03309, matur_yqeB, selenium-dependent molybdenum hydroxylase system protein, YqeB family. Members of this protein family are probable accessory proteins for the biosynthesis of enzymes with labile selenium-containing centers, different from selenocysteine-containing proteins
VVVRGAGDLATGVAHRLHRSGFKVLMTETEQPTVIRRTVAFAEAIYTGEVTVEGVTARRISNLAEVLKLL
QQGEIPVLVDPEASVIRELKPLIVVDAILAKKNLGTRIDMAPIVIALGPGFTAGKDVHAVIETNRGHNLG
RVIYCGEALPNTGIPGEIGGYTHERVLRAPADGIVTPTKAIGDSVKKGDVIATVGDVPVVAPIDGLLRGL
IHEGLTVTEGLKIGDVDPRGEKADCTTISDKARAIGGGVLEAILML
>gnl|CDD|274516 TIGR03310, matur_MocA_YgfJ, molybdenum cofactor cytidylyltransferase. Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide
DAIILAAGLSSRMGQNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVALLANHSNITLVHNP
QYAEGQSSSIKLGLELPVQSDGYLFLLGDQPFVTPDIIQLLLEAFALKNDEIVVPLYKGKRGHPVLFPRK
LFPELLALTGDTGGRQILRELPHEVKYVEVKDPGILFDIDTPEDYQAL
>gnl|CDD|132354 TIGR03311, Se_dep_XDH, selenium-dependent xanthine dehydrogenase. Members of this protein resemble conventional xanthine dehydrogenase enzymes, which depend on molybdenum cofactor - molybdopterin bound to molybdate with two sulfur atoms as ligands. But all members of this family occur in species that contain markers for the biosynthesis of enzymes with a selenium-containing form of molybdenum cofactor. The member of this family from Enterococcus faecalis has been shown to act as a xanthine dehydrogenenase, and its activity if dependent on SelD (selenophosphate synthase), selenium, and molybdenum [Purines, pyrimidines, nucleosides, and nucleotides, Other]
YEFIVNGREVDVNEEKKLLEFLREDLRLTGVKNGCGEGACGACTVIVNGKAVRACRFTTAKLAGKEITTV
EGLTEREKDVYAWAFAKAGAVQCGFCIPGMVISAKALLDKNPNPTEAEIKKALKGNICRCTGYVKIIKAV
RLAAKAFREEIEPPRGEPKGKLGENFPRVDAVPKVLGEGVYVDDMQIEGMLYGSALRSKYPRALVKSIDI
TVALKHPGVVAVLTAKDIPGNRKIGHIFKDWPALIAVGEITRYVGDAVALVAAKSKEALREALNLIKVDY
EELPPLTSPEEALAEGAPAIHPKGNILSEEHVVRGDAEEALENSAYVVTNHYSTPFTEHAFLEPESALAV
PEGDGVIIYTSTQGVYDEQRELASLLGLPKEKIRVINKFVGGGFGGKEDMSVQHHAALLAWATKRPVKVT
LTRKESILVHPKRHAMEMTFTTGCDEAGNLTAMKADIIADTGAYASLGGPVLQRACTHAAGPYKYPNVDI
RGTAVYTNNPPAGAFRGFGVTQSNFAMECNLNLLAEKVGLSPWEIRFKNAVEPGDTLPNGQVVSEGTAIK
ETLLAVKEVYEKSPCAGIACAFKNSGVGVGIPDTGRCNLAVEDGKVHIRTSAACIGQGLGTVLTQIVCET
TGLPPEVIVCELPDTALTPDSGTTTASRQSLFTGEATRRAAAKLKEALRGRTLAELEGEEFYGEYHSITD
PLNSDKENPVSHVGYGYATQVVILDDAGKVEKVVAAYDVGRAINPLNLEGQIEGGIVMGLGYALTEDFPL
REGIPTAKFGTLGLFRSTQVPEIETHLIEKNGTPLAYGAKGVGELATIPTAPAVAGAYYRFDGKFRLSLP
LENTPYTR
>gnl|CDD|132355 TIGR03312, Se_sel_red_FAD, probable selenate reductase, FAD-binding subunit. This protein is suggested by Bebien, et al., to be the FAD-binding subunit of a molydbopterin-containing selenate reductase. Our comparative genomics suggests it to be a subunit of a selenium-dependent molybdenum hydroxylase for an unknown substrate
IEQFFRPESTIQALELKKRHTGVAVWFAGGSKLNATPTRTDKKVAISLDKLALDKIELQGGALHIGAMCH
LQSLIDNELTPAALKEALGFVYSRHIRNQATIGGEIAAFQSESLLLPVLLALKATVVLANASQMDIEDYL
ASEQRELIVEVIIPNPNLMCATRNISRSAAGLAVVTAAVAVDQKGNMRIALDGVSPVPVRLRDVEAQDLK
GEALEQAVADAIHPVADLCGSVAYKRYIAGVVVADLLAECQQLAQEA
>gnl|CDD|132356 TIGR03313, Se_sel_red_Mo, probable selenate reductase, molybdenum-binding subunit. Our comparative genomics suggests this protein family to be a subunit of a selenium-dependent molybdenum hydroxylase, although the substrate is not specified. This protein is suggested by Bebien, et al., to be the molybdenum-binding subunit of a molydbopterin-containing selenate reductase. Xi, et al, however, show that mutation of this gene in E. coli conferred sensitivity to adenine, suggesting a defect in purine interconversion. This finding, plus homology of nearby genes in a 23-gene purine catabolism region in E. coli to xanthine dehydrogase subunits suggests xanthine dehydrogenase activity
FTLNGAPQTLECKLGENVQTLLFNMGMHSVRNSDDGFGFAGSDAILFNGVLKNASLLIAAQLEGAEVRTA
ESLGQWNQLSLVQQAMVDVGVVQSGYNDPAAALILTDLLDRNTQPNRAEIDDALSGLFSRDAGYQQFYQV
IELAVKRLKDPEHKQSIAPEFRDDLTIIGKNCPKIDAAKMVQAKPCYVEDRVPADACVIKMLRSPHPHAW
ITHLDVSKAEALPGVVHVITHLNCPDIYYTPGGQSAPEPSPLDRRMFGQKMRHVGDRVAAVVAESEEIAL
HALKLIEVEYDVLTPVMSIDEAMAAEAPIVHDEPIVYGAGAPDDLEEQNANADPRGEHMIINFPIGSRPR
KNIAASVHGHIGDLNKGFAEADVIIERTYESTQAQQCPTETHICFTYMDGERLVIHASTQVPWHVRRQVA
RIVGMKQHKVHVIKERVGGGFGSKQDILLEEVCAWATWVTGRPVYFRYTREEEFICNTSRHVAKVTVKLG
AKKDGKLTAIDMDFRANTGPYGNHSLTVPSNGPALSLPLYPCDNVDFRVTTYYSNICPTGAYQGYGAPKG
NFALTMAMAELAEELGIDQLEMIETNRVHEGQELKILGAIGEGKMPTSVPKAASCALEEILRQGRELIEW
DSPKQAKGDWKIGRGVAIIMQKSGIPDIDQANCMIKLESDGTFIVHSGGADIGTGLDTVVSKLTAEVLHC
PMDDVHVISGDTDHALFDKGAYASSGTCFSGNAAKRAAENLREKILFHGAEMLGEPVADVDLAAPGLVRG
KTGEVSYFDIAHKAETGTGFGQLVGTGSYITSEFAFPYGANFAEVAVNTRTGEIRLDKFYALLDCGTPVN
PELALGQIYGATMRAIGHSMTEEIVYDDNGIPLTRDLKSYGAPKIGDIPRDFRAVLVPSDDKVGPYGAKS
ISEIGVNGAAPAIATAIHDACGVWLRDWHFTPEKILKGLNK
>gnl|CDD|132357 TIGR03314, Se_ssnA, putative selenium metabolism protein SsnA. Members of this protein family are found exclusively in genomes that contain putative set of labile selenium-dependent enzyme accessory proteins as well as homologs of a labile selenium-dependent purine hydroxylase. A mutant in this gene in Escherichia coli had improved stationary phase viability. The function is unknown
LLIGNGTAVQLDPTRPIQEGGDIAIDGDVIKAVGPTEELKQKYPEATFIDAKGKLIMPGFINTHNHFYST
FARGMMADIPPPPDFISILKNLWWRLDRALTLEDVYYSGLICSLDAIKSGCTTVIDHHASPNAITGSLST
IRKAADEAGLRTMLCYETSDRDGGKEMQEGVEENIAFIKKSSGKEPYLVEAHIGAHAPFTVSDAGLEMCR
EAVQATGRGFHIHVAEDIYDVEDSHHKYGKDIVERLADFGLLGSKTLAAHCIYLSDREIELLNETDTFVV
HNPESNMGNAVGYNPVLRMFKNGILLGLGTDGYTSDMFESLKFANFKHKDAGGDLNAAWPESPAMLFENN
NEIAERNFGAKFGRLEPGAKADLIIVDYNAPTPLTADNINGHILFGMNGGSVDSTMVNGKVVMEDREFLH
FDEAPIYARARKLAQSVWKRM
>gnl|CDD|132358 TIGR03315, Se_ygfK, putative selenate reductase, YgfK subunit. Members of this protein family are YgfK, predicted to be one subunit of a three-subunit, molybdopterin-containing selenate reductase. This enzyme is found, typically, in genomic regions associated with xanthine dehydrogenase homologs predicted to belong to the selenium-dependent molybdenum hydroxylases (SDMH). Therefore, the selenate reductase is suggested to play a role in furnishing selenide for SelD, the selenophosphate synthase
GDIMRPIPFKKLLNWIFEEYKEDGSIFGIPKRKFYRADPGKYISLFGEKLETPVGPAAGPHTQLAQNIVA
SYLTGGRFFELKTVQVLDGLDLPKPCIDAADECYNVEWSTELTVPEAYDEYVKAWFLLHLLEKEFELGDP
RGFMFNMSVGYDLAGIKSPKVDRYIEEMQDASGTPIFAECRATLKKYIDYFKKVDDEFIDAISPKVCHSV
TLSTMHGCPPDEIEAICRYLLEEKGLHTFVKLNPTLLGYKFVRDTMDEMGFDYIVLKEESFSHDLQYEDA
VAMLQRLQLLAKEKGLGFGVKLTNTLPVTIAKGELPGEEMYMSGRALFPLSINLAAKLSREFDGKLQISY
SGGADIFNIKEIFDTGIWPITMATTLLKPGGYLRLNQCANELETSEYWGMGHVDLDKLAQLAAKALTDEY
TQKEWRPVESRKLRKTLPLTDCYVAPCTTGCPINQDIPEYIRLVGEKRYLEALEVIYDKNPLPAITGTIC
DHQCQYKCTRLDYDESVNIREMKKVAAEKGYDEYKTRWHKPQGKSSAHKVAVIGAGPAGLSAGYFLARAG
HPVTVFEKKEKPGGVVKNIIPEFRISAESIQKDIELVKFHGVEFKYGCSPDLTVAELKNQGYKYVILAIG
AWKHGPLRLEGGGERVLKSLEFLRAFKEGPTINPLGKHVVVVGGGNTAMDAARAALRVPGVEKVTVVYRR
TKRYMPASREELEEALEDGVDFKELLSPESFEDGTLTCEVMKLGEPDASGRRRPVGTGETVDLPADTVIA
AVGEQVDTDLLQKNGIPLDEYGWPVVNQATGETNITNVFVIGDANRGPATIVEAIADGRKAANAILSREG
LNSDVDKVFPINEEVRLAEVYQKKGILVIDDHSCFPEQESQRCLECSYVCEKCVDVCPNRANIVIYVPGF
RDQFQIVHLDGMCNECGNCATFCPYDGAPYKDKLTLFWLEEDFYNSTNSGFLVEDPVVKICKVRLNGEVS
TIQIDDQGKENDVPEELIDLIITMVHEYHYLL
>gnl|CDD|274517 TIGR03316, aspartate/ornithine_carbamoyltransferase, knotted carbamoyltransferase YgeW. Members of this protein family include the ygeW gene product of Escherichia coli. The function is unknown. Members show homology to ornithine carbamoyltransferase (TIGR00658) and aspartate carbamoyltransferase (carbamoyltransferase), and therefore may belong to the carbamoyltransferases in function. Members often are found in a large, conserved genomic region associated with selenium-dependent molybdenum hydroxylases
IKEYIEKLNKLDFKKMYNNDFFLTWEKTDDELKAVFTVADALRALRENNISTKIFDSGLGISLFRDNSTR
TRFSFASACNLLGLEVQDLDEGKSQIAHGETVRETANMISFMADVIGIRDDMYIGKGNAYMHEVSDSVQE
GYKDGVLEQRPTLVNLQCDIDHPTQSMADMLHLIHEFGGIENLKGKKVAMTWAYSPSYGKPLSVPQGVIG
LFTRFGMDVVLAHPEGYEVMPEVEEVAKKNAAESGGSFTKTNSMAEAFKDADIVYPKSWAPFAAMEKRTN
LYGEGDFAGIDALEKELLAQNATHKDWECTEELMKTTKDGKALYLHCLPADITGVSCEEGEVEASVFDRY
RVPLYKEASYKPYIIAAMIFLSKVKNPAATLEKLEEKATPR
>gnl|CDD|274518 TIGR03317, tRNA-modifying_protein_YgfZ, folate-binding protein YgfZ. YgfZ is a protein from Escherichia coli, homologous to the glycine cleavage system T protein, or aminomethyltransferase, GcvT (TIGR00528). Homologs of YgfZ other than members of the GcvT family share a well-conserved signature region that includes the motif, KGCYxGQE. Elsewhere, sequence diverge and length variation are substantial. Members of this family are mostly bacterial, largely absent from the Firmicutes and otherwise usually present. A few eukaryotic examples are found among the Apicomplexa, and a few archaeal sequences are found. Two functions implicated for this folate-binding protein are RNA modification (a function likely to be conserved) and replication initiation (a function likely to be highly variable). Many members of this family are, at the time of construction of this model, misnamed as the glycine cleavage system T protein [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
EAWELLRIAAGIPEGGAETSGEFIPQELNLDALGGVSFDKGCYVGQEVVARMHYRGKVKRRLVPLSL
>gnl|CDD|132361 TIGR03318, YdfZ_fam, putative selenium-binding protein YdfZ. This small protein has a very limited distribution, being found so far only among some gamma-Proteobacteria. The member from Escherichia coli was shown to bind selenium in the absence of a working SelD-dependent selenium incorporation system. Note that while the E. coli member contains a single Cys residue, a likely selenium binding site, some other members of this protein family contain two Cys residues or none [Unknown function, General]
MKTYDRNRNAITTGSRVMIAGTGHTGVIKAIHTEGLTAEQARREKCVELEGCEERFAPLDLIRLG
>gnl|CDD|188306 TIGR03319, RNase_Y, ribonuclease Y. Members of this family are RNase Y, an endoribonuclease. The member from Bacillus subtilis, YmdA, has been shown to be involved in turnover of yitJ riboswitch [Transcription, Degradation of RNA]
ILLALVALIVGLIIGYLLRKRIAEKKLGSAEELAKRIIEEAKKEAETLKKEALLEAKEEVHKLRAELERE
LKERRNELQRLERRLLQREETLDRKMESLDKKEENLEKKEKELSNKEKNLDEKEEELEELIAEQREELER
ISGLTQEEAKEILLEEVEEEARHEAAKLIKEIEEEAKEEADKKAKEILATAIQRYAGDHVAETTVSVVNL
PNDEMKGRIIGREGRNIRALETLTGVDLIIDDTPEAVILSGFDPVRREIARMALEKLIQDGRIHPARIEE
MVEKATKEVDNAIREEGEQAAFDLGVHGLHPELIKLLGRLKFRTSYGQNVLQHSIEVAHLAGIMAAELGE
DVKLAKRAGLLHDIGKAVDHEVEGSHVEIGAELAKKYKESPEVVNAIAAHHGDVEPTSIEAVLVAAADAL
SAARPGARRESLENYIKRLEKLEEIANSFEGVEKSYAIQAGREIRVMVKPEKISDDQAVVLARDIAKKIE
EELEYPGQIKVTVIRETRAVEYAK
>gnl|CDD|132364 TIGR03321, alt_F1F0_F0_B, alternate F1F0 ATPase, F0 subunit B. A small number of taxonomically diverse prokaryotic species, including Methanosarcina barkeri, have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, CC and in principle may run in either direction. This model represents the F0 subunit B of this apparent second ATP synthase
MLIDWFTVIAQLINFLILVWLLKRFLYRPILDAMDAREKKIAGELADADTKKREAEQERREYEEKNEELD
QQREVLLTKAKEEAQAERQRLLDEAREEADEIREKWQEALRREQAALSDELRRRTGAEVFAIARKVLTDL
ADTDLEERMVDVFVQRLRTLDPDEKAALAEALADSGNPVLVRSAFELPEEQREQIRDTIRETLGPEIRLR
FQTEPDLIGGIELTAGGHKLAWSVDDYLESLEEDVD
>gnl|CDD|132365 TIGR03322, alt_F1F0_F0_C, alternate F1F0 ATPase, F0 subunit C. A small number of taxonomically diverse prokaryotic species, including Methanosarcina barkeri, have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F0 subunit C of this apparent second ATP synthase
DSLTIIAVASIVTAGLTIAIGSIGPALGEGRAVAQALTALAQQPDASNTITRTLFVGLAMIESTAIYCFV
VSMILIFANPFWNHAL
>gnl|CDD|274519 TIGR03323, alt_F1F0_F1_gam, alternate F1F0 ATPase, F1 subunit gamma. A small number of taxonomically diverse prokaryotic species, including Methanosarcina barkeri, have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 gamma subunit of this apparent second ATP synthase
LRRKIESAADLQSVVRTMKALAAVSIRQYEDAVRALDDYYRTVELGLAVCLRRIPLAALSPSGPNQKVSG
HTGAIVFGSDQGLVGQFNEVILTFAAEELARLPGEATIWAVGERVASRLEDSGLTIGELFRLPNSVGAIT
PLVSELLIEVEARREQGQLAELYLFFNRPSSGGSYEPTCQRLLPLDETWQRQLATQQWPTKCLPELMGEP
EETFSALIREYLFVSLFRACAESLASENASRLAAMQRAEKNIDELLDDLNRRFHRLRQSAIDEELFDVVS
GFEAL
>gnl|CDD|132367 TIGR03324, alt_F1F0_F1_al, alternate F1F0 ATPase, F1 subunit alpha. A small number of taxonomically diverse prokaryotic species, including Methanosarcina barkeri, have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 alpha subunit of this apparent second ATP synthase
LTEVLDKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDE
VGVVLLGEYSHLQAGDEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRA
PVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVA
NLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRP
PGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQNISAYIPTNLISITDGQIYLSPTLFE
LGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEHGRRIRACL
KQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDEDREQIL
DIARGAL
>gnl|CDD|132368 TIGR03325, Cis-23-dihydrobiphenyl-23-diol_dehydrogenase, cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase. Members of this family occur as the BphD protein of biphenyl catabolism and as the TodD protein of toluene catabolism. Members catalyze the second step in each pathway and proved interchangeable when tested; the first and fourth enzymes in each pathway confer metabolic specificity. In the context of biphenyl degradation, the enzyme acts as cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (EC 1.3.1.56), while in toluene degradation it acts as cis-toluene dihydrodiol dehydrogenase
MRLKGEVVLVTGGASGLGRAIVDRFVAEGARVAVLDKSAAGLQELEAAHGDAVVGVEGDVRSLDDHKEAV
ARCVAAFGKIDCLIPNAGIWDYSTALVDIPDDRIDEAFDEVFHINVKGYLLAVKAALPALVASRGSVIFT
ISNAGFYPNGGGPLYTAAKHAVVGLVKELAFELAPYVRVNGVAPGGMSSDLRGPKSLGMADKSISTVPLG
DMLKSVLPIGRMPDAEEYTGAYVFFATRGDTVPATGAVLNYDGGMGVRGFFE
>gnl|CDD|188307 TIGR03326, rubisco_III, ribulose bisphosphate carboxylase, type III. Members of this protein family are the archaeal, single chain, type III form of ribulose bisphosphate carboxylase, or RuBisCO. Members act is a three-step pathway for conversion of the sugar moiety of AMP to two molecules of 3-phosphoglycerate. Many of these species use ADP-dependent sugar kinases, which form AMP, for glycolysis [Energy metabolism, Sugars]
DFVDLNYEPSDDDLVCTFRITPAEGVSIEDAAGRVASESSIGTWTTLQPWKDPERYKDLSAKVYDIEEHG
DGSIVRIAYPLGLFEEGNLPQLLSCIAGNIFGMKAVKGLRLLDFEFPAEFLRAFKGPQFGIEGVREILGI
KDRPITATVPKPKVGLSTEEHAKVAYELWSGGVDLLKDDENLTSQAFNRFEERVEKSLKVRDKVEAETGE
KKSYLINITADVREMERRAELVADLGGEYVMVDIVVAGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNP
KHGISMFVLAKLYRLIGVDQLHTGTAGVGKLEGGNEDTKGINDFLRQDWHHIKPVFPVASGGLHPGLVPP
LIDALGTDLVIQAGGGVHGHPDGTRAGAKALRAAIDAIIEGISLEEKAKSVPELKKALEKW
>gnl|CDD|274520 TIGR03327, AMP_phos, AMP phosphorylase. This enzyme family is found, so far, strictly in the Archaea, and only in those with a type III Rubisco enzyme. Most of the members previously were annotated as thymidine phosphorylase, or DeoA. The AMP metabolized by this enzyme may be produced by ADP-dependent sugar kinases
FLKVRPIDIKSGRYAVLLNEEDAKELGVHPGDRVRIESGGKSVVGIVASTDTLVEKGEIGLSHDVLEELG
ISEGEVVEVRPAGKPESVEYIKKKMDGEKLRKDEIRAIVADIVDDKLSDIEISAFVTASYINGMDMDEIE
ALTRAMAETGDMLSFDRHPIMDKHSIGGVPGNKISLLVVPIVAAAGLTIPKTSSRAITSAAGTADVMEVL
APVEFSLDEIKRIVEKTGGCLVWGGATNLAPADDKIIKVERPLSIDPRGQMLASVMAKKGAIGADHVVID
IPVGKGAKVETVEEGRKLARDFIELGDRLGMYVECAITYGGQPIGRAIGPALEAKEALKVLEDGEGPGSL
IEKSLGLAGILLEMGGVAPRGEGKNLAKEILESGKALEKFKEIIAAQGGDPDVKPEDIQVGDKTYTITAP
TDGYVTDIDNKAITQIAREAGAPNDKGAGVYLHVKVGEKVKKGDPLYTIYAESEWRLENAIELARRLEPI
KVEG
>gnl|CDD|274521 TIGR03328, dehydratase-enolase-phosphatase_complex_1, methylthioribulose-1-phosphate dehydratase. Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine [Amino acid biosynthesis, Aspartate family]
LIEAGRDLYKRGWVPGTGGNLSARLDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGGLKPSAETLLH
TQLYRLTGAGAVLHTHSVEATVLSRLYPSNGGFELEGYEMLKGLPGITTHEDTLVVPIIENTQDIARLAD
SVAPALNAYPDVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLKL
>gnl|CDD|274522 TIGR03329, Phn_aa_oxid, putative aminophosphonate oxidoreductase. This clade of sequences are members of the pfam01266 family of FAD-dependent oxidoreductases. Characterized proteins within this family include glycerol-3-phosphate dehydrogenase (1.1.99.5), sarcosine oxidase beta subunit (1.5.3.1) and a number of deaminating amino acid oxidases (1.4.-.-). These genes have been consistently observed in a genomic context including genes for the import and catabolism of 2-aminoethylphosphonate (AEP). If the substrate of this oxidoreductase is AEP itself, then it is probably acting in the manner of a deaminating oxidase, resulting in the same product (phosphonoacetaldehyde) as the transaminase PhnW (TIGR02326), but releasing ammonia instead of coupling to pyruvate:alanine. Alternatively, it is reasonable to suppose that the various ABC cassette transporters which are also associated with these loci allow the import of phosphonates closely related to AEP which may not be substrates for PhnW
PFWLEQALALEQPDPAPPLVGDTQADVCIVGGGFTGLWTAIMIKQQRPALDVLVLEADLCGAGASGRNGG
CMLTWSTKFFTLKRLFGEAEAARLVKASEQAVLEIAAFCEQHNIDAQLRLDGTLYTATNPAQVGSMDPVV
DALERRGINSWQRLSEGELARRTGSARHLEGFYSPVAASVQPGLLVRGLRRVALELGVEIHENTPMTGLE
EGQPAVVRTPDGQVTADKVVLALNAWMASHFPQFERSIAIVSSDMVITEPAPDLLAATGLDHGTSVLDSR
IFVHYYRSTPDGRLMLGKGGNTFAYGGRMLPVFNQPSPYEALLTRSLRKFFPALAEVPIAASWNGPSDRS
VTGLPFFGRLNGQPNVFYGFGYSGNGVAPSRMGGQILSSLVLGLDNPWTRSPLVKGPLGYFPPEPIRYLG
ALVVRNAIRRKERAEDEGRRPFLLDKWLAKFAAAAGKADK
>gnl|CDD|274523 TIGR03330, SAM_DCase_Bsu, S-adenosylmethionine decarboxylase proenzyme, Bacillus form. Members of this protein family are the single chain precursor of the two chains of the mature S-adenosylmethionine decarboxylase as found in Methanocaldococcus jannaschii, Bacillus subtilis, and a wide range of other species. It differs substantially in architecture from the form as found in Escherichia coli, and lacks any extended homology to the eukaryotic form (TIGR00535) [Central intermediary metabolism, Polyamine biosynthesis]
KTLGRHLIVDLYGCDPEKLDDVEFIEEILLEAAKVAGATLVASHFHKFSPGGVSGVVLLAESHISIHTWP
EYGYAAVDVFTCGDHSDPEKAFEYLVEALKPKRVEVRELDRG
>gnl|CDD|274524 TIGR03331, SAM_DCase_Eco, S-adenosylmethionine decarboxylase proenzyme, Escherichia coli form. Members of this protein family are the single chain precursor of the S-adenosylmethionine decarboxylase as found in Escherichia coli. This form shows a substantially different architecture from the form shared by the Archaea, Bacillus, and many other species (TIGR03330). It shows little or no similarity to the form found in eukaryotes (TIGR00535) [Central intermediary metabolism, Polyamine biosynthesis]
KLKLHGFNNLTKSLSFNIYDICYAKTEEEREAYIEYIDEQYNAERLTQILTDVAEIIGANILNIARQDYE
PQGASVTILISEEPVEPEKIDNSESPGPLPDAVVAHLDKSHITVHTYPESHPDNGISTFRADIDVSTCGV
ISPLKALNYLIHSFESDIVTIDYRVRGFTRDIDGRKHFIDHKINSIQNYISEDTKEKYQMIDVNVYQENI
FHTKMMLKDFDLDNYLFGTAKEDLSPEERREITARLKKEMLEIFYGRNI
>gnl|CDD|132375 TIGR03332, salvage_mtnW, 2,3-diketo-5-methylthiopentyl-1-phosphate enolase. Members of this family are the methionine salvage pathway enzyme 2,3-diketo-5-methylthiopentyl-1-phosphate enolase, a homolog of RuBisCO. This protein family seems restricted to Bacillus subtilis and close relatives, where two separate proteins carry the enolase and phosphatase activities that in other species occur in a single protein, MtnC (TIGR01691) [Amino acid biosynthesis, Aspartate family, Central intermediary metabolism, Sulfur metabolism]
SELLATYLLHDPGHDLEKKAEQIALGLTIGSWTDLPLLKQEQLKKHKGRVVHVEELAESEHTNSYLRKKV
KRAIIKIAYPELNFSPDLPALLTTTFGKLSLDGEVKLIDLEFSDEFKRHFPGPKFGIDGIRKLLGVHERP
LLMSIFKGMIGRDLGYLKEQLRQQALGGVDLVKDDEILFETGLAPFEKRITEGKEVLQEVYEQTGHKTLY
AVNLTGRTFDLKDKAKRAAELGADVLLFNVFAYGLDVLQSLAEDDEIPVPIMAHPAVSGAYTSSPFYGFS
HSLLLGKLLRYAGADFSLFPSPYGSVALEREDALAISKELTEDDAPFKKTFAVPSAGIHPGMVPLIMRDF
GIDHIINAGGGIHGHPNGAQGGGRAFRAAIDAVLEAKPLHEKAADDIDLKLALDKWG
>gnl|CDD|213797 TIGR03333, salvage_mtnX, 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase. Members of this family are the methionine salvage enzyme MnxX, a member of the HAD-superfamily hydrolases, subfamily IB (see TIGR01488). Members are found in Bacillus subtilis and related species, paired with MtnW (TIGR03332). In most species that recycle methionine from methylthioadenosine, the single protein MtnC replaces the MtnW/MtnX pair. In B. subtilis, mtnX was first known as ykrX [Amino acid biosynthesis, Aspartate family, Central intermediary metabolism, Sulfur metabolism]
FIICDFDGTITNNDNIISIMKQFAPPEWEALKDGVLSKTLSIQEGVGRMFGLLPSSLKEEITSFVLETAE
IREGFREFVAFINEHGIPFYVISGGMDFFVYPLLEGIVEKDRIYCNEADFSNEYIHIDWPHPCDGTCQNQ
CGCCKPSLIRKLSEPNDYHIVIGDSVTDVEAAKQSDLCFARDYLLNECEELGLNHAPFQDFYDVRKELEN
VKEV
>gnl|CDD|274525 TIGR03334, Indolepyruvate_oxidoreductase_subunit_IorB, indolepyruvate ferredoxin oxidoreductase, beta subunit. This model represents the beta subunit of indolepyruvate ferredoxin oxidoreductase, an alpha(2)/beta(2) tetramer, as found in Pyrococcus furiosus and Methanobacterium thermoautotrophicum. Cofactors for the tetramer include TPP, 4Fe4S, and 3Fe-4S. It shows considerable sequence similarity to subunits of several other ketoacid oxidoreductases
YNIYITGVGGQGIILASVIIGEAALKAGLPVRAAETHGMAQRGGSVINHIRIGEVYGSMIPEGGADLLLA
FEPLEALRYLPYLSEGGEVILNTSPIPPVTVTRGLHPYPPLDEILSTLEERAGSVRAFNAEEIALEAGNI
LTLNVVMLGAASATPGFPLEEESLLESMRDSVPSKTIDVNLRAFELGFG
>gnl|CDD|132378 TIGR03335, F390_ftsA, coenzyme F390 synthetase. This enzyme, characterized in Methanobacterium thermoautotrophicum and found in several other methanogens, modifies coenzyme F420 by ligation of AMP (or GMP) from ATP (or GTP). On F420, it activates an aromatic hydroxyl group, which is unusual chemistry for an adenylyltransferase. This enzyme name has been attached to numbers of uncharacterized genes likely to instead act as phenylacetate CoA ligase, based on proximity to predicted indolepyruvate ferredoxin oxidoreductase (1.2.7.8) genes. The enzyme acts during transient exposure of the organism to oxygen [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Energy metabolism, Methanogenesis]
YFNPDIETMERGELDALVEERIRYTVHYAAEHSPFYKKWFQENNISPSDIKSHEDLLELPVISGEVIRKN
QPPVTDDFMFKSADWKDIYTIHETSGTSGTPKSFFLTWDDWKRYAEKYARSFVSQGFTAGDRMVICASYG
MNVGANTMTLAAREVGMSIIPEGKCTFPIRIIESYRPTGIVASVFKLLRLARRMKAEGIDPAESSIRRLV
VGGESFADESRNYVEELWGCEVYNTYGSTEGTMCGECQAVAGLHVPEDLVHLDVYDPRHQRFLPDGECGR
IVLTTLLKPGERCGSLLINYDTEDTTVVISRDRCPCGRTHMRILNPEREAETIWISGVPFNRVDVERAVF
QRENMDSLTGEYEAFLYGEEEGEITLRVSLECEDKDNCSIHDIQENFTGTFLKYKPELIGSYDEGIFQIL
VNFTGPGELELHKIKGRPKRLVDRR
>gnl|CDD|274526 TIGR03336, IOR_alpha, indolepyruvate ferredoxin oxidoreductase, alpha subunit. Indolepyruvate ferredoxin oxidoreductase (IOR) is an alpha 2/beta 2 tetramer related to ketoacid oxidoreductases for pyruvate (1.2.7.1, POR), 2-ketoglutarate (1.2.7.3, KOR), and 2-oxoisovalerate (1.2.7.7, VOR). These multi-subunit enzymes typically are found in anaerobes and are inactiviated by oxygen. IOR in Pyrococcus acts in fermentation of all three aromatic amino acids, following removal of the amino group by transamination. In Methanococcus maripaludis, by contrast, IOR acts in the opposite direction, in pathways of amino acid biosynthesis from phenylacetate, indoleacetate, and p-hydroxyphenylacetate. In M. maripaludis and many other species, iorA and iorB are found next to an apparent phenylacetate-CoA ligase
MKELLLGNEAIARGALEAGVGVAAAYPGTPSSEITDTLAKVAKRAGVYFEWSVNEKVAVEVAAGAAWSGL
RAFCTMKHVGLNVAADPLMTLAYTGVKGGLVVVVADDPSMHSSQNEQDTRHYAKFAKIPCLEPSTPQEAK
DMVKYAFELSEKFGLPVILRPTTRISHMRGDVELGEIPKEEVVKGFEKDPERYVMVPAIARVRHKKLLSK
QHKLREELNESPLNRLEINGAKIGVIASGIAYNYVKEALERLGVDVSVLKIGFTYPVPEGLVEEFLSGVE
EVLVVEELEPVVEEQVKALAGTAGLNIKVHGKEDGFLPREGELNPDIVVNALAKFGLAPSVTHEKPVPKP
LPVRPPSLCAGCPHRATFYAMKKVADREAIFPSDIGCYTLGIQPPLGTVDTTLCMGASIGVASGLSKAGE
KQRIVAFIGDSTFFHTGIPGLINAVYNKANITVVILDNRITAMTGHQPNPGTGVTGMGEATKEISIEELC
RASGVEFVEVVDPLNVKETIEVFKAALAAEGVSVIIAKQPCVLSNKRAGKRAGPYKVDQDKCIGCKKCIK
ELGCPAIEPEDKEAVIDPLCTGCGVCAQICPFDAI
>gnl|CDD|132380 TIGR03337, phnR, phosphonate utilization transcriptional regulator PhnR. This family of proteins are members of the GntR family (pfam00392) containing an N-terminal helix-turn-helix (HTH) motif. This clade is found adjacent to or inside of operons for the degradation of 2-aminoethylphosphonate (AEP) in Salmonella, Vibrio Aeromonas hydrophila, Hahella chejuensis and Psychromonas ingrahamii [Regulatory functions, DNA interactions]
PQYLYIKDHLSYQIRAGALLPGDKLPSERDLGERFNTTRVTIREALQQLEAEGLIYREDRRGWFVSPPRL
RYNPTRTQNFHEYVREQGREPKTELIGVTVTPAPARMAELLQLQPFDRLFLLQRLRYADGRPVCYCENYI
LPARVPGLLKEDLNGSLTEIYRNHYGLVYHSMNLRFKPTALLEEAAQALGATAGLPALHLERTNYDQHGR
VLDLDIEYWRHDALTIEVDTN
>gnl|CDD|132381 TIGR03338, phnR_burk, phosphonate utilization associated transcriptional regulator. This family of proteins are members of the GntR family (pfam00392) containing an N-terminal helix-turn-helix (HTH) motif. This clade is found adjacent to or inside of operons for the degradation of 2-aminoethylphosphonate (AEP) in Polaromonas, Burkholderia, Ralstonia and Verminephrobacter
TDAIQLLQSSSLTTLVQDEIERAILSGELPPGAKLNESDIAARLGVSRGPVREAFRALEEAGLVRNEKNR
GVFVREISLAEADEIYELRAVLDEIVGRRLAARITPTQLKVLKGLLDAMEDAAKAKDADRYARLNLRFHD
ALVEHAGNNKLTDTYRRLVKELSLFRRAALADGGAMAVSAAEHRAIVDAIASGDAERAGALMRAHVAASR
ER
>gnl|CDD|132382 TIGR03339, phn_lysR, aminoethylphosphonate catabolism associated LysR family transcriptional regulator. This group of sequences represents a number of related clades with numerous examples of members adjacent to operons for the degradation of 2-aminoethylphosphonate (AEP) in Pseudomonas, Ralstonia, Bordetella and Burkholderia species. These are transcriptional regulators of the LysR family which contain a helix-turn-helix (HTH) domain (pfam00126) and a periplasmic substrate-binding protein-like domain (pfam03466) [Regulatory functions, DNA interactions]
QLKAFHAVARCGSFTRAAERLGLSQPTVTDQVRKLEERYGVELFHRNGRRLELTDAGHRLLPIVERLFQQ
EAEAEFLLRESGALREGSLRIAATAPYYVLDLVARFRQRYPGIEVSVRIGNSQEVLQALQSYRVDVAVSS
EVVDDPRLDRVVLGNDPLVAVVHRQHPLAERESVTLEELAGQPLLMREPGSVTRQTTEEALAAAGVAPRP
ALEIGSREAIREAVLAGLGVSVVSAAEVGRDPRLRVLPIVGAEPTMDEYLYCLKERRGARLIAAFLELA
>gnl|CDD|274527 TIGR03340, phn_DUF6, phosphonate utilization associated putative membrane protein. This family of hydrophobic proteins has some homology to families of integral membrane proteins such as (pfam00892) and may be a permease. It occurs in the vicinity of various types of operons for the catabolism of phosphonates in Vibrio, Pseudomonas, Polaromonas and Thiomicrospira
LALTLVVFSALMHAGWNLMAKSHADKEPDFLWWALLAHSVLLTPYGLWYLAQVGWSRLPATFWLLLAISA
VANMVYFLGLAQAYHHADVGLVYPLARSSPLLVAIWATLTLGETLSPLAWLGILIITLGLLVLGLSRFAQ
HRRKAYGWALAAALGTAIYSLSDKAAALGVPAFYSALGYLGIGFLAMGWPFLLLYLKRHGRSMFPYARQI
LPSATLGGLMIGGAYALVLWAMTRLPVATVVALRNTSIVFAVVLGIWFLNERWYLTRLMGVCIIVAGLVV
L
>gnl|CDD|132384 TIGR03341, YhgI_GntY, IscR-regulated protein YhgI. IscR (TIGR02010) is an iron-sulfur cluster-binding transcriptional regulator (see Genome Property GenProp0138). Members of this protein family include YhgI, whose expression is under control of IscR, and show sequence similarity to IscA, a known protein of iron-sulfur cluster biosynthesis. These two lines of evidence strongly suggest a role as an iron-sulfur cluster biosynthesis protein. An older study designated this protein GntY and suggested a role for it and for the product of an adjacent gene, based on complementation studies, in gluconate utilization [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
ITITEAAQAYLAKLLAKQNEGTGIRVFVVNPGTPYAECCVSYCPPDEVEPSDIKLEFNGFSAYVDALSAP
FLEDAVIDFVTDRMGGQLTLKAPNAKMPKVADDAPLEERINYVLQSEINPQLASHGGKVTLVEITDDGVA
VLQFGGGCNGCSMVDVTLKDGVEKTLLERFPELKGVRDATDHTRGEHSYY
>gnl|CDD|213798 TIGR03342, dsrC_tusE_dsvC, sulfur relay protein, TusE/DsrC/DsvC family. Members of this protein family may be described as TusE, a partner to TusBCD in a sulfur relay system for 2-thiouridine biosynthesis, a tRNA base modification process. Other members are DsrC, a functionally similar protein in species where the sulfur relay system exists primarily for sulfur metabolism rather than tRNA base modification. Some members of this family are known explicitly as the gamma subunit of sulfite reductases
LEVNGKEIELDEDGYLLDLDDWSEDVAEALAEEEGIELTEAHWEVINFLRDFYAEYNISPAVRMLVKAMG
KKLGEEKGNSRYLYRLFPKGPAKQACKIAGLPKPTGCL
>gnl|CDD|132386 TIGR03343, 2-hydroxy-6-oxo-6-phenylhexa-24-dienoate_hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase. Members of this family are 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase, or HOPD hydrolase, the BphD protein of biphenyl degradation. BphD acts on the product of ring meta-cleavage by BphC. Many species carrying bphC and bphD are capable of degrading polychlorinated biphenyls as well as biphenyl itself
LTESSTSKFVKINEKGLSNFRIHYNEAGNGEAVIMLHGGGPGAGGWSNYYRNIGPFVDAGYRVILKDSPG
FNKSDAVVMDEQRGLVNARAVKGLMDALDIEKAHLVGNSMGGATALNFALEYPDRIGKLILMGPGGLGPS
LFAPMPMEGIKLLFKLYAEPSYETLKQMLNVFLFDQSLITEELLQGRWENIQRQPEHLKNFLISSQKAPL
STWDVTARLGEIKAKTLVTWGRDDRFVPLDHGLKLLWNMPDAQLHVFSRCGHWAQWEHADAFNRLVIDFL
RN
>gnl|CDD|213799 TIGR03344, VI_effect_Hcp1, type VI secretion system effector, Hcp1 family. This family includes Hcp1 (hemolysin coregulated protein 1), an exported, homohexameric ring-forming virulence protein from Pseudomonas aeruginosa. Hcp1 lacks a conventional signal sequence and is instead exported by means of the type VI secretion system, encoded by a pathogenicity cluster of a class previously designated IAHP (IcmF-associated homologous protein). Homologs of Hcp1, in this protein family, are found in various bacteria of which most but not all are known pathogens. Pathogens may have many multiple members of this family, with three to ten in Erwinia carotovora, Yersinia pestis, uropathogenic Escherichia coli, and the insect pathogen Photorhabdus luminescens [Cellular processes, Pathogenesis]
ANPIYLTITGKTQGLISAGCSTADSIGNKYQEGHEDEIMVLAFDHSISRPQNPQSGLPTGRVVHQPIVIT
KPIDKSSPLLYQALSSGEKLEECEIKFYRTSAAGKQELYYTIKLEGALIVDIKPYMPHCLDPNNAQPLED
VSFRYRKITWTHHIAGTSGYSSWTEP
>gnl|CDD|274528 TIGR03345, VI_ClpV1, type VI secretion ATPase, ClpV1 family. Members of this protein family are homologs of ClpB, an ATPase associated with chaperone-related functions. These ClpB homologs, designated ClpV1, are a key component of the bacterial pathogenicity-associated type VI secretion system [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPRGN
TRTPVFSPHLVELLQEAWLLASLELGDGRIRSGHLLLALLTDPELRRLLGSISPELAKIDREALREALPA
LVEGSAEASAAAADAAPAGAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNN
PILTGEAGVGKTAVVEGLALRIAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQ
PIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEP
DEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKAVSLLDTACARVALSQNATPAA
LEDLRRRIAALELELDALEREAALGADHDERLAELRAELAALEAELAALEARWQQEKELVEAILALRAEL
EADADAPADDDDALRAQLAELEAALASAQGEEPLVFPEVDAQAVAEVVADWTGIPVGRMVRDEIEAVLSL
PDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITI
NMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDG
EGREIDFKNTVILLTSNAGSDLIMALCADPETAPDPEALLEALRPELLKVFKPAFLGRMTVIPYLPLDDD
VLAAIVRLKLDRIARRLKENHGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILERLA
AGEPIERIHLDV
>gnl|CDD|274529 TIGR03346, chaperone_ClpB, ATP-dependent chaperone ClpB. Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins [Protein fate, Protein folding and stabilization]
LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKVS
GPGGQVYLSPDLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGTLGKLLKEAGATADALEAAINAVRG
GQKVTDANAEDQYEALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAI
VEGLAQRIVNGDVPEGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVG
AGKAEGAMDAGNMLKPALARGELHCIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKE
RYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRMEIDSKPEELDELDRRIIQLEIE
REALKKEKDEASKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIEQVRLELEQAEREGDL
AKAAELQYGKLPELEKQLQAAEQKLGEEQNRLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHMEE
ELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDM
SEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQG
RTVDFRNTVIIMTSNLGSDFIQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARI
VEIQLGRLRKRLAERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTI
RVDVEGGRLV
>gnl|CDD|274530 TIGR03347, VI_chp_1, type VI secretion protein, VC_A0111 family. Work by Mougous, et al. (2006), describes IAHP-related loci as a type VI secretion system (). This protein family is associated with type VI secretion loci, although not treated explicitly by Mougous, et al [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
EPHRFNFFQALRLLERLAPRRPPLGTADRPADEPVRFRQSPSLGFPPSEVAAVERDGDGRYRLTTNFLGL
LGPNGPLPLHYTELLLERERQRDHALRAFLDLFHHRLLSLFYRAWAKYRYAVQFDRGADDRFSAYLLALS
GLGLPGLRDRLALPDSALLAYAGLLAQRPRSAEGLAALLAHYFGVPVTVEEFVGRWVPIPPEQQSRLGGR
NARLGRDAVLGSRVWDRQGKFRLVIGPLDRAQYLRFLPGGELLRALRALVRFYLGDELAWDLQLVLRRDE
VPPARLGRGAARLGWTSWLG
>gnl|CDD|274531 TIGR03348, VI_IcmF, type VI secretion protein IcmF. Members of this protein family are IcmF homologs and tend to be associated with type VI secretion systems [Cellular processes, Pathogenesis]
LSLLGLILLCILIWWAGPLLAVGDYKPLESVWARLLIIAVLLLVWLLWLLIRQWRARRRNQQLLAALAAP
TKLKADAAAEAEIRELRARFNEALALLKRSRLGGRRYLYDLPWYLVIGPPGSGKTTLLQNSGLKFPLAER
LGAAALRGVGGTRNCDWWFTDEAVLIDTAGRYTTQDSDPEEDAAAWLGFLGLLRKHRRRQPLNGVVVTVS
LADLLTADPAERKAHARAIRQRLQELREQLGARFPVYLVLTKADLLAGFEEFFADLDAEEREQVWGFTFP
LDEADDDNAAEEFAAEFEGLLQRLNARLLERLHQERDAARRAAIFRFPAQLAALKDRLVQFLEEAFAANR
YEEAPLLRGVYFTSATQEGTPIDRLLGALARGFGLSPGPPAAARGEGRSYFLKDLFKEVIFPEAGLAGLN
RRAERRRRWLRRGAYAAAALAALGLLGLWSLSYLANRDYLDEVRTQLEAYRALAQAIPAAPADVLALLPA
LDALRDAPLGFGNYDEAPPLLARFGLYQGDKLGEAVRETYLRALQAVLLPRLMQRLEAQLQAQEQDPEEL
YETLKVYLMLGDPSRRDADFVKAWFASRWEQQYPGEYQRELREALLGHLRALLSLDQDAVPAFPLDDALV
EQARAELRAIPLAQRVYQRLKLQPLDAALPDLSLADALGPQADLVFERRSGKPLSLGIPGLYTRAGYHDV
FLPQIANLVERALEDAWVLGGASGNSQLSEADRQALAREVRKLYFADYINQWDALLNDLRLKPFESLAQA
AALARALASPDSPLARLLRAVARETRLTPVDGAPADGGSNAAAKKLSGLASALGAQLLPAAPGAAALPEP
GAVERHFEPLRRLLAPNGGPGAALDALLAALNELYQQLQALAASPNPGQAALKARMSGLADALSALRQAA
ARLPEPLRGWLGSLAADTWKLVLQAARSHLNARWQSEVYSFCQQAIAGRYPFSPNSSKDVPLADFERFFG
PGGLLDSFFQQNLAPFVDTSANPWRWKGGDGGSLGISPSVLAQFQRAARIRDAFFRSGGGEPAVSFTLKP
ISLDPNIRRFVLEVDGQTLRYAHGPTRPVSLTWPGPNDGGLARLTLKPADGGSPRTLTFSGPWALFRLLD
AGRLTRTGSRDRLDLRFDVGGGAVRYELRAGSADNPFTSGLLSGFRCPG
>gnl|CDD|274532 TIGR03349, IV_VI_DotU, type IV / VI secretion system protein, DotU family. At least two families of proteins, often encoded by adjacent genes, show sequence similarity due to homology between type IV secretion systems and type VI secretion systems. One is the IcmF family (TIGR03348). The other is the family described by this model. Members include DotU from the Legionella pneumophila type IV secretion system. Many of the members of this protein family from type VI secretion systems have an additional C-terminal domain with OmpA/MotB homology [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
LVTQLRATPAPPDVEALREQLVEELRLFERRLRAAGYSSEDIEAARYALCALLDEAVLNTPWGGRSVWSR
QPLLSRFHNETWGGEKFFERLERLLADPAEHLDLLELYYLCLSLGFEGKYRVEEDGREQLEALRDRLYRL
LRGARGPVPPALSPHWQGPAAARRRLRRYVPLWVILALAALVL
>gnl|CDD|274533 TIGR03350, type_VI_ompA, type VI secretion system peptidoglycan-associated domain. The flagellar motor protein MotB, the Gram-negative bacterial outer membrane protein OmpA (with an N-terminal outer membrane beta barrel domain) share a C-terminal peptidoglycan-associating homology region. This model describes a domain found fused to type VI secretion system homologs of the type IV system protein DotU (see model TIGR03349), with OmpA/MotB homology [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
RLRALLAPEIAAGLLTVDEDGDRSVVRLRGDELFASGSAEVRAEFEPLLLRIAKALAAVPGRITVVGHTD
NVPIRTARFPSNWHLSEARAKAVADVLAQAGGPAGRVRAEGRGDSEPIASNATAAGRARNRRVEIDV
>gnl|CDD|274534 TIGR03351, PhnX-like, phosphonatase-like hydrolase. This clade of sequences are the closest homologs to the PhnX enzyme, phosphonoacetaldehyde (Pald) hydrolase (phosphonatase, TIGR01422). This phosphonatase-like enzyme and PhnX itself are members of the haloacid dehalogenase (HAD) superfamily (pfam00702) having a a number of distinctive features that set them apart from typical HAD enzymes. The typical HAD N-terminal motif DxDx(T/V) here is DxAGT and the usual conserved lysine prior to the C-terminal motif is instead an arginine. Also distinctive of phosphonatase, and particular to its bi-catalytic mechanism is a conserved lysine in the variable "cap" domain. This lysine forms a Schiff base with the aldehyde of phosphonoacetaldehyde, providing, through the resulting positive charge, a polarization of the C-P bond necesary for cleavage as well as a route to the initial product of cleavage, an ene-amine. The conservation of these elements in this phosphonatase-like enzyme suggests that the substrate is also, like Pald, a 2-oxo-ethylphosphonate. Despite this, the genomic context of members of this family are quite distinct from PhnX, which is almost invariably associated with the 2-aminoethylphosphonate transaminase PhnW (TIGR02326), the source of the substrate Pald. Members of this clade are never associated with PhnW, but rather associate with families of FAD-dependent oxidoreductases related to deaminating amino acid oxidases (pfam01266) as well as zinc-dependent dehydrogenases (pfam00107). Notably, family members from Arthrobacter aurescens TC1 and Nocardia farcinica IFM 10152 are adjacent to the PhnCDE ABC cassette phosphonates transporter (GenProp0236) typically found in association with the phosphonates C-P lyase system (GenProp0232). These observations suggest two possibilities. First, the substrate for this enzyme family is also Pald, the non-association with PhnW not withstanding. Alternatively, the substrate is something very closely related such as hydroxyphosphonoacetaldehyde (Hpald). Hpald could come from oxidative deamination of 1-hydroxy-2-aminoethylphosphonate (HAEP) by the associated oxidase. HAEP would not be a substrate for PhnW due to its high specificity for AEP. HAEP has been shown to be a constituent of the sphingophosphonolipid of Bacteriovorax stolpii, and presumably has other natural sources. If Hpald is the substrate, the product would be glycoaldehyde (hydroxyacetaldehyde), and the associated alcohol dehydrogenase may serve to convert this to glycol
ISLVVLDMAGTTVDEDGLVYRALRQAVTAAGLSPTPEEVQSAWMGQSKIEAIRALLAADGADEAEAQAAF
ADFEERLAEAYDDGPPVALPGAEEAFRSLRSSGIKVALTTGFDRDTAERLLEKLGWTVGDDVDAVVCPSD
VAAGRPAPDLILRAMELTGVQDVQSVAVAGDTPNDLEAGINAGAGAVVGVLTGAHDAEELSRHPHTHVLD
SVADLPALLD
>gnl|CDD|274535 TIGR03352, VI_chp_3, type VI secretion lipoprotein, VC_A0113 family. Work by Mougous, et al. (2006), describes IAHP-related loci as a type VI secretion system (). This protein family is associated with type VI secretion loci, although not treated explicitly by Mougous, et al [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
SSAPPPKEPTYVTLTLTAAPDVNPDADGRASPVVVRVYELKSDTKFEAADFFALTEDAKKALGDDLIETD
EIILLPGEKRKITITLDEGTRYIGVVAAYRDIDNAEWRVVYKVPPKGKYTIDVMLDAQAI
>gnl|CDD|274536 TIGR03353, VI_chp_4, type VI secretion protein, VC_A0114 family. Work by Mougous, et al. (2006), describes IAHP-related loci as a type VI secretion system (). This protein family is associated with type VI secretion loci, although not treated explicitly by Mougous, et al [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
RVVWSEGMFLRPQHFQQQDRYLEHLLELRARALSPYFWGVSELEFDQDALSLGKIALTSASGIFPDGTPF
DIPGDDPLPPPLDLDPGVRTLVVYLALPLLRPGGNNVSTPERRAAQVSRYVAVEEEVRDLNSGGDEETIQ
LARLNLRLLLEGEDLSGYVSLPIARIKEVRADGGIILDPSFIPPCLSIGASPPLGQRLRELLGLLRARAE
ALAGRRRESDQQAGSADIADFLLLQLLNRYEPLLAHLLRAPQLHPEELYRELLQLAGELSTFSTESRRPR
DLPAYDHDDLGEVFAPLEDLLRELLSTVLEQRAVSLPLEERRDGIYVARLDDDRLLESARFVLAVRADMP
AEELRRQFPAQAKVGAVEQIRDLVNLALPGIPLTALPVAPRAIPYRAGYVYFELDKTGPLWQRMLRSGAI
AIHIPGDFPDLQLELWAVR
>gnl|CDD|274537 TIGR03354, VI_FHA, type VI secretion system FHA domain protein. Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
LVLTVLNAHQLTPGIAAQKTFGTNGGTIGRSEDCDWVLPDPERHVSGRHARIRYRDGAYLLTDLSTNGVF
LNGSGSPLGRGNPVRLEQGDRLRLGDYEIRVSLGDPLVSRQASESRADTSLPTAGGPPTPDPAPLAQLDP
LKALDQEPLSAADLDDLSAPLFPPLDARLPAFAAPIDAEPTMVPPFVPLPAPEPAPAPASQAPSSDAVAL
TPFLRGLGLPLELLDSQAAEDVLEELGRLLRAMVEGLLQLLRARAELKNELRLNQTTIRPAENNPLKFSA
DYDEALAVLLAPRSPGHLSAEAAIEEAFRDLRAHQVALLAAVRAALRRMLDAFSPEALEARFEQYRRSGL
LLFGGRDAWAWDMYLRYYRELRSDREQGFERLFGEDFAQAYEEALR
>gnl|CDD|274538 TIGR03355, VI_chp_2, type VI secretion protein, EvpB/VC_A0108 family. Work by Mougous, et al. (2006), describes IAHP-related loci as a type VI secretion system (). This protein family is associated with type VI secretion loci, although not treated explicitly by Mougous, et al [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
ELSLLDSILEETRLAREEEAYDRAKDGVSAFLTEALKGTVVVERDLKATIDEMIAEIDRLISRQLDAILH
APEFQQLESTWRGLKYLVDRTETRENLKIRVLNVSKEDLLKDFEDAPEFDQSGLFKKVYEEEYGTFGGEP
FGALIGDYEFSHSPQDVELLRNMSKVAAAAHAPFIAAAAPEFFGLDSFTELPNPRDLSKIFEGPEYAKWR
SFRESEDSRYVGLTLPRFLLRLPYGPKTNPVEEFNYEEDVDGNDHDKYLWGNAAYAMAARITRSFAKYGW
CTNIRGVESGGAVEDLPVHLFESDDGEVQLKCPTEVAISDRREFELAELGFIPLVHRKNSDYAAFFSAQS
VQKPKKYDNTEATANARLSARLPYIFAVSRFAHYLKVIQRDKIGSFKERADLERELNNWINQYVSDNDDP
SQEVKARRPLRAARVEVSEVPGNPGYYRAVLFLRPHFQLEGLTVSLRLVAKLP
>gnl|CDD|274539 TIGR03356, BGL, beta-galactosidase
PKDFLWGVATASYQIEGAVNEDGRGPSIWDTFSHTPGKVKDGDTGDVACDHYHRYEEDVALMKELGVDAY
RFSIAWPRIFPEGTGPVNQKGLDFYDRLVDELLEAGIEPFVTLYHWDLPQALEDRGGWLNRDTAEWFAEY
AAVVAERLGDRVKHWITLNEPWCSAFLGYGLGVHAPGLRDLRAALRAAHHLLLAHGLAVQALRANGPGAK
VGIVLNLTPVYPASDSPEDVAAARRADGLLNRWFLDPLLKGRYPEDLLEYLGDLPFVQDGDLETIAQPLD
FLGINYYTRSVVKADPGAGAGFVEVPEGVPKTAMGWEVYPEGLYDLLLRLKEDYPGPPIYITENGAAFDD
EVTDGEVHDPERIAYLRDHLAALHRAIEEGVDVRGYFVWSLLDNFEWAEGYSKRFGLVHVDYETQKRTPK
DSALWY
>gnl|CDD|274540 TIGR03357, hypothetical_protein_Atu4338, type VI secretion system lysozyme-like protein. The description for Pfam family pfam04965 cites acidic lysozyme activity for some phage-encoded members. This family represents a different subgroup of the proteins from pfam04965, where all members are associated with bacterial type VI secretion system genomic contexts
TPSLFERLPDASGESPSTRRSSAEQLRESIRRHLERLLNTRRGSCASLPDYGLPDLNDLSLSSADDRRRI
RRAIEQAIERYEPRLSRVRVTALPDEEDPLALRFRIEAELDVDGGPEPVSFDALLDPSGRYRV
>gnl|CDD|132401 TIGR03358, VI_chp_5, type VI secretion protein, VC_A0107 family. Work by Mougous, et al. (2006), describes IAHP-related loci as a type VI secretion system (). This protein family is associated with type VI secretion loci, although not treated explicitly by Mougous, et al [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
KKLSRVRKPRVQITYDVETGGAEEKVELPLVVGVLGDLSGGPTEPLTPLEERKFVEVDKDNFDEVMEAMN
PRLSFAVKNTLSDDGEELPVDLKFESMDDFSPDAVAKQVPELKKLLEAREALRDLKGPLDNNPDLRKLLQ
ELLKDKDLLEKLLSELGAK
>gnl|CDD|274541 TIGR03359, VI_chp_6, type VI secretion protein, VC_A0110 family. This protein family is associated with type VI secretion in a number of pathogenic bacteria. Mutation is associated with impaired virulence, such as impaired infection of plants by Rhizobium leguminosarum
LLKYYERELAYLRELGAEFAERYPKIAGRLGLSGEESEDPHVERLLEGFAFLTARIRQKLDDDFPELTEA
LLEVLYPHYLRPIPSMSIVQFEPDPGSLTQGVTIPRGTELTSRPVDGTRCRFRTCYDVTLWPLSITEASL
TNAPAAAPALRLPAGARSVLRLRLALLGGLDLAELDLDSLRLYLHGDPQLASALYELLFAQLVGIVIEPG
AGGRWIRLPADALRPVGFDDDEALLPYPKRSFPGYRLLQEYFAFPEKFLFFDLTGLDRALARGDGGEFEL
HFYLDERAAPLELRVDAENFRLGCTPVVNLFEQDAEPIRLDHRQTEYPLVPDRRRPDAYEVYSVDRVTGV
NRGGGEEREFPPFYSFRHGADHGRTGLYWHARREPRLRGGGPGTETFLSLVDADFEPYRPATETLSIDLT
CTNRDLPRRLPVGGINGFLTEGSPPVATVRNLRPPTRPLRPPLDGDLLWRLISHLSLNYLSLTGNGAEAL
KELLRLYDFQGSPASRRQIDGIVGIETKPVTRRVPGKGFAGFVRGLEITLTLDESAFAGGSLYLFGSVLE
RFFALYASINSFTRLVVRSSQRGELYRWPPRAGQQPLL
>gnl|CDD|132403 TIGR03360, VI_minor_1, type VI secretion-associated protein, VC_A0118 family. Members of this protein family, including VC_A0118 from Vibrio cholerae El Tor N16961, are restricted to a subset of bacteria with the type VI secretion system, and are encoded among the type VI-associated pathogenicity islands. However, many species with type VI secretion lack a member of this family. This lack suggests that members of this family may be targets rather than components of the type VI secretion system
AWELCRQEPSALERLACYDRAGAPGEAVAIEKANPYGAEWQRALAQEKGRQPESGAFLLTQEEGSGSMTL
IRTPAIGETPPPVLMISCVDNITRLQLALPKPVAGSRVQVSLDGEGATVSQSWFVRENGLLLESGRGLPA
IEEIKRLIGARRLTVRGDNGAADGLRFDLSGLNEALDPLRQQCHW
>gnl|CDD|274542 TIGR03361, VI_Rhs_Vgr, type VI secretion system Vgr family protein. Members of this protein family belong to the Rhs element Vgr protein family (see TIGR01646), but furthermore all are found in genomes with type VI secretion loci. However, members of this protein family, although recognizably correlated to type VI secretion according the partial phylogenetic profiling algorithm, are often found far the type VI secretion locus
FTLSTPLGPDALQVLSFSGDEALSRLFSFRLELVSADPDIDLEDLLGQPATLTLGRDGGGPRYFHGIVTR
FEQGGTGRRLTRYRLTLVPWLWLLTLRRDSRIFQNKSVPEIITEVLKEHGITDFRFRLSKSYPPREYCVQ
YRESDLDFVSRLLEEEGIFYYFEHTEDGHTLVLGDDASAHAPLPGASLPYNPDSGGVADRPVISQWTYRR
QVRPGQVALRDYDFKKPAASLEAQASADEQGHQAPDLEHYDYPGRFKDQERGKRLARVRLEALRADAKRA
EGESNCRRLAPGYLFTLSGHPRAALNREYLVVSVHHHGRQPQVLEESGGSGAGYRNSFQCIPATVPFRPP
RRTPKPRIDGPQTATVVGPAGEEIYTDEYGRVKVQFHWDRYGKRDEKSSCWVRVAQPWAGNGWGSVAIPR
VGQEVVVDFLEGDPDRPIVTGRVYNAENMPPYSLPANKTQSGFRSRSSKGGGGFNELRFEDKAGAEEIYL
HAQRDMNTEVENDSTHTVGNNRT
>gnl|CDD|274543 TIGR03362, VI_chp_7, type VI secretion-associated protein, VC_A0119 family. This protein family is one of two related families in type VI secretion systems that contain an ImpA-related N-terminal domain (pfam06812) [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
QRAQNEAAPAAVPTAPASAPAPATTAAAPQPPEPPASVVDDSSSERALRDTLLQVADLLLEQDPDDPRGY
RLRRTALWGTITALPMSNADGRTRLAPPPADRVADYQELLAQADWAALLQRVEQSLSLAPFWLDGQRLSA
QALERLGYAAVAQAIRDELAAFLERLPGLLELKFSDGTPFADDETRAWLAQHATRSNAASVAPVAEVGEE
SDWEELREEARALAAEGGLEAALQRLQQRLAQAREPRERFHWRLLLARLLEQAGKAELAQQLYAALDQQI
QQLGLAEWEPALALRVLQLAL
>gnl|CDD|274544 TIGR03363, VI_chp_8, type VI secretion-associated protein, ImpA family. This protein family is one of two related families in type VI secretion systems that contain an ImpA-related N-terminal domain (pfam06812)
LSLEALLAPISDDSPCGEDLEYSAEFDRLKEARREDDPELQQGDWVTELKAADWPAVERLASELLKTRSK
DLRLAAWLTEAWLQLRGLPGLADGLALVAGLLERYWDDVHPLLDDDDDEDRVARLNWLNGQSLLLLLRRT
PLTDGTSGRFSLRDYERAQVQNLARKDPDAAKRAIEEGKLSLEIFEEALRDTSPDFLQAKAQALAAALSA
LQALQALVDARLGEAAPSLSPLRKALQDLLRLVLRFAADRPQDLQEAPAAAPDASEDGGHGPAAAPATSA
NPASAARGEIASREDAIRQLLEIAEYFRRTEPHSPVPYLIERAARWGNMPLHEWLRELIKDGSALSRLQE
LLG
>gnl|CDD|132407 TIGR03364, putative_secreted_oxidoreductase, FAD dependent oxidoreductase TIGR03364. This clade of FAD dependent oxidoreductases (members of the pfam01266 family) is syntenically associated with a family of proposed phosphonatase-like enzymes (TIGR03351) and is also found (less frequently) in association with phosphonate transporter components. A likely role for this enzyme involves the oxidative deamination of an aminophosphonate differring slightly from 2-aminoethylphosphonate, possibly 1-hydroxy-2-aminoethylphosphonate (see the comments for TIGR03351). Many members of the larger FAD dependent oxidoreductase family act as amino acid oxidative deaminases
YDLIIVGAGILGLAHAYAAARRGLSVTVIERSSRAQGASVRNFGQVWPTGQAPGPAWDRARRSREIWLEL
AAKAGIWVRENGSLHLARTEEELAVLEEFAATREPAEYRVELLTPAEVAAKFPALRLDGLRGGLHSPDEL
RVEPREAIPALAAYLAEQHGVEFHWNTAVTSVETGTVRTSRGDVHADQVFVCPGADFETLFPELFAASGV
RRCKLQMMRTAPQPRLPLGTALLTGLSLRRYEGFAELPSAAALKARLQEEEPELLEWGIHLMVSQNPDGE
LIIGDSHEYGLAPDPFDDEEIDNLILAEAKTILGLPDLDIVERWQGVYASSPPAPIFLERPDDGVTVVVV
TSGAGMTLSFGLAEE
>gnl|CDD|274545 TIGR03365, Bsubt_queE, 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE. This uncharacterized enzyme, designated QueE, participates in the biosynthesis, from GTP, of 7-cyano-7-deazaguanosine, also called preQ0 because in many species it is a precursor of queuosine. In most Archaea, it is instead the precursor of a different tRNA modified base, archaeosine [Protein synthesis, tRNA and rRNA base modification]
KKIPVLEIFGPTIQGEGMVIGQKTMFVRTAGCDYRCSWCDSAFTWDGSAKDDWRPMTAEEIWQELKALGG
GTFLHVTLSGGNPALQKPLGELIDLLHEKGYRFALETQGSVWQDWFTDIDDLTLSPKPPSSGMETDWQKL
DDCIERLGPGPQISLKVVVFDDADYAYAKTVHARYPHLPFYLQPGNHTPPPSDDDDLIDGLLDRMEWLVD
KVAADREWFDVRVLPQLHTLLWGNKRGV
>gnl|CDD|274546 TIGR03366, HpnZ_proposed, putative phosphonate catabolism associated alcohol dehydrogenase. This clade of zinc-binding alcohol dehydrogenases (members of pfam00107) are repeatedly associated with genes proposed to be involved with the catabolism of phosphonate compounds
VLGHEIVGEVVALRGGFTPADDGVPLRLGQRVVWSVTVPCGRCFRCRRGLTAKCDSLRKYGHEAMDSGWP
LSGGYAEHCVLPAGTPVVPVPDDLPDAVAAPAACATATVMAALEAAGDLKGRRVLVVGAGMLGLTAAAAA
AEAGASRVVVADPNADRRELALSFGATALAEDEVLAERQGGLQNGRGVDVALEFSGMTAAVNACLESLDV
GGCLVLAGSVAPGGPVALDPEQLVRRWLTIRGVHNYEPRHLDQAVRFLARTGQRFPWEKLVGKPFPLDEV
>gnl|CDD|274547 TIGR03367, queuosine_QueD, queuosine biosynthesis protein QueD. Members of this protein family, closely related to eukaryotic 6-pyruvoyl tetrahydrobiopterin synthase enzymes, are the QueD protein of queuosine biosynthesis. Queuosine is a hypermodified base in the wobble position of tRNAs for Tyr, His, Asp, and Asn in many species. This modification, although widespread, appears not to be important for viability. The queuosine precursor made by this enzyme may be converted instead to archeaosine as in some Archaea [Protein synthesis, tRNA and rRNA base modification]
ITKEFTFDAAHRLPGYPGKCARLHGHTYKVEVTVSGEVLDEAGMVMDFSDLKAIVKEVVDRLDHALLNDV
LGLENPTAENLARWIYDRL
>gnl|CDD|132411 TIGR03368, cellulose_yhjU, cellulose synthase operon protein YhjU. This protein was identified by the partial phylogenetic profiling algorithm () as part of the system for cellulose biosynthesis in bacteria, and in fact is found in cellulose biosynthesis gene regions. The protein was designated YhjU in Salmonella enteritidis, where disruption of its gene disrupts cellulose biosynthesis and biofilm formation () [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
GGWNLYFILKFALFWAGYLNFHPLLNLAFAAFLLLPIPNRWLRILRQFIAVPAGIALLYRDSWLPPLDRL
WSQGGQLQGFSLGYLVELLGRFVNWQMLLAIFVVLVAYLLLNQWIRVTTFVVAALIALSLWQALSPTLAV
TVANAQAQAQSAGAAATAPPTDANLNAALNAFFAQEAQRVVTFPALLADPAQQFDLLVLNICSLSWDDLE
AAGLRNHPLLSRFDILFDNFNSATSYSGPAAIRLLRASCGQESHADLYDPAPEQCHLFSNLAKLGFTENL
LLNHDGHFDNFLQLVRENGGMQSPLMSQTGLPVAQRSFDGSPIYDDYAVLNRWLQERLGEPDGPVALYYN
TISLHDGNRIPNSGMTSLASYPLRAKKLLDDLDRFFDELEKSGRKVVVVLVPEHGAALRGDKMQISGLRE
IPSPSITHVPVGVKFFGLGAPRRGATVTITAPSSYLALSELVSRLVAGSPFAPGSVDLAKLVSDLPQTQM
VAENEGTVVMQYQGKPYVRLPGGDWVEY
>gnl|CDD|274548 TIGR03369, cellulose_bcsE, cellulose biosynthesis protein BcsE. This protein, called BcsE (bacterial cellulose synthase E) or YhjS, is required for cellulose biosynthesis in Salmonella enteritidis. Its role is this process across multiple bacterial species is implied by the partial phylogenetic profiling algorithm. Members are found in the vicinity of other cellulose biosynthesis genes. The model does not include a much less well-conserved N-terminal region about 150 amino acids in length for most members. Solano, et al. suggest this protein acts as a protease [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
RPLLARFHRLFAGLASLQQQQGQYLWDVDFWRSKTGVAANEVLMLRFDDNGWLLAQAEEPASLASSGAPL
SDEDRVLVSRAALEGGPPLPEHWQIVDDNDALVAAASGAHAATVVLSCTGTTQLEQLAAQVHALRRQCGS
ALKIVVREMKECLRQQDERLLLQLGANLVVPRNTPFSRMLSLIESLQGQVFSRPIPADYESLLSAVLPTA
AKGYLPPDTFCSYVRKVLERSLVLQLSGVLVKLRLLPGIRHADALRLCHIRRAGDLCTAGNNSLYLFLFA
CRLNDVDIALNHIFKLPVSDLFSSRTVCSDNGSILAELKQLE
>gnl|CDD|132413 TIGR03370, VPLPA-CTERM, VPLPA-CTERM protein sorting domain. A probable protein export sorting signal, PEP-CTERM, was described by Haft, et al. (). It is predicted to interact with a putative transpeptidase we designate exosortase. This model describes a variant with conserved motif VPLPA, rather than VPEP. It appears to be the recognition sequences for exosortase D (TIGR04152). This variant is found prominently in two members of the Rhodobacterales, namely Jannaschia sp. CCS1 and Roseobacter denitrificans OCh 114. One interesting member protein has a full-length duplication and therefore two copies of this putative sorting domain
VPLPAGALLLLAGLGGLGAMRRRRR
>gnl|CDD|274549 TIGR03371, cellulose_yhjQ, cellulose synthase operon protein YhjQ. Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMDWSVRDGWARALLNGADWAA
AAYRSPDGVLFLPYGDLSADEREAYQAHDAGWLARLLQQLDLAARDWVLIDLPRGPSPITRQALAAADLV
LVVVNADAACYATLHQLALALFAGSGPRDGPRFLINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDEA
VSEALARGTPVLNYAPHSQAAHDIRTLAGWLLSKLS
>gnl|CDD|132415 TIGR03372, Putrescine_aminotransferase, putrescine aminotransferase. Members of this family are putrescine aminotransferase, as found in Escherichia coli, Erwinia carotovora subsp. atroseptica, and closely related species. This pyridoxal phosphate enzyme, as characterized in E. coli, can act also on cadaverine and, more weakly, spermidine [Central intermediary metabolism, Polyamine biosynthesis]
ANALACSAHALHLIEKDTLDHDDMAALNQEVIECFKEHVNPGFLEYRKSVTAGGDYGAVEWQAGGLNTLI
DTQGNEFIDCLGGFGIFNVGHRNPNVIAAVENQLAKQPLHSQELLDPLRALLAKTLAALTPGKLKYSFFC
NSGTESVEAALKLAKAYQSPRGKFTFIAASGAFHGKSLGALSATAKPAFRKPFMPLLPGFHHVAFGDIEA
MLKALNECKKTGDDVAAIILEPIQGEGGVILPPEGYLPAVRALCDEFGALLILDEVQTGMGRTGKMFACE
HEGVQPDILCLAKALGGGVMPIGATIATEAVFSVLFDNPFLHTTTFGGNPLACAAALATINELLEKNLPA
QAAIKGDFLLDGFQQLAAEYPDLIIEARGKGLLMAIEFRDNEIGYAFAKELFQQNILVAGTLNNAKSIRI
EPPLTITIEQCALVIKAAKDAL
>gnl|CDD|132416 TIGR03373, VI_minor_4, type VI secretion-associated protein, BMA_A0400 family. Members of this protein family are found exclusively, although not universally, in bacterial species that possess a type VI secretion system. Genes are found in type VI secretion-associated gene clusters. The specific function is unknown. This model represents the rather well-conserved amino-terminal domain of a protein family in which carboxy-terminal regions, when present, show little conservation [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
GYFGKLPARGDFVKRALPHQFAQPWDRWLQAGLAASRQQLGDDWKDAYLTAPVWRFALAPGARGGQALAG
VLIPSRDRVGRYFPLTVAAALPAAAPLTFLLLSPDAWFGQVEALLLSSLDAEADVGALLEALAALP
>gnl|CDD|132417 TIGR03374, ABALDH, 1-pyrroline dehydrogenase. Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family
QHKLLINGELVSGEGEKQPVYNPATGEVILEIAEASAEQVDAAVRAADAAFAEWGQTTPKARAECLLKLA
DVIEENAQVFAELESRNCGKPLHSVFNDEIPAIVDVFRFFAGAARCLSGLAAGEYLEGHTSMIRRDPLGV
VASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVNILFGRGKTVGDPL
TGHEKVRMVSLTGSIATGEHILSHTAPSIKRTHMELGGKAPVIVFDDADIDAVVEGVRTFGFYNAGQDCT
AACRIYAQRGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVMKAVEEAKALGHIKVITGGE
KRKGNGYYFAPTLLAGAKQDDAIVQKEVFGPVVSITSFDDEEQVVNWANDSQYGLASSVWTKDVGRAHRL
SARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHIMVK
>gnl|CDD|274550 TIGR03375, type_I_sec_LssB, type I secretion system ATPase, LssB family. Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
LLDCLLLLARHYGRPVSREALVAGLPLEDGRLTPELLPRAARRAGLSARLVKRSLDDISPLLLPAILLLK
DGRACVLLGIDEDGKARVLLPETGDGEQELSLDALEALYSGYAIFVRPQFRFDARADELISPRPKHWFWS
TLKESWPLYRDVLIASLLINLLALASPLFVMNVYDRVVPNQAFETLWVLAIGVALAIVFDFVLKTLRSYF
LDVAGKKADLILSAKLFERVLGLRMEARPASVGSFANQLREFESVRDFFTSATLTALIDLPFALLFLLVI
AIIGGPLVWVPLVAIPLILLPGLLLQRPLSRLAEESMRESAQRNAVLVESLSGLETIKALNAEGRFQRRW
EQTVAALARSGLKSRFLSNLATNFAQFIQQLVSVAIVVVGVYLISDGELTMGGLIACVMLSGRALAPLGQ
LAGLLTRYQQAKTALQSLDELMQLPVERPEGTRFLHRPRLQGEIEFRNVSFAYPGQETPALDNVSLTIRP
GEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIA
LGAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTS
AMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVLEALRKGR
>gnl|CDD|274551 TIGR03376, Glycerol-3-phosphate_dehydrogenase, glycerol-3-phosphate dehydrogenase (NAD(+)). Members of this protein family are the eukaryotic enzyme, glycerol-3-phosphate dehydrogenase (NAD(+)) (EC 1.1.1.8). Enzymatic activity for 1.1.1.8 is defined as sn-glycerol 3-phosphate + NAD(+) = glycerone phosphate + NADH. Note the very similar reactions of enzymes defined as EC 1.1.1.94 and 1.1.99.5, assigned to families of proteins in the bacteria
RVAVVGSGNWGTAIAKIVAENARALPELFEESVRMWVFEEEIEGRNLTEIINTTHENVKYLPGIKLPANL
VAVPDLVEAAKGADILVFVIPHQFLEGICKQLKGHVKPNARAISCIKGLEVSKDGVKLLSDIIEEELGIP
CGVLSGANLANEVAKEKFSETTVGYRDPADFDVDARVLKALFHRPYFRVNVVDDVAGVEIAGALKNVVAI
AAGFVDGLGWGDNAKAAVMRRGLLEMIKFARMFFPTGEVTFTFESCGVADLITTCLGGRNFKVGRAFAKT
GKSLEELEKELLNGQSLQGVATAKEVHELLKNKNKDDEFPLFEAVYQILYEGLPPKKLPECL
>gnl|CDD|274552 TIGR03377, glycerol3P_GlpA, glycerol-3-phosphate dehydrogenase, anaerobic, A subunit. Members of this protein family are the A subunit, product of the glpA gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase [Energy metabolism, Anaerobic]
MRDLALRGLRCILLEQGDLAHGTTGRNHGLLHSGARYAVTDQESARECIEENRILKRIARHCVEDTGGLF
ITLPEDDLEFQKQFLAACREAGIPAEEIDPAEALRLEPNLNPDLIGAVKVPDGTVDPFRLVAANVLDAQE
HGARIFTYTKVTGLIREGGRVTGVKVEDHKTGEEERIEAQVVINAAGIWAGRIAEYAGLDIRMFPAKGAL
LIMNHRINNTVINRCRKPSDADILVPGDTISIIGTTSERIDDPDDLPVTQEEVDVLLREGAKLAPMLAQT
RILRAFAGVRPLVAVDDDPSGRNISRGIVLLDHAERDGLPGFITITGGKLTTYRLMAEWATDVVCKKLGN
DRPCRTADEPLPGSEDPTAVKTLKKLISLPSPIAGSAVYRHGERAPQVLKDNRLDNQVICECEMVTAGEV
EYAIRELDVNNLVDLRRRTRLGMGTCQGEFCAYRAAGLLSREGLIDPEQSTELLREFLEERWKGIRPILW
GDALREAELTYWIYQGLFGLEHLPAD
>gnl|CDD|213807 TIGR03378, glycerol3P_GlpB, glycerol-3-phosphate dehydrogenase, anaerobic, B subunit. Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase [Energy metabolism, Anaerobic]
FDVIIIGGGLAGLSCALRLAEAGKKCAIIAAGQSALHFSSGSLDLLSRLPDGQAVEQPMDALEALAQQAP
EHPYSKLGKTKVLALLQWFERLLKAQGLPLVGQSELNHWRLTPLGTLRATWLSPPFVPTVPLNDAFPHDR
ILLVGIEGFRDFQPQLAADNLKQHPQFAHCEITTAELELPQLDELRRNPREFRSVDIARLLDKEENFNAL
ADELSRLANGADLVVLPACFGLGDGLELLRELEQATGLTLCELPTMPPSLLGIRLEEALKHRFEQLGGVM
LPGDRVLRAEFEGNRVTRIHTRNHRDIPLRADHFVLASGSFFSNGLVAEFDKIYEPIFGLDVLQLPDRDQ
WYQHRFFAPHPFMQFGVKTDAQLRPSRGGQTIENLYAIGAVLGGYDPIFEGCGSGVAVSTALHAAEQIL
>gnl|CDD|132422 TIGR03379, glycerol3P_GlpC, glycerol-3-phosphate dehydrogenase, anaerobic, C subunit. Members of this protein family are the membrane-anchoring, non-catalytic C subunit, product of the glpC gene, of a three-subunit, FAD-dependent, anaerobic glycerol-3-phosphate dehydrogenase. GlpC lasks classical hydrophobic transmembrane helices; Cole, et al suggest interaction with the membrane may involve amphipathic helices. GlcC has conserved Cys-containing motifs suggestive of iron-sulfur binding. This complex is found mostly in Escherichia coli and closely related species [Energy metabolism, Anaerobic]
DTSFESCIKCTVCTVYCPVAKANPLYPGPKQAGPDGERLRLKSAELYDEALKYCTNCKRCEVACPSDVKI
GDIIARARNKYQKKKPNIKKLRDFVLSHTDLMGSISTPFAPIVNAITGLKPVKKLLDKTLGVSKHRTLPK
YSFGTFRRWYKKNATSQALYERQVAYFHGCYVNYNHPQLGKDLVKVLNAMNIGVQLLEKEKCCGVPLIAN
GFPDKAKKQAQFNVKQIEAMVDENGIPVISTSSTCSFTLRDEYPHVLGVDNAKVRDHIELVTRFLYRLFM
EGKTPPMKPLPLKVAYHTPCHMEKMGWAPYTLELLKMIPGLEVVVLDSQCCGIAGTYGFKSENYETSQAI
GKSLFDQIEQSGADYVITDCETCKWQIEMSTSLECIHPISLLAMALA
>gnl|CDD|132423 TIGR03380, Putative_agmatine_deiminase, agmatine deiminase. Members of this family are agmatine deiminase (3.5.3.12), as characterized in Pseudomonas aeruginosa and plants. Related deiminases include the peptidyl-arginine deiminase (3.5.3.15) as found in Porphyromonas gingivalis [Central intermediary metabolism, Polyamine biosynthesis]
TTPKQDGFRMPAEFEPQAQCWMIWPERPDNWRNGAKPAQKAFAEVAEAIAEFEPVTMLVSPAQYENARAQ
LPSNIRVVEMSSNDAWMRDTGPTFVVNDKGEIRGVDWEFNAWGGLVDGLYFPWDKDDLVARKVCELEGID
RYRADFVLEGGSIHVDGEGTLLTTEECLLSEGRNPHLTKEQIEEKLKDYLGVEKVIWLPDGLYNDETNGH
VDNLCCFVRPGEVALSWTDDESDPQYEISKEAYDVLSNTTDAKGRKLKVHKLPIPGPLYITEEEAAGVDP
VEGTLPREAGERLAASYVNFYIANGGIILPLFDDPNDKLAQQQLQELFPDRKVVGVPAREILLGGGNIHC
ITQQQPA
>gnl|CDD|274553 TIGR03381, putative_carbon-nitrogen_hydrolase, N-carbamoylputrescine amidase. Members of this family are N-carbamoylputrescine amidase (3.5.1.53). Bacterial genes are designated AguB. The AguAB pathway replaces SpeB for conversion of agmatine to putrescine in two steps rather than one [Central intermediary metabolism, Polyamine biosynthesis]
VTVAALQMACSDDVETNIARAERLVREAAARGAQIILLPELFEGPYFCKDQDEDYFALAQPVEGHPAIKR
FQALAKELGVVIPVSFFEKAGNAYYNSLAMIDADGSVLGVYRKSHIPDGPGYQEKFYFRPGDTGFKVWDT
RYGRIGVGICWDQWFPETARAMALMGAEVLFYPTAIGSEPHDPDLDSRDHWQRVMQGHAAANLVPVVAAN
RIGTEIGDGGEQTFYGSSFIADHTGELVAEAGRSEEAVLVATFDLDEIAKQRAAWGFFRDRRPELYGPL
>gnl|CDD|213808 TIGR03382, GC_trans_RRR, Myxococcales GC_trans_RRR domain. The domain described here is small (about 30 amino acids), hydrophobic, only moderately conserved, and similar to numerous other transmembrane helix-containing sequence regions from convergent evolution. This domain is found, once per protein but in many proteins per genome in several bacteria of the order Myxococcales. It begins with a signature Gly-Cys motif. Its other features, including a hydrophobic transmembrane helix, Arg-rich cluster, and location at the protein C-terminus, resemble the PEP-CTERM proposed protein targeting domain
GCSAAGGAGGLLALALLALAALLRRRR
>gnl|CDD|274554 TIGR03383, Structure_Of_Uricase, urate oxidase. Members of this protein family are urate oxidase, also called uricase. This protein contains two copies of the domain described by the uricase model pfam01014. In animals, this enzyme has been lost from primates and birds [Central intermediary metabolism, Other]
ELGQNRYGKAEVRVLRVHRDPLTHTIKELNVSVLLRGDFEASYTEGDNSDVVATDTQKNTVYALAKEHGI
TSIEEFAIYLAKHFLDTYSHVTGARVEIEEYPWERIEVDGKPHDHSFVRSGGETRTAEVTVDRGGTLQIT
SGIKDLTVLKTTGSGFVGFIRDEYTTLPETTDRILATDVTARWRYNNFEDATGVDFDAAYEQVRDILLDT
FAETYSPSVQNTLYLMGKAVLERFPEVEEVSLSMPNKHYFLVDLSPFGLENNGEVYTPADEPYGLIEATV
TR
>gnl|CDD|132427 TIGR03384, betaine_BetI, transcriptional repressor BetI. BetI is a DNA-binding transcriptional repressor of the bet (betaine) regulon. In sequence, it is related to TetR (pfam00440). Choline, through BetI, induces the expression of the betaine biosynthesis genes betA and betB by derepression. The choline porter gene betT is also part of this regulon in Escherichia coli. Note that a different transcriptional regulator, ArcA, controls the expression of bet regulon genes in response to oxygen, as BetA is an oxygen-dependent enzyme [Regulatory functions, DNA interactions]
PKVGMEPIRRAELIDATIESIGERGSLDVTIAQIARRAGVSSGIISHYFGGKQGLLEATMRHLLSELRAA
VVARLAKASSPRERLEAIVEANFDDSQFSPPAMKAWLAFWAEAMHSPQLARLQRINSRRLHSNLMSELRQ
LLPREQAERAAEGLAALIDGLWLRAALSDGPLDAAEARALARDYLDTLL
>gnl|CDD|163244 TIGR03385, Coenzyme_A_disulfide_reductase, CoA-disulfide reductase. Members of this protein family are CoA-disulfide reductase (EC 1.8.1.14), as characterized in Staphylococcus aureus, Pyrococcus horikoshii, and Borrelia burgdorferi, and inferred in several other species on the basis of high levels of CoA and an absence of glutathione as a protective thiol [Cellular processes, Detoxification]
SAASRVRRLDKESDIIVFEKTEDVSFANCGLPYVIGGVIDDRNKLLAYTPEVFIKKRGIDVKTNHEVIEV
NDERQTVVVRNNKTNETYEESYDYLILSPGASPIVPNIEGINLDIVFTLRNLEDTDAIKQYIDKNKVENV
VIIGGGYIGIEMAEALRERGKNVTLIHRSERILNKLFDEEMNQIVEEELKKHEINLRLNEEVDSIEGEER
VKVFTSGGVYQADMVILATGIKPNSELAKDSGLKLGETGAIWVNEKFQTSVPNIYAAGDVAESHNIITKK
PAWVPLAWGANKMGRIAGENIAGNDIEFKGVLGTNITKFFDLTIASTGVTENEAKKLNIDYKTVFVKAKT
HANYYPGNSPLHLKLIYEKDTRRILGAQAVGKEGADKRIDVLAAAIMAGLTVKDLFFFELAYAPPYSRVW
DPLNMAG
>gnl|CDD|274555 TIGR03388, L-ascorbate_oxidase, L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases
IRHYKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLHTEGVVIHWHGIRQIGTPWA
DGTAGVTQCAINPGETFIYNFVVDRPGTYFYHGHYGMQRSAGLYGSLIVDVPDGEKEPFHYDGEFNLLLS
DWWHKSIHEQEVGLSSKPMRWIGEPQSLLINGRGQFNCSLAAKFSSTNLPQCNLKGNEQCAPQILHVEPG
KTYRLRIASTTALAALNFAIEGHKLTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQDPSRNYWISVG
VRGRKPNTPPGLTVLNYYPNSPSRLPPTPPPVTPAWDDFDRSKAFSLAIKAAMGSPKPPETSDRRIVLLN
TQNKINGYTKWAINNVSLTLPHTPYLGSLKYNLLNAFDQKPPPENYPRDYDIFKPPPNPNTTTGNGIYRL
KFNTTVDVILQNANTLNGNNSETHPWHLHGHDFWVLGYGEGKFRPGVDEKSYNLKNPPLRNTVVIFPYGW
TALRFVADNPGVWAFHCHIEPHLHMGMGVVFAEGVEKVGKLPKEALGCGLT
>gnl|CDD|274556 TIGR03389, laccase_11, laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate
AEVRHYTFDVQEKNVTRLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQYNVTIHWHGVRQLRNGW
ADGPAYITQCPIQPGQSYVYNFTITGQRGTLWWHAHISWLRATVYGAIVILPKPGVPYPFPKPDREVPII
LGEWWNADVEAVINQANQTGGAPNVSDAYTINGHPGPLYNCSSKDTFKLTVEPGKTYLLRIINAALNDEL
FFAIANHTLTVVEVDATYTKPFKTKTIVIGPGQTTNVLLTADQSPGRYFMAARPYMDAPGAFDNTTTTAI
LQYKGTSNSAKPILPTLPAYNDTAAATNFSNKLRSLNSAQYPANVPVTIDRRLFFTIGLGLDPCPNNTCQ
GPNGTRFAASMNNISFVMPTTALLQAHYFGISGVFTTDFPANPPTKFNYTGTNLPNNLFTTNGTKVVRLK
FNSTVELVLQDTSILGSENHPIHLHGYNFFVVGTGFGNFDPKKDPAKFNLVDPPERNTVGVPTGGWAAIR
FVADNPGVWFMHCHLEVHTTWGLKMAFLVDNGKGPNQSLLPPPSDLPSC
>gnl|CDD|132431 TIGR03390, hypothetical_protein_CHGG_08781, L-ascorbate oxidase, fungal type. This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized
VVHDDSFQPDHILRVTSDNIKIACSSRYSVVVNGTSPGPEIRLQEGQTTWIRVYNDIPDNNVTMHWHGLT
QRTAPFSDGTPLASQWPIPPGHFFDYEIKPEPGDAGSYFYHSHVGFQAVTAFGPLIVEDCEPPPYKYDDE
RILLVSDFFSATDEEIEQGLLSTPFTWSGETEAVLLNGKSGNKSFYAQINPSGSCMLPVIDVEPGKTYRL
RFIGATALSLISLGIEDHENLTIIEADGSYTKPAKIDHLQLGGGQRYSVLFKAKTEDELCGGDKRQYFIQ
FETRDRPKVYRGYAVLRYRSDKASKLPSVPETPPLPLPNSTYDWLEYELEPLSEENNQDFPTLDEVTRRV
VIDAHQNVDPLNGRVAWLQNGLSWTESVRQTPYLVDIYENGLPATPNYTAALANYGFDPETRAFPAKVGE
VLEIVWQNTGSYTGPNGGVDTHPFHAHGRHFYDIGGGDGEYNATANEAKLENYTPVLRDTTMLYRYAVKV
VPGAPAGWRAWRIRVTNPGVWMMHCHILQHMVMGMQTVWVFGDAEDIV
>gnl|CDD|274557 TIGR03391, FeS_syn_CsdE, cysteine desulfurase, sulfur acceptor subunit CsdE. Members of this protein family are CsdE, formerly called YgdK. This protein, found as a paralog to SufE in Escherichia coli, Yersinia pestis, Photorhabdus luminescens, and related species, works together and physically interacts with CsdA (a paralog of SufS). CsdA has cysteine desulfurase activity that is enhanced by this protein (CsdE), in which Cys-61 (numbered as in E. coli) is a sulfur acceptor site. This gene pair, although involved in FeS cluster biosynthesis, is not found next to other such genes as are its paralogs from the Suf or Isc systems [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
IAPHPFGTEITAADLIATFAACRQWEDRYRQLILLAKQLPALPEALKTQATELTGCENRVWLGHQVLPDG
TLHFYGDSEGRIVRGLLAVLLTAVEGKTPEQLLAQDPLALFDELGLRAQLSASRSNGLAALAAAIQNIA
>gnl|CDD|274558 TIGR03392, FeS_syn_CsdA, cysteine desulfurase, catalytic subunit CsdA. Members of this protein family are CsdS. This protein, found Escherichia coli, Yersinia pestis, Photorhabdus luminescens, and related species, and related to SufS, works together with and physically interacts with CsdE (a paralog of SufE). CsdA has cysteine desulfurase activity that is enhanced by CsdE, a sulfur acceptor protein. This gene pair, although involved in FeS cluster biosynthesis, is not found next to other such genes as are its paralogs from the Suf or Isc systems [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
FNPAQFRRQFPALQDATVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVA
QLLNAPDAENIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIG
ADLLPDIDQLPELLTPRTRILALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDI
DFYAFSGHKLYGPTGIGVLYGKTELLEAMPPWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLS
AALEWLADIDINAAESWSVSLATLAEEALAQLPGFRSFRCQGSSLLAFDFAGVHHSDLVTLLAEQGIALR
AGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGRALELLVD
>gnl|CDD|274559 TIGR03393, Indole-3-pyruvate_decarboxylase, indolepyruvate decarboxylase, Erwinia family. A family of closely related, thiamine pyrophosphate-dependent enzymes includes indolepyruvate decarboxylase (EC 4.1.1.74), phenylpyruvate decarboxylase (EC 4.1.1.43), pyruvate decarboxylase (EC 4.1.1.1), branched-chain alpha-ketoacid decarboxylase, etc.. Members of this group of homologs may overlap in specificity. Within the larger family, this model represents a clade of bacterial indolepyruvate decarboxylases, part of a pathway for biosynthesis of the plant hormone indole-3-acetic acid. Typically, these species interact with plants, as pathogens or as beneficial, root-associated bacteria [Central intermediary metabolism, Other]
YTVGDYLLDRLTDIGIDHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNAAYAADGYARCKGAAALLTT
FGVGELSAINGIAGSYAEHLPVIHIVGAPGTAAQQRGELLHHTLGDGDFRHFYRMAAEVTVAQAVLTEQN
ATAEIDRVITTALRERRPGYLMLPVDVAAKAVTPPVNPLVTHKPAHADSALRAFRDAAENKLAMAKRVSL
LADFLALRHGLKHALQKWVKEVPMPHATLLMGKGILDEQQAGFYGTYSGSASTGAVKEAIEGADAVICVG
VRFTDTITAGFTHQLTPEQTIDVQPHAARVGNVWFTGIPMNDAIETLVELCEHAGLMWSSSGAIPFPQPD
ESRSALSQENFWQTLQTFLRPGDIILADQGTSAFGAADLRLPADVNFIVQPLWGSIGYTLPAAFGAQTAC
PNRRVILLIGDGSAQLTIQELGSMLRDKQHPIILVLNNEGYTVERAIHGAEQRYNDIALWNWTHLPQALS
LDPQSECWRVSEAEQLADVLEKVAAHERLSLIEVVLPKADIPPLLGALT
>gnl|CDD|274560 TIGR03394, Indole-3-pyruvate_decarboxylase, indolepyruvate/phenylpyruvate decarboxylase, Azospirillum family. A family of closely related, thiamine pyrophosphate-dependent enzymes includes indolepyruvate decarboxylase (EC 4.1.1.74), phenylpyruvate decarboxylase (EC 4.1.1.43), pyruvate decarboxylase (EC 4.1.1.1), branched-chain alpha-ketoacid decarboxylase, etc.. Members of this group of homologs may overlap in specificity. This model represents a clade that includes a Azospirillum brasilense member active as both phenylpyruvate decarboxylase and indolepyruvate decarboxylase
KLAEALLRALKDRGAQEMFGIPGDFALPFFKVIEETGILPLHTLSHEPAVGFAADAAARYRGTLGVAAVT
YGAGAFNMVNAIAGAYAEKSPVVVISGAPGTTEGNAGLLLHHQGRTLDSQFQVFKEVTCDQAVLDDPATA
PAEIARVLGSARELSRPVYLEIPRDMVNAEVEPVPDDPAWPVDRDALDACADEVLARMRSATSPVMMVCV
EVRRYGLEAKVAELAQRLGVPVVTTFMGRGLLADAPTPPLGTYLGVAGDAELSRLVEESDGLLLLGVILS
DTNFAVSQRKIDLRRTIHAFDRAVTLGYHVYADIPLAGLVDALLALLDGLPPSDRTTRGKGPHAYPRGLQ
ADAEPIAPMDIARAVNDRFARHGQMPLAADIGDCLFTAMDMDDAGLMAPGYYAGMGFGVPAGIGAQCTSG
KRILTLVGDGAFQMTGWELGNCRRLGIDPIVILFNNASWEMLRVFQPESAFNDLDDWRFADMAAGMGGDG
VRVRTRAELAAALDKAFATRGRFQLIEAMLPRGVLSDTLARFVQG
>gnl|CDD|132436 TIGR03395, Sphingomyelinase_C, sphingomyelin phosphodiesterase. Members of this family are bacterial proteins that act as sphingomyelin phosphodiesterase (EC 3.1.4.12), also called sphingomyelinase. Some members of this family have been shown to act as hemolysins [Cellular processes, Pathogenesis]
IKILSHNVYMLSTNLYPNWGQMERADLIASADYIKNQDVVILNEAFDTSASKRLLDNLREEYPYQTDVIG
RSKKGWDKTLGNYSSSALEDGGVAIVSKWPIEEKIQYIFNKGCGADNLSNKGFAYVKINKNGKKFHVIGT
HLQAQDSMCSKLGPASIRANQLNEIQDFIDSKNIPKDETVLIGGDLNVNKGSNEYHDMFKTLNVSEPRYV
GVPATWDATTNSIAKYYYPKEEPEYLDYIFVSKSHAQPPVWQNKVLDPKSVTSWFKKYTYDDFSDHYPVY
GFI
>gnl|CDD|274561 TIGR03396, PC_PLC, phospholipase C, phosphocholine-specific, Pseudomonas-type. Members of this protein family are bacterial, phosphatidylcholine-hydrolyzing phospholipase C enzymes, with a characteristic domain architecture as found in hemolytyic (PlcH) and nonhemolytic (PlcN) secreted enzymes of Pseudomonas aeruginosa. PlcH hydrolyzes phosphatidylcholine to diacylglycerol and phosphocholine, but unlike PlcN can also hydrolyze sphingomyelin to ceramide ((N-acylsphingosine)) and phosphocholine. Members of this family share the twin-arginine signal sequence for Sec-independent transport across the plasma membrane. PlcH is secreted as a heterodimer with a small chaperone, PlcR, encoded immediately downstream [Cellular processes, Pathogenesis]
TRRDFLKLAAAGGAAAAAAALPPSIRRALAIPANRRTGTIQDVEHVVILMQENRSFDHYFGTLRGVRGFG
DRRPIPLPDGKPVWYQPNAKGETVAPFHLDTSKTNAQRVGGTPHSWSDAHAAWNNGRMDRWPAAKGPLTM
GYYKREDIPFQYALADAFTICDAYHCSVQGGTNPNRLYLWTGTNGPLGGAGGPVTTNDDDWDGIGPGEGG
YTWTTYPERLEQAGVSWKVYQDMNDNFTDNPLAGFKQFRNASSDNPGSPLYLGARGMSTRDLLDQLRADV
QAGTLPQVSWIVAPAAYSEHPGSSPAQGAWYVSRVLDALTANPEVWSKTVLLLNYDENDGFFDHVPPPVP
PSYNADGTSAGKSTLDTAGEYFTVPDPAGARGRPIGLGPRVPMYVISPWSKGGWVNSQVFDHTSVLRFLE
KRFGVREPNISPWRRAVCGDLTSAFDFSRPDTTPFPALPDTSADYAVAAAALIPKYPPPPPATQQMPAQE
KGTRPARALPYELHVDARVDRAGGTLALTFANTGTAGAVFHVYDRLHLDGIPRRYTVEAGKQLDDSWDAV
SDAGGAYDLWVLGPNGFLREFRGNAAAAAGAVPEVRVCYDVANGNLYLTLSNAGRSPVTVTVTDNAYGGA
GPRTVTVAPGQRVELHWDLSASGGWYDFTVTADGDAGFLRRLAGRVETGKPSISDPAMG
>gnl|CDD|274562 TIGR03397, acid_phos_Burk, acid phosphatase, Burkholderia-type. A member of this family, AcpA from Burkholderia mallei, has been charactized as a surface-bound glycoprotein with acid phosphatase activity, as can be shown with the colorigenic substrate 5-bromo-4-chloro-3-indolyl phosphate. This family shares regions of sequence similarity with phosphocholine-preferring phospholipase C enzymes (TIGR03396) from many of the same species
VKNVVVIYAENRSFDNLYGNFPGANGLSNASPESKAQRDRDGTPLPTLPPIWGGLTVGGVTPPVEEAFTE
NLPNAPFALDDPNGENLPLSVVTRDLWHRFYQNQMQINGGRNDKFAAWADSGALVMGYYAQDASKLPMWK
LAQQYTLADNFFMGAFGGSFLNHQYLICACAPFYPDADKSPAKSSISVLDGDGPKGTRLKPADNSPASAL
DGPPKFVNDGNLTPDGYAVNTMQPPYQPSGIRPAEGGDPLYADPAKPNTLPPQTQATIGDRLSAKGVSWA
WYAGAWQAALDHGKGGSIPNFQYHHQPFNYFANYAPGTPARAEHLRDGGLGDESFIAAIDAGKLPQVSFY
KPQGNLNEHAGYADVAAGDRHIADVIAHLQKSPQWKNMVVIVTYDENGGFWDHVAPPKGDRWGPGTRIPA
IVVSPFAKKGYVDHTPYDTTSILRFITRRFGLPPLPGVKARDRALAARGAKPMGDLTNALDLN
>gnl|CDD|132439 TIGR03398, plc_access_R, phospholipase C accessory protein PlcR. The class of microbial phosphocholine-preferring phospholipase C enzymes described by model TIGR03396 has two members in Pseudomonas aeruginosa, one of which (PlcH) is hemolytic and can hydrolyzes sphingomyelin as well as phosphatidylcholine. This model describes PlcR, an accessory protein for PlcH with which it forms a heterodimer. The member of the family from P. aeruginosa, although not the members from various Burkholderia species, is encoded immediately downstream of phospholipase C
FRDQLAAYGRNRNSMPAAERAALARGLLAQLPRHVARGEIDPRQAEALSAALLPDAEADARTREAAIFSM
RMQLDDYAVQTVGPSPAEEPQYLEYAQQSRKVIAEVQASVPDPEQQQAAIDQRLQALRVQIFGEASPSLL
Q
>gnl|CDD|274563 TIGR03399, RNA_3'-terminal_phosphate_cyclase, RNA 3'-phosphate cyclase. Members of this protein family are RNA 3'-phosphate cyclase (6.5.1.4), an enzyme whose function is conserved from E. coli to human. The modification this enzyme performs enables certain RNA ligations to occur, although the full biological roll for this enzyme is not fully described. This model separates this enzyme from a related protein, present only in eukaryotes, localized to the nucleolus, and involved in ribosomal modification [Transcription, RNA processing]
IEIDGSYGEGGGQILRTALSLSALTGKPVRIYNIRANRPKPGLAPQHLTAVKAAAEICNAEVEGAELGST
ELEFIPGKIRGGDYRFDIGTAGSVTLVLQTLLPALLFANGPSRVTVSGGTDVPWAPPVDYLRNVFLPLLE
RMGIRAELELLRRGFYPRGGGEVRLRVEPVKKLKPLELEERGELLRVSGIAHAANLPAHVAERMAKAARE
ELRKLGLDPEIEIEVLDKGLGPGSGIVLWAETEHCRLGFSALGEKGKSAEKVGEEAAEQLLAELRSGAAV
DEHLADQLILYMALASGESRFTTSELTMHLRTNIWVIEQFLPVRFE
>gnl|CDD|274564 TIGR03400, 18S_RNA_Rcl1p, 18S rRNA biogenesis protein RCL1. Members of this strictly eukaryotic protein family are not RNA 3'-phosphate cyclase (6.5.1.4), but rather a homolog with a distinct function, found in the nucleolus and required for ribosomal RNA processing. Homo sapiens has both a member of this RCL (RNA terminal phosphate cyclase like) family and EC 6.5.1.4, while Saccharomyces has a member of this family only
LRFEGSRNFRQRLVLSTLSGKPVRITKIRSDDENPGLRDYEVSFLRLLEKVTNGSKIEISYTGTTVIYKP
GLITGGSVTHECPTSRGIGYYLEPLLLLAPFSKKPLSITLKGITNSTGDPSVDTIRTATLPLLKKFGIPD
EGLELKILKRGAPPLGGGEVELRCPVIKQLKTIHLTERGRVKRIRGVAYSTRVSPSLANRMIDAARGVLN
NLLPDVYITTDVWKGKNSGKSPGYGLSLVAETTNGCIISAEAVSSPGEPSLPEDLGKRAAYLLLEEIYKG
GCVDSTHQPLALLLMALGQEDVSKLRLGKLSEYTVEFLRDIKEFFGVTFKLKDDKSDNGSGKVLLTCVGI
GYTNVSKKIA
>gnl|CDD|188314 TIGR03401, Uncharacterized_protein_YFL061W/YNL335W, HD domain protein, cyanamide hydratase family. Members of this protein family are known, so far, in the Ascomycota, a branch of the Fungi, and contain an HD domain (pfam01966), found typically in various metal-dependent phosphohydrolases. The only characterized member of this family, from the soil fungus Myrothecium verrucaria, is cyanamide hydratase (EC 4.2.1.69), a zinc-containing homohexamer that adds water to the fertilizer cyanamide (NCNH2), a nitrile compound, to produce urea (NH2-CO-NH2). Homologs are likely to be nitrile hydratases
SKYGFTAVPRDAKAAISTVPKVKPPPAQSVEDTPLPDTPLVKFAQEYAKARLPPETYNHSLRVYYYGLAI
ARDQFPEWDLSDETWFLTCLLHDIGTTDENMTATKMSFEFYGGILALDVLKEQTGANQDQAEAVAEAIIR
HQDLGVDGTITTLGQLLQLATIFDNVGANTDLVHPDTVDAVNEAYPRHGWSSCFASTIRKENELKPWCHT
TALGDDFPKKVLANTLMY
>gnl|CDD|132443 TIGR03402, Cysteine_desulfurase_NifS, cysteine desulfurase NifS. Members of this protein family are NifS, one of several related families of cysteine desulfurase involved in iron-sulfur (FeS) cluster biosynthesis. NifS is part of the NIF system, usually associated with other nif genes involved in nitrogenase expression and nitrogen fixation. The protein family is given a fairly broad interpretation here. It includes a clade nearly always found in extended nitrogen fixation genomic regions, plus a second clade more closely related to the first than to IscS and also part of NifS-like/NifU-like systems. This model does not extend to a more distantly clade found in the epsilon proteobacteria such as Helicobacter pylori, also named NifS in the literature, built instead in TIGR03403
IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTE
SDNTAIKSALAAQPEKRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALV
SVMWANNETGTIFPIEEIGEIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYI
RKGTRFRPLLRGGHQERGRRAGTENVPGIVGLGKAAELATEHLEEENTRVRALRDRLEAGLLARIPDARL
NGDPTKRLPNTVNISFEYIEGEAILLLLDMEGICASSGSACTSGSLEPSHVLRAMGVPHTAAHGSIRFSL
SRYNTEEDIDYVLEVLPPIIARLRAMSPF
>gnl|CDD|132444 TIGR03403, nifS_epsilon, cysteine desulfurase, NifS family, epsilon proteobacteria type. Members of this family are the NifS-like cysteine desulfurase of the epsilon division of the Proteobacteria, similar to the NifS protein of nitrogen-fixing bacteria. Like NifS, and unlike IscS, this protein is found as part of a system of just two proteins, a cysteine desulfurase and a scaffold, for iron-sulfur cluster biosynthesis. This protein is called NifS by Olsen, et al. (), so we use this designation
VYLDNNATTMLDPKVKELMDPFFCDIYGNPNSLHQFGTATHPAIAEALDKLYKGINARDLDDIIITSCAT
ESNNWVLKGVYFDEILKGGKNHIITTEVEHPAVRATCAFLESLGVEVTYLPINEQGTITAEQVREAITEK
TALVSVMWANNETGMIFPIKEIGEICKERGVLFHTDAVQAIGKIPVDVQKAGVDFLSFSAHKFHGPKGVG
GLYIRKGVELTPLFHGGEHMGGRRSGTLNVPYIVAMGEAMRLANEYLDFEKSHVRRLRDRLEDALLELPD
VFVVGDREHRVPNTILISIKGVEGEAMLWDLNKAGIAASTGSACASEDLEANPVMVAIGADKELAHTAIR
LSLSRFTTEEEIDYTIEVFKKAVQRLRAISSS
>gnl|CDD|274565 TIGR03404, Oxalate_decarboxylase_OxdC, bicupin, oxalate decarboxylase family. Members of this protein family are defined as bicupins as they have two copies of the cupin domain (pfam00190). Two different known activities for members of this family are oxalate decarboxylase (EC 4.1.1.2) and oxalate oxidase (EC 1.2.3.4), although the latter activity has more often been found in distantly related monocupin (germin) proteins
GGLGATDPGPRNLARDKQNPDILAPPTTDHGSVPNLKWSFSDSHNRLENGGWAREVTVRDLPISTAIAGV
NMRLEPGAIRELHWHKEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGLDEGCEFL
LVFDDGNFSEDGTFLVTDWLAHTPKDVLAKNFGVPESAFDNLPLKELYIFPGTVPGPLDEEAVTGPAGEV
PGPFTYHLSEQKPKQVPGGTVRIADSTNFPVSKTIAAAIVTVEPGAMRELHWHPNADEWQYFIQGQARMT
VFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDETLVFLEVFKADRFADVSLNQWLALTPPQLVAAHLN
LDDEVIDSLKKEKQPVV
>gnl|CDD|274566 TIGR03405, iron-containing_alcohol_dehydrogenase, phosphonate metabolism-associated iron-containing alcohol dehydrogenase. This small clade of iron-containing alcohol dehydrogenases of the pfam00465 family is found in genomic contexts indicating a role in the metabolism of phosphonates. In Delftia acidovorans SPH-1, the gene ZP_01580650.1 is adjacent to and running in the same direction as ZP_01580649.1 encoding the enzyme phosphonatase (PhnX, TIGR01422). Upstream are also found genes encoding components of a phosphonate ABC transport complex. In Ralstonia eutropha H16 and Verminephrobacter eiseniae EF01-2 the dehydrogenase is followed by a homolog of the PhnB gene, a putative phosphonate-specific MFS-type transporter. In Azoarcus BH72 the gene is preceded by Phosphoenolpyruvate phosphomutase (aepX) and a putative phosphonopyruvate decarboxylase (aepY), two genes involved in the biosynthesis of phosphonoacetaldehyde (Pald). Ususally these two are accompanied by a specific transaminase, AepZ, which converts Pald to 2-aminoethylphosphonate (2-AEP). 2-hydroxyethylphosphonate (2-HEP), the presumed product of the reaction of Pald with an alcohol dehydrogenase, is a biologically novel but reasonable analog of 2-AEP and may be a constituent of as-yet undescribed natural products. In the case of Azoarcus, downstream of the dehydrogenase is a CDP-glycerol:glycerophosphate transferase homolog that may indicate the existence of a pathway for 2-HEP-derived phosphonolipid biosynthesis
YHNPVRIHFGAGSLALAPQLLHGRRVVVVTFPEARALGLARRLEALLGGRLAALIDDVAPNPDVAQLDGL
YARLWGDEGACDLVIALGGGSVIDTAKVLAVGLRRGEFDLLLQLLRNGRDFAPTARLPLVAIPTTAGTGS
EVTPWATVWDAENSKKYSLHLPFTYPEAAIVDAALMLSLPREHTLSTGLDALSHALESIWNVNANPVSRG
LAIQAAADISRALPEVLAQPGDLALRSDMALAALKAGLAFSNTKTALAHSISYEMTLRHGVPHGIACSFT
LPTVLRTALGRNPSRDALLQAVFGDTASAPARLRAFLDTLGVKTRFADYGVSRDEARRMVGEAFDGARGK
NFIGA
>gnl|CDD|213809 TIGR03406, FeS_long_SufT, probable FeS assembly SUF system protein SufT. The function is unknown for this protein family, but members are found almost always in operons for the the SUF system of iron-sulfur cluster biosynthesis. The SUF system is present elsewhere on the chromosome for those few species where SUF genes are not adjacent. This family shares this property of association with the SUF system with a related family, TIGR02945. TIGR02945 consists largely of a DUF59 domain (see pfam01883), while this protein is about double the length, with a unique N-terminal domain and DUF59 C-terminal domain. A location immediately downstream of the cysteine desulfurase gene sufS in many contexts suggests the gene symbol sufT. Note that some other homologs of this family and of TIGR02945, but no actual members of this family, are found in operons associated with phenylacetic acid (or other ring-hydroxylating) degradation pathways [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
VVLRRDVKARLVPSGDPITLPAGTEVTITQALGGNFTVVVEGNMARIDGKDADALGKEPPPPLDLPENAD
GEDNEDQVWEQLRTVYDPEIPVNIVDLGLVYGCRVEKLGEGQFRVDIEMTLTAPGCGMGPVLVEDVEDKV
LAVPNVDEVEVELVFDPPWSREMMSEAAKLELGM
>gnl|CDD|132448 TIGR03407, urea_ABC_UrtA, urea ABC transporter, urea binding protein. Members of this protein family are ABC transporter substrate-binding proteins associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. Members of this protein family tend to have the twin-arginine signal for Sec-independent transport across the plasma membrane [Transport and binding proteins, Amino acids, peptides and amines]
IKVGILHSLSGTMAISETTLKDAELMAIEEINASGGVLGKKIEPVVEDGASDWPTFAEKARKLITQDKVA
AVFGCWTSASRKAVLPVFEENNGLLFYPVQYEGEECSPNIFYTGAAPNQQIIPAVDYLLSKKGAKRFFLL
GSDYVFPRTANKIIKAYLKSLGGTVVGEDYTPLGHTDFQTIINKIKAFKPDVVFNTLNGDSNVAFFKQLK
NAGITAKDVPVVSFSVAEEEIRGIGPENLVGHLAAWNYFQSVDTPANKKFVKAFKAKYGDDRVTNDPMEA
AYLGVYLWKAAVEKAGSFDVDAVRDAAIGIEFDAPEGKVKVDGKNHHLTKTVRIGEIRADGQFDVVWESD
GPVEPDPWS
>gnl|CDD|132449 TIGR03408, urea_trans_UrtC, urea ABC transporter, permease protein UrtC. Members of this protein family are ABC transporter permease proteins associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity [Transport and binding proteins, Amino acids, peptides and amines]
PFHLSDFRLNLLGKYLCYAIVALGIDLIWGYTGILSLGQGVFFGLGGYAMAMYLKLQASGEGTTGLPDFM
LWNGVTELPWFWQPFASFPFALLAVVLVPGLLAFLLGYFVFRSRIKGVYFSIITQALALALALLFVGQQT
GTGGTNGLTDFKTLLGFDLSSDSTKRALYFLTAALLALAFLLCRWLVRSRFGRVLIAIRDAENRVRFLGY
DPANYKVFVFVLSAGIAGIAGALYVPQVGIISPSEMGIVPSIEMVIWVAVGGRGTLIGAVLGALLVNYAK
TFFSEAFPEAWLYILGALFVVVVLFLPKGLAGL
>gnl|CDD|200272 TIGR03409, urea_trans_UrtB, urea ABC transporter, permease protein UrtB. Members of this protein family are ABC transporter permease proteins associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity [Transport and binding proteins, Amino acids, peptides and amines]
ADQLFSGLSLGSILLLAALGLAITFGQMGVINMAHGEFIMIGAYTTYVVQQLFSSPGLADLYLLIAIPLA
FLVSALLGALIERTVIRHLYGRPLDTLLATWGISLILQQAVRSIFGAPNVPVTAPEWLSGGLEITGALSL
PYNRLFIIVLALAVLLALALLLYRTRLGLRVRAVTQNRSMAAALGINTRRVDALTFALGSGIAGVAGVAL
TLIGNVGPTLGQLYIVDSFLVVVFGGVGSLWGTVVAAFGLGVLNKILEYFTGASLAKVLVLVLIILFLQW
RPQGLFALKGR
>gnl|CDD|274567 TIGR03410, urea_trans_UrtE, urea ABC transporter, ATP-binding protein UrtE. Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity [Transport and binding proteins, Amino acids, peptides and amines]
LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH
ERARAGIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQL
AIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV
VASGAGDELDEDKVRRYLAV
>gnl|CDD|274568 TIGR03411, urea_trans_UrtD, urea ABC transporter, ATP-binding protein UrtD. Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity [Transport and binding proteins, Amino acids, peptides and amines]
PILYLEGLSVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTMMDVITGKTRPDEGSVLFGGTDLTGLP
EHQIARAGIGRKFQKPTVFENLTVFENLELALPRDKSVFASLFFRLSAEEKDRIEEVLETIGLADEADRL
AGLLSHGQKQWLEIGMLLMQDPKLLLLDEPVAGMTDEETEKTAELLKSLAGKHSVVVVEHDMEFVRSIAD
KVTVLHQGSVLAEGSLDQVQADPRVIEVYLGR
>gnl|CDD|132453 TIGR03412, iscX_yfhJ, FeS assembly protein IscX. Members of this protein family are YfhJ, a protein of the ISC system for iron-sulfur cluster assembly. Other genes in the system include iscSUA, hscBA, and fdx [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
KWTDSQEIAIALAEAHPDVDPKTVRFTDLHQWVLELPGFDDDPKRCNEKILEAIQMAWIDERE
>gnl|CDD|274569 TIGR03413, GSH_gloB, hydroxyacylglutathione hydrolase. Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753) [Cellular processes, Detoxification]
IIPIPALSDNYIWLLHDPDGQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAP
VYGPAEERIPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRLFEGT
PEQMYDSLQRLAALPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLER
ATNPFLRADDPAVRAALGSQGADPVEVFAALRAWKDNF
>gnl|CDD|188316 TIGR03414, ABC_choline_bnd, choline ABC transporter, periplasmic binding protein. Partial phylogenetic profiling () vs. the genome property of glycine betaine biosynthesis from choline consistently reveals a member of this ABC transporter periplasmic binding protein as the best match, save for the betaine biosynthesis enzymes themselves. Genomes often carry several paralogs, one encoded together with the permease and ATP-binding components and another encoded next to a choline-sulfatase gene, suggesting that different members of this protein family interact with shared components and give some flexibility in substrate. Of two members from Sinorhizobium meliloti 1021, one designated ChoX has been shown experimentally to bind choline (though not various related compounds such as betaine) and to be required for about 60 % of choline uptake. Members of this protein have an invariant Cys residue near the N-terminus and likely are lipoproteins [Transport and binding proteins, Amino acids, peptides and amines]
AAEPASCKTVRFADVGWTDITATTAVASVLLEGLGYQPKVTTLSVPITYAGLKNGDLDVFLGNWMPAMEP
DIKPYLEAGSVEVLGPNLEGAKYTLAVPTYVADAGVKSFADIAKFKDKLDGKIYGIEPGNDGNRLIQKMI
DKNAFGLGGFKLVESSEAGMLAQVARAVKRKEWIVFLGWEPHPMNTNFKMTYLTGGDDYFGPNYGGATVY
TNTRKGYAAECPNVGKLLTNLTFTLDMENQLMGAILNDGKDPEAAARQWLKANPEVLDPWLAGVTTVDGK
DGLAAVKAAL
>gnl|CDD|188317 TIGR03415, ABC_choXWV_ATP, choline ABC transporter, ATP-binding protein. Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines [Transport and binding proteins, Amino acids, peptides and amines]
IRFKNVDIVFGDQPDEALALLDQGKTREEILDRTGLVLGVHNASLDIEEGEICVLMGLSGSGKSTLLRAV
NGLNPVSRGSVLVKDGDGSVDVANCDAATLRRLRTHRVSMVFQQFALLPWRTVEENVAFGLEMQGMPKAE
RRKRVDEQLELVGLAQWADRKPGELSGGMQQRVGLARAFATEAPILLMDEPFSALDPLIRTQLQDELLEL
QSKLKKTIVFVSHDLDEALKIGNRIAIMEGGRIIQHGTPEEIVLNPANDYVADFVAHTNPLNVLTARDLM
RPLTTLEKVDGEWCVSKRYDTWLKTADKQVRRAAAGLPVAAWAAEQEVESLEKLPTVINPDTPMRDVLAA
RHRTGGAILLVENGRIVGVIGDQNIYHALLGH
>gnl|CDD|188318 TIGR03416, ABC_choXWV_perm, choline ABC transporter, permease protein
DHKIPIGAWAKSFVDWLTDNGAFFFDALAAVLESMIDGLLDLLQAPPPLLLIAIFAALAWWLQRSWSLAL
FVLLGLLLIINQGYWKETTETLALVLSATVVCMVIGVPLGIAAAHRPWLYAAMRPVLDLMQTLPTFVYLI
PALVLFGLGMVPGLIATVIFAIPAPIRLTHLGISSVPQELVEAGEAFGATPSQLLWKVELPYALPQIMAG
LTQTIMLSLSMVVIAALVGADGLGVPVVRALNTVNIALGFEAGLAIVVLAIVLDRMF
>gnl|CDD|274570 TIGR03417, chol_sulfatase, choline-sulfatase
TRPNILIIMADQLNGTLLPDYGPARWLHAPNLKRLAARSVVFDNAYCASPLCAPSRASFMSGQLPSRTGA
YDNAAEFASDIPTYAHYLRRAGYRTALSGKMHFCGPDQLHGFEERLTTDIYPADFGWTPDWRKPGERIDW
YHNMGSVTGAGPCERTNQLDYDDEVAFHARQKLYDLARGKDDRPFCLTVSFTHPHDPYVIRRKYWDLYED
CEILMPEVAIPYAEQDPHSQRLLDACDLRNFPITDEQIRRARRAYFGAISYIDDKIGELLDTLEETRQAD
DTIIVFTSDHGDMLGERGLWYKMSFFEGSARVPLMIAAPGRFAPGRVDAPVSTLDLLPTLVDLAGGDMDE
VAPWTDGRSLVPHLQGKGGHDEVIGEYAAEGSIAPLVMIRRGRYKFVYCEADPDQLYDLEADPHELTNLA
DDPAHADTLAAFRAEAAARWDLPAFDAQVRASQRRRWVVYEALRQGAYYPWDHQPLQDASERYMRNHMDL
DVLEESARFP
>gnl|CDD|188320 TIGR03418, chol_sulf_TF, putative choline sulfate-utilization transcription factor. Members of this protein family are transcription factors of the LysR family. Their genes typically are divergently transcribed from choline-sulfatase genes. That enzyme makes choline, a precursor to the osmoprotectant glycine-betaine, available by hydrolysis of choline sulfate
LSLQWLRVFESAARLASFTAAARELGSTQPAVSQQIKRLEEELGVPLFERKHRGVELTEDGQRLFEAVRR
GLDTIDAATAALRARRRRETLTLATDFAFATYWLMPRLHRFKAAMPDVDVSIVTSQDSHDGQRDDIDVAI
LFGDGRWPGGEAVRLFPEEVTPVCSPALRAGLPDPLSAADLLRLPLLHLEPTQPARWFDWAGWFRALGLE
RPPAPGGLRFNNYTLVIQAAIAGQGVALGWAPLVDELLAAGQLVRLGDEPVVTERGYYLVRPPRKPRDAA
VEAFRDWLLDE
>gnl|CDD|132460 TIGR03419, NifU_clost, FeS cluster assembly scaffold protein NifU, Clostridium type. NifU and NifS form a pair of iron-sulfur (FeS) cluster biosynthesis proteins much simpler than the ISC and SUF systems. Members of this protein family are a distinct group of NifU-like proteins, found always to a NifS-like protein and restricted to species that lack a SUF system. Typically, NIF systems service a smaller number of FeS-containing proteins than do ISC or SUF. Members of this particular branch typically are found, almost half the time, near the mnmA gene, involved in the carboxymethylaminomethyl modification of U34 in some tRNAs (see GenProp0704). While other NifU proteins are associated with nitrogen fixation, this family is not [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
YSEKVMDHFMNPRNVGEIENADGVGEVGNPKCGDIMKIFLKVEDDIIKDVKFKTFGCGAAIASSSMATEM
IKGKTLEEAWELTNKAVAEALDGLPPVKMHCSVLAEEAIHKAINDYREKNG
>gnl|CDD|274571 TIGR03420, DnaA_homol_Hda, DnaA regulatory inactivator Hda. Members of this protein family are Hda (Homologous to DnaA). These proteins are about half the length of DnaA and homologous over length of Hda. In the model species Escherichia coli, the initiation of DNA replication requires DnaA bound to ATP rather than ADP; Hda helps facilitate the conversion of DnaA-ATP to DnaA-ADP [DNA metabolism, DNA replication, recombination, and repair]
QLPLDVGLPDDPTFDNFYAGGNAELLAALRQLAAGKGDRFLYLWGESGSGKSHLLQAACAAAEERGKSAI
YLPLAELAQADPEVLEGLEQADLVCLDDVEAIAGQPEWQEALFHLYNRVREAGGRLLIAGRAAPAQLPLR
LPDLRTRLAWGLVFQLPPLSDEEKIAALQSRAARRGLQLPDEVADYLLRHGSRDMGSLMALLDALDRASL
AAKRKITIPFVKEVLA
>gnl|CDD|274572 TIGR03421, FeS_CyaY, iron donor protein CyaY. Members of this protein family are the iron-sulfur cluster (FeS) metabolism protein CyaY, a homolog of eukaryotic frataxin. ISC is one of several bacterial systems for FeS assembly; we find by Partial Phylogenetic Profiling vs. the ISC system that CyaY most like work with the ISC system for FeS cluster biosynthesis. A study of of cyaY mutants in Salmonella enterica bears this out. Although the trusted cutoff is set low enough to include eukaryotic frataxin sequences, a narrower, exception-type model (TIGR03421) identifies identifies members of that specific set [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
NESEFHQLAEALLDAIEEAIDDGDADIDCERQGGVLTLTFENGSQIIINKQEPLHQIWLAAKSGGFHFDY
DGGAWIDTRDGEELWALLARACSEQAGEPVVF
>gnl|CDD|132463 TIGR03422, Frataxin_homolog_mitochondrial, frataxin. Frataxin is a mitochondrial protein, mutation of which leads to the disease Friedreich's ataxia. Its orthologs are widely distributed in the bacteria, associated with the ISC system for iron-sulfur cluster assembly, and designated CyaY. This exception-type model allows those examples of frataxin per se that score above the trusted cutoff to the CyaY equivalog-type model (TIGR03421) to be named appropriately
EYHKVADEYLDHLLDKLEELGESRPDLDFDVEYSSGVLTLELPSVGTYVINKQPPNKQIWLSSPVSGPKR
YDYVNGEWIYLRDGSSLTELLEEELSK
>gnl|CDD|274573 TIGR03423, pbp2_mrdA, penicillin-binding protein 2. Members of this protein family are penicillin-binding protein 2 (PBP-2), a protein whose gene (designated pbpA or mrdA) generally is found next to the gene for RodA, a protein required for rod (bacillus) shape in many bacteria. PBP-2 acts as a transpeptidase for cell elongation (hence, rod-shape) [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
RRALVLGGLVLALFGVLAARLFYLQVIRGEEYATLSEDNRIRLVPIPPPRGLILDRNGVLLADNRPSFSL
EIVPEKVDDLDATLDRLAKLLDLDPEDIARFLKELKRSRRFEPIPLKSDLTEEEVARFAVNQYRLPGVEI
EARLKRYYPYGELAAHVLGYVGEINEEDLERLEPANYAGGDYIGKSGIEKYYEDELRGKPGYREVEVNAR
GRVIRTLSRVPPVPGKDLVLTIDARLQQAAEKALGGRRGAVVVMDPRTGEILAMVSTPSFDPNLFVDGIS
SKDYKALLNDPDRPLLNRAIQGVYPPGSTFKPVVALAALEEGVITPETRIYCPGYFQLGGRRFRCWKRGG
HGRVDLRKAIEESCDVYFYQLALRLGIDKIAEYAKRFGFGQKTGIDLPGEKSGLVPSREWKRKRFGQPWY
PGDTLNVSIGQGYVLVTPLQLAVATAALANGGKLYKPHLVKSIEDPDGGVVRRTEPEVLRPLPISPENLD
VVREGMRDVVNGPGGTARRARLGLPYKMAGKTGTAQVVSLKQGEKYDAEQIPERLRDHALFVAFAPYDNP
KIAVAVIVEHGGGGSSAAAPIARKIMDAYLLG
>gnl|CDD|132465 TIGR03424, urea_degr_1, urea carboxylase-associated protein 1. A number of bacteria degrade urea as a nitrogen source by the urea carboxylase/allophanate hydrolase pathway, which uses biotin and consumes ATP, rather than my means of the nickel-dependent enzyme urease. This model represents one of a pair of homologous, tandem uncharacterized genes found together with the urea carboxylase and allophanate hydrolase genes
DAVYDEVVPAGEPWSAVVKAGQTLRIVDLEGNQAVDTLFYNAHDTAERYSAQDTIRAQGNIYLTTGSVLY
SNEGNPMLTIVADTCGRHDTLGGACSAESNTVRYGHHKKYMHACRDNFLLAIAKYGLGKRDIVSNINFFM
NVPVTPDGSLTIVDGISAPGKYVELRAEMDVLVLISNCPQLNNPCNGFNPTPVRMLIW
>gnl|CDD|163257 TIGR03425, urea_degr_2, urea carboxylase-associated protein 2. A number of bacteria degrade urea as a nitrogen source by the urea carboxylase/allophanate hydrolase pathway, which uses biotin and consumes ATP, rather than my means of the nickel-dependent enzyme urease. This model represents one of a pair of homologous, tandem uncharacterized genes found together with the urea carboxylase and allophanate hydrolase genes
LLWAETVPGGGYWSKVLRRGTRLRLTDLEGGANVSLLLYNADAPLERYNMADTLKVQWTAYLTKGHVLLS
DMGRVLASIVEDTSGWHDALCGTSNAALNAAKYGEGRYQSARNAMFRNGRDNLLLELGKYGLGRRDLVPN
VNFFSKVAVDEDGRLHFVPGRSGAGDYVDLRAEMDTLVVLSNCPHPLDPRPDYQPKPVRLTAWRAPPVAA
DDPCRTARPENRRAFENTDLYFA
>gnl|CDD|274574 TIGR03426, shape_MreD, rod shape-determining protein MreD. Members of this protein family are the MreD protein of bacterial cell shape determination. Most rod-shaped bacteria depend on MreB and RodA to achieve either a rod shape or some other non-spherical morphology such as coil or stalk formation. MreD is encoded in an operon with MreB, and often with RodA and PBP-2 as well. It is highly hydrophobic (therefore somewhat low-complexity) and highly divergent, and therefore sometimes tricky to discover by homology, but this model finds most examples [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
LPIILILLSLLLALLLQLIPLPGFFLDGFRPDWVLLVLLYWAIALPHRVGIGTAFVLGLLQDVLSGSPLG
VHALALTLVAYLAASLFQRFRQFDLWQQALIIFLLLILGELLVFLILTLLGNAFFSLEYFWLFRLLPTLL
LNLLWPWVFFLL
>gnl|CDD|213811 TIGR03427, ABC_peri_uca, ABC transporter periplasmic binding protein, urea carboxylase region. Members of this family are ABC transporter periplasmic binding proteins associated with the urea carboxylase/allophanate hydrolase pathway, an alternative to urease for urea degradation. The protein is restricted to bacteria with the pathway, with its gene close to the urea carboxylase and allophanate hydrolase genes. The substrate for this transporter therefore is likely to be urea or a compound from which urea is easily derived [Transport and binding proteins, Unknown substrate]
KDKFKVCWSIYAGWMPWGYAAQQGIVDKWADKYGITIEVVQINDYVESINQYTAGKFDGCTMTNMDALTI
PAAGGVDTTALIVGDFSNGNDGIVLKGGKSLADLKGQKVNLVELSVSHYLLARALESVGLSEKDVKVVNT
SDADIVAAFITKDVTAVVTWNPQLSEIKAQPGANEVFDSSQIPGEILDLMVVNTQTLKANPNLGKALTGA
WYETMALMSAGDAAGKAALEAMAKASGTDLAGYKAQLKTTKMFYTPKEAVAFTTSPDLPKTMDKVRDFSF
DHGLLGEGAKSADFVGIEFPGGKVLGDPANVKLRFDPSYMQMAADGKL
>gnl|CDD|132469 TIGR03428, ureacarb_perm, permease, urea carboxylase system. A number of bacteria obtain nitrogen by biotin- and ATP-dependent urea degradation system distinct from urease. The two characterized proteins of this system are the enzymes urea carboxylase and allophanate hydrolase, but other, uncharacterized proteins co-occur as genes encoded nearby in multiple organisms. This family includes predicted permeases of the amino acid permease family, likely to transport either urea or a compound from which urea is derived. It is found so far only Actinobacteria, whereas a number of other species with the urea carboxylase have an adjacent ABC transporter operon
DLQRFGYQPQLHRKLGRYASFAAGFSFVSILTTIFQLFGFGYGFGGPAFFWTWPVVFVGQLLVALNFAEL
AARYPISGAIYQWSRRMGGEVIGWFAGWFMIIAQIVTAAAAAIALQVVLPNIWSGFQIIGEDPTLTSPSG
AANAVLLGSVLLVLTTVINCIGVEWMSRVNTIGVTCEIVGVLAVIGVLFTHAQRGPGVVFDTSVTGASPG
YYGAFLVSGLMAAYVMVGFGSAGELSEETKNPRRVAPRTILTALSVSALGGGLMILGALMAAPSLTDGRL
AAEGLPYVLSAVLDSPWGTVLLVDVAIAILVCTLAIQTAGSRLMFSMARDGKLPASAQLSRVHPRTGTPI
LPSIVIGVLCIGILLINVGNSALFATLASVCIVLIYLAYLLVTVPLLLRRLRGWPRGDQTDPAGLFSLGR
WGLPVNILAVVYGALMVVNLSWPRPEVYDPSGDGPIMLWSAPIFVGAVLLLGIWV
>gnl|CDD|274575 TIGR03429, Tryptophan_dimethylallyltransferase_2, aromatic prenyltransferase, DMATS type. Members of this protein family are mostly fungal enzymes of secondary metabolite production. Characterized or partially characterized members include several examples of dimethylallyltryptophan synthase, a brevianamide F prenyltransferase, LtxC from lyngbyatoxin biosynthesis, and a probable dimethylallyl tyrosine synthase
YDTLSKALPFPNEDQRYWWHHTGPMLARLLDAAGYSVHAQYEYLLFLRRHVLPVLGPYPSSGPPRWRSGL
TDDGSPFELSWNFQAGGKPTVRFAFEPIGPLAGTSKDPFNQRATRELLDRLARLLPGIDLEWFDHFKDAL
TLTPDEAALLKEKLPKGPLRPQMWLAFDLKGGGVVLKVYFFPRLKAAATGVPSSELVFEAIRRLDPKGLL
PALDLLEEYLASRPATLRPELLAIDCVDPAKSRLKIYLATPSVSFATVRDVWTLGGRLTDPTTMKGLELL
RELWRLLLGLPEGFSRDPDLPLRPGERPDEQLPLMYNYELRPGSPLPEPKLYFPVRQYGRNDAAVAEALE
AFFERLGWGELARSYKETLESAFPGRDLSESTGLHTYLSFSYTEEKGPYLTVYLS
>gnl|CDD|132471 TIGR03430, Tryptophan_dimethylallyltransferase, tryptophan dimethylallyltransferase. Members of this family are the enzyme tryptophan dimethylallyltransferase (EC 2.5.1.34), a distinct clade within a larger group of aromatic prenyltransferases that may act on on trp-containing cyclic dipeptides, or on tyrosine or other related substrates. Tryptophan dimethylallyltransferase and related enzymes typically are of fungal origin are involved in the biosynthesis of secondary metabolites such as ergot alkaloids
VYETLSLIFDFPNNDQRLWWHSTAPMFAKMLDTANYNVHDQYQHLGIFKKHIIPFLGVYPTKSKERWLSI
LTRYGTPFELSLNCSDSVVRYTYEPINEHTGTEKDPFNTFAIWESLQKLIRIQPGIDLEWFSYFKDELTL
NATESAYLASNDLVNEQIKTQNKLALDLKGDRFALKVYIYPHLKSVATGKSIHELIFGSVRKLSQKHPSI
QPPFNMLEDYVRSRNDPAEASKHTPLSPRLLSCDLVDPAKSRVKIYLLEQMVSLSAMEDLWTLGGRRTDA
STLEGLDMVRELWDLLQIPPGLKKYPAPYLPLGEIPDEQLPSMANYTLHHNDPMPEPQVYFTVFGMNDME
VTNALTTFFERHGWSEMARKYRVFLQSSYPHHDHESLNYLHAYISFSYRKNKPYLSVYLHSFETGDWPV
>gnl|CDD|132472 TIGR03431, PhnD, phosphonate ABC transporter, periplasmic phosphonate binding protein. This model is a subset of the broader subfamily of phosphate/phosphonate binding protein ABC transporter components, TIGR01098. In this model all members of the seed have support from genomic context for association with pathways for the metabolims of phosphonates, particularly the C-P lyase system, GenProp0232. This model includes the characterized phnD gene from E. coli. Note that this model does not identify all phnD-subfamily genes with evident phosphonate context, but all sequences above the trusted context may be inferred to bind phosphonate compounds even in the absence of such context. Furthermore, there is ample evidence to suggest that many other members of the TIGR01098 subfamily have a different primary function
MLRRLILSLVAAFMLISSNAQAEDWPKELNFGIIPTENASDLKQRWEPLADYLSKKLGVKVKLFFATDYA
GVIEGMRFGKVDIAWYGPSSYAEAYQKANAEAFAIEVNADGSTGYYSVLIVKKDSPIKSLEDLKGKTFGF
VDPNSTSGFLVPSYYLFKKNGIKPKEYFKKVTFSGSHEAAILAVANGTVDAATTNDENLDRMIRKGQPDA
MEDLRIIWKSPLIPNGPIVYRKDLPADLKAKIRKAFLNYHKTDKACFEKIAGGDLKGFVAASDKDYDPIR
DLKKAKIK
>gnl|CDD|163260 TIGR03432, yjhG_yagF, putative dehydratase, YjhG/YagF family. This homolog of dihydroxy-acid dehydratases has an odd, sparse distribution. Members are found in two Acidobacteria, two Planctomycetes, Bacillus clausii KSM-K16, and (in two copies each) in strains K12-MG1655 and W3110 of Escherichia coli. The local context is not well conserved, but a few members are adjacent to homologs of the gluconate:H+ symporter (see TIGR00791) [Unknown function, Enzymes of unknown specificity]
LDDPSHSLYTVRTHADGPDGALPLTAEMLLSRPSGDLFGLTQNAGMGWDPARLLGKEFLILSTHGGLRAA
DGTPIALGYHTGHWEVGLLMKAAAEEIKRDGAVPFAGFVSDPCDGRTQGTTGMFDSLPYRNDAAMVMRRL
IRSLPTRKGVIGIATCDKGLPAMMMALAATHHLPTVLVPGGVTLPPEVGEDAGKVQTIGARFSNGEITLE
EAAEAGCRACASPGGGCQFLGTAATSQVVAEALGLALPHSALAPSGQPIWLDMARRSARAALELSQKGLS
TRDILTDKAIENAMVVHAAFGGSTNLLLHIPAIAHAAGCRRPTVDDWTRINRKVPRLVDALPNGPVGHPT
VRVFLAGGVPEVMLHLRRAGLLHEDVLTVTGETLGENLDWWENSERRARMKQRLRERDGVDPDDVIMSPA
QAKARGLTSTVTFPKGNLAPEGSVIKSTAIDPSVVDEDGVYRHTGPARVFSSEKSAIAAIKHGKIEAGDV
LVLIGRGPSGTGMEETYQVTSALKYLSFGKHVALITDARFSGVSTGACIGHVGPEALAGGPIGKVRDGDL
IEIIIDRNTLEGTVNLVGTEDGNQLPEEGAAVLAARPLRPDLAPDPALPDDTRLWAALQQVSGGTWGGCV
YDVDKIIARL
>gnl|CDD|163261 TIGR03433, padR_acidobact, transcriptional regulator, Acidobacterial, PadR-family. Members of this protein family are putative transcriptional regulators of the PadR family, as found in species of the Acidobacteria. This family of proteins has expanded greatly in this lineage, and where it regularly is found in the vicinity of a putative transporter protein [Regulatory functions, DNA interactions]
LQGTLDLLILKTLSLGPLHGYGIAQRIQQISEDVLQVEEGSLYPALHRLERRGWIAAEWGESENNRRAKF
YRLTAAGRKQLAAETESWARLSAAIARVLG
>gnl|CDD|274576 TIGR03434, ADOP, Acidobacterial duplicated orphan permease. Members of this protein family are found, so far, only in three species of Acidobacteria, namely Acidobacteria bacterium Ellin345, Acidobacterium capsulatum ATCC 51196, and Solibacter usitatus Ellin6076, where they form large paralogous families. Each protein contains two copies of a domain called the efflux ABC transporter permease protein (pfam02687). However, unlike other members of that family (including LolC, FtsX, and MacB), genes for these proteins are essentially never found fused or adjacent to ABC transporter ATP-binding protein (pfam00005) genes. We name this family ADOP, for Acidobacterial Duplicated Orphan Permease, to reflect the restricted lineage, internal duplication, lack of associated ATP-binding cassette proteins, and permease homology. The function is unknown
LLQDLRYALRTLRRSPGFTAVAVLTLALGIGANTAIFSVVNAVLLRPLPYPDPDRLVALWERGPRAGGPG
GSFSYPDYEDWRAQNRSFSSLAAYSGASFNLTGGGEPERVRGAFVSANFFPVLGVQPALGRLFTPEDDRP
GAPPVVVLSYALWQRRFGGDPAVVGRTIRLNGRPYTVVGVMPPGFTFPGRDPDVWVPLAMDPALAGSANR
GSRWLRVIGRLKPGVTLAQAQAELDAIAARLAAAYPDTNAGRGLAVTPLRESLVGDVRPPLLVLLGAVGL
VLLIACANVANLLLARAAARQREIAVRLALGAGRGRLVRQLLTESLLLALAGGALGLLLAYWGLRLLLAL
LPASLPRLLEISLDGRVLLFALALSLLTGLLFGLAPALQATRSDLAEALKEGGRGSSGGRRRHRLRSALV
VAQVALSLVLLVGAGLLVRSLVRLQSVDPGFDPEHVLTFRLDLPGAGYPTDARLAAFYRRLLERLRALPG
VESAALASSLPLSGNGWSGGVTIEGRPPPPPGEEPLADYRRVSPGYFETMGIPLLRGRDFTERDTAGSPP
VAIVNEAFARRYFPGEDPIGKRIRLGGDDGPWFEIVGVVGDVRYAGLDEPPRPEVYLPYAQSPDRGMTLV
VRTAGDPAALAAAVRRAVRAIDPNLPVYDVRTMEEQVDRSLAQERFLALLLGLFAALALLLAAIGLYGVL
AYSVAQRTREIGIRMALGAQRGDVLRLVLRQGLRLAAAGLAIGLAAALALARLLASLLFGVSPTDPLTFA
AVAALLLAVALLACYLPARRAARVDPMIALRAE
>gnl|CDD|132476 TIGR03435, Soli_TIGR03435, soil-associated protein, TIGR03435 family. Bacterial reference strains encoding members of this protein family are all isolated from soil. These include 39 members from Solibacter usitatus Ellin6076, 27 from Acidobacterium sp. MP5ACTX8 (both Acidobacteria), and four from Pedosphaera parvula Ellin514 (Verrucomicrobia). The family is well-diversified, with few pairs showing greater than 50 % pairwise identity. A few members are fused to Peptidase_M56 domains (see pfam05569), to Sigma70_r2 domains (see pfam04542), or have a duplication of this domain
LEFEVASVKPAAPPAGGSVRSGGKIDGGRLTITNVTLRDLIQAAYGVKPYQVSGPDWLDSERFDIVAKAP
AGATREQVRLMLQTLLAERFKLAVHRETKEMPVYALVVAKGGPKLKEAPPDDGGGPNAGGPGQGGGGSIR
IECRKTTMAELAELLSRFLDRPVVDMTGLTGKYDFTLEWTPDAGSDNSAGPGAAAADPSGPSLFTALQEQ
LGLKLEPRKAPVEVLVVDHAEKKPTEN
>gnl|CDD|274577 TIGR03436, acidobact_VWFA, VWFA-related Acidobacterial domain. Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196
PTFRADVNLVLVDVTVTDKKGRPVTGLTKDDFTVLEDGKPQTIASFRRETDLPLTVGLVIDTSGSMRNDL
DRARAAAIRFLKTVLRPNDRVFVVTFNTRLRLLQDFTSDPRLLEAALNRLKPPLRTDYNSSGAFVRDGGG
TALYDAITLAALEQLANALAGIPGRKALIVISDGGDNRSRDTLERAIDAAQRADVAIYSIDARGLRAPDL
GAGAKAGLGGPEALERLAEETGGRAFYVNSNDLDGAFAQIAEELRSQYLIGYYPPNPAHDGKFRKIKVRV
KRKGLKVRARDGYYAP
>gnl|CDD|274578 TIGR03437, Soli_cterm, Solibacter uncharacterized C-terminal domain. This model describes a protein domain found in 90 proteins of Solibacter usitatus Ellin6076, nearly always as the C-terminal domain of a much larger protein. No homologs to this domain are detected outside of S. usitatus, a member of the Acidobacteria
PVAPGSIVSIFGTNLAPATLTAAGGPLPTSLGGVSVTVNGVAAPLLYVSPGQINAQVPYEVAPGAATVTV
TYNGGASAAVTVTVAAAAPGIFTLDGSGTGQAAALNNQDGSVNSAANPAAPGDVVVLYATGLGPTSPAVA
DGAPAPSSPLAPALAPVTVTIGGVPATVLYAGLAPGFVGLYQVNVRVPAGLATGAVPVVITVGGVTSNAV
TIAVQ
>gnl|CDD|274579 TIGR03438, conserved_hypothetical_protein, dimethylhistidine N-methyltransferase. This model represents a distinct set of uncharacterized proteins found in the bacteria. Analysis by PSI-BLAST shows remote sequence homology to methyltransferases [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
DLRRDVLAGLTQSPKTLPPKYFYDARGSELFEQICELPEYYPTRTEAAILERHADEIAAATGEGCELVEL
GSGSSRKTRLLLDALRAPARYVPIDISADALKESAAALAADYPQLEVHGICADFTQPLALPPEPRLGRRL
GFFPGSTIGNFTPEEAVAFLRRIRALLGPGDGLLIGVDLVKDPAVLEAAYNDAAGVTAAFNLNLLRRLNR
ELGGDFDPDAFRHRAFYNEERSRIEMHLVSRRDQTVTLAGLTVRFAAGETIHTENSYKFSLERFAALAAA
AGLRPEQVWTDPNDWFSLHLL
>gnl|CDD|274580 TIGR03439, hypothetical_protein, probable methyltransferase domain, EasF family. This model represents an uncharacterized domain of about 300 amino acids with homology to S-adenosylmethionine-dependent methyltransferases. Proteins with this domain are exclusively fungal. A few, such as EasF from Neotyphodium lolii, are associated with the biosynthesis of ergot alkaloids, a class of fungal secondary metabolites. EasF may, in fact, be the AdoMet:dimethylallyltryptophan N-methyltransferase, the enzyme that follows tryptophan dimethylallyltransferase (DMATS) in ergot alkaloid biosynthesis. Several other members of this family, including mug158 (meiotically up-regulated gene 158 protein) from Schizosaccharomyces pombe, contain an additional uncharacterized domain DUF323 (pfam03781)
IIDIRSNTVEDSLVTEIIQGLRPNGQPRTLPTLLLYDDEGLKLFEEITYSPEYYLTNDEIEILKKHSSDI
AASIPSGSMLVELGSGNLRKVGILLEALERQGKSVDYYALDVSRSELQRTLAELPLGNFSHVRCAGLLGT
YDDGLAWLKRPENRSRPTTILWLGSSIGNFSRPEAAAFLAGFLATALSPSDSFLIGLDGCKDPDKVLRAY
NDPGGVTRRFVLNGLVHANEILGHEAFREEDWEFLGEWDEELGRHEAFYIPKKDVSIGLEGVVIRKGEKI
RFECSGKYDKDEREQLCQSAGLKVVDVWTNEDGDYGIYL
>gnl|CDD|274581 TIGR03440, egtB_TIGR03440, ergothioneine biosynthesis protein EgtB. Members of this family include EgtB, and enzyme of the ergothioneine biosynthesis, as found in numerous Actinobacteria. Characterized homologs to this family include a formylglycine-generating enzyme that serves as a maturase for an aerobic sulfatase (cf. the radical SAM enzymes that serve as anaerobic sulfatase maturases) [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
LADRLREARERTLALLAPLSEEDLMLQSMPDASPPKWHLAHTTWFFETWLLREHLPGYRAFDPAFDYLFN
SYYEAVGERHPRAQRGLLSRPSLAEVLAYRAHVDDAVLELLARADDDDELLYLFELGLQHEQQHQELLLT
DLLHLFSQNPLRPAYQPPVPAPASAPPLRWVAFPGGEFEIGSDADGFAFDNERPRHRVLVPPFEIDARPV
TNGEYLEFIEDGGYRRPELWLSDGWAWVQAEGWQAPLYWRRDDGTWWVFTLGGLRPLDPDAPVCHVSYYE
ADAYARWAGARLPTEAEWEKAARWGDAPPNFAEANLGAPVGAYPAGAQGLGQLFGDVWEWTASPYEPYPG
FRPPPGAYGEYNGKFMDGQMVLRGGSCATPPRHLRPSYRNFFYPHRRWQFSGFRLA
>gnl|CDD|163267 TIGR03441, urea_trans_yut, urea transporter, Yersinia type. Members of this protein family are bacterial urea transporters, found not only is species that contain urease, but adjacent to the urease operon. It was characterized in Yersinia pseudotuberculosis. Members are homologous to eukaryotic members of solute carrier family 14, a family that includes urea transporters, and to bacterial proteins in species with no detectable urea degradation system [Transport and binding proteins, Other]
IKLIDVLLRGISQVVFQNNPLTGLFFLIALFIGNWAVGIGALIGVLVATLTARLLNYDKKSIRSGLYGFN
GVLVGIALPLFLAPSPQLWAIIVIGSILSTVVMAAVSEILKPWKVPALTMPFVLTTWIFLLASYAFKGLH
TDAPVLPHDIEPVAFGGPARENFFVAFFKGFSQVFLLDSAIAGVLILIGILIASRKAAIMALIGALISIL
AAILLGADLDSINQGLFGFNPVLTAIALGVVFLRPSIRSAAYAVLGVVLTVFVQGALDTLLTPLGLPTLT
FPFVLVTWLFLF
>gnl|CDD|132483 TIGR03442, TIGR03442, ergothioneine biosynthesis protein EgtC. Members of this strictly bacterial protein family show similarity to class II glutamine amidotransferases (see pfam00310). They are distinguished by appearing in a genome context with, and usually adjacent to or between, members of families TIGR03438 (an uncharacterized methyltransferase) and TIGR03440 (an uncharacterized protein) [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
MCRHLAYLGAPVSLADLLLDPPHSLLVQSYQPREMRHGLVNADGFGVGWYDSGKDTVPFRYRSTQPIWND
INFASLARYVESGCVLAAVRSATVGMAIDESACAPFSDGRWLFSHNGFVDNFRQTLYRPLRDRLPDIFYL
AIEGSTDSAHLFALLLNRLLENDPRALEEALAEVLLILFSAAAAPRVRLNLLLTDGSRLVATRWADTLYW
LKDPEGVIVASEPYDDDPGWQDVPDRHLLSVSEDDVTITPL
>gnl|CDD|274582 TIGR03443, L-aminoadipate-semialdehyde_dehydrogenase, L-aminoadipate-semialdehyde dehydrogenase. Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal
RWSERLDNPTLSVLPHDYLRPANNRLVEATYSLQLPSAEVTAGGGSTPFIILLAAFAALVYRLTGDEDIV
LGTSSNKSGRPFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPLFRLAF
QDAPDNQQTTYSTGSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGK
VSLITPSQKSLLPDPTKDLDWSGFRGAIHDIFADNAEKHPDRTCVVETPSFLDPSSKTRSFTYKQINEAS
NILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVIE
KAGTLDQLVRDYIDKELELRTEIPALALQDDGSLVGGSLEGGETDVLAPYQALKDTPTGVVVGPDSNPTL
SFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTAD
DIGTPGRLAEWMAKYGATVTHLTPAMGQLLSAQATTPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVN
MYGTTETQRAVSYFEIPSRSSDSTFLKNLKDVMPAGKGMKNVQLLVVNRNDRTQTCGVGEVGEIYVRAGG
LAEGYLGLPELNAEKFVNNWFVDPSHWIDLDKENNKPEREFWLGPRDRLYRTGDLGRYLPDGNVECCGRA
DDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDKSDELEEFKSEVDDEESSD
PVVKGLIKYRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAVAKNRSAS
AADEEFTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTI
KGFAKEVDRLKKGEELADEGDSEIEEEETVLELDYAKDAKTLVDSLPKSYPSRKELDASTPITVFLTGAT
GFLGSFILRDLLTRRSNSNFKVFAHVRAKSEEAGLERLRKTGTTYGIWDEEWASRIEVVLGDLSKEKFGL
SDEKWSDLTNEVDVIIHNGALVHWVYPYSKLRDANVIGTINVLNLCAEGKAKQFSFVSSTSALDTEYYVN
LSDELVQAGGAGIPESDDLMGSSKGLGTGYGQSKWVAEYIIREAGKRGLRGCIVRPGYVTGDSKTGATNT
DDFLLRMLKGCIQLGLIPNINNTVNMVPVDHVARVVVAAALNPPKESELAVAHVTGHPRIRFNDFLGTLK
TYGYDVEIVDYVHWRKSLERFVIERSEDNALFPLLHFVLDDLPQSTKAPELDDTNAATSLKADAAWTGVD
VSSGAGVTEEQIGIYIAYLVKVGFLPAPTKTGALPLPKIEISEAQLKLIASAGGRGSAA
>gnl|CDD|274583 TIGR03444, EgtA_Cys_ligase, ergothioneine biosynthesis glutamate--cysteine ligase EgtA. Members of this bacterial protein family, EgtA, resemble the glutamate--cysteine ligase of the two-step pathway for glutathione (GSH) biosynthesis, but instead are involved in the biosynthesis of the histidine-derived thiol, ergothioneine (EGT). Successful in vitro reconstitution of EGT biosynthesis using EgtBCDE and gamma-L-glutamyl-L-cysteine suggests that this enzyme is a bone fide glutamate--cysteine ligase [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
YIGGVCFKDGPPGLVGLELEWLTVQTPAAHCPDLAAPTRRPSPHRIRAVIPGSPAPPLPGGSRITVEPGG
QLELSGPPADGLTAAVAALAADLAVLRAALAEDGLALVGLGADPLRPPRRVLPGPRYRAMEQFFATGIGP
FGALMMCSTASVQVNLDAGTDPAEWAERWRLAHALGPVLIAAFANSPALGGRPTGWRSTRQRVWGQLDAA
RTGPVLAASGDDPADDWARYALDAPLMCVRNPDDGEPVPVTDGVTFADWVAGRDPVIGRRPTRADLDYHL
TTLFPPVRPRGWLELRYLDAQPGDGWPVPVATLTALLDDPVAAAEAAEAAAPVATRWDDAARLGLADREL
RAAAVRCLDLAAARAPTELAEAVLDLAARYVDRGRCPADE
>gnl|CDD|274584 TIGR03445, mycothiol_MshB, N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase. Members of this protein family are N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase, also called 1D-myo-inosityl-2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase, the MshB protein of mycothiol biosynthesis in Mycobacterium tuberculosis and related species [Cellular processes, Detoxification]
LLVHAHPDDETLTTGATIARYAARGADVTVVTCTLGEEGEVIGERWAQLAADRADQLGGYRIGELTAALR
ALGVGDPRFLGGAGRWRDSGMAGTPSRSRPRAFVDADVDEAAGALVAVIREVRPHVVVTYDPNGGYGHPD
HIQAHRVTTRAVEAAAEAPLPGTPWQVPKFYWTVTPRSALEEAFARLRGDLPGEWRLPAAEDVPFGVPDD
RITTVVDGTAYLAAKRAALRAHATQVTVAPSGRAFALSNNIAQPILAEEHYVLVRGEAGPRDPRGWETDL
FAGL
>gnl|CDD|132487 TIGR03446, mycothiol_Mca, mycothiol conjugate amidase Mca. Mycobacterium tuberculosis, Corynebacterium glutamicum, and related species use the thiol mycothiol in place of glutathione. This enzyme, homologous to the (dispensible) MshB enzyme of mycothiol biosynthesis, is described as an amidase that acts on conjugates to mycothiol. It is a detoxification enzyme [Cellular processes, Detoxification]
LRLMAVHAHPDDESSKGAATMARYAAEGHDVMVVTCTGGERGDILNPAMDKPAVEGRIAEVRREEMAEAA
EILGVEHRWLGFVDSGLPEGDPLPPLPEGCFALEPLEEAAEPLVRVIREFRPHVITTYDENGGYPHPDHI
MCHEVSVEAFEAAGDPERYPEAGEPWAPLKLYYTHGFIRERMEALHEELAERGLESPYAEWLARWLEDRA
DITARVTTQVECADYFEQRDDALRAHATQIDPNGFFFAVPLEIQRRLWPTEEFELARSRVPTSLPEDDLF
AGI
>gnl|CDD|132488 TIGR03447, mycothiol_MshC, cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase. Members of this protein family are MshC, l-cysteine:1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, an enzyme that uses ATP to ligate a Cys residue to a mycothiol precursor molecule, in the second to last step in mycothiol biosynthesis. This enzyme shows considerable homology to Cys--tRNA ligases, and many instances are misannotated as such. Mycothiol is found in Mycobacterium tuberculosis, Corynebacterium glutamicum, Streptomyces coelicolor, and various other members of the Actinobacteria. Mycothiol is an analog to glutathione [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
QSWPAPAVPALPGTGPPLRLFDTADGQVRPVEPGPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRD
AGHRVHYVQNVTDVDDPLFERAERDGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVE
KLLASGAAYIVEGPEYPDVYFSIDATEQFGYESGYDRATMLELFAERGGDPDRPGKRDPLDALLWRAARE
GEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAG
MIGLDGEKMSKSLGNLVFVSKLRAAGVDPAAIRLGLLAGHYRQDRDWTDAVLAEAEARLARWRAALALPD
APDATDLIARLRQHLANDLDTPAALAAVDGWAADALSYGGSDTEAPALVATAVDALLGVRL
>gnl|CDD|132489 TIGR03448, mycothiol_MshD, mycothiol synthase. Members of this family are MshD, the acetyltransferase that catalyzes the final step of mycothiol biosynthesis in various members of the Actinomyctes, Mycothiol replaces glutathione in these species [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
TWRAALDADLRRDVRELLAAATAVDGVAPVSEQVLRGLREPGAGHTRHLVAVDSDPIVGYANLVPARGTD
PAMAELVVHPAHRRRGIGRALIRALLAKGGGRLRVWAHGDLPAARALASRLGLVPTRELLQMRRPLRDLE
LPEPQVPDGVTVRAYVGAPDDAEWLRVNNAAFAWHPEQGGWTRADLAERRAEPWFDPAGLFLAFDDAPGE
LLGFHWTKVHPDEPALGEVYVVGVDPAAQGRGLGDALTLIGLHHLAARGLPAVMLYVEADNEAAVRTYEK
LGFTVAEVDVAY
>gnl|CDD|132490 TIGR03449, mycothiol_MshA, D-inositol-3-phosphate glycosyltransferase. Members of this protein family, found exclusively in the Actinobacteria, are MshA, the glycosyltransferase of mycothiol biosynthesis. Mycothiol replaces glutathione in these species
VAMISMHTSPLQQPGTGDAGGMNVYILETATELARRGIEVDIFTRATRPSQPPVVEVAPGVRVRNVVAGP
YEGLDKEDLPTQLCAFTGGVLRAEARHEPGYYDLIHSHYWLSGQVGWLLRDRWGVPLVHTAHTLAAVKNA
ALADGDTPEPEARRIGEQQLVDNADRLIANTDEEARDLVRHYDADPDRIDVVAPGADLERFRPGDRATER
ARLGLPLDTKVVAFVGRIQPLKAPDVLLRAVAELLDRDPDRNLRVIVVGGPSGSGLATPDALIELAAELG
IADRVRFLPPRPPEELVHVYRAADVVAVPSYNESFGLVAMEAQACGTPVVAARVGGLPVAVADGETGLLV
DGHDPADWADALARLLDDPRTRIRMGAAAVEHAAGFSWAATADGLLSSYRDALAA
>gnl|CDD|132491 TIGR03450, mycothiol_INO1, inositol 1-phosphate synthase, Actinobacterial type. This enzyme, inositol 1-phosphate synthase as found in Actinobacteria, produces an essential precursor for several different products, including mycothiol, which is a glutathione analog, and phosphatidylinositol, which is a phospholipid
VRVAIVGVGNCASSLVQGVEYYYNADPTSTVPGLMHVQFGPYHVGDVEFVAAFDVDAKKVGFDLSDAIFA
SENNTIKIADVPPTGVTVQRGPTLDGLGKYYRDTIEESDAEPVDVVQALKDAKVDVLVSYLPVGSEEADK
FYAQCAIDAGVAFVNALPVFIASDPEWAKKFTDAGVPIVGDDIKSQVGATITHRVLAKLFEDRGVRLDRT
MQLNVGGNMDFKNMLERDRLESKKISKTQAVTSNLPDRPLKDKNVHIGPSDHVGWLDDRKWAYVRLEGRA
FGDVPLNLEYKLEVWDSPNSAGVIIDAVRAAKIAKDRGIGGPVIPASSYLMKSPPEQLPDDVARAQLEEF
I
>gnl|CDD|132492 TIGR03451, S-hydroxymethylmycothiol_dehydrogenase, S-(hydroxymethyl)mycothiol dehydrogenase. Members of this protein family are mycothiol-dependent formaldehyde dehydrogenase (EC 1.2.1.66). This protein is found, so far, only in the Actinobacteria (Mycobacterium sp., Streptomyces sp., Corynebacterium sp., and related species), where mycothione replaces glutathione [Cellular processes, Detoxification]
TVRGVIARSKGAPVELETIVVPDPGPGEVIVDIQACGVCHTDLHYREGGINDEFPFLLGHEAAGVVEAVG
EGVTDVAPGDYVVLNWRAVCGQCRACKRGRPWYCFDTHNATQKMTLTDGTELSPALGIGAFAEKTLVHAG
QCTKVDPAADPAAAGLLGCGVMAGLGAAVNTGGVKRGDSVAVIGCGGVGDAAIAGAALAGASKIIAVDID
DRKLEWAREFGATHTVNSSGTDPVEAIRALTGGFGADVVIDAVGRPETYKQAFYARDLAGTVVLVGVPTP
DMTLELPLLDVFGRGGALKSSWYGDCLPERDFPMLVDLYLQGRLPLDAFVTERIGLDDVEEAFDKMHAGD
VLRSVVEL
>gnl|CDD|132493 TIGR03452, mycothione_red, mycothione reductase. Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate
RHYDLIIIGTGSGNSIPDPRFADKRIAIVEKGTFGGTCLNVGCIPTKMFVYAAEVAQSIGESARLGIDAE
IDSVRWPDIVSRVFGDRIDPIAAGGEDYRRGDETPNIDVYDGHARFVGPRTLRTGDGEEITGDQIVIAAG
SRPYIPPAIADSGVRYHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKLLRHLDE
DISDRFTEIAKKKWDIRLGRNVTAVEQDGDGVTLTLDDGSTVTADVLLVATGRVPNGDLLDAEAAGVEVD
EDGRIKVDEYGRTSARGVWALGDVSSPYQLKHVANAEARVVKHNLLHPNDLRKMPHDFVPSAVFTHPQIA
TVGLTEQEAREAGHDITVKIQNYGDVAYGWAMEDTTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITA
MAFGLDAREMARKQYWIHPALPEVVENALLGL
>gnl|CDD|274585 TIGR03453, partition_RepA, plasmid partitioning protein RepA. Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error [Mobile and extrachromosomal element functions, Plasmid functions]
DALIAAQARELSEQLQALRERLFPPNARKTLRKFTSGEVAKLLGVSDSYLRQLSLEGKGPEPETLSNGRR
SYTLEQINELRRHLAQRGREARRYLPHRRGGEHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAID
LDPQASLSALFGYQPEFDVGENETLYGAIRYDDERRPISEIIRKTYFPGLDLVPGNLELMEFEHETPRAL
SRGQGGDTIFFARVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGVLITVHPQMLDVMSMSQFLLM
TGDLLGVVREAGGNLSYDFMRYLVTRYEPNDGPQAQMVAFLRSLFGDHVLTNPMLKSTAISDAGLTKQTL
YEVERSQFTRSTYDRAMESLDAVNAEIEGLIKKAWGR
>gnl|CDD|274586 TIGR03454, partition_RepB, plasmid partitioning protein RepB. Members of this family are the RepB protein involved in replicon partitioning. RepB is found, in general, as part of a repABC operon in plasmids and small chromosomes, separate from the main chromosome, in various bacteria. This model describes a rather narrow clade of proteins; it should be noted that additional homologs scoring below the trusted cutoff have very similar functions, although they may be named differently [Mobile and extrachromosomal element functions, Plasmid functions]
SRKNLLGSLFSPAAAPASAPALGRPRQRVSSGAVGAMGRSLGELSQKAKRAEELEEQLAEGETVVELDPA
LIDPSFVRDRLDSDDEDFADLVESIREHGQQVPILVRPHPEAEGRYQIAYGHRRLRAARELGRPVKAVVR
ELSDEELVIAQGQENAARRDLSFIERALFAARLEDRGFDRDTIMAALSVDKTELSRMISVARRIPEELIE
AIGPAPGIGRPRWMELAELLEHPGNDAEALDEVASAAFKALESDQRFEALFAALSKKAKRSPAATKSWKA
ADGSVLAKIKRTAKALTLTLKKKEAPEFADFILERLDDLYEEFRR
>gnl|CDD|274587 TIGR03455, ATP_phosphoribosyltransferase, ATP phosphoribosyltransferase, C-terminal domain. This domain corresponds to the C-terminal third of the HisG protein. It is absent in many lineages
KREKIEQLLTRLQGVLAARGKVLLMMNVPRDNLDEVRAVLPGLEGPTVSPLADEGWVAVHAVVDEKVVNE
LIDKLKAAGARDILVLPIEKCR
>gnl|CDD|132497 TIGR03457, Sulfoacetaldehyde_acetyltransferase, sulfoacetaldehyde acetyltransferase. Members of this protein family are sulfoacetaldehyde acetyltransferase, an enzyme of taurine utilization. Taurine, or 2-aminoethanesulfonate, can be used by bacteria as a source of carbon, nitrogen, and sulfur [Central intermediary metabolism, Other]
KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIG
QNGPGVTNCVTAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLN
RCFERAWREMGPAQLNIPRDYFYGEIDVEIPRPVRLDRGAGGATSLAQAARLLAEAKFPVIISGGGVVMG
DAVEECKALAERLGAPVVNSYLHNDSFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLGPFGTLP
QYGIDYWPKNAKIIQVDANAKMIGLVKKVTVGICGDAKAAAAEILQRLAGKAGDANRAERKAKIQAERSA
WEQELSEMTHERDPFSLDMIVEQRQEEGNWLHPRQVLRELEKAMPEDAIVSTDIGNINSVANSYLRFEKP
RKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDIPVTAVVFRNRQWGAE
KKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAAQAEGKTTVIEIVCTREL
GDPFRRDALSKPVRLLDKY
>gnl|CDD|274588 TIGR03458, Propionyl-CoA:succinate_CoA_transferase, succinate CoA transferase. This family of CoA transferases includes enzymes catalyzing at least two related but distinct activities. The E. coli YgfH protein has been characterized as a propionyl-CoA:succinate CoA transferase where it appears to be involved in a pathway for the decarboxylation of succinate to propionate. The Clostridium kluyveri CAT1 protein has been characterized as a acetyl-CoA:succinate CoA transferase and is believed to be involved in anaerobic succinate degradation. The propionate:succinate transferase activity has been reported in the propionic acid fermentation of propionibacterium species, where it is distinct from the coupled activities of distinct nucleotide-triphosphate dependent succinate and propionate/acetate CoA transferases (as inferred from activity in the absence of NTPs). The family represented by this model includes a member from Propionibacterium acnes KPA171202 which is likely to be responsible for this activity. A closely related clade not included in this family are the Ach1p proteins of fungi which are acetyl-CoA hydrolases. This name has been applied to many of the proteins represented by this model, possibly erroneously
KVMSADEAAALIKDGMTVGMSGFTPAGYPKAVPAALAKRAKAAHAAGEPFKITLLTGASTGPELDGVLAE
ADAIARRLPYQSDPTLRKKINAGEVMYVDMHLSHVAQQLRYGFLGKVDVAVIEAAAITEDGRIIPTSSVG
NNPTFLELADKVIVEVNTWQPLELEGMHDIYEPGDPPHRRPIPITTPGDRIGTPYIQIDPDKIVAVVETN
APDRNSPFTPPDEVSQKIAGHLIDFLDHEVKAGRLPKNLLPLQSGVGNIANAVLAGLGDSPFENLTMYTE
VIQDSMLDLIDSGKLTFASATSLTLSPEALERFYANIDFYRDKIVLRPQEISNHPEIIRRLGVIAINTAI
EADIYGNVNSTHVMGTKMMNGIGGSGDFARNAYLSIFMTPSIAKGGKISSIVPMVSHVDHTEHDVMVIVT
EQGLADLRGLSPRERARAIIDNCAHPDYRDLLRDYYERASARGGHTPHLLDEALSWHTRLAETGS
>gnl|CDD|274589 TIGR03459, crt_membr, carotene biosynthesis associated membrane protein. This model represents a family of hydrophobic and presumed membrane proteins found in the Actinobacteria. The genes encoding these proteins are syntenically associated with (found proximal to) genes of carotene biosynthesis ususally including phytoene synthase (crtB), phytoene dehydrogenase (crtI) and geranylgeranyl pyrophosphate synthase (ispA)
PVWLGFLGSILITLGSFGAGAVRSRDGLLESLHLSWLRFGHGAGLSTIVLWIGVGLMILAWVILGRRVLA
GAVTLHTVRATIAIWIGPLLFAVPMMSRDVYSYLMQGALLRDGFDPYTVGAAANPGPLLDEVSPDWRNTT
TPYGPLHLLVGQAITTVTGDNVTAGTLAFKLLSLPGLAVMVWAVPKLATHLGVNPTVALWLGVLNPLVVI
HLIGGMHNEMLMVGLVSAGILLALKRRPVAGIALIAVAVALKATAGIALPFVVWIWVAHVAGPLAYAAGK
ALPDLWRRVGTFVAAALVGVLVFVAVFALITAAAGVGWGWLTALSGNSKVINPLALPSLVASVIEPVGSR
WLDDLDFNAVVDVIRPISMVIMLLGLVATWWLFRHDERAAVTGTAAAYAIAVVFNPVTLPWYYTWPLALA
ATFAQSRWLIYLTAGASTWVMFVFTGDGNHGLYNLW
>gnl|CDD|132500 TIGR03460, crt_membr_arch, carotene biosynthesis associated membrane protein
IFVTAIVFVQAPPLVTGSVGAAMAIEGIVYWLFFASMALPALLTRGRALGWRAGLLIVALGCYGGGLIET
VGVHTGWPFGEYVYGSALGPKILGHVPFVVPMAWFPLTLPSYVLARRHHRGRVRSLLLAALVLALWDVVI
DPAMVAAGFWRWLGPGPFYGVPLQNTAGWVLSGIAAVLLLTALPDQAGSTARNERAPLLYAALCLWAYGI
CLLANLTFPALIATLLPALLLW
>gnl|CDD|132501 TIGR03461, pabC_Proteo, aminodeoxychorismate lyase. Members of this protein family are aminodeoxychorismate lyase (ADC lyase), EC 4.1.3.38, the PabC protein of PABA biosynthesis. PABA (para-aminobenzoate) is a precursor of folate, needed for de novo purine biosynthesis. This enzyme is a pyridoxal-phosphate-binding protein in the class IV aminotransferase family (pfam01063) [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
WVNGVLQTQISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPLPDWDALREEMAQLAA
GYSLGVLKVIISRGSGGRGYSPPGCSDPTRIISVSPYPAHYSAWQQQGIRLGVSPVRLGRNPLLAGIKHL
NRLEQVLIKAELENSEADEALVLDTDGNVVECTAANIFWRKGNQVFTPDLSYCGVAGVMRQHVLALLPAL
GYEIEEVKAGLEELLSADEVFITNSLMGVVPVNAIGETSYPSRTLTRLLQP
>gnl|CDD|274590 TIGR03462, Bifunctional_lycopene_cyclase/phytoene_synthase, lycopene cyclase domain. This domain is often repeated twice within the same polypeptide, as is observed in Archaea, Thermus, Sphingobacteria and Fungi. In the fungal sequences, this tandem domain pair is observed as the N-terminal half of a bifunctional protein, where it has been characterized as a lycopene beta-cyclase and the C-terminal half is a phytoene synthetase. In Myxococcus and Actinobacterial genomes this domain appears as a single polypeptide, tandemly repeated and usually in a genomic context consistent with a role in carotenoid biosynthesis. It is unclear whether any of the sequences in this family truly encode lycopene epsilon cyclases. However a number are annotated as such. The domain is generally hydrophobic with a number of predicted membrane spanning segments and contains a distinctive motif (hPhEEhhhhhh). In certain sequences one of either the proline or glutamates may vary, but always one of the tandem pair appear to match this canonical sequence exactly
YLYLGVLLVWALPVLALLWVFRGPFLRLRALALALLIALPTFLVWDNLAIRRGVWTYNPRYILGIRLGDL
PIEEFLFFLLTPLLTVLWL
>gnl|CDD|274591 TIGR03463, osq_cycl, 2,3-oxidosqualene cyclase. This model identifies 2,3-oxidosqualene cyclases from Stigmatella aurantiaca which produces cycloartenol, and Gemmata obscuriglobus and Methylococcus capsulatus, which each produce the closely related sterol, lanosterol
LAALQDSAGDWEGDMGGCQFIIAIAVAGLHVMGRPPDAEERAAIIAHFELHQLADGAWGLDPEAPGQVFF
SVLAYVALRLLGLGKDDAGLARARAWFHAQPEGPKASGAWGKFILALLGLYEREGLNAVPPELFLLPESL
PFHPSRFWCHCRLIYLGIAWLSGRGARAPESDPLLAAIRQEIFAEGYEQVDFGAARERVAPTDLFTPISF
VLKAANDLLAGYERLAGKALRARALDFAFEQILAEDEATHYICIGPINGLLNCLAIFAHDPDGPDLAAHL
EGLEAWFWEDDAEGLRMNGANSNALWDTAFAVQALAALGELDEEAKHALEEAAAFIDAAQMLADLADPQE
AFRDPAKGGWCFSDGDHCWPISDCAAEALKALFALEELGDNRISEALGAARLQDAVEFILSMQNADGGFA
TYELQRGGKLLELLNPSDMFGQCMTDLSYVECTAACLGALAAWLKHHPDLPDAKIDAAIRKAEEFIRRRQ
LDDGSFMGFWGICFTYATFFGAKGLIAAGAEPADMALQAAAAFLLEKQRADGAWGEHVESCLEARWVEGK
HGHAVMTAWALLALAAAGEAAHDAAERGIAWLCEQQGEDGGWPPEGIAGIFFGAAAIDYDAYLRIFPTWA
LARC
>gnl|CDD|274592 TIGR03464, HpnC, squalene synthase HpnC. This family of genes are members of a superfamily (pfam00494) of phytoene and squalene synthases which catalyze the head-t0-head condensation of polyisoprene pyrophosphates. The genes of this family are often found in the same genetic locus with squalene-hopene cyclase genes, and are never associated with genes for the metabolism of phytoene. In the organisms Zymomonas mobilis and Bradyrhizobium japonicum these genes have been characterized as squalene synthases (farnesyl-pyrophosphate ligases). Often, these genes appear in tandem with the HpnD gene which appears to have resulted from an ancient gene duplication event. Presumably these proteins form a heteromeric complex, but this has not yet been experimentally demonstrated
KVAHYENFPVASLLLPARLRAPIHAVYAFARTADDIADEGDASAEERLALLDDLRAELDAIYSGEPAAPV
FVALARTVRRHGLPIEPFLDLLDAFRQDQVVTRYATWAELLDYCRYSANPVGRLVLDLYGASDPERLALS
DAICTALQLINFWQDVGVDLRKGRVYLPRDDLARFGVSEEDLAAGRATPAVRALMAFEVSRTRALLDRGA
PLVGRVDGRLGLELALFVRGGLRILEAIEAAGYDVLRERPKLGKTDWLGLLLRALW
>gnl|CDD|163278 TIGR03465, HpnD, squalene synthase HpnD. The genes of this family are often found in the same genetic locus with squalene-hopene cyclase genes, and are never associated with genes for the metabolism of phytoene. In the organisms Zymomonas mobilis and Bradyrhizobium japonicum these genes have been characterized as squalene synthases (farnesyl-pyrophosphate ligases). Often, these genes appear in tandem with the HpnC gene which appears to have resulted from an ancient gene duplication event. Presumably these proteins form a heteromeric complex, but this has not yet been experimentally demonstrated
AAASGSSFYYGMRLLPPERRRAMTALYAFCREVDDIVDEDSDPEVAQAKLAWWRAEIDRLYAGAPSHPVA
RALADPARRFDLPQEDFLEVIDGMEMDLEQTRYPDFAELDLYCDRVAGAVGRLSARIFGATDARTLEYAH
HLGRALQLTNILRDVGEDARRGRIYLPAEELQRFGVPAADILEGRYSPALAALCRFQAERARAHYAEADA
LLPACDRRAQRAARAMAAIYRALLDEIEADGFQVLRQRVSLTPLRKLWIALRTWLR
>gnl|CDD|163279 TIGR03466, HpnA, hopanoid-associated sugar epimerase. The sequences in this family are members of the pfam01370 superfamily of NAD-dependent epimerases and dehydratases typically acting on nucleotide-sugar substrates. The genes of the family modeled here are generally in the same locus with genes involved in the biosynthesis and elaboration of hopene, the cyclization product of the polyisoprenoid squalene. This gene and its association with hopene biosynthesis in Zymomonas mobilis has been noted in the literature where the gene symbol hpnA was assigned. Hopanoids are known to be components of the plasma membrane and to have polar sugar head groups in Z. mobilis and other species
MKVLVTGATGFVGSAVVRLLLEQGEEVRVLVRPTSDRRNLEGLDVEIVEGDLRDPASLRKAVAGCRALFH
VAADYRLWAPDPEEMYAANVEGTRNLLRAALEAGVERVVYTSSVATLGVRGDGTPADETTPSSLDDMIGH
YKRSKFLAEQAALEMAAEKGLPVVIVNPSTPIGPRDIKPTPTGRIIVDFLNGKMPAYVDTGLNLVHVDDV
AEGHLLALERGRIGERYILGGENLTLKQILDKLAEITGRPAPRVKLPRWLLLPVAWGAEALARLTGKEPR
VTVDGVRMAKKKMFFSSAKAVRELGYRQRPAREALRDAVEWFRANGYL
>gnl|CDD|274593 TIGR03467, HpnE, squalene-associated FAD-dependent desaturase. The sequences in this family are members of the pfam01593 superfamily of flavin-containing amine oxidases which include the phytoene desaturases. These sequences also include a FAD-dependent oxidoreductase domain, pfam01266. The genes of the family modeled here are generally in the same locus with genes involved in the biosynthesis and elaboration of squalene, the condensation product of the polyisoprenoid farnesyl pyrophosphate. This gene and its association with hopene biosynthesis in Zymomonas mobilis has been noted in the literature where the gene symbol hpnE was assigned. This gene is also found in contexts where the downstream conversion of squalene to hopenes is not evidence. The precise nature of the reaction catalyzed by this enzyme is unknown at this time
SAAVELARAGARVTLFEARPRLGGRARSFEDGGLGQTIDNGQHVLLGAYTNLLALLRRIGAEPRLQGPRL
PLPFYDPGGRLSRLRLSRLPAPLHLARGLLRAPGLSWADKLALARALLALRRTRFRALDDTTVGDWLQAA
GQSERLIERLWEPLLLSALNTPPERASAALAAKVLRDSFLAGRAASDLLLPRVPLSELFPEPARRWLDSR
GGEVRLGTRVRSIEANAGGIRALVRSGGETLPADAVVLAVPPRHAASLLPGEDLGALLTALGYSPITTVH
LRLDRAVRLPAPMVGLVGGLAQWLFDRGQLAGEPGYLAVVISAARDLVDLPREELADRIVAELRRAFPRV
AGAKPLWARVIKEKRATFAATPGLNRLRPGARTPWPNLFLAGDWTATGWPATMEGAVRSGYQAAEAVLK
>gnl|CDD|274594 TIGR03468, HpnG, hopanoid-associated phosphorylase. The sequences in this family are members of the pfam01048 family of phosphorylases typically acting on nucleotide-sugar substrates. The genes of the family modeled here are generally in the same locus with genes involved in the biosynthesis and elaboration of hopene, the cyclization product of the polyisoprenoid squalene. This gene is adjacent to the genes PhnA-E and squalene-hopene cyclase (which would be HpnF) in Zymomonas mobilis and their association with hopene biosynthesis has been noted in the literature. Extending the gene symbol sequence, we suggest the symbol HpnG for the product of this gene. Hopanoids are known to be components of the plasma membrane and to have polar sugar head groups in Z. mobilis and other species
ARPILAVTGLAFEARIAAGPGLLVCLSGGGPERARAAAARLMAAGAAGLVSFGTAGALDPALQPGDLVVP
EEVRADGDRFPTDPAWRRRLLEALPAGLRVHRGVLAASDTVVSTAAAKAALARATGAAAVDMESGAVAAV
AAAAGLPFAVIRVISDPADRALPRAALDALRPDGSTALAALLRGLLRRPLRLPALIRLARDAQAALATLR
AV
>gnl|CDD|213815 TIGR03469, HpnB, hopene-associated glycosyltransferase HpnB. This family of genes include a glycosyl transferase, group 2 domain (pfam00535) which are responsible, generally for the transfer of nucleotide-diphosphate sugars to substrates such as polysaccharides and lipids. The genes of this family are often found in the same genetic locus with squalene-hopene cyclase genes, and are never associated with genes for the metabolism of phytoene. Indeed, the members of this family appear to never be found in a genome lacking squalene-hopene cyclase (SHC), although not all genomes encoding SHC have this glycosyl transferase. In the organism Zymomonas mobilis the linkage of this gene to hopanoid biosynthesis has been noted and the gene named HpnB. Hopanoids are known to feature polar glycosyl head groups in many organisms
LFGLALTSLAIWIGLLFFRGGFWRCDQRLPPQTPSPEAWPAVVAVVPARNEADVIGECVTSLLEQDYPGK
LHVILVDDHSTDGTADIARAAARAYGRGDRLTVVSGQPLPPGWSGKLWAVSQGIAAARTLAPPADYLLLT
DADIAHGPDNLARLVARARAEGLDLVSLMVRLRCESFWEKLLIPAFVFFFQKLYPFRWVNDPRRRTAAAA
GGCILIRREALERIGGIAAIRGALIDDCTLAAAVKRSGGRIWLGLAARTRSLRPYDGLGEIWRMIARTAY
TQLRYSPLLLAGTVIGMALVYLAPPVLALFGGGRGNWPLAVLGLLAWLLMALAYVPTLRFYRLPPLWALA
LPLIALFYTLATLDSARRHWRGRGGAWKGRVYPA
>gnl|CDD|274595 TIGR03470, HpnH, hopanoid biosynthesis associated radical SAM protein HpnH. The sequences represented by this model are members of the radical SAM superfamily of enzymes (pfam04055). These enzymes utilize an iron-sulfur redox cluster and S-adenosylmethionine to carry out diverse radical mediated reactions. The members of this clade are frequently found in the same locus as squalene-hopene cyclase (SHC, TIGR01507) and other genes associated with the biosynthesis of hopanoid natural products. The linkage between SHC and this radical SAM enzyme is strong; one is nearly always observed in the same genome where the other is found. A hopanoid biosynthesis locus was described in Zymomonas mobilis consisting of the genes HpnA-E and SHC (HpnF). Continuing past SHC are found a phosphorylase enzyme (ZMO0873, i.e. HpnG, TIGR03468) and this radical SAM enzyme (ZMO0874) which we name here HpnH. Granted, in Z. mobilis, HpnH is in a convergent orientation with respect to HpnA-G, but one gene beyond HpnH and running in the same convergent direction is IspH (ZM0875, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase), an essential enzyme of IPP biosynthesis and therefore essential for the biosynthesis of hopanoids. One of the well-described hopanoid intermediates is bacteriohopanetetrol. In the conversion from hopene several reactions must occur in the side chain for which a radical mechanism might be reasonable. These include the four (presumably anaerobic) hydroxylations and a methyl shift
MAVPLRQKLRVGAYIIKQKLKGRKRYPLVLMLEPLFRCNLACAGCGKIQYPDEILKRRLSVEECVAAVEE
CGAPMVSIPGGEPLMHPEIDEIVRGLVARKKFVYLCTNALLLEKKLDKFEPSPYLTFSVHLDGLREHHDA
SVCQEGVFDRAVEAIREAKARGFRVTTNSTLFNGETPESVAEFFDYLQELGVDGMTISPGYAYEKAPDQD
HFLGREQTKELFRDVLANGNGRGWRFNHSPLFLDFLAGNQDYACTPWGMPAYNVFGWQKPCYLLNEGYVP
TFRELMEETDWEKYGTGRNPKCANCMVHCGYEPTAVLD
>gnl|CDD|132511 TIGR03471, HpnJ, hopanoid biosynthesis associated radical SAM protein HpnJ. The sequences represented by this model are members of the radical SAM superfamily of enzymes (pfam04055). These enzymes utilize an iron-sulfur redox cluster and S-adenosylmethionine to carry out diverse radical mediated reactions. The member of this clade from Acidithiobacillus ferrooxidans ATCC 23270 (AFE_0975) is found in the same locus as squalene-hopene cyclase (SHC, TIGR01507) and other genes associated with the biosynthesis of hopanoid natural products. Similarly, in Ralstonia eutropha JMP134 (Reut_B4901) this gene is adjacent to HpnAB, IspH and HpnH (TIGR03470), although SHC itself is elsewhere in the genome. Notably, this gene (here named HpnJ) and three others form a conserved set (HpnIJKL) which occur in a subset of all genomes containing the SHC enzyme. This relationship was discerned using the method of partial phylogenetic profiling. This group includes Zymomonas mobilis, the organism where the initial hopanoid biosynthesis locus was described consisting of the genes HpnA-E and SHC (HpnF). Continuing past SHC are found a phosphorylase enzyme (ZMO0873, i.e. HpnG, TIGR03468) and another radical SAM enzyme (ZMO0874), HpnH. Although discontinuous in Z. mobilis, we continue the gene symbol sequence with HpnIJKL. One of the well-described hopanoid intermediates is bacteriohopanetetrol. In the conversion from hopene several reactions must occur in the side chain for which a radical mechanism might be reasonable. These include the four (presumably anaerobic) hydroxylations and a methyl shift
MKTLFLNPPSFEGFDGGAGSRYQAKREIKSFWYPTWLAQPAAMIPGSRLVDAPPHGVTIDDTLAIAKDYD
LVVLHTSTPSFPSDVKTAEALKEQNPATKIGFVGAHVAVLPEKTLKQGPAIDFVCRREFDYTIKEVAEGK
PLAEIDGLSYRGKDGKIVHNPDRPMIEDMDALPFVAPVYKRDLDIERYFIGYLKHPYISLYTGRGCPSKC
TFCLWPQTVGGHRYRTRSAESVIEEVKYALENFPEVREFFFDDDTFTDDKPRAEEIARKLGPLGVTWSCN
ARANVDYETLKVMKENGLRLLLVGYESGDQQILKNIKKGLTVEIARRFTRDCHKLGIKVHGTFILGLPGE
TRETIRKTIDFAKELNPHTIQVSLAAPYPGTELYDQAKQNGWITQDSAAMVDDTGHQMAAISYPHLSREE
IFDGVERFYKRFYFRPKKIGRIVREMLFDWDMMKRRLREGVEFFQFLRKRKK
>gnl|CDD|132512 TIGR03472, HpnI, hopanoid biosynthesis associated glycosyl transferase protein HpnI. This family of genes include a glycosyl transferase, group 2 domain (pfam00535) which are responsible, generally for the transfer of nucleotide-diphosphate sugars to substrates such as polysaccharides and lipids. The member of this clade from Acidithiobacillus ferrooxidans ATCC 23270 (AFE_0974) is found in the same locus as squalene-hopene cyclase (SHC, TIGR01507) and other genes associated with the biosynthesis of hopanoid natural products. Similarly, in Ralstonia eutropha JMP134 (Reut_B4902) this gene is adjacent to HpnAB, IspH and HpnH (TIGR03470), although SHC itself is elsewhere in the genome. Notably, this gene (here named HpnI) and three others form a conserved set (HpnIJKL) which occur in a subset of all genomes containing the SHC enzyme. This relationship was discerned using the method of partial phylogenetic profiling. This group includes Zymomonas mobilis, the organism where the initial hopanoid biosynthesis locus was described consisting of the genes HpnA-E and SHC (HpnF). Continuing past SHC are found a phosphorylase enzyme (ZMO0873, i.e. HpnG, TIGR03468) and another radical SAM enzyme (ZMO0874), HpnH. Although discontinuous in Z. mobilis, we continue the gene symbol sequence with HpnIJKL. Hopanoids are known to feature polar glycosyl head groups in many organisms
LTIIGGVAALLSLAGCGYTLLAAALVRRFFRRAARAPRAWPPVSVLKPLHGDEPELYENLASFCRQDYPG
FQMLFGVQDPDDPALAVVRRLRADFPDADIDLVIDARRHGPNRKVSNLINMLPHARHDILVIADSDISVG
PDYLRQVVAPLADPDVGLVTCLYRGRPVPGFWSRLGAMGINHNFLPSVMVARALGRARFCFGATMALRRA
TLEAIGGLAALAHHLADDYWLGELVRALGLRVVLAPVVVDTDVHETSFATLLAHELRWSRTIRAVNPVGY
AGSFITQPVPLAVLALLLGAAWAWPLVAAALAARALLRLVMSRATGAPLRAAWLLPLRDLLSFAIWVASF
FGSRVVWRGRRFRVDRDGRLSPV
>gnl|CDD|132513 TIGR03473, HpnK, hopanoid biosynthesis associated protein HpnK. The sequences represented by this model are members of the pfam04794 "YdjC-like" family of uncharacterized proteins. The member of this clade from Acidithiobacillus ferrooxidans ATCC 23270 (AFE_0976) is found in the same locus as squalene-hopene cyclase (SHC, TIGR01507) and other genes associated with the biosynthesis of hopanoid natural products. Similarly, in Ralstonia eutropha JMP134 (Reut_B4902) this gene is adjacent to HpnAB, IspH and HpnH (TIGR03470), although SHC itself is elsewhere in the genome. Notably, this gene (here named HpnK) and three others form a conserved set (HpnIJKL) which occur in a subset of all genomes containing the SHC enzyme. This relationship was discerned using the method of partial phylogenetic profiling. This group includes Zymomonas mobilis, the organism where the initial hopanoid biosynthesis locus was described consisting of the genes HpnA-E and SHC (HpnF). Continuing past SHC are found a phosphorylase enzyme (ZMO0873, i.e. HpnG, TIGR03468) and a radical SAM enzyme (ZMO0874), HpnH. Although discontinuous in Z. mobilis, we continue the gene symbol sequence with HpnIJKL
MRRLIVTADDFGLSLEVNEAVEKAHRDGILTAASLMVGAPAAEDAVERARRLPGLGVGLHLVLVDGRPVL
PPDQIPDLVDGQGRFGDDMVRDGVRYFFLPAVRAQLAREIRAQFEAFAATGLPLDHVNAHKHFHLHPTVL
SLILEIGREYGLRAVRLPREPRALLTLEPVRRLGTLWDAFLFPWLGRMRARLDRAGIAHNDYVFGLADTG
HMDEARLLAALERLPEGVSEIYFHPATAQDAEITPSMPGYRHADELAALLSPRVKAALKELGITLGGFAD
LVA
>gnl|CDD|132514 TIGR03474, Replication_initiation_protein, incFII family plasmid replication initiator RepA. Members of this protein are the plasmid replication initiator RepA of incFII (plasmid incompatibility group F-II) plasmids. R1 and R100 are plasmids in this group. Immediately upstream of repA is found tap, a leader peptide of about 24 amino acids, often not assigned as a gene in annotated plasmid sequences. Note that other, non-homologous plasmid replication proteins share the gene symbol (repA) and similar names (plasmid replication protein RepA)
YRQVKNPNPVFTPREGKKTLPFCRKLMAKAEGFTSRFDFSIHVAFARSLGLRHRMPPLLRRRAIDALLQG
MCFHYDPLANRVQRSITNLAIECGLATESKSGNLSITRATRALTFLSELGLITYQTEYDPQIGCNIPTDI
TFTPALFSALDVSEVAVAAARRSRVEWENKQRKKQGLDTLEMDELIAKAWRFVRERFRSYQTERKSHGIK
RARARRDADRERQDIETLVKRQLTREIAEGRFTGNREAVKREVERRVKERMLLSRNNNYTRLATA
>gnl|CDD|132515 TIGR03475, Positive_regulator_of_RepFIC_repA1_expression, RepA leader peptide Tap. This protein is a translated leader peptide that actis in the regulation of the expression of the plasmid replication protein RepA in incF2 group plasmids [Mobile and extrachromosomal element functions, Plasmid functions]
MLRKVQYLFLCHLLLPCNISAGRCD
>gnl|CDD|274596 TIGR03476, HpnL, putative membrane protein. This family of hydrophobic proteins is observed in two distinct contexts. It is primarily found in the presence of genes for the biosynthesis and elaboration of hopene where we assign the gene symbol HpnL. In a subset of the genomes containing HpnL a second, often plasmid-encoded, homolog is observed in a context implying the biosynthesis of 2-aminoethylphosphonate head-group containing lipids
MKRIGLLASLLGLALALALVAREGFHDVAAALASAGWGLLLLAAFHLLPLLLDALAWYALLPPQARVSLP
FLLWARWVREAVNELLPVAQIGGEVLGVRLLTGRGLPAPDAGASVVVDLTLTALAQLLFTLAGVLVLSLA
ATDGAAAFRWAGILAGLALSLPGLALFILLQRRGGFRKIERALGRLLAGRDWLSLGDNGARLDAALRALY
RRRGRVLAAFFWQLLGWVAGAAEVWLALRFLGHPVSFLDALAIESLIQAVRSAAFLVPGALGVQEGGYIL
LGPLFGLDPEAALALSLLKRARELLIGLPALLSWQIVE
>gnl|CDD|274597 TIGR03477, Dimethylsulfide_dehydrogenase_subunit_gamma, DMSO reductase family type II enzyme, heme b subunit. This model represents a heme b-binding subunit, typically called the gamma subunit, of various proteins that also contain a molybdopterin subunit and an iron-sulfur protein. The group includes two distinct but very closely related periplasmic proteins of anaerobic respiration, selenate reductase and chlorate reductase. Other members of this family include dimethyl sulphide dehydrogenase and ethylbenzene dehydrogenase [Energy metabolism, Electron transport]
IPVKKVPDGDIPLDPDASVWAKAPAGEVPLVSAPLVHPSLADTGVTQTLDVQAARNGERLAVRLEWADPT
RDVNTPGTDEFVDGVAVQFPVSRDSLPYICMGDADNPVNIWYWKADGRTEELVAGGFGGLTPLEREALGL
VLRTVATYDDGEWQVVLSRPLASKGELLASLEAGGDMPVAFAVWNGGNAERSGLKSVSGEWIDFRF
>gnl|CDD|132518 TIGR03478, Dimethylsulfide_dehydrogenase_subunit_beta, DMSO reductase family type II enzyme, iron-sulfur subunit. This model represents the iron-sulfur subunit, typically called the beta subunit, of various proteins that also contain a molybdopterin subunit and a heme b subunit. The group includes two distinct but very closely related periplasmic proteins of anaerobic respiration, selenate reductase and chlorate reductase. Other members of this family include dimethyl sulphide dehydrogenase and ethylbenzene dehydrogenase [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]
KRQLAYVIDLNKCIGCQTCTVACKNLWTNRPGREYMYWNNVETYPGKGYPRNWERKGGGFKRGGKLKQPG
IIPTLIDYGDPWEFNHEEVLYEGKDETVRPHPTPTWGPNWDEDQGAGEYPNNYYFYLPRICNHCTNPACL
AACPTGAIYKREEDGIVLVDQERCKGYRYCVEACPYKKVYFNPQSQKSEKCIGCYPRIEKGIAPACVKQC
PGRIRFVGYLDDEEGPVHKLVKRWKVALPLHPEYGTEPNVFYVPPMGPRGFGEDGEITDKTRIPLDYLEG
LFGPGVKQALATLHTEREKKRKGQGSELMDLLIGKRWADRF
>gnl|CDD|132519 TIGR03479, Dimethylsulfide_dehydrogenase_subunit_alpha, DMSO reductase family type II enzyme, molybdopterin subunit. This model represents the molybdopterin subunit, typically called the alpha subunit, of various proteins that also contain an iron-sulfur subunit and a heme b subunit. The group includes two distinct but very closely related periplasmic proteins of anaerobic respiration, selenate reductase and chlorate reductase. Other members of this family include dimethyl sulphide dehydrogenase, ethylbenzene dehydrogenase, and an archaeal respiratory nitrate reductase. This alpha subunit has a twin-arginine translocation (TAT) signal for Sec-independent translocation across the plasma membrane
RRDFLKGSGAALLGAGLSSAASGWAFGFLKPIQDPLKAYPYRDWEDLYRKEWTWDKVGRGAHLNNCTGSC
AFYVYVKNGIVWREEQSADYPQCNPDIPDYNPRGCQKGACYNNYMYGDDRLKYPLKRVGERGEGKWKRIS
WDEALTEIADKIIDTFEAQGPDGISLDTPHPHMAPISFAAGSRFANLIGGVSPDIFDDYGDLYTGAFHTF
GKAHDSATSDDWFNADYIIMWGSNPSVTRIPDAHFLSEARYNGARVVSIAPDYNPSTIHADLWLPVRVGT
DAALALGMVQVIIDEKLYDAAFLKEQTDLPLLVRMDTGKFLREADVEAGGSDKVFYIWDSKTGKAVKAKG
SMGSEDKTLKLDDFDPALEGTFEARLKNGNTIQVRTVFEGLRAELADYTPEKAAAITGVPPSVIRELARE
FAKAKKASIITGFNSAKWYHGDLMERALFLLLALTGNWGKTGTGDTHYIGQDKNWVLPGVKALAFPTLKA
PTRTDEMGVPTTVWTYYHAGNLKAWTGPGLDETGAYLDESIDKGWMPNYPRDGKDPKVYIVLRGNPFRRA
KGAKAVRENLLPKLELIVDINFRMDSTAMYADIVLPAAWHYEKHDLRTTSGHRFINFFDRPVKPMGESKT
DWQIFALLAKKIQERAAARGITRFNDHNFKRKRDFDELYDDFTMDGALATDEDALKYIVEISPASKGITY
EEFVERGQRFLSMGTGAGWTSPVDVGKPYYPFRWHVDDKKPYPTLTGRQQFYLDHDWFLELGETLPTHKD
GPGVDGGDYPFKFNSPHTRWSIHSTWRTNSHMLRLQRGEPVVYINPKDAAEKGIKDGDQVRIFNDLAEFE
AMAKIYPGLQPGTCIMYHGWEAHQYKNWKPYNSLLAGLIKPLHLVGGYGHLRFYPNYWNPAGVDREVRVD
VK
>gnl|CDD|274598 TIGR03480, HpnN, hopanoid biosynthesis associated RND transporter like protein HpnN. The genomes containing members of this family share the machinery for the biosynthesis of hopanoid lipids. Furthermore, the genes of this family are usually located proximal to other components of this biological process. The proteins appear to be related to the RND family of export proteins, particularly the hydrophobe/amphiphile efflux-3 (HAE3) family represented by TIGR00921
LLVRLVGFCARHAWWVLAIALLLTALSVIYTVTNLSVNTDTSDLLSPDLPFRQDERAYEKAFPQDEDTIV
VVIEGPTPEQASRAAERLAEKLAADRTHFEDVYFPGGGPFFRRNGLLFLPLEDLEKLTDRLASAQPFLGR
LAADPSLRGLFTALTLALQGLKAGQAQLPGLAPILDALAEALRAFLEGKPAPFSWQALMSGKDAALAPRR
RFIIVQPVLDYSSLEPAEKAINAIRAAAKDLRLDEDHGVTVRLTGEVALSDEELATVSEGATVAGLLSFV
LVLVLLWLALRSPRLVFAVLVTLIVGLILTAAFATLAVGHLNLISVAFAVLFIGLGVDFAIQFSLRYREE
RFRGGNHREALSVAARRMGAALLLAALATAAGFFAFLPTDYKGVSELGIIAGTGMFIALFVTLTVLPALL
RLLRPPRRRKPPGYATLAPLDAFLRRHRRPVLGVTLILGIAALALLPQLRFDFNPLNLQDPKTESVRTFL
ELLADPDTSPYSAEVLAPSAPEARALTERLEALPEVDQVVTLPDFVPDDQEAKLALIADLALVLGPTLNP
GEADPAPSAEEVAAALRRLAARLRAAAAKSQDPDAAAAGRLAASLDRLLAKAPAQAATLRALQGALLAGL
PGELDRLRDSLQAEPVTLEDLPPDLRRRWVAKDGRARLEVFPKEDLNDNEALRRFVRAVRKVAPDATGAP
VSILESGDTVVGAFLQAFIYALVAITVLLLLTLRRVRDVLLVLAPLLLAGLLTVAAMVLLGIPFNFANII
ALPLLLGLGVDFGIYMVHRWRNGVDSGNLLQSSTARAVFFSALTTATAFGSLAVSSHPGTASMGILLSLG
LGLTLLCTLIFLPALLGKRRRG
>gnl|CDD|274599 TIGR03481, HpnM, hopanoid biosynthesis associated membrane protein HpnM. The genomes containing members of this family share the machinery for the biosynthesis of hopanoid lipids. Furthermore, the genes of this family are usually located proximal to other components of this biological process. The proteins are members of the pfam05494 family of putative transporters known as "toluene tolerance protein Ttg2D", although it is unlikely that the members included here have anything to do with toluene per-se
IACLLSGVAPVLSAAALAATAAAETPEAVIDALHGALLDVMKEAKKLGYQGRYTKLAPAVREAFDLPAMA
RLTLGSSWTSLSPEQRRRFIGAFRELSIATYASQFKSYAGERFEVEEQQPSPRGRVIVRSTIVSDGGDPV
KFDYIMRQGQGKWRIVDILADGVSDLAVRRAEYGSILSSGGFDGLIDKLETKIAAYLK
>gnl|CDD|274600 TIGR03482, Chlorate_reductase_assembly_chaperone_protein, DMSO reductase family type II enzyme chaperone. Type II members of the DMSO reductase family are heterotrimeric proteins with bis(molybdopterin guanine dinucleotide)Mo, iron-sulfur, and heme b prosthetic groups bound by the alpha, beta, and gamma subunits respectively. Members of this protein family are not part of the mature protein, although they are the product of a fourth clustered gene. Proteins in this family are interpreted as a chaperone, analogous to NarJ of nitrate reductases
ARSSVYRLLAGAFGYPDESFHRAFSDGEAHAALRACLDGLPVPAPRLDPAASFEDLEAEYLRAFENGGGR
PAASLYEGDHRPASDRPGLLLELIRFYEHFGLRYDQGGREWPDHLTIELEFLHYLTLLEAAAPVDGRDPE
PYARAARDFLERHLAAWLPGVRQRLSDEPTTTTYVALGRLLEQFVEADREELAARLG
>gnl|CDD|274601 TIGR03483, FtsZ_alphas_C, cell division protein FtsZ, alphaProteobacterial C-terminal extension. This model describes a domain found as a C-terminal extension to the cell division protein FtsZ in many but not all members of the alphaProteobacteria [Cellular processes, Cell division]
RMPRVSDFPPVAQAEIRRGAPSEASSEEDRGPMGLLKRLTNGLSRRDEEAPAAAPEPAPRAPAQQPVHPY
NKNRRAFAPQASIYAPRRGGLDDQGRPQPQARAMQEDDQLEIPAFLRRQAN
>gnl|CDD|132524 TIGR03485, hypothetical_protein_L8106_30105, CRISPR-associated protein Cas8a1/Csx13, MYXAN subtype. Members of this family are found among cas (CRISPR-Associated) genes close to CRISPR repeats in Leptospira interrogans (a spirochete), Myxococcus xanthus (a delta-proteobacterium), and Lyngbya sp. PCC 8106 (a cyanobacterium). It is found with other cas genes in Anabaena variabilis ATCC 29413. In Lyngbya sp., the protein is split into two tandem genes. This model corresponds to the N-terminal region or upstream gene; the C-terminal region is described by TIGR03486. CRISPR/cas systems are associated with prokaryotic acquired resistance to phage and other exogenous DNA
LFQRLLSPCMTPLLRAGLAGLAMTLKSLEKEYPPPAPRPGTLTWELTQDSIQLDWKGQDSKDLDWLFKHS
FQIKEGLISLPGLHPTKMPHPDQIHFHQALTGTFLQHGKFFKSGGGASTAVSIDDIPVLVYYKKAISYAH
QAFAILFCEKRGWLFEEPIELSGWLYPGAPVRHIAFTHETKWEETAADALALLFAPVACSYYELRPSRGT
YAIVIPELTDLETFARFRRDLTELNYINMFVGGPGDAGLKYLTYMATTGNKKDNSLNGCEVIVIGTVAWN
KQQKVRALVMRIHPTEKVNRIYKLMRGIFPNKIHVK
>gnl|CDD|132525 TIGR03486, hypothetical_protein_L8106_30100, CRISPR-associated protein Cas8a1/Csx13, MYXAN subtype, C-terminal region. Members of this family are found among cas (CRISPR-Associated) genes close to CRISPR repeats in Leptospira interrogans (a spirochete), Myxococcus xanthus (a delta-proteobacterium), and Lyngbya sp. PCC 8106 (a cyanobacterium). It is found with other cas genes in Anabaena variabilis ATCC 29413. In Lyngbya sp., the protein is split into two tandem genes. This model corresponds to the C-terminal region or downstream gene; the N-terminal region is modeled by TIGR03485. CRISPR/cas systems are associated with prokaryotic acquired resistance to phage and other exogenous DNA
IAENLAQGRPWYANFAKPLKWKIDFKERKRERDELNKMIENSEIWDSEAEQWFVQSFHEALRRIYAKIAS
HTKRRGSETLGDRWKRENERIYSSLARAKTSEQFRTFIADLWARAGRIPSLQEHWGALLKLISKDNWEYA
RDLALVALASYQ
>gnl|CDD|132526 TIGR03487, cas_csp2, CRISPR-associated protein Cas8c/Csp2, subtype PGING. Members of this protein family are cas, or CRISPR-associated, proteins. The two sequences in the alignment seed are found within cas gene clusters that are adjacent to CRISPR DNA repeats in two members of the order Bacteroidales, Porphyromonas gingivalis W83 and Bacteroides forsythus ATCC 43037. This cas protein family is unique to the Pging (Porphyromonas gingivalis) subtype
HPYIRYACAILLVDNHLSEIEEITLEEIKFEIEKALNSFRIQAQEPFAGGSKAQFSFDKIEDGDTKKGIF
LSPHIISKDKHAQKLWGAAAKFLEIDYLGKDNDKCDDLLKKDEIGMSEIPISGEFLSFGDKGDIGRGKAK
ISIEEQGFGIISTLTPLKPAFQYKIGKDGQPEMFNFCIIPDIPINEMVDFIALFDKMQIQHLNGDALLGD
IVTQTDKKGKIKDIIPHRPKIFNGNFPNPPKSDALGAIALLGAIGEFAKHAEFSDLALGVLDSLKGATLY
LIKYGNAIPFTFHHYIIDLAKEAKLHSIIDSLFYSKLFKKDKRSSGDTDYDKFDFFTNRFLQLFNKAAFD
DFFSFRAEYPEQIKILFNIFFTKMEKIDADIIASAQILGKWLNLVAYFAAKEEADSREGAGNIFEEIRKV
KAKFLVELESSIFAAKRGDALIAQIIILAGRLSGMDAPEEALLFMEKTISGDIDLDCAKNLLIAFMRIR
>gnl|CDD|132527 TIGR03488, cas_Cas5p, CRISPR-associated protein Cas5, subtype PGING. CC Members of this protein family are cas, or CRISPR-associated, proteins. The two sequences in the alignment seed are found within cas gene clusters that are adjacent to CRISPR DNA repeats in two members of the order Bacteroidales, Porphyromonas gingivalis W83 and Bacteroides forsythus ATCC 43037. This cas protein family is unique to the Pgingi (Porphyromonas gingivalis) subtype, but shows some sequence similarity to genes of the Cas5 type (see TIGR02593)
IDLAILGKDPDKIAKIKLHIEPHAPISMVSELPGSFYKALLVPDKHIICGLFENVLGWHFDRKDREAIQK
DIEKIRKKQKKGHIPNTIGSIFIPLLMDFFDLDDQPIIDFDEPCFFNDLWKRAFRRADAGKIHFGGTENI
DYRLIMDKFKFMCENERDEENEDKIDNHALEKFFKENIDFFPFFYATPTNREYIFFEGNYECPIKMDEQL
FDLLSDILDQNNIGYLGNNEGWVNLKL
>gnl|CDD|132528 TIGR03489, cas_csp1, CRISPR-associated protein Cas7/Csp1, subtype PGING. Members of this protein family are Csp1, a CRISPR-associated (cas) gene marker for the Pging subtype of CRISPR/cas system, as found in Porphyromonas gingivalis W83 and Bacteroides forsythus ATCC 43037. This protein belongs to the family of DevR (TIGR01875), a regulator of development in Myxococcus xanthus located in a cas gene region. A different branch of the DevR family, Cst2 (TIGR02585), is a marker for the Tneap subtype of CRISPR/cas system
LAPFENHIANGGEKLFGNASSIKRRPDGRVYVSGQMQRHVLFSAIDRLNHADKAHGDTFVSNGDGISNLI
EIDLRADLGGFMHPNKGDYSDRRIAPLSVTPATALDESEIGRDLLVRIKFDKSEDAKDQALATKEFSEQD
KMHMNFFLDISALGISKAFTYEDGFNLGTKYFKHANDDEKKRRAKLFLEATKIMNDYANQARNAVCGEPE
KVLIVFDDRLSRKACRFYTADEKEKANIIAELDERGAKCFIGDDASDKSVADAYQDALAFLDKATLFDFA
EGAEIKTFAEAF
>gnl|CDD|274602 TIGR03490, Uncharacterized_lipoprotein_lpp, mycoides cluster lipoprotein, LppA/P72 family. Members of this protein family occur in Mycoplasma mycoides, Mycoplasma hyopneumoniae, and related Mycoplasmas in small paralogous families that may also include truncated forms and/or pseudogenes. Members are predicted lipoproteins with a conserved signal peptidase II processing and lipid attachment site. Note that the name for certain characterized members, p72, reflects an anomalous apparent molecular weight, given a theoretical MW of about 61 kDa
KKATKLLLSILPISSISFLSVVSCSTTSSNSKQPEKKPEIKPNENTPKIPKKPDNKEPSENNNNKSNNEN
KDEENPSSTNPEKKPDPSKNKEEIEKPKDEPKKPDKKPQADQPNNVHADQPNNNKVDFSDLDKLKKELSF
ENFTLYSQKDPKTALSSLKGDLSTIFKTIFYKTNKDILDKYNLKLESNKEPKEDFEKGLIDNVKIKFTKN
KKSKIIEFTFTGFKKKEQNTNKENKKENYIKAKEKLDEKLKGLFPSLVAYMLLYSENPNNYKSLMQQKNV
INFEELENKNGNLFNDKFVGFGVGTKELLFEYNEELNKLYKDKIVAAGYDDINGTLGLKVEISNNDENNK
ITKEPSITKEFSFKGFRKIDFKNPNKNVLSLSLTQNNFKKMIKSKLLKTNIENLKSGNNKEGEKLDVSKV
KKNFLKQKIFKNLLVNIIDNSNNIYRSKQTLSLKNNKKNNYKSILGLAGNMSLYPFHTRINKDSIKNIYL
TLNKKDENKLKVTLEFEVYIPVFAQGLSDLKDFTSGNEKTLKIKVNTEALI
>gnl|CDD|274603 TIGR03491, TIGR03491, RecB family nuclease, putative, TM0106 family. Members of this uncharacterized protein family are found broadly but sporadically among bacteria. The N-terminal region is homologous to the Cas4 protein of CRISPR systems, although this protein family shows no signs of association with CRISPR repeats
ITDSDLLSFLRCRRRAWLDLYGDKQQKEAPPDFLLQLRQDKQAFVQLILEDPAARAEAGLDACAAGADGI
YGGRLKHDLPQNLPHVSHPDLLVKDPGRSAWGDWAYEPVLIKLGKRPKDEYRLVLAFHALLLESFQGVAP
KKGLIILRDGNSLKVELIKLLPQLRQDLADFLLTLNADLEPEVFISRKKCTLCSWRKDCEAVAKEEGHLS
LVPGIGPSRYRLLQELGIHTLEDLAAADPNDLEDFGEQGLGVAEQLVQQARAQLEGRPILLAPPKALPEL
PRAPGELIFDIESDPDENLDYLHGFLVVDKGQENEKYRPFLAEDPNTEELAWQQFLQLLQSYPDAPIYHY
GETEKDSLRRLAKRYGTPEAEIEELLKRFVDIHTIVRRSWILPIESYSLKSIARWLGFEWRQKEASGAKS
LLWYRQWKKTGDRRLLERILRYNEDDCRATWIVADWL
>gnl|CDD|274604 TIGR03492, TIGR03492, conserved hypothetical protein. This protein family is restricted to the Cyanobacteria, in one or two copies, save for instances in the genus Deinococcus. This protein shows some sequence similarity, especially toward the C-terminus, to lipid-A-disaccharide synthase (TIGR00215 or pfam02684). The function is unknown
LFLSNGHGEDLIAARIAKALLQLSPDLNLEALPLVGEGRAYQNLGIPIIGPTKELPSGGFSYQSLRGLLR
DLRAGLVGLTLGQWRALRKWAKKGDLIVAVGDIVPLLFAWLSGKPYAFVGTAKSDYYWESGPRRSPSDEY
HRLEGSLYLPWERWLMRSRRCLAVFVRDRLTARDLRRQGVRASYLGNPMMDGLEPPERKPLLTGRFRIAL
LPGSRPPEAYRNLKLLLRALEALPDSQPFVFLAAIVPSLSLEKLQAILEDLGWQLEGSSEDQTSLFQKGT
LEVLLGRGAFAEILHWADLGIAMAGTATEQAVGLGKPVIQLPGKGPQFTYGFAEAQSRLLGGSVFLASKN
PEQAAQVVRQLLADPELLERCRRNGQERMGPPGASARIAESILKQL
>gnl|CDD|274605 TIGR03493, cellullose_BcsF, celllulose biosynthesis operon protein BcsF/YhjT. Members of this protein family are found invariably together with genes of bacterial cellulose biosynthesis, and are presumed to be involved in the process. Members average about 63 amino acids in length and are not uncharacterized. The gene has been designated both YhjT and BcsF (bacterial cellulose synthesis F) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
MNISDILQLVLLCALVFFPLGYLARRSLRRIRDTLRLRLAKPRYLKPAGVLRRAAKQEATKK
>gnl|CDD|132533 TIGR03494, Isochorismate_synthase/isochorismate_lyase, salicylate synthase. Members of this protein family are salicylate synthases, bifunctional enzymes that make salicylate, in two steps, from chorismate. Members are homologous to anthranilate synthase component I from Trp biosynthesis. Members typically are found in gene regions associated with siderophore or other secondary metabolite biosynthesis
DLLQTLAAVLSEFAEEDYYVYERDGEWYLGIGVQAMLTIDSDGRRVTFTGVTDRQRWSGSIGDAAREAVD
ALLLEGDRVFGQVGFEFAAHARGLQFNAGEWPLLRLFVPRTEIVVTEDNVTLFGVSAGERRRLCRLVAEG
TTTTQIAPLPQARAVDTATDPSAYRARVARAVAEIAAGRYHKVILSRAVPLPFAIDFPATLLLGRRHNTP
VRSFLLRLGGIEALGFSPELVMSVRADGKVVTEPLAGTRALGGGPEHDKQLRDELLSDSKEIVEHAISVK
EAIEELEQVCEPGTVVVEDFMTVRERGSVQHLGSTVSGQLAPSKDAWDAFEVLFPAITASGIPKAAALEA
IMRLEKTPRGLYSGAVLLLDADGTLDAALVLRAAYQDSGRTWLQAGAGIIAQSTPERELTETCEKLASIA
PYLIA
>gnl|CDD|274606 TIGR03495, Probable_spanin_inner_membrane_subunit, phage lysis regulatory protein, LysB family. Members of this protein family are phage lysis regulatory protein, including the well-studied protein LysB (lysis protein B) of Enterobacteria phage P2. For members of this family, genes are found in phage or in prophage regions of bacterial genomes, typically near a phage lysozyme or phage holin
RTLIVLLVLLVAGLGWQSQRLRNARADLERANRALKAQQAELAMKANQLIVLLALAKRNEEAQAQLRQQL
AQARALLAQREQRIERLKRENEDLRRWADTPLPDDVIRLRQRPALTGAADYRQWLSEGDALPDAG
>gnl|CDD|274607 TIGR03496, FliI_clade1, flagellar protein export ATPase FliI. Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively [Cellular processes, Chemotaxis and motility]
GRVTRVVGLVLEAVGLRAPVGSRCEIESSDGDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPL
RLPVGDSLLGRVIDGLGRPLDGKGPLDAGERVPLYAPPINPLKRAPIDEPLDVGVRAINGLLTVGRGQRM
GIFAGSGVGKSTLLGMMARYTEADVVVVGLIGERGREVKEFIEDILGEEGLARSVVVAATADESPLMRLR
AAFYATAIAEYFRDQGKDVLLLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGNGEEG
KGSITAFYTVLVEGDDQQDPIADAARAILDGHIVLSRELAEQGHYPAIDILASISRVMPDVVSPEHRQAA
RRFKQLLSRYQENRDLISIGAYQAGSDPELDQAIALYPRIEAFLQQGMRERASFEESLEAL
>gnl|CDD|274608 TIGR03497, FliI_clade2, flagellar protein export ATPase FliI. Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively [Cellular processes, Chemotaxis and motility]
GKVTRVIGLTIESKGPKASIGELCSILTKGGKPVLAEVVGFKEENVLLMPLGEVEGIGPGSLVIATGRPL
AIKVGKGLLGRVLDGLGRPLDGEGPIIGEEPYPLDNPPPNPLKRPRIRDPLETGIKAIDGLLTIGKGQRV
GIFAGSGVGKSTLLGMIARNAKADINVIALIGERGREVRDFIEKDLGEEGLKRSVVVVATSDQPALMRLK
AAFTATAIAEYFRDQGKDVLLMMDSVTRFAMAQREIGLAVGEPPTTRGYTPSVFSLLPKLLERSGNSQKG
SITGFYTVLVDGDDMNEPIADAVRGILDGHIVLSRELAAKNHYPAIDVLASVSRVMNEIVSEEHKELAGK
LRELLAVYKEAEDLINIGAYKRGSNPKIDEAIRYIEKINSFLKQGIDEKFTFEETVQLLKELL
>gnl|CDD|163293 TIGR03498, FliI_clade3, flagellar protein export ATPase FliI. Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively
GRVTAVTGLLIEVRGLSRAVRLGDRCAIRARDGRPVLAEVVGFNGDRVLLMPFEPLEGVGLGCAVFAREG
PLAVRPHPSWLGRVINALGEPIDGKGPLPQGERRYPLRASPPPAMSRARVGEPLDTGVRVIDTFLPLCRG
QRLGIFAGSGVGKSTLLSMLARNTDADVVVIALVGERGREVREFLEDDLGEEGLKRSVVVVATSDESPLM
RRQAAYTATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPVARGYTPSVFSELPRLLERAGPG
AEGKGSITGIFTVLVDGDDHNEPVADAVRGILDGHIVLDRAIAERGRYPAINVLASVSRLAPRVWSPEER
KLVRRLRALLARYEETEDLIRLGAYRKGSDPELDEAIRLVPKIYEFLTQGPDEPTSLQDPFADLAAIL
>gnl|CDD|274609 TIGR03499, FlhF, flagellar biosynthetic protein FlhF [Cellular processes, Chemotaxis and motility]
MKIKKFTAPTMREALKKVKEELGPDAVILSTRKVRKGLFGKKFVEVTAAIDEEEAAAASAEEEASKALEQ
ADPKPLSATAEPLELPAPQEEPAAPAAQAAEPLLPEEELRKELEALRELLERLLAGLAWLQRPPERAKLY
ERLLEAGVSEELARELLEKLPEDADAEDAWRWLREALEGMLPVKPEEDPILEQGGVIALVGPTGVGKTTT
LAKLAARFALEHGKKKVALITTDTYRIGAVEQLKTYAEILGIPVKVARDPKELREALDRLRDKDLILIDT
AG
>gnl|CDD|274610 TIGR03500, FliO_TIGR, flagellar biosynthetic protein FliO. This short protein found in flagellar biosynthesis operons contains a highly hydrophobic N-terminal sequence followed generally by two basic amino acids. This region is reminiscent of but distinct from the twin-arginine translocation signal sequence. Some instances of this gene have been names "FliZ" but phylogenetic tree building supports a single FliO family
LLLVLALILALAWLLRRFGSAGLNGQGGKGLKVLESLPLGPKESLVLVEVGDRQLLLGVTDGGITLLKE
>gnl|CDD|274611 TIGR03501, secreted_trypsin-like_serine_protease, GlyGly-CTERM domain. This homology domain, GlyGly-CTERM, shares a species distribution with rhombosortase (TIGR03902), a subfamily of rhomboid-like intramembrane serine proteases. It is probably a recognition sequence for protein sorting and then cleavage by rhombosortase. Shewanella species have the largest number of target proteins per genome, up to thirteen. The domain occurs at the extreme carboxyl-terminus of a diverse set of proteins, most of which are enzymes with conventional signal sequences and with hydrolytic activities: nucleases, proteases, agarases, etc. The agarase AgaA from Vibro sp. strain JT0107 is secreted into the medium, while the same protein heterologously expressed in E. coli is retained in the cell fraction. This suggests cleavage and release in species with this domain. Both this suggestion, and the chemical structure of the domain (motif, hydrophobic predicted transmembrane helix, cluster of basic residues) closely parallels that of the LPXTG/sortase system and the PEP-CTERM/exosortase(EpsH) system. For this reason, the putative processing enzyme is designated rhombosortase
GGGSLGWLSLLLLLLLGLRRRK
>gnl|CDD|274612 TIGR03502, lipase_Pla1_cef, extracellular lipase, Pla-1/cef family. Members of this protein family are bacterial lipoproteins largely from the Gammaproteobacteria. Characterized members are expressed extracellularly and have esterase activity. Members include the lipase Pla-1 from Aeromonas hydrophila (AF092033) and CHO cell elongation factor (cef) from Vibrio hollisae
MKKLLLSLAIASALGLAGCGDNSDGTEDVVTNTPVQIPLARIVFDPANGDVPLPNDLLMSGTKDGTLNIP
GENNDAATGNPRIALGALDGWSTTSPISIDFTLPKGHSLDAASVAQPGAVRLFEATQGGTLSDAECKANP
AGKACKLGAELVFGVDFVVQASGSSIAIIPLKPLKASSSYILAVTDAIQDSNGRAVGTSSSYALAKQDIN
TYPLATESQLLLQTLTNSYEGIAVLSGVDASDIIYSSWFTTQSVGDVLGAVKGLTASGFPTGNLPTAATV
PTPPGANVAQAYTKGLTVPDDFSAALAEVASAANVYKGTVRLPYYLETPSAWNPQPFNSAMPSLAKRWAA
MCDSAVAAIGGALQAGVLSQAPFATDPAEQLKLVGSTLTLSDGDTALDSERHLTKYNPIPKVKSYENVPV
LLTTPNGPVIAAFRAGTGLETFAAPTDGWPVVIYQHGITGAKENALAFAGTLAAAGVATIAIDHPLHGAR
SFDANASGVNATNANVLAYMNLASLLVARDNLRQSILDLLGLRLSLNGSALAGAPLSGINVIDGSKVSFL
GHSLGGIVGTSFIAYANTPLGSPTADALYAVNAASLQNPGGGIANFLLGSPDFGPVIKGNLTYAASTTFK
AFVDAQAAANGDELEAAACYTAFVAALTPAQEAEISAFFSQFAFAAQTALDSADPINYAATLKALGTPVL
MIEVVGDGATNKPDQVIPNNVANLPLAGTEPLAKLLGLTGVSATQASATAVSGFVRFNKGHHSSFVDPAP
SAQADLAATVEMQTQVADFLAD
>gnl|CDD|274613 TIGR03503, TIGR03503, TIGR03503 family protein. This set of conserved hypothetical protein has a phylogenetic range that closely matches that of TIGR03501, a putative C-terminal protein targeting signal
NEISLLDNRFRIDPTVEEITLLFFREPGSPPVILVRPDGSKYYAWRVHPEDVSWYDESTMDIISIKNPMP
GPWQAIGKITPGNRIKVISNLRLEVEPLPSPLFQGETLKVTAKLLNDGEPLKLPDFRDVVKLTVRFVSTN
NAEDENFGADPIVVGEFEDDGEGLDERPGDGIFTGEFNLDVAPGEYRPTYLSRNPVFLREVEQPVLVYPL
PVSYTVIQSEDESGAHQLMVDADAGHIDPGSLVIHGELVFPNGQIQQFSIELEEPDVRVDLPANYEFGKY
RVKGSVFGTTISGRELQLTLPEFSFNVEEPLNAEPTAEPAASEEELAAKAEQEQALLEEREAKDSIFWII
IIVGNVVILLLGIVGFFVWRKKKV
>gnl|CDD|274614 TIGR03504, FimV_Cterm, FimV C-terminal domain. This protein is found at the extreme C-terminus of FimV from Pseudomonas aeruginosa, and of TspA of Neisseria meningitidis. Disruption of the former blocks twitching motility from type IV pili; Semmler, et al. suggest a role in peptidoglycan layer remodelling required by type IV fimbrial systems
TKLDLARAYIEMGDLEGARELLEEVIEEGDEAQREEARRLLAKL
>gnl|CDD|274615 TIGR03505, FimV_core, FimV N-terminal domain. This region is found at, or about 200 amino acids from, the N-terminus of FimV from Pseudomonas aeruginosa, TspA of Neisseria meningitidis, and related proteins. Disruption of FimV blocks twitching motility from type IV pili; Semmler, et al. suggest a role for this family in peptidoglycan layer remodelling required by type IV fimbrial systems. Most but not all members of this protein family have a C-terminal region recognized by TIGR03504. In between is a highly variable, often repeat-filled region rich in the negatively charged amino acids Asp and Glu
DTLWGIAQRVRPDNSVSLYQMMLALYRANPDAFIGGNINRLKVGQILRIPSEEEIQAVSPAEAIREVEAQ
NKAW
>gnl|CDD|274616 TIGR03506, FlgEFG_subfam, flagellar hook-basal body protein. This model encompasses three closely related flagellar proteins usually denoted FlgE, FlgF and FlgG. The names have often been mis-assigned, however. Three equivalog models, TIGR02489, TIGR02490 and TIGR02488, respectively, separate the individual forms into three genome-context consistent groups. The major differences between these genes are architectural, with variable central sections between relatively conserved N- and C-terminal domains. More distantly related are two other flagellar apparatus familis, FlgC (TIGR01395) which consists of little else but the N-and C-terminal domains and FlgK (TIGR02492) with a substantial but different central domain
MALYTALSGLNAQSSALDVIANNIANANTTGFKRSRAEFQDLLSQSVSGSGQVGGGVRTSGVATDFSQGS
LQSTGNSLDLAISGDGFFVVQTPDGSEAYTRAGSFKLDADGYLVTSDGYPLLDWGGGPITLPPDAGSVSI
GEDGTVSATYSNGQTVELGQIALANFPNPDGLRKEGGNLYSATPGSGAALVGAPGTGGFGTLVSGALEGS
NVDLAEELVNMISAQRAYQAN
>gnl|CDD|274617 TIGR03507, decahem_SO1788, decaheme c-type cytochrome, OmcA/MtrC family. The protein SO_1778 (MtrC) of Shewanella oneidensis MR-1, and its paralog SO_1779 (OmcA), with which it intteracts, are large decaheme proteins, about 900 amino acids in length, involved in the use of manganese [Mn(III/IV)] and iron [Fe(III)] as terminal electron acceptors. This model represents these and similar decaheme proteins, found also in Rhodoferax ferrireducens DSM 15236, Aeromonas hydrophila ATCC7966, and a few other bacterial species [Energy metabolism, Electron transport]
VVTSDGKPTVDFKVTDAAGVPVDGLGKVAPSARFAIAKLIPQGATGNGGPTQWQSYITATKAAGTTTSTV
PGLAGTDNGGTLVDNGDGSYTYTFKTDITSAANTGNVAFDPTATHRVGIQLGRNAVNGTLGAPVANPVFD
FIPAGGAPAATRNVVSIAACNSCHGELALHGGRRIDVELCVTCHNPSTADPGSGNSLDFAVMIHKIHMGK
KLPSVDSGDPYIGYGNAKIDFSDVGFPQDPRNCTTCHSGANTKTADADNWKTVPSMAACGSCHDNVNFAT
GANHVNQTQADDTQCAACHNAGSTASAHTVHAGTLANLAAAYKVKAVVSAIAAAGKAPTVTVQVTDPAGG
PIALDTITDTKFITPRLSLYVNWGTDGVANGTTVYSRDSINGNGSDNLASTAQAGGDGTYTYTVTDATTT
LPAKVAAGVATIGIEGRVADCATPGTDNSAVLPYVGIAKVPKFFSVDGTAVTTRRAVVDVAKCNGCHGAL
SIHGGNRHNTFEQCVVCHNPNRTDSYAGTAGSIPGESIDFKYLIHSIHAGEFLSIYGFGGSPNFSEVGYP
GDIGNCAACHVDGSYNLPLAANLGPLTTAGGATNNGLYYISPIAAACTSCHDSDAALAHMASNGAIVFGT
KADAVSATGVESCATCHGPGTVADVDKVH
>gnl|CDD|274618 TIGR03508, decahem_SO, decaheme c-type cytochrome, DmsE family. Members of this family are small, decaheme c-type cytochromes, related DmsE of Shewanella oneidensis MR-1, which has been shown to be part of an anaerobic dimethyl sulfoxide reductase
GADTCLTCHDDEKATAFFKNPHGKIANGKGPMAGLQCESCHGPGGKHVKGGGEPMITFGSFSNLPAEKQN
SVCLSCHKDGTRSNWHGSVHARNDVACTSCHSIHVAKDPVLLKATQPEVCYTCHADQKAQFSKPSHHPIR
EGKMTCSDCHNPHGSFNPKLLKKTTLNETCYKCHAEKRGPFLWEHAPVTEDCSTCHSPHGSVNPRLLKAR
VPFLCQQCHSGDPHANVGPGPNGGTVFNARGRSCTNCHSQIHGSNHPS
>gnl|CDD|274619 TIGR03509, OMP_MtrB_PioB, decaheme-associated outer membrane protein, MtrB/PioB family. Members of this protein family are integral proteins of the bacterial outer membrane, associated with multiheme c-type cytochromes involved in electron transfer. The MtrB protein of Shewanella oneidensis MR-1 (SO1776) has been shown to form a complex with 1:1:1 stochiometry with the small, periplasmic decaheme cytochrome MtrA and large, surface-exposed decaheme cytochrome MtrC [Energy metabolism, Electron transport]
GEVGVGVGYADNDDSRAFNEYNGTDDSGFYAIGDADLKQRGEGGYYLSADAYNLGFDSRSLQVSMGQQGS
YRLNLGYDEIPHYDNNSYLSPYNGGGNNTLLPSNWAPGTTPQGVPLLQGSLAEDDLGLKRDKFGLGFAYT
PNSVWKVYANYKHENKEGTKSAGFSRSGLLGSGSQMLPKPVDYETDTVDAGVSYGGEPWQVQLGYYGSFF
RNDIAALTWQNPYNGAFGAAYTNRYALAPDNQAHQLAVSGGYNLGGTTVAGRLLYGQMTQNEAFAPFTYN
PASPLPADSLDGEVNTLNANLKITSRPSPDLRLTAAYDYSDRDNQTPVYNVAGSGATNVNTATNRPYDKT
KQKAELAADYRFTRSVKLTAGYDYKNDDRSYQDRQETDESTVWAKLRYRLNPGLSLNLKGSYSNRDGSNY
EANRSTSSTGNPLLRKFYLADRERDKLKAFADYQPTEGLTLGATARYAKDDYPDTLIGLTESTDYGYDLD
ASYTFTDGLSLHAFYNQQWIDSNQAGSATYSTPDWTSDTTDSVTTIGAGLTYEGLLDLKLSLGGDYSYSN
GDSDYKSTTNTGGPYPDYFSNQHRLKLYGKYQLSKSSSLRLDYRYERYSDNDYAYNNTAYDTIATVTTLG
DQNPNYNAHYLGVSYSYLF
>gnl|CDD|274620 TIGR03510, conserved_hypothetical_protein, XapX domain. This model describes an uncharacterized small, hydrophobic protein of about 50 amino acids, found between the xapB and xapR genes of the E. coli xanthosine utilization system, and homologous regions in other small proteins, such as the N-terminal region of DUF1427 (pfam07235). We name this domain XapX, as it comprises the full length of the protein encoded between the genes for the well-studied XapB and XapR proteins [Unknown function, General]
EYLLSLLAGLLVGALYSLLDVPSPAPPVLAGLVGLLGMLLGEQAVPWVR
>gnl|CDD|274621 TIGR03511, GldH_lipo, gliding motility-associated lipoprotein GldH. Members of this protein family are predicted lipoproteins, exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). Members include GldH, a protein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Not all Bacteroidetes with members of this protein family may have gliding motility [Cellular processes, Chemotaxis and motility]
KSQVRGALSLFIGACLLVSCTYRADVYISYQQVPEGRWQKRDVLDFEIEITDITRSYSLFLEIRNNNRYP
YRNLWLLAYEVSVGGRMIRADTIDLTLADSTGQWNGKGVGSIYQNRIRVPSSARFPHSGLYTIELKHGMR
DETLSGITEVGIRIEK
>gnl|CDD|132551 TIGR03512, GldD_lipo, gliding motility-associated lipoprotein GldD. Members of this protein family are found a number of Bacteriodetes lineage bacteria, including both species such as Flavobacterium johnsoniae, which possess a poorly understood form of rapid gliding motility, and other species which apparently do not. Mutation of GldD blocks both this motility and chitin utilization in the model species, Flavobacterium johnsoniae [Cellular processes, Chemotaxis and motility]
NILVLSIIGLLILVSSCKNDVMPKPKGFLKLDYPEAKYDTLTGDCPYTFEYNSIAKIVPTKTAEPCWIDI
YYPEMKANIQITYKPVNNNLEELLKDAQKLANKHNIKADAIDEDVYINDTKNGYGMFYEVDGDAASQIQF
YVTDSTKHFLRGSVYFRTSPNFDSIAPAASYMKEDVMHLMETLKWK
>gnl|CDD|274622 TIGR03513, GldL_gliding, gliding motility-associated protein GldL. This protein family, GldL, is named for the member from Flavobacterium johnsoniae, which is required for a type of rapid gliding motility found in certain members of the Bacteriodetes. However, members are found also in several members of the Bacteriodetes that appear not to be motile [Cellular processes, Chemotaxis and motility]
KRVMNIVYGWGAAVVILGALFKIMHWPMGNPMLFVGLITEALIFAISAFEKPADEYDWERVYPELASKNP
RKRAAAYAEEPSAVGLLSQKLDAMLKEAKKDATLMQSLGNGINPFEGAAKTLAPMTDSYAQQQKYIEQMS
SLAANMEGLNTIYEAQLKGASSHADANNEIAINSSSLKEEMEKMAANLTSLNEVYGGMLTAM
>gnl|CDD|274623 TIGR03514, GldB_lipo, gliding motility-associated lipoprotein GldB
LIALLFILASCNDKCKVNPDASNIPINIEIVRFDKEFFQAKPEDLPKLKKKYPLFFPKYINIQRVPDSEW
VSKLVYKDPALNELYTEVEAKFPDFEKIEKDLTAAFKYIKYYFPEFKIPKVYTVISGVDYNRKVILSDSL
LLISLDKYLGKDHKFYPDFPTYIKRRYDPDYIVPDVVTAYAMSFNKPSPNDRTLLAEMIYYGKILYFVDQ
LLPCTSDSLKIGYTSEELKWCKENESQIWRYFVENKLLYSTDPKLVRRYIGEAPFSKYLEIDNESPGRVG
QWIGWQIVKKYMKKHPVSLQELLAMQDAEKIFNKSKYKP
>gnl|CDD|132554 TIGR03515, GldC, gliding motility-associated protein GldC. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldC is a protein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldC do not abolish the gliding phenotype but do impair it. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility
KKSEIKFNVELDDNNVPEQILWEATDGPSQGQNPTKAISLSIWDHDGKNTMRIDLWTKDMPVDEMKRFFI
ETLGGMADTFLNATGDEKMAEDIKDLCDRLAQKLKEEM
>gnl|CDD|132555 TIGR03516, hypothetical_protein, peptidyl-prolyl isomerase, gliding motility-associated. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldI is a FKBP-type peptidyl-prolyl cis-trans isomerase (pfam00254) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockout of this gene abolishes the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. This family is only found in Bacteroidetes containing the suite of genes proposed to confer the gliding motility phenotype
MKHLIAVILLLLLLLGCKTPEARRPISRSSGTTIKLSAERNKKLIAAEEAAIKRIISADSIVKYETSQNG
FWYYYNQKDTGEGTTPEFGDLVTFEYDIRALDGDVIYSEEELGPQTYKVDQQDLFSGLRDGLKLMKEGET
ATFLFPSHKAYGYYGDQNKIGPNLPIISTVTLLNIKP
>gnl|CDD|274624 TIGR03517, GldM_gliding, gliding motility-associated protein GldM. This protein family, GldM, is named for the member from Flavobacterium johnsoniae, which is required for a type of rapid gliding motility found in certain members of the Bacteriodetes. However, members are found also in several members of the Bacteriodetes that appear not to be motile. The best conserved region, toward the N-terminus, is centered on a highly hydrobobic probable transmembrane helix. Two paralogs are found in Cytophaga hutchinsonii
MAKGKESPRQKMINLMYLVLIAMLALNVSSEVLEGFGLMNESLEAAVGNSEEYNNALLAELNKAVAKAPG
KDKAWSASAQKVRTKSDSLMDYMNDLKEEIIRKADGEKEDGKPKGAKEKDDLEAVMVGTLGPINGKGYEL
QASLNKYREDVLSLIKDDAKMKLIKSALDTKSDPYDKNPDGKGKDWEKYNFEGTPLVAAVTVLSKLQSDV
KKIESEVLNSLLSEVGQDDLSVDNYQAIVVPKSDAVFAGETYEAEVVLGASDSTLQPTVQVNGQLLAVEG
IGVVTFKAGGVGKQTIKGQIKIKNNGKDIRRSFSVDYFVTPPVAQIQADKMNVLYRGCGNPINISVPGVG
ANYVTASGAGLKSLGRGGVVCIAPPTAQGTEATISVTGQLPGGARQIGKYTFRVKAIPDPTPYIRGGDEN
GNTKRGKGAVLGKKRLLKAATIGAALDDDPFDANYNVTSFEMVFARGPRPVVTIVVTGNKFSARQKAQIR
QAGKGDRFYITDIVRTGPGGTKEKLKSINPVVI
>gnl|CDD|132557 TIGR03518, ABC_transporter_permease_protein, gliding motility-associated ABC transporter permease protein GldF. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldF is believed to be a ABC transporter permease protein (along with ATP-binding subunit, GldA and a sunstrate-binding subunit, GldG) and is linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldF abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility
MKAIFKKEFNSFFSSPIGYLVIAVFLLANGLFLWVFPGDFNILDYGYADLTPFFSLAPWVFLFLIPAITM
RSFAEERKLGTLELLLTRPISDWQIILGKYLGSLTLVILALLPTLLYVFTIYQLGNPVGNLDIGSTFGSY
IGLLLLGSVYTAIGLFASSLTENQIVAFIIAVFLCFLFYFGFDGLASLLWGGSAYTISELGLSYHYESIS
RGVIDSRDVIYFLSITVLFLALTKLQLKSR
>gnl|CDD|274625 TIGR03519, bacteroidetes-specific_membrane_protein, type IX secretion system membrane protein, PorP/SprF family. This model describes a protein family unique to, and greatly expanded in, the Bacteriodetes. Species in this lineage include several, such as Cytophaga hutchinsonii and Flavobacterium johnsoniae, that have type IX secretion systems (T9SS) and exhibit a poorly understood rapid gliding phenotype. Several members of this protein family are found in operons with other genes whose loss leads to a loss a this motility
MKKILLLLLLLLLLTVQALAQQDPQFSQYYYNPLLLNPAFAGSEDNTRIRLNYRSQWVGIEGAPTTQTLS
ADGPIGDNSGVGLSLVNDKIGVLTTTGLSANYAYHIKLSENSNLSFGLQAGFVQRSLDFSKLTFEDQNDP
SIASNNGSNKFYPDFGAGIYYYSKKFYFGLSVPNLNQPNFSFGDSDNDKLPKHYYLTAGYKFSLNEEIKI
TPSILYKYQDGAPYQLDLGANLLYNDKLWAGAGYRGNDAVIALVGFNLNKNLSIGYSYDFSTSSLSAYNG
GSHEISVSYRF
>gnl|CDD|274626 TIGR03520, GldE, gliding motility-associated protein GldE. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldC is a protein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. GldE was discovered because of its adjacency to GldD in F. johnsonii. Overexpression of GldE partially supresses the effects of a GldB point mutant suggesting that GldB and GldE interact. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Not all Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility and in fact some do not appear to express the gliding phenotype
FILLILSALVSGSEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILIANNFINIAIVLLFTS
LSDNLFGSFNTELLRFLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRA
ITNFIHKKFGKQKSNISVDQLSQALELTDEEDTTKEEQKILQGIVSFGNTDTKQVMRPRLDIFALDIETS
FSEIIPKIIENGYSRIPVYKETIDNITGVLYIKDLLPHLNKKNFDWQSLLREPYFVPENKKLDDLLRDFQ
EKKNHLAIVVDEYGGTSGLVTLEDIIEEIVGDISDEFDDEDLIYSKIDDNNYVFEGKTSLKDFYKILKLE
EDMFDEVKGEAETLAGFLLEISGGFPKKGEKITFENFEFTIEAMDKKRIKQVKVTIN
>gnl|CDD|274627 TIGR03521, gliding_motility_protein_GldG, gliding-associated putative ABC transporter substrate-binding component GldG. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldG is a protein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldG abolish the gliding phenotype. GldG, along with GldA and GldF are believed to compose an ABC transporter and are observed as an operon. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility
LKSFIILLAILVVVNLLASEFFFRFDLTEDKRYTLSPASKEVVKKLDDPVSIDIFLDGELPADFRRLQKE
TRQLLEEFAAYNPNIKFRFVNPLEEEDEQGEEILDSLAQYGIKPANVTVNENGKQSQKLIFPWAIVSYRG
KETGVPLLKNILGASPEERVNQSIQNLEYEFADAISKLINPREKRIAVLKGNGELADLQIADLVSTLKEY
YFIAPFTLDSVATNPAKTLAALKKFDLIVIAKPTEAFSEREKYILDQYIMNGGKALFLVDAVAMEMDSLY
NGDGATFALPRDLNLDDLLFKYGIRINPDLVEDLNSAPIVLATGNQGNNTQYQPLPWPYYPQVYSFNKHP
ITKNLDAVKFEFASTIDTLKNGIKKTPLLQTSPYSKIEGTPAQISLSEVTEEPDPESYNLGNLPLAVLLE
GSFTSAYKNRILPFEIPFKRDQGKPTKMIVVADGDVIRNQLDNNGKPLELGYDRFTGNLYGNKEFLLNAV
NYLLDDTGLINIRSKEITLPPLDKQKIAEDRTTWQLINIGLPILLLLLFGLSFTYIRKRKYA
>gnl|CDD|132561 TIGR03522, GldA_ABC_ATP, gliding motility-associated ABC transporter ATP-binding subunit GldA. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility
MSIRVSSLTKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNP
KEVQRNIGYLPEHNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQ
RVGLAQALIHDPKVLILDEPTTGLDPNQLVEIRNVIKNIGKDKTIILSTHIMQEVEAICDRVIIINKGKI
VADKKLDELSAANKKQVIEVEFEEQIDLQLFETLEEISSVKNTGGNTWKLTFETPNDTRPEIFKLAQQKG
LKLISLQQNEKNLEQVFREIT
>gnl|CDD|274628 TIGR03523, hypothetical_protein_P700755_05002, gliding motility associated protien GldN. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldN is a protein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldN abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein also include those which are not believed to express the gliding phenotype, such as Prevotella intermedia and Porphyromonas gingivales
FSKLIFAIFCAVVLISSLATVARIPTEGEASGRGAETRTSDDDKPFPVRYIRERDIMWSKVVWRRIDLRE
KINLPLYYPTDPVGDRRSLFDYIFKAIVEGSIIEVYADDGFEIFTDTEPITLQEFQDRFYLYYEPSDRLD
GDSIFSADVYGYYIKEEWYFDKQRSDMKFRIIALCPIMTDSNGQQFTGAEVRYPLFWIKYFDARPVLAEA
IVFNPLNNAMPLTYDDLFNLRLFKSVIYKTENPYNRALADYCPGDSLMALLESNRIKEELLEFESNLWEY
>gnl|CDD|132563 TIGR03524, gliding_motility_protein_GldJ, gliding motility-associated lipoprotein GldJ. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldJ is a lipoprotein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae. Knockouts of GldJ abolish the gliding phenotype. GldJ is homologous to GldK. There is a GldJ homolog in Cytophaga hutchinsonii and several other species that has a different, shorter architecture and is represented by a separate model. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility
VNMKNVFKITFIVFVSLLFVSCKKKSSSSNKSRATGWSFNDKNGNYIRNNSFKGQEAPPGLVFVEGGTFT
MGQVQDDVMHDWNNTPTQQHVQSFYMDETEVTNSMYLEYLQYLKDVFPPSEANYKNIYSGALPDTLVWRN
RLGNNETMTENYLRHPAYADYPVVGVSWIQAVEFSKWRTNRVNEKVLEDKGNIKKGAKIDVTASSFFDTD
VYLVDPSKTYGGDTTVYKRGIGRTRRKKGEARPAVPEEKDAYQQRKDGIITQRYRLPTEAEWEYAAKANV
GNREYNNYRGRKKYPWNGKYTRSKNRRNRGDQLANFKQGKGDYGGIAGWSDDGADITNEIKSYPPNDFGL
YDMAGNVAEWVADVYRPIIDNEANDFNYYRGNLYTKNMIDSDGNVVFAGTQEIEYDTLPNGKVVARYLPG
EIAQVPVDKNETYLRTNFSKSDNANIRDGDKQSSRYYEFGDDEDEIARRPSMYNSPKSPIEIDPVGGMIV
LYDDDKKRTTLIDDRVRVYKGGSWRDREYWLDPAQRRYLPQYMATDYIGFRCAMSRVGPKSNGKKKPRN
>gnl|CDD|274629 TIGR03525, lipoprotein_putative, gliding motility-associated lipoprotein GldK. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldK is a lipoprotein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae. Knockouts of GldK abolish the gliding phenotype. GldK is homologous to GldJ. There is a GldK homolog in Cytophaga hutchinsonii and several other species that has a different, shorter architecture and is represented by a separate model. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility
MKKYLVFAALVVLVYSCGSGDKGELVGVEGKKWYPEKPYGMVLVPGGSFIMGKSDEDIAGVMNAPTKTVT
VRSFYMDETEITNSEYRQFVEWVRDSIVRTKLAELADLAGIGPGDGGGSIQDYAFKDAESDNATPYQKYM
YDNYYSLGETDDYAGRKLNKKTELIWDTSEYPDEYYVEVMDSLYLPEDESYNGLRTFDVTKLKYRYSWMD
IDAAARSKGSRKDFIKTEEVQVYPDTTVWIKDFNYSYNEPMHNDYFWHQAYDDYPVVGVTWKQARAFCNW
RTKYKNDFRKKKGPANVNTFRLPTEAEWEYAARGGLEGATYPWGGPYTKNDRGCFMANFKPVRGDYAADE
ALYTVEAKSYEPNDYGLYNMAGNVSEWTNSSYDPSSYEYMSTMNPNVNDSENTRKVVRGGSWKDVAYFLQ
VSTRDYEYADSARSYIGFRTVQDYLGTAVT
>gnl|CDD|132565 TIGR03526, selenium_YgeY, putative selenium metabolism hydrolase. SelD, selenophosphate synthase, is the selenium donor protein for both selenocysteine and selenouridine biosynthesis systems, but it occurs also in a few prokaryotes that have neither of those pathways. The method of partial phylogenetic profiling, starting from such orphan-selD genomes, identifies this protein as one of those most strongly correlated to SelD occurrence. Its distribution is also well correlated with that of family TIGR03309, a putative accessory protein of labile selenium (non-selenocysteine) enzyme maturation. This family includes the uncharacterized YgeY of Escherichia coli, and belongs to a larger family of metalloenzymes in which some are known peptidases, others enzymes of different types
FNQIKSEAEKYRGDMIRFLRDLVAIPSESGDEGRVALRIKQEMEKLGFDKVEIDPMGNVLGYIGHGPKLI
AMDAHIDTVGIGDMDQWQFDPYEGYEDEEIIYGRGASDQEGGIASMVYAGKIIKDLGLLDDYTLLVTGTV
QEEDCDGLCWQYIIEEDKIKPEFVVITEPTDMNIYRGQRGRMEIKVTVKGVSCHGSAPERGDNAIYKMAP
ILKELSQLNANLVEDPFLGKGTLTVSEIFFSSPSRCAVADGCTISIDRRLTWGETWEYALEQIRNLPAVQ
GAEAEVEMYEYDRPSYTGLVYPTECYFPTWVLPEDHLITKAALETYKRLFGKEPGVDKWTFSTNGVSIMG
RHGIPVIGFGPGDEDQAHAPNEKTWKEDLVKAAAMYAAIPTVYLQ
>gnl|CDD|274630 TIGR03527, selenium_YedF, selenium metabolism protein YedF. Members of this protein family are about 200 amino acids in size, and include the uncharacterized YedF protein of Escherichia coli. This family shares an N-terminal domain, modeled by pfam01206, with the sulfurtransferase TusA (also called SirA). The C-terminal domain includes a typical redox-active disulfide motif, CGXC. This protein family found only among those genomes that also carry the selenium donor protein SelD, and its connection to selenium metabolism is indicated by the method of partial phylogenetic profiling vs. SelD. Its gene typically is found next to selD. Members of this family are found even when selenocysteine and selenouridine biosynthesis pathways are, except for SelD, completely absent, as in Enterococcus faecalis. Its role in selenium metabolism is unclear, but may include either detoxification or a role in labile selenoprotein biosynthesis
IDARGLACPQPVILTKKALDELGEEGVLTVIVDNEAAKENVSKFATSLGYEVEVEEKEEGYWILIIKKGE
GAAEASPDEAAKEGKLVVVITSDKLGEGDEELGRILMKGFIYTLSELDPLPKRIIFVNGGVKLTTEGSEV
LEDLKELEKKGVEILSCGTCLDFYGLKDKLKVGTITNMYDIVEALTTADKVIRL
>gnl|CDD|274631 TIGR03528, 2_3_DAP_am_ly, diaminopropionate ammonia-lyase. Members of this protein family are the homodimeric, pyridoxal phosphate enzyme diaminopropionate ammonia-lyase, which adds water to remove two amino groups, leaving pyruvate
SIKIIINDNKKATNGTDLSLLSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGL
NAFKVLGGSYAIGKYLAEKLGKDISELSFEKLKSNEIREKLGDITFVTATDGNHGRGVAWAANQLGQKSV
VYMPKGSAQERLENIRAEGAECTITDLNYDDAVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTL
ALEALEQLKEQGVEKPTHVFLQAGVGSFAGAVQGYFASVYGEERPITVIVEPDKADCIYRSAIADDGKPH
FVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPDWVAAKGMRILGNPLKGDPRVISGESGAVGTGL
LAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG
>gnl|CDD|274632 TIGR03529, gliding_motility-associated_lipoprotein_GldK, gliding motility-associated lipoprotein GldK. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldK is a lipoprotein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae. Knockouts of GldK abolish the gliding phenotype. GldK is homologous to GldJ. This model represents a GldK homolog in Cytophaga hutchinsonii and several other species that has a different, shorter architecture than that found in Flavobacterium johnsoniae and related species (represented by (TIGR03525). Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility
RLLSITLGLAVATLLPGCGLFNKKGSASEKANRRGEVTGVPKRESWQQNVPVGMVVIPAGTFHMGQADED
VPATQINLNKQITISEFFMDKTEVTNNKYRQFLEVVLEGQLATGTPLPPEYDMEELYPDTTVWSTSFSHH
MGDPLMEYYFDHPAFDNYPVVGVDWNAAKQFCEWRTYHMNAYRNEESQYDMPRFRLPSEAEWEYAARGGR
DMAKYPWGGPYLRNKRGCMLANFKPGRGNYYDDGFPYTAPVAVYFPNDFGLYDMAGNVAEWVLDAYAATS
VPIVWDLNPVYEDPNEVRKIIRGGSWKDIAYYLETGTRTFEYEDVSQAHIGFRTVMTYLGRSSG
>gnl|CDD|132569 TIGR03530, gliding_motility-associated_lipoprotein_GldJ, gliding motility-associated lipoprotein GldJ. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldJ is a lipoprotein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae. Knockouts of GldJ abolish the gliding phenotype. GldJ is homologous to GldK. This model represents the GldJ homolog in Cytophaga hutchinsonii and several other species which is of shorter architecture than that found in Flavobacterium johnsoniae and is represented by a separate model (TIGR03524). Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility
IKHAAMLIAAASILFSCNKTPGYGNPTAIKPGGSSATTGAAFSFEENDENGFFVADNAEQIEGPNLKFIE
GGRAVLGSFEEDLMAFGDNLERTVTIANFYMDETEIANIDWLEFLFNMKKDSSADFIEKAEPDEDVWAGE
LAFNDLYQDHYFRFPGFNFFPVAGVNWIQANAYCIWRTEVVNELLAEEAGIDSPEGGGQIPIERGVALAD
FRLPNEAEWEYAAKALIGNQWLDENQEHGRIYPWDGHALRNPYNVKRKGKQMGDFLANFKRGRGDYAGIA
GNKLNDGAIIPTNIYDFAPNDFGLYCMAGNMNEWVYDVYRPLSFQDFDDLNPLRKDGFFDEEEGYDKAGF
QSLLDDEFRVYKGGSWKDVAYWLSPGTRRFLAEDSATAAIGFRCAMIQAGEK
>gnl|CDD|211833 TIGR03531, O-phosphoseryl-tRNASec_selenium_transferase, O-phosphoseryl-tRNA(Sec) selenium transferase. In the archaea and eukaryotes, the conversion of the mischarged serine to selenocysteine (Sec) on its tRNA is accomplished in two steps. This enzyme, O-phosphoseryl-tRNA(Sec) selenium transferase, acts second, after a phosphophorylation step catalyzed by a homolog of the bacterial SelA protein [Protein synthesis, tRNA aminoacylation]
LIPKSYVKQGRLALNSHEKLIERLLEQRKIPEEGWDDETIELFLHELSVMDTNNFPNNVGVGEREGRVFS
KLVARRHYRFCHGIGRSGDLVAPQPKAAGSSLLYKLTNKLVKDFLKLLGLRSIKSAFVVPLATGMSLSLC
LSALRHKRPKAKYVIWPRIDQKSCIKAISTAGFEPRVIETVLDGDELTTDVEDIERAIEEIGPDNILCVL
STTSCFAPRSPDDIEEIAKICANYDIPHIVNNAYGLQSNKYMELINKAIKVGRVDAVVSSTDKNFMVPVG
GAIIYSFDENFIQEISKSYPGRASASPSLDVLITLLSLGSKGYLELLKERKEMYKYLKELLQKLAERHGE
RLLDTPENPISSAMTLSTLKGKDPTMLGSMLYSRRVTGPRVVTNGDSKTVGGCEFKGYGSHTSNYPCPYI
TAAAAIGMTKEDVDTFVSRLEKSL
>gnl|CDD|132571 TIGR03532, DapD_Ac, 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase. This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-acetyltransferase. Note that IUBMB lists this alternate name as the accepted name. Unfortunately, the related succinyl transferase acting on the same substrate (EC:2.3.1.117, TIGR00695) uses the opposite standard. We have decided to give these two enzymes names which more clearly indicated that they act on the same substrate
AQEIIRYIGNAKKSTPVKVYVKGDLEQVDFPESIKKFGSGHSGVLFGEWEDIEPFIEANKDKIKDYRIEN
DRRNSAIPLLDLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKN
VHIGAGAVLAGVIEPPSAKPVVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKV
IKQVDEKTKDKTELEDDLRKL
>gnl|CDD|274633 TIGR03533, L3_gln_methyl, protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific. Members of this protein family methylate ribosomal protein L3 on a glutamine side chain. This family is related to HemK, a protein-glutamine methyltranferase for peptide chain release factors [Protein synthesis, Ribosomal proteins: synthesis and modification]
LHTIRDFLRWAVSRFNAAGLFFGHGTDNAWDEAVYLVLHALHLPLDILEPFLDARLTPSEKERILELIER
RIEERIPVAYLTNEAWFAGLEFYVDERVLIPRSPIAELIEDGFAPWLEPEPVKRILDLCTGSGCIAIACA
YAFPEAEVDAVDISPDALAVAEINIERHGLEDRVTLIQSDLFAALPGRKYDLIVSNPPYVDAEDMADLPA
EYHHEPELALASGEDGLDLVRRILAEAADHLNENGVLVVEVGNSMEALEEAYPDVPFTWLEFENGGDGVF
LLTR
>gnl|CDD|274634 TIGR03534, RF_mod_PrmC, protein-(glutamine-N5) methyltransferase, release factor-specific. Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3 [Protein fate, Protein modification and repair]
DAELLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPR
PETEELVEAALERLKKGPRVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGLENVEF
LQGDWFEPLPSGKFDLIVSNPPYIPEADIHLLDPEVRDFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGG
WLLLEIGYDQGEAVRALFEAAGFADVETRKDLAGKDRVVL
>gnl|CDD|274635 TIGR03535, DapD_actino, 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase. This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. This model represents a clade of the enzyme specific to Actinobacteria. Alternate name: tetrahydrodipicolinate N-succinyltransferase
RSAWGWGLATVTADGTVLDTWFPEPELGEADPAGTERLDVDPAELAALAGRDADRGVERVAVRTVIADLD
AAPADAYDAYLRLHLLSHRLVKPHTVNLDGIFGLLPNVVWTNHGPCAVDDFELTRARLRARGPVTVYSVD
KFPRMVDYVVPTGVRIGDADRVRLGAHLAEGTTVMHEGFVNFNAGTLGASMVEGRISAGVVVGDGSDIGG
GASIMGTLSGGGKEVISIGERCLLGANSGLGISLGDDCVVEAGLYVTAGTKVTVWGPVAAGGPDGEVVKA
RELSGASNLLFRRNSVSGAVEALARKGQGIELNEALHAN
>gnl|CDD|211834 TIGR03536, DapD_gpp, 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase. 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (DapD) is involved in the succinylated branch of the "lysine biosynthesis via diaminopimelate (DAP)" pathway (GenProp0125). This model represents a clade of DapD sequences most closely related to the actinobacterial DapD family represented by the TIGR03535 model. All of the genes evaluated for the seed of this model are found in genomes where the downstream desuccinylase is present, but known DapD genes are absent. Additionally, many of the genes identified by this model are found proximal to genes involved in this lysine biosynthesis pathway
LFSLALGVGTQNRKGEWLEVFYPTPLLNPSAELVAAVAEVLGYAGGNQAIELTPAQCQALAVALKEAGDA
AQAALAAAFAESSRPLVAVLLAEDAAPSSTPEAYLKLHLLSHRLVKPHGVNLDGIFGLLPNVAWTNEGAI
DLDELAERQLEARLNGEVLEVDSVDKFPKMTDYVVPKGVRIADTARVRLGAYVGEGTTVMHEGFINFNAG
TEGPGMIEGRISAGVFVGKGSDLGGGCSTMGTLSGGGNIVISVGEGCLIGANAGIGIPLGDRCTVEAGLY
ITAGTKVAVLDDKGELVKTVKARDLAGQSDLLFRRNSQNGAVECLTNKSAIALNEALHAHN
>gnl|CDD|274636 TIGR03537, DapC, succinyldiaminopimelate transaminase. The four sequences which make up the seed for this model are not closely related, although they are all members of the pfam00155 family of aminotransferases and are more closely related to each other than to anything else. Additionally, all of them are found in the vicinity of genes involved in the biosynthesis of lysine via the diaminopimelate pathway (GenProp0125), although this amount to a separation of 12 genes in the case of Sulfurihydrogenibium azorense Az-Fu1. None of these genomes contain another strong candidate for this role in the pathway. Note: the detailed information included in the EC:2.6.1.17 record includes the assertions that the enzyme uses the pyridoxal pyrophosphate cofactor, which is consistent with the pfam00155 family, and the assertion that the amino group donor is L-glutamate, which is undetermined for the sequences in this clade
RLYDFGTGDPKEPTPDFIRKALRDAVPEVSQYPSVLGTKALREAIAGYLERRFGVKLNPDTQILPSAGSK
EAIFHFPLAFLDPEEDRKRVIYPTPGYPVYERGTLFAGGEPTPVKLKKEDGFLLRLDAVEKSILRETKIV
WINYPHNPTGATAPASYLKRVAAMAREYGFIVCSDECYTDIYFGEPPHSMLEFGRENVLAFHSLSKRSGM
TGYRSGFMAGDEKLVSFYRKLRASFGVASPDFIQAAATAAWSDDAHVAERRKIFKRKRDLFLEFFARVGL
EYLYPDATFYLWVKAPSGIDAKSYALRLLENGIVVSPGENFGSGEEGYVRVALVPTLEECEEAIRLWERL
>gnl|CDD|274637 TIGR03538, DapC_gpp, succinyldiaminopimelate transaminase. This family of succinyldiaminopimelate transaminases (DapC) includes the experimentally characterized enzyme from Bordatella pertussis. The majority of genes in this family are proximal to genes encoding components of the lysine biosynthesis via diaminopimelate pathway (GenProp0125)
NPNLSRLQPYPFEKLAALLAGVTPPASKPPIALSIGEPKHPTPAFVLEALRENLHGLSTYPTTKGLPELR
QAIARWLERRFDLPTGVDPERHVLPVNGTREALFAFAQAVINPGQAPLVVMPNPFYQIYEGAALLAGAEP
YFLNCTAENGFLPDFDAVPESVWRRCQLLFVCSPGNPTGAVLSLDTLKKLIELADQYGFIIASDECYSEL
YFDEGNPPAGLLQAAAQLGRDDFRRCLVFHSLSKRSNLPGLRSGFVAGDAEILKAFLRYRTYHGCAMPIP
TQLASIAAWNDEQHVRENRALYREKFAAVLEILGQVLDLELPDAGFYLWPKVPGDDEAFARALYEEENVT
VLPGRFLAREAEGVNPGEGRVRIALVAPLEECVEAAERIRSFI
>gnl|CDD|132578 TIGR03539, DapC_actino, succinyldiaminopimelate transaminase. This family of actinobacterial succinyldiaminopimelate transaminase enzymes (DapC) are members of the pfam00155 superfamily. Many of these genes appear adjacent to other genes encoding enzymes of the lysine biosynthesis via diaminopimelate pathway (GenProp0125)
LPDFPWDSLAPYKAKAASHPDGIVDLSVGTPVDPVPPLIRAALAAAADAPGYPQTWGTPELREAIVDWLE
RRRGVPGLDPTAVLPVIGTKELVAWLPTLLGLGPGDTVVIPELAYPTYEVGALLAGATPVAADDPTELDP
VGPDLIWLNSPGNPTGRVLSVDELRAIVAWARERGAVVASDECYLELGWEGRPVSILDPRVCGGDHTGLL
AVHSLSKRSNLAGYRAGFVAGDPALVAELLTVRKHAGLMVPAPVQAAMVAALGDDGHVAEQKARYAARRA
QLKPALEKAGFRIDHSEAGLYLWATRGEDAWDTVDRLAELGILVAPGDFYGPAGSQHVRVALTATDERIA
AAVARLT
>gnl|CDD|274638 TIGR03540, DapC_direct, LL-diaminopimelate aminotransferase. This clade of the pfam00155 superfamily of aminotransferases includes several which are adjacent to elements of the lysine biosynthesis via diaminopimelate pathway (GenProp0125). Every member of this clade is from a genome which possesses most of the lysine biosynthesis pathway but lacks any of the known aminotransferases, succinylases, desuccinylases, acetylases or deacetylases typical of the acylated versions of this pathway nor do they have the direct, NADPH-dependent enzyme (ddh). Although there is no experimental characterization of any of the sequences in this clade, a direct pathway is known in plants and Chlamydia and the clade containing the Chlamydia gene is a neighboring one in the same pfam00155 superfamily so it seems quite reasonable that these enzymes catalyze the same transformation
KLADRLENLPPYLFAEIDKKKAEKKAEGVDVIDLGIGDPDLPTPKHIVEALKKAAEKPENHRYPSYEGML
AYRKAVADWYKRRFGVELDPETEVLSLIGSKEGIAHFPLAFVNPGDIVLVPDPGYPVYRIGTLFAGGEPY
EMPLKEENGFLPDFDAIPEDIAKKAKIMFLNYPNNPTGAVADKEFFKEVVEFAKKYNIIVCHDNAYSEIY
FDGYKPPSFLEVDGAKDVGIEFHSLSKTYNMTGWRIGMAVGNADLIAGLGKVKTNIDSGVFQAIQYAGIA
ALNGPQDVVKEIRKIYQERRDLLLEALKKIGIDLKKPKATFYLWVPVPEGYTSAEFAKRLLEETGVVVTP
GVGFGEYGEGYIRISLTVPDERLEEAVARIAKL
>gnl|CDD|132580 TIGR03541, reg_near_HchA, LuxR family transcriptional regulatory, chaperone HchA-associated. Members of this protein family belong to the LuxR transcriptional regulator family, and contain both autoinducer binding (pfam03472) and transcriptional regulator (pfam00196) domains. Members, however, occur only in a few members of the Gammaproteobacteria that have the chaperone/aminopeptidase HchA, and are always encoded by the adjacent gene
AELLFQAVRQIEQASTLEAIQDAVREFAQNLGYDRFVLFSAHSAKDELIERIFWVEGDWFDDGNAVDAQT
YLRHCPVTRHILEADEPFFWSKTPNENGERYRVVRNPSGRGVHGLQVPVFGRTGLEGAVSLGGKLIDLSA
RFRLALQLLCVTAFFAARRLLEAPLLREAGVLSEREREVLAWTALGRRQADIAAILGISERTVENHLRSA
RRKLGVATTAQAIAIALRKGDI
>gnl|CDD|163316 TIGR03542, DAPAT_plant, LL-diaminopimelate aminotransferase. This clade of the pfam00155 superfamily of aminotransferases includes several which are adjacent to elements of the lysine biosynthesis via diaminopimelate pathway (GenProp0125). This clade includes characterized species in plants and Chlamydia. Every member of this clade is from a genome which possesses most of the lysine biosynthesis pathway but lacks any of the known succinylases, desuccinylases, acetylases or deacetylases typical of the acylated versions of this pathway nor do they have the direct, NADPH-dependent enzyme (ddh)
MKRNPHFLKLKSSYLFSEINKRVAEFRKKNPSADIIRLGIGDTTQPLPASVIEAFHNAVDELASPETFRG
YGPEQGYPFLREAIAENDYRGRIDPEEIFISDGAKCDVFRLQSLFGPDNTVAVQDPVYPAYLDSNVMAGR
AGVLDDDGRYSKITYLPCTAENNFIPELPEEPHIDIIYLCSPNNPTGTVLTKEQLKELVDYANEHGSLIL
FDAAYSAFISDPSLPHSIFEIPGARFCAIEFRSFSKTAGFTGVRLGWTVVPKELTYADGHSVIQDWERRQ
CTKFNGASYPVQRAAEAGYAGEGLQPILEAISYYMENARILRKALEAAGFKVYGGEHAPYLWVKTPEGIS
SWDFFDFLLYEYHVVGTPGSGFGPSGEGFVRFSAFGKRENIIEACERIKEAL
>gnl|CDD|188337 TIGR03543, divI1A_rptt_fam, DivIVA domain repeat protein. Members of this protein family contain two full and two partial repeats of a domain found at the N-terminus of Bacillus subtilis cell-division initiation protein DivIVA. The portion repeated four times in these proteins includes the motif GYxxxxVD
FPRSGKRKLGYDPAQVDAFLERAHAAYDNEGGNLTSHDIRNVAFDLRKRGYSPAQVDAALDRLERAFADR
ERTAEIAQHGRQAWKAQVEKLAQEIQDRLERPEGERFKRGSPKGPGYDKKDVDRLVDRIVGYLEDDATLS
ADEVRNAVFRQAKGKKGYDEAQVDAFLDRVVELLLALE
>gnl|CDD|274639 TIGR03544, cell_division_initiation_protein_DivIVA, DivIVA domain. This model describes a domain found in Bacillus subtilis cell division initiation protein DivIVA, and homologs, toward the N-terminus. It is also found as a repeated domain in certain other proteins, including family TIGR03543
LTPEDIRNKRFKKKLRGYDAAEVDAFLDRVADDL
>gnl|CDD|274640 TIGR03545, TIGR03545, TIGR03545 family protein. This model represents a relatively rare but broadly distributed uncharacterized protein family, distributed in 1-2 percent of bacterial genomes, all of which have outer membranes. In many of these genomes, it is part of a two-gene pair
MIRWSGLLGFLIIVAVILALLYFFFDPLAKKAIERSLEKAFGAKVEIAQVDTGLFPLQLSIQGLQVTDPD
KPMRNLFEIDRINASLDWDALLRGKVVIEELAIEGLAFGTERSTSGAVPETKDETPASAPSSIKEQKSSE
LKKVDSQLPDPRALLKGEDLKTVETAEEIEKSLKAMQQKWKKRKKDLPNKQDLEEYKKRLEAIKKKDIKN
PLELQKIKEEFDKLKKEGKADKQKIKSAKNDLQNDKKQLKADLAELKKAPQNDLKRLENKYAIKSGDLKN
FAVDLFGPEIRKYLQKFLKYYDQAEPLLNKSKKEPKEEAVETLANGEDYDFKDDNPYPDFLIKKADVSGK
MPDGDVGEIKGEVSNITNDHDLLGKPTTINLSAEASGKGKLTVKGVLDLRQPGEQKADLDFNVPNLDITD
IELLQSKDLPVTLAGGILSIGGKISIVGKDVEGNIDNKYTQVDLSVDGGAGSFEATKYILQVLKKIDVLT
VDADIKGILEDPNLKINSNLDKLLAKAFKKEIAAQIEKAKAKLKAKLNEKLSEQLGTTDSELNKL
>gnl|CDD|200289 TIGR03546, TIGR03546, TIGR03546 family protein. Members of this family are uncharacterized proteins, usually encoded by a gene adjacent to a member of family TIGR03545, which is also uncharacterized
KLLFSLFKALNSNTSPAQLALAVALGMILGLTPFLNLLNIALLFLVLILRVNLGAFILSAILFSGLAYLL
DPISDQVGEWLLEQESLQPVFTALYNIPLVPLARFNNTIVMGSFVVGLILLPPAFAISKVIIAKYRKRIV
AWVNKFKIVKLLKN
>gnl|CDD|274641 TIGR03547, muta_rot_YjhT, mutatrotase, YjhT family. Members of this protein family contain multiple copies of the beta-propeller-forming Kelch repeat. All are full-length homologs to YjhT of Escherichia coli, which has been identified as a mutarotase for sialic acid. This protein improves bacterial ability to obtain host sialic acid, and thus serves as a virulence factor. Some bacteria carry what appears to be a cyclically permuted homolog of this protein
LPDLPVGFKNGTGAIIGDKVYVGLGSAGTSWYKLDLKKPSKGWQKIADFPGGPRNQAVAAAIDGKLYVFG
GIGKANSEGSPQVFDDVYRYDPKKNSWQKLDTRSPVGLLGASGFSLHNGQAYFTGGVNKNIFDGYFADLS
AADKDSEPKDKLIAAYFSQPPEDYFWNKNVLSYDPSTNQWRNLGENPFLGTAGSAIVHKGNKLLLINGEI
KPGLRTAEVKQYLFTGGKLEWNKLPPLPPPKSSSQEGLAGAFAGISNGVLLVAGGANFPGAQENYKNGKL
YAHEGLIKAWSSEVYALDNGKWSKVGKLPQGLAYGVSVSWNNGVLLIGGENSGGKAVTDVYLLSWD
>gnl|CDD|274642 TIGR03548, mutarot_permut, cyclically-permuted mutarotase family protein. Members of this protein family show essentially full-length homology, cyclically permuted, to YjhT from Escherichia coli. YjhT was shown to act as a mutarotase for sialic acid, and by this ability to be able to act as a virulence factor. Members of the YjhT family (TIGR03547) and this cyclically-permuted family have multiple repeats of the beta-propeller-forming Kelch repeat
NLGVSGLLAGKTGDYLVVAGGCNFPEKPVAEGGKKKYYKDIYTLKLDANSALKWVKAGQLPYEIAYGASV
STPYGIYYVGGSPSSESFSDVLLLSLDDTKEALIIETLPSLPVAFDNGSATYKDGKIYVGGGNANGKPSN
KFYCLDLSNDTSGWEELPEFPGEARVQPVCQALHGKLYVFGGFQLGGDAIIYTDGYAYSPKTNTWQTVAD
PVLSDGEPITLLGGNSVKLGDSLMLVIGGVNYDIFFDAVDRLRQMKDESLKSEKAEYFGHPPQWYRFNDK
VLIYNVRSNEWKSIGAVPFVARAGAALLLHGDNIFSINGEIKPGIRTPRIY
>gnl|CDD|132588 TIGR03549, TIGR03549, YcaO domain protein. This family consists of remarkably well-conserved proteins from gamma and beta Proteobacteria, heavily skewed towards organisms of marine environments. Its gene neighborhood is not conserved. This family has an OsmC-like N-terminal domain. It shares a YcaO domain, frequently associated with ATP-dependent cyclodehydration for peptide modification. The function is unknown. Fifteen of the first sixteen members of this family are from selenouridine-positive genomes, but this correlation may not be meaningful
EIKVNFLDNLRLEAKFDDFTVIADQPIRYKGDGSAPGPFDYFLASSALCAAYFVKVYCNARDIPTENIRL
SQNNIVDPEDRYNQIFKIQVELPEDISEKDRQGILRSIDRCTVKKVVQTGPEFQIETVENLDADAQALLM
GTPDSGASTYIEGKDLPLEQTIANMTAILADLGMKIEIASWRNIVPNVWSLHIRDAASPMCFTNGKGATK
ESALCSALGEFIERLNCNFFYNDQFFGEDIANSAFVHYPNEKWFKPGDDDALPAGILDEYCLAIYNPDGE
LRGSHLIDTNSGRTDRGICSLPFVRQSDGETVYFPSNLIENLFLSNGMSAGNTLAEAQVQCLSEIFERAV
KKEIIEEEIVLPDVPQEVLAKYPGILAGIKALEEQGFPVLVKDASLGGQFPVMCVTLMNPRTGGVFASFG
AHPSFEVALERSLTELLQGRSFEGLNDLPQPTFNSMAVTEPNNFVEHFIDSSGVVSWRFFSAKHDYDFVE
WDFSGTNEEEAATLFGILEDMGKEVYIAVYEDLGAPACRILVPGYSEVYPVEDLIWDNTNKALDYREDIL
NLHRLDDEALEDLLERLEESQLDNYTDIRTLIGIEFDENTVWGQLTILELKLLIYLALQRHEDALELVGM
FLQFNDNTVERGLFYQAVNAVLEVTLDEELELEDYRRNFNRMYGEETMDAVIGSVNGSVRFYGLTPTSMK
LEGLDRHLRLIESYKKLH
>gnl|CDD|132589 TIGR03550, F420_cofG, 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofG subunit. This model represents either a subunit or a domain, depending on whether or not the genes are fused, of a bifunctional protein that completes the synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin, or FO. FO is the chromophore of coenzyme F(420), involved in methanogenesis in methanogenic archaea but found in certain other lineages as well. The chromophore also occurs as a cofactor in DNA photolyases in Cyanobacteria [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
TYSRNVFIPLTRLCRNRCGYCTFRRPPGELEAALLSPEEVLEILRKGAAAGCTEALFTFGEKPEERYPEA
REWLAEMGYDSTLEYLRELCELALEETGLLPHTNPGVMSRDELARLKPVNASMGLMLETTSERLCKGEAH
YGSPGKDPAVRLETIEDAGRLKIPFTTGILIGIGETREERAESLLAIRELHERYGHIQEVIVQNFRAKPG
TPMENHPEPSLEEMLRTVAVARLILPPDISIQVPPNLNREDYRLLLDAGIDDWGGVSPVTPDHVNPEAPW
PEIDELARATEEAGFTLKERLPVYPEYVREGWLSPRISEHIE
>gnl|CDD|132590 TIGR03551, F420_cofH, 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit. This enzyme, together with CofG, complete the biosynthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, the chromophore of coenzyme F420. The chromophore is also used in cyanobacteria DNA photolyases [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
ITKEEALELFEARGNLFELFRLADELRRDIVGDTVTYVVNRNINFTNVCYGGCGFCAFRKRKGDADAYLL
SLEEIAERAAEAWKAGATEVCIQGGIHPDLDGDFYLDILRAVKEEVPGMHIHAFSPMEVYYGARNSGLSV
EEALKRLKEAGLDSMPGTAAEILDDEVRKVICPDKLSTAEWIEIIKTAHKLGIPTTATIMYGHVETPEHW
VDHLLILREIQEETGGFTEFVPLPFVHYNAPLYLKGMARPGPTGREDLKVHAIARILLHGLIDNIQASWV
KLGKKLAQVALRCGANDLGGTLMEESISRAAGASHGEYLSPEELEAIIEDAGRIPKQRTTLYE
>gnl|CDD|274643 TIGR03552, F420_cofC, 2-phospho-L-lactate guanylyltransferase. Members of this protein family are the CofC enzyme of coenzyme F420 biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
RAVIPVKRLANAKSRLSPVLSPEEREELALAMLRDVITALRGAGAGAVLVVSPDPALLEAARNLGAPVLR
DPGPGLNNALNAALAEAREPGGAVLILMADLPLLTPRELKRLLAAATEGDVVIAPDRGGGTNALFLRPPS
ALRPAFGGDSFLRHRRSAAKRGLRVRIYDSFGLALDVDTPEDLAEALLHGVGTAT
>gnl|CDD|132592 TIGR03553, F420_FbiB_CTERM, F420 biosynthesis protein FbiB, C-terminal domain. Coenzyme F420 differs between the Archaea and the Actinobacteria, where the numbers of glutamate residues attached are 2 (Archaea) or 5-6 (Mycobacterium). The enzyme in the Archaea is homologous to the N-terminal domain of FbiB from Mycobacterium bovis, and is responsible for glutamate ligation. Therefore it seems likely that the C-terminal domain of FbiB modeled here, is involved in additional glutamate ligation [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
QAVLLRRSVRRFSDDPVDPDAVRAAVAAALTAPAPHHTRPVRFVWVEDAERRTRLLDAMADAWRADLRAD
GLSADAIDRRVARGDILRDAPELVIPCLVPDGAHSYPDERRTAAEHTMFTVAVGAAVQNLLVALAVEGLG
SCWVGSTIFAADVVRAELDLPADWEPLGAVAVGHPAEPPGPRPPRDPEDFLVRR
>gnl|CDD|213827 TIGR03554, F420_G6P_DH, glucose-6-phosphate dehydrogenase (coenzyme-F420). This family consists of the F420-dependent glucose-6-phosphate dehydrogenase of Mycobacterium and Nocardia. It shows homology to several other F420-dependent enzymes rather than to the NAD or NADP-dependent glucose-6-phosphate dehydrogenases [Energy metabolism, Pentose phosphate pathway]
ELKLGYKASAEQFAPRELVELAVLAEAHGMDSATVSDHFQPWRHQGGHAPFSLSWMTAVGERTNRLLLGT
SVLTPTFRYNPAVIAQAFATMGCLYPGRVFLGVGTGEALNEIATGYQGEWPEFKERFARLRESVRLMREL
WTGDRVDFDGEYYRTKGASIYDVPEGGVPVYIAAGGPVVAKYAGRAGDGFICTSGKGEELYTEKLMPAVA
EGAAKADRDVDSIDKMIEIKISYDTDPELALENTRFWAPLSLTAEQKHSIDDPIEMEKAADALPIEQVAK
RWIVASDPDEAVEQVGQYVDWGLNHLVFHAPGHDQRRFLELFQRDLAPRLR
>gnl|CDD|132594 TIGR03555, 510-methylenetetrahydromethanopterin_reductase, 5,10-methylenetetrahydromethanopterin reductase. Members of this protein family are 5,10-methylenetetrahydromethanopterin reductase, an F420-dependent enzyme of methanogenesis. It is restricted to the Archaea [Energy metabolism, Methanogenesis]
FGIEFVPDDPITKIAYYVKLAEDNGFEYAWITDHYNNRNVYSTLTLLALNTNTIKLGPGVTNPYTRSPAI
TASAIATLDEISGGRAVLGIGPGDKATFDAMGIEWVKPLTTIREAIEVIRQLLAGKKVEYDGEYVKFAGA
KLGFKAIQGSIPIYMGAQGPKMLKTAGEIADGVLINASNPKDFEVAVPLIKEGAEKAGRSLDEIDVAAYA
CFSIDKDADKAINAAKIVVAFIVAGSPPVVLERHGIPTDAVEQIGEALGKGDFGGAIGLVDDDMIEAFSI
AGTPDDVIEKIEELLKAGVTQVVAGSPIGPDKEKAIKLIGKEVIP
>gnl|CDD|274644 TIGR03556, photolyase_8HDF, deoxyribodipyrimidine photo-lyase, 8-HDF type. This model describes a narrow clade of cyanobacterial deoxyribodipyrimidine photo-lyase. This group, in contrast to several closely related proteins, uses a chromophore that, in other lineages is modified further to become coenzyme F420. This chromophore is called 8-HDF in most articles on the DNA photolyase and FO in most literature on coenzyme F420 [DNA metabolism, DNA replication, recombination, and repair]
ALILFWHRRDLRLSDNIGLAAARAQSAKVVGLFCLDPQILQSADMAPVRVAYLQGCLQELQQRYQQAGSR
LLILRGDPQQLIPQLAQQLQAEAVYWNQDVEPYGRDRDRAVAAALKTKGIRAVTLWDQLLHSPDQILSGS
GNPYTVYGPFWKNWSSQPKPTPVATPTELEDLTEEEQTAAAPLGLSELPTAKDLGFDWDGDLIVAPGEAA
AQARLQEFCDRAIADYDEQRNFPAEAGTSGLSPALKFGVIGIRQVWQATSAAHALSRSEEARNSIRTWQQ
ELAWREFYQHALYHFPSLADGPYRSLFQQFPWENNEAHFTAWCEGQTGYPIVDAAMRQLNETGWMHNRCR
MIVASFLTKDLIINPQWGEQYFMQKLIDGDLAANNGGWQWSASSGMDPKPLRIFNPASQAQKFDPTAEYI
RRWLPELRSVDTKDLVTGEITPLERHAVGYPAPIVDHNLQQQQFKQLYQQL
>gnl|CDD|274645 TIGR03557, F420_G6P_family, F420-dependent oxidoreductase, G6PDH family. Members of this protein family include F420-dependent glucose-6-phosphate dehydrogenases (TIGR03554) and related proteins. All members of this family come from species that synthesize coenzyme F420, with the exception of those that belong to TIGR03885, a clade within this family in which cofactor binding may instead be directed to FMN [Unknown function, Enzymes of unknown specificity]
IGYFLMCEQSGPRELVRQAVAAEQAGFDFLWISDHFHPWLDEQGHSPFVWSVLGALAQATERLPLTTAVT
CPTMRYHPAIVAQAAATSAVLSDGRFTLGLGSGENLNEHVVGDGWPSVDVRLEMLREAVEIIRELWQGGY
VDHRGKHYTVDSARLYDLPEEPPPIGVSAFGPRAVRLAARIGDGLIATEPDADLVEAFREAGGGGKPVQG
QVPVCWDPDEDAAVKTAHRQFRWFALGWKVNQELPTPAHFAAATQLVREEDVAASIPCGPDPDRHVEAVR
EYVDAGFDEVALVQIGPDQDGFFDFYATELLPALRE
>gnl|CDD|274646 TIGR03558, oxido_grp_1, luciferase family oxidoreductase, group 1. The Pfam domain family pfam00296 is named for luciferase-like monooxygenases, but the family also contains several coenzyme F420-dependent enzymes. This protein family represents a well-resolved clade within family pfam00296 and shows no restriction to coenzyme F420-positive species, unlike some other clades within pfam00296 [Unknown function, Enzymes of unknown specificity]
LSVLDLSPIREGSTAADALRNTVELAQHAERLGYHRFWVAEHHNMPGIASSAPEVLIGHIAAATSRIRVG
SGGVMLPNHSPLKVAEQFGTLEALYPGRIDLGLGRAPGTDPLTARALRRGLDAGADDFPEQVAELQAYLG
PEGHPYAGVRAVPGPGTNPPLWLLGSSLYSAQLAARLGLPFAFASHFAPDALEEALDAYRERFRPSAQLD
EPYVMVAVNVVAADTDEEAERLATSLDQAFLRLRRGRPGPLPPPEEAIDYLLSPAERAAIEQNLSRSIVG
SPETVREQLEALAERTGADELMVTTPIYDHEARLRSYELLAEA
>gnl|CDD|274647 TIGR03559, F420_Rv3520c, probable F420-dependent oxidoreductase, Rv3520c family. Members of this protein family are predicted to be oxidoreductases dependent on coenzyme F420. The family includes a single member in Mycobacterium tuberculosis (Rv3520c/MT3621) but four in Mycobacterium smegmatis. Prediction that this family is F420-dependent is based primarily on Partial Phylogenetic Profiling vs. F420 biosynthesis [Unknown function, Enzymes of unknown specificity]
RLGLALGYSGPPRNAVDLVAAAEKAGLDSVWVAEAYGFDAVTPLGYLAARTSRVRLGTGVLQLYARTPTL
TAMTAAGLDHLSGGRFILGLGASGPQVVEGWHGVPFDRPLGRTREYIEICRKVWRREGPVTHDGRHYQLP
LPGDRGTGLGKPLKLINHPVRARIPIYLAALGPKNVALTAEIADGWLPIFYSPEKAADVWGEALAEGFAK
RGASLGDLEIAAGAQLAVGDDVEAALDWVKPQLALYIGGMGAKGRNFYNDLAARYGYEEEAARIQDLYLA
GRKDEAAAAVPDELVEDTSLIGPRDYVRERLAAWREAGVTTLLVT
>gnl|CDD|274648 TIGR03560, F420_Rv1855c, probable F420-dependent oxidoreductase, Rv1855c family. Coenzyme F420 has a limited phylogenetic distribution, including methanogenic archaea, Mycobacterium tuberculosis and related species, Colwellia psychrerythraea 34H, Rhodopseudomonas palustris HaA2, and others. Partial phylogenetic profiling identifies protein subfamilies, within the larger family called luciferase-like monooxygenanases (pfam00296), that appear only in F420-positive genomes and are likely to be F420-dependent. This model describes one such subfamily, exemplified by Rv1855c from Mycobacterium tuberculosis [Unknown function, Enzymes of unknown specificity]
DFRIFTEPQQLYPDLLAVARAAEDAGFDALFRSDHFLQMPMVGPPEGPTLEAWTTLAGLARETSRIRLGT
LVTGVTYRHPGLLAKMVATVDVLSGGRAELGLGAGWYEREHRAYGIPFPPLAERFERLEEALQIITGMWS
GEGVTFDGRHYRLADAIALPKPLQRPHPPILIGGGGEKRTLRLAARYADEFNLVFGPPDELAHKFEVLRA
HCEAAGRDPDEIRRSVA
>gnl|CDD|274649 TIGR03561, organ_hyd_perox, peroxiredoxin, Ohr subfamily. pfam02566, OsmC-like protein, contains several deeply split clades of homologous proteins. The clade modeled here includes the protein Ohr, or organic hydroperoxide resistance protein [Cellular processes, Detoxification]
LYTTKATATGGRDGRVRSDDGLLDLDLAPPKELGGDGGGTNPEQLFAAGYAACFDGALKLVAGQAKVKLP
ADAEVTATVGLGKNEDGGFGLSVELKVTLPGLDQAEAEALVEAAHQVCPYSKATRGNIDVTLTV
>gnl|CDD|274650 TIGR03562, osmo_induc_OsmC, peroxiredoxin, OsmC subfamily. pfam02566, OsmC-like protein, contains several deeply split clades of homologous proteins. The clade modeled here includes the protein OsmC, or osmotically induced protein C. The member from Thermus thermophilus was shown to have hydroperoxide peroxidase activity. In many species, this protein is induced by stress and helps resist oxidative stress [Cellular processes, Detoxification]
RTASAVWEGDLKEGKGTISTQSGALSETPYSFKTRFEDGPGTNPEELIAAAHAGCFSMALSAALAEAGFT
PESLDTTATVTLDKVGGGFAITGIHLTVRAKVPGIDEAKFQEIAEKAKEGCPVSKALAAVEITLD
>gnl|CDD|132602 TIGR03563, perox_SACOL1771, peroxiredoxin, SACOL1771 subfamily. This protein family belongs to the OsmC/Ohr family (pfam02566, OsmC-like protein) of peroxiredoxins
HHFYLQANWPGGRNSVGTIQGGNLSEQISIPKEMDGPGVGTNPDEMLLGAAATCYIITLAAMLERAGLED
EKLTLESEGIVDVTNGVFTYEKIIHYPKIVLKKEAKQNLEKKAPKLAKKAESSCMISRAIQGNVEIEL
>gnl|CDD|274651 TIGR03564, F420_MSMEG_4879, F420-dependent oxidoreductase, MSMEG_4879 family. Coenzyme F420 is produced by methanogenic archaea, a number of the Actinomycetes (including Mycobacterium tuberculosis), and rare members of other lineages. The resulting information-rich phylogenetic profile identifies candidate F420-dependent oxidoreductases within the family of luciferase-like enzymes (pfam00296), where the species range for the subfamily encompasses many F420-positive genomes without straying beyond. This family is uncharacterized, and named for member MSMEG_4879 from Mycobacterium smegmatis [Unknown function, Enzymes of unknown specificity]
LVADARRAAAAGLDSAWLGQVYGYDALTALALVGRAVPGIELGTAVVPTYPRHPLALASQALTAQAAAHG
RLTLGLGLSHRWIVEDMFGLPFDRPARRLREYLTVLRPLLAGGAVDFHGETVTAHLPTSVRVPGATPVPV
LVAALGPQMLRVAGELADGTVLWLAGPRTIGDHIVPTITAAAEAAGRPAPRIVAGVPVAVTDDPDEARAR
AAAQLAFYETLPSYRAVLDREGAENAADLAIIGDEDAVARQLRRYADAGATDVVA
>gnl|CDD|274652 TIGR03565, alk_sulf_monoox, alkanesulfonate monooxygenase, FMNH(2)-dependent. Members of this protein family are monooxygenases that catalyze desulfonation of aliphatic sulfonates such as methane sulfonate. This enzyme uses reduced FMN, although various others members of the same luciferase-like monooxygenase family (pfam00296) are F420-dependent enzymes [Central intermediary metabolism, Sulfur metabolism]
NIFWFIPTHGDGRYLGTSEGGRAVDHGYLKQIAQAADRLGYTGVLLPTGRSCEDSWVTASSLAPLTERLK
FLVAVRPGLMSPTVAARMAATLDRLSGGRLLINVVTGGDPVELAGDGIFLDHDERYEATDEFLTVWRRLL
AGETVDFDGKHIKVENAKLLFPPVQQPYPPLYFGGSSDAAIELAAEHVDVYLTWGEPPAQVAEKIAKVRK
RAAKRGRTVRFGIRLHVIVRETEEEAWAAADRLISHLDDDTIARAQKAFARMDSVGQRRMAALHGGRRDK
LEISPNLWAGVGLVRGGAGTALVGDPETVAARIREYQDLGIDTFILSGYPHLEEAYRFAELVFPLL
>gnl|CDD|211840 TIGR03566, FMN_reduc_MsuE, FMN reductase, MsuE subfamily. Members of this protein family use NAD(P)H to reduce FMN and regenerate FMNH2. Members include the NADH-dependent enzyme MsuE from Pseudomonas aeruginosa, which serves as a partner to an FMNH2-dependent alkanesulfonate monooxygenase. The NADP-dependent enzyme from E. coli is outside the scope of this model
KVVGVSGSLTRPSRTLALVEALVAELAARLGISPRTIDLADLAPSLGGALWRSQLPPDAERILQAIESAD
LLVVGSPVYRGSYTGLFKHLFDLVDPNALIGKPVLLAATGGSERHALMVEHQLRPLFGFFQALTLPTGVY
ASDADFADYRLASEALRARIALAVDRAAPLLAAR
>gnl|CDD|274653 TIGR03567, FMN_reductase_NADPH, FMN reductase, SsuE family. Members of this protein family use NAD(P)H to reduce FMN and regenerate FMNH2. Members include the homodimeric, NAD(P)H-dependent enzyme SsuE from Escherichia coli, which serves as a partner to an FMNH2-dependent alkanesulfonate monooxygenase. It is induced by sulfate starvation. The NADH-dependent enzyme MsuE from Pseudomonas aeruginosa is outside the scope of this model (see model TIGR03566) [Central intermediary metabolism, Sulfur metabolism]
RVLTLSGSPSTPSRSSALLRHAREALQEQGVEVDHLSVRDLPAEDLLFARFDSPALKAATAQVAQADGVV
VATPVYKASYSGVLKALLDLLPQRALRGKVVLPIATGGTIAHLLAVDYALKPVLSALGARHILHGVFALD
SQIERQEDGPQRLDEEIKERLDEALETLVQA
>gnl|CDD|274654 TIGR03568, Polysialic_acid_biosynthesis_protein_P7, UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing. This family of enzymes catalyzes the combined epimerization and UDP-hydrolysis of UDP-N-acetylglucosamine to N-acetylmannosamine. This is in contrast to the related enzyme WecB (TIGR00236) which retains the UDP moiety. NeuC acts in concert with NeuA and NeuB to synthesize CMP-N5-acetyl-neuraminate
KICVVTGTRADYGLLRPLLKALQDDPDLELQLIVTGMHLSPEYGNTVNEIEKDGFDIDEKIEILLDSDSN
AGMAKSMGLTIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTEGAIDESIRHAI
TKLSHLHFVATEEYRQRVIQMGEDPDRVFNVGSPGLDNILSLDLLSKEELEEKLGIDLDKPYALVTFHPV
TLEKAEAEEQIKELLKALDELNKNIIFTYPNADAGSRIINEAIEEYVEKHPNFRLFKSLGQERYLSLLKN
ADAVIGNSSSGIIEAPSFGVPTINIGTRQKGRLRADSVIDVDPDKEEIVKAIEKALDPAFKKSLKKVKNP
YGDGNSSKRIIEIL
>gnl|CDD|274655 TIGR03569, ORF_8_similar_to_NeuB_family, N-acetylneuraminate synthase. This family is a subset of the pfam03102 and is believed to include only authentic NeuB N-acetylneuraminate (sialic acid) synthase enzymes. The majority of the genes identified by this model are observed adjacent to both the NeuA and NeuC genes which together effect the biosynthesis of CMP-N-acetylneuraminate from UDP-N-acetylglucosamine
TFIIAEAGVNHNGDLELAKKLVDAAAEAGADAVKFQTFKAEDLVSKNAPKAEYQKINTGAEESQLEMLKK
LELSEEDHRELKEYCESKGIEFLSTPFDLESADFLEDLGVPRFKIPSGEITNAPLLKKIARFGKPVILST
GMATLEEIEAALGVLRDAGTPDSNITLLHCTTEYPAPFEDVNLNAMDTLKEAFDLPVGYSDHTLGIEAPI
AAVALGATVIEKHFTLDKNLPGPDHKASLEPDELKEMVQGIRNVEKALGDGVKRPTPSEQKNRDVARKSL
VAAKDIKKGEIFTEDNLTVKRPGNGISPMEYWEVIGKKASRDYEEDELI
>gnl|CDD|274656 TIGR03570, NeuD_NnaD, sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family. This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff
KLVIIGAGGHGRVVADILERSGWEVVGFLDDNPALQGTEVDGLPVLGGDEDLLRYPPDEVDLVVAIGDNK
LRRRLVEKLKAKGYRFATLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGD
FVHIAPGVTLSGGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA
>gnl|CDD|274657 TIGR03571, lucif_BA3436, luciferase-type oxidoreductase, BA3436 family. This family is a distinct subgroup among members of the luciferase monooxygenase domain family. The larger family contains both FMN-binding enzymes (luciferase, alkane monooxygenase) and F420-binding enzymes (methylenetetrahydromethanopterin reductase, secondary alcohol dehydrogenase, glucose-6-phosphate dehydrogenase). Although some members of the domain family bind coenzyme F420 rather than FMN, members of this family are from species that lack the genes for F420 biosynthesis. A crystal structure, but not function, is known (but unpublished) for the member from Bacillus cereus, PDB|2B81 [Unknown function, Enzymes of unknown specificity]
APGGLTLGLMLPLDNYQGRPVPDMERQVELAQRAEALGFAALWLRDVPLYDPDFGDAGQVFDPFVYLGYL
AAVTSRIALGTAAIVLPLRHPLHVAKAAASLDQLSGGRFLLGVASGDRPSEYPAFGVDFESRGERFREAI
DVLRAALREPFPSIRSSLGELDGGLDLLPKPTSGRIPLLATGSAQQSLEWIARNMDGWMTYPRPPETQRA
RIDEWREAVASGGFKPFGQSMHLDLSEDPDEPPTPIRLGYRTGRNALIELLDALREAGVNHVALNLRPSR
RPAAEVLDELAEEVLPHF
>gnl|CDD|132611 TIGR03572, WbuZ, glycosyl amidation-associated protein WbuZ. This clade of sequences is highly similar to the HisF protein, but generally represents the second HisF homolog in the genome where the other is an authentic HisF observed in the context of a complete histidine biosynthesis operon. The similarity between these WbuZ sequences and true HisFs is such that often the closest match by BLAST of a WbuZ is a HisF. Only by making a multiple sequence alignment is the homology relationship among the WbuZ sequences made apparent. WbuZ genes are invariably observed in the presence of a homolog of the HisH protein (designated WbuY) and a proposed N-acetyl sugar amidotransferase designated in WbuX in E. coli, IfnA in P. aeriginosa and PseA in C. jejuni. Similarly, this trio of genes is invariably found in the context of saccharide biosynthesis loci. It has been shown that the WbuYZ homologs are not essential components of the activity expressed by WbuX, leading to the proposal that these to proteins provide ammonium ions to the amidotransferase when these are in low concentration. WbuY (like HisH) is proposed to act as a glutaminase to release ammonium. In histidine biosynthesis this is also dispensible in the presence of exogenous ammonium ion. HisH and HisF form a complex such that the ammonium ion is passed directly to HisF where it is used in an amidation reaction causing a subsequent cleavage and cyclization. In the case of WbuYZ, the ammonium ion would be passed from WbuY to WbuZ. WbuZ, being non-essential and so similar to HisF that a sugar substrate is unlikely, would function instead as a amoonium channel to the WbuX protein which does the enzymatic work
MLKKRIIPCLLLKDGRLVKTVQFKDPRYIGDPVNAARIYNAKGADELIVLDIDASKRGREPLFELISNLA
EECFMPLTVGGGIRSLEDAKKLLSLGADKVSINTAALENPDLIEEAARRFGSQCVVVSIDVKKELDGSDY
KVYSDNGRRATGRDPVEWAREAEQLGAGEILLNSIDRDGTMKGYDLELIKTVSDAVSIPVIALGGAGSLD
DLVEVALEAGASAVAAASLFHF
>gnl|CDD|274658 TIGR03573, WbuX, N-acetyl sugar amidotransferase. This enzyme has been implicated in the formation of the acetamido moiety (sugar-NC(=NH)CH3) which is found on some exopolysaccharides and is positively charged at neutral pH. The reaction involves ligation of ammonia with a sugar N-acetyl group, displacing water. In E. coli (O145 strain) and Pseudomonas aeruginosa (O12 strain) this gene is known as wbuX and ifnA respectively and likely acts on sialic acid. In Campylobacter jejuni, the gene is known as pseA and acts on pseudaminic acid in the process of flagellin glycosylation. In other Pseudomonas strains and various organisms it is unclear what the identity of the sugar substrate is, and in fact, the phylogenetic tree of this family sports a considerably deep branching suggestive of possible major differences in substrate structure. Nevertheless, the family is characterized by a conserved tetracysteine motif (CxxC.....[GN]xCxxC) possibly indicative of a metal binding site, as well as an invariable contextual association with homologs of the HisH and HisF proteins known as WbuY and WbuZ, respectively. These two proteins are believed to supply the enzyme with ammonium by hydrolysis of glutamine and delivery through an ammonium conduit
MKFCKRCVMPTTRPGITFDEDGVCSACRNFEEKSKIDWDEREKELEELVDKIKKKGGGRYDCIIGVSGGK
DSTYQAHVLKKKLGLNPLLVTVDPGWNTELGVKNLNNLIKKLGFDLHTITINPETFRKLQRAYFKKVGDP
EWPQDHAIFASVYQVALKFNIPLIIWGENIAEEYGGDSEEELNPDEWKYNKRGIDAANIKDFSDKGLSER
DLYAYTYPDKEKLQSKGVKVIYLGYYVKWDKKKNYEFIKKRGGWREGPHPGTYENYKHIDSIFTIFHDYL
KYLKFGFGRATDHASIDIRSGRITREEAIELVKEYDGEFPKEDLEYFLKYLGISEEEFWKTVE
>gnl|CDD|132613 TIGR03574, L-seryl-tRNASec_kinase, L-seryl-tRNA(Sec) kinase, archaeal. Members of this protein are L-seryl-tRNA(Sec) kinase. This enzyme is part of a two-step pathway in Eukaryota and Archaea for performing selenocysteine biosynthesis by changing serine misacylated on selenocysteine-tRNA to selenocysteine. This enzyme performs the first step, phosphorylation of the OH group of the serine side chain. This family represents archaeal proteins with this activity [Protein synthesis, tRNA aminoacylation]
LIILTGLPGVGKSTFSKELAKKLSEKNIDVIILGTDLIRESFPVWKEKYEEFIRDSTLYLIKTALKNKYS
VIVDDTNYYNSMRRDLINIAKEYNKNYIIIYLKAPLDTLLRRNIERGEKIPNEVIKDMYEKFDEPGTKYS
WDLPDLTIDTTKKIDYNEILEEILEISENKLKIEKPKKPKRRTDENILNKIDKRTRQIVGELIKTGKLDK
ELIKKLSELRKEFLKSIKDIKAEKEDFRRVEKEFKDYLN
>gnl|CDD|188340 TIGR03575, L-seryl-tRNASec_kinase, L-seryl-tRNA(Sec) kinase, eukaryotic. Members of this protein are L-seryl-tRNA(Sec) kinase. This enzyme is part of a two-step pathway in Eukaryota and Archaea for performing selenocysteine biosynthesis by changing serine misacylated on selenocysteine-tRNA to selenocysteine. This enzyme performs the first step, phosphorylation of the OH group of the serine side chain. This family represents eukaryotic proteins with this activity
LCVLCGLPAAGKSTLARSLSATLRRERGWAVAVITYDDIIPEAAFELDQSRPLPSQWKQFRQELLKYLEH
FLVAVINGSELSAPPGKTEGMWEDFVDCLKEQGLIISSGASEAQGCHSLTKPAVSRPLCLVLDDNFYYQS
MRYEVYQLARKYSLGFCQLFLDCPVESCLLRNKQRPVPLPDETIQLMGRKIEKPNPEKNAWEHNSLVIQS
SACISEDSLEVTDLLNTALENPIKCVEENLEQKETDRIICSTNILHQADQTLRRIISQTMREAKDEQASA
YNLKLLAEELNKLKADFLEDLRQGNCKKYLCFQQTCDLSDIISLFHYERDNIVQKYFSKE
>gnl|CDD|213830 TIGR03576, pyridox_MJ0158, pyridoxal phosphate enzyme, MJ0158 family. Members of this archaeal protein family are pyridoxal phosphate enzymes of unknown function. Sequence similarity to SelA, a bacterial enzyme of selenocysteine biosynthesis, has led to some members being misannotated as functionally equivalent, but selenocysteine is made on tRNA in Archaea by a two-step process that does not involve a SelA homolog [Unknown function, Enzymes of unknown specificity]
VNEVKRREKALEIIREKISRGGRDSLYDLTGLAGGFKIDEEDLELLETYVGPAIFEEKVQELGREHLGGP
EEKILVFNRTSSAILATILALEPPGRKVVHYLPEKPAHPSIPRSCKLAGAEYFESDELSELKKIDGTSLV
VITGSTMDLKVVSEEDLKRVIKQAKSKEAIVLVDDASGARVRRLYGQPPALDLGADLVVTSTDKLMDGPR
GGLLAGRKELVDKIKSVGEQFGLEAQAPLLAAVVRALEEFELSRIRDAFKRKEEVYLRLFDKLNVERTPT
GFVIKGVEEEKLIEIGLDLLRNYGIITITAVGMPGASKTLRFDLAAKDAERIGDDYLVEAVKDSLK
>gnl|CDD|132616 TIGR03577, EF_0830, conserved hypothetical protein EF_0830/AHA_3911. Members of this family of small (about 120 amino acid), relatively rare proteins are found in both Gram-positive (e.g. Enterococcus faecalis) and Gram-negative (e.g. Aeromonas hydrophila) bacteria, as part of a cluster of conserved proteins. The function is unknown [Hypothetical proteins, Conserved]
ITVVIGDRLGKGQKVAKGVEAAGGRAVVIPGMAADMKLGDVMKQENADLGISFCGSGGAGAITAQTKYGY
KARYGMRSVEEGVTAINEGKNVLGFGFMDKEELGKRLTEAFLKKH
>gnl|CDD|213831 TIGR03578, EF_0831, conserved hypothetical protein EF_0831/AHA_3912. Members of this family of small (about 100 amino acid), relatively rare proteins are found in both Gram-positive (e.g. Enterococcus faecalis) and Gram-negative (e.g. Aeromonas hydrophila) bacteria, as part of a cluster of conserved proteins. The function is unknown [Hypothetical proteins, Conserved]
KKMITTTVIVSGKGNTKQLAFASALSKIQKKVMKENPAVLLRIEPVDVHILKAEESVYTEKFLFFFFPRK
RREYSVELDVTVKVTAIKVEEVDFKK
>gnl|CDD|132618 TIGR03579, EF_0833, conserved hypothetical protein EF_0833/AHA_3914. Members of this family of relatively rare proteins are found in both Gram-positive (e.g. Enterococcus faecalis) and Gram-negative (e.g. Aeromonas hydrophila) bacteria, as part of a cluster of conserved proteins. The function is unknown
KNFWYADWSFPIFVGLLSSGIFAGTHMYYVYGIGAFNEVAIVAMLKAGMDGGGYGAAAAFGASFLFARIL
EGSLVGILDIGGSIQTGIGIGVPAILLGAGIVAPVENFGLSLLTGAVLGLAVGYVIILIRKFTVGQSNST
FGADVMMGAGNSSGRFLGPLIVLSAAGASIPIGIGSTIGALIFYIWKKPIAGGAILGAMIFGAIFPVSL
>gnl|CDD|274659 TIGR03580, EF_0832, conserved hypothetical protein EF_0832/AHA_3913. Members of this family of relatively rare proteins are found in both Gram-positive (e.g. Enterococcus faecalis) and Gram-negative (e.g. Aeromonas hydrophila) bacteria, as part of a cluster of conserved proteins. The function is unknown [Unknown function, General]
GALVGVGVGAGAARMFHAPTTQGMGAFRTLGELNACEGDPASHFSFGLGFFFNAWASSVGAGAFTQDVDH
RIIPNWAAAALMVKNKNVTETMHNPKKMGIAGGIIGMIVVAFLNSTASAIPESLQVTAVKVLVPAANLLI
NIVMPVIFWLAALDAGKRSGFWGTIFGGLAQLIMGNAVPGVVLGILIGKGVDDSGWTKVTKGMLGAIILL
FILSGFFRGFDLEMIESFRLTVPQWLENLHNVLSGK
>gnl|CDD|188342 TIGR03581, EF_0839, conserved hypothetical protein EF_0839/AHA_3917. Members of this family of relatively uncommon proteins are found in both Gram-positive (e.g. Enterococcus faecalis) and Gram-negative (e.g. Aeromonas hydrophila) bacteria, as part of a cluster of conserved proteins. The function is unknown [Hypothetical proteins, Conserved]
YKNRVCLNVLANSVENAKEIYEAAEGHVLVGVLSKNYPTVEEAVEDMKKYSKEIDNAVSVGLGAGDPNQS
AMVADISAHTQPQHINQVFTGVGTSRALLGQDDTVINGLVSPTGTVGLVNISTGPLSSQGEEAIVPIETA
IAMLKDMGGSSVKYFPMGGLKHLEEYAAVAKACAKHGFYLEPTGGIDLENFEEIVQIALDAGVEKVIPHV
YSSIIDKETGNTRVEDV
>gnl|CDD|132621 TIGR03582, EF_0829, PRD domain protein EF_0829/AHA_3910. Members of this family of relatively uncommon proteins are found in both Gram-positive (e.g. Enterococcus faecalis) and Gram-negative (e.g. Aeromonas hydrophila) bacteria, as part of a cluster of conserved proteins. This protein contains a PRD domain (see pfam00874). The function is unknown [Unknown function, General]
EGEAQEIIRKSENPELLVQVIQQTENLLREEHIVPTEVQKQMLISHLNAMVYRSTTGETLPEVDRSLFDE
ISKESIKLAEEVVAALGNLAEDEAYLLSVHFEVAKEN
>gnl|CDD|132622 TIGR03583, EF_0837, probable amidohydrolase EF_0837/AHA_3915. Members of this family of relatively uncommon proteins are found in both Gram-positive (e.g. Enterococcus faecalis) and Gram-negative (e.g. Aeromonas hydrophila) bacteria, as part of a cluster of conserved proteins. These proteins resemble aminohydrolases (see pfam01979), including dihydroorotases. The function is unknown [Hypothetical proteins, Conserved]
YDLLIKNGRTVNGTPVDIAIEDGKIAAVGTTITGSAKQTIDLEGETYVSAGWIDDHTHCFPKSALYYDEP
DEIGVKTGVTTVVDAGSTGADDIDDFYRLAQQAKTNVFALLNISRIGLVAQDELADLSNLDASAVKQAVE
RYPDFIVGLKARMSKSVVGDNGIEPLEIAKQIQQENLELPLMVHIGSAPPELDEILALMEKGDVLTHCFN
GKPNGILRETGEVKPSVLEAYNRGVILDVGHGTASFSFHVAEKAKRAGIFPDTISTDIYIRNRINGPVYS
LATVMSKFLALGYSLEEVIEKVTKNAAEILKLTQKGRLQEGYDADLTIFTVKAEPKKLTDSEGDSRIAEE
QIKPLAVIIGGEYYE
>gnl|CDD|274660 TIGR03584, PseF, pseudaminic acid cytidylyltransferase. The sequences in this family include the pfam02348 (cytidyltransferase) domain and are homologous to the NeuA protein responsible for the transfer of CMP to neuraminic acid. According to, this gene is responsible for the transfer of CMP to the structurally related sugar, pseudaminic acid which is observed as a component of sugar modifications of flagellin in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci
IAIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDEEIAEVAKSYGASVPFLRPKE
LADDFTGTAPVVKHAIEELKLQKQYDHACCIYATAPFLQAKILKEAFELLKQPNAHFVFSVTSFAFPIQR
AFKLKENGGVEMFQPEHFNTRSQDLEEAYHDAGQFYWGKSQAWLESGPIFSPHSIPIVLPRHLVQDIDTL
EDWERAELLYKL
>gnl|CDD|274661 TIGR03585, PseH, UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase. Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar
KNFTPLNSEELELVLEWRNHPDVRANMYSDHLIDWEEHLHFIEALKQDPNRRYWIVCQESRPIGVISFTD
INLVHKSAFWGIYANPFCKPGVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGFEREGVFR
QGGEYYDVLLMY
>gnl|CDD|163337 TIGR03586, PseI, pseudaminic acid synthase. Members of this family are included within the larger pfam03102 (NeuB) family. NeuB itself (TIGR03569) is involved in the biosynthesis of neuraminic acid by the condensation of phosphoenolpyruvate (PEP) with N-Acetyl-D-Mannosamine. In an analagous reaction, this enzyme, PseI, condenses PEP with 6-deoxy-beta-L-AltNAc4NAc to generate pseudaminic acid
PPFIIAELSANHNGSLERALAMIEAAKAAGADAIKLQTYTPDTITLDSDRPEFIIKGGLWDGRTLYDLYQ
EAHTPWEWHKELFERAKELGLTIFSSPFDETAVDFLESLDVPAYKIASFEITDLPLIRYVAKTGKPIIMS
TGIATLEEIQEAVEACREAGCKDLVLLKCTSSYPAPLEDANLRTIPDLAERFNVPVGLSDHTLGILAPVA
AVALGACVIEKHFTLDRSDGGVDSAFSLEPDEFKALVKEVRNAWLALGEVNYELSEKEKKSRQFRRSLYV
VKDIKKGETFTEENVRSVRPGFGLHPKYLDEILGKKANQDIKKGTPL
>gnl|CDD|132626 TIGR03587, Pse_Me-ase, pseudaminic acid biosynthesis-associated methylase. Members of this small clade are methyltransferases of the pfam08241 family and are observed within operons for the biosynthesis of pseudaminic acid, a component of exopolysaccharide and flagellin glycosyl modifications. Notable among these genomes is Pseudomonas fluorescens PfO-1. Possibly one of the two hydroxyl groups of pseudaminic acid, at positions 4 and 8 is converted to a methoxy group by this enzyme
MKTEQEQFWAGEFGKEYIDRNSRQSLVAAKLAMFARALNRLPKIASILELGANIGMNLAALKRLLPFKHI
YGVEINEYAVEKAKAYLPNINIIQGSLFDPFKDNFFDLVLTKGVLIHINPDNLPTAYRELYRCSNRYILI
AEYYNPSPVEISYRGNSGRLWKRDFAGEMMDRYPDLKLVDYGFPYHRDPEFPNDDITWFLLEKR
>gnl|CDD|274662 TIGR03588, PseC, UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase. This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species
LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGD
RVWTTPITFVATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAAKGKLPKAIVPVDFAGKSVDMQAI
AALAKKHGLKIIEDASHALGAEYGGKPVGNCRYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLR
SHGITKDPLLFEKQDEGPWYYEQQELGFNYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPY
FTPLTIPLGSKSAWHLYPILLDQEFGCTRKEVFEALRAAGIGVQVHYIPVHLQPYYRQGFGDGDLPSAEN
FYLAEISLPLHPALTLEQQQRVVETLRKVL
>gnl|CDD|132628 TIGR03589, PseB, UDP-N-acetylglucosamine 4,6-dehydratase (inverting). This enzyme catalyzes the first step in the biosynthesis of pseudaminic acid, the conversion of UDP-N-acetylglucosamine to UDP-4-keto-6-deoxy-N-acetylglucosamine. These sequences are members of the broader pfam01073 (3-beta hydroxysteroid dehydrogenase/isomerase family) family
MFNNKSILITGGTGSFGKAFISRLLENYNPKKIIIYSRDELKQWEMQQKFPAPCLRFFIGDVRDKERLTR
ALRGVDYVVHAAALKQVPAAEYNPFECIRTNINGAQNVIDAAIDNGVKRVVALSTDKAANPINLYGATKL
ASDKLFVAANNISGSKGTRFSVVRYGNVVGSRGSVVPFFKSLKEEGVTELPITDPRMTRFWITLEQGVNF
VLKSLERMLGGEIFVPKIPSMKITDLAEAMAPECPHKIVGIRPGEKLHEVMITEDDARHTYELGDYYAIL
PSISFWNKDRYALGEGGKRVPEGFEYSSGTNTEWLSVEELRELI
>gnl|CDD|274663 TIGR03590, PseG, UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase. This protein is found in association with enzymes involved in the biosynthesis of pseudaminic acid, a component of polysaccharide in certain Pseudomonas strains as well as a modification of flagellin in Campylobacter and Hellicobacter. The role of this protein is unclear, although it may participate in N-acetylation in conjunction with, or in the absence of PseH (TIGR03585) as it often scores above the trusted cutoff to pfam00583 representing a family of acetyltransferases
KILFRADASSEIGLGHVMRCLTLARALHAQGAEVAFACKPLPGDLIDLLLSAGFPVYELPDESSRYDDAL
ELINLLEEEKFDILIVDHYGLDADWEKLIKEFGRKILVIDDLADRPHDCDLLLDQNLGADASDYQGLVPA
NCRLLLGPSYALLREEFYQLATANKRRKPLRRVLVSFGGADPDNLTLKLLSALAESQINISITLVTGSSN
PNLDELKKFAKEYPNIILFIDVENMAELMNEADLAIGAAGSTSWERCCLGLPSLAICLAENQQSNSQQL
>gnl|CDD|274664 TIGR03591, polynuc_phos, polyribonucleotide nucleotidyltransferase. Members of this protein family are polyribonucleotide nucleotidyltransferase, also called polynucleotide phosphorylase. Some members have been shown also to have additional functions as guanosine pentaphosphate synthetase and as poly(A) polymerase (see model TIGR02696 for an exception clade, within this family) [Transcription, Degradation of RNA]
EYGGRTLTLETGKIARQADGAVVVRYGDTVVLVTAVAAKEAKEGQDFFPLTVDYQEKFYAAGKIPGGFFK
REGRPSEKETLTSRLIDRPIRPLFPKGFRNEVQVVATVLSYDPENDPDILAIIGASAALAISGIPFNGPI
AAVRVGYIDGQYVLNPTVDELEKSDLDLVVAGTKDAVLMVESEAKELSEEVMLGAILFGHEAIQPVIEAI
EELAKEAGKEKREFEPPEVDEELKAKVKELAEEAVLKAAYQITEKQERYAALDAIKEEVLEALAAEEEDE
ELAYREKEIKEAFKDLEKKIVRERILKEGKRIDGRDLDTIRPISIEVGVLPRTHGSALFTRGETQALVVT
TLGTERDEQIIDDLEGEYRKRFMLHYNFPPYSVGEVGRLGGPGRREIGHGALAERALKAVLPSEEEFPYT
IRVVSEILESNGSSSMASVCGGSLALMDAGVPIKAPVAGIAMGLIKEGDEYAVLSDILGDEDHLGDMDFK
VAGTRDGITALQMDIKIDGITREIMEQALEQAKEGRLHILDKMNKVISEPRAELSPYAPRIETIKINPDK
IRDVIGPGGKVIREITEETGAKIDIEDDGTVKIAASDGEAAEAAIKMIEGITAEPEVGKIYEGKVVRIMD
FGAFVEILPGKDGLVHISEIANERVEKVEDVLKEGDEVKVKVLEIDRQGRIKLSRKAV
>gnl|CDD|274665 TIGR03592, yidC_oxa1_cterm, membrane protein insertase, YidC/Oxa1 family, C-terminal domain. This model describes full-length from some species, and the C-terminal region only from other species, of the YidC/Oxa1 family of proteins. This domain appears to be univeral among bacteria (although absent from Archaea). The well-characterized YidC protein from Escherichia coli and its close homologs contain a large N-terminal periplasmic domain in addition to the region modeled here [Protein fate, Protein and peptide secretion and trafficking]
NWGLAIILLTIIVRLILLPLTLKQYKSMRKMQELQPKLKEIQEKYKEDPQKLQQEMMKLYKEEGVNPLGG
CLPLLIQMPIFIALYQVLLRSIELRHAPFLWIIDLSSPDPYYILPILMGVTMFLQQKLSPKGPPDPAQQK
MMMYFMPLMFLFFFLSFPAGLVLYWVVSNLFTIIQQLII
>gnl|CDD|274666 TIGR03593, yidC_nterm, membrane protein insertase, YidC/Oxa1 family, N-terminal domain. Essentially all bacteria have a member of the YidC family, whose C-terminal domain is modeled by TIGR03592. The two copies are found in endospore-forming bacteria such as Bacillus subtilis appear redundant during vegetative growth, although the member designated spoIIIJ (stage III sporulation protein J) has a distinct role in spore formation. YidC, its mitochondrial homolog Oxa1, and its chloroplast homolog direct insertion into the bacterial/organellar inner (or only) membrane. This model describes an N-terminal sequence region, including a large periplasmic domain lacking in YidC members from Gram-positive species. The multifunctional YidC protein acts both with and independently of the Sec system [Protein fate, Protein and peptide secretion and trafficking]
NRRLILAIALSFVIFLLWQAWQSDPGPPPPKPPAAAQEASAASATAAATSAAAPAAADAPSAAAAADAAA
ATAKRITVETDVLRASISTKGGDIDSLELKKYKETLDKDSPPVLLLSDGAERLYVAQSGLIGANGADLAL
PGHRTVWQAEGGEYTLTPGQLPVTLTWDNSNGVTVTKTYTFDRDSYLIDVEYKVTNNGDAPVSLSLYGQL
KRDLSPTEKSTYFLHETFTGAAYYTDGEKYQKVSFKDIEKKKLNVETKGGAGWVGMLQHYFASAWIPPAG
SDGTTAFYYGRKLGNNVYIAGFVSPVVTVAPGQSATIKSRLYAGPKEQDVLKAIAPGLDLAVDYGWLWFI
AKPLFWLLDFFHSLVG
>gnl|CDD|274667 TIGR03594, GTPase_EngA, ribosome-associated GTPase EngA. EngA (YfgK, Der) is a ribosome-associated essential GTPase with a duplication of its GTP-binding domain. It is broadly to universally distributed among bacteria. It appears to function in ribosome biogenesis or stability [Protein synthesis, Other]
VAIVGRPNVGKSTLFNRLTGKRDAIVDDTPGVTRDRIYGDAEWGGREFILIDTGGIEEDDDGIDAQIREQ
AEIAIEEADVILFVVDGREGLTPEDEEIAKWLRKSGKPVILVANKIDGPKEDADAAEFYSLGFGEPIPIS
AEHGRGIGDLLDAILELLPEEEEEEEEEEDPIKIAIIGRPNVGKSTLVNALLGEERVIVSDIAGTTRDSI
DIPFERDGKKYTLIDTAGIRRKGKVTEGVEKYSVLRTLKAIERADVVLLVLDATEGITEQDLRIAGLALE
AGKALVIVVNKWDLVEDEKTRKEIKKELRRKLPFLDFAPIVFISALTGQGVDKLLDAIDKVYESANKRIS
TSKLNRVLEEAVAAHPPPLVGGRRVKIKYATQVGTNPPTFVLFGNRPELLPFSYKRYLENQFREAFGFEG
TPIRLEFK
>gnl|CDD|274668 TIGR03595, Obg_CgtA_exten, Obg family GTPase CgtA, C-terminal extension. CgtA (see model TIGR02729) is a broadly conserved member of the obg family of GTPases associated with ribosome maturation. This model represents a unique C-terminal domain found in some but not all sequences of CgtA. This region is preceded, and may be followed, by a region of low-complexity sequence
FEIERDGDGVFVVSGKKIERWVAKTPFNNDEALRRFARKLKKLGVEDALRKAGAKAGDTVRIGDFEFEW
>gnl|CDD|274669 TIGR03596, GTPase_YlqF, ribosome biogenesis GTP-binding protein YlqF. Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members [Protein synthesis, Other]
IQWFPGHMAKARREIKENLKLVDVVIEVLDARIPLSSRNPMIDEIRGNKPRLIVLNKADLADPAVTKQWL
KYFEEKGIKALAVNAKKGAGVKKIIKAAKKLLKEKNEKLKAKGLKNRPIRAMIVGIPNVGKSTLINRLAG
KKVAKVGNRPGVTKGQQWIKLSDNLELLDTPGILWPKFEDQEVGLKLAATGAIKDEALDLEDVALFLLEY
LLEHYPELLKERYKLDELPEDPVELLEAIAKKRGCLLKGGELDLDRAAEILLNDFRKGKLGRISLE
>gnl|CDD|213834 TIGR03597, GTPase_YqeH, ribosome biogenesis GTPase YqeH. This family describes YqeH, a member of a larger family of GTPases involved in ribosome biogenesis. Like YqlF, it shows a cyclical permutation relative to GTPases EngA (in which the GTPase domain is duplicated), Era, and others. Members of this protein family are found in a relatively small number of bacterial species, including Bacillus subtilis but not Escherichia coli [Protein synthesis, Other]
CIGCGAAIQTTDPKKPGYTPKSALEKEEVYCQRCFRLKHYNEIQDVELNDDDFLNLLNSLGDSNALIVYV
VDIFDFEGSLIPELKRFVGGNPVLLVGNKIDLLPKSVNLSKIKEWMKKRAKELGLKPVDIILVSAKKGNG
IDELLDKIKKARNKKDVYVVGVTNVGKSSLINKLLKQNNGDKDVITTSPFPGTTLDLIEIPLDDGHSLYD
TPGIINSHQMAHYLDKKDLKYITPKKEIKPKTYQLNPNQTLFLGGLARFDYLKGEKTSFTFYVSNELNIH
RTKLENADELYNKHLGNLLSPPCLDDKFNLPELVFHTFTIKEKTDIVFSGLGWITVKRGGAKVKVYAPKG
VGVSLRKALI
>gnl|CDD|274670 TIGR03598, GTPase_YsxC, ribosome biogenesis GTP-binding protein YsxC/EngB. Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes [Protein synthesis, Other]
AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVD
LPGYGYAKVSKEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKAD
KLKKSELNKQLKKIKKALKKDADDPSVQLFSSLKKTGID
>gnl|CDD|274671 TIGR03599, YloV, DAK2 domain fusion protein YloV. This model describes a protein family that contains an N-terminal DAK2 domain (pfam02734), so named because of similarity to the dihydroxyacetone kinase family family. The GTP-binding protein CgtA (a member of the obg family) is a bacterial GTPase associated with ribosome biogenesis, and it has a characteristic extension (TIGR03595) in certain lineages. This protein family described here was found, by the method of partial phylognetic profiling, to have a phylogenetic distribution strongly correlated to that of TIGR03595. This correlation implies some form of functional coupling
LADMIRSGANNLENNAEEINALNVFPVPDGDTGTNMLLTMTSAVKEIEKLEEGSVGEVAKALAKGLLMGA
RGNSGVILSQIFRGFAKALENKEELDAEDLAAAFQEAVETAYKAVMKPVEGTILTVLREAAEAAEKAAEE
GDDLEEVMEAAVEAAEKALARTPELLPVLKEAGVVDSGGQGLVVILEGMLAALTGEPIELAPYKPEPPEG
DEIASEEHHDIEFGYCTEFLVKLKDKFDEEKFRKELEKLGDSLVVVGDDDLVKVHVHTNDPGLVLEYGQK
YGELIKIKIENMREQHEEILEGTSNEEKKKEEKEYAIVAVAPGEGIAELFKSLGADVVIEGGQTMNPSTE
DILKAIEKVNAKNVIVLPNNKNIILAAEQAAELADKNVVVIPTKTIVQGLAALLVFDPEASLEDNKEAME
EAIKAVRSGEVTYAVRDTKINGLEIKKGDFLGIVDGKIVAVGKDPEDAAKKLLDKLLDEDSELITIFYGE
DATEEEAEELEAFIEEKYPDVEVEIYEGGQPLYPYLIGVE
>gnl|CDD|274672 TIGR03600, phage_DnaB, phage replicative helicase, DnaB family, HK022 subfamily. Members of this family are phage (or prophage-region) homologs of the bacterial homohexameric replicative helicase DnaB. Some phage may rely on host DnaB, while others encode their own verions. This model describes the largest phage-specific clade among the close homologs of DnaB, but there are, or course, other DnaB homologs from phage that fall outside the scope of this model [Mobile and extrachromosomal element functions, Prophage functions]
SIEAEQAVLGGLLLDNDFIERVMAILKPEHFYSQDHRIIFEAMLDMFAENRPVDPLTLADKLEAEGEAEK
VGGLAYLAEISNNTPSAANISSYARIVREKAKERKLIAACQRIITLACSPDGGTAEQKVEEAQAALLALT
MSDGQEDGFVTFGEVLEDVVRDLDKRFNPKGELTGLSTGLPKLDRLTNGLVKGDLIVIGARPSMGKTTLA
LNIAENVALREGKPVLFFSLEMSAEQLGERLLASKSGINTGNIRTGRFNDSEFNRLLNAVDRLSEKDLYI
DDTGGLTVAQIRSIARRIKRKKGGLDLIVVDYIQLMAPARGRDRNEELGGISRGLKALAKELDVPVVLLA
QLNRGSEKRTDKRPIMSDLRDSGAIEQDADVIGLIHREGYYDAREPPAGIAELILAKNRHGPTGTVELLF
>gnl|CDD|274673 TIGR03601, B_an_ocin, bacteriocin, heterocycloanthracin/sonorensin family. Numerous bacteria encode systems for producing bacteriocins by extensive modification of ribosomally produced precursors. Members of the TOMM class (thiazole/oxazole-modified microcins) are recognizable by association with cyclodehydratase (and often dehydrogenase) maturation proteins. This family consists of a special subclass, the heterocycloanthracin family, that share a homologous leader peptide region and then a repeat region with Cys as every third residue. In Bacillus anthracis and Bacillus cereus, the RiPP (ribosomally translated and post-translationally modified natural product) precursor is encoded far from its maturase genes, and every strain has the system. In other species (e.g. B. licheniformis, B. sorenensis), precursor and maturase genes are close together. Sonorensin, from B. sonorensis MT93, was shown to have broad spectrum antimicrobial activity, affecting Gram-positive and Gram-negative bacteria [Cellular processes, Toxin production and resistance]
MNNFQQELQSLNLNDYQPGNVVYWDQQNQYPYYYIQDDARRCGGCGRCGGCCGGRCGGCGGFRCGGCFGC
FGCFGGCGGCGGCFNCFI
>gnl|CDD|132641 TIGR03602, streptolysinS, bacteriocin protoxin, streptolysin S family. Members of this family are bacteriocin precursors. These small, ribosomally produced polypeptide precursors are extensively processed post-translationally. This family belongs to a class of heterocycle-containing bacteriocins, including streptolysin S from Streptococcus pyogenes, and related bacteriocins from Streptococcus iniae and Clostridium botulinum. Streptolysin S is hemolytic. Bacteriocin genes in general are small and highly diverse, with odd sequence composition, and are easily missed by many gene-finding programs [Cellular processes, Toxin production and resistance]
MLKFNEHILATSNAENNKVTVAPGGCCCCCCCCCFSIATGGGNAQTGGGAAAGQGG
>gnl|CDD|200298 TIGR03603, cyclo_dehy_ocin, thiazole/oxazole-forming peptide maturase, SagC family component. Members of this protein family include enzymes related to SagC, a protein involved in thiazole/oxazole cyclodehydration modifications during biosynthesis of streptolysin S in Streptococcus pyogenes from the protoxin polypeptide (product of the sagA gene). Recent evidence suggests that the YcaO/SagD-like component, not this component, performs an ATP-dependent cyclodehydration. This protein family serves as a marker for widely distributed prokaryotic systems for making a general class of heterocycle-containing bacteriocins. Note that this model does not find all possible examples of bacteriocin biosynthesis cyclodehydratases, an in particular misses the E. coli plasmid protein McbB of microcin B17 biosynthesis [Cellular processes, Pathogenesis]
WDRNEAILDLEESKENFVVPFKEIVKVLVKGIKISDEDIYYNHLEQLTKRNLIRIIDNLNSGPMLIVEDY
QKHLKKSKVLLGKLGLNVCQALSNSNAQNLFLSDDTYLRETAESDLYSKDDIQLKRDRLLTSNLDILESK
SLVDDKKDTLKDYEMIIVCAEHGNISLLRELNRLSLEFKKPFVIAFIDGPFGYVGPLLFPPETACFECLE
RRQLSHLTDFKLYGAFKEHDRKAQNNVSSAYFPLLNILAELVVSEIFFITNMGQSKFEGRLLSIDLPTLE
ITTQDILKVPRCPTCGSLNKIKFEEQNISTRNIVKELLS
>gnl|CDD|274674 TIGR03604, hypothetical_protein, thiazole/oxazole-forming peptide maturase, SagD family component. Members of this protein family include enzymes related to SagD, previously referred to as a scaffold or docking protein involved in the biosynthesis of streptolysin S in Streptococcus pyogenes from the protoxin polypeptide (product of the sagA gene). Newer evidence describes an enzymatic activity, an ATP-dependent cyclodehydration reaction, previously ascribed to the SagC component. This protein family serves as a marker for widely distributed prokaryotic systems for making a general class of heterocycle-containing bacteriocins
GYGLSYDEALLSAIGEALERYSGAYLPDKERIVFASYAELGERALNPLSLGLHSEEQYADPGFPFRPFDP
DTPIQWVPGWSLTTGRPVLVPAQLVYYSYPEERGEDAFVPSTSTGLAAGSTLEEAILNGLLEVIERDAFM
LTWYGRLPLPRIDVDSEDPEFRLLVARLGELTGYEVHLLDITTDLGIPVVGALAKNKDDALPLLVVGAGA
HLDPERALRKALMEAAQMLEALRDNTRSDREYLANMIKDYRLVRDLEDHVLLYALPRAQERFDFLLESEL
PLSTLEDANRPDGLDDLEELLDRLKDAGLEAIVVDITPPDIRALGLYVVRVIIPGLLPITFGHHPFLGGP
RLYTVPRELGLEPLTEEELNPIPHPFP
>gnl|CDD|188352 TIGR03605, antibiot_sagB, SagB-type dehydrogenase domain. SagB of Sterptococcus pyogenes participates in the maturation of streptolysin S from a ribosomally produced precursor polypeptide. Chemically similar systems operate on highly diverse sets of bacteriocin precursors in numerous other bacteria. This model describes a domain within SgaB and homologous regions from other proteins, many of which appear to be involved in biosynthesis of secondary metabolites. While some substrates may be intermediates in non-ribosomal peptide syntheses, others are involved in heterocycle-containing bacteriocin biosynthesis, and can be found near SgaC-like (see TIGR03603, cyclodehydratase) and SgaD-like (see TIGR03604, "docking") proteins. Members of this domain family are heterogeneous in length, as many have a partial second copy of the domain represented here. The incomplete second domain scores below the cutoffs to this model in most cases
TLEELSQLLWYSAGVRSIKLPYNDGILFRRPYPSGGGLYPLEIYLYVKNIEGLPDGVYHYDPEEHRLILI
RAGEENVDAFLVNALLNAENANPPPVIIFITARFWKNFWKYGNRAYRLALLDVGIIIQNFYLVATALGLG
SCAIGGFDDDYIAELLGLDGIEEHVVGVFPVGR
>gnl|CDD|274675 TIGR03606, Quinoprotein_glucose_dehydrogenase_B, dehydrogenase, PQQ-dependent, s-GDH family. PQQ, or pyrroloquinoline-quinone, serves as a cofactor for a number of sugar and alcohol dehydrogenases in a limited number of bacterial species. Most characterized PQQ-dependent enzymes have multiple repeats of a sequence region described by pfam01011 (PQQ enzyme repeat), but this protein family in unusual in lacking that repeat. Below the noise cutoff are related proteins mostly from species that lack PQQ biosynthesis
AFADVPLNPSQFAKAASENFDKKVLLSGLNKPWALLWGPDNQLWVTERATGKILRVNPETGEVKVVFTLP
EIVNDAQHNGLLGLALHPDFMQEKGNPYVYISYTYKNGDKELPNHTKIVRYTYDKSTQTLEKPVDLLAGL
PAGNDHNGGRLVFGPDGKIYYTIGEQGRNQGANFFLPNQAQHTPTQQELNGKDYHAYMGKVLRLNLDGSI
PKDNPSINGVVSHIFTYGHRNPQGLAFTPDGTLYASEQGPNSDDELNIIVKGGNYGWPNVAGYKDDSGYV
YANYSAAANKSIKTLAQNGIPAGVPVTKESEWTAKNFVPPLKTLYTVQDTYNYNDATCGEMTYICWPTIA
PSSAYYYKGGEKGITGWENSLLIPSLKRGVIYRIKLDPDYSTVYGDAVPMFKTNNRYRDVIASPDGNVLY
VATDNFGNVQKDDGSVTNTLENPGSIIVFTYKGK
>gnl|CDD|274676 TIGR03607, TIGR03607, patatin-related protein. This bacterial protein family contains an N-terminal patatin domain, where patatins are plant storage proteins capable of phospholipase activity (see pfam01734). Regions of strong sequence conservation are separated by regions of significant sequence and length variability. Members of the family are distributed sporadically among bacteria. The function is unknown [Unknown function, General]
ELRLALVMYGGVSLAVYMHGVTKEINRLVRASRAYHRYADEESAGTEAVYGRLLAALGAHVRLRVRVDVI
SGTSAGGINGVLLAYALAYGADLDPLRDLWLELADIDALLRPDAKAWPRLRRPGSLLDGEYFLPLLLDAL
QAMVRAGPAGRSLLPTGARLDLFVTATDLRGRSTRLFDDDGTVVEEREHRGVFRFTEADRTGGRLSDFDP
ANAPRLAFAARATASFPGAFPPSRLAEIDDVLARRDLPWGGRDAFLHPDFPDYAELGSDPRPRYVVDGGV
LDNRPFAPALEAIRARPARREVDRRLVYIDPSPDAPDPPSGDGAGRPGFFATILGALSGLPRYQSIRDDL
EAIRRHNRRVRRLRAIVDARRPEVARLVEALFGRTLLESPTPELLDAYRLRALEQAAERAGAAYAAYGQL
KLLGAADGLAELIAEAAGVGRDSDRAHAVGTILRAWPDRRALPAPDALPEGAAWGAPAFDRAFDLAFRLR
RLAFLLRRLDALYAAVGGRDRIRGEQLGLHLLPEALRALRDRIYRALRPLARRAPAVRSDELRGWLERTG
DARLALAAGDPDPGALEGAADQLAKGFAIDRLGDVRERLARALADLDDDVDAALAAAAVLSILAGMSARA
RRRVLLGELEELLSYLALYLGLLFLDVATLPLLGGEDLDEIDPIELDRISPDDATSLRGPDTPDKLAGIE
LGNFGAFFSRSWRENDWLWGRLDGADRLVDILLSPRRL
>gnl|CDD|188353 TIGR03608, L_ocin_972_ABC, putative bacteriocin export ABC transporter, lactococcin 972 group. A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKA
SKFRREKLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQ
QRVALARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL
>gnl|CDD|132648 TIGR03609, S_layer_CsaB, polysaccharide pyruvyl transferase CsaB. The CsaB protein (cell surface anchoring B) of Bacillus anthracis adds a pyruvoyl group to peptidoglycan-associated polysaccharide. This addition is required for proteins with an S-layer homology domain (pfam00395) to bind. Within the larger group of proteins described by pfam04230, this model represents a distinct clade that nearly exactly follows the phylogenetic distribution of the S-layer homology domain (pfam00395) [Cell envelope, Surface structures, Protein fate, Protein and peptide secretion and trafficking]
ALLCGYYGFGNLGDEALLAALLRELPPGVEPTVLSNDPAETAKLYGVEAVNRRSLLAVLRALRRADVVIW
GGGSLLQDVTSFRSLLYYLGLMRLARLFGKPVILWGQGIGPLRRRLSRWLVRRVLRGCRAISVRDAASYR
LLKRLGIPAELAADPVWLLPPEPWPGGEPLPEPVIVVSLRPWPLLDVSRLLRLLRALDRLQRDTGAFVLF
LPFQQPQDLPLARALRDQLLGPAEVLSPLDPEELLGLFASARLVIGMRLHALILAAAAGVPFVALSYDPK
VRAFAADAGVPGFELAAL
>gnl|CDD|274677 TIGR03610, RutC, pyrimidine utilization protein C. This protein is observed in operons extremely similar to that characterized in E. coli K-12 responsible for the import and catabolism of pyrimidines, primarily uracil. This protein is a member of the endoribonuclease L-PSP family defined by pfam01042
MPKKVIIPAGTSKPLAPFVPGTLADGVVYVSGTLPFDKDNNVVHVGDAAAQTRHVLETIKSVIETAGGTM
DDVTFNHIFIRDWADYAAINEVYAEYFPGEKPARYCIQCGLVKPDALVEIASVAHIG
>gnl|CDD|211851 TIGR03611, RutD, pyrimidine utilization protein D. This protein is observed in operons extremely similar to that characterized in E. coli K-12 responsible for the import and catabolism of pyrimidines, primarily uracil. This protein is a member of the hydrolase, alpha/beta fold family defined by pfam00067
HYELHGPPDADAPVVVLSSGLGGSGSYWAPQLAVLTQRFHVVTYDHRGTGRSPGELPPDYSIAHMADDVL
QLLDALGIERFHFVGHALGGLIGLQLALDYPERLTSLVLINGWSRPDPHTRRCFDVRIALLYHAGPEAYV
HAQPLFLYPADWISENAPRLAADEAHALAHFPGKNNVLRRINALEAFDVSARLDRIRHPVLLIAARDDML
VPYTCSLRLAAALPNAQLKLLPYGGHASNVTDPETFNR
>gnl|CDD|163355 TIGR03612, RutA, pyrimidine utilization protein A. This protein is observed in operons extremely similar to that characterized in E. coli K-12 responsible for the import and catabolism of pyrimidines, primarily uracil. This protein is a member of the luciferase family defined by pfam00296 and is likely a FMN-dependent monoxygenase [Unknown function, Enzymes of unknown specificity]
MDIGVFIPIGNNGWLISENAPQYMPSFELNKAIVQKAEQYGFDFALSMIKLRGFGGKTEFWDHNLESFTL
MAGLAAVTSRIKLYATAATLTLPPAIVARMASTIDSISNGRFGVNLVTGWQKPEYSQMGLWPGDEYFADR
YEYLAEYVQVLRELWETGVSDFKGEFFQMDDCRVSPRPQAEMKIICAGQSDAGMAFSAQYADYNFCFGKG
VNTPTAFAPTAARLLAAAEKTGRDVGSYVLFMVIADETDEAARAKWEHYKDGADEEALAWLTLQGAKDTK
SGADTNVRQMADPTSAVNINMGTLVGSYETVARMLDEVAEVPGTGGVLLTFDDFLEGVEDFGTRIQPLMT
SRAHV
>gnl|CDD|274678 TIGR03613, RutR, pyrimidine utilization regulatory protein R. This protein is observed in operons extremely similar to that characterized in E. coli K-12 responsible for the import and catabolism of pyrimidines, primarily uracil. This protein is a member of the TetR family of transcriptional regulators defined by the N-teminal model pfam00440 and the C-terminal model pfam08362 (YcdC-like protein, C-terminal region)
KRSRAVEAKRKAILSAALDTFSRFGFHGTSLEQIAELAGVSKTNLLYYFPSKDALYLAVLRQILDIWLSP
LKAFTEDFAPLAAIKAYIRAKLEMSRDHPQASRLFCMEMLAGAPLLMDELTGPLKALIDAKSAVIAGWVK
SGKLAPIDPQHLIFMIWASTQHYADFAPQVEAVTGKTLRDEVFFNETVANVQRIVLEGILPR
>gnl|CDD|163356 TIGR03614, RutB, pyrimidine utilization protein B
TLPARPEPITLDPEQTALIVVDMQNAYATPGGYLDLAGFDVSGTKPVIENIKKAVTAARAAGIQVIYFQN
GWDNDYVEAGGPGSPNWHKSNALKTMRKRPELQGKLLAKGTWDYELVDELQPQPGDIVLPKPRYSGFFNT
PLDSMLRARGIRNLVFTGIATNVCVESTLRDGFHLEYFGVVLEDATHQAGPDFMQKAALYNIETFFGWVS
DVADFCGTFSQNAPLA
>gnl|CDD|132654 TIGR03615, flavoprotein_oxidoreductase, pyrimidine utilization flavin reductase protein F. This protein is observed in operons extremely similar to that characterized in E. coli K-12 responsible for the import and catabolism of pyrimidines, primarily uracil. This protein is a member of the flavin reductase family defined by pfam01613. Presumably, this protein recycles the flavin of the RutA luciferase-like oxidoreductase
VDQQAFRDAMSRLGAAVNIITTDGPAGRAGFTASAVCSVTDTPPTLLVCLNRSASAYPAFKQNGTLCVNT
LAAGQEDLSNLFGGKTPMEERFAAGQWRTLVTGAPVLEDALVSFDCRISQSHSVGTHDILFCAVEAIAHS
AGADALVYFNRRYHTL
>gnl|CDD|132655 TIGR03616, Putative_pyrimidine_permease_RutG, pyrimidine utilization transport protein G. This protein is observed in operons extremely similar to that characterized in E. coli K-12 responsible for the import and catabolism of pyrimidines, primarily uracil. This protein is a member of the uracil-xanthine permease family defined by TIGR00801. As well as the The Nucleobase:Cation Symporter-2 (NCS2) Family (TC 2.A.40)
MAEPWFPKWKPKQGSLEHHPVAPDERLPAAQTIVMGLQHAVAMFGATVLMPLLMGFDPNLTILMSGIGTL
LFFLITGGRVPSYLGSSAAFVGAVIAATGYNGQGTNPNIALALGGIIACGLVYAAIGLVVMRTGTRWIER
LMPPVVTGAVVMAIGLNLAPIAVKSVSASGFDSWMAVLTILCIGAVAVFTRGMLQRLLILVGLIAAYLAY
FILTNVFGLGKAVDFSPISQAAWFGLPNFHTPVFNANAMLLIAPVALILVAENLGHFKAVAGMTGRNLDP
YMGRAFVGDGLATMLSGSVGGTGVTTYAENIGVMAVTKVYSTLVFVAAAVFAILLGFSPKFGALIHTIPV
AVLGGASIVVFGLIAVAGARIWVQNKVDLTQNGNLIMVAVTLVLGAGDFALTIGAFTLGGIGTATFGAIV
LNALLNRDS
>gnl|CDD|132656 TIGR03617, F420_MSMEG_2256, probable F420-dependent oxidoreductase, MSMEG_2256 family. Coenzyme F420 has a limited phylogenetic distribution, including methanogenic archaea, Mycobacterium tuberculosis and related species, Colwellia psychrerythraea 34H, Rhodopseudomonas palustris HaA2, and others. Partial phylogenetic profiling identifies protein subfamilies, within the larger family called luciferase-like monooxygenanases (pfam00296), that appear only in F420-positive genomes and are likely to be F420-dependent. This model describes one such subfamily, exemplified by MSMEG_2256 from Mycobacterium smegmatis [Unknown function, Enzymes of unknown specificity]
ARALEEAGFDGLWTFETAHDPFLPLTLAAEATRRVELGTSVAIAFPRSPMHLAYAAWDLQLYSGGRFVLG
LGTQVKAHIERRFSMPWSRPAARMREYILALRAIWDAWQDGTRLDFRGEFYTHTLMTPFFSPGPHPYGPP
PVYLAAVGPRMTRVAGEVADGLLVHPFTSARYLREVTLPALARGLARAGRSRSDFEVAAPAFVATGEDDE
ELAEARAATRQQIAFYGSTPAYRPVLELHGWGDLQPELHRLSKQGRWAEMGGLIDDEVLAAFAVVGPPEE
LAAALRARFGGLADRVSLYFPYPPGPEFVRALLDALRG
>gnl|CDD|274679 TIGR03618, Rv1155_F420, PPOX class probable F420-dependent enzyme. A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomyces, make F420. The Partial Phylogenetic Profiling algorithm identifies this members of this protein family as high-scoring proteins to the F420 biosynthesis profile. A member of this family, Rv1155, was crytallized after expression in Escherichia coli, which does not synthesize F420; the crystal structure shown to resemble FMN-binding proteins, but with a recognizable empty cleft corresponding to, yet differing profounding from, the FMN site of pyridoxine 5'-phosphate oxidase. We propose that this protein family consists of F420-binding enzymes [Unknown function, Enzymes of unknown specificity]
LRDLLSERRLAVLATIRPDGRPQLSPVWFALDGDELVFSTTAGRAKARNLRRDPRVSLSVLDPDGPYRYV
EIEGTAEVSPDPDAVRDLVDRLAERYRGAAGEDEYRRPMVDPRRVVVRVTPERVYG
>gnl|CDD|274680 TIGR03619, F420_Rv2161c, probable F420-dependent oxidoreductase, Rv2161c family. Coenzyme F420 has a limited phylogenetic distribution, including methanogenic archaea, Mycobacterium tuberculosis and related species, Colwellia psychrerythraea 34H, Rhodopseudomonas palustris HaA2, and others. Partial phylogenetic profiling identifies protein subfamilies, within the larger family called luciferase-like monooxygenanases (pfam00296), that appear only in F420-positive genomes and are likely to be F420-dependent. This model describes a domain found in a distinctive subset of bacterial luciferase homologs, found only in F420-biosynthesizing members of the Actinobacteria [Unknown function, Enzymes of unknown specificity]
AELARAAEELGFDSLLAYEHVAIPARRETPWPDSGGGDAPDRTLDPFVALAFAAAVTSRLRLGTGVLVLP
QRDPLLLAKQAATLDLLSGGRLRLGVGVGWLREEFRALGVDFDERGRLLDEAIEALRALWTQDPVSFHGE
FVDFDPAVVRPKPVQRPPPIWIGGNSEAALRRAARLGDGWMPFGPPVDRLAAAVARLRDLAAAAGRDPDA
VEVVLVRTDPDGDADADAEDLAAYADLGVTRLVVNL
>gnl|CDD|274681 TIGR03620, F420_MSMEG_4141, probable F420-dependent oxidoreductase, MSMEG_4141 family. Members of this protein family, related to F420-dependent oxidoreductases within the larger family of a bacterial luciferase (an FMN-dependent enzyme), occurs only within the small subset of species that synthesize F420. Most such proteins are from members of the Actinobacteria, but at least one species, Sphingomonas wittichii, belongs to the Alphaproteobacteria [Unknown function, Enzymes of unknown specificity]
LGRFGVWSSQLRWSPDARARAEAAAELEELGYGALWLGGSPGAELDLVEALLDATERLVVATGIVNIWVR
PADEVAASFARLEAAHPGRFLLGLGVSHPPLVGRYRKPLAALVEYLDELDAAGVPRERRVLAALGPRMLE
LARDRAAGAHPYLVTPEHTARAREILGPGPLLAPEQKVVLDTDAEQARAIARVALRFYLGLPNYVNNLLR
LGFTEDDLAGGGSDRLVDALVAWGDADTVAARVREHLDAGADHVAVQVLTDDPTPLPREQWRELAGAL
>gnl|CDD|200301 TIGR03621, F420_MSMEG_2516, probable F420-dependent oxidoreductase, MSMEG_2516 family. Coenzyme F420 is produced by methanogenic archaea, a number of the Actinomycetes (including Mycobacterium tuberculosis), and rare members of other lineages. The resulting information-rich phylogenetic profile identifies candidate F420-dependent oxidoreductases within the family of luciferase-like enzymes (pfam00296), where the species range for the subfamily encompasses many F420-positive genomes without straying beyond. This family is uncharacterized, and named for member MSMEG_2516 from Mycobacterium smegmatis [Unknown function, Enzymes of unknown specificity]
FRFGIALEGPESARDLVDLARRAEDAGFDVLTVPDHLGAPAPFAALTAAAAATTTLRLGTLVLNNDFRHP
ALLAREAATLDALSDGRLELGLGAGYVRSEFDAAGIPFDSPGVRVDRLEETLTYLRRLLADEPVTFPGHH
GTPRPRQGPRPPLLIGGNGDRLLRLAARHADIVGLAGASANPDAGLLTHATADPLAERVAFVREAAGDRF
DDIELNLLIQAVVVTDDREAAAAELAATLPGLTPEQILESPYVLIGSPEQIAERLRERRERYGVSYFTVL
DPHADAFAPVIALLR
>gnl|CDD|132661 TIGR03622, urea_t_UrtB_arc, urea ABC transporter, permease protein UrtB. Members of this protein family are ABC transporter permease subunits restricted to the Archaea. Several lines of evidence suggest this protein is functionally analogous, as well as homologous, to the UrtB subunit of the Corynebacterium glutamicum urea transporter. All members of the operon show sequence similarity to urea transport subunits, the gene is located near the urease structural subunits in two of three species, and partial phylogenetic profiling identifies this permease subunit as closely matching the profile of urea utilization
AALLLQFLDSFAFIVLAAVGLAVIFGMMGVINLAHGEFILVGAYGTTLTYHQAGLPLPVAMVSGVVMTVI
FGIIVERLIIQHLYDRLLDSMVATFGLALILTQGLRITFGNSLDSISTPFGNVAYGPYTYSTYRVFLPLV
AIGVLVGLYVLFTRTEFGVRARATIQDPETARAMGVDTDRMYVTTFAIGSGLAGLTGALYAPIGAITPDR
GSIFLVEAFVAVVVGGPSVVLGTALAGGLLGFINAVFSNLYGTFVGLIALLIVAIIALRVLPDGITGYIE
QWR
>gnl|CDD|274682 TIGR03623, TIGR03623, probable DNA repair protein. Members of this protein family are bacterial proteins of about 900 amino acids in length. Members show extended homology to proteins in TIGR02786, the AddB protein of double-strand break repair via homologous recombination. Members of this family, therefore, may be DNA repair proteins
GALVLTANNRLARRLRQEYARAQLAQGRKVWTTPDILPWSQWLQQLWEEALLDGDAPELPHALLSSFQEQ
FLWEEVIAQSEPAGALLDVDGLARLAQEAWRLLHEWGLPPDAGEASLTEETRLFLQWRTRFEARCRREGW
IDAAQLPEQLLDLLEQGGLRLPKQIILAGFDELTPQQQALLAALEARGVDVQQWLPESGEQASAQRLACA
DPEAEIRAAARWARQQLEANPAARIGVVVPNLEALRSQLARILDDVLHPQALLPTSADAPRPFNISLGRP
LAEEPLVRTALLLLELLRGKLEQAEASALLRSPYIAGAEEERLARAQLDARLRELAEASLTLAQLLARAG
EENRLQLCPLLAELLSAAMAFLQKPSSLRLLPSAWAARFQRWLKALGWPGDRALDSEEYQAVKAWEELLA
EFAALDLVSPALTFSEALRLLRQLAAETLFQPETPEAPIQVLGLLEAAGLQFDALWVMGLTDEQWPAPPR
PNPFLPLALQRAVGMPHASAERELDYARQVTQRLLKSAPEVVFSYPRRDGDRELRPSPLIAHLPLKAEED
AELADYQDLAAAVAAGSRLEVLDDAQAPPLAAGERISGGTGLLKAQAACPFRAFAQHRLGARALEEPVDG
LDALERGTLVHRVLELFWERLKNQEALNALDEAELEQLIAEAIEEALAEERARHSQTFPERFLELEQERL
LQLLLEWLELERKRPPFEVVATEQNHSIEIGGLELKLRIDRIDRLADGSRLIIDYKTGAPSVKDWLGERP
VEPQLPLYALLAEDEVAGVAFAQVRAGKVKFAGLAEDAELIPGVKAFAKLKAEDEPDSWEAVLARWRQEL
TELAEEFSAGYAAVDPKNGETTCRYCDLQPLCRI
>gnl|CDD|274683 TIGR03624, TIGR03624, putative hydrolase. Members of this protein family have a phylogenetic distribution skewed toward the Actinobacteria (high GC Gram-positive bacteria), but with a few members occuring in the Archaea and Chloroflexi. The function is unknown [Unknown function, General]
VNWDLAARIARQLARPGPDLSTAEAVVDALAEAVRLAELWLRGVTGLAPTGPPTAEAWDRAEWIDATVPT
WKRLCEPVAEKVSTALTAAGPMGAMMGQMGGANTGAQLGAALGFLASEVLGQYDPGLPLAPAGRLALVPP
NIAAVARGLGVPPDEFRLWLALHEVTHARQFRHVPWLRDHLLGAVEAYAAGLAIDTSTLEERLRQVDESL
RDPSELEEALEQGLLELVQTPEQREALDRLETLLALVEGWADHVMDAAGPAVVPSVAALREAFRRRRATG
GPAERAFRRLLGLDAKPRQYREGAAFWRAVVEAVGMAGRNRVWEHPDTLPTADELDNPARWIDRVL
>gnl|CDD|274684 TIGR03625, L3_bact, 50S ribosomal protein uL3, bacterial form. This model describes bacterial (and mitochondrial and chloroplast) class of ribosomal protein L3. A separate model describes the archaeal form, where both belong to pfam00297. The name is phrased to meet the needs of bacterial genome annotation. Organellar forms typically will have transit peptides, N-terminal to the region modeled here
GLLGKKVGMTQIFTEDGKAVPVTVIEVGPNVVTQVKTVEKDGYNAVQLGFGEKKEKRVNKPEAGHFAKAG
VEPKRHLKEFRVDDAAGYEVGDEITVDIFEAGQKVDVTGTSKGKGFAGVMKRHNFSGGPASHGSSKSHRA
PGSIGQRQTPGRVFKGKKMAGHMGNERVTVQNLEVVKVDAERNLLLVKGAVPGAKGSLVLVK
>gnl|CDD|274685 TIGR03626, L3_arch, ribosomal protein uL3, archaeal form. This model describes exclusively the archaeal class of ribosomal protein L3. A separate model (TIGR03625) describes the bacterial/organelle form, and both belong to pfam00297. Eukaryotic proteins are excluded from this model [Protein synthesis, Ribosomal proteins: synthesis and modification]
HRPRRGSLAFSPRKRAKRIVPRIRSWPEVDGEPKLQGFAGYKAGMTHVIMVDDRKNSPTEGKEISVPVTV
LEAPPLRVAAIRAYGKDPYGLKVLTEVWANNLDKELSRKITLPKNYDVEEKLEKIEELLENDADDVRLIV
HTQPKLVTGVPKKKPEIMEIRIGGGSVEERFEYALSILGKEISVSDVFKEGQLVDVIAVTKGKGFQGVVK
RWGVKLLPRKHKRRKGGRHIGTLGPWTPSRVRWTVPQAGQMGYHQRTEYNKRILKIGEDGDEITPKGGFV
NYGLVRNDYVLIKGSVPGPSKRLIRLRDAIRPPKPPEGAPEITYISLESK
>gnl|CDD|132666 TIGR03627, uS9_arch, ribosomal protein uS9, archaeal form. This model describes exclusively the archaeal ribosomal protein S9P. Homologous eukaryotic and bacterial ribosomal proteins are excluded from this model [Protein synthesis, Ribosomal proteins: synthesis and modification]
VVITSGKRKTAIARATIREGKGRVRINGVPVELYPPELARLKIMEPLILAGDIAKEVDIDVKVSGGGIMG
QADAARTAIARGLVEFTGDKELRDAFRAYDRTLLVNDPRRKEPKKPGGRGARAKRQKSYR
>gnl|CDD|274686 TIGR03628, arch_S11P, ribosomal protein uS11P, archaeal form. This model describes exclusively the archaeal ribosomal protein S11P. It excludes homologous ribosomal proteins S14 from eukaryotes and S11 from bacteria [Protein synthesis, Ribosomal proteins: synthesis and modification]
KWGIAHIYSSFNNTIITITDITGAETIARVSGGMVVKADRDEPSPYAAMQAARRAAEKALERGITGVHIK
VRAPGGNGSKTPGPGAQAAIRALARAGLKIGRIEDVTPIPHDGTRPP
>gnl|CDD|213839 TIGR03629, uS13_arch, ribosomal protein uS13, archaeal form. This model describes exclusively the archaeal ribosomal protein S13P. It excludes the homologous eukaryotic 40S ribosomal protein S18 and bacterial 30S ribosomal protein S13 [Protein synthesis, Ribosomal proteins: synthesis and modification]
EFKYIVRIADTDLDGNKPVEYALTGIKGIGRRFARAIARKLGVDPNAKLGYLDDEEIEKLEEAVENYEYG
IPSWLLNRRKDYETGEDLHLIGSDLDMTVREDINRMKKIRSYRGIRHELGLKVRGQRTKSTGRRGRTVGV
SRKK
>gnl|CDD|274687 TIGR03630, 30S_ribosomal_protein_S17P, ribosomal protein uS17, archaeal form. This model describes exclusively the archaeal ribosomal protein S17P. It excludes the homologous ribosomal protein S17 from bacteria, and is not intended for use on eukaryotic sequences, where some instances of ribosomal proteins S11 score above the trusted cutoff [Protein synthesis, Ribosomal proteins: synthesis and modification]
IGIPVKPPEEECNDPKCPFHGHLKVRGQILEGVVVSDKMNKTVVVEREYLYYIRKYERYERRRSKIHAHN
PPCIDVKVGDIVIIAETRPLSKTKSFVVLGKV
>gnl|CDD|274688 TIGR03631, uS13_bact, ribosomal protein uS13, bacterial form. This model describes bacterial ribosomal protein S13, to the exclusion of the homologous archaeal S13P and eukaryotic ribosomal protein S18. This model identifies some (but not all) instances of chloroplast and mitochondrial S13, which is of bacterial type [Protein synthesis, Ribosomal proteins: synthesis and modification]
RIAGVDIPNNKRVEIALTYIYGIGRTRARKILEKAGIDPDKRVKDLTEEELNAIREEIEAKYKVEGDLRR
EVTLNIKRLMDIGCYRGLRHRRGLPVRGQRTKTNARTRKGPRK
>gnl|CDD|274689 TIGR03632, uS11_bact, ribosomal protein uS11, bacterial form. This model describes the bacterial 30S ribosomal protein S11. Cutoffs are set such that the model excludes archaeal and eukaryotic ribosomal proteins, but many chloroplast and mitochondrial equivalents of S11 are detected [Protein synthesis, Ribosomal proteins: synthesis and modification]
GIVHIHATFNNTIVTITDPQGNVLSWASAGTSGFKGSRKSTPYAAQMAAEKAAKKAMEMGMKTVDVYVKG
PGAGRESAIRALQAAGLEVTSIKDVTPIPHNGCRPPKR
>gnl|CDD|163366 TIGR03633, arc_protsome_A, proteasome endopeptidase complex, archaeal, alpha subunit. This protein family describes the archaeal proteasome alpha subunit, homologous to both the beta subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated [Protein fate, Degradation of proteins, peptides, and glycopeptides]
MGYDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIG
AATSGLVADARVLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDGG
PRLFETDPSGALLEYKATAIGAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEDKLTPENVEVAYI
TVEDKKFRKLSVEE
>gnl|CDD|274690 TIGR03634, arc_protsome_B, proteasome endopeptidase complex, archaeal, beta subunit. This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated [Protein fate, Degradation of proteins, peptides, and glycopeptides]
GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELR
RGRPMSVKALATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVL
EDEYREDMSVEEAKKLAVRAIKSAIERDVASGNGIDVAVITKDGV
>gnl|CDD|274691 TIGR03635, uS17_bact, ribosomal protein uS17, bacterial form. This model describes the bacterial ribosomal small subunit protein S17, while excluding cytosolic eukaryotic homologs and archaeal homologs. The model finds many, but not, chloroplast and mitochondrial counterparts to bacterial S17 [Protein synthesis, Ribosomal proteins: synthesis and modification]
RKTLQGVVVSDKMDKTVVVLVERRVKHPLYKKIVKRTKKYHAHDENNECKVGDVVRIIETRPLSKTKRWR
LV
>gnl|CDD|274692 TIGR03636, 50S_ribosomal_protein_L23P, ribosomal protein uL23, archaeal form. This model describes the archaeal ribosomal protein L23P and rigorously excludes the bacterial counterpart L23. In order to capture every known instance of archaeal L23P, the trusted cutoff is set lower than a few of the highest scoring eukaryotic cytosolic ribosomal counterparts [Protein synthesis, Ribosomal proteins: synthesis and modification]
PLVTEKAMNLIEKENKLTFIVDRRATKGDIKRAVEKLFDVKVEKVNTLITPRGEKKAYVKLAEEYSAEEI
ASRLGVF
>gnl|CDD|132676 TIGR03637, cas1_YPEST, CRISPR-associated endonuclease Cas1, subtype I-F/YPEST. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes the Cas1 protein particular to the YPEST subtype of CRISPR/Cas system
ILHSKRANIYYLEKCRVLVNGGRVEYVTDEGNESLYWNIPIANTTVLLLGTGTSITQAAMRELAKAGVMV
GFCGGGGTPLFSANEVEVDVSWLSPQSEYRPTEYLQAWMKFWFDDDKRLAAAKAFQLIRIELLSQHWKKS
LDLREHGFYPDENALEALLNRYEQDIDRAENSQTLLAAEARLTKALYKLAANTTGYGDFTRDKRGGGIDP
ANRFLDHGNYLAYGLAATALWVLGIPHGLAVLHGKTRRGGLVFDVADLIKDALVLPQAFICAMAGDSEQE
FRQQCIAILQDSDALDYMIESIKEIAL
>gnl|CDD|274693 TIGR03638, cas1_ECOLI, CRISPR-associated endonuclease Cas1, subtype I-E/ECOLI. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes the Cas1 protein particular to the ECOLI subtype of CRISPR/Cas system
LAELPRVKDRISFLYLERGRLDVDDGAVVLIDAEGIRVHIPVASLSCLLLGPGTSVTHAAVRLLARHGCL
VVWVGEGGVRFYAAGLGGTRSSDRLLRQARLWADPRRRLEVARRMYAMRFGEELPPRLTLEQLRGLEGAR
VREAYRLLAEKYGVPWKGRRYDPGDWEAGDPVNRALSAANACLYGICHAAILAAGYSPALGFIHTGKPLS
FVYDIADLYKAETTIPLAFSLAATNPDNLEREVRHACRDLFRETKLLPRIIPDIEELL
>gnl|CDD|274694 TIGR03639, cas1_NMENI, CRISPR-associated endonuclease Cas1, subtype II/NMENI. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is a prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes the Cas1 variant of the NMENI subtype of CRISPR/Cas system
WRVVEISNHEKLSLKLNQLVIKKDGEEVTLPLEDIDVILIENPQITISSALLSALAENNIALIFCDEKHL
PVGQLLPFYGHHRSLKRLKLQIDWSLPLKKQLWQKIIKQKILNQAFVLEKLNLDEDSEKLENLANKVESG
DKTNREAHAAKLYFKTLFGKDFSRDDDGEDPINAALNYGYAILRSAVARALVKSGLLPRLGIFHKSEYNP
FNLADDLMEPFRPLVDYLVYELLIEEFNDDLTKEIKRKLFSVLNEKIIYNGKNMSLNNAIDKYVASLI
>gnl|CDD|188360 TIGR03640, cas1_DVULG, CRISPR-associated endonuclease Cas1, subtype I-C/DVULG. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes the Cas1 protein particular to the DVULG subtype of CRISPR/Cas system
KLLNTLYVTTQGTYLHKDGETVVVEVEGEKKARVPLHHLGGIVCFGNVGLSPFLMGRCAEDGISLVFLTE
NGRFLARVEGPVSGNVLLRRAQYRAADDPERSLAIARSIVAGKIRNARQVLLRAARDHGEEDDAAALEAA
ADRLAVALRRLQRADDLDSLRGIEGEAARLYFAVFDHLLRQDRPAFRFDGRSRRPPLDPVNALLSFLYTL
LTHDCRSALEGVGLDPAVGFLHRDRPGRPSLALDLMEEFRAVLADRLALSLINRGQLTAKDFEVREGGAV
LLTDDARKTVLVAYQERKQEEILHPFLGEKVPLGLLPHVQARLLARHLRGDLDGYPPFLW
>gnl|CDD|274695 TIGR03641, cas1_HMARI, CRISPR-associated endonuclease Cas1, subtype I-B/HMARI/TNEAP. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes Cas1 subgroup that includes Cas1 proteins of the related HMARI and TNEAP subtypes of CRISPR/Cas system
KTYYIFSDGRLKRKENTLYFENKDEKKYIPVENIDEIYVFGEVSLNSKALSFLSKKGIPIHFFNYYGYYS
GSFYPRESLNSGYLIVKQVEHYLDSEKRLELARSFVEGAAHNMRRVLKYYKKRGKDLDKIEAYLESLKEA
KSINELMGVEGNIRKTYYSAFDEILPKGFRFEKRTRRPPKNELNALISFGNSLLYTTVLSEIYKTHLNPT
ISYLHEPSERRFSLALDIAEIFKPIIVDRLIFRLVNKKIIKEKHFEKDLNGVLLNEEGRKKFIKEFEEKL
KTTIKHRKLKRKVSYRRLIRLELYKLIKHLLGEEEYKPFK
>gnl|CDD|274696 TIGR03642, cas_csx14, CRISPR-associated protein, Csx14 family. This model describes a protein N-terminal protein sequence domain strictly associated with CRISPR and CRISPR-associated protein systems. This model and TIGR02584 identify two separate clades from a larger homology domain family, both CRISPR-associated, while other homologs are found that may not be. Members are found in bacteria that include Pelotomaculum thermopropionicum SI, Thermoanaerobacter tengcongensis MB4, and Roseiflexus sp. RS-1, and in archaea that include Thermoplasma volcanium, Picrophilus torridus, and Methanospirillum hungatei. The molecular function is unknown
GTSPMVITEAIDYLKKKGEPISDVILIYTKDPYVLSALRALKDSLLKKFYKAEVHKIPLKFDDILSDEDI
LTFMSIAAKEVKKERENYGCERIIVNISGGRKIMTIILALYAQLLFEDEVYHII
>gnl|CDD|132682 TIGR03643, TIGR03643, TIGR03643 family protein. This model describes an uncharacterized bacterial protein family. Members average about 90 amino acids in length with several well-conserved uncommon amino acids (Trp, Met). The majority of species are marine bacteria. Few species have more than one copy, but Vibrio cholerae El Tor N16961 has three identical copies [Hypothetical proteins, Conserved]
DIDRIIEMAWEDRTPFEAIEQQFGLSEKEVIKLMRQNLKPSSFKLWRKRVSGRKTKHAKRRDSERTRFKC
KR
>gnl|CDD|274697 TIGR03644, marine_trans_1, probable ammonium transporter, marine subtype. Members of this protein family are well conserved subclass of putative ammonimum transporters, belonging to the much broader set of ammonium/methylammonium transporter described by TIGR00836. Species with this transporter tend to be marine bacteria. Partial phylogenetic profiling (PPP) picks a member of this protein family as the single best-scoring protein vs. a reference profile for the marine environment Genome Property for a large number of different query genomes. This finding by PPP suggests that this transporter family represents an important adaptation to the marine environment
YALDTFYFLISGALVMWMAAGFAMLEAGLVRSKNTTEILTKNIALFAIACIMYLLVGYNIMYPGGGIFLG
GILGSFLLGADNPVGDLIAGFEGDADYSSGSDFFFQVVFVATAMSIVSGAVAERMKLWPFLLFAVVLTGF
IYPIEGSWTWGGGWLDDLGFSDFAGSGIVHMAGAAAALAGVLLLGPRKGKYGKNGEVNPIPGSNLPLATL
GTFILWMGWFGFNGGSQLALSDVADANAVARIFANTNAAAAGGAIAALLLTKLLFGKADLTMVLNGALAG
LVAITAEPLTPSPLAATLIGAVGGVIVVFSIVLLDKLKIDDPVGAISVHGVAGIWGTLVVPITNGDASFG
AQLIGAATIFAWVFVTSLIVWFILKATMGIRVSEEEEYEGLDIAECGMEAYPEF
>gnl|CDD|132684 TIGR03645, glyox_marine, lactoylglutathione lyase family protein. Members of this protein family share homology with lactoylglutathione lyase (glyoxalase I) and are found mainly in marine members of the gammaproteobacteria, including CPS_0532 from Colwellia psychrerythraea 34H. This family excludes a well-separated, more narrowly distributed paralogous family, exemplified by CPS_3492 from C. psychrerythraea. The function is of this protein family is unknown
YPRTFSHIGISVPDLDAAVKFYTEVLGWYLIMPPTEIVEDDSAIGEMCTDVFGEGWGSFKIAHLSTGDRI
GVELFEFKNQENPEDNFEYWKTGVFHFCVQDPDVEGLAERIVAAGGKKRMPVPRYYYPGEKPYRMIYMED
PFGNILEIYSHSYELTYSAGAY
>gnl|CDD|132685 TIGR03646, YtoQ_fam, YtoQ family protein. Members of this family are uncharacterized proteins, including YtoQ from Bacillus subtilis. This family shows some sequence similarity to a family of nucleoside 2-deoxyribosyltransferases (COG3613 as iterated through CDD), but sufficiently remote that PSI-BLAST starting from YtoQ and exploring outwards does not discover the relationship
LTVYLAGEIHTDWREEIKEGAKSKNLPIVFSGPVTDHEASDNIGEDILGKQPSNFWRDDAAASINNIRTR
KLIEKADVVIALFGEKYKQWNAAFDAGYAAALGKPLIILRPEELIHPLKEVDNKAQAVVETPEQAIETLK
YILE
>gnl|CDD|132686 TIGR03647, Na_symport_sm, putative solute:sodium symporter small subunit. Members of this family are highly hydrophobic bacterial proteins of about 90 amino acids in length. Members usually are found immediately upstream (sometimes fused to) a member of the solute:sodium symporter family, and therefore are a putative sodium:solute symporter small subunit. Members tend to be found in aquatic species, especially those from marine or other high salt environments [Transport and binding proteins, Unknown substrate]
AYWRANLRLIAVLLAIWFVVSFGAGILFADELNSFTFFGFPLGFWFAQQGSIYVFVVLIFVYAWRMNRLD
RKYGVDE
>gnl|CDD|274698 TIGR03648, Na_symport_lg, probable sodium:solute symporter, VC_2705 subfamily. This family belongs to a larger family of transporters of the sodium:solute symporter superfamily, TC 2.A.21. Members of this strictly bacterial protein subfamily are found almost invariably immediately downstream from a member of family TIGR03647. Occasionally, the two genes are fused
TYLFVGATFALYIGIGIWSRAGSTSEFYVAGRGVPPVANGMATAADWMSAASFISMAGLIAFLGYDGLAY
LMGWTGGYVLLALLLAPYLRKFGKYTVPDFIGDRYYSNTARLVAVICAIFISFTYVAGQMRGVGVVFSRF
LEVDFETGVFIGMAIVFFYAVLGGMKGVTWTQVAQYIVLIVAYLVPAIFISLKLTGNPVPQLGYGSALSG
VYLLDKLDELEVDLGFAEYTEPFGSKSRINVFALTLALMVGTAGLPHVIVRFYTVPKVRDARWSAGWALF
FIALLYTTAPAVAAFARYNLITTVNGTPYAELPGWVANWEKTGLLKFEDKNGDGILQYSGDAGNELTIDR
DIIVLATPEIAGLPYWVIGLVAAGGLAAALSTAAGLLLVISSAISHDLYYRIINPNASEKQRLLVARIAL
VVAAVIAGYFGLNPPGFIAQVVAFAFGLAAASFFPALVLGIFWKRMNREGAIAGMLTGLGFTFSYIVYFK
PWGFIGTNPGANVPENWWFGISPEGIGLIGMPVNFAVAIVVSLVTPPPPQEIQDLVEDIRYP
>gnl|CDD|274699 TIGR03649, ergot_alkaloid_biosynthetic_protein_A, ergot alkaloid biosynthesis protein, AFUA_2G17970 family. This family consists of fungal proteins of unknown function associated with secondary metabolite biosynthesis, such as of the ergot alkaloids such as ergovaline. Nomenclature differs because gene order differs - this is EasG in Neotyphodium lolii but is designated ergot alkaloid biosynthetic protein A in several other fungi
TILLTGGTGKTASRIARLLQAASVPFLVASRSSSSSAGPNEKHVKFDWLDEDTWDNPFSSDDGMEPEISA
VYLVAPPIPDLAPPMIKFIDFARSKGVRRFVLLSASIIEKGGPAMGQVHAHLDSLGGVEYTVLRPTWFME
NFSEEFHVEAIRKENKIYSATGDGKIPFVSADDIARVAYRALTDKVAPNTDYVVLGPELLTYDDVAEILS
RVLGRKITHVKLTEEELAQRLQSFGMPEDLARMLASLDTAVKNGAEVRLNDVVKAVTGSKPRGFRDFAES
NKALW
>gnl|CDD|132689 TIGR03650, hypothetical_protein_PTD2_19497, violacein biosynthesis enzyme VioE. This enzyme catalyzes the third step in violacein biosynthesis from a pair of Trp residues, as in Chromobacterium violaceum, but the first step that distinguishes that pathway from staurosporine (an indolocarbazole antibiotic) biosynthesis [Cellular processes, Toxin production and resistance]
PPLLPAQWSSAYVSYWMPMQPDDQITSGYCWFDYTRNICRIDGLFNPWSEIKMGNRLWMSEIGYANTDES
FKQKVAYAREDMASGEQLSAQVLDDEIDPFHELFLPQKVLIECGARHMGRETVLGREADKWLFQRPGKGP
STYYLIAGTNHLLRMVTGDPKICASVRDFPNFNTYKIPDEVFKP
>gnl|CDD|274700 TIGR03651, possible_peptide_antibiotic_precursor?, circular bacteriocin, circularin A/uberolysin family. Circular bacteriocins are antibiotic proteins made by ribosomal translation of a precursor molecular, followed by cleavage and circularization. Members of this subclass of the circular bacteriocins include circularin A from Clostridium beijerinckii, bacteriocin AS-48 from Enterococcus faecalis, uberolysin from Streptococcus uberis, and carnocyclin A from Carnobacterium maltaromaticum. The mature circularized peptides average about 70 amino acids in size [Cellular processes, Toxin production and resistance]
AEVAGTLGISTATATTVVNIIDTGSTIVTIISIIAAIVGSGGLSVLLAAGIDAIIATVKKKIKKNGKAAA
IAW
>gnl|CDD|274701 TIGR03652, FeS_repair_RIC, iron-sulfur cluster repair di-iron protein. Members of this protein family, designated variously as YftE, NorA, DrnN, and NipC, are di-iron proteins involved in the repair of iron-sulfur clusters. Previously assigned names reflect pleiotropic effects of damage from NO or other oxidative stress when this protein is mutated. The suggested name now is RIC, for Repair of Iron Centers [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
VGEIVTEIPRAARIFRKYGIDFCCGGNVSLAEACKEKGLDPDEILAELNALQQEPENSGAKDWREAPLSE
LIDHIVDRHHEYLREELPELIPLATKVARVHGDHHPELIGLAELFRELKAELEQHLMKEEQILFPAIIEY
KRGNPAQAIGTPISVMESEHDEAGDLLKELRELTNDYTPPEDACNTWRALYSGLEELEDDLHEHIHLENN
ILFPRA
>gnl|CDD|274702 TIGR03653, uL6_arch, ribosomal protein uL6, archaeal form. Members of this protein family are the archaeal form ofribosomal protein uL6 (previously L9 in yeast and human). The top-scoring proteins not selected by this model are eukaryotic cytosolic uL6. Bacterial ribosomal protein L6 scores lower and is described by a distinct model [Protein synthesis, Ribosomal proteins: synthesis and modification]
REEIEIPEGVSVTIEGNIVTVKGPKGEVTREFWYPGIEISVEDGKVVIETDFARKKDKAMVGTFRSHIKN
MIKGVTEGFEYKMKVVYSHFPMQVKVEGNKVIIENFLGEKAPRRAKILGGVKVKVKGEEVIVEGIDKEDV
GQTAANIEQATRIKGRDPRVFQDGIYIVEK
>gnl|CDD|274703 TIGR03654, L6_bact, ribosomal protein L6, bacterial type [Protein synthesis, Ribosomal proteins: synthesis and modification]
SRIGKKPIAIPAGVEVTIDGNVVTVKGPKGELSRTFHPGVTVKVEDGQITVSRPNDSKEARALHGTTRAL
INNMVIGVSEGFEKKLEIVGVGYRAQLQGKKLNLSLGYSHPVEYEIPEGITVEVPKPTEIVVKGIDKQLV
GQVAAEIRAFRPPEPYKGKGIRYAGEVVRRKEGKK
>gnl|CDD|274704 TIGR03655, hypothetical_protein_VT2-Sap32, restriction alleviation protein, Lar family. Restriction alleviation proteins provide a countermeasure to host cell restriction enzyme defense against foreign DNA such as phage or plasmids. This family consists of homologs to the phage antirestriction protein Lar, and most members belong to phage genomes or prophage regions of bacterial genomes [Mobile and extrachromosomal element functions, Prophage functions, DNA metabolism, Restriction/modification]
LKPCPFCGGADVYLRRGFDPLDLSHYFECSDCGASGPAEEDEAEAIEAWNRRA
>gnl|CDD|274705 TIGR03656, IsdC, heme uptake protein IsdC. Isd proteins are iron-regulated surface proteins found in Bacillus, Staphylococcus and Listeria species and are responsible for heme scavenging from hemoproteins. The IsdC protein consists of an N-terminal hydrophobic signal sequence, a central NEAT (NEAr Transporter, pfam05031) domain, which confers the ability to bind heme, and a C-terminal SrtB processing signal which targets the protein to the cell wall. IsdC is believed to make a direct contact with, and transfer heme to, the heme-binding component (IsdE) of an ABC transporter in the cytoplasmic membrane, and to receive heme from other NEAT-containing heme-binding proteins also localized in the cell wall
MKKILVFAFFTTILAFIILSAGFSNSANLADGTYTINYTVYKADNDSASMANDYFEKPAKLIVKNGKMTV
QITVNHSHWITGFKVEGNGVNVVSKNEAADKRTVEFPVSDLSGPIDGKIHVYVDDKVNYDHHYTIRLKFD
GPTSVAGANAAGKDDKNSAEGSDKGSNGTTTKQSKSESSNKDKVDNPQTGDGTPIYLYAIALLIAGALLI
RKKSKGN
>gnl|CDD|213844 TIGR03657, IsdB, heme uptake protein IsdB. Isd proteins are iron-regulated surface proteins found in Bacillus, Staphylococcus and Listeria species and are responsible for heme scavenging from hemoproteins. The IsdB protein is only observed in Staphylococcus and consists of an N-terminal hydrophobic signal sequence, a pair of tandem NEAT (NEAr Transporter, pfam05031) domains, which confers the ability to bind heme, and a C-terminal sortase processing signal which targets the protein to the cell wall. IsdB is believed to make a direct contact with methemoglobin facilitating transfer of heme to IsdB. The heme is then transferred to other cell wall-bound NEAT domain proteins such as IsdA and IsdC
MNKQQKEFKSFYSIRKSSLGVASVAISTLLLLMSNGEAQAAEETGGTNTEAQPKTEAVASPTTTTEKAPE
AKPVANAVSVSNKEVEAPTSETKEAKEVKEVKAPKETKEVKPAAKADNNTYPILNQELREAIKNPAIKDK
DHSAPNSRPIDFEMKKKDGTQQFYHYASSVKPARVIFTDSKPEIELGLQSGQFWRKFEVYEGDKKLPIKL
VSYDTVKDYAYIRFSVSNGTKAVKIVSSTHFNNKEEKYDYTLMEFAQPIYNSADKFKTEEDYKAEKLLAP
YKKAKTLERQVYELNKIQDKLPEKLKAEYKKKLEETKKALDEQVKSAITEFQNVQPTNEKMTDLQDTKYV
VYESVENNESMMDTFVKHPIKTGMLNGKKYMVMETTNDDYWKDFMVEGQRVRTISKDAKNNTRTIIFPYV
EGKTLYDAIVKVHVKTIDYDGQYHVRIVDKEAFTKANADKTNKKEQQDNSAKKETTPATPSKPTTPPVEK
ESQKQDSQKDDNKQSPSVEKENDASSESGKDKTPATKPAKGEVESSSTTPTKVVSTTQNVAKPTTASSET
TKDVVQTSAGSSEAKDSAPLQKANIKNTNDGHTQSQNNKNTQENKAKSLPQTGEESNKDMTLPLMALLAL
SSIVAFVLPRKRKN
>gnl|CDD|132697 TIGR03658, IsdH_HarA, haptoglobin-binding heme uptake protein HarA. HarA is a heme-binding NEAT-domain (NEAr Transporter, pfam05031) protein which has been shown to bind to the haptoglobin-hemoglobin complex in order to extract heme from it. HarA has also been reported to bind hemoglobin directly. HarA (also known as IsdH) contains three NEAT domains as well as a sortase A C-terminal signal for localization to the cell wall. The heme bound at the third of these NEAT domains has been shown to be transferred to the IsdA protein also localized at the cell wall, presumably through an additional specific protein-protein interaction. Haptoglobin is a hemoglobin carrier protein involved in scavenging hemoglobin in the blood following red blood cell lysis and targetting it to the liver
MNKHHPKLRSFYSIRKSTLGVASVIVSTLFLITSQHQAQAAENTNTSDKISENQNNNATTTQPPKDTNQT
QPATQPANTAKNYPAADESLKDAIKDPALENKEHDIGPREQVNFQLLDKNNETQYYHFFSIKDPADVYYT
KKKAEVELDINTASTWKKFEVYENNQKLPVRLVSYSPVPEDHAYIRFPVSDGTQELKIVSSTQIDDGEET
NYDYTKLVFAKPIYNDPSLVKSDTNDAVVTNDQSSSDASNQTNTNTSNQNTSTINNANNQPQATTNMSQP
AQPKSSANADQASSQPAHETNSNGNTNDKTNESSNQSDVNQQYPPADESLQDAIKNPAIIDKEHTADNWR
PIDFQMKNDKGERQFYHYASTVEPATVIFTKTGPIIELGLKTASTWKKFEVYEGDKKLPVELVSYDSDKD
YAYIRFPVSNGTREVKIVSSIEYGENIHEDYDYTLMVFAQPITNNPDDYVDEETYNLQKLLAPYHKAKTL
ERQVYELEKLQEKLPEKYKAEYKKKLDQTRVELADQVKSAVTEFENVTPTNDQLTDLQEAHFVVFESEEN
SESVMDGFVEHPFYTATLNGQKYVVMKTKDDSYWKDLIVEGKRVTTVSKDPKNNSRTLIFPYIPDKAVYN
AIVKVVVANIGYEGQYHVRIINQDINTKDDDTSQNNTSEPLNVQTGQEGKVADTDVAENSSTATNPKDAS
DKADVIEPESDVVKDADNNIDKDVQHDVDHLSDMSDNNHFDKYDLKEMDTQIAKDTDRNVDKGADNSVGM
SSNVDTDKDSNKNKDKVIQLNHIADKNNHTGKAAKLDVVKQNYNNTDKVTDKKTTEHLPSDIHKTVDKTV
KTKEKAGTPSKENKLSQSKMLPKTGETTSSQSWWGLYALLGMLALFIPKFRKESK
>gnl|CDD|274706 TIGR03659, heme_ABC_transporter_heme-binding_protein_isdE, heme ABC transporter, heme-binding protein isdE. This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron
KKILSLVLLAVLSLGLTGCSSSKEKSKVSNKKSKEERIVATSVAVTEILDKLDLDLVGVPTSQKTLPKRY
KDVPEVGNPMSPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQLGVEATFLNLTSVDGMKKSITELGEKYGR
EEQAEKLVKEINEKEAEVKKKVKGKKKPKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKGNKQEYL
SSNTEYLLKANPDIILRAAHGMPDEVKKMFDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEA
LDELKKILY
>gnl|CDD|132699 TIGR03660, T1SS_rpt_143, T1SS-143 repeat domain. This model represents a domain of about 143 amino acids that may occur singly or in up to 23 tandem repeats in very large proteins in the genus Vibrio, and in related species such as Legionella pneumophila, Photobacterium profundum, Rhodopseudomonas palustris, Shewanella pealeana, and Aeromonas hydrophila. Proteins with these domains represent a subset of a broader set of proteins with a particular signal for type 1 secretion, consisting of several glycine-rich repeats modeled by pfam00353, followed by a C-terminal domain modeled by TIGR03661. Proteins with this domain tend to share several properties with the RtxA (Repeats in Toxin) protein of Vibrio cholerae, including a large size often containing tandemly repeated domains and a C-terminal signal for type 1 secretion [Cellular processes, Pathogenesis]
GQFTVTQGADGVVSYQLDDSTNPVAGLTSGGQAVTLSETSNADGNFTYTATAGGNPVFTLTLNADGSYEF
TLEGPLDHAAGSDELTLNFPIIATDFDGDTSSITLPVTIVDDVPTITDVDALTVDEDDLPGGSDGSK
>gnl|CDD|274707 TIGR03661, T1SS_VCA0849, type I secretion C-terminal target domain (VC_A0849 subclass). This model represents a C-terminal domain associated with secretion by type 1 secretion systems (T1SS). Members of this subclass do not include the RtxA toxin of Vibrio cholerae and its homologs, although the two classes of proteins share large size, occurrence in genomes with T1SS, regions with long tandem repeats, and regions with the glycine-rich repeat modeled by pfam00353 [Cellular processes, Pathogenesis]
DTITDFTLGEDKLDLSDLLSGEGVSSANLDQYLNVTTSGEDGNTVISVDSDGSAGSAAVTQTITLEGVDL
SSTSADIINQLLDNNQLI
>gnl|CDD|274708 TIGR03662, Chlor_Arch_YYY, Chlor_Arch_YYY domain. Members of this highly hydrophobic probable integral membrane family belong to two classes. In one, a single copy of the region covered by this model represents essentially the full length of a strongly hydrophobic protein of about 700 to 900 residues (variable because of long inserts in some). The domain architecture of the other class consists of an additional N-terminal region, two copies of the region represented by this model, and three to four repeats of TPR, or tetratricopeptide repeat. The unusual species range includes several Archaea, several Chloroflexi, and Clostridium phytofermentans. An unusual motif YYYxG is present, and we suggest the name Chlor_Arch_YYY protein. The function is unknown
VIAWLITILALGITIYPLIGPLFPRLHDRGYAFARPLGLLLLGYVAWLLGSLGLLRFTSPGILIGLLVLL
GVGLFLWRKQGTLPRRKSLLRGELVFLAAFLFMLIVRAFNPDIWGGEKFMDFGFLNAILRSPSFPPLDPW
FAGGSINYYYFGHLLMAVLGKLSGVAPAFGYNLALATLFALLATGAYGLGYNLLRTRLLPRRIRAGLTAA
LFVGLLGNLWLIPSGLLGAQIFNLIYSWLELAGGGEEFSYWDSSRVIPYTINEFPLFSFLLGDLHAHMIA
IPFTLLALALALAWWLRPKGEQRPRWLILLLLALVLGLLAVTNSWDFPIYAGLAGLVVFAAYGRPYRAPG
NGWLREAVILALGQAVLVPVLSLLLYAPFYLSFWQGPASGRGIGLVETRTTIHQFLIIHGLFLFLFISFL
ITGLTGDSRRKKARWILLAPFIALLLGLSLGIPLLALLLPLLVTTWLLRRRDAPVGFETLLALGGLGLLL
LVEIIYVRDNIGGDYYRMNTVFKFYMQAWILLGLAAAVILGWLLRAYRGRRKRQFLRKGWAAICAILLLL
AGIYPVVAVPTRIRDGEAGPTLDGMAYLEESHPEDAAAIRWLRQNIDGTPVILEAAGDSYTYASRVSAAT
GLPTVIGWAGHEWQWRGGVDETEVGERVDDVETIYTSGDPTEARELLERYGVDYVYVGPLERQRYGLSTD
ALEDLGDLEPVFEQGSVVIYQVR
>gnl|CDD|274709 TIGR03663, TIGR03663, TIGR03663 family protein. Members of this protein family, uncommon and rather sporadically distributed, are found almost always in the same genomes as members of family TIGR03662, and frequently as a nearby gene. Members show some N-terminal sequence similarity with pfam02366, dolichyl-phosphate-mannose-protein mannosyltransferase. The few invariant residues in this family, found toward the N-terminus, include a dipeptide DE, a tripeptide HGP, and two different Arg residues. Up to three members may be found in a genome. The function is unknown
TLLVILIVLFALLLRLFELGLRVFHHDEAIHASFILKLLETGVYSYDPAYHGPFLYHITAAVFHLFGISD
ATARLLPAVFGVLLPLTAWLYRKRLGDNEVLWAAVLLAFSPVMVYYSRFMRNDIFVAFFTLLAVGAAFRY
LDTGKRRYLFLAASALALAFTSKENAYLIILIFGGLLAIYLDWKKERAGARETLTRKRSLFWRWLRDLIG
SVAVFAAIIMFFYTSLFRHPERLFSIVEAGTIKAVEHWASMHRIARIYGPFYYYLPILLLYELPALIFAA
AGVLGFLANRYATDKRRSFFLFACYWTLASLLFYSYIQEKVPWLVVHILVPLAILAAVGLSAVVLTGKKA
IAAGDTVAVILALTLLFSAAAGIHVNYYTPVDPDEPLVYAQPSEDIRPLMEKIDAFATSTEGLDVYVIGP
VNLYWPLPWYLRDYNATAT
>gnl|CDD|274710 TIGR03664, purine_and_other_phosphorylases_family_1_protein, futalosine hydrolase. This enzyme catalyzes the conversion of futalosine to de-hypoxanthine futalosine in a pathway for the biosynthesis of menaquinone distinct from the pathway observed in E. coli
ILIVTAVTAEASALLRGLGGRYAGSVGGAGFDVLVTGVGPVNAAAATARLLARAPYELVINAGIAGGFPG
KAAVGDLVVADSEIAADLGAETPEGFLPLEALGFPQLPGGGRSYFNRIPLDPDLVERAVQLARALGLPVA
RGPFLTVSTVSGTAARAEALARRFGAVAENMEGAAVALAALRYGVPFLELRGISNLVGPRDRSRWRIKEA
LAALQRAAAKLL
>gnl|CDD|274711 TIGR03665, KH_domain-containing_protein_MJ0443, arCOG04150 universal archaeal KH domain protein. This family of proteins is universal among the 41 archaeal genomes analyzed, and is not observed outside of the archaea. The proteins contain a single KH domain (pfam00013) which is likely to confer the ability to bind RNA
YVKIPKDRIGVLIGKGGETKKEIEERTGVKLDIDSETGEVKIEPEDEDPLAVMKAREVVKAIGRGFSPEK
ALKLLDDDYMLEVIDLKEYGKSPNALRRIKGRIIGEGGKTRRIIEELTGVSISVYGKTVGIIGDPEQVQI
AREAIEMLIEGAPHGTVYKFLERKRRELKRRR
>gnl|CDD|274712 TIGR03666, Rv2061_F420, PPOX class probable F420-dependent enzyme, Rv2061 family. A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomycetales, make F420. A variant of the Partial Phylogenetic Profiling algorithm, SIMBAL, shows that this protein likely binds F420 in a cleft similar to that in which the homologous enzyme pyridoxamine phosphate oxidase (PPOX) binds FMN [Unknown function, Enzymes of unknown specificity]
PMTPTFADLARARYALLTTFRKDGTPVPTPVWAAVDGDKLLVRTKEDSWKVKRIRNNPRVTLAPCDRRGR
PTGPVVPGRARILDGAETARARDLLARRYGLQGRLFPLFSKLRRGRDRNVGLELTPAGDTPG
>gnl|CDD|132706 TIGR03667, Rv3369, PPOX class probable F420-dependent enzyme, Rv3369 family. A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomycetales, make F420. A variant of the Partial Phylogenetic Profiling algorithm, SIMBAL, shows that this protein likely binds F420 in a cleft similar to that in which the homologous enzyme pyridoxamine phosphate oxidase (PPOX) binds FMN [Unknown function, Enzymes of unknown specificity]
TEFTAKVARRLREESIVWLTTVRRSGQPQPVPVWFLWDGTEFLIYSRPQAAKLRNIRRNPRVSLHLNSDG
RGGDVVVFTGTAEVVADAPPAREIPAYLAKYREDAARIGMTPERFAADYSVPLRVTPERL
>gnl|CDD|132707 TIGR03668, Rv0121_F420, PPOX class probable F420-dependent enzyme, Rv0121 family. A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomycetales, make F420. A variant of the Partial Phylogenetic Profiling algorithm, SIMBAL, shows that this protein likely binds F420 in a cleft similar to that in which the homologous enzyme pyridoxamine phosphate oxidase (PPOX) binds FMN [Unknown function, Enzymes of unknown specificity]
LEFEARTRFAQARVARLATVSPDGEPHLVPVVFAVGAGAVAAGDAVIYTAVDAKPKTTPRLRRLRNIEEN
PRVSLLVDRYDDDWTRLWWVRADGRAEILRPGEEEHAAAVRLLRAKYHQYQAVPLEGPVIAIRVERWASW
G
>gnl|CDD|132708 TIGR03669, urea_ABC_arch, urea ABC transporter, substrate-binding protein, archaeal type. Members of this protein family are identified as the substrate-binding protein of a urea ABC transport system by similarity to a known urea transporter from Corynebacterium glutamicum, operon structure, proximity of its operons to urease (urea-utilization protein) operons, and by Partial Phylogenetic Profiling vs. urea utilization [Transport and binding proteins, Amino acids, peptides and amines]
IKLGVLEDRSGNFALVGTPKWHASQLAIEEINKSGGILGRQIELIDPDPQSDNERYQELTRRLLNRDKVD
ALWAGYSSATREAIRPIIDRNEQLYFYTNQYEGGVCDEYTFAVGATARQQLGTVVPYMVEEYGKKIYTIA
ADYNFGQLSADWVRVIAKENGAEVVGEEFIPLSVSQFSSTIQNIQKADPDFVMSMLVGANHASFYEQAAS
ANLNLPMGTSTAMAQGYEHKRFEPPALKDVYAGVNYMEEIDTPENEAFVERFYAKFPDAPYINQEAENNY
FSVYMYKQAVEEAGTTDQDAVRDVLESGVEMDAPEGKVCIDGATHHMSHTMRLARADADHNITFVKEQEI
IPYFLSETVGCDLTKKDDTTQYTP
>gnl|CDD|274713 TIGR03670, DNA-directed_RNA_polymerase_subunit_B', DNA-directed RNA polymerase subunit B. This model represents the archaeal version of DNA-directed RNA polymerase subunit B (rpoB) and is observed in all archaeal genomes
VYLNGRLIGYHDDPEELVEEVRKLRRSGKLSQEVNVAYYEETNEVYINCDAGRIRRPLIVVENGKPKLTR
EHVEKLKEGELTWDDLVKQGVIEYLDAEEEENAYIALDPEELTPEHTHLEIDPSAILGIIASTIPYPEHN
QSPRNTMGAAMAKQSLGLYAANYRIRLDTRGHLLHYPQKPLVKTRVLELIGYDDRPAGQNFVVAVMSYEG
YNIEDALIMNKASIERGLARSTFFRTYEAEERRYPGGQEDRFEIPEPDVRGYRGEEAYKHLDEDGIVYPE
VEVKGGDVLIGKTSPPRFLEELREFGLVTERRRDTSVTVRHGEKGIVDKVIITETEEGNKLVKVRVRDLR
IPELGDKFASRHGQKGVIGMIVPQEDMPFTEDGIVPDLIINPHAIPSRMTVGQLLEMIAGKVAALEGRRV
DGTPFEGEPEEELRKELLKLGFKPDGKEVMYDGITGEKLEAEIFIGVIYYQKLHHMVADKIHARSRGPVQ
VLTRQPTEGRAREGGLRFGEMERDVLIGHGAAMLLKERLLDESDKYVVYVCENCGHIAWEDKRKGTAYCP
VCGETGDISPVEMSYAFKLLLDELKSLGISPRLELGDKV
>gnl|CDD|274714 TIGR03671, CCA-adding_enzyme, CCA-adding enzyme
VLEEVLERIKPTEEEREKLKKVADELIARLEEIIEELGVDAEVVLVGSYARGTWLKGDRDIDIFILFPKD
TSREELEEYGLEIGHEVLKRLGNYEERYAEHPYVSGEIEGFEVDVVPCYKVESGEEIISAVDRTPFHTRY
VLERLDGKQRDDVRLLKQFLKGIGVYGSELKTRGFSGYLCELLVIHYGSFENVLKAASKWKPPVVIDIEE
HGAKKFDDPLVVIDPVDPKRNVAAALSLENLARFILAARMFLKNPSLEFFFPPPLEAEEVLERLERRGTT
LLAIVFRTPDVVDDILYPQLERSGRSLVKLLEREGFEVLRYGVWADENTCYLLLELESAELPRVKLHVGP
PVWVRDHAEKFIEKYEDVDGVPFIEGDRLYVEKPRKYTTAEDLLRDELSKGDVSLGKN
>gnl|CDD|274715 TIGR03672, 50S_ribosomal_protein_L4, 50S ribosomal protein uL4, archaeal form. One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome
MKAKVYDLDGEVVGEIELPAVFEEPVRPDLIKRAVLAAQTNRLQPYGRDPYAGKRTSAESWGSGRGIARV
PRLKGGSRAARVPQAVGGRRAHPPKVEKDLHEKINKKERRLAIRSAIAATADPDLVKARGHVFEGDELPI
VVVDDFEKLKKTKEVRELLEALGVYDDIERAKEGKKIRAGKGKMRGRRYKEPKSVLIVVGDNSGISKAAR
NLPGVDVVTVNNLNVEHLAPGGHPGRLTVWTESAIEKLEER
>gnl|CDD|274716 TIGR03673, 50S_ribosomal_protein_L14, 50S ribosomal protein uL14, archaeal form. Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L24e, part of which may contact the 16S rRNA in 2 intersubunit bridges
KGIRAGITRALPVGALLVCADNTGAKEVEVISVKGYKGVKRRLPSAGVGDMVVVSVKKGTPEMRKQVFRA
VVVRQRKEYRRPDGTRVKFEDNAAVIVTPDGEPKGTEIKGPVAREAAERWPKIASIASIIV
>gnl|CDD|274717 TIGR03674, Flap_endonuclease_1, flap structure-specific endonuclease. Endonuclease that cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Has 5'-endo-/exonuclease and 5'-pseudo-Y-endonuclease activities. Cleaves the junction between single and double-stranded regions of flap DNA
MGVDLRDLLAKEEIELEDLSGKVVAVDAFNALYQFLSSIRQPDGTPLMDSRGRITSHLSGLFYRTINLLE
NGIKPVYVFDGKPPELKAETLEERREIREEAEEKWEEALEKGDLEEARKYAQRSSRLTSEIVESSKKLLD
LMGIPYVQAPSEGEAQAAYMAKKGDVDYVGSQDYDSLLFGAPRLVRNLTISGKRKLPGKNIYVEVKPELI
ELEEVLSELGITREQLIDIAILVGTDYNEGVKGIGPKTALKLIKEHGDLEKVLKARGEDIENYDEIREFF
LNPPVTDDYELEWRKPDKEGIIEFLCDEHDFSEDRVERALERLEAAYKSKQKTLDRWF
>gnl|CDD|274718 TIGR03675, Uncharacterized_protein_MJ1236, arCOG00543 universal archaeal KH-domain/beta-lactamase-domain protein. This family of proteins is universal in the archaea and consistsof an N-terminal type-1 KH-domain (pfam00013) a central beta-lactamase-domain (pfam00753) with a C-terminal motif associated with RNA metabolism (pfam07521). KH-domains are associated with RNA-binding, so taken together, this protein is a likely metal-dependent RNAase. This family was defined as arCOG01782
LKEIKEIINKLLPKGVKITDVEFEGPELVIYTKNPELFAKDGDLVKELAKKLRKRIVIRPDPSVLLPPEE
AIKKIKEIVPEEAGITDIYFDDVTGEVIIEAEKPGLVIGKGGSTLREITKETGWTPKVVRTPPIESRTIK
NIREYLRSESKERKEFLRKLGRRIHRDPIFKDRWVRVTALGGFREVGRSALLLSTPESRILLDCGVNVGA
DGDNAYPYLDVPEFDLDELDAVVITHAHLDHSGLVPLLFKYGYDGPVYCTPPTRDLMVLLQLDYIDVAQK
EGKKPPYSSKDVREALKHTITLDYGEVTDIAPDIKLTFYNAGHILGSAIAHLHIGDGLYNIVYTGDFKYE
KTRLLDPAVNKFPRVETLIMESTYGGRDDYQPSREEAEKELIKVVNETIKRGGKVLIPVFAVGRAQEVML
VLEEAMRKGLIPEVPVYLDGMIWEATAIHTAYPEYLNKELRERIFHEGENPFLSEIFVRVEGSDERREII
ESDEPAIILATSGMLNGGPVVEYLKLLAPDPRNSLVFVGYQAEGTLGRRIQSGWREIPLTDDGKTETIKI
NMEVETVDGFSGHSDRRQLMNYVRRMQPKPEKIILNHGEPSKCLDLASSIYKKFKIETYAPKNLETIRLL
>gnl|CDD|274719 TIGR03676, Peptide_chain_release_factor_subunit_1, peptide chain release factor 1, archaeal and eukaryotic forms. Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. This model identifies both archaeal (aRF1) and eukaryotic (eRF1) of the protein. Also known as translation termination factor 1 [Protein synthesis, Translation factors]
EKYEFKKLLEELKKKKGRGTELISLYIPPDKQISDVVKQLRDEYSQAANIKSKQTRKNVQSAIESIMQRL
KLYKKPPENGLVLFCGMVPTGGGKEKMETYVIEPPEPINTYLYRCDSKFYLEPLEEMLEEKDVYGLIVLD
RREATIGLLKGKRIEVLKELTSGVPGKHRAGGQSARRFERLIEIAAHEFYKRVGEAANEAFLPLKDKKLK
GIIIGGPGPTKEEFAEGDYLHYELKKKIIGLVDVSYTGESGLRELVEKAEDALKDLEYMKEKKLMERFFK
ELAKDTGLAAYGEDEVRKALEMGAVDTLLISEDLRKIRVTFKCPNCGYEEEKTVKPEEGDKSGTCPKCGS
QLEIVEEEDIIEELSELAEESGAKVEIISTDTEEGEQLLKAFGGIAAILRYRV
>gnl|CDD|188367 TIGR03677, eL8_ribo, ribosomal protein eL8, archaeal form. This model specifically identifies the archaeal version of the large ribosomal complex protein eL8, previously designated L8 in yeast and L7Ae in the archaea. The family is a narrower version of the pfam01248 model which also recognizes the L30 protein
YVKFEVPEELADKALEAVEKARETGKIKKGTNEVTKAVERGIAKLVVIAEDVEPPEIVAHLPALCEEKGI
PYIYVKSKEDLGAAAGLEVGAASAAIVDAGKAEELLKEIIEKVEALK
>gnl|CDD|163391 TIGR03678, microcyclamide_precursor_protein, bacteriocin leader peptide, microcyclamide/patellamide family. This model represents a conserved N-terminal region shared by microcyclamide and patellamide bacteriocins precursors. These bacteriocin precursors are associated with heterocyclization. Related precursors are found in family TIGR04446
MDKKNILPQQGQPVIRLTAGKLPSQLAELSEEAL
>gnl|CDD|188368 TIGR03679, arCOG00187, arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein. This protein consists of an N-terminal possible metal-binding domain (pfam04068) followed by a 4Fe-4S cluster binding domain (pfam00037) followed by a C-terminal ABC transporter, ATP-binding domain (pfam00005). This combination of N-terminal domains is observed in the RNase L inhibitor, RLI. This model has the same scope as an archaeal COG (arCOG00187) and is found in all completely sequenced archaea and does not recognize any known non-archaeal genes
AALYSGGKDSNYALYKALEEGHEVTCLITVVPENEDSYMFHTPNIELTRLQAEALGIPLVEIETSGEKEK
EVEDLKGALKELKEEGVEGIVTGAIASEYQKSRIERICEELGLKVFAPLWGRDPEEYLRELVERGFRFII
VSVSAYGLDESWLGREIDEKYIEELKALNKRYGINPAGEGGEYETLVLDAPLFKRRIEIVEYEKKWSGGG
GYLIIERA
>gnl|CDD|274720 TIGR03680, eif2g_arch, translation initiation factor 2 subunit gamma. This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA
RQPEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELKRGISIRLGYADAEIYKCPECDGPECYTTEPVCP
NCGSETELLRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPCPQPQTKEHLMALEIIGIKNIVIV
QNKIDLVSKEKALENYEEIKEFVKGTVAENAPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYV
ARSFDVNKPGTPPEKLKGGVIGGSLIQGKLKVGDEIEIRPGIKVEKGGKTKWEPIYTEITSLRAGGYKVE
EARPGGLVGVGTKLDPALTKADALAGQVVGKPGTLPPVWESLELEVHLLERVVGTEEELKVEPIKTGEVL
MLNVGTATTVGVVTSARKDEIEVKLKRPVCAEEGDRVAISRRVGGRWRLIGYGIIK
>gnl|CDD|274721 TIGR03682, arCOG04112, diphthamide biosynthesis enzyme Dph2. Members of this family are the archaeal protein Dph2, members of the universal archaeal protein family designated arCOG04112. The chemical function of this protein is analogous to the radical SAM family (pfam04055), although the sequence is not homologous. The chemistry involves [4Fe-4S]-aided formation of a 3-amino-3-carboxypropyl radical rather than the canonical 5'-deoxyadenosyl radical of the radical SAM family
NAKKVLLQAPEGLKRRAFEIAQKLEEKGYEVIISGEPCYGACDLADDEARELVDLIVHFGHSPLPNVKYE
IPVIFIEARSDVDVEEVIEKALENLKGKRIGLTTTIQHVHKLDKVKEILEERGIEVVIGKGDGRVTYPGQ
VLGCNFSAAKSVEADAFLFVGTGLFHPLGLALATNKPVYAADPFSGKVKDIEAEIDKFLRVRYARISKAL
DAKKFGILVSTKKGQRRLELAEELKKLLEELGKEAILILLDNISPDYLRNLRFDAYVNTACPRIAIDDYA
RFKKPVLTPQEFEIVLGKRSWYVFDEIL
>gnl|CDD|274722 TIGR03683, A-tRNA_syn_arch, alanyl-tRNA synthetase. This family of alanyl-tRNA synthetases is limited to the archaea, and is a subset of those sequences identified by the model pfam07973 covering the second additional domain (SAD) of alanyl and threonyl tRNA synthetases
EDEYQLKFFKENGFVRKQCQVCGSYFWTLDPERETCGDAPCDEYSFIGNPIFSKKYTLDEMREAFLSFFE
KHGHTRIKRYPVVARWRDDVYLTIASIADFQPWVTSGLVPPPANPLVISQPCIRLNDIDNVGRTGRHLTC
FEMMAHHAFNYPDKEIYWKDETVEYCFEFLEELGIDPEEITYKESPWEGGGNAGPCFEVIVGGLELATLV
FMQYEEDKEGEIEIKGGRYSEMPLKIVDTGYGLERFVWASQGTPTAYDAIFPEIVDKLKENAGVELIDEE
ILAENARLAGMMDIEDEEDLRELRKKVADKIGIDVEELEKIIAPVERIYAIADHTRCLAFMLGDGIVPSN
VKEGYLARLVIRRTLRLMRELGLDIPLSDLVEMQLEELKKIYPELKENKDYILDILDLEEEKYRETLERG
RRIVERLLKTKKEIPLDDLIELYDSHGIPPEIVKEIAAELGAEVEIPDNFYSIVAERHEKEEKEEESPKD
YEERAKDLPETRRLFYEDPTMREFEAKVLGVFDNYVVLDQTAFYPEGGGQPADTGYLITNGGEYRVVDVQ
KVGGVIVHKVDGEGIKEGDEVKGEIDWERRLRLMRHHTATHVLLAAARRVLGRHVWQAGAQKDTDKARLD
ITHYKRISEEEIKEIERLANRIVMENRPVSVKWMDRNEAEQKYGFRLYQGGVPPGREIRVVEIEDWDVQA
CGGTHCRNTGEIGPIKILKTERIQDGVERIEFAAGEAALEYIQELEDLLRESSDILKVPPEQLPETVKRF
FEEWKEQRKEIERLKKKLAELKIYELISEAERIGGVEVIVELVDADMDELQEIAEKLAEKGLVVVLVSGG
GGNGRVVISSGEKAGVDAGELVREIAKELGGGGGGKPDLAQGGGPDDLNVDEALEKIKSFLR
>gnl|CDD|274723 TIGR03684, arCOG00985, arCOG04150 universal archaeal PUA-domain protein. This universal archaeal protein contains a domain possibly associated with RNA binding (pfam01472, TIGR00451)
RHFLSKKEIKELLEELKEYYGIDIEKAKLEVAETDKFEIYLVDGKPLLFEVDGRLFPTLYGLLELNPDKN
VVVVDEGAVKFIINGADIMAPGIVEADPSIKEGDIVFVVDETHGKPLAVGIALMDAEEMVEEKKGKAVKN
IHHVGDKIWE
>gnl|CDD|274724 TIGR03685, ribo_P1_arch, 50S ribosomal protein P1. This model represents P1 the L12P protein of the large (50S) subunit of the archaeal ribosome
MEYIYAALLLHSAGKEINEENLKAVLEAAGVEVDEARVKALVAALEGVNIEEAIKKAAAAPVAAAAAAAA
AAAAAEEEEEEEEEEEEEKEESEEEAMAGLGALFG
>gnl|CDD|274725 TIGR03686, pupylate_PafA, Pup--protein ligase. Members of this family are the Pup--protein ligase PafA (proteasome accessory factor A), a protein shown to regulate steady-state levels of certain proteasome targets in Mycobacterium tuberculosis. Iyer, et al (2008) first suggested that PafA is the ligase for Pup, a ubiquitin analog attached to an epsilon-amino group of a Lys side-chain to direct the target to the proteasome [Protein fate, Degradation of proteins, peptides, and glycopeptides]
RRIFGVETEYGITCTTGGSRRLDPDEVARYLFRPVVSWGRSSNVFLRNGSRLYLDVGSHPEYATAECDSL
RQLIAHDRAGELILNDLADEAEARLAEEGIGGRVYLFKNNTDSAGNSYGCHENYLVRRRGEFKRLARQLL
PFLVTRQLICGAGKVTQTPPGAPDGYCFSQRADHIWEGVSSATTRSRPIINTRDEPHADAERYRRLHVIV
GDSNMSETTTALKVGSTDLVLEMIEAGVGLRDLELANPIRAIREISRDLTGRAPVRLANGRTASALEIQR
EYYERVRAFLATRGDPNAEIERVLDLWGRTLDAIESGDFSAVDTEIDWAIKKKLLDRYQRRHDLDLTDPR
LAQLDLAYHDIAPGRGLFYLLQARGLARRLVTDETIEQAVDQPPQTTRAALRGRFVKAAQELGRDFTVDW
VHLKLNDPAPQTVLLKDPFRAVDERVDALIESM
>gnl|CDD|200311 TIGR03687, pupylate_cterm, ubiquitin-like protein Pup. Members of this protein family are Pup, a small protein whose ligation to target proteins steers them toward degradation. This protein family occurs in a number of bacteria, especially Actinobacteria such as Mycobacterium tuberculosis, that possess an archeal-type proteasome. All members of this protein family known during model construction end with the C-terminal motif [FY][VI]QKGG[QE]. Ligation is thought to occur between the C-terminal COOH of Pup and an epsilon-amino group of a Lys on the target protein. The N-terminal half of this protein is poorly conserved and not represented in the seed alignment [Protein fate, Degradation of proteins, peptides, and glycopeptides]
LTEGVDDLLDEIDDVLETNAEEFVRGFVQKGGQ
>gnl|CDD|274726 TIGR03688, pupylate_PafA2, proteasome accessory factor PafA2. This protein family is paralogous to (and distinct from) the PafA (proteasome accessory factor) first described in Mycobacterium tuberculosis (see TIGR03686). Members of both this family and TIGR03686 itself tend to cluster with each other, with the ubiquitin analog Pup (TIGR03687) associated with targeting to the proteasome, and with proteasome subunits themselves [Protein fate, Degradation of proteins, peptides, and glycopeptides]
RRIMGTETEYGISTPSDPNANPILTSTQAVVAYAAGAGEHRAKRARWDYEEESPLRDARGFDLRRYAARA
PVVDPHALGVANVILTNGARFYVDHAHPEYSSPEVTNPRDAVLYDKAGDRIMAAAAEHAASVPGAPPLKL
YKNNVDGKGASYGSHENYLMARETPFDDIVRALTPFFVTRQVVIGAGRVGIGQQGEEPGFQISQRADYIE
VEVGLETTLNRGIINTRDEPHADADKYRRLHVIIGDANMSETSNYLKLGTTSLVLDAIEAGFDFSDLALA
NPVAAVHAVSHDLTLTHLLRLADGRELTALELQREYRDRVAKLVEDRDGDPDTTDVLALWEEILDLLEND
PMSTADRLDWTAKLQLLEGFRRRDGLSWDDPRLKLVDLQYADIDPAKSLYHALVRKGRMKRLVSAEDIAR
AATTPPEDTRAYFRGRLLARFGDDVAAASWDSVIVDTPRDSLVRVPTLEPLRGTKAHVGTLLDSA
>gnl|CDD|200312 TIGR03689, pup_AAA, proteasome ATPase. In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity [Protein fate, Degradation of proteins, peptides, and glycopeptides]
EDLRELQAQNSSLAARNAKLAEALKAARDELAELKEQLDALAQPPSTYGTLLQVATDDRTAEVFTAGRRM
RVGVSPNVDAAELVPGQTVRLNEALQVVEACDFERTGEIVTLKEVLDDGRALVTDRSGEERVVKLAGALA
DEGLRPGDTLLVDPRAGYAFEAIPRTEVEDLVLEEVPDVTYADIGGLGSQIEQIRDAVELPFLHPELYRE
YGLKPPKGVLLYGPPGCGKTLIAKAVANSLAARIGAEGGGKSYFLNIKGPELLNKYVGETERQIRLIFQR
AREKASEGRPVIVFFDEMDSLFRTRGSGVSSDVETTVVPQLLAEIDGVESLDNVIVIGASNREDMIDPAI
LRPGRLDVKIRIERPDAEAAADIFAKYLTDDLPLPEDLAAHDGDREATAAALIQRVVDALYARSEANRYV
EVTYANGSTEVLYFADFVSGAMLANIVDRAKKRAIKDHITGGQVGLRAEHLLAAVEDEFRENEDLPNTTN
PDDWARISGRKGERIVYIRTLV
>gnl|CDD|163402 TIGR03690, 20S_bact_beta, proteasome, beta subunit, bacterial type. Members of this family are the beta subunit of the 20S proteasome as found in Actinobacteria such as Mycobacterium, Rhodococcus, and Streptomyces. In Streptomyces, maturation during proteasome assembly was shown to remove a 53-amino acid propeptide. Most of the length of the propeptide is not included in this model [Protein fate, Degradation of proteins, peptides, and glycopeptides]
HGTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAGLAIELVRLFQVELEHYEK
IEGVPLTLDGKANRLAAMVRGNLPAAMQGLAVVPLLAGYDLDAGAGRIFSYDVTGGRYEERGYHAVGSGS
VFAKGALKKLYSPDLDEDDALRVAVEALYDAADDDSATGGPDLVRGIYPTVVVITADGARRVPESELEEL
ARAIVESRA
>gnl|CDD|163403 TIGR03691, 20S_bact_alpha, proteasome, alpha subunit, bacterial type. Members of this family are the alpha subunit of the 20S proteasome as found in Actinobacteria such as Mycobacterium, Rhodococcus, and Streptomyces. In most Actinobacteria (an exception is Propionibacterium acnes), the proteasome is accompanied by a system of tagging proteins for degradation with Pup [Protein fate, Degradation of proteins, peptides, and glycopeptides]
MTMPFYVSPEQIMRDRAELARKGIARGRSVVVLTYADGILFVAENPSRSLHKISELYDRIGFAAVGKYNE
FENLRRAGIRYADMRGYSYDRRDVTGRGLANAYAQTLGTIFTEQQKPYEVEICVAEVGETPDQDQLYRIT
FDGSIVDERGFVVMGGTTEPIATALKESYRDGLSLADALGLAVQALRAGGNGEKRELDAASLEVAVLDRS
RPRRAFRRITGEALERLL
>gnl|CDD|274727 TIGR03692, ATP_dep_HslV, ATP-dependent protease HslVU, peptidase subunit. The ATP-dependent protease HslVU, a complex of hexameric HslU active as a protein-unfolding ATPase and dodecameric HslV, the catalytic threonine protease [Protein fate, Degradation of proteins, peptides, and glycopeptides]
TTILAVRRNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYQGN
LTRAAVELAKDWRTDRYLRRLEAMLIVADKETSLLISGTGDVIEPDDGIAAIGSGGNYALAAARALLRNT
DLSAEEIAREALKIAADICIYTNHNITVEEL
>gnl|CDD|163405 TIGR03693, ocin_ThiF_like, putative thiazole-containing bacteriocin maturation protein. Members of this protein family are found in a three-gene operon in Bacillus anthracis and related Bacillus species, where the other two genes are clearly identified with maturation of a putative thiazole-containing bacteriocin precursor. While there is no detectable pairwise sequence similarity between members of this family and the proposed cyclodehydratases such as SagC of Streptococcus pyogenes (see family TIGR03603), both families show similarity through PSI-BLAST to ThiF, a protein involved in biosynthesis of the thiazole moiety for thiamine biosynthesis. This family, therefore, may contribute to cyclodehydratase function in heterocycle-containing bacteriocin biosyntheses. In Bacillus licheniformis ATCC 14580, the bacteriocin precursor gene is adjacent to the gene for this protein [Cellular processes, Toxin production and resistance]
MSHLPAHAKLKANKDTFFLPDPNGGAYFRNNAGSFRLDGDGIANWFEKLLPMFNGEHSLADITDGLPAPY
QKRVFEIGEILYKNGFVRDVSQDAPHELESALLDRYAAQIEFIEADADSGALKFELSRNAKILAAGSGDF
LTKLVRSLIDSGFPRFHAIVTDAEEHALDRIHELAEIAEETDDALLVQEIDFAEDQHLHEAFEPADWVLY
VSDNGDIDDLHALHAFCKEEGKGFIPAICLKQVGLAGPVFQQHGDECFEAAWHRLHESALHEENSLAAFP
LAGKAMLANIIVFELFKAAADDEHLEKKNQFFLLDLATLEGGWHAFIKHPDASCEKDSADLICDLEAKLE
EHPGKETESDLFQCFDELTSKETGIFHLWDEKDLHQLPLAQCFIQTADPLSDGPAELLPEITCSGLTHNE
ARREAGLTGIEMYAAEILHRLIPEHGDFAIAAGETLAEGVLRALEKCLEHKLCERIKHGKEEISLVDLDD
IEDKHCAFYLDALATIHEAPEIALGEEIEGFPVAWAGINDRWYGASGINITLALRKALELALLHIQNDED
PLKANILPESADILLDPDEFKLAIPAEAAIPSTKSLLLALKHLEEHHFYPFVFDLAIEPFLKEKLAGIYC
VLIAKED
>gnl|CDD|274728 TIGR03694, exosort_acyl, N-acyl amino acid synthase, PEP-CTERM/exosortase system-associated. Members of this protein family are restricted to bacterial species with the PEP-CTERM/exosortase system predicted to act in exopolysaccharide-associated protein targeting. PSI-BLAST and CDD reveal relationships to the acyltransferase family that includes N-acyl-L-homoserine lactone synthetase, and recent work shows long-chain N-acyl amino acid biosynthesis activity. Several members of this family may be found in a single genome. These acyltransferases may produce a quorum signalling molecule or may contribute to chemical modifications in exopolysaccharide and biofilm structural material production
ADHFNKYFEIIPAVTPELLEEAFRLRYQVYCEELGFEPPSDYPDGLETDEYDAHSVHSLLRHRRTGTFVG
CVRLVLPNSSDPDQPFPFEKHCSHSLDGLFLDPRRLPRSRIAEVSRLAVSKDFRRRKGEKLKPSGVGVIE
TEAPFSESERRRFPHIPLGLYLGLIALSSANGITHWYAIMEPRLARLLSRFGIQFRQVGPPVDYHGLRAP
YYLELEELLARLEQEFPDLWELITNDGRALL
>gnl|CDD|274729 TIGR03695, menH_SHCHC, 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase. This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAQLLLATLLDQLGI
EPFFLVGYSMGGRIALYYALQYPERVQGLILESGSPGLQTEEERAARRQNDEQLAQRFEQEGLEAFLDDW
YQQPLFASQKNLPPEQRQALRAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFV
QIAKEMQKLIPNLTLHIIPNAGHNIHLENPEAFAKILLAFLE
>gnl|CDD|274730 TIGR03696, tRNA_nuclease_WapA, RHS repeat-associated core domain. This model represents a conserved unique core sequence shared by large numbers of proteins. It is occasional in the Archaea Methanosarcina barkeri) but common in bacteria and eukaryotes. Most fall into two large classes. One class consists of long proteins in which two classes of repeats are abundant: an FG-GAP repeat (pfam01839) class, and an RHS repeat (pfam05593) or YD repeat (TIGR01643). This class includes secreted bacterial insecticidal toxins and intercellular signalling proteins such as the teneurins in animals. The other class consists of uncharacterized proteins shorter than 400 amino acids, where this core domain of about 75 amino acids tends to occur in the N-terminal half. Over twenty such proteins are found in Pseudomonas putida alone; little sequence similarity or repeat structure is found among these proteins outside the region modeled by this domain
YDPYGEVLSESGAAPNPLRFTGQYYDAETGLYYNGARYYDPELGRFLSPDPIGLGGGLNLYAYVGNNPVN
WVDPLGL
>gnl|CDD|163409 TIGR03697, NtcA_cyano, global nitrogen regulator NtcA, cyanobacterial. Members of this protein family, found in the cyanobacteria, are the global nitrogen regulator NtcA. This DNA-binding transcriptional regulator is required for expressing many different ammonia-repressible genes. The consensus NtcA-binding site is G T A N(8)T A C [Regulatory functions, DNA interactions]
GKTIFFPGDPAEKVYFLRRGAVKLSRVYESGEEITVALLRENSVFGVLSLITGHRSDRFYHAVAFTRVEL
LAVPIEQVEKAIEEDPDLSMLLLQGLSSRILQTEMMIETLAHRDMGSRLVSFLLILCRDFGVPGQRGVTI
DLRLSHQAIAEAIGSTRVTITRLLGDLRKKKLISIHKKKITVHDPIALGQRFA
>gnl|CDD|163410 TIGR03698, clan_AA_DTGF, clan AA aspartic protease, AF_0612 family. Members of this protein family are clan AA aspartic proteases, related to family TIGR02281. These proteins resemble retropepsins, pepsin-like proteases of retroviruses such as HIV. Members of this family are found in archaea and bacteria [Protein fate, Degradation of proteins, peptides, and glycopeptides]
TLDVELSNPKNPEFMEVRALVDTGFSGFLLVPPDIVNKLGLPELDQRRVYLADGREVLTDVAKASIIING
LEIDAFVESLGYVDEPLLGTELLEGLGIVIDYRNQGL
>gnl|CDD|274731 TIGR03699, menaquin_MqnC, dehypoxanthine futalosine cyclase. members of this protein family are involved in menaquinone biosynthesis by an alternate pathway via futalosine [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
ERLSREEALELYKEADLLALGALADEVRRRRHPGNVVTFVVDRNINYTNICVVGCKFCAFYRPPGHPEGY
VLSVEEILQKIEELVAYGGTQILLQGGVNPDLGLDYYEDLFRAIKARFPHIHIHGFSPVEIVYIAKKEGL
SLREVLERLKEAGLDSIPGGGAEILSDRVRRIISPKKISSEEWLEVMETAHKLGLPTTATMMFGHVETLE
ERIEHLERIRELQDKTGGFTAFIPWTFQPGNTELGKKRPATSTEYLKVLAISRIFLDNIPNIQASWVTQG
KEVGQLALHFGANDFGSTMIEENVVAAAGASHRASREEIIRIIREAGFIPAQRDTLYNIL
>gnl|CDD|213851 TIGR03700, mena_SCO4494, putative menaquinone biosynthesis radical SAM enzyme, SCO4494 family. Members of this protein family appear to be involved in menaquinone biosynthesis by an alternate pathway via futalosine, based on close phylogenetic correlation with known markers of the futalosine pathway, gene clustering in many organisms, and paralogy with the SCO4550 protein [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
IREKVEAGQRLSFEDGLFLYASDDLLTLGELAALVRERKHGDKVYFNVNRHLNYTNICVNGCAFCAFQRE
RGEPGAYAMSLEEIVARVKEAYAPGATEVHIVGGLHPNLPFEWYLDMIRTLKEAYPDLHVKAFTAVEIHH
FSKISGLPTEEVLDELKEAGLDSMPGGGAEIFAEEVRQQICPEKISAERWLEIHRTAHELGLKTNATMLY
GHIETPAHRVDHMLRLRELQDETGGFQAFIPLAFQPDNNRLNRLLAKGPTGLDDLKTLAVSRLYLDNIPH
IKAYWVMLGLKLAQVALAFGVNDLDGTVVEEKIGHDAGAKSPQALSKDELVRLIRDAGRVPVERDTLYNE
V
>gnl|CDD|163413 TIGR03701, mena_SCO4490, menaquinone biosynthesis decarboxylase, SCO4490 family. Members of this protein family are putative decarboxylases involved in a late stage of the alternative pathway for menaquinone, via futalosine, as in Streptomyces coelicolor and Helicobacter pylori [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
EFIALLEKRGELRRIKEPVDPYLEIAEIADRVVKKGGPALLFENVKGSDFPVLMNLFGTEKRVKLALGVE
DLEEIADRIRALLKLPPPKGFLEKLKMLPKLASLRNIFPKRVKKAPCQEVVLRGDEVDLEKLPILTTWPK
DGGPFITLPLVYTQDPETGIRNLGMYRLQVYDKRTLGMHWQIHKDGAHHFHEAKQAGEKLPVAIALGGDP
ALIYAATAPLPPGIDELLFAGFLRGEPVELVKCLTVPLPVPADAEIVLEGYVDPGELRPEGPFGDHTGFY
TPAEPYPVFHVTAITHRKDPIYPATVVGKPPQEDKYLGKATERIFLPLLQLIAPEIVDYHMPEEGVFHNL
ILVSIKKRYPGHAKKVMHALWGLGQMSFTKHIVVVDEDVDLHDYDAVLWYVLGRFDPKRDLLISEGPVDA
LDHASPEFAFGGK
>gnl|CDD|163414 TIGR03702, lip_kinase_YegS, lipid kinase YegS. Members of this protein family are designated YegS, an apparent lipid kinase family in the Proteobacteria. Bakali, et al. report phosphatidylglycerol kinase activity for the member from Escherichia coli, but refrain from calling that activity synonymous with its biological role. Note that a broader, subfamily-type model (TIGR00147), includes this family but also multiple paralogs in some species and varied functions [Unknown function, Enzymes of unknown specificity]
KALLILNGKQADNEDVREAVGDLRDEGIQLHVRVTWEKGDAQRYVAEALALGVSTVIAGGGDGTLREVAT
ALAQIRDDAAPALGLLPLGTANDFATAAGIPLEPAKALKLALNGAAQPIDLARVNGKHYFLNMATGGFGT
RVTTETSEKLKKALGGAAYLITGLTRFSELTAASCEFRGPDFHWEGDFLALGIGNGRQAGGGQVLCPDAL
INDGLLDVRILPAPELLPATLSTLFGGDKNPEFVRARLPWLEIEAPQPLTFNLDGEPLSGRHFRIEVLPG
ALRCHLPPGCPLL
>gnl|CDD|274732 TIGR03703, plsB, glycerol-3-phosphate O-acyltransferase. Members of this protein family are PlsB, glycerol-3-phosphate O-acyltransferase, present in E. coli and numerous related species. In many bacteria, PlsB is not found, and appears to be replaced by a two enzyme system for 1-acyl-glycerol-3-phosphate biosynthesis, the PlsX/Y system [Fatty acid and phospholipid metabolism, Biosynthesis]
LLRLPLSLLVRSKVIPSDPIQELGLDPERPIVYVLPTRSLSDLLALQKACRKLGLPDPLEPLVIGGQRLP
RYVFLDRPPPLFSDRQKKSTSLPLLHRLLELHREDPELDVQLVPVSVFWGRAPGKESSGWKLLFLDSWAS
PGRLRKFLIVLFLGRDNFVRFSPPVSLRYMADEHGTDESIAHKLARVARVHFRRQRLAAIGPDLSHRRTL
FNKLLASPSVRKAIRDEAKSKKISEEKARKRALKYLDEIAADYSYSLIRFLDRFLTWLWNKLYQGINVNN
ADRVRKLAQKGHEIIYVPCHRSHMDYLLLSYVLYHEGLVPPHIAAGINLNFWPAGPIFRRGGAFFIRRSF
KGNKLYSAVFREYLHELFAKGYSVEYFVEGGRSRTGRLLPPKTGMLAMTLQAMLRGIRRPITLVPVYIGY
EHVMEVATYLKELRGKRKEKESVFGVLKTLRKLRNFGQGYVNFGEPINLNDYLNKHVPNWRDDINPIEEE
KPTWLTPAVNELANQVMTRINNAAAVNAVNLCALALLASRKHALSREELLAQLDLYLSLLRNVPYSERST
VPEEDPEELLEHALELNKFTVEEDSLGEIISLDREQAVLMTYYRNNILHLFALPSLVASIVIHNKKISRA
ELQALVRLLYPLLKAELFLRWSEEELPEVIDRILDELVRQGLIEQDGDVLTRNAARSREFVQLQLLAASI
QETLQRYAITLSLLQRSGSISRDALEKQSQQLAQRLSVLHGINAPEFFDKAVFSTFIATLREQGYLDDDG
DGKLIFDEKLEELADQLKALLSPEVRQTI
>gnl|CDD|274733 TIGR03704, PrmC_rel_meth, putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific. This protein family is closely related to two different families of protein-(glutamine-N5) methyltransferase. The first is PrmB, which modifies ribosomal protein L3 in some bacteria. The second is PrmC (HemK), which modifies peptide chain release factors 1 and 2 in most bacteria and also in eukaryotes. The glutamine side chain-binding motif NPPY shared by PrmB and PrmC is N[VAT]PY in this family. The protein substrate is unknown [Protein synthesis, Ribosomal proteins: synthesis and modification]
VVTRLRAAGCVFAEDEAALLVDAARTPGELAAMVDRRVAGLPLEHVLGWAEFCGLRIAVDPGVFVPRRRT
EFLVDEAAALARPRSGTLVVVDLCCGSGAVGAALAAALDGIELHAADIDPAAVRCARRNLADAGGTVHEG
DLYDALPTALRGRVDILAANAPYVPTDAIALMPPEARDHEPRVALDGGADGLDVLRRVAAGAPDWLAPGG
HLLVETSERQAPLAVEAFARAGLIARVASSEELYATVVIGT
>gnl|CDD|274734 TIGR03705, poly_P_kin, polyphosphate kinase 1. Members of this protein family are the enzyme polyphosphate kinase 1 (PPK1). This family is found in many prokaryotes and also in Dictyostelium. Sequences in the seed alignment were taken from prokaryotic consecutive two-gene pairs in which the other gene encodes an exopolyphosphatase. It synthesizes polyphosphate from the terminal phosphate of ATP but not GTP, in contrast to PPK2 [Central intermediary metabolism, Phosphorus compounds]
YINRELSWLAFNERVLEEAADPSVPLLERLRFLSISSSNLDEFFMVRVAGLKRQIRAGVDQPSPDGLTPK
EQLAAISEKAHELVEEQYRILNELLPELAREGIRVLNRDELTEAQREWLRKYFREEVFPVLTPLALDPAH
PFPFLPNKSLNLAVELERDAFGRESQLALVQVPRALPRFIRLPPEGGKGKRFILLEDVIRLFLDELFPGY
TVKGCYQFRVTRDSDLDVDEEEAEDLLEALESELKQRRRGDAVRLEVEADMPEELLKFLLEELGLSEDDV
YVVGGPVNLKDLSQLPDLVDRPDLKFPPYPPRFPERLREHEGIFDAIRKKDILLHHPYESFDPVVEFLRQ
AAEDPDVLAIKQTLYRTSKDSPIIDALIEAAENGKEVTVVVELKARFDEEANIRWARRLEEAGVHVVYGV
VGLKTHAKLALVVRREGGELRRYVHLGTGNYHPKTARLYTDLSLFTADPEIGRDVARVFNYLTGYSRPPK
FKHLLVSPFTLRKRLLELIDREIENARAGKPARIIAKMNSLVDPDLIDALYEASQAGVKIDLIVRGICCL
RPGVPGLSENIRVRSIVGRFLEHSRIYYFGNGGEEKVYISSADWMTRNLDRRVEVLFPIEDPTLKQRVLD
EILEAYLADNVKARILQPDGSYRRVKRGNKEPFNAQLALMEN
>gnl|CDD|274735 TIGR03706, exo_poly_only, exopolyphosphatase. It appears that a single enzyme may act as both exopolyphosphatase (Ppx) and guanosine pentaphosphate phosphohydrolase (GppA) in a number of species. Members of the seed alignment use to define this exception-level model are encoded adjacent to a polyphosphate kinase 1 gene, and the trusted cutoff is set high enough (425) that no genome has a second hit. Therefore all members may be presumed to at least share exopolyphospatase activity, and may lack GppA activity. GppA acts in the stringent response [Central intermediary metabolism, Phosphorus compounds]
PIAAIDIGSNSVRLVIARGVEGSLQVLFNEKEMVRLGEGLDSTGRLSEEAIERALEALKRFAELLRGFPV
DEVRAVATAALRDAKNGPEFLKEAEAILGLPIEVISGEEEARLIYLGVAHTLPIADGLVVDIGGGSTELI
LGKDGEPGEGVSLPLGCVRLTEQFFPDGPISKKSLKQARKAAREELASLKWLKKGGWRPLYGVGGTWRAL
ARLHMAQRGYPLHGLHGYEITAEGLLELLEELIKLSREERLKLPGLSKDRADILPGGAAILEELFRALGI
EQIIFSSGGLREGVLYELLG
>gnl|CDD|213852 TIGR03707, PPK2_P_aer, polyphosphate kinase 2, PA0141 family. Members of this protein family are designated polyphosphate kinase 2 (PPK2) after the characterized protein in Pseudomonas aeruginosa. This family comprises one of three well-separated clades in the larger family described by pfam03976. PA0141 from this family has been shown capable of operating in reverse, with GDP preferred (over ADP) as a substrate, producing GTP (or ATP) by transfer of a phosphate residue from polyphosphate. Most species with a member of this family also encode a polyphosphate kinase 1 (PPK1) [Central intermediary metabolism, Phosphorus compounds]
RMSRKEYEAELERLQIELVKLQEWVKETGARIVIVFEGRDAAGKGGTIKRITEHLNPRGARVVALPKPTD
RERTQWYFQRYVQHLPAAGEIVLFDRSWYNRAGVERVMGFCTDEQYEEFLRQVPEFERMLVDDGIHLFKY
WLSVSREEQLRRFKARENDPLKQWKLSPMDLESLDKWDDYTRAKDEMFARTDTEEAPWTVVRSDDKKRAR
LNAIRHILSKLDYEDKDREA
>gnl|CDD|274736 TIGR03708, poly_P_AMP_trns, polyphosphate:AMP phosphotransferase. Members of this protein family contain a domain duplication. The characterized member from Acinetobacter johnsonii is polyphosphate:AMP phosphotransferase (PAP), which can transfer the terminal phosphate from poly(P) to AMP, yielding ADP. In the opposite direction, this enzyme can synthesize poly(P). Each domain of this protein family is homologous to polyphosphate kinase, an enzyme that can run in the forward direction to extend a polyphosphate chain with a new terminal phosphate from ATP, or in reverse to make ATP (or GTP) from ADP (or GDP) [Central intermediary metabolism, Phosphorus compounds]
FESAELGHSLDKATYKKQVPDLREALLDLQYELLESAGFPVIILIEGWDGAGKGETINLLNEWMDPRGIE
THAFGRPSDEERERPPMWRFWRRLPPKGKIGIFFGSWYTRPLIERLEGRIDEAKLDSHIEDINRFERMLA
DDGALILKFWLHLSKKQQKERLKKLEKDPETRWRVTPEDWKQLKVYDRYRKLAERMLRYTSTPYAPWTVV
EGEDDRYRSLTVGRTLLAAIRARLAQKELAQAQGEAPPAKTPLPPDEPSVLDKLDLSQKLDKDEYEERLE
LLQGRLAKLQRDPRFRKRSLVLVFEGWDAAGKGGAIRRVTEALDARQYRVVPIAAPTDEEKAQHYLWRFW
RHIPRRGRITIFDRSWYGRVLVERVEGFCSEAEWLRAYGEINDFEEQLTEHGAIVVKFWLHIDKEEQLRR
FEERENTPFKRYKITDEDWRNREKWDAYEDAVNDMIDRTSTIIAPWTLVEANDKRYARIKVLRTVCDAIE
AAL
>gnl|CDD|274737 TIGR03709, PPK2_rel_1, polyphosphate:nucleotide phosphotransferase, PPK2 family. Members of this protein family belong to the polyphosphate kinase 2 (PPK2) family, which is not related in sequence to PPK1. While PPK1 tends to act in the biosynthesis of polyphosphate, or poly(P), members of the PPK2 family tend to use the terminal phosphate of poly(P) to regenerate ATP or GTP from the corresponding nucleoside diphosphate, or ADP from AMP as is the case with polyphosphate:AMP phosphotransferase (PAP). Members of this protein family most likely transfer the terminal phosphate between poly(P) and some nucleotide, but it is not clear which [Central intermediary metabolism, Phosphorus compounds]
LDTFRVTPGKKVNLADIDTDDTPGYDSKEEAEALLAELVARLSDLQEKLYAEGRRSLLLVLQAMDAAGKD
GTIRHVMSGVNPQGCQVTSFKAPSAEELDHDFLWRIHKALPERGEIGIFNRSHYEDVLVVRVHGLIPKAI
WERRYEDINDFERYLTENGTTILKFFLHISKEEQKKRFLARLDDPTKNWKFSPADLKERAYWDDYMEAYE
DALTATSTKHAPWYVVPADDKWFRRLAVAEILLDALESLDLKYPEPDPDLAAEL
>gnl|CDD|274738 TIGR03710, OAFO_sf, 2-oxoacid:acceptor oxidoreductase, alpha subunit. This family of proteins contains a C-terminal thiamine diphosphate (TPP) binding domain typical of flavodoxin/ferredoxin oxidoreductases (pfam01855) as well as an N-terminal domain similar to the gamma subunit of the same group of oxidoreductases (pfam01558). The genes represented by this model are always found in association with a neighboring gene for a beta subunit (TIGR02177) which also occurs in a 4-subunit (alpha/beta/gamma/ferredoxin) version of the system. This alpha/gamma plus beta structure was used to define the set of sequences to include in this model. This pair of genes is not consistantly observed in proximity to any electron acceptor genes, but is found next to putative ferredoxins or ferredoxin-domain proteins in Azoarcus sp. EbN1, Bradyrhizobium japonicum USDA 110, Frankia sp. CcI3, Rhodoferax ferrireducens DSM 15236, Rhodopseudomonas palustris BisB5, Os, Sphingomonas wittichii RW1 and Streptomyces clavuligerus. Other potential acceptors are also sporadically observed in close proximity including ferritin-like proteins, reberythrin, peroxiredoxin and a variety of other flavin and iron-sulfur cluster-containing proteins. The phylogenetic distribution of this family encompasses archaea, a number of deeply-branching bacterial clades and only a small number of firmicutes and proteobacteria. The enzyme from Sulfolobus has been characterized with respect to its substrate specificity, which is described as wide, encompassing various 2-oxoacids such as 2-oxoglutarate, 2-oxobutyrate and pyruvate. The enzyme from Hydrogenobacter thermophilus has been shown to have a high specificity towards 2-oxoglutarate and is one of the key enzymes in the reverse TCA cycle in this organism. Furthermore, considering its binding of coenzyme A, it can be reasonably inferred that the product of the reaction is succinyl-CoA. The genes for this enzyme in Prevotella intermedia 17, Persephonella marina EX-H1 and Picrophilus torridus DSM 9790 are in close proximity to a variety of TCA cycle genes. Persephonella marina and P. torridus are believed to encode complete TCA cycles, and none of these contains the lipoate-based 2-oxoglutarate dehydrogenase (E1/E2/E3) system. That system is presumed to be replaced by this one. In fact, the lipoate system is absent in most organisms possessing a member of this family, providing additional circumstantial evidence that many of these enzymes are capable of acting as 2-oxoglutarate dehydrogenases and
DVVIRIGGAAGDGIQTAGEIFAKALARAGYYVFTFRDYPSRIRGGHSYFQIRISDEPVRSPGDGVDVLVA
LNPETLKEHLDELRPGGIIIYDSDLFDEEDLEKARVIPVPLTEIAKEAKGRKRMKNMVALGALAALLGLD
LEPLEEVIREKFGKKPEIAEANLKALRAGYDYAEETEKTDYLVLPAPPKDGDRILISGNEAIALGAIAGG
LRFLAAYPITPATDILHFLAKHLKKFGVVVVQAEDEIAAINMAIGASYAGARAMTATSGPGFALMSEALG
LAGMTETPLVIVDVQRGGPSTGLPTKTEQSDLLFALYGGHGEFPRIVLAPGSPEECFYLAAEAFNLAEKY
QTPVIVLSDQYLANSYATVPPPDLDDLPAIDRGKVLEPEEEYKRYELTEDGISPRAIPGTPGGIHRATGL
EHDETGHISEDPENRVKMMEKRARKLETIAKEIPEPEVYGDEDADVLIIGWGSTYGAIREAVERLRAEGI
KVALLHLRLLYPFPKNELAELLEGAKKVIVVEQNATGQLAKLLRAETGIVKVRSILKYDGRPFTPEEIVE
AI
>gnl|CDD|163423 TIGR03711, acc_sec_asp3, accessory Sec system protein Asp3. This protein is designated Asp3 because, along with SecY2, SecA2, and other proteins it is part of the accessory Sec system. The system is involved in the export of serine-rich glycoproteins important for virulence in a number of Gram-positive species, including Streptococcus gordonii and Staphylococcus aureus. This protein family is assigned to transport rather than glycosylation function, but the specific molecular role is unknown [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
YQIYWTDISETTYLYGTTVKFLSDNEVYFENPLMPSGETIHTWSSLTNYQAARTVPSLPLLKRGQTYKLS
LNADASPEGSVYLKITFFDRQGEEIGTEIEKDDSIIFIYPDEAYFYKISLISAGSESFTFHYLKI
>gnl|CDD|274739 TIGR03712, acc_sec_asp2, accessory Sec system protein Asp2. This protein is designated Asp2 because, along with SecY2, SecA2, and other proteins it is part of the accessory secretory protein system. The system is involved in the export of serine-rich glycoproteins important for virulence in a number of Gram-positive species, including Streptococcus gordonii and Staphylococcus aureus. This protein family is assigned to transport rather than glycosylation function, but the specific molecular role is unknown [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
RILQIGGDNWEKKFNIPENMEWDYFDIGLFVFDSGSSEAEKKILEKEGIKSFDAVLVTDKTYSPQLFKLL
QLIEPYTTFYDKNLQANQYDQEKFLKKKCAQPLDYESPEQLIRKLSKVLFSGQYGDKLFPSQIQVNPHFK
GIYEYEGNSSLELEGDFGEDFQPLVTWKYNIVSDKDKVIEIWLEYEKEGDCEIRLTIRLIQPGSDDDIVE
ELVFSEKDLNQPIQLEARDFDGFLSVSLEAKGKGTLKIGALHKRWSRLGLGQFILGGQRLVDSKRQEFIY
YFNPGDFKPPLNVYFSGYRPAEGFEGYFMMKRLGAPFLLIGDPRLEGGAFYLGSDEYEQGIINVIQEKLD
YLGFDHDQLILSGLSMGTFGALYYGAKLSPHAIIVGKPLVNLGTIASRMRLDRPDEFGTALDILLLNTGG
TSSEDVVKLDNRFWKKFKKSDLSKTTFAIAYMKNDDYDPTAFQDLLPYLSKQGAQVMSKGIPGRHNDDSP
TVNSWFINFYNIILEDDFGRV
>gnl|CDD|274740 TIGR03713, acc_sec_asp1, accessory Sec system protein Asp1. This protein is designated Asp1 because, along with SecY2, SecA2, and other proteins it is part of the accessory secretory protein system. The system is involved in the export of serine-rich glycoproteins important for virulence in a number of Gram-positive species, including Streptococcus gordonii and Staphylococcus aureus. This protein family is assigned to transport rather than glycosylation function, but the specific molecular role is unknown [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
MKYFIPAWYNSNRWWYDDIVPWYIKIPNTEFDDTISQMTMFQKNDEESRLIVLNYQPQLRYFLHRYDLLE
MTYWSVFDEIQGIHHFEPQAIDYRDLNWPEDTEFIYTPFLVLAVKSGKLFAKVQFSQEGYLLWIEYFEDE
QIARRLIFDDRGFVSSIRYFDDGGEAYQEYLNPKGEWIFREDLKTGKVTVNPEFQFHFKKLEYSNMDELI
REKFQRYLKVEVKDDDEIIVASDDRHNFLVADTFPAKNLIFSLFSERNRHHTYLDLYESLSRADLIIVDR
EDIERLLEENYRENYVEFDISRITPFDTRLRLGQSQQLYETEIGFWIDGLSDEELQQILQQLLQYILKNP
DYELKILTYNNDNDITQLLEDILEQINEEYNQDKNFFSLSEQDENQPILQTDEEQKEKERIAFTTLTNEE
DLISALDKLRLIIDLSKEPDLYTQISGISAGIPQINKVETDYVEHNKNGYIIDDISELLKALDYYLDNLK
NWNYSLAYSIKLIDDYSSENIIERLNELI
>gnl|CDD|163426 TIGR03714, Protein_translocase_subunit_SecA_2, accessory Sec system translocase SecA2. Members of this protein family are homologous to SecA and part of the accessory Sec system. This system, including both five core proteins for export and a variable number of proteins for glycosylation, operates in certain Gram-positive pathogens for the maturation and delivery of serine-rich glycoproteins such as the cell surface glycoprotein GspB in Streptococcus gordonii [Protein fate, Protein and peptide secretion and trafficking]
INNLRLKKLRKILNKINALKGKMATLSDEELQAKTAEFKNRLVEGESLDDILPEAYAVVREADKRVLGMF
PYDVQVLGAIVLHQGNIAEMKTGEGKTLTATMPLYLNALTGKGAMLVTTNDYLAKRDAEEMGPVYEWLGL
TVSLGVVDDPDEEYDANEKRKIYNSDIVYTTNSALGFDYLIDNLASNKEGKFLRPFNYVIVDEVDSVLLD
SAQTPLVISGAPRVQSNLYHIADTFVRTLKEDVDYIFKKDKKEVWLTDKGIEKAEQYFKIDNLYSEEYFE
LVRHINLALRAHYLFKRNKDYVVTNGEVVLLDRITGRLLEGTKLQSGIHQAIEAKEHVELSKETRAMASI
TYQNLFKMFNKLSGMTGTGKVAEKEFIETYSLSVVKIPTNKPIIRIDYPDKIYATLPEKLMATLEDVKEY
HETGQPVLLITGSVEMSEIYSELLLREGIPHNLLNAQNAAKEAQIIAEAGQKGAVTVATSMAGRGTDIKL
GKGVAELGGLAVIGTERMENSRVDLQLRGRSGRQGDPGSSQFFVSLEDDLIKRWSPSWLKKYYKKYSVKD
SKLKPSALFKRRFRKIVEKAQRASEDKGESAREQTNEFEESLSIQRENIYAERNRLIEGSDFLDDDVDQI
IDDVFNMYAEEQDLSNKSLLKRFILENLSYQFKNDPDEFDLKNKEAIKDFLKEIADKELSEKKKVLNNDY
LFNDFERLSILKAIDENWIEQVDYLQQLKTVVTNRQNGQRNPIFEYHKEALESYEYMKKEIK
>gnl|CDD|274741 TIGR03715, cell_surface_protein_precursor, KxYKxGKxW signal peptide. This model describes a novel form of signal peptide that occurs as an N-terminal domain with a recognizable motif, reminiscent of the YSIRK and PEP-CTERM forms of signal peptide. This domain tends to occur on long, low-complexity (usually Serine-rich and heavily glycosylated) proteins of the Firmicutes, and (as with YSIRK) the majority of these proteins have the LPXTG cell wall-anchoring motif at the C-terminus
KKRYKMYKSGKHWVFAGIATLAL
>gnl|CDD|274742 TIGR03716, R_switched_YkoY, integral membrane protein, YkoY family. Rfam model RF00080 describes a structured RNA element called the yybP-ykoY leader, or SraF, which may precede one or several genes in a genome. Members of this highly hydrophobic protein family often are preceded by a yybP-ykoY leader, which may serve as a riboswitch. From the larger group of TerC homologs (pfam03741), this subfamily contains proteins YceF and YkoY from Bacillus subtilis. A transport function is proposed
VILEGLLSADNALVLAVMVKHLPEKQRKKALFYGLIGAYVFRFIALFLASFLIKFWWIKAIGALYLLYLA
IKHFRKKKKGKEDEEAEKKKAHSGFWRTVLKVELMDIAFSVDSILAAVALSGQFWVVFLGGIIGILIMRF
AATIFVKLLERFPELETAAFLLIGWIGVKLLLETLAHPSIPILHIEFPHSALWKLIFWGVLVAIAVVGWI
LSYRR
>gnl|CDD|163429 TIGR03717, R_switched_YjbE, integral membrane protein, YjbE family. Rfam model RF00080 describes a structured RNA element called the yybP-ykoY leader, or SraF, which may precede one or several genes in a genome. Members of this highly hydrophobic protein family commonly are preceded by a yybP-ykoY leader, which may serve as a riboswitch. From the larger group of TerC homologs (pfam03741), this subfamily contains protein YjbE from Bacillus subtilis. A transport function is proposed
ALLQIIAIDLVLGGDNAVVIALAARNLPAHQRKKAIFWGTAGAIVLRILLTAVAVYLLAIPFLKLIGGLL
LLWIGWKLLLEEEEEQGGDVKGSTTLWAAIKTIVIADAVMSLDNVLAVAGAAHGHLGLLIFGLLLSIPII
VWGSTLILKLMDRFPWIIYIGAALLGYVAGEMIVTD
>gnl|CDD|274743 TIGR03718, R_switched_Alx, integral membrane protein, TerC family. Rfam model RF00080 describes a structured RNA element called the yybP-ykoY leader, or SraF, which may precede one or several genes in a genome. Members of this highly hydrophobic protein family often are preceded by a yybP-ykoY leader, which may serve as a riboswitch. From the larger group of TerC homologs (pfam03741), this subfamily contains TerC itself from Alcaligenes sp. plasmid IncHI2 pMER610 and from Proteus mirabilis. It also contains the alkaline-inducible E. coli protein Alx, which unlike the two TerC examples is preceded by a yybP-ykoY leader
PLWLWIGFIALVLLLLALDLGVLHRKAHVVSFKEALLWSAVWVSLALLFGGGVWFYLGGEAALEFLTGYL
IEKSLSVDNLFVFLLIFSYFAVPREYQHRVLFWGILGALVLRAIFIAAGAALIEQFHWVLYIFGAFLLYT
GIKMLFEGDEEDDPENNPLVRLVRRVLPVTDKYHGDRFFVRENGKRYATPLFLVLVLVETTDLIFAVDSI
PAIFAVTQDPFIVFTSNIFAILGLRALYFLLAGLLERFHYLKYGLAVILVFIGVKMLLHATDVYHIPIGV
SLGVIVGTLAVSIVASLWKTRK
>gnl|CDD|274744 TIGR03719, ABC_ABC_ChvD, ATP-binding cassette protein, ChvD family. Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown
AQYIYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKV
GYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLD
SQLEIAMDALRCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGT
VVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPK
GRQAKSKARLARYEELLSQEFQKRNETAEIYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGI
VGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKLGKRE
IPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA
GCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEEDKKRRLGEDADQPHRIKYKKL
>gnl|CDD|274745 TIGR03720, collagen_triple_helix_repeat, exosporium leader peptide. This domain is found as a leader peptide in at least two proteins targeted to the exosporium, a structure that occurs as the outermost layer of Bacillus anthracis, B. cereus, and B. thuringiensis spores. The exosporium consists of a basal layer and a nap of hair-like filaments. BclA, the major protein of the nap filaments, is targeted there by this leader peptide [Cellular processes, Sporulation and germination]
INPELIGPTLPPVPPFTLP
>gnl|CDD|274746 TIGR03721, exospore_TM, BclB C-terminal domain. This domain occurs as the C-terminal region in a number of proteins that have extensive collagen-like triple helix repeat regions. Member domains are predicted by TmHMM to have four or five transmembrane helices. Members are found mostly in the Firmicutes, but also in Acanthamoeba polyphaga mimivirus. Members include spore surface glycoprotein BclB from Bacillus anthracis, a protein of the exosporium. The exosporium is an additional outermost spore layer, lacking in B. subtilis and most other spore formers, consisting of a basal layer and, above it, a nap of fine filaments
IIPFASGTTLALTTNAGGLAGTPGLIGFGSSAPGLSLVGGTIDLAGGLTNYAFSMPRDGIITSLAAYFSA
TAALALLGPVTITAQLYIAPAPSNVFTPVPGAPVTLTPPITGPIAVGSTASGIITGLNIPVTAGDRLLLV
VSATASGLSPIATVAGYVSAGLAIV
>gnl|CDD|274747 TIGR03722, tRNA_N6-adenosine_threonylcarbamoyltransferase, universal archaeal protein Kae1. This family represents the archaeal protein Kae1. Its partner Bud32 is fused with it in about half of the known archaeal genomes. The pair, which appears universal in the archaea, corresponds to EKC/KEOPS complex in eukaryotes. A recent characterization of the member from Pyrococcus abyssi, as an iron-binding, atypical DNA-binding protein with an apurinic lyase activity, challenges the common annotation of close homologs as O-sialoglycoprotein endopeptidase. The latter annotation is based on a characterized protein from the bacterium Pasteurella haemolytica [DNA metabolism, DNA replication, recombination, and repair]
LGIEGTAHTFGVGIVDEDGEILANVSDTYVPEKGGIHPREAAEHHAEVAPKLIKEALEEAGVSLEDIDAV
AFSQGPGLGPCLRVGATAARALALKLNKPLVGVNHCVAHIEIGRLTTGAKDPVVLYVSGGNTQVIAYRNG
RYRVFGETLDIGLGNALDKFAREVGLGHPGGPKIEELAEKGKEYIELPYTVKGMDLSFSGLLTAALRAYK
KGARLEDVCYSLQETAFAMLVEVTERALAHTGKKEVLLVGGVAANRRLREMLELMAEDRGAKFYVPPPEY
AGDNGAMIAYTGLLMYKHGVTIPVEESRVRQRWRTDEVEVPW
>gnl|CDD|274748 TIGR03723, T6A_TsaD_YgjD, tRNA threonylcarbamoyl adenosine modification protein TsaD. This model represents bacterial members of a protein family that is widely distributed. In a few pathogenic species, the protein is exported in a way that may represent an exceptional secondary function. This model plus companion (archaeal) model TIGR03722 together span the prokaryotic member sequences of TIGR00329, a protein family that appears universal in life, and whose broad function is unknown. A member of TIGR03722 has been characterized as a DNA-binding protein with apurinic endopeptidase activity. In contrast, the rare characterized members of the present family show O-sialoglycoprotein endopeptidase (EC. 3.4.24.57) activity after export. These include glycoprotease (gcp) from Pasteurella haemolytica A1 and a cohemolysin from Riemerella anatipestifer (GB|AAG39646.1). The member from Staphylococcus aureus is essential and is related to cell wall dynamics and the modulation of autolysis, but members are also found in the Mycoplasmas (which lack a cell wall). A reasonable hypothesis is that virulence-related activities after export are secondary to a bacterial domain-wide unknown function [Protein synthesis, tRNA and rRNA base modification]
ILGIETSCDETAVAIVDDGKGLLSNVVASQIDLHARYGGVVPELASRAHLENIPPLIEEALAEAGLTLSD
IDAIAVTAGPGLIGALLVGVSFAKALALALNKPLIGVNHLEGHLLAPFLEKPLEFPFLALLVSGGHTQLV
LVKGVGDYELLGETLDDAAGEAFDKVARLLGLGYPGGPAIDRLAKQGDPKAFKFPRPMLDRPGLDFSFSG
LKTAVLNLIEKLKQKGEELTKADIAASFQAAVVDVLVEKTKRALKKTGLKTLVVAGGVAANSRLRERLEE
LAEKRGLEVFFPPLELCTDNAAMIAAAGYERLK
>gnl|CDD|274749 TIGR03724, Probable_serine/threonine-protein_kinase, Kae1-associated kinase Bud32. Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine [Unknown function, General]
LIAKGAEAIIYLGDFLGRKAVIKERVPKSYRHPELDERLRKERTRREARLLSRARKAGVNTPVIYDVDPD
NKTIVMEYIEGKPLKDVIEENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKVYLIDFGLGKYSD
EIEDKAVDLHVLKRSLESTHPDKAEELFEAFLEGYREVFGEAKDVLERVKEIELRGRYV
>gnl|CDD|274750 TIGR03725, T6A_YeaZ, tRNA threonylcarbamoyl adenosine modification protein YeaZ. This family describes a protein family, YeaZ, now associated with the threonylcarbamoyl adenosine (t6A) tRNA modification. Members of this family may occur as fusions with ygjD (previously gcp) or the ribosomal protein N-acetyltransferase rimI, and is frequently encoded next to rimI [Protein synthesis, tRNA and rRNA base modification]
ILAIDTSTEALSVALLDDGKVLAERTEPAGRNHSERLLPMIEELLAEAGLSLQDLDAIAVGVGPGSFTGL
RIGLATAKGLALALGIPLVGVSSLEALAAQAAAQDGGGPVLVAIDARRGEVYWGLYDLKPLEEPAVLSPE
ELLELLKELNVLLVGDGAEAYALALLAAAADALPDAAALARLALARLKAGEPLDVEELEPLYLR
>gnl|CDD|274751 TIGR03726, strep_RK_lipo, putative cross-wall-targeting lipoprotein signal. The YSIRK signal domain targets proteins to the cross-wall, or septum, of dividing Gram-positive bacterial. Lipoprotein signal motifs direct a characteristic N-terminal cleavage and lipid modification for membrane anchoring. This Streptococcal-only signal peptide variant appears to be a hybrid between the two, likely directing protein targeting of nascent surface lipoproteins to the cross-wall. Nearly all members of this family have the characteristic LPXTG cell wall anchor signal at the C-terminus
YGFRKSKKYKTLCGAVLGTTVTAATAGTVVHADE
>gnl|CDD|274752 TIGR03727, urea_t_UrtC_arc, urea ABC transporter, permease protein UrtC, archaeal type. Members of this protein family are ABC transporter permease subunits restricted to the Archaea. Several lines of evidence suggest this protein is functionally analogous, as well as homologous, to the UrtC subunit of the Corynebacterium glutamicum urea transporter. All members of the operon show sequence similarity to urea transport subunits, the gene is located near the urease structural subunits in two of three species, and partial phylogenetic profiling identifies this permease subunit as closely matching the profile of urea utilization
KLGSPDILPSRLRSKLEGPNTLGNSRVFWAAFGVGVALLVVYPLIRDSYAAGQFSLFLALALLGLSLSVV
WGYTGILSFGQVAFFGIAAYTFGVVSINFGTAGGITAALPIAIVVGTISAAILGYFMFYGGVRDVYVTII
TLVVTLVLETFMAQTAGSEWAIGEAKLGGFNGMPDIPNLTLGVGGASFSFSGSEFYYLVLAVLVLTYLGL
RILVNSKYGYSMVAVREDEERTEMFGYNVKKIKLVVFTFGGALAGLSGVFYANWGNYIDPSVFTILFATL
PVVWVSLGGRESLLGAIVATVAIEWLRKWFSINAGEFAIVFVGLLLMVTILVIPRGIVPGLREGIEHGRD
TIQSRADSETPGSSEVMRE
>gnl|CDD|163440 TIGR03728, glyco_access_1, glycosyltransferase, SP_1767 family. Members of this protein family are putative glycosyltransferases. Some members are found close to genes for the accessory secretory (SecA2) system, and are suggested by Partial Phylogenetic Profiling to correlate with SecA2 systems. Glycosylation, therefore, may occur in the cytosol prior to secretion
VKSIDETLDYIIKNNCSVVRFGDGEIDLIAGESIGYQSYDPELAKRLKEILGNESDENLLVCLPDVFTSL
ERYNEDARYFWKGHLERYGDLYKELIKPDYWYGSTFVSRPYIDFEDKSKSGSYFEKLKQIWKNKDILIVE
GETSRSGVGNDLFDNAKSIKRIICPSKNAFSKYDEILEAIRENAKNKLILLMLGPTAKVLAYDLSDLGYQ
ALDIGHIDSEYEWFLMGAKYKVKLKNKHTAEVNFDENINEIDDNQYESQIIAKIE
>gnl|CDD|163441 TIGR03729, acc_ester, putative phosphoesterase. Members of this protein family belong to the larger family pfam00149 (calcineurin-like phosphoesterase), a family largely defined by small motifs of metal-chelating residues. The subfamily in this model shows a good but imperfect co-occurrence in species with domain TIGR03715 that defines a novel class of signal peptide typical of the accessory secretory system
KIAFSSDLHIDLNHFDTEEMLETLAQYLKKQKIDHLHIAGDISNDFQRSLPFIEKLQELKGIKVTFNAGN
HDMLKDLTYEEIESNDSPLYLHNRFIDIPNTQWRIIGNNGWYDYSFSNDKTSKEILRWKKSFWFDRRIKR
PMSDPERTAIVLKQLKKQLNQLDNKQVIFVTHFVPHRDFIYVPMDHRRFDMFNAFLGSQHFGQLLVKYEI
KDVIFGHLHRRFGPLTIGGTTYHNRPLGY
>gnl|CDD|163442 TIGR03730, tungstate_WtpA, tungstate ABC transporter binding protein WtpA. Members of this protein family are tungstate (and, more weakly, molybdate) binding proteins of tungstate(/molybdate) ABC transporters, as first characterized in Pyrococcus furiosus. Model seed members and cutoffs, pending experimental evidence for more distant homologs, were chosen such that this model identifies select archaeal proteins, excluding weaker archaeal and all bacterial homologs. Note that this family is homologous to molybdate transporters, and that at least one other family of tungstate transporter binding protein, TupA, also exists
VKLKIFHAGSLSVPFEEMEKEFEAKHPNVDVQREAAGSVAAVRKITELGKPADILASADYTLIPQMMIPN
YADWYIMFATNEIVLAYTDKSKYADEINSDNWYEILQRPDVRWGFSDPNDDPCGYRSLMVIQLAELYYND
PTIFDNLLLKNTNITVEENNGTYLIHVPKEIDVNRSKIFIRPKEVELLSLLESGEIDYAFIYKSVAVQHG
LKYIELPDEINLGDYSYADFYKKVSVELGGGKKTITGKPIVYGITVPKNAPNREEAIEFLKFL
>gnl|CDD|274753 TIGR03731, Lantibiotic_mutacin-1140, lantibiotic, gallidermin/nisin family. Members of this family are lantibiotic precursors in the family that includes gallidermin, nisin, mutacin, epidermin, and streptin [Cellular processes, Toxin production and resistance]
EKLFDFDLDVTAVSKSNDSDVDPRITSKSLCTPGCATGSNTLFNSYCC
>gnl|CDD|274754 TIGR03732, lanti_perm_MutE, lantibiotic protection ABC transporter permease subunit, MutE/EpiE family. Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family is largely restricted to gallidermin-family lantibiotic cassettes, but also include orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes. In most species, this subunit is paralogous to an adjacent gene, modeled separately
NYIKSENLKIKRTFSKKLIWIAPIIFLLLAFLLSPSYFQYATFNWWYVIFLPGMIALICALLHKKEKKAS
NYRAILSLPVDLKKVWIAKILVIAIYLLISCIILFIGLVLIGFVIPPSNISIGQALLASLLIWLTSLWQI
PLCLFLARKFGMFVSILVNLVLGLIFGIVLATKSFWWLFPYSWPSRLMCPILGILPNGLPLEAGSPLLNY
SVIPIGIILSIVLFILLTFLTAKWFKKQEVK
>gnl|CDD|163445 TIGR03733, lanti_perm_MutG, lantibiotic protection ABC transporter permease subunit, MutG family. Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family is largely restricted to gallidermin-family lantibiotic cassettes, but also include orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes. In most species, this subunit is paralogous to an adjacent gene modeled separate by TIGR03732, while in some species only one subunit is found
RLLKSDFIKLKRTSILWIHICAPILGSLLFLLYYSFRGLDNIDIIEGYFQVLAIVLPLLIGIVCGMVVEQ
EESAGNFKNLLSTTKSKYKAYLSKLLLLLLCGFFSTFLAIGIFALGFKYLLKVANLPLSLFLIAALLLII
GSLFLYIIHLFVSFAFGMGASIGIGIVGTLMAALMLTGLGDKIWQYIPWAWGVRLSDYPGIYSKKAIDPS
FYSSLSQELSTGLIVCAFVTIIVFIISLIWFKRWEGRK
>gnl|CDD|274755 TIGR03734, PRTRC_parB, PRTRC system ParB family protein. A novel genetic system characterized by six major proteins, included a ParB homolog and a ThiF homolog, is designated PRTRC, or ParB-Related,ThiF-Related Cassette. It is often found on plasmids. This protein family the member related to ParB, and is designated PRTRC system ParB family protein
LIVPGNNPRRYFDPAEMAELVESIRAKGVLQPILVRPVPGSDLYEVVAGERRYRAALEVFGEDYDIPALI
KVLTDEEAEAAALIENVQRADMSPAEEAEAAARLLGRCKGDREEAARRLGWSPATLDRRLALMNCTDEVR
QALIDRKILLGHAELLAGLPKDKQDNVLTAILAEKPTVAELKKMIESAALSLSAAIFDKADCGACPHNSA
RQQALFGESIGEGNCTNRECFDEKTEAALESRAAALRDDYQVVRIVRPGDNFTVIPLAADGTLGVGEEQA
TACRSCEDFGAAVSALPGSLGKVTKGLCFDTVCNTTKVAARKKAERAAAAAAQKPAAPAAGPGTPAKEKS
PAETATSGAAKPAAKKAVPSSQPSNRVKDYREKVWRKALARELALNPEQNRRVLIALALASDARVIKDEK
FGKAFGKLTGEKSAAAADLGTALTQAMALDDEHLAKLLQALPASAAEGLEVHALKSLLNYLEVDLTRHWK
LNKEFLELLTKSEIDALADEIGLKAAMGKEFKKLRAGKKGDFIKALLAVPGFDYAGKLPKVLRW
>gnl|CDD|163447 TIGR03735, PRTRC_A, PRTRC system protein A. A novel genetic system characterized by six major proteins, included a ParB homolog and a ThiF homolog, is designated PRTRC, or ParB-Related,ThiF-Related Cassette. It is often found on plasmids. This protein family is designated protein A
DAILQAVFPTVAAPRFGVLEPLEKPGHRFIVAADGVWREVRRPWLHAIQRVAPASPITVPYGAVEETLEF
LCGPIPASLLEEFAEAARAALPNEVAAWIVWNSETGSLRLAALESIEASPGHIDYRRPRLDDGEHLVVDL
HSHGTGSAFFSETDDADDKGEVKISGVLGCLDQGTPQAVFRLCLLGVFVPLK
>gnl|CDD|163448 TIGR03736, PRTRC_ThiF, PRTRC system ThiF family protein. A novel genetic system characterized by six major proteins, included a ParB homolog and a ThiF homolog, is designated PRTRC, or ParB-Related,ThiF-Related Cassette. This family is the PRTRC system ThiF family protein
HKIPPALLSRPVSVVLVGAGGTGSQVIAGLARLHHALKALGHPGGLAVTVYDDDTVSEANVGRQAFYPAD
VGQNKAIVLVNRLNQAMGTDWTAHPERVERSSTLHRPDIVIGCVDNRAARLAILRAFEGGYSGYAYWLDL
GNRADDGQVILGQVPSRAKGENRLRLPHVGELFPELIDPSVDPDDDRPSCSLAEALAKQSLFINQAIAVF
AMNLLWKLFRKGRLEFHGVFVNLATGRTNPLPVD
>gnl|CDD|274756 TIGR03737, PRTRC_B, PRTRC system protein B. A novel genetic system characterized by six major proteins, included a ParB homolog and a ThiF homolog, is designated PRTRC, or ParB-Related,ThiF-Related Cassette. This protein family is designated protein B
FALSKAILLYGARSGYSDTTYATAHDVEDSSGKPVIGAGRPLTRDDLMELVRQLAQQQAPDLEFLDPNVL
ALSPGLMVWWTPAATRRVFFQSKMFGLRSGVVPHPGLVFAAHQEGLRVFALKGSERPGPETKLYQAPLFN
VWSNGEICAGNARLPDRPTVANISAWEDAFFSSRFTHPNPASKDRLTYGVGPYAFWKDMLDGKFKEFPES
VLVPMKLTLGQLLARITE
>gnl|CDD|163450 TIGR03738, PRTRC_C, PRTRC system protein C. A novel genetic system characterized by six major proteins, included a ParB homolog and a ThiF homolog, is designated PRTRC, or ParB-Related,ThiF-Related Cassette. It is often found on plasmids. This protein family is designated PRTRC system protein C
STTTLSRVFTYNGVRLADPSPAMSPEQVRDFYSAQYPELLNAEVEGPVVKGGVQTYTFRRAVGAKG
>gnl|CDD|274757 TIGR03739, PRTRC_D, PRTRC system protein D. A novel genetic system characterized by six major proteins, included a ParB homolog and a ThiF homolog, is designated PRTRC, or ParB-Related,ThiF-Related Cassette. It is often found on plasmids. This protein family is designated PRTRC system protein D. The gray zone, between trusted and noise, includes proteins found in the same genomes as other proteins of the PRTRC systems, but not in the same contiguous gene region
AVDVGYGNTKFVSQVRGTDIRCASFPSVAPPSSRESPAWPGGSEARKTVCVPVGGLFYEVGPDVSLAADT
NRARQLHDEYTETPEYMALLRGALALSKVREIDQLVVGLPVATLTTYKSALEKAVTGEHDIGAGKAVTVR
KVLAVPQPQGALVHFVAQHGKLLTGKEQSLIIDPGYFTFDWLVARGMRLVQKRSGSVNGGMSDIYRLLAA
EISKDIGTPAYRDIDRIDLALRTGKQPRIYQKPVDIKRCLELAETVAQQAVSTMMTWIGAPESIQNIVLV
GGGAFLFKKAVKAAFPKHRIVEVDEPMFANVRGFQIAGLA
>gnl|CDD|163452 TIGR03740, galliderm_ABC, gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit. Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes
LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLH
KIGSLIESPPLYENLTARENLKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALL
NHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK
SENLEKLFVEVVK
>gnl|CDD|274758 TIGR03741, PRTRC_E, PRTRC system protein E. A novel genetic system characterized by six or seven major proteins, included a ParB homolog and a ThiF homolog, is designated PRTRC, or ParB-Related,ThiF-Related Cassette. It is often found on plasmids. This protein family averages about 150 amino acids in length, but the last third contains low-complexity sequence that complicates sequence comparisons. This model does not include the low-complexity region
MFQALHPLLTAATKLTVSLTAVGDKLTVTVTPTPKSGAKDAALTKPLVLTGTPAELDAGFAEALGQYVEA
RQSLAEQAAATRAVLEAAKAAEAAKAAKAASKKP
>gnl|CDD|274759 TIGR03742, PRTRC_F, PRTRC system protein F. A novel genetic system characterized by seven (usually) major proteins, including a ParB homolog and a ThiF homolog, is commonly found on plasmids or in bacterial chromosomal regions near phage, plasmid, or transposon markers. It is most common among the beta Proteobacteria. We designate the system PRTRC, or ParB-Related,ThiF-Related Cassette. This protein family is designated protein F. It is the most divergent of the families
DTLVLPRISPEVPLYVTGESAAASNLALASFLAEKGALRAPDVPDPADLADAVQQALQAWLRGQVGARLC
LGPDFAISAIDEQGLGYEFEDPTPLPLWLAIELANNWVYYFELEPLGPRIEALEAASPGLGWTVLDVIYR
ASARGPGLYTPDALFDHFSYIYWEGETDEEEALEELCDEDDEDREAYLPSVVEQALLEDDFLPSHLLGWA
ARKQLDAAGRVALVRLRARSDPAVRDVVTAALELPALFAKRRGAYDDFAPDQDGESIGSGALIRWDDSDF
ATEIIDDLEEDASQGGDADDTLFVVFVPLDTEPAALAEWLRDMRLYFQAIAALDRLLALLSD
>gnl|CDD|274760 TIGR03743, SXT_TraD, conjugative coupling factor TraD, SXT/TOL subfamily. Members of this protein family are the putative conjugative coupling factor, TraD (or TraG), rather distantly related to the well-characterized TraD of the F plasmid. Members are associated with conjugative-transposon-like mobile genetic elements of the class that includes SXT, an antibiotic resistance transfer element in some Vibrio cholerae strains [Mobile and extrachromosomal element functions, Other]
YENLLRPAYELYAAAAWAAAALLALVAPWALALPPPVGLATAGAAFAMGVYRLRQALRVLRYRRRLSGLP
LYAVSTSQLPVSSKKKPDSLFLGRGFEWTQKHTQRAYDILKRDVEEYVGLPRWARKAEERLLLAKLTNLD
GKKNPVRPLPPVGGSPWIHGVEPKEEDVYLPLGHRVGHTLVLGTTGVGKTRLAELLITQDIRRGDVVIVI
DPKGDADLKRRMRAEAKRAGRPDRFYYFHPGFPEISARYNPLGNFSRVSEVASRIAQLLSGEGESAAFKE
FAWRFVNIVARGLVAIGQRPSYKLILRYVESGIEPLLEKYLEKFFTQHYPPDWEEIVKIIAKIAEKNLPV
LMKGRPRLVAMIAVYLSEFIGKKLGDDVLDGLISAVRHDREHFDKIVASLLPLLEKLTTGELGKLLSPDY
NDLEDTRPIFDWEKVIRKKGVLYIGLDSLSDPTVASAVGNSMLADLVSVAGSIYNFGIGKSKPPRINLHV
DEANEAINDPFIPLLNKGRGAGFQVTAATQTISDIEARLGSKAKARQVLGNFNNLIMLRVRDTETAELLS
EQLPEVAIRTKTVVSGSSDTSEDPGTEFSSSVSDRVSEERVPLIPPSLLGQLPKLQYFALLSGGRLYKGR
IPIP
>gnl|CDD|274761 TIGR03744, traC_PFL_4706, conjugative transfer ATPase, PFL_4706 family. Members of this protein family are predicted ATP-binding proteins apparently associated with DNA conjugal transfer. Members are found both in plasmids and in bacterial chromosomal regions that appear to derive from integrative elements such as conjugative transposons. More distant homologs, outside the scope of this family, include type IV secretion/conjugal transfer proteins such as TraC, VirB4 and TrsE. The granularity of this protein family definition is chosen so as to represent one distinctive clade and act as a marker through which to define and recognize the class of mobile element it serves [Mobile and extrachromosomal element functions, Plasmid functions]
TIADEKRLYGRPPSFVDLLPWVEYLPEEKVFLLDDGVSVGAVFELVPIGTEGRTPDWLQERRDAVQDALQ
DSFDELDEAPWVVQFYCQDETDLDQYVERLRDYIHPRARGSEFTQAWLAEMERHLRAISKPGGLFEDTTV
TGLPWRGQQRRVRMVIYRRLGKNGKEPRGQDPIEMLNQVCERLIAALANAGVTARRQNGRQIYEWLLRWF
NPNPELAGGDPGELYRLAPYPDGEDPLPFGNDFAENLFFSQPRSDVDAGLWWFDGMPHRVLVVDNLRRAP
KIGHFTGEVRRGDKINALFDRLPEGTMLAITMVVTPQDKLEAHLERLSKKAVGETAESIHTRQDVETVRE
YMGRGHKLYRAGLAFYVRGRDEKELDRRSNELSAVLLGAGLQPVRPEDEVAPLNSYLRWLPMNFNPDLDR
KSRWYTRLMFAQHIANLLPVFGRSTGTGHPGITFFNRGGEPLTFDPLNKLDRKKNAHLLILGPTGAGKSA
TLTNLLMQVMAVHRPRLFIVEAGNSFGLLADYAARLGLSVNRVSLKPGSGVSLPPFADAHRLLETPEDVK
ALDADELEEEDADDEDPDDEDEEQRDILGEMEIAARLMITGGEEKEDARMSRADRSLIRQAILAAARTAS
AAGRQVLTQDVRNALETISRDPDLPEHRRARAAEMGEAMDMFCQGFEGELFNREGTPWPEADVTLVDLAT
LAREGYEAQLAIAYISLINTVNNLAERDQHDGRPIVMVTDEGHIITTNPLLAPYVVKITKMWRKLGAWFW
LATQNLADFPDSAEKMLNMIEWWLCLNMPPDEVEQIARFRELTEEQKAMLLSARKEPGKYTEGVVLSKNM
EALFRNVPPSLYLALAMTEKEEKAERRRLMQEHGCSELEAAYMVAEKLDRARG
>gnl|CDD|274762 TIGR03745, conj_TIGR03745, integrating conjugative element membrane protein, PFL_4702 family. Members of this protein family are found occasionally on plasmids such as the Pseudomonas putida TOL plasmid pWWO_p085. Usually, however, they are found on the bacterial main chromosome in a region flanked by markers of conjugative transfer and/or transposition [Mobile and extrachromosomal element functions, Plasmid functions]
ILLALAALLLPQSAFAALPTVEAPSRGEGSGIMQTIKNYGYDGGILLGLLIAAIAFIGVAYHALGTYHEI
RTGKATWGDFGATVVVGAILLVVIIWLLTKATTIL
>gnl|CDD|163458 TIGR03746, conj_TIGR03746, integrating conjugative element protein, PFL_4703 family. Members of this protein family are found occasionally on plasmids such as the Pseudomonas putida TOL plasmid pWWO_p085. Usually, however, they are found on the bacterial main chromosome in regions flanked by markers of conjugative transfer and/or transposition. The function is unknown [Mobile and extrachromosomal element functions, Plasmid functions]
FRKAVANRDAHILTLRIAIGLLALILLALWFGWRTAPKDLTIHVPPDLRSGSTRKWWEVPPENVYAFAFY
IFQQLNRWPKDGEQDYGANIFRLSPYLTPSCRAFLQQDYELRRSNGELRQRVRGVYEIPGRGYSENRVIV
HSDDSWTVNLDLSVDEYYGGEPVKRALVRYPLRVVRWDVDPERNPWGLALDCYAGAPQRLEP
>gnl|CDD|163459 TIGR03747, conj_TIGR03747, integrating conjugative element membrane protein, PFL_4697 family. Members of this protein family are found occasionally on plasmids such as the Pseudomonas putida TOL plasmid pWWO_p085. Usually, however, they are found on the bacterial main chromosome in regions flanked by markers of conjugative transfer and/or transposition [Mobile and extrachromosomal element functions, Plasmid functions]
RPGLIGGLITLPFRLLGVLLGSLIFSILIEWVGMAFFWPEQGWLHSQQMMTTELGWLSEGFTRSLLVQEP
GRTASELIQTAYDWLFVKSGLLDWIQDETTVAAAGGRGRSLRYWAAWLYVYARDYLLAAVYVTLVFLVRL
VILVLAIPLFLLAAFVGLVDGLVRRDLRRFGAGRESSFVYHHAKRFVKPLMILPWVLYLSLPISIYPNLI
LLPAALLLGLAVSITASTFKKYL
>gnl|CDD|163460 TIGR03748, conj_PilL, conjugative transfer region protein, TIGR03748 family. This model describes the conserved N-terminal region of a variable length protein family associated with laterally transfered regions flanked by markers of conjugative plasmid integration and/or transposition. Most members of the family have the lipoprotein signal peptide motif. A member of the family from a pathogenicity island in Salmonella enterica serovar Dublin strain was designated PilL for nomenclature consistency with a neighboring gene for the pilin structural protein PilS. However, the species distribution of this protein family tracks much better with markers of conjugal transfer than with markers of PilS-like pilin structure [Mobile and extrachromosomal element functions, Plasmid functions]
VRYGRYTLVETRPEAAQRDLLNQVIDITIPPSLVATVGDALRYLLRRSGYSLCPASALSEAALLTLPLPA
AHRKLGPMTLRDALQVLAGPAWRLKVDDVTREVCF
>gnl|CDD|163461 TIGR03749, conj_TIGR03749, integrating conjugative element protein, PFL_4704 family. Members of this protein family are found occasionally on plasmids such as the Pseudomonas putida TOL plasmid pWWO_p085. Usually, however, they are found on the bacterial main chromosome in a region flanked by markers of conjugative transfer and/or transposition [Mobile and extrachromosomal element functions, Plasmid functions]
GAALLVASAAQAVEILKWERLPLAIPLVVGQERIVFVDKNVRVGVPQQLAGKLRVQSTGGAVYLRASEPF
PPTRLQLQDVDSGEIILLDIAATPKKAGQKSLEPVRIVYESKVATRTGSDGSDEAAASEPDKNARETPVP
VVLTRYAAQSLYAPLRTVEPVAGIRRVPLRLPLALTTLLPGAPVEAVPLAAWRLGDYYVTAVRLRNRSNR
PVTLDPRELQGRFVAATFQHPWLGPAGTPEDTTTLYLVTRGRPLATA
>gnl|CDD|274763 TIGR03750, hypothetical_protein, conjugative transfer region protein, TIGR03750 family. Members of this protein family are found occasionally on plasmids. Usually, however, they are found on the bacterial main chromosome in regions flanked by markers of conjugative transfer and/or transposition [Mobile and extrachromosomal element functions, Plasmid functions]
IPFLPDRLNREPVVFRGLTADELGVAAGVGLAAGLVLGLLLALLTGPWALIPTGALLGPILVVLIGGKLL
ARLKRGKPEGYLYRRLEWKLARLGLGGHRLILRSGGWSLRR
>gnl|CDD|274764 TIGR03751, conj_TIGR03751, conjugative transfer region lipoprotein, TIGR03751 family. Members of this protein family are found occasionally on plasmids. Usually, however, they are found on the bacterial main chromosome in regions flanked by markers of conjugative transfer and/or transposition [Mobile and extrachromosomal element functions, Plasmid functions]
MLLAALLLSGCSTSKEEMLPEGGLTMLDIWNGGGSSSRQLQDYRQTLRRPLSDPENYASLNEQESYTRTA
ENEISQLFPRLPNPDLVMYVFPHLAGGDPTPVPGYSTVFPFYEQVQYALPGERT
>gnl|CDD|274765 TIGR03752, conj_TIGR03752, integrating conjugative element protein, PFL_4705 family. Members of this protein family are found occasionally on plasmids such as the Pseudomonas putida toluene catabolic TOL plasmid pWWO_p085. Usually, however, they are found on the bacterial main chromosome in regions flanked by markers of conjugative transfer and/or transposition [Mobile and extrachromosomal element functions, Plasmid functions]
KSNKLLKVLVIPVILVVVLIGIKSFSGSGSPEPTSDTALAELSPEELKALGIEGDTPADTLRTLVAEVKE
LRKRLAKLISENEALKAENERLQKREQSIDQQIQQAVQSETQELTKEIEQLKSERQQLQGLIDQLQRRLA
GVLTGPSGGGSDLPVGLGLDPGGGAQFEGGGGVVWVEPQDALPTDRNGNSGAPSKFSFPTSFDNALDRGK
KALTRVTKGAPSQSANSKEKKARPVYTIPENSTLMGSVAMTALIGRVPIDGTVTDPYPFKVLIGPDNLTA
NGIELPDVAGAVVSGTASGDWTLSCVRGQVRSLTFVFNDGTIRTVPRPRNNSQTNGGDSGKSNGGLGWIS
DPYGIPCISGERRTNAPQYLGTQALITAAGAGAAGLALAQSQNTTTVNAGGGVTSGVTGDSGNYALGQAL
SGGVDEVADWVNKRYGQSFDAVYVPPGAQVAVHIDQELAIDYEPKGRKVDYG
>gnl|CDD|274766 TIGR03753, hypothetical_protein, beta-carotene 15,15'-monooxygenase, Brp/Blh family. This integral membrane protein family includes Brp (bacterio-opsin related protein) and Blh (Brp-like protein). Bacteriorhodopsin is a light-driven proton pump with a covalently bound retinal cofactor that appears to be derived beta-carotene. Blh has been shown to cleave beta-carotene to product two all-trans retinal molecules. Mammalian enzymes with similar enzymatic function are not multiple membrane spanning proteins and are not homologous
LIALLAVLLLGLPHGALDHLIAARLGGRRSIRFFAKFLLLYLLLAGLVLALWLVAPVAALLLFLAISAYH
FGEGDLYFLIKTRPGRALAILVRGGLVILLPLLFHPEEVADIFSALTGLFASFVPQLRLILGAIWGLLTL
GLLGLGLKRRPRRSWRLDAGELLLLLALFALLPPLVAFGLYFCLWHSLRHVARIVRVLDGGRASRSLLRF
ARWAAILTLATLILLLGLYLLLPDPLESLLALIFIGLAALTLPHMLLVD
>gnl|CDD|274767 TIGR03754, conj_TOL_TraD, conjugative coupling factor TraD, TOL family. Members of this protein are assigned by homology to the TraD family of conjugative coupling factor. This particular clade serves as a marker for an extended gene region that occurs occasionally on plasmids, including the toluene catabolism TOL plasmid. More commonly, the gene region is chromosomal, flanked by various markers of conjugative transfer and insertion
MEALLRPPVELWTAATCASAALLCVVAPWALALTPSIGLVTALAFAGFGLVRGRQALRVLRYQRNLRRLP
RYAMSSRQIPVSKKRLFLGKGFRWTQKHTQRLLDTKRPEVERYVQPSTCYRLARDLERRLESPLPWLAKL
TRTDSPLNPVRPLPPVGGSPVLHGVEPEEVPVSLPLGERVGHTLVLGTTRVGKTRLAELLITQDIRRGDV
VIVFDPKGDADLLKRMYAEAKRAGREDEFYVFHLGWPEISARYNAIGRFGRISEVATRIAGQLSGEGNSA
AFKEFAWRFVNIVARALVALGQRPDYTLILRYVTNIDPLFMEYAEKILRKHDPKAWELIEELIARLTDRN
LPRNMQGRPNRVVAIEQYLSEKKLYDPVLDGLRSAVRYDRTYFDKIVASLLPLLEKLTTGKTAKLLSPDY
SDMNDPRPIFDWMQVIRKKGIVYVGLDALSDAEVAAAVGNSMFADLVSVAGHIYKFGIDDGLPDGKYTEQ
KPPINLHCDEFNELMGDEFIPLINKGGGAGFQVTAYTQTLSDIEARIGSKAKAGQVIGNFNTLIMLRVRE
EATAELLTKQLPKVEVYTKTLVSGVTDTSNPEDGVDFTSNNEDRVSTTSVPMIEPADIISLPKGQAFALL
EGGRLWKIRMPLP
>gnl|CDD|274768 TIGR03755, conj_TIGR03755, integrating conjugative element protein, PFL_4711 family. Members of this protein family are found in genomic regions associated with conjugative transfer and integrated TOL-like plasmids. The specific function is unknown [Mobile and extrachromosomal element functions, Plasmid functions]
SDDVYYSIGGGSAVSAPPGRAGQMKAIGVGAGWRANLMCGNFDLKTTVTNQLNGITSGFKNLMGNVIQNA
TGAVASLPAMIIQRANPGLYNLLTNGVLQARLDFDRSKKTCEAMAKKMADGTDPQEGWTKLADGEAWKDA
VSTGGGDAVSAVKKVEKKNGNNGVPWVGGQKAGGSGQPPIKVVGDVVKAGYNLLNNRPVTDTSSVSASSC
SGLLCQTWPSPEEAADWAVRVLGEQEIRTCTDDCTKTSTKAGVGLTPLIEEEYDSNLEALQKLVSGATPP
TQENLAKASSPSLPITRGVIEALREDPDQSLLVQRLASEIALADTLEKALLMRRMLLTGLQEPNVAANKP
AQQEVDKAIDKLDREINNLKTELELRKELASNTALTILQRHHARRASSSPGIEQQDPDPKRLNDLRVP
>gnl|CDD|274769 TIGR03756, conj_TIGR03756, integrating conjugative element protein, PFL_4710 family. Members of this protein family are found in genomic regions associated with conjugative transfer and integrated TOL-like plasmids. The specific function is unknown [Mobile and extrachromosomal element functions, Plasmid functions]
INTATIVASTLSPSCLDYKVVGICYWLLCTPFGCKVKTSVKVRHFIPDLVVSSYNRPGGNPWVEMRALSQ
PAAGAQLYQTLYTGSAVGGGNDGGTPGNRHNNLERFKNADVIGHPAGAYFSAFASRSGYLCPSAATPFVP
YYLSTLDALAWRTGIPELLYPEALIPGLREIGIGTSTNMWGNVYPRSGFVTQPDDYKAAAVVAQRAADIV
TRTGQPHVYQPLTGSPGDGYWPPGPLVENDNNTGKWQELYPKLSSSCAVFPDSGPDKQAANGNYAWALWR
PYSCCQRRGQTFLGSTD
>gnl|CDD|163469 TIGR03757, conj_TIGR03757, integrating conjugative element protein, PFL_4709 family. Members of this protein belong to extended genomic regions that appear to be spread by conjugative transfer [Mobile and extrachromosomal element functions, Plasmid functions]
AADVVVFTDSAHPPVNATPGTRVIELDAPERLEAQLSAGLPADPQQAAAQARQRLQSPDWARLQRRLAQA
YQGVADAWQLGVTKIPAVVVDRRYVVYGETDVARALALIQQWR
>gnl|CDD|163470 TIGR03758, conj_TIGR03758, integrating conjugative element protein, PFL_4701 family. Members of this family of small, hydrophobic proteins are found occasionally on plasmids such as the Pseudomonas putida TOL (toluene catabolic) plasmid pWWO_p085. Usually, however, they are found on the bacterial main chromosome in regions flanked by markers of conjugative transfer and/or transposition [Mobile and extrachromosomal element functions, Plasmid functions]
TSAQQSAFQAASGIDPQAMNTLILGLVLAVLFLWGAWALLTAYRGWAEGKLRQRALLGSAIRVAL
>gnl|CDD|274770 TIGR03759, conj_TIGR03759, integrating conjugative element protein, PFL_4693 family. Members of this protein family, such as model protein PFL_4693 from Pseudomonas fluorescens Pf-5, belong to extended genomic regions that appear to be spread by conjugative transfer. Most members have a predicted N-terminal signal sequence. The function is unknown [Mobile and extrachromosomal element functions, Plasmid functions]
LQDSQKQRAKEWGLTEDEWQRYQQLMQGPRGVYSPGLDPLTALGIEARSDEERRRYAELWVKQEAQRVEK
ELAFQRAYDAAWQRLYPNVLPVNLFDPSGAAGPIALQGGGRLALFVKDDCVACDARVQRLLADNAPLDLY
LVGSQGDDERIRQWANRHQIDPAKVRSRQITLNHDNGRWLQLGLQGQLPAVVQQVNGGWQ
>gnl|CDD|163472 TIGR03760, ICE_TraI_Pfluor, integrating conjugative element relaxase, PFL_4751 family. Members of this protein family are the TraI putative relaxases required for transfer by a subclass of integrating conjugative elements (ICE) as found in Pseudomonas fluorescens Pf-5, and understood from study of two related ICE, SXT and R391. This model represents the N-terminal domain. Note that no homology is detected to the similarly named TraI relaxase of the F plasmid
PGYFLPLSASDLLSTPRRQQLLQQLWRNSSLSAAVYEQLYLQPLERLAELVQQLPASENHHHAYLGGLLD
HTLEVTAAAVRLSKGYLLPPGAAPEEQAAQSDAWNAAVFYAALLHDLGKLAVDIEVELQDGQRWHPWLGV
PGGPYRFRFKKERDTRLAQRLGALLAPRLLPAEALAWLSSNPEVLATLLAVLSGDYEDAGVLGEIVREAD
RKSGAQNL
>gnl|CDD|274771 TIGR03761, ICE_PFL4669, integrating conjugative element protein, PFL_4669 family. Members of this protein family, such as PFL4669, are found in integrating conjugative elements (ICE) of the PFGI-1 class as in Pseudomonas fluorescens
GSLRSEITLTLHTHHAIRLWQGRRAEEGERKPGIIGMPGFASLLNRIWQASEQDDPYADWALLRIEEKLL
SARAEMQALLERLDDLMASLPPALTLSENLSSSPVTVPLFFNTPLGYRAVYLLVDYDQLVRRVLLAHHIG
LISRQDLEDWLDKGAHLIRSLFGLAQRYRHSGVTRDDFAANNARARKAIERFGELPQDILEGTRRSSFAP
PIKRSS
>gnl|CDD|274772 TIGR03762, hypothetical_protein_ABOONEI_785, archaeosortase C, PEF-CTERM variant. Members of this family are archaeal homologs to bacterial PEP-CTERM-sorting protein exosortase (TIGR02602). Members of this family are found in species with an archaeal variant sorting motif, PEF-CTERM (TIGR03024). Members are found in the thermoacidophilic Aciduliprofundum boonei, the mesophilic psychromethanogens Methanosarcina mazei and Methanococcoides burtonii, and in Ferroglobus placidus DSM 10642 [Protein fate, Protein and peptide secretion and trafficking]
ENKYLLFILLVLALFMGYFIEYSEGSTLIGVILFLVIVVLDTQINYKKLSSKFSVGNSKVYFIIGIIIVV
ADLLYNFNPGHTLGTLDVMTVFFGASLTFYGLQNSQIRNLWEFGAYISFVFAVLYLIFYSMFTTLFIDFL
HTFDHYTILFPTVKIINLFGIPVTVGPNETVLPNGVERITMLIGGPCSGLYSMFLLIGIVIGYSLREKMK
WWATATLLGFGAIVDYIVNLIRVTILYLIAYYYGMEIMQLVHTHLGWIIFALVAVFIMYWMVIK
>gnl|CDD|163475 TIGR03763, conserved_hypothetical_protein, cyanoexosortase A. The predicted protein-sorting transpeptidase that we call exosortase (see TIGR02602) has distinct subclasses that associated with different types of exopolysaccharide production loci and/or different taxonomic lineages. We designate this relatively divergent cyanobacterial type to be type 3. We propose the gene symbol xrtC. This type coexists with a TIGR02602-recognized form in Nostoc sp. PCC 7120 [Protein fate, Protein and peptide secretion and trafficking]
IKKPVFWLLGLATGLLSIHFTLLLQAGDVAHLAMSLLFWLAALSLLWDKRQQLKLDSNILSTLLGILIIA
LVLLKSLQSPTGYYLAFSPFICAIGLMLLASGVQGLRQYWRELLILFFLGYPKLILLFLIDISKITAKFS
TFILWYLGFDVSLDGVFIQLPTGGVEVVPGCSGLEIMTYMFGIAVLFLLMFPLRTSQKLFCPVVAVLIGF
VVNGIRIALLALLVAQNDPEAFDYWHGGDGSLVFSMVSVLLFGLFCWFII
>gnl|CDD|213858 TIGR03764, ICE_PFGI_1_parB, integrating conjugative element, PFGI_1 class, ParB family protein. Members of this protein family carry the ParB-type nuclease domain and are found in integrating conjugative elements (ICE) in the same class as PFGI-1 of Pseudomonas fluorescens Pf-5
SDPISDTPMVLTLDQLRPYEDNPRTTRNPKYDEIKASIRERGLDQPPKVTRRPGESDYIIRNGGNTRLQI
LKELWQETGDERFFRIHCLFKPWPGELQALIGHLAENDLRGDLTFIEKALGVQKARALYEKELGESLSQR
ELARRLSADGYPISQSHISRMGDTVEYLYPAIPNLLYSGLGRPQIEKLLSLRKAAEKIWNRYSSGVEVDF
EEVFQEVLARFDDPEEFSLERFRDELIGEMAKALGLNYDVLLLELDPK
>gnl|CDD|274773 TIGR03765, conserved_hypothetical_protein, integrating conjugative element protein, PFL_4695 family. This model describes a protein family exemplified by PFL_4695 of Pseudomonas fluorescens Pf-5. Full-length proteins in this family show some architectural variety, but this model represents a conserved domain. Most or all member proteins belong to laterally transferred chromosomal islands called integrative conjugative elements, or ICE
MLPVRSPRLTPGKVERRPLNLPGLTPLFLIGDDPASRQWLQQNAAALKSLGAVGLVVNVETAAALQRLRA
LAPGLPLLPVSGDDLAERLGLRHYPVLITATGIEQ
>gnl|CDD|274774 TIGR03766, hypothetical_protein_lp_2141, conserved hypothetical integral membrane protein. Models TIGR03110, TIGR03111, and TIGR03112 describe a three-gene system found in several Gram-positive bacteria, where TIGR03110 (XrtG) is distantly related to a putative transpeptidase, exosortase (TIGR02602). This model describes a small clade that correlates by both gene clustering and phyletic pattern, although imperfectly, to the three gene system. Both this narrow clade, and the larger set of full-length homologous integral membrane proteins, have an especially well-conserved region near the C-terminus with an invariant tyrosine. The function is unknown
INIIFILLFSITFYFAIQSVNLNLWGISTTLIVLLLILIIFLILIIIYFWKKVKKRYRFLMRHKGVTIIV
IFVLALILQLILVTALHPLIGWDAGAVHTAATKTNESSISNYFSRNPNNLFLLLFMHFLYKLFGETSWLF
FDVVNIVLVDLSALILYKAVKKVFNKKKAFVALYLFVLLLALSPYILIPYTDTWVLPFVSLFLFLYTVIS
KKTHLRKKIALSILLGVLLAIAYFIKPSAIIFVIAIIIVLFLQLLKANNKKQILKFTLVVLIFLLSFGIT
YSILNYAISNQTYVKIDKSRAIPAIHFINMGLTGDGGYNAEDVLATLSLPTKAEKNKYSIKEIKRRLKEM
GFAGYIKFLIQKQRNNTADGTFGWLYEGVFLEPKPPKNGGFQNVIRTFLYPDGKHWSDFRFIAQFIWILS
LGIIIFAWKRNKDDKSLVLRLAIFGGFLFLLIFEGGRSRYLIQFLPFILLLSALGISQLREKI
>gnl|CDD|213859 TIGR03767, P_acnes_RR, metallophosphoesterase, PPA1498 family. This model describes a small collection of probable metallophosphoresterases, related to pfam00149 but with long inserts separating some of the shared motifs such that the homology is apparent only through multiple sequence alignment. Members of this protein family, in general, have a Sec-independent TAT (twin-arginine translocation) signal sequence, N-terminal to the region represented by this model. Members include YP_056203.1 from Propionibacterium acnes KPA171202
SGYRRLGAGPGWPSVVRTELADARAGRADRRTGLASFVQVTDVHLVDVQSPMRVEYLHPFTGSAFRPQEF
LTLHGAVALVQRVNALQGGPVTGTALDFVVSTGDNTDNAEYNELDWFLTVLDGGTIVPNSGDPDRYESVQ
DSGDPLFWNPESTPEDAYKKAGFPMIPGLLDAAIAPVTSPGLDLPWYSVFGNHDDLVQGTNPPGASDLAR
MYTGDRKLMSLDQAKATVGVKKGGDPKALSFKTMLSRIVTPDPDRAPFTPAEFIKAHLDPAATGPGPVGH
GYSEDNLSAGTGYYTFDIAGGVRGISMDTTNRAGGDEGSLGQTQFKWIKDTLRASSDTLFVLFSHHTSWS
MVNELTDPVDPGEKRHLGTELVSLLLEHPNVLAWVNGHTHSNKITAHRRVEGVGKDKGFWEINTASHIDF
PQQGRIIELADNQDGTVSIFTTLIESAAPYAWDAADLEPLGLAALYRELGANDIHARDNRLGTPSDRNTE
LLLAAP
>gnl|CDD|163480 TIGR03768, RPA4764, metallophosphoesterase, RPA4764 family. This model describes a small collection of probable metallophosphoresterases, related to pfam00149. Members of this protein family usually have a Sec-independent TAT (twin-arginine translocation) signal sequence, N-terminal to the region represented by this model. This model and TIGR03767 divide a narrow clade of pfam00149-related enzymes
NGYGEWTYGSGLPIEVRTDLMPAGYGKPASGTGKRLLRFFTISDVHITDKESPNQLIYLQQTEPAAAPNT
SIYSPVMLYSTQVLDAAVQTVNDLHKRDRFDFGISLGDACNSTQYNELRWYIDVLDGKPITPSSGAHAGA
DTIDYQKPFQAAGLDKSIPWYQVLGNHDHFWIGSFPVDGDPTVGLRSAFVGDKVWALGDVLVPNPEHFPA
LFDDRGLTATPAYYMGVLDGSTPYGTIIHAGPVDSFASPPTVVADPNRRSLLRAEWMQEFLNTSSLPKGH
GFGLIDGAGNDFACYSFVPKSDVPLKVIVLDDTQSEHDGSHDIHGHGSLDAKRWDWLKAELARGQADGQL
MIIAAHIPIAVSPIGSEMEWWLGAADANPDLQNAVSLTGLVTTLQKYPNLLMWIAGHRHLNTVKAFPSPD
PARPEYGFWQVETASLRDFPQQFRTFEIYLNSDDTVSIEAVNVDVAVAEGTPAAKSRSYAIAAQQIIGKD
KV
>gnl|CDD|274775 TIGR03769, P_ac_wall_RPT, actinobacterial surface-anchored protein domain. This model describes a repeat domain that one to three times in Actinobacterial proteins, some of which have LPXTG-type sortase recognition motifs for covalent attachment to the Gram-positive cell wall. Where it occurs with duplication in an LPXTG-anchored protein, it tends to be adjacent to the substrate-binding protein of the gene trio of an ABC transporter system, where that substrate-binding protein has a single copy of this same domain. This arrangement suggests a substrate-binding relay system, with the LPXTG protein acting as a substrate receptor
THTHANWVFTKPGTYTLTVQATATLTDGKVSSDPQTLTFAV
>gnl|CDD|163482 TIGR03770, anch_rpt_perm, anchored repeat-type ABC transporter, permease subunit. This protein family is the permease subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in the adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous permease subunits outside the scope of this family include manganese transporter MntB in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown [Transport and binding proteins, Unknown substrate]
SPIDFLTDLTNPALAFLPKALLVAVLSSIVCGVVGTHVVLRGMAFIGDAVAHAVFPGLAVAFALQGSLLL
GGAVAGVATAILIAVFSQNRRLKEDSIIGIFFVAAFALGLVIISRVPGYTGSLQQFLFGSITGIPDSDIV
VAAVVGAVVLLAVAALHKELVAVSLDRETARAMGLPVFLLDLVLYVLVTAAVVISVQTIGNILVLALLIT
PAATARLLTDRLGVMMALSPVIGGVGSFLGLYLSWSIDVPTGGTIVLVLTAVFLASWFVA
>gnl|CDD|163483 TIGR03771, anch_rpt_ABC, anchored repeat-type ABC transporter, ATP-binding subunit. This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown [Transport and binding proteins, Unknown substrate]
LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHEFAWDFPISVAH
TVMSGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEP
FTGLDMPTQELLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQLQDPAPWMTTFG
VSDSSPLLRIVGA
>gnl|CDD|163484 TIGR03772, anch_rpt_subst, anchored repeat ABC transporter, substrate-binding protein. Members of this protein family are ABC transporter permease subunits as identified by pfam00950, but additionally contain the Actinobacterial insert domain described by TIGR03769. Some homologs (lacking the insert) have been described as transporters of manganese or of chelated iron. Members of this family typically are found along with an ATP-binding cassette protein, a permease, and an LPXTG-anchored protein with two or three copies of the TIGR03769 insert that occurs just once in this protein family [Transport and binding proteins, Unknown substrate]
QVVTTTPILADLVRHVAGDRAAVTSLVPDGADPHTYEPSLRDVRDVVYADVAFSNYLLLEPHSVIKTIDA
NLPEGVPNVSLAEGAVKYGAEVIPLVENVALDTVWLGMRVRGKGARHGADRASEVHLSATSAEGPGDATA
YITGTFGNPEIYFDSTDGFDEGDTAMLPPDAHTHMSWAFSKPGIYRLSFAAQLSVDPGKVPMGEQTFTFA
VGVDPHSVPGMAAATVLDAGHADLAVDLDQQRIYLFGDPEGGGIAKQQVYDPAKTVISVPNKALQEIPGD
PRFRFLGRPGSEVYQLPQAVLGKHVHGEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYI
HRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQAYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLK
VPAVFLEPNLAARSTTLNEIADELGVRVCAIYGDTFDDDVTNYVDLMRFNADSLADCLG
>gnl|CDD|274776 TIGR03773, anch_rpt_wall, putative ABC transporter-associated repeat protein. Members of this protein family occur in genomes that contain a three-gene ABC transporter operon associated with the presence of domain TIGR03769. That domain occurs as a single-copy insert in the substrate-binding protein, and occurs in two or more copies in members of this protein family. Members of this family typically are encoded adjacent to the said transporter operon and may serve as a substrate receptor
TLRLKDSGDAAGEAVWRDPANVVLIVKEGALTAIPRTAQTAFLGNAGEKVYILPETQEQGLLWPGWSTEG
VPVKTGKNYVKINLRSVPGPGAFMAFSGGTLGKVTPLFTIGDSSKPASFKAEGPTHVHGNWGFTEPGIYE
LTVTATADLADGGAKSKPETYTVVVGKVEVDKIDPARCATGAGKPQNDANGPAADKPLFDDPASGVQALG
DESAFSPGQQATVQIGKSVRLPADAPLGVAAVVVKAAPSTGSSDAEGGLTIIETGHLDFGPQLVNDKLGS
YIKDDRSRPAVWRDPSKVVLWVKPNAKVTLPAGTEFIGKGGDTVWMLPQTQDPGVIWPGWNTMHESHAAG
VGGDVTWKLTSVDGPGQMYVFLFGNFGGVAERIFDSAGSPAGYHVPGNTHAHPNWAFSKPGTYKLQVTQS
ATTTNGKKASDTTTLTFAVGDNNDPVGAVGPLSASTPTDGAPGGKGCELAAKGAEGSGKKADKGKTGLLA
NTGLGLMALAMLLIGAGFWILGA
>gnl|CDD|163486 TIGR03774, NADH-quinone_oxidoreductase_subunit_C, Rickettsial palindromic element RPE2 domain. This model describes protein translations of a second family, RPE2, of Rickettsia palindromic elements (RPE). The elements spread within a genome as selfish genetic elements, inserting into genes additional coding regions that does not disrupt the reading frame. This model finds RPE-encoded regions in several Rickettsial species and, so far, no where else
IVNSVGFGYKERGAKPITNRRATSDDVGESKSIDY
>gnl|CDD|163487 TIGR03775, RPE3, Rickettsial palindromic element RPE3 domain. This model describes protein translations of a second family, RPE3, of Rickettsia palindromic elements (RPE). The elements spread within a genome as selfish genetic elements, inserting into genes additional coding regions that does not disrupt the reading frame. This model finds RPE-encoded regions in several Rickettsial species and, so far, no where else
IQLNSKSFRQDEFQGKPAERILVREHRQDSQNSLVSSLLNDTV
>gnl|CDD|163488 TIGR03776, RPE5, Rickettsial palindromic element RPE5 domain. This model describes protein translations of a family, RPE5, of Rickettsia palindromic elements (RPE). The elements spread within a genome as selfish genetic elements, inserting into genes additional coding region that does not disrupt the reading frame. This model finds RPE-encoded regions in several Rickettsial species and, so far, no where else
MKNCYTKFNLEKSNRSVSRGAERIIIREHPRTYKDDVANFSSS
>gnl|CDD|274777 TIGR03777, RPE4, Rickettsial palindromic element RPE4 domain. This model describes protein translations of a family, RPE4, of Rickettsia palindromic elements (RPE). The elements spread within a genome as selfish genetic elements, inserting into genes additional coding region that does not disrupt the reading frame. This model finds RPE-encoded regions in several Rickettsial species and, so far, no where else
LSSRGLTTGSSKSKNNDSISCFLDPVVKPRDD
>gnl|CDD|274778 TIGR03778, VPDSG_CTERM, VPDSG-CTERM protein sorting domain. Through in silico analysis, we previously described the PEP-CTERM/exosortase system (). This model describes a PEP-CTERM-like variant C-terminal protein sorting signal, as found at the C-terminus of twenty otherwise unrelated proteins in Verrucomicrobiae bacterium DG1235. The variant motif, VPDSG, seems an intermediate between the VPEP motif (TIGR02595) of typical exosortase systems and the classical LPXTG of sortase in Gram-positive bacteria
VPDSGSTLALLGLGLLGLLGIRRR
>gnl|CDD|274779 TIGR03779, Bac_Flav_CT_M, Bacteroides conjugative transposon TraM protein. Members of this protein family are designated TraM and are found in a proposed transfer region of a class of conjugative transposon found in the Bacteroides lineage [Cellular processes, DNA transformation]
EKQKRKKLLVLPLMGLVFLGSLWLIFAPSEEEDAAEEETKGFNADIPQPKDEGIIGDKMKAYEQEALEQK
QKDKKRTLQDLADSFEKSDKESQDESSSDSGFDEEPDEPAETAGSLRPIRSSAAAYRDINRELGSFYEYP
KTDEEKELLREVEELESRLATEPSPAPELEEQLALMEKSYELAAKYMPRGQERLPVAPESKKGKKPSVQP
VRAVEEKAVSSLQQPMSDAEFVAEYSKPRNRGFNTAVGSGEVSERNTIRACVHETQTVVDGSAVKLRLLE
PIQAGDLVIPKGTVLYGTAKIQGERLDIKISSIEYNGTILPVELSVYDTDGQEGIYVPGSAERDAAKEVA
ANMGGSLGTSISFATSAGAQWAADAARGVIQGTSQYLSKKIRTVKVTLKAGYQVLLVSKK
>gnl|CDD|163492 TIGR03780, Bac_Flav_CT_N, Bacteroides conjugative transposon TraN protein. Members of this family are the TraN protein encoded by transfer region genes of conjugative transposons of Bacteroides. The family is related to conjugative transfer proteins VirB9 and TrbG of Agrobacterium Ti plasmids [Cellular processes, DNA transformation]
MKKIFGIMLASLLGVLASNAQQEGLNRKLTYENMIQPKGLEITYDKTTHIIFPSPIKYVDLGSNDIIADK
ADGAENVLRVKAAKEGFEGETNLSVITEDGRFYVFNLNYADEPKDLNTEMEDFLADGDTVDYLNELGNES
PALVELIMKRIYKNSKRKIRHIGCKKFGIQFLLNGIYTHNDLLYFHTSLENKTNIPFDIDFIRFKIVDKK
KAKRTAMQEIEIDPLRVYNSVIVIAGKSTYRTVYVLPKFTIPDDKLLTIEMYEKNGGRHQTLRIDNEDLL
KADPI
>gnl|CDD|200324 TIGR03781, Bac_Flav_CT_K, Bacteroides conjugative transposon TraK protein. Members of this protein family are designated TraK and are found in a proposed transfer region of a class of conjugative transposon found in the Bacteroides lineage. PSI-BLAST reveals a distant relationship to proteins TrbF and VirB8 in Proteobacterial conjugal transfer systems [Cellular processes, DNA transformation]
LKNIETSFRQIRLFAIAFVALCILITGYALWSSYSFAEAQRKKIYVLDNGKSLMLALSQDLSQNRPVEAK
EHVRRFHELFFTLSPDKKAIEYNIERALYLADKSAFNYYKDLKEKGYYNRIISGNINQTIEIDSVKCDFN
NYPYKVRTYARQRIERESNITERSLVTRCRLLNAVRSDNNPHGFIIENFTILENKDLQTIKR
>gnl|CDD|274780 TIGR03782, Bac_Flav_CT_J, Bacteroides conjugative transposon TraJ protein. Members of this protein family are designated TraM and are found in a proposed transfer region of a class of conjugative transposon found in the Bacteroides lineage. This family is related conjugation system proteins in the Proteobacteria, including TrbL of Agrobacterium Ti plasmids and VirB6 [Cellular processes, DNA transformation]
DFDNLHEVLRSLYDEMMPLCSDMTGVAKGIAGLGALFYVALRVWQSLARAEPIDVYPLLRPFALGLCIMF
FPTFVLGTINGVLSPVVQGTHSMLEGQTLDMNRYREQKDKLEYEAMVRDPETAYLVSDEEFDRKLDELGW
SPSDMKTMAGMYMERAAYNMKKSVRDWFRELLELLFQAAALVIDTLRTFFLIVLSILGPIAFAISVYDGF
QSTLTQWITRYISIYLWLPVSDLFSSILARIQVLMLQKDIAQLQDPNFIPDSSNSVYIIFMIIGIIGYFT
VPTVSGWIIQAGGGGNYGRNVNSTAMKAGSAAAAVAGAAMGNA
>gnl|CDD|163495 TIGR03783, Bac_Flav_CT_G, Bacteroides conjugation system ATPase, TraG family. Members of this family include the predicted ATPase, TraG, encoded by transfer region genes of conjugative transposons of Bacteroides, such as CTnDOT, found on the main chromosome. Members also include TraG homologs borne on plasmids in Bacteroides. The protein family is related to the conjugative transfer system ATPase VirB4 [Cellular processes, DNA transformation]
MRNVLKATTLESRFPLLAVENGCIVSKDADITVAFRVELPELFTVTSAEYEAIHSAWHKAVKVLPEYSIV
HKQDWFIKENYRPELDKEDLSFLSRSFERHFNERPFLNHRCYLFLTKTTKERSRQQSNFSTLCRGTLLPK
EVRDKDTVRRFLEAVEQFERIMNDSGFIRLRRLTTDEITGTDERPGLVEKYLSLSLEDTTVLEDIQLGAE
QMRIGDKRLCLHTLSDTEDLPGKVATDMRYERLSTDRSDCRLSFAAPVGLLLPCNHIYNQYLFIDDSEEN
LQRFEKSARNMHSLSRYSRSNQINKEWIEEYLNEAHSKGLTSVRCHCNVMAWSDDREELRRIKNDVGSQL
ALMECKPRHNTVDVPTLYWAGIPGNAGDFPAEESFYTFIEQALCLFTEETNYRSSLSPFGIKMADRLTGK
PLHLDISDLPMKRGIITNRNKFILGPSGSGKSFFTNHLVRQYYEQGTHILLVDTGNSYQGLCELIHRKTR
GEDGIYFTYTEENPIAFNPFYTDDGVFDVEKRESIKTLILTLWKREDEPPTRSEEVALSNAVSAYIRLIS
EDRGIAPSFNTFYEYVKDDYRAELEEKKVREKDFDIDNFLNVLEPYYKGGEYDFLLNSDKQLDLLHKRFI
VFEIDAIKDNKILFPVVTIIIMEAFINKMRRLKGVRKMILIEEAWKAIASANMAEYIKYLYKTVRKYFGE
AIVVTQEVDDIISSPIVKESIINNSDCKILLDQRKYMNKFDQIQALLGLTDKEKSQILSINMANHPGRLY
KEVWIGLGGTQSAVYATEVSAEEYLTYTTEETEKMEVLALAEELGGNLELAIRHLAETK
>gnl|CDD|163496 TIGR03784, marine_sortase, sortase, marine proteobacterial type. Members of this protein family are sortase enzymes, cysteine transpeptidases involved in protein sorting activities. Members of this family tend to be found in proteobacteria, rather than in Gram-positive bacteria where sortases attach proteins to the Gram-positive cell wall or participate in pilin cross-linking. Many species with this sortase appear to contain a signal target sequence, a protein with a Vault protein inter-alpha-trypsin domain (pfam08487) and a von Willebrand factor type A domain (pfam00092), encoded by an adjacent gene. These sortases are designated subfamily 6 according to Comfort and Clubb (2004)
LLVAGLLLCGNGAYMQAKAWLAQVLIEQAWAQTLADGKEHKPWPWADTYPVAKLSAPRLGASLYVLAGAS
GRNLAFGPGHMLATAQPGAQGNSVIAGHRDTHFAFLQELRPGDVIRLQTPDGQWQSYQVTATRVVDESET
GLDLPADDSQLVLITCYPFDALGSGGPLRYVVEA
>gnl|CDD|163497 TIGR03785, marine_sort_HK, proteobacterial dedicated sortase system histidine kinase. This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase
LRRKLLLLSLFLLLLPWAGYQYVWEMEKYLRQGQEQTLVGTARALATALHERPALFDTQASFLGQVKGGR
DLYAYPLDTAIYLDGYLDDWPEYQHRFQQYGQLQTAGKPKPLSLSFTHMVGKYDQYLYLLFQVTDNRLQY
RGPNARSIQNNDHLEIALLAPDGQFQRYIVATEQPGWISAFRLPENPRKAPEHRIQGHWLETGAGYNIEL
RLPLAMLGSKLGFAITDVDDSKARVINAIIGTRNGNDVEKLGTVLVPSPEIENILKGMSHTGSRIWVVDQ
HARVLASSGDLNSSIGVWAKTLKEQHPDSWWQQFEQQYLHPLYYKILTKPPADFIDQLQDSQALEGSHII
KALQGQPASTWRLSPDSKAVILSAAYPIWIDTEVLGAVIAEQTTNGIRTLRNSALEKLFNVILAIMSIGT
LALFGFASWISWRIRRLSDDAEAAIDSQGRISGAIPASRSRDEIGDLSRSFAQMVARLRQYTHYLENMSS
RLSHELRTPVAVVRSSLENLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDL
SEVLSGCMQGYQMTYPPQRFELNIPETPLVMRGSPELIAQMLDKLVDNAREFSPEDGLIEVGLSQNKSHA
LLTVSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQQNDGVVFRI
SLP
>gnl|CDD|274781 TIGR03786, strep_pil_rpt, streptococcal pilin isopeptide linkage domain. This model describes a domain that occurs once in the major pilin of Streptococcus pyogenes, Spy0128, but in higher copy numbers in other streptococcal proteins. The domain occurs nine times in a surface-anchored protein of Bifidobacterium longum. All members of this family have LPXTG-type sortase target sequences. The S. pyogenes major pilin has been shown to undergo isopeptide bond cross-linking, mediated by sortases, that are critical to maintaining pilus structural integrity. One such Lys-to-Asn isopeptide bond is to a near-invariant Asn near the C-terminal end of this domain (column 81 of the seed alignment). A Glu in the S. pyogenes major pilin (column 25 of the seed alignment), invariant as Glu or Gln, is described as catalytic for isopeptide bond formation
FSPLTFTKVGTYTYTVTEVKGKEPGVTYDTTVHTVTVTVTDDEQGKLVATVIYDKEKNPITFT
>gnl|CDD|163499 TIGR03787, marine_sort_RR, proteobacterial dedicated sortase system response regulator. This model describes a family of DNA-binding response regulator proteins, associated with an adjacent histidine kinase (TIGR03785) to form a two-component system. This system co-occurs with, and often is adjacent to, a proteobacterial variant form of the protein sorting transpeptidase called sortase (TIGR03784), and a single target protein for the sortase. We give this protein the gene symbol pdsR, for Proteobacterial Dedicated Sortase system Response regulator
KRIAIVEDEAAIRENYADALKRQGYQVTTYADRPSAMQAFRQRLPDLAIIDIGLGEEIDGGFMLCQDLRS
LSATLPIIFLTARDSDFDTVSGLRLGADDYLTKDISLPHLLARITALFRRAEALQKPQKQDDLITRGPLT
LDSDRMTVFWQDQPIDLTVTEFWMVHALAKHPGHVKSRQQLMDAAKIVVDDSTITSHIKRIRKKFQAVDD
NFDCIQTVYGMGYRWDS
>gnl|CDD|274782 TIGR03788, marine_srt_targ, marine proteobacterial sortase target protein. Members of this protein family are restricted to the Proteobacteria. Each contains a C-terminal sortase-recognition motif, transmembrane domain, and basic residues cluster at the the C-terminus, and is encoded adjacent to a sortase gene. This protein is frequently the only sortase target in its genome, which is as unusual its occurrence in Gram-negative rather than Gram-positive genomes. Many bacteria with this system are marine. In addition to the LPXTG signal, members carry a vault protein inter-alpha-trypsin inhibitor domain (pfam08487) and a von Willebrand factor type A domain (pfam00092)
LDTDANITVTGLIARTEVTQTFRNPSQFWVEGRYVFPLPENAAVDSLTMHIGERVIVGQIMPKAAARAIY
EQAKAEGKKAALVEQQRPNLFTNKVANIGPGETVVVTIEYQQPVSYSSGTFSLRLPLTVTPRYIPGSTVN
TVTDVNNSGWAIPTTQVPDADKISAPRVLDPDDDAPSSQASINVDLNAGLPLDSITSPSHPIQIEQQGQS
GYTISLAQGQVIADRDFVLTWRPAQGEAPSAALFREQIGGERYGLAMVMPPTEAAVAQVLPRELVFVIDT
SGSMAGESIEQAKSALLLALDQLRPGDRFNIIQFDSDVTLLFPVPVPATAHNLARARQFVAGLQADGGTE
MAGALSAALRDDGPESSGALRQVVFLTDGAVGNEDALFQLIRTKLGDSRLFTVGIGSAPNSYFMRKAAQF
GRGSFTFIGSTDEVQRKMSQLFAKLEQPALTDIALTFDNGNAADVYPSPIPDLYRGEPLQIAIKLQQAAG
ELQLTGRTGSQPWSQQLDLDSAAPGKGIDKLWARRKIDSLEDSLRYGANEEKVKDQVTALALNHHLVSPF
TSFVAVEETPIRPAAESLNSEASPNNLPAGWSPGLV
>gnl|CDD|274783 TIGR03789, pdsO, proteobacterial sortase system peptidoglycan-associated protein. A newly defined histidine kinase (TIGR03785) and response regulator (TIGR03787) gene pair occurs exclusively in Proteobacteria, mostly of marine origin, nearly all of which contain a subfamily 6 sortase (TIGR03784) and its single dedicated target protein (TIGR03788) adjacent to to the sortase. This protein family shows up in only in those species with the histidine kinase/response regulator gene pair, and often adjacent to that pair. It belongs to the pfam00691 domain family, which is the peptidoglycan-associated region of flagellar motor protein MotB, OmpA (whose N-terminal region forms an outer membrane beta barrel), and peptidoglycan-associated lipoprotein Pal. Its function is unknown. We assign the gene symbol pdsO, for Proteobacterial Dedicated Sortase system OmpA family protein [Protein fate, Protein and peptide secretion and trafficking]
KKTIIALLLAALFTSSVAATTYQNQPHLQTPQETEQQEADQEALIGLGSGALLGALVGGPVGAIIGGITG
GLIGQAVNNDETLKQQQQHIAQQRQQMVALTQKQQALEQLEAEYQQAQVHLETLQQDQQQLLEELALGMN
VQFRTGSSDIEPHFQPQLDEVATLMKQSPELKLDLSGYADRRGDSQYNQALSEQRVLEVRSYLIKQGVDE
ARLTTQAFGESAPLKDEQESESDFFDRRVTLTL
>gnl|CDD|274784 TIGR03790, conserved_hypothetical_protein, TIGR03790 family protein. Despite a broad and sporadic distribution (Cyanobacteria, Verrucomicrobia, Acidobacteria, beta and delta Proteobacteria, and Planctomycetes), this uncharacterized protein family occurs only among the roughly 8 percent of prokarotyic species that carry homologs of the integral membrane protein exosortase (see TIGR02602), a proposed protein-sorting system transpeptidase
DEVAVVVNGADPESVQIARYYAEKRGIPEENLITLDLPPKETISREEFFQQIKEPLRAYLVENRWWKLQG
RAVGAVLGARIRVLVLTWGVPLRVAGDPGLGSTNCASVDSELALLFDRGYCRKGCLPNPYFNSDSAQPFP
DHGIRLVMRLDAPSFATAKALIDRGLAAEKTGLAGRAYVDAGGGYKDGDRWLRAAAFALRRKGLPVVVDD
TPGLFPRDFPQDVALYFGWYSTGLYGPFRLPTFRFVPGAIADHLTSFSAATLRSSQMSWSLPLLEAGATA
TYGNVYEPYLQKFPRPDVFLDRLLQGATLAEAYWKSLPVVSW
>gnl|CDD|163503 TIGR03791, TTQ_mauG, tryptophan tryptophylquinone biosynthesis enzyme MauG. Members of this protein family are the tryptophan tryptophylquinone biosynthesis (TTQ) enzyme MauG, as found in Methylobacterium extorquens and related species. This protein is required to complete the maturation of the TTQ cofactor in the methylamine dehydrogenase light (beta) chain
LTIEKAALGKALFFDPRLSRDGSMSCATCHNPGLGWSDGLILALGADGVEHARRTPPVLNLAWGTAFMWD
GRADSLEAQAILPITAADEMNFEMDLLLERLKAVAGYAPLFANAFGDAEPIGAKHLTAALASFQRTLVSG
EAPFDRWAEGDESAIGADAKRGFALFKGKAGCAACHSSWRFTDDSFHDIGLKAGLDLGRGAFAPPQVTAM
QHAFKTPSLRDLPMEGPFMHDGQLGSLDAVIDHYEKGGEKRPSISAEMKPFELSEREREDLIAFIETLDA
ELAAIELPQLP
>gnl|CDD|274785 TIGR03792, conserved_hypothetical_protein, uncharacterized cyanobacterial protein, TIGR03792 family. Members of this family are found, no more than one to a genome, exclusively in (but not universal to) the Cyanobacteria. These proteins are small, 100-150 amino acids. The function is unknown [Unknown function, General]
VIEWLRFKVPPEDREAFLEADEEIWTPWLAKQPGFLGKEVWWDPEKPEEGVLLIRWESREQWKAIPQEEL
EAVEQRFEQAMGGNPYPLIE
>gnl|CDD|274786 TIGR03793, TOMM_pelo, NHLP leader peptide domain. This model represents a domain that is conserved among a large number of putative ribosomal natural products (RNP) precursor, including the thiazole/oxazole-modified microcins (TOMMs). As a leader peptide domain, likely to be removed from the mature product, this domain is unusual in several ways. First, it is longer than most previously described RNP leader peptides. Second, most of the domain is homologous to nitrile hydratase alpha subunits. Finally, it appears that this domain correlates with a specific family of cleavage/export proteins while members undergo modifications by different classes of peptide maturase, including cyclodehydratases, lantibiotic synthases, radical SAM peptide maturases. This family is expanded especially in Pelotomaculum thermopropionicum SI [Cellular processes, Biosynthesis of natural products]
TRKEFEEKIIAKAWEDEAFKQALLTNPKEALEREGVQVPAEVEVKVVEESPTVLYLVLPVNPDGELTDEQ
LDAVAGG
>gnl|CDD|274787 TIGR03794, conserved_hypothetical_protein, NHLM bacteriocin system secretion protein. Members of this protein family are homologs of the HlyD membrane fusion protein of type I secretion systems. Their occurrence in prokaryotic genomes is associated with the occurrence of a novel class of microcin (small bacteriocins) with a leader peptide region related to nitrile hydratase. We designate the class of bacteriocin as Nitrile Hydratase Leader Microcin, or NHLM. This family, therefore, is designated as NHLM bacteriocin system secretion protein. Some but not all NHLM-class putative microcins belong to the TOMM (thiazole/oxazole modified microcin) class as assessed by the presence of the scaffolding protein and/or cyclodehydratase in the same gene clusters [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
RLSSPDQLDQLVQVVSPRSWLALAALGVIVVAALAWGIFGSIPITVSGNGILILSSGVDTIQSPGSGVVI
DLDVEVGDQVKKGQVVARLFQPELRERLQESYQKLTQLQEQLEEVRNYTGRLKEGRERHFQKSKEALEET
IGRLREELAALSREVGKQRGLLSRGLATFKRDRILQQQWREEQAKYDAADKARAIYALQTKADERNLETV
LQSLSQADFQLAGVAQQELETVEARIKEARYEIEELENKLNLNTRIVSQHSGRVIELNYTPGQLVAAGAP
LASLEVEDQTDEGLEGVAYFPVAEGKKIRPGMSVQITPSTVKAERDGYIRGTVTSVSEYPATKEAMDRTL
GNEAFVQYLLAQGPPIEVFVALERDRSSPSGFKWSSGSGPDIKISAGTLCSASVVVEKERPITLVFPGLR
K
>gnl|CDD|163507 TIGR03795, RNP_Burkhold, ribosomal natural product, two-chain TOMM family. Members of this protein family are found sparsely, mostly in members of the genus Burkholderia. Members often occur as tandem homologous genes, such as BMA_0021 and BMA_0022 in Burkholderia mallei ATCC 23344, or else have a duplication. The genes regularly are encoded near a cyclodehydrogenase/docking protein fusion protein of TOMM (thiazole/oxazole-modified microcins) biosynthetic clusters, suggesting a role in bacteriocin biosynthesis. The role of the putative natural product is unknown, but function as a two-chain bacteriocin is suggested [Cellular processes, Biosynthesis of natural products]
DNAVPTYESLLEFRAVYLRAIALAWHSPEFKDELLADPVDALEKYFDYRCPWILDLKVTENSSDWTPYGW
GAWTQGRWNLPVNRLTLGIPPAPEHLAEEAIALAAYNDAGPAYL
>gnl|CDD|274788 TIGR03796, ABC_transporter_related, NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein. This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
RTPTVLQMEAVECGAASLAMILAYYGRYVPLEELREECGVSRDGSKASNLLKAARSYGLEAKGFRKELDA
LAELPLPYIVFWNFNHFVVVEGFRGGRVYLNDPALGPRTVSLEEFDESFTGVVLTFEPGPEFQKGGRKPS
LLRALWRRLRGSRGALLYLLLAGLLLVLPGLVIPAFSQIFVDEILVQGRQDWLRPLLLGMGLTALLQGVL
TWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLNDQVAEFLSGQLATTALDAVM
LVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGL
ESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMS
SFLEPVNNLVGFGGTLQELEGDLNRLDDVLRNPVDPLLEEPEGSAATSEPPRRLSGYVELRNITFGYSPL
EPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQ
DIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARAL
VRNPSILILDEATSALDPETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWA
VGGAYARLIR
>gnl|CDD|274789 TIGR03797, ABC_transporter_related, NHLM bacteriocin system ABC transporter, ATP-binding protein. Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
GDPLLVACGAVGRAMGIEIRPPARSENLERRKDPLEAIARASRLRIRRVRLEGGWWRQDSGPLLAYTAED
GRPVALLPVSRGGYEIFDPATGTRRRVDAAMAATLAPEAYMFYRPLPDKALGLRDLLRFALRGARRDLLA
ILAMGLLGTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDAS
LQAAVWDRLLRLPVSFFRQYSTGDLASRAMGISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALV
AVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKL
ELSAQRIENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILA
VIPLWERAKPILEALPEVDEAKTDPGKLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGS
GKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWE
AARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSES
LERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQL
>gnl|CDD|274790 TIGR03798, ocin_TIGR03798, nif11-like leader peptide domain. This model describes a conserved, fairly long (about 65 residue) leader peptide region for a family of putative ribosomal natural products (RNP) of small size. Members of the seed alignment tend to have the Gly-Gly motif as the last two residues of the matched region. This is a cleavage site for a combination processing/export ABC transporter with a peptidase domain. Members include the prochlorosins, lantipeptides from Prochlorococcus [Cellular processes, Biosynthesis of natural products]
EEQLKAFLEKVKTDPDLREKLKAAEDPEDRVAIAKEAGFEFTGEDLKEAGEELSDEELEAVAGG
>gnl|CDD|274791 TIGR03799, NOD_PanD_pyr, putative pyridoxal-dependent aspartate 1-decarboxylase. This enzyme is proposed here to be a form of aspartate 1-decarboxylase, pyridoxal-dependent, that represents a non-orthologous displacement to the more widely distributed pyruvoyl-dependent form (TIGR00223). Aspartate 1-decarboxylase makes beta-alanine, used usually in pathothenate biosynthesis, by decarboxylation from asparatate. A number of species with the PanB and PanC enzymes, however, lack PanD. This protein family occurs in a number of Proteobacteria that lack PanD. This enzyme family appears to be a pyridoxal-dependent enzyme (see pfam00282). The family was identified by Partial Phylogenetic Profiling; members in Geobacter sulfurreducens, G. metallireducens, and Pseudoalteromonas atlantica are clustered with the genes for PanB and PanC. We suggest the gene symbol panP (panthothenate biosynthesis enzyme, Pyridoxal-dependent) [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
RSADASLESLLRIFTVPEAPDSTLGRIEQEISENLAGFLGEHIVAIEKPLHEIEKDFSSAEIPEQPTFVS
DHTQHLLDKLVAHSVHTASPSFIGHMTSALPYFLLPLSKLMVGLNQNLVKIETSKAFTPLERQVLGMMHH
LVYQQDDSFYRRWMHSADHSLGAFCSGGTVANITALWVARNRLLKADGDFRGIAREGLFAALRHYGYDGL
AILVSERGHYSLGKAADVLGIGRDNLVPVKTDENNRIRVDALRDKCLELAAQNIKPMAIVGVAGTTETGN
IDPLDEMADIAQEAGCHFHVDAAWGGATLLSNTYRHLLKGIERADSVTIDAHKQMYVPMGAGMVLFKDPA
LTSAIEHHAEYILRKGSKDLGSHTLEGSRPGMAMLVYACLHIIGRKGYEMLINQSIDKAHYFANLIDQQP
DFELVTEPELCLLTYRYVPENVKAALAIADEEQREKINDALNALTKFIQKRQRETGKSFVSRTRLTPAQY
DHQPTIVFRVVLANPLTTHEILQDILIEQREL
>gnl|CDD|274792 TIGR03800, PLP_synth_Pdx2, pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2. Pyridoxal 5'-phosphate (PLP) is synthesized by the PdxA/PdxJ pathway in some species (mostly within the gamma subdivision of the proteobacteria) and by the Pdx1/Pdx2 pathway in most other organisms. This family describes Pdx2, the glutaminase subunit of the PLP synthase [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
KIGVLALQGAVREHARALEALGVEGVEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNFILSG
LPVFGTCAGLIMLAKEIIGQKEGQLGLLDMTVERNAYGRQVDSFEAEVDIKGVGDDPITGVFIRAPKIVS
VGNGVEILAKVGNRIVAVRQGNILVSSFHPELTDDHRVHEYFLE
>gnl|CDD|163513 TIGR03801, For_A_Pyridoxal-5-_Phosphate, aspartate 4-decarboxylase. This enzyme, aspartate 4-decarboxylase (EC 4.1.1.12), removes the side-chain carboxylate from L-aspartate, converting it to L-alanine plus carbon dioxide. It is a PLP-dependent enzyme, homologous to aspartate aminotransferase (EC 2.6.1.1) [Energy metabolism, Amino acids and amines]
LSPFELKDELIKLAKSTKKSDRTMLNAGRGNPNWTATTPREAFFLLGQFAVEETRRSWSYPGGLGGMPQK
EGIEERFETFLAENKSQPGAEFLRDIISYVIDQLGFDPDAFLYEMCDGIIGDNYPVPDRMLPHSEKIVHQ
YLIQEMCGNKPPPGEFDLFAVEGGTAAMCYIFDSLKANELLKKGDKIALMTPIFTPYLEIPELPRYDFEV
VRIKADEMTEDGTHTWQYPDKELEKLRDPSIKALFVVNPSNPPSVAMSDESIEKIVDIVANDRPDLMILT
DDVYGTFVDDFRSLFAELPYNTIGVYSFSKYFGATGWRLGTIALHKDNIFDKLIAELPEEKKKELDKRYS
SLTTEPRKLKFIDRLVADSRQVALNHTAGLSTPQQVQMALFSLFALMDKENAYKAETKDICRRREKLLFR
GLGLPLQEDPNDVAYYTLIDLEEWAEKNYGEEFSSYLKKNYSPVDVLFRLAEETGIVLLPGGGFGGPEWS
VRVSLANLNEYDYAEIGRAIRKILDEYYEAW
>gnl|CDD|274793 TIGR03802, Asp_Ala_antiprt, aspartate-alanine antiporter. All members of the seed alignment for this model are asparate-alanine anti-transporters (AspT) encoded next to the gene for aspartate 4-decarboxylase (AspD), which converts asparate to alanine, releasing CO2. The exchange of Asp for Ala is electrogenic, so the AspD/AspT system confers a proton-motive force. This transporter contains two copies of the AspT/YidE/YbjL antiporter duplication domain (TIGR01625)
EWLHNLLRSNPEIALFLSLALGYLIGKIKFGSFQLGGVAGSLIVAVLIGQLGIQIDPDVKAVFFALFIFA
IGYEVGPQFFASLKKDGLREIILALVFAVSGLITVYALAKIFGLDKGTAAGLAAGGLTQSAVIGTAGDAI
EKLGLSPEQKTAYQGNVAVAYAVTYIFGTIGVIIVLVNILPWLMGIDLREAAKKLEAELHGGNDVLGVGQ
SAALPELVGRAYRVNRASSLIGKTVGDLENLFADRVTIERIRRDGKLLTVSPDLVLNAGDVVLVVGRRDA
VVQFGAEIGEEVQEVEGLDVPMETKDVVLTNKEYNGKTVAEILKNAQDKFRHGVYVEKIKRDDQKLPILP
ETVLQRGDVVTLVGTPQDVDRAAKQLGYAIAPTDKTDFVFLGLGIVLGLLIGAIVVKIGSIPLTLGTGGG
ALISGLVFGWLRSKHPTFGNIPSSASWLLKDLGLALFIAVVGLSAGPQAVTAIKEMGLTLFLLGIVVTIL
PLIITMLIGKYVLKYDPALLLGALAGARTATPALGAVLERAGSSVPALGYTITYALGNVLLTLLGPLIVA
LL
>gnl|CDD|274794 TIGR03803, hypothetical_protein_CfE428DRAFT_0741, Gloeo_Verruco repeat. This model describes a rare protein repeat, found so far in two species of Verrucomicrobia (Chthoniobacter flavus and Verrucomicrobium spinosum) and in four different proteins of Gloeobacter violaceus PCC7421. In the Verrucomicrobial species, the repeat region is followed by a PEP-CTERM protein-sorting signal, suggesting an extracellular location
DGTLYGTTSGGGASGFGTLYRLDPAGGFTTLHSF
>gnl|CDD|274795 TIGR03804, para_beta_helix, parallel beta-helix repeat (two copies). This model represents a tandem pair of an approximately 22-amino acid (each) repeat homologous to the beta-strand repeats that stack in a right-handed parallel beta-helix in the periplasmic C-5 mannuronan epimerase, AlgA, of Pseudomonas aeruginosa. A homology domain consisting of a longer tandem array of these repeats is described in the SMART database as CASH (SM00722), and is found in many carbohydrate-binding proteins and sugar hydrolases. A single repeat is represented by SM00710. This TIGRFAMs model represents a flavor of the parallel beta-helix-forming repeat based on prokaryotic sequences only in its seed alignment, although it also finds many eukaryotic sequences
GIYLESSSNNTLSNNTASNNSYGIYLYDSSNNTLSNNTASNNGY
>gnl|CDD|163517 TIGR03805, beta_helix_1, parallel beta-helix repeat-containing protein. Members of this protein family contain a tandem pair of beta-helix repeats (see TIGR03804). Each repeat is expected to consist of three beta strands that form a single turn as they form a right-handed helix of stacked beta-structure. Member proteinsa occur regularly in two-gene pairs along with another uncharacterized protein family; both protein families exhibit either lipoprotein or regular signal peptides, suggesting transit through the plasma membrane, and the two may be fused. The function of the pair is unknown [Unknown function, General]
LQEALIAAQPGDTIVLPEGVFQFDRTLSLDADGVTIRGAGMDETILDFSGQVGGAEGLLVTSDDVTLSDL
AVENTKGDGVKVKGSDGIIIRRLRVEWTGGPKSSNGAYGIYPVESTNVLVEDSYVRGASDAGIYVGQSQN
IVVRNNVAEENVAGIEIENSQNADVYNNIATNNTGGILVFDLPGLPQPGGSNVRVFDNIIFDNNTPNFAP
AGSIVASVPAGTGVVVMANRDVEIFGNVISNNDTANVLISSYHSTGLPDQPPDDGFDPYPRNISIHDNTF
SDGGTNPDGLDLQALAQALAALGGALPDVLWDGV
>gnl|CDD|163518 TIGR03806, chp_HNE_0200, conserved hypothetical protein, HNE_0200 family. The model TIGR03805 describes an uncharacterized protein family that contains repeats associated with the formation of a right-handed helical stack of parallel beta strands, homologous to those found in a number of carbohydrate-binding proteins and sugar hydrolases. This model describes another uncharacterized protein family, found in the same species as TIGR03805 member proteins, usually as the adjacent gene or in a fusion protein. An example is HNE_0200 from Hyphomonas neptunium ATCC 15444. Sometimes two members of this family are with a single member of TIGR03805. The function is unknown [Hypothetical proteins, Conserved]
PPPKLSDYGLFSPANNTLQPAAGVIPYDLNTPLFSDYADKYRFVYVPAGTSATYNAEGVLDFPVGTVLVK
TFALPSDLRGPTNGRLIETRLLIRRAQGWAALPYVWNEAQTDATLANAGKVVALSLVDPDGEGQTFTYLV
PSRNQCKQCHQLAADIVPLGPKARQLNREYDYPGGAINQLQRWTEAGILSGLPDLALVPRMPAWSDPDDG
TLAQRARAYLDVNCAHCHNPGGLASNSGLDLRFDDPLGYTLGVCKQPVAAGGGSGGLKYDIVPGDPEKSI
LLYRMHSTEPGVRMPELGRSLVHQEGLALIRQWIASL
>gnl|CDD|213864 TIGR03807, RR_fam_repeat, putative cofactor-binding repeat. This model describes a small repeat found in a family of proteins that crosses the plasma membrane by twin-arginine translation, which usually signifies the presence of a bound cofactor. This repeat shows similarity to the beta-helical repeat, in which three beta-strands per repeat wind once per repeat around in a right-handed helical stack of parallel beta structure
SVDNVAGWGIYLEFDAVVTGNVIRNAG
>gnl|CDD|163520 TIGR03808, RR_plus_rpt_1, twin-arg-translocated uncharacterized repeat protein. Members of this protein family have a Sec-independent twin-arginine tranlocation (TAT) signal sequence, which enables tranfer of proteins folded around prosthetic groups to cross the plasma membrane. These proteins have four copies of a repeat of about 23 amino acids that resembles the beta-helix repeat. Beta-helix refers to a structural motif in which successive beta strands wind around to stack parallel in a right-handed helix, as in AlgG and related enzymes of carbohydrate metabolism. The twin-arginine motif suggests that members of this protein family bind some unknown cofactor
MDLNRRRLLGASAAGAAGALALPSAAARAAPLTSTLGRDATQYGVRPNSPDDQTRALQRAIDEAARAQTP
LALPPGVYRTGPLRLPSGAQLIGVRGATRLVFTGGPSLLSSEGADGIGLSGLTLDGGGIPLPQRRGLIHC
QGGRDVRITDCEITGSGGNGIWLETVSGDISGNTITQIAVTAIVSFDALGLIVARNTIIGANDNGIEILR
SAIGDDGTIVTDNRIEDIKAGPGGSGQYGNAINAFRAGNVIVRGNRIRNCDYSAVRGNSASNIQITGNSV
SDVREVALYSEFAFEGAVIANNTVDGAAVGVSVCNFNEGGRLAVVQGNIIRNLIPKRPIGTAPDDDAGIG
IYVEADTAVTGNVVENAPSFGIVAGWGKYLRDVAISGNVIRNAFVGIGVSVVDGAGTALVNNNVISETPR
GAVVGLDHAKPVTPDLAAPGAAKFAQVVLGGNAVR
>gnl|CDD|163521 TIGR03809, TIGR03809, TIGR03809 family protein. This protein family contains proteins with a median length of about 175, including a strongly conserved N-terminal region of about 55 amino acids, a conserved extreme C-terminal region of about 15 amino acids, and highly variable sequence in between the two. Members are found invariably with a member of family TIGR03808
GRAIVERWCVLAEQRLDYLTELFESGRWRRYHSELAFLENIQEAKAAVETWRGLATREATPDNRPVDLSW
LGRNKKLPPRAPFYAADETVEPRRFAPPAALPASAPAIVALPEEAAAEPRAAPDVPAEPNDASDADVAEV
AEPDVVPEWQHALDLDQLQQRYPLLRKA
>gnl|CDD|163522 TIGR03810, arginine-ornithine_antiporter, arginine-ornithine antiporter. Members of this protein family are the arginine/ornithine antiporter, ArcD. This exchanger of ornithine for arginine occurs in a system with arginine deiminase, ornithine carbamoyltransferase, and carbamate kinase, with together turn arginine to ornithine with the generation of ATP and release of CO2 [Transport and binding proteins, Amino acids, peptides and amines]
KKLGLGALTALVVGSMIGSGIFSLPSDMAAGAAAGAVLIGWVITGVGMLALAFSFQNLANKKPELDGGVY
SYAKAGFGPFMGFISAWGYWLSAWLGNVAYATLLFSTLGYFFPIFGGGNNPPSIIGASVLLWCVHFLVLR
GVEGAAFINTITTIAKLVPLFVFIVIGIFAFKGDTFTNDFWGNANGGFSLGSVMTQVKNMMLVTVWVFIG
IEGASMLSARAEKRSDVGKATVIGLIGVLAIYVLVSVLSYGIMTQAQLAGLKNPSMAYVLEHMVGTWGAV
LINIGLIISILGAWLSWTLLPAEIPLLMAKDKLMPKYFGKENANGAPTNALWLTNGLIQIFLLTTLFSEQ
AYNFAISLATSAILVPYLWSAAYQVKLSWRGGQERGRRKQLLIGLVALLYAVWLIYAAGLKYLLLSAILY
APGIYFYARARKEKGGPVFTKGELLIFAAIVAGAVIAIYLLATGLISL
>gnl|CDD|163523 TIGR03811, tyrosine_decarboxylase, tyrosine decarboxylase, Enterococcus type. This model represents tyrosine decarboxylases in the family of the Enterococcus faecalis enzyme Tdc. These enzymes often are encoded next to tyrosine/tyramine antiporter, together comprising a system in which tyrosine decarboxylation can protect against exposure to acid conditions. This clade differs from the archaeal tyrosine decarboxylases associated with methanofuran biosynthesis [Cellular processes, Adaptations to atypical conditions]
DLNLNALFIGDKAENGQLYKDLLNKLVDEHLGWRQNYMPQDKPVISPQERTSKSFTKTVNNMKDVLDELS
SRLRTESVPWHSAGRYWGHMNSETLMPAILAYNYAMLWNGNNVAYESSPATSQMEEEVGKEFATLMGYKN
GWGHIVADGSLANLEGLWYARNIKSLPFAMKEVKPELVAGKSDWELLNMPTKEIMDLLESAGDQIDEIKA
HSARSGKDLQKLGKWLVPQTKHYSWLKAADIIGIGLDQVIPVPVDSNYRMDINELEKIIRKLAAEKTPIL
GVVGVVGSTEEGAVDGIDKIVALRNKLMKEGIYFYLHVDAAYGGYGRAIFLDEDDNFIPYDDLQEVHAEY
GVFTEKKEYISREVYNAYKAISEAESVTIDPHKMGYIPYSAGGIVIQDIRMRDVISYFATYVFEKGADIP
ALLGAYILEGSKAGATAASVWAAHKVLPLNVTGYGKLIGASIEGAHRFYDFLNNLEFKVGDKEIEVHPLT
KPDFNMVDYVFNEKGNDDLVKMNKLNHAFYDYASYVKGSIYNNEFITSHTDFAIPDYGDSPFAFVNSLGF
SDEEWQRAGKVTILRASVMTPYMNDKENFDEYAPKIKAAMQEKLEKIY
>gnl|CDD|274796 TIGR03812, L-tyrosine_decarboxylase, tyrosine decarboxylase MnfA. Members of this protein family are the archaeal form, MnfA, of tyrosine decarboxylase, and are involved in methanofuran biosynthesis. Members show clear homology to the Enterococcus form, Tdc, that is involved in tyrosine decarboxylation for resistance to acidic conditions [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
SEEEVLEELKEYRSEDLKYSDGRILGSMCTNPHPIAVKAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGN
LLHLPDAYGYIVSGGTEANIQAVRAAKNLAREEKRTPNIIVPESAHFSFEKAAEMLGLELRYAPLDEDYT
VDVKDVEDLIDDNTIGIVGIAGTTELGQIDDIEELSKIALENGIYLHVDAAFGGFVIPFLKKGYNPPPFD
FSLPGVQSITIDPHKMGLSPIPAGGILFRSKSYLKYLSVDAPYLTVKKQATITGTRSGASAAATYAVIKY
LGREGYRKIVAECMENTRYLVEELKKIGFEPVIEPVLNIVAFEVDDPEEVRKKLRDRGWYVSVTRCPKAL
RIVVMPHVTREHIEEFLEDLKEI
>gnl|CDD|163525 TIGR03813, put_Glu_GABA_T, putative glutamate/gamma-aminobutyrate antiporter. Members of this protein family are putative putative glutamate/gamma-aminobutyrate antiporters. Each member of the seed alignment is found adjacent to a glutamate decarboxylase, which converts glutamate (Glu) to gamma-aminobutyrate (GABA). However, the majority belong to genome contexts with a glutaminase (converts Gln to Glu) as well as the decarboxylase that converts Glu to GABA. The specificity of the transporter remains uncertain
KKLTVVTLAIMNITAVVSLRGLPAEAEYGLSAAFYYLFAAIFFLVPVSLVAAELATAWPEKGGVFRWVGE
AFGARWGFLAIFMLWAQVTIWFPTVLTFGAVSLAFIGPEATVDESLAGNKLYVLVSVLFVYWLATFIALR
GVAAFTKVAKWGGIVGTIIPAAILVILGISYLLTGGESQIPLRWDDAFPDFTNFDNVVLAASIFLFYAGM
EMNAVHVKDVDNPDKNYPIAILIAALGTVLIFVLGTLAIAFIIPREDISLTQSLLVAFDNAFHWAGLSWL
GPILAFALAIGVLAGVVTWVAGPSSGMLAVAKAGYLPTFFQKTNKNGMPIHIMFVQGIAVSVLSVLFVVM
PSVQAAFQILSQLTVILYLVMYLLMFASAIYLRYSQPDRPRPYRIPGGLAGMWFIGGLGFVGSALAFVLS
FIPPSQIGTGSPTRYVGLLIGLAALFVTAPFLIYARRKPHWRDPNSNFEPFAWE
>gnl|CDD|274797 TIGR03814, Glutaminase_1, glutaminase A. This family describes the enzyme glutaminase, from a larger family that includes serine-dependent beta-lactamases and penicillin-binding proteins. Many bacteria have two isozymes. This model is based on selected known glutaminases and their homologs within prokaryotes, with the exclusion of highly-derived (long branch) and architecturally varied homologs, so as to achieve conservative assignments. A sharp drop in scores occurs below 250, and cutoffs are set accordingly. The enzyme converts glutamine to glutamate, with the release of ammonia. Members tend to be described as glutaminase A (glsA), where B (glsB) is unknown and may not be homologous (as in Rhizobium etli). Some species have two isozymes that may both be designated A (GlsA1 and GlsA2) [Energy metabolism, Amino acids and amines]
LEDIVEEARPLIGEGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALED
LGEDEVWERVGVEPSGDPFNSIVQLELEPGKPRNPFINAGAIAVTSLLPGRTSDEKLERILEFVRKLAGN
RSITIDEEVAQSERETGFRNRALAYLLKSFGNLENDVEEVLDVYFKQCSIEMTCKDLARAGLFLANGGVN
PLTGEQVISAEVAKRINALMLTCGLYDASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGN
SVAGQKALELLSEKLGLSIF
>gnl|CDD|274798 TIGR03815, CpaE_hom_Actino, helicase/secretion neighborhood CpaE-like protein. Members of this protein family belong to the MinD/ParA family of P-loop NTPases, and in particular show homology to the CpaE family of pilus assembly proteins (see). Nearly all members are found, not only in a gene context consistent with pilus biogenesis or a pilus-like secretion apparatus, but also near a DEAD/DEAH-box helicase, suggesting an involvement in DNA transfer activity. The model describes a clade restricted to the Actinobacteria
GVELDVAADPEAARRAWARAPLVLVDADMAEACAAAGLPRRRRVVLVGGGEPGGALWRAAAAVGAEHVAV
LPEAEGWLVELLADLDQSPPARGVVVAVIGGRGGAGASTLAAALALAAARHGLRTLLVDADPWGGGLDLL
LGAEDVPGLRWPDLSQARGRLPAGALRDALPRRGGLSVLSWGRAVGAALPPAAVRAVLDAARRGGDLVVV
DLPRRLTPAAETALESADLVLVVVPADVRAVAAAARVCPELGRRNPDLRLVVRGPAPAGLDPEEIAESLG
LPLLGEVRDQRGLARALERGGLPAASRRRPLGRAAAEVLDVL
>gnl|CDD|274799 TIGR03816, tadE_like_DECH, helicase/secretion neighborhood TadE-like protein. Members of this small, highly hydrophobic protein family occur in a pilus/secretion-like region that usually is next to an uncharacterized DEAH-box helicase, in Actinobacteria. Members show sequence similarity to the TadE-like family described by pfam07811. The function is unknown [Unknown function, General]
DRGSATVLAAAVLAALVALGAAVLAVGQAVVARHRAQSAADLAALAAAAALAAGAGAACAAAREVARANG
ARLVSCRVEGEDVVVTVEVRVLLGRGGARDARARARAGP
>gnl|CDD|274800 TIGR03817, DECH_helic, helicase/secretion neighborhood putative DEAH-box helicase. A conserved gene neighborhood widely spread in the Actinobacteria contains this uncharacterized DEAH-box family helicase encoded convergently towards an operon of genes for protein homologous to type II secretion and pilus formation proteins. The context suggests that this helicase may play a role in conjugal transfer of DNA
LTHVEHLPARAGRTAPWPAWAHPDVVAALEAAGIHRPWQHQARAAELAHAGRHVVVATGTASGKSLAYQL
PVLSALADDPRATALYLAPTKALAADQLRAVRELTLRGVRPATYDGDTPTEERRWAREHARYVLTNPDML
HRGILPSHARWARFLRRLRYVVIDECHSYRGVFGSHVALVLRRLRRLCARYGASPVFVLASATTADPAAA
ASRLIGAPVVAVTEDGSPRGARTVALWEPPLTELTGENGAPVRRSASAEAADLLADLVAEGARTLTFVRS
RRGAELVAAIARRLLGEVDPDLAERVAAYRAGYLPEDRRELERALRDGELLGVATTNALELGVDISGLDA
VVIAGFPGTRASLWQQAGRAGRRGQGALVVLVARDDPLDTYLVHHPEALFDRPVEATVFDPDNPYVLGPH
LCCAAAELPLTEADLELFGPAAAEVLDQLVEQGLLRRRPAGWFWTRRERAHDAVDIRGGGGAPVAIVEAE
TGRLLGTVDAGAAHSTVHPGAVYLHQGESYVVDELDLEDGVALVHAEDPDYTTFARETTDISVVEERRRR
AWGDVRVALGEVEVTSQVVGYLRRRLITGEVLDEVPLDLPPRTLRTRAVWYTVTPELLDDAGIDAADVPG
ALHAAEHAAIGLLPLVATCDRWDIGGVSTAVHPDTGLPTVFVYDGHPGGAGFAERGFAKAREWLAATRDA
IASCECESGCPSCVQSPKCGNGNDPLDKAGAARLLAAVLGAL
>gnl|CDD|274801 TIGR03818, MotA1, flagellar motor stator protein MotA. The MotA protein, along with its partner MotB, comprise the stator complex of the bacterial flagellar motor. MotAB span the cytoplasmic membrane and undergo conformational changes powered by the translocation of protons. These conformational changes in turn are communicated to the rotor assembly, producing torque. This model represents one family of MotA proteins which are often not identified by the "transporter, MotA/TolQ/ExbB proton channel family" model, pfam01618
MLKIIGLVVVLGSVFGGYALAGGHLAALWQPAELLIIGGAALGAFIIANPPKVLKETLKGLPAVFKGSKY
GKADYLDLLSLLYELLRKARREGLMAIESHIENPEESSIFSKYPKILKDHHLVEFICDYLRLMVMGNMNP
HELEALMEEEIETHHHELLKPAHALQKVADALPGFGIVAAVLGVVITMGSIDGPPEVLGHHIAAALVGTF
LGILLCYGFVGPLAAALEQRVEEEIKFLECVKVVLVAFLNGYAPQLAVEFGRKVIPSDVRPSFAELEEWV
RG
>gnl|CDD|200328 TIGR03819, heli_sec_ATPase, helicase/secretion neighborhood ATPase. Members of this protein family comprise a distinct clade of putative ATPase associated with an integral membrane complex likely to act in pilus formation, secretion, or conjugal transfer. The association of most members with a nearby gene for a DEAH-box helicase suggests a role in conjugal transfer
LLERVRRRLAAGSGPPTPAAVAAAVRAEAGRVLGDAEVLAAARALRRDLVGAGPLEPLLADPGVTDVLVN
GPDEVWVDRGRGLERTDVRFPDEAAVRRLAQRLAAAAGRRLDDAQPWVDARLPDGTRLHAVLPPVATDGT
CLSLRVPRRRTFTLDELVAAGTIPPGVARLLRALVAARLAFLVSGGTGSGKTTLLSALLALVPPDERIVL
VEDAAELRPDHPHVVRLEARPANVEGAGAVTLTDLVRQALRMRPDRIVVGEVRGAEVVDLLAALNTGHDG
GAGTLHANSPADVPARLEALGALAGLDRAALHSQLAAALDVVLHVRRTPRGRRRVAEIGV
>gnl|CDD|163532 TIGR03820, lys_2_3_AblA, lysine-2,3-aminomutase. This model describes lysine-2,3-aminomutase as found along with beta-lysine acetyltransferase in a two-enzyme pathway for making the compatible solute N-epsilon-acetyl-beta-lysine. This compatible solute, or osmolyte, is known to protect a number of methanogenic archaea against salt stress. The trusted cutoff distinguishes a tight clade with essentially full-length homology from additional homologs that are shorter or highly diverged in the C-terminal region. All members of this family have the radical SAM motif CXXXCXXC, while some but not all have a second copy of the motif in the C-terminal region
NATESEWKDWKWQLRHSIRDIDTFEKLLGITFSEEEREELKETLEKFPMSITPYYLSLIDPEDLRNDPIF
MQSFPSPAELIVSNHDMEDPLAEDEDSPVPGITHRYPDRVLFLVSNTCAMYCRHCTRKRKVGDRDSIPSK
EQILEGIEYIRNTPQIRDVLLSGGDPLLLSDDYLDWILTELRAIPHVEVIRIGTRVPVVLPQRITDELVA
ILKKHHPVWLNTHFNHPREITASSKKALAKLADAGIPLGNQSVLLAGVNDCPRIMKKLVHKLVANRVRPY
YLYQCDLSEGLSHFRTPVGKGIEIIESLIGHTSGFAVPTYVVDAPGGGGKIPVMPNYLISWSTNKVVLRN
YEGVITTYKEPDSYEPTFCDRNCDDCDLQLNLEDADESRAIGIEKLLSDHDDTISLVPENNERLERR
>gnl|CDD|163533 TIGR03821, EFP_modif_epmB, EF-P beta-lysylation protein EpmB. Members of this radical SAM protein subfamily, including yjeK in E. coli, form a distinctive clade, homologous to lysine-2,3-aminomutase of Bacillus, Clostridium, and methanogenic archaea. Members of this family are found in E. coli, Buchnera, Yersinia, etc. The gene symbol is now reassigned as EpmB (Elongation factor P Modification B) [Protein fate, Protein modification and repair]
WQQQLADAITDPQELLRLLDLPEALLQEAEKARKLFPLRVPRSFVARMKKGDPDDPLLRQVLPLHAEFEQ
HPGYSADPLDEQDANPVPGLLHKYHGRVLLIVTGGCAINCRYCFRRHFPYQENQPNKAQWKEALEYIAQH
PEINEVILSGGDPLMAKDHRLDWLLNLLEQIPHLKRLRIHTRLPVVIPDRITSGLCDLLANSRLQTVLVV
HINHANEIDAEVADALAKLRNAGITLLNQSVLLRGVNDNADTLAALSERLFDAGVLPYYLHLLDKVQGAA
HFDVDDERARALMAELLARLPGYLVPRLVREIPGEPSKTPL
>gnl|CDD|163534 TIGR03822, AblA_like_2, lysine-2,3-aminomutase-related protein. Members of this protein form a distinctive clade, homologous to lysine-2,3-aminomutase (of Bacillus, Clostridium, and methanogenic archaea) and likely similar in function. Members of this family are found in Rhodopseudomonas, Caulobacter crescentus, Bradyrhizobium, etc
LRTADDLIEAGLIPAAALAALEAVAARYAIAITPALAALIDRDDPDDPIARQFVPDPAELVTAPEERADP
IGDDAHSPVPGIVHRYPDRVLLKPVHVCPVYCRFCFRREMVGPEGLGVLSPAELDAAFAYIADHPEIWEV
ILTGGDPLVLSPRRLGDIMARLAAIDHVKIVRFHTRVPVADPARVTPALIAALKTSGKTVYVALHANHAR
ELTAEARAACARLIDAGIPMVSQSVLLRGVNDDPETLAALMRAFVECRIKPYYLHHLDLAPGTAHFRVTI
EEGQALVRALRGRISGLAQPTYVLDIPGGHGKAPVGPSYLE
>gnl|CDD|163535 TIGR03823, FliZ, flagellar regulatory protein FliZ. FliZ is involved in the regulation of flagellar assembly and possibly also the down-regulation of the motile phenotype. FliZ interacts with the flagellar translational activator FlhCD complex
MMVQHLKKRPLSRYLKDFKHSQTHCSHCHKLLDRISLVFRGQIINKESISRMDTLIDDNGWSVLQQELAA
LCRFCSEIYCNTTSDYFDIMAFKQYLFEQTEMSHSTVREYVVRLRRLDELLVAQNYPAEQFQDGFLQERL
ADWLPSTATNNYRIALRKYDQYLRWQCT
>gnl|CDD|274802 TIGR03824, FlgM_jcvi, flagellar biosynthesis anti-sigma factor FlgM. FlgM interacts with and inhibits the alternative sigma factor sigma(28) FliA. The C-terminus of FlgM contains the sigma(28)-binding domain
MKINGIGPPPVNAALRSTRSQAAAKASAAAAAAAAASGDSVSLSSLAQQLQSLEAALASSPDVDAEKVAE
IKAAIANGSYKVDAEKIADKLLDFE
>gnl|CDD|274803 TIGR03825, FliH_bacil, flagellar assembly protein FliH. This bacillus clade of FliH proteins is not found by the Pfam FliH model pfam02108, but is closely related to the sequences identified by that model. Sequences identified by this model are observed in flagellar operons in an analogous position relative to other flagellar operon genes
MSNIIKSTKSVIPAQERGIIPLRQVTDVPETEQELADEEQEFEQILEKAEAEAAQIIEQAEAQAAAIREQ
IEQERAQWEEERERLIQEAKQEGYEAGFQAGESEALSIYQSTIDEANAIVEEAKDDYEEKIESAQPLIIE
LACALAEKVIGVSLAEDKNAFQALVRQVLSEVREFDEVSIYVHPHWYERVAAQKDELQSILPACEHLAVY
PDEKLPDGGCYVETNFGRIDASVDTQLEQLKEKLLEALKEGDFAR
>gnl|CDD|163538 TIGR03826, YvyF, flagellar operon protein TIGR03826. This gene is found in flagellar operons of Bacillus-related organisms. Its function has not been determined and an official gene symbol has not been assigned, although the gene is designated yvyF in B. subtilus. A tentative assignment as a regulator is suggested in the NCBI record GI:16080597
MELANCPKCGRLFVKTGRDVCPSCYEEEEREFEKVYKFLRKHENRQATVSEIVEETGVSEKLILKFIREG
RLQLKHFPNLGYPCERCGTSIREGRLCDSCAGELKRQLSAGEQEKTKKKEKETEKKDTYYIQDTKNK
>gnl|CDD|163539 TIGR03827, GNAT_ablB, putative beta-lysine N-acetyltransferase. Members of this protein family are GNAT family acetyltransferases, based on a seed alignment in which every member is associated with a lysine 2,3-aminomutase family protein, usually as the adjacent gene. This family includes AblB, the enzyme beta-lysine acetyltransferase that completes the two-step synthesis of the osmolyte (compatible solute) N-epsilon-acetyl-beta-lysine; all members of the family may have this function. Note that N-epsilon-acetyl-beta-lysine has been observed only in methanogenic archaea (e.g. Methanosarcina) but that this model, paired with TIGR03820, suggests a much broader distribution
GSLIQHGPFNDRIYVMKLTGNDVEALIPDLDALAKKEGYTKIIAKVPGSDKPLFEERGYLEEAKIPGYFN
GHDAYFMSKYLDEDRRISSHSEKEDEVLEAALSKPRKPKIALPEGFTLRIATEDDADAMAALYRKVFPTY
PFPIHDPAYLLETMKSNVVYFGVEDGGKIIALASAEMDPENGNAEMTDFATLPEYRGKGLAKILLAAMEK
EMKEKGIRTAYTIARASSYGMNITFARLGYAYGGTLVNNTNISGGFESMNIWYKQL
>gnl|CDD|274804 TIGR03828, pfkB, 1-phosphofructokinase. This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688)
IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALL
REEGIKTDFVRVPGETRINVKIKEPSGTETKLNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGSLPPG
VPPDFYAELIALAREKGAKVILDTSGEALRDGLKAKPFLIKPNDEELEELFGRELKTLEEIIEAARELLD
LGAENVLISLGADGALLVTKEGALFAQPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSA
AAFSEGTGLPDPEDIEELLPQVTI
>gnl|CDD|163541 TIGR03829, YokU_near_AblA, uncharacterized protein, YokU family. Members of this protein family occur in various species of the genus Bacillus, always next to the gene (kamA or ablA) for lysine 2,3-aminomutase. Members have a pair of CXXC motifs, and share homology to the amino-terminal region of a family of putative transcription factors for which the C-terminal is modeled by pfam01381, a helix-turn-helix domain model. This family, however, is shorter and lacks the helix-turn-helix region. The function of this protein family is unknown, but a regulatory role in compatible solute biosynthesis is suggested by local genome context [Unknown function, General]
KCRWCEEEKAIARTTTVYWELPDGTKAIEIKETPSISCSHCGMEYQDDTTVKEIEDQLLLVDTKKLPDET
TYEELMKMPRLLKRNYFDF
>gnl|CDD|274805 TIGR03830, transcriptional_regulator_XRE_family, putative zinc finger/helix-turn-helix protein, YgiT family. This model describes a family of predicted regulatory proteins with a conserved zinc finger/HTH architecture. The amino-terminal region contains a novel domain, featuring two CXXC motifs and occuring in a number of small bacterial proteins as well as in the present family. The carboxyl-terminal region consists of a helix-turn-helix domain, modeled by pfam01381. The predicted function is DNA binding and transcriptional regulation
CPICGKGELVREVKDEPFTYKGESITIGVPGWYCPACGEELFDPEDSKRNSAALADFYRKVDGLLTGPEI
RRIRKKLGLSQREAAELLGGGVNAFSRYERGEVRPSKALDKLLRLLDKHPELLEELR
>gnl|CDD|274806 TIGR03831, hypothetical_protein, YgiT-type zinc finger domain. This domain model describes a small domain with two copies of a putative zinc-binding motif CXXC (usually CXXCG). Most member proteins consist largely of this domain or else carry an additional C-terminal helix-turn-helix domain, resembling that of the phage protein Cro and modeled by pfam01381
CPICGGEELEGKTTTETFEYGGELIVIENVPALVCPQCGEEYLDAE
>gnl|CDD|163544 TIGR03832, putative_ammonia_lyase/transferase, tyrosine 2,3-aminomutase. Members of this protein family are tyrosine 2,3-aminomutase. It is variable from member to member as to whether the (R)-beta-Tyr or (S)-beta-Tyr is the preferred product from L-Tyr. This enzyme tends to occur in secondary metabolite biosynthesis systems, as in the production of chondramides in Chondromyces crocatus. This class of enzyme has a prosthetic group, MIO (4-methylideneimidazol-5-one), that forms posttranslationally from an Ala-Ser-Gly motif
IDGETLTVDAVRRVAEQRAPCRVPAESLAKAAKSRAIFEGIAEQNVPIYGVTTGYGEMIYMLVDKEHEVE
LQTNLVRSHSAGVGPLFAEDEARAIVAARLNALAKGHSAVRPEILERLALYLNLGITPAIPEIGSLGASG
DLAPLSHVASTLIGEGYVLRDGRPVETAQVLRERGIEPLELRFKEGLALINGTSAMTGLGALVVGRALEQ
VQQAEIVTALVIEALRGSTGPFLAEGHDIARPHPGQIDSAANMRALMRGSGLTVEHADLRREVQERKEAE
KSVQRTEIYMQKAYSLRAIPQVLGAVRDTLYHARTKLEIELNSANDNPLFFEGREIFHGANFHGQPVAFA
MDFVTIALTQLGVLSERRLNRLLNRHLSYGLPEFLVAGDPGLHSGFAGAQYPATALVAENRTIGPASTQS
VPSNGDNQDVVSMGLIAARNARRVLSNNNKILAVELLAAAQAVDLAGRFDGLSPAARATYEAVRRLVPTL
GVDRYMADDIELVADAL
>gnl|CDD|274807 TIGR03833, TIGR03833, conserved hypothetical protein. A pair of adjacent genes, ablAB (acetyl-beta-lysine biosynthesis) encodes lysine 2,3-aminomutase and beta-lysine acetyltransferase in methanogenic archaea. Homologous pairs, possibly with identical function, occur in a wide range of species, including Bacillus subtilis. This model describes a conserved hypothetical protein, small in size, with a phylogenetic distribution moderately well correlated to that of the acetyltransferase family. This protein family is also described as DUF2196 and COG4895. The function is unknown [Hypothetical proteins, Conserved]
NGTKRSNIKPGLSVDIVLKQDQRTGKLTRGIVKDILTNSPTHPHGIKVRLEDGQVGRVKEIL
>gnl|CDD|213869 TIGR03834, EAGR_box, EAGR box. The EAGR box (Enriched in Aromatic and Glycine Residues) is found in three different proteins of the Mycoplasma genitalium terminal organelle, which acts in both cytadherence and gliding motility. The presence of this domain in a genome predicts the Mycoplasma-type terminal organelle structure, gliding motility, and cytadherence. The EAGR box may occur from one to nine times in a protein
VGNEEYGYYDENGEWIWKGYFDEDGNWV
>gnl|CDD|274808 TIGR03835, DnaJ-like_protein_MG200_homolog, terminal organelle assembly protein TopJ. This model describes TopJ (MG_200, CbpA), a DnaJ homolog and probable assembly protein of the Mycoplasma terminal organelle. The terminal organelle is involved in both cytadherence and gliding motility [Cellular processes, Chemotaxis and motility]
KRDYYEVLGIDRDADEQEIKKAFRKLAKKYHPDRNKAPDAASIFAEINEANDVLSNPKKRANYDKYGHDG
VDREDDFDFQADVFNSFFEEINKSGEFDNITDDDTPSKKKKKKKKKGWFWAKSKQESKTIETEEIIDVGA
SVNQANETRLFDDTLDDQLEESVSTQSTDDGERLFDQNKEPSFTAGLDDEVQSEVPQPEEDSDWEAFIGN
PDYGYFDENGEWIWKGYFDEDGNWVWTRELEPQDDSEDDYVIPDAEIISSPTLEVTAPKEVEQPLQPEPV
DEETVAETKAEEEPQPTQTVETKPTSAPESTVEENLPEINQPTQAVQPTSETISTTPVEPTDQLKPKEVD
QIQEELKKTKEIEVEELPTKKNDLVEINFDDLEELKFELVQTNQEKEPEKAVENWATDYQLDEPTQSNID
WYKQEDPKDLEQLVQDQATLEITEENQISPEPVEEQPSVESTAPEDQVVEAIKEEEELLEQKKAAEFAEL
FGQPTPTTSIEELLNPEQTQPTEFDEIIIENNLDNVSVADDQNYQLKDDNKKFINISLPTIVSSNESDDL
IYDPLQQPVRPMHTSDSETYEFSVDLLRKQAGPNLAKTDAKMEGIDGTNPNLLNQINDLSDFKSRLFKKL
FLTNQLPFISQPPASEYQEPNLDETNVNLVYEEEVPQILFFNNQIKEIKYTRHTVDGNTESTTNEAITLE
IQLPITSQLNISAIFKGFGHDFGNGCGDLKVVFKVIPSNFFQIKNDGLHVAALVDPLVAYNGGIIDVFGP
NKLFNVRIPGGIKVNDQVIFKDLGLTKTKYDKGSLIVHLYYSSVMKKNDRTNVQVQQFNKLALREYKLLK
YNQKELQNFQSNLSNGKKSLDQKSYQNLAFE
>gnl|CDD|163548 TIGR03836, termin_org_HMW1, cytadherence high molecular weight protein 1 N-terminal region. This model describes the N-terminal region of the Mycoplasma cytadherence protein HMW1, up to but not including the first EAGR box domain. The apparent orthologs in different Mycoplasma species differ profoundly in archictecture C-terminally to the region described here
EDVFETKDYTEEEPEAIFGNLYDGKGTVPEDGSIKVAYDADGNGYYIAFNPETGVYYDPYGDTEYDISAL
FDANGNPFVFFA
>gnl|CDD|274809 TIGR03837, EarP, Elongation-Factor P (EF-P) rhamnosyltransferase EarP. This model describes a conserved protein that typically is encoded next to the gene efp for translation elongation factor P
WDIFCRVVDNYGDIGVCWRLARQLAAEHGHQVRLWVDDLSAFARLCPEVDPDAGVQLVAGVEIRHWRAPF
PDLAPADVVIEAFACELPPEYLAAMAARGSKPVWINLEYLSAEDWVEGCHGLPSPQPGLGLTKYFFFPGF
TPATGGLLREPDLLERRDAFQADPAAQRALLRRLGVGPEPDALLVSLFCYENAALPALLDALAQSGSPVH
LLVPEGRALAAVAAWLGDALLAAGDVHRRGALTVAVLPFVPQDDYDRLLWACDLNFVRGEDSFVRAQWAG
KPFVWHIYPQEEDAHLAKLEAFLDLYCAGLAPEAAAALRAFWRAWNGGEALSADWPALRAALPEWQQHAQ
AWAARLAAQPDLATKLVQFVA
>gnl|CDD|274810 TIGR03838, queuosine_YadB, glutamyl-queuosine tRNA(Asp) synthetase. This protein resembles a shortened glutamyl-tRNA ligase, but its purpose is to modify tRNA(Asp) at a queuosine position in the anticodon rather than to charge a tRNA with its cognate amino acid [Protein synthesis, tRNA and rRNA base modification]
YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEV
VYQSQRHALYQAALDRLLAAGLAYPCQCTRKEIAAARDGGGIYPGTCRNGLPGRPGRPAAWRLRVPDGVI
AFDDRLQGPQQQDLAAAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGL
PPPRYLHLPLVVNADGEKLSKQNGAPALDDSRPLPALLAALRFLGLPPPPELAAASPAELL
>gnl|CDD|274811 TIGR03839, Adhesin_P1, adhesin P1. Members of this protein family are the major adhesin of the Mycoplasma terminal organelle. The protein is called adhesin P1, cytadhesin P1, P140, attachment protein, and MgPa, with locus names MG191 in Mycoplasma genitalium and MPN141 in M. pneumoniae. A conserved C-terminal region is shared by additional paralogs in M. pneumoniae and M. gallisepticum, as well as by the member of this family [Cell envelope, Surface structures, Cellular processes, Pathogenesis]
LTAGITLLALIGVGGFFLAVSGAKPNNLKPVNQPGEMNSQHQSALLEKLTPWTYRNSNFSSLSITGENPG
ALVLVRSKSAKGITAGSGSQQTTYPTRTEAALTASTTFAIRRYDLYGRALYDFDPGKLNPQTPTRDLTGK
VGFNPFTGFGLSGDAPFNWNELKSKVPVEVTQDPEDPNVFYVLLVPDAAVQYEQLQRGLQEQKTEDQVFE
SYFGAMFGLKVKNAMSDAPKTGEKLAEGTASSAGSGSSSSAAGGGAVAPTAAKALKREVEEGSSSGMGTM
LPKNDTAETPIKYNSDSGKIVKLKALLDSTESSESINGGRWRPWLTTAQINTQNNLQAVIVKVYDAPYSE
NPTAVENVDHIDPKDMVDNYPPSWTTPKWNHHGFWDYYARRLLLQTTGFFNPRRHPEWFDDGQTVADNEK
TGFDVDNSENTKQGFQKDKSAPIALPFEAYFANIGNLYAKGGMVYLFGGNGHVTKVNNTSPLSIGVFRTK
YENRTAEAPVTGWPYAILFSGIFNAQTNGLKDLPLGQNRWFEYVPRMAVGGVKGVGGNLVLAGTITMGDT
ATVPRLLYDELESNLNLVAQGQGLLREDLQWFTPYGWANRPDTPVGAWSSGALQSSGNPYYFHNNPDSQD
MPNSNGVEAIIKPWEDKDDAKYIYPYRYSGSYAWQSVNWSNKLTSKPLSADFVNENTYQPNSLFAAILNL
DLLNSLPDKVKYGKENEFAANEYERFNQFLSYAPLDGTNWSHFSPTLSRFSTGTNLDSSVLDQVLDYVPW
IGNGYRYGNNTAPQTSAGSSSGLPTFSNITVGTKQQLASTLAGENTMITGGSPQLWTGAGWRNDKASDEN
HTKFTSAQGQSGTSAGNPRSKQDNISKSGDSQEATNYTNLPPNLTPTADWLNALTFTNKNNDQRDQLFLR
GLLGNIPVLVNTSGNNTNKFQATDQKWTYTYQVGGNLPTWGEVNGLYNTALNITYYNLTRGDFGSNTPST
PGIGFKPEQNNDSDATLVSSGLNWTPQDVGNLVVSTGTQQGFQLGGWYVTFTDFTPPRQGYLGLQLTGLD
QRALIWAPRPWQDFKGSTTTASGAVISNWDKAGYSSRPDDSTTFNTSKILPEPFQKYKPNTSSGSTNSSP
YLELTAPVNVTSLDSYYVQLNNLLDPNQVRTKLRQGTTSGNGGGAGGGSSGSVNTVARVSGWLVGQLPPD
SSALALNPNRITNPLMNRDNVIGQGESAFIKMNDIPSGFVETPLNDLVDGEGQTTDADGKEVKFKSPDQI
DFNRLFTHPVTDLFDPVTMLVYDQYIPLIYRYPPPQNNPDIRLKVLSIDRSRQTLGLRLEFNDFIKLLPQ
DGEFVPVLQASSVGPQTEFTPFNQWPDYVLPLAITVPIVVIALSVTLGLGIGIPMHQNKKALKAGFALSN
KKVDVLTKAVGSVFKEIINRTGISN
>gnl|CDD|213871 TIGR03840, TMPT_Se_Te, thiopurine S-methyltransferase, Se/Te detoxification family. Members of this family are thiopurine S-methyltransferase from a branch in which at least some member proteins can perform selenium methylation as a means to detoxify selenium, or perform a related detoxification of tellurium. Note that the EC number definition does not specify a particular thiopurine, but rather represents a class of activity
EFWHERWQEGQIGFHQSEVNPLLVKHWPALGLPAGARVFVPLCGKSLDLAWLAEQGHRVLGVELSEIAVE
QFFAENGLTPTVTQQGEFTRYRAGNIEIFCGDFFALTAADLGPVDAVYDRAALIALPEEMRQRYAAHLLA
LLPPGARQLLITLDYDQSEMAGPPFSVSPAEVEALYGGHYEIELLESRDVLEDNPRFGKKGLSRLTESVW
LLT
>gnl|CDD|274812 TIGR03841, F420_Rv3093c, probable F420-dependent oxidoreductase, Rv3093c family. This model describes a small family of enzymes in the bacterial luciferase-like monooxygenase family, which includes F420-dependent enzymes such as N5,N10-methylenetetrahydromethanopterin reductase as well as FMN-dependent enzymes. All members of this family are from species that produce coenzyme F420; SIMBAL analysis suggests that members of this family bind F420 rather than FMN [Unknown function, Enzymes of unknown specificity]
LPLWQDRPLAEATRLARAADELGYTDVWSGEMAGYDAFALATLVAAWAPRLRLGVGPLPVTVRGPGLLAM
GAASVADLTGRRVDLALGASSPAIVEDWHGRERADPARALRESLRFLRALLAGERVEFAGETFRSRGFRL
RLPAPPPRLTLAAFGPGMLRLAAEEADGVVLNLLSPEDVARVRARLALASARMGRAVPRLEVWAPAAVCP
TDPAAEARDLGRRGLAPYLAAPGYGEMFAWLGFGEVLRLARAAADRRELLAAVPDEVVDAVAAHGDAAQV
RARLEAYVDAGVDTVVLVPEP
>gnl|CDD|163554 TIGR03842, F420_CPS_4043, F420-dependent oxidoreductase, CPS_4043 family. This model represents a family of putative F420-dependent oxidoreductases, fairly closely related to 5,10-methylenetetrahydromethanopterin reductase (mer, TIGR03555), both within the bacterial luciferase-like monoxygenase (LLM) family. A fairly deep split (to about 40 % sequence identity) in the present family separates a strictly Actinobacterial clade from an alpha/beta/gamma-proteobacterial clade, in which the member is often the only apparent F420-dependent LLM family member. The specific function, and whether Actinobacterial and Proteobacterial clades differ in function, are unknown [Unknown function, Enzymes of unknown specificity]
DFGVVLQTDPPASRVVELARQAERHGFDYVWTFDSHILWQEPFVIYSQILAATRNMVVGPMVTNPLTRDW
TVTASLFATLNEMFGNRTVCGIGRGDSAVRVLGGKPATLARLREAMHVIKELANGREVDYGGAPVRLPWA
RGGELPVWVAAYGPKALKLAGEVADGFILQLADPDIAKWMIDAVREAAEDAGRDPDSVKVCVAAPAYVGD
DLEHQREQCRWFGGMVGNHVADIVARYGADSGLVPKALTDYIKGRRGYDYSEHGRAGNPHTDFVPDEIVD
RFCVLGPAEAHIEKLRELRALGVDQFAIYLQHDDKEETIAAYGRHIIPAF
>gnl|CDD|274813 TIGR03843, Phosphatidylinositol_3-_and_4-kinase, conserved hypothetical protein. This model represents a protein family largely restricted to the Actinobacteria (high-GC Gram-positives), although it is also found in the Chloroflexi. Distant similarity to the phosphatidylinositol 3- and 4-kinase is suggested by the matching of some members to pfam00454
LRDGELTVLGRLVDASNATLLCEVTLDGVSARAVYKPVRGERPLWDFPDGTLAGREVAAYLVSEALGWGL
VPPTVLRDGPFGPGMVQLWIDPDDDPDLVDLVHADHPQLRRMAVFDAVVNNADRKGGHVLPGPDGRVWGV
DHGVTFHVEPKLRTVLWGWAGEPLPAELLADLARLRDDLDGDLGRELAELLTPEEVAALRRRVDRLLETG
VFPAPSGHWPAIPWPP
>gnl|CDD|163556 TIGR03844, cysteate_syn, cysteate synthase. Members of this family are cysteate synthase, an enzyme of alternate pathway to sulfopyruvate, a precursor of coenzyme M [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Energy metabolism, Methanogenesis]
YTLRCPGCGEVLPDHYTLSCPLDCGLLRAEYAERQLTLRDLPGIFRYYDWLPVTGHLRTRGGPVTYKSEG
LARELGLSDLYITFSGYWPERGAFMRTCSFKELEALPTMQRLKERGGKTLVVASAGNTGRAFAEVSAITG
QPVILVVPKSSADRLWTTEPASSVLLVTVDGDYTDAIALADRIATLPGFVPEGGARNVARRDGMGTVMLD
AAVTIGSLPDHYFQAVGSGTGGIAAWEAAMRLIEDGRFGSKLPRLHLAQNLPFVPMVNAWQEGRREIIPE
SDMPDAENSIEEVYSDVLTNRTPPYGVTGGVFDALIATGGQMYGVSNKEAVSAGKLFEESEGIDILPAAA
VAVAALVKAVESGFIGPDDDILLNITGGGYKRLREDLPRYQIEPDLTV
>gnl|CDD|163557 TIGR03845, sulfopyru_alph, sulfopyruvate decarboxylase, alpha subunit. This model represents the alpha subunit, or the N-terminal region, of sulfopyruvate decarboxylase, an enzyme of coenzyme M biosynthesis. Coenzyme M is found almost exclusively in the methanogenic archaea. However, the enzyme also occurs in Roseovarius nubinhibens ISM in a degradative pathway, where the resulting sulfoacetaldehyde is desulfonated to acetyl phosphate, then converted to acetyl-CoA (see) [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Energy metabolism, Methanogenesis]
EEAVYNILKDAGIDLVASVPCDNLKNLLPLIEKDFRHIPLTREEEGVGICAGAYLAGKKPAILMQSSGLG
NSINALASLNKTYGIPLPILASWRGVYKEKIPAQIPMGRATPKLLDTLGIPYTIPREPEEAKLIEKAISD
AYENSRPVAALLDPKYW
>gnl|CDD|274814 TIGR03846, sulfopy_beta, sulfopyruvate decarboxylase, beta subunit. Nearly every member of this protein family is the beta subunit, or else the C-terminal region, of sulfopyruvate decarboxylase, in an archaeal species capable of coenzyme M biosynthesis. However, the enzyme also occurs in Roseovarius nubinhibens ISM in a degradative pathway, where the resulting sulfoacetaldehyde is desulfonated to acetyl phosphate, then converted to acetyl-CoA (see)
RIDAIRAIASYLEDELVVSNIGVPSKELYAIRDRPLNFYMLGSMGLASSIGLGLALATDRTVIVIDGDGS
LLMNLGVLPTIAAESPKNLILVILDNGAYGSTGNQPTPASRRTDLELVAKAAGIRNVEKVADEEELRDAL
KALAMKGPTFIHVKVKPGNAKVPNIPLSPEEIKERFMEAIR
>gnl|CDD|213872 TIGR03847, TIGR03847, conserved hypothetical protein. The conserved hypothetical protein described here occurs as part of the trio of uncharacterized proteins common in the Actinobacteria
RIHVFDPPDRFVAGTVGPPGARTFYLQAREGSRVVSVALEKQQVAALAERIDELLDEVGRRFGAVVPAES
PDELVDLDPLEEPIEEEFRVGTMGLGWDPETDRVVIEAQALTEDEIDDSVVLDDTEDGPDALRVRLTPGQ
ARAFAKRARRVVAAGRPPCPLCGRPIDPDGHICPRQN
>gnl|CDD|163560 TIGR03848, MSMEG_4193, probable phosphomutase, MSMEG_4193 family. A three-gene system broadly conserved among the Actinobacteria includes MSMEG_4193 and homologs, a subgroup among the larger phosphoglycerate mutase family protein (pfam00300). Another member of the trio is a probable kinase, related to phosphatidylinositol kinases; that context supports the hypothesis that this protein acts as a phosphomutase
TVILVRHGRSTANTAGTLAGRTPGVDLDERGREQAAALAERLADLPIAAIVSSPLERCRETAEPIAEARG
LPPRVDERLGECDYGDWTGRELKELAKEPLWPVVQAHPSAAVFPGGESLAQVQARAVAAVREHDARLAAE
HGPDAVWVACSHGDVIKSVLADALGMHLDLFQRIVVDPCSVSVVRYTPLRPFVLRVNDTGGDLS
>gnl|CDD|163561 TIGR03849, arch_ComA, phosphosulfolactate synthase. This model finds the ComA (Coenzyme M biosynthesis A) protein, phosphosulfolactate synthase, in methanogenic archaea. The ComABC pathway is one of at least two pathways to the intermediate sulfopyruvate. Coenzyme M occurs rarely and sporadically outside of the archaea, as for expoxide metabolism in Xanthobacter autotrophicus Py2, but candidate phosphosulfolactate synthases from that and other species occur fall below the cutoff and outside the scope of this model. This model deliberately is narrower in scope than pfam02679 [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Energy metabolism, Methanogenesis]
ITMVLDKGLPPKFVEDYLKVCGDYITFVKFGWGTSALIDRDIVKEKIEMYKDYGIKVYPGGTLFEIAHSK
GKFDEYLNECDELGFEAVEISDGSMEISLEERCNLIERAKDNGFMVLSEVGKKSPEKDSELTPDDRIKLI
NKDLEAGADYVIIEGRESGKNIGLFDEKGNVKEDELDVLAENVDINKVIFEAPQKNQQVEFILKFGPDVN
LGNIPPEEVISLETLRRGLRGDTFGKV
>gnl|CDD|274815 TIGR03850, ABC_transporter_substrate-binding_protein, carbohydrate ABC transporter substrate-binding protein, CPR_0540 family. Members of this protein are the substrate-binding protein of a predicted carbohydrate transporter operon, together with permease subunits of ABC transporter homology families. This substrate-binding protein frequently co-occurs in genomes with a family of disaccharide phosphorylases, TIGR02336, suggesting that the molecule transported will include beta-D-galactopyranosyl-(1-_3)-N-acetyl-D-glucosamine and related carbohydrates. Members of this family are sporadically strain by strain, often in species with a human host association, including Propionibacterium acnes and Clostridium perfringens, and Bacillus cereus [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
KKLLALALALAMAASSLAGCGSGTADGASTGEEVTLKVAAFEGGYGTKMWEEVVEAFEKSHEGVKVELTV
SKNLEDVITPQIQAGDYPDVVYLATGRESGLTETLIKDKALADLTDVLDMKVPGEDVTVKDKILPGFVGS
SATNPYGDGKTYLAPMFYSPTGLFYNKTLFEEKGWEVPTTWDEMFALGDKAKAEGISLFTYPTTGYFDAF
FYALLAEAGGDDFFNKAMNYEEGIWDTEEAKKAFDTVGKLATYTEPTTVANANNQDFTKNQQLVLDNKAL
FMPNGTWVVGEMKDAPRADGFEWGMTALPAVKEGGDRYSYTFFEQMWIPAAAKNKDLAKEFIAFLYSDEA
AKIFAKSGAVQPVKGIADKLSGENKVFYSIYDNGAKAVIGGFAATKAVEGVDMKDTLYGTVNSVVSGDKT
VEEWQDSVEEASDKLRA
>gnl|CDD|274816 TIGR03851, chitin_NgcE, carbohydrate ABC transporter, N-acetylglucosamine/diacetylchitobiose-binding protein. Members of this protein family are the substrate-binding protein, a lipid-anchored protein of Gram-positive bacteria in all examples found so far, that include NgcE of the chitin-degrader, Streptomyces olivaceoviridis, and close homologs from other species likely to share the same function. NgcE binds both N-acetylglucosamine and the chitin dimer, N,N'-diacetylchitobiose [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
GPGAGLLSACASGGGSDDASSTGGGAAKSADNPFGVADDAPLEVVIFNGGYGDDYAKDAEPLYKKKYPGA
TVKVSPTQKIAPQLQPRFAGGNPPDLIDNSGADAMDMSALVAEGQLEDLTPLFDAPSWDDPGKKVRDTLL
PGVLEPGTFDGKPYALNYVYTVYGLWYSATLFEENGWTPPKTWDEFLALGEEAKAKGIAPFAYAGKHAPY
YYRELLLDSAAKIGGDEVVKDIDNLEDGAWKHPAVKAAFTAWEELVKKGYILPGGAGLDHTQSQTAWNQG
KAAFYPSGSWLENEMKSQTPADFEMTGAPTPSLTASDKLPYGALHAAAGEPFIVPAKAKNPAGGLEYLRI
MLSKEGAANFTELTKSLTVVKGTADGLGLSTALASASALLSAAGTNVVTWYFADWYVGLNKDQLVLTNEF
MAGRITADEFCERMQKAADKIAKDSSVKKQ
>gnl|CDD|163564 TIGR03852, sucrose_gtfA, sucrose phosphorylase. In the forward direction, this enzyme uses phosphate to cleave sucrose into D-fructose + alpha-D-glucose 1-phosphate. Characterized representatives from Streptococcus mutans and Bifidobacterium adolescentis represent well-separated branches of a molecular phylogenetic tree. In S. mutans, the region including this gene has been associated with neighboring transporter genes and multiple sugar metabolism
NKAMLITYADSLGKNLKELNKVLENYFKDAVGGVHLLPFFPSTGDRGFAPMDYTEVDPAFGDWSDVEALS
EKYYLMFDFMINHISRQSEYYQDFLEKKDNSKYKDLFIRYKDFWPNGRPTQEDVDLIYKRKDRAPYQEVT
FADGSTEKVWNTFGEEQIDLDVTSETTKRFIRDNLENLAEHGASIIRLDAFAYAVKKLGTNDFFVEPEIW
ELLDEVRDILAPTGAEILPEIHEHYTIQFKIAEHGYYVYDFALPMLVLYSLYSGKTNRLADWLRKSPMKQ
FTTLDTHDGIGVVDVKDLLTDEEIDYTSEELYKVGANVKKIYSTAAYNNLDIYQINCTYYSALGDDDQAY
LLARAIQFFAPGIPQVYYVGLLAGKNDIELLEETKEGRNINRHYYTLEEIAEEVKRPVVAKLLNLLRFRN
TSKAFDLDGSIDIETPSENQIEIVRTNKDGGNKAILTANLKTKTFTITEN
>gnl|CDD|163565 TIGR03853, hypothetical_protein, probable metal-binding protein. This model describes a family of small cytosolic proteins, about 80 amino acids in length, in which the eight invariant residues include three His residues and two Cys residues. Two pairs of these invariant residues occur in motifs HxH (where x is A or G) and CxH, both of which suggest metal-binding activity. This protein family was identified by searching with a phylogenetic profile based on an anaerobic sulfatase-maturase enzyme, which contains multiple 4Fe-4S clusters. The linkages by phylogenetic profiling and by iron-sulfur cluster-related motifs together suggest this protein may be an accessory protein to certain maturases in sulfatase/maturase systems
SIHGHEVLNLMLASGEPYTRESLKAAIEQKFGEDARFHTCSAEGMTADELLQFLLKKGKFIESDGGFTTN
ADRICNH
>gnl|CDD|163566 TIGR03854, F420_MSMEG_3544, probable F420-dependent oxidoreductase, MSMEG_3544 family. Coenzyme F420 has a limited phylogenetic distribution, including methanogenic archaea, Mycobacterium tuberculosis and related species, Colwellia psychrerythraea 34H, Rhodopseudomonas palustris HaA2, and others. Partial phylogenetic profiling identifies protein subfamilies, within the larger family called luciferase-like monooxygenanases (pfam00296), that appear only in F420-positive genomes and are likely to be F420-dependent. This model describes a small family, closely related to other such families in the putative F420-binding region, exemplified by MSMEG_3544 in Mycobacterium smegmatis [Unknown function, Enzymes of unknown specificity]
RFGVGLGADVAPAELPAIVDRLESTGVDSLWLSELVYSPAVDPFVGMAFALGRTSRLKVGTSVAVLPGRH
PVLVAKQLASLAALAPRRVLPVFGLRSARPAEREAFVVPPGRRGAVFDESLELLRALLREPRVTFHGRFF
SVTDVGVGPKPARPLDIWLGGSAPAALRRIGRLGDGWLGSFVTPEEARAGRRTIEAAAAAAGREIEPDHF
GISLAVADGDLPAPVIAALRRRRPDVDPAELIAVGWAQLHRRIDAYLDAGLTKFVIRPAGTGDWDAFLDR
FVTELLPREN
>gnl|CDD|163567 TIGR03855, NAD_NadX, aspartate dehydrogenase. Members of this protein family are L-aspartate dehydrogenase, as shown for the NADP-dependent enzyme TM_1643 of Thermotoga maritima. Members lack homology to NadB, the aspartate oxidase (EC 1.4.3.16) of most mesophilic bacteria (described by TIGR00551), which this enzyme replaces in the generation of oxaloacetate from aspartate for the NAD biosynthetic pathway. All members of the seed alignment are found adjacent to other genes of NAD biosynthesis, although other uses of L-aspartate dehydrogenase may occur
NFEIAAVYDRNPKDAKELAERCGAKIVSDFDEFLPEDVDIVVEAASQEAVKEYAEKILKNGKDLLIMSVG
ALADRELRERLREVARSSGRKVYIPSGAIGGLDALKAASLGRIERVVLTTTKPPASLGRDIKEPTTIFEG
SASEAIKLFPANINVAATLSLAAGFDAKVEIVADPEADRNIHEIFVESDFGEMEIRVENVPSPENPRTSY
LAALSALRLLRNLASPLVI
>gnl|CDD|213873 TIGR03856, F420_MSMEG_2906, probable F420-dependent oxidoreductase, MSMEG_2906 family. This model describes a small family of enzymes in the bacterial luciferase-like monooxygenase family, which includes F420-dependent enzymes such as N5,N10-methylenetetrahydromethanopterin reductase as well as FMN-dependent enzymes. All members of this family are from species that produce coenzyme F420; SIMBAL analysis suggests that members of this family bind F420 rather than FMN [Unknown function, Enzymes of unknown specificity]
IRIGVQLQPQHAPDYRTWRDAVRRAEDLGVDVIFNWDHFFPLYGDPDGAHFEGWTMLAAWAEQTSRAEIG
ALVTCNSYRNPDLLADMARTVDHISGGRLILGIGSGWYEKDYDEYGYEFGTAGSRLDLLAAALPRIKARL
AKLNPPPLRDIPILIGGGGEKKTLPLVARHADIWHSFLDIETYRRKSQILDRHCADVGRDPATIERSVSW
PGLDSADAYVAAGVTLFTVGIGGPDYDLTAVEELLRWRD
>gnl|CDD|213874 TIGR03857, F420_MSMEG_2249, probable F420-dependent oxidoreductase, MSMEG_2249 family. Coenzyme F420 has a limited phylogenetic distribution, including methanogenic archaea, Mycobacterium tuberculosis and related species, Colwellia psychrerythraea 34H, Rhodopseudomonas palustris HaA2, and others. Partial phylogenetic profiling identifies protein subfamilies, within the larger family called luciferase-like monooxygenanases (pfam00296), that appear only in F420-positive genomes and are likely to be F420-dependent. This model describes a distinctive subfamily, found only in F420-biosynthesizing members of the Actinobacteria of the bacterial luciferase-like monooxygenase (LLM) superfamily [Unknown function, Enzymes of unknown specificity]
LGAYVLPGRGADPAQAIDEARAAERLGFGTVYLSERWNLKEAGVVAGAIGAVTSRVRIATGITHPATRHP
LHLASLAATAHALSGGRFTLGLGRGVGAMWRAVGLPTATNAALVDYADVMRRLWRGEAVRYDGPAGNYRV
LRLGDLPEDPAPPLVFGAIGPKGLALAGRAFDGVILHPFLTPEAVARSVAIVRRAAEAAGRDPASVRVYA
TVVTAPDLPPDEERAVVGARAVTYLQIPGYGELLARVNGWDPAPLERLRAHPLLAGIRGSADTAFTREQL
VDVADLIPDEWLEASAAIGSAAQCARRLQDYRDAGADEVVLHGSTPDQL
>gnl|CDD|274817 TIGR03858, LLM_2I7G, probable oxidoreductase, LLM family. This model describes a highly conserved, somewhat broadly distributed family withing the luciferase-like monooxygenase (LLM) superfamily. Most members are from species incapable of synthesizing coenzyme F420, bound by some members of the LLM superfamily. Members, therefore, are more likely to use FMN as a cofactor
ELGIDTFGDTTDDATGRTVSHAERLRQLVEEIELADQVGLDVFGLGEHHRPDYAVSAPEVVLAAAAARTK
RIRLTSAVTVLSSDDPVRVFQRFATLDALSNGRAEIMAGRGSFTESFPLFGYDLADYDALFEEKLDLLLK
LREQEPVTWSGKFRPALNGQGVYPRPEQGPLPIWIGVGGTPESVVRAGRLGLPLMLAIIGGNPARFAPLV
DLYREAAREAGHPPEQLPVGVHSHGFVAETDEEAADEFFPPYAAMMNRIGRERGWPPMTRAQFDAERGPE
GALYVGSPETVAEKIADTIEALGLDRFTLHYSVGPLPHEQVMRAIELYGTKVAPLVR
>gnl|CDD|274818 TIGR03859, PQQ_PqqD, coenzyme PQQ biosynthesis protein PqqD. This model identifies PqqD, a protein involved in the final steps of the biosynthesis of pyrroloquinoline quinone, coenzyme PQQ [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
PALRRGYRLQWERAQDCWVLLYPEGMVKLNDSAGEILELCDGKRSLAEIIQELAQRFPAAEEIEDDVIAF
LAVARAKHWLE
>gnl|CDD|274819 TIGR03860, FMN_nitrolo, FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family. This model represents a distinctive clade, in which all characterized members are FMN-binding, within the larger family of luciferase-like monooxygenases (LLM), among which there are both FMN- and F420-binding enzymes. A well-characterized member is nitrilotriacetate monooxygenase from Aminobacter aminovorans (Chelatobacter heintzii), where nitrilotriacetate is a chelating agent used in detergents [Unknown function, Enzymes of unknown specificity]
LGAFLNGVGHHPGLWRHPRARADAYLDLDYWTELARTAERGKFDALFFADVLGVYDVPDAALRRAAQLPR
FEPLTLLSALAAVTEHIGLGATASTTYEEPYNLARRFASLDHLSGGRAGWNIVTSYLDSAARNFGLDEHP
PHDERYERAEEFVDVVYKLWDSWEDDAFVRDKASGVFADPAKVHPINHKGKHFSVRGPLNIPRSPQGTPV
LFQAGSSERGREFAARHAEAVFTAQPTLEDAQAFYADIKARAAAAGRDPDDVKILPGITPIVGRTEAEAR
AKYAELQDLISPEGGLALLSGWTGIDLSQYDLDAPLPDLPTEAGQKSRFDLILELARRENLTLRQLALRL
AGGRGHPVFVGTPEQVADQLEEWFEEGAADGFNLMPPVLPGGLEDFVDLVVPELQRRGLFRTEYEGGTLR
EH
>gnl|CDD|163573 TIGR03861, ABC_efflux_transporter_permease_protein, alcohol ABC transporter, permease protein. Members of this protein family, part of a larger class of efflux-type ABC transport permease proteins, are found exclusively in genomic contexts with pyrroloquinoline-quinone (PQQ) biosynthesis enzymes and/or PQQ-dependent alcohol dehydrogenases, such as the phenylethanol dehydrogenase PedE of Pseudomonas putida U. Members include PedC, an apparent phenylethanol transport protein whose suggested role is efflux to limit intracellular concentrations of toxic metabolites during phenylethanol catalysis [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
LICFNGIVLREALRFVQQRSRFLSALVRPLLWLLVFAAGFRAALGISIIEPYDTYITYEVYIVPGLCCMI
LLFNGMQSSLSMVYDREMGSMRVLLTSPLPRPFLLFCKLLASALISLLQVYAFLAIAALVGVQPPVWGYV
SVLPALVLVAFMLGALGLALSNLIRQLENFAGVMNFVIFPMFFLSSALYPLWKMQEASTWLYWICALNPF
THAVELVRFALYGQLNLPALGWTLGATTLFTLLAFWGFDPQHG
>gnl|CDD|274820 TIGR03862, flavo_PP4765, uncharacterized flavoprotein, PP_4765 family. This model describes a sharply distinctive clade of proteins within the larger family of flavoproteins described by pfam03486 and TIGRFAMs model TIGR00275. The function is unknown
GLEVDVFEAKPSVGRKFLMAGKSGLNLTHSEPLPRFIERYGDAAEWLAPWLEAFDAVALQDWARGLGIET
FVGSSGRVFPVEMKAAPLLRAWLKRLAEQGVQFHTRHRWIGWQGGTLRFETPDGQSTIEADAVVLALGGA
SWSQLGSDGAWQQVLDQRGVSVAPFAPANCGFLVDWSAHFASRFAGEPLKRVNATAGTQQTRGEIVITAR
GLEGGLIYALSAALREQIKAGGSANLFLDLLPDLSLEQVTKRLAAPRGKQSLSNHLRKALGLDGVKRALL
REVFPKAAWSQPETLAQTIKALPLPLDGTRPIDEAISTAGGVRQDALDESLMLKARPGVFCAGEMLDWEA
PTGGYLLTACFATGRAAGEGVHSWLE
>gnl|CDD|274821 TIGR03863, PQQ_ABC_bind, ABC transporter, substrate binding protein, PQQ-dependent alcohol dehydrogenase system. Members of this protein family are putative substrate-binding proteins of an ABC transporter family that associates, in gene neighborhood and phylogenomic profile, with pyrroloquinoline-quinone (PQQ)-dependent degradation of certain alcohols, such as 2-phenylethanol in Pseudomonas putida U [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
PLSNLDGPPEDLGLAGARLALADNNTTGRFLGQTFALDEVAVPPPEDLLAALQALLAQGVRFFVLDLPAA
DLLALADAAKAKGALLFNAGAPDDALRGADCRANLLHTLPSRAMLADALAQYLAAKRWRRILLIQGPLPE
DALFADALRRSAKRFGLKIVAERPFTFSGDPRRTDQAEVPLFTQGADYDVVVVADEAGDFARYLPYNTWL
PRPVAGSAGLVPTAWHRAWERWGATQLQSRFRKLAGRPMTELDYAAWLAVRAVGEAVTRTGSADPATLRD
YLLSDEFELAAFKGRPLSFRPWDGQLRQPVLLVHPRAVVSVAPQEGFLHQTNELDTLGADAPESACR
>gnl|CDD|274822 TIGR03864, PQQ_ABC_ATP, ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system. Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
ALEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPR
AALARLGVVFQQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRR
VEIARALLHRPALLLLDEPTVGLDPASRAAITAHVRALARDQGLSVLWATHLVDEIEASDRLVVLHRGRV
LADGAAAELRGATGGADLEAAFLALT
>gnl|CDD|274823 TIGR03865, PQQ_CXXCW, PQQ-dependent catabolism-associated CXXCW motif protein. Members of this protein family have a CXXXCW motif, consistent with a possible role in redox cofactor binding. This protein family shows strong relationships by phylogenetic profiling and conserved gene neighborhoods with a transport system for alcohols metabolized by PQQ-dependent enzymes
LLLLLAAAAAAALFEPEGYRTDQYRAPVPATLAGARVLDTEEAQALWARGPVALIDVYPRPPKPKNLLEG
TVWRDEPRLSLPGSLWLPNTGYGNLAPAWQAYLRRGLARATGGDKGRPLVFYCRADCWMSWNAAKRALAL
GYTNVYWYPDGTDGWQAAGLPL
>gnl|CDD|274824 TIGR03866, PQQ_ABC_repeats, PQQ-dependent catabolism-associated beta-propeller protein. Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol
LLLAAGSAAAETAYVSNEKDNTISVIDTATLKVTRTFPVGQRPRGITFSKDGKLLYVCASDSDTIQVIDP
ATGEVLHTLPSGPDPEQFALHPNGKILYIANEDDALVTVIDIETRKVLAQIDVGVEPEGMAVSPDGKIVV
NTSETTNMAHWIDTATYEIVDNTLVDARPRFAEFTADGKELWVSSEIGGTVTVIDVATRKVIKKITFAIP
GVHPEKVQPVGIKLTKDGKTAFVALGPANRVAVVDAKTYEVLDYLLVGQRVWQLAFTPDESRLLTTNGVS
NDVSVIDVAALKVIKSIKVGRLPWGVVVRP
>gnl|CDD|274825 TIGR03867, MprA_tail, MprA protease C-terminal rhombosortase-interaction domain. This model describes the Ralstonia lineage variant of the GlyGly-CTERM domain (TIGR03501), a predicted target for protein sorting and cleavage by rhombosortase, a member of the family of rhomboid proteases. Note that some MprA family proteases are full-length homologs except for the lack of this domain. All members of the present family are predicted serine proteases
GGGGALPLWLAALLLAAGLAGFQRRRR
>gnl|CDD|274826 TIGR03868, transport_system_substrate-binding_protein, proposed F420-0 ABC transporter, periplasmic F420-0 binding protein. This small clade of ABC-type transporter periplasmic binding protein components is found as a three gene cassette along with a permease (TIGR03869) and an ATPase (TIGR03873). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this periplasmic binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter
PVTVDNCGTDVTFDSAPQRVVTIKSSTTELLLALGLGDRIVGTAFPDGPVPAEWATDAAAVPPLSERVPS
PEAVLETEPDLVYAGWESNLTAEGAGERADLASLGVNTYVAPSACKEDGYQPDPLTFDDVFAEITEVGTI
FDVPDAAASLVAEQRAQLAAIEPDDRGLTALWYSSGSDTPFVGAGIGAPQMVMDTAGLTNIAADVHDTWT
PMSWEAVVDADPDVIVLVDSAWNSAEKKIEVLESNPATSNLTAVQEQRYVVVPFAATEAGVRNVDAAASL
ADQLAEL
>gnl|CDD|163581 TIGR03869, transport_system_permease_protein, proposed F420-0 ABC transporter, permease protein. his small clade of ABC-type transporter permease protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and an ATPase (TIGR03873). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with an F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this permease protein is a component of a F420-0 (that is, F420 lacking only the polyglutamate tail) transporter
ALLASLVVAVTIGPADISVGEVWRSVAAHLGRGEGFPGVALSRLQDAIVWDLRLPRVLTAAAVGAGLAIA
GAVMQSLTRNPLADPYLLGLSSGASLGAVAVLVLGVAVLLPVAAFAGALLALAATLGLARTLGTLTPTRT
ILAGLAVSQLCAAVTSFVIFWSATGDSYREILSWLMGSLAGATWGSVAIAGGALLVVGLVLLASGRVLDA
FAFGDSSAAALGVDVERTRWLLLTLVALLTGALVSVSGAIGFVGLILPHAVRLLTGPRHRLLLPVSALAG
AVFLVWADTLARTVFAPRELPVGIITALIGAPVFAVLLYRSRSGA
>gnl|CDD|274827 TIGR03870, ABC_MoxJ, methanol oxidation system protein MoxJ. This predicted periplasmic protein, called MoxJ or MxaJ, is required for methanol oxidation in Methylobacterium extorquens. Two differing lines of evidence suggest two different roles. Forming one view, homology suggests it is the substrate-binding protein of an ABC transporter associated with methanol oxidation. The gene, furthermore, is found regular in genomes with, and only two or three genes away from, a corresponding permease and ATP-binding cassette gene pair. The other view is that this protein is an accessory factor or additional subunit of methanol dehydrogenase itself. Mutational studies show a dependence on this protein for expression of the PQQ-dependent, two-subunit methanol dehydrogenase (MxaF and MxaI) in Methylobacterium extorquens, as if it is a chaperone for enzyme assembly or a third subunit. A homologous N-terminal sequence was found in Paracoccus denitrificans as a 32Kd third subunit. This protein may, in fact, be both, a component of a periplasmic enzyme that converts methanol to formaldehyde and a component of an ABC transporter that delivers the resulting formaldehyde to the cell's interior [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Energy metabolism, Other]
TLRVCAATKEAPYSTKDGSGFENKIAAALAAAMGRKVVFVWLAKPAIYLVRDGLDKKLCDVVLGLDTGDP
RVLTTKPYYRSSYVFLTRKDRNLDIKSWNDPRLKKVSKIGVIFGSPAETMLKQIGRYEDNFAYLYSLVNF
KSPRNQYTQIDPRKLVSEVATGKADLAVAFAPEVARYVKASPEPLRMTVIPDDATRSDGAKIPMQYDQSM
GVRKDDTALLAEIDAALAKAKPRIDAILKEEGIPLL
>gnl|CDD|274828 TIGR03871, extracellular_solute-binding_protein_family_3, quinoprotein dehydrogenase-associated probable ABC transporter substrate-binding protein. This protein family, a sister family to TIGR03870, is found more broadly. It occurs a range of PQQ-biosynthesizing species, not just in known methanotrophs. Interpretation of evidence by homology and by direct experimental work suggest two different roles. By homology, this family appears to be the periplasmic substrate-binding protein of an ABC transport family. However, mutational studies and direct characterization for some sequences related to this family suggests this family may act as a maturation chaperone or additional subunit of a methanol dehydrogenase-like enzyme
ALRVCADPNNLPFSNEKGEGFENKIAQLLADDLGLPLEYTWFPQRRGFVRNTLNAGRCDVVIGVPAGYEM
VLTTRPYYRSTYVFVTRKGDALDVKSLDDPRLKKLRIGVFAGTPPAHWLARHGLVENVVGYSLFGDRRPE
SPPGRMVEDLAAGEIDVAIVWGPIAGYFAKQAGPPLVVVPLLPEDGGIPFDYRIAMGVRKGDKAWKDELN
AVLDRRQAEIDAILREYGVPLL
>gnl|CDD|274829 TIGR03872, Cytochrome_c-L, cytochrome c(L), periplasmic. This model describes a periplasmic c-type cytochrome that serves as the primary electron acceptor for the quinoprotein methanol dehydrogenase, a PQQ enzyme. The member from Paracoccus denitrificans is also characterized as an electron acceptor for methylamine dehydrogenase, a tryptophan tryptophylquinone enzyme. This protein is called cytochrome c(L) in methylotrophic bacteria such Methylobacterium extorquens, but c551i in Paracoccus denitrificans [Energy metabolism, Electron transport]
LVFRNTVTGEPLDLSGAKEGRDTEAVKQFLETGENPYNGDAEALKKGESLFATACSGCHGHLAEGKLGPG
LNDDYWTYPKNATDKGLFETIFGGANGMMGPQYGNLTLDEMLQIMAWIRHLYTGDPKKAEWLT
>gnl|CDD|163585 TIGR03873, ABC_transporter, proposed F420-0 ABC transporter, ATP-binding protein. This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter
GLRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSR
RARARRVALVEQDSDTAVPLTVRDVVALGRIPHRSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSG
GERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVL
DGGRVVAAGPPREVLTPALIRAVYGVDATVLTHPDTGRPIIAFSPL
>gnl|CDD|163586 TIGR03874, 4cys_cytochr, c-type cytochrome, methanol metabolism-related. This family represents a c-type cytochrome related to (but excluding) cytochrome c-555 of Methylococcus capsulatus. Members contain four invariant Cys residues, including two from a heme-binding motif shared with c-555, and two others
DTAAAKSEDGKYFDKEGVPTFKIAEDGTVDWFTYSGYRRYHSECHVCHGPDGMGSTYAPALKDSVKRMSY
GDFLGVVANGRQNVSAAQNNVMPAFGDNPNVMCYLDDLYVYLRARGTDALGRGRPAKKEDKSEAYKEAEK
ACM
>gnl|CDD|163587 TIGR03875, RNA_lig_partner, RNA ligase partner, MJ_0950 family. This uncharacterized protein family is found almost perfectly in the same set of genomes as the Pab1020 family described by model TIGR01209. These pairs are found mostly in Archaea, but also in a few bacteria (e.g. Alkalilimnicola ehrlichei MLHE-1, Aquifex aeolicus). While the partner protein has been described as homodimeric ligase that has RNA circularization activity, the function of this protein (also called UPF0278) is unknown
RFVLDTSAFTDPELREQLGDEDLCEAVRTFLDLIARARLKLGIECYMPPSVYKELRRFLERNGCDPETLA
KLDTWVVKKSPNRYEVKIPAEIFYEYIEEVRERIDKGLRVAEEHVREAALAGDEISAEHEKKEEVGKIIR
KLREKYREALRKGILDSAEDLDVLLLAKELDAAVVSADEGIRKWAERLGLRFVDARNFPEMLEELL
>gnl|CDD|274830 TIGR03876, cas_csaX, CRISPR type I-A/APERN-associated protein CsaX. This family comprises a minor CRISPR-associated protein family. It occurs only in the context of the (strictly archaeal) Apern subtype of CRISPR/Cas system, and is further restricted to the Sulfolobales, including Metallosphaera sedula DSM 5348 and multiple species of the genus Sulfolobus
LEIPDNELRDVLQLASSIARGKEEERRKRIEKTKKIEGILRIIPLSGNDKKPFEQALKCLNFPTQSTISE
VLKNFNPDMKKECQKVSAPSFVKPEMYEFGRYPGYRGSTKVEVKVDPVYLIVAVAGWVISRLGEAMVSNG
DRVGVNVFTVTVDRLYSVLPNLSGLIPGFKPETAFLLWLAYQVVSSKAEIRSGIRIYAMSDAGGQNPTTI
VGGFSIDVEKLLEKKILRDEQLYAVERVAREALRYDSGKRDYAIRISNLLYEVLMGSKRSEDLMYFANRE
L
>gnl|CDD|163589 TIGR03877, thermo_KaiC_1, KaiC domain protein, Ph0284 family. Members of this family contain a single copy of the KaiC domain (pfam06745) that occurs in two copies of the circadian clock protein kinase KaiC itself. Members occur primarily in thermophilic archaea and in Thermotoga
KRVKTGIPGMDEILHGGIPERNVVLLSGGPGTGKSIFSQQFLWNGLQMGEPGIYVALEEHPVQVRRNMAQ
FGWDVRKYEEEGKFAIVDAFTGGIGEAAEREKYVVKDPTDVRELIDVLRQAIRDINAKRVVIDSVTTLYI
TKPAMARSIVMQLKRVLSGLGCTSIFVSQVSVGERGFGGPGVEHAVDGIIRLDLDEIDGELKRSLIVWKM
RGTKHSMRRHPFEITDKGIIVYPDKVL
>gnl|CDD|274831 TIGR03878, thermo_KaiC_2, KaiC domain protein, AF_0795 family. This KaiC domain-containing protein family occurs sporadically across a broad taxonomic range (Euryarchaeota, Aquificae, Dictyoglomi, Epsilonproteobacteria, and Firmicutes), but exclusively in thermophiles
LFGVPTGIEGLDELFYKVEIEEGKIVRKPLGGIPAYSVINITGVSDTGKSLMVEQFAIKQASRGNRVLFV
TVESPANFVATSLKLRANAMGVDFDKIEDNIILIDAASSTKLRENVPNLLATLAYAIKEYKVKNTVIDSI
TGLYEAKEMMAREIVRQLYNFMKKWYQTALFVSQKRSGHEELSAEAAGGYAVSHIVDGTIVLAKELIMSR
FDASMYKKPIGEIVRLFRIDGCRMCGHDTKTHFLEITETGLVKIGPPLS
>gnl|CDD|163591 TIGR03879, Uncharacterized_protein_MJ1053, probable regulatory domain. This model describes a common domain shared by two different families of proteins, each of which occurs regularly next to its corresponding partner family, a probable regulatory with homology to KaiC. By implication, this protein family likely is also involved in sensory transduction and/or regulation
DVLGGIKKLAERLTWVDSLAEAAAALAREEAGKTASEIAEELGRTEQTVRNHLKGETKAGGLVKLAYEKL
KEG
>gnl|CDD|163592 TIGR03880, KaiC_arch_3, KaiC domain protein, AF_0351 family. This model represents a rather narrowly distributed archaeal protein family in which members have a single copy of the KaiC domain. This stands in contrast to the circadian clock protein KaiC itself, with two copies of the domain. Members are expected to have weak ATPase activity, by homology to the autokinase/autophosphorylase KaiC itself
GIPGLDEMLGGGFPEGHVIVVIGEYGTGKTTFSLQFLYQGLKNGEKAMYISLEEREERILGYAKSKGWDL
EDYIDKSLYIVRLDPSDFKTSLNRIKNELPILIKELGASRVVIDPISLLETLFDDDAERRTELFRFYSSL
RETGVTTILTSEADKTNVFASKYGLIEYLADGVIILKYVRNSDLRDVRLAVEVVKMRRSKHSREIKPYEI
TDSGITVYSEAEIF
>gnl|CDD|163593 TIGR03881, KaiC_arch_4, KaiC domain protein, PAE1156 family. Members of this protein family are archaeal single-domain KaiC_related proteins, homologous to the Cyanobacterial circadian clock cycle protein KaiC, an autokinase/autophosphorylase that has two copies of the domain
RLSTGVEGLDKLLEGGIPRGFFVAVTGEPGTGKTIFCLHFAYKGLRDGDPVIYVTTEESRESIIRQAAQF
GMDFEKAIEEGKLVIIDALMKEKEDEWSLRELSIEELLNKVIEAKKYLGYGHARLVIDSMSAFWLDKPAM
ARKYSYYLKRVLNRWNFTILLTSQYAITTSQAFGFGIEHVADGIIRFRKVVVDGELRRYLIVEKMRQTNH
DKRAWEIDIVPGKGLVLKG
>gnl|CDD|274832 TIGR03882, hypothetical_protein, bacteriocin biosynthesis cyclodehydratase domain. This model describes a ThiF-like domain of a fusion protein found in clusters associated with the production of TOMMs (thiazole/oxazole-modified microcins), small bacteriocins with characteristic heterocycle modifications. This domain is presumed to act as a cyclodehydratase, as do members of the SagC family modeled by TIGR03603
RPWLPVRPSGGEAWIGPLFRPGKPGCWHCLATRLRANRPDEAFLARLQGTPLAGPRPPWLTPAALAAVAA
LAAAELAKWLAGERPRLEGAVLTLDLATLTVSRHPLLPRPQCPVCGDLPDDTPEPAVLALRPKPKTSPGG
YRARSPEETLALYQHYVDPRTGVV
>gnl|CDD|274833 TIGR03883, DUF2342_F420, uncharacterized protein, coenzyme F420 biosynthesis associated. A phylogenetic tree of the DUF2342 family (TIGR03624) consists of two major branches. One of these branches, modeled here, is observed almost entirely to be found in coenzyme F420 biosynthesizing species of the Actinobacterial, Chloroflexi and Archaeal lineages. The few organisms having genes within this family and lacking F420 biosynthesis may either have an undiscovered F420 transporter, or may represent F420-to-FMN revertants. This family includes a Chloroflexus Aurantiacus protein whose crystal structure has been determined (PDB:3CMN_A). This has been annotated as a putative hydrolase, but the support for that assertion is untraceable. There is no cofactor present in the structure
IDWDLAAATAVRLARPGPRLSRAERRAVVADLRRAADRAEGHVRDVTGLEFDEPPPPVRVVDRPGWIDAN
VAGFRRLLGPLEEKLLEGDGAPGALLGAVGGRVTGAQLGAVLAFLSGRVLGQYDPFLLLADAGPPGRLLL
VAPNIVAVERELGVDPHDFRLWVCLHEVTHRVQFTAAPWLRDHLEGELEALLEALDEDVGDLVERLRRAV
RSLRQGTRSGETGLLELVQTPEQREALDRLQALMTLLEGHADHVMDAVGPAVVPSVADIRARFDQRRQGR
GPLDRLVRRLLGLDAKLRQYRRGAAFVRAVVDRVGMEGFNRVWESPETLPTLAEIDDPDRWIARVL
>gnl|CDD|163596 TIGR03884, selenium_binding_protein, selenium-binding protein. This model describes a homopentameric selenium-binding protein with a suggested role in selenium transport and delivery to selenophosphate synthase, the SelD protein. This protein family is closely related to pfam01906, but is shorter because of several deleted regions. It is restricted to the archaeal genus Methanococcus
FIITTADEIPGLQLYYLGIVSTESDNVDEIVENLREKVKAKGGMGLIAFRITCADGKFLGYGTAVKADEG
QFTM
>gnl|CDD|274834 TIGR03885, putative_dehydrogenase_protein, probable non-F420 flavinoid oxidoreductase. This model represents a clade of proteins within the larger subfamily TIGR03557. The parent model includes the F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554) and many other proteins. Excepting the members of this family, all members of TIGR03557 occur in species capable of synthesizing coenzyme F420. All members of the seed alignment for this model are from species that lack F420 biosynthesis. It is suggested that members of this family bind FMN, or FO, or a novel flavinoid cofactor, but not F420 per se [Unknown function, Enzymes of unknown specificity]
IGYHASHEQFAPSDLLQYVQAAEQAGFDAVMSSDHFHPWSERQGQSGFAWSWLGAALQATSLPFGIVTAP
GQRYHPAILAQAAATLAEMFPGRFWIALGSGEALNEHITGDAWPAKAERNARLRECAEIIRALLRGETVT
HRGLVTVEEARLYSLPETPPPLIGAALTVETARWAGAWADGLITVNQPPEKLQEIVEAFREGGGAGKPVY
LQVQLSYAPTEEEALAAAHEQWRNNVLPPEVLWDLRRPEDFDAAARSVRPEDVDEHVRISDDLGQHAEWI
QELADLGFDEIYLHNVGRDQERFIDDFGEHVLPAL
>gnl|CDD|188401 TIGR03886, hypothetical_protein_SlinDRAFT_56750, spore photoproduct lyase family protein. This uncharacterized radical SAM domain protein occurs rarely and sporadically in species that include select Alphaproteobacteria and Actinobacteria, and in Deinococcus deserti VCD115. It is a distant but full-length homolog to the Bacillus subtilis spore photoproduct lyase (spl), which monomerizes thymine dimers created as DNA damage by uv radiation
IRRIYAEPAAAALPRGREILARFPDAERVEVPSHWNIPELHGNEGNVEDWVRIKRETLVLGVKKTLTARP
NGRSADFIAPSTANGCAMACAYCYVPRRKGYANPITVFTNIEQITAALRRHVARQGPKPEPNQCDPRSWV
YDIGENSDCSVDALISDNVRDLVALFRGLPNAKASFATKFVNRDLLTYDPRGRTRIRFSLMPAHIAKLVD
VRTSPIAERIAAIDDFVEAGYEVHVNFSPVVLYEGWEADWRELFRQLDDSLSPAAKAQLAAEVIFLTHNE
GLHQVNLGWHPKAEELLWRPDLQESKRSQNGGWNVRYRSGWKGKWVARFTALVAAELPYCRVRYAF
>gnl|CDD|188402 TIGR03887, Thiocyanate_hydrolase_subunit_gamma, thiocyanate hydrolase, gamma subunit. Members of this family are the gamma subunit of thiocyanate hydrolase. This family is closely related to the nitrile hydratase, alpha subunit (TIGR01323)
EEVSDFEILETAIRELAIEKGLFSAEDHRRFTEWAETLGPLPAARLVAKAWLDPEFKKLLLADGVEASKA
VGVDWLTPTGFGTPSDYTNLRVLEDTPTLHHVIVCTLCSCYPRPILGQSPEWYRTPNYRRRLVRWPRQVL
AEFGLQLPPDVEVRVHDSNQKTRFMVMPMRPEGTDGWTEDQLAEIVTRDCLIGVAVPKPG
>gnl|CDD|274835 TIGR03888, nitrile_beta, nitrile hydratase, beta subunit. Members of this protein family are the beta subunit of nitrile hydratase. The alpha subunit is represented by model TIGR01323. While nitrile hydratase is given the specific EC number 4.2.1.84, nitriles are a class of compounds, and one genome may carry more than one nitrile hydratase. The enzyme occurs in both non-heme iron and non-corrin cobalt forms [Energy metabolism, Amino acids and amines]
MNGVHDLGGVDGFGPVDPEPNKPVFHAEWEKRAFAMFAAAGALGAFNIDEVRHGIERMNPADYLESSYYE
KWVIGVATLLVEKGYLTEDELDERAGPVGSPPKPGVKAALSPFELVAPVLSRGRPARRPTDAPPRFEVGD
RVRVRNEYPAGHTRLPAYVRGKVGVVEHRHGEHVFPDAAGHGLGEAPEPLYHVEFTAEELWGDDADPGSS
VYADLFEPYLEPA
>gnl|CDD|188404 TIGR03889, nitrile_hydratase_activator_P14k, nitrile hydratase accessory protein. Members of this protein family are found in operons with the alpha and beta subunits of nitrile hydratase, an enzyme with Fe(III) or Co(III) at the active site, and appear to be accessory proteins for maturation or activation of the enzyme. This protein is homologous to the beta subunit (see TIGR03888)
FDEPWQAQAFALTVHLHEAGLFPWSEWAERLSAAIKRAGASRGLDGGDDYYDHWLAALERLVVELGLAAP
EDIA
>gnl|CDD|188405 TIGR03890, hypothetical_protein_WH5701_11654, nif11 domain/cupin domain protein. Members of this protein family occur exclusively in the Cyanobacteria and contain both a nif11 and a cupin domain. The function is unknown
AEQDLQRFLEKVRQLQALVQSLETDPERREQLAACSDHNQVVALARAWGFEIGRRWGEPEGASRSAGPDN
LLQTPCPPPGEESEDVLLEGPGWRLELIHSNAASSPEGFWYDQSEHEWVLLLRGSARLRFEDPDEAVDLS
VGDQLLIPPHRRHRVERTDPHPGTLWLALYW
>gnl|CDD|274836 TIGR03891, lantibiotic_dehydratase, thiopeptide-type bacteriocin biosynthesis domain. This domain occurs within longer proteins that contain lantibiotic dehydratase domains (see pfam04737 and pfam04738), and as single-domain proteins in bacteriocin biosynthesis genomic contexts. Three named genes in this family, SioK in Streptomyces sioyaensis, TsrD in Streptomyces laurentii, and NosD in Streptomyces actuosus, all occur in regions associated with thiopeptide biosynthesis [Cellular processes, Toxin production and resistance]
WLYLKIYGPPSTADELLADHLPPLLDELEAAGLIDKWFFIRYRDPEPHLRLRFHGAPPENYALVLSRIGD
WLAPLRESGLISRVQIDTYEPEIERYGGPAAMELAEDLFHADSRLVLDLLSKEDSELDRRLLAALSIVSL
LRAFGLDLEEQLELLARVAEHFKYEKPLKRQLRDRYRALRNPLNNWTALAATPGGEPILKILQERSEALA
AYGEALAALAEAGTLTRGLRSILASLIHMHWNRLFGIDRAAERVIYRLARHTI
>gnl|CDD|200334 TIGR03892, hypothetical_protein, thiazolylpeptide-type bacteriocin precursor. Members of this protein family are the precursors of a family of small bacteriocins (i.e. microcins) with thiopeptide type modifications, a highly modified subclass of heterocycle-containing peptide antibiotics. Members tend to be found clustered in genomes with proteins recognized by TIGR03891 and proteins/domains annotated as lantibiotic dehydratase (pfam04737, pfam04738), and with a cyclodehydratase/docking protein fusion protein characteristic of heterocycle formation. The seed alignment includes both an N-terminal leader peptide region and a C-terminal low-complexity region consisting mostly of Cys and Ser residues. Members with known function block translation by inhibiting translation factor activity [Cellular processes, Toxin production and resistance]
LEELDIETFEISDYADESEMGASGSTSCSSSSSCTTTSCTCSC
>gnl|CDD|274837 TIGR03893, conserved_domain_protein, type 2 lantibiotic, SP_1948 family. This model recognizes a number of type 2 lantibiotic-type bacteriocins, related to but distinct from the family that includes lichenicidin and mersacidin. Sequence similarity among members consists largely of a 20-residue block of conserved sequence that covers most of the leader peptide region, absent from the mature lantibiotic. This is followed by a region with characteristic composition for lantibiotic precursor regions, rich in Ser and Thr and including a near-invariant Cys near or at the C-terminus, involved in cyclization. Members of this family typically are shorter than 70 amino acids [Cellular processes, Toxin production and resistance]
NNKKIVGDSFEELSIEEMALIQGSGDVNARTTPICVTVAAAVSSAAASFVVSYALSAVTKC
>gnl|CDD|188409 TIGR03894, chp_P_marinus_1, conserved hypothetical protein, TIGR03894 family. This protein family is restricted to the Prochlorococcus and Synechococcus lineages of the Cyanobacteria, and is sporadic in those lineages. Members average 100 amino acids in length, including a 30-residue, highly polar, low complexity region sandwiched between an N-terminal region of about 60 residues and a C-terminal [KR]VVR[KR]RS motif, both well-conserved. The function is unknown [Hypothetical proteins, Conserved]
ADKELLKEVALELWNTVKKLRPGLPKAPRAQLVLKALLTIGDLSDQLQAAMVVGVIAEQEPDDEENEGED
SETKEDSESESESSREGPRVVRKRS
>gnl|CDD|274838 TIGR03895, hypothetical_protein, cyanobactin maturation protease, PatA/PatG family. This model describes a protease domain associated with the maturation of various members of the cyanobactin family of ribosomally produced, heavily modified bioactive metabolites. Members include the PatA protein and C-terminal domain of the PatG protein of Prochloron didemni, TenA and a region of TenG from Nostoc spongiaeforme var. tenue, etc
HGTHVASIIFGQPGSPVPGIAPKCRGLIIPIFFDGARRISQLDLARAIELAVNAGANIINISAGQLTDTG
EAERWLEDAVRLCQENNILIVAAAGNDGCECLHVPAALPGVLAVGAMDDDGRPLDFSNWGEAYQAQGILA
PGENILGAQPGGETVRLSGTSFATPVVTGVAALLLSLQLQQGETPDPQAVRTALLNSAIPCDPEDDEECE
RCLAGRLNIPGAIQLLTGETMSEGLVTSEQDGVEEASGCGVQGTIESSTSVIPPGRAAEPAPVSIPVAAP
GESATPAAAQIELSAGVLPNAISPATPVRPAANGVTPSQAPSAEPQLVYALGTLGYDFGTEARRDSFKQL
MPAVVADGVQVPANPYDPRQMVDYLDDNPSEAKSLIWTLNQELTPIYAIEPVGAFAREIYEALQELLAGQ
LEPEDSEEYVERVSIPGRLTGRTVKLFSGQVVPVIYPQDPRGMYGWKVNTLVSAALEAVRTEAGEASDES
IRKTLTSFLNRVYYDLRNLGQTSQDRALNFAATNAFQAASTFSQAVATGMELDSITVEKSPFCRPDSDCW
DVKLKFFDPENSRRAKKVYRFTIDVSDLIPVTLGEVRSWSVP
>gnl|CDD|274839 TIGR03896, cyc_nuc_ocin, bacteriocin-type transport-associated protein. Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797
IDWMVAIGHQREIAAGTTLIEEGKAADFLFILLDGTFTVTTPQPEDNPLTRAFELARLSRGEIVGEMSLL
ETRPPVATIKAVPKSRVMSIPVGELAAKLQSDVGFAAHFYRAIAIKLALQIQNQNHQLHRRNGADSEPLR
KVLFIFGELHESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEASLSISPDGPGREVGSSRRGE
ILGETPFLNGSLPGTATVKAIENSVLLAIDKQQLAAKLQQDVGFASRFYRVIASLLSQRSRDQVSSRGYA
RRVYLREGLEYDEELDLNTLDRMSIAGKRFDWLCGRL
>gnl|CDD|274840 TIGR03897, Lantibiotic_mersacidin_modifying_enzyme, type 2 lantibiotic biosynthesis protein LanM. Members of this family are known generally as LanM, a multifunctional enzyme of lantibiotic biosynthesis. This catalysis by LanM distinguishes the type 2 lantibiotics, such as mersacidin, cinnamycin, and lichenicidin, from LanBC-produced type 1 lantibiotics such as nisin and subtilin. The N-terminal domain contains regions associated with Ser and Thr dehydration. The C-terminal region contains a pfam05147 domain, which catalyzes the formation of the lanthionine bridge [Cellular processes, Toxin production and resistance]
EFLLPFVAYARERLKKTLSELSQIILSEEILEQLLRSLAERLLNLSSRTLILELNIAREEGLLQGETPEE
RYQYFINQLLSDGEYLLDLFEEYPVLARLIATIIENWIENTKEILQRLAEDRSEIQQTFGIGSDLKLTSI
KLGLGDSHNGGRSVAILTFSSGLKLVYKPRSLAIDAAFQDLLEWLNQKGLNLPLKTPKVLDRDDYGWMEF
IEHEPCESEEEVERFYQRAGVLLALLYLLNGTDFHYENIIAHGEYPVLIDLETLFHPRVPDDEEGESAED
KASELLSDSVLRTGLLPQWIFGGDDGAGIDLSGLGGKEGQLTPFKVPVIVNINTDEMRIEREEVVLPKKK
NLPVLNGKVVDPSDYIDDIIDGFREMYRLLLENKDELLEEDGPLAAFKGLKVRVVLRPTQVYAKLLQESY
HPDYLRDGLDREKLLENLWLYPEEKPKLWRIIPSEIEDLLNGDIPYFTTRTDSKDLYDSDGTEIPDFFKT
SGLERVLERIKDLSEKDLEEQLRLIRMSLLALLENPGSYDLPKTASKKPSNPLSKEDLLEEAKKIADRLL
DNAIEGDDGSVNWIGLNLSFDEERWSLGPLGNDLYDGLAGIALFLAYLAALTGDKRYRDLARKALQPLRK
YLETLVELARSMGLGAFSGLGSIIYALAHLGQLLNDPELLNDAKKILNRLEELIIKDEEFLDLIGGAAGA
ILVLLNLYEVTGDPEVLELAIACGEHLLKQAVEQEGGAAWKTSQSNKPLTGFSHGAAGIAWALLRLYKVT
GDQRYLEAAKEALAYERSLFDPEEGNWPDLREDGGPQFPVAWCHGAPGILLSRLGLLEILDDDEIREDIE
IALETTLKYGFGDNDSLCHGDLGNLEILLEAAKVLDDEELQELARRIASQVLARLTKNGRYRLGLPRGVE
SPGLMTGLAGIGYGLLRLANP
>gnl|CDD|274841 TIGR03898, hypothetical_protein_SrosN15_20203, type 2 lantibiotic, mersacidin/lichenicidin family. This model recognizes a number of type 2 lantibiotic-type bacteriocins, including mersacidin and lichenicidin. Members often are found as gene pairs encoding two-chain bacteriocins. Maturation is accomplished, at least in part, by a LanM-type enzyme (TIGR03897). This model describes only the leader peptide region [Cellular processes, Toxin production and resistance]
EIIRAWKDPEYRSSLSDAERAALPANPAGLTELSDEELAAITGG
>gnl|CDD|274842 TIGR03899, hypothetical_protein, TIGR03899 family protein. Members of this protein family are conserved hypothetical proteins with a limited species distribution within the Gammaproteobacteria. It is common in the genera Vibrio and Shewanella, and in this resembles the C-terminal domain and putative protein sorting motif TIGR03501. This model, but design, does not extend to all homologs,but rather represents a particular clade
IARQHGLDSELYRPSDATVAERAQHRQRKLQEQQQKNLESILKLALSYCPDEVTGEDPDPDWLYRFFQMA
EDIHNRSMQELWAKILAREITNPGSFSLRTLKTLKQMTQREAQIFQKALSLACRFGNDTSLKLLLGYKKQ
GGLFSLFRKPTTTNINLGQFGLPYSSLLTLIELGLLHSTELESGELNAGQPLPLSYQGKKLTLTPKSKGL
TLTYYRFTPTGDELAQLIGPKPNNEYKQALKALLSQDFKV
>gnl|CDD|274843 TIGR03900, carboxyl-terminal_protease_family_protein, putative carboxyl-terminal-processing protease, deltaproteobacterial. This model describes a multidomain protein of about 1070 residues, restricted to the order Myxococcales in the Deltaproteobacteria. Members contain a PDZ domain (pfam00595), an S41 family peptidase domain (pfam03572), and an SH3 domain (pfam06347). A core region of this family, including PDZ and S41 regions, is described by TIGR00225, C-terminal processing peptidase, which recognizes the Prc protease. The species distribution of this family approximates that of largely Deltaproteobacterial C-terminal putative protein-sorting domain, TIGR03901, analogous to LPXTG and PEP-CTERM, but the co-occurrence may reflect shared restriction to the Myxococcales rather than a substrate/target relationship
YDLRSLPVLNWTILTVSDNYVDPKRVDPKEMLLAALEAVERHVPEVLVDPDADPGKLTVTVGDQEKRFDI
AEVDSLWKVSDRLREVFEFLQDHLRLTAEDLRDVEYAAVNGMLSTLDPHTNLLRPEAFKEMKLNTRGAFG
GLGIVIGMRDRNLTVVRVIPGTPAARAGLQRNDVIVKIDDESTVNMTLNDAVGRLRGPPDTKVTIWVRRE
GWDEAKRFELTRAMIKVESVEARMLPGNVGYLRLRTFQATTTRELLAALQDLRSKGQLKGLVLDLRGNPG
GLLEQAIEVSDLFLDQGTIVSTVGASERREEKKATGDTVVEAKVPVVVLVNEGSASASEIVAGALKNLDR
AVIIGRQTFGKGSVQVLYDATPADRSALKLTIAQYLTPGDRSIQSVGVTPDIELLPVRVLEEELRYYAPF
RSMRERDLSAHLPNAVAAAHAEAALALEKPPLELRYLSVSPQRAQEEGELPPEIALQEEGGDAAERFLRD
FEIRFARDLALRAPSTRRREQLEALPAIVEQRQAEEDERIAAALGKLGVDWADAPAAGPGDAQLEVSVSP
VTDKPGALHRAGETMTLTVTVTNPGTEPLYRVRAWTDSDNNYLDRRELLFGAIPPGESKSWKVKLKLPKD
ALSRVDRLTVHFEVAEGAAPADASVAVTVVGADRPVFAFSYQIIDDPHLGNGDGLLQRGETVHLRLTVKN
AGKGPAPDTRVLLRNLSGDGLFLEKGRFKLGALKPGETKTVDFGFEVKPGLPSDELPLELTVGDAKLRES
VMEKLRFPISPPRDARGEASGGKVVGDEEADLYNGAAESAPVVARLPAGAVLPVTGSAGGWYRVRLGKGR
FAFVPASELRAAKGGKARAAGAPTAVYQVDPPRIVLADDPGAGGPVTEDDTVTLSGVALDPERVRDVYVF
VNNAGPAQPERKVFYKANRAGAAPKRLEFSAEVPLSPGNNVVTVVARENDDVMSRRTLVVRRR
>gnl|CDD|274844 TIGR03901, hypothetical_protein, MYXO-CTERM domain. This model describes MYXO-CTERM, a C-terminal putative protein sorting domain, analogous to LPXTG (TIGR01167) and PEP-CTERM (TIGR02595). It is restricted to the Myxococcales, a division of the Deltaproteobacteria, with over 60 members occurring in Plesiocystis pacifica SIR-1. An example protein is TraA, involved in outer membrane exchange (lipids and proteins) through which one strain of Myxococcus can repair a mobility defect in another. The trusted cutoff for this model is set artificially high to avoid false positives, and consequently only about half of all members are recognized
GCSCSSGGGPPAPPGLLGLLALGLLAGRRRR
>gnl|CDD|274845 TIGR03902, hypothetical_protein, rhomboid family GlyGly-CTERM serine protease. This model describes a rhomboid-like intramembrane serine protease. Its species distribution closely matches model TIGR03501, GlyGly-CTERM, which describes a protein targeting domain analogous to LPXTG and PEP-CTERM. In a number of species (Ralstonia eutropha, R. metallidurans, R. solanacearum, Marinobacter aquaeolei, etc) with just one GlyGly-CTERM protein (i.e., a dedicated system), the rhombosortase and GlyGly-CTERM genes are adjacent
SDLLAYDRAAILDGEWWRLLTGHFVHLNWWHLLMNLAGLLLLWALFGRHLRARRLLLLLLLLSLLISLGL
LLFLPSLQWYVGLSGVLHGLFAWGALRDIRYGRRSGWLLLLGVIAKLAWEQLFGASAFTAALIGAPVATE
AHLAGAISGLLIAL
>gnl|CDD|274846 TIGR03903, TOMM_kin_cyc, TOMM system kinase/cyclase fusion protein. This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein [Cellular processes, Toxin production and resistance]
MTGHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFAVFEYVPGRTLREVL
AADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLLPGVRDADV
ATLTRTTEVLGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVDVSLP
PWIAGHPLGQVLRKALNKDPRQRAASAPALAERFRALELCALVGILRMGEGAGREAIAAPLVASGTLDGE
TGERRQLTALCCHVGLSTPPEPAEGVEEDDEELDLLLRSWLTRCADIAVRYGAHVGGVLGDTLLFYFGYP
SAAERDARRAARAALEMVRQAGRKGEAAAGEGKWRVEIAAGIHTGLVLAQAPHASGGTTPNAAVRMQAQA
EPGQILVSEAARKLLRRHADFDPTALEEAAAGAESQPVFELLGERAARTPFTSLDGGTTTPLVGRSRELE
ALRRRWRDTVAGRGRAILVVGEAGIGKSRLVHELVEKVRGRPHAFLECRCLPEQENHALFPVLRLVRAHW
GLDRNAPPEQALAAIDALLTANGCDLAEARPLLAGWLSLPGGAYPVPEWSPARQKELLFDVLVQLLFSLA
QGAPVLLLVEDLHWADSATLEFLAALAEDPATARLCLVLTARPERLPRWRMGAALRVQLRRLDRARAEEM
VSGLLQPTPLPRAVLDQLVSRTDGVPLFIEELARMLMETLPGRDGELPSRAQADRLPIPSTLRDSLELRF
DRLGPARETAQLAATIGREFDAELLADASPHDEAELDRDLRALADARLVYAQHRVGNPSYLFRHALIRDA
AYESMLRAMRREVHERVAAALLARFPRVVAARPDLLALHFARADAFAQAVPYGIKAARRALMRSLNDEAI
RYATAVLAWLEVVDEAERAEDELGLDGTLIHARMARHGWADPQIRERIEQSLELVDLLGDSPLVAPALWT
LGTYHHVAGHRVGVRRIGERLLALARQSGDAGLVVAADTGLGMALWVEGRYAEAREAFDAALALYDARRD
AKHAVYLGLDTRAWAQAARAFVRWGLGDDDLAAAYARSAVTWATCLDHLPSLGLTMMYLARFLQAQGDRD
QARAVADAALELSHRYGLPAVEVYAAVIRAWAVRDRAGARADIDALRQSGCGLGLTYYASLLAELDAERG
RYGAALAIIDECLALAESPDERYYLAELLLKKGRCLRAAGERAVAAEACLRRAVEVARQQGMKRIERKAA
AALREL
>gnl|CDD|274847 TIGR03904, putative_radical_SAM_protein_YgiQ, uncharacterized radical SAM protein YgiQ. Members of this family are fairly widespread uncharacterized radical SAM family proteins, many of which are designated YgiQ [Unknown function, Enzymes of unknown specificity]
FLPTTREEMEARGWDELDVILVTGDAYVDHPSFGAAIIGRLLESAGYRVGIIAQPDWRSPEDFKRLGRPR
LFFGVTAGNMDSMVNHYTAAKKRRSDDAYTPGGKAGKRPDRAVIVYTNLIREAFKDVPIIIGGIEASLRR
FAHYDYWSDKVRRSILLDSKADLLVYGMGERAIVEIARRLAAGEPIKDIRDIRGTAYITKEKPEGWDYVE
LPSYEEVSADKEAYAEAFRLQYLEQDPINGRTLVQKHGDRYVVQNPPALPLSTEELDAVYALPYTRRPHP
SYKKAGGIPAIEEIKFSITSHRGCFGGCSFCAITFHQGRIIQSRSEESILREAKRLTKMPDFKGYISDVG
GPTANMYGMSCKKQEKHGACRRKSCLFPKPCPNLKVDHSPYLELLRKLRKLPGVKKVFIRSGIRYDLLLA
DKDDEYLRELVRHHVSGQLKVAPEHISDKVLKLMGKPGIEVFERFKEKFEKINKKAGKKQYLVPYLISSH
PGCTLKDMVELAEYLKKLGFRPEQVQDFTPTPGTLSTCMYYTGLDPYTGEPVYVPKTPREKRLQRALLQ
>gnl|CDD|188420 TIGR03905, conserved_hypothetical_protein_TIGR03905, uncharacterized protein TIGR03905. This model describes a family of conserved hypothetical proteins of small size, typically ~85 residues, with four invariant Cys residues. This small protein is distantly homologous to a C-terminal domain found in proteins identified by N-terminal homology as ribonucleotide reductases. The rare and sporadic distribution of this protein family falls mostly within the subset of bacterial genomes containing the uncharacterized radical SAM protein modeled by TIGR03904 [Unknown function, General]
ITYITSGVCSTEIQFDIEGDKVKEVRFSGGCDGNLKAISKLVEGMPVKDVIQKLEGITCGDKATSCADQL
AKALEQAA
>gnl|CDD|274848 TIGR03906, quino_hemo_SAM, quinohemoprotein amine dehydrogenase maturation protein. Members of this protein family are radical SAM enzymes responsible for post-translational modifications to the gamma subunit of quinohemoprotein amine dehydrogenases. Ono, et al. () suggest that this protein is responsible for intrapeptidyl thioether cross-linking rather than cysteine tryptophylquinone biogenesis in the gamma subunit [Protein fate, Protein modification and repair]
HNIHTIEVDGRRVLLHVPSTSIFALDEVARSVLDLLRQRPMVYGEDLQARFAGRYSPADLADLIRELISL
GIVSDEPREPEIPPVIPVERYPLSTLVLNVNTGCNLSCTYCYKEDLTTPSKGPKMSLETAKASVELLLAE
SGHRERVNVVFFGGEPLTNFPLIRAVVEYAEQRAAAAGKQIEFSLTTNATLLTEEIVDFLNAHRFGITVS
MDGPKALHDKHRITIGGKGTYDVVARKVRMLLERYTSRPVGARVTLTNGVTDVAGIYRHLKDELGFAEVG
FAPVTSGPISSFNLDDNELDEVFASMKALGREYVAAALEGRNIGFSNMHQLITDLIQGTRKVLPCGAGLG
LLAVDHKGDLSLCHRFTGSDLPTFGNVDSGIDKDKLSDFLSRAQDRSKYGCATCRIRSLCAGGCYHESYA
RYGDPFHPTYHYCELIREWVDFGIEAYGEIAARNPAFLERHITPRSA
>gnl|CDD|211887 TIGR03907, QH_beta, quinohemoprotein amine dehydrogenase, beta subunit. Quinohemoprotein amine dehydrogenase is a three subunit enzyme with both a heme group and a cysteine tryptophylquinone group derived by post-translational modification of the gamma subunit. This model describes the beta subunit. This enzyme catalyzes oxidative deamination of primary aliphatic and aromatic amines () [Energy metabolism, Amino acids and amines]
HEYLVVVNRPNNLHVVDLASRKVYKTCKMPDAFGPGTAQVSPDGKTAYVLNNRYEDVYGIDLDTGKNVFR
ADLSSAGERGKAIFAFALSPDGKELYVVQNPTQLLRDEYKVKPPRIAVYDTAAGLDAKPVRTFPAPRQVT
LLAYSDDGDTLYAAGPDMYKFDVKTGKFEVTLPIRHWQRPGYSAPDVLYVWPQQEPRHDFSTPYTVARFK
KDPQDPATFLYGLLSVDLKTGKLHTQEFEPLTEIYFSGARSPKDRNEAYGVLNRLAKYDIKQGKLLKAVD
LEHTYYCVNVSSDGKKLYIGGTFNDIAVYDAETLEKVGNIKLPGGPDMSLTTLRVFVR
>gnl|CDD|274849 TIGR03908, QH_alpha, quinohemoprotein amine dehydrogenase, alpha subunit. Quinohemoprotein amine dehydrogenase is a three subunit enzyme with both a heme group and a cysteine tryptophylquinone group derived by post-translational modification of the gamma subunit. This model describes the beta subunit. This enzyme catalyzes oxidative deamination of primary aliphatic and aromatic amines () [Energy metabolism, Amino acids and amines]
AAPGIPVGEQLLNEKCGACHTADAKGKLSRISWVRKTPEGWDMTVARMSRLHGLQLSDDERRAIVKYLAD
TQGLAPSETAGVRYLLERRLNTVEHAPNEEITQMCARCHSYARIALQRRTEAEWEKLVNFHLGQFPSAEY
QAMGRDRNWWPIALKEAVPYLAKHYPLDTPAWTAWQAARPQAAKLSGRWVVSGHLPGKGAYTGTMTLAPA
GEGDRYSVSMSLRYADGSTLTGKGKAIVYTGYEWRGTLKLGDQETRQVFALSADGSSLSGRWFEKDNDEI
GGDFIAVRADAGPRVLAVQPGMLRAGTEAEVTLVGVGLDGDVDLGKGVEVVKVVSQSPGEVVVRVRVAAD
APVGARDVSVGSSVLGAALAVYQRIDYVKVEPAFAVARLGGNGGPTPKVQAQFEAIAFLNGADGKPGTAD
DVRIGVVPASWSVENFDEVAAKDEDTKYAGSMEDNGLFTPADAGPNPARKMSTNNVGNLKVIATVKDGGK
TLTGEGHLIVTVQRWNDPPI
>gnl|CDD|188424 TIGR03909, carbamoylphosphate_synthase_large_subunit, pyrrolysine biosynthesis protein PylC. This protein is PylC, part of a three-gene cassette that is sufficient to direct the biosynthesis of pyrrolysine, the twenty-second amino acid, incorporated in some species at a UAG canonical stop codon [Amino acid biosynthesis, Other]
TVCIIGGKLQGVEAAYLSKKAGWKVVLIDRNRKALIANMADEFICFDITEEPEKLVAISKNVDLIIPANE
NLEVLEFIKDIALKAGCPVLFDFDAYRISSSKIRSKELFASIDLPTPKPWPGCGFPYFVKPSCESGSEGV
YIINDRRELNELLKLGNLDNWVKEEYLEGPSYSIEVIGDGGNYQVFQITELEMDATYDCKRVLAPAQLDT
EKQPEFREQAYKLARALNLKGIMDVEVILHDEKLKVLEIDARLPSQTPTVVYHSTGINMVELLGKAFPGG
LKRREIQEIGETRYVIYEHLKVRSNGLIEPVGEHILSMAGRLHILKKFFGADEAIEIYDRDKEEWVFTLI
IWGKDREEAWAKRTKVIKRIMQEF
>gnl|CDD|188425 TIGR03910, biotin_synthase, pyrrolysine biosynthesis radical SAM protein. This model describes a radical SAM protein, PylB, that is part of the three-gene cassette sufficient for the biosynthesis of pyrrolysine (the twenty-second amino acid) when expressed heterologously in E. coli. The pyrrolysine next is ligated to its own tRNA and incorporated at special UAG codons [Amino acid biosynthesis, Other]
ATLDLEEILEKIITGSELSDEDIRALLSLSDPDEMEKLFYVAREVRNKYFGNRVFLYGFLYFSTFCKNNC
AFCYYRKSNHAIRRYRKTREEIKAAARALADSGVHLIDLTMGEDPYYHNDPRGFERLAELVRMVKEETGL
PVMISPGVVDNETLKKLKEAGANWYACYQETHDRELYNKLRVGQSFDERMNSKRHAKRIGYLIEEGILTG
VGDDIEDTAISLRGMKSLDADQVRVMTFVPQKGTPLEGKDVEGNLAELRIIAIMRLLFPDRLIPASLDVD
GIDGLVHRLNAGANVVTSIIPPNSGLAGVANYSRDIAERDRDVKSIIPILKSMGLEPATQAEYEKWL
>gnl|CDD|188426 TIGR03911, hypothetical_protein_DtoxDRAFT_11660, pyrrolysine biosynthesis protein PylD. This protein is PylD, part of a three-gene cassette that is sufficient to direct the biosynthesis of pyrrolysine, the twenty-second amino acid, incorporated in some species at a UAG canonical stop codon [Amino acid biosynthesis, Other]
TRLTPEDIESILRQLNEYDATLLAKTGKRLAGIAAHAYGTTSADIPDPGKVAVVPITCGNGIIGGFSESV
AAITEFLGFRAFVTDSPDVKGYAEAVERGAEIIFMADDNRFIAHNLKTGKIADNSEATGRGYAAALDCLT
GGLKSKDVLVIGLGPVGRAAAFHLVDKGFHVYVYDKNLEVSEKLAQDLCSIGIERELDEAMHKFSAIFEA
TPEAGTIREDHLHDDCCISAPGIPLGIQAELIEKVEGRLVHDPLQIGVATMLYSIL
>gnl|CDD|188427 TIGR03912, hypothetical_protein_DtoxDRAFT_11670, pyrrolysyl-tRNA synthetase, N-terminal region. PylS is the enzyme responsible for charging the pyrrolysine tRNA, PylT, by ligating a free molecule of pyrrolysine. Pyrrolysine is encoded at an in-frame UAG (amber) at least in several corrinoid-dependent methyltransferases of the archaeal genera Methanosarcina and Methanococcoides, such as trimethylamine methyltransferase. This protein occurs as a fusion protein in Methanosarcina but as split genes in Desulfitobacterium hafniense and other bacteria. This model describes the small, N-terminal region [Protein synthesis, tRNA aminoacylation]
KKVPLDNLVEKIGLWPSRSGTLHGIKSHEISGNTIEIETHCGERFIVNNSRSSRAARWLRHKKYRKVCKR
CRVPDEKIQKFSTTMMEQK
>gnl|CDD|188428 TIGR03913, radical_SAM_domain_protein, Y_X(10)_GDL-associated radical SAM protein. This narrowly distributed protein family contains an N-terminal radical SAM domain. It occurs in Pseudomonas fluorescens Pf0-1, Ralstonia solanacearum, and numerous species and strains of Burkholderia. Members always occur next to a trio of three mutually homologous genes, all of which contain the domain pfam08898 as the whole of the protein (about 60 amino acids) or as the C-terminal domain. The function is unknown, but the fact that all phylogenetically correlated proteins are mutually homologous with prominent invariant motifs (an invariant tyrosine and a GDL motif) and as small as 60 amino acids suggests that post-translational modification of pfam08898 domain-containing proteins may be its function. This view is supported by closer homology to the PqqE radical SAM protein involved in PQQ biosynthesis from the PqqA precursor peptide than to other characterized radical SAM proteins [Unknown function, Enzymes of unknown specificity]
DPRPARYLSDTDLKRFVPVHVVWEITLACDLKCLHCGSRAGHRRPNELNTAECLEVIDSLARLGTREVSL
IGGEAYLRKDWTQLIRAIRSHGMYCAIQTGGRNLTPKRLQQAVDAGLNGVGVSLDGLAPLHDKVRNVPGS
FDRALDTLRRARAAGLAVSVNTQIGAQTMPDLPALMDTIIELGATHWQIQLTVAMGNAVDNDELLLQPYQ
LLELMPLLARLYKEGVSRGLLMNVGNNIGYYGPYEHLWRGFGDERVHWSGCAAGQTVIALEADGTVKGCP
SLATVGFSGGNVRDMSLEDIWRTSEGIHFGRLRSVDDLWGFCRTCYYADVCRGGCTWTSHSLLGKPGNNP
YCHYRVLELQKQGLRERIVKVQDAGPASFAVGRFDLVTERIADGEPVASVVRSGQVIELAWKNQGKRSPE
VGRVPPQLALCRSCLSYIHAHEQTCPHCGADVAAAAAAHRQDAQRRQALMNTLEQLL
>gnl|CDD|274850 TIGR03914, SPO1_DNA_polymerase-related_protein, uracil-DNA glycosylase family domain. This model represents a clade within the uracil-DNA glycosylase superfamily. Among characterized proteins, it most closely resembles the Thermus thermophilus uracil-DNA glycosylase TTUDGA, which acts uracil (deamidated cytosine) in both single-stranded DNA and U/G pairs of double-stranded DNA. This domain may occur either as a stand-alone protein or as the C-terminal domain of a fusion with another domain that always pairs with a particular radical-SAM family protein
LIPELIAGAEARERAMAAAAPTEPPPRHHRLAPAAADDESPGTLAALRAAARACRRCPLHCPATQTVFGE
GPEDAPLMIVGEQPGDQEDLAGRPFVGPAGQLLDRALAEAGIDRSRAYVTNAVKHFKFEPRGKRRLHQKP
NAGEVDACRWWLEAERALVRPKLVVALGATAAQALLGKGVRISKVRGRPIRLDDGSELLVTVHPSYLLRL
PDEEAREEEYARFVEDLRAV
>gnl|CDD|274851 TIGR03915, putative_DNA_metabolism_protein, probable DNA metabolism protein. This model represents a conserved hypothetical protein that almost invariably pairs with an uncharacterized radical SAM protein. The pair occurs in about twenty percent of completed prokaryotic genomes. About forty percent of the members of this family occur as fusion proteins, where the C-terminal domain belongs to the uracil-DNA glycosylase family, a DNA repair family (because uracil in DNA is deamidated cytosine). The linkage by gene clustering and correlated species distribution to a radical SAM protein, and by gene fusion to a DNA repair protein family, suggests a role in DNA modification and/or repair
YLYDGSFEGLLTAIYEAYARKIEPENIVWEGEAQPDLFDEYVEVATDPEKAERVWRSIKKKISPEAFRQL
YYAFLSEDPDREDLLYRFLRLGFKHGKRVLEMLADPDVLRVFKLAKKVGREAHRMKGFVRFRELEDGVLY
AWIEPDHNVLPLLAPHFADRFPDENWIIYDPKRKYAAVYDGEELELVPLEEDEDPELSEEEDEYQALWKT
YFKSIAIPERKNPKLQRQHMPKRYWKYLPEK
>gnl|CDD|188431 TIGR03916, hypothetical_protein, putative DNA modification/repair radical SAM protein. This uncharacterized protein of about 400 amino acids in length contains a radical SAM protein in the N-terminal half. Members are present in about twenty percent of prokaryotic genomes, always paired with a member of the conserved hypothetical protein TIGR03915. Roughly forty percent of the members of that family exist as fusions with a uracil-DNA glycosylase-like region, TIGR03914. In DNA, uracil results from deamidation of cytosine, forming U/G mismatches that lead to mutation, and so uracil-DNA glycosylase is a DNA repair enzyme. This indirect connection, and the recurring role or radical SAM protein in modification chemistries, suggest that this protein may act in DNA modification, repair, or both [Unknown function, Enzymes of unknown specificity]
LKEKLEILADAAKYDVSCSSSGSSRKNKKGGLGNAGASGICHSFTEDGRCISLLKILLTNHCIYDCAYCV
NRRSNDVKRAAFTPEEVVDLTIEFYRRNYIEGLFLSSGIFKSPDYTMERLVRVAKKLRTEYHFNGYIHLK
TIPGASPELIEEAGLLADRLSVNLELPTEEGLKLLAPEKSHQSILKPMRFIQNGIIQSKEERKKYRHTPK
FAPAGQSTQMIIGATGETDYQILKVAESLYQKYGLKRVFYSAYVPVNEDDKLPALGTQPPLLREHRLYQA
DWLLRFYGFKADEILDEQNPNFDLELDPKLDWALRHLELFPVEVNRAPYEMLLRVPGIGVKSARRIVAAR
RFGKLDYDHLKKIGVVLKRAKYFITCNGKMMYQKKLDPDDLRRLLIQPDRKKYSEMFLYEQLSLF
>gnl|CDD|274852 TIGR03917, hypothetical_protein, Frankia-40 domain. This model describes a paralogous domain of length 40, restricted to smaller proteins of the genus Frankia, a member of the Actinobacteria. The function is unknown
HALTVRPGADAADLAAALARLPAGARFVEHFGDVDVVLVF
>gnl|CDD|274853 TIGR03918, hydrogenase_maturation_GTPase_HydF [FeFe] hydrogenase H-cluster maturation GTPase HydF. This model describes the family of the [Fe] hydrogenase maturation protein HypF as characterized in Chlamydomonas reinhardtii and found, in an operon with radical SAM proteins HydE and HydG, in numerous bacteria. It has GTPase activity, can bind an 4Fe-4S cluster, and is essential for hydrogenase activity [Protein fate, Protein modification and repair]
TPKGNRLHIGIFGRRNAGKSSLINALTGQDIAIVSDVPGTTTDPVYKAMELLPLGPVVLIDTAGLDDEGE
LGELRVEKTREVLDKTDLALLVVDAEQGPGEYELELIEELKERKIPYIVVINKIDLGEESAEKEKLEKKF
GLPPIFVSALTGEGIDELKEAIIELLPEDKEEPTIVGDLVPPGDLVVLVVPIDSAAPKGRLILPQVQTIR
DILDHGAIALVVKERELKEALSNLKKKPDLVITDSQVFKKVAADVPEDIPLTSFSILFARYKGDLATLVE
GAKAIDRLKPGDRVLIAEACTHHPQCDDIGRVKIPRWLRKYTGKDLEFEFVSGRDFPEDLSDYKLIIHCG
GCMLNRREMLSRIELAKEQGVPITNYGVAIAYLNGILERAL
>gnl|CDD|274854 TIGR03919, putative_membrane_protein, type VII secretion protein EccB, Actinobacterial. This model represents the transmembrane protein EccB of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccB1, EccB2, etc. This model does not identify functionally related proteins in the Firmicutes such as Staphylococcus aureus and Bacillus anthracis [Protein fate, Protein and peptide secretion and trafficking]
TTRLQVSGHRFLVRRLEHALVRRDVRMLDDPLRRQSRALAAGAVLAVLALAGCAVLALFRPGGKLGDAPI
VVDRETGALYVRVDGTLHPVLNLASARLILGSPANPVTVKSSELDKMPRGPLVGIPGAPAALPDPAPSES
PWTVCDTVATPGSGAVTTTVIAGPLALGQRAAPLRADQAVLVSYGGETYLLWDGGRSRIDLADRAVTRAL
GILEGVTPRPVSEALLNALPEGPPLAAPAIPGAGAPGPVGLPGAPVGSVVRVSTAGGGEQYYVVLADGLQ
PITPVTAALLRNTNSYGAAEPPTVAPDVVARAPVVTALPVSTLPDTPPELVDTADDPVLCASWQPGAGGQ
RASTSLLSGRALPVPPDARAVGLVQADGAGPNADRVYVPPGRGYFVQSTGLEPGSAARGSLYLVTDTGVR
YGIPDDEAAKALGLTGAPVPAPWPVLALLPAGPELS
>gnl|CDD|274855 TIGR03920, T7SS_EccD, type VII secretion integral membrane protein EccD. Members of this family are EccD, a component of actinobacterial type VII secretion systems (T7SS) with ten to eleven predicted transmembrane helix regions [Protein fate, Protein and peptide secretion and trafficking]
VTILAGKRQVDLVLPAAVPVAEILPEVVDLVDAPADDLGGAPLEAGRWVLARPGGPPLDLDLSLDEAGVV
DGDLLVLRPVSDTEPAPVIEDVADALAALSSSRSRPWRPRTTRELGALAALVTAAVLALGLVAAGRGLGG
WWGAPIAAGVIGLLVLAAAVVARTLRDRAVAALSLLGAALVLVAVAGALAVPGALGVPHVLLAGTVLAAL
AVLALRLTGRGLAVFTAVVAVAVILALAAAVGMLWQTPVPGIAAGLILLGLAVLSAAPRLSALLAGLPLP
PLPSPGEDLDVADALESMTDLTARARRADALLTGLVAAGALVLAAGALALAVPGTGSRWLGLALALLTAV
ALLLRARRYASAWCAWALIVAAAAVATALLVSAARGAPSGAWLALAVLVLALAVAALAAGWISPASRLSP
VTRRWLELLEGLALAAILPLALWLLGVFSLVRG
>gnl|CDD|274856 TIGR03921, T7SS_mycosin, type VII secretion-associated serine protease mycosin. Members of this family are subtilisin-related serine proteases, found strictly in the Actinobacteria and associated with type VII secretion operons. The designation mycosin is used for members from Mycobacterium [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair]
LSLEQAWKFSTGAGVTVAVIDTGVDDHPRLPGLVLPGGDFVGSGDGTDDCDGHGTLVAGIIAGRPGEGDG
FSGVAPDARILPIRQTSAAFEPDEGTSGVGDLGTLAKAIRRAADLGADVINISLVACLPAGSGADDPELG
AAVRYALDKGVVVVAAAGNTGGDGQKTTVVYPAWYPGVLAVGSIDRDGTPSSFSLPGPWVDLAAPGENIV
SLSPGGDGLATTSGTSFAAPFVSGTAALVRSRFPDLTAAQVRRRIEATADHPARGGRDDYVGYGVVDPVA
ALTGELPPEDGRPLRPAPAPARPVAAPAPPPPPDDTPRGRVALWGAGLAALAVVVGLAAAAVRRRGRRRR
>gnl|CDD|188437 TIGR03922, T7SS_EccA, type VII secretion AAA-ATPase EccA. This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc [Protein fate, Protein and peptide secretion and trafficking]
FTAATNLDPSMCDAWLGRIAAGDVDLAVLAAAWRTIATFGWLQRELGLAEGQLGAEIDTGLYLQFRVTSP
DDFQLAYAVALAEAGEYAEADRLLAGVEARRPGWVDARWVRVVIYYRTQRWPDVLNQLPPGVGWPSLDDK
AAHAAAAAHGVALARLGMFAEALRRLEEAIEGPRGPAAAPVADGAYAKAMVLRALGEEDEAQELLQDLYA
NHPENTQVEEALDDPSYRLVTTTAETIEARTDPWDPSSAPSRAEFVDPAAAERKAKLLAEAEAELAEQIG
LERVKRQVAALKSSTAMALARAERGLPVAQTSNHMLFAGPPGTGKTTIARVVAKIYCGLGVLRKPLVREV
SRADLIGQYIGESEAKTNEIIDSALGGVLFLDEAYTLVETGYGQKDPFGLEAIDTLLARMENDRDRLVVI
GAGYRKDLDKFLEVNEGLRSRFTRVIEFPSYSPDELVEIARRMATERDSVLDDAAADALLEAATTLAQDT
TPDANGDLRRGLDIAGNGRFVRNVVERAEEERDFRLDHSDRLDAVTVDDLMEITADDVARAVASLLR
>gnl|CDD|274857 TIGR03923, T7SS_EccE, type VII secretion protein EccE. This model represents the transmembrane protein EccB of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccE1, EccE2, etc. This model represents a conserved core region, and many members have 200 or more additional C-terminal residues [Protein fate, Protein and peptide secretion and trafficking]
GRITLALLVVVQAAVAAAWQATRQAGWWVALGVAVVVVLLLFVRWRGRTVTGWLARRLAWLRRRRRLPPD
AGDPAALDVPLGDDPVGVRWDGGFLTVVLEVTPPPDALTVITRSSVLTDNVLPLPLLAELLDQYDIRLDS
IDVVSHGQRTGAGGAAVALYERLLGPRPAAAHRRTWLVLRLDAADNLAALQARGGRIGLARTAVAAARRL
ADHLREAGWRARPLTAPEIPAAVAALTADTAPAPVRETWRGLRGDNGYLAAYRVDPDPILSDTLAQLWAL
PADETTVTVRLRPGAGRPTIAALVALRTDDRPVRPPLAGLTRLRGRQRPALAALLPLATPR
>gnl|CDD|274858 TIGR03924, T7SS_EccC_a, type VII secretion protein EccCa. This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes [Protein fate, Protein and peptide secretion and trafficking]
GPLLQKLLPVVMVVAVVGMVVMMFASGGRQRNPMFLIFPLMMLVSMLGMLAGGRGGGGKKTPELDEDRRD
YLRYLDQLRREVRETAAAQRAALEWRHPDPDTLWALVGTPRMWERRPGDPDFLEVRVGVGVQPLATRLVV
PETGPVEDLEPVTAVALRRFLRAHSTVPDLPVAVSLRGFARISLVGDRDQARALARAMLCQLAVFHGPDD
VGIAVVTSDPDRDWDWLKWLPHNQHPTRFDAAGPARLVYTSLAELEAALAELLADRGRFSPDDAASLPHL
VVVVDGGDLPGWEDLIGESGLDGVTVIDLGGSLPGLPDRRGLRLVVEADRLDARTADGVEEFGVAPDQLS
IAEAEALARRLARWRAATAGTVDAPLTGARDLLELLGIGDPATLDVDRLWRPRPGRDRLRVPIGVGDDGE
PVELDLKESAEGGMGPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKGGATFLGLEGLPHV
SAVITNLADEAPLVDRMQDALAGEMNRRQELLRAAGNFANVAEYEKARAAGADLPPLPALFVVVDEFSEL
LSQHPDFADLFVAIGRLGRSLGVHLLLASQRLDEGRLRGLESHLSYRIGLKTFSASESRAVLGVPDAYHL
PSTPGAGYLKVDTAEPVRFRAAYVSGPY
>gnl|CDD|274859 TIGR03925, T7SS_EccC_b, type VII secretion protein EccCb. This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes [Protein fate, Protein and peptide secretion and trafficking]
TVLDVVVDRLAGQGPPAHQVWLPPLPEPPALDDLLPRLDVDPWRVDYGQRGRLTVPVGIVDRPFEQRQDP
LVVDLSGAAGHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPHVGGVAGRL
DPERVRRTVAEVEGLLRRRERLFRTHGIDSMAQYRARRAAGRLPEDPFGDVFLVIDGWGTLRQDFEDLED
KVTDLAARGLAYGVHVVLTASRWSEIRPALRDLIGTRIELRLGDPMDSEIDRRAAARVPAGRPGRGLTPD
GLHMLIALPRLDGIASVDDLGTRGLVAVIRDVWGGPPAPPVRLLPARLPLSALPAGGGAPRLRVPLGLGE
SDLAPVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRRTLLGAVPEDYLAGYA
ATSAALTELIAALAALLERRLPGPDVTPQQLRARSWWSGPEIYVVVDDYDLVATGSGNPLAPLVELLPHA
RDIGLHVVVARRSGGAARALMDPVLARLKDLGAPGLLLSGDRDEGPLLGGVRPRPLPPGRGVLVTRGGGP
QLIQVA
>gnl|CDD|188441 TIGR03926, T7_EssB, type VII secretion protein EssB. Members of this family are associated with type VII secretion of WXG100 family targets in the Firmicutes, but not in the Actinobacteria. This protein is designated YukC in Bacillus subtilis and EssB is Staphylococcus aureus [Protein fate, Protein and peptide secretion and trafficking]
YLEDQLTAQFEKEKDTYTLTFQRSKIKLQDLLELELLKQHSPLFVPAEIDEDEDEFVISYQPPPAAKSFE
SIKKKTRNEKLRLALNLADLEEHLNSRLTFILHPENLVFTKGLTPSIIHRGVKESLPPYELDEERFLKQY
KAFIIALFDGKYRFEELYNGSLETLKLSPFAKKILEAETLDALLAFLDEQYIKEEEKKEKTLAFVPKKKW
RIFKYIGIGLIILLVPLIIPLIYLLFFAQPKQEAILAANTAFLKDDYSQVITTLEDYSPEKLPKSVKYEL
AYSYVQTEKLSEDQKENILNNVTLKSDELYLLYWIYIGRGEFEEALDIAKYLDDNDLIMYALVKYREQVK
NDTDLSGDERQEKLDELEKELDEYLKK
>gnl|CDD|200340 TIGR03927, T7SS_EssA_Firm, type VII secretion protein EssA. Members of this family are associated with type VII secretion of WXG100 family targets in the Firmicutes, but not in the Actinobacteria. This highly divergent protein family consists largely of a central region of highly polar low-complexity sequence containing occasional LF motifs in weak repeats about 17 residues in length, flanked by hydrophobic N- and C-terminal regions [Protein fate, Protein and peptide secretion and trafficking]
LLLFLSLFLFLPSADSAAENDGKLQVKPNRYEKKDIEINTDYLQEETELDKELFTPEEQKKITFQKHKEK
PEQEELKNQLFSENATENNTVKATKKQLFSSEYEQTSSSSESTSEEETKKTSSILLPVLYAGLILLLAAG
IYFLIRKVKD
>gnl|CDD|274860 TIGR03928, T7_EssCb_Firm, type VII secretion protein EssC, C-terminal domain. This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria [Protein fate, Protein and peptide secretion and trafficking]
KDYPDYHRSPRIIYEEPTDKVKISKPPQEPDKPKRGLLRIILPPLVMIAVTVLISIFQPRGIFIIASIAM
SLVTIIFSTTTYFREKKKYKKDVEKRNRSYRLYLDKKRKELQALSEKQRHVLHYHNPSVEELKEMVENVN
SRIWEKTPEHHDFLHVRLGTGNVPSSFEIKFPEEEFSQRKDELLDEAQELKEKYNTIENVPIVLDLSNGP
IGYVGKRSLVLEELQNLVGQLAFFHSYHDVQFVTIFPEEEKKKWEWMRWLPHFWLRDINVRGFVYNERTR
DQLLNSLYQILKERKLALDDANSKEKKRFSPHYVFLITDRKLILDHVIMEYLNEDPSELGISLIFVQDVM
ESLPENVKTVIDIKNRNEGEIVLEEGELVEKSFTPDHLDNEDLEEYSRTLAPLNHLQNLKNSIPESVTFL
EMYGVKKVEELNIQERWAKNETYKSLAVPIGLRGKDDIVYLNLHEKAHGPHGLVAGTTGSGKSEILQTYI
LSLAVNFHPHEVAFLLIDYKGGGMANLFKNLPHLLGTITNLDGAQSMRALASIKAELKKRQRLFGENNVN
HINQYQKLYKQGKAKEPMPHLFLISDEFAELKSEQPEFMKELVSTARIGRSLGVHLILATQKPSGVVDDQ
IWSNSRFKLALKVQDASDSNEILKTPDAAEITVPGRAYLQVGNNEVYELFQSAWSGAPYDPDKDKKEEED
IYMINDLGQYELLNEDLSGLKRKKEIKEVPTELEAVIDEIQAYTEELNIEALPSPWLPPLEEKIYLDDLH
AVEFDKLWSKPKEPLQATIGLLDDPELQSQEPLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSP
EQLHFYLFDFGTNGLLPLKKLPHVADYFTLDEEEKIEKLIRRIKKEIDRRKKLFSEYGVASISMYNKASG
EKLPQIVIIIDNYDAVKEEPFYEDFEELLIQLAREGASLGIYLVMTAGRQNAVRMPLMNNIKTKIALYLI
DKSEYRSIVGRTKFTIEEIPGRGLIKKDEPTLFQTALPVKGEDDLEVIENIKAEIQKMNEAWTGERPKPI
PMVPEELSLEEFRERYEVRKILEEGSIPIGLDEETVEPVYIDLTENPHLLIVGESDDGKTNVLKSLLKTL
AKQEKEKIGLIDSIDRGLLAYRDLKEVATYIEEKEDLKEILAELKEEIELREAAYKEALQNETGEPAFKP
ILLIIDDLEDFIQRTDLEIQDILALIMKNGKKLGIHFIVAGTHSELSKSYDGVPKEIKQLRTGILGMRKS
DQSFFKLPFTRSEKELEPGEGYFVVNGKYQKIKIPE
>gnl|CDD|274861 TIGR03929, T7_esaA_Nterm, type VII secretion protein EsaA, N-terminal domain. Members of this family are associated with type VII secretion of WXG100 family targets in the Firmicutes, but not in the Actinobacteria. This model represents the conserved N-terminal domain
LIFLVLFIVLLPGLFFLAIGQNPKKQKTNQNAKMNIAVVNEDQGVSFDGKTYNFGASFVKAIERDNSQEW
SVVSRGAAENGLKNNTYDAVVYIPSDFSKKVLSVNKENPEKATIQYKVNANGNAVLKEEAQREAEDILND
FNSQMSDLYWASILQNLQTAQDNVQAIVNKEAEFQSTYYKNYLPSSANLTNQF
>gnl|CDD|274862 TIGR03930, WXG100_ESAT6, WXG100 family type VII secretion target. Members of this protein family include secretion targets for the two main variants of type VII secretion systems (T7SS), one found in the Actinobacteria, one found in the Firmicutes. This model was derived through iteration from pfam06013. The best characterized member of this family is ESAT-6 from Mycobacterium tuberculosis. Members of this family usually are ~100 amino acids in length but occasionally have a long C-terminal extension
QIKVDPEELRQAAARFGKTAQELQQLLQRLRSEIDALQGTWEGAAADAFQAEFQQWDPAAERLINALQEI
SEALRQAADKFEQADQEAAS
>gnl|CDD|274863 TIGR03931, T7SS_Rv3446c, type VII secretion-associated protein, Rv3446c family, C-terminal domain. Members of this protein family occur as part of the ESX-4 cluster of type VII secretion system (T7SS) proteins in Mycobacterium tuberculosis and in similar T7SS clusters in other Actinobacteria genera, including Corynebacterium, Nocardia, Rhodococcus, and Saccharopolyspora. This model describes the better-conserved C-terminal region [Protein fate, Protein and peptide secretion and trafficking]
GGAPTGDTPKAKVREASTAQATAESTTPAPPPPRAGVTRLVEGRVAVEVPAGWRLTGGPGSPRTQILTGA
DPNLRIHVTEDPLDGAGLDAVAAELRAAIDADPTFTDLEEDDVVAGRPVVTYRETPGDGSTVLWHVWVDD
GHQVSVGCQSRPGANEVVRAACRKAVESLHAR
>gnl|CDD|188447 TIGR03932, IcaD_partial, intracellular adhesion protein D. Members of this protein family are IcaD (intracellular adhesion protein D), which with catalytic subunit IcaA forms an N-acetylglucosaminyltransferase. In the absence of IcaC, this enzyme forms N-acetylglucosamine oligomers up to 20 in length [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
VKSSLNIVRECVLFIISCTFWLYCLIVVIVYIGTLFLQDFESVQTIRIALNVENREIVDIFETLLAFVII
IFVFFTSSLILQKWRQGR
>gnl|CDD|188448 TIGR03933, Poly-beta-16-N-acetyl-D-glucosamine_N-deacetylase, intercellular adhesin biosynthesis polysaccharide N-deacetylase. A common motif in bacterial biosynthesis of polysaccharide for export is modification that follows polymerization. This model describes a subfamily of polysaccharide N-deacetylases that acts on poly-beta-1,6-N-acetyl-D-glyscosamine as produced by Staphylococcus epidermidis and S. aureus. The end product in these species is designated polysaccharide intercellular adhesin (PIA), and this gene designated icaB (intercellular adhesion protein B) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Cellular processes, Pathogenesis]
NSALALNYHRVRKDDPLNNFISLLSSSKEIKNYSVSDSEFESQIKWLKAHDAKFLTLKEFIKYKEKGKFP
KRSVWINFDDMDQTIYDNAFPILKKYKIPATGFVITGHIGDENFHNLNLIDLKQLKEMYATGLWDFESHT
HDLHNLKKSNKSKFLHSSKAGAKKDIDKSEKYLNKNFNKNQTSIAYPYGLINDDKIKVLKKAGIRYGFTL
EEKAVTPDDNNYRIPRILVSNDAFEKLIKKWDGFN
>gnl|CDD|274864 TIGR03934, fibronectin-binding_protein_I_partial, TQXA domain. This model describes a domain of about 40 residues with an invariant TQ dipeptide in an almost invariant TQxA[VI]W motif. This domain occurs in surface-expressed proteins of Gram-positive bacteria, many of which are anchored by LPXTG-containing sortase target domains. Numerous members of this family have domains pfam05738 (Cna protein B-type domain) and pfam08341 (fibronectin-binding protein signal sequence)
KILWILANGYPNKSNGELGGLTEEEARAVTQLAIWYFTDGLD
>gnl|CDD|188450 TIGR03935, fragilysin, fragilysin. Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This enzyme is a Zn metalloprotease. Three distinct subtypes included in this family all are produced by enterotoxigenic (by definition) strains of Bacteroides fragilis [Cellular processes, Pathogenesis]
LLLFLGTAALLAACSNEADSVTTTIDPPVTASINLQSVDYTDLATQLNDVSDFGKTIILKDNGFNRQVHV
SMDKRTKIQEDNENVRLFNGRDKDSISFILGDEYAVLRFYRNGDLISYIAYKEAQMMAEIAEYYAAHFKK
TRAINEKKIFECIYDSRTRSAGKDIVSVKINIDKAISINKILNLPECDYINDYIKTPQVPHGITESQSRA
VPSEPKTLYVILIREKGSTGYPHEVTAQMQDAANSLKRLVNNHFVLVEYTTEYSCPSGGADESKGLDGFT
ASLKSNPKAKGYDKQIYILIRWGTWDNNILGIGWLNSYNVNTASNFEASGMSTTQLMYPGTLAHELGHIL
GAEHTDNEKDLMYTWYTGYWRLNHLSEKNMVRIAKN
>gnl|CDD|274865 TIGR03936, radical_SAM-linked_protein, radical SAM-linked protein. This model describes an uncharacterized protein encoded adjacent to, or as a fusion protein with, an uncharacterized radical SAM protein
RYRIRFSKTGRARFLSHLDLMRLFERALRRAGLPVAFSQGFNPHPKISFAPALPVGVESEAEYMDIELTE
EIDPEEVLERLNAVLPEGIEVLEVEEVPDKAPSLMSLIDAAEYRITLPLPDEEDLQEAIEAFLAAEEIIV
EKKTKKGKKEVDIRPLIKSLEVEDGLRLLMTLSCGSEGNLRPEEVLEALLELSGLELALARIHRLELY
>gnl|CDD|274866 TIGR03937, Poly-beta-16-N-acetyl-D-glucosamine_synthase, poly-beta-1,6 N-acetyl-D-glucosamine synthase. Members of this protein family are biofilm-forming enzymes that polymerize N-acetyl-D-glucosamine residues in beta(1,6) linkage. One named members is IcaA (intercellular adhesin protein A), an enzyme that acts (with aid of subunit IcaD) in Polysaccharide Intercellular Adhesin (PIA) biosynthesis in Staphylococcus epidermis). The homologous member in E. coli is designated PgaC. Members are often encoded next to a polysaccharide deacetylase and involved in biofilm formation. Note that chitin, although also made from N-acetylglucosamine, is formed with beta-1,4 linkages
LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWPLPRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLAL
RYPNFEIIAINDGSKDNTAEILDRLAAQDPRLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDP
DAAYWMVEHFLSNPRVGAVTGNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKS
ALHDVGYWSTDMITEDIDISWKLQLAGWNIRYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQ
LWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQVNILPYTPLVYSISLFQWSGLLLTFICLLQFTVS
LFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKRAVWVSPDRG
>gnl|CDD|274867 TIGR03938, hypothetical_protein_Pcar_2791, poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB. Two well-characterized systems produce polysaccharide based on N-acetyl-D-glucosamine in straight chains with beta-1,6 linkages. These are encoded by the icaADBC operon in Staphylococcus species, where the system is designated polysaccharide intercellular adhesin (PIA), and the pgaABCD operon in Gram-negative bacteria such as E. coli. Both systems include a putative polysaccharide deacetylase. The PgaB protein, described here, contains an additional domain lacking from its Gram-positive counterpart IcaB (TIGR03933). Deacetylation by this protein appears necessary to allow export through the porin PgaA [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
NTFVVLCYHDVRDDSAADQDPYAVSTDALIEHFNWLRQNGYHPVSVDQILDARRGGKPLPEKAVLLTFDD
GYRSFYTRVFPLLKAYNYPAVLALVGSWLDTPANQKVDYGGEKLPRDRFLTWEQIREMQASGLVEIASHT
YDLHHGILANPQGNELPAATTRAYDPATGRYETDAEYRQRIRDDLKKSSALIKKYTGKAPRVMVWPYGAY
NGTAIKIAKELGMPVALTLDDGPNTVDDPLNALRRILVDNNPSLEDLARELRNVQTEKPPQRVVHVDLDY
VYDPDPAQQERNLDKLIDRIKDLGPNTVYLQAFADPDGDGVADALYFPNRHLPMRADLFNRVAWQLRTRA
GVKVYAWMPVLAFDLPPSLPRVKRLVPTTGGAPIDPMQYPRLSPFDPRARQLIKDIYEDLARYAKFDGIL
FHDDATLSDFEDASPAALAAYRKWGLPGSIAEIRADPQLLARWTRFKTKYLIDFTLELAAAVRAYQPGLK
TARNLYAQPILSPDSEAWFAQNLDDFLKAYDYTAIMAMPYMEGAAFKDPEAWLARLVKAVKQRPGALDKT
VFELQAVDWRTGQPIPSEELADWMRLLQLNGAKNFGYYPDDFIKNQPELKKIRPVFSLN
>gnl|CDD|274868 TIGR03939, PGA_TPR_OMP, poly-beta-1,6 N-acetyl-D-glucosamine export porin PgaA. Members of this protein family are the poly-beta-1,6 N-acetyl-D-glucosamine (PGA) export porin PgaA of Gram-negative bacteria. There is no counterpart in the poly-beta-1,6 N-acetyl-D-glucosamine biosynthesis systems of Gram-positive bacteria such as Staphylococcus epidermidis. The PGA polysaccharide adhesin is a critical determinant of biofilm formation. The conserved C-terminal domain of this outer membrane protein is preceded by a variable number of TPR repeats
LTLLFALFLAPAWANASPADEKYDQLIIQARAGDTAPALSGLQQLYRKTPLDRKVLDDLLAVLSWAGRDK
EAIDVCERYSPVGLPARVLEALAKAYRNEKQWDKALELYRKLLQRDPNNPDGLLGLALTLADAGKDAEAL
KYLKEYVARFPTDAARYEALAYVLRAAEDHLDALQAWQQALTLEPDNPEAALELYRILTRLGAPPAAARL
AKQYPDLFTPEDQRWLEHDQAAELVRLGENPSRSEKERFAIADRALADLQALLDKWGPQANPLYRRARID
RLGALLVRKRYAEVIREYESLEAEGQPLPPYAQEAVADAYLALRQPEKALPIYRELAAAEPADNNLELTI
KLFYAYLEAEQYDEAQALLDGLKESTPPQRWDFTRSTKAPNDDYLEAQQLLVLSLAWRGDLPEAEARLDE
LLATAPGNPWLRLALADVYRARGWPRRAEQEYKQAESLDPDSLSAERGQAETALDLQEWRQAEQLTDDLV
ARYPEDEQVQRLARRRDVHNRPELRVSGGKGHSSGPPVSGSRDLSYEARLYSPPLAEGWRVFAGGQYSKG
EFEEGKGSARRIGAGVEYRFRPFTLEAEAGQGFGLNDKAGARLSAGYDLNDHWRIGLSGELNSADTPLRA
LKNGVTANDAGAGVTYRQNERRSLGLSASASDFSDGNRRQEYGLWGEERLWSGPRYKLDGILSLSASRNS
EIDASYYNPKSDRNIELALALSHRLYRRYDTSLSQQLKAGVGQYWQKGFGTGAVWALSYGQRWRWNDVID
LGYGVGRDKRPYDGERENNNYINANLNWRF
>gnl|CDD|188455 TIGR03940, PGA_PgaD, poly-beta-1,6-N-acetyl-D-glucosamine biosynthesis protein PgaD. Members of this protein family are PgaD, essential to the production of poly-beta-1,6-N-acetyl-D-glucosamine (PGA). This cytoplasmic membrane protein appears to be an auxiliary subunit to the PGA synthase, PgaC (TIGR03937) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
PLIINKRHQLPWSKRLASGILTALFWGGFLYLWAPLLTLFAWLIGLRLTYEISHRIFSALSLFTLESYLL
ILLVTAVVLLLWAWYNRLRFVGEERRTRPPALDEDEYARYFGLSETLLAQLRTSKVLTVHHDEHGRIVGV
E
>gnl|CDD|274869 TIGR03941, conserved_hypothetical_protein, putative tRNA adenosine deaminase-associated protein. This model describes a protein family about 200 amino acids in length with only five invariant residues, including an Arg, a Ser-Asp pair, and two Gly residues. Members always are found exclusively in Actinobacteria, and always adjacent to homologs of TadA, a tRNA-specific adenosine deaminase from Escherichia coli. Homology, phyletic pattern, and gene neighborhood together suggest a housekeeping function in tRNA metabolism [Unknown function, General]
SDFAVAVAREDGGWRVAELDLDALEDLDDLIDALRDLRSDGAVFGLVEVDDEFFVIVRPDPGGVRVFLSD
ATAAVDDDLAADVLDDLDIDVPDDDDDEDDDTDPWPEGDLDILADLGLSEEELGVLCDDEDLYPDEVLSE
IAERLGFADELDRA
>gnl|CDD|188457 TIGR03942, sulfatase_rSAM, anaerobic sulfatase-maturating enzyme. Members of this protein family are radical SAM family enzymes, maturases that prepare the oxygen-sensitive radical required in the active site of anaerobic sulfatases. This maturase role has led to many misleading legacy annotations suggesting that this enzyme maturase is instead a sulfatase regulatory protein. All members of the seed alignment are radical SAM enzymes encoded next to or near an anaerobic sulfatase. Note that a single genome may encode more than one sulfatase/maturase pair [Protein fate, Protein modification and repair]
HVMAKPTGAKCNLDCDYCFYLEKEDLYPKPKPKMSDETLETFIKQYIASQDGPEVNFAWQGGEPTLAGLD
FYRKAVELQQRYAPGKTISNSLQTNGILLNDEWAEFFKEHNFLVGISIDGPKELHDKYRVTKSGKGTFER
VMRALKLLKEHNVEFNTLTVVNNHNARHGKEVYRFLKELGSRYMQFIPCVEPDNATREVTDWSVTPKDYG
RFLCDVFDEWVKNDVGRVFIRNFENALAIWLGNPSQSCVHSPTCGQNLVVESNGDVYSCDHYVYPEYKLG
NINETSLAEMASSEKQKQFGQAKSLSLPEKCRRCDVLFLCNGGCPKHRILATPGGENGHNYLCAGYKAFF
SHTLPYLQAMAEL
>gnl|CDD|274870 TIGR03943, TIGR03943, TIGR03943 family protein. Members of this occur in gene pairs with members of pfam03773. The N-terminal region contains several predicted transmembrane helix regions while the few invariant residues (G, CxxD, and W) occur in the C-terminal region
LTGRLLLYIHPRYFPLLIAAAVVLLLLALAQLLRLFRRGGDEHHHHQHKTHLKRPLGYWLLLLPILLGLL
FPPAALGSDTAAQRGLAFSLTQDLRQPFPPLPTLRPIERSLEDYVRTLRVIYPDPDSYDGRKVEVTGFVY
RDPDLPDNEFVLARFVITCCAADAQPVGLLVKGPNAEQLPNDTWVRVEGTLSTETPNGRRIPVIQVTSVE
PIPAPENPY
>gnl|CDD|274871 TIGR03944, ornithine_cyclodeaminase, 2,3-diaminopropionate biosynthesis protein SbnB. Members of this protein family are probable NAD-dependent dehydrogenases related to the alanine dehydrogenase of Archaeoglobus fulgidus (see TIGR02371, PDB structure 1OMO and) and more distantly to ornithine cyclodeaminase. Members include the staphylobactin biosynthesis protein SbnB and tend to occur in contexts suggesting non-ribosomal peptide synthesis, always adjacent to (occasionally fused with) a pyridoxal phosphate-dependent enzyme, SbnA. The pair appears to provide 2,3-diaminopropionate for biosynthesis of siderophores or other secondary metabolites [Cellular processes, Biosynthesis of natural products]
MLYLNGSDVEALLAGREQALIDAVEEAYLAHAAGDTVQPDSPFLRFPDEPADRIIALPAYLGGDFPVAGI
KWIASFPGNPQRGLPRASAVIILNDPDTGYPVAILEGSLISAMRTAASAALAARHLAAGRGFTRVGIIGC
GPIAREILRFLLALGPEIRRVVLYDLDPARAEAFAARCQELGPHKVTVAASAEAALRQADLVVTATVAGT
PYIDDPAWFQPGALVLNISLRDLAPEVILKADNIVDDWEHVCRANTSLHLAEQEGGHREFITATLGEILT
GEVPGREDDDEPIIFSPFGLGILDLAVARWVYEQAQAAGIGTRLPDF
>gnl|CDD|274872 TIGR03945, cysteine_synthase, 2,3-diaminopropionate biosynthesis protein SbnA. Members of this family include SbnA, a protein of the staphyloferrin B biosynthesis operon of Staphylococcus aureus. SbnA and SbnB together appear to synthesize 2,3-diaminopropionate, a precursor of certain siderophores and other secondary metabolites. SbnA is a pyridoxal phosphate-dependent enzyme [Cellular processes, Biosynthesis of natural products]
ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLG
IALAMICAYKGLRFICVVDPNISPQNLKLLRAYGAEVEKVTEPDETGGYLGTRIARVRELLASIPDAYWP
NQYANPDNPRAHYHGTGREIARAFPTLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIFGGP
PGRRHIPGLGASVVPELLDESLIDDVVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEG
STVVAILPDRGERYLDTVYNDEWV
>gnl|CDD|188461 TIGR03946, viomycin_VioC, arginine beta-hydroxylase, Fe(II)/alpha-ketoglutarate-dependent. Members of this protein family are L-arginine beta-hydroxylase, members of a broader family of enzymes dependent on Fe(II), alpha-ketoglutarate, and molecular oxygen. Enzymes in the broader family but excluded by this model include clavaminate synthase, taurine dioxygenase, and prolyl-4-hydroxylase [Cellular processes, Biosynthesis of natural products]
LRLTAQEAAAAAALAAELAQRYPEIDDPELLRDAPVLAAKLPPHLRRFLDRFRLDDPSHALVIRGNDVDQ
DRLGPTPEHWRDAQTPGSRLPLEFLLMLYAALLGDVFGWATQQDGRVVHDVLPIKGHEHYLLGSSSLQEL
GWHTEDAFHPYRADYVGLMSLRNPDEVATTVAGLDDDDLPNLDVDVLFEPRFTIRPDNSHLPQNNSESTG
GRTEDSFEGIKSANENPVRVAILYGHRQAPYMRLDPYFTKMDDGDEEAAEALDALCKLIDAKMYEVVLDP
GDVAFIDNRRAVHGRRPFRARYDGTDRWLKRINITRDLRRSRAWRPAADDRVL
>gnl|CDD|188462 TIGR03947, putative_aminotransferase, capreomycidine synthase. Members of this family are the enzyme capreomycidine synthase, which performs the second of two steps in the biosynthesis of 2S,3R-capreomycidine from arginine. Capreomycidine is an unusual amino acid used by non-ribosomal peptide synthases (NRPS) to make the tuberactinomycin class of peptide antibiotic. The best characterized member is VioD from the biosynthetic pathway for viomycin [Cellular processes, Biosynthesis of natural products]
LEDWLREYYFTAVHDISSSGVHDYSFAELRTLCGIPAEDLDALVFRDGPSLGGEGLRAAIADRWRGGDAH
VVMTTHGSSEAIYLVLTALLRPGDEVVVVDPAYHSLSHLAVATGCEVRPWPLLAVRGFRPDLDALRALLT
PRTRAVVVNFPHNPTGASVTPRELDELLERAARSGAVLLWDNAFADLVHDAPPLPDPSALYDRVISFGTL
SKAFGLPGLRVGWCVGPADLLAELVRLRDYTTLSLSPLVELLAEVAVEHADALIGPRLAEARANRRRLLD
WAAAHPDVVRCTPPEGGVAAFPRFPGHADVTDLCRRLLARHGVLLVPGSCFGAADRMRLGFGGSSAELRA
GLARLSAFL
>gnl|CDD|188463 TIGR03948, hypothetical_protein_FAEPRAM212_02812, butyryl-CoA:acetate CoA-transferase. This enzyme represents one of at least two mechanisms for reclaiming CoA from butyryl-CoA at the end of butyrate biosynthesis (an important process performed by some colonic bacteria), namely transfer of CoA to acetate. An alternate mechanism transfers the butyrate onto inorganic phosphate, after which butyrate kinase transfers the phosphate onto ADP, creating ATP [Energy metabolism, Fermentation]
DFKEEYAQKLVTADEAVKVVKSGDWVDYGWTTGTPVALDAALAKRMPELEDVNIRGGILMWPPEIFKIEN
PAEHFTWNSWHMGGIERKAIAKGFAFYSPIRYSELPRYYRESNTPVDVAMFQVAPMDEHGYFNFGPSASH
LGAVCEKAKKIIVEVNENMPRCLGGFEEGVHISKVDMIVEGDNPAIGELGAGGAATEVDKAVAKLIVEEI
PNGACLQLGIGGMPNAVGSLIAESDLKDLGVHTEMYVDAFVDIAKAGKINGSKKNIDRGRQVYAFGAGTK
KMYDYLDDNPECMSAPVDYTNDIRSISALDNFISINNAVDIDLFGQVNAESAGIKQISGAGGQLDFVLGA
YLSKGGKSFICLSSTFTDKDGQLHSRIRPTLHNGSIVTDTRANTHYVVTEYGKVNLKGLSTWQKAEALIS
IAHPDFRDELIKEAEKMHIWRRSNK
>gnl|CDD|274873 TIGR03949, bact_IIb_cerein, class IIb bacteriocin, lactobin A/cerein 7B family. Members of this protein family are described variably as bacteriocins per se, one chain of a two-chain bacteriocin, or bacteriocin enhancer proteins. All members of the seed alignment occur in paired gene contexts with another member of the same protein family. This family includes bacteriocins that appear not to undergo post-translational modification, other than cleavage at a Gly-Gly motif coupled to sec-independent export. For many members, the N-terminal bacteriocin cleavage motif region is recognized by TIGR01847. C-terminal to the cleavage motif, these proteins are hydrophobic and low in complexity, consistent with pore-forming activity as a mechanism of bacteriocin action
FKELTEEELENVNGGVAPIAVAIAVGGGAGGAAGAGFVAGAAAGY
>gnl|CDD|274874 TIGR03950, hypothetical_protein, siderophore ferric iron reductase, AHA_1954 family. Members of this protein family are 2Fe-2S cluster binding proteins, found regularly in the context of siderophore transporters. Members are distantly related to FhuF from E. coli, a ferric iron reductase linked to removal of iron from hydroxamate-type siderophores () [Energy metabolism, Electron transport, Transport and binding proteins, Cations and iron carrying compounds]
LFEHSQQVTPYLDGRIGAAGADLIHADSDNSEIIASLYEYLRQAHPEAGSAYWLTRTWTLLCWQPIYLAF
IAVYQLRALPDLSRMGQYVDNGFVAGFRFADHDLQQGSREELIARAGKQLKALFEAYREQLSQWTRIRPG
FTEHLLADGVLAALLKLQQLRPLLSNEQLLEQARLWLDALGLPGKHLQSLKLDPGRGQLSLVRTSCCLHY
KREDGELCSDCPR
>gnl|CDD|274875 TIGR03951, Fe_III_red_FhuF, siderophore-iron reductase FhuF. Members of this protein family, including FhuF of E. coli, are siderophore ferric iron reductases that appear to play a role in iron removal from certain hydroxamate-type siderophores, including coprogen, ferrichrome, ferrioxamine B, and aerobactin. Genes occur in regularly in siderophore transport and/or biosynthesis clusters. The C-terminus includes four Cys residues in a C-C-10(X)-C-X-X-C motif that binds a 2Fe-2S cluster. Family TIGR03950 is similar, but especially in the C-terminal region, but likely acts on a different panel of siderophores [Energy metabolism, Electron transport, Transport and binding proteins, Cations and iron carrying compounds]
DARALLSLWSKYYFGLLIPPGMLALLVLGRALPLAPERLRVELHETGLPDAFYLPHEGDALLDTPPDPLQ
RFAGLLDDHLQPVIEALAAYGGINPRLLWSNAGYYIDWYLGELAELLGPAPLAALGLALFFEPQLPDGRR
NPLFGPVRTVVLRNGLLFRQRRVCCLRYKLPGVGQCGDCPLL
>gnl|CDD|274876 TIGR03952, conserved_hypothetical_protein, zinc-dependent metalloproteinase lipoprotein, BF0631 family. Members of this protein family are zinc-dependent metalloproteinases, related to ulilysin and other members of the pappalysin family. Members occur as predicted lipoproteins and occur mostly in the genera Bacteriodes and Prevotella [Protein fate, Degradation of proteins, peptides, and glycopeptides]
LLMLLAALVLLVACSDEEDISTEDGGISIKIKEDDTTEPELEDYVYKLPVVFHVFYQDSTDETQYVPATR
LREILDNVNELYQGNTYSNSENTNVEFVLATEDPAGKKLDEPGVEYIKLSEYPIDCEVFMKDKSGKYKKY
LWDPNKYINVYVYHFKQTDENGTTLGISHMPYTIKGDHALEGLEVLNGNKYTLNNLSYPLCVSLNSKYIN
TESTRYTDDPNKKGYIYSSADFNVTLAHELGHYLGLFHVFGEEKTSGYIDDCKDTDYCEDTPTYNRKAYD
KWLQEYIKKHDANLTYADLNELFKRTNCSGKTFESNNIMDYAISYSNRFTPDQVERIRYVLYYSPLIPGP
K
>gnl|CDD|274877 TIGR03953, rplD_bact, 50S ribosomal protein L4, bacterial/organelle. Members of this protein family are ribosomal protein L4. This model recognizes bacterial and most organellar forms, but excludes homologs from the eukaryotic cytoplasm and from archaea [Protein synthesis, Ribosomal proteins: synthesis and modification]
IELNDAVFGVEPNEHLLHQVVKAQLANRRQGTHKTKTRSEVSGGGKKPWRQKGTGRARQGSIRSPLWRGG
GVAFGPKPRDYSYKLNKKVRRLALRSALSEKAREGKLVVVDDFDLEEPKTKDLAKILKNLGLGKKVLIVT
DEVDENLYLSARNLPNVKVLPANGLNVYDLLRADKVVITEAAVKKLEE
>gnl|CDD|274878 TIGR03954, hypothetical_protein, integral membrane protein. This model describes a strictly bacterial integral membrane domain of about 85 residues in length. It occurs in proteins that on rare occasions are fused to transporter domains such as the major facilitator superfamily domain. Of three invariant residues, two occur as a His-Gly dipeptide in the middle of three predicted transmembrane helices [Unknown function, General]
FRVIAFAEGVSLLLLLFIAMPLKYLAGNPEAVKIVGPIHGVLFILYLVAALDLARKARWSLKRTLLALLA
SVIPFGSFVFERKLR
>gnl|CDD|274879 TIGR03955, iron-only_hydrogenase_maturation_rSAM_protein_HydG [FeFe] hydrogenase H-cluster radical SAM maturase HydG. This model describes the radical SAM protein HydG. It is part of an enzyme metallocenter maturation system, working together with GTP-binding protein HydF and another radical SAM enzyme, HydE, in H-cluster maturation in [FeFe] hydrogenases [Protein fate, Protein modification and repair]
YDPKSSKAEEFINHEEILETLAYAEENKDNKELIDSILEKAAKCKGLTHREASVLLACEDPEKIEEIYKL
AEQIKKKFYGNRIVMFAPLYLSNYCVNGCVYCPYHAKNKHIARKKLTQEEIRREVIALQDMGHKRLALEA
GEDPVNNPIEYILESIKTIYSIKHKNGAIRRVNVNIAATTVENYRKLKEAGIGTYILFQETYHKESYEEL
HPTGPKHDYAYHTEAMDRAMEGGIDDVGLGVLFGLNLYRYDFAGLLMHAEHLEAVFGVGPHTISVPRIRP
ADDIDPDDFDNGISDDIFAKIVACIRIAVPYTGMIISTRESQKVRERVLHLGISQISGGSRTSVGGYAEP
EPEDENSAQFDVSDNRTLDEVVNWLMDLGYIPSFCTACYREGRTGDRFMSLCKSGQIANCCHPNALMTLK
EYLEDYASPDTRKKGEELIAKELPKIPNEKVREIAQENLDAIEEGKRDFRF
>gnl|CDD|274880 TIGR03956, iron-only_hydrogenase_maturation_rSAM_protein_HydE [FeFe] hydrogenase H-cluster radical SAM maturase HydE. This model describes the radical SAM protein HydE, one of a pair of radical SAM proteins, along with GTP-binding protein HydF, for maturation of [Fe] hydrogenase in Chlamydomonas reinhardtii and numerous bacteria [Protein fate, Protein modification and repair]
LIDKLRKEHTLSKEEFKRLLENRDEEDAEYLFELAREVRLRYYGNKVYIRGLIEFTNYCKNDCYYCGIRK
SNPNAERYRLTKEEILSCCREGYELGFRTFVLQGGEDPYFTDERIVEIVSAIKEEYPDCAITLSLGEKSY
ESYQRYFDAGADRYLLRHETANEEHYRKLHPPEMSLENRKQCLWDLKEIGYQTGTGFMVGSPYQTVEHLA
EDLLFIKELNPEMVGIGPFIPHHDTPFADEPAGTLELTLFLLSIIRLMLPKVLLPATTALGTIDPDGREK
GILAGANVVMPNLSPVEVRKKYLLYDNKICTGDEAAECRGCLERRMASIGYEIVTDRGDY
>gnl|CDD|188472 TIGR03957, rSAM_HmdB, 5,10-methenyltetrahydromethanopterin hydrogenase cofactor biosynthesis protein HmdB. Members of this archaeal protein family are HmdB, a partially characterized radical SAM protein with an unusual CX5CX2C motif. Its gene flanks the H2-forming methylene-H4-methanopterin dehydrogenase gene hmdA, found in hydrogenotrophic methanogens. HmdB appears to act in in biosynthesis of the novel cofactor of HmdA [Protein fate, Protein modification and repair, Energy metabolism, Methanogenesis]
LADDEALKLFKSDNSRDLLKLFDIASRVRDYFRGKIKLTSTIHITNICHVRPKCLYCGFAAGTSKEGYYE
PFRKTDEEIKEAAKAIEESGIPRVSCSGAHGYGGKEAVRAARIVKENTSLELLINVGADLTEESIEELAR
YGTDTICCNLETTNEELFKKLKPGEELEDRIRVCEMVCKYGIELSSGLLIGIGESYEDRLEHLKFLKRFE
NLGEIPIMGFNPYPGTPMENHPPCSLLEQAKTIAVTRLMYPDIRITVPTPTIGPENVQFALMAGADNVAT
VIPDNHPHDVKGVGNPRTGNLEDVVKMIMDLGLKPQL
>gnl|CDD|274881 TIGR03958, monoFe_hyd_HmdC, 5,10-methenyltetrahydromethanopterin hydrogenase cofactor biosynthesis protein HmdC. Members of this protein family are HmdC, whose gene regularly occurs in the context of genes for HmdA (5,10-methenyltetrahydromethanopterin hydrogenase) and the radical SAM protein HmdB involved in biosynthesis of the HmdA cofactor. Bioinformatics suggests this protein, a homolog of eukaryotic fibrillarin, may be involved in biosynthesis of the guanylyl pyridinol cofactor in HmdA [Protein fate, Protein modification and repair, Energy metabolism, Methanogenesis]
MHDLIKEAVNDLDAALELRKLAINTEKDIIEVVDAVGDLSREETQKLGSNFRRFPLGCDLTEIAVGPCAS
DLTLPDLLGNCMLSDTMGAPIHVCAYAFADIAEAEGMRPIELMREVRENVEVPLDLDHFGRYGPMRFPKE
ITGCGGQCYLEGPPFKGCPRGRIHKRLIDKEKEYLEDFEEWIKLSSSVCVNVTEEQGGEEHAAPLDEMKD
VAELARKYGKGVEAIMHVGDGYDDLITGLKACLDMGVDVFVVEGGPFNRAKDRLKAFARAVAAARILVPG
KVVATNGAYEDECRVGLRSGLNAILSGFPKNHHGYMCGYSPGTAKRGNFGLPRVLKIIKEEAESRWTHVP
IQKEELEALARAVKFLGNNLVYPRKIGGTYIGDAHWAALPNSNLYRRLHVNKTVDDIEDGVIADTVALLG
GRFVSWGIADALDGGVDEVYISDADPWVEHATIKNLRSELGTNAYPGNGDDKKALESADKSIITSTIPEI
ALKIKNKFGDAVTLI
>gnl|CDD|274882 TIGR03959, putative_iron-only_hydrogenase_system_regulator, putative iron-only hydrogenase system regulator. Members of this protein family occur as part of a system for producing iron-only hydrogenases, dependent on radical SAM proteins HydE and HydG and GTPase HydF. One member of this family, TM_1266 from Thermotoga maritima, has a known crystal structure. The small size, about 80 residues, and a distant relationship to the nickel regulator NikR of the CopG transcriptional regulator family suggest a role as a transcription factor [Regulatory functions, DNA interactions]
RIAVVGIIVEDRESVAKVNEILHEYGDYIIGRMGIPYREKGVSIISIIVDATTDEIGALTGKLGMIKGVS
VKTAYS
>gnl|CDD|188475 TIGR03960, radical_SAM_domain_protein, radical SAM family uncharacterized protein. This model describes a radical SAM protein, or protein region, regularly found paired with or fused to a region described by TIGR03936. PSI-BLAST analysis of TIGR03936 suggests a relationship to the tRNA pseudouridine synthase TruA, suggesting that this system may act in RNA modification [Unknown function, Enzymes of unknown specificity]
DEILLKVQKPARYIGGEVNSVVKDKEKVDVRFAFCFPDVYEIGMSHLGIKILYDLFNRREDVWCERVFSP
WPDMEEIMREENIPLFGLESQDPIKDFDFLGFTLQYEMCYTNILQMLDLAGIPLLAKDRKEDDPIVIGGG
PCAYNPEPLADFFDLFYLGEGEEVNVELIDLYKKAKKEGGTREEFLERAAKIPGVYVPSLYDVTYNEDGT
IKSFTPNREGAPAKVRKQIVMDMDSVYYPEKFVVPFIKAVQDRVVLEIQRGCIRGCRFCQAGMIYRPTRE
KSLETLKKYARELLKNTGYDEISLSSLSTSDYSQLEELLDFLIDEFKPEHVNISLPSLRIDAFSLDVMSK
IQDVRKSGLTFAPEAGTQRLRDVINKGVTEEDILNGCKQAFEGGWNKVKLYFMLGLPTETLEDIKGIADL
AQKVVDLYYEVPKEPRKGKVQVTVSTSFFVPKPFTPFQWAPQDTMEEYLRKQKHLLDKIKSRSIKYNWHD
SDTSVLEGVLARGDRRLGKVILEAYKKGAIFDGWSEYFDYDIWMEAFEECGIDPDFYAYRERELDEIFPW
DFIDTGVSKKFLVREWERAKAEKVTPNCRQKCSGCGANKLGGGVC
>gnl|CDD|188476 TIGR03961, rSAM_PTO1314, archaeal radical SAM protein, PTO1314 family. Members of this protein family average about 340 residues in length, with a radical SAM domain in the N-terminal 200 residues. The taxonomic distribution is restricted to non-methanogenic archaea, including Picrophilus torridus (locus PTO1314), Sulfolobus sp., Thermoplasma sp., Picrophilus torridus, and Metallosphaera sedula. The gene neighborhood is not conserved, and the function of this family is unknown [Unknown function, Enzymes of unknown specificity]
LKPMTGGNIKRKILGRGVKKLPLIAGHKLLYTCNLRCEMCPFWRRKDEKLLSLEEEIKMMDALERAGVLF
MGFEGGEPLLRRDLPQILEESHKRFHTSLVTNGWLLKDRIKSISEYLDYLFVSIDGIGEVHDKQRGIPGS
FERAVEGIKEAKRYLPVSISFTITNENLDQIFDVVELARKLGVSVSIQVSYDYSTAEKLSPERKKLYDVL
EGLKELKRRGYPIVESEEYFEAIINSWYNGIPWICKPWLTINIDPQGRIVLPCYVLNEYSGKKKVWEVDI
KKLWNSYDWGQYENCNKCALACYLEPSLFSWKKPSMVRERIINNIFSYIADY
>gnl|CDD|188477 TIGR03962, mycofact_rSAM, mycofactocin radical SAM maturase. Members of this family are uncharacterized radical SAM proteins from the Mycobacterium tuberculosis and many other Actinobacteria, as well as some deltaproteobacteria (e.g. Geobacter uraniireducens), firmicutes (Pelotomaculum thermopropionicum and Desulfotomaculum acetoxidans), and Chloroflexi (Thermomicrobium roseum DSM 5159 and Sphaerobacter thermophilus DSM 20745). They resemble several characterized radical SAM enzymes of peptide modification (PqqE, AlbA), and are always found next to the proposed target, TIGR03969, the putative mycofactocin precursor [Unknown function, Enzymes of unknown specificity]
VEQFRRGLDAPICLTWELTYACNLACVHCLSSSGKRDPRELTTAECKRLIDELAAMQVFYVNIGGGEPTV
RPDFWELMDYATAHGVGVKFSTNGVRIDPEVADRLAATDYVDVQISLDGATAEVNDAVRGAGSFDLARRA
MDNLAAAGFRGFKISVVLTRRNFGQLDEFYALADRYGAQLRLTRLRPSGRGADVWDELHPTAAQQRQLYD
WLVAHGERVLTGDSFFHLAALGQPLPGLNMCGAGRVVCLIDPVGDVYACPFVIHEEFLAGNVREDGGFAG
VWRTSPLFRRLREPQSGGACQSCSAYDSCRGGCMAAKFFTGLPLDGPDPECVFGHGTGA
>gnl|CDD|188478 TIGR03963, rSAM_QueE_Clost, putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE, clostridial. Members of this radical SAM domain protein family appear to be the Clostridial form of the queuosine biosynthesis protein QueE. QueE is involved in making preQ0 (7-cyano-7-deazaquanine), a precursor of both the bacterial/eukaryotic modified tRNA base queuosine and the archaeal modified base archaeosine. Members occur in preQ0 operons species that lack members of related protein family TIGR03365 [Protein synthesis, tRNA and rRNA base modification]
FKVVEKFVSINGEGKRAGELATFIRFAGCNLNCSYCDTTWANDKDCPYELLSADEIYDYIKETGVKNVTL
TGGEPLLQENIDELIELLLGDAGLEVEIETNGSVDIAPFKERPDRLIFTMDYKLPSSGMENNMCLDNLSY
LTKKDVVKFVVGSIEDLEKAKEIISKYNLTEKCQVYFSPVFGKIEPEEIVEFMKEHHLNGVRLQLQLHKV
IWDPEMRGV
>gnl|CDD|274883 TIGR03964, uncharacterized_protein_putative_amidase, mycofactocin system creatininase family protein. Members of this protein family are uncharacterized Actinobacterial proteins, with homology to creatinine amidohydrolase from Pseudomonas. Members occur only in the context of the mycofactocin system [Unknown function, Enzymes of unknown specificity]
LADATWPELDGRPATLLVPLGSTEQHGPHLPLDTDTRIATAVAEGAAARLDDRVLLAPAIAYGASGEHEG
FPGTVSIGTEALHLLLVEYGRSACRWAGRVVFVNGHGGNLDALRRAVALLRYEGRDVAWWPCAVAGADAH
AGRTETSLLLHLSPDRVRMDRAEAGNTAPLAELMPRLRAGGVAAVSPNGVLGDPTGATAEEGARLLAEMV
GRCAAAVARWEPDADGRL
>gnl|CDD|274884 TIGR03965, glycosyltransferase_Rv0696_family, mycofactocin system glycosyltransferase. Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin
LRLDRRVRRYGGGRVLLGGSPLRLLRLAPAAARLLGGGRGGALEVRDETSAALLRRLLDSGVVHPRPALL
PSPPSVTVVVPVRNRPAGLARLLAALLALDYPRDRLEVIVVDDGSEDPVPTRAARGARLPVRVIRHPRRQ
GPAAARNAGARAARTEFVAFTDSDVVPRPGWLRALLAHFDDPGVALVAPRVVALPAADTRLARYEAVRSS
LDLGPEEAVVRPRGPVSYVPSAALLVRRRALLEVGGFDERLEVGEDVDLCWRLCEAGGRVRYEPAAVVAH
DHRTRLWPWLARRAFYGTSAAPLARRHPGSVRPMVVPAWTLLALGALAAAGRSSRLALLSALPALADAAT
RLRRARRAGAPLPTRAAALAVARGHGAALYQLASAVCRHYWPVLLLAVLLSRRLRLLVLAALVGDGLVDW
RRLRPGLDPVRFVLLRRLDDLAYGLGVWVGCLRHRTLAALLPQISL
>gnl|CDD|274885 TIGR03966, actino_HemFlav, heme/flavin dehydrogenase, mycofactocin system. Members of this protein family possess an N-terminal heme-binding domain and C-terminal flavodehydrogenase domain, and share homology to yeast flavocytochrome b2, to E. coli L-lactate dehydrogenase [cytochrome], to (S)-mandelate dehydrogenase, etc. This enzyme appears only in the context of the mycofactocin system. Interestingly, it is absent from the four species detected so far with mycofactocin but without an F420 biosynthesis system
TRAWFETVAEAQRRARKRLPRSVYAALIAGTEKGVTLADNVAAFDELGFRPHVAGLPPKRELSTTVMGQE
ISFPVLISPTGVQAVHPDGEVAVARAAAARGTAMGLSSFASKPVEEVVAANPKTFFQIYWVGSRDDILAR
LERARAAGAKGLILTLDWSFASRRDWGSPEIPEKIDLRTMLRFAPEVLVRPGWLLRYLRSGRIPDLTVPN
LALRGETPPTFFGAYGEWMGTPPPTWEDVAWLREQWGGPFMLKGITRPDDARRAVDAGATAISVSNHGGN
NLDGTPAAIRALPAIAEAVGDQVEVLLDGGIRRGSDVVKALALGARAVMIGRAYLWGLAANGEAGVENVL
DILRQGIDSALLGLGKASVHELSREDLVIPEGFTR
>gnl|CDD|274886 TIGR03967, hypothetical_protein_FraEuI1cDRAFT_6405, putative mycofactocin binding protein MftB. Families TIGR03969 and TIGR03962 describe, respectively, the putative mycofactocin precursor and its cognate radical SAM peptide maturase. This small protein family appears in the same sporadically distributed cassette and may serve as a scaffolding protein during mycofactocin maturation or as a carrier protein for the mature product, a putative novel redox carrier. A feature of mycofactocin-encoding genomes is co-clustering with sets of NAD-binding oxidoreductases in which the NAD is not exchangeable. Therefore it is proposed that mature mycofactocin, bound by a member of this family as a carrier protein, docks with the nicotinoprotein to allow electron transfer. Mediation of electron transfer through this system would define a segregated redox pool [Unknown function, General]
DARYRLAPGVALRPEPFGALVYDFGTRRLSFLKDRTLVEVVESLGDAPVAEAALAAAGVPDDQAEPAYLR
ALERLVERGFI
>gnl|CDD|188483 TIGR03968, transcriptional_regulator_TetR_family, mycofactocin system transcriptional regulator. Members of this family are TetR family putative transcriptional regulators that occur in genome contexts near proteins of the mycofactocin system. These include the precursor peptide (TIGR03969), a radical SAM peptide maturase (TIGR03962), and a putative carrier protein (TIGR03967) [Regulatory functions, DNA interactions]
SRPGRRRSTTRAEIETIALELFTERGFDETTVDDIAAAAGIARRTFFRYFASKNDVPWGDFDAHLDALRA
LLAATPDDLPVMDALRRAVLAFNTFPAEEVAEHRQRMRLILRVPALQAYSTLMYAGWRRVIAEFVARRLG
LPPDDLLPRTVGWLTLGVALSAYEQWLADEDADLTELLDAAFRALADGFA
>gnl|CDD|274887 TIGR03969, conserved_hypothetical_protein, mycofactocin precursor. Members of this protein family occur in Mycobacterium tuberculosis and many other Actinobacteria, as well as some delta-Proteobacteria (e.g. Geobacter uraniireducens), Firmicutes (Pelotomaculum thermopropionicum and Desulfotomaculum acetoxidans), and Chloroflexi (Thermomicrobium roseum DSM 5159 and Sphaerobacter thermophilus DSM 20745). Members sometimes are missed during gene model identification but always occur in the vicinity of radical SAM (rSAM) enzyme TIGR03962, which resembles several rSAM enzymes of peptide maturation (PqqE, AlbA). Species with this protein always carry members of unusual clades of nicotinoproteins that are restricted to mycofactocin-containing species and in which the NAD, when studied, has appeared non-exchangeable. It is proposed that the mature form of mycofactocin is a novel redox carrier for a segregated redox pool
EESEVVEELLVEEVSIDGMCGVY
>gnl|CDD|274888 TIGR03970, Rv0697, dehydrogenase, Rv0697 family. This model describes a set of dehydrogenases belonging to the glucose-methanol-choline oxidoreductase (GMC oxidoreductase) family. Members of the present family are restricted to Actinobacterial genome contexts containing also members of families TIGR03962 and TIGR03969 (the mycofactocin system), and are proposed to be uniform in function
SDVLIVGAGSAGSVLAARLSEDPSCTVTVLEAGPGYRDPSRLPAQLTDGLRLPIGPASPVVWRYGVELTD
GPRRASQIVRGRVLGGSGAVNGGYFCRALPADFDAWPIPGWSWDDVLPHFRAIETDLDFDGPLHGTAGPI
PVRRTAELDGISAAFVAAALGAGFGWIADLNGSGPGLPGGVGAVPLNVDGGRRVSTAVAYLLPALKRPNL
TVEADTRVVRILFSGTRAVGVEVLGDGGPRTLRADRVVLCAGAVESAHLLLLSGIGPAEQLRAAGIAVVL
DLPVGSDFVDHPEWVLPYRWRPTHDRPPTSPVLETVLNTADIEIRPYTAGFTALVPGSPRDDPHLGVALM
RPHSRGRIRLASADPADPPRIEHRYDSSAADRAALRAGAALAHELLGSPELGPLLEPAVREGEASWVLAR
LATSQHLCGSCRMGGRDDPGAVVDARCRVRGVEGLWVVDGSILPVIPSRGPHATAVMVAERAAEFLG
>gnl|CDD|274889 TIGR03971, short-chain_dehydrogenase/reductase_SDR, SDR family mycofactocin-dependent oxidoreductase. Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. See EC 1.1.99.36 [Unknown function, Enzymes of unknown specificity]
LEGKVAFITGAARGQGRSHAVRLAEEGADIIAVDICADIDTVPYPLATPDDLAETVRLVEALGRRIVARQ
ADVRDRAALQAAVDAGVAEFGRLDIVVANAGICSIGPLWELTEEQWDDMIDVNLTGVWNTVKAAAPHMIE
RGGGSIVLTSSTAGLKGGPGGAHYVAAKHGVVGLMRSLALELAPHGIRVNAVHPTGVNTPMIDNEAMYRL
FRPDLDTPTDAAEAFRSMNALPVPWVEPEDISNAVLFLASDEARYVTGVTLPVDAGALAK
>gnl|CDD|274890 TIGR03972, rSAM_TYW1, wyosine biosynthesis protein TYW1. Members of this protein family are the archaeal protein TWY1, a radical SAM protein that catalyzes the second step in creating the wye-bases, wyosine and derivatives such as wybutosine, for tRNA base modification [Protein synthesis, tRNA and rRNA base modification]
IKKALRKQGYHFVGRHSAVKPCHWTKKALTGGRSCYKSKFYGIESHRCVQMTPTLAWCNQRCLFCWRPLE
HDVGEEWDETKDDPEDIVEESIKAQRKLLSGYKGNPKVDREKWEEALEPKHVAISLSGEPTLYPRLPELI
EEFHKRGFTTFLVTNGTRPDVLEKLEAEPTQLYVSLDAPDKETYKRICRPVIPDAWERILESLELLPSKS
TRTVIRITLVKGLNMDDPEGYAKLIEKANPDFVEVKAYMHVGYSRYRLTRDNMPSHEEVREFAKKLAELT
GYKILDESEPSRVVLLS
>gnl|CDD|274891 TIGR03973, conserved_hypothetical_protein, six-cysteine peptide SCIFF. Members of this protein family are essentially universal in the class Clostidia and therefore highly abundant in the human gut microbiome. This short peptide is designated SCIFF, for Six Cysteines in Forty-Five residues. It is a presumed ribosomal natural product precursor, always found associated with a yet-uncharacterized radical SAM protein, family TIGR03974, that resembles other peptide modification radical SAM enzymes and is designated SCIFF radical SAM maturase
KHIKTLNKRNLKKSLKKGGCGECQTSCQSACKTSCTVGNQVCE
>gnl|CDD|274892 TIGR03974, six-Cys-in-45_modification_radical_SAM_protein, SCIFF radical SAM maturase. Members of this protein family are predicted radical SAM enzymes universally associated with Six Cysteines in Forty-Five protein, or SCIFF (family TIGR03973), a predicted ribosomal natural product precursor that is nearly universal in the class Clostridia. Similarity of this family to radical SAM maturases (PqqE and subtilosin A maturase) found in the vicinity of other peptide precursors suggests this protein is the SCIFF radical SAM maturase [Cellular processes, Biosynthesis of natural products]
IHQYKNNGYNIVLDVNSGSVHVVDDVTYDVIALYEEGKDKETPEEIKEKLKGKYSEEDIEEAYDEITELK
EAGQLFTEDIYEDYIIDFKKMRKTVVKALCLHVAHDCNLACKYCFAEEGEYHGRRALMSFEVGKKALDFL
IANSGSRRNLEVDFFGGEPLMNFDVVKDLVAYGRSIEKEHNKNFRFTLTTNGVLLNDEIIEFANKEMSNV
VLSLDGRKEVNDRMRPTRNGKGSYDLIVPKFQKLVESRGQKKYYVRGTFTHNNLDFSKDVLHLADLGFKQ
ISVEPVVADPEEPYALTEEDLPIIFEEYEKLAKEMIKRKKEGKGFNFFHFMIDLTGGPCVYKRLSGCGSG
TEYLAVTPWGDLYPCHQFVGNEEFKMGNVFDGITNTDIRDEFKKCNVYSKEKCKDCWARFYCSGGCAANS
YNFTGDINDPYDLGCELQRKRIECAIMIKAA
>gnl|CDD|274893 TIGR03975, hypothetical_protein_PPSIR1_38941, ribosomal peptide maturation radical SAM protein 1. Models TIGR03793 and TIGR03798 describe bacteriocin precursor families to occur often in large paralogous families and are subject to various modifications, including by LanM family lantibiotic synthases and by cyclodehydratases. This model represents a radical SAM protein family that regularly occurs in the context of these bacteriocins, and may occur where other familiar peptide modification enzymes are absent [Cellular processes, Toxin production and resistance]
VALVNMPFASIERPSLALGLLKAALRQAGLSARVLYANLDFAERIGLDLYEYISESRPETLAGEWLFAGE
LFPEFDPSHDEYLRLILAEEGRLGWLGRLRDPKAALRALRAVIPGFIEECAADIAAGRPRIVGFTSTFQQ
TCASLALLRRIKELAPEIVTVFGGANCEGEMGAELIRSFPWVDYVFSGEGDDSFPALCRRILDKGRDPDA
IPGVSHRDGGEAERPAPRAPVTDLDALPTPDYDDYFEQLGASRLAGAIQPKLPFETSRGCWWGQKHHCTF
CGLNGGGMQYRSKSPDRVLDELEELARRYGLRKFEAVDNILDMNYFKTLLPRLAERKPDLRIFYEVKANL
RREQLRQLADAGVRYIQPGIESLSTRLLKLMDKGVTALQNIQLLKWCREFGIQVSWNILYGFPGESAEDY
AEMLELLPLLHHLQPPSGVGRIRLDRFSPYFSRPERFGLRNLRPAPAYAYIYPLDREDLERLAYFFDDDL
NPAEETDRPYVAALDRAVNAWKEAWQRETPPRLSMYFDAGDRITIEDTRPCAVAREYRLTGLAAQVYQLC
DSPVSEARLLEKLDEASPGEIEEILAELVARKLLLREEGRLLALAL
>gnl|CDD|274894 TIGR03976, hypothetical_protein, His-Xaa-Ser system protein HxsD. This rare conserved hypothetical protein of small size occurs exclusively, and perhaps universally, in the context of a pair of (uncharacterized) radical SAM proteins, TIGR03977 and TIGR03978. Many members of this family have invariant motifs LYW and LLNDYxLRE, but PSI-BLAST starting from family members well below 20 % pairwise sequence identity to this group eventually brings in the entire family as modeled here. The family TIGR03979 represents the fourth regularly conserved member of this system
LDKEIYSEDVVRKAAYWFSDRFYIHLGEDDNQWFVTFEAKEEEGNTADEEVEKEFENELNDQQLREQIEK
KTGDIREIIVAKALASIDDR
>gnl|CDD|274895 TIGR03977, radical_SAM_domain_protein, His-Xaa-Ser system radical SAM maturase HxsC. This model describes the downstream member, HxsC, of a pair of uncharacterized radical SAM proteins, regularly found in the context of a small protein with four or more repeats of the tripeptide His-Xaa-Ser (HXS). This enzyme appears to be part of a peptide modification system
SLEDGDVVRVNPDGRVRVLYRRRSNHNTLLVTERCNNYCLMCSQPPKKVDDSWLLDEALEAIALFPENPR
VLGITGGEPTLLGEGFFRFLRFIKKKLPQTALHVLTNGRAFSDREFAKQLAALCHERLTFGIPLYAAIAE
LHDYIVQARGAFEETIRGLYNLGRLGINIELRIVVTKLNYERLPELAEFIARNLPFVSHVALMGLEPTGF
AKKNWDALWIDPADYFEELSEAVLILRRRGIPVSLYNFPLCHLPPSLWPYARQSISDWKNYYPEECEDCA
LKSSCGGFFSSS
>gnl|CDD|274896 TIGR03978, paired_radical_SAM_protein_1, His-Xaa-Ser system radical SAM maturase HxsB. This model describes the upstream member, HxsB, of a pair of uncharacterized radical SAM proteins, regularly found in the context of a small protein with four or more repeats of the tripeptide His-Xaa-Ser (HXS). This enzyme appears to be part of a peptide modification system
LLPFNFERLSDDKVLITNDAGEHIFLSNEELQRLVNGELTPSSELFKELRSKHFISDGDDSYAMRLLASR
LRKRKSFLQDFTPLHIFVPTLRCNHSCKYCQVSRASEDASGFDMSEETARKAVDLIFQSPSPSLKIEFQG
GEPLLRFDLIKKIVEYAEEKNKSENKEIEFVIATNLSLLTDEMLDFFKDHKVLISTSLDGPEALHNKNRP
LPGGNSYEKVVSGLKKARERLGPDRVSALMTTTKESLKYPEEIVDEYVRLGFNSIFLRPLSPYGFARKNE
QKIGYTAEEFLAFYKKALDYIIELNKQGVPFREHYAAILLRRILTPFATGYVDLRSPSGAGLGVLVYNYD
GDVYPSDEARMLAEMGDITFRLGNVNSDSYESLFGSEKLRAILSASLNESLPGCSDCAYQPYCGADPVQN
YSTQGDIIGHKPLSEFCQRHKGIFDYLFELLYENDPEAAKILKSWA
>gnl|CDD|274897 TIGR03979, His_Ser_Rich, His-Xaa-Ser repeat protein HxsA. Members of this protein share two defining regions. One is a histidine/serine-rich cluster, typically H-R-S-H-S-S-H-R-S-H-S-S-H. Members are found always in the context of a pair of radical SAM proteins, HxsB and HxsC, and a fourth protein HxsD. The system is predicted to perform peptide modifications, likely in the His-Xaa-Ser region, to produce some uncharacterized natural product
RLAALLPGVLALGFAPTKGAAAPEAGLTDDNLEPTDVELAPLNVDIPNLLAGHRSHSSHRSHSSHGSHAS
SASGSYSVPSGDTSTYSYPVPSPSYSPSPGSSIQSLPSTTGVRPQSSASNANSEKRKLLVIRVQTALVVF
GYYGGIIDGVMGEATRVALKRYQMDNGLPVTGTIDTQTLNALGISA
>gnl|CDD|274898 TIGR03980, conserved_hypothetical_protein, hybrid cluster protein-associated redox disulfide domain. Members of this protein family resemble the domain of unknown function DUF1858 described by pfam08984, but all members contain an apparent redox-active disulfide. In at least one member protein, a cysteine in the CXXC motif is substituted by a selenocysteine. Most member proteins consist of this domain only, but a few members are fused to or adjacent to members of the hybrid-cluster (prismane) family or the nitrite/sulfite reductase family [Energy metabolism, Electron transport]
ITKDMTIGEILRKYPETAEVFMRFGMHCVGCPSAQFETLEEAAMVHGIDVDELLEELN
>gnl|CDD|188496 TIGR03981, putative_methylamine_utilization_protein_MauG, His-Xaa-Ser system putative quinone modification maturase. One clue for the interpretation of this protein family is homology to the MauG protein (see TIGR03791) involved in the tryptophan tryptophylquinone post-translational modification of methylamine dehydrogenase light (beta) chain. The other is occurrence only in a five gene context in which two members are radical SAM proteins (TIGR03977 and TIGR03978) also likely involved in post-translational modification
VLLLGFLASTRTYALSLDDRLTRVIETFSLNPASCQTNPQIKNPNLAAVGRVLFNTPVLSGGKDTSCATC
HLDSKALTDGLPVAVGVGGHGEGEERLASDGIVVPRNAFTLFNRSHSKYKTFFWDGKVIAQDGKIFSPIG
EGASLGFNSALAVAAVLPLLARDEFLGEQQIYRSSRHLDLVESVYYDEKVNAANKLIQERLLTFNSEEVK
ELLKLKEEAGIETADLTLPNVGNALASFIAVKVSNECQVSQWEKYLAGNKPALSPVQKRGAILFFGKGRC
AACHSGDLFSDMGFHSIGVPQGDFGTHIHGQDIGRAGVTFDQKDRYKFRTPPLLGVSKTPPYGHNGSFQD
LITVVRFHVNPIPFLAKNGWTSERELLTYGKILSSRSEILGYIDVESEQELEALVSFLEGL
>gnl|CDD|188497 TIGR03982, hypothetical_protein_MDG893_13129, His-Xaa-Ser system protein, TIGR03982 family. Members of this rare protein family occur in the presence of TIGR03981 and TIGR03979, which in turn occur only in the context of radical SAM protein families TIGR03977 and TIGR03978. The function is unknown
KTVFYFIVSLFCIAWIGKNIVAPVFAYFYYKNQYMELAAQCANAMDETWFIEQLGSDTLNQTAKVHLLAC
HEYDKTRKIMLAMGLPESVLGYLGLEALELHQRSIEPLVEQHRFRER
>gnl|CDD|274899 TIGR03983, hypothetical_protein_LA3181, CRISPR-associated endonuclease Cas1, subtype MYXAN. Members of this protein are the Cas1 endonuclease, or Cas1 domain in Cas4/Cas1 fusion proteins, of the MYXAN subtype of CRISPR/Cas systems. These systems typically feature repeats and spacers each about 36 base pairs in length. Species with this type of CRISPR system include Myxococcus xanthus, Cyanothece sp., Leptospira interrogans, Sorangium cellulosum, Anabaena variabilis ATCC 29413, etc
PVRLFPEDDERQVLHVLEPGTRIGRTGEQLKVTRREGADEKIPIQQVSQVVLHGFSQISTQALHFLASEE
IGVHWVSGGGRYIGSFDGRSGSVQRRIRQFRALTQEDFCLGLARKLVAAKGEGQLRFLLRAKRGDKESRP
ELESAIAQMRAVLKQVEQAESLESLLGIEGNLAALYFGALPALLGKDVDDSLRFSGRNRRPPKDRFNALL
SFGYSLLYKDVMNAILAVGLEPAFGFYHQPRTQAPPLALDLMELFRVPLVDMPVVGSINRRQWDIDEDFE
ITGQQVWLSDSGRRKFIELYERRKAETWKHPVLGYSLSYARLIELEVRLLEKEWSGEPGLFAQLRVR
>gnl|CDD|274900 TIGR03984, hypothetical_protein_FrEUN1fDRAFT_5778, CRISPR-associated protein, TIGR03984 family. Members of this protein family are found exclusively in CRISPR-containing organisms, in operon contexts with RAMP (repeat-associated mystery protein) proteins also linked to CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats)
LLAWSDHGVCWGRLDEGKLHFYDDEALALDPSYLFEARLFNENGELRWWRSDGQGKARLLSDEGEAGEEV
EAIDARQLLWGEPVEAPTGGWTLLAEGRGGKLIVPLELLLKNLLKNAARVYLVTREYIGYDDIGQAGVID
ERLVKLE
>gnl|CDD|274901 TIGR03985, hypothetical_protein_sll7078, CRISPR-associated protein, TIGR03985 family. Members of this protein family belong to CRISPR-associated (Cas) gene clusters. The majority of members are Cyanobacterial
QRLFLHLDYILSEEKQERVDDYQEQLEQLWQENPGPPVQFDYWSARLNKTVNVTVYPVCLYYARRAKYLC
AYGQDPEGQVGWYNYRLDRISSKLAVLSWDDPDIPLPLQQRYQQGELPTPDYIQEQLDEAWGFDFYLPAD
LLILRFPPDFARRYIDNTFRHPTFKKISYSELVQLIQQQAKSTEQQQLLEIVRQRPPTDAYYRLWYRVGD
INVIMRLRDWRPNVEVIAPLKLRQQMAEEAQAELQFYQ
>gnl|CDD|274902 TIGR03986, CRISPR-associated_protein, CRISPR-associated protein. Members of this protein family, part of the larger RAMP family, are found exclusively in species with CRISPR systems, in local contexts containing other RAMP (Repeat-Associated Mystery Proteins)
PYNFVPLPDKVIKAYDLEDGPPSHDRYHKDLLSGRIECTLTTKTPLFIGDSKKENNENQHKSYEFFSDPD
GKPAIPGSSLRGMLRNLVEILTNSKFRVFNDKRLFYRDPAGRGGSYKPAYIRGLPNRDKAGFLKLVKEKD
EYAIRPAVKGPSYRIDGKVVKLYLLKKEKKIDEFKYAKTSEGYKPVRHKGKKVVAKSIEIARSRNWLHFP
EENGLTEGYLVKTGRIVGKKHNYAFFFPPKEEEDARIRLDKELIEDYQEDESEQLKGRRDNNSSDLLKEY
RKLPEGLKPVFYVEPDEGGKVTSFGHSPIYRLAYERSIGDLLPEELKPSESEEKLDPAEAIFGWVDGDAG
ESQALAGRVSFSDAVLVKPGPEYDEEVTLAILGSPKPTTYQFYLEQRDGADRDTYDGYDDEGAVLRGRKF
YWHHRESDDELEKNSENPNKNEKLNTVIKPVKEGTTFRFRIRFENLSPVELGALLWALDLGEGWYHKIGM
GKPLGFGSVKITVDGLFLLNRKERYSSLFASDDATEKVDEYIEAFKKYMEEKLGSSLKETAQIEDLKALL
SW
>gnl|CDD|274903 TIGR03987, TIGR03987_family_protein, TIGR03987 family protein. Conserved hypothetical protein
LIFAIIFITLALVFYTIGVFSERKSGTLKKWHVIFFWLGLVCDTTGTTLMSKIAKSSGSSFSIHGITGLL
AIILMLFHAVWATIVLVKKDEKKKATFHKFSIVVWLIWLIPYIIGMIIGM
>gnl|CDD|274904 TIGR03988, antisig_RsrA, mycothiol system anti-sigma-R factor. Members of this family are the anti-sigma-R factor RsrA, which contains a CXXC motif as a thiol-disulphide redox switch. It interacts with sigma-R. It regulates and is regulated by the mycothiol system, which occurs in many actinomycetes [Transcription, Transcription factors]
DCSEVLAEVYEYLDGELDDEDCARLRAHLDECPPCLEQYGLEEEVKSLVARCCGGESAPEELRARILARI
REIRVII
>gnl|CDD|274905 TIGR03989, Zn-dependent_alcohol_dehydrogenase_class_III, NDMA-dependent alcohol dehydrogenase, Rxyl_3153 family. This model describes a clade within the family pfam00107 of zinc-binding dehydrogenases. The family pfam00107 contains class III alcohol dehydrogenases, including enzymes designated S-(hydroxymethyl)glutathione dehydrogenase and NAD/mycothiol-dependent formaldehyde dehydrogenase. Members of the current family occur only in species that contain the very small protein mycofactocin (TIGR03969), a possible cofactor precursor, and radical SAM protein TIGR03962. We name this family for Rxyl_3153, where the lone member of the family co-clusters with these markers in Rubrobacter xylanophilus [Unknown function, Enzymes of unknown specificity]
KTKAAVLWGPGQPWEVEEIELDDPKAGEVLVKLVASGLCHSDEHLVTGDLPMPRYPILGGHEGAGVVTKV
GPGVTGVKPGDHVVLSFIPACGRCRYCSTGLQNLCDLGAALLTGSQISDGTYRFHADGQDVGQMCLLGTF
SEYTVVPEASVVKIDDDIPLDKACLVGCGVPTGWGSAVNIADVRPGDTVVVMGIGGVGINAVQGAAVAGA
RKVIAVDPVEFKREQALKFGATHAFASMEEAVQLVRELTNGQGADKTIITVGEVDGEHIAEALSATRKGG
RVVVTGLGPMADVDVKVNLFELTLLQKELQGTLFGGANPRADIPRLLELYRAGKLKLDELITRTYTLDQI
NEGYQDMLDGKNIRGVIVY
>gnl|CDD|274906 TIGR03990, Arch_GlmM, phosphoglucosamine mutase. The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result [Central intermediary metabolism, Amino sugars]
MLLFGTSGIRGIVGEELTPELALKVGKAFGTYLRGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLG
IAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESGDFERADWDEIG
TVTSDEDAIDDYIEAILDKVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGR
NPEPTPENLKDLSALVKATGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLLEHGGGKVVTNVS
SSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEE
GKPLSELLAELPKYPMSKEKVELPDEDKEEVMEAVEEEFADAEIDTIDGVRIDFEDGWVLVRPSGTEPIV
RIYAEAKTEERAEELLEEGRSLV
>gnl|CDD|274907 TIGR03991, alt_bact_glmU, UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase. The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Homologs of this enzyme are identified in a number of bacterial organisms and modeled here. A number of these are observed in proximity to the GlmS and GlmM genes, and phylogenetic profiling by PPP identifies the LEPBI_I0518 gene in Leptospira biflexa as a likely Glm-system candidate. Multiple sequence alignments of these bacterial homologs with their archaeal counterparts reveals significant structural differences, necessitating the construction of separate models [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
MQILLFEDRGVEALLPLTFTRPVYELRCGIFTLRERWERLLGSAKFTTHRNPLTEDYLAGRYPLVLVNRL
LEVDALLVNGRLLPWDLIATNGKAIERDFELLTEGRKSIPVHDGSVVVVNPSHVFIEEGATVRPGAVLDA
SDGPIYIGKDARIEPFSFLEGPVYIGPGARVKAGARIYGGTSIGPTCKIGGEVENSIIEGYSNKHHDGFL
GHSYLGSWCNLGAGTNTSDLKNNYGEVKIREGDGFVDTGLQFLGLFMGDHSKCGIGTMFNTGTVVGVGSN
IFGSGFPPKYVPSFTWGGSGGFTEYRLDKAIETARKVMARRKVELSAAEEELLRALF
>gnl|CDD|274908 TIGR03992, Arch_glmU, UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase. The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them
MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRG
GVPIEYVVQEEQLGTADALGSAKEYVDDEFLVLNGDVLLDSDLLERLIRAEAPAIAVVEVDDPSDYGVVE
TDGGRVTGIVEKPENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF
WLDVGRPWDLLDANEALLDNLEPRIEGTVEENVTIKGPVVIGEGAVIRSGTYIEGPVYIGKNCDIGPNAY
IRPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCNFGAGTKVANLRHDDKPVKVTVKGK
RVDTGRRKLGAIVGDGVKTGINVSINPGVKIGSGARIYPGEVV
>gnl|CDD|274909 TIGR03993, HupJ_contains_rubredoxin_domain [NiFe] hydrogenase assembly chaperone, HybE family. Members of this family are chaperones for the assembly of [NiFe] hydrogenases, in the family of HybE, which is specific for hydrogenase-2 of Escherichia coli. Members often have an additional N-terminal rubredoxin domain
LLEAAFREIAERRMRDLPFYNPALPVEAVGFRLFEGQWIGVVITPWFMNLVLLPGPGQDWPARTVGEKLA
LALPAGTYEFTVGELEGIGQYLSCSLFSPMFEFLDQEQAVALAEAALRALLSLPVAAPAARAPPAPSRRA
FFR
>gnl|CDD|274910 TIGR03994, coproporphyrinogen_dehydrogenase_HemZ, coproporphyrinogen dehydrogenase HemZ. Members of this radical SAM protein family are HemZ, a protein involved in coproporphyrinogen III decarboxylation. Alternative names for this enzyme (EC 1.3.99.22) include coproporphyrinogen dehydrogenase and oxygen-independent coproporphyrinogen III oxidase. The family is related to, but distinct from HemN, and in Bacillus subtilis was shown to be connected to peroxide stress and catalase formation [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
KNELKRLLYRLLSEYTGKELPWGTLTGVRPTKIAMDLLEEGKTEEEIRARFRETYLVSEEKADLAIDIAR
REKPLLKQIDYENGYSLYVGIPFCPTRCLYCSFTSYPIGKWKKRVDEYLDALCKELEAVAKILKGLKLDT
VYIGGGTPTTLSAEQLERLLGKIEENFDLSHLREFTVEAGRPDSITAEKLEVLKRHGVTRISINPQTMND
KTLDLIGRRHTVEDIKEAFALAREAGFDNINMDLIAGLPGETLEDVRDTLEQVKKLAPESITVHTLAIKR
ASRLNQEKDKYQLPSFEDTAEMIDLAAEYARDMGMEPYYLYRQKNMAGNLENVGYAKPGKEGLYNILIME
EKQTIIALGAGASTKLVFPEGGRIERIENVKDVYEYIERIDEMIERKRKLL
>gnl|CDD|274911 TIGR03995, hypothetical_protein_BcellDRAFT_3296, putative rSAM target protein, CGCGG family. Members of this family of small proteins, approx. 100 amino acids in length, co-occur with a subfamily of radical SAM protein in several species in the Halobacteria and in Bacillus. The radical SAM protein belongs to a branch in which most characterized members act on peptide substrates. The lack of homology of this family to any known enzyme and the distinctive C-terminal region motif, with the common modification target residue Cys flanked by sterically permissive Gly residues
KHDTSWSANLEHPEYADDRDLVVRQAIDAVDETAAGNHVNLVTHGEHGHPEEYLTDALEEAFGESIDVEY
VDQCGCGGHVTRVY
>gnl|CDD|188511 TIGR03996, mycofact_OYE_1, mycofactocin system FadH/OYE family oxidoreductase 1. The yeast protein called old yellow enzyme and FadH from Escherichia coli (2,4-dienoyl CoA reductase) are enzymes with 4Fe-4S, FMN, and FAD prosthetic groups, and interact with NADPH as well as substrate. Members of this related protein family occur in the vicinity of the putative mycofactocin biosynthesis operon in a number of Actinobacteria such as Frankia sp. and Rhodococcus sp. The function of this oxidoreductase is unknown
RLSQAITLAGRRAPSRVLFGPHETNLGRGRALSERHVAYYERRAAGGAGIVVTEVASVTSDDWPYERAPL
ASECGSGWAAVAAACRPHGTLVLAGLGHTGGQGSSAYSQSVLWGPSPVADVVSREVPMEMDQAEIDSLVA
GFRAGAARAVAAGLDGVELDAGPRSLLRQFLSGLTNRRGDDYGRDRLRLTREVLTAVREEVGDTPILSLR
LSCDEEAPWAGITPDLAAGHAGALADLLDLLVVVRGGPFSTGAYRPDFHTPPAFNTDLCRRIRRAAAGRV
PVVLQGSVVDTADAQQALDSAVADVVEMTRAQIADPDLVVKAGRGHRPRPCVLCNQTCQVRDPRNPVVTC
VGNPAAGHETVDPDEGGRAATPGDVLVVGGGPAGLEAARVLAARGHRVTLAERSAHLGGMLRIAARGPGL
HRLAALADWLEAECRRLGVRIRLGAAIGVEELDRARAAGGVVLLATGSVPRPLPAPVDATVRVLDAVHVL
AAGPALPQGPVVVHDPLGGPVGVATAEWLAALGRPVSIVTPDSVVGSRLGASGDLAPANTRLQRAGVTRQ
LRSRVRAIGPDGLVLEDAWTGERSILACAVVIDCSPRLPRDTLHSLRPDLPRAGDAVAPRTILEAVREGR
RRA
>gnl|CDD|274912 TIGR03997, NADH:flavin_oxidoreductase, mycofactocin system FadH/OYE family oxidoreductase 2. The yeast protein called old yellow enzyme and FadH from Escherichia coli (2,4-dienoyl CoA reductase) are enzymes with 4Fe-4S, FMN, and FAD prosthetic groups, and interact with NADPH as well as substrate. Members of this related protein family occur in the vicinity of the putative mycofactocin biosynthesis operon in a number of Actinobacteria such as Frankia sp. and Rhodococcus sp., in Pelotomaculum thermopropionicum SI (Firmicutes), and in Geobacter uraniireducens Rf4 (Deltaproteobacteria). The function of this oxidoreductase is unknown
RLFSPLRIGPVTLPNRIVFGAHLTNYAVNNLPSERHAAYYAERAKGGAGLIITEELSVHPSDRPYEKLID
GYRPAVIPGYRRITDAVHAHGVKIFAQLNHNGGQGDSSYSRLPVWAPSAVPDPLFREVPKAMEESDIAEV
VAGFARVAGHVVAGGFDGIEIQASHSSLVRQFLSPLTNRRTDEYGGSLENRARFLLEVLEAVRKAIGPDR
ALGVRLCGDELVPGGLTLADAVEIARLLEALGLVDYINTSIGVATYTLHLVEASMHVPPGYAAFLAAAIR
EAVDLPVFAVGRINDPAQAERALAEGQADLVGMVRGQIADPDFAAKALEGREEDIRTCLSCNQECIGRVG
LNRWLGCVVNPRAGREFGTVTLPPPRRPKRVLVVGGGPAGLEAAATAARRGHRVTLFEREDRLGGQVRLA
ARLPGRGEFADLIRNLASELRRAGVEVRLGVEADAELVLAEKPDAVVVATGSRPVRPPWAGADGPRVVTV
REVLTGRAEPGGRVLVVDELGFHQATSVAEFLAARGKKVTIITPSLFVGQDLGPTLDLEGWYRRAFQKGI
EQTTDSLVTAVDGGTVTVVHHPTGRVRVLTGVDWVVLAAPPRPDDELYLSLKGRVPEVYRIGDCLAPRRV
HAAIREGHRVGLAI
>gnl|CDD|274913 TIGR03998, thiol_BshC, bacillithiol biosynthesis cysteine-adding enzyme BshC. Members of this protein family are BshC, an enzyme required for bacillithiol biosynthesis and described as a cysteine-adding enzyme. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
FSKLFADYLNGDAAVASFFPYDPHQEEAFERRLEDLAKRNFDREALANLLKAYNKRLGLSEATEQNIEKL
ADGNAVVVVTGQQAGLLTGPLYTIYKAISAIVLAKELEEKLGRPVVPVFWIAGEDHDFEEINHTYVPEKK
GTLKKITLEAKGATKRAASGHRLLKEELAEWLETLFDLLPETEHTNELLELLKRAYRESDTLADAFARLM
HSLFADYGLVLLDPDDPELRQLEAPFFKRILEKADAVSAAVAATQEQLERAGYTPQVETEPRAANLFYVE
DGERELLEYDGDRFVLKDTERTFTREELLEILERHPERFSNNVVTRPLMQETLLPTLAYVGGPGEIAYWA
QLKEVFELFGLKMPPIVPRLSATLIEPRVEKLLDKYQLSVADIFTGVEGLKERFLERQDPEPIDALFEEA
KEQITAAHKPLREELAAVDPTLQGLAEKNLAKITKQVEFLEKRLLRAIRRKHDVELQQFDRIQTNLRPNG
ALQERVWNVFYYLNKYGPDLIEKLLEAPFPYTGEHKLI
>gnl|CDD|274914 TIGR03999, thiol_BshA, N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA. Members of this protein family are BshA, a glycosyltransferase required for bacillithiol biosynthesis. This enzyme combines UDP-GlcNAc and L-malate to form N-acetyl-alpha-D-glucosaminyl L-malate synthase. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
MKIGITCYPTYGGSGVVATELGKALAERGHEVHFITSSQPFRLEKFHPNIFFHEVEVNQYPLFQYPPYDL
ALASKIAEVAKEEKLDLLHVHYAIPHAIAAYLARQMLGKEGIDIPIVTTLHGTDITLVGADPSFKPAVRF
SIEKSDGVTAVSESLKEETYELFDIDKPIEVIPNFVDTDRYRRKNDPALKRKLGAPEDEKVLIHISNFRP
VKRVEDVIEVFARVQQEVPAKLLLVGDGPERSPAEQLVRELGLTDRVLFLGKQDDVAELLSISDLFLLPS
EKESFGLAALEAMACGVPVIASNAGGIPEVVEHGVTGFLCDVGDVETMAEYAISLLEDEELLQRFSAAAR
ERAKERFDSEKIVPQYEALYRRLL
>gnl|CDD|188515 TIGR04000, thiol_BshB2, bacillithiol biosynthesis deacetylase BshB2. Members of this protein family are BshB2 (YojG), an enzyme of bacillithiol biosynthesis; either BshB1 (YpjG) or BshB2 must be present, and often both are present. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
RHVLVIFPHPDDEAFGVAGTIALYRQKGIPVTYACLTLGEMGRNMGNPPFATRESLPEIRKKELIEACKA
MGITDLRMLGLRDKTIEFEDDEELADMVKGIIEELNPSLIITFYPGYAVHPDHDATGRAVIRAVRRMPKS
ERPTVHAVAFSNDAEEELGEPDIVTDVSEVAETKLAAIRAHRSQTAGMLKELEKKDDDGEPEALEWLGVE
RFYTYQF
>gnl|CDD|274915 TIGR04001, thiol_BshB1, bacillithiol biosynthesis deacetylase BshB1. Members of this protein family are BshB1 (YpjG), an enzyme of bacillithiol biosynthesis; either BshB1 or BshB2 (YojG) must be present, and often both are present. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
KLDILAFGAHPDDVELGCGGTIAKYVQQGYKVGICDLTRGELSSNGTVESRQEEAAAAAEILGVSARINL
GLPDRGLNPTEENIREVVEVIRRYRPKLVFAPYPEDRHPDHGKAARLVTEACFYAGLRKYETETPQEPHR
PRHVYYYMQNGFHEPDFVVDVSETYEQKRAALLAYKSQFYRPPDSPQTPLTNGEFLESLEARDRYFGKQI
GVAYGEGFILEKPLGL
>gnl|CDD|188517 TIGR04002, TIGR04002_family_protein, TIGR04002 family protein. TIGR04002 family proteins, a division within DUF1393 (pfam07155), occur strictly as part of a tandem gene pair with an uncharacterized radical SAM protein [Unknown function, General]
FAALICLTTAYIFHIPVGPNGGYVHFGDAFIYLAASLLPTPYALAAAAIGGGLADLLTGAPIWAPPTIII
KPLIVLPFTSKSDKILNVRNVVAPFVAGIISTVGYYLAEGILFGSFTAAFASIAGGLVQSGGSAVIFIIL
GAALDKIGFKK
>gnl|CDD|188518 TIGR04003, benzylsuccinate_synthase_activating_enzyme [benzylsuccinate synthase]-activating enzyme. Members of this radical SAM protein family are [benzylsuccinate synthase]-activating enzyme, a glycyl radical active site-creating enzyme related to [pyruvate formate-lyase]-activating enzyme and additional uncharacterized homologs activating additional glycyl radical-containing enzymes [Protein fate, Protein modification and repair]
PLITEIQRFSLQDGPGIRTTIFLKGCPLRCPWCHNPETQDTRQEFYYYPNRCVGCGRCVAVCPAGTSRLV
DNSDGRTIVVVDRTKCQRCMRCVAACLTEARGIVGQAMSVDEILREALSDSPFYRNSGGGVTISGGDPLM
YPEFTLELARRLHDRGVHVAIETSCFPKHWEVMEPLVEHVDLFIVDLKCLNAKKHEEVVGWPLQPILRNL
ENLFERNATVRIHIPVIPGFNDSEEDFDDYAEYLAGHADRLNGVDILNYHSYGEGKYAALGRMETYQYAG
VAENPAEKVVPLVKALKDKGIPGVTIGGLVGITC
>gnl|CDD|188519 TIGR04004, WcaM, colanic acid biosynthesis protein WcaM. This protein of uncharacterized function is the final gene in the conserved colanic acid biosynthesis cluster observed in Enterobacteraceae
PSKKLSRRTFLTASSALAALPLLHSRFARALEGRQTVNIADYNPDDWIASFKQAFSEAQTVVVPAGLVCE
NINTGIFIPAGKTLRVLGALRGNGRGRFVLQDGCQVVGEKGGSLHNITLDVRGSDCVIKGIAMSGFGPVT
QIYIGGKKPRVMRNLTIDDITVTHANYAILRQGFHNQVDGARITNSRFSDLQGDAIEWNVAINDRDILIS
DHVIERINCTNGKINWGIGIGLAGSTYDNAYPEDQAVKNFVVANITGSDCRQLVHVENGKHFVIRNVKAK
NITPDFSKKAGIDNATVAIYGCDNFVIDNIDMVNSAGMLIGYGVIKGKYLSIPQNFKLNNIHLDNRQLAY
KLRGIQISSGNATSFVAITNVDMKRATLELHNKPQHLFLRNINVMQESAVGPALKMNFDLRKDVRGKFMA
KDDTLLSLANVHAVNEKGQSSVDIDRINHQVVNVEALNFRLPER
>gnl|CDD|188520 TIGR04005, wcaL, colanic acid biosynthesis glycosyltransferase WcaL. This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species
MKVSFFLLKFPLSSETFVLNQITAFIDMGYEVEIVALQKGDTQNTHAAWTEYNLAAKTRWLQDEPEGKLA
KLRYRASQTLRGLFRASTWKALNMSRYGDESRNLILSAICGQVPQPFKADVFIAHFGPAGVTAAKLRELG
VIDGKIATIFHGIDISSREVLNHYTPEYQQLFRRGDLMLPISDLWAGRLKAMGCPPEKIAVSRMGVDMTR
FTHRPVKAPGTPLEIISVARLTEKKGLHVAIEACRQLKAQGVAFRYRILGIGPWERRLRTLIEQYQLEDV
VEMPGFKPSHEVKAMLDDADVFLLPSVTGTDGDMEGIPVALMEAMAVGIPVVSTVHSGIPELVEAGKSGW
LVPENDAHALADRLAAFSRIDTQTLRPVLTRAREKVEADFNQQVINRQLASLLQTL
>gnl|CDD|188521 TIGR04006, wcaK, colanic acid biosynthesis pyruvyl transferase WcaK. This gene is the pyruvyl transferase involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species
MKLLILGNHTCGNRGDSAILRGLLDAINQLEPEAEVDVMSRYPVSSSWLLNRPVMGDPLYSQMKQHNNAA
GVMGRVKKVLRRRYQHQVLLSRVTDTGKLRNIAIAQGFTDFVRLLSGYDAIIQVGGSFFVDLYGVPQFEH
ALCTFMAKKPLYMIGHSVGPFQNPQFNQLANYVFGHCDALILRESVSLDLMKRSQIDTSKVEHGVDTAWL
VDHHNDDFVASYAVQHWLDVAARQKTVAITLRELAPFDKRLGTTQQAYEKAFAGVVNRILDEGYQVLALS
TCTGIDSYNKDDRMVALNLRKLVNDPSRYHVVMDELNDLEMGKILGACELTVGTRLHSAIISMNFGTPAI
AINYEHKSAGIMQQLGLPEMAIDIRHLLDGSLQAMVADTLGQLPALNARLANAVTAEREKGFQMVKSVLD
RIGEAK
>gnl|CDD|188522 TIGR04007, wcaI, colanic acid biosynthesis glycosyl transferase WcaI. This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species
MKILVYGINYSPELTGIGKYTGEMVEWMARQGHEVRVITAPPYYPQWKVGENYSAWRYRREEGAATVWRC
PLYVPKQPSTLKRLLHLGSFALSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDY
EVDAMLGLGMAGKGKGGKVARLASAFERSGLHNVDNVSTISRSMMNKAQEKGVAAEKVIFFPNWSEVARF
RDVKDADVEALRSQLGLPDDKKIILYSGNIGEKQGLENVIDAAARLTDRPWIFAIVGQGGGKARLEKMAR
ERGLTNVKFFPLQPYEALPALLKMGDCHLVVQKRGAADAVLPSKLTNILAVGGNAVITAEPHTELGQLCI
TYPGIAVCVEPESVDALVAGIVQALAMPKNNTVAREYAERTLEKENVLRQFIADIRG
>gnl|CDD|188523 TIGR04008, WcaF, colanic acid biosynthesis acetyltransferase WcaF. This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species. This acetyltransferase is believed to catalyze the addition of the acetyl group that is attached through an O linkage to the first fucosyl residue of the colanic acid repetitive unit (E unit)
MQDLSGFSVPKGFRGGNAIKVQLWWAVQATLFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPW
KLTLGDYAWVGDDAVLYTLGEITIGAHSVISQKSYLCTGSHDYMSKHFDINATPIVIGEKCWLATDVFVA
PGVTIGDGTVVGARSSVFKSLPANKICRGNPAVVTRERVE
>gnl|CDD|188524 TIGR04009, wcaE, colanic acid biosynthesis glycosyl transferase WcaE. This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species
MLLSVITVAFRNYEGVVKTWRSLRNLARDPSLSFEWIVVDGGSNDGTAEFLEKLNGEFNLRFVSEKDNGI
YDAMNKGIAMAQGRYTLFLNSGDIFHEDVADFVRQLARQKDNAMYIGDALLDFGDGNKIRRSAKPGWYIY
HSLPASHQAIFFPTSGLKKYPYDLQYKVSSDYALAAKLYKSGYPFRRIKGLVSEFSMGGVSTSNNLELCQ
DAKKVQRNILRVPGFWAELSYLLRLKTTGKTKALYNKA
>gnl|CDD|188525 TIGR04010, WcaD, putative colanic acid polymerase WcaD. This membrane protein is believed to function as the colanic acid repeating unit polymerase (in an analagous fashion to wzy proteins in O-antigen polymerization)
MSRSIRICSYLLLPLIYLLVNVKIAQLGESFPITIVTFLPVLLLLFVERISVKKLMIALGIGAGLTAFNY
LFGQSLDASKYVTSTMLFVYIVIIIGMVWSIRFKTISPHNYRKILRFFYLVVGFVVALAAVEMAQIILTG
GSSLMEGISKYLIYSNSYVLNFIKFGGKRTTALYFEPAFFALALISIWLSIKQFGIKTPKTDAMILAGII
LSGSFSGVMTFILFYLLEWAFQYLNKDAIKKKLPLAIISLAVFLVGVVFAFPYIATRLGDLGTEGSSSYY
RIVGPLVMVGYSLTHIDGVVRFGSLYEYVASFGIFNGADVGKTIDNGLYLLIIYFSWFAVLLTLWYMFKV
LKMMLNAFGDNQNFRVQLYLFTPVSLFFTGSIFSPEYAFLIVCPFILRKALNIT
>gnl|CDD|274916 TIGR04011, poly_gGlu_PgsC, poly-gamma-glutamate biosynthesis protein PgsC/CapC. Of four genes commonly found to be involved in biosynthesis and export of poly-gamma-glutamate, pgsB(capB) and pgsC(capC) are found to be involved in the synthesis per se. Members of this family are designated PgsC, covering both cases in which the poly-gamma-glutamate is secreted and those in which it is retained to form capsular material. PgsC binds tightly to PgsB, which has been shown to have poly-gamma-glutamate activity [Cell envelope, Other]
IGIGVILSLVFTEITGISPGGLVVPGYLALFLDQPVLIIVTILISILTYLIVRVISKFTILYGRRKFVAT
IILSILLKTLVHFLFPVYAESFYIFGLAVIGIIVPGLIALTIDRQGVIKTLSSLVILSVLTR
>gnl|CDD|188527 TIGR04012, poly_gGlu_PgsB, poly-gamma-glutamate synthase PgsB/CapB. Of four genes commonly found to be involved in biosynthesis and export of poly-gamma-glutamate, pgsB(capB) and pgsC(capC) are found to be involved in the synthesis per se. Members of this family are designated PgsB, a nomeclature that covers both cases in which the poly-gamma-glutamate is secreted and those in which it is retained to form capsular material.PgsB has been shown to have poly-gamma-glutamate activity by itself but is bound tightly by PgsC (TIGR04011) [Cell envelope, Other]
IFEKIRHDKNLKKIPIRIHVNGTRGKSTVTRLITAGLREGGYKVVGKTTGTDARMIYPDGSEFPIFRPGG
ANIGEQKRVVKKAVKLKADALVLECMAVQPDYQIVFELKLVKANIGVITNVREDHMDVMGPTLDDVAEAF
TATIPYNGDLFTAEDDYLDFFKEAAKDRNTKLIVADAEEISDDILRKFGYIVFPENVALALAVAEALGVD
REIALRGMLNAPPDPGAMKILYLNDKNKRIFFVNAFAANDPVSTERIWDRVCAKGYPTDKPVLIMNCRAD
RVDRTKQFAEDVLPWSPADKLVLIGEGTELFTSVYKKGKIPPNKYLNLENKSTIEIVEMILEESSSALIF
GVGNIHGGGEELVEYI
>gnl|CDD|274917 TIGR04013, Radical_SAM_domain_protein, B12-binding domain/radical SAM domain protein, MJ_1487 family. Members of this family have both a B12 binding homology domain (pfam02310) and a radical SAM domain (pfam04055), and occur only once per genome. Some species with members of this family have a related protein with similar domain architecture. This protein is occurs largely in archaeal methanogens but also in a few bacteria, including Thermotoga maritima and Myxococcus xanthus [Unknown function, Enzymes of unknown specificity]
IVFRYIKKNRYSIAALLAAIESAPAVDTLSPGADLDEIDKPLPGDVVLYSFMSFDADEVLEEVKSLKKKG
YITIAGGPHASADPEETLKLGFDYVVVGEGEETLPELLAALEEGGDPREVPGVAYGEGGKVGRRKRVDLD
AYPPFSERRRLFGPIEITRGCPFGCAYCQTPRIFGRRMRHRSIESIVRYAKRMVDRGRRDIRFITPNAFA
YGSKDGITPNLEKVEELLRSLKKIPGGRIFFGTFPSEVRPEFVTEEALELIKKYCDNRRLHIGAQSGSDR
VLKAIRRGHTVEDVERAVELALEHGFTPVVDFIFGLPGETEEDQEATLELIRKLVKMGAKVHAHYFMPLP
GTPLENAPPGPLSPETRKFLGRLALKGKLTGSW
>gnl|CDD|274918 TIGR04014, B12_SAM_MJ_0865, B12-binding domain/radical SAM domain protein, MJ_0865 family. Members of this family have both a B12 binding homology domain (pfam02310) and a radical SAM domain (pfam04055), and occur only once per genome. This protein occurs so far only in methanogenic archaea. Some species with members of this family have a related protein with similar domain architecture (see TIGR04013) [Unknown function, Enzymes of unknown specificity]
KVTVISPEVYTYGAMLIGGILRDAGHSVILRRSPDPKKSDVVILSLFSTLHLLDPAIREIVRKAREFGGP
VYVGGPVSIVPEMVLGELDVDLVVMGEGEETVPPLLETGEDEGDFEDVPGIAYLEDGEIVVTEPKPPPDL
DHPLPLIPDDIGRQDIRGANVYIETHRGCPGNCTFCQVPRFFGRRIRSRPLEDIVEEVRELKRGGARRFA
ISGGTGSLYGSKKGIDEEAFIELLERLSEVLGRKNVSVPDIRVDLVDDEILEAIREYTIGWVFFGIESGS
DRMLRLMRKGITVDDVCEAVELAREYGVKVAGSFIVGYPGETEDDYEATKDLMEELMLDDVFVSIAEPIP
GTELARLVLELPEDENPVFVPHEGEYRALLLSEAEARAFDLMLHAEMCRSVPRPLTDDLYNTYLEEARKQ
GRDIRAVTRLLRKY
>gnl|CDD|274919 TIGR04015, WcaC, colanic acid biosynthesis glycosyl transferase WcaC. This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species
MNILQFNVRLAEGGAAGVALDLHQRALQKGLTSHFVYGYGKGGKKSVSHDNYPQVIKHTPRLTSIANIAL
FRFFNRDLFGNLDNLYRTITRTPGPVVLHFHVLHSYWLNLAKVVAFCEKVKAHKPDVTLVWTLHDHWSVT
GRCAFTDGCEGWKTGCQKCPTLDNYPPVKIDRAHQLVDGKRQRFRDMLALGCQFISPSQHVADAFNSLYG
AGRCRIINNGIDVATEAILAELPPVPEGQGKPKIAVVAHDLRYDGKTNQRLVRDMMALGDKIELHTFGKF
SPFTGTNVVNHGFETDKRKLMSALNQMDALVFSSRVDNYPLILCEALSIGVPVIATHSEAAQEVLAKSGG
KTVSESEVLQLAQRSKPEIAQAVFGTTLEAFRARSREAYSGQQMLEEYVSFYQNL
>gnl|CDD|188531 TIGR04016, WcaB, colanic acid biosynthesis acetyltransferase WcaB. This gene is one of the acetyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species
MVLAYRIAHFCSVWRKKNVLNNLWAAPVLVLYRLITECLFGYEIQAAATIGRRFTIHHGYAVVINKNVVA
GDDFTIRHGVTIGNRGADSLACPVIGNGVELGANVIILGDITIGNNVTIGAGSVVLDSIPDNALVVGEKA
RVKVIK
>gnl|CDD|274920 TIGR04017, WcaA, colanic acid biosynthesis glycosyl transferase WcaA. This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species
TTDNPLISIYMPTWNRQQLAIRAIKSVLRQDYDNWEMIIVDDCSSSYEQLQQFVEALNDPRVRYTHNDIN
SGACAVRNQAIMQAKGEYITGIDDDDEWTPNRLSVFLAHKHQLVTHAFLYANDYVCEGEVYSQPASLPLY
PKSPYSRRLFYKRNIIGNQVFTWAWRFKECLFDTELKAAQDYDIFLRMVVEYGEPWKVEEATQILHINHG
EMQITSSPKKFSGYFHFYRKHKDKFDRASKKYQLFTLYQIRNKRMTWRTLLTLLSVRNTKRLADGLRGR
>gnl|CDD|188533 TIGR04018, thioredoxin_reductase, putative bacillithiol system oxidoreductase, YpdA family. Members of this protein family, including YpdA from Bacillus subtilis, are apparent oxidoreductases present only in species with an active bacillithiol system. They have been suggested actually to be thiol disulfide oxidoreductases (TDOR), although the evidence is incomplete [Unknown function, Enzymes of unknown specificity]
DVIIIGAGPCGLACAIEAQKAGLSYLIIEKGNLVNSIYRYPTNMTFFSTSERLEIGGIPFISENPKPTRN
EALEYYRRVAERFKLNIRLYEEVLKVKKTDGGFEVTTEKGTYQAKNVIVATGYYDIPNLLNVPGEDLPKV
SHYYKEAHPYFGQKVVVVGGSNSAVDAALELYRKGAEVTMVHRGDEVSSSVKYWVRPDIENRIKEGSIKA
YFNSRVKEITEDSVTLETPDGEVHTIPNDFVFALTGYRPDFEFLESLGVELDEDTGIPVYNPETMETNVP
GLYLAGVIAAGMDTNKIFIENGRFHAPLIAEHIASK
>gnl|CDD|274921 TIGR04019, hypothetical_protein, bacillithiol system protein YtxJ. Members of this protein family, including YtxJ from Bacillus subtilis, occur in species that encode proteins for synthesizing bacillithiol. The protein is described as thioredoxin-like, while another bacillithiol-associated protein, YpdA (TIGR04018), is described as thioredoxin reductase-like [Unknown function, Enzymes of unknown specificity]
KKLTTEEQLDEIKEESKEKPVLIFKHSTTCPISAMALREFERFADESPEQVPVYYLDLIEYRPVSNEIAE
TFGVKHESPQVIVIKNGEVVWHASHWDITADALKE
>gnl|CDD|274922 TIGR04020, non-ribosomal_peptide_synthetase, natural product biosynthesis luciferase-like monooxygenase domain. This model describes a subfamily within the bacterial luciferase-like monooxygenase (LLM) family that regularly occurs within large non-ribosomal protein synthases/polyketide synthases, but also as small proteins. The LLM family includes members that bind either FMN or F420, and FMN is more likely in this case because many members are from species that lack F420 biosynthesis capability. An example member is the MupA protein of mupirocin biosynthesis in Pseudomonas fluorescens NCIMB 10586
FSLFYFAGDEDASRGDKYRLLLEGARFADANGFSAVWTPERHFHAFGGLYPNPSVLSAALAAVTKRIQLR
AGSVVLPLHHPIRVAEEWSVVDNLSGGRVGLSFASGWHPNDFVLAPENYEDRREVMFEGIDTVRRLWRGE
TVTFPGGGGREVEVKTLPRPVQPELPVWLTAAGNPETFREAGRLGANVLTHLLGQTLEELAQKIALYREA
LAEAGHDPGSGHVTLMLHTFVGEDMAEVREAVRAPFCDYLRSSVDLFAGLAASLGLDIDLDSLSEDDLDA
LLEHAFERYFETSGLFGTPESCLEMVERLQAAGVDEIACLIDFGVDPDLVLESLPYLARLR
>gnl|CDD|274923 TIGR04021, LLM_DMSO2_sfnG, dimethyl sulfone monooxygenase SfnG. This family of FMNH2-dependent members of the luciferase-like monooxygenase (LLM) family includes SfnG, a monooxygenase that converts dimethylsulphone (DMSO2) to methanesulphonate. This step can be followed immediately by methanesulfonate sulfonatase (an alkanesulfonate monooxygenase - see TIGR03565) for the FMNH2-dependent conversion an inorganic form [Central intermediary metabolism, Sulfur metabolism]
LKFAYWVPNVSGGLVVSTIEQRTDWDYDYNLKLAQTAEEVGFEYALSQIRFFASYGADKQHESTSFSLAL
LAATEKLKVIAAVHPGLWHPGVLAKFIATADHISNGRFAVNIVSGWFKGEFTGFGEPWLEHDERYRRSEE
FIRVLKGIWTEDRFTFRGDFYRINDFTLKPKPVQKPHPEIFQGGNSTAARRMAGRVSDWYFMNGNSLEGL
REQIDDVRALARENGREVKFGLNAFVIVRDTEKEARETLREIIAKADKEAVEGFGAAVKQAGNSSPEGEG
MWADSSFEDLVQYNDGFRTGLIGTPEQIAERILELKAIGVDLILTGFLHFQEELEAFGEEVIPLVRELEA
>gnl|CDD|274924 TIGR04022, Acyl-CoA_dehydrogenase_type_2_domain, sulfur acquisition oxidoreductase, SfnB family. Members of this protein family belong to the greater family of acyl-CoA dehydrogenases. This family includes the sulfate starvation induced protein SfnB of Pseudomonas putida strain DS1, which is both encoded nearby to and phylogenetically closely correlated with the dimethyl sulphone monooxygenase SfnG. This family shows considerable sequence similarity to the Rhodococcus dibenzothiophene desulfurization enzyme DszC, although that enzyme falls outside of the scope of this family [Central intermediary metabolism, Sulfur metabolism]
AHIIASDAEALEIARRLAAEFAPGAAERDRERRLPWAELDAFSQSGLWGITVPRAYGGAGVSYATLAEVI
AIISAADPSLGQIPQNHFYALEVLRLTGSEEQKRFFFGEVLAGERFGNAFSERGTRNVLDFQTRLRRDGD
GYRLNGRKFYSTGALFAHWIPVLALDDEGRAVLAFVPRDAPGLTVIDDWSGFGQRTTASGTVLLDDVRVP
AEHVVPIQRAFDRPTAAGPVAQIIHAAIDAGIARAALADTLAFVRERARPWIDSGVERASDDPLTIAEVG
DLAIRLHAAEALLERAGRAVDAARAEPTEESVAAASIAVAEAKVLTTEIALLAASKLFELAGTRSTLAEH
NLDRHWRNARTHTLHDPVRWKYHAIGNYYLNGVNPPRHGWL
>gnl|CDD|274925 TIGR04023, Pyridoxamine_5'-phosphate_oxidase, PPOX class F420-dependent enzyme, MSMEG_5819/OxyR family. A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomycetales, make F420. This subfamily within the PPOX family occurs in at least 19 distinct species of F420 producers and is likely to bind F420 rather than FMN. The member OxyR was shown to use F420 to catalyze a C5a-C11a reduction in oxytetracycline biosynthesis [Unknown function, Enzymes of unknown specificity]
FTEEELAYLASQRLGRLATVDPDGQPQVVPVGFEYDGTLGTIDIGGYNMSATRKFRNVAANGKVALVVDD
LASTDPWRVRGIEIRGTAEALTDGGPPGPGPYIRIHPRRIWSWGL
>gnl|CDD|188539 TIGR04024, 510-methylenetetrahydromethanopterin_reductase, coenzyme F420-dependent oxidoreductase, NP1902A family. This subfamily of the luciferase-like monooxygenases is restricted to the order Halobacteriales. SIMBAL analysis strongly suggests this oxidoreductase binds coenzyme F420 rather than FMN. Occasional annotations of members of this family as N5,N10-methylenetetrahydromethanopterin reductase appear to represent overly aggressive transfer of annotation [Unknown function, Enzymes of unknown specificity]
ERDVHLPVAAQDSLDDVVDRAQRAEELGYDRAWLPETWGRDAVTTLTAIADRTDDIGLGNSIVSPYSRSP
ALLGQTAATLQEASDGRFRLGLGPSGPAVIEGWHGAEFERPLRRTRETIDIVRQVLAGEEVDYDGDYFDL
PGFRLRCDVPDPSPPVDVAGMGPKAVELAGRFADGWHPQLFTADGLRDRLEDLRRGAELGDRDLDDLRVT
LIVRCCALEDAERARDLARQHTAFYVGGMGPFYRDSLARQGYEAVASEIHDAWQDGDRERAAAAVTDDLL
DDLAAAGTPADVREWVERYAAIDGVDAVRVSFPRGADEDEIVQTMEALAP
>gnl|CDD|274926 TIGR04025, hypothetical_protein, PPOX class probable FMN-dependent enzyme, DR_2398 family. Members of the PPOX family (see pfam01243) may contain either FMN or F420 as cofactor. This subfamily consists of proteins mostly from species that lack the capability to synthesize F420, and therefore most likely all bind FMN
EELRALYGAPSERALNKVLDRLDPHYRAFIEASPFCVLATVGPDGNLDVSPRGDPPGFVRVLDDRTLLIP
DRPGNNRIDSLRNILRDPRVGLLFLVPGVGETLRVNGTARISTDPDLLARFAVNGKRPRSVLVVTVEEVY
FHCAKALMRSGLWDPETWVDRSALPSLGQILKDQTKGGFDGEAYDRALPERYRKTLY
>gnl|CDD|274927 TIGR04026, hypothetical_protein, PPOX class probable FMN-dependent enzyme, alr4036 family. Members of the PPOX family (see pfam01243) may contain either FMN or F420 as cofactor. This subfamily described here is widespread in Cyanobacteria and plants, and is named for alr4036 from Nostoc sp. PCC 7120. The family consists mostly of proteins from species that lack the capability to synthesize F420, so it is probable that all members bind FMN rather than F420 [Unknown function, Enzymes of unknown specificity]
LPPWRPLLKRALHRERRLPSSRWLQLATVTSDGTPRNRTVVFRGWEDSNQLELITDSRSEKIEQLAQNPA
AEICWYFPKTREQFRLRGKATLVTADDSPERLQAHWQQLSDAARAQWFWPHPGQPLEPSAAFPEELPDPA
PPPEHFVLLLLEIQSVDHLELRGHPHNRRRWIRDENGWKEQRLNP
>gnl|CDD|274928 TIGR04027, Luciferase-like_monooxygenase, putative FMN-dependent luciferase-like monooxygenase, KPN_01858 family. This protein family consists of luciferase-like monooxygenases (LLM), and include KPN_01858 from Klebsiella pneumoniae as a representative member. Most are from species that lack F420 biosynthesis, so the family is likely to bind FMN as its cofactor. This family is closely associated with a binding protein-dependent ABC transporter, suggesting a role in catabolism [Unknown function, Enzymes of unknown specificity]
KRLGFFTRLLDDVPAAERYRLATEQIQHAERLGFDSAWVAQHHFHEDEGGLPSPFVFLAHVAARTSRIRL
GTGVITLPMEDPLRVAEDAAVLDLLSDGRLEVGLGSGGTPSSFAAFGLDSAQRGEIFADHLAVLRDALAG
RPLRGGDNRLYPAAPQLAERVWQATFSVEGGARAGRAGDGLMLSRTQPRPAGAPDAPLDELQNPIIDAYL
AALPAGRAPRILASRTAFVADDRARALRLAEIGLRRVAARFAASGHRIGGDSLEDLIRAFDVHVGTPDEV
IASLAADTALARATDLVFQVHSIDPPHALILRSIELIATEVAPALG
>gnl|CDD|274929 TIGR04028, extracellular_solute-binding_protein_family, ABC transporter substrate binding protein, KPN_01854 family. Members of this protein family are ABC transporter substrate-binding proteins related to KPN_01854 from Klebsiella pneumoniae, and occur in both Gram-positive and Gram-negative species. This transport protein family is closely associated with a putative FMN-dependent luciferase-like monooxygenase of unknown function (TIGR04027), as well as with the other proteins of its transporter complex [Transport and binding proteins, Unknown substrate]
TLTYLEPQAHTNLYPPAGGFYPNGGVLNQITDRLLYQNPETLELEPWIAESWPEVNADATEYTFKIRKGV
TYSDGTPLDAENVAKNFDLYGLGDKDRKLTVSEVINNYDRSEVVDPLTVKFYFSKPSPGFLQGTSVINSG
LVSLATLALPFEGFGPGNATKIIGSGPFVVESEELGTELVLKAREDYDWAPPSRAHQGRAYLDGIKYIVA
AEDSVRVGALLAGQADLARQIEAPDEKQVEDQGFAIYAAPTRGVNNSFAFRFDNPLLADIRVRQALIHAT
DRKEIVDTLFSDSYPLATSVLASTALGYVDLSDKYTFDPEKAAALLDEAGWKPGPDGIRQKDGQRLALTF
NEALPQPRNKEVLTLVQQQLAKVGVKLNVLAGDQAAQTADSLDPDKTQVYHSMVGRADPDVLKSQYYPTN
RNALLNKGGDSDKVKFGDEKLNALLEAIASEPDEEKRLAASGAVQDYLTDQAYVLPIFEEPQVFAGAPYV
KGFAFEAVGRPSFYGTWLD
>gnl|CDD|213885 TIGR04029, CMD_Avi_7170, CMD domain protein, Avi_7170 family. Sequences in this family occur as the N-terminal domain of a fusion protein with a C-terminal peroxidase-like protein, or as discrete protein encoded next to a peroxidase-like protein. The two partners regularly are encoded near to, and in the same genomes as, a putative FMN-dependent luciferase-like monooxygenase (LLM) (TIGR04027), and an ABC transporter in which TIGR04028 models the substrate-binding protein. CDD identifies this family as falling within the CMD superfamily that includes carboxymuconolactone decarboxylase
DLLDTLAEIAPDSPLAQARATRPAATDNAQRSYEALFEPADAGDFSLAERYAVATFVAGLHQDEALAAFY
ADLLQDEAAPLVAAIRAAIRRGASTGPYSVPGFLWRPDAAALGPRLAAALDHAHLLVFHPRDAAPQALGA
LTAAGWSADDIVTLSQLVAFLSFQSRLLRGLRVL
>gnl|CDD|188545 TIGR04030, perox_Avi_7169, alkylhydroperoxidase domain protein, Avi_7169 family. Members of this family represent a narrow clade that falls within a family of alkylhydroperoxidase-related proteins, fused to or adjacent to a sequence described by TIGR04029. These two partners occur almost always in the context of a putative FMN-dependent luciferase-like monooxygenase (LLM) (TIGR04027), and an ABC transporter in which TIGR04028 models the substrate-binding protein
APDAFTQDELGWEPWIAPKPLAEFTEEEQAALIRPGRADSPYFRLLARDPPALEARTLTDLDIFYNPGGG
LPRAERELAATVTSRYNGCIYCASVHARKASQLSKRRDDVQRLLDVGPGADLGSERWQAIIDAAAALSAT
PAAFNAAHVAALRAQGLDDLAIVDLIQSAAFFNWANRLMLTLGEP
>gnl|CDD|188546 TIGR04031, Htur_1727_fam, rSAM-partnered protein, Htur_1727 family. Members of this protein family show homology to the putative PaaH (or PaaB) subunit of the phenylacetate-CoA oxygenase complex. However, all members are found in the Halobacteriales in the vicinity of a radical SAM protein homologous to the PqqE protein of pyroquinoline quinone (PQQ) biosynthesis. Members are well-conserved to about residue 75, but then become low-complexity and hypervariable
ERRRIVDEPRAATGREWELFVREDSEDPLTHVGSVSAPSADIAREQACSLFAWYAEDLWVCPADDVTRYT
T
>gnl|CDD|274930 TIGR04032, conserved_hypothetical_protein, antimicrobial peptide, SdpC family. This protein family contains the antimicrobial peptide SdpC, used in cannibalistic killing by Bacillus subtilis, and related sequences in species as distant as Myxococcus xanthus from the Deltaproteobacteria. A conserved gene neighborhood includes proteins associated with immunity
AAANKAYSGEEIFKGLVFGQGPAAKKLPELWQKNLIKAYNNSPEAKELANDLIAKIKKKDPAYFDRLKEA
VYSGDPLKVDELLTKGGELLQEAAAESTIALSKDGTVPGDANAVAVVAVAAGLYVVVVAAVAVATVALAA
AAVVPAVDSWPVTENPSKLDRDNLVAELAKKL
>gnl|CDD|274931 TIGR04033, conserved_hypothetical_protein, antimicrobial peptide system protein, SdpB family. Members of this protein family resemble SdpB (Sporulation Delaying Protein B), an integral membrane protein associated with production of the cannibalism peptide SdpC in Bacillus subtilis. Similar proteins are found in Myxococcus xanthus
LIYSVDPWSNAYWLGRLLLAVATLSILLFTSTAHLFAQVGKAAPGPVCEGFTHFSIFCVIPEYNFEHVRW
AKALILLAVVSGWRPRITGLLHWYATYSLSLSASLPDGGEQIALLLAFLLLPASLSDDRRWHWKPSSERK
QVYAVKDGVAAAAIIMLRVQVAYIYLDATVAKFKIAEWANGTASYYVVNDPMFGDPGPLASLMSPLLGSP
LVLLLTWGVLVLELILALGILGNARLRRIALFLGILFHAGIIIFIGLFSFSLVMIAALIAALTPVE
>gnl|CDD|274932 TIGR04034, YitP_like_protein, antimicrobial peptide system protein, SdpA family. Members of this protein family resemble SdpA (Sporulation Delaying Protein A), a protein associated with production and export of the cannibalism peptide SdpC in Bacillus subtilis. Similar proteins are found in Myxococcus xanthus, Stigmatella aurantiaca DW4/3-1, Streptomyces sp. ACTE, etc
YNVVGLLPQNPINLFFSKQFFFFTLLPQGWAFFTKDPRDENIFVYSAENNYSSLLWTPNNKRENLFGISR
DGRAQGVELGRLAAEIPNSAWVKCKEDETSCLEKALRPQKTIKNTAPRPLLCGKYIIGLQVPVPWSWSNL
VQDPNSLTRKVLKVVI
>gnl|CDD|274933 TIGR04035, glucan_65_rpt, glucan-binding repeat. This model describes a region of about 63 amino acids that is composed of three repeats of a more broadly distributed family of shorter repeats modeled by pfam01473. While the shorter repeats are often associated with choline binding (and therefore with cell wall binding), the longer repeat described here represents a subgroup of repeat sequences associated with glucan binding, as found in a number glycosylhydrolases. Shah, et al. describe a repeat consensus, WYYFDANGKAVTGAQTINGQTLYFDQDGKQVKG, that corresponds to half of the repeat as modeled here and one and a half copies of the repeat as modeled by pfam01473
YYFDADGKAVTGAQTIDGVTYYFDENGKQVKGDFVTNGGGTYYYDKDSGALVTNRFVTIKDG
>gnl|CDD|274934 TIGR04036, family_protein, putative luciferase-like monooxygenase, FMN-dependent, CE1758 family. This tightly conserved subfamily of the bacterial luciferase-like monooxygenase (LLM) family, with members showing _ 60 % pairwise sequence identity, includes proteins from both species with and species without the ability to make coenzyme F420. Therefore, the like cofactor is FMN rather than F420. The presence of three members in Kineococcus radiotolerans SRS30216 and two in Saccharopolyspora erythraea NRRL 2338 suggest closely related (subfamily) rather than exactly conserved (equivalog) function. Gene neighborhoods around members are not conserved [Unknown function, Enzymes of unknown specificity]
MQFGIFTVGDVTTDPTTGRTPTEHERIKAMVEIALKAEEVGLDVFATGEHHNPPFVPSSPTTLLAYIAAQ
TSRLILSTATTLITTNDPVRIAEDYAMLQHLADGRVDLMLGRGNTGPVYPWFGKDIRQGIPLAIENYALL
RRLWREDVVDWEGQFRTPLQGFTSTPRPLDGVPPFVWHGSIRSPEIAEQAAYYGDGFFHNNIFWPKEHTQ
QMVALYRQRFEHYGHGTADQAIVGLGGQVFMRRNSQDAVREFRPYFDNAPVYGHGPSLEEFTRQTPLTVG
SPQQVIERTLTFREYVGDYQRQLFLIDHAGLPLKTVLEQLDLLGTEVVPVLRREFAARRPAGVPDAPTHA
SRVAA
>gnl|CDD|274935 TIGR04037, predicted_flavoprotein, LLM-partnered FMN reductase, CE1759 family. This family represents a distinct clade within pfam03358. That family includes enzymes such as the NADH-dependent FMN reductase MsuE. Members of the present family regularly co-occur in genomes, typically as gene pairs, with members of TIGR04036, a probable FMN-dependent member of the bacterial luciferase-like monooxygenase (LLM) family. At least one member, RF|YP_001509627.1 from Frankia sp. EAN1pec, is fused to the LLM protein. The function of these gene pairs is unknown
LVVVSAGLSTPSSTRLLADRLAEATEAALGARGEEVEVTVIELRELAHDLANAMVTGFPSPALRAALDAV
AGADGLIAVTPVFSASYSGLFKSFFDVLDPDALTGKPVLIAATGGTPRHSLVLDHAMRPLFSYLRAVVVP
TGVFAATEDWGGGEGAGLPRRIERAAGELADLIVPAPRRRPAGADPFADFLPFEQLLR
>gnl|CDD|274936 TIGR04038, hypothetical_protein_MED92_00180, radical SAM protein, TatD family-associated. Members of this family are radical SAM proteins found in about 5 percent of microbial genomes. A portion occur as gene fusions with, or adjacent to, members of the TatD family of hydrolases (pfam01026). The TatD family may have several paralogs per genome, including TatD itself from E. coli (a soluble protein not actually part of the twin-arginine translocation complex), which appears to act in quality control for TAT, directing turnover of misfolded TAT substrates. The functions of TatD family hydrolases in general (other than TatD itself, which may be exceptional within its larger family), and of this radical SAM domain protein modeled here, are unknown
TIAYVIRNSLYLNITNRCTLRCQFCPKHRDFQVKGYDLWLDKEPSAEEVIAAIGDPKKYDEVVFCGYGEP
LLRLDVVKEVAKWIKEQGGKVRINTDGLANLFHGRNILPELAGLVDALSISLNAQDAETYQRICRPPFGN
AYEAVIEFIKEAKKYIPEVIVSAVNLPGVDIKACEKIAESLGVKFRVREYD
>gnl|CDD|188554 TIGR04039, MXAN_0977_Heme2, di-heme enzyme, MXAN_0977 family. This model describes a subfamily of di-heme proteins related to the di-heme cytochrome c peroxidase and to MauG (methylamine utilization G), an enzyme that performs a tryptophan tryptophylquinone modification to the methylamine dehydrogenase light chain
VPADNPMTEEKVELGRHLFYDKRLSGNGTQSCASCHIQSLAFTDGLATPVGSTGERHPRNSQSLVNVAYN
ATLTWANPGLTTLEDQALVPLFGEHPVELGLTGAEEEVLARLQSDPIYPTLFAAAFPEAEEPISVDNVVK
ALASFVRSLISGNSPYDRYAYRGNDSALSEQAKRGLALFFSERLECFHCHGGFNFSDSTVHEGTAQEEFP
FHNTGLYNIDGKGAYPEPDRGLYELTGKAADKGRFRAPSLRNIAVTAPYMHDGSIATLEEVIDHYAAGGR
NITTGPFAGDGRASPLKSGFIRGFTLTADEKADLVAFLESLTDEEFLSNPKFSDPF
>gnl|CDD|274937 TIGR04040, glycyl_YjjI, glycine radical enzyme, YjjI family. Members of this family are homologs to enzymes known to undergo activation by a radical SAM protein to create an active site glycyl radical. This family appears to be activated by the YjjW radical SAM protein, usually encoded by an adjacent gene [Unknown function, Enzymes of unknown specificity]
NRILEIIKDPNLTYKQKRHFLALEAENSLDYPNISDEVQEALDQGIICDLFEGNAPYRPRYILPDYAKFL
EKGSEFLELEPPKDLDEALNALLILYHHVPSITSYPVYLGQLDELLEPFVEGLDEEEAYRKIKLFLIHID
RTLPDSFCHANIGPKDTRAGRLILRADRELKQAAPNLTLKYDPEITPDDFARLAVKTALECSKPSFANYP
MHVKDFGDKAYGIVSCYNSLPIGGGAYTLVRLNLKEVAKKAESVEDFLDNVLPHYVKLMAELIDARIRFL
VEESNFFESSFLVKEGLIDEDRFTPMFGIYGLAEAVNHLLGAEGLNERFGHSEEANELGLKISDKLKEIV
ENHPVKYCEGTGGRALLHAQVGISSDKGVTPGCRIPYGEEPDLPTHLKQSAPFHKYFPSGISDIFTFDET
AKDNPEAVVDIIKGAFKEGMRYFTANVSDSDLIRVTGYLVKKSDVEKFEKGEGVRRNTTWLGAGAAKNTN
ILERKPR
>gnl|CDD|274938 TIGR04041, glycine_radical_enzyme_activase_YjjW_family, glycine radical enzyme activase, YjjW family. Members of this family are radical SAM enzymes, designated YjjW in E. coli, that are paired with and appear to activate a glycyl radical enzyme of unknown function, designated YjjI. This activase and its target are found in Clostridial species as well as E. coli and cousins. Members of this family may be misannotated as pyruvate formate lyase activating enzyme [Protein fate, Protein modification and repair]
KALVNKIIPFSCVDGPGNRLAIFLQGCNFDCKYCHNPETINHCDHCGDCVAGCPAGALSLVDGKVVWDKE
RCIGCDTCIKVCPHQSSPKTKEYTVEELLDRIRKNMPFIRGITVSGGECTLQLDFLTELFKAIKAAGLTC
FIDSNGSLDLTGWPKLLPVLDGAMLDLKAWDSETHRWLTGRDNHRVLKNIRFLAELGKLYEVRLVHIPGL
SDLEQEIDGLARFLGDLPSDTRIKLIAFRHHGVRGEALEWPSPTDEQMEELAEALIKRGFRDIILP
>gnl|CDD|274939 TIGR04042, conserved_hypothetical_protein, MSMEG_0570 family protein. This small protein, about 90 residues long, has no detectable homologs outside the set used to characterize this model. Member proteins serve as markers for an eight-gene region whose overall function is unknown. One member of the cluster is a radical SAM protein with some similarity to enzymes of cofactor biosynthesis, another a glycosyltransferase, several hydrolases or oxidoreductases, and several unknown
PEMHFTVRWPDGSEQQCYSPSTVVKDYLTPGESYPVADFVERSREALTEASERVRAKYGFACSSAMDQLA
RIEQAAARFAGDPDAKVRVL
>gnl|CDD|274940 TIGR04043, hypothetical_protein_WH5701_02349, radical SAM protein, MSMEG_0568 family. Members of this protein family are radical SAM proteins related to MSMEG_0568 from Mycobacterium smegmatis. Members occur within 8-gene operons in species as diverse as M. smegmatis, Rhizobium leguminosarum, Synechococcus elongatus, and Sorangium cellulosum. The function of the operon is unknown, but similarity of MSMEG_0568 to some cofactor biosynthesis radical SAM proteins suggests a similar biosynthetic function [Unknown function, Enzymes of unknown specificity]
TDLQSNGLRLVDPVAGNPGRRGGAGPSDHKAVTIDGLTVMVPVYTAAAQDSPYLVEPPDADGQSRLLRDG
TPVGTVEFPRRPRFYDLKTADGIPYSKIALLHGRDVLATTVLQTCIRYRDRARSCQFCAIEQSLAAGRTI
ARKTPEQLAEVAEAAVRLDGVKQMVMTTGTPNTTDRGARILAECARAVKAAVDLPIQVQCEPPDDLAWFT
RLKAAGADSLGMHLEAVDPEVRRRIMPGKATVPLERYFAAFEAAVRVFGRGQVSTYLLAGLGDSPDELVA
GAERLIDMGVYPFVVPFVPISGTPLEGHPAPSPAFMADVYQPVAKMLRAAGMSSADIKAGCAKCGACSAL
STFE
>gnl|CDD|188559 TIGR04044, MSMEG_0572_fam, MSMEG_0572 family protein. This model describes a family of proteins with remote similarity to the DsrE/DsrF-like family (see pfam02635). All members are found in a context of at least seven genes that includes a radical SAM protein, suggesting biosynthesis. The system is sparsely but broadly distributed in bacteria, including Actinobacteria, Proteobacteria, and Cyanobacteria
PEVPHPAHPKGDFLVDYEEKVFPDVQAEDGEKALTTFHTVAFEGSIGFVNILQATRLLRKGFETSILLYG
PGVNLGVQRGFPTLGDEAFPGHQNINDQLKKFMKEGGKVYACRFALQALYGHGEESLIEGIRPINPLDVQ
DLILLHAKEGAIINDTWTV
>gnl|CDD|274941 TIGR04045, acetyltransferase_GNAT_family_protein, putative N-acetyltransferase, MSMEG_0567 N-terminal domain family. Members of this family belong to the GNAT family (pfam00583), in which numerous characterized examples, though not all, are are shown to be N-acetyltransferases or to interact with acetyl-CoA. This family occurs in a sparsely distributed biosynthetic cluster that occurs in Actinobacteria, Cyanobacteria, and Proteobacteria
EFRVKLAESPWERRGYYALRRAVFCEEQGIFAGDDRDEIDAHAYPIVALSTEGGAPDRVVGTVRIHEEEP
GLWYGGRLAVHAAFRRQGRIGKGLIRLAVSTAHALGCRRFLATVQSQNVPFFRRLHWQSLDELEIHGRPH
HLMEADLAHYPPC
>gnl|CDD|274942 TIGR04046, predicted_flavoprotein_involved_in_K+_transport, flavin-dependent oxidoreductase, MSMEG_0569 family. Members of this protein family belong to a conserved seven-gene biosynthetic cluster found sparsely in Cyanobacteria, Proteobacteria, and Actinobacteria. Distant homologies to characterized proteins suggest that members are enzymes dependent on a flavinoid cofactor
YPVVIIGAGQAGLSVSYYLKQAGIDHVVLEKHTVAHSWRDERWDSFCLVTPNWQCRLPGHPYDGTDPDGF
MVKDEIVAYLDGYARSFNPPVREGTEVTSLRKHGAGGFRVSTSAGAFTADQVVIATGGYHVPVIPPLAER
LPADVLQLHSSEYRNPDQLPDGAVLVVGSGQSGCQIAEDLHLAGRKVHLAVGSAPRCARFYRGRDVVDWL
DDMGYYDLPVDEHPDPESVRDKTNHYVTGRDGGRDIDLRRFALEGMQLYGRLEDIREGQLRFAPDLKANL
DGADAVYNRINASIDAYIAKNGIEAPPESPYQPVWEPEEEPTELDLAAAGITSVIWCTGFRPDYSWVDLP
VFDGAGYPVHDRGVTAVPGLYFLGLPWLHTWGSGRFSGIARDAAYLADQI
>gnl|CDD|274943 TIGR04047, MSMEG_0565_glyc, glycosyltransferase, MSMEG_0565 family. A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster [Unknown function, Enzymes of unknown specificity]
RIALLTYSTKPRGGVVHTLELAEALTALGHDVTVWALAADGFGFFRDPPCAVRLVPVAPAPGDTDAMVEQ
RIARSIDHLRAHFARGFDVVHAQDCISGNALATLRAEGLIPGFVRTVHHLDDFDDPRLAACQERAIVEAD
AVLCVSAAWAAELRAEWGIDATVVPNGVDAARFSPAADAADAALRRRLGLRGGPYVLAVGGIEPRKNTID
LLEAFALLRARRPQAQLVIAGGATLFDYDAYRREFRARAAELGVDPGPVVITGPVPDADLPALYRCADAF
AFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYLGRFDAAWADPSDPDSIADALALALDPARRPALRAA
GPELAARYTWDASARAHLEFYRR
>gnl|CDD|188563 TIGR04048, nitrilase_sll0784_family, putative nitrilase, sll0784 family. This family represents a subfamily of a C-N bond-cleaving hydrolases (see pfam00795). Members occur as part of a cluster of genes in a probable biosynthetic cluster that contains a radical SAM protein, an N-acetyltransferase, a flavoprotein, several proteins of unknown function, and usually a glycosyltransferase. Members are closely related to a characterized aliphatic nitrilase from Rhodopseudomonas rhodochrous J1, for which an active site Cys was found at position 165 [Unknown function, Enzymes of unknown specificity]
RIVRAAAVQISPVLFSLEGTLAKVLEAIAEAAGKGVQLIVFPETFVPYYPYFSFVQPPVLMGKEHLRLYE
QAVVVPGPVTDAVAEAAREHGMVVVLGVNERDHGSLYNTQLIFDADGELVLKRRKITPTYHERMVWGQGD
GAGLKVVDTAVGRVGALACWEHYNPLARYALMAQHEEIHCAQFPGSLVGPIFADQMEVTIRHHALESGCF
VVNATGWLTPEQIAQITPDEGLHKALSGGCHTAIISPEGKHLAGPLTEGEGMAIADLDFSLITKRKRMMD
SVGHYSRPELLSLLIDRRPAR
>gnl|CDD|188564 TIGR04049, AIR_rel_sll0787, AIR synthase-related protein, sll0787 family. Members of this family include sll0787 from Synechocystis sp. PCC 6803 and resemble the C-terminal region of MSMEG_0567 from Mycobacterium smegmatis, where the N-terminal is a GNAT family N-acetyltransferase. The conserved cluster is found broadly (Cyanobacteria, Proteobacteria, Actinobacteria) in about 8 percent of genomes and appears to be biosynthetic. The product is unkown [Unknown function, Enzymes of unknown specificity]
LDDLAEALRATPGIAHKRDIQLAAAQLGAAAPDPLLGLAAALGDDCAAIPDGDGYLLLAIEGMLPDFVAT
DPWFAGWSGVMVNISDIAAMGGRPIAVVDALWSAGSAQAQQLLEGMQAASAAFGVPIVGGHTNIRSPYGQ
LSVAILGRARRLLSSFDARPGDRLLMAIDLRGQFRENYPFWDAATGAPPERLRADLALLPQLAEAGLVDA
AKDISMGGILGTALMLLECSGVGADLDLDAIPRPPGVDLDRWLTSFPSFGFLLAVRPADVDAVAQRFAAR
GLACAAIGEITAGGQVVLKDGGESALFWDLQQQPLT
>gnl|CDD|274944 TIGR04050, MSMEG_0567_Cter, AIR synthase-related protein, MSMEG_0567 C-terminal family. Members of this family include the C-terminal region of MSMEG_0567 from Mycobacterium smegmatis, where the N-terminal is a GNAT family N-acetyltransferase, and resemble the full length of sll0787 from Synechocystis sp. PCC 6803. The conserved cluster that contains these is found broadly (Cyanobacteria, Proteobacteria, Actinobacteria) in about 8 percent of genomes and appears to be biosynthetic. The product is unkown [Unknown function, Enzymes of unknown specificity]
VARLVAATKAPLGAVLAPLRTVGDALGGAGFVGDDGAPVPGSDLVAACDAIIPSMVERDPEWAGWCGVLV
NINDLAAMGATPVGLLDAVAAPTASHLARVLGGLRAAATAWGVPVLGGHTQLGVPAALSVTALGRTADPV
PAGGGRAGDAVRLTADLGGGWRPGYTGRQWDSTSSRRTAELAAMASFVARTRPAAAKDVSMAGIAGTLGM
LAEASGCGAELDVAAVPRPASATMGDWLTCFPGFGMLTADRAGRAVAPAGPATSAVCGRLTAGPGVRLRW
PDGVTTRALPGTVTGL
>gnl|CDD|188566 TIGR04051, rSAM_NirJ, heme d1 biosynthesis radical SAM protein NirJ. Heme d1 occurs in the cytochrome cd1 subunit of nitrite reductase in species such as Pseudomonas stutzeri. NirJ is a radical SAM protein involved in its bioynthesis. In a number of species, distinct genes NirJ1 and NirJ2 are found in similar genomic regions; this model describe authentic NirJ from genomes with NirJ only [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
GPVVIWNLIRRCNLTCKHCYSTSADIDFPGELSTAEVLRVIDDLKAFGVPALILSGGEPLLRPDIFEIAA
RARQLGFYVALSTNGTLIDEGNIARIAAAGFDYVGISIDGLEATHDRFRRLKGAFDAALAGIRLCKAAGI
KVGLRFTLTEDNAAQLPALLDLMEEEGVDKFYLSHLNYAGRGNRNRGEDAHHQRTRDAMDLLFDRAWQDA
QQGRETDFVTGNNDADGVYLLQWAKRRFPEQLAHLRARLAAWGGNASGVGVANIDNLGEVHPDTYWWHHT
VGNVRERPFSDIWTDTSDPLMAGLRQRPRPLKGRCGACAYLAICNGNTRVRAFQLTGDPWAEDPGCYLSD
AEIG
>gnl|CDD|188567 TIGR04052, hypothetical_protein_MettrDRAFT_3899, AZL_007920/MXAN_0976 family protein. Members of this rare protein family regularly occur next to a member of the MXAN_0977 subfamily (TIGR04039) of the di-heme cytochrome c peroxidase/MauG family (pfam03150). MauG itself (TIGR03791) is a protein modification enzyme responsible for the tryptophan tryptophylquinone (TTQ) modification involved in methylamine dehydrogenase activation. All members of this family have a motif of four spaced invariant Cys residues, while additional homologs outside the scope of this family lack the four Cys residues
FRFYVSDVALIDADGQEVPLTLDQDGKWQSAGVALLDFEDKSGGCTNGTTATNLVVSGTVPAGNYQGLQF
TVGVPEELNHLDPLLAPSPLNDSGMFWSWQQGYKFLRIDVSPNASVGKSTGWVVHLGSTGCAGSPARGES
SACTNPNRLPVTLPGFDPNSQKVELDLAALFEGSNLGANPGGAVGCMSGYADPDCPAIFRQLGLNL
>gnl|CDD|274945 TIGR04053, sam_11, radical SAM protein, BA_1875 family. Members of this subfamily of the radical SAM domain superfamily show closer sequence relationships to peptide-modifying proteins of bacteriocin and PQQ biosynthesis than to other characterized radical SAM proteins. Within this subfamily, targets are likely to be diverse [Unknown function, Enzymes of unknown specificity]
HDFNERPLIVIWEVTRACALACKHCRASAQPKPLPGELTTEEGKALLDQIAEFGDPYPLLVLTGGDPLMR
PDLFELVDYATSLGLRVSLSPSVTPNLTREAIAALKEAGVSAVSLSLDGATAETHDAFRGVPGSFDRTVN
AIRAALELGIPVQINTTVTAENVHELPDVAKLLKDLGVKLWSVFFLVPTGRGQALDDLTPEEAEDVLHWL
YDVSDRYGFDVKTTEAPHYRRVALQRKGLEKDELRGGELYRQLTEKLTELLGEPVGRPPRRPMGTRDGNG
FIFVSHTGDVYPSGFLPLSAGNVREESLVEIYRESPLFKSLRDPDEFKGKCGRCEFRHVCGGSRARAYAV
TGDPLAEDPACVYRP
>gnl|CDD|274946 TIGR04054, rSAM_NirJ1, putative heme d1 biosynthesis radical SAM protein NirJ1. Members of this radical SAM protein subfamily, designated NirJ1, occur in genomic contexts with a paralog NirJ2 and with other nitrite reductase operon genes associated with heme d1 biosynthesis, as in Heliobacillus mobilis and Heliophilum fasciatum. NirJ1 is presumed by bioinformatics analysis (Xiong, et al.) to be a heme d1 biosynthesis protein by context, perhaps involved in conversions of acetate groups to methyl groups in conversion from uroporphyrinogen III. A very closely related protein, involved in alternative heme b biosynthesis, occurs in Desulfovibrio and in methanogens [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
ISITKLLCNTENFGDSLRYVHGAKGQKHGASPGHGPVVVWNCTRTCNLRCIHCYADSDNKKYEGELTTEE
AKRFIDDLADFKVPVLLFSGGEPLMREDIFELAEYAKKRNIRSTISTNGTLIDKDVAKRLKKIGVGYVGI
SLDGIGENNDKFRGKKGAFDAALAGIRNCVAVGQKVGLRFTINRHNYKELEDIFDLIEEENIPRVCFYHL
VYSGRGSKMVAEDISHEESRQAMDLIMERTLDFHRRGLDKEILTVDNHADAVYLYLKLKKKDPDKADKIL
KLLKTNGGNRSGIAFANVDFKGNVHPDQFTQNHTFGNVRERKFGEIWTDLSNPILAGLKNRKPLLKGRCA
SCKWLNVCNGNFRTRAEAVTGDFWESDPACYLTDEEI
>gnl|CDD|274947 TIGR04055, rSAM_NirJ2, putative heme d1 biosynthesis radical SAM protein NirJ2. Members of this radical SAM protein subfamily, designated NirJ2, occur in genomic contexts with a paralog NirJ1 and with other nitrite reductase operon genes associated with heme d1 biosynthesis, as in Heliobacillus mobilis and Heliophilum fasciatum. NirJ2 is presumed by bioinformatics analysis (Xiong, et al.) to be a heme d1 biosynthesis protein by context. This model has been redone (2014) to remove the branch (TIGR04545) that included DVU_0855, from a similar pathway for heme b biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
IISWNTTNKCNMYCDHCYRDAGVKAEGELSTEEGKKLIDEIAKAGFKIMIFSGGEPLMRPDIFELIAYAT
SRGLRPVLGTNGTLITPEVARKLKKAGAMGMGISLDSLDPKKHDGFRAYDGAWQDAVEGMRNCREAGLPF
QIHTTVMDWNKDEVEDITDFAVELGAVAHHVFFLVPTGRAVNIEEESLRAEQYEELLTRIMKKQKEVNIE
LKPTCAPQFMRIAKQMGVKTRFSRGCLAGISYCIISPKGDVQPCAYLDIPAGNVREKPFGEIWKESPVLK
ELRTLEYKGGCGSCKYKKKCGGCRARAAYYNNGDYMAEEPWCLYHG
>gnl|CDD|274948 TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores [Transport and binding proteins, Unknown substrate]
ITVTGVVVDETGEPLIGASVVVKGTTNGTITDIDGNFSLKVPPGAVLVFSYIGYKTQEVKVKGQKNLNIT
LKEDTQELDEVVVVGYGTQKKKSLTGAVSTVKAKELKKVPVSNLSNALQGKVAGVIITQSSGEPGGDAEI
WIRGISSFGGNNSPLYVIDGVPRDNGLSDLNPEDIESISVLKDASATAIYGSRGANGVILITTKRGKEGK
PKISYNAEFGFSTPTRLPEMLNAYEYAELYNEALLNRGSSPPDIYTDEEIEAYRNGLDPDLYPNTDWQDE
IFKRTAFNQRHNLSVSGGTEKARYYVSLGYYNEEGILKNSDYKRYNFRANIDAKLTKTLKLSLNVSGSLS
KYNNPGGSTSNIWGALMLFPRGTPYSTPPVYSDGYYPAYNSGNTSLQNPYALLNRGYNENERNRLNGNAS
LEQKITKGLKLKGTFSYDYSNYKNKKYYKNPYYYNATGGANNGYYSESNSRSRNYYLEATLNYNRTFGKH
NVSALLGYSQQENKSSSYGGLLDDLPSLDAGTSDASVSGSDSEYRLQSLFGRATYSYKDRYLLEFNFRYD
GSSRFAKGNRWGFFPSVSLGWRISEEKFMKKLKKWLSFLKLRASYGIVGNDNIGDRYPYLSLYNLGDGGY
NFGTNNGTSVTGITESRYGNPNLKWEKTKKWNLGLDLGFFNNRLSLTVDYYYKKTKDILQSRSLPSVTGY
SSPYANIGKVKNKGVELSLNYRNKIGKDFSWSVRGNFTYNKNKILELDEGAYLPVKYPYISKEGGPIGQI
YGYIADGLFKDDDSPKQTFGNVRPGDIKYKDVNGDGKIDDDDRVPIGYSNTPDLTYGFGNSFSYKGFDLS
ALFQGSGGGDVFNDGRGFYPFNGGDWGNVLKIVADNRWTPENPNADYPRLSYGDSNNSNNYQASTRWLED
GSYLRLKNLTLGYTLPKKWLKKIGISNLRVYFSGQNLFTFSKYKGWDPELQGNDGGAYPLQRTFSFGVNL
T
>gnl|CDD|274949 TIGR04057, SusC_RagA_signa, TonB-dependent outer membrane receptor, SusC/RagA subfamily, signature region. This model describes a 31-residue signature region of the SusC/RagA family of outer membrane proteins from the Bacteriodetes. While many TonB-dependent outer membrane receptors are associated with siderophore import, this family seems to include generalized nutrient receptors that may convey fairly large oligomers of protein or carbohydrate. This family occurs in high copy numbers in the most abundant species of the human gut microbiome
DIESISVLKDASAAAIYGSRGANGVILITTK
>gnl|CDD|188573 TIGR04058, AcACP_reductase, long-chain fatty acyl-ACP reductase (aldehyde-forming). This enzyme, found in cyanobacteria, reduces a long-chain (mainly C16 or C18) fatty acyl ACP ester to its corresponding fatty aldehyde, releasing the acyl carrier protein (ACP). NADPH or NADH is the reductant for this reaction. This enzyme may be distantly related to the short-chain dehydrogenase or reductase (SDR) family (pfam00106). The purpose of this reaction is in the first step of alkane biosynthesis (GenProp0942) [Central intermediary metabolism, Other]
MFGLIGHLTSLEHAQRVARDLGYPEYADQGLDFWCSAPPQIVDEITVTSITGQTIEGKYVESCFLPEMLA
QRRFKTATRKVLNAMALAQKRGINITALGGFSSIIFENFNLDQLRQVRNITLDFQRFTTGNTHTAYVICR
QVEQAAPRLGIDLAQATVAVVGATGDIGSAVCRWLDAKTGVAELLLVARNQERLENLQAELGRGKILSLE
EALPEADIVVWVASMPKGVEIDPESLKKPCLMIDGGYPKNLDTKVQGPGIHVLKGGIVEHSLDIDWKIMK
IVNMDNPARQMFACFAEAMLLEFEGLHTNFSWGRNQITVEKMEQIGEASVKHGFSPLLL
>gnl|CDD|274950 TIGR04059, Ald_deCOase, long-chain fatty aldehyde decarbonylase. This cyanobacterial family of fatty aldehyde decarbonylases acts on mainly C16 and C18 substrates to form hydrocarbons and carbon monoxide. Note that the corresponding EC number (4.1.99.5) dating from 1989 refers to a nonorthologous Pisum sativum enzyme that acts on C18 and longer chains and attaches the overly narrow narrow name octadecanal decarbonylase [Central intermediary metabolism, Other]
LDFTSETYKDAYSRINAIVIEGEQEAHDNYISLAELLPDHAEELKKLAKMENRHKKGFQACGRNLGVTPD
MEFAKKFFSPLHGNFQKAAAEGKVVTCLLIQALIIECFAIAAYNIYIPVADPFARKITEGVVKDEYLHLN
FGEEWLKANFETVKEELEEANRQNLPLVWKMLNQVADDAAVLGMEKEALVEDFMIAYGEALSNIGFSTRE
IMRMSAYGLV
>gnl|CDD|274951 TIGR04060, formate_focA, formate transporter FocA. FocA (formate channel A) forms a pentameric formate-selective channel through the plasma membrane. The focA gene is largely restricted to Proteobacteria and occurs adjacent to genes for pyruvate formate lyase (PFL) and the PFL activase, a radical SAM protein. FocA is homologous to a nitrite transport protein, NirC [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
LEMAQIAEDTGVYKATKAPLKSFLSAITAGAFIALAFVFYLTVTTGTSDAPWGLAKLVGGLAFSLGLILV
VVCGGELFTSSTLTLVARASKRITTCQLLKNWIVVYIGNLIGALFFVALIWFAGQYMAANGQWGLNILKT
AQHKIHHTWIEAFFLGILCNMMVCLAVWMSYAGKSLTDKAFIMILPVAMFVASGFEHSIANMFMIPLGIL
IAHFASPEFWQAIGVTPEQFADLTLYHFILNNLIPVTLGNIVGGGVLVGLTYWFIYR
>gnl|CDD|274952 TIGR04061, hypothetical_protein_MettrDRAFT_3896, AZL_007950 family protein. This set of proteins includes PP_3335 from Pseudomonas putida, a protein of unknown function, and AZL_007950, a member of a putative biosynthetic cluster from Azospirillum sp. B510
FPDYPSNARTFVRLDARLLPYWHTLFDVCPRLLKLDPPDGLNIFRPFMTWAYRNRLALNWTYHLSVCRWL
LQSPFRARVTEEHIEALMTAAAARWVAADRSEARGIVLAWQGAADRVFDWKPRARAGPRQVEQEQPLPPP
PWDFAWCPLPGKGLDGFPGWLPIP
>gnl|CDD|274953 TIGR04062, hypothetical_protein_CY0110_29519, dnd system-associated protein 4. A DNA sulfur modification system, dnd (degradation during electrophoresis), is sparsely and sporadically distributed among the bacteria. Members of this protein fam ily are strictly limited to species with the dnd operon, and are found close to the dnd operon on the chromosomes of species such as Nostoc sp. PCC 7120, Geobacter uraniireducens Rf4, and Roseobacter denitrificans OCh 114 [DNA metabolism, Restriction/modification]
NRIRIAKDKEELVKKLVDDKGGTGPFQTYADVIVFAAALGVKYKKRIPLKAIKEPSPIDLEIFISRGYDA
VIKLIAIAETNDIKILSSDNAEAEDERVKIFEEYANGGLEILQRELFRGAVDYSERLLLLIISERIDETQ
PDEEFDLSKFL
>gnl|CDD|274954 TIGR04063, Glycosyl_transferase_group_1, PEP-CTERM/exosortase A-associated glycosyltransferase, Daro_2409 family. PEP-CTERM/exosortase is a protein-sorting system associated with exopolysaccharide production. Members of this protein family are group 1 glycosyltransferases (see pfam00534) in which the overwhelming majority occur in species with the EpsH1 form of exosortase (see TIGR03109), and usually co-clustered with the exosortase. A typical member is Daro_2409 from Dechloromonas aromatica RCB
RILHVLDHSLPLHSGYTFRTRAILRAQRALGWETRHLTGPKHGAAGALEEEVDGLHFYRTPPPAGARLPL
LRELAVMQALARRLEEVAREWRPDILHAHSPALNGLAALRVGRRLGIPVVYEIRAFWEDAAVDHGTTREG
SLRYRLTRALETYALRRADAVTTICEGLRGDLVARGIPAEKITVIPNAVDLDLFGLPAPRDPALAAELGL
EGAPVIGFIGSFYAYEGLDLLVAALPRLLRRHPDARLLLVGGGPQEEALRAQAAALGLADRVVFTGRVPH
DEVERYYSLIDVLAYPRLPMRLTELVTPLKPLEAMAQGRLVAASDVGGHRELIRDGETGVLFPAGDPAAL
AAALLALLDNRAQWPELRAAARRFVETERNWAASVARYQDVYRRLLA
>gnl|CDD|274955 TIGR04064, rSAM_nif11, nif11-like peptide radical SAM maturase. Members of this family are radical SAM enzymes that occur co-clustered with nif11-related ribosomal natural product (RNP) precursors described by TIGRFAMs model TIGR03798. Homology within the bacteriocin family reflects largely constraints on the leader peptide, tied to processes such as cleavage and export, and members associate with various families of maturation enzyme. The gene symbol assigned is nlpM, for Nif11-class Leader Peptide family Radical SAM Maturase [Cellular processes, Toxin production and resistance]
LAPFHRFTYRGRSYVLNIERMAAARISDRTAAFLAAIEGDPRVRLPQEVRGALRKTDLLAGERGKIAPDL
AGAAAPISTLCLFVAQECNLACVYCYGNAGSYGGGGLMTSATARQAIDWLIRHSGGNKKLGLSFFGGEPL
LNFPLIKRVVEYAKQRGEESGKTFAFSITTNGSLLDDEKIAFLRENQFQVIVSFDGPADIQDRQRPFKDG
QGSYDAVAPKIKKLLSAFPEACARATLYGDTDPGGVLAALKEMGFRSCHLVPASGSLFTGEPEEKALFRR
TRSRLAGLEREAEAWLAAVKSRDADALRQLKDDSSLVTSFGALLFMRKKYFFCGAGRNYVAVDVTGGIYP
CHRFVGLREYKLGGVGAEDPNRGLYLESPVTTSEECRRCFARYYCGGGCAHDNIASSGSPFRPSEAYCRL
RRRTAELAAYAASRLTGDDWEFLYQEGIVIPKPCPLDF
>gnl|CDD|274956 TIGR04065, hypothetical_protein_CpapDRAFT_0557, putative bacteriocin precursor, CLI_3235 family. Members of this protein family are Cys-rich putative bacteriocin precursor peptides restricted to the Clostridia but found in multiple species with up to three per genome. They are found next to a CLI_3234 family radical SAM protein that may perform post-translational modification. This model describes approximately 35 residues starting from the N-terminus. Precursor peptides average about 50 amino acids in length [Cellular processes, Toxin production and resistance]
MKKLGKKLESKKETVEAYSCNCDSNCSCYCRCGG
>gnl|CDD|274957 TIGR04066, conserved_hypothetical_protein, peptide maturation system protein, TIGR04066 family. Members of this protein family occur in various Clostridial genomes, always in the context of a short peptide and a radical SAM protein predicted to modify the short peptide. PSI-BLAST analysis suggests a sequence relationship to archaeal proteins designated as subunits of an H+-transporting two-sector ATPase. The modified peptide is likely to be a bacteriocin, and this protein is a candidate to act in either maturation or immunity
EKLLIYPFNYEFAPLLRHRNLLKDYEIVALVSPNGWGLIGKDAGVADGGTDTGIVVTDDFESELEKCDTV
LFVDSSLKLDYKKYILPKIKEAVEKGKKIICNLNLDDKIKEEIEELCEKKGVEFVYFKNENNFNIEDSDE
EIKEIDTPVIFVMGLGENTNKFDIQLALRKKLEKQGYKVSQIGSREYCELFGFHSFPEFMYSKNISETEK
IIMFNNFIKKIEKEEKPDIIIIGIPGGIMPFNRKITNYFGILAFIVSQAVRPDIAILSLYYEDYNPEYLE
NIKQFVKYKFGTDVDYYNISNKKIDWYETEEIKKLSYITLDEKFVEEKIEELNNDNLPIFNILNDEDILE
LTEYIIEELSE
>gnl|CDD|188582 TIGR04067, bacteriocin_precursor_CLOSPO_01332_family, putative bacteriocin precursor, CLOSPO_01332 family. Members of this protein family are Cys-rich putative bacteriocin precursor peptides found in a few strains of Clostridium and Anaerococcus. This family is related to the family of CLI_3235 (TIGR04065). Members of both families are found next to a CLI_3234 family radical SAM protein that appears to perform post-translational modification
MKFINPFGRTGGGGAQPQACMCSTTGHADYRGTSDSCLHCGCGCDSKGQYRTGNRVASL
>gnl|CDD|274958 TIGR04068, Radical_SAM_domain_protein, Cys-rich peptide radical SAM maturase CcpM. Members of this family are radical SAM enzymes that occur next to clostridial Cys-rich predicted bacteriocin (or other class of ribosomal natural product) precursors (see families TIGR04065 and TIGR04067). They include a TIGR04085 C-terminal additional 4Fe4S cluster-binding domain that is associated with peptide modification by radical SAM enzymes, and they are proposed to be ribosomal natural product maturases. The gene symbol ccpM is assigned, for Clostridial Cys-rich Peptide Maturase [Cellular processes, Toxin production and resistance]
FIHLFKTPGQKYFYDVNTNSILKVNEEVYEELNKYEKSDETPEEKEVIKKLQDKGYLKEKRVEEIEHPET
KLLEYYLENKIQMLILQVTQQCNLRCKYCAYSGSYDNRVHSNKRMSIETAKKAIDFLIKHSEDTDELNLG
FYGGEPLLEFELIKECVEYAKEKAEGKKINFNMTTNGTLLTEEIIEFLYDNEFNLTISLDGPKEIHDKNR
VFADGKGSFDKIMENIKMIKKKYPEYYSKVRFNTVLDPENDFSCINNFFSNYELVKDATVNASLVSELYA
KEEISISEEYIIEYRYERFKLLLSKLGKLDKKHVSKLFRSEFADIKRIYYELKEDIDSLPKKWHHGGPCI
PGVQRLFVNVDGKFYPCERVSEESEAMKIGNIDSGFDIDKIKKLLNIGKLTEEKCKNCWALRFCSLCAAF
ADDNGELSNEKKLSNCAKVRESTEEMLKDICVLKEFGYD
>gnl|CDD|274959 TIGR04069, hypothetical_protein, peptide maturation system acyl carrier-related protein. Both PSI-BLAST and large numbers of noise-level HMM hits show a relationship between this family and the phosphopantetheine attachment site domain modeled by pfam00550. That domain includes acyl carrier proteins (ACP) and features an essentially invariant serine residue that is the attachment site for the phosphopantetheine prosthetic group. In this family, the corresponding residue is not Ser and is not conserved. Members are found in genomic contexts associated with a small Cys-rich peptide and a radical SAM protein we predict modifies the peptide [Cellular processes, Toxin production and resistance]
EIEKKLENIFNDRFNIDFDKINNDLKNENLLGSKLGLSPRDLVYLLFDVEKQFNISIPEEEIANGKFNTF
NNIYKII
>gnl|CDD|213890 TIGR04070, photo_TT_lyase, spore photoproduct lyase. DNA damage to bacterial spores from ultraviolet light accumulates in the form of 5-thyminyl-5,6-dihydrothymine, spore photoproduct. The damage is repaired by spore photoproduct lyase, a member of the radical SAM family of enzymes. The score of this model is set to restrict itself to spore-forming members of the Firmicutes, but additional homologs scoring below the trusted cutoff tend to occur in radioresistant organisms (e.g. Kineococcus radiotolerans) and may be functionally equivalent. A related family in the Mycobacterium lineage is described by family TIGR03886, and may or may not be equivalent in function [DNA metabolism, DNA replication, recombination, and repair, Cellular processes, Sporulation and germination]
FIPKRVIFEPKALEYPLGKEIYNQFKDKGVEIIETSSHNRVTGIPGKTPYEMYREGKKTLVVGVRKSLKF
QTCKPSAHYQLPLVSGCPGMCEYCYLNTTLGKKPYVKVYVNIDEILNKAQKYIDERKPEITIFEGAATSD
PIPVEHYTGALKKAIEFFGKQEHGRFRFVTKFTDVDSLLDLEHNGHTRFRFSINTDYVIKNFEHRTPSLE
ERIEAARKVAKAGYPLGFIIAPIFLYEGWKEEYKELLEELKRKLPKDLEPPLTFELISHRFTKRAKNNIL
EVFPNTKLPMDEEERKFKYGQFGYGKYVYPKEDLDEMKEFFRGNINEYFPNAKIEYFI
>gnl|CDD|274960 TIGR04071, Methanobactin_mb-OB3b, methanobactin precursor, Mb-OB3b family. Methanobactins are siderophore-like copper-chelating natural products with considerable variety from species to species. The 11-residue methanobactin of Methylosinus trichosporium OB3b is derived from a 30-residue precursor. A very similar 31-residue precursor is found in the rice endophyte Azospirillum sp. B510, which has not yet been shown to produce a methanobactin. This model models the shared region of the first 25 amino acids, including a Cys-Gly-Ser motif
MTIRIAKRITLNVIGRAGALCGSTCAATNG
>gnl|CDD|188587 TIGR04072, Radical_SAM_domain_protein, lipid biosynthesis B12-binding/radical SAM protein. Members of this protein family occur in conserved genomic contexts highly suggestive of lipid biosynthesis, including an island shared between Kuenenia stuttgartiensis, which produces ladderanes, and Desulfotalea psychrophila, which produces a different kind of unusual polyunsaturated hydrocarbon
LISSNTTVEPYPVYPLGMAVIAGALSGAGHEVRQFDYLADGASLELLRPLLERFRPDYIGLSIRNIDNVD
SLSSENYINGAKNIVDLIRELSKAPIVLGGPAFSLMPEELLEYLGADYGVVGEGEQLMVWLADRLSRGKP
SPRILRSEQPL
>gnl|CDD|274961 TIGR04073, hypothetical_protein, putative exosortase-associated protein, TIGR04073 family. Members of this protein family are found in beta, gamma, and delta proteobacteria, and in the verrucomicrobia. Twenty-two of twenty-four species encountered contain the PEP-CTERM/exosortase system for modulating extracellular polysaccharide biosynthesis production, suggesting a role in protein sorting. The N-terminal signal sequence is divergent and not included in the model. PSI-BLAST and HMM searches suggest a distant sequence relationship between a region of this protein of about 100 amino acids and a corresponding region of the very large eukaryotic protein vps13, associated with vacuolar protein sorting in yeast
GPARKLGRGLANVATGVVEIPKQIYLTTREDGAAAGFTVGPLKGIGMTVGRTLVGAYEIVTFPFPTYKPT
YDPPY
>gnl|CDD|274962 TIGR04074, Methyltransferase_type_12, 3' terminal RNA ribose 2'-O-methyltransferase Hen1. Members of this protein family are bacterial Hen1, a 3' terminal RNA ribose 2'-O-methyltransferase that acts in bacterial RNA repair. All members of the seed alignment belong to a cassette with the RNA repair enzyme polynucleotide kinase-phosphatase (Pnkp). Chemically similar Hen1 in eukaryotes acts instead on small regulatory RNAs [Transcription, RNA processing, Protein synthesis, tRNA and rRNA base modification]
LLTITTTHQPATDLGYLLHKHPDRVQTFELSFGKAHVFYPEASEERCTAALLLDVDPVGLVRGKRGSSGD
GLGQYVNDRPYAASSFLSVAIGKVFRTALNGRCKARPELADTALPLTVRLPALPCRGGEELVRRLFEPLG
YTVSAEPLPLDEKFPEWGDSRYVTLTLTGTVRLSDLLNHLYVLIPVLDDAKHYWVGDDEVEKLLRKGEGW
LAEHPERELITRRYLKHRRSLARDALARLAEADEAEPEEAEEEEAQEEAAEKPPSLNRQRLEAVVAALRE
SGARSVLDLGCGEGKLLRLLLAEKQFERIAGVDVSARELEIAARRLKLDRMPERQRERIQLFQGSLTYRD
KRLKGFDAAVLVEVIEHLDPPRLPALERVVFEFARPRTVIVTTPNAEYNVLFESLPAGGLRHRDHRFEWT
RAEFAAWAEGVAERFGYTVEFLPIGDEDPEVGAPTQMAVFTR
>gnl|CDD|274963 TIGR04075, Ser/Thr_phosphatase_family_protein, polynucleotide kinase-phosphatase. Members of this protein family are the bacterial polynucleotide kinase-phosphatase (Pnkp) whose genes occur paired with genes for the 3' terminal RNA ribose 2'-O-methyltransferase Hen1. All members of the seed alignment belong to a cassette with the Hen1. The pair acts in bacterial RNA repair. This enzyme performs end-healing reactions on broken RNA, preparing from the RNA ligase to close the break. The working hypothesis is that the combination of Pnkp (RNA repair) and Hen1 (RNA modification) serves to first repair RNA damage from ribotoxins and then perform a modification that prevents the damage from recurring [Transcription, RNA processing]
MKITIPELSLVVLVGASGSGKSTFARKHFKPTEVLSSDFCRGLVSDDENDQSASSDAFDVLYYIAGKRLA
RGLLTVIDATNVQPEDRKGLVALAREYHVLPVAIVLDLPEKVCLERNAARPDRDFGPHVVRRQHQELRRS
LKGLKREGFRKVHVLRSPEEVDAATIEREPLWNDKRDEHGPFDIIGDVHGCRDELETLLEELGYQIERDE
GGRGVDVTHPEGRKAVFVGDLVDRGPDSPGVLRLVMGMVAAGTALCVPGNHDVKLLRALRGRNVKLTHGL
AETLEQLAAESEEFRAEVKEFLDGLVSHYVLDDGKLVVAHAGLKEEYHGRGSGRVREFALYGETTGETDE
FGLPVRYDWAADYRGRAMVVYGHTPVPEAEWVNNTICIDTGCVFGGKLTALRYPERELVSVPAERVYYEP
VRPLVPVATGLSAQQRDDDVLDIDDVLGKRHIETRLRGRVTIREENAAAALEVMSRFAVDPRWLIYLPPT
MSPCETSKLDGYLEHPAEAFAYYRARGVEEVVCEEKHMGSRAVVVVCRDEAVARRRFGVTDGGIGVCYTR
TGRPFFDDPALETALLARLRAALTKAGLWEELDTDWVCLDCELMPWSAKAQGLIRSQYASVGAAARAALD
AAVAALEQAAARGLDVADLLERTAARAAAAEAYVEAYRRYCWPVNGLDDLRLAPFHILATEGRVHFDRDH
VWHMETLARLAAADPSLFMATRYRVVDLTDEESVAAAVAWWEELTAAGGEGMVVKPLAFLVRGSRGLVQP
AIKVRGREYLRIIYGPEYTEPENLERLRQRGLGRKRSLALREFALGLEALERFVRGEPLWRVHECVFGVL
ALESEPVDPRL
>gnl|CDD|274964 TIGR04076, conserved_hypothetical_protein, TIGR04076 family protein. Members of this protein family are uncharacterized. The only invariant residue, and one of three other residues better than 90 percent conserved are both Cys. Phylogenetic profiling results and occasional fusion genes suggest a role for members of this family in redox reactions or iron cluster metabolism. Species occasionally have two or three copies
MKKVRITVVKPIEGPCPCGHKVGDVFIVDGGLIPEGFLCLYAWAAILPYVPALQRGGSYNDWMNDDGVAI
FCCPDPDRPVIFRIERIDE
>gnl|CDD|188592 TIGR04077, hypothetical_protein_HMPREF0348_0872, exported signaling peptide, YydF/SAG_2028 family. This family describes a rare family of small proteins, about 50 residues in length, that includes YydF from Bacillus subtilis and SAG_2028 from Streptococcus agalactiae 2603V/R. Mutational analysis and genomic context show that members of this family likely are modified by a (variably present) radical SAM enzyme, are exported by an ABC transporter, and serve as signaling peptide. The member from Bacillus subtilis induces the LiaRS two-component system [Regulatory functions, Protein interactions]
MKQKNIQKPILKDLEFKKLLTKSNKLAKVNDLWYFVKSKKNRWIAGSGH
>gnl|CDD|188593 TIGR04078, radical_SAM_domain_protein_protein, peptide modification radical SAM enzyme, YydG family. Members of this radical SAM protein family for peptide modification occur only in the context of members of family TIGR04077, which average about 50 amino acids in length. In Bacillus subtilis, this protein (YydG) appears to act on its cognate target peptide (YydF) prior to its export, and result in the creation of a signaling molecule that induces the LiaRS two-component system [Regulatory functions, Protein interactions]
KSVVINLSQRCNASCDHCCFSCSPTSVNCLTKEEIEALVRYFETNEDIELISFTGGEAFLRYSFLLELIH
ILSILGKDVTLISNGFWGTNDKNVKSYFTDMNTAGVRYLTISYDNYHSEFIKVDNIKNILLHSRKYPDIE
IALNMAVDKKNRGVDILDKLGESILGVPITKFPAIPVGRAKNINMEDLQNYYSLIDELELTCPGWEFVYH
HDGYVYPCCSPAIFETNLRLGSEGDQDFSETEDKFNSNLLLYILRREGFTWFINIMKNNNEFSHLDITKE
FSSICEVCKFLFSDMNKIKSITPYMKKYY
>gnl|CDD|188594 TIGR04079, hypothetical_protein_SMSK564_1567, KxxxW-cyclized secreted peptide. Members of this family are short precursor peptides in which the mature form undergoes a cyclization between a Lys and a Trp four residues away. The modification enzyme appears to be an adjacent encoded radical SAM protein. Genomes encoding this system include Streptococcus thermophilus LMD-9 and Lactococcus lactis subsp. cremoris MG1363, among others [Cellular processes, Biosynthesis of natural products]
PELLAELEKVLENSSIAKGDGWA
>gnl|CDD|188595 TIGR04080, rSAM_pep_cyc, KxxxW cyclic peptide radical SAM maturase. Members of this family are radical SAM enzymes that appear to perform a cyclization on an adjacent cognate peptide from family TIGR04079. Genomes with the complete system include Streptococcus thermophilus LMD-9 and Lactococcus lactis subsp. cremoris MG1363, among others. The gene symbol assigned is kwcM, for KxxxW Cyclic peptide Maturase [Protein fate, Protein modification and repair]
MMTISDDFLFRLEKFGGILINKNNFDRIELDESEAIFLSLVKEHGFEIAFNEFIKEFKADKLEKILLEKI
YRDGEIEEKGINPDEIINKAQKHIAELKKHNIISFPLELVIYPSMYCDLHCGFCFLANREDENAHLADDW
EKILRQAKDNGILSFSILGGEPTKYFDIDNLLIACDELKIKTTITTNAQEIKKSTIDIIAKSDYITPVIS
LESIDDFKNFELMGTRPDRGIELAKLFHERGKKCRINAVYSKQSEEDIIELLDFAIENEIDRFSIADYSE
VTGFTKIKKIYDIADLRKLEEKVRDYILDNEIANFNFATEGCFLFTAFPELIEEGEEFSEFEEMYFGCRA
KFTKMEILSNGDILPCIAFLGEKHTKQNAFEKDLDDIWKDDPLYGGIREFKTENKDCLKCGLLKICEGGC
YPKLIKEKNPKVFKDKTCNL
>gnl|CDD|188596 TIGR04081, hypothetical_protein_Dthio_PD0538, radical SAM modification target peptide, selenobiotic family. Members of this protein family are small peptides found in the vicinity of a peptide modification-type radical SAM protein family. Multiple members of this protein family occur in species with a selenocysteine incorporation systems and have a TGA stop codon at position that aligns with cysteine residues from other homologs. This finding strongly suggests that GSU_1558 and similar members of the family are selenopeptides. The selenocysteine insertion sequence (SECIS) finder bSECISearch finds two homologous SECIS elements for two TGA codons in the extension of GSU_1558. Meanwhile, the pairing with the radical SAM enzyme suggests additional modification
MDKSDAKTYLAGLCLAALLTGATLAAPGPALGNSGCG
>gnl|CDD|274965 TIGR04082, Radical_SAM_domain_protein, selenobiotic family peptide radical SAM maturase. Members of this protein family are radical SAM (rSAM) enzymes similar in sequence to others with known or postulated roles in peptide modification, and regularly found adjacent to members of the GSU_1558 peptide family described by model TIGR04081. GSU_1558 and several other members of that family appear to be selenoproteins, hence the term selenobiotic
IFPATLRLLDDEALSRLLGDQDKSPEAFPDLLDSLSRELGLPPFLPDLARLELALHTVASAADDVPPPVH
EIVINPTLQLVPLRWSGLPDLLEGAKDEECAPVSGQEGVLVWKDPGTGRVRVEPADQNDLLALKIVAEGI
PPEEAALEAGVAPGTIDRLLDHAVRKGLLLAPPSRIRRDPQIFSDDPSIPERFLSASVFTLQWHITQACD
LHCRHCYDRSQRSPLPLDQALAVLDDFASFCRERNVRGQVSFSGGNPLLYPHFLELYREAVRRGFAVAIL
GNPVSRERLEELLAIQRPDYYQVSLEGLEEHNDSIRGPGHFDRVLAFLELLRELGIPSQVMLTLTRDNMD
QVLPLAELLRGKTDLFTFNRLSQVGEGAALLLPSPEAYAAFLAEYLDAAERNPVLGLKDNLLNIVREERG
QPLFGGCTGFGCGAAFNFVALLPDGEVHACRKFPSPIGNIAQDGLEEIYDSPAARRYRAGSEACRDCRLR
PVCGGCLAVVHGLGLDPFKDRDPFCF
>gnl|CDD|274966 TIGR04083, rSAM_pep_methan, putative peptide-modifying radical SAM enzyme, Mhun_1560 family. Members of this family are radical SAM enzymes, homologous to a variety of other peptide-modifying radical SAM, and found primarily in methanogenic archaea
HVMIIPTLGCPSKCKYCWSSEETSPVMSIDTVKDIVEWLKDFRDDRVTFTFHGGEPLLAGADFYRQALPL
LSEGLAHLKPEFAMQTNLWLMTPELAEIFAEYNVPIGSSIDGPEEINDYQRGEGYYQKTMKGYEIAKEHG
LDVRFICTFTSYSVKQKEEIFNFFLENGFTLKLHPALPSLRSDNPGEWALDPEEYGELLVYLLDKYLENM
DKIEVMNINDLCRCVFTRRGTVCTFVDCMGTTFAVGPDGSIYPCYRFVGMPEYVMGNVRDRPTMEDLMES
DAGKLMLAFKEYVDTHCAKCSHIKYCRGGCPYNAIAPTDGEIKGVDPHCIAYKRIFDEITDRLNREMFGS
PPMEMAGFGPPPMRKEKPGIMALMRK
>gnl|CDD|274967 TIGR04084, rSAM_AF0577, putative peptide-modifying radical SAM enzyme, AF0577 family. This radical SAM family contains a C-terminal region motif CXXCX5CX3C that is found in PqqE and other radical SAM enzymes that act on peptide substrates. Members of this family are found primarily in the Archaea, but also several eukaryotes (Trichomonas vaginalis G3, Entamoeba dispar SAW760, Giardia intestinalis ATCC 50581, etc.). The function is unknown
LFTTGKCNLRCDYCGGSFPEKVVPWRIKYDINKLKNLIEKDKDATVIFYGGEPLLNPRFIMQVMDNVRAK
RFGIQTNGTLVKLLPEEYWRRMNVALLSIDGRPEVTDKHRGKGVYKRVVKAARYLKELGVETIARMAVTE
DSDIYRDVTHLLSLGFDKVHWQLNVVWDDEWDFLSWAKNSYLPGIRKLVDLFLSELREGRVLGIVPILGV
ISAYFFKPYRGVPCGAGYDSFAITTDGRILSCPIAVREKWAELGNVNVGFRLLEEPVLPEECLSCEYRRY
CGGRCLYAIKERYWGEEGFKAVDEVTKEYLRTVLEIIPEIESLVDKGVIKLSDLYYDPILDSTEVIP
>gnl|CDD|274968 TIGR04085, radical_SAM_protein, radical SAM additional 4Fe4S-binding SPASM domain. This domain contains regions binding additional 4Fe4S clusters found in various radical SAM proteins C-terminal to the domain described by model pfam04055. Radical SAM enzymes with this domain tend to be involved in protein modification, including anaerobic sulfatase maturation proteins, a quinohemoprotein amine dehydrogenase biogenesis protein, the Pep1357-cyclizing radical SAM enzyme, and various bacteriocin biosynthesis proteins. The motif CxxCxxxxxCxxxC is nearly invariant for members of this family, although PqqE has a variant form. We name this domain SPASM for Subtilosin, PQQ, Anaerobic Sulfatase, and Mycofactocin
CGAGRNSLVVDPDGDVYPCDHFVYPEYKLGNIREDSLEEILNSSKQLEFGRWKSPKLPEECRSCKYLPLC
GGGCPANRYLKTGDINGPKNPLC
>gnl|CDD|274969 TIGR04086, hypothetical_protein, putative membrane protein, TIGR04086 family. Members of this family of strongly hydrophobic putative transmembrane protein average about 125 amino acids in length and occur mostly, but not exclusively, in the Firmicutes. Members are quite diverse in sequence. The function is unknown
SAVLKGLLVAYILTLILLLILALLLYFTDLSEGSLSWLILIIYILSVFIGGFIAGKKAGSKGWLWGLLTG
LLYFLILLLISFLFYPGPLFTLGQLLKLLLCLLAGALGGMLGVNL
>gnl|CDD|274970 TIGR04087, hypothetical_protein_BcellDRAFT_2107, YqxM protein. Members of this protein, including the partially characterized YqxM of Bacillus subtilis, are always found adjacent to a variant form, SipW, of signal peptidase, and are targets for this signal peptide, as is the biofilm protein constituent TasA. The function may always be associated with biofilm formation. In one instance, this protein is fused with the SipW signal peptidase
RLSRLRRFRKKKKKIMIFFQLSLIFYLAIAICSQLTGDTTASFHDVKSFSLSVQAGEDFQYTDDNWDGSD
LHFTGQTTTKGTVCAPLELFAELKNRGKEMTKSTWKWELYFSANGNKPLQNGNKIEEGTITPLKSGSIYK
LEYKAMKPGIYAFKVYQPPGYPANDEGETFEWSEKMVLAKCKEPET
>gnl|CDD|274971 TIGR04088, hypothetical_protein, SipW-cognate class signal peptide. This model describes a protein N-terminal domain found regularly in proteins encoded near a variant form of signal peptidase I such as the SipW protein of Bacillus subtilis. Many though not all members are homologs of camelysin (a casein-cleaving metalloprotease) and TasA (CotN), a metalloprotease that is secreted, along with extracellular polysaccharide (EPS), to be the major protein constituent of the Bacillus subtilis biofilm matrix. Sequencing from several known TasA/CotN proteins shows the cleavage location to be near the center of the alignment and typical of type I signal peptidases, with small residues at -3 and -1. This domain, therefore, appears to be a special subclass of signal peptide
IAAAGLALLLGGGGTLAYFTDSETASNTFTAGTL
>gnl|CDD|274972 TIGR04089, conserved_hypothetical_protein, alternate signal-mediated exported protein, RER_14450 family. Members of this Actinobacterial protein family contain the cognate signal peptide domain, modeled by TIGR04088, for the variant SipW form of the signal peptidase I family. The remainder of this protein, however, differs from families such as Peptidase_M73 (pfam12389) and YqxM (TIGR04087) that share the same signal peptide domain. Some additional homologs to this family lack full-length homology and are excluded by the trusted cutoff as set. The two known targets for export by the SipW signal peptidase in Bacillus subtilis act in producing biofilm matrix material
MNKKTKGAIAAGAAAALLLGGAGTFALWNDSATVSGGTITAGTLALSAATGGGWKDVTGAGAVAIDIATY
KIVPGDTLTYTCTFTVTAVGDNLKATLTLDTSSIVTANSATGGLTAAVAAATTAATSTGTNATTLIDLPD
GGTQTVTVTVTVTFKPGTTGTTAQGQTASLDNVTLTLTQ
>gnl|CDD|274973 TIGR04090, hypothetical_protein, alternate signal-mediated exported protein, CPF_0494 family. Members of this largely Clostridial protein family contain the cognate signal peptide domain, modeled by TIGR04088, for the variant SipW form of the signal peptidase I family. The remainder of this protein, however, differs from families such as Peptidase_M73 (pfam12389) and YqxM (TIGR04087) that share the same signal peptide domain. Some additional homologs to this family lack full-length homology and are excluded by the trusted cutoff as set. The two known targets for export by the SipW signal peptidase in Bacillus subtilis act in producing biofilm matrix material. Members include CPF_0494, adjacent to SipW homolog CPF_0493
KKSLLAIIGLAAVAVIGGTLAYFSQTLTVDNEFKTAKYDSTIVEEFTPPDEWLPGVTVNKDVTVDNTGDV
DVVVRAKITETWTRRGEGKPISPAKGETIPNTFVDENGSVVNGQVTWVNDVVYLDSGKQAEAKDKWVYGD
KDGYFYYNGIIGAGGDTPRLLDSVTLNPLIDSWVTEKNTFPDENGITDDGETGWVKVSETPNDATVTRTV
VNGNYGYDDANYTLTITAQTVQATKEAVAGVFGD
>gnl|CDD|274974 TIGR04091, hypothetical_protein, D-alanyl-lipoteichoic acid biosynthesis protein DltB. Members of this protein family are DltB, part of a four-gene operon for D-alanyl-lipoteichoic acid biosynthesis that is present in the vast majority of low-GC Gram-positive organisms. This protein may be involved in transport of D-alanine across the plasma membrane [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
TPYGNPSFFLILILALLPAIILGLFGKRFKYYELLVSLVFLVLIFGGDKWQLIALILYVIWQTLLVKGYL
AYRKKKNSKWVFYLAVFLSILPLVLVKVSPLFPLHSLLGFLGISYLTFKAVQIIIEIRDGLIKEISLWDF
LYFLLFFPTISSGPIDRSRRFEKDYEKVPSREEYLELLGKGIHYIFLGFLYKFILAYLIGTLLLPKLEKD
ALFFWNLLGYMYAYSFYLFFDFAGYSLFAVGISYLMGIETPMNFNKPFLSKDIKDFWNRWHISLSFWFRD
FVFMRFVFFLMKKKWFKNRLTTSNVAYLINMLIMGFWHGLTWYYIAYGLYHGLLLALTDAWQRKSKKYKK
NKKNKWTKALSIFVTFHLVCFGFLIFSGFL
>gnl|CDD|274975 TIGR04092, hypothetical_protein, D-alanyl-lipoteichoic acid biosynthesis protein DltD. Members of this protein family are DltD, part of the DltABCD system widely distributed in the Firmicutes for D-alanylation of lipoteichoic acids. The most common form of LTA, as in Staphylococcus aureus, has a backbone of polyglycerolphosphate
FGPIILALVLFVLLLFLPSKINKSLISKKTDKSAATSLSPNKFKGLDIKKQALEDKYVPFFGSSELSRFD
PFHPSVLFNKYNRDYTPFLIGRGGTQSLTHAINMGSIGDSLKNKKAVFIISPQWFTKKGVDPDAFQSYFS
PLQFYNFLKNKKISTETKRYAAKRLLELLVVKSDKILENLLKRLYANDKKLSKFDKVYLKPYYRNLLEKE
DDLFSRFKLKKYKKKIKPAAKKLPEKYDWEELDKKAVKEGKKRTTNNPFGIDNKFYNKRIKKKLKKLKGS
QKNFDYLKSPEYGDFQLVLDIFKELGIDVLFVIPPVNGKWYDYTGLSKEMRQQYYKKIKYQLKSQGFNIA
DLSDKEYEPYFMEDTIHLGWKGWLAVDEAIYKFL
>gnl|CDD|274976 TIGR04093, hypothetical_protein_L8106_25395, CRISPR-associated endonuclease Cas1, subtype CYANO. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes a clade of Cas1 limited to the CYANO subtype of CRISPR/Cas system and most often the type found there
STLYITQPDAKISKDDGRIIVVDSDGEEKVASFPLIKVETIVVFGEATLTTPALAHLLERGIVLHYLTRF
GKYFGSLVPELTRNTILRVAQHQAHISPQQRLAIAREIVRGKLRNSRTMLYRRGRKQTKIPELEKPVDDK
NSLDSLRGLEGEAAAIYFGCLSDLLPDEWSFHGRTRRPPTDPVNALLSLGYALLRTQVLSALRIVGLDPY
IGFLHVDRHGRPALALDLMEEFRPIIVDAVVLRLINRKMLKPKDFQEEPGAVRLKDEAFKLFLGKFEEKM
QSEFKHPIFKYKVSYRRAIELQARLLAKALMGEIKEYPPLIIR
>gnl|CDD|274977 TIGR04094, AraC_family_transcriptional_regulator, YSIRK-targeted surface antigen transcriptional regulator. Bacteria whose genomes encode only one protein with the YSIRK variant form of signal peptide (TIGR01168) were examined for conserved genes near that one tagged protein. This protein is found adjacent to at various classes of repetitive or low-complexity YSIRK proteins (whether unique in genome or not), in a range of species (Enterococcus faecalis X98, Ruminococcus torques, Coprobacillus sp. D7, Lysinibacillus fusiformis ZC1, Streptococcus equi subsp. equi 4047, etc). The affliated YSIRK proteins include Streptococcal protective antigen (see) and proteins with the Rib/alpha/Esp surface antigen repeat (see TIGR02331). The last quarter of this protein has an AraC family helix-turn-helix (HTH)transcriptional regulator domain
LLKSLHVCLKLPITVFDKDFSVLKSYESDRTKLLPYDFKLTLNKKSKETIQFLFFSGILNEMFLIYPFQD
YYIIIGPWRSNVIDKLFFKNKLADINQHELSQESLYQYLEQLPVFSLGDIRDLLILIHYLFSGKLEDLYS
EPLHLYTKKNKQKLEKEKSEELSKQNFTSETYLFHYENQILELVKKGDIQQLKELVFQLSNSVIPIVSGD
DLRSEKNYSIIIFEKLSQLAIQMGVDIVDAYRLRDYYIQEIEEQTSLMDVLKLRDSAIIYFTELLHEISI
NHHSPLIRAVIQYINLNLYDPLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEAKYLLRSQI
PVSEVSNELGFYDLSHFSRTFKKHTGVSPKQYQ
>gnl|CDD|274978 TIGR04095, type_III_restriction_protein_res_subunit, DNA phosphorothioation system restriction enzyme. The DNA phosphorothioate modification system dnd (DNA instability during electrophoresis) recently has been shown to provide a modification essential to a restriction system. This protein family was detected by Partial Phylogenetic Profiling as linked to dnd, and its members usually are clustered with the dndABCDE genes
PSIPPTFELRDYQKEAIRAWFKNNGRGILKMATGTGKTLTALAAASKLYEKIGLLVLLVVCPYQHLVDQW
AREAEKFGLNPILCYESVSNWQSELSTGLYNLNSGNQKFLAIITTNATFIGKNFQSQLRRFPGKTLLIGD
EAHNLGAPRIRESLPDNIGFRLGLSATPERHFDEEGTNALLDYFGKIVYEFTLKEAIKDGALVRYLYYPI
IVELTEDETDEYVELTEKIGKLLGNAEDDESEANGPLKMLLIKRARLIGSAQNKLPALRDLLSKRLETSH
TLFYCGDGSVEPISDEEDRQIDAVVRLLGNELGMRVNTFTAEESKEEREELLRQFESGLLQGLVAIRCLD
EGVDIPATRTAYILASSSNPRQFIQRRGRVLRPHPGKNRATIYDFIVVPPTEADDLDDNTFEVERSLLKR
ELKRFVEFAQLAENAGEALSKLLEIKKRYNL
>gnl|CDD|274979 TIGR04096, conserved_hypothetical_protein, DNA phosphorothioation-associated putative methyltransferase. Members of this protein family show distant local sequence similarity to a number of S-adenosyl-methionine-dependent methyltransferases. The family is identified by Partial Phylogenetic Profiling as closely tied to the DNA phosphorothioation system (dnd), and members are found adjacent to dnd genes in at least 13 species (Streptomyces lividans TK24, Shewanella frigidimarina NCIMB 400, Mycobacterium abscessus ATCC 19977, Nostoc punctiforme PCC 73102, Vibrio fischeri MJ11, etc.). The DNA phosphorothioation enables a novel form of restriction enzyme activity. Most members of this family appear in species with the DNA phosphorothioation system [DNA metabolism, Restriction/modification]
QIDRHKTAIVRKELSRPVRLALEDGLLNPDYTFFDYGCGRGDDLRELAAHGYDSAGWDPYYRPDAPLIPS
DIVNLGYVINVIEDQDERREALIRAWELTQKVLIVSAQMLIDDRDISGFTPYGDGVITRRNTFQKYYEQE
ELKSYIEQVLNVDAIPIAPGIYYVFRDKAEAQEFLASRFRSHTSWPRITAPVKRFEDYQELLAPLMDFCL
DRGRLPVNGELEESTEIREEFGTHRRAFKLILQVTDEAEWDAIADKRRQDLLVYLALSLFGKRPKFSQLP
ETLKRDIKAFFGSYKKACALADRLLFSLGDPEIIEKACNNSPVGKLTPGSLYVHISALEKLPPLLRLYEG
CASQTYGRLEEATLVKLHIQSPKVSYLFYPDFDTEPHPRLRTRMKIDLRDLDVDFRDYVREENPPPLHRK
ELFVTPDYPDYEKFAKLTKQEVDLGLLDHPKEIGTLEGWESCLEEHGAEIRGHRLIWR
>gnl|CDD|274980 TIGR04098, conserved_hypothetical_protein, biosynthesis cluster domain. Radical SAM family TIGR04043 is a marker for a widespread eight-gene probable biosynthetic cluster of unknown function. This protein family describes a domain that occurs as an additional protein for some of those clusters, but also as the N-terminal domain of large, multidomain polyketide synthases and in other contexts
RVVLGMPQLCGGGLSENWLLKELGDRHWDLLAAACGTDVPDFRDADGAPVYAAFCATRLRGARLDQLREG
DELSVTSRLFRVGGTSVLSRHRLSRAGRPVADVELLSRFVRRTVPGSNRSLARVSPPGFRGAHLPLLPAQ
YSPRRIRARARRAGAFGMHPGPPGRDVPDLLALEYEPCPSQDFNGAGLLYFASFQAIVDRAEWRLWRGLG
RPLRAFLRVLDRDVFYLGNADAGERLDVRLTRHREECDGELHDVELRRADDGRLLAVAFT
>gnl|CDD|274981 TIGR04099, conserved_hypothetical_protein, probable biosynthetic protein, Pnap_2097 family. Radical SAM family TIGR04043 is a marker for a widespread eight-gene probable biosynthetic cluster of unknown function. This protein family occurs only in the context of TIGR04043 member-containing biosynthetic clusters, although in a minority of such clusters. This protein family belongs to the TIGR04098 domain family, which also includes N-terminal domains of several probable polyketide synthases. A role in biosynthetic processes is suspected
LGMPQLSPTGLSENWLLKECGHRHWLLLAAAAGRDVPDFRDADGRPVYAAFCAVSLDDARLDSVRENDAL
EIRSTLARVSGTQHASRHRLRVRGRPVGEVEMLSAFVRREVAGSNRSIARVRLDGRPPAEPGEALALAAL
AARLRAGDRETHPGLARGEARELATFRFEPCPNQDFNGAGLLYFASFQAFVDRAEWQWFRRAAPPVTRAR
DLFFHGNVDPGDALTVRLLALRDDEGGLSHWSELRRDSDGTLIADVFT
>gnl|CDD|188615 TIGR04100, Radical_SAM_domain_protein, radical SAM enzyme, TIGR04100 family. Members of this protein family are radical SAM enzymes that appear paired with members of TIGR04002, a family of small (~170 residue), mostly hydrophobic protein. This family of radical SAM enzymes belongs to a larger family TIGR04038, in which some members show regularly in contexts with TatD
TIIYEYGNKLYVNITNKCPCACTFCIRNQGDGAGGSDSLWLEHEPSLEEIIAALDAFDLSGYEELVFCGY
GEPTERLDALLEVAKYIREKYDIKIRINTNGLADLIHGRSTAPELAGLIDAVSISLNAPDAESYLEVTRP
KFGIDSFDAMLDFARDCKRYIPEVVFSVVDVIPEEQIEASKKLAESLGIPLRVRHFS
>gnl|CDD|200352 TIGR04101, 3-ketoacyl-acyl-carrier-protein_reductase, CCGSCS motif protein. This protein family, with average protein length about 58 residues, occurs in several marine bacteria, such as Shewanella benthica KT99, Marinobacter sp. ELB17, and Photobacterium profundum 3TCK. The striking feature is a C-terminal motif CCGSCS, which (perhaps coincidentally) resembles conserved core motif [LC]CGSC shared by two methanobactin precursors (see TIGR04071). There is no detectable conserved gene region for these proteins
MALSFKKIFKKKKSAAKQVKLELEAIQQAQQSEEQVAADIEEKKKPKHGEPGVCCGSCS
>gnl|CDD|200353 TIGR04102, SEC-C_motif_domain_protein, SWIM/SEC-C metal-binding motif protein, PBPRA1643 family. Members of this protein family have a SWIM, or SEC-C, domain (see pfam02810), a 21-amino acid putative Zn-binding domain that is shared with SecA, plant MuDR transposases, etc. This small protein family of unknown function occurs primarily in marine bacteria
KFFFKGRIDKRPKHNSSGYNTKREVKLGSEKNPLTLVVQSEERKAEVEAILAEHELFANIEVNADQEENI
VELDGLLNKPKTTTFEKTPNRNDPCPCGSGKKYKKCCG
>gnl|CDD|200354 TIGR04103, heme_biosynthesis_protein, nif11-class peptide radical SAM maturase 3. Members of this protein family are peptide-modifying radical SAM enzymes, with a C-terminal additional 4Fe-4S cluster binding domain like many other peptide-modifying radical SAM enzymes. This form occurs primarily in the genera Cyanothece and Nostoc
YYRTSYAVWEITLKCNLACQHCGSRAGQPRTQELSTAEALNLVQQLAEVGIREVTLIGGEAFLRPDWLEI
AAAITRAGMICGMTTGGYGISLQLAQRMKEAGIAAVSVSIDGLETTHDRLRGKQGAWHSAFRTMQHLKEV
GIPFGCNTQINRLSAPEFPRIYEQIRDAGVYAWQIQLTVPMGHAADNWEILLQPCELLDLYPMLAQVAQR
AAQEGVRVYAGNNIGYYGPYERLLRGGGHPWAFWQGCGAGLSTLGIEADGTIKGCPSLPTSAYAGGNIRD
QPLRSIMEQSEELRFNLNAGTPEGTAHLWGFCKTCEFAELCRGGCNWTAHVFFGRRGNNPYCHHRALNLA
KQGLRERLALKIPAPGLPFDNGQFLLIEEPLNAPWPEPDPLYFTADQIQWPSSWTEQPEKVC
>gnl|CDD|274982 TIGR04104, hypothetical_protein, cxxc_20_cxxc protein. This small, uncommon, poorly conserved protein is found primarily in the Firmicutes. It features are pair of CxxC motifs separated by about 20 amino acids, followed by a highly hydrophobic region of about 45 amino acids. It has no conserved gene neighborhood, and its function is unknown
PICKNCNEKFSYKELLKSLWFLYRPIKCPNCGTKQYLTAKSRKKSVLTVFIPLLLVLFLLNIFGLPFLLI
ILIYIILLLLIVLLTPFFVKFTDK
>gnl|CDD|274983 TIGR04105, hypothetical_protein [FeFe] hydrogenase, group B1/B3. See for descriptions of different groups
FDTNVQKIRHEVLTEVAKLAFEGKLEEEIEDIPYEIIPGEKPRYRCCVYKERAIIRERVRLALGLDPRDA
DDELKLLSEYAIAELEYDPPIINVIDEACDACPINRYTVTDACRGCLAHPCIEVCPKGAISMVNGRAYID
QEKCIECGKCKKACPYNAIVEIERPCEKACPVGAISSDEDGRAVIDYDKCISCGACMVACPFGAISDKSQ
IVQVIKALKSGKKVYAMVAPAIVGQFGPKATPGQVKTALKKLGFADVVEVALGADMVAVHEAEEFAERVE
EGKKFMTTSCCPAFVNMIKKHFPELAENISTTVSPMVATARYIKKKDPDAKVVFIGPCIAKKLEAQRDEV
KGDVDYVLTFEELAAMFDAKGIDLEECEEEDLDDASAFGRGFAVSGGVAAAVKAAIKEKGPDVEVKPVKC
NGLDECKKALTLAKAGKLPGNFIEGMACEGGCVGGPGTLVSP
>gnl|CDD|274984 TIGR04106, hypothetical_protein_GobsU_11505, CRISPR-associated protein GSU0052/csb3, Dpsyc system. This model describes a CRISPR-associated (cas) protein unique to the Dpsyc subtype (named for Desulfotalea psychrophila), a variant type I-C subtype, although not universal to the that subtype. Members of this family occur in CRISPR loci of Geobacter sulfurreducens PCA, Gemmata obscuriglobus UQM 2246, Rhodospirillum centenum SW, Planctomyces limnophilus DSM 3776, and Methylosinus trichosporium OB3b
PISIPVDLTNPGQFFACCGLLELADRLWPGAEGWFDGGTRRFLLRTKGAENAFATLVGFLTRARLVALAP
DSGLRRSTELWSVETKRLEEFPSLDPEKKALLKALQEDGVRLPAPFDIWLDWFWDEKSGVDNVKTWAGQQ
SVASIARDMLSALKSLTWDIHSADPFLAAAPQSSSLRFDFDRDYNTQGIPLDVGFSPNDHKTVKMVGRPL
VELLAFVGLQRFRPLRIDKLNRYRYGAWTLPLPPLLARAALGGAELPFRRRSFEFRLLYRTRYIKSFLEA
TP
>gnl|CDD|274985 TIGR04107, coproporphyrinogen_III_oxidase, putative heme utilization radical SAM enzyme HutW. HutW is a radical SAM enzyme closely related to HemN, the heme biosynthetic oxygen-independent coproporphyrinogen oxidase. It belongs to operons associated with heme uptake and utilization in Vibrio cholerae and related species, but neither it not HutX has been shown to be needed, as is HutZ, for heme utilization. HutW failed to complement a Salmonella enterica hemN mutant (), suggesting a related but distinct activity. Some members of this family are fused to hutX
RFAFPERRAAHPGGGSRPVPPEEWQSVWQRLTATPRSARKLLYIHIPFCRTRCTFCGFFQNAWSPELGAA
YTDALIAELAAEAALPLTQSGPIHAVYIGGGTPTALSADDLARLIRAIRRYLPLAPDCEITLEGRINGFD
DEKADAALEAGVNRFSIGVQSFDTEVRRRLGRKDDREEVLARLEELSALDRAAVVIDLIYGLPGQTDEIW
QQDLRIAADLGLDGVDLYALNVFPGTPLAKAVEKGKLPPPATTPEQARMYAYGVEFLAAHGWRQLSNSHW
ARTNRERNLYNSLAKSGAECLAFGAGAGGNLGGYSYMNHRDLDTYLEAIAAGQKPLAMMTRQSPNHALFA
AIKAGFERGRLDLAALPAALGTDLRAALAPLLAQWQQAGLVELSGDYLRLTLAGRFWAVNLAQGLIEVLA
>gnl|CDD|274986 TIGR04108, Heme_utilization_protein_HuvX, putative heme utilization carrier protein HutX. Members of this protein family are HutX, found paired with HutW in some heme utilization loci although not shown directly to be necessary for heme utilization. This protein is homologous to the heme carrier protein HemS, while its partner HutW is homologous to (but does not complement) HemN, the radical SAM enzyme oxygen-independent coproporphyrinogen III oxidase involved in heme biosynthesis
LRALLAENPDAVLEAIARELGVSELEVVRALPEEMVTLVPGDHFDEILQDLSGWGDVTTIVHTGDVIFEV
KGPLPKGKVAHGYYNLMGKKGGLHGHLKADNCAAIALVSRPFMGKETHSVQFFNAEGEAMFKVYLGRDEK
RQLLPEQVERFRAL
>gnl|CDD|200360 TIGR04109, heme_ox_HugZ, heme oxygenase, HugZ family. Members of this protein family are HugZ, a class of heme oxygenase that belongs to the PPOX family (pfam01243) and lacks homology to the HmuO family (pfam01126). Characterized members of this family include HP0318 from Helicobacter pylori and CJ1613c from Campylobacter jejuni. This enzyme releases iron during the conversion of heme to biliverdin
RIIEHMNAHHVDDLAVLCKKFGKVENVTNVRLKSVDEDGMDIGYNGNETLRVEFPKKAEDEGEIKNEIIE
LCSSAKKEQGIAAVEEEINAFIDSFKSVILSTLNANGEVVCSYAPFVSDGGDYYIYISEVSEHFANLKNN
PNKVEVMFLEDESKAKSIIARKRLRYKANARFLERGAKFDEIFDKFQEKTGGEGGIKTIRAMKDFHLVKL
EFKKGRFVKGFGQAYDIDGGEITHVGQDGNPHN
>gnl|CDD|200361 TIGR04110, hypothetical_protein_VSWAT3_12502, heme utilization protein HutZ. Members of this family are heme utilization proteins, typically designated HutZ. They are members of the PPOX family (pfam01243) and, except for the lack of an N-terminal extension, are closely related to one form of heme oxidase (1.14.99.3), HugZ (TIGR04109). Members typically are found in a three-gene operon with radical SAM enzyme HutW and a protein of unknown function, HutX
SEKQERLQNRLGPEIQEFRDERQTLQLATVDKEGNPNVSYAPFALNDDGYYVLISEIARHARNLKAVPKV
SLMLIEDEAEARTIFARKRLTFDATAELVERDSERWTQAIAALKARFGEIIDGLSGLGDFNLFRLKPTQG
LFVKGFGQAFQVSGDDLVDFVHLREGHK
>gnl|CDD|274987 TIGR04111, conserved_hypothetical_protein, phage-associated protein, BcepMu gp16 family. Members of this protein family occur in Burkholderia phage BcepMu, Pseudomonas phage B3, and Burkholderia phage KS10, and many bacterial putative prophage regions. The member from Burkholderia phage BcepMu is named gp16. Homology suggests DNA-binding activity [Mobile and extrachromosomal element functions, Prophage functions]
TAEQAKAEFRRQGISIAQWARENGFSPRLVYDVLNGRRKGRRGKSHEIAVKLGLK
>gnl|CDD|274988 TIGR04112, hypothetical_protein, putative selenium metabolism protein, YedE family. For 79 of the first 80 reference genomes in which a member of this protein family, YedE, is found, a selenium utilization system is found, spread over a broad taxonomic range (Firmicutes, spirochetes, delta-proteobacteria, Fusobacteria, Bacteriodes, etc. This family is less widespread than YedF, also involved in selenium metabolism
GVILTGLVIGLLAALLVKLGNPGNMGFCIACFLRDIAGALGLHRAAVVQYIRPEIIGLVLGAFIAALITK
EFRARGGSSPLVRFFLGFFVMIGALVFLGCPLRMVLRLAGGDLNAVVGLLGFIAGIGIGVFFLKRGFSLG
RAYPTSKAEGYILPVVMIVLLVLLLAAPSFIFFSEKGPGSMHAPILISLAAGLIVGALAQRSRLCMVGGF
RDLILFKDTHLLSGFVAILVAALIGNLVLGQFKLGFAGQPIAHTDGLWNFLGMALVGLASVLLGGCPLRQ
LILAGEGNTDSAVTVLGMLVGAAFAHNFGLAASPAGPTLNGKIAVIIGLIVVLAIGF
>gnl|CDD|274989 TIGR04113, hypothetical_protein_AaLAA1DRAFT_1703, CRISPR-associated protein Csx17, subtype Dpsyc. Members of this protein family are found exclusively in CRISPR-associated (cas) type I system gene clusters of the Dpsyc subtype. Markers for that type include a variant form of cas3 (model TIGR02621) and the GSU0054-like protein family (model TIGR02165). This family occurs in less than half of known Dpsyc clusters
IALPGCSPDPLGSYLKALGVLRLLSEQRDPDARGWWDDETFMLRTELDPEDLTSFFLEEYQPTPIIAPWN
GGSGFFRGDNEEALEALRNSTSERFRPYRDTIEAADEALADFNLSEKPGSKDKVALLARLRARLPDEALE
WLDAAAVLTADRRSYPPLLGTGGNDGRLDFTNNFMQRLEELFLPTGSPRNASKDFLRSALFGEPVTGLVK
GAIGQFSPGAAGGYNSGTGFDAGSLVNPWDFILAIEGALLFASSASKRLGAQSGSTLAFPFTVRPSAAGF
GSVATEDEGDARAEIWMPLWRRPASLPELSQLFSEGRAQLGRRLARNGLDFARAIASLGVDRGITAFQRY
AFLMRNGSAYLAVPLGRFAVRRQPRADLINELDGWLNRFRSFPRDGKASFLSARRRIEEAIFAAATHPHP
SRFQELLIALGEAERRLALSPALRERVHVRPLPLLSPEWVLADDDGSPEFRIALALASIHDGPVGPIRSF
LAPVEPGRRGRWVWEEEPPRVVWTGGDLARNLAAVLERRLLEEARKDNDDRPQGGPCTASLSDIAQFLRG
ELDDRRIADLLWGLSLIDWRASNKRRQMNKPEKDTEVDATSLPAAYALLKLLFAPEALLRRALRETGGRS
LPVPRAVLRLLRAGDADRAVELALRRLRISGLRPAHPGVDVDTHDPRRLAAALLFPIWDRDRTTLFTRLL
LPQ
>gnl|CDD|274990 TIGR04114, hypothetical_protein_CLOSPO_02925, modification target Cys-rich repeat. This model describes a cysteine-rich repeat found in a number of bacterial putative radical-SAM modified natural product precursors. A substantial fraction of members of this family have been missed during gene-finding. A true hit to the model must exceed both TC on the whole and trusted cutoff 2 for at least one domain, to avoid false-positives from African swine fever virus proteins
GCSGSCSGTCTGTCSGCC
>gnl|CDD|200366 TIGR04115, radical_SAM_superfamily_protein, radical SAM peptide maturase, CXXX-repeat target family. Members of this radical SAM domain protein are predicted peptide maturases, similar to PqqE, AlbA, the mycofactocin radical SAM maturase, and many others that share the peptide modification radical SAM protein C-terminal additional 4Fe4S-binding domain (TIGR04085). Members co-occur with a protein of unknown function that may be a chaperone or immunity protein and with a peptide that may have twelve or more cysteines occurring regularly spaced every fourth residue. These Cys residues tend to be flanked by residues with small side chains that provide minimal steric hindrance to crosslink formation by the radical SAM enzyme as in the subtilosin A system
AKSITFIVTDDCQLACKYCYQTGKNKNKRMSFETAKKAVDYILSGNKGFGEPSVIWDFIGGEPLLEIELI
DRICDYIKNRMIELNHPWFNSYRFSFSTNGVCYFEEKVQRFIQKNNQHLSISITIDGTKEKHDSCRVFPD
GRGSYDLVVSNAPLWLNQFPYASTKVTIAPADVPHVKESVTHLIDLGYNEVNINCVYEEGWQMGDDTVFE
DQLKKLADYILEHDMYNDYYCSFFSENFGHPLDCKLDNENWCGGGVMLAVDPDGIFYPCLRFAEYSLRQK
EAYSIGNVDDGIDRNRVRPFLKLDRRTQSTDECINCPVASGCAWCQGYNYDVAGTPTIYQRATYICDMHK
ARVRANIYF
>gnl|CDD|274991 TIGR04116, putative_cytoplasmic_protein, CXXX repeat peptide modification system protein. Members of this protein family occur strictly in the presence of a peptide modification radical SAM enzyme described by model TIGR04115 and some small peptide in which, for a stretch, every fourth amino acid is Cys. Cysteine residues usually are flanked by residues with sterically small side chains, as with many radical SAM-modified peptides. Many of the latter are recognized by model TIGR04114
IVGKVTEEERNEIEELFEKIASLEELIKILSNNPLEVEEFNELYEKVINDLGETKKKYQNWWDDIYEKYN
WEKNDGEKWIIDFETCTIYL
>gnl|CDD|274992 TIGR04117, Syntroph_Cxxx, Syntrophus aciditrophicus Cys-Xaa-Xaa-Xaa repeat radical SAM target protein. This model represents a paralogous family, in Syntrophus aciditrophicus SB, of peptides a conserved N-terminal region followed by ten to seventeen direct repeats of the sequence CXXX (see repeats model TIGR04114). The N-terminal region includes a hydrophobic patch that is not shared by most members of family TIGR04114
MMDEDSFKKKEIESAYGKTEKVDRRGFLITAGKIIIPTLGILGLSLMMLSPRPAAADCNSTCSGGCSGTC
QTGCTGSCSGTCHRTCSDICADSCS
>gnl|CDD|200369 TIGR04118, hypothetical_protein_CpapDRAFT_0305, modification target Cys-rich peptide, AC3_0185 family. Radical SAM enzyme family TIGR04115 is paired with a number of short peptides with multiple tandem repeats of Cys-Xaa-Xaa-Xaa (see TIGR04114). This family represent a peptide family with a TIGR04114-like region, although the repeat region is relatively short in this group
MKHLFSAKKISKVNKDVQGYMCSDCSGTCINGCANLCTSHCGNGCS
>gnl|CDD|200370 TIGR04119, Radical_SAM_domain_protein, CXXX repeat peptide maturase. This model describes a peptide maturase that works with, usually fused to, a radical SAM enzyme in a system that modifies peptides with multiple tandem repeats of CXXX sequences. This protein includes an iron-sulfur cluster binding region associated with peptide modification as described in domain model TIGR04085
NCILNVNKNDIKNLYDYIEKLFGKVNRINLNIKDVDKWNNFDLDLYKSQLAKISDYIADLYKKGIIKEIN
VITDRLMLKKMNNCDAGENSFTLAPNGKIYICPAFYFDDPDSYIGSLKDGININNNQLFKLENAPICKEC
DAYQCKRCVYLNKKMTNEVNVPSKIQCRISHIEREVSRNLQQKLRENKDVFFEYEINELDYLDPIDKLLK
>gnl|CDD|274993 TIGR04120, DNA_ligase, DNA ligase, ATP-dependent, PP_1105 family. This model describes a family of ATP-dependent DNA ligases present in about 12 % of prokaryotic genomes. It occurs as part of a four-gene system with an exonuclease, a helicase and a phosphoesterase, with all four genes clustered or at least the first two and last two paired. This family resembles DNA ligase I (see TIGR00574 and pfam01068), and its presumed function may be in DNA repair, replication, or recombination
KAFAALLDRLDYTPSRNAKLALLQDYFRTTPDPDRGWALAALTGGLPFRNVKPSLLRELAAERVDPVLFE
LSYDYVGDLAETIALIWPAPDETPDLGLAPWLSEVVLALRGTSKAELPALLAGWLDRLDPSGRFALLKLA
TGGLRVGVSARLAKQALAQLGGVDVDEIEELWHGLTPPYLPLFAWLEGGGERPDPAAAAPFRPVMLAHPL
EEPDLALLDPADYAAEWKWDGIRVQLVRRGGGRRLYSRTGDDISDSFPDLLEALPFGGVLDGELLVWREG
EVAPFADLQQRLNRKTVGKKLLADYPAFLRAYDLLEWDGEDLRALPFAERRARLEALVARLDPARLDLSP
LVPFGDWDELAALRAGPRAAGIEGLMLKRRDSAYLAGRPKGPWWKWKRDPLTVDAVLMYAQRGHGKRSSF
YSDYTFGVWDGDEGGRELVPVGKAYSGFTDAELKELDRFVRNNTIERFGPVREVEPELVFEVAFEGINRS
TRHKSGVAMRFPRISRIRWDKPAAEADRLATLEAML
>gnl|CDD|274994 TIGR04121, ATP-dependent_helicase, DEXH box helicase, DNA ligase-associated. Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H
SPFEAWFAARGWTPRPFQLEMWAAALEGRSGLLIAPTGSGKTLAGFLPSLIDLAGPEAPKEKGLHTLYIT
PLRALAVDIARNLQAPIEELGLPIRVETRTGDTSSSERARQRKKPPDILLTTPESLALLLSYPDAARLFK
DLRCVVVDEWHELAGSKRGDQLELALARLRRLAPGLRRWGLSATIGNLEEARRVLLGVGGAPAVLVRGKL
PKAIEVISLLPESEERFPWAGHLGLRALPEVYAEIDQARTTLVFTNTRSQAELWFQALWEANPEFALPIA
LHHGSLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVIQIGSPKGVARLLQRAGRSNHRPGEP
SRALLVPTNRLELLECAAAREAVAAGAVEGRPPPPGPLDVLAQHLLTLACGGGFDPDELFAEVRSTAPYA
DLTREEFDWVLDFVATGGYALRAYDRYRKVVRDEDGRYRVTDPRIARRHRLNIGTIVSDAMLKVRLRGGG
VLGEIEEYFISRLKPGDTFLFAGRVLEFVRIRDMTAYVRRAKGKDPKVPSWAGGRMPLSTQLAHRVREML
ADAAQWPSLPELRAVRPWLELQQRRSALPGADELLVETFPTREGHHLFVYPFEGRLVHQGLGMLLARRLE
RLGPIPFSFAANDYGFELLSAQPVDDEEALLDDLFSPDMLGDDLEAWLNASELAKRRFREIAVIAGLVEQ
GYPGKRKSGRQVQASSDLIYDVLRKHEPDHLLLRQARAEVLEGQLDLGRLGDALERIRGSRIVHKALDRP
TPLAFPLLVERGRERVSGEKLDDRLARMAAELEK
>gnl|CDD|274995 TIGR04122, hypothetical_protein, putative exonuclease, DNA ligase-associated. Members of this protein family frequently are found annotated as a putative exonuclease involved in mRNA processing. This protein is found, exclusively in bacteria, associated with three other proteins: an ATP-dependent DNA ligase, a helicase, and putative phosphoesterase
LLTFTPEGLYCPAGDFYIDPWRPVDRALITHGHSDHARWGHGAYLATPETLAILRLRLGEDIAIQTVAYG
ETIRINGVKVSLHPAGHVLGSAQVRLEYGGEVWVVSGDYKRAPDPTCAPFEPVPCDTFITEATFGLPVFR
WPPPAEEIAKILAWWAQNPEAGRASLLGAYALGKAQRVLALLRAAYDRPIYLHGAVENLTDLYREQGVDL
PPTRPVTEEGDKKALAGAIVIAPPSALGSRWARRFGDPVTAFASGWMQVRGRRRRRGVDLGFVLSDHADW
PGLLRTIKETGAEEVWVTHGYEDALVRWLREQGIDARPLHTVYEDE
>gnl|CDD|274996 TIGR04123, hypothetical_protein, metallophosphoesterase, DNA ligase-associated. Members of this protein family are an uncharacterized putative metallophosphoesterase associated with a DNA ligase, a helicase, and a putative exonuclease. It may play a role in DNA repair. Its system is present in about 12 % of prokaryotic reference genomes
ISIAGETLVLLPSGALYWPAERLLVVADLHLGKAAHFRARGIPLPPYDTRATLERLAALIQRYQPRRLIV
LGDLFHDRIGAERLTWEDFAAWRRLHAGRDWVLIEGNHDRLAPDPPEDLGGEVVDELRLGPLTFRHEPEP
GPGGFEIAGHLHPGARLRGRGRRLRLPCFAFDGNRLILPAFGAFTGGLNVDPEAGDRVFAVAEGRVVP
>gnl|CDD|274997 TIGR04124, archaeo_artE, archaeosortase family protein ArtE. This protein family is related to the predicted protein-sorting transpeptidase Exosortase (EpsH), with the Cys, Arg, and His putative active site residues preserved, but it is strictly archaeal and is not associated with any known PEP-CTERM-like target sequence. The immediate gene neighborhood in most genomes suggests RNA (methylase, cyclase) and cofactor (thiamine pyrophosphate) metabolism. The function is unknown. It is designated archaeosortase family protein ArtE
NKKNKSLFLIKFYVYFLVIYFILMYFEKYLIYIVAYQSYFILKLIIPDASLSGNLIYLPNNTIEVVEECT
GSFLIAIFLALIFSYSKSIKEFLIGLFFVLLAYFGNIIRIVLICYLANMYPENSELYHDIIGYIVILTLT
VILVLIYLKLIKK
>gnl|CDD|274998 TIGR04125, exosort_PGF_TRM, archaeosortase A, PGF-CTERM-specific. This family is an archaeal variant of the (normally bacterial) putative protein-sorting integral membrane protein exosortase, hence archaeosortase. In species a member of this family, its PGF-CTERM cognate sequence (TIGR04126) occurs at the C-termini of from two to over fifty proteins per genome. Those target proteins may not share homology to each other in regions N-terminal to the PGF-CTERM region
LLWLVSALFFLSALLPGRHRRYVGAGAWALFGLFWLLLVPHFFEINSYVEPILAILAVPFCLYTGYLLLN
GRDSLLTLTRAAAIMGLIYLPFETIPPLRNWLIETVADQTSWLLQLLGYPPTLVDWNTFYFNGFTVEIIL
ACTGIGSIAIFAGLIAAVEAPLRRKLRAFLVSVPVIYVLNLFRNVFIIIAYGEQWFPYVPALFGNTDPGR
VSFFIAHRVIAQLLAVVALIVIAYLVFKILPELGDLADDLLYLVTGEEYDLV
>gnl|CDD|274999 TIGR04126, hypothetical_protein, PGF-CTERM archaeal protein-sorting signal. This model describes a strictly archaeal putative protein-sorting motif, PGF-CTERM. It is the (predicted) recognition sequence for an exosortase homolog, archaeosortase (TIGR04125). In some archaea, up to fifty proteins have this domain as their C-terminal region, usually preceded by a Thr-rich region likely to be heavily glycosylated. The removal of this sorting signal may be associated with a C-terminal prenyl group modification in the halobacterial major cell surface glycoprotein, an S-layer protein
TTDGGPGFGVVVALVALLAAALLARRRR
>gnl|CDD|275000 TIGR04127, conserved_hypothetical_protein, exosortase F-associated protein. Members of this protein family are always found next to an exosortase/archaeosortase-like protein, and occur so far only in the flavobacteria, within the Bacteroidetes. Members do not have an obvious PEP-CTERM-like C-terminal protein sorting domain
KILLIGLLLVGLVLVRFFENDLFYDPLLDFFHSDYKNADLPEFDLGKLFANLSFRYLLNTLLSLLIIYIL
FKDKGIIKFSAILYLVVFVILIILFYILLHDFEEENYLLLFYVRRFLIQPIFVLLLLPAFYYQKKT
>gnl|CDD|275001 TIGR04128, hypothetical_protein_HMPREF0204_10576, exosortase family protein XrtF. Members of this protein family are exosortase-related proteins found always in association with a member of family TIGR04127, a small, hydrophobic, uncharacterized protein limited to the Bacteriodetes. Exosortases are proposed transpeptidases with a cysteine active site (3.4.22.-), but usually are associated with specific C-terminal target motifs (PEP-CTERM, PEF-CTERM, PGF-CTERM, etc)
IFRKYKPVLGFLLTFFGIYVVLTFIYQFYLNSGDDSGYYPDAITHMVAHQTESLLNAFGYDANIEPHPNE
PSMKLYVNNNYVARVVEGCNAISVIILFISFVLAFSKGWKKTLLFILAGSVLIYILNLFRIALLTIGLYY
YPEYEHILHGIVFPLIIYGSVFLLWLLWVKKFSK
>gnl|CDD|275002 TIGR04129, conserved_hypothetical_protein, CxxH/CxxC protein, BA_5709 family. Members of this protein family occur exclusively in the Firmicutes, in at least 50 different species. Members average about 55 residues in length, and four of the five invariant or nearly invariant residues occur in motifs CxxH and CxxC. The function is unknown
YYCCKEHIELAIDDYVDEYETAPDLEKLEEVKKLSTTCEYCSEPAVYLV
>gnl|CDD|275003 TIGR04130, L-fucosamine_synthetase, UDP-N-acetylglucosamine 4,6-dehydratase/5-epimerase. The FnlA enzyme is the first step in the biosynthesis of UDP-FucNAc from UDP-GlcNAc in E. coli (along with FnlB and FnlC). The proteins identified by this model include FnlA homologs in the O-antigen clusters of O4, O25, O26, O29 (Shigella D11), O118, O145 and O172 serotype strains, all of which produce O-antigens containing FucNAc (or the further modified FucNAm). A homolog from Pseudomonas aerugiosa serotype O11, WbjB, also involved in the biosynthesis of UDP-FucNAc has been characterized and is now believed to carry out both the initial 4,6-dehydratase reaction and the subsequent epimerization of the resulting methyl group at C-5. A phylogenetic tree of related sequences shows a distinct clade of enzymes involved in the biosynthesis of UDP-QuiNAc (Qui=qinovosamine). This clade appears to be descendant from the common ancestor of the Pseudomonas and E. coli fucose-biosynthesis enzymes. It has been hypothesized that the first step in the biosynthesis of these two compounds may be the same, and thus that these enzymes all have the same function. At present, lacking sufficient confirmation of this, the current model trusted cutoff only covers the tree segment surrounding the E. coli genes. The clades containing the Pseudomonas and QuiNAc biosynthesis enzymes score above the noise cutoff. Immediately below the noise cutoff are enzymes involved in the biosynthesis of UDP-RhaNAc (Rha=rhamnose), which again may or may not produce the same product
MFKDKILLITGGTGSFGNAVLRRFLDTDIKEIRIFSRDEKKQDDMRKKYNNSKLKFYIGDVRDYRSILNA
TRGVDFIYHAAALKQVPSCEFHPMEAVKTNVLGTENVLEAAIANGVKRVVCLSTDKAVYPINAMGISKAM
MEKVMVAKSRNVDSSKTVICGTRYGNVMASRGSVIPLFVDLIKAGKPLTITDPNMTRFMMTLEDAVDLVL
YAFEHGNNGDIFVQKAPAATIETLAIALKELLNAHEHPVNIIGTRHGEKLYEALLSREEMIAAIDMGDYY
RVPPDLRDLNYGKYVEHGDRRISEVEDYNSHNTQRLDVEGMKELLLKLPFIRALRAG
>gnl|CDD|275004 TIGR04131, conserved_hypothetical_protein, gliding motility-associated C-terminal domain. This model describes a protein homology domain unique to, and greatly expanded in, the Bacteriodetes. Species in this lineage include several, such as Cytophaga hutchinsonii and Flavobacterium johnsoniae, that exhibit a poorly understood rapid gliding phenotype. Several members of this protein family are found in operons with other genes whose loss leads to a loss a this motility. Proteins with this domain frequently pair with members of family TIGR03519, whether one such pair or many occur in a genome. More than 30 members may occur in one genome
IGYPKFFTPNGDGYNDTWNIIGLENYPNAKIYIFDRYGKLLKQLSPDSIGWDGTYNGKPLPSSDYWFKLE
YEDGRIFKGHFSLKR
>gnl|CDD|275005 TIGR04132, intra_fol_E_lig, putative folate metabolism gamma-glutamate ligase. This protein family is related to CofE, a gamma-glutamyl ligase of coenzyme F420 biosynthesis. However, it occurs in a different gamma-glutamyl ligase context, polyglutamylated tetrahydrofolate biosynthesis-like regions in two widely separated lineages that both occur as intracellular bacteria - Chlamydia and Wolbachia
MKVTPIKTRRIECHDDLYEILEESLPELRERSIVAITSKIVSLCEGAVVDKTACSKEELIKQEADAYVFV
EHYGIYLTKKDGILIPSAGIDESNGNEYYVLYPKDLLKSANSIGNWLKNFYHLKHLGIIITDSHTTPMRR
GVTGLGLCWYGFSPLYSYVGKPDCFDRPLKMTQSNLLDALAASAVLCMGEGDEQTPLAIIEGAPKITFHS
SPTTQEEESSLKIDETEDLYGPLLMSVAWEK
>gnl|CDD|200384 TIGR04133, coenzyme_PQQ_synthesis_protein_E, radical SAM enzyme, rSAM/lipoprotein system. Members of this protein family are radical SAM enzymes with an additional 4Fe4S cluster-binding C-terminal domain (TIGR04085) shared with PqqE and many other peptide and protein-modifying radical SAM enzymes. All members occur in the context of a predicted lipoprotein that usually is encoded by an adjacent gene
LRKRLALEAFRRYRHNEIKEHPLRYLFWECTLRCNLACLHCGSDCKKDSSVPDMPLEDFLKVLDSITPHV
DPHDVLVIITGGEPLVRPDLEEIGRELYRRGYPWGMVTNGLALTEERLTSLLNSGLRSITISLDGFEDSH
NWLRGNPHSFERALNAIRLIAKTPELTFDVVTCVNRKNLGQLPEFKELLIKLGVKRWRIFTIFPVGRAAE
DPELQLTDEEFRQVLDFIRDTRKEGRINLSYGCEGFLGNYEGEVRDHPFFCRAGVSVASILCDGSISACP
SIRSNYHQGNIYRDDFWDVWQNRFQPFRDRSWAKKGECADCKYWRYCEGNGMHLRDDEGELLFCHLKRLE
>gnl|CDD|200385 TIGR04134, hypothetical_protein, putative lipoprotein, rSAM/lipoprotein system. Members of this family are Bacteroidetes lineage putative lipoproteins that always occur in pairs with a radical SAM enzyme, TIGR04133, from a branch of the radical SAM superfamily in which many members perform peptide or protein modifications. In some members, the region distal to the Cys of the putative lipoprotein cleavage motif is duplicated
KVLRLLNRLLSGFLGLLGFASCDEEGGEIPVEYGTPYAKYEVKGKVTDEEGEPIEDIQVIVKRKYSGDDR
SWVYLTDTVYTDANGEFQIENEVTFGFNKYRVIAEDIDGVKNGRYASDSVDVKMESDDFKGGSGWYEGSD
KKEIDIKLKK
>gnl|CDD|200386 TIGR04135, hypothetical_protein_CUS_2485, Cys-rich radical SAM target, FibroRumin family. Members of this protein family are cysteine-rich small peptides, about 52 amino acids long, that are proposed targets for modification by a radical SAM enzyme. Known occurrences are as tandem gene pairs Fibrobacter succinogenes subsp. succinogenes S85 (missed gene calls) and in Ruminococcus albus 8
ISADTEAYMEMFGNIADEFMAAAACACVACNGCKCACKCRASKEEDDGEFEW
>gnl|CDD|200387 TIGR04136, radical_SAM_domain_protein, radical SAM peptide maturase, FibroRumin system. Members of this protein family are radical SAM enzymes proposed to act on small, Cys-rich peptides encoded by tandem gene pairs. Members occur in enzymes Fibrobacter succinogenes subsp. succinogenes S85 (genes for their target peptides missed) and in Ruminococcus albus 8. This enzyme family is similar in sequence to the SCIFF (Six Cysteines in Forty-Five) system maturase (TIGR03974)
FSRFTHKFEVGDAVALYHSLRMKPVFLSRDKFEQLETFIAESCCNQISDAPEEIAKEVAELAKWKILIDS
EDEDDKMLRFVKSKLPEPAISICYFILSEQCNLACKYCFLGNNDKEKRHNFAKELMSKEIADKAIEFFIK
QLEASELDAEDNKAAIIFYGGEPLMNFETLKYVAEKFNSLKSEEKCLENAEFSMVSNGLLLSEERIIELR
DLGVSIAISIDGCDEAANAMRVDLAGNIVFPKILETLDIAKELGVNVSLSITLSEETIKDQQDVIDLIDE
YGIKGLGFNIMMGDDRFPLPADYNDKAAQFIIDEFKELREIGIYEDRIMRKLKAFAKAQVYFSDCAATGA
GQIVIAADGAVGICHGCLFDKKYFNSCIDDDDFNAIDDPTFIEWNHLSPIEKDECQDCEALGICGGGCPI
NAMGEHEGNTIHSIDERFCVHAKKTLEFFIGDLHRLIT
>gnl|CDD|275006 TIGR04137, hypothetical_protein, Chlam_Verruc_Plancto small basic protein. Members of this protein family are commonly found next to markers of rRNA processing such as YbeY. They are extremely lineage-restricted, in the Planctomycetes and Chlamydiae/Verrucomicrobia group. Since classification is based on rRNA molecular phylogeny, this provides additional support for a role in rRNA metabolism. This small protein, about 50 amino acids in length, is rich in basic residues, a third line of support for rRNA interaction
MSIHKSLKVKGKLGRKRNVLKRFERIELLKKRGRWKEGDSVLGLPKTKVE
>gnl|CDD|275007 TIGR04138, conserved_hypothetical_protein, Verruc_Plancto-restricted protein. Members of this protein family are extremely lineage-restricted, occurring exclusively in the Planctomycetes and Chlamydiae/Verrucomicrobia group, although not in Chlamydia itself. The function is unknown; the lack of invariant residues other than a single Phe suggests an ancient, conserved, non-enzymatic role
AVSEIVRRDPRYAREAYAFVREALDFTQKRLPKQRTKARRHVSGQELLEGLRDYALKQFGPMALTVLNEW
GVRKTEDFGEIVFNLIEYGLLSKTERDSREDFDDVYDFEEAFDEPFLPARTK
>gnl|CDD|200390 TIGR04139, hypothetical_protein_HMPREF0765_0482, putative peptide modification target, TIGR04139 family. This model describes a rare family of small putative polypeptides, including three encoded in tandem in Sphingobacterium spiritivorum ATCC 33300, in the vicinity of a TIGR04085 protein. This pairing is conserved in Chryseobacterium gleum ATCC 35910, Kordia algicida OT-1, and other species. TIGR04085 describes a C-terminal additional 4Fe4S-binding domain in PqqE and other radical SAM enzymes that seems to be a marker for peptide modification, and the family modeled here is a candidate modified peptide precursor
LNGMKSFSSLENKKLDLNVLGGVAGSRGGGKYKYVGSNFLNAYGCRDVDMYDSGGRIMYRGWDKSG
>gnl|CDD|275008 TIGR04140, hypothetical_protein_TERMP_659, TIGR04140 family protein. This model represents an uncharacterized small archaeal protein
MRRIIKTAIPPEELEIIAEKSGAEVRIKLLEVEPYFGIPRTEVVIEGEEEEIEKFMEKLRLARAGG
>gnl|CDD|275009 TIGR04141, conserved_hypothetical_protein, sporadically distributed protein, TIGR04141 family. This model describes a sporadically distributed conserved hypothetical protein in which complete members average over 500 amino acids in length, although matching sequences frequently are truncated or broken into tandem ORFs. Regular co-clustering with known markers of mobility (integrases, transposases, phage proteins, restriction enzymes, etc.) suggests this family also is part of the mobilome. The function is unknown
LSIYLLKEGVTDFEALLKESARLTKEYPLDGLGLEAKLYVKKSDPKPPKWAKLFSRLTGQEIPDLKNSSP
GAVLLVKVDGRTFAITFGYGRHLLNDEAIERDFGLRVALNSLDPDKLRSLDKATLDDVARNTRSQSSRGS
DVSEFGVDSDRDILRSVTGVPEDDVLGRHVTGGDSLSITLEIDLEDLPADLEEILERYRSDDYKENFPWV
DNIRPVRDKELIEELDGELADALNSNKDERIWLAVPEIVDYEDASGFKFTGRSGRAATHPDLDLEDYLEY
LGGKGAGITIEALKRGRIHACFDDDEPEIKRWSLYRCLVAEITLEGERYILSDGQWYRIDKDFVEEVDDY
FERIPDPTSISLPPWNGDREGDYNERVAAADGDYLLLDKKLISPGGHRSKIEFCDLLTPDKELIHVKKYG
SSSVLSHLFSQGAVSAELLLSDPEFRKKLNEKLEALYGLAALNDRPKPRPYRVVFAIATKKGGELPLDLP
FFSKVNLRRAARTLRSLGFKVELAKI
>gnl|CDD|200393 TIGR04142, PCisTranLspir, putative peptidyl-prolyl cis-trans isomerase, LIC12922 family. Members of this protein family have a known crystal structure (3NRK) showing similarity to the peptidyl-prolyl cis-trans isomerase SurA. Members are found in Leptospira species next to an uncharacterized radical SAM enzyme and a cytidylyltransferase family protein
ESLNRVIATVGTVSISELDLDDATEKYNRLQKHLKHEDYRKSFRTRIIDFLIDRAIVDVVAEEESIQVNE
QRVDSEIEKRMEVMGITNRKQFEKTMETSSGMPFELWVTELPYQIKKGQLLQLKIAVPPPNEQEIRSWYN
QNKDKVGFEIRYRIISIAPENDSIQEENRLYKEVSEIRKSILADPSSFALIAGSPRNDPALRARRGMVEW
ISSFDLYKYSKITATIAAPLPNGGVSEVFRDERKRYCILKIEGKRPTPMENLRGGIQNILYRDKEEDTFH
RWLKESRAEIPIQIFDEAYRKENKIPLKEETFHLD
>gnl|CDD|200394 TIGR04143, VPxxxP_CTERM, VPXXXP-CTERM protein sorting domain. This C-terminal protein sorting domain is detected, so far, in Methanohalophilus mahii DSM 5219 (five members) and Methanohalobium evestigatum Z-7303 (nine members). This domain resembles the PEP-CTERM, PEF-CTERM, and PGF-CTERM domains of other exosortase/archaeosortase systems. Member proteins co-cluster with a variant member of the exosortase/archaeosortase protein family, and represent a boutique second sorting system in these species
VPTANPLLLVGVLGIAGVLFLRRRQ
>gnl|CDD|200395 TIGR04144, archaeo_VPXXXP, archaeosortase B, VPXXXP-CTERM-specific. Members of this protein family are found so far in Methanohalophilus mahii DSM 5219 and Methanohalobium evestigatum Z-7303, along with five and nine proteins, respectively, with the VPXXXP-CTERM protein sorting signal (TIGR04143). In these species, this boutique system represents a second exosortase/archaeosortase-type system
IAKFAALYIFYIGIFTGLYIFFKDDLEFFRNITADGFSAILGLFGIQNSVDENIIHFENGIIALKVIDEC
TGIYELLVYSGCVLAYSTTFDKKIMGIAFGVPAILGINMVRLVCLAFVGLWFPAIFDYVHYYLWQVTLIL
IIVLVTLIWIEKVVKR
>gnl|CDD|200396 TIGR04145, hypothetical_protein, Firmicu-CTERM domain. This C-terminal domain is found only in the Firmicutes, where its presence is sporadically distributed. Proteins with this domain are most conserved in the C-terminal region, where the pattern of ending with a transmembrane domain resembles both the LPXTG (sortase target) and PEP-CTERM (exosortase target) domain structures. However, members occur exclusively in the presence of an exosortase-like protein XrtG (TIGR03110), a putative glycosyltransferase (TIGR03111), and a 6-pyruvoyl tetrahydropterin synthase-related protein (TIGR03112)
ITLSNPNLGNQGITIAGGSTGPYIGAGIAVVIAGGGVFKYRRKRR
>gnl|CDD|275010 TIGR04146, Geranylgeranylglyceryl_phosphate_synthase, phosphoglycerol geranylgeranyltransferase. This enzyme, known also as GGGP synthase and GGGPS, catalyzes the stereospecific first step in the biosynthesis of the characteristic membrane diether lipids of archaea. Interestingly, the closest homologs outside this family are not the functionally equivalent enzymes of other archaea, but rather functionally distinct bacterial enzymes
WKKWRHVTKLDPDKKITPKEIAEIADSGTDALMLSGTQNVTKENVAELLDMVKEYGLPLVVEPAGPSAVR
FDGIDYLFVPSVLNTKDPEWIVGKHKDWVRNYDNIVWDKVIPEAYIVLNPNSAVGRVTKAVCGLTPEEAA
AYAEVADRYFKFPIVYIEYSGTYGNPELVKAVKEALDNARLYYGGGIDSREKAAEMAKYADTIVVGNAVY
EKGIEVLKETV
>gnl|CDD|275011 TIGR04147, Geranylgeranylglyceryl_phosphate_synthase, phosphoglycerol geranylgeranyltransferase, putative. In most archaea, phosphoglycerol geranylgeranyltransferase (EC 2.5.1.41), also known as GGGP synthase and GGGPS, catalyzes the stereospecific first step in the biosynthesis of their characteristic membrane diether lipids. However, some groups of archaeal GGGPS homologs are more closely related to certain bacterial proteins than to each other. This family represents the putative GGGPS family as found in the Halobacteria
PWDDWDHILKIDPDKSLVDGETFEDVCATGTDAIEIGGTLDMTEEKMQRVVDACAEYDVPLYQEPSNPAV
VVESDALDGYLVPTVLNAGDPFWITGAHKEWVRIDDLDWDRTATEAYIVMNPEASVAEYTEADCDLTADD
VAAYAEVAERMLGQEIVYVEYSGTFGDPKKVAAAAEALDEATLFYGGGIHDYESANTMAAHADTIVVGDL
VHDEGVDAVRETVEGAKDA
>gnl|CDD|200399 TIGR04148, conserved_hypothetical_protein, radical SAM peptide maturase, GG-Bacteroidales family. Members of this protein family are radical SAM enzymes (pfam04055) with the additional C-terminal region (TIGR04085) that is frequently a marker of peptide modification. Many members of this family are found in the vicinity of one or several ORFs encoding short polypeptides with a Gly-Gly motif (common for bacteriocin leader peptide cleavage), followed by a Cys-rich patch and then poorly conserved sequences
FGDITESDIKQELANLRQLTFEVTDACNLQCKYCSYGDLYNNYDERENKNIDFDNAKTLIDYLFSLWESK
YNTSVKNTVTIGFYGGEPLLNMDFIKEIINYIEKLHIDGLNFHYNMTTNAMLLRKYMDFLVENDFHLLIS
LDGDKYNDGYRVFKNGKSSFDKVFDNIKYLKNKYPEYFDKNVNFNSVLHNRNSVEEIYEFIYTEFGKIPS
ISELNTNGIAPEKKEEFEKMFHSKTQSSIESLTKDSNYKQELDLESPNFKTLTKFLFHYSGNVYRDYVDL
FYGDKNVKYIPTGTCIPFSRKIFVTVNGKILPCERIGQQYALGKVTDGKVILDCDAIAKKYNKYYNKIEN
QCKHCYLKRSCSQCIFYLKNLDKQPVCPNFTSREDFEKYLANYISYLEKYPDDYFRIMKEI
>gnl|CDD|275012 TIGR04149, predicted_protein, natural product precursor, GG-Bacteroidales family. Sequences in this protein domain family include a leader peptide region, up to and including a Gly-Gly cleavage motif, and about 15 additional residues, usually Cys-rich, from a family of predicted ribosomal natural product precursors. Many of these are associated with peptide-modifying radical SAM enzymes. The core region, up through the diglycine motif, resembles and contains some overlapping hits with the bacteriocin precuror leader peptide region modeled by TIGR01847, but is longer with an extreme N-terminal region with consensus sequence MKKLKKLKL [Cellular processes, Biosynthesis of natural products]
MKKLKKLKLNKLSKNELSEREMKRLKGGYYCGCGCEYNGSSGN
>gnl|CDD|275013 TIGR04150, conserved_hypothetical_protein, pseudo-rSAM protein, GG-Bacteroidales system. Many peptide-modifying radical SAM enzymes have two 4Fe4S-binding regions, an N-terminal one recognized by Pfam radical SAM domain-defining model pfam04055 and a C-terminal one recognized by TIGR04085. Members of this protein family occur in cassettes with such a radical SAM family (TIGR04148) and with a peptide modification target (TIGR04149). Surprisingly, members of this family show full-length homology to each other, with several scoring at least borderline hits to both pfam04055 and TIGR04085, and yet differ in the presence/absence of a signature CX(3)CX(2)CX(9)C motif. Instead, members are best-conserved in the TIGR04085-like C-terminal region. Therefore, this protein family is designated a pseudo-radical-SAM protein, which likely works in partnership with a TIGR04148 family protein
WFYIEPYVFIWIKNKKALLYNTLNGKGYIFSENEKVITILEQLLDEENLYSVLLDEENLRDNEVKEFVSE
LREKFMGDIIEVSLFPGKPIIILPILNLQRDVERLKEFKKALLGENILNNLHEITIYLDGTCNSECPYCS
TCYKQILCCTESNQVLDIDKLKSILDQLSYNNIYRINLFGGNIFKYPYLRELLSLLEQYSGKKQLYLDYK
NFYESDLKKLLNNPNFSIKILVHFPVDEELLNSLIALLKDRDPVEWIFIVTSENEYEEAEKIIEKYNIDN
VQIRPFYTGDNIDFFEEYVFLDKEDILSTKLTKKDIFAHQKLNTNFFGKLTILPNGDVYANVNHSSIGNI
QDDSIKEIVYKEIEEGTSWLRIRNQLEPCCDCVYQYLCPSPSNYELAIGKNNLCHVK
>gnl|CDD|200402 TIGR04151, eight_transmembrane_protein_EpsH, exosortase C, VPDSG-CTERM-specific. Through in silico analysis, we previously described the PEP-CTERM/exosortase system (). This model describes the exosortase subtype specific for the VPDSG-CTERM variant (TIGR03778) of PEP-CTERM. Systems are found, so far, in Verrucomicrobiae bacterium DG1235 (twenty) and bacterium Ellin514 (two). This system may coexist with other system variants [Protein fate, Protein and peptide secretion and trafficking]
PRSEAKAASNHDAENEGKGFLPPLRLSYTLIGAIIALSACFGKPLLHLAEFALKSDLDSHILLIPFVSLY
LVRLEKQGPTGASEPARGLAILPALGGAALLAGYLFIEREGDPPAGDDQEALIFFAGGAYVLFFIGACCA
CAGKDAVRAHAFPICFLLFLVPFHLELKIAIETFFQHASADAADLLFKTSGTPFFREELIFELPGIALEV
APECSGIHSSLILFITSFIASYLFLKKPWKRAVIIFAVIPLGIARNGFRIFIIAELCVHIGPEMIHGAFH
HRGGPPFFALSLIPFFALLILFKRSERKS
>gnl|CDD|275014 TIGR04152, hypothetical_protein, exosortase D, VPLPA-CTERM-specific. This model describes a variant sub class, exosortase D, of protein sorting enzyme (see parent exosortase model TIGR02602), specific for the VPLPA-CTERM variant (TIGR03370) of the PEP-CTERM protein sorting signal [Protein fate, Protein and peptide secretion and trafficking]
LARWWGTPEYSHGPLIPFVSLYLFWRKLRDPLASTPSTDSWPGVLLLILALALGLLGELGGIEDIVYYSL
IIWVGGVLLTSFGWRKLRHVGFPVVLLLFMLPLPQFLYNKLTTGLQLVSSELGVWFLQLLGVPVYLEGNI
IDLGVYKLQVVEACSGLRYLFPLLSFSYLVAYLYRGPLWHKVLLFLSAIPLAVFMNSLRIAVTGVLVNYY
GPEVAEGFLHDFEGWVIFLACIAILFGVAWLLRKLTPRPKSLGDAFDLDSSGLGTQAGRILGIRPSRALI
AALLLLLASALALQFLPNSEPVAPERESFDLFPLRVGEWSGVRQPLDQDVLDILGADDYVIGSYRNPEDQ
APVGLYMAYYEAQTKGEGIHSPEVCLPGGGWEIESLEIIELSMPGYGTFRVNRAVIEKGGRRQLVYYWFE
QRGRRLTNDYQAKLYLFWDALTRGRTDGALVRVITPIYPGESEADAEARLQDFMAELLPPLPRFLP
>gnl|CDD|275015 TIGR04153, hypothetical_protein_L8106_04486, cyanosortase A-associated protein. Members of this protein family are found exclusively in the Cyanobacteria, usually usually encoded next to and in at least one case fused to a gene encoding cyanoexosortase A. Note that family TIGR04533 shows a similar relationship to cyanoexosortase B (TIGR04156), and no EpsI is found
STPFLFPQQVPLSGWQLIDSTPLVLQKGDKPGKIPGQLYRYQQNNLTLEIEMRYVKYTHGNIEQLLRKYQ
PSPSKTIFPQVKHQKGVGYYGLFEDENRAYLSACINPRGGSTVTEEQFIQNRYLYDWRLSRTLPWLLGQE
DLRDHRCLWTHLSIPISNDKSPEETYQILESAWLSWYQWWQPRFPS
>gnl|CDD|275016 TIGR04154, archaeo_STT3, oligosaccharyl transferase, archaeosortase A system-associated. Members of this protein family occur, one to three members per genome, in the same species of Euryarchaeota as contain the predicted protein-sorting enzyme archaeosortase (TIGR04125) and its cognate protein-sorting signal PGF-CTERM (TIGR04126)
IPVLLVVMLFALWIRILPYGNFISDGSVRFSGNDPWYHLRRIEYTVHNFPNTLWFDPYTNYPYGTEVGWG
PLFDQLGATLALIVGLGAPSRETIETVAAFLPPLLGALTVIPVYFIGKRLGDRKTGLLAAFLLAVLPGQF
LYRSLFGFVDHHIAEVLFSTLAVLAFILALAVAREHKPSLEDLDTLKKPLLYAVLAGIALGLYLLTWPGA
VLFAGIVGVFTLVQFILDLFRGRSPEYLAIVGAVTFAVAALLVLPFGFTLGFSATYYSLFQPLALLGVAL
GAVFLAGLSRFWERKDLPRYYYPAAVAGLAALGLAVLALLLPDLFSLIINGLRFFFGRTGTALTIAEAQP
LFSTGGGFSLAPAWSNFGLGFLLAIAGLALLLYRLLRKYRPEELFLLVWSLFILYATLTQVRFEYYLAVN
VAVLSAYLLGWVLDFAGRLPLRRSLKNKKDIETYQVSRIAVILLLIVILVLAYPSIWATAAQSTGPGGPN
QDWVDALEWLKNNTPDTGLDYYGIYEEKDDFPYPEGSYGVMSWWDYGHWITYIGERIPNANPFQQGVPGA
AAFFLAQSEEEAEEILDKLGTRYVMTDVEMATGKFYAMAVWLAGEDPSDYYMPYYQQGPQGTGYGTVSVP
TQRYYETMEARLHLFDGSGLEPYRLVHEYETPSASEGSYPGVTNAEQMNASEAQATAESYNNMPAAGQRV
PALQHYRLVHESPTSATSSGTRDIRYVKIFERVKGATITGTAPGETVTAEVELTTNTGRTFTYRQQSVAD
ENGTFEFTVPYSTTGTDYDVKATGPYRITSGGTTKEVQVTEEAVLGG
>gnl|CDD|275017 TIGR04155, hypothetical_protein, PEP-CTERM protein sorting domain, cyanobacterial subclass. This domain model describes a subclass with family TIGR02595 of PEP-CTERM protein sorting signals associated with bacterial exosortases. This subclass is restricted to Cyanobacteria, including the genera Cyanothece, Nostoc, Trichodesmium, Lyngbya, Arthospira, etc. This PEP-CTERM subclass features strongly conserved residues within the transmembrane region, including a Gx4GxG motif. Model TIGR03763 describes a corresponding cyanobacterial form of exosortase found in most species with this domain
VPEPLTILGTGTALGFGTLFKRKLS
>gnl|CDD|275018 TIGR04156, eight_transmembrane_protein_EpsH, cyanoexosortase B. This model describes a cyanobacterial-restricted form of exosortase, associated with a PEP-CTERM domain subclass described in model TIGR04155. This is one of two such cyanoexosortases, either of which is sufficient to accompany TIGR04155 family members. The cyanoexosortase is TIGR03763 [Protein fate, Protein and peptide secretion and trafficking]
LLNVAIIALLVLLYAPLLLHWYDGWLNKSISIEHEYFSHGIIGLPFAAYIAWTNRQKWQRLPNKSHPLGA
FLLGIGGVFYLSGISELVNLSFPIILAGLCLWLKGIPGLKLQGFPLLLVFLATPNAIPYLITPYTLPLQS
FIAGVAGFILNQFGMDVTVDGIYLYVNGRIVEVAPYCAGLKMLFTSLYVSLMLLYWTGALSSRRKTIFFL
SSAVLISVIANIIRNTLLTLFHGTGQDAAFKWLHEGWGGDLYSAGMLGLLVPLLNWMDNYFSNSKESEEE
>gnl|CDD|275019 TIGR04157, hypothetical_protein_BACCELL_00210, glycosyltransferase, GG-Bacteroidales peptide system. Members of this protein family are predicted glycosyltransferases that occur in conserved gene neighborhoods in various members of the Bacteroidales. These neighborhoods feature a radical SAM enzyme predicted to act in peptide modification (family TIGR04148), peptides from family TIGR04149 with a characteristic GG cleavage motif, and several other proteins
HIYIINDYSRASQYGIGTYIKQLINCLRQSSSIHLTVVELRSEVEEFEECEVDGVRYLKFPKPYSNNARE
LIQVYYRNIAYLLKLYIPDSENNIFHFNYLHHYKLAKELKKIFSKCKIILTIHYFDWCFKLKGNVSLLRS
ILRKEETKNELEKLIKEEFEREKEMFQLADRVICLSQYTQNLLYEDYGIPKEKIVVIYNGLTDEAIYLSE
VERKKLRKKLGFSEDEKIILFVGRLDEIKGVDYLIEAFKIVLKKDPNCRLVIVGDGDYSRYLQECKKIWS
KITFTGKLDKEKLYELYQIADVGVLPSFHEQCSYVAIEMMMHGLPLIGTTSTGLSEMIEDGLNGYKIPIK
EYRDYVELDKKELVQKLLKLLSSSDEAKQMGKNARRRYLEKYSLEVMRENMKSLY
>gnl|CDD|275020 TIGR04158, rSAM_MIA_synth, 3-methyl-2-indolic acid synthase. Members are a radical SAM enzyme that converts L-Trp to 3-methyl-2-indolic acid synthase through a complex rearrangement. This enzyme is closest to ThiH, which also does a complex rearrangement, among other characterized radical SAM enzymes
RAEAATVDTRAVLALAEGEEPAESRAAVALALWEDRSIGTAELQAAAEARCGARRPRLHTFVPLYTTNYC
DSECKMCSMRKGNHRLDRKFSGRKEITEQLEILYHHEGVRGVGFLTGEYEDKHTRLASAFRIGWAIRTAL
DLGFERVYFNIGSMEQDEIDVLGEWIGREDPVTMCVFQESYDRETYRRFMGKTSVGVPKADFDRRVVSFD
RWLDAGYRYVNPGVLVGLHDDLSAELVSLVAHGDHLRSRGATADLSVPRMRPAMKSRDTTRVGDDDYLRL
MSVVAFTCPEQRLVLTTREPQEFQDVALGLAGVISPGSPDVAPYRAGCEARNDEKSSQFLVADLRRPRHI
LGRIEASGTPVDHFVNPA
>gnl|CDD|200410 TIGR04159, conserved_hypothetical_protein, methanobactin biosynthesis cassette protein MbnB. The first characterized methanobactin is made from a ribosomal precursor in Methylosinus trichosporium OB3b. Two additional species with homologous precursor peptides (family TIGR04071) are Azospirillum sp. B510 and Gluconacetobacter sp. SXCC-1. This model describes a clique of related sequences, domain or full-length, that occurs always and only next to a methanobactin precursor. The model excludes some close homologs from species where no similar precursor can be found
LIDEGHIDYVELLIDNFLHLPPEEIAKKFDCPVAFHIMQSKFLERDEEELKYLSSRLRQMIDAMQPLYVS
DHIALFTHNGRNLYHLAEIDY
>gnl|CDD|275021 TIGR04160, hypothetical_protein_MettrDRAFT_3896, methanobactin biosynthesis cassette protein MbnC. The first characterized methanobactin is made from a ribosomal precursor in Methylosinus trichosporium OB3b. Two additional species with homologous precursor peptides (family TIGR04071) are Azospirillum sp. B510 and Gluconacetobacter sp. SXCC-1. This model describes a clique of related sequences, domain or full-length, that occurs always and only next to a methanobactin precursor of the Mb-OB3b type. The model excludes several Pseudomonas proteins whose function is unknown, which likewise are in model TIGR04061, but which diverge toward the C-terminus
EDILLELAGAAAARWAIIDRDIDACGIAIGSRGIAGAATVGAKCDAIDCQLEEIQEIEFEADLPLEDDEF
GYFLIFDFEIDHFPGWRPI
>gnl|CDD|275022 TIGR04161, conserved_hypothetical_protein, VPEID-CTERM protein sorting domain. Proteins belonging to this family are small, 80 to 120 residues, including a signal peptide, a central low-complexity region, and this roughly 31-amino acid extreme C-terminal region. Members occur paired with a variant form of exosortase. Species include Ruegeria sp., Phaeobacter gallaeciensis, Roseovarius nubinhibens ISM, and two in Methylobacter tundripaludum
VPEIDASSGTLALAAVAAALLLAWELYRRRR
>gnl|CDD|200413 TIGR04162, CAAX_amino_terminal_protease_family_protein, exosortase E/protease, VPEID-CTERM system. Members of this protein family are fusion proteins of exosortase (N-terminal) and a CAAX prenyl protease domain (C-terminal). Members are restricted to the alpha Proteobacteria. The variant C-terminal protein sequence VPEID-CTERM occurs only in these species, often adjacent
VLLLLAVAELAAIMLAFQLFASVECRNTSAETACRALRSLPLRVLFLLAALGLYTWARPNLWHALAHLAA
SAPGRRLRWAALHVAGLVLILVPLARLPLAQLNAQFSQALPLFLAGGALAALGALLWLLPLRAWKRWLRG
NGAFLPLVVLVAALLPDLAEATGPLWGENRALTRVTFQGVAGVLALTGTEVVTDPAERIIGTKGFLVEIA
SSCSGVEGFALVAVFMALYALLMRRTLRLTRYWLVLFPVALLLSWLFNVLRIAVLIMIGANISPELAVNG
FHSYAGWLMFTLLALAVLAIVHRMAFLHRGPEKPGSAPGLPLRADPLAARIVPFILFMLSGVLVQSLWAN
PAQGYPLRAAFMAAGLWLFWPALRALDWRPGPADLLTGAAVAAMWILSSAPETTASLTQAPDPLWILCRV
LGTTLLVPVIEELFFRGYLLERLAGTSGRAPWRVLLALAVSSLLFALLHDRWIAGAAAGVIFGALYLRRG
RLGDAVLAHMVANAIIAAVAIATGNWALI
>gnl|CDD|200414 TIGR04163, rSAM_cobopep, peptide-modifying radical SAM enzyme CbpB. Members of this family are radical SAM enzymes that modify a short peptide encoded by an upstream gene. A role in metal chelation is suggested
LQELEIGHPRYVAVLDPDSAFWALVEKDELERALDAGALVGDYRARADAFLEEMDALRFGLKPSAVYFNP
TERCNLNCSYCYIPEEMRRSGKHMSPEELEEALGRLKEYFCTVMPEGRKPQIIFHGAEPLMNKDAIFAAI
DAFRDDFRFGIQTNGTLLDDEAAEFLTSRGVGIGLSLDSPTAEVADRTRRTWSGKGVYDAVVRAIEKLKG
YASFNVITTVTRENLQHLPAMVDFLHAGEVPTCMLNPVRCTQPGGRDLKPPDGVMAKYYLKALDRAHELY
QETGRKLVVANFANILIGIVAPTARRLMCDISPCGGGRCFFALSADGSLFPCSEFIGLEEFKGGNLFTDD
VSSVLESAAFRAVTGRKVEQIEPCRTCAIRHFCGSPCPAEAHEMNGGMNRIGAYCEFYKEQVRYAFRLIA
DGKADDYL
>gnl|CDD|200415 TIGR04164, hypothetical_protein_Pcar_3203, modified peptide precursor CbpA. Members of this family are short peptides predicted to reach mature form after modification by a radical SAM enzyme (TIGR04163)
VIAYRKSCKADGTGLSHYVLMDKKK
>gnl|CDD|275023 TIGR04165, conserved_hypothetical_protein, Cys-rich peptide, TIGR04165 family. Members of this small peptide family occur strictly in a subset of archaeal methanogens. Members have four invariant Cys residues in two Cys-Xaa-Xaa-Cys-Gly motifs and may have other Cys residues as well. At least two members occur next to family TIGR04083 radical SAM enzymes predicted to act in peptide or protein modification
MKLEELLKKCPKCGCKDKTVSRKFDDEHKAHAELGEIKCSKCGYVFETCD
>gnl|CDD|275024 TIGR04166, methano_MtrB, tetrahydromethanopterin S-methyltransferase, subunit B. Members of this protein family are the MtrB protein of the tetrahydromethanopterin S-methyltransferase complex. This system is universal in archaeal methanogens [Energy metabolism, Methanogenesis]
AYVKIIPELGLVMDPETGIVAEGREDVILLSMDPVNEEIDKLEAAADDLVNSLDPRTTPLGSYPGREGVY
EIAGLFTNIFYGFIIGLIIIFLLLF
>gnl|CDD|275025 TIGR04167, radical_SAM_domain_protein, radical SAM/Cys-rich domain protein. Members of this protein family have an N-terminal radical SAM domain (pfam04055) and a C-terminal pfam12345 domain. The C-terminal region has several conserved Cys residues, one of which is replaced by selenocysteine in at least five bacterial reference genomes
PLRRDSLETLQVNLGYLCNLSCRHCHVDAGPNRTEMMSRETMEQCLEVLKRHPIKTLDITGGAPEMNPHF
RYLVEEARKLGVRVIDRCNLTILLEPGYEDLPEFLAEHKVEVVASLPCYLEENVDRQRGDGVFDKSIEAL
KKLNALGYGREGSGLELNLVYNPGGAFLPPSQAALEADYKRELKERFGIVFNHLFTITNMPIGRFGAFLE
RSGNLEDYMQLLADAFNPATVEGVMCRSLISVDWDGYLYDCDFNQMLGLPLGGGKPKHISDLLEEDLEGR
PIATADHCYGCTAGAGSSCGGAL
>gnl|CDD|275026 TIGR04168, Ser/Thr_protein_phosphatase_family_protein, TIGR04168 family protein. Members of this uncharacterized protein family are restricted, in 49 of 50 genomes, to organisms with a family TIGR04167 radical SAM protein, which occasionally is a selenoprotein
LKQLGPDLVLFVGDFGNEDLELVRAIASLPLPKAVILGNHDAWYTATAWGRDKCPYDRQKEDRLQQQLDL
LGEAHCGWGKRDFPEPGLSVVGGRPFSWGGPGWKLSKFVQAVFGVVSFEESAARIVAAAQSAPHDPLIFL
AHNGPTGLGSDAESPCGRDWKPPGGDWGDPDLALAIAQIRKLKQIPLVVFGHMHHRLRHTKGRLRRTVVR
DRQGTVYLNAACVPRIGKDEEGRKLRHFSWVELENGKVSHVSHRWVDPDGSLASEETLY
>gnl|CDD|200420 TIGR04169, perox_w_seleSAM, alkylhydroperoxidase/carboxymuconolactone decarboxylase family protein. Members of this family are usually annotated as putative carboxymuconolactone decarboxylases, are related also to alkylhydroperoxidase AhpD, and contain a peroxidase-like Cys-X-X-Cys putative redox-active disulfide. All members occur in genomes with a radical SAM protein of family TIGR04167, which occasionally are selenoproteins
DTYYDPADLAKFGEIGEDAPELADKFFDYYGAVFEEGALSEREKALIALAVAHAVQCPYCIDAYTQTSLE
KGANKEQMMEAVHVAAAIRGGATLVHGVQMKNKAKKLSF
>gnl|CDD|211905 TIGR04170, RNR_1b_NrdE, ribonucleoside-diphosphate reductase, class 1b, alpha subunit. Members of this family are NrdE, the alpha subunit of class 1b ribonucleotide reductase. This form uses a dimanganese moiety associated with a tyrosine radical to reduce the cellular requirement for iron
DYHALNNELNLYDDNGKIQFDKDKEALDAYFLEHVNQNTVFFHNLKEKLDYLVENNYYEEEVLDKYSFEF
VIELFEHAYASKFRFPSFMGAFKFYTSYALKTNDGKRYLERYEDRVCMVALTLANGDEELAKQLVDEMIS
QRYQPATPTFLNAGRARRGELVSCFLLRVEDNMNSIGRAINSALQLSKRGGGVALNLSNLREAGAPIKGI
ENQSSGVIPVMKLLEDAFSYANQLGQRQGAGAVYLNAFHPDILRFLDTKKENADEKIRIKTLSLGVVIPD
KFFELAKENKDMYLFSPYDVEREYGVPFDDIDITEKYDEMVANPRIRKKKINARDFFQTLAEIQFESGYP
YIMFEDTVNRANPIIGRIKMSNLCSEILQVSEASLYNDYLEYDEIGHDISCNLGSLNIANVMDSPDFGRT
VETAIRALTAVSDMSHIRNVPSIRKGNAASHAIGLGQMNLHGYLAREGIAYGSPEALDFTNIYFMTVNYY
SLRRSMEIARERGETFAGFEQSDYASGEYFDKYVSQEFAPKTEKVRELFEGIHIPTREDWAELKDDVMEY
GLYHQNRLAVAPTGSISYINHSTSSIHPIVSKIEIRKEGKIGRVYYPAPFLTNENLEYYQDAYDIDMEKI
IDTYATATQHVDQGLSLTLFFKDTATTRDLNRAQIYAWHKGIKTLYYIRLRQLALEGTEIEGCVSCAL
>gnl|CDD|275027 TIGR04171, ribonucleotide-diphosphate_reductase_subunit_beta, ribonucleoside-diphosphate reductase, class 1b, beta subunit. Members of this family are NrdF, the beta subunit of class 1b ribonucleotide reductase. This form uses a dimanganese moiety associated with a tyrosine radical to reduce the cellular requirement for iron [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
YKAINWNRIEDDKDLEFWEQNTSQFWLPEEIPLSNDLDSWRTLSPEEQDLYKKVFGGLTLLDTLQGTVGM
PALIPDADTLHEKAVLNNMGFMESVHAKSYSSIFSTLCTTEEIDEIFRWVENNEYLQKKAEKILEYYEND
DPLKAKVASVFLESFLFYSGFYLPLYLAGQGKLTNSAEIIRLIIRDESIHGVYIGYKAQEGFNKLSEEEQ
EELKDWMYDLLYELYENEEKYTEELYDEVGLTEDVKKFVRYNANKALMNLGFEPLFPEEATDVNPIVLNG
LSTETKNHDFFSGKGNGYVKGKVEALEDDDFDF
>gnl|CDD|275028 TIGR04172, putative_dgqhr_domain_containing_protein, DNA phosphorothioation-associated DGQHR protein 1. The DND system produces an phosphorothioation modification to DNA, replacing a non-bridging oxygen of a phosphate group with sulfur. The modification causes DNA degradation during electrophoresis in Tris buffer. This protein, like DndB (TIGR03233), contains a DGQHR domain (TIGR03187), which also occurs in several contexts that suggest lateral transfer rather than DNA phosphorothioation-dependent restriction
IPAIRVSQPLGDFYAFKISAEDLLKITYSMNAAYNDDGYKLSGVQRKLRLPRLKDIAKYIDSDEAAFPNS
IILAANYDNDGNAIEDEDLRWTVEQTEGDCYSLIIPSNLRLASIIDGQHRLFGFRYAEEERLDMDLLCSV
FIDLPPPYQAYIFATINFNQKKVDKSLAYELFGYDVDEEPREYWSPEKLAVYLTRKLNTDSESPLYQKIK
LAALSDLEEVTADDWLISTATVVDGILRLISSNPKKDRDTLRAGKSSNTGRKKLKDPKDKSPLRDFYIEG
NDKVIEEIVNNYFSAVNELFWKNASEDSYLTKTIGIQALFDILRAILASEAIEESDISMENFEKLLFPIK
DVDFTNNKFTASGIGRTKIRRILLEAIG
>gnl|CDD|200424 TIGR04173, PKD_domain_containing_protein_partial, PIP-CTERM protein sorting domain. Proteins closely related to MJ_1469.1 from Methanocaldococcus jannaschii DSM 2661 are designated archaeosortase D (ArtD). ArtD appears to be a dedicated protein-sorting enzyme with a single target, a PKD domain (pfam00801) repeat protein encoded by adjacent gene. This model describes the C-terminal putative protein-sorting region structurally similar to PEP-CTERM (TIGR02602) and found only on these methanogen PKD domain proteins
VPIPIYIKILSVITTIICIFYIIRWLK
>gnl|CDD|275029 TIGR04174, hypothetical_protein, IPTL-CTERM protein sorting domain. This model describes a variant form of the PEP-CTERM C-terminal protein-sorting domain, with a consensus motif IPTL replacing the more typical VPEP. A majority of these sequences have a WG (Trp-Gly) motif at positions 7-8 of the domain. Species with multiple (up to 15) copies of this domain include Acidovorax citrulli, Acidovorax delafieldii 2AN, Delftia acidovorans SPH-1, and gamma proteobacterium NOR5-3
IPTLSEWGLALLSLLLGLLGARRRRRR
>gnl|CDD|200426 TIGR04175, archaeo_artD, archaeosortase D. This model describes archaeosortase D, one of several strictly archaeal subfamilies related to exosortase, the bacterial protein-sorting putative transpeptidase (see TIGR02602). ArtD is found in the genus Methanocaldococcus. Its predicted target, encoded by an adjacent gene, has a C-terminal VPIP motif-containing region (TIGR04173) likely to be its recognition site
ENKKYLINFLIYFLIIYFVLKFLEDFISRLLANILSHILNTYYYGNIIIFKKTIFSVSPACTCSFEMSLF
LGYIFGTPKVPIKYKVIYSVFGLIIINISNILRIILIIKYSDMKNYLLIHDLISFIIFPVALILNFIWIL
ILKKLNVIKN
>gnl|CDD|275030 TIGR04176, hypothetical_protein, EPS-associated transcriptional regulator, MarR family. Members of this family of MarR-family transcriptional regulators are associated with long genomic loci consisting of genes encoding enzymes for the biosynthesis of exopolysaccharides. These genes include glycosyl transferases, sugar modifying enzymes (epimerases, isomerases, methyltransferases, aminotransferases, etc.), and exopolysaccharide polymerases (wzx, wzy). In Leptospira interrogans, borgpeterenii and biflexa, this gene is observed first in unidirectional EPS biosynthesis loci as long as 90 genes. MarR genes (pfam01407) are known to bind to DNA regions with palindromic or pseudopalindromic sequences as homodimers, and to bind small molecules as triggers for conformational changes controlling on/off states
LRDELRFRVLRLLEENPELSQRELAKELGISLGKVNYCLKALIDKGLIKAGNFRNSDNKLAYAYLLTPSG
IEEKARLTRRFLKRKMAEYEALRAEIEELRREVEG
>gnl|CDD|200428 TIGR04177, conserved_hypothetical_protein_partial, exosortase H, IPTLxxWG-CTERM-specific. This model describes exosortase subfamily H, for which most cognate recognition sequences are found by the IPTLxxWG-CTERM model TIGR04174. Species with this exosortase and multiple (up to 15) copies of the target domain include Acidovorax citrulli, Acidovorax delafieldii 2AN, Delftia acidovorans SPH-1, and gamma proteobacterium NOR5-3 [Protein fate, Protein and peptide secretion and trafficking]
VRFAVTFGILCLLLFTLAMLNWVQESLFEPLTRHLARVSACCLGPFDIHPAAQGLTLWNSQTGFAVSIET
GCNGLEAGIVLFAFVIAFPISWRRKLIGLALGFPALQAGNILRIISLFYLGQWKQNVFEFVHVYLWQVLI
MLDVLVVCMLWLRAASPA
>gnl|CDD|275031 TIGR04178, hypothetical_protein, exosortase/archaeosortase family protein. This model represents the most conserved region of the multitransmembrane protein family of exosortases and archaeosortases. The region includes nearly invariant motifs at the ends of three predicted transmembrane helices on the extracytoplasmic face: a Cys (often Cys-Xaa-Gly), Asn-Xaa-Xaa-Arg, and His. This model is much broader than the bacterial exosortase model (TIGR02602), and has in intended scope similar to (or broader than) pfam09721
VEVAEACSGLRSLILLLALGLLFAYLFPRSLRRKLLLLLLGVPIIYLANILRIVLLILLGYYFGPEAFEF
AHDILGWLLFLLVALLLLLLVLWLLPR
>gnl|CDD|275032 TIGR04179, hypothetical_protein_GM18DRAFT_2302, rhombotail lipoprotein. Members of this protein family are probable lipoproteins. Nearly every member ends with a C-terminal region consisting of a glycine-rich probable cleavage site, a hydrophobic probable transmembrane helix, and a cluster of basic residues, as described in putative protein sorting region model TIGR03501. Furthermore, members tend to be encoded next to a rhomboid family protease, called rhombosortase (TIGR03902) predicted to perform a C-terminal cleavage
LSGCAQNSTRSSRSSSLVEYLYPVADQREAEQPSIPVLTLPLRVGIAFVPSSQGRHEAVPETTQIALLEK
VKEQFRAYPYVSSIEIIPTTYLAPGGGFTNLDQIRRMYGVDVIALVSYDQVQFTDEGVASLLYWTIVGAY
VVPGNENDTQTLMDTAVFDIPSRKMLFRAPGTSQVEGRSTAVNLSEELRQDSVQGFDLATGDMITNLDAQ
LARFKERVKEEPGEVKIEHKGGYSGGGSFGFLPLGLLALICLAAWLRK
>gnl|CDD|275033 TIGR04180, NAD-dependent_epimerase/dehydratase, NAD dependent epimerase/dehydratase, LLPSF_EDH_00030 family. This clade within the NAD dependent epimerase/dehydratase superfamily (pfam01370) is characterized by inclusion of its members within a cassette of seven distinctive enzymes. These include four genes homologous to the elements of the neuraminic (sialic) acid biosynthesis cluster (NeuABCD), an aminotransferase and a nucleotidyltransferase in addition to the epimerase/dehydratase. Together it is very likely that these enzymes direct the biosynthesis of a nine-carbon sugar analagous to CMP-neuraminic acid. These seven genes form the core of the cassette, although they are often accompanied by additional genes that may further modify the product sugar. Although this cassette is widely distributed in bacteria, the family nomenclature arises from the instance in Leptospira interrogans serovar Lai, str. 56601, where it appears as the 30th gene in the 91-gene lipopolysaccharide biosynthesis cluster
VLVTGADGFIGSHLVEALVRQGYEVRAFVLYNSFNSWGWLDTSPPEVKDKIEVVTGDIRDPDSVRKAMKG
CDVVFHLAALIAIPYSYIAPDSYVDTNVTGTLNVLQAARDLGVEKVVHTSTSEVYGTAQYVPIDEKHPLQ
GQSPYSASKIGADQLALSFYRSFNTPVTIIRPFNTYGPRQSARAVIPTIITQIASGKRRIKLGSLSPTRD
FNYVTDTVRGFIAIAESDKTVGEVINIGSNFEISIGDTVKLIAEIMGSEVEIETDEERLRPEKSEVERLW
CDNSKIKELTGWQPKYS
>gnl|CDD|275034 TIGR04181, DegT/DnrJ/EryC1/StrS_aminotransferase, aminotransferase, LLPSF_NHT_00031 family. This clade of aminotransferases is a member of the pfam01041 (DegT/DnrJ/EryC1/StrS) superfamily. The family is named after the instance in Leptospira interrogans serovar Lai, str. 56601, where it is the 31st gene in the 91-gene lipopolysaccharide biosynthesis locus. Members of this family are generally found within a subcluster of seven or more genes including an epimerase/dehydratase, four genes homologous to the elements of the neuraminic (sialic) acid biosynthesis cluster (NeuABCD) and a nucleotidyl transferase. Together it is very likely that these enzymes direct the biosynthesis of a nine-carbon sugar analogous to CMP-neuraminic acid. These seven genes form the core of the cassette, although they are often accompanied by additional genes that may further modify the product sugar
IPLHEPNFGGNEKKYVKECIDSGWVSSVGAYVDRFEEKLAEYTGAKHAVAVVNGTAALHLALHLAGVKPG
DEVITPALTFVATANAISYLGAEPVFVDVDPDTLGLDPDALEEFLEEEAERKDGVLINKETGRRIKACVP
VHVFGHPADMDEIMEICDEWNLPVVEDAAESLGSFYKGKHTGTFGDLGVFSFNGNKIITTGGGGMILTND
EELAKRAKHLSTTAKQPHPWEFEHDEVGYNYRMPNINAALGCAQLEQLEEFLARKRELAEIYKEFFSGIP
GVEFLPEPAGARSNYWLNALLLDSKLDRDELLEALNENGIQTRPLWTLMHELPMYRDCPRDDLPVAENLE
ERLINLPSS
>gnl|CDD|275035 TIGR04182, glyco_TIGR04182, glycosyltransferase, TIGR04182 family. Members of this family are glycosyltransferases restricted to the archaea. All but two members are from species with the PGF-CTERM/archaeosortase A system, a proposed maturation system for exported, glycosylated proteins as are found often in S-layers
DVCVLIPTLNEAATIGDVIDGFQELGYSDILVIDGNSTDGTQEIAKEAGARVVIQSGKGKGQAVREAFEL
IDAPYVLMLDGDGTYLPADADALLEPLLSGRADHVIGNRFADMEPGAFTRLNLVGNRLINRLFRIIHGVD
LRDILSGYRAFTRESIRRMELTETGFEIETEIAVECVKKNLRVEVVPITYRARPDGSDTKLNPLRDGFKI
GLTIYRLAKTNNPLFYFGIIGAIFGLAGFLLGIYVVVEWLKGISHEPLAILTALLIIFGVQLFMFGVLSD
MILTLHREQMREI
>gnl|CDD|275036 TIGR04183, hypothetical_protein, Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification
IYPNPAKGTLIIILLSSSGKVKVEIYDLSGKLVKKTTLNNSNSIDLSNLSSGVYIVKITTGNGTITKKII
KK
>gnl|CDD|275037 TIGR04184, hypothetical_protein_HMPREF0204_12500, ATP-grasp ribosomal peptide maturase, MvdD family. The pair of ATP-grasp proteins MvdD and MvdC (microviridin D and C), as well as an acetyltransferase, produce microviridin K, an example of a RiPP (ribosomally synthesized and posttranslationally modified peptide). Microviridins are peptidase inhibitors
VLIITHSHDNESIPLVTKAIEAQGGKAFRFDTDRYPTEVQLDIYYGDGTEQSFLTTEDQKLDLSDVSAVW
YRRMRIGKKLPDTMDKQLREASVEESRATIRGMIASLRGFHLDPISNVRRAENKQLQLQIARKLGLDIPR
TLTTNNPEAVKQFAAECQQGIITKMLSSFAIYGDKGEENVVFTNPVTEEDLENLEGLRFCPMTFQENIPK
ALELRITIVGEQVFTAAVNSQQLEGAKYDWRKQGVALIDAWQPYTLPPDVEAKLLQLMDELGLNYGAIDM
IVTPDGRYVFLEINPVGEFFWLERLLPGLPISQAIAEVLLD
>gnl|CDD|275038 TIGR04185, RimK-like_ATP-grasp_domain_protein, ATP-grasp ribosomal peptide maturase, MvdC family. The pair of ATP-grasp proteins MvdD and MvdC (microviridin D and C), as well as an acetyltransferase, produce microviridin K, an example of a RiPP (ribosomally synthesized and posttranslationally modified peptide). Microviridins are peptidase inhibitors. This family includes MvdC and corresponding members of similar cassettes
VLLITHSGDFFTIDRVAEALSSKGVQPFRLDTDRFPLEVKLSAHFNNGKSKHRLEYGGGSIDTEQVQAVW
MRRIWQPSLSEELDPDYRDACLRESQATLYGFWDSLRHARWIDPLEKINAASNKLRQLRLAAEVGLVIPR
TLVTNDPEAAREFFQQLGGKMVAKLLTPTSYSMEGSSFFLYTSVVKEEDLEEAESLRYCPMVFQEEIPKQ
RELRVVYVNGNFFVGALDASQYATSAVDWRRPGVNRGFWQHYELPEDVLARLTSFMAELGLTFGAFDFIL
TPDGEYVFLEVNPTGEWGMLERDLDLPISEAIADTLIK
>gnl|CDD|275039 TIGR04186, conserved_hypothetical_protein, putative ATP-grasp target RiPP. A RiPP is a ribosomally produced, post-translationally modified peptide. This family regularly occurs next to ATP-grasp enzymes related to those of microviridin maturation and next to a methyltransferase
VRPWGLRRVRPYPETVPVPAATVVYDPDTQLGVDVDGRGLIVEMGKHGTSTTTGTTTSTSGDQDSDTDHD
QD
>gnl|CDD|275040 TIGR04187, conserved_hypothetical_protein, ATP-grasp ribosomal peptide maturase, SAV_5884 family. Members of this protein family are ATP-grasp ligase family enzymes that regularly occur in a contexts with a methyltransferase and a putative ribosomally translated post-translationally modified peptide precursor. Because of this conserved gene neighborhood and close sequence similarity to ATP-grasp enzymes from microviridin/marinostatin biosynthesis cassettes, this enzyme is suggested also to serve as a peptide maturase
TVLVLTNEQDVTADLVIAELHRRGVPVVRLDPGDFPAQLTLSAEYGDGGWRGTLRTGHRTVDLDDVRSVW
YRRPSPFRLPAHLPAQERRWAAREARMGLGGVLAALPGALWVNHPHRIARAEYKPWQLAAAARCGLRVPA
TLITNDPDAARDFAARYGGVVYKPLSGTPYTEDGRAGVVYTTRVTAEEIDDAVAGTAHLFQARVDKAADV
RLTVVGDRIFAARIDAHSEAARLDWRSDYDALTYSPVTVPDRVATAVRRYLRRLGLVYGAFDFAVTPDGR
WWFLECNPNGQWGWLEDETGLPIAAAIADLLE
>gnl|CDD|275041 TIGR04188, conserved_hypothetical_protein, methyltransferase, ATP-grasp peptide maturase system. Members of this protein family are predicted SAM-dependent methyltransferases that regularly occur in the context of a putative peptide modification ATP-grasp enzyme (TIGR04187, related to enzymes of microviridin maturation) and a putative ribosomal peptide modification target (TIGR04186)
LAARLAAAGVLTDPAWREAVEAVPRHLFLPGFFTQLPDGRGWRPVTADRPDPDEWLALVYSDETLVTQLD
GDLAADAAGGPVTGRPTSSSTQPSLVARMLEALDVEDGHRVLEIGTGTGYSAALLCHRLGDDNVTSVEVD
PGLAARAASALAAAGYAPTVVTGDGLLGHPPRAPYDRIIATCAVRRVPPAWLRQTRPGGVILTTLSGWLY
GGGLVRLTVDDDGTAEGRFLPGYASFMPARPQAPPPAAGDLSAAAADAGDRRTTRLPPALLEDWTGAFLA
QLAAPDAQLLTLTPDTGSPQVLLDVADGSWAELTPDGGGWTVRQGGPRRLWDAVEEALDAWQAAGRPDRD
AFGLTVTPNGHHV
>gnl|CDD|275042 TIGR04189, gliding_motility-related_protein, cell surface protein SprA. SprA is a cell surface protein widely distributed in the Bacteroidetes lineage. In Flavobacterium johnsoniae, a species that shows gliding motility, mutation disrupts gliding
PLDLLLPSNIKTEIEYDSATDRYIVTEKLGDTDIRVPIVLTPEEYEDYVLRQSMKSYWRDKGDAAADKGT
PERFKLLDPNFYVNSPFFEKIFGGNKVDLRPQGSAELDFGGRYNKVDNPSLSPRQRKNLGFDFDQQISMN
VTGKVGDRLKVNVNYDTQSTFDFQNQLKLEYTGKEDDIIQRIEAGNVSMPLNSSLIRGAQSLFGIKAQLQ
FGKLTVTGVFSQQKSQAKEVTIKGGAQTTEFEISADDYDENRHFFLSQYFRDNYDKALSGLPNINSGVQI
TRVEVWVTNKRNSTDNVRNIVALQDLGEPESLYTKNNNPIGPTFTNRLPDNGANNLYPTLIGIPNGIRDI
ATVVQGFGGLVQQGRDYAKLENARKLEPSDYTYDPKLGYISLNQRLQNDEVLAVAFEYTYNGRVYQVGEF
STDGPPDTYTNQLLYVKLLKSPTLSPTLPIWDLMMKNVYSLGAYQLSRENFKLNIYYKDDTTGNYLPPLP
EGNSAGRPLLRVFGLDRLNQYNDPQPDGFFDFVEGITIDPQTGKIIFPVVEPFGSGLAKAFSTNNALADK
YVFQELYDSTKTQAQQFAEKNKYRLKGRYKSSSGSEIRLGAINVPRGSVRVTAGGRTLQEGVDYTVDYQL
GRVTILNEALLASGTPISVSYENNALFNTQRKTLLGTRLDYQFNKNFLIGATALNLSERPLTTKVNLGEE
PINNTIWGVNANYKTESQWLTRAVDKLPFIQTTAPSNISFRGEFAQLRPGHNKASDFEEGTSYIDDFEGT
QTGIDLRSPYSWYLASTPDSAGDSLFFEGTLSDDLDYGYNRAKLAWYSIDPVFYRSSSQTPDYISDDDLS
NHFVREVFIQEIFPNRDVGSGQNQVLPTLDLAYYPNERGPYNYNPDMTADGLLLNPEKRWGGIMRALDSS
DFELSNIEYIEFWVLDPFIENATTNGGDLYFNLGSISEDILKDGRKFFENGLPVNGDTSNTDTTVWGRVP
AQQSLVYAFDNDSGNRRKQDVGLDGLTSADESAFFSSYLNALRGNVDPDAKLLNDPAGDNYHYYLGDDYD
SGPGSILERYKNYNGTEGNSPVAVQNTNYNRGNTTIPDVEDINRDNTLNTIESYFEYRVSLSPSDMVVGQ
NYIVDKREVEVELPNGQKETVTWYQFRIPIREYDSKVGNIQDFKSIRFMRMFMTGFSDEVVLRFATLELV
RGDWRTYTEPLSNTAPDDPADDNTYVDVSTVNIEENSSRTPINYVLPPGVVREQDRTNNTNRQQNEQALS
LKVENLAPGDARGVYKNFNVDLRQYKRLRMFIHAEALADTNGWLSDGELRAFIRLGTDFTNNYYEYEVPL
KLTPVGASSPEEVWPKENQLDIPLSDLTDLKLERNRLQSSSDPVVTYLDDGSEPSNTGNRLSVVGNPSLG
EVRTIMIGVRNPSSDDGNNRSGEVWFNELRLSDFDEKGGWAAVANLNLNLADLANVSASGRMSTAGFGAL
DQKPNERAREDTLQYDVATNLNLGKLLPEKLGISIPFYYSYSSETITPEYDPLDGDILLKDALDAVRSQA
ERDSLRKLAEDYTTRKSFNLTNVRKIKTNGEKLNMPYDIENFSFSYSYSETSHRSPEIEYDLDQNYRAAL
EYNYTFKPKPVEPFKKLKKKSPYLKLIKDFNFNYLPSSISFRTDLNRSFSETQFRDVDLSGPGTGEPVLY
QKNFTFNRLYNLNWNLTKSLRLNFNANTNAIIDEPNYGDVNGKLFGEDYHAWKDTVWRSFLDLGRPDRYT
QTFNVNYTLPLDKIPALDWVNADYTYTADYNWQRGSLALREIDLGNTIRNQRSLQLNGSLNLDKLYNKLG
FLKQRSQDKQSKRKKPQPRTEKPEDKPKQNKTIIPPPRTKILSAVFRLLTMLKNIDVNYSQNKGTVLPGF
LPSVKFFGVDLGGLAPGWGFVFGLQSDDFRDEAARNGWLTTFQSFNSQFTQRFSQNLQLRANLEPIPGLK
IDLTANRTYTRRTQYRYNNVTGVYQSMTPNTSGNFSISTIAIGTAFSNSSDGNSSEAFEKFRENRLTIAN
RLAEQYGGTVYPSDGFGIGYGKNSQDVLIPAFLSAYTGSDPDKSRLSTFPPIPLPNWRITYTGLMRIPWF
KKNFRSVTLAHSYRSSYSVNSYRSNLNYEDLGRDDGTGFRQDNLNGNLIPTYDISAVSLNEQFAPLIGVD
ATFKNGLTIKLEYNKSRALSLSLTNYQLTETRNNEYVIGVGYRIKNFRSVFKGTGVRKRLKNDLNLKLDF
SLRDMFTLIRKLDLDFPQVTSGNKRWSINPSADYDLSKNLTLRFYYDYQINEPLISTSYPRTTTNFGLQL
RFNLG
>gnl|CDD|211913 TIGR04190, Fe-S_oxidoreductase, B12-binding domain/radical SAM domain protein, Ta0216 family. Members of this family are enzymes with an N-terminal B12-binding domain and central radical SAM domain. Families TIGR03975, TIGR04013 and TIGR04014 exhibit a similar architecture, which may be associated with lipid metabolism
DVVFLHAPSVYDFRKRDIMYGPISDVIPSTPVFEMYPVGFISIANYLEQSGFNVRIFNLAARMLRDPKFD
VEKYLKRIEARIFAIDLHWLPHAHGAIEVAKIVKKIHPESPVVFGGLSATYYREELITNYPFIDFVLLGD
STEEPIKQLVEALERGMGLEEVPNLIWRDNGKIRENPITYVPKSLDDVFIDYGYLLRNAIKYHDLKNHLP
YASWLKNPIAAVLTEKGCPLNCAFCGGSNFAYKSNFNRRKLAYRSPETIVEEIEFIQEILRSPIFIVGDL
RMAGPKYYEEFFKLLKERDISNELIFEFFTPPPKEVLKLLSKAVPDFYLEISPESHDEDIRRFNGRPYSN
KSLENFVSNAEKLGFKKIDLYFMVGLPKQTYEDVISCVDYFRKLMKKFRASKRLDTFVSPLAPFVDPGSL
AFENPEKYGYRITARTLEEHRRLLLGRSWYDFLNYETDWMTRDEIAEATYEAAIRLNKLKYEYGLIDEEA
YDEILERIKNARDGIPYLSDEKKSKIKLNELRYKEDDVEWSIISKLTFRSLVSLIYKDYARFI
>gnl|CDD|275043 TIGR04191, hypothetical_protein, putative bacilliredoxin, YphP/YqiW family. This protein family is one of several observed in species that express bacillithiol, an analog of glutathione and mycothiol. Rather than being involved in bacillithiol biosynthesis, members are likely to act in bacillithiol-dependent processes. A suggested term is bacilliredoxin (a glutaredoxin-like thiol-dependent oxidoreductase), and a suggested role of YphP is de-bacillithiolation - removing bacillithiol that became linked to protein thiols under oxidative stress. An older description of YphP as a disulphide isomerase therefore may be wrong
YPEELVQPMREELTRAGFEELTTAEDVDEAMENAEGTTLVVVNSVCGCAAGLARPAVAQALQNDKKPDHL
VTVFAGQDKEATAKAREYFLGYPPSSPSIALFKDGELVHFIERHHIEGRSAEEIAADLQAAFDEYC
>gnl|CDD|275044 TIGR04192, hypothetical_protein_KAOT1_08203, ATP-GRASP peptide maturase, grasp-with-spasm system. Members of this protein family are ATP-GRASP proteins that occur in a peptide maturation cassette with a SPASM domain protein. SPASM (TIGR04085) usually occurs as a C-terminal extension to radical SAM enzymes that act as peptide maturases, although it can occur independently
ILIISRENDISTSDVIDWLRHLGKPVIRINSEDDVFELHFIKKDIVLFKNTKSNRNQFLLNEIKAVWYRR
GGISFKNFRFHNQELDRYLFDVQKSLLREWKDLKEYIIYTLEQKPNIGNYSNSDVNKLIVLEKAKEAGLD
TPDYFLVSNKEDLIPSTIANEVITKSISGGPIISQDNQSYYTYTELITQEKFAGLPENFFPSLIQEKIEK
KYELRVFYLNGKFYSMAIFSQSDEQTRVDFRKYNDQKPNRNVPYKLPAHVEHKIDKLMNELDLNCGSLDF
IVTEDNEFYFLEVNPVGQFGMTSLPCNYYLEKEIAAYL
>gnl|CDD|211916 TIGR04193, hypothetical_protein_KAOT1_08193, SPASM domain peptide maturase, grasp-with-spasm system. A 4Fe-4S-binding C-terminal domain is shared by radical SAM maturases for Subtilosin A (S), PQQ (P), Anaerobic sulfatases (AS), and mycofactocin (M), hence SPASM. Radical SAM proteins with SPASM tend to be peptide maturases. All members of this family, like some members of the quasi-rSAM family TIGR04105, lack the 4Fe-4S cluster of the radical SAM domain (pfam04055) in the N-terminal region. Members of this family occur with an ATP-GRASP family protein, known as a possible maturase from microviridin biosynthetic clusters. Systems occur in Microscilla marina ATCC 23134, Kordia algicida OT-1, Sphingobacterium spiritivorum ATCC 33300, etc
YFNLFSNCFIVKGYTRSLICDVSRQKVYFVPNEYYELVTVLKSNSIGTIASMYDDDSKIIFKEFIDYLLE
IELGFVTEELELFPEISTEYDHPSDITNSIIEVRDEMHDFKKIINQLEILACYHLQIRAYNTTSVEFLEE
ILSIFKGSNFRSVELLLPYDGEITAEFAALLTKYEIRLVTYHVYNMEEAEAKKRSRYYHGSLAYFKKEVS
KCSSCGLISMKSLNIRDIKGFTENQNHNGCLNKKISIDETGNIKNCPSMTKDYGNINETSLEEIINDKGF
QKLWNINKDSIETCKDCEFRYICTDCRAYTENGGDNYSKPLKCGYNPYTNTWEDWSINPLKQ
>gnl|CDD|211917 TIGR04194, hypothetical_protein_M23134_00169, grasp-with-spasm leader A domain. This model describes the leader peptide domain, ending in a Gly-Gly cleavage motif, for a post-ribosomal natural product (PRNP) precursor. The corresponding modification enzymes include an ATP-GRASP enzyme and a SPASM-domain protein, related to the C-terminal region of numerous peptide-modification radical SAM enzymes
MKKLSKLNNKLFSNNKLNNIQKQYIKGG
>gnl|CDD|211918 TIGR04195, hypothetical_protein_SPBc2p022, peptide S-glycosyltransferase, SunS family. Members of this family include SunS, the S-glycosyltransferase that transfers a sugar (substrate is variable in reconstitution assays) onto the precursor of the glycopeptide sublancin, which once was thought to be a lantibiotic
LNDIVLELEHGHADSLLLKDLSLIQGIEEYEKDIWGDLSDSMNINELVAGYEKADTPSITCGIITYNEEK
CIKKCLDSLGDDFDEIIVLDSHSTDDTTDIIKCDFPDVEIIYEKWIDDFSFARNKIIELASSEWIYFIDA
DNLYCKDNKGKFAKVAKLIEFFSIDCIISPMIEEHIGHLYSDNRKMFRLKGGIKFHGKVHEEPINADGSI
PFNFIVDIKICHDGYDPEEINIKEKNDRNIKLTEEMLEEEPENPKWLFFFARELHLALDDDEEAEDLLIK
AIDLYKKFNDKRHFIDAILLLCSILFQKNNIRDLNEYLDILEEEQPLCSDVDYFRSAILFVDIQLKLGKL
LDNLIDEALEDEKYSAIDSSKDHFKAILIELNCQIDDWEGAFEIFDEIKNDEAKKEFKQRLANILHHIEH
KI
>gnl|CDD|211919 TIGR04196, putative_lipoprotein, glycopeptide, sublancin family. Members of this family, including sublancin, are post-ribosomal natural products (PRNP) with an S-linked glycosylation. Sublancin itself also has two disulfide bonds. A related gene cluster in Bacillus cereus E33L includes the four Cys involved in the disulfide cluster but lacks the region with the glycosylated Cys, and have been excluded
MEELFKELKLEELENFEGGYDGVNYMHQHDGGGAGGGSGIGKAQCAAFKALCASGGSEWLGGYGGCGGGA
NACELARKFC
>gnl|CDD|275045 TIGR04197, conserved_hypothetical_protein, type VII secretion effector, SACOL2603 family. Members of this protein family are similar in length and sequence (although remotely) to the WXG100 family of type VII secretion system (T7SS) targets, described by family TIGR03930. Phylogenetic profiling shows that members of this family are similarly restricted to species with T7SS, marking this family as a related set of T7SS effectors. Members include SACOL2603 from Staphylococcus aureus subsp. aureus COL. Oddly, members of family pfam10824 (DUF2580), which appears also to be related, seem not to be tied to T7SS
IKSNLETAQQHATAIKSASSALSGVGSVTKDDQTTLTGNTNAHEAIDQLQTLVSQIQSALEQDATNIHSV
ANEFEAVDQEIAQQI
>gnl|CDD|275046 TIGR04198, Includes:_mRNA_guanine-N7--methyltransferase, mRNA capping enzyme, paramyxovirus family. This model represents a common C-terminal region shared by paramyxovirus-like RNA-dependent RNA polymerases (see pfam00946). Polymerase proteins described by these two models are often called L protein (large polymerase protein). Capping of mRNA requires RNA triphosphatase and guanylyl transferase activities, demonstrated for the rinderpest virus L protein and at least partially localized to the region of this model
LLKRAIRLAKVINWAYGDDSNLWKLILNLLKARTDLDLDELRLLTPFPTSGNLLHRLSDSSTQHGFFPAS
LPRVSSYVHISTDTLNLISDGGKNYNLIFQQVMLLGLSIMETIFRYSSSTGIQEGTLHLHTECSCCIREI
DEPVLEPSLVLVPELPSPKLNKLIYDPSPLIGKDLHRLDLISFKLKEGNFDSLSGEEKIYLLSRCTGFLL
ADTILSEDRSKENDAIFPSDISNSWITEFLYVDPRLFLVGLGTGLLLELAYQLYYLRIRGRYAILEYLKS
PLERISGSVLGILSPTLSHPKILRRLVDVGIIEPVPHPNPASYPLTKLSLGILLRNYLRFLSYLLTGVET
NLSVIIPEDLEDDLSDRVWIFLDRRLCLLIGLYSLSSESPKLRGLNSTEKCKVLTEYLRLLGHLLSWLLS
DPDIDAYPSNLYFIRRKIRTSDASKSIPEKESVLTESLSWGCEYVSLSLGVTFSLPSLYTPFSEPVPESS
IPRVPDPLHHGLRSVGVASSAHYKARSILSLLKKLKILYGDCLFLGEGSGGMLSLLERLVPPSKIYYNSL
LDLDDNPPQREFPPPPSALAGLGSGTGRCDNFEDLWNGPSDLTDITTWDYFNFILNQVPLDSLDLIHCDM
ELTDDKDIEKVLQFSSVQLLSTKYSSPHSSEVYVVFKRLAQSILIALSRVLSSLSTLVIWGSKLIGSELL
EEFTRALESLLSRLGVGIPPLIRNPLSSLDTLLISLGGESGSSYGLVDSRVSILADFSKVKGLLSSAILT
LLKELIRTLDSSKSLTPPYPLSILGKLRTLIGLLTLKSLSLYLRTLLLLNESWRIKWVRKLLKGKFRLSS
ILSWDEYLRDRRLLLNRLGKGEWLYLLMGRSLLRLSRSELKKLLKLIGSSLSG
>gnl|CDD|275047 TIGR04199, Exosortase_EpsH-related_protein, exosortase J. Exosortase J occurs as a three-member paralogous family in Acidobacterium sp. MP5ACTX8. It contains an N-terminal exosortase/archaeosortase domain and a novel C-terminal domain comprising about half of total protein length. The presumptive target, found as an adjacent gene for two of the three paralogs, consists of a possible lipoprotein signal peptide followed almost immediately by a C-terminal region with some PEP-CTERM-like characteristics
IAVLVTIGSVSILPLWLALGHLWATDPLKSIGALFPFVSFILILRAWRSLGWELDGSWWGIALLALSILL
AHLRDVSNLVIFFQSEWIGLLPPGALVAFLYAAGVVLLFGGVRLLRAGIFPLCLMFFVDPVPQFFNSAVD
LPLQHASALTARAFAHLIGLNLTGAQLRMMFAPDFGMFIAPGCNGVRGSITLGYLALIFGYSYRFRPRVL
GLIVLGAVLLGYVFNLLRLCVLVLYYKLALEVPSLQRYGVEIDYLIGACLFLIATLLLFTLIRSLEPRHD
VREKSTAATPEPTPSNSPQATLVQIAAFVALVMVFILPASRSLKVDPSMRPKESEILAAFPQHVGPYRLI
RTWSEHDSTGMIVYGWGEYEATGNATTSAATHVSLGISPALGDHDVAHCHAARGERPDWHGSFDAPALQG
PIDFASTFYNDGITQQLEAETVCSGGGCVQYSIGSGHQGAVYSAPGVRDLLFVSSTRPLPVLLRGDTPDT
DPTPSSNLRTQLEADLRVFLEHADLLPLTMSY
>gnl|CDD|211923 TIGR04200, hypothetical_protein_AciX8DRAFT_1317, XrtJ-associated TM-motif-TM protein. This model represents essentially the full length, ~60 residues, of a two-gene paralogous family from Acidobacterium sp. MP5ACTX8. Sequences consist of an N-terminal signal sequence ending in a GC motif, suggestive of the lipoprotein signal sequence, followed immediately by a C-terminal domain sequence with characteristics PEP-CTERM-like sequences, including a PExP motif and a transmembrane helix. Both members occur next to the novel exosortase variant, XrtJ, which contains a novel C-terminal domain
QFLFAAAALAFLAAMPAHAQGVLTGCSDSPEAPTYVLILAGLSGGAYASSALMKLLRAKRKC
>gnl|CDD|275048 TIGR04201, Myxo_Cys_RPT, Cys-rich repeat, Myxococcales-type. This repeat is restricted to the Myxococcales, a division of the deltaproteobacteria. It occurs in several surface proteins, and may form a stalk region. The repeat averages about 21 amino acids in length with four or five Cys, three of which are nearly invariant
VCVECTADSDCGAGQVCDAGTC
>gnl|CDD|275049 TIGR04202, RNA-dependent_RNA_polymerase, RNA endonuclease, cap-snatching, arenavirus family. This model describes a shared signature region from an RNA endonuclease region associated with cap-snatching for mRNA production by RNA viruses. This domain usually is part of a multifunctional protein, the L protein responsible for RNA-dependent RNA polymerase activity. Cap-snatching is a viral alternative to synthesizing a eukaryotic-like mRNA cap itself
VTPDNYKLTGNVLILLEVFVRVDPESFEKKYKEKYEKLLSLKGDLLSPGITLVPVVDGRTD
>gnl|CDD|275050 TIGR04203, YSIRK_type_signal_peptide_partial, Streptococcal surface-anchored protein repeat, S. criceti family. This model describes a repeat sequence that occurs primarily LPXTG-anchored Streptococcus surface proteins, although it does occur elsewhere. It can comprise a major fraction of the length of repeat proteins taht exceed 2000 in length
TPTVTVTDNGDGTHTITITNGDGKETTTVTVKDGKDGK
>gnl|CDD|275051 TIGR04204, MAST_ArtA_sort, MAST domain. This model describes a domain (or in most cases the full length) of archaeal surface proteins that are putative targets for C-terminal processing by archaeosortase A (TIGR04125). Most members of this family belong to proteins encoded by tandem genes in the genus Methanosarcina. The putative processing signal, PGF-CTERM (TIGR04126), included within the domain definition, takes a variant form, with consensus motif PAF instead of PGF. We suggest the name MAST domain: Methanosarcina Archaeosortase-Sorted Tandem gene family domain
SIDVYYNDKLLPGKEVAKPTLKIGEPFKVKINITVYQKSRVSVEVSSIGPGRFEIINGDTSKMNLYSPDR
ILDRNSGKVYEWTVKPTELWAGGSLPLNFVYQINETGTDEPLVPGEFTIAYPIISNEHYEGETPTSEQPE
TENQPTSKKPASENSSSPASAPAFSLVTAISALALVFFRLSR
>gnl|CDD|275052 TIGR04205, classIII_w_PIP, class III signal peptide protein, archaeosortase D/PIP-CTERM system. Members of this protein family are short proteins that consist largely of the archaeal class III signal peptide (see pfam04021). Members are encoded in a gene cassette between archaeosortase D (TIGR04175) and its PIP-CTERM target protein (TIGR04173)
NKGQISLEFALLLALIVATASIVGFYYLKMVSFGSATAKNISGSTESAMANKTVRRVEKVKEALNGQ
>gnl|CDD|275053 TIGR04206, hypothetical_protein_ZOD2009_07744, TIGR04206 family protein. Members of this integral membrane protein family are found exclusively in halophilic archaea. In at least three species (Haloarcula marismortui, Haloquadratum walsbyi, and Haloferax volcanii), members are found in the gene neighborhood of archaeosortase A, suggesting a role in protein sorting
PARRLFLWLLALALVPWSVQVFSGGGVTLVFPWGLVNTNPGEVTPLPDYLFRFTSGLPPYILAWPLGVAL
YLFAVGSAVAGVFGREDVRVTAGLLALAGVTQLSVALGFSTRPGRTAVPVGALVLLLVAWWFYWPDRRG
>gnl|CDD|275054 TIGR04207, hypothetical_protein_HborDRAFT_0626, surface glycoprotein signal peptide. This N-terminal homology domain appears to be a specialized class of signal peptide. It occurs mostly in the halophilic archaea, primarily on proteins with the C-terminal PGF-CTERM domain, including the S-layer-forming major surface glycoprotein of several species. The PGF-CTERM domain is the putative archaeosortase A recognition sequence. However, this N-terminal domain occurs also in several archaeal proteins that lack PGF-CTERM, and occurs in bacteria on a protein from Clostridium leptum DSM 753
KLRAVFLAALMVMSVFAGGVAFAGSAAAAD
>gnl|CDD|275055 TIGR04209, sarcinarray, sarcinarray family protein. Members of this protein family are exclusive to archaea, probably all of which have S-layer surface protein arrays. All member proteins have an N-terminal signal sequence. The majority of known members belong to codirectional tandem arrays in the genus Methanosarcina (nine in M. barkeri str. Fusaro). Nearly all members have an additional 50 residues, (trimmed from the seed alignment for this model), consisting of low-complexity sequence rich in E,N,Q,T,S, and P, followed by a variant (PAF) form of the PGF-CTERM putative archaeal surface glycoprotein sorting signal. The coined name, sarcinarray family protein, evokes the predicted archaeal surface layer localization, the taxonomic bias of known members, and the tandem organization of most members
FLLAFVSLVSASSDYGSIDVYYNGKLLPGAEVAKPVLKIGEPFTVKINMTVYQKSTVSVKLSELGGGSFE
IISGPSPMNIYSSRILEKNETHTFEWTVAPTDNWAGGSLPVDFHYQINDFGTPEPLVNGSFTVAYPYISN
EHYE
>gnl|CDD|211933 TIGR04210, Contains:_Non-structural_protein_NSm, bunyavirus nonstructural protein NSm. This model describes a protein region that is cleaved from a bunyavirus polyprotein to become the nonstructural protein NSm (encoded by the M segment). It is flanked by glycoprotein GP2 and glycoprotein GP1
SLCKSKGSSLILSILTAVLILSFITPIEGTLTNYSEEKYTLEELPDDFLGLIEKINIYEQICEINSIITI
CLLLIILILLYLLNKIIHLLLKIYYVFCAECGMYHEKKGLKYNGDFTNKCGFCTCGQLEDVEGLIIHKKS
KNCLYKYKIKWVKNILILLIFLLILKNSTIVVA
>gnl|CDD|275056 TIGR04211, hypothetical_protein, SH3 domain protein. Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region
YISDELFVYMRSGPGNQYRILGSLKSGTPVTVLERSEDGYSRVRTPKGREGWVLSRYLSDTPSARERLPE
LQQELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQISANAIELDEENRELREE
LAELKQENEALEAENERLQENEQRRWFLYGGGVLFLGILLGLILPRLLPRRRRRSDGW
>gnl|CDD|275057 TIGR04212, conserved_hypothetical_protein, Acinetobacter rhombotarget A. Members of this protein family are found, so far, exclusively in the genus Acinetobacter. Members average just over 600 amino acids in length, including a 22-amino acid C-terminal putative protein sorting recognition sequence, GlyGly-CTERM (TIGR03501). The GlyGly-CTERM signal always co-occurs with a subfamily of the rhomboid family intramembrane serine proteases called rhombosortase (TIGR03902). Members occur paired with a second rhombosortase target, with which it also shares an N-terminal motif CSLREA. This protein is designated Acinetobacter rhombotarget A (rbtA)
MLKRSIAIALLAIAGHAYSADIQVTTTVDEDKDDTVCSLREAVEYINQRMPDQYEAGYNGCGGKDASSTI
ILERDKEYKLNNHIEIKADLTIRTAYDTSVFETDQPGLNNATIKMVGSDQLFRIDDGSVEKALITVLLKE
VNLQGCAKDCGVNQGGLIYNNEYLTLEYSRLTNGYANQGGAIYNAGQLSETEKTAGIVEIRNSLIQNNKA
DQGAVIYSEMPRFRISQSVIRDNKTTAASGALIYSQTSFSDETTGSFLASRAIGLSNSTIFHNKGGYVIN
VRDGMVLNNLTMIKNAAGLYFDAPLGKAYLSNSIIVGNGTKNCTAAANDKSIVQSNLVTQECNGNAASYY
PNIMWSGNKLIAGSTVEGVCDAPPADGLLCPYSTPKDKFLGFFKPRLLMSYNSLSDSLIVNKGRIYSDGT
SIGLASCEAIDQRGKNRSGYDELCDLGAIELVVNRSTISLVGQDIRYGQVAKFSIADSLGDGELVPPATC
EAILGKRPDGKEWQPGCLEVVQTQTPSKGKLTIDQEGNVVYTPNGNWHGADIFKIRVVTTTTRFNDHINS
YIEIPVQIVQEPPNHFESKTVNTGGGSIGLGSILGLLGLIGLRRF
>gnl|CDD|275058 TIGR04213, PGF_pre_PGF, PGF-pre-PGF domain. This domain occurs in archaeal species. Most domains in this family end with a motif PGF, after which the member sequences change in character to low-complexity sequence (usually Thr-rich) for about 40 residues. The low complexity region usually is followed by a PGF-CTERM domain (TIGR04126), which we suggest is the recognition sequence for archaeosortase A (TIGR04125), a putative protein-sorting transpeptidase. The similarity between the PGF motif in this domain and in the PGF-CTERM domain is highly suggestive
EPASNVEVKELSQRFVTSGEPVKFDFTENATPVTSIEFDAKKTAGKVTTIVEVLKNTSTLVDELPPGKVY
KNLNIWVGNSGFASPNNIENATIGFKVEKSWIEENNIDPSSIVLMRYNEGKWEELPTEKIGEDDGYVYFE
AETPGFSPFAITG
>gnl|CDD|211937 TIGR04214, conserved_hypothetical_protein, CSLREA domain. This model describes an N-terminal region, with a motif CSLREA, shared by tandem genes in Acinetobacter that both have the GlyGly-CTERM putative protein-sorting domain. Many proteins with this domain are putative outer membrane proteins (OMPs) with predicted beta strand-forming repeats
IVVTTTADEDDDNCGTCSLREAIQAAN
>gnl|CDD|275059 TIGR04215, conserved_hypothetical_protein, choice-of-anchor A domain. This domain may occur as essentially the full length of a protein, except for an N-terminal sequence and a C-terminal protein-sorting signal such as PEP-CTERM or LPXTG. Most often, the putative surface protein is longer and contains repetitive sequence regions. This is one of very few domains for which both anchoring domains occur, and designated choice-of-anchor A domain. The best characterized member is Bacillus anthracis protein BA0871, a collagen-binding protein with five CNA-family protein B-type repeats toward the C-terminus and an LPXTG cell wall attachment motif
GDYNVFVFGDFTSSGSDVEGRVAVGGNITLGGYSVGSNLPGSDGSDALVVGGDLTLGNGQVNNGNAVYGG
TVSGTGSVTVNNGTASQGTIVSGPIDFAAAFAELRALSAALAGLAANGTVVRSGNGGGLTLTGTGSSGLN
VFNVDAADLFGANNITFGVPAGSTVVINVSGTTVTLSGGSGSGGGGDDANRVLWNFPDATTLTLSGAGFQ
GSVLAPNADVTTNGGNINGRVIAGSLTGGGEIHNYPFNG
>gnl|CDD|275060 TIGR04216, halo_surf_glyco, major cell surface glycoprotein. Members of this family are the S-layer-forming halobacterial major cell surface glycoprotein. The highest scores below model cutoffs are fragmentary paralogs to actual members of the family. Modifications include at N-linked and O-linked glycosylation, a C-terminal diphytanylglyceryl modification, and probable cleavage of the PGF-CTERM tail
TVQSGARVFQGEEDLSFDGGNGASNSPQLSRTGGNNEGVPLDSPIPQDQPTGTYDVDGSDSADTFNVTLQ
TPRVTDLEVLNNSGGDVTGSTLSTSQAGDAYVNADYNYEAAEDLELTVEDESGTDITNEILSGTDTFVDD
GSSGSNSDTGGGVEIDPSDVDAGEYTITVEGAEDLDFGDATETMTVTISSDDEASLNLDNDEVTQGENVQ
YTVENSPEGNYHVVAVDSSDFRDDITAEQAKEVFRNVGDTSEVGIVNSSGSTNTIGSDTGPTDADTVDYA
YAVVEIDGGSGVGGIETQYLDDSSVDVELYPASDSATAPYLASGQDATNANLVDLIQTDDDQDLDVEEGE
ITLDSPTGAYVVGSEVDINGTANSGVDSVAIYARDNGDYELVEIDGSNTISVDSDDTFEEEDIALSDGSG
GGNSILSLPGTYRIGVIDASDADVGGDGSVDDSLTTSDFNSGVSSSNSIRVTDTALTGQFTTYNGQVAPD
DTGQVDVEGTAPGKDNVLVIFVDSRGNVNYQEVSVDSDDTFDEEDIDIGGLTQGTVTAHILSSGRDGEIG
DTGTSNGATLNDLIGYLDTYAGGSNTGEQIREQILSNTVDDTASDDLIVTETFRLADGLTTIESVYNPVE
AGGTLEVAGSTNRKPDDNTITVELLNEDDTSVTLESTDEWNSDGQWSVEVDLSDVETGNYTVEADDGDNT
DRVNVEVVEETEEPDTTTPSDNEEDTTTTTDGPTETTETTEPTTTTPEPTEETTTGSSTPGFG
>gnl|CDD|211940 TIGR04217, archae_ser_T, archaetidylserine synthase. The activity CDP-2,3-di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase (archaetidylserine synthase) was demonstrated experimentally in Methanothermobacter thermautotrophicus. Members represent an exception within the broader family (TIGR00473) of CDP-diacylglycerol-serine O-phosphatidyltransferases
MNIFQMLKLPDLVSLLNAIFGIGAIFAAFSGSFGLAFVLILLAAVADGADGYIARRIKSGELGEQLDSLA
DAVSFGVAPAVLIFLIYGVEEPYIVGIFACLYAVCGILRLARFNTKSKPIPDFEGLPITASGVVLASYLL
LGEKYIIVDVILILTLLLSILMISTHPYPKIRGPKALAFVAIVFGITVLSYFILVEYMRVFSTILFLLML
LYLESPIMKIP
>gnl|CDD|211941 TIGR04218, PtnA_protein, ribosomal natural product, plantazolicin-class. Members of this protein family are precursors of TOMMs, that is, thizazole/oxazole-modified microcins. Members are about 42 residues in length, have a C-terminal region of extremely low complexity rich in Ser, and are often missed by ab initio gene callers. The plantazolicin from Bacillus amyloliquefaciens FZB42 is a peptide antibiotic effective against Bacillus anthracis
MTTIALPTALAATVHGEGQHLFEPMAARCTCTTIISSSSTF
>gnl|CDD|275061 TIGR04219, hypothetical_protein, outer membrane protein. Members of this protein family are outer membrane proteins (OMP), as can be seen by their homology to YfaZ protein (see) and by the OMP targeting region at the C-terminus, including a C-terminal Phe residue. Members of this protein family are found in the great majority of genomes with the GlyGly-CTERM protein sorting signal and the rhombosortase putative sorting enzyme, although the relationship may be fortuitous
KKLLLALAVAALASTSAQADTILGVYAGADYWQADPSGDIGDSIDNGDDLNYDDETQPSGYVALEHPIPL
IPNVKIRYTDLDFEGSGTGTRTTDVDLSHTDFTLYYELLDNDLVSLDLGLTLRQFDGTVRVNGAGTTETT
DFDETVPMLYAAAEVGLPGTGLSVFAEGNYGSYDGSKLTDAQAGVQYRFIDLPAVDLGLRAGYRVMDIDF
DDVDDLSADLKFDGPFAGAEVHF
>gnl|CDD|211943 TIGR04220, hypothetical_protein_L8106_29040, cyanobactin biosynthesis protein, PatB/AcyB/McaB family. Members of this protein family are small (~ 80 amino acids) and occur in biosynthesis clusters for cyanobactins, a type of ribosomal natural product, thiazole/oxazole-modified microcin (TOMM). The function of this protein family is unknown, and the recognized cyanobactin precursors (e.g. microcyclamides and patellamides) are encoded by a different protein (see TIGR03678). In this protein family, however, a core region of about 62 amino acids (modeled) is followed by a hypervariable region of 5 to 23 amino acids, with hallmarks of possible cyclodehydratase modification sites. The hallmarks include Cys residues flanked by Gly, and variable length Ser-rich tripeptide repeats. Further, members of this family were shown dispensible for patellamide biosynthesis, and two may occur in a cluster. Therefore, this family may represent a precursor of another type of ribosomal natural product
MRLPKLSPPVKRPHFIHPHECVDVIHGRVEDLVSIRMDLLHGANYNDPAAFAYRSYGQVKM
>gnl|CDD|275062 TIGR04221, SecA2_Mycobac, accessory Sec system translocase SecA2, Actinobacterial type. Members of this family are the SecA2 subunit of the Mycobacterial type of accessory secretory system. This family is quite different SecA2 of the Staph/Strep type (TIGR03714)
LFSWFWKALGSSTERNQKRSLAIVPAAASRMKELSALDDEELTKAARDLVLSGEAADAAQFLAILREAAE
RTLGMRPFDVQLLGALRLLAGDVIEMATGEGKTLAGAMAATGFALLGKRVHVVTVNDYLARRDAEWMGPL
VDFFGLTVGWVTEDSTPDERRAAYACDVTYASVNEIGFDVLRDQLVTDRADLVQPAADVALIDEADSVLV
DEALVPLVLAGNEPGEAPRGRITDLVRRLREDKHYTVDEDGRNVHLTEDGARAVEAELGIDDLYSEEHVG
TTLVQVNVALHAHALLIRDVHYIVRDGKVALIDASRGRVAQLQRWPDGLQAAVEAKEGLEVTEGGEVLDT
ITVQALIGRYPTVCGMTGTAVAAGEQLRQFYDLGVSVIPPNTPNIRFDEADRVYATAAEKNDAIVEEIAE
VHKTGQPVLVGTQDVAESEELAEALLEAGVPCNVLNAKNDAEEAAIIAEAGDIGAVTVSTQMAGRGTDIR
LGGSDEADHDRVAELGGLHVIGTGRHRTARLDNQLRGRAGRQGDPGSSVFFVSLEDDVVAVGGAGETVPA
QPAEDGRIESPRVQDFVDHAQRVAEGQLLEIHANTWRYNQLIAQQRDIIDERRETLLDTDTAWQELSERA
ADRAAELKKEVSEDALERAAREIMLYHLDRGWAEHLAYLDDVRESIHLRALGRETPLDEFHRMAVRAFKE
LAQRAVDKAVETFEEVEIDADGAHLDEAGLARPSATWTYMVHDNPLASSGNSLLSSIGNIFR
>gnl|CDD|275063 TIGR04222, integral_membrane_protein, TIGR04222 domain. The majority of the proteins with a domain as described by this model have an extreme C-terminal sequence that is consists of extremely low-complexity sequence, rich in Ser or in Gly interspersed with Cys. That C-terminal region resembles ribosomal natural product precursors, although there is no evidence that C-terminal regions of these proteins undergo any modification or have any such function
FYLLALAVALVLALVLRRVLRRRRARPGPAPRALDPYELAYLAGGPARVVDTALASLVRRGRLRVGRGGR
VTVVGPAPAGSDPLERAVLDALAAALPGSVARLRLAAAVGPAVRAIRDRLVRRGLLLPPGQRRRARALGA
LPLLAVLALGLVRLVAGLARGRPVGFLVLLLLATAVLGLVLARVPARRTRAGRRALARLRARHAGLRPSG
PGDLALAVALFGLAALV
>gnl|CDD|275064 TIGR04223, quorum_AgrD, cyclic lactone autoinducer peptide. Members of this family of short peptides are precursors to thiolactone (unless Cys is replaced by Ser) cyclic autoinducer peptides, used in quorum-sensing systems in Gram-positive bacteria. The best characterized is the AgrD precursor, processed by the AgrB protein. Nearby proteins regularly encountered include a histidine kinase and a response regulator. This model is related to pfam05931 but is newer and currently broader in scope
KKILKLLAKLALKVATVAANSACWFILYQPKVPEELK
>gnl|CDD|275065 TIGR04224, cell_wall_surface_anchor_family_protein, serine-rich repeat adhesion glycoprotein AST domain. This model describes a definitive conserved N-terminal domain shared by Streptococcal serine-rich adhesion glycoproteins. These highly repetitive proteins may exceed 4000 amino acids in length, consisting largely of long regions in which every second amino acid is Ser. Members of this family, if sequenced completely and assigned the correct start site, begin with a KxYKxGKxW motif region (see TIGR03715) and end with an LPXTG motif region (see TIGR01167). Members are exported by the accessory secretory system (SecA2 and SecY2). They are highly variable among the Streptococci and may help determine host ranges for pathogenesis
FGLFKVMRGGVDESSVSVQVVEEQVRLSSSGLDLLKGILATGAVLGGAVV
>gnl|CDD|275066 TIGR04225, surface-associated_protein_CshA_partial, CshA-type fibril repeat. Many proteins with this repeat are LPXTG-anchored surface proteins of Firmicutes species, but the repeat occurs more broadly. Members include CshA from Streptococcus gordonii
VTPTATDATSTGIQGQPQTGTPTFTPGDPTVPIDDEVPATLVDGTTGKPTTVTVPGEGTYTVDPDGTVTF
TPEKDFVGTATPVTVQRVDKNGTPATATYTPTV
>gnl|CDD|275067 TIGR04226, Fimbrial_subunit_type_2, fimbrial isopeptide formation D2 domain. The Streptococcus Pneumoniae pilus backbone protein, RrgB, has three tandem domains with Lys-to-Asn isopeptide bonds, but these three regions are extremely divergent in sequence. This model represents the homology domain family of the D2 domain. It occurs just once in many surface proteins but up to twenty times in some pilin subunit proteins. Three of every four members have the typical Gram-positive C-terminal motif, LPXTG, although in many cases this motif may be involved in pilin subunit cross-linking rather than cell wall attachment. Proteins with this domain include fimbrial proteins with lectin-like adhesion functions, and the majority of characterized members are involved in surface adhesion to host structures
EEPTITKKVNDKDDADVNIGDEVTYTITTTVPADIADYKSFVITDTLDDGLTYKGSVKVTVDGKTLTVDT
DYTVTDGQTVTVTFTDAGLKKLAGKKITVTYTAKVKEGAVLGKGIPNTATLTYN
>gnl|CDD|211950 TIGR04227, zinc_metalloproteinase_C, zinc metalloproteinase 18-residue repeat. This model describes a short (18-amino acid) tandem repeat that occurs variable numbers of times in zinc metalloproteinase C (zmpC) homologs in various species of Streptococcus. This repeat occurs, oddly, as an interruption in a region of tandem repeats of another type
VHEVPELTEYGTVPDTAP
>gnl|CDD|275068 TIGR04228, isopep_sspB_C2, adhesin isopeptide-forming domain, sspB-C2 type. This domain has a conserved Lys (position 3 in seed alignment) and Asn at 177 that form an intramolecular isopeptide bond. The Asp (or Glu) at position 59
PTKKNTNDAGVNIDGKTVLPGSTNYYRLTWDLSQYKGIKASKEAIAKGFGYVDDYDEEALTVDQDKITIT
DSNGKDVTGLFTMYHVLSVKEAPAKVQAILKAAGITPKGEFQVWVAKDPQAFYKNYVQTGQNITIVLPMT
VKKDKTGGKVENTAYQIDFGNGYETNTVTNNVP
>gnl|CDD|275069 TIGR04229, geopeptide, putative radical SAM-modified peptide. This family of short peptides occurs near radical SAM/SPASM domain proteins and is proposed to be modified by that enzyme
VEVLDEGIANKEEGDIACCTSAF
>gnl|CDD|275070 TIGR04230, seadorna_VP11, seadornavirus VP11 protein. This protein family occurs in the seadornavirus virus group, with designations VP11 in Banna virus, and VP12 in Kadipiro virus and Liao ning virus. The function has not been assigned
TIQVQNSGCCNGRPFCVHKMVALIVLIISAAITVVDQLYQKLPSTDQKYIVSLICDGINATIISIMAIFG
MTNLNKVRYSLDENGVYSQEMVTMPVLSDAANNETKLVKKQNKDLENKGLYPNPKLTEPTAKMIHNYMYD
HKTQGAYLITEHQIEQIKINSVDPNNTPLKIEVRS
>gnl|CDD|275071 TIGR04231, seadorna_VP5, seadornavirus VP5 protein. This protein family occurs in the seadornavirus virus group, with designations VP5 in Banna virus, and VP6 in Kadipiro virus and Liao ning virus. The function is unassigned
LRTISRTASVVIGIPSKLKFFDEKEEKDVILTASEFKSNNAFLFKDSGNLFLGLENIFRNSLDELKRILV
LAGGSTSKSKITQAGLSHLIEYCENYCLPDDAGVLKALCFIIFQIHDSSQRRGGVCTLFDILYNYLNQRN
LNQESGLLSYGLYKEKKVIYVNFKTVTYVCKNADAKAIKTELLNSKSHMTYADTIGSFRKSASINGGMDA
VTFLTIKMDASCTVFIFGKTYNVGPLYYRQLNAEVNALKKVLKNIGDHSRVKMHGNSRFGFVKPLDDAQK
SRSTGLIRALDDSNSIRFKSIGVGRDEKLSYAYDGCLLYYIKKIQNGNRGLCVTIDNINKLIEHKLLHDC
GLGHSCRDPSCGVKGCDDPALLSQLEERGHDIVANETMSDMCDEGEQETAAVETSEDAKLDSRIVQNKGS
RYMSASVYDKRHNLESAVVDDVQKYRLEEVKTGNSASGLLKAKESSGVLINDNTTFKINSDVVFDASSSV
IADTSKGISKPLKNK
>gnl|CDD|211955 TIGR04232, seadorna_VP3, seadornavirus VP3 protein. Members of this protein family are VP3 proteins in the seadornavirus group. Sequences show sequence similarity to methyltransferases
ELFSDDGSIVENFKERINKLVFDYSLNHDGTFRKTYKNQNDRMYYMLGDAYHANLSGKCLMIFNSEKDIF
EGLGFKSKGSEVNVSKTAILRNYEINFESIIGVEPNGLKAISTTKNGKRLYDIYSYKSSLHPIDDFKSHC
VDRWKMSLSPSLERIIRSLVIKYRNNYLRMFSELHNIIPTVEDSFSEMTHFTSMFRGPANVALIDNKLVT
EGVCFGAPVLSKSIEDGRLKNEFRTKGLIMTHNYYVLIGESPGPHYKKYTKFMNKDNCVFWDPRDTDHSD
IFTHIKSYFTNADIRRVVKYTSDALDQGLNPLVRIDIRKDKPKNLNGNENSEWERMVQEDNELTADLINA
LPENVTICAKLRPSYMKVNEMPKLSRPFRVLPLPYLRRSTAEFNMFVPRKELMNGTELRDVTYDDLVEMS
NEVCALKNIVGGLYNMYLKDQHLNLGVVNKAVNLSDNSSALWSLSNSNNMRITNFEFNNIRDYLYTAPYS
SFTTLVVNRQTHGRSYSDNCLNILDEINLIDGLYIPLYALPGGGQITSHDFVNVVVTDQEPLIDFTQPER
QLSTQVVKLVSFILKDSCTSKGLNWTELDNEIRSNRLESLSGVGFTVTKMLDGTVLVNDKVVTVSGHMLY
ILLGSILGLPYGIKRYLKEIELNILKPGSSYERGVGSRVWHGLHSHYLAVDCASDVITGLMMCTYDERSK
LNVVLNWVKSKLLELALKYNVYLNVDERLVI
>gnl|CDD|211956 TIGR04233, seadorna_VP8, seadornavirus VP8 protein. This protein family occurs in the seadornavirus virus group, with designations VP8 in Banna virus, and VP9 in Kadipiro virus and Liao ning virus. The function has not been assigned
FLDNPHPVGVNYVDSGSRQFARTTELLASKLIDGSRESLRSNNESPFVNAYSKFAGDNPRHLRVNTGGKR
ADALTRVIRSYYSINAPAIVPQIEIIRLGSKLTSSDDMANADAIFNTVPIIEVLSPAQTTVSIVGSKRAD
VTMLNTGAGAANITMSFGQAESVILKGSVPFQLARQGQAMQAAVFTYKLRSLDAGPYIFVIPAGNRMPFV
ISATAATSIDVPLAFNKALVESGFQRAKADGLFDTVNYYSSFDEFIIAQYHALPGINSTCAILGLLLEAY
EQVNRALPVRR
>gnl|CDD|275072 TIGR04234, putative_RNA-dependent_RNA_polymerase_VP1, seadornavirus RNA-directed RNA polymerase. Members of this protein family are the seadornavirus VP1 protein, the RNA-directed RNA polymerase
IYLGTLINRESREYEDLSSIKDERLNRLVEYDPGWYPLAVKIQRALDEGLSIESAKPIPYDPNFSNNIKH
PTKENKFLKVKVIKECDTFILMKDDNGIDDPDVIRAWDISTIPEFVELGGEIFNLRKEMIRRIKDEAPFY
FFCRIIPYAVTNIDKDDPMWREWLSYFIGGEDFFKFNGGSYDCSKSLLAHKRFEVALMHQRRIRKFPMDA
EALECMNEGAKYIMKDPIYRSYVLRGAFGDLNQHVFARTLGPNLGWSYTGVETTNFILSNVNGADGYQDR
FNLIDREAVEESLKELRMQGLPKNADLLLRNMTATINPVNLKKGKLNRMILSLCGYTGSHKASAAVKQFE
GTEDMGPNVTDEFFTAVSNNMFEYVREGFQPLERGMLDKSTRLDILFKGGTSSASSTNPHKSIGARYRYN
SPFIMDSDVDSKSIDVFDTYAPGKYVLTIISLKLKSKNANILTHPENFINFDHDNLDRVVNAGSRLVRGT
RAKRIITPNYGSIYALSLLTVLPAVRLLSSRRTNMSALSMNGRVGTTYLGALPHDVMAPQMAATSSSRSY
CAVALDFSQFDSSQGGRISKAHADGVRRVANEYFPGTNTDLSDVLDLLELSMSKFLYITSESYERPLKYK
SDGIVAEAAGVKSGELTTQLRNTVTNKAHTTQYLETYNRTKVRQGFRKIELVQENIVGDDKNVILRTADG
KPLTLRDAKLYINCAFDVAAENHLEISAKRSVVGNVVTEHIKIWVKKGYILLDVFLDSMTSEKNSFREMG
YMDGLNTLYDIAMTMMIRYAQNDPLMELMMNDMPLMEGVRHGKYTFIPTPKHLLASGGPEILPSAPELRG
FARYLHDYDSDLYSVMNSLNATLRSNSGTTQFESQVRKQLSEELNDNLVSPVWSEHFKRKNDYDVDDVGI
EMVTKLKKLMPEGCREYLVERVISTLKEPVILIMNDADIIENLLSGKLKKYQKPKFKYSNFFITIYGVSG
VSSPYLAADEGVRNVHKVIGLSRRNTKFPSPTERLSRLLRSYPGVHPAYLDGADILSALSGLGRSSQRWR
TVLELLDFSEMHASSFIQRLPNLMHRYLIEKNVNSTTLYDNTSRTYDVSDASMNKRVGIVSNNRANSSTS
RGYRFEGMKHVLYMARRGLSVHAS
>gnl|CDD|211958 TIGR04235, seadorna_VP4, seadornavirus VP4 protein. This protein family occurs in the seadornavirus virus group, with designation VP4 in Banna virus, Kadipiro virus, and Liao ning virus. Although this family has been suggested to resemble methyltransferases, members show apparent N-terminal sequence similarity to the outer capsid protein VP5 of the orbivirus group, such as bluetongue virus, which also belong to the Reoviridae
SQSSIISLTGNDRYVPDGSFNSALMPRAVIANEREHFMKTRIDRIEHDIIKSTKQEMMDRQVLKEDYKAL
ALAVGQEIKFDNATQHQLNRLGSAIYKADHEREKELTDLLNAINENEIAVNDIIENQKAITAAEKADLIL
EIVISTARAVAATGRAAADGVGVVPVFGPSVANGAKVGIDTAESVAETAIAVKASGIITQLNDVFHAFQS
VHVAPNDVIKPAVVVAGTSTDLIGKLKAIYDRLRRHNDIGFSKATVPDTIPNSYMVKPVVSDEYDSWQLY
VIHPVQGSLGLVVQMMGDALSYNVFAQYGTLDSSGFGKTILSGGATNTALEGTRVVKFQTKVTAQQALAM
TMALQSAVSMLSQGELVGYFEQYINLALEPDNLSVQDAMHKYHHLLTSDNSPIDWHYHDEEMLKWLDSRK
TTNYEAMKKKLGAGSSDIHVPKGFNDLRNTTLHCKLEGRQTIGGYTVYEYLIGPFAHYGDIDYSVVVDAL
NEETKWYCQVIGIDGQLLISKSIQHKPEKILELTVDDDGVTTIKGKNGDRLKLRIYVKDSLSVRVFRGWI
SGINTPRVKPKTFNDHKGVKYDYSHFDRNIDPAHLTLTIDLGWHTWEQYNAGNWTNIK
>gnl|CDD|275073 TIGR04236, seadorna_VP2, seadornavirus VP2 protein. This protein family occurs in the seadornavirus virus group, with the designation VP2 in Banna virus, Kadipiro virus, and Liao ning virus
PNKRSRTIKNDEKIQTGTVQTQDFKGAIQPDTVTAQLIKEAFNSRQVGDKGDIVYDSGSTSKLADVVDQG
PEPHNADGAVKDGRIAPVKLDLEKDKLDKAKLFETSPTDPLTVKNNQEVVDKLRAAQSSGIQKVVPTKEF
AVELQFGVDSEDMDAIYGALAAVSKENSSLVYEVKRGTHEIRKVPIGPHNLELITSDNGRHALIKEDLGF
WPIETGVSLVNQAGVLAVQLAKKYGLDKPFVLDAGSNYFTTSFIDTRKYCTDGLSYRQIVKALNAQRAYY
DRPELTPSENRTILSQSLIYDDTDGNSVSVVFDGAIKHAIFTYAQSQWNKNIIKLDDYIREITLTIPKHY
RPKEYSEIEHTHGYVYYELRQGSLRPLVDALLKECSSYFFKKLMSSISNVPVDSRTTQSSTSAIAADTGV
SMNRASHANMLLNRLTLSNAESVRAITILTCMFKNFRIGMTYAQDPNIMDVAAATFMLLFRPAQSISDEQ
YRSCLQTIASFLTNRTIDIINGNTTDQLRMELRNHGWPFVERYTPIQIDLSVSPLRSPGEIGKYYNPFNI
NSTKRHVEDDLSDFLNQMSVGRWRNANSNAVGALLSAFLRVARDKTSANWQGYSDVVSRYRSLIPNELAE
SLDNIRGEYNINPQDEVSYFFALARVNFTDEFIDAIDKMAAEYLDEYATLARDISNSLTLVRAIFSPLEP
TSASIVSYSNNLNRVIDHVWESAADKPLISETMLKLLAAAGTTGKDGYKNWLNKLVGHNDYPVYVEPLVN
IMNFVSAIFIANLSAFGITDEILIMPNHVNIPVDARFGGIFRDSPFVATMPVNDYRRISYYELSMMEDIA
EVISQGVIVYGVPFNYSYDIMTGDGVTKLREDIVIVTDTGNDIKPIEFYIYFENGNDKKAEYEDIMNVSY
RLYIKTPPNLLPISDYNRAQVDYVSADSSAVYIKDHAVLYTRL
>gnl|CDD|211960 TIGR04237, seadorna_VP9, seadornavirus/coltivirus VP9 protein. This model, broader than related pfam08978, describes proteins VP9 in Coltivirus, and proteins with various designations in the seadornavirus group: VP9 in Banna virus, VP10 in Liao ning virus, and VP11 in Kadipiro virus
MSSETELRALKRLSRTTNRVAGEQTLALPSNVKLSKGEVEKLAVTKKEMKDKLAQCNLPSIELNTREHTF
NGDFARFMAWAFIMHGQLLMHARPVAVRMNMQYATNVAGSAVKATNVASGNVVKLGYIQAGVLGGPYSNK
GSSLFITYEQNLIGSTIDTGKVNVLFQTSLTTASSTNSYAYSHCSVPITKWDPKMIKLTSETSCPSLTSM
TNLANSLVEGDRTPPVGLYVDIPGVTVTTSASLSSLPITTIPFNTPVIFSACVKDVEEVGVINTLYSLSY
>gnl|CDD|275074 TIGR04238, seadorna_dsRNA, seadornavirus double-stranded RNA-binding protein. This protein family occurs in the seadornavirus virus group, with an N-terminal domain for binding double-stranded RNA, is designated VP12 in Banna virus, VP8 in Kadipiro virus, and VP11 in Liao ning virus
NVVGMLQELAVKRGLELPVYEKVGKEGPDHAPTFTIKLTANDIEVIEAASSKKQAEKLAAATIYEDMKEN
GLLEVHDTRKSVSIMSILLVSKFFANALINKVIDLFSTCKQDIILCSDDVTFDYGLSNLMSSGLLLRSAW
YNRLYKLLSDLALENGFNCITRHFRSLLNDDLVANESFKNSILIVAFDTDEKKEVSMLVYA
>gnl|CDD|275075 TIGR04239, GlpG_protein, rhomboid family protease GlpG. GlpG in E. coli is a rhomboid family intramembrane serine protease that has been extensively characterized as a proxy for rhomboid family proteases in animals. It efficiently cleaves eukaryote-derived model substrates. This multiple membrane-spanning protein excludes inappropriate substrates from access to its cleavage site, and shows activity against truncated versions, but not full-length versions, of the E. coli multidrug transporter MdfA. This finding suggests a housekeeping function in removing faulty proteins. In contrast, several eukaryotic rhomboid family proteases release peptide hormones for signaling functions, and the Shewanella and Vibrio protein rhombosortase appears to be part of a protein-sorting system, cleaving a C-terminal anchoring helix domain
RLIQLSNPRLAQAFIDYMATQGIDLQLQPEEEGVALWLADEQQLAQAEAELDRFLQNPNDPRYQAASWQT
GETRTGLAYGSPSLLASFKAQAGPLTLSVMALCILVFLLMQLGGDQQVFSALAFPADPSQQSQLWRWFTP
ALLHFSLLHIIFNLLWWWYLGGQIEKRLGSGKLLVLFLVSALLSNWAQYLVSGPNFGGLSGVVYALVGYV
WLRGERAPESGLGLPRGLMGFMLVWLVLGFFDLLGMSIANAAHLAGLLIGLLMAFWDSRL
>gnl|CDD|213897 TIGR04240, envelope_protein, flavivirus envelope glycoprotein E, stem/anchor domain. This model describes the C-terminal domain, containing a stem region followed by two transmembrane anchor domains, of the envelope protein E. This protein is cleaved from the large flavivirus polyprotein, which yields three structural and seven nonstructural proteins
GKAFELTMRGAERMAILGDAAWDFGSVGGVFTSIGKALHQVFGGAFRALFGGVSWITKILIGVLLIWLGL
NSRNTTLSLTFLAVGGILLFLTTGVGA
>gnl|CDD|211964 TIGR04241, cr1_alpha_protein, mastadenovirus E3 CR1-alpha-1. This domain occurs only in the adenovirus E3 region CR1-alpha-1 protein. It may occur once, twice, or three times
TLYFTNSTTNITLNCSCFSTYILWTFNNSSCATYDNDGVLLPNNLSLTFSASSQKLTLFPPFVPGTYTCQ
AGPCQHTFKLV
>gnl|CDD|275076 TIGR04242, glycosyl_transferase_family_2, chitooligosaccharide synthase NodC. Members of this family are NodC, an N-acetylglucosaminyltransferase involved in the production of nodulation factors through which rhizobia establish symbioses with leguminous plants
DLLATTSTVAVSLYALLSTAYKSAQVFYARPTDVPATSSDALPSDPLPSVDVIVPCFNEDPRTLSECLAS
IASQDYAGKLRVYVVDDGSTNRDALVPVHDAYASDPRFNFILLPKNVGKRKAQIAAIRRSSGDLVLNVDS
DTTIAPDVVTKLALKMRDPAVGAAMGQLTASNRRDTWLTRLIDMEYWLACNEERAAQARFGAVMCCCGPC
AMYRRSALLSLLDQYETQLFRGKPSDFGEDRHLTILMLKAGFRTEYVPDAIAATVVPDKLGPYLRQQLRW
ARSTFRDTLLALRLLPGLDRYLTLDVIGQNLGPLLLALSVLTGLAQLALTATVPWWTILVIAAMTIIRCC
VAALRARQLRFLGFSLHTFINIFLLLPLKAYALCTLSNSDWLSRG
>gnl|CDD|211966 TIGR04243, polysaccharide_deacetylase, chitooligosaccharide deacetylase NodB. Nodulation factors are lipooligosaccharide signalling molecules produced by rhizobia, the symbiotic nitrogen-fixing bacteria that form nodules in plants. These Nod factor sustems have the NodABC genes in common but differ subtly in what they produce, which affects host range. NodB is a chitooligosaccharide deacetylase
SRSVYLTFDDGPNPFCTPQILDVLAEHRVPATFFVIGAYAAEHPELIRRIIAEGHEVANHTMTHPDLSRC
GPEEVRREILEANKAIRHACPQASVRHLRAPYGIWTDEVLRVAAKAGLTPLHWSVDPRDWSRPGVDAIVD
AVLANARPGSIVLLHDGCPPDEWASCSRAGLRDQTLAALSRLIPALHERGFVIRSLP
>gnl|CDD|275077 TIGR04244, nitrous-oxide_reductase_precurser, nitrous-oxide reductase, TAT-dependent. Members of this family are the nitrous-oxide reductase structural protein, NosZ, with an N-terminal twin-arginine translocation (TAT) signal sequence (see TIGR01409). The TAT system replaces the Sec system for export of proteins with bound cofactor
GLSRRGFLGTAALAGLAGAGASGGLGACAAAAAAAAAAAGGKYHVAPGELDEYYGFWSGGHSGEVRILGL
PSMRELMRIPVFNRDSATGWGITNESKKILGEGLLPETKKFLAADGQGKYLNGDLHHPHMSFTDGTYDGR
YLFVNDKANTRVARIRCDVMKCDKITEIPNVQGIHGLRPQKYPRTGYVFCNGEFEIPLPNDGRDLDDPKK
YVSIFTAVDADTMEVAWQVIVDGNLDNTDADYDGKYAFSTCYNSEMGVHLAEMMAAERDWVVVFNIARIE
EAVKAGDFKTLNGVPVVDGRKGANTAYTRYIPVPNNPHGVNAAPDGKHFICNGKLSPTVTVIDVRKLDDL
FDGKIDPRDAVVAEPELGLGPLHTAFDGKGNAYTTLFLDSQIVKWNIDKAIKAYNGEKVNPIVDKLDVHY
QPGHNHTSMGETKEADGKWLISLNKFSKDRFLNVGPLKPENDQLIDISGDKMKLVHDGPTFAEPHDSIIV
HRSKVKPRSVYDRDDPMFPDARKQAKADGVTLETESKVIRDGNKVRVYMTSQAPAFSLREFTVKQGDEVT
VYVTNLDKVEDLTHGFTIPNHGIAMEVGPQATSSVTFIADKPGVYWYYCQWFCHALHMEMRGRMLVE
>gnl|CDD|211968 TIGR04245, Nodulation_protein_A_NodA, N-acyltransferase NodA. Nodulation factors are lipo-chitooligosaccharides made by bacterial nitrogen-fixing bacteria as a signal to plant hosts. Nod factors differ slightly from system to system are serve as host range determinants. Because the N-acyl group varies from one NodA to another, the family treated as a subfamily, but all members of this family belong to NodABC systems
QVQWRLCWENELELADHAELAEFFRKTYGPTGAFNAKPFEGGRSWAGARPELRAIGYDSRGVAAHMGLLR
RFIKVGAVDLLVAELGLYGVRPDLEGLGIGHSIRAMYPVLQELGVPFAFGTVRHALRNHVERLCRNGLAT
IVSGVRVRSTLPDVHLDLPPTRIEDVLVVVFPIGRSMDEWPAGTLIERNGPEL
>gnl|CDD|275078 TIGR04246, nitrous_NosZ_Gp, nitrous-oxide reductase, Sec-dependent. This model represents the nitrous-oxide reductase protein NosZ as characterized in Geobacillus thermodenitrificans. In contrast to the related form in Pseudomonas stutzeri, this version lacks a recognizable twin-arginine translocation (TAT) signal at the N-terminus. Consequently, its accessory protein may differ. Some members of this family have an additional cytochrome c-like domain at the C-terminus
ALKTYVPPGKKDEFYAFSSGGHSGQVSVYGIPSMRLLKTIPVFSPEPWQGYGFDEESKPMLETGHGEIPW
GDTHHPALSETNGKYDGRWLFINDNANPRVARIDLRDFETKQIVENPNSSGNHGSPFVTPNTEYVVAATR
FSVPLPQAYVPIEEYKEKYRGVLTFVKFDPKKGRMDVKFQVELPPYSYDLSDAGKGPSHGWAFFTSYNTE
EAYPLLEVNASQRDKDYIAAVNWKKAEECAKEGKYKNINGKKVKVIDPADKPGALYLVPEPKSPHGVDVT
PDGEYIVVSGKLAPVITVYSFEKIQEAIEAKEFEGDEYGIPVLKYESVLEGEVELGLGPLHTQFDGKGYA
YTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPELPQSA
QLIDISGDKMKLLYDFPTIGEPHYAQAIKAEKIKPWEVYPLTENKHPYAVLSEGDARIERKGNEVHVYMT
AIRSHFTPDNIEVNVGDTVTFHLTNLEQDWDITHGFAIGGYNINLLLMPGETKTLKFVADKPGVYPFYCT
DFCSALHQEMQGYLRVKP
>gnl|CDD|275079 TIGR04247, nitrous_oxide_maturation_protein_NosD, nitrous oxide reductase family maturation protein NosD. Members of this family include NosD, a repetitive periplasmic protein required for the maturation of the copper-containing enzyme nitrous-oxide reductase. NosD appears to be part of a complex with NosF (an ABC transporter family ATP-binding protein) and NosY (a six-helix transmembrane protein in the ABC-2 permease family). However, NosDFY-like complexes appear to occur also in species whose copper requiring enzymes are something other than nitrous-oxide reductase
LQEAIDAARPGDTIRLAPGTYKGNIVIDKPLTLIGEGGAVIDGEGKGTVITIKAPDVTIEGLTVRNSGTS
LTEDDAGIKVEKADRAVIENNRLEDNLFGIYLQEAHDSLIENNRITGKPDLRSNDRGNGIHLWNSPGNVI
EGNTVRGGRDGIYIEFSHHNLIRNNTSHNLRYGLHFMYSNDNLVEDNVFRGNSVGYALMYSKRLTVRGNV
FLNNWGDAGYGILLKEINDSEIEGNTVLGNTKGLFIDNSPRNVFRDNDFEYNGIGIHFTAGSERNRFEGN
AFIGNREQVKYVGTRSLEWSENGRGNYWSDYEGYDLDGDGIGDVPYRPNDLFDKLVWRYPAARLLLGSPA
VQLLRWAQKAFPVLTPIGVVDSAPLMR
>gnl|CDD|211971 TIGR04248, SCM_PqqD_rel, SynChlorMet cassette protein ScmD. A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Members of this family are the PqqD-like protein
IANPLIVLREEFDDWAILFDPDDGQSFGLNPVSVFIWKRLDGKHTVSDIVSEIRNRFDEVPEHAEDSVRV
FVEDLIDRGLAGCE
>gnl|CDD|275080 TIGR04249, SCM_chp_ScmC, SynChlorMet cassette protein ScmC. A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Members of this family are designated ScmC
YILGLSAGKTWLISAEEPAQKWLDFFAHILGLSCSDGIPSMETDIIHSRAGSRPDFHPYTFLTEACRDPE
DEWLYRFQGTMQIRQNRYPQGIICDIDDSGPLAVQIVSMWYLLYPAYRRALERGGLPVHAALVEKDGEGY
LLAASGGTGKSTCCRRIGDPWRCHCDDESLVVPDTDKGYRAHPFPTWSNFLFGSEEKTWQSMRSVPVRAI
FFLEQAETDEVSPLNQAFAAAFLNDAALQFWHRYANFLEETLRKKLRIMIFRNACDIARVVPAYRLAASL
DGCFWEEMEKAL
>gnl|CDD|211973 TIGR04250, SCM_rSAM_ScmE, SynChlorMet cassette radical SAM/SPASM protein ScmE. A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the closer in sequence
TPRSVDIDITGRCNLRCRYCSHFSSAAETPTDLETAEWLRFFRELNRCSVLRVVLSGGEPFMRSDFREII
DGIVKNRMRFSILSNGTLITDAIASFLAATRRCDYVQVSIDGSTPGTHDRLRGTGSFLQAVEGIELLRKH
AIPVVVRVTIHRWNVDDLRPIAALLLDDLGLPAFSTNAASYMGLCRSNTDDVQLDTAERTLAMEILLELE
KEYPGRISASAGPLADARTWASMEQARIDQQGNMPGRGYLSGCGGIFMSLAVRADGVIVPCNQLSHIELG
RINRDSLRELWQNHPVLLQLRNRVTIPLTDFEFCKDCDYIPYCTGNCPALAYTTFGEINHPSPDACLRRF
LEEGGRLP
>gnl|CDD|211974 TIGR04251, SCM_rSAM_ScmF, SynChlorMet cassette radical SAM/SPASM protein ScmF. A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the more distant in sequence
HPLHQIYFYLTEGCNLKCRHCWIDPKYQGEGEQHPSLDPSLFRSIIRQAIPLGLTSVKLTGGEPLLHPAI
GEILECIGENNLQLSVETNGLLCTPQTARDLASCETPFVSVSLDGVDAATHDWMRGVKGAFDKAVRGIHN
LVEAGIHPQIIMTVTRRNVGQMEQIVRLAESLGAESVKFNHVQPTSRGSKMHENGETLSIGELVALGEWM
ERTLIPSTALRIDFGHPPAFRPLGRMFGEKPGGCGLCGIFGILGVLSDGSYALCGIGESIPELVFGNAGS
DRLDSVWSENPVLNEIRNGMPGRLEGVCGECLMKEKCLGSCIAQNYYAKRHLWSPFWYCEEAYEAGLFPS
SRL
>gnl|CDD|211975 TIGR04252, SCM_precur_ScmA, SynChlorMet cassette protein ScmA. A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. This model identifies a conserved open reading frame that was identified as a predicted gene in only one of those species (Chlorobium), but that may represent the ribosomally produced peptide precursor of the system. As with most other radical SAM enzyme-modified ribosomal natural products, these polypeptides are Cys-rich in the C-terminal half
YQEPKIISLAEKAAGGSSCRCGSGSSPNCSTGGSPRSAGACGAGYNAGG
>gnl|CDD|211976 TIGR04253, mesacon_CoA_iso, mesaconyl-CoA isomerase. Members of this protein family belong by homology to the family of CoA transferases. However, the characterized member from Chloroflexus aurantiacus appears to perform an intramolecular transfer, making it an isomerase. The enzyme converts mesaconyl-C1-CoA to mesaconyl-C4-CoA as part of the bicyclic 3-hydroxyproprionate pathway for carbon fixation
GILHGLRVVEGSAFVAAPLGGMTLAQLGADVIRFDPIGGGLDYKRWPLTLDGKHSLFWAGLNKGKRSIAI
DIRHPRGQELLTQLICAPGDHAGLFITNFPAKGWLAYDALKAHRADLIMVNLTGRRDGGSEVDYTLNPQL
GLPFMTGPTSSPDVVNHVFPAWDFISGQMIALGLLAAERHRRLTGEGQLVKIALKDVALAMIGHFGMIAE
AMINDADRPRQGNYLYGAFGRDFETLDGKRLMVVGLTDLQWKALGKATGLRDAFNALAARLGLDFDDEGD
RFRARHEIAALFEPWFHARTLAEAALIFDAHGVTWAPYRSVREAIAADPDCSTDNPMFALTEQPGIGRYL
MPGSPLDFAAVPRLPAMPAPRLGEHTDEILLDILGLSEAEVGRLHDAGIVAGP
>gnl|CDD|275081 TIGR04254, hypothetical_protein, putative globular PEP-CTERM protein. Representatives of this family include a 13-member paralogous family of proteins about 215 amino acids in length from the termite gut bacterium Opitutaceae bacterium TAV2, a member of the Verrucomicrobia. The signal peptide (N-terminal) and PEP-CTERM putative protein sorting signal (C-terminal) are not included in the seed alignment. Conserved residues such as an invariant Arg and a lack of conspicuous low-complexity sequence suggest a globular structure and possible enzymatic activity. Members average about thirty percent sequence identify overall, but over seventy percent in the PEP-CTERM region. The function of this family is unknown
DGASGADGYIATFWYGTTDQGDLTLVGAGTFLDAYYDGPEYAGLFGWSTFLAGGWLNTGTTFYAEIRVFQ
YTPGTVITQTYVEGLYADDALASFWNLIQGTEVSQGEVTGTFTTPPDGTVTGVTSTFTTLDLVLSG
>gnl|CDD|275082 TIGR04255, hypothetical_protein, TIGR04255 family protein. Members of this uncharacterized protein family are found broadly but sporadically among bacteria and archaea, including members of the genera Mycobacterium, Nostoc, Acinetobacter, Planctomyces, Geobacter, Streptomyces, Methanospirillum, etc. The function is unknown
RLKNAPLVEVIIEIRFPPILNLSSEALFGMLQERLKDDYPLIEEQPSVEINIPEDGRGPDPNLEYVPLYR
FVSEDGTWLLQLGPNSLTFSTTPYPGWEDFKEEFLSLLDALKEIYKPPEVSRIGLRYIDEIRVPDGEESW
SDYLSPELLGLPGGLEGFFLSESIQLRTELLDDGFVLVVRIGLQPGPTELGNPPPTEEPGFILDIDVFVE
GRSPIDFDEEIIDILDALHEIVKKLFFKLITEELLERFG
>gnl|CDD|275083 TIGR04256, conserved_hypothetical_protein, GxxExxY protein. Members of this protein family average about 130 residues in length and include an almost perfectly conserved motif GxxExxY. Members occur in a wide range of prokaryotes, including Proteobacteria, Perrucomicrobia, Cyanobacteria, Bacteriodetes, Archaea, etc
ELTYKIIGAAYEVHRELGPGLLESVYEEALAIELRKRGLPVERQKPLPVIYKGIVLGEGYRADLLVEDKV
IVELKAVEALTPVHEAQLLNYLKLTGLKLGLLINFGVPKLKIKRIV
>gnl|CDD|275084 TIGR04257, cytochrome_c_family_protein, c(7)-type cytochrome triheme domain. This domain binds three hemes, and itself occurs as a repeating unit. It occurs, for instance, four times in the dodecaheme c-type cytochrome protein GSU_1996, whose crystal structure shows elongation and a nanowire-like arrangement of twelve hemes that could function in extracellular electron transport processes
KDITFKVKGAGPVVFSHDFHLGKYKCGDCHNKLFKAGAGNKRVTMAEMEKGKSCGACHNGKKAFSVAGNC
DKCHK
>gnl|CDD|275085 TIGR04258, hypothetical_protein, four helix bundle suffix domain. This domain occurs as a suffix domain to some members of the much broader protein family TIGR02436, a few of whose other members are encoded within intervening sequences of bacterial 23S ribosomal RNA. Some proteins with this domain, in turn, are followed by a predicted DNA topoisomerase type C4 zinc finger
DEVAANIAITLIHQADYLLDRQLEKLEEDFLEEGGFRERMYRARLEYRA
>gnl|CDD|275086 TIGR04259, oxalate:formate_antiport_protein, oxalate/formate antiporter. This model represents a subgroup of the more broadly defined model TIGR00890, which in turn belongs to the Major Facilitator transporter family. Seed members for this family include the known oxalate/formate antiporter of Oxalobacter formigenes, as well as transporter subunits co-clustered with the two genes of a system that decarboxylates oxalate into formate. In many of these cassettes, two subunits are found rather than one, suggesting the antiporter is sometimes homodimeric, sometimes heterodimeric
RWLQLVIGVVCMCMIANLQYGWTLFVNPIDATHGWGRAAIQVAFTLFVVTETWLVPIEGWFVDKYGPRIV
VMFGGIMCGLGWVLNAYADSLPALYAAAVVAGIGAGAVYGTCVGNALKWFPDKRGLAAGLTAAGFGAGAA
LTVVPIAAMIKVSGYQAAFMYFGLGQGIVIVLLALLLRAPSPGQVPKQARVVQTRRDFSPGEMLRTPVFW
VMYTMFVMVAAGGLMATAQLGPIAKDFGVADVPVTLLGLTMAALTFALSIDRILNGFTRPFFGWISDKIG
RENTMFVAFGIEGVGIYLLPTFGHNPVAFVILSALVFFAWGEIYSLFPATCADTFGSKYAATNAGLLYTA
KGTAALLVPLASILSTSTGWNAVFLIAAALNILAAALALFVLKPMRRRVKRQVKL
>gnl|CDD|275087 TIGR04260, hypothetical_protein, rSAM-associated Gly-rich repeat protein. Members of this protein family average 125 in length, roughly half of which is the repetitive and extremely Gly-rich C-terminal region. Virtually all members occur in the Cyanobacteria, in a neighborhood that includes a radical SAM/SPASM domain, often a marker of peptide modification systems
MNITTLISLVGFLLASAVLTVSAAAAVSSQPDAGNNAIEARLERISNAIQQRWGILISNEIGGADGNLIA
RGWGNGGGRGWGNGGGGGGWGNGGGGWGNGGWVNGGGWRNGGGGFANRW
>gnl|CDD|211984 TIGR04261, putative_arylsulfatase_regulatory_protein, radical SAM/SPASM domain protein, GRRM system. Members of this protein family are radical SAM/SPASM domain proteins (see pfam04055 and TIGR04085) related to anaeroboic sulfatase maturating enzymes and the peptide modification enzyme PqqE. Members are found primarily in Cyanobacteria adjacent to a short protein, ~150 residues, in which the last ~60 residues tends to be repetitive and highly glycine-rich (see TIGR04260). The arrangement suggests modifications to the repetitive C-terminal region by this radical SAM domain enzyme, but the purpose of this system on the whole is unknown
IQPTSFCNLDCDYCYLPDRQLKNRLSLDLIEPILKRILESPFVGPGFTICWHAGEPLTVPISFYDEATEI
IREALEEYNQQPVQIEQSVQTNGTLINQAWCDCFKRNRIVVGVSLDGPAFIHDAHRRTRTGRGSHAATMR
GIRALQKNEIPFSVIAVLTEDSLDYPDEIFDFFRDNGITDVGFNMEETEGVNTSSSLQGQGTEERYRAFL
QRFWELTAQAGGELRLREFEDICSLIYTGQRLLQTDMNRPFAIVSVDHQGNFSTFDPELLSVKTDHYGDF
ILGNVLTDSLESACQTEKFQKLYQDMTAGVELCRQTCDYFGLCGGGAGSNKYWENGTFNSSETQACRYRI
QIVADVVLEALEE
>gnl|CDD|275088 TIGR04262, possible_ABC_transporter_solute_binding_protein, extracellular substrate-binding orphan protein, GRRM family. This subfamily belongs to bacterial extracellular solute-binding protein family 3 (pfam00497). In that family, most members are ABC transporter periplasmic substrate-binding proteins. However, members of the present subfamily are orphans in the sense of being adjacent to neither ABC transporter ATP-binding proteins or permease subunits. Instead, most members are encoded next to the two signature proteins of the proposed Glycine-Rich Repeat Modification (GRRM) system, a radical SAM/SPASM protein GrrM (TIGR04261) and the Gly-rich repeat protein itself GrrA (TIGR04260)
GVLRAVVRGDVLPLYQKDDAGYDGLSFDVLELIRDQLQAELGKPITIQFVVVNSVQEGLPKLRSGKADIA
CGVAFTWERQMFVDYSLPFAVSGIRLLAPKGNDGTPESLEGKTVGVVKDSVAAAVLANVVPKATLQPFAT
PAEALAALKAGKVDALAGDSLWLAANRQRAAPNDDLVPDQPYARSGIGCIVPENNSKLLNLSNIAIGKLL
QGYVDGDAKVRTMINRWIGPGSDVGLPPDLIKDYFETVLSTTAEFPL
>gnl|CDD|275089 TIGR04263, cell_wall_surface_anchor_family_protein, SasC/Mrp/FmtB intercellular aggregation domain. This domain, about 375 amino acids long on average, occurs only in Staphylococcus and Streptococcus. It occurs as a non-repetitive N-terminal domain of LPXTG-anchored surface proteins, including SasC, Mrp, and FmtB. This region in SasC was shown to be involved in cell aggregation and biofilm formation, which may explain the methicillin resistance seen for Mrp and FmtB
TTANTDPLNANETGPGIINGNFTFDSGGILPSTNRSRPAVTVVSNLPGWTSVNGGKVGELPLVLTRTAVF
DYGDPMNDQASGNGVVLGRYNGNDNNDHGDPDFNGIYQDIDVVPGSELIVNFISTTMTTNNGKGGAKLVI
KNANNDTELADKRVNGGGYPTGGLSRLFNVPDNVNRLRLQFLPINNISTDTRRITRLLDGYNYYGGGFVD
NVGVNSGSYLVSYVKQTEYNATATSATDFTVNATIENNGENKGHLSSNKTVYKVTLPEGVTYVSNSGATS
NYDRNTNTLTFSSNGLTPGTSKDITYTVRLPNSTPKEVDFNGTLTYKTDADFRGNGTQKTGTNTVDPQTV
TVIMNKDDLQAKVNKI
>gnl|CDD|275090 TIGR04264, hypothetical_protein_SAO11_2114, hyperosmolarity resistance protein Ebh, N-terminal domain. Staphylococcal protein Ebh (extracellular matrix-binding protein homolog) is a giant protein, sometimes over 10,000 amino acids long as reported. This model describes a non-repetitive amino-terminal domain of about 2400 amino acids
DKDKLQAFFDASYHDYRFIDRDKADNKEYNQVKATFDKVNTFLGNNDNPNSKSLQLLYKELEQAVALIRT
LPQRQVRTRRNNREARSVRSRRAESRSVGSYNNAKTEYYVENENDGSGYPSGTYIHASNKGAPYYLPTTP
WNTLSASDVKGIAYITAKRVKDGYEWTINFNKGHIPHENMIFWFGLPKDQTPVGPVRFSITDPNGTNTSS
SSGVGDGEGQPLPRMWDSAGGIDPSRAYNFRQGPRTGYEFYDWPTVHINNFGDFARAPEYFNREGAPNKA
RVYGDQNFRYLNGEVPDQIQGLDTIYAFIGKGNASYTIQFKTQGPTTDRLYYAAGGRALEYNQLFNYNQL
YVEPLEEYQDRIQSIVDVINRTYHLGNTKNVYDVPERRYVTKHILDSDDFNTHDYADDPLSYVRNPSNHV
IGFFPYNAPTDRYRHGGVNPLNSYEIHQLFSEEKLKEAARTGNPIKLMIGFNVPDRYGNGETLKPVNLYV
KPELQQNIGFFSNNETQNREESPESKAAGHPVFLVQAGNMGNTSTNGGNKDTYVQPIRIQLTSNEPFSDN
DWEISGIPPTLRIENAVGRTNNAREKNLELVGNLPPGDYFGTVRLGNREQIFEIRAKPNPPTISTTAAQL
RGKGGQKPTITVTNVPQDTNAKVYLVAGGNGATDGTNDPGTIPSGYTILASATATGTGNTVTFNPSDYIQ
PLPNNGVIRAITYYNKSVQSNFSNAVTILPDDTPPTISNPVGLQNKYYRGDQVNFTIPVSDNAYGTGIKQ
VSVTGLPQGWTSNFVKNANGEAGTLTITGTISNSQTFNSDILVQVSATDNANNTTQTKTIAIHIGKLSDD
KPPIVLSNQEKIVVVNPTSISQDERNDIINALKAKNTNISSYLATSNPYMVDNNGNVVLTYKDGSTRRID
PTNVITYEPIRKSIYAEGNNTKEATITIAKGQEFEIGDLKQYFSLSNGQDIPNNSFTTITANDTIPTPQQ
ISRLNAGTYTYHINASNAYNQDTERLTIKLKVVDVNQPSGDQRVYRTSTFNLTDDEINQVKQAFINANRG
QLNLTDSDITVNNTPNSNHVSTVTVTITKGKLTKSFTSNFDHMNFLRWVNFPNDYTVTWTSQKIPGRGTD
GGFEWSPDHKSLIYRYDATTGRQITLNDVLSLLTATTSIPGLRNNISGQEKALAEAGGTPGYKPVGYSKT
NSISDGLRQYTYNGQVIQVLDLVQSSTGYGGQPVTYSNYRSNSSNSTVVNGNIPAANGAPAFTLDHVIKQ
NSGNGVMGAVYKAQLYLTPYGAKQYIERLNQSTDNTTDVINVYFVPSDKVKPTISLGNYNNHVVFSGETF
RNTITATDNYGLKSVTVPQTSQIAGTVNNNNQIISGVAPNVTTPTTKTVKVIATDTSNNETTQSFNVTIK
PLKDKYRVTTSSTEQNPIRIANIRNNATLSQADKQAIINSLTITNNIPNRNYVTAGANEIRSKEVSNVSR
TGNNANVTVTITYADGTTSQITVPVKHVIPEIVAIPRYTVQGQNFPAGKGANPNDFFKLNNGSPVPDATI
TWVNGNGPNINSTRIGVDITVRANILFDGETTPIEKEASYMVVKSVPKRVFETTRNGNFPGINNSYNPGS
YVQPINNSWPQGAQAMNFDFGPNSGGPNSNVVGIFTRTIRVTYPNGQVENVKVLAKVKPDPPRIDSNSVT
YKAGLTNQQIKVNNVLNNSPVKLYKSDGTELTNTTTTYGSNGSATVTVSGALPLGNIKAKSSITVNNVTY
TTQNNSGQVVNVTRNESVESDDSAPVRVTPQLHATNGGAKFVKGGDNFDFNNAARYIDNLPDGATVEWED
NPDTWKNTVGNTTKTAVVTLPNGQGTRTVNIPVKVYPVATAKAPQRDVKGHQLTYGTDAMNYVTFEPNTN
MNGITATWKNNNQPNNNQAGVQNLTANVTYPGISTPYRVPVKVYVYKFDFAQSEYTTTVGTTFAGGTNVN
NYVHLENANGLPTDGFHYVWNQATTGSNSEQWSALAKPNQAFVKNAKYDVLDNGNHVFATSQPAKFIVTN
VQPNKATITESDVGDITITPGANKSVNTRTGNVTTYADRLVIKKNGQVITTFIRANNTSPWTKESSAINV
PGVSGSPNGITINAGTFPPGDNIQVVATQGNGELISDEAISDTFTVVAPQPNQATSKIWQNGTFEITPNN
PNAHTTNPTDAVEITYTEKLGNSTEQSKTLTVTKGNNGQWSITNKPDYVTLDSATGKVTFNANTIKPNSL
ITTISKAGSGNTESTNTNTITAPAAHTVTIHEIVKDYGSNVTNEEINNAVQVANKRHATIKQGTALPTNL
AGGSTTTIPVTITYNDGSTEEVTETIRTKADKRELINARNHLDD
>gnl|CDD|211988 TIGR04265, bac_cardiolipin, cardiolipin synthase. This model is based on experimentally characterized bacterial cardiolipin synthases (cls) from E. coli, Staphylococcus aureus (two), and Bacillus pseudofirmus OF4. This model describes just one of several homologous but non-orthologous forms of cls. The cutoff score is set arbitrarily high to avoid false-positives. Note that there are two enzymatic activites called cardiolipin synthase. This model represents type 1, which does not rely on a CDP-linked donor, but instead does a reversible transfer of a phosphatidyl group from one phosphatidylglycerol molecule to another
TLVSWILILGFILNLAFAFIIIFMERRAAPSTWAWLLVLYILPLVGFILYLAFGRLHLGKRRAEKKAIED
ARAFWPITAQQLNDLKAENHIFANEQSQKAAPLFKMLLRNQGIFLTEGNQLKLMTDGDDVYDALIQDIKN
ARHYIHLEYYIWQPDGLGDQILESLMAKAKQGVHVRILYDDVGSVALFKSWPELFRNAGGEVVAFFPVKL
PLLNLRMNNRNHRKIIVIDGQIGYVGGFNIGDEYLGKDAKFGYWRDTHLRIEGDAVTALQLIFILDWNSQ
TGRRIIPYDPDYFPMPNEQAGGHGIQIIASGPDFPWEQIKYGYLKMIYSAKKSIYIQSPYFIPDDDLLHA
IKIAALSGVDVSIMIPNKPDHPLVFWASRSNFTELLAAGVKIYQYENGFLHSKSVLVDDEIASVGTANMD
MRSFWLNFEVNAFIYDKGFAKDLAAAYDDDISRSRQLTKRLYAKRPLWQRFKESLSYLLSPLL
>gnl|CDD|211989 TIGR04266, NDMA-dependent_methanol_dehydrogenase, NDMA-dependent methanol dehydrogenase. Members of this family belong to the iron-dependent alcohol dehydrogenase family (see pfam00465). The NADP(H) cofactor is bound too tightly for exchange (although non-convalently), so enzymatic activity depends on a second substrate or electron carrier. The radical SAM-modified natural product mycofactocin is proposed to fill this role. In Rhodococcus erythropolis N9T-4, a role was shown for this protein in CO2 fixation during extreme oligotrophic (or possibly chemoautotrophic) growth
ELNQIWDFPIKEFHPFPRALLGVGAHDIIGVEAKNLGFKRTLLMTTGLRGSGIIEELKGKIEYQGVEVVL
YDKVESNPKDYNVMEAAALYQSEKCDSIISIGGGSSHDAAKGARVVIAHDGRNINEFEGFAKSTNKQNPP
HIAVSTTAGTGSETSWAYVITDTSDMDQPHKWVGFDEATIVTLAIDDPLLYYTCPQHFTAYCGFDVLAHG
SEPYVSRLDFAPSLGNALYSVELVAKHLREAVFEPRNLKAREGMMNAQYIAGQAFNSGGLGIVHSISHAV
SAFFDSHHGLNNAIALPRVWEYNLPSRYERYAQLATAMGVDTRNMTTVQAADAAVEAAIRLSKDVGIPDN
FGQVRKDSYDKNRMNTGKYSGRGPVIKGDDKTVRAISEHIQGDWCTPGNPREVTVESMIPVVSHAINKSY
>gnl|CDD|275091 TIGR04267, hypothetical_protein, HEXXH motif domain. Some proteins with this domain toward the C-terminus have an N-terminal region with a radical SAM domain (pfam04055) and a SPASM domain (TIGR04085), a combination frequently associated with peptide modification. All seed alignment members, and all family members that are not fused to a radical SAM domain, have a motif HEXXH that suggests metalloprotease activity. A role in peptide or protein maturation is suggested
FDALAAGGGGAAAVRELRAAQRSRRLLLLRALLDRARDRAPAGATLPGADRAWELLEEAERRAPAAVAAV
LLHPSVGAWAARCLRRLRAPSDGPLAADLGYLGAIAAAAALRAGLPFRLAVPLRDGRLLLPTLGRVLLPE
AGDGAATVVTAGGSLRVGGAGETVSVPGPREGAPGWRPIRRLRAEAGGRRLSVLLDDADPYRMCDGPPAV
RPARRLTAAAARRWQSALAAAWRLLRRTDPAYAAEVAAALRALVPLPSSGPGRSVSASSADAFGAVALSL
PADAEDLAETLVHEFQHAKLGALLDLVPLVDPDDSPLYYAPWRDDPRPLEGLLHGVYAFLAVADFWRRRA
ARGEDGAARRRAAFEFARWRDQVAEALDVLRASGALTPLGRRFVDGLAA
>gnl|CDD|275092 TIGR04268, FxSxx-COOH, FXSXX-COOH protein. Members of this family are very short (~60 residue) polypeptides, among which the fifth and third to last residues are nearly always Phe and Ser, respectively. Because members occur in a conserved context with a putative peptide-modifying radical SAM/SPASM domain protein, we suggest that members of this family may be the modification target. The gene symbol fxsA reflects both the FXA motif and the proposed role as a ribosomal natural product
VDLTDLPLADLDGLPSSALARALRRVLDEAAPRREAVAAFDSSL
>gnl|CDD|275093 TIGR04269, radical_SAM_family_protein, radical SAM/SPASM domain protein, FxsB family. This model describes a radical SAM (pfam04055)/SPASM domain (TIGR04085) fusion subfamily distinct from PqqE, MftC, anaerobic sulfatase maturases, and other peptide maturases. The combined region described in this model can itself be fused to another domain, such as TIGR04267, or stand alone. Members occurring in the same cassette as a member of family TIGR04268 should be designated FxsB
IRQFVLKVHSRCDLACDHCYVYEHADQSWRARPKVMSAETRRAFARRLAEHAAAHDLPSVAVILHGGEPL
LAGAERLRAFAAELRSALDPVTALDLRLQTNGVLLDDEALDLLVEHDIGVGVSLDGDRAANDRHRLTRDG
RSSHDQVLRALELLRRPEYRHLFAGLLCTVDVANDPVAVYEALAALDPPRIDFLLPHATWDRPPPRRGPD
GSPTAYARWLLAVFDRWLADGRPMPVRTFDSLLSTLRGGPSLTEALGLGPVDLAVIETDGTYEQLDSLKV
AYDGAPATGGDVFDHTIDEVAAHPGIAARRAGLAGLSETCRACPVVDSCGGGLYPHRYRSDSGFDNPSVY
CADLKALIAHVQE
>gnl|CDD|211993 TIGR04270, Rama_corrin_act, methylamine methyltransferase corrinoid protein reductive activase. Members of this family occur as paralogs in species capable of generating methane from mono-, di-, and tri-methylamine. Members include RamA (Reductive Activation of Methyltransfer, Amines) from Methanosarcina barkeri MS (DSM 800). Member proteins have two C-terminal motifs with four Cys each, likely to bind one 4Fe-4S cluster per motif
YAIALDLGTSGFRAQAINLEDRETLSTVITSRHPLPGANVMDHMDFAINYGQEVAHGLIVEAVNRLIAAL
DVPLEEVSRFAVCGNPIQLSLFQGIEIRDLAYAGKNKLEKLGVQVPTRNARVIKASEIPGLDLFPDCDVV
IPPAIKHEIGADALAMIVKSGMLDRDEISLVTDYGTNAEMALKVGGRIYTGSAAAGPALEGQQISCGMLA
SPGAICDLEPEGGFWRNMVLDEEMKPVPGPLVDPRTGEFKESGNPRPAKGITGTGVIAAIYLGIECGLIE
LPHIKTPDGKIHLGEDIYLTEKDLIEAGKAIGAIRAGHITLCVEAGIAYEDIDTVYMSGASGTYVDAEKA
QKLGLIPARVKKIVQVGNTSLAMARDLVLNPDRLSELQEIARKIKGNHIMFATSPTFKKIYVLELAYWTE
GMPLEKYNSLLERYGLPDLPEVAGTPEIERLVEKDIEDLGVMGLTILEEVGTSLEAQVEGCIACQKCVKE
CPGKALSILESEPPRIDTDRCLGTACRRCERVCPEKVFDIRNFFS
>gnl|CDD|275094 TIGR04271, thiamine_biosynthesis_protein_ThiI, thiazole biosynthesis domain. The ThiI protein of Escherichia coli is a bifunctional protein in which most of the length of the protein is responsible for sulfurtransferase activity in 4-thiouridine modification to tRNA (EC 2.8.1.4 - see model TIGR00342). This rhodanese-like C-terminal domain, by itself, is able to synthesize the thiazole moiety during thiamin biosynthesis. Note that the invariant Cys residue in this domain is unusual in being required for both activities of the bifunctional ThiI protein
IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKT
YLLYCDKGVMSRLQALYLKEQGFTNVKVYRP
>gnl|CDD|275095 TIGR04272, hypothetical_protein, CxxC-x17-CxxC domain. This domain, with a pair of CXXC motifs separated by 17 amino acids, is a candidate zinc finger domain based on these motifs. Some proteins have two copies of the domain, while others are fused to another probable zinc-binding domain, described by pfam13451
REMYEAVCAECGQETQVPFKPTGDRPVYCRECFQKRR
>gnl|CDD|275096 TIGR04273, activator_of_XA21-mediated_immunity_Ax21, sulfation-dependent quorum factor, Ax21 family. This family consists of proteins closely related to Ax21 (Activator of XA21-mediated immunity), a protein that is secreted by a type I secretion system (RaxABC), and that appears to be sulfated on an N-terminal region tryosine in a motif LSYN. Ax21 acts in a quorum-sensing system. Homologous peptide-mediated quorum-sensing systems appear to exist in other species, such as the emerging opportunistic pathogen Stenotrophomonas maltophilia. Intriguingly, the rice genome encodes a receptor (XA21) for this protein that triggers innate immunity [Cellular processes, Pathogenesis]
LALGLLAALPFAASAAEGLSYNYVEGGYVRTDADGQDADGWAVKGSYAFAPNFHVFGDYSKQKTDSTDLD
FQQWRVGVGYNYEIANHTDLVARVAYKRFDLSSPNINFNGWSAEVGLRTAFGPYLEVYALAGYEDYLKKD
GIDPDGQFYGRLGAQAKFNQNWGLSGDMKMGKQGDKEWFVGPRFTW
>gnl|CDD|211997 TIGR04274, conserved_hypothetical_protein, hypoxanthine-DNA glycosylase. Members of this protein family represent family 6 of the uracil-DNA glycosylase superfamily, where the five previously described families all act as uracil-DNA glycosylase (EC 3.2.2.27) per se. This family, instead, acts as a hypoxanthine-DNA glycosylase, where hypoxanthine results from deamination of adenine. Activity was shown directly for members from Methanosarcina barkeri and Methanosarcina acetivorans
GFPPVLPSDPRILILGSLPGNLSLRKQQYYAHPGNQFWRIIESLIGEPHSLNYPTRIELLKRHGIALWDV
CAACEREGSLDSNIKDEVPNDINELVEMHPTIKLILFNGQKAGKLFKKHFRDIPGIETIILPSTSPANAR
LSFEEKLNNW
>gnl|CDD|275097 TIGR04275, beta_prop_Msarc, beta propeller repeat, Methanosarcina surface protein type. This model describes a repeat region found mostly in cell surface proteins of various methanogens. Methanosarcina barkeri, for example, has twenty such proteins, often with either seven or fourteen repeats. These repeats resemble the beta propeller repeats of the TolB periplasmic protein of Gram-negative bacteria, part of a complex associated with various functions including biopolymer transport (see TIGR02800)
ETQITTDGSDQINPAIYGDRVVWEDNRNGNWDIYMYDLST
>gnl|CDD|275098 TIGR04276, conserved_hypothetical_protein, FxsC C-terminal domain. This model describes a sequence region found regularly as the C-terminal domain of a protein (where the N-terminal domain resembles a TIR domain - see pfam13676) in the vicinity of a proposed peptide-modifying radical SAM/SPASM domain protein, FxsB (TIGR04269)
VQITVAAPTRDDLPEGRSPDYYGPTPRDWNPYHPASHRPLAELAAALVRDLGYQVNVVPFDEEQDRLRET
APPRQPLILLVDPWALRVPQLRRQLAALDERNRPATGVLVPRAPDDLESAERGDRLRELLLRTLPRRLSR
GRSPHSELFRVGVRTADAFGRWLATVVEAAQNRYLRHARTYPGSAVPGPARPRLGG
>gnl|CDD|212000 TIGR04277, MYND_finger_family_protein, squalene--tetrahymanol cyclase. This enzyme, also called squalene--tetrahymanol cyclase, occurs a small number of eukaryotes, some of them anaerobic. The pathway can occur under anaerobic conditions, and the product is thought to replace sterols, letting organisms with this compound build membrane suitable for performing phagocytosis
IIGIFLFSSVNAKVDIEEVQNAIRDAQEICWAELHDNEWVYPPYLGELFISEYYFELKALGWIHKSAFEA
SKFTEILLGSQFEDGSWEQVEDANIETGQLDATIFNYWYLKAIGIDIHIDAALKKAQEWIKANGGIEAAQ
TMTKFKLAAFGQYPWEDLFKIPLFIFKKKGIFKPLYIKDITAQWVYPHLTALAYLQNQRIIFNVAVADIR
ELWINKAKKGIKHQKKERPSFFIDNDLLILMDEIFKLKQPLGSFGAYTISTLLSLLAFKDFQGKHPHKHK
NEIQDALEDGLDFVEFNYFNFREAYHGSLDDGRWWDTILISWAMLESGEDKEKIFPIVENMLKEGLQPKG
GIEYGYDFEYAPDADDTGLLLQVLSYYGEAFADAIDEGAEFLFSMQNDDGGFPAFDKGKMEDNLLFKFAF
KIAGIADSAEIFDPSCPDITAHILEGLGEFGDQANHDQIQKMIKYFMDTQEKFGSWEARWGINYIMAAGA
VLPALAKMNYDLNEGWAKNAINWLLNKQNADGGFGECTLSYNDPEKWNGIGKSTVTQTSWGLLALLAVED
HNDQIKEAADKAAQYLLDQFKRDDGEFKDHSTIGTGHRGLLYLQYPSYAQSFPLIALGRFLDIQ
>gnl|CDD|212001 TIGR04278, viperin-like_protein, antiviral radical SAM protein viperin. Viperin (Virus Inhibitory Protein, ER-associated, Iterferon-inducible) is a radical SAM enzyme found in human and other vertebrates. It is both induced by interferon and demonstrably active in blocking replication by several types of virus, apparently by modifying lipid chemistries in lipid droplets and membrane rafts
LLSAFRQPLGSLWSSLLSLLCWLRAALWLAGSEKSRQQLRGEPTRKEEEEDPDQPTTPTSVNYHFTRQCN
YKCGFCFHTAKTSFVLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRGEFLGKLVQFCKEELQLPSVSI
VSNGSLIRERWFKKYGEYLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRNWCRDYKVAFKINSVI
NRFNVEEDMREQIKALNPVRWKVFQCLLIEGENAGEDALREAERFVISDEEFEGFLERHKSVSCLVPESN
QKMRDSYLILDEYMRFLNCRNGRKDPSKSILDVGVEEAIKFSGFDEKMFLKRGGKYVWSKADMKLDW
>gnl|CDD|275099 TIGR04279, TIGR04279, TIGR04279 methanogen extracellular domain. This domain, with length just over 300 amino acids, occurs in predicted extracellular proteins in a number of methanogens, in one to three proteins per genome. The aromatic residue tyrosine, comprising about five percent of the amino acid composition, is overrepresented among the most highly conserved columns of the multiple sequence alignment. The three members of this family in Methanosarcina barkeri occur all within a six-gene region
WISLSGGEEFQLPSPMSFTYNGINHTSFAGKGRNIKIDLNVDNYTDYTITYPYETHPMYTDTDDVSFTFY
GSEAFANKEVDVYLINSNIGSLKDALDKLMQGNSASINDLFEESKNNEYKNVTLDENGDLSITYGSLDAG
SYGIVIILADDITRENKVLSATAFEVLDYDSKIKAPSIIDNGKNLDVDISLENAPDDDYTYGAVLIKESA
YRADIRMETNGTKDGTNVSVNEIPLIDGFDLNGINKSNLNKSDVKNKIQTLIGEDNGTIAIGTVEGNQAT
LSLTTTDLPEGDYILLTGAYSGGKGLVAFNQDEVSI
>gnl|CDD|275100 TIGR04280, radical_SAM_family_protein, putative geopeptide radical SAM maturase. This family is the radical SAM/SPASM domain putative peptide maturase for geopeptide, described by model TIGR04229. The SPASM domain (see model TIGR04085) frequently marks peptide-modifying radical SAM enzymes
MPLSRYVKIFPCPDRPGHLLLYSTRRGAVIRVPEELLAAIREGTLSPAEAETLSRLGFLVEDREAEREEM
RSLFDRINRERRHFAAIVVLNLDCNLACPYCFEGPFRGKRYMDDATADLLVSYLVRERLAQGRDVSLDFY
GGEPLLSLDLIRRIATPLKAAAASRGLSFSFSLVTNGTLLTRDVVEELLPLGLTGAKVTLDGPPEIHDRQ
RPFVSGKGSFDTIVANLKAVCDLIAIQIGGNYTRENYREFPRLLDLLLAEGLTPERLALVRFSPVVSRAG
GAALPDFNSGCASSNEPWLIEASLFLREETLKRGYPVPKLRPGACMVELEDDLVVNHDGTLYKCPAFMGR
EGLAVGSLADGLSDYRDSHGLDLWKNEECLDCAYLPLCFGGCRFLTLLKTGAIDGVDCRRDYLDATLERY
VRQDLGYR
>gnl|CDD|275101 TIGR04281, periplasmic_binding_protein, putative ABC transporter PGF-CTERM-modified substrate-binding protein. Members of this archaeal protein family resemble periplasmic substrate-binding proteins of ABC transporters and appear in gene neighborhoods with permease and ATP-binding cassette proteins. Notably, essentially all members also have the PGF-CTERM putative protein-sorting domain at the C-terminus, while more distant homologs (excluded by the trusted cutoff) instead have what appear to be lipoprotein signal peptides at the N-terminus
CEFPVTETDATGTEVTLEEEPERVVTLNPSAAQTMWEIGARDKVVGVSQYTDYLDGADERTNVSGDDGLT
VNVEAVVDLDPDLVLAPNTANDDTVEQLRDAGLTVYVFPAATSIDDVAEKTETTGRLTGECEGAAETVDW
MDDRLEAVEEALADEDRPLVLYAMGDGYTAGSGTFIHDIITTAGGENVAAEAGITGYPQISEEVVVEQDP
EWIVYPDTAEVPPTPAYESTTAVEEGNVVAVNANYLSQPAPRVVEAVETLAEAFHPEAYEEAETADTEAD
TTTDDSTTESTDGTTTTSDGTATDDDIPGFGVVAALAALLAAAGLLARRR
>gnl|CDD|275102 TIGR04282, hypothetical_protein, transferase 1, rSAM/selenodomain-associated. Members of this protein family show strongly correlated phylogenetic distribution, and in most cases co-clustering, with an unusual radical SAM enzyme (TIGR04167) whose C-terminal pfam12345 domain often contains a selenocysteine residue. Other members of the conserved gene neighborhood include another putative glycosyltransferase, an alkylhydroperoxidase family protein (TIGR04169), and a phosphoesterase family protein (TIGR04168). The cassette is likely to be biosynthetic but its exact function is unknown [Unknown function, Enzymes of unknown specificity]
LIIFARAPEPGRVKTRLAPALGPEGAAELYRRLLEHTLAVAKSLANADVELAYSPDGPHALFDDWLGPGV
ELSLQGGGDLGERMARAFQRAFAAGYEKVVLIGSDCPDLTSEDLEQAFEALEQHDVVLGPAEDGGYYLIG
LKRLHPELFEGIPWGTETVLAQTLARLKALGLSVALLPELNDIDTPEDL
>gnl|CDD|275103 TIGR04283, glycosyl_transferase_family_2, transferase 2, rSAM/selenodomain-associated. This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine [Unknown function, Enzymes of unknown specificity]
LSIIIPVLNEAATLPELLADLQALRGDAEVIVVDGGSTDGTVEIARSLGAKVIHSPKGRARQMNAGAALA
KGDILLFLHADTRLPKDFLEAIRRALAKPGYVAGAFDLRFDGPGLLLRLIEWGVNLRSRLTGIPYGDQGL
FVRRSLFEQIGGFPDIPLMEDIELSRRLRRLGRLAILPAPVVTSARRWEKNGILRTILLNWRLRLLYRLG
VSPEELARLY
>gnl|CDD|275104 TIGR04284, aldehyde_dehydrogenase, aldehyde dehydrogenase, Rv0768 family. This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive [Unknown function, Enzymes of unknown specificity]
SRLLIDGKLVAGSAGTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDETDWSRDTALRVRCLRQLR
DALRAHVEELRELTIAEVGAPRMLTAGAQLEGPVDDLGFAADLAESYAWTTDLGVASPMGIPTRRTLRRE
AVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIAEHTDFPPGVVNIVTSSDH
RLGALLAKDPRVDMVSFTGSTATGRAVMADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMH
AGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRF
ACGGGRPADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVFGAD
PERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLIATAA
>gnl|CDD|275105 TIGR04285, parB-like_partition_protein, nucleoid occlusion protein. This model describes nucleoid occlusion protein, a close homolog to ParB chromosome partitioning proteins including Spo0J in Bacillus subtilis. Its gene often is located near the gene for the Spo0J ortholog. This protein bind a specific DNA sequence and blocks cytokinesis from happening until chromosome segregation is complete
EVQQIPIDKIVPNPYQPRKVFDEESIEELAQSIKEHGLIQPIVVRKKDDKYEIIAGERRFRACKLLGWEE
VPAIVREMNDEETASIALIENLQRENLTAIEEAEAYQQLIELHGLTQEELAQRLGKSQSTIANKLRLLKL
PEEVQEALLERKITERHARALLKLPDEELQLEVLNEIIEKGLNVKQTEELIKKLLEKPEKKKKKKKRRKG
FSKDVRIAVNTIKQSVKMIKKTGIKVKTKEEDLDDYYEITIRIPK
>gnl|CDD|275106 TIGR04286, hypothetical_protein_HMPREF9455_00034, MSEP-CTERM protein. Members of this protein family average over 900 residues in length and appear to have multiple membrane-spanning helices in the N-terminal half. The extreme C-terminal region consists of a motif with consensus sequence MSEP, then a transmembrane alpha helix, then a short region with several basic residues. This region, hereby dubbed MSEP-CTERM, resembles other putative sorting signals associated with the archaeosortase/exosortase protein family (see TIGR04178). Genes for all members of this family are found next to a gene for exosortase K
KKLHKPYWILLSITLPQLLLLGLFYTSFDIIKGLLGPATLFTAYAGILLLLFLGLISYYVYKKIREKNIS
KVYWLLLLGLYICFSYFMIALYENLIPSDIPDWMISSINFPLYPLYLLMPAIFYLILDLAFKFTPSEKSR
NNGINFAVAVSIPFFIYVLVNIILINGSFIGLNHLIMIFAIGGTYSFLFLILRFLYILITRRNLSFKNPE
LLIVILVGIIFPVLGLALNNNFGGIFGNFSSPWFYIIAILNGLLLLLPLQKNVLLRLILFYGKSAGFPYI
LYFFIVFLPLLPLGFIAIIIYGLGFLMLTPAVAFILQLRTISREFKTLKKTYGKPILILCGIAGLLTLPV
SFTGNCRQDRNNFHTALRYTYSPNASNTYAKVDTERLERSLKNIDKGKRRSRWEVGFGSTRTPILSSFYK
WIVLDNLTISERKLAKIQALFLGEEVNSSNEYIPRQRPVNSEVKIKDVQVSTEYDEKQDAYRSWVDLTIT
NASSVGQREYRTTFTLPDGAFISDYYLYVGEEKKFGILAEKKAATWIYEQIVNTRRDPGLLHYLNGNTLS
LRVFPFKKEETRKTGFEVIHKEPVHLTIDGTPIDLKGDSEPQKQHTSEISLNGVAYLSAAYKKTLPKVEL
PPYYHFVVDCSAKSDKKFLIQRIEEYSKKNNLEKAEVLFVNTDVKSKSLEDIWQAAAQPQAPEGGFNFDR
AVEQILYKHEPQGTYPVIVAVSDNMNKAVGPFSTAGMAQTFPESRYYYALNEDLSLIPHSFYDNKRVTEK
TNAPIPAEVREYNGLSAPIAVLDNDQKSLVPGYDPLKSRQISSNAYENALLLQAFWQHQLLNPEPKDEHW
LNLIKESFKTRILTPQTAFIVVETEAQEEMLLAKQEEILNGKKALDAGEETVTMSEPSLWLLLLVLLVII
GYRKRKMKCA
>gnl|CDD|213900 TIGR04287, hypothetical_protein_HMPREF9455_00033, exosortase K. Members of this protein family are exosortase K, a bacterial branch of the archaeosortase/exosortase family of protein-processing enzymes (see TIGR04178). All members of the seed alignment are encoded next to a member of family TIGR04286, which has the putative processing signal MSEP-CTERM (see family TIGR04286) at the extreme C-terminus
KKIIIYLLVVLLAFCLKGGYRTASTADLRFLLYPTIKLVELFTNSPFVYIPGQGYSSPGGNFVIGKSCAG
FNFLIISFLILAFLFIKNFEGFIKKILRIPLSLILAYFLTIIVNTFRIIAAIPFARLEFFHAFLIHEIIG
IIVYLAFLILLYLLLEYFLSKKQ
>gnl|CDD|213901 TIGR04288, CGP_CTERM, CGP-CTERM domain. This domain has an essentially invariant motif, Cys-Gly-Pro, followed by a highly hydrophobic transmembrane domain, always at the protein C-terminus. It occurs, so far, strictly in the family Thermococcaceae (includes Thermococcus and Pyrococcus) within the Euryarchaeota. It occurs in ten proteins per genome on average, and proteins with the domain may lack similarity elsewhere. The presumed sorting/processing protein, for which this domain contains the recognition sequence, is unknown, but it is unlikely to be a member of the exosortase/archaeosortase family. The Cys residue suggests a lipid modification. Upstream, from this domain, most member proteins have an extremely Thr-rich sequence, suggesting archaeal surface protein O-linked glycosylation
ICGPALIVLLALLPLLLRRR
>gnl|CDD|275107 TIGR04289, hypothetical_protein_PF0600, eight-cysteine-cluster domain. In this domain of about 50 residues, eight of twelve invariant residues are Cys. Proteins with this domain tend to have N-terminal signal sequences, suggesting an extracytoplasmic location for this domain
ECKSDADCKTGGCSGEVCAPKNEEVVTICVYREWYDCLKLTSCGCVNGTCTW
>gnl|CDD|275108 TIGR04290, hypothetical_protein_OB2597_19321, methyltransferase, Rta_06860 family. Members of this family are methyltransferases that mark a widely distributed large conserved gene neighborhood of unknown function. It appears most common in soil and rhizosphere bacteria
SLARRIEELGPWFHNLHLPGIETAPDHFLGDFPAFKWREFAHAIPEDLSGWSVLDIGCNAGFYSIEMKRR
GAGRVLGIDSDPRYLAQARFAAEVLGLDIEFRQMSVYDLGRLGERFDLVLFMGVLYHLRHPLLALDLLRE
HVAGDLLLFQTLTRGSEEVGEVEEDYPFTERGPFLREDWPKMHFIEHRYAGDPTNWWVPNRAGVEAMLRS
AGFRIVAHPEDEVYLC
>gnl|CDD|275109 TIGR04291, Arsenical_pump-driving_ATPase, arsenical pump-driving ATPase. The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite)
ELPPYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALE
IDPQAAAQAYRARIVDPVRGVLPDDVVSSIEEQLSGACTTEIAAFDEFTGLLTDAELTQDFDHIIFDTAP
TGHTIRLLQLPGAWSDFLDTNPNGASCLGPLAGLEKQRAQYAKAVEALSDPERTRLILVARPQKSTLLEV
ARTHQELAAIGLKNQYLVINGVLPETEASDDPLAQAIYKREQKALQHMPAILANLPRYTLPLKPYNLVGL
EALRQLLNDDQPQLSLDITTPQVPDLPSLSRLIDEIAKSEKGLIMTMGKGGVGKTTVAAAIAVRLANKGL
DVHLTTSDPAAHLSVTLTGSLNNLQVSRIDPKQETERYRQEVLATKGKELDEDGKAYLEEDLRSPCTEEI
AVFQAFSRIIREAGDRFVVMDTAPTGHTLLLLDATGAYHREVERKMGDTPEHVTTPMMQLQDPERTKVLL
VTLPETTPVLEAARLQEDLRRAGIEPWWWVINNSLAATNTTSPLLSQRAQNELKWIEKVKRIHADRYAVI
PLQAEE
>gnl|CDD|275110 TIGR04292, hypothetical_protein_PF0600, heavy-Cys/CGP-CTERM domain protein. Members of this protein family are restricted to the Pyrococcus and Thermococcus genera of the archaea. Member proteins have a C-terminal, Cys-containing predicted surface anchor domain, where the Cys may be the site of cleavage and lipid attachment (see domain TIGR04288). Members also contain a region crowded with 10 invariant Cys in 60 residues (see domain TIGR04289), possible ligands to some redox cofactor. Note that a sorting motif is CGP. Previously, the motif was named incorrectly as GCP-CTERM in this model due to a typographical error
ASACFSPQDLYAVEVELNKPGIEYNLEPLLHAKNVIIENGTIIYRSHYDPRLIVILWNGDSGLHVRIQIP
TKFKESKIYVAEFEGILPITEDALEKAKALGWKVEGYTFEKDNVTVQLTPKQGKECKSDSDCATGGCSGE
VCAPKNEAKEIVSPCVYREWYECLKLTSCGCYNGTCTWKPNPEFESCLKEHGVDPEKVIKAGYTEVYIEI
YGKLPEEDIAEIEELLSALGISCNIELKFEKSSRSALVPVIDPSEVNASEALRVELEWLREIGVLKISDE
DIEEISEVAEWGYAGYNSHIGWYETKNGTYAWIPYFESSNALLVRCVGSGFPAYDEPLPTTPPSIPSSTT
PSAICGPGIILLLSLLAALGGRR
>gnl|CDD|213906 TIGR04293, archaeo_artF, archaeosortase family protein ArtF. Members of this protein family, ArtF, belong to the archaeosortase/exosortase family, in which many members associate with specific protein C-terminal putative protein sorting domains (exosortase A with PEP-CTERM, archaeosortase A with PGF-CTERM, etc.). This subgroup is observed in Thermococcus gammatolerans EJ3 and Thermococcus sp. AM4, but the gene neighborhood is not conserved. The cognate sequence to ArtF is unknown, but should not be ICGP-CTERM (model TIGR04288), found also in many Pyrococcus species that lack any archaeosortase family member
MKRNSLAFGILQLLGYLLLFSILILVIGAKFGDPLVKIEAKNIHVLLKILGVPNILLGNMVYLPEERLSF
EITWQCSGMFSISLYTIVYLTFPGIRRNLWEWFFGVSVLYLANFFRVLTSILLYHHFGEEVFSFFHYILG
PALMFGVVVLLLGDLLVKSLKERRQN
>gnl|CDD|213907 TIGR04294, hypothetical_protein, prepilin-type processing-associated H-X9-DG domain. This model describes a region of ~16 residues found typically about 30 residues away from the C-terminus of large numbers of proteins in the Planctomycetes, Lentisphaerae, and Verrucomicrobia, on proteins with a prepilin-type N-terminal cleavage/methylation domain (see TIGR02532). The motif H-X(9)-D-G is nearly invariant. Single genomes may encode over 200 such proteins
RHGGRANVLFADGHVA
>gnl|CDD|275111 TIGR04295, B12_rSAM_oligo, B12-binding domain/radical SAM domain protein, rhizo-twelve system. A variety of bacteria, including multiple species of Bradyrhizobium, Mesorhizobium, and Methylobacterium, have a typically twelve-gene cassette (hence the designation rhizo-twelve) for the biosynthesis of some unknown oligosaccaride. This family is a B12-binding domain/radical SAM domain protein found in roughly have of these cassettes, but nowhere else
RVALVNPPWSFTGSIYFGCREPHLPLELGYARALLENAGHAALLVDAQADGLSLEELRRRVAAFRPDMTV
VTTAPSYLFWRCAPPELRVPMATLRALRETGGTLVAVGPHASTTPRAALRKLGVDVVVLGECEEVLVELA
GGPWRQIDGICYRRGDEVHVQGGPAAADMTTLPALRWPEATIARHAHHHHRFDAAPEGPGAEVETSRGCP
YHCTFCAKDNFRNKYRKRPLATILEEIDALIAQGVRYVYFIDEIFLPDRPLLEEIVARNVSFGVQTRIDL
WKEEMLDLLGRAGCVSIEAGVESITEEGRELLAKNCRMSTEELTELLIHAKRSVPFVQANLIDSPKDDPA
EVARWRQRLQGHGVWANEPVPLFPYPGSPDYTRRWGAPDDNAWERAHAHYLAEFRTFSDIQDQRPLPLAE
LE
>gnl|CDD|275112 TIGR04296, Hypothetical_protein, PEFG-CTERM domain. This putative protein sorting/processing domain occurs about ten times per genome in members of the Thaumarchaeota. Its putative handling protein, a member of the archaeosortase/exosortase protein family, is exceptional in having a Ser rather than Cys at the putative active site. The highly conserved motif resembles the PEF-CTERM protein sorting domain of family TIGR03024, but membership does not overlap
VVPEFGTIALMILAVAIMSIILLSKKSFLI
>gnl|CDD|213910 TIGR04297, hypothetical_protein_Nlim_0204, thaumarchaeosortase. This member of the archaeosortase/exosortase family occurs exclusively in the Thaumarchaeota, where the corresponding proposed sorting signal is PEFG-CTERM (see model TIGR04296). This family is unusual in that the suspected active site residue, Cys in every other defined subfamily of archaeosortases and exosortases is replaced by Ser
IAGIGIIASPILFALIAFPDSFALSWNEGRGGFLFALVFVVAELIGLKIIISKKRLLAVIPIAAATISYI
AGLEYGLRDYILASAEQFDVQLIYSWTWMWDFIVMAIFIVVALSIFFGKRWIRIAPAGPIFLAGSAIILS
LDAFFPYDTLGPLQYIVPYFVQANVWLINALDLGTATARDNIMFLRGDFGPMALQVFWPSAGVHSIIIFS
LVIGAFLLKMNIPRARKSIYFGIGIAGTIGINLIRIFSLSWYALKVTTDPKAWEEFHKIAGEIMFLPWLF
AFILIVILIESKRLKKLEEQDGSKNKS
>gnl|CDD|213911 TIGR04298, hypothetical_protein_HMPREF9690_04798, histidine-histamine antiporter. Members of this protein family are antiporters that exchange histidine with histamine, product of histidine decarboxylation. A system consisting of this protein, and a histidine decarboxylase encoded by an adjacent gene, creates decarboxylation/antiport proton-motive cycle that provides a transient resistance to acidic conditions
KMGVIALTLVTASNMMGSGVFLLPTNLAGIGAISIFGWIFTIIGVIALALVFAKTSLIHERIGGIVAYAR
DAFGPFIGFQSTIAYWISAWIGNVALLVAGVGYLAFFFPELKDPTVGTTYGCIAAIIILWAFVFLASFGA
KVAGRAQSFTAICGLAVILGVGIFGWFWFKPEMYLEVINATGNSNFSAIIAAASIALWGFLGIESAVVST
GQVENPEKTVPKATVMGLLIAAVCYVASCTVIAGIIPHEVLINSAAPFADAAKYMFDNELAGNIASALSI
IACFGSISGWFILQSEAPRAAAEQGLFPKFFADLNKNDVPMKSLIFTAILMCCVLLLTASPNLAEQFEII
ILMSVFASLLPYLYAIIALPIILTAKKLKKDGNFKFHCLLVLIGIIYCIFALLGSGADSIFWGILLMMFM
IPLFSFPAA
>gnl|CDD|213912 TIGR04299, ornithine/putrescine_exchanger, putrescine-ornithine antiporter. Members of this protein family are putrescine-ornithine antiporter. They work together with an enzyme that decarboxylates ornithine to putrescine. This two-gene system has the net effect of removing a protein from the cytosol, providing transient resistance to acid conditions
AKKKKMSVVQLTILTAVNMMGSGIIMLPTNLAQVGTMSIISWLVTAVGAMALAWAFARAGMYSSKSGGMG
GYAEYSFGKAGNFMANYTYGVSLVIANAAIAISAVGYGAELLGAHLSPVQIALATIGVLWIATVLNFGGA
RITGQISSFTVWGVIIPVVGISIIGWFWFSGTLYADSWNPHHAGFFSGVGSSISITLWAFLGLESACANT
DVVENPKKNVPIAVLGGTIGAAVMYIISTNVIAGIVPNMELANSNAPFGLAFSQMFNPTVGKIVMGLMVI
SCFGSLLGWQFTIAEVFRSSADEGYFPKIFSKTIGNGTPLIGMLIITILQSLLALMTISPSLSKQFTILV
NLAVVTNIIPYILSMAALKTMQKVANVPPKGAKVTNFIAFVAALYSLYALYSSGEEAMLYGSIVTFAGWT
LYGLVSPRFD
>gnl|CDD|213913 TIGR04300, exosort_XrtM, exosortase family protein XrtM. Members of this family, part of the larger exosortase/archaeosortase family, are known from five related cassettes of genes in Methylomonas methanica MC09, a gammaproteobacterial methanotroph. Each xrtM gene occurs near a large YD repeat (see TIGR01643) protein of 1500-2500 residues and a small, uncharacterized protein of about 200 residues. No PEP-CTERM-like recognition sequence has been identified, so this protein is designated as exosortase family, but not necessarily a functional exosortase
SVTFDYAYLKIPDLSTDVFYLNSVAAISADLINFLAPFEQVFVKHNHLLSAKADLEIVRGCSGSGALFLV
IAAVLVFPSSLKRKALGILFGIGLISTLNLLRIVVLYFIIAYHPGWFQLIHTYIAPTLMIILCCLYFAWW
AFGATPSIHE
>gnl|CDD|275113 TIGR04301, Ornithine_decarboxylase_inducible, ornithine decarboxylase SpeF. Members of this family are known or trusted examples of ornithine decarboxylase, all encoded in the immediate vicinity of an ornithine-putrescine antiporter. Decarboxylation of ornithine to putrescine, followed by exchange of a putrescine for a new ornithine, is a proton-motive cycle that can be induced by low pH and protect a bacterium against transient exposure to acidic conditions
MKKLKIAVSELLPDCFSTNREVVDINNTDFTDVAAVVISVDDIKNGVLEQIEETGFGIPVFVILNDEETV
PAEILPRVTGVIDLNESDIDFYGRQIETAATKYEEKLLPPFFGALVKYVEQGNSAFDCPGHQGGQFFRKH
PAGRQFYDFFGENLFRSDLCNADVALGDLLIHEGAPCDAQQHAAKVFNADKTYFVLNGTSASNKVVLNAL
LTPGDLVLFDRNNHKSNHHGALIQAGATPVYLETARNPFGFIGGIDEHCFEEEYLRELIREVAPERAKEK
RPFRLAIIQLGTYDGTIYNARQVVDKIGHLCDYILFDSAWVGYEQFIPMMKDCSPLLLELNPEDPGILVT
QSVHKQQAGFSQTSQIHKKDSHIKGQARYCNHKRFNNAFMMHASTSPFYPLFAALDVNAKMHEGESGRRL
WMDCVKTGIEARKLLLKNCKYIRPFIPEMVDGKPWQDYDTDQIANDLRFFNFVPGEKWHSFEGYGENQYF
VDPCKLLLTTPGIDAETGEYEDFGIPATILANFLRENGIIPEKCDLNSILFLLTPAEDMAKMQHLVAQIA
RFEKLLEEDAPLAEVLPSVYKANEERYKGYTIRQLCQEMHDLYVSRNVKQLQKEMFRKAHFPEVVMNPQE
ANIEFVRGEAELVPLEQAEGRIAAEGALPYPPGVLCVVPGEIWGGAVQQYFLALEEGINLLPGFAPELQG
VYLEKDEDGRKRAYGYVLK
>gnl|CDD|213915 TIGR04302, hypothetical_protein, GeoRSP system PqqD family protein. Members of this PqqD-related family so far occur only in the genus Geobacter, always together with a PqqE-like radical SAM domain/SPASM domain protein and a second SPASM domain protein with traces of a degenerate radical SAM domain. The extended gene region includes a high-molecular-weight cytochrome c family protein. Besides authentic PqqD (TIGR03859), another example of a PqqD family protein occurs in the SynChlorMet cassette, again with two PqqE-like proteins. The system is named GeoRSP for its prevalence in Geobacter, its Radical SAM protein, is SPASM domain protein, and its PqqD family protein
MKKIHRNPDVMWREEADSLARAQAALEKGEEVEETGTSLLFSDGTMLTLNFLGTEIWKLCDGRAVDEIVA
ELLPQFEVEEAVLREDVRAFLDELAAKGFISY
>gnl|CDD|213916 TIGR04303, radical_SAM_protein, GeoRSP system radical SAM/SPASM protein. Members of this family are radical SAM/SPASM domain proteins from a cassette restricted to the genus Geobacter. Genes always found adjacent include a non-radical SAM protein with a closely related SPASM domain and a short stretch of N-terminal homology as well to this family, and also a PqqD-like protein. The three-gene cassette is designated GeoRSP for the genus Geobacter, this radical SAM protein, the SPASM domain protein, and the PqqD family protein
LKAPLTINWAINNNCNFACRHCYSRGDTHEELPRDVLCACLGKVAAAGVFSVNFGGGEPLLRPDLLEIAS
CAAGSGMRVSMNSNGYLIDRDKAAALKDAGFSKVGISIDSHLPRVHDRFRGVDGSHGRAVNALRHLAEAG
IKTSISTVICRINHTAIDDLITFAREQGVGQLNFHNFKCSGLGLSNRDELDLTPAEWQEFYRGALAAKER
ESGLDISLDDPIIASLGARDAGSLVKGSVCGKLSLNIKSNGDITPCGFIPVVIGNIVRDDLKEVWRDSAV
LEALRTKKPTGKCAGCSDYEECLGGCSARALALTGDFNSPDPHCW
>gnl|CDD|213917 TIGR04304, GeoRSP_SPASM, GeoRSP system SPASM domain protein. Members of this protein family are encoded by one of two consecutive genes for SPASM domain proteins. The two are closely homologous in the SPASM domain regions, and also in a small N-terminal region, but the other family (TIGR04303) has an intact radical SAM domain (pfam04055) that this "quasi-rSAM" protein lacks. A PqqD-family protein, TIGR04302, is always adjacent
ELKTPIRIYWDLPATAADPSLLLAIAEQIIDLRILSLNVTSTAPTSPGWLLEVLERFRGGPIAVSLTIPP
QAHDDAVLALVAHGAVRELLVDVDHADDLALVDRGEWQDAGEPSAGVSFAVTADNWRELPELVSYCLDRG
ITRLVLPMQRLYGGEPPFFLTRNERRELSNALDAEGGPQRMALTIHDPFLWRVFFPGVPFPQGSCQAANT
MLAIAPDGDVYPCPTLPVRLGNLGEMTLQEIVASEAKKALRERLLEHPRGCGACGELAECRGGCRGRGYF
MHQSWDEEDPSCW
>gnl|CDD|275114 TIGR04305, TENA/THI-4_family_protein, putative folate metabolism protein, CADD family. This protein family, related to but outside the family of PqqC proteins involved in PQQ biosynthesis, includes the well-studied Chlamydia protein CADD (Chlamydia protein Associating with Death Domains), which can induce apoptosis in a host cell. Other members of this family occur in Rickettsia and Wolbachia, unrelated in terms of phylogeny (both are alphaproteobacteria) but similar in living intracellularly. Local gene context in these species, although not in Trichodesmium or Nitrosomonas eutropha, suggests a role in folate metabolism, and some species with this protein lack FolE but have other folate synthesis proteins
FLQQLDKILEEKHLLKHPFYQAWNRGKLTKEQLQEYAKQYYHHVKAFPRYLSAVHSKCEDIEARKVLLDN
LIDEEQGDENHPELWKRFAEGLGLDDKEVRNAPALPSTQKLVDTFFRLCRSSFAAGLGALYAYERQIPEV
AEVKIAGLKKFYGISDERGLQFFTVHEEADVWHSQECKELIEELTPKEQAKALKAAKTVADALWGFLDGV
YE
>gnl|CDD|213919 TIGR04306, salvage_TenA, thiaminase II. The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the C-terminal region of trifunctional protein Thi20p from Saccharomyces cerevisiae, perform cleavages on thiamine and related compounds to produce 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP), a substrate a salvage pathway for thiamine biosynthesis. The gene symbol tenA, for Transcription ENhancement A, reflects a misleading early characterization as a regulatory protein. This family is related to PqqC from the PQQ biosynthesis system (see TIGR02111), heme oxygenase (pfam01126), and CADD (Chlamydia protein Associating with Death Domains), a putative folate metabolism enzyme (see TIGR04305)
VKPIWDDYINHPFVQKIGDGTLERDKFRFYIEQDYAYLVEYAKVHALGGSKACDEDMEKELVEQIQGGVE
TEMGQHKRLAEVLGISDEEYFQKIKPGPALRSYTSYMYDVSRRGNWQELVAALLPCLWGYGEAATKLKGK
HTAPEHSVYHKWIETYSSSWFREAVNEGENLLNHLAETSSPEELEKLKTIFAESCEYEYNFWTMAYEY
>gnl|CDD|213920 TIGR04307, Gram-positive_signal_peptide_protein_YSIRK, proline-rich tail region repeat. This model describes a proline-rich tandem repeat of about 24 residues found in C-terminal regions of Gram-positive surface proteins with LPXTG sequences for processing and cell surface attachment by sortase
PTPPTPPTPPKTKTVEVPDEPTE
>gnl|CDD|275115 TIGR04308, hypothetical_protein, surface protein repeat SSSPR-51. This repeat domain is designated SSRS51, Streptococcal and Staphylococcal Surface Protein Repeat of size 51. These repeats are homologous to the listerial repeats of pfam13461, but shorter on average by about 8 amino acids. Up to twelve tandem repeats can occur, on some of the longest proteins of their respective species. Nearly all member proteins carry the C-terminal sortase target sequence, LPXTG, recognizable by model TIGR01167. The repeat structure and probable surface location suggest a possible adhesion function. A protein with this class of repeats may have other classes as well
RWVDENGNPLKPTEEGTKPPKDIPGYEFVTTTTDENGNTTHIYKKVTT
>gnl|CDD|213922 TIGR04309, putative_MSDIN-like_protein, amanitin/phalloidin family toxin. Members of this family are ribosomally produced precursors of toxins produced by several mushrooms. These precursors undergo extensive post-translational modification to become amatoxins (e.g. alpha-amanitin) and phallotoxins (e.g. phalloidin)
MSDINATRLPIWGPLGCNPCVGDDINMTLTRGE
>gnl|CDD|213923 TIGR04310, hypothetical_protein_SKA34_00842, pantocin A family RiPP. Members of this family are ribosomally-synthesized and posttranslationally-modified peptide (RiPP) precursors about 30 amino acids in length encoded in the vicinity of PaaA and PaaB homologs. Members include PaaP from Pantoea agglomerans, whose central tripeptide EEN appears to be the source of the mature product, pantocin A. Note, however, that the corresponding residues in Photobacterium sp. SKA34 and Photobacterium asymbiotica are EEK rather than EEN. This family, therefore, resembles the PQQ precursor PqqA as a peptide precursor of an extremely small mature product
IKFKTLSHRISAISEEKAMYSKGEKIVLK
>gnl|CDD|275116 TIGR04311, Radical_SAM_domain_protein, putative metalloenzyme radical SAM/SPASM domain maturase. This model describes a family of radical SAM/SPASM enzymes largely from the deltaproteobacteria. The family is most closely related to radical SAM enzyme family regularly in archaea in the vicinity of tungsten-containing oxidoreductases. A single member of the family in archaea may correspond to multiple tungsten enzymes, e.g. five in Pyrococcus furiosus. Therefore, the lack of a conserved gene neighborhood for members of this family in deltaprotebacteria suggests members may be involved in the maturation of multiple metalloenzymes
YPSKLFVEVTTRCNLRCRMCVKQAGGSDIPEGDMTPETFRALEPALPHLEALVLNGIGEPLLHPDLEAFI
ALARQAMPETGWIGFQSNGLLLTEERARSLLDAGLDRICLSVDSLSPELFGKVRGGGDLGDLERAFAALA
AARRRCGRPKLRLGVEFVLMRDNLRELPAVLRWAAARGADFALVSHLLPYDAAAAEQSLFGPNTDAAIAI
FQRWRARAAEQGLDLRRYFDVVWKYGKSPEEKRLVDFVRQMRAEARRQGIFLNLPNLLQRDDGAVDDVEA
VFARAEAVAEECGLELRLPALAPRFERRCDFVEDGGAFISWDGKVHPCYFLWHRYSCFLDGWEKQVRPKV
FGNVTERDLLEIWNGPEFRAFREEVLEYDYPYCSNCTVAPCDDIQTEEFETDCYGVTVPCGDCPWCMGLL
QCL
>gnl|CDD|275117 TIGR04312, conserved_hypothetical_protein, choice-of-anchor B domain. This domain, about 385 amino acids long, can have either of at least two types of C-terminal sorting signal. Members from Shewanella and allies have the rhombosortase target domain GlyGly-CTERM (TIGR03501), while members of the Bacteroidetes have the Por secretion system C-terminal domain (TIGR04183). Most other members lack any C-terminal extension, but in most of those, the normal signal sequence is replaced by a lipoprotein signal sequence. Member sequences show a region of local similarity to the LVIVD repeat sequence (pfam08309)
PCENGFAGNYPCNNIDLLSHLPLATLSASSGNDIWGWTDLNTGREYAIIGLNNGTAFVDITDPENPVYLG
KLPTHGTRSSWRDIKVYQNHAYIVSEASGHGMQVFDLTRLRNVNPPQTFTADAHYTDFGSAHNIYINEES
GYAYIVGTNTFGGGPHFIDLSDPKNPILAGGYSGSGYTHDAQVVIYNGPDTDYTGCEILIDSNENEVVIW
DVTDKSNPQEISTISYSNVAYTHQGWFSEDQRYFFLGDELDELNFGFNTRTRVFDLTDLDSPVLAGSYQG
PTKAIDHNGYVKGNRYYMSNYTAGLRILDISNPTNGNPTEVGYFDTYPESDSAQFNGAWSVYPYFPSGNI
LVSDINSGLFVLKK
>gnl|CDD|275118 TIGR04313, hypothetical_protein_MoviS_02069, aromatic cluster surface protein. Members of this family are absolutely restricted to the Mollicutes (Mycoplasma and Ureaplasma). All have a signal peptide, usually of the lipoprotein type, suggesting surface expression. Most members have lengths of about 280 residues but some members have a nearly full-length duplication. The mostly nearly invariant residue, a Trp,is part of a strongly conserved 9-residue motif [ND]-W-[LY]-[WF]-X-[LF]-X-N-[LI], where X usually is hydrophobic. Because the hydrophobic six-residue core of this motif almost always contains three to four aromatic residues, we name this family aromatic cluster surface protein. Multiple paralogs may occur in a given Mycoplasma, usually clustered on the genome
MKKKKKKLLIIFSLILASLSLISCSSKSLNKIIKNKIDTKKDKKDKKWQVFLNNKYINNLLNLVFKNDED
EKNKYIKSQKNLNDELYLKLLKLSLEYLNNINSSYSNDSDFGPYLYEKSKKKLNELFSKNWLWTLFNLDK
FEFVFYDYWDLFKKQNEEFNIDAKHNSLFLGKFKKKKPKNNKFIDNYIDKLKNGEESGHSNNYNVYLLNK
DNFIFRINITKDDNKKSKVKIFPYIYIYPKLLNNKINLKEIFNLIHYAIIHNDQEGKSNFEKEKILFEKY
GGDPLRYTLVDID
>gnl|CDD|213927 TIGR04314, cytochrome_C_partial, methanogenesis multiheme c-type cytochrome. Members of this protein family are multiheme cytochrome c proteins of Methanosarcina acetivorans C2A and several other archaeal methanogens. All members have N-terminal signal peptides and are presumed to act in electron transfer reactions associated with methanogenesis. Putative heme-binding motifs include five (or six) CXXCH motifs, a CXXXCH motif, and a CXXXXCH motif. These proteins show multiple regions of local homology, in the same order, with multiheme cytochrome c proteins such as octaheme tetrathionate reductase from Shewanella
RLKAILLGVAVFLLFAAGIYAYLGYSGNDAIASHYMTDGEWSDSVCGGCHFGVYENVAQSYHVQRDMDRW
SPLTNFDIEVQGEEEWVKEFGPYHPGGGPLEEYGVDIDCMMCHEQYGLYDFDARAEAIANGDFENANSAA
MENASHEVQQDPIHVFTYTLNVLTPLPLLIVFHDAVNGAPQKSSCADYCHSTDVETTAVMWADEDYHESD
VHADVNCVECHETEEHQIGRSNTSGTPDLPASHEVGAEMKSCDDAGCHEGISHGPIVDAHLEFLACESCH
IPALPGGDLPGGEPLKSFSWSNGEREDSYREADFQPALAWSNGQSGDELPSVDTRNDTGVKLTPFNVITG
TWWDAGIDSEVLANPNTSISTGDPIPVSYVKAADSNGDGEVTVEEMQSYDGDGDGEADYPNAVLRTVELY
YKLNHNIASSDVGLADPLTCDDCHGVSATVIDWAALGYESDPAETDPPTNFSVKSIAVTVPGAKPPEVER
EPAF
>gnl|CDD|275119 TIGR04315, cytochrome_c_family_protein, octaheme c-type cytochrome, tetrathionate reductase family. Members of this protein family bind heme covalently and contain eight (at least) CXXCH heme-binding motifs. A characterized member is the respiratory enzyme octaheme tetrathionate reductase from Shewanella
LKGPFKSGPEVTKACLTCHTEAAKQFMKTIHWTWEGPPPVTGQTLRYGKKNVINNFCISIQSNEPRCTSC
HAGYGWKDSSFDFTDEENVDCLVCHDTTGTYKKFPGGAGHPVDSEFKFLFKPVDLAKAAQSVGAPGRANC
GSCHFYGGGGDAVKHGDLDSSLIKPDRSLDVHMGSDGLNFTCQDCHTTEGHQISGSRYALSAKDTRNRAS
CESCHGLAPHKMNAKLNDHTAKVACQTCHIPEFARGGPTKMWWDWSTAGKLDGKPITEKDEYGKETYLKK
KGDFVWGKNVVPEYAWFNGTVEYYLLGDKIDPSKPVKINKPEGSITDPKARIWPFKVMRGKQPYDKENKY
LLIPHTFGKDDNAYWKNFDWQKAIRLGMEAAGLPYSGEYGFVETEMYWPITHMVAPKEQALKCNDCHSKG
GRLDWLALGY
>gnl|CDD|275120 TIGR04316, 23-dihydro-23-dihydroxybenzoate_dehydrogenase, 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase. Members of this family are 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EC 1.3.1.28), the third enzyme in the biosynthesis of 2,3-dihydroxybenzoic acid (DHB) from chorismate. The first two enzymes are isochorismate synthase (EC 5.4.4.2) and isochorismatase (EC 3.3.2.1). Synthesis is often followed by adenylation by the enzyme DHBA-AMP ligase (EC 2.7.7.58) to activate (DHB) for a non-ribosomal peptide synthetase
VLVTGAAQGIGYAVARALAEAGARVAAVDRNFEQLLELVADLRRYGYPFATYKLDVADSAAVDEVVQRLE
REYGPIDVLVNVAGILRLGAIDSLSDEDWQATFAVNTFGVFNVSQAVSPRMKRRRSGAIVTVGSNAANVP
RMGMAAYAASKAALTMLTKCLGLELAPYGIRCNVVSPGSTDTEMQRQLWNDEYGEQQVIAGSPEQFRLGI
PLGKIAEPSDIANAVLFLASDLASHITMHDLVVDGGATLG
>gnl|CDD|275121 TIGR04317, W_rSAM_matur, tungsten cofactor oxidoreducase radical SAM maturase. Members of this family are radical SAM enzymes involved in the maturation of tungsten (W)-containing cofactors in the enzymes aldehyde ferredoxin oxidoreductase, formaldehyde ferredoxin oxidoreductase, and others, and tend to be encoded by an adjacent gene
PDLKKLYVEITTRCNLNCKMCFRNAWEEKEGDMDKDLFEKILEEAVELPELKEIVLGGIGEPTVHPDFID
MLTEAKSRGFAVGLSTNGYLLEEMAEELVGLGVDKIYVSIDALPDKPYKDIGHGDLAKVLENLKKLYEIK
IKKGSDKPHVGIEFVATKENYKELPELVELARKLGVSSIIVSNLLPYTEEYIDEILYDGPGELEPLKDEL
ERVAGSGLEYGVKRLPEFKLRTERYCNFVENRAAVIRWDGGVSPCYRFLHNYTEYVFGRKKKVYAHSFGN
VNEESLIDIWTSREYKWFRFIVYNSRYPSCTDCPLVDGCDFVLDNEYDCWGNSPSCADCLWSRDIIICP
>gnl|CDD|275122 TIGR04318, ornithine_decarboxylase, putative ornithine decarboxylase. In at least ten species of Lactobacillus, this close homolog to known ornithine decarboxylase occurs in a three-gene neighborhood, along with an amino acid permease family transporter and pyridoxal phosphate-dependent enyzme from the cystathionine gamma-lyase family. Species include L. acidophilus, L. amylovorus, L. crispatus, L. delbrueckii, L. farciminis, L. helveticus, L. johnsonii, etc. The combination of a decarboxylase with an antiporter in a two-gene system suggests a decarboxylation/antiport proton-motive cycle for transient resistance to acidic conditions. The substrate for this decarboxylase might be ornithine but is unknown
MHYLKIAAGKTLLPYLPKDWPIVELTENVNGAELAAVVINKNDSRARGKAQELKEKSGLDIPLIEVDAKT
SSADIQKIIQAAQQYEEENVPGFLRDLINFADQKPISFTTPGHHNGQFYDRHPAGVVFKNFFGDNFMRAD
TSDTVPELGDTMTHTGTPLTAEQEAAKAYNADKVYFCTNGTTSANTICASAVLSEGDLVLFDRNNHKSLY
NSALVMTGAKPVYLPTDRNPLGLIGPLVPDDLDEDKIRREIAKVDPKRAKAKRPFRLAVLQLETYDGVFY
DAKWILDKIGKLCDYILFDCAWGGYEQFVPIMKHLSPLQLTYGPDDPGILVTQSLHKQQAGVAQTSQILK
KDSHIKGQKRYVDHKHFNHAYLKYVTTSYSYPIYASLVVNAAMAAGPANKKWWDETLRLGIEFRKKLLRK
SKLFKPLVPQNWENIPTDVLATDLSYWKLSPTDDWHGFKKIAKGEAMISPLKLTVVTPGIDLATAKYTET
GIPGPIVAEFLMEKRIIPAKADLYSTLFLLTPGETEVDLDTLLTAFLEFEKAYLTDAPLEQVLPRLVKQY
PDRYQGYTLKQLCQEMHEYYAENEIFKLQQALFIKPDFQNYEMTPAEADRLFMRNESKLVDLDDIEGRIA
LEGALPYPPGVFIVAPGEKWQKIDVDYFKVLLGAIEKFPGFVPEIQGVYLDQNDDGTLRVQAEVL
>gnl|CDD|275123 TIGR04319, hypothetical_protein_LzeaK3_11797, surface protein repeat Ser-Ala-175. This serine and alanine-rich surface protein repeat, about 175 amino acids long, occurs up to nine times in surface proteins of some Lactobacillus strains, particularly in Lactobacillus rhamnosus. Members proteins have the N-terminal variant signal sequence described by TIGR03715 and C-terminal LPXTG signals for surface attachment by sortase
ASTASTTASSANAVASSAASRFPDNQSLASLAKTASSANSVTSSYAASASADASAASSLATKVSSANKAA
SSAASQANAALAAGNLDAASSYANQASTAASNASSLADKANSAASKALSEALQASSAAAIASSAASSAAT
LAGSLASTAAASDDASAASDAATSASVVASTASTV
>gnl|CDD|275124 TIGR04320, hypothetical_protein, SEC10/PgrA surface exclusion domain. This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion
ALAAAQAELNQAQAKVDKANALAGVNTITLPANYNIDALKNIYESGDFDNSDAAKAEAEKAAAEAKSLNN
YKSNAADKNRTVDINNLTDEQQNELSQYAADLINQVRKQLGLPPVVVTEGSLDFAQAVAKAYKKDNSGTG
GHDETAINKAAAENGLDNTYENLGSISSNNENTTMDDLKRAIYDSILGMLFNDADSNWGHAQNLLGDDKI
NAGAYLGVSISNDGGVTIHFVNFNDSYIADGNKFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTA
QAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNLATAQAALANAEARLAKAKEALANLNADLAK
KQAALD
>gnl|CDD|275125 TIGR04321, hypothetical_protein_TresaDRAFT_0163, spiro-SPASM protein. This three-domain protein is restricted to the spirochetes and widely distributed (excepting Borrelia). It has a conserved C-terminal SPASM domain, a 4Fe-4S binding domain shared by a number of peptide-modifying and heme-modifying radical SAM proteins. It has a central radical SAM domain, although half the members have lost the signature 4Fe-4S-binding Cys residues, fail to register with the radical SAM domain definition of pfam04055, and must be considered pseudo-SAM proteins. PSI-BLAST shows a relationship between the N-terminal domain and various predicted glycosyltransferases (e.g. Bacillus subtilis SpsF) and cytidyltransferases. In some Treponema species, this protein appears to split into two tandem genes
AFVVLLDGELSPYAFEPLFSGKSALSLFLEKAASLPPELNVFLNTSAPSKDEVSPTSSSNKLDPVKVVSR
DDWTEIALLEKISSESEDADCFLYFPGDAPFLDPDLTEKLLERHLEYLAEYSFADGYPYGIAPEIISRGA
LPILPELAKTKEIPVSREAIFDILKKDINSFDIETEISPPDLRLLRLDLSADSKRNALLCSRLIKAKLDL
NAEEISEILEEEPELLRTLPAYYEIQIYRGCPLACSYCPYPKFPDASTEKKFMDPEVFKSLLDKIAEFSE
DAVISLSGWGEPLLHPDFAEIVEEVLSYPNLSLLIETSGIGWDSSLLEKLAALSEKAPGRLTWIVSLDAV
EQELYAKIRGDGELEEALSNIDALSKIFPGNVYVQFTRMKENEDELESFYRFWKKKGGEVIIQKYNRFCG
LLPDRRVADLSPLIRDPCWHLKRDLTILADGSVPLCRQDINKGHSLGNVFEESLEEIWKKGEELYLEHLN
GEYPGPCANCDEYYTFNF
>gnl|CDD|275126 TIGR04322, organic_radical_activating_enzyme, putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE. Members of this radical SAM domain protein family appear to be the E. coli form of the queuosine biosynthesis protein QueE. QueE is involved in making preQ0 (7-cyano-7-deazaquanine), a precursor of both the bacterial/eukaryotic modified tRNA base queuosine and the archaeal modified base archaeosine. Members occur in species that lack known forms of QueE but usually are not found in queuosine biosynthesis operons. Members of this family tend to form bi-directional best hit matches to members of known (TIGR03365) and putative (TIGR03963) QueE families from other lineages
FETIQGEGSFTGVPAIFIRLQGCPVGCSWCDTKHTWEVDPEDQVSLGQILAKKADSPTWANLSAEEILAL
IKQQGYTAKHVVITGGEPCMYDLRPLTELLEAHGYSCQIETSGTFEILCTESTWVTVSPKINMKGGYPVL
ASALSRANEIKHPVAMQKHIEELDALLAGLKDLKNKVICLQPISQKKRATELAIKTCIARNWRLSVQTHK
YLNIE
>gnl|CDD|213936 TIGR04323, hypothetical_protein_HIMB100_00022940, sporadic carbohydrate cluster protein, LIC12192 family. Members of this uncharacterized protein family mark a rare but widely distributed carbohydrate biosynthesis cluster found sporadically in genera Bradyrhizobium, Leptospira, Magnetospirillum, Oscillatoria, Prochlorococcus, etc
GLRGYITSRPFGGERLPQRVQNLVIRDYARRKGLTFLLSATEYAFENCYMQLNSVLDELDELEGIIFYSL
FMLPKDSEKRLEIYDRVLNKGASLHFALEDLKLSIEKDIERIEDILLLKKIL
>gnl|CDD|275127 TIGR04324, conserved_hypothetical_protein, sporadic carbohydrate cluster 2OG-Fe(II) oxygenase. This family, related to streptomycin biosynthesis protein StrG and to phytanoyl-CoA dioxygenase, belongs to the 2-oxoglutarate and Fe(II)-dependent oxygenase superfamily, which includes not just dioxygenases, but also some chlorinating enzymes involved in natural product biosynthesis. Most members of this family are adjacent to a member of TIGR04323, and occur in a larger carbohydrate biosynthesis cluster found sporadically in genera Bradyrhizobium, Leptospira, Magnetospirillum, Oscillatoria, Prochlorococcus, etc
SKNFIEKGYVIFKVEDTAALDAIRSTIVNLIKESLKIKKKDLNELHKKVSVSDLNELRLKAYNSLNKLSD
FREKYFSLAKPEIEELVGNELAMQKNINLSIQMPGDDTSLLPLHSDVWSGDSPFEVVVWIPLVNVYKTKS
MYILNPEISKEMLSRMKKLKCRGMEDLFKKYKKKAHWIEINYGEALLFSPTLLHGNVVNEEDETRVSINC
RFKSLFSPYASPEKKLGEFYEPITKRPVTKLGLEYKDP
>gnl|CDD|275128 TIGR04325, conserved_hypothetical_protein, putative methyltransferase, LIC12133 family. Members of this family tend to occur next to glycosyltransferases and other characteristic enzymes of O-antigen biosynthetic regions. The founding member is LIC12133 from Leptospira interrogans serovar Copenhageni. PSI-BLAST reveals distant homology to known SAM-dependent methyltransferases, as in pfam13489
GFRGVYESFDEAEAHARSVGYDNDDILQKVLEAIRKVKLGEAVYERDSEYNYPLLFWLLRLAREGRLRVL
DFGGSLGSTYYQYKRFLPLPDGLRWTVVEQPEVVEAGRRLAEDGDRLSFYTDLEDAEGPDVLLLSGVLQY
LEDPLAELLALLAYNPRYILLNRTPFHEGPDFVTLQNVGSASYPYWFFNEEELVEGLEKAGYRLVDRWPS
PERRFSIPGHPEKSVESYRGFLFRL
>gnl|CDD|275129 TIGR04326, hypothetical_protein_HMPREF0179_02238, surface carbohydrate biosynthesis protein, LIC13510 family. This uncharacterized, rare protein occurs in the highly variable O-antigen region of some strains of Leptospira, as well as strains of and serves as a phylogenetic marker for the likely presence of six additional proteins, including an activated sugar-nucleotidyltransferase, an activated sugar epimerase and a dehydratase, an aldolase, and a DegT family aminotransferase. The patterns suggests a role in preparing a novel sugar for O-antigen incorporation
VAHWDSYSVPDDQISVPALLDAHFVRIRREYLAWAYRTGLVRVGGKTLVEHLQAGDGLSMWWMSLLVEKH
PKKTPFLYEILKLRALELLLDEKGVTELELRGCDANLAKILLAFCKATGIRFSHRPGSKDASLGRNRISP
GWAIYERLPALSAALARFLHWWWRVRRQLPPFPGSQPVSPGSIATYFPNLDMKAAENGRFRSRYWENLHD
ALDNAAVRTNWLFIYFPSPQVNLGDAIALRDRFRANGQDGASFHFLEEFLTLGDILRALLDYLRLAWRSR
ALERSVRELCRFPGSALDLWPLLQGDWADSTRGWRGLQRCLMLNAIDRYLKDLPPQEWGIFPQENQPWER
ALIHAWHSGGNGPVFGVQHSTVRPTDLRYFEDPRSFQDKACAAAMPDVIACNGNAALRALRAGGFPEDRL
ALVEALRYLYLASARAGRARPARGSPSKTRLLIVTSFFEDETRAQLQMLAAAAKAGLLAGYEVVVKPHPA
LPVEEDLAPLLGGPPAVVDGPITELLTPGTVVWASNSTSVALEAALKGLPVVVQLSGDDFNMCPLLGVPG
VVFVRSANELAAALAAPFLPKLPDDYFCLDPELPRWKKLLGL
>gnl|CDD|275130 TIGR04327, hypothetical_protein_LlicsVM_10020, outer membrane protein, LA_2444/LA_4059 family. Members of this family are predicted outer membrane proteins, apparently restricted to the Leptospiraceae (Leptospira and Leptonema)
KKKSFELLIRRNTYSWIPYEFTRYSDFSPPETNIEINSIQGNTKTLYPFGFVYENFSKKFRIEGNFFEFE
ITNPNSSVIRINPYGYQISTSLYNTLYRSEQELNLLKIYNLIENWRLSPGLGIRNLQSSKRRYGFYNYEG
AFSEYFNTLGPQVSLRSEYQLPRFFSFYINADYFYTEGTRFTKTNLASISSYSFVTSSAGRTGQFRGYEL
DASFSYYLFENLKLFFGYEYIYSYLSYLGFNQWNASFVSSSSSITLSNISTPLIRSNIEYAFRSGNLEIL
SGFYLGISVKF
>gnl|CDD|213941 TIGR04328, hypothetical_protein_HMPREF9709_01098, CRISPR-associated protein Cas4, subtype PREFRAN. Members of this family are the Cas4 protein of a novel CRISPR subtype, PREFRAN, found in Prevotella bryantii B14, Prevotella disiens FB035-09AN, Francisella tularensis subsp. novicida, Francisella philomiragia, Butyrivibrio proteoclasticus B316, Helcococcus kunzii ATCC 51366, etc
ILIAELNDFIFCPYSIYLHNYYLDFNDGIYKSTSQTKGSHAHKAIDENRYSTKKNDLQGTSVYCERYGLT
GKIDTFYINEGKLVERKKQVKQIFDGYIYQLYAQYFCLLEMGYKVNSIEFYSIDDNKHYPIDIPCEDKKE
MFEKFISVINQINPFDYSNFTNRKKCENCIYNPLCDKT
>gnl|CDD|213942 TIGR04329, hypothetical_protein_SbacW_07302_partial, CRISPR-associated endonuclease Cas1, subtype PREFRAN. Members of this family are the Cas1 endonuclease of a novel CRISPR subtype, PREFRAN, found in Prevotella bryantii B14, Prevotella disiens FB035-09AN, Francisella tularensis subsp. novicida, Francisella philomiragia, Butyrivibrio proteoclasticus B316, Helcococcus kunzii ATCC 51366, etc
DIEYKTIVFVNCNEGEKLRVSNGNLIVEDVNDSEIKTKLTFYKILALFIVGNISVTTPLIERCKKFNIAL
VLMKPSFRPYESFGDAAEANYLLRRKQYNMSENDISIAKIFVKNKIANQLTLLKSTRMKDELLTEAKFKL
TRYIDAIDAIEDDKRLMGIEGNVSKSFFKAYFQNNDWTGRKPRIKSDALNATLDLGYTILFNYIESFLRM
FGFDIYAGVYHKLWYKRKSLVCDLIEPFRCIIDNQVRKSFNLKQFTDEDFVINNGQWRLKTDKNKDYVRI
LFDAIIRYKGDIFKYVQAYYRAFMRGKTIADYPIFLI
>gnl|CDD|275131 TIGR04330, conserved_hypothetical_protein, CRISPR-associated protein Cpf1, subtype PREFRAN. This family is the long protein of a novel CRISPR subtype, PREFRAN, which is most common in Prevotella and Francisella, although widely distributed. The PREFRAN type has Cas1, Cas2, and Cas4, but lacks the helicase Cas3 and endonuclease Cas3-HD
YQEFTNLYSLSKTLRFELRPQGKTLENIKELGLLEQDKARAESYKELKKIIDKYHKDFIEETLSNVELSF
DLLEEYFDLYNKLKKSKKDKKDLAKEQDTLRKQIVKSLQDNLPESIFKNIFSKKLLKGVLEDFIKNTHKD
SEDEQNILIDIKEFKGFTTYFSGFHENRKNVYSQEDKSTSIAYRIIHENLPIFLANIPKFEKIKEKEALA
KNLSEIMGDFELYVAVSELDEIFSLDYYNNVLSQSGIDSYNAIIGGIMKNDAKIKGLNEYINLYNQKIKD
KKLPLPKLKQLHKQILSDREAKSFLPDMFEDDSEVVKAIKEFYEQTLEQGNVIGKLKTLLEKLDKLDLKG
IYIRNDNQLTTLSQQVYGNYNVIRTALEEYIKKQIEPKKGKSKKEKYDKFIKKVVKKQDYLSIQFINDLL
EKYIKEDDSKGRLFENIRDYFAEISLMRNEDFQTNDNIANIKTAYQTFERILLKSRKDLKQDEEVVKLIK
SLLDALKNLQHFIKPLLGKGDELDKDEIFYGDFDPIYEKLNNITPLYNKVRNYVTQKPYSDEKIKLNFEN
PTLANGWDENKEIDNTAIILRKDNKYYLAIMNKKNNKIFDKDEKTKDDYEKMVYKLLPGANKMLPKVFFS
KKNIEEYTPSERIIEIYKKGTHKKTGIGIEENFNISDCRYLIDFFKESISKHEEWSKFDFGFSDTDSYND
ISEFYREVETQGYKIEFINISEEYINKMVDEGKLYLFQIYNKDFSPFSKGKPNLHTLYFKALFSEENLQN
IIYKLNGQAEIFYRKASLPNKVTHPAKSILVAIKNKNGENVPMHIKESIFKYYNGFIIESELFIMAYLAE
HDVAIKKANEDIIKDKRYTEDKFFFHLPITINFKATGRTYINDKVEEYLRTADDVHIIGIDRGERHLLYY
SVIDSKGNIVEQKSLNIIDNNDLETNYHDLLDEREKEREHARKNWQTIENIKELKEGYISQVVHQIAKLM
LKYNAIVVMEDLNFGFKRGRFKVEKQVYQKFEKMLIDKLNYLVFKKKKEDEAGGLLNAYQLTNKFESFNK
LGKQSGFIFYVPAWNTSKIDPVTGFVNLFDTKYETIDKAKQFFGKFDDIRYNADKGYFEFEFDYNNFYPK
AELGTRTEWTICTFGERIKSKRNKDKNNYWDTEEINLTEEIKALLEDNAINYGDGNCDKEAIAGKSDKKF
FADLLSLLKLTLQMRNSETGTENDYLISPVANDEGNFFDSRNGPKLPKDADANGAYNIAKKGLMLIRKIK
QEYRGDKKLDLSISNTEWLDFVQNKP
>gnl|CDD|275132 TIGR04331, conserved_hypothetical_protein, putative transferase, LIC12162 family. This protein family shows C-terminal sequence similarity to various surface carbohydrate biosynthesis enzymes: spore coat polysaccharide biosynthesis protein SpsB, UDP-N-acetyl-D-glucosamine 2-epimerase, lipid A disaccharide synthetase LpxB, etc. It may occur in O-antigen biosythesis regions
LVLSALEEFWDEDANHLFLGPWCKVYDRRKVWEKVDFEVLPYPWSDREDFVQDYDYLDALYERILPSLAK
RLNAIHGTQHSLRYWRILLGPWLIHFIPILYDRYLSIKLALEKVPDVKALVLEEKDFRPRGDFDDFNHLL
SDDDYNFWLYSELLKYLKPPAIQKSILEPLPVNDIRKDTLQNSPLPLAKIQAFLLRLRVFLGRLFCRSQP
PVLILDSYFSALNKILLIIWLGGRPRRIKFYTSSQVGASRNFRKRLDLTLPFFALNEFENFLFRLLPQLL
PKSYLEGFKALLRSSLSKYPGSPKLIFTANALWYDEKFKIWAAAQVEKGAKLIYVQHGGNYGQGRVFNAE
DHEEKISDRFITWGWSEESIRNKVIPLPSPKFKGKKIRRKDNQGEILFVGTAMPRYSYRLASGPLSDQML
AYLKWQIDFFSALSPETRSNLIYRPYPSDSGWNQTQRWLEDFFPRLKIDDGNRSFEELMARCRLIVCDYL
STTFLEALAANKPTILFWDREAWELRPEAEPYFDRLRDAGILFEDPESAAAHVNQIWDDPEGWWNSPEVQ
AARKLFCEQYARESGNPFKYWKQEL
>gnl|CDD|275133 TIGR04332, hypothetical_protein, poly-gamma-glutamate system protein. Poly(gamma-glutamic acid), or PGA, is an extracellular structural polymer found in Bacillus subtilis and a number of other species. PGA is sometimes capsule-forming, sometimes secretory, and may be produced by Gram-positive (single plasma membrane) and Gram-negative (inner and outer membranes), so export and/or attachment machinery may differ from system to system. Members of this family occur in a subset of PGA operons, in lineages that include Francisella, Leptospira, Treponema, Thermotoga, Fusobacterium, and Clostridium, among others. Because gene symbols pgsWXYZ are not yet in use, we suggest pgsW, as one of a series of poly-gamma-glutamate synthesis auxiliary proteins
IWLLLLLAILLLGLLLLLRPKGTVKTDNYAEKIEAAQLMRRAMAVLKEEKLKRGIPIDPELDPNRTGLIG
EEWSPITTTLGSLEAKRTSANPDFAALVVRWFKKAGLKEGDTIAVGASGSFPGLNLAVLSAAETMGLKVI
IISSLGASTYGANDPEFTWPDMERILRERGLLSTKSLAYSLGGDDDIGGGLPEEGLELLVRRAERNGVPL
LYEKSLEESIAKRMALYEAGKPPKAFVNIGGSLANLGTSPEVLKLPPGLLRPPVKSEDAGDGLIGYFLRR
GIPVIHLLNIKGLARDYGLPYDPQPIP
>gnl|CDD|213946 TIGR04333, hypothetical_protein_IYC_10989, Cys-rich peptide, Clo7bot family. Members of this protein family range in size from 34 to 53 residues, including from four to seven Cys residues. Multiple strains of Clostridium botulinum show seven tandem members upstream of a radical SAM/SPASM domain protein likely to act as a ribosomal natural product maturase. By analogy to subtilosin A, the Cys residues are likely targets for modifications that may introduce new crosslinks. Across multiple strains of Clostridium botulinum and C. sporogenes, the adjacent radical SAM enzyme is nearly invariant
MKYIKKPSKKYVLGYCVASCSDNCHNNCGRQCVV
>gnl|CDD|213947 TIGR04334, rSAM_Clo7bot, radical SAM/SPASM domain Clo7bot peptide maturase. In multiple strains of Clostridium botulinum, this single radical SAM domain protein occurs next to a tandem array of seven homologous Cys-rich small peptides (see TIGR04333). Because this radical SAM enzyme contains the SPASM domain, associated with peptide modification, it is proposed to modify all seven C. botulinum targets, hence the name Clo7bot for this system. Suggested gene symbol is ctpM (Clostridial Tandem Peptide Maturase) [Protein fate, Protein modification and repair]
KVSKYNLIWNLEDGKTIAFNSMTCALAEVDDDFINIIENINHINYEELDDKEKTLVDNMLEGNYIVHDDF
DELKLLKYEHFSGKFNNNSLGLTIAPTLSCNFACPYCYENPKSGIMDKNVTDALIEMITEEAKKKKDINI
TWYGGEPLIAKNVVFDMSQKIIEICKKHNTNYSAYIVTNGYLIDDVVISKLNDLKINGAQITLDGPPNIH
NKRRKLKNSDEGTFEVILSNVKKLKKNGINIIIRMNIDKTNMDSIEELLDILEENGLKDVSISLGKVTAY
TGTCVSMAESCLNTEEYAKENLKYQQKLFQRGFNIGGFYPFYPTMKANYCGADNIGTFVLDPEGYMYKCW
NDVGNTDRAVGNVLERKNDPDEKMYMRNVDYILWSPFDHEECLECNVLPICMGGCPYNGLMNGSKPECEK
WKYNLEEVLELTYLQKNIEN
>gnl|CDD|275134 TIGR04335, AMMECR1_domain_protein, AmmeMemoRadiSam system protein A. Members of this protein family belong to the same domain family as AMMECR1, a mammalian protein named for AMME - Alport syndrome, Mental Retardation, Midface hypoplasia, and Elliptocytosis. Members of the present family occur as part of a three gene system with a homolog of the mammalian protein Memo (Mediator of ErbB2-driven cell MOtility), and an uncharacterized radical SAM enzyme
RILLKLARQAIESALANGRLPDLSPGPPKLNEKGGCFVTLHKNGELRGCIGTIEADRPLVEDVAENAIAA
AFKDPRFPPLTEDELDRLTIEVSVLSPPEPLPVEDEEELLEELRPGRDGLILEDGGRRGLFLPQVWEELP
DPEEFLRHLCLKAGLPPDAWRDDVTIYRFTVEVF
>gnl|CDD|275135 TIGR04336, hypothetical_protein, AmmeMemoRadiSam system protein B. Members of this protein family belong to the same domain family as the mammalian protein Memo (Mediator of ErbB2-driven cell MOtility). Members of the present family occur as part of a three gene system with an uncharacterized radical SAM enzyme and a homolog of the mammalian protein AMMECR1, a mammalian protein named for AMME - Alport syndrome, Mental Retardation, Midface hypoplasia, and Elliptocytosis. Memo in humans has protein-protein interaction activity with binding of phosphorylated Try, but members of this family may be active as enzymes, as suggested by homology to a class of nonheme iron dioxygenases
RPPAVAGRFYPGDPEELREQIEEFLSHAPPEGGPGKAKGLIVPHAGYVYSGPVAAHAYAALKKGRPETVV
LLGPNHTGYGSGIALPPEGSWETPLGDVPVDEELAEELLEHSPIIELDDLAHLREHSLEVQLPFLQYFFP
DFKIVPIVVGDQSPEVAAALGEALAEAIKELGRDVLIVASSDLSHYEPDEEARRLDRAAIEAILALDPEG
LYDVVREKNISMCGAGPIAALLEAAKRLGALKAELLDYATSGDVSGDRSRVVGYASIVF
>gnl|CDD|275136 TIGR04337, Radical_SAM, AmmeMemoRadiSam system radical SAM enzyme. Members of this protein family are uncharacterized radical SAM enzymes that occur in a prokaryotic three-gene system along with homologs of mammalian proteins Memo (Mediator of ErbB2-driven cell MOtility) and AMMERCR1 (Alport syndrome, Mental Retardation, Midface hypoplasia, and Elliptocytosis). Among radical SAM enzymes that have been experimentally characterized, the most closely related in sequence include activases of pyruvate formate-lyase and of benzylsuccinate synthase
TRYWHRLDDGRIQCDLCPRFCKLREGQRGLCFVRARQDGQIVLTTYGRSSGFCIDPIEKKPLNHFLPGTP
VLSFGTAGCNLACKFCQNWDISKSREMDTLADQASPEQIARAALRLGCRSVAFTYNDPVIFAEYAIDVAQ
ACRERGIKTVAVTAGYICPEPRAEFFAHMDAANVDLKAFTEDFYHKLCGGHLQPVLDTLRYLRHETDVWL
EITTLLIPGENDSDAELEAMCEWIVENLGPDVPLHFTAFHPDFKMLDTPPTPPATLTRAREIALANGLHY
VYTGNVHDPDGGSTYCPGCGARLIGRDWYELGEWRLDAQGRCPRCGTPLAGVFEAAPGDWGRRRLPVRI
>gnl|CDD|275137 TIGR04338, hypothetical_protein, putative metallohydrolase, TIGR04338 family. This protein family is restricted to the Actinomycetales, including Mycobacterium, Rhodococcus, Nocardia, Gordonii, and others. The invariant motif HEXXH, at the core of the best conserved region in the protein, suggests metallohydrolase activity, as does local sequence similarity in this region to other metallohydrolases
RDSQRARVYAAERLVRTLFDRAGGSRTVQIAGTQLTLPPEARFASVESVQRYVDRVLALPSVRARFPRAA
VPVRVRARRGTRAAHYERAGGTIAVPDGRDGRWALRELVVLHELAHHLDDGEGPAHGPEFVATLIELVGL
VMGPEAAFVLRVVLADSGV
>gnl|CDD|213952 TIGR04339, hypothetical_protein_SacmaDRAFT_2380, Actinobacterial PQQ system protein. Members of this protein family are restricted to members of the Actinobacteria (Mycobacterium smegmatis, Streptomyces hygroscopicus, Geodermatophilus obscurus, Pseudonocardia dioxanivorans, Saccharomonospora marina, etc) that synthesize PQQ. This small protein, 155 amino acids long on average, is found regularly next to a much larger protein, a PQQ-dependent oxidoreductase, and might be a companion subunit or an accessory protein such as chaperone involved in cofactor insertion
TAEERSALLAELGLDGQNRAALGRLLGTGSIGHAEEGPDGRMRATIRIPPDELIWDPAILVLPHGGDLEL
EIINDDKNTHCALLPSNGDSKFIWLPNHSKGTATLNLDGPGYYWYGSPIGNDEGRGLTGAIVVGGEVPPS
ARLDRPQQPRP
>gnl|CDD|213953 TIGR04340, radical_SAM_domain_protein, radical SAM/SPASM domain protein, ACGX system. Members of this protein family are radical SAM/SPASM domain proteins likely to be involved in the modification of small, Cys-rich peptides. Members of the family of proposed target sequences, TIGR04341, average 75 amino acids in length and average six instances of the motif ACGX, where X is A, S, or T
PYFSFQWHITDDCDQRCKHCYIYSGGSNAEVNRMSFEQMQDTLDNIEDFCRKFGREPYLYITGGDPILHP
DFWNLLDLLKSKNIPFTILGNPFHLNDEVCERLKDLGCERYQLSIDGLRQTHDWIRKPGSFDETLAKIPM
IRKAGIRAAVMTTVSDVNAAEIPAIIDAVVEHHVDVFAFARYCPTLGERDTGLSPMEYRALLDRCWKKFE
AYKDSGCETYFNLKDHLWTLYEYEEGLFSIPKNADEGIIYDGCNCGNGHLTILSTGDVYACRRFESKVGN
ALTDRLYDVFLGNEMDKYRQIDKFEKCSRCELLRFCRGCPAVARGYDGSFYAADPQCWKEV
>gnl|CDD|213954 TIGR04341, hypothetical_protein_HMPREF9457_01855, ACGX-repeat peptide. Members of this family average 75 amino acids in length and average six instances of the motif ACGX, where X is A, S, or T. Members are proposed target sequences for modification by adjacent radical SAM/SPASM domain proteins (family TIGR04340). Cys residues adjacent to Gly residues are common as proposed sites for modification by radical SAM enzymes
MALSNLFGWVNEKEVKAQAACGAEEKKTACGTACGAGDKKPAEKPAACGTACGAGDK
>gnl|CDD|275138 TIGR04342, hypothetical_protein, EXLDI protein. The most conserved region in this protein family is the C-terminal pentapeptide, with motif ExLDI. Members from the Firmicutes average about 120 amino acids in length, while members from the Actinobacteria have an additional 45-residue amino-terminal segment not included in the model. In it is suggested that the member from Streptococcus mutans UA159, and its homologs, participate in bacteriocin production, export, or immunity
FEEIELRVGEDGIRRRKRFQGRKLASWSRPSEDGTRITTKRVYRTRKGKYVVYTRTDPNWAAGPSDNWSD
PKSWRRLFLVGQDWGDRVLEVVDTLEELRDKLPKELYERLESKVEHPPIEDLDI
>gnl|CDD|275139 TIGR04343, pyridoxal-phosphate-dependent_transferase, ergothioneine biosynthesis PLP-dependent enzyme EgtE. Members of this protein family are the pyridoxal phosphate-dependent enzyme EgtE, which catalyzes the final step in the biosynthesis of ergothioneine [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
LAERWRAARPPVAGVHLDSAACSRQSFATLDAVAQHARHEAEVGGYVAAEAAAPVLDAGRAAVAALTGMP
AADVVFTTGSNHALDLLLGSWPGPSRTVACLPGEYGPNLAIMAAHGFEVRELPVDDDGRLDVDGAASALR
ADPPALVHLTVVGSHRGTVQPAAAVAELCRAAGVPLVVDAAQALGHLDCAVGADAYYSSSRKWLAGPRGV
GVLAVRPELLERLAPRLPPPDWPEASPLAVAQRLEHGEANIAARVGFSVAVGEHLAAGPAAVRARLAEVG
RAARRALADVPGWRVVEPVDEPSAITTLEPTDGADPAAVRRRLIAERRIVTTYAGVARAPFELTTPVLRV
SPHVDVTAEELEQLARVLAR
>gnl|CDD|275140 TIGR04344, generic_methyltransferase, 5-histidylcysteine sulfoxide synthase. Ovothiol A is N1-methyl-4-mercaptohistidine. In the absence of S-adenosylmethione, a methyl donor, the intermediate produced is 4-mercaptohistidine. In both Erwinia tasmaniensis and Trypanosoma cruzi, a protein occurs with 5-histidylcysteine sulfoxide synthase activity, but these two enzymes and most homologs share an additional C-terminal methyltransferase domain. Thus OvoA may be a bifunctional enzyme with 5-histidylcysteine sulfoxide synthase and 4-mercaptohistidine N1-methyltranferase activity. This model describes the 5-histidylcysteine sulfoxide synthase domain, a homolog of the ergothioneine biosynthesis protein EgtB [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
RPPDLSGGDVEQKRKEIRDYFENTWELYESLFSLLKDEDAFYLKPDPLRHPLIFYFGHTATFYINKLVLA
GLIDERINPRFESIFAIGVDEMSWDDLNDAHYDWPSVDEVRAYRQKVRALVLELIDTTPLSLPITWESPL
WAILMGIEHERIHLETSSVLIRQLPLELVKPPELWPYCPDHSGDAPENELISVPGGEVKLGKPDDDPTYG
WDNEYGSHRAEVKPFKASKYLVSNGEFLEFVKAGGYENQRYWSEEGWEWKQFRNAKHPTFWVPDSHGYRL
RTMFEEIPMPWDWPVEVNYLEAKAFCRWKSAKTGKPIRLPTEAEWHRLRDKSGVSDDPDWRDEAPANLNL
AYGASSCPVDRFSQGGFYDVVGNVWQWTETPIYPFPGFEVHPLYDDFSTPTFDGKHNLIKGGSWISTGNE
ALRSARYAFRRHFFQHAGFRYV
>gnl|CDD|275141 TIGR04345, hypothetical_protein, putative 4-mercaptohistidine N1-methyltranferase. Ovothiol A is N1-methyl-4-mercaptohistidine. In the absence of S-adenosylmethione, a methyl donor, the intermediate produced is 4-mercaptohistidine. In both Erwinia tasmaniensis and Trypanosoma cruzi, a protein occurs with 5-histidylcysteine sulfoxide synthase activity, but these two enzymes and most homologs share an additional C-terminal methyltransferase domain. Thus OvoA may be a bifunctional enzyme with 5-histidylcysteine sulfoxide synthase and 4-mercaptohistidine N1-methyltranferase activity. This model describes C-terminal putative 4-mercaptohistidine N1-methyltranferase domain [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
YETDPLVSQYCEAHYGEEYFGVPNFPVKLAELALAQFRNKSRKRALDIGCAVGRASFELARYFDEVDGID
FSARFIRPAVALKERGSLRYALKEEGELVSFKEVTLSDLGLDEVRDRVSFFQGDACNLKPHFTGYDLILA
ANLLDRLYDPAAFLSSIHERLNPGGLLVIASPYTWLEEYTPKENWLGGFKKDGENVTTLDGLKEILSKNF
ELVGEPTDVPFVIRETARKFQHTISELTVWRK
>gnl|CDD|275142 TIGR04346, DotA_TraY, conjugal transfer/type IV secretion protein DotA/TraY. Members of this protein family include transfer protein TraY of IncI1 plasmid R64 and DotA (defect in organelle trafficking A) of Legionella pneumophila
LSVQILDSLFGSVVNNPLGGSGGPDTILGSIFGVFNLVILIVGSILLSYTIIAGLLNTAHDGELLGKKYS
SVWTPLRTVIGIALLLPIAKGFSLIQLLVLWLAVQGIGLANLVWSAGADALNFGGGVLVTTQPVQPKTAE
VAKGLLESEVCRAADNVNKGSGAPNLGPISKSSIGYSGAWSTGSTSYGYTLKFGNATGSVGICGSVSFSF
SGDDAQSVNGAGLAPFTTGDLDSVCQAQQQALVTAISDLITAASEIANTIWQGASITGTALPEVAASIET
AADAYEALVADALSAASSDQQAQIKKENFATTAKELGWASAGAWYWTISRLNQKVLAAANSLPTVTGPSG
SGLGSRFSGLFDAYIEALSQVILADAYATPAGTSALAGAEAVASAAEAGDNFSAIWKFLRGLMSMWVGTS
ISFTSNETSSGTNPLIAMKNIGDYLIGIAEATYGAGAVLGAVGSGVALGGVIAGFLGFVGGGAAALSGLL
SAISFVLFPLALALFIMGLILAYYLPFIPFIIWMGAVVGWLILVVEAVVAAPLWALAHLLPEGDGLAGQR
AGQGYLLLLSILLRPPLMVIGFFAAILLSDVIGTLLNKLFAIALANVQSGSVTGILGFIAMLVIYAVILF
LLIAKLFGLIHELPDHVLRWIG
>gnl|CDD|275143 TIGR04347, pseudo_SAM_Halo, pseudo-rSAM protein/SPASM domain protein. Members of this family all have a C-terminal SPASM domain (see model TIGR04085), a region usually found as a C-terminal second 4Fe-4S domain of radical SAM domain (see pfam04055) proteins. A majority of rSAM/SPASM proteins modify ribosomally produced peptides. In a few members of this family, the key Cys residues of the radical SAM domain have been lost, making this a pseudo-rSAM family. Members of this family are restricted so far to Haloarchaea, always occur next a member of family TIGR04031, and are often accompanied by another rSAM/SPASM domain protein. The function of this two or three gene cassette is unknown
ISVSKLLCDLGAEGDGLRYDAADGADSEQITEEKQRRPVVVWNTTRRCNLYCEHCYAGADTEAAPGELST
AEAKALLDDLADYGVPVILFSGGEPLVRDDLEELVAYAADAGIRPVLSTNGTLLTEERAEALRDAGLDYA
GVSVDGLPERNDEFRGKDGAFDAAVRGIENCLDVGLKTGLRYTITEANAPDLEEVVDLLADVGLDRFCFY
HLDYGGRGAEISDLDLDPAAQRRAVRRVCDLTLEYHDRGEEIETLLVGNYADAAYIVEYAREELGEDRAE
AIYRYLESNGGDPTGERVADVDYQGNVHLTQFWQGYSLGNVRDRPFGDIWEDESNPLLAKLRDREEHLTG
KCADCQYKSICRGGSRLRALAAGGDLFAPDPQCYLTDEER
>gnl|CDD|275144 TIGR04348, glycosyl_transferase_group_1, putative glycosyltransferase, TIGR04348 family. This putative glycosyltransferase is found in marine bacteria such as Marinobacter and soil bacteria such as Anaeromyxobacter, but does not seem to occur in known pathogenic bacteria
IVIITPALADSNNGNWQTARRWARFLRGAHQVRVATAWDGAPADLMIALHARRSADSIAAWADAHPDRPL
IVVLTGTDLYRDIHTDPEAQRSLELADRLVVLQDRGLDALPPALRAKARVIYQSAPARRPRAKTKRHFRV
VMVGHLRDEKDPLTAALAARLLPGHSDIRIDHIGGALDPEWAAAARAEMAANPRYRWLGELPHAATRQHI
QRAHLLVISSRMEGGANVISEAVASGTPVLASRISGNVGMLGDDYPGYFPVGDAAALARLLLRAEQDPAF
LAALRAQCAARAPLFAPERERAALRRLVAR
>gnl|CDD|275145 TIGR04349, Radical_SAM_domain_protein, putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE, gammaproteobacterial type. Members of this radical SAM domain protein family appear to be a form of the queuosine biosynthesis protein QueE. QueE is involved in making preQ0 (7-cyano-7-deazaquanine), a precursor of both the bacterial/eukaryotic modified tRNA base queuosine and the archaeal modified base archaeosine. Members occur in preQ0 operons species that lack members of related protein family TIGR03365
LRITEIFYSLQGETSTVGLPTVFVRLTGCPLRCVYCDTAYAFSGGERMSLDDILAQVASYGARYVTVTGG
EPLAQPACLPLLTALCDAGYEVSLETSGALDISGVDPRVVKVMDLKTPGSGEVARNLWENLALLTPHDQI
KFVLCDRADYDWARQKLREHALAERCEVLFSPVYGQLAPADLAEWILADRLPVRFQLQLHKLLWGDAPGR
>gnl|CDD|275146 TIGR04350, aminotransferase_class_I_and_II, putative C-S lyase. Members of this subfamily are probable C-S lyases from a family of pyridoxal phosphate-dependent enzymes that tend to be (mis)annotated as probable aminotransferases. One member is PatB of Bacillus subtilis, a proven C-S-lyase. Another is the virulence factor cystalysin from Treponema denticola, whose hemolysin activity may stem from H2S production. Members of the seed alignment occur next to examples of the enzyme 5-histidylcysteine sulfoxide synthase, from ovothiol A biosynthesis, and would be expected to perform a C-S cleavage of 5-histidylcysteine sulfoxide to leave 1-methyl-4-mercaptohistidine (ovothiol A)
FDRVIDRHGTDSEKYDLREERFGRADVLPMWVADMDFATPPAVLEALKQRLEHPVFGYTLPPDSLYAAVI
NWLAQRHGWQIDPEDIVFLPGVVPSLFAAVRALTAPGEGVIVQTPVYPPFLSAVKSNGRELVLNPLKLDE
GRYRFDLEDLEDAITEKARLLLLCSPHNPVGRVWTREELTRLAELCLRHNVVVVSDEIHADLVYPPNKHI
PLASLSPEPAERTVTLLSPGKTFNIAGLNISFAIIPNPELRRAFQEAAQRVHIQHGNLFGYVAFEAAYRD
GEPWLDALLAYLRGNRDLVEEFIAKRLPQIRVRPPEATYLAWLDCRALGLDDADLRAFFIEQAGLGLNPG
ISFGDGGSGFMRLNFGCPRSTLEQALERLRQALA
>gnl|CDD|213964 TIGR04351, hypothetical_protein_SclaA2_02770, putative TOMM peptide. Members of this family of short peptides average about 110 amino acids in length, with greatest variability in the last thirty. The conserved region resembles the alpha subunit of nitrile hydratase, as with the NHLP leader peptide domain (TIGR03793), and members usually are found near a cyclodehydratase (maturase) enzyme, marking these as like thiazole/oxazole-modified microcins (TOMM), but these precursor forms lack the GlyGly cleavage motif that marks the clear end of a leader peptide region. Genomes with this system include Streptomyces clavuligerus ATCC 27064, Verrucosispora maris AB-18-032, and Kitasatospora setae KM-6054
RFAELVARAWLEPELADRYQNDPAEVLAEFGITLPAGAQPPLLPPKPV
>gnl|CDD|275147 TIGR04352, hypothetical_protein_imdm_1353, HprK-related kinase A. A number of protein families resemble HPr kinase (see TIGR00679) but do not belong to that system. They include this family, which appears instead to be the marker for a different type of gene neighborhood, in which one of the conserved neighboring proteins resembles (but is distinct from) PqqD
LSLRLGPFNVRIRSDVPSVARSLALLYADFPLADDDGFVDFHIALLRGPGLRRWFRPQVRFWFDGQSPFK
PLPLDQAFPLLEWGLNWCVATRAHHYLLLHAAVLERDGRALILPAPPGSGKSTLCAALALRGWRLLSDEF
ALLDLEDGLLLPLPRPISLKNESIDIIRAFAPGAVLGPVFPDTRKGTVAHLRPPRESVVRRDEPARPAWI
VFPRYQPGAPLTLEPRSRARAFMRLAENSFNYEVLGEVGFDAVARLVDRCDCYEFSYSDLDEAVEVLDQL
>gnl|CDD|275148 TIGR04353, hypothetical_protein_MarpuDRAFT_0194, PqqD family protein, HPr-rel-A system. Members of this protein show distant homology to PqqD, and belong to a three-gene cassette that included the HPr kinase related protein family of TIGR04352. The role of the cassette, and of this protein, are unknown
WDDEAVVYHPRSGDTHLLNSPALELLAALDEGPATEDALLAALAERLGLEEPDEAEDSLEQALAELRELG
LIR
>gnl|CDD|275149 TIGR04354, conserved_hypothetical_protein, amphi-Trp domain. This domain usually comprises most of the span of bacterial or archaeal proteins with a length of about 90 amino acids. Some members, however, are extended by one or two copies of domain pfam07411 in the C-terminal region. No residue in this domain is invariant. A striking feature of this domain is a C-terminal region that alternates strongly charged with strongly hydrophobic residues and usually ends with a Trp residue, e.g. LEIEIEW or FEIKVRW, suggesting an amphipathic beta strand structure. We suggest the name amphi-Trp for this domain. Some members of this function occur regularly in genomic contexts that include putative kinases of unknown specificity related to (but distinct from) HPr kinase, a Ser-specific protein kinase. The function is unknown
FEHESLLSREEAAAYLEALADGLEEGELTLSDGDEEVTLEPPELVELEVEAEEKGGEEKLEIELSWK
>gnl|CDD|275150 TIGR04355, HPr_serine_kinase_domain-containing_protein, HprK-related kinase B. Members of this protein family resemble (and often are misannotated as) HprK, the serine kinase/phosphatase of the phosphocarrier protein HPr. However, members do not occur with an HPr homolog, but instead as part of a distinctive gene cassette of unknown function
TLAELVASIRKNHPATHTLFLQFGDCRLRVHTNSPELYDKLARYFRDFLAPAGATDISITAHEAAPPDLG
LPFTVKQPDPGKTKIKEEFADLPDGRVVRKRLTGMVFAFGDGENLAVGPCTANDNQVVNFINNRFIELKL
NRGCLLGHAAGVAHNGRGLALAGFSGMGKSTLALHLMSSGTTFVSNDRIMVERDTQGLTMYGVAKHPRIN
PGTALHNPDLAGVIPPEDRARFAALPPDELWELEHKYDALIDECFGPGRFVLGAPMDGLVVLNWRRDGSP
TRIQRVDLEERKDLLPAFMKSTGLFYLPEPGGRAIDPSQDAYLDLLSGCPVIEISGGVDFDAAADACLDF
L
>gnl|CDD|213969 TIGR04356, RimK_domain_protein_ATP-grasp, ATP-grasp enzyme, GAK system. Members of this family are ATP-grasp family enzymes related to a number of characterized glutamate ligases, including the ribosomal protein S6 modification enzyme RimK. This group belongs to a conserved gene neighborhood that also features an HPr kinase-related protein (see TIGR04355). We assign this system the initial designation GAK, for Grasp (this ATP-grasp family enzyme), Amphipathic (for the member of family TIGR04354, designated Amphi-Trp), and Kinase, for the HPr-kinase homolog TIGR04355
KIGVVGIPGKWSTERLADALEARTGFRLVIDMAQVELDLERGRVRYEGQDLSELDGLIIKKIGAVYSPDL
LDRLEMLRFLEGRGVPIFSRPESIIRLIDRLSCTVSLRQGDIPMPPTVVTEDLDAALEAVERYGKAVFKP
LYSTKARGMEVLEPGPGLRAALEAFRQGNPFMYIQQKVNLPGRDLGLVFLGGEYLGTYARVSRGDSWNTT
TNSGGKYAPCEPDAEIIELARKAQALFDLDFTCVDVAETADGPVVFEVSAFGGFRGLLEACGVDAAGLYA
DYVIEKL
>gnl|CDD|275151 TIGR04357, conserved_hypothetical_protein, CofD-related protein, GAK system. Members of this family are distantly related to CofD, the enzyme LPPG:FO 2-phospho-L-lactate transferase, involved in coenzyme F420 biosynthesis. This family appears to belong to a biosynthesis cassette of unknown function
GPRILFFSGGTALRGLSRQLTRYTHNSVHLITPFDSGGSSAVLRRAFAMPAVGDLRNRLMALADRTVLGN
PEIYRLFNYRLPKDASQEALRAELKAMASGRHPLVAAIPDPMRKLIRQHLRFFLEAMPEDFDLRGASIGN
LILAGGYLNNNRHLDPVIFLFSKLVQVRGVVRPVVDANLHLAAELEDGEVVVGQHRLTGKETPPLSSPIR
RLYLSDSLDGPEPVRVPLSEKNRRLIQSADLICYPMGSFYSSVVANLLPVGVGQAVARNPCPKVYIPNLG
HDPELLGMSLEDQVATLLYYLRADAGEDGKPSQLLDFVLVDSRHGEYPGGIDPEELERLGIRVIDAPLVS
EDSAPYYDPQLLAQALLS
>gnl|CDD|275152 TIGR04358, conserved_hypothetical_protein, XXXCH domain. Members of this family show C-terminal sequence similarity, perhaps indicating distant homology, to cytochrome c-prime (see pfam01322). However, the motif CxxCH is replaced by xxxCH. Genes for this protein occur in a sporadically distributed genome context, largely in deltaProteobacteria, in which an ATP-grasp family glutamate ligase homolog and a CofD (LPPG:FO 2-phospho-L-lactate transferase) homolog suggest a novel biosynthesis
YKTLKKRMKASFKQILESVADGQLPSEEEVQRFIRDSRRMVSYPGKGDEYYEAFLALADQLQAAVKNGDL
EAAVAAVDELEQAKKFCHER
>gnl|CDD|275153 TIGR04359, conserved_exported_hypothetical_protein, entry exclusion lipoprotein TrbK. The characterized model example of TrbK, from incompatibility group P (IncP) plasmid RP4, is an N-terminally processed lipoprotein, localized to the periplasmic face of the plasma membrane. TrbK prevents entry through conjugation by other IncP plasmids. Unrelated, uncharacterized proteins encoded in equivalent positions in other plasmid P-type conjugative transfer regions (e.g. TIGR04360) may have analogous functions [Mobile and extrachromosomal element functions, Plasmid functions]
LILILAALVAALLAGCDNEPMPEVNDENCKPENIKKIEDKAQRQEFASKCLRRHRGEFKPSPKKEW
>gnl|CDD|275154 TIGR04360, hypothetical_protein, conjugative transfer region protein TrbK. Members of this family regularly are encoded between the TrbJ and TrbL proteins essential for P-type conjugal transfer, and therefore are designated TrbK. Positional analogy to family TIGR04359 (the entry exclusion lipoprotein TrbK of IncP plasmid RP4), which is a lipoprotein and not homologous, suggests this protein may also be involved in entry exclusion. Members of this family are small, with a non-lipoprotein signal peptide and a conserved disulfide bond [Mobile and extrachromosomal element functions, Plasmid functions]
ARLVAVVFVAVAITAALIELRRRPAEPPVEAPAAEPQADPLRAELRRCRTLGMAAAEDPRCRAAWAENRR
RFFG
>gnl|CDD|275155 TIGR04361, entry-exclusion_protein, entry exclusion protein TrbK, Ti-type. Members of this family are encoded between the genes for TrbJ and TrbL of P-type plasmid conjugal transfer systems, and therefore are TrbK, a member of a guild of unrelated TrbK protein families. The similarly located TrbK of plasmid RP4 (family TIGR04359) functions in entry exclusion, and the current family may as well, despite lacking any detectable homology. Members of this family include TrbK of the Ti plasmid from Agrobacterium, shown not to be required for transfer, which would be consistent with a role in entry exclusion rather than transfer itself. Li et al. cite unpublished results that showed an entry exclusion function for TrbK of the Ti plasmid. This small protein shares close C-terminal sequence homology to the much longer protein encoded by the neighboring gene TrbJ [Mobile and extrachromosomal element functions, Plasmid functions]
RRLIIIAALAGVVAAASAGTVIWVVVQPSPAPTEEQRERREKFFGTGKERPIRGGQEMKPRW
>gnl|CDD|275156 TIGR04362, hypothetical_protein, choice-of-anchor C domain. This family describes an extracellular bacterial domain that occurs on a number of proteins with PEP-CTERM (exosortase recognition site) sequences at the C-terminus, as well some with an apparent alternate anchor sequence. Note that related pfam04862 (DUF642), as of release 26, is double the length of this model because it has two tandem regions homologous to this domain. pfam04862, in turn, belongs to a Pfam clan called the galactose-binding domain-like superfamily
NLITNGSFESGSDPGNGFSTLSAGSSAITGWTVGSGSVDLINGYWQASEGSRSIDLNGTTGPGGISQTFN
TVAGQTYRVTFDLAGNPDGGPGLKDLTVSVGGASQDFSFDTTGKTTANMGWTTKSFDFTATSTSTTLSFT
SLDNGGAWGPALDNVSV
>gnl|CDD|275157 TIGR04363, hypothetical_protein, FxLD family lantipeptide. Members of this protein family occur with a cassette of lanthionine-type peptide modification enzymes. Members are small (about 60 amino acids long), rich in Cys, and variable in copy number per genome (from one to three). These features suggest that members of this family are modified to become lantipeptides, although not necessarily a lantibiotic. There is no GlyGly cleavage motif to separate a leader peptide from core region.The considerable abundance in Streptomyces and relatively strong consideration hints at a non-antibiotic function. The motif FxLD in the N-terminal region is nearly invariant
DPFDLDVRVVEGGPVAAGLACDTDDGCGSTCGSACTS
>gnl|CDD|275158 TIGR04364, methyltran_FxLD, methyltransferase, FxLD system. Members of this family resemble occur regularly in the vicinity of lantibiotic biosynthesis enzymes and their probable target, the FxLD family of putative ribosomal natural product precursor (TIGR04363). Members resemble protein-L-isoaspartate O-methyltransferase (TIGR00080) and a predicted methyltranserase, TIGR04188, of another putative peptide modification system
AARLRAALVDELREDGVIRSPRVEAAFRTVPRHLFAPGAPLEKAYAANRAVVTKRDEDGRALSSVSAPHI
QAMMLEQAGVEPGMRVLEIGSGGYNAALLAELVGPSGEVTTVDIDEDVTDRARACLAAAGYPQVTVVLAD
AEAGVPELAPYDRIIVTVGAWDIPPAWLDQLAPGGRLVVPLRMRGLTRSIAFERAGDHLVSVSAQLCGFV
PMQGSGAHDERLILLDGGDVALRFDDGQPADPAALARALDSPRLEVWSGVTFRLPESFDTLELWLATALP
GFCRLAADNDAVETGLVAPSYPWGVPAVVEGGSFAYLARRPTEGGGGFEFGVIAHGPDAEALADAVAEQI
RAWDRDHRGGPAPTIRVYPAPTPDTELPGRRVIDKRHSRVALSW
>gnl|CDD|213978 TIGR04365, Autonomous_glycyl_radical_cofactor, autonomous glycyl radical cofactor GrcA. This small protein, previously designated YfiD in E. coli, is closely homologous to pyruvate formate_lyase (PFL) in a region surrounding the stable glycyl radical that is prepared by the action of pyruvate formate-lyase activase, a radical SAM enzyme. When damage at the site of this radical breaks the main chain of PFL, this protein acts as a spare part that reintroduces the needed stable glycyl radical. Cutoffs for this model are set to exclude a set of closely related phage proteins that appear to have a corresponding function
IKGIQITKAANQALLNSFWLLDEETNQARCLVAKAGFAADQVVPLSELGDFEYREIAIEAPAKVEGGQHL
NVNVLTRETLEDAVKNPEKYPQLTIRVSGYAVRFNSLTPEQQRDVITRTFTESL
>gnl|CDD|275159 TIGR04366, hypothetical_protein, cupin fold metalloprotein, WbuC family. Members of this family show sequence similarity to cupin fold proteins (see pfam07883), including conserved His residues likely to serve as metal-binding ligands. Many members occur in bacterial O-antigen biosynthesis regions. Some members have acquired the gene symbol wbuC (e.g. Jarvis, et al, 2011), but publications using this term do not ascribe a function
LIDQELLDELKAQAAKSPRLRANLNLHPSLDDPVQRMLIALEPGTYVRPHRHPHKSETFIVLEGELDVLL
FDDDGEVTERVVLSPGGGTFGVEIPPGTWHTLVALSEGTVIFEVKEGPYDPLADKDFAPWAP
>gnl|CDD|275160 TIGR04367, protein_of_the_SAM_superfamily, hopanoid C-3 methylase HpnR. Members of this are family are a B12-binding domain/radical SAM domain protein required for 3-methylhopanoid production. Activity was confirmed by mutant phenotype by disrupting this gene in Methylococcus capsulatus strain Bath. This protein family should only occur in genomes that encode a squalene-hopene cyclase (see TIGR01507) [Fatty acid and phospholipid metabolism, Biosynthesis]
MKVLAVHPSPLMYTKIFLRLEPLGLELVAGAARRAGHEVRLIDLQVESHADYLRLLESFRPDVVGFSLNY
LANVPEVIDLAKETKRRLPGCFVFVGGHSASFVARELLEHAEGAIDCVLRGEGEASAPLLLEAVADGGDL
LTVPGVVTLEGEGPPPRFLPSLDEPRPARDLLRHRRKYFIGVLDPCASIEFTRGCPWDCSFCSAWTFYGR
SYRTLSPEVAGEELARIREPGIFIVDDVAFIHAEHGMAIGEAIERRGIRKEYYLETRGDVLLRNKEVFEF
WKRLGLKYMFLGLEAIDAEGLKLFRKRVSLDKNFEALEFARSLGITVAINLIADPDWDRERFEVIRQWCL
EIPEIVNISVNTPYPGTEIWHTESRKLTTRDYRLFDIQHAVLPTTLPLEEFYEELVKTQQVLNRKHLGWR
ALRGTAGIVARLLARGQTNFLRMLWKFNSVYNPELQLADHARPVRYEMAPPPAPSTQKPDPKTLYVHQPA
>gnl|CDD|275161 TIGR04368, lysine_23-aminomutase_YodO_family_protein, glutamate 2,3-aminomutase. Members of this family are glutamate 2,3-aminomutase, a radical SAM enzyme with a pyridoxal phosphate group. It is closely related to lysine 2,3-aminomutase, but distinguished by architecture (longer N-terminal region, shorter C-terminal region) and replacement of key lysine-binding residues Asp293 and Asp330 (inferred from the crystal structure) by glutamate-binding residues Lys and Asn. Activity was demonstrated for sequences from Clostridium difficile, Thermoanaerobacter tengcongensis MB4, and Syntrophomonas wolfei str. Goettingen. The action of this enzyme creates beta-glutamate, an osmolyte [Cellular processes, Adaptations to atypical conditions]
EKREISLKRAAELKSRIEDYLEARDTIPTGLELEEEIEKRKEKILKYFGATEEDWNDWKWQLKNRISDVE
TLSKILNLTEEEIEEIKKVGRKYRWAISPYYLSLMDPDNPNCPIRLQSIPSIAELLDEKGELDPMGEEFT
SPAPAITRRYPDRLIINVTNQCAMYCRHCQRRRNIGEVDRHASREDLEAALDYIRNNPEIRDVLITGGDA
LLLSDETLDWLLTELDNIPHVEIKRIGTRVPVTLPQRITDELCAILKKHPPIYINTQFNHPLEVTPEAKE
ACDKLIKAGVVLGNQAVLLKGINNDPHVMKKLNQELLKIRVRPYYIFHAKPVKGTSHFITSVEEGLEIME
KLRGYTSGLAVPTYIINAPGGYGKTPILPQYLLSRGEDKVVIRTWEGKVFEYPN
>gnl|CDD|275162 TIGR04369, selenidewater_dikinase, oxidoreductase/SelD-related fusion protein. Some selenium donor proteins (selenide,water dikase, product of the selD gene, model TIGR00476) are fusion proteins with an N-terminal extension described by model TIGR03169. Members of this family have a C-terminal region similar to yet outside the scope of the SelD model, fused to an N-terminal region similar to but outside the scope of TIGR03169
LAGGGHSHALLLRRWAMRPHLRPAGLITLVSRSSTALYSGMVPGLIAGLYKLEEAAIDLRSLADRAGVSF
VQAEITGLDPHEKKLLLANRPPLRYSRLSLNVGAETFPAFERLVKRLAFPIKPLEPALAWIEQQDIHDPE
SSAPFRVVGSGLAAVEVALALRKRWPKRPLLLQARSRKINAKLRKALNAAGIELVTSLPSDAGPLLLCTG
SRAPSWLAASGLPVDGHGRVLTNATLQVEGHPHIFAVGDCAVIAAAPRPASGVWAVRAAKPLAANLERSL
KGRSLRPWRPQRIALQLLGGFPSGRPKAWALWGPFVIGPSRWLWRWKQRIDRRFMAGFRPLSPMMKVKEE
EPMACRGCAAKLPAAPLNAALKQAGLEGLGPSPEDAALIGSSNGGDLLLQSVDGFPALVSDPWLNGRLTA
LHACSDLWACGARVISAQAVVTLPKVSSALQQELLVQTLAGIKSVLEPQGAELIGGHTLESRSEPPEPIS
LGIQISLSVNGQLAPGRKPWPKGGLQPGDELLLSRPLGTGVLFAAAMAGAAEPEWLDAALEQMQQSQHPL
VELLAKHQNEDSFGIHACTDITGFGLLGHLGEMLESSNEPLRVLLDANAIPALPGALELLEAGFASTLAP
ANRRAWSLLEPDKNQPRIELFLGDISLNSSAHQALLELLVDPQTCGPLLIACPEKYAQALLAAGGWYRIG
LV
>gnl|CDD|275163 TIGR04370, hypothetical_protein, oligosaccharide repeat unit polymerase. Members of this subfamily of highly hydrophobic proteins, with few highly conserved residues, all may act to polymerize the oligosaccharide repeat units of surface polysaccharides, including O-antigen in Gram-negative bacteria such as Leptospira (assign gene symbol wzy) and capsular polysaccharide in Gram-positive bacteria such as Streptococcus. O-antigen biosynthesis enzymes produce a repeat unit, usually an oligosaccharide, which itself is polymerized. O-antigen polymerase, usually designated Wzy. This family bears homology to the O-antigen ligase WaaL, but known examples of WaaL fall outside the bounds defined here. This model is much broader than pfam14296 [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
SYKKKKDILSPIILFSLIWLLIFLLSLLLLSYLSFLYPLSDYTYLIIILGILIFIFGSLFLSLSLKSKKR
KTRKKKLSKISISLIILFLFFLILILLLLIILLLLLYIISLIGILGILSLLGSALGYLALSGSTFLSGLI
ILLYILIILLLLLFLLLLLKKKRKKLLLLLILLALLISLLTGSRTGLILLILSLLFIYYLFYKKKSLKKI
LKILLLLILVFILILLLFIRYIRSGDSLSESFESLLIYLIIYLGGPIYAFDNNLSNLNGPLGSLTFGEST
FRGIYSLLNSLGGGLSNFNPAYLFLPFVGGKGGGNVYTIFGDFYYDFGYIGVIIFSFLLGFIFGYLYKKK
KKNPFYLLLYAYLLYILIFSFFRDGFFSLLSIFILILFLILL
>gnl|CDD|275164 TIGR04371, conserved_hypothetical_protein, putative sugar O-methyltransferase. Members of this family appear to be SAM-dependent O-methyltransferases acting on sugars, based on iterated sequence searches and gene context. Members occur in Leptospira O-antigen regions, as well NanM from the biosynthesis cluster for nanchangmycin, which produces 4-O-methyl-L-rhodinose as an intermediate [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
DSAYQPTNYWRWQESRIVQELRRAGLTSFRSDPYTLGFFVPNFGGPGFQPTTKVVRTLSDLIVRRFPGWG
KLILELAKKLSRESTAVADYRLVNASSIQDGGPLLEKFSESDVGSPIEVFSFDGRSFSRSYLNYVLRLNF
LKKFFGDLSVFRVLEIGGGYGRLGEILLKLFPNAIYYIVDLPPQLALSEAYLSEVFPEEKVVLYAQTRKQ
ENIDLPDDGRIYFLPPWQLPLLGNGKIDLFVNFISFQEMEPDVVDNYLSLIDKLCKDAVFLRN
>gnl|CDD|275165 TIGR04372, hypothetical_protein, putative glycosyltransferase, TIGR04372 family. This domain occurs in proteins of various lengths, in contexts that include O-antigen biosynthesis regions of various Leptospira species. Hits to this model and PSI-BLAST analysis suggest distant sequence similarity to family 9 glycosyltransferases (pfam01075), including ADP-heptose:LPS heptosyltransferase (RfaF), an enzyme involved in LPS inner core region biosynthesis [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
AWFVCLHVRDSGYLKEEDGSLHSYRNADIEDYLDAIEALVDRGYQVIRMGDPVMTPLDPEHPGVIDYAHS
DYRSDFMDIYLLANCRFFIGTTSGLSLIALIFGKPVLLVNLIPLDILPWSANTLFIPKKLRDTKSGRYLS
FREIYSRPLGRYRTAEDFAKNGIELIDNTPEEILAAVKEMLERLDGTWVYTPEDNKLQKRFRALL
>gnl|CDD|275166 TIGR04373, protein_of_unknown_function_DUF323, EgtB-related enzyme signature domain. This model represents a signature C-terminal region of a distinct clade in the EgtB subfamily, other members of which participate in ergothioneine biosynthesis
YREYSQPWFGTHRVLRGGSFATRARLKHPRYRNFYLPERRDPFAGFRTCA
>gnl|CDD|275167 TIGR04374, hypothetical_protein_RS9916_38182, hercynine metabolism small protein. Hercynine is the betaine (trimethylated amino group) form of histidine. This small protein occurs in a conserved four-gene cyanobacterial cassette along with a EgtD, the methyltransferase that converts histidine to hercynine, and an EgtB homolog as in ergothioneine biosynthesis, likely to attach some thiol through its sulfur to the imidazole ring
SREDQRQAIKFQREKLIEELEAVYKHAFDRIGGLELGEGSVARLTQLLLRSRDAAITPLEEEIEKPLITK
APL
>gnl|CDD|275168 TIGR04375, conserved_hypothetical_protein, hercynine metabolism protein. Hercynine is the betaine (trimethylated amino group) form of histidine. This protein occurs in a conserved four-gene cyanobacterial cassette along with a EgtD, the methyltransferase that converts histidine to hercynine as in ergothioneine biosynthesis, an EgtB homolog that is likely to attach some thiol (e.g. gamma-glutamyl-cysteine) through its sulfur to the hercynine imidazole ring, and a small protein of unknown function (TIGR04374). Members are distantly related to phage shock protein A (PspA)
SWLDQLERELEQRLEAFLRANPDQDQLLREQHLQDRQQDLQRQRQQLQSEAEELRRQLLTLAEEVRAWRE
RSQRARAAGASDLAGRAEQHLQSLMEQGRQLWQELEALGRRFKEVEQQLAALKQQQKQPSGSSLDEDWAL
FEAEQELEELRRRQ
>gnl|CDD|275169 TIGR04376, conserved_hypothetical_protein, TIGR04376 family protein. Members of this protein family resemble TIGR04375 and, more distantly, to phage shock protein A (PspA). Members are restricted to the Cyanobacteria
GLFDDLSRFLETRLEEFLRNNPHLELQALLEQLREQEEDTLRLITDLQRQEKRLEDEILATAQEIQRWHE
RIEKAKAAGRLDLAEAAQEREAALLRQGNQLWGQMQGLKERIQQSQELLRQIQQRRQEVQAKAAEAQAAQ
AKSQTQQNWETKGWNQPSNYNSYSAFDPLEEQFRRWETDDELEQLKRNM
>gnl|CDD|275170 TIGR04377, 3D-35/4-trihydroxycyclohexane-12-dione_hydrolase, 3,5/4-trihydroxycyclohexa-1,2-dione hydrolase. Members of this protein family, 3,5/4-trihydroxycyclohexa-1,2-dione hydrolase (iolD), represent one of eight enzymes in a pathway converting myo-inositol to acetyl-CoA. IolD hydrolyzes the cyclic molecule 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione to yield 5-deoxy-D-glucuronic acid. TPP is a cofactor [Energy metabolism, Sugars]
RLTMAQALVRFLAAQYVERDGEEVPFFAGVFAIFGHGNVAGLGEALEEDPDDLPTYRGRNEQGMAHAAIA
YAKQKNRRRIMACTSSIGPGATNMVTAAALATVNRLPVLLLPGDTFATRQPDPVLQQLEDFSDLTVSVND
AFRPVSRYFDRITRPEQLMTALPNAMRVLTDPAETGAVTLALPQDVQAEAYDYPESFFAKRVHRIRRPEP
DPAELERAVAAIRAAKKPLIVAGGGVHYSEAGEALAAFAEKHGIPVAETQAGKGALPWDHPLNLGAIGVT
GTLAANALAAEADLVIAVGTRLQDFTTASKTLFQNPDVRFVNINVARFDAYKHDALPLVADARAGLEALS
EALGGYRADSAWAAEAAAAKAAWDAEVDRLYAAEYTAGGLPTQAEVIGAVNRAAGPDDVVVCAAGSLPGD
LHKLWRTRDPGGYHMEYGYSCMGYEIAGGLGVKLAEPDREVYVMVGDGSYLMLNSELATSVQEGKKIIVV
LLDNRGFGCINNLQMSTGGASFNTELRYEDTGRLDGGLLPVDFAAHAAALGAKTYKVTTIAELEAALARA
KAADRTTLIVIDTDPKTMTEGYGSWWDVGVAEVSERESVRKAREEYEEAKKAQRK
>gnl|CDD|275171 TIGR04378, Myo-inositol_catabolism_IolB_domain_protein, 5-deoxy-glucuronate isomerase. Members of this protein family, 5-deoxy-glucuronate isomerase (iolB), represent one of eight enzymes in a pathway converting myo-inositol to acetyl-CoA [Energy metabolism, Sugars]
VEITPESAGWTYVGFRVHHLSKGESLTEATGDQEVCLVPLSGKATVKADGGRWENIGGRESVFDGIPDSV
YLPNGTEFEITAESDARIALCAAPADKDLPPRLIPPEEVGVELRGGGNASRQVNNILPPDFPADRLLVVE
VYTPGGNWSSYPPHKHDEDSEPEEAYLEETYYHEIDPPQGFAFQRVYTDDRSLDETMMVRDGDVVLVPRG
YHPVVAPPGYDLYYLNVMAGPAREWKFTDDPDHEWIR
>gnl|CDD|275172 TIGR04379, myo-inositol_catabolism_protein, myo-inosose-2 dehydratase. Members of this family include the enzyme myo-inosose-2 dehydratase, product of the gene iolE, as found in inositol utilization cassettes in many species [Energy metabolism, Sugars]
KVKLGIAPIAWTNDDLPELGGDTTLEQCLSEMALAGFTGTELGNKFPRDPAVLRAALEERGLELVSGWYS
GLLLTRSVEEEIEAFRPHLEFLKAMGAKVIVVCETGGSIQGDPDTPLSDRPVLTDEEWERLGEGLNRLGE
IAAEQGMKLAYHHHMGTVVETEEEIDRLMAMTDPELVGLLYDTGHATFAGGDPLAVLEKHGDRIVHVHLK
DVRPEVLERVRNEDLSFLDAVLKGVFTVPGDGCIDFAPIFAALAARDYEGWIVVEAEQDPAKAHPLEYAK
KAYKYLSALA
>gnl|CDD|275173 TIGR04380, hypothetical_protein_HOLDEFILI_04020, inositol 2-dehydrogenase. All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se [Energy metabolism, Sugars]
KLKVGIIGAGRIGKVHAENLATHVPGARLKAIVDPFADAAAELAEKLGIEPVTQDPEAALADPEIDAVLI
ASPTDTHADLIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAG
KIGKPEILRITSRDPAPPPVAYVKVSGGLFLDMTIHDFDMARFLLGSEVEEVYAQGSVLVDPAIGEAGDV
DTAVITLKFENGAIAVIDNSRRAAYGYDQRVEVFGSKGMLRAENDTESTVILYDAEGVRGDKPLNFFLER
YRDAYRAEIQAFVDAILEGRPPPVTGEDGLKALLLALAAKRSLEEGRPVK
>gnl|CDD|275174 TIGR04381, transcriptional_regulatory_protein_TyrR, TyrR family helix-turn-helix domain. This model describes the C-terminal DNA-binding helix-turn-helix domain of several regulators of aromatic amino acid metabolism. Examples include TyrR in Escherichia coli and PhhR in Pseudomonas putida. Most members of this family have a sigma-54 interaction domain [Regulatory functions, DNA interactions]
SLDEIMKRFEASLLRRLYASYPSTRQLAKRLGVSHTAIANKLREYGIGK
>gnl|CDD|275175 TIGR04382, myo-inositol_catabolism_protein, 5-dehydro-2-deoxygluconokinase. All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863 [Energy metabolism, Sugars]
KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYL
RREGVDTSHVVTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQ
EPSREAVLKALEYARAAGVRVVLDIDYRPYLWKSPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEA
AARALLDAGVEILVVKRGPEGSLVYTGDGEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALR
YGNACGAIVVSRHSCSPAMPTLEELEAFL
>gnl|CDD|275176 TIGR04383, hypothetical_protein_HMPREF1015_01194, processed acidic surface protein. Members of this family are acidic surface proteins with an N-terminal signal peptide and a variant C-terminal sortase recognition sequence, LPXTA rather than LPXTG. The N-terminal region past the signal peptide is repeated a second or third time in many members of this family. Members occur in Firmicutes, encoded next to a dedicated sortase related to SrtC that assembles pilins, suggesting that this protein serves a structural rather than enzymatic role. Processing by the neighboring sortase may result in polymerization as well as surface attachment [Cell envelope, Surface structures]
MKRLILVIVAFLFALSLLPTGAFAAPSEEELDQYLQEIGWTKEDLENYLAKYDLSLDDFDSVEELKDFLG
TPITEENLQALLTRYGLTEEELEALLGEFGESLQDYTFIEDLEDAVDFYLYHEDWMQQINDFLSEIGLTE
EEIRRLIEHLLSLNNPNLEEQLEALSERLEAFGDFESASELTKEQIAELLSIWNEMLDLFELQAKFYLVK
DGVKKPVSLETLMSLESTNGADLLVELYNLEGEFLADVLLTAEMFGSDLIIDTGEKLIHVGTLALEMKKT
VKGAKLPKTASHYLENLLAGLLLLLVGLFLYRRVRR
>gnl|CDD|275177 TIGR04384, Putrescine_carbamoyltransferase, putrescine carbamoyltransferase. Members of this family are putrescine carbamoyltransferase (EC 2.1.3.6). There is some overlapping specificity with ornithine carbamoyltransferase (EC 2.1.3.3). The gene regularly is found next to agmatine deiminase and a carbamate kinase, suggesting a conserved catabolic agmatine deiminase pathway [Energy metabolism, Amino acids and amines]
DFIDTNDFTKEEILDIIDLSLKIKEAIKDGYYPPLLKNKSLGMIFEQSSTRTRVSFETAMTQLGGHAQYL
APGQIQLGGHESIEDTARVLSRLVDIIMARVDRHETVVELAKYATVPVINGMSDYNHPTQELGDLFTMIE
HLPAGKKLEDCKVVFVGDATQVCVSLMFICTKMGMDFVHFGPKGYQIPEEWLAIAEANCKVSGGSVTVTD
DVDEAVKGADFIYTDVWYGLYDQELSEEERMAIFYPKYQVNPELMAKAGPHAKFMHCLPASRGEEVTDEV
MDSPQSICFDEAENRLTAIRALLVYFLYPRLKPPDEAVAAKAKAELEAFL
>gnl|CDD|275178 TIGR04385, radical_SAM_superfamily_protein, putative variant cofactor biosynthesis B12-binding domain/radical SAM domain protein 1. Members of this protein family are one of two tandem B12-binding domain/radical SAM domain proteins that occur in a genome context with a pair of homologs to ThiC (phosphomethylpyrimidine synthase, EC 4.1.99.17), an enzyme that performs a complex rearrangement involved in thiamin biosynthesis, and a putative CobT (nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase), an enzyme of cobalamin biosynthesis
RILLIQAISMEGMDIERVYPIGIVTLAGHIQGHGRYEIDIFDMNMARDPYGELREKLLTFQPDAIGISLR
NIDPLGNRTTSLIVPFAVTLRFIRTVLPDAKLMAGGTAFSLFPERLMREFPEIDYGIVGEAEVSFVALLD
SINDPPPMPGLCRREGSRVHVSPPATNFDMGNYVMANRLLLDPALYLGVNKYVESIGVETKRGCCYNCGY
CVYPQLSGKRLRCRPPTAVVDEIELLHKDYGVQRIHFTDSIVNFPHGHLDAICEELLRRKLKIHWSGFFR
EDLLTPENAALYERSGCECFSLSPDGLCQESLDVLDKHLSVAQILKTASLLSQVGITTVYHFLVNVPGET
EKTCEESKQFIDRIYDIHSKKKNLGTIVLNLIRIMPGTKIEKLALAQGVITPETDLLYPTYYNPKPFSTF
RYKLEIYHQCRNIFMWQG
>gnl|CDD|275179 TIGR04386, thiamine_biosynthesis_protein_ThiC, ThiC-like protein 1. Members of this protein family closely resemble ThiC, an enzyme that performs a complex rearrangement during thiamin biosynthesis, but instead occur as one of two adjacent additional paralogs to bona fide ThiC, in a conserved gene neighborhood with a pair of B12 binding domain/radical SAM domain proteins. Members of the ThiC family are non-canonical radical SAM enzymes, using a C-terminal Cys-rich motif to ligand a 4Fe-4S cluster that cleaves S-adenosylmethionine (SAM), but that sequence region does not belong to pfam04055
TQVLKARAGIITEEMEKVALREGVDPEFIREGVAEGRIVIPKNKNRKNFKYCGIGEGLRTKVNALIGTSS
DRDDMEMEARKLRAAEEAGADAFMDLSTGGDIDGMRRQSLASANIAVGSVPVYQAGVEAIEKYGSVVAMT
EEDIFEAIEKQAADGIDFMAIHCALNRSVLERLQKTGRVTDIVSRGGAFLTGWMLHNQKENPLYEQFDRV
LEILKAYDVTLSIGDAIRPGCIADSLDGAQIQGLIVAGELVKRALEAGVQVMVEGPGHVPLNHIETTMQL
QKQLCHNVPYYILGTLATDVAPGYDHITGAIGGAFAGASGADFLCYVTPAEHLGLPTEEDVRMGVIAARI
AAHAADIAKGVKGAWERDLAMARARVALDWDRQIELAIDPEKLRQIRAAKNEPGHHACAACGEGCAADVA
AEYFGI
>gnl|CDD|275180 TIGR04387, hypothetical_protein, major capsid protein, N4-gp56 family. Members of this family are phage major capsid proteins as found in phage N4 (a double-stranded DNA virus) plus many additional lytic phage and integrated prophage regions [Mobile and extrachromosomal element functions, Prophage functions]
TTSTDLSPLVNPFWSKKLLERALPKLVFSKFAQVKPLPKNPGDTIKFRRYVPLPGAPTPLTEGVTPKGEK
LTFTDLTVTLEQYGKFVELTDVAADTHEDPELGEATELLGEQAAQTIDELTRDVLAGATNVIYAGAGTAR
NAVTADDVTYDDIRRAVRKLKDNRAPKITTVLTASVMVGTEPSYVAVIHPDLEPDLRDDPGFIPVEKYGA
ADPIMKGEIGMIEGVRFVETPEVLPWADAGAAGGNADVYPILIVGKDAFGTVPKNGKASTKHKIKGEGTA
DSGDPLGQRGTVGWKMWYAAFILNDAWMVRIETAA
>gnl|CDD|275181 TIGR04388, hypothetical_protein_LinasL1_02240, putative large structural protein. Members of this family are restricted so far to the lineage Leptospira, where they may be the longest protein encoded by the genome. Two or three paralogs are often found. The seed alignment for this model includes sequences with significant length variability, and stops adjacent to an intein feature most full-length members of this family share. Oddly, members closely related in sequence up to the start of the intein (see TIGR01445) usually show very little sequence similarity C-terminal to the end of the intein (see TIGR01443) [Unknown function, General]
LLLFPVSPLFSQPVNVPNFNAPQFQQQNMDQTVSVANQSQSLNNWDAIVGQGLSIIKTNWENAAQQEITA
LVNSVTTSDSYASVQDYQNYVSAYLWSQESNAETAWLTQVDSQLSQARDNFLNSQLGANISASTNSNQQF
NLNSNGNLSQAVQWSNDYQTNLQNGLQTFSDSLTGLQRNYQNQLSQINQTDAQYQANLQQLQQYENAVKQ
QIQSSVSQLQSSLNNTALFYNTNPDGTTNWTSLNQDGRDLQTLINNLVQGLQNGSPLSTLANQMNTYLQT
QETQAQTNAAYWSQQAYPYNLGLSGYSYGQGVQSYGNSALYQYGNSGFSENGLIKAIKEYIDGGSNIQDS
TLINYLYSNYGNSLNGVQILGINSADFRGFSNEDNNYCPDPIGCGHSGGNATYSESGYNAFDFIATGLGA
WGGFLLVTIEFTEDTFWYSINFQVQDLNAYANATTWNGFVSQLNSELHSWNNVTPSITNWEGQVAAYQAQ
YAAWHAQAQTYIDSLQQSYTTGVQDLQSQEQSWLANMGNQFQAQSSFAQASNDLDNLKTQQILDSLSPKI
SQVNLPSSSDVLSRNADAPVPDQSSLNNVLSIFQQSLMGASNLALENQLNNQAIDEKLNAIQGIASSLGS
NAVVDSHGNIVYTTVIEDGHAKLKAGGDATNASDYEANTTDRVVTIAAPATIAIGAAAAGDLFQSWDTGS
VVSQNFTNLGSFNSSYNSTINSLNHQVAALNSLNAKNDSSFQEDAQAKASIASLIQSLAQAVLLGGSFGS
WVKGQIQDKVNSAIATALANTTGMSPDMAAQLVSWFEKQQAAKKAKAKARTEDITSGVVVVASIALSFLA
GPEMLAVGQAALQAVQGYQSGGTEGALVGAASGAISAYAREVGVNGYVSYTKKGGFGGGVSAGSSALNVG
FSFSQHGSTSFNTGGSYGNVSYNPSSGFSGSVNLTFDKVGGGVMVNVGQHTGPSLTYQTDGEASGVGASL
TISGKGNITLSATYRNATVVSATGNTHTPSSFGNLTLNDNFQNDFNQNLAMENADENLQAGQAELEMGRE
KIAETGNEHQREALNNENASAQDQHDVLATLAKANEFLNDPSSASTWLGRTAQDVVGSFLGSTGLGASDS
NGFIDKNGKYVQRT
>gnl|CDD|275182 TIGR04389, putative_lipoprotein, lipoprotein, Leptospiral tandem type. Members of this family are lipoproteins restricted (so far) to the genus Leptospira, sometimes with several paralogs clustered with each other, such as four in a row (out of six) in Leptospira interrogans str. UI 13372. The tandem set may be co-clustered with a putative structural protein that is usually the longest encoded by the leptospiral genome (and that often is an intein-containing protein) [Cell envelope, Other]
KKIKIVIVITIFLISLTGCKKSPEELAKEEDVQKRKLVSENINSVYALGGNGLAFLVDPENVKKFKDACF
DFKPKEGKASVKFYQHPEIYNLEVKTKNELEYVLIYQGKEADLKLELEGDLPVKEGTMDVLTAKVNLVIP
GDSKSSGEIGRVDLAYGSDSSADSRHGRFKTLEECEAQITRDEELGETLRKQKSTCEGPGC
>gnl|CDD|275183 TIGR04390, hypothetical_protein, outer membrane protein, YaiO family. Members of this family share a domain of bacterial outer membrane beta barrel, up to the protein C-terminal residue (usually Phe or Trp). The member YaiO was shown experimentally to be localized to the outer membrane [Unknown function, General]
WRIELSYDYEDLSGGYGDWRYQSLRLYYRQTPLGTLIGRLNYSRRFGTNGTQLELGLYPRLSPGLYAYVS
VGASPDAPFLPKYRAGAELYRKLPKSFELSLGARYLRYSDGTVTILTLGVGYYFGNWILSARTRLTPSDP
GGSWSGALSLRGYYGEGADYWGLRLGYGFGPEAYQALSAPELVRFRSQFASLRWRHWLTKRLGLRAGLGY
YRPGDSYNRLGFGLGLFKRF
>gnl|CDD|275184 TIGR04391, hypothetical_protein, CcmD family protein. Members of this protein family are small (typically less than 50 amino acids in length), with the first half highly hydrophobic like transmembrane alpha helices and containing a nearly invariant tyrosine residue. Members from the Desulfovibrionales appear in the position of ccmD of system I c-type cytochrome biogenesis operons (see pfam04995). This family and pfam04995 appear very similar in sequence properties, but the very low level of actual sequence identify makes it unclear that the similarity reflects homology per se
TYLFAAYAIIWLGIFGYVLFLGRRQKKLEKELEQLE
>gnl|CDD|275185 TIGR04392, hypothetical_protein_Met49242DRAFT_3479, hydroxylamine oxidation protein HaoB. Members of this family occur as the HaoB (hydroxylamine oxidation B) protein encoded next to the homotrimeric HaoA, hydroxylamine oxidoreductase, a protein with eight heme groups. It appears all species with this enzyme are nitrifying bacteria
SLGVPLAAAGIALLSYVWFNPGPAPYTYTLAELREGSAEEFPNLGLGAFPGQQIRRYELTAEETDQPLAV
ARYADRDNGRQVALLWPNEVTEPVLTADGKRYELTALAEAIRRHAPEDALVLAWWDTSRRLHLLAGRETW
LDSPGAQPLLIPAWWKQAGAIRLLEKVRASPEEPELFGRFADALTADAAAGLAILRELAGGRPAYLAVHV
DDLYKLGALAPDRFGFEYKDFPGGGDLHGVIARVKQWMREQGYAGYLVQQLGDATIRAWFLTDKKDKDTL
LARLLPFTTSLPLLLPGVKLVYQSGGYWVYRL
>gnl|CDD|275186 TIGR04393, hypothetical_protein, T5SS/PEP-CTERM-associated repeat. This model describes a repeat about 50 amino acids in length, appearing sometimes more than ten times in tandem in a single protein. Most proteins with this repeat have a C-terminal autotransporter domain (TIGR01414, pfam03797) and/or an N-terminal type V secretion system signal peptide (pfam13018), while others instead have a C-terminal PEP-CTERM domain (TIGR02595)
DGYIGANAGSTGTVTVTGAGSTWTNSGDLYVGSSGTGTLTISNGGTVSS
>gnl|CDD|275187 TIGR04394, putative_formate_C-acetyltransferase, choline trimethylamine-lyase. Members of this family, homologs to pyruvate formate-lyases and benzylsuccinate synthases, are glycine radical enzymes that appear to act as choline TMA-lyase, that is, to perform a C-N bond cleavage turning choline into trimethylamine (TMA) plus acetaldehyde. The gene symbol is cutC, for choline utilization. The activase, CutD, is a radical SAM enzyme [Energy metabolism, Amino acids and amines]
PTERLVRLKENYLKQVPSITIYRARAITEIAKENPGMPKILLRAKAFRKCCETAPLVIQDDELIVGAPCG
APRAGAFSPDIAWRWLRDELDTIGTRPQDPFYISEEDKKIMREEIFPFWEGKSLDEYCEDQYREAGVWEL
SGESFVSDCSYHAVNGGGDSNPGYDVILMKKGMLDIQAEAKEHLAELSYENPEDIDKIYFYKSVIDTTEG
VMIYAKRLSEYAAELAAKEQDPKRKAELEKIAEVNARVPAHKPRTFWEAIQSVWTVESLLVVEENQTGMS
IGRVDQYMYPFYKADIEAGRMTEYEAFELAGCMLIKMSEMMWLTSEGGSKFFAGYQPFVNMCVGGVTREG
GDATNDLTYLLMDAVRHVKVYQPSLACRIHNKSPQKYLKKIVDVVRAGMGFPACHFDDAHIKMMLAKGVS
IEDARDYCLMGCVEPQKSGRLYQWTSTAYTQWPICIELVLNHGVPLWYGKQVCPDTGDLSQFDTYEKFDA
AVKEQIKYITKWSAVATVISQRVHRDLAPKPLMSLMYEGCMEKGKDVSAGGAMYNFGPGVVWSGLATYAD
SMAAIKKLVYDDKKYTLEQLNEALKANFEGYEQIRADCLDAPKYGNDDDYADLIAADLVNFTEREHRKYK
TLYSHLSHGTLSISNNTPFGQLTGASANGRLAWTPLSDGISPTQGADFKGPTAIIKSVSKMANDSMNIGM
VHNFKLMSGLLDTPEGENGLITLLRTASILGNGEMQFNYLDNETLLDAQQHPEKYRDLVVRVAGYSAFFV
ELCKDVQDEIISRTMLEHF
>gnl|CDD|275188 TIGR04395, putative_pyruvate_formate-lyase_activating_enzyme, choline TMA-lyase-activating enzyme. Members of this family are CutD, a radical enzyme that serves as an activase for choline TMA-lyase, CutC. CutC is a glycyl radical enzyme related to pyruvate formate-lyase, and this enzyme, CutD, is related to pyruvate formate-lyase activase [Energy metabolism, Amino acids and amines]
IERKARIFNIQKYNMYDGPGVRTLVFFKGCPLRCKWCSNPEGQERKFQVLFKKDICVDCGACVAVCPVGI
HKMLAEGGKHVIDRSIDCIGCRKCEEACPKHALAIMGEDKTISELLEIIEEDRPFYEMSGGGVTLGGGEV
LAQPEAAANLLMACKQRGIHTAIETCGYAKPEVILKVAEFVDLFLFDIKHMDSERHYELTGVRNELILSN
LQELLENGYNVKIRMPLLKGVNDGEEEIDQVIRFLKPYKYYKNFKGVDLLPYHKMGVNKYAQLDMDYPIE
GDPSLDDADLERIESWIKGYDFPVTVIRH
>gnl|CDD|275189 TIGR04396, hypothetical_protein, surface carbohydrate biosynthesis protein. This model describes an uncharacterized homology region found broadly in proteins of surface carbohydrate biosynthesis regions. This family shows distant homology to regions of family TIGR04326, of spore coat polysaccharide biosynthesis protein SpsB from Bacillus subtilis, etc [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
TIYIPVEHKVRELDAKLLLAYYAAKRGYRVVLGPLYLIRSLLPYLPPGIYLLKHLRPGNKELFERLKKLG
HKVGVLDEEGLVYPNPDLYADFRIGAGVLDLVDAFFAWGEEQADAIEKAYPLKADKIVITGNPRFDLLRP
KYREFYSNEARALKKKYGDFILINTNFTQANPFDGGLGFLERLKKGGKGEDEKFFEKLIEYIRKIFESFI
DLLKELSKAFPDVNIVLRPHPSENLEPYRKLFSGYSNVHVIHEGNVIPWILASDLLIHNGCTTAIEAYML
GKPVISYRPINSERYESELPNKVSYECRSEEELIELIKKIL
>gnl|CDD|275190 TIGR04397, preprotein_translocase_subunit_SecA, accessory Sec system translocase SecA2, Bacillus type. Members of this family always occur in genomes with the preprotein translocase SecA (TIGR00963) and closely resemble it, hence the designation SecA2. However, this appears to mark a different type of accessory Sec system SecA2 (TIGR03714) from the serine-rich glycoprotein type found in Staphylococcus and Streptococcus, and the actinobacterial SecA2 (TIGR04221). This type occurs in species including Bacillus anthracis, Geobacillus thermoglucosidasius, Solibacillus silvestris, etc [Protein fate, Protein and peptide secretion and trafficking]
VKKLKGDSSARELKRYEKLVAQINELEPKMEKLSDEELRQKTITFKERLEDGKTVDDIKVEAFAVVREAS
KRVLGMRHYDVQLIGGLVLLEGNIAEMPTGEGKTLVASLPSYLRALEGKGVHVITVNDYLARRDRELIGQ
IHEFLGLTVGLNVPMMEASEKKEAYQADITYGVGTEFGFDYLRDNMVYSLSDKVQRPYHFAIIDEIDSVL
IDEAKTPLIIAGKTGSSSELHYICARIIKSFEETEDYEYDPETKAASLTEEGITKIERAFGIDNLYDLEH
QTLYHYLIQALRAHVLFKRDVDYIVKDGKIELVDMFTGRIMEGRSLSDGLHQAIEAKEGLEITEENKTQA
SITIQNYFRMYPKLSGMTGTAKTEEKEFRETYGMDVVQIPTNRPRIRVDWPDRVFMTYEAKYKAVAKEVK
KRHETGQPILIGTTSILQSETVAKYLDKEKIPYQLLNAKTVEQEADLIALAGQKGQVTIATNMAGRGTDI
LLGEGVHELGGLHVIGTERHESRRIDNQLRGRSGRQGDPGSSQFIISLEDDMFRRYAAEELEKWKKKLKT
DETGEILNKDVHEFVDKVQRIIEGSHYSAREYNLKLDDVINEQRNVIYQLRDKLLEEEDAISEVLKMIRS
AVEQIIDQYCPEEVLPEEWDLERLTEELNRIFPVTFVTFDKRIADKEELKDLVKDTYEQYIAALEKLPEN
EEIQMRLKHVMLSVIDAHWTRHLDAMNLLKEGIGLRSYQQEDPMRLYQKEGLELFEAMYQNIEREICTEL
ARLL
>gnl|CDD|275191 TIGR04398, hypothetical_protein, SLAP domain. This domain is duplicated in SlaP (S-layer assembly protein), a partner of SecA2 in the Bacillus anthracis type of accessory Sec system (see TIGR04397). The domain is found, either once or twice, in additional Firmicutes species
ELSLEPSWEKNLSDEQKEVLEFLLKELPPLKEGEVSFSGISIKLNEDGKLVVTVFIRNGLEKPINLEELP
LTLLDANGEVVARGTFDLEDGEIPPNSARPWTFIFPKEDLKKEEIDLSDWKLAFE
>gnl|CDD|275192 TIGR04399, hypothetical_protein_HMPREF9372_1019, accessory Sec system S-layer assembly protein. Members of this family, designated S-layer assembly protein (SlaP), occur next to a Bacillus anthracis-type accessory Sec system SecA2. . Members have two tandem copies of a duplicated domain (TIGR04398) that may also occur in other contexts. SlaP is found both free in the cytoplasm and membrane-associated. SecA2 and SlaP appear to work together to modify Sec for efficient S-layer secretion [Protein fate, Protein and peptide secretion and trafficking]
FFKKKKKKGKDSAVSASELLGNTEDESGDEEVKTTLSFHPSWNVSQEQKYVFQFLHNELPPLKPNQISLS
GIELKKAEGGYLVTAFIRSSLDKPIQFGEITLLLLDKDGELIARKEFDLSELGEIPANSARPWVFVFEKE
DILTEELPQEGWKLAFELQGKHQLDLDESWEKQLPEEQKEKLQELVESLPPPKPGEVNFMGLQAKQNENG
DLHVTLLIRNGSNKNINLEQLPLEVEDASGEVVARGAFKLDDLEVKANTSKPWTFIFPKELVTKEEPDLS
RWKVYIPQ
>gnl|CDD|275193 TIGR04400, hypothetical_protein_Lbro5_07294, Arg-Lys translocation region protein phosphatase. The Sec-independent protein export system TAT, or twin-arginine translocation, is unusual in Leptospira, with Lys replacing Arg in the second position of the twin-Arg motif. This protein, restricted to Leptospira and showing distant homology to the phosphoserine phosphatases RsbU and SpoIIE, is always encoded immediately downstream of the tatC gene and appears to be part of the variant TAT system. It lacks a TAT signal itself, and so is more likely to be part of the Sec-independent translocation machinery than to be a substrate. The suggested symbol is rktP, for RK-Translocation Phosphatase [Protein fate, Protein and peptide secretion and trafficking]
IHSKLKLSFAIFTIAFLFFLLFTIIDDAILKGGLALAKRILLSIRLALAFSFSSAIAGLTFFFLHLIYKS
LRSLTHLAQDWGNDVYEETGAEERDDEIGELARAFRIAFFQKKEKEADISHESLGEIEKEIADKIEAAFH
RIQLHKILNLDISIFPRMSEDSNCDYGNVIPSADGCLGILAGFPNNGFLESAFKARIEGIFSLANETSEI
PGEDLLFKIDKALRKMPIPFLNLSLFYIETKTGEIGFIHCQELPAFIHKNNEFISLEKNKARFFDFKAAD
LDIHKTVLKQGEFIVLISDRLHEAAGGEAKEFLKKFQNVLAGKEFQNSRDLILDCGRTLEAEAGKKTLEK
AAILAIGR
>gnl|CDD|275194 TIGR04401, conserved_hypothetical_protein, twin-arginine translocation signal/Cys-rich four helix bundle protein. Members of this family average about 150 amino acids in length, beginning with a twin-arginine translocation signal sequence, then a His-rich spacer region, followed by a ~105-residue region in which thirteen positions are nearly invariant Cys residues. CDD (Conserved Domain Database) assigns members of this family to clan cl13994, the DUF326 superfamily, based on homology to PA2107 from Pseudomonas aeruginosa. PA2107 is a cysteine-rich four helical bundle protein, with solved structure PDB:3KAW
MNRREFITAAGAAAALAAAASAAAAAGHHHAHDHGHHHPAAAAKYAALLEAAAHCVSTGEACLAHCLRLL
SMGDTSMAACAKAVNQMLALCAALQSLAAQNSPLTPALAKVCAEACEACAKECKKHADHHAECKACGDSC
KACAEECKKV
>gnl|CDD|275195 TIGR04402, hypothetical_protein_LEP1GSC019_1649, mobilome CxxCx(11)CxxC protein. Members of this family share twin CxxC motifs near the C-terminus, suggesting a DNA- or RNA-binding activity. The spacing between CxxC motifs is variable, from 11 to 16 amino acids. Members in general occur on plasmids or near other markers of lateral gene transfer (transposases, integrases, endonucleases, etc)
SEDDIRAELKQIEFDALGAHEIFKRRLASLNWLRNTRTFLGIVVPIIVGFALLTFAKLTRFKTWALTISG
VASVFQLLLSVWSLISRWDDKYEKSIQSMRDNTEIENEARSIGSRNKDEADLEWFYEYVSARDERDEARD
SSLEVSQKELAYRYRAKLSELGKPCHTCNESPATLKKGKKCQLCGN
>gnl|CDD|275196 TIGR04403, synthesis_of_sporulation_killing_factor_A, sporulation killing factor system radical SAM maturase. Members of this family are a radical SAM enzyme of post-translational modification of ribosomally translated peptides. In Bacillus subtilis, the enzyme SkfB creates a sactipeptide (sulfur-to-alpha-carbon) crosslink of Cys-4 to Met-12 of the mature form of sporulation killing factor (SkfA). In Paenibacillus larvae subsp. larvae B-3650, the Met is replaced by Leu, so the modification must be different. SkfB has 2 4Fe-4S clusters, one in its radical SAM domain (pfam04055) and one in a region that somewhat resembles the SPASM domain (TIGR04085)
TETEQQDLPELAIHLQPHGAVMIDRKSMYYFRLSGRGAQLAFLLSKNKSIRKTARIWEITKKEEITADQL
LEELSAHPFTEAWTNGLLEQPLPVYGSLRSYLPISCTLQLTNACNLSCSFCYASSGKPYPEELATDQWIQ
VMQKLAAVGVADVTLTGGEAKLIKGFKEIVTVASSLFTNVNVFSNGLNWRDEEVELLSHLGNVSVQISID
GTPETHNLLRGRKGAFEESMNTIKRLAEANIPVIVAMTINEKNADTVKDVVKDCANAGARIFRAGKTLSV
GRATEGFKALTDEFESCVQQQLKEARRKWGDQLNIIDWEHEESSFTTDFCTPGYLAWYIRADGYVTPCQL
EDEPLGHILRDSIGDIGSPERLLRLKCEAKNCKCIGKVELSEPDLPFIYEGK
>gnl|CDD|275197 TIGR04404, hypothetical_protein_PlarlB_23158, sporulation killing factor. Members of this family are ribosomally synthesized and post-translationally modified peptide natural products, modified by sulfur-to-alpha-carbon cross-link introduced by a radical SAM enzyme, SkfB (TIGR04403)
RNQKEWESVSKKNLSKPGGTSIVKAAGCMGCWASKSIAMTRVCALPHPAMRAI
>gnl|CDD|275198 TIGR04405, hypothetical_protein, sporulation killing factor system integral membrane protein. Members of this family, SkfF, occur only in cassettes of the sporulation killing factor system. This protein has multiple membrane-spanning domains and is encoded next to a protein with ATP-binding cassette (ABC) homology (SkfE), suggesting ABC transporter permease activity for this protein
MNNIISLLWLHSYRRFTSVTQEKKMPFLILLLFFAAIGFQISIVSGDGPWNASIAGWIIVGIFILYTLFG
LFSNRLPSQMEDILWLYGVPLSFYKVVYSVFIPKVIWRAVLWIGSAIVADILLLFLNQGFYHLLGSSMSS
FLLLVTLEFWCLVVSCARTNKMYKRVWAGLFLLMLGIFSMGITYLFILRESSVYIEPVAPFGYQVGLLTG
TFSLAGVLFIGGIAALSFMLIYVSSLKLEMKESLVKEASFWEEFKDFQSLVSSIRGKDRPTWWGLRRLRG
IWSFLWLEFLIIKKYLKFHLFQTVLLVGLMYVVLQWAPHWFGLIFGLILIAVLLSSYYSGIVRHAQTGDL
FLFPGALIKKIYTLELISTLWLYILYLVSLIWSIASNGIYWSIYGTGPYIWFLTIRLFAFTESSRVTQYY
LSLFKYYLSILAAIIVSGACLNFIHLVTYAWPTSIWIVSVGSRRFIECYRKR
>gnl|CDD|275199 TIGR04406, LPS_export_lptB, LPS export ABC transporter ATP-binding protein. Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPM
HERARLGIGYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGE
RRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISD
GKVLAEGTPAEIVANEKVRRVYLGEQFRL
>gnl|CDD|275200 TIGR04407, LptF_YjgP, LPS export ABC transporter permease LptF. Members of this family are LptF, one of homologous, two tandem-encoded permease genes of an export ATP transporter for lipopolysaccharide (LPS) assembly in most Gram-negative bacteria. The other permease subunit is LptG (TIGR04408) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
IDRYLFRELLKSFLAVLLVLLLIFLSNQLIRLLGDAADGGIPADVVLSLLGLSLPSFLPLILPLALFLAV
LLTLGRLYRDSEMVVLFASGISLGRLLRPVLVFALPVALLVALLSLWLAPWANQQFKQLLAEAKARALLS
LLQPGRFQELGNGGRVLYVEGIDDDGGVLRNVFIADRRDPGRPSVITARRGTIETDPDGDRFLVLENGRR
YEGDPGTADYRITEFDRYGIRLGEQTPARSPNRRPKAMPTAELLASDNPEARAELHWRISLPLAVLLLAL
LAVPLSRVNPRQGRFAKLLPALLLYLIYFNLLSLGRSWVEDGKIPPWLGLWLVHLVFLLLAILLLA
>gnl|CDD|275201 TIGR04408, LptG_lptG, LPS export ABC transporter permease LptG. Members of this family are LptG, one of homologous, two tandem-encoded permease genes of an export ATP transporter for lipopolysaccharide (LPS) assembly in most Gram-negative bacteria. The other permease subunit is LptF (TIGR04407) [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
ILDRYIARTVLSATLLVLLVLLGLFLIIDFIEELRNVGRGGYSVGEALLYVLLSIPRIIYEFLPLAVLLG
ALLGLGSLARNSELVVMRAAGVSRLRILAPVLKVALLLSLLTFAIGEWVAPRTEQQAQAIRATALGGGSA
LSSKSGLWLRDGNNFINIRAVLPDGTLRGVTIYRFDDEGRLTSRIDAASAIYQGGSWLLRDVVETRFDED
GVETESFPELPWESSLTPEQLSVVLVDPEELSISELYDYIRYLEENGQDATRYELAFWSKISQPLALLVM
VLLALPFIFGPLRSGGMGARIFIGILLGFAFYVLNRIFGPLGLVGGLPPILAAWLPSLLFLLLGIWLLRR
V
>gnl|CDD|275202 TIGR04409, LptC_YrbK, LPS export ABC transporter periplasmic protein LptC. Members of this family are LptC, a periplasmic protein tethered to the inner membrane in the lipopolysaccharide (LPS)exporter transenvelope complex (Lpt), which is responsible for conducting LPS to the outer leaflet of the outer membrane in most Gram-negative bacteria. LptC is homologous to LptA, another member of the transenvelope complex. Genes lptC and lptA are often adjacent [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
RLLPLLLLLILALLTYWLVRNQDPDRPAVEPLDNHEPDYIAENFSTTQYDEDGKLQYRLTADKAEHYPDD
GTTEFTNPVLILFDEDGKPTWTITADRAKLNKDGKELYLYGNVRVTRLAGDGPPQTLTTENLTVDLDTQD
ATSDQPVTITGPGFTITGVGMKANLKTGTAELLSQVRGTY
>gnl|CDD|275203 TIGR04410, hypothetical_protein_LEP1GSC017_3433, type II secretion system-associated lipoprotein. Members of this family occur only in spirochetes (Leptospira, Leptonema, Turneriella), as part of a type II secretion system (T2SS) cassette. Properly extended gene models always include an N-terminal signal sequence ending with a Cys residue, suggesting this small protein (about 100 amino acids) is a lipoprotein
IRFVVFLLALVFSFGCGSRLIKKERLREINEYYQGKIYALKEDIKVSQTETFKKGTLVKIYVESTPSLVK
VKAYPADQKRESAIGKLILYQVNDDFKKKTIELEDLRKIIANELTEV
>gnl|CDD|275204 TIGR04411, hypothetical_protein, type II secretion system protein N, Leptospira/Geobacter-type. Members of this family are the N (or GspN) protein of type II secretion systems (T2SS) as found in Leptospira, Geobacter, Myxococcus, and several other genera. Sequence similarity to GspN as found in, say, Gammaproteobacteria (see pfam01203) is extremely remote [Protein fate, Protein and peptide secretion and trafficking]
RWKQRLGYGAFGVVAFFLFLLLLFPYDELRRRLLREAAQPGLAVRAGSLGPALPLGVSAEGVTLSDEGGV
ALTADEATLRLSLFPLLSGKPRVDFDASAYGGEVDGSVLLLGGGKRGNLHLAGLDLEPIPLLTKATGADV
AGTLNGDLDLTLPKGREGGGHGELSLSVSGLVLRGGKIPGMPLPDIALGELRGRIRLKKGKATVERLQLD
GPDAYLRLTGTIRLSPPLEFSRLNLKVCLRPTPEFAERQGLVILLLALYGKSPGAYCLPLRGTLGKPQF
>gnl|CDD|275205 TIGR04412, type_II_secretion_system_protein_M, type II secretion system protein M, XcpZ-type. Members of this family are a variant form of the type II secretion system (T2SS) protein M, GspM, as found in several species of Pseudomonas. Members, including XcpZ, are short relatives to most members of pfam04612 (as of release 26.0)
EWWQRRRLLLAGWVLVALLLLYLVAREGWAGWQEARQWQALAVSAAALPAVQPLSAERLRQSAQASRVLL
TGVEAREGGWQVQGQIADAQDLNRWLQAVAGEGWRVSRWSLQRADAGLVFELQTQR
>gnl|CDD|275206 TIGR04413, hypothetical_protein_LEP1GSC082_4029, CRISPR type MYXAN-associated protein Cmx8. Members of this family occur only in CRISPR/cas loci of the MYXAN type, but are present in a minority of such systems. This protein appears to replace the MYXAN system Cas8a1/Csx13 protein (TIGR03485/TIGR03486), compared to which it shows similar length and composition but only about 12 percent sequence identity
EYQLAELPSSQHKAGLAGLVLIIEWLEKQEIAKELCKLTQLDDAGVTVTLTRKGLQALFDELYDASLEEV
ESKSKWKGAEPIREEEKEEKDKKGKKKTKKLYIYPVVVPKGSFLPSYDKSADNGLWIKLWRDMLWSILRG
VPATRNPFKARASGNPCKDVIKAWKQLIQKEEKTVDLSSTLFLGAQANNAENIPFKDRARENFLLHFWPF
AAQLYVPRTIDKEGKRNKGDFNGYAIAIPDIAKLKSFCEEFPKLLQNRSIEKKGYRPRESIIDLPEESAL
DFLKRLHDRLSKTIGEQSYSDSVLGVDVIHTEKKGNNVKLLGASRIEPEVDMLNKYAAIKKKYWNPLFRK
QRLLNLLNGKPWYVGFDSLLCTYPYEQFETGEDYFKHDARKKFEEEELKFTGETEMSEDGNEPKTIELLV
FQIVRSYVLSKLESKYELKWDKGKKVLGSPKLEKDYNEKKEKIAKDAFLAVRSRSEKEDFINYFTSTLCS
VPQHLKEEDYVKLAEALYEDTGWEKIRALTLLALSANS
>gnl|CDD|275207 TIGR04414, glycosyltransferase_tibC, autotransporter strand-loop-strand O-heptosyltransferase. Both Aah (autotransporter adhesin heptosyltransferase) and TibC (tib is enterotoxigenic invasion locus B) are protein O-heptosyltransferases that act on multiple sites from repeat regions of proteins exported by autotransporters. Aah glycosylates AIDA, or autotransporter adhesin involved in diffuse adherence, TibC acts on TibA, but TibC can replace Aah [Protein fate, Protein modification and repair]
AEIPTQEGPEGIRYDFNDGCRVLLPDGKWRVRLSDLDTGNILFDCELDAGWVSSTKRYFVRFRIEVWKDE
TLVFSHDYDLRGQPVLIQFPVGTLGDILGWFPYAARFQEKHGCRLTCAMAEPLIPLLKDAYPDIEFVTPE
EVKKERYYATYRVGLFFGDDANVHQPTDFRLVGLHRTAAYILGVDPTEEPPRIALSDDSRPIAEPYVCIA
VQSSSQCKYWNNPTGWREVVAFLKAAGYRVICIDQKAVHGQGLVWNHIPYGAEDQTGDRPLQERARWLRH
AAFFIGLSSGLSWLAWAVGTPVVLISGFTHPTNEFYTPYRVINWHACNSCWNDIRVRFDHTDFLWCPRHK
GTPRQFECTRLITGEQVIRAIKRI
>gnl|CDD|275208 TIGR04415, hypothetical_protein_GfraN1_13426, autotransporter passenger strand-loop-strand repeat. This model describes two tandem copies of a strand-loop-strand repeat that occurs often in type V secretion system (T5SS). These repeats usually occur in the passenger domain of the classical monomeric autotransporter. Proteins with this repeat often are encoded next to a member of family TIGR04414, the Aah/TibC family O-heptosyltransferase, and may be glycosylated in regions with this repeat
SASGTTVNSGGTQTVSSGGTATGTTVNSGGTQTVSSGG
>gnl|CDD|275209 TIGR04416, hypothetical_protein, group II intron reverse transcriptase/maturase. Members of this protein family are multifunctional proteins encoded in most examples of bacterial group II introns. These group II introns are mobile selfish genetic elements, often with multiple highly identical copies per genome. Member proteins have an N-terminal reverse transcriptase (RNA-directed DNA polymerase) domain (pfam00078) followed by an RNA-binding maturase domain (pfam08388). Some members of this family may have an additional C-terminal DNA endonuclease domain that this model does not cover. A region of the group II intron ribozyme structure should be detectable nearby on the genome by Rfam model RF00029 [Mobile and extrachromosomal element functions, Other]
KENLLLAYKRVKANKGAAGVDGVTIEDFEEYLEENLYKLWNRLKSGSYRPQPVRRVEIPKPNGKQRPLGI
PTVRDRVVQQAVKQVLEPIFEPDFSENSYGFRPGRSAHDAIAKARKRLNRGYRWVVDADIKGFFDNINHD
LLMKAVARRISDKRVLRLIRRWLKAGVMEDGEVQETEEGTPQGGVISPLLANIYLHYLDDEWEKRGYKVR
FVRYADDFVILCRSKEAAERVLEALTKRLEELGLELNPEKTKIVHCKDGGFDFLGFTFRKRKSKNGKGKL
LIKPSKKAVKKFKEKIRELTKRRRGLSLEELIKKLNPILRGWANYFGIANSSRTFSKLDHWIRRRLRRWL
RKKW
>gnl|CDD|275210 TIGR04417, hypothetical_protein_LEP1GSC007_1570, polysaccharide biosynthesis PFTS motif protein. Members of this protein family are found in O-antigen biosynthesis loci in Leptospira, two tandem homologs in a polysaccharide biosynthesis region in the archaeon Methanoregula formicicum, in Rhizobium leguminosarum bv. trifolii WSM2297, etc. Members are more strongly conserved in the C-terminal region, where an invariant sequence PFTS is found [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
LRDEDDIEKVKNEKPELLKEEYQRVQQKVLYLLFNDILPKIDMVFRQYFLGMLASIELNKKLELIWGSIK
SKIVLNLFAEYRNFIIKTGFRVSNLKSRFLWYIKSAIYICYPLFEVCKILMPSLLRFPTYQVGIRIYFDD
IGFSNKPRRFDFLSDNDIISWYNNIWCDEEPVLDPILHTILESKNYAGLKIRNILFNAQPLFSVLSIVKR
FLPAWKYCLLFFLSIVLIFRGLWWLVLLLEIQYKLLLWDCFAQKYLIRHYLITNSSLPYDPIRTIKAEFK
GVKTWFYAYSTNSFDFKKPLGYPDETFTLFAFMQWSEFVVWGRKQKDFIKKPNSIANIRIFGPLWFSDPS
QQIREKLLENDTQRSFNITIFDVQPLKDKALLSVFALSFEYYTPEDLIRFLSDIINLLEDGPEVKIILKR
KRNLSSLSQAHPRYIKFLEKLIKHGRLVSIDPSVSDPSELIAKVDLVISMPFTSPSIIANGLGKKSIYYD
ATGKLECHYYLKHPRFIIHGYDELKSWID
>gnl|CDD|275211 TIGR04418, PriB_gamma, primosomal replication protein PriB. Members of this protein family are primosomal replication protein N (PriB), virtually always encoded between rpsF (ribosomal protein S6) and rpsR (ribosomal protein S18). Note that only this short form, as found primarily in the gamma-Proteobacteria, of the single-stranded DNA binding protein family (see model TIGR00621) may partner with PriA and be involved in priming for re-initiation of replication [DNA metabolism, DNA replication, recombination, and repair]
NRLVLSGTVAETPKLRYTPAGIPHLEFVLEHRSQQEEAGQPRQVECEIQAVASGELAEKLARLTVGSRVR
VTGFLARKSHRNGLQLVLHAQQIEFI
>gnl|CDD|275212 TIGR04419, no_iron_rSAM, HemN-related non-iron pseudo-SAM protein PsgB. Members of this protein family are related to radical SAM enzymes HemN (oxygen-independent coproporphyrinogen III oxidase) and HutW (a putative heme utilization enzyme) but lack the signature CxxxCxxC motif for 4Fe-4S binding. Members occur exclusively in Borrelia, which appears to live without iron, as the only radical SAM enzyme homolog in any Borrelia genome. We designate this enzyme PsgB (Pseudo-SAM, Genus Borrelia)
NFLPLTELSIYIDLSKCFSYVFFNKILGELSYYLEVLGFPKIKTLYIKYEDLGLGNDDSLKSFLTSLSKN
FNFATLDEFTFELHPGEITFSLLTILDDFFVSRISLDVKSFSSKFLKILGIPEISVEKVNIAIKNIRKFD
FDLNIDLTINIPYQEKMHLKSDLVKLISYAPEHICLSEVLVDEENCIIDDFKDVSSNYNEIKAEDLWFYA
LDFLESNGYINYEISNFALKGHESKHNKRYWELKPYLGLGLNAVSLLFCSKNNGLRAVIRKDDNFLGSSN
SSATFELLSDLDFFIYHFITNLGTKQGLDVSILRRRFIYNQEDFYKFINYLLSLSKSVVFSNDILYLDGH
ERFKLDFYLRLIREYFIDNSFKVNFKFL
>gnl|CDD|275213 TIGR04420, Sec_Non_Glob, Sec region non-globular protein. Members of this family occur only in the genus Leptospira, always encoded between genes for the YajC and SecD components of the Sec preprotein translocase. Sequences have an N-terminal signal peptide and a C-terminal transmembrane segment. Between these are regions of non-globular, low-complexity sequence including Lys-rich and Ser/Thr/Asn/Glu-rich regions
MKKILCLLLIFLLSFSLFSQDGEEIDFLDKVSEPKKTTTSKKKETTATKKQTKVVKKKGKKKGKKKKSKK
KSKQNQLQKEEELKKNTNLDANPPDQGKNSGDPNGSNKVTEKTLVDEEKQPAVLEEEEELQKPYWVNEEV
SVEPNNLPGYSADSALPKEDISFREKLGEILKLGKDKKKEEEKKKAAEGKSQGNFSGFFSEYKKAIIILG
IILLFALYRLRAARPRSSRRSPVTINKVRRD
>gnl|CDD|275214 TIGR04421, hypothetical_protein_LEP1GSC041_1958, FemAB family protein. Members of this family are FemA/FemB family proteins from a cassette that some Leptospira have in their O-antigen biosynthesis regions and share with a cassette from gamma proteobacterium IMCC1989 [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
IQKILNFIQSWKFFFHFKNENLELWSLLFLKADYQPVAYSDLALDFQYLYQKEKETSTIDLSFIIKDMGK
PIGIWPLSICESKKTKKLNFYGLTLQSPLLINTELRVLERIANEFYLFLEKLLNILKEKELLISLPFIGK
LFYVIDPWHKAALDFGAKPSINYDLYIDLNLPLEEIRSQFRKSYKPLISKGLELWNTFVLTDRDEEVWEE
YRQLHISAAGRVTRCKETWDVQLKSIENKKAVLVTLRDESDTLVGAGFFMFTKHEARYDTAAYNRNLFDK
PLGHVVQYIAIQEFKKRGISSYIVGRRPYDFDSPQYTEKELSIAKFKSGFTSSLFPRFHFKKRLL
>gnl|CDD|275215 TIGR04422, hypothetical_protein_LEP1GSC007_1569, putative PLP-dependent aminotransferase. Members of this family are PLP-dependent enzymes, probable aminotransferases of the DegT/DnrJ/EryC1/StrS. Members occur in some Leptospira have in their O-antigen biosynthesis regions and in a related cassette in gamma proteobacterium IMCC1989 [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
RSFFLWPDYNPIHSLSRIIYSKKISSIEDMLETFFPSGYPVLCSSGRAAIGLALEFLDLKRNDFLGVFPF
ASHCVLDAVSRYTTPLTGISSKNTKNRIVYHQWGYVQEYNLPANTIEDCVDTLCVPGAKLFPAGGIFEIW
SLPKILGTSSGGVLWCRDEDVANQIRAIRDSRKYSGIIQWYLKLFSYKFPSLLSYWTGVEASCGKFGFLQ
MGEIHYALNNWQKFIDDKLNRIEIALELFPSWLKQTPDRIPSIIPVELTISSEKFSEWGLSSGMRTFEKC
IKEKSELIQVFPLPLHFQIPLKQFKKIVLELEDIK
>gnl|CDD|275216 TIGR04423, predicted_protein, CRISPR type III-associated protein, TIGR04423 family. Members of this protein family occur only in species with CRISPR systems, in the context of type III systems that resemble type III-A (MTUBE) and III-B (the RAMP module). It occurs in several species of Prevotella, Helicobacter, Campylobacter, and Bacteroides
EKYEGYLWMSDEDKPRVFDEEPLIERDLHEGLNPFVAEGYLYDKETQRSISIKYVNGRYIVLEFDLKAAD
FKSEDVTEVEFLANRMKGKRNLKFLQYWEEVEDELCDDFKVLRPTKTVFVGFKK
>gnl|CDD|275217 TIGR04424, Microcin_B17-processing_protein_McbB, McbB family protein. This family includes the partially characterized zinc metalloprotein McbB, part of the maturase system for microcin B17, a thiazole/oxazole-modified microcin (TOMM). Other members of this family belong to very different gene neighborhoods. The Cys residues that act as zinc ligands are conserved in most members, but for rare members are jointly absent
YKINPFIILNLEEDETLVQNEKGIVRITDKKLIDFLKKLDAKKVISFSESELEKFFEESNLDKVLEFLLE
NKLLSKKEEENLYFKKVIVFSDNQNFAELLEQIIQELSVNRFFYSNSNSSLNENLNDRDLIILFLNPYDY
KKAKKIYDLLKEKNKSAISFAYYYNNHFYIDNLYSPEWGNPCHFCFISRLESSLRSEKFRNSRNSWQTLI
DLLYNKETTFNPEIPLNQYDIFFIVGEIIKRIQQLTEDSVSFRYQDDFLSSISLDLNTGKISEDPAIHWE
LCDCLE
>gnl|CDD|275218 TIGR04425, 3-dehydroquinate_synthase, putative sugar phosphate phospholyase (cyclizing). Members of this family tend to be found in O-antigen biosynthesis regions. Members frequently are misidentified as the closely related 3-dehydroquinate synthase, AroB (see family TIGR01357), the phospholyase that converts 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate to 3-dehydroquinate during chorismate biosynthesis. Most bacteria with this enzyme have a true AroB in a chorismate biosynthesis gene cluster [Biosynthesis of cofactors, prosthetic groups, and carriers, Lipoate]
IQSHKGDYTVEFVEDLLDLLAELVAEGTHFIIDKNVAELYKEELDPVLDKPRVLLIEATEENKSLEAVPP
IIEHLVANGAKRNHTLIAIGGGIIQDITCFIASTLYRGVRWIFIPTTLLAQADSCIGSKSSINFGSFKNI
LGTFYPPDQIYICPAFLRTLSERDIRSGIGEILKFHLIAGPEGFDQIAADYDKLFTDREKLLKYIRRSLE
IKKSYIEEDEFDKGIRNLLNYGHTFGHAIESATNYAIPHGIAVTLGMDMANFVSVRRGLLSEEHFNRIHE
VLKKNYPIGFELHPFDLDAIIAALKKDKKNTGDQLTLILPDGEGKLEKVDDVNDEEFRSALNEYLEEL
>gnl|CDD|275219 TIGR04426, hypothetical_protein_HMPREF0975_02898, TDP-4-amino-4,6-dideoxy-D-glucose deaminase. Members of this protein family, including DesII, are radical SAM enzymes that deaminate TDP-4-amino-4,6-dideoxy-D-glucose to TDP-3-keto-4,6-dideoxy-D-glucose. This is the fourth step of the six step pathway in Streptomyces venezuelae for synthesizing D-desosamine, or 3-(dimethylamino)-3,4,6-trideoxyglucose, a precursor for many macrolide antibiotics
PGGDLAAAVDALRTRLETVRGETEDDAETVAEHLVRLANRYGNHPFTPLEQARRRLGLDRAEFARLLELF
HRVPELRTAVERGPAGKYWTNTILPLERRGALDAAVEGKPAFPYSVGLYPGPTCMFRCHFCVRVTGARYE
ASALTPGNAMLASVIDEVPTDNPNAMYLSGGLEPLTNPGLGELASRAAARGFDLTLYTNAFALTEQTLDR
QPGLWDLGAIRTSLYGLSDEEYEATTGKRGAFSRVRANLRRFQRLRAERGSPLRLGLNYIILPGRAGRLL
DLVDFIADLNEASPDRPLDFVTVREDYSGRPDGRLAPSERAELREGLGAFEEYASERTPSLHIDYGYALE
SLRLGVDAELPRIRPETMRPTAHPQVAVQVDLLGDVYLYREAGFPGLEGADRYIAGRVTPDTSLHEVVRN
FVEEGREIAPRPGDEYFLDGFDQVVTARLNQLETDVADGWGDYRGFLR
>gnl|CDD|275220 TIGR04427, hypothetical_protein_HMPREF0975_02897, dTDP-4-dehydro-6-deoxyglucose aminotransferase. Members of this family are pyridoxal phosphate-dependent aminotransferases that convert TDP-4-keto-6-deoxy-D-glucose to the 4-amino sugar form, TDP-4-amino-4,6-dideoxy-D-glucose. In Streptomyces venezuelae, this enzyme is designated DesI, catalyzing the third of six steps in the biosynthesis of TDP-D-desosamine, a component of a number of different macrolide antibiotics made by that organism. Related proteins, scoring below the trusted cutoff, include sugar aminotranferases in O-antigen biosynthesis regions
MKRALDDLAIFGGPAAFLQPLLVGRPNVGDRARFFERLEWALDNEWLTNGGPLVREFETRIADLAGVRHC
VATCNATAALQLLLRAAGVTGEVIMPSMTFAATAHAASWLGLEPVFCDVDPDTGCLDPDRVAAAITPRTG
AIVGVHLWGRPCPVDELAKLAAEHGLRLFFDAAHALGCTADGRPVGSFGDAEVFSFHATKVVNSFEGGAV
VTDDAELAARLRALHNFGFGLDGGVPAGGTNAKMSEASAAMGLTSLDAFAEVVEHNRRNHALYREELRDL
PGVRVLDFDPHERNNYQYVIVEIDEAVTGIHRDLLITVLRAEGVVAQPYFSPGCHQMEPYRTEPPVRLPH
TERLAAQVLALPTGPAVSSEDIRRVCDIIRLAATRGEEIT
>gnl|CDD|275221 TIGR04428, hypothetical_protein_AATC3_27493, tryptophan 2-C-methyltransferase. Members of this family are the B12-binding domain/radical SAM domain enzyme tryptophan methyltransferase, named TsrT in the cassette for thiostrepton biosynthesis. Thiostrepton and related thiopeptides are synthesized by extensive modification of a ribosomally translated product, but this enzyme is involved in a pathway that converts a free Trp residue to a quinaldic acid moiety before it is appended [Cellular processes, Toxin production and resistance]
LVTLVNPNLVHPPITPYALDILTTSLEAAGFEAEVLDLTFRRDDWRTALHEYFAERSPMLVGVTVRNTDT
IYAQEQRPFLDSHREIIDEIRRLTAAPVVGGGVGFSSMPFALVDYFGIEFGVKGPGEKIIVLLAEALAEG
RSTTAVPGLIVNRGVGHVTRVPPGDLQIRRGRARPVNTVTPYTRRSGVPHKVDNLEYYRRGGLGNILTKN
GCAYACSHCVEPDAKGTRFARRAPSAVVDEMESLTAQGVHDLHTTDSEFNLSIAHSKNVLREIIRRRDAD
ARSPLHELRLWIYCQPSPFDEEFAELLAAAGCAGINVAPDHVRDEVLDGWKVTGKGRRFYTFEDVERLCG
LCHGLGMLTMVEVLLGMPGETEETVRECVRRTLDLDATVTGYSLGIRLFPYSPLGINLAEQCAGVRTIPG
LQSNTATEPIVLKPLDQCASPVEYERQFMFDEHGRFRPVYYFSPDLPEDPATAASPSGRWEKSVALLWDL
VPAADRHRVMLPTLPGLSEEDNNYADNPFLLSLNELGYTGAFWSHWPQREAIMRG
>gnl|CDD|275222 TIGR04429, hypothetical_protein_bmyco0001_31490, Phr family secreted Rap phosphatase inhibitor. Phr peptides are short peptides, best conserved in their amino-terminal regions, that are almost always encoded immediately downstream of a Rap phosphatase. A portion of the Phr peptide is secreted, enters another cell, and forms a quorum-sensing system by inhibiting its Rap phosphatase partner. The set of Phr peptides recognized by this N-terminal region model is disjoint from the PhrC/PhrF set recognized by pfam11131 [Regulatory functions, Protein interactions]
MKKIKSILLGLAVVGVLSFGVNSSFTSQ
>gnl|CDD|275223 TIGR04430, OM_asym_MlaD, outer membrane lipid asymmetry maintenance protein MlaD. Members of this protein family are the MlaD (maintenance of Lipid Asymmetry D) protein of an ABC transport system that seems to remove phospholipid from the outer leaflet of the Gram-negative bacterial outer membrane (OM), leaving only lipopolysaccharide in the outer leaflet. The Mla locus has long been associated with toluene tolerance, consistent with the proposed role in retrograde transport of phospholipid and therefore with maintaining the integrity of the OM as a protective barrier
RSSKLEIWVGLFVLAGAAALLFLALKVGNLSSFSSGDTYTVTASFDNIGGLKVGAPVKIAGVKVGRVTDI
SLDPKTYQAVVTLSIDKDYKLPDDSSASILTSGLLGEQYIGLSPGGDEDYLKDGDEIEDTQSAVVLESLI
GKFLFS
>gnl|CDD|275224 TIGR04431, aminoglycoside-6'-N-acetyltransferase_type_Ib, aminoglycoside N(6')-acetyltransferase, AacA4 family. Members of this family are the aacA4 type of aminoglycoside N(6')-acetyltransferase (EC 2.3.1.82), an enzyme that modifies and inactivates aminoglycoside antibiotics such as kanamycin, neomycin, tobramycin, and amikacin. Members are regularly spread among pathogens into integron, transposon, and plasmid loci, with recombination often happening within the protein-coding region. Most of the region amino-terminal to the recombination site or sites was removed from this model [Cellular processes, Toxin production and resistance]
MSNSNDPVTLRLMTEHDLPMLHEWLNRPHIVEWWGGEEERPTLADVQEHYLPRVLAEESVTPYIAMLGEE
PIGYAQSYVALGSGDGWWEDETDPGVRGIDQSLANPSQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSP
NNHRAIRCYEKAGFVRQKTITTPDGPAVYMVQTRQAFERARSAA
>gnl|CDD|275225 TIGR04432, ribosomal_RNA_large_subunit_methyltransferase_Cfr, 23S rRNA (adenine(2503)-C(8))-methyltransferase Cfr. This model identifies Cfr, a 23S rRNA methyltransferase, EC 2.1.1.224, responsible for a transmissible form of chloramphenicol/florfenicol resistance. It is closely related to RlmN (see TIGR00048), an adenine C2-methyltransferase that acts at the same site where Cfr acts as a C8-methyltransferase [Protein synthesis, tRNA and rRNA base modification]
KNKSKYEKIKQILSDLKQPDYRYKQITKAIFKQRISTFEKMTILPKALREELINEFGPNVLSIIPVKEQT
SQQVTKVLFEISGGERVEAVRLKYKAGWESFCISSQCGCGFGCTFCATGTIGLKRNLTADEITDQLLYFH
LNGHSLDSISFMGMGEALANPQLFDALNILTDPNLFGLSPRRITISTIGIIPGIKRLTQEFPQVNLTFSL
HSPFEEQRSELMPINNRFPLDEVMNALDEHIRHTGRKVYIAYIMLRGVNDSTEHAEAVVKLLRGRGPWEH
LYHVNLIPYNSTDKTPESFGESDEERIKTFYKILKSAGISVTIRTQFGSDIDAACGQLYGE
>gnl|CDD|275226 TIGR04433, hypothetical_protein, UrcA family protein. Members of this family feature an N-terminal signal sequence, small size, and two invariant Cys residues, 10-20 residues apart. One member of this family, UrcA from the aerobic bacterium Caulobacter crescentus, is expressed so highly in response to uranium, but not other heavy metals, that a genetically engineered strain expressing green fluorescent protein in place of UrcA serves as a biodetector for micromolar uranyl ion. Caulobacter crescentus tolerates high levels of U(VI) exposure by mineralizing the uranium. UrcA and its homologs may participate in such a process
KVLAAALAALALAGTAVAAAAESEAVTVEVSYSDLDLSTEAGQRRLDARIRRAARRVCGARGRDLATAAA
ARACRREARADAVAQLAAAIA
>gnl|CDD|275227 TIGR04434, hypothetical_protein_D187_02973, B12-binding domain/radical SAM domain protein, Pput_1520 family. Members of this family are radical SAM domain (pfam04055) enzymes with an N-terminal B12-binding domain (pfam02310), as is fairly common for radical SAM enzymes with lipid substrates. However, both domains as found in this family seem to be long-branch. The function is unknown, but all cases a PLP-dependent enzyme (a cysteine desulfurase homolog) is found nearby
LRAIAVSAPDWISGAKDGRALNSTDPASLFNACRYAASLAKQRKGAWGNSNWARLDKKLREHTLLMYSLD
DMPRFENLIQRSRPNLLLIGAMTLCLPGAVACAKVAREMLGDRVLIVLGGRHVSETIYLADESKRLPSLV
KHHRASPLRLIREGRLPPVFDVVISGDGEKLIAALGEAVSAANQSPLHATFIAENLDMKTPGRWIAGLDD
RDFPRILVSDGVPLKRDELPSPVRTFGVTASFDVFGGRMTAHIFSDTGRGCVYDCNFCSERRSITGGIRD
IAGSPRRLHNQLAEAVSAIMEDHPSRGASAFVEDSVFLGGSPRLIDQFCDLLEKAPLDIIFGGQLTIDQI
LTRKAVIARLAKCGLRYVFIGVETLEPEEIGGMSKDVGRNKATWKDRFHRALDFLGENGIDCGCALLFGL
GEAHESRLNLLNGLIKLRQETGQPIPLSANWAVQHPLCGSDGGAGYNYLRWGTPEGPLLEYFHRFGEASL
RYPLPNVGAPRLGEVKEIILLLNEF
>gnl|CDD|275228 TIGR04435, ABC_transporter, restriction system-associated AAA family ATPase. Members of this family are AAA family ATPases by homology. They occur regularly in a conserved gene neighborhood with the restriction (R), modification (M), and specificity (S) proteins of an apparent type I restriction enzyme system, plus one additional uncharacterized protein. It is not clear whether members of this family contribute to restriction per se, or to another process such as transfer of mobile elements
MKLLRLKITDPKGFRSLQKGFEINFRDEWDLSEESTFAPFCFAGPNGSGKSNVLEALAAIFYHLECIYLK
YLPDSFEYDEETNPKGFRREVSTPDAFELEYLIPISNKNFKVKASKDNAHVRITKKEGKSPDILWLNYKD
FELDELEDLSRDEIKSLLPQYVLGYSSGENETLSLPFFKMRFVQFDEYWDALSKQLPYSGRPESRLAYLD
ESFSQAILLCNLLFQDKKTLKPFREEVGIEGIRSFRIIIRTEQLKHFGSEKKDYQVNLTKELEAYIDKLK
RCATCFYEDESSDTLYLDYYVNEATKQAFQEYFASSALELFQAFQVLLTLNLYIVSEELKEELYKSESLY
VSETVPTPASDERVFRFKEFELIKEGLEKPVLLKSLSDGEHQLLHSLGLCLLFKDTNSLFLLDEPETHFN
PKWRASFISRLRQCLEAGNTKNVMQEMLITTHSPFLISDCKPENVLVFKKNKENGKVEISLPKFNTFGAS
INKITMETFGKRETIGDYAQKQLKELRERFEEGEDDDELIKKILRNLGDSVEKVLLLKKILDSKE
>gnl|CDD|275229 TIGR04436, hypothetical_protein_LEP1GSC071_3095, putative 2OG-Fe(II) oxygenase. This family, related to streptomycin biosynthesis protein StrG and to phytanoyl-CoA dioxygenase, belongs to the 2-oxoglutarate and Fe(II)-dependent oxygenase clan, which includes not just dioxygenases such as phytanoyl-CoA dioxygenase PhyH, but also some chlorinating enzymes involved in natural product biosynthesis. Members of this family occur so far only in O-antigen biosynthesis regions of select Leptospira, and include an ~80 residue additional C-terminal region shared by no other proteins
KVLNVADVTSNIKKNGFSVGISKILSDSKHRELEQIIDRLLEDSSIRKDYSSNAPVLLDLVGVDPRLDLL
LEEILTHPIIDRLLLDVLGTDYKIWELSARYSLPGDNGLGLHQDAPGETNLAFLLNDQPSPEGSTVFLPG
SHLLPRWANYISWIRPKIANLFTKPLIGKKGDYAFFINKTWHSRRKNDGREVKKVLLFSFFPNGANYNPV
YPPPDSLEQIDPSCQELIRRLSVSNGVEKIDSNQVRVLSDTHLAATPEYSKLIEENLHFNFWSPWLYVQL
LILESIFKPMSLLFSIYKFL
>gnl|CDD|275230 TIGR04437, lipopolysaccharide_core_biosynthesis_protein, Kdo-III transferase WaaZ. Members of this family are WaaZ, or Kdo-III transferase. This enzyme, present in some strains of E. coli and its allies but not others, performs a non-stoichiometric addition of a third 3-deoxy-D-manno-oct-2-ulosonic acid (KDO-III) onto some fraction of KDO-II in the lipopolysaccharide (LPS) inner core [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
YITHEDVNSLIGERTSDDCIIFLSGPTSVKTPLSLLRSKDVIAVNGSARYLINNNIKPFIYVLTDVRFLH
NRRDDFYKFSQNSQHTIVNEDVYERASEEDKEYLLENCLILKSFYKREKGGFLKKIKFKILSRIHKNLLI
SVPVSKKGRLVGFSKDISLGYCSCHTVAYAAIQIAYSLKYKRIICSGLDLTGSCSRFYDENNNPMPSELS
RDLFKILPFFSFMRDNVKDINIYNLSDDTAIHYDIIPFIKAS
>gnl|CDD|275231 TIGR04438, hypothetical_protein, small Trp-rich protein. Members of this bacterial protein family average 80 residues in length, and average nearly 6 Trp residues (two of which are invariant) in the first 45, which are strongly hydrophobic. Past this region, the protein is highly charged, with large numbers of Lys, Arg, Asp, and Glu residues. Members usually are divergently transcribed from a gene encoding a c-type cytochrome
MYLLGLGLLLLVLKYLEIGPVAAWSWWWVLLPFALAAAWWAWADASGYTKRKAMEKMDQRKQARIDKQKE
ALGLGP
>gnl|CDD|275232 TIGR04439, hypothetical_protein, putative histamine N-monooxygenase. Members of this family are involved in synthesizing N-hydroxyhistamine as a precursor to acinetobactin, a siderophore found in Acinetobacter baumannii. Assuming histidine is first decarboxylated to histamine, then hydroxylated, members of this family are histamine N-monooxygenase. The putative histidine decarboxylase is found in the same biosynthetic cluster
DIAGIGIGPFNLGLAALLSHHPELSSVFLERKPEFRWHEGLLLPGTTLQVPFLADLVTMADPTHPLSYLN
YLHQHDRLYQFYYYENFLIPRREYDHYCRWAAQQLPNCRFGEEVSDVSYDAKSDRFTIESELASGEKKQY
RSRNLAIGVGTKPWLPKWAQACDHPLVKHSAEFAHLQEQLAQCKRVTVVGSGQSAAECVLALFRSLTPEQ
VAAGASIRWITRSAGFHPMEYSKLGQECFTPAYMDYFHSLPREKRREIVAGQGLLYKGISFSTIGEIFDL
LYERSIGGRDPGLSLYSNCEVESIEETGGSGALRITCYHTQLDQTFTLETDAVVAATGYRHAWPQWLEQL
KGSVLATDEHGDCIVEEDFTAQRCDQGKGRIFIQNAEIFQHGVGSPDLGIGAYRNAVIINQLLGREHYRL
PKRSAFQHYGL
>gnl|CDD|275233 TIGR04440, hypothetical_protein, glycosyltransferase domain. This model describes a putative glycotransferase domain, related to the group 2 family glycosyltransferases of pfam00535
KLTIIIPTYNRPEYLKRWLRYYSDFGCDYRIIIADSSDEKFNENNLKVFKNYSNPNITYLHYPDLGVPFY
EKLLDALEQVETPYVVICADDDFIIPSGLTECLSFLEANPDYSAAQGRYVYFEDRGDRVYGDQPFQYYPD
YSIEQDDPIERLAQFFSNYMHLWYSVFRTDVIKKAYKDLKDLNIRNPNFSEFLLGFILVASGKIKTLPSL
FGIRQ
>gnl|CDD|275234 TIGR04441, lept_O_ant_chp1, surface carbohydrate biosynthesis protein. Members of this protein family occur only in a subset of Leptospira species, and in those species occur only in O-antigen biosynthesis regions. Members average about 375 amino acids in length. The function is unknown [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
FFFKSKKIWSFPKKAELLIYDKVGYDAFFEYIDRYNPEVLDVRGESLNFYIFLLTFLKGNISLQGYINTY
IKSVRPKVVITFIDNNPKFYKLKKLFPNIITVFVQNGFRGEIGDIFGYLDPKENYNVDYMLVFGSDIGEK
YSKYIKGKSIVSGSFKNNKVSKKNQNIKKKSILFISQYITRPKNDKEPFFYEPNGRKYYWDQFYLTESIL
LPFLKEYCFRNNFSLKVCGRSKKGDEDEYNFFKEYIHGLDWKFLTRDNSLSSYELVDSAKVIVFIDSTLG
YESLARGKKTAAFTIRCRSLQNDSYKFGWPGDYPDNGPFWTNKLDVEEFKRVMDFAINISEEDWKELHQS
YFSRLMKFDPGNSLFINLLKKLL
>gnl|CDD|275235 TIGR04442, TIGR04442, TIGR04442 family protein. Members of this family occur exclusively in certain Deltaproteobacteria, including Geobacter and Pelobacter. The function is unknown
QDIRLHGQIDDSIEYYVTVAGTEAYQRYFFNIVQEVGELRIFSPGNEFILGRTGIRHEGNGGSFCEYMFG
VDQPLPDLTKGEVINRLVMYGASYRDESGELEFSNRTSGRESYDTIFFEGNAVCNYFFFVHSSRISGPLK
EQQEELVRLLGKVLKRSPAVGEEDDDRLVDELFPLLGDESAQLFLIKLINKKHQAYHDLFRSLYFKYKKI
ADDDYARLTVLAERHDIDRYQQERIRIDVMYKHPANRRIVDEYRNILIGCHLRGEISRLENARLTRLKTL
SVRNKIPGALFYTLDEVLKKDKLLVSSEEQDYIAETRQILEGIFLHERQIDSAIDREDMVRLLKAKKLAM
ENRDHAFDQLLLDASKACDEKIRDGADVALLEGFSYIITYFDRYDSTSSLINQLAFMENVRISEEMLRGL
LENKKAFDNLRPGLFDELFFKGLFENKYLGRYGRRKVLALRKGLRQIEENRLTVEALIRRLLDIDQEERL
YLRLLEHVRERIRNFYSRYTTKADQDALRREVTEELKARKLIDGDLPDHLFRETILTIQKEAVYLHNLLP
RIIADRDIALREDFLENSGLDRFYVEELEREYYELNGLDLEELYQIRK
>gnl|CDD|275236 TIGR04443, F420_CofF, coenzyme gamma-F420-2:alpha-L-glutamate ligase. Members of this family are the CofF, a RimK-related glutamate ligase that caps the gamma-glutamyl tail of the archaeal form of coenzyme F420, a hydride carrier. This enzyme does not appear in bacterial species, such as Mycobacterium tuberculosis, that make F420 with a different type of tail [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
ITIVCAEGGSTIYSLKNAIEELGEKCEILLLSSDNLLVDDSFNIETDLIHSRCGIGDYLDRLTLFSWQVL
NALEVEGHKFINPLKTIYNSSDKFKTIKILSKNNIKTPKTALIRDYEDAKKFMEKNNLEYPVILKNSFSK
CGLKVFKAKNDEELKELTKNAIWESKLIQEYIDFKNNGLYKDIRILVVDGEVVGGYRRVSNNFITNLYLG
NKVEPLKINDELEEIALKCAEVMNGYIMGVDILPKKDEYYVIEVNTAPGTKGFRQLGINADKKIAKCLIR
YAK
>gnl|CDD|275237 TIGR04444, hypothetical_protein_ThecoDRAFT_3161, chorismatase, FkbO/Hyg5 family. Members of this include two chemically distinct enzymes that cleave pyruvate from chorismate. FkbO and RapK convert chorismate to pyruvate plus (4R,5R)-4,5-dihydroxycyclohexa-1,5-dienecarboxylic acid (DCDC). HygB and Bra8 convert chorismate to pyruvate, water, and 3-hydroxybenzoate. These two enzymes are closely related, and lack homology to chorismate lyase, EC 4.1.3.40, which converts chorismate to pyruvate plus 4-hydroxybenzoate
GGRNVLGVVEYGTGHRPPSLLEGVPRLEVRMTAPEDEPFAEVWTTDGPAEAGRQDGLVYAHDGEYLFCAG
RIPEGDRYADATRAVYTAAFELMDELGYPRLFRMWNYVGDINEDNADGLEVYRDFCVGRAEAFEAWGIRP
AGMPAATGIGSHGGGIAFYFLACRSGGVTHIENPRQLPAYHYPRRYGPRSPSFARATVLESDAGGVRLFV
SGTASILGHETVHPGDVAAQCEVALENIELLIGAENLGRHGIARGYGLTDVDRIKVYVRHREDLPAVRRR
CAEALSPDADIAFLNVDICRSDLLVEIEGVV
>gnl|CDD|275238 TIGR04445, preny_LynF_TruF, peptide O-prenyltransferase, LynF/TruF/PatF family. Members of this family are prenytransferases that modify mostly, perhaps exclusively, ribosomally derived cyclic peptides. Note that in some cases, the natural product becomes C-prenylated through a non-enzymatic rearrangement after initial O-prenylation. Prenylated products carry names such as prenylagaramide, anacyclamide, and piricyclamide
QRLQFIRTHQQAFDVEPVYPLPLFEEFVLEIEGSCTIEASCKIEKDKLFAGRFLLFFDQGQDWPQSLTDA
LNFFDKVESRVGVQIDRSLLQQFLGLHFDFSKIENNTVGIDLRPELADSSLKIHIRLEDYPEKVKTALAL
DGGFYSDELTQVLLNDTLLIGFDFFLDGRSEIELYPELPGKKFQRPDLQAYLQSNFSPKALSLLKASDLF
GVGFSKANTEPVLYFYLKNIKDLLNYFLFNDLGNRVYSFYQNQDCITYMWVGVAESELEKNRIENFRLYY
HK
>gnl|CDD|275239 TIGR04446, anacyclamide_precursor, prenylated cyclic peptide, anacyclamide/piricyclamide family. Members of this protein family occur primarily in Cyanobacteria. They average about 50 residues in length and are the ribosomally translated precursors of peptide natural products whose modifications include cleavage, cyclization, and prenylation. Sequences are well-conserved in the N-terminal region. They are nearly invariant over the last eight residues, but hypervariable just before that stretch. A related family, often in a similar genome context, is TIGR03678
MKKKKLTPRQAAPVQRENISTVSDDGNAITPLTNGDGQCNPFAGDDAE
>gnl|CDD|275240 TIGR04447, hypothetical_protein, cyanobactin cluster PatC/TenC/TruC protein. Members of this family usually are small proteins (PatC, TenC, TruC) of unknown function in cyanobactin (prenylated cyclic peptide) biosynthesis clusters, where a different small protein is a known cyanobactin precursor (patellamide, anacyclamide, piricyclamide, etc). They may instead be the C-terminal domain of a longer protein that otherwise consists mostly of lectin-like or VWF type A domains, in similar context. Similar to the cyanobactin precursors, members of this family have two very strongly conserved regions separated by a hypervariable region, suggesting these proteins may undergo a similar maturation
TGLEDYGYWSKEVAKEQKKQERNDKPFRRGRIWA
>gnl|CDD|275241 TIGR04448, creatininase, creatininase. Members of this family are creatininase (EC 3.5.2.10), an amidohydrolase that interconverts creatinine + H(2)O with creatine. It should not be confused with creatinase (EC 3.5.3.3), which hydrolyzes creatine to sarcosine plus urea [Central intermediary metabolism, Nitrogen metabolism]
ELTWPEYEEAVAEGAVIILPIGSTEQHGPHLPLGTDALLATAVAEAVAERIDGLVAPALSYGYKSQPLSG
GGNHFPGTTSLDGATLILLVRDVVREFVRHGFRRIVLVNGHYENQWFIVEGIDLALRELRYGIPDAKIMV
LEYWDFVQEATIDKLFPEGFPGWDLEHAAVMETSLMLHLHPELVDMDRAVDDAPAKFPPYDVYPVDPDFV
PPSGVLSSAKGASAEKGKLLAEDVVEGIAAAIRKEF
>gnl|CDD|275242 TIGR04449, halocin_C8_dom, halocin C8-like bacteriocin domain. This model describes the 76-amino C-terminal domain of the halocin C8 precursor that actually becomes the mature bacteriocin halocin C8 after export and cleavage, as well as homologous C-terminal regions from many other archaea. Surprisingly, this Cys-rich region occurs also in many strains of Staphylococcus epidermidis. Gene regions do not provide evidence for post-translational modification other than cleavage. Halocin C8 is active against a broad range of archaea; the region N-terminal to the bacteriocin domain modeled here serves as the immunity protein for the cell secreting the bacteriocin [Cellular processes, Toxin production and resistance]
CSACTTAVGLLCRLGCGAGCAAICGLLGLATFGIGGLACAGFCAAVCWLISGYGCGAAARYICGKAGYC
>gnl|CDD|275243 TIGR04450, Gpos_C8_like, putative immunity protein/bacteriocin. This model describes full-length proteins of Gram-positive bacteria that consist of an N-terminal signal peptide, a central region of unknown function, and a Cys-rich C-terminal region. In both the overall architecture and the apparent weak homology of the C-terminal region itself, these proteins resemble archaeal proteins such as the halocin C8 precursor. In that precursor, the C-terminal region is a bacteriocin but the N-terminal region functions as the immunity protein. The related family of halocin C8-like bacteriocins and their bacterial homologs are recognized by model TIGR04449
SILMAFTLFLVPIASYNTSPADNANVLGTNCTSCSLEGAESENYLKELLKSKNFKETILSKKDKSQVEQL
VNDKKEKDLEVKEQMKVAGTKKNDLENKSYGIIYFETNEVDKIGYLYDTYFGITFDENGELLVITIKYSN
YNKKLVNFTEGGLDKLFSGDISPLIADSDSSFKTKKVDGDESCRGFKWWGKAFACGMSGALACLSYCGVF
GLWNLAAGTVCGTVCGIAFAAACS
>gnl|CDD|275244 TIGR04451, lanti_SCO0268, lantipeptide, SCO0268 family. Members of this family are putative lantipeptide (most likely lantibiotic) precursors, about 53 amino acids long, found in a lantibiotic-type biosynthetic cluster in several species of Streptomyces (S. coelicolor, S. griseoflavus, S. ambofaciens, etc.). This family is described in AntiSMASH as Streptomyces PEQAXS motif lantipeptide precursor
MRTEIVLSNDAPELDLDLDLRVSDLPEQAESFGQGTFTSPSSYAIGTRCPVCC
>gnl|CDD|275245 TIGR04452, hypothetical_protein_LEP1GSC192_2752, small lipoprotein, LA_3946 family. Members of this family of small lipoproteins that occur in at least nineteen species of Leptospira, but not so far anywhere outside that genus. Notable features include the putative lipoprotein modification Cys and an additional Cys near the C-terminus, both invariant, plus a well-conserved (although not invariant) Tyr-Tyr pair. From one to four paralogs occur in most Leptospira species. Members include LA_3946
ILLLLFFTNCNLLDTLGLSPDRVKGSEAKKKILDAAIIGDLVYASSLFGAQGASVLLLSILAPQLAGIDE
SKYYKKSDVDDCVKEIKTLGLLLLGSSITFITGFSCDLKPDGYII
>gnl|CDD|275246 TIGR04453, Lepto_8Cys, Cys-rich protein, LA_1312 family. Members of this protein family occur, so far, exclusively in the genus Leptospira. Members, although small (about 90 amino acids), have a predicted signal peptide followed by a region with eight invariant Cys residues. Some members have an additional Cys in the signal peptide region that suggests handling as a lipoprotein, but this Cys is not well conserved
KRTLPLLLLVLLFGSCQAAVEQKCNEACDFFVGCVEEEFPGKLSEEQKNKVRIGCLNGCRKHQSKILVCL
ENEKTQCKGFNTCLM
>gnl|CDD|275247 TIGR04454, Lepto_4Cys, small lipoprotein, LB_250 family. Members of this family average about 92 amino acids in length, including an apparent lipoprotein signal peptide and a mature portion with four additional invariant Cys residues. This family is universal, so far, across at least twenty species of Leptospira but unknown outside the genus
MKKTLFLILAILLLSLLVSCGGAKVSQAECEPVVNELFTNLTAGQTPEQAEKLAALQAQLKPKLLKECMS
GKYDLTCLKSAKTIAALATCKK
>gnl|CDD|275248 TIGR04455, hypothetical_protein_LEP1GSC192_0546, probable lipoprotein, LA_1396/MXAN_6521 family. Members of this family are predicted lipoproteins, near 200 residues in length, found in multiple species of Leptospira (a spirochete) but also in the Myxococcales branch of the Deltaproteobacteria (Myxococcus xanthus, Chondromyces apiculatus, Cystobacter fuscus, Corallococcus coralloides), an uncommon mix of species. In both lineages, the N-terminal region appears to be a lipoprotein signal peptide
MRRTLLFFGLIVLTGNCAVKYVRIRPDYEKDLDQFKRLVVVTQSLSDGGQAEGDLWSLIAEQYLNHHKEF
IVYPDRSTDGTFCALCVGKVQGVLWLKPREKLTGDGAELSVLAQLIRCRDGEILWEAEASGSYSSNDEEY
QSLRNTYTQKFGEEVAPKVVPYYKLLQALLDTLPNPVLNEAEKDEKIELEE
>gnl|CDD|275249 TIGR04456, hypothetical_protein_ACD_77C00477G0043, LruC domain. This domain is abundant in the Leptospira, in Bacteroides, and in Vibrio (three widely separated lineages). Most members have plausible lipoprotein signal peptides, including lipoprotein LruC from Leptospira interrogans and BACOVA_00967, from Bacteroides ovatus, with a solved crystal structure. Note that the C-terminal region of pfam13448 (length 83) matches the N-terminal region of some members of this domain (length 243)
GTLAFEDLWPSKGDYDMNDVVVRYRVTEYLNANNEVKRIKITGTLVARGAGYHNGFAIQLPGVDPSNVKV
TSIRLTINGVTQSSNGLEAGQSEAVIIVFDDLKDVLPGGCSFFNTEAGCQEVDGKTFTITIEFNNPVSLS
DLGAAPYDPFIFVPGTPGRGKEIHLPNYAPTDLADTSLFGTGDDASDPAAGRYYKTSNNLPWAINIPDEW
QHPLEKVDITKAYPKFADWAESGGTTNTDWYK
>gnl|CDD|275250 TIGR04457, lipo_LenA_lepto, lipoprotein LenA. Members of this family are LenA (Leptospira Endostatin-like protein A), found in pathogenic and intermediate species of Leptospira but not in saprophytes. LenA binds plasminogen, laminin, and complement regulator factor H. Behavior during outer membrane solubilization by low concentrations of Triton X-114 and conservation in all family members of an apparent lipoprotein signal sequence, with invariant Cys residue, strongly suggest that LenA is a lipoprotein. Just outside this family is a full-length homolog found in another spirochete, Turneriella parva DSM 21527
LLVLLFALFFLAGCGKKEEDAPQAQIAGTRYAGYDQWIYKKPGSTAKGDQVTLVYGMEEVEGLEIVVEEK
TDKKGPKGVTEYIKVKTVDNKEGFAPAKNFADAVLFVLSDGDKAFAKPSLTAPSKGKLARGMYCLEIEAI
GEFSKVRCYGSIVTGGKLNNHYDVWIQPISTNISKDPLLGDSIRNLKSASQKLIEEGKKSDTNKNEELKG
SAAKALKAVAEKGD
>gnl|CDD|275251 TIGR04458, putative_cytochrome_P450, 4-nitrotryptophan synthase. Members of this family are cytochrome P450 enzymes that convert L-tryptophan into L-4-nitrotryptophan. In thaxtomin gene clusters, this enzyme (TxtE) uses nitric acid (NO) derived from arginine by the nitric oxide synthase TxtD, and O2, to perform the tryptophan nitration. L-4-nitrotryptophan is then used as a non-proteinogenic amino acid by non-ribosomal peptide synthases (NRPS)
PSPLADPSIVPDPYPVYADLARREPVHWCEGLNAWAVLKYADCAAALKDPRLKAERMTEVLEAKFPGQPL
PPDSIYHRFTKNVMMYTDPPLHDALRRSTHAGFTRAAHEHYDQVIERVAADLVASVPAGATEIDAVPALA
AQLPVRSAVHAFGVPEEDLDFVIPRVETLMTYWSGPQDQPVELERLLELLTDLHTYASELLEGKRGKVLP
DTVIARLAAAQDGLTETTPEQTVHQLVLLFIALFAPTTPGSLSSGMLAFARNPDQIERFLADPACVDNTA
NEVVRYNASNQFTWRVATTDVDMGGVRIKAGQAVALFLGAANRDPEVFERPNDFDLDRPNSGRHLSFGQG
VHACLGRQIASLQLKWFFVALLGRFPGIRPAGEPLWNENLEFRSLRSLPLSLR
>gnl|CDD|275252 TIGR04459, TisB_tox, type I toxin-antitoxin system toxin TisB. Members of this family are the TisB toxin protein of a type I toxin-antitoxin system, meaning that the antitoxin is a non-coding RNA. TisB is induced by some types of stress (SOS, ciprofloxacin) and appears to induce a persister state by dissipating transmembrane potential, thus depleting ATP. Persister cells, unable to grow until the persister state changes, survive a number of challenges, including exposure to most antibiotics [Cellular processes, Adaptations to atypical conditions]
MGVVDIVILILKLIVAVLQLLDAVLKYLR
>gnl|CDD|275253 TIGR04460, endura_MppR, enduracididine biosynthesis enzyme MppR. Members of this family are MppR, one of three enzymes involved in synthesizing enduracididine, a non-proteinogenic amino acid used in non-ribosomal peptide synthases to make natural products such as enduracidin from Streptomyces fungicidicus ATCC 21013. MppR is belongs to the acetoacetate decarboxylase-like superfamily. MppR catalyzes an aldol condensation and a dehydration, not a decarboxylation
PVGYSLPLSPTGEAAMLTPPPWHFSGEVVMVEYRVDPDAAARFLPPGLEPGPDPGAAAAVFATWQWCSDS
GAELTDPERCQFGEFLILLGCEFRGRPMARCPYAWVDQAVPLVRGWVQGMPKQFGVIHQTRPVTVGRAGS
RLAPGGRFDGALSVHGRRVVEAAVTVRRETDDPPPLHDVPLVHSLVFPEWVPSGEGPRPRLVASEVTDVE
FSPIWTGSADLTFFDGLGDDFGTLAPLEVGTGHVFSYGETLVGGRLL
>gnl|CDD|275254 TIGR04461, PLP-dependent_aminotransferse, enduracididine biosynthesis enzyme MppQ. Members of this family are MppQ, one of three enzymes involved in synthesizing enduracididine, a non-proteinogenic amino acid used in non-ribosomal peptide synthases to make natural products such as enduracidin from Streptomyces fungicidicus ATCC 21013. MppQ is a PLP-dependent enzyme, predicted by homology to be an aminotransferase
WRAGVVQEVAPAGVLDLGPGYLEPALLPVRLLRDAYAQALDEYGAAALGYGHNPGAAPLRAALAARAGTA
DGRPCGPEHVLVTAGTSQALHLLATLLARPGDTVLAEPLSYDLGLRILTDCRLRIEVVASDMSGMVPEAL
TAALARTARAGRRTAFVYLTPTHHNPTGVTMPDERRRRLLEEAADHGVLIVEDDAYAELRLDDGPPEPPS
LAALAGRRGVVRLGSFSKTLGPGLRLGWLEADPALADRCAAHGLFDSGGGLNHLTSLAVAGLLSGGDYDR
HLAWLRAELRARRDALVDALRRTAGERLGVVPPYGGFFLWLRAGAGADEQALLARAARAGVSVAAGSRFG
ATGEGAVRLAFSFNPPPVLEAAAHRLTAAWAGSAPLDAIGTS
>gnl|CDD|275255 TIGR04462, PLP-dependent_aminotransferase, enduracididine biosynthesis enzyme MppP. Members of this family are MppP, one of three enzymes involved in synthesizing enduracididine, a non-proteinogenic amino acid used in non-ribosomal peptide synthases to make natural products such as enduracidin from Streptomyces fungicidicus ATCC 21013. MppP is a PLP-dependent enzyme, predicted by homology to be an aminotransferase
LSCYSSSVAMEILSRALAPATGSVALVHPTFDNIADLLRGNGLRLVPLEEDPLHEDDLSAALLESVGCVF
VTTPNNPTGRVLSEERLARLAAQCAAHGVVLALDTSFRGFDTRAHYDHYEVLRASGCRWVVIEDTGKLWP
TLDLKVGMLVHSENLGLPVEKIYSDILLGVSPLILVMVRRFSEDAAAGGLADLHRFIADNRALVRATLAD
LPDLAVPDPDSRASVERVDLGELTGTDVWERLRQHGVYALPCRAFHWADPARGDHTLRLALARVPGPLEQ
AVRALRHVL
>gnl|CDD|275256 TIGR04463, Radical_SAM_domain_protein, radical SAM/SPASM domain protein maturase. Members of this family are probable protein/peptide-modifying radical SAM/SPASM domain proteins. The majority of members of this family seem to target Cys-rich repetitive regions of large proteins rather than of bacteriocin-sized small precursors. This arrangement suggests the modification target may be multifunctional, with the C-terminal domain behaving like a bacteriocin but other parts of the same precursor serving an immunity function, as occurs for the halocin C8 precursor
YNIFVPLVNEKALLYNTLSGGLSLLEPEDVQIYRSLEQNRLCETLTPILDSLSSQGFAVPADRDELLVTE
KLYGQSRFNDSHLILTVAPTLGCNFACDYCFQGLDKKHGKMSEDVQDKILDLIDTNHKNLQSLEVHWYGG
EPLNDRQVIYALSDMLIKYCDERGIRYFASMVTNGYQLTGEVARDLYKRRVKWVQVTIDGAKSIHDTRRI
LLSGKGSFDKIIRNLKEIVAQTPIKIVIRVNVDNRNIDQIYDLIDDLAAQGLSNSNVTIYFAPIQTMTEE
CHSINEFTLGKRDYAEKELKLMRYAHDKGLLKFDLPGVFNGICVAVRPKGWVIDPSGNIHKCWDTVQYED
LKVGDVTSPDELANSPYLKMWRSWTPFQLPTCRNCKILPNCGGSCAYKFLHRDKTEGDDTQLPCPSLKYN
IAERLFEFAIDQGLITHAD
>gnl|CDD|275257 TIGR04464, chaper_lep, LipL41-expression chaperone Lep. Members of this protein family are Lep, an outer membrane lipoprotein LipL41-binding protein that appears to function as a chaperone important to its expression. LipL41 is the third most abundant lipoprotein in the pathogen Leptospira interrogans, but is found in saprophytic Leptospira species as well and is not essential for virulence
ISLKFGSCEKSGRITSAFLFCISVLFLSDCRTKPNEEECVDAQIHIVKLIADDEEMPKQMQALMLRSILK
PETSEAIVLRCVSNKTLKQVQCELSKEKFSDLQECKKFGKEESK
>gnl|CDD|275258 TIGR04465, ArgArg_F420, TAT-translocated F420-dependent dehydrogenase, FGD2 family. Members of this family are F420-binding enzymes with a proven functional N-terminal twin-arginine translocation (TAT) signal. Members are homologous to the cytosolic F420-dependent glucose-6-phosphate dehydrogenase but do not share the same function
TGISRRTFGRLAAGAGVLGAAGLAAGCAKPGTSHGTPAAPPEPAGKGVGFVLSHEQFRTDRLVAQAQAAE
QAGFRYVWASDHIQPWQDNEGHSMFPWLTLALVGNSTSHVSFGTGVTCPTYRYHPATVAQAFASLAILNP
GRVFLGVGTGERLNEQAATNQFGNYRERHDRLIEAIQLIRQLWSGQRISFSGRYFQTNSLKLYDVPATPP
PIFVAAGGPKSATLAGQYGDGWITQARDVTNPKLLAAFAAGAQAAGRDPATLGKRAELFAVVGDDAEAAR
AATLWRFTAGAVDQPNPVEIQRAAESNPIDKVLAGWTVGTDPAVHIGAVQAVLDAGAVPFLHFPQDDPVT
AIEFYRTNVLPELH
>gnl|CDD|275259 TIGR04466, hypothetical_protein_Radical_SAM, cytosylglucuronate decarboxylase. BlsE, part of the blasticidin S biosynthetic pathway, is a radical SAM enzyme that performs a decarboxylation at C5 of the glucoside residue. MilG in mildiomycin biosynthesis is equivalent. This enzyme follows CGA synthase and makes the pyranoside core moiety of a class of peptidyl nucleoside antibiotics [Cellular processes, Toxin production and resistance]
RDRYLFIRILEACNADCFMCEFALSRDTYRFSLEDFDELLPQAVEAGVGYVRFTGGEPLMHGEVLELVRE
GTAAGMKMSLITNGMRLPRMVDRLAEAGLAQVIVSLDGSSGETHDVYRRSPGMFDRGLRGLRRASRLGVL
PRVNTVVGPHNYTQMPELQRVLTEAGVQQWELSALKLERHIAYPDPDHVLAACEPVYLADPERWLVPLGK
RFYGDTPEEQELYFERSVTPRASRPLCHVTDDVIYLDGKYGRAFACSCLPHREGDDGPGGAPLREERGVV
RLDTPVFRTHADEFKQQGPTVCNGCSTTAAGYSDDVARLGAVPAWHY
>gnl|CDD|275260 TIGR04467, cytosylglucuronic_acid_synthase, hydroxymethylcytosylglucuronate/cytosylglucuronate synthase. Members of this family synthesize cytosylglucuronate (or hydroxymethylcytosylglucuronate) from UDP-glucuronate and free cytosine (or hydroxymethylcytosine). This reaction is followed by a decarboxylation at C5 of the glucoside residue. The net reaction makes the pyranoside core moiety of a class of peptidyl nucleoside antibiotics
SGVEFGWGSAGKLSAVLSALRSRSTEPLRFTGLGSGLGRPVLTELGIDRWYDVPVSPGDGPAAVNALIRE
LAVDAALVVLDGALATALEAAGCPVVYVDSLPFLWTEHDALPLDVTLYCAQKCLELPPECRTVLARVRAL
RWVEPVVGTPHSAGLAAALQAEAGAPYREAVLNLGGLRSPFTLRDDDSYPRLVLPPALDALSAAGIEEVV
IAGNLPPDLARLPDAGTMPPTVTAGRLAHGAFLDRLLRADVLVTSPGLTTLLEAAALGVPAVCLPPQNLS
QVFNGRLVEHACGAELRVSWPEQVLTEAEALALRRQGEEHAVERIYARIAAAAAEPDHDVVTHALRDGIL
AGLDGLANGTRSWGALTQTVGAGGAAQVADALLERL
>gnl|CDD|275261 TIGR04468, arginine_aminomutase, arginine 2,3-aminomutase. Members of this family are arginine 2,3-aminomutase, a radical SAM enzyme more closely related to lysine 2,3-aminomutase than to glutamate 2,3-aminomutase. The enzyme makes L-beta-arginine, sometimes in the context of antibiotic biosynthesis (blasticidin S, mildiomycin, etc). Activity is proven in Streptomyces griseochromogenes, which makes blasticidin S
QWNDWKFQLRNRIRTLEQLKEWVNVSPEEEKAIAATEGKYRWMVTPYYASLMDKTDPNCPIRLQAIPHLG
EFMENQGADVDPVGDTKYRKTNRVVHKYPDRVIMLVTDTCPVYCRHCTRKYHTTDVNGTYFERDEAESYE
EDFEYIANHPEIRDVLLTGGDPLTYSDKKLESIISRLRSIPHVEIIRIGSRYPVLLPQRITDEFCQMLEK
YHPIWLNTHFNHPKEVTPEAASACDRLLRHGIPVQNQTVLLKGINDDLETMRALLRALLKIRVRPYYLYH
CDNVTGVSHFMTSLEKGREIMRGLVGYETGFAVPQYVITTKLGKIPLNRQYVVEQGDGLILRNYEGKELD
I
>gnl|CDD|275262 TIGR04469, hypothetical_protein, CGA synthase-related protein. Members of this family are related to cytosylglucuronate (CGA) synthase (TIGR04466), and found in the same clusters as CGA synthase and CGA decarboxylase. These clusters produce peptidyl nucleoside antibiotics with a pyranoside core moiety, found in a number of Streptomyces species. Removal of the S. griseochromogenes member of this family, BlsF, from a heterologous expression system caused an increase, not blockage, of blasticidin S [Cellular processes, Toxin production and resistance]
ILLVARPDDLDSATALGRVAAHLGELRLLPESGSTDSGPGRPPPDAALVCDDSGAAERLLPAGVPVVHLS
SGAEPTNLPGTTAAVVRVHRPGWLPAPGPRPPGVRPAGLLAPARQVRSRNRAGALLLLSAWGVPDAEAAA
FAGELLRALAQEALRRTGRCAVVGDTGPGLARLTGEVLAELRGVRVPRARDVDVDALHARADVLVASPTL
TALALAQTARIPLALLPPLGPHQRDLARVVREAVALPGADDPDDLALWAPDDQQAAGAWPRLDPRLDDLR
GAQRVARTLRQLALAPL
>gnl|CDD|275263 TIGR04470, hypothetical_protein_ALIPUT_00462, radical SAM mobile pair protein B. Members of this family are the downstream member (B) of a pair of tandem-encoded radical SAM enzymes. Most of these radical SAM gene pairs have an additional upstream regulatory gene in the MarR family. Examples of high sequence identity (over 96 percent) from cassettes in several Treponema species of the oral cavity to those in multiple Firmicutes in the gut microbiome suggest recent lateral gene transfer, as might be expected for antibiotic resistance genes. The function is unknown
IREVETKNIMTKSSLPVGGYSVNPYVGCTHACKYCYASFMKRFTGHTEPWGTFLDVKHWKEIKNPHKYDG
QRVVIGSVTDGYNPQEEQFHNTRKLLEQLRGSDAEILICTKSDLVVRDIDLLKSFGKVTVSWSINTLDEQ
FCADMDNAVSIERRLKAMKQTYDAGIRTVCFVSPVFPGITDFEAIFERVKNQCDLIWLENLNLRGGFKGG
IMDYIREKYPDLIPLYEEIYNKKRRSYFQALEQDAENYAKEQGCPFVDNELPYGRSEKGHPVIVNYFYHE
EIRGT
>gnl|CDD|275264 TIGR04471, hypothetical_protein_ALIPUT_00463, radical SAM mobile pair protein A. Members of this family are the upstream member (A) of a pair of tandem-encoded radical SAM enzymes. Most of these radical SAM gene pairs have an additional upstream regulatory gene in the MarR family. Examples of high sequence identity (over 96 percent) from cassettes in several Treponema species of the oral cavity to those in multiple Firmicutes in the gut microbiome suggest recent lateral gene transfer, as might be expected for antibiotic resistance genes. The function is unknown
VCIKSQIQNMNLVIGCTIGCPYCYARNNCRRFHIIDDFEKPEYFEGKLRIMEKSRPQVFLLTGMSDFSGW
KPEWRAEVFEKISSNPQHQYLFLTKRPDKISFSTDLDNAWFGVTVTRSSEKRRIDALRKNIKARHYHVTF
EPLFDDIGEVDFTGIDWIVIGTETGNRKGKSYSRPEWVLSLTEQAHALGIPVFMKEDLLPIMGDERMIQE
LPEAFTKVLE
>gnl|CDD|275265 TIGR04472, reg_rSAM_mob, mobile rSAM pair MarR family regulator. A number of human microbiome species from both the Firmicutes and the spirochete genus Treponema share a gene cassette encoding a pair of radical SAM enzymes and, in most cases, this MarR family transcriptional regulator as well. Sequence identity can exceed 96 percent, suggesting recent lateral transfer. These observations suggest the cassette confers resistance to a toxic compound such as an antibiotic
NGGFLVTKIKQLGDRIFEKILSEKNIDAFNGAQGRILYVLWQEDGIPIKSLSEKCGLAITSLTTMLERME
NQGLISRVQDETDKRKTLLFLTEKAHSLKDEYDSVSDEMGSIYYKGFSEKEITQFEEYLERIRKNLEEWQ
E
>gnl|CDD|275266 TIGR04473, phenylalanine_aminomutase, phenylalanine aminomutase (L-beta-phenylalanine forming). Members of this family are the phenylalanine aminomutase known from taxol biosynthesis. This enzyme has the MIO prosthetic group (4-methylideneimidazole-5-one), derived from an Ala-Ser-Gly motif. Other MIO enzymes include Phe, Tyr, and His ammonia-lyases. This model serves as an exception to overrule assignments by equivalog model TIGR01226 for phenylalanine ammonia-lyase
MGFAVESRSHVKDILGLINTFNEVKKITVDGTTPITVAHVAALARRHDVKVALEAEQCRARVETCSSWVQ
RKAEDGADIYGVTTGFGACSSRRTNQLSELQESLIRCLLAGVFTKGCASSVDELPATATRSAMLLRLNSF
TYGCSGIRWEVMEALEKLLNSNVSPKVPLRGSVSASGDLIPLAYIAGLLIGKPSVIARIGDDVEVPAPEA
LSRVGLRPFKLQAKEGLALVNGTSFATALASTVMYDANVLLLLVETLCGMFCEVIFGREEFAHPLIHKVK
PHPGQIESAELLEWLLRSSPFQDLSREYYSIDKLKKPKQDRYALRSSPQWLAPLVQTIRDATTTVETEVN
SANDNPIIDHANDRALHGANFQGSAVGFYMDYVRIAVAGLGKLLFAQFTELMIEYYSNGLPGNLSLGPDL
SVDYGLKGLDIAMAAYSSELQYLANPVTTHVHSAEQHNQDINSLALISARKTEEALDILKLMIASHLTAM
CQAVDLRQLEEALVKVVENVVSTLADECGLPNDTKARLLYVAKAVPVYTYLESPCDPTLPLLLGLKQSCF
DSILALHKKDGIETDTLVDRLAEFEKRLSDRLENEMTAVRVLYEKKGHKTADNNDALVRIQGSKFLPFYR
FVREELDTGVMSARREQTPQEDVQKVFDAIADGRITVPLLHCLQGFLGQPNGCANGV
>gnl|CDD|275267 TIGR04474, conserved_hypothetical_protein, three-Cys-motif partner protein. Members of this family occur regularly as a partner to as a member of family pfam07505, which has been called a phage protein but which seems to occur also in other contexts. Members average about 400 residues in length, but the conserved region covered by the model averages 260 residues and excludes the C-terminus. Conserved motifs suggest enzymatic activity. Note that its frequent partner protein (see pfam07505) has a three-cysteine motif that resembles the Cx3CxxC motif of radical SAM proteins, and that in one branch (see TIGR04471) actually becomes Cx3CxxC. We suggest the name three-Cys-motif partner protein (tcmP), and renaming pfam07505 to three-Cys-motif family protein
EHSKAKHEILQKYLRAYAPVLGSKPQQEKFRLTYIDGFAGPGRYKDGDTGEIDGSPLIALEALPEAERLI
NELDYIFIDKDPERFEALQQLLQELGGPKLLKVEIFHGDFNETLDAILSKIGKVGKRRAFFFLDPYGYKD
VPWETIEKLAKTKKTEVLLTFSVDDLNRFLSGTNNNSKRDKLDRLFGTPDWRRLVYLKELPKGLWRAAIV
ELYRERLKTCGAKYVTPFFIRNSKGQPLYWLIFASKHELARDVMKDIHWKVD
>gnl|CDD|275268 TIGR04475, putative_phenylalanine_ammonia_lyase_EncP, phenylalanine aminomutase (D-beta-phenylalanine forming). Members of this family have the MIO prosthetic group (4-methylideneimidazole-5-one), derived from an Ala-Ser-Gly motif. Other MIO enzymes include Phe, Tyr, and His ammonia-lyases. The member from Pantoea agglomerans, and probably all members, convert Phe to D-beta-phenylalanine (EC 5.4.3.11). By contrast, members of family TIGR04473 convert Phe to L-beta-phenylalanine (5.4.3.10), as in taxol biosynthesis
TFVISPGERVSLEDIARAARDDLPVELDDEVRNRVAASRKLLEKFVADGRVIYGVNTSMGGFVDYLVPIE
KASELQENLINAVATNVGEYFDDTTVRATMLARIVSLSRGNSAISLENFDKLIAIYNAGVVPCIPEKGSL
GTSGDLGPLAAIALVCTGQWKARYQGEILSGAEALEKAGIAPMELSYKEGLALINGTSAMVGLAALNYQE
ARRLLDQYLSISALSIEGLAGKTKPFHPDVHQLKPHRGQQEVATRIWEALADSKLAVDELETEANLAEEM
TNVVKAEDMQIEDAYSIRCTPQILGPVLDTLDFIKRTLENELNSSNDNPLILPEEGDVFHNGHFHGQYIS
MAMDHLSIALTTLSNLSDRRIDRFMDKSNSNGLPPFLCAENPGLRLGLMGGQFMSASITAENRSLCVPVS
IQSLTTTGDFQDIVSFGLVAARRAREVLQNTRYVVAFELLCACQAVDIRGAEKLSSRTRALYERVRELVP
YLDRDETITDYLEALAAFVL
>gnl|CDD|275269 TIGR04476, transmembrane_exosortase, exosortase N. Members of this family are exosortase N (xrtN), a bacterial exosortase variant whose single target, encoded always by an adjacent gene, belongs to the vault protein inter-alpha-trypsin family. This system occurs in a number of spirochete (Leptospira) and Bacteriodetes species
FKLAILALGFVLLMFALGPKLKYLNNTDFLFILGILVLPIVLSFKTSKKINRFLLPALLFLLLSIVLPTK
TLVFIALLLFLLFLVEYLTGKFSFLALFLLLLISPIFNYFSEVLGFPIRLGLTEIAVETLKLAGSIIQAE
GNIIFLNGAKFSVDQACMGLKMLKTSLLIAAFIIAYYQRKLQKKLSFLQILTILLLTLPLNIISNLFRIV
VLVLFQIMPETWLHEAAGLICFLCYVVLPLLFLIKWFPKPKFVNPVLQKRSPPIILWLILSLLLLVLSLA
RFIETKTNIDPSIISQFPLGFKGEWLNNEVAKLENDEALIYIKPPLNFYGTDHNPMICWKGSGYKFIEIQ
EKNIGGKEIYFAELEKGKDKLYTLWWYENGPQKTISQLEWRWRKLLGAEPFYL
>gnl|CDD|275270 TIGR04477, sorted_by_XrtN, XrtN system VIT domain protein. Members of this subfamily average about 850 amino acids in length, ending with a variant form of PEP-CTERM sorting signal. Members have a VIT (vault protein inter-alpha-trypsin inhibitor heavy chain) domain (pfam08487). Other bacterial subfamilies of VIT domain proteins have members with either GlyGly-CTERM or LPXTG C-terminal sorting signals. Members of this subfamily occur only in context next to a protein sorting/processing enzyme, exosortase N (XrtN). These subsystems occur both among the Bacteriodetes and in the spirochete genus Leptospira
ILVGLSVILLSFLLFFFDLGLHSANNDEFFSLFFINYGIAIIYLLFSLIIRLLRPKFKSNKPLPLTILLL
LLFFISAFSLNKEINVFENSVSWLSLTLFLSSITLFLFAFMEKIPKFVISFLFFLLGLAFVLFAYYALYL
APFYLIGLLGAIGLGISLHALVPLLLLIVTIVFIRKNHRQKKILSYMFVSGILLPIILIIYFAVQWNNEN
QKVSKIQNQQTLNTEGELPNWVNLSQELPPNFVTEKVLKSDLVYQTSESFGDSFFFPGKGFNEPKKHDPL
VVIASLFRGTIELDREDRIKILKALYDLRHETQERLWSGDDLITSNIKTNVQIFPELRLAYTEKTLSVEN
ESQSSWRPPQEAIYTFHLPEGSVVSSLSLWINGREEKARLTTKGKADKAYNTIVGVERRDPSVVHWQEGN
RVRVRVFPCNPEEDRQFKIGITSPLKLENNKLIYENIYFEGPSASGASEIVNVQFESTPKDLAISSGFSS
DGNGTYWHEGAYLPDWELSIPAEPLSSHTFSFAGVSYQVAPLKKQYQPFDPESIYLDLNSSWSRDEINQA
VAIIKKRVVYFYNEEFETLTKQNADRLFAELEALNFSLFPIHKISDPGNSLLITKSNTQSPNLGDLKDSE
FSKKLKTYLSKNETPVKVFNIGDNLSPYLKTLKELNVFQYVQGSLSTLVKLLKNKRFIEYVEQENEVAIP
PAGLSIEKSAGTGKTTNAPDHLLRLFAYNKIMKKVGKHYFDRDYVNDDLVDEAKEANIVSPVSSLIVLET
QKDYDRFGIEESKNSLGNAAINSSGAVPEPHEWALIILIALVFIYLWYKKKR
>gnl|CDD|275271 TIGR04478, radical_SAM_superfamily_domain_protein, radical SAM/CxCxxxxC motif protein YfkAB. Members of this highly conserved family in some Firmicutes have an N-terminal radical SAM domain (pfam04055) and a C-terminal pfam08756 domain with a CxCxxxxC motif that suggests binding to an additional metallocluster. It appears all correct sequences in this family are about 370 amino acids in length, containing the YfkA and YfkB regions originally reported as separate ORFs in Bacillus subtilis. Partial Phylogenetic Profiling shows occurrences almost exclusively in the Bacilli, with very few examples of either lateral transfer or gene loss. The essentially monophyletic distribution suggests a housekeeping function. Members have no well-conserved gene neighborhood. The function is unknown [Unknown function, Enzymes of unknown specificity]
QPISPHYDPWEAYRDLEEHGEHRLTSVEFTVTNLCNMRCEHCAVGYTLQPKDPERLPLDLILRRLDEVEH
LRTLSITGGEPMFSKKSVRNYVVPLLKYAKERGIRTQINSNLTLDLDRYELIAPYLDVMHISHNYGTVED
FAEIGFARMDRKPSFEAAAKLFERMIENARALSEAGVFVSAETMINKRTLPHLGKIHRLIVEMGCQRHEV
HPMYPSDFASNLPVLSLDETREAIHRLLDVRDEDLWMLFGTLPFYACSPDEEDRELLRRLRSEPNVTVRN
DPDGRNRLNVNIFTGDVIVTDFGDVPPLGNIQTDRLDDAFDRWQDHPLNKSLNCHCPAVGCLGPNLLVKN
AYYPGVDFRKRKA
>gnl|CDD|275272 TIGR04479, bcpD_PhpK_rSAM, radical SAM P-methyltransferase, PhpK family. Characterized members of this family are B12-binding domain/radical SAM domain enzymes that use methylcobalamin as a methyl donor to methylate a phosphorous atom during the biosynthesis of natural products such as bialaphos and phosalacine. These syntheses create an extremely rare C-P-C bond. All members of the seed alignment derive from genomic regions that include a non-ribosomal peptide synthase. Note that a single organism, Pelosinus fermentans JBW45 from Cr(VI)-contaminated groundwater, has eight additional homologs of unknown function that score between trusted and noise cutoffs of this model [Cellular processes, Toxin production and resistance]
KDCLIIGFNDGDFDDYVKMLERVGDESPAYRDMRLNFVVVNGQRYPALDALSELRTNSTGAHRDYHNADL
LWLAVLYLGTYLRRHGFSADYVNLFQDEKDKLAELLASNNPNTVAITTTFYVMPAPVIEIVDFIREHNPS
AHIIVGGPFIDNQCKAGDTDELQDLFDYIGADIYINSSQGEDALAQILEALNKGRDLSGVPNIIYRDGKT
WKRTRKEPEYNSLEDCSIDWKLFSPENIGPTVSLRTAKSCPYSCSFCGYPIRAGAYKTLSVDTVEKELDA
IAELGTVKNVVFVDDTFNVPKKRFKDMLRMMIRNDYGFKWNSFFRCDHADDETIDLMAESGCEGVFLGIE
SGNDQMLKNMNKTARTSDYRRGISQLKKRGIATHASFIVGFPGETEKTVQETIDFINEAKPDFYRAQVWY
CDPATPIWKNREAYGLEGNGYSWSHATMDSEEAADLTEEFFLRVTNSTWLPQYGFDFWSLFYLLGQGMEI
SEVKSFLKLFNDVV
>gnl|CDD|275273 TIGR04480, D-proline_reductase_PrdA_proprotein, D-proline reductase (dithiol), PrdA proprotein. Members of this family are the PrdA proprotein. The polypeptide undergoes an autocatalytic cleavage that creates two subunits, one with a Cys-derived pyruvoyl motiety critical for activity. The D-proline reductase complex also contains a subunit derived from the prdB gene. The complex acts on D-proline, which may be supplied from L-proline by an active proline racemase encoded nearby
TVETAKEHANDPAVLCCRAEEGTVIGPSNLEDPAIFPDLVDSGLLTIPENVLKIGQVLGAKLIKTIDALT
PLTPDVLEGINAPSEEAEEKVEAAAEAAPAAEAAPVAAPAGPGGVVRIHIGEGKDINLEIPLGVAGAGAV
APAAAAGEAVAVAATEEAKPEGEEKVIRTLKKKHFKIEKVEFGDETKIEGTTLYIREGLCKEALKADELV
KDLKLDIITPDNYHVYSNTIMDVQPIATKEEGELGEGVTRVLDGVVMMLTGTDENGVQIGEFGSSEGELD
ENIMWGRPGAPDKGEIFIKTHVTIKAGTNMERPGPLAAHKACDYITQEIREALKKADDSLVVDEEEIEQV
RRPGKKRVVIVKEIMGQGAMHDNLILPVEPVGVLGAKPNVDLGNVPVVLSPLEVLDGGIHALTCIGPASK
EMSRHYWREPLVEEAAADEEIDLVGVVFVGSPQVNSEKFYVSKRLGMLVEAMDVDGAIVTTEGFGNNHID
FASHIEQIGKRGIPVVGVTYSAVQGALVVGNKYMDAMVDNNKSKGGIENEILGNNTLCKEDAIRALAMLK
TKMAGEEIKAAERKWNPNVKLNNIELI
>gnl|CDD|275274 TIGR04481, hypothetical_protein, proline reductase-associated electron transfer protein PrdC. Members of this family are encoded near the prdA and prdB genes for proteins of the proline reductase complex, are induced by proline, and are designated PrdC by Bouillaut, et al. Some members are selenoproteins (at two different positions), as is PrdB. Members are homologous to, but distinct from, electron transport protein RnfC
YVFLLKQHVGAPSEPVVKVGDKVKRGQLIAKPEGLGANIHSSVSGVVKEITEKAIIIEADEVQPDDYVKI
KKGDTPLELIKEAGIVGLGGAGFPTHVKLNVDLEGGYVIANAAECEPILSHNIKQIEEEPELIIRGLKYA
MEATNASKGIIAIKAKHTKAIEALKEAIKNDDNISIHELPDIYPMGEERAIVREILGKLLDPTQLPSAAN
AVVINVETLARIAEAVEDKKPVIDKDITVAGKLKEGNKPQVFMDVPIGTSVGDLIERAGGIDGEYGEIIM
GGPFTGKSTTLDAPITKTTGGIIVTEPFPNGPRKMGLLVCACGANEARLREIAKKMGAEVVGVEKCKQAV
EVKGTLKCENPGNCPGQAQKVLKLKKAGAEVLLISNCTDCTNTVMGVAPKLKLPVYHQTDHVLRTVGHKL
IRRLK
>gnl|CDD|275275 TIGR04482, D_pro_red_PrdD, proline reductase cluster protein PrdD. Members of this family are PrdD, encoded in the proline reductase gene cluster. Members are closely homologous to PrdA, which cleaves during maturation to create two subunits of the subunits of the proline reductase complex, one of which has a Cys-derived pyruvoyl active site
RRLVIKAFHVEEVVFGDKTKITKGVLTIPKSILDELLEKEELIKSIDIRIIKPDEHDIEVNSIMDIIPIS
TKVLGKLGEGITHTLTGVYVMLTGADEDGIQLHEFGSSEGILKEQIVFGRAGTPSEDDYIISFDVTLKAG
KGFDREGPTAAHRLCDDFIQEIREYLKKLDGRYCTEKHEYYDKVRPGKKKVVIVKQVAGQGAMYDNQLFP
KEPSGFIGGKSIIDMGNMPILLTPNEYRDGAIRAMV
>gnl|CDD|275276 TIGR04483, D_pro_red_PrdB, D-proline reductase (dithiol), PrdB protein. Members of this family form the PrdB subunit, usually a selenoprotein, in the D-proline reductase complex. The usual pathway is conversion of L-protein to D-proline by a racemase, then use of D-proline as an electron acceptor coupled to ATP generation under anaerobic conditions
TTAKGLKSEIFVPITPPPVWTPLKKPLSECKVAFATAGGVHLKSQKPFNTAGDFSYREIPSDTPSSELMV
THGGFDNSDVNKDVNAMFPIDRLHELAEEGFIGSVAPTLIGFMGGGGNVQKFREETGPEIAKILKEEGVD
IVLLTGGCGTCHRSATIVQRAIEEAGISTIIIAALPPIAKQQGAPRITAPHVPIGSNAGEPNNVEMQTAI
LKDTLEAMEEMTSFGQMKTLPYEYRHNV
>gnl|CDD|275277 TIGR04484, sulfur_oxidation_protein_SoxA, sulfur oxidation c-type cytochrome SoxA. Members of this family are SoxA, a c-type cytochrome with a CxxCH motif, part of a heterodimer with SoxX. SoxXA, SoxYZ, and SoxB contribute to thiosulfate oxidation to sulfate
PGELAVEDGEELWNTPFGPKGKSLASCLGLGPGVLKGAAAQYPRYDEDTGKVVTLEQRINACREANQGEK
PLKVKSGEMEALTAYIASQSRGMPINVKIDHPRAKAAYELGKELFYTRRGQLDLSCASCHVQNAGKRLRA
QPLSPLLGHTTHWPAYRLKWGELGTLQRRFRGCMKQVRAPPPKYGSDEMVALELYLAYMANGLPIEGPGV
R
>gnl|CDD|275278 TIGR04485, monoheme_cytochrome_c_SoxX, sulfur oxidation c-type cytochrome SoxX. Members of this family are SoxX, a c-type cytochrome with a CxxCH motif, part of a heterodimer with SoxA. SoxXA, SoxYZ, and SoxB contribute to thiosulfate oxidation to sulfate
SKGNCLACHQIPGSEVFPGNIGPSLTGYGARYPDEAYLRAKIADAKAVNPCTVMPRFGKNGILTEQEIED
VVAYLLTL
>gnl|CDD|275279 TIGR04486, Sulfur_oxidation_protein_SoxB, thiosulfohydrolase SoxB. SoxB, a di-manganese(II) enzyme, works with SoxYZ and the c-type cytochrome SoxXA in oxidation of thiosulfate to sulfate
SRREFLQLLAAAGAAGLGLPRAARAARLTPEDLYDFPPFGNVTLLHITDCHAQLKPIYFREPSVNLGVGP
AEGRPPHLVGEAFLKYYGIKPGTLEAYALTYLDFEELARRYGKMGGFAHLATLVKRIRAERGGDKVLLLD
GGDTWQGSGTSLWTRGQDMVDAMNLLGVDVMTGHWEFTYGQERVKELVEKLKGEFLAQNVFDADFGDPVF
KPYVIKERGGVKVAVIGQAFPYTPIANPRRFTPDWSFGIREEELQKLVDELRAKGADAVVLLSHNGMDVD
LKLASRVKGIDVILGGHTHDAVPQPVRVGNTLVTNAGSNGKFLGRLDLDVKKGKVKDFRYRLLPVFSNLL
PADPEMAALIEKVRAPYEAKLSEVLAVTESLLYRRGNFNGTFDQLICDALRAERDAEIAFSPGFRWGTTL
LPGQAITMEDVLDQTAITYPEVYVFEMTGEQIKAVLEDVADNLFNPDPYYQQGGDMVRVGGLSYTIDPGA
PMGKRISDMTLGGKPLDAAKSYKVAGWASVGEAAEGPPVWDVVAEYLRDKKTVKIRPNNNVKVKGV
>gnl|CDD|275280 TIGR04487, SoxY_para_1, SoxY-related AACIE arm protein. Members of this family are paralogs to the authentic thiosulfate oxidation system protein SoxY. True SoxY end with the sequence GGCG(G), the swinging arm in which the Cys residue covalently binds the inorganic sulfur moiety. In this family, members end with a different swinging arm sequence [AS]AC[IVT]E. The few species with a member of this family always have authentic SoxY
NRRQLLLAGGAGLLALAWVRPARAFAPKLAAAIREFTGGASVQDGRVTLDIPPLVENGNAVPLTVSVDSP
MTADDHVKSIAVFNEKNPQPNVATFHLGPRAGRATVTTRIRLADSQTVVAIAEMSDGSFWSASADVIVTL
AACTE
>gnl|CDD|275281 TIGR04488, sulfur_oxidation_protein_SoxY, thiosulfate oxidation carrier protein SoxY. Members of this family are bona fide SoxY, the sulfate carrier protein with the GGCGG ir GGCG swinging arm C-terminal sequence. The Cys in the swinging arm is the residue to which the inorganic sulfate moiety becomes covalently attached. In some species, a closely related paralog occurs as well (TIGR04487), with a swinging arm sequence AACIE. More distantly related forms have an additional C-terminal SoxZ-related domain. All members are periplasmic and have an N-terminal twin-arginine translocation (TAT) signal sequence
TRRRFLKLAAGAAAAAAAAGPSVAFAAWNKKAFDAKSLEDALKALTGGKTPAESKDIKLKAPEIAENGAV
VPVTVSVDLPGVKSIAILAEKNPNPLVATFELPAGGEPYVSTRIKMAQTSNVRAVAVMADGKLYSASKEV
KVTIGGCG
>gnl|CDD|275282 TIGR04489, exosort_XrtO, exosortase O. Members of this protein are a variant form of exosortase, XrtO, with a dedicated target typically encoded by the adjacent gene. Members have a unique C-terminal extension very different from EpsI (TIGR02914), the extension that many exosortases have. The targets of XrtO all are members of family TIGR02921, which describes a PEP-CTERM protein about 950 residues long, found in more than 15 genera so far. These PEP-CTERM proteins are unusually hydrophobic in stretches, suggesting an integral membrane location, which is unusual. About one third of the members of TIGR02921 are in genomes with this protein, exosortase O, always encoded by an adjacent gene. Genomes include Synechocystis sp. PCC 7509, Xenococcus sp. PCC 7305,Pleurocapsa sp. PCC 7327, Microcoleus vaginatus, Hahella chejuensis, Vibrio azureus NBRC 104587, etc
WLFANYLTVQWLLSSVREPSALNLIIIGIVVTGLLVQAIRRSPPLHLSLTPVLRALPLALMLGSAIASIA
LQWIIDIPQLSVTLFILGSYGLLGLFVAPALWRKGLPIAALLACALPFSLQFNSGLGFPVRVLTARLVEQ
LLSALGVSALSSHDIILLENGIAQVDLPCSGLKSLWVGTLFLLAATWLEGRQLSWRWLLVLIANILLLIS
ANAVRILALVLLSEVLNQPQIAEILHLPLGILGFVLACLLTWLLLQLVPKTSSEKRAESPSQPASQKNQK
SLEPWIIVGVCVLALILQTPHPKPASALSIASLPLPPQISTESISLSPIEQDFFNNYAGTVAQKLRFEWR
GLSGSMLLVASRSWQAHHAPELCFLGSGVKVDDMKTKQLSPHVHGRWLSLNQGARSATYWFQSAQRTTDD
FLSRIWSAITHKEKSWVMVSVLFDSSISPD
>gnl|CDD|275283 TIGR04490, sulfur_oxidation_protein_SoxZ, thiosulfate oxidation carrier complex protein SoxZ. SoxZ forms a heterodimer with SoxY, the subunit that forms a covalent bond with a sulfur moiety during thiosulfate oxidation to sulfate. Note that virtually all proteins that have a SoxY domain fused to a SoxZ domain are functionally distinct and not involved in thiosulfate oxidation
AKKKGDVVEVKALISHPMETGLRKDKKTGKLIPAHFINEVTVKLNGKVVFTADWGPSVSKNPYFAFKFKG
AKAGDTLTVTWKDNKGETDSATAKI
>gnl|CDD|275284 TIGR04491, dehydratase_reactivation_factor_large_subunit, diol dehydratase reactivase alpha subunit. Members of this family are the alpha (large) subunit of the alpha-2/beta-2 tetrameric enzyme that reactivates B12-dependent trimeric diol dehydratases (1,2-propanediol dehydratase, glycerol dehydratase). Note that the beta subunit of the reactivase is homologous to the beta (medium) subunit of the diol dehydratase. The reactivase catalyzes the exchange of chemically inactivated B-12 for active B12. This model excludes homologs from Mycobacterium (e.g. M. smegmatis), where the several paralogous forms of the dehydratase occur and are exceptional also by not being found in a carboxysome-like microcompartment
LIAGVDIGNSTTEVAIAEVDGGEVRFLSSALVKTTGIKGTVDNVAGILAALKQALAKIGRSISDLDLIRL
NEATPVIGDVAMETITETIITESTMIGHNPSTPGGVGLGVGTTILLDDLGNAAPGEPYIVVIPKSVDFED
AAEIINEAFDRGVNVKGAILQKDDGVLINNRLRKKIPIVDEVSLIDKVPLGMLAAVEVAPPGRTIRTLSN
PYGIATLFDLSPEETKQIVPIARALIGNRSAVVIKTPKGDVKERVIPAGKITISGNRRSAEVDVDEGAEA
IMEAVESVGPIEDIEGEPGTNVGGMLERVRQTMADLTGQPISEIKIQDLLAVDTFVPQKVQGGLAGEFSM
ENAVGLAAMVKTDKLPMQAIAEKLEEELGVKVEIGGVEAEMAILGALTTPGTDLPLAILDMGGGSTDAAI
IDEDGKVKSVHLAGAGDMVTLLINSELGLDDRELAEDIKKYPLAKVESLFHIRHEDGTVQFFEEPLDPRL
FARVVILKEDGMIPIPLDHSLEKIRQVRREAKRKVFVTNALRALEQVAPTGNIRDIDFVVLVGGSALDFE
IPEMITDALSEYGVVAGRGNIRGTEGPRNAVATGLVLS
>gnl|CDD|275285 TIGR04492, polyketide_synthase, iminophenyl-pyruvate dimer synthase VioB. Following the action of a flavin-dependent L-amino acid oxidase that converts L-tryptophan to indole-3-pyruvate imine, the enzymes VioB (this family), RebD, and StaD can ligate two molecules, forming a coupled iminophenyl-pyruvate dimer. In the violacein biosynthesis pathway, this compound is acted on by VioE before it cyclizes spontaneously to chromopyrrolic acid. In the pathways of homolog StaD (staurosporine), chromopyrrolate is formed, and the enzyme is referred to as chromopyrrolate synthase. RebD is very similar to StaD, but acts on chlorinated Trp-derived molecules [Cellular processes, Biosynthesis of natural products]
MSILDFPRLHFRGFARVNVPTANRNTHGHIDITTNTVLMAGAPFDLKRHPSEFHAHLKALEPRFNAQGRP
DPEGQFNHAAGYNAIGNNHFSWENTRVTGVQLKEGSVDTGDPLVGAKLALWGHYNDYLRTTFNRARWVDN
DPTRRDTALIYAGQLTISDGDAGPHTPSLLSADIDCAHGVRWLRPGHIVERGGHFLDEEFGRARLFQFSV
SKDNAHFLFNSLNIDSAFLRALQQALEDEEVLGLTVQYALFNMSTPSQPDTPVFYDLVGTIGLWRRQELA
TYPAGRLLLPRQSGLGPVAVKVKDDRVSLNMPTAIPFTTRAAVPVSQQHLTPKLGHKQALGDLILRDDSG
ALLAVIPEALYQDYWRHHGVVDVPLLVQLATGSLSLQSELANWHETDWVIQSDSNILYLEAPNRKKGLFF
PETITVQSYFRGELAPIPALIPRIEDPNNLRLDLYISTQGSGYAQLRLTGLRPGSTRIVLGDGHSPIQVR
ILPDDWHLDDVPAEQVDYAFLYRHVMSYYELLYPFMADKVFSLADRCKCETYARLMWQMCDPQNRDKSYY
MPSTRELSSPKSRLFLKYLSHVEGSARTKEPPQRGPQPSIKSKAQLVAELRKAVDLELSLMLQYLYAAYS
IPNYAQGEQYVRSGRWTAEQLELACGSKDRRRNSGWRGALLEIAHEEMIHYLVVNNLLMALGEPFYPGEP
LFGEAARQKFGLDTEFSFEPFSEHVLARFVRFEWPHFLPSPGKSIADFYAEIRQALNDIPDLFTQDMGKR
GGEHHLFLNELTNRAYPAYQLEVFDRDSALFGIDFVTEQGEGAALDSPHFEHSHFQRLRSLSKRFTASDK
PFEPALPALKNPVLEQRAGCNVVTDPNARALMTLYQGCHELMFKMMAQHFAQKPLGSLRRSRLMNAAIDL
MTGLLRPLSVALMNLPSGLAGRNAGPPLPQPIKFKATSDYAKGCRALAQACLELAETARELEAGPVPEAQ
IELLEFYQRQMTDLATGKLSREA
>gnl|CDD|275286 TIGR04493, propanediol_utilization_protein, microcompartment protein PduM. Members of this family are PduM, a protein essential for forming functional microcompartments in which a trimeric B12-dependent enzyme acts as a dehydratase for 1,2-propanediol (Salmonella enterica) or glycerol (Lactobacillus reuteri)
QRIVEEVVARLQQRAQSTATLSVAQLRDAPSRTIFLQNASLRLQQVDLPLLRQLAEMDTSDPAVAWLHEA
LAYGVRVQLSLHRQLLPALPVKMLARLPLTFCDEQGQPVYLHHGRVITYADVARLPDGSLVLRRRQLITA
LAREALSKRNIQL
>gnl|CDD|275287 TIGR04494, cytochrome_c550, cytochrome c-550 PedF. Members of this family are c-type cytochromes with some remote similarity to the sulfur oxidation cytochrome SoxX
AAGALAALLLTGTAWAHGDVTPQAVDTKGLPPLGDEWLEENPYRTGHKEAIRIGASAYNQNCARCHGLEA
ISGGIAPDLRKLDAGEDGDEWFVERVRHGAVRDGRVYMPPFEGILSQEALWAIRTYLETVHVE
>gnl|CDD|275288 TIGR04495, RiPP_XyeA, putative rSAM-modified RiPP, XyeA family. Members of this family are short polypeptides with a conserved GG motif as found in bacteriocins that are cleaved upon export. Each gene occurs immediately upstream of a gene for a peptide-modifying radical SAM/SPASM domain protein. The system is designated Xye for genera Xenorhabdus, Yersinia, and Erwinia, hence XyeA for the precursor peptide. The vicinity will also contain a transport protein with a C39 family peptidase domain (see pfam03412), characteristic of GG motif cleave-on-export systems. The function of this RiPP family is unknown
SRLKKEITETKTVIDVSDAKKNQPQHLAEDVLEQIAGGAGWINAFANWTRSF
>gnl|CDD|275289 TIGR04496, rSAM_XyeB, radical SAM/SPASM domain peptide maturase, XyeB family. Members of this family are radical SAM/SPASM domain enzymes associated with maturation of the XyeA family of GG-motif containing RiPP (Ribosomally synthesized, Post-translationally modified Peptide) natural products
IKHLEIILKISERCNINCDYCYVFNKGNSLADDSPARISNKNIHALVGFLQRACAEYDIETIQIDFHGGE
PLLMKKENFDNMCDQLTQGNYCGSNIELALQTNGTLIDDEWIALFEKYSVHVSISIDGPKHINDRHRLDT
KGRSTYEGTVRGLRMLQNAYQQGRLPGEPGILCVANAQANGAEIYRHFVDELGVYSFDFLIPDDHYDDAH
SDAVGIGRFLNEALDEWFKDGNPKIFVRLFQTHIATLLGQKFSGVLGHTPNVTGAYAFTVTSDGLLRVDD
TLRSTSDEIFNAIGHLSELNLSNVLNSPQFQEYLSIGSSLPTECAGCIWENICAGGRIVNRFSRENRFNR
KSVYCYSMRLFLSRASAHLLNMGIDEERIMKNIQK
>gnl|CDD|275290 TIGR04497, GRASP_targ_2, putative ATP-grasp target RiPP. Members of this small family are putative RiPP (Ribosomally translated, Post-translationally modified Peptides) precursors, modified by RimK-like ATP-grasp proteins. Members are encoded near both an ATP-grasp protein and C39 peptidase domain-containing transporter. Members are short polypeptides that contain the GG motif expected for cleavage on export
RNTVITDIPAEGAELSEAELAEVGGGRRKEWRSSKTIDDVPGWWGT
>gnl|CDD|275291 TIGR04498, hypothetical_protein_X730_20110, abortive infection protein, AbiV family. This family includes AbiV (abortive infection system V) from Lactococcus lactis, a phage resistance protein that causes certain phage infections to fail to lead to successful phage replication. Abortive infection mechanisms differ greatly. AbiV interacts directly with the protein SaV in phage p2 and blocks translation of phage proteins
EGMNAALDNARRLLEDAELLLENGSYARAYFLAILAIEEIGKASILRDALLGGDEVDWKKLKKRLRNHKK
KNKLALPSLVLVGARLLEDFREAVDFAEDAPKGLNNLKNNSLYVDCDDGGFSSPSEVIDKELAEELLLLA
I
>gnl|CDD|275292 TIGR04499, abortive_AbiA, abortive infection protein, AbiA family. Members of this protein family average about 650 amino acids in length, with an N-terminal region related to reverse transcriptases. The only characterized member is AbiA, with reported activity as an abortive infection protein for phage defense in Lactococcus lactis and (heterologously) in Streptococcus thermophilus
FFISYKDWKDACKMYFKLSQGSLNKYLQWFPFSKLTEQDKEYLLSEKFFQKYIKNGAFFGYQEEFGVYDN
YIQKTDGSFRDSKLVSPVLYLYLQAIGKEISKKYVRKRERDISAYYAGNLLENTAYYKSSYDEFFKEINA
YAEEYKYFIKTDISNFFSNIDIDKLLNKIDININEESMRFDPKQLLQIKELLQYIGQGKFPLVENSIASS
FLATIVYLDDIDLILDDYIKKKIKEIESFKIIRYVDDLYIFINSKESINDLDQIYNSIRNEYSSILKKYG
LALNTKKTYLKESSELKEELKKSLYNESVNDEYIDIEDYFDKNTPLEFLDSLFNELLKYKLDFEEYKKII
DISFSSDDIESTPDEILNSIVYDKSELLQDPEIINKISSLINFNYDFVKVDPKRLTIMILKTRNGDLIKA
LLNQLFTKNKNGTWNIYDTVIAIKYLLQRNFSHKDLLKKLKANDHNLKDYIDYYCTGSFLKSLPKNNINF
YIKLTGVDWKLYYLYFMYIIEQKKLNVLEEFAYYKNYFDRLTAEIAFYLNIDKKNKPKYKAYYKKDALKK
LYSKFVPDEICIIIRKAHDLRNSNPLSHSSAELLIDWDVTKEEIKQSINDLGKLL
>gnl|CDD|275293 TIGR04500, PpiC_rel_mature, putative peptide maturation system protein. Members of this protein family have a novel N-terminal sequence region. Close homologs to the C-terminal region of this protein score well to PpiC-type peptidyl-prolyl cis-trans isomerase models (see pfam00639), yet no sequence within the family scores well to such models, suggesting origin within a branch of the PpiC family but subsequent neofunctionalization with a rapid change of sequence. The genome context for members always includes an ATP-grasp enzyme associated with peptide modification and a short polypeptide likely to be the modification target
ALEDAVGLLRRLDPGAAGAERALEDLRARHPGVRARLVRHREAGDPSVHFGLLIDHPGGGTVTLSWPPER
AVPWLLRGSQRWAESMLLRVNGVHLSVSQALTYLDVLWEETALLDRLVAQCLVRQELEEDPVPLSAAELQ
EAMDAFRRARGLLTPAATLAWMAARGLSHQALEELVEREAAVARLRARVEAERVPGWFAAHRADFDRVRI
ARVRFAERVAAEGAVELWRTRIQDCDRLAYAAGAAAAFAVASATVGEVFQTWLRTDRELELPEALFGAAP
GTVLGPVPLAGGWLLVKVLSRTAAEDDPETLAAAGRRAFGRWLAERRASARIEWFWG
>gnl|CDD|275294 TIGR04501, propanediol_utilization_protein_PduB, microcompartment protein PduB. Members of this family are PduB, a protein of bacterial microcompartments for coenzyme B(12)-dependent utilization of 1,2-propanediol (hence pdu) or glycerol. The most closely related protein in ethanolamine utilization microcompartments is EutL (TIGR04502)
TEFVGTAIGDTIGLVIANVDSQLHEAMGLDKKYRSIGIISARTGAGPQIMAADEAVKATNTEVVSIELPR
DTKGGAGHGSLIIFGAEDVSDVRRAVEVALKELDRTFGDVYGNDAGHLEFQYTARASYALNKAFGAPVGK
AFGLIVGAPAAIGVVMADTAVKSANVEVVGYASPGHGTSFSNEVIITISGDSGAVRQAVIAAREVGLKLL
GAMGSEPKSPTTPYI
>gnl|CDD|275295 TIGR04502, ethanolamine_utilization_protein_EutL, microcompartment protein EutL. Members of this family are EutL, a protein of bacterial microcompartments for ethanolamine utilization (eut). The most closely related protein in microcompartments for utilization of 1,2-propanediol (hence pdu) or glycerol is PduB (TIGR04501)
DPIRANVLAVRIIPNVDPALAEKLNLKPHHRSLGLITADIDDVTYTALDEATKKADVDVVYAKSFYAGAA
HASGPLSGEVIGILAGPSPAEVRSGLDAAIDFIENGAYFYSANEDGSIAYFAHTVSRTGSYLSKEAGIEE
GEALAYLIAPPLEAMYGLDAALKAADVELVVFYGPPSETNFGGGLLTGSQSACKAACDAFAEAVLEVARN
PLKY
>gnl|CDD|275296 TIGR04503, mft_etfB, electron transfer flavoprotein, mycofactocin-associated. Members of this small protein family are putative electron transfer flavoproteins, related to FixA from E. coli and EtfB from Methylophilus methylotrophus but clearly forming a distinctive clade. All members occur in species with a mycofactocin system. We have proposed that mycofactocin is a redox carrier synthesized from a ribosomally translated peptide with aid from a radical SAM enzyme, analogous to PQQ
VVVALRWADPRPRVDPLTGEVSADARAAGLSAADEAALEHALRLAEALGGRVVAVTVGPPGAEEMLREAL
ALGADEALRVDRPDERPPDGAAEDEAATARALAAALTAGLGEPDLVLCGDRSADRGTGATPAFLAARLGA
AQALGLVELEVEVNGVGGGSPRLLGVRRLDGGRRERLRVPLPAVCSVEAAGARLRRAPLPAALAAGDAAI
PVVPVPGVAAARPPVRVGSVRPYRPRTRVVPPPQGATAHDRLLALTGALQDREPPTVLGPLSAEEAADEL
LAYLRRHGYL
>gnl|CDD|275297 TIGR04504, SDR_subfam_2, SDR family mycofactocin-dependent oxidoreductase. Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36 [Unknown function, Enzymes of unknown specificity]
GRVALVTGAARGIGAATVRRLAADGWRVVAVDLCADDPAVGYPLATRAELDAVAAACPDQVLPVIADVRD
PAALAAAVALAVERWGRLDAAVAAAGVIAGGRPLWETTDAELDLLLDVNLRGVWNLARAAVPAMLARPDP
RGGRFVAVASAAATRGLPHLAAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAATARLYGL
TDVEEFAGHQLLGRLLEPEEVAAAVAWLCSPASSAVTGSVVHADGGFTG
>gnl|CDD|275298 TIGR04505, phosphate_transporter, phosphate ABC transporter substrate-binding protein. Members of this family are the substrate-binding protein of the phosphate ABC transporter as found in Mollicutes genera such as Mycoplasma, Mesoplasma, and Spiroplasma. The most similar sequences outside this family are PtsS in family TIGR02136, but sequence architecture differs considerably. Members of this family are never lipoproteins
MNKKMSLILTIVLALIISIWIWTFAAANNVIVIGGSTSVDPIMQKLTNQYKRDTKKDFLYNSTGSGAGAV
GVKNGTYSIGFISKDVTSTSIPGDDGENFQQLCNENKEERFNKLENKDSYHFLVFAKDSIVFVYNIPNTG
LTKIDDQLQFIEFNLNDNVNFNEQGTEALKKIYSVNNISWKDFYKQLTGKDEINISNKTKVYTYTRESGS
GTRSSFESLSGIKKKNYKTGQVVNSNGAMFQQITKSPGSFGYVSMSYAQQIKKFGNLRSVIIKDGIKWDD
PEWDINESINEQFEFKDYPLNRPFTAIYNTTGNQLNEILKFIAWMSDS
>gnl|CDD|275299 TIGR04506, fluorothreonine_transaldolase, fluorothreonine transaldolase. Members of this family are fluorothreonine transaldolase, and enzyme involved in biosynthesis of 4-fluorothreonine, one of the few known known naturally occurring organofluorine compounds [Cellular processes, Biosynthesis of natural products]
LSLNAIRELVAQEESESGTVLHLTANETVLSPAAQQVLSSPLVNRYLLEHLDMREDSPSRLNNFLYRGLN
RINAIEQSATEVCRRLFGAEYAEFRCLSGLHAMQTTFAALSQPGDKIMRISTKDGGHFLTELICRSFGRR
SCTYAYRDIMTIDLDRTREIFERERPSLLFVDAMNYLFPFPLAELKEICGDVPLVFDASHTLGLIAGGQF
QDPLGEGADILQANTHKTFFGPQKGIILGRSRSLMERIGYTLSNGMVSSQHTASTLALFIALHEMYYDGR
EYAARVVENARYLAGALHDRGVPVLAADRGFTANHMFFVDTRPLGAGPALLERLLRAGISVNRSVAFEHT
DTLRLGVQEVTRRGYDNADLDEIADWLAALLLRDAEPERIARRVAELVGRRREIRYCGPTAAAAQQPARE
TGHAPAGQLPARPRWIGIMLTPAALRIDRPAYEGARYLGQLAGVFEHQTDSAGNISFQTDGRTFVTASGS
YIKDLAPADFVELTDCTGWTLRCRGDGPPSAESYMHYLLRTRVDAAYVVHNHYIPDDELELIDVLVIPPK
EYGSVALAEAVAKAALQSQIIYVRRHGLVFWSASLEECSALLEKVARRL
>gnl|CDD|275300 TIGR04507, fluorinase, adenosyl-fluoride synthase. Members of this family are fluorinase (adenosyl-fluoride synthase, EC 2.5.1.63), an enzyme involved in the first committed step in the biosynthesis of at least two different organofluorine compounds. Few organofluorine natural products are known. Related enzymes include chlorinases (EC 2.5.1.94) that lack fluorinase activity, although a fluorinase may show chlorinase activity [Cellular processes, Biosynthesis of natural products]
SDLGTTDDSVAQCKGLMLSICPDVTVVDVCHSMTPWDVEEGARYIVDLPRFFPEGTVFATTTYPATGTTT
RSVAVRIKQAAKGGARGQWAGSGAGFERAEGSYIYIAPNNGLLTTVLEEHGYLEAYEVTSPKVIPEQPEP
TFYSREMVAIPSAHLAAGFPLSEVGRRLEDDEIVRFNRPAVEQVGEALVGVVTAIDHPFGNVWTNIHRTD
LEKAGIGYGTRLRLTLDGVLPFEAPLTPTFADAGEIGNIAIYLNSRGYLSLARNAASLAYPYNLKAGLSV
RVEAR
>gnl|CDD|275301 TIGR04508, queE_Cx14CxxC, 7-carboxy-7-deazaguanine synthase, Cx14CxxC type. In the pathway of 7-cyano-7-deazaquanine (preQ0) biosynthesis, the radical SAM enzyme QueE is quite variable. This model describes a variant form in which the three-Cys motif that binds the signature 4Fe-4S cluster takes the form Cx14CxxC, as in Burkholderia multivorans ATCC 17616. The crystal structure is known
YSVKEIFYTLQGEGAQAGRAAVFCRFAGCNLWSGREQDRAKAVCRFCDTDFVGTDGENGGKFADADALAA
HIAALWPGGGATPYVVCTGGEPLLQLDDALIDALHARGFEVAIETNGTLPAPEGIDWICVSPKAGAPLVQ
TSGDELKLVYPQPGLLPELFEALDFEHFLLQPMDGPQRAANTQAAIDYCLAHPRWRLSLQTHKYLGIP
>gnl|CDD|275302 TIGR04509, mod_pep_NH_fam, putative modified peptide. Members of this family average 110 residues in length, with strong N-terminal homology to both the nitrile hydratase (NH) alpha subunit and family TIGR03793 of NH-related ribosomally translated natural product precursors. A neighboring gene resembles SagB, the dehydrogenase of many thiazole and oxazole modified peptide systems, supporting the hypothesis that members of this family are post-translationally modified
PLSPAVADALLDLLSTDDAFRALFQSDPAAALAQLGHAELGAAVVPCCLNGQLASKEEIAAARDQLVAML
TSGAAFTVPFLFEGG
>gnl|CDD|275303 TIGR04510, mod_pep_cyc, putative peptide modification system cyclase. Members of this family show homology to mononucleotidyl cyclases and to tetratricopeptide repeat (TPR) proteins. Members occur in next to two other markers of ribosomal peptide modification systems. One is a dehydrogenase related to SagB proteins from thiazole/oxazole modification systems. The other is the putative precursor, related to the nitrile hydratase-related leader peptide (NHLP) and nitrile hydratase alpha subunit families. These systems occur in many species of Xanthomonas and Stenotrophomonas, among others
HAPQLRTLLFTDLCDSLALVERIGDAAAAELFQEHDRLVLALQQRWRGRLIDRSDGLLLLFERPIDALGF
ALDYQRGLQPLGQARKLELRARAGLHVGEVLTWENSDEAVRVGAKPLEVEGLAKPTAARLMTLARPGQIL
LSAVAESLTHRAARELGERGERLLWKSHGRWRFKGVPTPMEVYEVGEIGFAPLRMPRPNAKARRDLPLWR
RPAALAAEALLVLAAGLGLWLLLRPEPAIAFAERDWVVVGDVRNLTGNVVLDDSLDQAFRISLEQSRYVN
VLSDMKVRDTLTRMRRDPDTTLDRATASEVALRDGARAVLLPSVSEVGGRLRVSVEVVDPATQQTVYVES
ADGRGLESVLASVDDVTGQLRERLGEALASIRRNSKPLPQVTTSSLDALRAYALGQEAYGQGDFREALAL
FQRAVEIDPDFALAYLGQARAHFANSDYADARPLLAKAQRLRGRLPARERLYLDAWAAELGDPGAALEAW
KQLARLYPDYFAAQANAAWALFVANRYADALPYARAAAVSQNPLRSIALDLLGRIQLAQGKYAQALRAFE
RAALLGGGGALRRLAAVLAAQGDYAEADAVLARLDKNGFANRLERTSIALDQGKWEAARAAAAAAAAAAG
QAAPFDRRLYGVVQLAVRAATGRRAAAADVARLAATALLAALQADNPDEPDRGDRLVAALAAAYLAQRLG
DDALAARVLAQLGVLALASGDPALAQLRAVVDAEQLLLSGDPEAAIALLVPTLDGSELFQVRVALRRALL
AAGRKADALRQADWLRDHRGRAYAEAACSYCLQALNVVDSRLAS
>gnl|CDD|275304 TIGR04511, SagB_rel_DH_2, putative peptide maturation dehydrogenase. Members resemble the peptide maturation dehydrogenase SagB of thiazole and oxazole modification systems, and occur in a what appears to be a new type of peptide modification system. One adjacent marker is a new type of nitrile hydratase alpha subunit-related putative precursor, TIGR04509, distantly related the NHLP leader peptide family TIGR03793. Another is a large protein, TIGR04510, with regions similar to adenylate cyclases and TPR proteins
IRRCAVLFLEPREDVDFDLAALLAGGSGLVRSLRWLALAPHLDQEVEVDAAARALLGALSAERWQAREPE
EDAGAAALARLLEAGLLLADEQAADAALRARDERLRAAHWWPLAALAHRFSRWQGVDSVAAMEGHGLPTA
AGLRERLGPPPPEVAERGDVGAAVPLPVPEPDAFDALLARRATCRNFDTARVLPLALLARLLQRVFGAQG
RVEVGPDAVFLKKNSPSGGGLHPVEAYLLVQRVDGLAPGLYHYHPVAHALEPLPAPPAPLADFALRMVAG
QHWFADAPVLVVLAPRFDRNFWKYRNHAKAYRAVTLDAGHLSQTLYLAATEAGLGAFVTAAINEIDIERA
LGLDPLREGVLAVCGFGWRAQQMTTAELDP
>gnl|CDD|275305 TIGR04512, hypothetical_protein_MMCAP2_0033, STREFT protein. Members of this family occur strictly in the genus Mycoplasma, average 1050 in length with little length variability, have an N-terminal signal sequence, and exhibit no detectable sequence similarity to any characterized protein. Up to four tandem copies occur in some Mycoplasma (e.g. M. putrefaciens KS1). Incorrect inclusion of a 57-amino acid stretch of one family member in pfam08178, for a helix-turn-helix transcriptional regulator in several E. coli phage, has caused many members of this family to be annotated, in error, as GnsA/GnsB family proteins. We suggest the name STREFT (Secreted Thousand Residue Frequently Tandem) protein as a distinctive name to spread and replace the incorrect GnsA/GnsB designation [Unknown function, General]
LKFLKNNKKWYIIILVLLVFISSFLGFIKSYVDSKKQKLVNKIQNYVQASSYAVRSKILKDTEGLNEDYV
NQKLANKKILDEFGSDFIWKPNNSKTTSTDTISDLLKTYFGKSTDLFTKNLQYQYKKDNNKLKDIENSKN
GEITPKNIDFLISISKSAEKFLNGFSPSLASLGLSLLQNNVLKNRDDPNFIKNNDGLKKFVDYIENNQNL
FSYLGKILIPKSLDKSFYKNLTVKQAFNKNINQISSVITNKKEFNHDVDKLPEDLDKLLWELILDIIKEE
FAKLDKKNIIDKIKNIFNKIKNKFNKKNFLDKILPALARYLKSELFFGLYYVVNEKLKNPSQLLDQKVDD
SKFKALTNNKLDLGVLLNGLSKVLKDKKSFNRFLDFIFKRFDKSKIYFDSNNIPSNIGTGNLIFDLINWV
QKKLLNTSNLLKTVIPFIEEYIALNKEKIKKTITEKITSFLKKKLPGGNVNLGWWKPEFDNGKLEISIQY
KGWLTWLNVADGHINFFGKNGLITNLINILKSIISSISDISSTISNYIKHIFYRDKEQSFDFKKAFENLS
NLIKIFNNLLEDQYILNINLEIGNLVIFLKNIAKIKSIYDILNLPNASLYNTPFLGSLIKKFAGKKIKPY
LKPIKNILEKLKKYKFITDTKKFREQFPKYLKKLIKFIEKYENNAIPKYDLIDNLYTGDGNFITDFTKKW
ADFLVPDITDKDNPLLPIVRAITKDPNEKIESLADIKNAITSKGAKLIKKIAFFKNISKIRNIKIPLPKE
LLKHLGLENLNDLTITELLEQIGKYILDYLKKNPNKVIGFNISSIGKILKALTIKVTVTYKKKNNKKDKD
KNILKALADSLDSHDNKNDENNDIRPKESYYNWDKIEFKLDGKDKPTIDRKILKIDSSYSPLHMLLGINP
DKTKYIKGSIGYSLGTLIGGLNANDPNYNLSIENKNSVISILNAFNYVLDKKQKELKKKEYQIAGQYYDK
NAWTTKLISSNDNEIKYQLIRTKTSNNDESKKIGKRFEVTLTKNKNNSYWKISQIIALDYK
>gnl|CDD|275306 TIGR04513, VPAMP_CTERM, VPAMP-CTERM protein sorting domain. This domain is found as the extreme C-terminal region of four extracellular protein (mostly protease) precursor sequences in Chthoniobacter flavus Ellin428, first representative sequenced from the Spartobacteria class of phylum Verrucomicrobia. This domain contains the cognate signal for one four exosortase family enzymes in the C. flavus genome, and coexists with the more common PEP-CTERM domain, found on more than 50 proteins
VPAMPGWGYIVLGALLVLVAARFLPRTG
>gnl|CDD|275307 TIGR04514, hypothetical_conserved_protein, GWxTD domain. This domain, about 100 amino acids long, occurs in Actinobacteria and other little-studied Gram-negative bacteria, Sec-dependent proteins 300-800 in length. The domain is rich in aromatic residues, with Trp, Tyr, or Phe as the majority amino acid in ten of the twenty-four most-conserved residue positions
ELIEPLRYIITSEERKELLKLSDEERKKFIDQFWLKRDPTPGTPANELIEEYYRRVEYANKLFSSYKEGW
KTDRGMIYILYGPPDEIERHPFSTDTYPYEIWYYY
>gnl|CDD|275308 TIGR04515, cytochrome_P450_monooxygenase, P450-derived glycosyltranferase activator. Members of this family resemble cytochrome P450 by homolog, but lack a critical heme-binding Cys residue. Members in general are encoded next to a glycosyltransferase gene in a natural products biosynthesis cluster, physically interact with it, and help the glycosyltransferase achieve high specificity while retaining high activity. Many members of this family assist in the attachment of a sugar moiety to a natural product such as a polyketide
LGRRLQTLRGLQWLHGAKGDPYALLLRGEDDDPHPLYERIRERGPLWRSSTGAWVTADHAVAAAVLADPR
FGARHPDGGPPAEPVLPLDGAFLGLDRADYERLGRLAAPALGAAAADAARAAVERVCARLLAGLGGRFDL
VADVARPVAVEALAALLGLPAADRDRFAEALAAAAPALDALLCPQRLATARALLAAVAELRALLAELPAR
PGGTPGLAAALLLAVVGVEVAANLVANAVLALLDHPGQWARLRADPGLAAAAVEETLRHAPPVRLESRVA
REDLELAGQRIPAGDHVVVLVAAANRDPAVFADPDRFDPDRPDAAAPLALLPGLPGGLVAPLVRAQAEAA
LRALAARLPGLRPAGPVLRRRRSPVTGGLLRLPV
>gnl|CDD|275309 TIGR04516, probable_glycosyltransferase, glycosyltransferase, activator-dependent family. Many biosynthesis clusters for secondary metabolites feature a glycosyltransferase gene next to a P450 homolog, often with the P450 lacking a critical heme-binding Cys. These P540-derived sequences seem to be allosteric activators of glycosyltransferases such as the member of this family. This model describes a set of related glycosyltransferases, many of which can be recognized as activator-dependent from genomic context
MRVLFTSFAHNTHFHGLVPLAWALRAAGHEVRVASQPALTDAITGAGLTAVPVGEDHDLDELLAEVGGDL
LPYHRDFDFTEKRPERLTWEYLLGMETVLTSAFYALINNDSMIDDLVAFARSWRPDLVIWEPFTFAGAVA
ARATGAAHARLLWGPDLIGRARRAFLALLAGQPPEHREDPLAEWLTWTLERYGCTFDEELVTGQWTIDPM
PASLRLDLGLPTVPMRYVPYNGPSVVPDWLREPPERPRVCLTLGVSARETMGGDGVSVGELLDALADLDA
EVVATLDAAQRELLGPVPDNVRLVDFVPLDALLPTCAAIVHHGGAGTWATAAAHGVPQIILPDLWDAVVR
AQRLEALGAGLALPPAELTAERLRDAVVRVLDEPSFRAGAARLRAEMLAEPSPAEVVPVLERLTARHR
>gnl|CDD|275310 TIGR04517, hypothetical_protein_RLEG3_02865, radical SAM family RiPP maturation amino acid epimerase. This model describes PoyD and its homologs. These are divergent putative radical SAM enzymes, with the classical CxxxCxxC motif but with few members approaching the cutoff score of pfam04055. PoyD appears responsible for catalyzing a unidirectional L-to-D epimerization of 18 the 48 residues in the core peptide of the first characterized polytheonamide. The RiPP (ribosomally translated natural product) precursor, and peptides encoded near many other members of this family, belong to the nitrile hydratase leader peptide (NHLP) family
VAHIKRFLERWTADPDFRSALLQNPRETLAEYGLEVDPEEVRPLWDAEYLKYKKEKEIELPPLLKLWREF
IEEKLRHRDRLRAEASSPADPRFRAWRERQIARCNSELGKERNDSIVHPPVAFELSKGCSVGCWFCGLSA
PRLSGVFRYSPENARLWRGVLEVLKEILGPAAGTGFCYWATDPLDNPDYEKFLADFHEILGALPQTTTAA
PLKDPERTRRLLKLSREYGRVVNRFSVLSLKMLRRIHAEFSPEELLGVELILQNKESLIVKARAGRAWEA
RLREISNGEEGVALSDEQGTIACVSGFLVNMVERSVKLISPCNASERWPLGYRVYDEGSFETADDLRELL
ERMIEKHMPESIPPDDLIRFRRDLKYEELEDGFQLTSRAKKIRFEDDPALAELGELIAKGDKTAAEIAAL
LVYKGVSALETMGALNNLFKKGLLD
>gnl|CDD|275311 TIGR04518, conserved_hypothetical_protein, ECF transporter S component, folate family. Members of this model are the multiple membrane-spanning S (specificity) component of ECF (energy coupling factor) type uptake transporters. All seed members were found in the vicinity of the bifunctional enzyme folC, involved in making active cofactor from imported folate. However, some species have multiple members of this family, suggesting some diversity of function [Transport and binding proteins, Unknown substrate]
KFTVKNLTILALLVALSIILSRFLSIQTGNLRISFGFLPVILAGMLFGPVAGAIVGAVADLLGCMLFGYG
TFFPGFTLSAALTGLIYGLFFYKKKNKKLFLRLAAAVVIVQIIISLVLTSIWLSILYGSPLTALLPIRLI
KAIIMIPVEIVVIYLLLKNLAK
>gnl|CDD|275312 TIGR04519, oxidoreductase_iron-sulfur_binding, MoCo/4Fe-4S cofactor protein extended Tat translocation domain. This model describes a forty-five residue domain in which the last six residues represent the start of a TAT (Twin-Arginine Translocation) sorting signal. TAT allows proteins already folded, with cofactor already bound, to transit the membrane and reach the periplasm with the ability to perform redox or other cofactor-dependent activities. TAT signals are not normally seen so far from a well-supported start site. Member proteins may all be mutually homologous, with both a molybdenum cofactor-binding domain and a 4Fe-4S dicluster-binding domain
KKYWRSLEELADTPEFKELLQNEFPESAPELEDSGVSRRDFLK
>gnl|CDD|275313 TIGR04520, ECF_ATPase_1, energy-coupling factor transporter ATPase. Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes [Transport and binding proteins, Unknown substrate]
IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEE
NLWEIRKKVGMVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGG
QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMN
KGKIVAEGTPREIFSQVELLKEIGLDVPFITELAKALKKRGIPLPPDILTEEELVDEL
>gnl|CDD|275314 TIGR04521, ECF_ATPase_2, energy-coupling factor transporter ATPase. Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes [Transport and binding proteins, Unknown substrate]
IKLKNVSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDIT
AKKKKKLKDLRKKVGLVFQFPEHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERSP
FELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYA
DRVIVMHKGKIVLDGTPREVFSDVDELEKIGLDVPEITELARKLKEKGLPVPKDPLTVEEAADEILK
>gnl|CDD|275315 TIGR04522, EcfS_MSC_0063, putative energy coupling factor transporter S component, MSC_0063 family. This family of proteins is restricted to the Mollicutes (including Mycoplasma, Spiroplasma, and Ureaplasma). Members belong to a superfamily of multiple membrane-spanning proteins, among which those with assigned activities function as the S component (the specificity component) of ECF transporters. However, members fail to score better than the trusted cutoffs to previously built models for S component proteins (see pfam07155) [Transport and binding proteins, Unknown substrate]
KKKSLKYLVTTAILTALLVVLAYITSMIRIGTKSILQLADGLFLSLINFIPGPMMLISGILYGIIIDLIS
GGAIYIPISIVIKLLMFFITKLLKKKINFYLVIFIAYLMIFLYVLYAYILFDPSVAIVELITDSIQYGVS
VVSAIVLSIVF
>gnl|CDD|275316 TIGR04523, conserved_hypothetical_protein, helix-rich Mycoplasma protein. Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown
MKKLISLLAAISVFTATGFSYVGYKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKI
NNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNI
DKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKI
QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNN
KKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE
LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQE
KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE
LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE
KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS
SIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRM
IRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKFDDAF
>gnl|CDD|275317 TIGR04524, mycoplas_M_dom, IgG-blocking virulence domain. This model defines a domain restricted to Mycoplasma and Ureaplasma proteins. Members include protein M of Mycoplasma genitalium, MG_281, a virulence protein that binds the IgG light chain to block the binding of antibody to antigen. The crystal structure of the protein M antibody-binding region is solved (PDB|4NZR), and includes this homology domain. Full-length homologs to MG_281 are known in a few other Mycoplasma species, but this model's seed alignment demonstrates distant homology to many additional proteins with a much wider distribution across the Mollicutes. Member proteins include paralogous families in some species, such as MCAP_0345, MCAP_0347, MCAP_0349, and MCAP_0351 in Mycoplasma capricolum [Cellular processes, Pathogenesis]
YWQSTEYFNNRVLMPILQDTNSRYMNYNREYSDVSRQKGNYPGWEKKDASVSFSENGVSSNSYIKVYEYT
ANGELNASFPNLFFELIKTLDIDDKQAYDKFQSIINKTLKQYSPIDYVVIRNVGGDSLQDLKDLKLPESV
KKLTLFGKYTTINLIKLPNKKIQELELYSDSNANLWSINPLALKGVTNIIFDYNYSIRFTSIDLNTLTFD
NGDDISKLNEALEIVYNDRIKERAFQGYFAGGYITSLDLSN
>gnl|CDD|275318 TIGR04525, prot_M_MG281, IgG-blocking protein M. Members of this family, including MG_281 of Mycoplasma genitalium, bind conserved regions of the IgG light chain sequences, blocking IgG's normal function of antigen-specific binding. It is therefore an important virulence protein. Members of this family are found also in Mycoplasma pneumoniae, M. penetrans, M. gallisepticum, and M. iowae. Model TIGR04524 describes a region within this protein that is shared by many additional Mycoplasma and Ureaplasma proteins [Cellular processes, Pathogenesis]
FKKKLLWILGSVGAISVLLSGIIYLSVQSGNSLYVDGRGGGVGFPLATTNNLIAFSTLNSSSNNDGDYES
NIKLNGSVVFRDKLRNFANVLSSNISTQPKNLDGPVPKVESSGLIKTGSTFITPEFTAGYYDTVSGDGDT
LKYYQSTEYFNNRVLMPILDTTEGIYTANNRTYSDIFLGNFPGWIAVVAARVYSRNNSLSAYWNYNAAAG
TELLAKYPNHPSRLQFTLALDAKQINAAMINELLKEYSPDYVIISGLSGDSSTLKDLVLPESVKKVTLYG
DYTTINDAKLPFSEVQELEIYSTSNLKSINPLVLPPSTNIISDTVASKRFTEIDLSSATLTNNAQKLQVA
VEDVYVRRIKERAFQGYFAGGYIDSWLLKNTGITSFNNVSIKNLNDGTDRFYIAGVNVSYDGNENYYPNE
SIYETERPSNDSQIQDWIDQRAEGWGKVFEVEVKDLRLSVSYEVPFQEIMGFIAKYPNVKVVSILKYKLN
DTRVTILDIKKVLLKSISVKYGEESLYAKIPFVNVV
>gnl|CDD|275319 TIGR04526, predic_Ig_block, putative immunoglobulin-blocking virulence protein. Members of this family are putative virulence proteins of Mycoplasma and Ureaplasma species. Members share a region of sequence similarity (see TIGR04524) with protein M, a Mycoplasma genitalium protein that binds a conserved light chain region of IgG and blocks its protective function of antigen-specific binding. The seed alignment for this model includes an N-terminal signal-anchor domain and a proline-rich linker domain, and a C-terminal extension, in addition to the protein M-like domain recognized by TIGR04524 [Cellular processes, Pathogenesis]
KSKKKKIILISLSSSALSSASTGGAVYSANNFNSLSNNNIIYSTSAPSLILKNNLDINDASFSNRDNNLK
EVPKPEPQEKIEKPIVKIEPPKEPKPEPKPEIPKPEPPPVPPIPKPTPPPSETEKKIIIINGVKVRAPVE
TPPPRDDPSSDIEKGITNRSPYINQIVPKIISVEVTDELKKAAKKNALGGGEDELKRLISDQLFEKEKIY
RNNIDLWDNIWKKFKKLLDSGNVVEFLKEEAKSEYQISKEKNKLREQQKYLWLISNLDRTKFTKLSKDEL
KYLKQGYTPSPDENGEWDSHAYNPSDNPVTNRMYRDNNERRVFGYDSYYGRSPDDIENGNYPGWTKTDVT
SDNSFSKYGIGKDDGIKVYKYTRNDKNEDPGKKNEGIVVELDASNPNGYQKFLELIKKLKQKGKKITGYR
IKNMGKKDSTQNFKDILKALPDKIPQLELFFDNSTNTSSLIALENKKIKELSLYTNGNSLDDNWSINPNA
LKNVDWINTFDYNVSADYGPGEKIATRITFNTLAFDKNDYDYERINEGLRIAYYSRNNERIFQGGFGGKG
SYPTGLDFSRTPKIKSLKGLDFHDINKPFNKPRKLKKLTLYNDSSVFEISASDLNNAQFDHVLAKGEPEP
PKPKIKFSNGEQTQKIKITLTGNDLSSSGLSNLQKFIEYAKRSGSFKKIYVDSGALKLYNQL
>gnl|CDD|275320 TIGR04527, mycoplas_twoTM, two transmembrane protein. Members of this family are uncharacterized proteins from the genus Mycoplasma, typically about 260 amino acids long, with a hydrophobic predicted transmembrane alpha helix toward each end. Often two family members are encoded in tandem, e.g. MG_279 and MG_280 from Mycoplasma genitalium
MVKFLKKLSKFLLLIFGILVVGGLLGAGVAALYFREPIVNYYKQGVNSISSLNNEIKKILDNINNIIPKI
TNNLNSLKTDLNKTLENVEDVLKELEELKGIANNTDSNIKSTLNELEGTLRKINNSVIGVDNFSDNVGII
TIDEVKTQVKNFLNQVNSILNEIEQIINNPNNPEQFNEYYDIVSQILIAVGGSILGLGILSGILSLIFYK
KIDGVRVSRSNAKKQLADHLVKILKKYPDIKNEVI
>gnl|CDD|275321 TIGR04528, pyrrolo-quinoline_quinone, acido-empty-quinoprotein group A. Members of this family closely resemble quinoproteins and quinohemoproteins such as PQQ-dependent methanol, glucose, and shikimate dehydrogenases, but restricted to species of Acidobacteria unable to synthesize PQQ. Seven members occur in candidatus Solibacter usitatus Ellin6076, eleven in Acidobacteriaceae bacterium KBS 96, etc. Members have N-terminal signal sequences. They lack the pair of adjacent Cys residues, involved in electron transfer, typical for family TIGR03075, and they lack CxxCH motifs for cytochrome c-like heme-binding. What cofactor these paralogous families of enzymes might use is unclear
PPTDSWPTYNGDYSGRRFSPLTQINRANVKSLSLAWAFQTTGGGGGTIKSTPLLVNGILYFTVPDNVWAV
DARTGRQLWHYTWPPNGGTHIGNRGVGMYKDWLYFETPDCHLVSLDAKDGKERWDVEIADLKLGYFSTMA
PLVVKNHVIVGVSGDDLDVPGFLESRDPETGKLQWRWYTTPKPGEPGSETWPNLDAMAHGGGMTWMTGTY
DPELNLYYWGTGNPTPVLAGKGRPGDNLYTCSIVALNPDTGKLAWYFQPSPHDTHDWDAVETPVLFDGTF
DGKPRKLLAQASRNGYFFVLDRTTGKNLLTSPFVDTNWAKGIDAKGQPIPNPAKEPAPDGALVSPDSGGA
TNWPPPSFDPQTGLFYVNAHRSYSIYYLTDPDDKPEGWGGADYGLWSKSFLEAIDYKTGKIRWTHEWGEG
GGGAGVLTTAGGLLFTGDASGNLLALDAATGKTLWHARLGGSVSNGPITYELDGKQYVLVAAGDTLYAFA
L
>gnl|CDD|275322 TIGR04529, hypothetical_protein, hemophore-related protein, Rv0203/Rv1174c family. Members of this family occur as paralogs in most Mycobacterium strains, including 2 in M. tuberculosis, 6 in M. avium, and 9 in M. smegmatis. Members have a cleaved N-terminal signal peptide and exactly two Cys residues in the mature protein, both at invariant positions. The best characterized member, Rv0203, is a hemophore, that is, a secreted polypeptide that binds heme and delivers it to a transport system for import. Hemophores are protein analogs of siderophores, natural products that chelate non-heme iron and deliver it to receptors for transport. The unrelated HasA family of hemophores has been described in Gram-negative bacteria such as Yersinia pestis and Pseudomonas aeruginosa [Transport and binding proteins, Other]
CTAAQVAAALSAVAPAAAAYLDAHPDANQFLTAFLAQPPDQRQAAVQAYFDANPQVAAELRAIRQPLTDL
ANTCGNY
>gnl|CDD|275323 TIGR04530, hemophoreRv0203, hemophore, mycobacterial-type. Members of this family, including Rv0203 from Mycobacterium tuberculosis, are secreted heme-binding proteins used in heme acquisition. Such proteins are called hemophores. Members have a cleavable N-terminal signal peptide, and a mature region just over 100 amino acids long with a pair of invariant Cys residues. An unrelated hemophore, HasA, occurs in Gram-negative pathogens such as Yersinia pestis [Transport and binding proteins, Other]
FAAAAAGGAAVAALAGPSATAAPDPCAASEVARTVGSVATSTGDYLDANPETNQALTTISQQQAGPQSVA
SLKTYFDANPKVASDLQRLQQPLTALSGRCKLPVTLPQALGLM
>gnl|CDD|275324 TIGR04531, putative_pipecolic_acid_hydroxylase, putative nonproteinogenic amino acid hydroxylase. This extremely rare protein family, a branch of the 2-oxoglutarate dependent oxygenase family related to proline 3-hydroxylase, appears only in natural product biosynthetic clusters that include nonribosomal peptide synthases. One members is PlyP from the polyoxypeptin A cluster, suggested to hydroxylate 3-methylproline. Another, GetF from the GE81112 biosynthetic gene cluster, is a proposed to hydroxylate pipecolic acid
LKSQRLATLPIDSYDLDSELSIVDSHDYGGEYDAFTFGSWSAHVLANGSGADEDTSFRPHEGRLTLTELG
RKLPGIMSLVTDNFPLDRLQWVRIFSLRDGIIAPHVDFLEFAEPGTRLQIPLRTDEESLHSENDIVYHLR
RGEVWKIHTTDPHSAQSVSGFARLSLCLDFAGADEPVEIRNDIPATEPIRIIDRPSPTEAELEELLSSGA
GLSADTMRTDFRRFAALHFARRAHATAAFDWFIEAAVRTGDPALVAKAKAFRTYCIEKRGYGEAFEW
>gnl|CDD|275325 TIGR04532, polyketide_synthase, iterative type I PKS product template domain. Sequences found by this model are the so-called product template (PT) domain of various fungal iterative type I polyketide synthases. This domain resembles pfam14765, designated polyketide synthase dehydratase by Pfam, but members of that family are primarily bacterial, where type I PKS are predominantly modular, not iterative. The dehydratase active site residues well-conserved in pfam14765 (His in the first hot dog domain, Asp in the second hot dog domain) seem well conserved in this family also
TTSVHRVVEETSDGSKATVVFESDLSDPDLLAAIQGHRVNGVPLCPSSVYADMALTAAKYLLKRLRGSKD
AADVGLDVRDMEVDKPLVADPSDSDPQLLRVTATADASTSSRVSISFSSSSSSGKKTEEHATCTVRFGDP
AAAWLAEWSRTAYLVKSRIDALRQSAKEGSAHRLSRRMAYKLFSSLVDYSPKYRGMQEVVLDSDGLEATA
TVKLPTDPPDGGFTVSPYWIDSLLHLAGFIMNANDAVDSKDEVYINHGWGSLRFAEPLSPGKTYRSYVRM
QPVEGGLYAGDVYVFDGDRKIVAVCGGIKFQRVPRRLLNRLLPP
>gnl|CDD|275326 TIGR04533, cyanosortB_assc, cyanoexosortase B-associated protein. Members of this protein family are found exclusively in the Cyanobacteria, usually encoded next to a gene encoding cyanoexosortase B (TIGR04156). This relationship resembles the association of the unrelated protein family TIGR04153 with cyanoexosortase A (TIGR03763), and of most exosortases with EpsI
KLKKRLQLSQLVLLLLLLLLLAVGAVPGYLTGQWSWTDPPPVANLKELRKLRKTGLTLPGWQTIEQQEIQ
IGGHKWSLQVIKKDGQKQAILLLLPQNYPKDQPQVEWTDINGWQKWKTDSHRSLNFTVKSPSQEGKVKAR
FFRAWTQQQTFAVVQWYAWPNGGHPSPSHWFWADQWAQLRKQRVPWVAVSILIPMEPLGDIETVQSLAKS
LGQTVQSALMK
>gnl|CDD|275327 TIGR04534, hypothetical_protein, ELWxxDGT repeat. This model describes protein repeat with a well-conserved motif ELWxxDGT, and a periodicity of about 48. A single protein may have as many as 18 repeats. It may consist nearly entirely of this repeat, or may have other repeats as well (e.g. hyalin repeat). It is most common in the Deltaproteobacteria
GTLYFSADDGVHGRELWKSDGTAAGTVLVKDINPGPGSSSPSNLTVV
>gnl|CDD|275328 TIGR04535, conserved_hypothetical_protein, ferritin-like protein. Two families of proteins are known to be encoded, with some regularity, next to the gene for encapsulin (pfam04454), with surrounds the target protein to form a prokaryotic proteinaceous organelle. One is the family of enzymes that includes Dyp-type peroxidases. The other is this family, with a resemblance to bacterioferritins. Encapsulin-associated forms of the proteins in these two families have a necessary C-terminal motif that resembles DGSL[SGN]IGSL[KR]. Members of this family that include the last columns of the model in the hit region (and are encoded next to the encapsulin gene) should be designated encapsulin-associated ferritin-like protein
YHEPFEGLSEETRELHRAIRSLAEELEAIDWYNQRAEATDDPELKAVLAHNRDEEIEHAGMLLEWLRRND
PVWDEELRTYLFTEGEVTELEEEAGAAGGAEASSGSLTIGSLK
>gnl|CDD|275329 TIGR04536, geobac_encap, encapsulated protein. Members of this family are lineage-restricted uncharacterized proteins found mostly in Brevibacillus and Geobacillus. Members are encoded next to the gene for encapsulin (which once was called a bacteriocin), and have the C-terminal motif for associating with encapsulin [Unknown function, Enzymes of unknown specificity]
QELKELHAIFTRTKEAIESFMAMLQPIIDAANDEHERLYYHHIYEEEEQRLDRLKELIPYLEQLIAEKAL
DSLSNREFSRLLQDINLEKFGLHNFREHLDLALYEFKDEETRPKLDSMRDMTHADYLRVKEILATLNERF
SDGAHPDLTDPDDGHDHQVDHLKASASSANAKASSHSAPIQPGKKGLTVGSLKG
>gnl|CDD|275330 TIGR04537, hypothetical_protein, encapsulation C-terminal sorting signal. This model describes a diverse region of extremely small size (11 residues), so unavoidably there are both false-positives and false-negatives. All true hits should occur in proteins encoded next to an encapsulating protein (see pfam04454), and should occur near the extreme C-terminus. Families previously known to have this domain on some members to mediate encapsulation include dye-decolorizing peroxidases and a ferritin-like protein, but (as this model helps show) there are others, including some hemerythrin family proteins and novel family TIGR04536
DGSLGIGSLKG
>gnl|CDD|275331 TIGR04538, P450_cycloAA_1, cytochrome P450, cyclodipeptide synthase-associated. Members of this subfamily are cytochrome P450 enzymes that occur next to tRNA-dependent cyclodipeptide synthases. This group does NOT include CYP121 (Rv2275) from Mycobacterium tuberculosis, adjacent to the cyclodityrosine synthetase Rv2276
SVFSPQFEINPYSYFEYLRESDPVHYEESVDSYFISRYDDVKYILKSPDIFTTKSLAERAEPVMGDRVLA
QMTGKEHDAKRKIVLRGLSGKYLDHLLPLIRENTNNLLAPYLEKGEIDLVNDFGKTFAVCVTMDLLGLDK
RDHEKIREWHSGIAKFITSLNQSPEERMHSLECSEKLREYLMPIIEERRKNPGSDLISILCTSEDEGNAM
SDTEILALILNILLAATEPADKTLAYMIYHLLNNPEQLNDVLDDRKLLRRAIAETLRLHSPVQLIPRQLS
QDVTISGKEIKKGDTVFCMIGAANRDPEAFEDPDEFNIHRKDLVNKSAFTGAARHLAFGSGVHNCVGAAF
AKRQLEIVANILLDLLKNIRLEEDFSYVERGLYTRGPVSLLLSFD
>gnl|CDD|275332 TIGR04539, CycloL-leucyl-L-phenylalanyl_synthase, tRNA-dependent cyclodipeptide synthase. Members of this family take two aminoacylated tRNA molecules and produce a cyclic dipeptide with two peptide bonds. This enzyme therefore produces a type of nonribosomal peptide, but by a mechanism entirely different from the typical non-ribosomal peptide synthase (NRPS) that relies on adenylation to activate amino acids. Three characterized members of this family are the cyclodityrosine synthase of Mycobacterium tuberculosis (an essential gene), a cyclo(L-Phe-L-Leu) synthase from Streptomyces noursei involved in natural product biosynthesis, and cyclodileucine synthase YvmC from Bacillus licheniformis. Many cyclodipeptide synthases are found next to a cytochrome P450 that further modifies the product
FEVEPLTPNCRRIYERGEHALIGVSPGNSYFSEDRIAALLRWAARRFERVDVLIPDTHAATTLEALGYPP
AKARRKARREGRDLRRRIRRALEAAGGAYPRVRVLDLSELADNPAYRALLARVERAFAEDPEFRAACEEM
SREVLAGRLKGGVEPTEEQLDAAVRYLLAELPFFLDTPEILGVPSSVFCYHRPLPLLELLYGGEFPLRAA
PGQGYAVVRP
>gnl|CDD|275333 TIGR04540, CLB_0814_fam, conserved hypothetical protein. Members of this family are conserved hypothetical proteins in a narrow range of species. In Clostridium botulinum A ATCC 19397, the gene occurs immediately after a five gene operon for biosynthesis of the natural product bacimethrin, a thiamin antivitamin antibiotic
RLFYKTQKELATALNDLVDAYWEDEISEEELEELIKKIIENNEDKLYKNGKITTKLKQILGKRRLEVINK
ILK
>gnl|CDD|275334 TIGR04541, Thiaminase_I_Thiamine_pyridinylase., thiamine pyridinylase. Members of this family are thiamine pyridinylase (EC 2.5.1.2), also called thiaminase I. Most examples of this secreted, thiamine-degrading enzyme are encoded with a cluster for biosynthesis of the thiamine antivitamin bacimethrin [Cellular processes, Biosynthesis of natural products]
LSLLLSFLMIFTSVAGLNVAFSDAEPKQTLNVALYPYVPDPIRFKKAVETEWNKKEPNVKLNFVDWDCYS
EDPPKDLDVFVFDAIFLSHFVKEGYLSPIPEKDIKNKEDILPFAMEGCKIKGSAYAIPQIICTNLLFYRK
GDYDIQKVNSVYDLYDKLGKFTSEDIILPNNKGLLIDMSGGTTKACMYLDALIDTTGEYTKFCLLPNLNE
LNKDAIESLRLLQSMAGKSQANYWPENNDSYIRAKWFINGKGRAYIGYSESMSQMKEFANDIDFKTISLS
KNSNIPLFYGDVVGVNSSTTNSYKKELAIELANVIADKNTMVQAVSPDENGKYPQYLLPARRSVYHNLGQ
KYPIYGKLYKIADNSNNKLFRTGPEIREWLK
>gnl|CDD|275335 TIGR04542, GMC_mycofac_2, GMC family mycofactocin-associated oxidreductase. This model describes a set of dehydrogenases belonging to the glucose-methanol-choline oxidoreductase (GMC oxidoreductase) family. Members of the present family are restricted to the bacterial genus Gordonia, and seem to replace the related family TIGR03970, which occurs in Actinobacteria generally but not in the genus Gordonia. Members of both this family and TIGR03970 are associated with the mycofactocin biosynthesis operon in Actinobacteria [Unknown function, Enzymes of unknown specificity]
DVVVVGAGSAGCVVAERLSRDPGRSVLLLEAGPAGWPGAAVLDLRRLPIAAGSPRVRHYRERRGLPVVRG
RGLGGSSAVNGGYFLRWHRDDFAGWPSGWPIDAIAAAYDELDAPGGRMSVSPVADDELGDAARAFETYWA
TRAPVRPVAGRWPVVGVNRVRSNRVGGLRWTAAEAYLRPALDRPNLTVRTGARVDRLVVAGGRVTGVRTG
GEVIRAGEVILCAGTLGTAALLLRSGLVGGPSLEVHEHREVLVRYRPRGPARPAPLLPTVVHTDDGLEIR
CYSDDFASYIRGLPPTGPAVGVAAMRPGTPGRLTLDGGRLVVDLGEPDADVADRLSAGVEEVVEMLASPE
FADVVEPGSVSVDPVVGTSQHAWGTLPMGTRTDWLGGVDGVRGLRVVDGSILPTGGRSGPHATIMMVAAL
IADRL
>gnl|CDD|275336 TIGR04543, 2-ketoarginine_methyltransferase, 2-ketoarginine methyltransferase. This SAM-dependent C-methyltransferase performs the middle step of a three step conversion from arginine to beta-methylarginine. It performs a C-methylation at position 3 of 5-guanidino-2-oxopentanoic acid (keto-arginine). An aminotransferase converts arginine to 5-guanidino-2-oxopentanoic acid, and later converts 5-guanidino-3-methyl-2-oxopentanoic acid to beta-methylarginine
IEAIQPIRGFVLAQAIYHLFESGLFDELAEAGPRSVGELAEELGLDSDRLTGFLRYLANEGIVVESDGVF
SLTEKGRELAEFRPWYELLVGGYGETFLQLGEVLQQGAGWASRDGTKVGIGSCGISHYDAIPLVRSLLAR
LPGAPASLVDLGCGDGRFLADFCEALPEISAIGVDPDAGSYRAARALIRERGLADRVSLVNAGAEDFLRS
DLGSGPDFFVLGFVLQEILGQEGRGAVVGFLRTILARFPDAHLIVIEVDHRPDDPAVMRHGLGLAYYNPY
YLLHYFTEQRLETDAFWEELFAEAGLSVVAKLTTDPEVDSTGLELGYLLRR
>gnl|CDD|275337 TIGR04544, aminotransferase_class_I_and_II, beta-methylarginine biosynthesis bifunctional aminotransferase. Members of this family are the bifunctional aminotransferase that catalyzes the first and third steps in the three-step conversion of arginine to beta-methylarginine. It first converts arginine to 2-ketoarginine, then converts 3-methyl-2-ketoarginine to 3-methylarginine. All members of the seed alignment are encoded next to a 2-ketoarginine methyltransferase (EC 2.1.1.243)
ALSPLQQRLAYAASRPNEPWRVLVENVPVWPEGPRPKAEAASDDDYQYADSQGHPTLINAICSRERELYG
LDLTGENILVTNGGMHGLSLIFRHLTGRGYRKAVCAAPVFDSVPDLLRASGLDVYLLRLTGAFIDWDELV
DICLGPTSLVYLNFPHNPTGECLSEDTMRDLVALAERRGVSLVLDLVYDSFIFDPGVLRSPFALAVNWDD
LYTVNSMSKNYGAPGLRIGWIVADPKNIERLTGRLEWERVAVSGRAQQQAARLISLGNQPLVERVRAGRR
LVLTWASSLELAHAPLPSGGTQLWVDLGVVDIEAFADFMLEEHGLVLTTSANYAPALGGHIRIPTGCPPS
RLRRSLELLAQGLERW
>gnl|CDD|275338 TIGR04545, rSAM_ahbD_hemeb, heme b synthase. Members of this family are AhbD (alternative heme biosynthetic protein D), a radical SAM enzyme in sulfate-reducing bacteria and methanogens that performs the last decarboxylations to synthesize heme b from Fe-coproporphyrin III. Members include DVU_0855, previously included in error in TIGR04055, the NirJ2 family thought to be involved in heme d1 biosynthesis [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
LIAWEVTRSCNLACVHCRASATSEPYAGELSTDEAKHLIDEIAAFGRPILILTGGEPLLREDVYELAAYG
TDKGLRVVLATNGTLLTPGIARRMKESGVQRVSISIDGPDAESHDAFRGMPGAFEGSMRGIEYLKKAGME
FQINTTITKRNLHEISAIFDLAVRLGAVAHHIFLLVPTGRGRDLENQEISAADYERVLNWFYDAQKTCPI
QLKATCAPHYYRIMRQRAKAEGREVTVKTHGYEAMTRGCLGGISFCFISHTGQVQPCGYLELNCGNIREA
PFEEIWENSEVFQKLRNPEELSGKCGHCEYKKVCGGCRARAYAATGDYLAEEPYCIYEP
>gnl|CDD|275339 TIGR04546, rSAM_ahbC_deAc, 12,18-didecarboxysiroheme deacetylase. This model describes one of a pair of radical SAM enzymes involved in the alternative heme biosynthesis (ahb) pathway for heme b biosynthesis from siroheme. This anaerobic pathway occurs in sulfate-reducing bacteria and methanogens. A very similar pair of radical SAM enzymes (TIGR04054, TIGR04055) is involved in heme d1 biosynthesis in species such as Heliobacillus mobilis and Heliophilum fasciatum [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
IGISKLYCGTVEPSDALRYGRHSGKLPSHLLQFSKDKKPVVVWNMTRRCNLKCVHCYAHAQDEEFKDEMS
TEEGKALIDDLAAFGAPVLLFSGGEPLMRKDLPELAAYAVSKGMRAVISTNGTLITKEKARELKEVGLSY
VGISLDGGEEVHDRFRGVPGAFDAALKGIENCREEGIKVGLRFTINKRNVADIPAIFDLLEAEDIPRVCF
YHLVYSGRGSKLVKEDLSHEETRATVDLIMDRTRDLFERGLPKEVLTVDNHADGPYLYLRMLKEDPKRAA
EVLELLQMNEGNSSGRGIGCVSWDGEVHADQFWRHHSFGNVRERPFSEIWTDPSNELLARLKDKKPHVQG
RCAACRWLDVCGGNFRARAEAVTGDLWAPDPACYLTDEEI
>gnl|CDD|275340 TIGR04547, putative_liporotein, MOLPALP family lipoprotein. Members of this family are surface lipoproteins, about 900 amino acids long on average, found only in the Mollicutes (Mycoplasma, Entomoplasma, Acholeplasma, Mesoplasma, Spiroplasma). Paralogs occur, such as MCAP_0360, MCAP_0361, and MCAP_0362 in Mycoplasma capricolum. This family shares significant N-terminal sequence similarity with STREFT (Secreted Thousand Residue Frequently Tandem), described by model TIGR04512; several members of the STREFT family have been misannotated as GnsA/GnsB family proteins. For proteins in this family, we suggest the name MOLPALP (Mollicutes Paralogous Lipoprotein) family lipoprotein [Cell envelope, Surface structures]
MKKLLAILGAMSLVASSSATVIACTTTEKDKFEYNNSLKNLQGIASLFAKSAILADQNGISLDYILNTFK
NKKAEDLLKKYNLKLDNNDRSIDKKSTLEELLKRYFGKDSYLKKTELDDNINLDGKKGTSNGLLSEIFPE
GLNGQNTDTTSNSIIKILSLISGLNTLLLGSLFNSQGSTLKSFILKDKTDLISLLEKLILTNPKLIETIN
KFIDKIDVNKKYKDLSLENLDNALYISLTNGIGLILNIKDFKPVELSTKNDINDSLKNASKALWDIIQKK
DESSKNKEEDWENVAKILAYILRALQLLQKKLSLFDDTKDYYQPKDANNLFSKTKTNSEFLKEVLKDKTI
EKITKFKISSINLKYLLSFLKYYLGNLKKDPNGYNLQKLLAILFGTPKKVEYSPETNNIDNLKPFYESYQ
ANSGGDLLYKIIESLLNKKLSLILYIIFKSLKSLKIGTKENFLKLTDLFYKLIPSIFYSLANQGKLIKDS
LKSILQLLKKGFIEEVKKIAFFLLSKIGNKFLKNLFLALYSGDFFKEILQLINDLGVIQKLIDNINNSID
TIFGNDKPLNLKTLLTTPLDKFLGSFWKIDKKIFLYGLTDKSISDIIDDLASDFEVDENEKLKDLESYII
NLTDIKELVNKIFNYTYKWKDNGNSTKTNLLSLLLENPDKALEILGFTKDKNNKFKEGSLLDALSNKFGN
PNKNKNLPAKDTLQELINVLAKIYSNLNKAKYIKDEFNEDFLDQKNWTFEFTFSKKNKSDQNKDIKSQTL
LAYYKNKKNNSQTKYTFKYSRDSKQSKFKFTKITK
>gnl|CDD|275341 TIGR04548, hypothetical_dnad-like_replication_protein, DnaD family protein, Mollicutes type. This model describes the full length of a family of proteins in the Mollicutes (Mycoplasma, Spiroplasma, Mesoplasma, etc.) homologous to the N-terminal region of DnaD from Bacillus subtilis [DNA metabolism, DNA replication, recombination, and repair]
FDLLKKGLISKKKLLLENYKKIGLTENQVMIILMIMHLSDDDKKFITPNELAKYMNLSESEIEKEIEKLV
EKDLIKIKPKEIDFSPLFNKIAIIIENEYLNKENKDFFQQIEEKLGFKLTEDQKAELKKLINNNISKPQL
LEIINNNNIKNFEELLKIIGKYLNNKPKSLTKFNWLDD
>gnl|CDD|275342 TIGR04549, LP_HExxH_w_tonB, substrate import-associated zinc metallohydrolase lipoprotein. Members of this family are lipoproteins with the typical zinc metallohydrolase HExxH motif and additional similarities to a better-documented zinc peptidase family, pfam06167. The seed alignment begins immediately after the lipoprotein motif Cys residue. Up to five members of this protein family occur per genome, in the context of certain gene pairs related to RagA and RagB, or to SusC and SusD. Those gene pairs, like the present family, are restricted to the Bacteriodetes, may number up to 100 pairs per genome, and are linked to TonB-dependent uptake of biopolymer-derived nutrients such as glycans. A possible function for this lipoprotein is to hydrolyse larger molecules to prepare substrates for import and utilization [Unknown function, Enzymes of unknown specificity]
SKDDLDSTSIFPDTPTEKNEFDKWLLKNYTEPYNIEFKYRWEDIESDMNYNLVPADYDKSIPLAKLVKYL
WLDAYDEVAGPDFIKKYFPKQIVLIGSPAYNSNGTIVLGTAEGGRKITLYNVNNLDIKNIDALNEYYFHT
IHHEFTHILNQTKPYPTDFKKISEGGYVGSDWYNVSDAEALQLGFISPYASSEPDEDFAEMISIYLTNSK
AEWDAILNSAGATGRAIIRQKLAIVRNYMKDSWNIDLDKLRDIVLRRIDEV
>gnl|CDD|275343 TIGR04550, Methane_monooxygenase_component_D, soluble methane monooxygenase-binding protein MmoD. Members of this family are MmoD, a protein that binds the soluble (as opposed to the membrane-bound, copper-rich, particulate) methane monooxygenase and may regulate its activity. Recent work suggests that MmoD, together with methanobactin, acts a copper switch to regulate which enzyme form is produced
DTEAERILIHSDERYAAYTQDLEFMWRWEIYRDGEFVQEGCSLSLDSSREAVDHVLSFFQRSDK
>gnl|CDD|275344 TIGR04551, hypothetical_protein_CAP_1272, TIGR04551 family protein. Members of this family are proteins of unknown function, about 620 amino acids in length, and universal in but restricted to the Myxococcales, an order within the Deltaproteobacteria with at least 15 sequenced genomes as of 8/2014. The most closely related homologs outside the Myxococcales show localized homology only and display sharply lower scores. Relatively few protein families (roughly 20) could be built to have a comparable restriction to the Myxococcales. The putative protein sorting signal MYXO-CTERM (TIGR03901) appears so far universal in but restricted to the Myxococcales, making the present family a candidate to be involved in recognizing and processing proteins with that signal
FELDGYFRVRPNLFYKFDLGRPPSGWRSLFPRPPRNSGSSGTGSANENTQAGANMRLRLEPTLNISENVR
VKAQIDVLDNVVLGSTPDSLFPGPDGYYPFGLFSSTQAPPAAGVNALKDSISVKRAWGEVQTPVGLLRFG
RMPSHWGLGMLRNDGDCLDCDYGDTVDRIQFVTGPFGGIYFTPMLDFNSEGATSAYFGDGLGQPVDLTQA
DDAHQWVLAIARRDTPEQIRAKLDRNEGVLNYGLYFTYRTQRWENPASTGETGDGATLTPGDAVTNPGFV
PRDASLYIPDLWLRLLEKKWRLEAEAAAVYGSIGNRGTTESDYADPPQDQSLTVRQFGGAAQAEYRALPN
KLRLGLELGFASGDDAPGFGAQPGRRGSNTAPGDIDGPQFSCGGGCSDRTIRNFRFNPAYRVDLILFREI
LGGVTDAWYVRPSLRYDIAQGLDVGGAAIYSQAIYAESTPSNTSRPLGLELDAGATYQSEDGFIATVAYG
ILFPLGGLGDLEGLQDLDLSTAQTVRTRLGIRF
>gnl|CDD|275345 TIGR04552, hypothetical_protein_Q664_03455, TIGR04552 family protein. Members of this family are bacterial proteins, roughly 400 amino acids in length. Most members belong to the Deltaproteobacteria. All members of the Myxococcales, and order withing the Deltaproteobacteria, have a member. The arrangement of conserved residues into invariant motifs suggests enzymatic activity. The function is unknown
FLFDWEILRLILGGGSVIDWRRLNFQDLEEVDRFLRLYGFDPDDPADRARLRTVHREAVEYLRRVFEGLD
LRIPEEVAMPEDIRDLLLYASGRKGTRERRRWACAVLKVMHVIHHADGRLLLRRLPEIQAQVFDRFEEYV
LRDADQLMLADGEIKLPLVEFETKSRKTRDSLLTKLLAKPENVAAQVFDRLGVRLVTKTRFDLLPVLRFL
IRRNLIPFNNVVPGRSRNTLVDLEALLEVYMSLRNDLSEPRFLQAIERELLDRDLEQRKGDRNPFSGRDY
RSIQFTVRLLIRLDNPLPKPDKDARPDGGRRFFYLYEFQLMDEETHERNESGEASHEAYKKRQRERARKR
LFR
>gnl|CDD|275346 TIGR04553, ABC_peri_selen, putative selenate ABC transporter periplasmic binding protein. Members of this family ABC transporter periplasmic binding proteins and represent one clade within a larger family that includes phosphate, phosphite, and phosphonate transporters. All members of the seed alignment occur near a gene for SelD, the selenium-activating protein needed to make selenocysteine or selenouridine. Context therefore suggests members should be able to transport selenate, although transporting other substrates as well (e.g. phosphonates) is possible. This model has no overlap with TIGR03431, whose members are found regularly with phosphonate catabolism operons
VFVFTAIPDEDPTELQRRFAPLADYLEEELGVEVRFVPVTDYAAAVEAFRNNQVQLAWFGGLTGVQARVR
VPGSVPLAQRVEDEAFRSVFIAHESTILELADGLPELKGKTFTFGSKSSTSGRLMPRSFLLEAGEAPDDD
FKRVGYSGAHDATLALVEAGTYDAGALNISVWEKEVADGKVDTDKVRVIWTTPGYPDYNWTVRGDVDERF
GEGFTDKVTQALLDLDPSTAEDKEILELFRASRFIPTSNDNYAGIEAAAREAGLLD
>gnl|CDD|275347 TIGR04554, hypothetical_protein_MMCAP2_0629, three transmembrane helix protein. Members of this rare family are small, highly hydrophobic, and restricted so far to the genus Mycoplasma, where it appears not be be essential. All members have three hydrophobic transmembrane helical segments
ITPVSVIGLVLTLLAIIFLSWLVYKNKDKIISNKVNLAIVAIGYVVLLIALILASVAISKYNSPGLGDLF
ASDLPAKLKGLAYSGLVFSLIGAGVTGFIFTKFKK
>gnl|CDD|275348 TIGR04555, probable_sulfite_oxidase_molybdopterin_subunit, sulfite dehydrogenase. Members of this family are the sulfite dehydrogenase SoxC. All members have a twin-arginine translocation (TAT) signal for secretion of proteins with bound cofactor across the plasma membrane
RRDFLRRGAAAAGAAAAAAAAAATAGDVAPLEVPPWTTTLGAPVNERPYGMPSKFEKNVVRRIVPWLTAD
PGSSVSFTPLQELEGIITPNGLHFERHHNGVPDIDPAQHRLMIHGLVERPLVFTMEDLMRYPSVSRIHFI
ECPANGGMEWRGAQLNTVQFTHGMLSCAEWTGVPLSTLLDEAGVKPEAKWVLAEGADGAAMTRSIPIEKA
LDDALVAYAQNGEALRPEQGYPLRLVVPGWEGNMNVKWLRRLKVGDQPWMSREETSKYTDLMPDGKARQF
TFVMEAKSVITSPSPGQPLRGPGFYEISGLAWSGRGRIKRVDVSLDGGRNWREARLQGPVLPKALTRFRL
PWDWDGKPALLQSRAIDETGYVQPTREQLRAVRGVNSVYHNNAIQTWAVAADGEVTNV
>gnl|CDD|275349 TIGR04556, type_I_polyketide_synthase, polyketide synthase-associated domain. This model describes a rare domain found as the N-terminal region of a number of dinoflagellate-specific proteins that resemble type I polyketide synthases
DLDGFDIVLGPKSDPDVVGEEIADCLATKGFCVMKLFVASEDLDSAVDVAKKLEDAGQFFRLAVEFEEGY
LGKEGSAKVAWLDPSSPDAPDAVKDSPLKKMDANFSSIAQMLQPYSQESLGFEVYSRTNALLRLPLPDGD
EEEYPPAEADDGEAEKYLHTMCRRKLTVLVFMGPTGGTLTLQPKEEGGDSVEVPAEPGTVVLIRSDAYEY
SYEPTGESLTLSSFLMQD
>gnl|CDD|275350 TIGR04557, hypothetical_protein, quinoprotein dehydrogenase-associated SoxYZ-like carrier. Members of this family are fusion proteins, with the N-terminal region similar to the sulfur oxidation protein SoxY (TIGR04488) and the C-terminal region similar to sulfur oxidation protein SoxZ (TIGR04490). Members occur exclusively in species with PQQ-dependent enzymes that have a Cys-Cys motif (TIGR03075) for electron transfer to c550 family cytochrome. By homology to the sulfur moiety-binding subunit SoxY, we predict the conserved Cys in the Gly-Gly-Cys motif binds some unknown adduct
WEDLRKDLFGDRPIVFDDGRVKLEAPYRAEDAAQVPVTIDASALAGYVKRITLVIDLNPIPLAATFTFGP
AAGPADLSTRVRVNQYTPVRAIAETADGVLHMGGRFVKASGGCSAPAGKDDAEALARLGKMKGRLFPEAS
GAPRRARLMIRHPNDTGLQMDQVTRLYIPAFYIEKLEVDQGGEPLFRMEGGISISENPVFRFDFTPAGDG
PLTVVARDNNGNRFE
>gnl|CDD|275351 TIGR04558, beta-lactamase_domain-containing_protein, quinoprotein relay system zinc metallohydrolase 1. By homology, members are Zn metallohydrolases in the same family as the SoxH protein associated with sulfate metabolism, Bacillus cereus beta-lactamase II (see PDB:1bc2), and, more distantly, hydroxyacylglutathione hydrolase (glyoxalase II). All members occur in genomes with both PQQ biosynthesis and a PQQ-dependent (quinoprotein) dehydrogenase that has a motif of two consecutive Cys residues (see TIGR03075). The Cys-Cys motif is associated with electron transfer by specialized cytochromes such as c551. All these genomes also include a fusion protein (TIGR04557) whose domains resemble SoxY and SoxZ from thiosulfate oxidation. A conserved Cys in this fusion protein aligns to the Cys residue in SoxY that carries sulfur cycle intermediates. In many genomes, the genes for PQQ biosynthesis enzymes, PQQ-dependent enzymes, their associated cytochromes, and members of this family are clustered. Note that one to three closely related Zn metallohydrolases may occur; this family represents a specific clade among them [Unknown function, Enzymes of unknown specificity]
PLDYGLTPRKVAPGTWVFEGATEDFSRANGGNIVNTAFIVTDEGVIVIDTGPSRRYGEQLRAAIAQVTGK
PVRRVLNTHHHPDHFLGNQAFADVPIAALPATIAGIRAEGDAYADNMYRLVGDWMRGTEPVPPNEALEAG
PLTIGGRRLELLALSGHTGADLVILDEATGVLFAGDLVFLDRAPTTPHADLADWLASLDRLEALPAKVLV
PGHGPVDRDGAGIAQTRDYLAWLDATLRDAAERGLDMTEVMALPIPERFAGLAAAPAEFRRSVSHLYPAY
EQAAL
>gnl|CDD|275352 TIGR04559, metallo-beta-lactamase_family_protein, quinoprotein relay system zinc metallohydrolase 2. By homology, members are Zn metallohydrolases in the same family as the SoxH protein associated with sulfate metabolism, Bacillus cereus beta-lactamase II (see PDB:1bc2), and, more distantly, hydroxyacylglutathione hydrolase (glyoxalase II). All members occur in genomes with both PQQ biosynthesis and a PQQ-dependent (quinoprotein) dehydrogenase that has a motif of two consecutive Cys residues (see TIGR03075). The Cys-Cys motif is associated with electron transfer by specialized cytochromes such as c551. All these genomes also include a fusion protein (TIGR04557) whose domains resemble SoxY and SoxZ from thiosulfate oxidation. A conserved Cys in this fusion protein aligns to the Cys residue in SoxY that carries sulfur cycle intermediates. In many genomes, the genes for PQQ biosynthesis enzymes, PQQ-dependent enzymes, their associated cytochromes, and members of this family are clustered. Note that one to three closely related Zn metallohydrolases may occur; this family represents a specific clade among them. Some members of this family have a short additional N-terminal domain with four conserved Cys residues [Unknown function, Enzymes of unknown specificity]
ALSVEEIAPGVFVHQGVHADPDPDNRGDIANIGFIVGEDAVAVIDTGGSRAEGEALLAAIRQRTDLPIRY
VINTHVHPDHIFGNAAFREDGAEFVGHAKLPRALAARGEFYLASFARLLGEAFLGTEIVPPTRLVADPLE
LDLGGRVLELTAWPTAHTDNDLTVFDEKTGTLFTGDLLFVEHIPVLDGSLLGWLAVLDRLKARPAARVVP
GHGPVSLDWPAALAPQRRYLETLRDDVRAAIKDGLPLEEAVETAAQSEKGKWALFDEYNRRNVTAAYAEL
EWE
>gnl|CDD|275353 TIGR04560, hypothetical_protein_MED134_13161, ribosomal small subunit protein bTHX. Members of this protein are the lineage-specific bacterial ribosomal small subunit proteint bTHX (previously THX), originally shown to exist in the genus Thermus. The protein is conserved for the first 26 amino acids, past which some members continue with additional sequence, often repetitive or low-complexity. This model also finds eukaryotic organelle forms, which have additional N-terminal transit peptides [Protein synthesis, Ribosomal proteins: synthesis and modification]
MGKGDKKTKRGKISRGSYGKRRPRKK
>gnl|CDD|275354 TIGR04561, hypothetical_protein_SCULI_v1c03640, integral membrane protein. Members of this protein are short (about 85-residue), low-complexity sequences of unknown function, with a highly hydrophobic N-terminal region of about 40 amino acids followed by a charged (Asp, Glu, Lys, and Arg-rich), sometimes repetitive C-terminal region. Members occur exclusively among the Mollicutes (Mycoplasma, Mesoplasma, Acholeplasma, Spiroplasma, Entomoplasma). The gene neighborhood of this protein is not conserved
FLSGIEVFGITIPFWVILYIFAIIAGLALLIYILNLLFRKRKFKKKEQVNAEEFKKLTKIEKQKNDIDDE
IASIIKDRKQGK
>gnl|CDD|275355 TIGR04562, TIGR04562, TIGR04562 family protein. Members of this family are proteins of unknown function, about 400 amino acids in length. Members are universal among the Myxococcales (a branch of the Deltaproteobacteria) and occur sporadically elsewhere [Unknown function, General]
DWESLRLVLGGGSVIDWRRLNLHDLEEAERFLRAYGFDPDDPADRARLEGVHQEALQFLRRVFLEGLDLD
IPEEVRMLADPRELLLLASGRPPTGERQRWACAVLKVMHTIHHLDGDLLLRYLPEIQQQVFDRFEEYIHR
DAGQMRFLKDGAYGIPLVEFETKSRKTRDSLVTKLLHKAENVAADIFDRLGVRLVTRTRFDALPVLRFLT
RRNLIPFHNVKPGRSRNTLVDLEALREKYPDLIKMSLRPDLSEDRFLEAMERELLENSPGTRGDNPFSGR
SYRAIQFTVRLLIRLPAPLLPIPDLSAEARGRRFFYPFEVQIMDRASHKRNESGEASHAAYKKRQREAAR
KRLFG
>gnl|CDD|275356 TIGR04563, Hypothetical_protein_CAP_4887, MXAN_4361/MXAN_4362 family small protein. Members of this family are small proteins that appears to be restricted to and yet universal in the Myxococcales. The function is unknown. Members include two tandem loci in Myxococcus xanthus DK 1622, MXAN_4361 and MXAN_4362, although members are not tandem in other Myxococcales
ASTDKRKQSLYFPEEMLREIQEEATRQDRSLSWIVQQAWRLARAEIKKFPSVN
>gnl|CDD|275357 TIGR04564, hypothetical_protein, Synergist-CTERM protein sorting domain. This model identifies a C-terminal domain of about 27 residues whose features are 1) a short Gly/Ser-rich region that ends in an invariant Gly-Cys motif, 2) a highly hydrophobic probable transmembrane alpha helix with a nearly invariant Pro near the end, and 3) a cluster of basic residues (Arg, Lys), and then the end of the protein. This domain occurs, so far, only in species of Synergistetes (Dethiosulfovibrio peptidovorans, Aminiphilus circumscriptus, Aminomonas paucivorans, Fretibacterium fastidiosum, Cloacibacillus evryensis, Synergistes jonesii, etc). This region closely resembles the MXYO-CTERM region of the Myxococcales, a division of the Deltaproteobacteria (see TIGR03901), but that domain lacks the the conserved Pro, frequently has two Cys residues instead of one, and most importantly, has a spacer region separating the Gly-Cys motif from the transmembrane segment. As with MYXO-CTERM, the enzyme presumed to recognize and cleave the sorting signal is not known. The lack of a spacer region between motif and TM segment suggests the presumed protease is located largely within the membrane, like rhombosortase and archaeosortase, rather than merely tethered to it like sortase
SGGGCAAGFAPLALLLLLPLLLLRRR
>gnl|CDD|275358 TIGR04565, hypothetical_protein_N47_G32130, outer membrane beta-barrel protein. Members of this family are outer membrane beta-barrel proteins, as inferred by distant homologies to other families (e.g. pfam13505) and by the concentration of aromatic residues, especially Phe, in the OMP signal region, which is flush with the C-terminus in some members, but followed by a few residues in others. Members have variable insertions and deletions, affecting scores, so this model does not cleanly separate all members from all non-members. Members are common in the Myxococcales, with five occurring in Myxococcus xanthus DK 1622
AGVLSIEDFGSTYVFGLRLGYHLTEDWALEARYGYATAGLTSYERLSGGAPLLTPDDRRDLSYYGLSLGW
NPIYGKLFLGDDKAFNFDLYLLAGAGNTDFAGESHFTVNLGAGYRFFLTDWLALRLDVRDHIFESEILGE
SKLTHNLELTLGLSFFF
>gnl|CDD|275359 TIGR04566, hypothetical_protein_Q664_47920, outer membrane exchange protein TraA, N-terminal region. In Myxococcus xanthus, the protein pair TraA (MXAN_6895) and TraB (MXAN_6898) are required for contact-dependent exchange of outer membrane proteins. The C-terminal half of TrA consists largely of Cys-rich tandem repeats. This model describes the N-terminal region of TraA, and related protein MXAN_4924. This region is suggested to be similar to the lectin PA14. Members of this family are restricted to a subset of the Myxococcales, and so have a narrower species distribution than the MYXO-CTERM putative protein sorting signal (TIGR03901), which is universal in the Myxococcales. Note that TIGR04201 matches at least seven repeats in the C-terminal region of TraA. T [Protein fate, Protein and peptide secretion and trafficking]
VVISGDPVAPSPEQPGTGLCMASSVSTDPAADFPQSQSTYNGGLNAFMETNPGRRVTSVLRTPFDLSNNN
TDGDQLSYGDFENAVPGCPSGGCDFFYNDTSTSFGTRLRGYLNVTSDMVGRPLHFGFYADDAVSFTIFDR
DQTSYQVINRPPQLGAPTWRTTNSVTFEQPGLYPVEVLYAEVTEHAALEMSVFVGAFSDFERPATQPPIV
KLDDAGFTLATPEQFFQTESGRPSFPDPNQ
>gnl|CDD|275360 TIGR04567, DNA-directed_RNA_polymerase_subunit_delta, DNA-directed RNA polymerase delta subunit. Members of this family are the RNA polymerase delta subunit, as found in the Firmicutes and the Mollicutes. All members of the seed alignment have an extended C-terminal low-complexity region, consisting largely of Asp and Glu, that is not included in the model. Proteins giving borderline scores should be checked to confirm a similar acidic C-terminal domain [Transcription, DNA-dependent RNA polymerase]
NELSMVDLAYEILKEKKEPMSFYDLWNEVAKLKGLSDEEIEERIAQFYTDLNLDGRFISLGENKWGLRSW
YPFEEIDEETAPI
>gnl|CDD|275361 TIGR04568, arch_SelU_Nterm, selenouridine synthase, SelU N-terminal-like subunit. This protein is involved in biosynthesis of a selenonucleotide, probably 2-selenouridine, in tRNA of some archaea, such as Methanococcus maripaludis. This protein resembles the N-terminal region of bacterial SelU, and its partner protein resembles the C-terminal region [Protein synthesis, tRNA and rRNA base modification]
MDEGILSRLLTFKNDVILCIVLKTGRKMITNGKKILAGKIEGELASFILSASKEILKPGVLKFKDEDIYF
EPIDIKKYLGSIGGELVDNVITVSEFLELIKEDVIIVDARSPREFKEKTIPGAINIPLFLDDEHETIGKT
YKQEGREKAIEIATDIIEKSIKRILNEAKKLDRNKLIVVFCARGGMRSQTMATILKLLGFKVKRLIGGFK
AYNHA
>gnl|CDD|275362 TIGR04569, arch_SelU_Cterm, selenouridine synthase, SelU C-terminal-like subunit. This protein is involved in biosynthesis of a selenonucleotide, probably 2-selenouridine, in tRNA of some archaea, such as Methanococcus maripaludis. This protein resembles the C-terminal region of bacterial SelU, and its partner protein resembles the N-terminal region [Protein synthesis, tRNA and rRNA base modification]
MIIFGLFGKTGCGKTEILDELKKKHPVIDIEGCANTRGSILGDLYHLSSSTQEKFDTLLNEQIEKAKSTG
YCIVEFEGKKIGGRTKLTIPEPFSDLKNYNYNIVINCPYECQIKRLLSWYRPKNESEKEILIDKFVDLKT
VFKKPEKIELVDKIIELIKKDEYYDAAKLIEEKLYSEHYMRHIKKIKHDLIVYNEDNLKSAEIISRFIDE
KLKEHNI
>gnl|CDD|275363 TIGR04570, Hypothetical_transmembrane_protein, small integral membrane protein. Members of this extremely rare protein family occur in Mycoplasma mycoides and two species of Spiroplasma. The protein is small and hydrophobic with two predicted transmembrane (TM) regions [Unknown function, General]
MNEFNLAKDKGLIQKIFKKIPWFYHLIFFLIGIVAGLLFQFLRIKRFAFPYFFIFFFAIILLYCVLFIIF
SPIIKQNWFIKKGFNEK
>gnl|CDD|275364 TIGR04571, LmtA_Leptospira, lipid A Kdo2 1-phosphate O-methyltransferase. This family describes LmtA, which methylates a phosphate on the Kdo2 sugar of lipid A. The model is classified as exception (more specific than equivalog) to reflect that its scope is limited to the genus Leptospira, whereas homologs with matching activity might exist more broadly. Members of this family belong to the broader family of pfam04191, phospholipid methyltransferase, which includes a characterized yeast enzyme that acts on a range of unsaturated phospholipids [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
MALIEELDQQGNFLFRWRSYIPGFILLLSLYYLPYYQFLQGSYESNLYYAAACFVVSLLGLFVRCFVIGY
APARTSGRNTKEQVADVVNQEGIYSLVRHPLYVGNFLMYLGPVLYLRDFPLALVFILFFGFYYERIMFAE
EKFLRGKFGDAYLSWADKVPAFIPKLSGYVKPNLDFSIRNVLKREYPSLFGILVIFVVFDLIASYFNEFG
LWVVPWEVITEPQIWFFGIGLIFYIITRLIVKTTKLLEVEGR
>gnl|CDD|237975 cd00001, PTS_IIB_man, PTS_IIB, PTS system, Mannose/sorbose specific IIB subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIB PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation. The active site histidine receives a phosphate group from the IIA subunit and transfers it to the substrate
IVLARIDDRLIHGQVATTWTKELNANRIIVVNDEVANDELRKTLLKLAAPPGVKLRIFTVEKAIEAINSP
KYDKQRVFLLFKNPQDVLRLVEGGVPIKTINVGNMAFRPGKVQITKAVSLDEEDVAAFKELAQKGVKVEI
QMVPNDKKVDL
>gnl|CDD|237976 cd00002, YbaK_deacylase, This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia coli and other related bacterial proteins. These trans-acting, single-domain proteins are homologs of ProX and also the cis-acting prolyl-tRNA synthetase (ProRS) inserted (INS) editing domain. The bacterial amino acid trans-editing enzyme YbaK is a deacylase that hydrolyzes cysteinyl-tRNA(Pro)'s mischarged by prolyl-tRNA synthetase. YbaK also hydrolyzes glycyl-tRNA's, alanyl-tRNA's, seryl-tRNA's, and prolyl-tRNA's. YbaK is homologous to the INS domain of prolyl-tRNA synthetase (ProRS) as well as the trans-editing enzyme ProX of Aeropyrum pernix which hydrolyzes alanyl-tRNA's and glycyl-tRNA's
KTPAIRLLDKAKIPYELHEYEHDEDASDGLEAAEKLGLDPEQVFKTLVVEGDKKGLVVAVVPVDEELDLK
KLAKALGAKKVEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQD
LAKLTGAKFADI
>gnl|CDD|237977 cd00003, PNPsynthase, Pyridoxine 5'-phosphate (PNP) synthase domain; pyridoxal 5'-phosphate is the active form of vitamin B6 that acts as an essential, ubiquitous coenzyme in amino acid metabolism. In bacteria, formation of pyridoxine 5'-phosphate is a step in the biosynthesis of vitamin B6. PNP synthase, a homooctameric enzyme, catalyzes the final step in PNP biosynthesis, the condensation of 1-amino-acetone 3-phosphate and 1-deoxy-D-xylulose 5-phosphate. PNP synthase adopts a TIM barrel topology, intersubunit contacts are mediated by three ''extra'' helices, generating a tetramer of symmetric dimers with shared active sites; the open state has been proposed to accept substrates and to release products, while most of the catalytic events are likely to occur in the closed state; a hydrophilic channel running through the center of the barrel was identified as the essential structural feature that enables PNP synthase to release water molecules produced during the reaction from the closed, solvent-shielded active site
RLGVNIDHVATLRNARGTNYPDPVEAALLAEKAGADGITVHLREDRRHIQDRDVRLLRELVRTELNLEMA
PTEEMLEIALEVKPHQVTLVPEKREELTTEGGLDVAGQAEKLKPIIERLKDAGIRVSLFIDPDPEQIEAA
KEVGADRVELHTGPYANAYDKAEREAELERIAKAAKLARELGLGVNAGHGLNYENVKPIAKIPGIAELNI
GHAIISRALFVGLEEAVREMKDLI
>gnl|CDD|320674 cd00004, Sortase, Sortase domain. Sortases are cysteine transpeptidases, mainly found in Gram-positive bacteria, which either anchor surface proteins to peptidoglycans of the bacterial cell wall envelope or link proteins together to form pili by working alone, or in concert with other enzymes. They do so by catalyzing a transpeptidation reaction in which the surface protein substrate is cleaved at a conserved cell wall sorting signal and covalently linked to peptidoglycan for display on the bacterial surface. Sortases are grouped into different classes based on sequence, membrane topology, genomic positioning, and cleavage site preference. The different classes are called class A to F sortases. Most Gram-positive bacteria contain more than one sortase and it is thought that the different sortases attach different surface protein classes. The typical eight-stranded beta-barrel fold is observed in all known sortases, along with the conserved catalytic triad consisting of cysteine, histidine and arginine residues. Some sortases contain an N-terminal signal peptide only and the C-terminus serves as a membrane anchor, which represents a type I membrane topology, with the N-terminal enzymatic portion projecting towards the bacterial surface and the C-terminal end residing in the cytoplasm. Other sortases adopt a type II membrane topology, with the N-terminal hydrophobic segment inside the cytoplasm and the C-terminal enzymatic portion located across the plasma membrane. The N-terminus either functions as both a signal peptide for secretion and a stop-transfer signal for membrane anchoring. Sortases are also present in some Gram-negative and Archaebacterial species, but the functions of these enzymes are unknown
YEYIGILEIPKINLKLPVLSGTSYENLKIAPGRYYGSALGENGNIVIAGHNGNGGSHFGNLKKLKKGDEI
YLTDKGKTYTYKVTEIEEVEPTDVEVILVTSGDKDLTLITCTPYNGTKRLIVRAK
>gnl|CDD|187674 cd00005, CBM9_like_1, DOMON-like type 9 carbohydrate binding module of xylanases. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends
VATAKYGTPVIDGEVDDVWAKAEEITTDKKVSGTDGATATARTLWDEDNLYVLAEVKDPVLNKASANPWE
QDSVEIFVDENNAKTSSYEDDDAQYRVNFDNEQSFGGGAIAERFTSATKLTDGGYVVEAAIPLKTITPAA
GTVIGFDLQVNDADDGGKRIGVANWNDPTGNGYQDTSRFGVLLLV
>gnl|CDD|237978 cd00006, PTS_IIA_man, PTS_IIA, PTS system, mannose/sorbose specific IIA subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIA PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation. IIA subunits receive phosphoryl groups from HPr and transfer them to IIB subunits, which in turn phosphorylate the substrate
VGIIIATHGGFASGLLNSAEMILGEQENVEAIDFPPGESPDDLLEKIKAALAELDSGEGVLILTDLFGGS
PNNAAARLSMEHPPVEVIAGVNLPMLLEAARARELGLSLDELVENALEAGRE
>gnl|CDD|350199 cd00008, PIN_53EXO-like, FEN-like PIN domains of the 5'-3' exonucleases of DNA polymerase I, bacteriophage T4 RNase H and T5-5' nucleases, and homologs. PIN (PilT N terminus) domains of the 5'-3' exonucleases (53EXO) of multi-domain DNA polymerase I and single domain protein homologs, as well as, the PIN domains of bacteriophage T5-5'nuclease (T5FEN or 5'-3'exonuclease), bacteriophage T4 RNase H (T4FEN), bacteriophage T3 (T3 phage exodeoxyribonuclease) and other similar nucleases are included in this family. The 53EXO of DNA polymerase I recognizes and endonucleolytically cleaves a structure-specific DNA substrate that has a bifurcated downstream duplex and an upstream template-primer duplex that overlaps the downstream duplex by 1 bp. The T5-5'nuclease is a 5'-3'exodeoxyribonuclease that also exhibits endonucleolytic activity on flap structures (branched duplex DNA containing a free single-stranded 5'end). T4 RNase H, which removes the RNA primers that initiate lagging strand fragments, has 5'- 3'exonuclease activity on DNA/DNA and RNA/DNA duplexes and has endonuclease activity on flap or forked DNA structures. These nucleases are members of the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LVDGHHLAYRTFHANKGLTTSGEPVQAVYGFAKSILKALKEDSGDAVIVVFDAKKPSFRHEAYGGYKANR
AEKYAEEKPTPEDFFEQLALIKELVKLLGLARLEIPGYEADDVLASLVKKAEKEGYEVRIISADGDLYQL
LSDRVHVLSPTEGYLITP
>gnl|CDD|99707 cd00009, AAA, The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases
VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGH
FLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALY
DRLDIRIVIPL
>gnl|CDD|237980 cd00010, AAI_LTSS, AAI_LTSS: Alpha-Amylase Inhibitors (AAI), Lipid Transfer (LT) and Seed Storage (SS) Protein family; a protein family unique to higher plants that includes cereal-type alpha-amylase inhibitors, lipid transfer proteins, seed storage proteins, and similar proteins. Proteins in this family are known to play important roles, in defending plants from insects and pathogens, lipid transport between intracellular membranes, and nutrient storage. Many proteins of this family have been identified as allergens in humans. These proteins contain a common pattern of eight cysteines that form four disulfide bridges
LAPCLSYLTGGATAPPSDCCSGLKSVVKSDPKCLCAALNGPGASLLGLKNATRALALPAACGL
>gnl|CDD|153270 cd00011, BAR_Arfaptin_like, The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-like proteins, a dimerization module that binds and bends membranes. The BAR domain of Arfaptin-like proteins, also called the Arfaptin domain, is a dimerization, lipid binding and curvature sensing module present in Arfaptins, PICK1, ICA69, and similar proteins. Arfaptins are ubiquitously expressed proteins implicated in mediating cross-talk between Rac, a member of the Rho family GTPases, and Arf (ADP-ribosylation factor) small GTPases. Arfaptins bind to GTP-bound Arf1, Arf5, and Arf6, with strongest binding to GTP-Arf1. Arfaptins also binds to Rac-GTP and Rac-GDP with similar affinities. The Arfs are thought to bind to the same surface as Rac, and their binding is mutually exclusive. Protein Interacting with C Kinase 1 (PICK1) plays a key role in the trafficking of AMPA receptors, which are critical for regulating synaptic strength and may be important in cellular processes involved in learning and memory. Islet cell autoantigen 69-kDa (ICA69) is a diabetes-associated autoantigen that is involved in membrane trafficking at the Golgi complex in neurosecretory cells. ICA69 associates with PICK1 through their BAR domains to form a heterodimer which is involved in regulating the synaptic targeting and surface expression of AMPA receptors. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
DLELELQLELLRETKRKYESVLQLGRALTAHLYSLSQTQHALGDAFADLSQKDPELAGEEFGYNAEAQKL
LCKNGETLLGAVNFFVSSINTLVTKAIEDTLLTVKQYEAARLEYDAYRLDLKELSLEPRDDTAGTRGRLR
SAQATFQEHRDKFEKLRGDVAIKLKFLEENKIKVMHKQLLLFHNTVSAYFAGNQKVLEQTLQQ
>gnl|CDD|466786 cd00012, ASKHA_ATPase-like, ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily. The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I & II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion
LGIDLGSTSTKVAVPIVITVAAGDRDANRVATITEAILLLQTNAATFALFTGPPVRIVNEAVAAAIGALL
TLGPEGLLVVDLGGGTDISANVVLVGGGARNNGLAKRLKELLLFRGGLKVVKAVDPDEAVALGAA
>gnl|CDD|200435 cd00013, ADF_gelsolin, Actin depolymerization factor/cofilin- and gelsolin-like domains. Actin depolymerization factor/cofilin-like domains are present in a family of essential eukaryotic actin regulatory proteins; these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments
DWVLFKVDAKKEEIVVGSTGAGFLDEFLEELPEDDPRYAFYRFKYPHSDDKRSKFVFISWIPDGVSIKQK
MVYATNKQTLKEALFGLAVPVQIRDGD
>gnl|CDD|409031 cd00014, CH_SF, calponin homology (CH) domain superfamily. CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav)
EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACK
KLGLPELDLFEPEDLYEKGNLKKVLGTLWALAL
>gnl|CDD|237982 cd00015, ALBUMIN, Albumin domain, contains five or six internal disulphide bonds; albuminoid superfamily includes alpha-fetoprotein which binds various cations, fatty acids and bilirubin; vitamin D-binding protein which binds to vitamin D, its metabolites, and fatty acids; alpha-albumin which binds water, cations (such as Ca2+, Na+ and K+), fatty acids, hormones, bilirubin and drugs; and afamin of which little is known; these belong to a multigene family with highly conserved intron/exon organization and encoded protein structures; evolutionary comparisons strongly support vitamin D-binding protein as the original gene in this group with subsequent local duplications generating the remaining genes in the cluster
KQICSRLKKLGERDFKALTLVRYSQKAPQATFEELVKLVKEVTKVAKKCCAGDKAPECAEEELSALLDEL
CSDEEKLSISPGVSHCCEKSGLERRPCFLALKKDEPPVPPSFNPFVFPEDEEVCQAFEEDPQKFLGRFLY
EYSRRHPELSVPELLRLAKEYEELLEKCCAAEDKEACFDTKRAEL
>gnl|CDD|293732 cd00016, ALP_like, alkaline phosphatases and sulfatases. This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases
KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTG
NGSADPELPSRAAGKDEDGPTIPELLKQAGYRTGVIGLLKAIDETSKEKPFVLFLHFDGPDGPGHAYGPN
TPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADGKADKSHTGMRVPFIAY
GPGVKKGGVKHELISQYDIAPTLADLL
>gnl|CDD|237984 cd00017, ANATO, Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to repeats in fibulins
KNSEKAAQYKDKELRKCCLDGMRENPMGQTCEERAAYITDGKECRKAFLECCVYAEELRDEEREDGLGLA
>gnl|CDD|237985 cd00018, AP2, DNA-binding domain found in transcription regulators in plants such as APETALA2 and EREBP (ethylene responsive element binding protein). In EREBPs the domain specifically binds to the 11bp GCC box of the ethylene response element (ERE), a promotor element essential for ethylene responsiveness. EREBPs and the C-repeat binding factor CBF1, which is involved in stress response, contain a single copy of the AP2 domain. APETALA2-like proteins, which play a role in plant development contain two copies
SKYRGVRQRPWGKWVAEIRDPSGGRRIWLGTFDTAEEAARAYDRAALKLRGSSAVLNFPDS
>gnl|CDD|237986 cd00019, AP2Ec, AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites; the alignment also contains hexulose-6-phosphate isomerases, enzymes that catalyze the epimerization of D-arabino-6-hexulose 3-phosphate to D-fructose 6-phosphate, via cleaving the phosphoesterbond with the sugar
IGAHVSAAGFGLENALKRAKEIGFDTVAMFLGNPRSWLSRPLKKERAEKFKAIAEEGPSICLSVHAPYLI
NLASPDKEKREKSIERLKDEIERCEELGIRLLVFHPGSYLGQSKEEGLKRVIEALNELIDKAETKGVVIA
LETMAGQGNEIGSSFEELKEIIDLIKEKPRVGVCIDTCHIFAAGYDISTVEGFEKVLEEFDKVIGLEYLK
AIHLNDSKGELGSGKDRHEPIGEGDIDGEELFKELKKDPYQNIPLILETPSENRDAAKIKKEIKLLRKL
>gnl|CDD|380813 cd00021, Bbox_SF, B-box-type zinc finger superfamily. The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interactions. Based on different consensus sequences and the spacing of the 7-8 zinc-binding residues, B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2)
MCQEHDEEKANKYCVTCEVLYCALCKKSGAHPDHEVAPL
>gnl|CDD|237989 cd00022, BIR, Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger
EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL
>gnl|CDD|237990 cd00023, BBI, Bowman-Birk type proteinase inhibitor (BBI); family of plant serine protease inhibitors that block trypsin or chymotrypsin.They are either single-headed (one reactive site, one inactive site, present mainly in monocotyledonous seeds) or double-headed (two reactive sites, present mainly in dicotyledonous seeds)
CCDNCVCTRSIPPQCRCVDVVSSCHSACKSCVCTRSNPPKFRCLDTYDGFCGPPC
>gnl|CDD|349274 cd00024, CD_CSD, CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains. Members of this group are chromodomains or chromo shadow domains; these are SH3-fold-beta-barrel domains of the chromo-like superfamily. Chromodomains lack the first strand of the SH3-fold-beta-barrel, this first strand is altered by insertion in the chromo shadow domains. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. Chromodomain-containing proteins include: i) those having an N-terminal chromodomain followed by a related chromo shadow domain, such as Drosophila and human heterochromatin protein Su(var)205 (HP1), and mammalian modifier 1 and 2; ii) those having a single chromodomain, such as Drosophila protein Polycomb (Pc), mammalian modifier 3, human Mi-2 autoantigen, and several yeast and Caenorhabditis elegans proteins of unknown function; iii) those having paired tandem chromodomains, such as mammalian DNA-binding/helicase proteins CHD-1 to CHD-4 and yeast protein CHD1; (iv) and elongation factor eEF3, a member of the ATP-binding cassette (ABC) family of proteins, that serves an essential function in the translation cycle of fungi. eEF3 is a soluble factor lacking a transmembrane domain and having two ABC domains arranged in tandem, with a unique chromodomain inserted within the ABC2 domain
YEVEKILDHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPELIKEYEK
>gnl|CDD|237992 cd00025, BPI1, BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) N-terminal domain; binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria.; Apolar pockets on the concave surface bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide
GAVARLSPKGLKFAKQQGLKVLQAELEKLQIPDILGAMKIKLLGKGRVGLSNKEIQELKLPSSSIKLVEV
KGLDLSISNVSIGLSGVWKYNYRFILDGGNVELSVEGMNIQADLRLGRDPSGRPKLSLSDCSSTVGSLRV
HLGGSLGWLAKLFMNFIESLLKKVLKGQLCPVIDASLVSMLESLLQLPKLPPVDSNAGVDYSLTSPPVLT
ASYLDSDIKGTFQ
>gnl|CDD|237993 cd00026, BPI2, BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) C-terminal domain; binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria.; Apolar pockets on the concave surface bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide
MVYLAVSEHVFNSAALVYFQAGALNLLLTDDMPPSKSRLTTSIFGIFIPELAKKYPNMPQQLKISVSSPP
HLVLSEGGATLAQQLDVEIFATLPDSQLRPLFRLGVDTSSSAQLSVSKKKLIGSLNLDRFLLELKSSNIG
SFIPELLQAILTTILEITVLPNVNDKLRRGFPLPLPKNFTLYDAEIQVHKDFLLLGADVQ
>gnl|CDD|349339 cd00027, BRCT, C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains. The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage
LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLDC
>gnl|CDD|237995 cd00028, B_lectin, Bulb-type mannose-specific lectin. The domain contains a three-fold internal repeat (beta-prism architecture). The consensus sequence motif QXDXNXVXY is involved in alpha-D-mannose recognition. Lectins are carbohydrate-binding proteins which specifically recognize diverse carbohydrates and mediate a wide variety of biological processes, such as cell-cell and host-pathogen interactions, serum glycoprotein turnover, and innate immune responses
SNPLSSGQTLVSSGSLFELGFFKLIMQSRDYNLILYKGSSRTVVWVANRDNPSGSSCTLTLQSDGNLVIY
DGSGTVVWSSNTTRVNGNYVLVLLDDGNLVLYDSDGNFLWQSFDYP
>gnl|CDD|410341 cd00029, C1, protein kinase C conserved region 1 (C1 domain) superfamily. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme
HRFVPTTFSSPTFCDVCGKLIWGLFKQGLKCSDCGLVCHKKCLDKAPSPC
>gnl|CDD|175973 cd00030, C2, C2 domain. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPESDTLTVEVWDK
DRFSKDDFLGEVEIPLSELLDSGKEGELWLPL
>gnl|CDD|206635 cd00031, CA_like, Cadherin repeat-like domain. Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers. This family also includes the cadherin-like repeats of extracellular alpha-dystroglycan
IPDGSAVEGRSRGSFRVSIPTDLIASSGEIIKISAAGKEALPSWLHWEPHSGILEGLEKLDREDKGVHYI
SVSAASLGANVPQTSSVFSIEVYDENDN
>gnl|CDD|237997 cd00032, CASc, Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent aspartate-directed proteases that mediate programmed cell death (apoptosis). Caspases are synthesized as inactive zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologs
IYKMNSKRRGLALIINNENFDKGLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPD
HSDSDSFVCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDS
GADEPPDVETEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILT
KVNRKVAEKFESVNGKKQMPCFRSTLTKKLYFF
>gnl|CDD|153056 cd00033, CCP, Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system. SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function
CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE
>gnl|CDD|349275 cd00034, CSD, chromo shadow domain. The chromo shadow domain (CSD) is always found in association with a related N-terminal chromo (CHRromatin Organization MOdifier) domain. CSD domains have only been found in proteins that also possess a chromodomain, while chromodomains can exist in isolation. CSDs are found for example in Drosophila and human heterochromatin protein (HP1) and mammalian modifier 1 and modifier 2. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. The HP1 CSD, in addition to interacting with various proteins bearing the PXVXL motif, also interacts with a region of histone H3 that bears the similar PXXVXL motif. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3). The CSD domains of all three human HP1 homologs have similar affinities to the PXXVXL motif of histone H3
LEVEKILGATDSDGELMFLIKWKGSDEADLVPAKEANEKCPQIVIQFYESRL
>gnl|CDD|211311 cd00035, ChtBD1, Hevein or type 1 chitin binding domain. Hevein or type 1 chitin binding domain (ChtBD1), a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements
RCGSQAGGPPCPNNLCCSQYGYCGTGDDYCGEGCQSQCD
>gnl|CDD|213175 cd00036, ChtBD3, Chitin/cellulose binding domains of chitinase and related enzymes. This group contains proteins related to the cellulose-binding domain of Erwinia chrysanthemi endoglucanase Z (EGZ) and Serratia marcescens chitinase B (ChiB). Gram negative plant parasite Erwinia chrysanthemi produces a variety of depolymerizing enzymes to metabolize pectin and cellulose on the host plant. Cellulase EGZ has a modular structure, with an N-terminal catalytic domain linked to a C-terminal cellulose-binding domain (CBD). CBD mediates the secretion activity of EGZ. Chitinases allow certain bacteria to utilize chitin as a energy source. Typically, non-plant chitinases are of the glycosidase family 18. Bacillus circulans Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal catalytic domain, and 2 fibronectin type III-like domains. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiA1 chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)). Streptomyces griseus Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. ChiC contains the characteristic chitin-binding aromatic residues. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source
AWPNPTHYTAGQSVVYNGNLYTANWYTAGSVPGSDSSWTQ
>gnl|CDD|153057 cd00037, CLECT, C-type lectin (CTL)/C-type lectin-like (CTLD) domain. CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model
SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKWSDGSP
LVDYTNWAPGEPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK
>gnl|CDD|237999 cd00038, CAP_ED, effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels
LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFG
ELALLGNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL
>gnl|CDD|119409 cd00039, COLIPASE, Colipase; a stoichiometric cofactor for pancreatic lipase, allowing the enzyme to anchor itself to the water-lipid interface and stabilizing the active enzyme conformation
APDPRGIIINLEAGELCLNSAQCKSGCCQHASSLSLARCAAKASENSECSPQTLYGVYYKCPCERGLTCE
GDKSIVGSITNTNYGICLDA
>gnl|CDD|238000 cd00040, CSF2, Granulocyte Macrophage Colony Stimulating Factor (GM-CSF) is a member of the large family of polypeptide growth factors called cytokines. It stimulates a wide variety of hematopoietic and nonhematopoietic cell types via binding to members of the cytokine receptor family, mainly the GM-CSF receptor
APTRSPSPVTRPWQHVDAIKEALSLLNNSNDTAAVMNETVEVVSEMFDPQEPTCLQTRLKLYKQGLRGSL
TKLKGPLTMMASHYKQHCPPTPETSCETQIITFKSFKENLKDFLFDIPFDC
>gnl|CDD|238001 cd00041, CUB, CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast
CGGTLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSS
PLLGRFCGSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA
>gnl|CDD|238002 cd00042, CY, Cystatin-like domain; Cystatins are a family of cysteine protease inhibitors that occur mainly as single domain proteins. However some extracellular proteins such as kininogen, His-rich glycoprotein and fetuin also contain these domains
GGPSDIPANDPEVQELADFAVAEYNKKSNDKYLEFFKVLSAKSQVVAGTNYYITVEAGDTNCKKSSVPLD
CPDCKLLEEGKKKFCTAKVWEKPWENFKELLSFKC
>gnl|CDD|410207 cd00043, CYCLIN_SF, Cyclin box fold superfamily. The cyclin box is a protein binding domain that functions in cell-cycle and transcriptional control. It is about 100 amino acids in length, composed of five helices, and is present in cyclins, transcription initiation factor IIB (TFIIB), and retinoblastoma tumour suppressor protein (Rb). Cyclins consist of 8 classes of cell cycle regulators that function as regulatory subunits of cyclin-dependent kinases (CDKs), which are serine/threonine kinases. The catalytic activities of CDKs are modulated not only by their interactions with cyclins but also by CDK inhibitors (CKIs). CDKs, cyclins and CKIs play key roles in transcription, epigenetic regulation, metabolism, stem cell self-renewal, neuronal functions, and spermatogenesis. TFIIB is a transcription factor that binds the TATA box. Members in this superfamily contain one or two copies of the cyclin box
KAVDFIRRLCSKLGLPEEVLELAIELLDRFLSKGLLLGRSPELIAAACLYLACKLEELPRTLKEIAKVSG
VSEKELRKAEKE
>gnl|CDD|238004 cd00044, CysPc, Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. Functions in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction
TLLQICLLSGVLFEDPDFPPNDSSLGFDDSLSNGQPKKVIEWKRPSEIFADDGNSNPRLFVNGASPSDVC
QGILGDCWFLAALAALAERPELLKRVIPPDQSFEENYAGIYHFRFWKNGEWVEVVIDDRLPTSNGGLLFM
HSRDRNELWVALLEKAYAKLHGSYEALVGGNTAEALEDLTGGPTERIDLKSADASSGDNDLFALLLSFLQ
GGSLIGCSTGSRSEEEARTANGLVKGHAYSVLDVREVQEEGLRLLRLRNPWGVGEWWGGWSDDSSEWWVI
DAERKKLLLSGKDDGEFWMSFEDFLRNFDGLYVCN
>gnl|CDD|260016 cd00045, DED, Death Effector Domain: a protein-protein interaction domain. Death Effector Domains comprise a subfamily of the Death Domain (DD) superfamily. DED-containing proteins include Fas-Associated via Death Domain (FADD), Astrocyte phosphoprotein PEA-15, the initiator caspases (caspase-8 and -10), and FLICE-inhibitory protein (FLIP), among others. These proteins are prominent components of the programmed cell death (apoptosis) pathway. Some members also have non-apoptotic functions such as regulation of insulin signaling (DEDD and PEA15) and cell cycle progression (DEDD). DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes
YRQLLLKISDELTSEELRSLKFLCKDVIPAGKLERISRGRDLFTELEKQGKISPGNLSLLEELLRSIGRR
DLLEKVE
>gnl|CDD|350668 cd00046, SF2-N, N-terminal DEAD/H-box helicase domain of superfamily 2 helicases. The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region
GENVLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLRELFGPGIRVAVLVGGSSAE
EREKNKLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV
ILLSAT
>gnl|CDD|350343 cd00047, PTPc, catalytic domain of protein tyrosine phosphatases. Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active
YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEY
GDITVTLVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG
PIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE
>gnl|CDD|380679 cd00048, DSRM_SF, double-stranded RNA binding motif (DSRM) superfamily. DSRM (also known as dsRBM) is a 65-70 amino acid domain that adopts an alpha-beta-beta-beta-alpha fold. It is not sequence specific, but highly specific for double-stranded RNAs (dsRNAs) of various origin and structure. The DSRM domains are found in a variety of proteins including dsRNA dependent protein kinase PKR, RNA helicases, Drosophila Staufen protein, E. coli RNase III, RNase H1, and dsRNA dependent adenosine deaminases. They are involved in numerous cellular mechanisms ranging from localization and transport of messenger RNAs, through maturation and degradation of RNAs, to viral response and signal transduction. Some members harbor tandem DSRMs that act in small RNA biogenesis
NELCQKNKWPPPEYETVEEGGPHNPRFTCTVTVNGQTFEGEGKSKKEAKQAAAEKAL
>gnl|CDD|199811 cd00049, MH1, N-terminal Mad Homology 1 (MH1) domain. The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. Receptor-regulated SMAD proteins (R-SMADs, including SMAD1, SMAD2, SMAD3, SMAD5, and SMAD9) are activated by phosphorylation by transforming growth factor (TGF)-beta type I receptors. The active R-SMAD associates with a common mediator SMAD (Co-SMAD or SMAD4) and other cofactors, which together translocate to the nucleus to regulate gene expression. The inhibitory or antagonistic SMADs (I-SMADs, including SMAD6 and SMAD7) negatively regulate TGF-beta signaling by competing with R-SMADs for type I receptor or Co-SMADs. MH1 domains of R-SMAD and SMAD4 contain a nuclear localization signal as well as DNA-binding activity. The activated R-SMAD/SMAD4 complex then binds with very low affinity to a DNA sequence CAGAC called SMAD-binding element (SBE) via the MH1 domain
PIVKRLLGWKQGGEEEKWAKKAVKSLVKKLKEKKQLDSLEKAITTQGGVPSKCVTIPRSLDGRLQVAHRK
GLPHVIYCRLWRWPDLHSHHELKALELCQFAFNMKKDEVCVNPYHYQRVES
>gnl|CDD|199819 cd00050, MH2, C-terminal Mad Homology 2 (MH2) domain. The MH2 domain is found in the SMAD (small mothers against decapentaplegic) family of proteins and is responsible for type I receptor interactions, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain which prevents it from forming a complex with SMAD4. The MH2 domain is multifunctional and provides SMADs with their specificity and selectivity, as well as transcriptional activity. Several transcriptional co-activators and repressors have also been reported to regulate SMAD signaling by interacting with the MH2 domain. Mutations in the MH2 domains of SMAD2 and especially SMAD4 have been detected in colorectal and other human cancers
WCSIAYYELNTRVGELFHVYSPSVAVDGFTDPSNGDRFCLGQLSNVNRNETIERTRRHIGKGVHLYYVGG
EVWAECLSDHAIFVQSRNLDYPHGRHPLTVCKIPPGCSIKVFDNQEFAQLLHQSVNTGFEGVYELTKMCT
IRMSFVKGWGPEYHRQDITSTPCWIEIHLH
>gnl|CDD|238008 cd00051, EFh, EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers
ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA
>gnl|CDD|238009 cd00052, EH, Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I) [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs
YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN
>gnl|CDD|238010 cd00053, EGF, Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium
ECAASNPCSNGGTCVNTPGSYRCVCPPGYTGDRSCE
>gnl|CDD|238011 cd00054, EGF_CA, Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements
DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE
>gnl|CDD|238012 cd00055, EGF_Lam, Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ
>gnl|CDD|238013 cd00056, ENDO3c, endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
FEVLVSEILSQQTTDKAVNKAYERLFERYGPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEG
FGGLVLDDPDAREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKTPEELEELLEE
LLPKPYWGEANQALMDLG
>gnl|CDD|238014 cd00057, FA58C, Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes
EPLGMESGLADDQITASSSYSSGWEASRARLNSDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGG
SSEWVTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLE
LYG
>gnl|CDD|466989 cd00058, beta-trefoil_FGF, FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) superfamily. The FGF superfamily includes FGF1-23 and similar proteins. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. They play essential roles in patterning and differentiation during vertebrate embryogenesis and have neurotrophic activities. FGFs have a high affinity for heparan sulfate proteoglycans and require heparan sulfate to activate one of four cell surface FGF receptors. Upon binding to FGF, the receptors dimerize, and their intracellular tyrosine kinase domains become active. The structure of FGFs is typical of the beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry
RLVRLYSRTGYFLQILPDGTVNGTKDENSPYAILELQSVGTGLVRIKGVKTGRYLAMDKNGKLYGTKKPT
EDCVFKETLEENGYNTYSSYKYYHTRKGWYLAIKKNGKPKRGKKTKPGQKSTQFLPL
>gnl|CDD|410788 cd00059, FH_FOX, Forkhead (FH) domain found in Forkhead box (FOX) family of transcription factors and similar proteins. The FOX family comprises diverse tissue- and cell type-specific transcription factors with an evolutionary conserved "Forkhead (FH)" or "winged helix" DNA-binding domain. FH is named for the Drosophila fork head protein, a transcription factor which promotes terminal rather than segmental development. The structure of the FH domain contains 2 flexible loops or "wings" in the C-terminal region, hence the term winged helix. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'. They participate in a variety of cellular processes, such as cell cycle progression, proliferation, differentiation, migration, metabolism, and DNA damage response. Their expression can be regulated by multiple factors, and they can act as co-activators and/or transcriptional repressors. Fifty FOX-encoding genes in humans have been categorized into 19 subfamilies based on protein sequence homology (FOXA to FOXS)
PPYSYAALIALAILSSPDKRLTLSEIYKWIEDNFPYYRTATKGWKNSIRHNLSLNKCFVKVPREPSDPGK
GSYWT
>gnl|CDD|438714 cd00060, FHA, forkhead associated (FHA) domain superfamily. Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function
RLIVLDGDGGGREFPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTFVNGKRI
TPPVPLQDGDVIRLGDTTFRFE
>gnl|CDD|238018 cd00061, FN1, Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. FN1 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. FN1 domains also found in coagulation factor XII, HGF activator, and tissue-type plasminogen activator. In tissue plasminogen activator, FN1 domains may form functional fibrin-binding units with EGF-like domains C-terminal to FN1
EKCFDPQTGVFYRVGETWERPSEGHVLQCTCLGNRGEARCDPV
>gnl|CDD|238019 cd00062, FN2, Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats
NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC
>gnl|CDD|238020 cd00063, FN3, Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases
PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEY
EFRVRAVNGGGESPPSESVTVTT
>gnl|CDD|238021 cd00064, FU, Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors
PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL
>gnl|CDD|277249 cd00065, FYVE_like_SF, FYVE domain like superfamily. FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger
RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGSGKPVRVCDSCY
>gnl|CDD|206639 cd00066, G-alpha, Alpha subunit of G proteins (guanine nucleotide binding). The alpha subunit of G proteins contains the guanine nucleotide binding site. The heterotrimeric GNP-binding proteins are signal transducers that communicate signals from many hormones, neurotransmitters, chemokines, and autocrine and paracrine factors. Extracellular signals are received by receptors, which activate the G proteins, which in turn route the signals to several distinct intracellular signaling pathways. The alpha subunit of G proteins is a weak GTPase. In the resting state, heterotrimeric G proteins are associated at the cytosolic face of the plasma membrane and the alpha subunit binds to GDP. Upon activation by a receptor GDP is replaced with GTP, and the G-alpha/GTP complex dissociates from the beta and gamma subunits. This results in activation of downstream signaling pathways, such as cAMP synthesis by adenylyl cyclase, which is terminated when GTP is hydrolized and the heterotrimers reconstitute
VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNIPYGDPENEKD
AKKILSLAPRAEEGPLPPELAEAIKRLWKDPGIQACYDRRNEYQLNDSAKYFLDNLDRISDPDYIPTEQD
ILRSRVKTTGIIETDFSIKNLKFRMFDVGGQRSERKKWIHCFEDVTAIIFVVALSEYDQVLVEDESVNRM
QESLKLFDSICNSRWFANTSIILFLNKKDLFEEKIKKSPLTDYFPDYTGPPNDYEEAAKYIKKKFLDLNR
NPNKEIYPHFTCATDTENIRFVFDAVKDIILQNNL
>gnl|CDD|238023 cd00067, GAL4, GAL4-like Zn2Cys6 binuclear cluster DNA-binding domain; found in transcription regulators like GAL4. Domain consists of two helices organized around a Zn(2)Cys(6)motif; Binds to sequences containing 2 DNA half sites comprised of 3-5 C/G combinations
RVRRACDRCRRRKIKCDGEKPPCSNCIKLGLECTYS
>gnl|CDD|238024 cd00068, GGL, G protein gamma subunit-like motifs, the alpha-helical G-gamma chain dimerizes with the G-beta propeller subunit as part of the heterotrimeric G-protein complex; involved in signal transduction via G-protein-coupled receptors
VDQLKKEVEQLRKELSRERLKVSKAAAELLKYCEQNAENDPLLTGPPSPSNPWIEKK
>gnl|CDD|200450 cd00069, GHB_like, Glycoprotein hormone beta chain homologues. This family of cystine-knot hormones includes the beta chains of gonadotropins, thyrotropins, follitropins, choriogonadotropins and more. The members are reproductive hormones that consist of two glycosylated chains (alpha and beta), which form a tightly bound dimer
CHPRNYTIAVEKEGCGVCLAINTTICAGRCDTRDPVYKSPPYKPSHQPVCTYDEWRYETVRLPGCPPGVD
PTYTYPVALSCRCGLCNTDTTDCTRL
>gnl|CDD|238025 cd00070, GLECT, Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation
PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSSDIALHFNPRFDENVIVRNSFLNGNWGPEERSG
GFPFQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE
>gnl|CDD|238026 cd00071, GMPK, Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines
LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAE
FHGNYYGTSKAAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPPDYVIVNDDLEKAYEELK
>gnl|CDD|238027 cd00072, GYF, GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and other proteins. Involved in signaling lymphocyte activity. Also present in other unrelated proteins (mainly unknown) derived from diverse eukaryotic species
EVQWFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRLDNGGEFYTLGDILFDLG
>gnl|CDD|238028 cd00073, H15, linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, consisting of an octamer of core histones, two full turns of DNA, a linker histone (H1 or H5) and a variable length of linker DNA; H1/H5 are chromatin-associated proteins that bind to the exterior of nucleosomes and dramatically stabilize the highly condensed states of chromatin fibers; stabilization of higher order folding occurs through electrostatic neutralization of the linker DNA segments, through a highly positively charged carboxy- terminal domain known as the AKP helix (Ala, Lys, Pro); thought to be involved in specific protein-protein and protein-DNA interactions and play a role in suppressing core histone tail domain acetylation in the chromatin fiber
PPSHPPYSEMVTEAIKALKERKGSSLQAIKKYIEAKYKVDDENFNKLLKLALKKGVAKGKLVQVKGTGAS
GSFKLSKKKKKKKKPAKK
>gnl|CDD|467020 cd00074, HFD_H2A, histone-fold domain found in histone H2A and similar proteins. Histone H2A is the core component of the nucleosome, which wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA
QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQ
LAIRNDEELNKLFKGVTIA
>gnl|CDD|340391 cd00075, HATPase, Histidine kinase-like ATPase domain. This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains
LEQVLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKSREGGGTGL
GLAIVRRIVEAHGGRITVESEPGGGTTFTVTL
>gnl|CDD|467021 cd00076, HFD_SF, histone fold domain (HFD) superfamily. The histone fold domain (HFD) is a structurally conserved interaction motif involved in heterodimerization of the core histones and their assembly into the nucleosome octamer. Histone fold heterodimers play crucial roles in gene regulation. The minimal HFD consists of three alpha helices connected by two short, unstructured loops. The HFD is found in core histones, TATA box-binding protein-associated factors (TAFs), and many other transcription factors. HFD plays a role in the nucleosomal core particle by conserving histone interactions; these contain more than one HFD. The structure of the nucleosome core particle has two modes that have the largest interaction surfaces, and these are the H3-H4 and H2A-H2B heterodimer interactions. Several TAFs interact via histone-fold (HF) motifs. Five HF-containing TAF pairs have been described in transcription factor II D (TFIID): TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10
LLRSAVARILKSAGFDSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE
>gnl|CDD|238032 cd00077, HDc, Metal dependent phosphohydrolases with conserved 'HD' motif
EHRFEHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAITEEESELEKDHAIVGAEILRE
LLLEEVIKLIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRDSREKRRRIAEED
LEELL
>gnl|CDD|238033 cd00078, HECTc, HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains
LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPD
DSGLLYPNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKS
LKELLDNDGDEDDLELTFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEA
FRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERK
KFLQFVTGSSRLPVGGFADLNPKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAG
FG
>gnl|CDD|188616 cd00080, H3TH_StructSpec-5'-nucleases, H3TH domains of structure-specific 5' nucleases (or flap endonuclease-1-like) involved in DNA replication, repair, and recombination. The 5' nucleases of this superfamily are capable of both 5'-3' exonucleolytic activity and cleaving bifurcated or branched DNA, in an endonucleolytic, structure-specific manner, and are involved in DNA replication, repair, and recombination. The superfamily includes the H3TH (helix-3-turn-helix) domains of Flap Endonuclease-1 (FEN1), Exonuclease-1 (EXO1), Mkt1, Gap Endonuclease 1 (GEN1) and Xeroderma pigmentosum complementation group G (XPG) nuclease. Also included are the H3TH domains of the 5'-3' exonucleases of DNA polymerase I and single domain protein homologs, as well as, the bacteriophage T4 RNase H, T5-5'nuclease, and other homologs. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the C-terminal region of the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Both the H3TH domain and the helical arch/clamp region are involved in DNA binding. Studies suggest that a glycine-rich loop in the H3TH domain contacts the phosphate backbone of the template strand in the downstream DNA duplex. Typically, the nucleases within this superfamily have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors (i. e., Mg2+, Mn2+, Zn2+, or Co2+) required for nuclease activity. The first metal binding site is composed entirely of Asp/Glu residues from the PIN domain, whereas, the second metal binding site is composed generally of two Asp residues from the PIN domain and one or two Asp residues from the H3TH domain. Together with the helical arch and network of amino acids interacting with metal binding ions, the H3TH region defines a positively charged active-site DNA-binding groove in structure-specific 5' nucleases
EQFIDLCALVGCDYSDNPGVPGIGPKTAAKLALKYGSLEGILENLDELKGKKREKLEEPKEYAFLSRKLA
T
>gnl|CDD|238035 cd00081, Hint, Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins and undergo protein splicing (e.g. DnaB, RIR1-2, GyrA and Pol). In protein splicing an intervening polypeptide sequence - the intein - is excised from a protein, and the flanking polypeptide sequences - the exteins - are joined by a peptide bond. In addition to the autocatalytic splicing domain, many inteins contain an inserted endonuclease domain, which plays a role in spreading inteins. Hedgehog proteins are a major class of intercellular signaling molecules, which control inductive interactions during animal development. The mature signaling forms of hedgehog proteins are the N-terminal fragments, which are covalently linked to cholesterol at their C-termini. This modification is the result of an autoprocessing step catalyzed by the C-terminal fragments, which are aligned here
CFTGDTLVLLEDGGRKKIEELVEKKGDKVLALDETGKLVFSKVLKVLRRDYEKKFYKIKTESGREITLTP
DHLLFVLEDGELKWVFASDLKPGDYVLVPVLEKVKEIEEIEYTGGVYDLTVEDNHNFIANGVLVHN
>gnl|CDD|119399 cd00082, HisKA, Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes
LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR
>gnl|CDD|381392 cd00083, bHLH_SF, basic Helix Loop Helix (bHLH) domain superfamily. bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. Members of the bHLH superfamily have two highly conserved and functionally distinct regions. The basic part is at the amino end of the bHLH that may bind DNA to a consensus hexanucleotide sequence known as the E box (CANNTG). Different families of bHLH proteins recognize different E-box consensus sequences. At the carboxyl-terminal end of the region is the HLH region that interacts with other proteins to form homo- and heterodimers. bHLH proteins function as a diverse set of regulatory factors because they recognize different DNA sequences and dimerize with different proteins. The bHLH proteins can be divided to cell-type specific and widely expressed proteins. The cell-type specific members of bHLH superfamily are involved in cell-fate determination and act in neurogenesis, cardiogenesis, myogenesis, and hematopoiesis
ERRRRDKINDAFEELKRLLPELPDSKKLSKASILQKAVEYIRELQS
>gnl|CDD|438789 cd00084, HMG-box_SF, high mobility group (HMG)-box domain superfamily. The High Mobility Group (HMG)-box is found in a variety of eukaryotic chromosomal proteins and transcription factors. HMGs bind to the minor groove of DNA and have been classified by DNA binding preferences. Two phylogenetically distinct groups of Class I proteins bind DNA in a sequence specific fashion and contain a single HMG box. One group (SOX-TCF) includes transcription factors, TCF-1, -3, -4, and also SRY and LEF-1, which bind four-way DNA junctions and duplex DNA targets. The second group (MATA) includes fungal mating type gene products MC, MATA1 and Ste11. Class II and III proteins (HMGB-UBF) bind DNA in a non-sequence specific fashion and contain two or more tandem HMG boxes. Class II members include non-histone chromosomal proteins, HMG1 and HMG2, which bind to bent or distorted DNA such as four-way DNA junctions, synthetic DNA cruciforms, kinked cisplatin-modified DNA, DNA bulges, cross-overs in supercoiled DNA, and can cause looping of linear DNA. Class III members include nucleolar and mitochondrial transcription factors, UBF and mtTF1, which bind four-way DNA junctions
RPLSAYLLFSKEKRPKLKKENPDLSFTEISKLLGERWKELSEEEKQPYEEKAKEDKERY
>gnl|CDD|238038 cd00085, HNHc, HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins
RSHRLVLLARDGLCPYCGKPGGTEGLEVDHIIPLSDGGNNDLDNLVLLCRKCHRKKH
>gnl|CDD|238039 cd00086, homeodomain, Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner
RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE
>gnl|CDD|238040 cd00087, FReD, Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation
PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGN
LDGEFWLGLEKIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALSYHN
GMKFSTFDRDNDGASGNCAESYSGGWWYNSCHASNLNGRYYSGGHRNEYDNGINWATWKGSTYSLKFTEM
KIRPK
>gnl|CDD|238041 cd00088, HPT, Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades
MEELLELFLEEAEELLEELERALLELEDAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRD
GLEVTPELIDLLLDALDALKAELE
>gnl|CDD|212008 cd00089, HR1, Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases. The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region
SKLQQRLEELRRKLEKELKIREGAENLLKLYSNPKVKKDLAEVQLNLKESKEKIDLLKRQLERYNALV
>gnl|CDD|238042 cd00090, HTH_ARSR, Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions
LKALSDPTRLRILRLLLEGPLTVSELAERLGLSQSTVSRHLKKLEEAGLVESRREGRRVYYSLTDAERLL
ALLESLLE
>gnl|CDD|238043 cd00091, NUC, DNA/RNA non-specific endonuclease; prokaryotic and eukaryotic double- and single-stranded DNA and RNA endonucleases also present in phosphodiesterases. They exists as monomers and homodimers
LQYGRPGVLADTEVLSYTHYVLSYNRATRLPLWVAEHIDKEDLGKNVDRKYDQFKQDPRIPPLFSATNSD
YKGSGSLDRGHLAPAADPVWSQDAQDATFYLTNMAPQVQGFNQGNWAYLEDYLRDLAASEGKDVYVVTGP
LFLPDLDGDGGSYLSTQVINNGKVAVPTHFWKVIIDEKAPGNLSVGAFVLPNNNPHDTLEFILCVEKTFQ
VPVASVEKATGLSFFCNVPDSVSAVLELKKK
>gnl|CDD|238044 cd00092, HTH_CRP, helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic regulatory proteins belonging to the catabolite activator protein family
AKERLASFLLNLSLRYGAGDLVQLPLTRQEIADYLGLTRETVSRTLKELEEEGLISRRGRGKYRVNP
>gnl|CDD|238045 cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators
GERLKELRKEKGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALGVSLDEL
>gnl|CDD|238046 cd00094, HX, Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat
PDACDPLSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKG
DKYWVYTGKNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIE
TDFPGVPDKVDAAFRWLDGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC
>gnl|CDD|238047 cd00095, IFab, Interferon alpha, beta. Includes also interferon omega and tau. Different from interferon gamma family. Type I interferons(alpha, beta) belong to the larger helical cytokine superfamily, which includes growth hormones, interleukins, several colony-stimulating factors and several other regulatory molecules. All function as regulators of cellular activty by interacting with cell-surface receptors and activating various signalling pathways. Interferons produce antiviral and antiproliferative responses in cells. Receptor specificity determines function of the various members of the family
LRHQHRLFNRRCLKLLRQMRRLPPQSCLKDRADFGFPQELLQGDQFQKAQAASVLHEMLQQIFNIFSTPS
SSAAWNETLLESLLNELHQQLNHLETCLEQEMGEEETPGPRNTHLHLRKYFQRIQLYLKEKKYSPCAWEV
VRAEIMRNFSSI
>gnl|CDD|409353 cd00096, Ig, Immunoglobulin domain. The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV
>gnl|CDD|409354 cd00098, IgC1, Immunoglobulin Constant-1 (C1)-set domain. The members here are composed of C1-set domains, classical Ig-like domains resembling the antibody constant domain. Members of the IgC1 family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and major histocompatibility complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, while the IgC domain is involved in oligomerization and molecular interactions. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other strands by G, F, C, and C'
TVTLLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTSSPVEPNDGTYSVTSSLTVPPS
DWDEGATYTCVVTHESLKSPLSKTW
>gnl|CDD|409355 cd00099, IgV, Immunoglobulin variable domain (IgV). The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E and, D strands in one sheet and A', G, F, C, C', and C" strands in the other
VTQSPRSLSVQEGESVTLSCEVSSSFSSTYIYWYRQKPGQGPEFLIYLSSSKGKTKGGVPGRFSGSRDGT
SSFSLTISNLQPEDSGTYYCAVSESGGTDKLTFGSGTRLTV
>gnl|CDD|466776 cd00100, beta-trefoil_IL1, beta-trefoil domain found in the interleukin-1 (IL-1) family of cytokines. The IL-1 family of cytokines comprises 11 members, including 7 pro-inflammatory agonists (IL-1alpha, IL-1beta, IL-18, IL-33, IL-36alpha, IL-36beta, IL-36gamma) and 4 defined or putative antagonists (IL-1R antagonist (IL-1Ra), IL-36Ra, IL-37, and IL-38) exerting anti-inflammatory activities. These members can have complimentary or distinct biological functions. All family members share a common structure at the C-terminus, which is comprised by of a typical beta-trefoil fold consisting of 12-beta-strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry
EKRNFVIRDSNDKSLYLRGNNELVAEDLSDVEKSAKITIYYYKSDSDEDFKGIPVVLNFTGTNCFLSCVK
EGDKPSLQLEECNKEELKNGDEEEWPFVFYMKASHDNTCRFESAAHPGWFICTKKDQPVGLTKELGKTED
TDFYF
>gnl|CDD|238049 cd00101, IlGF_like, Insulin/insulin-like growth factor/relaxin family; insulin family of proteins. Members include a number of active peptides which are evolutionary related including insulin, relaxin, prorelaxin, insulin-like growth factors I and II, mammalian Leydig cell-specific insulin-like peptide (gene INSL3), early placenta insulin-like peptide (ELIP; gene INSL4), insect prothoracicotropic hormone (bombyxin), locust insulin-related peptide (LIRP), molluscan insulin-related peptides 1 to 5 (MIP), and C. elegans insulin-like peptides. Typically, the active forms of these peptide hormones are composed of two chains (A and B) linked by two disulfide bonds; the arrangement of four cysteines is conserved in the "A" chain: Cys1 is linked by a disulfide bond to Cys3, Cys2 and Cys4 are linked by interchain disulfide bonds to cysteines in the "B" chain. This alignment contains both chains, plus the intervening linker region, arranged as found in the propeptide form. Propeptides are cleaved to yield two separate chains linked covalently by the two disulfide bonds
LCGRELVRALIFVCGDRGFYRGIVDECCFRGCTLRELASYC
>gnl|CDD|238050 cd00102, IPT, Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers
PVITSISPSSGPVSGGTEVTITGSNFGSGSNLRVTFGGGVPCSVLSVSSTAIVCTTPPYANPGPGPVEVT
VDRGNGGITSSPLTFTYVP
>gnl|CDD|238051 cd00103, IRF, Interferon Regulatory Factor (IRF); also known as tryptophan pentad repeat. The family of IRF transcription factors is important in the regulation of interferons in response to infection by virus and in the regulation of interferon-inducible genes. The IRF family is characterized by a unique 'tryptophan cluster' DNA-binding region. Viral IRFs bind to cellular IRFs; block type I and II interferons and host IRF-mediated transcriptional activation
KMRLRPWLVEQVDSGTYPGLIWLDEEKTIFRIPWKHAARHDVQEADAKIFKAWAVERGIYQPGGTPDPAE
WKARLLCALRSSRGFEEVKDKSKDTPGDPHRVYRLLP
>gnl|CDD|238052 cd00104, KAZAL_FS, Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters), which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD
CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC
>gnl|CDD|411802 cd00105, KH-I, K homology (KH) RNA-binding domain, type I. KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability
EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGERVVTITGTPEAVEKAKELIE
>gnl|CDD|276812 cd00106, KISc, Kinesin motor domain. Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward
NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLV
DSALEGYNGTIFAYGQTGSGKTYTMLGPDPEQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEK
IYDLLSPVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTI
HVKQRNREKSGESVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPY
RDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK
>gnl|CDD|238055 cd00107, Knot1, The "knottin" fold is stable cysteine-rich scaffold, in which one disulfide bridge crosses the macrocycle made by two other disulfide bridges and the connecting backbone segments. Members include plant lectins/antimicrobial peptides, plant proteinase/amylase inhibitors, plant gamma-thionins, and arthropod defensins
GTCFSDSYCDKECKKKGASGGYCYGQGLACWCY
>gnl|CDD|238056 cd00108, KR, Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides
TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDP
NVRWEYCDIPRCE
>gnl|CDD|438633 cd00109, Kunitz-type, Kunitz/Bovine pancreatic trypsin inhibitor (BPTI) domain. This family contains the Kunitz domain which is a common structural fold found in a family of reversible serine protease inhibitors. This domain is thought to have evolved over 500 million years and is ubiquitous in all kingdoms of life and has been incorporated into many different genes. In general, each domain is encoded by a single exon. Some genes encode proteins with a single Kunitz domain, e.g. bovine pancreatic trypsin inhibitor (BPTI), trophoblast Kunitz domain protein (TKDP), amyloid beta-protein precursor (ABPP), as well as Kunitz-type venom peptides such as dendrotoxin. Genes that encode multiple Kunitz domains include hepatocyte growth factor activator inhibitors HAI1 and HAI2 (two domains), tissue factor pathway inhibitor TFPI1 and TFPI2 (three domains) and Caenorhabditis elegans papilin (eleven domains). In addition, the Kunitz domain has been integrated into multi-domain proteins, e.g. the collagen alpha3(VI), alpha1(VII) and alpha1(XXVIII) chains, WFIKKN1 (containing WAP, Follistatin/Kazal, Immunoglobulin, two Kunitz and NTR domains) and papilin. Furthermore, each domain within a multi-Kunitz domain protein may exhibit different protease activity, such as for the three tandemly repeated domains within both tissue factor pathway inhibitors 1 and 2. The Kunitz domain is a representative of alpha/beta proteins with irregular secondary structure stabilized by three disulfide bonds and presenting three peptide loops that can be varied without introducing much destabilization to the scaffold. Protease inhibitors meet the scaffold criteria in that they are small, stable and capable of evolving the binding activity of exposed peptide loops through targeted randomization to construct combinatorial libraries. Kunitz domain-based scaffolds have been successfully utilized to construct and select a library of protease inhibitors with the potential for therapeutic application
CLLPPDPGPCRAYFPRWYYNSETGQCEEFIYGGCGGNANNFETKEECEATC
>gnl|CDD|238058 cd00110, LamG, Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules
GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLV
LSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPG
FVGCIRDLKVN
>gnl|CDD|238059 cd00111, Trefoil, P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated molecules, largely found in epithelia of gastrointestinal tissues. Function is not known but it was originally identified from mucosal tissues, where it may have a regulatory or structural role and has also been implicated as a growth fractor in other tissues.The domain is found in 1 to 6 copies where it occurs
EWCSVPPSERIDCGPPGITQEECEARGCCFDPSISGVPWCFYPK
>gnl|CDD|238060 cd00112, LDLa, Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure
CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC
>gnl|CDD|238061 cd00113, PLAT, PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates
CRYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRR
DGSGLSDGWYCESITVQALGTKKVYTFPVNRWVLGGKWYTSVRSLK
>gnl|CDD|238062 cd00114, LIGANc, NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining the breaks in duplex DNA during DNA replication, repair and recombination, utilizing either ATP or NAD(+) as a cofactor, but using the same basic reaction mechanism. The enzyme reacts with the cofactor to form a phosphoamide-linked AMP with the amino group of a conserved Lysine in the KXDG motif, and subsequently transfers it to the DNA substrate to yield adenylated DNA. This alignment contains members of the NAD+ dependent subfamily only
ERIAELRELLNKHDYRYYVLDEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRH
PVPMLSLDNAFDEEELRAFDERIKRFLGEEPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTE
NVRTIRSIPLTLAGAPETLEVRGEVFMPKADFEALNKEREERGEKPFANPRNAAAGSLRQLDPKITAKRP
LRFFIYGLGEAEGLGPKTQSEALAFLKEWGFPVSPETRLCKNIEEVLAFYDEIEAKRDSLPYEIDGVVVK
VDDLALQRELGFTSKAPRWAIAYKFPA
>gnl|CDD|319970 cd00115, LMWP, Low molecular weight phosphatase family. Low molecular weight phosphatases (LMWPs) are a group of small soluble enzymes that are characterized by a highly conserved active site motif (V/I)CXGNXCRS and share no sequence similarity with other types of protein tyrosine phosphatases (PTPs). This family includes protein tyrosine phosphatases, arginine phosphatases and arsenate reductases
SILFICTGNICRSPMAEAIFKQLLGDEWKVDSAGTGAHHGEGADPRAVRVLKEVGIDISHRSDQIKSEHL
DNYDLVLVMDGSNLDKIPRIFPEARGKTWLPHVKLEHGEIDDPYRGDIEDFRRVRDELENASKRFAE
>gnl|CDD|238064 cd00116, LRR_RI, Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1)
LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRIPRGL
QSLLQGLTKGCGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALE
KLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGA
SALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESL
LELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF
>gnl|CDD|467060 cd00117, TFP, three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily. The LU (also known as Ly-6 antigen/uPA receptor)-like extracellular domain (ECD) occurs singly in GPI-linked cell-surface glycoproteins (Ly-6 family, CD59, thymocyte B cell antigen, Sgp-2) or as three-fold repeated domain in urokinase-type plasminogen activator receptor. It is a structural domain involved in protein-protein interactions, tolerating an unusual degree of variation and binding with high specificity to a broad spectrum of targets. The snake toxin domain is present in short and long neurotoxins, cytotoxins, and short toxins, and in other miscellaneous venom peptides. The toxin acts by binding to the nicotinic acetylcholine receptors in the postsynaptic membrane of skeletal muscles and preventing the binding of acetylcholine, thereby blocking the excitation of muscles. Both the LU-like ECD and the snake toxin domain belong to three-fingered protein (TFP) fold, which is characterized by containing 70 to 100 amino acids including eight to ten cysteine residues spaced at conserved distances
LKCYQCNSSNDPNCCNSSPTLVTCSSPETFCRKIVGKVGGGETLVIRGCATECECGCTECCSGTGTSGTT
CTSCCDTDLCN
>gnl|CDD|212030 cd00118, LysM, Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes
KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI
>gnl|CDD|340357 cd00119, LYZ, C-type lysozyme and alpha-lactalbumin. C-type lysozyme (chicken or conventional type, 1,4-beta-N-acetylmuramidase) and alpha-lactalbumin (lactose synthase B protein, LA). They have a close evolutionary relationship and similar tertiary structure, however, functionally they are quite different. Lysozymes have primarily bacteriolytic function; hydrolysis of peptidoglycans of prokaryotic cell walls and transglycosylation. LA is a calcium-binding metalloprotein that is expressed exclusively in the mammary gland during lactation. LA is the regulatory subunit of the enzyme lactose synthase. The association of LA with the catalytic component of lactose synthase, galactosyltransferase, alters the acceptor substrate specificity of this glycosyltransferase, facilitating biosynthesis of lactose. Some lysozymes have evolved into digestive enzymes, both in mammals and invertebrates
KVFTRCELARLLKDIGGYGGISLPNWVCLMKHESGYDTQATNENNNGSTDYGLFQINSRYWCKDGQTPGA
RNICDISCSKLLTDDITDAIMCAKKIVDDKGIDAWVAWKNHCQNKLRQYVSC
>gnl|CDD|238067 cd00120, MADS, MADS: MCM1, Agamous, Deficiens, and SRF (serum response factor) box family of eukaryotic transcriptonal regulators. Binds DNA and exists as hetero and homo-dimers. Composed of 2 main subgroups: SRF-like/Type I and MEF2-like (myocyte enhancer factor 2)/ Type II. These subgroups differ mainly in position of the alpha 2 helix responsible for the dimerization interface; Important in homeotic regulation in plants and in immediate-early development in animals. Also found in fungi
GRGKIEIKRIENKTSRQVTFSKRRNGLFKKASELSVLCDAEVAVIVFSPSGKLYEFWSS
>gnl|CDD|238068 cd00121, MATH, MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane and are capable of cleaving growth factors, extracellular matrix proteins, and biologically active peptides. TRAF molecules serve as adapter proteins that link cell surface receptors of the Tumor Necrosis Factor and 1nterleukin-1/Toll-like families to downstream kinase cascades, which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. Other members include the ubiquitin ligases, TRIM37 and SPOP, and the ubiquitin-specific proteases, HAUSP and Ubp21p. A large number of uncharacterized members mostly from lineage-specific expansions in C. elegans and rice contain MATH and BTB domains, similar to SPOP. The MATH domain has been shown to bind peptide/protein substrates in TRAFs and HAUSP. It is possible that the MATH domain in other members of this superfamily also interacts with various protein substrates. The TRAF domain may also be involved in the trimerization of TRAFs. Based on homology, it is postulated that the MATH domain in meprins may be involved in its tetramer assembly and that the MATH domain, in general, may take part in diverse modular arrangements defined by adjacent multimerization domains
GKHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESGDYLSLYLELDKGESDLEKWSVRAEFTL
KLVNQNGGKSLSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEVK
>gnl|CDD|238069 cd00122, MBD, MeCP2, MBD1, MBD2, MBD3, MBD4, CLLD8-like, and BAZ2A-like proteins constitute a family of proteins that share the methyl-CpG-binding domain (MBD). The MBD consists of about 70 residues and is defined as the minimal region required for binding to methylated DNA by a methyl-CpG-binding protein which binds specifically to methylated DNA. The MBD can recognize a single symmetrically methylated CpG either as naked DNA or within chromatin. MeCP2, MBD1 and MBD2 (and likely MBD3) form complexes with histone deacetylase and are involved in histone deacetylase-dependent repression of transcription. MBD4 is an endonuclease that forms a complex with the DNA mismatch-repair protein MLH1. The MBDs present in putative chromatin remodelling subunit, BAZ2A, and putative histone methyltransferase, CLLD8, represent two phylogenetically distinct groups within the MBD protein family
PLRDPLPPGWKRELVIRKSGSAGKGDVYYYSPCGKKLRSKPEVARYLEKTGPSSLDLENFSF
>gnl|CDD|238070 cd00123, DmpA_OAT, DmpA/OAT superfamily; composed of L-aminopeptidase D-amidase/D-esterase (DmpA), ornithine acetyltransferase (OAT) and similar proteins. DmpA is an aminopeptidase that releases N-terminal D and L amino acids from peptide substrates. This group represents one of the rare aminopeptidases that are not metalloenzymes. DmpA shows similarity in catalytic mechanism to N-terminal nucleophile (Ntn) hydrolases, which are enzymes that catalyze the cleavage of amide bonds through the nucleophilic attack of the side chain of an N-terminal serine, threonine, or cysteine. OAT catalyzes the first and fifth steps in arginine biosynthesis, coupling acetylation of glutamate with deacetylation of N-acetylornithine, which allows recycling of the acetyl group in the arginine biosynthetic pathway. The superfamily also contains an enzyme, endo-type 6-aminohexanoate-oligomer hydrolase, that have been shown to be involved in nylon degradation. Proteins in this superfamily undergo autocatalytic cleavage of an inactive precursor at the site immediately upstream to the catalytic nucleophile
PRGVVVGTAPVGEADDGRDGFTVIASTAPATVSVVFTRGRFAGPLCREAVAGGQFRHGVVVLARNEGEEN
AREVREAVARARGLPRTGFAEEGEXLIASTYDIGRQYTPXESIRAHLRTALWPAGEGGFDRGRASAGAAR
AIXTTDTGPGEARRSVGGATIVAIVKGNGXLEIVDRAGTVVRGQEAFAEQVPPVTPDXATLITFFATDAR
LDPAELDRLARVXDRTFNRVSIDTDTSTGDTAVAFATGLAGLPTTPGSSRGRLEVDAGEFEEAAHTAALA
AVKDAA
>gnl|CDD|276950 cd00124, MYSc, Myosin motor domain superfamily. Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSADLPPHVFAVADAAYRAMLR
DGQNQSILISGESGAGKTETTKLVLKYLAALSGSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDN
SSRFGKFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYY
YLNDYLNSSGCDRIDGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAE
VADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRIN
AALSPTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFID
FPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKLEFGIKHYAGDV
TYDADGFLEKNKDTLPPDLVDLLRSGSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQ
LRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKV
FLR
>gnl|CDD|153091 cd00125, PLA2c, PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers
NLLQFGKMIKCTTGRSALDYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGCSPYFTSYSYTCS
DGQITCSDANDKCARALCECDRAAALCFARAPYNPKYRNYDKKRC
>gnl|CDD|238072 cd00126, PAH, Pancreatic Hormone domain, a regulator of pancreatic and gastrointestinal functions; neuropeptide Y (NPY)b, peptide YY (PYY), and pancreatic polypetide (PP) are closely related; propeptide is enzymatically cleaved to yield the mature active peptide with amidated C-terminal ends; receptor binding and activation functions may reside in the N- and C-termini respectively; occurs in neurons, intestinal endocrine cells, and pancreas; exist as monomers and dimers
MPSKPENPGDDASPEELRQYLAALREYINLITRPRF
>gnl|CDD|350200 cd00128, PIN_FEN1_EXO1-like, FEN-like PIN domains of Flap endonuclease-1 (FEN1)-like and exonuclease-1 (EXO1)-like nucleases, structure-specific, divalent-metal-ion dependent, 5' nucleases. PIN (PilT N terminus) domain of Flap endonuclease-1 (FEN1) and exonuclease-1 (EXO1)-like nucleases: FEN1, EXO1, Mkt1, Gap endonuclease 1 (GEN1) and Xeroderma pigmentosum complementation group G (XPG) nuclease. These nucleases are members of the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LWQFIGEAKEPISIESLKGKTVAIDASIWVYQFLTAKREQGGDIGVTNSHLRGLFYRIIKLLSNGIKPIF
VFDGGPPPLKKETITKKMYQECKHLLSLFGIPYVVAPYEAEAQCAYLLKAGIVDAAITEDSDCLLFGAPR
VIRNMTFEGPHVEEFDASSILE
>gnl|CDD|238074 cd00129, PAN_APPLE, PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth factor proteins, plasma prekallikrein/coagulation factor XI and microneme antigen proteins, plant receptor-like protein kinases, and various nematode and leech anti-platelet proteins. Common structural features include two disulfide bonds that link the alpha-helix to the central region of the protein. PAN domains have significant functional versatility, fulfilling diverse biological functions by mediating protein-protein or protein-carbohydrate interactions
VDEFCKSAGTTLIKIALKIKTTKANTADECANRCEKNGLPFSCKAFVFAKARKQCLWFPFNSMSGVRKEF
SHGFDLYENK
>gnl|CDD|238075 cd00130, PAS, PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction
LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLR
RKDGSVIWVLVSLTPIRDEGGEVIGLLGVVRDI
>gnl|CDD|238076 cd00131, PAX, Paired Box domain
GQGGVNQLGGVFVNGRPLPDSIRQRIVELAQSGIRPCDISRQLRVSHGCVSKILNRYYETGSIRPGAIGG
SKPRVATPEVVKKIEIYKQENPGMFAWEIRDRLLQEGVCDKSNVPSVSSINRILRNKA
>gnl|CDD|238077 cd00132, CRIB, PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. CRIB-containing effector proteins are functionally diverse and include serine/threonine kinases, tyrosine kinases, actin-binding proteins, and adapter molecules
MEISTPTDFKHISHVGWDGVGFDGANLPPDLQSLFQTAGISA
>gnl|CDD|99904 cd00133, PTS_IIB, PTS_IIB: subunit IIB of enzyme II (EII) is the central energy-coupling domain of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). In the multienzyme PTS complex, EII is a carbohydrate-specific permease consisting of two cytoplasmic domains (IIA and IIB) and a transmembrane channel IIC domain. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include chitobiose/lichenan, ascorbate, lactose, galactitol, mannitol, fructose, and a sensory system with similarity to the bacterial bgl system. The PTS is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, polyols, amino sugars, and other sugar derivatives. The four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB), can phosphorylate or interact with numerous non-PTS proteins thereby regulating their activity
KILVVCGSGIGSSSMLAEKLEKAAKELGIEVKVEAQGLSEVIDLADADLIISTVPLAARFLGKPVIVVSP
LLNEKDGEKILEKL
>gnl|CDD|238079 cd00135, PDGF, Platelet-derived and vascular endothelial growth factors (PDGF, VEGF) family domain; PDGF is a potent activator for cells of mesenchymal origin; PDGF-A and PDGF-B form AA and BB homodimers and an AB heterodimer; VEGF is a potent mitogen in embryonic and somatic angiogenesis with a unique specificity for vascular endothelial cells; VEGF forms homodimers and exists in 4 different isoforms; overall, the VEGF monomer resembles that of PDGF, but its N-terminal segment is helical rather than extended; the cysteine knot motif is a common feature of this domain
SSCKPRETLVEISEELPDETNTIFKPPCVEVKRCGGCCNDESLECVPTETSNVTMQVLKISPKRKPRSKL
VEISFEEHTECECRPR
>gnl|CDD|467153 cd00136, PDZ_canonical, canonical PDZ domain. Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
TVTLEKDPGGGLGFSIRGGKDGGGGIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLK
SAGGEVTLTVR
>gnl|CDD|176497 cd00137, PI-PLCc, Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C. This subfamily corresponds to the catalytic domain present in prokaryotic and eukaryotic phosphoinositide-specific phospholipase C (PI-PLC), which is a ubiquitous enzyme catalyzing the cleavage of the sn3-phosphodiester bond in the membrane phosphoinositides (phosphatidylinositol, PI; Phosphatidylinositol-4-phosphate, PIP; phosphatidylinositol 4,5-bisphosphate, PIP2) to yield inositol phosphates (inositol monosphosphate, InsP; inositol diphosphate, InsP2; inositol trisphosphate, InsP3) and diacylglycerol (DAG). The higher eukaryotic PI-PLCs (EC 3.1.4.11) have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. They play a critical role in most signal transduction pathways, controlling numerous cellular events, such as cell growth, proliferation, excitation and secretion. These PI-PLCs strictly require Ca2+ for their catalytic activity. They display a clear preference towards the hydrolysis of the more highly phosphorylated PI-analogues, PIP2 and PIP, to generate two important second messengers, InsP3 and DAG. InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. In contrast, bacterial PI-PLCs contain a single catalytic domain. Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. They participate in Ca2+-independent PI metabolism. They are characterized as phosphatidylinositol-specific phospholipase C (EC 4.6.1.13) that selectively hydrolyze PI, not PIP or PIP2. The TIM-barrel type catalytic domain in bacterial PI-PLCs is very similar to the one in eukaryotic PI-PLCs, in which the catalytic domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. The catalytic mechanism of both prokaryotic and eukaryotic PI-PLCs is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes a distinctly different type of eukaryotic PLC, glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC), an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG), releasing dimyristyl glycerol (DMG), which may facilitate the evasion of the protozoan to the host#s immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs, but not mammalian PI-PLCs
HHPDTQPLAHYSIPGTHDTYLTAGQFTIKQVWGLTQTEMYRQQLLSGCRCVDIRCWDGKPEEPIIYHGPT
FLDIFLKEVIEAIAQFLKKNPPETIIMSLKNEVDSMDSFQAKMAEYCRTIFGDMLLTPPLKPTVPLPSLE
DLRGKILLLNKKNGFSGPTGSSNDTGFVSFEFSTQKNRSYNISSQDEYKAYDDEKVKLIKATVQFVDYNK
NQLSRNYPSGTSGGTAWYYYAMDSNNYMPQMFWNANPAGCGIVILDFQTMDLPMQQYMAVIEFN
>gnl|CDD|197200 cd00138, PLDc_SF, Catalytic domain of phospholipase D superfamily proteins. Catalytic domain of phospholipase D (PLD) superfamily proteins. The PLD superfamily is composed of a large and diverse group of proteins including plant, mammalian and bacterial PLDs, bacterial cardiolipin (CL) synthases, bacterial phosphatidylserine synthases (PSS), eukaryotic phosphatidylglycerophosphate (PGP) synthase, eukaryotic tyrosyl-DNA phosphodiesterase 1 (Tdp1), and some bacterial endonucleases (Nuc and BfiI), among others. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze the transphosphatidylation of phospholipids to acceptor alcohols. The majority of members in this superfamily contain a short conserved sequence motif (H-x-K-x(4)-D, where x represents any amino acid residue), called the HKD signature motif. There are varying expanded forms of this motif in different family members. Some members contain variant HKD motifs. Most PLD enzymes are monomeric proteins with two HKD motif-containing domains. Two HKD motifs from two domains form a single active site. Some PLD enzymes have only one copy of the HKD motif per subunit but form a functionally active dimer, which has a single active site at the dimer interface containing the two HKD motifs from both subunits. Different PLD enzymes may have evolved through domain fusion of a common catalytic core with separate substrate recognition domains. Despite their various catalytic functions and a very broad range of substrate specificities, the diverse group of PLD enzymes can bind to a phosphodiester moiety. Most of them are active as bi-lobed monomers or dimers, and may possess similar core structures for catalytic activity. They are generally thought to utilize a common two-step ping-pong catalytic mechanism, involving an enzyme-substrate intermediate, to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
EALLELLKNAKESIFIATPNFSFNSADRLLKALLAAAERGVDVRLIIDKPPNAAGSLSAALLEALLRAGV
NVRSYVTPPHFFERLHAKVVVIDGEVAYVGSANLSTASAAQNREAGVLV
>gnl|CDD|340436 cd00139, PIPKc, Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family. The Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family includes phosphatidylinositol 5-phosphate 4-kinases (PIP5Ks) and similar proteins. PIP5Ks catalyze the phosphorylation of phosphatidylinositol phosphate on the fourth or fifth hydroxyl of the inositol ring, to form phosphatidylinositol bisphosphate. The family includes type I and II PIP5Ks (-alpha, -beta, and -gamma) kinases. Signalling by phosphorylated species of phosphatidylinositol regulates secretion, vesicular trafficking, membrane translocation, cell adhesion, chemotaxis, DNA synthesis, and cell cycling
GKFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELKESEGKSGSFFFFTSDGKFIIKTITKSELK
FLLKILPDYYEHIKKNPNSLLTRFYGLYSIKLQKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSK
EKEKKKGLKVLKDLDFLEKGEKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRLVYYLGIIDI
LQEYNLRKKLERFLKSLLYGKDSGISCVPPDEYAERFLKFMES
>gnl|CDD|238082 cd00140, beta_clamp, Beta clamp domain. The beta subunit (processivity factor) of DNA polymerase III holoenzyme, refered to as the beta clamp, forms a ring shaped dimer that encircles dsDNA (sliding clamp) in bacteria. The beta-clamp is structurally similar to the trimeric ring formed by PCNA (found in eukaryotes and archaea) and the processivity factor (found in bacteriophages T4 and RB69). This structural correspondence further substantiates the mechanistic connection between eukaryotic and prokaryotic DNA replication that has been suggested on biochemical grounds
MKFTINREALLEALQKVSRAIESRNTIPILSNVLIEASDGGLTLTATDLEISIKTTIPAEEVEEEGSVTV
PAKKLLDIVRKLPDEEVTLETEENRLTIKSGKSRFSLNTLPAEEFPELPEIENGSSFTIPASELKELIKK
TAFAVSTDETRPILNGVLLEIEDNKLRAVATDGHRLALREIELESGAEEDFNVIVPRKTLNELLKLLEDD
DEEVEISISENQILFKLGNTTFTSRLIEGEFPDYERVIPKEFEKSLTVDREELLEALKRVSLLSNEKNRG
VKLEISEGQLKLSANNPEIGEAEEELEVEYEGEELEIGFNPKYLLDALKAIDSEEVRLSFTDSNSPVLIT
PEDDDNFLYLIMPVR
>gnl|CDD|143386 cd00141, NT_POLXc, Nucleotidyltransferase (NT) domain of family X DNA Polymerases. X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family
QEIADILEELADLLELLGGNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKL
RKLEELREDVPPGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGAKLEQNILIGLEYYEDFQQRIPR
EEALAIAEIIKEALREVDPVLQVEIAGSYRRGKETVGDIDILVTHPDATSRGLLEKVVDALVELGFVTEV
LSKGDTKASGILKLPGGWKGRRVDLRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLFDGV
DGERLPGETEEEIFEALGLPYIEPELR
>gnl|CDD|270621 cd00142, PI3Kc_like, Catalytic domain of Phosphoinositide 3-kinase and similar proteins. Members of the family include PI3K, phosphoinositide 4-kinase (PI4K), PI3K-related protein kinases (PIKKs), and TRansformation/tRanscription domain-Associated Protein (TRAPP). PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives, while PI4K catalyze the phosphorylation of the 4-hydroxyl of PtdIns. PIKKs are protein kinases that catalyze the phosphorylation of serine/threonine residues, especially those that are followed by a glutamine. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. PI4Ks produce PtdIns(4)P, the major precursor to important signaling phosphoinositides. PIKKs have diverse functions including cell-cycle checkpoints, genome surveillance, mRNA surveillance, and translation control. The PI3K-like catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
NALDVGILKVIHSKQRPKKITLIGADGKTYSFLLKRRDDLRKDERSFQFMRLIQSILEKESVNLVLPPYK
VIPLSENSGLIEIVKDAQTIEDLLKSLWRKSPSSQSWLNRRENFSCSLAGYSVLGYIFGIGDRHPSNIMI
EPSGNIFHIDFGFIFSGRKLAEGVETVPFRLTPMLENAMGTAGVNGPFQISMVKIMEILREHADLIVPIL
EHSLRD
>gnl|CDD|238083 cd00143, PP2Cc, Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity
FSAGVSDKGGDRKTNEDAVVIKPNLNNEDGGLFGVFDGHGGHAAGEFASKLLVEELLEELEETLTLSEED
IEEALRKAFLRADEEILEEAQDEPDDARSGTTAVVALIRGNKLYVANVGDSRAVLCRNGEAVQLTKDHKP
VNEEERERIEKAGGRVSNGRVPGVLAVTRALGDFDLKPGVSAEPDVTVVKLTEDDDFLILASDGLWDVLS
NQEAVDIVRSELAKEDLQEAAQELVDLALRRGSHDNITVVVVRL
>gnl|CDD|277316 cd00144, MPP_PPP_family, phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain. The PPP (phosphoprotein phosphatase) family is one of two known protein phosphatase families specific for serine and threonine. This family includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFML
LNFLYGFYDERTLRCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNIRPIENP
DDQLVEDLLWSDPDESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITI
FSAPNYCGKGGNKLAALVV
>gnl|CDD|99912 cd00145, POLBc, DNA polymerase type-B family catalytic domain. DNA-directed DNA polymerases elongate DNA by adding nucleotide triphosphate (dNTP) residues to the 5'-end of the growing chain of DNA. DNA-directed DNA polymerases are multifunctional with both synthetic (polymerase) and degradative modes (exonucleases) and play roles in the processes of DNA replication, repair, and recombination. DNA-dependent DNA polymerases can be classified in six main groups based upon their phylogenetic relationships with E. coli polymerase I (class A), E. coli polymerase II (class B), E. coli polymerase III (class C), euryarchaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB, and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family B DNA polymerases include E. coli DNA polymerase II, some eubacterial phage DNA polymerases, nuclear replicative DNA polymerases (alpha, delta, epsilon, and zeta), and eukaryotic viral and plasmid-borne enzymes. DNA polymerase is made up of distinct domains and sub-domains. The polymerase domain of DNA polymerase type B (Pol domain) is responsible for the template-directed polymerization of dNTPs onto the growing primer strand of duplex DNA that is usually magnesium dependent. In general, the architecture of the Pol domain has been likened to a right hand with fingers, thumb, and palm sub-domains with a deep groove to accommodate the nucleic acid substrate. There are a few conserved motifs in the Pol domain of family B DNA polymerases. The conserved aspartic acid residues in the DTDS motifs of the palm sub-domain is crucial for binding to divalent metal ion and is suggested to be important for polymerase catalysis
EPYEGGYVFDPIPGLYENVIVLDFKSLYPSIIITYNLSPTTLVGNGEIAAPEDYIGVGFRSPKDRKGLLP
RILEELLNFRDEAKKRMKAAKLAPEERVLYDNRQQALKVLANSFYGYLGAKFFRFYDPEVAASITSFGRE
IIQDTIALVEEHGARVIYGDTDSIFVSLPKMGTKEDAIKEGREILQELADEHLLELEFEKVYLPFFLGKK
KRYAGLDIWKGQDEGKIDIKGLETRRRDSPPLVKKFQKEVLELILEEERKVEAVKEYIDELDKVKYVVTR
GGKGVPDYERADPPLEDLDKRHRIDYEYYLERLLQPPLERIFE
>gnl|CDD|238084 cd00146, PKD, polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases
PTASVSAPPVAELGASVTFSASDSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVG
SSSTKTTTVVV
>gnl|CDD|132835 cd00147, cPLA2_like, Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids. Catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. Group IV cPLA2 includes six intercellular enzymes: cPLA2alpha, cPLA2beta, cPLA2gamma, cPLA2delta, cPLA2epsilon, and cPLA2zeta
VRLASDLCDEEKEFLEKRRKVVAKALKKFLGLENDLNPDEVPVIAILGSGGGYRAMTGGAGALKALDEGG
LLDCVTYLSGLSGSTWLMASLYSNPDWSQKDLDEAIEWLKRHVIKSPLLLFSPERLKYYAKELEEKKKAG
FNVSLTDFWGLLLGYTLLKELTDSSLSDQREFVQNGQNPLPIYTALNVKPGETSINDFATWFEFTPYEVG
FPKYGAFIPTEYFGSKFFMGRLVKKIPEDRLGFLMGTWGSAFSIILLDAGKYPNFFYGLNLHKSYLRSPN
PLITSSDTLHLVDAGLDINNIPLPPLLRPERDVDVILSFDFSADDPDWPNGLKLVATYERQASSNGIPFP
KIPDSVTFDNLGLKECYVFFGCDDPDAPLVVYFPLVNDTFRKYDFDDPNSPYSTFNLSYTDEEFDRLLEL
AFYNVTNNKDTILQALRA
>gnl|CDD|238085 cd00148, PROF, Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and poly-L-proline. Profilin can inhibit actin polymerization into F-actin by binding to monomeric actin (G-actin) and terminal F-actin subunits, but - as a regulator of the cytoskeleton - it may also promote actin polymerization. It plays a role in the assembly of branched actin filament networks, by activating WASP via binding to WASP's proline rich domain. Profilin may link the cytoskeleton with major signalling pathways by interacting with components of the phosphatidylinositol cycle and Ras pathway
SWQAYVDDNLLGTGKVDSAAIVGHDDGSVWAASAGGFNLTPEEVGTLVAGFKDPDGVFSTGLTLGGQKYM
VIRADDRSIYGKKGAGGVVIVKTKQALVIGMYEEGVQPGQANKVVEKLADYLRSQGY
>gnl|CDD|119410 cd00150, PlantTI, Plant trypsin inhibitors such as squash trypsin inhibitor. Plant proteinase inhibitors play important roles in natural plant defense. Proteinase inhibitors from squash seeds form an uniform family of small proteins cross-linked with three disulfide bridges
CPRILMECKRDSDCLAECICLENGYCG
>gnl|CDD|238086 cd00152, PTX, Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their Ca2+ dependent ligand binding, such as Serum amyloid P component (SAP) and C-reactive Protein (CRP), which are cytokine-inducible acute-phase proteins implicated in innate immunity. CRP binds to ligands containing phosphocholine, SAP binds to amyloid fibrils, DNA, chromatin, fibronectin, C4-binding proteins and glycosaminoglycans. "Long" pentraxins have N-terminal extensions to the common pentraxin domain; one group, the neuronal pentraxins, may be involved in synapse formation and remodeling, and they may also be able to form heteromultimers
QTDLSGKVFVFPKESDTSYVKLKPELPKPLQAFTLCLWVYTDLSTREYSLFSYATKGQDNELLLYKEKDG
GYSLYIGGKEVTFKVPESDGAWHHICVTWESTSGIAELWVNGKLSVRKSLKKGYTVGPGGSIILGQEQDS
YGGGFDATQSFVGEISDVNMWDSVLSPEEIKNVYSEGGTLSGNILNWRALNYEINGGVVIK
>gnl|CDD|340449 cd00153, RA_RalGDS_like, Ras-associating (RA) domain of RalGDS family. The RalGDS family RA domains can interact with activated Ras and may function as effectors for other Ras family. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes and is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. The RalGDS family includes RalGDS, RGL, RGL2/Rlf and RGL3. All family members have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal RA domain. The RA domain mediates the GTP-dependent interaction with Ras and Ras-related proteins
DSRIIRVSLEDGSEDGNLYKSILLTNQDRTPSVIRRALEKHNLEDEDPDDFSLVQILPDDKELVIPDNAN
VFYAMNSSANLNFILRKK
>gnl|CDD|206640 cd00154, Rab, Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases). Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible
FKIVLIGDSGVGKTSLLLRFVDNKFSENYKSTIGVDFKSKTIEVDGKKVKLQIWDTAGQERFRSITSSYY
RGAHGAILVYDVTNRESFENLDKWLNELKEYAPPNIPIILVGNKSDLEDERQVSTEEAQQFAKENGLLFF
ETSAKTGENVDEAFESLAR
>gnl|CDD|238087 cd00155, RasGEF, Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of the Ras superfamily function as molecular switches in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. Guanine-nucleotide-exchange factors (GEFs) positively regulate these GTP-binding proteins in response to a variety of signals. GEFs catalyze the dissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors
FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIHLSPNLERFIERFNNLSNWVASEILLCTN
PKKRARLLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNF
KNYRKLLKSVGPNPPCVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQSNSYELNR
DEDILAFLWKLLELILNEDELYELSLE
>gnl|CDD|381085 cd00156, REC, phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs). Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays
LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDI
PVIVLTAKADEEDAVRALELGADDYLVKP
>gnl|CDD|206641 cd00157, Rho, Ras homology family (Rho) of small guanosine triphosphatases (GTPases). Members of the Rho (Ras homology) family include RhoA, Cdc42, Rac, Rnd, Wrch1, RhoBTB, and Rop. There are 22 human Rho family members identified currently. These proteins are all involved in the reorganization of the actin cytoskeleton in response to external stimuli. They also have roles in cell transformation by Ras in cytokinesis, in focal adhesion formation and in the stimulation of stress-activated kinase. These various functions are controlled through distinct effector proteins and mediated through a GTP-binding/GTPase cycle involving three classes of regulating proteins: GAPs (GTPase-activating proteins), GEFs (guanine nucleotide exchange factors), and GDIs (guanine nucleotide dissociation inhibitors). Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Since crystal structures often lack C-terminal residues, this feature is not available for annotation in many of the CDs in the hierarchy
IKIVVVGDGAVGKTCLLISYTTNKFPTEYVPTVFDNYSANVTVDGKQVNLGLWDTAGQEEYDRLRPLSYP
QTDVFLLCFSVDSPSSFENVKTKWYPEIKHYCPNVPIILVGTKIDLRDDGNTLKKLEKKQKPITPEEGEK
LAKEIGAVKYMECSALTQEGLKEVFDEAIRA
>gnl|CDD|238089 cd00158, RHOD, Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins
ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLL
RKAGGTNVYNLEGGMLAWK
>gnl|CDD|238090 cd00159, RhoGAP, RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins
PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPL
IPFELYDEFIELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAP
TLLRPPDSDDELLEDIKKLNEIVEFLIEN
>gnl|CDD|238091 cd00160, RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains
RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEW
DKSGPRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESECGRLKLESLLLKPVQ
RLTKYPLLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN
>gnl|CDD|467293 cd00161, beta-trefoil_Ricin-like, ricin B-type lectin domain, beta-trefoil fold. The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats
GTYRIVNAASGKCLDVAGGSTANGAPVQQWTCNGGANQQWTLTPVGDGYYTIRNVASGKCLDVAGGSTAN
GANVQQWTCNGGDNQQWRLEPVGDGYYRIVNKHSGKCLDVSGGSTANGANVQQWTCNGGANQQW
>gnl|CDD|438111 cd00162, RING_Ubox, RING finger (Really Interesting New Gene) domain and U-box domain superfamily. The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates
CPICREEMNDRRPVVLLSCGHTFSRSAIARWLEGSKQKCPFC
>gnl|CDD|119386 cd00163, RNase_A, RNase A family, or Pancreatic RNases family; includes vertebrate RNase homologs to the bovine pancreatic ribonuclease A (RNase A). Many of these enzymes have special biological activities; for example, some stimulate the development of vascular endothelial cells, dendritic cells, and neurons, are cytotoxic/anti-tumoral and/or anti-pathogenic. RNase A is involved in endonucleolytic cleavage of 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates. The catalytic mechanism is a transphosphorylation of P-O 5' bonds on the 3' side of pyrimidines and subsequent hydrolysis to generate 3' phosphate groups. The RNase A family proteins have a conserved catalytic triad (two histidines and one lysine); recently some family members lacking the catalytic residues have been identified. They also share three or four disulfide bonds. The most conserved disulfide bonds are close to the N and C termini and contribute most significantly to the conformational stability. 8 RNase A homologs had initially been identified in the human genome, pancreatic RNase (RNase 1), Eosinophil Derived Neurotoxin (EDN/RNASE 2), Eosinophil Cationic Protein (ECP/RNase 3), RNase 4, Angiogenin (RNase 5), RNase 6 or k6, the skin derived RNase (RNase 7) and RNase 8. These eight human genes are all located in a cluster on chromosome 14. Recent genomic analysis has extended the family to 13 sequences. However only the first eight identified human RNases, which are refered to as "canonical" RNases, contain the catalytic residues required for RNase A activity. The new genes corresponding to RNases 9-13 are also located in the same chromosome cluster and seem to be related to male-reproductive functions. RNases 9-13 have the characteristic disulfide bridge pattern but are unlikely to share RNase activity. The RNase A family most likely started off in vertebrates as a host-defense protein, and comparative analysis in mammals and birds indicates that the family may have originated from a RNase 5-like gene. This hypothesis is supported by the fact that only RNase 5-like RNases have been reported outside the mammalian class. The RNase 5 group would therefore be the most ancient form of this family, and all other members would have arisen during mammalian evolution
SKARTFRRQHIDYPKSNGDPRYCNSMMRRKKVTENGSCKKQHTFIHESLEEVQAVCNNPSVFCKNGGENC
HRSKRPLDLTVCKLTGGSRIPNCRYNTTYTEKFILVTCDDKPIVPVHLD
>gnl|CDD|238094 cd00164, S1_like, S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of RNA-associated proteins. Originally identified in S1 ribosomal protein. This superfamily also contains the Cold Shock Domain (CSD), which is a homolog of the S1 domain. Both domains are members of the Oligonucleotide/oligosaccharide Binding (OB) fold
VTGKVVSITKFGVFVELEDGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS
>gnl|CDD|238095 cd00165, S4, S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, charged residues that define a likely RNA-binding site; Found in stress proteins, ribosomal proteins and tRNA synthetases; This may imply a hitherto unrecognized functional similarity between these three protein classes
MRLDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKPGDVIEVDGKSIEEDIVYEDKKLLVVN
>gnl|CDD|238096 cd00167, SANT, 'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA
PWTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRERWRNLL
>gnl|CDD|349397 cd00168, CAP, CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family. The CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain, also called SCP (sperm-coating glycoprotein), is found in eukaryotes and prokaryotes. This family includes plant pathogenesis-related protein 1 (PR-1), which accumulates after infections with pathogens, and may act as an anti-fungal agent or be involved in cell wall loosening. This family also includes CRISPs (cysteine-rich secretory proteins), which combine the CAP/SCP domain with a C-terminal cysteine rich domain, and allergen 5 from vespid venom. Roles for CRISP, in response to pathogens, fertilization, and sperm maturation have been proposed. One member, Tex31 from the venom duct of Conus textile, has been shown to possess proteolytic activity sensitive to serine protease inhibitors. The human GAPR-1 protein has been reported to dimerize, and such a dimer may form an active site containing a catalytic triad. CAP/SCP has also been proposed to be a Ca++ chelating serine protease. The Ca++-chelating function would fit with various signaling processes that members of this family, such as the CRISPs, are involved in, and is supported by sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how helothermine, a toxic peptide secreted by the beaded lizard, blocks Ca++ transporting ryanodine receptors. Little is known about the biological roles of the bacterial and archaeal CAP/SCP domains
XQEILDLHNSYRSSVSPPASNMPLMAWDQELADVAIGYAKDCIFSHSSPTSRQLAGENIAASSYDMDGVA
ALQAWHNEIKNYNFGTAQPGFNSGTGHYTQMVWEKTTKLGCGVADCSDNSKFVVCNYI
>gnl|CDD|238098 cd00169, Chemokine, Chemokine: small cytokines, including a number of secreted growth factors and interferons involved in mitogenic, chemotactic, and inflammatory activity; distinguished from other cytokines by their receptors, which are G-protein coupled receptors; divided into 4 subfamilies based on the arrangement of the two N-terminal cysteines; some members can bind multiple receptors and many chemokine receptors can bind more than one chemokine; this redundancy allows precise control in stimulating the immune system and in contributing to the homeostasis of a cell; when expressed inappropriately, chemokines play a role in autoimmune diseases, vascular irregularities, graft rejection, neoplasia, and allergies; exist as monomers, dimers and multimers, but are believed to function as monomers; found only in vertebrates and a few viruses. See CDs: Chemokine_CXC (cd00273), Chemokine_CC (cd00272), Chemokine_C (cd00271), and Chemokine_CX3C (cd00274) for chemokine subgroups
CCLKYTSKPIPPKNIKSYRVQEAGGHCSIPAVIFTTKKGRKVCADPKEPWVKDLIQKLD
>gnl|CDD|469559 cd00170, SEC14, Sec14p-like lipid-binding domain. Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits
LEELLELLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDL
KGFSLSNLSDLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSDLEEL
LEYIDPDQLPKELGGT
>gnl|CDD|238100 cd00171, Sec7, Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the central domain of the guanine-nucleotide-exchange factors (GEFs) of the ADP-ribosylation factor family of small GTPases (ARFs) . It carries the exchange factor activity
RKTLLSEGRQLFNRKPKKGISFLIEKGFLEDDSPKEIAKFLYETEGLNKKAIGEYLGENNEFNSLVLHEF
VDLFDFSGLRLDEALRKFLQSFRLPGEAQKIDRLLEKFSERYCECNPGIFSSSADAAYTLAYSIIMLNTD
LHNPNVKKKMTLEDFIKNLRGINDGEDFPREFLKELYDSIKNNEI
>gnl|CDD|381000 cd00172, serpin, SERine Proteinase INhibitors (serpin) family. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
ANNDFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLDEEDLHSAFKELL
SSLKSSNENYTLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNPEEARKEINKWVEEKTNGKIK
DLLPPGSIDPDTRLVLVNAIYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQ
VLELPYKGDRLSMVIILPKEGDGLAELEKSLTPELLSKLLSSLKPTEVELTLPKFKLESSYDLKEVLKKL
GITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEVDEEGTEAAAATAVVIVLRSAPPPPIEFIADRPFLF
LIRDKKTGTILFMGR
>gnl|CDD|198173 cd00173, SH2, Src homology 2 (SH2) domain. In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others
PWFHGSISREEAERLLRGKPDGTFLVRESSSEPGDYVLSVRSGDGKVKHYLIERNEGGYYLLGGSGRTFP
SLPELVEHY
>gnl|CDD|212690 cd00174, SH3, Src Homology 3 domain superfamily. Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction
YARALYDYEAQDDDELSFKKGDIITVLEKDDDGWWEGELNGGREGLFPANY
>gnl|CDD|238102 cd00175, SNc, Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds
RVIDGDTIRVRLPPGPLITVRLSGIDAPETARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDR
YGRTLGTVYLNGGENIAEELVKEGLARVYRYYPDDSEYYDELLEAEEAAKKARKGLWSD
>gnl|CDD|238103 cd00176, SPEC, Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG
HPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLES
VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE
EAL
>gnl|CDD|176851 cd00177, START, Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins. This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells
EEAIEELLELLEEPEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKN
FEEFEVIEEIDEHTDIIYYKTKPPWPVSPRDFVYLRRRRKLDDGTYVIVSKSVDHDSHPKEKGYVRAEIK
LSGWIIEPLDPGKTKVTYVLQVDPKGSIPKSLVNSAAKKQLASFLKDLRKAKK
>gnl|CDD|467384 cd00178, beta-trefoil_STI, soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold. The STI-like domain is found in the soybean trypsin inhibitor (Kunitz) family of protease inhibitors. They inhibit proteases by binding with high affinity to their active sites. Plant Kunitz-type inhibitors are thought to be important in defense, especially against insect pests. The STI-like domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry
GVPYYILPAIWGGGGGLTLAKTGNETCPLDVVQSPSDTDNGLPVTFSPANPKDGVIRESTDLNIKFSADT
TCCAESTVWKVVGDDSTGGRFVTTGGVKGNETLNSWFKIEKAGNGNGYKLVFCPSVCGCKVVCGDVGIVV
DNGNRRLALTEGEPLEVVFKK
>gnl|CDD|238105 cd00179, SynN, Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane; they are a family of receptors for intracellular transport vesicles; each target membrane may be identified by a specific member of the syntaxin family; syntaxins contain a moderately well conserved amino-terminal domain, called Habc, whose structure is an antiparallel three-helix bundle; a linker of about 30 amino acids connects this to the carboxy-terminal region, designated H3 (t_SNARE), of the syntaxin cytoplasmic domain; the highly conserved H3 region forms a single, long alpha-helix when it is part of the core SNARE complex and anchors the protein on the cytoplasmic surface of cellular membranes; H3 is not included in defining this domain
LEEFFEEVEEIRGNIDKISEDVEELQKLHSQLLTAPDADPELKQELESLVQEIKKLAKEIKGKLKELEES
NEQNEALNGSSVDRIRKTQHSGLSKKFVEVMTEFNKAQRKYRERYKERIQRQLEITGGEATDEELEDMLE
SGNSEIFTSQI
>gnl|CDD|270622 cd00180, PKc, Catalytic domain of Protein Kinases. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase
LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVM
EYCEGGSLKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAK
DLDSDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYELEELKDLIRRMLQYDPKKRPSAKE
LLEHL
>gnl|CDD|438624 cd00181, chemoreceptor_sensor, 4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr. The ligand binding sensor domain of chemoreceptors and related sensor histidine kinases forms homodimers and binds to ligands via the dimerization interface, a feature that appears to be conserved in this domain superfamily. This family includes ligand binding sensor domain of several chemoreceptors, such as Escherichia coli Tar, Tsr, NarQ, NarX, Pseudomonas aeruginosa KinB, Rhodopseudomonas palustris histidine kinase HK9 chemoreceptors, Comamonas testosteroni CNB-2 MCP2201 and Anaeromyxobacter dehalogenans histidine kinase Adeh_2942, among others
QEIRQQASAISSLESLVLQARVTLRAEALTGVEELGDALIRALKQTAAVLAQFRALTRDPPEAEAEILDK
VQDYQKALAALIPALLERGAESALFDQSEAQGGLELLLSLLQQLTAAGI
>gnl|CDD|410312 cd00182, T-box, DNA-binding domain of the T-box transcription factor family. The T-box family is an ancient family of transcription factors which plays a multitude of diverse functions throughout development. The founding member of the family is Brachyury (also known as TBXT, or T). Members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns. The T-box factors in Caenorhabditis elegans have evolved very differently than those in other organisms; its genome contains 22 T-box genes which encode factors which are diverse in DNA-binding specificity, function and sequence, and only 3 of these factors fall into the conserved T-box subfamilies
ITVSLRNEELWKKFHELGTEMIVTKSGRRMFPTLEYSVSGLDPNKLYSVSLHFERVDNKRYKFNNGKWVP
SGKAEPPPEPSRIYVHPDGPQTGSFWMKKGVSFDKVKITNNKEDKKEGHILLHSMHKYIPVLTIYEVDDN
GLLSKLVKEFRFPETEFIAVTAYQNDEITQLKIDNN
>gnl|CDD|238107 cd00183, TFIIS_I, N-terminal domain (domain I) of transcription elongation factor S-II (TFIIS); similar to a domain found in elongin A and CRSP70; likely to be involved in transcription; domain I from TFIIS interacts with RNA polymerase II holoenzyme
SEEVLRAKKKLEKKDSNEEVSRLLDLLRLLKKLPLTVEILKETRIGKKVNSLRKHSNEKIRKLAKALIKS
WKKLVD
>gnl|CDD|238108 cd00184, TNF, Tumor Necrosis Factor; TNF superfamily members include the cytokines: TNF (TNF-alpha), LT (lymphotoxin-alpha, TNF-beta), CD40 ligand, Apo2L (TRAIL), Fas ligand, and osteoprotegerin (OPG) ligand. These proteins generally have an intracellular N-terminal domain, a short transmembrane segment, an extracellular stalk, and a globular TNF-like extracellular domain of about 150 residues. They initiate apoptosis by binding to related receptors, some of which have intracellular death domains. They generally form homo- or hetero- trimeric complexes.TNF cytokines bind one elongated receptor molecule along each of three clefts formed by neighboring monomers of the trimer with ligand trimerization a requiste for receptor binding
PAAHLIGTNSSSGGTGLSWESDDGRAFLSGGLELQNGELVVPQDGLYYIYSQVYFRGQCCSTLSVSHVLQ
LRTDSYPEPILLLKGIRSVCSSVSEGWYNSVYLGGLFQLRAGDRLSVNVSAPALLDLSQGTTFFGAF
>gnl|CDD|276900 cd00185, TNFRSF, Tumor necrosis factor receptor superfamily (TNFRSF). Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens
CCQRCPPGEYLSSDCTATTDTVCSPCPPGTYSESWNSLSKCLPCTTCGGGNQVEKTPCTATDNRCCTCKP
GFYCDEGTNVEECKPCT
>gnl|CDD|238110 cd00186, TOP1Ac, DNA Topoisomerase, subtype IA; DNA-binding, ATP-binding and catalytic domain of bacterial DNA topoisomerases I and III, and eukaryotic DNA topoisomerase III and eubacterial and archael reverse gyrases. Topoisomerases clevage single or double stranded DNA and then rejoin the broken phosphodiester backbone. Proposed catalytic mechanism of single stranded DNA cleavage is by phosphoryl transfer through a tyrosine nucleophile using acid/base catalysis. Tyr is activated by a nearby group (not yet identified) acting as a general base for nucleophilic attack on the 5' phosphate of the scissile bond. Arg and Lys stabilize the pentavalent transition state. Glu then acts as a proton donor for the leaving 3'-oxygen, upon cleavage of the scissile strand
ENLVNAQLARRILDRLVGFNLSRLLTKKLRRKGVLSAGRVQSPTLGLIVEREREIKAFVPEDYWEIKEAV
VVSVEKKEKKKNPPPPFTTSTLQQEASSKLGFSAKKTMQIAQKLYEAGLITYPRTDSTRLSEEAILEARE
YIQAIYGKEYLYPAPLLGRRNPKRGKKEQGAHEAIRPTKVAPTPELEANLSEDEFKLYELIWRRFLASQM
ADAKYEETTVTLEIGGEKFKASGKVLLEDGWLEVYPEEKDDEEEEPPPLKEGDELKLEEVELEEKETQPP
PRYTEASLIKLMEKRGIGRPSTYASIIETLLDRGYVEKEKKKLIPTELGFAVIELLEKHFPELVDPEFTA
KLEEKLDEIAEGKKDYQEVLEEFYEEFKKIV
>gnl|CDD|238111 cd00187, TOP4c, DNA Topoisomerase, subtype IIA; domain A'; bacterial DNA topoisomerase IV (C subunit, ParC), bacterial DNA gyrases (A subunit, GyrA),mammalian DNA toposiomerases II. DNA topoisomerases are essential enzymes that regulate the conformational changes in DNA topology by catalysing the concerted breakage and rejoining of DNA strands during normal cellular growth
NGRALPDVRDGLKPVQRRILYAMFKRGLTPDKPEKKVARLVGDVAGKYHPHGDSSLYDTIVRMAQDFSNN
IPLLDPQGNFGSRDGDDAAAMRYTETRLSPIARLLLPDIDDPTVDFVPNYDGQEVEPEVLPPIFPNLLVN
GSSGIAVGMATNIPPHNLREVIDALRALIDNPEASIDELMEIIKGPDFPTGGIIEGRAGIREAYETGRGR
YIIRGKYEIEDDEGRNTIEITELPYQVNKAKLKEKIAELVKDKKIEGISDVRDESDREGIRFVIELKRGA
MAEVVLNGLYKVTKLQTTFGINMVAFDPNGRPKKLNLKEILQEFLDHRLEVYTRRKEYELGKAEARLHIL
EGLLKAILNIDEVINLIRSSDEAKKALIEELEKLGFSEIQADAILDMRLRRLTKLEREKLLKELKELEAE
IEDLEKILASEERPKDLWKEELDEF
>gnl|CDD|173773 cd00188, TOPRIM, Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type IA, type IIA and type IIB topoisomerases, bacterial DnaG-type primases, small primase-like proteins from bacteria and archaea, OLD family nucleases from bacterial and archaea, and bacterial DNA repair proteins of the RecR/M family. This domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases and in strand joining in topoisomerases and, as a general acid in strand cleavage by topisomerases and nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function
KKLIIVEGPSDALALAQAGGYGGAVVALGGHALNKTRELLKRLLGEAKEVIIATDADREGEAIALRLLEL
LKSLGKKVRRLLL
>gnl|CDD|238113 cd00190, Tryp_SPc, Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues
IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQV
IKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD
VLQEVNVPIVSNAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGC
ARPNYPGVYTRVSSYLDWIQKT
>gnl|CDD|238114 cd00191, TY, Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases
PCERERASALESLAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC
>gnl|CDD|270623 cd00192, PTKc, Catalytic domain of Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KKLGEGAFGEVYKGKLKGGDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEP
LYLVMEYMEGGDLLDFLRKSRPVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGE
DLVVKISDFGLSRDIYDDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPG
LSNEEVLEYLRKGYRLPKPENCPDELYELMLSCWQLDPEDRPTFSELVERLE
>gnl|CDD|277192 cd00193, SNARE, SNARE motif. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, Qb- and Qc-SNAREs are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
ESLEQLEASIGELKDIGRDMAMELEEQGEQLDRIEERAESTQARVSRAEKSLAK
>gnl|CDD|270455 cd00194, UBA_like_SF, UBA domain-like superfamily. The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. UBA domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only bind the UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains
LVDITGASQEEAQQALEACGGNLNIAAN
>gnl|CDD|467407 cd00195, UBCc_UEV, Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain. The family includes ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain and ubiquitin (Ub) E2 variant (UEV) domain. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. E2 is part of the ubiquitin-mediated protein degradation pathway in which a thioester linkage forms between a conserved cysteine and the C-terminus of ubiquitin, and complexes with ubiquitin protein ligase enzymes, E3. This pathway regulates many fundamental cellular processes. There are also other E2s which form thioester linkages without the use of E3s. Several UBC homologs (TSG101, Mms2, Croc-1 and similar proteins) contains the UEV domain, which lacks the active site cysteine essential for ubiquitination and appear to function in DNA repair pathways
KRLQKELKELQKNPPPGISVEPVDDDLFHWKATIKGPEGTPYEGGVFKLDIEFPDDYPFKPPKVRFLTPI
YHPNVDPDGEICLDILKSEGWSPALTLRSVLLSIQSLLSDPN
>gnl|CDD|340450 cd00196, Ubiquitin_like_fold, Beta-grasp ubiquitin-like fold. Ubiquitin is a protein modifier that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a ubiquitin-like manner but with biochemically distinct roles. Ubiquitin and ubiquitin-like proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some other ubiquitin-like domains have adaptor roles in ubiquitin-signaling by mediating protein-protein interaction. In addition to Ubiquitin-like (Ubl) domain, Ras-associating (RA) domain, F0/F1 sub-domain of FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, TGS (ThrRS, GTPase and SpoT) domain, Ras-binding domain (RBD), Ubiquitin regulatory domain X (UBX), Dublecortin-like domain, and RING finger- and WD40-associated ubiquitin-like (RAWUL) domain have beta-grasp ubiquitin-like folds, and are included in this superfamily
VKVETPSLKKIVVAVPPSTTLRQVLEKVAKRIGLPPDVIRLLFNGQVLDDLMTAKQVGLEPGEELHFV
>gnl|CDD|340764 cd00197, VHS_ENTH_ANTH, VHS, ENTH and ANTH domain superfamily. This superfamily is composed of proteins containing a VHS, CID, ENTH, or ANTH domain. The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It is located at the N-termini of proteins involved in intracellular membrane trafficking. The CTD-Interacting Domain (CID) is present in several RNA-processing factors and binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase II (RNAP II or Pol II). The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. A set of proteins previously designated as harboring an ENTH domain in fact contains a highly similar, yet unique module referred to as an AP180 N-Terminal Homology (ANTH) domain. VHS, ENTH, and ANTH domains are structurally similar and are composed of a superhelix of eight alpha helices. ENTH and ANTH (E/ANTH) domains bind both inositol phospholipids and proteins and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. E/ANTH domain-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding
FEKTVEKATSNENMGPDWPLIMEICDLINETNVGPKEAVDAIKKRINNKNPHVVLKALTLLEYCVKNCGE
RFHQEVASNDFAVELLKFDKSGLLGDDVSTNVREKAIELVQLWAS
>gnl|CDD|238119 cd00198, vWFA, Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains
ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAID
ALKKGLGGGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIG
DDANEDELKEIADKTTGGAVF
>gnl|CDD|238120 cd00199, WAP, whey acidic protein-type four-disulfide core domains. Members of the family include whey acidic protein, elafin (elastase-specific inhibitor), caltrin-like protein (a calcium transport inhibitor) and other extracellular proteinase inhibitors. A group of proteins containing 8 characteristically-spaced cysteine residuesforming disulphide bonds, have been termed '4-disulphide core' proteins. Protease inhibition occurs by insertion of the inhibitory loop into the active site pocket and interference with the catalytic residues of the protease
GNNMTKPGSCPRPVEKPGRCPMVNPPSLGIPPNRCSSDSDCPGDKKCCENGCGKSCLTPV
>gnl|CDD|238121 cd00200, WD40, WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment
LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGS
SDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS
VAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK
CLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGS
ADGTIRIWD
>gnl|CDD|238122 cd00201, WW, Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs
PPGWEERWDPDGRVYYYNHNTKETQWEDPRE
>gnl|CDD|238123 cd00202, ZnF_GATA, Zinc finger DNA binding domain; binds specifically to DNA consensus sequence [AT]GATA[AG] promoter elements; a subset of family members may also bind protein; zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C
ACSNCGTTTTPLWRRGPSGGSTLCNACGLYWKKHGVMRPLSKRKKDQIKRRNRK
>gnl|CDD|238124 cd00203, ZnMc, Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease
KVIPYVVVADDRDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDKADIAILVTRQDFDGGTGGW
AYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTIDDTLNAEDDDYYSVM
SYTKGSFSDGQRKDFSQCDIDQINKLY
>gnl|CDD|119412 cd00205, rhv_like, Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids composed of 60 copies each of 4 virus encoded proteins; alignment includes picornaviridae, like poliovirus, hepatitis A virus, rhinovirus, foot-and-mouth disease virus and encephalomyocarditis virus; common structure is an 8-stranded beta sandwich
VESFADRPTTVGTNNWNSSASGTQLFQWKLSPALGFLLLQNTPLGALLSYFTYWRGDLEVTVQFNGSKFH
TGRLLVAYVPPGAPAPTTGDTRWQATLNPHVIWDLGTNSSVTFVVPYVSPTPYRSTRYDGYGPLNSFGTL
VVRVLTPLTVPSGAPTTVDITVYVRAGDFELYGPRPPR
>gnl|CDD|467061 cd00206, TFP_snake_toxin, Snake toxin domain. The snake toxin domain is present in short and long neurotoxins, cytotoxins and short toxins, and in other miscellaneous venom peptides. The toxin acts by binding to the nicotinic acetylcholine receptors in the postsynaptic membrane of skeletal muscles and preventing the binding of acetylcholine, thereby blocking the excitation of muscles. This domain contains 60-75 amino acids that are fixed by 4-5 disulfide bridges and is nearly all beta sheets; it exists as either a monomer or a dimer. The snake toxin domain exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold), which also includes extracellular domain (ECD) found in Ly-6 antigen/uPA receptor-like (LU) superfamily
LICYNCPSSTCPTTKTCPPGENLCYKKWWRDGPRGKRIERGCAATCPKPKPGEKVKCCSTDKCN
>gnl|CDD|238126 cd00207, fer2, 2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin
VTINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYV
LACQTRVTDGLVIE
>gnl|CDD|100038 cd00208, LbetaH, Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms
VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAV
IGAGAVVT
>gnl|CDD|238127 cd00209, DHFR, Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis
ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPRRPLPGRTNIVLSRQLDYQD
AEGVEVVHSLEEALELAENTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPEIDESEWELVS
EEEVFEEDGYSYTFETYE
>gnl|CDD|238128 cd00210, PTS_IIA_glc, PTS_IIA, PTS system, glucose/sucrose specific IIA subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIA PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation
LASPITGEIVPLDQVPDEVFASKMMGDGFAIKPSDGKVVAPVDGTIVQIFPTKHAIGIESDSGVEILIHI
GIDTVKLNGEGFTSHVEEGQRVKQGDKLLEFDLPAIKAAGLDDTTPVIVTNSDE
>gnl|CDD|238129 cd00211, PTS_IIA_fru, PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIA PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation
LTKENIRLNLKAKSKEEAIEELAQLLVAAGYVEEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGI
AVLRLKEPVDFGSLDGQPVHLIFLLAAPDSNEHLKALSQLARLLSDEEFVEQLLNAQSKEEILALL
>gnl|CDD|238130 cd00212, PTS_IIB_glc, PTS_IIB, PTS system, glucose/sucrose specific IIB subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIB PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation
EQLAKDILEALGGKENIVSLDHCATRLRLTVKDESKVDEAALKKLGGVKGVVKNGGQYQVIIGPGVADVY
KEAIKLLG
>gnl|CDD|238131 cd00213, S-100, S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins
SELEKAIETIIDVFHKYSGKEGDKDTLSKKELKELLETELPNFLKNQKDPEAVDKIMKDLDVNKDGKVDF
QEFLVLIGKLAVACHEFF
>gnl|CDD|238132 cd00214, Calpain_III, Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Catalytic domain and the two calmodulin-like domains are separated by C2-like domain III. Domain III plays an important role in calcium-induced activation of calpain involving electrostatic interactions with subdomain II. Proposed to mediate calpain's interaction with phospholipids and translocation to cytoplasmic/nuclear membranes. CD includes subdomain III of typical and atypical calpains
RKWHTKSFNGEWRRGQTAGGCRNNPDTFWTNPQFRIRVPEPDDDEGKCTVLIALMQKNRRHLRKKGLDLL
TIGFHVYKVPGENRHLRRDFFLHKAPRARSSTFINTREVSLRFRLPPGEYVIVPSTFEPGEEGEFLLRVF
SEKSIKSSEL
>gnl|CDD|238133 cd00215, PTS_IIA_lac, PTS_IIA, PTS system, lactose/cellobiose specific IIA subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIA PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation. This family of proteins normally function as a homotrimer, stabilized by a centrally located metal ion. Separation into subunits is thought to occur after phosphorylation
LELISFQIILHAGNARSKALEALKAAKEGDFAEAEELLEEANDSLNEAHHAQTKLLQQEASGEKVEVSLL
LVHAQDHLMTTITLKDLAKEMIELYKK
>gnl|CDD|199833 cd00216, PQQ_DH_like, PQQ-dependent dehydrogenases and related proteins. This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ
ADNVFQLTPAWSFSTGDGGNRGSELTPIVVDGVMYATTSFSRVFALDADDGKEIWSYDPALKDGWFEACC
DLVNRGVAVWGGKVYIGVLDGRVYALNAETGKVAWKVKNADVLGGYTATSAPVVVDGLVIIGSSGDEFGV
RGYLTAYDVATGEEKWRFYLVMPDPNLLPGKDSTVTDRNTPTGDEHTWTSGGGTGWSSAAYDAELNLIYV
GGGNPTPWNWGGNRTPGDNLYTSSIVAVNADTGEMKWQYQTTPHDAWDYDGDNTPVLADIKVKGKKVKVL
FAPAKNGNFYVLDRRNGELVSARPLVPDSYDPDRELFYVPANGRIMALDPVTGVVVWEKSELHPLLGGPL
STAGNLVFVGTSDGYLKAYNADTGEKLWQQKVPSGFQAEPVTYEVDGEQYVLIQAGGGGAFPLWGGMADL
TRGTQMGGTVVVYK
>gnl|CDD|271174 cd00217, INT_Flp_C, Flp Tyrosine-based site-specific recombinases (also called integrases), C-terminal catalytic domain. Yeast Flp-like recombinases mediate the amplification of the 2 micron circular plasmid copy number by catalyzing the intra-molecular recombination between two inverted repeats during replication. They belong to the DNA breaking-rejoining enzyme superfamily, which also includes prokaryotic tyrosine recombinases and type IB topoisomerases. These enzymes share the same fold in their catalytic domain containing six conserved active site residues and the overall reaction mechanism. Flp-like recombinases are almost exclusively found in yeast and are highly diverged in sequence from the prokaryotic tyrosine recombinases. They cleave their target DNA in trans with a composite active site in which the catalytic tyrosine is provided by a promoter bound to a site other than the one being cleaved. Thus each active site within Flp complexes is assembled by domain swapping and contains catalytic residues from two different monomers. Two DNA segments are synapsed by the tetrameric enzyme, carrying the nucleophilic tyrosine in each active site with only two of the four monomers active at a given time. The catalytic domain is linked through a flexible loop to the N-terminal domain, which is largely responsible for non-specific DNA binding and isomerization. Its overall fold is similar to the SAM domain fold also found in the N-terminal domains of lambda integrase and XerD recombinase
LIPVRPAILIELFLELFGKDKIEDKRKLASLLTYLILMAFPAITEVKRGTFRKYKTIISNSLSFDYSRKT
IQFKYRLKKNRLLQKGLEDAEPPYKFVILSDKRQEENLFIIDKVPLEPNTESKHIRNSEVNLEFTNILSE
KESIWKIIYKILDSFEENTSRTTTKARYKLLLLATFTNCCRISDLKNLDPSTFELVKNKYLGTIVRAHVT
ETKTRISRTVYFFPARGRCDLLLALDEYLRICKPIPKTVVSDQNVNQKYQLLKESLVRSYNKFLSKHPAE
PIFKIKNGPKSHLGRHLMASFLSKNELDKEANSLGNWSKVREIGSAVARRNYTHTITPCPDSLFAFISGY
YQISPEGSEIELNNNKNPMERVHTIPELPTSEDELQLRYGHWAKIISHDVLAFLSEYSRK
>gnl|CDD|132995 cd00218, GlcAT-I, Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan synthesis. Beta1,3-glucuronyltransferase I (GlcAT-I) domain; GlcAT-I is a Key enzyme involved in the initial steps of proteoglycan synthesis. GlcAT-I catalyzes the transfer of a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region of trisaccharide Gal-beta-(1-3)-Gal-beta-(1-4)-Xyl of proteoglycans. The enzyme has two subdomains that bind the donor and acceptor substrate separately. The active site is located at the cleft between both subdomains in which the trisaccharide molecule is oriented perpendicular to the UDP. This family has been classified as Glycosyltransferase family 43 (GT-43)
PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPSDPT
WLKPRGVEQRNLALRWIREHLSAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVC
ENGKVVGWHTAWKPERPFPIDMAGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVLDRKELEPLANN
CSKVLVWHTRTEK
>gnl|CDD|119405 cd00219, ToxGAP, GTPase-activating protein (GAP) domain found in bacterial cytotoxins, ExoS, SptP, and YopE. Part of protein secretion system; stimulates Rac1- dependent cytoskeletal changes that promote bacterial internalization
VLQSALPSALKGLDKASELESLDAEQLRKNHDRLATGNGPLRSLVTALQGIRQGSQGGQLRDQATRLLNT
QIGGIPFSQWGTCGGAASELVDSASPEQLTEAAKQLHGLMQEVALLLSAV
>gnl|CDD|238135 cd00220, VMO-I, Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in the outer layer of the vitelline membrane of poultry eggs; VMO-I, lysozyme, and VMO-II are tightly bound to ovomucin; this complex forms the backbone of the outer layer; VMO-I has three distinct internal repeats; all three repeats are used to define the domain here; VMO-I has recently been shown to synthesize N-acetylchito-oligosaccharides from N-acetylglucosamine; may be a carbohydrate-binding protein; member of the beta-prism-fold family
TVIESPNGGNWGTWGQWERCPSGSFANGFQLKYETPQGFSDDTGLNAIALFCNPPDGKTSNSENEIISGE
GPWGSWREIQWCPNGTVIVGFALRSEPEQGKGDDTGANNFAAYCGRPEGRRKKTLSAEGDTNEWGSWTKD
QFCPAGQAVCGIQTRIEPPQGLGDDTALNNVNLKCCR
>gnl|CDD|411702 cd00221, Vsr, Very short patch repair endonuclease. Very short patch repair (Vsr) is an endonuclease functioning in DNA repair that recognizes damaged DNA and cleaves the phosphodiester backbone. Vsr endonucleases have a common endonuclease topology that has been tailored for recognition of TG mismatches. It belongs to a superfamily of nucleases including archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI
FTPEKRSRIMSRIRSKNTKPELAVRKALWARGLRYRLHVKKLPGKPDIVFPKYKVAVFVDGCFWHGCPCK
KGKIPKSNREFWRAKIERNRERDRRVNAELRKLGWRVLRIWEHEIKKNPEKCARKILRALRKR
>gnl|CDD|212461 cd00222, CollagenBindB, Repeat unit of collagen-binding protein domain B. The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold
TDITVTKTWDDDDNQDGKRPESITVQLLANGKETGDTVTLTASNDWTYTFTNLPKYDENGKEITYTVKEV
PVPGYTTTVTGDDGGFTITNTH
>gnl|CDD|173774 cd00223, TOPRIM_TopoIIB_SPO, TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in the type IIB family of DNA topoisomerases and Spo11. This subgroup contains proteins similar to Sulfolobus shibatae topoisomerase VI (TopoVI) and Saccharomyces cerevisiae meiotic recombination factor: Spo11. Type II DNA topoisomerases catalyze the ATP-dependent transport of one DNA duplex through another, in the process generating transient double strand breaks via covalent attachments to both DNA strands at the 5' positions. TopoVI enzymes are heterotetramers found in archaea and plants. Spo11 plays a role in generating the double strand breaks that initiate homologous recombination during meiosis. S. shibatae TopoVI relaxes both positive and negative supercoils, and in addition has a strong decatenase activity. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD. For topoisomerases the conserved glutamate is believed to act as a general base in strand joining and, as a general acid in strand cleavage. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function
DFVLVVEKEAVFQRLIEEGFHERNNCILITGKGYPDRATRRFLRRLHEELDLPVYILVDGDPYGISILLT
YKYGSIKLAYESESLATPDLRWLGLRPSDIIRLPDLPLLPLSERDLKRAKSLLRRPRFKELPEWKRELQL
MLKLGKKAEIEALASCGLEF
>gnl|CDD|238137 cd00224, Mog1, homolog to Ran-Binding Protein Mog1p; binds to the small GTPase Ran, which plays an important role in nuclear import. Binding is independent of Ran's nucleotide state (RanGTP/RanGDP)
CPLFGGAFSAILPPGFIDVSDLRPVPDNQEVFCHPSTDQSLIVELLELQAHVRDEEAARYHFEDLASVND
AEGVEVLSVQPLSLEGTSLTGCCAWLLSGKQENQEVAKDVTIHVALIRLPQYQTDLLLTFNQPPPDSRSS
VGSNLLSPASCWSLGDFEQLVTSLTLHDPNLFG
>gnl|CDD|119406 cd00225, API3, Ascaris pepsin inhibitor-3 (API3); protein inhibitor that reversibly inhibits aspartic proteinase cathepsin E, and gastric enzymes pepsin and gastricsin
TFAVSGGGGGSAGCVVTDNVLFANGFPLRELTPDEQQELAQYVEDVADYKEEVKQALKERQEGLKLRRAG
KKKKAVTLAEEKLPKAPKKPSFCSPDDTTQFYFDGCMVQNNKVYVGNTYARDLTPKEIAELKTFEKKQTA
YQEPEAPPEPPEPPNFCTA
>gnl|CDD|238138 cd00226, PRCH, Photosynthetic reaction center (RC) complex, subunit H; RC is an integral membrane protein-pigment complex which catalyzes light-induced reduction of ubiquinone to ubiquinol, generating a transmembrane electrochemical gradient of protons used to produce ATP by ATP synthase. Subunit H is positioned mainly in the cytoplasm with one transmembrane alpha helix. Provides proton transfer pathway (water channels) connecting the terminal quinone electron acceptor of RC, to the aqueous phase. Found in photosynthetic bacteria: alpha, beta, and gamma proteobacteria
MVGGAIFQYFDLAQLVIYAFWIFFAGLIYYLRRENMREGYPLEDPDGGPSENGGVFPLPYPKTFKLPHGG
TVTVPRVEAETRALALARTAPFEGAPLVPTGNPMLDGVGPASWAERRDLPDLDVHGHPKIVPMRVATGFS
VAAGDVDPRGLPVVGADGEVAGKVTDLWVDRPEQLFRYLEVELAGGGRTVLLPMGFAKVKSDRVKVTAIL
SEHFANVPTIKSPDQVTLLEEDKICAYYAGGLLYAT
>gnl|CDD|238139 cd00227, CPT, Chloramphenicol (Cm) phosphotransferase (CPT). Cm-inactivating enzyme; modifies the primary (C-3) hydroxyl of the antibiotic. Related structurally to shikimate kinase II
TGRIIILNGGSSAGKSSIARALQSVLAEPWLHFGVDSFIEALPLKCQDAEGGIEFDGDGGVSPGPEFRLL
EGAWYEAVAAMARAGANVIADDVFLGRAALQDCWRSFVGLDVLWVGVRCPGEVAEGRETARGDRVPGQAR
KQARVVHAGVEYDLEVDTTHKTPIECARAIAARVQ
>gnl|CDD|238140 cd00228, eu-GS, Eukaryotic Glutathione Synthetase (eu-GS); catalyses the production of glutathione from gamma-glutamylcysteine and glycine in an ATP-dependent manner. Belongs to the ATP-grasp superfamily
PPIPDDKDQLEELAKDANDWAVANGLVMRDKSVQESSVVASHAPFTLLPSPFPEALFEQAVEVQPDFNEL
VDRISQDGKFLQQSLSSTKKVDEFTSRLLDIHKKVLEENKKQPVRLGIFRSDYMFDEKDGTKGLKQIEIN
TISSSFGGLSSRVTELHRYVLSALGYSKGLDSNRIPSNNAVKGIAEALAKAWEEYGDPRAVVLFVVQNEE
RNIYDQRFLEAELLERHQIHVIRKTLADVDEEGSLDDDGTLFVDGQEVAVVYFRAGYTPDDYPSESEWEA
RLLMERSSAIKCPSISTQLAGTKKIQQELAEPGVLERFLPNPEEVAKLRATFAGLYSLDDTEEGDEIVRK
ALEKPELFVLKPQREGGGNNIYGEEMREALLKLQGSEERAAYILMEKIFPEPSENYLLRAGGPSHKEQAI
SELGIYGTYLRNKDEVVMNKQSGHLLRTKPISSAEGGVAAGFAVLDSIYLV
>gnl|CDD|238141 cd00229, SGNH_hydrolase, SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid
ILVIGDSITAGYGASSGSTFYSLLLYLLLLAGGPGVEVINLGVSGATTADALRRLGLRLALLKDKPDLVI
IELGTNDLGRGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEAIKAVAA
ENPAPSGVDLVDLAALLGDEDKSLYSPDGIHPNPAGHKLIAEALASA
>gnl|CDD|238142 cd00231, ZipA, ZipA C-terminal domain. ZipA, a membrane-anchored protein, is one of at least nine essential gene products necessary for assembly of the septal ring which mediates cell division in E.coli. ZipA and FtsA directly bind FtsZ, a homolog of eukaryotic tubulins, at the prospective division site, followed by the sequential addition of FtsK, FtsQ, FtsL, FtsW, FtsI, and FtsN. ZipA contains three domains: a short N-terminal membrane-anchored domain, a central P/Q domain that is rich in proline and glutamine and a C-terminal domain, which comprises almost half the protein
EAVIILNVAAHHGSEFNGEKLLQSIQQSGFIFGDMNIFHRHLSLSGSGPVLFSVANMVKPGTFDPDNMAD
FSTPGISFFMQLPSPGDALQNFKLMLQAAQRIADDLGGVVLDDQRRMMTPQKLRAYRDRI
>gnl|CDD|350855 cd00232, HemeO-like, heme oxygenase. Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. This family serves a variety of specific needs in different branches of life: in vertebrates, HO plays a role in heme homeostasis and oxidative stress response, and cellular signaling in mammals that include isoforms HO-1 and HO-2; in photosynthetic organisms including cyanobacteria, algae, and higher plants, biliverdin is used for photosynthetic pigment formation or light-sensing; and, in pathogenic bacteria, HO is part of a pathway for iron acquisition from host heme and heme products. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology
LSKRLKKATREVHNVSESLVNSRLPALFVSKDNYAKFLACQYYFFVALEAAYDEALLKGDFDKDPLLEGL
ARADAFKQDLADLGGPTWQADLGTKSQAKDYEAHLAELGRSSPALLLAHLYTQELSMLSGGQFLKKWAQK
LFQLPDDVGAAHFAYPGESRNKLWSAFVKQLDELELTPELEDQAISEALAAFGHNNALLEE
>gnl|CDD|238144 cd00233, VIP2, VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative insecticidal proteins (VIPs) possesses high specificity against the major insect pest, corn rootworms, and belongs to a classs of binary toxins and regulators of biological pathways distinct from classical A-B toxins. A novel family of insecticidal ADP-ribosyltransferses were isolated from Bacillus cereus during vegetative growth, where VIP1 likely targets insect cells and VIP2 ribosylates actin. VIP2 shares significant sequence similarity with enzymatic components of other binary toxins, Clostridium botulinum C2 toxin, C. perfringens iota toxin, C. piroforme toxin, C. piroforme toxin and C. difficile toxin
KTLDFKNDIDEAEAWGNKNYKKWLKKLSPSEKEAIREYTGSDYKKINNYLRGNGGPENSLNSELDKQIEN
IDSAFKKKPIPENITVYRGVDMTYLGLIFQSTDGTINKTVNKQFEAKFLGKIYKDDGFMSTSLVSESAFG
GRPIILRLTVPKGSKGAYISPISGFPGELEVLLPRGSTYKINKITVSSDGNKQIVIDAELI
>gnl|CDD|119413 cd00235, TLP-20, Telokin-like protein-20 (TLP-20) domain; a baculovirus protein that shares some antigenic similarities to the smooth muscle protein telokin, a kinase-related protein
MATNSNGTVDIAVYVRLDREEDRNVLSFIVQDEYHLKKLAVGAYAVNVLDSSLLDALHNGAYSTVACGDY
TVVYNLNANSNGINVILFNKKPIILKKGSCIFKIKYWN
>gnl|CDD|238145 cd00236, FinO_conjug_rep, FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two component FinOP system which is responsible for repressing bacterial conjugation; the FinOP system represses the transfer (tra) operon of the F-plasmid which encodes the proteins responsible for conjugative transfer of this plasmid from host to recipient Escherichia coli cells; antisense RNA, FinP is thought to interact with traJ mRNA to occlude its ribosome binding site, blocking traJ translation and thereby inhibiting transcription of the tra operon; FinO protects FinP against degradation by binding to FinP and sterically blocking the cellular endonuclease RNase E; FinO also also binds to the complementary stem-loop structures in traJ mRNA and promotes duplex formation between FinP and traJ RNA in vitro; this domain contains two independent RNA binding regions
VGKNKLAEKADREAELAAKKKPARQALSIYLNLPTVEYAVECLKKWFPGLFPGDTPRLLKCGIKDGILQD
VAQHPNIPLTHEELRCAVKAITRRESYLQAMVAGAPRYDLEGYVAGHISQEAEVYAARLLDKIRRQQRIK
KELKRV
>gnl|CDD|107218 cd00237, p23, p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis
PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNGDNVKIYNEIELYDRVDPNDSKHKRTDRSI
LCCLRKGKEGVAWPRLTKEKAKPNWLSVDFDNWRDW
>gnl|CDD|238146 cd00238, ERp29c, ERp29 and ERp38, C-terminal domain; composed of the protein disulfide isomerase (PDI)-like proteins ERp29 and ERp38. ERp29 (also called ERp28) is a ubiquitous endoplasmic reticulum (ER)-resident protein expressed in high levels in secretory cells. It contains a redox inactive TRX-like domain at the N-terminus. The expression profile of ERp29 suggests a role in secretory protein production, distinct from that of PDI. It has also been identified as a member of the thyroglobulin folding complex and is essential in regulating the secretion of thyroglobulin. The Drosophila homolog, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase. ERp38 is a P5-like protein, first isolated from alfalfa (the cDNA clone was named G1), which contains two redox active TRX domains at the N-terminus, like human P5. However, unlike human P5, ERp38 also contains a C-terminal domain with homology to the C-terminal domain of ERp29. It may be a glucose-regulated protein. The function of the all-helical C-terminal domain of ERp29 and ERp38 remains unclear. The C-terminal domain of Wind is thought to provide a distinct site required for interaction with its substrate, Pipe
IEELDELAKEFVDASDEERKELLEKVKEAVEKLKEAEAKYAKYYVKVMEKILEKGEDYVEKELARLERLL
EKKGLAPEKADELTRRLNILRSF
>gnl|CDD|119414 cd00239, PapG_CBD, PapG carbohydrate / receptor binding domain (CBD); PapG, the adhesin of the P-pili, is situated at the tip, mediating the attachment of uropathogenic Escherichia coli to the uroepithelium of the human kidney; PapG has a two-domain architecture: a carbohydrate binding N-terminus (this domain) and chaperone binding C-terminus (C-terminal pilin region). The carbohydrate-binding domain interacts with the receptor glycan. There are 3 PapG alleles, class I-III, which bind to different receptor isotypes, GbO3, GbO4, and GbO5, respectively
WHNVMFYSFNDYIYYPGGNVKVTDRPQFIIPWNTGTATATYVSCNGPEFASGVYFQEYIAWVVVPKHVST
QNGYNIFLEVQSKGSWSLENTGDNDNYYFLKGYEWDEWTFDGGRTCFNPGEKKQLANKFNDLTFNVLLPV
DLPKGDYTFPVKYIRGIQRHYYDYWGGRYKIPYSQMKTLPATNTLMFSFKNTGG
>gnl|CDD|238147 cd00240, TFIIFa, Transcription initiation factor IIF, alpha subunit, N-terminal region of RAP74. Subunit of transcription initiation complex involved in initiation, elongation and promoter escape.Tetramer of 2 alpha and 2 beta TFIIF subunits interacts directly with RNA polymerase II. TFIIF inhibits non-specific transcription initiation by PolII and recruits the polymerase to the preinitiation complex on promoter DNA for site-specific transcription initiation. The PolII/TFIIF-complex attaches through direct interactions of TFIIF with promoter DNA, TFIIB and the TAF250 subunit of TFIID, and provides scaffolding for addition of TFIIE and TFIIH. Together with TFIIE, TFIIF participates in DNA strand separation (open complex formation). N-terminal domains of RAP30 and RAP74 co-fold to form a single core structure, a triple barrel heterodimer, and has pseudo-2-fold symmetry
YEFSVRVPKLCLKKYRVMAFNASDKVDFAGWVVVRLEREYNVRAIAPTEENQFEFGAGSEYNRSLREEAR
RKKFGIAQRKYRPENQPWILEVEGKGQRQFKGIREGGVNENATYYVFTMQPDGEFEAYPVGEWYNFNPVA
RYKTLTAEEAEEEFKRRRKVMN
>gnl|CDD|187675 cd00241, DOMON_like, Domon-like ligand-binding domains. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases
GALDIDPSGLGGGGPGDLSATVKLAWDGEYLYFLVEVTDDVLRDTAALSLVWDGDGVELFFDPDNDGTDG
NAFGYGIDLYGFSVDLADGSGTAADYGTEGGREGVSSSAKKGGGGYTVEFAIPLAALDGLDPGKGKGYGF
AFAINDGSADDRRHPSVF
>gnl|CDD|153074 cd00242, Ecotin, Protease Inhibitor Ecotin; homodimeric protease inhibitor. Protease Inhibitor Ecotin; homodimeric protease inhibitor which binds two chymotrypsin-like serine proteases to form a heterotetramer. Found in bacterial periplasm. Inhibits a broad range of serine proteases including collagenase, trypsin, chymotrypsin, elastase, and factor Xa but not thrombin. Inhibition mechanism involves binding at two different protease contact sites: the primary and secondary binding sites. Primary site loops of ecotin bind to the active site of target proteases in a substrate-like manner with the P1 residue in ecotin mimicking the interactions of a canonical P1 substrate residue
QPLEKIAPYPQAEKGMKRQVIFLDPQGDESTLKVELIIGRTLEVDCNQHRLGGNLEEKTLEGWGYDYYVV
DKVSSPVSTMMACPDGKKEQKFVTANLGAGMLRYNSRLPIVVYTPKDVEVRYRIWKAGEKIQNAVV
>gnl|CDD|119415 cd00243, Lysin-Sp18, Sp18 and Lysin from Archaegastropoda (marine mollusks of the families Halotidae and Trochidae) sperm. Both proteins play an important role in fertilization: sp18 mediates fusion between sperm and egg cell membrane, lysin dissolves the vitelline envelope surrounding the egg; they are believed to be a product of gene duplication and subsequent divergence
VGRENEVALKVGIIAGLDRKLDKWLRRHGDRLSPPQKKTLYFVNRRRMQTHWQNYMLWSKKIIRKLGRPP
NVKDYTRLGREIGRRIYMEHLYSFLVRRNRRPKLTPYMRKLLATRPADLPVR
>gnl|CDD|238148 cd00244, AlgLyase, Alginate Lyase A1-III; enzymatically depolymerizes alginate, a complex copolymer of beta-D-mannuronate and alpha-L-guluronate, by cleaving the beta-(1,4) glycosidic bond
VVAAARLVPPSGYYADVLKRKGPKAYDCTAVPNPYTGELVFRSKYEGSDHARATLNEPAEKAFRDFTKDI
TTLERGYVKTVMQYMRDGRPVYLTCLLNMLDAWAKADALLSYDFNHTGKSMRKWALGSLAGAYSRLKFSP
SHPLAADTEQAERIEKWFARVADQVVSDWSGLPLKKINNHSYWAAWSVMATGVATNRRDLFDWAVGEYKV
AAGQVDEDGFLPNELKRRQRALAYHNYALPPLAMIAEFAQRNGVDLRKENGGALHRLAKRVLAGVKDPDL
FKEYAGEDQDMTDLKPDRKFAWLEPYCALYGCAPDVRELKFMTVPFKDFRLGGDVTRVF
>gnl|CDD|238149 cd00245, Glm_e, Coenzyme B12-dependent glutamate mutase epsilon subunit-like family; contains proteins similar to Clostridium cochlearium glutamate mutase (Glm) and Streptomyces tendae Tu901 NikV. Glm catalyzes a carbon-skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate. The first step in the catalysis is a homolytic cleavage of the Co-C bond of the coenzyme B12 cofactor to generate a 5'-deoxyadenosyl radical. This radical then initiates the rearrangement reaction. C. cochlearium Glm is a sigma2epsilon2 heterotetramer. Glm plays a role in glutamate fermentation in Clostridium sp. and in members of the family Enterobacteriaceae, and in the synthesis of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis. S. tendae Tu901 glutamate mutase-like proteins NikU and NIkV participate in the synthesis of the peptidyl nucleoside antibiotic nikkomycin. NikU and NikV proteins have sequence similarity to Clostridium Glm sigma and epsilon components respectively, and may catalyze the rearrangement of 2-oxoglutaric acid to 2-keto-3-methylsuccinic acid during nikkomycin synthesis
KNFAKKLEKADKEGKLVVQPRAGFPLLEEHIELLRTLQEEGAADVLPLTIDSYTRVNDYEEAEEGLEESI
KAGKSLLNGFPIVNHGVKTCRKLLEGVDFPVQVRHGTPDARLLAEIAIASGFDATEGGPISYNLPYSKNV
PLEKSIENWQYCDRLVGFYEENGVPINREPFGPLTGTLVPPSILIAIQILEALLAAEQGVKSISVGYAQQ
GNLTQDIAALRALRELAKEYLPKYGYKDVDIHTVFHQWMGGFPRDESGAFGLIGYAATIAALSGATKVIV
KTPDEAHGIPTIEANVAGLKATATVLNMLRGQKFPPSEAIEQEEEIIKAEVKAILDKVFELGDGDVARGT
VKAFEAGVLDIPFCPSIYNAGKMRPARDDNGRIRYLEFGNLPIPEDIKDFHRQRLAERAKAEGRELSFQM
VIDDIFAV
>gnl|CDD|238150 cd00246, RabGEF, Nucleotide exchange factor for Rab-like small GTPases (RabGEF), Mss4 type; RabGEF positely regulates the function of Rab GTPase by promoting exchange of GDP for GTP; members of the Rab subfamily of Ras GTPases are important in vesicular transport
KAVLCQRCGSRVLTIQPGTVLFLPRQLFLPSMRKKPGSNPDGDLLEDHWLVVDMFTFENVGFSKDVGNLK
YLVCADCEKGPIGYHCLDDKNSEYVALERVSHE
>gnl|CDD|238151 cd00247, Endostatin-like, Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of collagen XV/XVIII, a proteoglycan/collagen found in vessel walls and basement membranes; this domain has a compact globular fold similar to that of C-type lectins; endostatin XVIII is monomeric and contains a heparin-binding epitope and zinc binding sites while endostatin XV is trimeric and contains neither of these sites; the generation of endostatin or endostatin-like collagen XV/XVIII fragments is catalyzed by proteolytic enzymes within the protease-sensitive hinge region of the C-terminal domain; endostatin inhibits endothelial cell migration in vitro and appears to be highly effective in murine in vivo studies
QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKG
EVLFNSWESLFSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVT
GQASSLSSGKLLEQKAYSCENKLIVLCIENS
>gnl|CDD|238152 cd00248, Mth938-like, Mth938-like domain. The members of this family include: Mth938, 2P1, Xcr35, Rpa2829, and several uncharacterized sequences. Mth938 is a hypothetical protein encoded by the Methanobacterium thermoautotrophicum (Mth) genome. This protein crystallizes as a dimer, although it is monomeric in solution, with one disulfide bond in each monomer. 2P1 is a partially characterized nuclear protein which is homologous to E3-3 from rat and known to be alternately spliced. Xcr35 and Rpa2829 are hypothetical proteins of unknown function from the Xanthomonas campestris and Rhodopseudomonas palustris genomes, respectively, for which the crystal structures have been determined
PIDGYGPGGFRIAGQVYRGPLLVLPDGVVPWDGTSLSDLDPEALLPLLAEDRPDILLIGTGAEIAFLPRA
LRAALRAAGIGVEVMSTGAACRTYNVLLSEGRRVAAALI
>gnl|CDD|238153 cd00249, AGE, AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is structurally and mechanistically distinct from the other four types of epimerases. The AGE domain monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is also found in glucoamylase and cellulase. The active form is a homodimer. The alignment also contains subtype III mannose 6-phosphate isomerases
IAETLQELAQLAGWLLEDLLPFWLEAGLDREAGGFFECLDRDGQPFDTDRRLWLQARQVYCFAVAYLLGW
RPEWLEAAEHGLEYLDRHGRDPDHGGWYFALDQDGRPVDATKDLYSHAFALLAAAQAAKVGGDPEARALA
EETIDLLERRFWEDHPGAFDEADPGTPPYRGSNPHMHLLEAMLAAYEATGEQKYLDRADEIADLILDRFI
DAESGVVREHFDEDWNPYNGDKGRHQEPGHQFEWAWLLLRIASRSGQAWLIEKARRLFDLALALGWDPER
GGLYYSFLDDGGLLEDDDKRWWPQTEALKAALALAGITGDERYWQWYQRAWAYLWRHFIDPEYGLWFGYL
DADGKVLLTPKGPAKTFYHVVRALYEALDVLAAL
>gnl|CDD|238154 cd00250, CAS_like, Clavaminic acid synthetase (CAS) -like; CAS is a trifunctional Fe(II)/ 2-oxoglutarate (2OG) oxygenase carrying out three reactions in the biosynthesis of clavulanic acid, an inhibitor of class A serine beta-lactamases. In general, Fe(II)-2OG oxygenases catalyze a hydroxylation reaction, which leads to the incorporation of an oxygen atom from dioxygen into a hydroxyl group and conversion of 2OG to succinate and CO2
LRRFERPAQRLWGSLCKALPVLSFLEVLELDSPLGKLLLASAGVGFAELEGAPLDPAALLGLAERIGFIR
GTLYGDVVPVPGKENAQNGAYTNTLLPLHTDLAYHEYRPGLQILHCLRNTATGGATLLVDGFRVALKLLR
EDPEAFELLSRVPVRHAYPGSSGTMFSSYQLAPVLELDPEDPVLRYNNYDNFSVPFDEVKEAYEALAELV
ALIEDPDNQLTVKLEPGDLLIFDNRRVLHGRTAFSPRYGGDRWLKGCYVDRD
>gnl|CDD|119403 cd00251, Mth_Ecto, The ectodomain of Methuselah (Mth); Mth mutants have a 35% increase in average lifespan and increased resistance to several forms of stress, including heat, starvation, and oxidative damage; The protein affected by this mutation is related to G protein-coupled receptors of the secretin receptor family; Mth, like secretin receptor family members, has a large N-terminal ectodomain, which may constitute the ligand binding site
CDFFDTVNITGSQRFPNGSYLYEGIIIPAHLTGEYDYVILPDGSREPVPEHLRGCVCKLKPCIRFCCPHG
KIMDNGQCSDTVQEELRYDPYVNITLADGSVDLRHVLTEFIVQGDLPLPCESMYELDRENEFDEWTLFEN
GTLLRHYDSRLLSKQEYCLQPRNFNNESIELVPHNC
>gnl|CDD|320009 cd00252, EFh_SPARC_EC, EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC)-like proteins. The SPARC protein family represents a diverse group of proteins that share a follistatin-like (FS) domain and an extracellular calcium-binding (EC) domain with two EF-hand motifs. It includes SPARC (for secreted protein acidic and rich in cysteine, also termed osteonectin/ON, or basement-membrane protein 40/BM-40), SPARC-like protein 1 (for secreted protein, acidic and rich in cysteines-like 1/ SPARCL1, also termed high endothelial venule protein/Hevi, or MAST 9, or SC-1, or RAGS-1, or QR1, or ECM 2), testicans 1, 2, and 3 (also termed SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycans, or SPOCK), secreted modular calcium-binding protein SMOC-1 (also termed SPARC-related modular calcium-binding protein 1) and SMOC-2 (also termed SPARC-related modular calcium-binding protein 2, or smooth muscle-associated protein 2/SMAP-2), follistatin-related protein 1 (FRP-1, also termed follistatin-like protein 1/fstl-1, TSC-36/Flik, TGF-beta inducible protein). The SPARC proteins have been implicated in modulating cell interaction with the extracellular milieu, including regulation of extracellular matrix assembly and deposition, counter-adhesion, effects on extracellular protease activity, and modulation of growth factor/cytokine signaling pathways, as well as in development and disease
CPGSELMQFPDRLLDWLLLLKEQDENRSYDNNKRGHDLSGTMRKEIAQWEFDNLDNNKDGKLDKRELAPF
RAPLMPLEHCARGFFESCDLNKDKKISLQEWLGCFGV
>gnl|CDD|238156 cd00253, PL_Passenger_AT, Pertactin-like passenger domains (virulence factors) of autotransporter proteins of the type V secretion system. Autotransporters are proteins used by Gram-negative bacteria to transport proteins across their outer membranes. The C-terminal (beta) domain of autotransporters forms a pore in the outer membrane through which the N-terminal passenger domain is transported. Following transport, the passenger domain is generally cleaved by an outer membrane protease with the passenger domain either remaining in contact with the surface via a noncovalent interaction with the beta domain or cleaved to release a soluble protein. These proteins are highly diverse and perform a variety of functions that promote virulence, including catalyzing proteolysis, serving as an adhesin, mediating actin-promoted motility, or serving as a cytotoxin. Proteins in this family share similarity in the C-terminal region of the passenger domain as seen in the pertactin structure P.69, a Bordetella pertussis agglutinogen responsible for human pertussis. The P.69 protein consists of a 16-stranded parallel beta-helix with a V-shaped cross-section, and is one of the largest beta-helix known to date
GTLSGNATINGGGDLTLGGGGALTLTGNSVWLGTLQAGGGTVSLNSNSLWTLTGDSTVNGNLTNSGGTVD
FGSASGAFNTLTVNGNYLGGNGTFVLNTDLGGDNSPTDKLVVTGNASGTTNVAVVNAGGEGASTGDGIEL
VEVNGGSDAAFSLAGRVDAGAYEYTLYKGGVGNNGNWYLRSTLAPP
>gnl|CDD|381594 cd00254, LT-like, lytic transglycosylase(LT)-like domain. Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue
PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGRRGVDDLFDPEENIRAGARYLRELLDRFGGD
LELALAAYNAGPGAVDRWGGGEVPPYKETRNYVQRVLAYYQ
>gnl|CDD|238158 cd00255, nidG2, Nidogen, G2 domain; Nidogen is an important component of the basement membrane, an extracellular sheet-like matrix. Nidogen is a multifunctional protein that interacts with many other basement membrane proteins, like collagen, perlecan, lamin, and has a potential role in the assembly and connection of networks. Nidogen consists of 3 globular domains (G1-G3), G3 is the lamin-binding domain, while G2 binds collagen IV and perlecan. Also found in hemicentin, a protein which functions at various cell-cell and cell-matrix junctions and might assist in refining broad regions of cell contact into oriented, line-shaped junctions. Nidogen G2 consists of an N-terminal EGF-like domain (excluded from this alignment model) and an 11-stranded beta-barrel with a central helix, a topology that exhibits high structural similarity to the green flourescent proteins of Cnidaria
GIPQRVNGKVSGNINVGQSPVEFGDADLHSYVVTSDGRAYTAISNIPESLGPSLRPLAPIGGTIGWLFAL
EQGGAKNGFSLTGGEFTRQAEVTFYTGGEKLRITQVARGLDSHGHLLLDTVISGRVPQVPAGATVHIEDY
TELYHYTGPGVLTSSSTREYTVDEGGESQTLSYQWNQTITYEECPHDDEAAPDLQQLLVARIFALYNPEE
EILRFAITNSIGPG
>gnl|CDD|238159 cd00256, VATPase_H, VATPase_H, regulatory vacuolar ATP synthase subunit H (Vma13p); activation component of the peripheral V1 complex of V-ATPase, a heteromultimeric enzyme which uses ATP to actively transport protons into organelles and extracellular compartments. The topology is that of a superhelical spiral, in part the geometry is similar to superhelices composed of armadillo repeat motifs, as found in importins for example
SQFQEIAAEVRARKINWQSYMRSQMISEEDYQFIKALEKKRVKEEILDVLSGQYVKTFVNLLSQIDKDDT
VRYVLTLIDDMLQEDDTRVKLFHDDALLKKKTWEPFFNLLNRQDQFIVHMSFSILAKLACFGLAKMEGSD
LDYYFNWLKEQLNNITNNDYVQTAARCLQMLLRVDEYRFAFVLADGVPTLVKLLSNATLGFQLQYQSIFC
IWLLTFNPHAAEVLKRLSLIQDLSDILKESTKEKVIRIVLAIFRNLISKRVDREVKKTAALQMVQCKVLK
TLQSLEQRKYDDEDLTDDLKFLTEELKNSVQDLSSFDEYKSELRSGRLHWSPVHKSEKFWRENADRLNEK
NYELLKILIHLLETSVDPIILAVACHDIGEYVRHYPRGKDVVEQLGGKQRVMRLLNHEDPNVRYEALLAV
QKLMVHNWE
>gnl|CDD|467441 cd00257, beta-trefoil_FSCN-like, fascin-like domain, beta-trefoil fold, found in the fascin-like family. The fascin-like family includes actin-bundling/crosslinking proteins facsin1-4, singed, hisactophilin, and FSHD region gene 1 protein (FRG1). Fascin, also called fascin-1, is an actin-binding protein that contains 2 major actin binding sites. It is involved in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. It plays an important role for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. It mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to nerve growth factor (NGF). Fascin-2, also called retinal fascin, is a photoreceptor-specific paralog of the actin-bundling protein fascin. It may play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis. Fascin-3, also called testis fascin, is a novel paralog of the actin-bundling protein fascin expressed specifically in the elongate spermatid head. Protein singed acts as an actin-bundling protein that may have a role in the asymmetric organization and/or movement of cytoplasmic components. It has a role in somatic cells during the formation of adult bristles and hairs, and in the female germline during oogenesis. Hisactophilin is a histidine-rich actin-binding protein from Dictyostelium discoideum. It exists in two isoforms, hisactophilin-1 (HatA, also called HS I) and hisactophilin-2 (HatB, also called HS II), which are both myristoylated and distributed between plasma membrane and cytoplasm. Hisactophilin may act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments. Protein FRG1 binds to mRNA in a sequence-independent manner. It may play a role in regulation of pre-mRNA splicing or in the assembly of rRNA into ribosomal subunits. It may be involved in mRNA transport, as well as in epigenetic regulation of muscle differentiation through regulation of activity of the histone-lysine N-methyltransferase KMT5B. This family also contains many homologs from bacteria, such as Zobellia galactanivorans beta-porphyranase A (PorA). PorA (EC 3.2.1.178) cleaves the sulfated polysaccharide porphyran at the (1-_4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1-_3)-beta-D-galactose. It is inactive on the non-sulfated agarose portion of the porphyran backbone and displays a strict requirement for C6-sulfate in the -2 and +1-binding subsites. Members of this family contain a fascin-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The fascin subfamily contains four copies of the fascin-like domain
GTVALKSSNGKYLSAENGGGGPLVANRDAAGPWETFTLVDLGDGKVALKSSNGKYLSAENGGGGTLVANR
TAIGPWETFTLVPLGNGKVALKSANGKYLSADNGGGGTLIANATSIGAWEKFTI
>gnl|CDD|238161 cd00258, GM2-AP, GM2 activator protein (GM2-AP) is a non-enzymatic lysosomal protein that acts as cofactor in the sequential degradation of gangliosides. GM2A is an essential cofactor for beta-hexosaminidase A (Hex A) in the enzymatic hydrolysis of GM2 ganglioside to GM3. Mutation of the gene results in the AB variant of Tay-Sachs disease. GM2-AP and similar proteins belong to the ML domain family
NGFSWSNCDGESLPAVIKSLTVNPDPINIPGDLTVSTVGSTSVPLSSPLKVILTLEKEVAGLWMKIPCLD
NIGSCTYDNACDLLDTLIPPGQQCPEPLRTYGLPCHCPFKEGVYSLPDSTFTLPNVDLPSWLTNGNYRIT
GILMADGKELGCGKFTFSLESS
>gnl|CDD|119404 cd00259, STNV, STNV domain; satellite tobacco necrosis virus (STNV) are small plant viruses which are completely dependent on the presence of a specific helper virus, TNV, for their replication; 60 identical subunits, this domain is one of them; form an icosahedral shell around a single RNA molecule. Half of the RNA codes for the coat protein with the other half being non-coding. The STNV domain has a "Swiss roll" Greek key topology with its two 4-stranded antiparallel beta sheets
RKQSQPSSKSDVKRVVKSIIGQSLEHKRFALLNPPNTVNTAGTVYNLSNGIIQGDDISQRTGDQIRLEQQ
VLRVRRTAITNSQTFRFIWFRDNTNRGTTPAVTEVLNSASFMSQYNPLTLQQKRFTILKDVELDCSLTGE
SIKHRLTFNQKVQVFYNGAAAVAASNGPGAIFFLVIGDSVVGQWDVGYEAVYTDA
>gnl|CDD|271229 cd00260, Sialidase, sialidases/neuraminidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates as well as playing roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed beta-propeller fold. This hierarchy includes eubacterial, eukaryotic, and viral sialidases
NFIPRPGEMSGSLCTRIPSVDCSPTECCYFALVILGTCRDRSHRHLISALLVLRTTAGRIPPTVENSISL
DDTQNRWSCSVCHDGRGCDMICSKGPETEEEDYNSAVNALMAIGYLGFDGQYHPVDLDVTTLFEAWNILR
TGEGGGSCIDGRCWFSVTDGSAPGRIQQRILSIKEGTLGRIPKLTVPTGTVLHGAEGTILTVGTSHFCYC
RDSSYFSPRPVYPMTVSTATLHSPYTCNAFTRDGPRPCQASARCPNSCVTGVKGDPYPLIFYTLRGTWGT
RTDSETSRLGMESAVFYDADATKRSRGTRVVSSKTKGGYSTSTCFKDVKTNCYYCCSIVEISNTLDKGKW
GSFAIVPLCVE
>gnl|CDD|238163 cd00261, AAI_SS, AAI_SS: Alpha-Amylase Inhibitors (AAIs) and Seed Storage (SS) Protein subfamily; composed of cereal-type AAIs and SS proteins. They are mainly present in the seeds of a variety of plants. AAIs play an important role in the natural defenses of plants against insects and pathogens such as fungi, bacteria and viruses. AAIs impede the digestion of plant starch and proteins by inhibiting digestive alpha-amylases and proteinases. Also included in this subfamily are SS proteins such as 2S albumin, gamma-gliadin, napin, and prolamin. These AAIs and SS proteins are also known allergens in humans
QQQCQPGQQQPQQPLNSCREYLRQQCSGVGGPPVWPQQSCEVLRQQCCQQLAQIPEQCRCEALRQMVQGV
IQQQQQQQEQQQGQEVERMRQAAQNLPSMCNLYPPPYCPF
>gnl|CDD|238164 cd00264, BPI, BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) domain; binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria.; Apolar pockets on the concave surface bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide
MVVLRLSEDVLNSALQVYLKAGALLLTLTIPDIPKALKLKLSGIIPLGAKKYPDMNLQLKILSLSSPTLK
LSPKGLDLSQSVSIELFVTWPASDGGNPLFSLEVEISASLQLSVDPGRLTLSLSLCSSTVELLSSNIGGF
GNFIVSLLQKVLNTILCPVVLPALNSKLRSGLPLLPVPPVPSPAGVDYSLTAEPVLSASFLLLDADVT
>gnl|CDD|238165 cd00265, MADS_MEF2_like, MEF2 (myocyte enhancer factor 2)-like/Type II subfamily of MADS (MCM1, Agamous, Deficiens, and SRF (serum response factor) box family of eukaryotic transcriptional regulators. Binds DNA and exists as hetero and homo-dimers. Differs from SRF-like/Type I subgroup mainly in position of the alpha helix responsible for the dimerization interface. Important in homeotic regulation in plants and in immediate-early development in animals. Also found in fungi
GRGKIEIKRIENSTNRQVTFSKRRNGLLKKAHELSVLCDAEVALIIFSSSGKLYEFSSPSMEKIIERYQK
TSGSSLW
>gnl|CDD|238166 cd00266, MADS_SRF_like, SRF-like/Type I subfamily of MADS (MCM1, Agamous, Deficiens, and SRF (serum response factor) box family of eukaryotic transcriptional regulators. Binds DNA and exists as hetero- and homo-dimers. Differs from the MEF-like/Type II subgroup mainly in position of the alpha 2 helix responsible for the dimerization interface. Important in homeotic regulation in plants and in immediate-early development in animals. Also found in fungi
GRKKIKIKRIENKKKRAVTFSKRRQGLFKKASELSTLCGAEVAVIVYSPSGKLYVFWPSSEVEGVISRFE
VLSALERKKKAVD
>gnl|CDD|213179 cd00267, ABC_ATPase, ATP-binding cassette transporter nucleotide-binding domain. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE
LRRRIGYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDP
ELAELAADRVIVLKDGK
>gnl|CDD|350669 cd00268, DEADc, DEAD-box helicase domain of DEAD box helicases. DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAP
TRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYL
VLDEADRMLDMGFEEDVEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE
>gnl|CDD|238168 cd00270, MATH_TRAF_C, Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF domain, C-terminal MATH subdomain; TRAF molecules serve as adapter proteins that link cell surface TNFRs and receptors of the interleukin-1/Toll-like family to downstream kinase signaling cascades which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. There are at least six mammalian and three Drosophila proteins containing TRAF domains. The mammalian TRAFs display varying expression profiles, indicating independent and cell type-specific regulation. They display distinct, as well as overlapping functions and interactions with receptors. Most TRAFs, except TRAF1, share N-terminal homology and contain a RING domain, multiple zinc finger domains, and a TRAF domain. TRAFs form homo- and heterotrimers through its TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors
GVLIWKIKDYSRKLQEAVAGSNTVLYSPPFYTSRYGYKLCLRLYLNGDGTGKGTHLSLFVHVMKGEYDAL
LEWPFRGKITLTLLDQSDDSKRKHITETFMPDPNSSAFQRPPTGENNIGFGYPEFVPLEKLESRGYVKDD
TLFIKVEVD
>gnl|CDD|238169 cd00271, Chemokine_C, Chemokine_C, C or lymphotactin subgroup, 1 of 4 subgroup designations of chemokines based on the arrangement of two N-terminal, conserved cysteine residues. Most of the known chemokines (cd00169) belong to either the CC (cd00272) or CXC (cd00273) subclass. The two other subclasses each have a single known member: fractalkine for the CX3C (cd00274) class and lymphotactin for the C (cd00271) class. Chemokine_Cs differ structurally since they contain only one of the two disulfide bridges that are conserved in all other chemokines and they possess a unique C-terminal extension, which is required for biological activity and thought to play a role in receptor binding. Lymphotactin, a mediator of mucosal immunity, has been found to chemoattract neutrophils and B cells through the XCR1 receptor and thought to be a factor in acute allograft rejection and inflammatory bowel disease
VGSEVLEKSSCVSLTTQRLPVQKIKTYTIKEGSVRAVIFITKRGLKICADPQAKWVKSAVKTIDRRASTR
KN
>gnl|CDD|238170 cd00272, Chemokine_CC, Chemokine_CC: 1 of 4 subgroup designations based on the arrangement of the two N-terminal cysteine residues; includes a number of secreted growth factors and interferons involved in mitogenic, chemotactic, and inflammatory activity; some members (e.g. 2HCC) contain an additional disulfide bond which is thought to compensate for the highly conserved Trp missing in these; chemotatic for monocytes, macrophages, eosinophils, basophils, and T cells, but not neutrophils; exist as monomers and dimers, but are believed to be functional as monomers; found only in vertebrates and a few viruses; a subgroup of CC, identified by an N-terminal DCCL motif (Exodus-1, Exodus-2, and Exodus-3), has been shown to inhibit specific types of human cancer cell growth in a mouse model. See CDs: Chemokine (cd00169) for the general alignment of chemokines, or Chemokine_CXC (cd00273), Chemokine_C (cd00271), and Chemokine_CX3C (cd00274) for the additional chemokine subgroups, and Chemokine_CC_DCCL for the DCCL subgroup of this CD
CCLSYSKKRIPLRVLKSYRRTSSSCSKPAVIFKTKRGREVCADPKQKWVQRYMKLLD
>gnl|CDD|238171 cd00273, Chemokine_CXC, Chemokine_CXC: 1 of 4 subgroup designations based on the arrangement of the two N-terminal cysteine residues; includes a number of secreted growth factors and interferons involved in mitogenic, chemotactic, and inflammatory activity; many members contain an RCxC motif which may be a general requirement for binding to CXC chemokine receptors; those with the ELR motif are chemotatic for neutrophils and have been shown to be angiogenic, while those without the motif act on T and B cells, and are typically angiostatic; exist as monomers and dimers, but are believed to be functional as monomers; found only in vertebrates and a few viruses. See CDs: Chemokine (cd00169) for the general alignment of chemokines, or Chemokine_CC (cd00272), Chemokine_C (cd00271), and Chemokine_CX3C (cd00274) for the additional chemokine subgroups
ELRCRCIKTTSGFVHPKSIKKLEVIPPGPHCPNTEIIATLKNGRKVCLNPEAPWVQKIIKKLLK
>gnl|CDD|238172 cd00274, Chemokine_CX3C, Chemokine_CX3C: 1 of 4 subgroup designations based on the arrangement of the two N-terminal cysteines; differ structurally from the other subgroups in that they are attached to a membrane-spanning domain via a mucin-like stalk and can be proteolytically cleaved to a freely diffusible form; chemotatic for T cells, monocytes, and natural killer cells; function as monomers and are found only in vertebrates and a few viruses; currently only fractalkine (sometimes called neurotactin) has been identified as a member of this subfamily; the primary source of fractalkine is neurons, and they exhibit cell adhesion and chemoattractive properties in the central nervous system. See CDs: Chemokine (cd00169) for the general alignment of chemokines, or Chemokine_CXC (cd00273), Chemokine_CC (cd00272), and Chemokine_C (cd00271) for the additional chemokine subgroups
QHHGVTKCNITCSKMTSKIPVALLIHYQQNQESCGKRAIILETRQHRLFCADPKEQWVKDAMQHLDRQAA
ALTRNG
>gnl|CDD|175974 cd00275, C2_PLC_like, C2 domain present in Phosphoinositide-specific phospholipases C (PLC). PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology
PLTLTIKIISGQQLPKPKGDKGSIVDPYVEVEIHGLPADDSAKFKTKVVKNNGFNPVWNETFEFDVTVPE
LAFLRFVVYDEDSGDDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT
>gnl|CDD|175975 cd00276, C2B_Synaptotagmin, C2 domain second repeat present in Synaptotagmin. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
GELLLSLSYLPTAERLTVVVLKARNLPPSDGKGLSDPYVKVSLLQGGKKLKKKKTSVKKGTLNPVFNEAF
SFDVPAEQLEEVSLVITVVDKDSVGRNEVIGQVVLGPDSGGEELEHWNEMLASPRKPIARWHKL
>gnl|CDD|238173 cd00279, YlxR, Ylxr homologs; group of conserved hypothetical bacterial proteins of unknown function; structure revealed putative RNA binding cleft; proteins are encoded by an operon that includes other proteins involved in transcription and/or translation
PLRKCIVTGEMKPKKELIRFVAGPEGEVVPDPTGKLPGRGAYVCADRECIEKAKKKKLFNRAFKAKVSDS
VYDELIEYV
>gnl|CDD|238174 cd00280, TRFH, Telomeric Repeat binding Factor or TTAGGG Repeat binding Factor, central (dimerization) domain Homology; TRFH. Telomeres are protein/DNA complexes that make up the physical ends of eukaryotic linear chromosomes and are essential for chromosome stability, protecting the chromosome ends from degradation and end-to-end fusion. Proteins TRF1, TRF2 and Taz1 bind telomeric DNA and are also involved in recruiting interacting proteins, TIN2, and Rap1, to the telomeres. It has also been demonstrated that PARP1 associates with TRF2 and is capable of poly(ADP-ribosyl)ation of TRF2, which affects binding of TRF2 to telomeric DNA. TRF1, TRF2 and Taz1 proteins contain three functional domains: an N-terminal acidic domain, a central TRF-specific/dimerization domain, and a C-terminal DNA binding domain with a single Myb-like repeat. Homodimerization, a prerequisite to DNA binding, results in the juxtaposition of two Myb DNA binding domains
EADAEAVANRWVLDFYFHSACRAFREGRYEDFRRTRDIAEALLVGPLKLTATQLKTLRIMQFLSRIAEGK
NLDCQFENDEELTPLESALMVLESIEKEFSLPETLHEEIRKLIKEQAVAVCMENGEFKKAEEVLKRLFSD
PESQKLRMKLLMIIREKDPAHPVLQNFSYSHFMQKMKSYVELVLDEKESPFLLKAAAKVV
>gnl|CDD|176449 cd00281, DAP_dppA, Peptidase M55, D-aminopeptidase dipeptide-binding protein family. M55 Peptidase, D-Aminopeptidase dipeptide-binding protein (dppA; DAP dppA; EC 3.4.11.-) domain: Peptide transport systems are found in many bacterial species and generally function to accumulate intact peptides in the cell, where they are hydrolyzed. The dipeptide-binding protein (dppA) of Bacillus subtilis belongs to the dipeptide ABC transport (dpp) operon expressed early during sporulation. It is a binuclear zinc-dependent, D-specific aminopeptidase. The biologically active enzyme is a homodecamer with active sites buried in its channel. These self-compartmentalizing proteases are characterized by a SXDXEG motif. D-Ala-D-Ala and D-Ala-Gly-Gly are the preferred substrates. Bacillus subtilis dppA is thought to function as an adaptation to nutrient deficiency; hydrolysis of its substrate releases D-Ala which can be used subsequently as metabolic fuel. This family also contains a number of uncharacterized putative peptidases
MKVYISADIEGIAGISHWDEATIGQPGYEAFREQMTEAVIAACEGSLAAGATQVLVKDSHDSGRNLIPER
LPEPVQLISGSGHPYCMVQGLDRSFDALLFIGYHARAGTAANVMAHSYTTEVSQIRINGQAIAEFHLNAL
TAGYYGVPVVMVAGDAEVCKEAKAYDAQVETVVTKKGMGRFSVKAPSPQKVLRAIREGTEGSLQRLPRKR
KLPDHFTPVQLEVEFKDPARAYRKSFYPGCEWIAGSTVRLEVSDWFEVLRALLFM
>gnl|CDD|238175 cd00283, GIY-YIG_Cterm, GIYX(10-11)YIG family of class I homing endonucleases C-terminus (GIY-YIG_Cterm). Homing endonucleases promote the mobility of intron or intein by recognizing and cleaving a homologous allele that lacks the sequence. They catalyze a double-strand break in the DNA near the insertion site of that element to facilitate homing at that site. Class I homing endonucleases are sorted into four families based on the presence of these motifs in their respective N-termini: LAGLIDADG, His-Cys box, HNH, and GIY-YIG. This CD contains several but not all members of the GIY-YIG family. The C-terminus of GIY-YIG is a DNA-binding domain which is separated from the N-terminus by a long, flexible linker. The DNA-binding domain consists of a minor-groove binding alpha-helix, and a helix-turn-helix. Some also contain a zinc finger (i.e. I-TevI) which is not required for DNA binding or catalysis, but is a component of the linker and directs the catalytic domain to cleave the homing site at a fixed distance from the intron insertion site
KAKNKMSASYSGEKNPMFGKTHSEETKAKISKNRSGENNPMFGKKHSDETKAKISAKKKGRKNLNAKKKQ
SDTDGYIGIFDSTTEAARFLKVHSGTISKNIKSGKLLYKFYFI
>gnl|CDD|238176 cd00284, Cytochrome_b_N, Cytochrome b (N-terminus)/b6/petB: Cytochrome b is a subunit of cytochrome bc1, an 11-subunit mitochondrial respiratory enzyme. Cytochrome b spans the mitochondrial membrane with 8 transmembrane helices (A-H) in eukaryotes. In plants and cyanobacteria, cytochrome b6 is analogous to eukaryote cytochrome b, containing two chains: helices A-D are encoded by the petB gene and helices E-H are encoded by the petD gene in these organisms. Cytochrome b/b6 contains two bound hemes and two ubiquinol/ubiquinone binding sites. The C-terminal portion of cytochrome b is described in a separate CD
PKLIEVNNSLIDLPPPSNISYWWNFGSLLGTCLVIQILTGVFLAMHYTPDVTLAFSSVQYIMRDVNFGWL
IRSLHANGASMFFLMLYLHIFRGLYYGSYKKPRELTWVIGVILLLLTMATAFMGYVLPWGQMSYWGATVI
TNLFSAIPVIGITLVEWLWGGFSVDNATLTRFFALHFLLPFIIAVIVILHLLFLHEQGSS
>gnl|CDD|276954 cd00286, Tubulin_FtsZ_Cetz-like, Tubulin protein family of FtsZ and CetZ-like. This family includes tubulin alpha-, beta-, gamma-, delta-, epsilon, and zeta-tubulins as well as FtsZ and CetZ, all of which are involved in polymer formation. Tubulin is the major component of microtubules, but also exists as a heterodimer and as a curved oligomer. Microtubules exist in all eukaryotic cells and are responsible for many functions, including cellular transport, cell motility, and mitosis. FtsZ forms a ring-shaped septum at the site of bacterial cell division, which is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria, archaea, and chloroplasts. A recent study found that CetZ proteins, formerly annotated FtsZ type 2, are not required for cell division, whereas FtsZ proteins play an important role. Instead, CetZ proteins are shown to be involved in controlling archaeal cell shape dynamics. The results from inactivation studies of CetZ proteins in Haloferax volcanii suggest that CetZ1 is essential for normal swimming motility and rod-cell development
EIVTIQVGQCGNQIGAAFWEQAVLVDLEPAVLDELLSGPLRQLFHPENIILIQKYHGAGNNWAKGHSVAG
EEYQEEILDAIRKEVEECDELQGFFITHSLGGGTGSGLGPLLAERLKDEYPNRLVVTFSILPGPDEGVIV
YPYNAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTEALRFEGSLNVDL
RELAENLVPLPRGHFLMLGYAPLDSATSATPRSLRVKELTRRAFLPANLLVGCDPDHGEAIAALLVIRGP
PDLSSKEVERAIARVKETLGHLFSWSPAGVKTGISPKPPAEGEVSVLALLNS
>gnl|CDD|238177 cd00287, ribokinase_pfkB_like, ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase)
RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVGADAVVISGLSPAP
EAVLDALEEARRRGVPVVLDPGPRAVRLDGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAAL
LLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA
>gnl|CDD|238178 cd00288, Pyruvate_Kinase, Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low affinity T state. PK exists as several different isozymes, depending on organism and tissue type. In mammals, there are four PK isozymes: R, found in red blood cells, L, found in liver, M1, found in skeletal muscle, and M2, found in kidney, adipose tissue, and lung. PK forms a homotetramer, with each subunit containing three domains. The T state to R state transition of PK is more complex than in most allosteric enzymes, involving a concerted rotation of all 3 domains of each monomer in the homotetramer
LRRTKIVCTIGPATDSVENLKKLIKAGMNVARMNFSHGSHEYHQSRIDNVREAAEKTGGPVAIALDTKGP
EIRTGLFKGGKDISLKAGDKFLVTTDPAAKKGTKEKIYVDYKNLTKDVSPGNTILVDDGLLSLKVLSKDD
DKTLVCEVLNGGVLGSRKGVNLPGTDVDLPALSEKDKADLRFGVEQGVDMIFASFVRKASDVLEIREVLG
EKGKDIKIIAKIENQEGVNNFDEILEASDGIMVARGDLGVEIPAEEVFLAQKMLIAKCNLAGKPVITATQ
MLESMIYNPRPTRAEVSDVANAVLDGTDCVMLSGETAKGKYPVEAVKAMARICLEAEKALSHRVLFNEMR
RLTPRPTSTTEAVAMSAVRAAFELGAKAIVVLTTSGRTARLVSKYRPNAPIIAVTRNEQTARQLHLYRGV
YPVLFEEPKPGWQEDTDARLKAAVNVAKEKGLLKKGDLVVVVQGWPVGSGSTNTMRILTV
>gnl|CDD|238179 cd00290, cytochrome_b_C, Cytochrome b(C-terminus)/b6/petD: Cytochrome b is a subunit of cytochrome bc1, an 11-subunit mitochondrial respiratory enzyme. Cytochrome b spans the mitochondrial membrane with 8 transmembrane helices (A-H) in eukaryotes. In plants and cyanobacteria, cytochrome b6 is analogous to eukaryote cytochrome b, containing two chains: helices A-D are encoded by the petB gene and helices E-H are encoded by the petD gene in these organisms. Cytochrome b/b6 contains two bound hemes and two ubiquinol/ubiquinone binding sites. The C-terminal domain is involved in forming the ubiquinol/ubiquinone binding sites, but not the heme binding sites. The N-terminal portion of cytochrome b, which contains both heme binding sites, is described in a separate CD
NPLGLASDMDKISFHPYFWPKDLLGAFPILIIFMILVFYAPNLLGHPDNGIPANPLATPLHILPEWYFLP
VYAILRAIPNKLLGVLAMAASILSLFLVPFLENSNKRSQFRPLRPTAFWVFLAGTLVLGWLGIQPVEYPF
SLILQLF
>gnl|CDD|238180 cd00291, SirA_YedF_YeeD, SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and YhhP) belongs to a family of bacterial two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding
TLDLRGLPCPLPVLKTKKALEKLKSGEVLEVLLDDPGAVEDIPAWAKETGHEVLEVEEEGGVYRILIRK
>gnl|CDD|238181 cd00292, EF1B, Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the exchange of GDP bound to the G-protein, EF1A, for GTP, an important step in the elongation cycle of the protein biosynthesis. EF1A binds to and delivers the aminoacyl tRNA to the ribosome. The guanine nucleotide exchange domain of EF1B, which is the alpha subunit in yeast, is responsible for the catalysis of this exchange reaction
MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEA
ISEEDGVQSVDVEAFNKL
>gnl|CDD|467483 cd00293, USP-like, universal stress protein (USP) and similar proteins. The universal stress protein (USP) is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. USP enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae Usp reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, although USP lacks ATP-binding activity
KILVAVDGSEESERALEWALELAKRPGAELTLLHVVDPPPSSSLSGGLEELADELKEEAEELLEEAKKLA
EEAGVEVETIVVEGDPAEAILEEAKELGADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVLVV
>gnl|CDD|238183 cd00295, RNA_Cyclase, RNA 3' phosphate cyclase domain - RNA phosphate cyclases are enzymes that catalyze the ATP-dependent conversion of 3'-phosphate at the end of RNA into 2', 3'-cyclic phosphodiester bond. The enzymes are conserved in eucaryotes, bacteria and archaea. The exact biological role of this enzyme is unknown, but it has been proposed that it is likely to function in cellular RNA metabolism and processing. RNA phosphate cyclase has been characterized in human (with at least three isozymes), and E. coli, and it seems to be taxonomically widespread. The crystal structure of RNA phospate cyclase shows that it consists of two domains. The larger domain contains three repeats of a fold originally identified in the bacterial translation initiation factor IF3
LDGAKGEGGCEILRHALSLAMISGQPFRIEGIRADEADPGLKDQHLSALKAAEEICGASVEEAELGGQRF
IFRPGNIIGGDVRFACGSAGGCGLFLEPILIACLFADGPSRLELSGGTDNNEAIGADFIRRSLEPLLAKI
FIHGDELELRHGFRGAAGGGGAEENFLCASFKELLLGERGSEFGRQFRGEGIAAGTRVPPAFAEREIASA
AGSFNLFEPDIFILPDDQRGDECGNGPGNSISLEAESEKGCSEAAEHCGEAGESAEDVAAFCAKELKEVI
ASGAAVDEYLADQLLLGMALAGEAGEFIVAGPLCHLLQLTNFARDVEAFFNCEFRFIE
>gnl|CDD|238184 cd00296, SIR2, SIR2 superfamily of proteins includes silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose. Sir2 proteins, also known as sirtuins, are found in all eukaryotes and many archaea and prokaryotes and have been shown to regulate gene silencing, DNA repair, metabolic enzymes, and life span. The most-studied function, gene silencing, involves the inactivation of chromosome domains containing key regulatory genes by packaging them into a specialized chromatin structure that is inaccessible to DNA-binding proteins. The oligomerization state of Sir2 appears to be organism-dependent, sometimes occurring as a monomer and sometimes as a multimer. Also included in this superfamily is a group of uncharacterized Sir2-like proteins which lack certain key catalytic residues and conserved zinc binding cysteines
KRVVVFTGAGISTESGIPDFRGLGTGLWTRLDPEELAFSPEAFRRDPELFWLFYKERRYTPLDAKPNPAH
RALAELERKGKLKRIITQNVDGLHERAGSRRNRVIELHGSLDRVRCTSCGKEYPRDEVLEREKPPRCPKC
GGLLRPDVVDFGEALPKEWFDRALEALLEADLVLVIGTSLTVYPAARLLLRAPERGAPVVIINREPTPAD
ALKKADLVILGD
>gnl|CDD|107219 cd00298, ACD_sHsps_p23-like, This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small heat shock proteins (sHsps) and a similar domain found in p23-like proteins. sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is this ACD. sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps. p23 is a cochaperone of the Hsp90 chaperoning pathway. It binds Hsp90 and participates in the folding of a number of Hsp90 clients including the progesterone receptor. p23 also has a passive chaperoning activity. p23 in addition may act as the cytosolic prostaglandin E2 synthase. Included in this family is the p23-like C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1) and the p23-like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR)
WYQTDDEVVVTVDLPGVKKEDIKVEVEDNVLTISGKREEEEERERSYGEFERSFELPEDVDPEKSKASLE
NGVLEITLPK
>gnl|CDD|198286 cd00299, GST_C_family, C-terminal, alpha helical domain of the Glutathione S-transferase family. Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases
VRALEDWADATLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVAL
APVLARLEALGPYYDLLDEYPRLKAWYDRL
>gnl|CDD|133418 cd00300, LDH_like, L-lactate dehydrogenase-like enzymes. Members of this subfamily are tetrameric NAD-dependent 2-hydroxycarboxylate dehydrogenases including LDHs, L-2-hydroxyisocaproate dehydrogenases (L-HicDH), and LDH-like malate dehydrogenases (MDH). Dehydrogenases catalyze the conversion of carbonyl compounds to alcohols or amino acids. LDHs catalyze the last step of glycolysis in which pyruvate is converted to L-lactate. Vertebrate LDHs are non-allosteric, but some bacterial LDHs are activated by an allosteric effector such as fructose-1,6-bisphosphate. L-HicDH catalyzes the conversion of a variety of 2-oxo carboxylic acids with medium-sized aliphatic or aromatic side chains. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like subfamily is part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
ITIIGAGNVGAAVAFALIAKGLASELVLVDVNEEKAKGDALDLSHASAFLATGTIVRGGDYADAADADIV
VITAGAPRKPGETRLDLINRNAPILRSVITNLKKYGPDAIILVVSNPVDILTYVAQKLSGLPKNRVIGSG
TLLDSARFRSLLAEKLDVDPQSVHAYVLGEHGDSQVVAWSTATVGGLPLEELAPFTKLDLEAIEEEVRTS
GYEIIRLKGATNYGIATAIADIVKSILLDERRVLPVSAVQEGQYGIEDVALSVPAVVGREGVVRILEIPL
TEDEEAKLQKSAEALKEVLN
>gnl|CDD|381182 cd00301, lipocalin_FABP, lipocalin/cytosolic fatty acid-binding protein family. Lipocalins are diverse, mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules as well as membrane bound-receptors. They have a large beta-barrel ligand-binding cavity. Members include retinol-binding protein, retinoic acid-binding protein, complement protein C8 gamma, Can f 2, apolipoprotein D, extracellular fatty acid-binding protein, beta-lactoglobulin, oderant-binding protein, and bacterial lipocalin Blc. Lipocalins are involved in many important processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty acid-binding proteins also bind hydrophobic ligands in a non-covalent, reversible manner, and are involved in protection and shuttling of fatty acids within the cell, and in acquisition and removal of fatty acids from intracellular sites
KFSGKWYEVASASNAPEEDEGKCTTAEYTLEGNGNLKVTNSFVRDGVCKSITGTLKKTDGPGKFTVTYPG
YTGKNELYVLSTDYDNYAIVYSCKNLDGGHTVVAWLLSR
>gnl|CDD|410651 cd00302, cytochrome_P450, cytochrome P450 (CYP) superfamily. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs with _ 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis
GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAF
TPRALAALRPVIREIARELLDRLAAGGEVGDDVADLAQPLALDVIARLLGGPDLGEDLEELAELLEALLK
LLGPRLLRPLPSPRLRRLRRARARLRDYLEELIARRRAEPADDLDLLLLADADDGGGLSDEEIVAELLTL
LLAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDGTPEDLSKLPYLEAVVEETLRLYPPVPLLPR
VATEDVELGGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREEPRYAHLPFGAGPHRCLGARL
ARLELKLALATLLRRFDFELVPDEELEWRPSLGTLGPASLP
>gnl|CDD|133136 cd00303, retropepsin_like, Retropepsins; pepsin-like aspartate proteases. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A
LKGKINGVPVRALVDSGASVNFISESLAKKLGLPPRLLPTPLKVKGANGSSVKTLGVILPVTIGIGGKTF
TVDFYVLDLLSYDVILGRPWLE
>gnl|CDD|238185 cd00304, RT_like, RT_like: Reverse transcriptase (RT, RNA-dependent DNA polymerase)_like family. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses. These elements can be divided into two major groups. One group contains retroviruses and DNA viruses whose propagation involves an RNA intermediate. They are grouped together with transposable elements containing long terminal repeats (LTRs). The other group, also called poly(A)-type retrotransposons, contain fungal mitochondrial introns and transposable elements that lack LTRs
FDVKSFFTSIPLPQGSPLSPALANLYMEKLEAPILKQLLDITLIRYVDDLVVIAKSEQQAVKKRELEEFL
ARLGLNLSDEKTQFTEKEKKFKFLGILV
>gnl|CDD|238186 cd00305, Cu-Zn_Superoxide_Dismutase, Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene causes familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Cytoplasmic and periplasmic SODs exist as dimers, whereas chloroplastic and extracellular enzymes exist as tetramers. Structure supports independent functional evolution in prokaryotes (P-class) and eukaryotes (E-class) [PMID:8176730]
VSAVAVLKGPDGKVVGTVTFTQQSGGVTITGELSGLTPGLHGFHIHEFGDCTNGCTSAGGHFNPFGKKHG
GPNDEGRHAGDLGNIVADKDGVATVSVLDPLISLKGGNSIIGRSLVVHAGQDDLGKGPDELSGGTGNAGV
RVAC
>gnl|CDD|173787 cd00306, Peptidases_S8_S53, Peptidase domain in the S8 and S53 families. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values
VTVAVIDTGVDPDHPDLDGLFGGGDGGNDDDDNENGPTDPDDGNGHGTHVAGIIAASANNGGGVGVAPGA
KLIPVKVLDGDGSGSSSDIAAAIDYAAADQGADVINLSLGGPGSPPSSALSEAIDYALAKLGVLVVAAAG
NDGPDGGTNIGYPAASPNVIAVGAVDRDGTPASPSSNGGAGVDIAAPGGDILSSPTTGGGGYATLSGTSM
AAPIVAGVAALLLSANPDLTPAQVKAALLST
>gnl|CDD|238187 cd00307, RuBisCO_small_like, Ribulose bisphosphate carboxylase/oxygenase (Rubisco), small subunit and related proteins. Rubisco is a bifunctional enzyme catalyzes the initial steps of two opposing metabolic pathways: photosynthetic carbon fixation and the competing process of photorespiration. Rubisco Form I, present in plants and green algae, is composed of eight large and eight small subunits. The nearly identical small subunits are encoded by a family of nuclear genes. After translation, the small subunits are translocated across the chloroplast membrane, where an N-terminal signal peptide is cleaved off. While the large subunits contain the catalytic activities, it has been shown that the small subunits are important for catalysis by enhancing the catalytic rate through inducing conformational changes in the large subunits. This superfamily also contains specific proteins from cyanobacteria. CcmM plays a role in a CO2 concentrating mechanism, which cyanobacteria need to to overcome the low specificity of their Rubisco and fusions to Rubisco activase, a type of chaperone, which promotes and maintains the catalytic activity of Rubisco. CcmM contains an N-terminal carbonic anhydrase fused to four copies of the Rubisco-small subunit domain
SEDVVEQVRQLLAQGYKIGLEHADARRFRTSSWQSCGPIEGRSEAQVLAALEACLAEHPGEYVRLIGIDP
KAKRRVLEIIIQRP
>gnl|CDD|238188 cd00308, enolase_like, Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase
VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGEVISGIDMALWDLAAKALGVPLAELLGGG
SRDRVPAYGSIERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAAL
RRRTGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIG
TAAALHLAAALPNDRAIET
>gnl|CDD|238189 cd00309, chaperonin_type_I_II, chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis
KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEV
AKSQDDEVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELL
KVATTSLNSKLVSGGDDFLGELVVDAVLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSP
YMPKRLENAKILLLDCKLEYVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDL
TPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVP
GGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGG
DVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV
>gnl|CDD|349411 cd00310, ATP-synt_Fo_a_6, ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes). Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis
GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTP
LPLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVA
FIQAYVFTLLTAVYIS
>gnl|CDD|238190 cd00311, TIM, Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. The reaction is very efficient and requires neither cofactors nor metal ions. TIM, usually homodimeric, but in some organisms tetrameric, is ubiqitous and conserved in function across eukaryotes, bacteria and archaea
PLVAGNWKMNGTLAEALELAKALNAVLKDESGVEVVVAPPFTYLAAVAEALEGSKIKVGAQNVSPEDSGA
FTGEISAEMLKDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVV
AAQLAAVLAGVEDLAPVVIAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGEVAEKVRILYGGSVNP
ENAAELLAQPDIDGVLVGGASLKAESFLDIIK
>gnl|CDD|238191 cd00312, Esterase_lipase, Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate
LVVTPNGKVRGVDEGGVYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQWDQLGGGLWNA
KLPGSEDCLYLNVYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGDGLAREGDNVIVVSINYRLGVLGF
LSTGDIELPGNYGLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQS
GSALSPWAIQENARGRAKRLARLLGCNDTSSAELLDCLRSKSAEELLDATRKLLLFSYSPFLPFGPVVDG
DFIPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAAMLLNFDAKLIIETNDRWLELLPYLLFYADDALADK
VLEKYPGDVDDSVESRKNLSDMLTDLLFKCPARYFLAQHRKAGGSPVYAYVFDHRSSLSVGRWPPWLGTV
HGDEIFFVFGNPLLKEGLREEEEKLSRTMMKYWANFAKTGNPNTEGNLVVWPAYTSESEKYLDINIEGTE
IKQ
>gnl|CDD|349412 cd00313, ATP-synt_Fo_Vo_Ao_c, ATP synthase, membrane-bound Fo/Vo/Ao complexes, subunit c. Subunit c of the Fo/Vo/Ao complex is the main transmembrane subunit of F-, V- or A-type family of ATP synthases with rotary motors. These ion-transporting rotary ATP synthases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contains three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao (oligomycin sensitive) complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthase (AoA1-ATPases) is exclusively found in archaea and function like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes
ALGAGLAIGLAAIGAGIGIGLAGAAALEAIARQPEAAGKIFTTMLIGLALIESLAIYGLVIAFLL
>gnl|CDD|173823 cd00314, plant_peroxidase_like, Heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase
DAIKAILEDLITQAGALAGSLLRLAFHDAGTYDIADGKGGGADGSIRFEPELDRPENGGLDKALRALEPI
KSAYDGGNPVSRADLIALAGAVAVESTFGGGPLIPFRFGRLDATEPDLGVPDPEGLLPNETSSATELRDK
FKRMGLSPSELVALSAGAHTLGGKNHGDLLNYEGSGLWTSTPFTFDNAYFKNLLDMNWEWRVGSPDPDGV
KGPGLLPSDYALLSDSETRALVERYASDQEKFFEDFAKAWIKMVN
>gnl|CDD|238192 cd00315, Cyt_C5_DNA_methylase, Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many aspects of biology. Cytosine-specific DNA methylases are found both in prokaryotes and eukaryotes. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the mammalian genome. These effects include transcriptional repression via inhibition of transcription factor binding or the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability
LRVIDLFAGIGGFRLGLEKAGFEIVAANEIDKSAAETYEANFPNKLIEGDITKIDEKDFIPDIDLLTGGF
PCQPFSIAGKRKGFEDTRGTLFFEIIRILKEKKPKYFLLENVKGLLTHDNGNTLKVILNTLEELGYNVYW
KLLNASDYGVPQNRERVFIIGIRKDLILNFFSPFPKPSEKKKTLKDILRIRDPDEPSPTLTASYGKGTGS
VHPTAPDMIGKESNIRRLTPRECARLQGFPDDFEFPGKSVTQAYRQIGNSVPVPVAEAIAKAIKE
>gnl|CDD|238193 cd00316, Oxidoreductase_nitrogenase, The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. This group contains both alpha and beta subunits of component 1 of the three known genetically distinct types of nitrogenase systems: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium-dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase) and, both subunits of Protochlorophyllide (Pchlide) reductase and chlorophyllide (chlide) reductase. The nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). The most widespread and best characterized nitrogenase is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers whose alpha and beta subunits are similar to the alpha and beta subunits of MoFe. For MoFe, each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains a single [4Fe-4S] cluster from which, electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo at the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. Pchlide reductase and chlide reductase participate in the Mg-branch of the tetrapyrrole biosynthetic pathway. Pchlide reductase catalyzes the reduction of the D-ring of Pchlide during the synthesis of chlorophylls (Chl) and bacteriochlorophylls (BChl). Chlide-a reductase catalyzes the reduction of the B-ring of Chlide-a during the synthesis of BChl-a. The Pchlide reductase NB complex is a an N2B2 heterotetramer resembling nitrogenase FeMo, N and B proteins are homologous to the FeMo alpha and beta subunits respectively. The NB complex may serve as a catalytic site for Pchlide reduction and, the ZY complex as a site of chlide reduction, similar to MoFe for nitrogen reduction
INPAKGCAPLGAARVALGIKDAIPLVHGPQGCAYFTRLTLRRHFKEPIPLFTTSMTEKDVVFGGGEKLLE
AIINELKRYKPKVIFVYTTCTTELIGDDIEAVAKEASKEIGIPVVPASTPGFRGSQSAGYDAAVKAIIDH
LVGTAEPEETEPGSVNLIGGYNLGGGDLRELKRLLEEMGIRVNALFDGGTTVEELRELGNAKLNLVLCRE
SGLYLARYLEEKYGIPYILINPIGLEATDAFLRKLAELFGIEKEVPEVIARERARLLDALADYHEYLGGK
KVAIFGDGDLLLALARFLLELGMEVVAAGTTFGHKADYERREELLGEGTEVVDDGDLEELEELIRELKPD
LIIGGSKGRYIAKKLGIPLVRIGFPIHRRPYVGYEGALNLAEEIANALL
>gnl|CDD|238194 cd00317, cyclophilin, cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing
TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGGSGPGYKFPDE
NFPLKYHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIK
PVTISD
>gnl|CDD|238195 cd00318, Phosphoglycerate_kinase, Phosphoglycerate kinase (PGK) is a monomeric enzyme which catalyzes the transfer of the high-energy phosphate group of 1,3-bisphosphoglycerate to ADP, forming ATP and 3-phosphoglycerate. This reaction represents the first of the two substrate-level phosphorylation events in the glycolytic pathway. Substrate-level phosphorylation is defined as production of ATP by a process, which is catalyzed by water-soluble enzymes in the cytosol; not involving membranes and ion gradients
IDDLDLKGKRVLVRVDFNVPVDDGKITDDTRIRAALPTIKYLLEQGAKVVLLSHLGRPKGEPNEKYSLAP
VAKALSELLGQPVTFANDCVGPEAEEAVEALKPGDVLLLENVRFYPEEEGKRDDDKEADEEFAKKLASLG
DVYVNDAFGTAHRAHASMVGIALLLPSAAGFLMEKELKYLAKALENPERPFVAILGGAKVSDKIQVIENL
LDKVDYLIIGGGMAFTFLKAQGMDIGKSLFEEDGIELAKSLLEKAKAKGVKIVLPVDVVVADKFKADANT
KVVTDDGIPDGWMGLDIGPKTIELFAEVIRKAKTIVWNGPMGVFEFPAFAKGTKAIADAIAAATKAGAFS
IIGGGDTAAAAEKFGLADKISHVSTGGGASLELLEGKELPGVAALEE
>gnl|CDD|238196 cd00319, Ribosomal_S12_like, Ribosomal protein S12-like family; composed of prokaryotic 30S ribosomal protein S12, eukaryotic 40S ribosomal protein S23 and similar proteins. S12 and S23 are located at the interface of the large and small ribosomal subunits, adjacent to the decoding center. They play an important role in translocation during the peptide elongation step of protein synthesis. They are also involved in important RNA and protein interactions. Ribosomal protein S12 is essential for maintenance of a pretranslocation state and, together with S13, functions as a control element for the rRNA- and tRNA-driven movements of translocation. S23 interacts with domain III of the eukaryotic elongation factor 2 (eEF2), which catalyzes translocation. Mutations in S12 and S23 have been found to affect translational accuracy. Antibiotics such as streptomycin may also bind S12/S23 and cause the ribosome to misread the genetic code
RKKSKVPALKGAPFRRGVCTVVRTVTPKKPNSALRKVAKVRLTSGYEVTAYIPGEGHNLQEHSVVLIRGG
RVKDLPGVRYHIVRGVYDAAGVKDR
>gnl|CDD|238197 cd00320, cpn10, Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL), an ATPase, to assist the folding and assembly of proteins and is found in eubacterial cytosol, as well as in the matrix of mitochondria and chloroplasts. It forms heptameric rings with a dome-like structure, forming a lid to the large cavity of the tetradecameric cpn60 cylinder and thereby tightly regulating release and binding of proteins to the cpn60 surface
KIKPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRNENGERVPLSVKVGDKVLFPKYA
GTEVKLDGEEYLILRESDILAVI
>gnl|CDD|238198 cd00321, SO_family_Moco, Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Assimilatory NRs catalyze the reduction of nitrate to nitrite which is subsequently converted to NH4+ by nitrite reductase. Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate
FVRNHGGVPPEIDPDDWRLEVDGLVEKPLSLTLDDLKALPQVEVIATLHCVGNRWGGGAVSNAEWTGVPL
RDLLEEAGPKPGARYVVFEGADDPGGDGYTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVVPGLY
GWKSVKWLRRIEVTDE
>gnl|CDD|99778 cd00322, FNR_like, Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H)
VATEDVTDDVRLFRLQLPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTVKIVPGGPFSA
WLHDLKPGDEVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADL
LFLDELEELAKEGPNFRLVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREAL
VSLGVPEERIHTE
>gnl|CDD|271245 cd00323, uS7, Ribosomal protein S7. uS7, also known as Ribosomal protein (RP)S7, is an important part of the translation process which is universally present in the small subunit of prokaryotic and eukaryotic ribosomes. The ribosome small subunit is one of the two subunits of ribosome organelles that use mRNA as a template for protein synthesis in a process called translation. The small subunits of bacteria and eukaryotes have the same shape of head, body, platform, beak, and shoulder. RPS7 is located at the head of the small subunit. RPS7 is a primary ribosomal RNA (rRNA) binding protein that assists in rRNA folding and the binding of other proteins during small subunit assembly in all species. RPS7 is also involved in the formation of the mRNA exit channel at the interface of the large and small subunits. Some ribosomal proteins have extra ribosomal functions in cell differentiation and apoptosis
KLLLKKFINILMKDGKKSKAEKIFSKALKILKKKTKKNPLKLLVEAIENIKPLVEVRSIKKRGKVYQVPV
PLSPNRQVSLAIKWLLKAVRKRKETSFAERLANEILDASNNKGASIKKKDDLHKLAEANR
>gnl|CDD|381595 cd00325, chitinase_GH19, Glycoside hydrolase family 19, chitinase domain. Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Glycoside hydrolase family 19 chitinases are found primarily in plants (classes I, III, and IV), but some are found in bacteria. Class I and II chitinases are similar in their catalytic domains. Class I chitinases have an N-terminal cysteine-rich, chitin-binding domain which is separated from the catalytic domain by a proline and glycine-rich hinge region. Class II chitinases lack both the chitin-binding domain and the hinge region. Class IV chitinases are similar to class I chitinases, but they are smaller in size due to certain deletions. Despite lacking any significant sequence homology with lysozymes, structural analysis reveals that family 19 chitinases, together with family 46 chitosanases, are similar to several lysozymes including those from T4-phage and from goose. The structures reveal that the different enzyme groups arose from a common ancestor glycohydrolase antecedent to the prokaryotic/eukaryotic divergence
VTEDLFNELFPHRNDPAKGFYTYDAFLAAAGSFPGFGNTGTDDIRKRELAAFLAHIAHETGGGWAAAGGP
YAWGLCYIEEIGCASDDCCSSSTGYPCAPGKSYYGRGPIQLSWNYNYGAASEALGGKDDLLNNPDLVATD
PTLAFKTAIWFWMTPQGPKPSCHDVILSADRAAGRGPGFGATINIINGGLECGGGNNAQVQNRIGYYKRF
CDILGVSPGDNLDC
>gnl|CDD|238200 cd00326, alpha_CA, Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues and a fourth conserved histidine plays a potential role in proton transfer
GKRQSPINIVTSAVVYDPSLPPLNFDYYPTTSLTLVNNGHTVQVNFDDDGGTLSGGGLPGRYKLVQFHFH
WGSENSPGSEHTIDGKRYPLELHLVHYNSDYYSSEAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKI
KYKGKETTLPPFDLSDLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDREGKP
LVNNYRPVQPLNGRVVY
>gnl|CDD|238201 cd00327, cond_enzymes, Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products
TGLGITASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACAT
GLTALALAVQQVQNGKADIVLAGGSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVP
AVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRSPAVSATLIMTGHPLGA
AGLAILDELLLMLEHEFIPPTPREPRTVLLLGFGLGGTNAAVVL
>gnl|CDD|163705 cd00328, catalase, Catalase heme-binding enzyme. Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Most catalases exist as tetramers of 65KD subunits containing a protoheme IX group buried deep inside the structure. In eukaryotic cells, catalases are located in peroxisomes
RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFY
TEEGNFDLVGNNTPIFFIRDAIKFPDFIHAQKPNPQTALPDADRFWDFLSLRPESLHQVSFLFSDRGIPA
AYRHMNGYGSHTFKLVNANGKVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSW
ELYIQVMTFNDAEKFPFNPLDPTKVWPEELVPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSE
DPLLQGRLFSYADTQLYRLGPNFQQLPVNRPYAPVHNNQRDGAGNMNDNTGVPNYEPNAKDVRYPAQGAP
KFDRGHFSHWKSGVNREASTTNDDNFTQARLFYRSLTPGQQKRLVDAFRFELADAVSPQIQQRVLDQFAK
VDAAAAKRVAKAL
>gnl|CDD|238202 cd00329, TopoII_MutL_Trans, MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the C-terminal domain of type II DNA topoisomerases (Topo II) and DNA mismatch repair (MutL/MLH1/PMS2) proteins. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. The GyrB dimerizes in response to ATP binding, and is homologous to the N-terminal half of eukaryotic Topo II and the ATPase fragment of MutL. Type II DNA topoisomerases catalyze the ATP-dependent transport of one DNA duplex through another, in the process generating transient double strand breaks via covalent attachments to both DNA strands at the 5' positions. Included in this group are proteins similar to human MLH1 and PMS2. MLH1 forms a heterodimer with PMS2 which functions in meiosis and in DNA mismatch repair (MMR). Cells lacking either hMLH1 or hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 accounts for a large fraction of Lynch syndrome (HNPCC) families
LKDRLAEILGDKVADKLIYVEGESDGFRVEGAISYPDSGRSSKDRQFSFVNGRPVREGGTHVKAVREAYT
RALNGDDVRRYPVAVLSLKIPPSLVDVNVHPTKEEVR
>gnl|CDD|153075 cd00330, phosphagen_kinases, Phosphagen (guanidino) kinases. Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK) or phosphoarginine in the case of arginine kinase, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CK exists in tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial and cytosolic) isoforms. They are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK and AK, the most studied members of this family are also other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK) and hypotaurocyamine kinase (HTK). The majority of bacterial phosphagen kinases appear to lack the N-terminal domain and have not been functionally characterized
VLSSRVRLGRSFEGIRFPPRYSNEEASSIEQQFEDQLSSQEIPLIGKYYLLRMMDPAEQQQLIDDHFLFP
NLTRFLQTANACREWPFGRGILHNDEKTFLVWVNEEDHLRIISMQKGGQLKEVMKRANTVDDWIEEKVDF
AFNEQRGYLTSCPTNLGTGLRASVHIHLPALVKTINRIIPAINQLGLQVRGTYGEGTEAVGGVFDISNQI
RLGKSEQDIVEDLNDGAAQLIEMERS
>gnl|CDD|238203 cd00331, IGPS, Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis
FKAALKRPGGLGVIAEVKRASPSKGLIREDFDPVEIAKAYEKAGAAAISVLTEPKYFQGSLEDLRAVREA
VSLPVLRKDFIIDPYQIYEARAAGADAVLLIVAALDDEQLKELYELARELGMEVLVEVHDEEELERALAL
GAKIIGINNRDLKTFEVDLNTTERLAPLIPKDVILVSESGISTPEDVKRLAEAGADAVLIGESLMRAPDP
GAALREL
>gnl|CDD|176460 cd00332, PAL-HAL, Phenylalanine ammonia-lyase (PAL) and histidine ammonia-lyase (HAL). PAL and HAL are members of the Lyase class I_like superfamily of enzymes that, catalyze similar beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. PAL, present in plants and fungi, catalyzes the conversion of L-phenylalanine to E-cinnamic acid. HAL, found in several bacteria and animals, catalyzes the conversion of L-histidine to E-urocanic acid. Both PAL and HAL contain the cofactor 3, 5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) which is formed by autocatalytic excision/cyclization of the internal tripeptide, Ala-Ser-Gly. PAL is being explored as enzyme substitution therapy for Phenylketonuria (PKU), a disorder which involves an inability to metabolize phenylalanine. HAL failure in humans results in the disease histidinemia
GSLTLEDVVAVARGGEKVELSPEARERVDASRAALEEAAAEGKPVYGVNTGFGALADVRIDDADLRALQR
NLLRSHAAGVGPPLPEEVVRAAMLLRLNSLARGHSGVRPEVLERLVALLNAGVTPVVPERGSVGASGDLA
PLAHIALALIGEGEVFYKGERMPAAEALARAGLEPLELGAKEGLALINGTAVMTALAALALHDAERLLDL
ADIAGALSLEALRGSDAPFDPRIHAARPHPGQIEVAANLRALLAGSSLWESHDGERRVQDPYSLRCAPQV
HGAARDALRYAARVLEIELNSVTDNPLVDPDNGEVLSGGNFHGQPVALAMDFLAIALAELANLSERRIAR
LVNPALSGLPAFLVADPGLNSGFMIAQYTAAALVAENKALAHPASVDSIPTSAGQEDHVSMGLIAARKLR
EIVDNLRRILAIELLAAAQALDLR
>gnl|CDD|238204 cd00333, MIP, Major intrinsic protein (MIP) superfamily. Members of the MIP superfamily function as membrane channels that selectively transport water, small neutral molecules, and ions out of and between cells. The channel proteins share a common fold: the N-terminal cytosolic portion followed by six transmembrane helices, which might have arisen through gene duplication. On the basis of sequence similarity and functional characteristics, the superfamily can be subdivided into two major groups: water-selective channels called aquaporins (AQPs) and glycerol uptake facilitators (GlpFs). AQPs are found in all three kingdoms of life, while GlpFs have been characterized only within microorganisms
RKYLAEFLGTFLLVFFGCGSVLAVKLAGGASGGLLGIALAWGFAIFVLVYAVGHISGGHINPAVTLALAV
GGRFPLIRVIPYIIAQLLGAILGAALLYGLYYGLYLEFLGANNIVAGIFGTYPSPGVSNGNAFFVEFIGT
FILVLVVFATTDDPNGPPPGGLAPLAIGLLVAAIGLAGGPITGASMNPARSLGPALFTGLARHWHYFWVY
WVGPLIGAIAGALVYDYV
>gnl|CDD|238205 cd00336, Ribosomal_L22, Ribosomal protein L22/L17e. L22 (L17 in eukaryotes) is a core protein of the large ribosomal subunit. It is the only ribosomal protein that interacts with all six domains of 23S rRNA, and is one of the proteins important for directing the proper folding and stabilizing the conformation of 23S rRNA. L22 is the largest protein contributor to the surface of the polypeptide exit channel, the tunnel through which the polypeptide product passes. L22 is also one of six proteins located at the putative translocon binding site on the exterior surface of the ribosome
AKAKGRYLRISPKKARLVARLIRGMSVDEALAQLEFVPKKAAKIILKLLKSAEANAENNGLDDPDKLYIK
HIQVNKGPTLKRRRPRARGRANPIRKRTCHITVVL
>gnl|CDD|466774 cd00337, Ribosomal_uL14, Ribosomal protein uL14. Ribosomal protein uL14 (L14 in bacteria and mitochondria, L23 in eukaryotes, L38 in fungal mitochondria) is part of the large ribosomal subunit, located between the centers of activity for peptidyl transferase and GTPase. uL14 has an "all beta" fold that binds 23S rRNA. Ribosomal proteins, which are components of ribosomal subunits, are RNA-binding proteins that might have multiple extra ribosomal functions and may be involved in tumorigenesis in mammals
QVGTRLNVADNSGAKKVKCIKVLGKKGRRYAGVGDIIVVSVKKAKPEKKVKKGEVVKAVIVRTKKEIRRK
DGSYIRFDDNAVVLINKKGEPLGTRIFGPVARELRAKKFPKILS
>gnl|CDD|238206 cd00338, Ser_Recombinase, Serine Recombinase family, catalytic domain; a DNA binding domain may be present either N- or C-terminal to the catalytic domain. These enzymes perform site-specific recombination of DNA molecules by a concerted, four-strand cleavage and rejoining mechanism which involves a transient phosphoserine linkage between DNA and serine recombinase. Serine recombinases demonstrate functional versatility and include resolvases, invertases, integrases, and transposases. Resolvases and invertases (i.e. Tn3, gamma-delta, Tn5044 resolvases, Gin and Hin invertases) in this family contain a C-terminal DNA binding domain and comprise a major phylogenic group. Also included are phage- and bacterial-encoded recombinases such as phiC31 integrase, SpoIVCA excisionase, and Tn4451 TnpX transposase. These integrases and transposases have larger C-terminal domains compared to resolvases/invertases and are referred to as large serine recombinases. Also belonging to this family are proteins with N-terminal DNA binding domains similar to IS607- and IS1535-transposases from Helicobacter and Mycobacterium
IYARVSTDKQEQGDSLERQREALREYAARNGLEVVGEYEDAGSSATSLVDRPGLQRLLADVKAGKIDVVL
VEKLDRLSRNLVDLLELLELLEAHGVRVVTADGEIDLDSEDGRLMLGILAAMAEEESKLISERTKRG
>gnl|CDD|238207 cd00340, GSH_Peroxidase, Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes
SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEP
GSNEEIKEFCETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFA
PTTDPEELEKDI
>gnl|CDD|238208 cd00342, gram_neg_porins, Porins form aqueous channels for the diffusion of small hydrophillic molecules across the outer membrane. Individual 16-strand anti-parallel beta-barrels form a central pore, and trimerizes thru mainly hydrophobic interactions at the interface. Trimers are stabilized by hytrophillic clamping of Loop L2. Loop 3 bends into the pore, creating an elliptical constriction of about 7 x 11A, large enough to allow passage of a glucose molecule without steric hindrance. Removal of the C-terminal residue (usuallly F) destabilizes the trimer and removal of the 16th beta-sheet abolishes trimerization. Unlike typical membrane proteins, porins lack long hydrophobic stretches. Short turns are found at the smooth, periplasmic end, longer irregular loops are found at the rough, extracellular end. C-terminal residue forms salt bridge with N-terminus
SSVTLYGRIDAGVEYVNNAGGGGAGQMTSGGNNGSRWGLRGSEDLGGGLKAIFQLESGFNLNTGALGQGG
RLFGRQAYVGLSSDTYGTLTLGRQYTPLYDVLGTTDPFGGSGGGSAPGDGDNLAGTGRANNSVKYTSPFF
GGLTFGAMYAFGNQAGSTSNGRGYGAGLSYENGPLSLGAAYDQQRNGGGAAGGAAGATSQRAYGAGASYD
FGGLKLGAGYTNTRNDNGGGGGSAKFNGYELGATYQLTPALRLGAAYYYTKDRNDGGGDGKANQVALGAD
YALSKRTDLYAEYGYQKNSGGASTGLAGGGGPSSGNNQDGVAVGIRHKF
>gnl|CDD|188629 cd00344, FBP_aldolase_I, Fructose-bisphosphate aldolase class I. Fructose-bisphosphate aldolase class I. Fructose-1,6-bisphosphate aldolase is an enzyme of the glycolytic and gluconeogenic pathways found in vertebrates, plants, and bacteria. The enzyme catalyzes the cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP). Mutations in the aldolase genes in humans cause hemolytic anemia and hereditary fructose intolerance. The enzyme is a member of the class I aldolase family, which utilizes covalent catalysis through a Schiff base formed between a lysine residue of the enzyme and ketose substrates. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin
KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPRIGGVILFHE
TLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVL
KIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHI
YLEGTLLKPNMVTPGHACTQKFSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPL
LKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLAAQ
>gnl|CDD|238209 cd00347, Flavin_utilizing_monoxygenases, Flavin-utilizing monoxygenases
MKFGLFLPPPGGGGATAAEDLEYLVELARLAERLGFDAAWVAIWFGGSSPPVAEQAGESGDGLLFAAREP
PEEVAEALARYREAAAAAGR
>gnl|CDD|100101 cd00349, Ribosomal_L11, Ribosomal protein L11. Ribosomal protein L11, together with proteins L10 and L7/L12, and 23S rRNA, form the L7/L12 stalk on the surface of the large subunit of the ribosome. The homologous eukaryotic cytoplasmic protein is also called 60S ribosomal protein L12, which is distinct from the L12 involved in the formation of the L7/L12 stalk. The C-terminal domain (CTD) of L11 is essential for binding 23S rRNA, while the N-terminal domain (NTD) contains the binding site for the antibiotics thiostrepton and micrococcin. L11 and 23S rRNA form an essential part of the GTPase-associated region (GAR). Based on differences in the relative positions of the L11 NTD and CTD during the translational cycle, L11 is proposed to play a significant role in the binding of initiation factors, elongation factors, and release factors to the ribosome. Several factors, including the class I release factors RF1 and RF2, are known to interact directly with L11. In eukaryotes, L11 has been implicated in regulating the levels of ubiquinated p53 and MDM2 in the MDM2-p53 feedback loop, which is responsible for apoptosis in response to DNA damage. In bacteria, the "stringent response" to harsh conditions allows bacteria to survive, and ribosomes that lack L11 are deficient in stringent factor stimulation
IKLQVPAGKASPAPPLGPALGQLGVNIMKFCKEFNARTKDYKGLPVPVKITVYNDRSFTFEVKTPPASAL
LKKAAGIEKGSKKPNKEKVGNITLDQVYEIAKIKLPDLNAKTLKSAVKEILGTARSMGITV
>gnl|CDD|238210 cd00350, rubredoxin_like, Rubredoxin_like; nonheme iron binding domain containing a [Fe(SCys)4] center. The family includes rubredoxins, a small electron transfer protein, and a slightly smaller modular rubredoxin domain present in rubrerythrin and nigerythrin and detected either N- or C-terminal to such proteins as flavin reductase, NAD(P)H-nitrite reductase, and ferredoxin-thioredoxin reductase. In rubredoxin, the iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), but iron can also be replaced by cobalt, nickel or zinc and believed to be involved in electron transfer. Rubrerythrins and nigerythrins are small homodimeric proteins, generally consisting of 2 domains: a rubredoxin domain C-terminal to a non-sulfur, oxo-bridged diiron site in the N-terminal rubrerythrin domain. Rubrerythrins and nigerythrins have putative peroxide activity
KYVCPVCGYIYDGEEAPWVCPVCGAPKDKFEKL
>gnl|CDD|238211 cd00351, TS_Pyrimidine_HMase, Thymidylate synthase and pyrimidine hydroxymethylase: Thymidylate synthase (TS) and deoxycytidylate hydroxymethylase (dCMP-HMase) are homologs that catalyze analogous alkylation of C5 of pyrimidine nucleotides. Both enzymes are involved in the biosynthesis of DNA precursors and are active as homodimers. However, they exhibit distinct pyrimidine base specificities and differ in the details of their catalyzed reactions. TS is biologically ubiquitous and catalyzes the conversion of dUMP and methylene-tetrahydrofolate (CH2THF) to dTMP and dihydrofolate (DHF). It also acts as a regulator of its own expression by binding and inactivating its own RNA. Due to its key role in the de novo pathway for thymidylate synthesis and, hence, DNA synthesis, it is one of the most conserved enzymes across species and phyla. TS is a well-recognized target for anticancer chemotherapy, as well as a valuable new target against infectious diseases. Interestingly, in several protozoa, a single polypeptide chain codes for both, dihydrofolate reductase (DHFR) and thymidylate synthase (TS), forming a bifunctional enzyme (DHFR-TS), possibly through gene fusion at a single evolutionary point. DHFR-TS is also active as a dimer. Virus encoded dCMP-HMase catalyzes the reversible conversion of dCMP and CH2THF to hydroxymethyl-dCMP and THF. This family also includes dUMP hydroxymethylase, which is encoded by several bacteriophages that infect Bacillus subtilis, for their own protection against the host restriction system, and contain hydroxymethyl-dUMP instead of dTMP in their DNA
QYLDLWRKILEEGYRKTDDRTGTGTRSLFGAQLRFDLSEGFPLLTTKKVPWKSAIEELLWFLRGDTNAER
LKEYGVSIWDEWASKEGDLGYTYGFQWRHWGAPGQGVDQIEKVIEKLKNNPDSRRAIISAWNPADLDLMA
LPPCHTLIQFYVRNGKLSLTLYQRSNDAFLGVPFNIASYALLTEMIARVTGLEPGEFIHTIGDAHIYENH
LEQVK
>gnl|CDD|238212 cd00352, Gn_AT_II, Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer
CGIFGIVGADGAASLLLLLLLRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGV
ALGHVRLATNGLPSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLG
REGGLFEAVEDALKRLDGPFAFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPFKG
VRRLPPGELL
>gnl|CDD|238213 cd00353, Ribosomal_S15p_S13e, Ribosomal protein S15 (prokaryotic)_S13 (eukaryotic) binds the central domain of 16S rRNA and is required for assembly of the small ribosomal subunit and for intersubunit association, thus representing a key element in the assembly of the whole ribosome. S15 also plays an important autoregulatory role by binding and preventing its own mRNA from being translated. S15 has a predominantly alpha-helical fold that is highly structured except for the N-terminal alpha helix
KKQEILKEFGLAEGDTGSPEVQLALLTERIVNLTEHLEKNKKDKHSKRGLLLLVSKRRRLLKYLKRKDRL
RYEWLIEKLG
>gnl|CDD|238214 cd00354, FBPase, Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway. The alignment model also includes chloroplastic FBPases and sedoheptulose-1,7-biphosphatases that play a role in pentose phosphate pathway (Calvin cycle)
LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALK
SSGVVAVLASEEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPG
RNQVAAGYALYGPSTMLVLTLGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKY
IDDCKAGEDGGKPYNLRYIGSMVADVHRILVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKAT
DGKERILDIVPTSLHQRVPVILGSKEEVERVEEYL
>gnl|CDD|100098 cd00355, Ribosomal_L30_like, Ribosomal protein L30, which is found in eukaryotes and prokaryotes but not in archaea, is one of the smallest ribosomal proteins with a molecular mass of about 7kDa. L30 binds the 23SrRNA as well as the 5S rRNA and is one of five ribosomal proteins that mediate the interactions 5S rRNA makes with the ribosome. The eukaryotic L30 members have N- and/or C-terminal extensions not found in their prokaryotic orthologs. L30 is closely related to the ribosomal L7 protein found in eukaryotes and archaea
KVTRVRSLIGRPPKQRKTLKALGLRKINQTVFVKDTPSIRGMLRKVKHLVTVG
>gnl|CDD|238215 cd00361, arom_aa_hydroxylase, Biopterin-dependent aromatic amino acid hydroxylase; a family of non-heme, iron(II)-dependent enzymes that includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH), eukaryotic tyrosine hydroxylase (TyrOH) and eukaryotic tryptophan hydroxylase (TrpOH). PheOH converts L-phenylalanine to L-tyrosine, an important step in phenylalanine catabolism and neurotransmitter biosynthesis, and is linked to a severe variant of phenylketonuria in humans. TyrOH and TrpOH are involved in the biosynthesis of catecholamine and serotonin, respectively. The eukaryotic enzymes are all homotetramers
PRVDYTEEEHATWRTLYRRLKKLLPTHACREYLEGLELLGLPEDRIPQLEDVSEFLKALTGWTLVPVAGL
ISPRDFFALLAFRVFPVTQYIRHPEEPDYTPEPDIFHELFGHVPLLADPSFADFSQEYGLASLGASDLEE
IEKLARLYWFTVEFGLIKEDGELKAYGAGLLSSYGELQHALSDKPKRIPFDPERVARTPYDITSFQPTYF
VIESFEQLKEK
>gnl|CDD|238216 cd00363, PFK, Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to PFK family that includes ATP- and pyrophosphate (PPi)- dependent phosphofructokinases. Some members evolved by gene duplication and thus have a large C-terminal/N-terminal extension comprising a second PFK domain. Generally, ATP-PFKs are allosteric homotetramers, and PPi-PFKs are dimeric and nonallosteric except for plant PPi-PFKs which are allosteric heterotetramers
KKIGVLTSGGDAPGMNAAIRGVVRSAIAEGLEVYGIYEGYAGLVEGDIKELDWESVSDIINRGGTIIGSA
RCKEFRTEEGRAKAAENLKKHGIDALVVIGGDGSYTGADLLTEEWPSKYQGFNVIGLPGTIDNDIKGTDY
TIGFDTALKTIVEAIDRIRDTASSHQRTFVVEVMGRHCGDIALEAGLATGADIIFIPEEPAADEWEEEMV
DVIKKRRERGKRHGIVIVAEGAIDFIPKPITEKLLAKLVEERLGFDTRATVLGHVQRGGTPTAFDRILAS
RLGAEAVELLLEGTGGTPVGIQNLNENQVVRHPLTEAVNMTKRVGVDLEGRPFKKFAK
>gnl|CDD|466775 cd00364, Ribosomal_uS17, Ribosomal protein uS17. Ribosomal protein uS17 is one of the three primary assembly proteins (S4, S17 and S20) that stabilize the entire 5' rRNA domain and increase the global stability of the rRNA structure. uS17 is highly conserved in all three major phylogenetic divisions. In eukaryotes, the S17 ortholog of the cytoplasmic ribosome is called S11 as are those of the mitochondrial and chloroplast ribosomes. uS17 plays a critical role in both subunit assembly and translational fidelity
KILIGVVVSDKMDKTVVVRVERLVYHPKYKKYVKRTKKYHAHDEPNECKVGDIVRIGECRPLSKTKRWVV
VEI
>gnl|CDD|153080 cd00365, HMG-CoA_reductase, Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) is a tightly regulated enzyme, which catalyzes the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. In mammals, this is the rate limiting committed step in cholesterol biosynthesis. Bacteria, such as Pseudomonas mevalonii, which rely solely on mevalonate for their carbon source, catalyze the reverse reaction, using an NAD-dependent HMGR to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. There are two classes of HMGR: class I enzymes which are found predominantly in eukaryotes and contain N-terminal membrane regions and class II enzymes which are found primarily in prokaryotes and are soluble as they lack the membrane region. With the exception of Archaeoglobus fulgidus, most archeae are assigned to class I, based on sequence similarity of the active site, even though they lack membrane regions. Yeast and human HMGR are divergent in their N-terminal regions, but are conserved in their active site. In contrast, human and bacterial HMGR differ in their active site architecture. While the prokaryotic enzyme is a homodimer, the eukaryotic enzyme is a homotetramer
PAFRTLSPHAARLDHIGQLLGLSHDDVQLLANAALPMDIANGMIENVIGTFELPYAVASNFQIDGRDVLV
PLVTEEPSIVAAASYMAKLARAGGGFTTSSSAPLMHAQVQIVLIQDPLNAKLSLLRSGKDEIIELANRKD
QLLNSLGGGCRDIEVHTFGPMLVAHLIVDVGDAMGANMINTMAEAVAPLMEAYTGGMQVRLRSLSNLTGD
GRLARAQARITPQQLETAEFSGEAVIEGILDAYAFKAAVDSYRAATHNKGIMNGVDPLIVACGQDWRAVE
VGAHAYACRHYGSLTTWEKDNNGHLVITLEMSMPVGLVGGATKTHPLAQASLRILGVKTAQALARIAVAV
GLAQNLGAMRALATEGIQRGHMALHA
>gnl|CDD|466787 cd00366, ASKHA_NBD_FGGY, nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases. This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains
YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDI
AAIGISGQMPGVVLVDADGNPLRPAIIWLDRRAKFLQPNDYIVFRLTGEFAIDYSNASGTGLYDIKTGDW
SEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTAAAALGAGVVEPGDAVDST
GTSSVLSVCTDEPVPPDPRLLNRCHVVPGLWLLEGAINTGGASLRWFRDEFGEEEDSDAEYEGLDELAAE
VPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVKIKE
IRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA
>gnl|CDD|238217 cd00367, PTS-HPr_like, Histidine-containing phosphocarrier protein (HPr)-like proteins. HPr is a central component of the bacterial phosphoenolpyruvate sugar phosphotransferase system (PTS). The PTS catalyses the phosphorylation of sugar substrates during their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate is transferred to HPr by enzyme I (EI). Phospho-HPr then transfers the phosphoryl group to one of several sugar-specific phosphoprotein intermediates. The conserved histidine in the N-terminus of HPr serves as an acceptor for the phosphoryl group of EI. In addition to the phosphotransferase proteins HPr and E1, this family also includes the closely related Carbon Catabolite Repressor (CCR) proteins which use the same phosphorylation mechanism and interact with transcriptional regulators to control expression of genes coding for utilization of less favored carbon sources
TVTITNPLGLHARPAALLVQLASKFKSDITLRKGGRKANAKSILGLMSLGAKQGDEITLSAEGEDAEEAL
EALAELL
>gnl|CDD|238218 cd00368, Molybdopterin-Binding, Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site
PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRGKFVP
ISWDEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALK
AFGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRP
GTDAALALAEWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRP
GGGLGPGGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTEGRVQLF
RQAVEPPGEARSDWEILRELAKRL
>gnl|CDD|238219 cd00371, HMA, Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions
ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEVSPEELLEAIEDAGYKAR
>gnl|CDD|238220 cd00374, RNase_T2, Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases). Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleotides. They are also expressed in response to wounding or pathogen invasion. S-RNases are thought to prevent self-fertilization by acting as selective cytotoxins of "self" pollen
FDYYVLVLQWPPTFCATGPCKCCGTPPPDSFTIHGLWPDNCDGTYPQFCDSSSFFDKSKDSDLLDELNKY
WPDLMPGKDSSFWKHEWNKHGTCSGTLLDQDDYFRTALKLLDKLDLLSILAKAGIKPSDGSTYTLAFIQN
AIKAATGATPSLKCTKDPGKGLLTEIWICFDKDALKFIDCPTPGKSTCPADGIKF
>gnl|CDD|238221 cd00375, Urease_alpha, Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers
KISREAYADMYGPTTGDKVRLGDTDLWIEVEKDYTTYGDEVKFGGGKVLRDGMGQSSGYTREDVLDLVIT
NALIIDYTGIYKADIGIKDGRIVAIGKAGNPDIMDGVTPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFIC
PQQIEEALASGITTMIGGGTGPAAGTKATTCTPGPWNIKRMLQAADGLPVNIGFLGKGNGSSPDALAEQI
EAGACGLKLHEDWGATPAAIDTCLSVADEYDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTYHTEGAGGG
HAPDIIKVAGHPNVLPSSTNPTRPFTVNTLDEHLDMLMVCHHLDPNIPEDVAFAESRIRAETIAAEDVLH
DLGAISIMSSDSQAMGRVGEVILRTWQTAHKMKAQRGPLPEDSGDADNFRVKRYIAKYTINPAIAHGISH
EVGSVEVGKLADLVLWEPAFFGVKPEMVLKGGFIAYAQMGDPNASIPTPQPVMMRPMFGAHGKAPAATSV
TFVSQASLDAGIAEELGLRRRVVAVKNCRGVGKKDMKLNSATPDIEVDPETYEVRVDGELLTCEPADELP
LAQRYFL
>gnl|CDD|119340 cd00377, ICL_PEPM, Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. Known members are phosphoenolpyruvate mutase (PEPM), phosphonopyruvate hydrolase (PPH), carboxyPEP mutase (CPEP mutase), oxaloacetate hydrolase (OAH), isocitrate lyase (ICL), and 2-methylisocitrate lyase (MICL). Isocitrate lyase (ICL) catalyzes the conversion of isocitrate to succinate and glyoxylate, the first committed step in the glyoxylate pathway. This carbon-conserving pathway is present in most prokaryotes, lower eukaryotes and plants, but has not been observed in vertebrates. PEP mutase (PEPM) turns phosphoenolpyruvate (PEP) into phosphonopyruvate (P-pyr), an important intermediate in the formation of organophosphonates, which function as antibiotics or play a role in pathogenesis or signaling. P-pyr can be hydrolyzed by phosphonopyruvate hydrolase (PPH) to from pyruvate and phosphate. Oxaloacetate acetylhydrolase (OAH) catalyzes the hydrolytic cleavage of oxaloacetate to form acetate and oxalate, an important pathway to produce oxalate in filamentous fungi. 2-methylisocitrate lyase (MICL) cleaves 2-methylisocitrate to pyruvate and succinate, part of the methylcitrate cycle for the alpha-oxidation of propionate
LRALLESGGPLVLPGAWDALSARLAERAGFKAIYTSGAGVAASLGLPDGGLLTLDEVLAAVRRIARAVDL
PVIADADTGYGNALNVARTVRELEEAGAAGIHIEDQVGPKKCGHHGGKVLVPIEEFVAKIKAARDARDDL
PDFVIIARTDALLAGEEGLDEAIERAKAYAEAGADGIFVEGLKDPEEIRAFAEAPDVPLNVNMTPGGNLL
TVAELAELGVRRVSYGLALLRAAAKAMREAARE
>gnl|CDD|99733 cd00378, SHMT, Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). SHMT carries out interconversion of serine and glycine; it catalyzes the transfer of hydroxymethyl group of N5, N10-methylene tetrahydrofolate to glycine resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers; the mammalian enzyme forms a homotetramer comprising four pyridoxal phosphate-bound active sites
ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLA
IERAKKLFGAEYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFTKVSASGKLFESVPYG
VDPETGLIDYDALEKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPN
PLPGADVVTTTTHKTLRGPRGGLILTRKGELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAY
AKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSSPF
VPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVAEL
>gnl|CDD|238222 cd00379, Ribosomal_L10_P0, Ribosomal protein L10 family; composed of the large subunit ribosomal protein called L10 in bacteria, P0 in eukaryotes, and L10e in archaea, as well as uncharacterized P0-like eukaryotic proteins. In all three kingdoms, L10 forms a tight complex with multiple copies of the small acidic protein L12(e). This complex forms a stalk structure on the large subunit of the ribosome. The N-terminal domain (NTD) of L10 interacts with L11 protein and forms the base of the L7/L12 stalk, while the extended C-terminal helix binds to two or three dimers of the NTD of L7/L12 (L7 and L12 are identical except for an acetylated N-terminus). The L7/L12 stalk is known to contain the binding site for elongation factors G and Tu (EF-G and EF-Tu, respectively); however, there is disagreement as to whether or not L10 is involved in forming the binding site. The stalk is believed to be associated with GTPase activities in protein synthesis. In a neuroblastoma cell line, L10 has been shown to interact with the SH3 domain of Src and to activate the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott-Aldrich Syndrome Protein (WASP) and the WASP-interacting protein (WIP). Some eukaryotic P0 sequences have an additional C-terminal domain homologous with acidic proteins P1 and P2
EKKEELVEELKELLKKYKSVVVVDYRGLTVAQLTELRKELRESGAKLKVGKNTLMRRALKGTGFEELKPL
LKGPTALAFTNEDPVEVAKVLKDFAKENKKLFAKGGVVAGKVLDPAGVTALAKLPSREELLAMLIGLLKA
PIAKLARLLNALGIG
>gnl|CDD|240504 cd00380, KOW, KOW: an acronym for the authors' surnames (Kyrpides, Ouzounis and Woese). KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. The KOW motif contains an invariants glycine residue and comprises alternating blocks of hydrophilic and hydrophobic residues
GDVVRVLRGPYKGREGVVVDIDPRFGIVTVKGATGSKGAELKVRFDDVD
>gnl|CDD|238223 cd00381, IMPDH, IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents
GLTFDDVLLVPGYSTVLPSEVDLSTKLTKNITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIE
EQAEEVRKVKGRLLVGAAVGTREDDKERAEALVEAGVDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIA
GNVVTAEAARDLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSG
DIVKALAAGADAVMLGSLLAGTDESPGEYIEINGKRYKEYRGMGSLGAMKKGGGDRYFGEEAKKLVPEGV
EGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLKELQEKARFVRI
>gnl|CDD|238224 cd00382, beta_CA, Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes
QKPKALIIGCSDSRVPPELIFGLGPGDLFVVRNAGNLVPPYDLDVLASLEYAVEVLGVKHIIVCGHTDCG
AVKALVEENVREQVENLRSHPLIQEAVAPGELKVHGWVYDIETGKLEVL
>gnl|CDD|294013 cd00383, trans_reg_C, DNA-binding effector domain of two-component system response regulators. Bacteria and some eukaryotes use two-component signal transduction systems to detect and respond to changes in the environment. The systems consists of a sensor histidine kinase and a response regulator. The former autophosphorylates a histidine residue on detecting an external stimulus. The phosphate is then transferred to an invariant aspartate residue in a highly conserved receiver domain of the response regulator. Phosphorylation activates a variable effector domain of the response regulator, which triggers the cellular response. This C-terminal effector domain belongs to the winged helix-turn-helix family of transcriptional regulators and contains DNA and RNA polymerase binding sites. Several dimers or monomers bind head to tail to small tandem repeats upstream of the genes. The RNA polymerase binding sites interact with the alpha or sigma subunit of RNA polymerase
LRLDPARREVTVDGEEVELTPKEFELLELLARNPGRVVSREELLEAVWGYDYEVDDRTVDVHISRLRKKL
EDDPEPRLIKTVRGVGYRL
>gnl|CDD|238226 cd00384, ALAD_PBGS, Porphobilinogen synthase (PBGS), which is also called delta-aminolevulinic acid dehydratase (ALAD), catalyzes the condensation of two 5-aminolevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (PBG), which is the second step in the biosynthesis of tetrapyrroles, such as heme, vitamin B12 and chlorophyll. This reaction involves the formation of a Schiff base link between the substrate and the enzyme. PBGSs are metalloenzymes, some of which have a second, allosteric metal binding site, beside the metal ion binding site in their active site. Although PBGS is a family of homologous enzymes, its metal ion utilization at catalytic site varies between zinc and magnesium and/or potassium. PBGS can be classified into two groups based on differences in their active site metal binding site. They either contain a cysteine-rich zinc binding site (consensus DXCXCX(Y/F)X3G(H/Q)CG) or an aspartate-rich magnesium binding site (consensus DXALDX(Y/F)X3G(H/Q)DG). The cysteine-rich zinc binding site appears more common. Most members represented by this model also have a second allosteric magnesium binding site (consensus RX~164DX~65EXXXD, missing in a eukaryotic subfamily with cysteine-rich zinc binding site)
RRLRRSPALRDLVRETRLSPDDLIYPLFVVEGIDEKEEISSMPGVYRLSVDSLVEEAEELADLGIRAVIL
FGIPEHKDEIGSEAYDPDGIVQRAIRAIKEAVPELVVITDVCLCEYTDHGHCGILKDDYVDNDATLELLA
KIAVSHAEAGADIVAPSDMMDGRVAAIREALDEAGFSDVPIMSYSAKYASAFYGPFRDAADSAPSFGDRK
TYQMDPANRREALREVELDIEEGADILMVKPALAYLDIIRDVRERFDLPVAAYNVSGEYAMIKAAAKNGW
IDEERVVLESLTSIKRAGADLIITYFAKDAARWL
>gnl|CDD|173830 cd00385, Isoprenoid_Biosyn_C1, Isoprenoid Biosynthesis enzymes, Class 1. Superfamily of trans-isoprenyl diphosphate synthases (IPPS) and class I terpene cyclases which either synthesis geranyl/farnesyl diphosphates (GPP/FPP) or longer chained products from isoprene precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), or use geranyl (C10)-, farnesyl (C15)-, or geranylgeranyl (C20)-diphosphate as substrate. These enzymes produce a myriad of precursors for such end products as steroids, cholesterol, sesquiterpenes, heme, carotenoids, retinoids, and diterpenes; and are widely distributed among archaea, bacteria, and eukaryota.The enzymes in this superfamily share the same 'isoprenoid synthase fold' and include several subgroups. The head-to-tail (HT) IPPS catalyze the successive 1'-4 condensation of the 5-carbon IPP to the growing isoprene chain to form linear, all-trans, C10-, C15-, C20- C25-, C30-, C35-, C40-, C45-, or C50-isoprenoid diphosphates. Cyclic monoterpenes, diterpenes, and sesquiterpenes, are formed from their respective linear isoprenoid diphosphates by class I terpene cyclases. The head-to-head (HH) IPPS catalyze the successive 1'-1 condensation of 2 farnesyl or 2 geranylgeranyl isoprenoid diphosphates. Cyclization of these 30- and 40-carbon linear forms are catalyzed by class II cyclases. Both the isoprenoid chain elongation reactions and the class I terpene cyclization reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, stabilizing reactive carbocation intermediates. Generally, the enzymes in this family exhibit an all-trans reaction pathway, an exception, is the cis-trans terpene cyclase, trichodiene synthase. Mechanistically and structurally distinct, class II terpene cyclases and cis-IPPS are not included in this CD
FRPLAVLLEPEASRLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAVAIDGLPEAILAGDLLLADAFE
ELAREGSPEALEILAEALLDLLEGQLLDLKWRREYVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAE
LLEALRKLGRALGLAFQLTNDLLDYEGDAERGEGKCTLPVLYALEYGVPAEDLLLVEKSGSLEEALEELA
KLAEEALKELNELILSLPDVPRALLALALNLYR
>gnl|CDD|238227 cd00386, Heme_Cu_Oxidase_III_like, Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria
HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGAGLDPLDLPLLNTNTLLLSGSSVTWAH
ASLAARRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLL
VVLIRLRRGHFTPRHHLGLEAAALYWHFVDVVWLFLFPLVYLW
>gnl|CDD|100102 cd00387, Ribosomal_L7_L12, Ribosomal protein L7/L12. Ribosomal protein L7/L12 refers to the large ribosomal subunit proteins L7 and L12, which are identical except that L7 is acetylated at the N terminus. It is a component of the L7/L12 stalk, which is located at the surface of the ribosome. The stalk base consists of a portion of the 23S rRNA and ribosomal proteins L11 and L10. An extended C-terminal helix of L10 provides the binding site for L7/L12. L7/L12 consists of two domains joined by a flexible hinge, with the helical N-terminal domain (NTD) forming pairs of homodimers that bind to the extended helix of L10. It is the only multimeric ribosomal component, with either four or six copies per ribosome that occur as two or three dimers bound to the L10 helix. L7/L12 is the only ribosomal protein that does not interact directly with rRNA, but instead has indirect interactions through L10. The globular C-terminal domains of L7/L12 are highly mobile. They are exposed to the cytoplasm and contain binding sites for other molecules. Initiation factors, elongation factors, and release factors are known to interact with the L7/L12 stalk during their GTP-dependent cycles. The binding site for the factors EF-Tu and EF-G comprises L7/L12, L10, L11, the L11-binding region of 23S rRNA, and the sarcin-ricin loop of 23S rRNA. Removal of L7/L12 has minimal effect on factor binding and it has been proposed that L7/L12 induces the catalytically active conformation of EF-Tu and EF-G, thereby stimulating the GTPase activity of both factors. In eukaryotes, the proteins that perform the equivalent function to L7/L12 are called P1 and P2, which do not share sequence similarity with L7/L12. However, a bacterial L7/L12 homolog is found in some eukaryotes, in mitochondria and chloroplasts. In archaea, the protein equivalent to L7/L12 is called aL12 or L12p, but it is closer in sequence to P1 and P2 than to L7/L12
LKVEEIVEALKELTLLEAAELVKALEEKFGVSASAAAAAAAAAAPAAAAAAAAEAEEKTEFDVVLESFGA
AKKIAVIKEVREITGLGLKEAKDLVESAPKVLKEGVSKEEAEEIKKKLEEAGAKVEL
>gnl|CDD|238228 cd00389, microbial_RNases, microbial_RNases. Ribonucleases (RNAses) cleave phosphodiester bonds in RNA and are essential for both non-specific RNA degradation and for numerous forms of RNA processing. The alignment contains fungal RNases (U2, T1, F1, Th, Pb, N1, and Ms) and bacterial RNases (barnase, binase, RNase Sa), the majority of which are guanyl specific and fungal ribotoxins
AQAALNLIASGGPFGYSIYGHVFNNREGFLPFKGSGYYHEYPVNTPGGGSRGADRVVYGGDGEFYGTIDH
Y
>gnl|CDD|238229 cd00390, Urease_gamma, Urease gamma-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, archaea, fungi and plants. Their primary role is to allow the use of external and internally-generated urea as a nitrogen source. The enzyme consists of three subunits, alpha, beta and gamma, which can exist as separate proteins or can be fused on a single protein chain. The alpha-beta-gamma heterotrimer forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers
TPRELEKLLIFTAAELARKRLARGLKLNYPEAVALIADEILEGARDGKSVAELMSLGKTVLTRDDVMEGV
PEMLHDVQVEATFPDGTKLVTVHDPI
>gnl|CDD|238230 cd00392, Ribosomal_L13, Ribosomal protein L13. Protein L13, a large ribosomal subunit protein, is one of five proteins required for an early folding intermediate of 23S rRNA in the assembly of the large subunit. L13 is situated on the bottom of the large subunit, near the polypeptide exit site. It interacts with proteins L3 and L6, and forms an extensive network of interactions with 23S rRNA. L13 has been identified as a homolog of the human breast basic conserved protein 1 (BBC1), a protein identified through its increased expression in breast cancer. L13 expression is also upregulated in a variety of human gastrointestinal cancers, suggesting it may play a role in the etiology of a variety of human malignancies
WHVIDAKGQVLGRLASKVAKLLLGKHKPTYTPHVDCGDYVVVVNAEKIVITGKKWRQKVYYRHTGYPGGL
KNPTAGPLHPRAPERILKRAVRGMLPKNKLGRAALKRLKVYEGA
>gnl|CDD|132923 cd00394, Clp_protease_like, Caseinolytic protease (ClpP) is an ATP-dependent protease. Clp protease (caseinolytic protease; ClpP; endopeptidase Clp; Peptidase S14; ATP-dependent protease, ClpAP)-like enzymes are highly conserved serine proteases and belong to the ClpP/Crotonase superfamily. Included in this family are Clp proteases that are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth, targeting DNA-binding protein from starved cells. The functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP. Active site consists of the triad Ser, His and Asp, preferring hydrophobic or non-polar residues at P1 or P1' positions. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function. Another family included in this class of enzymes is the signal peptide peptidase A (SppA; S49) which is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Mutagenesis studies suggest that the catalytic center of SppA comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. In addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members, the E. coli SppA contains an amino-terminal domain. Others, including sohB peptidase, protein C, protein 1510-N and archaeal signal peptide peptidase, do not contain the amino-terminal domain. The third family included in this hierarchy is nodulation formation efficiency D (NfeD) which is a membrane-bound Clp-class protease and only found in bacteria and archaea. Majority of the NfeD genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named stomatin operon partner protein (STOPP). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 from Pyrococcus horikoshii has been shown to possess serine protease activity having a Ser-Lys catalytic dyad
VIFINGVIEDVSADQLAAQIRFAEADNSVKAIVLEVNTPGGRVDAGMNIVDALQASRKPVIAYVGGQAAS
AGYYIATAANKIVMAPGTRVGSHGPIGGYGGNGNPTAQEADQRIILYFIARFISLVAENRGQTTEKLEED
IEKDLVLTAQEALEYGLVDAL
>gnl|CDD|173893 cd00395, Tyr_Trp_RS_core, catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase. Tyrosinyl-tRNA synthetase (TyrRS)/Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. These enzymes attach Tyr or Trp, respectively, to the appropriate tRNA. These class I enzymes are homodimers, which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding
TLYCGIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRI
AAQYLAVGIFEDPTQATLFNNSDWPGPLAHIQFLRDLGKHVYVNYMERKTSFQSRSEEGISATEFTYPPL
QAADFLLLNTTEGCDIQPGGSDQWGNITLGRELARRFNGFTIAEGLTIPLVTKLDGPKFGKSESGPKWLD
TEKTSPYEFYQFWINAVDSDVINILKYFTFLSKEEIERLEQEQYEAPGYRVAQKTLAEEVTKT
>gnl|CDD|100027 cd00396, PurM-like, AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM (formylglycinamidine ribonucleotide) synthase and Selenophosphate synthetase (SelD). The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain
SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDILEDVVDGVAEACNQ
LGVPIVGGHTSVSPGTMGHKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTGVDAVLELVAAGDVHAMHD
ITDGGLLGTLPELAQASGVGAEIDLEAIPLDEVVRWLCVEHIEEALLFNSSGGLLIAVPAEEADAVLLLL
NGNGIDAAVIGR
>gnl|CDD|271175 cd00397, DNA_BRE_C, DNA breaking-rejoining enzymes, C-terminal catalytic domain. The DNA breaking-rejoining enzyme superfamily includes type IB topoisomerases and tyrosine based site-specific recombinases (integrases) that share the same fold in their catalytic domain containing conserved active site residues. The best-studied members of this diverse superfamily include Human topoisomerase I, the bacteriophage lambda integrase, the bacteriophage P1 Cre recombinase, the yeast Flp recombinase, and the bacterial XerD/C recombinases. Their overall reaction mechanism is essentially identical and involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. The enzymes differ in that topoisomerases cleave and then rejoin the same 5' and 3' termini, whereas a site-specific recombinase transfers a 5' hydroxyl generated by recombinase cleavage to a new 3' phosphate partner located in a different duplex region. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity
ELEKLLDAIDEDKKIDLRDRAILLLLLETGLRISELLALKVKDIDLDNGTIRVRGKKTKGGKERTVPLPK
ELAEELKEYLKERRDKRGPLLKSLYLNKLFGTKLGERLSRRTLRRIFKKAGIEAGRKITPHSLRHTFATN
LLENGVDIKVVQKLLGHSSISTTQRYL
>gnl|CDD|238232 cd00398, Aldolase_II, Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations
EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGKKPS
SETPLHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVYFTGDIPCTPYMTPETGEDEIGT
QRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH
>gnl|CDD|259843 cd00399, RNAP_largest_subunit_N, Largest subunit of RNA polymerase (RNAP), N-terminal domain. This region represents the N-terminal domain of the largest subunit of RNA polymerase (RNAP). RNAP is a large multi-protein complex responsible for the synthesis of RNA. It is the principle enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. At least three distinct RNAP complexes are found in eukaryotic nuclei; RNAP I transcribes the ribosomal RNA precursor, RNAP II the mRNA precursor, and RNAP III the 5S and tRNA genes. A single distinct RNAP complex is found in prokaryotes and archaea, respectively, which may be responsible for the synthesis of all RNAs. Structure studies reveal that prokaryotic and eukaryotic RNAPs share a conserved crab-claw-shaped structure. The largest and the second largest subunits each make up one clamp, one jaw, and part of the cleft. All RNAPs are metalloenzymes. At least one Mg2+ ion is bound in the catalytic center. In addition, all cellular RNAPs contain several tightly bound zinc ions to different subunits that vary between RNAPs from prokaryotic to eukaryotic lineages. This domain represents the N-terminal region of the largest subunit of RNAP, and includes part of the active site. In archaea and some of the photosynthetic organisms or cellular organelle, however, this domain exists as a separate subunit
MSPEEIRKWSVAKVIKPETIDNRTLKAERGGKYDPRLGSIDRCEKCGTCGTGLNDCPGHFGHIELAKPVF
HVGFIKKVPSFLGPEWMILTCLPVPPPCLRPSVIIEERWRLLQEHVDTYLDNGIAGQPQTQKSGRPLRSL
AQRLKGKEGRFRGNLMGKRVDFSGRSVISPDPNLRLDQVGVPKSIALTLDGDPVLFNRQPSLHKLSIMAH
RVRVLPGSTFRLNPLVCSPYNADFDGDEMNLHVPQSEEARAEARELMLVPNNILSPQNGEPLIGLSQDTL
LGAYLLTLGKQIVSAALPGGLLHTVTRELGPEKAAKLLSNLQRVGFVFLTTSGFSVGIGDVIDDGVIPEE
KTELIEEAKKKVDEVEEAFQAGLLTAQEGMTLEESLEDNILDFLNEARDKAGSAASVNLDLVSKFNSIYV
MAMSGAKGSFINIRQMSACVGQQSVEGKRIPRGFSDRTLPHFSKDDYSPEAKGFIRNSFLEGLTPLEYFF
HAMGGREGLVDTAVKTAESGYLQRRLVKALEDLVVHYD
>gnl|CDD|238233 cd00400, Voltage_gated_ClC, CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. This domain is found in the halogen ions (Cl-, Br- and I-) transport proteins of the ClC family. The ClC channels are found in all three kingdoms of life and perform a variety of functions including cellular excitability regulation, cell volume regulation, membrane potential stabilization, acidification of intracellular organelles, signal transduction, transepithelial transport in animals, and the extreme acid resistance response in eubacteria. They lack any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. Unlike cation-selective ion channels, which form oligomers containing a single pore along the axis of symmetry, the ClC channels form two-pore homodimers with one pore per subunit without axial symmetry. Although lacking the typical voltage-sensor found in cation channels, all studied ClC channels are gated (opened and closed) by transmembrane voltage. The gating is conferred by the permeating ion itself, acting as the gating charge. In addition, eukaryotic and some prokaryotic ClC channels have two additional C-terminal CBS (cystathionine beta synthase) domains of putative regulatory function
GVLSGLGAVLFRLLIELLQNLLFGGLPGELAAGSLSPLYILLVPVIGGLLVGLLVRLLGPARGHGIPEVI
EAIALGGGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLSRNDRRILVACGAAA
GIAAAFNAPLAGALFAIEVLLGEYSVASLIPVLLASVAAALVSRLLFGAEPAFGVPLYDPLSLLELPLYL
LLGLLAGLVGVLFVRLLYKIERLFRRLPIPPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLALAGELSL
LLLLLLLLLKLLATALTLGSGFPGGVFAPSLFIGAALGAAFGLLLPALFPGLVASPGAYALVGMAALLAA
VLRAPLTAILLVLELTGDYSLLLPLMLAVVIAY
>gnl|CDD|240619 cd00401, SAHH, S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains. S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+
EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQ
DDVAAALAEAGIPVFAWKGETEEEYWWCIEQALDHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETT
TGVHRLRAMEKEGKLLFPAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGC
AMRARGLGARVIVTEVDPICALQAAMDGFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCN
AGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRRIILLAEGRLVNLACATGHPSFVMDMSFANQALA
QIELWKNRDKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQAEYLGSW
>gnl|CDD|293928 cd00402, Riboflavin_synthase_like, Riboflavin synthase and similar proteins. Riboflavin synthase catalyzes the dismutation of two molecules of 6,7-dimethyl-8-(1'-D-ribityl)-lumazine (DMRL) to yield riboflavin (vitamin B12) and 4-ribitylamino-5-amino-2,6-dihydroxypyrimidine (RAADP). Riboflavin synthase is a homotrimer and the catalysis does not require any cofactors. Active sites are located between pairs of monomers, but only one active site catalyzes a reaction, the other two sites are inactive. Humans do not produce riboflavin synthase, and thus it is a good target for antimicrobial agents. This family also include lumazine protein (LumP) from bioluminescent bacteria. LumP serves as an optical transponder in bioluminescence emission
MFTGIIEEIGTVKSIEKKGGGARLTIEAPKVLEDLKIGDSIAVNGVCLTVTEIDGDSFTFDVSPETLRRT
TLGNLKVGDRVNLERALRLGDRLGGHIVQGHVDGVGTIVSIEKEGNSLRLTIEIPKELARYIVEKGSIAI
DGVSLTVNEVDEDTFSVSLIPHTLENTTLGTLKVGDRVNIEVDIL
>gnl|CDD|238235 cd00403, Ribosomal_L1, Ribosomal protein L1. The L1 protein, located near the E-site of the ribosome, forms part of the L1 stalk along with 23S rRNA. In bacteria and archaea, L1 functions both as a ribosomal protein that binds rRNA, and as a translation repressor that binds its own mRNA. Like several other large ribosomal subunit proteins, L1 displays RNA chaperone activity. L1 is one of the largest ribosomal proteins. It is composed of two domains that cycle between open and closed conformations via a hinge motion. The RNA-binding site of L1 is highly conserved, with both mRNA and rRNA binding the same binding site
LEEAIKALKKTSVKKRKFDETVELQINLKKDDRKKDQRIRGTVILPHGLGKDVKVCVFAKDEQAKEAKAA
GADVVGGEDLKKKIKNGEAKKLAKDFDLFLADPRIMMLLPKLLGKVLGPRGKMPNPKTGTVTEDLAKAIE
EAKSSVEFRLDKGGCIHVPVGKVSMSPEQLVENIEAVINALVKKLPSKKGQNIKSIYLKTTMGPSLPI
>gnl|CDD|238236 cd00404, Aconitase_swivel, Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The aconitase family contains the following proteins: - Iron-responsive element binding protein (IRE-BP). IRE-BP is a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid
KVAGNITTDHISPAGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFA
DPEDYLKLHTGDELDIYP
>gnl|CDD|238237 cd00405, PRAI, Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan biosynthesis, the conversion of N-(5'- phosphoribosyl)-anthranilate (PRA) to 1-(o-carboxyphenylamino)- 1-deoxyribulose 5-phosphate (CdRP). Most PRAIs are monomeric, monofunctional and thermolabile, but in some thermophile organisms PRAI is dimeric for reasons of stability and in others it is fused to other components of the tryptophan biosynthesis pathway to form multifunctional enzymes
VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAALPPFVKRVGVFVNEDLEEILEIAE
ELGLDVVQLHGDESPEYCAQLRARLGLPVIKAIRVKDEEDLEKAAAYAGEVDAILLDSKSGGGGGGTGKT
FDWSLLRGLASRKPVILAGGLTPDNVAEAIRLVRPYGVDVSSGVETSPGIKDPEKIRAFIEAA
>gnl|CDD|238238 cd00407, Urease_beta, Urease beta-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, archaea, fungi and plants. Their primary role is to allow the use of external and internally-generated urea as a nitrogen source. The enzyme consists of three subunits, alpha, beta and gamma, which can exist as separate proteins or can be fused on a single protein chain. The alpha-beta-gamma heterotrimer forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers
MIPGEIILKEGDIELNAGREAVTLKVKNTGDRPIQVGSHYHFFEVNPALKFDREKAYGMRLDIPAGTAVR
FEPGEEKEVELVPIGGKRRVYGFNGLVNGPL
>gnl|CDD|188630 cd00408, DHDPS-like, Dihydrodipicolinate synthase family. Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family
VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVI
AGVGANSTREAIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLS
PETIARLAEHPNIVGIKDSSGDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLA
VALYEAARAGDLEEARALQDRLLPLIEALFKEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEAL
L
>gnl|CDD|199205 cd00411, L-asparaginase_like, Bacterial L-asparaginases and related enzymes. Asparaginases (amidohydrolases, E.C. 3.5.1.1) are dimeric or tetrameric enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases, one highly specific for asparagine and localized to the periplasm (type II L-asparaginase), and a second (asparaginase- glutaminase) present in the cytosol (type I L-asparaginase) that hydrolyzes both asparagine and glutamine with similar specificities and has a lower affinity for its substrate. Bacterial L-asparaginases (type II) are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL). A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. This wider family also includes a subunit of an archaeal Glu-tRNA amidotransferase
PNITILATGGTIAGVGDSATYSAYVAGALGVEKLIKAVPELKELANVKGEQLMNIASEDITPDDWLKLAK
EVAKLLDSDVDGIVITHGTDTXEETAYFLSLTLKNDKPVVLVGAMRPSTAMSADGPFNLYNAVRVAKDKD
SRGRGVLVVMNDKVHSGRDVSKTNTSGFDAFRSINYGPLGEIKDNKIYYQRKPARKHTDESEFDVSDIKS
LPKVDIVYLYPGLSDDIYDALVDLGYKGIVLAGTGNGSVPYDVFPVLSSASKRGVAVVRSSQVIYGGVDL
NAEKVDLKAGVIPAGDLNPEKARVLLMWALTHTKDPEEVQ
>gnl|CDD|238239 cd00412, pyrophosphatase, Inorganic pyrophosphatase. These enzymes hydrolyze inorganic pyrophosphate (PPi) to two molecules of orthophosphates (Pi). The reaction requires bivalent cations. The enzymes in general exist as homooligomers
EVVNVVIEIPKGSNAKYEIDKETGPIKVDRFLYSSMGYPWNYGFIPQTLEDDGDPLDVLVIGEEPLFPGS
VIRVRPLGVLKMIDEGETDWKVIAVPVDDPRYSHINDISDVPPHLLDEIKHFFEHYKDLEGKKEVKVAGW
KDKEEALKIIKESIE
>gnl|CDD|185683 cd00413, Glyco_hydrolase_16, glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues
DDFDGLALDTSKWTIQDGPSWGGNMTNSPNNVYVENDGGLTLRTDRDQTDGPYSSAEIDSQKNNYTYGYY
EARAKLAGGPGAVSAFWTYSDDDDPPDGGEIDIEFLGRDPTTVQTNVHWPGYGAGATTGEEKSVHLPFDP
ADDFHTYRVDWTPGEITFYVDGVLVATITNQVPDDPMNIILNLWSDGGWWWGGPPPGAPAYMEIDWVRVY
>gnl|CDD|185672 cd00418, GlxRS_core, catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase. Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains
TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEG
PYRQSDRFDLYRAYAEELIKKGGYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRF
YHFPRLLLEDGTKLSKRKLNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNS
ADATFDWAKLEWLNREYIRE
>gnl|CDD|238240 cd00419, Ferrochelatase_C, Ferrochelatase, C-terminal domain: Ferrochelatase (protoheme ferrolyase or HemH) is the terminal enzyme of the heme biosynthetic pathway. It catalyzes the insertion of ferrous iron into the protoporphyrin IX ring yielding protoheme. This enzyme is ubiquitous in nature and widely distributed in bacteria and eukaryotes. Recently, some archaeal members have been identified. The oligomeric state of these enzymes varies depending on the presence of a dimerization motif at the C-terminus
EALADHIREALAELPREKDRLLFSAHGLPVRDIKKGDPYPDQCEETARLVAERLGLPFDEYELAYQSRFG
PGEWLEPSTDDALEELAKEGVKNVVVVPIGFVSDHLETLYELDIEYRELAEEAGGENYRRVPCLN
>gnl|CDD|238241 cd00421, intradiol_dioxygenase, Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of catecholate derivatives to citric acid cycle intermediates. This family contains catechol 1,2-dioxygenases and protocatechuate 3,4-dioxygenases which are mononuclear non-heme iron enzymes that catalyze the oxygenation of catecholates to aliphatic acids via the cleavage of aromatic rings. The members are intradiol-cleaving enzymes which break the catechol C1-C2 bond and utilize Fe3+, as opposed to the extradiol-cleaving enzymes which break the C2-C3 or C1-C6 bond and utilize Fe2+ and Mn+. Catechol 1,2-dioxygenases are mostly homodimers with one catalytic ferric ion per monomer. Protocatechuate 3,4-dioxygenases form more diverse oligomers
ADLTEDAPGEPLTLTGTVLDGDGCPVPDALVEIWQADADGRYSGQDDSGLDPEFFLRGRQITDADGRYRF
RTIKPGPYPIGRPPHIHFKVFAPGYNRRLTTQLYFPGDPLNDSDPVFAPYSENVRPTLIADFDGIEFLEY
RFDIVL
>gnl|CDD|238242 cd00423, Pterin_binding, Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). DHPS, a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS. Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH
TLIMGILNVTPDSFSDGGKFLSLDKALEHARRMVEEGADIIDIGGESTRPGAEPVSVEEELERVIPVLRA
LAGEPDVPISVDTFNAEVAEAALKAGADIINDVSGGRGDPEMAPLAAEYGAPVVLMHMDGTPQTMQNNPY
YADVVDEVVEFLEERVEAATEAGIPPEDIILDPGIGFGKTEEHNLELLRRLDAFRELPGLPLLLGVSRKS
FLGDLLSVGPKDRLAGTAAFLAAAILNGADIVRVHDVKELRDAIKVAE
>gnl|CDD|176453 cd00424, PolY, Y-family of DNA polymerases. Y-family DNA polymerases are a specialized subset of polymerases that facilitate translesion synthesis (TLS), a process that allows the bypass of a variety of DNA lesions. Unlike replicative polymerases, TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. The active sites of TLS polymerases are large and flexible to allow the accomodation of distorted bases. Most TLS polymerases are members of the Y-family, including Pol eta, Pol kappa/IV, Pol iota, Rev1, and Pol V, which is found exclusively in bacteria. In eukaryotes, the B-family polymerase Pol zeta also functions as a TLS polymerase. Expression of Y-family polymerases is often induced by DNA damage and is believed to be highly regulated. TLS is likely induced by the monoubiquitination of the replication clamp PCNA, which provides a scaffold for TLS polymerases to bind in order to access the lesion. Because of their high error rates, TLS polymerases are potential targets for cancer treatment and prevention
LHIDFDNFFASVEQLARPELKGRPVVVVPFNSDSTCVIACSYEARKYGVKRGMPVREARKMCPNLILVPA
RLDLYRRLSERLLSELEEVAPLVEVASIDELFLDLTGSARLLGLGSEVALRIKRHIAEQLGGITASIGIA
SNKLLAKLAAKYAKPDGLTILDPEDLPGFLSKLPLTDLPGIGAVTAKRLEAVGINPIGDLLAASPDALLA
LWGGVSGERLWYALRGIDDEPLSPPRPRKSFSHERVLPRDSRNAEDARPLLRLLLEKLARRLRRDGRGAT
RLRLWLRTVDGRWSGHADIPSRSAPRPISTEDGELLHALDKLWRALLDDKGPRRLRRLGVRLS
>gnl|CDD|238243 cd00427, Ribosomal_L29_HIP, Ribosomal L29 protein/HIP. L29 is a protein of the large ribosomal Subunit. A homolog, called heparin/heparan sulfate interacting protein (HIP), has also been identified in mammals. L29 is located on the surface of the large ribosomal subunit, where it participates in forming a protein ring that surrounds the polypeptide exit channel, providing structural support for the ribosome. L29 is involved in forming the translocon binding site, along with L19, L22, L23, L24, and L31e. In addition, L29 and L23 form the interaction site for trigger factor (TF) on the ribosomal surface, adjacent to the exit tunnel. L29 forms numerous interactions with L23 and with the 23S rRNA. In some eukaryotes, L29 is referred to as L35, which is distinct from L35 found in bacteria and some eukaryotes (primarily plastids and mitochondria). The mammalian homolog, HIP, is found on the surface of many tissues and cell lines. It is believed to play a role in cell adhesion and modulation of blood coagulation. It has also been shown to inhibit apoptosis in cancer cells
KELREKSDEELQEKLDELKKELFNLRFQKATGQLENPHRIRKVRKDIARIKTVLNEK
>gnl|CDD|238244 cd00429, RPE, Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis
KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPE
RYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGF
GGQKFIPEVLEKIRKLRELIPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKEL
R
>gnl|CDD|143481 cd00430, PLPDE_III_AR, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase. This family includes predominantly bacterial alanine racemases (AR), some serine racemases (SerRac), and putative bifunctional enzymes containing N-terminal UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase (murF) and C-terminal AR domains. These proteins are fold type III PLP-dependent enzymes that play essential roles in peptidoglycan biosynthesis. AR catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. SerRac converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. murF catalyzes the addition of D-Ala-D-Ala to UDPMurNAc-tripeptide, the final step in the synthesis of the cytoplasmic precursor of bacterial cell wall peptidoglycan. Members of this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. AR and other members of this family require dimer formation and the presence of the PLP cofactor for catalytic activity. Fungal ARs and eukaryotic serine racemases, which are fold types I and II PLP-dependent enzymes respectively, are excluded from this family
RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREA
GITAPILVLGGTPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRPEEAE
ELLEALKALPGLELEGVFTHFATADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEA
HFDMVRPGIALYGLYPSPEVKSPLGLKPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYA
DGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVTDIPDVKVGDEVVLFGRQGDEEITAEELAELAGTI
NYEILCRISKRVPRIYV
>gnl|CDD|238245 cd00431, cysteine_hydrolases, Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine amidohydrolase), involved in creatine metabolism and nicotinamidase, converting nicotinamide to nicotinic acid and ammonia in the pyridine nucleotide cycle. It also contains isochorismatase, an enzyme that catalyzes the conversion of isochorismate to 2,3-dihydroxybenzoate and pyruvate, via the hydrolysis of the vinyl ether bond, and other related enzymes with unknown function
ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAELLWPPHCVKGT
EGAELVPELAPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIV
VEDACATRDEEDHEAALERLA
>gnl|CDD|238246 cd00432, Ribosomal_L18_L5e, Ribosomal L18/L5e: L18 (L5e) is a ribosomal protein found in the central protuberance (CP) of the large subunit. L18 binds 5S rRNA and induces a conformational change that stimulates the binding of L5 to 5S rRNA. Association of 5S rRNA with 23S rRNA depends on the binding of L18 and L5 to 5S rRNA. L18/L5e is generally described as L18 in prokaryotes and archaea, and as L5e (or L5) in eukaryotes. In bacteria, the CP proteins L5, L18, and L25 are required for the ribosome to incorporate 5S rRNA into the large subunit, one of the last steps in ribosome assembly. In archaea, both L18 and L5 bind 5S rRNA; in eukaryotes, only the L18 homolog (L5e) binds 5S rRNA but a homolog to L5 is also identified
RRRKRLGTQERPRLVVRKSNKHIYAQIIDDSGDKTLVSASTLELAIKGVLGSGNNVEAAYLVGRLLAKRA
LEKGIKKVVFDRGGYRYHGRVKALAKGAREGGL
>gnl|CDD|238247 cd00433, Peptidase_M17, Cytosol aminopeptidase family, N-terminal and catalytic domains. Family M17 contains zinc- and manganese-dependent exopeptidases (EC 3.4.11.1), including leucine aminopeptidase. They catalyze removal of amino acids from the N-terminus of a protein and play a key role in protein degradation and in the metabolism of biologically active peptides. They do not contain HEXXH motif (which is used as one of the signature patterns to group the peptidase families) in the metal-binding site. The two associated zinc ions and the active site are entirely enclosed within the C-terminal catalytic domain in leucine aminopeptidase. The enzyme is a hexamer, with the catalytic domains clustered around the three-fold axis, and the two trimers related to one another by a two-fold rotation. The N-terminal domain is structurally similar to the ADP-ribose binding Macro domain. This family includes proteins from bacteria, archaea, animals and plants
ADGLVLGVFEGEGGLPPAAEKLDAASSGALAALLKASGFKGKAGETLLLPALGGGAKRVALVGLGKEEDL
DVENLRKAAGAAARALKKLGSKSVAVDLPTLAEDAEAAAEGALLGAYRFDRYKSKKKKTPLLVVLELGND
KAAEAALERGEAIAEGVNLARDLVNTPANDLTPTYLAEEAKELAKELGVKVEVLDEKELEELGMGALLAV
GKGSEEPPRLIVLEYKGKGASKKPIALVGKGITFDTGGLSLKPAAGMDGMKYDMGGAAAVLGAMKAIAEL
KLPVNVVGVLPLAENMISGNAYRPGDVITSRSGKTVEILNTDAEGRLVLADALTYAQEFKPDLIIDIATL
TGAAVVALGHDYAGLFTNDDELAKQLLAAGEASGERVWRLPLWEEYREQLKSDIADLKNIGGRGPAGSIT
AALFLKEFVGDGIPWAHLDIAGTAWKSKPGYLPKGATGFGVRLLVEFL
>gnl|CDD|238248 cd00435, ACBP, Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected
LQEEFEAAAEKVKKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAM
KAYIAKVEELIAKYA
>gnl|CDD|350155 cd00436, UP_TbUP-like, uridine phosphorylases similar to Trypanosoma brucei UP. Uridine phosphorylase (UP) catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose 1-phosphate. Trypanosoma brucei UP has a high specificity for uracil-containing (deoxy)nucleosides, and may function as a dimer. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
ELILNPDGSIYHLHLKPEDLADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTG
IGTDNIDIVLNELDALVNIDFKTRTPKEEKTSLNIIRLGTSGALQPDIPVGSLVISSYAIGLDNLLNFYD
HPNTDEEAELENAFIAHTSWFKGKPRPYVVKASPELLDALTGVGYVVGITATAPGFYGPQGRQLRLPLAD
PDLLDKLSSFSYGGLRITNFEMETSAIYGLSRLLGHRALSICAIIANRATGEFSKDYKKAVEKLIEKVLE
AL
>gnl|CDD|380337 cd00438, cupin_RmlC, RmlC carbohydrate epimerase, involved in dTDP-L-rhamnose production. RmlC (deoxythymidine diphosphate (dTDP)-4-keto-6-deoxy-D-hexulose 3, 5-epimerase or dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase; also known as RfbC) is a carbohydrate epimerase involved in the production of dTDP-L-rhamnose, a precursor of the bacterial cell wall constituent, L-rhamnose. L-Rhamnose (6-deoxy-l-mannose) plays an important role in the cell-wall structure of many bacterial species. It has been found to contribute to the virulence of several species, including the Gram-negative Salmonella enterica and Vibrio cholerae, where it is present as a part of the O-antigen, and is essential for the growth of Gram-positive bacteria such as Streptococcus pyogenes. RmlC converts dTDP-6-deoxy-D-xylo-4-hexulose to dTDP-6-deoxy-L-xylo-hexulose by catalyzing the epimerization of the 5-methyl and 3-hydroxyl groups of hexulose, the third of four steps in the dTDP-L-rhamnose biosynthetic pathway. RmlC belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
FTETAIPGVLLIEPKVFGDERGFFAETFNKEEFAEAGINPDFVQDNHSFSKKGVLRGLHFQLPPHAQAKL
VRCLRGAIFDVAVDLRKGSPTFGQWVGVELSAENHRQLYIPEGFAHGFQTLSDDAEVLYKCSDYYAPESE
RGIRWNDPDLGIDWPLPEPILSEKDRNA
>gnl|CDD|188631 cd00439, Transaldolase, Transaldolase. Transaldolase. Enzymes found in the non-oxidative branch of the pentose phosphate pathway, that catalyze the reversible transfer of a dihydroxyacetone group from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. They are members of the class I aldolases, who are characterized by using a Schiff-base mechanism for stabilization of the reaction intermediates
SPWYDTLDRPATDLLPLIRGVRGVTTNPSIIQAAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDA
CKLFEPIYDQTEADGRVSVEVSARLADDTQGMVEAAKYLSKVVNRRNIYIKIPATAEGIPAIKDLIAAGI
SVNVTLIFSIAQYEAVADAGTSVASPFVSRIDTLMDKMLEQIGLDLRGKAGVAQVTLAYKLYKQKFKKQR
VLWASFSDTLYVAPLIGCDTVTTMPDQALEAGVDKFKKDFES
>gnl|CDD|381596 cd00442, Lyz-like, lysozyme-like domains. This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides
VLAAIIGQESGGNKPANAGSGSGAAGLFQFMPGTWKAYGKNSSSDLNDPEASIEAAAKY
>gnl|CDD|238250 cd00443, ADA_AMPD, Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase catalyzes a similar reaction leading to the hydrolytic removal of an amino group at the 6 position of the adenine nucleotide ring, a branch point in the adenylate catabolic pathway
LPKVELHAHLSGSISPETLLELIKKEFFEKFLLVHNLLQKGEALARALKEVIEEFAEDNVQYLELRTTPR
LLETEKGLTKEQYWLLVIEGISEAKQWFPPIKVRLILSVDRRGPYVQNYLVASEILELAKFLSNYVVGID
LVGDESKGENPLRDFYSYYEYARRLGLLGLTLHCGETGNREELLQALLLLPDRIGHGIFLLKHPELIYLV
KLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDL
CELNRNSVLSSFAKDEEKKSLLEVL
>gnl|CDD|238251 cd00445, Uricase, Urate oxidase (UO, uricase) is a peroxisomal enzyme that catalyzes the oxidation of uric acid to allantoin in most fish, amphibian, and mammalian species. The enzymatic process involves catalyzing the oxidative opening of the purine ring during the purine degradation pathway. In humans and certain other primates, however, the enzyme has been lost by some unknown mechanism. Each monomer contains two instances of this domain. Its functional form is a homotetramer for most species, though there are reports that some may form heterotetramers based on a few biochemical studies
TYGKDLVRVLRVWRDGFGGVHEVVEVNVGVSLGGDFLTSYTEGDNSDIVATDTIKNTVYVLAKEYGITSI
EEFAIILATHFLSKYSHVTGAHVNIEEKPWERVQQDGKPHDHAFIRTPTEKRTTEVIVVRSGILTVTSGI
KGLSVLKTTQSGFEGFLRDEYTTLPETRDRILATYVTASWRYSNTEDSPAKSPDFDAAWEQVRDILLDTF
AGPPDVGVYSPSVQHTLYLMAKQILDRFPQISSVSFQMPNKHYFPIDLSIKGLENNNEVYLPTDEPHGLI
EATVTR
>gnl|CDD|271355 cd00446, GrpE, nucleotide exchange factor GrpE. GrpE is the adenine nucleotide exchange factor of DnaK (Hsp70)-type ATPases. In bacteria, the DnaK-DnaJ-GrpE (KJE) chaperone system functions at the fulcrum of protein homeostasis. GrpE participates actively in response to heat shock by preventing aggregation of stress-denatured proteins; unfolded proteins initially bind to DnaJ, the J-domain ATPase-activating protein (Hsp40 family), whereupon DnaK hydrolyzes its bound ATP, resulting in a stable complex. The GrpE dimer binds to the ATPase domain of Hsp70 catalyzing the dissociation of ADP, which enables rebinding of ATP, one step in the Hsp70 reaction cycle in protein folding. In eukaryotes, only the mitochondrial Hsp70, not the cytosolic form, is GrpE dependent. Over-expression of Hsp70 molecular chaperones is important in suppressing toxicity of aberrantly folded proteins that occur in Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, as well as several polyQ-diseases such as Huntington's disease and ataxias
KELKDKLLRAQAEFENYRKRTEKEKEEAKKYAIEKFAKDLLPVLDNLERALEAAPKEEELKNLLEGVEMT
LKQLLKVLEKHGVEEIEPEGEKFDPNLHEAVMQVESPDKEPGTVVEVLQKGYKLHDRVLRPAMVVV
>gnl|CDD|238253 cd00447, NusB_Sun, RNA binding domain of NusB (N protein-Utilization Substance B) and Sun (also known as RrmB or Fmu) proteins. This family includes two orthologous groups exemplified by the transcription termination factor NusB and the N-terminal domain of the rRNA-specific 5-methylcytidine transferase (m5C-methyltransferase) Sun. The NusB protein plays a key role in the regulation of ribosomal RNA biosynthesis in eubacteria by modulating the efficiency of transcriptional antitermination. NusB along with other Nus factors (NusA, NusE/S10 and NusG) forms the core complex with the boxA element of the nut site of the rRNA operons. These interactions help RNA polymerase to counteract polarity during transcription of rRNA operons and allow stable antitermination. The transcription antitermination system can be appropriated by some bacteriophages such as lambda, which use the system to switch between the lysogenic and lytic modes of phage propagation. The m5C-methyltransferase Sun shares the N-terminal non-catalytic RNA-binding domain with NusB
SAREIAFQALYQVEIRNGISLEAVLSALEKLQLAKKDRPFALELVYGVLRNLPELDDIISPLLKKWLLDR
LDKVDRAILRLLLYELYQLLYDVPPPVAINEAVELAKRFGDDDSAKFVNGVLRRIAKES
>gnl|CDD|100004 cd00448, YjgF_YER057c_UK114_family, YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site
YSQAVRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAA
VNEVYDEFFGEGPPPARTAVGVAALPPGALVEIEAIA
>gnl|CDD|238254 cd00449, PLPDE_IV, PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity
DRGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYDREELREALKELVAANNGASLYIRPL
LTRGVGGLGVAPPPSPEPTFVVFASPVGAYAKGGEKGVRLITSPDRRRAAPGGTGDAKTGGNLNSVLAKQ
EAAEAGADEALLLDDNGYVTEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPIS
LDELYAADEVFLTGTAAEVTPVTEIDGRGIGDGKPGPVTRKLRELL
>gnl|CDD|212095 cd00451, GH38N_AMII_euk, N-terminal catalytic domain of eukaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). The family corresponds to a group of eukaryotic class II alpha-mannosidases (AlphaMII), which contain Golgi alpha-mannosidases II (GMII), the major broad specificity lysosomal alpha-mannosidases (LAM, MAN2B1), the noval core-specific lysosomal alpha 1,6-mannosidases (Epman, MAN2B2), and similar proteins. GMII catalyzes the hydrolysis of the terminal both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2 (GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. LAM is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. Different from LAM, Epman can efficiently cleave only the alpha 1,6-linked mannose residue from (Man)3GlcNAc, but not (Man)3(GlcNAc)2 or other larger high mannose oligosaccharides, in the core of N-linked glycans. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst
LNVHLIPHSHCDVGWLKTFDEYYNGDVKSILDSVVKALNNDPERKFIWAEIGFLERWWEDQGNDTKQQFK
KLVKNGQLEFVGGGWVMNDEACTTYESIIDQMTEGHQFLKDTFGVRPRVGWQIDPFGHSSTTPTLFSKMG
FKGLVINRIPYSLKAEMKDNKQLEFVWRGSPSLGPDSEIFTHVLDDHYSYPESLDFGGPPITDYNIAERA
DEFVEYIKKRSKTYRTNHILIPLGDDFRFKNASLQFSNMDKLIAYINS
>gnl|CDD|188632 cd00452, KDPG_aldolase, KDPG and KHG aldolase. KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources
LKAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQAD
AAIAAGAQFIVSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAVGPAYIKALKGP
FPQVRFMPTGGVSLDNAAEWLAAGVVAVGGGSLLPKDAVAAGDWAAITAL
>gnl|CDD|238255 cd00453, FTBP_aldolase_II, Fructose/tagarose-bisphosphate aldolase class II. This family includes fructose-1,6-bisphosphate (FBP) and tagarose 1,6-bisphosphate (TBP) aldolases. FBP-aldolase is homodimeric and used in gluconeogenesis and glycolysis; the enzyme controls the condensation of dihydroxyacetone phosphate with glyceraldehyde-3-phosphate to yield fructose-1,6-bisphosphate. TBP-aldolase is tetrameric and produces tagarose-1,6-bisphosphate. There is an absolute requirement for a divalent metal ion, usually zinc, and in addition the enzymes are activated by monovalent cations such as Na+. Although structurally similar, the class I aldolases use a different mechanism and are believed to have an independent evolutionary origin
VQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQFSNGGASFIAGKGVKSDVPQGAAILGA
ISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWIDGLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEI
CSKYLERMSKIGMTLEIELGCTGGEEDGVDNSHMDASALYTQPEDVDYAYTELSKISPRFTIAASFGNVH
GVYKKGNVVLTPTILRDSQEYVSKKHNLPHNSLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATW
EGVLNYYKANEAYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEKAFQELNAID
>gnl|CDD|381253 cd00454, TrHb1_N, truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins); group 1 (N). The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. They are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). Typical of the TrHb1s (N) group is a protein matrix tunnel. It includes a Mycobacterium tuberculosis TrHb1, Mt-trHbN, which is encoded by the glbN gene. Mt-trHbN is expressed during the Mycobacterium stationary phase, and plays a specific defense role against nitrosative stress. The cyanobacterium Synechococcus sp. PCC 7002 TrHb1 GlbN, is constitutively expressed, and likely also protects cells from reactive nitrogen species
ERLGGEEGIEAVVDDFYDRVLADPRIKPFFAGVDMARLKKKQTEFLCEAFGGPCEYTGRDMKEAHAGLNI
TDEHFDAFVEHLKEALEELGVPEELIDEVLAILEPLRPDIV
>gnl|CDD|238257 cd00455, nuc_hydro, nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains eukaryotic, bacterial and archeal proteins similar to the inosine-uridine preferring nucleoside hydrolase from Crithidia fasciculata, the xanthosine-inosine-uridine-adenosine-preferring nucleoside hydrolase RihC from Salmonella enterica serovar Typhimurium, the purine-specific inosine-adenosine-guanosine-preferring nucleoside hydrolase from Trypanosoma vivax and, pyrimidine-specific uridine-cytidine preferring nucleoside hydrolases such as URH1 from Saccharomyces cerevisiae, RihA and RihB from Escherichia coli. Nucleoside hydrolases are of interest as a target for antiprotozoan drugs as, no nucleoside hydrolase activity or genes encoding these enzymes have been detected in humans and, parasitic protozoans lack de novo purine synthesis relying on nucleoside hydrolase to scavenge purine and/or pyrimidines from the environment
VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGE
IPAAYPEIHGEGGLGLPIPPIIEADDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVK
EIVIMGGAFLVPGNVTPVAEANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGL
LIKPMIDYYYKAYQKPGIEGSPIHDPLAVAYLLNPSMFDYSKVPVDVDTDGLTRGQTIADFRENPGNGVT
RVAVNLDYPDFIELI
>gnl|CDD|176642 cd00457, PEBP, PhosphatidylEthanolamine-Binding Protein (PEBP) domain. PhosphatidylEthanolamine-Binding Proteins (PEBPs) are represented in all three major phylogenetic divisions (eukaryotes, bacteria, archaea). A number of biological roles for members of the PEBP family include serine protease inhibition, membrane biogenesis, regulation of flowering plant stem architecture, and Raf-1 kinase inhibition. Although their overall structures are similar, the members of the PEBP family bind very different substrates including phospholipids, opioids, and hydrophobic odorant molecules as well as having different oligomerization states (monomer/dimer/tetramer)
TLESPEVGPSGSVLPPEYSFEGVGRFPSLSWDGPPPDVKEYVLVMEDPDAPLGRPIVHGLVYGIPANKTS
LSNDDFVVTDNGKGGLQGGFKYGKNRGGTVYIGPRPPLGHGPHRYFFQVYALDEPLDRSKLGDGRTKFEV
ARFAEGNVLGAVGEWVGQF
>gnl|CDD|238258 cd00458, SugarP_isomerase, SugarP_isomerase: Sugar Phosphate Isomerase family; includes type A ribose 5-phosphate isomerase (RPI_A), glucosamine-6-phosphate (GlcN6P) deaminase, and 6-phosphogluconolactonase (6PGL). RPI catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate, the first step of the non-oxidative branch of the pentose phosphate pathway. GlcN6P deaminase catalyzes the reversible conversion of GlcN6P to D-fructose-6-phosphate (Fru6P) and ammonium, the last step of the metabolic pathway of N-acetyl-D-glucosamine-6-phosphate. 6PGL converts 6-phosphoglucono-1,5-lactone to 6-phosphogluconate, the second step of the oxidative phase of the pentose phosphate pathway
AKEALKFIEDKXEKLLEEKDDMVIGLGTGSTPAYFYKLLGEKLKRGEISDIVGFPTDERYVPLDSDQSNF
RQAKLLAFEHDIIPASNVHYVDTSLPIEKACEKYEREILDQVDAIDLAVDGAGYRAGTVIVLVDGRKKVD
YLCQNTEPGVIENGIFADIRGKEKDIVIV
>gnl|CDD|132901 cd00460, RNAP_RPB11_RPB3, RPB11 and RPB3 subunits of RNA polymerase. The eukaryotic RPB11 and RPB3 subunits of RNA polymerase (RNAP), as well as their archaeal (L and D subunits) and bacterial (alpha subunit) counterparts, are involved in the assembly of RNAP, a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. At least three distinct RNAP complexes are found in eukaryotic nuclei: RNAP I, RNAP II, and RNAP III, for the synthesis of ribosomal RNA precursor, mRNA precursor, and 5S and tRNA, respectively. A single distinct RNAP complex is found in prokaryotes and archaea, which may be responsible for the synthesis of all RNAs. The assembly of the two largest eukaryotic RNAP subunits that provide most of the enzyme's catalytic functions depends on the presence of RPB3/RPB11 heterodimer subunits. This is also true for the archaeal (D/L subunits) and bacterial (alpha subunit) counterparts
VKILEKEKNYVDFVLENEDHTLGNSLRRILLKSPVEFAAYYVEHPVKLQRTDEDKFILRIETVGSIPPEE
ALRRAVEILRKKLEHL
>gnl|CDD|238259 cd00462, PTH, Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the nascent peptide and tRNA when peptidyl-tRNA is released prematurely from the ribosome. This ensures the recycling of peptidyl-tRNAs into tRNAs produced through abortion of translation and is essential for cell viability.This group also contains chloroplast RNA splicing 2 (CRS2), which is closely related nuclear-encoded protein required for the splicing of nine group II introns in chloroplasts
LIVGLGNPGPKYENTRHNVGFMVLDALAERYGVSFKKKKKKGLVGEGRIGGEKVLLLKPQTYMNLSGEAV
AALANFYKIPPEDILVIHDDLDLPLGKIRLKKGGGSGGHNGLKSIIAHLGTEDFPRLRIGIGRPPNKMDV
ADYVLSKFSKEERELLEEAIEKAADALEDIL
>gnl|CDD|199209 cd00463, Ribosomal_L31e, Eukaryotic/archaeal ribosomal protein L31. Ribosomal protein L31e, which is present in archaea and eukaryotes, binds the 23S rRNA and is one of six protein components encircling the polypeptide exit tunnel. It is a component of the eukaryotic 60S (large) ribosomal subunit, and the archaeal 50S (large) ribosomal subunit
IEEVVEREYTINLRKRKHVPRKKRAPRAIKEIRKFAAKHMKTEDVRIDPKLNEAIWSRGIEKPPRRVRVR
VSRKREETEDAVL
>gnl|CDD|238260 cd00464, SK, Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP
NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKEN
AVIATGGGAVLREENRRLLLENGIVVWLDASPEELLERLARDKTRPLLQDEDPERLRELLEEREPLYREV
ADLTIDTDELSPEE
>gnl|CDD|238261 cd00465, URO-D_CIMS_like, The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases, as well as cobalamine (B12) independent methionine synthases. Despite their sequence similarities, members of this family have clearly different functions. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane, and methionine synthases transfer a methyl group from a folate cofactor to L-homocysteine in a reaction requiring zinc
PVQCEGQTGIMEASETMAISEEPGETSKAEWGITLVEPEEIPLDVIPVHEDDVLKVAQALGEWAFRYYSQ
APSVPEIDEEEDPFREAPALEHITAVRSLEEFPTAGAAGGPFTFTHHSMSMGDALMALYERPEAMHELIE
YLTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLGPKMFKKFALPAYKKVAEYKAAGEVPIVHHSCYDA
ADLLEEMIQLGVDVISFDMTVNEPKEAIEKVGEKKTLVGGVDPGYLPATDEECIAKVEELVERLGPHYII
NPDCGLGPDSDYKPEHLRAVVQLVDE
>gnl|CDD|238262 cd00466, DHQase_II, Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes the reversible dehydration of 3-dehydroquinate to form 3-dehydroshikimate. This reaction is part of two metabolic pathways: the biosynthetic shikimate pathway and the catabolic quinate pathway. There are two types of DHQases, which are distinct from each other in amino acid sequence and three-dimensional structure. Type I enzymes usually catalyze the biosynthetic reaction using a syn elimination mechanism. In contrast, type II enzymes, found in the quinate pathway of fungi and in the shikimate pathway of many bacteria, are dodecameric enzymes that employ an anti elimination reaction mechanism
KILVLNGPNLNLLGKREPEIYGTTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGADGII
INPGAYTHTSIALRDALAAVSIPVIEVHISNIHAREEFRHHSVISPVATGVIAGLGADGYRLALEALASL
>gnl|CDD|238263 cd00468, HIT_like, HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH/Qxx (x, a hydrophobic amino acid), are a superfamily of nucleotide hydrolases and transferases, which act on the alpha-phosphate of ribonucleotides. On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified in the literacture into three major branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the Fhit branch, that consists of diadenosine polyphosphate hydrolases, and the GalT branch consisting of specific nucloside monophosphate transferases. Further sequence analysis reveals several new closely related, yet uncharacterized subgroups
VPDDEHSFAFVNLKPAAPGHVLVCPKRHVETLPDLDEALLADLVITAQRVAAELEKHGNVPSLTVFVNDG
AAAGQSVPHVHLHVLP
>gnl|CDD|238264 cd00470, PTPS, 6-pyruvoyl tetrahydropterin synthase (PTPS). Folate derivatives are essential cofactors in the biosynthesis of purines, pyrimidines, and amino acids, as well as formyl-tRNA. Mammalian cells are able to utilize pre-formed folates after uptake by a carrier-mediated active transport system. Most microbes and plants lack this system and must synthesize folates de novo from guanosine triphosphate. One enzyme from this pathway is PTPS which catalyzes the conversion of dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin. The functional enzyme is a hexamer of identical subunits
SATLTRRFSFSACHRLHSPPLSDEENLEVFGKCNNPNGHGHNYKVEVTVRGEIDPVTGMVMNLTDLKKAI
EEAIMKPLDHKNLDDDVPYFADVVSTTENLAVYIWDNLQKVLPVGLLYEVKVHETDKNIVVYRGE
>gnl|CDD|100103 cd00472, Ribosomal_L24e_L24, Ribosomal protein L24e/L24 is a ribosomal protein found in eukaryotes (L24) and in archaea (L24e, distinct from archaeal L24). L24e/L24 is located on the surface of the large subunit, adjacent to proteins L14 and L3, and near the translation factor binding site. L24e/L24 appears to play a role in the kinetics of peptide synthesis, and may be involved in interactions between the large and small subunits, either directly or through other factors. In mouse, a deletion mutation in L24 has been identified as the cause for the belly spot and tail (Bst) mutation that results in disrupted pigmentation, somitogenesis and retinal cell fate determination. L24 may be an important protein in eukaryotic reproduction: in shrimp, L24 expression is elevated in the ovary, suggesting a role in oogenesis, and in Arabidopsis, L24 has been proposed to have a specific function in gynoecium development. No protein with sequence or structural homology to L24e/L24 has been identified in bacteria, but a functionally equivalent protein may exist. Bacterial L19 forms an interprotein beta sheet with L14 that is similar to the L24e/L14 interprotein beta sheet observed in the archaeal L24e structures. Some eukaryotic L24 proteins were initially identified as L30, and this alignment model contains several sequences called L30
MKTEKCSFCGYKIYPGHGKMYVRNDGKVFRFCSSKCEKNFLRKRNPRKLKWTVA
>gnl|CDD|275385 cd00473, bS6, Bacterial ribosomal protein S6. bS6 is one of the components of the small subunit of the prokaryotic ribosome, a ribonucleoprotein organelle that decodes the genetic information in messenger RNA and forms peptide bonds to synthesize the corresponding polypeptides. Ribosomes consist of a large and a small subunit, which assemble during the initiation stage of protein synthesis. Prokaryotic ribosomes consist of three molecules of RNA and more than 50 proteins. The small subunits of bacterial and eukaryotic ribosomes have the same overall shapes (with structural elements described as head, body, platform, beak and shoulder). The bacterial ribosomal protein S6 is important for the assembly of the central domain of the small subunit via heterodimerization with ribosomal protein S18
KYELMFILDPDLSEEEVKALIEKVKKIIEKNGGEIVKVEDWGKRKLAYPIKKKKEGYYVLINFEAEPEAI
AELERRLRINEDVLRFLIVKL
>gnl|CDD|211317 cd00474, eIF1_SUI1_like, Eukaryotic initiation factor 1 and related proteins. Members of the eIF1/SUI1 (eukaryotic initiation factor 1) family are found in eukaryotes, archaea, and some bacteria; eukaryotic members are understood to play an important role in accurate initiator codon recognition during translation initiation. eIF1 interacts with 18S rRNA in the 40S ribosomal subunit during eukaryotic translation initiation. Point mutations in the yeast eIF1 implicate the protein in maintaining accurate start-site selection but its mechanism of action is unknown. The function of non-eukaryotic family members is also unclear
KIHIKVEQRSGGKKVTKVEGLPAYIDLRKLADELKKKLGCGGSVEGEKMEIEIQGDHTDQIIVALEEKGI
DKDWVELL
>gnl|CDD|259850 cd00475, Cis_IPPS, Cis (Z)-Isoprenyl Diphosphate Synthases. Cis (Z)-Isoprenyl Diphosphate Synthases (cis-IPPS) catalyze the successive 1'-4 condensation of the isopentenyl diphosphate (IPP) molecule to trans,trans-farnesyl diphosphate (FPP) or to cis,trans-FPP to form long-chain polyprenyl diphosphates. A few can also catalyze the condensation of IPP to trans-geranyl diphosphate to form the short-chain cis,trans- FPP. In prokaryotes, the cis-IPPS, undecaprenyl diphosphate synthase (UPP synthase), catalyzes the formation of the carrier lipid UPP in bacterial cell wall peptidoglycan biosynthesis. Similarly, in eukaryotes, the cis-IPPS, dehydrodolichyl diphosphate (dedol-PP) synthase catalyzes the formation of the polyisoprenoid glycosyl carrier lipid dolichyl monophosphate. cis-IPPS form homodimers and are mechanistically and structurally distinct from trans-IPPS, which lack the DDXXD motifs, yet require Mg2+ for activity
HVAIIMDGNRRWAKKRGLPRTEGHRAGAEALREILEWCLELGIKYLTLYAFSTENWKRPKEEVDALMKLL
REYLEKELEELHKNGVRLRVIGDLSLLPEDLREAIEEAEEATKNNTGLTLNIALNYGGRDEIVRAVRKIA
RDVKAGELDPEDITEELISKHLYTADLPDPDLLIRTSGEQRLSNFLLWQSAYAELYFTDVLWPDFRKEDL
LRAILDYQR
>gnl|CDD|133468 cd00476, SAICAR_synt, 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase. SAICAR synthetase (the PurC gene product) catalyzes the seventh step of the de novo biosynthesis of purine nucleotides (also reported as eighth step). It converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate
TLYRGKTKIVYETKDGVLLLEFKDDISAGDGARRNFLDEKGDITAKLTLFIFKYLSEAGIPTHFVERLGP
RTLLVDKLKXIPLEVVVRNRATGSFVKRYGGFKEGREFPPPLVEFFYKDDAEHDPIVSEDQLERLGFIGK
VDVERXKELAVKINTVLKKLFSPAGLELWDFKLEFGLDEEGEIVLGDEISPDSSRLWRKGGEPYDKDLFR
RRASLGQIIEKYEEVAELVR
>gnl|CDD|349750 cd00477, FTHFS, formyltetrahydrofolate synthetase. Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ATP-dependent activation of formate ion via its addition to the N10 position of tetrahydrofolate. FTHFS is a highly expressed key enzyme in both the Wood-Ljungdahl pathway of autotrophic CO2 fixation (acetogenesis) and the glycine synthase/reductase pathways of purinolysis. The key physiological role of this enzyme in acetogens is to catalyze the formylation of tetrahydrofolate, an initial step in the reduction of carbon dioxide and other one-carbon precursors to acetate. In purinolytic organisms, the enzymatic reaction is reversed, liberating formate from 10-formyltetrahydrofolate with concurrent production of ATP
IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGAL
GKKAIAALRQPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENTLD
IDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIMAILALSTDLADLRERLGRIVVA
YSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSIIADKIALKLADYV
VTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAGEENLEALKKGCANLRKHIE
NIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAVSEHWAKGGKGALELAEAVIEACEKPKSNFK
FLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTG
FTLPIRDVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDIDDTGKIEGL
>gnl|CDD|238267 cd00480, malate_synt, Malate synthase catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA, which hydrolyzes to malate and CoA. This reaction is part of the glyoxylate cycle, which allows certain organisms, like plants and fungi, to derive their carbon requirements from two-carbon compounds, by bypassing the two carboxylation steps of the citric acid cycle
ALAFVAELHREFNPRRRELLAARDERQARLDAGHALPDFLPETAYIRRDGDWKVAPDPPDLDDRRVEITG
PQDRKMVINALNSGAAVFMADFEDSSAPTWENKVEGQRNLLDAVRGTISFTDSKNGKSYRLNLLDGRATL
FVRPRGWHLTEKHILVDGEPVPGGLFDFGLYFFHNAHALKARGSGPYFYLPKMESPLEARLWNDVFSRAE
DYLGLPRGTIKATVLIETLPAAFEMDEILYELRDHSAGLNCGRWDYIFSEIKTFRNHPDFVLPDRAKVTM
TSPFMRAYEKLLVKTCHRRGAHAMGGMAAQIPIKGDPAANEAAMAKVRADKLREAKAGHDGTWVAHPGLA
PLAALVFHKVMPGPNQLFRKREDVKVTADDLLTIPVAEGDITEEGLRNNIQVALGYVVAWLNGNGAVPII
NLMEDAATAEISRSQLWQWLRHGVCLDDGVPVTLELVAKLVDEENARLPAYRPPNFFDSIAFKEAADLFF
EGVTAEEFPEFLTEPLYHLLR
>gnl|CDD|238268 cd00481, Ribosomal_L19e, Ribosomal protein L19e. L19e is found in the large ribosomal subunit of eukaryotes and archaea. L19e is distinct from the ribosomal subunit L19, which is found in prokaryotes. It consists of two small globular domains connected by an extended segment. It is located toward the surface of the large subunit, with one exposed end involved in forming the intersubunit bridge with the small subunit. The other exposed end is involved in forming the translocon binding site, along with L22, L23, L24, L29, and L31e subunits
LRLQKRLAADILKCGKNRVWIDPNELEEIANANTREDIRKLIKDGLIIKKPKKGHSRGRARKRHEARRKG
RHRGPGSRKGTKGARMPSKELWIRRIRALRRLLKKLRDSGKIDKHTYRELYLKAKGNVFKNKRHLKEYIH
KAKAE
>gnl|CDD|238269 cd00483, HPPK, 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK). Folate derivatives are essential cofactors in the biosynthesis of purines, pyrimidines, and amino acids as well as formyl-tRNA. Mammalian cells are able to utilize pre-formed folates after uptake by a carrier-mediated active transport system. Most microbes and plants lack this system and must synthesize folates de novo from guanosine triphosphate. One enzyme from this pathway is HPPK which catalyzes pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP). The functional enzyme is a monomer. Mammals lack many of the enzymes in the folate pathway including, HPPK
VYLALGSNLGDRLANLRAALRALAALPGIEILAVSPLYETAPVGFTDQPDFLNAVVELETSLSPLELLDA
LQAIEQRLGRVRKERWGPRTLDLDILLYGDEVIDTPDLTLPHPRMHERAFVLVPLAEI
>gnl|CDD|238270 cd00484, PEPCK_ATP, Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates toward gluconeogenesis. It catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate to yield phosphoenolpyruvate and carbon dioxide, using a nucleotide molecule (ATP) for the phosphoryl transfer, and has a strict requirement for divalent metal ions for activity. PEPCK's separate into two phylogenetic groups based on their nucleotide substrate specificity, this model describes the ATP-dependent groups
THIHHNLSPAELYEEALKRGEGVLTSTGALAVDTGKKTGRSPKDKFIVDEPSSEDDIWWGKVNQPISEET
FEILRERAVDYLNTKKLFVFDGFAGADPEYRLKVRVITERAWHALFMRNMFIRPTEEELENFGPDFTIYN
APKFKANPETDGMNSETFVIINFAEREMVIGGTEYAGEMKKGIFSVMNYLLPKKGVLSMHCSANVGKKGD
VALFFGLSGTGKTTLSADPNRKLIGDDEHGWSDRGVFNIEGGCYAKCINLSEEKEPEIYNAIKFGAVLEN
VVVDEETREVDYDDDSITENTRAAYPIEHIPNAVIPGVGGHPKNIIFLTADAFGVLPPVSKLTPEQAMYH
FLSGYTAKVAGTERGITEPTATFSACFGAPFLPLHPTVYAEMLGEKIKKHGAKVWLVNTGWTGGSYGVGK
RIPLKYTRAIIDAILSGELNNAEYEKDPVFNLAIPTSIPGVPSEILNPRNTWADKEAYDETAKKLAKLFI
ENFKKFADKVSEEIAAAG
>gnl|CDD|238271 cd00487, Pep_deformylase, Polypeptide or peptide deformylase; a family of metalloenzymes that catalyzes the removal of the N-terminal formyl group in a growing polypeptide chain following translation initiation during protein synthesis in prokaryotes. These enzymes utilize Fe(II) as the catalytic metal ion, which can be replaced with a nickel or cobalt ion with no loss of activity. There are two types of peptide deformylases, types I and II, which differ in structure only in the outer surface of the domain. Because these enzymes are essential only in prokaryotes (although eukaryotic gene sequences have been found), they are a target for a new class of antibacterial agents
IVQYPDPVLRKKAKPVEEFDDELKQLIDDMFETMYAAPGVGLAAPQIGVSKRIFVIDVPDEENKEPPLVL
INPEIIESSGETEYGEEGCLSVPGYRGEVERPKKVTVRYLDEDGNPIELEAEGFLARCIQHEIDHLNGIL
F
>gnl|CDD|238272 cd00488, PCD_DCoH, PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known as DCoH (dimerization cofactor of hepatocyte nuclear factor-1), is both a transcription activator and a metabolic enzyme. DCoH stimulates gene expression by associating with specific DNA binding proteins such as HNF-1alpha (hepatocyte nuclear factor-1) and Xenopus enhancer of rudimentary homologue (XERH). DCoH also catalyzes the dehydration of 4alpha- hydroxy- tetrahydrobiopterin (4alpha-OH-BH4) to quinoiddihydrobiopterin, a percursor of the phenylalanine hydroxylase cofactor BH4 (tetrahydrobiopterin). The DCoH homodimer has a saddle-shaped structure similar to that of TBP (TATA binding protein). Two DCoH proteins have been identifed in humans: DCoH1 and DCoH2. Mutations in human DCoH1 cause hyperphenylalaninemia. Loss of enzymic activity of DCoH in humans is associated with the depigmentation disorder vitiligo. DCoH1 has been reported to be overexpessed in colon cancer carcinomas and in malignant melanomas
GWELADGDALERTFKFKDFKEAIAFVNRVAELAEALNHHPDISNVYNKVTVTLTTHDAGGLTENDFILAA
KIDAL
>gnl|CDD|238273 cd00489, Barstar_like, Barstar is an intracellular inhibitor of barnase, an extracellular ribonuclease of Bacillus amyloliquefaciens. Barstar binds tightly to the barnase active site and sterically blocks it, thus inhibiting its potentially lethal RNase activity inside the cell. Barstar also binds and inhibits a ribonuclease called RNase Sa (produced by Streptomyces aureofaciens) which belongs to the same enzyme family as does barnase
VVIDGEDIADWEDFHARLKKKLGFPDYYGHNLDALWDCLTGLVEEPLVLRWRNLEHLKRLTPEDAESVLQ
CFRDVAREPAEANRE
>gnl|CDD|119402 cd00490, Met_repressor_MetJ, Met Repressor, MetJ. MetJ is a bacterial regulatory protein that uses S-adenosylmethionine (SAM) as a corepressor to regulate the production of Methionine. MetJ binds arrays of two to five adjacent copies of an eight base-pair 'metbox' sequence. MetJ forms sufficiently strong interactions with the sugar-phosphate backbone to accomodate sequence variation in natural operators. However, it is very sensitive to particular base changes in the operator. MetJ exists as a homodimer
AEWNGEYISPYAEHGKKSEQVKKITVSIPLKVLKILTDERTRRQVNNLRHATNSELLCEAFLHAFTGQPL
PDDADLRKERSDEIPEAAKELMREMGIEPETWE
>gnl|CDD|238274 cd00491, 4Oxalocrotonate_Tautomerase, 4-Oxalocrotonate Tautomerase: Catalyzes the isomerization of unsaturated ketones. The structure is a homohexamer that is arranged as a trimer of dimers. The hexamer contains six active sites, each formed by residues from three monomers, two from one dimer and the third from a neighboring monomer. Each monomer is a beta-alpha-beta fold with two small beta strands at the C-terminus that fold back on themselves. A pair of monomers form a dimer with two-fold symmetry, consisting of a 4-stranded beta sheet with two helices on one side and two additional small beta strands at each end. The dimers are assembled around a 3-fold axis of rotation to form a hexamer, with the short beta strands from each dimer contacting the neighboring dimers
PFVQIYILEGRTDEQKRELIERVTEAVSEILGAPEATIVVIIDEMPKENWGIGGESAS
>gnl|CDD|238275 cd00493, FabA_FabZ, FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct enzyme types of the dissociative, type II, fatty acid synthase system (found in bacteria and plants) required to complete successive cycles of fatty acid elongation. The third step of the elongation cycle, the dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP, is catalyzed by FabA or FabZ. FabA is bifunctional and catalyzes an additional isomerization reaction of trans-2-acyl-ACP to cis-3-acyl-ACP, an essential reaction to unsaturated fatty acid synthesis. FabZ is the primary dehydratase that participates in the elongation cycles of saturated as well as unsaturated fatty acid biosynthesis, whereas FabA is more active in the dehydration of beta-hydroxydecanoyl-ACP. The FabA structure is homodimeric with two independent active sites located at the dimer interface
PHRYPMLLVDRVLEIDPGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKGN
PPRLGYLAGVRKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAAA
>gnl|CDD|270213 cd00494, PBP2_HMBS, Hydroxymethylbilane synthase possesses the type 2 periplasmic binding protein fold. Hydroxymethylbilane synthase (HMBS), also known as porphobilinogen deaminase (PBGD), is an intermediate enzyme in the biosynthetic pathway of tetrapyrrolic ring systems, such as heme, chlorophyll, vitamin B12 and related macrocycles. HMBS catalyzes the conversion of porphobilinogen (PBG) into hydroxymethylbilane (HMB). This family includes the three domains of HMBS. The enzyme is believed to bind substrate through a hinge-bending motion of domains 1 and 2. The C-terminal domain 3 contains an invariant cysteine that forms the covalent attachment site for the DPM (dipyrromethane) cofactor. HMBS is found in all organisms except viruses. The domains 1 and 2 have the same overall topology as found in the type 2 periplasmic-binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor
PLRIGTRGSPLALAQAEEVRATLRAAHPGLELEIVPIKTTGDKILDTPLAKVGGKGLFTKELDEALLEGE
ADIAVHSLKDLPTELPPGLVLAAILPREDPRDALVSPDNLTLDELPAGARVGTSSLRRRAQLLHLRPDLE
VVPIRGNVETRLAKLDNGEIDAIVLAAAGLKRLGLEDRIARILSPDEMLPAPGQGALAIEVREDDDKTVD
LLAALDDPESRLEVTAERAFLATLEGGCRVPIAAYATLDGDELTLRALVLSLDGSEFIRETRTG
>gnl|CDD|198379 cd00495, Ribosomal_L25_TL5_CTC, Ribosomal L25/TL5/CTC N-terminal 5S rRNA binding domain. L25 is a single-domain protein, homologous to the N-terminal domain of TL5 and CTC. CTC is a known stress protein, and proteins of this family are believed to have two functions, acting as both ribosomal and stress proteins. In Escherichia coli, cells deleted for L25 were found to be viable; however, these cells grew slowly and had impaired protein synthesis capability. In Bacillus subtilis, CTC is induced under stress conditions and located in the ribosome; it has been proposed that CTC may be necessary for accurate translation under stress conditions. Ribosomal_L25_TL5_CTC is mostly found in bacteria, with a few exceptions such as plants or stramenopiles. Due to its limited taxonomic diversity and the viability of cells deleted for L25, this protein is not believed to be necessary for ribosomal assembly. Eukaryotes contain a protein called L25, which is not homologous to bacterial L25, but rather to bacterial L23
TLKAEKREETGKGAARRLRREGKVPAVIYGKGEEPIPISVDAKELEKLLRKEGENTVIELEIDGKKENVL
IKDVQRHPVKDEILHVDFLR
>gnl|CDD|238277 cd00496, PheRS_alpha_core, Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH ribose of the appropriate tRNA, PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. PheRS is an alpha-2/ beta-2 tetramer
HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYINDPARLLLRTHTSAVQ
ARALAKLKPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRF
RPSYFPFTEPSFEVDVYCPGCLGWLEILGCGMVRPEVLENAGIDEEYSGFAFGIGLERLAMLKYGIPDIR
LFYSNDLR
>gnl|CDD|211322 cd00497, PseudoU_synth_TruA_like, Pseudouridine synthase, TruA family. This group consists of eukaryotic, bacterial and archeal pseudouridine synthases similar to Escherichia coli TruA, Saccharomyces cerevisiae Pus1p, S. cerevisiae Pus3p Caenorhabditis elegans Pus1p and human PUS1. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. S. cerevisiae PUS1 catalyzes the formation of psi34 and psi36 in the intron containing tRNAIle, psi35 in the intron containing tRNATyr, psi27 and/or psi28 in several yeast cytoplasmic tRNAs and, psi44 in U2 small nuclear RNA (U2 snRNA). The presence of the intron is required for the formation of psi 34, 35 and 36. In addition S. cerevisiae PUS1 makes psi 26, 65 and 67. C. elegans Pus1p does not modify psi44 in U2 snRNA. S. cerevisiae Pus3p makes psi38 and psi39 in tRNAs. Psi44 in U2 snRNA and, psi38 and psi39 in tRNAs are highly phylogenetically conserved. Psi 26,27,28,34,35,36,65 and 67 in tRNAs are less highly conserved. Mouse Pus1p regulates nuclear receptor activity through pseudouridylation of Steroid Receptor RNA Activator. Missense mutation in human PUS1 causes mitochondrial myopathy and sideroblastic anemia (MLASA)
FGYDGTKYHGFQRQNDVPTVEGELIIALLKAGNIPYFIKAAARTDRGVSALGQVVAIETERRLTPEALNG
ILPGDIRVFAVHSVPPDFHAPRYCDHRTYRYYIPSFPLDDERLKSAASRFLGTHDFTNFSKKDTRNTVRT
IISIECKDLNPFVVVEFKAKSFLWHQVRRMVGFLMLVGEGLHSPSSVSRLLAGPAPPIPMVPAPAEGLLL
VDVKY
>gnl|CDD|238278 cd00498, Hsp33, Heat shock protein 33 (Hsp33): Cytosolic protein that acts as a molecular chaperone under oxidative conditions. In normal (reducing) cytosolic conditions, four conserved Cys residues are coordinated by a Zn ion. Under oxidative stress (such as heat shock), the Cys are reversibly oxidized to disulfide bonds, which causes the chaperone activity to be turned on. Hsp33 is homodimeric in its functional form
LVRFIADDGDVRGEAVRLTETVQEALRRHDYPPTATALLGRTLVAAALLGASLKFDGRLTVQIQGDGPVG
LIVADADADGTVRGYVRNPEVDLPLNEDGKLDVGDAVGNGYLAVTKDLGLGEPYQGVVPLVSGEIAEDLE
YYFAQSEQLPSAVGLGVLVNPDGTVKAAGGLLLQVLPGADEEDIDAWEKVIKLMPTVSALELLGLSPEEL
LYRLFHEEEVRILEKQPVRFRCDCSRERVAAALLTLGKEELADMIEEDGGIEVTCEFCGEKYHFD
>gnl|CDD|238279 cd00501, Peptidase_C15, Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: Enzymes responsible for cleaving pyroglutamate (pGlu) from the N-terminal end of specialized proteins. The N-terminal pGlu protects these proteins from proteolysis by other proteases until the pGlu is removed by a PGP. PGPs are cysteine proteases with a Cys-His-Glu/Asp catalytic triad. Type I PGPs are found in a wide variety of prokaryotes and eukaryotes. It is not clear whether the functional form is a monomer, a homodimer, or a homotetramer
KKVLVTGFGPFGGEPVNPSWEAVKELPKLILGGAEVVGLELPVVFQKAVEVLPELIEEHKPDLVIHVGLA
GGRSTITIERVAINIDDARIPDNEGNQPIDEPIVPGGPAAYFSTLPVKAIVKALREAGIPARVSNDAGTY
LCNHVYYGSLHESATRGPFIRAGFIHVPYSPEQVADKGAPSMSLETILRALEAA
>gnl|CDD|188633 cd00502, DHQase_I, Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase). Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase). Catalyzes the cis-dehydration of 3-dehydroquinate via a covalent imine intermediate to produce dehydroshikimate. Dehydroquinase is the third enzyme in the shikimate pathway, which is involved in the biosynthesis of aromatic amino acids. Type I DHQase exists as a homodimer. Type II 3-dehydroquinase also catalyzes the same overall reaction, but is unrelated in terms of sequence and structure, and utilizes a completely different reaction mechanism
KICVPLTGPDLLEEALSLLELLLGADAVELRVDLLEDPSIDDVAEQLSLLRELTPLPIIFTVRTKSEGGN
FEGSEEEYLELLEEALKLGPDYVDIELDSALLEELINSRKKGNTKIIGSYHDFSGTPSDEELVSRLEKMA
ALGADIVKIAVMANSIEDNLRLLKFTRQVKNLYDIPLIAINMGELGKLSRILSPVFGSPLTYASLPEPSA
PGQLSVEELKQALSL
>gnl|CDD|238280 cd00503, Frataxin, Frataxin is a nuclear-encoded mitochondrial protein implicated in Friedreich's ataxia (FRDA), an human autosomal recessive neurodegenerative disease; Frataxin is found in eukaryotes and in purple bacteria; lack of frataxin causes iron to accumulate in the mitochondrial matrix suggesting that frataxin is involved in mitochondrial iron homeostasis and possibly in iron transport; the domain has an alpha-beta fold consisting of two helices flanking an antiparallel beta sheet
MNESEFHRLADDLLLKIEDTLEEQDDDADIDVETQGGVLTLTFGNGSTIVINRQEPLRQIWLASKVGGYH
FDYKNGKWICTRSGEELWELLEEECSAQSGEDVEF
>gnl|CDD|238281 cd00504, GXGXG, GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit (gltB) of glutamate synthase (GltS), in subunit C of tungsten formylmethanofuran dehydrogenase (FwdC) and in subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC). It is also found in a primarily archeal group of proteins predicted to encode part of the large subunit of GltS. It is characterized by a repeated GXXGXXXG motif. GltS is a complex iron-sulfur flavoprotein that catalyzes the synthesis of L-glutamate from L-glutamine and 2-oxoglutarate. It requires the transfer of ammonia and electrons among three distinct active centers that carry out L-Gln hydrolysis, conversion of 2-oxoglutarate into L-Glu, and electron uptake from a donor. These catalytic sites occur in other domains within the protein or or encoded by separate genes, and are not present in the domain in this CD. FwdC and FmdC are reversible ion pumps that catalyze the formylation and deformylation of methanofuran in hyperthermophiles and bacteria. They require the presence of either tungstun (FwdC) or molybdenum (FmdC). The specific function of this domain also remains unidentified in the formylmethanofuran dehydrogenases
RAVGTRGSRYIGKRPGLPEDTVEIIINGSAGQSFGAFMAGGTITVEGNANDYVGKGMSGGEIVIHPPAGD
ENGIAGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDDFGGEYMTGGTIVVLGDAGRNFGAGM
SGGVIYVRG
>gnl|CDD|132996 cd00505, Glyco_transf_8, Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+
IAIVIVATGDEYLRGAIVLMKSVLRHRTKPLRFHVLTNPLSDTFKAALDNLRKLYNFNYELIPVDILDSV
DSEHLKRPIKIVTLTKLHLPNLVPDYDKILYVDADILVLTDIDELWDTPLGGQELAAAPDPGDRREGKYY
RQKRSHLAGPDYFNSGVFVVNLSKERRNQLLKVALEKWLQSLSSLSGGDQDLLNTFFKQVPFIVKSLPCI
WNVRLTGCYRSLNCFKAFVKNAKVIHFNGPTKPWNK
>gnl|CDD|211323 cd00506, PseudoU_synth_TruB_like, Pseudouridine synthase, TruB family. This group consists of eukaryotic, bacterial and archeal pseudouridine synthases similar to Escherichia coli TruB, Saccharomyces cerevisiae Pus4, M. tuberculosis TruB, S. cerevisiae Cbf5 and human dyskerin. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E. coli TruB, M. tuberculosis TruB and S. cerevisiae Pus4, make psi55 in the T loop of tRNAs. Pus4 catalyses the formation of psi55 in both cytoplasmic and mitochondrial tRNAs. Psi55 is almost universally conserved. S. cerevisiae Cbf5 and human dyskerin are nucleolar proteins that, with the help of guide RNAs, make the hundreds of psueudouridnes present in rRNA and small nuclear RNAs (snRNAs). Cbf5/Dyskerin is the catalytic subunit of eukaryotic box H/ACA small nucleolar ribonucleoprotein (snoRNP) particles. Mutations in human dyskerin cause X-linked dyskeratosis congenitas
GLFAVDKPQGPSSHDVVDTIRRIFLAEKVGHGGTLDPFATGVLVVGIGKATKLLKHLLAATKDYTAIGRL
GQATDTFDATGQVIEETPYDHITHEQLERALETLTGDIQQVPPLYSAVKRQGQRAYELARRGLLVPDEAR
PPTIYELLCIRFNPPHFLLEVEVVCETGTYIRTLIHDLGLELGVGAHVTELRRTRVGPFKVENAVTLHHL
>gnl|CDD|238282 cd00508, MopB_CT_Fdh-Nap-like, This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
EEYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARV
TDRVRPGTVFMPFHWGGEVSGGAANALTNDALDPVSGQPEFKACAVRIEK
>gnl|CDD|238283 cd00512, MM_CoA_mutase, Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM)-like family; contains proteins similar to MCM, and the large subunit of Streptomyces coenzyme B12-dependent isobutyryl-CoA mutase (ICM). MCM catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA. The reaction proceeds via radical intermediates beginning with a substrate-induced homolytic cleavage of the Co-C bond of coenzyme B12 to produce cob(II)alamin and the deoxyadenosyl radical. MCM plays an important role in the conversion of propionyl-CoA to succinyl-CoA during the degradation of propionate for the Krebs cycle. In higher animals, MCM is involved in the breakdown of odd-chain fatty acids, several amino acids, and cholesterol. Methylobacterium extorquens MCM participates in the glyoxylate regeneration pathway. In M. extorquens, MCM forms a complex with MeaB; MeaB may protect MCM from irreversible inactivation. In some bacteria, MCM is involved in the reverse metabolic reaction, the rearrangement of succinyl-CoA to methylmalonyl-CoA. Examples include Propionbacterium shermanni MCM during propionic acid fermentation, E.coli MCM in a pathway for the conversion of succinate to propionate and Streptomyces MCM in polyketide biosynthesis. P. shermanni and Streptomyces cinnamonensis MCMs are alpha/beta heterodimers, with both subunits being homologous members of this family. It has been shown for P. shermanni MCM that only the alpha subunit binds coenzyme B12 and substrates. Human MCM is a homodimer with two active sites. Mouse and E.coli MCMs are also homodimers. ICM from S. cinnamonensis is comprised of a large and a small subunit. The holoenzyme appears to be an alpha2beta2 heterotetramer with up to 2 molecules of coenzyme B12 bound. The small subunit binds coenzyme B12. ICM catalyzes the reversible rearrangement of n-butyryl-CoA to isobutyryl-CoA (intermediates in fatty acid and valine catabolism, which in S. cinnamonensis can be converted to methylmalonyl-CoA and used in polyketide synthesis). In humans, impaired activity of MCM results in methylmalonic aciduria, a disorder of propionic acid metabolism
PWTQRQLAGFGTAEETNKRYRRNLAAGQTGLSVAFDLPTLRGYDSDNPRDAGEVGMCGVAIDTLEDMDEL
FQGIPLEQTSVSMTINGPALPALALYVVVAERQGVDASDLAGTLQNDIIKEYIAQGTYIFPPEPSLRVLG
DIIEYCSANIPKWNPVSISGYHMQEAGATPVQELAYTLATGIEYVRACLERGLDVDEFAPRLSFFFGIGM
NFFEEIAKLRAARRIWARITRDFGGAEPKSRRLRYHVQTSGRSLTAQQPYNNVARTSIQAMAATLGGAQS
LHTNAYDEAIGLPTEFSARIALRTQQVLAEESGLARVIDPLGGSYYVEELTDSLEDAAWKEFQEIEKRGG
MLKAVETGYVKGVIDESAAERQARIESGKQPIVGVNKYRMEEAPPIEPK
>gnl|CDD|238284 cd00513, Ribosomal_L32_L32e, Ribosomal_L32_L32e: L32 is a protein from the large subunit that contains a surface-exposed globular domain and a finger-like projection that extends into the RNA core to stabilize the tertiary structure. L32 does not appear to play a role in forming the A (aminacyl), P (peptidyl) or E (exit) sites of the ribosome, but does interact with 23S rRNA, which has a "kink-turn" secondary structure motif. L32 is overexpressed in human prostate cancer and has been identified as a stably expressed housekeeping gene in macrophages of human chronic obstructive pulmonary disease (COPD) patients. In Schizosaccharomyces pombe, L32 has also been suggested to play a role as a transcriptional regulator in the nucleus. Found in archaea and eukaryotes, this protein is known as L32 in eukaryotes and L32e in archaea
KKFKRHQSDRYKRLGDSWRKPRGIDNKVRRRFKGKPAMPKIGYGSPKKTRGLHPSGFKKVLVHNVKELEV
LDMHNRTYAARIAHTVGARKRKEIVERAKELGIKVLN
>gnl|CDD|238285 cd00515, HAM1, NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ inosine triphosphatase. HAM1 protects the cell against mutagenesis by the base analog 6-N-hydroxylaminopurine (HAP) in E. Coli and S. cerevisiae. A Ham1-related protein from Methanococcus jannaschii is a novel NTPase that has been shown to hydrolyze nonstandard nucleotides such as XTP to XMP and ITP to IMP, but not the standard nucleotides, in the presence of Mg or Mn ions. The enzyme exists as a homodimer. The HAM1 protein may be acting as an NTPase by hydrolyzing the HAP triphosphate
IVFATGNKGKLKEFKEILAPFGIEVVSLKDIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVD
ALNGFPGVYSARFAGEHDDAENNEKLLELLEGDEDRSAYFVCVIALVDPDGEPLVFEGEVEGKIVTEPRG
TGGFGYDPIFIPEGYGKTFAEMSPEEKNAISHRGKALRKLKEF
>gnl|CDD|238286 cd00516, PRTase_typeII, Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an important role in NAD production by either allowing quinolinic acid (QA), quinolinate phosphoribosyl transferase (QAPRTase), or nicotinic acid (NA), nicotinate phosphoribosyltransferase (NAPRTase), to be used in the synthesis of NAD. QAPRTase catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide, an important step in the de novo synthesis of NAD. NAPRTase catalyses a similar reaction leading to NAMN and pyrophosphate, using nicotinic acid an PPRP as substrates, used in the NAD salvage pathway
DLYKLTMIQAYPPPDTRATAEFTAREDPYGVLAGLEEALELLELLRFPGPLVILAVPEGTVVEPGEPLLT
IEGPARELLLLERVLLNLLQRLSGIATATARYVEAAKGANTKVHDFGTRKTTPGLRLLEKYAVLIGGGDG
HRNGLSDAILIKDNHGTMAHSIIQAFGELAAVKALRRWLPELFIALIDVEVDTLEEALEAAKAGGADGIR
LDSGSPEELDPAVLILKARAHLDGKGLPRVKIEASGGLDEENIRAYAETGVDVFGVGTLLHSAPPLDIVL
K
>gnl|CDD|173895 cd00517, ATPS, ATP-sulfurylase. ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, catalyzes the transfer of an adenylyl group from ATP to sulfate, forming adenosine 5'-phosphosulfate (APS). This reaction is generally accompanied by a further reaction, catalyzed by APS kinase, in which APS is phosphorylated to yield 3'-phospho-APS (PAPS). In some organisms the APS kinase is a separate protein, while in others it is incorporated with ATP sulfurylase in a bifunctional enzyme that catalyzes both reactions. In bifunctional proteins, the domain that performs the kinase activity can be attached at the N-terminal end of the sulfurylase unit or at the C-terminal end, depending on the organism. While the reaction is ubiquitous among organisms, the physiological role of the reaction varies. In some organisms it is used to generate APS from sulfate and ATP, while in others it proceeds in the opposite direction to generate ATP from APS and pyrophosphate. ATP sulfurylase can be a monomer, a homodimer, or a homo-oligomer, depending on the organism. ATPS belongs to a large superfamily of nucleotidyltransferases that includes pantothenate synthetase (PanC), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain
LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDGTLWPIPIVLDVSEEDAKRLKEGER
VALRYPGQPLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPDFDQY
RLTPAELRALFKERGWRRVVAFQTRNPMHRAHEELMKRAAEKLLNDGLLLHPLVGWTKPGDVPDEVRMRA
YEALLEEYYLPERTVLAILPLPMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEI
FKKLAPELGIEPVPFREAAYCPKCDGMASEDTCPHGEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVL
REY
>gnl|CDD|99872 cd00518, H2MP, Hydrogenase specific C-terminal endopeptidases, also called Hydrogen Maturation Proteases (H2MP). These enzymes belong to the peptidase family M52. Maturation of [FeNi] hydrogenases includes formation of the nickel metallocenter, proteolytic processing and assembly with other subunits. Hydrogenase maturation endopeptidases are responsible for the proteolytic processing, liberating a short C-terminal peptide by cleaving after a His or an Arg residue, e.g., HycI (E. coli) is involved in processing of HypE, the large subunit of hydrogenase 3. This cleavage is nickel dependent. This CD also includes such hydrogenase-processing proteins as HydD, HupW, and HoxW, as well as, proteins of the F420-reducing hydrogenase of methanogens (e.g., FrcD). Also included, is the Pyrococcus furiosus FrxA protein, a bifunctional endopeptidase/ sulfhydrogenase found in NADP-reducing hyperthermophiles.The Pyrococcus FrxA is not related to those found in Helicobacter pylori
LVLGIGNPLRGDDGFGPAVAERLEERYLPPGVEVIDGGTLGLELLDLLEGADRVIIVDAVDSGGEPGTVR
RLEPEELPAYLSALSTHQLGLAELLALLRLLGGLPPEVVLIGIQPESLELGEGLSPEVAAAVPKAVELI
>gnl|CDD|238287 cd00519, Lipase_3, Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site
DYEKLKYYAKLAAAAYCVDANILAKAVVFADIALLNVFSPDKLLKTDKQYDTQGYVAVDHDRKTIVIAFR
GTVSLADWLTDLDFSPVPLDPPLCSGGKVHSGFYSAYKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGA
LASLLALDLRLRGPGSDVTVYTFGQPRVGNAAFAEYLESTKGRVYRVVHGNDIVPRLPPGSLTPPEGYTH
VGTEVWIDHLPYFYIDALC
>gnl|CDD|238288 cd00520, RRF, Ribosome recycling factor (RRF). Ribosome recycling factor dissociates the posttermination complex, composed of the ribosome, deacylated tRNA, and mRNA, after termination of translation. Thus ribosomes are "recycled" and ready for another round of protein synthesis. RRF is believed to bind the ribosome at the A-site in a manner that mimics tRNA, but the specific mechanisms remain unclear. RRF is essential for bacterial growth. It is not necessary for cell growth in archaea or eukaryotes, but is found in mitochondria or chloroplasts of some eukaryotic species
ILKEAKEKMEKSLEALKEELNKIRTGRANPALLDSITVEYYGAPTPLNQLASISVPEPRTIVINPFDKSA
IKAIEKAILNSDLGLNPNNDGAVIRVNLPPLTEERRKELVKDAKKIAEEAKVAIRNIRRDANDKIKKLEK
EKEISEDEVKKAEEDLQKLTDEYIKKIDELLKSKEKELL
>gnl|CDD|213981 cd00522, Hemerythrin-like, Hemerythrin family. Hemerythrin (Hr) and related proteins are found in bacteria, archaea and eukaryotes. They are non-heme diiron oxygen transport proteins. In addition to oxygen transport, members are involved in cadmium fixation and host anti-bacterial defense. They have the same "four alpha helix bundle" motif and similar active site structures. Some members, like Hr, form oligomers, the octameric form being most prevalent, while others are monomeric
DVFDDEHWRLFQLVFLYCDKLSKAQSLYATFKEFKXHFQIENEYMIGLLQQRSQTIYNVHSDNHLSFXLS
LFEKGLKQLKERLEAFTRWLVNHIKSEDFEYKG
>gnl|CDD|411703 cd00523, Holliday_junction_resolvase, Holliday junction resolvase. Holliday junction resolvases (HJRs) are endonucleases that specifically resolve Holliday junction DNA intermediates during homologous recombination. HJRs occur in archaea, bacteria, and in the mitochondria of certain eukaryotes; however, this CD includes only the archeal HJRs. The bacterial and archeal HJRs perform a similar function but differ in both sequence and structure. Structural similarity does however, exist between the archeal HJRs and type II restriction endonucleases, such as EcoRV, BglII, and Fok, and this similarity includes their active site configurations
MKRKGSRFERELVKLLWEKGFAVVRVAGSGSSPRPLPDIVAGNGGKYLAIEVKSTKKDKIYIDREQVEKL
LEFARRFGAEPYIAVKFPRKGWRFIPPEKLERTEKGYKIDEIARSDGIDLEELAGA
>gnl|CDD|238290 cd00524, SORL, Superoxide reductase-like (SORL) domain; present in a family of mononuclear non-heme iron proteins that includes superoxide reductase and desulfoferrodoxin. Superoxide reductase-like proteins scavenge superoxide anion radicals as a defense mechanism against reactive oxygen species and are found in anaerobic bacteria and archeae, and microaerophilic Treponema pallidum. The SORL domain contains an active iron site, Fe[His4Cys(Glu)], which in the reduced state loses the glutamate ligand. Superoxide reductase (class II) forms a homotetramer with four Fe[His4Cys(Glu)] centers. Desulfoferrodoxin (class I) is a homodimeric protein, with each protomer comprised of two domains, the N-terminal desulforedoxin (DSRD) domain and C-terminal SORL domain. Each domain has a distinct iron center: the DSRD iron center I, Fe(S-Cys)4; and the SORL iron center II, Fe[His4Cys(Glu)]
EEKHVPVIEKPDSVEPFDVKVKVGSVPHPMTEEHYIEWIELYFGDEKVGRVELTPGTKPEATFTVKAPKK
GKLVALSYCNLHGLWE
>gnl|CDD|238291 cd00525, AE_Prim_S_like, AE_Prim_S_like: primase domain similar to that found in the small subunit of archaeal and eukaryotic (A/E) DNA primases. The replication machineries of A/Es are distinct from that of bacteria. Primases are DNA-dependent RNA polymerases which synthesis the short RNA primers required for DNA replication. In eukaryotes, this small catalytically active primase subunit (p50) and a larger primase subunit (p60), referred to jointly as the core primase, associate with the B subunit and the DNA polymerase alpha subunit in a complex, called Pol alpha-pri. In addition to its catalytic role in replication, eukaryotic DNA primase may play a role in coupling replication to DNA damage repair and in checkpoint control during S phase. Pfu41 and Pfu46 comprise the primase complex of the archaea Pyrococcus furiosus; these proteins have sequence identity to the eukaryotic p50 and p60 primase proteins respectively. Pfu41 preferentially uses dNTPs as substrate. Pfu46 regulates the primase activity of Pfu41. Also found in this group is the primase-polymerase (primpol) domain of replicases from archaeal plasmids including the ORF904 protein of pRN1 from Sulfolobus islandicus (pRN1 primpol). The pRN1 primpol domain exhibits DNA polymerase and primase activities; a cluster of active site residues (three acidic residues, and a histidine) is required for both these activities. The pRN1 primpol primase activity prefers dNTPs to rNTPs; however incorporation of dNTPs requires rNTP as cofactor. This group also includes the Pol domain of bacterial LigD proteins such Mycobacterium tuberculosis (Mt)LigD. MtLigD contains an N-terminal Pol domain, a central phosphoesterase module, and a C-terminal ligase domain. LigD Pol plays a role in non-homologous end joining (NHEJ)-mediated repair of DNA double-strand breaks (DSB) in vivo, perhaps by filling in short 5'-overhangs with ribonucleotides; the filled in termini would be sealed by the associated LigD ligase domain. The MtLigD Pol domain is stimulated by manganese, is error-prone, and prefers adding rNTPs to dNTPs in vitro
RPVSPIRPPGKGPFQRHWPFGATTDDAEILAWLANLPPGNIGLSLGRYDKLWKPDLLVFDLDPDDYDCWE
DVKEAALLLRELLDEDGLNTLVVTSGSRGLHVYVRLIDIRVNARGRLLVAPPSVHPRPGGPPSWPL
>gnl|CDD|238292 cd00527, IF6, Ribosome anti-association factor IF6 binds the large ribosomal subunit and prevents the two subunits from associating during translation initiation. IF6 comprises a family of translation factors that includes both eukaryotic (eIF6) and archeal (aIF6) members. All members of this family have a conserved pentameric fold referred to as a beta/alpha propeller. The eukaryotic IF6 members have a moderately conserved C-terminal extension which is not required for ribosomal binding, and may have an alternative function
AIRLSFEGSPNIGVFAKATNSYCLVPPGGDENFVSKFEEELGVPVVRTTIGGSRLVGSLTVGNSNGLLLP
HTTTDQELQHIRNSLPDEVGVLRVKENLSALGNVILCNDHGALVHPDLSKEAEEIIEDVLGVEVFRGTIA
GIKTVGSAGVLTNKGGLVHPKTSDEELEELSELFKVPVVAGTVNFGSQYVGAGLVANSKGAVVGSDTTGP
ELSRIEDALG
>gnl|CDD|238293 cd00528, MoaC, MoaC family. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, an essential cofactor of a diverse group of redox enzymes. MoaC, a small hexameric protein, converts, together with MoaA, a guanosine derivative to the precursor Z by inserting the carbon-8 of the purine between the 2' and 3' ribose carbon atoms, which is the first of three phases of Moco biosynthesis
MVDVSDKAVTERTAVAEGRVRLSPETLDLIREGQLPKGDVLAVARIAGIMAAKRTSELIPLCHPLPLTGV
DVDFELDEDTSGVRIRATVRTTGKTGVEMEALTAVSVAALTIYDMCKAVDKDMVIENIRLLEKSGG
>gnl|CDD|438561 cd00529, RuvC-like, Crossover junction endodeoxyribonuclease RuvC and similar proteins. The RuvC-like family consists of bacterial RuvC, fungal Cruciform cutting endonuclease 1 (CCE1), bacterial YqgF and monokaryotic chloroplast 1 protein (MOC1). RuvC, CCE1 and MOC1 are Holliday junction resolvases (HJRs), endonucleases that specifically resolve Holliday junction DNA intermediates during homologous recombination. RuvC is part of the RuvABC pathway in Escherichia coli and other Gram-negative bacteria that is involved in processing Holliday junctions, which are formed by the reciprocal exchange of strands between two DNA duplexes. CCE1 is a HJR specific for 4-way junctions; it is involved in the maintenance of mitochondrial DNA. Escherichia coli YqgF has been shown to act as a pre-16S rRNA nuclease, presumably as a monomer. It is involved in the processing of pre-16S rRNA during ribosome maturation. HJRs occur in archaea, bacteria, and in the mitochondria of certain fungi. RuvC and its orthologs are homodimers and display structural similarity to RNase H and Hsp70
VLGIDPGTKSLGLAVLSQNGVTALQVEVIKTLEVLVGPSRGRLDAARIVELLKEFQPDTIAVEQQFNYPG
TGGALRVGFARGMAIVIHVASGVPVVLYDDRADALLIAAG
>gnl|CDD|238295 cd00530, PTE, Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including the chemical warfare agents VX, soman, and sarin as well as the insecticide paraoxon. PTE exists as a homodimer with one active site per monomer. The active site is located next to a binuclear metal center, at the C-terminal end of a TIM alpha- beta barrel motif. The native enzyme contains two zinc ions at the active site however these can be replaced with other metals such as cobalt, cadmium, nickel or manganese and the enzyme remains active
GVTLTHEHLIIDSSGFVRDPPEVDDFDLADVEAAKEELKRFRAHGGRTIVDATPPGIGRDVEKLAEVARA
TGVNIVAATGFYKDAFYPEWVRLRSVEELTDMLIREIEEGIEGTGIKAGIIKEAGGSPAITPLEEKVLRA
AARAQKETGVPISTHTQAGLTMGLEQLRILEEEGVDPSKVVIGHLDRNDDPDYLLKIAALGAYLEFDGIG
KDKIFGYPSDETRADAVKALIDEGYGDRLLLSHDVFRKSYLEKRYGGHGYDYILTRFIPRLRERGVTEEQ
LDTILVENPARFL
>gnl|CDD|238296 cd00531, NTF2_like, Nuclear transport factor 2 (NTF2-like) superfamily. This family includes members of the NTF2 family, Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases, and the beta subunit of Ring hydroxylating dioxygenases. This family is a classic example of divergent evolution wherein the proteins have many common structural details but diverge greatly in their function. For example, nuclear transport factor 2 (NTF2) mediates the nuclear import of RanGDP and binds to both RanGDP and FxFG repeat-containing nucleoporins while Ketosteroid isomerases catalyze the isomerization of delta-5-3-ketosteroid to delta-4-3-ketosteroid, by intramolecular transfer of the C4-beta proton to the C6-beta position. While the function of the beta sub-unit of the Ring hydroxylating dioxygenases is not known, Scytalone Dehydratases catalyzes two reactions in the biosynthetic pathway that produces fungal melanin. Members of the NTF2-like superfamily are widely distributed among bacteria, archaea and eukaryotes
AEQFLYRYARLLDAGDREWLALLYADDAYFEPPGGDGLIYPDDGREAIEDRVRRLPFGPSRTRHLVSNVD
VQPGDDGEGVVVSVFGVLRTRGDGEQDVFAGGQTFVLRPQGGGGKIANRRFRLD
>gnl|CDD|238297 cd00532, MGS-like, MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site
GVFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEDGEPTVDAAIAEKGKFD
VVINLRDPRRDRCTDEDGTALLRLARLYKIPVTTPNATAMFV
>gnl|CDD|238298 cd00534, DHNA_DHNTPE, Dihydroneopterin aldolase (DHNA) and 7,8-dihydroneopterin triphosphate epimerase domain (DHNTPE); these enzymes have been designated folB and folX, respectively. Folate derivatives are essential cofactors in the biosynthesis of purines, pyrimidines, and amino acids, as well as formyl-tRNA. Mammalian cells are able to utilize pre-formed folates after uptake by a carrier-mediated active transport system. Most microbes and plants lack this system and must synthesize folates de novo from guanosine triphosphate. One enzyme from this pathway is DHNA which catalyses the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate. Though it is known that DHNTPE catalyzes the epimerization of dihydroneopterin triphosphate to dihydromonapterin triphosphate, the biological role of this enzyme is still unclear. It is hypothesized that it is not an essential protein since a folX knockout in E. coli has a normal phenotype and the fact that folX is not present in H. influenza. In addition both enzymes have been shown to be able to compensate for the other's activity albeit at slower reaction rates. The functional enzyme for both is an octamer of identical subunits. Mammals lack many of the enzymes in the folate pathway including, DHNA and DHNTPE
MDRVFIKGLRFYTIHGVFEEERLLGQKFVVDLTLWYDLSKAGESDDLADTLNYAEVAKLIKKIVEGSPFK
LIETLAEEIADILLEDYPKVSAIKVKVEKPNAPIPASADGVGVEIERE
>gnl|CDD|238299 cd00537, MTHFR, Methylenetetrahydrofolate reductase (MTHFR). 5,10-Methylenetetrahydrofolate is reduced to 5-methyltetrahydrofolate by methylenetetrahydrofolate reductase, a cytoplasmic, NAD(P)-dependent enzyme. 5-methyltetrahydrofolate is utilized by methionine synthase to convert homocysteine to methionine. The enzymatic mechanism is a ping-pong bi-bi mechanism, in which NAD(P)+ release precedes the binding of methylenetetrahydrofolate and the acceptor is free FAD. The family includes the 5,10-methylenetetrahydrofolate reductase EC:1.7.99.5 from prokaryotes and methylenetetrahydrofolate reductase EC: 1.5.1.20 from eukaryotes. The bacterial enzyme is a homotetramer and NADH is the preferred reductant while the eukaryotic enzyme is a homodimer and NADPH is the preferred reductant. In humans, there are several clinically significant mutations in MTHFR that result in hyperhomocysteinemia, which is a risk factor for the development of cardiovascular disease
ISFEFFPPKTADGEENLEAAADLLGALDPDFVSVTDGAGGSTRDMTLLAAARILQEGGIEPIPHLTCRDR
NRIELQSILLGAHALGIRNILALRGDPPKGGDQPGAKPVGFVYAVDLVELIRKENGGGFSIGVAAYPEGH
PEAPSLEEDIKRLKRKVDAGADFIITQLFFDNDAFLRFVDRCRAAGITVPIIPGIMPLTSYKQAKRFAKL
CGVEIPDWLLERLEKLKDDAEAVRAEGIEIAAELCDELLEHGVPGIHFYTLNREEATAEILENL
>gnl|CDD|238300 cd00538, PA, PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2
DVILATTGYAGSALLFNPPSSPVGVVAGPLVGCGYGTTDDSGADVKGKIVLVRRGGCSFSEKVKNAQKAG
AKAVIIYNNGDDPGPQMGSVGLESTDPSIPTVGISYADGEALLSLLEAGKTVTVDL
>gnl|CDD|238301 cd00539, MCR_gamma, Methyl-coenzyme M reductase (MCR) gamma subunit. MCR catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea, in which methyl-coenzyme M and coenzyme B are converted to methane and the heterodisulfide of coenzyme M and coenzyme B (CoM-S-S-CoB). MCR is a dimer of trimers, each of which consists of one alpha, one beta, and one gamma subunit, with two identical active sites containing nickel porphinoid factor 430 (F430)
QYYPGETKIAQNRRKHMNPDYELEKLREISDEDLVKVLGHRAPGEEYKSVHPPLEEMDEPEDAVREMVEP
TEGAKAGDRVRYIQFTDSMYFAPAQPYDRARTYMWRYRGVDTGTLSGRQIIEARERDLEKIAKELLETEL
FDPARTGVRGATVHGHSLRLDEDGLMFDALRRYRLDEETGEVEYVKDQVGIPLDEPVDLGKPLPEEELKK
RTTIYRVDGVAMRDDEEAVEVVQRIHWLRTLGGFQP
>gnl|CDD|187726 cd00540, AAG, Alkyladenine DNA glycosylase catalyzes the first step in base excision repair. Alkyladenine DNA glycosylase (AAG), also known as 3-methyladenine DNA glycosylase, catalyzes the first step in base excision repair (BER) by cleaving damaged DNA bases within double-stranded DNA to produce an abasic site. AAG bends DNA by intercalating between the base pairs, causing the damaged base to flip out of the double helix and into the enzyme active site for cleavage. Although AAG represents one of six DNA glycosylase classes, it lacks the helix-hairpin-helix active site motif associated with other BER glycosylases and is structurally distinct from them
FFDRDALEVARELLGKVLVRRLPGGVLSGRIVETEAYLGPDDPASHAYRGRTTRREAMFGPPGTAYVYLI
YGMHHCLNVVTGPEGEPAAVLIRALEPLEGLDLMRRRRGKKRGRELTNGPGKLCQALGIDKSLNGLDLTD
PSGLWIEDGGERPPEEIVATPRIGIDYAGEAADKPWRFYVKGNPFVS
>gnl|CDD|238302 cd00541, OMPLA, The outer membrane phospholipase A (OMPLA) is an integral membrane enzyme that catalyses the hydrolysis of acylester bonds in phospholipids using calcium as a cofactor. The enzyme has a fold of transmembrane beta-barrels and is widespread among Gram-negative bacteria, both in pathogens and nonpathogens. In pathogenic bacteria such as Campylobacter coli and Helicobacter pylori OMPLA is involved in pathogenesis and virulence. In nonpathogenic bacteria the physiological function of OMPLA is less clear. The Escherichia coli enzyme is involved in the secretion of bacteriocins, antibacterial peptides that are produced in order to survive under starvation conditions. The enzyme activity of OMPLA is strictly regulated to prevent uncontrolled breakdown of the surrounding phospholipids. The activity of OMPLA can be induced by membrane perturbation and concurs with dimerization of the enzyme
FLLPPYDPNYLLPSYYSPMYFLTAYEAGNLDDTEAKFQLSFKYPLFEGLLGPNDDLYFGYTQTSLWQLYN
SDDSSPFRETNYEPELFYVYPTNYKLAGGTLRMLGLGYNHESNGRSGPLSRSWNRLYLRPGWEKGNLTLG
VRPWYRIPESDDDDNPDIADYRGYGDLKLAYGLGDHLFVLLLLRYNLRTNRGSVELDYTYPITGGLRLYV
QYFNGYGESLIDYNHRQTRIG
>gnl|CDD|238303 cd00542, Ntn_PVA, Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), catalyzes the hydrolysis of penicillin V to yield 6-amino penicillanic acid (6-APA), an important key intermediate of semisynthetic penicillins. PVA has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which PVA belongs. This nucleophilic cysteine is exposed by post-translational prossessing of the PVA precursor. PVA forms a homotetramer
CTSLTLSTKDGDHVFGRTMDFAFDLGSQIIIIPRGYEWTSRSQGKSYTTKYAFIGMGAVGDDYPLLFDGV
NEKGLAIAGLYFPGYASYSKETKEGKTNIAPFEFITWVLGNFASVEEVKEALKNINVVDDPINLLGPVPP
LHWIISDKSGRSIVVEPTKGGLKVYDNPVGVLTNSPDFDWHLTNLRNYINLSPEPPKNVKLGGVNLTAFG
QGSGTLGLPGDYTPPSRFVRAAYLKNYAPQPKDEEEAVNNAFHILNSVDIPKGAVITENGSSDYTQYTSV
MDLETGTYYYKTYDNNQIRAVDL
>gnl|CDD|410861 cd00544, CobU, Adenosylcobinamide kinase / adenosylcobinamide phosphate guanyltransferase (CobU). CobU is a bacterial bifunctional cobalbumin biosynthesis enzyme which display adenosylcobinamide kinase and adenosylcobinamide phosphate guanyltransferase activity and is a key participant in the final stages of cobalamin biosynthesis where it is involved in nucleotide loop assembly. CobU is a homotrimer which functions both as a kinase and as a nucleotidyl transferase. It phosphorylates of adenosylcobinamide to form adenosylcobinamide phosphate (using a variety of nucleotides as the phosphate donor) and then adds GMP to adenosylcobinamide phosphate to form adenosylcobinamide-GDP, specifically using GTP
ILVTGGARSGKSRFAERLALQSGKDVVYVATAEAFDDEMAERIERHRKRRPAGWQTVEEPLDLAEALRAL
PKGSVVLLDCLTLWLTNLLFADDGWVEAAIEEEIEALLEALKACPATLIIVSNEVGWGIVPENPLGRRFR
DLLGRLNQRLAAAADEVYLVVAGIPL
>gnl|CDD|238305 cd00545, MCH, Methenyltetrahydromethanopterin (methenyl-H4MPT) cyclohydrolase (MCH). MCH is a cytoplasmic enzyme that has been identified in methanogenic archaea, sulfate- reducing archaea, and methylotrophic bacteria. It catalyzes the reversible formation of N(5), N(10)-methenyltetrahydromethanopterin (methenyl-H4MPT+) from N(5)-formyltetrahydromethanopterin (formyl- H4MPT), in the third step of the reaction to reduce CO2 to CH4. The protein functions as a homodimer or homotrimer, depending on the organism
SVNELALPLVERLIEDAEELRIEVSKLENGATVIDAGVNAPGSLEAGRLIAEICLGGLATVTITVDGDFG
LWPPTVEVHTDNPVIACLGSQYAGWSLSVGDFFALGSGPARALALKPEELYEEIGYRDDAEVAVLVLESD
KLPPEEVAEKVAAECGVDPENVTLIVAPTASLAGSVQIVARVVEVALHKAHELGFDLNKVKDGAGSAPIA
PPAPDDLQAMGRTNDAILYGGRVHLTVKGDDEAAEELAKELPSSASRDYGKPFAEVFKEADYDFYKIDPG
LFAPARVTVNDLETGKTFRAGKVDPELLAQSF
>gnl|CDD|238306 cd00546, QFR_TypeD_subunitC, Quinol:fumarate reductase (QFR) Type D subfamily, 15kD hydrophobic subunit C; QFR couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, the opposite reaction to that catalyzed by the related protein, succinate:quinine oxidoreductase (SQR). QFRs oxidize low potential quinols such as menaquinol and are involved in anaerobic respiration with fumarate as the terminal electron acceptor. SQR and QFR share a common subunit arrangement, composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are classified as Type D as they contain two transmembrane subunits (C and D) and no heme groups. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit containing the electron donor (quinol). The quinone binding site resides in the transmembrane subunits
RKPYVRPMTPTWWKKLDFYRFYMLREATAVPTVWFSLVLLYGLFALGSGPESWAGFVSFLQNPIVVLLNI
IALAAALLHAKTWFEMAPKVMNIIVKGERVPPEAITKALWAVTAVVSVVALVLV
>gnl|CDD|238307 cd00547, QFR_TypeD_subunitD, Quinol:fumarate reductase (QFR) Type D subfamily, 13kD hydrophobic subunit D; QFR couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, the opposite reaction to that catalyzed by the related protein, succinate:quinine oxidoreductase (SQR). QFRs oxidize low potential quinols such as menaquinol and are involved in anaerobic respiration with fumarate as the terminal electron acceptor. SQR and QFR share a common subunit arrangement, composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are classified as Type D as they contain two transmembrane subunits (C and D) and no heme groups. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit containing the electron donor (quinol). The quinone binding site resides in the transmembrane subunits
SPKRSDEPIFWGLFGAGGMWSAIVTPVLILLLGILLPLGLIPAALSYDRIIAFAQSWIGKLFLLVLIILP
MWHAMHRIHHGLHDLKIHHVPAGKIIFYGLAALYSVLALFAVFTL
>gnl|CDD|349426 cd00548, NrfA-like, cytochrome c nitrite reductase and similar proteins. This family contains cytochrome c nitrite reductase (also known as cytochrome c552, or NrfA) and similar proteins. The pentaheme enzyme NrfA catalyzes the electron reduction of nitrite to ammonia in the nitrogen cycle. This enzyme can also transform nitrogen monoxide and hydroxylamine, two potential bound reaction intermediates, into ammonia. It is a homodimer, with each monomer containing four classical CXXCH type heme-binding sites along with an alternative CXXCK heme-binding motif, which is important for catalysis. This family also includes octaheme nitrite reductase (TvNiR) from the haloalkaliphilic bacterium Thioalkalivibrio paradoxus which catalyzes the reduction of nitrite and hydroxylamine to ammonia as well as the reduction of sulfite to sulfide
DPEVWGKNYPNQYESYLKTKEMTPTTKYGGSKLEEKLEEDPYLVILWAGYGFAKDYNEPRGHAYALEDVR
ETLRTGAGKQPAACLTCKSPDVPRLIEEMGDDYYKMPFAELGAEVTHPIGCADCHDPKTMELRITRPALI
EALKRLGKDTEKASRQEMRSLVCAQCHVEYYFDPETKTVTFPWDNGLTPEDIEAYYDEIGFKDWTHAVTG
APMLKAQHPEFETWSGGIHAKAGVSCADCHMPYVREGGKKYSSHWVTSPLKNIEQSCLTCHRESEEELKA
RVDDIQDRTKELLRRAEDALVKAIDAIEAAWEAGATEEELKEARELHRKAQWRWDFVAAENSMGFHNPEE
ALRILADSIDYARQARLLLA
>gnl|CDD|200451 cd00551, AmyAc_family, Alpha amylase catalytic domain family. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; and C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost this catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
VIYQLFPDRFTDGDSSGGDGGGDLKGIIDKLDYLKDLGVTAIWLTPIFESPEYDGYDKDDGYLDYYEIDP
RLGTEEDFKELVKAAHKRGIKVILDLVFNHDILRFWLDEGVDGFRLDAAKHVPKPEPVEFLREIRKDAKL
AKPDTLLLGEAWGGPDELLAKAGFDDGLDSVFDFPLLEALRDALKGGEGALAILAALLLLNPEGALLVNF
LGNHDTFRLADLVSYKIVELRKARLKLALALLLTLPGTPMIYYIKKLIAL
>gnl|CDD|238308 cd00552, RaiA, RaiA ("ribosome-associated inhibitor A", also known as Protein Y (PY), YfiA, and SpotY, is a stress-response protein that binds the ribosomal subunit interface and arrests translation by interfering with aminoacyl-tRNA binding to the ribosomal A site. RaiA is also thought to counteract miscoding at the A site thus reducing translation errors. The RaiA fold structurally resembles the double-stranded RNA-binding domain (dsRBD)
NINITGRNIEVTDALREYVEEKLEKLEKYFDRIISVDVVLSVEKNHGKRFKVEITIHLPGGVLRAEASAE
DLYAAIDLAVDKLERQLRKYKEK
>gnl|CDD|467484 cd00553, NAD_synthase, NAD(+) synthase. NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source
IDPEEIIEALVCFLRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRALGAENVLALIMPSRYSSKETRDDA
KALAENLGIEYRTIDIDPIVDAFLKALEHAGGSEAEDLALGNIQARLRMVLLYALANLLGGLVLGTGNKS
ELLLGYFTKYGDGAADINPIGDLYKTQVRELARYLGVPEEIIEKPPSAELWPGQTDEDELGMPYEELDLI
LYGLVDGKLGPEEILSPGEDEEKVKRIFRLYRRNEHKR
>gnl|CDD|100025 cd00554, MECDP_synthase, MECDP_synthase (2-C-methyl-D-erythritol-2,4-cyclodiphosphate synthase), encoded by the ispF gene, catalyzes the formation of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MEC) in the non-mevalonate deoxyxylulose (DOXP) pathway for isoprenoid biosynthesis. This pathway is present in bacteria, plants and some protozoa but is distinct from that used by mammals and Archaea. MECDP_synthase forms a homotrimer, carrying three active sites, each of which is formed in a cleft between pairs of subunits
RIGIGYDVHRFVEGRPLILGGVEIPHEKGLLGHSDGDVLLHALTDALLGAAGLGDIGEHFPDTDPKWKGA
DSRILLEEALKLIREKGYEIVNIDITIIAERPKISPYREAMRANLAELLGIPPSRVNIKATTTEGLGFTG
RGEGIAAQAVVLL
>gnl|CDD|238310 cd00555, Maf, Nucleotide binding protein Maf. Maf has been implicated in inhibition of septum formation in eukaryotes, bacteria and archaea, but homologs in B.subtilis and S.cerevisiae are nonessential for cell division. Maf has been predicted to be a nucleotide- or nucleic acid-binding protein with structural similarity to the hypoxanthine/xanthine NTP pyrophosphatase Ham1 from Methanococcus jannaschii, RNase H from Escherichia coli, and some other nucleotide or RNA-binding proteins
LILASASPRRRELLEQLGIPFEVVPSDIDETPIKGESPEDYVLRLAEAKAEAVAARLPPDALVIGADTVV
VLDGRILGKPKDREEAREMLKRLSGRTHEVYTGVALIDPGGKLVTDVESTKVRFRELSDEEIEAYVASGE
PLDKAGAYGIQGLGGALIERIEGDYSNVVGLPLPELLKLL
>gnl|CDD|238311 cd00556, Thioesterase_II, Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene
DRFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGASGFASLDHHIYFHRPGDADEWLLYEVESLR
DGRSRALRRGRAYQRDGKLVASATQSFLV
>gnl|CDD|238312 cd00557, Translocase_SecB, Preprotein translocase subunit SecB. SecB is a cytoplasmic component of the multisubunit membrane-bound enzyme termed Sec protein translocase, which is the main constituent of the General Secretory (type II) Pathway involved in translocation of nascent polypeptides across the cytoplasmic membrane. SecB has been shown to function as export-specific molecular chaperone that selectively binds preproteins, maintains them in a translocation competent state and delivers them to SecA, the membrane-bound ATPase, that drives the translocation reaction. In solution, SecB exists as homotetramer, which is organized as a dimer of dimers
LQIQRIYVKDISFEAPNAPHLFQKDWKPRLNLDLDTEITQLKNDNKYEVVLNITAGAKLEFAKSAFYCEV
KQAGVFEIIGIEIDQMAHCLEINCPAILFPYARELISSITARATFPPLNLPPINFDALFAN
>gnl|CDD|238313 cd00559, Cyanase_C, Cyanase C-terminal domain. Cyanase (Cyanate lyase) is responsible for the hydrolysis of cyanate. It catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. This allows organisms that possess the enzyme to overcome the toxicity of environmental cyanate and to use cyanate as a source of nitrogen for growth. This enzyme is a homodecamer, formed by five dimers. Each monomer is composed of two domains, an N-terminal helix-turn-helix and this structurally unique C-terminal domain
MVPTDPLIYRFYEIVQVYGPTLKALIHEKFGDGIMSAIDFKLDVDKVEDPGGDRVVITLDGKFLPYKPF
>gnl|CDD|185673 cd00560, PanC, Pantoate-beta-alanine ligase. PanC Pantoate-beta-alanine ligase, also known as pantothenate synthase, catalyzes the formation of pantothenate from pantoate and alanine. PanC belongs to a large superfamily of nucleotidyltransferases that includes, ATP sulfurylase (ATPS), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain
MRIITTIAELRAWLRNWRAQGKTIGFVPTMGALHEGHLSLVRRARAENDVVVVSIFVNPLQFGPNEDLDR
YPRTLEADLALLEEAGVDLLFAPSVEEMYPEGLFSTFVDVGPLSEVLEGASRPGHFRGVATVVAKLFNLV
QPDRAYFGEKDAQQLAVIRRMVRDLNLPVEIVGCPTVREEDGLALSSRNVYLSAEERKEALALYRALKAA
AEAIAAGERDAEDIIAAARDVLEAAGFRVDYLEIVDPETLEPVEEIDKPAVILVAARVGKTRLIDNI
>gnl|CDD|410862 cd00561, CobA_ACA, CobA-type ATP:corrinoid adenosyltransferase. CobA-ATP:corrinoid adenosyltransferase is one of three sequence and structurally unrelated groups of ATP:corrinoid adenosyltransferase, PduO and EutT being the other two. CobA has been shown to be involved in cobalamin (vitamin B12) biosynthesis and scavenging of incomplete corrinoids. This enzyme is a homodimer, which catalyzes the adenosylation reaction: ATP + cob(I)alamin + H2O
KGLVIVYTGNGKGKTTAALGLALRALGHGMKVLIVQFIKGGWKYGELKALKKLPNIEIHRMGEGFTWKTQ
DREEDIAAAREGWELAKEALASGEYDLVILDEINYALKYGLLPVEEVLELLKNKPPDLEVVLTGRNAPPE
LIELADLVTEMREVKHPFDQGIKAQKGIEY
>gnl|CDD|238315 cd00562, NifX_NifB, This CD represents a family of iron-molybdenum cluster-binding proteins that includes NifB, NifX, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme. This domain is a predicted small-molecule-binding domain (SMBD) with an alpha/beta fold that is present either as a stand-alone domain (e.g. NifX and NifY) or fused to another conserved domain (e.g. NifB) however, its function is still undetermined.The SCOP database suggests that this domain is most similar to structures within the ribonuclease H superfamily. This conserved domain is represented in two of the three major divisions of life (bacteria and archaea)
KIAVASSDGGRVDQHFGRAPEFLIYEVEPGGIKLVEVRENPAACGGGGEGKLAARLLALEGCDAVLVGGI
GGPAAAKLEAAGIKPIKAAEGGTIEEALEALQ
>gnl|CDD|238316 cd00563, Dtyr_deacylase, D-Tyrosyl-tRNAtyr deacylases; a class of tRNA-dependent hydrolases which are capable of hydrolyzing the ester bond of D-Tyrosyl-tRNA reducing the level of cellular D-Tyrosine while recycling the peptidyl-tRNA; found in bacteria and in eukaryotes but not in archea; beta barrel-like fold structure; forms homodimers in which two surface cavities serve as the active site for tRNA binding
MRAVIQRVSEASVTVDGEVVGAIGQGLLVLVGVTHDDTEEDAEYLARKILNLRIFEDEEGKMNLSVKDVN
GEILVVSQFTLYADTKKGRRPSFSAAAPPDKAEPLYESFVELLREKGIKVETGVFGAMMQVSLVNDGPVT
IILDS
>gnl|CDD|238317 cd00564, TMP_TenI, Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions
LYLITDRRLDGEDLLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALA
VGADGVHLGQDDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLE
LLREIAELVEIPVVAIGGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA
>gnl|CDD|340451 cd00565, Ubl_ThiS, ubiquitin-like (Ubl) domain found in sulfur carrier protein ThiS. ThiS, also termed Thiamine biosynthesis protein (ThiaminS), is a sulfur carrier protein involved in thiamin biosynthesis in prokaryotes. It has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub), and is activated in an ATP-dependent manner by sulfurtransferases, similar to the activation mechanism of Ub-activating enzyme E1. ThiS has common evolutionary origin with Ub-related protein modifiers in eukaryotes, a beta-grasp fold as Ub, and is closely related to proteins MoaD and Urm1
ITVNGEPREVDEGLTLAELLEELGFTPKGVAVELNGEIVPRSEWAETILKDGDRIEIVTFVGGG
>gnl|CDD|173838 cd00567, ACAD, Acyl-CoA dehydrogenase. Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLGAALLLAYGTEEQKERYLPPLASGEAI
AAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEEGPGHRGISAFLVPAD
TPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAARAALD
EAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAAR
EVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR
>gnl|CDD|238318 cd00568, TPP_enzymes, Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes
RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCI
AGDGGFMMTGQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNPDFAALAEAYGAKGV
RVEDPEDLEAALAEALAAGGPALIEVKT
>gnl|CDD|259851 cd00569, HTH_Hin_like, Helix-turn-helix domain of Hin and related proteins. This domain model summarizes a family of DNA-binding domains unique to bacteria and represented by the Hin protein of Salmonella. The basic HTH domain is a simple fold comprised of three core helices that form a right-handed helical bundle. The principal DNA-protein interface is formed by the third helix, the recognition helix, inserting itself into the major groove of the DNA. A diverse array of HTH domains participate in a variety of functions that depend on their DNA-binding properties. HTH_Hin represents one of the simplest versions of the HTH domains; the characterization of homologous relationships between various sequence-diverse HTH domain families remains difficult. The Hin recombinase induces the site-specific inversion of a chromosomal DNA segment containing a promoter, which controls the alternate expression of two genes by reversibly switching orientation. The Hin recombinase consists of a single polypeptide chain containing a C-terminal DNA-binding domain (HTH_Hin) and a catalytic domain
GRPPKLTPEQIAEARRLLAAGESVAEIARELGVSRSTLYRYL
>gnl|CDD|238319 cd00570, GST_N_family, Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK subfamily, a member of the DsbA family). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxin 2 and stringent starvation protein A
LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYL
A
>gnl|CDD|238320 cd00571, UreE, UreE urease accessory protein. UreE is a metallochaperone assisting the insertion of a Ni2+ ion in the active site of urease, an important step in the in vivo assembly of urease, an enzyme that hydrolyses urea into ammonia and carbamic acid. The C-terminal region of UreE contains a histidine rich nickel binding site
MIITRILGNIKDIALTDGQIDTVVLTWDDRQKRRLRLKSDHGEELGIRLPRGQVLRDGDVLFLDDGRLVV
VRAAPEDVLVITPKDMLELARLAYHLGNRHVPLQIEEDELYIPYDHVLEDMLRKLGVRYERVERPF
>gnl|CDD|238321 cd00575, NOS_oxygenase, Nitric oxide synthase (NOS) produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOSs also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN. While prokaryotes can produce NO as a byproduct of denitrification, using a completely different set of enzymes than NOS, a few prokaryotes also have a NOS which consists solely of the NOS oxygenase domain. Prokaryotic NOS binds to the substrate L-Arg, zinc, and to the cofactors heme and tetrahydrofolate
ELLPQAKDFINQYYSSIKRSGSEAHEARLEEVEKEIEATGTYQLTEEELIYGAKMAWRNAPRCIGRIQWS
KLQVFDARDVTTAQEMFEAICNHIKYATNGGNIRSAITVFPQRTDGKHDFRIWNSQLIRYAGYKQPDGSI
IGDPANVEFTELCIQLGWKPKGGRFDVLPLVLQANGEDPELFEIPPELVLEVPIEHPKYEWFAELGLKWY
ALPAVSNMLLEIGGLEFPAAPFNGWYMGTEIGVRNLCDTQRYNILEKVARKMGLDTRKNSSLWKDRALVE
LNVAVLHSFQKAGVTIVDHHTAAESFMKHLENEYRARGGCPADWVWLVPPMSGSLTPVFHQEMLNYVLSP
SFFYQP
>gnl|CDD|153083 cd00576, RNR_PFL, Ribonucleotide reductase and Pyruvate formate lyase. Ribonucleotide reductase (RNR) and pyruvate formate lyase (PFL) are believed to have diverged from a common ancestor. They have a structurally similar ten-stranded alpha-beta barrel domain that hosts the active site, and are radical enzymes. RNRs are found in all organisms and provide the only mechanism by which nucleotides are converted to deoxynucleotides. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs use a diiron-tyrosyl radical while Class II RNRs use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. PFL, an essential enzyme in anaerobic bacteria, catalyzes the conversion of pyruvate and CoA to acteylCoA and formate in a mechanism that uses a glycyl radical
AERIYEAVKSGVITVGRPDLPFTGCVLVDYGDSLDPGIKGVNETAKSINEAIQKTYQIIALAASNQNGGG
VSFARASSILSPYGSRDYAKGSGTETDAVEAADAFNLALKEVGQGNGRTGAATGFIGGVHKGKGDKISQE
FLNLALANGGEGIPLNFPNLSVRVSSDKPGILVKAVELKQLIAEEARKTGSPGIFNDELCNLVSLNLARI
MEKAINGSMDVVLEELEELAFLAVRALDCVIDSHDERIPTIELGGDERRTVGLGIAGVADLLIKLGLEKV
GDPEADDLAAELVDQLKKHLVKATNERGFNFLLGLSPSESNSSGAPATNGVSPSRGXIAIVLNGDIGPEE
SLASVAILQFYADNGISDTITIPDSATNLDQLLAVIDGAAAIKTTHVRVNP
>gnl|CDD|238322 cd00577, PCNA, Proliferating Cell Nuclear Antigen (PCNA) domain found in eukaryotes and archaea. These polymerase processivity factors play a role in DNA replication and repair. PCNA encircles duplex DNA in its central cavity, providing a DNA-bound platform for the attachment of the polymerase. The trimeric PCNA ring is structurally similar to the dimeric ring formed by the DNA polymerase processivity factors in bacteria (beta subunit DNA polymerase III holoenzyme) and in bacteriophages (catalytic subunits in T4 and RB69). This structural correspondence further substantiates the mechanistic connection between eukaryotic and prokaryotic DNA replication that has been suggested on biochemical grounds. PCNA is also involved with proteins involved in cell cycle processes such as DNA repair and apoptosis. Many of these proteins contain a highly conserved motif known as the PIP-box (PCNA interacting protein box) which contains the sequence Qxx[LIM]xxF[FY]
ATLSNAKLLKKIVDALSKLVDEANFDITEDGISLQAMDSSHVALVSLFLPKELFEEYRCDEEISLGVNLK
SLLKILKCAGNEDCVTLRADDEDPLKILFESSKGDVTSEFSLKLMDIDSEQLPIPELEYDATVTLPSDEL
KDIVRDLESISDSVTISASKDGFKFSAEGELGGASVTLLPKDSDLLVTIECSEPVSSTYSLKYLKDFTKA
APLSDKVTLSFGSDGPLSLEFKIADGGHLTFYLAPKIE
>gnl|CDD|238323 cd00578, L-fuc_L-ara-isomerases, L-fucose isomerase (FucIase) and L-arabinose isomerase (AI) family; composed of FucIase, AI and similar proteins. FucIase converts L-fucose, an aldohexose, to its ketose form, which prepares it for aldol cleavage (similar to the isomerization of glucose in glycolysis). L-fucose (or 6-deoxy-L-galactose) is found in various oligo- and polysaccharides in mammals, bacteria and plants. AI catalyzes the isomerization of L-arabinose to L-ribulose, the first reaction in its conversion to D-xylulose-5-phosphate, an intermediate in the pentose phosphate pathway, which allows L-arabinose to be used as a carbon source. AI can also convert D-galactose to D-tagatose at elevated temperatures in the presence of divalent metal ions. D-tagatose, rarely found in nature, is of commercial interest as a low-calorie sugar substitute
PKIGFVTGSQHLYGEELLEQVEEYAREVADLLNELPVEVVDKPEVTGTPDEARKAAEEFNEANCDGLIVW
MHTFGPAKMWIAGLSELRKPVLLLATQFNREIPDFMNLNQSACGLREFGNILARLGIPFKVVYGHWKDED
VLRKIESWARAAAAVATLRGLRVGRFGDRMRGMAVTEGDKVLAQIKFGVSVEYLEVGELVRRIDEVSDEE
VEELLEEYEENYDVVLDAKGLTDESLRKAARLYLALRRLLEDGGLDAFTIQCFEDLTDLGQLPCLAEQRL
NAEGIPFACEGDWKGALLMRIGKVLSGGGASFADDYTYDFDENDVVLLAHMGEAPPSIAERAKPRLEVHP
LGFRGDGGSLVFDAKPGPVTLARLIDDGGRYRLVVGEGESVEPPEERPKLPVTRAWWKPPPDLDEFMEAW
ILAGGAHHTALSYGHTAEELEDLAEILGIEVV
>gnl|CDD|238324 cd00580, CHMI, 5-carboxymethyl-2-hydroxymuconate isomerase (CHMI) is a trimeric enzyme catalyzing the isomerization of the unsaturated ketone 5-(carboxymethyl)-2-hydroxymuconate to 5-(carboxymethyl)-2-oxo-3-hexene-1,6-dionate. This is one step in the homoprotocatechuate pathway, one of the microbial meta-fission pathways that degrade aromatic carbon sources to citric acid cycle intermediates. Despite the structural similarity of CHMI with 4-oxalocrotonate tautomerase (4-OT) and macrophage migration inhibitory factor (MIF), there is no significant sequence similarity among these protein families, and therefore, they are not combined in one hierarchy
PHLIIEYSANLEGRADIPELLRALHDALVASGLFPLGGIKVRAIRADHYRVGDGDEDDAFIHVTLRILAG
RSEEQKQELSEALLAALRAHLAPVFAKRYLSLSVEIRELDPAS
>gnl|CDD|238325 cd00581, QFR_TypeB_TM, Quinol:fumarate reductase (QFR) Type B subfamily, transmembrane subunit; QFR couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, the opposite reaction to that catalyzed by the related protein, succinate:quinone oxidoreductase (SQR). QFRs oxidize low potential quinols such as menaquinol and rhodoquinol and are involved in anaerobic respiration with fumarate as the terminal electron acceptor. SQR and QFR share a common subunit arrangement, composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are classified as Type B as they contain one transmembrane subunit and two heme groups. The heme and quinone binding sites reside in the transmembrane subunit. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit containing the electron donor (quinol). The Type B enzyme from Desulfovibrio gigas is capable of fumarate reduction and succinate oxidation
LDFLQSATGLFLALFMWAHMLFVSSILLGKEAMYWVARFFEGAFFFGHGYPWVVSVVAAIVFALFVAHAF
LALRKFPANYRQWRAFRRHMQLMKHGDTSLWWIQAVTGFVLFFLASAHLYEMLTNPEIIGPHTSAYRVVH
GGWWLLYLALLPAVELHGGIGLYRLAVKWGWFASESRKRLRRIKNVLSAFFLVLGLLTLLAYIKIG
>gnl|CDD|411704 cd00583, MutH-like, Restriction endonuclease MutH and similar endonucleases. MutH is a 28kD endonuclease involved in methyl-directed DNA mismatch repair in gram negative bacteria. MutH is both sequence-specific and methylation-specific, introducing a nick in the unmethylated strand of a hemi-methylated d(GATC) DNA duplex. MutH is homologous to the type II restriction endonuclease Sau3AI which also recognizes the d(GATC) sequence however, Sau3AI cleaves both strands regardless of their methylation state. The active form of MutH is monomeric while that of Sau3AI is homodimeric. In addition to MutH, MutS, involved in mismatch recognition, and MutL, involved in mediating the interactions between MutH and MutS, are essential in initiating mismatch repair in Escherichia coli
LARARALAGLTLGELAAQLGVPVPANLRRAKGWVGQLLELALGATAGSKPEPDFPHLGIELKTLPIDANG
KPLESTFVCTAPLLGNHGLTWETSRVRRKLARVLWVPVEADRGIPLAERRIGTPFLWSPNAEQEALLRAD
WEELMELIALGQVEEITARLGEYLQIRPKAANGRVLTDAIGADGEIILTLPRGFYLRTSFTAAILARH
>gnl|CDD|467468 cd00584, Prefoldin_alpha, Prefoldin alpha subunit. Alpha subunits of prefoldin, a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils
LAEQLQELREQIEALQEEIEQLEEEQAEIDEAKEALEELKKEGSEVLVPLGGNAYVRAEVVDIDKVIVHL
GLGYYAERDPDGAIEILEKKEDELDKRIEELQAELAELEDEYDQLEQQAQQ
>gnl|CDD|238328 cd00585, Peptidase_C1B, Peptidase C1B subfamily (MEROPS database nomenclature); composed of eukaryotic bleomycin hydrolases (BH) and bacterial aminopeptidases C (pepC). The proteins of this subfamily contain a large insert relative to the C1A peptidase (papain) subfamily. BH is a cysteine peptidase that detoxifies bleomycin by hydrolysis of an amide group. It acts as a carboxypeptidase on its C-terminus to convert itself into an aminopeptidase and peptide ligase. BH is found in all tissues in mammals as well as in many other eukaryotes. Bleomycin, a glycopeptide derived from the fungus Streptomyces verticullus, is an effective anticancer drug due to its ability to induce DNA strand breaks. Human BH is the major cause of tumor cell resistance to bleomycin chemotherapy, and is also genetically linked to Alzheimer's disease. In addition to its peptidase activity, the yeast BH (Gal6) binds DNA and acts as a repressor in the Gal4 regulatory system. BH forms a hexameric ring barrel structure with the active sites imbedded in the central channel. The bacterial homolog of BH, called pepC, is a cysteine aminopeptidase possessing broad specificity. Although its crystal structure has not been solved, biochemical analysis shows that pepC also forms a hexamer
LSPELLEKFRKDFLSDPKNRLAQNALTNNGILKAALNRQALRKLNRVFSIEVPTEPVTNQKSSGRCWLFA
ALNVLRHQFMKKLNLKEFEFSQSYLFFWDKLEKANYFLENIIETADEPLDDRLVQFLLANPQNDGGQWDM
LVNLIEKYGLVPKSVMPESFNSENSRRLNYLLNRKLREDALELRKLVAKGASKEEIEAKKEEMLKEVYRI
LAIALGEPPEKFDWEYRDKDKKYHEIKELTPLEFYKKYVKFDLDDYVSLINDPRPDKPYNKLYTVEYLGN
VVGGRPILYLNVPMDVLKKAAIAQLKDGEPVWFGCDVGKFSDRKSGILDTDLFDYELLFGIDFGLNKAER
LDYGESLMTHAMVLTGVDLDEDGKPVKWKVENSWGEKVGKKGYFVMSDDWFDEYVYQVVVDKKYLPEEVL
DLLKQEPIVLPPWDPMG
>gnl|CDD|238329 cd00586, 4HBT, 4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII)
FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDR
LTVETRVLRLGRKSFTFEQEIFREDGELLATAETVLVCVD
>gnl|CDD|238330 cd00587, HCP_like, The HCP family of iron-sulfur proteins includes hybrid cluster protein (HCP), acetyl-CoA synthase (ACS), and carbon monoxide dehydrogenase (CODH), all of which contain [Fe4-S4] metal clusters at their active sites. These proteins have a conserved alpha-beta rossman fold domain. HCP, formerly known as prismane, is thought to play a role in nitrogen metabolism but its specific function is unknown. Acetyl-CoA synthase (ACS), is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide and CoA
MVLHGAAAHTEHGRHLPDFESKSLHSGMIDSLPKRIDASVSEVLASTHRGKDLDVDNLVENARRAGGADW
TGAHILTALSDALKVGIAVVDGTIPGVALIVGCNNDKKQDKAYADIAKELMKRGVMVLATGCAAEALLKL
GLEDGAGILGGLPIVFDMGNCVDNSHAANLALKLANMFGGYDRSDLPAVASAPGAYSQKAAAIATGAVFL
GVPVHVGPPLPVDGSIPVWKVLTPEASDNEGGYFISVTDYQDIVQKAM
>gnl|CDD|238331 cd00588, CheW_like, CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in the chemotaxis associated histidine kinase CheA binds to CheW, suggesting that these domains can interact with each other
ILQVLLFRVGDELYAIPIAVVEEILPLPPITRVPNAPDYVLGVINLRGEILPVIDLRRLFGLEAAEPDTD
ETRIVVVEVGDRKVGLVVDSVLGVLEVVIKDIEPPPDVGSSNAPGISGATILGDGRVVLILDVDKL
>gnl|CDD|409669 cd00590, RRM_SF, RNA recognition motif (RRM) superfamily. RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs)
LFVGNLPPDTTEEDLRELFSKFGEVVSVRIVRDRDGKSKGFAFVEFESPEDAEKALEALNGTELGGRPLK
VS
>gnl|CDD|259852 cd00591, HU_IHF, DNA sequence specific (IHF) and non-specific (HU) domains. This family includes integration host factor (IHF) and HU, also called type II DNA-binding proteins (DNABII), which are small dimeric proteins that specifically bind the DNA minor groove, inducing large bends in the DNA and serving as architectural factors in a variety of cellular processes such as recombination, initiation of replication/transcription and gene regulation. IHF binds DNA in a sequence specific manner while HU displays little or no sequence preference. IHF homologs are usually heterodimers, while HU homologs are typically homodimers (except HU heterodimers from E. coli and other enterobacteria). HU is highly basic and contributes to chromosomal compaction and maintenance of negative supercoiling, thus often referred to as histone-like protein. IHF is an essential cofactor in phage lambda site-specific recombination, having an architectural role during assembly of specialized nucleoprotein structures (snups). Bacillus phage SPO1-encoded transcription factor 1 (TF1) is another related type II DNA-binding protein. Like IHF, TF1 binds DNA specifically and bends DNA sharply
KKELIDAIAAKTGLTKKQAEAVLDAFEEVITEALAAGEEVTLPGFGKFKVKKRAARTGRNPATGETIEIP
AKKVVKFTPSKALKD
>gnl|CDD|133378 cd00592, HTH_MerR-like, Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators. Helix-turn-helix (HTH) MerR-like transcription regulator, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
YTIGEVAKLLGVSVRTLRYYEEKGLLPPERSENGYRLYSEEDLERLRLIRRLRELGLSLKEIRELLDARD
EELSLAALLALLDEKLAELEEKIARLEALL
>gnl|CDD|238333 cd00593, RIBOc, RIBOc. Ribonuclease III C terminal domain. This group consists of eukaryotic, bacterial and archeal ribonuclease III (RNAse III) proteins. RNAse III is a double stranded RNA-specific endonuclease. Prokaryotic RNAse III is important in post-transcriptional control of mRNA stability and translational efficiency. It is involved in the processing of ribosomal RNA precursors. Prokaryotic RNAse III also plays a role in the maturation of tRNA precursors and in the processing of phage and plasmid transcripts. Eukaryotic RNase III's participate (through direct cleavage) in rRNA processing, in processing of small nucleolar RNAs (snoRNAs) and snRNA's (components of the spliceosome). In eukaryotes RNase III or RNaseIII like enzymes such as Dicer are involved in RNAi (RNA interference) and miRNA (micro-RNA) gene silencing
SLLLEALTHPSYANEHGRFNNERLEFLGDAVLELVVTEYLFKKFPDLSEGDLTRLRSALVSNETLARLAR
ELGLGKYLRLGKGEEKSGGRLRPKILADVFEALIGAIYLDGGFEAARKFLLRLLGPLIEEISL
>gnl|CDD|238334 cd00594, KU, Ku-core domain; includes the central DNA-binding beta-barrels, polypeptide rings, and the C-terminal arm of Ku proteins. The Ku protein consists of two tightly associated homologous subunits, Ku70 and Ku80, and was originally identified as an autoantigen recognized by the sera of patients with an autoimmunity disease. In eukaryotes, the Ku heterodimer contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by non-homologous end-joining. The bacterial Ku homologs does not contain the conserved N-terminal extension that is present in the eukaryotic Ku protein
RAIWKGALSLGLDVSIPVKLYSAATEEKPPSFKQLDRKTGERVKVKRVCKYTGGKEVEKEDIVKGYEYGG
DYVPLTEEELEQLKLETSKGLDILGFVPASEIPPYYFDKESYYLVPDDSDKGSEKAFSALRRALLEKDKV
AIARYVLRRNSRPRLVALRPQEEEDPEGLVLVTLPFADDVRSYPFPLLLDIKTEKPTDEELELAKQLIDS
LDLDDFDPEKFPNPYLQRLYALLEAKALGEEIPEPPEDLTLPPPEEIPKRVIDLLEALKKSL
>gnl|CDD|238335 cd00595, NDPk, Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the synthesis of nucleoside triphosphates (NTPs), are involved in numerous regulatory processes associated with proliferation, development, and differentiation. They are vital for DNA/RNA synthesis, cell division, macromolecular metabolism and growth. The enzymes generate NTPs or their deoxy derivatives by terminal (gamma) phosphotransfer from an NTP such as ATP or GTP to any nucleoside diphosphate (NDP) or its deoxy derivative. The sequence of NDPk has been highly conserved through evolution. There is a single histidine residue conserved in all known NDK isozymes, which is involved in the catalytic mechanism. The first confirmed metastasis suppressor gene was the NDP kinase protein encoded by the nm23 gene. Unicellular organisms generally possess only one gene encoding NDP kinase, while most multicellular organisms possess not only an ortholog that provides most of the NDP kinase enzymatic activity but also multiple divergent paralogous genes. The human genome codes for at least nine NDP kinases and can be classified into two groups, Groups I and II, according to their genomic architecture and distinct enzymatic activity. Group I isoforms (A-D) are well-conserved, catalytically active, and share 58-88% identity between each other, while Group II are more divergent, with only NDPk6 shown to be active. NDP kinases exist in two different quaternary structures; all known eukaryotic enzymes are hexamers, while some bacterial enzymes are tetramers, as in Myxococcus. The hexamer can be viewed as trimer of dimers, while tetramers are dimers of dimers, with the dimerization interface conserved
ERTLALIKPDAVAEGLLGEIIMRIEDAGFEIVAMKELHLTEEQAEEFYVEHKGRPFFPDLVQFMSSGPVV
AMILEKDNAVGEWREMLGPTNPEIARHLAPGSLRADFGTDVLRNAVHGSDSVESAAREIAFFF
>gnl|CDD|349427 cd00596, Peptidase_M14_like, M14 family of metallocarboxypeptidases and related proteins. The M14 family of metallocarboxypeptidases (MCPs), also known as funnelins, are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
ILITGGIHGNEVIGVELALALIEYLLENYGNDPLKRLLDNVELWIVPLVNPDGFARVIDSGGRKNANGVD
LNRNFPYNWGKDGTSGPSSPTYRGPAPFSEPETQALRDLAKSHRFDLAVSYHSSSEAILYPYGYTNEPPP
DFSEFQELAAGLARALGAGEYGYGYSYTWYSTTGTADDWLYGELGILAFTVELGTADYPLPGTLLDRRLE
RNLAAL
>gnl|CDD|119349 cd00598, GH18_chitinase-like, The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model
VICYYDGWSSGRGPDPTDIPLSLCTHIIYAFAEISSDGSLNLFGDKSEEPLKGALEELASKKPGLKVLIS
IGGWTDSSPFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYPGAADNSDRENFITLLRELRSALGAA
NYLLTIAVPASYFDLGYAYDVPAIGDYVDFVNVMTYDLVLGVPFYSLGAKAKYAKQKGLGGVMIWELDQD
>gnl|CDD|119373 cd00599, GH25_muramidase, Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity
KGIDVSSWQGSIDWNAVKAAGIDFVFIKATEGTTYVDPKFATNRARARAAGLLVGAYHFARPCANAEAQA
DNFVNTVPRDPGSLPLVLDVEDTGGGCSAAALAAWLNAFLNEVEALTGKKPIIYTSPSFWDDYLASSQLS
DYPLWIAHYRGEPPPAPGAWRPWTLWQYTSSGRVPGISGPVDLNVF
>gnl|CDD|212462 cd00600, Sm_like, Sm and related proteins. The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. Sm-like proteins exist in archaea as well as prokaryotes that form heptameric and hexameric ring structures similar to those found in eukaryotes
LKDFIGKTVSVELKDGRVLTGTLVAFDKYMNLVLDDVVETGRDGKVRVLGLVLIRGSNIVSIR
>gnl|CDD|238336 cd00602, IPT_TF, IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated Tcells (NFAT), and recombination signal J-kappa binding protein (RBP-Jkappa). The IPT domains in these proteins are involved in DNA binding. Most NF-kappaB/Rel proteins form homo- and heterodimers, while NFAT proteins are largely monomeric (with TonEBP being an exception). While the majority of sequence-specific DNA binding elements are found in the N-terminal domain, several are found in the IPT domain in loops adjacent to, and including, the linker region
LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEKGPGETVWEAEAMFRQEDVRQVAIVFKTPPYHN
KWITRPVQVPIQLVRPDDRKRSEPLTFTYTP
>gnl|CDD|238337 cd00603, IPT_PCSR, IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup contains IPT domains of plexins, receptors, like the plasminogen-related growth factor receptors, the hepatocyte growth factor-scatter factors, and the macrophage-stimulating receptors and of fibrocystin. Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT_PCSR domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains
PVITSISPSSGPLSGGTRLTITGSNLGSGSPRVRVTVGGVPCKVLNVSSTEIVCRTPAAATPGEGPVEVT
VDGANVSARVLSNTTFTYVE
>gnl|CDD|238338 cd00604, IPT_CGTD, IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These enzymes are involved in the enzymatic hydrolysis of alpha-1,4 linkages of starch polymers and belong to the glycosyl hydrolase family 13. Most consist of three domains (A,B,C) but CGTase is more complex and has two additional domains (D,E). The function of the IPT/D domain is unknown
PLIGSVGPVMGKPGNTVTISGEGFGSTGGTVYFGGTAAEVLSWSDTSIVVEVPRVAPGNYNISVTTVDGV
TSNGYNFEVLT
>gnl|CDD|238339 cd00606, fungal_RNase, fungal type ribonuclease. Ribonucleases (RNAses) cleave phosphodiester bonds in RNA and are essential for both non-specific RNA degradation and for numerous forms of RNA processing. The members of this CD belong to the superfamily of microbial ribonucleases which are predominantly guanyl specific nucleases. Guanyl specific RNAses are endonucleases which split RNA phosphodiester bonds at the 3' oxygen end of guanosine residues to yield oligonucleotides with the guanosine-2',3'-cyclophosphate at the 3' end and the hydroxyl group at the 5' end. The terminal guanosine-2,3'-cyclophosphate is hydrolysed by guanyl RNAses to give guanosine-3'-phosphate. The alignment also contains ribotoxins, a fungal group of cytotoxins, specifically cleaving the sarcin/ricin loop (SRL) structure of the 23-28S rRNA and therefore being very potent inhibitors of protein synthesis
SYTCGSNCYSSSDVSTAINHAYSSYEEGKGSSSYPHWYNNYEGFDFPVDGPYYEFPIFSDGHVYTGGSPG
ADRVIYNYNGEFCGIITHTGASGNNFVECS
>gnl|CDD|238340 cd00607, RNase_Sa, RNase_Sa. Ribonucleases first isolated from Streptomyces aureofaciens. In general, ribonucleases cleave phosphodiester bonds in RNA and are essential for both non-specific RNA degradation and for numerous forms of RNA processing. RNAse Sa is a guanylate specific endoribonuclease which belongs to the superfamily of microbial ribonucleases. Typical of this sub-family, the enzyme hydrolyses the phosphodiester bonds of RNA at the 3' oxygen end of guanosine residues to yield oligonucleotides with the guanosine-2',3'-cyclophosphate at the 3' end and the hydroxyl group at the 5' end. The terminal guanosine-2,3'-cyclophosphate is hydrolysed by guanyl RNAses to give guanosine-3'-phosphate
VLGTVCLAQLPPEAQDTLNLIAKGGPFPYSKDGVVFGNREGRLPKQSRGYYHEYTVKTPGSRDRGARRIV
CGGPPRDTGECYYTDDHYASFKRID
>gnl|CDD|238341 cd00608, GalT, Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer
HRRYNPLTGEWVLVSPHRAKRPWQGQQEAPKKLPEYDPDCPLCPGNERADTGEQNPDYDVRVFENDFPAL
KPDAPAPEDSDDGLFRTAPARGRCEVICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKNPRIKYVQI
FENKGAEMGASLPHPHGQIWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFV
AVVPFWARWPFEVHILPKRHVSRFTDLTDEEREDLAEILKRLLARYDNLFNCSFPYSMGWHQAPTGGKEL
ENWYYHWHFEIPPRRSATVLKFMAGFELGAGEFINDVTPEQAAARLREV
>gnl|CDD|99734 cd00609, AAT_like, Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein
IDLSIGEPDFPPPPEVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGGVDVPPEEIVVTNGAQE
ALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLEAAKTPKTKLLYLNN
PNNPTGAVLSEEELEELAELAKKHGILIISDEAYAELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPG
LRIGYLIAPPEELLERLKKLLPYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGP
LVVVKPSGGFFLWLDLPEGDDEEFLERLLLEAGVVVRPGSAFGEGGEGFVRLSFATPEEELEEALERLAE
>gnl|CDD|99735 cd00610, OAT_like, Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation
LFERDRKVLWHGYTVRPYPLVIVRAEGAYLYDVDGNRYLDFLSGIGVLNLGHNHPEVVEALKEQLAKLTH
FSLGFFYNEPAVELAELLLALTPEGLDKVFFVNSGTEAVEAALKLARAYTGRKKIISFEGAYHGRTLGAL
SLTGSKKYRGGFGPLLPGVLHVPYPYRYRPPAELADDLEALEEALEEHPEEVAAVIVEPIQGEGGVIVPP
PGYLKALRELCRKHGILLIADEVQTGFGRTGKMFAFEHFGVEPDIVTLGKGLGGGLPLGAVLGREEIMDA
FPAGPGLHGGTFGGNPLACAAALAVLEVLEEEGLLENAAELGEYLRERLRELAEKHPLVGDVRGRGLMIG
IELVKDRATKPPDKELAAKIIKAALERGLLLRPSGGNVIRLLPPLIITEEEIDEGLDALDEAL
>gnl|CDD|99736 cd00611, PSAT_like, Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major group in this CD corresponds to phosphoserine aminotransferase (PSAT). PSAT is active as a dimer and catalyzes the conversion of phosphohydroxypyruvate to phosphoserine
INFSAGPAALPEEVLEQAQKELLDFNGLGMSVMEMSHRSKDFEAIVNEAESDLRELLNIPDNYKVLFLQG
GATGQFAAVPLNLLGDKGTADYVVTGAWSAKAAKEAKRYGGVVVIVAAKEEGKYTKIPDVETWDLAPDAA
YVHYCSNETIHGVEFDEVPDTGGVPLVADMSSNILSRPIDVSKFGVIYAGAQKNLGPAGVTVVIVRKDLL
GKARKITPSMLNYKTHADNNSLYNTPPTFAIYMMGLVLKWLKEQGGVEAMEKRNRQKAQLLYDTIDNSNG
FYRGPVDKRARSRMNVPFRLGKEELEKEFLKEAEAAGMIGLKGHRSVGGIRASIYNALSLEGVQALADFM
KEFQK
>gnl|CDD|99737 cd00613, GDC-P, Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=_ S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life
ETEVLRHLKRLASKNKALDQSMSFLGSGTYKHNPPAVIKRNILENEFYTAYTPYQPEISQGRLQALFELQ
TMLCELTGMDVANASLQDEATAAAEAAGLAAIRAYHKRNKVLVPDSAHPTNPAVARTRGEPLGIEVVEVP
SDEGGTVDLEALKEEVSEEVAALMVQYPNTLGVFEDLIKEIADIAHSAGALVYVDGDNLNLTGLKPPGEY
GADIVVGNLQKTGVPHGGGGPGAGFFAVKKELVRFLPGRLVGVTKDAEGNRAFRLALQTREQHIRREKAT
SNICTGQALLALMAAMYIVYLGPEGLKEIAERAHLNANYLAKRLKEVGGVLPFNGPFFHEFVLRLPPLYG
IRAEDLAKALIDGGFHAPTMYLPVDGTLMIEPTETETKEELDALLEAL
>gnl|CDD|99738 cd00614, CGS_like, CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life
GAVAPPIYQTSTFVFPSPAEAADLFALREGGYIYSRIGNPTVDALEKKLAALEGGEAALAFSSGMAAIST
VLLALLKAGDHVVASDDLYGGTYRLFERLLPKLGIEVTFVDPDDPEALEAAIKPETKLVYVESPTNPTLK
VVDIEAIAELAHEHGALLVVDNTFATPYLQRPLELGADIVVHSATKYIGGHSDVIAGVVVGSGEALIQRL
RFLRLALGTILSPFDAWLLLRGLKTLPLRMERHSENALKVAEFLEKHPKVERVYYPGLPSHPQHELAKKQ
MSGYGGVFSFELKGGLEAAKKFLNALKLFSLAVSLGGVESLVEHPASMTHSQLPPEERAAAGITPGLVRL
SVGIEDVEDLIADLEQALK
>gnl|CDD|99739 cd00615, Orn_deC_like, Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life
PLFEALKEYAKRGIISFHVPGHKGGRGFRKSFYEFYGENLFKADVTELTGLDDLLDPTGPIKEAQELAAR
AFGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYGIAGGI
PPETFKKALIEHPDAKAAVITNPTYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPILPSSAAMAG
ADIVVQSTHKTLPALTQGSMIHVKGDLVNPDRVNEALNLHQSTSPSYLILASLDVARAMMALEGKELVEE
LIELALYARQEINK
>gnl|CDD|99740 cd00616, AHBA_syn, 3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD
ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVA
TANAILLLGATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDA
AQALGATYKGRKVGTFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFKYEHEILG
YNYRLSEIQAAIGLAQLEKLDEIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGE
SRDELIEALKEAGIETRVHYPPLHHQPPYKKLLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEA
LR
>gnl|CDD|99741 cd00617, Tnase_like, Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to tryptophanase (Tnase) and tyrosine phenol-lyase (TPL). Tnase and TPL are active as tetramers and catalyze beta-elimination reactions. Tnase catalyzes degradation of L-tryptophan to yield indole, pyruvate and ammonia and TPL catalyzes degradation of L-tyrosine to yield phenol, pyruvate and ammonia
ERERALKEAGYNVFLLRSEDVYIDLLTDSGTGAMSDYQWAAMMLGDEAYAGSKSFYDLEDAVQDLFGFKH
IIPTHQGRGAENILFSILLKPGRTVPSNMHFDTTRGHIEANGAVPVDLVIDEAHDAQELIPFKGNIDVAK
LEKLIDEVGAENIPYIVLTITNNTAGGQPVSMANLREVRELAHKYGIPVVLDAARFAENAYFIKEREEGY
RDKSIAEIAREMFSYADGCTMSAKKDGLVNIGGFLALRDDELYEEARQRVVLYEGFVTYGGMAGRDMEAL
AQGLREAVEEDYLRHRVEQVRYLGDRLDEAGVPIVEPAGGHAVFIDAREFLPHIPQEQFPAQALAAELYL
EAGVRAVELGIFSAGRDPNTGENKYPELELVRLAIPRRVYTQDHMDYVAAAVIALYERREDIRGLRIVYE
PKLLRHFTARL
>gnl|CDD|153092 cd00618, PLA2_like, PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers
LPYGCYCGPGGSACPSGQPVDETDRCCRKHDCCYDQISDGGCCDGCLSYSFSEGGVTCLTNSDLCTRSHC
DCDRRLAICLARA
>gnl|CDD|238342 cd00619, Terminator_NusB, Transcription termination factor NusB (N protein-Utilization Substance B). NusB plays a key role in the regulation of ribosomal RNA biosynthesis in eubacteria by modulating the efficiency of transcriptional antitermination. NusB along with other Nus factors (NusA, NusE/S10 and NusG) forms the core complex with the boxA element of the nut site of the rRNA operons. These interactions help RNA polymerase to counteract polarity during transcription of rRNA operons and allow stable antitermination. The transcription antitermination system can be appropriated by some bacteriophages such as lambda, which use the system to switch between the lysogenic and lytic modes of phage propagation
RRRARELAVQALYAWELAPEILAEVVSLLELLQYKSKKVLPFALKLVRGVLENIEEIDELIEKHLRNWSL
DRLAIVERAILRLAVYELLFLPDVPHPVVINEAIELAKRFGGDDSHKFVNGVLDKIAKDL
>gnl|CDD|238343 cd00620, Methyltransferase_Sun, N-terminal RNA binding domain of the methyltransferase Sun. The rRNA-specific 5-methylcytidine transferase Sun, also known as RrmB or Fmu shares the RNA-binding non-catalytic domain with the transcription termination factor NusB. The precise biological role of this domain in Sun is unknown, although it is likely to be involved in sequence-specific RNA binding. The C-terminal methyltransferase domain of Sun has been shown to catalyze formation of m5C at position 967 of 16S rRNA in Escherichia coli
MNARSTAAEVLRDVLQRGASLNAVLSALQKKDKSDRDRGLATELVYGTLRWLALLDWIINPLLKKPDVGK
DPDVRNLLRLGLYQLLYLDVPPHAAVDETVEIAKIRKDLGRAGLVNAVLRRFERED
>gnl|CDD|143482 cd00622, PLPDE_III_ODC, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase. This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein
ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPE
RIIFANPCKSISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEE
ARELLRRAKELGLNVVGVSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVV
PSFEEIAAVINRALDEYFPDEGVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRERWYYLNDGVYGSFN
EILFDHIRYPPRVLKDGGRDGELYPSSLWGPTCDSLDVIYEDVLLPEDLAVGDWLLFENMGAYTTAYAST
FNGFPPPKIVYV
>gnl|CDD|238344 cd00625, ArsB_NhaD_permease, Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, antimonite, sulfate and organic anions across biological membranes in all three kingdoms of life. A typical anion permease contains 8-13 transmembrane helices and can function either independently as a chemiosmotic transporter or as a channel-forming subunit of an ATP-driven anion pump
YVLIRPEKLPRAVVALLGAVLLVLLGVVSPKEALSAIDWETILLLFGMMILSAALEETGLFDRLAAKLAR
ASKGSRRLLLLLMLLTAALSAFFSNDATAVLLTPIVLALLRKLGLSPPVPLLLALAFAANIGGAATPIGN
PPNLIIASLSGLGFLDFLAFMAPPALGLLLLLLGLLYLLFRKKLLLPDEDKLTVLAEPLPARPLLKKFLL
LALLLLLLFVLLFFFLIPLGLIALLGALLLLLLLVRGLDPEEVLKSVDWGTLLFFAGLFVLVGALESTGL
LEWLAELLVALVGLPPLAALLLIGLLSALLSNFISNVPTVALLLPIAASLAPPEPAWLALALGSTLGGNL
TLIGSLANLIPLGAAENAGVGISFGEFLKVGLPLTLLSLVVSLLYL
>gnl|CDD|132719 cd00630, RNAP_largest_subunit_C, Largest subunit of RNA polymerase (RNAP), C-terminal domain. RNA polymerase (RNAP) is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is the final target in many regulatory pathways that control gene expression in all living cells. At least three distinct RNAP complexes are found in eukaryotic nuclei, RNAP I, RNAP II, and RNAP III, for the synthesis of ribosomal RNA precursor, mRNA precursor, and 5S and tRNA, respectively. A single distinct RNAP complex is found in prokaryotes and archaea, which may be responsible for the synthesis of all RNAs. Structure studies revealed that prokaryotic and eukaryotic RNAPs share a conserved crab-claw-shape structure. The largest and the second largest subunits each make up one clamp, one jaw, and part of the cleft. The largest RNAP subunit (Rpb1) interacts with the second-largest RNAP subunit (Rpb2) to form the DNA entry and RNA exit channels in addition to the catalytic center of RNA synthesis. The region covered by this domain makes up part of the foot and jaw structures. In archaea, some photosynthetic organisms, and some organelles, this domain exists as a separate subunit, while it forms the C-terminal region of the RNAP largest subunit in eukaryotes and bacteria
GEAVGVLAAQSIGEPGTQMTLRTFHFAGVASMNVTLGLPRLKEILNAASIHEMLEALGIEAARETIIREI
QKVLASQGVSVDRRHIELIADVMTYSGGLRGVTRSGFRASKTSPLMRASFEKTTKHLLDAAAAGEKDELE
GVSENIILGRPAPLGTGS
>gnl|CDD|467469 cd00632, Prefoldin_beta, Prefoldin beta subunit. Beta subunits of prefoldin, a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils
EVLALKSQKEELERKINEQKVVLDELSNLKKNRKVYRQQGNIFILASKEETLSELKKTLDHLQKEIKELE
QQLKAKEK
>gnl|CDD|238346 cd00633, Secretoglobin, Secretoglobins are relatively small, secreted, disulphide-bridged dimeric proteins with encoding genes sharing substantial sequence similarity. Their family subunits may be grouped into five subfamilies, A-E. Uteroglobin (subfamily A), which is identical to Clara cell protein (CC10), forms a globular shaped homodimer with a large hydrophobic pocket located between the two dimers. The uteroglobin monomer structure is composed of four alpha helices that do not form a canonical four helix-bundle motif but rather a boomerang-shaped structure in which helices H1, H3, and H4 are able to bind a homodimeric partner. The hydrophobic pocket binds steroids, particularly progesterone, with high specificity. However, the true biological function of uteroglobin is poorly understood. In mammals, uteroglobin has immunosuppressive and anti-inflammatory properties through the inhibition of phospholipase A2. The other four main subfamilies of secretoglobins are found in heterodimeric combinations, with B and C subfamilies disulphide-bridged to the E and D subfamilies, respectively [See review by Laukaitis C.M. & Karn R.C. (2005). Biological Journal of the Linnean Society 84, 493]. These include rat prostatic steroid-binding protein (PBP or prostatein), human mammaglobin (or heteroglobin), lipophilins, major cat allergen Fel dI, the hamster Harderian gland proteins and mouse salivary androgen-binding protein (ABP). Example of such a heterodimer: ABPalpha-like sequences are closely related to cat Fel dI chain 1, whereas ABPbeta-gamma-like sequences are closely related to Fel dI chain 2. Thus, the heterodimeric structure of ABPalpha-beta and ABPalpha-gamma is recapitulated by the sequence-similar Fel dI chains 1 and 2. This conservation of primary and quaternary structure indicates that the genome of the eutherian common ancestor of cats, rodents, and primates contained a similar gene pair
CPALESVIEGFLLGSEEEYKAELEKFNATPEAVEAKEKLKQCVDEQSLETKENIAKLLEKILASPLC
>gnl|CDD|143483 cd00635, PLPDE_III_YBL036c_like, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, YBL036c-like proteins. This family contains mostly uncharacterized proteins, widely distributed among eukaryotes, bacteria and archaea, that bear similarity to the yeast hypothetical protein YBL036c, which is homologous to a Pseudomonas aeruginosa gene that is co-transcribed with a known proline biosynthetic gene. YBL036c is a single domain monomeric protein with a typical TIM barrel fold. It binds the PLP cofactor and has been shown to exhibit amino acid racemase activity. The YBL036c structure is similar to the N-terminal domain of the fold type III PLP-dependent enzymes, bacterial alanine racemase and eukaryotic ornithine decarboxylase, which are two-domain dimeric proteins. The lack of a second domain in YBL036c may explain limited D- to L-alanine racemase or non-specific racemase activity
IAENLEEVRERIAAAAERAGRDPDEVTLVAVSKTVPAEAIREAIEAGQRDFGENRVQEALDKAEELPDPD
IEWHFIGHLQTNKVKYAVRLFDLIHSVDSLKLAEELNKRAEKEGRVLDVLVQVNIGGEESKSGVAPEELE
ELLEEIAALPNLRIRGLMTIAPLTEDPEEVRPYFRELRELRDELGAKGGVNLKELSMGMSGDFEIAIEEG
ATLVRIGTAIFG
>gnl|CDD|238347 cd00636, TroA-like, Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake
KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGS
GLEAWLDKLSKIAIPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPK
KKVSLVVG
>gnl|CDD|410626 cd00637, 7tm_classA_rhodopsin-like, rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor superfamily. Class A rhodopsin-like receptors constitute about 90% of all GPCRs. The class A GPCRs include the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. Based on sequence similarity, GPCRs can be divided into six major classes: class A (rhodopsin-like family), class B (Methuselah-like, adhesion and secretin-like receptor family), class C (metabotropic glutamate receptor family), class D (fungal mating pheromone receptors), class E (cAMP receptor family), and class F (frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections
LAVLYILIFVVGLVGNLLVILVILRNRRLRTVTNYFILNLAVADLLVGLLVIPFSLVSLLLGRWWFGDAL
CKLLGFLQSVSLLASILTLTAISVDRYLAIVHPLRYRRRFTRRRAKLLIALIWLLSLLLALPPLLGWGVY
DYGGYCCCCLCWPDLTLSKAYTIFLFVLLFLLPLLVIIVCYVRIFRKLRRHRRRIRSSSSNSSRRRRRRR
ERKVTKTLLIVVVVFLLCWLPYFILLLLDVFGPDPSPLPRILYFLALLLAYLNSAINPIIYAFFN
>gnl|CDD|107202 cd00640, Trp-synth-beta_II, Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine
TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKGVIIESTGGNTGIALAAAAA
RLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQGT
IGLEILEQLGGQKPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPEVVTVSDEEALEAIRLLAREEG
ILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG
>gnl|CDD|238348 cd00641, GTP_cyclohydro2, GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5' phosphate, formate, pyrophosphate (APy), and GMP in the biosynthetic pathway of riboflavin. Riboflavin is the precursor molecule for the synthesis of the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) which are essential to cell metabolism. The enzyme is present in plants and numerous pathogenic bacteria, especially gram negative organisms, who are dependent on endogenous synthesis of the vitamin because they lack an appropriate uptake system. For animals and humans, which lack this biosynthetic pathway, riboflavin is the essential vitamin B2. GTP cyclohydrolase II requires magnesium ions for activity and has a bound catalytic zinc. The functionally active form is thought to be a homodimer. A paralogous protein is encoded in the genome of Streptomyces coelicolor, which converts GTP to 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (FAPy), an activity that has otherwise been reported for unrelated GTP cyclohydrolases III
LVEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQL
EEALEEIAEEGGGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLG
IKSVRLLTNNPDKIDALEGYGIEVVERVPLEVEPNEENKGYLKTKRDKMGHLL
>gnl|CDD|238349 cd00642, GTP_cyclohydro1, GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin triphosphate. The enzyme product is the precursor of tetrahydrofolate in eubacteria, fungi, and plants and of the folate analogs in methanogenic bacteria. In vertebrates and insects it is the biosynthtic precursor of tetrahydrobiopterin (BH4) which is involved in the formation of catacholamines, nitric oxide, and the stimulation of T lymphocytes. The biosynthetic reaction of BH4 is controlled by a regulatory protein GFRP which mediates feedback inhibition of GTP-CH-I by BH4. This inhibition is reversed by phenylalanine. The decameric GTP-CH-I forms a complex with two pentameric GFRP in the presence of phenylalanine or a combination of GTP and BH4, respectively
ERLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDPKNTAIFDEDHDEMVIVKDI
TLFSMCEHHLVPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVV
IEATHMCMVMRGVRKPGSKTVTSAMLGVFKEDPKTREEFLRLIRK
>gnl|CDD|153081 cd00643, HMG-CoA_reductase_classI, Class I hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR), class I enzyme, homotetramer. Catalyzes the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. In mammals this is the rate limiting committed step in cholesterol biosynthesis. Class I enzymes are found predominantly in eukaryotes and contain N-terminal membrane regions. With the exception of Archaeoglobus fulgidus, most archeae are assigned to class I, based on sequence similarity of the active site, even though they lack membrane regions. Yeast and human HMGR are divergent in their N-terminal regions, but are conserved in their active site. In contrast, human and bacterial HMGR differ in their active site architecture
EEIIDLLSAGHIKLYKLEKSLEDAERAVRIRRLYLEKSTGKSLEHLPYTTYDYSEVLGRNIENVIGYVQV
PVGVAGPLLINGEYAGGEFYVPMATTEGALVASTNRGCKAINLSGGATTRVLGDGMTRAPVFRFPSAREA
AEFKAWIEENFEAIKEVAESTSRHARLQSIKPYIAGRSVYLRFEYTTGDAMGMNMVTKATEAACDWIEEN
FPDMEVISLSGNFCTDKKPSAINWIEGRGKSVVAEATIPREVVKEVLKTTPEALVEVNIAKNLIGSAMAG
SGGFNAHAANIVAAIFIATGQDAAQVVESSNCITTMELTADGDLYISVTMPSLEVGTVGGGTGLPTQREC
LELLGCYGAGDEPGANARKLAEIVAATVLAGELSLLAALAAGHLVRSHEKLGR
>gnl|CDD|153082 cd00644, HMG-CoA_reductase_classII, Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR), class II, prokaryotic enzyme is a homodimer. Class II enzymes are found primarily in prokaryotes and Archaeoglobus fulgidus and are soluble as they lack the membrane region. Enzymes catalyze the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. Bacteria, such as Pseudomonas mevalonii, which rely solely on mevalonate for their carbon source, catalyze the reverse reaction, using an NAD-dependent HMGR to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. Human and bacterial HMGR differ in their active site architecture
KGFYKLSPEERLQILAEFAGLSEEDVQLLKSGGALPLELADQMIENVIGTFSLPLGVATNFLVNGKDYLV
PMATEEPSVVAAASNAAKIARKSGGFKTSSSDRLMIGQIQLVDVSDPAKARAFILAHKDEILEIANEAHP
SLVKRGGGARDIEVRVLDADLGDFLSVHLLVDTKDAMGANIVNTMLEAVAPLLEEITGGEVLLRILSNYA
TERLVRAKVSIPVEALGTKGGSGEEVAKKIALASAFAQVDPYRAATHNKGIMNGIDAVVLATGNDWRAVE
AGAHAYAARSGQYRSLSTWEIDDGKLVGELELPLAVGTVGGSTKVHPLAKLALKILGVPSAKELAEIIAA
VGLAQNFAALRALATEGIQKGHMKLHARNLAIAAGATGEEIDKVVKQLIEEKTVNLERAKEILKELR
>gnl|CDD|238350 cd00645, AsnA, Asparagine synthetase (aspartate-ammonia ligase) (AsnA) catalyses the conversion of L-aspartate to L-asparagine in the presence of ATP and ammonia. AsnA is a homodimeric enzyme which is structurally similiar to the catalytic core domain of class II aminoacyl-tRNA synthetases. Ammonia-dependent AsnA is not homologous to the glutamine-dependent asparagine synthetase AsnB
QKAIKFIKDFFQDNLAKELNLIRVSAPLFVEKGSGLNDNLNGVEKPVSFKVKALPDATLEVVHSLAKWKR
LALARYGFSLGEGLYTDMNAIRPDEDLDNIHSIYVDQWDWEKVISKGERNLETLKETVNKIYKAIKETEL
EVNEKYPQLEPILPEEITFITSQELEDRYPDLTPKEREDAICKEHGAVFIIGIGGKLSDGKKHDGRAPDY
DDWTLNGDILVWNPVLQRAFELSSMGIRVDEESLQKQLKLAGDEDRLELPFHKMLLNGELPQTIGGGIGQ
SRLCMFLLQKAHIGEVQASVWPDEIREEC
>gnl|CDD|270214 cd00648, Periplasmic_Binding_Protein_Type_2, Type 2 periplasmic binding fold superfamily. This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences
TLTVASIGPPPYAGFAEDAAKQLAKETGIKVELVPGSSIGTLIEALAAGDADVAVGPIAPALEAAADKLA
PGGLYIVPELYVGGYVLVVRKGSSIKGLLAVADLDGKRVGVGDPGSTAVRQARLALGAYGLKKKDPEVVP
VPGTSGALAAVANGAVDAAIVWVPAAERAQLGNVQLEVLPDDLGPLVTTFGVAVRK
>gnl|CDD|173824 cd00649, catalase_peroxidase_1, N-terminal catalytic domain of catalase-peroxidases. This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear
GGGTSNQDWWPNRLNLKILHQHSPKSNPMGEDFNYAEEFKKLDLEALKEDLKALMTDSQDWWPADYGHYG
PLFIRMAWHSAGTYRIADGRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAG
NVALESMGFKTFGFAGGREDVWEPDEDVYWGPEKEWLADKRYSGDRDLENPLAAVQMGLIYVNPEGPDGN
PDPLAAAKDIRETFARMAMNDEETVALIAGGHTFGKTHGAGPASHVGPEPEAAPIEQQGLGWKNSYGTGK
GKDTITSGLEGAWTPTPTKWDNNYLKNLFGYEWELTKSPAGAWQWVPKNAAGENTVPDAHDPSKKHAPMM
LTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKLTHRDMGPKSRYLGPEVPEEDL
>gnl|CDD|133419 cd00650, LDH_MDH_like, NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family. Members of this family include ubiquitous enzymes like L-lactate dehydrogenases (LDH), L-2-hydroxyisocaproate dehydrogenases, and some malate dehydrogenases (MDH). LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH/MDH-like proteins are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
IAVIGAGGNVGPALAFGLADGSVLLAIELVLYDIDEEKLKGVAMDLQDAVEPLADIKVSITDDPYEAFKD
ADVVIITAGVGRKPGMGRLDLLKRNVPIVKEIGDNIEKYSPDAWIIVVSNPVDIITYLVWRYSGLPKEKV
IGLGTLDPIRFRRILAEKLGVDPDDVKVYILGEHGGSQVPDWSTVRIATSIADLIRSLLNDEGEILPVGV
RNNGQIGIPDDVVVSVPCIVGKNGVEEPIEVGLTDFELEKLQKSADTLKKELE
>gnl|CDD|238351 cd00651, TFold, Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with different functions: dihydroneopterin-triphosphate epimerase (DHNTPE), dihydroneopterin aldolase (DHNA), GTP cyclohydrolase I (GTPCH-1), 6-pyrovoyl tetrahydropterin synthetase (PTPS), and uricase (UO,uroate/urate oxidase). They bind to substrates belonging to the purine or pterin families, and share a fold-related binding site with a glutamate or glutamine residue anchoring the substrate and a lot of conserved interactions. They also share a similar oligomerization mode: several T-folds join together to form a beta(2n)alpha(n) barrel, then two barrels join together in a head-to-head fashion to made up the native enzymes. The functional enzyme is a tetramer for UO, a hexamer for PTPS, an octamer for DHNA/DHNTPE and a decamer for GTPCH-1. The substrate is located in a deep and narrow pocket at the interface between monomers. In PTPS, the active site is located at the interface of three monomers, two from one trimer and one from the other trimer. In GTPCH-1, it is also located at the interface of three subunits, two from one pentamer and one from the other pentamer. There are four equivalent active sites in UO, six in PTPS, eight in DHNA/DHNTPE and ten in GTPCH-1. Each globular multimeric enzyme encloses a tunnel which is lined with charged residues for DHNA and UO, and with basic residues in PTPS. The N and C-terminal ends are located on one side of the T-fold while the residues involved in the catalytic activity are located at the opposite side. In PTPS, UO and DHNA/DHNTPE, the N and C-terminal extremities of the enzyme are located on the exterior side of the functional multimeric enzyme. In GTPCH-1, the extra C-terminal helix places the extremity inside the tunnel
TDGVRVKDLLKVTRLGFVTLERTVGQIFEVDVTLSWDGKKAAASDDVATDTVYNTIYRLAKEYVEGSQLI
ERLAEEIAYLIAEHFLSSVAEVKVEEKKPHAVIPDRGVFKPTDSPGVTIERG
>gnl|CDD|238352 cd00652, TBP_TLF, TATA box binding protein (TBP): Present in archaea and eukaryotes, TBPs are transcription factors that recognize promoters and initiate transcription. TBP has been shown to be an essential component of three different transcription initiation complexes: SL1, TFIID and TFIIIB, directing transcription by RNA polymerases I, II and III, respectively. TBP binds directly to the TATA box promoter element, where it nucleates polymerase assembly, thus defining the transcription start site. TBP's binding in the minor groove induces a dramatic DNA bending while its own structure barely changes. The conserved core domain of TBP, which binds to the TATA box, has a bipartite structure, with intramolecular symmetry generating a saddle-shaped structure that sits astride the DNA. New members of the TBP family, called TBP-like proteins (TBLP, TLF, TLP) or TBP-related factors (TRF1, TRF2,TRP), are similar to the core domain of TBPs, with identical or chemically similar amino acids at many equivalent positions, suggesting similar structure. However, TLFs contain distinct, conserved amino acids at several positions that distinguish them from TBP
SPKIQNIVATVNLGCELDLRKIALAARNAEYNPKRFPGVIMRLREPKTTALIFSSGKMVITGAKSEEDAK
LAARKYARILQKLGFPVEKFPEFKVQNIVASCDLGFPIRLEELALKHPENASYEPELFPGLIYRMDEPKV
VLLIFVSGKIVITGAKSREDIYEAVEKIYPILKE
>gnl|CDD|238353 cd00653, RNA_pol_B_RPB2, RNA polymerase beta subunit. RNA polymerases catalyse the DNA dependent polymerization of RNA. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial. and chloroplast polymerases). Each RNA polymerase complex contains two related members of this family, in each case they are the two largest subunits.The clamp is a mobile structure that grips DNA during elongation
LVKQQIDSFNYFLNVGLQEIVKSIPPITDTDDDGRLKLKFGDIYLGKPKVEEGGVTRKLTPNECRLRDLT
YSAPLYVDIRLTVNDKGKIKEQEVFIGEIPIMLRSKLCNLNGLTPEELIKLGECPLDPGGYFIINGTEKV
IINQEQRSPNVIIVEDSKGKRIYTKTSIPSYSPYRGSWLEVKSDKKKDRIYVRIDLKRQEEALKYIGKRF
EDLIYMIRKLILLVLGKGKLDDIDHLGNKRVRLAGELLQNLFRSGLKRLEREVKEKLQKQLSKKKDLTPQ
LLINSKPITSGIKEFLATGNWGSKRFLMQRSGLSQVLDRLNPLSELSHKRRISSLGLFRERKGFEVRDLH
PSHWGRICPIETPEGENCGLVKNLALMARISGRIERPYRIVEKEVTHIEISPSQILSVAASLIPFPEHNQ
SPRNLYQSNMQKQAVGTPALNQQYRMDTKLYLLLYPQKPLVGTGIEEYIAFGELPLGQNAIVAVMSYSGY
NFEDAIIINKSSVDRGFFRSIHYKKYEIELRKTKNGPEEITRGDIPNVSEEKLKNLDEDGIIRPGARVEP
GDILVGKITPKGETESTPIFGEKARDVRDTSLKYPGGEKGIVDDVKIFSRELNDGGNKLVKVYIRQKRKP
QIGDKFASRHGQKGVISKILPQEDMPFTEDGIPPDIILNPHGFPSRMTIGQLLESLLGKAGALLGKFGDA
TPFDGAEEEDISELLGEAGLNYYGKEVLYDGRTGEPLEAPIFVGPVYYQRLKHMVDDKIHARSTGPYSLL
TRQPLKGRSRGGGQRFGEMERDALIAHGAAYLLQERLTIKSDDVVARVCVKCGIILSANLCRLCKKGTNI
SKVGIPYAFKLLFQELQSMNIDPRLK
>gnl|CDD|238354 cd00655, RNAP_Rpb7_N_like, RNAP_Rpb7_N_like: This conserved domain represents the N-terminal ribonucleoprotein (RNP) domain of the Rpb7 subunit of eukaryotic RNA polymerase (RNAP) II and its homologs, Rpa43 of eukaryotic RNAP I, Rpc25 of eukaryotic RNAP III, and RpoE (subunit E) of archaeal RNAP. These proteins have, in addition to their N-terminal RNP domain, a C-terminal oligonucleotide-binding (OB) domain. Each of these subunits heterodimerizes with another RNAP subunit (Rpb7 to Rpb4, Rpc25 to Rpc17, RpoE to RpoF, and Rpa43 to Rpa14). The heterodimer is thought to tether the RNAP to a given promoter via its interactions with a promoter-bound transcription factor.The heterodimer is also thought to bind and position nascent RNA as it exits the polymerase complex
FQILEIADLVSVPPKYFGDDCKGVKKCLLQEKGEGDRTPVVGIILAIKDTKDIPEGAIRPGDGSAYVNVS
FRAVVFKPFS
>gnl|CDD|259791 cd00656, Zn-ribbon, C-terminal zinc ribbon domain of RNA polymerase intrinsic transcript cleavage subunit. The homologous C-terminal zinc ribbon domains of subunits A12.2, Rpb9, and C11 in RNA Polymerases (Pol) I, II, and III, respectively are required for intrinsic transcript cleavage. TFS is a related archaeal protein that is involved in RNA cleavage by archaeal polymerase. These proteins have two zinc-binding beta-ribbon domains, N-terminal zinc ribbon (N-ribbon) and C-terminal zinc ribbon (C-ribbon). Transcription Factor IIS (TFIIS) domain III is homologous to the C-ribbon domain that stimulates the weak cleavage activity of Rpb9 for Pol II
TLPTTDRTCPKCGHDEAYWWMLQTRSADEPPTRFYKCTKCGHTWR
>gnl|CDD|153097 cd00657, Ferritin_like, Ferritin-like superfamily of diiron-containing four-helix-bundle proteins. Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF)
RLLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAHLLAAYA
LPKTSDDPAEALRAALEVEARAIAAYRELIEQADDPELRRLLERILADEQRHAAWFRKLL
>gnl|CDD|271176 cd00659, Topo_IB_C, DNA topoisomerase IB, C-terminal catalytic domain. Topoisomerase I promotes the relaxation of both positive and negative DNA superhelical tension by introducing a transient single-stranded break in duplex DNA. This function is vital for the processes of replication, transcription, and recombination. Unlike Topo IA enzymes, Topo IB enzymes do not require a single-stranded region of DNA or metal ions for their function. The type IB family of DNA topoisomerases includes eukaryotic nuclear topoisomerase I, topoisomerases of poxviruses, and bacterial versions of Topo IB. They belong to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their C-terminal catalytic domain and the overall reaction mechanism with tyrosine recombinases. The C-terminal catalytic domain in topoisomerases is linked to a divergent N-terminal domain that shows no sequence or structure similarity to the N-terminal domains of tyrosine recombinases
ERDAKKFERARRLKKAIPKIRRRYRKDLKSKELMKERQLAVALYLIDKFALRVGNEKYEEENDTVGCCTL
RKEHVTLEPNVVEFDFLGKDSIRYYNEVPVDPRVFKNLKIFMKLPGDDLFDYVDVRRLNTSKLNAYLREL
MGGLTAKDFRTYGASLTLQQQLKELTAPDSNIPAKKKVYNRANRAVAILCNHTPAVSKKSYIDPRITVAW
>gnl|CDD|238356 cd00660, Topoisomer_IB_N, Topoisomer_IB_N: N-terminal DNA binding fragment found in eukaryotic DNA topoisomerase (topo) IB proteins similar to the monomeric yeast and human topo I and heterodimeric topo I from Leishmania donvanni. Topo I enzymes are divided into: topo type IA (bacterial) and type IB (eukaryotic). Topo I relaxes superhelical tension in duplex DNA by creating a single-strand nick, the broken strand can then rotate around the unbroken strand to remove DNA supercoils and, the nick is religated, liberating topo I. These enzymes regulate the topological changes that accompany DNA replication, transcription and other nuclear processes. Human topo I is the target of a diverse set of anticancer drugs including camptothecins (CPTs). CPTs bind to the topo I-DNA complex and inhibit re-ligation of the single-strand nick, resulting in the accumulation of topo I-DNA adducts. In addition to differences in structure and some biochemical properties, Trypanosomatid parasite topo I differ from human topo I in their sensitivity to CPTs and other classical topo I inhibitors. Trypanosomatid topos I play putative roles in organizing the kinetoplast DNA network unique to these parasites. This family may represent more than one structural domain
KWTTLEHNGVIFPPPYEPLPKNVKFYYDGKPVKLPPEAEEVATFFAVMLETDYATKEVFRKNFFKDFRKI
LTKEEKHIIKKLSKCDFTPIYQYFEEEKEKKKAMSKEEKKAIKEEKEKLEEPYGYCLVDGHKEKVGNFRI
EPPGLFRGRGEHPKMGKLKRRIMPEDITINIGKDAPVPEPPAGHKWKEVRHDNTVTWLASWKENINGQFK
YVMLA
>gnl|CDD|238357 cd00667, ring_hydroxylating_dioxygenases_beta, Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, Ketosteroid isomerase and scytalone dehydratase.The degradation of aromatic compounds by aerobic bacteria frequently begins with the dihydroxylation of the substrate by nonheme iron-containing dioxygenases. These enzymes consist of two or three soluble proteins that interact to form an electron-transport chain that transfers electrons from reduced nucleotides (NADH) via flavin and [2Fe-2S] redox centers to a terminal dioxygenase. Aromatic-ring-hydroxylating dioxygenases oxidize aromatic hydrocarbons and related compounds to cis-arene diols. These enzymes utilize a mononuclear non-heme iron center to catalyze the addition of dioxygen to their respective substrates. The active site of these enzymes however is in the alpha sub-unit. No functional role has been attributed to the beta sub-unit except for a structural role
DLQAEVEQFLYREARLLDDRRWDEWLALFAEDCHYWVPARENRERRDEDPGLELSAIYDDDRRMLEDRVV
RLRTGRAWSEDPPSRTRHLVSNVRVLEGDGGEIEVRSNFVVVRTRLDGESDVFAGGRYDDLRRSEDGLRI
ASRRVVLDNDRIPTVNLSPF
>gnl|CDD|185674 cd00668, Ile_Leu_Val_MetRS_core, catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function
KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGRKKKTIWI
EEFREDPKEFVEEMSGEHKEDFRRLGISYDWSDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPVRITE
QWFFDMPKFKEKLLKALRRGKIVPEHVKNRMEAWLESLLDWAISRQRYWGTPLPEDVFDVWFDSGIGPLG
SLGYPEEKEWFKDSYPADWHLIGKDILRGWANFWITMLVALFGEIPPKNLLVHGFVLDEGGQKMSKSKGN
VIDPSDVVEKYGADALRYYLTSLAPYGDDIRL
>gnl|CDD|238358 cd00669, Asp_Lys_Asn_RS_core, Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA
FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLD
RVFEINRNFRNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLP
FPRLTYREALERYGQPLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSRLHDPDIQAEVF
QEQGINKEAGMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR
>gnl|CDD|238359 cd00670, Gly_His_Pro_Ser_Thr_tRS_core, Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA
GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRELRDTDLVLRPAAC
EPIYQIFSGEILSYRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFGEPEEAEEERREWLELAE
EIARELGLPVRVVVADDPFFGRGGKRGLDAGRETVVEFELLLPLPGRAKETAVGSANVHLDHFGASFKID
EDGGGRAHTGCGGAGGEERLVLALL
>gnl|CDD|185675 cd00671, ArgRS_core, catalytic core domain of arginyl-tRNA synthetases. Arginyl tRNA synthetase (ArgRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine
KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEKWRKLVEES
IKADLETYGRLDVRFDVWFGESSYLGLMGKVVELLEELGLLYEEDGALWLDLTEFGDDKDRVLVRSDGTY
TYFTRDIAYHLDKFERGADKIIYVVGADHHGHFKRLFAALELLGYDEAKKLEHLLYGMVNLPKEGKMSTR
AG
>gnl|CDD|173899 cd00672, CysRS_core, catalytic core domain of cysteinyl tRNA synthetase. Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding
RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDD
KIIKRAREEGLSWKEVADYYTKEFFEDMKALNVLPPDVVPRVWHIECSAMAMKYLGETFDIHGGGVDLIF
PHHENEIAQSEAATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPL
DFS
>gnl|CDD|238360 cd00673, AlaRS_core, Alanyl-tRNA synthetase (AlaRS) class II core catalytic domain. AlaRS is a homodimer. It is responsible for the attachment of alanine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its predicted structure and the presence of three characteristic sequence motifs
ASEIRETFLSFFEKKGHTRVPSSPVVPRDDPTLLFTNAGMNQFKPIFLGEVPPPANRLVNSQKCIRAGDI
DNVGKTGRHHTFFEMLGNFSFGDYFKEEAIAFAWELLTEVLGLPKDRLYVSVFEGDDEEEAIWWWKIGLP
GIRIERIGFKDNFWEMGGNGPCGPCSEIFYDRGEERDAASLPNEDDDRYLEIWNLVFMQYNRDADGTYRP
LPKKIVDTGMGLERLVWVLQGV
>gnl|CDD|173900 cd00674, LysRS_core_class_I, catalytic core domain of class I lysyl tRNA synthetase. Class I lysyl tRNA synthetase (LysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity
MHWADVIAEKIIEERKGKEKYVVASGISPSGHIHIGNFREVITADLVARALRDLGFEVRLIYSWDDYDRL
RKVPPNVPESYEQYIGMPLSSVPDPFGCCESYAEHFERPFEESLEKLGIEVEFISQSQMYKSGLYDENIL
IALEKRDEIMAILNEYRGRELQETWYPFMPYCEKCGKDTTTVEAYDAKAGTVTYKCECGHEETVDIRTGR
GKLTWRVDWPMRWAILGVDFEPFGKDHASAGGSYDTGKEIAREIFGGEPPVPVMYEFIGLKGGGKMSSSK
GNVITPSDWLEVAPPEVLRYLYARRKNPEKHIGFDLDILRLYDEYDRLERKYYGVEDAAEKEERELKRIY
ELS
>gnl|CDD|238361 cd00677, S15_NS1_EPRS_RNA-bind, S15/NS1/EPRS_RNA-binding domain. This short domain consists of a helix-turn-helix structure, which can bind to several types of RNA. It is found in the ribosomal protein S15, the influenza A viral nonstructural protein (NSA) and in several eukaryotic aminoacyl tRNA synthetases (aaRSs), where it occurs as a single or a repeated unit. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions in the formation of tRNA-synthetases into multienzyme complexes. While this domain lacks significant sequence similarity between the subgroups in which it is found, they share similar electrostatic surface potentials and thus are likely to bind to RNA via the same mechanism
EVQIALLTERIRNLKEHLAKNKKDKHSKRGLDLLVSKRLRLLKYLK
>gnl|CDD|176852 cd00680, RHO_alpha_C, C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases. C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenase (RHO) family. RHOs, also known as aromatic ring hydroxylating dioxygenases, utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC), and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this family include the alpha subunits of Pseudomonas resinovorans strain CA10 anthranilate 1,2-dioxygenase, Stenotrophomonas maltophilia dicamba O-demethylase, Ralstonia sp. U2 salicylate-5-hydroxylase, Cycloclasticus sp. strain A5 polycyclic aromatic hydrocarbon dioxygenase, toluene 2,3-dioxygenase from Pseudomonas putida F1, dioxin dioxygenase of Sphingomonas sp. Strain RW1, plant choline monooxygenase, and the polycyclic aromatic hydrocarbon (PAH)-degrading ring-hydroxylating dioxygenase from Sphingomonas CHY-1. This group also includes the C-terminal catalytic domains of MupW, part of the mupirocin biosynthetic gene cluster in Pseudomonas fluorescens, and Pseudomonas aeruginosa GbcA (glycine betaine catabolism A). This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket
GRYEYEVDCNWKLAVENFLECYHVPTVHPDTLATGLPLPLLFGDHYRVDDTGEGPGEGLSRHWGDGKGPQ
SALPGLKPGGYLYLYLFPNLMIGLYPDSLQVQQFVPIGPNKTRLEVRLYRPKDEDAREEFDAELESLAGI
LRQVLDEDIELCERIQRGLRSGAFRGGPLSPLEEGIRHFHRWLRRALG
>gnl|CDD|173831 cd00683, Trans_IPPS_HH, Trans-Isoprenyl Diphosphate Synthases, head-to-head. These trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) catalyze a head-to-head (HH) (1'-1) condensation reaction. This CD includes squalene and phytoene synthases which catalyze the 1'-1 condensation of two 15-carbon (farnesyl) and 20-carbon (geranylgeranyl) isoprenyl diphosphates, respectively. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions (DXXXD) located on opposite walls. These residues mediate binding of prenyl phosphates. A two-step reaction has been proposed for squalene synthase (farnesyl-diphosphate farnesyltransferase) in which, two molecules of FPP react to form a stable cyclopropylcarbinyl diphosphate intermediate, and then the intermediate undergoes heterolysis, isomerization, and reduction with NADPH to form squalene, a precursor of cholestrol. The carotenoid biosynthesis enzyme, phytoene synthase (CrtB), catalyzes the condensation reaction of two molecules of geranylgeranyl diphosphate to produce phytoene, a precursor of beta-carotene. These enzymes produce the triterpene and tetraterpene precursors for many diverse sterol and carotenoid end products and are widely distributed among eukareya, bacteria, and archaea
AYCRAILRKGSRSFYLASRLLPPELRRAVCALYAFCRAADDIVDDPAAPPDEKLALLDAFRAELDAAYWG
GAPTHPVLRALADLARRYGIPREPFRDLLAGMAMDLDKRRYETLDELDEYCYYVAGVVGLMLLRVFGASS
DEAALERARALGLALQLTNILRDVGEDARRGRIYLPREELARFGVTLEDLLAPENSPAFRALLRRLIARA
RAHYREALAGLAALPRRSRFCVRAAAMLYRTILDEIEARGYDVLSVRVRVPKARK
>gnl|CDD|173832 cd00684, Terpene_cyclase_plant_C1, Plant Terpene Cyclases, Class 1. This CD includes a diverse group of monomeric plant terpene cyclases (Tspa-Tspf) that convert the acyclic isoprenoid diphosphates, geranyl diphosphate (GPP), farnesyl diphosphate (FPP), or geranylgeranyl diphosphate (GGPP) into cyclic monoterpenes, diterpenes, or sesquiterpenes, respectively; a few form acyclic species. Terpnoid cyclases are soluble enzymes localized to the cytosol (sesquiterpene synthases) or plastids (mono- and diterpene synthases). All monoterpene and diterpene synthases have restrict substrate specificity, however, some sesquiterpene synthases can accept both FPP and GPP. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions located on opposite walls. These residues mediate binding of prenyl diphosphates, via bridging Mg2+ ions (K+ preferred by gymnosperm cyclases), inducing conformational changes such that an N-terminal region forms a cap over the catalytic core. Loss of diphosphate from the enzyme-bound substrate (GPP, FPP, or GGPP) results in an allylic carbocation that electrophilically attacks a double bond further down the terpene chain to effect the first ring closure. Unlike monoterpene, sesquiterene, and macrocyclic diterpenes synthases, which undergo substrate ionization by diphosphate ester scission, Tpsc-like diterpene synthases catalyze cyclization reactions by an initial protonation step producing a copalyl diphosphate intermediate. These enzymes lack the aspartate-rich sequences mentioned above. Most diterpene synthases have an N-terminal, internal element (approx 210 aa) whose function is unknown
RPSANFPPSLWGDDHFLSLSSDYSEEDELEEEIEELKEEVRKMLEDSEYPVDLFERLWLIDRLQRLGISY
HFEDEIKEILDYIYRYWTERGESNEDDLYTTALGFRLLRQHGYNVSSDVFKKFKDEDGKFKESLTQDVKG
MLSLYEASHLSFPGEDILDEALSFTTKHLEEKLESNWIIDPDLSGEIEYALEIPLHASLPRLEARWYIEF
YEQEDDHNETLLELAKLDFNILQALHQEELKILSRWWKDLDLASKLPFARDRLVECYFWAAGTYFEPQYS
LARIALAKTIALITVIDDTYDVYGTLEELELFTEAVERWDISAIDQLPEYMKIVFKALLNTVNEIEEELL
KEGGSYVVPYLKEAWKDLVKAYLVEAKWAHEGYVPTFEEYMENALVSIGLGPLLLTSFLGMGDILTEEAF
EWLESRPKLVRASSTIGRLMNDIATYEDEMKRGDVASSIECYMKEYGVSEEEAREEIKKMIEDAWKELNE
EFLKPSSDVPRPIKQRFLNLARVIDVFYKEGDGFTHPEGEIKDHITSLLFEP
>gnl|CDD|173833 cd00685, Trans_IPPS_HT, Trans-Isoprenyl Diphosphate Synthases, head-to-tail. These trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) catalyze head-to-tail (HT) (1'-4) condensation reactions. This CD includes all-trans (E)-isoprenyl diphosphate synthases which synthesize various chain length (C10, C15, C20, C25, C30, C35, C40, C45, and C50) linear isoprenyl diphosphates from precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). They catalyze the successive 1'-4 condensation of the 5-carbon IPP to allylic substrates geranyl-, farnesyl-, or geranylgeranyl-diphosphate. Isoprenoid chain elongation reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions (DDXX(XX)D) located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, protecting and stabilizing reactive carbocation intermediates. Farnesyl diphosphate synthases produce the precursors of steroids, cholesterol, sesquiterpenes, farnsylated proteins, heme, and vitamin K12; and geranylgeranyl diphosphate and longer chain synthases produce the precursors of carotenoids, retinoids, diterpenes, geranylgeranylated chlorophylls, ubiquinone, and archaeal ether linked lipids. Isoprenyl diphosphate synthases are widely distributed among archaea, bacteria, and eukareya
SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPELEAALRLAAAIELLHTASLVHDDVMDNSDLRRG
KPTVHKVFGNATAILAGDYLLARAFELLARLGNPYYPRALELFSEAILELVEGQLLDLLSEYDTDVTEEE
YLRIIRLKTAALFAAAPLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLR
EGKCTLPVLLALRELAREYEEKALEALKALPESPAREALRALADFILER
>gnl|CDD|173834 cd00686, Terpene_cyclase_cis_trans_C1, Cis, Trans, Terpene Cyclases, Class 1. This CD includes the terpenoid cyclase, trichodiene synthase, which catalyzes the cyclization of farnesyl diphosphate (FPP) to trichodiene using a cis-trans pathway, and is the first committed step in the biosynthesis of trichothecene toxins and antibiotics. As with other enzymes with the 'terpenoid synthase fold', this enzyme has two conserved metal binding motifs that coordinate Mg2+ ion-bridged binding of the diphosphate moiety of FPP. Metal-triggered substrate ionization initiates catalysis, and the alpha-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. These enzymes function as homodimers and are found in several genera of fungi
MENFPTEYFLNTTVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQQLLKVDPKRLQASLQTI
VGMVVYSWAKVSKECMADLSIHYTYTLVLDDSKDDPYPTMVNYFDDLQAGREQAHPWWALVNEHFPNVLR
HFGPFCSLNLIRSTLDFFEGCWIEQYNFGGFPGSHDYPQFLRRMNGLGHCVGASLWPKEQFNERSLFLEI
TSAIAQMENWMVWVNDLMSFYKEFDDERDQISLVKNYVVSDEISLHEALEKLTQDTLHSSKQMVAVFSDK
DPQVMDTIECFMHGYVTWHLCDRRYRLSEIYEKVKEEKTEDAQKFCKFYEQAANVGAVSPSEWAYPPVAQ
LANVRSK
>gnl|CDD|173835 cd00687, Terpene_cyclase_nonplant_C1, Non-plant Terpene Cyclases, Class 1. This CD includes terpenoid cyclases such as pentalenene synthase and aristolochene synthase which, using an all-trans pathway, catalyze the ionization of farnesyl diphosphate, followed by the formation of a macrocyclic intermediate by bond formation between C1 with either C10 (aristolochene synthase) or C11 (pentalenene synthase), resulting in production of tricyclic hydrocarbon pentalenene or bicyclic hydrocarbon aristolochene. As with other enzymes with the 'terpenoid synthase fold', they have two conserved metal binding motifs, proposed to coordinate Mg2+ ion-bridged binding of the diphosphate moiety of FPP to the enzymes. Metal-triggered substrate ionization initiates catalysis, and the alpha-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. These enzymes function in the monomeric form and are found in fungi, bacteria and Dictyostelium
PSPFPYRLNPYVKEAQDEYLEWVLEEMLIPSEKAEKRFLSADFGDLAALFYPDADDERLMLAADLMAWLF
VFDDLLDRDQKSPEDGEAGVTRLLDILRGDGLDSPDDATPLEFGLADLWRRTLARMSAEWFNRFAHYTED
YFDAYIWEGKNRLNGHVPDVAEYLEMRRFNIGADPCLGLSEFIGGPEVPAAVRLDPVMRALEALASDAIA
LVNDIYSYEKEIKANGEVHNLVKVLAEEHGLSLEEAISVVRDMHNERITQFEELEASLIKSGDLEEESPA
VRAYVEGLHNWISGNLDWHRTSP
>gnl|CDD|238362 cd00688, ISOPREN_C2_like, This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two broadly specific proteinase inhibitors alpha2-macroglobulin (alpha (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and C5 components of vertebrate complement. Class II terpene cyclases include squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY), these integral membrane proteins catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. The protein prenyltransferases include protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II) which catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Alpha (2)-M is a major carrier protein in serum and involved in the immobilization and entrapment of proteases. PZP is a pregnancy associated protein. Alpha (2)-M and PZP are known to bind to and, may modulate, the activity of placental protein-14 in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system
IEKHLKYLLRYPYGDGHWYQSLCGEQTWSTAWPLLALLLLLAATGIRDKADENIEKGIQRLLSYQLSDGG
FSGWGGNDYPSLWLTAYALKALLLAGDYIAVDRIDLARALNWLLSLQNEDGGFREDGPGNHRIGGDESDV
RLTAYALIALALLGKLDPDPLIEKALDYLLSCQNYDGGFGPGGESHGYGTACAAAALALLGDLDSPDAKK
ALRWLLSRQRPDGGWGEGRDRTNKLSDSCYTEWAAYALLALGKLGDLEDAEKLVKWLLSQQNEDGGFSSK
PGKSYDTQHTVFALLALSLY
>gnl|CDD|173825 cd00691, ascorbate_peroxidase, Ascorbate peroxidases and cytochrome C peroxidases. Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water
APVVSAAYAAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAG
LDIARKLLEPIKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADH
LRDVFYRMGFNDQEIVALSGAHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWKLPTPGLLMLPT
DKALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKLSELGVPFP
>gnl|CDD|173826 cd00692, ligninase, Ligninase and other manganese-dependent fungal peroxidases. Ligninases and related extracellular fungal peroxidases belong to class II of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites
ATCPGGQTVCNAACCVWFDILDDIQGNLFNGGECGEEAHESLRLTFHDAIGFSPALAAGQFGGGGADGSI
VLFDDIETAFHANIGLDEIVEALRPFHQKHNVSMADFIQFAGAVAVSNCPGAPRLEFYAGRKDATQPAPD
GLVPEPFDSVDKILARFADAGFSPDELVALLAAHSVAAQDFVDPSIAGTPFDSTPGVFDTQFFIETLLKG
TAFPGSGGNQGEVESPLPGEFRLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQDNISL
TDCSDVIPPPKPLSQDPTFPAGLTMDDVEQACAATPFPTLPTAPGPAT
>gnl|CDD|173827 cd00693, secretory_peroxidase, Horseradish peroxidase and related secretory plant peroxidases. Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites
QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN
LSLRGFDVIDDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGNLPSPF
FSVSQLISLFASKGLTVTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGG
DDDTLVPLDPGTPNTFDNSYYKNLLAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGN
IGVLTGSQGEIRKNCRVV
>gnl|CDD|133420 cd00704, MDH, Malate dehydrogenase. Malate dehydrogenase (MDH) is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. MDHs belong to the NAD-dependent, lactate dehydrogenase (LDH)-like, 2-hydroxycarboxylate dehydrogenase family, which also includes the GH4 family of glycoside hydrolases. They are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
LHVLITGAAGQIGYNLLFLIASGELFGDDQPVILHLLDIPPAMKALEGVVMELQDCAFPLLKGVVITTDP
EEAFKDVDVAILVGAFPRKPGMERADLLRKNAKIFKEQGEALNKVAKPTVKVLVVGNPANTNALIALKNA
PNLPPKNFTALTRLDHNRAKAQVARKLGVRVSDVKNVIIWGNHSNTQVPDLSNAVVYGPGGTEWVLDLLD
EEWLNDEFVKTVQKRGAAIIKKRGASSAASAAKAIADHVKDWLFGTPPGEIVSMGVYSPGNPYGIPPGIV
FSFPCTCKGGGWHVVEDLKLNDWLREKLKATEEELIEEKEIAL
>gnl|CDD|238363 cd00707, Pancreat_lipase_like, Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site
IDVRFLLYTRENPNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGEESWISDLRKAYLSRGDYNVI
VVDWGRGANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRI
TGLDPAGPLFSGADPEDRLDPSDAQFVDVIHTDGGLLGFSQPIGHADFYPNGGRDQPGCPKDILSSDFVA
CSHQRAVHYFAESILSPCGFVAYPCSSYDEFLAGKCFPCGSGCVRMGYHADRFRREGKFYLKTNA
>gnl|CDD|100039 cd00710, LbH_gamma_CA, Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain
DEPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEGYSVWIGKN
VSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADAL
PDVTDSAREFNEKVITVNNELAEGYKA
>gnl|CDD|238364 cd00712, AsnB, Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia
CGIAGIIGLDGASVDRATLERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQPMVSEDGRLVL
VFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRF
GIKPLYYGRDGGGLAFASELKALLALPGVPRELDEAALAEYLAFQYVPAPRTIFKGIRKLPPGHYLTVDP
GGVEIRRYWD
>gnl|CDD|238365 cd00713, GltS, Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a homodimer that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine, an important step in ammonia assimilation in bacteria, cyanobacteria and plants. The N-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamic acid and ammonia, and has a fold similar to that of other glutamine amidotransferases such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), and beta lactam synthetase (beta-LS), as well as the Ntn hydrolase folds of the proteasomal alpha and beta subunits
CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELPEAG
EYAVGMLFLPRDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGDD
GEAFERKLYLLRKRIEKAIRAADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRF
STNTFPSWPLAQPFRYLAHNGEINTIRGNRNWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVL
ELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYHSSLMEPWDGPAAIAFTDGRQVGASLDRNGLR
PARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRILDDEEIKDQLAKRH
>gnl|CDD|238366 cd00714, GFAT, Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin
CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGH
TRWATHGEPTDVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGL
DLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDG
DIAVI
>gnl|CDD|238367 cd00715, GPATase_N, Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer
CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGH
VRYSTAGSSSLENAQPFVVNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAK
DDLFEAIIDALERVKGAYSLVIMTADGLIAVRDPHGIRPLVLGKLEGDGYVVASESCALDIIGAEFVRDV
EPGEIVVIDDDGLESSQRAPKPKPAPCIFEYVYFARPDSVID
>gnl|CDD|153076 cd00716, creatine_kinase_like, Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes. Eukaryotic creatine kinase-like phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK), which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CKs are found as tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial, cytosolic, and flagellar) isoforms. Mitochondrial and cytoplasmic CKs are dimeric or octameric, while the flagellar isoforms are trimers with three CD domains fused as a single protein chain. CKs are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK, one of the most studied members of this family, this model also represents other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK), and echinoderm arginine kinase (AK)
APENFPDLSKHNNHMAKVLTPEMYAKLRDKVTPNGVTLDKCIQTGVDNPGHPFIKTVGCVAGDEESYEVF
KDLFDPVIDERHGGYKPTAKHPTDLDPTKLKGGQFDPKYVLSSRVRTGRSIRGFCLPPHCSRAERREVEK
IAVEALASLDGDLKGKYYPLSGMTEEEQQQLIEDHFLFDKPVSPLLLSSGMARDWPDARGIWHNDDKTFL
VWVNEEDHLRVISMQKGGDMKAVFARFCRGLTEVEKLMKKKGYEFMWNEHLGYVLTCPSNLGTGLRASVH
VKLPNLSKDPRFDEILRKLRLQKRGTGGVDTAAVGGTYDISNADRLGKSEVELVQFVIDGVNLLIEMEKR
LEKGKSI
>gnl|CDD|238368 cd00717, URO-D, Uroporphyrinogen decarboxylase (URO-D) is a dimeric cytosolic enzyme that decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, without requiring any prosthetic groups or cofactors. This reaction is located at the branching point of the tetrapyrrole biosynthetic pathway, leading to the biosynthesis of heme, chlorophyll or bacteriochlorophyll. URO-D deficiency is responsible for the human genetic diseases familial porphyria cutanea tarda (fPCT) and hepatoerythropoietic porphyria (HEP)
LRALRGEPVDRPPVWFMRQAGRYLPEYRELRAKYSFLELCKNPELAAEVTLQPVRRFGVDAAIIFSDILV
PLEAMGMDVEFVEGKGPVIPNPIRTEADVDRLLVPDPEEELSYVYEAIKLTRKELPGEVPLIGFAGAPWT
LASYMIEGGGSKDFAKAKKMMYTDPEAFHALLDKLTDATIEYLKAQIEAGAQAVQIFDSWAGALSPEDFE
EFVLPYLKRIIEEVKKRLPGVPVILFAKGAGGLLEDLAQLGADVVGLDWRVDLDEARKRLGPKVALQGNL
DPALLYAPKEAIEKEVKRILKAFGGAPGHIFNLGHGILPDTPPENVKALVEAVHS
>gnl|CDD|198380 cd00719, GIY-YIG_SF, GIY-YIG nuclease domain superfamily. The GIY-YIG nuclease domain superfamily includes a large and diverse group of proteins involved in many cellular processes, such as class I homing GIY-YIG family endonucleases, prokaryotic nucleotide excision repair proteins UvrC and Cho, type II restriction enzymes, the endonuclease/reverse transcriptase of eukaryotic retrotransposable elements, and a family of eukaryotic enzymes that repair stalled replication forks. All of these members contain a conserved GIY-YIG nuclease domain that may serve as a scaffold for the coordination of a divalent metal ion required for catalysis of the phosphodiester bond cleavage. By combining with different specificity, targeting, or other domains, the GIY-YIG nucleases may perform different functions
GVYVLYDEDNGLIYVGQTKNLRNRIKEHLRKQRSDWTKGLKPFEILYLEVAPEAESELLDLEAALIKKL
>gnl|CDD|238369 cd00727, malate_synt_A, Malate synthase A (MSA), present in some bacteria, plants and fungi. Prokaryotic MSAs tend to be monomeric, whereas eukaryotic enzymes are homomultimers. In general, malate synthase catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA, which hydrolyzes to malate and CoA. This reaction is part of the glyoxylate cycle, which allows certain organisms, like plants and fungi, to derive their carbon requirements from two-carbon compounds, by bypassing the two carboxylation steps of the citric acid cycle
ILTPEALDFLAELHRRFNPRRKELLAARKERQARLDAGELPDFLPETAHIRDGDWKVAPVPPDLQDRRVE
ITGPVDRKMVINALNSGAKVFMADFEDANAPTWENQVEGQINLRDAVRGTISFTSPEGKEYKLNDTPATL
IVRPRGWHLPEKHVLVDGEPVSGSLFDFGLYFFHNAKALLARGSGPYFYLPKMESHLEARLWNDVFVFAQ
DYLGLPRGTIKATVLIETLPAAFEMDEILYELRDHSAGLNCGRWDYIFSFIKKFRNHPDFVLPDRAQVTM
TVPFMRAYSELLIKTCHRRGAHAMGGMAAQIPIKDDPAANEAALAKVRADKLREATAGHDGTWVAHPGLV
PVAMEVFDKHMPGPNQLDVLREDVKVTAADLLLVPVEGGITEEGLRQNISVGLQYLAAWLRGNGCVPIYN
LMEDAATAEISRAQLWQWIRHGVRLLDDGRPVTAELVEKLLAEELAKLKAEVGQAGFATGRLAEAAELFE
ELVTAEEFPEFLTLPAYDDLV
>gnl|CDD|238370 cd00728, malate_synt_G, Malate synthase G (MSG), monomeric enzyme present in some bacteria. In general, malate synthase catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA, which hydrolyzes to malate and CoA. This reaction is part of the glyoxylate cycle, which allows certain organisms to derive their carbon requirements from two-carbon compounds, by bypassing the two carboxylation steps of the citric acid cycle
NLRVAGCLYDFVNEEALPGTGIDADAFWAGFDEIVHDLTPRNRALLAKRDELQAKIDDWHRDNPGPPLDQ
AAYKKFLKEIGYLVPEPADFTITTDNVDDEIATQAGPQLVVPLMNARYALNAANARWGSLYDALYGTDVI
PEENGAERGKGYNPVRGAKVIAYARRFLDESVPLTNGSHADATGYKVVDGQLVVTLDDGKTTTLKDPAQF
VGYRGDANAPSAVLLKHNGLHIEIQIDRNHQIGKTDPAGVKDVVVEAALTTIMDCEDSVAAVDAEDKVLV
YRNWLGLMKGDLAEEVEKNGRTFTRKLNADRNYTTPDGGEITLPGRSLMFVRNVGHLMTNDAILDSDGNE
VPEGIMDAVITSLIALHDLKGNSAFGNSRTGSIYIVKPKMHGPEEVAFANELFSRVEDLLGLPQNTIKMG
IMDEERRTSVNLKECIRAARDRVVFINTGFLDRTGDEIHTSMEAGPMARKADMKSSPWIGAYEDNNVDIG
LAAGLSGKAQIGKGMWAMPDLMADMMEQKIAHPKAGANTAWVPSPTAATLHALHYHQVNVFAVQKELAKR
RPADLDDLLTIPLAENANWSPQEIQSELDNNVQGILGYVVRWVDQGIGCSKVPDINNVGLMEDRATLRIS
SQHIANWLRHGICTKEQVQESLERMAKVVDQQNAGDPSYRPMAPDFDDSIAFKAACDLIFQGKEQPNGYT
EPLLHARRLEKK
>gnl|CDD|238371 cd00729, rubredoxin_SM, Rubredoxin, Small Modular nonheme iron binding domain containing a [Fe(SCys)4] center, present in rubrerythrin and nigerythrin and detected either N- or C-terminal to such proteins as flavin reductase, NAD(P)H-nitrite reductase, and ferredoxin-thioredoxin reductase. In rubredoxin, the iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), and believed to be involved in electron transfer. Rubrerythrins and nigerythrins are small homodimeric proteins, generally consisting of 2 domains: a rubredoxin domain C-terminal to a non-sulfur, oxo-bridged diiron site in the N-terminal rubrerythrin domain. Rubrerythrins and nigerythrins have putative peroxide activity
KVWVCPVCGYIHEGEEAPEKCPICGAPKEKFEEF
>gnl|CDD|238372 cd00730, rubredoxin, Rubredoxin; nonheme iron binding domains containing a [Fe(SCys)4] center. Rubredoxins are small nonheme iron proteins. The iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), but iron can also be replaced by cobalt, nickel or zinc. They are believed to be involved in electron transfer
KYECRICGYIYDPAEGDPDEGIPPGTPFEDLPDDWVCPVCGAGKDDFEPL
>gnl|CDD|238373 cd00731, CheA_reg, CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. Activated by the chemotaxis receptor a histidine phosphoryl group from CheA is passed directly to an aspartate in the response regulator CheY. This signalling mechanism is modulated by the methyl accepting chemotaxis proteins (MCPs). MCPs form a highly interconnected, tightly packed array within the membrane that is organized, at least in part, through interactions with CheW and CheA. The CheA regulatory domain belongs to the family of CheW_like proteins and has been proposed to mediate interaction with the kinase regulator CheW
LAIIKGLLVRVGDETYAIPLSAVVETVRIKPKDIKRVDGGKEVINVRGELLPLVRLGELFNVRGENEEPD
EGVVVVVRTGGRKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVALILDVPAL
>gnl|CDD|238374 cd00732, CheW, CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. CheW interacts with the histidine kinase CheA, most likely with the related regulatory domain of CheA. CheW is proposed to form signalling arrays together with CheA and the methyl-accepting chemotaxis proteins (MCPs), which are involved in response modulation
ELEVVTFRLGDEEYGIPIMQVREILKPTPITPIPNAPPYVLGVINLRGRIVPVIDLRKRLGLPPAEDTKN
TRIIVVEVGDQVVGLLVDSVSEVLRLSTDDIQPPPPVLSDINAKFIRGVVKLEGRLLILLDLDKILDERE
>gnl|CDD|238375 cd00733, GlyRS_alpha_core, Class II Glycyl-tRNA synthetase (GlyRS) alpha subunit core catalytic domain. GlyRS functions as a homodimer in eukaryotes, archaea and some bacteria and as a heterotetramer in the remainder of prokaryotes and in arabidopsis. It is responsible for the attachment of glycine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. This alignment contains only sequences from the GlyRS form which heterotetramerizes. The homodimer form of GlyRS is in a different family of class II aaRS. Class II assignment is based upon structure and the presence of three characteristic sequence motifs
TFQDLILKLQKFWASQGCLIIQPYDMEVGAGTFHPATFLRALGPEPWNVAYVEPSRRPTDGRYGENPNRL
QHYYQFQVIIKPSPDNIQELYLESLEALGINPKEHDIRFVEDNWESPTLGAWGLGWEVWLDGMEVTQFTY
FQQVGGIPCKPISVEITYGLERIAMYLQGVDNVYDIEWNKKITYGDVFLQNEIEQSVYNFEYANVDMLFQ
LFEDYEKEAKRLLELGLPLPAYDYVLKCSHTFNLLDARGAISVTERQRYILRIRNLAREIAKLYVEQRE
>gnl|CDD|381597 cd00735, T4-like_lys, bacteriophage T4-like lysozymes. Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium
TIREMLRQDEGYRLKAYKDTEGYPTIGIGHLIGKKGASLTNGTITKDEAEALFEQDVDRAVRDMLRNPKL
APVYAQLNAARRMALINMAFQMGVGGLAKFKNMLAAIKAGDWEEAADGMLNSLWAKQTPNRANRVSAVMR
TGTWAP
>gnl|CDD|381598 cd00736, lambda_lys-like, Bacteriophage lambda lysozyme and similar proteins. Lysozyme from bacteriophage lambda hydrolyzes the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), as do other lysozymes. However, unlike other lysozymes, bacteriophage lambda does not produce a reducing end upon cleavage of the peptidoglycan, but rather uses the 6-OH of the same MurNAc residue to produce a 1,6-anhydromuramic acid terminal residue and is therefore a lytic transglycosylase. An identical 1,6-anhydro bond is formed in bacterial peptidoglycans by the action of the lytic transglycosylases of E. coli, though they differ structurally
PNVRAFLDMIAVAEGTSGDDGYRVLFGGGLFSDFSDHPRILVCRKGGGLKSTAAGAYQFLGRTWDDLAKQ
LGLPDFSPESQDLAAIALIKERGALDDILAGRIEEAIAKLAKEWASLPGSGYGQPEHSMEELLAKYEKAL
G
>gnl|CDD|381599 cd00737, lyz_endolysin_autolysin, endolysin and autolysin. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan
GLDLIKEFEGLRLKAYRDPAGVWTIGYGHTGGVVVKPGDTITEAQAEALLRQDLARFEAAVNRLVKVPLN
QNQFDALVSFAFNVGAGAFKSSTLLRKLNAGDYAGAADEFLRWNKAGGKVLPGLVRRRAAEAALFL
>gnl|CDD|238379 cd00738, HGTP_anticodon, HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b)
PIDVAIVPLTDPRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGK
VTVKSRDTGESETLHVDELPEFLV
>gnl|CDD|238380 cd00739, DHPS, DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS
TQIMGILNVTPDSFSDGGRFLSLDKAVAHAEKMIAEGADIIDIGGESTRPGADPVSVEEELERVIPVLEA
LRGELDVLISVDTFRAEVARAALEAGADIINDVSGGSDDPAMLEVAAEYGAPLVLMHMRGTPKTMQENPY
YEDVVDEVLSFLEARLEAAESAGVARNRIILDPGIGFGKTPEHNLELLRRLDELKQLGLPVLVGASRKSF
IGALLGREPKDRDWGTLALSALAAANGADIVRVHDVKATRDALKVAD
>gnl|CDD|238381 cd00740, MeTr, MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH
FLNIGERTNVTGSKKFRELIKAEDYDEALDVARQQVEGGAQILDLNVDYGGLDGVSAMKWLLNLLATEPT
VPLMLDSTNWEVIEAGLKCCQGKCVVNSINLEDGEERFLKVARLAKEHGAAVVVLAFDEQGQAKTRDKKV
EIAERAYEALTEFVGFPPEDIIFDPLILPIATGIEEHRPYALETIDAIRMIKERLPAVKISLGVSNVSFG
FNPAAREALNSVFLYEAIKAGLDMAIVNAGKLAPIEDIPEEL
>gnl|CDD|238382 cd00741, Lipase, Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site
KGFYKAARSLANLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLDLRGRGLGRLVRVYTFGPPRVGN
AAFAEDRLDPSDALFVDRIVNDNDIVPRLPPGGEGYPHGGAEFYINGGKSQPGCCKNVLEAVDIDFGNIG
LSGNGLCDHLRYF
>gnl|CDD|381183 cd00742, FABP, intracellular fatty acid-binding protein family. Members of this family are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner. They protect and shuttle fatty acids within the cell and are involved in acquisition and removal of fatty acids from intracellular sites. They include cellular retinol-binding proteins (CRBPs) which participate in the cellular uptake of vitamin A in the form of free retinol, cellular retinoic acid-binding proteins (CRABPs) which participate in the metabolism of vitamin A and retinoic acid, and bind all trans retinoic acid, but not retinol, and FABPs similar to FABP3 which plays an important role in fatty acid transportation, cell growth, cell signaling, and gene transcription
KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEE
ETPDGRKVKSTYTLEGGKLVQTQKGPDGKEVTITREVVGDKLVVTMTVGDVTAKRVYKR
>gnl|CDD|381184 cd00743, lipocalin_RBP_like, retinol-binding protein 4 and similar proteins. Retinol-Binding Protein 4 (RBP4) is a plasma protein that transports retinol (vitamin A) from the liver stores to the peripheral tissues. The RBP4-retinol complex interacts with transthyretin (TTR - transports thyroxine and retinol) which protects it from renal excretion. In addition to retinol, other endogenous and synthetic retinoids bind RBP4, including all-trans and 13-cis retinoic acid, retinyl acetate, N-(ethyl)retinamide, and fenretinide. This group also includes purpurin, a retinol-specific protein that plays a role in neural retina cell adhesion during development of the chicken retina; it also binds retinol and may participate in retinol transporter in the retina. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
CRVSSFRVKENFDKARYAGTWYAMAKKDPEGLFLQDNIVAEFSVDENGTMTATAKGRVRLLNNWDVCADM
VGTFTDTEDPAKFKMKYWGVASYLQKGNDDHWVIDTDYDTYAITYSCRLLNLDGTCADSYSFVFSRDPNG
LPPEVQKIVRQRQEELCLARQYRLVVHNGYC
>gnl|CDD|238383 cd00751, thiolase, Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways
VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAG
LPESVPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLD
DGLTDPFTGLSMGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDR
DEGPRPDTTLEKLAKLKPAFKKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDP
AIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGA
RIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER
>gnl|CDD|340452 cd00754, Ubl_MoaD, ubiquitin-like (Ubl) domain found in molybdenum cofactor biosynthesis protein D (MoaD) and similar proteins. MoaD, also termed molybdopterin synthase sulfur carrier subunit, or MPT synthase subunit 1, or MPT synthase small subunit, or molybdopterin-converting factor small subunit, or molybdopterin-converting factor subunit 1, is a conserved small sulfur carrier protein that has beta-grasp ubiquitin-like (Ubl) fold involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor of a diverse group of redox enzymes. MoaD is activated in an ATP-dependent manner by sulfurtransferases similar to the activation mechanism of ubiquitin-activating enzyme E1
VKVLYFARARELAGKSEEELELPAGTTVEELLEELAAKYPALAAILKSVRVAVNQEYVDDDTELKDGDEV
AFIPPVSGG
>gnl|CDD|238384 cd00755, YgdL_like, Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown
YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVM
AERIRDINPECEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKL
DPTRIRVADISKTSGDPLARKVRKRLRKRGIFFGVPVVYSTEPPDPPKADELVCGDEVGADAALQGLRRA
GLGSASTVPAVFGLAIASEVI
>gnl|CDD|238385 cd00756, MoaE, MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor for a diverse group of redox enzymes. Moco biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), which carries the cis-dithiolene group responsible for molybdenum ligation. This dithiolene group is generated by MPT synthase in the second major step in Moco biosynthesis. MPT synthase is a heterotetramer consisting of two large (MoaE) and two small (MoaD) subunits
FDLAELLAALRDPEAGAVVTFVGTVRDHDEGKGVEALEYEAYPPMAEKELEEIAEEARERWGLLRVAIIH
RVGRLPPGEAIVLVAVSSPHRKEAFEACEFLIDRLKHRAPIWKKEIFEGGEEWV
>gnl|CDD|238386 cd00757, ThiF_MoeB_HesA_family, ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1)
RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEA
DVGQPKAEAAAERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLV
SGAVLGFEGQVTVFIPGEGPCYRCLFPEPPPPGVPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLA
GRLLLFDALSMSFRTLKL
>gnl|CDD|238387 cd00758, MoCF_BD, MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. The domain is presumed to bind molybdopterin
RVAIVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGV
GRRDVTPEALAELGEREAHGKGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL
>gnl|CDD|132997 cd00761, Glyco_tranf_GTA_type, Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities
VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARN
AGLKAARGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLLFRRELLEEIGGFDEALLSGEED
DDFLLRLLRGGKVAFR
>gnl|CDD|133442 cd00762, NAD_bind_malic_enz, NAD(P) binding domain of malic enzyme. Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts
IQGTASVAVAGLLAALKVTKKKISEHKVLFNGAGAAALGIANLIVXLXVKEGISKEEACKRIWXVDRKGL
LVKNRKETCPNEYHLARFANPERESGDLEDAVEAAKPDFLIGVSRVGGAFTPEVIRAXAEINERPVIFAL
SNPTSKAECTAEEAYTATEGRAIFASGSPFHPVELNGGTYKPGQGNNLYIFPGVALGVILCRIRHITDDV
FLSAAEAIASSVTEESLKPGRLYPPLFDIQEVSLNIAVAVAKYA
>gnl|CDD|238388 cd00763, Bacterial_PFK, Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include bacterial ATP-dependent phosphofructokinases. These are allosrterically regulated homotetramers; the subunits are of about 320 amino acids
KRIGVLTSGGDAPGMNAAIRGVVRSAIAEGLEVYGIRDGYAGLIAGDIVPLDRYSVSDIINRGGTFLGSA
RFPEFKDEEGQAKAIEQLKKHGIDALVVIGGDGSYMGAMRLTEHGFPCVGLPGTIDNDIPGTDYTIGFDT
ALNTVVEAIDRIRDTSSSHQRISVVEVMGRHCGDIALAAGIAGGAEFIVIPEAEFDREEVANRIKAGIER
GKKHAIVVVAEGVYDVDELAKEIEEATGFETRATVLGHIQRGGSPTAFDRILASRMGAYAVELLLAGKGG
LAVGIQNEQLVHHDIIDAIENMKPFKKDWLALAKKLS
>gnl|CDD|238389 cd00764, Eukaryotic_PFK, Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include eukaryotic ATP-dependent phosphofructokinases. These have evolved from the bacterial PFKs by gene duplication and fusion events and exhibit complex allosteric behavior
GAGKAIAVLTSGGDAQGMNAAVRAVVRMGIYVGAKVFFVYEGYEGLVKGGDYIKQAEWESVSNWLQEGGT
IIGSARCKEFREREGRLQAAYNLIQRGITNLCVIGGDGSLTGADLFRSEWPSLLEELVKDGKITEEEVAK
YQHLNIVGMVGSIDNDFCGTDMTIGTDSALHRICEVVDAITTTAQSHQRTFVLEVMGRHCGYLALVSGLA
TGADWIFIPERPPEDGWEDQMCRRLSEHRSRGKRLNIIIVAEGAIDDQLKPITSEDVKDLVVERLGLDTR
VTTLGHVQRGGTPSAFDRILASLMGVEAVMALLEATPDTPACVVSLNGNKAVRLPLMECVQLTKDVQKAM
DEKRFDEAAALRGKSFDKNWNLYKLLAIELPQPLPEKTNLNIAIVNVGAPAAGMNAAVRSAVRYGLAHGH
RPYAIYDGFEGLAKGQIVELGWIDVGGWTGRGGSELGTKRTLPKKDLETIAYNFQKYGIDGLIIVGGFEA
YKGLLQLREAREQYEEFCIPMVLIPATVSNNVPGTDFSLGSDTALNALMKYCDRIKQSASGTKRRVFIVE
TMGGYCGYLATMTGLAVGADAAYVFEEPFNIRDLQENVEHLTEKMKTTIGRGLVLRNEKCNENYTTVFTY
ELYSEEGKGVFDCRTNVLGHVQQGGAPSPFDRNFGTKFAVKAMKWIEQKLKENYAAGNEFANDPDFNCVN
GVKKYAVLFEPVEELKQTTFEHRIPKEQWWLSLRPLLKILAKYKISADISDHGQLEHVTRGQ
>gnl|CDD|238390 cd00765, Pyrophosphate_PFK, Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include pyrophosphate-dependent phosphofructokinases. These are found in bacteria as well as plants. These may be dimeric nonallosteric enzymes as in bacteria or allosteric heterotetramers as in plants
MVYSLVQQERINYTPKLPSVLKGDFNNIKIVEGPATSAAGDPDALAKLFPGTYGQPSVAFVPDQDAPSSA
PKLKIGIVLSGGQAPGGHNVISGLFDYLKERAKGSTLYGFKGGPAGILKCDYIELNAEYIQPYRNTGGFD
MICSGRTKIETEDQFKQAEETAKKLDLDALVVIGGDDSNTNAALLAENFRSKGLKTRVIGVPKTIDGDLK
NKEIETSFGFDTATKIYSELIGNVMRDARSTGKYWHFVKLMGRSASHIALECALKTHPNICIISEEVSAQ
KQTLKNITDYMVDVICKRAELGYNFGVVLVPEGLIEFIPEVKELIAELNEILANEVVEFNGLWKKKLTEQ
SLKLFDLLPKGVYLPLFIEAIQEQLMLERDPHGNVQVSRIETEKLLIQMVETRLEKMKQAGAYKGQFMGQ
SHFFGYEGRCAFPSNFDADYCYALGYGAGVLLNSGKTGYISSVGNLAAPVEEWTVGGVPLTMLMNMERRH
GKFKPVIKKALVDLEGAPFKKFASLREEWALKNRYIYPGPVQYTGPSEGSDELSHTLLLE
>gnl|CDD|238391 cd00768, class_II_aaRS-like_core, Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ
IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSH
IRKLPLRLAEIGPAFRNEGGRRGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKLDIVF
VEKTPGEFSPGGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARAADLYFLDEALEYRYPPTIGFGLGLER
L
>gnl|CDD|238392 cd00769, PheRS_beta_core, Phenylalanyl-tRNA synthetase (PheRS) beta chain core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure. While class II aaRSs generally aminoacylate the 3'-OH ribose of the appropriate tRNA, PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. PheRS is an alpha-2/ beta-2 tetramer. While the alpha chain contains a catalytic core domain, the beta chain has a non-catalytic core domain
PLQKLERKLRRLLAGLGFQEVITYSLTSPEEAELFDGGLDEAVELSNPLSEEYSVLRTSLLPGLLDALAR
NLNRKNKPLRLFEIGRVFLKDEDGPEEEEHLAALLSGNREPESWQGKGRPVDFYDAKGILEALLRALGII
VEFELEELDADLFHPGRSAKIYVNGEVIGFIGELHPEVLKEFDLKEPVYAFELDLDAL
>gnl|CDD|238393 cd00770, SerRS_core, Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer
DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRG
FTPVIPPFLVRKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPC
FRKEAGSAGRDTRGLFRVHQFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFA
AAKKYDIEAWMPGQGKYREISSCSNCTDFQARRLNIRYRDKKDGKKQYVHTLNGTALATPRTIVAILENY
QTEDGSVVIPEVLRPYM
>gnl|CDD|238394 cd00771, ThrRS_core, Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain
DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWD
HYRENMFPFEEEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQ
DDAHIFCTPDQIKEEIKGVLDLIKEVYSDFGFFDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLP
YEINEGEGAFYGPKIDFHVKDALGREWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERF
IGILIEHYAGKFPLWLAP
>gnl|CDD|238395 cd00772, ProRS_core, Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain
DASEKSLEHIGKAELADQGPGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAE
HDEGFSKELAVFKDAGDEELEEDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFL
RAREFIMKDGHSAHADAEEADEEFLNMLSAYAEIARDLAAIDFIEGEADEGAKFAGASKSREFEALMEDG
KAKQAETGHIFGEGFARAFDLKAKFLDKDGKEKFFEMGCWGIGISRFIGAIIEQ
>gnl|CDD|238396 cd00773, HisRS-like_core, Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain
EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSKEMYRFKDKGGRDLALRPDLTAPVAR
AVAENLLSLPLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDF
QIKINHRGILDGIAGLLEDREEYIERLIDKLDKEALAHLEKLLDYLEALGVDIKYSIDLSLVRGLDYYTG
IVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE
>gnl|CDD|238397 cd00774, GlyRS-like_core, Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a homodimer in eukaryotes, archaea and some bacteria and as a heterotetramer in the remainder of prokaryotes. It is responsible for the attachment of glycine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP binding and hydrolysis. This alignment contains only sequences from the GlyRS form which homodimerizes. The heterotetramer glyQ is in a different family of class II aaRS. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the N-terminus of the accessory subunit of mitochondrial polymerase gamma (Pol gamma b). Pol gamma b stimulates processive DNA synthesis and is functional as a homodimer, which can associate with the catalytic subunit Pol gamma alpha to form a heterotrimer. Despite significant both structural and sequence similarity with GlyRS, Pol gamma b lacks conservation of several class II functional residues
LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPELMFKTS
IGPVESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEF
FVDPEKSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRG
DRFLQHHPNESAHYASDCWDAEKLYVPGWIEVSGGADRTDYDLL
>gnl|CDD|238398 cd00775, LysRS_core, Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate
NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKR
LIVGGFERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEYGGK
ELDFTPPFKRVTMVDALKEKTGIDFPELDLEQPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTL
IQPTFIIDHPVEISPLAKRHRSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEA
MMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFPAMRP
>gnl|CDD|238399 cd00776, AsxRS_core, Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs in the core domain. This family includes AsnRS as well as a subgroup of AspRS. AsnRS and AspRS are homodimers, which attach either asparagine or aspartate to the 3'OH group of ribose of the appropriate tRNA. While archaea lack asnRS, they possess a non-discriminating aspRS, which can mischarge Asp-tRNA with Asn. Subsequently, a tRNA-dependent aspartate amidotransferase converts the bound aspartate to asparagine. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate
DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGK
PAYLAQSPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYI
FKRVLERCAKELELVNQLNRELLKPLEPFPRITYDEAIELLREKGVEEEVKWGEDLSTEHERLLGEIVKG
DPVFVTDYPKEIKPFYMKPDDDNPETVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWY
LDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPRDPK
>gnl|CDD|238400 cd00777, AspRS_core, Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain
LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQLLMVSGFD
RYFQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELTTPFPRMTYAEAM
ERYGFKFLWIVDFPLFEWDEEEGRLVSAHHPFTAPKEEDLDLLEKDPEDARAQAYDLVLNGVELGGGSIR
IHDPDIQEKVFEILGLSEEEAEEKFGFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFPKTQN
>gnl|CDD|238401 cd00778, ProRS_core_arch_euk, Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria
DFSEWYTEVITKAELIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKE
HIEGFAPEVAWVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFL
RTREFLWQEGHTAHATEEEAEEEVLQILDLYKEFYEDLLAIPVVKGRKTEWEKFAGADYTYTIEAMMPDG
RALQSGTSHNLGQNFSKAFDIKYQDKDGQKEYVHQTSWGISTRLIGAIIMI
>gnl|CDD|238402 cd00779, ProRS_core_prok, Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes
DAEIISHKLLLRAGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRW
DAYGPELLRLKDRHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFL
MKDAYSFDIDEESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLSPLKITKGIEVGH
IFQLGTKYSKALGATFLDENGKPKPLEMGCYGIGVSRLLAAIIEQ
>gnl|CDD|238403 cd00780, NTF2, Nuclear transport factor 2 (NTF2) domain plays an important role in the trafficking of macromolecules, ions and small molecules between the cytoplasm and nucleus. This bi-directional transport of macromolecules across the nuclear envelope requires many soluble factors that includes GDP-binding protein Ran (RanGDP). RanGDP is required for both import and export of proteins and poly(A) RNA. RanGDP also has been implicated in cell cycle control, specifically in mitotic spindle assembly. In interphase cells, RanGDP is predominately nuclear and thought to be GTP bound, but it is also present in the cytoplasm, probably in the GDP-bound state. NTF2 mediates the nuclear import of RanGDP. NTF2 binds to both RanGDP and FxFG repeat-containing nucleoporins
SAEDVAKAFVQQYYSIFDNNREGLHRLYGDTSMLSREGMKQVTGRDAIVEKLSSLPFQKTKHKITTVDSQ
PTPSGGVIVMVTGSLKLDEQPPRKFSQTFVLAPQNGGYFVLNDIFRFVD
>gnl|CDD|238404 cd00781, ketosteroid_isomerase, ketosteroid isomerase: Many biological reactions proceed by enzymatic cleavage of a C-H bond adjacent to carbonyl or a carboxyl group, leading to an enol or a enolate intermediate that is subsequently re-protonated at the same or an adjacent carbon. Ketosteroid isomerases are important members of this class of enzymes which are the most proficient of all enzymes known and have served as a paradigm for enzymatic enolizations since its discovery in 1954. This CD includes members of this class that calalyze the isomerization of various beta,gamma-unsaturated isomers at nearly a diffusion-controlled rate. These enzymes are widely distributed in bacteria
TPQEMKAAVQRYVEAVNAGDPEGIVALFADDATVEDPVGSPPRSGRAAIAAFYAQSLGGAKRLELTGPVR
ASHGGEAAFAFRVEFEWEGQPCVVRVIDVMRFDADGRIVSMRAYWGPVNLHV
>gnl|CDD|238405 cd00782, MutL_Trans, MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the C-terminal domain of DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. Included in this group are proteins similar to human MLH1, hPMS2, hPMS1, hMLH3 and E. coli MutL, MLH1 forms heterodimers with PMS2, PMS1 and MLH3. These three complexes have distinct functions in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Roles for hMLH1-hPMS1 or hMLH1-hMLH3 in MMR have not been established. Cells lacking either hMLH1 or hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 causes predisposition to HNPCC, Muir-Torre syndrome and Turcot syndrome (HNPCC variant). Mutation in hPMS2 causes predisposition to HPNCC and Turcot syndrome. Mutation in hMLH1 accounts for a large fraction of HNPCC families. There is no convincing evidence to support hPMS1 having a role in HNPCC predisposition. It has been suggested that hMLH3 may be a low risk gene for colorectal cancer; however there is little evidence to support it having a role in classical HNPCC. It has been suggested that during initiation of DNA mismatch repair in E. coli, the mismatch recognition protein MutS recruits MutL in the presence of ATP. The MutS(ATP)-MutL ternary complex formed, then recruits the latent endonuclease MutH
LKDRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGRSSKDRQFLFVNGRPVRDKLLSKAINEAYRS
YLPKGRYPVFVLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL
>gnl|CDD|238406 cd00786, cytidine_deaminase-like, Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine deaminases, nucleoside deaminases, deoxycytidylate deaminases and riboflavin deaminases. Also included are the apoBec family of mRNA editing enzymes. All members are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate
MTEALKAADLGYAKESNFQVGACLVNKKDGGKVGRGCNIENAAYSMCNHAERTALFNAGSEGDTKGQMLY
VALSPCGACAQLIIELGIKDVIVVLT
>gnl|CDD|238407 cd00788, KU70, Ku-core domain, Ku70 subfamily; Ku70 is a subunit of the Ku protein, which plays a key role in multiple nuclear processes such as DNA repair, chromosome maintenance, transcription regulation, and V(D)J recombination. The mechanism underlying the regulation of all the diverse functions of Ku is still unclear, although it seems that Ku is a multifunctional protein that works in the nuclei. In mammalian cells, the Ku heterodimer recruits the catalytic subunit of DNA-dependent protein kinase (DNA-PK), which is dependent on its association with the Ku70/80 heterodimer bound to DNA for its protein kinase activity
RALFRLPLELGPGNKLVISVKGYSLVSHAKKPRKYKLDREKNEERREVKSKRKFFDVESGKTLEKADIKK
GYKIGGEKIIFTKEELKKIKSFGEPGLRLIGFKPRSTLKPYHNIKKSYFIYPDESDYKGSTRLFAALLRS
CLKKNKVAICWYILRKNSPPRLVALVPQEEELDEPDGQVLPPGFHLVPLPFADDIRKLPSLLEENASAES
ASDELVDKAKQIIKKLRLLSYDPDKFPNPSLQKHYKILEALALDEEDPEKPDDLTLPDTEGIDKRLGDLI
EEFKKLL
>gnl|CDD|238408 cd00789, KU_like, Ku-core domain, Ku-like subfamily; composed of prokaryotic homologs of the eukaryotic DNA binding protein Ku. The alignment includes the core domain shared by the prokaryotic YkoV-like proteins and the eukaryotic Ku70 and Ku80. The prokaryotic Ku homologs are predicted to form homodimers. It is proposed that the Ku homologs are functionally associated with ATP-dependent DNA ligase and the eukaryotic-type primase, probably as components of a double-strand break repair system
RAIWKGAISFGLVNIPVKLYSATESEDISFHQLHKKDGARIRYQRVCPETGKEVPRDDIVKGYEYEKGEY
VILTDEELEALPPESTRTIEIVDFVPLDEIDPIYFDKPYYLAPDKGGEKAYALLREALRDTGKVAIAKVV
LRTRERLAALRPRGKGLVLNTLRYPDEVRSPEELFLPIKAVKVDPKELEMAKQLIEQLTGDFDPEKYEDE
YREALMELIEAKIEGKAIEAAEPAPAASGNVVDLMEALKKSLEAAK
>gnl|CDD|238409 cd00794, NOS_oxygenase_prok, Nitric oxide synthase (NOS) prokaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. Nitric oxide synthases are homodimers. Most prokaryotes produce NO as a byproduct of denitrification, using a completely different set of enzymes than NOS. However, a few prokaryotes also have a NOS, consisting solely of the NOS oxygenase domain. Prokaryotic NOS binds to the substrate L-Arg, zinc, and to the cofactors heme and tetrahydrofolate
MLFKEARAFLTNMYEELGETGELNKRLAAVESEIDETGTYTHTTEELVYGAKMAWRNSNRCIGRLFWESL
NVRDARDVRTEEEVAEALLDHITEATNGGKIRPYITIFAPEAPGKDGPRIWNNQLIRYAGYERPGANIGD
PASAKFTRLAERLGWKGKGTNFDVLPLIIQLPGDRPKWFELPNDAVKEVPITHPHYPKIRKLGLKWYAVP
IISDMDLEIGGIHYPAAPFNGWYMGTEIGARNLADEYRYNLLPKVAEALGLDTLKNRSLWKDRALVELNV
AVLHSFKKAGVSIVDHHTAAKQFERFEEREARAGRKVTGKWSWLIPPLSPATTHIFHRGYDNTEVHPNFF
YQK
>gnl|CDD|238410 cd00795, NOS_oxygenase_euk, Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain, which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOS's also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN
FVRVKNWETGSILYDTLHSKATQDGPCTERRCLGSIMDPKKLTRRPRDGRPKEELLPQAKDFINQYYSSI
KRSGSEAHLARLEEVTKEIEATGTYQLTEDELIFGAKQAWRNAPRCIGRIQWSKLQVFDARDCTTAQEMF
EAICNHIKYATNKGNLRSAITVFPQRTDGKHDFRIWNSQLIRYAGYKQPDGSIIGDPANVEFTELCIKLG
WKPKYGRFDVLPLVLQANGEDPELFEIPPELVLEVPIEHPKYEWFKELGLKWYALPAVSNMLLEIGGLEF
TACPFNGWYMGTEIGVRDLCDQQRYNILEEVAKKMGLDTRKTSSLWKDKALVEINVAVLHSFQKANVTIV
DHHSASESFMKHMENEYRARGGCPADWVWIVPPMSGSITPVFHQEMLNYVLSPSYEYQPDPW
>gnl|CDD|271177 cd00796, INT_Rci_Hp1_C, Shufflon-specific DNA recombinase Rci and Bacteriophage Hp1_like integrase, C-terminal catalytic domain. Rci protein is a tyrosine recombinase specifically involved in Shufflon type of DNA rearrangement in bacteria. The shufflon of plasmid R64 consists of four invertible DNA segments which are separated and flanked by seven 19-bp repeat sequences. RCI recombinase facilitates the site-specific recombination between any inverted repeats results in an inversion of the DNA segment(s) either independently or in groups. HP1 integrase promotes site-specific recombination of the HP1 genome into that of Haemophilus influenza. Bacteriophage Hp1_like integrases are tyrosine based site specific recombinases. They belong to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism is essentially identical and involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA
RDRFLTEDEEARLLAALEESTNPHLRLIVLLALYTGARRGEILSLRWDDIDLEVGLIVLPETKNGKPRTV
PLSDEAIAILKELKRKRGKDGFFVDGRFFGIPIASLRRAFKKARKRAGLEDLRFHDLRHTFASRLVQAGV
PIKTVAKILGHSSIKMTMRYAH
>gnl|CDD|271178 cd00797, INT_RitB_C_like, C-terminal catalytic domain of recombinase RitB, a component of the recombinase trio. Recombinases belonging to the RitA (also known as pAE1 due to its presence in the deletion prone region of plasmid pAE1 of Alcaligenes eutrophus H1), RitB, and RitC families are associated in a complex referred to as a Recombinase in Trio (RIT) element. These RIT elements consist of three adjacent and unidirectional overlapping genes, one from each family (ritABC in order of transcription). All three integrases contain a catalytic motif, suggesting that they are all active enzymes. However, their specific roles are not yet fully understood. All three families belong to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism
YTDAEIRRLLAAADQLPPESPLRPLTYATLFGLLYATGLRVGEALRLRLEDVDLDSGILTIRQTKFGKSR
LVPLHPSTVGALRDYLARRDRLLPSPSSSYFFVSQQGGRLTGGGVYRVFRRLLRRIGLRGAGDGRGPRLH
DLRHTFAVNRLTRWYREGADVERKLPVLSTYLGHVNVTDTYWYLTATPELMELASLRL
>gnl|CDD|271179 cd00798, INT_XerDC_C, XerD and XerC integrases, C-terminal catalytic domains. XerDC-like integrases are involved in the site-specific integration and excision of lysogenic bacteriophage genomes, transposition of conjugative transposons, termination of chromosomal replication, and stable plasmid inheritance. They share the same fold in their catalytic domain containing six conserved active site residues and the overall reaction mechanism with the DNA breaking-rejoining enzyme superfamily. In Escherichia coli, the Xer site-specific recombination system acts to convert dimeric chromosomes, which are formed by homologous recombination to monomers. Two related recombinases, XerC and XerD, bind cooperatively to a recombination site present in the E. coli chromosome. Each recombinase catalyzes the exchange of one pair of DNA strand in a reaction that proceeds through a Holliday junction intermediate. These enzymes can bridge two different and well-separated DNA sequences called arm- and core-sites. The C-terminal domain binds, cleaves, and re-ligates DNA strands at the core-sites, while the N-terminal domain is largely responsible for high-affinity binding to the arm-type sites
VDEVERLLDAPDTDTPLGLRDRAILELLYASGLRVSELVGLDLSDVDLDEGLVRVTGKGNKERLVPFGSY
AVEALEEYLEERRPLLLKKKPPDALFLNKRGKRLSRRGVWRILKKYAERAGLPKHVSPHTLRHSFATHLL
EGGADLRVVQELLGHASLSTTQIYTHVSFERL
>gnl|CDD|271180 cd00799, INT_Cre_C, C-terminal catalytic domain of Cre recombinase (also called integrase). Cre-like recombinases are tyrosine based site specific recombinases. They belong to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The bacteriophage P1 Cre recombinase maintains the circular phage replicon in a monomeric state by catalyzing a site-specific recombination between two loxP sites. The catalytic core domain of Cre recombinase is linked to a more divergent helical N-terminal domain, which interacts primarily with the DNA major groove proximal to the crossover region
LKAMLATLDDTTLRGLRDRALLLLGFAGALRRSELVALRVEDLTRFVDGGLLIRLRRSKTDQDGEGEIKA
LPYGPETCPVRALRAWLEAAGIPSGPLFRRIRRGGSVGTTRLSDRSVARIVKRRAALAGLDPGDFSGHSL
RRGFATEAARAGASLPEIMAQGGHKSVATVMRYIREADRFKDNAAAKL
>gnl|CDD|271181 cd00800, INT_Lambda_C, C-terminal catalytic domain of Lambda integrase, a tyrosine-based site-specific recombinase. Lambda-type integrases catalyze site-specific integration and excision of temperate bacteriophages and other mobile genetic elements to and from the bacterial host chromosome. They are tyrosine-based site-specific recombinase and belong to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The phage lambda integrase can bridge two different and well-separated DNA sequences called arm- and core-sites. The C-terminal domain binds, cleaves and re-ligates DNA strands at the core-sites, while the N-terminal domain is largely responsible for high-affinity binding to the arm-type sites
AEYAAIYAEAPPLLRLAMELALLTGQRQGDLLRLKWSDITDGGLLVEQSKTGKKLLIPWTPSLRALVDRI
RALPRKRSEYLINSRKGGPLSYDTLKSAWRRARKAAGLKGETEGFTFHDLRAKAATDYAEQGGSTDAQAL
LGHKSDAMTERYTRKRGQKWV
>gnl|CDD|271182 cd00801, INT_P4_C, Bacteriophage P4 integrase, C-terminal catalytic domain. P4-like integrases are found in temperate bacteriophages, integrative plasmids, pathogenicity and symbiosis islands, and other mobile genetic elements. The P4 integrase mediates integrative and excisive site-specific recombination between two sites, called attachment sites, located on the phage genome and the bacterial chromosome. The phage attachment site is often found adjacent to the integrase gene, while the host attachment sites are typically situated near tRNA genes. This family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA
SPDELPELWRALDTANLSPPTKLALRLLLLTGQRIGELARARWSEIDLEEKTWTIPAERTKNKRPHRVPL
SDQALEILEELKEFTGDSGYLFPSRRKKKKPISENTINKALKRLGYKGKEFTPHDLRRTFSTLLNELGID
PEVIERLLNHVLGGVVRAAYNRYDYLEERREALQAWADYL
>gnl|CDD|173901 cd00802, class_I_aaRS_core, catalytic core domain of class I amino acyl-tRNA synthetase. Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding
TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIE
RIKEDVEYMFLQAADFLLLYETECDIHLGGSDQLGHIELGLELLKKAGGPARPFGLTFGRVMGADGTKMS
KSK
>gnl|CDD|173902 cd00805, TyrRS_core, catalytic core domain of tyrosinyl-tRNA synthetase. Tyrosinyl-tRNA synthetase (TyrRS) catalytic core domain. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formationof the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding
LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKY
YKKQLKAILDFIPPEKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYP
LLQAYDFVYLDVDLQLGGSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMSKSEGNAIWDPVLD
SPYDVYQKIRNAFDPDVLEFLKLFTFLDYEEIEELEEEHAEGPLPRDAKKALAEELTKL
>gnl|CDD|173903 cd00806, TrpRS_core, catalytic core domain of tryptophanyl-tRNA synthetase. Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding
RVLSGIQPSGSLHLGHYLGAFRFWVWLQEAGYELFFFIADLHALTVKQLDPEELRQNTRENAKDYLACGL
DPEKSTIFFQSDVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESVNIGLLTYPVLQAADILLYKACL
VPVGIDQDPHLELTRDIARRFNKLYGEIFPKPAALLSKGAFLPGLQGPSKKMSKSDPNNAIFLTDSPKEI
KKKIMKAATDGGRTEHRRDGGGPGVSNLVEIYSAFFNDDDEELEEIDEYRSGGLGYGECKKLLAEAIQEF
>gnl|CDD|185676 cd00807, GlnRS_core, catalytic core domain of glutaminyl-tRNA synthetase. Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme
KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKV
TYASDYFDQLYEYAEQLIKKGKAYVHHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYW
LCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQ
GVSKADSTIDWDKLEACVRKDLNPTAPR
>gnl|CDD|173905 cd00808, GluRS_core, catalytic core domain of discriminating glutamyl-tRNA synthetase. Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding
KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEG
PDVGGPYGPYRQSERLEIYRKYAEKLLEKGDGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYE
ALGWEPPKFAHLPLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIE
LFDLERVSKSPAIFDPEKLDWLNGQYIRE
>gnl|CDD|173906 cd00812, LeuRS_core, catalytic core domain of leucyl-tRNA synthetases. Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids
KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEY
NIKKMKEQLKRMGFSYDWRREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEAPVNWCKLLDQWFLKYSETE
WKEKLLKDLEKLDGWPEEVRAMQENWIGCSRQRYWGTPIPWTDTMESLSDSTWYYARYTDAHNLEQPYEG
DLEFDREEFEYWYPVDIYIGGKEHAPNHLLYSRFNHKALFDEGLVTDEPPKGLIVQGMVLLEGEKMSKSK
GNVVTPDEAIKKYGADAARLYILFAAPPDADFDW
>gnl|CDD|173907 cd00814, MetRS_core, catalytic core domain of methioninyl-tRNA synthetases. Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function
KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDK
YHEIFKDLFKWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLPEWREEEHY
FFRLSKFQDRLLEWLEKNPDFIWPENARNEVLSWLKEGLKDLSITRDLFDWGIPVPLDPGKVIYVWFDAL
IGYISATGYYNEEWGNSWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYLTVEGKK
MSKSRGNVVDPDDLLERYGADALRYYLLRERPEGKDSDF
>gnl|CDD|185677 cd00817, ValRS_core, catalytic core domain of valyl-tRNA synthetases. Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids
PVFVIDTPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEKKLGIEGKTRH
DLGREEFLEKCWEWKEESGGKIREQLKRLGASVDWSREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLV
NWCPKLRTAISDIEVCSRSGDVIEPLLKPQWFVKVKDLAKKALEAVKEGDIKFVPERMEKRYENWLENIR
DWCISRQLWWGHRIPAWYCKDGGHWVVAREEDEAIDKAAPEACVPCGGEELKQDEDVLDTWFSSSLWPFS
TLGWPEETKDLKKFYPTSLLVTGHDIIFFWVARMIMRGLKLTGKLPFKEVYLHGLVRDEDGRKMSKSLGN
VIDPLDVIDGYGADALRFTLASAATQGRDINL
>gnl|CDD|173909 cd00818, IleRS_core, catalytic core domain of isoleucyl-tRNA synthetases. Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids
PEFVFHDGPPYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKELGISGKKDI
EKMGIAEFNAKCREFALRYVDEQEEQFQRLGVWVDWENPYKTMDPEYMESVWWVFKQLHEKGLLYRGYKV
VPWPLIYRATPQWFIRVTKIKDRLLEANDKVNWIPEWVKNRFGNWLENRRDWCISRQRYWGTPIPVWYCE
DCGEVLVRRVPDVLDVWFDSGSMPYAQLHYPFENEDFEELFPADFILEGSDQTRGWFYSLLLLSTALFGK
APYKNVIVHGFVLDEDGRKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVYAEDLRF
>gnl|CDD|238417 cd00819, PEPCK_GTP, Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates toward gluconeogenesis. It catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate to yield phosphoenolpyruvate and carbon dioxide, using a nucleotide molecule (GTP) for the phosphoryl transfer, and has a strict requirement for divalent metal ions for activity. PEPCK's separate into two phylogenetic groups based on their nucleotide substrate specificity, this model describes the GTP-dependent group
LLEWVEEAAELCQPDSVYICDGSEEEYDRLRDLMVEQGEEIRLNKYPNSYLARSDPSDVARVESRTFICS
EDEEDAGPTNNWMDPEEMKAELKELFKGCMRGRTMYVIPFSMGPLGSPISKIGVELTDSPYVVHSMRIMT
RMGKAVLDALGEGEFVPCLHSVGAPLSAGQKDVWPCNPEKKYIVHFPEEREIWSFGSGYGGNALLGKKCF
ALRIASVMARDEGWLAEHMLILGVTNPEGEKKYFAAAFPSACGKTNLAMLIPPLPGWKVETVGDDIAWMK
FGEDGRLYAINPEAGFFGVAPGTNAKTNPNAMATLHKNTIFTNVALTEDGDVWWEGLTEEPPEHLTDWQG
LGKRWTPGDGEPAAHPNSRFTAPASQCPNIDPEWENPEGVPIDAIIFGGRRPDTVPLVYEAFNWNHGVFI
GASMGSETTAAAEGKVGVVRRDPFAMLPFCGYNMGDYFRHWLSFGRKLGAKLPKIFGVNWFRKDEDGKFL
WPGFGENSRVLKWIFRRVEGKANAIETPIGYIPKYGDLDLKGLGKSKLDFLFSVDEDYWLQELIEIEEYL
EKIGRADLPQELFDELEAL
>gnl|CDD|238418 cd00820, PEPCK_HprK, Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates toward gluconeogenesis. It catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate to yield phosphoenolpyruvate and carbon dioxide, using a nucleotide molecule (ATP or GTP) for the phosphoryl transfer, and has a strict requirement for divalent metal ions for activity. PEPCK's separate into two phylogenetic groups based on their nucleotide substrate specificity (the ATP-, and GTP-dependent groups).HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of HPr and its dephosphorylation by phosphorolysis. PEPCK and the C-terminal catalytic domain of HprK/P are structurally similar with conserved active site residues suggesting that these two phosphotransferases have related functions
GTTSLHGVLVDVYGKVGVLITGDSGIGKTELALELIKRKHRLVGDDNVEIREDSKDELIGRNPELGLEIR
LRLNIFLITKKTVNVRPGDKEGWPGFRNVAVIIEVAA
>gnl|CDD|275388 cd00821, PH, Pleckstrin homology (PH) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KEGYLLKRGGGGLKSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSIPLSGILEVEEVSPKERPHCFELVTP
DGRTYYLQADSEEERQEWLKAL
>gnl|CDD|238419 cd00822, TopoII_Trans_DNA_gyrase, TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the type found in proteins of the type IIA family of DNA topoisomerases similar to the B subunits of E. coli DNA gyrase and E. coli Topoisomerase IV which are heterodimers composed of two subunits. The type IIA enzymes are the predominant form of topoisomerase and are found in some bacteriophages, viruses and archaea, and in all bacteria and eukaryotes. All type IIA topoisomerases are related to each other at amino acid sequence level, though their oligomeric organization sometimes differs. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. TopoIIA enzymes also catenate/ decatenate duplex rings. E.coli DNA gyrase is a heterodimer composed of two subunits. E. coli DNA gyrase B subunit is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes
GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAAL
TRAINDYAKKNNLLKKKDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEE
WLEENPEEAKKILEKAILAAKAREAARKAREL
>gnl|CDD|238420 cd00823, TopoIIB_Trans, TopoIIB_Trans: Transducer domain, having a ribosomal S5 domain 2-like fold, of the type found in proteins of the type IIB family of DNA topoisomerases similar to Sulfolobus shibatae topoisomerase VI (topoVI). The sole representative of the Type IIB family is topo VI. Topo VI enzymes are heterotetramers found in archaea and plants. S. shibatae topoVI relaxes both positive and negative supercoils, and in addition has a strong decatenase activity. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes
GEENLEKGLKKELNPDFVAAVTRKPKVYRGHPFIVEVGIAYGGDIPADEKVELLRFANRVPLLYDAGACV
ITKAVESINWKRYGLEQPGQGPLVVLVHVASTKVPFTSEGKEAIADIPEIEEEIKLALQEVARKLKRYLS
KKRKERELQQK
>gnl|CDD|238421 cd00825, decarbox_cond_enzymes, decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units)
RAVITGLGSYVSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKA
MFPGASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGAL
STPEKASRTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARA
AKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAV
LMLEHGFIPPSIHIEELDEAGLNIVTETTPRELRTALLNGFGLGGTNATLVL
>gnl|CDD|238422 cd00826, nondecarbox_cond_enzymes, nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways
AGAAMTAFGKFGGENGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHA
GGLQEAPAIGMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNAKEKHIDVLINKYGMRAC
PDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFGDEASLDEIAKLRPAFDKEDFLT
AGNACGLNDGAAAAILMSEAEAQKHGLQSKAREIQALEMITDMASTFEDKKVIKMVGGDGPIEAARKALE
KAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGAS
GAAICAELCFELKGEAGKRQGAGAGLALLCIGGGGGAAMCIES
>gnl|CDD|238423 cd00827, init_cond_enzymes, "initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues
DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDI
GLLIVATESPIDKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIAS
YLLDEGSALEPTLGDGAAAMLVSRNPGILAAGIVSTHSTSDPGYDFSPYPVMDGGYPKPCKLAYAIRLTA
EPAGRAVFEAAHKLIAKVVRKALDRAGLSEDIDYFVPHQPNGKKILEAVAKKLGGPPEKASQTRWILLRR
VGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFTAEAFVL
>gnl|CDD|238424 cd00828, elong_cond_enzymes, "elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues
SRVVITGIGVVSPHGEGCDEVEEFWEALREGRSGIAPVARLKSRFDRGVAGQIPTGDIPGWDAKRTGIVD
RTTLLALVATEEALADAGITDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLSPNTV
AGWVNILLLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALSTAE
EEPEEMSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKGIARAI
RTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGA
LQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLKVRAALVNAFGFGGSNAALVL
>gnl|CDD|238425 cd00829, SCP-x_thiolase, Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein
VGVGMTPFGRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKPA
TRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPPGGLTPPALY
ALAARRYMHRYGTTREDLAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAA
VVLASEERARELTDRPVWILGVGAASDTPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCF
TIAELLALEDLGFCEKGEGGKLVREGDTAIGGDLPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGA
RQVPGARVGLAHNIGGTGSAAVVTI
>gnl|CDD|238426 cd00830, KAS_III, Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA
NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDAD
DIDLIIVATSTPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAET
LSRILDWTDRSTAVLFGDGAGAVVLEATEEDPGILDSVLGSDGSGADLLTIPAGGSRSPFEDAEGGDPYL
VMDGREVFKFAVRLMPESIEEALEKAGLTPDDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNT
SAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAALL
>gnl|CDD|238427 cd00831, CHS_like, Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions
AATILAIGTAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLCAKTGIETRYLVLPGGEETYAPRPEM
SPSLDERNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRY
NLGGMGCSAGAIALDLAKDLLEANPGARVLVVSTELCSLWYRGPDHRSMLVGNALFGDGAAAVLLSNDPR
DRRRERPLFELVRAASTLLPDSEDAMGWHLGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLGIGLFKLA
FDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAF
GPGFTCESAVW
>gnl|CDD|238428 cd00832, CLF, Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine
RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDR
MTRLALAAADWALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYQSFAWFYAVN
TGQISIRHGMRGPSGVVVAEQAGGLDALAQARRLVRRGTPLVVSGGVDSALCPWGWVAQLSSGRLSTSDD
PARAYLPFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGSGRPPGLARAIRLAL
ADAGLTPEDVDVVFADAAGVPELDRAEAAALAAVFGPRGVPVTAPKTMTGRLYAGGAPLDVATALLALRD
GVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRGGFNSALVV
>gnl|CDD|238429 cd00833, PKS, polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits
EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPGKTYTRRGGFLDDVDAFD
AAFFGISPREAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYA
ATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFS
KAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEA
QAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQPLLIGSVKSNIGHLEAAA
GLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHVI
L
>gnl|CDD|238430 cd00834, KAS_I_II, Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP
RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDR
FAQFALAAAEEALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMA
AGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRN
DDPEKASRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARA
MRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIA
TLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGHNASLVF
>gnl|CDD|269907 cd00835, RanBD_family, Ran-binding domain. The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBP2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The RanBD proteins of the nuclear pore complex (NPC): nucleoporin 1 (NUP1), NUP2, NUP61, and Nuclear Pore complex Protein 9 (npp-9) are present in the parent, but specific models were not made due to lineage. To date there been no reports of inositol phosphate or phosphoinositide binding by Ran-binding proteins
TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLT
KMGNNDRAWVWTAMDDSEDGEGKPETFAVRFKTAEDAEEFKKAFEEAQ
>gnl|CDD|275389 cd00836, FERM_C-lobe, FERM domain C-lobe. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GVEFFPVKDKSKKGSPIILGVNPEGISVYDELTGQPLVLFPWPNIKKISFSGAKKFTIVVADEDKQSKLL
FQTPSRQAKEIWKLIVGYHRFLL
>gnl|CDD|269909 cd00837, EVH1_family, EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain. The EVH1 domains are part of the PH domain superfamily. EVH1 subfamilies include Enables/VASP, Homer/Vesl, WASP, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains
SIFSARAHVMQIDDSNKNWVPAGGKGASRVSYFKDTTRNSFRIIGVDIKDKKVVINCTITKNLVYNKATQ
TFHQWADDRTVFGLNFASEEDATKFAEAVQEAL
>gnl|CDD|277317 cd00838, MPP_superfamily, metallophosphatase superfamily, metallophosphatase domain. Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LVISDIHGNLEALEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIPVYVVPGNHDIL
VTHGPPYDPLDEGSPGEDPGSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLVVNPG
>gnl|CDD|277318 cd00839, MPP_PAPs, purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain. Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
PDTPLKFAVFGDMGQNTNNSTNTLDHLEKELGNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVP
YMVAPGNHEADYNGSTSKIKFFMPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLKGDNISPQYD
WLEADLAKVDRSRTPWIIVMGHRPMYCSNDDDADCIEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCP
VYNNTVANSKDNIYTNPKGPVHIVIGAAGNDEGLDDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEW
VRNQDGQVADSFWIVK
>gnl|CDD|277319 cd00840, MPP_Mre11_N, Mre11 nuclease, N-terminal metallophosphatase domain. Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
RFLHTADWHLGYPLYGLSRREEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRL
CEAGIPVFVIAGNHDSPARVAIYGLPYLRDERLERLFEDLELRPRLLKPDWFNILLLHQGVDGAGPSDSE
RPIVPEDLLPDGFDYVALGHIHKPQIIEGGGPPIVYPGSPEPTSFS
>gnl|CDD|277320 cd00841, MPP_YfcE, Escherichia coli YfcE and related proteins, metallophosphatase domain. YfcE is a manganase-dependent metallophosphatase, found in bacteria and archaea, that cleaves bis-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine, but is unable to hydrolyze 2',3 ' or 3',5' cyclic nucleic phosphodiesters, and various phosphomonoesters, including p-nitrophenyl phosphate. This family also includes the Bacilus subtilis YsnB and Methanococcus jannaschii MJ0936 proteins. This domain family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
KIGVISDTHGNLEAIEKALELFEDGVDAVIHAGDFVSPFVLNALLELKAPLIAVRGNNDGEVDQLLGRPI
LPEFLTLEIGGLRILLTHGHLFGVLEALYLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGGR
PTYAILDIEKLEVEII
>gnl|CDD|277321 cd00842, MPP_ASMase, acid sphingomyelinase and related proteins, metallophosphatase domain. Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
FLHISDIHYDPLYKVGSEYANCRSPLCCRDESGPGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKP
DFILWTGDLVRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSNSPSWLYDA
LAELWKPWLPTEAKETFKKGGYYSVDVKDGLRVISLNTNLYYKKNFWLYSNNTDPCGQLQWLEDELEDAE
QKGEKVWIIGHIPPGLNSYDADWSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTGSPINVAYIA
PSVTPYTGNNPSFR
>gnl|CDD|277322 cd00844, MPP_Dbr1_N, Dbr1 RNA lariat debranching enzyme, N-terminal metallophosphatase domain. Dbr1 is an RNA lariat debranching enzyme that hydrolyzes 2'-5' phosphodiester bonds at the branch points of excised intron lariats. This alignment model represents the N-terminal metallophosphatase domain of Dbr1. This domain belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
IAVEGCCHGELDKIYETLEKYEKKNGTKVDLLICCGDFQAVRNEADLKCMAVPPKYKKMGDFHKYYSGEK
KAPILTIFIGGNHEASNYLWELPYGGWVAPNIYYLGYAGVVNFGGLRIGGISGIYKSHDYKKGHFERPPY
NPSTIRSAYHVRNIDVFKLKQLKHPIDIFLSHDWPRGIEKHGDKKQLLRRKPFFRQDIESGTLGSPAAEE
LLEHLKPRYWFSAHLHVKFAALVQHENQESTTPIGTTNKTKTNLETRFLALDKCLPGRDFL
>gnl|CDD|277323 cd00845, MPP_UshA_N_like, Escherichia coli UshA-like family, N-terminal metallophosphatase domain. This family includes the bacterial enzyme UshA, and related enzymes including SoxB, CpdB, YhcR, and CD73. All members have a similar domain architecture which includes an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LTILHTNDLHGHLDPHSNGGIGGAARLAGLVKQIRAENPNTLLLDAGDNFQGSPLSTLTDGEAVIDLMNA
LGYDAATVGNHEFDYGLDQLEELLKQAKFPWLSANVYEDGTGTGEPGAKPYTIITVDGVKVGVIGLTTPD
TPTVTPPEGNRGVEFPDPAEAIAEAAEELKAEGVDVIIALSHLGIDTDERLAAAVKGIDVILGGHSHTLL
EEPEVVNGTLIVQAGAYGKYVGRVDLEFDKATKNVATTSGELVDV
>gnl|CDD|238431 cd00851, MTH1175, This uncharacterized conserved protein belongs to a family of iron-molybdenum cluster-binding proteins that includes NifX, NifB, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme. This domain is a predicted small-molecule-binding domain (SMBD) with an alpha/beta fold that is present either as a stand-alone domain (e.g. NifX and NifY) or fused to another conserved domain (e.g. NifB) however, its function is still undetermined.The SCOP database suggests that this domain is most similar to structures within the ribonuclease H superfamily. This conserved domain is represented in two of the three major divisions of life (bacteria and archaea)
MKIAIPVSGNGGKVSPHFGRAPYFLIYDVETGKIKNVEVIENPAAHATGGAGGKAAEFLADEGVDVVIVG
GIGPRALNKLRNAGIKVYKGAEGTVEEAIEALL
>gnl|CDD|238432 cd00852, NifB, NifB belongs to a family of iron-molybdenum cluster-binding proteins that includes NifX, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme as part of nitrogen fixation in bacteria. This domain is sometimes found fused to a N-terminal domain (the Radical SAM domain) in nifB-like proteins
LVAVASKGGGRVNQHFGHATEFQIYEVSGSGVKFVEHRKVDPYCGGGDCGDEEDRLDAIIKLLSDCDAVL
CAKIGDEPKEKLEEAGIEVIEAYAGEYIEEALLELY
>gnl|CDD|238433 cd00853, NifX, NifX belongs to a family of iron-molybdenum cluster-binding proteins that includes NifB, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme. The protein is part of the nitrogen fixation gene cluster in nitrogen-fixing bacteria and has sequence similarity to other members of the cluster
KVAFASSDLERVDAHFGSARRFAIYEVSPEGARLVEVRSFGGALEDGNEDKLAARLEALEDCAILYCAAI
GGPAAARLVRAGIHPIKVPEGEPIAELLEELQ
>gnl|CDD|238434 cd00854, NagA, N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling
LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDGT
AEALKTIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEILGIHLEGPFISPEKKGAHPP
EYLRAPDPEELKKWLEAAGGLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATH
VTHLFNAMSPLHHREPGVVGAALSDDDVYAELIADGIHVHPAAVRLAYRAKGADKIVLVTDAMAAAGLPD
GEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAVRNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSL
KPGKDADLVVLDDDLNVKATWING
>gnl|CDD|349487 cd00855, SWIB-MDM2, SWIB/MDM2 domain family. The SWIB/MDM2 protein domain, short for SWI/SNF complex B/MDM2, has been found in both SWI/SNF complex B (SWIB) and the negative regulator of the p53 tumor suppressor MDM2, which are homologous and share a common fold. The SWIB domain is a conserved region found within proteins in the SWI/SNF (SWItch/Sucrose Non-Fermentable) family of complexes. SWI/SNF complex proteins display helicase and ATPase activities and are thought to regulate transcription of certain genes by altering the chromatin structure around those genes. The mammalian complexes are made up of 9-12 proteins called BAFs (BRG1-associated factors). MDM2 is an inhibitor of p53 tumor repressor. It binds to the transactivation domain and down-regulates the ability of p53 to activate transcription. This family corresponds to the SWIB domain and the p53 binding domain of MDM2
LSPELEALLKSYETFTLKEILQALWQYIKKKNLMDPDDPSIVVCDERLRQLFEVPSFPFSEIPKALKKH
>gnl|CDD|238435 cd00858, GlyRS_anticodon, GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only
LLEHSFRVREGDEGRIVLRLPPALAPIKVAVLPLVKRDELVEIAKEISEELRELGFSVKYDDSGSIGRRY
ARQDEIGTPFCVTVDFDTLEDGTVTIRERDSMRQVRVKIEELPSYLRELIR
>gnl|CDD|238436 cd00859, HisRS_anticodon, HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only
EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTV
KDLETGEQETVALDELVEELK
>gnl|CDD|238437 cd00860, ThrRS_anticodon, ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only
PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSV
RTRDGGDLGSMSLDEFIEKLK
>gnl|CDD|238438 cd00861, ProRS_anticodon_short, ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only
PFDVVIIPMNMKDEVQQELAEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSAAEGI
VEIKVRKTGEKEEISIDELLEFLQ
>gnl|CDD|238439 cd00862, ProRS_anticodon_zinc, ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs
GLVLPPRVAPIQVVIVPIGIKDEKREEVLEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPL
RIEIGPRDLEKNTVVIVRRDTGEKKTVPLAELVEKVPELLDEIQEDLYERALEFRDATRIVDTWEEFKEA
LNEKGIVLAPWCGEEECEEEIKEETAATILCIPFDEAKLEEGGKCVVCGRPAKAYARFAKSY
>gnl|CDD|238440 cd00864, PI3Ka, Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in PI3 and PI4-kinases. Its role is unclear, but it has been suggested to be involved in substrate presentation. Phosphoinositide 3-kinases play an important role in a variety of fundamental cellular processes and can be divided into three main classes, defined by their substrate specificity and domain architecture
AWERKPLLAILLYPPFSTLTEEEKELLWKFRYYLLNVPKALPKLLKSVNWNDDEEVSELYQLLKWWAPLS
PEDALELLSPKYPDPVVRQYAVRVLESASDDELLLYLPQLVQALKYEPYLDSYLARFLLERALKSQRLGH
QLYWNLKSEIHD
>gnl|CDD|176643 cd00865, PEBP_bact_arch, PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in bacteria and archaea. PhosphatidylEthanolamine-Binding Proteins (PEBPs) are represented in all three major phylogenetic divisions (eukaryotes, bacteria, archaea). The members in this subgroup are present in bacterial and archaea. Members here include Escherichia coli YBHB and YBCL which are thought to regulate protein phosphorylation as well as Sulfolobus solfataricus SsCEI which inhibits serine proteases alpha-chymotrypsin and elastase. Although their overall structures are similar, the members of the PEBP family have very different substrates and oligomerization states (monomer/dimer/tetramer). In a few of the bacterial members present here the dimerization interface is proposed to form the ligand binding site, unlike in other PEBP members
KLTSPAFFDGGPIPKKYAFTCDGENVSPPLSWSGVPAGTKSLALIVEDPDAPTGGGFVHWVVWNIPADTT
ELPEGASRGALPAGAVQGRNDFGEAGYGGPCPPDGGPHRYVFTVYALDVPLLLPPGATRAELLFAMKGHV
LAKAELTGTY
>gnl|CDD|176644 cd00866, PEBP_euk, PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes. PhosphatidylEthanolamine-Binding Proteins (PEBPs) are represented in all three major phylogenetic divisions (eukaryotes, bacteria, archaea). The members in this subgroup are present in eukaryotes. Members here include those in plants such as Arabidopsis thaliana FLOWERING LOCUS (FT) and TERMINAL FLOWER1 (FT1) which function as a promoter and a repressor of the floral transitions, respectively as well as the mammalian Raf kinase inhibitory protein (RKIP) which inhibits MAP kinase (Raf-MEK-ERK), G protein-coupled receptor (GPCR) kinase and NFkappaB signaling cascades. Although their overall structures are similar, the members of the PEBP family have very different substrates and oligomerization states (monomer/dimer/tetramer)
VDLTVSYGSSGVVTPGNLLTPSETQKAPTVSFSSEDPPDKLYTLVMVDPDAPSRDDPKFREWLHWLVTNI
PGSDTTTGLVSKGEVLVPYLGPGPPKGTGPHRYVFLLFKQPGGLDFPESKLPPTSGLGRRGFDVREFAKK
NGLGLPVAANFFQV
>gnl|CDD|173836 cd00867, Trans_IPPS, Trans-Isoprenyl Diphosphate Synthases. Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of class 1 isoprenoid biosynthesis enzymes which either synthesis geranyl/farnesyl diphosphates (GPP/FPP) or longer chained products from isoprene precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), or use geranyl (C10)-, farnesyl (C15)-, or geranylgeranyl (C20)-diphosphate as substrate. These enzymes produce a myriad of precursors for such end products as steroids, cholesterol, sesquiterpenes, heme, carotenoids, retinoids, diterpenes, ubiquinone, and archaeal ether linked lipids; and are widely distributed among archaea, bacteria, and eukareya. The enzymes in this family share the same 'isoprenoid synthase fold' and include the head-to-tail (HT) IPPS which catalyze the successive 1'-4 condensation of the 5-carbon IPP to the growing isoprene chain to form linear, all-trans, C10-, C15-, C20- C25-, C30-, C35-, C40-, C45-, or C50-isoprenoid diphosphates. The head-to-head (HH) IPPS catalyze the successive 1'-1 condensation of 2 farnesyl or 2 geranylgeranyl isoprenoid diphosphates. Isoprenoid chain elongation reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, stabilizing reactive carbocation intermediates. Mechanistically and structurally distinct, cis-IPPS are not included in this CD
SRPLLVLLLARALGGDLEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLRRFGNALAILAGDYL
LARAFQLLARLGYPRALELFAEALRELLEGQALDLEFERDTYETLDEYLEYCRYKTAGLVGLLCLLGAGL
SGADDEQAEALKDYGRALGLAFQLTDDLLDVFGDAEELGKVGSDLREGRITLPVILARERAAEYAEEAYA
ALEALPPSLPRARRALIALADFLYRR
>gnl|CDD|173837 cd00868, Terpene_cyclase_C1, Terpene cyclases, Class 1. Terpene cyclases, Class 1 (C1) of the class 1 family of isoprenoid biosynthesis enzymes, which share the 'isoprenoid synthase fold' and convert linear, all-trans, isoprenoids, geranyl (C10)-, farnesyl (C15)-, or geranylgeranyl (C20)-diphosphate into numerous cyclic forms of monoterpenes, diterpenes, and sesquiterpenes. Also included in this CD are the cis-trans terpene cyclases such as trichodiene synthase. The class I terpene cyclization reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, stabilizing reactive carbocation intermediates. Mechanistically and structurally distinct, class II terpene cyclases and cis-IPPS are not included in this CD. Taxonomic distribution includes bacteria, fungi and plants
LHQEELKELSRWWKELGLQEKLPFARDRLVECYFWAAGSYFEPQYSEARIALAKTIALLTVIDDTYDDYG
TLEELELFTEAVERWDISAIDELPEYMKPVFKALYDLVNEIEEELAKEGGSESLPYLKEAWKDLLRAYLV
EAKWANEGYVPSFEEYLENRRVSIGYPPLLALSFLGMGDILPEEAFEWLPSYPKLVRASSTIGRLLNDIA
SYEKEIARGEVANSVECYMKEYGVSEEEALEELRKMIEEAWKELNEEVLKLSSDVPRAVLETLLNLARGI
YVWY
>gnl|CDD|238441 cd00869, PI3Ka_II, Phosphoinositide 3-kinase (PI3K) class II, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. In general, class II PI3-kinases phosphorylate phosphoinositol (PtdIns), PtdIns(4)-phosphate, but not PtdIns(4,5)-bisphosphate. They are larger, having a C2 domain at the C-terminus
IETQEKLLDLIQKQSTYTLSTEDKDLLWEKRLYCTNEPNALPLVLASAPSWDWANLMDVYQLLHQWAPLR
PLIALELLLPKFPDQEVRAHAVQWLARLSNDELLDYLPQLVQALKFELYLKSALVRFLLSRSLVSLRFAH
ELYWLLKDALDDCYFSSAYQDLGAALRCQ
>gnl|CDD|238442 cd00870, PI3Ka_III, Phosphoinositide 3-kinase (PI3K) class III, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. In general, PI3Ks class III phosphorylate phosphoinositol (PtdIns) only. The prototypical PI3K class III, yeast Vps34, is involved in trafficking proteins from Golgi to the vacuole
DKDLKPNSKERKELNKILKYPPTTKLTDEEKDLIWKFRFYLTNNKKALTKFLKSVNWSDEQEVKQALELM
PKWAKIDIEDALELLSPYFTNPVVRKYAVSRLKLASDEELLLYLLQLVQALKYENLDLSPLPRLDSPLAD
FLIERALKNPKLANFLYWYLKVELED
>gnl|CDD|238443 cd00871, PI4Ka, Phosphoinositide 4-kinase(PI4K), accessory domain (PIK domain); PIK domain is conserved in PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. PI4K phosphorylates hydroxylgroup at position 4 on the inositol ring of phosphoinositide, the first commited step in the phosphatidylinositol cycle
AWAISPRLAIHLPSRFPNSKLKSEVTRLVRKHPLAVVKIPEALPFLVTGKSVDENSPDLKYLLYWAPVSP
VQALSLFTPQYPGHPLVLQYAVRVLESYPVETVFFYIPQIVQALRYDKMGYVEEYILETAKRSQLFAHQI
IWNMQTNCYKDEEGKPKDPAIKPTLDRVMEKIIDS
>gnl|CDD|238444 cd00872, PI3Ka_I, Phosphoinositide 3-kinase (PI3K) class I, accessory domain; PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. In general, PI3K class I prefer phosphoinositol (4,5)-bisphosphate as a substrate. Mammalian members interact with active Ras. They form heterodimers with adapter molecules linking them to different signaling pathways
NEEREQLEAIIARDPLSELTEEDKELLWKLRHECRKKPQALPKLLLSVKWNKRDDVAQMYQLLKRWPKLK
PEQALELLDCNFPDEHVREFAVRCLEKLSDDELLQYLLQLVQVLKYEPYHDSDLVRFLLKRALRNQRIGH
FFFWHLRSEMHNPSVSQRFGLLLEAYLRGCG
>gnl|CDD|238445 cd00873, KU80, Ku-core domain, Ku80 subfamily; Ku80 is a subunit of the Ku protein, which plays a key role in multiple nuclear processes such as DNA repair, chromosome maintenance, transcription regulation, and V(D)J recombination. The mechanism underlying the regulation of all the diverse functions of Ku is still unclear, although it seems that Ku is a multifunctional protein that works in nuclei. In mammalian cells, the Ku heterodimer recruits the catalytic subunit of DNA-dependent protein kinase (DNA-PK), which is dependent on its association with the Ku70/80 heterodimer bound to DNA for its protein kinase activity
VAAFKGQLTLGSPLSIAVELYKKTKEERPPKLKKVSDAEKTGEDAFEDVKSERSYDVNDDDKTEVEKEDL
IKGYRYGRDIVPLSEEDEEATKLSTSKGLDILGFIKASNVPRYYLMGESSYVVPQQDDEAAALAFSALVR
ALAELDKYAIARYVYKDNSEPQLGVLFPRIKEDYECLVLVRLPFAEDVRQYRFPSLDKLKTPNLPTEEQL
EAMDDLVDSMDLDDDEEDDPEEALKPDETPNPVLQRIYQALRHRALHPDEPLPPLLQVLLRYLEPPEEVL
EKSKEALKKIKEKFPLKEVP
>gnl|CDD|238446 cd00874, RNA_Cyclase_Class_II, RNA 3' phosphate cyclase domain (class II). These proteins function as RNA cyclase to catalyze the ATP-dependent conversion of 3'-phosphate to a 2'.3'-cyclic phosphodiester at the end of RNA molecule. A conserved catalytic histidine residue is found in all members of this subfamily
IDGSYGEGGGQILRTALALSAVTGKPVRIVNIRANRSNPGLSRQHLTAVRAAARICNAEVEGAELGSTEL
EFEPGKIKGGDYEFDIGTAGSITLVLQTLLPALLFADGPSTVTISGGTDVPWAPPIDYLRNVTLPLLERM
GIEAELEVLRRGFYPRGGGEVVLTVEPSKLLPPLLLEERGEIEKIRGISHAANLPPHVAERQAEAAAALL
RKALGLQIEIEPEDQSALGPGSGIVLWAEYEHSRLGFSALGKKGVPAEKVGEEAAEELLAYLSSGAAVDE
HLADQLIPFMALAGGSEFRTGELTLHLQTNIWVIEKFLGVKFRIEE
>gnl|CDD|238447 cd00875, RNA_Cyclase_Class_I, RNA 3' phosphate cyclase domain (class I) This subfamily of cyclase-like proteins are encoded in eukaryotic genomes. They lack a conserved catalytic histidine residue required for cyclase activity, so probably do not function as cyclases. They are believed to play a role in ribosomal RNA processing and assembly
TKKILIFKGSNFFRQRLVLATLSGKPIIIKKIRSDDTNPGLRDHEVSFLRLLEKVTNGSVIEISYTGTTL
IYKPGLITGGVLNHDCPVSRGIGYFLEPLLLLAPFGKKPLSITLKGITNSTGDPSVDSIRTATLPLLKKF
GIPDEELELKILKRGVAPGGGGEVGFRCPVRKPLTPHLNDSPGRIKRIRGVAYSTRVSPSIANRMIDAAR
GVLNPFIPDVYIYTDVRKGDNSGKSPGFGISLVAETTTGVLYSAENVSPAGGESEVPEDLGRECAYQLLE
EISRGGCVDSYQQPLALLLMALGSEDVGRLRLGGPLIDEEFKIHLLRDLKEFFGIMFKIDD
>gnl|CDD|206642 cd00876, Ras, Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases). The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
KLVVLGAGGVGKSALTIRFVSGEFVEEYDPTIEDSYRKQIVVDGETYTLDILDTAGQEEFSAMRDQYIRN
GDGFILVYSITSRESFEEIKNIREQILRVKDKEDVPIVLVGNKCDLENERQVSTEEGEALAEEWGCPFLE
TSAKTNINIDELFNTLVREI
>gnl|CDD|206643 cd00877, Ran, Ras-related nuclear proteins (Ran)/TC4 family of small GTPases. Ran GTPase is involved in diverse biological functions, such as nuclear transport, spindle formation during mitosis, DNA replication, and cell division. Among the Ras superfamily, Ran is a unique small G protein. It does not have a lipid modification motif at the C-terminus to bind to the membrane, which is often observed within the Ras superfamily. Ran may therefore interact with a wide range of proteins in various intracellular locations. Like other GTPases, Ran exists in GTP- and GDP-bound conformations that interact differently with effectors. Conversion between these forms and the assembly or disassembly of effector complexes requires the interaction of regulator proteins. The intrinsic GTPase activity of Ran is very low, but it is greatly stimulated by a GTPase-activating protein (RanGAP1) located in the cytoplasm. By contrast, RCC1, a guanine nucleotide exchange factor that generates RanGTP, is bound to chromatin and confined to the nucleus. Ran itself is mobile and is actively imported into the nucleus by a mechanism involving NTF-2. Together with the compartmentalization of its regulators, this is thought to produce a relatively high concentration of RanGTP in the nucleus
FKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLDFHTNRGKIRFNVWDTAGQEKFGGLRDGYY
IQGQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKPKQITFHRKKNLQYYEIS
AKSNYNFEKPFLWLARKLLGNPNLEF
>gnl|CDD|206644 cd00878, Arf_Arl, ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases. Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions
RILMLGLDGAGKTTILYKLKLGEVVTTIPTIGFNVETVEYKNVKFTVWDVGGQDKIRPLWKHYYENTDGL
IFVVDSSDRERIEEAKNELHKLLNEEELKGAPLLILANKQDLPGALTESELIELLGLESIKGRRWHIQPC
SAVTGDGLDEGLDWLIEQ
>gnl|CDD|206645 cd00879, Sar1, Sar1 is an essential component of COPII vesicle coats. Sar1 is an essential component of COPII vesicle coats involved in export of cargo from the ER. The GTPase activity of Sar1 functions as a molecular switch to control protein-protein and protein-lipid interactions that direct vesicle budding from the ER. Activation of the GDP to the GTP-bound form of Sar1 involves the membrane-associated guanine nucleotide exchange factor (GEF) Sec12. Sar1 is unlike all Ras superfamily GTPases that use either myristoyl or prenyl groups to direct membrane association and function, in that Sar1 lacks such modification. Instead, Sar1 contains a unique nine-amino-acid N-terminal extension. This extension contains an evolutionarily conserved cluster of bulky hydrophobic amino acids, referred to as the Sar1-N-terminal activation recruitment (STAR) motif. The STAR motif mediates the recruitment of Sar1 to ER membranes and facilitates its interaction with mammalian Sec12 GEF leading to activation
FIFDWFYNVLSSLGLYKKEAKIVFLGLDNAGKTTLLHMLKDDRLAQHVPTLHPTSEELTIGNVKFTTFDL
GGHEQARRVWKDYFPEVDGIVFLVDAADPERFQESKEELDSLLNDEELANVPILILGNKIDKPGAVSEEE
LREALGLYGTTTGKGGVSLKVSNIRPVEVFMCSVVKRQGYGEGFRWLSQYL
>gnl|CDD|206646 cd00880, Era_like, E. coli Ras-like protein (Era)-like GTPase. The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family
AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLGRERVEEA
RQVADRADLVLLVVDSDLTPVEEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRERKLELLPDLPVI
AVSALPGEGIDELRKKIAELL
>gnl|CDD|206647 cd00881, GTP_translation_factor, GTP translation factor family primarily contains translation initiation, elongation and release factors. The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function
NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTP
GHEDFSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFDEVLREIK
ELLKLIGFTFLKGKDVPIIPISALTGEGIEELLDAIVEHLPPP
>gnl|CDD|206648 cd00882, Ras_like_GTPase, Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases). Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions
VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELAR
LLLRGADLILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVP
VFEVSAKTGEGVDELFEKLIE
>gnl|CDD|238448 cd00883, beta_CA_cladeA, Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes
NRAWAEEKKAKDPDFFPRLAKGQTPEYLWIGCSDSRVPENTILGLLPGEVFVHRNIANLVSPTDLNCLSV
LQYAVDVLKVKHIIVCGHYGCGGVKAALTGKRLGLLDNWLRPIRDVYRLHAAELDALEDEEERVDRLVEL
NVVEQVKNLCKTPIVQDAWKRGQELEVHGWVYDLGDGLLRDL
>gnl|CDD|238449 cd00884, beta_CA_cladeB, Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes
GFRRFRKEYFPEERELFEKLAKGQSPKALFIACSDSRVVPALITQTQPGELFVVRNVGNLVPPYEPDGGF
HGTSAAIEYAVAVLKVEHIVVCGHSDCGGIRALLSPEDLLDKLPFIGKWLRIAEPAKEVVLAELSHADFD
DQLRALEKENVLLSLENLLTYPFVRERLEAGTLSLHGWYYDIETGELYAY
>gnl|CDD|238450 cd00885, cinA, Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin
TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGP
THDDLTREAVAKAFGRPLVLDEEALERIEARFARRGREMTEANLKQAMLPEGATLLPNPVGTAPGFSVEH
NGKNVFLLPGVPSEMKPMLEEEVLPRLRER
>gnl|CDD|238451 cd00886, MogA_MoaB, MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers
LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGG
TGLAPRDVTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEV
ILPELPHLLDLL
>gnl|CDD|238452 cd00887, MoeA, MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF), an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MoeA, together with MoaB, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes
VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLRVVGE
IPAGEPPDGPLGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVL
LPAGTRLTPADIGLLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAE
VVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGR
LGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPPRVKARLAEDLKSKPGRREFLRVRLERDEGG
LVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL
>gnl|CDD|467470 cd00890, Prefoldin, prefoldin. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits; the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes, there are two or more paralogous genes encoding each subunit, adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils
QVQALSQQIEQLNRQINELEEALDELSNLDKDTEEVYRSVGGVFIEKSKEETKEELEEKLDELQKEIKKL
EQQLEAKTK
>gnl|CDD|270624 cd00891, PI3Kc, Catalytic domain of Phosphoinositide 3-kinase. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class II PI3Ks comprise three catalytic isoforms that do not associate with any regulatory subunits. They selectively use PtdIns as a susbtrate to produce PtsIns(3)P. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
REELLKQVKVLDELKEIAKKIKEEPSEERKEVLEKLLQKLELPKKFTLPLDPRMEVKGLIVEKCKVMDSK
KLPLWLVFKNADPGGDPIKVIFKAGDDLRQDQLTLQLLRIMDKLWKKEGLDLRMTPYKCIATGDEVGMIE
VVPNSETTAAIQKKYGGFGAAFKDTPISNWLKKHNPTEEEYEEAVENFIRSCAGYCVATYVLGIGDRHND
NIMVTKSGHLFHIDFGHFLGNFKKKFGIKRERAPFVFTPEMAYVMGGEDSENFQKFEDLCCKAYNILRKH
GNLLINLFSLMLSAGIPELQSIEDIEYLRDALQLDLSDEEAAEHFRKLIHESLN
>gnl|CDD|270625 cd00892, PIKKc_ATR, Catalytic domain of Ataxia telangiectasia and Rad3-related proteins. ATR is also referred to as Mei-41 (Drosophila), Esr1/Mec1p (Saccharomyces cerevisiae), Rad3 (Schizosaccharomyces pombe), and FRAP-related protein (human). ATR contains a UME domain of unknown function, a FAT (FRAP, ATM and TRRAP) domain, a catalytic domain, and a FATC domain at the C-terminus. Together with its downstream effector kinase, Chk1, ATR plays a central role in regulating the replication checkpoint. ATR stabilizes replication forks by promoting the association of DNA polymerases with the fork. Preventing fork collapse is essential in preserving genomic integrity. ATR also plays a role in normal cell growth and in response to DNA damage. ATR is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The ATR catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
ISGFEDEVEIMPSLQKPKKITLVGSDGKKYPFLCKPKDDLRKDARMMEFNTLINRLLSKDPESRRRNLHI
RTYAVIPLNEECGIIEWVPNTVTLRSILSTLYPPVLHEWFLKNFPDPTAWYEARNNYTRSTAVMSMVGYI
LGLGDRHGENILFDSTTGDVVHVDFDCLFDKGLTLEVPERVPFRLTQNMVDAMGVTGVEGTFRRTCEVTL
RVLRENRETLMSVLETFVHDPLVEWSR
>gnl|CDD|270626 cd00893, PI4Kc_III, Catalytic domain of Type III Phosphoinositide 4-kinase. PI4Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 4-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) to generate PtdIns(4)P, the major precursor in the synthesis of other phosphoinositides including PtdIns(4,5)P2, PtdIns(3,4)P2, and PtdIns(3,4,5)P3. There are two types of PI4Ks, types II and III. Type II PI4Ks lack the characteristic catalytic kinase domain present in PI3Ks and type III PI4Ks, and are excluded from this family. Two isoforms of type III PI4K, alpha and beta, exist in most eukaryotes. The PI4K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
RFGEDWTDKTERIREKSPYGNLKGWKLVSLIVKTGDDLKQEQLALQLISQFDQIFKEEGLPLWLRPYEIL
SLGPDSGIIEMIKNAVSIDSLKKKLDSFNKFVSLSDFFDDNFGDEAIQKARDNFLQSLVAYSLVCYFLQI
KDRHNGNILLDKEGHIIHIDFGFFLSSHPGFYGFEGAPFKLSSEYIEVLGGVDSELFKEFRKLFLKGFMA
LRKHSDKILSLVEMMYSGHGITCFGKKTIQQLKQRFNPELTEGELEVYVLSLINKSLDNWRTRWYDKYQY
FSQGIF
>gnl|CDD|270627 cd00894, PI3Kc_IB_gamma, Catalytic domain of Class IB Phosphoinositide 3-kinase gamma. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kgamma signaling controls diverse immune and vascular functions including cell recruitment, mast cell activation, platelet aggregation, and smooth muscle contractility. It associates with one of two regulatory subunits, p101 and p84, and is activated by G-protein-coupled receptors (GPCRs) by direct binding to their betagamma subunits. It contains an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
LHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLPESFRVPYDPGLRAGALVI
EKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYG
CISTGDKIGMIEIVKDATTIAKIQQSTVGNTGAFKDEVLNHWLKEKCPIEEKFQAAVERFVYSCAGYCVA
TFVLGIGDRHNDNIMITETGNLFHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSLHFQK
FQDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKSEEDAKKHFLDQIEVCRDK
GWTVQFNWFLHLVLGIK
>gnl|CDD|119421 cd00895, PI3Kc_C2_beta, Catalytic domain of Class II Phosphoinositide 3-kinase beta. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. The class II beta isoform, PI3K-C2beta, contributes to the migration and survival of cancer cells. It regulates Rac activity and impacts membrane ruffling, cell motility, and cadherin-mediated cell-cell adhesion. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PtdIns as a substrate to produce PtdIns(3)P, but can also phosphorylate PtdIns(4)P. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a Phox homology (PX) domain, and a second C2 domain at the C-terminus. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
REEFDRQCWLVNVLAKLAQQVREAAPSARQGILREGLEEVKQFFSINGSCRLPLSPSLLVKGIVPRDCSY
FNSNAVPLKLSFQNVDPLGENIRVIFKCGDDLRQDMLTLQMIRIMNKIWVQEGLDMRMVIFRCFSTGRGR
GMVEMIPNAETLRKIQVEHGVTGSFKDRPLADWLQKHNPTEDEYEKAVENFIYSCAGCCVATYVLGICDR
HNDNIMLKTTGHMFHIDFGRFLGHAQMFGNIKRDRAPFVFTSDMAYVINGGDKPSSRFHDFVDLCCQAYN
LIRKHTHLFLNLLGLMLSCGIPELSDLEDLKYVYDALRPQDTEADATTYFTRLIESSLGSVATKLNFFIH
NLAQ
>gnl|CDD|270628 cd00896, PI3Kc_III, Catalytic domain of Class III Phosphoinositide 3-kinase. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. Class III PI3Ks, also called Vps34 (vacuolar protein sorting 34), contain an N-terminal lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They phosphorylate only the substrate PtdIns. They interact with a regulatory subunit, Vps15, to form a membrane-associated complex. Class III PI3Ks are involved in protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
REALKRQQEFVDRLRSLMKEVKNEKGSRDKKIERLRELLSDSELGLLLFFEPLPLPLDPSVKVTGIIPEK
STVFKSALMPLKLTFKTLDGGEYKVIFKHGDDLRQDQLVLQIITLMDRLLKKENLDLKLTPYKVLATSPN
DGLVEFVPNSKALADILKKYGSILNFLRKHNPDESGPYGIKPEVMDNFVKSCAGYCVITYILGVGDRHLD
NLLLTKDGHLFHIDFGYILGRDPKPFPPPMKLCKEMVEAMGGANSEGYKEFKKYCCTAYNILRKHANLIL
NLFSLMVDANIPDIALEPDKAVLKVQEKFRLDLSDEEAEQYFQNLIDESVNALFPAVVETIHKIAQ
>gnl|CDD|132998 cd00897, UGPase_euk, Eukaryotic UGPase catalyses the synthesis of UDP-Glucose. UGPase (UDP-Glucose Pyrophosphorylase) catalyzes the reversible production of UDP-Glucose and pyrophosphate (PPi) from Glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids, glycoproteins, and proteoglycans. UGPase is found in both prokaryotes and eukaryotes. Interestingly, while the prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity. This family consists of mainly eukaryotic UTP-glucose-1-phosphate uridylyltransferases
LNKLVVLKLNGGLGTSMGCTGPKSLIEVRDGKTFLDLTVQQIEHLNKTYGVDVPLVLMNSFNTDEDTKKI
LKKYAGVNVDIHTFNQSRYPRISKETLLPVPSWADSPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYL
FVSNIDNLGATVDLRILNHMVDNKAEYIMEVTDKTRADVKGGTLIQYEGKLRLLEIAQVPKEHVDEFKSI
KKFKIFNTNNLWVNLKAVKRVVEENALDLEIIVNPKTVDGGLNVIQLETAVGAAIKNFDNALGVNVPRSR
FLPVKTTSDLLLVRSDLYSL
>gnl|CDD|132999 cd00899, b4GalT, Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids. Beta-4-Galactosyltransferase transfers galactose from uridine diphosphogalactose to the terminal beta-N-acetylglucosamine residues, hereby forming the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids. At least seven homologous beta-4-galactosyltransferase isoforms have been identified that use different types of glycoproteins and glycolipids as substrates. Of the seven identified members of the beta-1,4-galactosyltransferase subfamily (beta1,4-Gal-T1 to -T7), b1,4-Gal-T1 is most characterized (biochemically). It is a Golgi-resident type II membrane enzyme with a cytoplasmic domain, membrane spanning region, and a stem region and catalytic domain facing the lumen
RHKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCF
IFHDVDLLPENDRNLYGCEEGPRHLSVPLDKFHYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGED
DDLYNRIKAAGLKITRPSGDTGRYKMIRHIHDKRNRDNPNRFALLQNSRERDHSDGLNSLKYKVLSIELA
PLYTNILVD
>gnl|CDD|275390 cd00900, PH-like, Pleckstrin homology-like domain. The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins
LKFRAVRVYREPTKRVEGTLYITSDRLILRDKNDGGLELSIPISDIVNVNVSPQGPSSRYLVLVLKDRGE
FVGFSFPKEEDAIEISDAL
>gnl|CDD|153098 cd00904, Ferritin, Ferritin iron storage proteins. Ferritins are the primary iron storage proteins of most living organisms and members of a broad superfamily of ferritin-like diiron-carboxylate proteins. The iron-free (apoferritin) ferritin molecule is a protein shell composed of 24 protein chains arranged in 432 symmetry. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the dinuclear ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite; the protein shell can hold up to 4500 iron atoms. In vertebrates, two types of chains (subunits) have been characterized, H or M (fast) and L (slow), which differ in rates of iron uptake and mineralization. Bacterial non-heme ferritins are composed only of H chains. Fe(II) oxidation in the H/M subunits take place initially at the ferroxidase center, a carboxylate-bridged diiron center, located within the subunit four-helix bundle. In a complementary role, negatively charged residues on the protein shell inner surface of the L subunits promote ferrihydrite nucleation. Most plant ferritins combine both oxidase and nucleation functions in one chain: they have four interior glutamate residues as well as seven ferroxidase center residues
SEKVEAAVNRQLNLELYASYTYLSMATYFDRDDVALKGVAHFFKEQAQEEREHAEKFYKYQNERGGRVEL
QDIEKPPSDEWGGTLDAMEAALKLEKFVNQALLDLHELASEEKDPHLCDFLESHFLDEQVKEIKQVGDIL
TNLERLNGQQAGSGEYLFDR
>gnl|CDD|153099 cd00907, Bacterioferritin, Bacterioferritin, ferritin-like diiron-binding domain. Bacterioferritins, also known as cytochrome b1, are members of a broad superfamily of ferritin-like diiron-carboxylate proteins. Similar to ferritin in architecture, Bfr forms an oligomer of 24 subunits that assembles to form a hollow sphere with 432 symmetry. Up to 12 heme cofactor groups (iron protoporphyrin IX or coproporphyrin III) are bound between dimer pairs. The role of the heme is unknown, although it may be involved in mediating iron-core reduction and iron release. Each subunit is composed of a four-helix bundle which carries a diiron ferroxidase center; it is here that initial oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of ferric-hydroxyphosphate at the core. Some bacterioferritins are composed of two subunit types, one conferring heme-binding ability (alpha) and the other (beta) bestowing ferroxidase activity
KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNL
QRLGKLRIGEDVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLI
DKMGLQNYLQSQM
>gnl|CDD|238454 cd00912, ML, The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, Niemann-Pick type C2 (Npc2) protein, phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP), mite allergen Der p 2 and several proteins of unknown function in plants, animals and fungi. These single-domain proteins form two anti-parallel beta-pleated sheets stabilized by three disulfide bonds and with an accessible central hydrophobic cavity, and are predicted to mediate diverse biological functions through interaction with specific lipids
LVDCSDNSANIKEVLLSPCDPLPCPDHRGGNYNLSVTGTLREDIKSLYVDLALMSQGIKVLNPDNSYDFC
EAGLPKPSFCPLRKGQQYSYAKTVNVPEFTIPTIEYQVVLEDVTDKGEVLACAQATI
>gnl|CDD|238455 cd00913, PCD_DCoH_subfamily_a, PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known as DCoH (dimerization cofactor of hepatocyte nuclear factor-1), is both a transcription activator and a metabolic enzyme. DCoH stimulates gene expression by associating with specific DNA binding proteins such as HNF-1alpha (hepatocyte nuclear factor-1) and Xenopus enhancer of rudimentary homologue (XERH). DCoH also catalyzes the dehydration of 4alpha- hydroxy- tetrahydrobiopterin (4alpha-OH-BH4) to quinoiddihydrobiopterin, a percursor of the phenylalanine hydroxylase cofactor BH4 (tetrahydrobiopterin). The DCoH homodimer has a saddle-shaped structure similar to that of TBP (TATA binding protein)
GWELADDGLKLERTFRFKNFVEALEFVNAVGEIAEAEGHHPDLSLGWGRVRVTWWTHSIGGLSENDFIMA
AKIDAL
>gnl|CDD|238456 cd00914, PCD_DCoH_subfamily_b, PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known as DCoH (dimerization cofactor of hepatocyte nuclear factor-1), is both a transcription activator and a metabolic enzyme. DCoH stimulates gene expression by associating with specific DNA binding proteins such as HNF-1alpha (hepatocyte nuclear factor-1) and Xenopus enhancer of rudimentary homologue (XERH). DCoH also catalyzes the dehydration of 4alpha- hydroxy- tetrahydrobiopterin (4alpha-OH-BH4) to quinoiddihydrobiopterin, a percursor of the phenylalanine hydroxylase cofactor BH4 (tetrahydrobiopterin). The DCoH homodimer has a saddle-shaped structure similar to that of TBP (TATA binding protein). Two DCoH proteins have been identifed in humans: DCoH1 and DCoH2. Mutations in human DCoH1 cause hyperphenylalaninemia. Loss of enzymic activity of DCoH in humans is associated with the depigmentation disorder vitiligo. DCoH1 has been reported to be overexpessed in colon cancer carcinomas and in malignant melanomas
GWTLVDGRDAIHKSFKFKDFNEAFGFMTRVALEAEKMNHHPEWFNVYNKVDITLTTHDAGGLTERDIKLA
KFIEKA
>gnl|CDD|238457 cd00915, MD-1_MD-2, MD-1 and MD-2 are cofactors required for LPS signaling through cell surface receptors. MD-2 and its binding partner, Toll-like receptor 4 (TLR4), are essential for the innate immune responses of mammalian cells to bacterial lipopolysaccharide (LPS); MD-2 directly binds the lipid A moiety of LPS. The TLR4-like receptor, RP105, which mediates LPS-induced lymphocyte proliferation, interacts with MD-1; MD-1 enhances RP105-mediated LPS-induced growth of B cells. These proteins belong to the ML domain family
HWVCNSSDLEFSYSSCDPMQDFSFSAEPCSTLKGTNGFIRIKFILRRDIKELYFNLSLNVNGIEVLTRSE
IICHGYLDKYSFCGALKGETVYYVGPFSFKGILIPQGQYRCVAELIVENRETVACANFTI
>gnl|CDD|238458 cd00916, Npc2_like, Niemann-Pick type C2 (Npc2) is a lysosomal protein in which a mutation in the gene causes a rare form of Niemann-Pick type C disease, an autosomal recessive lipid storage disorder characterized by accumulation of low-density lipoprotein-derived cholesterol in lysosomes. Although Npc2 is known to bind cholesterol, the function of this protein is unknown. These proteins belong to the ML domain family
FRDCGSSRPTPSEVRISGCATLPCKLKRGSTAKVSIDFTPNFDSTSLKTEVHAILLGVPVPFPLPNPDAC
KNLGTSCPLSAGEDVTYTLSLPVLAPYPGISVTVEWELTDDDGQVLTCFQIPA
>gnl|CDD|238459 cd00917, PG-PI_TP, The phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP) has been shown to bind phosphatidylglycerol and phosphatidylinositol, but the biological significance of this is still obscure. These proteins belong to the ML domain family
FEYCDKGGEDIVKVTSVEISPNPPAAGQNLTIEASGSVGKEIEDGAYVVVEVKYGFIRLLSETYDLCDET
KNVDLSCPIEPGDKFLTKLVDLPGEIPPGKYTVSARAYTKDDEEITCLSFSV
>gnl|CDD|238460 cd00918, Der-p2_like, Several group 2 allergen proteins belong to the ML domain family. They include Dermatophagoides pteronyssinus, group 2 (Der p 2) and D. farinae, group 2 (Der f 2) allergens. These house dust mites cause heavy atopic diseases such as asthma and dermatitis. Although the allergenic properties of these proteins have been well characterized, their biological function in mites is unknown
FKDCGKGEIKSLEVDGCSGDYCVIHRGKPLTLEAKFTANQDTAKAKIKITASIDGLEIDVPGIETDGCKY
VKCPIKKGQHYDIKYTWNVPAILPKIKAVVKAVLIGDHGVLACGIVNGEV
>gnl|CDD|238461 cd00919, Heme_Cu_Oxidase_I, Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily
HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNL
LPPLIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHL
AGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDP
AGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMF
TVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPL
DIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGL
LGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL
>gnl|CDD|259860 cd00920, Cupredoxin, Cupredoxin superfamily. Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II
ITVTASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVQFVNKLGENHSVTIAGFGVPVVAMAGGANPGLVNT
LVIGPGESAEVTFTTDQAGVYWFYCTIPGHNHAGMVGTIN
>gnl|CDD|238462 cd00922, Cyt_c_Oxidase_IV, Cytochrome c oxidase subunit IV. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Found only in eukaryotes, subunit IV is the largest of the nuclear-encoded subunits. It binds ATP at the matrix side, leading to an allosteric inhibition of enzyme activity at high intramitochondrial ATP/ADP ratios. In mammals, subunit IV has a lung-specific isoform and a ubiquitously expressed isoform
EVVGYGANSLPTYADIPDRPLPMIRFRELSAEIKALREKEKGDWKQLTLEEKKALYRISFGETGPEMNAP
TGEWKTVFGGVLAFIGITGVIFGLQRAFVYGPKPHTFTEEWQEAQLERMLDMKVNPITGYASKWDY
>gnl|CDD|238463 cd00923, Cyt_c_Oxidase_Va, Cytochrome c oxidase subunit Va. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Found only in eukaryotes, subunit Va is one of three mammalian subunits that lacks a transmembrane region. Subunit Va is located on the matrix side of the membrane and binds thyroid hormone T2, releasing allosteric inhibition caused by the binding of ATP to subunit IV and allowing high turnover at elevated intramitochondrial ATP/ADP ratios
SEETDEEFDARYETYFNRPDIDGWELRRGLNNLFGYDLVPEPKVIEAALRACRRVNDFALAVRILEAIKD
KCGAHKEIYPYILQEIKPTLKELGISTPEELGY
>gnl|CDD|238464 cd00924, Cyt_c_Oxidase_Vb, Cytochrome c oxidase subunit Vb. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Found only in eukaryotes, subunit Vb is one of three mammalian subunits that lacks a transmembrane region. Subunit Vb is located on the matrix side of the membrane and binds the regulatory subunit of protein kinase A. The abnormally extended conformation is stable only in the CcO assembly
AAEGEVPTDLEQATGLERKELLAKLEGIDDFDMKPLKGPFGTKEDPNLVPSAFDKRIVGCICEPDSHDVI
WMWLEKGKPKRCPECGHVFKLVDVGPP
>gnl|CDD|238465 cd00925, Cyt_c_Oxidase_VIa, Cytochrome c oxidase subunit VIa. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Found only in eukaryotes, subunit VIa is expressed in two tissue-specific isoforms in mammals but not fish. VIa-H is the heart and skeletal muscle isoform; VIa-L is the liver or non-muscle isoform. Mammalian VIa-H induces a slip in CcO (decrease in proton/electron stoichiometry) at high intramitochondrial ATP/ADP ratios, while VIa-L induces a permanent slip in CcO, depending on the presence of cardiolipin and palmitate
ETAAKGEHAAGTSELWKKISFYVALPAVALCMLNAYLKHKEHEEHERPEFVEYEHLNIRTKPFPWGDGNK
TLFHNPHVNALPTGYE
>gnl|CDD|238466 cd00926, Cyt_c_Oxidase_VIb, Cytochrome c oxidase subunit VIb. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Found only in eukaryotes, subunit VIb is one of three mammalian subunits that lacks a transmembrane region. It is located on the cytosolic side of the membrane and helps form the dimer interface with the corresponding subunit on the other monomer complex
DAGPLTTAPFDPRFPNQNQTKHCWQRYVDYHRCIKAKGEDASPCKKFRRVYESLCPQEWLEKWDEQREEG
TFPGK
>gnl|CDD|438621 cd00927, CcO_VIc-like, Cytochrome c oxidase subunit VIc-like. Cytochrome c oxidase subunit VIc-like proteins are subunits of the cytochrome c oxidase (CcO, also called complex IV or CIV), the terminal oxidase in the mitochondrial electron transport chain which drives oxidative phosphorylation. CcO is a multi-chain transmembrane protein complex located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 14 in mammalian mitochondria. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 11 subunits are encoded within the nuclear genome. The VIc subunit-like proteins are single-pass membrane proteins found only in eukaryotes and their specific function remains unclear
LPGLIKRRLRKDIGYGLMLGLIPGTFFKFGVAEKKQKEREDFYAAYDKRK
>gnl|CDD|238468 cd00928, Cyt_c_Oxidase_VIIa, Cytochrome c oxidase subunit VIIa. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Found only in eukaryotes, subunit VIIa has two tissue-specific isoforms that are expressed in a developmental manner. VIIa-H is expressed in heart and skeletal muscle but not smooth muscle. VIIa-L is expressed in liver and non-muscle tissues
GKNKVKELQKKFQADDGLPVHLKGGVVDRILYRLTMALTVVGTGYSLYLLYMLSF
>gnl|CDD|238469 cd00929, Cyt_c_Oxidase_VIIc, Cytochrome c oxidase subunit VIIc. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. The VIIc subunit is found only in eukaryotes and its specific function remains unclear. Peroxide inactivation of bovine CcO coincides with the direct oxidation of tryptophan (W19) within subunit VIIc, along with other structural changes in other subunits
SHYGEGPGSNLPFSVTNKWRLTALFHLFFGSGFSAPFIVVRHQLLK
>gnl|CDD|238470 cd00930, Cyt_c_Oxidase_VIII, Cytochrome oxidase c subunit VIII. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Found only in eukaryotes, subunit VIII is the smallest of the nuclear-encoded subunits. It exists in muscle-specific and non-muscle-specific isoforms that are differently expressed in different species, suggesting species-specific regulation of energy metabolism
IHSKPPKTPLSAAESAIGLSVFFTTFLLPAGWVLSHLENYKKR
>gnl|CDD|238471 cd00933, barnase, Barnase, a member of the family of homologous microbial ribonucleases, catalyses the cleavage of single-stranded RNA via a two-step mechanism thought to be similar to that of pancreatic ribonuclease. The mechanism involves a transesterification to give a 2', 3'-cyclic phosphate intermediate, followed by hydrolysis to yield a 3' nucleotide. The active site residues His and Glu act as general acid-base groups during catalysis, while the Arg and Lys residues are important in binding the reactive phosphate, the latter probably binding the phosphate in the transition state. Barstar, a small 89 residue intracellular protein is a natural inhibitor of Barnase
INTFQGVADYLQTYHRLPDNYITKSQAKELGWVAPKGNLWDVAPGKSIGGDRFSNREGRLPAAGGRTWRE
ADINYQGGHRGADRLLYSNDGLIYKTTDHYRTFTRIR
>gnl|CDD|269911 cd00934, PTB, Phosphotyrosine-binding (PTB) PH-like fold. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains
ASFQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHR
ISYCGRDPDNPNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF
>gnl|CDD|238472 cd00935, GlyRS_RNA, GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes
LAPLRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDKELALQP
>gnl|CDD|238473 cd00936, WEPRS_RNA, WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes
LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG
>gnl|CDD|238474 cd00938, HisRS_RNA, HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes
AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE
>gnl|CDD|238475 cd00939, MetRS_RNA, MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes
LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK
>gnl|CDD|411993 cd00941, FokI_N, N-terminal DNA recognition domain of restriction endonuclease FokI and similar proteins. Restriction endonuclease FokI (EC3.1.21.4), also called R.FokI, or endonuclease FokI, is a type IIS restriction enzyme that require only divalent metals (such as Mg2+ or Mn2+) as cofactors to catalyze the hydrolysis of DNA. FokI recognizes the double-stranded sequence 5'-GGATG-3'/3'-CATCC-5' and cleaves 14 bases after G-1 and 13 bases before C-1, respectively. It contains an N-terminal DNA recognition domain and a C-terminal endonuclease domain. This model describes the DNA recognition domain. The family also includes endonuclease StsI, a type IIS restriction endonuclease found in Streptococcus sanguinis 54. It recognizes the same sequence as FokI but cleaves at different positions
TFGWVQNPSDFEKLKKVVQIFDPNSKIYKELRDTKIPQLIEDDDLRNELIEKLNNKPLEITYKELVGTGT
KKRGSDAVADGLIQATIPGQSRKTTYTDDWTADGFLRWAVSLGFLDYDRETDTFSITELGKELSQAEDDS
DEEKEILTEALLSYPPAVRILSLLENAGKPLTKFELGKQLGFIGEAGFTSYPQDLYIDALAEAEDKKEKK
KIRSNWEGTSDKYARMIAGWLSKLGLVKKVSKKVTVIIGGKYEESILQSYKITGKGLHALKRANGKSKNK
RIPKNVMWEMLATKGKNRNYLRTRRALILKALSESPKSLTAIQEALKINGINESPETIKDDIKGLNNIGI
RIEIDGNKYKLKDKINDFEIPVL
>gnl|CDD|411705 cd00942, BamHI-like, Restriction endonuclease BamHI and similar proteins. Restriction endonuclease BamHI (EC 3.1.21.4), also termed R.BamHI, or endonuclease BamHI, is a type II restriction enzyme that require only divalent metals (such as Mg2+ or Mn2+) as cofactors to catalyze the hydrolysis of DNA. BamHI recognizes the double-stranded sequence GGATCC and cleaves after G-1. It shows striking resemblance to the structure of EcoRI, but lacks sequence similarity between them. The family also includes a BamHI isoschizomer, OkrAI endonuclease, which recognizes and cleaves the same DNA sequence (TATGGATCCATA) as BamHI. However, OkrAI does not have the equivalent of N- and C-terminal helices of BamHI, and it has higher star activity compared to BamHI
MKIVKTYILIDAGEFSESPEWSEIREEIEDSIRSIEWPPGSGTFTINPEKNGNGVVPIKEAFMQHLKEQG
WALEKPLDLGSDTSKPGPIDAVKEFREGGLFAVEWETGNISSSHRALNKMALGLLSGEIIGGVLILPSRD
LYYYLTDRVGNFEELEPYFPLWEKLNVEEGLLAVIVIEHDALSSDVPRIPKGTDGR
>gnl|CDD|411706 cd00943, EcoRI-like, Restriction endonuclease EcoRI and similar proteins. Restriction endonuclease EcoRI (EC 3.1.21.4), also termed R.EcoRI, or endonuclease EcoRI, is a type II restriction enzyme that require only divalent metals (such as Mg2+ or Mn2+) as cofactors to catalyze the hydrolysis of DNA. EcoRI recognizes the double-stranded sequence GAATTC and cleaves after G-1. The family also includes an EcoRI isoschizomer, RsrI endonuclease, which also catalyzes the cleavage of duplex DNA and oligodeoxyribonucleotides between the first two residues of the sequence GAATTC. RsrI differs from EcoRI in its N-terminal amino acid sequence, susceptibility to inhibition by antibodies, sensitivity to N-ethylmaleimide, isoelectric point, state of aggregation at high concentrations, temperature lability, and conditions for optimal reaction. It displays a reduction of specificity ("star activity") under conditions that also relax the specificity of EcoRI
GVVGIFGDDAKIHDLEVGEISKLVLKKLEEEYPNLTFRYRTSITKKEINESLKKIDPELGQTLFVENASI
KPDGGIIEVKDDSGNWRVVLVSEAKHQGKDIENIKKGILVGKKKDQDLMAAGNAIERSHKNISEIANFML
SESHFPYILFLEGSNFLTETITVTRPDGRVVTLEYNSGILNRLDRLTAANYGMPINTNLCENKFVKHKDK
TIMLQAASIYTQGDGGKWNNEEMFEIMLEVAKTSLKILGSDLFN
>gnl|CDD|188634 cd00945, Aldolase_Class_I, Class I aldolases. Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin
IDLTLLHPDATLEDIAKLCDEAIEYGFAAVCVNPGYVRLAADALAGSDVPVIVVVGFPTGLTTTEVKVAE
VEEAIDLGADEIDVVINIGSLKEGDWEEVLEEIAAVVEAADGGLPLKVILETRGLKTADEIAKAARIAAE
AGADFIKTSTGFGGGGATVEDVKLMKEAVGGRVGVKAAGGIKTLEDALAAIEAGADGIGTS
>gnl|CDD|238476 cd00946, FBP_aldolase_IIA, Class II Type A, Fructose-1,6-bisphosphate (FBP) aldolases. The enzyme catalyses the zinc-dependent, reversible aldol condensation of dihydroxyacetone phosphate with glyceraldehyde-3-phosphate to form fructose-1,6-bisphosphate. FBP aldolase is homodimeric and used in gluconeogenesis and glycolysis. The type A and type B Class II FBPA's differ in the presence and absence of distinct indels in the sequence that result in differing loop lengths in the structures
GDDVLKLFDYAKENGFAIPAVNCTSSSTINAVLEAARDAKSPIIIQFSNGGAAFYAGKGLKNEKQKASIA
GAIAAAHHVRSMAEHYGVPVVLHTDHCAKKLLPWFDGLLEADEEYFKQHGEPLFSSHMLDLSEEPLEENI
EICKKYLERMAKINMWLEMEIGITGGEEDGVDNSGVDNAELYTQPEDVWYVYEALSKISPNFSIAAAFGN
VHGVYKPGNVKLQPEILGEHQDYVREKLGLADDKPLYFVFHGGSGSTKEEIREAISYGVVKMNIDTDTQW
AYWEGVRNYYLKNEDYLQGQIGNPEGPDKPNKKYYDPRVWLREGEKSMVARVKKAFEDLNSVNKL
>gnl|CDD|238477 cd00947, TBP_aldolase_IIB, Tagatose-1,6-bisphosphate (TBP) aldolase and related Type B Class II aldolases. TBP aldolase is a tetrameric class II aldolase that catalyzes the reversible condensation of dihydroxyacetone phosphate with glyceraldehyde 3-phsophate to produce tagatose 1,6-bisphosphate. There is an absolute requirement for a divalent metal ion, usually zinc, and in addition the enzymes are activated by monovalent cations such as Na+. The type A and type B Class II FBPA's differ in the presence and absence of distinct indels in the sequence that result in differing loop lengths in the structures
TKELLKKAREGGYAVGAFNINNLETLKAILEAAEETRSPVILQISEGAIKYAGLELLVAMVKAAAERASV
PVALHLDHGSSFELIKRAIRAGFSSVMIDGSHLPFEENVAKTKEVVELAHAYGVSVEAELGRIGGEEDGV
VGDEGLLTDPEEAEEFVEETGVDALAVAIGTSHGAYKGGEPKLDFDRLKEIAERVNVPLVLHGGSGIPDE
QIRKAIKLGVCKININTDLRLAFTAALREYLAENPKEFDPRKYLAPAIEAVKEVVKHKMELFGSAG
>gnl|CDD|188635 cd00948, FBP_aldolase_I_a, Fructose-1,6-bisphosphate aldolase. Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes the cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP). This family includes proteins found in vertebrates, plants, and bacterial plant pathogens. Mutations in the aldolase genes in humans cause hemolytic anemia and hereditary fructose intolerance. The enzyme is a member of the class I aldolase family, which utilizes covalent catalysis through a Schiff base formed between a lysine residue of the enzyme and ketose substrates
KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPGLGQYISGVILFEET
LYQKTDDGKPFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLK
IGNGTPSELAIKENAHGLARYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVL
LEGTLLKPNMVTPGADCKKKASPEEVAEYTVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLP
KPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRAKANSLAALGKY
>gnl|CDD|188636 cd00949, FBP_aldolase_I_bact, Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria. Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria. The enzyme catalyzes the cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP). The enzyme is member of the class I aldolase family, which utilizes covalent catalysis through a Schiff base formed between a lysine residue of the enzyme and ketose substrates
QEQLERMKSGKGFIAALDQSGGSTPKALAAYGIEEDAYSNEEEMFDLVHEMRTRIITSPAFDGDKILGAI
LFEQTMDREIEGKPTADYLWEKKQIVPFLKVDKGLAEEKNGVQLMKPIPNLDELLMRAKEKGVFGTKMRS
VIKEANPKGIAAVVDQQFELAKQILSHGLVPIIEPEVDIHSADKAKCEAILKAEILKHLDKLPEGQQVML
KLTLPTEANFYSELIEHPKVLRVVALSGGYSREEANELLAKNNGVIASFSRALTEGLSADQSDAEFNATL
EKSIDEIYQASI
>gnl|CDD|188637 cd00950, DHDPS, Dihydrodipicolinate synthase (DHDPS). Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue. The functional enzyme is a homotetramer consisting of a dimer of dimers. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways
FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRV
PVIAGTGSNNTAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGV
NIEPETVLRLAEHPNIVGIKEATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAP
KLMAEMVRAALAGDLEKARELHRKLLPLIKALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKL
RAAL
>gnl|CDD|188638 cd00951, KDGDH, 5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH). 5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH), which is member of dihydrodipicolinate synthase (DHDPS) family that comprises several pyruvate-dependent class I aldolases. The enzyme is involved in glucarate metabolism, and its mechanism presumbly involves a Schiff-base intermediate similar to members of DHDPS family. While in the case of Pseudomonas sp. 5-dehydro-4-deoxy-D-glucarate is degraded by KDGDH to 2,5-dioxopentanoate, in certain species of Enterobacteriaceae it is degraded instead to pyruvate and glycerate
GSGLLSFPVTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRV
PVLAGAGYGTATAIAYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYNRANAVLTA
DSLARLAERCPNLVGFKDGVGDIELMRRIVAKLGDRLLYLGGLPTAEVFALAYLAMGVPTYSSAVFNFVP
EIALAFYAAVRAGDHATVKRLLRDFFLPYVDIRNRRKGYAVSIVKAGARLVGRDAGPVRPPLTDLTEEEL
AQLTALIKT
>gnl|CDD|188639 cd00952, CHBPH_aldolase, Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA). Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA). HBPHA catalyzes HBP to salicyaldehyde and pyruvate. This reaction is part of the degradative pathways for naphthalene and naphthalenesulfonates by bacteria. CBPHA is homologous to HBPHA and catalyzes the cleavage of CBP to 2-carboxylbenzaldehyde and pyruvate during the degradation of phenanthrene. They are member of the DHDPS family of Schiff-base-dependent class I aldolases
DIKGVWAIVPTPSKPDASDWRATDTVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATV
VETVAGRVPVFVGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEAVPEMAIAI
YANPEAFKFDFPRAAWAELAQIPQVVAAKYLGDIGALLSDLAAVKGRMRLLPLEDDYYAAARLFPEEVTA
FWSSGAACGPAPVTALRDAVATGDWTDARALTDRMRWAAEPLFPRGDFSEFSKYNIALEKARFDAAGYMR
AGPARPPYNTAPEAYLEGARESGRRWAEL
>gnl|CDD|188640 cd00953, KDG_aldolase, KDG (2-keto-3-deoxygluconate) aldolases found in archaea. KDG (2-keto-3-deoxygluconate) aldolases found in archaea. This subfamily of enzymes is adapted for high thermostability and shows specificity for non-phosphorylated substrates. The enzyme catalyses the reversible aldol cleavage of 2-keto-3-dexoygluconate to pyruvate and glyceraldehyde, the third step of a modified non-phosphorylated Entner-Doudoroff pathway of glucose oxidation. KDG aldolase shows no significant sequence similarity to microbial 2-keto-3-deoxyphosphogluconate (KDPG) aldolases, and the enzyme shows no activity with glyceraldehyde 3-phosphate as substrate. The enzyme is a tetramer and a member of the DHDPS family of Schiff-base-dependent class I aldolases
MPDKITPVITPFTGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITDKVIF
QVGSLNLEESIELARAAKSFGIYAIASLPPYYFPGIPEEWLIKYFTDISSPYPTFIYNYPKATGYDINAR
MAKEIKKAGGDIIGVKDTNEDISHMLEYKRLVPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVK
IKDHVAIEDAFKLQFLINEVLDASRKYGSWSANYSLVKIFQGYDAGEPRPPFYPLDEEEEEKLRKEVNE
>gnl|CDD|188641 cd00954, NAL, N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL). N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL), which catalyses the reversible aldol reaction of N-acetyl-D-mannosamine and pyruvate to give N-acetyl-D-neuraminic acid (D-sialic acid). It has a widespread application as biocatalyst for the synthesis of sialic acid and its derivatives. This enzyme has been shown to be quite specific for pyruvate as the donor, but flexible to a variety of D- and, to some extent, L-hexoses and pentoses as acceptor substrates. NAL is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases
LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGK
VTLIAHVGSLNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAASLPMIIYHIPALT
GVNLTLEQFLELFEIPNVIGVKFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNV
NGKRYRKIFEAFNAGDIDTARELQHVINDVITVLIKNGLYPTLKAILRLMGLDAGPCRLPLRKVTEKALA
KAKELAAK
>gnl|CDD|188642 cd00955, Transaldolase_like, Transaldolase-like proteins from plants and bacteria. Transaldolase-like proteins from plants and bacteria. Transaldolase is found in the non-oxidative branch of the pentose phosphate pathway, that catalyze the reversible transfer of a dihydroxyacetone group from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. They are members of the class I aldolases, who are characterized by using a Schiff-base mechanism for stabilization of the reaction intermediates
SLWLDNLSRSFIDNGFLKRLIEEQGVVGVTSNPAIFEKAIAGSAAYDDQIRALKGQGLDAEAIYEALAIE
DIQDACDLLAPVYEQTGGNDGYVSLEVSPRLADDTQGTIAEAKRLWKAVGRPNLMIKIPATEAGLPAIEE
LIAAGISVNVTLIFSLEQYEAVAEAYLRGLERRVEGGGDLSQVASVASFFVSRVDTLIDKKLDAPEAKAL
QGKVAIANAKLAYQEYQEKFSGPRWAALAAAGAKPQRLLWASTGVKNPAYPDVLYVEELIGPDTVNTMPD
ATLKAFADHGEVRPTLEEGLEEAERVLAELERLGIDLDAVTEKLLKEGVKKFKDSFEK
>gnl|CDD|188643 cd00956, Transaldolase_FSA, Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea. Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea, which are member of the MipB/TalC subfamily of class I aldolases. FSA catalyze an aldol cleavage of fructose 6-phosphate and do not utilize fructose, fructose 1-phosphate, fructose 1,6-phosphate, or dihydroxyacetone phosphate. The enzymes belong to the transaldolase family that serves in transfer reactions in the pentose phosphate cycle, and are more distantly related to fructose 1,6-bisphosphate aldolase
KIFLDTADLEEIKKASETGLLDGVTTNPSLIAKSGRIDFEAVLKEICEIIDGPVSAQVVSTDAEGMVAEA
RKLASLGGNVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDG
MELIREIRTIFDNYGFDTKILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDWQ
S
>gnl|CDD|188644 cd00957, Transaldolase_TalAB, Transaldolases including both TalA and TalB. Transaldolases including both TalA and TalB. The enzyme catalyses the reversible transfer of a dyhydroxyacetone moiety, derived from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. The catalytic mechanism is similar to other class I aldolases. The enzyme is found in the non-oxidative branch of the pentose phosphate pathway and forms a dimer in solution
NQLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISN
ALDKLLVNFGTEILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQA
AKQLEKEGIHCNLTLLFSFAQAVACAEAGVTLISPFVGRILDWYKKHSGDKAYTAEEDPGVASVKKIYNY
YKKFGYKTKVMGASFRNIGQILALAGCDYLTISPALLEELKNSTAKVERKLDPAASKALDIHPNFLDESA
FRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI
>gnl|CDD|188645 cd00958, DhnA, Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs). Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs) found in bacteria and archaea. Catalysis of the enzymes proceeds via a Schiff-base mechanism like other class I aldolases, although this subfamily is clearly divergent based on sequence similarity to other class I and class II (metal dependent) aldolase subfamilies
LVILAVDHGIEHGFGPNPGLEDPEETVKLAAEGGADAVALTKGIARAYGREYAGDIPLIVKLNGSTSLSP
KDDNDKVLVASVEDAVRLGADAVGVTVYVGSEEEREMLEELARVAAEAHKYGLPLIAWMYPRGPAVKNEK
DPDLIAYAARIGAELGADIVKTKYTGDAESFKEVVEGCPVPVVIAGGPKKDSEEEFLKMVYDAMEAGAAG
VAVGRNIFQRPDPVAMLRAISAVVH
>gnl|CDD|188646 cd00959, DeoC, 2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family. 2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family. DERA belongs to the class I aldolases and catalyzes a reversible aldol reaction between acetaldehyde and glyceraldehyde 3-phosphate to generate 2-deoxyribose 5-phosphate. DERA is unique in catalyzing the aldol reaction between two aldehydes, and its broad substrate specificity confers considerable utility as a biocatalyst, offering an environmentally benign alternative to chiral transition metal catalysis of the asymmetric aldol reaction
LASLIDHTLLKPDATEEDIRKLCDEAKEYGFAAVCVNPCFVPLAREALKGSGVKVCTVIGFPLGATTTEV
KVAEAREAIADGADEIDMVINIGALKSGDYEAVYEEIAAVVEACGGAPLKVILETGLLTDEEIIKACEIA
IEAGADFIKTSTGFGPGGATVEDVKLMKEAVGGRVGVKAAGGIRTLEDALAMIEAGATRIGTS
>gnl|CDD|238478 cd00974, DSRD, Desulforedoxin (DSRD) domain; a small non-heme iron domain present in the desulforedoxin (rubredoxin oxidoreductase) and desulfoferrodoxin proteins of some archeael and bacterial methanogens and sulfate/sulfur reducers. Desulforedoxin is a small, single-domain homodimeric protein; each subunit contains an iron atom bound to four cysteinyl sulfur atoms, Fe(S-Cys)4, in a distorted tetrahedral coordination. Its metal center is similar to that found in rubredoxin type proteins. Desulforedoxin is regarded as a potential redox partner for rubredoxin. Desulfoferrodoxin forms a homodimeric protein, with each protomer comprised of two domains, the N-terminal DSRD domain and C-terminal superoxide reductase-like (SORL) domain. Each domain has a distinct iron center: the DSRD iron center I, Fe(S-Cys)4; and the SORL iron center II, Fe[His4Cys(Glu)]
MLEVYKCEICGNIVEVLNVGGGTLVCCGQPMKLI
>gnl|CDD|381600 cd00978, chitosanase_GH46, chitosanase belonging to the glycosyl hydrolase 46 family. This family is composed of the chitosanase enzymes which hydrolyzes chitosan, a biopolymer of beta (1,4)-linked-D-glucosamine (GlcN) residues produced by partial or full deacetylation of chitin. Chitosanases play a role in defense against pathogens such as fungi and are found in microorganisms, fungi, viruses, and plants. Microbial chitosanases can be divided into 3 subclasses based on the specificity of the cleavage positions for partial acetylated chitosan. Subclass I chitosanases such as N174 can split GlcN-GlcN and GlcNAc-GlcN linkages, whereas subclass II chitosanases such as Bacillus sp. no. 7-M can cleave only GlcN-GlcN linkages. Subclass III chitosanases such as MH-K1 chitosanase are the most versatile and can split both GlcN-GlcN and GlcN-GlcNAc linkages
PAQKRRAMQLTSVFENSTTDWAKQYGYIEDIGDGRGYTAGIIGFTTGTGDMLEVVKRYTKLNPANNLAKY
LPALRLKAVGGSDSHVGLLKGFVKAWKAAANDPAFRKAQDDVADELYFTPAVKLAKQDGGLSALGQAIYY
DAAVQHGPGSDKDSFGGIRKRALKLGGTPASGGDEKKYLAAFLDVRRQVLRNEPAHGSQSVDRVDAQRQL
LDDGNWDLKLPL
>gnl|CDD|238480 cd00980, FwdC/FmdC, FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran dehydrogenase, an enzyme that catalyzes the first step in methane formation from CO2 in methanogenic archaea, hyperthermophiles and bacteria. There are two isoenzymes, a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The subunits C of both isoenzymes (FwdC/FmdC) are characterized by a repeated GXXGXXXG motif
RVPLGDFFEVSGDGADADTKLVIEGDVPRLKRIGARMTAGEIVVEGDVGMYVGAGMKGGKLVVEGNAGSW
AGCEMKGGEITIKGNAGDYVGSAYRGDWRGMSGGTITIEGNAGDRLGERMRRGEILIKGDAGIFAGIRMN
GGTIIVRGDAGAHPGYEMKRGTIVIGGEIEELLPTFKEEGTEEDVFVSGEELSGTFYKFTGDL
>gnl|CDD|238481 cd00981, arch_gltB, Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown function found in the large subunit of glutamate synthase, which is encoded by gltB and found in most bacteria and eukaryotes. It is predicted to be homologous to the C-terminal domain of glutamate synthase based upon sequence similarity coupled with genome organization data, showing that this domain is found in a gene cluster with other domains of Glts, which are annotated. This domain is found primarily in archaea, but is also present in a few bacteria, likely as a result of lateral gene transfer
VVIDAKGLHYKELNQKIREAVEKGADEIVLDNVLGQRYIGDGLPGNVRINIYGVPGNDLGAFMSGPTIIV
YGNAQDDVGNTMNDGKIVIHGSAGDVLGYAMRGGKIFIRGNAGYRVGIHMKEYKDKVPVLVIGGTAGDFL
GEYMAGGVIIVLGLGTDEEPVGRYIGTGMHGGVIYIRGKVERSKLGKEVPKFELTEEDLEFIEKYIEEFC
KEFGYDKAEILDEEFTKLKPKS
>gnl|CDD|238482 cd00982, gltB_C, gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate synthase (GltS). GltS encodes a complex iron-sulfur flavoprotein that catalyzes the synthesis of L-glutamate from L-glutamine and 2-oxoglutarate. It requires the transfer of ammonia and electrons among three distinct active centers that carry out L-Gln hydrolysis, conversion of 2-oxoglutarate into L-Glu, and electron uptake from a donor. These catalytic sites appear to occur in other domains within the protein, and not the domain in this CD. This particular domain has no known function, but it likely has a structural role as it interacts with the amidotransferase and FMN-binding domains of gltS
LDDKLIADAEPALIENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPEDTIKIKFEGSAGQSFGAF
LAKGVTLELEGDANDYVGKGLSGGRIVVRPPKDATFKPEENIIIGNVCLYGATSGEAFIRGRAGERFAVR
NSGATAVVEGVGDHGCEYMTGGTVVVLGKTGRNFAAGMSGGVAYVLDEDGDFEKKVNHEMVDLERLEDAE
DEEQLKELIEEHVEYTGSEKAKEILANWEAYLKKFVKVIPR
>gnl|CDD|410863 cd00983, RecA, recombinase A. RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange
DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAK
KLGVDIDNLLVSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQAL
RKLTGSLSKSKTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVK
VVKNKVAPPFKQAEFDILYGEGISR
>gnl|CDD|410864 cd00984, DnaB_C, C-terminal domain of DnaB helicase. DnaB helicase C-terminal domain. The hexameric helicase DnaB unwinds the DNA duplex at the chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis
GLPTGFTDLDKLTGGLQPGDLIIIAARPSMGKTAFALNIAENIALDEGLPVLFFSLEMSAEQLAERLLSS
ESGVSLSKLRTGRLDDEDWERLTAAMGELSELPLYIDDTPGLTVDEIRAKARRLKREHGGLGLIVIDYLQ
LIRGSKRAENRQQEVAEISRSLKALAKELNVPVIALSQLNRGVESRTDKRPMLSDLRESGSIEQDADVVI
FLYRDEYYDKDSEDKGIAEIIIAKNRNGPTGTVYLAFNPEYTRFTD
>gnl|CDD|238485 cd00985, Maf_Ham1, Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum formation in eukaryotes, bacteria and archaea. A Ham1-related protein from Methanococcus jannaschii is a novel NTPase that has been shown to hydrolyze nonstandard nucleotides, such as hypoxanthine/xanthine NTP, but not standard nucleotides
LILASGSPRRLEELKQIGGIEFEVLPSDIDETGLKGEPEDTVEELALLKARAVAERLPDAPVIADDTGLV
VDGRPGGKPARFAEALEMLRGLSGRTAEFVTAVALVDPDGKIITFEGETEGKIALRKLLEL
>gnl|CDD|467618 cd00990, cpPDZ_AtDEGP1-like, circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Arabidopsis thaliana DEGP1 (also known as protease Do-like 1, chloroplastic, protein DEGRADATION OF PERIPLASMIC PROTEINS 1, DEGP PROTEASE 1 and DEG1), and related domains. DEGP1 is a serine protease that is required at high temperature and may be involved in the degradation of damaged proteins. This family also includes Arabidopsis protease DEGP8/Do-like 8 (chloroplastic), a probable serine protease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This AtDEGP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus
VVRPGLGISFAPDQVARQLGVRSGVLVLDVPPGGPAAKAGLRGTKRDEFGRIVLGDVIVAVDGKPVKNES
DLYRALDEYKVGDVVTLKVLRGGTKVDLKVTL
>gnl|CDD|270215 cd00993, PBP2_ModA_like, Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein fold. Molybdate binding domain ModA. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arranged around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has revealed a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. This octahedral geometry was rather unexpected. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
ELTVFAAASLKDALQELAKQFKKATGVTVVLNFGSSGALAKQIEQGAPADVFISADQKWMDYLVAAGLIL
PASVRPFAGNRLVLVVPKASPVSGTPLLELALDEGGRIAVGDPQSVPAGRYAKQVLEKLGLWDKLPPKLV
EAPDVRQVLGLVESGEADAGFVYASDALAAKKVKVVATLPEDLHEPIVYPVAVLKGSKNKAEAKAFLDFL
LSPEGQRIFERYGFL
>gnl|CDD|270216 cd00994, PBP2_GlnH, Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold. This periplasmic substrate-binding component serves as an initial receptor in the ABC transport of glutamine in bacteria and eukaryota. GlnH belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLTVATDTTFVPFEFKQDGKYVGFDIDLWEAIAKEAGFKYELQPMDFKGIIPALQTGRIDIAIAGITITE
ERKKVVDFSDPYYDSGLAVMVKADNNSIKSIDDLAGKTVAVKTGTTSVDYLKENFPDAQLVEFPNIDNAY
MELETGRADAVVHDTPNVLYYAKTAGKGKVKVVGEPLTGEQYGIAFPKGSELREKVNAALKTLKADGTYD
EIYKKWFG
>gnl|CDD|173853 cd00995, PBP2_NikA_DppA_OppA_like, The substrate-binding domain of an ABC-type nickel/oligopeptide-like import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding domain of nickel/dipeptide/oligopeptide transport systems, which function in the import of nickel and peptides, and other closely related proteins. The oligopeptide-binding protein OppA is a periplasmic component of an ATP-binding cassette (ABC) transport system OppABCDEF consisting of five subunits: two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Similar to the ABC-type dipeptide and oligopeptide import systems, nickel transporter is comprised of five subunits NikABCDE: the two pore-forming integral inner membrane proteins NikB and NikC; the two inner membrane-associated proteins with ATPase activity NikD and NikE; and the periplasmic nickel binding NikA, which is the initial nickel receptor that controls the chemotactic response away from nickel. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand binding domains of ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLTVALGSDPTSLDPAFATDASSGRVLRLIYDGLVRYDPDGELVPDLAESWEVSDDGKTYTFKLRDGVKF
HDGTPLTAEDVVFSFERLADPKNASPSAGKADEIEGVEVVDDYTVTITLKEPDAPFLALLAYPAASPVPK
AAAEKDGKAFGTKPVGTGPYKLVEWKPGESIVLERNDDYWGPGKPKIDKITFKVIPDASTRVAALQSGEI
DIADDVPPSALETLKKNPGIRLVTVPSLGTGYLGFNTNKPPFDDKRVRQAISYAIDREEIIDAVLGGYGT
PATSPLPPGSWGYYDKDLEPYEYDPEKAKELLAEAGYKDGKGLELTLLYNSDGPTRKEIAEAIQAQLKEI
GIKVEIEPLDFATLLDALDAGDDFDLFLLGWGADYPDPDNFLSPLFSSGASGAGNYSGYSNPEFDALLDE
ARAETDPEERKALYQEAQEILAEDAPVIPLYYPNNVYAYSKRVKGF
>gnl|CDD|270217 cd00996, PBP2_AatB_like, Polar amino acids-binding domain of ATP-binding cassette transporter-like systems that belong to the type 2 periplasmic binding fold protein superfamily. This subfamily includes periplasmic binding domain of ATP-binding cassette transporter-like systems that serve as initial receptors in the ABC transport of amino acids and their derivatives in eubacteria. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The Abp proteins belong to the PBPI superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
KEKGKIVIGLDDTFAPMGFRDENGEIVGFDIDLAKEVAKRLGVEVEFQPIDWDMKETELNSGNIDLIWNG
LTITDERKKKVAFSKPYLENRQIIVVKKDSPINSKADLKGKTVGVQSGSSGEDALNADPNLLKKNKEVKL
YDDNNDAFMDLEAGRIDAVVVDEVYARYYIKKKPLDDYKILDESFGSEEYGVGFRKEDTELKEKINKALD
EMKADGTAAKISQKWFG
>gnl|CDD|270218 cd00997, PBP2_GluR0, Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold. Glutamate receptor domain GluR0. These domains are found in the GluR0 proteins that have been shown to function as prokaryotic L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. The GluR0 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
SAQTLTVATVPRPPFVFYNDGELTGFSIDLWRAIAERLGWETEYVRVDSVSALLAAVAEGEADIAIAAIS
ITAEREAEFDFSQPIFESGLQILVPNTPLINSVNDLYGKRVATVAGSTAADYLRRHDIDVVEVPNLEAAY
TALQDKDADAVVFDAPVLRYYAAHDGNGKAEVTGSVFLEENYGIVFPTGSPLRKPINQALLNLREDGTYD
ELYEKWFG
>gnl|CDD|270219 cd00998, PBP2_iGluR_ligand_binding, The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic binding protein type II superfamily. This subfamily represents the ligand binding of ionotropic glutamate receptors. iGluRs are heterotetrameric ion channels that comprises of three functionally distinct subtypes based on their pharmacology and structural similarities: AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid), NMDA (N-methyl-D-aspartate), and kainate receptors. All three types of channels are also activated by the physiological neurotransmitter, glutamate. iGluRs are concentrated at postsynaptic sites, where they exert a variety of different functions. While this ligand-binding domain of iGluRs is structurally homologous to the periplasmic binding fold type II superfamily, the N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain belongs to the periplasmic-binding fold type I
KTLKVVVPLEPPFVMFVTGSNAVTGNGRFEGYCIDLLKELSQSLGFTYEYYLVPDGKFGAPVNGSWNGMV
GEVVRGEADLAVGPITITSERSVVIDFTQPFMTSGIGIMIPIRSIDDLKRQTDIEFGTVENSFTETFLRS
SGIYPFYKTWMYSEARVVFVNNIAEGIERVRKGKVYAFIWDRPYLEYYARQDPCKLIKTGGGFGSIGYGF
ALPKNSPLTNDLSTAILKLVESGVLQKLKNKWL
>gnl|CDD|270220 cd00999, PBP2_ArtJ, The solute binding domain of ArtJ protein, a member of the type 2 periplasmic binding fold protein superfamily. An arginine-binding protein found in Chlamydiae trachomatis (CT-ArtJ) and pneumoniae (CPn-ArtJ) and its closely related proteins. CT- and CPn-ArtJ are shown to have different immunogenic properties despite a high sequence similarity. The ArtJ proteins display the type 2 periplasmic binding fold organized in two alpha-beta domains with arginine-binding region at their interface
MDKDVIIVGTESTYPPFEFRDEKGELVGFDIDLAEAISEKLGKKLEWRDMAFDALIPNLLTGKIDAIAAG
MSATPERAKRVAFSPPYGESVSAFVTVSDNPIKPSLEDLKGKSVAVQTGTIQEVFLRSLPGVEVKSFQKT
DDCLREVVLGRSDAAVMDPTVAKVYLKSKDFPGKLATAFTLPEWGLGKALAVAKDDPALKEAVNKALDEL
KKEGELAALRKKW
>gnl|CDD|270221 cd01000, PBP2_Cys_DEBP_like, Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 periplasmic-binding protein fold. This family comprises of the periplasmic-binding protein component of ABC transporters specific for cysteine and carboxylic amino acids, as well as their closely related proteins. The cysteine and aspartate-glutamate binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
LDDIKSRGVLIVGVKPDLPPFGARDANGKIQGFDVDVAKALAKDLLGDPVKVKFVPVTSANRIPALQSGK
VDLIIATMTITPERAKEVDFSVPYYADGQGLLVRKDSKIKSLEDLKGKTILVLQGSTAEAALRKAAPEAQ
LLEFDDYAEAFQALESGRVDAMATDNSLLAGWAAENPDDYVILPKPFSQEPYGIAVRKGDTELLKAVNAT
IAKLKADGELAEIYKKWL
>gnl|CDD|270222 cd01001, PBP2_HisJ_LAO_like, Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and related proteins; the type 2 periplasmic-binding protein fold. This family comprises the periplasmic substrate-binding proteins, including the lysine-, arginine-, ornithine-binding protein (LAO) and the histidine-binding protein (HisJ), which serve as initial receptors for active transport. HisJ and LAO proteins belong to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
ADTLRIGTEGDYPPFNFLDADGKLVGFDIDLANALCKRMKVKCEIVTQPWDGLIPALKAGKYDAIIASMS
ITDKRRQQIDFTDPYYRTPSRFVARKDSPITDTTPAKLKGKRVGVQAGTTHEAYLRDRFPEADLVEYDTP
EEAYKDLAAGRLDAVFGDKVALSEWLKKTKSGGCCKFVGPAVPDPKYFGDGVGIAVRKDDDALRAKLDKA
LAALKADGTYAEISKKYF
>gnl|CDD|270223 cd01002, PBP2_Ehub_like, Substrate binding domain of ectoine/hydroxyectoine specific ABC transport system; the type 2 periplasmic binding protein fold. This family represents the periplasmic substrate-binding component of ABC transport systems that involved in uptake of osmoprotectants (also termed compatible solutes) such as ectoine and hydroxyectoine. To counteract the efflux of water, bacteria and archaea accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
STLERLKEQGTIRIGYANEPPYAYIDADGEVTGESPEVARAVLKRLGVDDVEGVLTEFGSLIPGLQAGRF
DVIAAGMFITPERCEQVAFSEPTYQVGEAFLVPKGNPKGLHSYADVAKNPDARLAVMAGAVEVDYAKASG
VPAEQIVIVPDQQSGLAAVRAGRADAFALTALSLRDLAAKAGSPDVEVAEPFQPVIDGKPQIGYGAFAFR
KDDTDLRDAFNAELAKFKGSGEHLEILEPFGF
>gnl|CDD|270224 cd01003, PBP2_YckB, Substrate binding domain of an ABC cystine transporter; the type 2 periplasmic binding protein fold. Periplasmic cystine-binding domain (YckB) of an ATP-binding cassette (ABC) transporter from Bacillus subtilis and its related proteins. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GSIVVATSGTLYPTSYHDTDSDKLTGYEVEVVREAGKRLGLKIEFKEMGIDGMLTAVNSGQVDAAANDIE
VTKDREKKFAFSTPYKYSYGTAVVRKDDLSGISSLKDLKGKKAAGAATTVYMEIARKYGAEEVIYDNATN
EVYLKDVANGRTDVILNDYYLQTMAVAAFPDLNITIHPDIKYYPNKQALVMKKSNAALQEKVNKALKEMS
KDGTLTKISEQFFNGADVS
>gnl|CDD|270225 cd01004, PBP2_MidA_like, Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 periplasmic binding protein fold. This subgroup includes the periplasmic binding component of ABC transporter involved in uptake of mimosine MidA and its similar proteins. This periplasmic binding domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
AGTLTVGTNPTYPPYEFVDEDGKLIGFDVDLAKAIAKRLGLKVEIVNVSFDGLIPALQSGRYDIIMSGIT
DTPERAKQVDFVDYMKDGLGVLVAKGNPKKIKSPEDLCGKTVAVQTGTTQEQLLQAANKKCKAAGKPAIE
IQTFPDQADALQALRSGRADAYLSDSPTAAYAVKQSPGKLELVGEVFGSPAPIGIAVKKDDPALADAVQA
ALNALIADGTYKKILKKWGL
>gnl|CDD|270226 cd01005, PBP2_CysP, Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic binding fold superfamily. This family contains sulfate binding domain of CysP proteins that serve as initial receptors in the ABC transport of sulfate and thiosulfate in eubacteria. After binding the ligand, CysP interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The CysP proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
ADVTLLNVSYDVTRELYEEVNPAFAKYWKEKTGQTVTIKQSHGGSGKQARAVIDGLEADVVTLALEYDID
RIVKAGLIAPDWQQRLPNNSIPYTSTIVFLVRKGNPKGIRDWDDLVKPGVSVITPNPKTSGGARWNYLAA
WGYALKKGGSEAKAKEFVTSLYKNVPVLDSGAREATTTFVKRGIGDVLITWENEAILANKELGGDKFEIV
YPSVSILAEPPVAVVDKNVDKHGTREVAEAYLEFLYSPEAQEIAAKNGYRPRDPEVAAKYAKQFPAINLF
FIIDDFGGWAKAQKKHFGDGGIFDQIY
>gnl|CDD|270227 cd01006, PBP2_phosphate_binding, Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 periplasmic-binding fold superfamily. This phosphate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
ASELTISGSTSVAPIXDVWAEKYNQQHPETYVAVQGVGSTAGISQLKAGTVDIGASDAYLSESEAANKGL
HTFTLAIDGLAIVVNQPGPVTNLTLNGKQLYGIYKGQIKNWDDVGIAALNPGVNLPDQKIAVVTREDGSG
TRFSFTSYLGKTKTEKDGKGTTEVSDVAPTALGVNGNSGXKTLVNHNPGAVGYISIGSVDQSSLKAIQLY
PISRPFLILHYSDQKDAATDEQTKEFIAWAKSEGAAKLIVEYG
>gnl|CDD|270228 cd01007, PBP2_BvgS_HisK_like, The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine kinase receptors, and related proteins. This family comprises the periplasmic sensor domain of the two-component sensor-kinase systems, such as the sensor protein BvgS of Bordetella pertussis and histidine kinase receptors (HisK), and uncharacterized related proteins. Typically, the two-component system consists of a membrane spanning sensor-kinase and a cytoplasmic response regulator. It serves as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. The N-terminal sensing domain of the sensor kinase detects extracellular signals, such as small molecule ligands and ions, which then modulate the catalytic activity of the cytoplasmic kinase domain through a phosphorylation cascade. The periplasmic sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
HPVIRVGVDPDWPPFEFIDEGGEPQGIAADYLKLIAKKLGLKFEYVPGDSWSELLEALKAGEIDLLSSVS
KTPEREKYLLFTKPYLSSPLVIVTRKDAPFINSLSDLAGKRVAVVKGYALEELLRERYPNINLVEVDSTE
EALEAVASGEADAYIGNLAVASYLIQKYGLSNLKIAGLTDYPQDLSFAVRKDWPELLSILNKALASISPE
ERQAIRNKWL
>gnl|CDD|270229 cd01008, PBP2_NrtA_SsuA_CpmA_like, Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily. This family represents the periplasmic binding proteins involved in nitrate, alkanesulfonate, and bicarbonate transport. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. Other closest homologs involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB) are also included in this family. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TVRIGYQAGPLAGPLIVAKEKGLFEKEKEGIDVEWVEFTSGPPALEALAAGSLDFGTGGDTPALLAAAGG
VPVVLIAALSRSPNGNGIVVRKDSGITSLADLKGKKIAVTKGTTGHFLLLKALAKAGLSVDDVELVNLGP
ADAAAALASGDVDAWVTWEPFLSLAEKGGDARIIVDGGGLPYTDPSVLVARRDFVEENPEAVKALLKALV
EA
>gnl|CDD|270230 cd01009, PBP2_YfhD_N, The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold protein superfamily. This subfamily includes the solute binding domain YfhD_N. These domains are found in the YfhD proteins that are predicted to function as lytic transglycosylases that cleave the glycosidic bond between N-acetylmuramic acid and N-acetylglucosamin in peptidoglycan, while the YfhD_N domain might act as an auxiliary or regulatory subunit. In addition to periplasmic solute binding domain, they have an SLT domain, typically found in soluble lytic transglycosylases, and a C-terminal low complexity domain. The YfhD proteins might have been recruited to create localized cell wall openings required for transport of large substrates such as DNA. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
GELRVLTRNSPTTYYIDRGGPRGFEYELAKAFADYLGVELEIVPADNLEELLEALEEGKGDLAAAGLTIT
PERKKKVDFSFPYYYVVQVLVYRKGSPRPRSLEDLSGKTIAVRKGSSYAETLQKLNKGGPPLTWEEVDEA
LTEELLEMVAAGEIDYTVADSNIAALWRRYYPELRVAFDLSEPQPLAWAVRKNSPSLLAALNRFLAQIKK
DGTLARLYERYYG
>gnl|CDD|238493 cd01011, nicotinamidase, Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, converts nicotinamide to nicotinic acid (niacin) and ammonia, which in turn can be recycled to make nicotinamide adenine dinucleotide (NAD). The same enzyme is also called pyrazinamidase, because in converts the tuberculosis drug pyrazinamide (PZA) into its active form pyrazinoic acid (POA)
TDALLVVDVQNDFCPGGALAVPGGDAIVPLINALLSLFQYDLVVATQDWHPANHASFASNHPGQMPFITL
PPGPQVLWPDHCVQGTPGAELHPGLPVPDIDLIVRKGTNPDIDSYSAFFDNDRRSSTGLAEYLRERGIDR
VDVVGLATDYCVKATALDALKAGFEVRVLEDACRAVDPETIERAIEEMKEAGVVLV
>gnl|CDD|238494 cd01012, YcaC_related, YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown specificity. Despite its weak sequence similarity, it is structurally related to other amidohydrolases and shares conserved active site residues with them. Multimerisation interface seems not to be conserved in all members
ALLLVDVQEKLAPAIKSFDELINNTVKLAKAAKLLDVPVILTEQYPKGLGPTVPELREVFPDAPVIEKTS
FSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQ
AGAVLTTSESVLFELQR
>gnl|CDD|238495 cd01013, isochorismatase, Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the conversion of isochorismate, in the presence of water, to 2,3-dihydroxybenzoate and pyruvate, via the hydrolysis of a vinyl ether, an uncommon reaction in biological systems. Isochorismatase is part of the phenazine biosynthesis pathway. Phenazines are antimicrobial compounds that provide the competitive advantage for certain bacteria
AIPKIASYPLPTAESFPANKVDWQIDPKRAVLLVHDMQRYFLDFYDESAEPVPQLIANIARLRDWCRQAG
IPVVYTAQPGNQTPEQRALLNDFWGPGLTASPEETKIVTELAPQPDDTVLTKWRYSAFKRSPLLERLKES
GRDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVADAIADFSLEEHRMALKYAATRCAMVVSTD
>gnl|CDD|238496 cd01014, nicotinamidase_related, Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share the catalytic triad with other amidohydrolases, like nicotinamidase, which converts nicotinamide to nicotinic acid and ammonia
ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGSFAPGSEGWEIHPELAP
LEGETVIEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLP
DHGGVLSAEEIHAHY
>gnl|CDD|238497 cd01015, CSHase, N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, carbon dioxide and ammonia. CSHase is involved in one of the two alternative pathways for creatinine degradation to glycine in microorganisms.This CSHase-containing pathway degrades creatinine via N-methylhydantoin N-carbamoylsarcosine and sarcosine to glycine. Enzymes of this pathway are used in the diagnosis for renal disfunction, for determining creatinine levels in urine and serum
ALLVIDLVEGYTQPGSYLAPGIAAALENVQRLLAAARAAGVPVIHTTVVYDPDGADGGLWARKVPAMSDL
VEGSPLAAICDELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGF
RPIVVRECVGDRAPAPHEANLFDIDNKYGDVVSTDDALA
>gnl|CDD|238498 cd01016, TroA, Metal binding protein TroA. These proteins have been shown to function as initial receptors in ABC transport of Zn2+ and possibly Fe3+ in many eubacterial species. The TroA proteins belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence)
KPNVVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEGKMSDVLS
KLGSSKSVIALEDTLDRSQLILDEEEGTYDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYV
EELDSLDAYAKKKIAEIPEQQRVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERK
IKAIFVESSVNQKSIEALQDAVKARGHDVQIGGELYSDAMGEEGTSEGTYIGMFKHNVDTIVEALK
>gnl|CDD|238499 cd01017, AdcA, Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of Zn2+ and Mn2+ and in competence for genetic transformation and adhesion. The AdcA proteins belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a long alpha helix and they bind their ligand in the cleft between these domains. In addition, many of these proteins have a low complexity region containing metal binding histidine-rich motif (repetitive HDH sequence)
SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKV
LKSLQNKKLKVVEASKGIKLLKAGGAEHDHDHSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDN
KEYYEKNAAAYAKKLEALDQEYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLA
ELVEFVKKSDVKYIFFEENASSKIAETLAKETGAKLLVLNPLETLTKEEIDDGKDYFSLMKENLETLKRA
LK
>gnl|CDD|238500 cd01018, ZntC, Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a long alpha helix and bind their specific ligands in the cleft between these domains. In addition, many of these proteins possess a metal-binding histidine-rich motif (repetitive HDH sequence)
DKPTVAVSIEPQKYFVEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEEVWLERF
RSNNPKMQVVNMSKGITLIPMADHHHHHHGEHEHHHHGNYDPHIWLSPANAKIMAENIYEALAELDPQNA
TYYQANLDALLAELDALDSEIRTILSKLKQRAFMVYHPAWGYFARDYGLTQIPIEEEGKEPSPADLKRLI
DLAKEKGVRVVFVQPQFSTKSAEAIAREIGAKVVTIDPLAADWEENLLKVADAFAH
>gnl|CDD|238501 cd01019, ZnuA, Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in the ABC uptake of Zn2+. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a single helix and bind their specific ligands in the cleft between these domains. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence)
AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKV
LQGRKKGKVLTLAKLIDLKTLEDGASHGDHEHDHEHAHGEHDGHEEGGLDPHLWLSPENAAEVAQAVAEK
LSALDPDNAATYAANLEAFNARLAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEI
DPGAKRLAKIRKEIKEKGATCVFAEPQFHPKIAETLAEGTGAKVGELDPLGGLIELGKNSYVNFLRNLAD
SLASCL
>gnl|CDD|238502 cd01020, TroA_b, Metal binding protein TroA_b. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence)
GKINVVASTNFWGSVAEAVGGDHVEVTSIITNPDVDPHDFEPTPTDAAKVSTADIVVYNGGGYDPWMTKL
LADTKDVIVIAADLDGHDDKEGDNPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVASLKPL
AAKIAELSAKYKGAPVAATEPVFDYLLDALGMKERTPKGYTATTESETEPSPADIAAFQNAIKNRQIDAL
IVNPQQASSATTNITGLAKRSGVPVVEVTETMPNGTTYLTWMLKQVDQLEKALQ
>gnl|CDD|381601 cd01021, GEWL, Goose egg-white lysozyme. Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; GEWL) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). Mammals have two lysozymes. This family corresponds to human and mouse lysozyme G-like protein 2
ETTGASAATAKQDGLLYGGVAASEKMAETDLNRLNKYKDCIKQVGKKLCIDPALIAAIISRESRAGAALD
KNGWGDHGNGFGLMQVDKRYHPPKGAWDSEEHIEQATGILIDFIKTVQRKHPSWSPEQQLKGGIAAYNAG
VGNVQSYAGMDIGTTGNDYSNDVIARAQWYKNNG
>gnl|CDD|212096 cd01022, GH57N_like, N-terminal catalytic domain of heat stable retaining glycoside hydrolase family 57. Glycoside hydrolase family 57(GH57) is a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57s cleave alpha-glycosidic bonds by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation
YFILHNHQPYVRRAGDQPLGEEWLHEAIAGCYIPLLELLEDLVDEGPDPKVALTISGVLLEQLADPVVQK
GFTSRYNDNVLDALKELVDTGQVELLGCGYTHAYLPLLGPKEDVRAQIEAGLDTFERLFGRRPKGVWLPE
CAYRPGLEKVLREAGIEYFVVDPDHFSRAGDGETAPHRPYWLPLGGRGLIIFARDQGLSQKIWFRSLGYP
GDPAMEQAEEHAADFAGYLERVLRELFGRPAVVVIALDGENFGHRWFEGVGFLRELLELLTSSEKLKLVT
PSEYLEALEPRGGVVELADGSWGAGGDFSIWKN
>gnl|CDD|173775 cd01025, TOPRIM_recR, TOPRIM_recR: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in Escherichia coli RecR. RecR participates in the RecFOR pathway of homologous recombinational repair in prokaryotes. This pathway provides a single-stranded DNA molecule coated with RecA to allow invasion of a homologous molecule. The RecFOR system directs the loading of RecA onto gapped DNA coated with SSB protein. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). In RecR sequences this glutamate in the first turn of the TOPRIM domain is semiconserved, the DXD motif is not conserved
NKLCVVEEPRDVLAIEESGEYRGLYHVLGGLISPLDGIGPDDLNIDKLLERIAKGQVKEVILATNPTVEG
EATALYIAKLLKDFGVKVTRLAQGIPVGGELEYADEITLSRA
>gnl|CDD|173776 cd01026, TOPRIM_OLD, TOPRIM_OLD: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in bacterial and archaeal nucleases of the OLD (overcome lysogenization defect) family. The bacteriophage P2 OLD protein, which has DNase as well as RNase activity, consists of an N-terminal ABC-type ATPase domain and a C-terminal Toprim domain; the nuclease activity of OLD is stimulated by ATP, though the ATPase activity is not DNA-dependent. Functional details on OLD are scant and further experimentation is required to define the relationship between the ATPase and Toprim nuclease domains. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general acid in strand cleavage by nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function
FFADKVILVEGDSEEILLPALAKKLGLDLDEAGISIIPVGGKNFKPFIKLLNALGIPVAVLTDLDAKRNE
KKDDAGKGRNKKLDSKDDVSKNLATLE
>gnl|CDD|173777 cd01027, TOPRIM_RNase_M5_like, TOPRIM_ RNase M5_like: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in Ribonuclease M5: (RNase M5) and other small primase-like proteins from bacteria and archaea. RNase M5 catalyzes the maturation of 5S rRNA in low G+C Gram-positive bacteria. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general base in nucleotide polymerization by primases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function
IGEVIIVEGKNDTESLKKLGIEAEIIETNGSIINKETIELIKKAYRGVIILTDPDRKGEKIRKKLSEYLS
GPVPEIKRAFL
>gnl|CDD|173778 cd01028, TOPRIM_TopoIA, TOPRIM_TopoIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in the type IA family of DNA topoisomerases (TopoIA). This subgroup contains proteins similar to the Type I DNA topoisomerases: E. coli topisomerases I and III, eukaryotic topoisomerase III and, ATP-dependent reverse gyrase found in archaea and thermophilic bacteria. Type IA DNA topoisomerases remove (relax) negative supercoils in the DNA. These enzymes cleave one strand of the DNA duplex, covalently link to the 5' phosphoryl end of the DNA break and allow the other strand of the duplex to pass through the gap. Reverse gyrase is also able to insert positive supercoils in the presence of ATP and negative supercoils in the presence of AMPPNP. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). For topoisomerases the conserved glutamate is believed to act as a general base in strand joining and, as a general acid in strand cleavage. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function
KVLIIAEKPSKAKTIAKILGKGSKKKGFYGEGGGYVVTASVGHLLELPFPEEYVDWDKDWPLELFPFEPK
YVVIPDKKKQLKALKKLAKKADEIVLATDPDREGELIAWEILEVLKCDNKPVKRAWFSEITPKAIREAFK
NL
>gnl|CDD|173779 cd01029, TOPRIM_primases, TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in the active site regions of bacterial DnaG-type primases and their homologs. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. The prototypical bacterial primase. Escherichia coli DnaG is a single subunit enzyme
DEVIIVEGYMDVLALHQAGIKNVVAALGTANTEEQLRLLKRFARTVILAFDNDEAGKKAAARALELLLAL
GGRVRVPPL
>gnl|CDD|173780 cd01030, TOPRIM_TopoIIA_like, TOPRIM_TopoIIA_like: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in proteins of the type IIA family of DNA topoisomerases similar to Saccharomyces cerevisiae Topoisomerase II. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. These proteins also catenate/ decatenate duplex rings. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general base in strand joining and as a general acid in strand cleavage by topisomerases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function
CELILVEGDSAGGSAKQGRDRVFQAVFPLRGKILNVEKASLKKILKNEEIQNIIKALGLGIGKDDFDLDK
LRYGKIIIMTDADVDGSHIRTLLLTFFYRFWPSLLENGFLYIAQT
>gnl|CDD|238504 cd01031, EriC, ClC chloride channel EriC. This domain is found in the EriC chloride transporters that mediate the extreme acid resistance response in eubacteria and archaea. This response allows bacteria to survive in the acidic environments by decarboxylation-linked proton utilization. As shown for Escherichia coli EriC, these channels can counterbalance the electric current produced by the outwardly directed virtual proton pump linked to amino acid decarboxylation. The EriC proteins belong to the ClC superfamily of chloride ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge. In Escherichia coli EriC, a glutamate residue that protrudes into the pore is thought to participate in gating by binding to a Cl- ion site within the selectivity filter
IGLLAGLVAVLFRLGIDKLGNLRLSLYDFAANNPPLLLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQV
EGVLAGLLPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGAAIGQGVSKWFKTSPEERRQLIAAGAA
AGLAAAFNAPLAGVLFVLEELRHSFSPLALLTALVASIAADFVSRLFFGLGPVLSIPPLPALPLKSYWLL
LLLGIIAGLLGYLFNRSLLKSQDLYRKLKKLPRELRVLLPGLLIGPLGLLLPEALGGGHGLILSLAGGNF
SISLLLLIFVLRFIFTMLSYGSGAPGGIFAPMLALGALLGLLFGTILVQLGPIPISAPATFAIAGMAAFF
AAVVRAPITAIILVTEMTGNFNLLLPLMVVCLVAYLVADLLGGKPIYEALLE
>gnl|CDD|238505 cd01033, ClC_like, Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) transporters found in eubacteria. They belong to the ClC superfamily of halogen ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. This superfamily lacks any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge
GVGAGLGGGLLTLLLHGVQHLAFGYSEGSFLTGVAAVSPIRRALSLTVGGLIAGLGWYLLRRKGKKLVSI
KQAVRGKKRMPFWETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRFSDWLGLTVADRRLLVACAAGA
GLAAVYNVPLAGALFALEILLRTISLRSVVAALATSAIAAAVASLLKGDHPIYDIPPMQLSTPLLIWALL
AGPVLGVVAAGFRRLSQAARAKRPKGKRILWQMPLAFLVIGLLSIFFPQILGNGRALAQLAFSTTLTLSL
LLILLVLKIVATLLALRAGAYGGLLTPSLALGALLGALLGIVWNALLPPLSIAAFALIGAAAFLAATQKA
PLTALILVLEFTRQNPLFLIPLMLAVAGAVAVSRFILQ
>gnl|CDD|238506 cd01034, EriC_like, ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, are putative halogen ion (Cl-, Br- and I-) transport proteins found in eubacteria. They belong to the ClC superfamily of chloride ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. This superfamily lacks any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge
GLVALLFAKLADLALALFQRLTATHPWLPLLLTPAGFALIAWLTRRFFPGAAGSGIPQVIAALELPSAAA
RRRLLSLRTAVGKILLTLLGLLGGASVGREGPSVQIGAAVMLAIGRRLPKWGGLSERGLILAGGAAGLAA
AFNTPLAGIVFAIEELSRDFELRFSGLVLLAVIAAGLVSLAVLGNYPYFGVAAVALPLGEAWLLVLVCGV
VGGLAGGLFARLLVALSSGLPGWVRRFRRRRPVLFAALCGLALALIGLVSGGLTFGTGYLQARAALEGGG
GLPLWFGLLKFLATLLSYWSGIPGGLFAPSLAVGAGLGSLLAALLGSVSQGALVLLGMAAFLAGVTQAPL
TAFVIVMEMTGDQQMLLPLLAAALLASGVSRLVCPEPLYH
>gnl|CDD|238507 cd01036, ClC_euk, Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) channel proteins that perform a variety of functions including cell volume regulation, membrane potential stabilization, charge compensation necessary for the acidification of intracellular organelles, signal transduction and transepithelial transport. They are also involved in many pathophysiological processes and are responsible for a number of human diseases. These proteins belong to the ClC superfamily of chloride ion channels, which share the unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge. Some proteins possess long C-terminal cytoplasmic regions containing two CBS (cystathionine beta synthase) domains of putative regulatory function
GLLMGLVAVVLDYAVESSLDAGQWLLRRIPGSYLLGYLMWVLWSVVLVLISSGICLYFAPQAAGSGIPEV
MAYLNGVHLPMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAGLLQGRSRTLGCHVHLFQLF
RNPRDRRDFLVAGAAAGVASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQIYNSFNSGFE
LLDRSSAMFLSLTVFELHVPLNLYEFIPTVVIGVICGLLAALFVRLSIIFLRWRRRLLFRKTARYRVLEP
VLFTLIYSTIHYAPTLLLFLLIYFWMSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIGAES
ATLWADPGVYALIGAAAFLGGTTRLTFSICVIMMELTGDLHHLLPLMVAILIAKAVADAFCESLYH
>gnl|CDD|411707 cd01037, PDDEXK_nuclease-like, PDDEXK family nucleases. Superfamily of PDDEXK nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI
LLEDLLLKLLNLLGIERELNIVKQGESGGGGPDFLIVRDGRGLVIEVKSTKLKRSSIDLLKAKVLKLLEY
LKLGGKLALLIVP
>gnl|CDD|411708 cd01038, Endonuclease_DUF559, Putative endonuclease. Domain of unknown function 559 (DUF559) is a putative endonuclease of unknown function, belongs to a superfamily of nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI
QTEAERKLWQHLRNRQFLGLKFRRQKPIGFYIVDFYCAEKKLVIEIDGGQHHEKKAEEYDARRDKYLESL
GYTVLRFWNEEVLNNIEGVLEKIEKFL
>gnl|CDD|381254 cd01040, Mb-like, myoglobin-like; M family globin domain. This family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The M family exhibits the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). In Adgbs, the globin domain is split into two: helices C-H are followed by helices A-B and the two parts are separated by the IQ motif. Although rearranged, the globin domain of most Adgbs contains a number of conserved residues which play critical roles in heme-coordination and gas ligand binding. Adgbs have been omitted from this A-H helix cd
VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLDLKGSPEFKAHAKRVVGALDSLIDNLDD
PEALDALLRKLGKRHKRRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI
>gnl|CDD|153100 cd01041, Rubrerythrin, Rubrerythrin, ferritin-like diiron-binding domain. Rubrerythrin domain is a nonheme iron binding domain found in many air-sensitive bacteria and archaea and member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The homodimeric rubrerythrin protein contains a binuclear metal center located within a four helix bundle. Many, but not all, rubrerythrin proteins have a second domain with a rubredoxin-like hexacoordinated iron center. Rubrerythrin is thought to reduce hydrogen peroxide as part of an oxidative stress protection system but its function is still poorly understood
KTEKNLLAAFAGESQARNRYTYFAEKARKEGYEQIARLFRATAENEKEHAKGHFKLLKGLGGGDTGPPIG
IGDTLENLKAAIAGETYEYTEMYPEFAEVAEEEGFKEAARSFEAIAEAEKVHAERYKKALENLE
>gnl|CDD|153101 cd01042, DMQH, Demethoxyubiquinone hydroxylase, ferritin-like diiron-binding domain. Demethoxyubiquinone hydroxylases (DMQH) are members of the ferritin-like, diiron-carboxylate family which are present in eukaryotes (the CLK-1/CAT5 family) and prokaryotes (the Coq7 family). DMQH participates in one of the last steps of ubiquinone biosysnthesis and is responsible for DMQ hydroxylation, resulting in the formation of hydroxyubiquinone, a precursor of ubiquinone. CLK-1 is a mitochondrial inner membrane protein and Coq7 is a proposed interfacial integral membrane protein. Mutations in the Caenorhabditis elegans gene clk-1 affect biological timing and extend longevity. The conserved residues of a diiron center are present in this domain
LARILRVNHAGEVGAVRIYRGQLAVARDPAVRPLIKEMLDEEKDHLAWFEELLPELGVRPSLLLPLWYVA
GFALGALTALLGKKAAMACTAAVETVVEEHYNDQLRELPAQPDKELRAIIEQFRDDELEHADIAEELGAE
KAPLYALLKALIKAGCKVAIWLAKR
>gnl|CDD|153102 cd01043, DPS, DPS protein, ferritin-like diiron-binding domain. DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic
EALNQLLADLYVLYLKLKNYHWNVKGPNFFALHELFEELYDELREAIDEIAERIRALGGKPLGTLKEYAE
LSTIKEEPAGVLSAKEMVAELLEDYETLIEELREAIELADEAGDPATADLLTEIIRELEKQAWMLRAHL
>gnl|CDD|153103 cd01044, Ferritin_CCC1_N, Ferritin-CCC1, N-terminal ferritin-like diiron-binding domain. Ferritin-like N-terminal domain present in an uncharacterized family of proteins found in bacteria and archaea. These proteins also have a C-terminal CCC1-like transmembrane domain and are thought to be involved in iron and/or manganese transport. This domain has the conserved residues of a diiron center found in other ferritin-like proteins
KRLRKFQKDEITEAAIYRKLAKREKDPENREILLKLAEDERRHAEFWKKFLGKRGVPPPRPKLKIFFYKL
LARIFGPTFVLKLLERGEERAIEKYDRLLEERPELKEIIADELEHEEVLIALLDE
>gnl|CDD|153104 cd01045, Ferritin_like_AB, Uncharacterized family of ferritin-like proteins found in archaea and bacteria. Ferritin-like domain found in archaea and bacteria (Ferritin_like_AB). This uncharacterized domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins whose function is unknown. This family includes unknown or hypothetical proteins which were sequenced from mostly anaerobic or microaerophilic metal-metabolizing and/or nitrogen-fixing microbes. The family includes sequences from ferric-, sulfate-, and arsenic-reducing bacteria, Geobacter, Magnetospirillum, Desulfovibrio, and Desulfitobacterium. Also included are several nitrogen-fixing endosymbiotic bacteria, Rhizobium, Mesorhizobium, and Bradyrhizobium; also phototrophic purple nonsulfur bacteria, Rhodobacter and Rhodopseudomonas, as well as, obligate thermophiles, Thermotoga, Thermoanaerobacter, and Pyrococcus. The conserved residues of a diiron center are present in this uncharacterized domain
EILALAIKMEEEAAEFYLELAEKAKDPELKKLFEELAEEEKEHAERLEELYEKLFGEELPELEPEDYKEE
VEEEPEFKKALESLMDPLEALRLAIEIEKDAIEFYEELAEKAEDPEVKKLFEELAEEERGHLRLLEELY
>gnl|CDD|153105 cd01046, Rubrerythrin_like, rubrerythrin-like, diiron-binding domain. Rubrerythrin-like domain, similar to rubrerythrin, a nonheme iron binding domain found in many air-sensitive bacteria and archaea, and member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Rubrerythrin is thought to reduce hydrogen peroxide as part of an oxidative stress protection system. The rubrerythrin protein has two domains, a binuclear metal center located within a four-helix bundle of the rubrerythrin domain, and a rubredoxin domain. The Rubrerythrin-like domains in this CD are singular domains (no C-terminus rubredoxin domain) and are phylogenetically distinct from rubrerythrin domains of rubrerythrin-rubredoxin proteins
DLEEDLEANFKGETTEVGMYLAMARVAQREGYPEVAEELKRIAMEEAEHAARFAELLGKVSEDTKENLEM
MLEGEAGANEGKKDAATEAKAEGLDEAHDFFHEAAKDEARHGKMLKGLLERYF
>gnl|CDD|153106 cd01047, ACSF, Aerobic Cyclase System Fe-containing subunit (ACSF), ferritin-like diiron-binding domain. Aerobic Cyclase System, Fe-containing subunit (ACSF) is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Rubrivivax gelatinosus acsF codes for a conserved, putative binuclear iron-cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethyl ester. AcsF and homologs have a leucine zipper and two copies of the conserved glutamate and histidine residues predicted to act as ligands for iron in the Ex(29-35)DExRH motifs. Several homologs of AcsF are found in a wide range of photosynthetic organisms, including Chlamydomonas reinhardtii Crd1 and Pharbitis nil PNZIP, suggesting that this aerobic oxidative cyclization mechanism is conserved from bacteria to plants
TLLTPRFYTTDFDEMAALDISKNREEFEAMLAEFKADYNRHHFVRNDEFDQAADKIDPELRQIFLEFLER
SCTSEFSGFLLYKELGRRLKNTNPVVAELFRLMARDEARHAGFLNKALSDFNLALDLGFLTKTRKYTFFK
PKFIFYATYLSEKIGYWRYITIYRHLERNPENQFHPIFKYFENWCQDENRHGDFFAALLRAQPHLLNDGK
NKLWIRFFLLSVYATMYLNDHQRPDFYEALGLDTTEFDMHVIRETNETAARVFPAVLDVDNPEFRRGLDR
LVDLNLKLEAIGASAPGLVKKLQRLPLIAALGELIARLLMKPV
>gnl|CDD|153107 cd01048, Ferritin_like_AB2, Uncharacterized family of ferritin-like proteins found in archaea and bacteria. Ferritin-like domain found in archaea and bacteria, subgroup 2 (Ferritin_like_AB2). This uncharacterized domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins whose function is unknown. The conserved residues of a diiron center are present within the putative active site
EIAALLYALEEEKLARDVYLALYEKFGGLRPFSNIAESEQRHMDALKTLLERYGLPDPVDPFSGGVFTNP
QYNQLVEQGPKSLQDALEVGVLIEELDIADYDRLLERTQNPDIRDVFENLQAASRNHHLPFFRRL
>gnl|CDD|153108 cd01049, RNRR2, Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain. Ribonucleotide Reductase, R2/beta subunit (RNRR2) is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The RNR protein catalyzes the conversion of ribonucleotides to deoxyribonucleotides and is found in all eukaryotes, many prokaryotes, several viruses, and few archaea. The catalytically active form of RNR is a proposed alpha2-beta2 tetramer. The homodimeric alpha subunit (R1) contains the active site and redox active cysteines as well as the allosteric binding sites. The beta subunit (R2) contains a diiron cluster that, in its reduced state, reacts with dioxygen to form a stable tyrosyl radical and a diiron(III) cluster. This essential tyrosyl radical is proposed to generate a thiyl radical, located on a cysteine residue in the R1 active site that initiates ribonucleotide reduction. The beta subunit is composed of 10-13 helices, the 8 longest helices form an alpha-helical bundle; some have 2 addition beta strands. Yeast is unique in that it assembles both homodimers and heterodimers of RNRR2. The yeast heterodimer, Y2Y4, contains R2 (Y2) and a R2 homolog (Y4) that lacks the diiron center and is proposed to only assist in cofactor assembly, and perhaps stabilize R1 (Y1) in its active conformation
FNLNPIKYPWAWELYKKAEANFWTPEEIDLSKDLKDWEKLTEAERHFIKRVLAFLAALDSIVGENLVELF
SRHVQIPEARAFYGFQAFMENIHSESYSYILDTLGKDEERDELFEAIETDPALKKKADWILRWYDNLDDN
TKESFAERLVAFAILEGIFFYSGFAAIFWLARRGKMPGLAEIIELISRDESLHGDFACLLIRELLNENPE
LFTEEFKEEVYELIKEAVELEKEFARDLLPDGILGLNKEDMKQYIEYVANRRLENLGLEKLFNVEDKNPF
DWMELISD
>gnl|CDD|153109 cd01050, Acyl_ACP_Desat, Acyl ACP desaturase, ferritin-like diiron-binding domain. Acyl-Acyl Carrier Protein Desaturase (Acyl_ACP_Desat) is a mu-oxo-bridged diiron-carboxylate enzyme, which belongs to a broad superfamily of ferritin-like proteins and catalyzes the NADPH and O2-dependent formation of a cis-double bond in acyl-ACPs. Acyl-ACP desaturases are found in higher plants and a few bacterial species (Mycobacterium tuberculosis, M. leprae, M. avium and Streptomyces avermitilis, S. coelicolor). In plants, Acyl-ACP desaturase is a plastid-localized, covalently ACP linked, soluble desaturase that introduces the first double bound into saturated fatty acids, resulting in the corresponding monounsaturated fatty acid. Members of this class of soluble desaturases are specific for a particular substrate chain length and introduce the double bond between specific carbon atoms. For example, delta 9 stearoyl-ACP is specific for stearic acid and introduces a double bond between carbon 9 and 10 to yield oleic acid in the ACP-bound form. The enzymatic reaction requires molecular oxygen, NAD(P)H, NAD(P)H ferredoxin oxido-reductase and ferredoxin. The enzyme is active in the homodimeric form; the monomer consists mainly of alpha-helices with the catalytic diiron center buried within a four-helix bundle. Integral membrane fatty acid desaturases that introduce double bonds into fatty acid chains, acyl-CoA desaturases of animals, yeasts, and fungi, and acyl-lipid desaturases of cyanobacteria and higher plants, are distinct from soluble acyl-ACP desaturases, lack diiron centers, and are not included in this CD
TKLELLRSLEPVVEENLLNRLKPVEKDWQPHDFLPDSASEDFDLDVKELRERAAELPDDARVALVGNLLT
EEALPTYHSMLNRLFGLDDESPTAWARWVRRWTAEENRHGDLLNKYLYLTGRVDPRALERTRQYLIGSGF
DPGTDNSPYRGFVYTSFQELATRISHRNTARLAGAGDPVLAKLLGRIAADEARHEAFYRDIVEALFELDP
DGAVLAFADMMRKIVMPGHLMYPLFERFAAVAARAGVYTARDYDDILEPLVRRWRVEELTGLSGEGRKAQ
EYLCALPARLRRLAERA
>gnl|CDD|153110 cd01051, Mn_catalase, Manganese catalase, ferritin-like diiron-binding domain. Manganese (Mn) catalase is a member of a broad superfamily of ferritin-like diiron enzymes. While many diiron enzymes catalyze dioxygen-dependent reactions, manganese catalase performs peroxide-dependent oxidation-reduction. Catalases are important antioxidant metalloenzymes that catalyze disproportionation of hydrogen peroxide, forming dioxygen and water. Manganese catalase, a nonheme type II catalase, contains a binuclear manganese cluster that catalyzes the redox dismutation of hydrogen peroxide, interconverting between dimanganese(II) [(2,2)] and dimanganese(III) [(3,3)] oxidation states during turnover. Mn catalases are found in a broad range of microorganisms in microaerophilic environments, including the mesophilic lactic acid bacteria (e.g., Lactobacillus plantarum) and bacterial and archaeal thermophiles (e.g., Thermus thermophilus and Pyrobaculum caldifontis). L. plantarum and T. thermophilus holoenzymes are homohexameric structures; each subunit contains a dimanganese active site. The manganese ions are linked by a mu 1,3-bridging glutamate carboxylate and two mu-bridging solvent oxygens that electronically couple the metal centers. Several members of this CD lack the C-terminal strands that pack against the neighboring catalytic domains as seen in L. plantarum. One such sequence, Bacillus subtilis CotJC, is known to be a component of the inner spore coat that interacts with spore coat protein, CotJA. It has been suggested that CotJC could modulate the degree of Mn SodA-dependent cross-linking of an outer coat component, or the two enzymes could serve to protect specific cellular structures during the developmental process
MFYHVKKLQYPVRVDKPDPRFAKLLQEQLGGAFGELSAAMQYLFQSFNFREDPKYRDLLLDIGTEELSHL
EMVATLIAMLLKDSQGVPWTAAYIQSSGNLVADLRSNIAAESRARLTYERLYEMTDDPGVKDTLSFLLVR
EIVHQNAFGKALESLG
>gnl|CDD|153111 cd01052, DPSL, DPS-like protein, ferritin-like diiron-binding domain. DPSL (DPS-like). DPSL is a phylogenetically distinct class within the ferritin-like superfamily, and similar in many ways to the DPS (DNA Protecting protein under Starved conditions) proteins. Like DPS, these proteins are expressed in response to oxidative stress, form dodecameric cage-like particles, preferentially utilize hydrogen peroxide in the controlled oxidation of iron, and possess a short N-terminal extension implicated in stabilizing cellular DNA. This domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. These proteins are distantly related to bacterial ferritins which assemble 24 monomers, each of which have a four-helix bundle with a fifth shorter helix at the C terminus and a diiron (ferroxidase) center. Ferritins contain a center where oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of iron in the ferric form. Many of the conserved residues of a diiron center are present in this domain
GLDVDELIELLNKAFADEWLAYYYYTILAKHVKGPEGEGIKEELEEAAEEELNHAELLAERIYELGGTPP
RDPKDWYEISGCKCGYLPPDPPDVKGILKVNLKAERCAIKVYKELCDMTHGKDPVTYDLALAILNEEIEH
EEDLEELL
>gnl|CDD|153112 cd01053, AOX, Alternative oxidase, ferritin-like diiron-binding domain. Alternative oxidase (AOX) is a mitochondrial ubiquinol oxidase found in plants and some fungi and protists. AOX is a member of the ferritin-like diiron-carboxylate superfamily. The plant mitochondrial protein alternative oxidase catalyses dioxygen dependent ubiquinol oxidation to yield ubiquinone and water. AOX is a cyanide-resistant, salicylhydroxamic acid-sensitive oxidase that transfers electrons from ubiquinol to oxygen, bypassing the cytochrome chain. AOX has been proposed to contain a hydroxo-bridged diiron center within a four-helix bundle and a proximal redox-active tyrosine residue. AOX is proposed to be peripherally associated with the matrix side of the inner mitochondrial membrane. Fungal and protozoan AOXs generally exist as monomers. In plants, AOX is dimeric. Pyruvate is an allosteric activator of plant AOX involved in the reversible inactivation of the enzyme though the formation of an intermolecular disulfide bridge between monomeric subunits. The enzyme is non-proton-motive and does not contribute to the conservation of energy. The heat that dissipates from AOX activity is used in thermogenic plants to volatilize primary amines to attract pollinating insects. Other functions have been proposed: i) that the alternative oxidase allows Krebs-cycle turnover when the energy charge of the cell is high, and ii) that the enzyme protects against oxidative stress. The expression of AOX is induced when plants are exposed to a variety of stresses including chilling, pathogen attack, senescence and fruit ripening
YEDRWLARFIFLETVARVPGMVAGMLLHLYSLRGMWRDGGWIKTLLEEAENERMHLLIFEELGGPGWWFR
RFVAQHQAVFYNAYFLLYLISPRLAHRFVGYLEEEAVDTYTEFLKDIEEGLKPDLPAPEIAIEYYRLGED
ATLYDVFVAIRADEAEHRKVNHACADLG
>gnl|CDD|153113 cd01055, Nonheme_Ferritin, nonheme-containing ferritins. Nonheme Ferritin domain, found in archaea and bacteria, is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The ferritin protein shell is composed of 24 protein subunits arranged in 432 symmetry. Each protein subunit, a four-helix bundle with a fifth short terminal helix, contains a dinuclear ferroxidase center (H type). Unique to this group of proteins is a third metal site in the ferroxidase center. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite
SEKLEKALNEQINLELYSSYLYLAMAAWFDSKGLDGFANFFRVQAQEEREHAMKFFDYLNDRGGRVELPA
IEAPPSEFESLLEVFEAALEHEQKVTESINNLVDLALEEKDYATFNFLQWFVKEQVEEEALARDILDKLK
LAGDDGGGLYMLDKEL
>gnl|CDD|153114 cd01056, Euk_Ferritin, eukaryotic ferritins. Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary iron storage proteins of most living organisms and members of a broad superfamily of ferritin-like diiron-carboxylate proteins. The iron-free (apoferritin) ferritin molecule is a protein shell composed of 24 protein chains arranged in 432 symmetry. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the dinuclear ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite; the protein shell can hold up to 4500 iron atoms. In vertebrates, two types of chains (subunits) have been characterized, H or M (fast) and L (slow), which differ in rates of iron uptake and mineralization. Fe(II) oxidation in the H/M subunits take place initially at the ferroxidase center, a carboxylate-bridged diiron center, located within the subunit four-helix bundle. In a complementary role, negatively charged residues on the protein shell inner surface of the L subunits promote ferrihydrite nucleation. Most plant ferritins combine both oxidase and nucleation functions in one chain: they have four interior glutamate residues as well as seven ferroxidase center residues
HEECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVL
QDIKKPEKDEWGSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYI
TNLKRVGKPQSGLGEYLFDKY
>gnl|CDD|153115 cd01057, AAMH_A, Aromatic and Alkene Monooxygenase Hydroxylase, subunit A, ferritin-like diiron-binding domain. Aromatic and Alkene Monooxygenase Hydroxylases, subunit A (AAMH_A). Subunit A of the soluble hydroxylase of multicomponent, aromatic and alkene monooxygenases are members of a superfamily of ferritin-like iron-storage proteins. AAMH exists as a hexamer (an alpha2-beta2-gamma2 homodimer) with each alpha-subunit housing one nonheme diiron center embedded in a four-helix bundle. The N-terminal domain of the alpha- and noncatalytic beta-subunits possess nearly identical folds, however, the beta-subunit lacks critical diiron ligands and a C-terminal domain found in the alpha-subunit. Methane monooxygenase is a multicomponent enzyme found in methanotrophic bacteria that catalyzes the hydroxylation of methane and higher alkenes (as large as octane). Phenol monooxygenase, found in a diverse group of bacteria, catalyses the hydroxylation of phenol, chloro- and methyl-phenol and naphthol. Both enzyme systems consist of three components: the hydroxylase, a coupling protein and a reductase. In the MMO hydroxylase, dioxygen and substrate interact with the diiron center in a hydrophobic cavity at the active site. The reductase component and protein coupling factor provide electrons from NADH for reducing the oxidized binuclear iron-oxo cluster to its reduced form. Reaction with dioxygen produces a peroxy-bridged complex and dehydration leads to the formation of complex Q, which is thought to be the oxygenating species that carries out the insertion of an oxygen atom into a C-H bond of the substrate. The toluene monooxygenase systems, toluene 2-, 3-, and 4-monooxygenase, are similar to MMO but with an additional component, a Rieske-type ferredoxin. The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol. Alkane omega-hydroxylase (AlkB) and xylene monooxygenase are members of a distinct class of integral membrane diiron proteins and are not included in this CD
TRDLDWDFSYVDEDDKFPTKYKMPIKIPDWDKWKDPFKLTMREYVKMQAEKDKRVYGVLDAAVRSGAYEK
VDPRWVEAMKLFLGAITPGEYAAVRGMAMLGRFAPAAELRNGYLMQMLDELRHTQIQLYLPHYYAKNYAG
FDWAQKAFHGNWYAGAAKRFFFDGFITGDAVEAALALQFVFETAFTNLLFVALASDAAANGDYATPTVFL
SIQSDEARHMANGYPTLVLLENDPDNVPLLQRDLDKAFWRQHRLFDALVGMLMDYGTPKRVMSWKEFWEE
WIEEDFGSYFKDLEKYGLKKPWYWDDAKKEKDWYHHQLALGFYAWWPTNFWRPDAPTPEEMEWFEEKYPG
WYKYYGKFWEEIRKNAAEGKRELFYPETLPPLCNVCQVPCVFTEDLTAEAPRVLEYNGRKYHFCSEGCEW
IFEQEPERYAGHWNPVDRFLGGELADVILELGLLRSDGKTLIGQP
>gnl|CDD|153116 cd01058, AAMH_B, Aromatic and Alkene Monooxygenase Hydroxylase, subunit B, ferritin-like diiron-binding domain. Aromatic and Alkene Monooxygenase Hydroxylases, subunit B (AAMH_B). Subunit B (beta) of the soluble hydroxylase of multicomponent, aromatic and alkene monooxygenases are members of a superfamily of ferritin-like iron-storage proteins. AAMH exists as a hexamer (an alpha2-beta2-gamma2 homodimer) with each alpha-subunit housing one nonheme diiron center embedded in a four-helix bundle. The N-terminal domain of the alpha- and noncatalytic beta-subunits possess nearly identical folds; the beta-subunit lacks the C-terminal domain found in the alpha-subunit. Methane monooxygenase is a multicomponent enzyme found in methanotrophic bacteria that catalyzes the hydroxylation of methane and higher alkenes (as large as octane). Phenol monooxygenase, found in a diverse group of bacteria, catalyses the hydroxylation of phenol, chloro- and methyl-phenol and naphthol. Both enzyme systems consist of three components: the hydroxylase, a coupling protein and a reductase. In the MMO hydroxylase, dioxygen and substrate interact with the diiron center in a hydrophobic cavity at the active site. The reductase component and protein coupling factor provide electrons from NADH for reducing the oxidized binuclear iron-oxo cluster to its reduced form. Reaction with dioxygen produces a peroxy-bridged complex and dehydration leads to the formation of complex Q, which is thought to be the oxygenating species that carries out the insertion of an oxygen atom into a C-H bond of the substrate. The toluene monooxygenase systems, toluene 2-, 3-, and 4-monooxygenase, are similar to MMO but with an additional component, a Rieske-type ferredoxin. The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol. Alkane omega-hydroxylase (AlkB) and xylene monooxygenase are members of a distinct class of integral membrane diiron proteins and are not included in this CD
RRRRPSEYEDVTRYQQPTPDRQPTPNWHYRPLFDNGRPLYDRESTALRMSDWYAFRDPRQFWYRTYVQMR
AEQERYVERLFEFAEKRGLAEALSPEWREFLARYLGPLRHVEHGLQMANAYVAQYAPSTTITNAAAFQAM
DKLRIAQDIAYRGLELDGNTPGFDGDAAKEAWEEDPAWQGLRELVEKLLVTYDWGEAFVAQNLVFDPLVG
ELVRRELDRLAASNGDTLTPLLTEFMLDDAQRHRRWTDALVKTAAEDSPHNRALLQGWLEKWRPRALAAL
AALAIALSASLPAAVAAARADLAA
>gnl|CDD|153121 cd01059, CCC1_like, CCC1-related family of proteins. CCC1_like: This protein family includes the proteins related to CCC1, a yeast vacuole transmembrane protein responsible for the iron and manganese transport from the cytosol into vacuole. It also includes the proteins similar to nodulin-21, a plant nodule-specific protein that may be involved in symbiotic nitrogen fixation
LRAAVLGANDGLVSTFALVAGVAAAGDSTKAILLAGLAGLVAGAISMAAGEYVSVKSQRDKAALASGLSF
ILGGLLPLLPYLLLPAGSLALAVSVALVVALALFLLGAFVAKLGGAKKIRAALRMVVLGLLAAALTYLLG
RLF
>gnl|CDD|238511 cd01060, Membrane-FADS-like, The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane hydroxylases, beta carotene ketolases (CrtW-like), hydroxylases (CrtR-like), and other related proteins. They are present in all groups of organisms with the exception of archaea. Membrane FADSs are non-heme, iron-containing, oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains. They play an important role in the maintenance of the proper structure and functioning of biological membranes. Alkane hydroxylases are bacterial, integral-membrane di-iron enzymes that share a requirement for iron and oxygen for activity similar to that of membrane FADSs, and are involved in the initial oxidation of inactivated alkanes. Beta-carotene ketolase and beta-carotene hydroxylase are carotenoid biosynthetic enzymes for astaxanthin and zeaxanthin, respectively. This superfamily domain has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXX(X)H, HXX(X)HH, and HXXHH (an additional conserved histidine residue is seen between clusters 2 and 3). Spectroscopic and genetic evidence point to a nitrogen-rich coordination environment located in the cytoplasm with as many as eight histidines coordinating the two iron ions and a carboxylate residue bridging the two metals in the Pseudomonas oleovorans alkane hydroxylase (AlkB). In addition, the eight histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the rat stearoyl CoA delta-9 desaturase
LLLALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRRHHRYTNTPGKDP
DSAVNYLEHYGGDRPFDTDGEWLRTTDNSRNGWLNLLLTGGLGYHNEHHLFP
>gnl|CDD|238512 cd01061, RNase_T2_euk, Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases). Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleotides. They are also expressed in response to wounding or pathogen invasion. S-RNases are thought to prevent self-fertilization by acting as selective cytotoxins of "self" pollen. Generally, RNases have two distinct binding sites: the primary site (B1 site) and the subsite (B2 site), for nucleotides located at the 5'- and 3'- terminal ends of the sessil bond, respectively. This CD includes the eukaryotic RNase T2 family members
FDYLQLVLQWPDTYCSTGPCCCRPPPPDSFTIHGLWPDNCSGTYPQFCDSSSNFDSILISDLLNELNKYW
PDLTGPKNNQSFWEHEWNKHGTCSSTLLYNQYDYFDTALKLKDKLDLLKILAKAGIVPSTQTYTLSDIQN
AIKAATGVTPVIKCSKDPGKGELNEIWICFDKKGGEFIDCPRPPKSTCPDDGIKF
>gnl|CDD|238513 cd01062, RNase_T2_prok, Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases). Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleotides. They are also expressed in response to wounding or pathogen invasion. S-RNases are thought to prevent self-fertilization by acting as selective cytotoxins of "self" pollen. Generally, RNases have two distinct binding sites: the primary site (B1 site) and the subsite (B2 site), for nucleotides located at the 5'- and 3'- terminal ends of the sessil bond, respectively. This CD includes the prokaryotic RNase T2 family members
FDYYVLALSWQPGFCATQGDRPECATCGTLDAYGFTLHGLWPQKPKGGWPEYCGVTSEPPLSEETRSRLL
DVMPASGLIRHEWRKHGTCSGLDPDAYFAKARNLREALKIPPELRLLAGNIGVTASEIRQAFIKANPGLP
PDAVSVSCQGGLLTEVRICLDKDLKFAACPTADRDNCPAGTVDI
>gnl|CDD|133443 cd01065, NAD_bind_Shikimate_DH, NAD(P) binding domain of Shikimate dehydrogenase. Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts
TDGLGFVRALEEAGIELKGKKVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELGIAI
AYLDLEELLAEADLIINTTPVGMKPGDELPLPPSLLKPGGVVYDVVYNPLETPLLKEARALGAKTIDGLE
MLVYQAAEAFELWTG
>gnl|CDD|238514 cd01066, APP_MetAP, A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as metallopeptidase family M24. This family of enzymes is able to cleave amido-, imido- and amidino-containing bonds. Members exibit relatively narrow substrate specificity compared to other metallo-aminopeptidases, suggesting they play roles in regulation of biological processes rather than general protein degradation
IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGGYPAGPTIVGSGARTALPHYRPDDRRL
QEGDLVLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLE
EHGLGPNFGHRTGHGIGLEIHEPPVLKAGDDTVLEPGMVFAVEPGLYLPGGGGVRIEDTVLVTEDGP
>gnl|CDD|381255 cd01067, Globin-like, Globin-like protein superfamily. This globin-like domain superfamily contains a wide variety of all-helical proteins that bind porphyrins, phycobilins, and other non-heme cofactors, and play various roles in all three kingdoms of life, including sensors or transporters of oxygen. It includes the M/myoglobin-like, S/sensor globin, and T/truncated globin (TrHb) families, and the phycobiliproteins (PBPs). The M family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The S family includes GCS/globin-coupled sensors, Pgbs/protoglobins, and SSDgbs/sensor single domain globins. The T family is classified into three main groups: TrHb1s (N), TrHb2s (O) and TrHb3s (P). The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). For M family Adgbs, this globin domain is permuted, such that C-H are followed by A-B. The T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. PBPs bind the linear tetrapyrrole chromophore, phycobilin, a prosthetic group chemically and metabolically related to iron protoporphyrin IX/protoheme. Examples of other globin-like domains which bind non-heme cofactors include those of the Bacillus anthracis sporulation inhibitors pXO1-118 and pXO2-61 which bind fatty acid and halide in vitro, and the globin-like domain of Bacillus subtilis RsbRA which is presumed to channel sensory input to the C-terminal sulfate transporter/ anti-sigma factor antagonist (STAT) domain. RsbRA is a component of the sigma B-activating stressosome, and a regulator of the RNA polymerase sigma factor subunit sigma (B)
AWGYLEENQEEIVDDFYDRLFALPSLSELFSPPGRLAKCIRKQMHFLRYALYGLVDGDSIEEGLAGLGEA
HKSLGVPISYFIAALNVMKDVLTELLGDKFTPAAGEAWTKIFDYIISSM
>gnl|CDD|381256 cd01068, globin_sensor, Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor single-domain globins (SSDgbs); S family. This family includes sensor domains which binds porphyrins, and other non-heme cofactors. GCSs have an N-terminal sensor domain coupled to a functional domain. For heme-bound oxygen sensing/binding globin domains, O2 binds to/dissociates from the heme iron complex inducing a structural change in the sensor domain, which is then transduced to the functional domain, switching on (or off) the function of the latter. Functional domains include DGC/GGDEF, EAL, histidine kinase, MCP, PAS, and GAF domains. Characterized members include Bacillus subtilis heme-based aerotaxis transducer (HemAT-Bs) which has a sensor domain coupled to an MCP domain. HemAT-Bs mediates an aerophilic response, and may control the movement direction of bacteria and archaea. Its MCP domain interacts with the CheA histidine kinase, a component of the CheA/CheY signal transduction system that regulates the rotational direction of flagellar motors. Another GCS having the sensor domain coupled to an MCP domain is Caulobacter crescentus McpB. McpB is encoded by a gene which lies adjacent to the major chemotaxis operon. Like McpA (encoded on this operon), McpB has three potential methylation sites, a C-terminal CheBR docking motif, and a motif needed for proteolysis via a ClpX-dependent pathway during the swarmer-to-stalked cell transition. Also included is Geobacter sulfurreducens GCS, a GCS of unknown function, in which the sensor domain is coupled to a transmembrane signal-transduction domain. Pgbs are single-domain globins of unknown function. Methanosarcina acetivorans Pgbs is dimeric and has an N-terminal extension, which together with other Pgb-specific loops, buries the heme within the protein; small ligand molecules gain access to the heme via two orthogonal apolar tunnels. Pgbs and other single-domain globins can function as sensors, when coupled to an appropriate regulator domain
ERLEFLGLTEEDLALLRELRPLIEPHLDEILDAFYDHLLSFPELAAIFDDHSTIERLKQTQRAHWLELFS
GDFDEAYVERRRRIGRVHVRIGLEPRWYIGAYALLLEELIEIIAEELRKDPEELAELLLALVKALNLDMQ
LALEAY
>gnl|CDD|270231 cd01069, PBP2_PheC, Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein superfamily. This subfamily includes cyclohexadienyl dehydratase PheC. These proteins catalyze the decarboxylation of prephenate to phenylpyruvate in the alternative phenylalanine biosynthesis pathway in some proteobacteria and archaea. The PheC proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Since they the PheC proteins are so similar to periplasmic binding proteins, (PBP), it is evolutionarily plausible that several pre-existing PBP proteins might have been recruited to perform the enzymatic function
SRLDKILERGVLRVGTTGDYKPFTYRDNQGQYEGYDIDMAEALAKSLGVKVEFVPTSWPTLMDDLAADKF
DIAMGGISITLERQRQAFFSAPYLRFGKTPLVRCADVDRFQTLEAINRPGVRVIVNPGGTNEKFVRANLK
QATITVHPDNLTIFQAIADGKADVMITDAVEARYYQKLDPRLCAVHPDKPFTFSEKAYMIPRDDQALKRY
VDQWLHIMEGSGLLDQLSNKWL
>gnl|CDD|270232 cd01071, PBP2_PhnD_like, Substrate binding domain of phosphonate uptake system-like, a member of the type 2 periplasmic-binding fold superfamily. This family includes alkylphosphonate binding domain PhnD. These domains are found in PhnD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. PhnD is the periplasmic binding component of an ABC-type phosphonate uptake system (PhnCDE) that recognizes and binds phosphonate. PhnD belongs to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. The PBP2 have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
AAPKELRFGLVPAEDADELKKEFEPLADYLEEELGVPVELVVATSYAAVVEAMRNGKVDIAWLGPASYVL
AHDRAGAEALATEVRDGSPGYYSVIIVRKDSPIKSLEDLKGKTVAFVDPSSTSGYLFPRAMLKDAGIDPP
DFFFEVVFAGSHDSALLAVANGDVDAAATYDSTLERAAAAGPIDPDDLRVIWRSPPIPNDPLVVRKDLPP
ALKAKIRDALLDLDETDEGQKLLAGLGLTGFVPATDDDYDPIR
>gnl|CDD|270233 cd01072, PBP2_SMa0082_like, The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic binding protein fold. This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Sinorhizobium meliloti and its related proteins. The putative SMa0082-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
AAADTLDDIKKRGKLKVGVLVDAPPFGFVDASMQPQGYDVDVAKLLAKDLGVKLELVPVTGANRIPYLQT
GKVDMLIASLGITPERAKVVDFSQPYAAFYLGVYGPKDAKVKSPADLKGKTVGVTRGSTQDIALTKAAPK
GATIKRFDDDASTIQALLSGQVDAIATGNAIAAQIAKANPDKKYELKFVLRTSPNGIGVRKGEPELLKWV
NTFIAKNKANGELNALSQKWFGTPLPDL
>gnl|CDD|133444 cd01075, NAD_bind_Leu_Phe_Val_DH, NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase. Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts
PSPPTAYGVFLGMKAAAEHLLGTDSLEGKTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAEL
FGATVVAPEEIYSVDADVFAPCALGGVINDDTIPQLKAKAIAGAANNQLADPRHGQMLHERGILYAPDYV
VNAGGLINVADELYGGNEARVLAKVEAIYDTLLEIFAQAKQDGITTLEAADRMAEERIAA
>gnl|CDD|133445 cd01076, NAD_bind_1_Glu_DH, NAD(P) binding domain of glutamate dehydrogenase, subgroup 1. Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. Glutamate DH is a multidomain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia assimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha -beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts
GGSLGREEATGRGVAYATREALKKLGIGLAGARVAIQGFGNVGSHAARFLHEAGAKVVAVSDSDGTIYNP
DGLDVPALLAYKKEHGSVLGFPGAERITNEELLELDCDILIPAALENQITADNADRIKAKIIVEAANGPT
TPEADEILHERGVLVVPDILANAGGVTVSYFEWVQNLQGFYWDEEEVNSRLETKMREAFEAVLETAEKYG
VDLRTAAYVLALERVAE
>gnl|CDD|133446 cd01078, NAD_bind_H4MPT_DH, NADP binding domain of methylene tetrahydromethanopterin dehydrogenase. Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts
SNGSNTTAAAAVAAAGKALELMGKDLKGKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAAD
SLRARFGEGVGAVETSDDAARAAAIKGADVVFAAGAAGVELLEKLAWAPKPLAVAADVNAVPPVGIEGID
VPDKGVDREGKVPYGAIGVGGLKMKTHRACIAKLFESNPLVLDAEEIYDLAKEM
>gnl|CDD|133447 cd01079, NAD_bind_m-THF_DH, NAD binding domain of methylene-tetrahydrofolate dehydrogenase. The NAD-binding domain of methylene-tetrahydrofolate dehydrogenase (m-THF DH). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. M-THF DH is a component of an unusual monofunctional enzyme; in eukaryotes, m-THF DH is typically found as part of a multifunctional protein. NADP-dependent m-THF DHs in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofunctional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains only the monofunctional DHs from S. cerevisiae and certain bacteria. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts
PHKDVEGLSHKYIFNLYHNIRFLDPENRKKSILPCTPLAIVKILEFLGIYNKILPYGNRLYGKTITIINR
SEVVGRPLAALLANDGARVYSVDINGIQVFTRGESIRHEKHHVTDEEAMTLDCLSQSDVVITGVPSPNYK
VPTELLKDGAICINFASIKNFEPSVKEKASIYVPSIGKVTIAMLLRNLLRLYHNQHH
>gnl|CDD|133448 cd01080, NAD_bind_m-THF_DH_Cyclohyd, NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase. NADP binding domain of the Methylene-Tetrahydrofolate Dehydrogenase/cyclohydrolase (m-THF DH/cyclohydrolase) bifunctional enzyme. Tetrahydrofolate is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofucntional DH, as well as bifunctional m-THF m-THF DHm-THF DHDH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains the bifunctional DH/cyclohydrolase. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains
PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNAT
VTVCHSKTKNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDKSGGKLVGDVDFESAKEK
ASAITPVPGGVGPMTVAMLMKNTVEAAK
>gnl|CDD|185695 cd01081, Aldose_epim, aldose 1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism; they catalyze the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate and the histidine as the active site acid to protonate the C-5 ring oxygen
AVAVIAPRGANIISLKVKGDVDLLWGYPDAEEYPLAPTGGGGAILFPFANRISDGRYTFDGKQYPLNEDE
GGNAIHGFVRNLPWRVVATDEEEASVTLSYDLNDGPGGYPFPLELTVTYTLDADTLTITFTVTNLGDEPM
PFGLGWHPYFGLPGVAIEDLRLRVPASKVLPLDDLLPPTGELEVPGEEDFRLGRPLGGGELDDCFLLLGN
DAGTAEARLEDPDSRISVEFETGWPFWQVYTGDGGRRGSVAIEPMTSAPDAFFNNNGGLITLKPPGETRT
FSIT
>gnl|CDD|238517 cd01083, GAG_Lyase, Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of secreted bacterial lyase enzymes capable of acting on glycosaminoglycans, such as hyaluronan and chondroitin, in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen. These are broad-specificity glycosaminoglycan lyases which recognize uronyl residues in polysaccharides and cleave their glycosidic bonds via a beta-elimination reaction to form a double bond between C-4 and C-5 of the non-reducing terminal uronyl residues of released products. Substrates include chondroitin, chondroitin 4-sulfate, chondroitin 6-sulfate, and hyaluronic acid. Family members include chondroitin AC lyase, chondroitin abc lyase, xanthan lyase, and hyalurate lyase
EFDALRKRWADIITGNPAYDTSMAKAITLLDEKARDNLSDLDPASSRTGVWYDKDNFEDSANLTATYRRL
ETLAKAYTTPGSTYYQDEELKSDILDALDYLYDQGYNDGKGSYGNWWDWEIGIPRALNNTLVLMYDELSE
ELIKKYTDAIRWFVPDPEHQRTKPNPITSTGANRVDLARVVLIRGLLEKDAVKLKQASDGLSSVLQYVTE
GDGFYADGSFIQHGGVPYTGGYGNVLLKGLSQLLYLLSGTPFEVSDEARSNLYKWILEAYAPLIYKGEMM
DMVRGRSISRSNAQSHAVGVEILASLLLLADAAPKALAAALRSLIKRWITRDTYYPVFNNPKSYSDIKLL
LADASIAPAAEPQGHKQFNSMDRAVHRRPDFAFGLSMYSTRTANYEAGNGENLKGWYTGDGMTYLYNNDG
DQYSDFYWPTWDWYRLPGTTTIHLPLADLVEGSWGMKRGTSNFVGGVSLGKYGAAGMDLDNWDQSLTAKK
SWFFLDDEIVALGSGITNTSGAPVETTVDQRKLTGPGTVYVNGKETALGEQSFTLTGGSWVHLEGDNIGY
YFPKGATLSVSKEERTGAWKDINANGSDKEVTGNFFTLWIDHGKNPTNASYAYVLLPGATREKVKAYAKK
PNVEVLENDETAQAVYDNTLGVTGANFWKDGTSTLSLEITVNKPCSVMIRKESNGLKLSVSDP
>gnl|CDD|238518 cd01085, APP, X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline aminopeptidase, aminopeptidase P, and aminoacylproline aminopeptidase. Catalyses release of any N-terminal amino acid, including proline, that is linked with proline, even from a dipeptide or tripeptide
GMRAAHIRDGVALVEFLAWLEQEVPKGETITELSAADKLEEFRRQQKGYVGLSFDTISGFGPNGAIVHYS
PTEESNRKISPDGLYLIDSGGQYLDGTTDITRTVHLGEPTAEQKRDYTLVLKGHIALARAKFPKGTTGSQ
LDALARQPLWKAGLDYGHGTGHGVGSFLNVHEGPQSISPAPNNVPLKAGMILSNEPGYYKEGKYGIRIEN
LVLVVEAETTEFGG
>gnl|CDD|238519 cd01086, MetAP1, Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and Peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides
IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGI
PDDRVLKDGDIVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHA
IEKYAEKNGYSVVREFGGHGIGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWT
VVTKDGSLSAQFEHTVLITEDGPEILTL
>gnl|CDD|238520 cd01087, Prolidase, Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline dipeptidase., imidodipeptidase, peptidase D, gamma-peptidase. Catalyses hydrolysis of Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro
IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGARLAYSYIVAAGSNAAILHYVHNDQPL
KDGDLVLIDAGAEYGGYASDITRTFPVNGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVL
AEGLKELGILKGDVDEIVESGAYAKFFPHGLGHYLGLDVHDVGGYLRYLRRARPLEPGMVITIEPGIYFI
PDLLDVPEYFRGGGIRIEDDVLVTEDGPENLTR
>gnl|CDD|238521 cd01088, MetAP2, Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides
LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGAGPAFPVNLSINECAAHYTPNAGDDTV
LKEGDVVKLDFGAHVDGYIADSAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESY
GFKPIRNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRDKP
LRLPRARKLLDVIYENFGTLPFARRWLDRLGETKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTII
VREDGKEVTTR
>gnl|CDD|238522 cd01089, PA2G4-like, Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family members have been implicated in cell cycle control
VTKYKTAGQIANKVLKQVISLCVPGAKVVDLCEKGDKLILEELGKVYKKEKKLEKGIAFPTCISVNNCVC
HFSPLKSDATYTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETPVTGKKADVIAAAHYALEAALRLL
RPGNQNSDITEAIQKVIVDYGCTPVEGVLSHQLKRVVSSGEGKAKLVECVKHGLLFPYPVLYEKEGEVVA
QFKLTVLLTPNGVTVLTG
>gnl|CDD|238523 cd01090, Creatinase, Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea
IALIRHGARIADIGGAAVVEAIREGVPEYEVALAGTQAMVREIAKTFPEVELMDTWTWFQSGINTDGAHN
PVTNRKVQRGDILSLNCFPMIAGYYTALERTLFLDEVSDAHLKIWEANVAVHERGLELIKPGARCKDIAA
ELNEMYREHDLLRYRTFGYGHSFGVLSHYYGREAGLELREDIDTVLEPGMVVSMEPMIMLPEGQPGAGGY
REHDILVINENGAENITG
>gnl|CDD|238524 cd01091, CDC68-like, Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in cell division control protein 68, a transcription factor
LNNIKKASDATVDVLKKFFVDEVEEIIDQEKKVTHSKLSDKVEKAIEDKKKYKAKLDPEQLDWCYPPIIQ
SGGNYDLLKSSSSSDKLLYHFGVIICSLGARYKSYCSNIARTFLIDPTSEQQKNYNFLLALQEEILKELK
PGAKLSDVYQKTLDYIKKKKPELEPNFTKNLGFGIGLEFRESSLIINAKNDRKLKKGMVFNLSIGFSNLQ
NPEPKDKESKTYALLLSDTILVTEDEPAIVLTN
>gnl|CDD|238525 cd01092, APP-like, Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse hydrolysis of Xaa-Pro dipeptides and/or release of any N-terminal amino acid, including proline, that is linked with proline
IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEGPSFDTIVASGPNSALPHGVPSDRK
IEEGDLVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVI
EEAGYGEYFIHRTGHGVGLEVHEAPYISPGSDDVLEEGMVFTIEPGIYIPGKGGVRIEDDVLVTEDGC
>gnl|CDD|238526 cd01093, CRIB_PAK_like, PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. This subgroup of CRIB/PBD-domains is found N-terminal of Serine/Threonine kinase domains in PAK and PAK-like proteins
PEISSPTNFKHRVHVGFDPQTGEFTGLPEEWQRLLKSSGITKEEQK
>gnl|CDD|238527 cd01094, Alkanesulfonate_monoxygenase, Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the conversion of alkanesulfonates to the corresponding aldehyde and sulfite. Alkanesulfonate monoxygenase (SsuD) has an absolute requirement for reduced flavin mononucleotide (FMNH2), which is provided by the NADPH-dependent FMN oxidoreductase (SsuE)
LEFGWFIPNVSGGWSLSTPPRGRPWDFEYNRQIAQAAEELGFDGALSPTGSSGPDGWTVAAALAAATERL
KFLVAIRPGLIAPTVAARQAATLDHISGGRLGLNVVTGGDPAELRMDGDFLDHDERYARADEFLEVLRRL
WTSDEPFDFEGKFYRFKNAFLRPKPPQQPHPPIYFGGSSEAAIEFAARHADVYFTWGEPPAQVAEAIARV
RAAAAAAGRDVRFGIRLHVIVRDTEEEAWAYADR
>gnl|CDD|238528 cd01095, Nitrilotriacetate_monoxgenase, nitrilotriacetate monoxygenase oxidizes nitrilotriacetate utilizing reduced flavin mononucleotide (FMNH2) and oxygen. The FMNH2 is provided by an NADH:flavin mononucleotide (FMN) oxidorductase that uses NADH to reduce FMN to FMNH2
LHLGAFLHGAGHHAAAWRHPAPPDASIDFDHYVRLARTAERAKFDAVFLADGLAIRALSRPHPVARLEPL
TLLAALAAVTERIGLVATASTTYNEPYHLARRFASLDHISGGRAGWNVVTSANPGEARNFGRDEHPEHDE
RYARAEEFVEVVKGLWDSWEDDALVRDKASGRFADPAKVHPLDHVGDHFGVRGPLNGPRSPQGRPVIVQA
GSSEAGREFAARHAEAVFTAQQTLEEAQAFYADVKARAAAAGRLDPPPPDLPDLGSRLSASRLLLADLLA
RGGLHRREVGTAREVADRLERAAGGGTVVGPEQIADELEEWFEAGAADGFNIMPPYLPGGLDDFVDLVVP
ELQRRGLF
>gnl|CDD|238529 cd01096, Alkanal_monooxygenase, Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with reduced flavin mononucleotide (FMNH2) and reacts with an aldehyde to yield the carboxylic acid, oxidized flavin (FMN) and a blue-green light. Bacterial luciferases are heterodimers made of alpha and beta subunits which are homologous. The single activer center is on the alpha subunit. The alpha subunit has a stretch of 30 amino acid residues that is not present in the beta subunit. The beta subunit does not contain the active site and is required for the formation of the fully active heterodimer. The beta subunit does not contribute anything directly to the active site. Its role is probably to stabilize the high quantum yield conformation of the alpha subunit through interactionbs across the subunit interface
MKFGLFFLNFQPPGESSEEVLDRMVDTGVLVDKLNFDTALVLEHHFSENGIVGAPLTAAAFLLGLTERLN
VGSLNQVITTHHPVRIAEEALLLDQMSKGRFILGFSDCLYDKDMRFFGRPMESQRQLFEACYEIINDALT
TGYCHPDNDFYNFPKISVNPHAYSKGGPPQYVTAESAETVEWAAKKGLPLVLSWIDSLAEKKAYAELYLE
VAKEGGDDISNIDHQLTLIVNVNEDGEKAQDECREFLENYYDEYYPATNTERKIDESIEENAVGTPEECI
EIIQLAIEATGIKNILLSFESMGSEDEIIASINMF
>gnl|CDD|238530 cd01097, Tetrahydromethanopterin_reductase, N5,N10-methylenetetrahydromethanopterin reductase (Mer) catalyzes the reduction of N5,N10-methylenetetrahydromethanopterin with reduced coenzyme F420 to N5-methyltetrahydromethanopterin and oxidized coenzyme F420
MRFGIFLSPEQPGPRELVELARAAEEAGFDSVWVSLDALSGGRFILGLGAGGPEVEEGWGGPWFKPPARR
REELEAIRRLRALRRGDPVGEDGRFLGTRSAALPPPPRGEIPIYIGALGPKMLELAGEIADGWLPVAAPP
ELYEAALPAVREGAAAAGRVVGDPDDVAEALRRYREAGVTEVVLDVVGGAIDGDVERLIDLL
>gnl|CDD|238531 cd01098, PAN_AP_plant, Plant PAN/APPLE-like domain; present in plant S-receptor protein kinases and secreted glycoproteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions. S-receptor protein kinases and S-locus glycoproteins are involved in sporophytic self-incompatibility response in Brassica, one of probably many molecular mechanisms, by which hermaphrodite flowering plants avoid self-fertilization
TPLNCGGDGSTDGFLKLPDVKLPDNASAITAISLEECREACLSNCSCTAYAYNNGSGGCLLWNGLLNNLR
SLSSGGGTLYLRLA
>gnl|CDD|238532 cd01099, PAN_AP_HGF, Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen/hepatocyte growth factor proteins, and various proteins found in Bilateria, such as leech anti-platelet proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions
LNDFKFVLVLNKILVSEVKTEITVASLEECLRKCLEETEFTCRSFNYNYKSKECILSDEDRMSSGVKLLY
DSNVDYYENK
>gnl|CDD|238533 cd01100, APPLE_Factor_XI_like, Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, microneme antigen proteins, and a few prokaryotic proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions
CPSSCFRQGSNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTKSKKCFLKSSEGTLTKSTGAVSG
PRL
>gnl|CDD|238534 cd01102, Link_Domain, The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It is found in the CD44 receptor and in human TSG-6. TSG-6 is the protein product of the tumor necrosis factor-stimulated gene-6. TSG-6 has a strong anti-inflammatory effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. This group also contains the link domains of the chondroitin sulfate proteoglycan core proteins (CSPG) including aggrecan, versican, neurocan, and brevican and the link domains of the vertebrate HAPLN (HA and proteoglycan binding link) protein family. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates in which other CSPGs substitute for aggregan might contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN gene family are physically linked adjacent to CSPG genes. TSG-6 contains a single link module which supports high affinity binding with HA. The functional HA-binding domain of CD44 is an extended domain comprised of a link module flanked with N-and C- extensions. These extensions are essential for folding and functional activity. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of the CSPG aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) which contains link modules 3 and 4 which lack HA-binding activity. HAPLNs contain two contiguous link modules
VVFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGG
RNPGVRSYGNPAPSGRYDAYCF
>gnl|CDD|133379 cd01104, HTH_MlrA-CarA, Helix-Turn-Helix DNA binding domain of the transcription regulators MlrA and CarA. Helix-turn-helix (HTH) transcription regulator MlrA (merR-like regulator A), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. Its close homolog, CarA from Myxococcus xanthus, is involved in activation of the carotenoid biosynthesis genes by light. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Many MlrA- and CarA-like proteins in this group appear to lack the long dimerization helix seen in the N-terminal domains of typical MerR-like proteins
YTIGAVARLTGVSPDTLRAWERRYGLPAPQRTDGGHRLYSEADVARLRLIRRLTSEGVRISQAAALAL
>gnl|CDD|133380 cd01105, HTH_GlnR-like, Helix-Turn-Helix DNA binding domain of GlnR-like transcription regulators. Helix-turn-helix (HTH) transcription regulator GlnR and related proteins, N-terminal domain. The GlnR and TnrA (also known as ScgR) proteins have been shown to regulate expression of glutamine synthetase as well as several genes involved in nitrogen metabolism. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules
VIGIGEVSKLTGVSPRQLRYWEEKGLIKSIRSDGGGQRKYSLADVDRLLVIKELLDEGFTLAAAVEKLRR
RRVQAEVRRRLMKDGLQG
>gnl|CDD|133381 cd01106, HTH_TipAL-Mta, Helix-Turn-Helix DNA binding domain of the transcription regulators TipAL, Mta, and SkgA. Helix-turn-helix (HTH) TipAL, Mta, and SkgA transcription regulators, and related proteins, N-terminal domain. TipAL regulates resistance to and activation by numerous cyclic thiopeptide antibiotics, such as thiostrepton. Mta is a global transcriptional regulator; the N-terminal DNA-binding domain of Mta interacts directly with the promoters of mta, bmr, blt, and ydfK, and induces transcription of these multidrug-efflux transport genes. SkgA has been shown to control stationary-phase expression of catalase-peroxidase in Caulobacter crescentus. These proteins are comprised of distinct domains that harbor an N-terminal active (DNA-binding) site and a regulatory (effector-binding) site. The conserved N-terminal domain of these transcription regulators contains winged HTH motifs that mediate DNA binding. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Unique to this family, is a TipAL-like, lineage specific Bacilli subgroup, which has five conserved cysteines in the C-terminus of the protein
YTVGEVAKLTGVSVRTLHYYDEIGLLKPSRRTENGYRLYTEEDLERLQQILFLKELGFSLKEIKELLKDP
SEDLLEALREQKELLEEKKERLDKLIKTIDRTL
>gnl|CDD|133382 cd01107, HTH_BmrR, Helix-Turn-Helix DNA binding domain of the BmrR transcription regulator. Helix-turn-helix (HTH) multidrug-efflux transporter transcription regulator, BmrR and YdfL of Bacillus subtilis, and related proteins; N-terminal domain. Bmr is a membrane protein which causes the efflux of a variety of toxic substances and antibiotics. BmrR is comprised of two distinct domains that harbor a regulatory (effector-binding) site and an active (DNA-binding) site. The conserved N-terminal domain contains a winged HTH motif that mediates DNA binding, while the C-terminal domain binds coactivating, toxic compounds. BmrR shares the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements
FTIGEFAKLSNLSIKALRYYDKIGLLKPAYVDPDTGYRYYSAEQLERLNRIKYLRDLGFPLEEIKEILDA
DNDDELRKLLREKLAELEAEIEELQRILRLLEDRLKQI
>gnl|CDD|133383 cd01108, HTH_CueR, Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators. Helix-turn-helix (HTH) transcription regulators CueR and ActP, copper efflux regulators. In Bacillus subtilis, copper induced CueR regulates the copZA operon, preventing copper toxicity. In Rhizobium leguminosarum, ActP controls copper homeostasis; it detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations. These proteins are comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain winged HTH motifs that mediate DNA binding, while the C-terminal domains have two conserved cysteines that define a monovalent copper ion binding site. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements
MNIGEAAKLTGLSAKMIRYYEEIGLIPPPSRSDNGYRVYNQRDIEELRFIRRARDLGFSLEEIRELLALW
RDPSRASADVKALALEHIAELERKIAELQAMRRTLQQLADSCHGDDRPDCPILEGLA
>gnl|CDD|133384 cd01109, HTH_YyaN, Helix-Turn-Helix DNA binding domain of the MerR-like transcription regulators YyaN and YraB. Putative helix-turn-helix (HTH) MerR-like transcription regulators of Bacillus subtilis, YyaN and YraB, and related proteins; N-terminal domain. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
YTIKEVAEKTGLSADTLRYYEKEGLLPPVKRDENGIRDFTEEDLEWLEFIKCLRNTGMSIKDIKEYAELR
REGDSTIPERLELLEEHREELEEQIAELQETLAYLDYKIDYYE
>gnl|CDD|133385 cd01110, HTH_SoxR, Helix-Turn-Helix DNA binding domain of the SoxR transcription regulator. Helix-turn-helix (HTH) transcriptional regulator SoxR. The global regulator, SoxR, up-regulates gene expression of another transcription activator, SoxS, which directly stimulates the oxidative stress regulon genes in E. coli. The soxRS response renders the bacterial cell resistant to superoxide-generating agents, macrophage-generated nitric oxide, organic solvents, and antibiotics. The SoxR proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the unusually long spacer between the -35 and -10 promoter elements. They also harbor a regulatory C-terminal domain containing an iron-sulfur center
ELSVGEVAKRSGVAVSALHFYEQKGLIASWRNAGNQRRYPRDVLRRIAFIKVAQRLGLSLAEIAEALATL
PEDRTPTKADWERLSRAWRDRLDERIAELQQLRDQLDGCIGCGCLSLKKCPLYNPEDRLGAQGPGARLL
>gnl|CDD|133386 cd01111, HTH_MerD, Helix-Turn-Helix DNA binding domain of the MerD transcription regulator. Helix-turn-helix (HTH) transcription regulator MerD. The putative secondary regulator of mercury resistance (mer) operons, MerD, has been shown to down-regulate the expression of this operon in gram-negative bacteria. It binds to the same operator DNA as MerR that activates transcription of the operon in the presence of mercury ions. The MerD protein shares the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily, which promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are conserved and contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules such as metal ions, drugs, and organic substrates
YSISQLALDAGVSVHIVRDYLLRGLLHPVARTEGGYGLFDDCALQRLRFVRAAFEAGIGLDELARLCRAL
DAGDGKQPEACLAQLRQKIEVRRAALNALTTQLAEMA
>gnl|CDD|238535 cd01115, SLC13_permease, Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been shown to translocate Krebs cycle intermediates such as succinate, citrate, and alpha-ketoglutarate across plasma membranes rabbit, human, and rat kidney. It is related to renal and intestinal Na+/sulfate cotransporters and a few putative bacterial permeases. The SLC13-type proteins belong to the ArsB/NhaD superfamily of permeases that translocate sodium and various anions across biological membranes in all three kingdoms of life. A typical ArsB/NhaD permease is composed of 8-13 transmembrane helices
LAILVFAAVLFVTEALPLDVTALLVPVLLVLLGVVPPKEAFSGFSDPAVILFLAGFILGAALTRTGLAKR
IATKLLKRAGKGERRLLLLLMLVTAFLSAFMSNTATVAIMLPVALGLAAKLDISPSRLLMPLAFAASIGG
MLTLIGTPPNLVASGYLESLGGQGFSFFEFTPIGLPLLIIGLLYLWFIFRLAVLIITIVLLAALAAITGL
LPVSVAIAIGAIVLVFGGVLLTKEDYKSIDWGIIFLFAGGIPLGKALESSGAAALIAEALISLLGGLPPF
AILLLLCLLTLVLTNFISNTATAVLLAPIALSIALSLGLPPEALLLAVAIGASCAFMLPVGTPPNAIVLG
PGGYKFSDFAKVGLPLSILSLVVSVTMIPLIW
>gnl|CDD|238536 cd01116, P_permease, Permease P (pink-eyed dilution). Mutations in the human melanosomal P gene were responsible for classic phenotype of oculocutaneous albinism type 2 (OCA2). Although the precise function of the P protein is unknown, it was predicted to regulate the intraorganelle pH, together with the ATP-driven proton pump. It shows significant sequence similarity to the Na+/H+ antiporter NhaD from Vibrio parahaemolyticus. Both proteins belong to ArsB/NhaD superfamily of permeases that translocate sodium, arsenate, sulfate, and organic anions across biological membranes in all three kingdoms of life. A typical ArsB/NhaD permease contains 8-13 transmembrane domains
FIITYALIIFEKVHRTVAALAGALWLVILGLATLSPDLETIVSWVDWETLALLLGMMIIVSILSETGVFE
YLAIWAVKISKGRPWRLLLLLGLLTAFLSAFLDNVTTVLLMVPVTIRLCEVLGLNPVPVLISEVIAANIG
GAATLIGDPPNIMIGSAAGLTFNDFLLHMLPSVVLALVVTFILLYFLYRNILKAREEDVLALAELEPKYP
IKDKVLLLKSLTILTLVIIGFVLHSPLGVSLGWIALLGALLLLLLADKLDFEDVLSRVEWDTLLFFAGLF
VLVGGLEELGIIEWIAELLVGVILGRIAVAVILILWISALLSAFIDNIPVTATMIPIVKDLASQLGIPLL
PLWWALALGACLGGNGTLIGASANVVAAGIAEQHGYKISFWEFLKVGFPIMLVSLILATVYLL
>gnl|CDD|238537 cd01117, YbiR_permease, Putative anion permease YbiR. Based on sequence similarity, YbiR proteins are predicted to function as anion translocating permeases in eubacteria, archaea and plants. They belong to ArsB/NhaD superfamily of permeases that have been shown to translocate sodium, sulfate, arsenite and organic anions. A typical ArsB/NhaD permease is composed of 8-13 transmembrane domains
LALGRVPGLRLDRWAIALLGAALMLLFGVISLEDAPAAIDLDTIILLFGLMVVSAALELSGFFDALGSRI
LVKAGSPRRLLFLLVLLSGILSALLTNDTACLVFTPIVLELARVAGLPPIPLLLALATAANIGSAATPIG
NPQNLLIASESGISFPFFLAAMAPLALLGLLLLLILLLVLFPGELKGLPLDKATKEEGVGARKLAVKLLV
LILLLLVAFLALLGVIPLWTAALVAAVLLLLTRLKPRRVLKKVDWGLLLFFAGLFILVGGFAQGLPLEGL
SRLLPLLDSVLSLFLVSIGLSQLISNVPAVLLLLPFLPSADEKDWLLLAAGSTIAGNLTLLGSAANLIVA
EAAERRGVRLSFGEFLKYGVPLTLLTAAIGILWL
>gnl|CDD|238538 cd01118, ArsB_permease, Anion permease ArsB. These permeases have been shown to export arsenate and antimonite in eubacteria and archaea. A typical ArsB permease contains 8-13 transmembrane helices and can function either independently as a chemiosmotic transporter or as a channel-forming subunit of an ATP-driven anion pump (ArsAB). The ArsAB complex is similar in many ways to ATP-binding cassette transporters, which have two groups of six transmembrane-spanning helical segments and two nucleotide-binding domains. The ArsB proteins belong to the ArsB/NhaD superfamily of permeases that translocate sodium, arsenate, sulfate, and organic anions across biological membranes in all three kingdoms of life
LAIAIFVLTLVLVIWRPFGLPEAVWAVLGAVIALILGLVSPHDALEVWGIVWDVTLTLIGVILLSLLLDE
EGFFEWVAALAARWARGSGRKLFTLIVLLGAAVTAFFANDGTALILTPIVIALLRALGAKKNRTLPFLYA
CAFIADAASLPLPISNLVNIVTAGYFGIGFTEYAALMFLPSIVSILATYVVLYLFFRRALPKRLETASVK
KPSLAIKDPLLFGLAWTLLVLLVVSAFGVDILLIPPSFIAGVLALIFLLLARRGGAINPLKVLKEAPWGV
LLFSLGLYVVVFGLKNAGLTAILADLLNWLVSQGLLAAILGVGLLAAFLSNVMNNLPAVLIGALALAAGH
APEALVYANLIGVDLGPKLTPIGSLATLLWLHVLRRKGIRVSWGYYLKVGLIVTPPVLVVTLAALI
>gnl|CDD|238539 cd01119, Chemokine_CC_DCCL, Chemokine_CC_DCCL: subgroup of the Chemokine_CC subgroup based on the presence of a DCCL motif involving the two N-terminal cysteine residues; includes a number of small inducible cytokines capable of reversibly inhibiting normal hematopoietic progenitor proliferation by blocking progression through the cell cycle; DCCL subgroup contains Exodus-1 (also known as CCL20, MIP-3alpha, LARC, ST38 (mouse)), Exodus-2 (also known as CCL21, SLC, 6-Ckine, TCA4, CKbeta9), and Exodus-3 (also known as CCL-19, ELC, MIP-3beta, CKbeta11). Exodus-3 was shown to inhibit the growth of human breast cancer cells in vivo in a mouse model; Exodus-1, -2, and -3 were all shown to significantly inhibit chronic myelogenous leukemia progenitor cell proliferation; Exodus-2 and -3 show potent immunotherapeutic activity toward solid tumors; chemotatic for T cells, B cells, dendritic cells, macrophage progenitor cells, and NK cells; exist as monomers and dimers, but are believed to be functional as monomers; found only in vertebrates. See CDs: Chemokine_CC (cd00272) for the entire CC subgroup, Chemokine (cd00169) for the general alignment of chemokines, or Chemokine_CXC (cd00273), Chemokine_C (cd00271), and Chemokine_CX3C (cd00274) for the additional chemokine subgroups
EDCCLSYTQHPIPWRVLRGYTYQEISESCDIPAIIFHTRRGRKVCADPKQDWVKRAIQLLS
>gnl|CDD|410865 cd01120, RecA-like_superfamily, RecA-like_NTPases. RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTILEAIEDLIEEKKLDIIIIDSLSSLARASQGDR
SSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR
>gnl|CDD|410866 cd01121, RadA_SMS_N, bacterial RadA DNA repair protein. Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules
YVCQECGYESPKWLGRCPSCGEWNTFVEEVVSASSSASRRASASPSPSKPLPLSDVEAEEEERISTGIGE
LDRVLGGGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQIKLRAERLGLGSDNLY
LLAETNLEAILAEIEELKPSLVVIDSIQTVYSPELTSSPGSVSQVRECAAELLRLAKETGIPVFLVGHVT
KDGAIAGPKVLEHMVDTVLYFEGDRGSSYRILRSVKNRFGPTNEIGVFEMTENGLREV
>gnl|CDD|410867 cd01122, Twinkle_C, C-terminal domain of Twinkle. Twinkle (T7 gp4-like protein with intramitochondrial nucleoid localization, also known as C10orf2, PEO1, SCA8, ATXN8, IOSCA, PEOA3 or SANDO) is a homohexameric DNA helicases which unwinds short stretches of double-stranded DNA in the 5' to 3' direction and, along with mitochondrial single-stranded DNA binding protein and mtDNA polymerase gamma, is thought to play a key role in mtDNA replication. Mutations in the human gene cause infantile onset spinocerebellar ataxia (IOSCA) and progressive external ophthalmoplegia (PEO) and are also associated with several mitochondrial depletion syndromes. This group also contains viral GP4-like and related bacterial helicases
SITTFDDLRELVYEELLNSEQVAGVQWKRFPSLNKLLKGHRRGELTIFTGPTGSGKTTFLSEYSLDLCMQ
GVNTLWGSFEIKNVRLAKTMLTQFAGKNLEDNLREFDEWADKFELLPMYFMKFHGSTDIDEVLDAMEHAV
YVYDIQHIVIDNLQFMMGTQASGSDRFELQDLIIGKFRRFATNNNVHITLVIHPRKEDDDNELTTSSIFG
SAKATQEADNVLILQDKRLISGEGKKFLQIKKNRFDGDLGVIPLEFNKNSLTYSET
>gnl|CDD|410868 cd01123, Rad51_DMC1_archRadA, recombinase Rad51, DMC1, and archaeal RadA. This group of recombinases includes the eukaryotic proteins RAD51, RAD55/57 and the meiosis-specific protein DMC1, and the archaeal protein RadA. They are closely related to the bacterial RecA group. Rad51 proteins catalyze a similar recombination reaction as RecA, using ATP-dependent DNA binding activity and a DNA-dependent ATPase. However, this reaction is less efficient and requires accessory proteins such as RAD55/57
ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLCHTLAVTCQLPIDRGGGEGKAIYIDTEGTFRPERL
RAIAQRFGLDPDDVLDNVAYARAFNSDHQTQLLDQAAAMMVESRFKLLIVDSATALYRTDYSGRGELSAR
QMHLAKFLRMLQRLADEFGVAVVVTNQVVAQVDGAMMFAADPKKPIGGNILAHASTTRLYLRKGRGETRI
CKIYDSPCLPEAEAVFAITADGVG
>gnl|CDD|410869 cd01124, KaiC-like, Circadian Clock Protein KaiC. KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation
VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLRNAKSFG
WDFDEMEDEGKLIIVDAPPTEAGRFSLDELLSRILSIIKSFKAKRVVIDSLSGLRRAKEDQMRARRIVIA
LLNELRAAGVTTIFTSEMRSFLSSESAGGGDVSFIVDGVILLRYVEIEGELRRTIRVLKMRGTGHDTGTH
PFEITDKGIVVF
>gnl|CDD|410870 cd01125, RepA_RSF1010_like, Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins. This family includes the homo-hexameric replicative helicase RepA encoded by plasmid RSF1010. RSF1010 is found in most Gram-negative bacteria and some Gram-positive bacteria . The RepA protein of Plasmid RSF1010 is a 5'-3' DNA helicase which can utilize ATP, dATP, GTP and dGTP (and CTP and dCTP to a lesser extent)
GTLGMLVGPPGSGKSFLALDLAVAVATGRDWLGERRVKQGRVVYLAAEDPRDGLRRRLKAIGAHLGDEDA
ALAENLVIENLRGKPVSIDAEAPELERIIEELEGVRLIIIDTLARVLHGGDENDAADMGAFVAGLDRIAR
ETGAAVLLVHHTGKDAAGDSQQAARGSSALRGAADAEINLSKMDATEAEKVGLDKDLRRRFVRLDVTKAN
YAAPGAVRWFKREEGAIALGEPKGVLLP
>gnl|CDD|410871 cd01127, TrwB_TraG_TraD_VirD4, TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins. The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases
NTLVLGTTGSGKTTSIVIPLLDQAARGGSVIITDPKGELFLVIPDRDDSFAALRALFFNQLFRALTELAS
LSPGRLPRRVWFILDEFANLGRIPNLPNLLATGRKRGISVVLILQSLAQLEAVYGKDGAQTILGNCNTKL
YLGT
>gnl|CDD|410872 cd01128, rho_factor_C, C-terminal ATP binding domain of transcription termination factor rho. Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain
ELSTRVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLLIDERPEEVTDMRRSVKG
EVVASTFDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSGGVDANALH
KPKRFFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGT
RKEELLLTPEELQKIWLLRRILSPMDPIEAMEFLLKKLK
>gnl|CDD|410873 cd01129, PulE-GspE-like, PulE-GspE family. PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB
ARLRRLIKRPHGLILVTGPTGSGKTTTLYAMLRELNGPERNIITIEDPVEYQIPGINQSQVNEKIGLTFA
DALRAILRQDPDIIMVGEIRDAETAEIAIRAALTGHLVLSTLHTNDALGAITRLLDMGIEPFLLASALRG
VIAQRLVGRTAIAEVLVLD
>gnl|CDD|410874 cd01130, VirB11-like_ATPase, Type IV secretory pathway component VirB11-like. Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase
MAAFLRLAVRARKNILISGGTGSGKTTLLNALLSFIPPDERIVTIEDTRELQLPHPNVVHLLTRPGGGEK
GEVTMADLLKAALRMRPDRIIVGEVRGGEAYDMLQAMNTGHPGSITTIHANSAEDAIDRLATLVLEAGVN
LDEEALRRLIASAIDVIVHVKRLGDGVRRVTEIYEVP
>gnl|CDD|410875 cd01131, PilT, Pilus retraction ATPase PilT. Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility
IPTFEELGLPPVLKDLALKPRGLVLVTGPTGSGKSTTLAAMIDYINETRSKHIITIEDPIEFVHKHKKSL
INQREVGRDTESFAAALRAALREDPDVILVGEMRDLETIELALTAAETGHLVFSTLHTNSAAQTIDRIID
VFPPEQQEQVRIQLASSLRGVISQRLLPKKDGGGRVAAFEILINTPAIRNLIREGKTHQIPSLIQTGARD
GMQTMDQSLYELY
>gnl|CDD|410876 cd01132, F1-ATPase_alpha_CD, F1 ATP synthase alpha subunit, central domain. The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain
IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQ
RELIIGDRQTGKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAP
LQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAK
LSDELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG
>gnl|CDD|410877 cd01133, F1-ATPase_beta_CD, F1 ATP synthase beta subunit, central domain. The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain
SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKI
GLFGGAGVGKTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGLSKVALVYGQMN
EPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQ
ERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP
>gnl|CDD|410878 cd01134, V_A-ATPase_A, V/A-type ATP synthase catalytic subunit A. V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria
PLSVELGPGLLGSIFDGIQRPLEVIAETGSIFIPRGVNVQRWPVRQPRPVKEKLPPNVPLLTGQRVLDTL
FPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPITGESLMERT
VLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLG
ARLAEFYERAGRVRCLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSIN
WLISYSKY
>gnl|CDD|410879 cd01135, V_A-ATPase_B, V/A-type ATP synthase subunit B. V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit
VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQ
KLPIFSGSGLPHNELAAQIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLAN
DPTIERIITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIY
ERAGRVEGRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSG
IG
>gnl|CDD|410880 cd01136, ATPase_flagellum-secretory_path_III, Flagellum-specific ATPase/type III secretory pathway virulence-related protein. Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway
SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRI
GIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVR
AAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKG
SITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV
>gnl|CDD|238557 cd01137, PsaA, Metal binding protein PsaA. These proteins have been shown to function as initial receptors in ABC transport of Mn2+ and as surface adhesins in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence)
LAACASLGSSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLI
LYNGLNLEPWLERLVKNAGKDVPVVAVSEGIDPIPLEEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEA
DPANAETYQKNAAAYKAKLKALDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEG
TPKQVATLIEQVKKEKVPAVFVESTVNDRLMKQVAKETGAKIGGQLYTDSLSEKGGPADTYLDMMEHNLD
TIVEGLG
>gnl|CDD|238558 cd01138, FeuA, Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains
GEVEIPAKPKRIVALSGETEGLALLGIKPVGAASIGGKNPYYKKKTLAKVVGIVDEPNLEKVLELKPDLI
IVSSKQEENYEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGN
DKSVAVLRGRKQIYVFGEDGRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFT
GPEAKADFESLPIWKNLPAVKNNHVYIVDAWVFYFADG
>gnl|CDD|238559 cd01139, TroA_f, Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains
ITVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFPEIAD
IPLIGSTYNGDFSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRL
LGKALGREERAEEFIEFYQERIDRIRDRLAKINEPKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGD
NIADGLIPGTSGELNAEYVIAANPEIIIATGGNWAKDPSGVSLGPDGTTADAKESLLRALLKRPGWSSLQ
AVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFKDLDPEATLQEFHRQFLPVDYSGTFW
>gnl|CDD|238560 cd01140, FatB, Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains
HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSSTLPEYLKKYKDDKYANVGTLFEPDLEAIAA
LKPDLIIIGGRLAEKYDELKKIAPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEA
KSAAKGKKKALVVLVNGGKLSAFGPGSRFGWLHDLLGFEPADENIKASSHGQPVSFEYILEANPDWLFVI
DRGAAIGAEGSSAKEVLDNDLVKNTTAWKNGKVIYLDPDLWYLSGGGLESLKQMIDDLKK
>gnl|CDD|238561 cd01141, TroA_d, Periplasmic binding protein TroA_d. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains
AKTIKVPPKRIVVLSPTHVDLLLALDKADKIVGVSASAYDLNTPAVKERIDIQVGPTGSLNVELIVALKP
DLVILYGGFQAQTILDKLEQLGIPVLYVNEYPSPLGRAEWIKFAAAFYGVGKEDKADEAFAQIAGRYRDL
AKKVSNLNKPTVAIGKPVKGLWYMPGGNSYVAKMLRDAGGRYLSAE
>gnl|CDD|238562 cd01142, TroA_e, Periplasmic binding protein TroA_e. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains
PAATAATRTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQQEPWLYRLAPSLENV
ATGGTGNDVNIEELLALKPDVVIVWSTDGKEAGKAVLRLLNALSLRDAELEEVKLTIALLGELLGRQEKA
EALVAYFDDNLAYVAARTKKLPDSERPRVYYAGPDPLTTDGTGSITNSWIDLAGGINVASEATKKGSGEV
SLEQLLKWNPDVIIVGNADTKAAILADPRWQNLRAVKNGRVYVNPEGAFWWDRPSAEEALLGLWLAKTLY
PERFTDDDM
>gnl|CDD|238563 cd01143, YvrC, Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains
KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSS
LAELLEKLKDAGIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKV
YIEVSLGGPYTAGKNTFINELIRLAGAKNIAADSGGWPQVSPEEILKANPDVIIL
>gnl|CDD|238564 cd01144, BtuF, Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence)
MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVC
AVVDQLRAAGIPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQ
EWIDPLMTAGGDWVPELIALAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCGFGFTPAILRKEPAW
QALPAVRNGRVYAVDGNWYFRPSPRLVDGLEQLAA
>gnl|CDD|238565 cd01145, TroA_c, Periplasmic binding protein TroA_c. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains
AALNVVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGFEPKLA
ELSSNSKVQPGIKILIEDSDTVGMVDRAMGDYHGKGNPHVWLDPNNAPALAKALADALIELDPSEQEEYK
ENLRVFLAKLNKLLREWERQFEGLKGIQVVAYHPSYQYLADWLGIEVVASLEPLPELPPTSSH
>gnl|CDD|238566 cd01146, FhuD, Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains
AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLIL
GSASRHDEIYDQLSQIAPTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKG
PKPVSVVRFSDAGSIRLYGPNSFAGSVLEDLGLQNPWAQETTNDSGFATISLERLAKADADVLFVFTYED
EELAQALQANPLWQNLPAVKNGRVYVVDDVWWFFGGGLSAARLLLD
>gnl|CDD|238567 cd01147, HemV-2, Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence)
VPKPVERVVAAGPGALRLLYALAAPDKIVGVDDAEKSDEGRPYFLASPELKDLPVIGRGGRGNTPNYEKI
AALKPDVVIDVGSDDPTSIADDLQKKTGIPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESI
LADVEERTKDIPDEEKPTVYFGRIGTKGAAGLESGLAGSIEVFELAGGINVADGLGGGGLKEVSPEQILL
WNPDVIFLDTGSFYLSLEGYAKNRPFWQSLKAVKNGRVYLLPALPFNWYDTP
>gnl|CDD|238568 cd01148, TroA_a, Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains
YPLTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDLPELKAKYDKVPELAKKYP
SKETVLAARPDLVFGGWSYGFDKGGLGTPDSLAELGIKTYILPESCGQRRGEATLDDVYNDIRNLGKIFD
VEDRADKLVADLKARLAEISAKVKGDGKKVAVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDES
WTTVSWETVIARNPDVIVIIDYGDQNAAEQKIKFLKENPALKNVPAVKNNRFIVLPLAEATPGIRNVDAI
EKLA
>gnl|CDD|238569 cd01149, HutB, Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains
PERIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGP
PEALDQLRAAGVPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRV
LFLLSHGGGAAMAAGRNTAADAIIALAGAVNAAAGFRGYKPLSAEALIAAQPDVILVMSRGLDAVGGVDG
LLKLPGLAQTPAGRNKRILAMDDLL
>gnl|CDD|173839 cd01150, AXO, Peroxisomal acyl-CoA oxidase. Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment
PDLDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRELPSKHLSREELYEELKRKAKTDV
ERMGELMADDPEKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQ
TELGHGSNLQGLETTATYDPLTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPGKNHGLHAFIVP
IRDPKTHQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGA
MLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPSDPEVQILDYQLQQYRLFPQLAAAYAFHF
AAKSLVEMYHEIIKELLQGNSELLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDD
NDPFCTYEGDNTVLLQQTANYLLKKYAQAFSLADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNN
SQVHLRCAAKAHTEYTVLQRFHESVEEIVDPSVRAVLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAV
REALLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLFEEARK
>gnl|CDD|173840 cd01151, GCD, Glutaryl-CoA dehydrogenase. Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans
FNWEDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAG
LSSVAYGLIAREVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSD
PGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWARNDETGKIRGFILERGMKGLSAPKIQGKFSLRA
SITGEIVMDNVFVPEENLLPGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAA
FQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEY
HIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF
>gnl|CDD|173841 cd01152, ACAD_fadE6_17_26, Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26. Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position
PSEEAFRAEVRAWLAAHLPPELREESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLI
FREEMAAAGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAV
RDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPKHRGISILLVDMDSPGVTVRPIRSINGGEFFNEVF
LDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLAR
LEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTAALLRDPAPGAELAGRW
EADYLRSRATTIYGGTSEIQRNIIAERLLG
>gnl|CDD|173842 cd01153, ACAD_fadE5, Putative acyl-CoA dehydrogenases similar to fadE5. Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position
VLEEVARLAENVLAPLNADGDREGPVFDDGRVVVPPPFKEALDAFAEAGWMALGVPEEYGGQGLPITVYS
ALAEIFSRGDAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAV
YQADGSWRINGVKRFISAGEHDMSENIVHLVLARSEGAPPGVKGLSLFLVPKFLDDGERNGVTVARIEEK
MGLHGSPTCELVFDNAKGELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDL
IKAAPAVTIIHHPDVRRSLMTQKAYAEGSRALDLYTATVQDLAERKATEGEDRKALSALADLLTPVVKGF
GSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALDLIGRKIV
>gnl|CDD|173843 cd01154, AidB, Proteins involved in DNA damage response, similar to the AidB gene product. AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates
YLDDPVLQQTLRYFGDPEEEPDLSRLGELAGGELYELARLADRNPPVLEMWDRWGRRVDRVWVHPAWHAL
MRRLIEEGVINIEDGPAGEGRRHVHFAAGYLLSDAAAGLLCPLTMTDAAVYALRKYGPEELKQYLPGLLS
DRYKTGLLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLADAALVLARPEGAPAGARGL
SLFLVPRLLEDGTRNGYRIRRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIYYILEMLNISRLDNAVA
ALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAHM
ARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVLVK
>gnl|CDD|173844 cd01155, ACAD_FadE2, Acyl-CoA dehydrogenases similar to fadE2. FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position
RKAQELRARVKAFMEEHVYPAEQEFLEYYAEGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLT
NLEYAYLAEETGRSFFAPEVFNCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSD
ATNIECSIERDGDDYVINGRKWWSSGAGDPRCKIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPL
SVFGYDDAPHGHAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVS
REAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAARKEIAMIKVAAPRMALKIIDRAI
QVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK
>gnl|CDD|173845 cd01156, IVD, Isovaleryl-CoA dehydrogenase. Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates
GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIM
EEISRASGSVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEK
KGDRYVLNGSKMWITNGPDADTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELV
FEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQG
KLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLL
RDAKLYEIGAGTSEIRRMVIGRELFK
>gnl|CDD|173846 cd01157, MCAD, Medium chain acyl-CoA dehydrogenase. MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer
LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITE
ELAYGCTGVQTAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKG
DEYIINGQKMWITNGGKANWYFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGI
TFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVS
FMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKL
MRDAKIYQIYEGTSQIQRLIISREHLGK
>gnl|CDD|173847 cd01158, SCAD_SBCAD, Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases. Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers
EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEEL
AKVDASVAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD
DYVLNGSKMWITNGGEADFYIVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFED
VRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLA
DMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDA
KITEIYEGTSEIQRLVIAKHLLK
>gnl|CDD|173848 cd01159, NcnH, Naphthocyclinone hydroxylase. Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides
ARAEDLAPLIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAA
WVASIVATHSRMLAAFPPEAQEEVWGDGPDTLLAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILV
GAIVEDDDGGPLPRAFVVPRAEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMMAGDGPGGST
PVYRMPLRQVFPLSFAAVSLGAAEGALAEFLELAGKRVRQYGAAVKMAEAPITQLRLAEAAAELDAARAF
LERATRDLWAHALAGGPIDVEERARIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHAAA
QHAALNPETAAEAYGRALLG
>gnl|CDD|173849 cd01160, LCAD, Long chain acyl-CoA dehydrogenase. LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer
EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEEL
ARAGGSGPGLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDH
YVLNGSKTFITNGMLADVVIVVARTGGEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDD
CRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIA
ELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDA
RVQPIYGGTTEIMKELISRQMV
>gnl|CDD|173850 cd01161, VLCAD, Very long chain acyl-CoA dehydrogenase. VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer
SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGL
FGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIA
AFALTEPSSGSDAASIRTTAVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFI
VERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMK
RCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQIEAAISKVFA
SEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHAG
>gnl|CDD|173851 cd01162, IBD, Isobutyryl-CoA dehydrogenase. Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer
LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFE
ALSTGCVSTAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREG
DHYVLNGSKAFISGAGDSDVYVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFED
CRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLA
DMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRD
LRVHQILEGTNEIMRLIIARALLTR
>gnl|CDD|173852 cd01163, DszC, Dibenzothiophene (DBT) desulfurization enzyme C. DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup
ARARPLAARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIA
QALRAHFGFVEALLLAGPEQFRKRWFGRVLNGWIFGNAVSERGSVRPGTFLTATVRDGGGYVLNGKKFYS
TGALFSDWVTVSALDEEGKLVFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAP
DRGTLLTAIYQLVLAAVLAGIARAALDDAVAYVRSRTRPWIHSGAESARDDPYVQQVVGDLAARLHAAEA
LVLQAARALDAAAAAGTALTAEARGEAALAVAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRN
ARTHTLHNPVIYKERAVGDYALNGELP
>gnl|CDD|238570 cd01164, FruK_PfkB_like, 1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis
MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEAL
LKEEGIPDDFVEVAGETRINVKIKEEDGTETEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPP
GVPADFYAELVRLAREKGARVILDTSGEALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLI
ERGAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGS
ATAFSPGTG
>gnl|CDD|349496 cd01165, BTB_POZ, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain superfamily. Proteins in this superfamily are characterized by the presence of a common protein-protein interaction motif of about 100 amino acids, known as the BTB/POZ domain. Members include transcription factors, oncogenic proteins, ion channel proteins, and potassium channel tetramerization domain (KCTD) proteins. They have been identified in poxviruses and many eukaryotes, and have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats, among others. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. In ion channel proteins and KCTD proteins, the BTB/POZ domain is also called the tetramerization (T1) domain
VVLVVEGEKFHVNKELLAQSSEYFRALFRGGFRESGQAEINLRDISPEDFRALLEFLYGGKRDLDASNLL
ELLEAANFL
>gnl|CDD|238571 cd01166, KdgK, 2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources
DVVTIGEVMVDLSPPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRRE
GVDTSHVRVDPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLALSES
AREALLEALEAAKARGVTVSFDLNYRPKLWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAE
RALALALGVKAVVVKLGAEGALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFA
NAAAALVVTRPGDI
>gnl|CDD|238572 cd01167, bac_FRK, Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate
KVVCFGEALIDFIPEGSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVD
TRGIQFDPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDLLSEADILHFGSIALASEPSRSAL
LELLEAAKKAGVLISFDPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLL
FGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLLALDEDELAEALRF
ANAVGALTCTKAGAI
>gnl|CDD|238573 cd01168, adenosine_kinase, Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway
RYDVLGLGNALVDILAQVDDAFLEKLGLKKGDMILADMEEQEELLAKLPVKYIAGGSAANTIRGAAALGG
SAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDW
SLLAKAKYLYLEGYLLTVPPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELLPYVDILFGNEEE
AEALAEAETTDDLEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFL
YGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP
>gnl|CDD|238574 cd01169, HMPP_kinase, 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction
VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVD
AIKIGMLGSAEIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAE
LLTGLEIATEEDMMKAAKALLALGAKAVLIKGGHLPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTL
SSAIAANLAKGLSLEEAVREAKEYVTQAIRNA
>gnl|CDD|238575 cd01170, THZ_kinase, 4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the hydroxylgroup of Thz. A reaction that allows cells to recycle Thz into the thiamine biosynthesis pathway, as an alternative to its synthesis from cysteine, tyrosine and 1-deoxy-D-xylulose-5-phosphate
LEKLREKKPLVHCITNYVVMNFVANVLLAIGASPIMSDAPEEVEELAKIAGALVINIGTLTSEQIEAMLK
AGKAANQLGKPVVLDPVGVGATSFRTEVAKELLAEGQPTVIRGNASEIAALAGLTGLGKGVDSSSSDEED
ALELAKALARKYGAVVVVTGEVDYITDGERVVVVKNGHPLLTKITGTGCLLGAVIAAFLAVGDDPLEAAV
SAVLVYGIAGELAAERAKGPGSFRVALLDELY
>gnl|CDD|238576 cd01171, YXKO-related, B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily
PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIEE
LLELLERADAVVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKRYGPVVLTPHPGEFA
RLLGALVEEIQADRLAAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAA
LLAQGLSPLEAAALAVYLHGLAGDLAAKKKGAGLTAADLVAEIP
>gnl|CDD|238577 cd01172, RfaE_like, RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily
KVLVVGDVILDEYLYGDVERISPEAPVPVVKVEREEIRLGGAANVANNLASLGAKVTLLGVVGDDEAGDL
LRKLLEKEGIDTDGIVDEGRPTTTKTRVIARNQQLLRVDREDDSPLSAEEEQRLIERIAERLPEADVVIL
SDYGKGVLTPRVIEALIAAARELGIPVLVDPKGRDYSKYRGATLLTPNEKEAREALGDEINDDDELEAAG
EKLLELLNLEALLVTLGEEGMTLFERDGEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFL
ANAAAGVVVGKVGTAPVTPKELLL
>gnl|CDD|238578 cd01173, pyridoxal_pyridoxamine_kinase, Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria
RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLL
LEYDAVLTGYLGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADII
TPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTSVELADDDRIEMLGSTATEAWLVQRPKIPFP
AYFNGTGDLFAALLLARLLKGKSLAEALEKALNFVHEVLEATYE
>gnl|CDD|238579 cd01174, ribokinase, Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution
KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLE
NLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIP
LETVLAALRAARRAGVTVILNPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAK
GVKNVIVTLGAKGALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALS
VTRPGAQPSIPT
>gnl|CDD|238580 cd01175, IPT_COE, IPT domain of the COE family (Col/Olf-1/EBF) of non-basic, helix-loop-helix (HLH)-containing transcription factors. COE family proteins are all transcription factors and play an important role in variety of developmental processes. Mouse EBF is involved in the regulation of the early stages of B-cell differentiation, Drosophila collier is a regulator of the head patterning, and a related protein in Xenopus is involved in primary neurogenesis. All COE family members have a well conserved DNA binding domain that contains an atypical Zn finger motif. The function of the IPT domain is unknown
PCIKAISPSEGWTTGGATVIIIGDNFFDGLQVVFGTMLVWSELITPHAIRVQTPPRHIPGVVEVTLSYKS
KQFCKGTPGRFVYTA
>gnl|CDD|238581 cd01176, IPT_RBP-Jkappa, IPT domain of the recombination signal Jkappa binding protein (RBP-Jkappa). RBP-J kappa, was initially considered to be involved in V(D)J recombination because of its DNA binding specificity and structural similarity to site-specific recombinases known as the integrase family. Further studies indicated that RBP-J kappa functions as a repressor of transcription, via destabilization of the general transcription factor IID and recruitment of histone deacetylase complexes
PVTPVPVVSSLELNGGGDVAMLELHGENFTPNLKVWFGDVEAETMYRCEESLLCVVPDISAFREEWRWVR
QPVQVPISLVRNDGIIYPTGLTFTYTP
>gnl|CDD|238582 cd01177, IPT_NFkappaB, IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation
LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYH
DPDITEPVKVKIQLKRPSDGERSESVPFTYVP
>gnl|CDD|238583 cd01178, IPT_NFAT, IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes mainly involved in cell-cell-interaction
LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYH
NKHVAAPVQVQFYVVNGKRKRSQPQTFTYTP
>gnl|CDD|238584 cd01179, IPT_plexin_repeat2, Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains
PSITSLSPSYGPQSGGTRLTITGKHLNAGSSVRVTVGGQPCKILSVSSSQIVCLTPPSASPGEAPVKVLI
DGARRLAPLVFTYTE
>gnl|CDD|238585 cd01180, IPT_plexin_repeat1, First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains
PVITEFFPLSGPLEGGTRLTICGSNLGLRKNDVRHGVRVGGVPCNPEPPEYSSSEKIVCTTGPAGNPVFN
GPVEVTVGHGSFRTESSEGFSFVD
>gnl|CDD|238586 cd01181, IPT_plexin_repeat3, Third repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains
PTITRIEPEWSFLSGGTPITVTGTNLNTVQEPRIRVKYGGVEKTSCKVRNSTLMTCPAPSLALLNRSPEP
GERPVEFGLDGDNVQSLLILNRTSFSYYP
>gnl|CDD|271183 cd01182, INT_RitC_C_like, C-terminal catalytic domain of recombinase RitC, a component of the recombinase trio. Recombinases belonging to the RitA (also known as pAE1 due to its presence in the deletion prone region of plasmid pAE1 of Alcaligenes eutrophus H1), RitB, and RitC families are associated in a complex referred to as a Recombinase in Trio (RIT) element. These RIT elements consist of three adjacent and unidirectional overlapping genes, one from each family (ritABC in order of transcription). All three integrases contain a catalytic motif, suggesting that they are all active enzymes. However, their specific roles are not yet fully understood. All three families belong to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism
LTREEMKALLAAPDRNTSLGRRDHALLLLLYDTGARVQELADLTIRDLRLDDPATVRLHGKGRKERTVPL
WKETVAALKAYLQEFHLTPDPKQLFPLFPNRRGQPLTRDGVAYILNKYVALASNRCPSLPKRITPHTLRH
TKAMHLLQAGVDLTVIRDWLGHESVETTQIYAEADLEMKREALEKA
>gnl|CDD|271184 cd01184, INT_C_like_1, Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain. Tyrosine recombinase (integrase) belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain containing six conserved active site residues. The recombination reaction involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity
FTPEELAKIFSSPLYTGCKKKDPALYWLPLIGLYTGARLNEICQLRVDDIKEEDGIWCIDINDDAEGRRL
KTKASRRLVPIHPRLIELGFLDYVEALRADGKLFLFPEKRDKDGKYSKAASKWFNRLLRKLGIKDDERKS
FHSFRHTFITALKRAGVPEELIAQIVGHSRGGVTHDTYGK
>gnl|CDD|271185 cd01185, INTN1_C_like, Integrase IntN1 of Bacteroides mobilizable transposon NBU1 and similar proteins, C-terminal catalytic domain. IntN1 is a tyrosine recombinase for the integration and excision of Bacteroides mobilizable transposon NBU1 from the host chromosome. IntN1 does not require strict homology between the recombining sites seen with other tyrosine recombinases. This family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA
EELKRLMALELSDTSRLELVRDMFLFSCYTGLRFSDLKNLTWKNIVEASGRTWIRYRRKKTGKPVTVPLL
PVAREILEKYKDDRSEGKLFPVLSNQKINRYLKEIAKIAGIDKHLTFHVARHTFATLLLLKGVDIETISK
LLGHSSIKTTQIYAKIVDSKK
>gnl|CDD|271186 cd01186, INT_tnpA_C_Tn554, Putative Transposase A from transposon Tn554, C-terminal catalytic domain. This family includes putative Transposase A from transposon Tn554. It belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain contains six conserved active site residues. The recombination reaction involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity
VLTPREVQELINACNNLRDKFLLALLYETGLRIGEALGLRIEDIDMADNQIELVPREDNTNEARAKSMRE
RRIPVSQDLIDLYADYLTYIYCEEAEFSITVFVNVKGGNQGKAMNYSDVYDLVRRLKKRTGIDFTPHMFR
HTHATALIRAGWSIEVVARRLGHAHVQTTLNTYGHLSEEDIRRE
>gnl|CDD|271187 cd01187, INT_tnpB_C_Tn554, Putative Transposase B from transposon Tn554, C-terminal catalytic domain. This family includes putative Transposase B from transposon Tn554. It belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain containing six conserved active site residues. The recombination reaction involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity
WVAPNLAALDLLPQPIPVVQAAVFTGARASELATLKFGCLHAQTSDDGTFLYWLKWENKGGKQLDIPISK
KVAELIKTINWTLNELSELKNISDDHGERFRFHTHRFRHTVATRLANSGMGILVLQQLLGHSSPEMTLRY
AL
>gnl|CDD|271188 cd01188, INT_RitA_C_like, C-terminal catalytic domain of recombinase RitA, a component of the recombinase trio. Recombinases RitA (also known as pAE1), RitB, and RitC are encoded by three adjacent and overlapping genes. Collectively they are known as the Recombinase in Trio (RIT). This RitA family includes various bacterial integrases and integrases from the deletion-prone region of plasmid pAE1 of Alcaligenes eutrophus H1. All three integrases contain a catalytic motif, suggesting that they are all active enzymes. However, their specific roles are not fully understood. All three families belong to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism is essentially identical and involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA
SPDEVRRLLAAIDRLTPVGLRDYAILLLLARLGLRAGDVAGLRLDDIDWRSGTITVRQKKTGRPVELPLT
EPVGEALADYLRDGRPRTDSREVFLRARAPYRPLSSTSQISSIVRRYLRKAGIEPSHRGTHSLRHSLATR
MLRAGTSLKVIADLLGHRSIETTAIYAKIDVDDLREVAL
>gnl|CDD|271189 cd01189, INT_ICEBs1_C_like, C-terminal catalytic domain of integrases from bacterial phages and conjugate transposons. This family of tyrosine based site-specific integrases is has origins in bacterial phages and conjugate transposons. One member is the integrase from Bacillus subtilis conjugative transposon ICEBs1. ICEBs1 can be excised and transfered to various recipients in response to DNA damage or high concentrations of potential mating partners. The family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA
PEELKKLLEALKKRGDRYYLLFLLALLTGLRRGELLALTWSDIDFENGTIRINRTLVRKKKGGYVIKPPK
TKSSIRTIPLPDELIELLKELKAFKKLLKKAGLPRITPHDLRHTFASLLLEAGVPLKVIAERLGHSDIST
TLDVYAH
>gnl|CDD|271190 cd01190, INT_StrepXerD_C_like, Putative XerD in Streptococcus pneumonia and similar proteins, C-terminal catalytic domain. This family includes a putative XerD recombinase in Streptococcus pneumonia and similar tyrosine recombinases. However, the members of this family contain unusual active site motifs from the XerD from Escherichia coli. E. coli XerD and homologous enzymes show four conserved amino acids R-H-R-H that are spaced along the C-terminal domain. The putative S. pneumoniae XerD contains three unique replacements at the conserved positions resulting in L-Q-R-L. Severe growth defects in a loss-of-function xerD mutant demonstrate an important in vivo function of the S. pneumoniae XerD protein. This family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA
EPPEILDLSSFYQGDFLKGQLIALLILELGLTPSEIANLKWADFDLDFQVLTIEKGGIKRVLPLPKKLLP
FLEQHIKADYLEFDHEGKAYSRQWLFNQLKKFLNSIGLSGLTAQKLREQYILKQKEAGKSIYELAKLLGL
KSPVTLEKYY
>gnl|CDD|271191 cd01191, INT_C_like_2, Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain. Tyrosine recombinase (integrase) belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain contains six conserved active site residues. The recombination reaction involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity
VISNADYNFLKKCLKKDGNLEWYFVVRFLAATGARVSELIKIKVEHVELGYFDIYSKGGKLRRLYIPKKL
RNEALEWLKSTNRKSGYIFLNRFGERITTRGIAQQLKNYARKYGLNPKVVYPHSFRHRFAKNFLEKYNDI
ALLADLMGHESIETTRIYLRKTASEQQEIVDKIVTW
>gnl|CDD|271192 cd01192, INT_C_like_3, Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain. Tyrosine recombinase (integrase) belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain contains six conserved active site residues. The recombination reaction involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity
QIVEPIKDKKLIKEIKLYLKKANPRNYLLFIVGINTGLRISDLLSLKVEDVTNKDKLSIKEQKTGKQKTF
PLNPTLVKALKEYIDDLDLKRNDYLFKSLKQGPEKPISRKQAYKILKKAADDLGLNYNIGTHSLRKTFGY
HVYKQGKDIELLMKLLNHSSPSITLRYLGIDQEDVDKA
>gnl|CDD|271193 cd01193, INT_IntI_C, Integron integrase and similar protiens, C-terminal catalytic domain. Integron integrases mediate site-specific DNA recombination between a proximal primary site (attI) and a secondary target site (attC) found within mobile gene cassettes encoding resistance or virulence factors. Unlike other site specific recombinases, the attC sites lack sequence conservation. Integron integrase exhibits broader DNA specificity by recognizing the non-conserved attC sites. The structure shows that DNA target site recognition are not dependent on canonical DNA but on the position of two flipped-out bases that interact in cis and in trans with the integrase. Integron-integrases are present in many natural occurring mobile elements, including transposons and conjugative plasmids. Vibrio, Shewanella, Xanthomonas, and Pseudomonas species harbor chromosomal super-integrons. All integron-integrases carry large inserts unlike the TnpF ermF-like proteins also seen in this group
KLPVVLSPDEVRRILGALTELRHRLILSLLYGAGLRISELLRLRVKDIDFERGVIRVRQGKGGKDRVVPL
PEKLLEPLRRYLKSARPKEELDPAEGRAGVLDPRTGVERRHHISETTVQRALKKAVEQAGITKRVTPHTL
RHSFATHLLEAGTDIRTIQELLGHSDLSTTMIYTHV
>gnl|CDD|271194 cd01194, INT_C_like_4, Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain. Tyrosine recombinase (integrase) belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain contains six conserved active site residues. The recombination reaction involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity
LTLEQARQLLASLPIDDSIIGLRDRAIISLMVTEGLRTVEIVRADVGDLRQEGEGTILYVQGKGKTSKDD
FVYLRPDVLKALQAYLKARGKLDFEEPLFTSLSNNSKGQRLTTRSIRRIIKKYLRKAGLDDDRLTAHSLR
HTAGTLALKAGKSLREVQQLLRHSDPNTTMIYAH
>gnl|CDD|271195 cd01195, INT_C_like_5, Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain. Tyrosine recombinase (integrase) belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain contains six conserved active site residues. The recombination reaction involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity
SREEARQRLDAADRHTAKGKRDEALVRLLLDNALRRSEAVALDVEDLEKEHRRLRILGKGKKQREVVTLP
PTTREALAAWLAARGEAEGPLFVSLDRASRGRRLSPQAVYRIVRRLAERIGLGKRLSPHGLRHSAITLAL
DAGAGLIRKVQDFSRHADLRTLQVYDDQRD
>gnl|CDD|271196 cd01196, INT_C_like_6, Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain. Tyrosine recombinase (integrase) belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain contains six conserved active site residues. The recombination reaction involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity
TAPEARRLLESIDSTHPVGLRDRALIALMVYSFARIGAVLAMRVEDVYDQGRRLWVRLAEKGGKQHEMPC
HHDLEEYLRAYLEAAEIEEDPKGPLFRTTRGGTRKLTHNPLTQANAYRMVRRRAIAADIPTAIGNHSFRA
TGITAYLKNGGTLEDAQNMANHASTRTTQLYDRRSDKITLDEV
>gnl|CDD|271197 cd01197, INT_FimBE_like, FimB and FimE and related proteins, integrase/recombinases. This CD includes proteins similar to E.coli FimE and FimB and Proteus mirabilis MrpI. FimB and FimE are the regulatory proteins during expression of type 1 fimbriae in Escherichia coli. The fimB and fimE proteins direct the phase switch into the 'on' and 'off' position. MrpI is the regulatory protein of proteus mirabilis fimbriae expression. This family belongs to the integrase/recombinase superfamily
MKQRKYLTGKEVQALLQAACRGRTPARDYCLLLLAFRHGFRVSELCDLHLSDVDLESRRLHIRRLKNGFS
TTHPLRFDEREALEAWLKERANWKGADTDWIFLSRRGGPLSRQQAYRIIRDLGKEAGTVTQTHPHMLRHA
CGYALADRGADTRLIQDYLGHRNIRHTVIYTASNAARFANL
>gnl|CDD|238605 cd01200, WHEPGMRS_RNA, EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes
YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT
>gnl|CDD|275391 cd01201, PH_BEACH, Pleckstrin homology domain in BEACH domain containing proteins. The BEACH domain is present in several eukaroyotic proteins CHS, neurobeachin (Nbea), LRBA (also called BGL, beige-like, or CDC4L), FAN, KIAA1607, and LvsA-LvsF. CHS is a rare, autosomal recessive disorder that can cause severe immunodeficiency and albinism in mammals and beige is the name for the CHS disease in mice. The CHS disease is associated with the presence of giant, perinuclear vesicles (lysosomes, melanosomes, and others) and CHS protein is thought to play an important role in the fusion, fission, or trafficking of these vesicles. All BEACH proteins contain the following domains: PH, BEACH, and WD40. The WD40 domain is involved in mediating protein-protein interactions involved in targeting proteins to subcellular compartments. The combined PH-BEACH motifs may present a single continuous structural unit involved in protein binding. Some members have an additional N-terminal Laminin G-like (LamG) domains Ca++ mediated receptors or an additional C-terminal FYVE zinc-binding domain which targets proteins to membrane lipids via interaction with phosphatidylinositol-3-phosphate, PI3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKIVVINSQKVLSYKEHLVFKWSLSDIREV
HKRRYLLRDTALEIFFTDGTNYFLNFPSKERNDVYKKLLSLL
>gnl|CDD|269913 cd01202, PTB_FRS2, Fibroblast growth factor receptor substrate 2 phosphotyrosine-binding domain. FRS2 (also called Suc1-associated neurotrophic factor (SNT)-induced tyrosine-phosphorylated target) proteins are membrane-anchored adaptor proteins. They are composed of an N-terminal myristoylation site followed by a phosphotyrosine binding (PTB) domain, which has a PH-like fold, and a C-terminal effector domain containing multiple tyrosine and serine/threonine phosphorylation site. The FRS2/SNT proteins show increased tyrosine phosphorylation by activated receptors, such as fibroblast growth factor receptor (FGFR) and TrkA, recruit SH2 domain containing proteins such as Grb2, and mediate signals from activated receptors to a variety of downstream pathways. The PTB domains of the SNT proteins directly interact with the canonical NPXpY motif of TrkA in a phosphorylationdependent manner, they directly bind to the juxtamembrane region of FGFR in a phosphorylation-independent manner. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the IRS-like subgroup
DLHPNIFKVINVDDDGNELGSGILEVTETELILYQRGKEPVRWPLLCLRRYGYDSNLFSFESGRRCATGE
GIYAFKCKRAEELFNLVQRLIQ
>gnl|CDD|269914 cd01203, PTB_DOK1_DOK2_DOK3, Downstream of tyrosine kinase 1, 2, and 3 proteins phosphotyrosine-binding domain (PTBi). The Dok family adapters are phosphorylated by different protein tyrosine kinases. Dok proteins are involved in processes such as modulation of cell differentiation and proliferation, as well as in control of the cell spreading and migration The Dok protein contains an N-terminal pleckstrin homology (PH) domain followed by a central phosphotyrosine binding (PTB) domain, which has a PH-like fold, and a proline- and tyrosine-rich C-terminal tail. The PH domain is binds to acidic phospholids and localizes proteins to the plasma membrane, while the PTB domain mediates protein-protein interactions by binding to phosphotyrosine-containing motifs. The C-terminal part of Dok contains multiple tyrosine phosphorylation sites that serve as potential docking sites for Src homology 2-containing proteins such as ras GTPase-activating protein and Nck, leading to inhibition of ras signaling pathway activation and the c-Jun N-terminal kinase (JNK) and c-Jun activation, respectively. There are 7 mammalian Dok members: Dok-1 to Dok-7. Dok-1 and Dok-2 act as negative regulators of the Ras-Erk pathway downstream of many immunoreceptor-mediated signaling systems, and it is believed that recruitment of p120 rasGAP by Dok-1 and Dok-2 is critical to their negative regulation. Dok-3 is a negative regulator of the activation of JNK and mobilization of Ca2+ in B-cell receptor-mediated signaling, interacting with SHIP-1 and Grb2. Dok-4- 6 play roles in protein tyrosine kinase(PTK)-mediated signaling in neural cells and Dok-7 is the key cytoplasmic activator of MuSK (Muscle-Specific Protein Tyrosine Kinase). PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the IRS-like subgroup
EVKEFPVVVQRTEASERCRLKGSYLLRAGQDALELLDPQTKKPLYSWPYRFLRRFGRDKVMFSFEAGRRC
DSGEGLFTFETPQGNEIFQAVEAAIAAQK
>gnl|CDD|269915 cd01204, PTB_IRS, Insulin receptor substrate phosphotyrosine-binding domain (PTBi). Insulin receptor substrate (IRS) molecules are mediators in insulin signaling and play a role in maintaining basic cellular functions such as growth and metabolism. They act as docking proteins between the insulin receptor and a complex network of intracellular signaling molecules containing Src homology 2 (SH2) domains. Four members (IRS-1, IRS-2, IRS-3, IRS-4) of this family have been identified that differ as to tissue distribution, subcellular localization, developmental expression, binding to the insulin receptor, and interaction with SH2 domain-containing proteins. IRS molecules have an N-terminal PH domain, followed by an IRS-like PTB domain which has a PH-like fold. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the IRS-like subgroup
FEHVWQVTVKKKGLGQSKNLTGIYRLCLTSKTLSLVKLNSEKNPPSVEIQLMNIRRCGHSENFFFIEVGR
SAVTGPGELWMQVDDSVVAQNMHETILEAMKALSEE
>gnl|CDD|269916 cd01205, EVH1_WASP-like, WASP family proteins EVH1 domain. The Wiskott-Aldrich Syndrome Protein (WASP; also called Bee1p) and its homolog N (neuronal)-WASP are signal transduction proteins that promote actin polymerization in response to upstream intracellular signals. WAS is an X-linked recessive disease, characterized by eczema, immunodeficiency, and thrombocytopenia. The majority of patients with WAS, or a milder version of the disorder, X-linked thrombocytopenia (XLT), have point mutations in the EVH1 domain of WASP. WASP is an actin regulatory protein consisting of an N-terminal EVH1 domain called WH1 which binds LPPPEP peptides, a basic region (B), a GTP binding domain (GBP), a proline rich region, a WH2 domain, and a verprolin-cofilin-acidic motif (VCA) which activates the actin-related protein (Arp)2/3 actin nucleating complex. The B, GBD, and the proline-rich region are involved in autoinhibitory interactions that repress or block the activity of the VCA. Yeast members lack the GTP binding domain. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains
ILAAAVARLYYAEPDPDSWSYTGLTGALCFVKDNAKRSYFFRLVDLKTRGVVWEQELYEGFEYNQDRPFF
HTFEGDECMIGLNFADEDEAAAFYKKVQEKL
>gnl|CDD|269917 cd01206, EVH1_Homer_Vesl, Homer/Vesl family proteins EVH1 domain. Homer/Vesl proteins are synaptic scaffolding proteins, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation. They contains an N-terminal EVH1 domain and bind to both neurotransmitter receptors, such as the metabotropic group 1 glutamate receptor (mGluR) and to other scaffolding proteins via PPXXF motifs, in order to target them to the synaptic junction. These mGluRs possess a long C-terminal intracellular tail that may be important for subcellular localization of the receptor. The C-terminus is also the site of binding by the immediate early gene (IEG), Homer 1a. In contrast to Homer 1a, other Homer members additionally encode a C-terminal coiled-coil (CC) domain and form multivalent complexes that bind group 1 mGluRs. Homer 1a competes with constitutively expressed CC-Homers to modify the association of group 1 mGluRs with CC-Homer complexes. Since Homer proteins are strikingly enriched at the postsynaptic density (PSD), these observations suggest a role for the Homer family in regulating synaptic metabotropic receptor function. PSD-Zip45 (also named Homer 1c/Vesl-1L) has an EVH1 domain with a longer alpha-helix and its linking part included in the conserved region of Homer 1 (CRH1) interacts with the EVH1 domain of the neighbour CRH1 molecule in the crystal, suggesting that the EVH1 domain recognizes the PPXXF motif found in the binding partners, and the SPLTP sequence (P-motif) in the linking region of the CRH1. The two types of binding are partly overlapped in the EVH1 domain, implying a mechanism to regulate multimerization of Homer 1 family proteins. Homer 2 and Homer 3 are negative regulators of T cell activation. They bind the nuclear factor of activated T cells (NFAT) and compete with calcineurin binding. NFAT plays a critical role in calcium-dependent signaling in other cell types, including muscle and neurons. Homer-NFAT binding is also antagonized by active serine-threonine kinase AKT, enhancing TCR signaling via calcineurin-dependent dephosphorylation of NFAT resulting in changes in cytokine expression and an increase in effector-memory T cell populations in Homer-deficient mice. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains
EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQ
KFGQWADSRANTVYGLGFASEAELTKFAEKFQEAKEAAK
>gnl|CDD|269918 cd01207, EVH1_Ena_VASP-like, Enabled/VASP family EVH1 domain. Ena/VASP family includes proteins such as: Vasodilator-stimulated phosphoprotein (VASP), enabled gene product from Drosophila (Ena), mammalian enabled (Mena) and Ena/VASP-Like protein (EVL) localize to focal adhesions and to sites of actin filament dynamics. These proteins share a common modular organization with a highly conserved N- and C-terminal domains, termed Ena/VASP homology domains 1 and 2 (EVH1 and EVH2), that are separated by a central proline-rich domain. The EVH1 domain binds to other proteins at proline rich sequences. The majority of Ena-VASP type EVH1 domains recognize FPPPP motifs such as in the focal adhesion proteins zyxin and vinculin, and the ActA surface protein of Listeria monocytogenes, however the LIM3 domain of Tes lacks the FPPPP motif but still binds the EVH1 domain of Mena. It has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains. EVH2 mediates oligomerization within the family. The proline-rich region binds SH3 and WW domains as well as profilin, a protein that regulates actin filament dynamics. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains
SVASARASVMVYDDENKRWVPSGGSQGLSRVQIYHNTRNNTFRVVGRKLQDHEVVINCAILKGLKYNQAT
PTFHQWRDARQVYGLNFASKEEATEFAQAMLLALERLN
>gnl|CDD|269919 cd01208, PTB_X11, X11-like Phosphotyrosine-binding (PTB) domain. The function of the neuronal protein X11 is unknown to date. X11 has a PTB domain followed by two PDZ domains. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
PEDLIDGVIFGANYLGSTQLLSERNPSKNVRMAQAQEAVSRVKAPEGESQPSTEVDLFISTERIKVLNAD
TQETMMDHALRTISYIADIGNIVVLMARRRMPRSSSQECVETTPPSQEGKRQYKMICHVFESEDAQLIAQ
SIGQAFSVAYQEFLRANGINP
>gnl|CDD|269920 cd01209, PTB_Shc, Shc-like phosphotyrosine-binding (PTB) domain. Shc is a substrate for receptor tyrosine kinases, which can interact with phosphoproteins at NPXY motifs. Shc contains an PTB domain followed by an SH2 domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Shc-like subgroup
RGWLHPDQLGMGPGVSYPVRYVGCIEVLQSMRSLDFNTRTQVTREAINRVCEAVGGAKGAKRKRKSKALS
SILGKSNLQFAGMNISLTISTDGLNLVTPDTGQIIANHHMQSISFASGGDPDTYDYVAYVAKDPVNQRAC
HVLECGDGLAQDVIATIGQAFELRFKQYLK
>gnl|CDD|269921 cd01210, PTB_EPS8, Epidermal growth factor receptor kinase substrate (EPS8)-like Phosphotyrosine-binding (PTB) domain. EPS8 is a regulator of Rac signaling. It consists of a PTB and an SH3 domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
DTSQYRVEHLATFTLGREEGVQTVEDALRKLKELDAKGRIWSQEMLLQVNDGWVLLLDIETKEELESFPL
SSIQECTAVLSTCSYNSILLLVVQEPDQPKPEMHLFQCDEVGAELLVEDLQKALSGKRSGR
>gnl|CDD|269922 cd01211, PTB_Rab6GAP, GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain. GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
TIFNGVTYLGCAKVNAPRSETEALRIMAILREQSAQPIKVTLSVPNSSEGSVRLYDPTSNTEIASYPIYR
ILFCARGPDGTSESDCFAFTWSHGETAIFQCHVFRCEIPEAVSKVLYSFAKAFRRVPKS
>gnl|CDD|269923 cd01212, PTB_JIP, JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain. JIP is a mitogen-activated protein kinase scaffold protein. JIP consists of a C-terminal SH3 domain, followed by a PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
WRERFLLGFLGSVEVPYHKGNDVLCQAMQKIATARRLTVHLRPPQSCILEISDRGLKMVDRSKPNKKDGK
PCIHYFYSLKNISFCGFHPRNSRYFGFITKHPLLQRFACHVFVSQESTRPVAESVGRAFQRFYQEFIEYA
CPTEDIYLE
>gnl|CDD|269924 cd01213, PTB_tensin, Tensin Phosphotyrosine-binding (PTB) domain. Tensin is a a focal adhesion protein, which contains a C-terminal SH2 domain followed by a PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
GAACNVLYLGSVDTESLTGPQAVRKAVSETLERDPLPTPTVVHFKVSEQGITLTDNQRKLFFRRHYPLNT
VSFCGMDPENRKWQKYDLRGSKPSRIFGFVARKQGSSTENVCHLFAELDPEQPASAIVNFVNKVLL
>gnl|CDD|269925 cd01214, PTB_FAM43A, Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain. The function of FAM43A is currently unknown. Human FAM43A is located on chromosome 3 at location 3q29. It encodes a 3182 base pair mRNA which possesses one Pleckstrin homology-like domain. The mRNA translates into LOC131583, a hydrophilic protein that is predicted to localize in the nucleus. The FAM43A gene is conserved through a broad range of vertebrates. It is highly conserved from chimpanzees to zebrafish. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains
ITEEDPTYTVVYLGNVLTIWAKGEGCTDKPLATIWRNYTQGKKPDVKMKLTVTPSGLKATTKQHGLTEYW
LHRITYCSAPPNYPRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIALLLYQR
>gnl|CDD|269926 cd01215, PTB_Dab, Disabled (Dab) Phosphotyrosine-binding domain. Dab is a cystosolic adaptor protein, which binds to the cytoplasmic tails of lipoprotein receptors, such as ApoER2 and VLDLR, via its PTB domain. The dab PTB domain has a preference for unphosphorylated tyrosine within an NPxY motif. Additionally, the Dab PTB domain, which is structurally similar to PH domains, binds to phosphatidlyinositol phosphate 4,5 bisphosphate in a manner characteristic of phosphoinositide binding PH domains. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
DKTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAAGEHKQRIWLNISLEGIKIL
DEKTGALLHHHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFELKKK
EIEEKKA
>gnl|CDD|241252 cd01217, PTB_CG12581, CG12581 Phosphotyrosine-binding (PTB) domain. The function of CG12581 and its related proteins are unknown to date. Members here contain a single N-terminal PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
DSTPICRCRVLYLGSAVPHITKDGLQGIQEPLRELYPEQGALGARGIDSWLSVWSNGLLLENVDENKKTV
TRFFPIESLHYCAAVRYVLVPGFSNGGGGERFLPLDSPFARHPNAQHPPLFAAILRRTTGIKVLECHAFI
CKREKAANALVRCCFHAYADSSYAKQ
>gnl|CDD|269927 cd01218, PH_Phafin2-like, Phafin2 (also called EAPF, FLJ13187, ZFYVE18 or PLEKHF2) Pleckstrin Homology (PH) domain. Phafin2 is differentially expressed in the liver cancer cell and regulates the structure and function of the endosomes through Rab5-dependent processes. Phafin2 modulates the cell's response to extracellular stimulation by modulating the receptor density on the cell surface. Phafin2 contains a PH domain and a FYVE domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
NSEANRRRIAAVESCFGGSGQPLVKPGRVLVGEGVLTKVCRKKPKPRQFFLFNDILVYGSIVINKKKYNK
QRIIPLEDVKIEDLEDTGELKNGWQIISPKKSFVVYAATATEKSEWMDHINKC
>gnl|CDD|275392 cd01219, PH1_FGD1, FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 1, N-terminal Pleckstrin homology (PH) domain. In general, FGDs have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain. Mutations in the FGD1 gene are responsible for the X-linked disorder known as faciogenital dysplasia (FGDY). Both FGD1 and FGD3 are targeted by the ubiquitin ligase SCF(FWD1/beta-TrCP) upon phosphorylation of two serine residues in its DSGIDS motif and subsequently degraded by the proteasome. However, FGD1 and FGD3 induced significantly different morphological changes in HeLa Tet-Off cells and while FGD1 induced long finger-like protrusions, FGD3 induced broad sheet-like protrusions when the level of GTP-bound Cdc42 was significantly increased by the inducible expression of FGD3. They also reciprocally regulated cell motility in inducibly expressed in HeLa Tet-Off cells, FGD1 stimulated cell migration while FGD3 inhibited it. FGD1 and FGD3 therefore play different roles to regulate cellular functions, even though their intracellular levels are tightly controlled by the same destruction pathway through SCF(FWD1/beta-TrCP). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LIKEGHILKLSAKNGTTQDRYLILFNDRLLYCVPKLRLIGQKFSVRARIDVEGMELKESSSLNLPRTFLV
SGKQRSLELQARTEEEKKDWIQAIQATIQRHEQTLETF
>gnl|CDD|269928 cd01220, PH1_FARP1-like, FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin Homology (PH) domain, repeat 1. Members here include FARP1 (also called Chondrocyte-derived ezrin-like protein; PH domain-containing family C member 2), FARP2 (also called FIR/FERM domain including RhoGEF; FGD1-related Cdc42-GEF/FRG), and FARP6 (also called Zinc finger FYVE domain-containing protein 24). They are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases. Little is known about FARP1 and FARP6, though FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons. FARP1 and FARP2 are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains. FARP6 is composed of Dbl-homology (DH), and two C-terminal PH domains separated by a FYVE domain. This hierarchy contains the first PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LVQPGREFIREGCLQKLSKKGLQQRMFFLFSDVLLYTSRSPTPSLQFKVHGQLPLRGLMVEESEPEWGVA
HCFTIYGGNRALTVAASSEEEKERWLEDLQRAIDAAKKS
>gnl|CDD|269929 cd01221, PH_ephexin, Ephexin Pleckstrin homology (PH) domain. Ephexin-1 (also called NGEF/ neuronal guanine nucleotide exchange factor) plays a role in the homeostatic modulation of presynaptic neurotransmitter release. Specific functions are still unknown for Ephexin-2 (also called RhoGEF19) and Ephexin-3 (also called Rho guanine nucleotide exchange factor 5/RhoGEF5, Transforming immortalized mammary oncogene/p60 TIM, and NGEF/neuronalGEF). Ephexin-4 (also called RhoGEF16) acts downstream of EphA2 to promote ligand-independent breast cancer cell migration and invasion toward epidermal growth factor through activation of RhoG. This in turn results in the activation of RhoG which recruits ELMO2 and Dock4 to form a complex with EphA2 at the tips of cortactin-rich protrusions in migrating breast cancer cells. Ephexin-5 is the specific GEF for RhoA activation and the regulation of vascular smooth muscle contractility. It interacts with EPHA4 PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. The members of the Ephexin family contains a RhoGEF (DH) followed by a PH domain and an SH3 domain. The ephexin PH domain is believed to act with the DH domain in mediating protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KIKAFPLISSSRWLVKRGELTELVEDGGSLTFRKKFSKTPVYLFLFNDLLLITKKKSEERYLVLDYAPRN
LVQVEEVEDPLQLPQPLGKNLFLLTLLENHEGKTVELLLSAESESDRERWLSALSPPKSEL
>gnl|CDD|269930 cd01223, PH_Vav, Vav pleckstrin homology (PH) domain. Vav acts as a guanosine nucleotide exchange factor (GEF) for Rho/Rac proteins. They control processes including T cell activation, phagocytosis, and migration of cells. The Vav subgroup of Dbl GEFs consists of three family members (Vav1, Vav2, and Vav3) in mammals. Vav1 is preferentially expressed in the hematopoietic system, while Vav2 and Vav3 are described by broader expression patterns. Mammalian Vav proteins consist of a calponin homology (CH) domain, an acidic region, a catalytic Dbl homology (DH) domain, a PH domain, a zinc finger cysteine rich domain (C1/CRD), and an SH2 domain, flanked by two SH3 domains. In invertebrates such as Drosophila and C. elegans, Vav is missing the N-terminal SH3 domain. The DH domain is involved in RhoGTPase recognition and selectivity and stimulates the reorganization of the switch regions for GDP/GTP exchange. The PH domain is implicated in directing membrane localization, allosteric regulation of guanine nucleotide exchange activity, and as a phospholipid- dependent regulator of GEF activity. Vavs bind RhoGTPases including Rac1, RhoA, RhoG, and Cdc42, while other members of the GEF family are specific for a single RhoGTPase. This promiscuity is thought to be a result of its CRD. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but only a few (less than 10%) display strong specificity in binding inositol phosphates. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinases, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, cytoskeletal associated molecules, and in lipid associated enzymes
SIQDLIENLNESLADYGRLQIDGELKIKSHEDQKKKDRYAFLFDKVLLICKSLRGDQYEYKEIINLSEYR
IEDDPSRRTLKRDKRWSYQFLLVHKQGKTAYTLYAKTEELKKKWMEAIEMALSNIEP
>gnl|CDD|269931 cd01224, PH_Collybistin_ASEF, Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain. Collybistin (also called PEM2) is homologous to the Dbl proteins ASEF (also called ARHGEF4/RhoGEF4) and SPATA13 (Spermatogenesis-associated protein 13; also called ASEF2). It activates CDC42 specifically and not any other Rho-family GTPases. Collybistin consists of an SH3 domain, followed by a RhoGEF/DH and PH domain. In Dbl proteins, the DH and PH domains catalyze the exchange of GDP for GTP in Rho GTPases, allowing them to signal to downstream effectors. It induces submembrane clustering of the receptor-associated peripheral membrane protein gephyrin, which is thought to form a scaffold underneath the postsynaptic membrane linking receptors to the cytoskeleton. It also acts as a tumor suppressor that links adenomatous polyposis coli (APC) protein, a negative regulator of the Wnt signaling pathway and promotes the phosphorylation and degradation of beta-catenin, to Cdc42. Autoinhibition of collybistin is accomplished by the binding of its SH3 domain with both the RhoGEF and PH domains to block access of Cdc42 to the GTPase-binding site. Inactivation promotes cancer progression. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MENLEKLAAWQSTVEGWEGEDLSDRSSELIHSGELTKISAGRAQERTFFLFDHQLVYCKKDLLRRKNYIY
KGRIDTDNMEIEDLPDGKDDESGVTVKNAWKIYNASKNKWYVLCAKSAEEKQRWLEAFAEEREKVEKD
>gnl|CDD|269932 cd01225, PH_Cool_Pix, Cloned out of library/PAK-interactive exchange factor pleckstrin homology (PH) domain. There are two forms of Pix proteins: alpha Pix (also called Rho guanine nucleotide exchange factor (GEF) 6/90Cool-2) and beta Pix (GEF7/p85Cool-1). betaPix contains an N-terminal SH3 domain, a RhoGEF/DH domain, a PH domain, a GIT1 binding domain (GBD), and a C-terminal coiled-coil (CC) domain. alphaPix differs in that it contains a calponin homology (CH) domain, which interacts with beta-parvin, N-terminal to the SH3 domain. alphaPix is an exchange factor for Rac1 and Cdc42 and mediates Pak activation on cell adhesion to fibronectin. Mutations in alphaPix can cause X-linked mental retardation. alphaPix also interacts with Huntington's disease protein (htt), and enhances the aggregation of mutant htt (muthtt) by facilitating SDS-soluble muthtt-muthtt interactions. The DH-PH domain of a Pix was required for its binding to htt. In the majority of Rho GEF proteins, the DH-PH domain is responsible for the exchange activity. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VIHMSQVAVQNTGCQEKKERYFLLFPHVLLMLSASPRMSGFIYEGKLPLTGISVNRLEDTEGIKNAFEIS
GPLIERIVVICNSQQDQQEWLEHLQQQTKA
>gnl|CDD|269933 cd01226, PH_RalBD_exo84, Exocyst complex 84-kDa subunit Ral-binding domain/Pleckstrin Homology (PH) domain. The Sec6/8 complex, also called the exocyst complex, forms an octameric protein (Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70 and Exo84) involved in the tethering of secretory vesicles to specific regions on the plasma membrane. The regulation of Sec6/8 complex differs between mammals and yeast. Mamalian Exo84 and Sec5 are effector targets for active Ral GTPases which are not present in yeast. Ral GTPases are members of the Ras superfamily, and as such cycle between an active GTP-bound state and an inactive GDP-bound state. The Exo84 Ral-binding domain adopts a PH domain fold. Mammalian Exo84 and Sec5 competitively bind to active RalA. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VEVPGRYLLHEGDLLELDPDDYKPIQKVHLFLLNDVLLIASWLPNRRGPVRYKFQALYPLEDLAVVNVKD
LGPVKNAFKLLTFPETRVFQCENAKIKKEWLEKFEQAKRAKLAKE
>gnl|CDD|269934 cd01227, PH_Dbs, DBL's big sister protein pleckstrin homology (PH) domain. Dbs (also called MCF2-transforming sequence-like protein 2) is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
AITGYDGNLGDLGKLLMQGSFNVWTEHKKGHTKKLARFKPMQRHIFLYEKAVLFCKKRGENGEAPSYSYK
NSLNTTAVGLTENVKGDTKKFEIWLNGREEVFIIQAPTPEIKAAWVKAIRQVLLSQ
>gnl|CDD|269935 cd01228, PH_BCR-related, Breakpoint Cluster Region-related pleckstrin homology (PH) domain. The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. ABR, a related smaller protein, is structurally similar to BCR, but lacks the N-terminal kinase domain and has GAP activity for both Rac and Cdc42. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RQLVKDGFLVELSEGSRKLRHLFLFTDVLLCAKLKSAGRGFQGQYECKWYIPLRDLSLHPKDESEASPIV
PVTSDKELEVLKSKIAELKKQIRDDDAQRKKASSSGSKAIEKLRKKLAEQEAALLLASPSLPLRLYHRNG
KTYTFLLSSDYERSEWKEAILKLQKK
>gnl|CDD|269936 cd01229, PH_Ect2, Epithelial cell transforming 2 (Ect2) pleckstrin homology (PH) domain. Ect2, a mammalian ortholog of Drosophila pebble, plays a role in neuronal differentiation and brain development. Pebble and Ect2 have been identified as Rho-family guanine nucleotide exchange factors (GEF) that mediate activation of Rho during cytokinesis, but are proposed to play slightly different roles. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LKEVMTHINEDKRKTESQAQMFDIVNEIENCPPTLLSSHRSFVSRCEVVELGDSLKSGRGDSLTLFLFSD
LIEICKKRSSVKGTSKSPRGSTGSGLRESKKKYKHVKLMPLSTIKRVIDIRETEDCQRVFALLFRHPTEL
KEKLYSFQILDEETDKESFLKTLCKQVANTVCRADAENFL
>gnl|CDD|269937 cd01230, PH1_Tiam1_2, T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain. Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2.Neither of these fall in the PHn domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
GAVRKAGWLSVKNFLVHKKNKKVELATRRKWKKYWVCLKGCTLLFYECDERSGIDENSEPKHALFVEGSI
VQAVPEHPKKDFVFCLSNSFGDAYLFQATSQTELENWVTAIHSACASAFARQHGKED
>gnl|CDD|269938 cd01231, PH_SH2B_family, SH2B adapter protein 1, 2, and 3 Pleckstrin homology (PH) domain. SH2B family/APS proteins are a family of intracellular adaptor proteins that influences a variety of signaling pathways mediated by Janus kinase (JAK) and receptor tyrosine kinases (RTKs) including receptors for insulin, insulin-like growth factor-1, Janus kinase 2 (Jak2), platelet derived growth factor, fibroblast growth factor and nerve growth factor. They function in glucose homeostasis, energy metabolism, hematopoesis and reproduction. Mutations in human SH2B orthologs are associated with metabolic disregulation and obesity. There are several SH2B members in mammals: SH2B1 (splice variants: SH2B1alpha, SH2B1beta, SH2B1gamma, and SH2B1delta), SH2B2 (APS) and SH2B3 (Lnk). They contain a PH domain, a SH2 domain, a proline rich region, multiple consensus sites for tyrosine and serine/threonine phosphorylation and a highly conserved c-Cbl recognition motif. These domains function as protein-protein interaction motifs which allows SH2B proteins to integrate and transduce intracellular signals from multiple signaling networks in the absence of intrinsic catalytic activity. SH2B proteins bind via their SH2 domains to phosphotyrosine residues within the intracellular tails of several activated RTKs thereby contributing to receptor activation. SH2B proteins have been shown to interact with insulin receptor substrates IRS1 and IRS2, Grb2, Shc and c-Cbl which may or may not require RTK-stimulated tyrosine phosphorylation of SH2B. positively and negatively regulating RTK signaling. Understanding the physiological functions of SH2B proteins in mammals has been complicated by the presence of multiple SH2B isoforms and conflicting data. Both SH2-Bbeta and APS associate with JAKs, but the former facilitates JAK/STAT signaling while the latter inhibits it. Lnk plays a role in cell growth and proliferation with mutations resulting in growth reduction, developmental delay and female sterility. Recently Lnk Drosophila has been shown to be an important regulator of the insulin/insulin-like growth factor (IGF)-1 signaling (IIS) pathway during growth. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
ECRKEGIVNYLSGEETASDGGPRWQKCRLVLVKAAGGEGEYLLEFYVPPKSSKPKLGIFCSLIQEVRETT
ALEMPDNENTFVLKVENSTEYIIEAGDEQQMRSWLAEIRECMSPG
>gnl|CDD|269939 cd01233, PH_KIFIA_KIFIB, KIFIA and KIFIB protein pleckstrin homology (PH) domain. The kinesin-3 family motors KIFIA (Caenorhabditis elegans homolog unc-104) and KIFIB transport synaptic vesicle precursors that contain synaptic vesicle proteins, such as synaptophysin, synaptotagmin and the small GTPase RAB3A, but they do not transport organelles that contain plasma membrane proteins. They have a N-terminal motor domain, followed by a coiled-coil domain, and a C-terminal PH domain. KIF1A adopts a monomeric form in vitro, but acts as a processive dimer in vivo. KIF1B has alternatively spliced isoforms distinguished by the presence or absence of insertion sequences in the conserved amino-terminal region of the protein; this results in their different motor activities. KIF1A and KIF1B bind to RAB3 proteins through the adaptor protein mitogen-activated protein kinase (MAPK) -activating death domain (MADD; also calledDENN), which was first identified as a RAB3 guanine nucleotide exchange factor (GEF). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
PKSPVVSKRGYLLFLEDATDGWVRRWVVLRRPYLHIYSSEKDGDERGVINLSTARVEYSPDQEALLGRPN
VFAVYTPTNSYLLQARSEKEMQDWLYAIDPLLA
>gnl|CDD|269940 cd01234, PH_CADPS, Ca2+-dependent activator protein (also called CAPS) Pleckstrin homology (PH) domain. CADPS/CAPS consists of two members, CAPS1 which regulates catecholamine release from neuroendocrine cells and CAPS2 which is involved in the release of two neurotrophins, brain-derived neurotrophic factor (BDNF) and neurotrophin-3 (NT-3) from cerebellar granule cells. CADPS plays an important role in vesicle exocytosis in neurons and endocrine cells where it functions to prime the exocytic machinery for Ca2+-triggered fusion. Priming involves the assembly of trans SNARE complexes. The initial interaction of vesicles with target membranes is mediated by diverse stage-specific tethering factors or multi-subunit tethering complexes. CADPS and Munc13 proteins are proposed to be the functional homologs of the stage-specific tethering factors that prime membrane fusion. Interestingly, regions in the C-terminal half of CADPS are similar to the C-terminal region of Munc13-1 that was reported to bind syntaxin-1. CADPS has independent interactions with each of the SNARE proteins (Q-SNARE and R-SNARE) required for vesicle fusion. CADPS interacts with Q-SNARE proteins syntaxin-1 (H3 SNARE) and SNAP-25 (SN1) and might promote Q-SNARE heterodimer formation. Through its N-terminal R-SNARE VAMP-2 interactions, CADPS bound to heterodimeric Q-SNARE complexes could be involved in catalyzing the zippering of VAMP-2 into recipient complexes. It also contains a central PH domain that binds to phosphoinositide 4,5 bisphosphate containing liposomes. Membrane association may also be mediated by binding to phosphatidlyserine via general electrostatic interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RMDKPQNMKHCGYLYALGKSVWKKWKKRYFVLVQVSQYTFAMCSYREKKSEPQEMMQLDGYTVDYTDPQP
DLGLEGGRFFFNAVKEGDSVIFASDDENDRQLWVQALYRATGQSHKPVPPTQ
>gnl|CDD|269941 cd01235, PH_Sbf1_hMTMR5, Set binding factor 1 (also called Human MTMR5) Pleckstrin Homology (PH) domain. Sbf1 is a myotubularin-related pseudo-phosphatase. Both Sbf1 and myotubularin interact with the SET domains of Hrx and other epigenetic regulatory proteins, but Sbf1 lacks phosphatase activity due to several amino acid changes in its structurally preserved catalytic pocket. It contains pleckstrin (PH), GEF, and myotubularin homology domains that are thought to be responsible for signaling and growth control. Sbf1 functions as an inhibitor of cellular growth. The N-terminal GEF homology domain serves to inhibit the transforming effects of Sbf1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
ENRTHEGYLYKRGALLKGWKQRWFVLDSTKHQLRYYESREDTKCKGFIDLAEVESVTPATPIIGAPKRAD
EGAFFDLKTNKRVYNFCAFDAESAQQWIEKIQSCLS
>gnl|CDD|269942 cd01236, PH_RIP, Rho-Interacting Protein Pleckstrin homology (PH) domain. RIP1-RhoGDI2 was obtained in a screen for proteins that bind to wild-type RhoA. RIP2, RIP3, and RIP4 were isolated from cDNA libraries with constitutively active V14RhoA (containing the C190R mutation). RIP2 represents a novel GDP/GTP exchange factor (RhoGEF), while RIP3 (p116Rip) and RIP4 are thought to be structural proteins. RhoGEF contains a Dbl(DH)/PH region, a a zinc finger motif, a leucine-rich domain, and a coiled-coil region. The last 2 domains are thought to be involved in mediating protein-protein interactions. RIP3 is a negative regulator of RhoA signaling that inhibits, either directly or indirectly, RhoA-stimulated actomyosin contractility. In plants RIP3 is localized at microtubules and interacts with the kinesin-13 family member AtKinesin-13A, suggesting a role for RIP3 in microtubule reorganization and a possible function in Rho proteins of plants (ROP)-regulated polar growth. It has a PH domain, two proline-rich regions which are putative binding sites for SH3 domains, and a COOH-terminal coiled-coil region which overlaps with the RhoA-binding region. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
NKSKCKCCFCFRPRHSHLALEEARMQRKVIYCGWLYVAPPGTDFSNPSHRSKRWQRRWFVLYDDGELTYA
LDEMPDTLPQGSIDMSQCTEVTDAEARTGHPHSLAITTPERIHFVKADSKEEIRWWLELLAVYPRT
>gnl|CDD|269943 cd01237, PH_fermitin, Fermitin family pleckstrin homology (PH) domain. Fermitin functions as a mediator of integrin inside-out signalling. The recruitment of Fermitin proteins and Talin to the membrane mediates the terminal event of integrin signalling, via interaction with integrin beta subunits. Fermatin has FERM domain interrupted with a pleckstrin homology (PH) domain. Fermitin family homologs (Fermt1, 2, and 3, also known as Kindlins) are each encoded by a different gene. In mammalian studies, Fermt1 is generally expressed in epithelial cells, Fermt2 is expressed inmuscle tissues, and Fermt3 is expressed in hematopoietic lineages. Specifically Fermt2 is expressed in smooth and striated muscle tissues in mice and in the somites (a trunk muscle precursor) and neural crest in Xenopus embryos. As such it has been proposed that Fermt2 plays a role in cardiomyocyte and neural crest differentiation. Expression of mammalian Fermt3 is associated with hematopoietic lineages: the anterior ventral blood islands, vitelline veins, and early myeloid cells. In Xenopus embryos this expression, also include the notochord and cement gland. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
PELADYLKYFKPKKFTLKGYKRYWFVFKDTHLSYYKSKEESNGAPIQQINLKGCEVTPDVNVSQQKFCIK
LLVPSPEGMSEVWLRCDNEDQYAKWMAACRLASKGKTMADSSYDSEVSSILAFLS
>gnl|CDD|269944 cd01238, PH_Btk, Bruton's tyrosine kinase pleckstrin homology (PH) domain. Btk is a member of the Tec family of cytoplasmic protein tyrosine kinases that includes BMX, IL2-inducible T-cell kinase (Itk) and Tec. Btk plays a role in the maturation of B cells. Tec proteins general have an N-terminal PH domain, followed by a Tek homology (TH) domain, a SH3 domain, a SH2 domain and a kinase domain. The Btk PH domain binds phosphatidylinositol 3,4,5-trisphosphate and responds to signalling via phosphatidylinositol 3-kinase. The PH domain is also involved in membrane anchoring which is confirmed by the discovery of a mutation of a critical arginine residue in the BTK PH domain. This results in severe human immunodeficiency known as X-linked agammaglobulinemia (XLA) in humans and a related disorder is mice.PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LEGLLVKRSQGKKRFGPVNYKERWFVLTKSSLSYYEGDGEKRGKEKGSIDLSKVRCVEEVKDEAFFERKY
PFQVVYDDYTLYVFAPSEEDRDEWIAALRKVCRNNSNLHDKYHPGFWTGGKWSCCGQTSKSAPGCQPAFD
>gnl|CDD|269945 cd01239, PH_PKD, Protein kinase D (PKD/PKCmu) pleckstrin homology (PH) domain. Protein Kinase C family is composed of three members, PKD1 (PKCmu), PKD2 and PKD3 (PKCnu). Like the C-type protein kinases (PKCs), PKDs are activated by diacylglycerol (DAG). They are involved in vesicular transport, cell proliferation, survival, migration and immune responses. PKD consists of tandem C1 domains, followed by a PH domain and a kinase domain. While the PKD PH domain has not been shown to bind phosphorylated inositol lipids and is not required for membrane translocation, it is required for nuclear export. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
TKRRSSKVLKEGWMVHYTNKDPLRKRHYWRLDTKCITLFQNETTSRYYKEIPLSEILSVEPADNPSLPPG
TPPHCFEIRTANLVYYVGEDPDGESGPPKLIPPPESGSGTESARMWETAIRQALMPV
>gnl|CDD|269946 cd01240, PH_GRK2_subgroup, G Protein-Coupled Receptor Kinase 2 subgroup pleckstrin homology (PH) domain. GRKs are a family of serine-threonine kinases which phosphorylates activated G-protein coupled receptors leading to the release of the previously bound heterotrimeric G protein agonist and thus signal termination. There are seven mammalian GRKs (GRK1-7) grouped into three subfamilies: GRK1 (GRK1 and 7), GRK2 (GRK2 and 3), and GRK4 (GRK4-6). GRKs have three functional components: an N-terminal Regulators of G-protein signaling (RGS) which interacts with the seven-trans-membrane helical receptor protein and/or other membrane targets, a central catalytic protein kinase C (PKc) domain, and a C-terminal section containing a autophosphorylation region and a variable region that mediates membrane association. In both GRK2 (also known as beta-adrenergic receptor kinase-1) and GRK3 (beta-adrenergic receptor kinase-2), the C-terminal variable region contains a PH domain which gives binding specificity to Gbetagamma proteins. The GRK2 PH domain has an extended C-terminal helix, which mediates interactions with G beta gamma subunits. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
YAKGKDCIVHGYILKLGGPFLSAWQRRYFYLFPNRLELYGEGEDQQNKLELEEMDQVEETCIKGEKCIQL
KLKGGKQFLTNSDSEPELVQWKKELRDAFREAQRLLQRMPKKAGKIYG
>gnl|CDD|269947 cd01241, PH_PKB, Protein Kinase B-like pleckstrin homology (PH) domain. PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VSVVKEGWLLKRGEYIKNWRPRYFVLKSDGSFIGYKEKPKPNQDPPPLNNFSVAECQLMKTEKPKPNTFI
IRCLQWTTVIERTFHVESEEEREEWMKAIQGVASSLK
>gnl|CDD|269948 cd01242, PH_ROCK, Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain. ROCK is a serine/threonine kinase that binds GTP-Rho. It consists of a kinase domain, a coiled coil region and a PH domain. The ROCK PH domain is interrupted by a C1 domain. ROCK plays a role in cellular functions, such as contraction, adhesion, migration, and proliferation and in the regulation of apoptosis. There are two ROCK isoforms, ROCK1 and ROCK2. In ROCK2 the Rho Binding Domain (RBD) and the PH domain work together in membrane localization with RBD receiving the RhoA signal and the PH domain receiving the phospholipid signal. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SRLEGWLSLPNKQNIRRHGWKKQYVVVSSKKILFYNSEQDKANSNPILVLDIDKLFHVRSVTQGDVIRAD
AKEIPRIFQILYANEGESSRPAEVTDTLSVSREEKPNTIL
>gnl|CDD|269949 cd01243, PH_MRCK, MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain. MRCK is thought to be coincidence detector of signaling by Cdc42 and phosphoinositides. It has been shown to promote cytoskeletal reorganization, which affects many biological processes. There are 2 members of this family: MRCKalpha and MRCKbeta. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. The MRCK PH domain is responsible for its targeting to cell to cell junctions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
PLGIDPTRGIGTAYEGYVRVPKPGGVKKGWQRQFAVVCDFKLFLFDISEDKASQPSQVASQVLDMRDEEF
SVSSVLASDVIHANKKDIPCIFRVSASQLAPPSLKFSLLMLADSENEKQKWVDALNELHKLLKKN
>gnl|CDD|269950 cd01244, PH_GAP1-like, RAS p21 protein activator (GTPase activating protein) family pleckstrin homology (PH) domain. RASAL1, GAP1(m), GAP1(IP4BP), and CAPRI are all members of the GAP1 family of GTPase-activating proteins. They contain N-terminal SH2-SH3-SH2 domains, followed by two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. With the notable exception of GAP1(m), they all possess an arginine finger-dependent GAP activity on the Ras-related protein Rap1. They act as a suppressor of RAS enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. PH domains share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KEGYLIKRAQGRKKKFGRKNFKKRYFRLTNEALSYSKSKGKQPLCSIPLEDILAVERVEEESFKMKNMFQ
IVQPDRTLYLQAKNVVELNEWLSALRKVCLCNPNRLP
>gnl|CDD|269951 cd01247, PH_FAPP1_FAPP2, Four phosphate adaptor protein 1 and 2 Pleckstrin homology (PH) domain. Human FAPP1 (also called PLEKHA3/Pleckstrin homology domain-containing, family A member 3) regulates secretory transport from the trans-Golgi network to the plasma membrane. It is recruited through binding of PH domain to phosphatidylinositol 4-phosphate (PtdIns(4)P) and a small GTPase ADP-ribosylation factor 1 (ARF1). These two binding sites have little overlap the FAPP1 PH domain to associate with both ligands simultaneously and independently. FAPP1 has a N-terminal PH domain followed by a short proline-rich region. FAPP1 is a member of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), and Goodpasture antigen binding protein (GPBP). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. FAPP2 (also called PLEKHA8/Pleckstrin homology domain-containing, family A member 8), a member of the Glycolipid lipid transfer protein(GLTP) family has an N-terminal PH domain that targets the TGN and C-terminal GLTP domain. FAPP2 functions to traffic glucosylceramide (GlcCer) which is made in the Golgi. It's interaction with vesicle-associated membrane protein-associated protein (VAP) could be a means of regulation. Some FAPP2s share the FFAT-like motifs found in GLTP. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MEGVLWKWTNYLSGWQPRWFVLDDGVLSYYKSQEEVNQGCKGSVKMSVCEIIVHPTDPTRMDLIIPGEQH
FYLKASSAAERQRWLVALGSAKACLTDTRA
>gnl|CDD|269952 cd01248, PH_PLC_ELMO1, Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain. The C-terminal region of ELMO1, the PH domain and Pro-rich sequences, binds the SH3-containing region of DOCK2 forming a intermolecular five-helix bundle allowing for DOCK mediated Rac1 activation. ELMO1, a mammalian homolog of C. elegans CED-12, contains an N-terminal RhoG-binding region, a ELMO domain, a PH domain, and a C-terminal sequence with three PxxP motifs. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). All PLCs, except for PLCzeta, have a PH domain which is for most part N-terminally located, though lipid binding specificity is not conserved between them. In addition PLC gamma contains a split PH domain within its catalytic domain that is separated by 2 SH2 domains and a single SH3 domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LQQGTLLLKYREGSKPKERTFYLDPDGTRITWESSKKKSEKKSIDISDIKEIRPGKDTDGFKRKKKSNKP
KEERCFSIIYGSNNKTLDLVAPSEDEANLWVEGLRALL
>gnl|CDD|269953 cd01249, BAR-PH_GRAF_family, GTPase Regulator Associated with Focal adhesion and related proteins Pleckstrin homology (PH) domain. This hierarchy contains GRAF family members: OPHN1/oligophrenin1, GRAF1 (also called ARHGAP26/Rho GTPase activating protein 26), GRAF2 (also called ARHGAP10/ARHGAP42), AK057372, and LOC129897, all of which are members of the APPL family. OPHN1 is a RhoGAP involved in X-linked mental retardation, epilepsy, rostral ventricular enlargement, and cerebellar hypoplasia. Affected individuals have morphological abnormalities of their brain with enlargement of the cerebral ventricles and cerebellar hypoplasia. OPHN1 negatively regulates RhoA, Cdc42, and Rac1 in neuronal and non-neuronal cells. GRAF1 sculpts the endocytic membranes of the CLIC/GEEC (clathrin-independent carriers/GPI-enriched early endosomal compartments) endocytic pathway. It strongly interacts with dynamin and inhibition of dynamin abolishes CLIC/GEEC endocytosis. GRAF2, GRAF3 and oligophrenin are likely to play similar roles during clathrin-independent endocytic events. GRAF1 mutations are linked to leukaemia. All members are composed of a N-terminal BAR-PH domain, followed by a RhoGAP domain, a proline rich region, and a C-terminal SH3 domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
TKEGYLYLQEKKPLGSTWTKHYCTYRKESKMFTMIPYNQQSSGKLGTTEVVTLKSCVRRKTDSIDRRFCF
DIEVVDRPTVLTLQALSEEDRKLWLEAMDGKEPIY
>gnl|CDD|241281 cd01250, PH_AGAP, Arf-GAP with GTPase, ANK repeat and PH domain-containing protein Pleckstrin homology (PH) domain. AGAP (also called centaurin gamma; PIKE/Phosphatidylinositol-3-kinase enhancer) reside mainly in the nucleus and are known to activate phosphoinositide 3-kinase, a key regulator of cell proliferation, motility and vesicular trafficking. There are 3 isoforms of AGAP (PIKE-A, PIKE-L, and PIKE-S) the longest of which PIKE-L consists of N-terminal proline rich domains (PRDs), followed by a GTPase domain, a split PH domain (PHN and PHC), an ArfGAP domain and two ankyrin repeats. PIKE-S terminates after the PHN domain and PIKE-A is missing the PRD region. Centaurin binds phosphatidlyinositol (3,4,5)P3. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RAIPIKQGYLYKRSSKSLNKEWKKKYVTLCDDGRLTYHPSLHDYMENVHGKEIDLLRTTVKVPGKRPPRA
SSKSAFEFIIVSLDGKQWHFEAASSEERDEWVQAIEQQILASLQ
>gnl|CDD|241282 cd01251, PH2_ADAP, ArfGAP with dual PH domains Pleckstrin homology (PH) domain, repeat 2. ADAP (also called centaurin alpha) is a phophatidlyinositide binding protein consisting of an N-terminal ArfGAP domain and two PH domains. In response to growth factor activation, PI3K phosphorylates phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 3,4,5-trisphosphate. Centaurin alpha 1 is recruited to the plasma membrane following growth factor stimulation by specific binding of its PH domain to phosphatidylinositol 3,4,5-trisphosphate. Centaurin alpha 2 is constitutively bound to the plasma membrane since it binds phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate with equal affinity. This cd contains the second PH domain repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
DFLKEGYLEKTGPKQTDGFRKRWFTLDDRRLMYFKDPLDAFPKGEIFIGSKEEGYSVREGLPPGIKGHWG
FGFTLVTPDRTFLLSAETEEERREWITAIQKVLER
>gnl|CDD|269954 cd01252, PH_GRP1-like, General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain. GRP1/cytohesin3 and the related proteins ARNO (ARF nucleotide-binding site opener)/cytohesin-2 and cytohesin-1 are ARF exchange factors that contain a pleckstrin homology (PH) domain thought to target these proteins to cell membranes through binding polyphosphoinositides. The PH domains of all three proteins exhibit relatively high affinity for PtdIns(3,4,5)P3. Within the Grp1 family, diglycine (2G) and triglycine (3G) splice variants, differing only in the number of glycine residues in the PH domain, strongly influence the affinity and specificity for phosphoinositides. The 2G variants selectively bind PtdIns(3,4,5)P3 with high affinity,the 3G variants bind PtdIns(3,4,5)P3 with about 30-fold lower affinity and require the polybasic region for plasma membrane targeting. These ARF-GEFs share a common, tripartite structure consisting of an N-terminal coiled-coil domain, a central domain with homology to the yeast protein Sec7, a PH domain, and a C-terminal polybasic region. The Sec7 domain is autoinhibited by conserved elements proximal to the PH domain. GRP1 binds to the DNA binding domain of certain nuclear receptors (TRalpha, TRbeta, AR, ER, but not RXR), and can repress thyroid hormone receptor (TR)-mediated transactivation by decreasing TR-complex formation on thyroid hormone response elements. ARNO promotes sequential activation of Arf6, Cdc42 and Rac1 and insulin secretion. Cytohesin acts as a PI 3-kinase effector mediating biological responses including cell spreading and adhesion, chemotaxis, protein trafficking, and cytoskeletal rearrangements, only some of which appear to depend on their ability to activate ARFs. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
FNPDREGWLLKLGGRVKSWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVEDKKKPFCFELYSP
SNGQVIKACKTDSDGKVVEGNHTVYRISAASEEERDEWIKSIKASISRD
>gnl|CDD|269955 cd01253, PH_ARHGAP21-like, ARHGAP21 and related proteins pleckstrin homology (PH) domain. ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
AREGWLHYKQIVTDKGKRVSDRSWKQAWAVLRGHSLYLYKDKREQTPALSIELGSEQRISIRGCIVDIAY
SYTKRKHVFRLTTSDFSEYLFQAEDRDDMLGWIKAIQENSNAE
>gnl|CDD|269956 cd01254, PH_PLD, Phospholipase D pleckstrin homology (PH) domain. PLD hydrolyzes phosphatidylcholine to phosphatidic acid (PtdOH), which can bind target proteins. PLD contains a PH domain, a PX domain and four conserved PLD signature domains. The PLD PH domain is specific for bisphosphorylated inositides. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RNHLETFEFLEVSSLSFAPELGPKGKEGYLKKRSGGHRQGWRVCHFYCCCKAMCGRWSKRWFIVKDSFLA
YVKDPDSGAILDVFLFDQEFKVSRGGKETKYGSRHGLKITNLSRKLKLKCKSERKAKQWVESIEEA
>gnl|CDD|269957 cd01255, PH2_Tiam1_2, T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, C-terminal domain. Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. The DH domain of Tiam1 interacts with Switch regions 1 and 2 of Rac1 which blocks magnesium binding and GDP is released. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
QKIHEEYGAVFDQLIREQSGTKKEVADLSMGDLLLYGTVEWLNPPSSLGKVKKEPELAVFVFKTAVVLVC
KERSKQKKKLMGSHRKSSYEERDPFRFRHLIPVSALQVRNSNTADTESRCLWELIHTKSELEGRPEKVFQ
LCCSTPEFKNAFLKVIRSILREKVRRQSSKTE
>gnl|CDD|269958 cd01256, PH_dynamin, Dynamin pleckstrin homology (PH) domain. Dynamin is a GTPase that regulates endocytic vesicle formation. It has an N-terminal GTPase domain, followed by a PH domain, a GTPase effector domain and a C-terminal proline arginine rich domain. Dynamin-like proteins, which are found in metazoa, plants and yeast have the same domain architecture as dynamin, but lack the PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFA
LFNTDQRNVYKDYKQLELSCETQEEVDSWKASFLRAGVYPEK
>gnl|CDD|269959 cd01257, PH_IRS, Insulin receptor substrate (IRS) pleckstrin homology (PH) domain. Insulin receptor substrate (IRS) molecules are mediators in insulin signaling and play a role in maintaining basic cellular functions such as growth and metabolism. They act as docking proteins between the insulin receptor and a complex network of intracellular signaling molecules containing Src homology 2 (SH2) domains. Four members (IRS-1, IRS-2, IRS-3, IRS-4) of this family have been identified that differ as to tissue distribution, subcellular localization, developmental expression, binding to the insulin receptor, and interaction with SH2 domain-containing proteins. IRS molecules have an N-terminal PH domain, followed by an IRS-like PTB domain which has a PH-like fold. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.cytoskeletal associated molecules, and in lipid associated enzymes
TDVRKSGYLKKLKTMRKRYFVLRAESHGGPARLEYYENEKKFRRNAEPKRVIPLSSCFNINKRADAKHKH
LIALYTKDECFGLVAESEEEQDEWYQALLELQRPAR
>gnl|CDD|269960 cd01258, PHsplit_syntrophin, Syntrophin Split Pleckstrin homology (PH) domain. Syntrophins are scaffold proteins that associate with associate with the Duchenne muscular dystrophy protein dystrophin and the dystrophin-related proteins, utrophin and dystrobrevin to form the dystrophin glycoprotein complex (DGC). There are 5 members: alpha, beta1, beta2, gamma1, and gamma2) all of which contains a split (also called joined) PH domain and a PDZ domain (PHN-PDZ-PHC). The split PH domain of alpha-syntrophin adopts a canonical PH domain fold and together with PDZ forms a supramodule functioning synergistically in binding to inositol phospholipids. The alpha-syntrophin PH-PDZ supramodule showed strong binding to phosphoinositides PI(3,5)P2 and PI(5)P, modest binding to PI(3,4)P2 and PI(4,5)P2, and weak binding to PI(3)P, PI(4)P, and PI(3,4,5)P. There are a large number of signaling proteins that bind to the PDZ domain of syntrophins: nitric oxide synthase (nNOS), aquaporin-4, voltage-gated sodium channels, potassium channels, serine/threonine protein kinases, and the ATP-binding cassette transporter A1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VRSGLLELLVRERWHRVLATLSEDALTLSLEKVIPLKMCYVTRNLTMPDPENRLIELHSPDGRHSCILRC
KDSASAQSWFNAIHSNISA
>gnl|CDD|269961 cd01259, PH_APBB1IP, Amyloid beta (A4) Precursor protein-Binding, family B, member 1 Interacting Protein pleckstrin homology (PH) domain. APBB1IP consists of a Ras-associated (RA) domain, a PH domain, a family-specific BPS region, and a C-terminal SH2 domain. Grb7, Grb10 and Grb14 are paralogs that are also present in this hierarchy. These adapter proteins bind a variety of receptor tyrosine kinases, including the insulin and insulin-like growth factor-1 (IGF1) receptors. Grb10 and Grb14 are important tissue-specific negative regulators of insulin and IGF1 signaling based and may contribute to type 2 (non-insulin-dependent) diabetes in humans. RA-PH function as a single structural unit and is dimerized via a helical extension of the PH domain. The PH domain here are proposed to bind phosphoinositides non-cannonically ahd are unlikely to bind an activated GTPase. The tandem RA-PH domains are present in a second adapter-protein family, MRL proteins, Caenorhabditis elegans protein MIG-1012, the mammalian proteins RIAM and lamellipodin and the Drosophila melanogaster protein Pico12, all of which are Ena/VASP-binding proteins involved in actin-cytoskeleton rearrangement. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
NSVSCPEIEGFLYLKEDGKKSWKKRYFVLRASGLYYSPKGKSKESRDLQCLAQFDDYNVYTGLNGKKKYK
APTDFGFCLKPNKQQEKGSKDIKYLCAEDEQSRTCWLTAIRLAKYGKQLYENYR
>gnl|CDD|269962 cd01260, PH_CNK_mammalian-like, Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain. CNK family members function as protein scaffolds, regulating the activity and the subcellular localization of RAS activated RAF. There is a single CNK protein present in Drosophila and Caenorhabditis elegans in contrast to mammals which have 3 CNK proteins (CNK1, CNK2, and CNK3). All of the CNK members contain a sterile a motif (SAM), a conserved region in CNK (CRIC) domain, and a PSD-95/DLG-1/ZO-1 (PDZ) domain, and, with the exception of CNK3, a PH domain. A CNK2 splice variant CNK2A also has a PDZ domain-binding motif at its C terminus and Drosophila CNK (D-CNK) also has a domain known as the Raf-interacting region (RIR) that mediates binding of the Drosophila Raf kinase. This cd contains CNKs from mammals, chickens, amphibians, fish, and crustacea. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SRRRVSCKDLGRGDCQGWLWKKKEAKSFFGQKWKKYWFVLKGSSLYWYSNQQDEKAEGFINLPDFKIERA
SECKKKYAFKACHPKIKTFYFAAENLDDMNKWLSKLNMAINKYA
>gnl|CDD|269963 cd01261, PH_SOS, Son of Sevenless (SOS) Pleckstrin homology (PH) domain. SOS is a Ras guanine nucleotide exchange factor. SOS is thought to transmit signals from activated receptor tyrosine kinases to the Ras signaling pathway. SOS contains a histone domain, Dbl-homology (DH), a PH domain, Rem domain, Cdc25 domain, and a Grb2 binding domain. The SOS PH domain binds to phosphatidylinositol-4,5-bisphosphate (PIP2) and phosphatidic acid (PA). SOS is dependent on Ras binding to the allosteric site via its histone domain for both a lower level of activity (Ras GDP) and maximal activity (Ras GTP). The DH domain blocks the allosteric Ras binding site in SOS. The PH domain is closely associated with the DH domain and the action of the DH-PH unit gates a reciprocal interaction between Ras and SOS. The C-terminal proline-rich domain of SOS binds to the adapter protein Grb2 which localizes the Sos protein to the plasma membrane and diminishes the negative effect of the C-terminal domain on the guanine nucleotide exchange activity of the CDC25-homology domain of SOS. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
QCCNEFIMEGTLGKVGSGKRKTERHAFLFDGLLLLCKSNRRRTSTGGPKPEYRLKEKFFIRKVEINDLED
TEELKNAFEIVPRDQPSVILFAKSAEEKNNWMAALVMLN
>gnl|CDD|241293 cd01262, PH_PDK1, 3-Phosphoinositide dependent protein kinase 1 (PDK1) pleckstrin homology (PH) domain. PDK1 plays an important role in insulin and growth factor signalling cascades. It phosphorylates and activates many AGC (cAMP-dependent, cGMP-dependent, protein kinase C (PKC)) family of protein kinases members, including protein kinase B (PKB, also known as Akt), p70 ribosomal S6-kinase (S6K), serum and glucocorticoid responsive kinase (SGK), p90 ribosomal S6 kinase (RSK), and PKC. PDK1 contains an N-terminal serine/threonine kinase domain followed by a PH domain. Following binding of the PH domain to PtdIns(3,4,5)P3 and PtdIns(3,4)P2, PDK1 activates these enzymes by phosphorylating a Ser/Thr residue in their activation loop. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
QQQSENWWHFLVNGELILKMGLVDKRKGLFAKKRQLILTDGPRLYYVDPVKMVLKGEIPWSPELRPEVKN
FKTFFIHTPNRTYYLEDPEGNAKKWCKAIEEVLKLYK
>gnl|CDD|269964 cd01263, PH_anillin, Anillin Pleckstrin homology (PH) domain. Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SVEYRGFLTVFEDVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKKPIGSIDLTKCITEKVEPAPRELCAR
PNTFLLETLRPAEDDDRDDTNEKIRVLLSADTKEERIEWLSALNQTLADLR
>gnl|CDD|269965 cd01264, PH_MELT_VEPH1, Melted pleckstrin homology (PH) domain. The melted protein (also called Ventricular zone expressed PH domain-containing protein homolog 1) is expressed in the developing central nervous system of vertebrates. It contains a single C-terminal PH domain that is required for membrane targeting. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
QPVIEGQLKEKKGRWKFFKRWRTRYFTLSGAQLSYRGGKSKPDAPPIELSKIRSVKVVRKKDRSIPKAFE
IFTDDKTYVLKAKDEKNAEEWLQCLSIAVAQAHAR
>gnl|CDD|269966 cd01265, PH_TBC1D2A, TBC1 domain family member 2A pleckstrin homology (PH) domain. TBC1D2A (also called PARIS-1/Prostate antigen recognized and identified by SEREX 1 and ARMUS) contains a PH domain and a TBC-type GTPase catalytic domain. TBC1D2A integrates signaling between Arf6, Rac1, and Rab7 during junction disassembly. Activated Rac1 recruits TBC1D2A to locally inactivate Rab7 via its C-terminal TBC/RabGAP domain and facilitate E-cadherin degradation in lysosomes. The TBC1D2A PH domain mediates localization at cell-cell contacts and coprecipitates with cadherin complexes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RLCGYLNKLETRGLGLKGWKRRWFVLDESKCQLYYYRSPQDATPLGSIDLSGAAFSYDPEAEPGQFEIHT
PGRVHILKASTRQAMLYWLQALQSKRREYCNS
>gnl|CDD|241297 cd01266, PH_Gab1_Gab2, Grb2-associated binding proteins 1 and 2 pleckstrin homology (PH) domain. The Gab subfamily includes several Gab proteins, Drosophila DOS and C. elegans SOC-1. They are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. The members in this cd include the Gab1 and Gab2 proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
GGEVVCSGWLRKSPPEKKLRRYAWKKRWFVLRSGRLSGDPDVLEYYKNDHAKKPIRVIDLNLCEQVDAGL
TFNKKELENSYIFDIKTIDRIFYLVAETEEDMNKWVRNICDICGFNPTEEDTD
>gnl|CDD|241298 cd01268, PTB_Numb, Numb Phosphotyrosine-binding (PTB) domain. Numb is a membrane associated adaptor protein which plays critical roles in cell fate determination. Numb proteins are involved in control of asymmetric cell division and cell fate choice, endocytosis, cell adhesion, cell migration, ubiquitination of specific substrates and a number of signaling pathways (Notch, Hedgehog, p53). Mutations in Numb plays a critical role in disease (cancer). Numb has an N-terminal PTB domain and a C-terminal NumbF domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRKKPVRAVLWVSGDGLRVVDEKTK
GLIVDQTIEKVSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLSHAVGCAFAACLER
>gnl|CDD|269967 cd01269, PTB_TBC1D1_like, TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain. The TBC1D1-like members here include TBC1D1, TBC1D4 (also called Akt substrate of 160 kDa or AS160), and pollux (PLX), a calmodulin-binding protein, and are thought to have a role in regulating cell growth and differentiation. These proteins are thought to function as GTPase-activating protein for Rab family protein(s). They may play a role in the cell cycle and differentiation of various tissues. They all contain an N-terminal PTB domain, a calmodulin CBD domain, and a C-terminal TBC domain which is thought to be a GTPase activator protein of Rab-like small GTPases. Recently, TBC1D1 and TBC1D4 were recognized to potentially link the proximal signalling of insulin and/or exercise with GLUT4. TBC1D4 is thought to be involved in contraction-stimulated glucose uptake, but TBC1D4-independent mechanisms (potentially involving TBC1D1) are likely to be essential for most of the contraction's effect. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
DISPSNSQFFEVLYCGKIKVSHKKVPPTFIDDCLEKFRLHELEKSRSGPSSVQPTDSEENRTMLFQIGRS
ELRLISPDTKQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGGGFHFVCYVFKCQSESVVDEIMLTIK
QAF
>gnl|CDD|269968 cd01270, PTB_CAPON-like, Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) Phosphotyrosine-binding (PTB) domain. CAPON (also known as Nitric oxide synthase 1 adaptor protein, NOS1AP, encodes a cytosolic protein that binds to the signaling molecule, neuronal NOS (nNOS). It contains a N-terminal PTB domain that binds to the small monomeric G protein, Dexras1 and a C-terminal PDZ-binding domain that mediates interactions with nNOS. Included in this cd are C. elegan proteins dystrobrevin, DYB-1, which controls neurotransmitter release and muscle Ca(2+) transients by localizing BK channels and DYstrophin-like phenotype and CAPON related,DYC-1, which is functionally related to dystrophin homolog, DYS-1. Mutations in the dystrophin gene causes Duchenne muscular dystrophy. DYS-1 shares sequence similarity, including key motifs, with their mammalian counterparts. These CAPON-like proteins all have a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
SKKTYYNLVDDDYDTRIPLHNEEAFQHGITFQAKYIGSLEVPRPSSRVEIVAAMRRIRYEFKAKNIKKKK
VTITVSVDGVKVVLRKKKKKKGWTWDESKLLLMQHPIYRIFYVSHDSQDLKIFSYIARDGSSNVFKCNVF
KSKKKSQAMRIVRTIGQAFEVCHKLSLQHMQGNADDEAE
>gnl|CDD|269969 cd01271, PTB2_Fe65, Fe65 C-terminal Phosphotyrosine-binding (PTB) domain. The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The C-terminal PTB domain is responsible for APP binding. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDEEEVLVE
CRVRFLSFMGIGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK
>gnl|CDD|269970 cd01272, PTB1_Fe65, Fe65 N-terminal Phosphotyrosine-binding (PTB) domain. The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The N-terminal PTB domain was shown to interact with a variety of proteins, including the low density lipoprotein receptor-related protein (LRP-1), the ApoEr2 receptor, and the histone acetyltransferase Tip60. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPD
DRSVLHSQPIHSIRVWGVGRDNGRDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAERR
>gnl|CDD|269971 cd01273, PTB_CED-6, Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain. CED6 (also known as GULP1: engulfment adaptor PTB domain containing 1) is an adaptor protein involved in the specific recognition and engulfment of apoptotic cells. CED6 has been shown to interact with the cytoplasmic tail of another protein involved in the engulfment of apoptotic cells, CED1. CED6 has a C-terminal PTB domain, which can bind to NPXY motifs. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
IHPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQD
PKTKVIMHQFPLHRISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFL
ESNG
>gnl|CDD|269972 cd01274, PTB_Anks, Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain. Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKSTREMKKIPTIILSISYKGVKFIDA
TTKNLICEHEIRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLA
LRAQKS
>gnl|CDD|238606 cd01275, FHIT, FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH/Qxx (x, is a hydrophobic amino acid), On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified into three branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the Fhit branch, that consists of diadenosine polyphosphate hydrolases, and the GalT branch consisting of specific nucloside monophosphate transferases. Fhit plays a very important role in the development of tumours. Infact, Fhit deletions are among the earliest and most frequent genetic alterations in the development of tumours
CVFCDIPIKPDEDNLVFYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKAL
KVVYKPDGFNIGINDGKAGGGIVPHVHIHIVPRWNGDTNFMPVIIYTKVLPEDLED
>gnl|CDD|238607 cd01276, PKCI_related, Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ubiquitous HIT family of hydrolases that act on alpha-phosphates of ribonucleotides. The members of this subgroup have a conserved HxHxHxx motif (x is a hydrophobic residue) that is a signature for this family. No enzymatic activity has been reported however, for PKCI and its related members
DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEDEELLGHLLSAAAKVA
KDLGIAEDGYRLVINCGKDGGQEVFHLHLHLLGG
>gnl|CDD|238608 cd01277, HINT_subgroup, HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the superfamily of histidine triad hydrolases that act on alpha-phosphate of ribonucleotides. This subgroup includes members from all three forms of cellular life. Although the biochemical function has not been characterised for many of the members of this subgroup, the proteins from Yeast have been shown to be involved in secretion, peroxisome formation and gene expression
DCIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEELAELILAAKKVARAL
KKALKADGLNILQNNGRAAGQVVFHVHVHVIPR
>gnl|CDD|238609 cd01278, aprataxin_related, aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia syndrome. All the members of this subgroup have the conserved HxHxHxx (where x is a hydrophobic residue) signature motif. Members of this subgroup are predominantly eukaryotic in origin
LCHFCDIAKRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGRE
KLLRSDNTDPSEFRFGFHAPPFTSVSHLHLHVIA
>gnl|CDD|133387 cd01279, HTH_HspR-like, Helix-Turn-Helix DNA binding domain of HspR-like transcription regulators. Helix-turn-helix (HTH) transcription regulator HspR and related proteins, N-terminal domain. Heat shock protein regulators (HspR) have been shown to regulate expression of specific regulons in response to high temperature or high osmolarity in Streptomyces and Helicobacter, respectively. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules
LYPISVAAELLGIHPQTLRVYDRLGLVSPARTNGGGRRYSNNDLELLRQVQRLSQDEGFNLAGIKRIIEL
YPQVLLLQCRSCEHATELIGCAKPCRKE
>gnl|CDD|133388 cd01282, HTH_MerR-like_sg3, Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily. Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 3). Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
MRIGELAARTGVSVRSLRYYEEQGLLVPERSANGYRDYDEAAVDRVRQIRRLLAAGLTLEEIREFLPCLR
GGEPTFRPCPDLLAVLRRELARIDRQIADLTRSRDRLDAYLA
>gnl|CDD|238610 cd01283, cytidine_deaminase, Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. Cytidine deaminases catalyze the deamination of cytidine to uridine and are important in the pyrimadine salvage pathway in many cell types, from bacteria to humans. This family also includes the apoBec proteins, which are a mammal specific expansion of RNA editing enzymes, and the closely related phorbolins, and the AID (activation-induced) enzymes
IEAALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAV
SDEGGVWSPCGACRQVLAEFLPSRLYIIIDNPKGEEFAYTLS
>gnl|CDD|238611 cd01284, Riboflavin_deaminase-reductase, Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD (Diaminohydroxyphosphoribosylaminopyrimidine deaminase) catalyzes the deamination of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, which is an intermediate step in the biosynthesis of riboflavin.The ribG gene of Bacillus subtilis and the ribD gene of E. coli are bifunctional and contain this deaminase domain and a reductase domain which catalyzes the subsequent reduction of the ribosyl side chain
MRRALELAEKGRGLTSPNPPVGCVIVDDDGEIVGEGYHRKAGGPHAEVNALASAGEKLARGATLYVTLEP
CSHHGKTPPCVDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAAG
>gnl|CDD|238612 cd01285, nucleoside_deaminase, Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source
MRLAIELARKALAEGEVPFGAVIVDDDGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTL
YTTLEPCPMCAGALLWARIKRVVYGASDPKLGGIGFLIE
>gnl|CDD|238613 cd01286, deoxycytidylate_deaminase, Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor
DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERDDLPSGEDQKCCRTVH
AEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDDPAAAELLE
>gnl|CDD|238614 cd01287, FabA, FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the type II, fatty acid synthase system that binds ACP and catalyzes both dehydration and isomerization reactions, apparently in the same active site. The FabA structure is a homodimer with two independent active sites located at the dimer interface. Each active site is tunnel-shaped and completely inaccessible to solvent. No metal ions or cofactors are required for ligand binding or catalysis
PRLPGGQLLMLDRVTEIDPGGGTFGLGYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLI
WLGLGTGVDNPRFQGAPGGPGEWKYRGQITPHNKKVTYEVHIKEVGRDGPRPYIIADASLWVDGLRIYEA
KDIAVRLVEA
>gnl|CDD|238615 cd01288, FabZ, FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily catalyzes the dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP, the third step in the elongation phase of the bacterial/ plastid, type II, fatty-acid biosynthesis pathway
LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDFE
GKLVYFAGIDKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA
>gnl|CDD|238616 cd01289, FabA_like, Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ACP dehydratases (FabA) and beta-hydroxyacyl ACP dehydratases (FabZ). This group appears to lack the conserved active site histidine of FabA and FabZ
PWIAALIPHDGPMCLLDRVISWDDDSIHCRATVHPDPLFPLRAHGRLPAWVGIEYMAQAIAAHGGLLARQ
QGNPPRPGFLLGSRKYEAHVDRFDLGSTLLIVVAELLQGDSGLGVFECTIEDQGGVLASGRLNVYQPA
>gnl|CDD|211324 cd01291, PseudoU_synth, Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). Pseudouridine synthases contains the RsuA/RluD, TruA, TruB and TruD families. This group consists of eukaryotic, bacterial and archeal pseudouridine synthases. Some psi sites such as psi55,13,38 and 39 in tRNA are highly conserved, being in the same position in eubacteria, archeabacteria and eukaryotes. Other psi sites occur in a more restricted fashion, for example psi2604in 23S RNA made by E.coli RluF has only been detected in E.coli. Human dyskerin with the help of guide RNAs makes the hundreds of psueudouridnes present in rRNA and small nuclear RNAs (snRNAs). Mutations in human dyskerin cause X-linked dyskeratosis congenitas. Missense mutation in human PUS1 causes mitochondrial myopathy and sideroblastic anemia (MLASA)
LYKPGGDTMEAARQLAKLLGIPPKRVGYAGRKDKRAVTTQLVSNRFTITLRVKPLNLKWPEERKRALVLE
FTLPRGSYATMLLRELG
>gnl|CDD|238617 cd01292, metallo-dependent_hydrolases, Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others
FIDTHVHLDGSALRGTRLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEA
VAEAARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDESLRRVLE
EARKLGLPVVIHAGELPDPTRALEDLVALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLG
RDGEGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLGLSLEEALRLATINPARA
>gnl|CDD|238618 cd01293, Bact_CD, Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric
LLRNARLADGGTALVDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLDKTFTGGRWPNN
SGGTLLEAIIAWEERKLLLTAEDVKERAERALELAIAHGTTAIRTHVDVDPAAGLKALEALLELREEWAD
LIDLQIVAFPQHGLLSTPGGEELMREALKMGADVVGGIPPAEIDEDGEESLDTLFELAQEHGLDIDLHLD
ETDDPGSRTLEELAEEAERRGMQGRVTCSHATALGSLPEAEVSRLADLLAEAGISVVSLPPINLYLQGRE
DTTPKRRGVTPVKELRAAGVNVALGSDNVRDPWYPFGSGDMLEVANLAAHIAQLGTPEDLALALDLITGN
AARALGLEDYGIKVGCPADLVLLDAEDVAEAVARQPPRRVVIRKGRVV
>gnl|CDD|238619 cd01294, DHOase, Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric
LTIPRPDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADPGPNFTPLMT
LYLTENTTPEELREAKKKGGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKI
DVLDREAKFIPVLEPLAQRFPKLKIVLEHITTADAVEYVKSCNENVAATITPHHLLLTRDDLLGGGLNPH
LYCKPVAKRPEDREALRKAATSGHPKFFLGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNAL
DKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPEKIPFGNNGVVPFRAGETLRW
>gnl|CDD|238620 cd01295, AdeC, Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea
DAEGKYIVPGFIDAHLHIESSMLTPSEFAKAVLPHGTTTVIADPHEIANVAGVDGIEFMLEDAKKTPLDI
FWMLPSCVPATPFETSGAELTAEDIKELLEHPEVVGLGEVMDFPGVIEGDDEMLAKIQAAKKAGKPVDGH
APGLSGEELNAYMAAGISTDHEAMTGEEALEKLRLGMYVMLREGSIAKNLEALLPAITEKNFRRFMFCTD
DVHPDDLLSEGHLDYIVRRAIEAGIPPEDAIQMATINPAECYGLHDLGAIAPGRIADIVILDDLENFNIT
TVLAKGIAVVERHGKTGNIGVGFVKGFGLKEGAIASSVAHDSHNIIVIGTNDEDMALAVNRLKEIGGGIV
VVKNGKVLAELPLPIAGLMSDEPAEEVAEELKKLREALRELGYALDDPFMTLSFLSLPVIPELKITDKGL
FD
>gnl|CDD|238621 cd01296, Imidazolone-5PH, Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon
IAIRDGRIAAVGPAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILA
AGGGILSTVRATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDL
VSTFLGAHAVPPEYKGREEYIDLVIEEVLPAVAEENLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVK
IHADELSNIGGAELAAELGALSADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVP
VALGTDFNPGSSPTSSMPLVMHLACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDAP
SYEHLAYRFGVNLVEYVIKNG
>gnl|CDD|238622 cd01297, D-aminoacylase, D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics
DLVIRNGTVVDGTGAPPFTADVGIRDGRIAAIGPILSTSAREVIDAAGLVVAPGFIDVHTHYDGQVFWDP
DLRPSSRQGVTTVVLGNCGVSPAPANPDDLARLIMLMEGLVALGEGLPWGWATFAEYLDALEARPPAVNV
AALVGHAALRRAVMGLDAREATEEELAKMRELLREALEAGALGISTGLAYAPRLYAGTAELVALARVAAR
YGGVYQTHVRYEGDSILEALDELLRLGRETGRPVHISHLKSAGAPNWGKIDRLLALIEAARAEGLQVTAD
VYPYGAGSEDDVRRIMAHPVVMGGSDGGALGKPHPRSYGDFTRVLGHYVRERKLLSLEEAVRKMTGLPAR
VFGLADRGRIAPGYRADIVVFDPDTLADRATFTRPNQPAEGIEAVLVNGVPVVRDGAFTGARPGR
>gnl|CDD|238623 cd01298, ATZ_TRZ_like, TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD
ILIRNGTIVTTDPRRVLEDGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLL
RGLADDLPLMEWLKDLIWPLERLLTEEDVYLGALLALAEMIRSGTTTFADMYFFYPDAVAEAAEELGIRA
VLGRGIMDLGTEDVEETEEALAEAERLIREWHGAADGRIRVALAPHAPYTCSDELLREVAELAREYGVPL
HIHLAETEDEVEESLEKYGKRPVEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLA
SGIAPVPEMLEAGVNVGLGTDGAASNNNLDMFEEMRLAALLQKLAHGDPTALPAEEALEMATIGGAKALG
LDEIGSLEVGKKADLILIDLDGPHLLPVHDPISHLVYSANGGDVDTVIVNGRVVMEDGELL
>gnl|CDD|238624 cd01299, Met_dep_hydrolase_A, Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown
AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVEYRTIRATRQARAALRAGFTTVRDAGGADYGLL
RDAIDAGLIPGPRVFASGRALSQTGGHGDPRGLSGLFPAGGLAAVVDGVEEVRAAVREQLRRGADQIKIM
ATGGVLSPGDPPPDTQFSEEELRAIVDEAHKAGLYVAAHAYGAEAIRRAIRAGVDTIEHGFLIDDETIEL
MKEKGIFLVPTLATYEALAAEGAAPGLPADSAEKVALVLEAGRDALRRAHKAGVKIAFGTDAGFPVPPHG
WNARELELLVKAGGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDGDPLEDIAVL
>gnl|CDD|238625 cd01300, YtcJ_like, YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling
AVAVRDGRIVAVGSDAEAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALA
RIREDAAAAPPGEWILGFGWDESLLGEGRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAGITRD
TPDPPGGEIVRDADGEPTGVLVEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAADD
IEAYRRLAAAGELTLRVRVALYVSPLAEDLLEELGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPY
LDSPGTGGLLLISPEELEELVRAADEAGLQVAIHAIGDRAVDTVLDALEAALKDNPRADHRHRIEHAQLV
SPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRRLGEERAKRSYPFRSLLDAGVPVALGSDAPVAPPDPLL
GIWAAVTRKTPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV
>gnl|CDD|238626 cd01301, rDP_like, renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal dipeptidase, is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics. Although the biological function of the enzyme is still unknown, it has been suggested to play a role in the renal glutathione metabolism
PVVDGHNDLLYRLRREGKDFFTKDAGGHVDLPRLREGGVGGQVFAIFVPPGELQPTWLDALERALEQIDR
VRRLIAAYPRIFVLATSSADIRRALKEGKLAAIISIEGAHALGGDLALLRLLYRLGVRYLGLTWNGDNKF
ADGCGEKRGGGLTPFGKELVREMNRLGIIIDLSHLSERTFWDVLDISNAPVIASHSNARALCDHPRNLTD
AQLKAIAETGGVIGVNFYPAFLSPGADATLDDVVRHIDYIVDLIGIDHVGLGSDFDGIGGTPGGLEDVSD
LPNLTAELLERGYSEEEIEKIAGGNFLRV
>gnl|CDD|238627 cd01302, Cyclic_amidohydrolases, Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines
LLVLPGFIDIHVHLRDPGGTTYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYV
DFSFHAGIGPGDVTDELKKLFDAGINSLKVFMNYYFGELFDVDDGTLMRTFLEIASRGGPVMVHAERAAQ
LAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGKVNPPLRSKEDREA
LWEGVKNGKIDTIASDHAPHSKEEKESGKDIWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENP
ARIFGLYPKGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST
>gnl|CDD|238628 cd01303, GDEase, Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool
FRGTFIHTKSLPELELVEDALRVVEDGLIVVVDGNIIAAGAAETLKRAAKPGARVIDSPNQFILPGFIDT
HIHAPQYANIGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFLDELLRNGTTTACYFATIHPESTE
ALFEEAAKRGQRAIAGKVCMDRNAPEYYRDTAESSYRDTKRLIERWHGKSGRVKPAITPRFAPSCSEELL
AALGKLAKEHPDLHIQTHISENLDEIAWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLK
ERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAK
LSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLLADRMFRVESLEEALFKFLYLGDDR
NIREVYVAG
>gnl|CDD|238629 cd01304, FMDH_A, Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen
IKNGTVYDPLNGINGEKMDIFIRDGKIVESSSGAKPAKVIDASGKVVMAGGVDMHSHIAGGKVNVGRILR
PEDHRRDPVPKGALRRAGVGFSVPSTLATGYRYAEMGYTTAFEAAMPPLNARHTHEEMADTPILDKGAYP
LLGNNWFVLEYLRDGDMEKLAAYVAWTLKASKGYGIKVVNPGGTEAWGWGQNVLSLDDPVPYFDITPREI
LKGLAEANEELGLPHSIHVHCNNLGVPGNYETTLETMKAAEGVKPDPRRQVLHLTHVQFHSYGGTSWRDF
ESGAERIADYVNANDHVTIDVGQVIFGETTTMTGDGPMQFDLHGLTGLKWVNCDIELETGSGVVPFIYSP
KNPVNALQWAIGLELFLLIDDPWKVILTTDHPNGGPFTRYPRIIAWLMSKKFRAEEIATLHKWAQDRSAL
PGIDREYSLYEIAIMTRAGPAKLLGLSDKGHLGVGADADIAIYDDDPDQVDPSDYEKVEKAFSRAAYVLK
DGEIVVKDGEVVAEPWGRTYWVDVEVPSLDEEVEKDLESKFRRYYTVNLAN
>gnl|CDD|238630 cd01305, archeal_chlorohydrolases, Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. Some members of this subgroup are predicted to be chlorohyrolases
ILIPALVNAHTHLGDSAIKEVGDGLPLDDLVAPPDGLKHRLLAQADDRELAEAMRKVLRDMRETGIGAFA
DFREGGVEGIELLRRALGKLPVPFEVILGRPTEPDDPEILLEVADGLGLSSANDVDLEDILELLRRRGKL
FAIHASETRESVGMTDIERALDLEPDLLVHGTHLTDEDLELVRENGVPVVLCPRSNLYFGVGIPPVAELL
KLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRLQGYLSPLEILRMATVNAAEF
>gnl|CDD|238631 cd01306, PhnM, PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria
LPGLIDLHTDNLEKHVMPRPGVDWPMDIALAAHDRQLAAAGITTVFDALSFGDEEGGRRRLRNLRKLIDA
IRELHARGVLRADHRLHLRCELADPAVLPELESLMADPRVHLVSLMDHTPGQRQFRDLEKYREYYAKKYG
LSDEEVEEAILERKARAAAYAPANRSELAALARARGIPLASHDDDTPEHVAEAHELGVVISEFPTTLEAA
KAARELGLQTLMGAPNVVRGGSHSGNVSARELAAHGLLDILSSDYVPASLLHAAFRLADLGGWSLPEAVA
LVSANPARAVGLTDRGSIAPGKRADLILVDDMDGVPVVRTVWRGG
>gnl|CDD|238632 cd01307, Met_dep_hydrolase_B, Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown
DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVYQGGTRYGDRPDMIGVKSGVTTVVDAG
SAGADNIDGFRYTVIERSATRVYAFLNISRVGLVAQDELPDPDNIDEDAVVAAAREYPDVIVGLKARASK
SVVGEWGIKPLELAKKIAKEADLPLMVHIGSPPPILDEVVPLLRRGDVLTHCFNGKPNGIVDEEGEVLPL
VRRARERGVIFDVGHGTASFSFRVARAAIAAGLLPDTISSDIHGRNRTNGPVYALATTLSKLLALGMPLE
EVIEAVTANPARMLGLAEIGTLAVGYDADLTVFDLKDGRVELVDSEGDTLIAERLLVP
>gnl|CDD|238633 cd01308, Isoaspartyl-dipeptidase, Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides
FTLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEG
GPSTRTPEVTLSDLTTAGVTTVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSYEVPTRTITGSI
RKDLLLIDKVIGVGEIAISDHRSSQPTVEELARIAAEARVGGLLGGKAGIVHIHLGDGKRALSPIFELIE
ETEIPITQFLPTHINRTAPLFEQGVEFAKMGGTIDLTSSIDPQFRKEGEVRPSEALKRLLEQGVPLERIT
FSSDGNGSLPKFDENGNLVGLGVGSVDTLLREVREAVKCGDIPLEVALRVITSNVARILKLRKKGEIQPG
FDADLVILDKDLDINSVIAKGQIMVRNGKLLVKGTFE
>gnl|CDD|238634 cd01309, Met_dep_hydrolase_C, Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown
DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGLDEEGGVRETSDANEETDPVTPHVRAIDGIN
PDDEAFKRARAGGVTTVQVLPGSANLIGGQGVVIKTDGGTIEDMFIKAPAGLKMALGENPKRVYGGKGKE
PATRMGVAALLRDAFIKAQEYGRKYDLGKNAKKDPPERDLKLEALLPVLKGEIPVRIHAHRADDILTAIR
IAKEFGIKITIEHGAEGYKLADELAKHGIPVIYGPTLTLPKKVEEVNDAIDTNAYLLKKGGVAFAISSDH
PVLNIRNLNLEAAKAVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPTSKPEQ
VYIDGRLVY
>gnl|CDD|238635 cd01310, TatD_DNAse, TatD like proteins; E.coli TatD is a cytoplasmic protein, shown to have magnesium dependent DNase activity
LIDTHCHLDFPQFDADRDDVLARAREAGVIKIIVVGTDLKSSKRALELAKKYDNVYAAVGLHPHDADEHV
DEDLDLLELLAANPKVVAIGEIGLDYYRDKSPREVQKEVFRAQLELAKELNLPVVIHSRDAHEDVLEILK
EYGPPKRGVFHCFSGSAEEAKELLDLGFYISISGIVTFKNANELREVVKEIPLERLLLETDSPYLAPVPF
RGKRNEPAYVKHVAEKIAELKGISVEEVAEVTTENAKRLFG
>gnl|CDD|238636 cd01311, PDC_hydrolase, 2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase hydrolyzes PDC to yield 4-oxalomesaconic acid (OMA) or its tautomer, 4-carboxy-2-hydroxymuconic acid (CHM). This reaction is part of the protocatechuate (PCA) 4,5-cleavage pathway. PCA is one of the most important intermediate metabolites in the bacterial pathways for various phenolic compounds, including lignin, which is the most abundant aromatic material in nature
GAVDAHMHVFDPGYPFPPAPEKFTPYDPGIDDLRALRSTLGIDRVVIVQASIYGADNSNLLDALASNGKA
RGGATVDPRTTTDAELKEMHDAGVRGVRFNFLFGGVDNKDELDEIAKRAAELGWHVQVYFDAVDLPALLP
FLQKLPVAVVIDHFGRPDVTKGVDGAEFAALLKLIEEGNVWVKVSGPYRLSVKQEAYADVIAFARQIVAA
APDRLVWGTDWPHPRLREPDPMPDDGALLRLIPSWAPDAQLQRKNLVDNPARL
>gnl|CDD|238637 cd01312, Met_dep_hydrolase_D, Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown
DKILEVGDYEKLEKRYPGAKHEFFPNGVLLPGLINAHTHLEFSANVAQFTYGRFRAWLLSVINSRDELLK
QPWEEAIRQGIRQMLESGTTSIGAISSDGSLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRS
KSFESQLFIPAISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEESKGWFKHFWESFLKL
PKPKKLATAIDFLDMLGGLGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAG
IPVSLGTDGLSSNISLSLLDELRALLDLHPEEDLLELASELLLMATLGGARALGLNNGEIEAGKRADFAV
FELPGPGIKEQAPLQFILHAKEVRHLFISGK
>gnl|CDD|238638 cd01313, Met_dep_hydrolase_E, Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown
ALLPEGWERNVRIEVDADGRIAAVNPDTATEAVALLGGALLPGMPNLHSHAFQRAMAGLTEYRGSAADSF
WTWRELMYRFAARLTPEQIEAIARQLYIEMLLAGITAVGEFHYVHHDPDGTPYADPAELAQRVIAAASDA
GIGITLLPVLYARAGFGGPAPNPGQRRFINGYEDFLGLLEKALRAVKEHAAARIGVAPHSLRAVPAEQLA
ALAALASEKAPVHIHLAEQPKEVDDCLAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAV
VGLCPTTEANLGDGIFPAAALLAAGGRIGIGSDSNARIDLLEELRQLEYSQRLRDRARNVLATAGGSSAR
ALLDAALAGGAQALGLATGALEAGARADLLSLDLDHPSLAGALPDTLLDAWVFAAGDREVRDVVVGGR
>gnl|CDD|238639 cd01314, D-HYD, D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues
LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTA
DDFESGTRAAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV
KKGISSFKVFMAYKGLLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSR
PPEVEAEATARAIRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYWKDWFEG
AKYVCSPPLRPKEDQEALWDGLSSGTLQTVGSDHCPFNFAQKARGKDDFTKIPNGVPGVETRMPLLWSEG
VAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNAEKTISADTHHHNVDYNIFEGMKV
KGWPVVTISRGKVVVEDGELVGEKGSG
>gnl|CDD|238640 cd01315, L-HYD_ALN, L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid
DLVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWE
GFETGTKAAAAGGITTIIDMPLNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNLDQLRPLDEAG
VVGFKCFLCPSGVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASR
PVFTEVEAIQRILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEF
KCAPPIRDAANQEQLWEALENGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNK
RGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGR
VHATILRGTVVYQDGEVVGEPLGQLLL
>gnl|CDD|238641 cd01316, CAD_DHOase, The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate
RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARC
DYAFSIGATSTNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAV
LLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLPRGQYEVRPFLPTREDQEA
LWENLDYIDCFATDHAPHTLAEKTGNKPPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNL
PPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVAPPGFG
>gnl|CDD|238642 cd01317, DHOase_IIa, Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth
DAEVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKN
RAKDVGIVRVLPIGALTKGLKGEELTEIGELLEAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHP
EDPSLAGGGVMNEGKVASRLGLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGL
PVTAEVTPHHLLLDDEALESYDTNAKVNPPLRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAE
APPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPPGRLEVGAPADLVLFDPDAEWIVDE
ETFRSKSKNTPFDGQKLKGRVLAT
>gnl|CDD|238643 cd01318, DHOase_IIb, Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family
GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVV
DYGLYFGVTGSEDLEELDKAPPAGYKIFMGDSTGDLLDDEETLERIFAEGSVLVTFHAEDEDRLRENRKE
LKGESAHPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVEVTPHHLFLDVED
YDRLGTLGKVNPPLRSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLMLT
LVNKGILSLSRVVRLTSHNPARIFGIKNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEV
TGFPVMTIVRG
>gnl|CDD|238644 cd01319, AMPD, AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at position 6 of the adenine nucleotide ring. AMPD is a diverse and highly regulated eukaryotic key enzyme of the adenylate catabolic pathway
FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSAC
MNQKHLLRFIKKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKY
NPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLF
SPNVRWLIQIPRLYDVYKKSGIVNSFQEMLENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESKSE
RRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFRKARGFNTFVLRPHCGEAGDIDHLASAFLLAH
GISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFKRGLNVSLSTDDPLQFHFTKEP
LMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTNVPQIRMAYRYE
TLCEEL
>gnl|CDD|238645 cd01320, ADA, Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the irreversible hydrolytic deamination of both adenosine, as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively. ADA plays an important role in the purine pathway. Low, as well as high levels of ADA activity have been linked to several diseases
NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVELLELVVAAYNFSDLQDFLAKYDFGLSVLQTEED
FERLAYEYLEDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSP
ESAQETLELALKYRDKGVVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLG
AERIGHGIRAIEDPELVKRLAERNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGT
YLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEKAELLKRI
>gnl|CDD|238646 cd01321, ADGF, Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors with sequence similarty to adenosine deaminase
PGMHFFKAKDLIENSTLFKIIQKMPKGALLHVHDTAMVSSDWLIKNATYRFEQIFDIIDGLLTYLPIFRD
YYRRLLEELYEDNVQYVELRSSFSPLYDLDGREYDYEETVQLLEEVVEKFKKTHPDFIGLKIIYATLRNF
NDSEIKESMEQCLNLKKKFPDFIAGFDLVGQEDAGRPLLDFLPQLLWFPKQCAEIPFFFHAGETNGDGTE
TDENLVDALLLNTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPV
VISSDDPGFWGAKGLSHDFYQAFMGLAPADAGLRGLKQLAENSIRYSALSDQEKDEAVAKWEKKW
>gnl|CDD|238647 cd01324, cbb3_Oxidase_CcoQ, Cytochrome cbb oxidase CcoQ. Cytochrome cbb3 oxidase, the terminal oxidase in the respiratory chains of proteobacteria, is a multi-chain transmembrane protein located in the cell membrane. Like other cytochrome oxidases, it catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Found exclusively in proteobacteria, cbb3 is believed to be a modern enzyme that has evolved independently to perform a specialized function in microaerobic energy metabolism. The cbb3 operon contains four genes (ccoNOQP or fixNOQP), with ccoN coding for subunit I. Instead of a CuA-containing subunit II analogous to other cytochrome oxidases, cbb3 utilizes subunits ccoO and ccoP, which contain one and two hemes, respectively, to transfer electrons to the binuclear center. ccoQ, the fourth subunit, is a single transmembrane helix protein. It has been shown to protect the core complex from proteolytic degradation by serine proteases. See cd00919, cd01322, or cd01323 for more information on cbb3 oxidase
MDIGETLRGLADSWGLLYLALFFLGVVVWAFRPGRKKAFDEAANLPLA
>gnl|CDD|238648 cd01327, KAZAL_PSTI, Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins
EVFGCPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC
>gnl|CDD|238649 cd01328, FSL_SPARC, Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins
PCENHHCGAGKVCEVDDENTPKCVCIDPCPEEVDDRRKVCTNDNETFDSDCELYRTRCLCKGGKKGCRGP
KYQHLHLDYYGECKEI
>gnl|CDD|238650 cd01330, KAZAL_SLC21, The kazal-type serine protease inhibitor domain has been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters), which may regulate the specificity of anion uptake. The KAZAL_SLC21 domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins
LTSSCNSNCSCSESAYSPVCGENGITYFSPCHAGCTNSTGSGGSKIYTNCSCVG
>gnl|CDD|176461 cd01334, Lyase_I, Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions. The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits
IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGELN
GGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHEL
AAWAAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGFFGPAPNSTQAVSDRDFLVE
LLSALALLAVSLSKIANDLRLLSSGEFGEVELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALL
EALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLEGLEVN
>gnl|CDD|100105 cd01335, Radical_SAM, Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin
LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKK
ELPGFEISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFKERLEALKELREAGLG
LSTTLLVGLGDEDEEDDLEELELLAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEKLLRLIAA
>gnl|CDD|133421 cd01336, MDH_cytoplasmic_cytosolic, Cytoplasmic and cytosolic Malate dehydrogenases. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. Members of this subfamily are eukaryotic MDHs localized to the cytoplasm and cytosol. MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
EPIRVLVTGAAGQIAYSLLPMIAKGDVFGPDQPVILHLLDIPPALKALEGVVMELQDCAFPLLKSVVATT
DPEEAFKDVDVAILVGAMPRKEGMERKDLLKANVKIFKEQGEALDKYAKKNVKVLVVGNPANTNALILLK
YAPSIPKENFTALTRLDHNRAKSQIALKLGVPVSDVKNVIIWGNHSSTQYPDVNHATVELNGKGKPAREA
VKDDAWLNGEFISTVQKRGAAVIKARKLSSAMSAAKAICDHVHDWWFGTPEGEFVSMGVYSDGSYGVPEG
LIFSFPVTCKNGKWKIVQGLSIDDFSREKIDATAKELVEEKETAL
>gnl|CDD|133422 cd01337, MDH_glyoxysomal_mitochondrial, Glyoxysomal and mitochondrial malate dehydrogenases. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. Members of this subfamily are localized to the glycosome and mitochondria. MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
VKVAVLGAAGGIGQPLSLLLKLNPLVSELALYDIVNTPGVAADLSHINTPAKVTGYLGPEELKKALKGAD
VVVIPAGVPRKPGMTRDDLFNINAGIVRDLATAVAKACPKALILIISNPVNSTVPIAAEVLKKAGVYDPK
RLFGVTTLDVVRANTFVAELLGLDPAKVNVPVIGGHSGVTILPLLSQCQPPFTFDQEEIEALTHRIQFGG
DEVVKAKAGAGSATLSMAYAGARFANSLLRGLKGEKGVIECAYVESDVTEAPFFATPVELGKNGVEKNLG
LGKLNDYEKKLLEAALPELKKNIEKGVDFV
>gnl|CDD|133423 cd01338, MDH_chloroplast-like, Chloroplast-like malate dehydrogenases. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. Members of this subfamily are bacterial MDHs, and plant MDHs localized to the chloroplasts. MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
KPVRVAVTGAAGQIGYSLLFRIASGEMFGPDQPVILQLLELPQALKALEGVAMELEDCAFPLLAEIVITD
DPNVAFKDADWALLVGAKPRGPGMERADLLKANGKIFTAQGKALNDVASRDVKVLVVGNPCNTNALIAMK
NAPDIPPDNFTAMTRLDHNRAKSQLAKKAGVPVTDVKNMVIWGNHSPTQYPDFTNATIGGKPAAEVINDR
AWLEDEFIPTVQKRGAAIIKARGASSAASAANAAIDHMRDWVLGTPEGDWFSMAVPSDGSYGIPEGLIFS
FPVRSKGGGYEIVEGLEIDDFAREKIDATLAELLEEREAVKH
>gnl|CDD|133424 cd01339, LDH-like_MDH, L-lactate dehydrogenase-like malate dehydrogenase proteins. Members of this subfamily have an LDH-like structure and an MDH enzymatic activity. Some members, like MJ0490 from Methanococcus jannaschii, exhibit both MDH and LDH activities. Tetrameric MDHs, including those from phototrophic bacteria, are more similar to LDHs than to other MDHs. LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
ISIIGAGNVGATLAQLLALKELGDVVLLDIVEGLPQGKALDISQAAPILGSDTKVTGTNDYEDIAGSDVV
VITAGIPRKPGMSRDDLLGTNAKIVKEVAENIKKYAPNAIVIVVTNPLDVMTYVAYKASGFPRNRVIGMA
GVLDSARFRYFIAEELGVSVKDVQAMVLGGHGDTMVPLPRYSTVGGIPLTELITKEEIDEIVERTRNGGA
EIVNLLKTGSAYYAPAAAIAEMVEAILKDKKRVLPCSAYLEGEYGIKDIFVGVPVVLGKNGVEKIIELDL
TDEEKEAFDKSVESVKELID
>gnl|CDD|238651 cd01341, ADP_ribosyl, ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. Poly(ADP-ribose) polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length in part through poy(ADP_ribosylation) of telomere repeat binding factor 1 (TRF1). Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active
FLFHGSPPGNVISILKLGLRPASYGVLLNGGMFGKGIYSAPNISKSNGYSVGCDGQHVFQNGKPKVCGRE
LCVFGFLTLGVMSGATEESSRVLFPRNFRGATGAEVVDLLVAMCRDALLLPREYIIFEPYSQVSIRY
>gnl|CDD|293888 cd01342, Translation_Factor_II_like, Domain II of Elongation factor Tu (EF-Tu)-like proteins. Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits
LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGV
KDILTGDTLT
>gnl|CDD|238653 cd01343, PL1_Passenger_AT, Pertactin-like passenger domains (virulence factors), C-terminal, subgroup 1, of autotransporter proteins of the type V secretion system of Gram-negative bacteria. This subgroup includes the passenger domains of Neisseria and Haemophilus IgA1 proteases, SPATEs (serine protease autotransporters secreted by Enterobacteriaceae), Bordetella pertacins, and nonprotease autotransporters, TibA and similar AIDA-like proteins
GRLVSDGGNITAGDNAQLTLGGGALYGSSVTLTNGAVLDAGNANLSAAASYATLSGSNIRGTVVLGAGQP
LQALAELLLGGNAAWTGAIQGLNATVSLNLNSVWTLTGDSNVNNLTLNGGTVDFNGPSAGKFNTLTVNTL
SGNGTFVMRTDLAGGQGDKLVVTGSATGDFNLLVVNTGKEPTSGLNLTLVSTPKGGDAEFTLANGTVDLG
AYRYTLVKDGNGNWTLTGPKKES
>gnl|CDD|238654 cd01344, PL2_Passenger_AT, Pertactin-like passenger domains (virulence factors), C-terminal, subgroup 2, of autotransporter proteins of the type V secretion system of Gram-negative bacteria. This subgroup includes the passenger domains of the nonprotease autotransporters, Ag43, AIDA-1 and IcsA, as well as, the less characterized ShdA, MisL, and BapA autotransporters
GTITGNGGWKLGGDLTLGGGALTLTTSLTLTGTLLTGGAGTLTLDSTSTWNITGTSTLNVGNLTNAGTID
LGNGSPAGGTLTITGNYTGNGGTLRLNTVLGDDDSPTDRLVIDGDASGTTRVAVNNAGGSGATTGNGIEV
VEVGGTSSNGAFSLAGRVVAGAYEYRLYRGGVSGNDGNWYLRSELAPP
>gnl|CDD|238655 cd01345, OM_channels, Porin superfamily. These outer membrane channels share a beta-barrel structure that differ in strand and shear number. Classical (gram-negative) porins are non-specific channels for small hydrophillic molecules and form 16 beta-stranded barrels (16,20), which associate as trimers. Maltoporin-like channels have specificities for various sugars and form 18 beta-stranded barrels (18,22), which associate as trimers. Ligand-gated protein channels cooperate with a TonB associated inner membrane complex to actively transport ligands via the proton motive force and they form monomeric, (22,24) barrels. The 150-200 N-terminal residues form a plug that blocks the channel from the periplasmic end
GSWDAYFNPVLNIRQGLGQTPDDDLTLKXGYARANKAPSLYQTNPGNDDAKAETSDGKEIGLEFKRDGGW
LAGVTYARNDYTNKIEAGYVAVGQNAVGTDLYQWDNVPKAVVEGLEGSLNVPVSETVXWTNNYTYXLKSE
NKTTRLSIIPEYTLNVTLSWQAREDLSXQVTYTWYKKQQPKKYKEIDPYSIVGLSATWDVTKNVSLTGGY
DNLFDKRLWRAGNAQTTGDANYIAGAGAYTYNEPGDTWYXGVN
>gnl|CDD|238656 cd01346, Maltoporin-like, The Maltoporin-like channels (LamB porin) form a trimeric structure which facilitate the diffusion of maltodextrins and other sugars across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an 18-strand antiparallel beta-barrel (18,22). Loop 3 folds into the core to constrict pore size. Long irregular loops are found on the extracelllular side, while short turns are in the periplasm.Tightly-bound water molecules are found in the eyelet of the passage, and only substrates that can displace and replace the broken hydrogen bonds are likely to enter the pore. In the MPR structure, loops 4,6, and 9 have the greatest mobility and are highly variable; these are postulated to attract maltodextrins
FEFHGYARSGVGYSDGGGAQTCFAGGGGGSVGRLGNECDTYFELGLKKEVYNDNGVTADFVVMVAQGNGQ
SNDWTFAADDGDLNVRQAYVELKGLLPFLPGATFWAGKRFYRRHDIHILDFYYWNTSGTGAGIENVQLGD
GKLSFALVRSDNQDDDTTYDSDTNLNAIDLRYAGIPLNPGGSLQLGGKYGFANDSDSGYYDAKDGWMLTA
LHHQKDFLGGFNKTALQYGTGAGSGQGGSGGDYGGLDDGASSWRLAEYGEWQLGDRFGGGVALVYQRGND
PYGYGDDYQWASVGVRPAYKWSDNFKTAFEVGYDTVKADDGGGVTDDGSLYKLTVAPTFSAGTDFWSRPE
LRFYATYSNWNDAALRAFTAFGSAFGNSKDGWNFGVQVEAWW
>gnl|CDD|238657 cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore
SVSVITAEDIEKQPATSLADLLRRIPGVSVTRGGGGGGSTISIRGFGPDRTLVLVDGLPLASSNYGRGVD
LNTIPPELIERVEVLKGPSSALYGSGAIGGVVNIITKRPTDEFGGSVTAGYGSDNSGSSGGGGFDVSGAL
ADDGAFGARLYGAYRDGDGTIDGDGQADDSDEERYNVAGKLDWRPDDDTRLTLDAGYQDQDADGPGGTLP
ANGTGSSLGGGPSSNTNGDRDWDYRDRYRKRASLGLEHDLNDTGWTLRANLSYSYTDNDGDPLILNGGNN
AAGGDLGRSGYSSERDTTQLGFDAGLNAPFGTGPVAHTLTLGVEYRREELDEKQTALYAQDTIELTDDLT
LTLGLRYDHYDQDSKDTIAGGTTAKKSYSHWSPSLGLVYKLTDGLSLYASYSQGFRAPSLGELYGGGSHG
GTAAVGNPNLKPEKSKQYELGLKYDPGDGLTLSAALFRIDIKNEIVSTPTNTGLGLVTVYVNGGKARIRG
VELEASYDLTDGLGLTGSYTYTDTEVKRTDGATTGNRLPGIPKHTANLGLDYELPDEGLTAGGGVRYRGK
QYADTANGNNTVKVPGYTLVDLSASYQFTKNLTLRLGVNNLFDKDYYTSLSVRGSGLYGYYGPGRTYYLS
VSYKF
>gnl|CDD|153129 cd01351, Aconitase, Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Aconitase catalytic domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. Aconitase, in its active form, contains a 4Fe-4S iron-sulfur cluster; three cysteine residues have been shown to be ligands of the 4Fe-4S cluster. This is the Aconitase core domain, including structural domains 1, 2 and 3, which binds the Fe-S cluster. The aconitase family also contains the following proteins: - Iron-responsive element binding protein (IRE-BP), a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid
RVMLQDATGPMAMKAFEILAALGKVADPSQIACVHDHAVQLEKPVNNEGHKFLSFFAALQGIAFYRPGVG
IIHQIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPG
VTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATG
RPLLKNLWLAFPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEGTKIDQVLIGSCTNNR
YSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADG
EVGVSSGNRNFPGRLGTYERHVYLASPELAAATAIAGKI
>gnl|CDD|153130 cd01355, AcnX, Putative Aconitase X catalytic domain. Putative Aconitase X catalytic domain. It is predicted by comparative genomic analysis. The proteins are mainly found in archaea and proteobacteria. They are distantly related to Aconitase family of proteins by sequence similarity and seconary structure prediction. The functions have not yet been experimentally characterized. Thus, the prediction should be treated with caution
EAILNGEYGEAVAKAMEILVAVGELYGAERLIDIKSAHISGVSYKTIGDAGLEFLERLADQGAKVAVPTT
LNPISMDLHWRELGVDEEFAEKQARLVKAYKAMGVDPTFTCTPYQLENLPKKGEHIAWAESSAVVYANSV
LGARTNREGGPSALAAAITGRTPEYGVHLDENRKARLIVEVEAAEPLDDSDYGALGYLVGKIAGDRIPVI
TGLDARPSEDELKALGAAMATSGSVAMFHIVGVTPEAPTLGLDAAETVELTRADLDEARENLNADGSEPD
LVVLGCPHASLEELRKLADLLAGRRVAPSVPLYVTTSRAVYAKRMGYVDVIEKLGARVLTDTCMVVSPVN
EPNGYKNVMTNSGKAAHYLPGNTGVEVAFGELEDCIEAA
>gnl|CDD|238658 cd01356, AcnX_swivel, Putative Aconitase X swivel domain. It is predicted by comparative genomic analysis. The proteins are mainly found in archaea and proteobacteria. They are distantly related to Aconitase family of proteins by sequence similarity and seconary structure prediction. The functions have not yet been experimentally characterized. Thus, the prediction should be treated with caution
IVRGRVEGEALVSREPLSFWGGVDPETGKVIDPHHPLYGESIAGKVLVLPGGKGSTVGSYVLYELARNGT
APAAIVFEEAEPILAAGAILAGIPLVDSLPEVLFEALKDGDRVRGGGEVLAPD
>gnl|CDD|176462 cd01357, Aspartase, Aspartase. This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid
RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIV
KACDEIIAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVY
PTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARI
YKARERLREVNLGGTAIGTGINAPPGYIELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLA
VKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQ
LELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVENSIGIVTALNPYIGYEAAAEIA
KEALETGRSVRELVLEEGLLTEEELDEILS
>gnl|CDD|176463 cd01359, Argininosuccinate_lyase, Argininosuccinate lyase (argininosuccinase, ASAL). This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria
SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRL
IERIGDVGGKLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQP
ITFGHYLLAYAEMLERDLERLADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDR
DFVLEFLSAAALLMVHLSRLAEDLILWSTQEFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGA
LAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLLTGVISTLTVNPERMREAAEAGFSTATDLAD
YLVREKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDVREALDPENSVERRTSYGGTA
PAEVREQIARARALL
>gnl|CDD|176464 cd01360, Adenylsuccinate_lyase_1, Adenylsuccinate lyase (ASL)_subgroup 1. This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP)
RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKAKFDVERVKEIEAETKHDVIAF
VTAIAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGI
HAEPTTFGLKFALWYAEFKRHLERLKEARERILVGKISGAVGTYANLGPEVEERVAEKLGLKPEPISTQV
IQRDRHAEYLSTLALIASTLEKIATEIRHLQRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARV
IRSNVIPALENVALWHERDISHSSVERVILPDATILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIF
SQRVLLALVEKGMSREEAYEIVQREYYLKHVDEIFKR
>gnl|CDD|176465 cd01362, Fumarase_classII, Class II fumarases. This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle
RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIV
QAADEVIAGKLDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTF
PTAMHIAAALALQERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIAR
IEAALPRLYELALGGTAVGTGLNAHPGFAEKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTL
AVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGKVNPTQCEALTMVAAQVMGNDAAITIAGSSG
NFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLERSLMLVTALNPHIGYDKAAKI
AKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM
>gnl|CDD|276814 cd01363, Motor_domain, Myosin and Kinesin motor domain. Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros
VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMK
GVIPYLASVAFNGINKGETEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDI
AGFEIINESLNTLMNVLRATRPHFVRCISP
>gnl|CDD|276815 cd01364, KISc_BimC_Eg5, Kinesin motor domain, BimC/Eg5 spindle pole proteins. Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward
GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGGLADKSSTKTYTFDMVFGPEAKQIDVYRSV
VCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDRSPNEEYTWELDPLAGIIPRTLHQLFEKLEDNGTEYS
VKVSYLEIYNEELFDLLSPSSDVSERLRMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAA
TLMNAQSSRSHSVFSITIHIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTL
GRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEV
NQK
>gnl|CDD|276816 cd01365, KISc_KIF1A_KIF1B, Kinesin motor domain, KIF1_like proteins. Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively
ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKATREVPKSFSFDYSYWSHDSEDPNY
ASQEQVYEDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMS
YSVEVSYMEIYNEKVRDLLNPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVA
ATNMNDTSSRSHAVFTIVLTQKRHDAETNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLT
TLGKVISALADMSSGKSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADR
AKKIVNRAVVN
>gnl|CDD|276817 cd01366, KISc_C_terminal, Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward
KGNIRVFCRVRPLLPSEENEDTSHITFPDEDGQTIELTSIGAKQKEFSFDKVFDPEASQEDVFEEVSPLV
QSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETI
RDLLAPGNAPQKKLEIRHDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVF
ILHISGRNLQTGEISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYR
NSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL
>gnl|CDD|276818 cd01367, KISc_KIF2_like, Kinesin motor domain, KIF2-like group. Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward
KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKVDLTKYIENHTFRFDYVFDESSSNETVYRS
TVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALAARDVFRLLNKLPYKDNLGVTVS
FFEIYGGKVFDLLNRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRS
HAILQIILRDRGTNKLHGKLSFVDLAGSERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIP
FRGSKLTQVLKDSFIGENSKTCMIATISPGASSCEHTLNTLRYADRVK
>gnl|CDD|276819 cd01368, KISc_KIF23_like, Kinesin motor domain, KIF23-like subgroup. Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward
DPVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQK
EFFQGTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGGYSVFVSYIEIY
NEYIYDLLEPSPSSPTKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRES
SRSHSVFTIKLVQAPGDSDGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGT
CIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ
>gnl|CDD|276820 cd01369, KISc_KHC_KIF5, Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward
ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSETGKTFSFDRVFDPNTTQEDVYNFAAKPIVD
DVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEK
IRDLLDVSKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLIN
VKQENVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDS
KLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI
>gnl|CDD|276821 cd01370, KISc_KIP3_like, Kinesin motor domain, KIP3-like subgroup. Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward
SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGFFHGGSNNRDRRKRRNKELKYVFDRVFD
ETSTQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEK
EFEVSMSYLEIYNETIRDLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTD
ANATSSRSHAVLQITVRQQDKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGN
CINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI
>gnl|CDD|276822 cd01371, KISc_KIF3, Kinesin motor domain, kinesins II or KIF3_like proteins. Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward
ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKATANEPPKTFTFDAVFDPNSKQLDVYDETA
RPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLE
IYNEEIRDLLGKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSH
AIFTITIECSEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGK
STHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI
>gnl|CDD|276823 cd01372, KISc_KIF4, Kinesin motor domain, KIF4-like subfamily. Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward
SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLF
EGYNATVLAYGQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEE
IRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIF
TITLEQTKKNGPIAPMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISAL
GDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK
>gnl|CDD|276824 cd01373, KISc_KLP2_like, Kinesin motor domain, KIF15-like subgroup. Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward
DAVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPPKTFTFDHVADSNTNQESVFQSVGKPIVESC
LSGYNGTIFAYGQTGSGKTYTMWGPSESDNESPHGLRGVIPRIFEYLFSLIQREKEKAGEGKSFLCKCSF
LEIYNEQIYDLLDPASRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRS
HAVFTCTIESWEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVA
HGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNEDT
>gnl|CDD|276825 cd01374, KISc_CENP_E, Kinesin motor domain, CENP-E/KIP2-like subgroup. Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward
KITVTVRVRPLNSREIGINEQVAWEIDNDTIYLVEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALE
GYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPT
SQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGE
LEEGTVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGGHIPYRDSKLTR
ILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI
>gnl|CDD|276826 cd01375, KISc_KIF9_like, Kinesin motor domain, KIF9-like subgroup. Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward
KVQAFVRVRPTDDFAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDWSFKFDGVLHNASQELVYETVAK
DVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIY
NEQLYDLLSTLPYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSS
RSHCIFTIHLEAHSRTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD
KDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK
>gnl|CDD|276827 cd01376, KISc_KID_like, Kinesin motor domain, KIF22/Kid-like subgroup. Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward
NVRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPRNHGETLKYQFDAFYGEESTQEDIYAREVQPIV
PHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEAWALSFTMSYLEIYQEKILDL
LEPASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQR
ERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTR
LLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR
>gnl|CDD|276951 cd01377, MYSc_class_II, class II myosins, motor domain. Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQD
RENQSILITGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKGTLEDQILQANPILEAFGNAKTVRNN
NSSRFGKFIRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSY
YFFLSQGELTIDGVDDAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTE
EADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDT
KSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGLDLQP
TIDLIEKPNMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKKSEAHFILKHYAGDVEYNI
DGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSFRTVSQLHKEQLNKLMTTLR
STHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKG
FDDGKAACEKILKALQLDPELYRIGNTKVFFK
>gnl|CDD|276829 cd01378, MYSc_Myo1, class I myosin, motor domain. Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSE
KENQCVIISGESGAGKTEASKRIMQYIAAVSGGSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFG
KYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKS
GCFDVDGIDDAADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISDTSVLDFVAY
LLGVDPDQLEKALTHRTIETGGGGRSVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGG
KKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTPIKYFNNKIICDL
IEEKPPGIFAILDDACLTAGDATDQTFLQKLNQLFSNHPHFECPSGHFELRRGEFRIKHYAGDVTYNVEG
FLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCI
KPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVES
ILKDLNIPPEEYQMGKTKIFIR
>gnl|CDD|276830 cd01379, MYSc_Myo3, class III myosin, motor domain. Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQ
KKNQCIVISGESGAGKTESANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYL
EMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAKYKLPENKPPRYLQNDGL
TVQDIVNNSGNREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQTDKSSRISNPEA
LNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPD
RSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEDNR
PLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKSKYYWRPKSNALSFGIHHYAGKVLYDASGF
LEKNRDTLPPDVVQLLRSSENPLVRQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKV
LKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVANRENCRLILERLKLDNWALGKTKV
FLK
>gnl|CDD|276831 cd01380, MYSc_Myo5, class V myosin, motor domain. Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMAR
DEKNQSIIVSGESGAGKTVSAKYAMRYFATVGGSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFG
KYIEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQG
GSPVIDGVDDAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIAC
ELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQ
HSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFIDFYDNQPCIDLI
EGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKHFKKPRFSNTAFIVKHFADDVEYQVEGFLEKN
RDTVSEEHLNVLKASKNRKKTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRA
CGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR
>gnl|CDD|276832 cd01381, MYSc_Myo7, class VII myosin, motor domain. These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRN
KRDQCVVISGESGAGKTESTKLILQYLAAISGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYID
IHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLT
CEGRDDAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDNLDASEVRDPPNLERAAKL
LEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSR
TSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQHIEFVDNQDVLDLIA
LKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGINHFAGVVFYDTRGFLEKNR
DTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNE
YKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCA
VLGGDADYQLGKTKIFLK
>gnl|CDD|276833 cd01382, MYSc_Myo6, class VI myosin, motor domain. Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKV
LKQSQSIIVSGESGAGKTESTKYILRYLTESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKF
VEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLDDVGDFIRMD
KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQSLEYAAELLGLDQDELRVSL
TTRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFETSSYFIGVLDIAGF
EYFEVNSFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLD
EESKLPKPSDQHFTSAVHQKHKNHFRLSIPRKSKLKIHRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDA
LHASLESLICESKDKFIRSLFESSTNNNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIK
PNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLARLDPRLFCKALFK
ALGLNENDFKFGLTKVFFR
>gnl|CDD|276834 cd01383, MYSc_Myo8, class VIII myosin, motor domain. These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDSPHVYAVADTAYREMMRDEI
NQSIIISGESGAGKTETAKIAMQYLAALGGGSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIH
FDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTID
GVDDAKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCN
ANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISIL
DIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDFEDNQECLDLIEKKPLGL
ISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGERGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQ
LLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNN
KQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLSTSVAILQQF
NILPEMYQVGYTKLFFR
>gnl|CDD|276835 cd01384, MYSc_Myo11, class XI myosin, motor domain. These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle
PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMIN
EGKSQSILVSGESGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRF
GKFVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQ
SKCFELDGVDDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHL
KAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDP
NSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFVDNQDVLD
LIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLSRTDFTIDHYAGDVTYQTDLFLDK
NKDYVVAEHQALLNASKCPFVAGLFPPLPREGTSSSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKP
NNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAACKKILE
KAGLKGYQIGKTKVFLR
>gnl|CDD|276836 cd01385, MYSc_Myo9, class IX myosin, motor domain. Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRK
KKNQCIVISGESGSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKF
IQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDC
YTLEGEDEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIIS
ELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALLNKKDLEE
AKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEYTDNTGCLQ
LISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGKVKYQIKDFREK
NLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFREAGRRRAQRTAGHSLTLHDRT
TKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLET
VRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK
>gnl|CDD|276837 cd01386, MYSc_Myo18, class XVIII myosin, motor domain. Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMS
RRDQSIVLLGRSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQL
FSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPL
QKPEDKQKAAAAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAY
LLGCTLEELSSAIFKHHLSGGPQQSTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLIN
RSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEV
DFDLPELSPGALVALIDQAPQQALVRSDLRDEDRRGLLWLLDEEALYPGSSDDTFLERLFSHYGDKEGGK
GHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKETAAVKRKSPCLQIKF
QVDALIDTLRRTGLHFVHCLLPQHNAGKDERSTSSPAAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPD
HMPLGEFRRRFQVLAPPLTKKLGLNSEVADERKAVEELLEELDLEKSSYRIGLSQVFFR
>gnl|CDD|276838 cd01387, MYSc_Myo15, class XV mammal-like myosin, motor domain. The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDA
KQNQCVVISGESGSGKTEATKLIMQYLAAVNQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYL
EVFFEGGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCE
IAGKSDADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQEGVSVGSDAEIQWVAH
LLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLS
IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDWTEIAFADNQPVINLISKK
PVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMPLPEFTIKHYAGQVWYQVHGFLDKNRDQL
RQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPW
FVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGDM
CVSLLSRLCTVTPKDMYRLGATKVFLR
>gnl|CDD|438790 cd01388, HMG-box_SoxB, high mobility group (HMG)-box found in group B SRY-related high-mobility group (HMG) box (Sox) transcription factors. SoxB transcription factors play critical roles in the regulation of neurogenesis. They can be divided into two main subgroups, SoxB1 (Sox-1/Sox-2/Sox-3) and SoxB2 (SOX-14/SOX-21). SoxB1 proteins suppress neurogenesis by maintaining neural cells in an undifferentiated state. SoxB2 proteins may have the opposite activity and promote neuronal differentiation. SOX-1 is involved in the regulation of embryonic development and cell fate determination. It also acts as a tumor suppressor that plays an anti-tumorigenicity role in different cells and its expression is inhibited in a variety of cancers. SOX-2 plays an important role in various phases of embryonic development, including cell fate and differentiation. Its overexpression and gene amplification may be associated with tumor aggression and metastasis in various cancer types, including breast, prostate, lung, ovarian and colon cancer. SOX-3 is required during the formation of the hypothalamic-pituitary axis. It plays a role in both normal neural development and carcinogenesis. SOX-14, also called SOX-28, acts as a negative regulator of transcription. It is mainly involved in the regulation of neural development. It can also promote proliferation and invasion capacity of cervical cancer cells by activating the Wnt/beta-catenin pathway. SOX-21, also called SOX-A, or SOX-25, promotes the progression of vertebrate neurogenesis
DRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSEAEKRPFIDEAKRLRALHMKEHPDY
KYRPRRKTKT
>gnl|CDD|438791 cd01389, HMG-box_ROX1-like, high mobility group (HMG)-box found in Saccharomyces cerevisiae repressor ROX1 and similar proteins. This family includes class I members of the HMG-box superfamily of DNA-binding proteins, including Saccharomyces cerevisiae repressor ROX1, Schizosaccharomyces pombe mating-type M-specific polypeptide Mc (mat-Mc), Schizosaccharomyces pombe transcription factor ste11, Podospora anserina MAT+ sexual cell fertilization-promoting factor (FPR1), Podospora anserina sporulation minus regulator 2 (SMR2) and Candida albicans repressor of filamentous growth 1 (RFG1). These proteins contain a single HMG box, and bind the minor groove of DNA in a highly sequence-specific manner. ROX1, also called heme-dependent repression factor, or hypoxic function repressor, is a transcription factor that represses the expression of HEM13, COX5B, ANB1, CYC7 or AAC3. It binds to the DNA sequence 5'-RRRTAACAAGAG-3'. mat-Mc belongs to the mating type protein family, which contains sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. mat-Mc is a positive regulator of MFM genes and is required for conjugation and efficient meiosis. Its HMG box recognizes the DNA sequence 5'-AACAAAG-3'. Ste11 is a key transcription factor for sexual development. It activates the transcription of the matp, matm, mei2, mfm, ste6 and rgs1 genes. It binds specifically to a DNA fragment carrying a 10-base motif 5'-TTCTTTGTTY-3'. FPR1 controls fertilization, probably by determining the mating type. SMR2 is a transcription factor that is required for post-fertilization events. It is required for the developmental events that occur in the female organ after fertilization. RFG1 is a transcription regulator that functions in both the positive and negative regulation of filamentous growth, depending upon environmental conditions
IPRPPNAFILFRKEKHKQLRAQNPGLTNSEISKIIGKMWKNLSEEEKEPYKELAEEEKEEHKLKYPDYKY
QP
>gnl|CDD|438792 cd01390, HMG-box_NHP6-like, high mobility group (HMG)-box found in Saccharomyces cerevisiae non-histone chromosomal proteins NHP6A, NHP6B and similar proteins. This subfamily includes Saccharomyces cerevisiae high-mobility-group proteins NHP6A and its closely related paralog NHP6B. NHP6A and NHP6B seem to be functionally redundant. They are DNA-binding proteins that induce severe bending of DNA and are required for DNA-binding by the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. They augment the fidelity of transcription by RNA polymerase III independently of any role in the FACT complex. They may also play essential roles in transcriptional initiation fidelity of some but not all tRNA genes
KKKKGRKKKDPNAPKRGLSAYMFFSQDNREKVKEENPDATFGEVGKLLGEKWKELSEEEKAPYEEKAAKD
KKRYEEEKAAY
>gnl|CDD|380477 cd01391, Periplasmic_Binding_Protein_type1, Type 1 periplasmic binding fold superfamily. Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold
IIGVVTSSLHQIREQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSV
AIVIQNLAQLFDIPQLALDATSQDLSDKTLYKYFLSVVFSDTLGARLGLDIVKRKNWTYVAAIHGEGLNS
GELRMAGFKELAKQEGICIVASDKADWNAGEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGL
VGDVSVIGSDGWADRDEVGYEVEANGLTTIKQQKMGFGITAIKAMADGSQNMHEEVWFDEKGDALGRYIL
>gnl|CDD|143331 cd01392, HTH_LacI, Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators. HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites
KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT
>gnl|CDD|410881 cd01393, RecA-like, RecA family. RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB
GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLVQILEASPSSELELAEALSRLLYF
RPPDTLAHLLALDSLPESLFPPPNTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAA
QFNLAVVVTNQVTTKIRGGSGASLVPPALGNTWEHSVSTRLLLYR
>gnl|CDD|410882 cd01394, archRadB, archaeal RadB. The archaeal protein RadB shares similarity RadA, the archaeal functional homologue to the bacterial RecA. The precise function of RadB is unclear
LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTEGLSPERFQQIAGER
FESIASNIIVFEPYSFDEQGVAIQEAEKLLKSDKVDLVVVDSATALYRLELGDDSEANRELSRQMSKLLS
IARKYDIPVVITNQVYSDIDDDRLKPVGGTLLEHWSKAIIRLEKSPPGLRRATLEKHRSRPEGQSAGFRI
TDRGIR
>gnl|CDD|238689 cd01395, HMT_MBD, Methyl-CpG binding domains (MBD) present in putative histone methyltransferases (HMT) such as CLLD8 and SETDB1 proteins; CLLD8 contains a MBD, a PreSET and a bifurcated SET domain, suggesting that CLLD8 might be associated with methylation-mediated transcriptional repression. SETDB1 and other proteins in this group have a similar domain architecture. SETDB1 is a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins
PLHTPLLCGFQRMKYRARVGKVKKHVIYKAPCGRSLRNMSEVHRYLRETCSFLTVDNFSF
>gnl|CDD|238690 cd01396, MeCP2_MBD, MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a protein family that share the methyl-CpG-binding domain (MBD). The MBD, consists of about 70 residues and is defined as the minimal region required for binding to methylated DNA by a methyl-CpG-binding protein which binds specifically to methylated DNA. The MBD can recognize a single symmetrically methylated CpG either as naked DNA or within chromatin. MeCP2, MBD1 and MBD2 (and likely MBD3) form complexes with histone deacetylase and are involved in histone deacetylase-dependent repression of transcription. MBD4 is an endonuclease that forms a complex with the DNA mismatch-repair protein MLH1
KPEDPRLPPGWKRELVPRKSGSAGKFDVYYISPTGKKFRSKVELARYLEKNGPTSLDLSDFDFTVPKKLG
LGSPRRH
>gnl|CDD|238691 cd01397, HAT_MBD, Methyl-CpG binding domains (MBD) present in putative chromatin remodelling factor such as BAZ2A; BAZ2A contains a MBD, DDT, PHD-type zinc finger and Bromo domain suggesting that BAZ2A might be associated with histone acetyltransferase (HAT) activity. The Drosophila melanogaster toutatis protein, a putative subunit of the chromatin-remodeling complex, and other such proteins in this group share a similar domain architecture with BAZ2A, as does the Caenorhabditis elegans flectin homolog
ELRVPLELGWRRETRIRGLGGRIQGEVAYYAPCGKKLRQYPEVIKYLSKNGISLLSRENFSFSARAPVGD
FYE
>gnl|CDD|238692 cd01398, RPI_A, RPI_A: Ribose 5-phosphate isomerase type A (RPI_A) subfamily; RPI catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate, the first step of the non-oxidative branch of the pentose phosphate pathway. This reaction leads to the conversion of phosphosugars into glycolysis intermediates, which are precursors for the synthesis of amino acids, vitamins, nucleotides, and cell wall components. In plants, RPI is part of the Calvin cycle as ribulose 5-phosphate is the carbon dioxide receptor in the first dark reaction of photosynthesis. There are two unrelated types of RPIs (A and B), which catalyze the same reaction, at least one type of RPI is present in an organism. RPI_A is more widely distributed than RPI_B in bacteria, eukaryotes, and archaea
LKRAAARAAVDYVEDGMVIGLGTGSTVAYFIEALGERVREEGLNIVGVPTSFQTEELARELGIPLTDLDE
VPRLDLAIDGADEVDPDLNLIKGGGGALLREKIVASAAKKFIVIADESKLVERLGEFPLPVEVVPFAWSY
VARELEKLGGKPVLREGSGKGGPVVTDNGNYILDVHFGTIEDPEALEKELKSIPGVVEHGLFLNMADEVI
VGT
>gnl|CDD|238693 cd01399, GlcN6P_deaminase, GlcN6P_deaminase: Glucosamine-6-phosphate (GlcN6P) deaminase subfamily; GlcN6P deaminase catalyzes the reversible conversion of GlcN6P to D-fructose-6-phosphate (Fru6P) and ammonium. The reaction is an aldo-keto isomerization coupled with an amination or deamination. It is the last step of the metabolic pathway of N-acetyl-D-glucosamine-6-phosphate (GlcNAc6P). GlcN6P deaminase is a hexameric enzyme that is allosterically activated by GlcNAc6P
EEMSEAAAELIAELIREKPPAVLGLATGSTPLGVYEELIELHKEGGLSFSNVTTFNLDEYVGLPPDHPQS
YHYFMRENLFDHIDIKPENIHIPDGNAADLEAECRRYEALIAEAGGIDLQLLGIGENGHIGFNEPGSSLD
SRTRVVTLDESTRQANARFFDGDEDVPTQAITMGIGTIMKAKEILLLATGEGKAEAVKKALEGPVTEECP
ASILQLHPNVTVILDEAAASEL
>gnl|CDD|238694 cd01400, 6PGL, 6PGL: 6-Phosphogluconolactonase (6PGL) subfamily; 6PGL catalyzes the second step of the oxidative phase of the pentose phosphate pathway, the hydrolyzation of 6-phosphoglucono-1,5-lactone (delta form) to 6-phosphogluconate. 6PGL is thought to guard against the accumulation of the delta form of the lactone, which may be toxic through its reaction with endogenous cellular nucleophiles
EALAEALADRIAEALAAAIAKRGRFSLALSGGSTPKPLYELLAAAPALDWSKVHVFLGDERCVPPDDPDS
NYRLAREALLSHVAIPAANIHPIPTELGPEDAAAAYEKELRALFGGVPPFDLVLLGMGPDGHTASLFPGH
PALLEETDRLVVAVTDSPKPPPERITLTLPVLNNARRVVFLVTGAEKAEALKRALAGPDPEELPAARVLP
RPGEVLWFL
>gnl|CDD|238695 cd01401, PncB_like, Nicotinate phosphoribosyltransferase (NAPRTase), related to PncB. Nicotinate phosphoribosyltransferase catalyses the formation of NAMN and PPi from 5-phosphoribosy -1-pyrophosphate (PRPP) and nicotinic acid, this is the first, and also rate limiting, reaction in the NAD salvage synthesis. This salvage pathway serves to recycle NAD degradation products. This subgroup is present in bacteria, archea and funghi
RSLLDTDLYKLTMQQAVLHHYPDVQVTYEFTNRSPEDFLEEAAEALREQIDHLANLRFSEEELAYLRRSL
PFLKPDYLDYLELFRLNPEEVVVRLDTGKGQLDIRISGPWKDTILYEVPLLAIVSEVYFRFRDADWDYEE
QLEKLEEKLERLLEEAKRRDLNGFRFSDFGTRRRFSYEVQETVLKGLKQAAPGYLTGTSNVHFAMKYGLT
PIGTVAHEWFMAHQALTGDLKDSQKAALERWVREYGGDLGIALTDTFGTDAFLRDFDLYFAKLFDGVRHD
SGDPFEWGEKAIAHYEKLGIDPKTKTLVFSDGLDVEKALELYEYFKGRIKVSFGIGTNLTNDFGNKEKST
PLNIVIKLVECNGRPVAKISDSPGKNM
>gnl|CDD|238696 cd01403, Cyt_c_Oxidase_VIIb, Cytochrome C oxidase chain VIIb. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. The VIIb subunit is found only in eukaryotes and its specific function remains unclear. A rare polymorphism of the CcO VIIb gene may be associated with the high risk of nasopharyngeal carcinoma in a Cantonese family
ASPDFHDKYGNAVLISGATFCTAVWTYVMTQTGIEWNLSPVGRVTPKEWRE
>gnl|CDD|238697 cd01406, SIR2-like, Sir2-like: Prokaryotic group of uncharacterized Sir2-like proteins which lack certain key catalytic residues and conserved zinc binding cysteines; and are members of the SIR2 superfamily of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation
GRVVIFVGAGVSVSSGLPDWKTLLDEIASELGLEIDGYSVEAKDENDYLELAELLEKEFGTIGIKINAVL
EEKTRPDFEPSPLHELLLRLFINNEGDVIIITTNYDRLLETALKEINKVVKVIVSVQLALSASARFNGVY
KIHGDVDDDESIVLTKSDYERYYLKNGWATKFLKSDLEKYTVLFIGYSLTDPNIRYLLERLRKNYEGKHA
SHFALLQKPNEEESREKAKKTLNEHKIYRAII
>gnl|CDD|238698 cd01407, SIR2-fam, SIR2 family of proteins includes silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose. Sir2 proteins, also known as sirtuins, are found in all eukaryotes and many archaea and prokaryotes and have been shown to regulate gene silencing, DNA repair, metabolic enzymes, and life span. The most-studied function, gene silencing, involves the inactivation of chromosome domains containing key regulatory genes by packaging them into a specialized chromatin structure that is inaccessible to DNA-binding proteins. The oligomerization state of Sir2 appears to be organism-dependent, sometimes occurring as a monomer and sometimes as a multimer
KRIVVLTGAGISTESGIPDFRSPGGLWARLDPEELAFSPEAFRRDPELFWGFYRERRYPLNAQPNPAHRA
LAELERKGKLKRVITQNVDGLHQRAGSPKVIELHGSLFRVRCTKCGKEYPRDELQADIDREEVPRCPKCG
GLLRPDVVFFGESLPEELDEAAEALAKADLLLVIGTSLQVYPAAGLPLYAPERGAPVVIINLEPTPADRK
ADLVILGD
>gnl|CDD|238699 cd01408, SIRT1, SIRT1: Eukaryotic group (class1) which includes human sirtuins SIRT1-3 and yeast Hst1-4; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2 proteins have been shown to regulate gene silencing, DNA repair, and life span. The most-studied function, gene silencing, involves the inactivation of chromosome domains containing key regulatory genes by packaging them into a specialized chromatin structure that is inaccessible to DNA-binding proteins. The nuclear SIRT1 has been shown to target the p53 tumor suppressor protein for deacetylation to suppress DNA damage, and the cytoplasmic SIRT2 homolog has been shown to target alpha-tubulin for deacetylation for the maintenance of cell integrity
KKIVVLVGAGISTSAGIPDFRSPGTGLYANLARYNLPYPEAMFDISYFRKNPRPFYALAKELYPGQFKPS
VAHYFIKLLEDKGLLLRNYTQNIDTLERVAGVPDDRIIEAHGSFATAHCIKCKHKYPGDWMREDIFNQEV
PKCPRCGGLVKPDIVFFGESLPSRFFSHMEEDKEEADLLIVIGTSLKVAPFASLPSRVPSEVPRVLINRE
PVGHLGKRPFDVALLGDCDDGVREL
>gnl|CDD|238700 cd01409, SIRT4, SIRT4: Eukaryotic and prokaryotic group (class2) which includes human sirtuin SIRT4 and several bacterial homologs; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2 proteins have been shown to regulate gene silencing, DNA repair, metabolic enzymes, and life span
LQDFVARSRRLLVLTGAGISTESGIPDYRSEGGLYSRTFRPMTHQEFMRSPAARQRYWARSFVGWPRFSA
AQPNAAHRALAALEAAGRLHGLITQNVDGLHTKAGSRNVVELHGSLHRVVCLSCGFRTPRAELQDRLEAL
NPGFAEQAAGQAPDGDVDLEDEQVAGFRVPECERCGGVLKPDVVFFGENVPRDRVVTAAARLAEADALLV
LGSSLMVYSGYRFVLAAAEAGLPIAIVNIGPTRADHLATLKVDARCGEVL
>gnl|CDD|238701 cd01410, SIRT7, SIRT7: Eukaryotic and prokaryotic group (class4) which includes human sirtuin SIRT6, SIRT7, and several bacterial homologs; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2 proteins have been shown to regulate gene silencing, DNA repair, metabolic enzymes, and life span
KHLVVFTGAGISTSAGIPDFRGPNGVWTLLPEDKGRRRFSWRFRRAEPTLTHMALVELERAGLLKFVISQ
NVDGLHLRSGLPREKLSELHGNMFIEVCKSCGPEYVRDDVVETRGDKETGRRCHACGGILKDTIVDFGER
LPPENWMGAAAAACRADLFLCLGTSLQVTPAANLPLKAARAGGRLVIVNLQPTPKDKLADLVIHGD
>gnl|CDD|238702 cd01411, SIR2H, SIR2H: Uncharacterized prokaryotic Sir2 homologs from several gram positive bacterial species and Fusobacteria; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2 proteins have been shown to regulate gene silencing, DNA repair, metabolic enzymes, and life span
LQHILKNAKRIVFFTGAGVSTASGIPDYRSKNGLYNEIYKYSPEYLLSHDFLEREPEKFYQFVKENLYFP
DAKPNIIHQKMAELEKMGLKAVITQNIDGLHQKAGSKNVVEFHGSLYRIYCTVCGKTVDWEEYLKSPYHA
KCGGVIRPDIVLYEEMLNESVIEEAIQAIEKADLLVIVGTSFVVYPFAGLIDYRQAGANLIAINKEPTQL
DSPATLVIKDAVKVF
>gnl|CDD|238703 cd01412, SIRT5_Af1_CobB, SIRT5_Af1_CobB: Eukaryotic, archaeal and prokaryotic group (class3) which includes human sirtuin SIRT5, Archaeoglobus fulgidus Sir2-Af1, and E. coli CobB; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2 proteins have been shown to regulate gene silencing, DNA repair, metabolic enzymes, and life span. CobB is a bacterial sirtuin that deacetylates acetyl-CoA synthetase at an active site lysine to stimulate its enzymatic activity
RRVVVLTGAGISAESGIPTFRDADGLWARFDPEELATPEAFARDPELVWEFYNWRRRKALRAQPNPAHLA
LAELERRLPNVLLITQNVDGLHERAGSRNVIELHGSLFRVRCSSCGYVGENNEEIPEEELPRCPKCGGLL
RPGVVWFGESLPLALLEAVEALAKADLFLVIGTSGVVYPAAGLPEEAKERGARVIEINPEPTPLSPIADF
AFRGKAGEVLPALL
>gnl|CDD|238704 cd01413, SIR2_Af2, SIR2_Af2: Archaeal and prokaryotic group which includes Archaeoglobus fulgidus Sir2-Af2, Sulfolobus solfataricus ssSir2, and several bacterial homologs; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2 proteins have been shown to regulate gene silencing, DNA repair, metabolic enzymes, and life span. The Sir2 homolog from the archaea Sulfolobus solftaricus deacetylates the non-specific DNA protein Alba to mediate transcription repression
LTKSRKTVVLTGAGISTESGIPDFRSPDGLWKKYDPEEVASIDYFYRNPEEFWRFYKEIILGLLEAQPNK
AHYFLAELEKQGIIKAIITQNIDGLHQRAGSKNVIELHGTLQTAYCVNCGSKYDLEEVKYAKKHEVPRCP
KCGGIIRPDVVLFGEPLPQALLREAIEAAKEADLFIVLGSSLVVYPANLLPLIAKENGAKLVIVNADETP
FDYIADLVIQDK
>gnl|CDD|133469 cd01414, SAICAR_synt_Sc, non-metazoan 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase. Eukaryotic, bacterial, and archaeal group of SAICAR synthetases represented by the Saccharomyces cerevisiae (Sc) enzyme, mostly absent in metazoans. SAICAR synthetase catalyzes the seventh step of the de novo biosynthesis of purine nucleotides (also reported as eighth step). It converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate
LIYSGKVRDVYDLGDGRLLFVATDRISAFDVILPPDIPGKGEVLTQISAFWFELTEDIIPNHLISTDVED
LPEIKEPEDPDGRSMVVKKAKPIPIECIVRGYLTGSGWKEYQKGGTVCGIKLPEGLREAQKLPEPIFTPS
TKAEEGHDENISFEEAVEIIGAELADELRELALALYERAAEYAAKRGLILADTKFEFGLDENGEIILIDE
VLTPDSSRFWPADSYEPGKEQPSFDKQFVRDWLEASGWDKQDPPPPPLPAEVIEKTSARYIEAYERITG
>gnl|CDD|133470 cd01415, SAICAR_synt_PurC, bacterial and archaeal 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase. A subfamily of SAICAR synthetases represented by the Thermotoga maritima (Tm) enzyme and E. coli PurC. SAICAR synthetase catalyzes the seventh step of the de novo biosynthesis of purine nucleotides (also reported as eighth step). It converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate
LLYEGKAKIVYATDDPDVLIVEFKDDATAFNGKKKDTIEGKGVLNNEISALIFKYLEENGIKTHFIEKLS
DREQLVKKVEIIPLEVVVRNIAAGSLVKRLGIEEGTVLDPPIVEFYYKNDELGDPLINEDHILALGLATE
EELKEIKELALKINEVLSEFFAEIGIILVDFKLEFGRDKDGEIVLADEISPDTCRLWDKETGEKLDKDRF
RRDLGDVIEAYEEVLKRLGE
>gnl|CDD|133471 cd01416, SAICAR_synt_Ade5, Ade5_like 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase. Eukaryotic group of SAICAR synthetases represented by the Drosophila melanogaster, N-terminal, SAICAR synthetase domain of bifunctional Ade5. The Ade5 gene product (CAIR-SAICARs) catalyzes the sixth and seventh steps of the de novo biosynthesis of purine nucleotides (also reported as seventh and eighth steps). SAICAR synthetase converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate
LKLGKKLIEGKTKIVYELPDQPGLVLIQSKDRITAGDGARKDEIEGKAAISNKTTSNVFELLQEAGIKTH
FVKQCSPTAFIARKCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFSPPKLEFFYKDDANHDPQWSEEQLL
EAKLNCGGLKIGKKEVDIMTKSTIAIFEILEKAWATQDCTLVDMKIEFGVDVTTGEILLADVIDNDSWRL
WPSGDKRLMKDKQVYRNLKEVTDEALQEVKKNYEWVADKLEL
>gnl|CDD|238705 cd01417, Ribosomal_L19e_E, Ribosomal protein L19e, eukaryotic. L19e is found in the large ribosomal subunit of eukaryotes and archaea. L19e is distinct from the ribosomal subunit L19, which is found in prokaryotes. It consists of two small globular domains connected by an extended segment. It is located toward the surface of the large subunit, with one exposed end involved in forming the intersubunit bridge with the small subunit. The other exposed end is involved in forming the translocon binding site, along with L22, L23, L24, L29, and L31e subunits
LRLQKRLAASVLKCGKRKVWLDPNEISEISNANSRQSIRKLIKDGLIIKKPVKVHSRSRARKRHEAKRKG
RHMGYGKRKGTANARMPSKVLWMRRQRVLRRLLKKYRESKKIDKHLYHELYLKAKGNVFKNKRVLMEHIH
KAKAEKAREKELADQAEARRAKNK
>gnl|CDD|238706 cd01418, Ribosomal_L19e_A, Ribosomal protein L19e, archaeal. L19e is found in the large ribosomal subunit of eukaryotes and archaea. L19e is distinct from the ribosomal subunit L19, which is found in prokaryotes. It consists of two small globular domains connected by an extended segment. It is located toward the surface of the large subunit, with one exposed end involved in forming the intersubunit bridge with the small subunit. The other exposed end is involved in forming the translocon binding site, along with L22, L23, L24, L29, and L31e subunits
LSSQRRLAADILGVGINRVWIDPERLEEVAEAITRDDIRALIKEGVIKAKPKKGISRGRLKERHEKRKKG
RRRGPGSRKGKKGARTPKKERWIKTIRALRRYLKELRDKGKIDKKTYRKLYRKAKGGSFRSLSHLKSYLK
QHGLL
>gnl|CDD|238707 cd01419, MoaC_A, MoaC family, archaeal. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, an essential cofactor of a diverse group of redox enzymes. MoaC, a small hexameric protein, converts, together with MoaA, a guanosine derivative to the precursor Z by inserting the carbon-8 of the purine between the 2' and 3' ribose carbon atoms, which is the first of three phases of Moco biosynthesis
MVDISSKEDVAREAVASGFIKLKEETIKAIREGKVEKGNVIATARIAGILAVKKTPELIPMCHPIPITGV
DVDFEVEEDGIEVRCTVKTTYKTGVEMEALTGVSVALLTIWDMVKSAEKDEDGQYPETRIENVRVVEKIK
G
>gnl|CDD|238708 cd01420, MoaC_PE, MoaC family, prokaryotic and eukaryotic. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, an essential cofactor of a diverse group of redox enzymes. MoaC, a small hexameric protein, converts, together with MoaA, a guanosine derivative to the precursor Z by inserting the carbon-8 of the purine between the 2' and 3' ribose carbon atoms, which is the first of three phases of Moco biosynthesis
MVDVSDKAVTERTAVAEGRVRMSPETLDLITEGQLPKGDVLAVARIAGIMAAKRTSELIPLCHPLPLTGV
DVDFELDEETSGVRIEATVRTTGRTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGGIRLLEKSGGKSGD
>gnl|CDD|238709 cd01421, IMPCH, Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine biosynthesis pathway protein ATIC (purH). The bifunctional ATIC protein contains a C-terminal ATIC formylase domain that formylates 5-aminoimidazole-4-carboxamide-ribonucleotide. The IMPCH domain then converts the formyl-5-aminoimidazole-4-carboxamide-ribonucleotide to inosine monophosphate. This is the final step in de novo purine production
KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHG
GILARRDNEEHKDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTV
LVDPADYQKVLEELKSNGSISEETRRRLALKAFAHTAEYDAAISNYL
>gnl|CDD|238710 cd01422, MGS, Methylglyoxal synthase catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The first part of the catalytic mechanism is believed to be similar to TIM (triosephosphate isomerase) in that both enzymes utilize DHAP to form an ene-diolate phosphate intermediate. In MGS, the second catalytic step is characterized by the elimination of phosphate and collapse of the enediolate to form methylglyoxal instead of reprotonation to form the isomer glyceraldehyde 3-phosphate, as in TIM. This is the first reaction in the methylglyoxal bypass of the Embden-Myerhoff glycolytic pathway and is believed to provide physiological benefits under non-ideal growth conditions in bacteria
RIALIAHDNKKEDLVEFVKQHQELLSRHRLVATGTTGLLIQEATGLTVNRMKSGPLGGDQQIGALIAEGE
IDAVIFFRDPLTAQPHEPDVKALLRLCDVYNIPLATNRSTADAII
>gnl|CDD|238711 cd01423, MGS_CPS_I_III, Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain
KGILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDKPSLRELLAEG
KIDLVINLPSNRGKRVLDNDYVMRRAADDFAVPLITNPKCAKLFIE
>gnl|CDD|238712 cd01424, MGS_CPS_II, Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine
GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQL
VINTPSGKRAIRDGFSIRRAALEYKVPYFTTLDTARAAVE
>gnl|CDD|100106 cd01425, RPS2, Ribosomal protein S2 (RPS2), involved in formation of the translation initiation complex, where it might contact the messenger RNA and several components of the ribosome. It has been shown that in Escherichia coli RPS2 is essential for the binding of ribosomal protein S1 to the 30s ribosomal subunit. In humans, most likely in all vertebrates, and perhaps in all metazoans, the protein also functions as the 67 kDa laminin receptor (LAMR1 or 67LR), which is formed from a 37 kDa precursor, and is overexpressed in many tumors. 67LR is a cell surface receptor which interacts with a variety of ligands, laminin-1 and others. It is assumed that the ligand interactions are mediated via the conserved C-terminus, which becomes extracellular as the protein undergoes conformational changes which are not well understood. Specifically, a conserved palindromic motif, LMWWML, may participate in the interactions. 67LR plays essential roles in the adhesion of cells to the basement membrane and subsequent signalling events, and has been linked to several diseases. Some evidence also suggests that the precursor of 67LR, 37LRP is also present in the nucleus in animals, where it appears associated with histones
LLEAGVHLGHKTRRWNPKMKPYIYGERNGIHIIDLEKTLEKLRLALNFIANIAAKGGKILFVGTKPQAQR
AVKKFAERTGSFYVNGRWLGGTLTNWKTIRKSIKRLKKLEKEKLEKNLGGIKDMFRLPDLVIVLDPRKEH
QAIREASKLGIPVIAIVDTNCDPDLIDYPIPANDDSIRSIALILWLLARAILE
>gnl|CDD|349738 cd01426, ATP-synt_F1_V1_A1_AB_FliI_N, ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain. The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase
KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGNNETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEP
TGR
>gnl|CDD|319763 cd01427, HAD_like, Haloacid dehalogenase-like hydrolases. The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
AVLFDLDGTLLAVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLL
LLLLKLGVDPEEVLFVGDSENDIEAARAAGGRTVAV
>gnl|CDD|238713 cd01428, ADK, Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates
RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDSGKLVPDEIVIKLLKER
LKKPDCKKGFILDGFPRTVDQAEALDELLDEGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKD
DVTGEPLSQRSDDNEETIKKRLEVYKEQTAPLIDYYKKKGKLVEIDGSGDIDEV
>gnl|CDD|349744 cd01429, ATP-synt_F1_V1_A1_AB_FliI_C, ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain. The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase
HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE
>gnl|CDD|319764 cd01431, P-type_ATPases, ATP-dependent membrane-bound cation and aminophospholipid transporters. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine
VICSDKTGTLTKNGMTVTKLFIEEIPFNSTRKRMSVVVRLPGRYRAIVKGAPETILSRCSHALTEEDRNK
IEKAQEESAREGLRVLALAYREFDPETSKEAVELNLVFLGLIGLQDPPRPEVKEAIAKCRTAGIKVVMIT
GDNPLTAIAIAREIGIDTKASGVILGEEADEMSEEELLDLIAKVAVFARVTPEQKLRIVKALQARGEVVA
MTGDGVNDAPALKQADVGIAMGSTGTDVAKEAADIVLLDDNFATIVEAVEEGRAIYDNIKKNITYLLANN
VAEVFAIALALFLGGPLPLLAFQILWINLVTDLIPALAL
>gnl|CDD|238714 cd01433, Ribosomal_L16_L10e, Ribosomal_L16_L10e: L16 is an essential protein in the large ribosomal subunit of bacteria, mitochondria, and chloroplasts. Large subunits that lack L16 are defective in peptidyl transferase activity, peptidyl-tRNA hydrolysis activity, association with the 30S subunit, binding of aminoacyl-tRNA and interaction with antibiotics. L16 is required for the function of elongation factor P (EF-P), a protein involved in peptide bond synthesis through the stimulation of peptidyl transferase activity by the ribosome. Mutations in L16 and the adjoining bases of 23S rRNA confer antibiotic resistance in bacteria, suggesting a role for L16 in the formation of the antibiotic binding site. The GTPase RbgA (YlqF) is essential for the assembly of the large subunit, and it is believed to regulate the incorporation of L16. L10e is the archaeal and eukaryotic cytosolic homolog of bacterial L16. L16 and L10e exhibit structural differences at the N-terminus
KGNKLFFGEYGLVALEPGRITAEQLEAARIAINRYLKKKGGKLWIRVFPDHPVTKKPLETRMGKGKGKPE
GWVARVKPGQILFEVRGVPEEEVAKEALRRAAKKLPIKTKIV
>gnl|CDD|238715 cd01434, EFG_mtEFG1_IV, EFG_mtEFG1_IV: domains similar to domain IV of the bacterial translational elongation factor (EF) EF-G. Included in this group is a domain of mitochondrial Elongation factor G1 (mtEFG1) proteins homologous to domain IV of EF-G. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s) mtEFG2s are not present in this group
YRETITKPAEFEYRHKKQSGGAGQYGHVVLEIEPLPRGSGFEFVNKIVGGAIPKEYIPAVEKGFREALEK
GPLAGYPVVDVKVTLYDGSYHDVDSSEMAFKIAARMAFKEAFKKAK
>gnl|CDD|259844 cd01435, RNAP_I_RPA1_N, Largest subunit (RPA1) of eukaryotic RNA polymerase I (RNAP I), N-terminal domain. RPA1 is the largest subunit of the eukaryotic RNA polymerase I (RNAP I). RNAP I is a multi-subunit protein complex responsible for the synthesis of rRNA precursors. RNAP I consists of at least 14 different subunits, the largest being homologous to subunit Rpb1 of yeast RNAP II and subunit beta' of bacterial RNAP. The yeast member of this family is known as Rpb190. Structure studies suggest that different RNA polymerase complexes share a similar crab-claw-shaped structure. The N-terminal domain of Rpb1, the largest subunit of RNAP II in yeast, forms part of the active site. It makes up the head and core of one clamp, as well as the pore and funnel structures of RNAP II. The strong homology between RPA1 and Rpb1 suggests a similar functional and structural role
SFSFYSAEEIRKLSVKEITNPVTFDSLGHPVPGGLYDPALGPLDKDDICSTCGLNYLNCPGHFGHIELPL
PVYNPLFFDLLYKLLRGSCFYCHRFRISKWEVKLFVAKLKLLDKGLLVEAAELDFGYDMFFLDVLLVPPN
RFRPPSFLGDKVFENPQNVLLSKILKDNQQIRDLLASMRQAESQSKLDLISGKTNSEKLINAWLQLQSAV
NELFDSTKAPKSGKKSPPGIKQLLEKKEGLFRMNMMGKRVNYAARSVISPDPFIETNEIGIPLVFAKKLT
FPEPVTPFNVEELRQAVINGPDVYPGANAIEDEDGRLILLSALSEERRKALAKLLLLLSSAKLLLNGPKK
VYRHLLDGDVVLLNRQPTLHKPSIMAHKVRVLPGEKTLRLHYANCKSYNADFDGDEMNLHFPQSELARAE
AYYIASTDNQYLVPTDGKPLRGLIQDHVVSGVLLTSRDTFFTREEYQQLVYAALRPLFTSDKDGRIKLLP
PAILKPKPLWTGKQVISTILKNLIPGNAPLLNLSGKKKTKKKVGGGKWGGGSEESQVIIRNGELLTGVLD
KSQFGASAYGLVHAVYELYGGETAGKLLSALGRLFTAYLQMRGFTCGIEDLLLTPKADEKRRKILRKAKK
LGLEAAAEFLGLKLNKVTSSIIKACLPKGLLKPFPENNLQLMVQSGAKGSMVNASQISCLLGQQELEGRR
VPLMVSGKTLPSFPPYDTSPRAGGFITDRFLTGIRPQEYFFHCMAGREGLIDTAVKTSRSGYLQRCLIKH
LEGLKVNYD
>gnl|CDD|238716 cd01436, Dipth_tox_like, Mono-ADP-ribosylating toxins catalyze the transfer of ADP_ribose from NAD+ to eukaryotic Elongation Factor 2, halting protein synthesis. A single molecule of delivered toxin is sufficient to kill a cell. These toxins share mono-ADP-ribosylating activity with a variety of bacterial toxins, such as cholera toxin and pertussis toxin. The structural core is homologous to the poly-ADP ribosylating enzymes such as the PARP enzymes and Tankyrase. Diphtheria toxin is encoded by a lysogenic bacteriophage. Both diphtheria toxin and Pseudomonas aeruginosa exotoxin A are multi-domain proteins. These domains provide a EF2 ADP_ribosylating, receptor-binding, and intracellular trafficking/transmembrane functions
SSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGVVKVTYPG
LTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAK
ALSVELE
>gnl|CDD|238717 cd01437, parp_like, Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active. Poly(ADP-ribose)-like polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length through interactions with telomere repeat binding factor 1
KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQGSQLE
ELSNEFYTLIPHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEDDSDDPLDANYEKLKCKI
EPLDKDSEEYKIIEKYLKNTHAPTTEYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGI
LSQGLRIAPPEAPVTGYMFGKGIYFADMFSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKEL
PKGKHSVKGLGKTAPDPSEFEIDLDGVVVPLGKPVPSGHKTDTSLLYNEYIVYDVAQVRLKYLLEVK
>gnl|CDD|238718 cd01438, tankyrase_like, Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 poly-ADP-ribosylates Telomere Repeat Binding Factor 1 (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or TRF1. The tankyrases also contain multiple ankyrin repeats that mediate protein-protein interaction (binding TRF1 and insulin-responsive aminopeptidase) and may function as a complex. Overexpression of Tank1 promotes increased telomere length when overexpressed, while overexpressed Tank2 has been shown to promote PARP cleavage- independent cell death (necrosis)
QGRNPYLTFHCVNQGTILLDLAPDDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNIIRIQKVVNKKLRE
RYCHRQKEIAEENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGG
GTGCPTHKDRSCYVCHRQMLFCRVTLGKSFLQFSAMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQA
YPEYLITYQIVKP
>gnl|CDD|238719 cd01439, TCCD_inducible_PARP_like, Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation
LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDY
TQGHPGYRRPPLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY
>gnl|CDD|238720 cd01443, Cdc25_Acr2p, Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included in this CD are eukaryotic arsenate resistance proteins such as Saccharomyces cerevisiae Acr2p and similar proteins. Cdc25 phosphatases activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. The Cdc25 and Acr2p RHOD domains have the signature motif (H/YCxxxxxR)
LKYISPEELVALLENSDSNAGKDFVVVDLRRDDYEGGHIKGSINLPAQSCYQTLPQVYALFSLAGVKLAI
FYCGSSQGRGPRAARWFADYLRKVGESLPKSYILTGGIKAWYH
>gnl|CDD|238721 cd01444, GlpE_ST, GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine
RISVDELAELLAAGEAPVLLDVRDPASYAALPDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSA
QLAQALREAGFTDVRSLAGGFEAWRR
>gnl|CDD|238722 cd01445, TST_Repeats, Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only the second repeat contains the catalytically active Cys residue. The role of the 1st repeat is uncertain, but believed to be involved in protein interaction. This CD aligns the 1st and 2nd repeats
KSTEQLAENLEAGKVGKGFQLLDARAQSPGTREARGEYLETQPEPDAVGLDSGHIPGASFFDFEECLDEA
GFEESMEPSEAEFAAMFEAKGIDLDKHLIATDGDDLGGFTACHIALAARLCGHPDVAILDGGFFEWFH
>gnl|CDD|238723 cd01446, DSP_MapKP, N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain
TIDCAWLAALLREGGERLLLLDCRPFLEYSSSHIRGAVNVCCPTILRRRLQGGKILLQQLLSCPEDRDRL
RRGESLAVVVYDESSSDRERLREDSTAESVLGKLLRKLQEGCSVYLLKGGFEQFSSEFPELC
>gnl|CDD|238724 cd01447, Polysulfide_ST, Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins
LSPEDARALLGSPGVLLVDVRDPRELERTGMIPGAFHAPRGMLEFWADPDSPYHKPAFAEDKPFVFYCAS
GWRSALAGKTLQDMGLKPVYNIEGGFKDWKEAG
>gnl|CDD|238725 cd01448, TST_Repeat_1, Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction
LVSPDWLAEHLDDPDVRILDARWYLPDRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAEL
LGSLGISNDDTVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG
>gnl|CDD|238726 cd01449, TST_Repeat_2, Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the second repeat. Only the second repeat contains the catalytically active Cys residue
VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALF
AALGITPDKPVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWGS
>gnl|CDD|238727 cd01450, vWFA_subfamily_ECM, Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains
LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVK
NLKYLGGGGTNTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGV
GPADEEELREIASCPSERHVF
>gnl|CDD|238728 cd01451, vWA_Magnesium_chelatase, Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). In chlorophyll biosynthesis, insertion of Mg2+ into protoporphyrin IX is catalysed by magnesium chelatase in an ATP-dependent reaction. Magnesium chelatase is a three sub-unit (BchI, BchD and BchH) enzyme with a novel arrangement of domains: the C-terminal helical domain is located behind the nucleotide binding site. The BchD domain contains a AAA domain at its N-terminus and a VWA domain at its C-terminus. The VWA domain has been speculated to be involved in mediating protein-protein interactions
NLVIFVVDASGSMAARHRMAAAKGAVLSLLRDAYQRRDKVALIAFRGTEAEVLLPPTRSVELAKRRLARL
PTGGGTPLAAGLLAAYELAAEQARDPGQRPLIVVITDGRANVGPDPTADRALAAARKLRARGISALVIDT
EGRPVRRGLAKDLARALGGQYVRLPDLSADAIASAVRA
>gnl|CDD|238729 cd01452, VWA_26S_proteasome_subunit, 26S proteasome plays a major role in eukaryotic protein breakdown, especially for ubiquitin-tagged proteins. It is an ATP-dependent protease responsible for the bulk of non-lysosomal proteolysis in eukaryotes, often using covalent modification of proteins by ubiquitylation. It consists of a 20S proteolytic core particle (CP) and a 19S regulatory particle (RP). The CP is an ATP independent peptidase consisting of hydrolyzing activities. One or both ends of CP carry the RP that confers both ubiquitin and ATP dependence to the 26S proteosome. The RP's proposed functions include recognition of substrates and translocation of these to CP for proteolysis. The RP can dissociate into a stable lid and base subcomplexes. The base is composed of three non-ATPase subunits (Rpn 1, 2 and 10). A single residue in the vWA domain of Rpn10 has been implicated to be responsible for stabilizing the lid-base association
MVLEATMICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNSPEVLVTLTNDQG
KILSKLHDVQPKGKANFITGIQIAQLALKHRQNKNQKQRIVAFVGSPIEEDEKDLVKLAKRLKKNNVSVD
IINFGEIDDNTEKLTAFIDAVNGKDGSHLVSVPPGENLLSDALLSSP
>gnl|CDD|238730 cd01453, vWA_transcription_factor_IIH_type, Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five general transcription factors that binds RNA polymerase II holoenzyme. Orthologues of these genes are found in all completed eukaryotic genomes and all these proteins contain a VWA domain. The p44 subunit of TFIIH functions as a DNA helicase in RNA polymerase II transcription initiation and DNA repair, and its transcriptional activity is dependent on its C-terminal Zn-binding domains. The function of the vWA domain is unclear, but may be involved in complex assembly. The MIDAS motif is not conserved in this sub-group
GIMRHLIIVIDCSRSMEEQDLKPSRLAVVLKLLELFIEEFFDQNPISQLGIISIKNGRAEKLTDLTGNPR
KHIQALKTARECSGEPSLQNGLEMALESLKHMPSHGSREVLIIFSSLSTCDPGNIYETIDKLKKENIRVS
VIGLSAEMHICKEICKATNGTYKVILDETHLKELLLEHVTPPP
>gnl|CDD|238731 cd01454, vWA_norD_type, norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------_ NO2- ------_ NO -------_ N2O ---------_ N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif
LAVTLLLDLSGSMRSDRRIDVAKKAAVLLAEALEACGVPHAILGFTTDAGGRERVRWIKIKDFDESLHER
ARKRLAALSPGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYEGNVFATEDALRAVIEARK
LGIEVFGITIDRDATTVDKEYLKNIFGEEGYALI
>gnl|CDD|238732 cd01455, vWA_F11C1-5a_type, Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the functions of the members of this subgroup. The members of this subgroup are fused to the ancient AAA domain
KRLKLVVDVSGSMYRFNGYDGRLDRSLEAVVMVMEAFDGFEDKIQYDIIGHSGDGPCVPFVKTNHPPKNN
KERLETLKMMHAHSQFCWSGDHTVEATEFAIKELAAKEDFDEAIVIVLSDANLERYGIQPKKLADALARE
PNVNAFVIFIGSLSDEADQLQRELPAGKAFVCMDTSELPHIMQQIFTSTLL
>gnl|CDD|238733 cd01456, vWA_ywmD_type, VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the members of this subgroup. All members of this subgroup however have a conserved MIDAS motif
APLGSPAFALEPVETEPQLPPNVAIVLDNSGSMREVDGGGETRLDNAKAALDETANALPDGTRLGLWTFS
GDGDNPLDVRVLVPKGCLTAPVNGFPSAQRSALDAALNSLQTPTGWTPLAAALAEAAAYVDPGRVNVVVL
ITDGEDTCGPDPCEVARELAKRRTPAPPIKVNVIDFGGDADRAELEAIAEATGGTYAYNQSDLASL
>gnl|CDD|238734 cd01457, vWA_ORF176_type, VWA ORF176 type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses. In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. The members of this subgroup are Eubacterial in origin and have a conserved MIDAS motif. Not much is known about the biochemistry of these
ENRDYTLLIDKSGSMAEADEAKERSRWEEAQESTRALARKCEEYDSDGITVYLFSGDFRRYDNVNSSKVD
QLFAENSPDGGTNLAAVLQDALNNYFQRKENGATCPEGETFLVITDGAPDDKDAVERVIIKASDELDADN
ELAISFLQIGRDPAATAFLKALDDQLQEVGAKFDIVDTVTWDDMERLTNGDVLLKAITD
>gnl|CDD|238735 cd01458, vWA_ku, Ku70/Ku80 N-terminal domain. The Ku78 heterodimer (composed of Ku70 and Ku80) contributes to genomic integrity through its ability to bind DNA double-strand breaks (DSB) in a preferred orientation. DSB's are repaired by either homologues recombination or non-homologues end joining and facilitate repair by the non-homologous end-joining pathway (NHEJ). The Ku heterodimer is required for accurate process that tends to preserve the sequence at the junction. Ku78 is found in all three kingdoms of life. However, only the eukaryotic proteins have a vWA domain fused to them at their N-termini. The vWA domain is not involved in DNA binding but may very likey mediate Ku78's interactions with other proteins. Members of this subgroup lack the conserved MIDAS motif
KESVVFLVDVSPSMFESKDGEYESPFEEALKCIRQLMKSKIISSPKDLVGVVFYGTEESKNPVGYENIYV
LLDLDTPGAERVEDLKELIEPGGLSFAGQVGDSGQVSLSDALWVCLDLFSKGKKKKSHKRIFLFTNNDDP
HGGDSIKDSQAAVKAEDLKDKGIELELFPLSSPGKKFDVSKFYKDIIALVEDANEELLDEFTEPSKDLED
LLKRLRAK
>gnl|CDD|238736 cd01459, vWA_copine_like, VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. They are found in human and orthologues have been found in C. elegans and Arabidopsis Thaliana. None have been found in D. Melanogaster or S. Cereviciae. Phylogenetic distribution suggests that copines have been lost in some eukaryotes. No functional properties have been assigned to the VWA domains present in copines. The members of this subgroup contain a functional MIDAS motif based on their preferential binding to magnesium and manganese. However, the MIDAS motif is not totally conserved, in most cases the MIDAS consists of the sequence DxTxS instead of the motif DxSxS that is found in most cases. The C2 domains present in copines mediate phospholipid binding
IKKVYKSSGEVTLTDCRVQPTFLDYRSAGLESNLIVAIDFTKSNGWPGEKRSLHYISPGRLNPYQKAIRI
VGEVLQPYDSDKLIPAFGFGAIVTKDQSVFSFFPGYSESPECQGFEGVLRAYREALPNVSLSGPTNFAPV
IRAAANIAKASNSQSKYHILLIITDGEITDMNETIKAIVEASKYPLSIVIVGVGDGPFDAMERLDDDDGL
ESSDGRIATRDIVQFVPFTEFMSNAGNPEAALATAALAEIPSQL
>gnl|CDD|238737 cd01460, vWA_midasin, VWA_Midasin: Midasin is a member of the AAA ATPase family. The proteins of this family are unified by their common archetectural organization that is based upon a conserved ATPase domain. The AAA domain of midasin contains six tandem AAA protomers. The AAA domains in midasin is followed by a D/E rich domain that is following by a VWA domain. The members of this subgroup have a conserved MIDAS motif. The function of this domain is not exactly known although it has been speculated to play a crucial role in midasin function
LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDS
KSMSENNSKKLALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTD
IANLLKFTAQIFEDARTQSSSGSLWQLLLIISDGRGEFSEGAQKVRLREAREQNVFVVFIIIDNPDNKQS
ILDIKVVSFKNDKSGVITPYLDEFPFPYYVIVRDLNQLPSVLSDALRQWFELVNSS
>gnl|CDD|238738 cd01461, vWA_interalpha_trypsin_inhibitor, vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix
LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEY
VNRLQALGGTNMNDALEAALELLNSSPGSVPQIILLTDGEVTNESQILKNVREALSGRIRLFTFGIGSDV
NTYLLERLAREGRGIARRIYETDDIESQLLR
>gnl|CDD|238739 cd01462, VWA_YIEM_type, VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have a conserved MIDAS motif, however, their biochemical function is not well characterised
GPVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRDTYLILFDSEFQTKIVDKTDDLEEPVEFLSGVQ
LGGGTDINKALRYALELIERRDPRKADIVLITDGYEGGVSDELLREVELKRSRVARFVALALGDHGNPGY
DRISAEDELVGR
>gnl|CDD|238740 cd01463, vWA_VGCC_like, VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex
RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDT
LVQATTSNKKVLKEALDMLEAKGIANYTKALEFAFSLLLKNLQSNHSGSRSQCNQAIMLITDGVPENYKE
IFDKYNWDKNSEIPVRVFTYLIGREVTDRREIQWMACENKGYYSHIQSLD
>gnl|CDD|238741 cd01464, vWA_subfamily, VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif
MRRLPIYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYALESVEISVITFDSAARVIVPLTPLESFQP
PRLTASGGTSMGAALELALDCIDRRVQRYRADQKGDWRPWVFLLTDGEPTDDLTAAIERIKEARDSKGRI
VACAVGPKADLDTLKQITEGVPLLDDALSGLNFFKW
>gnl|CDD|238742 cd01465, vWA_subgroup, VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known
LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLT
AGGSTAGGAGIQLGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDN
YNEDLMEAIADAGNGNTAYIDNLAEARKVF
>gnl|CDD|238743 cd01466, vWA_C3HC4_type, VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known
VDLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSPLRRMTAKGKRSAKRVVDG
LQAGGGTNVVGGLKKALKVLGDRRQKNPVASIMLLSDGQDNHGAVVLRADNAPIPIHTFGLGASHDPALL
AFIAEITGGTFSYVK
>gnl|CDD|238744 cd01467, vWA_BatA_type, VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses. In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif
EGRDIMIALDVSGSMLAQDFVKPSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLDRESLKEL
LEDIKIGLAGQGTAIGDAIGLAIKRLKNSEAKERVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGV
GKSGSGPKPDGSTILDEDSLVEIADKTGGRIFRALDGFEL
>gnl|CDD|238745 cd01468, trunk_domain, trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface. Some members of this family possess a partial MIDAS motif that is a characteristic feature of most vWA domain proteins
PQPPVFVFVIDVSYEAIKEGLLQALKESLLASLDLLPGDPRARVGLITYDSTVHFYNLSSDLAQPKMYVV
SDLKDVFLPLPDRFLVPLSECKKVIHDLLEQLPPMFWPVPTHRPERCLGPALQAAFLLLKGTFAGGRIIV
FQGGLPTVGPGKLKSREDKEPIRSHDEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQL
AKSTGGQVYLYDSFQAPNDGSKFKQDLQR
>gnl|CDD|238746 cd01469, vWA_integrins_alpha_subunit, Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions
MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVK
HISQLLGLTNTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGV
GGHFQRENSREELKTIASKPPEEHFFNVTDFAALKDI
>gnl|CDD|238747 cd01470, vWA_complement_factors, Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains
LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKR
LEDFNYDDHGDKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNL
VYKNNKSDNPREDYLDVYVFGVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD
>gnl|CDD|238748 cd01471, vWA_micronemal_protein, Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners
LDLYLLVDGSGSIGYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLALN
AIRALLSLYYPNGSTNTTSALLVVEKHLFDTRGNRENAPQLVIIMTDGIPDSKFRTLKEARKLRERGVII
AVLGVGQGVNHEENRSLVGCDPDDSPCPLYLQSSWSEVQNVIKPFL
>gnl|CDD|238749 cd01472, vWA_collagen, von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif
ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVK
NLRYIGGGTNTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKN
ADEEELKQIASDPKELYVFNVADF
>gnl|CDD|238750 cd01473, vWA_CTRP, CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions
YDLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLK
KINDLKNSYRSGGETYIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGNDTSASKKELQDISLLYKEENV
KLLVVGVGAASENKLKLLAGCDINNDNCPNVIKTEWNNLNGISKFLTDKICD
>gnl|CDD|238751 cd01474, vWA_ATR, ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells
CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEV
LKKVTPSGQTYIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCV
GVTDFLKSQLINIADSKEYVFPVTSGFQALSGIIESVVKKACIEI
>gnl|CDD|238752 cd01475, vWA_Matrilin, VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands
GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRA
VRRMEYLETGTMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFA
VGVGRADEEELREIASEPLADHVFYVEDFSTIEELTKKFQGKICVVPDLCATLSHVCQQVCISTPGSYLC
ACTEGYALLEDNKT
>gnl|CDD|238753 cd01476, VWA_integrin_invertebrates, VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands
LDLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPKHNDGEELLEKV
DNLRFIGGTTATGAAIEVALQQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVPNIETFAVGTG
DPGTVDTEELHSITGNEDHIFTD
>gnl|CDD|238754 cd01477, vWA_F09G8-8_type, VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup
SPAAAYTDRECGSDIKNLWLDIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGTDYDDPRSTRVGLVT
YNSNATVVADLNDLQSFDDLYSQIQGSLTDVSSTNASYLDTGLQAAEQMLAAGKRTSRENYKKVVIVFAS
DYNDEGSNDPRPIAARLKSTGIAIITVAFTQDESSNLLDKLGKIASPGMNFTS
>gnl|CDD|238755 cd01478, Sec23-like, Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the budding and fusion of intracellular transport vesicles that selectively carry cargo proteins and lipids from donor to acceptor organelles. The two main classes of vesicular carriers within the endocytic and the biosynthetic pathways are COP- and clathrin-coated vesicles. Formation of COPII vesicles requires the ordered assembly of the coat built from several cytosolic components GTPase Sar1, complexes of Sec23-Sec24 and Sec13-Sec31. The process is initiated by the conversion of GDP to GTP by the GTPase Sar1 which then recruits the heterodimeric complex of Sec23 and Sec24. This heterodimeric complex generates the pre-budding complex. The final step leading to membrane deformation and budding of COPII-coated vesicles is carried by the heterodimeric complex Sec13-Sec31. The members of this CD belong to the Sec23-like family. Sec 23 is very similar to Sec24. The Sec23 and Sec24 polypeptides fold into five distinct domains: a beta-barrel, a zinc finger, a vWA or trunk, an all helical region and a carboxy Gelsolin domain. The members of this subgroup lack the consensus MIDAS motif but have the overall Para-Rossmann type fold that is characteristic of this superfamily
TSPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDY
TAKQIQDMLGLGGPAMRPSASQHPGAGNPLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPL
RCTGVALSIAVGLLEACFPNTGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFY
DSLAKRLAANGHAVDIFAGCLDQVGLLEMKVLVNSTGGHVVLSDSFTTSIFKQSFQR
>gnl|CDD|238756 cd01479, Sec24-like, Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the budding and fusion of intracellular transport vesicles that selectively carry cargo proteins and lipids from donor to acceptor organelles. The two main classes of vesicular carriers within the endocytic and the biosynthetic pathways are COP- and clathrin-coated vesicles. Formation of COPII vesicles requires the ordered assembly of the coat built from several cytosolic components GTPase Sar1, complexes of Sec23-Sec24 and Sec13-Sec31. The process is initiated by the conversion of GDP to GTP by the GTPase Sar1 which then recruits the heterodimeric complex of Sec23 and Sec24. This heterodimeric complex generates the pre-budding complex. The final step leading to membrane deformation and budding of COPII-coated vesicles is carried by the heterodimeric complex Sec13-Sec31. The members of this CD belong to the Sec23-like family. Sec 24 is very similar to Sec23. The Sec23 and Sec24 polypeptides fold into five distinct domains: a beta-barrel, a zinc finger, a vWA or trunk, an all helical region and a carboxy Gelsolin domain. The members of this subgroup carry a partial MIDAS motif and have the overall Para-Rossmann type fold that is characteristic of this superfamily
PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDDPRTRVGFITFDSTLHFFNLKSSLEQPQMMV
VSDLDDPFLPLPDGLLVNLKESRQVIEDLLDQIPEMFQDTKETESALGPALQAAFLLLKETGGKIIVFQS
SLPTLGAGKLKSREDPKLLSTDKEKQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRL
TGGQVYYYPSFNFSAPNDVEKLVNELARYLTRKI
>gnl|CDD|238757 cd01480, vWA_collagen_alpha_1-VI-type, VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions
GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKDPAGSWRVGVVQYSDQQEVEAGFLRDIRN
YTSLKEAVDNLEYIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDGHSDGSPDGGIEKAVNEADHLG
IKIFFVAVGSQNEEPLSRIACDGKSALYRENFAELLWSFFIDDETA
>gnl|CDD|238758 cd01481, vWA_collagen_alpha3-VI-like, VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions
KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVR
RLRLRGGSQLNTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIG
ARNADLAELQQIAFDPSFVFQVSDF
>gnl|CDD|238759 cd01482, vWA_collagen_alphaI-XII-like, Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions
ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIK
NLPYKGGNTRTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKD
ADESELKMIASKPSETHVFNVADF
>gnl|CDD|238760 cd01483, E1_enzyme_family, Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS
RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVN
VTAVPEGISEDNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDIGSLSAA
EAL
>gnl|CDD|238761 cd01484, E1-2_like, Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the second repeat of Ub-E1
KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCK
VVPYQNKVGPEQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTE
CIECTLYPPQKNFPMCTIASMPRLPEHCIEWARMLQWDDPEHIQFIFQASNERASQYNIRGVTYFLTKGV
AGRIIPAVATTNAVVAGVCALEVF
>gnl|CDD|238762 cd01485, E1-1_like, Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the first repeat of Ub-E1
LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVS
NSGMNRAAASYEFLQELNPNVKLSIVEEDSLSNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIP
FISCATYGLIGYAFFDFPIAAFLGGVVAQEAIKSISGKFTPLNNLYIYDGFESTGPMC
>gnl|CDD|238763 cd01486, Apg7, Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively. This leads to the covalent conjugation of Apg8 with phosphatidylethanolamine, an important step in autophagy. Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole
KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCKGGKPKAEAAAERLKEIFPS
IDATGIVLSIPMPGHPISESEVPSTLKDVKRLEELIKDHDVIFLLTDSRESRWLPTLLSAAKNKLVINAA
LGFDSYLVMRHGAGPQSQSGSGDSSSDSIPGSRLGCYFCNDVVAPGDSLKDRTLDQQCTVTRPGLSMIAS
SIAVELLVSLLQHPLGGHAPAESSSNEGDEPTTVLGILPHQIRGFLSNFSNLTLSGQAYDQCTACSDAVI
DEYHREGWEFVLKAFNSPDYLEELTGL
>gnl|CDD|238764 cd01487, E1_ThiF_like, E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown
KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQIGEPKVEALKENLREINPFVKI
EAINIKIDENNLEGLFGDCDIVVEAFDNAETKAMLAESLLGNKNKPVVCASGMAGFGDSNNIKTKKISDN
FYICGDLVNEAKEGLGLMAPRVNICAAHQANLVL
>gnl|CDD|238765 cd01488, Uba3_RUB, Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins. consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. UBA3 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2
KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVN
VTPHFGKIQDKDEEFYRQFNIIICGLDSIEARRWINGTLVSLLLYEDPESIIPLIDGGTEGFKGHARVIL
PGITACIECSLDLFPPQVTFPLCTIANTPRLPEHCIEYASLIQWPKEFPFVPLDGDDPEHIEWLYQKALE
RAAQFNISGVTYSLTQGVVKRIIPAVASTNAIIAAACCLEALKIATDCYENLNNYLMYNGVDGCYTYTFE
HERKEDCPVCS
>gnl|CDD|238766 cd01489, Uba2_SUMO, Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. UBA2 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2
KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVK
IVAYHANIKDPDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTEC
YECQPKETPKTFPVCTIRSTPSQPIHCIVWAKSLFFLFNKVFKDDIERLLSMEELWKTRKPPVPLSWKEL
TFDKDDQDALDFVAAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKVLSGDKEQ
CRTVFLNLQPNRRKRLLVPCKLDPPNPNCYVC
>gnl|CDD|238767 cd01490, Ube1_repeat2, Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the second repeat of Ub-E1
KVFLVGAGAIGCELLKNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAM
NPDLKITALQNRVGPETEHIFNDEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQV
VIPHLTESYSSSRDPPEKSIPLCTLKNFPNAIEHTIQWARDEFEGLFKQPPENVNQYLFEDCVRWARLLF
EKYFNNNIKQLLHNFPPDAVTSDGAPFWSGPKRCPTPLEFDVNNPLHLDFVLAAANLYAEVYGIPGFEKD
DDTNFHMDFITAASNLRARNYSIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKVVDGKRPLEAY
KNAFLNLALPFFAFSEPIPAPKVKYAYDEEWTIWDRFEVKGKQTLQELLIDYFKEKYGLEVTMLSQGVSM
LYSSFMPPAKLKERL
>gnl|CDD|238768 cd01491, Ube1_repeat1, Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the first repeat of Ub-E1
LYSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDI
GKNRAEASQARLAELNPYVPVTVSTGPLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRG
LFGSIFCDFGDEFTVYDPNGEEPKSGMISSISKDNPGVVTCLDETRHGFEDGDYVTFSEVEGMTELNGCE
PRKIKVKGPYTFSIGDTSSFSEYIRGGIVTQVKLSPMAAFFGGLAAQEVLKACSGKFTPLKQWLYFDALE
CLPEDE
>gnl|CDD|238769 cd01492, Aos1_SUMO, Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. Aos1 contains part of the adenylation domain
IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAE
DLGQNRAEASLERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYA
TGVHGLFGFVFADLLAPVAAVVGGILAQDVINALSKRESPLNNFFVFDGETSEAPIY
>gnl|CDD|238770 cd01493, APPBP1_RUB, Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain
QKYDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASS
LGKSRAEATCELLQELNPDVNGSAVEESPEALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPL
LYVRSYGLYGYIRIQLKEHTIVESHPDNALEDLRLDNPFPELREHADSIDLDDMDPAEHSHTPYIVILIK
YLEKWRSAHNGQLPSTYKEKKEFRDLVRSLMRSNEDEENFEEAIKAVNKALNRTKIPSSVEEIFNDDRCE
NLTSQSSSFWIMARALKEFVAEENGLLPLPGTLPDMTADTEKYIKLQNIYREKAEKDAAEVEKYVREILK
SLGRSPDSISDKEIKLFCKNAAFLRVIRGRSLEHNISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGIRS
KSATF
>gnl|CDD|99742 cd01494, AAT_I, Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V)
KLEELEEKLARLLQPGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAELAGAKPVPVP
VDDAGYGGLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPG
VLIPEGGADVVTFSLHKNLGGEGGGVVIVK
>gnl|CDD|275447 cd01513, Translation_factor_III, Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins. Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1)
QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEKKPPDSLQPGENGTVEVEL
QKPVVLERGKEFPTLGRFALRDGGRTVGAGLI
>gnl|CDD|238772 cd01514, Elongation_Factor_C, Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of elongation factors (EFs) bacterial EF-G, eukaryotic and archeal EF-2 and eukaryotic mitochondrial mtEFG1s and mtEFG2s. This group also includes proteins similar to the ribosomal protection proteins Tet(M) and Tet(O), BipA, LepA and, spliceosomal proteins: human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and yeast counterpart Snu114p. This domain adopts a ferredoxin-like fold consisting of an alpha-beta sandwich with anti-parallel beta-sheets, resembling the topology of domain III found in the elongation factors EF-G and eukaryotic EF-2, with which it forms the C-terminal block. The two domains however are not superimposable and domain III lacks some of the characteristics of this domain. EF-2/EF-G in complex with GTP, promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome. Tet(M) and Tet(O) mediate Tc resistance. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. Yeast Snu114p is essential for cell viability and for splicing in vivo. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. The function of LepA proteins is unknown
EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSM
EFSHYEPVP
>gnl|CDD|238773 cd01515, Arch_FBPase_1, Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family (FBPase class IV). These are Mg++ dependent phosphatases. Members in this family may have both fructose-1,6-bisphosphatase and inositol-monophosphatase activity. In hyperthermophilic archaea, inositol monophosphatase is thought to play a role in the biosynthesis of di-myo-inositol-1,1'-phosphate, an osmolyte unique to hyperthermophiles
WLEIARNIAKEIEKAIKPLFGTEDASEVVKIGADGTPTKLIDKVAEDAAIEILKKLGSVNIVSEEIGVID
NGDEPEYTVVLDPLDGTYNAINGIPFYSVSVAVFKIDKSDPYYGYVYNLATGDLYYAIKGKGAYLNGKRI
KVSDFSSLKSISVSYYIYGKNHDRTFKICRKVRRVRIFGSVALELCYVASGALDAFVDVRENLRLVDIAA
GYLIAEEAGGIVTDENGKELKLKLNVTERVNIIAANSELHKKLLELL
>gnl|CDD|238774 cd01516, FBPase_glpX, Bacterial fructose-1,6-bisphosphatase, glpX-encoded. A dimeric enzyme dependent on Mg(2+). glpX-encoded FPBase (FBPase class II) differs from other members of the inositol-phosphatase superfamily by permutation of secondary structure elements. The core structure around the active site is well preserved. In E. coli, FBPase II is part of the glp regulon, which mediates growth on glycerol or sn-glycerol 3-phosphate as the sole carbon source
DRNLALELVRVTEAAALAAARWMGRGDKNAADQAAVDAMREALNGLPMRGTVVIGEGERDEAPMLYIGEE
VGTGKGPEVDIAVDPLEGTTLLAKGQPNAIAVIAVAEKGSLLHAPDMYMEKIAVGPGAKGVIDLDAPVAE
NLRAVAKALGKPVEDLTVVVLDRPRHAALIEEIREAGARIKLIPDGDVAAAIATALPGSGVDVLMGIGGA
PEGVLAAAALKCLGGEMQGRLLPRNEEERARAREMGITDPNKILTLDDLVRGDDVVFAATGITDGELLKG
VRFFGGGARTHSLVMRSKTGTVRFIDSIH
>gnl|CDD|238775 cd01517, PAP_phosphatase, PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase family, and catalyses the hydrolysis of 3'-phosphoadenosine-5'-phosphate (PAP) to AMP. In Saccharomyces cerevisiae, HAL2 (MET22) is involved in methionine biosynthesis and provides increased salt tolerance when over-expressed. Bacterial members of this domain family may differ in their substrate specificity and dephosphorylate different targets, as the substrate binding site does not appear to be conserved in that sub-set
ELEVAILAVRAAASLTLPVFRNLGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA
LGRFWVLDPIDGTKGFLRGDQFAVALALIEDGEVVLGVIGCPNLPLDDGGGGDLFSAVRGQGAWLRPLDG
SSLQPLSVRQLTNAARASFCESVESAHSSHRLQAAIKALGGTPQPVRLDSQAKYAAVARGAADFYLRLPL
SMSYREKIWDHAAGVLIVEEAGGKVTDADGKPLDFGKGRKLLNNGGLIAAPGEIHEQVLEALRE
>gnl|CDD|238776 cd01518, RHOD_YceA, Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins
GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTG
GIRCEKASAYLKERGFKNVYQLKGGILKYLE
>gnl|CDD|238777 cd01519, RHOD_HSP67B2, Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized
YSFEEVKNLPNPHPNKVLIDVREPEELKTGKIPGAINIPLSSLPDALALSEEEFEKKYGFPKPSKDKELI
FYCKAGVRSKAAAELARSLGYENVGNYPGSWLDWAA
>gnl|CDD|238778 cd01520, RHOD_YbbB, Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP /GTP binding proteins including E. coli YbbB
ITAEDLLALRKADGPLIDVRSPKEFFEGHLPGAINLPLLDDEERALVGTLYKQQGREAAIELGLELVSGK
LKRILNEAWEARLERDPKLLIYCARGGMRSQSLAWLLESLGIDVPLLEGGYKAYRKFV
>gnl|CDD|238779 cd01521, RHOD_PspE2, Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins
HFEAKLAFETDCWDVAIALKNGKPDFVLVDVRSAEAYARGHVPGAINLPHREICENATAKLDKEKLFVVY
CDGPGCNGATKAALKLAELGFPVKEMIGGLDWWKREGYAT
>gnl|CDD|238780 cd01522, RHOD_1, Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins
LTPAEAWALLQADPQAVLVDVRTEAEWKFVGGVPDAVHVAWQVYPDMEINPNFLAELEEKVGKDRPVLLL
CRSGNRSIAAAEAAAQAGFTNVYNVLEGFEGDLDAAGHRGGVNGWRF
>gnl|CDD|238781 cd01523, RHOD_Lact_B, Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with rhodanese-like domains found N-terminal of the metallo-beta-lactamase domain
LDPEDLYARLLAGQPLFILDVRNESDYERWKIDGENNTPYFDPYFDFLEIEEDILDQLPDDQEVTVICAK
EGSSQFVAELLAERGYDVDYLAGGMKAWSE
>gnl|CDD|238782 cd01524, RHOD_Pyr_redox, Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain
VQWHELDNYRADGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARI
LTQNGFKVKNLDGGYKTYST
>gnl|CDD|238783 cd01525, RHOD_Kc, Member of the Rhodanese Homology Domain superfamily. Included in this CD are the rhodanese-like domains found C-terminal of the serine/threonine protein kinases catalytic (S_TKc) domain and the Tre-2, BUB2p, Cdc16p (TBC) domain. The putative active site Cys residue is not present in this CD
ISVYDVIRLLDNSPAKLAAVDIRSSPDFRRGHIEGSINIPFSSVFLKEGELEQLPTVPRLENYKGKIIVI
VSHSHKHAALFAAFLVKCGVPRVCILDGGINALKP
>gnl|CDD|238784 cd01526, RHOD_ThiF, Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains
LKLLSPEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSLQELPLDND
KDSPIYVVCRRGNDSQTAVRKLKELGLERFVRDIIGGLKAWADKVDPTFPLY
>gnl|CDD|238785 cd01527, RHOD_YgaP, Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, and similar uncharacterized putative rhodanese-related sulfurtransferases
LTTISPNDACELLAQGAVLVDIREPDEYLRERIPGARLVPLSQLESEGLPLVGANAIIFHCRSGMRTQQN
AERLAAISAGEAYVLEGGLDAWKAAGLPV
>gnl|CDD|238786 cd01528, RHOD_2, Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains
QISVAELAEWLADEREEPVLIDVREPEELEIAFLPGFLHLPMSEIPERSKELDSDNPDKDIVVLCHHGGR
SMQVAQWLLRQGFENVYNLQGGIDAWSLEVD
>gnl|CDD|238787 cd01529, 4RHOD_Repeats, Member of the Rhodanese Homology Domain superfamily. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. Only the second and most of the fourth repeats contain the putative catalytic Cys residue. This CD aligns the 1st, 2nd, 3rd, and 4th repeats
LLADWLGEHEPGTALLDVRAEDEYAAGHLPGKRSIPGAALVLRSQELQALEAPGRATRYVLTCDGSLLAR
FAAQELLALGGKPVALLDGGTSAWVA
>gnl|CDD|238788 cd01530, Cdc25, Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR)
LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRV
LIFHCEFSSKRGPRMARHLRNLDRELNSNRYPLLYYPEIYILEGGYKNFFE
>gnl|CDD|238789 cd01531, Acr2p, Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain superfamily. Included in this CD is the Saccharomyces cerevisiae arsenate reductase protein, Acr2p, and other yeast and plant homologs
VSYISPAQLKGWIRNGRPPFQVVDVRDEDYAGGHIKGSWHYPSTRFKAQLNQLVQLLSGSKKDTVVFHCA
LSQVRGPSAARKFLRYLDEEDLETSKFEVYVLHGGFNAWESSY
>gnl|CDD|238790 cd01532, 4RHOD_Repeat_1, Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 1st repeat which does not contain the putative catalytic Cys residue
VRQALLAREEIALIDVREEDPFAQSHPLWAANLPLSRLELDAWVRIPRRDTPIVVYGEGGGEDLAPRAAR
RLSELGYTDVALLEGGLQGWRA
>gnl|CDD|238791 cd01533, 4RHOD_Repeat_2, Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 2nd repeat which does contain the putative catalytic Cys residue
ELVEAVRHTPSVSADELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDPRTPIV
VNCAGRTRSIIGAQSLINAGLPNPVAALRNGTQGWTLAG
>gnl|CDD|238792 cd01534, 4RHOD_Repeat_3, Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 3rd repeat which does not contain the putative catalytic Cys residue
IGAAELARWAAEGDRTVYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADDDGVRAD
MTASWLAQMGWEVYVLEGGLAAALA
>gnl|CDD|238793 cd01535, 4RHOD_Repeat_4, Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 4th repeat which, in general, contains the putative catalytic Cys residue
TLAAWLGEGGQTAVVDVTASANYVKRHIPGAWWVLRAQLAQALEKLPAAERYVLTCGSSLLARFAAADLA
ALTVKPVFVLEGGTAAWIAAGLPVESGETRLASPRIDRYRRPYEGTDNPREAMQAYLDWEFGLVEQLGRD
GTHGF
>gnl|CDD|380478 cd01536, PBP1_ABC_sugar_binding-like, periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins
KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALV
PAVKKANAAGIPVVAVDTDIDGGGDVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDR
TKGFKEALKKYPDIEIVAEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTGDI
KIVGVDGTPEALKAIKDGELDATVAQDPYLQGYLAVEAAVKLLNGEKVPKEILTPVTL
>gnl|CDD|380479 cd01537, PBP1_repressor_sugar_binding-like, Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems. Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor
RIGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAG
VAEKARGQNVPVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGV
IKELNDKGIKTEQLQLDTGDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDIS
VFGYDALPEALKSGPLLTTILQDANNLGKTTFDLLLNLADNWKIDNKVVRVPYVL
>gnl|CDD|380480 cd01538, PBP1_ABC_xylose_binding-like, periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. Periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR
KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALS
PVVAEAKAEGIKVIAYDRLILNADVDYYISFDNEKVGELQAQALLDAKPEGNYVLIGGSPTDNNAKLFRD
GQMKVLQPAIDSGKIKVVGDQWVDDWLPANAQQIMENALTANGNNVDAVVASNDGTAGGAIAALKAQGLS
GGVPVSGQDADLAAIKRILAGTQTMTVYKDIRLLADAAAEVAVALMRGEKPPINGTTNNGLKDVPSYLLE
PVV
>gnl|CDD|380481 cd01539, PBP1_GGBP, periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR
IKIGVFIYNYDDTFISSVRKALEKAAKAGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTA
AQTIIDKAKAANIPVIFFNREPSREDLKSYDKAYYVGTDAEESGIMQGEIIADYWKANPEIDKNGDGKIQ
YVMLKGEPGHQDAIARTKYSVKTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKYGDKIELVIANNDD
MALGAIEALKAAGYNTGDGDKYIPVFGVDATPEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKE
PLETGYKFLVEGKYVRIPYKKV
>gnl|CDD|380482 cd01540, PBP1_arabinose_binding, periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR
KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDQKLGP
AIAAKAKAAGIPVIAVDDQLVDADPMKIVPFVGIDAYKIGEAVGEWLAKEMKKRGWDDVKEVGVLAITMD
TLSVCVDRTDGAKDALKAAGFPEDQIFQAPYKGTDTEGAFNAANAVITAHPEVKHWLVVGCNDEGVLGAV
RALEQAGFDAEDIIGVGIGGYLAADEEFKKQPTGFKASLYISPDKHGYIAAEELYNWITDGKPPPAETLT
DGVIVTRDNYKEVM
>gnl|CDD|380483 cd01541, PBP1_AraR, ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKSALPN
PNLDLYEELQKKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIFKSDDLQGVERYQ
GFIKALREAGLPIDDDRILWYSTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRV
PEDLSVVGFDDSYLASLSEPPLTSVVHPKEELGRKAAELLLRMIEEGRKPESVIFPPELIERES
>gnl|CDD|380484 cd01542, PBP1_TreR-like, ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEH
RKALKKLKIPVVVLGQEHEGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDEEDIAVGVARKQGYLDA
LKEHGIDEVEIVETDFSMESGYEAAKELLKENKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGG
YDLSEFVSPSLTTVKFDYEEAGEKAAELLLDMIEGEKVPKKQKLPYELI
>gnl|CDD|380485 cd01543, PBP1_XylR, ligand-binding domain of DNA transcription repressor specific for xylose (XylR). Ligand-binding domain of DNA transcription repressor specific for xylose (XylR), a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of XylR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
RVALLLETSRGYGRRLLRGIARYAREHGPWSLYLEPPGYEELLDLLKGWKGDGIIARLDDPELAEALRRL
GIPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFRNAAWSRERGEGFREALREAGYE
CHVYESPPSGSSRSWEEEREELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDE
LICELSSPPLSSIALDAEQIGYEAAELLDRLMRGERVPPEPILIPPLGVVTRQST
>gnl|CDD|380486 cd01544, PBP1_GalR, ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are structurally homologous to the periplasmic sugar binding of ABC-type transport systems
TIGIIQWYSEEEELEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLESLLEKVDGIIAIGKFSKEEIEK
LKKLNPNIVFVDSNPDPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSDDGEEIEDPRLRAF
REYMKEKGLYNEEYIYIGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISI
ISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVRLLLERINGGRTIPKKVLLPTKLIERES
>gnl|CDD|380487 cd01545, PBP1_SalR, ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
LIGLLYDNPSASYVSALQVGALRACREAGYHLVVEPCDSDDEDLADRLRRFLSRSRPDGVILTPPLSDDP
ALLDALDELGIPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGF
RDALAEAGLPLDPDLVVQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLS
VAGFDDSPIARLVWPPLTTVRQPIAEMARRAVELLIAAIRGAPAGPERETLPHELVIRES
>gnl|CDD|238794 cd01553, EPT_RTPC-like, This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate cyclase family (RTPC). These 2 families differ in that EPT is formed by 3 repeats of an alpha-beta structural domain while RTPC has 3 similar repeats with a 4th slightly different domain inserted between the 2nd and 3rd repeat. They evidently share the same active site location, although the catalytic residues differ
LDGAGGKGGGQILRSFLVLAAISGGPITVTGIRPDRAKPGLLRQHLTFLKALEKICGATVEGGELGSDRI
SFRPGTVRGGDVRFAIGSAGSCTDVLQTILPLLLFAKGPTRLTVTGGTDNPSAPPADFIRFVLEPELAKI
GAHQEETLLRHGFYPAGGGVVATEVSPVEKLNTAQLRQLVLPMLLASGAVEFTVAHPSCHLLTNFAVLEA
L
>gnl|CDD|238795 cd01554, EPT-like, Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine enolpyruvyl transferase. Both enzymes catalyze the reaction of enolpyruvyl transfer
LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMAGL
KAPQNALNLGNSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLK
GGKNLGPIHYEDPIASAQVKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQ
GPQKLTGQKYVVPGDISSAAFFLVAAAIAPGRLVLQNVGINETRTGIIDVLRAMGAKIEIGEDTISVESS
DLKATEICGALIPRLIDELPIIALLALQAQGTTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGM
IIKGKEKLHGARVNTFGDHRIGMMTALAALVADGEVELDRAEAINTSYPSFFDDLESL
>gnl|CDD|238796 cd01555, UdpNAET, UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan, a component of the bacterial cell wall. The reaction is phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine. This enzyme is of interest as a potential target for anti-bacterial agents. The only other known enolpyruvyl transferase is the related 5-enolpyruvylshikimate-3-phosphate synthase
LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENTLVIDASNINS
TEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAG
RLKGARIYLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVE
RLHGAEHTVIPDRIEAGTFLVAAAITGGDITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGRL
KAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFENRFMHVDELNRMGADIKVEGNTAIIRGVTK
LSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRAL
>gnl|CDD|238797 cd01556, EPSP_synthase, EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase (5-enolpyruvylshikimate-3-phosphate synthase) (EC 2.5.1.19) catalyses the reaction between shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form 5-enolpyruvylshkimate-3-phosphate (EPSP), an intermediate in the shikimate pathway leading to aromatic amino acid biosynthesis. The reaction is phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. It is found in bacteria and plants but not animals. The enzyme is the target of the widely used herbicide glyphosate, which has been shown to occupy the active site. In bacteria and plants, it is a single domain protein, while in fungi, the domain is found as part of a multidomain protein with functions that are all part of the shikimate pathway
LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGGGLGL
PPEAVLDCGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGG
GGLKGGEVEIPGAVSSQFKSALLLAAPLAEGPTTIIIGELESKPYIDHTERMLRAFGAEVEVDGYRTITV
KGGQKYKGPEYTVEGDASSAAFFLAAAAITGSEIVIKNVGLNSGDTGIIDVLKEMGADIEIGNEDTVVVE
SGGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGL
IIEGGPLKGAGVEVYTYGDHRIAMSFAIAGLVAEGGVTIEDPECVAKSFPNFFEDLESL
>gnl|CDD|238798 cd01557, BCAT_beta_family, BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leusine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two foms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism.Members of this subgroup are widely distributed in all three forms of life
SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDA
DWVPYGGGASLYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGEKGVSALVSSFRRAAPGGPGAA
KAGGNYAASLLAQKEAAEKGYDQALWLDGAHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILE
LARDLGIKVEERPITRDELYEADEVFATGTAAVVTPVGEIDYRGKEPGEGEVGPVTKKLYDLLTDIQYG
>gnl|CDD|238799 cd01558, D-AAT_like, D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes transamination between D-amino acids and their respective alpha-keto acids. It plays a major role in the synthesis of bacterial cell wall components like D-alanine and D-glutamate in addition to other D-amino acids. The enzyme like other members of this superfamily requires PLP as a cofactor. Members of this subgroup are found in all three forms of life
YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELI
RELVAKNEGGEGDVYIQVTRGVGPRGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVPDIRWLRCD
IKSLNLLNNVLAKQEAKEAGADEAILLDADGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIEL
AKELGIPVEERPFSLEELYTADEVFLTSTTAEVMPVVEIDGRPIGDGKPGPVTKRLREAY
>gnl|CDD|238800 cd01559, ADCL_like, ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria
DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAANDIDEGRIRLIL
SRGPGGRGYAPSVCPGPALYVSVIPLPPAWRQDGVRLITCPVRLGEQPLLAGLKHLNYLENVLAKREARD
RGADEALFLDTDGRVIEGTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDL
LAADEAFLTNSLLGVAPVTAIDDHDGPPGPLTRALRELL
>gnl|CDD|107203 cd01560, Thr-synth_2, Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, archaebacteria and eubacterial groups. This CD, Thr-synth_2, includes enzymes from fungi and eubacterial groups, as well as, metazoan threonine synthase-like proteins
KYVSTRGGNPGVSFSEALLSGLAPDGGLYVPEELPKLSAEEIASWSGLSYQELAFEVLSLFIGDEIPEDD
LKSLIDRAYSFFRHPDIAPLVQLGDNLYVLELFHGPTLAFKDMALQFLGRLLEYFLKRRNERITILVATS
GDTGSAAIEGFRGKPNVDVVVLYPKGGVSPIQELQMTTLPADNVHVVAVEGDFDDCQSLVKALFADEDFN
KKLKLSSANSINWARILAQIVYYFYAYLQLLKRGEGEKVEFSVPTGNFGNILAGYYAKKMGLPIKKLIVA
TNENDVLRRFFKTGRYDRRESLKQTLSPAMDILKSSNFERLLFLLAGRDRTKVKMLMEEFEATGFLSLPK
EELKKLREDFSSGSVSDEETLETIREVYEETGYLIDPHTAVGVRAAERVRKSPGTPGVVLSTAHPAKFPE
AVKEALGEEPVELPEELEGLEDLEKRHEDLLADKELLKSH
>gnl|CDD|107204 cd01561, CBS_like, CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine
GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAM
VAAAKGYRFIIVMPETMSEEKRKLLRALGAEVILTPEAEADGMKGAIAKARELAAETPNAFWLNQFENPA
NPEAHYETTAPEIWEQLDGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHK
IEGIGAGFIPENLDRSLIDEVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVT
ILPDSGERYLS
>gnl|CDD|107205 cd01562, Thr-dehyd, Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions
LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVA
ASAGNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFI
HPFDDPDVIAGQGTIGLEILEQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSL
AAGKPVTLPEVDTIADGLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALA
ALLSGKLDLKGKKVVVVLSGGNID
>gnl|CDD|107206 cd01563, Thr-synth_1, Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants
LWRYRELLPVTEDDIVSLGEGNTPLVRAPRLGERLGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV
KAVACASTGNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEEN
WIYLSNSLNPYRLEGQKTIAFEIAEQLGWEVPDYVVVPVGNGGNITAIWKGFKELKELGLIDRLPRMVGV
QAEGAAPIVRAFKEGKDDIEPVENPETIATAIRIGNPASGPKALRAVRESGGTAVAVSDEEILEAQKLLA
RTEGIFVEPASAASLAGLKKLREEGIIDKGERVVVVLTGHGLKD
>gnl|CDD|238801 cd01567, NAPRTase_PncB, Nicotinate phosphoribosyltransferase (NAPRTase) family. Nicotinate phosphoribosyltransferase catalyses the formation of NAMN and PPi from 5-phosphoribosy -1-pyrophosphate (PRPP) and nicotinic acid, this is the first, and also rate limiting, reaction in the NAD salvage synthesis. This salvage pathway serves to recycle NAD degradation products
LLDTDLYKLTMMQAYLYPYPNTRVVFEFTFRSNPFGGDYIVFAGLEEVLKLLENLRFTEEEIEYLKKLLI
FGEFFLYLLFLGKLPLEIYALPEGTVVFPKEPLLTIEGPWPEAGLLETPLLAIWNEATSIATKAARKKLA
AGGLLETKDNLEELGFKLHDFGTRRRHSPEAALSGGRAALIGGFGGTSNVAAAKKLGIPPIGTMAHSWIQ
AFGALEEAAFEAFARWLPQFGGGLGIALIDTYDTDNGFLNALKLAKALGAGGGLLGVRLDSGDPVELIKK
VRKHLDELGIDLNKKKIIISGDLDTEEAIELLLEQGASPNDAFGVGTSLTNDLGRPPLGFVYK
>gnl|CDD|238802 cd01568, QPRTase_NadC, Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other
DALLDRALAEDLGYGDLTTEALIPGDAPATATLIAKEEGVLAGLEVAEEVFELLDGIEVEWLVKDGDRVE
AGQVLLEVEGPARSLLTAERVALNLLQRLSGIATATRRYVEAARGTKARIADTRKTTPGLRLLEKYAVRA
GGGDNHRLGLSDAVLIKDNHIAAAGGITEAVKRARAAAPFEKKIEVEVETLEEAEEALEAGADIIMLDNM
SPEELKEAVKLLKGLPRVLLEASGGITLENIRAYAETGVDVISTGALTHSAPALDISLK
>gnl|CDD|238803 cd01569, PBEF_like, pre-B-cell colony-enhancing factor (PBEF)-like. The mammalian members of this group of nicotinate phosphoribosyltransferases (NAPRTases) were originally identified as genes whose expression is upregulated upon activation in lymphoid cells. In general, nicotinate phosphoribosyltransferase catalyses the formation of NAMN and PPi from 5-phosphoribosy -1-pyrophosphate (PRPP) and nicotinic acid, this is the first, and also rate limiting, reaction in the NAD salvage synthesis
LLATDSYKVSHRLQYPPGTTAVYSYLEPRGGKYYDQTVFFGLQYFLKKYLIDPVNRDFFIDEAEAVFEAH
FGMNDLPFNEDGWRHILELHDGYLPIEIRAVPEGTVVPTKNVLMTVENTDPDFFWLTNYLETILLRNVWY
PSTVATISREYKKILRKYAKETSDNLEFLPFQLHDFGMRGMSSLESAALGGAAHLVNFKGTDTIPALDAA
YAYYYEDPMAGFSIPAAEHSTMTAWGRERELEAFRNLLEQFGPGIVSVVSDSYDFWNALTLWGPRLKDEI
LARGGTLVIRPDSGDPVDIICGVLEILGEIFGGTVNSKGYKVLNPHVRIIQGDGITLERIEEILERLKAK
GFASENIVFGMGGGLLQKVTRDTQGFAMKASAIEINGKWRDVFKDPKTDPGKKSKKG
>gnl|CDD|238804 cd01570, NAPRTase_A, Nicotinate phosphoribosyltransferase (NAPRTase), subgroup A. Nicotinate phosphoribosyltransferase catalyses the formation of NAMN and PPi from 5-phosphoribosy -1-pyrophosphate (PRPP) and nicotinic acid, this is the first, and also rate limiting, reaction in the NAD salvage synthesis. This salvage pathway serves to recycle NAD degradation products. This subgroup is present in bacteria and eukaryota (except funghi)
ALLTDLYQLTMAQAYWKEGKHNKPAVFELFFRKLPFGGGYAVFAGLEELLEYLENFRFTEEDIDYLRSLG
IFDEEFLDYLRGFRFTGTIYAIPEGEVVFPNEPLLTVEGPLIEAQLLETLLLNLINFQTLIATKAARVRL
AAGGRPLLEFGLRRAQGPDAALSAARAAYIGGFDGTSNVLAGKLYGIPVSGTMAHSFVQAFDDELAAFRA
FAEAYPDNFTLLVDTYDTLRSGLPNAIAVAKELGALGYRLVGVRIDSGDLAYLSKEARKMLDEAGLTKVK
IVASNDLDEYTIAALNAQGAPIDAFGVGTRLVTSQSQPALGGVYKLV
>gnl|CDD|238805 cd01571, NAPRTase_B, Nicotinate phosphoribosyltransferase (NAPRTase), subgroup B. Nicotinate phosphoribosyltransferase catalyses the formation of NAMN and PPi from 5-phosphoribosy -1-pyrophosphate (PRPP) and nicotinic acid, this is the first, and also rate limiting, reaction in the NAD salvage synthesis. This salvage pathway serves to recycle NAD degradation products
GRFTDVYFLRTRKILEKKGPNPTVTMEFTQRSLPWAVLCGLEEVLALLEGLPVKVYALPEGTIFNPKEPV
LRIEGPYQDFGELETAILGILARASSIATNAARVKLAAGDKPVISFGDRRDHPAIQPMDGRAAYIGGCDG
VSTVLGAELLGEKPSGTMPHALIQIFGGDQVEAWKAFDETYPEDVPRIALIDTFNDEKEEALKAAKALGD
KLDGVRLDTPSSRRGVFRYLIREVRWALDIRGYKHVKIFVSGGLDEEDIKELEDVGVDAFGVGTAISKAP
PVDFTMDIVEVNGQPIAKRGKL
>gnl|CDD|238806 cd01572, QPRTase, Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other
DAIVRLALAEDLGRGDITSEAIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEVEWLVKDGDRV
EPGQVLATVEGPARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVR
CGGGDNHRFGLSDAVLIKDNHIAAAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDN
MSPEELREAVALLKGRVLLEASGGITLENIRAYAETGVDYISVGALTHSAPALDISLD
>gnl|CDD|238807 cd01573, modD_like, ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC operons in bacteria, which are involved in molybdate transport. In general, QPRTases are part of the de novo synthesis pathway of NAD in both prokaryotes and eukaryotes. They catalyse the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide
DAELERLLLEDAPYGDLTTEALGIGEQPGKITFRARDPGVLCGTEEAARILELLGLEVDLAAASGSRVAA
GAVLLEAEGPAAALHLGWKVAQTLLEWASGIATATAEMVAAARAVNPDIVVATTRKAFPGTRKLALKAIL
AGGAVPHRLGLSETILVFAEHRAFLGGPEPLKALARLRATAPEKKIVVEVDSLEEALAAAEAGADILQLD
KFSPEELAELVPKLRSLAPPVLLAAAGGINIENAAAYAAAGADILVTSAPYYAKPADIKVKI
>gnl|CDD|380488 cd01574, PBP1_LacI, ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators. Ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of LacI is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVDEDDPASVREALDRLLSQRVDGIIVIAPDEAVL
EALRRLPPGLPVVIVGSGPSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWRE
ALEEAGLPPPPVVEGDWSAASGYRAGRRLLDDGPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFD
DIPEAAYFVPPLTTVRQDFAELGRRAVELLLALIEGPAPPPESVLLPPELVVRES
>gnl|CDD|380489 cd01575, PBP1_GntR, ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators. This group represents the ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of GntR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding, which in turn changes the DNA binding affinity of the repressor
LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPAT
RKLLRAAGIPVVETWDLPDDPIDMAVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSRARQRLEGFR
DALAEAGLPLPLVLLVELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAI
AGFGDLDIAAALPPALTTVRVPRYEIGRKAAELLLARLEGEEPEPRVVDLGFELVRRES
>gnl|CDD|238808 cd01576, AcnB_Swivel, Aconitase B swivel domain. Aconitate hydratase B is involved in energy metabolism as part of the TCA cycle. It catalyses the formation of cis-aconitate from citrate. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The domain structure of Aconitase B is different from other Aconitases in that he swivel domain that is found at N-terminus of B family is normally found at C-terminus for other Aconitases. In most members of the family, there is also a HEAT domain before domain 4, which is believed to play a role in protein-protein interaction
FKVPGETNTDDLSPAPDAWSRPDIPLHALAMLKNKREGEIVAIAQLKPKGHPVAYVGDVVGTGSSRKSAT
NSVLWHTGKDIPFVPNKRAGGVVLGGKIAPIFFNTAEDSGALPIQLDVSVLDMGDILNIDG
>gnl|CDD|238809 cd01577, IPMI_Swivel, Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism
LFGDNIDTDQIIPARFLGDIIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVT
LADEDVEEVEAKPGDEVEVDL
>gnl|CDD|238810 cd01578, AcnA_Mitochon_Swivel, Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members
KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIK
WVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDI
LGLTDFAPG
>gnl|CDD|238811 cd01579, AcnA_Bact_Swivel, Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known
KVGDNITTDHIMPAGAKVLPLRSNIPAISEFVFHRVDPTFAERAKAAGPGFIVGGENYGQGSSREHAALA
PMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLELPL
>gnl|CDD|238812 cd01580, AcnA_IRP_Swivel, Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism
LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEG
GTTHHPPTGEVMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNL
VGMGILPLQFPPGENADSLGLTGEETYDIIG
>gnl|CDD|153131 cd01581, AcnB, Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3
LAQKIVGRACGVKGVRPGTYCEPKMTTVGSQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVD
VKTHRTLPDFISNRGGVALRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGV
MPLDMPESVLVRFKGKMQPGITLRDLVNAIPYYAIQQGLLTVEKKGKKNVFNGRILEIEGLPDLKVEQAF
ELTDASAERSAAACTVRLDKEPVIEYLESNVVLMKIMIANGYDDARTLLRRIIAMEEWLANPPLLEPDAD
AEYAAVIEIDLDDIKEPILACPNDPDDVKLLSEVAGKKIDEVFIGSCMTNIGHFRAAAKILRGKEFKPTR
LWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQARVADGATVFSTSTRNFDNRVGKGAEVY
LGSAELAAVCALLGRI
>gnl|CDD|153132 cd01582, Homoaconitase, Homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase catalytic domain. Homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases
HCMTHDNSWPVALKFMSIGATKIHNPDQIVMTLDHDVQNKSEKNLKKYKNIESFAKKHGIDFYPAGRGIG
HQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGV
TGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAKHLILDLSTLS
PYVSGPNSVKVSTPLKELEAQNIKINKAYLVSCTNSRASDIAAAADVVKGKKEKNGKIPVAPGVEFYVAA
ASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVGISATNRNFKGRMGSTEALAYLAS
PAVVAASAISGKI
>gnl|CDD|153133 cd01583, IPMI, 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate. Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes
LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGINFFDVGRQG
ICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPP
GVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGR
GKAYWKELKSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEGIKIDQVFIGSCTNGRLEDLRAA
AEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTS
NRNFKGRMGSPGARIYLASPATAAASAITGEI
>gnl|CDD|153134 cd01584, AcnA_Mitochondrial, Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Mitochondrial aconitase A catalytic domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediary product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members
RVAMQDATAQMALLQFMSSGLPKVAVPSTIHCDHLIEAQVGGEKDLKRAKDINKEVYDFLASAGAKYGIG
FWKPGSGIIHQIVLENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKL
TGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMK
KYLKATGRAEIADLADEFKDDLLVADEGAEYDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGW
PLDLRVGLIGSCTNSSYEDMGRAASIAKQALAHGLKCKSIFTITPGSEQIRATIERDGLLQTFRDAGGIV
LANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPATHAFVASPEIVTAMAIAGTL
>gnl|CDD|153135 cd01585, AcnA_Bact, Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Bacterial Aconitase-like catalytic domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This distinct subfamily is found only in bacteria and Archaea. Its exact characteristics are not known
DQTLTQDATGTMAYLQFEAMGVDRVRTELSVSYVDHNTLQTDFENADDHRFLQTVAARYGIYFSRPGNGI
CHQVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWV
TAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGR
EDDWVELAADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVREVAGIKVDQVAIGSCTNSSYEDLMTVA
AILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQAPPTGGVSVRTFNR
NFEGRSGTKDDLVYLASPEVAAAAALTGVI
>gnl|CDD|153136 cd01586, AcnA_IRP, Aconitase A catalytic domain. Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes
RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNR
ERYEFLKWGQKAFKNLRVVPPGTGIIHQVNLEYLARVVFTSEEDGDGVAYPDSVVGTDSHTTMINGLGVL
GWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAK
LSVADRATIANMAPEYGATCGFFPVDTQVVELDLSTVEPSVSGPKRPQDRVPLHGSVVIAAITSCTNTSN
PSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSGP
LPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLVVAYALAGTV
>gnl|CDD|176466 cd01594, Lyase_I_like, Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively
VRADLLVELAAALALVEEVLAGRAGELAGGLHGSALVHKGRSSNDIGTTALRLALRDALDDLLPLLKALI
DALALKAEAHKGTVMPGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEAAVAEALDALALAAAHLSKIA
EDLRLLLSGEFGELGEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNEDSP
SMREILADSLLLLIDALRLLL
>gnl|CDD|176467 cd01595, Adenylsuccinate_lyase_like, Adenylsuccinate lyase (ASL)_like. This group contains ASL, prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting
MRAIFSEENKLRTWLDVEAALAEAQAELGLIPKEAAEEIRAAADVFEIDAERIAEIEKETGHDVIAFVYA
LAEKCGEDAGEYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHA
LPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISGAVGTHASLGPKGPEVEERVAEKLGLKVPPITTQ
IEPRDRIAELLSALALIAGTLEKIATDIRLLQRTEIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLAR
LVRALAAPALENLVQWHERDLSDSSVERNILPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLI
LSEAVMMALAKKGLGRQEAYELVKEENYLGL
>gnl|CDD|176468 cd01596, Aspartase_like, aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle
RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIV
QACDEVIAGKLDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFP
PAAHIAAALALLERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARI
EAALERLRELNLGGTAVGTGLNAPPGYAEKVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLA
VSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGKVNPVIPEAVNMVAAQVIGNDTAITMAGSAGQ
LELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVENSLMLVTALNPHIGYEKAAEIA
KEALKEGRTLREAALELGLLTEEELDEILD
>gnl|CDD|176469 cd01597, pCLME, prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like. This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms
LLGDLFGTPAMREIFSDENRVQAMLDVEAALARAQAELGVIPKEAAAEIAAAADVERLDLEALAEATART
GHPAIPLVKQLTAACGDAAGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTP
MVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGGAAGTLASLGDQGLAVQEALAAEL
GLGVPAIPWHTARDRIAELASFLALLTGTLGKIARDVYLLMQTEIGEVAEPFAKGRGGSSTMPHKRNPVG
CELIVALARRVPGLAALLLDAMVQEHERDAGAWHAEWIALPEIFLLASGALEQAEFLLSGLEVNEDRMRA
NLDLTGGLILSEAVMMALAPKLGRQEAHDLVYEACMRAVEEGRPLREVLLEDPEVAAYLSDEELDALLDP
ANYLGSAPALVDRVLAR
>gnl|CDD|176470 cd01598, PurB, PurB_like adenylosuccinases (adenylosuccinate lyase, ASL). This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP)
LRPYFSEYALIKYRVQVEVEWLIALSNLEEIPEVPPLTKEELKFLRAIIENFSEEDALRIKEIEATTNHD
VKAVEYFLKEKFETLGLLKKIKEFIHFACTSEDINNLAYALMIKEARNEVILPLLKEIIDSLKKLAKEYA
DVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQIEILGKFNGAVGNFNAHLVAYPDVDWRKFSEF
FVTSLGLTWNPYTTQIEPHDYIAELFDALARINTILIDLCRDIWGYISLGYFKQKVKKGEVGSSTMPHKV
NPIDFENAEGNLGLSNALLNHLSAKLPISRLQRDLTDSTVLRNIGVAFGHSLIAYKSLLRGLDKLELNEA
RLLEDLDANWEVLAEPIQTVMRRYGIPNPYEKLKDLTRGKRIDKETLKEFIDSLDIPEEAKAELLALTPA
NYIGL
>gnl|CDD|259845 cd01609, RNAP_beta'_N, Largest subunit (beta') of bacterial DNA-dependent RNA polymerase (RNAP), N-terminal domain. Beta' is the largest subunit of bacterial DNA-dependent RNA polymerase (RNAP). This family also includes the eukaryotic plastid-encoded RNAP beta' subunit. Bacterial RNAP is a large multi-subunit complex responsible for the synthesis of all RNAs in the cell. Structure studies suggest that RNA polymerase complexes from different organisms share a crab-claw-shaped structure with two "pincers" defining a central cleft. Beta' and beta, the largest and the second largest subunits of bacterial RNAP, each makes up one pincer and part of the base of the cleft. Beta' contains part of the active site and binds two zinc ions that have a structural role in the formation of the active polymerase
LDFDAIRISLASPEQIRSWSHGEVTKPETINYRTLKPEKDGLFCERIFGPTKDYECACGKYKRIRYKGII
CDRCGVEVTRSKVRRERMGHIELAAPVAHIWFFKGLPSRIGLLLDLSPKDLERVIYFVVESFRKSGNRPE
WMILTVLPVIPPDLRPMVQLDGGRFATSDLNDLYRRVINRNNRLKKLLELGAPEIIVRNEKRMLQEAVDA
LIDNGRRGKPVTGANNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHQCGLPKEMALE
LFKPFVIRELIERGLAPNIKSAKKMIERKDPEVWDILEEVIKGHPVLLNRAPTLHRLGIQAFEPVLIEGK
AIQLHPLVCTAFNADFDGDQMAVHVPLSLEAQAEARVLMLSSNNILSPASGKPIVTPSQDMVLGLYYLTK
ERKGDKGEGIIETTVGRVIFNEILPEGLPFINKTLKKKVLKKLINECYDRYGLEETAELLDDIKELGFKY
ATRSGISISIDDIVVPPEKKEIIKEAEEKVKEIEKQYEKGLLTEEERYNKVIEIWTEVTEKVADAMMKNL
DKDPFNPIYMMADSGARGSKSQIRQLAGMRGLMAKPSGKIIELPIKSNFREGLTVLEYFISTHGARKGLA
DTALKTADSGYLTRRLVDVAQDVIVTEED
>gnl|CDD|238813 cd01610, PAP2_like, PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, includes type 2 phosphatidic acid phosphatase or lipid phosphate phosphatase (LPP), Glucose-6-phosphatase, Phosphatidylglycerophosphatase B and bacterial acid phosphatase, vanadium chloroperoxidases, vanadium bromoperoxidases, and several other mostly uncharacterized subfamilies. Several members of this superfamily have been predicted to be transmembrane proteins
RRLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDGDPLLLTEGGYSFPSGHAAFAFALALFLAL
LLPRRLLRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL
>gnl|CDD|340453 cd01611, Ubl_Autophagy_like, ubiquitin-like (Ubl) domain found in autophagy-related ubiquitin-like protein. Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. The autophagy-related ubiquitin-like proteins, such as Saccharomyces cerevisiae Atg8p, undergo a unique ubiquitin-like (Ubl) conjugation, a process essential for autophagosome formation. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. ATG8 family proteins undergo multistep modifications by the E1-like (ubiquitin activating) enzyme ATG7, and the E2-like (ubiquitin conjugating) enzyme ATG3. The mammalian ATG8 family is classified into three subfamilies: i) MAP1LC3 (microtubule associated protein 1 light chain 3) which includes MAP1LC3A, MAP1LC3B, MAP1LC3B2, and MAP1LC3C, ii) GABARAP (GABA type A receptor associated protein) which includes GABARAP, GABARAPL1, and GABARAPL3, and iii) GABARAPL2 (GABA type A receptor associated protein like 2), also known as GATE-16 (golgi-associated adenosine triphosphatase enhancer of 16 kDa)
KIPVILEKAGKTKIPILDKKKYLVPRDLTVGQLIDFIRKRLKLVAEEALFIFVNQFAPPTSAEMGTLYEE
HGDEDGFLYLHYSK
>gnl|CDD|340454 cd01612, Ubl_ATG12, ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12). Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. The autophagy-related ubiquitin-like (Ubl) proteins such as ATG12 protein have a conserved Ubl fold structure and undergo a unique Ubl conjugation, a process essential for autophagosome formation. ATG12 is conjugated to ATG5 by multistep modifications of the E1-like (ubiquitin activating) enzyme ATG7, and the E2-like (ubiquitin conjugating) enzyme ATG10. The ATG12-ATG5 conjugate facilitates the lipidation of ATG8 and directs its correct subcellular localization. ATG12 is localized at the developing autophagosome
KVVVLFKAVGDAPILKQKKFKVSASQKFASVIDFLRKQLKLKPSESLFLYINQSFAPSPDEEVGDLYDCF
GSNGKLVLNYCKTPAW
>gnl|CDD|133473 cd01614, EutN_CcmL, Ethanolamine utilisation protein and carboxysome structural protein domain family. Beside the Escherichia coli ethanolamine utilization protein EutN and the Synechocystis sp. carboxysome (beta-type) structural protein CcmL, this family also includes alpha-type carboxysome structural proteins CsoS4A and CsoS4B (previously known as OrfA and OrfB), propanediol utilizationprotein PduN, and some hypothetical homologous of various bacterial microcompartments. The carboxysome, a polyhedral organelle, participates in carbon fixation by sequestering enzymes. It is the prototypical bacterial microcompartment. Its enzymatic components, ribulose bisphosphate carboxylase/oxygenase(RuBisCO) and carbonic anhydrase (CA), are surrounded by a polyhedral protein shell. Similarly, the ethanolamine utilization (eut) microcompartment, and the 1,2-propanediol utilization (pdu) microcompartment encapsulate the enzymes necessary for the process of cobalamin-dependent ethanolamine degradation, and coenzyme B12-dependent degradation of 1,2-propanediol, respectively, within its polyhedral protein shells. It is interesting that both carboxysome structural proteins CcmL and CsoS4A assemble as pentamers in the crystal structures, which might constitute the twelve pentameric vertices of a regular icosahedral carboxysome. However, the reported EutN structure is hexameric rather than pentameric. The absence of pentamers in Eut microcompartments might lead to less-regular icosahedral shell shapes. Due to the lack of structure evidence, the functional roles of the CsoS4A adjacent paralog, CsoS4B, and propanediol utilization protein PduN are not yet clear
MLIARVIGTVVATRKHPSLAGKKLLVVQPLDGEGKPKGEPLVAVDPVGAGVGEWVLVATGSAARQAFGDK
DVPIDAAIIGIID
>gnl|CDD|119367 cd01615, CIDE_N, CIDE_N domain, found at the N-terminus of the CIDE (cell death-inducing DFF45-like effector) proteins, as well as CAD nuclease (caspase-activated DNase/DNA fragmentation factor, DFF40) and its inhibitor, ICAD(DFF45). These proteins are associated with the chromatin condensation and DNA fragmentation events of apoptosis; the CIDE_N domain is thought to regulate the activity of ICAD/DFF45, and the CAD/DFF40 and CIDE nucleases during apoptosis. The CIDE-N domain is also found in the FSP27/CIDE-C protein
PLRPFKVCDSDRSRKKGVAASSLEELLSKACEKLKLPSAPVTLVLEEDGTEVDDEEYFQTLPDNTVLMLL
EPGQKWTP
>gnl|CDD|340455 cd01616, TGS, TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold. This family includes eukaryotic and some bacterial threonyl-tRNA synthetases (ThrRSs), a distinct Obg family GTPases, and guanosine polyphosphate hydrolase (SpoT) and synthetase (RelA), which are involved in stringent response in bacteria, as well as uridine kinase (UDK) from Thermotogales. All family members contain a TGS domain named after the ThrRS, GTPase, and SpoT/RelA proteins where it occurs. It is a small domain with a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. The functions of the TGS domain remains unclear, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, with a regulatory role
EVFTVGKTPGTVFVMNKGATAYSCAMHLHEDYCRKSILALVDGQLWDMYYPLTKGDEIKFL
>gnl|CDD|340456 cd01617, DCX, Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold. Dublecortin (DCX) is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its DCX protein domains can occur in double tandem or as single DCX repeats. Proteins with DCX tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK). Single DCX repeat proteins are normally localized to actin-rich subcellular structures, or the nucleus such as DCDC2. DCX is not only a unique MAP in terms of structure, it also interacts with multiple additional proteins. Mutations in human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation
KRITVFRNGDKNFKGVKVLVKPRRFRTFDQLLDELTEKLGLPTGGVRKLYTPSGKLVKSLSDLEDGESYV
VCG
>gnl|CDD|240620 cd01619, LDH_like, D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains. D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain
MKVLIYDYRDDELEIEKEILKAGGVDVEIVTYLLNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKF
ISLRATGYDNIDLDYAKELGIGVTNVPEYSPNAVAEHTIALILALLRNRKYIDERDKNQDLQDAGVIGRE
LEDQTVGVVGTGKIGRAVAQRAKGFGMKVIAYDPFRNPELEDKGVKYVSLEELFKNSDIISLHVPLTPEN
HHMINEEAFKLMKKGVIIINTARGSLVDTEALIEALDSGKIFGAGLDVLEDETPDLLKDLEGEIFKDALN
ALLGRRPNVIITPHTAFYTDDALKNMVEISCENIVDFLEGEEE
>gnl|CDD|240621 cd01620, Ala_dh_like, Alanine dehydrogenase and related dehydrogenases. Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains
TLGFPKETKNNEFRVALTPSFVKKLVANGFKVYIETGAGSGAGFSDEDYLQAGAQIVPAASKEAYSADII
VKLKEPEFAEYDLIKKGQLLVTFLHAATNRGVVEVLMRKKLTAYALEDLENDFRPRLAPNSNIAGYAGVQ
LGAYELARIQGGRMGGAGGVPPAKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGVETLGGSRLR
YSQKEELEKELKQTDILINAILVDGPRAPILIMEELVGPMKRGAVIVDLAADQGGNDETSIPTTEGVPTY
EVDGVVIYGVDNMPSLVPREASELLSKNLLPYLVKLA
>gnl|CDD|319765 cd01624, HAD_VSP_like, vegetative storage proteins and related proteins, similar to soybean VSPalpha and VSPbeta proteins; belongs to the haloacid dehalogenase-like superfamily. Soybean [Glycine max (L.) Merr.] vegetative storage protein VSPalpha and VSPbeta levels were identified as storage proteins due to their abundance and pattern of expression in plant tissues, they accumulate to almost one-half the amount of soluble leaf protein when soybean plants are continually depodded. They possess acid phosphatase activity which appears to be low compared to several other plant acid phosphatases; it increases in the leaves of depodded soybean plants, but to no more than 0.1% of the total acid phosphatase activity in these leaves. This acid phosphatase activity has maximal activity at pH 5.0 - 5.5, and can liberate Pi from different substrates such as napthyl acid phosphate, carboxyphenyl phosphate, sugar-phosphates, glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, phosphoenolpyruvate, ATP, ADP, PPi, and short chain polyphosphates; they cleave phosphoenolpyruvate, ATP, ADP, PPI, and polyphosphates most efficiently. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Soybean VSPalpha and VSPbeta lack this active site aspartate, other members of this family have this aspartate and may be more active. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
KEAIAYAAGLDTVNAWVFDIDDTLLSSIDYLKKYGGTEGTAPGIWNSWLERGDSPPVPETLELAEYALEK
GVEVFFISDRWEKLREPTVENLKAAGYTVWSHLFLKPNGNKSKTVVVYKAKVRASIESKGYTIVANIGDQ
WSDLVGGYAERTFKLPNYLY
>gnl|CDD|319766 cd01625, HAD_PNP, polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional enzyme polynucleotide 5'-kinase/3'-phosphatase. Polynucleotide 3'-phosphatase (PNP) domain. This domain dephosphorylates single-stranded as well as double-stranded 3'-phospho termini. It is found in bifunctional enzyme polynucleotide kinase/phosphatase (PNKP) which contain both kinase and phosphatase domains. PNKP plays a key role in both base excision repair and non-homologous end-joining DNA repair pathway. DNA strand breaks can result from DNA damage by ionizing radiation and chemical agents, such as alkylating agents or anticancer agents. Such DNA damage often results in DNA strands with 5'-hydroxyl and 3'-phosphate termini. However, the repair of DNA damage by DNA polymerases and ligases requires 5'-phosphate and 3'-hydroxyl termini. PNKP acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
KVAAFDLDGTLIKTKSGKVFPTNASDWQILYPSVPEKLKALHKDGYKIVIFTNQGGIVRGKLTPEVFKGK
IEAILEKLGVPIQVYAATKKGKYRKPVTGMWDHLKEDLNSGIPINLKDSFYVGDAAGRPKDFSDSDRLFA
ENVGLKFFTPEEFF
>gnl|CDD|319767 cd01627, HAD_TPP, trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2. Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LLFLDYDGTLAPIVPDPDAAVPSPELLEALKKLAADPKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAE
IRLPGGGEWVTLAPKADLEWKEEVEAIFKYFTERTPGSLVEDKGASLAWHYRNADPEGARAALELALHLA
SDLLKALEVVPGKKVVEVRPVGVNKGEAVERILGELPFAGDFVLCAGDDVTDEDAFRALNGEGGFSVKVG
EGPTAAKFRLDDPPDVVA
>gnl|CDD|319768 cd01629, HAD_EP, Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. Oryzae enolase-phosphatase Xep. Enolase-phosphatase E1 (also called MASA) is a bifunctional enolase- phosphatase which promotes the conversion of 2,3-diketo-5-methylthio-1-phosphopentane to 1,2-dihydroxy-3-keto-5-methylthiopentene anion (an aci-reductone) in the methionine salvage pathway. The catalytic reaction is carried out continuously by enolization and dephosphorylation, and the enolase activity cannot be classified as typical enzymatic enolization. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
AILLDIEGTTTPISFVKDVLFPYARERLPDFLAEHWEDPEVKEDVLAAAAEAEGEAEASIEAVVANLLDW
MDEDRKATPLKALQGLIWREGYESGELKGHLYPDVVPALRRWHAAGLRLYIYSSGSVAAQKLLFGHSDAG
DLTPLFSGYFDTTIGPKREAASYRKIAEAIGVPPAEILFLSDVVAELDAAKEAGLQTVLLVRPG
>gnl|CDD|319769 cd01630, HAD_KDO-like, haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase. KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSGIEVAIITGRQSEAVRRRAKELGIEDL
FQGVKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGA
VREVCE
>gnl|CDD|340816 cd01635, Glycosyltransferase_GTB-type, glycosyltransferase family 1 and related proteins with GTB topology. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility
ILLVTGEYPPLRGGLELHVRALARALAALGHEVTVLALLLLALRRILKKLLELKPDVVHAHSPHAAALAA
LLAARLLGIPIVVTVHGPDSLESTRSELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALLKARLP
DLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAA
GKPVIATDVGGIPEFVVDGENGLLV
>gnl|CDD|238814 cd01636, FIG, FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with various substrates. Fructose-1,6-bisphospatase (both the major and the glpX-encoded variant) hydrolyze fructose-1,6,-bisphosphate to fructose-6-phosphate in gluconeogenesis. Inositol-monophosphatases and inositol polyphosphatases play vital roles in eukaryotic signalling, as they participate in metabolizing the messenger molecule Inositol-1,4,5-triphosphate. Many of these enzymes are inhibited by Li+
LEELCRVAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAE
EVMGRRDEYTWVIDPIDGTKNFINGLPFVAVVIAVYVILILAEPSHKRVDEKKAELQLLAVYRIRIVGSA
VAKMCLVALGLADIYYEPGGKRRAWDVAASAAIVREAGGIMTDW
>gnl|CDD|238815 cd01637, IMPase_like, Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent metal ions such as Mg++, and many members are inhibited by Li+ (which is thought to displace a bivalent ion in the active site). Substrates include fructose-1,6-bisphosphate, inositol poly- and monophosphates, PAP and PAPS, sedoheptulose-1,7-bisphosphate and probably others
LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNV
SDGGRVWVIDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSK
DTPLNDALLSTNASMLRSNRAAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGAL
IVEEAGGIVTDLDGEPLDTLNRSGIIAA
>gnl|CDD|238816 cd01638, CysQ, CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of the inositol monophosphatase family. It has been proposed that CysQ helps control intracellular levels of PAPS, which is an intermediate in cysteine biosynthesis (a principal route of sulfur assimilation)
LLELLIRIAREAGDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLR
LGWDRFWLVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSL
QARPPPLQPLRVVASRSHPDEELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGD
AVLRAAGGAVSDLDGSPLTYNREDFLNPDFIA
>gnl|CDD|238817 cd01639, IMPase, IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. They dephosphorylate inositol phosphate to generate inositol, which may be recycled into inositol lipids; in eukaryotes IMPase plays a vital role in intracellular signaling. IMPase is one of the proposed targets of Li+ therapy in manic-depressive illness. This family contains some bacterial members of the inositol monophosphatase family classified as SuhB-like. E. coli SuhB has been suggested to participate in posstranscriptional control of gene expression, and its inositol monophosphatase activity doesn't appear to be sufficient for its cellular function. It has been proposed, that SuhB plays a role in the biosynthesis of phosphatidylinositol in mycobacteria
LLNIAIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAG
GLTDEPTWIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVS
GRKELKDALVATGFPYDRGDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWD
VAAGALIVREAGGLVTDFDGGPFDLMSGNILAGN
>gnl|CDD|238818 cd01640, IPPase, IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness
LLRSLLAVAEKAGGIARDVVKKGRLLILLVEGKTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEE
DNEFENQEDESRDVDLDEEILEESCPSPSKDLPEEDLGVWVDPLDATQEYTEGLLEYVTVLIGVAVKGKP
IAGVIHQPFYEKTAGAGAWLGRTIWGLSGLGAHSSDFKEREDAGKIIVSTSHSHSVKEVQLITAGNKDEV
LRAGGAGYKVLQVLEGLADAYVHSTGGIKKWDICAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKGGLL
ATIRSNHEAYLDK
>gnl|CDD|238819 cd01641, Bacterial_IMPase_like_1, Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol monophosphatases. These enzymes may dephosphorylate fructose-1,6-bisphosphate, inositol monophospate, 3'-phosphoadenosine-5'-phosphate, or similar substrates
DLAFALELADAAGQITLPYFRTRLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGD
AGYVWVLDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAGGRPLRVR
ACADLAEAVLSTTDPHFFTPGDRAAFERLARAVRLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALI
PIIEGAGGVITDWDGGPLTGGSGRVVAAGDAELHEALL
>gnl|CDD|238820 cd01642, Arch_FBPase_2, Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. These are Mg++ dependent phosphatases. Members in this family may have fructose-1,6-bisphosphatase and/or inositol-monophosphatase activity. Fructose-1,6-bisphosphatase catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway
MLEVLEKITKEIILLLNEKNRQGLVKLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRK
GSGEYIAVLDPLDGSTNYLSGIPFYSVSVALADPRSKVKAATLDNFVSGEGGLKVYSPPTRFSYISVPKL
GPPLVPEVPSKIGIYEGSSRNPEKFLLLSRNGLKFRSLGSAALELAYTCEGSFVLFLDLRGKLRNFDVAA
ALGACKRLGLHGDPSNLLLSRIKDKSIDEIILEF
>gnl|CDD|238821 cd01643, Bacterial_IMPase_like_2, Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These enzymes may dephosphorylate inositol monophosphate or similar substrates
LSLAEAIAQEAGDRALADFGNSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSS
GWYWVIDPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQ
LPDCNVGFNRSSRASARAVLRVILRRFPGKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILR
EAGGSWTILDEEPAFLQTKDYLSAGFPTLIAA
>gnl|CDD|238822 cd01644, RT_pepA17, RT_pepA17: Reverse transcriptase (RTs) in retrotransposons. This subfamily represents the RT domain of a multifunctional enzyme. C-terminal to the RT domain is a domain homologous to aspartic proteinases (corresponding to Merops family A17) encoded by retrotransposons and retroviruses. RT catalyzes DNA replication from an RNA template and is responsible for the replication of retroelements
VWYLPHHAVIKPSKTTTKLRVVFDASARYNGVSLNDMLLKGPDLLNSLFGVLLRFRQGKIAVSADIEKMF
HQVKVRPEDRDVLRFLWRKDGDEPKPIEYRMTVVPFGAASAPFLANRALKQHAEDHPHEAAAKIIKRNFY
VDDILVSTDTLNEAVNVAKRLIALLKKGGFNLRKWASNSQEVLDDLPEERVLLDRDSDVTEKTLGLRWNP
KTD
>gnl|CDD|238823 cd01645, RT_Rtv, RT_Rtv: Reverse transcriptases (RTs) from retroviruses (Rtvs). RTs catalyze the conversion of single-stranded RNA into double-stranded viral DNA for integration into host chromosomes. Proteins in this subfamily contain long terminal repeats (LTRs) and are multifunctional enzymes with RNA-directed DNA polymerase, DNA directed DNA polymerase, and ribonuclease hybrid (RNase H) activities. The viral RNA genome enters the cytoplasm as part of a nucleoprotein complex, and the process of reverse transcription generates in the cytoplasm forming a linear DNA duplex via an intricate series of steps. This duplex DNA is colinear with its RNA template, but contains terminal duplications known as LTRs that are not present in viral RNA. It has been proposed that two specialized template switches, known as strand-transfer reactions or "jumps", are required to generate the LTRs
PVWIKQWPLTEEKLEALTELVTEQLKEGHIEPSTSPWNTPVFVIKKKSGKWRLLHDLRAVNAQTQDMGAL
QPGLPHPAALPKGWPLIVLDLKDCFFSIPLHPDDRERFAFTVPSINNKGPAKRYQWKVLPQGMKNSPTIC
QSFVAQALEPFRKQYPDIVIYHYMDDILIASDLEGQLREIYEELRQTLLRWGLTIPPEKVQKEPPFQYLG
YEL
>gnl|CDD|238824 cd01646, RT_Bac_retron_I, RT_Bac_retron_I: Reverse transcriptases (RTs) in bacterial retrotransposons or retrons. The polymerase reaction of this enzyme leads to the production of a unique RNA-DNA complex called msDNA (multicopy single-stranded (ss)DNA) in which a small ssDNA branches out from a small ssRNA molecule via a 2'-5'phosphodiester linkage. Bacterial retron RTs produce cDNA corresponding to only a small portion of the retron genome
LDISNFYDSIYTHSLPWALHGKIKAKQLLKLLRLLGNLLDLLLLSSQYGQTNGLPIGPLTSRFLANIYLN
DVDHELKSKLKGVDYVRYVDDIRIFADSKEEAEEILEELKEFLAELGLSLNLSKTEILPLPEGTASKDFL
GYRFSPILLIKSSERKMS
>gnl|CDD|238825 cd01647, RT_LTR, RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long terminal repeats (LTRs) in their DNA copies but not in their RNA template. RT catalyzes DNA replication from an RNA template, and is responsible for the replication of retroelements. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs are present in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and Caulimoviruses
GIIEPSSSPYASPVVVVKKKDGKLRLCVDYRKLNKVTIKDRYPLPTIDELLEELAGAKVFSKLDLRSGYH
QIPLAEESRPKTAFRTPFGLYEYTRMPFGLKNAPATFQRLMNKILGDLLGDFVEVYLDDILVYSKTEEEH
LEHLREVLERLREAGLKLNPEKCEFGVPEVEFLGHIV
>gnl|CDD|238826 cd01648, TERT, TERT: Telomerase reverse transcriptase (TERT). Telomerase is a ribonucleoprotein (RNP) that synthesizes telomeric DNA repeats. The telomerase RNA subunit provides the template for synthesis of these repeats. The catalytic subunit of RNP is known as telomerase reverse transcriptase (TERT). The reverse transcriptase (RT) domain is located in the C-terminal region of the TERT polypeptide. Single amino acid substitutions in this region lead to telomere shortening and senescence. Telomerase is an enzyme that, in certain cells, maintains the physical ends of chromosomes (telomeres) during replication. In somatic cells, replication of the lagging strand requires the continual presence of an RNA primer approximately 200 nucleotides upstream, which is complementary to the template strand. Since there is a region of DNA less than 200 base pairs from the end of the chromosome where this is not possible, the chromosome is continually shortened. However, a surplus of repetitive DNA at the chromosome ends protects against the erosion of gene-encoding DNA. Telomerase is not normally expressed in somatic cells. It has been suggested that exogenous TERT may extend the lifespan of, or even immortalize, the cell. However, recent studies have shown that telomerase activity can be induced by a number of oncogenes. Conversely, the oncogene c-myc can be activated in human TERT immortalized cells. Sequence comparisons place the telomerase proteins in the RT family but reveal hallmarks that distinguish them from retroviral and retrotransposon relatives
TDIKKCYDSIPQYYRQKVGIPQGSPLSSLLCSLYYADLENKYLSFLDVIDKDSLLLRLVDDFLLITTSLD
KAIKFLNLLLRGFINQYKTFVNFDKTQINFSFAQLDSSDLIPWCGLLIN
>gnl|CDD|238827 cd01650, RT_nLTR_like, RT_nLTR: Non-LTR (long terminal repeat) retrotransposon and non-LTR retrovirus reverse transcriptase (RT). This subfamily contains both non-LTR retrotransposons and non-LTR retrovirus RTs. RTs catalyze the conversion of single-stranded RNA into double-stranded DNA for integration into host chromosomes. RT is a multifunctional enzyme with RNA-directed DNA polymerase, DNA directed DNA polymerase and ribonuclease hybrid (RNase H) activities
KARIILIPKKGKPSDPKNYRPISLLSVLYKLLEKILANRLRPVLEENILPNQFGFRPGRSTTDAILLLRE
VIEKAKEKKKSLVLVFLDFEKAFDSVDHEFLLKALGVRQGDPLSPLLFNLALDDLLRLLNKEEEIKLGGP
GITHLAYADDIVLFSEGKSRKLQELLQRLQEWSKESGLKINPSKSKVMLIGNKKKRLKDITLNGTPIEAV
ETFKYLGVTI
>gnl|CDD|238828 cd01651, RT_G2_intron, RT_G2_intron: Reverse transcriptases (RTs) with group II intron origin. RT transcribes DNA using RNA as template. Proteins in this subfamily are found in bacterial and mitochondrial group II introns. Their most probable ancestor was a retrotransposable element with both gag-like and pol-like genes. This subfamily of proteins appears to have captured the RT sequences from transposable elements, which lack long terminal repeats (LTRs)
RRVYIPKPNGKKRPLGIPTVRDRIVQEALKLVLEPIYEPRFSDCSYGFRPGRSAHDALKAIRRNVKGGYT
WVIEGDIKGFFDNIDHDLLLKILKRRIGDKRVLRLIRKWLKAGVLEDGKLVETEKGTPQGGVISPLLANI
YLHELDKFVEEKLKEYYDTSDPKFRRLRYVRYADDFVIGVRGPKEAEEIKELIREFLEELGLELNPEKTR
ITHFKSEGFDFLGFTF
>gnl|CDD|153210 cd01653, GATase1, Type 1 glutamine amidotransferase (GATase1)-like domain. Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase
VAVLLFPGFEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLARDEALLA
LLREAAAAGKPILGICLGAQLLVLGVQFHPEAIDGAEAGARLLVN
>gnl|CDD|100099 cd01657, Ribosomal_L7_archeal_euk, Ribosomal protein L7, which is found in archaea and eukaryotes but not in prokaryotes, binds domain II of the 23S rRNA as well as the 5S rRNA and is one of five ribosomal proteins that mediate the interactions 5S rRNA makes with the ribosome. The eukaryotic L7 members have an N-terminal extension not found in the archeal L7 orthologs. L7 is closely related to the ribosomal L30 protein found in eukaryotes and prokaryotes
LYAVVRIRGIVGVPPKIRKTLQLLRLRRINNAVFVKLTKATIGMLKKVEPYVTWGEPNLETLRELIYKRG
RLKGNGQRIPLTDNYLVEKTLKKGIICIEDLAHEIYTGGPNFKEVNNFLPPFRLHPPRGGFKGKKRHFSE
GGELGYRGEDINELIRRMI
>gnl|CDD|100100 cd01658, Ribosomal_L30, Ribosomal protein L30, which is found in eukaryotes and prokaryotes but not in archaea, is one of the smallest ribosomal proteins with a molecular mass of about 7kDa. L30 binds the 23SrRNA as well as the 5S rRNA and is one of five ribosomal proteins that mediate the interactions 5S rRNA makes with the ribosome. The eukaryotic L30 members have N- and/or C-terminal extensions not found in their prokaryotic orthologs. L30 is closely related to the ribosomal L7 protein found in eukaryotes and archaea
LKITLVKSLIGRPKKQRATLKALGLKKINQTVVHKDTPSIRGMINKVKHLVKVE
>gnl|CDD|238829 cd01659, TRX_superfamily, Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others
LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEKELKRYGVGGVPTLVVFGPGIGVKYG
>gnl|CDD|238830 cd01660, ba3-like_Oxidase_I, ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919
AEKKLALAHFVVAFLALLLGGLFGLLQVLVRTGVFPLPSSGILYYQGLTLHGVLLAIVFTTFFIMGFFYA
IVARALLRSLFNRRLAWAGFWLMVIGTVMAAVPILLGQASVLYTFYPPLQAHPLFYIGAALVVVGSWISG
FAMFVTLWRWKKANPGKKVPLATFMVVTTMILWLVASLGVALEVLFQLLPWSLGLVDTVDVLLSRTLFWW
FGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFADPGIGPGWKFIHMV
LTFMVALPSLLTAFTVFASLEIAGRLRGGKGLFGWIRALPWGDPMFLALFLAMLMFIPGGAGGIINASYQ
LNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELAAKRLALAQPWLWFVGMTIMSTAMHVA
GLLGAPRRTAEAQYGGLPAAGEWAPYQQLMAIGGTILFVSGALFLYILFRTLL
>gnl|CDD|238831 cd01661, cbb3_Oxidase_I, Cytochrome cbb3 oxidase subunit I. Cytochrome cbb3 oxidase, the terminal oxidase in the respiratory chains of proteobacteria, is a multi-chain transmembrane protein located in the cell membrane. Like other cytochrome oxidases, it catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Found mainly in proteobacteria, cbb3 is believed to be a modern enzyme that has evolved independently to perform a specialized function in microaerobic energy metabolism. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. The cbb3 operon contains four genes (ccoNOQP or fixNOQP), with ccoN coding for subunit I. Instead of a CuA-containing subunit II analogous to other cytochrome oxidases, cbb3 utilizes subunits ccoO and ccoP, which contain one and two hemes, respectively, to transfer electrons to the binuclear center. The fourth subunit (ccoQ) has been shown to protect the core complex from proteolytic degradation by serine proteases. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. The polar residues that form the D- and K-pathways in subunit I of other cytochrome c and ubiquinol oxidases are absent in cbb3. The proton pathways remain undefined. A pathway for the transfer of pumped protons beyond the binuclear center also remains undefined. It is believed that electrons are passed from cytochrome c (the electron donor) to the low-spin heme via ccoP and ccoO, respectively, and directly from the low-spin heme to the binuclear center
GRDDVFAVHGALIAAAAGAVAAALPRSADAGAVDDRLEADRYSDGPVFVGVIATMFWGLVGSLVGLIAAL
QLAEPDLLFDLAWLSFGRLRPLHTNAVIFGFGGNALIATSFYVVQRTCRARLAGGNLAWFVFWGYNLFIV
LAATGYLLGITQGKEYAEPEWYVDLWLTVVWVAYLLPFLGTLLRRKEPHIYVANWYYLAFIVTVAVLHIV
NNLAVPVSWFGSKSYSAHAGVQDATTQWWYGHNAVGFFLTAGFLAMMYYFLPKIAERPVYSYRLSIIGFW
ALAFLYIWAGPHHLHYTALPDWLQTLGMVFSVMLWMPSWAGMINGLLTLRGAWDKLRTDPTLRFMVVGGA
FYGLSTFEGSFMAIRAVNSLSHYTDWTVGHVHLGALGWVGFITFGAIYFLVPRIWKREWPSPKLVEWHFW
LATIGIVIYFVAMWISGILQGLMWRDYDSDGFLVYSFIESVQATHPYYIARSVGGLLMLSGALVMAYNFW
MTI
>gnl|CDD|238832 cd01662, Ubiquinol_Oxidase_I, Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center
WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVF
GLMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYW
ILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFG
THFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGV
WVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVM
LASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFP
MHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATGDPWGARTLEW
ATSSPPPAYNF
>gnl|CDD|238833 cd01663, Cyt_c_Oxidase_I, Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center
TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFG
NWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFS
LHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSF
FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWA
HHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLA
NSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQH
FLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEGSTSLEWTL
>gnl|CDD|238834 cd01665, Cyt_c_Oxidase_III, Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme
ILGSFGLLLLALGLVLWMHGYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILF
ILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNR
KKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGH
FSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYWW
>gnl|CDD|340457 cd01666, TGS_DRG, TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein (DRG) family. DRG-1 and DRG-2 comprise a highly conserved DRG subfamily of GTP-binding proteins found in archaea, plants, fungi and animals. The exact function of DRG proteins is unknown, although phylogenetic and biochemical fraction studies have linked them to translation, differentiation and growth. Their abnormal expressions may trigger cell transformation or cell cycle arrest. DRG-1 and DRG-2 bind to DFRP1 (DRG family regulatory protein 1) and DFRP2, respectively. Both DRG-1 and DRG-2 contain a domain of characteristic Obg-type G-motifs that may be the core of GTPase activity, as well as the C-terminal TGS (ThrRS, GTPase and SpoT) domain, which has a predominantly beta-grasp ubiquitin-like fold and may be related to RNA binding. DRG subfamily belongs to the Obg family of GTPases
LGIIRVYTKPPGKKPDFDEPFILRRGSTVEDVAEKIHKDLAENFKYARVWGKSVKFDGQRVGLDHVLEDG
DIVEIHK
>gnl|CDD|340458 cd01667, TGS_ThrRS, TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar proteins. ThrRS, also termed cytoplasmic threonine--tRNA ligase, is a class II aminoacyl-tRNA synthetase (aaRS) that plays an essential role in protein synthesis by catalyzing the aminoacylation of tRNA(Thr), generating aminoacyl-tRNA, and editing misacylation. In addition to its catalytic and anticodon-binding domains, ThrRS has an N-terminal TGS domain, named after the ThrRS, GTPase, and SpoT/RelA proteins where it occurs. TGS is a small domain with a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions
IKITLPDGSVKEFPKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE
>gnl|CDD|340459 cd01668, TGS_RSH, TGS (ThrRS, GTPase and SpoT) domain found in the RelA/SpoT homolog (RSH) family. The RelA/SpoT homolog (RSH) family consists of long RSH proteins and short RSH proteins. Long RSH proteins have been characterized as containing an N-terminal region and a C-terminal region. The N-terminal region contains a pseudo-hydrolase (inactive-hydrolase) domain and a (p)ppGpp synthetase domain. The C-terminal region contains a ubiquitin-like TGS (ThrRS, GTPase and SpoT) domain, a conserved cysteine domain (CC), helical and ACT (aspartate kinase, chorismate mutase, TyrA domain) domains connected by a linker region. Short RSH proteins have a truncated C-terminal region without ACT domain. The RSH family includes two classes of enzyme: i) monofunctional (p)ppGpp synthetase I, RelA, and ii) bifunctional (p)ppGpp synthetase II/hydrolase, SpoT (also called Rel). Both classes are capable of synthesizing (p)ppGpp but only bifunctional enzymes are capable of (p)ppGpp hydrolysis. SpoT is a ribosome-associated protein that is activated during amino acid starvation and thought to mediate the stringent response. The function of the TGS domain of SpoT is in transcription of survival and virulence genes in respond to environmental stress. RelA is an ATP:GTP(GDP) pyrophosphate transferase that is recruited to stalled ribosomes and activated to synthesize (p)ppGpp, which acts as a pleiotropic secondary messenger
FVFTPKGDVVSLPKGATPIDFAYAIHTDVGNKCVGAKVNGKIVPLDYVLKNGDVVEIIT
>gnl|CDD|340460 cd01669, TGS_MJ1332_like, TGS (ThrRS, GTPase and SpoT) domain found in Methanocaldococcus jannaschii uncharacterized GTP-binding protein MJ1332 and similar proteins. This family includes a group of uncharacterized GTP-binding proteins from archaea, which belong to the Obg family of GTPases. The family members contain a domain of characteristic Obg-type G-motifs that may be the core of GTPase activity, as well as a C-terminal TGS (ThrRS, GTPase and SpoT) domain that has a predominantly beta-grasp ubiquitin-like fold
LKMIVVYPVEDENKLTDKKGNVLPDAILLKRGSTPRDLAYKIHTDLGKGFLYAIDARTKMRLGEDYELKH
GDVVKIVS
>gnl|CDD|260017 cd01670, Death, Death Domain: a protein-protein interaction domain. Death Domains (DDs) are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells
YFDLVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIG
RRDLAEKLE
>gnl|CDD|260018 cd01671, CARD, Caspase activation and recruitment domain: a protein-protein interaction domain. Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
LRKNRVELVEDLDVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRET
GQPHLAELL
>gnl|CDD|238835 cd01672, TMPK, Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP)
MFIVFEGIDGAGKTTLIELLAERLEARGYEVVLTREPGGTPIGEAIRELLLDPEDEKMDPRAELLLFAAD
RAQHVEEVIKPALARGKIVLSDRFVDSSLAYQGAGRGLGEALIEALNDLATGGLKPDLTILLDIDPEVGL
ARIEARGRDDRDEQEGLEFHERVREGYLELAAQEPERIIVIDASQPLEEVLAEILKAILE
>gnl|CDD|238836 cd01673, dNK, Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to yield corresponding monophosphates (dNMPs). This family consists of various deoxynucleoside kinases including deoxyribo- cytidine (EC 2.7.1.74), guanosine (EC 2.7.1.113), adenosine (EC 2.7.1.76), and thymidine (EC 2.7.1.21) kinases. They are key enzymes in the salvage of deoxyribonucleosides originating from extra- or intracellular breakdown of DNA
VIVVEGNIGAGKSTLAKELAEHLGYEVVPEPVEPDVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKD
ALEHLSTGQGVILERSIFSDRVFAEANLKEGGIMKTEYDLYNELFDNLIPELLPPDLVIYLDASPETCLK
RIKKRGRPEEQGIPLDYLEDLHEAYEKWFLPQMYEKAPVLIIDANEADIEYNK
>gnl|CDD|238837 cd01674, Homoaconitase_Swivel, Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases. This is the swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism
CDADNLNTDGIYPGKYTYQDDITPEKMAEVCMENYDSEFSTKTKQGDILVSGFNFGTGSSREQAATALLA
KGIPLVVSGSFGNIFSRNSINNALLSIELPFLVQKLREAFANESKELTRRTGWKLKWDV
>gnl|CDD|153084 cd01675, RNR_III, Class III ribonucleotide reductase. Ribonucleotide reductase (RNR) catalyzes the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, and bacteriophage, use a diiron-tyrosyl radical. Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in strict or facultative anaerobic bacteria, bacteriophage, and archaea, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. All three RNRs have a ten-stranded alpha-beta barrel domain that is structurally similar to the domain of PFL (pyruvate formate lyase). The class III enzyme from phage T4 consists of two subunits, this model covers the larger subunit which contains the active and allosteric sites
ENANVDSSPGSTMKDLAAGIVKKYYLLKILPKEIARAHLNGDIHIHDLDYLPLTPYCCGWDLRPLLEKGF
TTGNGIIEPPKHLSSALGHIVNFLGTVQNEQAGGQAFPEFDTYLAPFVRKDYLKYRLTATRKEIKQAMQG
FIYNLNTLSRRGGQTPFTNITLGLVCPKDLEFEGGGEPVFTYGDTDKEARMIQKAFLEVRLEGDAKGRPF
TFPIPTFNVTEGFNLDPNYDLKELAFECAAKRGYPYFLNFDNSDNVPGDVRAMGCRLFLDKNELKRGGGL
EGSGDGTGNIGVVTINLPRIAYEARGDEEKFFELLDEYLELAKDALEIRRKRLKEALARGLPPLYQEGLG
GGKLLFILKRHTLTIGFIGLNEAAEALTGKGIGESEEAREFGIRILEHIRERADEFKEETGLLYSVEATP
AESLAYRFAKKDRKKYGDIIPGVTDKPYYTNSFHVPVYEDIDPFEKIDIEAKLHPLTTGGHILHIELGEA
KPNPEALEALVKKAAKRGVIYFGINTPIDICNDCGYIGEGEGFKCPKCGSEDVEVISRITGYLGP
>gnl|CDD|153085 cd01676, RNR_II_monomer, Class II ribonucleotide reductase, monomeric form. Ribonucleotide reductase (RNR) catalyzes the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, and bacteriophage, use a diiron-tyrosyl radical. Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in anaerobic bacteria, bacteriophage, and archaea, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. All three RNRs have a ten-stranded alpha-beta barrel domain that is structurally similar to the domain of PFL (pyruvate formate lyase). Class II RNRs are found in bacteria that can live under both aerobic and anaerobic conditions. Many, but not all members of this class, are found to be homodimers. This particular subfamily is found to be active as a monomer. Adenosylcobalamin interacts directly with an active site cysteine to form the reactive cysteine radical
GEVTYYRTYSRPKEEGQNENWDQTVERVVEGTFELWERHLGNPLRWLNEKAEEEAEELRSLIFELKALPP
GRGLWLGGTDYSRQRRFASLNNCAFVSTEDVVYPFVFLMDLLMQGCGVGFDTAGSNISQIPRPLQEIKVQ
RVNRTEKGGIQNNVETYDPTQHTWIIKVPDSREGWVKSVQLLLDLYFNPAQTLIFDYSDIRPAGERLKGF
GGIASGPEPLKKLHKAIAAILNDRSGKPLTSVDIVDLMNLIGVCVVSGNVRRSAEIAFGQPEDEDFADLK
QYQWNPGRREHGWASNNSVVFESKPDRLEYSFACMLIRGNGEPGIAWLDNMKAYARMVLLTTPYHDLRAK
GGNPCGEISLESYELCNLVEVFPLKHEGDLEDLQETLYLAGRYAKTVTLLPLHWEITNEIILRNRRIGVS
MSGIADFIVRAGGDLTLHDLKRWRNIGYEAVYQYDERLSKWLGIPLSIKVTCVKPSGTISLLAGASPGMH
YPLGKYLIRRIRFQKHDPLAPALIAAGYHVEPDIYDPTSVLVEFPVKAGNADRTANTVSIVEQLSLLAFL
QTYWADNQVSNTISFDPSPEGPALIQALQQFQYQYKSVSLLPRFDTTKNAAQMPFEPITKERYEQRIAKL
KDVDYSGDYISPLEEDLQTFCDSGACPI
>gnl|CDD|153086 cd01677, PFL2_DhaB_BssA, Pyruvate formate lyase 2 and related enzymes. This family includes pyruvate formate lyase 2 (PFL2), B12-independent glycerol dehydratase (DhaB) and the alpha subunit of benzylsuccinate synthase (BssA), all of which have a highly conserved ten-stranded alpha/beta barrel domain, which is similar to those of PFL1 (pyruvate formate lyase 1) and RNR (ribonucleotide reductase). Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, the conversion of pyruvate and CoenzymeA to formate and acetylCoA. DhaB catalyzes the first step in the conversion of glycerol to 1,3-propanediol while BssA catalyzes the first step in the anaerobic mineralization of both toluene and m-xylene
TERIKRLKAKILTAKPSISIERARLYTESYKETEGKPVIIRRAKALKHILENATIYIQDDELIVGNRGGK
PRAVPVFPELSVHWVEDELDDLPKRPGDPFVISEDKKEYLEEIFPYWKGKTLRDRCFKYFPEETLIAMAA
GVFTEFMYFFSGPGHVAVDYPKVLEKGLDGLIEEAKEAIEALDLTGPEDIDKIYFYQAMIIVCEAVITYA
KRYAELAKELAAKETDPKRKAELLEIAEICRRVPAHPPRTFWEALQSFWFIHLILQIESNGHSISPGRFD
QYLYPFYKQDIEEGRLTREGAIELLECLWIKINEINKVRSGASAKYFAGYNTFQNLTIGGQTEDGSDATN
ELSYLILEATRRVRLPQPSLTVRYHAKSPDKFLKKAAEVIRLGLGYPAFFNDEVVIPALLRKGVSLEDAR
DYGLIGCVETGAPGRKYRWTGTGYINLAKVLEITLNNGKDPRSGKQVGPETGDATDFKTFEELWEAFKKQ
LRHFIKLSVRANNISDIAHAEVAPAPFLSALVDDCIEKGKDINAGGARYNFGGIQGVGIATLGDSLAAIK
KLVFEEKKLTMEELLEALKANFAEGYEERRRLLNNAPKYGNDDDYADNIARRVYEWYCKEVEKYQNPRGG
KFYPGTYSVSANVPFGSVTGATPDGRLAGTPLSDGVSPSQGTDKKGPTAVIKSVSKLDHFNISGGTLLNQ
KFSPSTLEGEEGLKKLAALIRTYFDLGGHHIQFNVVSAETLRDAQKHPEKYRDLIVRVAGYSAYFVELSK
EVQDEIIARTE
>gnl|CDD|153087 cd01678, PFL1, Pyruvate formate lyase 1. Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, the conversion of pyruvate and CoenzymeA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate in which two cysteines and one glycine form radicals that are required for catalysis. PFL has a ten-stranded alpha/beta barrel domain that is structurally similar to those of all three ribonucleotide reductase (RNR) classes as well as benzylsuccinate synthase and B12-independent glycerol dehydratase
AWEGFKGGKWQEEIDVRDFIQKNYTPYEGDESFLAGPTERTKKLWDKLEELLEEERAKGGVLDVDTKTVS
TITSHKAGYIDKELEVIVGLQTDKPLKRAIMPFGGIRMAEQALKAYGYELDPELKKIFTKYRKTHNDGVF
DAYTPEIRRARHSGIITGLPDAYGRGRIIGDYRRVALYGVDRLIEEKKKDLDNLGGDEMTDDTIRLREEV
AEQIKALKELKQMAASYGLDISRPATNAQEAIQWTYFGYLAAIKEQNGAAMSLGRVSTFLDIYIERDLKA
GTITEAEAQELIDQFIMKLRMVRFLRTPEYNELFSGDPTWVTESIGGMGNDGRSLVTKTSFRFLNTLYNL
GPAPEPNLTVLWSEKLPENFKRFCAKVSIDTSSIQYENDDLMRPDWGGDDYGIACCVSAMRIGKQMQFFG
ARANLAKALLYAINGGRDEKTGDQVGPDIEPITSDYLDYDEVMENYDKSMDWLADTYVNALNIIHYMHDK
YAYEALQMALHDTDVRRTMAFGIAGLSVAADSLSAIKYAKVKPIRDEDGLAVDFEIEGDFPRYGNDDDRA
DDIAVWVVKTFMNKLRKHKTYRNAEPTQSVLTITSNVVYGKKTGNTPDGRRAGEPFAPGANPMHGRDKKG
ALASLASVAKLPYRDANDGISNTFSIVPNALGKTDEERIDNLVGILDGYFTKGGHHLNVNVLNRETLLDA
MEHPEKYPQLTIRVSGYAVNFVKLTREQQLDVISRTFH
>gnl|CDD|153088 cd01679, RNR_I, Class I ribonucleotide reductase. Ribonucleotide reductase (RNR) catalyzes the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, and many viruses, use a diiron-tyrosyl radical. Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in anaerobic bacteria, bacteriophages, and archaea, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. All three RNRs have a ten-stranded alpha-beta barrel domain that is structurally similar to the domain of PFL (pyruvate formate lyase). Class I RNR is oxygen-dependent and can be subdivided into classes Ia (eukaryotes, prokaryotes, viruses and phages) and Ib (which is found in prokaryotes only). It is a tetrameric enzyme of two alpha and two beta subunits; this model covers the major part of the alpha or large subunit, called R1 in class Ia and R1E in class Ib
PQDRLMRVALGLASGDLEWAKEFYDLLSKQRFTPATPTLFNAGTPRGQLSSCFLLTVDDSLESIYDTIKE
CAQLSKIGGGIGLNLSNIRATGSPIRGTNGASNGVIPFLKLLNDTARYVDQGGQRKGAGAVYLEIWHPDI
EEFLDLKKNNGDERRRARDLFYGVWIPDLFMERVERDLWRKILESQFETGYPYILFKDTCNRKNPQKHLG
TIKSSNLCTEILQPTSPSEDEPGEDAVCNLASINLGNFVTFEKLEEVVKLAVRALDNVIDLNYYPVPEAK
RSNMRHRAIGLGVMGLHDYLALLRIPYESEEALDLNDRIFETINYYALKASCELAKERGGLRNSLLLAIA
PTASISQILGATPSIEPITSNIYVRRVLSGEFPVVNPHLEKDLWEYGLYKTAYEIDQRWLIDLAADRQKH
IDQGQSLNLFLTPPATTRDLNSLYFYAWKKGLKTLYYLRT
>gnl|CDD|238838 cd01680, EFG_like_IV, Elongation Factor G-like domain IV. This family includes the translational elongation factor termed EF-2 (for Archaea and Eukarya) and EF-G (for Bacteria), ribosomal protection proteins that mediate tetracycline resistance and, an evolutionarily conserved U5 snRNP-specific protein (U5-116kD). In complex with GTP, EF-G/EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site of the small subunit of ribosome and the mRNA is shifted one codon relative to the ribosome. It has been shown that EF-G/EF-2_IV domain mimics the shape of anticodon arm of the tRNA in the structurally homologous ternary complex of Petra, EF-Tu (another transcriptional elongation factor) and GTP analog. The tip portion of this domain is found in a position that overlaps the anticodon arm of the A-site tRNA, implying that EF-G/EF-2 displaces the A-site tRNA to the P-site by physical interaction with the anticodon arm
YRETIRKSVEATGEFERELGGKPQFGEVTLRVEPLERGSGVRVVDPVDEELLPAELKEAVEEGIRDACAS
GPLTGYPLTDVRVTVLDVPYHEGVSTEAGFRAAAGRAFESAAQKAG
>gnl|CDD|238839 cd01681, aeEF2_snRNP_like_IV, This family represents domain IV of archaeal and eukaryotic elongation factor 2 (aeEF-2) and of an evolutionarily conserved U5 snRNP-specific protein. U5 snRNP is a GTP-binding factor closely related to the ribosomal translocase EF-2. In complex with GTP, EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site of the small subunit of ribosome and the mRNA is shifted one codon relative to the ribosome. It has been shown that EF-2_IV domain mimics the shape of anticodon arm of the tRNA in the structurally homologous ternary complex of Phe-tRNA, EF-1 (another transcriptional elongation factor) and GTP analog. The tip portion of this domain is found in a position that overlaps the anticodon arm of the A-site tRNA, implying that EF-2 displaces the A-site tRNA to the P-site by physical interaction with the anticodon arm
DPVVSFRETVVETSSGTCLAKSPNKHNRLYMRAEPLPEELIEDIEKGKITLKDDKKKRARILLDKYGWDK
LAARKIWAFGPDRTGPNILVDDTKGVQYDKSLLNEIKDSIVAGFQWATKEGPLCEEPMRGVKFKLEDATL
HADAIHRGGGQIIPAARRACYAAFLLASPRLMEPMYL
>gnl|CDD|238840 cd01683, EF2_IV_snRNP, EF-2_domain IV_snRNP domain is a part of 116kD U5-specific protein of the U5 small nucleoprotein (snRNP) particle, essential component of the spliceosome. The protein is structurally closely related to the eukaryotic translational elongation factor EF2. This domain has been also identified in 114kD U5-specific protein of Saccharomyces cerevisiae and may play an important role either in splicing process itself or the recycling of spliceosomal snRNP
DPVVTFCETVVETSSAKCFAETPNKKNKITMIAEPLDKGLAEDIENGQLKLSWNRKKLGKFLRTKYGWDA
LAARSIWAFGPDTKGPNVLIDDTLPEEVDKNLLNSVKESIVQGFQWAVREGPLCEEPIRNVKFKLLDADI
ASEPIDRGGGQIIPTARRACYSAFLLATPRLMEPIYEV
>gnl|CDD|238841 cd01684, Tet_like_IV, EF-G_domain IV_RPP domain is a part of bacterial ribosomal protected proteins (RPP) family. RPPs such as tetracycline resistance proteins Tet(M) and Tet(O) mediate tetracycline resistance in both gram-positive and -negative species. Tetracyclines inhibit the accommodation of aminoacyl-tRNA into ribosomal A site and therefore prevent the addition of new amino acids to the growing polypeptide. RPPs Tet(M) confer tetracycline resistance by releasing tetracycline from the ribosome and thereby freeing the ribosome from inhibitory effects of the drug, such that aa-tRNA can bind to the A site and protein synthesis can continue
VIYKERPLGTGEGVEHIEVPPNPFWATVGLRVEPLPRGSGLQYESEVSLGSLPRSFQNAVEETVRETLQQ
GLYGWEVTDCKVTLTYGRYHSPVSTAADFRELTPRVLRQALKKAG
>gnl|CDD|238842 cd01693, mtEFG2_like_IV, mtEF-G2 domain IV. This subfamily is a part the of mitochondrial transcriptional elongation factor, mtEF-G2. Mitochondrial translation is crucial for maintaining mitochondrial function and mutations in this system lead to a breakdown in the respiratory chain-oxidative phosphorylation system and to impaired maintenance of mitochondrial DNA. In complex with GTP, EF-G promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site of the small subunit of ribosome and the mRNA is shifted one codon relative to the ribosome
IAYRETILEPARATDTLEKVIGDKKHSVTVTMEVRPNQASSSPVELIELANSAIEVLLKRIQEAVENGVH
SALLQGPLLGFPVQDVAITLHSLTIGPGTSPTMISACASQCVQKALKSAG
>gnl|CDD|238843 cd01699, RNA_dep_RNAP, RNA_dep_RNAP: RNA-dependent RNA polymerase (RdRp) is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage. RdRp catalyzes synthesis of the RNA strand complementary to a given RNA template. RdRps of many viruses are products of processing of polyproteins. Some RdRps consist of one polypeptide chain, and others are complexes of several subunits. The domain organization and the 3D structure of the catalytic center of a wide range of RdRps, including those with a low overall sequence homology, are conserved. The catalytic center is formed by several motifs containing a number of conserved amino acid residues. This subfamily represents the RNA-dependent RNA polymerases from all positive-strand RNA eukaryotic viruses with no DNA stage
LEKAVESLEDLPLIRPDLVFTTFLKDELRPLEKVEAGKTRLIQPRPLDYNIALRMYLGPFEAKLMKNRGG
LPIAVGINPYSRDWTILANKLRSFSPVAIALDYSRFDSSLSPQLLEAEHSIYNALYDDDDELERRNLLRS
LTNNSLHIGFNEVYKVRGGRPSGDPLTSIGNSIINCILVRYAFRKLGGKSFFKNVRLLNYGDDCLLSVEK
ADDKFNLETLAEWLKEYGLTMTDEDKVESPFRPLEEVEFLKRRFVLDEGGGWRAPLDPSSILSKLSWS
>gnl|CDD|176454 cd01700, PolY_Pol_V_umuC, umuC subunit of DNA Polymerase V. umuC subunit of Pol V. Pol V is a bacterial translesion synthesis (TLS) polymerase that consists of the heterotrimer of one umuC and two umuD subunits. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Pol V, RecA, single stranded DNA-binding protein, beta sliding clamp, and gamma clamp loading complex are responsible for inducing the SOS response in bacteria to repair UV-induced DNA damage
ALVDCNSFYASCERVFRPLLLGRPLVVLSNNDGCVIARSPEAKALGIKMGSPYFKVPDLLERHGVAVFSS
NYALYGDMSRRIMSILERFSPDVEVYSIDESFLDLTGSLRFGDLEELARKIRRRILQETGIPVTVGIGPT
KTLAKLANDLAKKKNPYGGVVDLTDEEVRDKLLKILPVGDVWGIGRRTAKKLNAMGIHTAGDLAQADPDL
LRKKFGVVGERLVRELNGIDCLPLEEYPPPKKSIGSSRSFGRDVTDLDELKQALAEYAERAAEKLRRQKS
VARTISVFIGTSGFSRQPKYYSATNTLPYPTNDTREIVKAALRLLYAIYRPGYAYRKAGVMLSD
>gnl|CDD|176455 cd01701, PolY_Rev1, DNA polymerase Rev1. Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Rev1 has both structural and enzymatic roles. Structurally, it is believed to interact with other nonclassical polymerases and replication machinery to act as a scaffold. Enzymatically, it catalyzes the specific insertion of dCMP opposite abasic sites. Rev1 interacts with the Rev7 subunit of the B-family TLS polymerase Pol zeta (Rev3/Rev7). Rev1 is known to actively promote the introduction of mutations, potentially making it a significant target for cancer treatment
FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADPSNSIHPDLQRIIMHVDFDCFFVSVSIRNRPDLK
GKPVAVCHGKGPNSEIASCNYEARSYGIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTD
NIEAVSCDEALIDITSLLEETYELPEELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHL
SAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTCGGLELRSKTKEKLQKVLGPKTGEKLYDYCRGIDD
RPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEESNVTGRQITLKLMKRAPGAPIEPPK
YMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL
>gnl|CDD|176456 cd01702, PolY_Pol_eta, DNA Polymerase eta. Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Unlike other Y-family members, Pol eta can efficiently and accurately replicate DNA past UV-induced lesions. Its activity is initiated by two simultaneous interactions: the PIP box in pol eta interacting with PCNA, and the UBZ (ubiquitin-binding zinc finger) in pol eta interacting with monoubiquitin attached to PCNA. Pol eta is more efficient in copying damaged DNA than undamaged DNA and seems to recognize when a lesion has been passed, facilitating a lesion-dependent dissociation from the DNA
AHIDMDAFFAQVEQVRLGLLRNDPVAVVQWNSIIAVSYAARAFGVTRFMTIDEAKKKCPDLILAHVATYK
KGEDEADYHENPSPARHKVSLDPYRRASRKILNILKRFGDVVEKASIDEAYLDLGSRIVEEIRQQVYDEL
GYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLPITSIRGLGGKLGEEIIDLLGLPTEGDV
AGFRSSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFPGKTALSTEDVQHWLLVLASE
LNSRLEDDRYENNRRPKTLVLSLRQRGDGVRRSRSCALPRYDAQKIVKDAFKLIKAINEEGLGLAWNYPL
TLLSLSFTK
>gnl|CDD|176457 cd01703, PolY_Pol_iota, DNA Polymerase iota. Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Pol iota is thought to be one of the least efficient polymerases, particularly when opposite pyrimidines; it can incorporate the correct nucleotide opposite a purine much more efficiently than opposite a pyrimidine, and prefers to insert guanosine instead of adenosine opposite thymidine. Pol iota is believed to use Hoogsteen rather than Watson-Crick base pairing, which may explain the varying efficiency for different template nucleotides
IHLDLDCFYAQVEEIRDPSLKSKPLGIQQKYIVVTCNYEARRLGVKKLMSIKDAKEICPDLVLVNGEDLT
PFRDMSKKVYRLLRSYSWNDRVERLGFDENFMDVTEMRLLVASHIAYEMRERIENELGLTCCAGIASNKL
LAKLVGSVNKPNQQTTLLPPSCADLMDFMDLHDLRKIPGIGYKTAAKLEAHGISSVRDLQEFSNRNRQTV
GAAPSLLELLLMVKEFGEGIGQRIWKLLFGRDTSPVKPASDFPQQISIEDSYKKCSLEEIREARNKIEEL
LASLLERMKQDLQEVKAGDGRRPHTLRLTLRRYTSTKKHYNRESKQAPIPSHVFQKLTGGNEIAARPIEK
ILMRLFRELVPPKNVKGFNLTLLNVCFTN
>gnl|CDD|238844 cd01709, RT_like_1, RT_like_1: A subfamily of reverse transcriptases (RTs). An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses. These elements can be divided into two major groups. One group contains retroviruses and DNA viruses whose propagation involves an RNA intermediate. They are grouped together with transposable elements containing long terminal repeats (LTRs). The other group, also called poly(A)-type retrotransposons, contain fungal mitochondrial introns and transposable elements that lack LTRs
KQQLLRLLATEILINTALYGEVTVVQSDFKWFGPSLPHSTILAVLKFFGVPEKWLDFFKKFLEAPLRFVA
DGPDAPPRIRKRGTPMSHALSDVFGELVLFCLDFAVNQATDGGLLYRLHDDLWFWGQPETCAKAWKAIQE
FAKVMGLELNKEKTGSVYLSDDTKTRDTTIDATLPEGPVRWGFLKLDPKTGRWEIDQSQVDAHIDELRKQ
LDACKSVLSWIQAWNSYIGRFFSNNFGKPANCFGREHVDAILATHERIQRRLFPDAGGGGGSVTEYLRQM
IESRFGVSDIPDGFFYFPEELGGLGLKNPFISLLLVRDSIKEDPEELIDKFLKAEREAYAAAKKRF
>gnl|CDD|467485 cd01712, PPase_ThiI, pyrophosphatase domain of thiamine biosynthesis protein ThiI. ThiI is required for thiazole synthesis in the thiamine biosynthesis pathway. ThiI is also responsible for the 4-thiouridine (S4U) modification at position 8 in some prokaryotic tRNAs. ThiI contains a PP-loop pyrophosphatase domain which binds ATP and activates tRNA by adenylation. The PP-loop pyrophosphatase catalytic domain of ThiI proteins is always accompanied by a THUMP domain towards the N terminus. THUMP domains are predicted to bind RNA and are widespread in bacteria, archaea, and eukaryotes. The acronym was derived from the names of RNA-modifying enzymes in which this domain is found, namely, thiouridine synthases (ThiI), methylases, and archaeal pseudouridine synthases. ThiI proteins from gamma-proteobacteria and from archaea of the genus Thermoplasma also contain a C-terminal extension of approximately 100 amino acid residues which accepts sulfur in the form of a persulfide on a cysteine residue. This persulfide is responsible for a nucleophilic attack of the adenylated tRNA substrate, completing the sulfur insertion forming a disulfide-bridge between the rhodanese-like domain and a second cysteine residue located in the PP-loop domain. The reaction releases AMP and modified tRNA, and leaves the enzyme in an oxidized state. The disulfide is then reductively cleaved to complete the enzymatic cycle. The pyrophosphatase domain of ThiI belongs to the adenine nucleotide hydrolase (AANH) superfamily and it binds to adenosine nucleotide
VGTSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVEKVKDLARVLSEYQGGVKLYLVP
FTDKIQKEILEKVPESYRIVLMRRMMYRIAEKIAERLGADALVTGESLGQVASQTLENLKVIDSVTDLPV
LRPLIGMDKEEIIDIARRIGTYEISILPYEDCCCLFAPKNPVTKP
>gnl|CDD|467486 cd01713, CTU1-like, cytoplasmic tRNA 2-thiolation protein 1 and similar proteins. This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group
IERRVHRTIRKYRLIKPGDRVAVGLSGGKDSTVLLYVLKELNKRHDYGVELIAVTIDEGIKGYRDDSLEA
ARKLAEEYGIPLEIVSFEDEFGFTLDELIVGKGGKKNACTYCGVFRRRALNRGARELGADKLATGHNLDD
EAETILMNLLRGDVARLLRTGPEPRSEGEGLVPRIKPLRYIPEKEIVLYAHLNGLPYFSTECPYAPEA
>gnl|CDD|467487 cd01714, ETF_beta, electron transfer flavoprotein (ETF) beta. The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for various mitochondrial dehydrogenases. ETF transfers electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase. ETF is a heterodimer, consisting of an alpha and a beta subunit, which binds one molecule of FAD per dimer. A similar system also exists in some bacteria. The homologous pair of proteins (FixA/FixB) are essential for nitrogen fixation. The beta subunit is distantly related to and forms a heterodimer with the alpha subunit
MKILVCVKQVPDTEEKKRDPKTGTLDREGVPSIINPFDENAVEEALRLKEKHGGEVTAVSMGPPQAEEAL
REALAMGADRAILVSDRAFAGADTLATAKALAAAIKKEGPDLILAGKQAIDGDTAQVGPQLAELLGWPQV
TYVSKIEIEGGKVTVERELEGGLETVEVPLPAVITVDLRLNEPRYPSLPGIMKAKKKPIEVWTAADLGVD
>gnl|CDD|467488 cd01715, ETF_alpha, electron transfer flavoprotein (ETF) alpha. The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for various mitochondrial dehydrogenases. ETF transfers electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase. ETF is a heterodimer, consisting of an alpha and a beta subunit, which binds one molecule of FAD per dimer. A similar system also exists in some bacteria. The homologous pair of proteins (FixA/FixB) are essential for nitrogen fixation. The alpha subunit of ETF is structurally related to the bacterial nitrogen fixation protein fixB which could play a role in a redox process and feed electrons to ferredoxin
SVLVVAEHRGGKLAPVSLELLTAARKLAGGEVTALVAGSGAKAVAAAELKVYGVDKVLVADDPALAHYLA
EPYAPLLVALIKKYKPSHVLAGATAFGKDLLPRVAAKLDVGLIADVTGLESDEDTFTRPIYAGNALATVK
SPDRPKVLTVRPTAFPAAEADGSGGSAVVEV
>gnl|CDD|212463 cd01716, Hfq, bacterial Hfq-like. Hfq, an abundant, ubiquitous RNA-binding protein, functions as a pleiotropic regulator of RNA metabolism in prokaryotes, required for transcription of some transcripts and degradation of others. Hfq binds small RNA molecules called riboregulators that modulate the stability or translation efficiency of RNA transcripts. Hfq binds preferentially to unstructured A/U-rich RNA sequences and is similar to the eukaryotic Sm proteins in both sequence and structure. Hfq forms a homo-hexameric ring similar to the heptameric ring of the Sm proteins
NLQDQFLNTLRKEKKPVTIYLVNGVRLKGKIKSFDNFTVLLESDGKQQLIYKHAISTIVP
>gnl|CDD|212464 cd01717, Sm_B, Sm protein B. The eukaryotic Sm proteins (B/B', D1, D2, D3, E, F and G) assemble into a hetero-heptameric ring around the Sm site of the 2,2,7-trimethyl guanosine (m3G) capped U1, U2, U4 and U5 snRNAs (Sm snRNAs) forming the core of the snRNP particle. The snRNP particle, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. Members of this family share a highly conserved Sm fold, containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet
KSSKMLQYINYRMRVTLQDGRQFVGTFLAFDKHMNLVLSDCEEFRKIKPKKKKKGEEREEKRVLGLVLLR
GENVVSMTVE
>gnl|CDD|212465 cd01718, Sm_E, Sm protein E. The eukaryotic Sm proteins (B/B', D1, D2, D3, E, F and G) assemble into a hetero-heptameric ring around the Sm site of the 2,2,7-trimethyl guanosine (m3G) capped U1, U2, U4 and U5 snRNAs (Sm snRNAs) forming the core of the snRNP particle. The snRNP particle, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. Sm subunit E binds subunits F and G to form a trimer which then assembles onto snRNA along with the D1/D2 and D3/B heterodimers forming a seven-membered ring structure
QKVMVQPINLIFRYLQNKSRVQIWLYEQTDMRIEGKIIGFDEYMNLVLDDAEEVHLKTNTRKPLGRILLK
GDNITLIQN
>gnl|CDD|212466 cd01719, Sm_G, Sm protein G. The eukaryotic Sm proteins (B/B', D1, D2, D3, E, F and G) assemble into a hetero-heptameric ring around the Sm site of the 2,2,7-trimethyl guanosine (m3G) capped U1, U2, U4 and U5 snRNAs (Sm snRNAs) forming the core of the snRNP particle. The snRNP particle, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. Sm subunit G binds subunits E and F to form a trimer which then assembles onto snRNA along with the D1/D2 and D3/B heterodimers forming a seven-membered ring structure
HPPELKKYMDKRLSLKLNGNRKVSGVLRGFDPFMNLVLDDAVEEVGDGEKTPIGMVVIRGNSIIMIEALD
>gnl|CDD|212467 cd01720, Sm_D2, Sm protein D2. The eukaryotic Sm proteins (B/B', D1, D2, D3, E, F and G) assemble into a hetero-heptameric ring around the Sm site of the 2,2,7-trimethyl guanosine (m3G) capped U1, U2, U4 and U5 snRNAs (Sm snRNAs) forming the core of the snRNP particle. The snRNP particle, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. Sm subunit D2 heterodimerizes with subunit D1 and three such heterodimers form a hexameric ring structure with alternating D1 and D2 subunits. The D1 - D2 heterodimer also assembles into a heptameric ring containing D2, D3, E, F, and G subunits
FNTGPLSLLTQSVKNNTQVLINCRNNKKLLARVKAFDRHCNMVLENVKEMWTEVPKTGKGKKSKPVNKDR
FISKMFLRGDSVILVLRNP
>gnl|CDD|212468 cd01721, Sm_D3, Sm protein D3. The eukaryotic Sm proteins (B/B', D1, D2, D3, E, F and G) assemble into a hetero-heptameric ring around the Sm site of the 2,2,7-trimethyl guanosine (m3G) capped U1, U2, U4 and U5 snRNAs (Sm snRNAs) forming the core of the snRNP particle. The snRNP particle, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. Sm subunit D3 heterodimerizes with subunit B and three such heterodimers form a hexameric ring structure with alternating B and D3 subunits. The D3 - B heterodimer also assembles into a heptameric ring containing D1, D2, E, F, and G subunits
PIKLLHEAEGHIVTVELKTGEVYRGKLIEAEDNMNCQLKDVTVTARDGKVSKLEQVYIRGSQIRFIILPD
>gnl|CDD|212469 cd01722, Sm_F, Sm protein F. The eukaryotic Sm proteins (B/B', D1, D2, D3, E, F and G) assemble into a hetero-heptameric ring around the Sm site of the 2,2,7-trimethyl guanosine (m3G) capped U1, U2, U4 and U5 snRNAs (Sm snRNAs) forming the core of the snRNP particle. The snRNP particle, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. Sm subunit F is capable of forming both homo- and hetero-heptamer ring structures. To form the hetero-heptamer, Sm subunit F initially binds subunits E and G to form a trimer which then assembles onto snRNA along with the D3/B and D1/D2 heterodimers
NPKPFLNGLTGKPVIVKLKWGMEYKGTLVSVDSYMNLQLANTEEYIDGKFTGNLGEVLIRCNNVLYIRE
>gnl|CDD|212470 cd01723, LSm4, Like-Sm protein 4. The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a hetero-heptameric ring around the 3'-terminus uridylation tag of the gamma-methyl triphosphate (gamma-m-P3) capped U6 snRNA. LSm2-8 form the core of the snRNP particle that, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. LSm1-7 is involved in recognition of the 3' uridylation tag and recruitment of the decapping machinery. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet
LPLSLLRTAQGHPVLVELKNGETYNGHLVNCDNWMNIHLKNVICTSKDGDRFWKMPECYIRGNTIKYLRL
PDEVID
>gnl|CDD|212471 cd01724, Sm_D1, Sm protein D1. The eukaryotic Sm proteins (B/B', D1, D2, D3, E, F and G) assemble into a hetero-heptameric ring around the Sm site of the 2,2,7-trimethyl guanosine (m3G) capped U1, U2, U4 and U5 snRNAs (Sm snRNAs) forming the core of the snRNP particle. The snRNP particle, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. Sm subunit D1 heterodimerizes with subunit D2 and three such heterodimers form a hexameric ring structure with alternating D1 and D2 subunits. The D1 - D2 heterodimer also assembles into a heptameric ring containing DB, D3, E, F, and G subunits
KLVRFLMKLSNETVTIELKNGTVVHGTITGVDVSMNTHLKNVKLTLKGKNPVSLDTLSIRGNNIRYIILP
DSLNLDTLLVDDTPKAKAKKRA
>gnl|CDD|212472 cd01725, LSm2, Like-Sm protein 2. The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a hetero-heptameric ring around the 3'-terminus uridylation tag of the gamma-methyl triphosphate (gamma-m-P3) capped U6 snRNA. LSm2-8 form the core of the snRNP particle that, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. LSm1-7 is involved in recognition of the 3' uridylation tag and recruitment of the decapping machinery. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet
LFFSFFKTLVGKEVTVELKNDLSITGTLHSVDQYLNIKLTNISVNDPEKYPHLLSVKNCFIRGSVVRYVQ
LPADEVDTELLQDATRREA
>gnl|CDD|212473 cd01726, LSm6, Like-Sm protein 6. The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a hetero-heptameric ring around the 3'-terminus uridylation tag of the gamma-methyl triphosphate (gamma-m-P3) capped U6 snRNA. LSm2-8 form the core of the snRNP particle that, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. LSm1-7 is involved in recognition of the 3' uridylation tag and recruitment of the decapping machinery. LSm657 is believed to be an assembly intermediate for both the LSm1-7 and LSm2-8 rings. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet
TPSKFLKKIIGKPVVVKLKNGVEYRGVLACLDGYMNLVLEDTEEYVDGQLVAKYGDAFIRGNNVLYIS
>gnl|CDD|212474 cd01727, LSm8, Like-Sm protein 8. The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a hetero-heptameric ring around the 3'-terminus uridylation tag of the gamma-methyl triphosphate (gamma-m-P3) capped U6 snRNA. LSm2-8 form the core of the snRNP particle that, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. LSm1-7 is involved in recognition of the 3' uridylation tag and recruitment of the decapping machinery. LSm657 is believed to be an assembly intermediate for both the LSm1-7 and LSm2-8 rings. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet
SSLLEDYLNKRVVVITTDGRVIVGTLKGFDQTTNLILSNCHERVYSSDEGVEEVPLGLYLLRGDNVAVIG
EVDEELDGSIDLSKIRAEPLK
>gnl|CDD|212475 cd01728, LSm1, Like-Sm protein 1. The eukaryotic LSm proteins (LSm1-7) assemble into a hetero-heptameric ring around the 3'-terminus of the gamma-methyl triphosphate (gamma-m-P3) capped U6 snRNA. Accumulation of uridylated RNAs in an lsm1 mutant suggests an involvement of the LSm1-7 complex in recognition of the 3' uridylation tag and recruitment of the decapping machinery. LSm1-7, together with Pat1, are also called the decapping activator. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet
PPGTASLEEELDKKILVVLRDGRKLIGILRSFDQFANLVLEDTVERIIVGNQYGDIPRGLFIIRGENVVL
LGEI
>gnl|CDD|212476 cd01729, LSm7, Like-Sm protein 7. The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a hetero-heptameric ring around the 3'-terminus uridylation tag of the gamma-methyl triphosphate (gamma-m-P3) capped U6 snRNA. LSm2-8 form the core of the snRNP particle that, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. LSm1-7 is involved in recognition of the 3' uridylation tag and recruitment of the decapping machinery. LSm657 is believed to be an assembly intermediate for both the LSm1-7 and LSm2-8 rings. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet
KESILDLSKYVDKKIRVKFQGGREVTGILKGYDQLLNLVLDDTVEYLRDPEDPYKLTDETRSLGLVVCRG
TSVVLISPVDGTEEIENPF
>gnl|CDD|212477 cd01730, LSm3, Like-Sm protein 3. The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a hetero-heptameric ring around the 3'-terminus uridylation tag of the gamma-methyl triphosphate (gamma-m-P3) capped U6 snRNA. LSm2-8 form the core of the snRNP particle that, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. LSm1-7 is involved in recognition of the 3' uridylation tag and recruitment of the decapping machinery. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet
EPLDLIRLSLDERVYVKLRGDRELRGRLHAYDQHLNMILGDVEETITTVEIDEETYEEIYKTTKRNIPML
FVRGDGVILVSP
>gnl|CDD|212478 cd01731, archaeal_Sm1, archaeal Sm protein 1. The archaeal Sm1 proteins: The Sm proteins are conserved in all three domains of life and are always associated with U-rich RNA sequences. They function to mediate RNA-RNA interactions and RNA biogenesis. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. Eukaryotic Sm proteins form part of specific small nuclear ribonucleoproteins (snRNPs) that are involved in the processing of pre-mRNAs to mature mRNAs, and are a major component of the eukaryotic spliceosome. Most snRNPs consist of seven Sm proteins (B/B', D1, D2, D3, E, F and G) arranged in a ring on a uridine-rich sequence (Sm site), plus a small nuclear RNA (snRNA) (either U1, U2, U5 or U4/6). Since archaebacteria do not have any splicing apparatus, their Sm proteins may play a more general role. Archaeal LSm proteins are likely to represent the ancestral Sm domain
RPLDVLNESLNKNVLVKLKGGKEVRGVLKGFDQHLNLVLENAEEIIEGESVRKLGTVLVRGDNVVFISP
>gnl|CDD|212479 cd01732, LSm5, Like-Sm protein 5. The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a hetero-heptameric ring around the 3'-terminus uridylation tag of the gamma-methyl triphosphate (gamma-m-P3) capped U6 snRNA. LSm2-8 form the core of the snRNP particle that, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. LSm1-7 is involved in recognition of the 3' uridylation tag and recruitment of the decapping machinery. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet
QILPLELIDKCIGSKIWIIMKSDKEFVGTLLGFDDYVNMVLEDVTEYEITPEGRKITKLDQILLNGNNIA
MLVPGG
>gnl|CDD|212480 cd01733, LSm10, Like-Sm protein 10. The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. LSm10 is an SmD1-like protein which is thought to bind U7 snRNA along with LSm11 and five other Sm subunits to form a 7-membered ring structure. LSm10 and the U7 snRNP of which it is a part are thought to play an important role in histone mRNA 3' processing
RERYRSENSLVCLLQALQGRVTTVELRNETSVRGIIDNVDGFMNITLSDATFTDRRGKQHHFDEFFVQGR
NIRYVHIP
>gnl|CDD|212481 cd01734, YlxS_C, Bacillus subtilis YxlS-like, C-terminal domain. YxlS is a Bacillus subtilis gene of unknown function with two domains that each have an alpha/beta fold. The N-terminal domain is composed of two alpha-helices and a three-stranded beta-sheet, while the C-terminal domain is composed of one alpha-helix and a five-stranded beta-sheet. This CD represents the C-terminal domain which has a fold similar to the Sm fold of proteins like Sm-D3
GLDRPLKKPEDFERFIGKEVKVKLKEPIDGRKKFTGELLGVDDDTVTLEVDDGKEVEIPFDNIAKARLVP
EF
>gnl|CDD|212482 cd01735, LSm12_N, Like-Sm protein 12, N-terminal domain. LSm12 belongs to a family of Sm-like proteins that associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet that associates with other Sm proteins to form hexameric and heptameric ring structures. In addition to the N-terminal Sm-like domain, LSm12 has a novel methyltransferase domain
EYFSVGSQVSCKTCFGQRIQGEVVAFDHPSKMLALKCPSSSGKPNLADISIVNLDYVSDVE
>gnl|CDD|212483 cd01736, LSm14_N, Like-Sm protein 14, N-terminal domain. LSm14 (also known as RAP55) belongs to a family of Sm-like proteins that associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold, containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet, that associates with other Sm proteins to form hexameric and heptameric ring structures. In addition to the N-terminal Sm-like domain, LSm14 has an uncharacterized C-terminal domain containing a conserved DFDF box. In Xenopus laevis, LSm14 is an oocyte-specific constituent of ribonucleoprotein particles
GTPYIGSKISLISKSDIRYEGILYTIDTEDSTIALKNVRSFGTEGRPTGRPIPPSDEVYDYIVFRGSDIK
DLTV
>gnl|CDD|212484 cd01737, LSm16_N, Like-Sm protein 16, N-terminal domain. LSm16 (also known as enhancer of decapping-3 or EDC3) has been shown to be associated with an mRNA-decapping complex Dcp1-Dcp2, required for removal of the 5-prime cap from mRNA prior to its degradation from the 5-prime end. EDC3 is believed to be a scaffold for decapping complex formation. It belongs to a family of Sm-like proteins that associate with RNA to form complexes involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold, containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet, that associates with other Sm proteins to form hexameric and heptameric ring structures. LSm16 has, in addition to its N-terminal Sm-like domain, a C-terminal Yjef_N-type Rossmann fold domain of unknown function
AEDFIGSAVSIHCGDTLGVYQGVISNVDPTNQTISLRKAFRNGLKCQVPEVTLSAKDIKDLKIIE
>gnl|CDD|212485 cd01739, LSm11_M, Like-Sm protein 11, middle domain. The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. LSm11 is an SmD2-like subunit which binds U7 snRNA along with LSm10 and five other Sm subunits to form a 7-membered ring structure. LSm11 and the U7 snRNP of which it is a part are thought to play an important role in histone mRNA 3' processing
LHRWMRDRTRVKVYIRKAKGIRGSCEGYLVAFDKHWNLALVDVDETWTRRKYKYGEQAIPDTR
>gnl|CDD|153211 cd01740, GATase1_FGAR_AT, Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase. Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site
VAVLRFPGSNCDRDMAYAFELAGFEAEDVWHNDLLAGRKDLDDYDGVVLPGGFSYGDYLRAGAIAAASPL
LMEEVKEFAERGGLVLGICNGFQILVELGLLPGALIRNKGLKFICRWQNRFVTLRVENNDSPFTKGYMEG
EVLRIPVAHGEGRFYADDETLAELEENGQIAQYVDDDGNVTERYPANPNGSLDGIAGICNEDGRVLGMMP
HPERAVEPWQWERLLGGSDGLKLFRNAV
>gnl|CDD|153212 cd01741, GATase1_1, Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase
RILILQHDTPEGPGLFEDLLREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVDEDDYPWLKKL
KELIRQALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPVFHW
HGDTVVELPPGAVLLASSEACPNQAFRYGDRALGLQFHPEERLLRNFL
>gnl|CDD|153213 cd01742, GATase1_GMP_Synthase, Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site
ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELG
VPVLGICYGMQLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVI
ASSDNCPVAAIANEEKKIYGVQFHPEVTHTEKGKEILKNFL
>gnl|CDD|153214 cd01743, GATase1_Anthranilate_Synthase, Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase. Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA
ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAG
KVPILGVCLGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLL
EVTASTEDGVIMALRHRDLPIYGVQFHPESILTEYGLRLLENFL
>gnl|CDD|153215 cd01744, GATase1_CPSase, Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I
VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKI
PIFGICLGHQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLN
DGTVEGIRHKDLPVFSVQFHPEASPGPHDTEYLFDEFL
>gnl|CDD|153216 cd01745, GATase1_2, Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase
IGITARLREEEGGYERRDYLNQYYVDAVRKAGGLPVLLPPVDDEEDLEQYLELLDGLLLTGGGDVDPPLY
GEEPHPELGPIDPERDAFELALLRAALERGKPILGICRGMQLLNVALGGTLYQDIRVNSLHHQAIKRLAD
GLRVEARAPDGVIEAIESPDRPFVLGVQWHPEWLADTDPDSLKLFEAFV
>gnl|CDD|153217 cd01746, GATase1_CTP_Synthase, Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase. Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site
VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEENAEEALKGADGILVPGGFGIRGV
EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQKGVKDLGGT
MRLGAYPVILKPGTLAHKYYGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPF
FVGTQFHPEFKSRPLKPHPLFVGFV
>gnl|CDD|153218 cd01747, GATase1_Glutamyl_Hydrolase, Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site
IGILTQPVDGAGSNKTGHSYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVDIDTS
GYARTAKIIYNLALERNDAGDYFPVWGTCLGFELLTYLTSGETLLLEATEATNSALPLNFTEDALQSRLF
KRFPPDLLKSLATEPLTMNNHRYGISPENFTENGLLSDFFNVLTTNDDWNGVEFISTVEAYKYPIYGVQW
HPEKNAFEWKKSSSIPHSEEAIRLTQYFANFFVNEARKSNNRFESAEEETKHLIYNYKPTYTG
>gnl|CDD|153219 cd01748, GATase1_IGP_Synthase, Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site
IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIAS
GKPFLGICLGMQLLFESSEEGGGTKGLGLIPGKVVRFPASEGLKVPHMGWNQLEITKESPLFKGIPDGSY
FYFVHSYYAPPDDPDYILATTDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNFL
>gnl|CDD|153220 cd01749, GATase1_PB, Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6
IGVLALQGDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLREFIRAGK
PVFGTCAGLILLAKEVEDQGGQPLLGLLDITVRRNAFGRQVDSFEADLDIPGLGLGPFPAVFIRAPVIEE
VGPGVEVLAEYDGKIVAVRQGNVLATSFHPELTDDTRIHEYFL
>gnl|CDD|153221 cd01750, GATase1_CobQ, Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ
IAVIRYPDISNFTDLDPLAREPGVDVRYVEVPEGLGDADLIILPGSKDTIQDLAWLRKRGLAEAIKNYAR
AGGPVLGICGGYQMLGKYIVDPEGVEGPGEIEGLGLLDVETEFGPEKTTRRVTGRLDEEGEGGEVTGYEI
HSGRTTLGDGARPLGKGYGNNGEDGTDGAVSGDNVIGTYLHGIFLNDAFRDALL
>gnl|CDD|238849 cd01751, PLAT_LH2, PLAT/ LH2 domain of plant lipoxygenase related proteins. Lipoxygenases are nonheme, nonsulfur iron dioxygenases that act on lipid substrates containing one or more (Z,Z)-1,4-pentadiene moieties. In plants, the immediate products are involved in defense mechanisms against pathogens and may be precursors of metabolic regulators. The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins
VKVKATVTVMKKNKLDLNDDGSGLDDLDDLLGRSLLLELVSSELDPKTGKGKKGKAAFLEGWGKSLAGES
AYEAEFEVPASFGPPGAVLVKNEHHSEFFLKSITLEGFGGSGTITFVCNSWVYPKKDYPDKRIFFPN
>gnl|CDD|238850 cd01752, PLAT_polycystin, PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins
YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLW
HDNSGLSPSWYLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPVA
>gnl|CDD|238851 cd01753, PLAT_LOX, PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. Both types of enzymes are cytosolic but need this domain to access their sequestered membrane or micelle bound substrates
AEYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYDFERGAVDEYKVKVPEDLGELLLVRLRK
RKYLLFDAWFCNYITVTGPGGDEYHFPCYRWIEGYGTLELREG
>gnl|CDD|238852 cd01754, PLAT_plant_stress, PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of its members are stress induced. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins
CVYTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAWGGLMGAGHDYFERGNLDRFSGRGPCLPSP
PCWMNLTSDGTGNHPGWYVNYVEVTQAGQHAPCMQHLFAVEQWLATDESPYMLTAVRNN
>gnl|CDD|238853 cd01755, PLAT_lipase, PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major subgroups, the lipoprotein lipase (LPL) and the pancreatic triglyceride lipase. LPL is a key enzyme in catabolism of plasma lipoprotein triglycerides (TGs). The central role of triglyceride lipases is in energy production. In general, PLAT/LH2 domain's proposed function is to mediate interaction with lipids or membrane bound proteins
WHYQVKVHLSGKKNLEVDGTFTVSLYGTKGETEQLPIVLGELKPNKTYSFLIDTEVDIGDLLKVKFKWEN
NVINSNSGETLPKLGARKIRVKSGETQKKFTFCSQDTVRELEVLQTLVKC
>gnl|CDD|238854 cd01756, PLAT_repeat, PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins
VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIG
HDNSGLGAGWFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS
>gnl|CDD|238855 cd01757, PLAT_RAB6IP1, PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an eight stranded beta-barrel. In RabIP1 this domain may participate in lipid-mediated modulation of Rab6IP1's function via it's generally proposed function of mediating interaction with lipids or membrane bound proteins
MPYHVVIVPSKKLGGSMFTANPWICVSGELGETPPLQIPKNSLEMTFDCQNLGKLTTVQIGHDNSGLLAK
WLVEYVMVRNEITGHTYKFPCGRWLGEGVDDGNGEDGSLERVLV
>gnl|CDD|238856 cd01758, PLAT_LPL, PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of plasma lipoprotein triglycerides (TGs) and has therefeore has a profound influence on triglyceride and high-density lipoprotein (HDL) cholesterol levels in the blood. In general, PLAT/LH2 domain's proposed function is to mediate interaction with lipids or membrane bound proteins
FHYQLKIHFFNQTNRIETDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKW
EGSSLWSNSWWTVQTIIPWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC
>gnl|CDD|238857 cd01759, PLAT_PL, PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and triglycerides to generate fatty acids for energy production or for storage and to release inositol phosphates that act as second messengers. The central role of triglyceride lipases is in energy production. The proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins
WRYKVSVTLSGKKKVTGTILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWNNNV
INITLPKVGAEKITVQSGKDGKVFNFCSSETVRENVLQTLTPC
>gnl|CDD|340461 cd01760, RBD, Ras-binding domain (RBD), structurally similar to a beta-grasp ubiquitin-like fold. The RBD of the serine/threonine kinase Raf is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. A Raf-like RBD is also present in Regulator of G protein Signaling (RGS12 and RGS14) members of GTPase activating proteins
NTFRLFLPNNETSVVVAVKPGKSLHEVLMPVLERHGLQLECVDVFLLGEKAPLDLNTDASSLIGQELRLD
F
>gnl|CDD|340462 cd01763, Ubl_SUMO_like, ubiquitin-like (Ubl) domain found in small ubiquitin-related modifier (SUMO) and similar proteins. SUMO (also known as "Smt3" and "sentrin" in other organisms) resembles ubiquitin (Ub) in structure, ligation to other proteins, and the mechanism of ligation. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of Ub and the epsilon-amino group of a substrate lysine. SUMOs, like Ub, are covalently conjugated to lysine residues in a wide variety of target proteins in eukaryotic cells and regulate numerous cellular processes, such as transcription, epigenetic gene control, genomic instability, and protein degradation. The mammalian SUMOs have four paralogs, SUMO1 through SUMO4, which all regulate different cellular functions by conjugating to different proteins. SUMO2-4 are more closely related to each other than to SUMO1
KITIKVRGQDGGKKVRFKVKKTTKLKKLFDAYAEKKGLDPDSLRFTFDGERISPNDTPESLGLEDGDIID
VV
>gnl|CDD|340463 cd01764, Ubl_Urm1, ubiquitin-like (Ubl) domain found in ubiquitin-related modifier 1 (Urm1). Urm1 acts as a sulfur carrier in the thiolation of eukaryotic tRNA via a mechanism that requires the formation of a thiocarboxylated Urm1, which is similar to that of prokaryotic sulfur carrier proteins such as ThiS and MoaD, containing the beta-grasp ubiquitin-like (Ubl) fold. Urm1 can be covalently conjugated to lysine residues of other proteins through a mechanism involving the E1-like protein Uba4. Urm1 is involved in yeast bioprocesses such as budding, nutrient sensing, high temperature sensitivity, antioxidant stress response and post-translation modification of the elongator subunit
ITVEFSGGLELLFGKQKKHEVELPSQKPWTLRDLLAWIRDNLLKERPELFIQGDTVRPGILVLINDADWE
LLGELDYELQDGDRITFISTLHGG
>gnl|CDD|340464 cd01765, FERM_F0_F1, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins. FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin
ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKHWLDLDKKISKQLKRSG
PYQFYFRVKF
>gnl|CDD|340465 cd01766, Ubl_UFM1, ubiquitin-like (Ubl) domain found in ubiquitin fold modifier 1 (UFM1). UFM1 belongs to the ubiquitin-like protein family with similar ubiquitin beta-grasp folds and mechanism of ligation to other proteins. UFM1 is present in nearly all eukaryotic organisms except fungi. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The UNF1 cascade has been implicated in endoplasmic reticulum functions, cell cycle control and cell differentiation. The involvement of the UFM1 cascade in diseases is diverse; reports include its involvement in ischemic heart diseases, diabetes, gastric lesions, schizophrenia, hip dysplasia and cancer
VTFKITLTSDPKLPFKVLSVPEEAPFTAVLKFAAEEFKVPAATSAIITNDGIGINPAQTAGNVFLKHGSE
LRLIP
>gnl|CDD|340466 cd01767, UBX, Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold. The UBXD family of proteins contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. Members in this family function as cofactors of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. Based on domain composition, UBXD proteins can be divided into two main groups, with and without ubiquitin-associated (UBA) domain
RIQIRLPDGSRIQRRFSKSDTLQDLYDFVESNLGDSPSSFSLVTSFPRRVLTDEDSDKTLEELGLTPNAV
LFVE
>gnl|CDD|340467 cd01768, RA_FERM_F0_F1_like, Ras-associating (RA) domain, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0/F1 sub-domain, structurally similar to a beta-grasp ubiquitin-like fold. RA domain-containing proteins function by interacting, directly or indirectly, with Ras proteins and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras protein is a small GTPase that is involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon. The FERM domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, also known as the N-terminal Ubl-like structural domain of the FERM domain (FERM_N), which is structurally similar to Ub. Some FERM domain-containing proteins contain an N-terminal region, which also has the beta-grasp Ub-like fold, precedes the FERM domain and has been referred to as the F0 domain
VLKIFGAGLASGANYKSVLATARSTARELVAEALERYGLAGSPGGGPGESSCVDAFALCDALGRPAAAGV
GSGEWRAEHLRVLGDSERPLLVQELWRARPGWARRFELRG
>gnl|CDD|340468 cd01770, UBX_UBXN2, Ubiquitin regulatory domain X (UBX) found in UBX domain-containing proteins UBXN2A, UBXN2B, NSFL1C/UBXN2C, and similar proteins. This family includes UBX domain-containing proteins UBXN2A, UBXN2B, and NSFL1C/UBXN2C, which contain a SEP (Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47) domain, and a ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold at the C-terminus. UBX domain participates broadly in the regulation of protein degradation. UBXN2A, UBXN2B, and UBXN2C function as the adaptor proteins of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation
SIQIRLADGSRLVARFNLTHTVGDIRQFIDSARPGYSRPFVLMTGFPPKELTDESQTLEEAGLLNAVVVQ
K
>gnl|CDD|340469 cd01771, UBX_UBXN3A, Ubiquitin regulatory domain X (UBX) found in FAS associated factor 1 (FAF1, also known as UBXN3A) and similar proteins. UBX domain-containing protein 3A (UBXN3A),also termed UBX domain-containing protein 12 (UBXD12), or FAF1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, FAF1 contains two tandem ubiquitin-like (Ubl) domains, which shows high structural similarity with UBX domain. FAF1 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The FAF1-p97 complex inhibits the proteasomal protein degradation in which p97 acts as a co-chaperone. Moreover, FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF1 is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kappaB (NF-kappaB) by interfering with the nuclear translocation of the p65 subunit. Although the precise role of FAF1 in the ubiquitination pathway remains unclear, FAF1 interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway. This family corresponds to UBX domain
TEPISKLRFRLPGGEFLTRRFLASEPLQVLLNFVASKGYPPDEYKLLTTFPRRDLTQLDPSKTLEELKLF
PQETLFLEER
>gnl|CDD|340470 cd01772, UBX_UBXN1, Ubiquitin regulatory domain X (UBX) found in UBX domain protein 1 (UBXN1) and similar proteins. UBXN1, also termed SAPK substrate protein 1 (SAKS1), UBA/UBX 33.3 kDa protein (Y33K), or UBXD10, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (Ubl or UBX) domain that has a beta-grasp ubiquitin-like fold without the C-terminal double glycine motif. UBXN1 has been identified as a substrate for stress-activated protein kinases (SAPKs). It binds polyubiquitin and valosin-containing protein (VCP), suggesting a role as an adaptor that directs VCP to polyubiquitinated proteins facilitating its destruction by the proteasome. In addition, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and be involved in the Ub-proteasome proteolytic pathways. UBXN1 can also associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domains
KKEYDECRLQVRLTNGSTLTQTFGAKEQLAAVRLYVELNRTDGDGPFSLMTTFPRKVFTEEDMEKPLKEL
GLVPSAVLIVT
>gnl|CDD|340471 cd01773, UBX_UBXN7, Ubiquitin regulatory domain X (UBX) found in UBX domain protein 7 (UBXN7) and similar proteins. UBXN7, also termed UBX domain-containing protein 7 (UBXD7), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN7 functions as a ubiquitin-binding adaptor that mediates the interaction between the AAA+ ATPase p97 (also known as VCP or Cdc48) and the transcription factor HIF1-alpha. It binds only to the active, NEDD8- or Rub1-modified form of cullins. In addition to having a UBX domain, UBXD7 contains a ubiquitin-associated (UBA), ubiquitin-associating (UAS), and ubiquitin-interacting motif (UIM) domains. Either UBA or UIM could serve as a docking site for neddylated-cullins. UBA domain is required for binding ubiquitylated-protein substrates, while the UIM motif is responsible for the binding to cullin RING ligases (CRLs), and the UBX domain is essential for p97 binding
KSKLMLRFPDGKREQLSLPASAKLKALVKYVSSKGYPNERYELVTNFPRRKLSHLDYDITLKEAGLCPQE
TIFVQE
>gnl|CDD|340472 cd01774, UBX_UBXN8, Ubiquitin regulatory domain X (UBX) found in UBX domain protein 8 (UBXN8) and similar proteins. UBXN8, also termed reproduction 8 protein (Rep8), or UBX domain-containing protein 6 (UBXD6), or D8S2298E, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN8 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. UBXN8 is a transmembrane protein that localizes to the endoplasmic reticulum (ER) membrane with its UBX domain facing the cytoplasm. It facilitates efficient ER-associated degradation (ERAD) by tethering p97 to the ER membrane
GAVTIALRFPGGRVHRRRFLTTENIQVLLDWMTKLGYHQTLYTLSTTYPRTILSDDADKTLEDLGITKDV
ALNVEE
>gnl|CDD|340473 cd01775, RA_PHLPP_like, Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein phosphatases, fungal adenylate cyclase, and similar proteins. PHLPP represents a novel family of Ser/Thr protein phosphatases, which is involved in two key signaling pathways, the phosphatidylinositol 3-kinase and diacylglycerol signaling pathways, by directly dephosphorylating and inactivating Akt serine-threonine kinases (Akt1, Akt2, Akt3) and protein kinase C (PKC) isoforms. PHLPP contains a putative Ras-associating (RA) domain followed by a pleckstrin homology (PH) domain, a series of leucine-rich repeats and a protein phosphatase 2C (PP2C) domain. Fungal adenylate cyclase regulates developmental processes such as hyphal growth, biofilm formation, and phenotypic switching. It plays an essential role in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP. Fungal adenylate cyclase has at least four domains, including an N-terminal adenylate cyclase G-alpha binding domain, a Ras-associating (RA) domain, a middle leucine-rich repeat region, and a catalytic domain. The RA domain of adenylate cyclase post-translationally modifies a small GTPase called Ras, which is involved in cellular signal transduction. The activity of adenylate cyclase is stimulated directly by regulatory proteins (Ras1 and Gpa2), peptidoglycan fragments and carbon dioxide
GSIRVYKADSKFTTVSCTINTTVSEIIAGLGRKSFLNANEDYRILLKHGGLVRRLRPDEKPLRIQRDLLL
LLGYTDPDRQEEATNPDLSYVIKFVFEKP
>gnl|CDD|340474 cd01776, RA_Rin, Ras-associating (RA) domain of Ras and Rab interactor (Rin) protein family. Family of Ras-interaction/interference (Rin) proteins, also known as Ras and Rab interactors, is composed of Rin1, Rin2, and Rin3, which have multifunctional domains, including SH2 and proline-rich domains in the N-terminal region, and RH, VPS9, and RA domains in the C-terminal region. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The RA domains of Rin1, Rin2, and Rin3 are well conserved and they all have Ras binding characteristics
QGFLRVAVPDENNGSIVSKTLPVRPSMTAREVCKMIAHKFRVTNPQDYGLFLLVDGEEIQLEDNECPQLI
KGELLATSKKPCYFAYKRID
>gnl|CDD|340475 cd01777, FERM_F1_SNX27, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 27 (SNX27). SNX27 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. In addition to a PX (Phox homology) domain that regulates its endosomal localization, SNX27 has a unique PDZ (Psd-95/Dlg/ZO1) domain and an atypical FERM (4.1, ezrin, radixin, moesin) domain that both function to bind short peptide sequence motifs in the cytoplasmic domains of the cargo receptors. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
SDVELKVLLPDRTTVTVSVKKNSNTDQVYQALVEKLGMDSETANYFALFEIIEYNFERKLQPNEFPHNLY
IQNYSTASATCITLRKWLFTLA
>gnl|CDD|340476 cd01778, RA_RASSF1_like, Ras-associating (RA) domain found in Ras-association domain family members, RASSF1, RASSF3, and RASSF5. The RASSF family of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain which is located either at the C-terminus (RASSF1-6, the classical group) or at the N-terminus (RASSF7-10). RASSF1-6 contains a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that functions in scaffolding and regulatory interactions. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. Classical RASSF members interact either directly or indirectly with activated Ras. Ras proteins are small GTPases that are involved in cellular signal transduction. The classical RASSF proteins seem to modulate some of the growth inhibitory responses mediated by Ras and may serve as tumor suppressor genes. This family contains RASSF1, RASSF3, and RASSF5
GSFQGFIRVHMNLTRPISVSAGTRPPSIYDVLKLEDSGDSRKTRTSFYLPKDTVKALHITSDTTAREVIE
ALLKKFKITDNPRKFALYERTHEEEGKVKLRKLSDDERPLYLCLLWGSQGDSKSFVLQEN
>gnl|CDD|340477 cd01779, RA_Myosin-IX, Ras-associating (RA) domain found in Myosin-IX. Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains and a C-terminal tail containing a Rho-GTPase activating protein (RhoGAP) domain. The RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis and IXb is expressed abundantly in tissues of the immune system
MVRVYPGALSPETEFLSVEATKQTTASEVIECLVAKLRLDKAECYELAEVCGSGGQGCKERRLGPSENPV
QVQLLWPKMAGDSDNQVTSYRFFLREK
>gnl|CDD|340478 cd01780, RA2_PLC-epsilon, Ras-associating (RA) domain 2 found in Phosphatidylinositide-specific phospholipase C (PLC)-epsilon. PLC is a signaling enzyme that hydrolyzes membrane phospholipids to generate inositol triphosphate. PLC-epsilon represents a novel forth class of PLC that has a PLC catalytic core domain, a CDC25 guanine nucleotide exchange factor domain and two RA (Ras-association) domains. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. Although PLC RA1 and RA2 have homologous ubiquitin-like folds only RA2 can bind Ras and activate it. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and involve in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. This family corresponds to the second RA domain of PLC-epsilon
EDTFLVCVHNVSPDQPYTILKAPVSSTAQDIIAQALVKARRSEDIPSDFVLVEELEKEPTSDKSSSKSSS
SKTEQRVLGDQENVYQAQSRWKGAGKFILKLR
>gnl|CDD|340479 cd01781, RA2_Afadin, Ras-associating (RA) domain 2 found in Afadin. Afadin, also termed ALL1-fused gene from chromosome 6 protein (AF-6), or canoe, is involved in many fundamental signaling cascades in cells. In addition, it is involved in oncogenesis and metastasis. Afadin has multiple domains: from the N-terminus to the C-terminus it has two Ras-associated (RA) domains, a forkhead-associated domain, a dilute domain, a PDZ domain, three proline-rich domains, and an F-actin binding domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Afadin is abundant at cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. This family corresponds to the second RA domain of afadin
GGTLKIYGDSLKPEVPYKTLLLSTNDTADFVVREALEKYGLEKENPKDYCLVQVVLPPGGSPRLDGGGGK
ERILDDDECPLAILMRWPPSKGTLVFQLRRRP
>gnl|CDD|340480 cd01782, RA1_Afadin, Ras-associating (RA) domain 1 found in Afadin. Afadin, also termed ALL1-fused gene from chromosome 6 protein (AF-6), or canoe, is involved in many fundamental signaling cascades in cells. In addition, it is involved in oncogenesis and metastasis. Afadin has multiple domains: from the N-terminus to the C-terminus it has two Ras-associated (RA) domains, a forkhead-associated domain, a dilute domain, a PDZ domain, three proline-rich domains, and an F-actin-binding domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Afadin is abundant at cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. This family corresponds to the first RA domain of afadin, which mediates its self-association
WNANRLDLFELSQPNEDLEFHGVMRFYFQDGGAKVATKCIRVSSTATTQDVIETLIEKFRPDMRMLSNPR
YSLYEVHPNGEERKLDDDEKPLVVQLNWNKDDREGRFLLKNE
>gnl|CDD|340481 cd01783, RA2_DAGK-theta, Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins. DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. There are ten mammalian isoforms of DAGK have been identified to date, these are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the second RA domain of DAGK-theta
GYIRVYPGWLKVGVAYKSIPVTKETTVEEVIKEALPKFGLQDEDPEDFRLVEVLMDKGVVERVMLRDECP
WLILLDIRKESLRQMRQTRFYLQQK
>gnl|CDD|340482 cd01784, RA_RASSF2_like, Ras-associating (RA) domain found in Ras-association domain family members, RASSF2, RASSF4, and RASSF6. The RASSF family of proteins shares a conserved RalGDS/AF6 RA domain either in the C-terminus (RASSF1-6) or N-terminus (RASSF7-10). The classical family members (RASSF1-6) contain a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that functions as scaffolding and regulatory interactions. The RA domain of the classical RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. Classical RASSF members interact either directly or indirectly with activated Ras. Ras proteins are small GTPases that are involved in cellular signal transduction. The classical RASSF protein family seem to modulate some of the growth inhibitory responses mediated by Ras and may serve as tumor suppressor genes. This family contains RASSF2, RASSF4, and RASSF6
NRKTSVFTPPYGSVTNVRVTSLMTTPEVIKLLLEKFKVENSPEEFALYVVKDSGERRRLKDDDYPLLTRV
LLGPSEDVAKIFIMERA
>gnl|CDD|340483 cd01785, RA_PDZ-GEF1, Ras-associating (RA) domain found in PDZ domain-containing guanine nucleotide exchange factor 1 (PDZ-GEF1) and similar proteins. PDZ-GEF1, also termed Rap guanine nucleotide exchange factor 2, or cyclic nucleotide ras GEF (CNrasGEF), or neural RAP guanine nucleotide exchange protein (nRap GEP), or Ras/Rap1-associating GEF-1 (RA-GEF-1), is a Rap-specific guanine nucleotide exchange factor (GEF) that has a PSD-95/DlgA/ZO-1 (PDZ) domain, a RA domain and a region related to a cyclic nucleotide binding domain (RCBD). The RA domain of PDZ-GEF interacts with Rap1 and also contributes to the membrane localization of PDZ-GEF. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and involve in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes
QVLKVYRADQSSKYILIHKETTAREVVMLALREFGITDDENSDNYSLCEVTVTPEGLIKQRRLPDQLSNL
ANRISLNGRYYLKNN
>gnl|CDD|340484 cd01786, RA_STE50, Ras-associating (RA) domain found in the fungal adaptor protein STE50. The fungal adaptor protein STE50 is an essential component of three MAPK-mediated signaling pathways that control the mating response, invasive/filamentous growth and osmotolerance (HOG pathway), respectively. STE50 functions in cell signaling between the activated G protein and STE11. The domain architecture of STE50 includes an amino-terminal SAM (sterile alpha motif) domain in addition to the carboxy-terminal ubiquitin-like RA (RAS-associated) domain. RA domain of STE50 interacts with the small GTPase Cdc42p, a member of Rho type of the Ras superfamily. This interaction activates Ste11p/Ste7p/Kss1pMAP kinase cascade that controls filamentous growth. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes
VSPTSSTIGSPELEPASPRNGIGPRPPEALKNRKVSVEDPCAKVLPAALKKYKINGDWRQYALFIAYGDK
ERCLSYDEKPLLVFQRLKEQGKNPVFVLRRI
>gnl|CDD|340485 cd01787, RA_MRL, Ras-associating (RA) domain of Mig10/RIAM/Lpd (MRL) family. MRL proteins share a common structural architecture, including a central structural unit consisting of a Ras-associating (RA) domain and a pleckstrin homology (PH) domain, an upstream coiled-coil region, and a number of polyproline motifs. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. RA and PH form a tandem domain pair (RA-PH), and serve tightly coordinated functions in both Ras GTPase signaling via the RA domain and membrane translocalization via the PH domain. MRL proteins have distinct functions in cell migration and adhesion, signaling, and in cell growth
KLVVKVHMEDGSSKTLLVDERMTVRQVLKQLIEKNHCDPSVDWCLVEQYPDLYMERVFEDHEKLVENLLN
WTRDSTNKLLFLERT
>gnl|CDD|340486 cd01788, Ubl_ElonginB, ubiquitin-like (Ubl) domain found in transcription elongation factor B (Elongin B) and similar proteins. Elongin B, also termed Elongin 18 kDa subunit, or EloB, or RNA polymerase II transcription factor SIII subunit B (SIII p18), is part of an E3 ubiquitin ligase complex called VEC that activates ubiquitination by the E2 ubiquitin-conjugating enzyme Ubc5. VEC is composed of von Hippel-Lindau tumor suppressor protein (pVHL), elongin C, cullin 2, NEDD8, and Rbx1. ElonginB binds elonginC to form the elonginBC complex which is a positive regulator of RNA polymerase II elongation factor Elongin A. The BC complex then binds VHL (von Hippel-Lindau) tumor suppressor protein to form a VCB ternary complex. Elongin B has a ubiquitin-like (Ubl) domain. Ub has a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair
DVFLMIRRKKTTIFTDAKESTTVFELKKIIEGILKRPPEDQRLYKDDQLLDDTKTLGDCGFTSQTARAQA
PATLGLAFRADGEFEPLEITPLSSPPELPDV
>gnl|CDD|340487 cd01789, Ubl_TBCB, ubiquitin-like (Ubl) domain found in tubulin-folding cofactor B (TBCB) and similar proteins. TBCB, also termed cytoskeleton-associated protein 1, or cytoskeleton-associated protein CKAPI, or tubulin-specific chaperone B, is one of protein cofactors A through E that is required for the folding of tubulins prior to their incorporation into microtubules and heterodimer assembly. TBCB comprises an N-terminal ubiquitin-like (Ubl) domain and a C-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain. The Ubl domain of TBCB is essential for proper folding and assembly of tubulin alpha. It has a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. TBC-A through E are necessary for the biogenesis of microtubules and for cell viability
VNLHITHSNLSSFFSEKRFDLSLTIGELKEKLELITGTPPSSMKLQLYDEDGKLIGTLDDDDALLGSYPV
RDGMRIHVVD
>gnl|CDD|340488 cd01790, Ubl_HERP, ubiquitin-like (Ubl) domain found in homocysteine-inducible endoplasmic reticulum stress protein HERP. HERP is an endoplasmic reticulum (ER) integral membrane protein containing an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold. The Ubl domain is required for the degradation of HERP itself as well as for HERP-mediated anti-apoptotic effects. HERP is induced by the ER stress response pathway and is involved in improving the balance of folding capacity and protein loads in the ER. There are two types of HERP, HERP1 and HERP2, which are encoded by the HERPUD1 and HERPUD2 genes, respectively
VTLVVKSPNQRIQDLTVNCTLGWTVLKLKEHLSEVYPSKPLPEDQKLIYSGKLLEDHQTLKDVLREDDPE
QVHTVHLV
>gnl|CDD|340489 cd01791, Ubl_UBL5, ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins. UBL5, known as Hub1 in yeast, is an atypical ubiquitin-like (Ubl) post-translational modifier that contains a conserved Ubl domain with a beta-grasp Ubl fold. At the C-terminal end of its Ubl fold is a di-tyrosine motif followed by a single variable residue instead of the characteristic di-glycine found in all other Ubl modifiers, and thus UBL5 does not form covalent conjugates with cellular proteins. The yeast Hub1p binds non-covalently to the HIND element of spliceosomal protein Snu66p (Snu66p is termed SART1 in mammals) and modifies the spliceosome by this unconventional Ubl modifier. In higher eukaryotes, UBL5/Hub1 plays a role in modulating pre-mRNA splicing. It also is required for signaling in the mitochondrial unfolded protein response, through interaction with the transcription factor DVE-1 and upregulation of chaperone genes in response to mitochondrial stress. Moreover, UBL5 functions as a factor that directly binds to and stabilizes FANCI, and promotes the functionality of the Fanconi anemia (FA) DNA repair pathway
MIEVICNDRLGKKVRVKCNPDDTIGDLKKLIAAQTGTRPEKIVLKKWYTIFKDHITLEDYEIHDGMNLEL
Y
>gnl|CDD|340490 cd01792, Ubl1_ISG15, ubiquitin-like (Ubl) domain 1 found in interferon-stimulated gene 15 (ISG15) and similar proteins. ISG15, also termed interferon-induced 15 kDa protein, or interferon-induced 17 kDa protein (IP17), or ubiquitin cross-reactive protein (UCRP), is an antiviral interferon-induced ubiquitin-like protein (Ubl) that upon viral infection, modifies cellular and viral proteins by mechanisms similar to ubiquitination. Although ISG15 has properties similar to those of other Ubl molecules, it is a unique member of the Ubl superfamily, whose expression and conjugation to target proteins are tightly regulated by specific signaling pathways, indicating it may have specialized functions in the immune system. ISG15 contains two tandem Ubl domains with a beta-grasp Ubl fold. This family corresponds to the first Ubl domain
WDLTVKMLTGNEFQVSVSPSMTVSELKAQITQKIGVPAFQQRLAVQPSGVELQDGVRLASQGLGPSSTVL
LVVKK
>gnl|CDD|340491 cd01793, Ubl_FUBI, ubiquitin-like (Ubl) domain found in ubiquitin-like protein FUBI and similar proteins. FUBI is a pro-apoptotic regulatory gene FAU encoding ubiquitin-like protein with ribosomal protein S30 as a C-terminal extension. FUBI functions as a tumor suppressor protein that may be involved in the ATP-dependent proteolytic activity of ubiquitin. The N-terminal ubiquitin-like (Ubl) domain of FUBI has the beta-grasp Ubl fold, and it may act as a substitute or an inhibitor of ubiquitin or one of ubiquitin's close relatives UCRP, FAT10, and Nedd8
MQLFVRAQSLHTLEVSGNETVADIKAHIAALEGIAVEDQVLLYAGAPLEDDVVLGQCGIPDLATLEVAVR
LLGG
>gnl|CDD|340492 cd01794, Ubl_UBTD, ubiquitin-like (Ubl) domain found in ubiquitin domain-containing proteins UBTD1, UBTD2, and similar proteins. This family represents a group of ubiquitin-like (Ubl) domain-containing proteins evolutionarily conserved and found in metazoa, fungi, and plants. They may regulate the activity and/or specificity of E2 ubiquitin conjugating enzymes belonging to the UBE2D family. Members in this family contain an N-terminal ubiquitin binding domain (UBD) and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions
LKLRLSTGKDLKLSVRSTDTVLQAKRRLQALEGIEPSRQRWFFSGKLLTDKTRIEDAKIPKGFVVQVIV
>gnl|CDD|340493 cd01795, Ubl_USP48, ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins. USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses
RRVRGERKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEP
PDDPDDADEADVSRARVPEEGFKGTALLG
>gnl|CDD|340494 cd01796, Ubl_Ddi1_like, ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family. The eukaryotic Ddi1 family, including yeast aspartyl protease DNA-damage inducible 1 (Ddi1) and Ddi1-like proteins from vertebrates and other eukaryotes, has been characterized by containing an N-terminal ubiquitin-like (Ubl) domain and a conserved retroviral aspartyl-protease-like domain (RVP) that is important in cell-cycle control. Yeast Ddi1 and many family members also contain a C-terminal ubiquitin-association (UBA) domain, however, Ddi1-like proteins from all vertebrates lack the UBA domain. Ddi1, also termed v-SNARE-master 1 (Vsm1), is an ubiquitin receptor involved in the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as an UBA-Ubl shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also termed transporter regulator RS1 (RS1), which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1. Ddi1-like proteins play a significant role in cell cycle control, growth control, and trafficking in yeast and may play a crucial role in embryogenesis in higher eukaryotes
MKLTVTTEDDDRLFSLEVSPDMTLEDLKALCEAETGIPAAEQVLLHNGQPLTDDKKTLEALGLKDGDLLL
LRP
>gnl|CDD|340495 cd01797, Ubl_UHRF, ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing proteins, UHRF1 and UHRF2, and similar proteins. UHRF1 is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma, gastric cancer, esophageal squamous cell carcinoma, colorectal cancer, prostate cancer, and breast cancer. UHRF1 can acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF2 was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) through interacting with HBV core protein and promoting its degradation. Both UHRF1 and UHRF2 contain an N-terminal ubiquitin-like domain (Ubl), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a set- and ring-associated (SRA) domain, and a C-terminal RING finger
MWIQVRTMDGKKEARVDGLSKLTKIEDLRERIEEKFDVEPELQRLFYRGKQLEDGHTLFDYDVGLNDIIQ
LMVR
>gnl|CDD|340496 cd01798, Ubl_parkin, ubiquitin-like (Ubl) domain found in parkin and similar proteins. Parkin, also termed Parkinson juvenile disease protein 2, is a RBR-type E3 ubiquitin-protein ligase that is associated with recessive early onset Parkinson's disease (PD), and exerts a protective effect against dopamine-induced alpha-synuclein-dependent cell toxicity. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Parkin functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPT5, TOMM20, USP30, ZNF746 and AIMP2. It mediates monoubiquitination as well as Lys-6-, Lys-11-, Lys-48- and Lys-63-linked polyubiquitination of substrates depending on the context. Parkin may enhance cell viability and protects dopaminergic neurons from oxidative stress-mediated death by regulating mitochondrial function. It also limits the production of reactive oxygen species (ROS), and regulates cyclin-E during neuronal apoptosis. Moreover, parkin displays a ubiquitin ligase-independent function in transcriptional repression of p53. Parkin contains an N-terminal ubiquitin-like (Ubl) domain and a C-terminal RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain use an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction
VFVRFNSSHGFPVEVDSDWSILQLKEVVAKRQGVPPDQLRIIFAGKELSDDLTLQNCDLGQQSIVHAVQG
PKRK
>gnl|CDD|340497 cd01799, Ubl_HOIL1, ubiquitin-like (Ubl) domain found in heme-oxidized IRP2 ubiquitin ligase 1 (HOIL-1) and similar proteins. HOIL-1, also termed RBCK1, or HOIL-1L, or RanBP-type and C3HC4-type zinc finger-containing protein 1, HBV-associated factor 4, or Hepatitis B virus X-associated protein 4, or RING finger protein 54 (RNF54), or ubiquitin-conjugating enzyme 7-interacting protein 3, or UbcM4-interacting protein 28 (UIP28), together with E3 ubiquitin-protein ligase RNF31 (also known as HOIP) and SHANK-associated RH domain interacting protein (SHARPIN), forms the E3-ligase complex (also known as linear-ubiquitin-chain assembly complex LUBAC) that regulates NF-kappaB activity and apoptosis through conjugation of linear polyubiquitin chains to NF-kappaB essential modulator (also known as NEMO or IKBKG). HOIL-1 plays a crucial role in TNF-alpha-mediated NF-kappaB activation. It also functions as an ubiquitin-protein ligase E3 that interacts with not only PKCbeta but also PKCzeta. It can recognize heme-oxidized IRP2 (iron regulatory protein2) and is thought to affect the turnover of oxidatively damaged proteins. HOIL-1 contains an N-terminal ubiqutin-like (UBL) domain and an Npl4 zinc-finger (NZF) domain, which regulate the interaction with the LUBAC subunit RNF31 and ubiquitin, respectively. The NZF domain belongs to RanBP2-type zinc finger (zf-RanBP2) domain superfamily. In addition, HOIL-1 has a RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain use an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction
TEISIKVYVEDKSSSSGPITLKVRPHTTIASLKRQIFLEYGFPPSVQRWIIGKRLATDDETLLSYGIKDS
GDPAFLYLVSA
>gnl|CDD|340498 cd01800, Ubl_SF3a120, ubiquitin-like (Ubl) domain found in splicing factor 3A 120kDa subunit (SF3a120) and similar proteins. Mammalian splicing factor SF3a consists of three subunits of 60, 66, and 120 kDa and functions early during pre-mRNA splicing by converting the U2 snRNP to its active form. The 120kDa subunit SF3a120, also termed splicing factor 3A subunit 1 (SF3A1), or spliceosome-associated protein 114 (SAP114), is the U2 snRNP-specific protein that is critical for spliceosome assembly and normal splicing events. During splicing, SF3a120, together with the U2 snRNP and other proteins, are recruited to the 3' splicing site to generate the splicing complex A after the recognition of the 3' splicing site. SF3a120 contains two N-terminal SWAP (suppressor-of-white-apricot) domains, referred to collectively as the SURP module, as well as a C-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions
PVTLKVQVPNVPDKPEWKLNGQVLELTLPLTDTISVLKEKIHEELGMPANKQKLQVEGGGFLKDSNSLAF
YNLGSGTVLTLSLK
>gnl|CDD|340499 cd01801, Ubl_TECR_like, ubiquitin-like (Ubl) domain found in trans-2,3-enoyl-CoA reductase (TECR) and similar proteins. This family includes TECR and many TECR-like proteins, such as TECRL. TECR, also termed very-long-chain enoyl-CoA reductase, or synaptic glycoprotein SC2, or TER, or GPSN2, is a synaptic glycoprotein that catalyzes the fourth reaction in the synthesis of very long-chain fatty acids (VLCFA) which is the reduction step of the microsomal fatty acyl-elongation process. Diseases involving perturbations to normal synthesis and degradation of VLCFA (e.g. adrenoleukodystrophy and Zellweger syndrome) have significant neurological consequences. The mammalian TECR P182L mutation causes nonsyndromic mental retardation. Deletion of the yeast TECR (TSC13) homolog is lethal. TECR contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions, as well as a C-terminal catalytic domain. TECRL, also termed steroid 5-alpha-reductase 2-like 2 protein (SRD5A2L2), is associated with life-threatening inherited arrhythmias displaying features of both long QT syndrome (LQTS) and catecholaminergic polymorphic ventricular tachycardia (CPVT). Both TECR and TECRL contain an N-terminal Ubl domain with a beta-grasp Ubl fold, and a C-terminal catalytic domain
KIEVVSRKGGKQIITLEVSSSATVADLKKAIHKKKKKLYPERQRLRLEVPKGKVLKDDKTLSSYGVKDGS
TLYFKDL
>gnl|CDD|340500 cd01802, Ubl_ZFAND4, ubiquitin-like (Ubl) domain found in AN1-type zinc finger protein 4 (ZFAND4) and similar proteins. ZFAND4, also termed AN1-type zinc finger and ubiquitin domain-containing protein-like 1 (ANUBL1), may function as an oncogene that promotes proliferation and regulates relevant tumor suppressor genes in gastric cancer, suggesting a role in gastric cancer initiation and progression. ZFAND4contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions, as well as a C-terminal AN1-type zinc finger. Unlike ubiquitin polyproteins and most ubiquitin fusion proteins, the N-terminal Ubl domain of ZFAND4 does not undergo proteolytic processing
MELFIETLTGTAFELRVSPFETVASVKAKIQRLEGIPVSQQHLIWSGRELEDDYCLHDYNITDGSTLKLV
LAMR
>gnl|CDD|340501 cd01803, Ubl_ubiquitin, ubiquitin-like (Ubl) domain found in ubiquitin. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like (Ubl) proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ubiquitin (Ub)and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Ub includes Ubq/RPL40e and Ubq/RPS27a fusions as well as homopolymeric multiubiquitin protein chains
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLV
LRLRGG
>gnl|CDD|340502 cd01804, Ubl_midnolin, ubiquitin-like (Ubl) domain found in midnolin and similar proteins. Midnolin, also termed midbrain nucleolar protein, is a nucleolar protein that may be involved in regulation of genes related to neurogenesis in the nucleolus. It is strongly expressed at the mesencephalon (midbrain) of the embryo in day 12.5 (E12.5) mice and its expression is developmentally regulated. Midnolin plays a role in cellular signaling of adult tissues and regulates glucokinase enzyme activity in pancreatic beta cells. It can also control development via regulation of mRNA transport in cells. Midnolin contains an N-terminal conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions
INLYIHPTTGGRFELSVPPNETVEGLKRRISKKLKVPKERITLLHKEKQLKDGTLRENGIGDGSKLTLLP
>gnl|CDD|340503 cd01805, Ubl_Rad23, ubiquitin-like (Ubl) domain found in the Rad23 protein family. The Rad23 family includes the yeast nucleotide excision repair (NER) proteins, Rad23p (in Saccharomyces cerevisiae) and Rhp23p (in Schizosaccharomyces pombe), their mammalian orthologs HR23A and HR23B, and putative DNA repair proteins from plants. Rad23 proteins play dual roles in DNA repair as well as in proteosomal degradation. They have affinity for both the proteasome and ubiquitinylated proteins and participate in translocating polyubiquitinated proteins to the proteasome. Rad23 proteins carry an ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. The Ubl domain is responsible for the binding to proteasome. The UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates, which suggests Rad23 proteins might be involved in certain pathways of Ub metabolism. Both the Ubl domain and the XPC-binding domain are necessary for efficient NER function of Rad23 proteins
MKITFKTLQQQTFEIEVEPSDTVLELKEKIEQEQGDFPASGQKLIYSGKVLKDDKTLSEYNIKEKDFVVV
MV
>gnl|CDD|340504 cd01806, Ubl_NEDD8, ubiquitin-like (Ubl) domain found in neural precursor cell expressed developmentally down-regulated protein 8 (NEDD8) and similar proteins. NEDD8, also termed Neddylin, or RELATED TO UBIQUITIN (RUB/Rub1p) in plant and yeast, is a ubiquitin-like protein that conjugates to nuclear proteins in a manner analogous to ubiquitination and sentrinization. It modifies a family of molecular scaffold proteins called cullins that are responsible for assembling the ROC1/Rbx1 RING-based E3 ubiquitin ligases, of which several play a direct role in tumorigenesis. NEDD8 deamidation and its inhibition of Cullin-RING ubiquitin ligases (CRLs) activity are responsible for Cycle-inhibiting factor (Cif)/Cif homolog in Burkholderia pseudomallei (CHBP)-induced cytopathic effect. NEDD8 contains a single conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Polyubiquitination, signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. Ubl NEDD8, contains many of the same lysines (K6, K11, K27, K33, K48) as Ub, where K27 has an role (other than conjugation) in the mechanism of protein neddylation
IKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIFSGKQMNDEKTAADYKIEGGSVLHLVLA
LRGG
>gnl|CDD|340505 cd01807, Ubl_UBL4A_like, ubiquitin-like (Ubl) domain found in ubiquitin-like proteins UBL4A and similar proteins. UBL4A, also termed GdX, is a ubiquitously expressed ubiquitin-like (Ubl) protein that forms a complex with partner proteins and participates in the protein processing through endoplasmic reticulum (ER), acting as a chaperone. As a key component of the BCL2-associated athanogene 6 (BAG6) chaperone complex, UBL4A plays a role in mediating DNA damage signaling and cell death. UBL4A also regulates insulin-induced Akt plasma membrane translocation through promotion of Arp2/3-dependent actin branching. Moreover, UBL4A specifically stabilizes the TC45/STAT3 association and promotes dephosphorylation of STAT3 to repress tumorigenesis. UBL4B is testis-specific, and encoded by an X-derived retrogene Ubl4b, which is specifically expressed in post-meiotic germ cells in mammals. As a germ cell-specific cytoplasmic protein, UBL4B is not present in somatic cells. Moreover, UBL4B is present in elongated spermatids, but not in spermatocytes and round spermatids, suggesting its function is restricted to late spermiogenesis. The function of UBL4A may be compensated by either UBL4B or other Ubl proteins in normal conditions. Both UBL4A and UBL4B contain a conserved Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions
MLITVKILQGKECTIEVSPTESVLTVKQLVAEQLNVPVSQQRLVFKGKTLADEHSLSDYSIGPGSKIHLV
VK
>gnl|CDD|340506 cd01808, Ubl_PLICs, ubiquitin-like (Ubl) domain found in eukaryotic protein linking integrin-associated protein (IAP, also known as CD47) with cytoskeleton (PLIC) proteins. The PLIC proteins (or ubiquilins) family contains human homologs of the yeast ubiquitin-like (Ubl) Dsk2 protein, PLIC-1 (also termed ubiquilin-1), PLIC-2 (also termed ubiquilin-2, or Chap1), PLIC-3 (also termed ubiquilin-3) and PLIC-4 (also termed ubiquilin-4, ataxin-1 interacting ubiquitin-like protein, A1Up, connexin43-interacting protein of 75 kDa, or CIP75), and mouse PLIC proteins. They are ubiquitin (Ub)-binding adaptor proteins involved in all protein degradation pathways through delivering ubiquitinated substrates to proteasomes. They also promote autophagy-dependent cell survival during nutrient starvation. PLIC-1 regulates the function of the thrombospondin receptor CD47 and G protein signaling. It plays a role in TLR4-mediated signaling through interacting with the Toll/interleukin-1 receptor (TIR) domain of TLR4. It also inhibits the TLR3-Trif antiviral pathway by reducing the abundance of Trif. Moreover, PLIC-1 binds to gamma-aminobutyric acid receptors (GABAARs) and modulates the Ub-dependent, proteasomal degradation of GABAARs. Furthermore, PLIC-1 acts as a molecular chaperone regulating amyloid precursor protein (APP) biosynthesis, trafficking, and degradation by stimulating K63-linked polyubiquitination of lysine 688 in the APP intracellular domain. In addition, PLIC-1 is involved in the protein aggregation-stress pathway via associating with the Ub-interacting motif (UIM) proteins ataxin 3, HSJ1a, and epidermal growth factor substrate 15 (EPS15). PLIC-2 is a protein that binds the ATPase domain of the HSP70-like Stch protein. It functions as a negative regulator of G protein-coupled receptor (GPCR) endocytosis. It also involved in amyotrophic lateral sclerosis (ALS)-related dementia. PLIC-3 is encoded by UbiquilinN3, a testis-specific gene. It shows high sequence similarity with the Xenopus protein XDRP1, a nuclear phosphoprotein that binds to the N-terminus of cyclin A and inhibits Ca2+-induced degradation of cyclin A, but not cyclin B. PLIC-4 is an ubiquitin-like (Ubl) nuclear protein that interacts with ataxin-1 and further links ataxin-1 with the chaperone and Ub-proteasome pathways. It also binds to the non-ubiquitinated gap junction protein connexin43 (Cx43) and regulates the turnover of Cx43 through the proteasomal pathway. PLIC proteins contain an N-terminal Ubl domain that is responsible for the binding of Ub-interacting motifs (UIMs) expressed by proteasomes and endocytic adaptors, and C-terminal Ub-associated (UBA) domain that interacts with Ub chains present on proteins destined for proteasomal degradation. In addition, mammalian PLIC2 proteins have an extra collagen-like motif region, which is absent in other PLIC proteins and the yeast Dsk2 protein
SIIKVTVKTPKEKEDFEVPEDSSVKEFKEEISKKFKAPVEQLVLIFAGKILKDQDTLSQHGIKDGLTVHL
VIK
>gnl|CDD|340507 cd01809, Ubl_BAG6, ubiquitin-like (Ubl) domain found in BCL2-associated athanogene 6 (BAG6) and similar proteins. BAG6, also termed large proline-rich protein BAG6, or BAG family molecular chaperone regulator 6, or HLA-B-associated transcript 3 (Bat3), or protein Scythe, or protein G3, is a nucleo-cytoplasmic shuttling chaperone protein that is highly conserved in eukaryotes. It functions in two distinct biological pathways, ubiquitin-mediated protein degradation of defective polypeptides and tail-anchored transmembrane protein biogenesis in mammals. BAG6 is a component of the heterotrimeric BAG6 sortase complex composed of BAG6, transmembrane recognition complex 35 (TRC35) and ubiquitin-like protein 4A (UBL4A). The BAG6 complex together with the cochaperone small, glutamine-rich, tetratricopeptide repeat-containing, protein alpha (SGTA) plays a role in the biogenesis of tail-anchored membrane proteins and subsequently shown to regulate the ubiquitination and proteasomal degradation of mislocalized proteins. Moreover, BAG6 acts as an apoptotic regulator that binds reaper, a potent apoptotic inducer. BAG6/reaper is thought to signal apoptosis, in part through regulating the folding and activity of apoptotic signaling molecules. It is also likely a key regulator of the molecular chaperone Heat Shock Protein A2 (HSPA2) stability/function in human germ cells. Furthermore, aspartyl protease-mediated cleavage of BAG6 is necessary for autophagy and fungal resistance in plants. BAG6 contains a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which provides a platform for discriminating substrates with shorter hydrophobicity stretches as a signal for defective proteins
LEVTVKTLDSQNRTFTVPEEITVKEFKEHIASSVNIPAEKQRLIFQGRVLQDDKKLKEYDVDGKVIHLVE
R
>gnl|CDD|340508 cd01810, Ubl2_ISG15, ubiquitin-like (Ubl) domain 2 found in interferon-stimulated gene 15 (ISG15) and similar proteins. ISG15, also termed interferon-induced 15 kDa protein, or interferon-induced 17 kDa protein (IP17), or ubiquitin cross-reactive protein (UCRP), is an antiviral interferon-induced ubiquitin-like protein that upon viral infection it modifies cellular and viral proteins by mechanisms similar to ubiquitination. Although ISG15 has properties similar to those of other ubiquitin-like (Ubl) molecules, it is a unique member of the Ubl superfamily, whose expression and conjugation to target proteins are tightly regulated by specific signaling pathways, indicating it may have specialized functions in the immune system. ISG15 contains two tandem Ubl domains with a beta-grasp Ubl fold. This family corresponds to the second Ubl domain
LSIFVRNEKGQSHTYEVRLTQTVDQLKQKVSGREGVHDDQFWLTFEGRPLEDQLPLGEYGLKPQSTIHMN
LRLR
>gnl|CDD|340509 cd01811, Ubl1_OASL, ubiquitin-like (Ubl) domain 1 found in 2'-5'-oligoadenylate synthase-like protein (OASL) and similar proteins. OASL, also termed 2'-5'-OAS-related protein (2'-5'-OAS-RP), or 59 kDa 2'-5'-oligoadenylate synthase-like protein, or thyroid receptor-interacting protein 14, or TR-interacting protein 14 (TRIP-14), or p59 OASL (p59OASL), is an interferon (IFN)-induced antiviral protein that plays an important role in the IFNs-mediated antiviral signaling pathway. It inhibits respiratory syncytial virus replication and is targeted by the viral nonstructural protein 1 (NS1). It also displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L. Moreover, OASL does not have 2'-5'-OAS activity, but can bind double-stranded RNA (dsRNA) to enhance RIG-I signaling. OASL belongs to the 2'-5' oligoadenylate synthase (OAS) family. While each member of this family has a conserved N-terminal OAS catalytic domain, only OASL has two tandem C-terminal ubiquitin-like (Ubl) repeats, which is required for its antiviral activity. This family corresponds to the first Ubl domain
IQVTVKQLGGKSLTLWVNPYDPIWQLKEEIEKEWCIPIYQQRLSFQEPGGERQVLRNDKTLADYGIFYDT
TILLL
>gnl|CDD|340510 cd01812, Ubl_BAG1, ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and similar proteins. BAG1, also termed Bcl-2-associated athanogene 1, or HAP, is a multifunctional protein involved in a variety of cellular functions such as apoptosis, transcription, and proliferative pathways, as well as in cell signaling and differentiation. It delivers chaperone-recognized unfolded substrates to the proteasome for degradation. BAG1 functions as a co-chaperone for Hsp70/Hsc70 to increase Hsp70 foldase activity. It also suppresses apoptosis and enhances neuronal differentiation. As an anti-apoptotic factor, BAG1 interacts with tau and regulates its proteasomal degradation. It also binds to BCR-ABL with a high affinity, and directly routes immature BCR-ABL for proteasomal degradation. It acts as a potential therapeutic target in Parkinson's disease. It also modulates huntingtin toxicity, aggregation, degradation, and subcellular distribution, suggesting a role in Huntington's disease. There are at least four isoforms of Bag1 protein that are formed by alternative initiation of translation within a common mRNA. BAG1 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal BAG domain
LTVTVIHGSNKHTIELPSQDEDEPTLQDLAEAIEEVTGVPVENQKLIFKGKSLKDPEQPLSALGVKNGSK
IMLIGKK
>gnl|CDD|340511 cd01813, Ubl_UBLCP1, ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) and similar proteins. UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity. It is localized in the nucleus and it contains conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which directly interacts with the proteasome. Knockdown of UBLCP1 in cells promotes 26S proteasome assembly and selectively enhances nuclear proteasome activity. UBLCP1 may also play a role in the regulation of phosphorylation state of RNA polymerase II C-terminal domain, a key event during mRNA metabolism
ITLIVKWSGKEYPVTVLSSDTVLDLKQRIFELTGVLPKRQKLLGLKVKGKPADDDVKLSSLKLKPNTKIM
MMGT
>gnl|CDD|340512 cd01814, Ubl_MUBs_plant, ubiquitin-like (Ubl) domain found in plant membrane-anchored ubiquitin-fold proteins (MUBs). The plant MUBs belong to a family of ubiquitin-fold proteins that are plasma membrane-anchored by prenylation. They may serve as docking site to facilitate the association of specific E2s to the plasma membrane. MUBs contain a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold
LIEIKFRLTDGSDIGPFRYSSATTVATLKEKVIAEWPKDKENGPKSINDVKLIYAGKVLENGKTLADSRT
PGKVPPGGVITMHVVVRPP
>gnl|CDD|340513 cd01815, Ubl_UBL7, ubiquitin-like (Ubl) domain found in ubiquitin-like protein 7 (UBL7) and similar proteins. UBL7, also termed bone marrow stromal cell ubiquitin-like (Ubl)protein (BMSC-UbP), or ubiquitin-like protein SB132, is a novel Ubl protein that may play roles in regulation of bone marrow stromal cell (BMSC) function or cell differentiation via an evocator-associated and cell-specific pattern. UBL7 contains an N-terminal Ubl domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-associated (UBA) domain. The Ubl domain interacts with 26S proteasome-dependent degradation, and the UBA domain links cellular processes and the ubiquitin system
HIAVKLADQPLAPKSILQLPETEPGDYPLGGYSISALKQLIAGKLPESLPDPELIDLIYCGRKLKDDQTL
DFYGIQSGSTIHVLRKSWPEPD
>gnl|CDD|340514 cd01816, RBD_RAF, Ras-binding domain (RBD) found in RAF family serine/threonine kinases. The RAF family includes three RAF serine/threonine kinases ARAF, BRAF, and RAF1/CRAF. These are encoded by proto-oncogenes, and activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions
SVIRAHLPNQQRTTVEVKPGQTLREALEKAMKRRGLTPEMCVVYRKGTREPVSWDTDISTLEGEEISVEI
L
>gnl|CDD|340515 cd01817, RBD1_RGS12_like, Ras-binding domain (RBD) 1 of regulator of G protein signaling 12 (RGS12) and similar proteins. Regulator of G protein signaling (RGS) proteins belong to a large family of GTpase-accelerating proteins (GAPs) which act as key inhibitors of G-protein-mediated cell responses in eukaryotes. This RGS12-like subfamily is composed of RGS12 and RGS14, with multidomain architectures including a RGS domain, two tandem Ras-binding domains (RBDs), and a second Galpha interacting domain, the GoLoco motif. The RBD is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair
KLCRVILPDGSTTVVQAKPGETIRQLLTRLLEKRGLSYAAFDVFIVGSDKPLDLNEDSSILGGKEVRVEQ
>gnl|CDD|132836 cd01819, Patatin_and_cPLA2, Patatins and Phospholipases. Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms
LSFSGGGFRGMYHAGVLSALAERGLLDCVTYLAGTSGGAWVAATLYPPSSSLDNKPRQSLEEALSGKLWV
SFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPAELYTSKSNLKEKGVRLVDGGVSNNLPAP
VLLRPGRGVTLTISP
>gnl|CDD|238858 cd01820, PAF_acetylesterase_like, PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor (PAF) and PAF-AH are key players in inflammation and in atherosclerosis. PAF-AH is a calcium independent phospholipase A2 which exhibits strong substrate specificity towards PAF, hydrolyzing an acetyl ester at the sn-2 position. PAF-AH also degrades a family of oxidized PAF-like phospholipids with short sn-2 residues. In addition, PAF and PAF-AH are associated with neural migration and mammalian reproduction
PAAAPTPVDDLDGDPRWMSRHERFVAEAKQKEPDVVFIGDSITQNWEFTGLEVWRELYAPLHALNFGIGG
DRTQNVLWRLENGELDGVNPKVVVLLIGTNNIGHTTTAEEIAEGILAIVEEIREKLPNAKILLLGLLPRG
QNPNPLRERNAQVNRLLAVRYDGLPNVTFLDIDKGFVQSDGTISHHDMPDYLHLTAAGYRKWADALHPTL
ARLL
>gnl|CDD|238859 cd01821, Rhamnogalacturan_acetylesterase_like, Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria
PTIFLAGDSTVADYDPGAPQAGWGQALPQYLDTGITVVNHAKGGRSSRSFRDEGRWDAILKLIKPGDYVL
IQFGHNDQKPKDPEYTEPYTTYKEYLRRYIAEARAKGATPILVTPVTRRTFDEGGKVEDTLGDYPAAMRE
LAAEEGVPLIDLNAASRALYEAIGPEKSKKYFPEGPGDNTHFSEKGADVVARLVAEEL
>gnl|CDD|238860 cd01822, Lysophospholipase_L1_like, Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity
VTILALGDSLTAGYGLPPEEGWPALLQKRLDARGIDVTVINAGVSGDTTAGGLARLPALLAQHKPDLVIL
ELGGNDGLRGIPPDQTRANLRQMIETAQARGAPVLLVGMQAPPNYGPRYTRRFAAIYPELAEEYGVPLVP
FFLEGVAGDPELMQSDGIHPNAEGQPIIAENVWPALE
>gnl|CDD|238861 cd01823, SEST_like, SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST), a causal agent of the potato scab disease, which hydrolyzes a specific ester bond in suberin, a plant lipid. The tertiary fold of this enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxylic acid
VRYVALGDSYAAGPGAGPLDDGPDDGCRRSSNSYPTLLARALGDETLSFTDVACSGATTTDGIEPQQGGI
APQAGALDPDTDLVTITIGGNDLGFADVVKACILTGGGSSLAQEKGAADGARDAALDEVGARLKAVLDRI
RERAPNARVVVVGYPRLFPPDGGDCDKSCSPGTPLTPADRPELNQLVDKLNALIRRAAADAGDYKVRFVD
TDAPFAGHRACSPDPWSRSVLDLLPTRQGKPFHPNAAGHRAIADLIVDA
>gnl|CDD|238862 cd01824, Phospholipase_B_like, Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases
SVHRLRPGDIKVIAALGDSLTAGNGAGSANNLDLLTEYRGLSWSIGGDSTLRGLTTLPNILREFNPSLYG
YSVGTGDETLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVDFKNDWKLITIFIGGNDLCSLCEDAN
PGSPQTFVKNLRKALDILRDEVPRAFVNLVGLLNVASLRSLTKKPLQCETLLAPECPCLLGPTENSYQDL
KKFYKEYQNEVEEIVESGEFDREDFAVVVQPFFEDTSLPPLPDGPDLSFFSPDCFHFSQRGHAIAANALW
NNLLEPVG
>gnl|CDD|238863 cd01825, SGNH_hydrolase_peri1, SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
RIAQLGDSHIAGDFFTDVLRGLLGVIYDNLGVNGASASLLLKWDAEFLQAQLAALPPDLVILSYGTNEAF
NKQLNASEYRQQLREFIKRLRQILPNASILLVGPPDSLQKTGAGRWRTPPGLDAVIAAQRRVAKEEGIAF
WDLYAAMGGEGGIWQWAEPGLARKDYVHLTPRGYERLANLLYEALLKAY
>gnl|CDD|238864 cd01826, acyloxyacyl_hydrolase_like, Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a leukocyte-secreted enzyme that deacetylates bacterial lipopolysaccharides
YEELLCGNSQPMGVILLGDSAGAHFHIPPEWLTVLLLSSEGFANIITIIANEFDWPMLSGATGFANSTRY
IIGGFTDSLYLRLRERNRCNHRDYQNLGVNGASSRNLLSIIKSIARNRTTDKPALVIYSMIGNDVCNGPN
DTINHTTPEEFYENVMEALKYLDTKLPNGSHVILVGLVDGRILYDTLHNRLHPIGQLNKDVTYPNLYDYL
NCLQVSPCWGWLNSNETLRNLTSERAAQLSNVLKRIAANETFNNFDVHYIDFPIQQIVDMWIAFGGQTWQ
LIEPVDGFHPSQIANALLAEVFWKK
>gnl|CDD|238865 cd01827, sialate_O-acetylesterase_like1, sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
IKVACVGNSITEGAGLRAYDSYPSPLAQMLGDGYEVGNFGKSARTVLNKGDHPYMNEERYKNALAFNPNI
VIIKLGTNDAKPQNWKYKDDFKKDYETMIDSFQALPSKPKIYICYPIPAYYGDGGFINDNIIKKEIQPMI
DKIAKKLNLKLIDLHTPLKGKPELVPDWVHPNEKGAYILAKVVYKAIT
>gnl|CDD|238866 cd01828, sialate_O-acetylesterase_like2, sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
ALVFLGDSLTEGGPWALLFPDVKVANRGISGDTTRGLLARLDEDVALQPKAIFIMIGINDLAQGTSDEDI
VANYRTILEKLRKHFPNIKIVVQSILPVGELKSIPNEQIEELNRQLAQLAQQEGVTFLDLWAVFTNADGD
LKNEFTTDGLHLNAKGYAVWAAALQPYLA
>gnl|CDD|238867 cd01829, SGNH_hydrolase_peri2, SGNH_peri2; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
RVLVIGDSLAQGLAPGLLRALADNPGIRVINRSKGSSGLVRPDFFDWPEKLKELIAEEKPDVVVVFLGAN
DRQDIRDGDGYLKFGSPEWEEEYRQRIDELLNVARAKGVPVIWVGLPAMRSPKLSADMVYLNSLYREEVA
KAGGEFVDVWDGFVDENGRFTYSGTDVNGKKVRLRTNDGIHFTAAGGRKLAFYVEKLIRR
>gnl|CDD|238868 cd01830, XynE_like, SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen anaerobe Prevotella bryantii XynE. The P. bryantii XynE gene is located in a xylanase gene cluster. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
SVVALGDSITDGRGSTPDANNRWPDLLAARLAARAGTRGIAVLNAGIGGNRLLADGLGPSALARFDRDVL
SQPGVRTVIILEGVNDIGASGTDFAAAPVTAEELIAGYRQLIRRAHARGIKVIGATITPFEGSGYYTPAR
EATRQAVNEWIRTSGAFDAVVDFDAALRDPADPSRLRPAYDSGDHLHPNDAGYQAMADAVDLDL
>gnl|CDD|238869 cd01831, Endoglucanase_E_like, Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
KIEFIGDSITCGYGVTGKSRCDFSAATEDPSLSYAALLARALNAEYSIIAYSGIGPDLVVINLGTNDFST
GNNPPGEDFTNAYVEFIEELRKRYPDAPIVLMLGPMLFGPYGTEEEIKRVAEAFKDQKSKKVHYFDTPGI
LQHNDIGCDWHPTVAGHQKIAKHLLPAIK
>gnl|CDD|238870 cd01832, SGNH_hydrolase_like_1, Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility
RYVALGDSITEGVGDPVPDGGYRGWADRLAAALAAADPGIEYANLAVRGRRTAQILAEQLPAALALRPDL
VTLLAGGNDILRPGTDPDTYRADLEEAVRRLRAAGARVVVFTIPDPAVLEPFRRRVRARLAAYNAVIRAV
AARYGAVHVDLWEHPEFADPRLWASDRLHPSAAGHARLAALVLAA
>gnl|CDD|238871 cd01833, XynB_like, SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
LRIMPLGDSITWGDKDHEGHSGYLIDQIAAAAADWVLAAKPDVVLLHLGTNDLVLNRDPDTAPDRLRALI
DQMRAANPDVKIIVATLIPTTDASGNARIAEYNAAIPGVVADLRTAGSPVVLVDMSTGYTTADDLYDGLH
PNDQGYKKMADAWYEAL
>gnl|CDD|238872 cd01834, SGNH_hydrolase_like_2, SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
GDRIVFIGNSITDRGGYVGYVETYLAARYPELKLTFRNLGWSGDTVSDLAARRDRDVLPAKPDVVSIMFG
INDSFRGFDDPVGLEKFKTNLRRLIDRLKNKESAPRIVLVSPIAYEANEDPLPDGAEYNANLAAYADAVR
ELAAENGVAFVDLFTPMKEAFQKAGEAVLTVDGVHPNEAGHRALARLWLEA
>gnl|CDD|238873 cd01835, SGNH_hydrolase_like_3, SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
PKRLIVVGDSLVYGWGDPEGGGWVGRLRARWMNLGDDPVLYNLGVRGDGSEDVAARWRAEWSRRGELNVP
NRLVLSVGLNDTARGGRKRPQLSARAFLFGLNQLLEEAKRLVPVLVVGPTPVDEAKMPYSNRRIARLETA
FAEVCLRRDVPFLDTFTPLLNHPQWRRELAATDGIHPNAAGYGWLAWLVLHWG
>gnl|CDD|238874 cd01836, FeeA_FeeB_like, SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of a biosynthetic gene cluster and may participate in the biosynthesis of long-chain N-acyltyrosines by providing saturated and unsaturated fatty acids, which it turn are loaded onto the acyl carrier protein FeeL. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
PPLRLLVLGDSTAAGVGVETQDQALAGQLARGLAAITGRGVRWRLFAKTGATSADLLRQLAPLPETRFDV
AVISIGVNDVTHLTSIARWRKQLAELVDALRAKFPGARVVVTAVPPLGRFPALPQPLRWLLGRRARLLNR
ALERLASEAPRVTLLPATGPLFPALFASDGFHPSAAGYAVWAEALAPAIAA
>gnl|CDD|238875 cd01837, SGNH_plant_lipase_like, SGNH_plant_lipase_like, a plant specific subfamily of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
PALFVFGDSLVDTGNNNYLPTLAKANFPPYGIDFPGRPTGRFSNGRLIIDFIAEALGLPLLPPPYLSPNG
SSDFLTGVNFASGGAGILDSTGFLGSVISLSVQLEYFKEYKERLRALVGEEAAADILSKSLFLISIGSND
YLNNYFANPTRQYEVEAYVPFLVSNISSAIKRLYDLGARKFVVPGLGPLGCLPSQRTLFGGDGGGCLEEL
NELARLFNAKLKKLLAELRRELPGAKFVYADIYNALLDLIQNPAKYGFENTLKACCGTGGPEGGLLCNPC
GSTVCPDPSKYVFWDGVHPTEAANRIIADALLSGP
>gnl|CDD|238876 cd01838, Isoamyl_acetate_hydrolase_like, Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the Saccharomyces cerevisiae IAH1. IAH1 may be the major esterase that hydrolyses isoamyl acetate in sake mash. The SGNH-family of hydrolases is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
KIVLFGDSITQFSFDQGEFGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEEKLAQPDLVTIF
FGANDAALPGQPQHVPLDEYKENLRKIVSHLKSLSPKTKVILITPPPVDEEAWEKSLEDGGSQPGRTNEL
LKQYAEACVEVAEELGVPVIDLWTAMQEEAGWLESLLTDGLHFSSKGYELLFEEIVKVI
>gnl|CDD|238877 cd01839, SGNH_arylesterase_like, SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating enzyme) of A. tumefaciens. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
TILCFGDSNTWGIIPDTGGRYPFEDRWPGVLEKALGANGENVRVIEDGLPGRTTVLDDPFFPGRNGLTYL
PQALESHSPLDLVIIMLGTNDLKSYFNLSAAEIAQGLGALVDIIRTAPIEPGMPAPKILIVAPPPIRTPK
GSLAGKFAGAEEKSKGLADAYRALAEELGCHFFDAGSVGSTSPVDGVHLDADQHAALGQALASVIRAL
>gnl|CDD|238878 cd01840, SGNH_hydrolase_yrhL_like, yrhL-like subfamily of SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. Most members of this sub-family appear to co-occur with N-terminal acyltransferase domains. Might be involved in lipid metabolism
DITAIGDSVMLDSSPALQEIFPNIQIDAKVGRQMSEAPDLIRQLKDSGKLRKTVVIGLGTNGPFTKDQLD
ELLDALGPDRQVYLVNPHVPRPWEPDVNAYLLDAAKKYKNVTIIDWYKAAKGHPDWFYGDGVHPNPAGAK
LYAALIAKAI
>gnl|CDD|238879 cd01841, NnaC_like, NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases. E. coli NnaC appears to be involved in polysaccharide synthesis
KNIVFIGDSLFEGWPLYEAEGKGKTVNNLGIAGISSRQYLEHIEPQLIQKNPSKVFLFLGTNDIGKEVSS
NQFIKWYRDIIEQIREEFPNTKIYLLSVLPVLEEDEIKTRSNTRIQRLNDAIKELAPELGVTFIDLNDVL
VDEFGNLKKEYTTDGLHFNPKGYQKLLEILEEYL
>gnl|CDD|238880 cd01842, SGNH_hydrolase_like_5, SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRLDLVIMNSCLWDLSRYQRNS
MKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGGFLLPELHDLSKSLRYDVLEGNFYSATLAKC
YGFDVLDLHYHFRHAMQHRVRDGVHWNYVAHRRLSNLLLAHVA
>gnl|CDD|238881 cd01844, SGNH_hydrolase_like_6, SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
PWVFYGTSISQGACASRPGMAWTAILARRLGLEVINLGFSGNARLEPEVAELLRDVPADLYIIDCGPNIV
GAEAMVRERLGPLVKGLRETHPDTPILLVSPRYCPDAELTPGRGKLTLAVRRALREAFEKLRADGVPNLY
YLDGEELLGPDGEALVDGIHPTDLGHMRYADRFEPVL
>gnl|CDD|238882 cd01846, fatty_acyltransferase_like, Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. Might catalyze fatty acid transfer between phosphatidylcholine and sterols
RLVVFGDSLSDTGNIFKLTGGSNPPPSPPYFGGRFSNGPVWVEYLAATLGLSGLKQGYNYAVGGATAGAY
NVPPYPPTLPGLSDQVAAFLAAHKLRLPPDTLVAIWIGANDLLNALDLPQNPDTLVTRAVDNLFQALQRL
YAAGARNFLVLNLPDLGLTPAFQAQGDAVAARATALTAAYNAKLAEKLAELKAQHPGVNILLFDTNALFN
DILDNPAAYGFTNVTDPCLDYVYSYSPREACANPDKYLFWDEVHPTTAVHQLIAEEVAAA
>gnl|CDD|238883 cd01847, Triacylglycerol_lipase_like, Triacylglycerol lipase-like subfamily of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. Members of this subfamily might hydrolyze triacylglycerol into diacylglycerol and fatty acid anions
FSRVVVFGDSLSDVGTYNRAGVGAAGGGRFTVNDGSIWSLGVAEGYGLTTGTATPTTPGGTNYAQGGARV
GDTNNGNGAGAVLPSVTTQIANYLAAGGGFDPNALYTVWIGGNDLIAALAALTTATTTQAAAVAAAATAA
ADLASQVKNLLDAGARYILVPNLPDVSYTPEAAGTPAAAAALASALSQTYNQTLQSGLNQLGANNIIYVD
TATLLKEVVANPAAYGFTNTTTPACTSTSAAGSGAATLVTAAAQSTYLFADDVHPTPAGHKLIAQYALSR
L
>gnl|CDD|206746 cd01849, YlqF_related_GTPase, Circularly permuted YlqF-related GTPases. These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases
DVVVEVVDARDPLSSRNPDIEVLINEKNKKLIMVLNKADLVPKEVLRKWVAELSELYGTKTFFISATNGQ
GILKLKAEITKQKLKLKYKKGIRVGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQDVKLDKEIYL
YDTPGI
>gnl|CDD|206649 cd01850, CDC_Septin, CDC/Septin GTPase family. Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities
RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTP
GFGDNINNSDCWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLS
KKVNIIPVIAKADTLTPEELTEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNE
EVEVNGKKVRGRKYPWGVVEVENEEHCDFVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK
>gnl|CDD|206650 cd01851, GBP, Guanylate-binding protein (GBP) family (N-terminal domain). Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach
LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKDTDGKKHAVLLLDTE
GTDGRERGEFENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTALETLGLAGLHNFSKPKPLLL
FVVRDFTGPTPLEGLDVTEKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQNDGRLKDLPPEF
RKALKALRQRFFSS
>gnl|CDD|206651 cd01852, AIG1, AvrRpt2-Induced Gene 1 (AIG1). This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins)
LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLS
KEIIRCLSLSAPGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLED
SCEALKRLLEKCGGRYVAFNNKAKGREQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE
>gnl|CDD|206652 cd01853, Toc34_like, Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like). The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon
REWVGFQFFPDATQTKLHELEAKLKKELDFSLTILVLGKTGVGKSSTINSIFGERKVSVSAFQSETLRPR
EVSRTVDGFKLNIIDTPGLLESQDQRVNRKILSIIKRFLKKKTIDVVLYVDRLDMYRVDNLDVPLLRAIT
DSFGPSIWRNAIVVLTHAQSSPPDGPNGTPFSYDRFVAQRKHIVQQAIQQAAGDPDLENPVVLVENSPRC
KKNRQGEKVLPNGTVWLPQLLLLCTSVKLLSEANILLD
>gnl|CDD|206747 cd01854, YjeQ_EngC, Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases. YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain
ANVDQVLIVFSLKEPFFNLRLLDRYLVAAEASGIEPVIVLNKADLVDDEELEELLEIYEKLGYPVLAVSA
KTGEGLDELRELLKGKTSVLVGQSGVGKSTLLNALLPELVLATGEISEKLGRGRHTTTHRELFPLPGGGL
IIDTPGFRELGLLHIDPEELAEYFPEFEELAGQCRFRDCTHINEPGCAVKAAVEAGEISEERYESYLKLL
E
>gnl|CDD|206748 cd01855, YqeH, Circularly permuted YqeH GTPase. YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases
CQRCFKLKHYNKLLDVEIPDEDFLEILSTLLNDNALVVHVVDIFDFPGSLIPGLAELIGAKPVILVGNKI
DLLPKDVKPNRLKQWVKKRLKIGGLKIKDVILVSAKKGWGVEELIEEIKKLAKYRGDVYVVGATNVGKST
LINALLKSNGGKVQAQALVQRLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI
>gnl|CDD|206749 cd01856, YlqF, Circularly permuted YlqF GTPase. Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga)
WFPGHMAKALRQIKEKLKLVDVVIEVRDARIPLSSRNPDLDKILGNKPRLIVLNKADLADPAKTKKWLKY
FKSQGEPVLFVNAKNGKGVKKLLKKAKKLLKENEKLKAKGLLPRPLRAMVVGIPNVGKSTLINRLRGKKV
AKVGNKPGVTRGQQWIRIGPNIELLDTPGIL
>gnl|CDD|206750 cd01857, HSR1_MMR1, A circularly permuted subfamily of the Ras GTPases. Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus
VWRQLWRVIERSDVVVQIVDARNPLFFRCPDLEKYVKEVDPSKENVLLLNKADLVTEEQRKAWARYFKKE
GIVVLFFSALNEATIGLVGYPNVGKSSLINALVGSKKVSVSSTPGKTKHFQTIFLEPGITLCDCPGLVFP
>gnl|CDD|206751 cd01858, NGP_1, A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases. Autoantigen NGP-1 (Nucleolar G-protein gene 1) has been shown to localize in the nucleolus and nucleolar organizers in all cell types analyzed, which is indicative of a function in ribosomal assembly. NGP-1 and its homologs show a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with NKXD motif) are relocated to the N terminus
ELYKVIDSSDVIIQVLDARDPMGTRCKHVEKYLRKEKPHKHLIFVLNKCDLVPTWVTKRWVKVLSKEYPT
LAFHASITNPFGKGALINLLRQFAKLHSDKKQISVGFIGYPNVGKSSVINTLRSKKVCKVAPIPGETKVW
QYITLMKRIYLIDCPGV
>gnl|CDD|206752 cd01859, MJ1464, An uncharacterized, circularly permuted subfamily of the Ras GTPases. This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus
WKRLVRRIIKEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKADLVPREVLEKWKEVFESEGL
PVVYVSARERLGTRILRRTIKELAIDGKPVIVGVVGYPKVGKSSIINALKGRHSASTSPIPGSPGYTKGI
QLVRIDSKIYLIDTPGV
>gnl|CDD|206653 cd01860, Rab5_related, Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion. The Rab5-related subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
QFKLVLLGDSSVGKSSIVLRFVKNEFSENQESTIGAAFLTQTVNLDDTTVKFEIWDTAGQERYRSLAPMY
YRGAAAAIVVYDITSEESFEKAKSWVKELQEHGPPNIVIALAGNKADLESKRQVSTEEAQEYADENGLLF
METSAKTGENVNELFTEIARKLP
>gnl|CDD|206654 cd01861, Rab6, Rab GTPase family 6 (Rab6). Rab6 is involved in microtubule-dependent transport pathways through the Golgi and from endosomes to the Golgi. Rab6A of mammals is implicated in retrograde transport through the Golgi stack, and is also required for a slow, COPI-independent, retrograde transport pathway from the Golgi to the endoplasmic reticulum (ER). This pathway may allow Golgi residents to be recycled through the ER for scrutiny by ER quality-control systems. Yeast Ypt6p, the homolog of the mammalian Rab6 GTPase, is not essential for cell viability. Ypt6p acts in endosome-to-Golgi, in intra-Golgi retrograde transport, and possibly also in Golgi-to-ER trafficking. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
HKLVFLGDQSVGKTSIITRFMYDTFDNQYQATIGIDFLSKTMYVDDKTVRLQLWDTAGQERFRSLIPSYI
RDSSVAVVVYDITNRQSFDNTDKWIDDVRDERGNDVIIVLVGNKTDLSDKRQVSTEEGEKKAKENNAMFI
ETSAKAGHNVKQLFKKIAQAL
>gnl|CDD|206655 cd01862, Rab7, Rab GTPase family 7 (Rab7). Rab7 subfamily. Rab7 is a small Rab GTPase that regulates vesicular traffic from early to late endosomal stages of the endocytic pathway. The yeast Ypt7 and mammalian Rab7 are both involved in transport to the vacuole/lysosome, whereas Ypt7 is also required for homotypic vacuole fusion. Mammalian Rab7 is an essential participant in the autophagic pathway for sequestration and targeting of cytoplasmic components to the lytic compartment. Mammalian Rab7 is also proposed to function as a tumor suppressor. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
LKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVTVDDRLVTLQIWDTAGQERFQSLGVAFY
RGADCCVLVYDVTNPKSFESLDSWRDEFLIQASPRDPENFPFVVLGNKIDLEEKRQVSTKKAQQWCKSKG
NIPYFETSAKEAINVDQAFETIARLALEQEKE
>gnl|CDD|206656 cd01863, Rab18, Rab GTPase family 18 (Rab18). Rab18 subfamily. Mammalian Rab18 is implicated in endocytic transport and is expressed most highly in polarized epithelial cells. However, trypanosomal Rab, TbRAB18, is upregulated in the BSF (Blood Stream Form) stage and localized predominantly to elements of the Golgi complex. In human and mouse cells, Rab18 has been identified in lipid droplets, organelles that store neutral lipids. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
LKILLIGDSGVGKSSLLLRFTDDTFDEDLSSTIGVDFKVKTVTVDGKKVKLAIWDTAGQERFRTLTSSYY
RGAQGVILVYDVTRRDTFDNLDTWLNELDTYSTNPDAVKMLVGNKIDKENREVTREEGQKFARKHNMLFI
ETSAKTRIGVQQAFEELVEKI
>gnl|CDD|133267 cd01864, Rab19, Rab GTPase family 19 (Rab19). Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. Similarity analysis indicated that Rab41 is closely related to Rab19. However, the function of these Rabs is not yet characterized. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
DFLFKIILIGDSNVGKTCVVQRFKSGTFSERQGNTIGVDFTMKTLEIQGKRVKLQIWDTAGQERFRTITQ
SYYRSANGAIIAYDITRRSSFESVPHWIEEVEKYGASNVVLLLIGNKCDLEEQREVLFEEACTLAEHYGI
LAVLETSAKESSNVEEAFLLMATEL
>gnl|CDD|206657 cd01865, Rab3, Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D. The Rab3 subfamily contains Rab3A, Rab3B, Rab3C, and Rab3D. All four isoforms were found in mouse brain and endocrine tissues, with varying levels of expression. Rab3A, Rab3B, and Rab3C localized to synaptic and secretory vesicles; Rab3D was expressed at high levels only in adipose tissue, exocrine glands, and the endocrine pituitary, where it is localized to cytoplasmic secretory granules. Rab3 appears to control Ca2+-regulated exocytosis. The appropriate GDP/GTP exchange cycle of Rab3A is required for Ca2+-regulated exocytosis to occur, and interaction of the GTP-bound form of Rab3A with effector molecule(s) is widely believed to be essential for this process. Functionally, most studies point toward a role for Rab3 in the secretion of hormones and neurotransmitters. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
MFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVYRNDKRIKLQIWDTAGQERYRTITTAY
YRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVILVGNKCDMEDERVVSAERGRQLADQLGFEF
FEASAKENINVKQVFERLVDIICDK
>gnl|CDD|206658 cd01866, Rab2, Rab GTPase family 2 (Rab2). Rab2 is localized on cis-Golgi membranes and interacts with Golgi matrix proteins. Rab2 is also implicated in the maturation of vesicular tubular clusters (VTCs), which are microtubule-associated intermediates in transport between the ER and Golgi apparatus. In plants, Rab2 regulates vesicle trafficking between the ER and the Golgi bodies and is important to pollen tube growth. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
YAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDGKQIKLQIWDTAGQESFRSIT
RSYYRGAAGALLVYDITRRETFNHLTSWLEDARQHSNSNMTIMLIGNKCDLESRREVSYEEGEAFAREHG
LIFMETSAKTASNVEEAFINTAKEIYDK
>gnl|CDD|206659 cd01867, Rab8_Rab10_Rab13_like, Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13). Rab8/Sec4/Ypt2 are known or suspected to be involved in post-Golgi transport to the plasma membrane. It is likely that these Rabs have functions that are specific to the mammalian lineage and have no orthologs in plants. Rab8 modulates polarized membrane transport through reorganization of actin and microtubules, induces the formation of new surface extensions, and has an important role in directed membrane transport to cell surfaces. The Ypt2 gene of the fission yeast Schizosaccharomyces pombe encodes a member of the Ypt/Rab family of small GTP-binding proteins, related in sequence to Sec4p of Saccharomyces cerevisiae but closer to mammalian Rab8. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
DYLFKLLLIGDSGVGKSCLLLRFSEDSFNPSFISTIGIDFKIRTIELDGKKIKLQIWDTAGQERFRTITT
SYYRGAMGIILVYDITDEKSFENIKNWMRNIDEHASEDVERMLVGNKCDMEEKRVVSKEEGEALAREYGI
KFLETSAKANINVEEAFLTLAKDILKK
>gnl|CDD|206660 cd01868, Rab11_like, Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25. Rab11a, Rab11b, and Rab25 are closely related, evolutionary conserved Rab proteins that are differentially expressed. Rab11a is ubiquitously synthesized, Rab11b is enriched in brain and heart and Rab25 is only found in epithelia. Rab11/25 proteins seem to regulate recycling pathways from endosomes to the plasma membrane and to the trans-Golgi network. Furthermore, Rab11a is thought to function in the histamine-induced fusion of tubulovesicles containing H+, K+ ATPase with the plasma membrane in gastric parietal cells and in insulin-stimulated insertion of GLUT4 in the plasma membrane of cardiomyocytes. Overexpression of Rab25 has recently been observed in ovarian cancer and breast cancer, and has been correlated with worsened outcomes in both diseases. In addition, Rab25 overexpression has also been observed in prostate cancer, transitional cell carcinoma of the bladder, and invasive breast tumor cells. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
DYLFKIVLIGDSGVGKSNLLSRFTRNEFNLDSKSTIGVEFATRTIQIDGKTIKAQIWDTAGQERYRAITS
AYYRGAVGALLVYDITKKSTFENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTEEAKAFAEKNGL
SFIETSALDGTNVEEAFKQLLTEIY
>gnl|CDD|206661 cd01869, Rab1_Ypt1, Rab GTPase family 1 includes the yeast homolog Ypt1. Rab1/Ypt1 subfamily. Rab1 is found in every eukaryote and is a key regulatory component for the transport of vesicles from the ER to the Golgi apparatus. Studies on mutations of Ypt1, the yeast homolog of Rab1, showed that this protein is necessary for the budding of vesicles of the ER as well as for their transport to, and fusion with, the Golgi apparatus. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
YLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTVKLQIWDTAGQERFRTITSS
YYRGAHGIIIVYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNKCDLTDKKVVDYTEAKEFADELGIP
FLETSAKNATNVEEAFMTMAREIKKR
>gnl|CDD|206662 cd01870, RhoA_like, Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC. The RhoA subfamily consists of RhoA, RhoB, and RhoC. RhoA promotes the formation of stress fibers and focal adhesions, regulating cell shape, attachment, and motility. RhoA can bind to multiple effector proteins, thereby triggering different downstream responses. In many cell types, RhoA mediates local assembly of the contractile ring, which is necessary for cytokinesis. RhoA is vital for muscle contraction; in vascular smooth muscle cells, RhoA plays a key role in cell contraction, differentiation, migration, and proliferation. RhoA activities appear to be elaborately regulated in a time- and space-dependent manner to control cytoskeletal changes. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. RhoA and RhoC are observed only in geranylgeranylated forms; however, RhoB can be present in palmitoylated, farnesylated, and geranylgeranylated forms. RhoA and RhoC are highly relevant for tumor progression and invasiveness; however, RhoB has recently been suggested to be a tumor suppressor. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
RKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSY
PDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTIRELAKMKQEPVKPEEG
RAMAEKIGAFGYLECSAKTKEGVREVFEMATRAAL
>gnl|CDD|206663 cd01871, Rac1_like, Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like consists of Rac1, Rac2 and Rac3. The Rac1-like subfamily consists of Rac1, Rac2, and Rac3 proteins, plus the splice variant Rac1b that contains a 19-residue insertion near switch II relative to Rac1. While Rac1 is ubiquitously expressed, Rac2 and Rac3 are largely restricted to hematopoietic and neural tissues respectively. Rac1 stimulates the formation of actin lamellipodia and membrane ruffles. It also plays a role in cell-matrix adhesion and cell anoikis. In intestinal epithelial cells, Rac1 is an important regulator of migration and mediates apoptosis. Rac1 is also essential for RhoA-regulated actin stress fiber and focal adhesion complex formation. In leukocytes, Rac1 and Rac2 have distinct roles in regulating cell morphology, migration, and invasion, but are not essential for macrophage migration or chemotaxis. Rac3 has biochemical properties that are closely related to Rac1, such as effector interaction, nucleotide binding, and hydrolysis; Rac2 has a slower nucleotide association and is more efficiently activated by the RacGEF Tiam1. Both Rac1 and Rac3 have been implicated in the regulation of cell migration and invasion in human metastatic breast cancer. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
AIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSY
PQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQG
LAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAV
>gnl|CDD|133275 cd01873, RhoBTB, RhoBTB protein is an atypical member of the Rho family of small GTPases. Members of the RhoBTB subfamily of Rho GTPases are present in vertebrates, Drosophila, and Dictyostelium. RhoBTB proteins are characterized by a modular organization, consisting of a GTPase domain, a proline rich region, a tandem of two BTB (Broad-Complex, Tramtrack, and Bric a brac) domains, and a C-terminal region of unknown function. RhoBTB proteins may act as docking points for multiple components participating in signal transduction cascades. RhoBTB genes appeared upregulated in some cancer cell lines, suggesting a participation of RhoBTB proteins in the pathogenesis of particular tumors. Note that the Dictyostelium RacA GTPase domain is more closely related to Rac proteins than to RhoBTB proteins, where RacA actually belongs. Thus, the Dictyostelium RacA is not included here. Most Rho proteins contain a lipid modification site at the C-terminus; however, RhoBTB is one of few Rho subfamilies that lack this feature
ETIKCVVVGDNAVGKTRLICARACNKTLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDGVSVSLRL
WDTFGDHDKDRRFAYGRSDVVLLCFSIASPNSLRNVKTMWYPEIRHFCPRVPVILVGCKLDLRYADLDEV
NRARRPLARPIKNADILPPETGRAVAKELGIPYYETSVVTQFGVKDVFDNAIRAA
>gnl|CDD|206664 cd01874, Cdc42, cell division cycle 42 (Cdc42) is a small GTPase of the Rho family. Cdc42 is an essential GTPase that belongs to the Rho family of Ras-like GTPases. These proteins act as molecular switches by responding to exogenous and/or endogenous signals and relaying those signals to activate downstream components of a biological pathway. Cdc42 transduces signals to the actin cytoskeleton to initiate and maintain polarized growth and to mitogen-activated protein morphogenesis. In the budding yeast Saccharomyces cerevisiae, Cdc42 plays an important role in multiple actin-dependent morphogenetic events such as bud emergence, mating-projection formation, and pseudohyphal growth. In mammalian cells, Cdc42 regulates a variety of actin-dependent events and induces the JNK/SAPK protein kinase cascade, which leads to the activation of transcription factors within the nucleus. Cdc42 mediates these processes through interactions with a myriad of downstream effectors, whose number and regulation we are just starting to understand. In addition, Cdc42 has been implicated in a number of human diseases through interactions with its regulators and downstream effectors. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
TIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSY
PQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETG
EKLARDLKAVKYVECSALTQKGLKNVFDEAILAAL
>gnl|CDD|133277 cd01875, RhoG, Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases). RhoG is a GTPase with high sequence similarity to members of the Rac subfamily, including the regions involved in effector recognition and binding. However, RhoG does not bind to known Rac1 and Cdc42 effectors, including proteins containing a Cdc42/Rac interacting binding (CRIB) motif. Instead, RhoG interacts directly with Elmo, an upstream regulator of Rac1, in a GTP-dependent manner and forms a ternary complex with Dock180 to induce activation of Rac1. The RhoG-Elmo-Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. Thus RhoG activates Rac1 through Elmo and Dock180 to control cell morphology. RhoG has also been shown to play a role in caveolar trafficking and has a novel role in signaling the neutrophil respiratory burst stimulated by G protein-coupled receptor (GPCR) agonists. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins
MQSIKCVVVGDGAVGKTCLLICYTTNAFPKEYIPTVFDNYSAQTAVDGRTVSLNLWDTAGQEEYDRLRTL
SYPQTNVFIICFSIASPSSYENVRHKWHPEVCHHCPNVPILLVGTKKDLRNDADTLKKLKEQGQAPITPQ
QGGALAKQIHAVKYLECSALNQDGVKEVFAEAVRAVLNPTPIKDTKSCVLL
>gnl|CDD|206665 cd01876, YihA_EngB, YihA (EngB) GTPase family. The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target
EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGK
LIEEYLENRENLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELN
LFNILPPVILFSSKKGTGIDELRALIAEWL
>gnl|CDD|206666 cd01878, HflX, HflX GTPase family. HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms
ETQLETDRRLIRERIAKLRKELEKVKKQRELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVLAED
QLFATLDPTTRRIKLPGGREVLLTDTVGFIRDLPHQLVEAFRSTLEEVAEADLLLHVVDASDPDREEQIE
TVEEVLKELGADDIPIILVLNKIDLLDDEELEERLRAGRPDAVFISAKTGEGLDLLKEAIEELL
>gnl|CDD|206667 cd01879, FeoB, Ferrous iron transport protein B (FeoB) family. Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent
ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGTYSLTPYSEDEKVARDF
LLGEEPDLIVNVVDATNLERNLYLTLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSA
RKGEGIDELLDAIAKLAES
>gnl|CDD|206668 cd01881, Obg_like, Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1. The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified
GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDGASEGRGLGEQIL
AHLYRSDLILHVIDASEDCVGDPLEDQKTLNEEVSGSFLFLKNKPEMIVANKIDMASENNLKRLKLDKLK
RGIPVVPTSALTRLGLDRVIRTIRKLL
>gnl|CDD|206669 cd01882, BMS1, Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes. Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes
AFAVQSAVRAARQFQRTQDLEEKKLHVPVVDRTPEEPPPLVVVVVGPPGVGKSTLIRSLIKRYTKQNLSD
IKGPITIVTGKKRRLTFIECPNDINSMIDVAKIADLVLLLIDGSYGFEMETFEFLNILQVHGFPKVMGVL
THLDKFKNNKTLRKTKKRLKHRFWTEVYDGAKLFYLSGIVHGRYPKTEILNLARFISVMKFRPLNWRNSH
PYVLADRMEDLTNPEDIRENP
>gnl|CDD|206670 cd01883, EF1_alpha, Elongation Factor 1-alpha (EF1-alpha) protein family. EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression
NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLA
KFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQL
IVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPTLLE
ALDSLEPPE
>gnl|CDD|206671 cd01884, EF_Tu, Elongation Factor Tu (EF-Tu) GTP-binding proteins. EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation
PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHV
DCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELV
EMEVRELLSKYGFDGDDTPIVRGSALKALEGDDPNKWVDKILELLDALDSYIPTP
>gnl|CDD|206672 cd01885, EF2, Elongation Factor 2 (EF2) in archaea and eukarya. Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity
RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITIKSSAISLYFEYEEEKMDGN
DYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRLILE
LKLSPEEAYQRLLRIVEDVNAIIETYAPEEFKQEKWKFSPQKGNVAFGSALDGWGFTIIKFADIYAVLEM
VVKHLPSP
>gnl|CDD|206673 cd01886, EF-G, Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis. Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members
NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGGATMDWMEQERERGITIQSAATTCFWKDHRINIID
TPGHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQI
REKLGANPVPLQLPIGAEDDFEGVVDLIEMKALYWDGELGEKIEETDIPEDLLEEAEEAREELIETLAEV
DDELMEKYLEGEEITEEEIKAAIRKGTIANKIVPVLCGSAFKNKGVQPLLDAVVDYLPSP
>gnl|CDD|206674 cd01887, IF2_eIF5B, Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family. IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s
PVVTVMGHVDHGKTTLLDKIRKTNVAAGEAGGITQHIGAYQVPIDVKIPGITFIDTPGHEAFTNMRARGA
SVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGTEADPERVKNELSELGLVGEEWGG
DVSIVPISAKTGEGIDDLLEAILLLAEVL
>gnl|CDD|206675 cd01888, eIF2_gamma, Gamma subunit of initiation factor 2 (eIF2 gamma). eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors
INIGTIGHVAHGKTTLVKALSGVWTVRHKEELKRNITIKLGYANAKIYKCPNCGCPRPYDTPECECPGCG
GETKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQPQTSEHLAALEIMGLKHIIILQNK
IDLVKEEQALENYEQIKEFVKGTIAENAPIIPISAQLKYNIDVLCEYIVKKIPTPPR
>gnl|CDD|206676 cd01889, SelB_euk, SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome. SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea
VNVGLLGHVDSGKTSLAKALSEIASTAAFDKNPQSQERGITLDLGFSSFEVDKPKHLEDNENPQIENYQI
TLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEEERKR
KIEKMKKRLQKTLEKTRLKDSPIIPVSAKPGEGEAELGGELKNLIVLPLINL
>gnl|CDD|206677 cd01890, LepA, LepA also known as Elongation Factor 4 (EF4). LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype
RNFSIIAHIDHGKSTLADRLLELTGTVSEREMKEQVLDSMDLERERGITIKAQAVRLFYKAKDGEEYLLN
LIDTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVK
QEIEDVLGLDASEAILVSAKTGLGVEDLLEAIVERIPPP
>gnl|CDD|206678 cd01891, TypA_BipA, Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases. BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity
KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTKINII
DTPGHADFGGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDE
VFDLFLELNATDEQLDFPIVYASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP
>gnl|CDD|206679 cd01892, Miro2, Mitochondrial Rho family 2 (Miro2), C-terminal. Miro2 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the putative GTPase domain in the C terminus of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature
QRNVFLCFVLGAKGSGKSALLQAFLGRSFSQNAYSPTIKPRYAVNTVEVPGQEKYLILREVGEDEEAILL
NDAELAACDVACLVYDSSDPNSFSYCAEVYKKYFMLGEIPCLFVAAKADLDEQQQRAEVQPDEFCRKLGL
PPPLHFSSRLGDSSNELFTKLATAAQYPHLSIPELESGKT
>gnl|CDD|206680 cd01893, Miro1, Mitochondrial Rho family 1 (Miro1), N-terminal. Miro1 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the N-terminal GTPase domain of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature
KDVRIVLIGDEGVGKSSLIMSLVSEEFPENVPRVLPEITIPADVTPERVPTTIVDTSSRPQDRANLAAEI
RKANVICLVYSVDRPSTLERIRTKWLPLIRRLGVKVPIILVGNKSDLRDGSSQAGLEEEMLPIMNEFREI
ETCVECSAKTLINVSEVFYYAQKAVLHP
>gnl|CDD|206681 cd01894, EngA1, EngA1 GTPase contains the first domain of EngA. This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability
AIVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEGISKEIREQA
EIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKEEEEAAEFYSLGFGEPIPISA
EHGRGIGDLLDAILELL
>gnl|CDD|206682 cd01895, EngA2, EngA2 GTPase contains the second domain of EngA. This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability
DPIKIAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTRDSIDVPFEYDGQKYTLIDTAGIRKKGKVTEGI
EKYSVLRTLKAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDEKTMKEFEKEL
RRKLPFLDYAPIVFISALTGQGVDKLFDAIKEVY
>gnl|CDD|206683 cd01896, DRG, Developmentally Regulated GTP-binding protein (DRG). The developmentally regulated GTP-binding protein (DRG) subfamily is an uncharacterized member of the Obg family, an evolutionary branch of GTPase superfamily proteins. GTPases act as molecular switches regulating diverse cellular processes. DRG2 and DRG1 comprise the DRG subfamily in eukaryotes. In view of their widespread expression in various tissues and high conservation among distantly related species in eukaryotes and archaea, DRG proteins may regulate fundamental cellular processes. It is proposed that the DRG subfamily proteins play their physiological roles through RNA binding
ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQ
VIAVARTADLILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKT
VKAILREYKIHNADVLIREDITVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLARIPNSVVISAEK
DLNLDELLERIWDYLGLIRIYTK
>gnl|CDD|206684 cd01897, NOG, Nucleolar GTP-binding protein (NOG). NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins
RTLVIAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGILDRPLEERNTIEM
QAITALAHLRAAVLFFIDPSETCGYSIEEQLSLFKEIKPLFNKPVIVVLNKIDLLTEEDLSEIEKELEKE
GEEVIKISTLTEEGVDELKNKACELLL
>gnl|CDD|206685 cd01898, Obg, Obg GTPase. The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain
ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGH
RFLRHIERTRVLLHVIDLSGEDDPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELL
KELKGKKVFPISALTGEGLDELLKKLAKLL
>gnl|CDD|206686 cd01899, Ygr210, Ygr210 GTPase. Ygr210 is a member of Obg-like family and present in archaea and fungi. They are characterized by a distinct glycine-rich motif immediately following the Walker B motif. The Ygr210 and YyaF/YchF subfamilies appear to form one major branch of the Obg-like family. Among eukaryotes, the Ygr210 subfamily is represented only in fungi. These fungal proteins form a tight cluster with their archaeal orthologs, which suggests the possibility of horizontal transfer from archaea to fungi
IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVGYVRVECPCKELGVSCNPRYGKCIDGKRYVP
VELIDVAGLVPGAHEGKGLGNQFLDDLRDADVLIHVVDASGGTDAEGNGVETGGYDPLEDIEFLENEIDM
WIYGILERNWEKIVRKAKAEKTDIVEALSEQLSGFGVNEDVVIEALEELELPADLSKWDDEDLLRLAREL
RKRRKPMVIAANKADIPDAEENISKLRLKYPDEIVVPTSAEAELALRRAAKQGLIKYVPGDSDFEITDED
GLSDKQREALENIRDEVLDRFGSTGVQEALNAAVFDLL
>gnl|CDD|206687 cd01900, YchF, YchF GTPase. YchF is a member of the Obg family, which includes four other subfamilies of GTPases: Obg, DRG, Ygr210, and NOG1. Obg is an essential gene that is involved in DNA replication in C. crescentus and Streptomyces griseus and is associated with the ribosome. Several members of the family, including YchF, possess the TGS domain related to the RNA-binding proteins. Experimental data and genomic analysis suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translational factor
IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVKPKKIVPATIEFVDIA
GLVKGASKGEGLGNKFLSHIREVDAIAHVVRCFEDDDITHVEGSVDPVRDIEIINTELILADLETIEKRL
ERLEKKAKSGDKEAKEELELLEKIKEHLEEGKPARTLELTDEEIKILKSLQLLTAKPVIYVANVSEDDLI
RGNNKVLKVREIAAKEGAEVIPISAKLEAELAELDEEEAAEFLEELGLEESGLDKLIRAGYELL
>gnl|CDD|238884 cd01901, Ntn_hydrolase, The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences
STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRY
GEPISVVALAKELAKLLQVYTQGRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPGAVATGSRSQRAKSL
LEKLYKPDMTLEEAVELALKALKS
>gnl|CDD|238885 cd01902, Ntn_CGH, Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide carbon-nitrogen bonds in choloylglycine and choloyltaurine, both of which are present in bile. CGH is present in a number of probiotic microbial organisms that inhabit the gut. CGH has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which CGH belongs
ACTRILWNTNNQGVITGRSMDWKEDTGPNLWVFPRGMERDGGTGDNSAKWTSKYGSVVASMYDIGTVDGM
NEKGLVANLLYLTESDYGPADPNKPTLSAGAWGQYLLDNYATVEEAVKALAKEPFVIVASVPGDGREATL
HLSISDATGDSAIIEYIDGKLVIHHGKQYQVMTNSPTYDQQLALNKYWKQEKDIGGTTGLPGNNNPADRF
VRASYYISALPKTADEREAVASVLSVIRNVSVPFGIPTPAPPNISDTRWRTVADHKMKRYFFESTLTPNL
FWVDLKKLDFS
>gnl|CDD|238886 cd01903, Ntn_AC_NAAA, AC_NAAA This conserved domain includes two closely related proteins, acid ceramidase (AC, also known as N-acylsphingosine amidohydrolase), and N-acylethanolamine-hydrolyzing acid amidase (NAAA). AC catalyzes the hydrolysis of ceramide to sphingosine and fatty acid. Ceramide is required for the biosynthesis of most sphingolipids and plays an important role in many signal transduction pathways by inducing apoptosis and/or arresting cell growth. An inherited deficiency of AC activity leads to the lysosomal storage disorder known as Farber disease. AC is considered a "rheostat" important for maintaining the proper intracellular levels of these lipids since hydrolysis of ceramide is the only source of sphingosine in cells. NAAA is a eukaryotic glycoprotein that hydrolyzes bioactive N-acylethanolamines, including anandamide (an endocannabinoid) and N-palmitoylethanolamine (an anti-inflammatory and neuroprotective substance), to fatty acids and ethanolamine at acidic pH. NAAA shows structural and functional similarity to acid ceramidase, but lacks the ceramide-hydrolyzing activity of AC
NIFYEIFTFCTSIVAQDSNGTIYHARNLDFGFFEELSKLTVNVDFQRNGKIVFKGTTFAGYVGLLTGQKP
GKFSLTINERFSLDGGYNGILALLKKDGIPVSWLIRETLENATSYEDAVEKLSTTPILAPAYFIVGGVKP
GEGVVITRNRDSVADVYPLDLKNGTWFLVQTNYDRWKPPPFLDDRRTPAIKCMNALGQANISFKTLYDVL
STKPVLNKLTIYTTLMSVRTG
>gnl|CDD|238887 cd01906, proteasome_protease_HslV, proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide
TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRY
GEPIPVEALAKLLANLLYEYTQSLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALG
ILEKLYKPDMTLEEAIELALKALKSALERDLYSGGNIEVAVI
>gnl|CDD|238888 cd01907, GlxB, Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits
CGIFGIMSKDGEPFVGALLVEMLDAMQERGPGDGAGFALYGDPDAFVYSSGKDMEVFKGVGYPEDIARRY
DLEEYKGYHWIAHTRQPTNSAVWWYGAHPFSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIA
YYLDLLLRKGGLPLEYYKHIIRMPEEERELLLALRLTYRLADLDGPFTIIVGTPDGFIVIRDRIKLRPAV
VAETDDYVAIASEECAIREIPDRDNAKVWEPRPGEYVIW
>gnl|CDD|238889 cd01908, YafJ, Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits
MCRLLGYSGAPIPLEPLLIRPSHSLLVQSGGPREMKGTVHADGWGIGWYEGKGGRPFRYRSPLPAWSDIN
LESLARPIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFRLLRRRLLRLLPRLPVGTTDS
ELAFALLLSRLLERDPLDPAELLDAILQTLRELAALAPPGRLNLLLSDGEYLIATRYASAPSLYYLTRRA
PFGCARLLFRSVTTPNDDGVVVASEPLTDDEGWTEVPPGELVVVSEG
>gnl|CDD|238890 cd01909, betaLS_CarA_N, Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam synthetase (CarA) is an ATP/Mg2+-dependent enzyme that catalyzes the formation of the beta-lactam ring in (5R)-carbapenem-3-carboxylic acid biosynthesis. CarA is homologous to beta-lactam synthetase (beta-LS), which is involved in the biosynthesis of clavulanic acid, a clinically important beta-lactamase inhibitor. CarA and beta-LS each have two distinct domains, an N-terminal Ntn hydrolase domain and a C-terminal synthetase domain, a domain architecture similar to that of the class-B asparagine synthetases (AS-B's). The N-terminal domain of these enzymes hydrolyzes glutamine to glutamate and ammonia. CarA forms a homotetramer while betaLS forms a heterodimer. The N-terminal folds of CarA and beta-LS are similar to those of other class II glutamine amidotransferases including lucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), and glutamate synthase (GltS). This fold is also somwhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits
SNGFCVVAGTGGKDINLFAHRGSHTGEALPNGAGTIVHAGSVDVQVARSETGTAYLIGELYNRDELRSLL
GAGEGRSAVLGDAELLLLLLTRLGLHAFRLAEGDFCFFIEDGNGRLTLATDHAGSVPVYLVQAGEVWATT
ELKLLAAHEGPKAFPFKSAGADTVSGLTGVQRVPPGTVNVLTFDGGSYGTAESRRTWTP
>gnl|CDD|238891 cd01910, Wali7, This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced by aluminum. Wali7 has a single domain similar to the glutamine amidotransferase domain of glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The Wali7 domain is also somewhat similar to the Ntn hydrolase fold of the proteasomal alph and beta subunits
LAVFSKAVAKPPEELVSAGSRTPAKTAEELLKRFLSANPSAVFVHLGAAGFLAYSHHNQSPLHPRLFAVK
DDIFCLFQGHLDNLGSLKQQYGLSKTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTST
VFVASDADGSVPLYWGIAADGSVVFSDDVELVKASCGKSFAPFPKGCFFHSEGGLRSFEHPMNKLKAVPR
VDSEGEMCGATFKV
>gnl|CDD|238892 cd01911, proteasome_alpha, proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 different alpha and 10 different beta proteasome subunit genes while archaea have one of each
YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCA
VAGLTADARVLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGP
QLYQTDPSGTYFGYKATAIGKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDKKAKNIEIAVV
>gnl|CDD|238893 cd01912, proteasome_beta, proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRN
GRELSVKAAANLLSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGIL
DRGYKPDMTLEEAVELVKKAIDSAIERDLSSGGGVDVAVITKDGVEELR
>gnl|CDD|238894 cd01913, protease_HslV, Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system that is the prokaryotic homolog of the proteasome. HslV is a dimer of hexamers (a dodecamer) that forms a central proteolytic chamber with active sites on the interior walls of the cavity. HslV shares significant sequence and structural similarity with the proteasomal beta-subunit and both are members of the Ntn-family of hydrolases. HslV has a nucleophilic threonine residue at its N-terminus that is exposed after processing of the propeptide and is directly involved in active site catalysis
TTILAVRKNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNGKVIAGFAGSTADAFTLFERFEAKLEQYPGN
LLRAAVELAKDWRTDRYLRRLEAMLIVADKEHTLLISGNGDVIEPDDGIAAIGSGGNYALAAARALLDHT
DLSAEEIARKALKIAADICIYTNHNITVEEL
>gnl|CDD|238895 cd01914, HCP, Hybrid cluster protein (HCP), formerly known as prismane, is thought to play a role in nitrogen metabolism but its specific function is unknown. HCP has three structural domains, an N-terminal alpha-helical domain, and two similar domains comprising a central beta-sheet flanked by alpha-helices. HCP contains two iron-sulfur clusters, one of which is a [Fe4-S4] cubane cluster similar to that of carbon monoxide dehydrogenase (CODH). The second cluster, referred to as the hybrid cluster, is a hybrid [Fe4-S2-O2] center located at the interface of the three domains. Although the hybrid cluster is buried within the protein, it is accessible through a large hydrophobic cavity
MFCYQCEQTAKGTGCTVRGVCGKDPEVANLQDYGLKGIAAYAEHARVLGYDDEEIYAFIEKALASLLDNP
LDADELLALALETGRMNLKVMELLDKANTETYGHPEPTEVNIGVRAGKGILVSGHDLKDLEELLEQTEGT
GVDVYTHGEMLPAHGYPELKKYPHLVGNYGGAWQNQQKEFARFPGPILMTTNCIIPPRESYKDRIFTTGI
VGWPGVKHIEGKDFSEVIEKAKELPGFPEEEESGTITTGFAHNQVLAVADKVVEAVKSGKIRHFFVVGGC
DGRHKGRNYYTEFAEKLPKDTVILTLGCGKYRFNKLDLGDIGGIPRLLDAGQCNDSYSAIVIALALAEAF
GCDVNDLPLSLVLSWYEQKAVAVLLALLALGVKNIRLGPTLPAFLTPNVLKVLVENFGLKPIGTVEEDLK
AIL
>gnl|CDD|238896 cd01915, CODH, Carbon monoxide dehydrogenase (CODH) is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA, respectively. CODH has two types of metal clusters, a cubane [Fe4-S4] center (B-cluster) similar to that of hybrid cluster protein (HCP) and a Ni-Fe-S center (C-cluster) where carbon monoxide oxidation occurs. Bifunctional CODH forms a heterotetramer with acetyl-CoA synthase (ACS) consisting of two CODH and two ACS subunits while monofunctional CODH forms a homodimer. Bifunctional CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP), while monofunctional CODH oxidizes carbon monoxide to carbon dioxide. CODH and ACS each have a metal cluster referred to as the C- and A-clusters, respectively
DPAVQEMLEKAKKDGIETVWDRFEAQQPQCGFGELGLCCRLCSNGPCRIDPKGPGKRGVCGATADTIVAR
NLLRMVAAGAAAHSHHARHAARTLKAAAEGKTDYEIKDEEKLKALAKRLGIDTEGKSINEIAVEVAEIAL
EDFGRPREEPSRWVEAFAPEKRLELWEELGILPGGIDSEIAEAMHRTHTGVDSDPVSLLLHSLRLGLAAG
YTGLMLATELQDILFGTPKPVVSEANLGVLDPDYVNIAVHGHNPVLSEAIVEAARELELQEEAKAAGAKG
INVVGICCTGNELLMRHGVPLAGNWLSQELAIATGAVDAMVVDVQCIMPSLPQYAECFHTKLITTSDVAK
IPGAEHIDFDPEEADESAKEIIRMAIEAFKRRKKSKVYIPQHKSKAVVGFSTEAILDALGGSLKPLIDAI
ASGNIKGVVGIVGCNNLKVQQDSSHVTLAKELIKRNVLVLATGCGAGALAKAGLMDPEAAELAGDGLKAV
CKALGIPPVLHMGSCVDNSRIVDLATALANELGVDIPDLPLVASAPEWMEEKAVAIGTWAVALGLPTHVG
PVPPVTGSDLVTKLLTEDLEDVTGGKFIVETDPKKAADKLEAHIEEKRKALGL
>gnl|CDD|238897 cd01916, ACS_1, Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA
MGPTPKPGIATLRDWDFKLLERYEPFYAPICDMCCLCTYGKCDLTGNKKGACGIDMAAQQARIVLLACCI
GTAAHAGHARHLVHLIEEKGEDVPIDLGSEVDVEAPIIRTVVGIKPKTLGDLEEALEYAEEQIVQLLSAV
HTGQEGSYLDFESKALHAGMIDSLGKEIADIAQIAAYDMPKGDPDAPLVEIGFGTIDKSKPVILVIGHNV
APGAEIMDYLEENGLEDKVEVGGICCTAIDLTRYNEKAKVVGPLSRQLKVVRSGIADVVVVDEQCIRADI
LEEAQKLGIPVIATNDKIMLGLPDVTDEDPDKIVEDLVSGKIPGVLILDPEKVGEVAVEVAMAVKPKRKG
EKKLPTDEEFQELAAKCTDCGWCTRACPNSLRIKEAMEAAKEGDFSGLADLFDQCVGCGRCEQECPKEIP
IINMIEKAARERIKEEKGKMRAGRGPIKDTEIRKVGAPIVLGDIPGVIALVGCSNYPNGTKDVYKIAEEF
LERNYIVVTTGCMAMDIGMYKDEDGKTLYEKYPGRFDAGGLVNIGSCVSNAHIHGAAIKVAAIFAKRPLR
GNYEEIADYILNRVGACGVAWGAMSQKAASIATGFNRLGIPVVVGPHGSKYRRAYIGRPDKEEDWKVYDA
RTGEEVEIEPAPEHLLYAAETWEEAIVMMAKLCIRPSDTPQGRQIKLTHYIDLHKKYLGTLPPDWHLFVR
TEADLPLAMRDELMKELEEKHGWKIDWKKKK
>gnl|CDD|238898 cd01917, ACS_2, Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA
EVYVGAITATSYAEILLNKAILEYGPDHPVGYPDTAYNLPVIRCLSGEKVETLGDLKPLLNRLRAQVEEV
LTFENARLAGEATLYAAEIIEALRYLKSEPPYKPPWTGFIGDPIVRGLGIKMVDWTIPGEAVILGRAKDS
KALKKIVDDLMGRGFMLFLCDEIVEQLLEENVKLGLDYIAYPLGNFTQAIHAANYALRAGLMFGGIEPGK
REEIRDYQRRRVRAFVLYLGELDMVKTAAAAGAIFTGFPVITDQELPEDKQIPDWFFSSSDYDKIVQNAL
EMRGIKL
>gnl|CDD|238899 cd01918, HprK_C, HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of Ser-46 of HPr and its dephosphorylation by phosphorolysis. The latter reaction uses inorganic phosphate as substrate and produces pyrophosphate. Phosphoenolpyruvate carboxykinase (PEPCK) and the C-terminal catalytic domain of HprK/P are structurally similar with conserved active site residues suggesting these two phosphotransferases have related functions. The HprK/P N-terminal domain is structurally similar to the N-terminal domains of the MurE and MurF amino acid ligases
PTVTVHGVLVEVGGIGVLITGPSGIGKSELALELIKRGHRLVADDRVVVKREGGRLVGRAPEALKGLIEI
RGLGIIDVPRLYGIEAVRDRKVIDLVIELEEWEEEKNFDRLGLEEEYKRILGVKVPLLRLPVSPGRNLAV
LIEVAAANF
>gnl|CDD|238900 cd01919, PEPCK, Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates toward gluconeogenesis. It catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate to yield phosphoenolpyruvate and carbon dioxide, using a nucleotide molecule (ATP or GTP) for the phosphoryl transfer, and has a strict requirement for divalent metal ions for activity. PEPCK's separate into two phylogenetic groups based on their nucleotide substrate specificity (the ATP-, and GTP-dependent groups)
DHIHINDENGRLLQQMLEEYGILRLTKNGALAVTDPRDTGRSPSDKVIVTQDQRRTVPIPKTGLSQLNRW
LSEEDFEKAFNARFPGLMKGRTLFVVDFFMGPGSPLRLIVRELTDSPYVAAFMRIMTIMPTDEELAAFGD
PDVKCLNSVGCPLPLQKWPGLPSLTLVAHNPDRREQIIFGTGYGGEMKKGFLRMMSRLAPEEGWLAMHMS
ANVGTNGDVLVFFGLSGTGKTTLSMDPKRELIGDDEHWWKDDGVFNPEGGCYAKAIGLSVKTEPNIYKAI
RKNAIFENVAETSDGGIDFEDISAHPNTRVCYPASHIPIIDAAWESAGHIEGVIFLTRDAFGVVPPVYRL
TWQQGVFVFAAGRTAATAGTEAGHKGKIPMFSPCFGRPFLGYHFTKYLEHLLSMMQHPLPKIFLVNTGRK
GKEGKFKRPGFGETRAIIDAIFNGILDKAETKLTPIFNLYIPKALNLVGLGHLNPRNMMELFSQSKEFWD
KLVEDFEKYFVDQVNACAIEREILA
>gnl|CDD|238901 cd01920, cyclophilin_EcCYP_like, cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to the cytosolic E. coli cyclophilin A and Streptomyces antibioticus SanCyp18. Compared to the archetypal cyclophilin Human cyclophilin A, these have reduced affinity for cyclosporin A. E. coli cyclophilin A has a similar peptidylprolyl cis- trans isomerase activity to the human cyclophilin A. Most members of this subfamily contain a phenylalanine residue at the position equivalent to Human cyclophilin W121, where a tyrptophan has been shown to be important for cyclophilin binding
EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEA
GNGLSNTRGTIAMARTNAPDSATSQFFINLKDNASLDYQNEQWGYTVFGEVTEGMDVVDKIAGVETYSFG
SYQDVPVQDVIIESA
>gnl|CDD|238902 cd01921, cyclophilin_RRM, cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a C-terminal RNA recognition motif domain (RRM). This subfamily of the cyclophilin domain family contains a number of eukaryotic cyclophilins having the RRM domain including the nuclear proteins: human hCyP-57, Arabidopsis thaliana AtCYP59, Caenorhabditis elegans CeCyP-44 and Paramecium tetrurelia Kin241. The Kin241 protein has been shown to have a role in cell morphogenesis
LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSQLYGR
QARFFEPEILPLLKHSKKGTVSMVNAGDNLNGSQFYITLGENLDYLDGKHTVFGQVVEGFDVLEKINDAI
VDDDGRPLKDIRIKHTHILDDPFPDP
>gnl|CDD|238903 cd01922, cyclophilin_SpCYP2_like, cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to Schizosaccharomyces pombe cyp-2. These proteins bind their respective SNW chromatin binding protein in autologous systems, in a CsA independent manner indicating interaction with a surface outside the PPIase active site. SNW proteins play a basic and broad range role in signaling
TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFED
EIHPELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRPID
EVKILK
>gnl|CDD|238904 cd01923, cyclophilin_RING, cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human cyclophilin A exhibit reduced peptidylprolyl cis- trans isomerase activity and lack a residue important for cyclophilin binding. Human hCyP-60 has been shown to physically interact with the proteinase inhibitor peptide eglin c and; C. elegans MOG-6 to physically interact with MEP-1, a nuclear zinc finger protein. MOG-6 has been shown to function in germline sex determination
YVRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPF
KDEFKPNLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDR
PKEEIKIEDTSVFVDPFEE
>gnl|CDD|238905 cd01924, cyclophilin_TLP40_like, cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) similar ot the Spinach thylakoid lumen protein TLP40. Compared to the archetypal cyclophilin Human cyclophilin A, these proteins have similar peptidylprolyl cis- trans isomerase activity and reduced affinity for cyclosporin A. Spinach TLP40 has been shown to have a dual function as a folding catalyst and regulator of dephosphorylation
GEATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGFPDPETGKSRT
IPLEIKPEGQKQPVYGKTLEEAGRYDEQPVLPFNAFGAIAMARTEFDPNSASSQFFFLLKDNELTPSRNN
VLDGRYAVFGYVTDGLDILRELKVGDKIESARVVEG
>gnl|CDD|238906 cd01925, cyclophilin_CeCYP16-like, cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) domain similar to Caenorhabditis elegans cyclophilin 16. C. elegans CeCYP-16, compared to the archetypal cyclophilin Human cyclophilin A has, a reduced peptidylprolyl cis- trans isomerase activity, is cyclosporin insensitive and shows an altered substrate preference favoring, hydrophobic, acidic or amide amino acids. Most members of this subfamily have a glutamate residue in the active site at the position equivalent to a tryptophan (W121 in Human cyclophilin A), which has been shown to be important for cyclophilin binding
EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGES
IYGEPFKDEFHSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEV
ETDKDERPVYPPKITSVEVLENPFDDIVPRI
>gnl|CDD|238907 cd01926, cyclophilin_ABH_like, cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome
PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGGKPFGYKGSTFHRVIPDFMIQGGDFT
RGNGTGGKSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDV
VKKIENVGSGNGKPKKKVVIADCG
>gnl|CDD|238908 cd01927, cyclophilin_WD40, cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a WD40 domain. This group consists of several hypothetical and putative eukaryotic and bacterial proteins which have a cyclophilin domain and a WD40 domain. Function of the protein is not known
IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFED
EFSPSLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPY
EDIKIINI
>gnl|CDD|238909 cd01928, Cyclophilin_PPIL3_like, Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a histidine at this position. The exact function of the protein is not known
MSVTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKK
FEDEFRETLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKY
RPLEEIRIKDVTI
>gnl|CDD|238910 cd01935, Ntn_CGH_like, Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins includes conjugated bile acid hydrolase (CBAH), penicillin V acylase (PVA), acid ceramidase (AC), and N-acylethanolamine-hydrolyzing acid amidase (NAAA) which cleave non-peptide carbon-nitrogen bonds in bile salt constituents. These enzymes have an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which they belong. This nucleophilic cysteine is exposed by post-translational prossessing of the precursor protein
CTSIVAQTKDGGVYLGRNMDFSFDYELRLLVFPRGYQRNGQTGDKSKWYAKYGSGGTSAGYIGLVDGMNE
KGLSVSLLYFPGYAYYPAGIKEGKDGLPAFELIRWVLENCDSVEEVKEALKKIPIVDFPIPLGGPAAPLH
YILSDKSGDSAVIEPIDGGLKIYDNPWFGVMTNHPTFDWHLPRRFVRVAYLKNTAQKNKETVEDVKNLFH
ILESVPIPNGLTVYTTVMD
>gnl|CDD|238911 cd01936, Ntn_CA, Cephalosporin acylase (CA) belongs to a family of beta-lactam acylases that includes penicillin G acylase (PGA) and aculeacin A acylase. PGA and CA are crucial for the production of backbone chemicals like 6-aminopenicillanic acid and 7-aminocephalosporanic acid (7-ACA), which can be used to synthesize semi-synthetic penicillins and cephalosporins, respectively. While both PGA and CA have a conserved Ntn (N-terminal nucleophile) hydrolase fold and the structural similarity at their active sites is very high, their sequence similarity to other Ntn's is low
IRRDTYGVPHIYAKDDADLAFGVGYAQAEDNFCLLADLYLTARGERAEYFGPFAAGYNAYGSNGWAVGPS
RTANGNGMLLINPHFPWTGGVRFYEAHLTSPGGLDVYGASLPGSPVINIGFNEHLGWTHTVNTPDHFDVY
RLTLDPEDPLGYLVDGEWRPLEKRTVTIPVKTADGGLATVERTVYRSVHGPVVEMPDGGAYAIRDANLDN
IRMLDQWLAMNKARSLEEFRAALARYQGPSNNTVYADREGNILYLDNSVVPNRSEGAVLDWDRSLPGDDS
ATIWTGLHPYDDLPQLLNPPSGFVQNSNDSPWLTANPASPLTGDSPLGYGTERTPRSLRTRMGLEELQPG
GRFTLEELQALKFDNRLYLAERVLPDLLAACAASDDAAADLAAACAVLAAWDRTADADSRGAALFREWGD
SYVQVVEFDDGGPRARGLLTYGQSTDPGSPHYSDQTELYSRKQLKPVLF
>gnl|CDD|238912 cd01937, ribokinase_group_D, Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time
KIVIIGHVTIDEIVTNGSGVVKPGGPATYASLTLSRLGLTVKLVTKVGRDYPDKWSDLFDNGIEVISLLS
TETTTFELNYTNEGRTRTLLAKCAAIPDTESPLSTITAEIVILGPVPEEISPSLFRKFAFISLDAQGFLR
RANQEKLIKCVILKLHDVLKLSRVEAEVISTPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPAS
KKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFIE
>gnl|CDD|238913 cd01938, ADPGK_ADPPFK, ADP-dependent glucokinase (ADPGK) and phosphofructokinase (ADPPFK). ADPGK and ADPPFK are proteins that rely on ADP rather than ATP to donate a phosphoryl group. They are found in certain hyperthermophilic archaea and in higher eukaryotes. A functional ADPGK has been characterized in mouse and is assumed to be desirable during ischemia/hypoxia. ADPGK and ADPPFK contain a large and a small domain with the binding site located in a groove between the domains. Partial domain closing is seen when ADP is bound, and further domain closing is observed when glucose is also bound. The oligomerization state apparently varies depending on the species, with some existing as monomers, some as dimers, and some as tetramers
AWERLIVNAFRNAKRAAPKVVGVNAAYDLNIDAVKLLDREDLEKRPGKFGEEEVQDEIESEEDLLQSFLH
SFQRGAAAERFVSSEEVFEYLVEWAKEIPWDELRMGGNAGLMANRLAGEGDLKVLLGVPQSSKLQAELFL
DGPIVVPTFENLIEEDEIHLILEYPRGESWGDFVAPRANRFIFHDDDNNPMLMREEFFSSILEFQPDLAV
LSGLQMMEGQSFDEGTRKELLERVKSILEILPPLIPIHLELASTVDEELREEILHEVVPYVDSLGLNEQE
LANLLQVLGGPHLSLASWNGGPPDVGAVLDILLWLLKEHGRDAATRTDLTRIHFHTLAYILATVSRKEET
RWANLFAALAAAARAAKGNIETIDTSRAGLRVPVSFAASASEGRLRIELNPEEPVVCWEREDVEFCFTPV
LVCKEPKSTVGIGDTISASGLVYSF
>gnl|CDD|238914 cd01939, Ketohexokinase, Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism
AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLD
DFQSRGIDISHCYRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDE
TLRMMQHIEEHNNRRPEIRITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAK
KAALLVCTWGDQGAGALGPDGEYVHSPAHKPIRVVDTLGAGDTFNAAVIYALNKGPDDLSEALDFGNRVA
SQKCTGVGFD
>gnl|CDD|238915 cd01940, Fructoselysine_kinase_like, Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown
RLAAIGDNVVDKYLHLGKMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV
KEGENAVADVELVDGDRIFGLSNKGGVAREHPFEADLEYLSQFDLVHTGIYSHEGHLEKALQALVGAGAL
ISFDFSDRWDDDYLQLVCPYVDFAFFSASDLSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYS
VAPRPVEVVDTLGAGDSFIAGFLLSLLAGGTAIAEAMRQGAQFAAKTCGHEGAF
>gnl|CDD|238916 cd01941, YeiC_kinase_like, YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time
EIVVIGAANIDLRGKVSGSLVPGTSNPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEE
SEKAGLNVRGIVFEGRSTASYTAILDKDGDLVVALADMDIYELLTPDFLRKIREALKEAKPIVVDANLPE
EALEYLLALAAKHGVPVAFEPTSAPKLKKLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLL
PGIKNVIVTLGAKGVLLSSREGGVETKLFPAPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQA
AAALTLES
>gnl|CDD|238917 cd01942, ribokinase_group_A, Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time
DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLE
ELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEADPDGLADIVHLSSGPGLIE
LARELAAGGITVSFDPGQELPRLSGEELEEILERADILFVNDYEAELLKERTGLSEAELASGVRVVVVTL
GPKGAIVFEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ
>gnl|CDD|238918 cd01943, MAK32, MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply
DFTTLGMFIIDEIEYPDSEPVTNVLGGAGTYAILGARLFLPPPLSRSISWIVDKGSDFPKSVEDELESWG
TGMVFRRDPGRLTTRGLNIYDGNDRRFFKYLTPKKRIDVSDDLNSTPLIRSSCIHLICSPERCASIVDDI
INLFKLLKGNSPTRPKIVWEPLPDSCDPENLEDLLQALPRVDVFSPNLEEAARLLGLPTSEPSSDEEKEA
VLQALLFSGILQDPGGGVVLRCGKLGCYVGSADSGPELWLPAYHTKSTKVVDPTGGGNSFLGGFAAGLAL
TKSIDEACIYGSVAASFAIEQVGLPRLTKVEGEELWNGETVEERLKEY
>gnl|CDD|238919 cd01944, YegV_kinase_like, YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time
KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQA
MRDEGIEILLPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDYVYLSGYTLASEN
ASKVILLEWLEALPAGTTLVFDPGPRISDIPDTILQALMAKRPIWSCNREEAAIFAERGDPAAEASALRI
YAKTAAPVVVRLGSNGAWIRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAA
AAIVVTRSG
>gnl|CDD|238920 cd01945, ribokinase_group_B, Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time
RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILA
ELAAEGVDTSFIVVAPGARSPISSITDITGDRATISITAIDTQAAPDSLPDAILGGADAVLVDGRQPEAA
LHLAQEARARGIPIPLDLDGGGLRVLEELLPLADHAICSENFLRPNTGSADDEALELLASLGIPFVAVTL
GEAGCLWLERDGELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRA
GLPT
>gnl|CDD|238921 cd01946, ribokinase_group_C, Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time
SLLVVGSVAFDAIETPFGKVDKALGGSATYFSLSASYFTDVRLVGVVGEDFPEEDYKLLNSHNIVTLGLL
SKEDGKTFHWAGRYHYDLNEADTLDTDLNVFADFDPQLPEHYKDSEFVFLGNIAPELQREVLEQVKDPKL
VVMDTMNFWISIKPEKLKKVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLF
TDDGYFAAPAYPLESVFDPTGAGDTFAGGFIGYLASQKDTSEANMRRAIIYGSAMASFCVEDFGTKR
>gnl|CDD|238922 cd01947, Guanosine_kinase_like, Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time
KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLE
ELESGGDKHTVAWRDKPTRKTLSFIDPNGERTITVPGERLEDDLKWPILDEGDGVFITAAAVDKEAIRKC
RETKLVILQVTPRVRVDELNQALIPLDILIGSRLDPGELVVAEKIAGPFPRYLIVTEGELGAILYPGGRY
NHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY
>gnl|CDD|238923 cd01948, EAL, EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria
ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEA
CRQLARWQAGGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRR
LRALGVRIALDDFGTGYSSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGV
ETEEQLELLRELGCDYVQGYLFSRPLPAEE
>gnl|CDD|143635 cd01949, GGDEF, Diguanylate-cyclase (DGC) or GGDEF domain. Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria
YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLR
ESDLVARLGGDEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLR
RADEALYRAKRSGRNRVV
>gnl|CDD|173886 cd01951, lectin_L-type, legume lectins. The L-type (legume-type) lectins are a highly diverse family of carbohydrate binding proteins that generally display no enzymatic activity toward the sugars they bind. This family includes arcelin, concanavalinA, the lectin-like receptor kinases, the ERGIC-53/VIP36/EMP46 type1 transmembrane proteins, and an alpha-amylase inhibitor. L-type lectins have a dome-shaped beta-barrel carbohydrate recognition domain with a curved seven-stranded beta-sheet referred to as the "front face" and a flat six-stranded beta-sheet referred to as the "back face". This domain homodimerizes so that adjacent back sheets form a contiguous 12-stranded sheet and homotetramers occur by a back-to-back association of these homodimers. Though L-type lectins exhibit both sequence and structural similarity to one another, their carbohydrate binding specificities differ widely
TSLNFSNFSNNNQSNWQLNGSATLTTDSGVLRLTPDTGNQAGSAWYKTPIDLSKDFTTTFKFYLGTKGTN
GADGIAFVLQNDPAGALGGGGGGGGLGYGGIGNSVAVEFDTYKNDDNNDPNGNHISIDVNGNGNNTALAT
SLGSASLPNGTGLGNEHTVRITYDPTTNTLTVYLDNGSTLTSLDITIPVDLIQLGPTKAYFGFTASTGGL
TNLHDILNWSFTS
>gnl|CDD|238924 cd01958, HPS_like, HPS_like: Hydrophobic Protein from Soybean (HPS)-like subfamily; composed of proteins with similarity to HPS, a small hydrophobic protein with unknown function related to cereal-type alpha-amylase inhibitors and lipid transfer proteins. In addition to HPS, members of this subfamily include a hybrid proline-rich protein (HyPRP) from maize, a dark-inducible protein (LeDI-2) from Lithospermum erythrorhizon, maize ZRP3 protein, and rice RcC3 protein. HyPRP is an embryo-specific protein that contains an N-terminal proline-rich domain and a C-terminal HPS-like cysteine-rich domain. It has been suggested that HyPRP may be involved in the stability and defense of the developing embryo. LeDI-2 is a root-specific protein that may be involved in regulating the biosynthesis of shikonin derivatives in L. erythrorhizon. Maize ZRP3 and rice RcC3 are root-specific proteins whose functions are yet to be determined. It has been reported that ZRP3 largely accumulates in a distinct subset of cortical cells
GPTCPRDALKLGVCANVLGLSLLLLGTPAVQPCCPLIGGLADLDAAVCLCTAIKANILGISINIPVALSL
LLNSCGRNVPPGFTC
>gnl|CDD|238925 cd01959, nsLTP2, nsLTP2: Non-specific lipid-transfer protein type 2 (nsLTP2) subfamily; Plant nsLTPs are small, soluble proteins that facilitate the transfer of fatty acids, phospholipids, glycolipids, and steroids between membranes. In addition to lipid transport and assembly, nsLTPs also play a key role in the defense of plants against pathogens. There are two closely-related types of nsLTPs, types 1 and 2, which differ in protein sequence, molecular weight, and biological properties. nsLTPs contain an internal hydrophobic cavity, which serves as the binding site for lipids. nsLTP2 can bind lipids and sterols. Structure studies of rice nsLTPs show that the plasticity of the hydrophobic cavity is an important factor in ligand binding. The flexibility of the sLTP2 cavity allows its binding to rigid sterol molecules, whereas nsLTP1 cannot bind sterols despite its larger cavity size. The resulting nsLTP2/sterol complexes may bind to receptors that trigger defense responses. nsLTP2 gene expression has been observed in barley and rice developing seeds, during Zinnia elegans cell differentiation, and under abiotic stress conditions in barley roots. The nsLTP2 of Brassica rapa has also been identified as a potent allergen
CNPTQLSPCLPAILGGSPPSAACCAKLKEQQSCLCQYAKNPSLKQYVNSPNARKVLAACGVPYPNC
>gnl|CDD|238926 cd01960, nsLTP1, nsLTP1: Non-specific lipid-transfer protein type 1 (nsLTP1) subfamily; Plant nsLTPs are small, soluble proteins that facilitate the transfer of fatty acids, phospholipids, glycolipids, and steroids between membranes. In addition to lipid transport and assembly, nsLTPs also play a key role in the defense of plants against pathogens. There are two closely-related types of nsLTPs, types 1 and 2, which differ in protein sequence, molecular weight, and biological properties. nsLTPs contain an internal hydrophobic cavity, which serves as the binding site for lipids. The hydrophobic cavity accommodates various fatty acid ligands containing from ten to 18 carbon atoms. In general, the cavity is larger in nsLTP1 than in nsLTP2. nsLTP1 proteins are located in extracellular layers and in vacuolar structures. They may be involved in the formation of cutin layers on plant surfaces by transporting cutin monomers. Many nsLTP1 proteins have been characterized as allergens in humans
ISCGQVTSLLAPCLGYLTGGGPAPSPACCSGVKSLNGLAKTTADRQAACNCLKSAAAGISGLNPGRAAGL
PGKCGVSIPYPISPSTDCS
>gnl|CDD|238927 cd01965, Nitrogenase_MoFe_beta_like, Nitrogenase_MoFe_beta_like: Nitrogenase MoFe protein, beta subunit_like. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen (N2) to ammonia. This group contains the beta subunits of component 1 of the three known genetically distinct types of nitrogenase systems: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium-dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase). These nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). The most widespread and best characterized of these systems is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers having alpha and beta subunits similar to the alpha and beta subunits of MoFe. For MoFe, each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains, a single [4Fe-4S] cluster from which electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo, the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo-nitrogenase in that it produces free hydrazine, as a minor product during N2-reduction and, ethane as a minor product during acetylene reduction
TINPAKACQPLGAALAFLGIEGCMPLVHGSQGCSSFARVLFTRHFKEPIPIASTSMTEDAAVFGGEDNLI
EALKNLLSRYKPDVIGVLTTCLTETIGDDVAGFIKEFRAEGPEPADFPVVYASTPSFKGSHETGYDNAVK
AIIEQLAKPSEVKKNGKVNLLPGFPLTPGDVREIKRILEAFGLEPIILPDLSDSLDGHLTDGYSPLTKGG
TTLEEIRDAGNAKATIALGEYSGRKAAKALEEKFGVPYILFPTPIGLKATDEFLRALSKLSGKPIPEELE
RERGRLLDAMLDSHFYLGGKRVAIAGDPDLLLGLSRFLLEMGAEPVAAVTGTDNPPFEKRMELLASLEGI
PAEVVFVGDLWDLESLAKEEPVDLLIGNSHGRYLARDLGIPLVRVGFPIFDRLGLHRRPYVGYRGALNLL
EEIANTLL
>gnl|CDD|238928 cd01966, Nitrogenase_NifN_1, Nitrogenase_nifN1: A subgroup of the NifN subunit of the NifEN complex: NifN forms an alpha2beta2 tetramer with NifE. NifN and nifE are structurally homologous to nitrogenase MoFe protein beta and alpha subunits respectively. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of the MoFe protein. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to the NifEN complex where it is further processed to FeMoco. The nifEN bound precursor of FeMoco has been identified as a molybdenum-free, iron- and sulfur- containing analog of FeMoco. It has been suggested that this nifEN bound precursor also acts as a cofactor precursor in nitrogenase systems which require a cofactor other than FeMoco: i.e. iron-vanadium cofactor (FeVco) or iron only cofactor (FeFeco)
SVNPLKLSQPLGAALAFLGIDGCMPLFHGAQGCTSFAKVLLVRHFKEPIPLQTTAMDEVSTILGGGENLE
EALDTLAERAKPKVIGLLSTGLTETRGEDIAGALKQFRAEHPELADVPVVYVSTPDFEGSLEDGWAAAVE
AIIEALVEPGSRTVTDPRQVNLLPGAHLTPGDVEELKDIIEAFGLEPIILPDLSGSLDGHLADDWSPTTT
GGTTLEDIRQMGRSAATLAIGESMRKAAEALEERTGVPYYVFPSLTGLEAVDALIATLAKLSGRPVPEKI
RRQRAQLQDAMLDGHFYLGGKRVAIALEPDLLAALSSFLAEMGAEIVAAVATTDSPALEKLPAEEVVVGD
LEDLEDLAAEADLLVTNSHGRQAAERLGIPLLRAGFPIFDRLGAAHKCTIGYRGTRDLLFEIANLFL
>gnl|CDD|238929 cd01967, Nitrogenase_MoFe_alpha_like, Nitrogenase_MoFe_alpha_like: Nitrogenase MoFe protein, alpha subunit_like. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen to ammonia. Three genetically distinct types of nitrogenase systems are known to exist: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase). These nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). This group contains the alpha subunit of component 1 of all three different forms. The most widespread and best characterized of these systems is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers having alpha and beta subunits similar to the alpha and beta subunits of MoFe. The role of the delta subunit is unknown. For MoFe, each alphabeta pair of subunits contains one P-cluster (located at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein is a homodimer which contains, a single [4Fe-4S] cluster from which electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo- nitrogenase in that it produces free hydrazine, as a minor product during dinitrogen reduction and, ethane as a minor product during acetylene reduction
PGPMTERGCCAFGGAGVVLGPIKDAVHIVHGPIGCAYYTWDTRRNLSSGENLFYKYGFSTDMQEKDIVFG
GEKKLKKAIKEAYERFPPKAIFVYSTCPTGLIGDDIEAVAKEASKELGIPVIPVNCEGFRGVSQSLGHHI
ANDAILDHLVGTKEPEEKTPYDVNIIGEYNIGGDAWVIKPLLEELGIRVNATFTGDGTVDELRRAHRAKL
NLVHCSRSMNYLAREMEERYGIPYMEVNFYGFEDTSESLRKIAKFFGDEEKAEEVIAEEEARIKPELEKY
RERLKGKKVIIYTGGARSWHVIAALRELGMEVVAAGYEFGHDDDYERIRKILDEGTLLVDDYNDLELEEL
VEKLKPDLILSGIKEKYVAQKLGIPFLDLHSERNGPYAGYEGFLNFARDIDTALNS
>gnl|CDD|238930 cd01968, Nitrogenase_NifE_I, Nitrogenase_NifE_I: a subgroup of the NifE subunit of the NifEN complex: NifE forms an alpha2beta2 tetramer with NifN. NifE and NifN are structurally homologous to nitrogenase MoFe protein alpha and beta subunits respectively. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of the MoFe protein. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to the NifEN complex where it is further processed to FeMoco. The NifEN bound precursor of FeMoco has been identified as a molybdenum-free, iron- and sulfur- containing analog of FeMoco. It has been suggested that this NifEN bound precursor also acts as a cofactor precursor in nitrogenase systems which require a cofactor other than FeMoco: i.e. iron-vanadium cofactor (FeVco) or iron only cofactor (FeFeco)
LPGGVTQRGCVFDGARVVLMPITDAAHLVHGPIGCAGYSWDIRGSRSSGSELYRMGFSTDLSEKDVIFGG
EKKLYKAILEIIERYHPKAVFVYSTCVVALIGDDIDAVCKTASEKFGIPVIPVHSPGFVGNKNLGNKLAC
EALLDHVIGTEEPEPLTPYDINLIGEFNVAGELWGVKPLLEKLGIRVLASITGDSRVDEIRRAHRAKLNV
VQCSKSMIYLARKMEEKYGIPYIEVSFYGIRDTSKSLRNIAELLGDEELIERTEELIAREEARLRPELAP
YRARLEGKKAALYTGGVKSWSLVSALQDLGMEVVATGTQKGTKEDYERIKELLGEGTVIVDDANPRELKK
LLKEKKADLLVAGGKERYLALKLGIPFCDINHERKHPYAGYEGMLNFAKEVDLAVNSPVW
>gnl|CDD|238931 cd01971, Nitrogenase_VnfN_like, Nitrogenase_vnfN_like: VnfN subunit of the VnfEN complex-like. This group in addition to VnfN contains a subset of the beta subunit of the nitrogenase MoFe protein and NifN-like proteins. The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of MoFe protein of the molybdenum(Mo)-nitrogenase. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to NifEN where it is further processed to FeMoco. VnfEN may similarly be a scaffolding protien for the iron-vanadium cofactor (FeVco) of the vanadium-dependent (V)-nitrogenase. NifE and NifN are essential for the Mo-nitrogenase, VnfE and VnfN are not essential for the V-nitrogenase. NifE and NifN can substitute when the vnfEN genes are inactivated
PIEQPRYGCALGGALYTVSAIPRAVPIIHSGPGCASKQSGAVAFGNGYQGGGYGVAPCTNATETEIVFGG
EDRLRELIKSTLSIIDADLFVVLTGCIAEIIGDDVGAVVSEFQEGGAPIVYLETGGFKGNNYAGHEIVLK
AIIDQYVGQSEEKEPGLVNLWGPVPYQDPFWRGDLEEIKRVLEGIGLKVNILFGPESNGEELRSIPKAQF
NLVLSPWVGLEFAQHLEEKYGQPYIHSPTLPIGAKATAEFLRQVAKFAGIEKAKVEAFIKAEEKRYYHYL
ERFSDFMARWGLPRRFAVIADSTYALGLARFLVNELGWVPAKQVITDNPPEKYRSAIENEFEAEGVSAEV
VFSEDGYAIGQSLRQSDFKYKPPIIFGSSWERDLAKELGGKILEVSFPVTNRVVLNRGYAGYRGALTLLE
DIYTTVI
>gnl|CDD|238932 cd01972, Nitrogenase_VnfE_like, Nitrogenase_VnfE_like: VnfE subunit of the VnfEN complex_like. This group in addition to VnfE contains a subset of the alpha subunit of the nitrogenase MoFe protein and NifE-like proteins. The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of MoFe protein of the molybdenum(Mo)-nitrogenase. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to NifEN where it is further processed to FeMoco. VnfEN may similarly be a scaffolding protein for the iron-vanadium cofactor (FeVco) of the vanadium-dependent (V)-nitrogenase. NifE and NifN are essential for the Mo-nitrogenase, VnfE and VnfN are not essential for the V-nitrogenase. NifE and NifN can substitute when the vnfEN genes are inactivated
KLQFSQASMCKFWTAFCILSGIRDAVVVQHGPIGCAAGQSFFNRLYRCGEMRRGLNEPVLSTNLTEKDVV
FGGEKKLEDTIKEAYSRYKPKAIFVATSCATGIIGDDVESVVEELEDEIGIPVVALHCEGFKGKHWRSGF
DAAFHGILRHLVPPQDPTKQEDSVNIIGLWGGPERTEQEDVDEFKRLLNELGLRVNAIIAGGCSVEELER
ASEAAANVTLCLDLGYYLGAALEQRFGVPEIKAPQPYGIEATDKWLREIAKVLGMEAEAEAVIEREHERV
APEIEELRKALKGKKAIVETGAAYGHLLIAVLRELGFGEVPVVLVFHHDPTYDRGDSEKDLLEHGVDPEI
DITKYTVSNGQYYQFYNLLKRVKPDFIIFRHGGLFPDATVYLGIPVVPLNDELNQPQFGYRGLLKIANKI
VDALEN
>gnl|CDD|238933 cd01973, Nitrogenase_VFe_beta_like, Nitrogenase_VFe_beta -like: Nitrogenase VFe protein, beta subunit like. This group contains proteins similar to the beta subunits of the VFe protein of the vanadium-dependent (V-) nitrogenase. Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen (N2) to ammonia. In addition to V-nitrogenase there is a molybdenum (Mo)-dependent nitrogenase and an iron only (Fe-) nitrogenase. The Mo-nitrogenase is the most widespread and best characterized of these systems. These systems consist of component 1 (VFe protein, FeFe protein or, MoFe protein respectively) and, component 2 (Fe protein). MoFe is an alpha2beta2 tetramer, V-and Fe- nitrogenases are alpha2beta2delta2 hexamers. The alpha and beta subunits of VFe and FeFe are similar to the alpha and beta subunits of MoFe. For MoFe each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein which has a practically identical structure in all three systems, it contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo-nitrogenase in that it produces free hydrazine, as a minor product during dinitrogen reduction and, ethane as a minor product during acetylene reduction
KERVGVINPMYTCQPAGAQYAGIGIKDCIPLVHGGQGCTMFVRLLFAQHFKENFDIASSSLHEDSAVFGG
AKRVEEGVLVLARRYPDLRVIPIITTCSTEIIGDDIEGVIRKLNEALKEEFPDREVHLIPVHTPSFKGSM
VTGYDEAVRSVVKTIAKKGAPSGKLNVFTGWVNPGDVVELKHYLSEMDVEANILMDTEDFDSPMLPDKSA
VTHGNTTIEDIADSANAIATIALARYEGGKAAEFLQKKFDVPAILGPTPIGIKNTDAFLQNIKELTGKPI
PESLVRERGIAIDALADLAHMFFANKKVAIFGHPDLVIGLAEFCLEVEMKPVLLLLGDDNSKYKKDPRIK
ALKEKADYDMEIVTNADLWELEKRIKNKGLELDLILGHSKGRYIAIDNNIPMVRVGFPTFDRAGLYRHPV
IGYRGAMWLGEAIANTLFADMEYKKNKEWILNVW
>gnl|CDD|238934 cd01974, Nitrogenase_MoFe_beta, Nitrogenase_MoFe_beta: Nitrogenase MoFe protein, beta subunit. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen to ammonia. The Molybdenum (Mo-) nitrogenase is the most widespread and best characterized of these systems. Mo-nitrogenase consists of the MoFe protein (component 1) and the Fe protein (component 2). MoFe is an alpha2beta2 tetramer. This group contains the beta subunit of the MoFe protein. Each alphabeta pair of MoFe contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction
REALTINPAKACQPLGAVYAALGFEGTLPFVHGSQGCVAYFRSHLSRHFKEPVSAVSSSMTEDAAVFGGQ
NNLIDGLKNAYAVYKPDMIAVSTTCMAEVIGDDLNAFIKNAKNKGSIPADFPVPFANTPSFVGSHITGYD
NMVKGILTHLTEGSGGAGKNGKLNIIPGFDTYAGNMREIKRLLELMGVDYTILPDTSDVLDTPADGEYRM
YPGGTTLEELKDAGNAKATLALQEYATEKTAKFLEKKCKVPVETLNMPIGVAATDEFLMALSELTGKPIP
EELEEERGRLVDAMTDSHQYLHGKKFALYGDPDFLIGLTSFLLELGMEPVHVLTGNGGKRFEKEMQALLD
ASPYGAGAKVYPGKDLWHLRSLLFTEPVDLLIGNTYGKYIARDTDIPLVRFGFPIFDRHHHHRFPIVGYE
GALRLLTTILNTLLD
>gnl|CDD|238935 cd01976, Nitrogenase_MoFe_alpha, Nitrogenase_MoFe_alpha_II: Nitrogenase MoFe protein, beta subunit. A group of proteins similar to the alpha subunit of the MoFe protein of the molybdenum (Mo-) nitrogenase. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen to ammonia. The Mo-nitrogenase is the most widespread and best characterized of these systems. Mo-nitrogenase consists of the MoFe protein (component 1) and the Fe protein (component 2). MoFe is an alpha2beta2 tetramer. Each alphabeta pair of MoFe contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction
IKSNIKSVPGVMTIRGCAYAGSKGVVWGPIKDMVHISHGPVGCGQYSWATRRNYYRGETGVDNFGTMQFT
TDFQEKDIVFGGDKKLAKAIDEAYELFPLNKGISVQSECPVGLIGDDIEAVARKASKELGIPVVPVRCEG
FRGVSQSLGHHIANDAIRDHILGKRNEFEPTPYDVNIIGDYNIGGDAWASRILLEEMGLRVVAQWSGDGT
LNEMENAHKAKLNLIHCYRSMNYIARMMEEKYGIPWMEYNFFGPTKIAESLRKIAAYFDDEITAKTEEVI
AEYKPAMEAVIAKYRPRLEGKTVMLYVGGLRPRHYIGAYEDLGMEVVGTGYEFAHRDDYERTEVIPKEGT
LLYDDVTHYELEEFVKRLKPDLIGSGIKEKYVFQKMGIPFRQMHSWDYSGPYHGFDGFAIFARDMDMAIN
S
>gnl|CDD|238936 cd01977, Nitrogenase_VFe_alpha, Nitrogenase_VFe_alpha -like: Nitrogenase VFe protein, alpha subunit like. This group contains proteins similar to the alpha subunits of, the VFe protein of the vanadium-dependent (V-) nitrogenase and the FeFe protein of the iron only (Fe-) nitrogenase Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen (N2) to ammonia. In addition to V- and Fe- nitrogenases there is a molybdenum (Mo)-dependent nitrogenase which is the most widespread and best characterized of these systems. These systems consist of component 1 (VFe protein, FeFe protein or, MoFe protein respectively) and, component 2 (Fe protein). MoFe is an alpha2beta2 tetramer, V-and Fe- nitrogenases are alpha2beta2delta2 hexamers. The alpha and beta subunits of VFe and FeFe are similar to the alpha and beta subunits of MoFe. For MoFe each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein which has a practically identical structure in all three systems, it contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo-nitrogenase in that it produces free hydrazine, as a minor product during dinitrogen reduction and, ethane as a minor product during acetylene reduction
PGSLSERGCAYCGAKLVIGGVIKDVIHVIHGPVGCTYDTWHTKRYPSDNDNFQLKYIWSTDMKESHVVFG
GEKKLKKNIIEAFKEFPDIKRMTVYTTCTTALIGDDIKAVAKEVMEELPDVDIFVCNAPGFAGPSQSKGH
HVLNIAWINQKVGTVEPEITSDYTINYIGDYNIQGDTEVLQKYFERMGIQVLSTFTGNGTYDDLRWMHRA
KLNVVNCARSAGYIANELKKRYGIPRLDVDGFGFEYCAESLRKIGAFFGIEDRAEAVIAEEMAKWKPELD
WYKERLKGKKVCIWTGGPKLWHWTKVIEDELGMQVVAMSSKFGHQEDFEKVIARGGEGTIYIDDPNELEF
FEILEMLKPDIILTGPRVGELVKKLHVPYVNIHAYHNGPYMGFEGFVNLARDMYNAIYSPIWQLA
>gnl|CDD|238937 cd01979, Pchlide_reductase_N, Pchlide_reductase_N: N protein of the NB protein complex of Protochlorophyllide (Pchlide)_reductase. Pchlide reductase catalyzes the reductive formation of chlorophyllide (chlide) from protochlorophyllide (pchlide) during biosynthesis of chlorophylls and bacteriochlorophylls. This group contains both the light-independent Pchlide reductase (DPOR) and light-dependent Pchlide reductase (LPOR). Angiosperms contain only LPOR, cyanobacteria, algae and gymnosperms contain both DPOR and LPOR, primitive anoxygenic photosynthetic bacteria contain only DPOR. NB is structurally similar to the FeMo protein of nitrogenase, forming an N2B2 heterotetramer. N and B are homologous to the FeMo alpha and beta subunits respectively. Also in common with nitrogenase in vitro DPOR activity requires ATP hydrolysis and dithoionite or ferredoxin as electron donor. The NB protein complex may serve as a catalytic site for Pchlide reduction similar to MoFe for nitrogen reduction
FECETGNYHTFCGLACVAWLYQKIEDSFFLVVGTKTCAHFLQNALGVMIFAEPRFAMAELEEGDLSALLN
DYAELDRVVTQIKRDRNPSVIFLIGSCTTEVIKMDLEGAAPRLSAEIGVPILVASASGLDYTFTQGEDTV
LAALVPRCPEKPSPERSLVLVGSLPDIVEDQLRRELEQLGIPVVGFLPPRRYTDLPVIGPGTYVLGIQPF
LSRTATTLMRRRKCKLLSAPFPIGPDGTRAWLEAICSAFGIFPSVLAEREARAWRALEPYLDLLRGKSIF
FMGDNLLEIPLARFLTRCGMIVVEVGTPYLDKRFQAAELELLPPMVRIVEKPDNYRQLDRIRELRPDLVV
TGLGLANPLEARGITTKWSIEFTFAQIHGFTNARDLAELFTRPLRR
>gnl|CDD|238938 cd01980, Chlide_reductase_Y, Chlide_reductase_Y : Y subunit of chlorophyllide (chlide) reductase (BchY). Chlide reductase participates in photosynthetic pigment synthesis playing a role in the conversion of chlorophylls(Chl) into bacteriochlorophylls (BChl). Chlide reductase catalyzes the reduction of the B-ring of the tetrapyrolle. Chlide reductase is a three subunit enzyme (subunits are designated BchX, BchY and BchZ). The similarity between these three subunits and the subunits for nitrogenase suggests that BchX serves as an electron donor for the BchY-BchY catalytic subunits
AYPTENGAGPHLHPQTMCPAFGSLRVLTRIEGAATVLVGDAGCLYGLTFVSHFYAARRSIVAVPLSSETL
STGKLFEDIREAIRKLADPPAYTFIPVISLCVAETAGVAEELLPKQIDGVRVILVRGPAFPIHSHPEAKD
VGAMLLLARFEDFDGPVAEPSLALLGEMFPADPVAIGSVLERMGLAAVPVVPTREWRELYAAGDAAAVAA
LHPFYTATIRELEEAGRPIVSGAPVGADGTAAWLEAVGEALGLDMDQVRKVANEEKAAAKGAIRAFSPIK
GRVLVSGYEGNELLVARLLIESGAEVPYVSTSIPKTSLSAPDYEWLSALGVEVRYRKSLEDDIAAVEEYR
PDLAIGTTPLVQYAKEKGIPALYYTNLISARPLFGAAGAGSLLQVVNALLANKDRFDKMREFFEGV
>gnl|CDD|238939 cd01981, Pchlide_reductase_B, Pchlide_reductase_B: B protein of the NB protein complex of Protochlorophyllide (Pchlide)_reductase. Pchlide reductase catalyzes the reductive formation of chlorophyllide (chlide) from protochlorophyllide (pchlide) during biosynthesis of chlorophylls and bacteriochlorophylls. This group contains both the light-independent Pchlide reductase (DPOR) and light-dependent Pchlide reductase (LPOR). Angiosperms contain only LPOR, cyanobacteria, algae and gymnosperms contain both DPOR and LPOR, primitive anoxygenic photosynthetic bacteria contain only DPOR. NB is structurally similar to the FeMo protein of nitrogenase, forming an N2B2 heterotetramer. N and B are homologous to the FeMo alpha and beta subunits respectively. Also in common with nitrogenase in vitro DPOR activity requires ATP hydrolysis and dithoionite or ferredoxin as electron donor. The NB protein complex may serve as a catalytic site for Pchlide reduction similar to MoFe for nitrogen reduction
MKLAYWMYEGPAHIGTLRVASSFKNVHAVMHAPLGDDYFNVMRSMLERERDFTPVTASTVDRHVLARGSQ
EKVVENITRKDKEEKPDLIVLTPTCTSSILQEDLQNFVRAAGLSSKSPVLPLDVNHYRVNELQAADETFE
QLVRFYAEKARPQGTPREKTEKPSVNLIGPSSLGFHNRHDCRELKRLLHTLGIEVNVVIPEGASVDDLNE
LPKAWFNIVPYREYGLSAALYLEEEFGMPSVKITPIGVVATARFLREIQELLGIQIIPELVNVEPYIDSQ
TRWVSQSARSSRSIDSQNLTGKRAFVFGDATHVAAATRILAREMGFRVVGAGTYCKEDAKWFREQATGYC
DEALITDDHTEVGDMIARTEPELIFGTQMERHIGKRLDIPCAVISAPVHIQNFPLGYRPFLGYEGTNVIA
DTVYNSLTLG
>gnl|CDD|238940 cd01982, Chlide_reductase_Z, Chlide_reductase_Z : Z subunit of chlorophyllide (chlide) reductase (BchZ). Chlide reductase participates in photosynthetic pigment synthesis playing a role in the conversion of chlorophylls(Chl) into bacteriochlorophylls (BChl). Chlide reductase catalyzes the reduction of the B-ring of the tetrapyrolle. Chlide reductase is a three subunit enzyme (subunits are designated BchX, BchY and BchZ). The similarity between these three subunits and the subunits for nitrogenase suggests that BchX serves as an electron donor for the BchY-BchY catalytic subunits
KTIRDESRASAYWGAVNTFCALKDVHVVADAPVGCYNLPGVAVMDYTDALPYLENLTPTSLTEEEISSSG
TAGAVIRTIDKLDPSGKLILVSSAESEMIGSDHTPMLTMQQPFVRFFIGENEWQGRDRALEWLFDEFDLR
KPWQIEPKPFVQGRKGTVNIIGPSYGCFNSPSDLAEVKRLVTGIGAEVNHVYPFESHLAEIPKLKNAAVN
VVMYREFGRGLAEDLGRPYLYAPFGIEETTAFLRELGRLLGLDPEAFIFREEEKRLTLLPVWWLWRGPQF
EWFPTFRFCATATKSYAAGGLLELLLELGMQCLFSRDAGEKDNDEPVRIEIRQKQPQFLFGRMNDKIYLA
ETLAKHRFIPAFIPAPFPGRALRRPTGTPFMGYWGAQEIVQELYNRLFNFLPNILPLGTENP
>gnl|CDD|349751 cd01983, SIMIBI, SIMIBI (signal recognition particle, MinD and BioD)-class NTPases. SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion
RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLDDYVLIDGGGGLETGLLLGTIVALLALKKADEV
IVVVDPELGSLLEAVKLLLALLLLGIGIRPDGIVLNK
>gnl|CDD|467489 cd01984, AANH_superfamily, Adenine nucleotide alpha hydrolase (AANH) superfamily. The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide
ILVPLSGGEDSSIALKHAKKFKTSKAEEVVVVHVGEIVEIAKAEGVDMVLMGVLVP
>gnl|CDD|467490 cd01986, AANH-like, adenine nucleotide alpha hydrolase (AANH)-like proteins. This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide
VVVGYSGGKDSSVALHLASRLGRKAEVAVVHIDHGIGFKEEAESVASIARRSILKKLAEKGARAIATGVL
RPLL
>gnl|CDD|467491 cd01987, USP_KdpD-like, USP domain of the osmosensitive K+ channel histidine kinase family. The KdpDE two component system is widespread in bacteria and archaea; it controls potassium homeostasis and virulence by regulating the transcription of multiple genes, including a kdpFABC operon, which encodes a high-affinity P-type ATPase transporter. The KdpD histidine kinase (HK, EC:2.7.13.3) contain an N-terminal sensory cytoplasmic region (NTR) composed of KdpD' and universal stress protein (USP) domains, a canonical transmembrane domain, and a cytoplasmic C-terminal region with a transmitter GAF domain and an EnvZ-like catalytic HK domain. Proteins containing the USP domain are induced by many environmental stressors such as nutrient starvation, drought, extreme temperatures, high salinity, and the presence of uncouplers, antibiotics, and metals. It enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity
RILVCISSSPTSEKLIRRAARLAERLNGELTAVYVETPEESRLDEESQRRLLTNLKLAEELGAEVVSVEG
DDVAEAIVEFARERNVTQIVLGQSRRRRWRRLFKGSLVDRLLREAPNIDVHIVP
>gnl|CDD|467492 cd01988, USP_NhaS5_C, C-terminal USP domain(s) of Na(+)/H(+) antiporter NhaS5 and similar proteins. Na(+)/H(+) exchange proteins eject protons from cells, effectively eliminating excess acid from actively metabolizing cells. Na(+)/H(+) exchange activity is also crucial for the regulation of cell volume, and for the reabsorption of NaCl across renal, intestinal, and other epithelia. These antiporters exchange Na(+) for H(+) in an electroneutral manner, and this activity is carried out by a family of Na(+)/H(+) exchangers, or NHEs, which are known to be present in both prokaryotic and eukaryotic cells. These exchangers are highly-regulated (glyco)phosphoproteins, which, based on their primary structure, appear to contain 10-12 membrane-spanning regions (M) at the N-terminus and a large cytoplasmic region at the C-terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. This is thought to be the region that is involved in the transport of sodium and hydrogen ions. The C-terminal region contains one or two domains that show homology with universal stress protein (USP), a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. USP enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity
RVLVPTANPPTAKLLLEFAAALAEDEKGAIVPLLYVGSPNHMDDKELEQAEQRFEELMELLNGVNVHPIV
RISHSVAARVTAREAKSFADLIVMGWRRTFLGNVLLGSTIDKVLMKAPTDVAVTR
>gnl|CDD|467493 cd01989, USP_STK_Ubox_N, N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins. This model represents the N-terminal domain found in some plant serine threonine kinases (STK, EC 2.7.11.-) and U-box domain-containing proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They play a role in the regulation of cell proliferation, programmed cell death (apoptosis), cell differentiation, and embryonic development. These enzymes belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. U-box domain-containing proteins function as E3 ubiquitin ligases (EC 2.3.2.27), mediating the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin. The N-terminal domain of these proteins is homologous to the universal stress protein (USP) family which has an ATP binding fold. The N-terminal domain is predicted to be involved in ATP binding
KVAVAVDGDDKKSKSALKWALDNLAPRGAKIVLVHVHPPVTMIPTPSGKVPPIQLREEEVSAYRKQEREK
TEKMLLPYLDMCSRKKVQAEKVVIESDDVAKGIVELISQHGITKLVMGAASDNHFSMKLKKSDVASSVMK
AAPDFCTVWVVCKG
>gnl|CDD|467494 cd01990, LarE-like, Lactate racemization operon protein LarE and similar proteins. This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus
KVVVAFSGGVDSSLLAKLAKEVLGDNVVAVTADSPLVPREELEEAKRIAEEIGIRHEIIKTDELDDEEYV
ANDPDRCYHCKKALYSTLKEIAKERGYDVVLDGTNADDLKDYRPGLLAAAELGIRSPLPELGLTKSEIRE
LARELGLPNWDKPASACLASRIPYGEEITPERLKRIEKAEELYLRLLGFRQVRVRHHGDIARIEVLDEEI
ESLLDKELREII
>gnl|CDD|467495 cd01991, Asn_synthase_B_C, C-terminal domain of asparagine synthase B. The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase
SDVPVGVLLSGGLDSSLIAALAARLLPETPIDLFTVGFEGSPTPDRAAARRVAEELGTEHHEVEVTIEEL
LDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRGWEALEEE
LLRDLDRLWTRNLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPRGGGEKYILREAARDLLPD
EIAWRPKRAIQFGS
>gnl|CDD|467496 cd01992, TilS_N, N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins. tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus
KILVAVSGGPDSMALLHLLKELRPKLGLKLVAVHVDHGLREESAEEAQFVAKLCKKLGIPLHILTVTEAP
KSGGNLEAAAREARYAFLERAAKEHGIDVLLTAHHLDDQAETVLMRLLRGSGLSGLAGMAARSKAGGIRL
IRPLLGISKAELLAYCRENGLPWVEDPSNADLKYTRNRIRHELLP
>gnl|CDD|467497 cd01993, TtuA-like, tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins. tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus
RYKMFEKDDKILVAVSGGKDSLALLAVLKKLGYNVEALYINLGIGEYSEKSEEVVKKLAEKLNLPLHVVD
LKEEYGLGIPELAKKSRRPPCSVCGLVKRYIMNKFAVENGFDVVATGHNLDDEAAFLLGNILNWNEEYLA
KQGPFLLPEHGGLVTRVKPLYEITEEEIALYALLNGIPYLEEECPYAEGA
>gnl|CDD|467498 cd01994, AANH_PF0828-like, putative ATP pyrophosphatase PF0828 and similar proteins. This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus
KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDKDSYMFQTVGHELLELQAEALGLPLIRREIRGKS
VTQELGYEGEEEDEVEDLYELLKKVKERPEVEAVVSGAILSDYQRNRVERVCERLGLKSLAPLWQRDQEE
LLEELIDLGFEARIVKVAAMGLDEEWLGRRLDEDQPEELLKLNEKYGVHVCGEGGEYETLVLDGPLFKKR
I
>gnl|CDD|467499 cd01995, QueC-like, 7-cyano-7-deazaguanine synthase QueC and similar proteins. 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group
MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKEELEAAKLIAKLLGIEHKVIDLSFLGELGG
SSLTDEGEEVPDGEYDEESIPSTWVPNRNLIFLSIAAAYAESLGASAIVIGVNAEDASGYPDCRPEFVEA
MNSALNLGTATGVKVVAPLIGLSKAEIVKLGVELGVPLELTWSCYRGGEKHCGRCESCRLRKRAFEEA
>gnl|CDD|467500 cd01996, AANH_WbpG-like, Rhizobium leguminosarum WbpG protein and similar proteins. This subfamily includes Rhizobium leguminosarum WbpG and Campylobacter jejuni PseA proteins. They belong to the of adenine nucleotide alpha hydrolase (AANH) superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus
GKGKPYDCIIGVSGGKDSTYAAHKAKEKYGLRPLLVTVDAGWNSPEAVKNIEKLVRALGVDLITFVPNWK
EMRDLQRLAFKSNGDQDWPQDHGIFTSLYKMAVKFGIPLIIWGENPAEELGGPRSELGVSTDETRHGFLG
YKEKDLKFYGYPSVQELN
>gnl|CDD|467501 cd01997, GMP_synthase_C, C-terminal domain of GMP synthetase (glutamine-hydrolyzing). The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus
IKRTVGDKKVLCLVSGGVDSTVCAALLHKALGDERVIAVHIDNGLMRKNESEQVEEALKKLGVINLAKVD
ASKRFLKKLKGVTDPEEKRKIIGDTFIEVFDEVAKELNLDPDDVYLAQGTLYPDLIESASSLASSKADTI
KTHHNVGGLPRELLKGKLVEPLRDLFKDEVRELGRELGLPEELVWRHPFPGPGLAIRVLGEVTPEKLEIL
READAIVEEELREAGLYDKISQAFAVLLPIKSVGVQGDGRTYGYVVALRAVETEDFMTAEWARPPYEVLD
KISNRITNEVPGVNRVVYDITSKPPATIEWE
>gnl|CDD|467502 cd01998, MnmA_TRMU-like, MnmA/TRMU family 2-thiouridylases and similar proteins. This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group
KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDEDNEKGGCCSEEDIEDARRVADQLGIPLYVVDFS
EEYWERVFDPFLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNRGRYRLLRAV
DPNKDQSYFLSRLSQEQLSRTLFPLGHLTKSEVREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLP
EKLPGPIVDIDGKVLGEHKGLWFYTIGQRKGLGIAAGEPLYVVKKDPEKNIVVVGPGHPALFSDTLRASD
LNWISPEPPLEPLECEAKIRYRQPPVPCTVTPLDDGRLKVEFDEPQRAVTPGQAAVFYDGDEVLGGGII
>gnl|CDD|467503 cd01999, ASS, argininosuccinate_synthase (ASS). Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate. In humans, a defect in the ASS gene causes citrullinemia, a genetic disease characterized by severe vomiting spells and mental retardation. ASS is a homotetrameric enzyme of about 400 amino-acid residues. An arginine residue seems to be important for the enzyme's catalytic mechanism. The sequences of ASS from various prokaryotes, archaeabacteria and eukaryotes show significant similarity
KKVVLAYSGGLDTSVILKWLKEEYGYEVIAFTADLGQGDEEEEIEEKALKLGAVKVYVVDLREEFAEDYI
FPAIKANAIYEGRYPLGTALARPLIAKKLVEVAREEGATAVAHGCTGKGNDQVRFELAIKALAPDLKVIA
PWRDWNFLTRAEEIAYAKKHGIPVPVTKKKPYSIDENLWGRSYEGGDLEDPWNEPPEDAFEWTVSPEKAP
DEPEYVTIEFEKGVPVAVNGEKLDPVELIEKLNEIAGRHGVGRIDIVENRLVGIKSRGVYEAPGATLLIK
AHRDLEDLTLDREVLHFKDIVSRKYAELVYNGLWFDPLREALEAFIDKTQERVTGEVRLKLYKGNVIVVG
RESPNSLYSEELATYEEGDGFDQKDAEGFIKIHGLQ
>gnl|CDD|238958 cd02000, TPP_E1_PDC_ADC_BCADC, Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine)
LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKE
MLAELFGKETGPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNE
GDFHEALNFAALWKLPVIFVCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEA
VERARAGGGPTLIEAVTYRLGGHSTSDDPSRYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEA
EVKAEVEEAVEFA
>gnl|CDD|238959 cd02001, TPP_ComE_PpyrDC, Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors
RIAAIAEIIEASGDTPIVSTTGYASRELYDVQDRDGHFYMLGSMGLAGSIGLGLALGLSRKVIVVDGDGS
LLMNPGVLLTAGEFTPLNLILVVLDNRAYGSTGGQPTPSSNVNLEAWAAACGYLVLSAPLLGGLGSEFAG
LLATTGPTLLHAPIAPG
>gnl|CDD|238960 cd02002, TPP_BFDC, Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors
LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRGGGLGWGLPAAVGAALANPDRKV
VAIIGDGSFMYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENAPDGLDLLDPGIDFAA
IAKAFGVEAERVETPEELDEALREALAEGGPALIEVVV
>gnl|CDD|238961 cd02003, TPP_IolD, Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism
QTEVLGALNEAIGDDDVVINAAGSLPGDLHKLWRARTPGGYHLEYGYSCMGYEIAAGLGAKLAKPDREVY
VLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSFGTEFRDRDQESGQLDGALLP
VDFAANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVIKTDPKSMTPGYGSWWDVGVAEVSE
>gnl|CDD|238962 cd02004, TPP_BZL_OCoD_HPCL, Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity
PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVV
LVEGDGAFGFSGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGLPVTTLLPDTRYDLVAEAFGG
KGELVTTPEELKPALKRALASGKPALINVIID
>gnl|CDD|238963 cd02005, TPP_PDC_IPDC, Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors
PLTQARLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRR
VILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDGYTIERAIHGPEASYNDIANWNYTKLPEVFGGGGG
GLSFRVKTEGELDEALKDALFNRDKLSLIEVILPKDDAPEALK
>gnl|CDD|238964 cd02006, TPP_Gcl, Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors
THFDDVPIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVA
AADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAFDMDYQVNLAFENINSS
ELGGYGVDHVKVAEGLGCKAIRVTKPEELAAAFEQAKKLMAEHRVPVVVEAILERVTNISMG
>gnl|CDD|238965 cd02007, TPP_DXS, Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6)
GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYD
AFGTGHSSTSISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSIS
PNVGTPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVTKKGKGY
>gnl|CDD|238966 cd02008, TPP_IOR_alpha, Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA
PRPPGLCPGCPHRPSFYALRKAFKKDSIVSGDIGCYTLGALPPLNAIDTCTCMGASIGVAIGMAKASEDK
KVVAVIGDSTFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPTTVIDIEALVRAI
GVKRVVVVDPYDLKAIREELKEALAVPGVSVIIAKRPC
>gnl|CDD|238967 cd02009, TPP_SHCHC_synthase, Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity
LTEPALARALPDHLPEGSQLFVGNSMPIRDLDLFALPSDKTVRVFANRGASGIDGTLSTALGIALATDKP
TVLLTGDLSFLHDLNGLLLGKQEPLNLTIVVINNNGGGIFSLLPQASFEDEFERLFGTPQGLDFEHLAKA
YGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD
>gnl|CDD|238968 cd02010, TPP_ALS, Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity
PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVV
AVSGDGGFMMNSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKG
YRIESADDLLPVLERALAADGVHVIDCPVDYSENIRL
>gnl|CDD|238969 cd02011, TPP_PK, Thiamine pyrophosphate (TPP) family, Phosphoketolase (PK) subfamily, TPP-binding module; PK catalyzes the conversion of D-xylulose 5-phosphate and phosphate to acetyl phosphate, D-glyceraldehyde-3-phosphate and H2O. This enzyme requires divalent magnesium ions and TPP for activity
GPGHGGPAVLANLYLEGSYSEFYPEISQDEEGMRKLFKQFSFPGGIPSHAAPETPGSIHEGGELGYSLSH
AYGAVFDNPDLIVACVVGDGEAETGPLATSWHSNKFLNPATDGAVLPILHLNGYKISNPTILARISHEEL
EALFRGYGYEPYFVEGDDPETMHQAMAATLDWAIEEIKAIQKRAREGGDASRPRWPMIVLRTPKGWTGPK
EVDGKKLEGSFRSHQVP
>gnl|CDD|238970 cd02012, TPP_TK, Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity
NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALA
GYLPEEDLKTFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLLGFDYRVYVLLGDGELQ
EGSVWEAASFAGHYKLDNLIAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALE
EAKKSKGKPTLIIAKTIKGKGVPFMENTAKWHGKPLGEEEVELAK
>gnl|CDD|238971 cd02013, TPP_Xsc_like, Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity
GNPMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAP
DRPVVAIAGDGAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESESFAKIAE
ACGAKGITVDKPEDVGPALQKAIAMMAEGKTTVIEIVCDQELGDPFRRDALKKPVR
>gnl|CDD|238972 cd02014, TPP_POX, Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors
PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDR
QVIALSGDGGFAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMG
IKGIRVEDPDELEAALDEALAADGPVVIDVVTDPNEPP
>gnl|CDD|238973 cd02015, TPP_AHAS, Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD
IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKT
VICIDGDGSFQMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAY
GIKGLRVEKPEELEAALKEALASDGPVLLDVLVDPEENVLPMVPPG
>gnl|CDD|238974 cd02016, TPP_E1_OGDC_like, Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex (OGDC). OGDC catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA and carbon dioxide, a key reaction of the tricarboxylic acid cycle
FEQFLATKFPGQKRFGLEGAESLIPALDELIDRAAELGVEEVVIGMAHRGRLNVLANVLGKPLEQIFSEF
EGKSEFPEDDEGSGDVKYHLGYSSDRKTPSGKKVHLSLAPNPSHLEAVNPVVMGKTRAKQDYRGDGERDK
VLPILIHGDAAFAGQGVVYETLNLSNLPGYTTGGTIHIVVNNQIGFTTDPRDSRSSPYCTDVAKMIGAPI
FHVNGDDPEAVVRATRLALEYRQKFKKDVVIDLVCYRRHGHNELDEPSFTQPLMY
>gnl|CDD|238975 cd02017, TPP_E1_EcPDC_like, Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme
LEIERRIRSLIRWNAMAMVHRANKKDLGIGGHIATFASAATLYEVGFNHFFRARGEGGGGDLVYFQGHAS
PGIYARAFLEGRLTEEQLDNFRQEVGGGGLSSYPHPWLMPDFWEFPTVSMGLGPIQAIYQARFNRYLEDR
GLKDTSDQKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCNLQRLDGPVRGNGKIIQELEGIFRG
AGWNVIKVIWGSKWDELLAKDGGGALRQRMEETVDGDYQTLKAKDGAYVREHFFGKYPELKALVTDLSDE
DLWALNRGGHDPRKVYAAYKKAVEHKGKPTVILAKTIKGYGLGAAGEGRNHAHQVKKMTEDELKALRDRF
GIPVSDEQLEEGPYYKPPEGSEEIKYLHERRHALGG
>gnl|CDD|238976 cd02018, TPP_PFOR, Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) subfamily, TPP-binding module; PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. PFORs can be homodimeric, heterodimeric, or heterotetrameric, depending on the organism. These enzymes are dependent on TPP and a divalent metal cation as cofactors
LTEEHGACAGCGEVTAVRVVLAALPAPEDTVIANSTGCSSVYASTAPFNSWAVPWVNSLFEDANAVASGL
KRGLKARFPKDRELDKKKDVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPL
GADSKMAPAGKKEDKKDLVLIAATHGCVYVARLSPALKKHFLKVVKEAISRTDGPTFIHAYTPCITEWGI
GSGKSLELARKAVKSRMFPLFEYDPRE
>gnl|CDD|238977 cd02019, NK, Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate
IIAITGGSGSGKSTVAKKLAEQLGGRSVVVLDEIVILEGLYASYKSRDARIRDLADLKIYLDADLVIDA
>gnl|CDD|238978 cd02020, CMPK, Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor
IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTGGIRTEEVGKLASEVAAIPEVRKALDERQRELAKKPGIVL
EGRDIGTVVFPDADLKIFLTASPEVRAKRRAKQLQAKGEGVDLEEILAEIIERDERDSTRYVAPLKLAED
AIVIDTS
>gnl|CDD|238979 cd02021, GntK, Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits
IIVVMGVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAKLAS
AGEGVVVACSALKRIYRDILRGGAANPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPGE
DEEDVIVIDV
>gnl|CDD|238980 cd02022, DPCK, Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis
IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEI
VFADPEKRKKLEAITHPLIRKEIEEQLAEARKEKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLM
KRDGLSEEEAEARIASQMPLEEKRARADFVIDNSGSLEE
>gnl|CDD|238981 cd02023, UMPK, Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK), catalyzes the reversible phosphoryl transfer from ATP to uridine or cytidine to yield UMP or CMP. In the primidine nucleotide-salvage pathway, this enzyme combined with nucleoside diphosphate kinases further phosphorylates UMP and CMP to form UTP and CTP. This kinase also catalyzes the phosphorylation of several cytotoxic ribonucleoside analogs such as 5-flurrouridine and cyclopentenyl-cytidine
IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQD
LKNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERD
IVERGRDLESVINQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK
>gnl|CDD|238982 cd02024, NRK1, Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide adenine dinucleotide (NAD+). This enzyme catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN). It defines the NR salvage pathway of NAD+ biosynthesis in addition to the pathways through nicotinic acid mononucleotide (NaMN). This enzyme can also phosphorylate the anticancer drug tiazofurin, which is an analog of nicotinamide riboside
IVGISGVTNSGKTTLAKLLQRILPNCCVIHQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWR
ETGHFPKFLRSHGNENDPEKEFIEDAQIEETKADLLGAEDLHILIVDGFLLYNYKPLVDLFDIRYFLRVP
YETCKRRREARTGYVTLEGFWPDPPGYFDGHVWPMYLKHHAEMFENG
>gnl|CDD|238983 cd02025, PanK, Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4'-phosphopantothenic, which is the first of five steps in coenzyme A (CoA) biosynthetic pathway. The reaction carried out by this enzyme is a key regulatory point in CoA biosynthesis
IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKF
LKDIKSGKKNVKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNPRLFVSDFFDFSIYVDADED
DIEKWYIKRFLKLRETAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKG
ADHSIEEVYL
>gnl|CDD|238984 cd02026, PRK, Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. This enzyme catalyzes the phosphorylation of D-ribulose 5-phosphate to form D-ribulose 1, 5-biphosphate, using ATP and NADPH produced by the primary reactions of photosynthesis
IIGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDYHSLDRKGRKETGITALDPRANNFDLMYEQLKALK
EGQAIEKPIYNHVTGLIDPPELIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAE
RGHSLEDVLASIEARKPDFEAYIDPQKQYADVVIQVLPTQLIPDDTEGKVLRVRLIQKEGVKDFVPVYLF
DEGSTISWIPCGRKLTCSYPGIKLAYGPDTYYGREVSVLEMDGQFDNLEELIYVESHLSNTST
>gnl|CDD|238985 cd02027, APSK, Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate
VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADA
GLIVIAAFISPYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAP
ENPDLVLDT
>gnl|CDD|238986 cd02028, UMPK_like, Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK)
VVGIAGPSGSGKTTFAKKLSNQLRVNGIGPVVISLDDYYVPRKTPRDEDGNYDFESILDLDLLNKNLHDL
LNGKEVELPIYDFRTGKRRGYRKLKLPPSGVVILEGIYALNERLRSLLDIRVAVSGGVHLNRLLRRVVRD
IQFRGYSAELTILMWPSVPSGEEFIIPPLQEAAIVMFNS
>gnl|CDD|238987 cd02029, PRK_like, Phosphoribulokinase-like (PRK-like) is a family of proteins similar to phosphoribulokinase (PRK), the enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. PRK catalyzes the phosphorylation of D-ribulose 5-phosphate to form D-ribulose 1, 5-biphosphate, using ATP and NADPH produced by the primary reactions of photosynthesis
VIAVTGSSGAGTTTVKRAFEHIFAREGIHPAVVEGDSFHRYERMEMKMAIAEALDAGRNFSHFGPEANLF
DLLEELFRTYGETGRGRSRYYLHSDEEAAPFNQEPGTFTPWEDLPEDTDLLFYEGLHGGVVTEGYNVAQH
ADLLVGVVPIINLEWIQKIHRDTAERGYSAEAVMDTILRRMPDYINYICPQFSRTDINFQRVPTVDTSNP
FIARDIPTADESFVVIHFRKPWGIDFPYLLNMLHDSFMSRPNTIVVPGGKMGLAMELILTPIIHRLM
>gnl|CDD|238988 cd02030, NDUO42, NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar to deoxyribonucleoside kinases (dNK). Members of this family have been identified as one of the subunits of NADH:Ubiquinone oxioreductase (complex I), a multi-protein complex located in the inner mitochondrial membrane. The main function of the complex is to transport electrons from NADH to ubiquinone, which is accompanied by the translocation of protons from the mitochondrial matrix to the inter membrane space
VITVDGNIASGKGKLAKELAEKLGMKYFPEAGIHYLDSTTGDGKPLDPAFNGNCSLEKFYDDPKSNDGNS
YRLQSWMYSSRLLQYSDALEHLLSTGQGVVLERSPFSDFVFLEAMYKQGYIRKQCVDHYNEVKGNTIPEL
LPPHLVIYLDVPVPEVQKRIKKRGDPHEMKVTSAYLQDIENAYKKTFLPEISEHSEVLQYDWTEAGDTEK
VVEDIEYLK
>gnl|CDD|349752 cd02032, Bchl-like, L-subunit of protochlorophyllide reductase. This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen
LVIAVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLTGFLIPTVIDVLQSVDFHYEEVWP
EDVIFTGYGGVDCVEAGGPPAGTGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYAD
YCLIVTANDFDSLFAANRIAAAVREKAKTYPVRLAGIIGNRTDKTDLIDKFVEAVPMPVLEVLPLIEDIR
RSRVKGKTLFEMEESEPELNYVCDEYLNIADQLLSDPEGVVPKPLPDREIFDLLGDF
>gnl|CDD|349753 cd02033, BchX, X-subunit of protochlorophyllide reductase. Chlorophyllide reductase converts chlorophylls into bacteriochlorophylls by reducing the chlorin B-ring. This family contains the X subunit of this three-subunit enzyme. Sequence and structure similarity between bchX, protochlorophyllide reductase L subunit (bchL and chlL) and nitrogenase Fe protein (nifH gene) suggest their functional similarity. Members of the BchX family serve as the unique electron donors to their respective catalytic subunits (bchN-bchB, bchY-bchZ and nitrogenase component 1). Mechanistically, they hydrolyze ATP and transfer electrons through a Fe4-S4 cluster
PNLKSFDARLRDEAAIEPSLEIPTGPPTKETQIIAIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPK
SDTTSLLFGGKACPTIIETSTRKKLAGEEVKIGDVCFKRGGVFAMELGGPEVGRGCGGRGIIHGFELLEK
LGFHDWGFDYVLLDFLGDVVCGGFGLPIARDMCQKVIVVGSNDLQSLYVANNVCSAVEYFRKLGGNVGVA
GIVINKDDGTGEAQAFAKAAGIPVLAAIPADEDIRRKSANYQIVGRPETQWGPLFAELATNVAEAPPMRP
TPLSQDELLGLFSSEETGRDVVLVPATDEDMRGKDAVPKPSLEVVYDDV
>gnl|CDD|349754 cd02034, CooC1, accessory protein CooC1. The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function
MKIAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKLPLIKTIGDIRERTGAKK
GEPPEGMSLNPYVDDIIKEIIVEPDGIDLLVMGRPEGGGSGCYCPVNALLRELLRHLALKNYEYVVIDME
AGIEHLSRGTIRAVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVRNEEEQELIEELLIKLK
LIGVIPYDEEIMEADLKGKPLFDLDSAAVKAIEKIVEKL
>gnl|CDD|349755 cd02035, ArsA, Arsenical pump-driving ATPase ArsA. ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence
RIIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKLGGETPVKGAPNLWAMEIDPE
EALEEYWEEVKELLAQYLRLPGLDEVYAEELLSLPGMDEAAAFDELREYVESGEYDVIVFDTAPTGHTLR
LLSLPLEQVRELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLPEEADDSFFLRR
RRQQQKYLDEIEELFEPLPVVEVPLLPEEVRGLEALRALA
>gnl|CDD|349756 cd02036, MinD, septum site-determining protein MinD. Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein
RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQ
ALIKDKRWENLYLLPASQTRDKDALTPEKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVT
NPEISSVRDADRVIGLLESKGIVNIGLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVAT
NRGEPLVLYKPNSLAAKAFENIARRL
>gnl|CDD|349757 cd02037, Mrp_NBP35, Mrp/NBP35 ATP-binding protein family. Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase
HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVGGI
KVMSIGFLLPEDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPIDGAVVVTT
PQEVSLIDVRKAIDMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPE
LAK
>gnl|CDD|349758 cd02038, FlhG-like, MinD-like ATPase FlhG. FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly
RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLEDII
VEGPEGLDIIPGGSGMEELANLDPEQKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIVVT
TPEPTSITDAYALIKVLSRRGGKKNFRLIVNMARSPKEGRATFERLKKVAKRFLDINLDFVGFIPYDQSV
RRAVRSQKPFVLLFPNSKAS
>gnl|CDD|185678 cd02039, cytidylyltransferase_like, Cytidylyltransferase-like domain. Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown
VGIIIGRFEPFHLGHLKLIKEALEEALDEVIIIIVSNPPKKKRNKDPFSLHERVEMLKEILKDRLKVVPV
DFPEVKILLAVVFILKILLKVGPDKVVVGEDFAFGKNASYNKDLKELFLDIEIVEVPRVRDGKKISSTLI
REL
>gnl|CDD|349759 cd02040, NifH, nitrogenase component II NifH. NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia
RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKAIPTVLDTLREKGEVEELED
VIKEGFNGIKCVESGGPEPGVGCAGRGIITAINLLEELGAYEEDLDVVFYDVLGDVVCGGFAMPIREGYA
DEVYIVTSGEMMALYAANNIAKGIVKYAERGGVRLGGLICNSRNVDREEELVEEFAERLGTQIIHFVPRS
NEVQEAELRGKTVIEYDPDSEQADEYRELAKKILENKKLVIPKPLTMEELEELLM
>gnl|CDD|349760 cd02042, ParAB_family, partition proteins ParAB family. ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition
KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWLYDYILIDTPPSLGLLTRNALAAA
DLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK
>gnl|CDD|381001 cd02043, serpinP_plants, serpin family P, plant serpins. Plant SERine Proteinase INhibitors (serpins) are potent inhibitors of a range of mammalian serine proteases in vitro, and at least seven serpin genes are expressed in Arabidopsis. Serpins from plants display a wide range of functions including protection of storage protein degradation by exogenous proteases and seed survival within the herbivore digestive tract. Comparison between Arabidopsis AtSerpin1 and other serpins reveals several distinguishing features including a plant-specific insertion between s2B and s3B, with a plant-specific motif YXXGXDXRXF and the presence of a beta-bulge in strand s2C. The conserved Asp-230 and Arg-232 in the motif form a network of hydrogen bonds stabilize a loop region, which is otherwise disordered in many other serpin structures. AtSerpin1 is targeted to the secretory pathway and was shown to interact with cysteine protease RD21 (RESPONSIVE TO DESICCATION-21). RD21 accepts peptides and ligates them to the N termini of acceptor proteins so it has been proposed that AtSerpin1 functions to curb this activity. This subgroup corresponds to clade P of the serpin superfamily. In general, serpins exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
SNQTDVALRLAKHLLSTEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSESIDDLNSLASQLV
SSVLADGSSSGGPRLSFANGVWVDKSLSLKPSFKELAANVYKAEARSVDFQTKAEEVRKEVNSWVEKATN
GLIKEILPPGSVDSDTRLVLANALYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDQYIASFDG
FKVLKLPYKQGQDDRRRFSMYIFLPDAKDGLPDLVEKLASEPGFLDRHLPLRKVKVGEFRIPKFKISFGF
EASDVLKELGLVLPFSPGAADLMMVDSPPGEPLFVSSIFHKAFIEVNEEGTEAAAATAVLIAGGSAPPPP
PPIDFVADHPFLFLIREEVSGVVLFVGHVLNP
>gnl|CDD|381002 cd02045, serpinC1_AT3, serpin family C member 1, antithrombin III. Antithrombin III (AT3/ATIII) is a non-vitamin K-dependent serine protease that inhibits coagulation by neutralizing the enzymatic activity of thrombin (factors IIa, IXa, Xa). It is the most important anticoagulant molecule in mammalian circulation systems, controlled by its interaction with the cofactor, heparin, which accelerates its interaction with target proteases. This subgroup corresponds to clade C of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
QKIPEATNPRVWELSKANSRFATTFYQHLADSKNNNENIFLSPLSISTAFAMTKLGACNDTLQQLMEVFK
FDTISEKTSDQIHFFFAKLNCRLYRKANKSSELVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKE
KPEQSRAAINKWVSNKTEGRITDVIPEEAINELTVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESC
SVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLILPKPEKSLAKVEKELTPEKLQEWLDELEETML
VVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIVAGGRDDLYVSDAFHKAFLEVNEEGSEAAAST
AVVIAGRSLNPNRVTFKANRPFLVFIREVPINTIIFMGRVANPCV
>gnl|CDD|381003 cd02046, serpinH1_CBP1, serpin family H member 1, collagen-binding protein 1. Collagen-binding protein 1 (CBP1, also called heat shock protein 47/hsp47 or colligin), because of its collagen binding ability, is a chaperone specific protein for the correct folding of types I-V procollagen in the endoplasmic reticulum (ER). It is induced under stress conditions through heat shock element-heat shock factor interaction and has been shown to be essential for collagen biosynthesis. Hsp47 transiently binds to procollagen in the ER, dissociates in the cis-Golgi or ER-Golgi intermediate compartment, and is then transported back to the ER via its RDEL retention sequence. Hsp47 recognizes collagenous (Gly-Xaa-Arg) repeats on triple-helical procollagen and can prevent local unfolding and/or aggregate formation of procollagen. Hsp47 is a non-inhibitory member of the SERPIN superfamily and corresponds to clade H. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
LSPKAATLAERSAGLAFSLYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSAEKLRDE
EVHAGLGELLRSLSNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINE
WAAQTTDGKLPEVTKDVERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNY
YDDEKEKLQIVEMPLAHKLSSLIILMPHHVEPLERLEKLLTKEQLKTWMGKMQKKAVAISLPKGVVEVTH
DLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFEWDTEGNPFDQDIYGREELRSPKLFYAD
HPFIFLVRDTQSGSLLFIGRLVRPKGDKMRDE
>gnl|CDD|381004 cd02047, serpinD1_HCF2, serpin family D member 1, Heparin cofactor II. Heparin cofactor II (HCF2/HC-II, also called protease inhibitor leuserpin-2/hLS2) is a protein encoded by the SERPIND1 gene that inhibits thrombin, the final protease of the coagulation cascade. HCII is allosterically activated by binding to cell surface glycosaminoglycans (GAGs). The specificity of HCII for thrombin is conferred by a highly acidic hirudin-like N-terminal tail, which becomes available after GAG binding for interaction with the anion-binding exosite I of thrombin. HCII deficiency can lead to increased thrombin generation and a hypercoagulable state. This subgroup corresponds to clade D of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
SMPLLPGDFHKENTVTNDLIPEGEEEEDYLDFDKILGEDDDYIDEIDAIPPDLADSETSRGNILQLFHGK
TRIQRLNIVNADFAFNLYRSLKNSTNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFKDFVNAS
SKYEISTVHNLFRKLTHRLFRRNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSDPAFIT
KANQRILKLTKGLIKEALENVDPATLMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKG
NFLAAADHELDCDILQLPYVGNISMLIVVPHKLSGMKTLEAQLTPQVVEKWQKSMTNRTREVLLPKFKLE
KNYDLIEVLKEMGVTDLFTANGDFSGISDKDIIIDLFKHQGTITVNEEGTEAAAVTTVGFMPLSTQNRFT
VDRPFLFLIYEHRTSCLLFMGRVANPAKS
>gnl|CDD|381005 cd02048, serpinI1_NSP, serpin family I member 1, neuroserpin. Neuroserpin (NSP, also called proteinase inhibitor 12/PI-12) is an inhibitory member of the serpin family that reacts preferentially with tissue-type plasminogen activator (tPA). It is located in neurons in regions of the brain where tPA is also found, suggesting that neuroserpin is the selective inhibitor of tPA in the central nervous system (CNS). This subgroup corresponds to clade I of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
DEAIAEFSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKNGEEFSFLKD
FSNMVTAKESQYVMKIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVANYINKWVENHTNNL
IKDLVSPRDFDALTYLALINAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGS
NEAGGIYQVLEIPYEGDEISMMIVLSRQEVPLATLEPLVKAQLIEEWANSVKKQKVEVYLPRFTVEQEID
LKDVLKALGITEIFIKDADLTAMSDNKELFLSKAVHKSFLEVNEEGSEAAAVSGMIAISRMAVLYPQVIV
DHPFFFLIRNRKTGTILFMGRV
>gnl|CDD|381006 cd02050, serpinG1_C1-INH, serpin family G member 1, plasma proteinase C1 inhibitor. Plasma proteinase C1 inhibitor (C1-INH/C1IN) is a protease inhibitor of the serpin family. It plays a pivotal role in regulating the activation of the classical complement pathway and of the contact system, via regulating bradykinin formation, inhibiting factor XII and kallikrein of the contact system, and via acting on factor XI in the coagulation cascade. This subgroup corresponds to clade G of the serpin superfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
RSDEAVLGEALTDFSLKLYSALSQSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSYPKDFTCV
HSALKGLKKKLALTSASQIFYSPDLKLRETFVNQSRTFYDSRPQVLSNNSEANLEMINSWVAKKTNNKIK
RLLDSLPSDTQLVLLNAVYFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMMYSKKYPVAHFYDPNLKAKV
GRLQLSHNLSLVILLPQSLKHDLQDVEQKLTDSVFKAMMEKLEGSKPQPTEVTLPKIKLDSSQDMLSILE
KLGLFDLFYDANLCGLYEDEDLQVSAAQHRAVLELTEEGVEAAAATAISFARSALSFEVQQPFLFLLWSD
QAKFPLFMGRVY
>gnl|CDD|381007 cd02051, serpinE1_PAI-1, serpin family E member 1, plasminogen activator inhibitor-1. Plasminogen activator inhibitor-1 (PAI-1/PLANH1, also called endothelial PAI) is the primary, fast-acting inhibitor of plasminogen activators. It is often bound to vitronectin, an abundant component of the extracellular matrix in many tissues. PAI1 deficiency is a rare bleeding disorder that causes excessive or prolonged bleeding due to blood clots being broken down too early. PAI-1 is a member of the serpin superfamily and belongs to clade E. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
SYVAELATDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQEKGMAPAL
RHLQKDLMGPWNKDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTK
GMISDFLGSGALDQLTRLVLLNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFTT
PDGVDYDVIELPYEGETLSMLIAAPFEKEVPLSALTNILSAQLISQWKQNMRRVTRLLVLPKFSLESEVD
LKKPLENLGMTDMFRQFKADFTRLSDQEPLCVSKALQKVKIEVNESGTKASSATAAIVYARMAPEEIILD
RPFLFVVRHNPTGAVLFMGQVMEP
>gnl|CDD|381008 cd02052, serpinF1_PEDF, serpin family F member 1, Pigment epithelium-derived factor (PEDF). Pigment epithelium-derived factor (PEDF, also called capsin or EPC-1) is an extracellular component of the retinal interphotoreceptor matrix, vitreous humor, and aqueous humor of the adult eye. PEDF is non-inhibitory member of the serpin superfamily. It exhibits neurotrophic, neuroprotective and antiangiogenic properties and is widely expressed in the developing and adult nervous systems. This subgroup corresponds to clade F1 of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
EEEDPFFKSPVNRLAAAVSNFGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYY
DLLNDPDIHATYKELLASLTAPRKSLKSASRIYLEKKLRIKSDFLNQVEKSYGARPRILTGNPRLDLQEI
NNWVQQQTEGKIARFVKELPEEVSLLLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPNYP
LRYGLDSDLNCKIAQLPLTGGVSLLFFLPDEVTQNLTLIEESLTSEFIHDLVRELQTVKAVLTLPKLKLS
YEGELKQSLQEMRLQSLFTSPDLSKITSKPLKLSQVQHRATLELNEEGAKTTPATGSAPRQLTFPLEYHV
DRPFLFVLRDDDTGALLFIGKVL
>gnl|CDD|381009 cd02053, serpinF2_A2AP, serpin family F member 2, alpha2-antiplasmin inhibitor. Alpha2-antiplasmin inhibitor (A2AP/API, also called plasmin inhibitor/PLI or alpha-2-antiplasmin) is the primary inhibitor of plasmin, a proteinase that digests fibrin, the main component of blood clots. Alpha2AP forms an inactive 1:1 stoichiometric complex with plasmin. It also rapidly crosslinks to fibrin during blood clotting by activated coagulation factor XIII, and as a consequence fibrin becomes more resistant to fibrinolysis. Therefore alpha2AP is important in modulating the effectiveness and persistence of fibrin with respect to its susceptibility to digestion and removal by plasmin. This subgroup corresponds to clade F2 of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
SPEEMRALGDAIMKFGLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHADSLPCL
HHALRRLLKELGKSALSVASRIYLKKGFEIKKDFLEESEKLYGSKPVTLTGNSEEDLAEINKWVEEATNG
KITEFLSSLPPNVVLLLLNAVHFKGFWKTKFDPSLTSKDLFYLDDEFSVPVDMMKAPKYPLSWFTDEELD
AQVARFPFKGNMSFVVVMPTSGEWNVSQVLANLNISDLYSRFPKERPTQVKLPKLKLDYSLELNEALTQL
GLGELFSGPDLSGISDGPLFVSSVQHQSTLELNEEGVEAAAATSVAMSRSLSSFSVNRPFFFAIMDDTTG
VPLFLGSVTNPNP
>gnl|CDD|381010 cd02054, serpinA8_AGT, serpin family A member 8, angiotensinogen. Angiotensinogen (AGT) is part of the renin-angiotensin system (RAS), which plays an important role in blood pressure regulation, renal hemodynamics, as well as fluid and electrolyte homeostasis. It is also involved in normal and abnormal growth processes. The growth promoting actions of angiotensin have been shown in a variety of cells and tissues. This subgroup represents clade A8 of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
YIHPFHLFAHNNSTCEQLQKQNAGKPKDPTFIPPPIQAKTSPVDEKTLDDQLVLAAEKLRDEDTQRAAVV
AMLANFLGFRMYGMLSELWGVHTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPWKSEDCTSRLDG
HKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGTFTAPGLDLKQPFVQGLADFTPASFPRSLDFTEPEVA
EEKINRFIQAVTGWKMKSSLKGVSPDSTLLFNTYVHFQGKMRGFSQLTSPQEFWVDNSTSVSVPMMSGTG
TFQHWSDAQDNFSVTQVPLSERATLLLIQPHEASDLDKVEALLFQNNILTWIKNLSPRTIELTLPQLSLS
GSYDLQDLLAQMKLPALLGTEANLQKSSKENFRVGEVLNSIVFELSAGEREVQESTEQGNKPEVLKVTLN
RPFLFAVYEQNSNALHFLGRVTNPTS
>gnl|CDD|381011 cd02055, serpinA10_PZI, serpin family A member 10, protein Z-dependent protease inhibitor. Protein Z-dependent protease inhibitor (ZPI) is a member of the serpin superfamily of proteinase inhibitors (clade A10). ZPI inhibits coagulation factor Xa, dependent on protein Z (PZ), a vitamin K-dependent plasma protein. ZPI also inhibits factor XIa in a process that does not require PZ. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
QQQTLTPAVQDLSNRNSDFGFNLYRKIASRHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQAL
DRDLDPDLLPDLFQQLRENITQNGELSLDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDFSNTSQAK
DTINQYIRKKTGGKIPDLVDEIDPQTKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRA
DKFALAYDKSLKCGVLKLPYRGGAAMLVVLPDEDVDYTALEDELTAELIEGWLRQLKKTKLEVQLPKFKL
EQSYSLHELLPQLGITQVFQDSADLSGLSGERGLKVSEVLHKAVIEVDERGTEAAAATGSEITAYSLPPR
LTVNRPFIFIIYHETTKSLLFMGRVVDPTK
>gnl|CDD|381012 cd02056, serpinA1_A1AT, serpin family A member 1, alpha-1-antitrypsin. Alpha-1-antitrypsin (also called A1AT, A1A, AAT, alpha1-proteinase inhibitor/A1PI, alpha1-antiproteinase/A1AP, proteinase inhibitor/PI, and serum trypsin inhibitor) is a protease inhibitor that belongs to the serpin superfamily. It is encoded in humans by the SERPINA1 gene. When the blood contains inadequate amounts of A1AT or functionally defective A1AT (such as in alpha-1 antitrypsin deficiency), neutrophil elastase is excessively free to break down elastin, degrading the elasticity of the lungs, which results in respiratory complications, such as chronic obstructive pulmonary disease. Normally, A1AT leaves its site of origin, the liver, and joins the systemic circulation; defective A1AT fails to do so, building up in the liver, which results in cirrhosis. This family contains other A1AT-like members of clade A of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
IAPNLAEFAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLTEIAEADIHKG
FQHLLQTLNRPDSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGT
QGKIVDLVKELDRDTVFALVNYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTL
SSWVLLMDYLGNATAIFLLPDEGKMQHLEDTLTKEIISKFLENRERRSANLHLPKLSISGTYDLKTVLGS
LGITKVFSNGADLSGITEEAPLKLSKALHKAVLTIDEKGTEAAGATVLEAIPMSLPPEVKFNKPFLFLIY
EHNTKSPLFVGKVVNPTQ
>gnl|CDD|381013 cd02057, serpinB5_maspin, serpin family B member 5, mammary serine proteinase inhibitor. Mammary serine proteinase inhibitor (maspin, also known as proteinase inhibitor 5/PI5), a member of the serpin superfamily, is related to the ov-serpins, with a multitude of effects on cells and tissues at an assortment of developmental stages. Maspin has tumor suppressing activity against breast and prostate cancer. All true inhibitory serpins rely on an exposed reactive center loop (RCL) to inhibit their target proteinase, in which the proteinase cleaves the RCL and becomes incorporated into a serpin-proteinase complex. Maspin differs from other serpins in that its RCL is necessary for activity, but it is not cleaved or rearranged. The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
MDALRLANSAFAVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVKDVPFGF
QTVTSDVNKLSSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDKLEETKGQINSSIKDLT
DGHFENILAENSVNDQTKILVVNAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNID
EINCKIIELPFQNKHLSMLILLPKDVEDESTGLEKIEKQLNSESLAQWTNPSTMANAKVKLSLPKFKVEK
MIDPKASLESLGLKDAFNEETSDFSGMSETKGVSLSNVIHKVCLEITEDGGESIEVPGARILQHKDEFNA
DHPFIYIIRHNKTRNIIFFGKFCSP
>gnl|CDD|381014 cd02058, serpinB_MENT-like, serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and similar proteins. Gallus gallus Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) is a nonhistone heterochromatin-associated serpin that is an effective inhibitor of cathepsin L as well as the papain-like cysteine proteases cathepsins K, L, and V in vitro. It's reactive center loop, which is essential for chromatin bridging, is able to mediate formation of a loop-sheet oligomer. It also contains an M-loop which contains two critical functional motifs: a classical nuclear localization signal (NLS) that is required for nuclear import and an AT-hook motif that is involved in chromatin and DNA binding. MENT belongs to the clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
EQVSASINNFTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQAVRAESSSV
ARPSRGRPKRRRMDPEHEQAENIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYK
AEPQAVNFKTAPEQSRKEINTWVEKQTESKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQ
PFRLSKTKTKPVKMMFMRDTFPMFIMEKMNFKMIELPYVKRELSMFILLPDDIKDNTTGLEQLERELTYE
RLSEWADSKMMMETEVELHLPKFSLEENYDLRSTLSNMGMTTAFTPNKADFRGISDKKDLAISKVIHKSF
VAVNEEGTEAAAATAVIISFRTSVIVLKFKADHPFLFFIRHNKTKTILFFGRFCSP
>gnl|CDD|381015 cd02059, serpinB14_OVA, serpin family B member 14, ovalbumin. The chicken protein ovalbumin (OVA3), a storage protein from egg white, lacking a loop insertion mechanism and therefore protease inhibitory activity, is a historical member of the serpin superfamily and the founding member of the subgroup known as ov-serpins (ovalbumin-related serpins). It has several modifications, including N-terminal acetylation, phosphorylation, and glycosylation. Ovalbumin is secreted from the cell, targeted by an internal signal sequence, rather than the N-terminal signal sequence commonly found in other secreted proteins. The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
GSIGAASMEFCFDVFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDKLPGFGDSIE
AQCGTSVNVHSSLRDILNQITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAADQ
ARELINSWVESQTNGIIRNVLQPSSVDSQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQM
MYQIGSFKVASMASEKMKILELPFASGTMSMLVLLPDEVSGLEQLESTISFEKLTEWTSSNVMEERKIKV
YLPRMKMEEKYNLTSVLMAMGITDLFSSSANLSGISSAESLKISQAVHAAHAEINEAGREVVGSAEAGVD
AASVSEEFRADHPFLFCIKHNPTNAILFFGRCVSP
>gnl|CDD|380311 cd02062, Nitro_FMN_reductase, nitroreductase family protein. Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase
IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAKLAAPNQKFIAGAPVV
IVVVADPDKSRPWALEDAGAAAQNLLLAAAALGLGSCWIGGFDFREDKVRELLGIPENLRPVALIAIGY
>gnl|CDD|185679 cd02064, FAD_synthetase_N, FAD synthetase, N-terminal domain of the bifunctional enzyme. FAD synthetase_N. N-terminal domain of the bifunctional riboflavin biosynthesis protein riboflavin kinase/FAD synthetase. These enzymes have both ATP:riboflavin 5'-phosphotransferase and ATP:FMN-adenylyltransferase activities. The N-terminal domain is believed to play a role in the adenylylation reaction of FAD synthetases. The C-terminal domain is thought to have kinase activity. FAD synthetase is present among all kingdoms of life. However, the bifunctional enzyme is not found in mammals, which use separate enzymes for FMN and FAD formation
TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGV
DYLLVLPFDKEFASLSAEEFVEDLLVKLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVT
LDGERVSSTRIREALAEGDVELANELLGRPYSIEGRVVHG
>gnl|CDD|239016 cd02065, B12-binding_like, B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 (adenosylcobamide) or methylcobalamin or methyl-Co(III) 5-hydroxybenzimidazolylcobamide. This domain is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. Cobalamin undergoes a conformational change on binding the protein; the dimethylbenzimidazole group, which is coordinated to the cobalt in the free cofactor, moves away from the corrin and is replaced by a histidine contributed by the protein. The sequence Asp-X-His-X-X-Gly, which contains this histidine ligand, is conserved in many cobalamin-binding proteins. Not all members of this family contain the conserved binding motif
KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLV
IEALKELGIDIPVVVGGAHPTADPEEPKVDAVVIGEGEYAGPALLEVEGIAYRKN
>gnl|CDD|239017 cd02066, GRX_family, Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -_ GSH reductase -_ GSH -_ GRX -_ protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family
KVVVFSKSTCPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWPTVPQIFINGEFIGGYDDLKAL
HE
>gnl|CDD|239018 cd02067, B12-binding, B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 (adenosylcobamide) or methylcobalamin or methyl-Co(III) 5-hydroxybenzimidazolylcobamide, it is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. Cobalamin undergoes a conformational change on binding the protein; the dimethylbenzimidazole group, which is coordinated to the cobalt in the free cofactor, moves away from the corrin and is replaced by a histidine contributed by the protein. The sequence Asp-X-His-X-X-Gly, which contains this histidine ligand, is conserved in many cobalamin-binding proteins
KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEV
IEELKEAGLDDIPVLVGGAIVTRDFKFLKEIGVDAYFGPATEAVEVLKK
>gnl|CDD|239019 cd02068, radical_SAM_B12_BD, B12 binding domain_like associated with radical SAM domain. This domain shows similarity with B12 (adenosylcobamide) binding domains found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase, but it lacks the signature motif Asp-X-His-X-X-Gly, which contains the histidine that acts as a cobalt ligand. The function of this domain remains unclear
PPLGLAYLAAVLEDAGFIVAEHDVLSADDIVEDIKELLKPDVVGISLMTSAIYEALELAKIAKEVLPNVI
VVVGGPHATFFPEEILEEPGVDFVVIGEGEETFLKLLEELEEGEDLSEVPGIAYRDG
>gnl|CDD|239020 cd02069, methionine_synthase_B12_BD, B12 binding domain of methionine synthase. This domain binds methylcobalamin, which it uses as an intermediate methyl carrier from methyltetrahydrofolate (CH3H4folate) to homocysteine (Hcy)
VEERLKHALVKGIRDGIEEDTEEARQQYARPLEIINGPLMDGMKVVGDLFGAGKMFLPQVLKSARVMKAA
VAYLEPYMEKEKGENSSKGKIVLATVKGDVHDIGKNLVGVILSNNGYEVIDLGVMVPIEKILEAAKEHKA
DIIGLSGLLVPSLDEMVEVAEEMNRRGIKIPLLIGGAATSRKHTAVKIAPEYDGPVVYVKDASRALGVAN
KLL
>gnl|CDD|239021 cd02070, corrinoid_protein_B12-BD, B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins that bind methyl-Co(III) 5-hydroxybenzimidazolylcobamide as a cofactor. They play a role on the methanogenesis from trimethylamine, dimethylamine or monomethylamine, which is initiated by a series of corrinoid-dependent methyltransferases
LADAIVDGDEEETVELVKKALEAGIDPQDIIEEGLAPGMDIVGDKYEEGEIFVPELLMAADAMKAGLDLL
KPLLGKSKSAKKGKVVIGTVEGDIHDIGKNLVATMLEANGFEVIDLGRDVPPEEFVEAVKEHKPDILGLS
ALMTTTMGGMKEVIEALKEAGLRDKVKVMVGGAPVNQEFADEIGADGYAEDAAEAVAIAKE
>gnl|CDD|239022 cd02071, MM_CoA_mut_B12_BD, methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), which initiates the conversion of succinyl CoA and methylmalonyl CoA by forming an adenosyl radical, which then undergoes a rearrangement exchanging a hydrogen atom with a group attached to a neighboring carbon atom. This family is present in both mammals and bacteria. Bacterial members are heterodimers and involved in the fermentation of pyruvate to propionate. Mammalian members are homodimers and responsible for the conversion of odd-chain fatty acids and branched-chain amino acids via propionyl CoA to succinyl CoA for further degradation
RILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEV
IELLRELGAGDILVVGGGIIPPEDYELLKEMGVAEIFGPGTSIEEIIDKIRD
>gnl|CDD|239023 cd02072, Glm_B12_BD, B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S)-glutamate with (2S,3S)-3-methylaspartate. The rearrangement reaction is initiated by the extraction of a hydrogen from the protein-bound substrate by a 5'-desoxyadenosyl radical, which is generated by the homolytic cleavage of the organometallic bond of the cofactor B12. Glm is a heterotetrameric molecule consisting of two alpha and two epsilon polypeptide chains
TIVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSLYGHGEIDCKGL
REKCDEAGLKDILLYVGGNLVVGKQDFEDVEKRFKEMGFDRVFAPGTPPEEAIADLKK
>gnl|CDD|319770 cd02073, P-type_ATPase_APLT_Dnf-like, Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2, -10D, -11B, -11C. Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. This subfamily includes mammalian flippases such as ATP11C which may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIPGISPTGPYTTLLPLLFVLGVTAIKEGYED
IRRHKSDNEVNNRPVQVLRGGKFVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDG
ETNLKIRQALPETALLLSEEDLARFSGEIECEQPNNDLYTFNGTLELNGGRELPLSPDNLLLRGCTLRNT
EWVYGVVVYTGHETKLMLNSGGTPLKRSSIEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHGRDLWYL
LPKEERSPALEFFFDFLTFIILYNNLIPISLYVTIEVVKFLQSFFINWDLDMYDEETDTPAEARTSNLNE
ELGQVEYIFSDKTGTLTENIMEFKKCSINGVDYGFFLALALCHTVVPEKDDHPGQLVYQASSPDEAALVE
AARDLGFVFLSRTPDTVTINALGEEEEYEILHILEFNSDRKRMSVIVRDPDGRILLYCKGADSVIFERLS
PSSLELVEKTQEHLEDFASEGLRTLCLAYREISEEEYEEWNEKYDEASTALQNREELLDEVAEEIEKDLI
LLGATAIEDKLQDGVPETIEALQRAGIKIWVLTGDKQETAINIGYSCRLLSEDMENLALVIDGKTLTYAL
DPELERLFLELALKCKAVICCRVSPLQKALVVKLVKKSKKAVTLAIGDGANDVSMIQEAHVGVGISGQEG
MQAARASDYAIAQFRFLRRLLLVHGRWSYQRLAKLILYFFYKNIAFYLTQFWYQFFNGFSGQTLYDSWYL
TLYNVLFTSLPPLVIGIFDQDVSAETLLRYPELYKPGQLNELFNWKVFLYWILDGIYQSLIIFFVP
>gnl|CDD|319771 cd02076, P-type_ATPase_H, plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+)-ATPases. This subfamily includes eukaryotic plasma membrane H(+)-ATPase which transports H(+) from the cytosol to the extracellular space, thus energizing the plasma membrane for the uptake of ions and nutrients, and is expressed in plants and fungi. This H(+)-ATPase consists of four domains: a transmembrane domain and three cytosolic domains: nucleotide-binding domain, phosphorylation domain and actuator domain, and belongs to the P-type ATPase type III subfamily. This subfamily also includes the putative P-type H(+)-ATPase, MJ1226p of the anaerobic hyperthermophilic archaea Methanococcus jannaschii. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
GLTSEEAAKRLKEYGPNELPEKKENPILKFLSFFWGPIPWMLEAAAILAAALGDWVDFAIILLLLLINAG
IGFIEERQAGNAVAALKKSLAPKARVLRDGQWQEIDAKELVPGDIVSLKIGDIVPADARLLTGDALQVDQ
SALTGESLPVTKHPGDEAYSGSIVKQGEMLAVVTATGSNTFFGKTAALVASAEEQGHLQKVLNKIGNFLI
LLALILVLIIVIVALYRHDPFLEILQFVLVLLIASIPVAMPAVLTVTMAVGALELAKKKAIVSRLSAIEE
LAGVDILCSDKTGTLTLNKLSLDEPYSLEGDGKDELLLLAALASDTENPDAIDTAILNALDDYKPDLAGY
KQLKFTPFDPVDKRTEATVEDPDGERFKVTKGAPQVILELVGNDEAIRQAVEEKIDELASRGYRSLGVAR
KEDGGRWELLGLLPLFDPPRPDSKATIARAKELGVRVKMITGDQLAIAKETARQLGMGTNILSAERLKLG
GGGGGMPGSELIEFIEDADGFAEVFPEHKYRIVEALQQRGHLVGMTGDGVNDAPALKKADVGIAVSGATD
AARAAADIVLTAPGLSVIIDAIKTSRQIFQRMKSYVIYRIAETLRILVFFTLGILILNFYPLPLIMIVLI
AILNDGATLTIAYDNVPPSPRPVRWNMPELLGIATVLGVVLTISSFLLLWLLDDQGWFEDIVLSAGELQT
ILYLQLSISGHLTIFVTRTRGPFWRPRPSPLLFIAVVLTQILATLLAVYGWFMFAGIGWGWALLVWIYAL
VWFVVLDFVKL
>gnl|CDD|319772 cd02077, P-type_ATPase_Mg, magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella typhimurium MgtA. MgtA is a membrane protein which actively transports Mg(2+) into the cytosol with its electro-chemical gradient rather than against the gradient as other cation transporters do. It may act both as a transporter and as a sensor for Mg(2+). In Salmonella typhimurium and Escherichia coli, the two-component system PhoQ/PhoP regulates the transcription of the mgtA gene by sensing Mg(2+) concentrations in the periplasm. MgtA is activated by cardiolipin and it highly sensitive to free magnesium in vitro. It consists of a transmembrane domain and three cytosolic domains: nucleotide-binding domain, phosphorylation domain and actuator domain, and belongs to the P-type ATPase type III subfamily. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
GLTNEEAEERLEKYGPNEISHEKFPSWFKLLLKAFINPFNIVLLVLALVSFFTDVLLAPGEFDLVGALII
LLMVLISGLLDFIQEIRSLKAAEKLKKMVKNTATVIRDGSKYMEIPIDELVPGDIVYLSAGDMIPADVRI
IQSKDLFVSQSSLTGESEPVEKHATAKKTKDESILELENICFMGTNVVSGSALAVVIATGNDTYFGSIAK
SITEKRPETSFDKGINKVSKLLIRFMLVMVPVVFLINGLTKGDWLEALLFALAVAVGLTPEMLPMIVTSN
LAKGAVRMSKRKVIVKNLNAIQNFGAMDILCTDKTGTLTQDKIVLERHLDVNGKESERVLRLAYLNSYFQ
TGLKNLLDKAIIDHAEEANANGLIQDYTKIDEIPFDFERRRMSVVVKDNDGKHLLITKGAVEEILNVCTH
VEVNGEVVPLTDTLREKILAQVEELNREGLRVLAIAYKKLPAPEGEYSVKDEKELILIGFLAFLDPPKES
AAQAIKALKKNGVNVKILTGDNEIVTKAICKQVGLDINRVLTGSEIEALSDEELAKIVEETNIFAKLSPL
QKARIIQALKKNGHVVGFMGDGINDAPALRQADVGISVDSAVDIAKEAADIILLEKDLMVLEEGVIEGRK
TFGNILKYIKMTASSNFGNVFSVLVASAFLPFLPMLPIQLLLQNLLYDFSQLAIPFDNVDEEFLKKPQKW
DIKNIGRFMIWIGPISSIFDILTFLVMWFVFKANTAASQALFQTGWFIEGLLTQTLVVHMIRTEKIPF
>gnl|CDD|319773 cd02078, P-type_ATPase_K, potassium-transporting ATPase ATP-binding subunit, KdpB, a subunit of the prokaryotic high-affinity potassium uptake system KdpFABC; similar to Escherichia coli KdpB. KdpFABC is a prokaryotic high-affinity potassium uptake system. It is expressed under K(+) limiting conditions when the other potassium transport systems are not able to provide a sufficient flow of K(+) into the bacteria. The KdpB subunit represents the catalytic subunit performing ATP hydrolysis. KdpB is comprised of four domains: the transmembrane domain, the nucleotide-binding domain, the phosphorylation domain, and the actuator domain. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
DKDIVKEAIKDSFKKLNPRVLAKNPVMFVVEIGSIITTVLTFFPLLFSGGGPAGFNLAVSLWLWFTVLFA
NFAEAIAEGRGKAQADSLRKTKTETQAKRLRNDGKIEKVPATDLKKGDIVLVEAGDIIPADGEVIEGVAS
VDESAITGESAPVIRESGGDRSSVTGGTKVLSDRIKVRITANPGETFLDRMIALVEGASRQKTPNEIALT
ILLVGLTLIFLIVVATLPPFAEYSGAPVSVTVLVALLVCLIPTTIGGLLSAIGIAGMDRLLRFNVIAKSG
RAVEAAGDVDTLLLDKTGTITLGNRQATEFIPVGGVDEKELADAAQLASLADETPEGRSIVILAKQLGGT
ERDLDLSGAEFIPFSAETRMSGVDLPDGTEIRKGAVDAIRKYVRSLGGSIPEELEAIVEEISKQGGTPLV
VAEDDRVLGVIYLKDIIKPGIKERFAELRKMGIKTVMITGDNPLTAAAIAAEAGVDDFLAEAKPEDKLEL
IRKEQAKGKLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAGNMVDLDSDPTKLIEVVEIGKQLLMTR
GALTTFSIANDVAKYFAIIPAMFAAAYPQLGALNIMHLASPYSAILSAVIFNALIIPALIPLALKGVKYR
PLSASALLRRNLLIYGLGGIIVPFIGIKLIDMLITAL
>gnl|CDD|319774 cd02079, P-type_ATPase_HM, P-type heavy metal-transporting ATPase. Heavy metal-transporting ATPases (Type IB ATPases) transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. These ATPases include mammalian copper-transporting ATPases, ATP7A and ATP7B, Bacillus subtilis CadA which transports cadmium, zinc and cobalt out of the cell, Bacillus subtilis ZosA/PfeT which transports copper, and perhaps also zinc and ferrous iron, Archaeoglobus fulgidus CopA and CopB, Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase, and Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This family belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
AALVSGALMLLAFALYLGLFGGLVQLLLWVSLLLALPALLYGGRPFLRGAWRSLRRGRLNMDVLVSLAAI
GAFVASLLTPLLGGIGYFEEAAMLLFLFLLGRYLEERARSRARSALKALLSLAPETATVLEDGSTEEVPV
DDLKVGDVVLVKPGERIPVDGVVVSGESSVDESSLTGESLPVEKGAGDTVFAGTINLNGPLTIEVTKTGE
DTTLAKIIRLVEEAQSSKPPLQRLADRFARYFTPAVLVLAALVFLFWPLVGGPPSLALYRALAVLVVACP
CALGLATPTAIVAGIGRAARKGILIKGGDVLETLAKVDTVAFDKTGTLTEGKPEVTEIEPLEGFSEDELL
ALAAALEQHSEHPLARAIVEAAEEKGLPPLEVEDVEEIPGKGISGEVDGREVLIGSLSFAEEEGLVEAAD
ALSDAGKTSAVYVGRDGKLVGLFALEDQLRPEAKEVIAELKSGGIKVVMLTGDNEAAAQAVAKELGIDEV
HAGLLPEDKLAIVKALQAEGGPVAMVGDGINDAPALAQADVGIAMGSGTDVAIETADIVLLSNDLSKLPD
AIRLARRTRRIIKQNLAWALGYNAIALPLAALGLLTPWIAALLMEGSSLLVVLNALR
>gnl|CDD|319775 cd02080, P-type_ATPase_cation, P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, and Synechocystis sp. PCC 6803 PMA1, a putative Ca(2+)-ATPase. This subfamily includes the P-type Na(+)-ATPase of an alkaliphilic bacterium Exiguobacterium aurantiacum Mna and cyanobacterium Synechocystis sp. PCC 6803 PMA1, a cation-transporting ATPase which may translocate calcium. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
GLTSEEAAERLERYGPNRLPEKKTKSPLLRFLRQFNNPLIYILLAAAVVTAFLGHWVDAIVIFGVVLINA
IIGYIQEGKAEKALAAIKNMLSPEATVLRDGKKLTIDAEELVPGDIVLLEAGDKVPADLRLIEARNLQID
ESALTGESVPVEKQEGPLEEDTPLGDRKNMAYSGTLVTAGSATGVVVATGADTEIGRINQLLAEVEQLAT
PLTRQIAKFSKALLIVILVLAALTFVFGLLRGDYSLVELFMAVVALAVAAIPEGLPAVITITLAIGVQRM
AKRNAIIRRLPAVETLGSVTVICSDKTGTLTRNEMTVQAIVTLCNDAQLHQEDGHWKITGDPTEGALLVL
AAKAGLDPDRLASSYPRVDKIPFDSAYRYMATLHRDDGQRVIYVKGAPERLLDMCDQELLDGGVSPLDRA
YWEAEAEDLAKQGLRVLAFAYREVDSEVEEIDHADLEGGLTFLGLQGMIDPPRPEAIAAVAECQSAGIRV
KMITGDHAETARAIGAQLGLGDGKKVLTGAELDALDDEELAEAVDEVDVFARTSPEHKLRLVRALQARGE
VVAMTGDGVNDAPALKQADIGIAMGIKGTEVAKEAADMVLADDNFATIAAAVEEGRRVYDNLKKFILFTL
PTNLGEGLVIIVAILFGVTLPLTPVQILWINMVTAITLGLALAFEPAEPGIMKRPPRDPSEPLLSRELIW
RILLVSLLMLGGAFGLFLWALDRGYSLETARTMAVNTIVVAQIFYLFNCRSLHRSILKLGVFSNKILFLG
IGALILLQLAFTYLPFMNSLFGTAPIDLVDWAIILLVGIVVFIVVELEK
>gnl|CDD|319776 cd02081, P-type_ATPase_Ca_PMCA-like, animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related Ca2(+)-ATPases including Saccharomyces cerevisiae vacuolar PMC1. Animal PMCAs function to export Ca(2+) from cells and play a role in regulating Ca(2+) signals following stimulus induction and in preventing calcium toxicity. Many PMCA pump variants exist due to alternative splicing of transcripts. PMCAs are regulated by the binding of calmodulin or by kinase-mediated phosphorylation. Saccharomyces cerevisiae vacuolar transporter Pmc1p facilitates the accumulation of Ca2+ into vacuoles. Pmc1p is not regulated by direct calmodulin binding but responds to the calmodulin/calcineurin-signaling pathway and is controlled by the transcription factor complex Tcn1p/Crz1p. Similarly, the expression of the gene for Dictyostelium discoideum Ca(2+)-ATPase PAT1, patA, is under the control of a calcineurin-dependent transcription factor. Plant vacuolar Ca(2+)-ATPases, are regulated by direct-calmodulin binding. Plant Ca(2+)-ATPases are present at various cellular locations including the plasma membrane, endoplasmic reticulum, chloroplast and vacuole. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
LEHRREVYGKNEIPPKPPKSFLQLVWEALQDPTLIILLIAAIVSLGLGFYTPFGEGEGKTGWIEGVAILV
AVILVVLVTAGNDYQKEKQFRKLNSKKEDQKVTVIRDGEVIQISVFDIVVGDIVQLKYGDLIPADGLLIE
GNDLKIDESSLTGESDPIKKTPDNQIPDPFLLSGTKVLEGSGKMLVTAVGVNSQTGKIMTLLRAENEEKT
PLQEKLTKLAVQIGKVGLIVAALTFIVLIIRFIIDGFVNDGKSFSAEDLQEFVNFFIIAVTIIVVAVPEG
LPLAVTLSLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTQNRMTVVQGYIGNKTECALLGFV
LELGGDYRYREKRPEEKVLKVYPFNSARKRMSTVVRLKDGGYRLYVKGASEIVLKKCSYILNSDGEVVFL
TSEKKEEIKRVIEPMASDSLRTIGLAYRDFSPDEEPTAERDWDDEEDIESDLTFIGIVGIKDPLRPEVPE
AVAKCQRAGITVRMVTGDNINTARAIARECGILTEGEDGLVLEGKEFRELIDEEVGEVCQEKFDKIWPKL
RVLARSSPEDKYTLVKGLKDSGEVVAVTGDGTNDAPALKKADVGFAMGIAGTEVAKEASDIILLDDNFSS
IVKAVMWGRNVYDSIRKFLQFQLTVNVVAVILAFIGAVVTKDSPLTAVQMLWVNLIMDTLAALALATEPP
TEDLLKRKPYGRDKPLISRTM
>gnl|CDD|319777 cd02082, P-type_ATPase_cation, P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins and Saccharomyces cerevisiae Ypk9p and Spf1p. Saccharomyces cerevisiae Yph9p localizes to the yeast vacuole and may play a role in sequestering heavy metal ions, its deletion confers sensitivity for growth for cadmium, manganese, nickel or selenium. Saccharomyces 1 Spf1p may mediate manganese transport into the endoplasmic reticulum. Human ATP13A2 (PARK9/CLN12) is a lysosomal transporter with zinc as the possible substrate. Mutation in the ATP13A2 gene has been linked to Parkinson's disease and Kufor-Rakeb syndrome, and to neuronal ceroid lipofuscinoses. ATP13A3/AFURS1 is a candidate gene for oculo auriculo vertebral spectrum (OAVS), being one of nine genes included in a 3q29 microduplication in a patient with OAVS. Mutation in the human ATP13A4 may be involved in a speech-language disorder. The expression of ATP13A1 has been followed during mouse development, ATP13A1 transcript expression showed an increase as development progressed, with the highest expression at the peak of neurogenesis. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
RVDQLLAYYGKNEIEINVPSFLTLMWREFKKPFNFFQYFGVILWGIDEYVYYAITVVFMTTINSLSCIYI
RGVMQKELKDACLNNTSVIVQRHGYQEITIASNMIVPGDIVLIKRREVTLPCDCVLLEGSCIVTEAMLTG
ESVPIGKCQIPTDSHDDVLFKYESSKSHTLFQGTQVMQIIPPEDDILKAIVVRTGFGTSKGQLIRAILYP
KPFNKKFQQQAVKFTLLLATLALIGFLYTLIRLLDIELPPLFIAFEFLDILTYSVPPGLPMLIAITNFVG
LKRLKKNQILCQDPNRISQAGRIQTLCFDKTGTLTEDKLDLIGYQLKGQNQTFDPIQCQDPNNISIEHKL
FAICHSLTKINGKLLGDPLDVKMAEASTWDLDYDHEAKQHYSKSGTKRFYIIQVFQFHSALQRMSVVAKE
VDMITKDFKHYAFIKGAPEKIQSLFSHVPSDEKAQLSTLINEGYRVLALGYKELPQSEIDAFLDLSREAQ
EANVQFLGFIIYKNNLKPDTQAVIKEFKEACYRIVMITGDNPLTALKVAQELEIINRKNPTIIIHLLIPE
IQKDNSTQWILIIHTNVFARTAPEQKQTIIRLLKESDYIVCMCGDGANDCGALKEADVGISLAEADASFA
SPFTSKSTSISCVKRVILEGRVNLSTSVEIFKGYALVALIRYLSFLTLYYFYSSYSSSGQMDWQLLAAGY
FLVYLRLGCNTPLKKLEKDDNLFSIYNVTSVLFGFTLHILSIVGCVESLQASPIYKEVNSLDAENNFQFE
TQHNTVLAFNILINFF
>gnl|CDD|319778 cd02083, P-type_ATPase_SERCA, sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3. SERCA is a transmembrane (Ca2+)-ATPase and a major regulator of Ca(2+) homeostasis and contractility in cardiac and skeletal muscle. It re-sequesters cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby also terminating Ca(2+)-induced signaling such as in muscle contraction. Three genes (ATP2A1-3/SERCA1-3) encode SERCA pumps in mammals, further isoforms exist due to alternative splicing of transcripts. The activity of SERCA is regulated by two small membrane proteins called phospholamban and sarcolipin. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
HSKTVEEVLAYFGVDPTRGLSDEQVKRRREKYGPNELPAEEGKSLWELVLEQFDDLLVRILLLAAIISFV
LALFEEGEEGVTAFVEPFVILLILIANAVVGVWQERNAEKAIEALKEYEPEMAKVLRNGKGVQRIRAREL
VPGDIVEVAVGDKVPADIRIIEIKSTTLRVDQSILTGESVSVIKHTDVVPDPRAVNQDKKNMLFSGTNVA
AGKARGVVVGTGLNTEIGKIRDEMAETEEEKTPLQQKLDEFGEQLSKVISVICVAVWAINIGHFNDPAHG
GSWIKGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGT
LTTNQMSVSRMFILDKVEDDSSLNEFEVTGSTYAPEGEVFKNGKKVKAGQYDGLVELATICALCNDSSLD
YNESKGVYEKVGEATETALTVLVEKMNVFNTDKSGLSKRERANACNDVIEQLWKKEFTLEFSRDRKSMSV
YCSPTKASGGNKLFVKGAPEGVLERCTHVRVGGGKVVPLTAAIKILILKKVWGYGTDTLRCLALATKDTP
PKPEDMDLEDSTKFYKYETDLTFVGVVGMLDPPRPEVRDSIEKCRDAGIRVIVITGDNKGTAEAICRRIG
IFGEDEDTTGKSYTGREFDDLSPEEQREACRRARLFSRVEPSHKSKIVELLQSQGEITAMTGDGVNDAPA
LKKAEIGIAMGSGTAVAKSASDMVLADDNFATIVAAVEEGRAIYNNMKQFIRYLISSNIGEVVSIFLTAA
LGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMKKPPRKPDEPLISGWLFFRYLAIGTYVGLATVG
AFAWWFMYYEEGPQVSFYQLTHFMQCSSWEPNFEGVDCEIFEDPHPMTMALSVLVVIEMFNALNSLSENQ
SLLVMPPWSNPWLVGAIALSMALHFVILYVPPLATIFQITPLSFAEWIAVIKISLPVILLDELLKFIAR
>gnl|CDD|319779 cd02085, P-type_ATPase_SPCA, golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory pathway Ca(2+) transporting 1/hSPCA1 and Saccharomyces cerevisiae Ca(2+)/Mn(2+)-transporting P-type ATPase, Pmr1p. SPCAs are Ca(2+) pumps important for the golgi-associated secretion pathway, in addition some function as Mn(2+) pumps in Mn(2+) detoxification. Saccharomyces cerevisiae Pmr1p is a high affinity Ca(2+)/Mn(2+) ATPase which transports Ca(2+) and Mn(2+) from the cytoplasm into the Golgi. Pmr1p also contributes to Cd(2+) detoxification. This subfamily includes human SPCA1 and SPCA2, encoded by the ATP2C1 and ATP2C2 genes; autosomal dominant Hailey-Hailey disease is caused by mutations in the human ATP2C1 gene. It also includes Strongylocentrotus purpuratus testis secretory pathway calcium transporting ATPase SPCA which plays an important role in fertilization. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
RRKLHGPNEFKVEDEEPLWKKYLEQFKNPLILLLLGSAVVSVVMKQYDDAVSITVAILIVVTVAFVQEYR
SEKSLEALNKLVPPECHCLRDGKLEHFLARELVPGDLVCLSIGDRIPADLRLFEATDLSIDESSLTGETE
PCSKTTEVIPKASNGDLTTRSNIAFMGTLVRCGHGKGIVIGTGENSEFGEVFKMMQAEEAPKTPLQKSMD
KLGKQLSLYSFIIIGVIMLIGWLQGKNLLEMFTIGVSLAVAAIPEGLPIVVTVTLALGVMRMAKRRAIVK
KLPIVETLGCVNVICSDKTGTLTKNEMTVTKIVTGCVCNNAVIRNNTLMGQPTEGALIALAMKMGLSDIR
ETYIRKQEIPFSSEQKWMAVKCIPKYNSDNEEIYFMKGALEQVLDYCTTYNSSDGSALPLTQQQRSEINE
EEKEMGSKGLRVLALASGPELGDLTFLGLVGINDPPRPGVREAIQILLESGVRVKMITGDAQETAIAIGS
SLGLYSPSLQALSGEEVDQMSDSQLASVVRKVTVFYRASPRHKLKIVKALQKSGAVVAMTGDGVNDAVAL
KSADIGIAMGRTGTDVCKEAADMILVDDDFSTILAAIEEGKGIFYNIKNFVRFQLSTSIAALSLIALSTL
FNLPNPLNAMQILWINIIMDGPPAQSLGVEPVDKDVIRQPPRNVKDPILTRSLILNVLLSAAIIVSGTLW
VFWKEMSDDNVTPRDTTMTFTCFVFFDMFNALSCRSQTKSIFEIGFFSNRMFLYAVGGSLIGQLLVIYFP
PLQRVFQTEALGLLDLLFLLGLTSSVFIVSELRK
>gnl|CDD|319780 cd02086, P-type_ATPase_Na_ENA, fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces cerevisiae Ena1p, Ena2p and Ustilago maydis Ena1, and the endoplasmic reticulum sodium transporter Ustilago maydis Ena2. Fungal-type Na(+)-ATPase (also called ENA ATPases). This subfamily includes the Saccharomyces cerevisiae plasma membrane transporters: Na(+)/Li(+)-exporting ATPase Ena1p which may also extrudes K(+), and Na(+)-exporting P-type ATPase Ena2p. It also includes Ustilago maydis plasma membrane Ena1, an K(+)/Na(+)-ATPase whose chief role is to pump Na(+) and K(+) out of the cytoplasm, especially at high pH values, and endoplasmic reticulum Ena2 ATPase which mediates Na(+) or K(+) fluxes in the ER or in other endomembranes. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
GLTNDEAERRLKEYGENELEGDTGVSAWKILLRQVANAMTLVLIIAMALSFAVKDWIEGGVIAAVIALNV
IVGFIQEYKAEKTMDSLRNLSSPNAHVIRSGKTETISSKDVVPGDIVLLKVGDTVPADLRLIETKNFETD
EALLTGESLPVIKDAELVFGKEEDVSVGDRLNLAYSSSTVTKGRAKGIVVATGMNTEIGKIAKALRGKGG
LISRDRVKSWLYGTLIVTWDAVGRFLGTNVGTPLQRKLSKLAYLLFFIAVILAIIVFAVNKFDVDNEVII
YAIALAISMIPESLVAVLTITMAVGAKRMVKRNVIVRKLDALEALGAVTDICSDKTGTLTQGKMVVRQVW
IPAALCNIATVFKDEETDCWKAHGDPTEIALQVFATKFDMGKNALTKGGSAQFQHVAEFPFDSTVKRMSV
VYYNNQAGDYYAYMKGAVERVLECCSSMYGKDGIIPLDDEFRKTIIKNVESLASQGLRVLAFASRSFTKA
QFNDDQLKNITLSRADAESDLTFLGLVGIYDPPRNESAGAVEKCHQAGITVHMLTGDHPGTAKAIAREVG
ILPPNSYHYSQEIMDSMVMTASQFDGLSDEEVDALPVLPLVIARCSPQTKVRMIEALHRRKKFCAMTGDG
VNDSPSLKMADVGIAMGLNGSDVAKDASDIVLTDDNFASIVNAIEEGRRMFDNIQKFVLHLLAENVAQVI
LLLIGLAFKDEDGLSVFPLSPVEILWINMVTSSFPAMGLGLEKASPDVMQRPPHDLKVGIFTRELIIDTF
VYGTFMGVLCLASFTLVIYGIGNGDLGSDCNESYNSSCEDVFRARAAVFATLTWCALILAWEVVDMRRSF
FNMHPDTDSPVKSFFKTLWKNKFLFWSVVLGFVSVFPTLYIPVINDDVFKHTGIGWEWGLVIACTVAFFA
GVELWKAGKR
>gnl|CDD|319781 cd02089, P-type_ATPase_Ca_prok, prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL and Listeria monocytogenes LMCA1. Ca(2+) transport ATPase is a plasma membrane protein which pumps Ca(2+) ion out of the cytoplasm. This prokaryotic subfamily includes the Ca(2+)-ATPase Synechococcus elongatus PacL, Listeria monocytogenes Ca(2+)-ATPase 1 (LMCA1) which has a low Ca(2+) affinity and a high pH optimum (pH about 9) and may remove Ca(2+) from the microorganism in environmental conditions when e.g. stressed by high Ca(2+) and alkaline pH, and the Bacillus subtilis putative P-type Ca(2+)-transport ATPase encoded by the yloB gene, which is expressed during sporulation. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
GLSEEEAERRLAKYGPNELVEKKKRSPWKKFLEQFKDFMVIVLLAAAVISGVLGEYVDAIVIIAIVILNA
VLGFVQEYKAEKALAALKKMSAPTAKVLRDGKKQEIPARELVPGDIVLLEAGDYVPADGRLIESASLRVE
ESSLTGESEPVEKDADTLLEEDVPLGDRKNMVFSGTLVTYGRGRAVVTATGMNTEMGKIATLLEETEEEK
TPLQKRLDQLGKRLAIAALIICALVFALGLLRGEDLLDMLLTAVSLAVAAIPEGLPAIVTIVLALGVQRM
AKRNAIIRKLPAVETLGSVSVICSDKTGTLTQNKMTVEKIYTIGDPTETALIRAARKAGLDKEELEKKYP
RIAEIPFDSERKLMTTVHKDAGKYIVFTKGAPDVLLPRCTYIYINGQVRPLTEEDRAKILAVNEEFSEEA
LRVLAVAYKPLDEDPTESSEDLENDLIFLGLVGMIDPPRPEVKDAVAECKKAGIKTVMITGDHKLTARAI
AKELGILEDGDKALTGEELDKMSDEELEKKVEQISVYARVSPEHKLRIVKALQRKGKIVAMTGDGVNDAP
ALKAADIGVAMGITGTDVAKEAADMILTDDNFATIVAAVEEGRTIYDNIRKFIRYLLSGNVGEILTMLLA
PLLGWPVPLLPIQLLWINLLTDGLPALALGVEPAEPDIMDRKPR
>gnl|CDD|319782 cd02092, P-type_ATPase_FixI-like, Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ATPase subfamily. FixI may be a pump of a specific cation involved in symbiotic nitrogen fixation. The Rhizobium fixI gene is part of an operon conserved among rhizobia, fixGHIS. FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalyzed by FixG, an iron-sulfur protein. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
AGFAAMNIMLLSVSVWSGAASATRDLFHWISALIALPAVAYAGRPFFRSAWAALRHGRTNMDVPISIGVL
LATGMSLFETLHGGEHAYFDAAVMLLFFLLIGRYLDHRMRGRARSAAEELAALEARGAQRLQADGSREYV
PVAEIRPGDRVLVAAGERIPVDGTVVSGTSELDRSLLTGESAPVTVAPGDLVQAGAMNLSGPLRLRATAA
GDDTLLAEIARLMEAAEQGRSRYVRLADRAARLYAPVVHLLALLTFVGWVAAGGDWRHALLIAVAVLIIT
CPCALGLAVPAVQVVASGRLFRRGVLVKDGTALERLAEVDTVVFDKTGTLTLGSPRLVGAHAISADLLAL
AAALAQASRHPLSRALAAAAGARPVELDDAREVPGRGVEGRIDGARVRLGRPAWLGASAGVSTASELALS
KGGEEAARFPFEDRPRPDAREAISALRALGLSVEILSGDREPAVRALARALGIEDWRAGLTPAEKVARIE
ELKAQGRRVLMVGDGLNDAPALAAAHVSMAPASAVDASRSAADIVFLGDSLAPVPEAIEIARRARRLIRQ
NFALAIGYNVIAVPLAIAGYVTPLIAALAMSTSSIVVVLNALRLR
>gnl|CDD|319783 cd02094, P-type_ATPase_Cu-like, P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B. The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA, Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
RRLILSLLLTLPLLLLMMGGMLGPPLPLLLLQLNWWLQFLLATPVQFWGGRPFYRGAWKALKHGSANMDT
LVALGTSAAYLYSLVALLFPALFPGGAPHVYFEAAAVIITFILLGKYLEARAKGKTSEAIKKLLGLQPKT
ARVIRDGKEVEVPIEEVQVGDIVRVRPGEKIPVDGVVVEGESSVDESMLTGESLPVEKKPGDKVIGGTIN
GNGSLLVRATRVGADTTLAQIIRLVEEAQGSKAPIQRLADRVSGVFVPVVIAIAILTFLVWLLLGPEPAL
TFALVAAVAVLVIACPCALGLATPTAIMVGTGRAAELGILIKGGEALERAHKVDTVVFDKTGTLTEGKPE
VTDVVPLPGDDEDELLRLAASLEQGSEHPLAKAIVAAAKEKGLELPEVEDFEAIPGKGVRGTVDGRRVLV
GNRRLMEENGIDLSALEAEALALEEEGKTVVLVAVDGELAGLIAVADPLKPDAAEAIEALKKMGIKVVML
TGDNRRTARAIAKELGIDEVIAEVLPEDKAEKVKKLQAQGKKVAMVGDGINDAPALAQADVGIAIGSGTD
VAIESADIVLMRGDLRGVVTAIDLSRATMRNIKQNLFWAFIYNVIGIPLAAGVLYPFGGILLSPMIAGAA
MALSSVSVVLNSLRLRR
>gnl|CDD|259797 cd02106, SPFH_like, core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons, and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome
RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLD
QIISGRDEIAKAVKEDLEEDLENFGVVISDVDITSIEPPD
>gnl|CDD|239025 cd02107, YedY_like_Moco, YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. Escherichia coli YedY has been proposed to form a heterodimer, consisting of a soluble catalytic subunit termed YedY, which is likely membrane-anchored by a heme-containing trans-membrane subunit YedZ. Preliminary results indicate that YedY may represent a new type of membrane-associated bacterial reductase. Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate
TTYNNFYEFGTGKDDPARNAGNLPTRPWTVSVSGLVKKPKTLDIDDLMKTFPLEERIYRFRCVEGWSMVV
PWVGFPLAALLARAEPTSEAKYVRFTTLLDKEQMPGQSGLFGVLPWPYVEGLRLDEAMHPLTLLAVGLYG
EALPKQNGAPIRLVVPWKYGFKSIKSIVKIEFTKEQPPTTWNLAAPDEYGFYANVNPSVDHPRWSQATER
RIGEGGRR
>gnl|CDD|239026 cd02108, bact_SO_family_Moco, bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This domain is found in a variety of oxidoreductases. Common features of all known members of this family, like sulfite oxidase and nitrite reductase, are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate. The specific function of this subgroup is unknown
LAPEFRRNGIRKPEALAYKALEANDFADYRLEVGGLVEHPLSLSLEELRALPQRTQITRHICVEGWSAIG
KWGGVPLRTILELVGPLPEAKYVVFKCADDFAGGDRYYESIDMASALHPQTLLAYEMNGQPLPIKNGAPL
RLRVETQLGYKQAKWVTEIELVNDLPGIGGGKGGYWEDQGYNWFG
>gnl|CDD|239027 cd02109, arch_bact_SO_family_Moco, bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding domains. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate. The specific function of this subgroup is unknown
LPPGQYLTEKFPVLDAGDVPEVDLEKWRLRVTGLVENPLSLTYEDLLALPQTEYTADFHCVTGWSKLDVV
WEGVSLKDLLEAARPDPEATFVMAHSYDGYTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVPHL
YFWKSAKWLRGIEFLDEDEPGFWERRGYHERGDPWREERF
>gnl|CDD|239028 cd02110, SO_family_Moco_dimer, Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved dimerization domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO)
LFFVRNHGGVPDIDPDAWRLEIHGLVERPLTLTLDDLKRLPSVEVVATLECSGNGRGGFIPVRSGAQWGH
GAVGNARWTGVPLKDLLEEAGVKPGAKHVLFEGADVPPGEKAADYTRSVPLSKALDDDALLAYEMNGEPL
PPDHGYPLRLVVPGWYGARSVKWLRRIEVTDQPSDGYWQTRDYTVPPPDVDAVGGKARRPIGEMPVKSVI
TSPSPGAELVSGGRVEIGGVAWSGGRGIRRVEVSLDGGRTWQEARLEGPLAGPRAWRQWELDWDLPPGEY
ELVARATDSTGNVQPERAEWNWNPGGYGNNHWHRVQV
>gnl|CDD|239029 cd02111, eukary_SO_Moco, molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Common features of all known members of the sulfite oxidase (SO) family of molybdopterin binding domains are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate
ALKVNSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVDPDTYSLEVEGPDGTTLSLSLEDLKSLFP
KHEVTATLQCAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPEDDSQGGLHVHFEGLD
VDPTGTPYGASIPLSKALDPEADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESD
SHWQQNDYKGFSPSVDWDNVDFSKAPAIQEMPVQSAICSPSVGAPVVTVPPGKITVKGYAWSGGGRKIVR
VDVSLDGGRTWKVAELEQEENVWPSGRKWAWTLWEATVPVPAGKEAEIIAKAVDSAYNVQPETVEPIWNL
RGVLNNAWHRVKVVV
>gnl|CDD|239030 cd02112, eukary_NR_Moco, molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze the reduction of nitrate to nitrite which is subsequently converted to NH4+ by nitrite reductase. Eukaryotic assimilatory nitrate reductases are cytosolic homodimeric enzymes with three prosthetic groups, flavin adenine dinucleotide (FAD), cytochrome b557, and Mo cofactor, which are located in three functional domains. Common features of all known members of the sulfite oxidase (SO) family of molybdopterin binding domains are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate
DLGTPDAWIPRDPRLIRLTGKHPFNSEPPLTELMDHGFITPSNLHYVRNHGPVPREKWEDWTVEVTGLVE
KPTTLTMDELVAMFPSVTFPVTLVCAGNRRKEQNMVKKTIGFNWGAAGTSTSLWTGVRLSDLLDRCGPKS
PKGGARHVCFEGADDLLPGPNGKYGTSITLSWAMDPSKDVMLAYKQNGELLHPDHGFPVRLIIPGQIGGR
MVKWLKRIVVSDRESQNHYHFHDNRVLPSHVDAELANEEGWWYKPEYIINDLNVNSAITTPAHDEVLPLN
GLTTAETYTMKGYAYAGGGRRVTRVEVSLDDGKSWKLASIDYPEDPTKYGKCWCWCFWSLDVPLSELLAA
KEICVRAWDESMNTQPRDMTWNVMGMMNNCWFRVKI
>gnl|CDD|239031 cd02113, bact_SoxC_Moco, bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. SoxC is involved in oxidation of sulfur compounds during chemolithothrophic growth. Together with SoxD, a small c-type heme containing subunit, it forms a hetrotetrameric sulfite dehydrogenase. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate
PLQDLEGIITPNGLHFERHHGGVPDIDPAQHRLMIHGMVKKPLVFTMDDLKRFPSVSRIYFLECSGNGGT
GWRGAPLPTAQYTHGMLSCSEWTGVPLSTLLEEAGVKPGAKWLLAEGADAAAMTRSIPLEKALDDALVAY
AQNGEALRPENGYPLRLVVPGWEGNTNVKWLRRIEVGDQPWMTREETSKYTDLLPDGRARQFSFVMEAKS
VITSPSGGQRLREPGFHEISGLAWSGRGRIRRVDVSFDGGRTWQDARLEGPVLPKALTRFRLPWKWDGRP
AVLQSRATDETGYVQPTRAELRAVRGTNSIYHNNAIQSWRVDEDGE
>gnl|CDD|239032 cd02114, bact_SorA_Moco, sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is involved in oxidation of sulfur compounds during chemolithothrophic growth. Together with SorB, a small c-type heme containing subunit, it forms a hetrodimer. It is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate
LPFDNGWRELVPFPQKRPLIRLTTRPPHLETPFSVFNEGLITPNDAFFVRYHLAGIPLDIDPDAYTLTID
GKVRTPLTLSLAELKRIEPRFEVVAVNQCSGNSRGFFQPRVQGAQLANGAMGNARWAGVPLKAVLAKAGV
QDGARQVAFRGLDQPVLDVTPDFVKSLDIDHALDGEVMLAWEMNGEPLPVLNGYPLRLVVPGFYATYWVK
HLSHITVLDKEFDGFWASQAYRIPDNADAGVEPGTAPDRTAPINRFKVRSFITSLENGAIVAPAGELALR
GIAFDGGSGIRRVDVSADGGDSWTQATLGPDLGRFSFRGWKLTLDGVKKGPLTLMVRATNNDGQTQPLRA
PWNPGGYMRNVVERTRI
>gnl|CDD|239033 cd02115, AAK, Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition
VIKFGGSSVSSEERLRNLARILVKLASEGGRVVVVHGAGPQITDELLAHGELLGYARGLRITDRETDALA
AMGEGMSNLLIAAALEQHGIKAVPLDLTQAGFASPNQGHVGKITKVSTDRLKSLLENGILPILSGFGGTD
EKETGTLGRGGSDSTAALLAAALKADRLVILTDVDGVYTADPRKVPDAKLLSELTYEEAAELAYAGAMVL
KPKAADPAARAGIPVRIANTENPGALALFTPDGGGTLI
>gnl|CDD|153139 cd02116, ACT, ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times
LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDGDLEKLLEALE
>gnl|CDD|349761 cd02117, NifH-like, NifH family. This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction
ESIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTIDEMLTEDGTAEELRR
EDLLFSGFNGVDCVEAGGPEPGVGCGGRGIGTMLELLEEHGLLDDDYDVVIFDVLGDVVCGGFAAPLRRG
FAQKVVIVVSEELMSLYAANNIVKAVENYSKNGVRLAGLVANLRDPAGTEEIQAFAAAVGTKILAVIPRD
PAVRRAELARVTVFEHDPVSPAASEFARLAAKIADAVPPVPGPRPLSDRELFALLG
>gnl|CDD|239035 cd02120, PA_subtilisin_like, PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This group contains various PA domain-containing subtilisin-like proteases including melon cucumisin, Arabidopsis thaliana Ara12, a nodule specific serine protease from Alnus glutinosa ag12, members of the tomato P69 family, and tomato LeSBT2. These proteins belong to the peptidase S8 family. Cucumisin from the juice of melon fruits is a thermostable serine peptidase, with a broad substrate specificity for oligopeptides and proteins. A. thaliana Ara12 is a thermostable, extracellular serine protease, found chiefly in silique tissue and stem tissue. Ara12 is stimulated by Ca2+ ions. A. glutinosa ag12 is expressed at high levels in the nodules, and at low levels in the shoot tips; it is implicated in both symbiotic and non-symbiotic processes in plant development. The tomato P69 protease family is comprised of various protein isoforms of approximately 69KDa. These isoforms accumulate extracellularly. Some of the P69 genes are tightly regulated in a tissue specific fashion, and by environmental and developmental signals. For example: infection with avirulent bacteria activates transcription of the genes for the P69 B and C isoforms, the P69 E transcript was detected only in roots, and the P69F transcript only in hydathodes. The Tomato LeSBT2 subtilase transcript was not detected in flowers and roots, but was present in cotyledons and leaves. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
VVTLGNGKTIVGQSLYPGNLKTYPLVYKSANSGDVDASLCLPGSLDPSKVKGKIVLCDRGGNTSRVAKGD
AVKAAGGAGMILANDPTDGLDVVADAHVLPAVHVDYEDGTAILSYINSTSNPTATI
>gnl|CDD|239036 cd02121, PA_GCPII_like, PA_GCPII_like: Protease-associated domain containing protein, glutamate carboxypeptidase II (GCPII)-like. This group contains various PA domain-containing proteins similar to GCPII including, GCPIII (NAALADase2) and NAALADase L. These proteins belong to the peptidase M28 family. GCPII is also known N-acetylated-alpha-linked acidic dipeptidase (NAALDase1), folate hydrolase or prostate-specific membrane antigen (PSMA). GCPII is found in various human tissues including prostate, small intestine, and the central nervous system. In the brain, GCPII is known as NAALDase1, it functions as a NAALDase hydrolyzing the neuropeptide N-acetyl-L-aspartyl-L-glutamate (alpha-NAAG), to release free glutamate. In the small intestine, GCPII releases the terminal glutamate from poly-gamma-glutamated folates. GCPII (PSMA) is a useful cancer marker; its expression is markedly increased in prostate cancer and in tumor-associated neovasculature. GCPIII hydrolyzes alpha-NAAG with a lower efficiency than does GCPII; NAALADase L is not able to hydrolyze alpha-NAAG. The GCPII PA domain (referred to as the apical domain) participates in substrate binding and may act as a protein-protein interaction domain
PVKRSLILTKPDGATGKLIEDTVLEEPPSPDVVPPFHAYSASGNVTAELVYANYGSPEDFEYLEDLGIDV
KGKIVIARYGGIFRGLKVKNAQLAGAVGVIIYSDPADDGYITGENGKTYPDGPARPPSGVQRGSVLFMSI
GPGDPLTPGYPSKPGAERRDKEESKGLPKIPSLPISYRDAQPLLKALGGPGAPSDWQGGLPVTYRLGFGG
PSPGKVRVNL
>gnl|CDD|239037 cd02122, PA_GRAIL_like, PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain containing E3 (ubiquitin ligases) similar to human GRAIL (gene related to anergy in lymphocytes) protein. Proteins in this group contain a C3H2C3 RING finger. E3 ubiquitin ligase is part of an enzymic cascade, the end result of which is the ubiquitination of proteins. In this cascade, E1 activates the ubiquitin, the activated ubiquitin is carried by E2, and E3 recognizes the acceptor protein as well as catalyzes the transfer of the activated ubiquitin from E2 to this acceptor. GRAIL, a transmembrane protein localized in the endosomes, controls the development of T cell clonal anergy, and may ubiquitinate membrane-associated targets for T cell activation. GRAIL1 is associated with, and regulated by, two isoforms of otubain 1 (the ubiquitin-specific protease). Additional E3s belonging to this group include human (h)Goliath and Xenopus GREUL1 (Goliath Related E3 Ubiquitin Ligase 1). hGoliath and GRAIL both have the property of self-ubiquitination. hGoliath is expressed in leukocytes; its expression and localization is not modified in leukemia. GREUL1 may play a role in the generation of anterior ectoderm. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
NITYVDPISNELTTEKTESGRYGEHSPKEEAKGLVVVPDPPNDHYGCDPDTRFPIPPNGEPWIALIQRGN
CTFEEKIKLAAERNASAVVIYNNPGTGNETVKMSHPGTGDIVAIMITNPKGMEILELLERGISVTMVI
>gnl|CDD|239038 cd02123, PA_C_RZF_like, PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA domain-containing proteins similar to C-RZF (chicken embryo RING zinc finger) protein. These proteins contain a C3H2C3 RING finger. C-RZF is expressed in embryo cells and is restricted mainly to brain and heart, it is localized to both the nucleus and endosomes. Additional C3H2C3 RING finger proteins belonging to this group, include Arabidopsis ReMembR-H2 protein and mouse sperizin. ReMembR-H2 is likely to be an integral membrane protein, and to traffic through the endosomal pathway. Sperizin is expressed in haploid germ cells and localized in the cytoplasm, it may participate in spermatogenesis. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
LLVVSPLATADKLALADSNLTDEFDDLPANFGPIPPGSGLKGVLVVAEPLNACSPIENPPLNSNASGSFI
VLIRRGNCSFETKVRNAQRAGYKAAIVYNDESNDLISMSGNDQEIKGIDIPSVFVGKSTGEILKKYASYE
KGVILIPDLPLKI
>gnl|CDD|239039 cd02124, PA_PoS1_like, PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA domain-containing proteins similar to Pleurotus ostreatus (Po)S1. PoSl, the main extracellular protease in P. ostreatus is a subtilisin-like serine protease belonging to the peptidase S8 family. Ca2+ and Mn2+ both stimulate the protease activity of (Po)S1. Ca2+ protects PoS1 from autolysis. PoS1 is a monomeric glycoprotein, which may play a role in the regulation of laccases in lignin formation. (Po)S1 participates in the degradation of POXA1b, and in the activation of POXA3, (POXA1b and POXA3 are laccase isoenzymes), but its effect may be indirect. The significance of the PA domain to PoS1 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
VVPAGGTSNGTTDFGYLPGFPALWNDTLPLWALSLDTSVADDACQPLPDDTPDLSGYIVLVRRGTCTFAT
KAANAAAKGAKYVLIYNNGSGPTDQVGSDADSIIAAVTPEDGEAWIDALAAGSNVTVDF
>gnl|CDD|239040 cd02125, PA_VSR, PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This group includes various PA domain-containing VSRs such as garden pea BP-80, pumpkin PV72, and various Arabidopsis VSRs including AtVSR1. In contrast to most eukaryotes, which only have one or two VSRs, plants have several. This may in part be a reflection of having a more complex vacuolar system with both lytic vacuoles and storage vacuoles. The lytic vacuole is thought to be equivalent to the mammalian lysosome and the yeast vacuole. Pea BP-80 is a type 1 transmembrane protein, involved in the targeting of proteins to the lytic vacuole; it has been suggested that this protein also mediates targeting to the storage vacuole. PV72 and AtVSR1 may mediate transport of seed storage proteins to protein storage vacuoles. The significance of the PA domain to VSRs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
NFGLPQYGGTLTGVVVYPKENRTGCKEFDVFFKPKKSEPGRRPVILLLDRGGCFFTLKAWNAQQAGAAAV
LVADNVDEPLLTMDTPEESGSADYIEKITIPSALITKAFGEKLKKAISNGEMVVIKL
>gnl|CDD|239041 cd02126, PA_EDEM3_like, PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This group contains various PA domain-containing proteins similar to mouse EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein). EDEM3 contains a region, similar to Class I alpha-mannosidases (gylcosyl hydrolase family 47), N-terminal to the PA domain. EDEM3 accelerates glycoprotein ERAD (ER-associated degradation). In transfected mammalian cells, overexpression of EDEM3 enhances the mannose trimming from the N-glycans, of a model misfolded protein [alpha1-antitrypsin null (Hong Kong)] as well as, from total glycoproteins. Mannose trimming appears to be involved in the selection of ERAD substrates. EDEM3 has a different specificity of trimming than ER alpha-mannosidase 1. The significance of the PA domain to EDEM3 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
TAGPAQFGMDLTGDKAGVGRVVKAKPYRACSEITNAEEVKGKIAIMERGDCMFVEKARRVQKAGAIGGIV
IDNNEGSSSDTAPMFAMSGDGDSTDDVTIPVVFLFSKEGSKLLAAIKEHQNVEVLL
>gnl|CDD|239042 cd02127, PA_hPAP21_like, PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted glycoprotein hPAP21 (human protease-associated domain-containing protein, 21kDa). This group contains various PA domain-containing proteins similar to hPAP21. Complex N-glycosylation may be required for the secretion of hPAP21. The significance of the PA domain to hPAP21 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
DFGTIFNTRYKHVPLVPADPLEACEELRNIHDINGNIALIERGGCSFLTKAINAQKAGALAVIITDVNND
SDEYYVEMIQDDSSRRADIPAAFLLGKNGYMIRKTLERLGLPYAIINI
>gnl|CDD|239043 cd02128, PA_TfR, PA_TfR: Protease-associated domain containing proteins like transferrin receptor (TfR). This group contains various PA domain-containing proteins similar to human TfR1 and TfR2. TfR1 and TfR2 are type II membrane proteins, belonging to the peptidase M28 family. TfR1 is homodimeric, widely expressed, and a key player in the uptake of iron-loaded transferrin (Tf) into cells. The TfR1 homodimer binds two molecules of Tf and this complex is internalized. In addition to its role in iron uptake, TfR1 may participate in cell growth and proliferation. TfR2 also binds Tf but with a significantly lower affinity than does TfR1. TfR2 is expressed chiefly in hepatocytes, hematopoietic cells, and duodenal crypt cells; its expression overlaps with that of hereditary hemochromatosis protein (HFE). TfR2 is involved in iron homeostasis. HFE and TfR2 interact in cells. By one model for serum iron sensing, at low or basal iron concentrations, HFE and TFR1 form a complex at the plasma membrane; at increased Tf, Tf competes with HFE for binding of TfR1, resulting in HFE disassociating from TfR1 and associating with TfR2 . The TfR1-TfR2 association might initiate a signal cascade leading to the induction of hepcidin (a small peptide hormone that controls systemic iron levels). Human mutations in TfR2 are associated with a form of hemochromatosis (HFE3). The significance of the PA domain to TfRs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
SVIIGDAGRLNELVENPGGYVAYSAAGTVTGKLVYANYGRKKDFEDLQSVGVSVNGSVVLVRAGKISFAE
KVANAEKLGAVGVLIYPDPADFPIDPSETALFGHVHLGTGDPYTPGFPSFNHTQFPPSQSSGLPNIPAQT
ISAAAAAKLLSKMGGPVCPSGWKGGDSTCRLGTSSSKNVKLTV
>gnl|CDD|239044 cd02129, PA_hSPPL_like, PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like (hSPPL)-like. This group contains various PA domain-containing proteins similar to hSPPL2a and 2b. These SPPLs are GxGD aspartic proteases. SPPL2a is sorted to the late endosomes, SPPL2b to the plasma membrane. In activated dendritic cells, hSPPL2a and 2b catalyze the intramembrane proteolysis of tumor necrosis factor alpha triggering IL-12 production. hSPPL2a and 2b may have a broad substrate spectrum. The significance of the PA domain to these SPPLs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAE
GLLIVSRERLVPPSGNRSEYEKIDIPVALLSYKDMLDIQQTFGDSVKVAM
>gnl|CDD|239045 cd02130, PA_ScAPY_like, PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae aminopeptidase Y (ScAPY). This group contains various PA domain-containing proteins similar to the S. cerevisiae APY, including Trichophyton rubrum leucine aminopeptidase 1(LAP1). Proteins in this group belong to the peptidase M28 family. ScAPY hydrolyzes amino acid-4-methylcoumaryl-7-amides (MCAs). ScAPY more rapidly hydrolyzes dipeptidyl-MCAs. Hydrolysis of amino acid-MCAs or dipeptides is stimulated by Co2+ while the hydrolysis of dipeptidyl-MCAs, tripeptides, and longer peptides is inhibited by Co2+. ScAPY is vacuolar and is activated by proteolytic processing. LAP1 is a secreted leucine aminopeptidase. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
SLSANGEAIPTTAFTYSPAGEVTGPLVVVPNLGCDAADYPASVAGNIALIERGECPFGDKSALAGAAGAA
AAIIYNNVPAGGLSGTLGEPSGPYVPTVGISQEDGKALVAALANGGEVSANL
>gnl|CDD|239046 cd02131, PA_hNAALADL2_like, PA_hNAALADL2_like: Protease-associated domain containing proteins like human N-acetylated alpha-linked acidic dipeptidase-like 2 protein (hNAALADL2). This group contains various PA domain-containing proteins similar to hNAALADL2. The function of hNAALADL2 is unknown. This gene has been mapped to a chromosomal region associated with Cornelia de Lange syndrome. The significance of the PA domain to hNAALADL2 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
DLLYSYAAYSAKGTLQAEVVDVQYGSVEDLRRIRDNMNVTNQIALLKLGQAPLLYKLSLLEEAGFGGVLL
YVDPCDLPKTRHTWHQAFMVSLNPGGDPSTPGYPSADQSCRQCRGNLTSLLVQPISAYLAKKLLSAPPSR
RKEGSCVPLALPS
>gnl|CDD|239047 cd02132, PA_GO-like, PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on protein GRO10. This group contains various PA domain-containing proteins similar to the functionally uncharacterized Arabidopsis GRO10. The PA domain may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
PFQLVKVQNWVDGDEGDELVGVTARFGASLPSKEDNANKTRAVLANPLDCCSPSTSKLSGSIALVERGEC
AFTEKAKIAEAGGASALLIINDQEELYKMVCEDNDTSLNISIPVVMIPQSAGDALNKSLDQGKKVEVLL
>gnl|CDD|239048 cd02133, PA_C5a_like, PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a peptidase. This group contains various PA domain-containing proteins similar to S. pyogenes C5a, including, i) Vpr, a minor extracellular serine protease from Bacillus subtilis, ii) a large molecular mass collagenolytic protease from Geobacillus collagenovorans MO-1, and iii) PrtS, a cell envelope protease from Streptococcus thermophilus CNRZ 385. Proteins in this group belong to the peptidase S8 family. C5a peptidase is a cell surface serine protease which specifically inactivates C5a [a chemotactic peptide, which attracts polymorphonuclear leukocytes (PMNs)], by cleaving it to release a 7-residue carboxy-terminal fragment which contains the PMN binding site. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
GTLTSGNETLKLMPAFSGNPTDLLGKTYELVDAGLGTPEDFEGKDVKGKIALIQRGEITFVEKIANAKAA
GAVGVIIYNNVDGLIPGTLGEAVFIPVVFISKEDGEALKAALESSKKLTFNTKKEKATNPDLADFSSRGP
WGP
>gnl|CDD|411779 cd02134, KH-II_NusA_rpt1, first type II K-homology (KH) RNA-binding domain found in transcription termination/antitermination protein NusA and similar proteins. NusA, also called N utilization substance protein A or transcription termination/antitermination L factor, is an essential multifunctional transcription elongation factor that participates in both transcription termination and antitermination. NusA anti-termination function plays an important role in the expression of ribosomal rrn operons. During transcription of many other genes, NusA-induced RNA polymerase pausing provides a mechanism for synchronizing transcription and translation. In prokaryotes, the N-terminal RNA polymerase-binding domain (NTD) is connected through a flexible hinge helix to three globular domains, the S1 and two K-homology (KH), KH1 and KH2. The KH domains of NusA belong to the type II KH RNA-binding domain superfamily. This model corresponds to the first KH domain of NusA and similar proteins
HPEFLKRLFELEVPEIADGIVEIKAIAREPGSRTKVAVASNDPRVDPVGACVGVRGSRIQAIVEELGGEK
IDIVLW
>gnl|CDD|380312 cd02135, YdjA-like, nitroreductase family protein similar to Escherichia coli YdjA. A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to nitroreductase YdjA from Escherichia coli. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer. Members of this family are also called NADH dehydrogenase, oxygen-insensitive NAD(P)H nitrogenase or dihydropteridine reductase
LELIKTRRSIRKFKLTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGEGRERLAELLAAAAAARAPG
ADPEKLEKAREKALRAPVVIAVVAKPDEDPKVPEWEQYAAVGAAVQNLLLAAHALGLGAVWRTGPVTYDP
AVREALGLPEDERIVGFLYLGT
>gnl|CDD|380313 cd02136, PnbA_NfnB-like, nitroreductase similar to Mycobacterium smegmatis NfnB. Members of this family utilize FMN as a cofactor and catalyze reduction of a variety of nitroaromatic compounds, including nitrofurans, nitrobenzens, nitrophenol, nitrobenzoate and quinones by using either NADH or NADPH as a source of reducing equivalents in an obligatory two-election transfer mechanism. The enzyme is typically a homodimer. Mycobacterium smegmatis nitroreductase NfnB plays a role in resistance to benzothiazinone
AIKSRRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTGKARERLKKAFFGAPVALFLTMDK
VLGPWSWFDLGAFLQNLMLAAHALGLGTCPQGALAGYPDVVRKELGIPDDEELVCGIALGYPDPDAPVNQ
FRTPREPLEEFV
>gnl|CDD|380314 cd02137, MhqN-like, nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN. A diverse subfamily of the nitroreductase family containing uncharacterized proteins; includes nitroreductases MhqN, YodC, YdgI, DrgA. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer
LEVIKSRRSVRNFDPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAAYNQPQVTTA
SAVILVLGDLNAGLAAMNLMLAAKAKGYDTCPMGGFDKEKVAELLNLPDRYVPVLLIAIGKAADKAPRSG
RLPVDEV
>gnl|CDD|380315 cd02138, TdsD-like, nitroreductase similar to Burkholderia pseudomallei TdsD. A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to Burkholderia pseudomallei TdsD, may be involved in the processing of organosulfur compounds. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer
LIAERWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFVVARRDTEAFEKLLDLLAEGNQSWAKNA
PVLIVVLAKTEFDHNGKPNRYALFDTGAAVANLALQATALGLVVHQMAGFDPEKAKEALGIPDEYEPITM
IAIGYPGDPESLPEKLLEREEAPRTRKPLSEIVF
>gnl|CDD|380316 cd02139, nitroreductase, nitroreductase family protein. A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer
VYEAIKKRRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLAEAANGQKFIAEA
PVVIVACADPSESGMGCGKPYYLVDVAIAMEHLVLAATEEGLGTCWIGAFDEDKVKEILGIPEEYRVVAL
TPLGYPAEEPPPRPRKPLEEIVFYE
>gnl|CDD|380317 cd02140, Frm2-like, nitroreductase family protein. A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to nitroreductase. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer. Members of this family are also called NADH dehydrogenase, oxygen-insensitive NAD(P)H nitrogenase or dihydropteridine reductase
FLEAAKARRTIYALGKNSPVSDEEIEEIVKEAVKHVPSSFNSQSSRAVILLGDEHKKLWDIVKDTLRPLV
PAEAFEATKEKLNGFKAGYGTVLFFEDQDVVKGLQEQFPAYADNFPVWSEQSSGMAQIAVWTALALEGIG
ANLQHYNPLIDAAVAKKWNIPSNWKLRAQLVFGSPEAPPGEKTFIPDEDRVK
>gnl|CDD|380318 cd02142, McbC_SagB-like_oxidoreductase, oxidase similar to the microcin B17 processing protein McbC. This family is the oxidase domain of NRPS (non-ribosomal peptide synthetase) and other systems that modify polypeptides by cyclizing a thioester to form a ring. These include EpoB, part of the epothilone biosynthesis pathway; TubD, part of the tubulysin biosynthesis pathway, MtsD, part of the myxothiozol biosynthesis pathway; IndC, part of the indigoidine biosynthesis pathway and TfxB, part of the trifitoxin processing pathway. All are FMN-dependent and oxidize the product of the cyclization of thioesters in short polypeptides
KSVPLPDPNLKPALLATLDLSEALLNRRSRRTFSSEPLTLRELSRLAARGIPGSGYGLRPYPSAGALYPI
EVYVIVKNVEGLPAGIYHYDPKRHRLVLIREGDFRLDLAHAAGNQAAFGSAAFSLIIVARFERIAWKYGE
RAYRYILLEAGHLAQNLYLAATALGLGLCAIGAFDDDALRELLGLDEVEEVVLYAFVVGG
>gnl|CDD|380319 cd02143, nitroreductase_FeS-like, nitroreductases with an N-terminal iron-sulfur cluster-binding domain. Members of this family utilize FMN as a cofactor. This family may be involved in the reduction of flavin or nitroaromatic compounds via an obligatory two-electron transfer. Nitroreductase is homodimer. Each subunit contains one FMN molecule
LLRSRRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLAELVIDWMRELIKEDP
ELAGKLFLDGIVAAWEKGIDVILRGAPHLVVAHAPKDAPTPPVDCAIALTYLELAAPSLGLGTCWAGFFT
AAANNYPPLREALGLPEGHKVGGAMMLGYPKYKYHRIPPRKPARVTW
>gnl|CDD|380320 cd02144, iodotyrosine_dehalogenase, iodotyrosine dehalogenase. Iodotyrosine dehalogenase catalyzes the removal of iodine from the 3, 5 positions of L-tyosine in thyroid, liver and kidney, using NADPH as electron donor. This enzyme is a homolog of the nitroreductase family. These enzymes are usually homodimers
FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREAAEEEEKEFYE
KRMGEEWVWDLKPLGTNWEKPYLTEAPYLIVVFKQKYGVLPDGKKKKHYYNEESVGIAVGILLAALHNAG
LVTLTHTPSPMPFLRDLLGRPKNEKPLLLLPVGYPAEDATVPDLKRKPLEEI
>gnl|CDD|380321 cd02145, BluB, 5,6-dimethylbenzimidazole synthase. BluB catalyzes the O2-dependent conversion of FMNH2 to 5,6-dimethylbenzimidazole (DMB), a component of vitamin B12; is is a subfamily of the nitroreductase family; nitroreductases typically reduce their substrates by using NAD(P)H as electron donor and often use FMN as a cofactor
YRVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRANAEAAEM
YTGERAAQYRTLKLEGIEEAPLQLAVFCDRARAGGHGLGRTTMPEMDLYSSVCAVQNLWLAARAEGLGVG
WVSILDPDEVKRLLGIPEHWEPVAYLCIGYPEFFYDEPELEQAGWEQRRPLEWVVF
>gnl|CDD|380322 cd02146, NfsA-like, nitroreductase similar to Escherichia coli NfsA. This family contains NADPH-dependent flavin reductase and oxygen-insensitive nitroreductase. These enzymes are homodimeric flavoproteins that contain one FMN per monomer as a cofactor. Flavin reductase catalyzes the reduction of flavin by using NADPH as an electron donor. Oxygen-insensitive nitroreductase, such as NfsA protein in Escherichia coli, catalyzes reduction of nitrocompounds using NADPH as electron donor
TIETILNHRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAELAGNQPYVAQA
PVFLVFCADLYRHQKIAEEAGGKDVGLDYLESFLVGVVDAALAAQNALVAAESLGLGIVYIGGIRNNPEE
VIELLGLPEYVFPLFGLTVGHPDPTPEVKPRLPLEAVVHEETYQDLTDLEDLAAYDETMSEYYAERGSNK
RTETWSQQIADRYLSKRDR
>gnl|CDD|380323 cd02148, RutE-like, nitroreductase similar to Escherichia coli RutE. A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to nitroreductase. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer. RutE is involved in the utilization of uracil as the sole nitrogen source; it appears to have the same function as YdfG, which reduces malonic semialdehyde to 3-hydroxypropionic acid
ALDQLFTEARTHNAWEDKPVSDEELRAIYDLAKWGPTAANCSPARIVFVRSAEAKERLVPHLSEGNREKT
MAAPVTAILAYDTEFYEHLPRLFPHGDARSWFFGSGPARAEETAFRNASLQAAYFILAARALGLDCGPMS
GFDAAGVDAEFFAGTRWKSNLVVNLGYGDPSKLFPRLPRLDFDEAC
>gnl|CDD|380324 cd02149, NfsB-like, nitroreductase similar to Escherichia coli NfsB. NAD(P)H:FMN oxidoreductase family. This domain catalyzes the reduction of flavin, nitrocompound, quinones and azo compounds using NADH or NADPH as an electron donor. The enzyme is a homodimer, and each monomer binds a FMN as co-factor. This family includes FRase I in Vibrio fischeri, wihich reduces FMN into FMNH2 as part of the bioluminescent reaction. The family also includes oxygen-insensitive nitroreductases that use NADH or NADPH as an electron donor in the ping pong bi bi mechanism. This type of nitroreductase can be used in cancer chemotherapy to activate a range of prodrugs
NILELLNFRYATKKFDPNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAPAAWFNQPQI
KDASHVVVFLAKKDWSAKQTYIALGNMLLAAAMLGIDSCPIEGFDPAKLDEILGLDEKGYKISVMVAFGY
RSEEKLPKSRKPLEDV
>gnl|CDD|380325 cd02150, nitroreductase, nitroreductase family protein. A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers
ILTRRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKIAEAHPYGKMLKEAPLAI
VVCGDPSKEKAPGYWVQDCSAATENILLAAHALGLGAVWLGVYPFEERVKAIREILNIPENIIPFCVIAL
GYPAEEKEPKDRFDEE
>gnl|CDD|380326 cd02151, nitroreductase, nitroreductase family protein. A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers
ELLKKRRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKLSECKPHGSAFLKGAP
AAIVVLADTEKSDTWIEDASIAATYIQLAAESLGLGSCWIQIRNRETQDGKTAEEYVRELLGIPENYRVL
CIIALGYPDEEKPPHED
>gnl|CDD|239065 cd02152, OAT, Ornithine acetyltransferase (OAT) family; also referred to as ArgJ. OAT catalyzes the first and fifth steps in arginine biosynthesis, coupling acetylation of glutamate with deacetylation of N-acetylornithine, which allows recycling of the acetyl group in the arginine biosynthetic pathway. Members of this family may experience feedback inhibition by L-arginine. The active enzyme is a heterotetramer of two alpha and two beta chains, where the alpha and beta chains are the result of autocatalytic cleavage. OATs found in the clavulanic acid biosynthesis gene cluster catalyze the fifth step only, and may utilize acetyl acceptors other than glutamate
PKGFRAAGVAAGIKKSGRKDLALIYSDVPATAAGVFTTNKFKAAPVLVSREHLADGKARAVVVNSGNANA
CTGEQGLEDAREMAELVAELLGIPEEEVLVASTGVIGEPLPMDKIRAGIPELVASLSEDGWEAAARAIMT
TDTFPKEAAVEVEIGGKTVTIGGIAKGSGMIHPNMATMLGFITTDAAISPELLQDALRRAVDRSFNRITV
DGDTSTNDTVLLLANGAAGNPPISEEDPDLEEFEEALTEVCLDLAKQIVRDGEGATKLIEVTVTGAASEE
DARKVARAIANSPLVKTAIFGEDPNWGRILAAVGYSGVEFDPERVSISLGGVLVVENGEPLDYDEAAASA
VMKEDEITITVDLGRGDGSATVWGCDLTYDYVKINADYRT
>gnl|CDD|239066 cd02153, tRNA_bindingDomain, The tRNA binding domain is also known as the Myf domain in literature. This domain is found in a diverse collection of tRNA binding proteins, including prokaryotic phenylalanyl tRNA synthetases (PheRS), methionyl-tRNA synthetases (MetRS), human tyrosyl-tRNA synthetase(hTyrRS), Saccharomyces cerevisiae Arc1p, Thermus thermophilus CsaA, Aquifex aeolicus Trbp111, human p43 and human EMAP-II. PheRS, MetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. The molecular chaperones Trbp111 and CsaA also contain this domain. CsaA has export related activities; Trbp111 is structure-specific recognizing the L-shape of the tRNA fold. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. An EMAP-II-like cytokine is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain. For homodimeric members of this group which include CsaA, Trbp111 and Escherichia coli MetRS this domain acts as a dimerization domain
LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGM
LLSAEELGLEEGSVGILELPEDAPVGDRI
>gnl|CDD|173912 cd02156, nt_trans, nucleotidyl transferase superfamily. nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain
KARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPPVKVWQDPHELEERKESIEEDISVCGEDFQQNR
ELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK
>gnl|CDD|173914 cd02163, PPAT, Phosphopantetheine adenylyltransferase. Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli
IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGL
LVDFARKHGANVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVS
GFVPPVVAKALKE
>gnl|CDD|173915 cd02164, PPAT_CoAS, phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes. The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD
KVAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTL
KYEIVPIDDPYGPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVKADEDGEKISSTRI
RRG
>gnl|CDD|185680 cd02165, NMNAT, Nicotinamide/nicotinate mononucleotide adenylyltransferase. Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis
IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDNPKFEVSD
IEIKRDGPSYTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLE
KLLLPGGRIILLDNPLLNISSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY
>gnl|CDD|173917 cd02166, NMNAT_Archaea, Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal. This family of archaeal proteins exhibits nicotinamide-nucleotide adenylyltransferase (NMNAT) activity utilizing the salvage pathway to synthesize NAD. In some cases, the enzyme was tested and found also to have the activity of nicotinate-nucleotide adenylyltransferase an enzyme of NAD de novo biosynthesis, although with a higher Km. In some archaeal species, a number of proteins which are uncharacterized with respect to activity, are also present
RALFIGRFQPFHLGHLKVIKWILEEVDELIIGIGSAQESHTLENPFTAGERVLMIRRALEEEGIDLSRYY
IIPVPDIERNSLWVSYVESLTPPFDVVYSGNPLVARLFKEAGYEVRRPPMFNREEYSGTEIRRLMLGGED
WEELVPKSVAEVIKEIGGVERLR
>gnl|CDD|173918 cd02167, NMNAT_NadR, Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins. NMNAT domain of NadR protein. The NadR protein (NadR) is a bifunctional enzyme possessing both NMN adenylytransferase (NMNAT) and ribosylnicotinamide kinase (RNK) activities. Its function is essential for the growth and survival of H. influenzae and thus may present a new highly specific anti-infectious drug target. The N-terminal domain that hosts the NMNAT activity is closely related to archaeal NMNAT. The bound NAD at the active site of the NMNAT domain reveals several critical interactions between NAD and the protein.The NMNAT domain of hiNadR defines yet another member of the pyridine nucleotide adenylyltransferase
IGIVFGKFAPLHTGHVYLIYKALSQVDELLIIVGSDDTRDDARTGLPLEKRLRWLREIFPDQENIVVHTL
NEPDIPEYPNGWDIWSNRVKTLIAENTRCRPDIVFTAEEYEAAFELVLAYLGAQVVLVDPDRTDISVSAT
QIRENPFRYWYHIPREVR
>gnl|CDD|173919 cd02168, NMNAT_Nudix, Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional proteins, also containing a Nudix hydrolase domain. N-terminal NMNAT (Nicotinamide/nicotinate mononucleotide adenylyltransferase) domain of a novel bifunctional enzyme endowed with NMN adenylyltransferase and Nudix hydrolase activities. This domain is highly homologous to the archeal NMN adenyltransferase that catalyzes NAD synthesis from NMN and ATP. NMNAT is an essential enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. The C-terminal domain of this enzyme shares homology with the archaeal ADP-ribose pyrophosphatase, a member of the 'Nudix' hydrolase family
YLVYIGRFQPFHNGHLAVVLIALEKAKKVIILIGSARTARNIKNPWTSEEREVMIEAALSDAGADLARVH
FRPLRDHLYSDNLWLAEVQQQVLEIAGGSASVGLVGHRKDASSYYLRSFPQWDYLEVPNYPDLNATDIRR
AYFEGKEAMYRAALPAGVYDFLTAFQDTPRYAQLVAEYRAI
>gnl|CDD|173920 cd02169, Citrate_lyase_ligase, Citrate lyase ligase. Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction
DLSLDYTVGIFDDAGELIATGSIAGNVLKCVAVCPKYQGEGLALKIVSELINKAYEEGIFHLFLFTKPKN
AKFFRGLGFKELANASDEAVLLENGKPGIEDYLKNLPKPDQPGKKIAAIVMNANPFTLGHRYLVEKAAAE
NDWVHLFVVSEDKSLFSFADRFKLVKKGTKHLKNVTVHSGGDYIISSATFPSYFIKEQDVVIKAQTALDA
RIFRKYIAPALNITKRYVGEEPFSRVTAIYNQTMQEELLSPAIEVIEIERKKYDGQPISASTVRQLLKEG
NLEEIAKLVPETTYEFL
>gnl|CDD|173921 cd02170, cytidylyltransferase, cytidylyltransferase. The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates
MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVIL
GHPWSYFKPLEELKPDVIVLGDDQKNGVDEEEVYEELKKRGKVIEVPRKKTEGISSSDIIKRILEL
>gnl|CDD|173922 cd02171, G3P_Cytidylyltransferase, glycerol-3-phosphate cytidylyltransferase. Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase
MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIP
ETNWEQKIEDIKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEMLKKL
>gnl|CDD|173923 cd02172, RfaE_N, N-terminal domain of RfaE. RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose
QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDY
VVLFDNPTALEIIDALQPNIYVKGGDYENPENDVTGKIAPEAEAVKAYGGKIVFTGEIVFSSSALINRIF
DELD
>gnl|CDD|173924 cd02173, ECT, CTP:phosphoethanolamine cytidylyltransferase (ECT). CTP:phosphoethanolamine cytidylyltransferase (ECT) catalyzes the conversion of phosphoethanolamine to CDP-ethanolamine as part of the CDP-ethanolamine biosynthesis pathway. ECT expression in hepatocytes is localized predominantly to areas of the cytoplasm that are rich in rough endoplasmic reticulum. Several ECTs, including yeast and human ECT, have large repetitive sequences located within their N- and C-termini
GDKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDE
VVIGAPYVITKELIEHFKIDVVVHGKTEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKN
RLAYEARNKKKE
>gnl|CDD|173925 cd02174, CCT, CTP:phosphocholine cytidylyltransferase. CTP:phosphocholine cytidylyltransferase (CCT) catalyzes the condensation of CTP and phosphocholine to form CDP-choline as the rate-limiting and regulatory step in the CDP-choline pathway. CCT is unique in that its enzymatic activity is regulated by the extent of its association with membrane structures. A current model posts that the elastic stress of the bilayer curvature is sensed by CCT and this governs the degree of membrane association, thus providing a mechanism for both positive and negative regulation of activity
RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDE
VVEGAPYVTTPEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYR
DYHRRNLQRG
>gnl|CDD|185684 cd02175, GH16_lichenase, lichenase, member of glycosyl hydrolase family 16. Lichenase, also known as 1,3-1,4-beta-glucanase, is a member of glycosyl hydrolase family 16, that specifically cleaves 1,4-beta-D-glucosidic bonds in mixed-linked beta glucans that also contain 1,3-beta-D-glucosidic linkages. Natural substrates of beta-glucanase are beta-glucans from grain endosperm cell walls or lichenan from the Islandic moss, Cetraria islandica. This protein is found not only in bacteria but also in anaerobic fungi. This domain includes two seven-stranded antiparallel beta-sheets that are adjacent to one another forming a compact, jellyroll beta-sandwich structure
FFEDFNSLDTGRWYKSDGWSNGGPFNCTWSADNVEFSDGGLALTLTNDTYGEKPYACGEYRTRGFYGYGR
YEVRMKPAKGSGVVSSFFTYTGPYDGDPHDEIDIEFLGKDTTKVQFNYYTNGVGGHEKLIDLGFDASEGF
HTYAFEWEPDSIRWYVDGELVHEATATDPNIPDTPGKIMMNLWPGDGVDDWLGPFDGGTPLTAEYDWVSY
TP
>gnl|CDD|185685 cd02176, GH16_XET, Xyloglucan endotransglycosylase, member of glycosyl hydrolase family 16. Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers in plant cell walls via a transglycosylation mechanism. Xyloglucan is a soluble hemicellulose with a backbone of beta-1,4-linked glucose units, partially substituted with alpha-1,6-linked xylopyranose branches. It binds noncovalently to cellulose, cross-linking the adjacent cellulose microfibrils, giving it a key structural role as a matrix polymer. Therefore, XET plays an important role in all plant processes that require cell wall remodeling
AVAASFDENFFVTWGPDHIRVSNDGTSVQLTLDQSSGSGFKSKNKYLFGFFSMRIKLPPGDSAGTVTAFY
LSSQGPDNHDEIDFEFLGNVTGQPYTLQTNVFANGVGGREQRIYLWFDPTADFHTYSILWNPHQIVFYVD
DVPIRVFKNNEALGVPYPSSQPMGVYASIWDGSDWATQGGRVKIDWSYAPFVASYRDFKLDGCVVDPGDS
FSSCSCTEDWWNGSTYQQLSANQQRAMEWVRRNYMVYDYCDDRKRYPVPPPEC
>gnl|CDD|185686 cd02177, GH16_kappa_carrageenase, Kappa-carrageenase, member of glycosyl hydrolase family 16. Kappa-carrageenase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of kappa-carrageenans, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Carrageenans are linear chains of galactose units linked by alternating D-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Depending on the position and number of sulfate ester modifications they are subdivided into kappa-, iota-, and lambda-carrageenases, kappa being modified once. Carrageenans form thermo-reversible gels widely used for industrial applications. Kappa-carrageenases exist in bacteria belonging to at least three phylogenetically distant branches, including pseudoalteromonas, planctomycetes, and baceroidetes. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold
TAKPGEQWTIKWSRSDEFNKNDPDWAKWNKTGENTGAWKWNNEKNVVISNGILELTMRRNANNTTFWDQQ
QVPDGPTYFTSGIFKSYAKGTYGYYEARIKGADIFPGVCPSFWLYSDIDYSVANEGEVVYSEIDVVELQQ
FDWYHQDDIRDMDHNLHAIVKENGQGVWKRPKMYPPTEQLNYHRPFDPSKDFHTYGCNVNQDEIIWYVDG
VEVGRKPNKYWHRPMNVTLSLGLRKPFVKFFDNKNNAKAREKASDFPTSMYVDYVRVWE
>gnl|CDD|185687 cd02178, GH16_beta_agarase, Beta-agarase, member of glycosyl hydrolase family 16. Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold
AAADWDPIPLPDQPGGGEWELNESVSDEFNGTSLDTSKWNPNNPNGWTGRGPTEFSADNVSVEDGNLVLS
ATRHPGTELGNGYKVTTGSITSKEKVKYGYFEARAKASNLPMSSAFWLLSDTKDSTTEIDILEHYGGDRE
EWFATRMNSNTHVFIRDPEQDYQPKDDGSWYYNPTELADDFHVYGVYWKDPDTIRFYIDGVLVRTVENSE
ITDGTGFDQPMYIIIDTETYDWRGEPTDEELADDSKNTFYVDYVRVYK
>gnl|CDD|185688 cd02179, GH16_beta_GRP, beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16. Beta-GRP (beta-1,3-glucan recognition protein) is one of several pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. They are present in insects and lack all catalytic residues. This subgroup also contains related proteins of unknown function that still contain the active site. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members
LIFEENFNGALLDLNKWTIEVRFPGEPDYEFVVYDDAPENLFVKDGNLVIEPTLLEEKFGEGFVREGLDL
LERCTGQLGTTECRRDARGSSILPPVVSARINTKNSFAFKYGRVEIRAKLPKGDWIYPELLLEPVNNYYG
SSDYASGQIRIAFARGNAVLRADGTDIGGKKLYGGPVLTDAEPHRSANLKTKINNELWSDDFHVYTLEWK
PDGITLMVDGEEYGEIEPGEGGYSEAANNPAASRWLGGTVMAPFDKEFYLSLGVGVGGHNDFPDSSIRGY
VKPWKNTGPKAMLKFWQARDKWFPTWSDDSALKVDYVKVYA
>gnl|CDD|185689 cd02180, GH16_fungal_KRE6_glucanase, Saccharomyces cerevisiae KRE6 and related glucanses, member of glycosyl hydrolase family 16. KRE6 is a Saccharomyces cerevisiae glucanase that participates in the synthesis of beta-1,6-glucan, a major structural component of the cell wall. It is a golgi membrane protein required for normal beta-1,6-glucan levels in the cell wall. KRE6 is closely realted to laminarinase, a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans
LVFSDEFNVDGRTFYPGDDPFWEAVDLHYWATNDLEWYDPDAVTTINGSLRITMDQFRNHGLNFRSGMLQ
SWNKLCFTGGYIEASASLPGKPDVSGLWPAVWTMGNLGRPGYLATTEGVWPYSYDGRGAPEIDIIEAQVG
NGLGIGQVSQSLQVAPFDAWYRPDYSSDFVTIYNDTTTIMNTYTGGVFQQAISCVTRLNDSWYPGNGNEF
QTYGFEYRPDDEDDGYITWFVDDEPTWTIYAKALGPNGNIGWRIIPEEPMYIILNLGISSNFQDIDWDEL
QFPATMRIDYVRVYQ
>gnl|CDD|185690 cd02181, GH16_fungal_Lam16A_glucanase, fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Group of fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Lam16A belongs to the 'nonspecific' 1,3(4)-beta-glucanase subfamily, although beta-1,6 branching and beta-1,4 bonds specifically define where Lam16A hydrolyzes its substrates, like curdlan (beta-1,3-glucan), lichenin (beta-1,3-1,4-mixed linkage glucan), and laminarin (beta-1,6-branched-1,3-glucan)
AYTLVDSYDGSNFFDGFDFFTGDDPTHGFVNYVDQSTATSLGLAYVNSGNVYLGVDSTTTLPSGAGRNSV
RIESKKTYNTGLFIADIAHMPGGCGTWPAFWTVGPNWPNGGEIDIIEGVNLQTSNQMTLHTGPGCTISNS
GSFTGTVTTTNCDVNQNGNAGCGVTSTSTNSYGAGFNAAGGGVYAMEWTSDGIKVWFFPRGSIPADITSG
SPDPSTWGTPAASFPGSSCDIDSFFKDQRIVFDTTFCGDWAGNVWISSSGCAAKTSTCEDYVANNPSAFS
EAYWEINSIKVYQ
>gnl|CDD|185691 cd02182, GH16_Strep_laminarinase_like, Streptomyces laminarinase-like, member of glycosyl hydrolase family 16. Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel
GWTLVWSDDFDGSAGSLPSSSKWIIDTGTSANWGTGEIQTYTNSTANVQLSGNGTLQITPLRDGSGKWTS
GRIETTRTDFAAPPGGKLRVEASIRLGDVPGSNQQGIWPAFWMLGDSYRGNGTNWPACGELDIMENVNGL
STGYGTLHCGVAPGGPCNEPTGIGAGTRLCDTGFHTYAVEIDRTNGDAESIRWYLDGVVYHTVTGARVGD
ETTWQALAHHPLFIILNVAVGGNWPGAPNGNTATGSGSAMEVDYVAVYS
>gnl|CDD|185692 cd02183, GH16_fungal_CRH1_transglycosylase, glycosylphosphatidylinositol-glucanosyltransferase. Group of fungal GH16 members related to Saccharomyces cerevisiae Crh1p. Chr1p and Crh2p are transglycosylases that are required for the linkage of chitin to beta(1-3)glucose branches of beta(1-6)glucan, an important step in the assembly of new cell wall. Both have been shown to be glycosylphosphatidylinositol (GPI)-anchored. A third homologous protein, Crr1p, functions in the formation of the spore wall. They belongs to the family 16 of glycosyl hydrolases that includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues
FDFTGNASSYDWTVTSGTVDYDDDGASLTIPKRGDGPTISSTFYIFYGKVEVTMKAAPGQGIVSSFVLQS
DDLDEIDWEWVGGDLTQVQTNYFGKGNTTTYDRGGYHPVPNPQTEEFHTYTIDWTKDRITWYIDGKVVRT
LTKADTTGGYGYPQTPMRLQIGIWAGGDPSNAPGTIEWAGGETDYDKGPFTMYVKSVTVTDYS
>gnl|CDD|100026 cd02185, AroH, Chorismate mutase (AroH) is one of at least five chorismate-utilizing enzymes present in microorganisms that catalyze the rearrangement of chorismate to prephenic acid, the first committed step in the biosynthesis of aromatic amino acids. In prokaryotes, chorismate mutase may be fused to prephenate dehydratase, prephenate dehydrogenase, or 3-deoxy-D-arabino-heptulosonat-7-phosphate (DAHP) as part of a bifunctional enzyme. The AroH domain forms a homotrimer with three-fold symmetry
VRGIRGATTVEENTAEEILEATRELLEEIIERNNIKPEDIISVIFTVTPDLDAAFPAKAARELGGWKYVP
LMCAQEMDVPGSLPRCIRVLIHVNTDKAQQEIKHVYLGGAKKLRPDL
>gnl|CDD|276955 cd02186, alpha_tubulin, The alpha-tubulin family. The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins
REIISIHVGQAGVQIGNACWELFCLEHGIQPDGQMPSDKTIGGDDDNFNTFFSETGSGKYVPRAVFVDLE
PTVIDEIRTGPYRQLFHPEQLISGKEDAANNFARGYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSV
GGGTGSGLTSLLLERLSVDYGKKSKLEFSIYPSPQVSTSVVEPYNSVLTTHSLLEHSDCSILLDNEALYD
ICRRQLDIERPTYTNLNRLIAQVVSSLTASLRFDGALNVDLNEFQTNLVPYPRIHFPLVSYAPIISAEKA
NHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGF
KVGINYQPPTVVPGSDLAKVDRSVCMLANSTAIAEAFQRLDHKFDLLYSKRAFVHWYVGEGMEEGEFSEA
REDLAALEKDYEEV
>gnl|CDD|276956 cd02187, beta_tubulin, The beta-tubulin family. The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins
REIIHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPG
TIDSVRSGPYGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGG
GTGSGLGTLLLSKLREEYPDRIMSTFSVLPSPKVSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNIC
QRTLKLTQPTYDDLNHLISQVMSGITSSLRFPGQLNSDLRKLATNLVPFPRLHFLTPGFAPLTSRGSQQY
RKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRISTKEVDEQMSKVQNKNSSYFVEWIPNNVKT
SVCDIPPRGLKMSATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNLNDLISE
YQQYQ
>gnl|CDD|276957 cd02188, gamma_tubulin, The gamma-tubulin family. Gamma-tubulin is a ubiquitous phylogenetically conserved member of tubulin superfamily. Gamma is a low abundance protein present within the cells in both various types of microtubule-organizing centers and cytoplasmic protein complexes. Gamma-tubulin recruits the alpha/beta-tubulin dimers that form the minus ends of microtubules and is thought to be involved in microtubule nucleation and capping
REIITLQVGQCGNQIGSEFWKQLCSEHGISPDGSLEDFATDGNDRKDVFFYQADDEHYIPRAILLDLEPR
VINSIQNSPYKNLFNPENIYLSKEGGGAGNNWASGYSQGEKVQEEILDIIDREAEGSDSLEGFVLCHSIA
GGTGSGMGSYLLERLSDRYPKKLIQTYSVFPNQEESSDVVVQPYNSILTLKRLTLNADCVVVLDNTALNR
IATDRLKIDNPSFSQINSLISTVMSASTSTLRFPGYMNNDLVSLISSLIPTPRLHFLMTSYTPLTSDQVA
SSVRKTTVLDVMRRLLQPKNRMVSTSTKNGCYISILNIIQGEVDPTQVHKSLQRIRERKLANFIPWGPAS
IQVALSKKSPYVQTAHRVSGLMLANHTSISSLFEKILSQYDKLRKRNAFLENYRKEDMFQDNLEEFDESR
EVVQSLIDEY
>gnl|CDD|276958 cd02189, delta_zeta_tubulin-like, The delta- and zeta-tubulin families. The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. Delta-tubulin plays an essential role in forming the triplet microtubules of centrioles and basal bodies
SIVTVQVGQCGNQLGDELFDTLADEADSSASEGDQNSSATRFFSPFSDGKLKARCVLVDMEPKVVQQVLS
RARSGAWSYDPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSG
LGSRVTELLRDEYPKAYLLNTVVWPYSSGEVPVQNYNTLLTLSHLQESSDGILLFENDDLHKICSKLLGL
KNPVSFSDINRVIARQLAGVLLPSSSPTSPSPLRRCPLGDLLEHLCPHPAYKLLTLRSLPQMPEPSRAFS
TYTWPSLLKRLRQMLITGAKLEEGIDWQLLDTSGSHNPNKSLAALLVLRGKDAMKVHSADLSAFKDPVLY
SPWVPNPFNVSVSPRPFNGYEKSVTLLSNSQNIVGPLDSLLEKAWQMFKAGAYLHQYEKYGVEEEDFLDA
FATLEQIIAAYKS
>gnl|CDD|276959 cd02190, epsilon_tubulin, The epsilon-tubulin family. The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The epsilon-tubulins which are widespread but not ubiquitous among eukaryotes play a role in basal body/centriole morphogenesis
REIITVQVGQCGNQIGCRFWDLALREHAAYNKDGVYDDSMSSFFRNVDTRSGDPGDDGGSPIKSLKARAV
LIDMEEGVVNELLKGPLGDLFDETQLVTDVSGAGNNWAHGYHEYGPQYGESILEKLRRAAEKCDSLQSFF
LLHSLGGGTGSGLGSYILELLEDEFPDVYRFVTSVFPSGDDDVITSPYNSVLALRELTEHADCVLPVENQ
ALMDIVNKIKSSKDKGKTGVLAAINSSGGGQKKGKKKPFDDMNNIVANLLLNLTSSMRFEGSLNVDLNEI
TTNLVPFPRLHFLLSSLSPLYALADVRLPPRRLDQMFSDAFSRDHQLLKADPKHGLYLACALLVRGNVSI
SDLRRNIDRLKRQLKFVSWNQDGWKIGLCSVPPVGQPYSLLCLANNTCIKPTFTEMHERFDKLYKRKAHL
HHYTQYMEQDDFDEALESLLDLIEEYKDL
>gnl|CDD|276960 cd02191, FtsZ_CetZ-like, Subfamily of FitZ and Cell-structure-related euryarchaeota tubulin/FtsZ homolog-like. FtsZ is a GTPase that is similar to the eukaryotic tubulins and is essential for cell division in prokaryotes. CetZ-like proteins are related to tubulin and FtsZ and co-exists with FtsZ in many archaea. However, a recent study found that Cetz proteins (formerly annotated FtsZ type 2) are not required for cell division. Instead, CetZ proteins are shown to be involved in controlling archaeal cell shape dynamics. The results from inactivation studies of CetZ proteins in Haloferax volcanii suggest that CetZ1 is essential for normal swimming motility and rod-cell development
AKIVVIGVGQAGGNLASALQSFDRETGFGAGVETVAINTAAQDLKSLKAKETLLIGQDRTNGHGVGGNPE
LGAQAAEEDQEEIMEALEGRVEADMIFVTTGLGGGTGSGGAPVLAEALKKVYDVLTVAVVTLPFADEGAL
YMQNAGEGLRTLAEEADALILVDNEKLRSIGGSLSEAYDAINEVLARRVGGLLEAIEATGLSVVDFADVK
TVMNSGGMAMLGYGSADASINRAREATRRALRTPLLLPDASGADGALVVIAGEPDTLPLKEVERVRRWVE
DETGSATVRGGDVIDESGRLRVLVVLTG
>gnl|CDD|100028 cd02192, PurM-like3, AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain
LRAFEGVTRKRDIQDVVAILPDAPFDSLGVAADLGDDAAAIPDGDGYLLLAADGIWPSLVEADPWWAGYC
SVLVNVSDIAAMGGRPLAMVDALWSPSAEAAAQVLEGMRDAAEKFGVPIVGGHTHPDSPYNALSVAILGR
ARKDLLISFGAKPGDRLILAIDLDGRVHPSPPPNWDATTMKSPALLRRQIALLPELAERGLVHAAKDISN
PGIIGTLGMLLEASGVGAEIDLDAIPRPEGVDLERWLKCFPGFGFLLTARPENADEVVAVFAAVGITAAV
IGE
>gnl|CDD|100029 cd02193, PurL, Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM
YGEAMKIEEHNHPAAIDPAAGAATGVGGAIRDIAATGIDAKPIALSANWMASAGHPGEDAILYDAVKGVA
ELCNQLGLPIPVGKDRMSMKTRWQEGNEQREMTHPPSLVISAFGRVRDDRHTLPQLSTEGNALLLIGGGK
GHNGLGGTALASVALSYRQLGDKSAQVRDPAQEKGFYEAMQALVAAGKLLAWHDRGAGGLLVALAELVFA
GHCGVQVDLAALGDDEPDMEPLEIALFESQERGVIQVRAEDRDAVEEAQYGLADCVHVLGQA
>gnl|CDD|100030 cd02194, ThiL, ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage of exogenous thiamine. Thiamine salvage occurs in two steps, with thiamine kinase catalyzing the formation of thiamine phosphate, and ThiL catalyzing the conversion of this intermediate to thiamine pyrophosphate. The N-terminal domain of ThiL binds ATP and is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, FGAM synthase and selenophosphate synthetase (SelD)
GEFELIDRLFKRLGAGPGVLLGIGDDAAVLKPPGGRLVVTTDTLVEGVHFPPDTTPEDIGWKALAVNLSD
LAAMGARPLGFLLSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELVISVTALGEVEKGKP
LRRSGAKPGDLLYVTGTLGDAAAGLALLLGGLKLPEELYEELIERHLRPEPRLELGRALAEGLATAMIDI
SDGLLADLGHIAEASGVGAVIDLDKLPLSPALRAAELGEDALELALSGGEDYELLFTVPPENAEAAAAKL
GVPVTVIGRVT
>gnl|CDD|100031 cd02195, SelD, Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate which is required by a number of bacterial, archaeal and eukaryotic organisms for synthesis of Secys-tRNA, the precursor of selenocysteine in selenoenzymes. The N-terminal domain of SelD is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, and FGAM synthase and is thought to bind ATP
LTSFMKCAGCGAKVGPGVLSQLLAGLPLPTDPNLLVGLGTGDDAAVYRLPGGLALVQTTDFFPPIVDDPY
LFGRIAAANALSDIYAMGAKPLSALAIVTLPRKLPALQEEVLREILAGGKDKLREAGAVLVGGHTIEGPE
PKYGLSVTGLVHPNKILRNSGAKPGDVLILTKPLGTGILFAAEMAGLARGEDIDAALESMARLNRAAAEL
LRKYGAHACTDVTGFGLLGHLLEMARASGVSAEIDLDKLPLLQTSGGLLAAVPPEDAAALLALLKAGGPP
AAIIGEV
>gnl|CDD|100032 cd02196, PurM, PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP
GGIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDY
IATGKLDPEVAAEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDGSKIKPG
DVLIGLPSSGLHSNGYSLVRKILFEEGLDYDDPEPGLGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAH
ITGGGLPENLPRVLPEGLGAVIDLGSWEIPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVL
EILEKLGEKAYVIGEVV
>gnl|CDD|100033 cd02197, HypE, HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase biosynthesis. HypE dehydrates its own carbamoyl moiety in an ATP-dependent process to yield the enzyme thiocyanate. The N-terminal domain of HypE is related to the ATP-binding domains of the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP
SGGKLMQELIEELFLKAFDNPILEVLEDAAALLVGGGRLAFTTDSFVVSPLFFPGGDIGKLAVCGTVNDL
AMMGAKPLYLSLGFILEEGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPKGKADGIFINTTGIGVIP
RGVIISPSNIRPGDKIIVSGTIGDHGAAILAAREGLGFETDIESDCAPLNGLVEALLEAGPGIHAMRDPT
RGGLAAVLNEIARASGVGIEIEEEAIPVREEVRGACEMLGLDPLYLANEGKFVAIVPPEDAEEVLEALRS
HPLGKEAAIIGEV
>gnl|CDD|100005 cd02198, YjgH_like, YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site
FGYSPAVRVGDTLFVSGQVGSDADGSVAEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMAAHL
PAFAAVKDEYFKEPYPAWTAVGVAWLARPGLLVEIKVVAVR
>gnl|CDD|100006 cd02199, YjgF_YER057c_UK114_like_1, This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site
ELGLELPPAPAPVGNYVPAVRTGNLLYVSGQLPRVDGKLVYTGKVGADLSVEEGQEAARLCALNALAALK
AALGDLDRVKRVVRLTGFVNSAPDFTEQPKVANGASDLLVEVFGEAGRHARSAVGVASLPLNAAVEVEAI
VE
>gnl|CDD|276961 cd02201, FtsZ_type1, Filamenting temperature sensitive mutant Z, type 1. FtsZ is a GTPase that is similar to the eukaryotic tubulins and is essential for cell division in prokaryotes. FtsZ is capable of polymerizing in a GTP-driven process into structures similar to those formed by tubulin. FtsZ forms a ring-shaped septum at the site of bacterial cell division, which is required for constriction of cell membrane and cell envelope to yield two daughter cells
AKIKVIGVGGGGGNAVNRMIESGLEGVEFIAINTDAQALEKSKAPNKIQIGEKLTRGLGAGGDPEVGRKA
AEESREEIKEALKGADMVFITAGMGGGTGTGAAPVIAKIAKEMGALTVAVVTLPFSFEGKKRMRNAEEGL
EELKKYVDTLIVIPNDKLLEIVGKNLPLLEAFKKADEVLAQAVKGITDLITKPGLINLDFADVKTVMKNG
GLALMGIGEASGENRAEEAVEKALNSPLLEDDIKGAKGVLVNITGGPDLTLEEVNEAAEIITEKADPDAN
IIFGAVIDEELGDEIRVTVIATG
>gnl|CDD|276962 cd02202, CetZ_tubulin-like, Cell-structure-related euryarchaeota tubulin/FtsZ homologs. CetZ proteins comprise a distinct tubulin/FtsZ family. The crystal structures of CetZ contain the FtsZ/tubulin superfamily fold and its family members have mosaic of tubulin-like and FtsZ-like amino acid residues. However, a recent study found that CetZ proteins (formerly annotated FtsZ type 2) are not required for cell division, whereas FtsZ proteins play an important role. Instead, CetZ proteins are shown to be involved in controlling archaeal cell shape dynamics. The results from inactivation studies of CetZ proteins in Haloferax volcanii suggest that CetZ1 is essential for normal swimming motility and rod-cell development
MKLAVIGVGQAGGRIADALLRAERRSGRSIVVNALAVNTDRADLSGLDHIPEERRILIGDTETGGHGVGG
DNELGAEVAEEDIDELLRALDTAPFSEADAFLVVAGLGGGTGSGAAPVLAEELKERYDKPVYALGVLPAA
EEGGRYALNAARSLRSLVELADAVILFDNDAWRRSGESIAEAYDRINEEIAERLGALLAAGEVDAPKSVG
ESVLDASDIINTLSGGGVATIGYASEDLPTDGRSGSGLLLGESDSDVDEQEAASRIETLVRKAVLSRLTL
PCDLESADRALVVVSGPPEELSRKGIEDARSWLEEETGSVEVRAGDYPRPDSDTVSVLVLLSGVTDVPRV
EELQERA
>gnl|CDD|100034 cd02203, PurL_repeat1, PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM
ELGMFAQMWSEHCRHKSFKSLLKMIWAVVFKVETHNHPSAIEPFGGAATGVGGIIRDILSMGARPIALLD
GLRFGDLDIPGYEPKGKLSPRRILDGVVAGISDYGNCIGIPTVGGEVRFDPSYYGNPLVNVGCVGIVPKD
HIVKSKAPGPGDLVVLVGGRTGRDGIGGATFSSKELSENSSELDRPAVQVGDPFMEKKLQEAILEARETG
LIVGIQDLGAGGLSSAVSEMAAKGGLGAEIDLDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLA
ICKKEDLEAAVIGEVTDDGRLRLYYKGEVVADL
>gnl|CDD|100035 cd02204, PurL_repeat2, PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM
DAAVLRIPGETDKGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVGADPLAITDCLNFGNPEKPEGE
MGQLVEAVLGLGDACRALGTPVIGGKDSLYNETEGVAIPPTLVIGAVGVVDDVRKIVTLDFKKEGDLLYL
IGETKDELGGSEYALAYHGLGGGAPPLVDLEREKALFDAVQELIKEGLVLSAHDVSDGGLAVALAEMAFA
GGLGAEVDLSKDDAEDELLFSESLGRVLVEVKPENEEVFEAEEAGVPATVIGTV
>gnl|CDD|341358 cd02205, CBS_pair_SF, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVI
TVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR
>gnl|CDD|380338 cd02208, cupin_RmlC-like, RmlC-like cupin superfamily. This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation
ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFL
VVS
>gnl|CDD|380339 cd02209, cupin_XRE_C, XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain. This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
GYTYELLSPGLPGRKMEPFLVTLPPGGSGGEPYSHEGEEFGYVLEGELELTVGGETYVLEAGDSIYFDSD
VPHRYRNPGDEPARVLWVIT
>gnl|CDD|380340 cd02210, cupin_BLR2406-like, Bradyrhizobium japonicum BLR2406 and related proteins, cupin domain. This family includes bacterial and fungal proteins homologous to BLR2406, a Bradyrhizobium japonicum protein of unknown function with a cupin beta barrel domain. Proteins in this subfamily appear to align closest to RmlC carbohydrate epimerase which is involved in dTDP-L-rhamnose production, and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
ISAETVGAKGLWMGVVTIPPGARTGAHHHGEHETAIYVLSGRAETRYGDRLEHRAEAGPGDFIYIPPGVP
HQEVNLSDDEPAVAVVARSDPEEQEVVV
>gnl|CDD|380341 cd02211, cupin_UGlyAH_N, (S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain. This family includes the N-terminal cupin domain of (S)-ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion, via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features
VTSVLPGWENTRASVLASPKLGATFVQYLVEVEPGGGSTAPEGGEGIERFLYVLEGEVELTVGGETHTLT
AGGYAYLPPGTKHSLRNAGDEPARLLWYKKRYEPLEGGAAPEVVVGN
>gnl|CDD|380342 cd02212, cupin_UGlyAH_C, (S)-ureidoglycine aminohydrolase and related proteins, C-terminal cupin domain. This family includes the C-terminal cupin domain of (S)-Ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion,via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features
FELRKLLPDSDGFDMNVNIMTFEPGASLPFVETHVMEHGLYMLEGQGIYRLGDDWYPVQAGDFIWMAPYC
PQWFYALGREPFRYLLYKDVNR
>gnl|CDD|380343 cd02213, cupin_PMI_typeII_C, Phosphomannose isomerase type II, C-terminal cupin domain. This family includes the C-terminal cupin domain of mannose-6-phosphate isomerases (MPIs) which have been classified broadly into two groups, type I and type II, based on domain organization. This family contains type II phosphomannose isomerase (also known as PMI-GDP, phosphomannose isomerase/GDP-D-mannose pyrophosphorylase), a bifunctional enzyme with two domains that catalyze the first and third steps in the GDP-mannose pathway in which fructose 6-phosphate is converted to GDP-D-mannose. The N-terminal domain catalyzes the first and rate-limiting step, the isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, while the C-terminal cupin domain (represented in this alignment model) converts mannose 1-phosphate to GDP-D-mannose in the final step of the reaction. Although these two domains occur together in one protein in most organisms, they occur as separate proteins in certain cyanobacterial organisms. Also, although type I and type II MPIs have no overall sequence similarity, they share a conserved catalytic motif
KSQRVKEIVEELKKRGRSEEHRTVYRPWGSYEVLDEGEGYKVKRLTVNPGKRLSLQRHHHRSEHWVVVSG
TAEVTLDGKEKLLKEGESIYIPKGTKHRLENPGKIPLEIIEVQTGEYLGEDDIVRL
>gnl|CDD|380344 cd02214, cupin_MJ1618, Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain. This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion
DGSLIRELLHPDNDGDPRYSLAHARVPPGESTLPHRLKGSEEVYYILEGEGTMEIDGEPREVGPGDAVLI
PPGAVQRIENTGEEDLVFLCICSPAWSPED
>gnl|CDD|380345 cd02215, cupin_QDO_N_C, quercetinase, N- and C-terminal cupin domains. This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase
PYVLRAGEGERYLVGGQLFTVLATGESTGGAFTLVTTEGPKGDAIPPHYHKRHHETFYVLEGRLQLWLDG
ESRLLTPGDFASVPPGTIHAYRMLSPDTRFLGVITPGGFERFFRALGEPYEG
>gnl|CDD|380346 cd02216, cupin_GDO-like_N, gentisate 1,2-dioxygenase, 1-hydroxy-2-naphthoate dioxygenase, and salicylate 1,2-dioxygenase, N-terminal cupin domain. This family includes the N-terminal cupin domains of three closely related bicupin aromatic ring-cleaving dioxygenases: gentisate 1,2-dioxygenase (GDO), salicylate 1,2-dioxygenase (SDO), and 1-hydroxy-2-naphthoate dioxygenase (NDO). GDO catalyzes the cleavage of the gentisate (2,5-dihydroxybenzoate) aromatic ring, a key step in the gentisate degradation pathway allowing soil bacteria to utilize 2,5-xylenol, 3,5-xylenol, and m-cresol as sole carbon and energy sources. NDO catalyzes the cleavage of 1-hydroxy-2-naphthoate as part of the bacterial phenanthrene degradation pathway. SDO is a ring cleavage dioxygenase from Pseudaminobacter salicylatoxidans that oxidizes salicylate to 2-oxohepta-3,5-dienedioic acid via a novel ring fission mechanism. SDO differs from other known GDOs and NDOs in its unique ability to oxidatively cleave many different salicylate, gentisate and 1-hydroxy-2-naphthoate substrates with high catalytic efficiency. The active site of these enzymes is located in the N-terminal domain but could be influenced by changes in the C-terminal domain, which lacks the strictly conserved metal-binding residues found in other cupin domains and is thought to be an inactive vestigial remnant
RRVLLLVNPGLPGTRATTHTLYAGLQLLPPGEVAPAHRHTPNALRFVLEGPGAYTTVDGERCDMEPGDLI
LTPPGTWHDHGNEGDEPAIWLDGLDAPLVTYLRASFFE
>gnl|CDD|380347 cd02218, cupin_PGI, cupin-type phosphoglucose isomerase. The cupin-type phosphoglucose isomerase (also called cupin-like glucose-6-phosphate isomerase or cPGI; EC 5.3.1.9) family is found in archaea and certain prokaryotes where they catalyze the reversible aldose-ketose isomerization of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P) as part of a unique variation of the Embden-Meyerhof glycolytic pathway. Cupin-PGIs represent a separate lineage in the evolution of phosphoglucose isomerases. Pyrococcus furiosus phosphoglucose isomerase (PfPGI) has been shown to be a metal-containing enzyme which catalyzes the interconversion of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P). These domains have a cupin beta-barrel fold capable of homodimerization
KSVRRLSDLKGVFADEEALEPELAEPLVYEVYRGVPPEEDKEGGLRYDITVIYPGKVGDEYFKTKGHYHA
KRDYPEVYEVLSGEGLLLLQKEDVGEVILVEAKPGDKVYIPPGYAHRTINTGDEPLVFANWWPSDAGHDY
EPIEEKGGFAYYVVEDGGVGNPNYKDVP
>gnl|CDD|380348 cd02219, cupin_YjlB-like, Bacillus subtilis YjlB and related proteins, cupin domain. This family includes bacterial and fungal proteins homologous to YjlB, a Bacillus subtilis protein of unknown function with a cupin beta barrel fold. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two-domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation
LPPDGGIPNSPRLPVLIYRGALPDDPDDAAAVEALFEANGWTPQWRNGIYDYHHYHSTTHEVLGVASGSA
TLQLGGPGGVEVTVEAGDVVVLPAGVGHKLLESSDDFQVVGAYPEGQEWDDCRGGPEEREAALERIAAVP
LPETDPVYGEDGPL
>gnl|CDD|380349 cd02220, cupin_ABP1, auxin-binding protein 1, cupin domain. Auxin-binding protein 1 (ABP1) is a soluble glycoprotein receptor that binds the plant hormone auxin, indole-3-acetic acid (IAA). ABP1 belongs to the ancient and functionally diverse germin/seed storage 7S protein superfamily. It is an important mediator of auxin action in plants and is essential for cell cycle control. Cellular auxin responses typically depend on auxin concentrations that mainly result from intercellular auxin transport and auxin biosynthesis, as well as metabolism. The functional inactivation of ABP1 results in cell cycle arrest, showing that ABP1 plays a critical role in cell cycle regulation, acting at both the G1/S and G2/M checkpoints. ABP1 is ubiquitous among green plants, found mainly within the endoplasmic reticulum (ER) and in smaller quantities at the cell surface associated with the plasma membrane. In Arabidopsis thaliana, ABP1 null mutations result in embryonic lethality while decreased ABP1 expression leads to severe retardation of leaf growth
PLVRNISELPQDSYGRPGLSHMTVAGAVHHGMKEVEVWLQTFAPGSGTPIHRHSCEEVFVVLKGSGTLYL
ASSSLKYPGKPQEFPIFPNSTFHIPVNDVHQVWNTGEHEDLQVLVIISRPPVKVFIYDDWSMPHTAAKLK
FPYVWDEQCYQ
>gnl|CDD|380350 cd02221, cupin_TM1287-like, Thermotoga maritima TM1287 decarboxylase, cupin domain. This family includes bacterial proteins homologous to TM1287 decarboxylase, a Thermotoga maritima manganese-containing cupin thought to catalyze the conversion of oxalate to formate and carbon dioxide, due to its similarity to oxalate decarboxylase (OXDC) from Bacillus subtilis. TM1287 shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer
GTVTVYHLLTPEELKGKGRLFARVTLPPGSSIGYHQHEGEFEIYYILSGEGLYTDNGKEYEVKAGDVTFT
RDGESHGIENTGDEDLVFIALIL
>gnl|CDD|380351 cd02222, cupin_TM1459-like, Thermotoga maritima TM1459 and related proteins, cupin domain. This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer
GVTIRVLIGPEDGAPNFAMRYFEIEPGGHTPLHTHPWEHEVYVLRGKGVVVIGGEEYPVKPGDVVYIPPN
EPHQFRNTGDEPLGFLCIVPK
>gnl|CDD|380352 cd02223, cupin_Bh2720-like, Bacillus halodurans Bh2720 and related proteins, cupin domain. This family includes bacterial, archaeal, and eukaryotic proteins similar to Bh2720, a Bacillus halodurans protein of unknown function with a cupin beta-barrel fold
FRRVLWTGKNLQLVLMSIPPGEDIGLEVHDDVDQFLRIEEGEGKAIMGGFESEVKDGDAIIVPAGTWHNV
INTGNEPLKLYTIYAPPEHPDGTVHKTK
>gnl|CDD|380353 cd02224, cupin_SPO2919-like, Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase with a cupin domain. This family includes proteins similar to sugar phosphate isomerase SPO2919 from Silicibacter pomeroyi and Afe_0303 from Acidithiobacillus ferrooxidans, but are as yet uncharacterized. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer
AGRHLRSLGDAAGLTQLGVNLERLPPGARSSPRHWHSAEEEFVYVLSGEGTLRLDGEEVLPRPGDFVGFP
AGTGVAHQLINRSDEPLVYLVVGTRLPDDVCTYPD
>gnl|CDD|380354 cd02225, cupin_PA3510-like, Pseudomonas aeruginosa PA3510 and related proteins, cupin domain. This family includes bacterial proteins homologous to PA3510, a Pseudomonas aeruginosa protein of unknown function with a beta-barrel fold that belongs to the cupin superfamily
MDRYVARFEDRWPDWKAFADALDPGYRRAQFRYIGSGGTGKHDDPNIIPAEHFTLSTMRLPPGQGGALHT
HEVEEVFFVLQGRLTVFWEDEGEEHERELGPRDMISVPAGVYRGFKNIGEEDALMQVMLGTGKPGRPTYP
DDSELAKARR
>gnl|CDD|380355 cd02226, cupin_YdbB-like, Bacillus subtilis YdbB and related proteins, cupin domain. This family includes bacterial proteins homologous to YdbB, a Bacillus subtilis protein of unknown function. It also includes protein Nmb1881 From Neisseria meningitidis, also of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
NLAEKLAAIDEYWSPKIVAEVNDQVVKLAKLKGEFVWHKHDDEDELFLVLEGELTIDFRDRDVTLGPGEF
FVVPKGVEHRPVAEEETVVLLIEP
>gnl|CDD|380356 cd02227, cupin_TM1112-like, Thermotoga maritima TM1112 and related proteins, cupin domain. This family includes bacterial and plant proteins homologous to TM1112, a Thermotoga maritima protein of unknown function with a cupin beta barrel domain. TM1112 (also known as DUF861) is a subfamily of RmlC-like cupins with a conserved "jelly roll-like" beta-barrel fold; structures indicate that a monomer is the biologically-relevant form
SWGIWECTPGKFPWNYDEDEFCYILEGEVRVTPEDGEPVTFKAGDLVVFPAGFSGTWEVLEPVRKHYVF
>gnl|CDD|380357 cd02228, cupin_EutQ, Clostridium difficile EutQ and related proteins, cupin domain. This family includes bacterial and fungal proteins homologous to ethanolamine utilization protein EutQ found in Clostridium difficile, as well as in other bacteria, including the enteric pathogens Salmonella enterica and Enterococcus faecalis. EutQ is encoded by the eutQ gene which is part of the eut (ethanolamine utilization) operon found to be essential during anoxic growth of S. enterica on ethanolamine and tetrathionate. In C. difficile, inability to utilize ethanolamine results in greater virulence and a shorter time to morbidity in the animal model, suggesting that, in contrast to other intestinal pathogens, the metabolism of ethanolamine can delay the onset of disease. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. In contrast to the metal-binding catalytic cupins, the EutQ family does not possess the histidine residues that are responsible for metal coordination in the oxidoreductase and epimerase classes of cupins
VFLKDVVTSEEGSPMSAGFMELEKKSFPWTLTYDEIKYVLEGELEITDDGQTVTAKPGDVLFIPKGSKIT
FSTPDYAKFFYVTY
>gnl|CDD|380358 cd02230, cupin_HP0902-like, Helicobacter pylori HP0902 and related proteins, cupin domain. This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity
VSRTLVQDDGLRVTLFAFDAGQELSEHTAPGDATVQVLEGEAEFTIGGETVTLKAGELIVMPANVPHALK
AEEDFKMLLTLIK
>gnl|CDD|380359 cd02231, cupin_BLL6423-like, Bradyrhizobium japonicum BLL6423 and related proteins, cupin domain. This family includes bacterial and fungal proteins homologous to BLL6423, a Bradyrhizobium japonicum protein of unknown function; it includes a structure of an uncharacterized protein from Novosphingobium aromaticivorans. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
AAFTLLWSTDSFPADNDDDDDPAAAPPPGLPPPGGTVFRVVDFPPGAESPMHRTESLDYGIVLEGEIELE
LDDGEEVTLKAGDVVVQRGTMHAWRNRSDEPARMAFVL
>gnl|CDD|380360 cd02232, cupin_ARD, acireductone dioxygenase (ARD), cupin domain. Acireductone dioxygenase (ARD; also known as 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase) catalyzes the oxidation of 1,2-dihydroxy-3-keto-5-methylthiopentene to yield two different products depending on which active site metal is present (Fe2+ or Ni2+) as part of the methionine salvage pathway. The ARD apo-enzyme, obtained after the metal is removed, is catalytically inactive. The Fe(II)-ARD reaction yields an alpha-keto acid and formic acid, while Ni(II)-ARD instead catalyzes a shunt out of the methionine salvage pathway, yielding methylthiocarboxylic acid, formic acid, and CO. ARD belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
AEELAELGVLYERWDADDLEAAGAAYDEELDALKKERGYKSRDVVTLSPETPNYEEKLKKFFEEHLHEDD
EVRFILDGSGYFDVRDKDDEWIRILVEKGDLIVVPAGIYHRFTLDENPYIKAVRLFKDEPGWVP
>gnl|CDD|380361 cd02233, cupin_HNL-like, Granulicella tundricola hydroxynitrile lyase (GtHNL) and related proteins, cupin domain. This family includes archaeal, eukaryotic, and bacterial proteins homologous to hydroxynitrile lyase from Granulicella tundricola (GtHNL), a novel class of HNLs that does not show any sequence or structural similarity to any other HNL and does not contain conserved motifs typical of HNLs. HNLs comprise a diverse group of enzymes that vary in terms of their substrate specificity, enantioselectivity and the need for a co-factor. In plants, they catalyze the reversible cleavage of cyanohydrins, yielding HCN and aldehydes or ketones. Also included in this family is TM1010 from Thermotoga maritima, a protein of unknown function. Some but not all members of this family have N- or C-terminal carboxymuconolactone decarboxylase domains in addition to the cupin domain. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
FTGTVWLDPLFPADEPSRVSVANVTFEPGARTAWHTHPGGQILIVTSGVGWVQEEGGPPQELRPGDVVWI
PPGVKHWHGAAPDSAMTHLAITEALDGGGVEWLEPV
>gnl|CDD|380362 cd02234, cupin_BLR7677-like, Bradyrhizobium japonicum BLR7677 and related proteins, cupin domain. This family includes bacterial and fungal proteins homologous to BLR7677, a Bradyrhizobium japonicum protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
ETVTVLYSQPLPNIPGKEVTVLLVTYPPGAASPPHRHPGFVFAYVLEGEVRSQVNGGPPRVYKAGESFYE
PPGAHHRVSRNASATEPAKLLAVFVVDTGAPEL
>gnl|CDD|380363 cd02235, cupin_BLL4011-like, Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain. This family includes bacterial and fungal proteins homologous to BLL4011, a Bradyrhizobium diazoefficiens protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
GIKRTVLQRTDLSVPGREVVQVRVEIPPGAVAGRHTHPGEESGYVLEGSLELEVDGQPPVTLKAGDSFFI
PAGTVHNAKNVGSGPAKLLATYIVEKGKPL
>gnl|CDD|380364 cd02236, cupin_CV2614-like, Chromobacterium violaceum CV2614 and related proteins, cupin domain. This family includes mostly bacterial proteins homologous to CV2614, a Chromobacterium violaceum protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
LLKTTTTWDGQPIPYPEGQPEITVLRITIPPGAELPWHTHPVPNAGYVLSGELTVEYEDGKKRTFKAGDA
FVEAVNTWHRGRNGGDEPVELLVFYAGAKGVP
>gnl|CDD|380365 cd02237, cupin_DAD_ChrR, 2,4'-Dihydroxyacetophenone dioxygenase (DAD) and anti-sigma factor ChrR, and similar proteins; cupin domain. This family includes the proteins 2,4'-Dihydroxyacetophenone dioxygenase (DAD) and anti-sigma factor ChrR. DAD catalyzes the oxidation of 2,4'-dihydroxyacetophenone to 4-hydroxybenzoate and formate as part of the 4-hydroxyacetophenone catabolic pathway. The enzyme is a homotetramer containing one iron per molecule of enzyme. Anti-sigma factor ChrR is a member of the ZAS (Zn2+ anti-sigma) subfamily of group IV anti-sigmas. It inhibits transcriptional activity by binding to the Rsp extra cytoplasmic function (ECF) sigma factor E (sigmaE). Some ChrR members contain tandem repeats of two distinct homologous functional domains. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
VEQRPLLIDPNTGLITAILRMAPGARLPDHEHVGGEEFYVLDGALTDEDGTAGAGDFVREPPGSRHSAVA
PREGCLILVILQ
>gnl|CDD|380366 cd02238, cupin_KdgF, pectin degradation protein KdgF and related proteins, cupin domain. This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
FVKWDELPWEELGPGVRRKILAGGEKLMLVEVRFEKGAVVPLHSHPHEQIGYVLSGRFEFTIGGETRILK
PGDSYYIPPNVPHGAEALEDSVLLDVFSPPREDF
>gnl|CDD|380367 cd02240, cupin_OxDC, Oxalate decarboxylase (OxDC), cupin domain. Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds and both domains are included in this alignment. Each OxDC cupin domain contains one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
DSEPIEENAGGSVRIATVTNFPISKDLSSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDGRF
ETFNLGAGDVGYVPSGSGHHIENIGDEDAEFLLIFDDGTFADVSLPWWLAMTPEEVLAATLDLGKFIDAL
PKAKH
>gnl|CDD|380368 cd02241, cupin_OxOx, Oxalate oxidase (germin), cupin domain. Oxalate oxidase (OxOx, also known as germin; EC 1.2.3.4) catalyzes the manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide (H2O2). It is widespread in fungi and various plant tissues and may play a role in plant signaling and defense. This enzyme has been employed in a widely used assay for detecting urinary oxalate levels. Also, the gene encoding OxOx from barley roots has been expressed in oilseed rape in order to provide a defense against externally supplied oxalic acid. In germin, the predominant protein produced during the early phase of wheat germination, it is believed that H2O2 production is employed as a defense mechanism in response to infection by pathogens. Germin is also a marker of growth onset in cell walls in germinating cereals. The H2O2 produced by OxOx, together with the Ca2+ released by degradation of calcium oxalate, are thought to mediate cell wall cross-linking at high concentrations. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
DPDPLQDFCVADLSSPRTPNGYPCKDPALVTADDFVFDFLNPPGNTSNPLGGSVTLANVANFPALNGLGI
SMARGDLAPCGVNPPHTHPRATELLYVVEGTLYVGFVDENGNRLFTKTLNPGDVFVFPQGLIHFQFNPGC
EPAVFVAAFNSEDPGTQQIAQALFGLPPPDDVLAAAFGLDGAQVEKLKSKF
>gnl|CDD|380369 cd02242, cupin_11S_legumin_N, 11S legumin seed storage globulin, N-terminal cupin domain. This family contains the N-terminal domains of 11S legumin seed storage proteins that supply nutrition for seed germination, such as glycinin and legumin, including many common food allergens such as the peanut major allergen Ara h 3, almond allergen Pru du 6, Pecan allergen Car i 4, hazelnut nut allergen Cor a 9, Brazil nut allergen Ber e 2, cashew allergen Ana o 2, pistachio allergen Pis v 2/5, and walnut allergen Jug n/r 4. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). They are synthesized as propeptides in the endoplasmic reticulum and transported to the secretory vesicles as a homotrimer. The propeptides are processed as they are sorted in the secretory vesicles. The homotrimer binds another homotrimer to form a homohexamer with 32-point symmetry formed by a face-to-face stacking of the two trimers. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
LDRLPALEPTRRIESEGGSYEYWDPNNPQLQCAGVAAGRLTIEPRGLLLPSYSNAPKLAYVLQGRGIVGV
VFPGCPETFQSSQQSQGQGQRFRDQHQKVRRIRKGDVIAVPAGVVHWWYNDGDSDLVIVFLGDTSNNANQ
LDGNFRRFFLAGNPQQEQQGQGQEQSGGGNIFSGFSTEFLAEAFGVDEETARKLQGSQDQRGLIVKVEE
>gnl|CDD|380370 cd02243, cupin_11S_legumin_C, 11S legumin seed storage globulin, C-terminal cupin domain. This family contains the C-terminal domains of 11S legumin seed storage proteins that supply nutrition for seed germination, such as glycinin and legumin, including many common food allergens such as the peanut major allergen Ara h 3, almond allergen Pru du 6, Pecan allergen Car i 4, hazelnut nut allergen Cor a 9, Brazil nut allergen Ber e 2, cashew allergen Ana o 2, pistachio allergen Pis v 2/5, and walnut allergen Jug n/r 4. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). They are synthesized as propeptides in the endoplasmic reticulum and transported to the secretory vesicles as a homotrimer. The propeptides are processed as they are sorted in the secretory vesicles. The homotrimer binds another homotrimer to form a homohexamer with 32-point symmetry formed by a face-to-face stacking of the two trimers. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
DVYVPRGGRITTLNSFKLPILRFVGLSAERVKLEPNAMFAPHWNANAHQVIYVTRGSGRVQVVGDNGKRV
LDGEVREGQLLVVPQFFAVAKIAGEEGFEWVSFKTSDNPIFSELAGRTSVLRALPPEVLANSYNISPEEA
KQLKSNREKETVLFP
>gnl|CDD|380371 cd02244, cupin_7S_vicilin-like_N, 7S vicilin seed storage globulin, N-terminal cupin domain. This family contains the N-terminal domains of plant 7S seed storage proteins such as vicilin, and includes beta-conglycinin, phaseolin, canavalin, conglutin-beta, a chromatin protein in Pisum sativum called P54, and a sucrose binding protein in soybean called SBP. These 7S globulins also include soybean allergen beta-conglycinin, peanut allergen conarachin (Ara h 1), walnut allergen Jug r 2, and lentil allergen Len c 1. Proteins in this family perform various functions, including a role in sucrose binding, desiccation, defense against microbes and oxidative stress. The vicilin peptides formed by trypsin or chymotrypsin digestion exhibit antihypertensive effects. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). Storage proteins are the cause of well-known allergic reactions to peanuts and cereals. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
VVRTEAGEIRVLERFDGRSRLLRGIENYRLAFITMEPNTLFLPHHLDADMVFYVHTGRGTITWVDEDKRE
SYNLERGDVYRIPAGSTFYLVNTDENEKLRIIALFDPVNSLTPGPFQSFFGAGGQNPESLLSGFSKEILE
AAFNVSEEELERLLSQQKPGPIVKASEEQIRALSRHAS
>gnl|CDD|380372 cd02245, cupin_7S_vicilin-like_C, 7S vicilin seed storage globulin, C-terminal cupin domain. This family contains C-terminal domain of plant 7S seed storage protein such as vicilin and includes beta-conglycinin, phaseolin, canavalin, conglutin-beta, a chromatin protein in Pisum sativum called P54, and a sucrose binding protein in soybean called SBP. These 7S globulins also include soybean allergen beta-conglycinin, peanut allergen conarachin (Ara h 1), walnut allergen Jug r 2 and lentil allergen Len c 1. Proteins in this family perform various functions, including a role in sucrose binding, desiccation, defense against microbes and oxidative stress. The vicilin peptides formed by trypsin or chymotrypsin digestion exhibit antihypertensive effects. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). Storage proteins are the cause of well-known allergic reactions to peanuts and cereals. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
PDFSNQYGWLYEADPEDYKQLKDLDVGVSFVNITQGSMMAPHYNSRATEIAVVVEGEGYVEMVCPHLSSQ
SQQGEEEGSGEYQKVRARLSEGDVFVVPAGHPVAQVASSNENLEFVGFGINAQNNERQFLAGKNNVLRQL
DREAKELAFNVPAEEVEEVLNAQDES
>gnl|CDD|380373 cd02247, cupin_pirin_C, pirin, C-terminal cupin domain. This family contains the C-terminal domain of pirin, a nuclear protein that is highly conserved among mammals, plants, fungi, and prokaryotes. It is widely expressed in dot-like subnuclear structures in human tissues such as liver and heart. Pirin functions as both a transcriptional cofactor and an apoptosis-related protein in mammals and is involved in seed germination and seedling development in plants. The pirins have been assigned as a subfamily of the cupin superfamily based on structure and sequence similarity. The pirins have two tandem cupin-like folds but the C-terminal cupin fold has diverged considerably and does not have a metal binding site. The exact functions of pirins are unknown but they have quercitinase activity in Escherichia coli and are thought to play important roles in transcription and apoptosis. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
PVLYLDITLEPGAKFTQPVPAGWNAFIYVLEGEATIGGEEVEAEAGHLAVLGPGGDGVELEAKEEGARFL
LIAGEP
>gnl|CDD|239068 cd02248, Peptidase_C1A, Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) similar to papain, including the mammalian CPs (cathepsins B, C, F, H, L, K, O, S, V, X and W). Papain is an endopeptidase with specific substrate preferences, primarily for bulky hydrophobic or aromatic residues at the S2 subsite, a hydrophobic pocket in papain that accommodates the P2 sidechain of the substrate (the second residue away from the scissile bond). Most members of the papain subfamily are endopeptidases. Some exceptions to this rule can be explained by specific details of the catalytic domains like the occluding loop in cathepsin B which confers an additional carboxydipeptidyl activity and the mini-chain of cathepsin H resulting in an N-terminal exopeptidase activity. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds. Parasitic CPs act extracellularly to help invade tissues and cells, to hatch or to evade the host immune system. Mammalian CPs are primarily lysosomal enzymes with the exception of cathepsin W, which is retained in the endoplasmic reticulum. They are responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. In addition to its inhibitory role, the propeptide is required for proper folding of the newly synthesized enzyme and its stabilization in denaturing pH conditions. Residues within the propeptide region also play a role in the transport of the proenzyme to lysosomes or acidified vesicles. Also included in this subfamily are proteins classified as non-peptidase homologs, which lack peptidase activity or have missing active site residues
PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSGNNGCNGGNPDN
AFEYVKNGGLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALANYGPVSVAIDASSSF
QFYKGGIYSGPCCSNTNLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYASYP
>gnl|CDD|239069 cd02249, ZZ, Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins
YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGKKGHPPDHSFTEI
>gnl|CDD|239070 cd02252, nylC_like, nylC-like family; composed of proteins with similarity to Flavobacterium endo-type 6-aminohexanoate-oligomer hydrolase (EIII), the product of the nylon oligomer degradation gene, nylC. EIII is an amide hydrolase that catalyzes the degradation of highly-polymerized 6-aminohexanoate oligomers. Together with other nylon degradation enzymes, such as 6-aminohexanoate cyclic dimer hydrolase (EI) and 6-aminohexanoate dimer hydrolase (EII), EIII plays a role in the detoxification and biological removal of the synthetic by-products of nylon manufacture. EIII shows sequence similarity to L-aminopeptidase D-amidase/D-esterase (DmpA), an aminopeptidase that releases N-terminal D and L amino acids from peptide substrates. Like DmpA, EIII undergoes autocatalytic cleavage in front of a nucleophile to form a heterodimer. DmpA shows similarity in catalytic mechanism to N-terminal nucleophile (Ntn) hydrolases, which are enzymes that catalyze the cleavage of amide bonds through the nucleophilic attack of the side chain of an N-terminal serine, threonine, or cysteine
ITDVPGIRVGHATDEEGLTGVTVILCPEGAVAGVDVRGGAPGTRETDLLDPENLVQKVHAIVLSGGSAFG
LAAADGVMRALEERGVGFPVGVPVVPIVPAAVLFDLGGGDKRWRPDAALGYAAAEAAGPGPFPLGRVGAG
TGATAGKVLDRALKGGLGSASIRLGDGVTVGALVVVNAVGNTTIGVVATDAALTKAEAKRLASMAHDGLA
RAIRPVHTPFDGDTVFALATGEVELPRSVDLTALGALAADVVARAILRAV
>gnl|CDD|239071 cd02253, DmpA, L-Aminopeptidase D-amidase/D-esterase (DmpA) family; DmpA catalyzes the release of N-terminal D and L amino acids from peptide susbtrates. DmpA is synthesized as a single polypeptide precursor, which is autocatalytically cleaved to the active heterodimeric form. The cleavage results in two polypeptide chains, with one chain containing an N-terminal nucleophile. This group represents one of the rare aminopeptidases that are not metalloenzymes. DmpA shows similarity in catalytic mechanism to N-terminal nucleophile (Ntn) hydrolases, which are enzymes that catalyze the cleavage of amide bonds through the nucleophilic attack of the side chain of an N-terminal serine, threonine, or cysteine
IPGRGKPGPLNAITDVAGVEVGHVTLISGEGPKGPVRTGVTAILPHGGNLFQEPVPAGVHVLNGFGKMTG
LTQVEELGLLETPILLTNTLSVGTVRDALIRWMLDQNPEIGRTTGWVNPVVAETNDGYLNDIRGFHVTPE
HVFAALDNASSGPVEEGNVGAGTGMICFGFKGGIGTASRRVPIGGGGYTVGVLVQANFGRREDLRIAGVP
VGRELKDADPPGEAKPPDDGSIIIVIATDAPLLPRQLKRLAKRAPLGLARTGSFGGNGSGDIFLAFSTAN
TVPHEASKAVQTVEMLPDDHLDPLFEAAVEATEEAILNALVAAETMTGRNGHTVPALPH
>gnl|CDD|187736 cd02255, Peptidase_C12, Cysteine peptidase C12 contains ubiquitin carboxyl-terminal hydrolase (UCH) families L1, L3, L5 and BAP1. The ubiquitin C-terminal hydrolase (UCH; ubiquitinyl hydrolase; ubiquitin thiolesterase) family of deubiquitinating enzymes (DUBs) consists of four members to date: UCH-L1, UCH-L3, UCH-L5 (UCH37) and BRCA1-associated protein-1 (BAP1), all containing a conserved catalytic domain with cysteine peptidase activity. UCH-L1 hydrolyzes carboxyl terminal esters and amides of ubiquitin (Ub). Dysfunction of this hydrolase activity can lead to an accumulation of alpha-synuclein, which is linked to Parkinson's disease (PD) and neurofibrillary tangles, linked to Alzheimer's disease (AD). UCH-L1, in its dimeric form, has additional enzymatic activity as a ubiquitin ligase. UCH-L3 hydrolyzes isopeptide bonds at the C-terminal glycine of either Ub or Nedd8, a ubiquitin-like protein. UCH-L3 can also interact with Lys48-linked Ub dimers to protect it from degradation while inhibiting its hydrolase activity at the same time. UCH-L1 and UCH-L3 are the most closely related of the UCH members. UCH-L5 (UCH37) is involved in the deubiquitinating activity in the 19S proteasome regulatory complex. It is also associated with the human Ino80 chromatin-remodeling complex (hINO80) in the nucleus. BAP1 binds to the wild-type BRCA1 RING finger domain, localized in the nucleus. It consists of the N-terminal UCH domain and two predicted nuclear localization signals (NLSs), only one of which is functional. The full-length human BRCA1 is a ubiquitin ligase. However, BAP1 does not appear to function in the deubiquitination of autoubiquitinated BRCA1. There is growing evidence that UCH enzymes and human malignancies are closely correlated. Studies show that UCH enzymes play a crucial role in some signaling pathways and in cell-cycle regulation
WLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLSMVPRPVCAVLLLFPITEKYEVFRTEEEEKIKS
QGQDVTSSVYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLKKFLEESVSMSPEERARYLENYDAIR
VTHETSAHEGQTEAPSIDEKVDLHFIALVHVDGHLYELDGRKPFPINHGETSDETLLEDAIEVCKKFMER
DPDELRFNAIAL
>gnl|CDD|239072 cd02257, Peptidase_C19, Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GLNNLGNTCYLNSVLQALFSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIV
CLECGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLP
PVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGSYKYELVAVVVHSGTSADSGH
YVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSSSAYILFYE
>gnl|CDD|199210 cd02258, Peptidase_C25_N, Peptidase C25 family N-terminal domain, found in Arg-gingipain (Rgp), Lys-gingipain (Kgp) and related proteins. Peptidase family C25 is a unique class of cysteine proteases, exemplified by gingipain, which is produced by Porphyromonas gingivalis. P. gingivalis is one of the primary gram-negative pathogens that causes periodontitis, a disease that is also associated with other diseases such as diabetes and cardiovascular disease. Gingipains are a group of extracellular Arg- and Lys-specific proteinases called Arg-gingipain (Rgp) and Lys-gingipain (Kgp); RgpA and RgpB are homologous Arg-specific gingipains encoded by two closely related genes, rgpA and rgpB, while Lys-specific gingipain is encoded by the single kgp gene. Mutant studies have shown that, among the large quantities of proteolytic enzymes produced by P. gingivalis, these three proteases are major virulence factors of this bacterium. All three genes encode an N-terminal pre-pro fragment, followed by the protease domain; however, rgpA and kgp also encode additional C-terminal HA (hemaglutinin/adhesion) subunits which consist of several sequence-related adhesion domains. Although unique, their cysteine protease active site residues (His and Cys) forming the catalytic dyad are well-conserved, cleaving the C-terminal peptide bond with Arg or Lys residues. Gingipains are evolutionarily related to other highly specific proteases including caspases, clostripain, legumains, and separase. Gingipains function by dysregulating host defense and inflammatory responses, and degrading host proteins, e.g. tissue, cells, matrix, plasma and immunological proteins. They are proposed to enhance gingival crevicular fluid (GCF) production through activation of the kallikrein/kinin pathways, thus increasing vascular permeability and causing gingival inflammation, a distinctive feature of periodontitis. RgpA and RgpB are also able to cleave and activate coagulation factors IX and X in order to activate prothrombin to produce thrombin, which in turn increases production of GCF. The gingipains also play a pivotal role in the survival of P. gingivalis in the host by attacking the host defense system through cleavage of several immunological molecules, while at the same time evading the host-immune response by dysregulating the cytokine network
VLNQNLHASTDPDYLIITPPSLRSQAERLADYRRSNDGLGVLVVTTEQIYNEFSSGEPDPTAIRRFMKYL
YDNAPQKLKYLLLFGDGSYDYKNRIANNANLVPTYESLESFSLVGSYASDDYFGFLDGDEGDNLGDDKPD
IGVGRIPAKTNAEAKNYVDKIIAYENNKSDGLWRKKILFIADDGDNNEHQTDADNLADTVESNKPEYNVN
KIYLDAYQKETTAGGQRYPQVRENITEAINQGALLINYFGHGGETGWAQERGLTLDDINGLNNKGKLPLV
ITATCDFGRFDSPNRPSLGEDWLLNPNGGAIALLTTTRPVYSSYNKELNRALYENLFSKEDGRNPTLGEI
LRLTKNKLLSGGGDDQANIRQFTLLGDPALRL
>gnl|CDD|239073 cd02259, Peptidase_C39_like, Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in all sub-families
GGGPLDCGLACLQMLLRYFGIPVRRDVLLNAQQRRQQGLSLADLVSLANKLGLTAQGVKLPLAALSRLQL
PALLLWKQGHFVILYGADKGQVLIADPLEEGPVTLSESELEERWTGHWVLLL
>gnl|CDD|187535 cd02266, SDR, Short-chain dehydrogenases/reductases (SDR). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
VLVTGGSGGIGGAIARWLASRGSPKVLVVSRRDVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLL
EAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQQWASEGWGNGLPATAVACGTWAGSG
MAKGPVAPEEILGNRRHGVRTMPPEEVARALLNALDRPKAGVCYII
>gnl|CDD|467610 cd02270, meso-DAPDH_N, N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins. Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain
IRVAIVGYGNLGRGVEEAIQANPDMELVGVFRRRDPKSTKELTPVVVVSVVEHISELDKVDVAILCGGSA
TDLPEQAPEFAQGFNTVDSFDTHARIPEHFAALDKAAKENGTVAVISAGWNPAFTASVLVAYARAAYRLA
KGGQYGAFTVP
>gnl|CDD|467611 cd02274, DHDPR_N, N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins. DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich
IKVAVAGATGRMGRELVKAILEAPDLELVGAVDRPGSGLLGGDAGGLAGIGTGVIVSLDLELAAADADVV
IDFTTPEATLENLEAAAKAGVPLVIGTTGFSEEQLAEIEEAAKKIPVVIAPNSREIFAPGALLAARWLA
>gnl|CDD|467612 cd02278, GAPDH_II_N, N-terminal NAD(P)-binding domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins. GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (EC 1.2.1.59). The family corresponds to type II NADP+ utilizing GAPDHs mainly from archaea
IKVGVNGYGTIGKRVADAVLLQDDMELVGVAKRSPDYEAKPAVERGIPLYVPDESRAEKFEEAGIPVAGT
LEDLLEKADVVVDCTPKGIGAKNKELYYKAGVKAIFQGGEKHFVAGVSFNAGANYEEALGKQFVRVVSQE
SIVIPENIDAIRAMLGLKDPEESIEKTNKAL
>gnl|CDD|467515 cd02280, AGPR_N, N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar proteins. AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC), while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase (EC 2.7.2.8) domain and a C-terminal AGPR domain. There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. This family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase, EC 1.2.1.103/EC 1.2.1.106), which is involved in both the arginine and lysine biosynthetic pathways. Members in this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain
PRVAIIGASGYTGLEIVRLLLGHPYLRVLTLSSRERAGPKLREYHPSLIISLQIQEFRPCEVLNSADILV
LALPHGASAELVAAISNPQVKIIDLSADFRFTDPEVYRRHPRPDLEGGWVYGLPELDREQRIANATRIAN
PNLVKGAAGAAVQNLNLALG
>gnl|CDD|467516 cd02281, ASADH_AGPR_N, N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and N-acetyl-gamma-glutamyl-phosphate reductase (AGPR). Aspartate-beta-semialdehyde dehydrogenase (ASADH, EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the second step of the aspartate biosynthetic pathway, an essential enzyme found in bacteria, fungi, and higher plants. ASADH catalyses the formation of L-aspartate-beta-semialdehyde (ASA) by the reductive dephosphorylation of L-beta-aspartyl phosphate (BAP), utilizing the reducing power of NADPH. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. N-acetyl-gamma-glutamyl-phosphate reductase (AGPR, EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, reversibly catalyses the NADPH-dependent reduction of N-acetyl-gamma-glutamyl phosphate; the third step of arginine biosynthesis. ASADH and AGPR proteins contain an N-terminal Rossmann fold NAD(P)H binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain
KKVGVVGATGYVGGEFLRLLLEHPFPLFEIVLLAASSAGAKKKYFHPKLWGRVLVEFTPEEVLEQVDIVF
TALPGGVSAKLAPELSEAGVLVIDNASDFRLDKDVPLVVPEVNREHIGELKGTKIIANPNLVKGAAGAAV
QIAEI
>gnl|CDD|467517 cd02314, VcASADH1_like_N, N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase 1 (ASADH1) and similar proteins. The family corresponds to a branch of bacterial ASADH enzymes mainly found from proteobacteria, such as Escherichia coli, Haemophilus influenzae, Pseudomonas aeruginosa and Vibrio cholerae. The first isoform of ASADH in Vibrio cholerae is one of the prototypes of this family. They have similar overall folds and domain organizations but sharing less sequence homology with fungal and archaeal ASADHs. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain
KRVGFVGWRGMVGSVLMQRMQEENDFDLIEPVFFSTSQVGQKGPTFGKDVGPLKDAYDIDALKKMDIIVT
CQGGDYTKEVYPKLRKAGWKGYWIDAASTLRMKDDAVIVLDPVNRDVIDSGLASGIKTFVGGNQLLWGAA
EPLRRMLRIL
>gnl|CDD|467518 cd02315, ScASADH_like_N, N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins. The family corresponds to a new branch of ASADH enzymes that has a similar overall fold and domain organization but sharing very little sequence homology with the typical bacterial ASADHs. They are mainly from archaea and fungi. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain. Family also includes NADP-dependent malonyl-CoA reductase (MCR, EC 1.2.1.75), which catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA
IKVGVLGATGMVGQRFIQLLANHPWFELAALGASERSAGKKYGDAVRWKQDTPIPEEVADMVVKECEPEE
FKDCDIVFSALDSDVAGEIEPAFAKAGIPVFSNASNHRMDPDVPLVIPEVNPDHLDLIEAQRKRRGWKGF
IVTNPNNTVRGAAGGAILNAEL
>gnl|CDD|467519 cd02316, VcASADH2_like_N, N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase 2 (ASADH2) and similar proteins. The family corresponds to a new branch of bacterial ASADH enzymes that has a similar overall fold and domain organization but sharing less sequence homology with the other bacterial ASADHs. The second isoform of ASADH in Vibrio cholerae is one of the prototypes of this family. It also includes ASADHs from Streptococcus pneumoniae, Mycobacterium tuberculosis, Thermus thermophilus, as well as from eukaryotes. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain
YNVAIVGATGAVGQEMLKVLEERNFPVSELRLLASARSAGKTLEFKGKELTVEELTEDSFKGVDIALFSA
GGSVSKEFAPIAAEAGAVVIDNSSAFRMDPDVPLVVPEVNPEALKNHKGIIANPNNLRKGAALNAVQIAE
LL
>gnl|CDD|100064 cd02325, R3H, R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner
REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGPNRRVVITK
>gnl|CDD|239074 cd02334, ZZ_dystrophin, Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan
AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY
>gnl|CDD|239075 cd02335, ZZ_ADA2, Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding
YHCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRVV
>gnl|CDD|239076 cd02336, ZZ_RSC8, Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of the RSC complex, which is closely related to the SWI/SNF complex and is involved in remodeling chromatin structure. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding
YHCFTCGNDCTRVRYHNLKAKKYDLCPSCYQEGRFPSNFQSSDFI
>gnl|CDD|239077 cd02337, ZZ_CBP, Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear
YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL
>gnl|CDD|239078 cd02338, ZZ_PCMF_like, Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination
VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQCI
>gnl|CDD|239079 cd02339, ZZ_Mind_bomb, Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster
IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY
>gnl|CDD|239080 cd02340, ZZ_NBR1_like, Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain
VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGVHPEHAMLKI
>gnl|CDD|239081 cd02341, ZZ_ZZZ3, Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding
FKCDSCGIEPIPGTRYHCSECDDGDFDLCQDCVVKGESHQEDHWLVKI
>gnl|CDD|239082 cd02342, ZZ_UBA_plant, Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding
IQCDGCGVLPITGPRYKSKVKEDYDLCTICFSRMGNEGEYTRI
>gnl|CDD|239083 cd02343, ZZ_EF, Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding
ISCDGCDEIAPWHRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEMVNM
>gnl|CDD|239084 cd02344, ZZ_HERC2, Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding
VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGRI
>gnl|CDD|239085 cd02345, ZZ_dah, Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila
LSCSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYEL
>gnl|CDD|411803 cd02393, KH-I_PNPase, type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins. PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain
YAPRITTIKIPPDKIGDVIGPGGKTIRAIIEETGAKIDIEDDGTVTIFATDKESAEAAKAMIEDIVAEPE
>gnl|CDD|411804 cd02394, KH-I_Vigilin_rpt6, sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins. Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one
MAFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRIEGSPEGVKKAKAEILELVD
>gnl|CDD|411805 cd02395, KH-I_BBP, type I K homology (KH) RNA-binding domain found in yeast branchpoint-bridging protein (BBP) and similar proteins. Yeast BBP, also called mud synthetic-lethal 5 protein, or splicing factor 1, or zinc finger protein BBP, is a mammalian splicing factor SF1 ortholog. It is involved in protein-protein interactions that bridge the 3' and 5' splice-site ends of the intron during the early steps of yeast pre-mRNA splicing. BBP interacts specifically with the pre-mRNA branchpoint sequence UACUAAC
KKQRKIYIPVDEYPDYNFIGLIIGPRGNTQKRMEKESGAKIAIRGKGSVKEGKGRSDPQPDPDEEEDLHV
LITADTEEKVDKAAKLIEKLLI
>gnl|CDD|411806 cd02396, KH-I_PCBP_rpt2, second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs). The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one
PITLRLLVPASQCGSLIGKGGSKIKEIRESTGASVQVASEMLPNSTERAVTISGSPEAITKCVEQICCVM
LE
>gnl|CDD|239090 cd02406, CRS2, Chloroplast RNA splicing 2 (CRS2) is a nuclear-encoded protein required for the splicing of group II introns in the chloroplast. CRS2 forms stable complexes with two CRS2-associated factors, CAF1 and CAF2, which are required for the splicing of distinct subsets of CRS2-dependent introns. CRS2 is closely related to bacterial peptidyl-tRNA hydrolases (PTH)
TPWLIAGLGNPGNKYKGTRHNVGFEMVDRIAEAEGITMNTIQFKSLLGIGSIGDVPVLLAKPQTYMNYSG
ESVGPLAAYYKVPLRHILVIYDDMSLPNGVLRLQPKGGHGRHNGLQSVIEHLDGSREFPRLSIGIGSPPG
KMDPRAFLLQKFSSEEREQIDTALEQGVDAVRTLVLKGFNGSAERFNLVQK
>gnl|CDD|239091 cd02407, PTH2_family, Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA from the premature translation termination product peptidyl-tRNA. Two structurally different enzymes have been reported to encode such activity, Pth present in bacteria and eukaryotes and Pth2 present in archaea and eukaryotes
YKMVIVVRNDLKMGKGKIAAQCAHAALAAYKKAMKDPPTLLRAWELEGQKKVVLKVPSEEELLELAKKAK
ELGLPHSLIQDAGRTQIPPGTPTVLAIGPAPKEKVDKVTGHLKLL
>gnl|CDD|411780 cd02409, KH-II_SF, type II K-homology (KH) RNA-binding domain superfamily. The K-homology (KH) domain binds single-stranded RNA or DNA, and is found in a wide variety of proteins including ribosomal proteins, transcription factors, and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but share a single "minimal KH motif" which is folded into a beta-alpha-alpha-beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension while type I KH domains (e.g. hnRNP K) contain a C-terminal extension, connected to the KH motif by variable loops that are different in different KH domains, whether they are type I or type II. KH-II superfamily members contain one or two KH domains, most of which are canonical type II KH domains that have the signature motif GXXG (where X represents any amino acid). The first KH domain found in archaeal cleavage and polyadenylation specificity factors (CPSFs) is a non-canonical type II KH domain that lacks the GXXG motif. Some others have mutated GXXG motifs which may or may not have nucleic acid binding ability
AEILEKLFPAAVTISDVEVEETPDGIRVIIAVEEGDPGIVIGKGGQRIRELRKELGKLGGGVEIDVV
>gnl|CDD|411781 cd02410, KH-II_CPSF_arch_rpt2, second type II K-homology (KH) RNA-binding domain found in archaeal cleavage and polyadenylation specificity factor (CPSF) and similar proteins. The archaeal CPSFs are predicted to be metal-dependent RNases belonging to the beta-CASP family, a subgroup of enzymes within the metallo-beta-lactamase fold. Within the CPSF family, all archaeal genomes contain one member with two N-terminal type II K-homology (KH) domains and one without. This family includes the CPSF homologs from archaea possessing N-terminal KH domains. This model corresponds to the second KH domain of CPSF, which is a canonical type II KH domain that contains the signature motif GXXG (where X represents any amino acid)
PEEAIEIIKEIVPEEAGISNIFFDPSTGEVIIEAEKPGLVIGKHGATLREITKETGWRPKVVRTPPIKSR
TIKSIR
>gnl|CDD|411782 cd02411, KH-II_30S_S3_arch, type II K-homology (KH) RNA-binding domain found in archaeal 30S ribosomal protein S3 and similar proteins. 30S ribosomal protein S3, also called small ribosomal subunit protein uS3, is part of the head region of the 30S ribosomal subunit and binds to the lower part of the 30S subunit head. It is believed to interact with mRNA as it threads its way from the latch into the channel. Members of this family are mainly from archaea and contain only one canonical type II K-homology (KH) domain that has the signature motif GXXG (where X represents any amino acid)
AIEKKFIEEGLKRMKIDEYLAKELERAGYGGMELKKTPLGTKVIIYAERPGMVIGRGGRNIRRLTEILEE
EFGLENPQIEVKEVENP
>gnl|CDD|411783 cd02412, KH-II_30S_S3, type II K-homology (KH) RNA-binding domain found in 30S ribosomal protein S3 and similar proteins. 30S ribosomal protein S3, also called small ribosomal subunit protein uS3, is part of the head region of the 30S ribosomal subunit and binds to the lower part of the 30S subunit head. It may also bind mRNA in the 70S ribosome, positioning it for translation. S3 protein is believed to interact with mRNA as it threads its way from the latch into the channel. Members of this family contain only one canonical type II K-homology (KH) domain that has the signature motif GXXG (where X represents any amino acid)
GQKVNPLGFRLGITKDWDSRWYADKKDYAKLLLEDLKIRKYIKKKLKKAGISRIEIERKADKIRVTIHTA
RPGIVIGKKGAEIEKLRKELEKLTGKKVNINVVEVKKP
>gnl|CDD|411784 cd02413, KH-II_40S_S3, type II K-homology (KH) RNA-binding domain found in 40S ribosomal protein S3 and similar proteins. 40S ribosomal protein S3, also called small ribosomal subunit protein uS3, is part of the head region of the 40S ribosomal subunit and is involved in translation. It is believed to interact with mRNA as it threads its way from the latch into the channel. 40S ribosomal protein S3 has endonuclease activity and plays a role in repair of damaged DNA. It cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA. Members of this family are mainly from prokaryotes and contain only one canonical type II K-homology (KH) domain that has the signature motif GXXG (where X represents any amino acid)
ISKKRKFVADGVFYAELNEFLTRELAEDGYSGVEVRVTPTRTEIIIRATRTQNVLGEKGRRIRELTSLVQ
KRFGFPEGSVELYAEKVANRG
>gnl|CDD|411785 cd02414, KH-II_Jag, type II K-homology (KH) RNA-binding domain found in protein Jag and similar proteins. Protein Jag, also called SpoIIIJ-associated protein, is associated with SpoIIIJ and is necessary for the third stage of sporulation. Members of this family are mainly from bacteria and contain only one canonical type II K-homology (KH) domain that has the signature motif GXXG (where X represents any amino acid)
EAKEFLEELLDAMGIEAEVEVEEEEGTVKLNIDGEDPGLLIGKHGETLDALQYLANLVLNKEFGKRVRVV
LDVEGYRER
>gnl|CDD|239098 cd02417, Peptidase_C39_likeA, A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in this sub-family
SATKPDSGLLALVLLARYHGIAADPEQLRHEFGLAGEPFNSTELLLAAKSLGLKAKAVRQPVERLARLPL
PALAWDDDGGHFILAKLDGQKYLIQDPISQRPEVLSREEFEARWSGELILV
>gnl|CDD|239099 cd02418, Peptidase_C39B, A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family
YPYVLQVDEMDCGAACLAMIAKYYGKNYSLAKLRELAGTDREGTSLLGLVKAAEKLGFETRAVKADMDLF
ELKDIPLPFIAHVIKEWKLNHYVVVYKIKKKKILIADPAVGITKISKEEFEKEWTGVALFLEPTPN
>gnl|CDD|239100 cd02419, Peptidase_C39C, A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family
LPVILQTEAAECGLACLAMIASYHGHHVDLASLRQRFPVSLKGATLADLIDIAQQLGLSTRALRLDLEEL
GQLKLPCILHWDMNHFVVLKKVSRRRIVIHDPALGKRKLSLEEASRHFTGVALELWP
>gnl|CDD|239101 cd02420, Peptidase_C39D, A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family
TPTVLQMEATECGAASLAIILAYYGRYVPLSELRIACGVSRDGSNASNLLKAAREYGLTAKGYKKDLEAL
REVSLPAIVFWNFNHFLVVEGFDKRKVFLNDPATGRRTVSLEEFDQSFTGVVLTM
>gnl|CDD|239102 cd02421, Peptidase_C39_likeD, A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in this sub-family
DLTRDDPLLDCLVLLARQFGKPASRDSLVAGLPLDDGRLSPALFPRAAARAGLSARVVRRPLDAIPTLLL
PAILLLKNGRACVLLGVDDGHARILDPESGGGEVEISLEELEEEYSGYAIFVKP
>gnl|CDD|239103 cd02423, Peptidase_C39G, A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature
DGVVRQSYDFSCGPAALATLLRYYGGINITEQEVLKLMLIRSEGFSMLDLKRYAEALGLKANGYRLNLDK
LNALQIPVIVLVNNGGYGHFVVIKGIDGDRVLVGDPALGNISMSREEFERIWTGNALFV
>gnl|CDD|239104 cd02424, Peptidase_C39E, A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family, which contains Colicin V perocessing peptidase
MKIIKQTDLNDCGIAVIQMLYNHYYKKKYDLNELKIKANLKKNGLSIYDLENLAKKFGLETESYQGSFLE
FLELKNKFIILLKSNGLNHFVIVKKIKKNKFIVLDPKKGKYKITYKEFEKIFNNIIITV
>gnl|CDD|239105 cd02425, Peptidase_C39F, A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family
VKPILQNNQTECGLACYAMILNYFGYKVSLNELREKYELGRDGLSLSYLKQLLEEYGFKCKVYKISFKKN
LYPLKLPVIIFWNNNHFVVLEKIKKNKVTIVDPAIGRIKISIDEFLENFSGYILTF
>gnl|CDD|239106 cd02426, Pol_gamma_b_Cterm, C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for processivity. Polymerase gamma replicates and repairs mitochondrial DNA. The c-terminal domain of its B subunit is strikingly similar to the anticodon-binding domain of glycyl tRNA synthetase
AQLAELSDGRKKGRQRQVLKLHPCLAPYKVAIDCGKGDTAELRDLCQGLKNELREAGLSVWPGYLETQHS
SLEQLLDKYDEMGVLFTLLISEQTLENGLLQLRSRDTTLKETIHISDLPDYLLRYIAA
>gnl|CDD|239107 cd02429, PTH2_like, Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA from the premature translation termination product peptidyl-tRNA. Two structurally different enzymes have been reported to encode such activity, Pth present in bacteria and eukaryotes and Pth2 present in archaea and eukaryotes. There is no functional information for this eukaryote-specific subgroup
LVQYVILRRDLQTKLSWPLGAVIAQACHAAVAVIHLFRSDPDTKKYAYLSNLDNMHKVVLEVPDEAALKN
LSSKLTENSIKHKLWIEQPENIPTCIALKPYPKETVASYLKKLKLL
>gnl|CDD|239108 cd02430, PTH2, Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA from the premature translation termination product peptidyl-tRNA, therefore allowing the tRNA and peptide to be reused in protein synthesis. PTH2 is present in archaea and eukaryotes
YKMVLVVRNDLKMGKGKIAAQCAHAALGAYKKAMKSNPELLRAWEREGQKKIVLKVNSEEELLELKKKAK
SLGLPTSLIQDAGRTQIAPGTITVLGIGPAPEELIDKVTGHLKLL
>gnl|CDD|153122 cd02431, Ferritin_CCC1_C, CCC1-related domain of ferritin. Ferritin_CCC1_like_C: The proteins of this family contain two domains. This is the C-terminal domain that is closely related to the CCC1, a vacuole transmembrane protein functioning as an iron and manganese transporter. The N-terminal domain is similar to ferritin-like diiron-carboxylate proteins, which are involved in a variety of iron ion related functions, such as iron storage and regulation, mono-oxygenation, and reactive radical production. This family may be unique to certain bacteria and archaea
VGDFVLGLNDALVEITGALAGLTGAINNTILVGLSGLIVGIAAALSMAIGAYLSTKSESGVKESNPVKSA
LYTGIAYIIGVVIPILPYLLLSSVYLALALSVTLAVLAILIFNFYISVASGISFRKKFIEMAGLALGAAF
ISFLLGYLL
>gnl|CDD|153123 cd02432, Nodulin-21_like_1, Nodulin-21 and CCC1-related protein family. Nodulin-21_like_1: This is a family of proteins closely related to nodulin-21, a plant nodule-specific protein that may be involved in symbiotic nitrogen fixation. This family is also related to CCC1, a yeast vacuole transmembrane protein that functions as an iron and manganese transporter
LIERLNWLRAAVLGANDGIVSVAGLVVGVAAATASSFTILIAGLAGLVAGALSMAAGEYVSVSSQRDTEK
ADIAKERRELAEDPEAELEELADIYEERGLSPELARQVADELMAKDALEAHARDELGITEGEYANPWQAA
LASAISFSVGALLPLLAILLAPAAWKVPVTIIATLLALALTGYVSARLGGASVLRAILRNVIWGALAMAL
TYLIGRLF
>gnl|CDD|153124 cd02433, Nodulin-21_like_2, Nodulin-21 and CCC1-related protein family. Nodulin-21_like_2: This is a family of proteins closely related to nodulin-21, a plant nodule-specific protein that may be involved in symbiotic nitrogen fixation. This family is also related to CCC1, a yeast vacuole transmembrane protein that functions as an iron and manganese transporter
HAEVVRGLAARGRHRMSGNLRAAVFGANDGLVSNLALVMGVAGAGVSNQTILLTGLAGLLAGALSMAAGE
YVSVTSQRELLEASIPDERRELRKHPLEEAAELALIYRAKGLDEEEAKRVASQLMNDPEQALDTLAREEL
GLDPELLGNPWSAAVSSFLLFALGALIPVLPFLFGMSGLAALVLSVLLVGLALLATGAVTGLLSGRSPGI
SALRQLAIGGGAAAVTYLLGLLFG
>gnl|CDD|153125 cd02434, Nodulin-21_like_3, Nodulin-21 and CCC1-related protein family. Nodulin-21_like_3: This is a family of proteins closely related to nodulin-21, a plant nodule-specific protein that may be involved in symbiotic nitrogen fixation. This family is also related to CCC1, a yeast vacuole transmembrane protein that functions as an iron and manganese transporter
EYLKSIVFGGLDGIVTIFAIVAGVVGAGLSPFVILIIGFANLLADGISMAAGEYVSTKAERDFLHSEKKR
EEWEIENYPEGEKSEMVEIYSLKGLSEEVADQVVELLSKYRKLFVDIMMTEELGLIPDDELPSPLKTALV
TFLSFLVFGIIPLLPYLLGLYYYSQKEIDSVFALSILIFVAFTLFLLGSFKSKLYNGKWIISGIIMLING
AASGGVSFFLGVLFT
>gnl|CDD|153126 cd02435, CCC1, CCC1. CCC1: This domain is present in the CCC1, an iron and manganese transporter of Saccharomyces cerevisiae. CCC1 is a transmembrane protein that is located in the vacuole and transfers the iron and manganese ions from the cytosol to the vacuole. This domain may be unique to certain fungi and plants
DPSSQHSTSSHSEKHFTSPRIVRDIIIGLSDGLTVPFALTAGLSSLGDTKLVITGGLAELAAGAISMGLG
GYLAAKSERDHYQREHKRKQEAVEASPSTEQEEIILYDLVQYGLVPLETAASTVTDLRKNPQALVDFLMR
FGLGLEEPDTSRALISALTIGLSYFIGGLIPLLPYFFVSTVGEALLLSVIVTLVALFVFGYVKTWFTGGW
GGAGGGVWGAVQMLVVGGLAAGAAWGLVKLL
>gnl|CDD|153127 cd02436, Nodulin-21, Nodulin-21. Nodulin-21: This is a family of proteins that may be unique to certain plants. The family member in soybean is found to be nodule-specific and is abundant during nodule development. The proteins of this family thus may play a role in symbiotic nitrogen fixation
QWLRAAVLGANDGLVSVASLMLGVGAVCADEHAMLLSGLAGLVAGACPMAIGEFVRVYRQYRRPRAARCL
RGRNRARGPAPDSEPEGLRRQAPSPSSAATASALSFAAGALFPLLAAWFVASYASRRVLPPQSSAPAAPP
GRSPATVTASSF
>gnl|CDD|153128 cd02437, CCC1_like_1, CCC1-related protein family. CCC1_like_1: This is a protein family closely related to CCC1, a family of proteins involved in iron and manganese transport. Yeast CCC1 is a vacuole transmembrane protein responsible for the iron and manganese accumulation in vacuole
STIRYGIYGLIDGSLSTLGVVFGASLAFDLDPKIIIAAGLGGAFALGISNGLGAAVAEEGSLRGMLEEKE
KILLRLEQMLTSTREELAIRKADLPSGLIQGISTTLGGLLPLLPFLPFDLWLAAGIAVAIVLAILFILGL
VIGKISKINVAISFVWAVGMVITGISLVFSVGKLF
>gnl|CDD|143332 cd02439, DMB-PRT_CobT, Nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase (DMB-PRT), also called CobT. Nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase (DMB-PRT/CobT, not to be confused with the CobT subunit of cobaltochelatase, which does not belong to this group) catalyzes the synthesis of alpha-ribazole-5'-phosphate, from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). This function is essential to the anaerobic biosynthesis pathway of cobalamin (vitamin B12), which is the largest and most complex cofactor in a number of enzyme-catalyzed reactions in bacteria, archaea and eukaryotes. Only eubacteria and archaebacteria can synthesize vitamin B12; multicellular organisms have lost this ability during evolution. DMB-PRT/CobT works sequentially with CobC (a phosphatase) to couple the lower ligand of cobalamin to a ribosyl moiety. DMB is the most common lower ligand of cobamides; other lower ligands include adenine, 5-methoxybenzimidazole or phenol. It has been suggested that earlier metabolic or enzymatic steps may control which lower ligand is available to DMB-PRT/CobT. In Salmonella enterica, for example, the lower ligand is DMB under aerobic conditions and adenine or 2-methyladenine under anaerobic conditions. Salmonella enterica DMB-PRT/CobT is a homodimer with two active sites, each active site is comprised of residues from both monomers. This group includes two distinct subfamilies, one archaeal-like, the other comprised of bacterial sequences
TKPLGSLGRLETLASQIAGIQGAGPPALPEKTVLTFAADHGVAAEGVSAYPQEVTAQMVGNFPTGGAAIN
ALARLAGADLLVVDAGLAVDPPVPPILLGKVRGGTANFAKGPAMTREEAEAALEAGIELAREALDSGYDL
LVIGEMGIGNTTTAAAVLAALGGDPAEEVSGRGTGLPDEGLERKIAVVEEALARNGPDPDDPLDVLAKVG
GPEIAAMAGLILGAAARRVPVLLDGFIQMAAALAAVRLAPDARDYLIATHRSVEPGHRLLLEALGLEPLL
DLGMRLGEGTGAALALPLLRGAAAELNEMATFEEA
>gnl|CDD|100107 cd02440, AdoMet_MTases, S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.)
RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVI
ISDPPLHHLVEDLARFLEEARRLLKPGGVLVLTLVLA
>gnl|CDD|133000 cd02503, MobA, MobA catalyzes the formation of molybdopterin guanine dinucleotide. The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target
ITGVILAGGKSRRMGGDKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALLGVPVIPDEPPGKG
PLAGILAALRAAPADWVLVLACDMPFLPPELLERLLAAAEEGADAVVPKSGGRLQPLHALYHKSLLPALE
ELLEAGERRLRRLLEKLGVQYVEFEDERLDAFFNINTPEDL
>gnl|CDD|133001 cd02507, eIF-2B_gamma_N_like, The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity. N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex
FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWS
SLSSKMIVDVITSDLCESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLEERRKKDKNAIATLTVL
LASPPVSTEQSKKTEEEDVIAVDSKTQRLLLLHYEEDLDEDLELIIRKSLLSKHPNVTIRTDLLDCHIYI
CSPDVL
>gnl|CDD|133002 cd02508, ADP_Glucose_PP, ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch. ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2
AIILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWD
LDRKNGGLFILPPQQRKGGDWYRGTADAIYQNLDYIERSDPEYVLILSGDHIYNMDYREMLDFHIESGAD
ITVVYKASMGIYIFSKDLLIELLEEDAADGSHDFGKDIIPAMLKKLKIYAYEFNGYWADI
>gnl|CDD|133003 cd02509, GDP-M1P_Guanylyltransferase, GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose. GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes
IYPVILAGGSGTRLWPLSRESYPKQFLKLFGDKSLLQQTLDRLKGLVPPDRILVVTNEEYRFLVREQLPE
GLPEENIILEPEGRNTAPAIALAALYLAKRDPDAVLLVLPSDHLIEDVEAFLKAVKKAVEAAEEGYLVTF
GIKPTRPETGYGYIEAGEKLGGGVYRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHA
PDIYEALEKALAAAGTDDFLRLLEEAFAKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL
>gnl|CDD|133004 cd02510, pp-GalNAc-T, pp-GalNAc-T initiates the formation of mucin-type O-linked glycans. UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins
SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREG
LIRARIAGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGG
FDWSLHFKWLPLPEEERRRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQC
GGSIEIVPCSRVGHIFRRKRKPYTFPGGSGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERK
ALRERLKCKSFKWYLENVY
>gnl|CDD|133005 cd02511, Beta4Glucosyltransferase, UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide. UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core
TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRWWDGFGAQRNFALELA
TNDWVLSLDADERLTPELADEILALLATDDYDGYYVPRRNFFLGRWIRHGGWYPDRQLRLFRRGKARFED
GRVHEQVVVDGGVGIVLKGDILHYGYKSLEEFLEKHNRYSSLEAKDLAAKGKKRSLLKGLLLGRPLLAFL
KMYILKRGFLDGRAGFILA
>gnl|CDD|133006 cd02513, CMP-NeuAc_Synthase, CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety. CMP-N-acetylneuraminic acid synthetase (CMP-NeuAc synthetase) or acylneuraminate cytidylyltransferase catalyzes the transfer the CMP moiety of CTP to the anomeric hydroxyl group of NeuAc in the presence of Mg++. It is the second to last step in the sialylation of the oligosaccharide component of glycoconjugates by providing the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), the substrate for sialyltransferases. Eukaryotic CMP-NeuAc synthetases are predominantly located in the nucleus. The activated CMP-Neu5Ac diffuses from the nucleus into the cytoplasm
KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAEVPFLRP
AELATDTASSIDVILHALDQLEELGRDFDIVVLLQPTSPLRSAEDIDEAIELLLSEGADSVFSVTEFHRF
PWRALGLDDNGLEPVNYPEDKRTRRQDLPPAYHENGAIYIAKREALLESNSFFGGKTGPYEMPRERSIDI
DTEEDFELAEALL
>gnl|CDD|133007 cd02514, GT13_GLCNAC-TI, GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I, GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13
VIPVLVIACNRPDYLRRMLDSLLSYRPSAEKFPIIVSQDGGYEEVADVAKSFGDGVTHIQHPPISIKNVN
PPHKFQGYYRIARHYKWALTQTFNLFGYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDN
GKEHFVDDTPSLLYRTDFFPGLGWMLTRKLWKELEPKWPKAFWDDWMRLPEQRKGRECIRPEISRTYHFG
KKGVSNGQFFDKYLKKIKLNTVFVVFTKLDLSYLKKDNYDKEFHRLVYGAVVLDHEKNPCELSFVPDTEG
KVRVVYTGRDDFKTWAKAFGVMDDLKDGVPRTAYKGIVRFFFKGNRVFLVPPPT
>gnl|CDD|133008 cd02515, Glyco_transf_6, Glycosyltransferase family 6 comprises enzymes responsible for the production of the human ABO blood group antigens. Glycosyltransferase family 6, GT_6, comprises enzymes with three known activities: alpha-1,3-galactosyltransferase, alpha-1,3 N-acetylgalactosaminyltransferase, and alpha-galactosyltransferase. UDP-galactose:beta-galactosyl alpha-1,3-galactosyltransferase (alpha3GT) catalyzes the transfer of galactose from UDP-alpha-d-galactose into an alpha-1,3 linkage with beta-galactosyl groups in glycoconjugates. The enzyme exists in most mammalian species but is absent from humans, apes, and old world monkeys as a result of the mutational inactivation of the gene. The alpha-1,3 N-acetylgalactosaminyltransferase and alpha-galactosyltransferase are responsible for the production of the human ABO blood group antigens. A N-acetylgalactosaminyltransferases use a UDP-GalNAc donor to convert the H-antigen acceptor to the A antigen, whereas a galactosyltransferase uses a UDP-galactose donor to convert the H-antigen acceptor to the B antigen. Alpha-1,3 N-acetylgalactosaminyltransferase and alpha-galactosyltransferase differ only in the identity of four critical amino acid residues
RPDVLTVTPWLAPIVWEGTFNPDVLDEYYRKQNITIGLTVFAVGKYTEFLERFLESAEKHFMVGYRVIYY
IFTDKPAAVPEVELGPGRRLTVLKIAEESRWQDISMRRMKTLADHIADRIGHEVDYLFCMDVDMVFQGPF
GVETLGDSVAQLHPWWYGKPRKQFPYERRPSSAAYIPEGEGDFYYHGAVFGGSVEEVYRLTRACHEGILA
DKANGIEARWHDESHLNKYFLLHKPTKVLSPEYLWDDRIGQAAEIRLPRLSWLPKNYQEVR
>gnl|CDD|133009 cd02516, CDP-ME_synthetase, CDP-ME synthetase is involved in mevalonate-independent isoprenoid production. 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs
VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKV
VKIVEGGATRQDSVLNGLKALPDADPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRV
DDDGVVVETLDREKLWAAQTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKIT
TPEDLALA
>gnl|CDD|133010 cd02517, CMP-KDO-Synthetase, CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the lipopolysaccharide. CMP-KDO Synthetase: 3-Deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) catalyzes the conversion of CTP and 3-deoxy-D-manno-octulosonate into CMP-3-deoxy-D-manno-octulosonate (CMP-KDO) and pyrophosphate. KDO is an essential component of the lipopolysaccharide found in the outer surface of gram-negative eubacteria. It is also a constituent of the capsular polysaccharides of some gram-negative eubacteria. Its presence in the cell wall polysaccharides of green algae and plant were also discovered. However, they have not been found in yeast and animals. The absence of the enzyme in mammalian cells makes it an attractive target molecule for drug design
KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAKGLDEVVVATDDERIADAVESFGGKVVMTSP
DHPSGTDRIAEVAEKLDADDDIVVNVQGDEPLIPPEMIDQVVAALKDDPGVDMATLATPISDEEELFNPN
VVKVVLDKDGYALYFSRSPIPYPRDSSEDFPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALE
NGYKIKVVETDHESIGVDTPEDLERVEAL
>gnl|CDD|133011 cd02518, GT2_SpsF, SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat. Spore coat polysaccharide biosynthesis protein F (spsF) is a glycosyltransferase implicated in the synthesis of the spore coat in a variety of bacteria challenged by stress as starvation. The spsF gene is expressed in the late stage of coat development responsible for a terminal step in coat formation that involves the glycosylation of the coat. SpsF gene mutation resulted in spores that appeared normal. But, the spores tended to aggregate and had abnormal adsorption properties, indicating a surface alteration
VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKRSKLIDEIVIATSTNEEDDPLEALAKKLGVKVFRG
SEEDVLGRYYQAAEEYNADVVVRITGDCPLIDPEIIDAVIRLFLKSGADYTSNTLPRTYPDGLDVEVFTR
DALERAAAEADDPYEREHVTPYIRRHPELFRIGYLEAPPDRLSDLRLTVDTPEDFELIKEIYEALYPKNP
DFSLEDIIELLDKNPELFEINAH
>gnl|CDD|133012 cd02520, Glucosylceramide_synthase, Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis. UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment
PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVG
INPKVNNLIKGYEEARYDILVISDSDISVPPDYLRRMVAPLMDPGVGLVTCLCAFGKSMALRREVLDAIG
GFEAFADYLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSRTR
>gnl|CDD|133013 cd02522, GT_2_like_a, GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function. Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families
LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGVVVISSPKGRARQMNAGAAA
ARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAFRLRFDDPGPRLRLLELGANLRSRLFGLPYGDQG
LFIRRELFEELGGFPELPLMEDVELVRRLRRRGRPALLPSPVTTSARRWERNGWLRTTLLNWLLLLLYLL
GVSPERLAKRY
>gnl|CDD|133014 cd02523, PC_cytidylyltransferase, Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline. This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide
AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKF
VYNPDYAETNNIYSLYLARDFLDEDFLLLEGDVVFDPSILERLLSSPADNAILVDKKTKEWEDEYVKDLD
DAGVLLGIISKAKNLEEIQGEYVGISKFSPEDADRLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKD
ISDGFWYEIDDLEDLERAE
>gnl|CDD|133015 cd02524, G1P_cytidylyltransferase, G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose. Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity
VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNS
DVTIDLGTNRIELHNSDIEDWKVTLVDTGLNTMTGGRLKRVRRYLGDDETFMLTYGDGVSDVNINALIEF
HRSHGKLATVTAVHPPGRFGELDLDDDGQVTSFTEKPQGDGGWINGGFFVLEPEVFDYIDGDDTVFEREP
LERLAKDGELMAYKHTGFWQCMDTLRDKQTLEELWNSGKAPWK
>gnl|CDD|133016 cd02525, Succinoglycan_BP_ExoA, ExoA is involved in the biosynthesis of succinoglycan. Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus
FVSIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRIQS
AGLNIGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIAVAQSSPLGS
GGSAYRGGAVKIGYVDTVHHGAYRREVFEKVGGFDESLVRNEDAELNYRLRKAGYKIWLSPDIRVYYYPR
STLKKLARQYFRYGKWRARTLRKHRKSLSLRHLLPLAFV
>gnl|CDD|133017 cd02526, GT2_RfbF_like, RfbF is a putative dTDP-rhamnosyl transferase. Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen
AVVVTYNPDLSKLKELLAALAEQVDKVVVVDNSSGNDIELRLRLNSEKIELIHLGENLGIAKALNIGIKA
ALENGADYVLLFDQDSVPPPDMVEKLLAYKILSDKNSNIGAVGPRIIDRRTGENSPGVRKSGYKLRIQKE
GEEGLKEVDFLITSGSLISLEALEKVGGFDEDLFIDYVDTEWCLRARSKGYKIYVVPDAVLKHELGDKRV
KRLGGVSVPLHSPLRRYYLFRNAIYLL
>gnl|CDD|133018 cd02537, GT8_Glycogenin, Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen. Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases
EAYVTLLTNDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANLL
KRPRFKDTYTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLPGEFAAAPDCGWPDLFNSGVFVLKPSEE
TFNDLLDALQDTPSFDGGDQGLLNSYFSDRGIWKRLPFTYNALKPLRYLHPEALWFGDEIKVVHFIGGDK
PWSWWRDPETKEKDDYNELHQWWWDIYDEL
>gnl|CDD|133019 cd02538, G1P_TT_short, G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase. This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced
MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSD
LGIRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDP
ERYGVVEFDENGRVLSIEEKPKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKL
SVELLGRGFAWLDTGTHESLLEASNFVQTI
>gnl|CDD|133020 cd02540, GT2_GlmU_N_bac, N-terminal domain of bacterial GlmU. The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively
AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNVEFVLQE
EQLGTGHAVKQALPALKDFEGDVLVLYGDVPLITPETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIR
DGNGKVLRIVEEKDATEEEKAIREVNAGIYAFDAEFLFEALPKLTNNNAQGEYYLTDIIALAVADGLKVA
AVLADDEEEVLGVNDRVQL
>gnl|CDD|133021 cd02541, UGPase_prokaryotic, Prokaryotic UGPase catalyses the synthesis of UDP-glucose. Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids, glycoproteins, and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity
RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYEL
EETLEKKGKTDLLEEVRIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQ
LIEAYEKTGASVIAVEEVPPEDVSKYGIVKGEKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIF
DILENTKPGKGGEIQLTDAIAKLLEEEPVYAYVFEGKRYDCGNKLGYLKATVEFALK
>gnl|CDD|239109 cd02549, Peptidase_C39A, A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures
PQLENGCGPTSLAMVLSYLGVKVTKPQLAAEGNTYDFAKDGYGTYPKPIVSAAARKYGLVVRPLTGLLAL
LRQLAAGHPVIVSVNLGVSITPSGHAMVVIGYDRKGNVYVNDPGGGRRLVVSFDEFEKAWKRMGGQAVVI
L
>gnl|CDD|211325 cd02550, PseudoU_synth_Rsu_Rlu_like, Pseudouridine synthase, Rsu/Rlu family. This group is comprised of eukaryotic, bacterial and archeal proteins similar to eight site specific Escherichia coli pseudouridine synthases: RsuA, RluA, RluB, RluC, RluD, RluE, RluF and TruA. Pseudouridine synthases catalyze the isomerization of specific uridines in a n RNA molecule to pseudouridines (5-ribosyluracil, psi) requiring no cofactors. E. coli RluC for example makes psi955, 2504 and 2580 in 23S RNA. Some psi sites such as psi1917 in 23S RNA made by RluD are universally conserved. Other psi sites occur in a more restricted fashion, for example psi2819 in 21S mitochondrial ribosomal RNA made by S. cerevisiae Pus5p is only found in mitochondrial large subunit rRNAs from some other species and in gram negative bacteria. The E. coli counterpart of this psi residue is psi2580 in 23S rRNA. psi2604in 23S RNA made by RluF has only been detected in E.coli
ILVLNKPSGLVCHPTDRDRDPTVVVRLDKLHGPRVHAAGRLDKDTSGLLLLTNDGRLQRRLTEPRREIEK
EYLVTVRGELDEEGIEDLATVRRGRLSGLVDEGVPLAVTKVRVIGEHGGTGRLRLTLKTGRTHQIRRHCA
AVGFPVLRLHRVRI
>gnl|CDD|211326 cd02552, PseudoU_synth_TruD_like, Pseudouridine synthase, TruD family. This group consists of eukaryotic, bacterial and archeal pseudouridine synthases similar to Escherichia coli TruD and Saccharomyces cerevisiae Pus7. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). E. coli TruD and S. cerevisiae Pus7 make psi13 in cytoplasmic tRNAs. In addition S. cerevisiae Pus7 makes psi35 in U2 small nuclear RNA (U2 snRNA) and psi35 in pre-tRNATyr. Psi35 in U2 snRNA and psi13 in tRNAs are highly phylogenetically conserved. Psi34 is the mammalian U2 snRNA counterpart of yeast U2 snRNA psi35
GRLKQRPEDFVVNEILLDGPVVHLWPKGEGEYLHFTLYKENKDTMEALREIAKALGVPPRDIGYAGTKDK
RAVTTQRVSVHKPGKERLALLNLELKGIRILEFGRHDKKLRLGDLKGNRFTITLRGVSPEEDELIERRLE
SLKEKGFPNYFGLQRFGSMYLHAYQSYLFNEVLSERIELYGFNRVVEGDVKPKNLKWSEERYDDLEGEKL
ALKLSFSLPRGSYATMVLRELL
>gnl|CDD|211327 cd02553, PseudoU_synth_RsuA, Pseudouridine synthase, Escherichia coli RsuA like. This group is comprised of eukaryotic and bacterial proteins similar to Escherichia coli RsuA. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E.coli RsuA makes psi516 in 16S RNA. Psi at this position is not generally conserved in other organisms
VYLMLNKPAGVVCATKDPHHPTVIDLLPEPDRRRDLFPVGRLDKDTTGLLLLTNDGQLAHRLTSPKKHVP
KTYEVTLAGPLTEDDIEAFAEGVLLHDGYPTKPAKLEILSPTTVRLTITEGKYHQVKRMFAAVGNKVVAL
HRIRIGGLELDDDLAPGEWRPLTEEEL
>gnl|CDD|211328 cd02554, PseudoU_synth_RluF, Pseudouridine synthase, Escherichia coli RluF like. This group is comprised of bacterial proteins similar to Escherichia coli RluF. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E.coli RluF makes psi2604 in 23S RNA. psi2604 has only been detected in E. coli. It is absent from other eubacteria despite a precursor U at that site and from eukarya and archea which lack a precursor U at that site
VYIAYNKPVGIDCTLERADEDNIIDFVNPPPRIFPIGRLDKDSEGLILLTNDGDLVNKILHADNNHEKEY
LVTVNKPITDEFIEGMSNGVVILGTVTKPCKVERLAKDKFRIVLTQGLNRQIRRMCEALGYRVTDLKRVR
IMNIELGDLAPGEWRPLTDAELFE
>gnl|CDD|211329 cd02555, PSSA_1, Pseudouridine synthase, a subgroup of the RsuA family. This group is comprised of bacterial proteins assigned to the RsuA family of pseudouridine synthases. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. The TruA family is comprised of proteins related to Escherichia coli RsuA
QLEPVTLLLHKPAGMVSEQALALLGPGQRSAADRSGRRPLKGHFARLAPIGPLDKDASGLLVFSQDGRVL
RKLIGDASRLEQEYLVEVRGELTAGGLERLNHGLTYDGRELPPAKVSWQNEQRLRFALKEPQPGQIRRMC
ESVGLEVVALRRIRIGRVSLGKLPLGQWRYLTTGERF
>gnl|CDD|211330 cd02556, PseudoU_synth_RluB, Pseudouridine synthase, Escherichia coli RluB like. This group is comprised of bacterial and eukaryotic proteins similar to E. coli RluB. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E.coli RluB makes psi2605 in 23S RNA. psi2605 has been detected in eubacteria but, not in eukarya and archea despite the presence of a precursor U at that site
RVLIYHKPEGLICTRKDPKGRPTVFDLLPKLGIPRWISVGRLDLNTEGLLLFTNDGELANRLMHPSNEIE
REYAVRVFGQVTDEQLKSLKKGVELEDGFAGFKSIQLEGGEGKNSWYRVTLREGRNREVRRLWEAFGLQV
SRLIRIRYGPIFLPGNLKRGQWEELPP
>gnl|CDD|211331 cd02557, PseudoU_synth_ScRIB2, Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2. Pseudouridine synthase, Saccharomyces cerevisiae RIB2_like. This group is comprised of eukaryotic and bacterial proteins similar to Saccharomyces cerevisiae RIB2, S. cerevisiae Pus6p and human hRPUDSD2. S. cerevisiae RIB2 displays two distinct catalytic activities. The N-terminal domain of RIB2 is RNA:psi-synthase which makes psi32 on cytoplasmic tRNAs. Psi32 is highly phylogenetically conserved. The C-terminal domain of RIB2 has a DRAP deaminase activity which catalyses the formation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate from 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate during riboflavin biosynthesis. S. cerevisiae Pus6p makes the psi31 of cytoplasmic and mitochondrial tRNAs
SHTVHRHEPPVTNDPIKIVHEDDDLLVVDKPSGIPVHPTGRYRYNTVTEILKSEYGLTELRPCHRLDRLT
SGLLLFAKTSQTASRLQQQIRSREVKKEYLARVKGEFPDGEVVVDQPIGLVSPKGGLRNDVDEKGKDART
IFKRLSYNGDLNTSVVLCKPITGRTHQIRVHLQYLGHPIVNDPIYNNLGIYLHALRYEGPDWSYETELPD
WAS
>gnl|CDD|211332 cd02558, PSRA_1, Pseudouridine synthase, a subgroup of the RluA family. This group is comprised of bacterial proteins assigned to the RluA family of pseudouridine synthases. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. The RluA family is comprised of proteins related to Escherichia coli RluA
GLVVDADGEPLDPDSPYRPGTFVWYYRELPDEPPIPFEETILHQDEHLLVADKPHFLPVTPRGRYVTETL
LVRLRRQTGNPDLTPAHRLDRLTAGLVLFSKRPETRGAYQTLFARREVSKTYEAVAPYVPALTFPLTVRS
RIVKGRGFFQAREVEGEPNAETRIELLARRGGWGLYRLSPHTGKTHQLRVHMAALGVPILNDPFYPVLLD
KDPDDFSRPLQLLAKELEFTDPLTGRPRRFESGRSL
>gnl|CDD|211333 cd02563, PseudoU_synth_TruC, tRNA pseudouridine isomerase C. Pseudouridine synthases catalyze the isomerization of specific uridines in an tRNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. TruC makes psi65 in tRNAs. This psi residue is not universally conserved
LEILYQDEHLVAINKPSGLLVHRSELDRHETRFALQTLRDQLGQHVYPVHRLDRPTSGVLLFALSSEVAR
KLGEQFTEHRVHKTYLAVVRGYVPESGTIDYPLSEELDKLADKFASDDKAPQAATTHYRLLAVEELPVVV
GKYPTSRYSLVELTPHTGRKHQLRRHLAHIRHPIIGDTTHGDGRHNRFFREHFGCHRLLLAATRLEFTHP
VTGERLLIEAPLD
>gnl|CDD|211334 cd02566, PseudoU_synth_RluE, Pseudouridine synthase, Escherichia coli RluE. This group is comprised of bacterial proteins similar to E. coli RluE. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. Escherichia coli RluE makes psi2457 in 23S RNA. psi2457 is not universally conserved
LILFNKPYGVLSQFTDESEKHKTLKDYIDDPGVYAAGRLDRDSEGLLLLTDDGRLQHRITDPSFKHPKTY
YVQVEGVPTEDALEQLRNGVELGDGLTLPAKVEKVDEPPWLWEREPPIRFRKNIPTSWIEITICEGKNRQ
VRRMTAAVGFPTLRLIRVSIGDIGLDNL
>gnl|CDD|211335 cd02568, PseudoU_synth_PUS1_PUS2, Pseudouridine synthase, PUS1/ PUS2 like. This group consists of eukaryotic pseudouridine synthases similar to Saccharomyces cerevisiae Pus1p, S. cerevisiae Pus2p, Caenorhabditis elegans Pus1p and human PUS1. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. S. cerevisiae Pus1p catalyzes the formation of psi34 and psi36 in the intron-containing tRNAIle, psi35 in the intron-containing tRNATyr, psi27 and/or psi28 in several yeast cytoplasmic tRNAs and, psi44 in U2 small nuclear RNA (U2 snRNA). The presence of the intron is required for the formation of psi 34, 35 and 36. In addition S. cerevisiae PUS1 makes are psi 26, 65 and 67. C. elegans Pus1p does not modify psi44 in U2 snRNA. Mouse Pus1p makes psi27/28 in pre- tRNASer, tRNAVal and tRNAIle, psi 34/36 in tRNAIle and, psi 32 and potentially 67 in tRNAVal. Psi44 in U2 snRNA and psi32 in tRNAs are highly phylogenetically conserved. Psi 26,27,28,34,35,36,65 and 67 in tRNAs are less highly conserved. Mouse Pus1p regulates nuclear receptor activity through pseudouridylation of Steroid Receptor RNA Activator. Missense mutation in human PUS1 causes mitochondrial myopathy and sideroblastic anemia (MLASA)
LLFGYCGTGYHGMQYNPGAYKTIEGELERALFKAGAISESNAGDPKKIGFSRAARTDKGVHAARNVVSLK
VIIDDPEGLGILEDLVEKLNSHLPSDIRVFGITRVTKSFNARKACDSRTYEYLLPTFALETLQRFNEILK
EYVGTHNFHNFTVKKKFEDPSANRFIKSFYVSEPFVIEEGLEWISIKIHGQSFMLHQIRKMIGLAIAIVR
GGAPESLIELSFNKDKIIIIPLAPGLGLLLERPHF
>gnl|CDD|211336 cd02569, PseudoU_synth_ScPus3, Pseudouridine synthase, Saccharomyces cerevisiae Pus3 like. This group consists of eukaryotic pseudouridine synthases similar to S. cerevisiae Pus3p, mouse Pus3p and, human PUS2. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. S. cerevisiae Pus3p makes psi38 and psi39 in tRNAs. Mouse Pus3p has been shown to makes psi38 and, possibly also psi 39, in tRNAs. Psi38 and psi39 are highly conserved in tRNAs from eubacteria, archea and eukarya
LRFAYLGWNYNGFAVQEETTNTVEETLFEALEKTRLIEDRQTSNYSRCGRTDKGVSAFGQVISLDVRSNL
KPEDGLDPSTDVKSTADEEELPYCKILNRVLPPDIRILAWAPVPPDFSARFSCVSRTYRYFFPKGDLDIE
LMRKAAKLLLGEHDFRNFCKMDVANQVTNYVRRVLSAEVEPVDQHPDGDGLYYFEVRGSAFLWHQVRCMM
AVLFLIGQGLEPPSVISQLLDVEKNPRKPQYTMASEVPLVLYDCGF
>gnl|CDD|211337 cd02570, PseudoU_synth_EcTruA, Eukaryotic and bacterial pseudouridine synthases similar to E. coli TruA. This group consists of eukaryotic and bacterial pseudouridine synthases similar to E. coli TruA, Pseudomonas aeruginosa truA and human pseudouridine synthase-like 1 (PUSL1). Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E. coli TruA makes psi38/39 and/or 40 in tRNA. psi38 and psi39 in tRNAs are highly phylogenetically conserved. P. aeruginosa truA is required for induction of type III secretory genes and may act through modifying tRNAs critical for the expression of type III genes or their regulators
LTIEYDGTNFSGWQRQPNGRTVQGELEKALSKIAGEPVRVIGAGRTDAGVHALGQVAHFDTPSEIPLEKL
IKALNSLLPPDIRVLSAEEVPDDFHARFSAKSRTYRYRILNRPVPSPFLRRYVWHVPRPLDIEAMQEAAK
LLLGTHDFSSFRAAGCQSKSTVRTIYRADVYREGDLIVFEIRANGFLYHMVRNIVGTLLEVGRGKLSPED
IKEILEAKDRTAAGPTAPAHGLYLVKVEY
>gnl|CDD|211338 cd02572, PseudoU_synth_hDyskerin, Pseudouridine synthase, human dyskerin like. This group consists of eukaryotic and archeal pseudouridine synthases similar to human dyskerin, Saccharomyces cerevisiae Cbf5, and Drosophila melanogaster Mfl (minifly protein). Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactor is required. S. cerevisiae Cbf5 and human dyskerin are nucleolar proteins that, with the help of guide RNAs, make the hundreds of psueudouridnes present in rRNA and small nuclear RNAs (snRNAs). Cbf5/Dyskerin is the catalytic subunit of eukaryotic box H/ACA small nucleolar ribonucleoprotein (snoRNP) particles. D. melanogaster mfl hosts in its fourth intron, a box H/AC snoRNA gene. In addition dyskerin is likely to have a structural role in the telomerase complex. Mutations in human dyskerin cause X-linked dyskeratosis congenitas. Mutations in Drosophila Mfl results in miniflies that suffer abnormalities
KYGVINLDKPSGPSSHEVVAWIKRILGVEKTGHSGTLDPKVTGCLPVCIDRATRLVKSQQEAGKEYVCVM
RLHDDVDEEKVRRVLEEFTGAIFQRPPLISAVKRQLRVRTIYESKLLEYDGERRLVLFRVSCEAGTYIRT
LCVHIGLLLGVGAHMQELRRTRSGPFSEEDNMVTLHDVLDAQ
>gnl|CDD|211339 cd02573, PseudoU_synth_EcTruB, Pseudouridine synthase, Escherichia coli TruB like. This group consists of bacterial pseudouridine synthases similar to E. coli TruB and Mycobacterium tuberculosis TruB. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). E. coli TruB and M. tuberculosis TruB make psi55 in the T loop of tRNAs. Psi55 is nearly universally conserved. E. coli TruB is not inhibited by RNA containing 5-fluorouridine
GILLLDKPAGLTSHDVVQKVRRLLGTKKVGHTGTLDPLATGVLPIALGEATKLSQYLLDADKTYRATVRL
GEATDTDDAEGEIIETSPPPRLTEEEIEAALKAFTGEIEQVPPMYSAVKVDGKRLYELARAGEEVERPPR
KVTIYSLELLSFDPENPEADFEVHCSKGTYIRSLARDLGKALGCGAHLSALRRTRSGPFTLEQAITLEEL
EAL
>gnl|CDD|211340 cd02575, PseudoU_synth_EcTruD, Pseudouridine synthase, similar to Escherichia coli TruD. This group consists of bacterial pseudouridine synthases similar to Escherichia coli TruD. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). E. coli TruD makes the highly phylogenetically conserved psi13 in tRNAs
GHLKATPEDFQVEEVLGYEPSGEGEHLLLHIRKTGLNTREVAKELAKALGVKERDVGYAGLKDRHAVTTQ
WFSVHLPGKEAPDLSALQLEGVKILEVTRHNRKLRRGHLKGNRFVIRLRGVSGNADKLEQRLETIAQKGV
PNYFGPQRFGRDGGNLLQGLRLLAGERKVRDRNKRSFLLSAARSYLFNRVLSERLEQGSWNRVLDGDVLQ
LAGSGSWFVPQRLAWQWPEDAGLELSFYLPAGSYATSVLRELL
>gnl|CDD|211341 cd02576, PseudoU_synth_ScPUS7, Pseudouridine synthase, TruD family. This group consists of eukaryotic pseudouridine synthases similar to Saccharomyces cerevisiae Pus7. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). Saccharomyces cerevisiae Pus7 makes psi35 in U2 small nuclear RNA (U2 snRNA), psi13 in cytoplasmic tRNAs and psi35 in pre-tRNATyr. Psi35 in yeast U2 snRNA and psi13 in tRNAs are highly phylogenetically conserved. Psi34 is the mammalian U2 snRNA counterpart of yeast U2 snRNA psi35
GFRGIIKQRYSDFVVNEIDLDGSVVHLTDYLHFTLYKENKDTMEAINKIAKLLRVKPSDFSYAGTKDKRA
VTVQRVSVKKVTASRLKALNSKLRGIRVGNFEYKDEPLKLGDLKGNEFTIVIRNVKADSEELIKQALESL
KEKGFINYYGLQRFGTFSIPTHEIGIAILKENWKEAVDLILKPRSELEEGDLVEAREIWKETGDAKAALK
KLPRKKVAEKALLRGLSKYGNGPNDYLGAIGSIPRNLRSMYVHAYQSYVWNLAVSKRIKLYGLKVVEGDL
VIVIYDVVLPLPGHDVIYPSNEIGEWYKEVLSKDGLDPDNMRRKEREFSLSGGYRKILVKPKNLEYSFLA
LKLKFSLPSSSYATMALRELM
>gnl|CDD|211342 cd02577, PSTD1, Pseudouridine synthase, a subgroup of the TruD family. This group consists of several hypothetical archeal pseudouridine synthases assigned to the TruD family of psuedouridine synthases. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). The TruD family is comprised of proteins related to Escherichia coli TruD
GRLKQYPEDFIVEEITPFDIGKKGKYLIYLLEKKNWDTLDAVRRIAKALGISRKRIGYAGTKDKHAVTTQ
YISIFDPKDEEKLSIKDIELKVLGRSRKPLRLGDLWGNRFEITVRDLGDEEIERIETLVEEVEKGGFPNY
FGSQRFGSVRPVTHFVGKLILEGDYEEAAKTYLTARYPLEETGDKKRALRLFPKWGDWERCLKEYPTNLE
ERRVKHLLAEPKDYKGAFLALPKNLRRMFVHAYQSYLFNEILSERIEEGGPLNEAVEGDILERKASVKPG
DFKIGEERPDELNPGKDKVVLSFTLPRGSYATSVLRELI
>gnl|CDD|259846 cd02582, RNAP_archeal_A', A' subunit of archaeal RNA polymerase (RNAP). A' is the largest subunit of the archaeal RNA polymerase (RNAP). Archaeal RNAP is closely related to RNA polymerases in eukaryotes based on the subunit compositions. Archaeal RNAP is a large multi-protein complex, made up of 11 to 13 subunits, depending on the species, that are responsible for the synthesis of RNA. Structure studies suggest that RNAP complexes from different organisms share a crab-claw-shaped structure. The largest eukaryotic RNAP subunit is encoded by two separate archaeal subunits (A' and A'') which correspond to the N- and C-terminal domains of eukaryotic RNAP II Rpb1, respectively. The N-terminal domain of Rpb1 forms part of the active site and includes the head and the core of one clamp as well as the pore and funnel structures of RNAP II. Based on a structural comparison among the archaeal, bacterial and eukaryotic RNAPs the DNA binding channel and the active site are part of A' subunit which is conserved. The strong similarity between subunit A' and the N-terminal domain of Rpb1 suggests a similar functional and structural role for these two proteins
PKRIKGIKFGLLSPEEIRKMSVVEIITPDTYDEDGYPIEGGLMDPRLGVIEPGLRCKTCGNTAGECPGHF
GHIELARPVIHVGFAKHIYDLLRATCRSCGRILLPEEEIEKYLERIRRLKEKWPELVKRVIEKVKKKAKK
RKVCPHCGAPQYKIKLEKPTTFYEEKEEGEVKLTPSEIRERLEKIPDEDLELLGIDPKTARPEWMVLTVL
PVPPVTVRPSITLETGERSEDDLTHKLVDIIRINQRLKENIEAGAPQLIIEDLWDLLQYHVTTYFDNEIP
GIPPARHRSGRPLKTLAQRLKGKEGRFRGNLSGKRVNFSARTVISPDPNLSINEVGVPEDIAKELTVPER
VTEWNIEKMRKLVLNGPDKWPGANYVIRPDGRRIRLRYVNREELAERLEPGWIVERHLIDGDIVLFNRQP
SLHRMSIMAHRVRVLPGKTFRLNLAVCPPYNADFDGDEMNLHVPQSEEARAEARELMLVQEHILSPRYGG
PIIGGIQDYISGAYLLTRKTTLFTKEEALQLLSAAGYDGLLPEPAILEPKPLWTGKQLFSLFLPKDLNFE
GKAKVCSGCSECKDEDCPNDGYVVIKNGKLLEGVIDKKAIGAEQPGSLLHRIAKEYGNEVARRFLDSVTR
LAIRFIELRGFTIGIDDEDIPEEARKEIEEIIKEAEKKVYELIEQYKNGELEPLPGRTLEETLEMKIMQV
LGKARDEAGKVASKYLDPFNNAVIMARTGARGSMLNLTQMAACLGQQSVRGERINRGYRNRTLPHFKPGD
LGPEARGFVRSSFRDGLSPTEFFFHAMGGREGLVDTAVRTSQSGYMQRRLINALQDLYVEYDGTVRDSRG
NIIQFKYGEDGVDPAKSDHGK
>gnl|CDD|259847 cd02583, RNAP_III_RPC1_N, Largest subunit (RPC1) of eukaryotic RNA polymerase III (RNAP III), N-terminal domain. Rpc1 (C160) subunit forms part of the active site region of RNAP III. RNAP III is one of the three distinct classes of nuclear RNAP in eukaryotes that is responsible for the synthesis of tRNAs, 5SrRNA, Alu-RNA, U6 snRNA genes, and some others. RNAP III is the largest nuclear RNA polymerase with 17 subunits. Structure studies suggest that different RNA polymerase complexes share a similar crab-claw-shaped structure. The N-terminal domain of Rpb1, the largest subunit of RNAP II in yeast, forms part of the active site, making up the head and core of the one clamp, as well as the pore and funnel structures of RNAP II. The strong homology between Rpc1 and Rpb1 suggests a similar functional and structural role
LSPEDIIRLSEVEVTNRNLYDIETRKPLPYGVLDPRLGTSDKDGICETCGLNLADCVGHFGYIKLELPVF
HIGYFKAIINILQCICKTCSRVLLPEEEKRKFLKRLRRPNLDNLQKKALKKKILEKCKKVRKCPHCGLLK
KAQEDLNPLKVLNLFKNIPPEDVELLLMNPLAGRPENLILTRIPVPPLCIRPSVVMDEKSGTNEDDLTVK
LSEIIFLNDVIKKHLEKGAKTQKIMEDWDFLQLQCALYINSELPGLPLSMQPKKPIRGFCQRLKGKQGRF
RGNLSGKRVDFSGRTVISPDPNLRIDQVGVPEHVAKILTYPERVTRYNIEKLRKLVLNGPDVHPGANFVI
KRDGGKKKFLKYGNRRKIARELKIGDIVERHLEDGDIVLFNRQPSLHRLSIMAHRAKVMPWRTFRFNECV
CTPYNADFDGDEMNLHVPQTEEARAEALELMGVKNNLVTPRNGEPLIAATQDFLTASYLLTSKDVFFDRA
QFCQLCSYMLDGEIKIDLPPPAILKPVELWTGKQIFSLLLRPNKKSPVLVNLEAKEKSYTKKSPDMCPND
GYVVIRNSELLCGRLDKSTLGSGSKNSLFYVLLRDYGPEAAAAAMNRLAKLSSRWLSNRGFSIGIDDVTP
SKELLKKKEELVDNGYAKCDEYIKQYKKGKLELQPGCTAEQTLEAKISGELSKIREDAGKACLKELHKSN
SPLIMALCGSKGSNINISQMIACVGQQIISGKRIPNGFEDRTLPHFPRNSKTPAAKGFVANSFYSGLTPT
EFFFHTMSGREGLVDTAVKTAETGYMQRRLMKALEDLSVQYDGTVR
>gnl|CDD|132720 cd02584, RNAP_II_Rpb1_C, Largest subunit (Rpb1) of Eukaryotic RNA polymerase II (RNAP II), C-terminal domain. RNA polymerase II (RNAP II) is a large multi-subunit complex responsible for the synthesis of mRNA. RNAP II consists of a 10-subunit core enzyme and a peripheral heterodimer of two subunits. The largest core subunit (Rpb1) of yeast RNAP II is the best characterized member of this family. Structure studies suggest that RNAP complexes from different organisms share a crab-claw-shape structure. In yeast, Rpb1 and Rpb2, the largest and the second largest subunits, each makes up one clamp, one jaw, and part of the cleft. Rpb1 interacts with Rpb2 to form the DNA entry and RNA exit channels in addition to the catalytic center of RNA synthesis. The C-terminal domain of Rpb1 makes up part of the foot and jaw structures
YRLNKEAFDWILGEIETRFNRSLVHPGEMVGTIAAQSIGEPATQMTLNTFHFAGVSAKNVTLGVPRLKEI
INVAKNIKTPSLTVYLEPGFAKDEEKAKKIQSRLEHTTLKDVTAATEIYYDPDPQNTVIEEDKEFVESYF
EFPDEDVEQDRLSPWLLRIELDRKKMTDKKLSMEQIAKKIKEEFKDDLNVIFSDDNAEKLVIRIRIINDD
EEKEEDSEDDVFLKKIESNMLSDMTLKGIEGIRKVFIREENKKKVDIETGEFKKREEWVLETDGVNLREV
LSHPGVDPTRTTSNDIVEIFEVLGIEAARKALLKELRNVISFDGSYVNYRHLALLCDVMTQRGHLMAITR
HGINRQDTGPLMRCSFEETVDILLEAAAFGETDDLKGVSENIMLGQLAPIGTGCFDLLLD
>gnl|CDD|319784 cd02585, HAD_PMM, phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis thaliana PMM. PMM catalyzes the interconversion of mannose-6-phosphate (M6P) to mannose-1-phosphate (M1P); the conversion of M6P to M1P is an essential step in mannose activation and the biosynthesis of glycoconjugates in all eukaryotes. M1P is the substrate for the synthesis of GDP-mannose, which is an intermediate for protein glycosylation, protein sorting and secretion, and maintaining a functional endomembrane system in eukaryotic cells. Proteins in this family contains a conserved phosphorylated motif DxDx(T/V) shared with some other phosphotransferases. This family contains two human homologs, PMM1 and PMM2; PMM2 deficiency causes congenital disorder of glycosylation type I-a, also known as Jaeken syndrome. PMM1 can also act as glucose-1,6-bisphosphatase in the brain after stimulation with inosine monophosphate; PMM2 on the other hand, is insensitive to IMP and demonstrates low glucose-1,6-bisphosphatase activity. Arabidopsis thaliana PMM converted M1P into M6P and glucose-1-phosphate into glucose-6-phosphate, with the latter reaction being less efficient. Arabidopsis thaliana and Nicotiana benthamian PPMs are involved in ascorbic acid biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LLLFDVDGTLTPPRQPITPEMAEFLAELRQKVKIGVVGGSDYDKIKEQLGDNVPLLDFDYVFPENGLVAY
RDGELLSRQSIIRALGEEKLQALINFCLRYIADLDLPKKRGTFIEFRNGMINISPIGRNCSQEERIEFEE
LDKKHKIREKFVSALKEEFADKGLTFSIGGQISFDVFPKGWDKTYCLRHLEEDLYEEIHFFGDKTQPGGN
DYEIYQDPRTIGHSVTSPKDTVRILEEL
>gnl|CDD|319785 cd02586, HAD_PHN, Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase. Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
IEAVIFDWAGTTVDYGSFAPVNAFVEAFAQRGVQITLEEARKPMGLLKIDHIRALLEMPRVAEAWRAVFG
RLPTEADVDALYEEFEPILIASLAEYSSPIPGVLEVIAKLRARGIKIGSTTGYTREMMDIVLPEAAAQGY
RPDSLVTPDDVPAGRPYPWMCYKNAIELGVYDVAAVVKVGDTVPDIKEGLNAGMWTVGVILSGNELGLSE
EEVEALDSEELAARRAEVRQRFKAAGAHYVID
>gnl|CDD|319786 cd02587, HAD_5-3dNT, 5'(3')-deoxyribonucleotidase. This family includes cytosolic 5'(3')-deoxyribonucleotidase (cdN) and mitochondrial 5'(3')-deoxyribonucleotidase (mdN). cdN and mdN specifically dephosphorylate the deoxyribo form of nucleoside monophosphates helps maintain homeostasis of deoxynucleosides required for mitochondrial DNA synthesis. Their preferred substrates are dUMP and dTMP. cdN also dephosphorylates dGMP and dIMP efficiently. They can also dephosphorylate the 5'- or 3'-phosphates of pyrimidine ribonucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
IVILVDMDGVLADFEGALVRAIRERFPDEPHVLLESRRGFWVIEQYKAPELSRKAADILEEPGFFRNLEP
IPGAVEALRELSDEGTDVYICTSPLNKYPTCVEEKYEWVEEHFPPLFYQRIVLTRDKTVVLADILIDDNP
ENLEAFEGPGWEHILFTACHN
>gnl|CDD|319787 cd02588, HAD_L2-DEX, L-2-haloacid dehalogenase. L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
KALVFDVYGTLIDWHSGLAAAERAFPGRGEELSRLWRQKQLEYTWLVTLMGPYVDFDELTRDALRATAAE
LGLELDESDLDELGDAYLRLPPFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSA
EDVRAYKPAPAVYELAAERLGVPPDEILHVASHAWDLAGARALGLRTAWINRPGEVPDPLGPAPDFVVPD
LGELAD
>gnl|CDD|319788 cd02598, HAD_BPGM, beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM). Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
GVIFDLDGVITDTAEYHYRAWKKLADKEELAARKNRIYVELIEELTPVDVLPGIASLLVDLKAKGIKIAL
ASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNPKDCIGVEDAQAGIRAIKAAG
FLVVGVGREEDLLGADIVVPDTTADLTIEELLEV
>gnl|CDD|319789 cd02601, HAD_Eya, protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) and related phosphatase domains. Eyes absent (Eya) is a transcriptional coactivator, and an aspartyl-based protein tyrosine phosphatase. Eya and Six operate as a composite transcription factor, within a conserved network of transcription factors called the retinal determination (RD) network. The RD network interacts with a broad variety of signaling pathways to regulate the development and homeostasis of organs and tissues such as eye, muscle, kidney and ear. To date it is not clear what the physiologically relevant substrates of the Eya protein tyrosine phosphatase are, or whether this phosphatase activity plays a role in transcription. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
PERVFVWDLDETIIIFHSLLTGTYATRYGKDTETSVRIGLMMEELIFNLADNHFFFNDLEECDQVHIDDV
SSDDNGQDLSTYNFLTDGFHMRAVAPNLCLPTGVRGVDWMRKLAFRYRRVKENYNTYKNNVGFLLGEAKR
EAWLQLRTEIEALTDQWLTLALKALDLISSRENCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATK
IGKESCFERIQQRFGRKCVYVCIGDGVEEEQAAKKHNVPFWRISTHSDLLALHHALELEYL
>gnl|CDD|319790 cd02603, HAD_sEH-N_like, N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive. This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
IRAVLFDFGGVLIDPDPAAAVARFEALTGEPSEFVLDTEGLAGAFLELERGRITEEEFWEELREELGRPL
SAELFEELVLAAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESCRLGVR
KPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDALRELA
>gnl|CDD|319791 cd02604, HAD_5NT, haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p. This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
VWFFDLDNTLYPLSTGLFDQIQARITEFVATKLGLSPEEARRLRKSYYKEYGTTLRGLMAEHGIDPDEFL
DRVVHLILYDHLKPDPKLRNLLLALPGRKIIFTNASKNHAIRVLKRLGLADLFDGIFDIEYAGPDPKPHP
AAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVLVGP
>gnl|CDD|319792 cd02605, HAD_SPP, sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP. Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LLVSDLDETLVGHDTNLQALERLQDLLEQLTADNDVILVYATGRSPESVLELIKEVMLPKPDFIISDVGT
EIYYGESGYLEPDTYWNEVLSEGWERFLFEAIADLFKQLKPQSELEQNPHKISFYLDPQNDAAVIEQLEE
MLLKAGLTVRIIYSSGLAYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIV
GNAQPELLKWADRVTRSRLAKGPYAGGILEGLAHF
>gnl|CDD|319793 cd02607, HAD_ThrH_like, bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to Pseudomonas aeruginosa ThrH. This family includes Pseudomonas aeruginosa ThrH which is a duel activity enzyme having both phosphoserine phosphatase and phosphoserine:homoserine phosphotransferase activities, i.e. it can dephosphorylate phosphoserine, and can transfer phosphate from phosphoserine to homoserine. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLADIQEVIATLKPL
EGAVEFVDWLRERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLQTDDDDRVVGYQLRQKDPKRQSVIAV
KSLYYRVIAAGDSYNDTTMLSEAHAGILFHAPENVIREFPQFPAVHTYEDLKAEF
>gnl|CDD|319794 cd02608, P-type_ATPase_Na-K_like, alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+)/K(+)-ATPase alpha subunits 1-4. This subfamily includes the alpha subunit of Na(+)/K(+)-ATPase a heteromeric transmembrane protein composed of an alpha- and beta-subunit and an optional third subunit belonging to the FXYD proteins which are more tissue specific regulatory subunits of the enzyme. The alpha-subunit is the catalytic subunit responsible for transport activities of the enzyme. This subfamily includes all four isotopes of the human alpha subunit: (alpha1-alpha4, encoded by the ATP1A1- ATP1A4 genes). Na(+)/K(+)-ATPase functions chiefly as an ion pump, hydrolyzing one molecule of ATP to pump three Na(+) out of the cell in exchange for two K(+)entering the cell per pump cycle. In addition Na(+)/K(+)-ATPase acts as a signal transducer. This subfamily also includes Oreochromis mossambicus (tilapia) Na(+)/K(+)-ATPase alpha 1 and alpha 3 subunits, and gastric H(+)/K(+)-ATPase which exchanges hydronium ion with potassium and is responsible for gastric acid secretion. Gastric H(+)/K(+)-ATPase is an alpha,beta-heterodimeric enzyme. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
GLTSARAAEILARDGPNALTPPPTTPEWVKFCKQLFGGFSMLLWIGAILCFLAYGIQAATEEEPSNDNLY
LGIVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIRDGEKMQINAEELVVGDLVEVKGGDRIPA
DIRIISAHGCKVDNSSLTGESEPQTRSPEFTHENPLETKNIAFFSTNCVEGTARGIVINTGDRTVMGRIA
TLASGLEVGKTPIAREIEHFIHIITGVAVFLGVSFFILSLILGYTWLEAVIFLIGIIVANVPEGLLATVT
VCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGASF
DKSSATWLALSRIAGLCNRAEFKAGQENVPILKRDVNGDASESALLKCIELSCGSVMEMRERNPKVAEIP
FNSTNKYQLSIHENEDPGDPRYLLVMKGAPERILDRCSTILINGKEQPLDEEMKEAFQNAYLELGGLGER
VLGFCHLYLPDDKFPEGFKFDTDEVNFPTENLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHP
ITAKAIAKGVGIIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQA
ADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTITILCIDLGTD
MVPAISLAYEKAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALAGFFTYFVIMAENGFLPSDLLG
LRVQWDDKYVNDLEDSYGQEWTYEQRKILEYTCHTAFFVSIVVVQWADLIICKTRRNSVFQQGMKNKILN
FGLFFETALAAFLSYCPGMDVALRMYPLKPTWWFCAFPFSLLIFVYDEVRKLIIRRNPGGWVEKE
>gnl|CDD|319795 cd02609, P-type_ATPase, uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized Streptococcus pneumoniae exported protein 7, Exp7. This subfamily contains P-type ATPase transporters of unknown function, similar to Streptococcus pneumoniae Exp7. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine
GLTTKEVEERQAEGKVNDQVEPVSRSVWQIVRENVFTLFNLINFVIAVLLILVGSYSNLAFLGVIIVNTV
IGIVQEIRAKRQLDKLSILNAPKVTVIRDGQEVKIPPEELVLDDILILKPGEQIPADGEVVEGGGLEVDE
SLLTGESDLIPKKAGDKLLSGSFVVSGAAYARVTAVGAESYAAKLTLEAKKHKLINSELLNSINKILKFT
SFIIIPLGLLLFVEALFRRGGGWRQAVVSTVAALLGMIPEGLVLLTSVALAVGAIRLAKKKVLVQELYSI
ETLARVDVLCLDKTGTITEGKMKVERVEPLDEANEAEAAAALAAFVAASEDNNATMQAIRAAFFGNNRFE
VTSIIPFSSARKWSAVEFRDGGTWVLGAPEVLLGDLPSEVLSRVNELAAQGYRVLLLARSAGALTHEQLP
VGLEPLALILLTDPIRPEAKETLAYFAEQGVAVKVISGDNPVTVSAIAKRAGLEGAESYIDASTLTTDEE
LAEAVENYTVFGRVTPEQKRQLVQALQALGHTVAMTGDGVNDVLALKEADCSIAMASGSDATRQVAQVVL
LDSDFSALPDVVFEGRRVVNNIERVASLFLVKTIYSVLLALICVITALPFPFLPIQITLISLFTIGIPSF
FLALEPNKRRIEGGFLRRVLTKALPPLNRWR
>gnl|CDD|319796 cd02612, HAD_PGPPase, phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C. This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LAFFDLDGTLIAGDSFFAFLRFKGIAERRAPLEELLLLRLMALYALGRLDGAGMEALLGFATAGLAGELA
ALVEEFVEEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTG
RIIGPPCYGEGKVKRLREWLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD
>gnl|CDD|319797 cd02616, HAD_PPase, pyrophosphatase similar to Bacillus subtilis PpaX. This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTREEVLPFIGPPLRETFEKIDPDKLEDMVEEFRKY
YREHNDDLTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPE
PVLKALELLGAEPEEALMVGDSPHDILAGKNAGVKTVGVTWGYKGREYLKAFNPDFIIDKMSDLLTI
>gnl|CDD|239110 cd02619, Peptidase_C1, C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; composed of two subfamilies of cysteine peptidases (CPs), C1A (papain) and C1B (bleomycin hydrolase). Papain-like enzymes are mostly endopeptidases with some exceptions like cathepsins B, C, H and X, which are exopeptidases. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds while mammalian CPs are primarily lysosomal enzymes responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. Bleomycin hydrolase (BH) is a CP that detoxifies bleomycin by hydrolysis of an amide group. It acts as a carboxypeptidase on its C-terminus to convert itself into an aminopeptidase and peptide ligase. BH is found in all tissues in mammals as well as in many other eukaryotes. It forms a hexameric ring barrel structure with the active sites imbedded in the central channel. Some members of the C1 family are proteins classified as non-peptidase homologs which lack peptidase activity or have missing active site residues
SVDLRPLRLTPVKNQGSRGSCWAFASAYALESAYRIKGGEDEYVDLSPQYLYICANDECLGINGSCDGGG
PLSALLKLVALKGIPPEEDYPYGAESDGEEPKSEAALNAAKVKLKDYRRVLKNNIEDIKEALAKGGPVVA
GFDVYSGFDRLKEGIIYEEIVYLLYEDGDLGGHAVVIVGYDDNYVEGKGAFIVKNSWGTDWGDNGYGRIS
YEDVYEMTFGANV
>gnl|CDD|239111 cd02620, Peptidase_C1A_CathepsinB, Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial nephritis antigen (TIN-Ag). Cathepsin B is a lysosomal papain-like cysteine peptidase which is expressed in all tissues and functions primarily as an exopeptidase through its carboxydipeptidyl activity. Together with other cathepsins, it is involved in the degradation of proteins, proenzyme activation, Ag processing, metabolism and apoptosis. Cathepsin B has been implicated in a number of human diseases such as cancer, rheumatoid arthritis, osteoporosis and Alzheimer's disease. The unique carboxydipeptidyl activity of cathepsin B is attributed to the presence of an occluding loop in its active site which favors the binding of the C-termini of substrate proteins. Some members of this group do not possess the occluding loop. TIN-Ag is an extracellular matrix basement protein which was originally identified as a target Ag involved in anti-tubular basement membrane antibody-mediated interstitial nephritis. It plays a role in renal tubulogenesis and is defective in hereditary tubulointerstitial disorders. TIN-Ag is exclusively expressed in kidney tissues
PESFDAREKWPNCISIGEIRDQGNCGSCWAFSAVEAFSDRLCIQSNGKENVLLSAQDLLSCCSGCGDGCN
GGYPDAAWKYLTTTGVVTGGCQPYTIPPCGHHPEGPPPCCGTPYCTPKCQDGCEKTYEEDKHKGKSAYSV
PSDETDIMKEIMTNGPVQAAFTVYEDFLYYKSGVYQHTSGKQLGGHAVKIIGWGVENGVPYWLAANSWGT
DWGENGYFRILRGSNECGIESEVVAG
>gnl|CDD|239112 cd02621, Peptidase_C1A_CathepsinC, Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine peptidase with chloride dependency and dipeptidyl aminopeptidase activity, resulting from its tetrameric structure which limits substrate access. Each subunit of the tetramer is composed of three peptides: the heavy and light chains, which together adopts the papain fold and forms the catalytic domain; and the residual propeptide region, which forms a beta barrel and points towards the substrate's N-terminus. The subunit composition is the result of the unique characteristic of procathepsin C maturation involving the cleavage of the catalytic domain and the non-autocatalytic excision of an activation peptide within its propeptide region. By removing N-terminal dipeptide extensions, cathepsin C activates granule serine peptidases (granzymes) involved in cell-mediated apoptosis, inflammation and tissue remodelling. Loss-of-function mutations in cathepsin C are associated with Papillon-Lefevre and Haim-Munk syndromes, rare diseases characterized by hyperkeratosis and early-onset periodontitis. Cathepsin C is widely expressed in many tissues with high levels in lung, kidney and placenta. It is also highly expressed in cytotoxic lymphocytes and mature myeloid cells
LPKSFDWGDVNNGFNYVSPVRNQGGCGSCYAFASVYALEARIMIASNKTDPLGQQPILSPQHVLSCSQYS
QGCDGGFPFLVGKFAEDFGIVTEDYFPYTADDDRPCKASPSECRRYYFSDYNYVGGCYGCTNEDEMKWEI
YRNGPIVVAFEVYSDFDFYKEGVYHHTDNDEVSDGDNDNFNPFELTNHAVLLVGWGEDEIKGEKYWIVKN
SWGSSWGEKGYFKIRRGTNECGIESQAVFAYPI
>gnl|CDD|100065 cd02636, R3H_sperm-antigen, R3H domain of a group of metazoan proteins that is related to the sperm-associated antigen 7. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner
RKSMEKEVSKFIKDSVRTREKFQPMDKVERSIVHDVAEVAGLTSFSFGEDEVDRYVMIFKK
>gnl|CDD|100066 cd02637, R3H_PARN, R3H domain of Poly(A)-specific ribonuclease (PARN). PARN is a poly(A)-specific 3' exonuclease from the RNase D family that, in Xenopus, deadenylates a specific class of maternal mRNAs which results in their translational repression. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA
IDEVIERIEAFLESEEDDLELEPCNGFQRKLIYQTLEQKYPKGIHVETLETEKKERLIVIEKGDK
>gnl|CDD|100067 cd02638, R3H_unknown_1, R3H domain of a group of eukaryotic proteins with unknown function. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner
VHRVSEELEIFLLSFQRYRVLLFPPLNSRRRYLIHQTVENRFLLSTFSVGEGWARRTVVCYK
>gnl|CDD|100068 cd02639, R3H_RRM, R3H domain of mainly fungal proteins which are associated with a RNA recognition motif (RRM) domain. Present in this group is the RNA-binding post-transcriptional regulator Cip2 (Csx1-interacting protein 2) involved in counteracting Csx1 function. Csx1 plays a central role in controlling gene expression during oxidative stress. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner
TLEIYSQLLLFKDDRMRDELAFPSSLSPAERRIVHLLASRLGLNHVSDGTGERRQVQITK
>gnl|CDD|100069 cd02640, R3H_NRF, R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB proteins that can silence the IFNbeta promoter via binding to a negative regulatory element (NRE). Beside R3H NRF also contains a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner
KNDYRQIIQNYAHSDDIRDMVFSPEFSKEERALIHQIAQKYGLKSRSYGSGNDRYLVISK
>gnl|CDD|100070 cd02641, R3H_Smubp-2_like, R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and an AN1-like Zinc finger domain and have been shown to bind single-stranded DNA. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA
VKHLKAMVKAFMKDPKATELEFPPTLSSHDRLLVHELAEELGLRHESTGEGSDRVITVSK
>gnl|CDD|100071 cd02642, R3H_encore_like, R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner
DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGGKCVIVNKT
>gnl|CDD|100072 cd02643, R3H_NF-X1, R3H domain of the X1 box binding protein (NF-X1) and related proteins. Human NF-X1 is a transcription factor that regulates the expression of class II major histocompatibility complex (MHC) genes. The Drosophila homolog shuttle craft (STC) has been shown to be a DNA- or RNA-binding protein required for proper axon guidance in the central nervous system and, the yeast homolog FAP1 encodes a dosage suppressor of rapamycin toxicity. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner
KNMAKKDPKFVKDVEKDLIELVESVNKGKQTSRSHSFPPMNREKRRIVHELAEHFGIESVSYDQEPKRNV
VATA
>gnl|CDD|100073 cd02644, R3H_jag, R3H domain found in proteins homologous to Bacillus subtilus Jag, which is associated with SpoIIIJ. SpoIIIJ is necessary for the third stage of sporulation. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner
RERREETLIRLAERAAEKVRRTGKPVKLEPMNAYERRIIHDALANDEDVETESEGEGPYRRVVISPK
>gnl|CDD|100074 cd02645, R3H_AAA, R3H domain of a group of proteins with unknown function, who also contain a AAA-ATPase (AAA) domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA or ssRNA in a sequence-specific manner
DALEEARLAIEQVVIPKGEPVELLPRSAYIRRLQHDLVERYQLRSESFGSEPNRRLRILP
>gnl|CDD|100075 cd02646, R3H_G-patch, R3H domain of a group of fungal and plant proteins with unknown function, who also contain a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the R3H domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner
IEDIKDEIEAFLLDSRDSLSFPPMDKHGRKTIHKLANCYNLKSKSRGKGKKRFVTVTK
>gnl|CDD|239113 cd02647, nuc_hydro_TvIAG, nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring nucleoside hydrolase from Trypanosoma vivax. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. Nucleoside hydrolases vary in their substrate specificity. This group contains eukaryotic and bacterial proteins similar to the purine specific inosine-adenosine-guanosine-preferring nucleoside hydrolase (IAG-NH) from T. vivax. T. vivax IAG-NH is of the order of a thousand to ten thousand fold more specific towards the naturally occurring purine nucleosides, than towards the pyrimidine nucleosides
KNVIFDHDGNVDDLVALLLLLKNEKVDLKGIGVSGIDADCYVEPAVSVTRKLIDRLGQRDAIPVGKGGSR
AVNPFPRSWRRDAAFSVDHLPILNERYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDS
DPDISSNIEEVYIMGGGVDAPGNVFTPPSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTRE
FLETDRQRFAAQRLPASDLAGQGYALVKPLEFNSTYYMWDVLTTLVLGAKEVDNTKESLILEVDTDGLSA
GQTVTSPNGRPLTLVTSNNSYGSNRFFDDYLE
>gnl|CDD|239114 cd02648, nuc_hydro_1, NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity
PHPIIIDTDPGVDDVLAILLALSSPEEVDVALISLTFGNTTLDHALRNVLRLFHVLERERAWRATPGVRY
RAFSADAEKPIVASGSDQPLEGERLTASYFHGRDGLSGVHWLHPDFTPVETWIPEIVAPLTPSDKPAYDV
ILDILREEPDHTVTIAALGPLTNLAAAARKDPETFAKVGEVVVMGGAIDVPGNTSPVAEFNCFADPYAAA
VVIDEPPSTAPEARRKLPLQVFPLDITTGHTLPYSSLFATYVTPRDAPERGSPLARWLEHVFISTFLTHP
RAFTPEEFLPDRSELFEMHDPLAVWYAIFADMPATGSIDGNGWKHTPRDFRVETSGQWTRGMCVVDRRGV
DEVTGTPGAKMFLERIG
>gnl|CDD|239115 cd02649, nuc_hydro_CeIAG, nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring nucleoside hydrolase from Caenorhabditis elegans. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains eukaryotic, bacterial and archeal proteins similar to the purine-preferring nucleoside hydrolase (IAG-NH) from C. elegans and the salivary purine nucleosidase from Aedes aegypti. C. elegans IAG-NH exhibits a high affinity for the substrate analogue p-nitrophenylriboside (p-NPR)
RKLIIDTDCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLL
GPGPTAAYFHGKDGFGDVGFPEPKDELELQKEHAVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSL
PQKIKRLYIMGGNREGVGNTTPAAEFNFHVDPEAAHIVLNSFGCPITIVPWETTLLAFPLDWEFEDKWAN
RLEKALFAESLNRREYAFASEGLGGDGWVPCDALAVAAALDPSIITRRLTYAVDVELHGELTRGQMVVDW
LGTLKKKPNARVITKIDREKFKELLY
>gnl|CDD|239116 cd02650, nuc_hydro_CaPnhB, NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes Purine/pyrimidine nucleoside hydrolase (pnhB). Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity
KLILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTR
PPFRIATFVHGDNGLGDVELPAPPRQPEDESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAK
LVKQVVVMGGAFTVPGNVTPAAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDSGGK
AGQFLADMLDYYIDFYQESPGLRGCALHDPLAVAAAVDPSLFTTREGVVRVETEGPTRGRTIGDRDGRRF
WDSSPNATVAVDVDVDERFLKRLM
>gnl|CDD|239117 cd02651, nuc_hydro_IU_UC_XIUA, nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, xanthosine-inosine-uridine-adenosine-preferring and, uridine-cytidine preferring nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains proteins similar to nucleoside hydrolases which hydrolyze both pyrimidine and purine ribonucleosides: the inosine-uridine preferring nucleoside hydrolase from Crithidia fasciculata, the inosine-uridine-xanthosine preferring nucleoside hydrolase RihC from Escherichia coli and the xanthosine-inosine-uridine-adenosine-preferring nucleoside hydrolase RihC from Salmonella enterica serovar Typhimurium. This group also contains proteins similar to the pyrimidine-specific uridine-cytidine preferring nucleoside hydrolases URH1 from Saccharomyces cerevisiae, E. coli RihA and E. coli RihB. E. coli RihA is equally efficient with uridine and cytidine, E. coli RihB prefers cytidine over uridine. S. cerevisiae URH1 prefers uridine over cytidine
PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVR
PLITASDIHGESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAER
IKEIVLMGGALGRGNITPAAEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVG
KMLAELLDFFAETYGSAFTEGPPLHDPCAVAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRP
ANAQVAVDVDVEKFWDLLLEAL
>gnl|CDD|239118 cd02652, nuc_hydro_2, NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial proteins similar to nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity
LILDTDIGGDPDDALALALAHALQKCDLLAVTITLADASARRAIDAVNRFYGRGDIPIGADYHGWPEDAK
DHAKFLLEGDRLHHDLESAEDALDAVKALRRLLASAEDASVTIVSIGPLTNLAALLDADADPLTGPELVR
QKVKRLVVMGGAFYDPDGNVQHREYNFVTDPKAAQRVAGRAQHLGIPVRIVWSGYELGEAVSYPHVLVIA
HPFNTPVFAAYWPRSHRRPLWDPLTLLAAVRGGGMLFDLREVQLGPGRVEVDSSGVTEFHPPESGRARRL
TSSPEKAALRAAE
>gnl|CDD|239119 cd02653, nuc_hydro_3, NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial proteins similar to nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity
KVIIDCDPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGADKPLAG
PLTTAQDTHGPDGLGYAELPASTRTLSDESAAQAWVDLARAHPDLIGLATGPLTNLALALREEPELPRLL
RRLVIMGGAFNSRGNTSPVAEWNYWVDPEAAKEVLAAFGGHPVRPTICGLDVTRAVVLTPNLLERLARAK
DSVGAFIEDALRFYFEFHWAYGHGYGAVIHDPLAAAVALNPNLARGRPAYVDVECTGVLTGQTVVDWAGF
WGKGANAEILTKVDSQDFMALFIERVLAIADTITRVLTNL
>gnl|CDD|239120 cd02654, nuc_hydro_CjNH, nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. This group contains eukaryotic and bacterial proteins similar to C. jejuni nucleoside hydrolase. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. C. jejuni nucleoside hydrolase is inactive against natural nucleosides or against common nucleoside analogues
KVILDNDIAMGRDTDDGLALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYAGANT
PLGRTNRAFHAWESLYGAYLWQGAWSPEYSDMYTNASIIRNASIPAALFMIEMVRKHPHEVSIVAAGPLT
NLALALRIDPDFAPLAKELVIMGGYLDDIGEFVNRHYASDFNLIMDPEAASIVLTAPWKSITIPGNVTNR
TCLTPEQIKADDPLRDFIRETLDLPIDYAKEFVGTGDGLPMWDELASAVALDPELATSSETFYIDVQTDS
DGGGQLIWPEDLLLAKGLRPYHVKVITAVDVAAFLNLI
>gnl|CDD|132721 cd02655, RNAP_beta'_C, Largest subunit (beta') of Bacterial DNA-dependent RNA polymerase (RNAP), C-terminal domain. Bacterial RNA polymerase (RNAP) is a large multi-subunit complex responsible for the synthesis of all RNAs in the cell. This family also includes the eukaryotic plastid-encoded RNAP beta" subunit. Structure studies suggest that RNAP complexes from different organisms share a crab-claw-shape structure with two pincers defining a central cleft. Beta' and beta, the largest and the second largest subunits of bacterial RNAP, each makes up one pincer and part of the base of the cleft. The C-terminal domain includes a G loop that forms part of the floor of the downstream DNA-binding cavity. The position of the G loop may determine the switch of the bridge helix between flipped-out and normal alpha-helical conformations
KLVELGEAVGIIAAQSIGEPGTQLTMRTFHTGGVATDITQGLPRVEELFEARKINPHDLLRIKFLGPEAV
QKYLVEEIQKVYRSQGVNINDKHIEIIVRQMTSKVKIIDPGDSGFLPGELVDLNEFEEENKRLLLLGKKP
AKYEPVLLGITKASLNTESFISAASFQETTKVLTEAAIEGKIDWLRGLKENVILGRLIPAGTGL
>gnl|CDD|239121 cd02656, MIT, MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear
ELLQQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKLLRKKVKEYLDRAEFLKELL
KKQKQ
>gnl|CDD|239122 cd02657, Peptidase_C19A, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQ
LLRMAFPQFAEKQNQGGYAQQDAEECWSQLLSVLSQKLPGAGSKGSFIDQLFGIELETKMKCTESPDEEE
VSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWK
RDIQKKAKILRKVKFPFELDLYELCTPSGYYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVS
EVTEEDILKLSGGGDWHIAYILLYK
>gnl|CDD|239123 cd02658, Peptidase_C19B, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKPASLKS
ENDPYQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPNDLFKFMIEDRLEC
LSCKKVKYTSELSEILSLPVPKDEATEKEEGELVYEPVPLEDCLKAYFAPETIEDFCSTCKEKTTATKTT
GFKTFPDYLVINMKRFQLLENWVPKKLDVPIDVPEELGPGKYELIAFISHKGTSVHSGHYVAHIKKEIDG
EGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ
>gnl|CDD|239124 cd02659, peptidase_C19C, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELT
DKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYF
LDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETM
MRIKINDRFEFPLELDMEPYTEKGLAKKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGK
WYKFNDDVVTPFDPNDAEEECFGGEETQKTYDSGPRAFKRTTNAYMLFYERKSP
>gnl|CDD|239125 cd02660, Peptidase_C19D, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPI
NLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRC
GGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSGTPTLSDCLDRFTRPEKLGDFAYKCSGCGSTQEATKQ
LSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELNMTPYTSSSIGDTQDSNSLDPDYTYDLFAVVV
HKGTLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFYH
>gnl|CDD|239126 cd02661, Peptidase_C19E, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIF
SSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLN
CKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIH
LKRFSNFRGGKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNM
DDSKVSPVSIETVLSQKAYILFYI
>gnl|CDD|239127 cd02662, Peptidase_C19F, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQQDAHELFQVLLETLEQLLKFPFDGLLASRIVCLQCG
ESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRCQTVIVRLPQILCIHLSRSVFD
GRGTSTKNSCKVSFPERLPKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKDKEPGSFVRMREGPSSTSH
PWWRISDTTVKEVSESEVLEQKSAYMLFYE
>gnl|CDD|239128 cd02663, Peptidase_C19G, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GLENFGNTCYCNSVLQALYFENLLTCLKDLFESISEQKKRTGVISPKKFITRLKRENELFDNYMHQDAHE
FLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLS
IDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIK
LFYRVVFPLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKIDENA
VEEFFGDSPNQATAYVLFYQ
>gnl|CDD|239129 cd02664, Peptidase_C19H, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEA
SRPPWFTPGSQQDCSEYLRYLLDRLHTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDLL
NYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSL
PVRVESKSSESPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGYSSESGHYFTYARDQTDADSTGQECPE
PKDAEENDESKNWYLFNDSRVTFSSFESVQNVTSRFPKDTPYILFYE
>gnl|CDD|239130 cd02665, Peptidase_C19I, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GLKNVGNTCWFSAVIQSLFSQQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGV
LEGKPFCNCETFGQYPLQVNGYGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFE
FNQGRPEKIHDKLEFPQIIQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVE
RDSFGGGRNPSAYCLMYI
>gnl|CDD|239131 cd02666, Peptidase_C19J, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTERRIGGREVSRSELQRSNQFVYEL
RSLFNDLIHSNTRSVTPSKELAYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKEQSDLIKR
LFSGKTKQQLVPESMGNQPSVRTKTERFLSLLVDVGKKGREIVVLLEPKDLYDALDRYFDYDSLTKLPQR
SQVQAQLAQPLQRELISMDRYELPSSIDDIDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDLKSYG
YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVFLFTLGNTATPYFLVYV
>gnl|CDD|239132 cd02667, Peptidase_C19K, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLRTFID
SIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKSECSIESCLKQFTEVEILEGNNKFACENCTKA
KKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLAPFCDPKCNSSEDKSSVLYRLYGVVEH
SGTMRSGHYVAYVKVRPPQQRLSDLTKSKPAADEAGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE
>gnl|CDD|239133 cd02668, Peptidase_C19L, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRS
VVDPSGFVKALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESS
LPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVF
DRKTGAKKKLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFN
DEDVEEMPGKPLKLGNSEDPAKPRKSEIKKGTHSSRTAYMLVYK
>gnl|CDD|239134 cd02669, Peptidase_C19M, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
PYLDTINRSVLDFDFEKVCSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCL
PDNYEIIDSSLDDIKYVLNPTYTKEQISDLDRDPKLSRDLDGKPYLPGFVGLNNIKNNDYANVIIQALSH
VKPIRNFFLLYENYENIKDRKSELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKVSKKKFSITEQSDP
VEFLSWLLNTLHKDLGGSKKPNSSIIHDCFQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVSPFLL
LTLDLPPPPLFKDGNEENIIPQVPLKQLLKKYDGKTETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFK
EKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLN
VKEVLPQLIFLSESYIQIWE
>gnl|CDD|239135 cd02670, Peptidase_C19N, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GAQNHCNVSCYLDALLFAMFAEQQDPEEFFNFITDKLLMPLLEPKVDIIHGGKKDQDDDKLVNERLLQIP
VPDDDDGGGITLEQCLEQYFNNSVFAKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVADDPR
ACSKCQLECRVCYDDKDFSPTCGKFKLSLCSAVCHRGTSLETGHYVAFVRYGSYSLTETDNEAYNAQWVF
FDDMADRDGVSNGFNIPAARLLEDPYMLFYQ
>gnl|CDD|239136 cd02671, Peptidase_C19O, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
DQVVPAPQPSSATSCEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSSF
LLNPEKYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEKDFQGQLVLRTRCLEC
ETFTERREDFQDISVPVQESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYT
EAERSLLFDKLPEVITIHLKCFAANGSEFDCYGGLSKVNTPLLTPLKLSLEEWSTKPKNDVYRLFAVVMH
SGATISSGHYTAYVRWLLFDDSEVKVTEEKDFLEALSPNTSSTSTPYLLFYK
>gnl|CDD|239137 cd02672, Peptidase_C19P, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GTEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNFTAIILVACPKESCLLCELGYLFSTLIQ
NFTRFLLETISQDQLGTPFSCGTSRNSVSLLYTLSLPLGSTKTSKESTFLQLLKRSLDLEKVTKAWCDTC
CKYQPLEQTTSIRHLPDILLLVLVINLSVTNGEFDDINVVLPSGKVMQNKVSPKAIDHDKLVKNRGQESI
YKYELVGYVCEINDSSRGQHNVVFVIKVNEESTHGRWYLFNDFLVTPVSELAYILLYQ
>gnl|CDD|239138 cd02673, Peptidase_C19Q, A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
RLVNTGNSCYFNSTMQALSSIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNP
LEAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMIDNKLDIDELLISNFKTWSPIEKDCSSCKCESAISS
ERIMTFPECLSINLKRYKLRIATSDYLKKNEEIMKKYCGTDAKYSLVAVICHLGESPYDGHYIAYTKELY
NGSSWLYCSDDEIRPVSKNDVSTNARSSGYLIFYD
>gnl|CDD|239139 cd02674, Peptidase_C19R, A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome
GLRNLGNTCYMNSILQCLSADQQDAQEFLLFLLDGLHSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYL
SLPIPSGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR
GSTRKLTTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSR
VTKVSESSVVSSSAYILFYE
>gnl|CDD|259861 cd02675, Ephrin_ectodomain, Ectodomain of Ephrins. Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands and the five EphB receptors bind to three transmembrane ephrin-B ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrins contain a highly conserved ectodomain for receptor binding, which is characterized by this domain hierarchy
LPPIYWNSTNPIFDNGDYVIEVNIGDKLDIICPRYESGTESEEYEYYKIYMVSKDGYDSCRLNTRSRLLL
RCDRPYKEKKFTILFQEFSPIPGGLEFQPGKDYYFISTSTGTEEGLDNTSGGLCSSHNMKLAIKVC
>gnl|CDD|239140 cd02677, MIT_SNX15, MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in sorting nexin 15 and related proteins. The molecular function of the MIT domain is unclear
DYLEQAAELIRLALEKEEEGDYEAAFEFYRAGVDLLLKGVQGDSSPERREAVKRKIAEYLKRAEEILRLH
LSRSL
>gnl|CDD|239141 cd02678, MIT_VPS4, MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear
DFLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNPKSKESIRAKCTEYLDRAEKLKEYL
AKKEK
>gnl|CDD|239142 cd02679, MIT_spastin, MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in the AAA protein spastin, a probable ATPase involved in the assembly or function of nuclear protein complexes; spastins might also be involved in microtubule dynamics. The molecular function of the MIT domain is unclear
IRGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAVPVPSAGVGSQWERARRLQQKMKTNLN
MVKTRLQVL
>gnl|CDD|239143 cd02680, MIT_calpain7_2, MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear
LDLERAHFLVTQAFDEDEKGNAEEAIELYTEAVELCINTSNETMDQALQTKLKQLARQALDRAEALKESM
SKASS
>gnl|CDD|239144 cd02681, MIT_calpain7_1, MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear
ALERDAVQFARLAVQRDQEGRYSEAVFYYKEAAQLLIYAEMAGTLNDSHLKTIQEKSNEYLDRAQALHQL
VQGQQG
>gnl|CDD|239145 cd02682, MIT_AAA_Arch, MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in mostly archaebacterial AAA-ATPases. The molecular function of the MIT domain is unclear
MLEEMARKYAINAVKAEKEGNAEDAITNYKKAIEVLSQIVKNYPDSPTRLIYEQMINEYKRRIEVLEKQN
PASSA
>gnl|CDD|239146 cd02683, MIT_1, MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with unknown function, co-occuring with an as yet undescribed domain. The molecular function of the MIT domain is unclear
SLELAAKEVLKRAVELDQEGRFQEALVCYQEGIDLLMQVLKGTKDEAKKKNLRQKISEYMDRAEAIKKRL
DQEKEDG
>gnl|CDD|239147 cd02684, MIT_2, MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with an n-terminal serine/threonine kinase domain. The molecular function of the MIT domain is unclear
ESLEKAIALVVQAVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQRKEALRQKVLQYVSRAEELKALI
ASDTQ
>gnl|CDD|239148 cd02685, MIT_C, MIT_C; domain found C-terminal to MIT (contained within Microtubule Interacting and Trafficking molecules) domains, as well as in some bacterial proteins. The function of this domain is unknown
NATGFSYDRLFGPYLDDGVTEITVEDPYIRNFHQIRNFLRFCELVVKPPCELKYIHLVTGEDEDNGKQQI
EALEEIKQSLASHGVEFTWEFSDTIHDREIRTDNGWIIKIGRGLDYFKPPEGKFSLGNRDQDFRPCKATE
VDIFHTKH
>gnl|CDD|199878 cd02688, E_set, Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the N or C terminus. The E or "early" set domains of sugar utilizing enzymes are associated with different types of catalytic domains at either the N-terminal or C-terminal end. These domains may be related to the immunoglobulin and/or fibronectin type III superfamilies. Members of this family include alpha amylase, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. A subset of these members were recently identified as members of the CBM48 (Carbohydrate Binding Module 48) family. Members of the CBM48 family include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase
GVTFRIFAPGAKSVYLIGSFNGWWQAQALPMTKNGGGVWSATIPLPLGTYEYKYVIDGGKNVLPYFDPYY
VAGDGNSGASIV
>gnl|CDD|349868 cd02690, M28, M28 Zn-peptidases include aminopeptidases and carboxypeptidases. Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases
GYNVIATIKGSDKPDEVILIGAHYDSVPLSPGANDNASGVAVLLELARVLSKLQLKPKRSIRFAFWDAEE
LGLLGSKYYAEQLLSSLKNIRAALNLDMIGGAGPDLYLQTAPGNDALVEKLLRALAHELENVVYTVVYKE
DGGTGGSDHRPFLARGIPAASLIQSESYNFPYYHTTQDTLENIDKDTLKRAGDILASFLYRL
>gnl|CDD|100036 cd02691, PurM-like2, AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain
MGEFGVGSRGEGDFYVHEKLAELIGKTGEVSIVAQDDDAGVDAADVEYIVVAIDGIHSRLSDFPFLAGFH
ATRAALRDVMVMGARPVALLSDIHLADDGDVGKLFDFTAGVTAVSEATGVPLVAGSTLRIGGDMVLGDRL
VGGVGAVGRSKSDPSRRKNAEPGDLILMTEGAGGGTITTTAIYHGMPDVVEETLNVDFIKACEALRDSGL
VSKVHSMTDVTNGGIRGDALEISKTAGVSLVFDEEKVRSLINPKVLKMLEELGIDPLGVSLDSLMIIAPE
EDAVDIIRTLREAGVRADEVGRVEEGRGVPLVVTGEGRELKPAFRESAYTPIKKVVGEYSPGDFEE
>gnl|CDD|119407 cd02696, MurNAc-LAA, N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall
TIVIDPGHGGKDPGAVGNDGLKEKDINLAIALKLAKLLEAAGAKVVLTRDDDTFVSLSERVAIANRAGAD
LFISIHANAAPNSSARGAEVYYYSGSSEESKRLAEAIQKELVKALGLRNRGVKQANLYVLRNTKMPAVLV
ELGFISNPEDAKLLNSPEYQDKIAEAIAEGIL
>gnl|CDD|349869 cd02697, M20_like, M20 Zn-peptidases include exopeptidases. Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc
HFDEEVRFLQKLVRVPTDTPPGNNAPHAERTAALLQGFGFEAERHPVPEAEVRAYGMESITNLIVRRRYG
DGGRTVALNAHGDVVPPGDGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVEL
HFTYDEEFGGELGPGWLLRQGLTKPDLLIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQG
AVAILNALYALNAQYRQVSSQVEGITHPYLNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIR
RVIADAAASMPGISVDIRRLLLANSMRPLPGNAPLVEAIQTHGEAVFGEPVPAMGTPLYTDVRLYAEAGI
PGVIYGAGPRTVLESHAKRADERLQLEDLRRATKVIARSLRDLL
>gnl|CDD|239149 cd02698, Peptidase_C1A_CathepsinX, Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase activity. It can also act as a carboxydipeptidase, like cathepsin B, but has been shown to preferentially cleave substrates through a monopeptidyl carboxypeptidase pathway. The propeptide region of cathepsin X, the shortest among papain-like peptidases, is covalently attached to the active site cysteine in the inactive form of the enzyme. Little is known about the biological function of cathepsin X. Some studies point to a role in early tumorigenesis. A more recent study indicates that cathepsin X expression is restricted to immune cells suggesting a role in phagocytosis and the regulation of the immune response
LPKSWDWRNVNGVNYVSPTRNQHIPQYCGSCWAHGSTSALADRINIARKGAWPSVYLSVQVVIDCAGGGS
CHGGDPGGVYEYAHKHGIPDETCNPYQAKDGECNPFNRCGTCNPFGECFAIKNYTLYFVSDYGSVSGRDK
MMAEIYARGPISCGIMATEALENYTGGVYKEYVQDPLINHIISVAGWGVDENGVEYWIVRNSWGEPWGER
GWFRIVTSSYKGARYNLAIEEDCAWADPI
>gnl|CDD|341048 cd02699, M4_M36, Peptidase M4 family (includes thermolysin, aureolysin, neutral protease and bacillolysin) and Peptidase M36 family (also known as fungalysin). This family includes the peptidases M4 as well as M36, both belonging to the Gluzincin family. The M4 peptidase family includes numerous zinc-dependent metallopeptidases that hydrolyze peptide bonds, such as thermolysin (EC 3.4.24.27), pseudolysin (the extracellullar elastase of Pseudomonas aeruginosa), aureolysin (the extracellular metalloproteinase from Staphylococcus aureus), neutral protease from Bacillus cereus, as well as bacillolysin (EC 3.4.24.28). The M36 family also known as fungalysin (elastinolytic metalloproteinase) family, includes endopeptidases from pathogenic fungi. Both M4 and M36 families have similar folds and contain the Zn-binding site and the active site HEXXH motif. The eukaryotic M36 and bacterial M4 families of metalloproteases also share a conserved domain in their propeptides called FTP (fungalysin/thermolysin propeptide)
IFAYDAKIRTTLPGVLWNEQYILAQDADNPFESNYDAAAVDAHYYAGLTYDYYKNTFGRESIWAPRIADG
KKYDEYNSPLRSYVHYGSGYNNAFWNGSKKAMVYGDGDGTTFTEFLSGGIDIVAHELTHAVTDGTHNQSN
LIYQNESGALNEAFSDIFATFVEFYFNELRNPDWEMGEDIYTPGKIGDALRSMSDPTKYGDPDHYSKRYT
GYRDNGGVHTNGGIINKAAYEVFQGITHYGVADLIRIVGRLAGVAGIGKDKLGKIYYRALTQYPTVDSNF
SQARDAIVQADTDLYGDSSAEVAAVKQAFRARG
>gnl|CDD|259848 cd02733, RNAP_II_RPB1_N, Largest subunit (Rpb1) of eukaryotic RNA polymerase II (RNAP II), N-terminal domain. The two largest subunits of RNA polymerase II (RNAP II), Rpb1 and Rpb2, form the active site, DNA entry channel and RNA exit channel. RNAP II is a large multi-subunit complex responsible for the synthesis of mRNA in eukaryotes. RNAP II consists of a 10-subunit core enzyme and a peripheral heterodimer of two subunits. Structure studies suggest that RNAP complexes from different organisms share a crab-claw-shape structure. In yeast, Rpb1 and Rpb2, each makes up one clamp, one jaw, and part of the cleft. Rpb1_N contains part of the active site, forms the head and core of the one clamp, and makes up the pore and funnel regions of RNAP II
KRVQFGILSPDEIRAMSVAEIEHPETYENGGGPKLGGLNDPRMGTIDRNSRCQTCGGDMKECPGHFGHIE
LAKPVFHIGFLTKILKILRCVCKRELSAERVLEIFKRISDEDCRILGFDPKFSRPDWMILTVLPVPPPAV
RPSVVMDGSARSEDDLTHKLADIIKANNQLKRQEQNGAPAHIIEEDEQLLQFHVATYMDNEIPGLPQATQ
KSGRPLKSIRQRLKGKEGRIRGNLMGKRVDFSARTVITPDPNLELDQVGVPRSIAMNLTFPEIVTPFNID
RLQELVRNGPNEYPGAKYIIRDDGERIDLRYLKKASDLHLQYGYIVERHLQDGDVVLFNRQPSLHKMSMM
GHRVKVLPYSTFRLNLSVTTPYNADFDGDEMNLHVPQSLETRAELKELMMVPRQIVSPQSNKPVMGIVQD
TLLGVRKLTKRDTFLEKDQVMNLLMWLPDWDGKIPQPAILKPKPLWTGKQIFSLIIPKINNLIRSSSHHD
GDKKWISPGDTKVIIENGELLSGILCKKTVGASSGGLIHVIWLEYGPEAARDFIGNIQRVVNNWLLHNGF
SIGIGDTIADKETMKKIQETIKKAKRDVIKLIEKAQNGELEPQPGKTLRESFENKVNRILNKARDKAGKS
AQKSLSEDNNFKAMVTAGSKGSFINISQIIACVGQQNVEGKRIPFGFRRRTLPHFIKDDYGPESRGFVEN
SYLRGLTPQEFFFHAMGGREGLIDTAVKTAETGYIQRRLVKAMEDVMVKYD
>gnl|CDD|132722 cd02735, RNAP_I_Rpa1_C, Largest subunit (Rpa1) of Eukaryotic RNA polymerase I (RNAP I), C-terminal domain. RNA polymerase I (RNAP I) is a multi-subunit protein complex responsible for the synthesis of rRNA precursor. It consists of at least 14 different subunits, and the largest one is homologous to subunit Rpb1 of yeast RNAP II and subunit beta' of bacterial RNAP. Rpa1 is also known as Rpa190 in yeast. Structure studies suggest that different RNAP complexes share a similar crab-claw-shape structure. The C-terminal domain of Rpb1, the largest subunit of RNAP II, makes up part of the foot and jaw structures of RNAP II. The similarity between this domain and the C-terminal domain of Rpb1, its counterpart in RNAP II, suggests a similar functional and structural role
KYMRSLVEPGEAVGLLAAQSIGEPSTQMTLNTFHFAGRGEMNVTLGIPRLREILMTASKNIKTPSMTLPL
KNGKSAERAETLKKRLSRVTLSDVVEKVEVTEILKTIERVFKKLLGKWCEVTIKLPLSSPKLLLLSIVEK
LARKAVIREIPGITRCFVVEEDKGGKTKYLVITEGVNLAALWKFSDILDVNRIYTNDIHAMLNTYGIEAA
RRAIVKEISNVFKVYGIAVDPRHLSLIADYMTFEGGYRPFNRIGMESSTSPLQKMSFETTLAFLKKATLN
GDIDNLSSPSSRLVVGKPVNGGTGLFDLL
>gnl|CDD|132723 cd02736, RNAP_III_Rpc1_C, Largest subunit (Rpc1) of Eukaryotic RNA polymerase III (RNAP III), C-terminal domain. Eukaryotic RNA polymerase III (RNAP III) is a large multi-subunit complex responsible for the synthesis of tRNAs, 5SrRNA, Alu-RNA, U6 snRNA, among others. Rpc1 is also known as C160 in yeast. Structure studies suggest that different RNA polymerase complexes share a similar crab-claw-shape structure. The C-terminal domain of Rpb1, the largest subunit of RNAP II, makes up part of the foot and jaw structures of RNAP II. The similarity between this domain and the C-terminal domain of Rpb1, its counterpart in RNAP II, suggests a similar functional and structural role
KYMRAKVEPGTAVGAIAAQSIGEPGTQMTLKTFHFAGVASMNITLGVPRIKEIINASKNISTPIITAKLE
NDRDEKSARIVKGRIEKTYLGEVASYIEEVYSPDDCYILIKLDKKIIEKLQLSKSNLYFLLQSLKRKLPD
VVVSGIPEVKRAVINKDKKKGKYKLLVEGYGLRAVMNTPGVIGTRTTSNHIMEVEKVLGIEAARSTIINE
IQYTMKSHGMSIDPRHIMLLADLMTFKGEVLGITRFGIAKMKESVLMLASFEKTTDHLFNAALHGRKDSI
EGVSECIIMGKPMPIGTGLF
>gnl|CDD|132724 cd02737, RNAP_IV_NRPD1_C, Largest subunit (NRPD1) of Higher plant RNA polymerase IV, C-terminal domain. Higher plants have five multi-subunit nuclear RNA polymerases: RNAP I, RNAP II and RNAP III, which are essential for viability; plus the two isoforms of the non-essential polymerase RNAP IV (IVa and IVb), which specialize in small RNA-mediated gene silencing pathways. RNAP IVa and/or RNAP IVb might be involved in RNA-directed DNA methylation of endogenous repetitive elements, silencing of transgenes, regulation of flowering-time genes, inducible regulation of adjacent gene pairs, and spreading of mobile silencing signals. NRPD1a is the largest subunit of RNAP IVa, whereas NRPD1b is the largest subunit of RNAP IVb. The full subunit compositions of RNAP IVa and RNAP IVb are not known, nor are their templates or enzymatic products. However, it has been shown that RNAP IVa and, to a lesser extent, RNAP IVb are crucial for several RNA-mediated gene silencing phenomena
GEPVGSLAATAISEPAYKALLDPPQSLESSPLELLKEVLECRSKSKSKENDRRVILSLHLCKCDHGFEYE
RAALEVKNHLERVTLEDLATTSMIKYSPQATEAIVGEIGDQLNTKKKGKKKAIFSTSLKITKFSPWVCHF
HLDKECQKLSDGPCLTFSVSKEVSKSSEELLDVLRDRIIPFLLETVIKGDERIKSVNILWEDSPSTSWVK
SVGKSSRGELVLEVTVEESCKKTRGNAWNVVMDACIPVMDLIDWERSMPYSIQQIKSVLGIDAAFEQFVQ
RLESAVSMTGKSVLREHLLLVADSMTYSGEFVGLNAKGYKAQRRSLKISAPFTEACFSSPIKCFLKAAKK
GASDSLSGVLDACAWGKEAPVGTGSKFEILW
>gnl|CDD|119331 cd02742, GH20_hexosaminidase, Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself
IRGIMLDVSRHFLSVESIKRTIDVLARYKINTFHWHLTDDQAWRIESKKFPELAEKGGQINPRSPGGFYT
YAQLKDIIEYAAARGIEVIPEIDMPGHSTAFVKSFPKLLTECYAGLKLRDVFDPLDPTLPKGYDFLDDLF
GEIAELFPDRYLHIGGDEAHFKQDRKHLMSQFIQRVLDIVKKKGKKVIVWQDGFDKKMKLKEDVIVQYWD
YDGDKYNVELPEAAAKGFPVILSNGYYLDIFIDGALDARKVYKNDPLAVPTPQQKDLVLGVIACLWGETV
KDTKTLQYRFWPRALAVAERSWS
>gnl|CDD|394871 cd02749, Macro_SF, macrodomain superfamily. Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response
DAIVNPANNDLYLGGGVAKAISKKAGGDLQEECEERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVASS
KKKTYEPLKKCVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA
>gnl|CDD|239151 cd02750, MopB_Nitrate-R-NarG-like, Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins
DKVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATDYPETPPDLPDYNPRGCQRGASFSWYLYSPDRVKYP
LKRVGARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAAGSRFASLIGGVSLS
FYDWYGDLPPGSPQTWGEQTDVPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVSPDYS
PSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYTDLPFLVYTPAWQEAITGVPRETVIRLA
REFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVGQPRVLFVWRGNLFGSSGK
GHEYFEDAPEGKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSD
WEIFKALAKKVPWRTLTGRQQFYLDHDWFLELGETLPTYKP
>gnl|CDD|239152 cd02751, MopB_DMSOR-like, The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins
PTACHWGPFKAHVKDGVIVRVEPDDTDQPRPCPRGRSVRDRVYSPDRIKYPMKRVGWLGNGPGSRELRGE
GEFVRISWDEALDLVASELKRIREKYGNEAIFGGSYGWASAGRLHHAQSLLHRFLNLIGGYLGSYGTYST
GAAQVILPHVVGSDEVYEQGTSWDDIAEHSDLVVLFGANPLKTRQGGGGGPDHGSYYYLKQAKDAGVRFI
CIDPRYTDTAAVLAAEWIPIRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLLGESDGVPK
TPEWAAEITGVPAETIRALAREIASKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGY
GYSNGGGPPRGGAGGPGLPQGKNPVKDSIPVARIADALLNPGKEFTANGKLKTYPDIKMIYWAGGNPLHH
HQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTGNYSNRYLIAMKQAVEPLGEA
RSDYEIFAELAKRLGVEEEFTEGRDEMEWLEHLYEETRAKAAGPGPELPSFEEFWEKGIVRVPAAPKPFV
AFADFREDPEANPLGTPSGKIEIYSETLADFGYDDCPGHPTWIEPWEGL
>gnl|CDD|239153 cd02752, MopB_Formate-Dh-Na-like, Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins
RTICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGSGKWEE
ISWDEALDEIARKMKDIRDASFVEKNAAGVVVNRPDSIAFLGSAKLSNEECYLIRKFARALGTNNLDHQA
RIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKNGAKLIVVDPRFT
RTAAKADLYVPIRSGTDIAFLGGMINYIIRYTPEEVEDICGVPKEDFLKVAEMFAATGRPDKPGTILYAM
GWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHSNVQGATDLGLLSHNLPGYLGGQNPNSSFPNA
NKVRRALDKLDWLVVIDPFPTETAAFWKNPGMDPKSIQTEVFLLPAACQYEKEGSITNSGRWLQWRYKVV
EPPGEAKSDGDILVELAKRLGFLYEKEGGAFPEPITKWNYGYGDEPTPEEIAREINGGALTDGYTGQSPE
RLKAHGQNVHTFDTLRDDGSTACGCWIYSGSYTEEGRMARRDTSDPDGLGLYPGWPWPWPVNRRILYNRA
SVDMEGKPGYPERPLVEWDGLGWWWKGDVPDGPWPAAKEHGCGPFIMAPEGQARLFVWNFDGPFPEHYEP
LESPRPDLHSKVAKNPTYK
>gnl|CDD|239154 cd02753, MopB_Formate-Dh-H, Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins
KTVCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEAS
WDEALSLVASRLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDHCARLCHSPTVAGLAE
TLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRP
GTDVALLNAMAHVIIEEGLYDEEFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKS
AAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQGACDMGALPNVLPGYVKALYI
MGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVE
PPGEARPDWEIIQELANRLGYPGFYSHPEEIFDEIARLTPQYAGISYERLERPGGLQWPCPDEDHPGTPI
LHTERFATPDGKARFMPVEYRP
>gnl|CDD|239155 cd02754, MopB_Nitrate-R-NapA-like, Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins
KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGGELVPV
SWDEALDLIAERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYK
RSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKKANPGAKIIVVDPRRTRTADIADLHLP
IRPGTDLALLNGLLHVLIEEGLIDRDFIDAHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGE
ARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGGLANLLPGHRSV
NNPEHRAEVAKFWGVPEGTIPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFV
VVQDAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARPDWWILADVARRLGFGEL
FPYTSPEEVFEEYRRLSRGRGADLSGLSYERLRDGGVQWPCPDGPPEGTRRLFEDGRFPTPDGRARFVAV
PYRPP
>gnl|CDD|239156 cd02755, MopB_Thiosulfate-R-like, The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins
VPSICEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGERGEGK
FREASWDEALQYIASKLKEIKEQHGPESVLFGGHGGCYSPFFKHFAAAFGSPNIFSHESTCLASKNLAWK
LVIDSFGGEVNPDFENARYIILFGRNLAEAIIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIK
PGTDLAFVLALIHVLISENLYDAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAA
PHAVVDPGWRGTFYSNSFQTRRAIAIINALLGNIDKRGGLYYAGSAKPYPIKALFIYRTNPFHSMPDRAR
LIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGGPAPAVATRQRAIEPLYDTRPGWDI
LKELARRLGLFGTPSGKIELYSPILAKAGYDPLP
>gnl|CDD|239157 cd02756, MopB_Arsenite-Ox, Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins
DRVPLPPVNAERYNVTCHFCIVGCGYHVYVWPVGEEGGPSPGQNAIGYDLVDQVPPLNLQWYPKTMHYVV
VTQDGREVYIVIVPDKECPVNSGNYSTRGGTNAERIWSPDNRVGETRLTTPLVRRGGQLQPTTWDDAIDL
VARVIKGILDKDGNDDAVFASRFDHGGGGGGFENNWGVGKFFFMALQTPFVRIHNRPAYNSEVHATREMG
VGELNNSYEDARLADTIVLWGNNPYETQTVYFLNHWLPNLRGATVSEKQQWFPPGEPVPPGRIIVVDPRR
TETVHAAEAAAGKDRVLHLQVNPGTDTALANAIARYIYESLDEVLAEAEQITGVPRAQIEKAADWIAKPK
EGGYRKRVMFEYEKGIIWGNDNYRPIYSLVNLAIITGNIGRPGTGCVRQGGHQEGYVRPPPPPPPWYPQY
QYAPYIDQLLISGKGKVLWVIGCDPYKTTPNAQRLRETINHRSKLVTDAVEAALYAGTYDREAMVCLIGD
AIQPGGLFIVVQDIYPTKLAEDAHVILPAAANGEMNETSMNGHERRLRLYEKFMDPPGEAMPDWWIAAMI
ANRIYELYQEEGKGGSAQYQFFGFIWKTEEDNFMDGSQEFADGGEFSEDYYVLGQERYEGVTYNRLKAVG
VNGIQLPVTTDTVTKILVTNVLRTEGVFDTEDGKAYVIDLAPWPGL
>gnl|CDD|239158 cd02757, MopB_Arsenate-R, This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
WVPSTCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNPRKGR
DVDPKFVPISWDEALDTIADKIRALRKENEPHKIMLHRGRYGHNNSILYGRFTKMIGSPNNISHSSVCAE
SEKFGRYYTEGGWDYNSYDYANAKYILFFGADPLESNRQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKA
DEWLPIKPGEDGALALAIAHVILTEGLWDKDFVGDFVDGKNYFKAGETVDEESFKEKSTEGLVKWWNLEL
KDYTPEWAAKISGIPAETIERVAREFATAAPAAAAFTWRGATMQNRGSYNSMACHALNGLVGSIDSKGGL
CPNMGVPKIKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMS
QENNLHPWLSIRQPVVKSLGEVREETEILIELAKKLDPKGSDGMKRYAPGQFKDPETGKNNRWEFENVFP
TETGKFEFYSETLKKYLQNHADKKKVSWDEVME
>gnl|CDD|239159 cd02758, MopB_Tetrathionate-Ra, The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins
YSSCLGCWTQCGIRVRVDKETGKVLRIAGNPYHPLNTAPSLPYNTPLKESLYLSLVGENGLKARATACAR
GNAGLQYLYDPYRVLQPLKRVGPRGSGKWKPISWEQLIEEVVEGGDLFGEGHVEGLKAIRDLDTPIDPDH
PDLGPKANQLLYTFGRDEGRTPFIKRFANQAFGTVNFGGHGSYCGLSYRAGNGALMNDLDGYPHVKPDFD
NAEFALFIGTSPAQAGNPFKRQARRLAEARTEGNFKYVVVDPVLPNTTSAAGENIRWVPIKPGGDGALAM
AMIRWIIENERYNAEYLSIPSKEAAKAAGEPSWTNATHLVITVRVKSALQLLKEEAFSYSLEEYAEICGV
PEAKIIELAKEFTSHGRAAAVVHHGGTMHSNGFYNAYAIRMLNALIGNLNWKGGLLMSGGGFADNSAGPR
YDFKKFFGEVKPWGVPIDRSKKAYEKTSEYKRKVAAGENPYPAKRPWYPLTPELYTEVIASAAEGYPYKL
KALILWMANPVYGAPGLVKQVEEKLKDPKKLPLFIAIDAFINETSAYADYIVPDTTYYESWGFSTPWGGV
PTKASTARWPVIAPLTEKTANGHPVSMESFLIDLAKALGLPGFGPNAIKDGQGNKFPLNRAEDYYLRVAA
NIAYDGKAPVPDASEEELKLTGVNRPIPALKRTLKPEEWRKVAYILARGGRFAPYEESYDGDNLRNRWGK
TLQIWNEKLAKSRNSVTGEYFSGCPTYYPPRFADG
>gnl|CDD|239160 cd02759, MopB_Acetylene-hydratase, The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins
KGTCPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVGERGENKW
ERISWDEALDEIAEKLAEIKAEYGPESIATAVGTGRGTMWQDSLFWIRFVRLFGSPNLFLSGESCYWPRD
MAHALTTGFGLGYDEPDWENPECIVLWGKNPLNSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAARADLW
LPIRPGTDAALALGMLNVIINEGLYDKDFVENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLY
ATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNLLIPYPVKMLIVFGTNPLASYADTAPV
LEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAENFVQLRQKAVEPYGEAKSDYEIVL
ELGKRLGPEEAEYYKYEKGLLRPDGQPGFNTPTGKVELYSTMLEELGYDPLPYYREP
>gnl|CDD|239161 cd02760, MopB_Phenylacetyl-CoA-OR, The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins
PTYCYNCVAGPDFMAVKVVDGVATEIEPNFAAEDIHPARGRVCVKAYGLVQKTYNPNRVLQPMKRTNPKK
GRNEDPGFVPISWDEALDLVAAKLRRVREKGLLDEKGLPRLAATFGHGGTPAMYMGTFPAFLAAWGPIDF
SFGSGQGVKCVHSEHLYGEFWHRAFTVAADTPLANYVISFGSNVEASGGPCAVTRHADARVRGYKRVQVE
PHLSVTGACSAEWVPIRPKTDPAFMFAMIHVMVHEQGLGKLDVPFLRDRTSSPYLVGPDGLYLRDAATGK
PLVWDERSGRAVPFDTRGAVPAVAGDFAVDGAVSVDADDETAIHQGVEGTTAFTMLVEHMRKYTPEWAES
ICDVPAATIRRIAREFLENASIGSTIEVDGVTLPYRPVAVTLGKSVNNGWGAFECCWARTLLATLVGALE
VPGGTLGTTVRLNRPHDDRLASVKPGEDGFMAQGFNPTDKEHWVVKPTGRNAHRTLVPIVGNSAWSQALG
PTQLAWMFLREVPLDWKFELPTLPDVWFNYRTNPAISFWDTATLVDNIAKFPFTVSFAYTEDETNWMADV
LLPEATDLESLQMIKVGGTKFVEQFWEHRGVVLRQPAVEPQGEARDFTWISTELAKRTGLLADYNAALNR
GAGGAPLKGEGYDQSLDESQEHDVEYIWDAICRASSASLSKGGEVHGLEWFKEHGFYTVPMSKEEWYLRP
TMEVQGLRYEMPYQERLLRIGRELGNRLHEFLMHWWDEQLSEYRALPHWHDVPGRWLDQA
>gnl|CDD|239162 cd02761, MopB_FmdB-FwdB, The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins
DVVCPFCGLLCDDIEVEVEDNKITKVRNACRIGAAKFARYERRITTPRIDGKPVSLEEAIEKAAEILKEA
KRPLFYGLGTTVCEAQRAGIELAEKLGAIIDHAASVCHGPNLLALQDSGWPTTTLGEVKNRADVIVYWGT
NPMHAHPRHMSRYSVFPRGFFREGGREDRTLIVVDPRKSDTAKLADIHLQIDPGSDYELLAALRALLRGA
GLVPDEVAGIPAETILELAERLKNAKFGVIFWGLGLLPSRGAHRNIEAAIRLVKALNEYTKFALLPLRGH
YNVRGFNQVLTWLTGYPFRVDFSRGYPRYNPGEFTAVDLLAEGEADALLIIASDPPAHFPQSAVKHLAEI
PVIVIDPPPTPTTRVADVVIPVAIPGIEAGGTAYRMDGVVVLPLKAVETERLPDEEILKQLLEKV
>gnl|CDD|239163 cd02762, MopB_1, The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
KRACILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGSFEEID
WDEAFDEIAERLRAIRARHGGDAVGVYGGNPQAHTHAGGAYSPALLKALGTSNYFSAATADQKPGHFWSG
LMFGHPGLHPVPDIDRTDYLLILGANPLQSNGSLRTAPDRVLRLKAAKDRGGSLVVIDPRRTETAKLADE
HLFVRPGTDAWLLAAMLAVLLAEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLARE
FAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAMFTTPALDLVGQTSGRTIGRGEWRSR
VSGLPEIAGELPVNVLAEEILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTR
HADYILPPASQLEKPHATFFNLEFPRNAFRYRRPLFPPPPGTLPEWEILARLVEALDAVLRAGFYGERAG
GTLLLAALLERPSGVDLGPLTPRLWQRLRTPDGRIHLAPPELLDELRRL
>gnl|CDD|239164 cd02763, MopB_2, The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
TTTCYMCACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGPRGSGQF
EEIEWEEAFSIATKRLKAARATDPKKFAFFTGRDQMQALTGWFAGQFGTPNYAAHGGFCSVNMAAGGLYS
IGGSFWEFGGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPG
TDGAFILALAHELLKAGLIDWEFLKRYTNAAELVDYTPEWVEKITGIPADTIRRIAKELGVTARDQPIEL
PIAWTDVWGRKHEKITGRPVSFHAMRGIAAHSNGFQTIRALFVLMMLLGTIDRPGGFRHKPPYPRHIPPL
PKPPKIPSADKPFTPLYGPPLGWPASPDDLLVDEDGNPLRIDKAYSWEYPLAAHGCMQNVITNAWRGDPY
PIDTLMIYMANMAWNSSMNTPEVREMLTDKDASGNYKIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDA
MSLLDRPISEADGPVDAIRVPIVEPKGDVKPFQEVLIELGTRLGLPGFTNEDGTRKYRDYPDFIVNFETT
PGVGFLAGWRGKDGDKAFVGEPNPNQLEQYAKNNGFFHYPLPEHMRYYRNVNKDYLEWAVRVGFVKFTDP
IIMQLYSEVLQKFRLAGQGLWEGEQPPEALRERVETYFDPLPFWYPPFE
>gnl|CDD|239165 cd02764, MopB_PHLH, The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs
RRGFLKLMGASLAMASAAACRYPVEKIVPYVIWPENIVPGETVYYATSLVPAGEGQGVLVKTVDGRPIKI
EGNPDHPASLGGTSARAQASVLSLYDPDRAQGPLRRGIDGAYVASDWADFDAKVAEQLKAVKDGGKLAVL
SGNVNSPTTEALIGDFLKKYPGAKHVVYDPLSAEDVNEAWQASFGKDVVPGYDFDKAEVIVSIDADFLGS
WISAIRHRHDFAAKRRLGAEEPMSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLIKKGAGSS
LPDFFRALNLAFKPAKVAELTVDLDKALAALAKALAAAGKSLVVAGSELSQTAGADTQVAVNALNSLLGN
DGKTVDHARPIKGGELGNQQDLKALASRINAGKVSALLVYDVNPVYDLPQGLGFAKALEKVPLSVSFGDR
LDETAMLCDWVAPMSHGLESWGDAETPDGTYSICQPVIAPLFDTRSAQESLLLALGGSLGGYEKLRRYTS
WIKAAIGDRSWEQALRDGVAADVNVSAGSTSFRR
>gnl|CDD|239166 cd02765, MopB_4, The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
YTACPPNCGGRCPLKCHVRDGKIVKVEPNEWPDKTYKRGCTRGLSHLQRVYSPDRLKYPMKRVGERGEGK
FERITWDEALDTIADKLTEAKREYGGKSILWMSSSGDGAILSYLRLALLGGGLQDALTYGIDTGVGQGFN
RVTGGGFMPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVP
IRPGTDPALALGMINYILEHNWYDEAFLKSNTSAPFLVREDNGTLLRQADVTATPAEDGYVVWDTNSDSP
EPVAATNINPALEGEYTINGVKVHTVLTALREQAASYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWG
FGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGVGQIKFMYFMGSNFLGNQPDRDRWLKVMKNLDFIVVV
DIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHPHVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDYFP
KTPEDYVRAFMNSDDPALDGITWEALKEEGIIMRLATPEDPYVAYLDQKFGTPSGKLEFYNEAAPELEEA
LPLPEEP
>gnl|CDD|239167 cd02766, MopB_3, The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
RSVCPLDCPDTCSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGRKGGQW
ERISWDEALDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFFHALGASELRGTICSGAGIEAQ
KYDFGASLGNDPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIR
PGTDGALALGVAKVLFREGLYDRDFLARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAK
PPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGAFYSNSGPPVKALWVYNSNPVAQAPDSNKVR
KGLAREDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYYLQYNEPAIPPPGEARSNTEIFRE
LAKRLGFGEPPFEESDEEWLDQALDGTGLPLEGIDLERLLGPRKAGFPLVAWEDRGFPTPSGKFEFYSER
AAKRGLPPLPE
>gnl|CDD|239168 cd02767, MopB_ydeP, The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
GFDCPGCAWGDPGQKLHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMR
YDAGSDHYRPISWDEAFAEIAARLRALDPDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEP
SSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFA
NPQNPESMLTGGTKIADEYFQVRIGGDIALLNGMAKHLIERDDEPGNVLDHDFIAEHTSGFEEYVAALRA
LSWDEIERASGLSREEIEAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMP
IRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDTVEAIEAALEGKVKAFISLGGNFAEAMP
DPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQAVTVEDSMSMTHTSRGRL
KPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIYEGFADFNQRGDQPGGFHLPNGA
RERKFNTPSGKAQF
>gnl|CDD|239169 cd02768, MopB_NADH-Q-OR-NuoG2, MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family
ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIKKGGKLVPVS
WEEALKTVAEGLKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRLRQSDLPADNRLRGNYLFN
TSIAEIEEADAVLLIGSNLRKEAPLLNARLRKAVKKKGAKIAVIGPKDTDLIADLTYPVSPLGASLATLL
DIAEGKHLKPFAKSLKKAKKPLIILGSSALRKDGAAILKALANLAAKLGTGAGLWNGLNVLNSVGARLGG
AGLDAGLALLEPGKAKLLLLGEDELDRSNPPAAVALAAADAFVVYQGHHGDTGAQADVILPAAAFTEKSG
TYVNTEGRVQRFKKAVSPPGDAREDWKILRALSNLL
>gnl|CDD|239170 cd02769, MopB_DMSOR-BSOR-TMAOR, The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins
PTASHWGAFRARVKDGRIVGVRPFEEDPDPSPLLDGVPDAVYSPTRIKYPMVRRGWLEKGPGSDRSLRGK
EEFVRVSWDEALDLVAAELKRVRKTYGNEAIFGGSYGWSSAGRFHHAQSLLHRFLNLAGGYVGSVGDYST
GAAQVILPHVVGSMEVYTEQQTSWPVIAEHTELVVAFGADPLKNAQIAWGGIPDHQAYSYLKALKDRGIR
FISISPLRDDTAAELGAEWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLLGESDGV
PKTPEWAAAICGIPAETIRELARRFASKRTMIMAGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGGFGF
GYHYSNGGGPPRGAAPPPALPQGRNPVSSFIPVARIADMLLNPGKPFDYNGKKLTYPDIKLVYWAGGNPF
HHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLERNDIGGSGDNRYIVAMKQVVEPVGEA
RDDYDIFADLAERLGVEEQFTEGRDEMEWLRHLYEESRAQAAARGVEMPSFDEFWAQGYVELPIPEADFV
RLADFREDPEANPLGTPSGRIEIFSETIAGFGYDDCPGHPTWLEPAEWL
>gnl|CDD|239171 cd02770, MopB_DmsA-EC, This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
WSACTVNCGGRCPLKAHVKDGVITRIETDDTGDDDPGFHQIRACLRGRSQRKRVYNPDRLKYPMKRVGKR
GEGKFVRISWDEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGAIARLLNLTGGYLNYYGTYS
WAQITTATPYTYGAAASGSSLDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLQAKKAGAKFIVIDPRYTD
TAVTLADEWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYCVGFDAEHLPEGAPPNESYKDYVLGTGY
DGTPKTPEWASEITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGG
NTGARPGGSAYNGAGLPAGKNPVKTSIPCFMWTDAIERGEEMTADDGGVKGADKLKSNIKMIWNYAGNTL
INQHSDDNNTTRALLDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTSNAGMMEYLIYSQK
AIEPLYECKSDYEICAELAKRLGVEDQFTEGKTEQEWLEELYGQTRAKEPGLPTYEEFREKGIYRVPRAL
PFVAFEDFREDPENNPLKTPSGKIEIYSKALADMAKTLPEGDEIPAIPKYVPAWEGP
>gnl|CDD|239172 cd02771, MopB_NDH-1_NuoG2-N7, MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins
PSICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGTLVPVS
WNEALDVAAARLKEAKDKVGGIGSPRASNESNYALQKLVGAVLGTNNVDHRARRLIAEILRNGPIYIPSL
RDIESADAVLVLGEDLTQTAPRIALALRQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNALA
TRLDDIAAESIRASPGGQARLGAALARAVDASAAGVSGLAPKEKAARIAARLTGAKKPLIVSGTLSGSLE
LIKAAANLAKALKRRGENAGLTLAVEEGNSPGLLLLGGHVTEPGLDLDGALAALEDGSADALIVLGNDLY
RSAPERRVEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKSGTFVNYEGRAQRFFKAYDDPAGDAR
SDWRWLHALAAKLGGKLVPSDAAILDEIIALVPGKAPVGGHLYGGDPGVTLF
>gnl|CDD|239173 cd02772, MopB_NDH-1_NuoG2, MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins
KSVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEDRLTKPMIKKDGQWQEVD
WETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLARGLGSDNIDHRLRQSDFRDDAKASGA
PWLGMPIAEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINPADDDFLFPLSGKAIVAPSALA
NALAQVAKALAEEKGLAVPDEDAKVEASEEARKIAASLVSAERAAVFLGNLAQNHPQAATLRALAQEIAK
LTGATLGVLGEGANSVGAYLAGALPHGGLNAAAMLEQPRKAYLLLNVEPELDCANPAQALAALNQAEFVV
ALSAFASAALLDYADVLLPIAPFTETSGTFVNLEGRVQSFKGVVKPLGEARPAWKVLRVLGNLL
>gnl|CDD|239174 cd02773, MopB_Res-Cmplx1_Nad11, MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins
ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRKNGKLKPATW
EEALAAIAKALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPADLRSNYLFNTTI
AGIEEADAVLLVGTNPRFEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHP
FSKALKDAKKPMIIVGSGALARKDGAAILAAVAKLAKKNGVVREGWNGFNVLHRAASRVGALDLGFVPGA
GAIRKSGPPKVLYLLGADEIDITPIPKDAFVVYQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQ
TRKAVSPPGDAREDWKILRALSEVL
>gnl|CDD|239175 cd02774, MopB_Res-Cmplx1_Nad11-M, MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex I, the second domain of the Nad11/75-kDa subunit of some protists. NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH-quinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. The Nad11 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins
ESIDVLDSLGSNIRVDIKGNEILRILPKINDELNEEWISDKIRFSYDSLKYQRIKTPLLKLSNNSFLEIG
WKTAFKFLNKFILLKKFSKLNFIIGSKIDLETLFYYKKLLNKLGSLNTNSNNFLENNNYFNLDLENYLFN
NSLKNLDKSDLCLLIGSNLRVESPILNIRLRNRYNKGNKKIFVIGNKFDTTYPSKHIGLSLNTLLKILEG
KHLFCKQLKKSKKPLIIIGSSFSLRKNYSFIISKLKNFSSNNENNFNFLNIISNSLYYLGIKKFNSNNKK
NLSNLYYIKETNFQKFNKNNFVIYQGHHFLNLANNSNLILPSKTFFEKEALYLNLEGILQKTKKILSFKE
NIKSDDNIIFSLILFL
>gnl|CDD|239176 cd02775, MopB_CT, Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs
LRDHFHSGTRTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLP
HGWGHRGGRGGNANVLTPDALDPPSGGPAYK
>gnl|CDD|239177 cd02776, MopB_CT_Nitrate-R-NarG-like, Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
PLNYLTPHGKWSIHSTYRDNLLMLRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRI
PRGTVFMYHAQERHVNVPGSKLTGKRGGIHNSVTRVRIKPTHLVGGYGQLSYGFNYYGPTGVNRDTRVVV
R
>gnl|CDD|239178 cd02777, MopB_CT_DMSOR-like, The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
YPLQLISPHPKRRLHSQLDNVPWLREAYKVKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVT
DRIMPGVVALPEGAWYDPDDNGGLDKGGNPNVLTSDIPTSKLAQGNPANTCLVEIEK
>gnl|CDD|239179 cd02778, MopB_CT_Thiosulfate-R-like, The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
EFRLIYGKSPVHTHGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIR
PDTVFMPHGFGHWAPALSRAYGGGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK
>gnl|CDD|239180 cd02779, MopB_CT_Arsenite-Ox, This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin
YKYWVNNGRANIIWQTAYHDQNNSEIAERVPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTN
TVKPGQTFMLMAHPRPGANGLVTPYVDPETIIPYYKGTWANIRKI
>gnl|CDD|239181 cd02780, MopB_CT_Tetrathionate_Arsenate-R, This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins
YPFILVTFKSNLNSHRSANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVR
PGVVAIEHGYGHWAYGAVASTIDGKDLPGDAWRGAGVNINDIGLVDPSRGGWSLVDWVGGAAARYDTPVK
IEK
>gnl|CDD|239182 cd02781, MopB_CT_Acetylene-hydratase, The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
EYPLILTTGARSYYYFHSEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTP
GIRPGVVRAEHGWWYPEREAGEPALGGVWESNANALTSDDWNDPVSGSSPLRSMLCKIYK
>gnl|CDD|239183 cd02782, MopB_CT_1, The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
DYPFLLLIGRRHLRSNNSWLHNDPRLVKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTD
DMMPGVVSLPHGWGHDYPGVSGAGSRPGVNVNDLTDDTQRDPLSGNAAHNGVPVRLARV
>gnl|CDD|239184 cd02783, MopB_CT_2, The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
QYPLTAFTQRPMAMYHSWGSQNAWLRQIHTRNYLYMHPKTAKELGIKDGDWVWVESVNGRVKGQARFTET
VEPGTVWTWNAIGKRPGAWGLKPDAPESVKGFLLNHLINDSLPPPGDAKRISNSDPVTGQAAWFDLRVRI
VKAADSEQQETQPQFT
>gnl|CDD|239185 cd02784, MopB_CT_PHLH, The MopB_CT_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding proteins. This CD is of the PHLH region homologous to the conserved molybdopterin-binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
AGLELVLRPDPALGDGRYANNAWLQELPRPLTKLVWDNAALVSPRTAEALGLLQGDVVRIRRGGRTIELP
VWIQPGHAEGVVLLALGYGRTHAGKVGNGVGHNAYPFRTSDVPDFVAGVEVTKTGRKYPLVTTQTHH
>gnl|CDD|239186 cd02785, MopB_CT_4, The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
KYPLACIQRHSRFRVHSQFSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDG
IQPGVVTAEQGWWSRYFQEGSLQDLTSPFVNPVHEYIYGPNSAFYDTLVEVRKA
>gnl|CDD|239187 cd02786, MopB_CT_3, The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
YPLRLITPPAHNFLNSTFANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDV
PPGVVVAEGGWWREHSPDGRGVNALTSARLTDLGGGSTFHDTRVEV
>gnl|CDD|239188 cd02787, MopB_CT_ydeP, The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQGRIVRGFRV
VEYDIPRGCLAAYYPEGNVLVPLDHRDPQSKTPAYKSVPVRL
>gnl|CDD|239189 cd02788, MopB_CT_NDH-1_NuoG2-N7, MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain, is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain and a C-terminal region (this CD) homologous to the formate dehydrogenase C-terminal molybdopterin_binding (MopB) region
WQLVPYYHLFGSEELSQRSPVIAERAPAPYARLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPA
GVVGLPLGAGFPGAPVAEQTVVKLAA
>gnl|CDD|239190 cd02789, MopB_CT_FmdC-FwdD, The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
MKVILNSGRTIDQGRIIEGGNKLTYEVDACAYCEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGV
PEGMVFIPMGPWANVVVDPYTDSTGSPIFKGVPVYI
>gnl|CDD|239191 cd02790, MopB_CT_Formate-Dh_H, Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
EEYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARV
TDRVPEGVVFMPFHFAEAAANLLTNAALDPVAKIPEFKVCAVRVEK
>gnl|CDD|239192 cd02791, MopB_CT_Nitrate-R-NapA-like, Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
AEYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRV
TDRVRPGEVFVPMHWGDQFGRSGRVNALTLDATDPVSGQPEFKHCAVRIEKV
>gnl|CDD|239193 cd02792, MopB_CT_Formate-Dh-Na-like, Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
EEFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALV
TDRVKPHEVGIPYHWGGMGLVIGDSANTLTPYVGDPNTQTPEYKAFLVNIEK
>gnl|CDD|239194 cd02793, MopB_CT_DMSOR-BSOR-TMAOR, The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
YPLHLLSNQPATRLHSQLDHGSLSRAYKVQGREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTD
GIMPGVVQLPTGAWYDPDDPGEPGPLCKHGNPNVLTLDIGTSSLAQGCSAQTCLVQIEK
>gnl|CDD|239195 cd02794, MopB_CT_DmsA-EC, The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
YPLQLIGWHYKRRTHSTFDNVPWLREAFPQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIM
PGVVALPQGAWYEPDANGIDKGGCINTLTGLRPSPLAKGNPQHTNLVQVEK
>gnl|CDD|271143 cd02795, CBM6-CBM35-CBM36_like, Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily. Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules. This alignment model also contains the C-terminal domains of bacterial insecticidal toxins, where they may be involved in determining insect specificity through carbohydrate binding functionality
RIEAEDATLTGGTAVSTAAGASGGGYVIGFSSGGDSVTFTVTVPKAGTYRLAVRYASPNGNGSRSVSLDG
NGKLVGTITVPSTGGWDTWGTASVSVNLPDAGGHTLKIVGTGDNGGANIDYVVV
>gnl|CDD|239196 cd02796, tRNA_bind_bactPheRS, tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. PheRS aminoacylate phenylalanine transfer RNAs (tRNAphe). PheRSs belong structurally to class II aminoacyl tRNA synthetases (aaRSs) but, as they aminoacylate the 2'OH of the terminal ribose of tRNA they belong functionally to class 1 aaRSs. This domain has general tRNA binding properties and is believed to direct tRNAphe to the active site of the enzyme
VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCGAPNVRAGDKVVVALPGAVLPGGLKIKKRKLRGVE
SEGMLCSAKELGLGEDSDGIIELPEDAPVGTDI
>gnl|CDD|239197 cd02798, tRNA_bind_CsaA, tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export related activities. CsaA has a putative tRNA binding activity. The functional unit of CsaA is a homodimer and this domain acts as a dimerization domain
ISYEDFEKVDLRVGTIVEVEDFPEARKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPP
KQIAGVLSEVLVLGADDEGGEVVLLVPDREVPNGAKV
>gnl|CDD|239198 cd02799, tRNA_bind_EMAP-II_like, tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain
VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMR
GVKSQGMVLCASNADHEKVELLEPPEGAKPGERVT
>gnl|CDD|239199 cd02800, tRNA_bind_EcMetRS_like, tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like proteins. This family includes EcMetRS and Aquifex aeolicus Trbp111 (AaTrbp111). This domain has general tRNA binding properties. MetRS aminoacylates methionine transfer RNAs (tRNAmet). AaTrbp111 is structure-specific molecular chaperone recognizing the L-shape of the tRNA fold. AaTrbp111 plays a role in nuclear trafficking of tRNAs. The functional unit of EcMetRs and AaTrbp111 is a homodimer, this domain acts as the dimerization domain
ITIDDFAKVDLRVGKVLEAERVEGSDKLLKLTVDLGEEERQIVSGIAKFYPPEELVGKKVVVVANLKPRK
LRGVESQGMILAAEDGGKLKLLTPDEEVEPGSRVS
>gnl|CDD|239200 cd02801, DUS_like_FMN, Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present
KLILAPMVGVTDLPFRLLCRRYGADLVYTEMISAKALLRGNRKRLRLLTRNPEERPLIVQLGGSDPETLA
EAAKIVEELGADGIDLNMGCPSPKVTKGGAGAALLKDPELVAEIVRAVREAVPIPVTVKIRLGWDDEEET
LELAKALEDAGASALTVHGRTREQRYSGPADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGV
MIGRGALGNPWLFREIKELLE
>gnl|CDD|239201 cd02803, OYE_like_FMN_family, Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase
FSPIKIGGLTLKNRIVMAPMTENMATEDGTPTDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGI
YDDEQIPGLRKLTEAVHAHGAKIFAQLAHAGRQAQPNLTGGPPPAPSAIPSPGGGEPPREMTKEEIEQII
EDFAAAARRAKEAGFDGVEIHGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFP
VGVRLSADDFVPGGLTLEEAIEIAKALEEAGVDALHVSGGSYESPPPIIPPPYVPEGYFLELAEKIKKAV
KIPVIAVGGIRDPEVAEEILAEGKADLVALGRALLADPDLPNKAREG
>gnl|CDD|239202 cd02808, GltS_FMN, Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor
YLLEIERLEEIQYFVFNRAERYGVYNRAGNSRGRPFGTLRDLLEFGAQLAKHPLEPDEEVDDRVTIGPNA
EKPLKLDSPFNISAMSFGALSKEAKEALAIGAALAGTASNTGEGGELPEEREGGGDIIKQVASGRFGVRP
EYLNKADAIEIKIGQGAKPGEGGHLPGEKVTEEIAKIRGIPPGVDLISPPPHHDIYSIEDLAQLIEDLRE
ATGGKPIGVKLVAGHGEGDIAAGVAAAGADFITIDGAEGGTGAAPLTFIDHVGLPTELGLARAHQALVKN
GLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALGCIQARKCHTNTCPVGVATQDPELRRRLD
VEGKAERVANYLKSLAEELRELAAALGKRSLELLGRSDLLAL
>gnl|CDD|239203 cd02809, alpha_hydroxyacid_oxid_FMN, Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate
ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIA
PTGLQGLAHPDGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEA
AGYKALVLTVDTPVLGRRLTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGA
PATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRD
ELERAMALLGCASLADLDP
>gnl|CDD|239204 cd02810, DHOD_DHPD_FMN, Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue
VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPPEGESYPEQLG
ILNSFGLPNLGLDVWLQDIAKAKKEFPGQPLIASVGGSSKEDYVELARKIERAGAKALELNLSCPNVGGG
RQLGQDPEAVANLLKAVKAAVDIPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLKTVG
PGPKRGTGGLSGAPIRPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGP
DVIRKIKKE
>gnl|CDD|239205 cd02811, IDI-2_FMN, Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway
RKDEHLELCLEENVESGGSTGFDDVRLVHNALPELDLDDIDLSTEFLGKRLSAPLLISAMTGGSEKAKEI
NRNLAEAAEELGIAMGVGSQRAALEDPELAESFTVVREAPPNGPLIANLGAVQLNGYGVEEARRAVEMIE
ADALAIHLNPLQEAVQPEGDRDFRGWLERIEELVKALSVPVIVKEVGFGISRETAKRLADAGVKAIDVAG
AGGTSWARVENYRAKDSDQRLAEYFADWGIPTAASLLEVRSALPDLPLIASGGIRNGLDIAKALALGADL
VGMAGPFLKAALEGEEAVIETIEQIIEELRTAMFLTGAKNLAELKQ
>gnl|CDD|239206 cd02812, PcrB_like, PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been characterized as a (S)-3-O-geranylgeranylglyceryl phosphate synthase (AfGGGPS). AfGGGPS catalyzes the formation of an ether linkage between sn-glycerol-1-phosphate (G1P) and geranylgeranyl diphosphate (GGPP), the committed step in archaeal lipid biosynthesis. Therefore, it has been proposed that PcrB-like proteins are either prenyltransferases or are involved in lipoteichoic acid biosynthesis although the exact function is still unknown
RHVTKLDPDKELVDEEIAKLAEESGTDAIMVGGSDGVSSTLDNVVRLIKRIRRPVPVILFPSNPEAVSPG
ADAYLFPSVLNSGDPYWIIGAQAEAAPEVGKIIPWLELIPEGYLVLNPDSTVARVTGAKTDLKPEDAAAY
ALAAEYLGMPIVYLEYSGAYGPPEVVRAVKKVLGDTPLIVGGGIRSGEQAKEMAEAGADTIVVGNIVEED
PNAALETVE
>gnl|CDD|239207 cd02825, PAZ, PAZ domain, named PAZ after the proteins Piwi Argonaut and Zwille. PAZ is found in two families of proteins that are essential components of RNA-mediated gene-silencing pathways, including RNA interference, the piwi and Dicer families. PAZ functions as a nucleic-acid binding domain, with a strong preference for single-stranded nucleic acids (RNA or DNA) or RNA duplexes with single-stranded 3' overhangs. It has been suggested that the PAZ domain provides a unique mode for the recognition of the two 3'-terminal nucleotides in single-stranded nucleic acids and buries the 3' OH group, and that it might recognize characteristic 3' overhangs in siRNAs within RISC (RNA-induced silencing) and other complexes. This parent model also contains structures of an archaeal PAZ domain
ADPVIETMCKFPKDREIDTPLLDSPREEFTKELKGLKVEDTHNPLNRVYRPDGETRLKAPSQLKHSDGKE
ITFADYFKERYNLTLTDLNQPLLIVKFSSKKSYSILLPPELCVIT
>gnl|CDD|239208 cd02826, Piwi-like, Piwi-like: PIWI domain. Domain found in proteins involved in RNA silencing. RNA silencing refers to a group of related gene-silencing mechanisms mediated by short RNA molecules, including siRNAs, miRNAs, and heterochromatin-related guide RNAs. The central component of the RNA-induced silencing complex (RISC) and related complexes is Argonaute. The PIWI domain is the C-terminal portion of Argonaute and consists of two subdomains, one of which provides the 5' anchoring of the guide RNA and the other, the catalytic site for slicing. This domain is also found in closely related proteins, including the Piwi subfamily, where it is believed to perform a crucial role in germline cells, via a similar mechanism
TPLILKGRVLPKPQILFKNKFLRNIGPFEKPAKITNPVAVIAFRNEEVDDLVKRLADACRQLGMKIKEIP
IVSWIEDLNNSFKDLKSVFKNAIKAGVQLVIFILKEKKPPLHDEIKRLEAKSDIPSQVIQLKTAKKMRRL
KQTLDNLLRKVNSKLGGINYILDSPVKLFKSDIFIGFDVSHPDRRTVNGGPSAVGFAANLSNHTFLGGFL
YVQPSREVKLQDLGEVIKKCLDGFKKSTGEGLPEKIVIYRDGVSEGEFKRVKEEVEEIIKEACEIEESYR
PKLVIIVVQKRHNTRFFPNEKNGGVQNPEPGTVVDHTITSPGLSEFYLASHVARQGTVKPTKYTVVFNDK
NWSLNELEILTYILCLTHQNVYSPISLPAPLYYAHKLAKRGRN
>gnl|CDD|239209 cd02843, PAZ_dicer_like, PAZ domain, dicer_like subfamily. Dicer is an RNAse involved in cleaving dsRNA in the RNA interference pathway. It generates dsRNAs which are approximately 20 bp long (siRNAs), which in turn target hydrolysis of homologous RNAs. PAZ domains are named after the proteins Piwi Argonaut and Zwille. PAZ is found in two families of proteins that are essential components of RNA-mediated gene-silencing pathways, including RNA interference, the piwi and Dicer families. PAZ functions as a nucleic-acid binding domain, with a strong preference for single-stranded nucleic acids (RNA or DNA) or RNA duplexes with single-stranded 3' overhangs. It has been suggested that the PAZ domain provides a unique mode for the recognition of the two 3'-terminal nucleotides in single-stranded nucleic acids and buries the 3' OH group, and that it might recognize characteristic 3' overhangs in siRNAs within RISC (RNA-induced silencing) and other complexes
DSSTLDIDWEFMEKIEANARIGPRATPDEARQPFKFDAEDYQDAVVMPWYRNFDQPQYFYVAEICTDLRP
LSKFPGPEYETFEEYYKKKYKLDIQNLNQPLLDVDHTSTRLNLLTPRYVNQK
>gnl|CDD|239210 cd02844, PAZ_CAF_like, PAZ domain, CAF_like subfamily. CAF (for carpel factory) is a plant homolog of Dicer. CAF has been implicated in flower morphogenesis and in early Arabidopsis development and might function through posttranscriptional regulation of specific mRNA molecules. PAZ domains are named after the proteins Piwi, Argonaut, and Zwille. PAZ is found in two families of proteins that are essential components of RNA-mediated gene-silencing pathways, including RNA interference, the Piwi and Dicer families. PAZ functions as a nucleic-acid binding domain, with a strong preference for single-stranded nucleic acids (RNA or DNA) or RNA duplexes with single-stranded 3' overhangs. It has been suggested that the PAZ domain provides a unique mode for the recognition of the two 3'-terminal nucleotides in single-stranded nucleic acids and buries the 3' OH group, and that it might recognize characteristic 3' overhangs in siRNAs within RISC (RNA-induced silencing) and other complexes
AEVLLMHRDYSTNEASDLLHLADGSFCACDLKGSVVTAPHNGRFYVISGILDLNANSSFPGKEGLGYATY
AEYFKEKYGIVLNHPNQPLLKGKQIFNLHNLLHNRFEEKGESEEKEKDRYFVELPPELCSVIDLP
>gnl|CDD|239211 cd02845, PAZ_piwi_like, PAZ domain, Piwi_like subfamily. In multi-cellular organisms, the Piwi protein appears to be essential for the maintenance of germline stem cells. In the Drosophila male germline, Piwi was shown to be involved in the silencing of retrotransposons in the male gametes. The Piwi proteins share their domain architecture with other members of the argonaute family. The PAZ domain has been named after the proteins Piwi, Argonaut, and Zwille. PAZ is found in two families of proteins that are essential components of RNA-mediated gene-silencing pathways, including RNA interference, the Piwi and Dicer families. PAZ functions as a nucleic acid binding domain, with a strong preference for single-stranded nucleic acids (RNA or DNA) or RNA duplexes with single-stranded 3' overhangs. It has been suggested that the PAZ domain provides a unique mode for the recognition of the two 3'-terminal nucleotides in single-stranded nucleic acids and buries the 3' OH group, and that it might recognize characteristic 3' overhangs in siRNAs within RISC (RNA-induced silencing) and other complexes
STTVLDRMHKLYRQETDERFREECEKELIGSIVLTRYNNKTYRIDDIDFDKTPLSTFKKSDGTEITFVEY
YKKQYNIEITDLNQPLLVSRPKRRDPRGGEKEPIYLIPELCFLTGLT
>gnl|CDD|239212 cd02846, PAZ_argonaute_like, PAZ domain, argonaute_like subfamily. Argonaute is part of the RNA-induced silencing complex (RISC), and is an endonuclease that plays a key role in the RNA interference pathway. The PAZ domain has been named after the proteins Piwi,Argonaut, and Zwille. PAZ is found in two families of proteins that are essential components of RNA-mediated gene-silencing pathways, including RNA interference, the Piwi and Dicer families. PAZ functions as a nucleic acid binding domain, with a strong preference for single-stranded nucleic acids (RNA or DNA) or RNA duplexes with single-stranded 3' overhangs. It has been suggested that the PAZ domain provides a unique mode for the recognition of the two 3'-terminal nucleotides in single-stranded nucleic acids and buries the 3' OH group, and that it might recognize characteristic 3' overhangs in siRNAs within RISC (RNA-induced silencing) and other complexes
AQPVIEFLKEFLGFDTPLGLSDNDRRKLKKALKGLKVEVTHRGNTNRKYKIKGLSAEPASQQTFELKDGE
KEISVADYFKEKYNIRLKYPNLPCLQVGRKGKPNYLPMELCNIV
>gnl|CDD|199879 cd02847, E_set_Chitobiase_C, C-terminal Early set domain associated with the catalytic domain of chitobiase (also called N-acetylglucosaminidase). E or "early" set domains are associated with the catalytic domain of chitobiase at the C-terminus. Chitobiase digests the beta, 1-4 glycosidic bonds of the N-acetylglucosamine (NAG) oligomers found in chitin, an important structural element of fungal cell wall and arthropod exoskeletons. It is thought to proceed through an acid-base reaction mechanism, in which one protein carboxylate acts as the catalytic acid, while the nucleophile is the polar acetamido group of the sugar in a substrate-assisted reaction with retention of the anomeric configuration. The C-terminus of chitobiase may be related to the immunoglobulin and/or fibronectin type III superfamilies. E set domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others
VPGAKIENGKLEANVAFPGLTIEYSLDGGEWQTYSAGPVAVSGKVKLRAFSAGGRKSRVVTV
>gnl|CDD|199880 cd02848, E_set_Chitinase_N, N-terminal Early set domain associated with the catalytic domain of chitinase. E or "early" set domains are associated with the catalytic domain of chitinase at the N-terminal end. Chitinases hydrolyze the abundant natural biopolymer chitin, producing smaller chito-oligosaccharides. Chitin consists of multiple N-acetyl-D-glucosamine (NAG) residues connected via beta-1,4-glycosidic linkages and is an important structural element of fungal cell wall and arthropod exoskeletons. On the basis of the mode of chitin hydrolysis, chitinases are classified as random, endo-, and exo-chitinases and belong to families 18 and 19 of glycosyl hydrolases based on sequence criteria. The N-terminal domain of chitinase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others
PGTPSIAWGETKFSFVEVNQAATTSYKDLVKRKDAADVPVSWDVWSGETGTTWKVLLDGVVVWSGSITGS
SGTASFEVSKGGRYQMTVELCNADGCSTSAPKEIV
>gnl|CDD|199881 cd02850, E_set_Cellulase_N, N-terminal Early set domain associated with the catalytic domain of cellulase. E or "early" set domains are associated with the catalytic domain of cellulases at the N-terminal end. Cellulases are O-glycosyl hydrolases (GHs) that hydrolyze beta 1-4 glucosidic bonds in cellulose. They are usually categorized into either exoglucanases, which sequentially release terminal sugar units from the cellulose chain, or endoglucanases, which also attack the chain internally. The N-terminal domain of cellulase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others
KIRVNQVGYLPNAPKVAVVVGDETAASTFELVDAATGKVVYTGTLTPAGGDAASGETVYIADFSAVTTPG
TYYLRVGGVRSYPFEI
>gnl|CDD|199882 cd02851, E_set_GO_C, C-terminal Early set domain associated with the catalytic domain of galactose oxidase. E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others
GFGAPRPTITSAPKTVGYGQTFTVTVSGPGGGIVRVTLVRPGFVTHSFNMGQRLVKLPVTGSGGDYTVTV
TAPPNANVAPPGYYMLFVVNADGVPSVAKWVRV
>gnl|CDD|199883 cd02853, E_set_MTHase_like_N, N-terminal Early set domain associated with the catalytic domain of Maltooligosyl trehalose trehalohydrolase (also called Glycosyltrehalose trehalohydrolase) and similar proteins. E or "early" set domains are associated with the catalytic domain of Maltooligosyl trehalose trehalohydrolase (MTHase) and similar proteins at the N-terminal end. This subfamily also includes bacterial alpha amylases and 1,4-alpha-glucan branching enzymes which are highly similar to MTHase. Maltooligosyl trehalose synthase (MTSase) and MTHase work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. The N-terminal domain of MTHase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others
GAELLGDGGVRFRVWAPAAESVELVLEGGRRLPMQRDGDGWFEAEVAAAGAGTRYRFRLDGGLPVPDPAS
RFQPDGVHGPSQVV
>gnl|CDD|199884 cd02854, E_set_GBE_euk_N, N-terminal Early set domain associated with the catalytic domain of eukaryotic glycogen branching enzyme (also called 1,4 alpha glucan branching enzyme). This subfamily is composed of predominantly eukaryotic 1,4 alpha glucan branching enzymes, also called glycogen branching enzymes or starch binding enzymes in plants. E or "early" set domains are associated with the catalytic domain of the 1,4 alpha glucan branching enzymes at the N-terminal end. These enzymes catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage, yielding a non-reducing end oligosaccharide chain, as well as the subsequent attachment of short glucosyl chains to the alpha-1,6 position. Starch is composed of two types of glucan polymer: amylose and amylopectin. Amylose is mainly composed of linear chains of alpha-1,4 linked glucose residues and amylopectin consists of shorter alpha-1,4 linked chains connected by alpha-1,6 linkages. Amylopectin is synthesized from linear chains by starch branching enzyme. The N-terminal domains of the branching enzyme proteins may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others
DGGWVYREWAPNAKAVYLIGDFNNWNRESHPLKRDEFGKWELFLPPKEGSPAIPHGSKVKLHVETWDGGR
LDRIPAWAKRVVQDPETKIFDGVFW
>gnl|CDD|199885 cd02855, E_set_GBE_prok_N, N-terminal Early set domain associated with the catalytic domain of prokaryotic glycogen branching enzyme. This subfamily is composed of predominantly prokaryotic 1,4 alpha glucan branching enzymes, also called glycogen branching enzymes. E or "early" set domains are associated with the catalytic domain of glycogen branching enzymes at the N-terminal end. Glycogen branching enzyme catalyzes the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage, yielding a non-reducing end oligosaccharide chain, as well as the subsequent attachment of short glucosyl chains to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. The N-terminal domain of the 1,4 alpha glucan branching enzyme may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others
HFDAYEKLGAHPVEVDGVGGVRFRVWAPNAKRVSVVGDFNDWDGRAHPMRRIGDSGVWELFIPGAKEGDL
YKYEIETADGEVLLKADPYAFYAELRPGTASVVYD
>gnl|CDD|199886 cd02856, E_set_GDE_Isoamylase_N, N-terminal Early set domain associated with the catalytic domain of Glycogen debranching enzyme and bacterial isoamylase (also called glycogen 6-glucanohydrolase). E or "early" set domains are associated with the catalytic domain of the glycogen debranching enzyme at the N-terminal end. Glycogen debranching enzymes have both 4-alpha-glucanotransferase and amylo-1,6-glucosidase activities. As a transferase, it transfers a segment of the 1,4-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or another 1,4-alpha-D-glucan. As a glucosidase, it catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Bacterial isoamylases are also included in this subfamily. Isoamylase is one of the starch-debranching enzymes that catalyze the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen. Isoamylase contains a bound calcium ion, but this is not in the same position as the conserved calcium ion that has been reported in other alpha-amylase family enzymes. The N-terminal domain of glycogen debranching enzyme may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others
YPLGATLDDGGVNFAVFSPHATAVELCLFDEDGDEETARIPLDPRTGDVWHVFVPGLPAGQRYGYRVDGP
WDPEAGLRFNPNKLLLDPYAKAISGPPDWDPALAAHDGDSDDWPDDRDSAPPAPKSVVVD
>gnl|CDD|199887 cd02857, E_set_CDase_PDE_N, N-terminal Early set domain associated with the catalytic domain of cyclomaltodextrinase and pullulan-degrading enzymes. E or "early" set domains are associated with the catalytic domain of the cyclomaltodextrinase (CDase) and pullulan-degrading enzymes at the N-terminal end. Members of this subgroup include CDase, maltogenic amylase, and neopullulanase, all of which are capable of hydrolyzing all or two of the following three types of substrates: cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. The N-terminal domain of the CDase and pullulan-degrading enzymes may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others
IYHDPTSYAYAYPGAGDTVTIRLRTAKDDVDSVFLRYGDDYDGEEKLVPMKKVGSDGLFDYYEAEIPLPE
KRLRYYFELEDGGETLYYGERGVSEEGPDDDSYYFQIPY
>gnl|CDD|199888 cd02858, E_set_Esterase_N, N-terminal Early set domain associated with the catalytic domain of esterase. E or "early" set domains are associated with the catalytic domain of esterase at the N-terminal end. Esterases catalyze the hydrolysis of organic esters to release an alcohol or thiol and acid. The term esterase can be applied to enzymes that hydrolyze carboxylate, phosphate and sulphate esters, but is more often restricted to the first class of substrate. The N-terminal domain of esterase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others
GRVRFRIKAPDAKSVQVDLGGGKYDMTKGADGVWTGTTGPLVPGFHYYFLIVDGVRVVDPASPTFYGCGR
AASGIEIP
>gnl|CDD|199889 cd02859, E_set_AMPKbeta_like_N, N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain of AMP-activated protein kinase beta subunit. E or "early" set domains are associated with the catalytic domain of AMP-activated protein kinase beta subunit glycogen binding domain at the N-terminal end. AMPK is a metabolic stress sensing protein that senses AMP/ATP and has recently been found to act as a glycogen sensor as well. The protein functions as an alpha-beta-gamma heterotrimer. This N-terminal domain is the glycogen binding domain of the beta subunit. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and isoamylase
PVTFRWPGPGGKEVYVTGSFDNWQQPIPLEKSGDGEFSATVELPPGRYEYKFIVDGEWVHDPDLPTVTDE
FGNLNNVLEV
>gnl|CDD|199890 cd02860, E_set_Pullulanase, Early set domain associated with the catalytic domain of pullulanase (also called dextrinase and alpha-dextrin endo-1,6-alpha glucosidase). E or "early" set domains are associated with the catalytic domain of pullulanase at either the N-terminal or C-terminal end, and in a few instances at both ends. Pullulanase is an enzyme with activity similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. The E set domain of pullulanase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase
GDLGATYTPEKTTFKLWAPTAQKVKLLLYDDGDDAKPAKTVPMKREEKGVWSVTVDGDLKGKYYTYEVTV
YGETNEVVDPYAKAVGVNGKRSVIVDL
>gnl|CDD|199891 cd02861, E_set_pullulanase_like, Early set domain associated with the catalytic domain of pullulanase-like proteins. E or "early" set domains are associated with the catalytic domain of pullulanase at either the N-terminal or C-terminal end, and in a few instances at both ends. Pullulanase (also called dextrinase or alpha-dextrin endo-1,6-alpha glucosidase) is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. The E set domain of pullulanase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase
DVSDEEPFGGTTVYVRGSMNGWGEDDALTYQGNGVYSVTITLAAGSYEFKVASADWSTVNFGSGSSDVLV
ATGTLETLAAGGDNLSLT
>gnl|CDD|239213 cd02862, NorE_like, NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR
SAAAQRLPGKLGMWVFILSELLAFGALFIAYAVYRALYPELFAAGSAHLDLLLGALNTLVLLTSSFTVAL
AVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHKIAAGIDPDAGLFFTLYFLLTGFHLLHVLIGLG
ILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLYLV
>gnl|CDD|239214 cd02863, Ubiquinol_oxidase_III, Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex
HHTNTGSKKILGFWIYLMSDCILFATLFATYAVLSGNTAGGPPGHELFELPLVFIETFLLLLSSFTCGLA
MIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEFHHLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIW
ILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVYLLG
>gnl|CDD|239215 cd02864, Heme_Cu_Oxidase_III_1, Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria
REPFKVSWGKAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFALRIGHFNIPLVLIAIMTFIL
ITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRPWGNPWGAAQFGASFF
MITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYEIVEIAGLYWHFVDLVWVFIFAFFYLW
>gnl|CDD|239216 cd02865, Heme_Cu_Oxidase_III_2, Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria
YVAGARSPGWWGLWVFMAVEGTLFALLISAYFMRMTSGDWQPGAPLPLPNLLSLNTAVLAASSVAMQWAR
RAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVAL
AIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT
>gnl|CDD|211343 cd02866, PseudoU_synth_TruA_Archea, Archeal pseudouridine synthases. This group consists of archeal pseudouridine synthases.Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. This group of proteins make Psedouridine in tRNAs
LKIAYDGTNFHGFQRQPDVRTVEGELIKALEELGIIESRARLYSAGRTDRGVHALGNVVVFETEKEPIPP
MINAKLPKDIWVLAGAKVPEDFDPRRWAHRKYYRYNLGSDYDVEAMKEAAKKLIGTHDFSNFSKRDGRKD
PVRTIERIEISENGEFITIDVVGESFLWNMVRRIVGALSEVGKGKRENEWVEKLLDGEFRPEGVPPAPPE
GLILVDVKY
>gnl|CDD|211344 cd02867, PseudoU_synth_TruB_4, Pseudouridine synthase homolog 4. This group consists of Eukaryotic TruB proteins similar to Saccharomyces cerevisiae Pus4. S. cerevisiae Pus4, makes psi55 in the T loop of both cytoplasmic and mitochondrial tRNAs. Psi55 is almost universally conserved. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi)
GVFAINKPSGITSAQVLNDLKPLFLNSALFKDKIQRAVAKRGKKARRRKGRKRSKLKIGHGGTLDPLATG
VLVVGVGAGTKQLQDYLSCSKTYEATGLFGASTTTYDREGKILKKKPYSHITREDIEEVLAKFRGDIKQV
PPLYSALKMDGKRLYEYAREGKPLPRPIERRQVVVSELLVKDWIEPGPLFTRTVEEEGKQYERSVVKMLG
KELKTFAEVTELTATAEGDPVEEVEATHEESKRKSEVEEEANEKSLGPEARSLESDAGRGSFSPAAMVRL
ARVGQGTYIRQDVKLIRTENLVSGEDAELGRE
>gnl|CDD|211345 cd02868, PseudoU_synth_hTruB2_like, Pseudouridine synthase, humanTRUB2_like. This group consists of eukaryotic pseudouridine synthases similar to human TruB pseudouridine synthase homolog 2 (TRUB2). Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi)
GLFAVYKPPGVHWKHVRDTIESNLLKYFPEDKVLVGVHRLDAFSSGVLVLGVNHGNKLLSHLYSNHPTRV
YTIRGLLGKATENFFHTGRVIEKTTYDHITREKIERLLAVIQSGHQQKAFELCSVDDQSQQAAELAARGL
IRPADKSPPIIYGIRLLEFRPPEFTLEVQCINETQEYLRKLIHEIGLELRSSAVCTQVRRTRDGPFTVDD
ALLRKQWNLQNIISNI
>gnl|CDD|211346 cd02869, PseudoU_synth_RluA_like, Pseudouridine synthase, RluA family. This group is comprised of eukaryotic, bacterial and archeal proteins similar to eight site specific Escherichia coli pseudouridine synthases: RsuA, RluA, RluB, RluC, RluD, RluE, RluF and TruA. Pseudouridine synthases catalyze the isomerization of specific uridines in a n RNA molecule to pseudouridines (5-ribosyluracil, psi) requiring no cofactors. E. coli RluC for example makes psi955, 2504 and 2580 in 23S RNA. Some psi sites such as psi1917 in 23S RNA made by RluD are universally conserved. Other psi sites occur in a more restricted fashion, for example psi2819 in 21S mitochondrial ribosomal RNA made by S. cerevisiae Pus5p is only found in mitochondrial large subunit rRNAs from some other species and in gram negative bacteria. The E. coli counterpart of this psi residue is psi2580 in 23S rRNA. psi2604in 23S RNA made by RluF has only been detected in E.coli
LLVVNKPAGLPVHPGPGHLTGTLVNALLKLLLLLGEEFRPGLVHRLDKDTSGLLLVAKNKKAAAKLSKQF
KERKVKKTYLALVDGKPPEDEGTIDAPLGRKKRKKRARVVVSEDGKPAITHYKVLERFGNVTLVELQLET
GRTHQIRVHLASIGHPIVGDPKYGGKASDSPGLKRLALHAYRLSF
>gnl|CDD|211347 cd02870, PseudoU_synth_RsuA_like, Pseudouridine synthases, RsuA subfamily. Pseudouridine synthases are responsible for the synthesis of pseudouridine from uracil in ribosomal RNA. The RsuA subfamily includes Pseudouridine Synthase similar to Ribosomal small subunit pseudouridine 516 synthase. Most of the proteins in this family are bacterial proteins
YLLLNKPRGVVSTVRDPEGRPTVLDLLKDVGERLFPVGRLDYDTEGLLLLTNDGELANRLTHPRYGVEKT
YLVKVRGVPSEEELRRLRAGVELDDGKTAPAKVKVLSRDPKNTLLEVTLHEGRNRQVRRMFEAVGHPVLR
LKRVRI
>gnl|CDD|119350 cd02871, GH18_chitinase_D-like, GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus
KVLVGYWHNWDNGAGSGRQDLDDVPSKYNVINVAFAEPTSDGGGEVTFNNGSSPGGYSPAEFKADIKALQ
AKGKKVLISIGGANGHVDLNHTAQEDNFVDSIVAIIKEYGFDGLDIDLESGSNPLNATPVITNLISALKQ
LKDHYGPNFILTMAPETPYVQGGYAAYGGIWGAYLPLIDNLRDDLTWLNVQYYNSGGMGGCDGQSYSQGT
ADFLVALADMLLTGFPIAGNDRFPPLPADKVVIGLPASPSAAGGGYVSPSEVIKALDCLMKGTNCGSYYP
AGGYPSLRGLMTWSINWDATNNYEFSKNYGAY
>gnl|CDD|119351 cd02872, GH18_chitolectin_chitotriosidase, This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens
VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPDGNIIILDEWNDIDLGLYERFNALKEKNPN
LKTLLAIGGWNFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRGGPPEDKENFVTLL
KELREAFEPEAPRLLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSAD
TGDQKYLNVDYAIKYWLSKGAPPEKLVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYY
EICEFLKSGWTVVWDDEQKVPYAYKGNQWVGYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGQG
KYPLLNAINRAL
>gnl|CDD|119352 cd02873, GH18_IDGF, The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects that include at least five members, some of which are encoded by genes in a tight cluster. The IDGF's have an eight-stranded alpha/beta barrel fold and are related to the glycosyl hydrolase family 18 (GH18) chitinases, but they have an amino acid substitution known to abolish chitinase catalytic activity. IDGFs may have evolved from chitinases to gain new functions as growth factors, interacting with cell surface glycoproteins involved in growth-promoting processes
KLVCYYDSKSYLREGLAKMSLEDLEPALQFCTHLVYGYAGIDADTYKIKSLNEDLDLDKSHYRAITSLKR
KYPHLKVLLSVGGDRDTDEEGENEKYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPKNKPKKVR
GTFGSAWHSFKKLFTGDSVVDEKAAEHKEQFTALVRELKNALRPDGLLLTLTVLPHVNSTWYFDVPAIAN
NVDFVNLATFDFLTPERNPEEADYTAPIYELYERNPHHNVDYQVKYWLNQGTPASKLNLGIATYGRAWKL
TKDSGITGVPPVLETDGPGPAGPQTKTPGLLSWPEICSKLPNPANLKGADAPLRKVGDPTKRFGSYAYRP
ADENGEHGIWVSYEDPDTAANKAGYAKAKGLGGVALFDLSLDDFRGQCTGDKFPILRSAKYRL
>gnl|CDD|119353 cd02874, GH18_CFLE_spore_hydrolase, Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis
AIEVLGYYTPRNGSDYESLRANAPYLTYIAPFWYGVDADGTLTGLPDERLIEAAKRRGVKPLLVITNLTN
GNFDSELAHAVLSNPEARQRLINNILALAKKYGYDGVNIDFENVPPEDREAYTQFLRELSDRLHPAGYTL
STAVVPKTSADQFGNWSGAYDYAAIGKIVDFVVLMTYDWHWRGGPPGPVAPIGWVERVLQYAVTQIPREK
ILLGIPLYGYDWTLPYKKGGKASTISPQQAINLAKRYGAEIQYDEEAQSPFFRYVDEQGRRHEVWFEDAR
SLQAKFELAKEYGLRGVSYWRLGLEDPQNWLLL
>gnl|CDD|119354 cd02875, GH18_chitobiase, Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase
RIILLILLILLAISKSYECPCIEPELCEPIEIGPRFEFLVFSVNSTNYPNYDWSKVTTIAIFGDIDDELL
CYAHSKGVRLVLKGDVPLEQISNPTYRTQWIQQKVELAKSQFMDGINIDIEQPITKGSPEYYALTELVKE
TTKAFKKENPGYQISFDVAWSPSCIDKRCYDYTGIADASDFLVVMDYDEQSQIWGKECIAGANSPYSQTL
SGYNNFTKLGIDPKKLVMGLPWYGYDYPCLNGNLEDVVCTIPKVPFRGANCSDAAGRQIPYSEIMKQINS
SIGGRLWDSEQKSPFYNYKDKQGNLHQVWYDNPQSLSIKVAYAKNLGLKGIGMWNGDLLDYSGLPIAEKQ
TEDMWNAL
>gnl|CDD|119355 cd02876, GH18_SI-CLP, Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein of unknown function that interacts with the endocytic/sorting transmembrane receptor stabilin-1 and is secreted from the lysosome. SI-CLP has a glycosyl hydrolase family 18 (GH18) domain but lacks a chitin-binding domain. The catalytic amino acids of the GH18 domain are not conserved in SI-CLP, similar to the chitolectins YKL-39, YKL-40, and YM1/2. Human SI-CLP is sorted to late endosomes and secretory lysosomes in alternatively activated macrophages
FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRKGNKFVIEGTHDIDKGWIEEVRKANKNIKIL
PRVLFEGWSYQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAYGVPDKRKELIQLVIHLG
ETLHSANLKLILVIPPPREKGNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSPQRPGPNAPLSWVRSCLEL
LLPESGKKRAKILLGLNFYGNDYTLPGGGGAITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKGGKHAV
FYPTLKSIQLRLDLAKELGTGISIWELGQGLDYFYDLL
>gnl|CDD|119356 cd02877, GH18_hevamine_XipI_class_III, This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin
GNIAVYWGQNSDEGSLREYCDTGNYDIVNISFLNVFGSGGTPGLNFAGHCGGSTYPNCPQLGADIKHCQS
KGKKVLLSIGGAGGSYSLSSDADAKDFADYLWNAFGGGTDSGVPRPFGDAVVDGFDFDIEHGSPENYDAL
AKRLRSLFASDPSKKYYLTAAPQCPYPDASLGDAIATGLFDFIFVQFYNNPCCSYASGNASGFNFNWDTW
TSWAKATSNAKVFLGLPASPEAAGSGYVDPSELASLVLPVKQKSPNFGGVMLWDASQDKQGTGYSSKIKD
>gnl|CDD|119357 cd02878, GH18_zymocin_alpha, Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase
KNIAYFEAYNLDRPCLNMDVTQIDTSKYTHIHFAFANITSDFSVDVSSVQEQFSDFKKLKGVKKILSFGG
WDFSTSPSTYQIFRDAVKPANRDTFANNVVNFVNKYNLDGVDFDWEYPGAPDIPGIPAGDPDDGKNYLEF
LKLLKSKLPSGKSLSIAAPASYWYLKGFPIKDMAKYVDYIVYMTYDLHGQWDYGNKWASPGCPAGNCLRS
HVNKTETLDALSMITKAGVPSNKVVVGVASYGRSFKMADPGCTGPGCTFTGPGSGAEAGRCTCTAGYGAI
SEIEIIDISKSKNKRWYDTDSDSDILVYDDDQWVAYMSPATKAARIEWYKGLNFGGTSDWAVDLQ
>gnl|CDD|119358 cd02879, GH18_plant_chitinase_class_V, The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the chitin-binding domain present in other GH18 enzymes. The GH18 domain of the class V chitinases has endochitinase activity in some cases and no catalytic activity in others. Included in this family is a lectin found in black locust (Robinia pseudoacacia) bark, which binds chitin but lacks chitinase activity. Also included is a chitinase-related receptor-like kinase (CHRK1) from tobacco (Nicotiana tabacum), with an N-terminal GH18 domain and a C-terminal kinase domain, which is thought to be part of a plant signaling pathway. The GH18 domain of CHRK1 is expressed extracellularly where it binds chitin but lacks chitinase activity
STIVKGGYWPAWSEEFPPSNIDSSLFTHLFYAFADLDPSTYEVVISPSDESEFSTFTETVKRKNPSVKTL
LSIGGGGSDSSAFAAMASDPTARKAFINSSIKVARKYGFDGLDLDWEFPSSQVEMENFGKLLEEWRAAVK
DEARSSGRPPLLLTAAVYFSPILFLSDDSVSYPIEAINKNLDWVNVMAYDYYGSWESNTTGPAAALYDPN
SNVSTDYGIKSWIKAGVPAKKLVLGLPLYGRAWTLYDTTTVSSYVYAGTTWIGYDDVQSIAVKVKYAKQK
GLLGYFAWAVGYDDNNWLS
>gnl|CDD|467528 cd02883, NUDIX_Hydrolase, NUDIX hydrolase superfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
VAVGAVVFDDEGRVLLVRRSDGPGPGGWELPGGGVEPGETPEEAAVREVREETGLDVEVLRLLGVYEFPD
PDEGRHVVVLVFLARVVGGEPPPLDDEEISEVRWVP
>gnl|CDD|467529 cd02885, NUDIX_IPP_Isomerase, Isopentenyl diphosphate isomerase. Isopentenyl diphosphate (IPP) isomerase, a member of the NUDIX hydrolase superfamily, is a key enzyme in the isoprenoid biosynthetic pathway. Isoprenoids comprise a large family of natural products including sterols, carotenoids, dolichols and prenylated proteins. These compounds are synthesized from two precursors: isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). IPP isomerase catalyzes the interconversion of IPP and DMAPP by a stereoselective antarafacial transposition of hydrogen. The enzyme requires one Mn2+ or Mg2+ ion in its active site to fold into an active conformation and also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. The metal binding site is present within the active site and plays structural and catalytical roles. IPP isomerase is well represented in several bacteria, archaebacteria and eukaryotes, including fungi, mammals and plants. Despite sequence variations (mainly at the N-terminus), the core structure is highly conserved
EVILVDEDDNPIGTAEKLEAHRKGTLLHRAFSVFLFNSKGELLLQRRALSKYTWPGLWTNTCCSHPLPGE
GVEDAAQRRLREELGIPVCDLEELPRFRYRATDDNGLVEHEIDHVFVGRADGDPVPNPEEVSDYRWVSLE
ELRELLAATPEAFTPWFRLILE
>gnl|CDD|153089 cd02888, RNR_II_dimer, Class II ribonucleotide reductase, dimeric form. Ribonucleotide reductase (RNR) catalyzes the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, and bacteriophage, use a diiron-tyrosyl radical. Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in anaerobic bacteria, bacteriophage, and archaea, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. All three RNRs have a ten-stranded alpha-beta barrel domain that is structurally similar to the domain of PFL (pyruvate formate lyase). Class II RNRs are found in bacteria that can live under both aerobic and anaerobic conditions. Many, but not all members of this class are found to be homodimers. Adenosylcobalamin interacts directly with an active site cysteine to form the reactive cysteine radical
ADEFFYLLLSQGFIPNSPTLMNAGTGELGQLSACFVLPVEDDSIEGIFDALKEAALIFKRGGGVGYNFSR
LRPKGDIVKSTGGVASGPVSFMRVFDAATGVIKQGGTRRGANMGVLDVDHPDIEEFIDAKMKEEKTVVLQ
NFNISVAVTDAFMEAVENDEPWELRNPREPDTGKVYRTVPARELWDKIVEAAWDSADPGVLFIDTINRWN
PLPGLGRINATNPCGEQPLLPYESCNLGSINLSKFVKNPFGGASFDFERLREAVRLAVRFLDNVIDVNRY
PLPEIAEETKATRRIGLGVMGLADMLIKLGIPYDSEEARELAERIMSFIRDAAYRASAELAKERGPFPLF
DASRYLMLKVIVNAKELPDDVLEEIEKYGIRNAHLTTIAPTGTISLIAGTSSGIEPIFSPEDHVRMQAAL
QPWVDGAISKTINLPNDATVEDVEAVYLLAWKLGLKGITVYRDG
>gnl|CDD|239219 cd02889, SQCY, Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. Bacterial SQCY catalyzes the convertion of squalene to hopene or diplopterol. Eukaryotic OSQCY transforms the 2,3-epoxide of squalene to compounds such as, lanosterol (a metabolic precursor of cholesterol and steroid hormones) in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain. This group also contains SQCY-like archael sequences and some bacterial SQCY's which lack this minor domain
IRRALDFLLSLQAPDGHWPGEYSQVWDTALALQALLEAGLAPEFDPALKKALEWLLKSQIRDNPDDWKVK
YRHLRKGGWAFSTANQGYPDSDDTAEALKALLRLQKKPPDGKKVSRERLYDAVDWLLSMQNSNGGFAAFE
PDNTYKYLELIPEVDGDIMIDPPYVECTGSVLEALGLFGKLYPEHRREIDPAIRRAVKYLEREQEPDGSW
YGRWGVCFIYGTWFALEALAAAGEDENSPYVRKACDWLLSKQNPDGGWGESYESYEDPSYAGGGRSTVVQ
TAWALLALMAAGEPDSEAVKRGVKYLLNTQQEDGDWPQEEITGVFFKNFYIRYHNYRNYFPLWALGRY
>gnl|CDD|239220 cd02890, PTase, Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The protein prenyltransferase family of lipid-modifying enzymes includes protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II). They catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between the C1 atom of farnesyl (15-carbon by FTase) or geranylgeranyl (20-carbon by GGTase-I, II) isoprenoid lipids and cysteine residues at or near the C-terminus of protein acceptors. FTase and GGTase-I prenylate the cysteine in the terminal sequence, "CAAX"; and GGTase-II prenylates both cysteines in the "CC" (or "CXC") terminal sequence. These enzymes are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTase-II does not recognize its protein acceptor directly but requires Rab to complex with REP (Rab escort protein) before prenylation can occur. These enzymes are found exclusively in eukaryotes
REKHIKYLQRCLKLLPSSYTSLDASRLWLLYWILSSLDLLGEDLDDENKDEIIDFIYSCQVNEDGGFGGG
PGQDPHLASTYAAVLSLAILGDDALSRIDREKIYKFLSSLQNPDGSFRGDLGGEVDTRFVYCALSILSLL
NILTDIDKEKLIDYILSCQNYDGGFGGVPGAESHGGYTFCAVASLALLGRLDLIDKERLLRWLVERQLAS
GGGFNGRPNKLVDTCYSFWVGASLKILGRLHLIDQEKLREYILSCQQSEVGGFSDKPGKPPDLYHTYYGL
SGLSLL
>gnl|CDD|239221 cd02891, A2M_like, Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier protein in serum. It is a broadly specific proteinase inhibitor. The structural thioester of alpha (2)-M, is involved in the immobilization and entrapment of proteases. This group contains another broadly specific proteinase inhibitor: pregnancy zone protein (PZP). PZP is a trace protein in the plasma of non-pregnant females and males which is elevated in pregnancy. Alpha (2)-M and PZ bind to placental protein-14 and may modulate its activity in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system. This group also contains C3, C4 and C5 of vertebrate complement. The vertebrate complement is an effector of both the acquired and innate immune systems The point of convergence of the classical, alternative and lectin pathways of the complement system is the proteolytic activation of C3. C4 plays a key role in propagating the classical and lectin pathways. C5 participates in the classical and alternative pathways. The thioester bond located within the structure of C3 and C4 is central to the function of complement. C5 does not contain an active thioester bond
SLGNLDYLLRYPYGCGEQTMSRAAPNLYVLKYLDATGQLTPEIREKALEYIRKGYQRLLTYQRSDGSFSA
WGNSDSGSTWLTAYVVKFLSQARKYIDVDENVLARALGWLVPQQKEDGSFRELGPVIHREMKGGVDDSVS
LTAYVLIALAEAGKACDASIEKALAYLETQLDGLLDPYALAILAYALALAGDSTRADEALKKLLEAAREK
GGTAHWSLSWPGDYGSSLRVEATAYALLALLKLGDLEEAGPIAKWLAQQRNSGGGFLSTQDTVVALQALA
AY
>gnl|CDD|239222 cd02892, SQCY_1, Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. This group contains bacterial SQCY which catalyzes the convertion of squalene to hopene or diplopterol and eukaryotic OSQCY which transforms the 2,3-epoxide of squalene to compounds such as, lanosterol in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain
IRRALEFLLSLQAPDGHWPGELEGPLFITAEYILLLYILGIPIDPEHRKEIARYLRNHQNPDGGWGLHHE
GPSTMFGTVLNYVALRLLGVSPDDPHMVKARNWILSHGGAARIPVWGKIWLALLGVYPWEGVPPLPPELW
LLPSWLPFHPYKFWCWARTVYVPMSYLYGKRPVAPITPLVLSLRDELYVEPYEKINWYKHRNDLYDYRPP
WQRLFDALDRLLHWYEPLPPKPLRRKALRKAYEWILYRDENTGYLGIIPPPKANNMLALWVLGYPDSPAF
KRHLERIDDFLWLGPEGMKMCQTNGSQVWDTALAVQALLEAGLAPEFDPALKKALDWLLESQILDNPGDW
KVKYRHLRKGGWAFSTANQGYPDSDDTAEALKALLRLQELPPFGEKVSRERLYDAVDWLLGMQNSNGGFA
AFEPDNTYHWLENLNPFEDFGDIMIDPPYVECTGSVLEALGLFGKLYPGHRREIDPAIRRAVKYLLREQE
PDGSWYGRWGVCYIYGTWFALEALAAAGEDYENSPYIRKACDFLLSKQNPDGGWGESYLSYEDKSYAGGG
RSTVVQTAWALLALMAAGEPDSEAVERGIKYLLNTQLPDGDWPQEEITGVGFPNFYIRYHNYRNYFPLWA
LGRY
>gnl|CDD|239223 cd02893, FTase, Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). FTases are a subgroup of PTase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. These proteins are heterodimers of alpha and beta subunits. Both subunits are required for catalytic activity. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids. Ftase attaches a 15-carbon farnesyl group to the cysteine within the C-terminal CaaX motif of substrate proteins when X is Ala, Met, Ser, Cys or Gln. Protein farnesylation has been shown to play critical roles in a variety of cellular processes including Ras/mitogen activated protein kinase signaling pathways in mammals and, abscisic acid signal transduction in Arabidopsis
REKHIKYLKKSLRQLPSSFTSLDASRPWLLYWILHSLELLGEELDQSYADDVISFLRRCQNPSGGFGGGP
GQLPHLATTYAAVNALAIIGTEEAYDVIDREALYKFLLSLKQPDGSFRMHVGGEVDVRGTYCAISVASLL
NILTDELFEGVAEYILSCQTYEGGFGGVPGNEAHGGYTFCALAALAILGKPDKLDLESLLRWLVARQMRF
EGGFQGRTNKLVDGCYSFWVGGSLPILEAILNAEKKFDDSAEGTLFDQEALQEYILLCCQSEEGGLRDKP
GKPRDFYHTCYALSGLSIA
>gnl|CDD|239224 cd02894, GGTase-II, Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-IIs are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-II). GGTase-II catalyzes alkylation of both cysteine residues in Rab proteins containing carboxy-terminal "CC", "CXCX" or "CXC" motifs. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTas-II requires an escort protein to bring the substrate protein to the catalytic heterodimer and to escort the geryanylgeranylated product to the membrane
LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQDNEDGGFG
GSPGHDPHILSTLSAIQILALYDLLNKIDENKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLT
LLGKLDLIDVDKAVDYLLSCYNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQL
PSGGLNGRPEKLPDVCYSWWVLSSLKIIGRLHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFG
LAGLSLL
>gnl|CDD|239225 cd02895, GGTase-I, Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-I s are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-I). GGTase-I prenylates the cysteine in the terminal sequence, "CAAX" when X is Leu or Phe. Substrates for GTTase-I include the gamma subunit of neural G-proteins and several Ras-related G-proteins. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity
KKKHVKFFQRCLQLLPSSYQSLDTNRLTIAFFALSGLDLLGALDSILVEEKDDIIEWIYSLQVLSNLPRG
GFRGSSTLGLPGTASKYDTGNLAMTYFALLSLLILGDDLSRVDRKAILNFLSKLQLPDGSFGSVLDSEGG
ENDMRFCYCAVAICYMLDDWSEEDIDKEKLIDYIKSSQSYDGGFGQGPGLESHGGSTFCAIASLSLLGKL
EELSEKFLERLKRWLVHRQVSGTGFNGRPNKPADTCYSFWVGASLKLLDAFQLIDFEKNRNYLLSTQQSL
VGGFAKNPDSHPDPLHSYLGLAALSLI
>gnl|CDD|239226 cd02896, complement_C3_C4_C5, Proteins similar to C3, C4 and C5 of vertebrate complement. The vertebrate complement system, comprised of a large number of distinct plasma proteins, is an effector of both the acquired and innate immune systems. The point of convergence of the classical, alternative and lectin pathways of the complement system is the proteolytic activation of C3. C4 plays a key role in propagating the classical and lectin pathways. C5 participates in the classical and alternative pathways. The thioester bond located within the structure of C3 and C4 is central to the function of complement. C5 does not contain an active thioester bond
SPEGLEKLIRLPTGCGEQTMIKLAPTVYALRYLDTTNQWEKLGPERRDEALKYIRQGYQRQLSYRKPDGS
YAAWKNRPSSTWLTAFVVKVFSLARKYIPVDQNVICGSVNWLISNQKPDGSFQEPSPVIHREMTGGVEGS
EGDVSLTAFVLIALQEARSICPPEVQNLDQSIRKAISYLENQLPNLQRPYALAITAYALALADSPLSHAA
NRKLLSLAKRDGNGWYWWTIDSPYWPVPGPSAITVETTAYALLALLKLGDIEYANPIARWLTEQRNYGGG
FGSTQDTVVALQALAEY
>gnl|CDD|239227 cd02897, A2M_2, Proteins similar to alpha2-macroglobulin (alpha (2)-M). This group also contains the pregnancy zone protein (PZP). Alpha(2)-M and PZP are broadly specific proteinase inhibitors. Alpha (2)-M is a major carrier protein in serum. The structural thioester of alpha (2)-M, is involved in the immobilization and entrapment of proteases. PZP is a trace protein in the plasma of non-pregnant females and males which is elevated in pregnancy. Alpha (2)-M and PZ bind to placental protein-14 and may modulate its activity in T-cell growth and cytokine production contributing to fetal survival. It has been suggested that thioester bond cleavage promotes the binding of PZ and alpha (2)-M to the CD91 receptor clearing them from circulation
ALQNLDNLLRMPYGCGEQNMVNFAPNIYVLDYLKATGQLTPEIESKALGFLRTGYQRQLTYKHSDGSYSA
FGESDKSGSTWLTAFVLKSFAQARPFIYIDENVLQQALTWLSSHQKSNGCFREVGRVFHKAMQGGVDDEV
ALTAYVLIALLEAGLPSERPVVEKALSCLEAALDSISDPYTLALAAYALTLAGSEKRPEALKKLDELAIS
EDGTKHWSRPPPSEEGPSYYWQAPSAEVEMTAYALLALLSAGGEDLAEALPIVKWLAKQRNSLGGFSSTQ
DTVVALQALAKY
>gnl|CDD|239228 cd02899, PLAT_SR, Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates. This subfamily contains Toxoplasma gondii Scavenger protein TgSR1
KTYTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTLSQGFYPGSLKRIRFRAADVGDINAIILSNTALN
DPWYCDYVRIKSEDGKVFAFNVKRWIGYPYEQSVEVSLK
>gnl|CDD|394872 cd02900, Macro_Appr_pase, macrodomain, Appr-1"-pase family. Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. The yeast protein Ymx7 and related proteins in this family contain a stand-alone macrodomain and may be specific phosphatases catalyzing the conversion of ADP-ribose-1"-monophosphate (Appr-1"-p) to ADP-ribose. Appr-1"-p is an intermediate in a metabolic pathway involved in pre-tRNA splicing
IYLLRDYEELVNAWRESFGRLYEQYQDSVEISNGDIFSGAPSTLSDAIVSPANSFGFMDGGFDLAISRYF
GGPQLTERLQEVLRTEWRGEALVGTCTVIPLQQCLRGADSNNGDGIKYLIHAPTMRVPSAVVWDTENVYL
AFWAVLLAVPKHNAELDTGLEPIRSVLCPGLGTGVGGVPPERCAKQMVLAYRHFA
>gnl|CDD|394873 cd02901, Macro_Poa1p-like, macrodomain, Poa1p-like family. Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation
KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKLLGGVAVLKRDGVKRYI
YYLITKKSYGPKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR
>gnl|CDD|394874 cd02903, Macro_BAL-like, macrodomain, B-aggressive lymphoma (BAL)-like family. Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to BAL (B-aggressive lymphoma) proteins, which contain one to three macrodomains. Most BAL family macrodomains belong to this family except for the most N-terminal domain in multiple-domain containing proteins. This family includes the second and third macrodomains of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors
YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPASGDVIVT
SGGNLPCKYVYHVVLPHYNPGNEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEV
LKFSSKNPSSSLKEVRFVIFPPETLQAFSDELAKR
>gnl|CDD|394875 cd02904, Macro_H2A-like, macrodomain, macroH2A-like family. Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family are similar to macroH2A, a variant of the major-type core histone H2A, which contains an N-terminal H2A domain and a C-terminal nonhistone macrodomain. Histone macroH2A is enriched on the inactive X chromosome of mammalian female cells. It does not bind poly ADP-ribose, but does bind the monomeric SirT1 metabolite O-acetyl-ADP-ribose (OAADPR) with high affinity through its macrodomain. This family also includes the ADP-ribose binding macrodomain of the macroH2A variant, macroH2A1.1. The macroH2A1.1 isoform inhibits PARP1-dependent DNA-damage induced chromatin dynamics. The putative ADP-ribose binding pocket of the human macroH2A2 macrodomain exhibits marked structural differences compared with the macroH2A1.1 variant
GPGDGFTILSEKKLFLGQKLTVVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRK
SNGPLEVAGAAISPGHNLPAKFVIHCNSPSWGSDKCEELLEKTVKNCLALADEKKLKSVAFPSIGSGRNG
FPKQTAAQTILKAISNYFVSVMSSSLKQIYFVLFDMESIGIYTSELAK
>gnl|CDD|394876 cd02905, Macro_GDAP2-like, macrodomain, GDAP2-like family. Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. This family contains proteins similar to human GDAP2, the ganglioside induced differentiation associated protein 2, whose gene is expressed at a higher level in differentiated Neuro2a cells compared with non-differentiated cells. GDAP2 contains an N-terminal macrodomain and a C-terminal Sec14p-like lipid binding domain. It is specifically expressed in brain and testis
RKIVLWDGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGGCRTGEAKLTKGYNLPAR
YVIHTVGPRYNEKYRTAAESALYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFL
EKHGSSFEAVVFVVTEEEMETYERLLPLY
>gnl|CDD|394877 cd02907, Macro_Af1521_BAL-like, macrodomain, Af1521-like family. Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. The macrodomains in this family show similarity to Af1521, a protein from Archaeoglobus fulgidus containing a stand-alone macrodomain. Af1521 binds ADP-ribose and exhibits phosphatase activity toward ADP-ribose-1"-monophosphate (Appr-1"-p). Also included in this family are the N-terminal (or first) macrodomains of BAL (B-aggressive lymphoma) proteins which contain multiple macrodomains, such as the first macrodomain of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors
GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAG
KLPCKYVIHAVGPRWSGGSKEECEDLLYKAVLNSLEEAEELKATSIAIPAISSGIFGFPLDLCAEAIVEA
IKDFSESNSSSSLKEIRL
>gnl|CDD|438955 cd02908, Macro_OAADPr_deacetylase, macrodomain, O-acetyl-ADP-ribose (OAADPr) family. Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. This family includes eukaryotic macrodomain proteins such as human MacroD1 and MacroD2, and bacterial proteins such as Escherichia coli YmdB; these have been shown to be O-acetyl-ADP-ribose (OAADPr) deacetylases that efficiently catalyze the hydrolysis of OAADPr to produce ADP-ribose and free acetate. OAADPr is a sirtuin reaction product generated from the NAD+-dependent protein deacetylation reactions and has been implicated as a signaling molecule. By acting on mono-ADP-ribosylated substrates, OAADPr deacetylases may reverse cellular ADP-ribosylation
KISLWRGDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKLGGVCPTGEAKITPGYNLPAK
YVIHTVGPIGEGGVEEEPELLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLE
EHDKIDRIIFVVFLDEDYKIYEELLP
>gnl|CDD|380374 cd02909, cupin_pirin_N, pirin, N-terminal cupin domain. This family contains the N-terminal domain of pirin, a nuclear protein that is highly conserved among mammals, plants, fungi, and prokaryotes. It is widely expressed in dot-like subnuclear structures in human tissues such as liver and heart. Pirin functions as both a transcriptional cofactor and an apoptosis-related protein in mammals and is involved in seed germination and seedling development in plants. The pirins have been assigned as a subfamily of the cupin superfamily based on structure and sequence similarity. The pirins have two tandem cupin-like folds but the C-terminal cupin fold has diverged considerably and does not have a metal binding site. The exact functions of pirins are unknown but they have quercitinase activity in Escherichia coli and are thought to play important roles in transcription and apoptosis. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold generally capable of homodimerization
ARVRRVLPTPELRNLDPFLLLDHFGPVKPEPYGAGFPPHPHRGFETVTYLLEGEVEHRDSLGNKGVIRPG
DVQWMTAGRGIVHSEMPPEEGGPLHGLQLWVNLP
>gnl|CDD|380375 cd02910, cupin_Yhhw_N, Escherichia coli YhhW and YhaK and related proteins, pirin-like bicupin, N-terminal cupin domain. This family includes the N-terminal cupin domains of YhhW and YhaK, Escherichia coli pirin-like proteins with unknown function. YhhW is structurally similar not only to human pirin but also to quercitin 2,3-dioxygenase (quercitinase). Although the function of YhhW is not completely understood, YhhW and its human ortholog have quercitinase activity and are likely to play an important role in transcription and apoptosis. This N-terminal cupin domain of YhhW has a metal coordination site and is thought to have catalytic activity while the C-terminal cupin-like domain has diverged considerably and has closer alignment with C-terminal pirin. YhaK is found in low abundance in the cytosol of E. coli and is strongly up-regulated by nitroso-glutathione (GSNO). There are major structural differences at the N-terminus of YhaK compared with YhhW; YhaK lacks the canonical cupin metal-binding residues of pirins and may be involved in chloride binding and/or sensing of oxidative stress in enterobacteria. YhaK showed no quercetinase and peroxidase activity; however, reduced YhaK was very sensitive to reactive oxygen species (ROS). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
WLKSRHTFSFADYYDPKNMGFGALRVINDDIVAPGTGFGTHPHRDMEIITYVLEGELTHRDSMGNKGVLK
RGDVQRMSAGTGIRHSEYNLSDTEPLRFLQIWILPDQRGLKPSYQQKRF
>gnl|CDD|239237 cd02911, arch_FMN, Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent flavin oxidoreductase (oxidored) FMN-binding family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN. The specific function of this group is unknown
PVALASMAGITDGDFCRKRADHAGLVFLGGYNLDERTIEAARKLVKRGRKEFLPDDPLEFIEGEIKALKD
SNVLVGVNVRSSSLEPLLNAAALVAKNAAILEINAHCRQPEMVEAGAGEALLKDPERLSEFIKALKETGV
PVSVKIRAGVDVDDEELARLIEKAGADIIHVDAMDPGNHADLKKIRDISTELFIIGNNSVTTIESAKEMF
SYGADMVSVARASLPENIEWLVE
>gnl|CDD|239238 cd02922, FCB2_FMN, Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit
HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFIS
PAALAKLAHPDGELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQPLFFQLYVNKDRTKTEELLKRA
EKLGAKAIFLTVDAPVLGKRERDERLKAEEAVSDGPAGKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRK
HTKLPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIRKHCPEVFDKIEVYVDGGV
RRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKAIQILKDEIETTMRLLGVTSLDQLGPS
>gnl|CDD|239239 cd02929, TMADH_HD_FMN, Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. TMADH is an iron-sulfur flavoprotein that catalyzes the oxidative demethylation of trimethylamine to form dimethylamine and formaldehyde. The protein forms a symetrical dimer with each subunit containing one 4Fe-4S cluster and one FMN cofactor. It contains a unique flavin, in the form of a 6-S-cysteinyl FMN which is bent by ~25 degrees along the N5-N10 axis of the flavin isoalloxazine ring. This modification of the conformation of the flavin is thought to facilitate catalysis.The closely related histamine dehydrogenase catalyzes oxidative deamination of histamine
RDPRHDILFEPIKIGPVTARNRFYQVPHCNGMGYRKPSAQAAMRGIKAEGGWGVVNTEQCSIHPSSDDTP
RISARLWDDGDIRNLAAMTDAVHKHGALAGIELWHGGAHAPNRESRETPLGPSQLPSEFPTGGPVQAREM
DKDDIKRVRRWYVDAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDT
KDAVGDDCAVATRFSVDELIGPGGIESEGEGVEFVEMLDELPDLWDVNVGDWANDGEDSRFYPEGHQEPY
IKFVKQVTSKPVVGVGRFTSPDKMVEVVKSGILDLIGAARPSIADPFLPKKIREGRIDDIRECIGCNICI
SGDEGGVPMRCTQNPTAGEE
>gnl|CDD|239240 cd02930, DCR_FMN, 2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction
LLSPLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVL
NSPRQAAGHRLITDAVHAEGGKIALQILHAGRYAYHPLCVAPSAIRAPINPFTPRELSEEEIEQTIEDFA
RCAALAREAGYDGVEIMGSEGYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYR
LSMLDLVEGGSTWEEVVALAKALEAAGADILNTGIGWHEARVPTIATSVPRGAFAWATAKLKRAVDIPVI
ASNRINTPEVAERLLADGDADMVSMARPFLADPDFVAKAAAGRADEINTCIACNQACLDHIFTGQRASCL
VNP
>gnl|CDD|239241 cd02931, ER_like_FMN, Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent reduction of carbon-carbon double bonds of several molecules, including nonactivated 2-enoates, alpha,beta-unsaturated aldehydes, cyclic ketones, and methylketones. ERs are similar to 2,4-dienoyl-CoA reductase from E. coli and to the old yellow enzyme from Saccharomyces cerevisiae
LFEPIKIGKVEIKNRFAMAPMGPLGLADNDGAFNQRGIDYYVERAKGGTGLIITGVTMVDNEIEQFPMPS
LPCPTYNPTAFIRTAKEMTERVHAYGTKIFLQLTAGFGRVCIPGFLGEDKPVAPSPIPNRWLPEITCREL
TTEEVETFVGKFGESAVIAKEAGFDGVEIHAVHEGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEE
IKARCGEDFPVSLRYSVKSYIKDLRQGALPGEEFQEKGRDLEEGLKAAKILEEAGYDALDVDAGSYDAWY
WNHPPMYQKKGMYLPYCKALKEVVDVPVIMAGRMEDPELASEAINEGIADMISLGRPLLADPDVVNKIRR
GRFKNIRPCISCHDGCLGRMALGGNLSCAVNP
>gnl|CDD|239242 cd02932, OYE_YqiM_FMN, Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs
LFTPLTLRGVTLKNRIVVSPMCQYSAEDGVATDWHLVHYGSRALGGAGLVIVEATAVSPEGRITPGDLGL
WNDEQIEALKRIVDFIHSQGAKIGIQLAHAGRKASTAPPWEGGGPLLPPGGGGWQVVAPSAIPFDEGWPT
PRELTREEIAEVVDAFVAAARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEV
VDAVRAVWPEDKPLFVRISATDWVEGGWDLEDSVELAKALKELGVDLIDVSSGGNSPAQKIPVGPGYQVP
FAERIRQEAGIPVIAVGLITDPEQAEAILESGRADLVALGRELLRNPYWPLHAAAE
>gnl|CDD|239243 cd02933, OYE_like_FMN, Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include 12-oxophytodienoate reductase, pentaerythritol tetranitrate reductase, morphinone reductase, and related enzymes
KLFSPLKLGNLTLKNRIVMAPLTRSRADPDGVPTDLMAEYYAQRASAGLIITEATQISPQGQGYPNTPGI
YTDEQVEGWKKVTDAVHAKGGKIFLQLWHVGRVSHPSLLPGGAPPVAPSAIAAEGKVFTPAGKVPYPTPR
ALTTEEIPGIVADFRQAARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVD
AVAEAIGADRVGIRLSPFGTFNDMGDSDPEATFSYLAKELNKRGLAYLHLVEPRVAGNPEDQPPDFLDFL
RKAFKGPLIAAGGYDAESAEAALADGKADLVAFGRPFIANPDLVERLKNGAPLNEYDR
>gnl|CDD|239244 cd02940, DHPD_FMN, Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN, and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue
DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSGRGQI
GFNNIELISEKPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGM
PERGMGAAVGQDPELVEEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVD
LDGTPPAPGVEGKTTYGGYSGPAVKPIALRAVSQIARAPEPGLPISGIGGIESWEDAAEFLLLGASVVQV
CTAVMNQGFTIVDDMCTGL
>gnl|CDD|239245 cd02947, TRX_family, TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins
EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFF
KNGKEVDRVVGADPKEELEEFLE
>gnl|CDD|239246 cd02948, TRX_NDPK, TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are fusion proteins which contain one redox active TRX domain containing a CXXC motif and three NDPK domains, and are characterized as intermediate chains (ICs) of axonemal outer arm dynein. Dyneins are molecular motors that generate force against microtubules to produce cellular movement, and are divided into two classes: axonemal and cytoplasmic. They are supramolecular complexes consisting of three protein groups classified according to size: dynein heavy, intermediate and light chains. Axonemal dyneins form two structures, the inner and outer arms, which are attached to doublet microtubules throughout the cilia and flagella. The human homolog is the sperm-specific Sptrx-2, presumed to be a component of the human sperm axoneme architecture. Included in this group is another human protein, TRX-like protein 2, a smaller fusion protein containing one TRX and one NDPK domain, which is also associated with microtubular structures. The other members of this group are hypothetical insect proteins containing a TRX domain and outer arm dynein light chains (14 and 16kDa) of Chlamydomonas reinhardtii. Using standard assays, the fusion proteins have shown no TRX enzymatic activity
QVEINNQEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELGDDLLHFATAEADTIDTLKRYRGK
CEPTFLFYKNGELVAVIRGANAPLLNKTITEL
>gnl|CDD|239247 cd02949, TRX_NTR, TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found only in oxygenic photosynthetic organisms containing both TRX and NTR domains. The TRX domain functions as a protein disulfide reductase via the reversible oxidation of an active center dithiol present in a CXXC motif, while the NTR domain functions as a reductant to oxidized TRX. The fusion protein is bifunctional, showing both TRX and NTR activities, but it is not an independent NTR/TRX system. In plants, the protein is found exclusively in shoots and mature leaves and is localized in the chloroplast. It is involved in plant protection against oxidative stress
GSYALRKLYHESDRLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPT
VQFFKDKELVKEISGVKMKSEYREFIE
>gnl|CDD|239248 cd02950, TxlA, TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport
VSLEQLAASSTPPEVALSNGKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFVMLNVDNPKWLPEID
RYRVDGIPHFVFLDREGNEEGQSIGLQPKQVLAQNLDALVAGEPLPYANAVGQTSELKSPKNPSSQDDPR
SH
>gnl|CDD|239249 cd02951, SoxW, SoxW family; SoxW is a bacterial periplasmic TRX, containing a redox active CXXC motif, encoded by a genetic locus (sox operon) involved in thiosulfate oxidation. Sulfur bacteria oxidize sulfur compounds to provide reducing equivalents for carbon dioxide fixation during autotrophic growth and the respiratory electron transport chain. It is unclear what the role of SoxW is, since it has been found to be dispensable in the oxidation of thiosulfate to sulfate. SoxW is specifically kept in the reduced state by SoxV, which is essential in thiosulfate oxidation
DLYEDLAEAAADGKKPLLLLFSQPGCPYCDKLKRDYLNDPAVQAYIRAHFVVVYINIDGDKEVTDFDGEA
LSEKELARKYRVRFTPTVIFLDPEGGKEIARLPGYLPPDEFLAYLEYVQEKAYKK
>gnl|CDD|239250 cd02952, TRP14_like, Human TRX-related protein 14 (TRP14)-like family; composed of proteins similar to TRP14, a 14kD cytosolic protein that shows disulfide reductase activity in vitro with a different substrate specificity compared with another human cytosolic protein, TRX1. TRP14 catalyzes the reduction of small disulfide-containing peptides but does not reduce disulfides of ribonucleotide reductase, peroxiredoxin and methionine sulfoxide reductase, which are TRX1 substrates. TRP14 also plays a role in tumor necrosis factor (TNF)-alpha signaling pathways, distinct from that of TRX1. Its depletion promoted TNF-alpha induced activation of c-Jun N-terminal kinase and mitogen-activated protein kinases
PLETAVRGYEEFLKLLKSHEGKPIFILFYGDKDPDGQSWCPDCVKAEPVVREALKAAPEDCVFIYCDVGD
RPYWRDPNNPFRTDPKLTTGVPTLLRWKTPQRLVEDECLQADLVEMFFE
>gnl|CDD|239251 cd02953, DsbDgamma, DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes
EAALAQALAQGKPVFVDFTADWCVTCKVNEKVVFSDPEVQAALKKDVVLLRADWTKNDPEITALLKRFGV
FGPPTYLFYGPGGEPEPLRLPGFLTADEFLEALE
>gnl|CDD|239252 cd02954, DIM1, Dim1 family; Dim1 is also referred to as U5 small nuclear ribonucleoprotein particle (snRNP)-specific 15kD protein. It is a component of U5 snRNP, which pre-assembles with U4/U6 snRNPs to form a [U4/U6:U5] tri-snRNP complex required for pre-mRNA splicing. Dim1 interacts with multiple splicing-associated proteins, suggesting that it functions at multiple control points in the splicing of pre-mRNA as part of a large spliceosomal complex involving many protein-protein interactions. U5 snRNP contains seven core proteins (common to all snRNPs) and nine U5-specific proteins, one of which is Dim1. Dim1 adopts a thioredoxin fold but does not contain the redox active CXXC motif. It is essential for G2/M phase transition, as a consequence to its role in pre-mRNA splicing
SGWAVDQAILSEEEKVVVIRFGRDWDPVCMQMDEVLAKIAEDVSNFAVIYLVDIDEVPDFNKMYELYDPP
TVMFFFRNKHMKIDLGTGNNNKINWVFEDKQEFIDIIETIYRGA
>gnl|CDD|239253 cd02955, SSP411, TRX domain, SSP411 protein family; members of this family are highly conserved proteins present in eukaryotes, bacteria and archaea, about 600-800 amino acids in length, which contain a TRX domain with a redox active CXXC motif. The human/rat protein, called SSP411, is specifically expressed in the testis in an age-dependent manner. The SSP411 mRNA is increased during spermiogenesis and is localized in round and elongated spermatids, suggesting a function in fertility regulation
YPWGEEAFEKARREDKPIFLSIGYSTCHWCHVMEHESFEDEEVAAILNENFVPIKVDREERPDVDKIYMN
AAQAMTGQGGWPLNVFLTPDLKPFFGGTYFPPEDRYGRPGFKTVLEKIRELWRE
>gnl|CDD|239254 cd02956, ybbN, ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria
QNFQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTV
YLFAAGQPVDGFQGAQPEEQLRQMLD
>gnl|CDD|239255 cd02957, Phd_like, Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as cytosolic regulators of G protein functions. Phd and PhLPs specifically bind G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane and impeding G protein-mediated signal transduction by inhibiting the formation of a functional G protein trimer (G protein alphabetagamma). Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain. Also included in this family is a PhLP characterized as a viral inhibitor of apoptosis (IAP)-associated factor, named VIAF, that functions in caspase activation during apoptosis
KGFGEVREISSKEFLEEVTKASKGTRVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAEKAFLVN
YLDIKVLPTLLVYKNGELIDNIVGFEELGGDDFTTEDLEKFLA
>gnl|CDD|239256 cd02958, UAS, UAS family; UAS is a domain of unknown function. Most members of this family are uncharacterized proteins with similarity to FAS-associated factor 1 (FAF1) and ETEA because of the presence of a UAS domain N-terminal to a ubiquitin-associated UBX domain. FAF1 is a longer protein, compared to the other members of this family, having additional N-terminal domains, a ubiquitin-associated UBA domain and a nuclear targeting domain. FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. ETEA is the protein product of a highly expressed gene in T-cells and eosinophils of atopic dermatitis patients. The presence of the ubiquitin-associated UBX domain in the proteins of this family suggests the possibility of their involvement in ubiquitination. Recently, FAF1 has been shown to interact with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway. Some members of this family are uncharacterized proteins containing only a UAS domain
FFQGSFEDAKQEAKSEKKWLLVYLQSEDEFDSQVLNRDLWSNESVKEFIRENFIFWQCDIDSSEGQRFLQ
SYKVDKYPHIAIIDPRTGEVLKVWSGNITPEDLLSQLIEFLEEF
>gnl|CDD|239257 cd02959, ERp19, Endoplasmic reticulum protein 19 (ERp19) family; ERp19 is also known as ERp18, a protein located in the ER containing one redox active TRX domain. Denaturation studies indicate that the reduced form is more stable than the oxidized form, suggesting that the protein is involved in disulfide bond formation. In vitro, ERp19 has been shown to possess thiol-disulfide oxidase activity which is dependent on the presence of both active site cysteines. Although described as protein disulfide isomerase (PDI)-like, the protein does not complement for PDI activity. ERp19 shows a wide tissue distribution but is most abundant in liver, testis, heart and kidney
DHIHWVTLEDGIKEAKDSGKPLMLLIHKTWCGACKALKPKFAESKEISELSHNFVMVNLEDDEEPKDEEF
SPDGGYIPRILFLDPSGDVHPEIINKKGNPNYKYFYSSAAQVTESMK
>gnl|CDD|239258 cd02960, AGR, Anterior Gradient (AGR) family; members of this family are similar to secreted proteins encoded by the cement gland-specific genes XAG-1 and XAG-2, expressed in the anterior region of dorsal ectoderm of Xenopus. They are implicated in the formation of the cement gland and the induction of forebrain fate. The human homologs, hAG-2 and hAG-3, are secreted proteins associated with estrogen-positive breast tumors. Yeast two-hybrid studies identified the metastasis-associated C4.4a protein and dystroglycan as binding partners, indicating possible roles in the development and progression of breast cancer. hAG-2 has also been implicated in prostate cancer. Its gene was cloned as an androgen-inducible gene and it was shown to be overexpressed in prostate cancer cells at the mRNA and protein levels. AGR proteins contain one conserved cysteine corresponding to the first cysteine in the CXXC motif of TRX. They show high sequence similarity to ERp19
GWGDDIIWVQTYEEGLYKAKKSNKPLMVIHHLEDCPHSQALKKAFAEHKEIQKLAQEDFIMLNLVHETTD
KNLSPDGQYVPRIMFVDPSLTVRADITGRYSNRLYTYEPADIPLLIENMKKALKLLKTEL
>gnl|CDD|239259 cd02961, PDI_a_family, Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29
VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANNDLCSEYGVR
GYPTIKLFPNGSKEPVKYEGPRTLESLVEFI
>gnl|CDD|239260 cd02962, TMX2, TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related transmembrane protein, identified and characterized through the cloning of its cDNA from a human fetal library. It contains a TRX domain but the redox active CXXC motif is replaced with SXXC. Sequence analysis predicts that TMX2 may be a Type I membrane protein, with its C-terminal half protruding on the luminal side of the endoplasmic reticulum (ER). In addition to the TRX domain, transmembrane region and ER-retention signal, TMX2 also contains a Myb DNA-binding domain repeat signature and a dileucine motif in the tail
DIRLGLLYLLLCIVVYLLAPQPLYMGPEHIKYFTPKTLEEELERDKRVTWLVEFFTTWSPECVNFAPVFA
ELSLKYNNNNLKFGKIDIGRFPNVAEKFRVSTSPLSKQLPTIILFQGGKEVARRPYYNDSKGRAVPFTFS
KENVIRHFDLDR
>gnl|CDD|239261 cd02963, TRX_DnaJ, TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of about 500-800 amino acids, containing an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40 kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network
DSFDYKYSLTFSQYENEIVPKSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERR
LARKLGAHSVPAIVGIINGQVTFYHDSSFTKQHVVDFVRKL
>gnl|CDD|239262 cd02964, TryX_like_family, Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX
LFLLDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEIVFVSRDRSEESFNEY
FSEMPPWLAVPFEDEELRELLEKQFKVEGIPTLVVLKPDGDVVTTNARDEVEEDPGACAFPW
>gnl|CDD|239263 cd02965, HyaE, HyaE family; HyaE is also called HupG and HoxO. They are proteins serving a critical role in the assembly of multimeric [NiFe] hydrogenases, the enzymes that catalyze the oxidation of molecular hydrogen to enable microorganisms to utilize hydrogen as the sole energy source. The E. coli HyaE protein is a chaperone that specifically interacts with the twin-arginine translocation (Tat) signal peptide of the [NiFe] hydrogenase-1 beta subunit precursor. Tat signal peptides target precursor proteins to the Tat protein export system, which facilitates the transport of fully folded proteins across the inner membrane. HyaE may be involved in regulating the traffic of [NiFe] hydrogenase-1 on the Tat transport pathway
PLVARLQTRHGWPRVDAATLDDWLAAGGDLVLLLAGDPVRFPEVLDVAVVLPELLKAFPGRFRAAVVGRA
DEQALAARFGVLRTPALLFFRDGRYVGVLAGIRDWDEYVAR
>gnl|CDD|239264 cd02966, TlpA_like_family, TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases
DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAVKA
FLKKYGITFPVLLDPDGELAKAYGVRGLPTTFLIDRDGRIRARHVG
>gnl|CDD|239265 cd02967, mauD, Methylamine utilization (mau) D family; mauD protein is the translation product of the mauD gene found in methylotrophic bacteria, which are able to use methylamine as a sole carbon source and a nitrogen source. mauD is an essential accessory protein for the biosynthesis of methylamine dehydrogenase (MADH), the enzyme that catalyzes the oxidation of methylamine and other primary amines. MADH possesses an alpha2beta2 subunit structure; the alpha subunit is also referred to as the large subunit. Each beta (small) subunit contains a tryptophan tryptophylquinone (TTQ) prosthetic group. Accessory proteins are essential for the proper transport of MADH to the periplasm, TTQ synthesis and the formation of several structural disulfide bonds. Bacterial mutants containing an insertion on the mauD gene were unable to grow on methylamine as a sole carbon source, were found to lack the MADH small subunit and had decreased amounts of the MADH large subunit
PTFDLTTIDGAPVRIGGISPGRPTLLFFLSPTCPVCKKLLPVIRSIARAEADWLDVVLASDGEKAEHQRF
LKKHGLEAFPYVLSAELGMAYQVSKLPYAVLLDEAGVIAAKGLV
>gnl|CDD|239266 cd02968, SCO, SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II
IGPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGGDDVQVVFISVDPE
RDTPEVLKAYAKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPEDDGDYLVDHSAAIYLVDPDGKLVRYY
GG
>gnl|CDD|239267 cd02969, PRX_like1, Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF
GSPAPDFSLPDTDGKTYSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIE
AYPEDSPENMKAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYRGRIDDSRPGNDPPVT
GRDLRAALDALLAGKPVPVPQTPSIGCSIKW
>gnl|CDD|239268 cd02970, PRX_like2, Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins
TAPDFELPDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESPEK
LEAFDKGKFLPFPVYADPDRKLYRALGLVRSLPWSNTPRALWKNAAIGFRGNDEGDGLQLPGVFVIGPDG
TILFAHVDR
>gnl|CDD|239269 cd02971, PRX_family, Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP), based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either TRX, glutathione, trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis, common to all PRXs, is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction, the resolution of the intermediate, distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid, phosphorylation and limited proteolysis
KAPDFTLPATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSH
KAWAEKEGGLNFPLLSDPDGEFAKAYGVLIEKSAGGGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL
>gnl|CDD|239270 cd02972, DsbA_family, DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) S-transferase kappa (GSTK), 2-hydroxychromene-2-carboxylate (HCCA) isomerase, an oxidoreductase (FrnE) presumed to be involved in frenolicin biosynthesis, a 27-kDa outer membrane protein, and similar proteins. Members of this family contain a redox active CXXC motif (except GSTK and HCCA isomerase) imbedded in a TRX fold, and an alpha helical insert of about 75 residues (shorter in DsbC and DsbG) relative to TRX. DsbA is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm. DsbC and DsbG function as protein disulfide isomerases and chaperones to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins
IVEFFDPLCPYCYLFEPELEKLLYADDGGVRVVYRPFPLLGGMPPNSLAAARAALAAAAQGKFEALHEAL
ADTALARALGVTGTPTFVVNGEKYSGAG
>gnl|CDD|239271 cd02973, TRX_GRX_like, Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins that show similarity to both TRX and GRX, including the C-terminal TRX-fold subdomain of Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). All members contain a redox-active CXXC motif and may function as PDOs. The archaeal proteins Mj0307 and Mt807 show structures more similar to GRX, but activities more similar to TRX. Some members of the family are similar to PfPDO in that they contain a second CXXC motif located in a second TRX-fold subdomain at the N-terminus; the superimposable N- and C-terminal TRX subdomains form a compact structure. PfPDO is postulated to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI). The C-terminal CXXC motif of PfPDO is required for its oxidase, reductase and isomerase activities. Also included in the family is the C-terminal TRX-fold subdomain of the N-terminal domain (NTD) of bacterial AhpF, which has a similar fold as PfPDO with two TRX-fold subdomains but without the second CXXC motif
VNIEVFVSPTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKVEFVGR
>gnl|CDD|239272 cd02974, AhpF_NTD_N, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD forming two contiguous TRX-fold subdomain similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -_ catalytic core of AhpF -_ NTD of AhpF -_ AhpC -_ peroxide substrates. The N-terminal TRX-fold subdomain of AhpF NTD is redox inactive, but is proposed to contain an important residue that aids in the catalytic function of the redox-active CXXC motif contained in the C-terminal TRX-fold subdomain
MLDANLKQQLKAYLERLENPVELVASLDDSEKSAELLELLEEIASLSDKITLEEDNDDERKPSFSINRPG
EDTGIRFAGIPMGHEFTSLVLALL
>gnl|CDD|239273 cd02975, PfPDO_like_N, Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold subdomain; composed of proteins with similarity to PfPDO, a redox active thermostable protein believed to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI), which are both involved in oxidative protein folding. PfPDO contains two redox active CXXC motifs in two contiguous TRX-fold subdomains. The active site in the N-terminal TRX-fold subdomain is required for isomerase but not for reductase activity of PfPDO. The exclusive presence of PfPDO-like proteins in extremophiles may suggest that they have a special role in adaptation to extreme conditions
GLLSDEDRKALKEEFFKEMKNPVDLVVFSSKEGCQYCEVTKQLLEELSELSDKLKLEIYDFDEDKEKAEK
YGVERVPTTIFLQDGGKDGGIRYYGLPAGYEFASLIEDIVRVS
>gnl|CDD|239274 cd02976, NrdH, NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein
EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDEDPEALEELKKLNGYRSVPVVVIGDEHLSGFRPDKLR
ALL
>gnl|CDD|239275 cd02977, ArsC_family, Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins including the transcriptional regulator, Spx. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione (GSH) via glutaredoxin (GRX), through a single catalytic cysteine. This family of predominantly bacterial enzymes is unrelated to two other families of arsenate reductases which show similarity to low-molecular-weight acid phosphatases and phosphotyrosyl phosphatases. Spx is a general regulator that exerts negative and positive control over transcription initiation by binding to the C-terminal domain of the alpha subunit of RNA polymerase
ITIYGNPNCSTSRKALAWLEEHGIEYEFIDYLKEPPTKEELKELLAKLGLGVEDLFNTRGTPYRKLGLAD
KDELSDEEALELMAEHPKLIKRPIVVDGDRLLVGF
>gnl|CDD|239276 cd02978, KaiB_like, KaiB-like family; composed of the circadian clock proteins, KaiB and the N-terminal KaiB-like sensory domain of SasA. KaiB is an essential protein in maintaining circadian rhythm. It was originally discovered from the cyanobacterium Synechococcus as part of the circadian clock gene cluster, kaiABC. KaiB attenuates KaiA-enhanced KaiC autokinase activity by interacting with KaiA-KaiC complexes in a circadian fashion. KaiB is membrane-associated as well as cytosolic. The amount of membrane-associated protein peaks in the evening (at circadian time (CT) 12-16) while the cytosolic form peaks later (at CT 20). The rhythmic localization of KaiB may function in regulating the formation of Kai complexes. SasA is a sensory histidine kinase which associates with KaiC. Although it is not an essential oscillator component, it is important in enhancing kaiABC expression and is important in metabolic growth control under day/night cycle conditions. SasA contains an N-terminal sensory domain with a TRX fold which is involved in the SasA-KaiC interaction. This domain shows high sequence similarity with KaiB. However, the KaiB structure does not show a classical TRX fold. The N-terminal half of KaiB shares the same beta-alpha-beta topology as TRX, but the topology of its C-terminal half diverges
RYVLRLYVAGRTPKSERALQNLKRILEELLGGPYELEVIDVLKQPQLAEEDKIVATPTLVKVLPPPRRRL
IG
>gnl|CDD|239277 cd02979, PHOX_C, FAD-dependent Phenol hydoxylase (PHOX) family, C-terminal TRX-fold domain; composed of proteins similar to PHOX from the aerobic topsoil yeast Trichosporon cutaneum. PHOX is a flavoprotein monooxygenase that catalyzes the hydroxylation of phenol and simple phenol derivatives in the ortho position with the consumption of NADPH and oxygen. This is the first step in the biodegradation and detoxification of phenolic compounds. PHOX contains three domains. The substrate and FAD/NAD(P) binding sites are contained in the first two domains, which adopt a complicated folding pattern. The third or C-terminal domain contains a TRX fold and is involved in dimerization. The functional unit of PHOX is a dimer, although active tetramers of the recombinant enzyme can be isolated when overproduced in bacteria
GRRFPSAPVVRQADALPVHLGHRLPADGRFRIYVFAGDIAPAQQKSRLTQLCDALDSPDSFPLRYTPRGA
DPDSVFDVVTIHAAPRREIELLDLPAVLRPFGEKKGWDYEKIYADDDSYHEGHGDAYEKYGIDPERGAVV
VVRPDQYVALVGPLDDVEALEAYFAGF
>gnl|CDD|239278 cd02980, TRX_Fd_family, Thioredoxin (TRX)-like [2Fe-2S] Ferredoxin (Fd) family; composed of [2Fe-2S] Fds with a TRX fold (TRX-like Fds) and proteins containing domains similar to TRX-like Fd including formate dehydrogenases, NAD-reducing hydrogenases and the subunit E of NADH:ubiquinone oxidoreductase (NuoE). TRX-like Fds are soluble low-potential electron carriers containing a single [2Fe-2S] cluster. The exact role of TRX-like Fd is still unclear. It has been suggested that it may be involved in nitrogen fixation. Its homologous domains in large redox enzymes (such as Nuo and hydrogenases) function as electron carriers
HHILVCTGTACGLRGAEELLEALEKELGIRGGDGRVTVERVGCLGACGLAPVVVVYPDGVWYGRVTPEDV
EEIVEEL
>gnl|CDD|239279 cd02981, PDI_b_family, Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI, calsequestrin and other PDI-related proteins like ERp72, ERp57, ERp44 and PDIR. PDI, ERp57 (or ERp60), ERp72 and PDIR are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive b domains are implicated in substrate recognition
VKELTSKEELEKFLDKDDVVVVGFFKDEESEEYKTFEKVAESLRDDYGFGHTSDKEVAKKLKVKPGSVVL
FKPFEEEPVEYDGEFTEESLVEFIKDN
>gnl|CDD|239280 cd02982, PDI_b'_family, Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI, calsequestrin and other PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5 and PDIR. PDI, ERp57, ERp72, P5 and PDIR are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive domains are implicated in substrate recognition with the b' domain serving as the primary substrate binding site. Only the b' domain is necessary for the binding of small peptide substrates. In addition to the b' domain, other domains are required for the binding of larger polypeptide substrates. The b' domain is also implicated in chaperone activity
NAETFFNYEESGKPLLVLFYNKDDSESEELRERFKEVAKKFKGKLLFVVVDADDFGRHLEYFGLKEEDLP
VIAIINLSDGKKYLMPEEELTAESLEEFVEDFL
>gnl|CDD|239281 cd02983, P5_C, P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI)-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. The C-terminal domain is likely involved in substrate binding, similar to the b and b' domains of PDI
APEIIELTSEDVFEETCEEKQLCIIAFLPHILDCQASCRNKYLEILKSVAEKFKKKPWGWLWTEAGAQLD
LEEALNIGGFGYPAMVAINFRKMKFATLKGSFSEDGINEFLRELSYGRGPTLPVNGLPKV
>gnl|CDD|239282 cd02984, TRX_PICOT, TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli
SEEEFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVP
TFVFFRNGTIVDRVSGADPKELAKKVE
>gnl|CDD|239283 cd02985, TRX_CDSP32, TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed of two TRX domains, a C-terminal TRX domain which contains a redox active CXXC motif and an N-terminal TRX-like domain which contains an SXXS sequence instead of the redox active motif. CDSP32 is a stress-inducible TRX, i.e., it acts as a TRX by reducing protein disulfides and is induced by environmental and oxidative stress conditions. It plays a critical role in plastid defense against oxidative damage, a role related to its function as a physiological electron donor to BAS1, a plastidic 2-cys peroxiredoxin. Plants lacking CDSP32 exhibit decreased photosystem II photochemical efficiencies and chlorophyll retention compared to WT controls, as well as an increased proportion of BAS1 in its overoxidized monomeric form
HSVEELDEALKKAKGRLVVLEFALKHSGPSVKIYPTMVKLSRTCNDVVFLLVNGDENDSTMELCRREKII
EVPHFLFYKDGEKIHEEEGIGPDELIGDVLYYG
>gnl|CDD|239284 cd02986, DLP, Dim1 family, Dim1-like protein (DLP) subfamily; DLP is a novel protein which shares 38% sequence identity to Dim1. Like Dim1, it is also implicated in pre-mRNA splicing and cell cycle progression. DLP is located in the nucleus and has been shown to interact with the U5 small nuclear ribonucleoprotein particle (snRNP)-specific 102kD protein (or Prp6). Dim1 protein, also known as U5 snRNP-specific 15kD protein is a component of U5 snRNP, which pre-assembles with U4/U6 snRNPs to form a [U4/U6:U5] tri-snRNP complex required for pre-mRNA splicing. Dim1 adopts a thioredoxin fold but does not contain the redox active CXXC motif
SKKEVDQAIKSTAEKVLVLRFGRDEDAVCLQLDDILSKTSHDLSKMASIYLVDVDKVPVYTQYFDISYIP
STIFFFNGQHMKVDYGSPDHTKFVGSFKTKQDFIDLIEVIYRGA
>gnl|CDD|239285 cd02987, Phd_like_Phd, Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein functions. It specifically binds G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane. This impedes the formation of a functional G protein trimer (G protein alphabetagamma), thereby inhibiting G protein-mediated signal transduction. Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain
EGSGTNTGPKGVINDWRKFKQLKESEQEDDDDDEDKEEFLQQYREQRMQEMHAKLPFGRRFGKVYELDSG
EQFLDAIDKEGKDTTVVVHIYEPGIPGCAALNSSLLCLAAEYPAVKFCKIRASATGASDEFDTDALPALL
VYKGGELIGNFVRVTEDLGEDFDAEDLESFLVEYG
>gnl|CDD|239286 cd02988, Phd_like_VIAF, Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) subfamily; VIAF is a Phd-like protein that functions in caspase activation during apoptosis. It was identified as an IAP binding protein through a screen of a human B-cell library using a prototype IAP. VIAF lacks a consensus IAP binding motif and while it does not function as an IAP antagonist, it still plays a regulatory role in the complete activation of caspases. VIAF itself is a substrate for IAP-mediated ubiquitination, suggesting that it may be a target of IAPs in the prevention of cell death. The similarity of VIAF to Phd points to a potential role distinct from apoptosis regulation. Phd functions as a cytosolic regulator of G protein by specifically binding to G protein betagamma (Gbg)-subunits. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain
TEWNDILRKKGILPPKPPSPKEEEEEALELAIQEAHENALEKKLLDELDEELDEEEDDRFLEEYRRKRLA
EMKALAEKSKFGEVYEISKPDYVREVTEASKDTWVVVHLYKDGIPLCRLLNQHLSELARKFPDTKFVKII
STQCIPNYPDKNLPTILVYRNGDIVKQFIGLLEFGGMNTTMEDLEWLLVQVG
>gnl|CDD|239287 cd02989, Phd_like_TxnDC9, Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; composed of predominantly uncharacterized eukaryotic proteins, containing a TRX-like domain without the redox active CXXC motif. The gene name for the human protein is TxnDC9. The two characterized members are described as Phd-like proteins, PLP1 of Saccharomyces cerevisiae and PhLP3 of Dictyostelium discoideum. Gene disruption experiments show that both PLP1 and PhLP3 are non-essential proteins. Unlike Phd and most Phd-like proteins, members of this group do not contain the Phd N-terminal helical domain which is implicated in binding to the G protein betagamma subunit
KGHGKYREVSDEKEFFEIVKSSERVVCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKAPFLVEK
LNIKVLPTVILFKNGKTVDRIVGFEELGGKDDFSTETLEKRLA
>gnl|CDD|239288 cd02990, UAS_FAF1, UAS family, FAS-associated factor 1 (FAF1) subfamily; FAF1 contains a UAS domain of unknown function N-terminal to a ubiquitin-associated UBX domain. FAF1 also contains ubiquitin-associated UBA and nuclear targeting domains, N-terminal to the UAS domain. FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. It is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kB (NF-kB) by interfering with the nuclear translocation of the p65 subunit. FAF1 also interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway
FFIGSLEAAFQEACYRKARDRKLLAIYLHHDESVLSNVFCSQLLCAESIVQYLSQNFITWGWDMTKESNK
ARFLSSCTRHFGSVAAQTIRNIKTDQLPAILIIMGKRSSNEVLNVIQGNTGVDELLMRLIEAMEMF
>gnl|CDD|239289 cd02991, UAS_ETEA, UAS family, ETEA subfamily; composed of proteins similar to human ETEA protein, the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. ETEA shows homology to Fas-associated factor 1 (FAF1); both containing UAS and UBX (ubiquitin-associated) domains. Compared to FAF1, however, ETEA lacks the ubiquitin-associated UBA domain and a nuclear targeting domain. The function of ETEA is still unknown. A yeast two-hybrid assay showed that it can interact with Fas. Because of its homology to FAF1, it is postulated that ETEA could be involved in modulating Fas-mediated apoptosis of T-cells and eosinophils of atopic dermatitis patients, making them more resistant to apoptosis
FYQGTYSQALNDAKQELRFLLVYLHGDDHQDTDEFCRNTLCAPEVIEYINTRMLFWACSVAKPEGYRVSQ
ALRERTYPFLAMIMLKDNRMTIVGRLEGLIQPEDLINRLTFIMDAN
>gnl|CDD|239290 cd02992, PDI_a_QSOX, PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein containing an N-terminal redox active TRX domain, similar to that of PDI, and a small C-terminal flavin adenine dinucleotide (FAD)-binding domain homologous to the yeast ERV1p protein. QSOX oxidizes thiol groups to disulfides like PDI, however, unlike PDI, this oxidation is accompanied by the reduction of oxygen to hydrogen peroxide. QSOX is localized in high concentrations in cells with heavy secretory load and prefers peptides and proteins as substrates, not monothiols like glutathione. Inside the cell, QSOX is found in the endoplasmic reticulum and Golgi. The flow of reducing equivalents in a QSOX-catalyzed reaction goes from the dithiol substrate -_ dithiol of the QSOX TRX domain -_ dithiols of the QSOX ERV1p domain -_ FAD -_ oxygen
DPVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDCADEENVAL
CRDFGVTGYPTLRYFPPFSKEATDGLKQEGPERDVNELREALIL
>gnl|CDD|239291 cd02993, PDI_a_APS_reductase, PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -_ C-terminal TRX domain -_ N-terminal reductase domain -_ APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly
EAVVTLSRAEIEALAKGERRNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSNVKVAKFNADGEQREFA
KEELQLKSFPTILFFPKNSRQPIKYPSEQRDVDSLLMFV
>gnl|CDD|239292 cd02994, PDI_a_TMX, PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC
SNVVELTDSNWTLVLEGEWMIEFYAPWCPACQQLQPEWEEFADWSDDLGINVAKVDVTQEPGLSGRFFVT
ALPTIYHAKDGVFRRYQGPRDKEDLISFIEE
>gnl|CDD|239293 cd02995, PDI_a_PDI_a'_C, PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones
PVKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATANDVPSEFV
VDGFPTILFFPAGDKSNPIKYEGDRTLEDLIKFI
>gnl|CDD|239294 cd02996, PDI_a_ERp44, PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol
SEIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAGKVVWGKVDCDKESDI
ADRYRINKYPTLKLFRNGMMMKREYRGQRSVEALAEFV
>gnl|CDD|239295 cd02997, PDI_a_PDIR, PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity
DVVHLTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVLAAVDCTKPEHDALKEE
YNVKGFPTFKYFENGKFVEKYEGERTAEDIIEFM
>gnl|CDD|239296 cd02998, PDI_a_ERp38, PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica
NVVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADEANKDLAKK
YGVSGFPTLKFFPKGSTEPVKYEGGRDLEDLVKFV
>gnl|CDD|239297 cd02999, PDI_a_ERp44_like, PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER
PPEEVLNIALDLMAFNREDYTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSLLSRYGV
VGFPTILLFNSTPRVRYNGTRTLDSLAAFY
>gnl|CDD|239298 cd03000, PDI_a_TMX3, PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase
LVLDLDDSFKDVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDATAYSSIASEFGV
RGYPTIKLLKGDLAYNYRGPRTKDDIVEFANRVA
>gnl|CDD|239299 cd03001, PDI_a_P5, PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain
DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGV
RGFPTIKVFGAGKNSPQDYQGGRTAKAIVSAAL
>gnl|CDD|239300 cd03002, PDI_a_MPD1_like, PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity
PVYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKNKPLCGKY
GVQGFPTLKVFRPPKKASKHAVEDYNGERSAKAIVDFVL
>gnl|CDD|239301 cd03003, PDI_a_ERdj5_N, PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation
PEIVTLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGV
NSYPSLYVFPSGMNPEKYYGDRSKESLVKFA
>gnl|CDD|239302 cd03004, PDI_a_ERdj5_C, PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus
PSVITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQAN
IRAYPTIRLYPGNASKYHSYNGWHRDADSILEFI
>gnl|CDD|239303 cd03005, PDI_a_ERp46, PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident protein containing three redox active TRX domains. Yeast complementation studies show that ERp46 can substitute for protein disulfide isomerase (PDI) function in vivo. It has been detected in many tissues, however, transcript and protein levels do not correlate in all tissues, suggesting regulation at a posttranscriptional level. An identical protein, named endoPDI, has been identified as an endothelial PDI that is highly expressed in the endothelium of tumors and hypoxic lesions. It has a protective effect on cells exposed to hypoxia
GVLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRELCSEFQ
VRGYPTLLLFKDGEKVDKYKGTRDLDSLKEFV
>gnl|CDD|239304 cd03006, PDI_a_EFP1_N, PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase (ThOX), also called Duox. ThOX proteins are responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones. EFP1 was isolated through a yeast two-hybrid method using the EF-hand fragment of dog Duox1 as a bait. It could be one of the partners in the assembly of a multiprotein complex constituting the thyroid hydrogen peroxide generating system. EFP1 contains two TRX domains related to the redox active TRX domains of protein disulfide isomerase (PDI). This subfamily is composed of the N-terminal TRX domain of EFP1, which contains a CXXS sequence in place of the typical CXXC motif, similar to ERp44. The CXXS motif allows the formation of stable mixed disulfides, crucial for the ER-retention function of ERp44
PVPFFSQRSPVLDFYKGQLDYAEELRTDAEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQVLFVAINCW
WPQGKCRKQKHFFYFPVIHLYYRSRGPIEYKGPMRAPYMEKFV
>gnl|CDD|239305 cd03007, PDI_a_ERp29_N, PDIa family, endoplasmic reticulum protein 29 (ERp29) subfamily; ERp29 is a ubiquitous ER-resident protein expressed in high levels in secretory cells. It forms homodimers and higher oligomers in vitro and in vivo. It contains a redox inactive TRX-like domain at the N-terminus, which is homologous to the redox active TRX (a) domains of PDI, and a C-terminal helical domain similar to the C-terminal domain of P5. The expression profile of ERp29 suggests a role in secretory protein production distinct from that of PDI. It has also been identified as a member of the thyroglobulin folding complex. The Drosophila homolog, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase
KGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAESSASATDDLLVAEVGIKDYGEKLNMEL
GERYKLDKESYPVIYLFHGGDFENPVPYSGADVTVDALQRFLKGNT
>gnl|CDD|239306 cd03008, TryX_like_RdCVF, Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is a thioredoxin (TRX)-like protein specifically expressed in photoreceptors. RdCVF was isolated and identified as a factor that supports cone survival in retinal cultures. Cone photoreceptor loss is responsible for the visual handicap resulting from the inherited disease, retinitis pigmentosa. RdCVF shows 33% similarity to TRX but does not exhibit any detectable thiol oxidoreductase activity
RVLIKNNSDRDELDTEREIVARLENRVLLLFFGAVVSPQCQLFAPKLKDFFVRLTDEFYVDRSAQLALVY
VSMDQSEQQQESFLKDMPKKWLFLPFEDEFRRELEAQFSVEELPTVVVLKPDGDVLAANAVDEILRLGPA
CFRNWQ
>gnl|CDD|239307 cd03009, TryX_like_TryX_NRX, Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors
DFLLRNDGGKVPVSSLEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKESGKNFEIVFISWDRDEESFND
YFSKMPWLAVPFSDRERRSRLNRTFKIEGIPTLIILDADGEVVTTDARELVLEYGADAFPF
>gnl|CDD|239308 cd03010, TlpA_like_DsbE, TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c
KPAPAFSLPALPGPDKTLTSADLKGKPYLLNVWASWCAPCREEHPVLMALARQGRVPIYGINYKDNPENA
LAWLARHGNPYAAVGFDPDGRVGIDLGVYGVPETFLIDGDGIIRYKHVGPLTPEVWE
>gnl|CDD|239309 cd03011, TlpA_like_ScsD_MtbDsbE, TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c
PLFTATTLDGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADYPVVSVALRSGDDGAVARFMQK
KGYGFPVINDPDGVISARWGVSVTPAIVIVDPGGIVFVTTGVTSEWGLRLRLW
>gnl|CDD|239310 cd03012, TlpA_like_DipZ_like, TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3
PEFEGILQWLNTDKPLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIGVHSPEFAFE
RDLANVKSAVLRYGITYPVANDNDYATWRAYGNQYWPALYLIDPTGNVRHVHFGEG
>gnl|CDD|239311 cd03013, PRX5_like, Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs
VGDKLPNVTLFEYVPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVIC
VSVNDPFVMKAWGKALGAKDKIRFLADGNGEFTKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVEE
DPGDVEVSSAENVLK
>gnl|CDD|239312 cd03014, PRX_Atyp2cys, Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing peroxidatic and resolving cysteines, similar to the homodimeric thiol specific antioxidant (TSA) protein also known as TRX-dependent thiol peroxidase (Tpx). Tpx is a bacterial periplasmic peroxidase which differs from other PRXs in that it shows substrate specificity toward alkyl hydroperoxides over hydrogen peroxide. As with all other PRXs, the peroxidatic cysteine (N-terminal) of Tpx is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Tpx is able to resolve this intermediate by forming an intramolecular disulfide bond with a conserved C-terminal cysteine (the resolving cysteine), which can then be reduced by thioredoxin. This differs from the typical 2-cys PRX which resolves the oxidized cysteine by forming an intermolecular disulfide bond with the resolving cysteine from the other subunit of the homodimer. Atypical 2-cys PRX homodimers have a loop-based interface (A-type for alternate), in contrast with the B-type interface of typical 2-cys and 1-cys PRXs
KVGDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLDNTVVLTISADLPF
AQKRWCGAEGVDNVTTLSDFRDHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYVELVPEITDEPDYEAA
LAA
>gnl|CDD|239313 cd03015, PRX_Typ2cys, Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure
VGKKAPDFKATAVVPNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVS
TDSHFSHLAWRNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDL
PVGRSVDETLRVLDALQFVEEHGEVCPANWKPG
>gnl|CDD|239314 cd03016, PRX_1cys, Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one conserved cysteine, which serves as the peroxidatic cysteine. They are homodimeric thiol-specific antioxidant (TSA) proteins that confer a protective role in cells by reducing and detoxifying hydrogen peroxide, peroxynitrite, and organic hydroperoxides. As with all other PRXs, a cysteine sulfenic acid intermediate is formed upon reaction of 1-cys PRX with its substrates. Having no resolving cysteine, the oxidized enzyme is resolved by an external small-molecule or protein reductant such as thioredoxin or glutaredoxin. Similar to typical 2-cys PRX, 1-cys PRX forms a functional dimeric unit with a B-type interface, as well as a decameric structure which is stabilized in the reduced form of the enzyme. Other oligomeric forms, tetramers and hexamers, have also been reported. Mammalian 1-cys PRX is localized cellularly in the cytosol and is expressed at high levels in brain, eye, testes and lung. The seed-specific plant 1-cys PRXs protect tissues from reactive oxygen species during desiccation and are also called rehydrins
LGDTAPNFEADTTHGPIKFHDYLGDSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSV
ESHIKWIEDIEEYTGVEIPFPIIADPDREVAKLLGMIDPDAGSTLTVRAVFIIDPDKKIRLILYYPATTG
RNFDEILRVVDALQLTDKHKVATPANWKPGDDVIVPPSVSDEEAKKKFPKGYETVDWYLRFTP
>gnl|CDD|239315 cd03017, PRX_BCP, Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth
DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVES
HAKFAEKYGLPFPLLSDPDGKLAKAYGVWGEKKKKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE
>gnl|CDD|239316 cd03018, PRX_AhpE_like, Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers
LEVGDKAPDFELPDQNGQEVRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISV
DSPFSLRAWAEENGLTFPLLSDFWPHGEVAKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRDL
PDYDEALDA
>gnl|CDD|239317 cd03019, DsbA_DsbA, DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in the CXXC motif. The highly unstable oxidized form of DsbA directly donates disulfide bonds to reduced proteins secreted into the bacterial periplasm. This rapid and unidirectional process helps to catalyze the folding of newly-synthesized polypeptides. To regain catalytic activity, reduced DsbA is then reoxidized by the membrane protein DsbB, which generates its disulfides from oxidized quinones, which in turn are reoxidized by the electron transport chain
EGKDYTVLSPPIPSGKPEVIEFFSYGCPHCYNFEPILEAWVKKLPKDVKFEKVPVVFGGGEGEPLARAFY
AAEALGLEDKLHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYK
ITGVPAFVVNGKYVVNPSAIGGDDTLQVLDELIEKVRY
>gnl|CDD|239318 cd03020, DsbA_DsbC_DsbG, DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active CXXC motif imbedded in a TRX fold. They function as protein disulfide isomerases and chaperones in the bacterial periplasm to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins. DsbC and DsbG are kept in their reduced state by the cytoplasmic membrane protein DsbD, which utilizes the TRX/TRX reductase system in the cytosol as a source of reducing equivalents. DsbG differ from DsbC in that it has a more limited substrate specificity, and it may preferentially act later in the folding process to catalyze disulfide rearrangements in folded or partially folded proteins. Also included in the alignment is the predicted protein TrbB, whose gene was sequenced from the enterohemorrhagic E. coli type IV pilus gene cluster, which is required for efficient plasmid transfer
TKVDSVFKTPVAGLYEVVTGGGVLYTDDDGRYLIQGNLYDAKGRKDDLTEARLAQLNAIDLSALPLDDAI
VYGKGNGKRVVYVFTDPDCPYCRKLEKELKPNADGVTVRIFPVPILGLPDSTAKAAAIWCAKDRAKAWTD
AMSGGKVPPPAASCDNPVAANLALGRQLGVNGTPTIVLADGRVVPGAPPAAQLEALL
>gnl|CDD|239319 cd03021, DsbA_GSTK, DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the GST family of enzymes which catalyzes the transfer of the thiol of GSH to electrophilic substrates. It is specifically located in the mitochondria and peroxisomes, unlike other members of the canonical GST family, which are mainly cytosolic. The biological substrates of GSTK are not yet known. It is presumed to have a protective role during respiration when large amounts of reactive oxygen species are generated. GSTK has the same general fold as DsbA, consisting of a thioredoxin domain interrupted by an alpha-helical domain and its biological unit is a homodimer. GSTK is closely related to the bacterial enzyme, 2-hydroxychromene-2-carboxylate (HCCA) isomerase. It shows little sequence similarity to the other members of the GST family
PKIELYYDVVSPYSYLAFEVLCRYQTAWNVDITYVPVFLGGIMKDSGNKPPIMLPNKAKYMAKDRKRSAE
FFGVPIRQPKDFFFMKKGTLTAQRFLTAISEQHPESTLTALEALFREFWVRPWSLTEPITESQSISVAAD
KLGGSAEQAEKLLKAASTPEVKNRLKENTDEALKYGAFGLPWIVVTNDKGKTEMFFGSDRFEQVADFLG
>gnl|CDD|239320 cd03022, DsbA_HCCA_Iso, DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a glutathione (GSH) dependent enzyme involved in the naphthalene catabolic pathway. It converts HCCA, a hemiketal formed spontaneously after ring cleavage of 1,2-dihydroxynapthalene by a dioxygenase, into cis-o-hydroxybenzylidenepyruvate (cHBPA). This is the fourth reaction in a six-step pathway that converts napthalene into salicylate. HCCA isomerase is unique to bacteria that degrade polycyclic aromatic compounds. It is closely related to the eukaryotic protein, GSH transferase kappa (GSTK)
IDFYFDFSSPYSYLAHERLPALAARHGATVRYRPILLGGVFKATGNVPPANRPPAKGRYRLRDLERWARR
YGIPLRFPPRFPPNTLRAMRAALAAQAEGDAAEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDADEL
LAAADDPAVKAALRANTEEAIARGVFGVPTFVVDGEMFWGQDRLDMLEEALA
>gnl|CDD|239321 cd03023, DsbA_Com1_like, DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer membrane-associated immunoreactive protein originally found in both acute and chronic disease strains of the pathogenic bacteria Coxiella burnetti. It contains a CXXC motif, assumed to be imbedded in a DsbA-like structure. Its homology to DsbA suggests that the protein is a protein disulfide oxidoreductase. The role of such a protein in pathogenesis is unknown
GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILGESSVLAARVALAVWKNGPGKYL
EFHNALMATRGRLNEESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDTVI
PGAVPADTLKEAID
>gnl|CDD|239322 cd03024, DsbA_FrnE, DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins
IDIWSDVVCPWCYIGKRRLEKALAELGDEVDVEIEWRPFELNPDMPPEGEDRREYLARKYGSTAEQAAAM
RRVEAAAAAEGLEFDFDRVRPPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEE
AGLDAAEARAVLASDEYADEVRADEARARQLGISGVPFFVFNGKYAVSGAQPPEVFLQALR
>gnl|CDD|239323 cd03025, DsbA_FrnE_like, DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif with similarity to DsbA and FrnE. FrnE is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins
LELYYFIDPLCGWCYGFEPLLEKLKEEYGGGIEVELHLGGLLPGNNARQITKQWRIYVHWHKARIALTGQ
PFGEDYLELLLFDLDSAPASRAIKAARLQGPERLLEMLKAIQRAHYVEGRDLADTEVLRELAIELGLDVE
EFLEDFQSDEAKQAIQEDQKLARELGINGFPTLVLEDDNGEGILLTGYYPYEP
>gnl|CDD|239324 cd03026, AhpF_NTD_C, TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) subfamily, C-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which then reduces hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD containing two contiguous TRX-fold subdomains similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -_ catalytic core of AhpF -_ NTD of AhpF -_ AhpC -_ peroxide substrates. The catalytic CXXC motif of the NTD of AhpF is contained in its C-terminal TRX subdomain
EDLLEQIRRLNGPINFETYVSLSCHNCPDVVQALNLMAVLNPNIEHEMIDGALFQDEVEERGIMSVPAIF
LNGELFGFGRMTLEEILAK
>gnl|CDD|239325 cd03027, GRX_DEP, Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of uncharacterized proteins containing a GRX domain and additional domains DEP and DUF547, both of which have unknown functions. GRX is a glutathione (GSH) dependent reductase containing a redox active CXXC motif in a TRX fold. It has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. By altering the redox state of target proteins, GRX is involved in many cellular functions
GRVTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIFPERKAELEERTGSSVVPQIFFNEKLVGGLTDLKS
LEE
>gnl|CDD|239326 cd03028, GRX_PICOT_like, Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum
IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVN
GELVGGCDIVKEMHESGELQ
>gnl|CDD|239327 cd03029, GRX_hybridPRX5, Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing peroxiredoxin (PRX) and GRX domains, which is found in some pathogenic bacteria and cyanobacteria. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins. PRX-GRX hybrid proteins from Haemophilus influenza and Neisseria meningitis exhibit GSH-dependent peroxidase activity. The flow of reducing equivalents in the catalytic cycle of the hybrid protein goes from NADPH -_ GSH reductase -_ GSH -_ GRX domain of hybrid -_ PRX domain of hybrid -_ peroxide substrate
ESVSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITGRSLRAVTGAMTVPQVFIDGELIGGSDDLEKY
FA
>gnl|CDD|239328 cd03030, GRX_SH3BGR, Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a recently-identified subfamily composed of SH3BGR and similar proteins possessing significant sequence similarity to GRX, but without a redox active CXXC motif. The SH3BGR gene was cloned in an effort to identify genes mapping to chromosome 21, which could be involved in the pathogenesis of congenital heart disease affecting Down syndrome newborns. Several human SH3BGR-like (SH3BGRL) genes have been identified since, mapping to different locations in the chromosome. Of these, SH3BGRL3 was identified as a tumor necrosis factor (TNF) alpha inhibitory protein and was also named TIP-B1. Upregulation of expression of SH3BGRL3 is associated with differentiation. It has been suggested that it functions as a regulator of differentiation-related signal transduction pathways
VIKVYIASSSGSTEIKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPNENGKPLPPQIFNGDEY
CGDYEAFFEAKENNTLEEFLKL
>gnl|CDD|239329 cd03031, GRX_GRX_like, Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive
RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAELKAVSLPRVFVDGRY
LGGAEEVLRLNESGELRKLLKGIRARAGGGVCEGCGGARFVPCSECNGSCKVFAENATAAGGFLRCPECN
ENGLVRC
>gnl|CDD|239330 cd03032, ArsC_Spx, Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding protein present in bacilli and some mollicutes. It inhibits transcription by binding to the C-terminal domain of the alpha subunit of RNAP, disrupting complex formation between RNAP and certain transcriptional activator proteins like ResD and ComA. In response to oxidative stress, Spx can also activate transcription, making it a general regulator that exerts both positive and negative control over transcription initiation. Spx has been shown to exert redox-sensitive transcriptional control over genes like trxA (TRX) and trxB (TRX reductase), genes that function in thiol homeostasis. This redox-sensitive activity is dependent on the presence of a CXXC motif, present in some members of the Spx subfamily, that acts as a thiol/disulfide switch. Spx has also been shown to repress genes in a sulfate-dependent manner independent of the presence of the CXXC motif
MIKLYTSPSCSSCRKAKQWLEEHQIPFEERNLFKQPLTKEELKEILSLTENGVEDIISTRSKAFKNLNID
IDELSLSELIRLISEHPSLLRRPIIIDEKRLQIGYNEDEIRQFLP
>gnl|CDD|239331 cd03033, ArsC_15kD, Arsenate Reductase (ArsC) family, 15kD protein subfamily; composed of proteins of unknown function with similarity to thioredoxin-fold arsenic reductases, ArsC. It is encoded by an ORF present in a gene cluster associated with nitrogen fixation that also encodes dinitrogenase reductase ADP-ribosyltransferase (DRAT) and dinitrogenase reductase activating glycohydrolase (DRAG). ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione via glutaredoxin, through a single catalytic cysteine
DIIFYEKPGCANNARQKALLEAAGHEVEVRDLLTEPWTAETLRPFFGDLPVAEWFNPAAPRVKSGEVVPE
ALDEEEALALMIADPLLIRRPLMQVGDRRMVGFDTARVDAWIG
>gnl|CDD|239332 cd03034, ArsC_ArsC, Arsenate Reductase (ArsC) family, ArsC subfamily; arsenic reductases similar to that encoded by arsC on the R733 plasmid of Escherichia coli. E. coli ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], the first step in the detoxification of arsenic, using reducing equivalents derived from glutathione (GSH) via glutaredoxin (GRX). ArsC contains a single catalytic cysteine, within a thioredoxin fold, that forms a covalent thiolate-As(V) intermediate, which is reduced by GRX through a mixed GSH-arsenate intermediate. This family of predominantly bacterial enzymes is unrelated to two other families of arsenate reductases which show similarity to low-molecular-weight acid phosphatases and phosphotyrosyl phosphatases
ITIYHNPRCSKSRNALALLEEAGIEPEIVEYLKTPPTAAELRELLAKLGISPRDLLRTKEAPYKELGLAD
PELSDEELIDAMAAHPILIERPIVVTGDGAVLGRPPEAVLEL
>gnl|CDD|239333 cd03035, ArsC_Yffb, Arsenate Reductase (ArsC) family, Yffb subfamily; Yffb is an uncharacterized bacterial protein encoded by the yffb gene, related to the thioredoxin-fold arsenic reductases, ArsC. The structure of Yffb and the conservation of the catalytic cysteine suggest that it is likely to function as a glutathione (GSH)-dependent thiol reductase. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from GSH via glutaredoxin, through a single catalytic cysteine
ITLYGIKNCDTVKKARKWLEARGVAYTFHDYRKDGLDAATLERWLAKVGWETLLNKRGTTWRKLDDAQKA
ALDAAKAIALMLEHPSLIKRPVLETGGKVLVGFSE
>gnl|CDD|239334 cd03036, ArsC_like, Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a CXXC motif with similarity to thioredoxin (TRX)-fold arsenic reductases, ArsC. Proteins containing a redox active CXXC motif like TRX and glutaredoxin (GRX) function as protein disulfide oxidoreductases, altering the redox state of target proteins via the reversible oxidation of the active site dithiol. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione via GRX, through a single catalytic cysteine
LKFYEYPKCSTCRKAKKWLDEHGVDYTAIDIVEEPPSKEELKKWLEKSGLPLKKFFNTSGKSYRELGLKD
KLPSLSEEEALELLSSDGMLIKRPFVVDDDKVLVGFKEEEW
>gnl|CDD|239335 cd03037, GST_N_GRX2, GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. coli GRX2, an atypical GRX with a molecular mass of about 24kD, compared with other GRXs which are 9-12kD in size. GRX2 adopts a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. It contains a redox active CXXC motif located in the N-terminal domain but is not able to reduce ribonucleotide reductase like other GRXs. However, it catalyzes GSH-dependent protein disulfide reduction of other substrates efficiently. GRX2 is thought to function primarily in catalyzing the reversible glutathionylation of proteins in cellular redox regulation including stress responses
MKLYIYEHCPFCVKARMIAGLKNIPVEQIILQNDDEATPIRMIGAKQVPILEKDDGSFMAESLDIVAFID
E
>gnl|CDD|239336 cd03038, GST_N_etherase_LigE, GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas paucimobilis beta etherase, LigE, a GST-like protein that catalyzes the cleavage of the beta-aryl ether linkages present in low-moleculer weight lignins using GSH as the hydrogen donor. This reaction is an essential step in the degradation of lignin, a complex phenolic polymer that is the most abundant aromatic material in the biosphere. The beta etherase activity of LigE is enantioselective and it complements the activity of the other GST family beta etherase, LigF
ITLYDLAGKDPVRAFSPNVWKTRLALNHKGLEYKTVPVEFPDIPPILGELTSGGFYTVPVIVDGSGEVIG
DSFAIAEYLEEAYP
>gnl|CDD|239337 cd03039, GST_N_Sigma_like, GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi and Alpha. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation and mediation of allergy and inflammation. Other class Sigma members include the class II insect GSTs, S-crystallins from cephalopods and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase and PGD2 synthase activities, and may play an important role in host-parasite interactions. Also members are novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST
YKLTYFNIRGRGEPIRLLLADAGVEYEDVRITYEEWPELDLKPTLPFGQLPVLEIDGKKLTQSNAILRYL
AR
>gnl|CDD|239338 cd03040, GST_N_mPGES2, GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a membrane-anchored dimeric protein containing a CXXC motif which catalyzes the isomerization of PGH2 to PGE2. Unlike cytosolic PGE synthase (cPGES) and microsomal PGES Type 1 (mPGES1), mPGES2 does not require glutathione (GSH) for its activity, although its catalytic rate is increased two- to four-fold in the presence of DTT, GSH or other thiol compounds. PGE2 is widely distributed in various tissues and is implicated in the sleep/wake cycle, relaxation/contraction of smooth muscle, excretion of sodium ions, maintenance of body temperature and mediation of inflammation. mPGES2 contains an N-terminal hydrophobic domain which is membrane associated, and a C-terminal soluble domain with a GST-like structure
KITLYQYKTCPFCCKVRAFLDYHGIPYEVVEVNPVSRKEIKWSSYKKVPILRVESGGDGQQLVDSSVIIS
TLKTYLG
>gnl|CDD|239339 cd03041, GST_N_2GST_N, GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed of uncharacterized proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains
PLELYEFEGSPFCRLVREVLTELELDVILYPCPKGSPKRDKFLEKGGKVQVPYLVDPNTGVQMFESADIV
KYLFKTY
>gnl|CDD|239340 cd03042, GST_N_Zeta, GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Zeta GSTs, also known as maleylacetoacetate (MAA) isomerases, catalyze the isomerization of MAA to fumarylacetoacetate, the penultimate step in tyrosine/phenylalanine catabolism, using GSH as a cofactor. They show little GSH-conjugating activity towards traditional GST substrates but display modest GSH peroxidase activity. They are also implicated in the detoxification of the carcinogen dichloroacetic acid by catalyzing its dechlorination to glyoxylic acid
MILYSYFRSSASYRVRIALNLKGLDYEYVPVNLLKGEQLSPAYRALNPQGLVPTLVIDGLVLTQSLAIIE
YLD
>gnl|CDD|239341 cd03043, GST_N_1, GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from bacteria, with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains
TLVIGNKNYSSWSLRPWLLLKAAGIPFEEILVPLYTPDTRARILEFSPTGKVPVLVDGGIVVWDSLAICE
YLA
>gnl|CDD|239342 cd03044, GST_N_EF1Bgamma, GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal TRX-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression
GTLYTYPGNPRSLKILAAAKYNGLDVEIVDFQPGKENKTPEFLKKFPLGKVPAFEGADGFCLFESNAIAY
YVANL
>gnl|CDD|239343 cd03045, GST_N_Delta_Epsilon, GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress
IDLYYLPGSPPCRAVLLTAKALGLELNLKEVNLMKGEHLKPEFLKLNPQHTVPTLVDNGFVLWESHAILI
YLVE
>gnl|CDD|239344 cd03046, GST_N_GTT1_like, GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals
ITLYHLPRSRSFRILWLLEELGLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVDGDLVLTESAAIILY
LAEKYG
>gnl|CDD|239345 cd03047, GST_N_2, GST_N family, unknown subfamily 2; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The sequence from Burkholderia cepacia was identified as part of a gene cluster involved in the degradation of 2,4,5-trichlorophenoxyacetic acid. Some GSTs (e.g. Class Zeta and Delta) are known to catalyze dechlorination reactions
LTIWGRRSSINVQKVLWLLDELGLPYERIDAGGQFGGLDTPEFLAMNPNGRVPVLEDGDFVLWESNAILR
YLA
>gnl|CDD|239346 cd03048, GST_N_Ure2p_like, GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related GSTs. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The N-terminal TRX-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. Characterized GSTs in this subfamily include Aspergillus fumigatus GSTs 1 and 2, and Schizosaccharomyces pombe GST-I. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of GSH with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes
MITLYTHGTPNGFKVSIMLEELGLPYEIHPVDISKGEQKKPEFLKINPNGRIPAIVDHNGTPLTVFESGA
ILLYLAEKYDK
>gnl|CDD|239347 cd03049, GST_N_3, GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains
MKLLYSPTSPYVRKVRVAAHETGLGDDVELVLVNPWSDDESLLAVNPLGKIPALVLDDGEALFDSRVICE
YLD
>gnl|CDD|239348 cd03050, GST_N_Theta, GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial dichloromethane (DCM) dehalogenase. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Mammalian class Theta GSTs show poor GSH conjugating activity towards the standard substrates, CDNB and ethacrynic acid, differentiating them from other mammalian GSTs. GSTT1-1 shows similar cataytic activity as bacterial DCM dehalogenase, catalyzing the GSH-dependent hydrolytic dehalogenation of dihalomethanes. This is an essential process in methylotrophic bacteria to enable them to use chloromethane and DCM as sole carbon and energy sources. The presence of polymorphisms in human GSTT1-1 and its relationship to the onset of diseases including cancer is subject of many studies. Human GSTT2-2 exhibits a highly specific sulfatase activity, catalyzing the cleavage of sulfate ions from aralkyl sufate esters, but not from aryl or alkyl sulfate esters
LKLYYDLMSQPSRAVYIFLKLNKIPFEECPIDLRKGEQLTPEFKKINPFGKVPAIVDGDFTLAESVAILR
YLARKF
>gnl|CDD|239349 cd03051, GST_N_GTT2_like, GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT2. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock
MKLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLAAGEQRSPEFLAKNPAGTVPVLELDDGTVITESVAIC
RYLE
>gnl|CDD|239350 cd03052, GST_N_GDAP1, GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; GDAP1 was originally identified as a highly expressed gene at the differentiated stage of GD3 synthase-transfected cells. More recently, mutations in GDAP1 have been reported to cause both axonal and demyelinating autosomal-recessive Charcot-Marie-Tooth (CMT) type 4A neuropathy. CMT is characterized by slow and progressive weakness and atrophy of muscles. Sequence analysis of GDAP1 shows similarities and differences with GSTs; it appears to contain both N-terminal TRX-fold and C-terminal alpha helical domains of GSTs, however, it also contains additional C-terminal transmembrane domains unlike GSTs. GDAP1 is mainly expressed in neuronal cells and is localized in the mitochondria through its transmembrane domains. It does not exhibit GST activity using standard substrates
LVLYHWTQSFSSQKVRLVIAEKGLRCEEYDVSLPLSEHNEPWFMRLNPTGEVPVLIHGDNIICDPTQIID
YLE
>gnl|CDD|239351 cd03053, GST_N_Phi, GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Phi GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity
VLKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTKGEHKSPEHLARNPFGQIPALEDGDLKLFESRAIT
RYLAEK
>gnl|CDD|239352 cd03054, GST_N_Metaxin, GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. Metaxin 2 binds to metaxin 1 and may also play a role in protein translocation into the mitochondria. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken and mammals. Sequence analysis suggests that all three metaxins share a common ancestry and that they possess similarity to GSTs. Also included in the subfamily are uncharacterized proteins with similarity to metaxins, including a novel GST from Rhodococcus with toluene o-monooxygenase and glutamylcysteine synthetase activities
LELYQWGRAFGLPSLSPECLKVETYLRMAGIPYEVVFSSNPWRSPTGKLPFLELNGEKIADSEKIIEYLK
KK
>gnl|CDD|239353 cd03055, GST_N_Omega, GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases
SSKHLAKGSAEPPPVPGIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPAL
EIDEGKVVYESLIICEYLD
>gnl|CDD|239354 cd03056, GST_N_4, GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains
MKLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKGETRTPEFLALNPNGEVPVLELDGRVLAESNAILV
YLA
>gnl|CDD|239355 cd03057, GST_N_Beta, GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH
MKLYYSPGACSLAPHIALEELGLPFELVRVDLRTKTQKGADYLAINPKGQVPALVLDDGEVLTESAAILQ
YLADLHP
>gnl|CDD|239356 cd03058, GST_N_Tau, GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones
VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYI
DEAW
>gnl|CDD|239357 cd03059, GST_N_SspA, GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal TRX-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis
MTLYSGPDDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPYGTVPTLVDRDLVLYESRIIMEYLD
ERF
>gnl|CDD|239358 cd03060, GST_N_Omega_like, GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to class Omega GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. Like Omega enzymes, proteins in this subfamily contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism
PILYSFRRCPYAMRARMALLLAGITVELREVELKNKPAEMLAASPKGTVPVLVLGNGTVIEESLDIMRWA
L
>gnl|CDD|239359 cd03061, GST_N_CLIC, GST_N family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLIC1-5, p64, parchorin and similar proteins. They are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division and apoptosis. They can exist in both water-soluble and membrane-bound states, and are found in various vesicles and membranes. Biochemical studies of the C. elegans homolog, EXC-4, show that the membrane localization domain is present in the N-terminal part of the protein. The structure of soluble human CLIC1 reveals that it is monomeric and it adopts a fold similar to GSTs, containing an N-terminal domain with a TRX fold and a C-terminal alpha helical domain. Upon oxidation, the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. The CLIC1 dimer bears no similarity to GST dimers. The redox-controlled structural rearrangement exposes a large hydrophobic surface, which is masked by dimerization in vitro. In vivo, this surface may represent the docking interface of CLIC1 in its membrane-bound state. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity, however, in other subfamily members, the second cysteine is not conserved
QEEPEIELFVKASSDGESIGNCPFCQRLFMVLWLKGVVFNVTTVDMKRKPEDLKDLAPGTQPPFLLYNGE
VKTDNNKIEEFLEETLCPPKY
>gnl|CDD|239360 cd03062, TRX_Fd_Sucrase, TRX-like [2Fe-2S] Ferredoxin (Fd) family, Sucrase subfamily; composed of proteins with similarity to a novel plant enzyme, isolated from potato, which contains a Fd-like domain and exhibits sucrolytic activity. The putative active site of the Fd-like domain of the enzyme contains two cysteines and two histidines for possible binding to iron-sulfur clusters, compared to four cysteines present in the active site of Fd
DPLVLVCTHGKRDKRCGICGPPLAAELRAELPEHGPGGVRVWEVSHVGGHKFAGNVIIYPKGDGIWYGRV
TPEHVPPIVDRLILGGKIIPELRRGGI
>gnl|CDD|239361 cd03063, TRX_Fd_FDH_beta, TRX-like [2Fe-2S] Ferredoxin (Fd) family, NAD-dependent formate dehydrogenase (FDH) beta subunit; composed of proteins similar to the beta subunit of NAD-linked FDH of Ralstonia eutropha, a soluble enzyme that catalyzes the irreversible oxidation of formate to carbon dioxide accompanied by the reduction of NAD to NADH. FDH is a heteromeric enzyme composed of four nonidentical subunits (alpha, beta, gamma and delta). The FDH beta subunit contains a NADH:ubiquinone oxidoreductase (Nuo) F domain C-terminal to a Fd-like domain without the active site cysteines. The absence of conserved metal-binding residues in the putative active site suggests that members of this subfamily have lost the ability to bind iron-sulfur clusters in the N-terminal Fd-like domain. The C-terminal NuoF domain is a component of Nuo, a multisubunit complex catalyzing the electron transfer of NADH to quinone coupled with the transfer of protons across the membrane. NuoF contains one [4Fe-4S] cluster and binds NADH and FMN
TRIYVPRDAAALALGADEVAEAIEAEAAARGLAATIVRNGSRGMYWLEPLVEVETPGGRVAYGPVTPADV
ASLLDAGALEGGEHPLCLGLTE
>gnl|CDD|239362 cd03064, TRX_Fd_NuoE, TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E subfamily; Nuo, also called respiratory chain Complex 1, is the entry point for electrons into the respiratory chains of bacteria and the mitochondria of eukaryotes. It is a multisubunit complex with at least 14 core subunits. It catalyzes the electron transfer of NADH to quinone coupled with the transfer of protons across the membrane, providing the proton motive force required for energy-consuming processes. Electrons are transferred from NADH to quinone through a chain of iron-sulfur clusters in Nuo, including the [2Fe-2S] cluster present in NuoE core subunit, also called the 24 kD subunit of Complex 1. This subfamily also include formate dehydrogenases, NiFe hydrogenases and NAD-reducing hydrogenases, that contain a NuoE domain. A subset of these proteins contain both NuoE and NuoF in a single chain. NuoF, also called the 51 kD subunit of Complex 1, contains one [4Fe-4S] cluster and also binds the NADH substrate and FMN
KHVIRVCTGTACHLRGAEALLEALEKKLGIKPGETTPDGRFTLEEVECLGACDLAPVMMINDDVYGRLTP
EKVDAILEAL
>gnl|CDD|239363 cd03065, PDI_b_Calsequestrin_N, PDIb family, Calsequestrin subfamily, N-terminal TRX-fold domain; Calsequestrin is the major calcium storage protein in the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. It stores calcium ions in sufficient quantities (up to 20 mM) to allow repetitive contractions and is essential to maintain movement, respiration and heart beat. A missense mutation in human cardiac calsequestrin is associated with catecholamine-induced polymorphic ventricular tachycardia (CPVT), a rare disease characterized by seizures or sudden death in response to physiologic or emotional stress. Calsequestrin is a highly acidic protein with up to 50 calcium binding sites formed simply by the clustering of two or more acidic residues. The monomer contains three redox inactive TRX-fold domains. Calsequestrin is condensed as a linear polymer in the SR lumen and is membrane-anchored through binding with intra-membrane proteins triadin, junctin and ryanodine receptor (RyR) Ca2+ release channel. In addition to its role as a calcium ion buffer, calsequestrin also regulates the activity of the RyR channel, coordinating the release of calcium ions from the SR with the loading of the calcium store. The N-terminal TRX-fold domain (or domain I) mediates front-to-front dimer interaction, an important feature in the formation of calsequestrin polymers
DFPEYDGKDRVIDLNEKNYKQVLKKYDVLCLLYHEPVESDKEAQKQFQMEELVLELAAQVLEDKGIGFGL
VDSKKDAKVAKKLGLDEEDSIYVFKDDEVIEYDGEFAADTLVEFLLDLIE
>gnl|CDD|239364 cd03066, PDI_b_Calsequestrin_middle, PDIb family, Calsequestrin subfamily, Middle TRX-fold domain; Calsequestrin is the major calcium storage protein in the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. It stores calcium ions in sufficient quantities (up to 20 mM) to allow repetitive contractions and is essential to maintain movement, respiration and heart beat. A missense mutation in human cardiac calsequestrin is associated with catecholamine-induced polymorphic ventricular tachycardia (CPVT), a rare disease characterized by seizures or sudden death in response to physiologic or emotional stress. Calsequestrin is a highly acidic protein with up to 50 calcium binding sites formed simply by the clustering of two or more acidic residues. The monomer contains three redox inactive TRX-fold domains. Calsequestrin is condensed as a linear polymer in the SR lumen and is membrane-anchored through binding with intra-membrane proteins triadin, junctin and ryanodine receptor (RyR) Ca2+ release channel. In addition to its role as a calcium ion buffer, calsequestrin also regulates the activity of the RyR channel, coordinating the release of calcium ions from the SR with the loading of the calcium store
PVEIINSERELQAFENIEDDIKLIGYFKSEDSEHYKAFEEAAEEFHPYIKFFATFDSKVAKKLGLKMNEV
DFYEPFMEEPVTIPDKPYSEEELVDFVEEHKR
>gnl|CDD|239365 cd03067, PDI_b_PDIR_N, PDIb family, PDIR subfamily, N-terminal TRX-like b domain; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity. The TRX-like b domain of PDIR is critical for its chaperone activity
PLIEDISDHKDFKKLLRTRNNVLVLYSKSAKSAEALLKLLSDVAQAVKGQGTIAWIDCGDSESRKLCKKL
KVDPSSKPKPVELKHYKDGDFHTEYNRQLTFKSMVAFLRDPE
>gnl|CDD|239366 cd03068, PDI_b_ERp72, PDIb family, ERp72 subfamily, first redox inactive TRX-like domain b; ERp72 exhibits both disulfide oxidase and reductase functions like PDI, by catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER and acting as isomerases to correct any non-native disulfide bonds. It also displays chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. ERp72 contains three redox-active TRX (a) domains and two redox inactive TRX-like (b) domains. Its molecular structure is a"abb'a', compared to the abb'a' structure of PDI. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. Similar to PDI, the b domain of ERp72 is likely involved in binding to substrates
PSKQLQTLKQVQEFLRDGDDVIIIGVFSGEEDPAYQLYQDAANSLREDYKFHHTFDSEIFKSLKVSPGQL
VVFQPEKFQSKYEPKSHVLNKKDSTSEDELKDFFKEH
>gnl|CDD|239367 cd03069, PDI_b_ERp57, PDIb family, ERp57 subfamily, first redox inactive TRX-like domain b; ERp57 (or ERp60) exhibits both disulfide oxidase and reductase functions like PDI, by catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER and acting as isomerases to correct any non-native disulfide bonds. It also displays chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. ERp57 contains two redox-active TRX (a) domains and two redox inactive TRX-like (b) domains. It shares the same domain arrangement of abb'a' as PDI, but lacks the C-terminal acid-rich region (c domain) that is present in PDI. ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins. Similar to PDI, the b domain of ERp57 is likely involved in binding to substrates
ASVELRTEAEFEKFLSDDDASVVGFFEDEDSKLLSEFLKAADTLRESFRFAHTSDKQLLEKYGYGEGVVL
FRPPRLSNKFEDSSVKFDGDLDSSKIKKFIRENI
>gnl|CDD|239368 cd03070, PDI_b_ERp44, PDIb family, ERp44 subfamily, first redox inactive TRX-like domain b; ERp44 is an endoplasmic reticulum (ER)-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. Through the formation of reversible mixed disulfides, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. ERp44 also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol. Similar to PDI, the b domain of ERp44 is likely involved in binding to substrates
IKEFRNLDELNNVDRSKRNIIGYFESKDSDEYDNFRKVANILRDDCSFLVGFGDVTKPERPPGDNIIYFP
PGHNAPDMVYLGSLTNFDLLK
>gnl|CDD|239369 cd03071, PDI_b'_NRX, PDIb' family, NRX subgroup, redox inactive TRX-like domain b'; composed of vertebrate nucleoredoxins (NRX). NRX is a 400-amino acid nuclear protein with one redox active TRX domain followed by one redox inactive TRX-like domain homologous to the b' domain of PDI. In vitro studies show that NRX has thiol oxidoreductase activity and that it may be involved in the redox regulation of transcription, in a manner different from that of TRX or glutaredoxin. NRX enhances the activation of NF-kB by TNFalpha, as well as PMA-1 induced AP-1 and FK-induced CREB activation. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. The mouse NRX gene is implicated in streptozotocin-induced diabetes. Similar to PDI, the b' domain of NRX is likely involved in substrate recognition
VLELSESNAVQLNEGPCLVLFVDSEDEGESEAAKQLIQPIAEKIIAKYKAKEEEAPLLFFVAGEDDMTDS
LRDYTNLPEAAPLLTILDMSARAKYVMDVEEITPAIVEAFVSDFLA
>gnl|CDD|239370 cd03072, PDI_b'_ERp44, PDIb' family, ERp44 subfamily, second redox inactive TRX-like domain b'; ERp44 is an endoplasmic reticulum (ER)-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. Through the formation of reversible mixed disulfides, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. ERp44 also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol. Similar to PDI, the b' domain of ERp44 is likely involved in substrate recognition and may be the primary binding site
VREITFENAEELTEEGLPFLILFHDKDDLESLKEFKQAVARQLISEKGAINFLTADGDKFRHPLLHLGKT
PADLPVIAIDSFRHMYLFPDFEDVYVPGKLKQFVLDLHSGK
>gnl|CDD|239371 cd03073, PDI_b'_ERp72_ERp57, PDIb' family, ERp72 and ERp57 subfamily, second redox inactive TRX-like domain b'; ERp72 and ER57 are involved in oxidative protein folding in the ER, like PDI. They exhibit both disulfide oxidase and reductase functions, by catalyzing the formation of disulfide bonds of newly synthesized polypeptides and acting as isomerases to correct any non-native disulfide bonds. They also display chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. ERp57 contains two redox-active TRX (a) domains and two redox inactive TRX-like (b) domains. It shares the same domain arrangement of abb'a' as PDI, but lacks the C-terminal acid-rich region (c domain) that is present in PDI. ERp72 contains one additional redox-active TRX (a) domain at the N-terminus with a molecular structure of a"abb'a'. ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. The b' domain of ERp57 is the primary binding site and is adapted for ER lectin association. Similarly, the b' domain of ERp72 is likely involved in substrate recognition
VGHRTKDNRAQFTKKPLVVAYYNVDYSKNPKGTNYWRNRVLKVAKDFPDRKLNFAVADKEDFSHELEEFG
LDFSGGEKPVVAIRTAKGKKYVMEEEFSDVDALEEFLEDFF
>gnl|CDD|239372 cd03074, PDI_b'_Calsequestrin_C, Protein Disulfide Isomerase (PDIb') family, Calsequestrin subfamily, C-terminal TRX-fold domain; Calsequestrin is the major calcium storage protein in the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. It stores calcium ions in sufficient quantities (up to 20 mM) to allow repetitive contractions and is essential to maintain movement, respiration and heart beat. A missense mutation in human cardiac calsequestrin is associated with catecholamine-induced polymorphic ventricular tachycardia (CPVT), a rare disease characterized by seizures or sudden death in response to physiologic or emotional stress. Calsequestrin is a highly acidic protein with up to 50 calcium binding sites formed simply by the clustering of two or more acidic residues. The monomer contains three redox inactive TRX-fold domains. Calsequestrin is condensed as a linear polymer in the SR lumen and is membrane-anchored through binding with intra-membrane proteins triadin, junctin and ryanodine receptor (RyR) Ca2+ release channel. In addition to its role as a calcium ion buffer, calsequestrin also regulates the activity of the RyR channel, coordinating the release of calcium ions from the SR with the loading of the calcium store. The C-terminal TRX-fold domain (or domain III) mediates back-to-back dimer interaction and also contriubutes to the front-to-front dimer interface, both of which are important features in the formation of calsequestrin polymers
PTLRKLKPENMFETWEDDLDGIHIVAFAEEEDPDGYEFLEILKEVARDNTDNPDLSIIWIDPDDFPLLVP
YWEKTFGIDLFRPQIGVVNVTDADSVWMEMDDDEDLPTAEELEDWIEDVL
>gnl|CDD|239373 cd03075, GST_N_Mu, GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1), thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation
PTLGYWDIRGLAQPIRLLLEYTGEKYEEKRYELGDAPDYDRSQWLNEKFKLGLDFPNLPYYIDGDVKLTQ
SNAILRYIARKH
>gnl|CDD|239374 cd03076, GST_N_Pi, GST_N family, Class Pi subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Pi GST is a homodimeric eukaryotic protein. The human GSTP1 is mainly found in erythrocytes, kidney, placenta and fetal liver. It is involved in stress responses and in cellular proliferation pathways as an inhibitor of JNK (c-Jun N-terminal kinase). Following oxidative stress, monomeric GSTP1 dissociates from JNK and dimerizes, losing its ability to bind JNK and causing an increase in JNK activity, thereby promoting apoptosis. GSTP1 is expressed in various tumors and is the predominant GST in a wide range of cancer cells. It has been implicated in the development of multidrug-resistant tumours
PYTLTYFPVRGRAEAIRLLLADQGISWEEERVTYEEWQESLKPKMLFGQLPCFKDGDLTLVQSNAILRHL
GRK
>gnl|CDD|239375 cd03077, GST_N_Alpha, GST_N family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Alpha subfamily is composed of eukaryotic GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals
KPVLHYFNGRGRMESIRWLLAAAGVEFEEKFIESAEDLEKLKKDGSLMFQQVPMVEIDGMKLVQTRAILN
YIAGKYNLY
>gnl|CDD|239376 cd03078, GST_N_Metaxin1_like, GST_N family, Metaxin subfamily, Metaxin 1-like proteins; composed of metaxins 1 and 3, and similar proteins including Tom37 from fungi. Mammalian metaxin (or metaxin 1) and the fungal protein Tom37 are components of preprotein import complexes of the mitochondrial outer membrane. Metaxin extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. Like the murine gene, the human metaxin gene is located downstream to the glucocerebrosidase (GBA) pseudogene and is convergently transcribed. Inherited deficiency of GBA results in Gaucher disease, which presents many diverse clinical phenotypes. Alterations in the metaxin gene, in addition to GBA mutations, may be associated with Gaucher disease. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken and mammals
MELHVWGGDWGLPSVDPECLAVLAYLKFAGAPLKVVPSNNPWRSPTGKLPALLTSGTKISGPEKIIEYLR
KQG
>gnl|CDD|239377 cd03079, GST_N_Metaxin2, GST_N family, Metaxin subfamily, Metaxin 2; a metaxin 1 binding protein identified through a yeast two-hybrid system using metaxin 1 as the bait. Metaxin 2 shares sequence similarity with metaxin 1 but does not contain a C-terminal mitochondrial outer membrane signal-anchor domain. It associates with mitochondrial membranes through its interaction with metaxin 1, which is a component of the mitochondrial preprotein import complex of the outer membrane. The biological function of metaxin 2 is unknown. It is likely that it also plays a role in protein translocation into the mitochondria. However, this has not been experimentally validated. In a recent proteomics study, it has been shown that metaxin 2 is overexpressed in response to lipopolysaccharide-induced liver injury
AALYQPYEEEQILLPDNASCLAVQTFLKMCNLPFNVRCRANAEFMSPSGKVPFIRVGNQIVSEFGPIVQF
VEAK
>gnl|CDD|239378 cd03080, GST_N_Metaxin_like, GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, predominantly uncharacterized, with similarity to metaxins and GSTs. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. One characterized member of this subgroup is a novel GST from Rhodococcus with toluene o-monooxygenase and gamma-glutamylcysteine synthetase activities. Also members are the cadmium-inducible lysosomal protein CDR-1 and its homologs from C. elegans, and the failed axon connections (fax) protein from Drosophila. CDR-1 is an integral membrane protein that functions to protect against cadmium toxicity and may also have a role in osmoregulation to maintain salt balance in C. elegans. The fax gene of Drosophila was identified as a genetic modifier of Abelson (Abl) tyrosine kinase. The fax protein is localized in cellular membranes and is expressed in embryonic mesoderm and axons of the central nervous system
MITLYQFPRAFGVPSLSPFCLKVETFLRMAGIPYENKFGGLAKRSPKGKLPFIELNGEKIADSELIIDHL
EEKYG
>gnl|CDD|239379 cd03081, TRX_Fd_NuoE_FDH_gamma, TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E subfamily, NAD-dependent formate dehydrogenase (FDH) gamma subunit; composed of proteins similar to the gamma subunit of NAD-linked FDH of Ralstonia eutropha, a soluble enzyme that catalyzes the irreversible oxidation of formate to carbon dioxide accompanied by the reduction of NAD+ to NADH. FDH is a heteromeric enzyme composed of four nonidentical subunits (alpha, beta, gamma and delta). The FDH gamma subunit is closely related to NuoE, which is part of a multisubunit complex (Nuo) catalyzing the electron transfer of NADH to quinone coupled with the transfer of protons across the membrane. Electrons are transferred from NADH to quinone through a chain of iron-sulfur clusters in Nuo, including the [2Fe-2S] cluster present in NuoE. Similarly, the FDH gamma subunit is hypothesized to be involved in an electron transport chain involving other FDH subunits, upon the oxidation of formate
RHVLKLCRAEACQAMGAEALAAHIKARLGIDFHETTADGSVTLEPVYCLGLCACSPAAMIDGEVHGRVDP
EKFDALLAEL
>gnl|CDD|239380 cd03082, TRX_Fd_NuoE_W_FDH_beta, TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E family, Tungsten-containing formate dehydrogenase (W-FDH) beta subunit; composed of proteins similar to the W-FDH beta subunit of Methylobacterium extorquens. W-FDH is a heterodimeric NAD-dependent enzyme catalyzing the conversion of formate to carbon dioxide. The beta subunit is a fusion protein containing an N-terminal NuoE domain and a C-terminal NuoF domain. NuoE and NuoF are components of Nuo, a multisubunit complex catalyzing the electron transfer of NADH to quinone coupled with the transfer of protons across the membrane. Electrons are transferred from NADH to quinone through a chain of iron-sulfur clusters in Nuo, including the [2Fe-2S] cluster in NuoE and the [4Fe-4S] cluster in NuoF. In addition, NuoF is also the NADH- and FMN-binding subunit. Similarly, the beta subunit of W-FDH is most likely involved in the electron transport chain during the NAD-dependent oxidation of formate
ALTVRVCDSLSCAMAGAEELLAALEAGLGPEGVRVVRAPCVGRCERAPAALVGQRPVDGATPAAVAAAVE
AG
>gnl|CDD|239381 cd03083, TRX_Fd_NuoE_hoxF, TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E subfamily, hoxF; composed of proteins similar to the NAD-reducing hydrogenase (hoxS) alpha subunit of Alcaligenes eutrophus H16. HoxS is a cytoplasmic hydrogenase catalyzing the oxidation of molecular hydrogen accompanied by the reduction of NAD. It is composed of four structural subunits encoded by the genes hoxF, hoxU, hoxY and hoxH. The hoxF protein (or alpha subunit) is a fusion protein containing an N-terminal NuoE-like domain and a C-terminal NuoF domain. NuoE and NuoF are components of Nuo, a multisubunit complex catalyzing the electron transfer of NADH to quinone coupled with the transfer of protons across the membrane. Electrons are transferred from NADH to quinone through a chain of iron-sulfur clusters in Nuo, including the [2Fe-2S] cluster in NuoE and the [4Fe-4S] cluster in NuoF. In addition, NuoF is also the NADH- and FMN-binding subunit. HoxF may be involved in the electron transport chain during the NAD-dependent oxidation of hydrogen through its NuoF domain. The NuoE-like domain of hoxF contains only one conserved cysteine in its putative active site, compared to four cysteines in NuoE, and may have lost the ability to bind [2Fe-2S] clusters
KYRIYLSDSITDRMNGYKAVLDALCRELGIRFGEVDEDGMVGLFFTSCTGLCDQGPALLINNRVFTRLTP
GRIDQIAELI
>gnl|CDD|100086 cd03084, phosphohexomutase, The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this family include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). These enzymes play important and diverse roles in carbohydrate metabolism in organisms from bacteria to humans. Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model
IFGTSGVRGVVGDDITPETAVALGQAIGSTGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAE
KEDEPSAVAYELGGSVKAVDILQRYFEALKKLFDVAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVI
PLNCEPDGNFGNINPDPGSETNLKQLLAVVKAEKADFGVAFDGDADRLIVVDENGGFLDGDELLALLAVE
LFLTFNPRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGVIFPEFHPGR
DGISAALLLLEILANLGKSLSELFSELPRYYYIRLKVRGWVLVRASGTEPAIRIYAEADTQEDVEQIKKE
ARELV
>gnl|CDD|100087 cd03085, PGM1, Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate (G-1-P) and glucose-6-phosphate (G-6-P) via a glucose 1,6-diphosphate intermediate, an important metabolic step in prokaryotes and eukaryotes. In one direction, G-1-P produced from sucrose catabolism is converted to G-6-P, the first intermediate in glycolysis. In the other direction, conversion of G-6-P to G-1-P generates a substrate for synthesis of UDP-glucose which is required for synthesis of a variety of cellular constituents including cell wall polymers and glycoproteins. The PGM1 family also includes a non-enzymatic PGM-related protein (PGM-RP) thought to play a structural role in eukaryotes, as well as pp63/parafusin, a phosphoglycoprotein that plays an important role in calcium-regulated exocytosis in ciliated protozoans. PGM1 belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model
QTVPTKPYEGQKPGTSGLRKKVKVFQQPNYLENFVQSIFNALPPEKLKGATLVVGGDGRYYNKEAIQIII
KIAAANGVGKVVVGQNGLLSTPAVSAVIRKRKATGGIILTASHNPGGPEGDFGIKYNTSNGGPAPESVTD
KIYEITKKITEYKIADDPDVDLSKIGVTKFGGKPFTVEVIDSVEDYVELMKEIFDFDAIKKLLSRKGFKV
RFDAMHGVTGPYAKKIFVEELGAPESSVVNCTPLPDFGGGHPDPNLTYAKDLVELMKSGEPDFGAASDGD
GDRNMILGKGFFVTPSDSVAVIAANAKLIPYFYKGGLKGVARSMPTSGALDRVAKKLGIPLFETPTGWKF
FGNLMDAGKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILAHRNVSVEDIVKEHWQKYGRNFYTRYDYE
EVDSEAANKMMDHLRALVSDLPGVGKSGDKGYKVAKADDFSYTDPVDGSVSKKQGLRIIFEDGSRIIFRL
SGTGSSGATIRLYIESYEKDPSKYGLDAQVALKPLIEIALKLSKLKEFTGREEPTVIT
>gnl|CDD|100088 cd03086, PGM3, PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 (N-acetylglucosamine-phosphate mutase), is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. AGM1 is a member of the alpha-D-phosphohexomutase superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model
SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGKTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPY
ATQLANASDDELLVLVLMLISVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVT
TPQLHYLVRAANTEGAYGEPTEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRL
KKGLSVKIINDGEEGPELLNDGCGADYVKTKQKPPRGFELKPPGVRCCSFDGDADRLVYFYPDSSNKFHL
LDGDKIATLFAKFIKELLKKAGEELKLTIGVVQTAYANGASTKYLEDVLKVPVVCTPTGVKHLHHAAEEF
DIGVYFEANGHGTVLFSESALAKIEENSSLSDEQEKAAKTLLAFSRLINQTVGDAISDMLAVELILAALG
WSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGRAFVRPSGTEDVV
RVYAEAATQEEADELANEVAELV
>gnl|CDD|100089 cd03087, PGM_like1, This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model
LFGTSGIRGVVGEELTPELALKVGKALGTYLGGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIV
PTPALQYAVRKLGDAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERFRRVAWDEVGSVR
REDSAIDEYIEAILDKVDIDGGKGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFPGRPPEPT
PENLSELMELVRATGADLGIAHDGDADRAVFVDEKGRFIDGDKLLALLAKYLLEEGGGKVVTPVDASMLV
EDVVEEAGGEVIRTPVGDVHVAEEMIENGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLAEEKPLSE
LLDELPKYPLLREKVECPDEKKEEVMEAVEEELSDADEDVDTIDGVRIEYEDGWVLIRPSGTEPKIRITA
EAKTEERAKELLEEGRSKV
>gnl|CDD|100090 cd03088, ManB, ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose 6-phosphate to mannose-1-phosphate in the second of three steps in the GDP-mannose pathway, in which GDP-D-mannose is synthesized from fructose-6-phosphate. In Mycobacterium tuberculosis, the causative agent of tuberculosis, PMM is involved in the biosynthesis of mannosylated lipoglycans that participate in the association of mycobacteria with host macrophage phagocytic receptors. ManB belongs to the the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model
KFGTSGLRGLVTDLTDEVCYAYTRAFLQHLESKFPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDC
GAVPTPALALYAMKRGAPAIMVTGSHIPADRNGLKFYRPDGEITKADEAAILAALVELPEALFDPAGALL
PPDTDAADAYIARYTDFFGAGALKGLRIGVYQHSSVGRDLLVRILEALGAEVVPLGRSDTFIPVDTEAVR
PEDRALAAAWAAEHGLDAIVSTDGDGDRPLVADETGEWLRGDILGLLTARFLGADTVVTPVSSNSAIELS
GFFKRVVRTRIGSPYVIAAMAEAAAAGAGRVVGYEANGGFLLGSDIERNGRTLKALPTRDAVLPILAVLA
AAKEAGIPLSELVASLPARFTASDRLQNFPTEKSQALIARLSADPEARAAFFFALGGEVASIDTTDGLRM
TFANGDIVHLRPSGNAPELRCYVEADSEERARELLARGL
>gnl|CDD|100091 cd03089, PMM_PGM, The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model
IFRAYDIRGIAGEELTEEIAYAIGRAFGSWLLEKGAKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDI
GLVPTPVLYFATFHLDADGGVMITASHNPPEYNGFKIVIGGGPLSGEDIQALRERAEKGDFAAATGRGSV
EKVDILPDYIDRLLSDIKLGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDPTD
PENLEDLIAAVKENGADLGIAFDGDGDRLGVVDEKGEIIWGDRLLALFARDILKRNPGATIVYDVKCSRN
LYDFIEEAGGKPIMWKTGHSFIKAKMKETGALLAGEMSGHIFFKDRWYGFDDGIYAALRLLELLSKSGKT
LSELLADLPKYFSTPEIRIPVTEEDKFAVIERLKEHFEFPGAEIIDIDGVRVDFEDGWGLVRASNTEPVL
VLRFEADTEEGLEEIKAELRKLL
>gnl|CDD|349762 cd03108, AdSS, adenylosuccinate synthetase. Adenylosuccinate synthetase (AdSS) catalyzes the first step in the de novo biosynthesis of AMP. IMP and L-aspartate are conjugated in a two-step reaction accompanied by the hydrolysis of GTP to GDP in the presence of Mg2+. In the first step, the r-phosphate group of GTP is transferred to the 6-oxygen atom of IMP. An aspartate then displaces this 6-phosphate group to form the product adenylosuccinate. Because of its critical role in purine biosynthesis, AdSS is a target of antibiotics, herbicides and antitumor drugs
KVTVVVGAQWGDEGKGKIVDYLAEKADIVVRFQGGNNAGHTVVVNGKKYKLHLLPSGILNPNATCVIGNG
VVIDPPALFEEIEELEKKGIDVKGRLLISDRAHLVFPYHQELDGLEEKERGGKKIGTTKRGIGPAYADKA
ARTGIRVGDPYVVDTVELLNEALKAGKKVLFEGAQGTLLDIDFGTYPYVTSSNTTAGGVCTGLGIPPRRV
DRVIGVVKAYTTRVGSGPFPTELFDEEGEKLRELGHEYGTTTGRPRRCGWLDLVALRYAVRINGLTELAL
TKLDVNAQKYIERIEELLGVPITYISVGPDREQTII
>gnl|CDD|349763 cd03109, DTBS, dethiobiotin synthetase. Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors
KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTGCPGLEDSDAELLRKLAGLLLDLELINPYR
FEAPLSPHLAAELEGRDIDLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVA
RGGLGTINHTLLTLEALKSRGLDVAGVVLNGIPPEPEAEADNAETLKEL
>gnl|CDD|349764 cd03110, SIMIBI_bact_arch, bacterial and archaeal subfamily of SIMIBI. Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown
IIAVLSGKGGTGKTTITANLAVLLYNVILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEKCIRCG
NCERVCKFGAILEFFQKLIVDESLCEGCGACVIICPRGAIYLKDRDTGKIFISSSDGGPLVHGRLNIGEE
NSGKLVTELRKKALERSKECDLAIIDGPPGTGCPVVASITGADAVLLVTEPTPSGLHDLKRAIELAKHFG
IPTGIVINRYDINDEISEEIEDFADEEGIPLLGKIP
>gnl|CDD|349765 cd03111, CpaE-like, pilus assembly ATPase CpaE. This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome
RVVAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQNLDRLDRT
LLDSAVTRHSSGLSLLPAPQELEDLEALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEIL
LVTQQDLPSLRNARRLLDSLRELEGSSDRLRLVLNRYDKKSEISPKDIEEALGLEVFATLPNDYKAVSES
ANTGRPLVEVAPRSALVRALQDLAA
>gnl|CDD|349766 cd03112, CobW-like, cobalamin synthesis protein CobW. The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterize it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K
PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGGGEEVVELSNGCICCTLKGD
LVKALEQLLERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEEDVSD
LAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG
>gnl|CDD|349767 cd03113, CTPS_N, N-terminal domain of cytidine 5'-triphosphate synthase. Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product
KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDL
GNYERFLDVNLTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPEPDVCIVEI
GGTVGDIESLPFLEALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCR
SEKPLDEETKEKIALFCNVPPEAVISVHDVSSIYEVPLLLEKQGLDDYILR
>gnl|CDD|349768 cd03114, MMAA-like, methylmalonic aciduria associated protein. Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems
ELIAGLRSGDRRALARAITLVESGRPDHRELAQELLDALLPQAGRAFRVGITGPPGAGKSTLIEALGRLL
REQGHRVAVLAVDPSSPRSGGSILGDKTRMQRLARDPNAFIRPSPSRGTLGGVARATREAILLCEAAGYD
VVLVETVGVGQSEVAVADMVDTFVLLLPPGGGDELQGIKAGIMEIADLVVVNKADGDLKTGARRAQRELT
SALKLLRPRSDGWRPPVLRTSALTGEGIDELWEAIEEHRAAL
>gnl|CDD|349769 cd03115, SRP_G_like, GTPase domain similar to the signal recognition particle subunit 54. The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain
NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASI
AQEAVEKAKLEGYDVLLVDTAGRLQKDEPLMEELKKVKEVESPDEVLLVLDATTGQEALSQAKAFNEAVG
LTGVILTKLDGTAKGGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL
>gnl|CDD|349770 cd03116, MobB, molybdopterin-guanine dinucleotide biosynthesis protein B. Molybdenum is an essential trace element in the form of molybdenum cofactor (Moco) which is associated with the metabolism of nitrogen, carbon and sulfur by redox active enzymes. In Escherichia coli, the synthesis of Moco involves genes from several loci: moa, mob, mod, moe and mog. The mob locus contains mobA and mobB genes. MobB catalyzes the attachment of the guanine dinucleotide to molybdopterin
KIVGVVGKSGSGKTTLIEKLIPELKARGLRVAVIKHTHHGFDIDTPGKDSYRHRQAGADAVLVSSPNRLA
LIHERPEWELTLLELLARFSDVDLVLVEGFKKEPIPKIEVFREEEGKPLLLPEDPNVIAVATDEPLDMLG
LPVFDLNDVEEIADFIL
>gnl|CDD|239391 cd03117, alpha_CA_IV_XV_like, Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This subgroup, restricted to animals, contains isozyme IV and similar proteins such as mouse CA XV. Isozymes IV is attached to membranes via a glycosylphosphatidylinositol (GPI) tail. In mammals, Isozyme IV plays crucial roles in kidney and lung function, amongst others. This subgroup also contains the dual domain CA from the giant clam, Tridacna gigas. T. gigas CA plays a role in the movement of inorganic carbon from the surrounding seawater to the symbiotic algae found in the clam's tissues. CA XV is expressed in several species but not in humans or chimps. Similar to isozyme CA IV, CA XV attaches to membranes via a GPI tail
GKRQSPINIVTKKVQYDENLTPFTFTGYDDTTTNWTITNNGHTVQVTLPDGAKISGGGLPGTYKALQFHF
HWGSNGSPGSEHTIDGERYPMELHIVHIKESYNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALS
NIPQKGGSTNLTPFSLRSLLPSVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFD
TDNGQPMVNNFRPVQPLNGRVVYA
>gnl|CDD|239392 cd03118, alpha_CA_V, Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme V. CA V is the mitochondrial isozyme, which may play a role in gluconeogenesis and ureagenesis and possibly also in lipogenesis
GTRQSPINIQWRDSVYDPQLAPLRVSYDPATCLYIWNNGYSFQVEFDDSTDKSGISGGPLENHYRLKQFH
FHWGANNEWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHHEGLQKLVDAL
PEVRHKDTVVEFNPFDPSCLLPACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLFTSR
GEEEKVMVNNFRPLQPLMNRKVRSSF
>gnl|CDD|239393 cd03119, alpha_CA_I_II_III_XIII, Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozymes I, II, and III, which are cytoplasmic enzymes. CA I, for example, is expressed in erythrocyes of many vertebrates; CA II is the most active cytosolic isozyme; while it is being expressed nearly ubiquitously, it comprises 95% of the renal carbonic anhydrase and is required for renal acidification; CA III has been implicated in protection from the damaging effect of oxidizing agents in hepatocytes. CAXIII may play important physiological roles in several organs
MSHHWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVSYDPATAKTILNNGHSFNVEF
DDTDDRSVLRGGPLTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNSKYGSFGEAAKQPDGL
AVVGVFLKVGEANPELQKVLDALDSIKTKGKQAPFTNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIV
LKEPISVSSEQMAKFRSLLFNAEGEPPCPMVDNWRPPQPLKGRKVRASF
>gnl|CDD|239394 cd03120, alpha_CARP_VIII, Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. CARP VIII may play roles in various biological processes of the central nervous system, and could be involved in protein-protein interactions. CARP VIII has been shown to bind inositol 1,4,5-triphosphate (IP3) receptor type I (IP3RI), reducing the affinity of the receptor for IP3. IP3RI is an intracellular IP3-gated Ca2+ channel located on intracellular Ca2+ stores. IP3RI converts IP3 signaling into Ca2+ signaling thereby participating in a variety of cell functions
GVEWGLLFPEANGEYQSPINLNSREARYDPSLLEVRLSPNYVVCRDCEVINDGHTIQIILKSKSVLSGGP
LPQGHEFELAEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIG
KEHVGLKAVTEILQDIQYKGKSKTIPCFNPNTLLPDPLLRDYWVYEGSLTTPPCSEGVTWILFRYPLTIS
QSQIEEFRRLRTHVKGAELVEGCDGLLGDNFRPTQPLSDRVIRAAF
>gnl|CDD|239395 cd03121, alpha_CARP_X_XI_like, Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup contains carbonic anhydrase related proteins (CARPs) X and XI, which have been implicated in various biological processes of the central nervous system. CARPs are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. CARP XI plays a role in the development of gastrointestinal stromal tumors
GPSFWGLVNSAWNLCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGTFYNTGRHVSFRPDKDPVVN
ISGGPLSYRYRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFV
KIGETSNPELRRLTNRDTITSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKP
IYITKEQMHSLRLLSQNSPSQEKAPMSPNFRPVQPLNNRPVRTNIN
>gnl|CDD|239396 cd03122, alpha_CARP_receptor_like, Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. This sub-family of carbonic anhydrase-related domains found in tyrosine phosphatase receptors may play a role in cell adhesion
NPKHWAKKYPACGEGRQQSPIDIVEDTQVQRQGLQPLHFDGYEELTASTTLENTGKTVILRLEGNSSDPF
VSGGPLLGRYKFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDSFEAIKSPGGVLALAYLFE
LSHEDNPFLDPIIEGLRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVP
ISSRQLEAFRELLTRRQDGVMSGDYLPNNGRPQQPLGSRTVFS
>gnl|CDD|239397 cd03123, alpha_CA_VI_IX_XII_XIV, Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Alpha CAs are mostly monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the secreted CA VI, which is found in saliva, for example, and the membrane proteins CA IX, XII, and XIV
GEDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHIRG
GPGTEYTAAQLHLHWGGRGSLSGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVG
YPENTYYEKIISHLHEIKYKGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLS
KEQLETLENTLMDTHNKTLQNNYRATQPLNGRVVEASF
>gnl|CDD|239398 cd03124, alpha_CA_prokaryotic_like, Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This sub-family includes bacterial carbonic anhydrase alpha, as well as plant enzymes such as tobacco nectarin III and yam dioscorin and, carbonic anhydrases from molluscs, such as nacrein, which are part of the organic matrix layer in shells. Other members of this family may be involved in maintaining pH balance, in facilitating transport of carbon dioxide or carbonic acid, or in sensing carbon dioxide levels in the environment. Dioscorin is the major storage protein of yam tubers and may play a role as an antioxidant. Tobacco Nectarin may play a role in the maintenace of pH and oxidative balance in nectar. Mollusc nacrein may participate in calcium carbonate crystal formation of the nacreous layer. This subfamily also includes three alpha carbonic anhydrases from Chlamydomonas reinhardtii (CAH 1-3). CAHs1-2 are localized in the periplasmic space. CAH1 faciliates the movement of carbon dioxide across the plasma membrane when the medium is alkaline. CAH3 is localized to the thylakoid lumen and provides CO2 to Rubisco
GPEHWGNLDPEFALCATGKNQSPIDITTKAVVSDKLPPLNYNYKPTSATLVNNGHTIQVNFEGNGGTLTI
DGETYQLLQFHFHSPSEHLINGKRYPLEAHLVHKSKDGQLAVVAVLFEEGKENPFLKKILDNMPKKEGTE
VNLPAILDPNELLPESRSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAAVYPNNARPVQPLN
GREVLL
>gnl|CDD|239399 cd03125, alpha_CA_VI, Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the secreted CA VI, which is found in saliva
DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNNGHTVQIDLPPTMSITTG
DGTVYTAVQMHFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSKYKSYEEAKDKPDGLAVLAFLYKVGH
YAENTYYSDFISKLAKIKYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLS
KTQIVKLENTLMDHHNKTIRNDYRRTQPLNHRVVEANFL
>gnl|CDD|239400 cd03126, alpha_CA_XII_XIV, Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the membrane proteins CA XII and XIV
GENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHIGG
LPFKYTASQLHLHWGQRGSPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVGP
FNPSYEKIFSHLHEVKYKDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQE
QLLALETALYSTEEDESREMVNNYRQVQPFNERLVFASF
>gnl|CDD|239401 cd03127, tetraspanin_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL). Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. The tetraspanin family contains CD9, CD63, CD37, CD53, CD82, CD151, and CD81, amongst others. Tetraspanins are involved in diverse processes such as cell activation and proliferation, adhesion and motility, differentiation, cancer, and others. Their various functions may relate to their ability to act as molecular facilitators, grouping specific cell-surface proteins and affecting formation and stability of signaling complexes. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web", which may also include integrins
FVYRDQLESLVSDTLNDAWDEYYVDDDFQEAMDALQSTFECCGVNGPTDYLDLRLLVPSSCCKGTDGNCG
LNLYTEGCLEKLVDFLRSNL
>gnl|CDD|153222 cd03128, GAT_1, Type 1 glutamine amidotransferase (GATase1)-like domain. Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain
VAVLLFGGSEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLAWDEALLA
LLREAAAAGKPVLGICLGAQLL
>gnl|CDD|153223 cd03129, GAT1_Peptidase_E_like, Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E_like proteins. Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E_like proteins. This group contains proteins similar to the aspartyl dipeptidases Salmonella typhimurium peptidase E and Xenopus laevis peptidase E and, extracellular cyanophycinases from Pseudomonas anguilliseptica BI (CphE) and Synechocystis sp. PCC 6803 CphB. In bacteria peptidase E is believed to play a role in degrading peptides generated by intracellular protein breakdown or imported into the cell as nutrient sources. Peptidase E uniquely hydrolyses only Asp-X dipeptides (where X is any amino acid), and one tripeptide Asp-Gly-Gly. Cyanophycinases are intracellular exopeptidases which hydrolyze the polymer cyanophycin (multi L-arginyl-poly-L-aspartic acid) to the dipeptide beta-Asp-Arg. Peptidase E and cyanophycinases are thought to have a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad typical of GATase1 domains by having a Ser in place of the reactive Cys at the nucleophile elbow. Xenopus peptidase E is developmentally regulated in response to thyroid hormone and, it is thought to play a role in apoptosis during tail reabsorption
LLLISGGGLDKAHARPILQDFLARAGGAGARVLFIPTASGDRDEYGEEYRAAFERLGVEVVHLLLIDTAN
DPDVVARLLEADGIFVGGGNQLRLLSVLRETPLLDAILKRVARGVVIGGTSAGAAVMGETGIGTTPSEPE
VTPPMAPGLGLLPGIIDPHFDSRGREGRLLELLAANPTPLGIGIDEGTALVVDGDGKAEVIGEGAVTVFD
>gnl|CDD|153224 cd03130, GATase1_CobB, Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase. Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase. CobB plays a role in cobalamin biosythesis catalyzing the conversion of cobyrinic acid to cobyrinic acid a,c-diamide. CobB belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobB
IAVARDEAFNFYYPENLELLEAAGAELVPFSPLKDEELPDADGLYLGGGYPELFAEELSANQSMRESIRA
FAESGGPIYAECGGLMYLGESLDDEEGQSYPMAGVLPGDARMTKRLGLGYREAEALGDTLLGKKGTTLRG
HEFHYSRLEPPPEPDFAATVRRGRGIDGGEDGYVYGNVLASYLHLHWASNPDLAERFV
>gnl|CDD|153225 cd03131, GATase1_HTS, Type 1 glutamine amidotransferase (GATase1)-like domain found in homoserine trans-succinylase (HTS). Type 1 glutamine amidotransferase (GATase1)-like domain found in homoserine trans-succinylase (HTS). HTS, the first enzyme in methionine biosynthesis in Escherichia coli, transfers a succinyl group from succinyl-CoA to homoserine forming succinyl homoserine. It has been suggested that the succinyl group of succinyl-CoA is initially transferred to an enzyme nucleophile before subsequent transfer to homoserine. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with GATase1 domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. It has been proposed that this cys is in the active site of the molecule. However, as succinyl has been found bound to a conserved lysine residue, this conserved cys may play a role in dimer formation. HTS activity is tightly regulated by several mechanisms including feedback inhibition and proteolysis. It represents a critical control point for cell growth and viability
IGILNLMPDKIQTERQFLRLLGNTPLQVEITFIRPSSHSSKNTPPEHVNRFYETFDDIRDAKFDGLIVTG
APVEHLPFEQVDYWEELTEILDWAKTHVTSTLFSCWAAMAALYYFYGIKKHQLPEKIFGVFPHTILEPHP
LLRGLDDGFDVPHSRYAEVDREDIEEAAGLTILAE
>gnl|CDD|153226 cd03132, GATase1_catalase, Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases. Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases. Catalase catalyzes the dismutation of hydrogen peroxide (H2O2) to water and oxygen. This group includes the large catalases: Neurospora crassa Catalase-1 and Catalase-3 and, Escherichia coli HP-II. This GATase1-like domain has an essential role in HP-II catalase activity. However, it lacks enzymatic activity and the catalytic triad typical of GATase1 domains. Catalase-1 and -3 are homotetrameric, HP-II is homohexameric. It has been proposed that this domain may facilitate the folding and oligomerization process. The interface between this GATase1-like domain of HP-II and the core of the subunit forms part of a channel which provides access to the deeply buried catalase active sites of HPII. Catalase-1 is associated with non-growing cells; Catalase-3 is associated with growing conditions. HP-II is produced in stationary phase. Catalase-1 is induced by ethanol and heat shock. Catalase-3 is induced under stress conditions such a hydrogen peroxide, paraquat, cadmium, heat shock, uric acid and nitrate treatment
GRKVGILVADGVDAAELSALKAALKAAGANVKVVAPTLGGVVDSDGKTLEVDQTYAGAPSVLFDAVVVPG
GAEAAFALAPSGRALHFVTEAFKHGKPIGAVGEGSDLLEAAGIPLEDPGVVTADDVKDVFTDRFIDALAL
HR
>gnl|CDD|153227 cd03133, GATase1_ES1, Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1. Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1. This group includes, proteins similar to ES1, Escherichia coli enhancing lycopene biosynthesis protein 2, Azospirillum brasilense iaaC and, human HES1. The catalytic triad typical of GATase1domains is not conserved in this GATase1-like domain. However, in common with GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Zebrafish ES1 is expressed specifically in adult photoreceptor cells and appears to be a cytoplasmic protein. A. brasilense iaaC is involved in controlling IAA biosynthesis
VAVVLSGCGVYDGSEIHEAVLTLLALDRAGAEVQCFAPDIEQMHVVNHLTGEAEGESRNVLVESARIARG
NIKDLAKLKAADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREFHQAGKPIGAICIAPALAAK
ILGEGVEVTIGNDAGTAAAIEKMGAEHVNCPVEEIVVDEKNKVVTTPAYMLADSIHEIADGIEKLVAKVL
KLA
>gnl|CDD|153228 cd03134, GATase1_PfpI_like, A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704
KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYDTVTVDLTIADVDADDYDALVIPG
GTNPDKLRRDPDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEV
VVDGNLITSRNPDDLPAFNRAILKA
>gnl|CDD|153229 cd03135, GATase1_DJ-1, Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme
VLVILADGFEEIEAVTPVDVLRRAGIEVTTASLEKKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGL
PGAQNLADNEKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFEDKLGGANYVDEPVVVD
GNIITSRGPGTAFEFALKIVEAL
>gnl|CDD|153230 cd03136, GATase1_AraC_ArgR_like, AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. A subgroup of AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to the Pseudomonas aeruginosa ArgR regulator. ArgR functions in the control of expression of certain genes of arginine biosynthesis and catabolism. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in some sequences in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow
FGFLLLPGFSLLALASAIEPLRAANRLAGRELYRWRVLSLDGAPVTSSNGLRVAPDAALEDAPPLDYLFV
VGGLGARRAVTPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAEAFPRVQVTR
DLFEIDGDRLTCAGGTAALDLMLELIARDHGAALAARVAEQFLHD
>gnl|CDD|153231 cd03137, GATase1_AraC_1, AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow
VAVLVFPGVSLLDLSGPAEVFGEANRALGPPAYELRVCSPEGGPVRSSSGLSLVADAGLDALAAADTVIV
PGGPDVDGRPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVD
PDVLYVDDGNVWTSAGVTAGIDLCLHLVREDLGAAVANRVARRLVVP
>gnl|CDD|153232 cd03138, GATase1_AraC_2, AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow
VTLLAYPGALASSLAGLLDLLRAANRLARRQQGGAPPFEVRLVSLDGGPVLLAGGILILPDATLADVPAP
DLVIVPGLGGDPDELLLADNPALIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRR
RFPKVRLDPDRVVVTDGNLITAGGAMAWADLALHLIERLAGPELAQLVARFLLID
>gnl|CDD|153233 cd03139, GATase1_PfpI_2, Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow
VGILLFPGVEVLDVIGPYEVFGRAPRLAAPFEVFLVSETGGPVSSRSGLTVLPDTSFADPPDLDVLLVPG
GGGTRALVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVVVDAR
WVVDGNIWTSGGVSAGIDMALALVARLFGEELAQAVALLIEYD
>gnl|CDD|153234 cd03140, GATase1_PfpI_3, Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow
IAVFLTDEFADWEGAYLAALLNSYEGFEVRTVSPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGD
SWDNPEAPDLAGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSNSLDFLKAHAPYYGGAEYYDEPQ
AVSDGNLITANGTAPVEFAAEILRALDVFT
>gnl|CDD|153235 cd03141, GATase1_Hsp31_like, Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein. Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein (EcHsp31). This group includes EcHsp31 and Saccharomyces cerevisiae Ydr533c protein. EcHsp31 has chaperone activity. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. EcHsp31 coordinates a metal ion using a 2-His-1-carboxylate motif present in various ions that use iron as a cofactor such as Carboxypeptidase A. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1 domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For EcHsp31, this Cys together with a different His and, an Asp (rather than a Glu) residue form a different catalytic triad from the typical GATase1 domain. For Ydr533c a catalytic triad forms from the conserved Cys together with a different His and Glu from that of the typical GATase1domain. Ydr533c protein and EcHsp31 are homodimers
ILIVLTSADKLGGTGRPTGLWLEELAHPYDVFTEAGYEVDFASPKGGKVPLDPRSLDAEDDDDASVFDND
EEFKKKLANTKKLSDVDPSDYDAIFIPGGHGPMFDLPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVK
LSDGKSLVAGKTVTGFTNEEEEAAGLKKVVPFLLEDELKELGANYVKAEPWAEFVVVDGRLITGQNPASA
AAVAEALVKAL
>gnl|CDD|153236 cd03142, GATase1_ThuA, Type 1 glutamine amidotransferase (GATase1)-like domain found in Sinorhizobium meliloti Rm1021 ThuA (SmThuA). Type 1 glutamine amidotransferase (GATase1)-like domain found in Sinorhizobium meliloti Rm1021 ThuA (SmThuA). This group includes proteins similar to SmThuA which plays a role in a major pathway for trehalose catabolism. SmThuA is induced by trehalose but not by related structurally similar disaccharides like sucrose or maltose. Proteins in this group lack the catalytic triad of typical GATase1 domains: a His replaces the reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. S. meliloti Rm1021 thuA mutants are impaired in competitive colonization of Medicago sativa roots but are more competitive than the wild-type Rml021 in infecting alfalfa roots and forming nitrogen-fixing nodules
VTVWNENRHEKADEAVAALYPDGMHGTIAAALAEYGFDVQTATLDEPEHGLTEEVLAETDVLLWWGHIAH
DEVKDEIVERVHRRVLDGMGLIVLHSGHYSKIFKKLMGTTCTLKWREAGERERVWVVEPGHPITDGIPEY
IELEQTEMYGEFFDIPTPDELVFVSWFEGGEVFRSGCTYRRGAGRIFYFSPGHETYPVYHHPDVQKVLAN
AVEWA
>gnl|CDD|153237 cd03143, A4_beta-galactosidase_middle_domain, A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group
VAIVFDYESWWALELQPQSAGLRYLDLALALYRALRELGIPVDVVPPDADLSGYKLVVLPDLYLLSDATA
AALRAYVENGGTLVAGPRSGAVDEHDAIPLGLPPPLGRLLGGLGVRVEELNAYGKGRAAWYVASLPDSGL
LVALLRRLAAEAGL
>gnl|CDD|153238 cd03144, GATase1_ScBLP_like, Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Saccharomyces cerevisiae biotin-apoprotein ligase (ScBLP). Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Saccharomyces cerevisiae biotin-apoprotein ligase (ScBLP). Biotin-apoprotein ligase modifies proteins by covalently attaching biotin. ScBLP is known to biotinylate acety-CoA carboxylase and pyruvate carboxylase. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, the Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in a typical GATase1 domain is conserved
NVLVYNGPGASPGSLKHLAELLRLYLAVSTVTADELAVGPWESKTALLVVPGGADLPYCRALNGKGNRRI
RNFVRNGGNYLGICAGAYLAYFNGGPVFEGADPEKGGNVEVLAR
>gnl|CDD|153239 cd03145, GAT1_cyanophycinase, Type 1 glutamine amidotransferase (GATase1)-like domain found in cyanophycinase. Type 1 glutamine amidotransferase (GATase1)-like domain found in cyanophycinase. This group contains proteins similar to the extracellular cyanophycinases from Pseudomonas anguilliseptica BI (CphE) and Synechocystis sp. PCC 6803 CphB. Cyanophycinases are intracellular exopeptidases which hydrolyze the polymer cyanophycin (multi L-arginyl-poly-L-aspartic acid) to the dipeptide beta-Asp-Arg. Cyanophycinase is believed to be a serine-type exopeptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad typical of GATase1 domains by having a Ser in place of the reactive Cys at the nucleophile elbow
KLVLIGGAEDKYDNRAILQRFVARAGGAGARIVVIPAASEEPAEVGEEYRDVFERLGAREVEVLVIDSRE
AANDPEVVARLRDADGIFFTGGDQLRITSALGGTPLLDALRKVYRGGVVIGGTSAGAAVMSDTMIAGGGA
GEAPRESEVDMAPGLGFVPNVIIDQHFSQRGRLGRLLTAVARNPAALGIGIDENTALVVDPDGRAEVIGE
GGVTIVD
>gnl|CDD|153240 cd03146, GAT1_Peptidase_E, Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E. Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E. This group contains proteins similar to the aspartyl dipeptidases Salmonella typhimurium peptidase E and Xenopus laevis peptidase E. In bacteria peptidase E is believed to play a role in degrading peptides generated by intracellular protein breakdown or imported into the cell as nutrient sources. Peptidase E uniquely hydrolyses only Asp-X dipeptides (where X is any amino acid), and one tripeptide Asp-Gly-Gly. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad typical of GATase1 domains by having a Ser in place of the reactive Cys at the nucleophile elbow. Xenopus PepE is developmentally regulated in response to thyroid hormone and, it is thought to play a role in apoptosis during tail reabsorption
KLLLTSGGGLGYLAHALPAIDDLLLSLTKARPKVLFVPTASGDRDEYTARFYAAFESLRGVEVSHLHLFD
TEDPLDALLEADVIYVGGGNTFNLLAQWREHGLDAILKAALERGVVYIGWSAGSNCWFPSIGTTDSMPIE
LPPSFNGLGLLPFQICPHYDSEDGETREERFHEFLEAGPTEPVIALDEGAALHVVGDGVADLLGEGAALV
FD
>gnl|CDD|153241 cd03147, GATase1_Ydr533c_like, Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein. Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein. This group includes proteins similar to S. cerevisiae Ydr533c. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. The catalytic triad typical of GATase1domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. This Cys together with a different His and Glu residue form a different catalytic triad from the typical GATase1domain. Ydr533c protein is a homodimer
KALIALTSYYGPFYPDGKNTGVFFSEALHPFNVFREAGFEVDFVSETGTFGFDDHSLDPDFLNGEDLEVF
SNKDSDFWKKLKNIKKADEVNPDDYGIFFVAGGHGTLFDFPHATNLQKIAQQIYANGGVVAAVCHGPAIL
ANLKDPKTGKPLIKGKTVTGFTDKGEEIMGVMEILKKRNLESIEDIAERAGANFIRPPGPWDDFTVVDGR
IVTGSNPASATSTAEAAIKAL
>gnl|CDD|153242 cd03148, GATase1_EcHsp31_like, Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 protein (EcHsp31). Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 protein (EcHsp31). This group includes proteins similar to EcHsp31. EcHsp31 has chaperone activity. EcHsp31 coordinates a metal ion using a 2-His-1-carboxylate motif present in various ions that use iron as a cofactor such as Carboxypeptidase A. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. This Cys together with a different His and, an Asp (rather than a Glu) residue form a different catalytic triad from the typical GATase1 domain. EcHsp31 is a homodimer
ILMIAADERYLPTDNGKLFSTGNHPVEMLLPLYHLHAAGFDFDVATLSGLPVKFEYWAMPHEDEAVMPFF
EKHKSKLRNPKKLADVVASLNADDSEYAAVFIPGGHGALIGIPESQDVAAALQWAIKNDRFVITLCHGPA
AFLAARHGGGKNPLEGYSVCVFPDSLDEGANIEIGYMPGHLTWLVGEELKKMGMNIINDDITGRVHKDRK
LLTGDSPLASNALGKLAAQEML
>gnl|CDD|239402 cd03149, alpha_CA_VII, Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme VII. CA VII is the most active cytosolic enzyme after CA II, and may be highly expressed in the brain. Human CA VII may be a target of antiepileptic sulfonamides/sulfamates
GNRQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLSISNNGHSVMVEFDDSDDKTVITGGPLENPYRLKQFH
FHWGAKHGSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETGDEHPGLNRLTDAL
YMVRFKGTKAQFLDFNPKCLLPKSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSE
EDQRNHMVNNFRPPQPLKGRTVRASF
>gnl|CDD|239403 cd03150, alpha_CA_IX, Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Alpha CAs are strictly monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the membrane protein CA IX. CA IX is functionally implicated in tumor growth and survival. CA IX is mainly present in solid tumors and its expression in normal tissues is limited to the mucosa of alimentary tract. CA IX is a transmembrane protein with two extracellular domains: carbonic anhydrase and, a proteoglycan-like segment mediating cell-cell adhesion. There is evidence for an involvement of the MAPK pathway in the regulation of CA9 expression
GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMAL
GPGQEYRALQLHLHWGAAGRPGSEHTVDGHRFPAEIHVVHLSTAFANLDEALGRPGGLAVLAAFLAEGLH
ENSAYEQLLSRLSEISEEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAK
QLHTLSDSLWGPHDSRLQLNFRATQPLNGRKIEASFP
>gnl|CDD|239404 cd03151, CD81_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), CD81_like subfamily. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". CD81, also referred to as Target for anti-proliferative antigen-1, TAPA-1, is found in virtually all tissues, may be involved in regulation of cell growth and has been described as a member of the CD19/CD21/Leu-13 signal transduction complex identified on B cells (the B-Cell co-receptor)
FINKDQIIKEVQNFYDSAYQDAVTDTRSKGTAVLKTFHSTLDCCGKGNLTALLSLLSTDLCPKKLLLDTK
DCHQEIDDLFSEKL
>gnl|CDD|239405 cd03152, CD9_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), CD9 family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". CD9 is found in virtually all tissues and is potentially involved in developmental processes. It associates with the tetraspanins CD81 and CD63, as well as with some integrin, and has been shown to be involved in a variety of activation, adhesion, and cell motility functions, as well as cell-cell interactions - such as during fertilization
FSNKDKVVKEVQTFYRQTYAKYKQSRDPPLKETLKAIHFALDCCGPTGGLEQFVTDTCPKKEGLENLITK
SCPDAIDDVFNSKL
>gnl|CDD|239406 cd03153, PHEMX_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), PHEMX_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Phemx (pan hematopoietic expression) or TSSC6 may play a role in hematopoietic cell function
LHSPTQVEDAVLDTYDLVYEQALKSISGSVRQELAAIQDTFLCCGKKSPFGLLGSTGATLCQGGEAMREV
AMLLCLFLWFAILSGHG
>gnl|CDD|239407 cd03154, TM4SF3_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF3_like subfamily. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This subfamily contaions transmembrane 4 superfamily 3 (TM4SF3) or D6.1a and related proteins. D6.1a associates with alpha6beta4 integrin and supports cell motility, it has been ascribed a role in tumor progression and metastasis
GIVGAVYKPKIENELKEKNTKLLSLLGQNAKSVKKSLEKFQKELKCCGLVNGADDWGNDIPASCNCTTTQ
SDCVVAYYGGSNVYKEPCISKIKDFLKKNL
>gnl|CDD|239408 cd03155, CD151_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), CD151_Like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". CD151strongly associates with integrins, especially alpha3beta1, alpha6beta1, alpha7beta1, and alpha6beta4; it may play roles in cell-cell adhesion, cell migration, platelet aggregation, and angiogenesis. For example, CD151 is is involved in regulation of migration of neutrophils, endothelial cells, and various tumor cell lines; it associates specifically with laminin-binding integrins and strengthens alpha6beta1 integrin-mediated adhesion to laminin-1; CD151 also specifically attenuates adhesion-dependent activation of Ras and correspdonding downstream effects, and is involved in epithelial cell-cell adhesion as a modulator of PKC- and Cdc42-dependent actin cytoskeletal reorganization
YTYYQQLEDELKESLKRTMQENYGQSGEEALTLTVDELQQEFKCCGSNNYTDWQDSEWINSNEANGRLVP
DSCCKTVVDRCGCLRDHPSNIYKVEGGCIPKLEDFLYDHL
>gnl|CDD|239409 cd03156, uroplakin_I_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), uroplakin_I_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Uroplakin Ia and Ib are components of the 16nm protein particles, which are packed hexagonally to form 2D crystals of asymmetric unit membranes, and cover the apical surface of mammalian urothelium, contributing to the urinay bladder's permeability barrier function. Uroplakins Ia and Ib are maturation facilitators. They trigger conformational changes in their single-transmembrane-domain binding partner proteins uroplakin II and IIIa, which in turn may lead to ER-exit, stabilization, and cell-surface expression
LALFFKKDLEDSFKNLLKNNYGNYNSTGDAITSTWNRVMIELKCCGVNGPTDFVDSTSFFRQKNEPNSPY
PESCCKRNSNSQIVDLDCPKLGSPNSYNKKGCYEKLSNPIERYA
>gnl|CDD|239410 cd03157, TM4SF12_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF12_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This sub-family contains proteins similar to human transmembrane 4 superfamily member 12 (TM4SF12)
WTYDEVPVQRSDMISLKSRMSNFGLQRYQWLTHAWNSFQTEFKCCGVIYFTDWLEMTEMEWPPDSCCSNQ
YPGCARQAHYNDLSDLYQEGCGPKIYSFIRGTK
>gnl|CDD|239411 cd03158, penumbra_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), penumbra_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Human Penumbra exhibits growth-suppressive activity in vitro and has been associated with myeloid malignancies
FIFSNQTIDLLEENIRKAIVHYYDDLDLQNIIDFVQKEFKCCGGDDYRDWSKNMYFNCSSPNPEACGVPY
SCCIRAKDQEVINTMCGYGVQNLERLEASKLIYTRGCIDAVVLWIEDNL
>gnl|CDD|239412 cd03159, TM4SF9_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF9_like subfamily. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This subfamily contaions transmembrane 4 superfamily 9 (TM4SF9) or Tetraspanin-5 and related proteins. TM4SF9 is strongly expressed witin the central nervous system, and expression levels appear to correlate with differentiation status of particular neurons, hinting at a role in neuronal maturation
FVFKDWIKDQLTEFLNNNIRAYRDDIDLQNLIDFLQEYWQCCGARGPDDWNLNIYFNCTDSNPSRERCGV
PFSCCVKDPAEDVVNTQCGYDVRKKPELELQHHIHTKGCVQAFEKWLQDNL
>gnl|CDD|239413 cd03160, CD37_CD82_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), CD37_CD82_Like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". CD37 is a leukocyte-specific protein, and its restricted expression pattern suggests a role in the immune system. A regulatory role in T-cell proliferation has been suggested. CD82 is a metastasis suppressor implicated in biological processes ranging from fusion, adhesion, and migration to apoptosis and alterations of cell morphology
IYFQRDKLKQEMGDIVEKVIQNYGGNPENKTAEEAWDYVQFQLQCCGWTGPQDWTDNSLIKNSSEPLYPC
SCCNSSATADSPRPSKGFCEAPASLDWPVYQEGCMEKLQSWLNENLG
>gnl|CDD|239414 cd03161, TM4SF2_6_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF2_6_like subfamily. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This subfamily contaions transmembrane 4 superfamily 2 (TM4SF2) or Tspan-7, transmembrane 4 superfamily 6 (TM4SF6) or Tspan-6, and related proteins. TM4SF2 has been identified as involved in some forms of X-linked mental retardation
FVFRHEIKGTFLRTYNEAVSNYNGDDERSDAVDTVQRTLHCCGVENYTDWLNSPYFLEKGIPLSCCKNRS
DCSPQDLKNLTKAATKVYQQGCFTLVTSFMEANM
>gnl|CDD|239415 cd03162, peripherin_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Peripherin, or RDS (retinal degradation slow) is a glycoprotein expressed in vertebrate photoreceptors, located at the rim of the disc membranes of the photoreceptor outer segments. RDS is thought to play a major role in folding and stacking of the discs. Mutations in RDS have been linked to hereditary retinal dystrophies, which typically exhibit a wide phenotypic spectrum
FIMRGSLEESLKTGLKNAMKFYKDTDTPGRCFLKKTIDMLQIEFQCCGNNGYRDWFEIQWISNRYLDFSS
KEVKDRIKSNVDGRYLTDGVPFSCCNPSSPRPCIQHQITDNSAHYNYDYQTEELNLWTRGCREALLEYYT
SKM
>gnl|CDD|239416 cd03163, TM4SF8_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF8_like subfamily. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This subfamily contaions transmembrane 4 superfamily 8 (TM4SF8) or Tspan-3 and related proteins. Tspan-3 has been reported to form a complex with integrin beta1 and OSP/claudin-11, which may be involved in oligodendrocyte proliferation and migration
GYVYRAKVEDELNPSIDKVFNKYNGTNAESRAVDYLQRQLQCCGIHNYTDWENTPWFKESKNNSVPLSCC
KETFTSCTGSLTQPKDLYQEGCEAKLVKKLQEVMM
>gnl|CDD|239417 cd03164, CD53_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), CD53_Like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". CD53 is a tetraspanin of the lymphoid-myeloid lineage and has been implicated in apoptosis protection. It associates with integrin alpha4beta1. Some of the cellular responses modulated by CD53 may be mediated by JNK activation and/or via the AKT pathway
FVYEKKLNNYVKEGLTDSLEQYHKDNNTSEAWDMIQSNLQCCGINGTTDWGSGVPSSCCSSDTEYKVEGC
YKKLKNWFESNFLYTG
>gnl|CDD|239418 cd03165, NET-5_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), NET-5_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This sub-family contains proteins similar to human tetraspan NET-5
FVFREKVDLTAKDDLKEGLELYGTRNNRGLTNAWDITQTEFRCCGVTNYTDWYEVLGENRVPDSCCQEDS
QDCGRNPTELWWKTGCYEKVQQWLVDNL
>gnl|CDD|239419 cd03166, CD63_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), CD63 family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". CD63 is present in platelets, neutrophils, and endothelial cells, amongst others. In platelets it associates with the integrin alphaIIBbeta3 and may modulate alphaIIbbeta3-dependent cytoskeletal reorganization
YVFRDKVMSEFNDSFNQMISNYNKTNDFRKILDRMQKDLKCCGANNYTDWENIPSLDTDSVPDSCCINVT
KGCGINFDEKVIHLEGCVTKIEGWLKKNI
>gnl|CDD|239420 cd03167, oculospanin_like_LEL, Tetraspanin, extracellular domain or large extracellular loop (LEL), oculospanin_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This subfamily contains sequences similar to oculospanin, which is found to be expressed in retinal pigment epithelium, iris, ciliary body, and retinal ganglion cells
VALWGPLQDGLEHTLRLAIAHYQDDPDLRFLIDQVQLGLQCCGASSYQDWQQNLYFNCSSPGVQACSLPA
SCCIDPREDGAVVNDQCGFGALGLDEDAAQRVVHLGGCGPPLRRWLRGNL
>gnl|CDD|153243 cd03169, GATase1_PfpI_1, Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow
KILILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFPGWQTYTEKPGHRFAVTADFD
EVDPDDYDALVIPGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKP
EVELAGGTVVDDGVVVDGNLVTAQAWPDHPAFLREFLKLL
>gnl|CDD|239421 cd03171, SORL_Dfx_classI, Superoxide reductase-like (SORL) domain, class I; SORL-domains are present in a family of mononuclear non-heme iron proteins that includes superoxide reductase and desulfoferrodoxin. Superoxide reductase-like proteins scavenge superoxide anion radicals as a defense mechanism against reactive oxygen species and are found in anaerobic bacteria and archeae, and microaerophilic Treponema pallidum. Desulfoferrodoxin (class I) is a homodimeric protein, with each protomer comprised of two domains, the N-terminal desulforedoxin (DSRD) domain and C-terminal SORL domain. Each domain has a distinct iron center: the DSRD iron center I, Fe(S-Cys)4; and the SORL iron center II, Fe[His4Cys(Glu)]
KEKHVPVIEKIGGGIKVKVGSVAHPMEEKHYIEWIELLADGKVYRKHLKPGDAPEAEFSVDADVVTARAY
CNLHGLWK
>gnl|CDD|239422 cd03172, SORL_classII, Superoxide reductase-like (SORL) domain, class II; SORL-domains are present in a family of mononuclear non-heme iron proteins that includes superoxide reductase and desulfoferrodoxin. Superoxide reductase-like proteins scavenge superoxide anion radicals as a defense mechanism against reactive oxygen species and are found in anaerobic bacteria and archeae, and microaerophilic Treponema pallidum. The SORL domain contains an active iron site, Fe[His4Cys(Glu)], which in the reduced state loses the glutamate ligand. Superoxide reductase (class II) forms a homotetramer with four Fe[His4Cys(Glu)] centers
KTDKEEKHVPVIECPEAVKAGEPFEVTVSVGKEIPHPNTTEHHIEWIELYFGVYLLGRVEFTAHGGVYTK
PEATFTVKIPKKGKKGKLVALSYCNIHGLWESEK
>gnl|CDD|176264 cd03173, DUF619-like, DUF619 domain of various N-acetylglutamate Kinases and N-acetylglutamate Synthases. DUF619-like: This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. This subgroup also includes the DUF619 domain of the FABP N-acetylglutamate kinase (NAGK), the enzyme that catalyzes the second reaction of arginine biosynthesis; the phosphorylation of the gamma-carboxyl group of NAG to produce N-acetylglutamylphosphate (NAGP) which is subsequently converted to ornithine in two more steps. The nuclear-encoded, mitochondrial polyprotein precursor (ARG5,6) consists of an N-terminal NAGK (ArgB) domain, a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-acetylglutamate phosphate reductase). The DUF619 domain function has yet to be characterized
ASYLKRLKNGKFASYADEPLEGVAIVTYEGNSIPYLDKFAVSDHLWLNNVTDNIFNLIRKDFPSLLWRVR
ENDANLKWYFSKSVGSLDKNGFILFWYG
>gnl|CDD|163674 cd03174, DRE_TIM_metallolyase, DRE-TIM metallolyase superfamily. The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM"
TDTTLRDGLQSEGATFSTEDKLEIAEALDEAGVDSIEVGSGASPKAVPQMEDDWEVLRAIRKLVPNVKLQ
ALVRNREKGIERALEAGVDEVRIFDSASETHSRKNLNKSREEDLENAEEAIEAAKEAGLEVEGSLEDAFG
CKTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLA
ALEAGADRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVEE
>gnl|CDD|198287 cd03177, GST_C_Delta_Epsilon, C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress
KKRAIVNQRLFFDSGTLYQRLRDYYYPILFGGAEPPEEKLDKLEEALEFLETFLEGSDYVAGDQLTIADL
SLVATVSTLEVVGFDLSKYPNVAAWYERLKALPPGEEENGEGAKELK
>gnl|CDD|198288 cd03178, GST_C_Ure2p_like, C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins. Glutathione S-transferase (GST) C-terminal domain family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p, YfcG and YghU from Escherichia coli, and related GST-like proteins. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. YfcG and YghU are two of the nine GST homologs in the genome of Escherichia coli. They display very low or no GSH transferase, but show very good disulfide bond oxidoreductase activity. YghU also shows modest organic hydroperoxide reductase activity. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of GSH with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain
ERAEVLQWLFFQMSGLGPMFGQAGHFLYFAPEKIPYAIERYTDEVKRLYGVLDKRLSDRPYLAGEEYSIA
DIALYPWTHYADLGGFADLSEYPNVKRWLERIAARPAVQK
>gnl|CDD|198289 cd03180, GST_C_2, C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 2; composed of uncharacterized bacterial proteins, with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain
AQRALADRWMDWQTSTLNPAFRYAFWGLVRTPPEQRDPAAIAASLAACNKLMAILDAQLARQAYLAGDRF
TLADIALGCSVYRWLELPIERPALPHLERWYARLSQRPAF
>gnl|CDD|198290 cd03181, GST_C_EF1Bgamma_like, Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins. Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds to membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF
EAAQVLQWISFANSELLPAAATWVLPLLGIAPYNKKAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLA
DIFVASALLRGFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKLCEKP
>gnl|CDD|198291 cd03182, GST_C_GTT2_like, C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces cerevisiae GST protein, GTT2. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock
TPLEKALIEMWQRRAELQGLAPVFQAFRHATPGLKPDREVQVPEWGERNKKRVIDFLPVLDKRLAESPYV
AGDRFSIADITAFVALDFAKNLKLPVPEELTALRRWYERMAARPSA
>gnl|CDD|198292 cd03183, GST_C_Theta, C-terminal, alpha helical domain of Class Theta Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial dichloromethane (DCM) dehalogenase. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Mammalian class Theta GSTs show poor GSH conjugating activity towards the standard substrates, CDNB and ethacrynic acid, differentiating them from other mammalian GSTs. GSTT1-1 shows similar cataytic activity as bacterial DCM dehalogenase, catalyzing the GSH-dependent hydrolytic dehalogenation of dihalomethanes. This is an essential process in methylotrophic bacteria to enable them to use chloromethane and DCM as sole carbon and energy sources. The presence of polymorphisms in human GSTT1-1 and its relationship to the onset of diseases including cancer is the subject of many studies. Human GSTT2-2 exhibits a highly specific sulfatase activity, catalyzing the cleavage of sulfate ions from aralkyl sufate esters, but not from the aryl or alkyl sulfate esters
KRARVDEYLAWQHTNLRLGCAAYFWQKVLLPLFGGTPVSPEKVKKAEENLEESLDLLENKFLKDKPFLAG
DEISIADLSAICEIMQPEAAGYDVFEGRPKLAAWRKRVKEAGNPLFDEAHKVIYKL
>gnl|CDD|198293 cd03184, GST_C_Omega, C-terminal, alpha helical domain of Class Omega Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases
YEKAQQKMLIERFSKVPSAFYKFLRSGEDRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWP
WFERLEALKLLDGYELCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY
>gnl|CDD|198294 cd03185, GST_C_Tau, C-terminal, alpha helical domain of Class Tau Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones
PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGGKPFFGGDTIGYLDIAL
GSFLGWFKAIEEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKAL
>gnl|CDD|198295 cd03186, GST_C_SspA, C-terminal, alpha helical domain of Stringent starvation protein A. Glutathione S-transferase (GST) C-terminal domain family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis
PVSRARSRLMMHRIEQDWYPLLDTILNGRDEKEAEKARKELRESLTALAPVFAASPYFLSEEFSLVDCYL
APLLWRLPALGIELPKQAKAIKDYMERVFARDSFQASL
>gnl|CDD|198296 cd03187, GST_C_Phi, C-terminal, alpha helical domain of Class Phi Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity
KERALVEQWLEVEAHQFDPPASKLVFELVFKPMLGLKTDEAVVEENEAKLKKVLDVYEARLSKSKYLAGD
SFTLADLSHLPNLHYLMATPSKKLFDSRPHVKAWWEDISARPAWKKVL
>gnl|CDD|198297 cd03188, GST_C_Beta, C-terminal, alpha helical domain of Class Beta Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they are involved in the protection against oxidative stress and are able to bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs, contributing to antibiotic resistance. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. One member of this subfamily is a GST from Burkholderia xenovorans LB400 that is encoded by the bphK gene and is part of the biphenyl catabolic pathway
LERARLLEWLNFIASELHKAFGPLFYPARWADDALAEEVKAAARERLERRLAYLDAQLAGGPYLLGDQFS
VADAYLFVVLRWARAVGLDLSDWPHLAAYLARVAARPAVQAAL
>gnl|CDD|198298 cd03189, GST_C_GTT1_like, C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals
PPPDTAEYADYLYWLHFAEGSLMPPLLLKLVFGKIGEAPPPFFRPISRKIADKPLQAFINPELKRHLDFL
EDHLAKHPYFAGDELTAADIMMSFPLEAALARGPLLEQYPNIAAYLERIEARP
>gnl|CDD|198299 cd03190, GST_C_Omega_like, C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae Omega-like subfamily; composed of three Saccharomyces cerevisiae GST omega-like (Gto) proteins, Gto1p, Gto2p (also known as Extracellular mutant protein 4 or ECM4p), and Gto3p, as well as similar uncharacterized proteins from fungi and bacteria. The three Saccharomyces cerevisiae Gto proteins are omega-class GSTs with low or no GST activity against standard substrates, but have glutaredoxin/thiol oxidoreductase and dehydroascorbate reductase activity through a single cysteine residue in the active site. Gto1p is located in the peroxisomes while Gto2p and Gto3p are cytosolic. The gene encoding Gto2p, called ECM4, is involved in cell surface biosynthesis and architecture. S. cerevisiae ECM4 mutants show increased amounts of the cell wall hexose, N-acetylglucosamine. More recently, global gene expression analysis shows that ECM4 is upregulated during genotoxic conditions and together with the expression profiles of 18 other genes could potentially differentiate between genotoxic and cytotoxic insults in yeast
PEELRKEIDELNEWIYDNINNGVYKAGFATTQEAYDKAVKELFEALDKLEKRLSKQPYLLGDRLTEADIR
LFTTLIRFDPVYHQHFKCNLKTIRDYPNLWRYLRRLYQNPGVFETTNFDHIKQHYYGSHFPINPNGIVPA
GP
>gnl|CDD|198300 cd03191, GST_C_Zeta, C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Class Zeta GSTs, also known as maleylacetoacetate (MAA) isomerases, catalyze the isomerization of MAA to fumarylacetoacetate, the penultimate step in tyrosine/phenylalanine catabolism, using GSH as a cofactor. They show little GSH-conjugating activity towards traditional GST substrates, but display modest GSH peroxidase activity. They are also implicated in the detoxification of the carcinogen dichloroacetic acid by catalyzing its dechlorination to glyoxylic acid
PKKRARVRAIALIIACDIHPLQNLRVLKYLTEKLGVSEEEKLAWAQHWIERGFQALEKLLASTAGKYCVG
DEPTLADICLVPQVYNARRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ
>gnl|CDD|198301 cd03192, GST_C_Sigma_like, C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi, and Alpha. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation, and mediation of allergy and inflammation. Other class Sigma-like members include the class II insect GSTs, S-crystallins from cephalopods, nematode-specific GSTs, and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase, and PGD2 synthase activities, and may play an important role in host-parasite interactions. Members also include novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST
EEEARVDAIVDTIADLRAEFAPYFYEPDGEEKKEKKKEFLEEALPKFLGKFEKILKKSGGGYFVGDKLTW
ADLALFDVLDYLLYLLPKDLLEKYPKLKALRERV
>gnl|CDD|198302 cd03193, GST_C_Metaxin, C-terminal, alpha helical domain of Metaxin and related proteins. Glutathione S-transferase (GST) C-terminal domain family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. Metaxin 2 binds to metaxin 1 and may also play a role in protein translocation into the mitochondria. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken, and mammals. Sequence analysis suggests that all three metaxins share a common ancestry and that they possess similarity to GSTs. Also included in the subfamily are uncharacterized proteins with similarity to metaxins, including a novel GST from Rhodococcus with toluene o-monooxygenase and glutamylcysteine synthetase activities. Other members are the cadmium-inducible lysosomal protein CDR-1 and its homologs from C. elegans, and the failed axon connections (fax) protein from Drosophila. CDR-1 is an integral membrane protein that functions to protect against cadmium toxicity and may also have a role in osmoregulation to maintain salt balance in C. elegans. The fax gene of Drosophila was identified as a genetic modifier of Abelson (Abl) tyrosine kinase. The fax protein is localized in cellular membranes and is expressed in embryonic mesoderm and axons of the central nervous system
ARALSRMVETHLYWALRREIYELALEDLEALSTLLGDKKFLFGDKPTSVDATVFAHLASILYPPEDSPLL
RVLVASSPNLVEYCERIR
>gnl|CDD|198303 cd03194, GST_C_3, C-terminal, alpha helical domain of an unknown subfamily 3 of Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 3; composed of uncharacterized proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain
RAARALARSACAEMHSGFSALRSACPMNLRARRPGVELSPAVQADIARIEAIWTEARARFGAGGPFLFGE
FSIADAFYAPVVTRFRTYGVPLSPAARAYVEALLALPAMQEWIEA
>gnl|CDD|198304 cd03195, GST_C_4, C-terminal, alpha helical domain of an unknown subfamily 4 of Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 4; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain
PRARARARQVQAWLRSDLLPLRQERPTEVVFYGPAVTPLSEAAQAAAEKLFAVAEALLPAGAAFLFGAWS
IADTDLALMLNRLVLNGDPVPQRLADYAERQWQRPSVQAWLALP
>gnl|CDD|198305 cd03196, GST_C_5, C-terminal, alpha helical domain of an unknown subfamily 5 of Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 5; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain
SLDPGALPEMLALIAENDGPFKPHLDRYKYADRYPEDDEEEYRAQAEEFLAELEARLSQHAYLFGDRPSL
ADYAIFPFVRQFAHVDRDWFDASPYPNLRRWLNRFLQSPLFSKIM
>gnl|CDD|198306 cd03197, GST_C_mPGES2, C-terminal, alpha helical domain of microsomal Prostaglandin E synthase Type 2. Glutathione S-transferase (GST) C-terminal domain family, microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a membrane-anchored dimeric protein containing a CXXC motif which catalyzes the isomerization of PGH2 to PGE2. Unlike cytosolic PGE synthase (cPGES) and microsomal PGES Type 1 (mPGES1), mPGES2 does not require glutathione (GSH) for its activity, although its catalytic rate is increased two- to four-fold in the presence of DTT, GSH, or other thiol compounds. PGE2 is widely distributed in various tissues and is implicated in the sleep/wake cycle, relaxation/contraction of smooth muscle, excretion of sodium ions, maintenance of body temperature, and mediation of inflammation. mPGES2 contains an N-terminal hydrophobic domain which is membrane associated and a C-terminal soluble domain with a GST-like structure. The C-terminal GST-like domain contains two structural domains, an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST active site is located in a cleft between the two structural domains
AQLADPEEKKWRKWVDDVLVHLLSPNIYRTFSEALQAFDYITTVGNFGPWERIVAKYVGAAAMYLISKRL
KKKRNIKDDVRESLYDALNDWVKALGKKRKFHGGSKPNLADLAVYGVLRSIEGLDAFKDVLANTKIGPWY
ERMKEAVGS
>gnl|CDD|198307 cd03198, GST_C_CLIC, C-terminal, alpha helical domain of Chloride Intracellular Channels. Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLICs (CLIC1-6 in vertebrates), p64, parchorin, and similar proteins. They are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. Biochemical studies of the Caenorhabditis elegans homolog, EXC-4, show that the membrane localization domain is present in the N-terminal part of the protein. CLICs display structural plasticity, with CLIC1 adopting two soluble conformations. The structure of soluble human CLIC1 reveals that it is monomeric and adopts a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. Upon oxidation, the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. The CLIC1 dimer bears no similarity to GST dimers. The redox-controlled structural rearrangement exposes a large hydrophobic surface, which is masked by dimerization in vitro. In vivo, this surface may represent the docking interface of CLIC1 in its membrane-bound state. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity, however, in other subfamily members, the second cysteine is not conserved
NPEANTAGEDLFAKFSAYIKNKDPAADEALRKALLKELSKLDAYLSSSSRKFLDGDTLTLADCNLLPKLH
HIRVAGKAYKDFDIPDDFTGLWRYLKNAYETDEFTKTCPADQEIILHYK
>gnl|CDD|198308 cd03199, GST_C_GRX2, C-terminal, alpha helical domain of Glutaredoxin 2. Glutathione S-transferase (GST) C-terminal domain family, Glutaredoxin 2 (GRX2) subfamily; composed of Escherichia coli GRX2 and similar proteins. Escherichia coli GRX2 is an atypical GRX with a molecular mass of about 24kD (most GRXs range from 9-12kD). It adopts a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. It contains a redox active CXXC motif located in the N-terminal domain, but is not able to reduce ribonucleotide reductase like other GRXs. However, it catalyzes GSH-dependent protein disulfide reduction of other substrates efficiently. GRX2 is thought to function primarily in catalyzing the reversible glutathionylation of proteins in cellular redox regulation including stress responses
RPEIAAWLKQVGPYYNRLLLPRFAKADLPEFATPSARAYFIRKKEASIGSFEELLAKTPELIAELNADLE
ALDPLILSSDAVNGELSYDDIILFPLLRNLTIVKGLEFPPKVRAYIDNMSALSDVPLY
>gnl|CDD|198309 cd03200, GST_C_AIMP2, Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2. Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 2 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP2, also called p38 or JTV-1, contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It plays an important role in the control of cell fate via antiproliferative (by enhancing the TGF-beta signal) and proapoptotic (activation of p53 and TNF-alpha) activities. Its roles in the control of cell proliferation and death suggest that it is a potent tumor suppressor. AIMP2 heterozygous mice with lower than normal expression of AIMP2 show high susceptibility to tumorigenesis. AIMP2 is also a substrate of Parkin, an E3 ubiquitin ligase that is involved in the ubiquitylation and proteasomal degradation of its substrates. Mutations in the Parkin gene is found in 50% of patients with autosomal-recessive early-onset parkinsonism. The accumulation of AIMP2, due to impaired Parkin function, may play a role in the pathogenesis of Parkinson's disease
ARFLFRLLGDESDDPVNATLIDSWVDTAIFQLLEGSSKEKAAVLRALNSALGRSPWLVGSEPTVADIALW
SAVLQTGLASGAPANVQRWMKSCENL
>gnl|CDD|198310 cd03201, GST_C_DHAR, C-terminal, alpha helical domain of Dehydroascorbate Reductase. Glutathione S-transferase (GST) C-terminal domain family, Dehydroascorbate Reductase (DHAR) subfamily; composed of plant-specific DHARs, which are monomeric enzymes catalyzing the reduction of DHA into ascorbic acid (AsA) using glutathione as the reductant. DHAR allows plants to recycle oxidized AsA before it is lost. AsA serves as a cofactor of violaxanthin de-epoxidase in the xanthophyll cycle and as an antioxidant in the detoxification of reactive oxygen species. Because AsA is the major reductant in plants, DHAR serves to regulate their redox state. It has been suggested that a significant portion of DHAR activity is plastidic, acting to reduce the large amounts of ascorbate oxidized during hydrogen peroxide scavenging by ascorbate peroxidase. DHAR contains a conserved cysteine in its active site and in addition to its reductase activity, shows thiol transferase activity similar to glutaredoxins
LKTPPEFASVGSKIFSTFVTFLKSKDANDGSEQALLDELTALDEHLKTNGPFIAGEKITAVDLSLAPKLY
HLRVALGHYKGWSVPESLTAVHKYMELLFSRESFKKTKAPDEMIIAGWAPK
>gnl|CDD|198311 cd03202, GST_C_etherase_LigE, C-terminal, alpha helical domain of Beta etherase LigE. Glutathione S-transferase (GST) C-terminal domain family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas paucimobilis beta etherase, LigE, a GST-like protein that catalyzes the cleavage of the beta-aryl ether linkages present in low-moleculer weight lignins using GSH as the hydrogen donor. This reaction is an essential step in the degradation of lignin, a complex phenolic polymer that is the most abundant aromatic material in the biosphere. The beta etherase activity of LigE is enantioselective and it complements the activity of the other GST family beta etherase, LigF. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains
LARFVESWSDLTLHPALARLILLDIHDRLDPADRDYFRQSREARFGRTLEEVAAGREERLAAFRAALEPL
RLTLAGQPFLGGAAPNYADYIVFGAFQWARSVSPLPLLEADDPVAAWRERMLDL
>gnl|CDD|198312 cd03203, GST_C_Lambda, C-terminal, alpha helical domain of Class Lambda Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Class Lambda subfamily; composed of plant-specific class Lambda GSTs. GSTs are cytosolic, usually dimeric, proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Lambda subfamily was recently discovered, together with dehydroascorbate reductases (DHARs), as two outlying groups of the GST superfamily in Arabidopsis thaliana, which contain conserved active site cysteines. Characterization of recombinant A. thaliana proteins show that Lambda class GSTs are monomeric, similar to DHARs. They do not exhibit GSH conjugating or DHAR activities, but are active as thiol transferases, similar to glutaredoxins. Members of this subfamily were originally identified as encoded proteins of the In2-1 gene, which can be induced by treatment with herbicide safeners
DPAKREFADELLAYADTFTKAVYSALIKGDMTAEAAAAFDYLENALSKFDDGPFFLGQFSLVDIAYAPFI
ERFQIVLSELRNYDITAGRPNLAKWIEEMNKIEAYTQTKVDPEELLELYK
>gnl|CDD|198313 cd03204, GST_C_GDAP1_like, C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein 1-like proteins. Glutathione S-transferase (GST) C-terminal domain family, Ganglioside-induced differentiation-associated protein 1 (GDAP1)-like subfamily; GDAP1 was originally identified as a highly expressed gene at the differentiated stage of GD3 synthase-transfected cells. More recently, mutations in GDAP1 have been reported to cause both axonal and demyelinating autosomal-recessive Charcot-Marie-Tooth (CMT) type 4A neuropathy. CMT is characterized by slow and progressive weakness and atrophy of muscles. Sequence analysis of GDAP1 shows similarities and differences with GSTs; it appears to contain both N-terminal thioredoxin-fold and C-terminal alpha helical domains of GSTs, however, it also contains additional C-terminal transmembrane domains unlike GSTs. GDAP1 is mainly expressed in neuronal cells and is localized in the mitochondria through its transmembrane domains. It does not exhibit GST activity using standard substrates
PDLAEAYTAKQKKLAIQLRDHEDSSYLKKILDELEVVLDQVEKELGERKRETDESGQQQWLCGESFTAAD
ISLSVLLHRLKFLGLSRRFWGNGKRPNIESYFERVRQRESF
>gnl|CDD|198314 cd03205, GST_C_6, C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization
ALRLEALADGICDAAVLIVYERRLRPEEKQHQPWIERQWGKIERALDALEAELGDLPGGRLTLGDIAVAC
ALGYLDFRFPELDWRAGHPALAAWFARFEARPSFQATPP
>gnl|CDD|198315 cd03206, GST_C_7, C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 7; composed of uncharacterized proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain
VQRWLSFAAGEIAHGPAAARLIHLFGAPLDPERARAISHRLLRLLDQHLAGRDWLAGDRPTIADVACYPY
IALAPEGGVSLEPYPAIRAWLARVEALPGF
>gnl|CDD|198316 cd03207, GST_C_8, C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization
YLRWLFFAAGTVEPPLLNKALGRFFEPPWGEPAIAAAYGDLDERLAALEAALAGRPYLVGERFSAADLLL
ASVLRWARAFGLLPEYPALRAYVARCTARPA
>gnl|CDD|198317 cd03208, GST_C_Alpha, C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Alpha subfamily is composed of vertebrate GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals
LKERALIDMYVEGTADLMEMIMMLPFLPPEEKEAKLALIKEKAKNRYFPVFEKVLKDHGQDFLVGNKLSR
ADVQLLEAILMVEELDPSILSDFPLLQAFKTRISNIPTIKKFLQPGSKRKPPPDEKYVETVRKVF
>gnl|CDD|198318 cd03209, GST_C_Mu, C-terminal, alpha helical domain of Class Mu Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1) thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation
KERIRVDMLEQQAMDLRMGLIRICYSPDFEKLKPDYLEKLPDKLKLFSEFLGDRPWFAGDKITYVDFLLY
EALDQHRIFEPDCLDAFPNLKDFLERFEALPKISAYMKSDRFIKWPINGWK
>gnl|CDD|198319 cd03210, GST_C_Pi, C-terminal, alpha helical domain of Class Pi Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Class Pi subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Class Pi GST is a homodimeric eukaryotic protein. The human GSTP1 is mainly found in erythrocytes, kidney, placenta and fetal liver. It is involved in stress responses and in cellular proliferation pathways as an inhibitor of JNK (c-Jun N-terminal kinase). Following oxidative stress, monomeric GSTP1 dissociates from JNK and dimerizes, losing its ability to bind JNK and causing an increase in JNK activity, thereby promoting apoptosis. GSTP1 is expressed in various tumors and is the predominant GST in a wide range of cancer cells. It has been implicated in the development of multidrug-resistant tumors
EKEAALIDMVNDGVEDLRLKYVRMIYQNYEAGKDDYIKDLPEQLKPFEKLLAKNNGKGFIVGDKISFADY
NLFDLLDIHLVLAPGCLDAFPLLKAFVERLSARPKLKAYLESDAFKNRPINGNGKQ
>gnl|CDD|198320 cd03211, GST_C_Metaxin2, C-terminal, alpha helical domain of Metaxin 2. Glutathione S-transferase (GST) C-terminal domain family, Metaxin subfamily, Metaxin 2; a metaxin 1 binding protein identified through a yeast two-hybrid system using metaxin 1 as the bait. Metaxin 2 shares sequence similarity with metaxin 1 but does not contain a C-terminal mitochondrial outer membrane signal-anchor domain. It associates with mitochondrial membranes through its interaction with metaxin 1, which is a component of the mitochondrial preprotein import complex of the outer membrane. The biological function of metaxin 2 is unknown. It is likely that it also plays a role in protein translocation into the mitochondria. However, this has not been experimentally validated. In a recent proteomics study, it has been shown that metaxin 2 is overexpressed in response to lipopolysaccharide-induced liver injury
AELYISWCDEETYNEVTKPRYGSVYPWPLNHILAYRKQREVLRKLKALGWSDKSLDQVFDEVEKCCQALS
EKLGTNQYFFGDQPTELDALVFGHLFTILTTPLPNDELAAIVKKYPNLVEFCRRIE
>gnl|CDD|198321 cd03212, GST_C_Metaxin1_3, C-terminal, alpha helical domain of Metaxin 1, Metaxin 3, and similar proteins. Glutathione S-transferase (GST) C-terminal domain family, Metaxin subfamily, Metaxin 1-like proteins; composed of metaxins 1 and 3, and similar proteins. Mammalian metaxin (or metaxin 1) is a component of the preprotein import complex of the mitochondrial outer membrane. Metaxin extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. Like the murine gene, the human metaxin gene is located downstream to the glucocerebrosidase (GBA) pseudogene and is convergently transcribed. Inherited deficiency of GBA results in Gaucher disease, which presents many diverse clinical phenotypes. Alterations in the metaxin gene, in addition to GBA mutations, may be associated with Gaucher disease. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken, and mammals
PALLYTLWVDEKNYVEVTRPWYAKALPFPLNFYYPGRYQRRAKDRLQLLRGLSELDSEEEVEKELYKDAK
ECLNLLSERLGEKKFFFGDRPTSLDALVFGYLAPLLKAPLPNNKLQNHLKGCPNLVQFVDRILQNYF
>gnl|CDD|213180 cd03213, ABCG_EPDR, Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily. ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus
GVTLSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLI
NGRPLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTS
GLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG
>gnl|CDD|213181 cd03214, ABC_Iron-Siderophores_B12_Hemin, ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins. ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters
EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE
LARKIAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELL
RRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG
>gnl|CDD|213182 cd03215, ABC_Carb_Monos_II, Second domain of the ATP-binding cassette component of monosaccharide transport system. This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter
GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPR
DAIRAGIAYVPEDRKREGLVLDLSVAENIALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK
AEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI
>gnl|CDD|213183 cd03216, ABC_Carb_Monos_I, First domain of the ATP-binding cassette component of monosaccharide transport system. This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter
LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR
DARRAGIAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISH
RLDEVFEIADRVTVLRDGRVVGT
>gnl|CDD|213184 cd03217, ABC_FeS_Assembly, ABC-type transport system involved in Fe-S cluster assembly, ATPase component. Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet
LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDITDLP
PEERARLGIFLAFQYPPEIPGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL
RLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRIVKSGDKELALEIEKKGY
>gnl|CDD|213185 cd03218, ABC_YhbG, ATP-binding cassette component of YhbG transport system. The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium
LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH
KRARLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERR
RVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK
VLAEGTPEEIAANELVRKVYLG
>gnl|CDD|213186 cd03219, ABC_Mj1267_LivG_branched, ATP-binding cassette component of branched chain amino acids transport system. The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ)
LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH
EIARLGIGRTFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRP
AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLA
DRVTVLDQGRVIAEGTPDEVRNNPRV
>gnl|CDD|213187 cd03220, ABC_KpsT_Wzt, ATP-binding cassette component of polysaccharide transport system. The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2
IELENVSKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG
IYPPDSGTVTVRGRVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPV
KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCD
RALVLEKGKIRFDG
>gnl|CDD|213188 cd03221, ABCF_EF-3, ATP-binding cassette domain of elongation factor 3, subfamily F. Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions
IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ
LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIEL
EDGK
>gnl|CDD|213189 cd03222, ABC_RNaseL_inhibitor, ATP-binding cassette domain of RNase L inhibitor. The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology
QLYPDCVKRYGVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI
DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSD
RIHVFEGEPGVYGIASQPKGTREGINRFLRGYLITFR
>gnl|CDD|213190 cd03223, ABCD_peroxisomal_ALDP, ATP-binding cassette domain of peroxisomal transporter, subfamily D. Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic)
IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLP
QRPYLPLGTLREQLIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGIT
VISVGHRPSLWKFHDRVLDLDGEGGW
>gnl|CDD|213191 cd03224, ABC_TM1139_LivF_branched, ATP-binding cassette domain of branched-chain amino acid transporter. LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules
LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH
ERARAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQM
LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRV
VLEGTAAELLAD
>gnl|CDD|213192 cd03225, ABC_cobalt_CbiO_domain1, First domain of the ATP-binding cassette component of cobalt transport system. Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems
ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSL
KELRRKVGLVFQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQK
QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG
K
>gnl|CDD|213193 cd03226, ABC_cobalt_CbiO_domain2, Second domain of the ATP-binding cassette component of cobalt transport system. Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems
RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR
KSIGYVMQDVDYQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAA
LLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV
>gnl|CDD|213194 cd03227, ABC_Class2, ATP-binding cassette domain of non-transporter proteins. ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins
KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVAAVSAE
LIFTRLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL
PELAELADKLIHIKKVITGVYK
>gnl|CDD|213195 cd03228, ABCC_MRP_Like, ATP-binding cassette domain of multidrug resistance protein-like transporters. The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD
LESLRKNIAYVPQDPFLFSGTIRENILSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALR
ALAKGKTVIVIAHRLSTIRDADRIIVLDDGR
>gnl|CDD|213196 cd03229, ABC_Class3, ATP-binding cassette domain of the binding protein-dependent transport systems. This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE
LPPLRRRIGMVFQDFALFPHLTVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVR
ALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK
>gnl|CDD|213197 cd03230, ABC_DR_subfamily_A, ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A. This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE
VKRRIGYLPEEPSLYENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRE
LKKEGKTILLSSHILEEAERLCDRVAILNNGRI
>gnl|CDD|213198 cd03231, ABC_CcmA_heme_exporter, Cytochrome c biogenesis ATP-binding export protein. CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE
LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS
IARGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLL
LSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLGFK
>gnl|CDD|213199 cd03232, ABCG_PDR_domain2, Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters. The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
GSVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILING
RPLDKNFQRSTGYVEQQDVHSPNLTVREALRFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD
SQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG
>gnl|CDD|213200 cd03233, ABCG_PDR_domain1, First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters. The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYN
GIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCKGNEFVRGISGGERKRVSIAEALVSRASVL
CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG
>gnl|CDD|213201 cd03234, ABCG_White, White pigment protein homolog of ABCG transporter subfamily. The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners
QRVLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFN
GQPRKPDQFQKCVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNL
VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRL
FDRILLLSSGEIVYSG
>gnl|CDD|213202 cd03235, ABC_Metallic_Cations, ATP-binding cassette domain of the metal-type transporters. This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates
EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRI
GYVPQRRSIDRDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQR
VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV
ASG
>gnl|CDD|213203 cd03236, ABC_RNaseL_inhibitor_domain1, The ATP-binding cassette domain 1 of RNase L inhibitor. The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology
ELEDEPVHRYGPNSFKLHRLPVPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEF
RGSELQNYFTKLLEGDVKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQL
SGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIH
CLYGEPGAYGVVTLPKSVREGINEFLDGYLPTENMRFREESIEFE
>gnl|CDD|213204 cd03237, ABC_RNaseL_inhibitor_domain2, The ATP-binding cassette domain 2 of RNase L inhibitor. The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology
YTYPTMKKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYI
KADYEGTVRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLD
EPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVANPPQSLRSGMN
RFLKNLDITFRRDPETGRPRINKLGSVKDREQKESG
>gnl|CDD|213205 cd03238, ABC_UvrA, ATP-binding cassette domain of the excision repair protein UvrA. Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases
LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKLIFIDQLQF
LIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGN
TVILIEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG
>gnl|CDD|213206 cd03239, ABC_SMC_head, The SMC head domain belongs to the ATP-binding cassette superfamily. The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains, and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression
IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGGVKAGI
NSASVEITFDKSYFLVLQGKVEQILSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDM
IKEMAKHTSQFIVITLKKEMFENADKLIGVLFVHGVST
>gnl|CDD|213207 cd03240, ABC_Rad50, ATP-binding cassette domain of Rad50. The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence
IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIREGEVR
AQVKLAFENANGKKYTITRSLAILENVIFCHQGESNWPLLDMRGRCSGGEKVLASLIIRLALAETFGSNC
GILALDEPTTNLDEENIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVEKDGRQKSR
>gnl|CDD|213208 cd03241, ABC_RecN, ATP-binding cassette domain of RecN. RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDIS
DEEEAKALLLELGIEDDDDLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPER
QLDLLDGGLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVA
QAVGKKLKELSRSHQVLCITHLPQVAAMADNHFLVEKEVEGGRTVTKVRELDKEERVEEIARMLSG
>gnl|CDD|213209 cd03242, ABC_RecF, ATP-binding cassette domain of RecF. RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKSHRTSRDKELIRWGAEEAKISA
VLERQGGELALELTIRSGGGRKARLNGIKVRRLSDLLGVLNAVWFAPEDLELVKGSPADRRRFLDRLLGQ
LEPAYAHVLSEYQKALRQRNALLKGPHRDDLLFFLNDKPAADFGSQGQQRTLALALKLAEIQLIKEVSGE
YPVLLLDDVLAELDLGRQAALLDAIEGRVQTFVTTTDLADFDALWLRRAQIFRVDAGTLS
>gnl|CDD|213210 cd03243, ABC_MutS_homologs, ATP-binding cassette domain of MutS homologs. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange
EIKGGRHPVLLALTKGETFVPNDINLGSGRLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIP
LVDRIFTRIGAEDSISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEK
GCRTLFATHFHELADLPEQVPGVKNLHMEELITTGGLTFTYKLIDGICDPSYALQIAELAGL
>gnl|CDD|213211 cd03244, ABCC_MRP_domain2, ATP-binding cassette domain 2 of multidrug resistance-associated protein. The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate
GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISK
IGLHDLRSRISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENL
SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVL
DKGRVVEFDSP
>gnl|CDD|213212 cd03245, ABCC_bacteriocin_exporters, ATP-binding cassette domain of bacteriocin exporters, subfamily C. Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane
GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQ
LDPADLRRNIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRG
LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIV
MDSGRIVADG
>gnl|CDD|213213 cd03246, ABCC_Protease_Secretion, ATP-binding cassette domain of PrtD, subfamily C. This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA
LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD
PNELGDHVGYLPQDDELFSGSIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA
ALKAAGATRIVIAHRPETLASADRILVLEDGRV
>gnl|CDD|213214 cd03247, ABCC_cytochrome_bd, ATP-binding cassette domain of CydCD, subfamily C. The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism
LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE
KALSSLISVLNQRPYLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSL
IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG
>gnl|CDD|213215 cd03248, ABCC_TAP, ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C. TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes
GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQ
VLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGY
DTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLS
TVERADQILVLDGGRI
>gnl|CDD|213216 cd03249, ABC_MTABC3_MDL1_MDL2, ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins. MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another
IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL
NLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQL
SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVL
QNGQVVEQGTHDELMAQKGVYAKLVKAQ
>gnl|CDD|213217 cd03250, ABCC_MRP_domain1, ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C. This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate
ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAY
VSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLAR
AVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR
>gnl|CDD|213218 cd03251, ABCC_MsbA, ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C. MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT
LASLRRQIGLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLS
GGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLE
DGKIVERGTHEELLAQGGVYAKLH
>gnl|CDD|213219 cd03252, ABCC_Hemolysin, ATP-binding cassette domain of hemolysin B, subfamily C. The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy
ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD
PAWLRRQVGVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLS
GGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVME
KGRIVEQGSHDELLAENGLYAYLYQLQ
>gnl|CDD|213220 cd03253, ABCC_ATM1_transporter, ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C. ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTL
DSLRRAIGVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSG
GEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKD
GRIVERGTHEELLAKGGLYAEMWKAQ
>gnl|CDD|213221 cd03254, ABCC_Glucan_exporter_like, ATP-binding cassette domain of glucan transporter and related proteins, subfamily C. Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI
SRKSLRSMIGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNL
SQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVL
DDGKIIEEGTHDELLAKKG
>gnl|CDD|213222 cd03255, ABC_MJ0796_LolCDE_FtsE, ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein. This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane
IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISK
LSEKELAAFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSE
LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRI
IELRDGKI
>gnl|CDD|213223 cd03256, ABC_PhnC_transporter, ATP-binding cassette domain of the binding protein-dependent phosphonate transport system. Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKG
KALRQLRRQIGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQ
RADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLARE
YADRIVGLKDGRIVFDGPPAELTDEVLDEIY
>gnl|CDD|213224 cd03257, ABC_NikE_OppD_transporters, ATP-binding cassette domain of nickel/oligopeptides specific transporters. The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF
LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLL
KLSRRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLN
RYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVA
KIADRVAVMYAGKIVEEG
>gnl|CDD|213225 cd03258, ABC_MetN_methionine_transporter, ATP-binding cassette domain of methionine transporter. MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLT
LLSGKELRKARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQ
LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDR
VAVMEKGEVVEEGTVEEVFANPQ
>gnl|CDD|213226 cd03259, ABC_Carb_Solutes_like, ATP-binding cassette domain of the carbohydrate and solute transporters-like. This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE
RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVA
LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV
QVG
>gnl|CDD|213227 cd03260, ABC_PstB_phosphate_transporter, ATP-binding cassette domain of the phosphate transport system. Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD)
IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIY
DLDVDVLELRRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHAL
GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRT
AFLLNGRLVEFGPTEQI
>gnl|CDD|213228 cd03261, ABC_Org_Solvent_Resistant, ATP-binding cassette transport system involved in resistant to organic solvents. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEA
ELYRLRRRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGG
MKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVL
YDGKIVAEGTPEELRASDDPLVRQF
>gnl|CDD|213229 cd03262, ABC_HisP_GlnQ, ATP-binding cassette domain of the histidine and glutamine transporters. HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein
IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKN
INELRQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQ
QQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDD
GRI
>gnl|CDD|213230 cd03263, ABC_subfamily_A, ATP-binding cassette domain of the lipid transporters, subfamily A. The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages
LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR
KAARQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKR
KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKL
RCIGSPQELK
>gnl|CDD|213231 cd03264, ABC_drug_resistance_like, ABC-type multidrug transport system, ATPase component. The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
LQLENLTKRYGKKRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL
RRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVG
IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE
G
>gnl|CDD|213232 cd03265, ABC_DrrA, Daunorubicin/doxorubicin resistance ATP-binding protein. DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE
VRRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRL
EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI
IAEGTPEELK
>gnl|CDD|213233 cd03266, ABC_NatA_sodium_exporter, ATP-binding cassette domain of the Na+ transporter. NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein
MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV
KEPAEARRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTG
MRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLH
RGRVVYEG
>gnl|CDD|213234 cd03267, ABC_NatA_like, ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA. NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein
IEVSNLSKSYRVYSKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGL
LQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSEL
LDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLT
SHYMKDIEALARRVLVIDKGRLLYDG
>gnl|CDD|213235 cd03268, ABC_BcrA_bacitracin_resist, ATP-binding cassette domain of the bacitracin-resistance transporter. The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein
LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA
LRRIGALIEAPGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALA
LLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG
>gnl|CDD|213236 cd03269, ABC_putative_ATPase, ATP-binding cassette domain of an uncharacterized transporter. This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN
RIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFI
AAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG
>gnl|CDD|213237 cd03270, ABC_UvrA_I, ATP-binding cassette domain I of the excision repair protein UvrA. Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases
IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDV
DSIEGLSPAIAIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVGIRERLGFLVDVGLGYLTLSRSAPTLSG
GEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVID
IGPGAGVHGGEIVAQG
>gnl|CDD|213238 cd03271, ABC_UvrA_II, ATP-binding cassette domain II of the excision repair protein UvrA. Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases
LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQPGNHDRIEGLEHID
KVIVIDQSPIGRTPRSNPATYTGVFDEIRELFCEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALEFF
ENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTLYILDEPTTGLHFHDVKK
LLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP
>gnl|CDD|213239 cd03272, ABC_SMC3_euk, ATP-binding cassette domain of eukaryotic SMC3 proteins. The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18)
IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPS
VMSAYVEIIFDNSDNRFPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQG
KINSLTNMKQDEQQEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSD
GAQFITTTFRPELLEVADKFYGVKFRNKVSTID
>gnl|CDD|213240 cd03273, ABC_SMC2_euk, ATP-binding cassette domain of eukaryotic SMC2 proteins. The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18)
MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKRG
QAGITKASVTIVFDNSDKSQSPIGFENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNN
PHFLIMQGRITKVLNMGGVWKESLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIG
RMIKTHFKGSQFIVVSLKEGMFNNANVLFRTRFVDGTSTVT
>gnl|CDD|213241 cd03274, ABC_SMC4_euk, ATP-binding cassette domain of eukaryotic SMC4 proteins. The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18)
LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAG
HPNLDSCSVEVHFQEIIDKPLLKSKGIDLDHNRFLILQGEVEQIAQMPKKSWKNISNLSGGEKTLSSLAL
VFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRLVGIYKTNNCTK
SV
>gnl|CDD|213242 cd03275, ABC_SMC1_euk, ATP-binding cassette domain of eukaryotic SMC1 proteins. The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18)
LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARVGKP
DSNSAYVTAVYEDDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESI
ASKNPPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPNF
QFIVISLKEEFFSKADALVGVYRDQECNSSKVLTLDL
>gnl|CDD|213243 cd03276, ABC_SMC6_euk, ATP-binding cassette domain of eukaryotic SM6 proteins. The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18)
IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESSAK
ITVTLKNQGLDANPLCVLSQDMARSFLTSNKAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEF
DVFMDMVNRKISTDLLVKEAKKQPGRQFIFITPQDISGLASSDDVKVFRMKDPRGPRR
>gnl|CDD|213244 cd03277, ABC_SMC5_euk, ATP-binding cassette domain of eukaryotic SMC5 proteins. The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18)
GSIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDE
GTIEIELYGNPGNIQVDNLCQFLPQDRVGEFAKLSPIELLVKFREGEQLQELDPHHQSGGERSVSTMLYL
LSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYFLITPKLLPGLNYHEKMTVLCVYNG
PHI
>gnl|CDD|213245 cd03278, ABC_SMC_barmotin, ATP-binding cassette domain of barmotin, a member of the SMC protein family. Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18)
LKKLELKGFKSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETR
KPANFAEVTLTFDNSDGRYSIISQGDVSEIIEAPGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCV
LDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLYGVTMQESGVSK
>gnl|CDD|213246 cd03279, ABC_sbcCD, ATP-binding cassette domain of sbcCD. SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini
MKPLKLELKNFGPFREEQVIDFTGLDNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFA
PGEDTAEVSFTFQLGGKKYRVERSRGLDYDQFTRIVLLPQGEFDRFLARPVSTLSGGETFLASLSLALAL
SEVLQNRGGARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLEVIKTPG
GSR
>gnl|CDD|213247 cd03280, ABC_MutS2, ATP-binding cassette domain of MutS2. MutS2 homologs in bacteria and eukaryotes. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange
RLREARHPLLPLQGEKVVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAAEGSSLP
VFENIFADIGDEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLER
GALVIATTHYGELKAYAYKREGVENASMEFDPETLKPTYRLLIGVPGRSNALEIARRLGL
>gnl|CDD|213248 cd03281, ABC_MSH5_euk, ATP-binding cassette domain of eukaryotic MutS5 homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange
EIQGGRHPLLELFVDSFVPNDTEIGGGGPSIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATIG
LVDKIFTRMSSRESVSSGQSAFMIDLYQVSKALRLATRRSLVLIDEFGKGTDTEDGAGLLIATIEHLLKR
GPECPRVIVSTHFHELFNRSLLPERLKIKFLTMEVLLNPTSTSPNEDITYLYRLVPGLADTSFAIHCAKL
AGI
>gnl|CDD|213249 cd03282, ABC_MSH4_euk, ATP-binding cassette domain of eukaryotic MutS4 homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange
IIRDSRHPILDRDKKNFIPNDIYLTRGSSRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYATLP
IFNRLLSRLSNDDSMERNLSTFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLAILECLIKK
ESTVFFATHFRDIAAILGNKSCVVHLHMKAQSINSNGIEMAYKLVLGLYRIVDDGIRFVRVLAL
>gnl|CDD|213250 cd03283, ABC_MutS-like, ATP-binding cassette domain of MutS-like homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange
EAKNLGHPLIGREKRVANDIDMEKKNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFELPPVKI
FTSIRVSDDLRDGISYFYAELRRLKEIVEKAKKGEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTI
GIISTHDLELADLLDLDSAVRNYHFREDIDDNKLIFDYKLKPGVSPTRNALRLMKKIGI
>gnl|CDD|213251 cd03284, ABC_MutS1, ATP-binding cassette domain of MutS1 homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange
EIEGGRHPVVEQVLDNEPFVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEI
GVVDRIFTRIGASDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHE
KIGAKTLFATHYHELTELEGKLPRVKNFHVAVKEKGGGVVFLHKIVEGAADKSYGIEVARLAGLPEEVIE
RAREIL
>gnl|CDD|213252 cd03285, ABC_MSH2_euk, ATP-binding cassette domain of eukaryotic MutS2 homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange
VLKEARHPCVEAQDDVAFIPNDVTLTRGKSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADI
PIVDCILARVGASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDGFGLAWAIAEYIAT
QIKCFCLFATHFHELTALADEVPNVKNLHVTALTDDASRTLTMLYKVEKGACDQSFGIHVAELANFPKEV
IEMAKQKALELE
>gnl|CDD|213253 cd03286, ABC_MSH6_euk, ATP-binding cassette domain of eukaryotic MutS6 homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange
CFEELRHPCLNASTASSFVPNDVDLGATSPRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRL
SLVDRIFTRIGARDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLVK
KVKCLTLFSTHYHSLCDEFHEHGGVRLGHMACAVKNESDPTIRDITFLYKLVAGICPKSYGLYVALMAGI
PDGVVERA
>gnl|CDD|213254 cd03287, ABC_MSH3_euk, ATP-binding cassette domain of eukaryotic MutS3 homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange
ILIKEGRHPMIESLLDKSFVPNDIHLSAEGGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASSAT
LSIFDSVLTRMGASDSIQHGMSTFMVELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLL
EEKKCLVLFVTHYPSLGEILRRFEGSIRNYHMSYLESQKDFETSDSQSITFLYKLVRGLASRSFGLNVAR
LAGLPKSIISRA
>gnl|CDD|213255 cd03288, ABCC_SUR2, ATP-binding cassette domain 2 of the sulfonylurea receptor SUR. The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity
AIASISGSSNSGLVGLGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRM
VDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVK
SLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVT
IAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTDK
>gnl|CDD|213256 cd03289, ABCC_CFTR2, ATP-binding cassette domain 2 of CFTR,subfamily C. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2
GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSV
PLQKWRKAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLS
HGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIE
ENKVRQYDSIQKLLNEKSHFKQAISPSDRLKLFPRRNSSKSKRKPRPQIQALQEETEEEVQDTRL
>gnl|CDD|213257 cd03290, ABCC_SUR1_N, ATP-binding cassette domain of the sulfonylurea receptor, subfamily C. The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity
VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSF
EATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN
LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADW
IIAMKDGS
>gnl|CDD|213258 cd03291, ABCC_CFTR1, ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C. The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2
TTGVIMENVTAFWDEGFGELLEKAKQENNDRKHSSDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITG
STGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEE
DITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANK
TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFSAERRNSILTETLRR
FS
>gnl|CDD|213259 cd03292, ABC_FtsE, Cell division ATP-binding protein FtsE, The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRG
RAIPYLRRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGG
EQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALE
RGKL
>gnl|CDD|213260 cd03293, ABC_NrtD_SsuB_transporters, ATP-binding cassette domain of the nitrate and sulfonate transporters. NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG
PGPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRV
ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPG
RIVAEVEVDL
>gnl|CDD|213261 cd03294, ABC_Pro_Gly_Betaine, ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system. This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
IKIKGLYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCI
NRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREER
AAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAEL
QKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDRAKV
>gnl|CDD|213262 cd03295, ABC_OpuCA_Osmoprotection, ATP-binding cassette domain of the osmoprotectant transporter. OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP
VELRRKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQ
QQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMK
NGEIVQVGTPDEILRSPANDFVAEFVGADRLL
>gnl|CDD|213263 cd03296, ABC_CysA_sulfate_importer, ATP-binding cassette domain of the sulfate transporter. Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP
VQERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGG
QRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVM
NKGRIEQVGTPDEVYDHPASPFVYSFLGE
>gnl|CDD|213264 cd03297, ABC_ModC_molybdenum_transporter, ATP-binding cassette domain of the molybdenum transport system. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
MLCVDIEKRLPDFTLKIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINL
PPQQRKIGLVFQQYALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRV
ALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL
QYIG
>gnl|CDD|213265 cd03298, ABC_ThiQ_thiamine_transporter, ATP-binding cassette domain of the thiamine transport system. Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
VRLDKIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR
PVSMLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALA
RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ
G
>gnl|CDD|213266 cd03299, ABC_ModC_like, ATP-binding cassette domain similar to the molybdate transporter. Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
LKVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK
RDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAI
ARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ
VGKPEEVFKKPKNEFVAEFLGFNNI
>gnl|CDD|213267 cd03300, ABC_PotA_N, ATP-binding cassette domain of the polyamine transporter. PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins
IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH
KRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVA
IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ
QIGTPEEIYEEPANRFVADFIG
>gnl|CDD|213268 cd03301, ABC_MalK_N, The N-terminal ATPase domain of the maltose transporter, MalK. ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed
VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK
DRDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVA
LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ
QIG
>gnl|CDD|176471 cd03302, Adenylsuccinate_lyase_2, Adenylsuccinate lyase (ASL)_subgroup 2. This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting
LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRH
DVMAHVHAFGLLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLG
FTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELV
TKKAGFKKVYPVTGQTYSRKVDIDVLNALSSLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKR
NPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSANRRIAIPEAFLAADAILITLQNISEGLVVYP
KVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQEGGDNDLIERIKNDAYFKPI
WDELDALLDPKTFIGR
>gnl|CDD|239423 cd03307, Mta_CmuA_like, MtaA_CmuA_like family. MtaA/CmuA, also MtsA, or methyltransferase 2 (MT2) MT2-A and MT2-M isozymes, are methylcobamide:Coenzyme M methyltransferases, which play a role in metabolic pathways of methane formation from various substrates, such as methylated amines and methanol. Coenzyme M, 2-mercaptoethylsulfonate or CoM, is methylated during methanogenesis in a reaction catalyzed by three proteins. A methyltransferase methylates the corrinoid cofactor, which is bound to a second polypeptide, a corrinoid protein. The methylated corrinoid protein then serves as a substrate for MT2-A and related enzymes, which methylate CoM
LAALNGQPVDRVPVICPTQTGTVELMEATGAYWPEAHSDAEKMADLAAAGHEVAGFEAVRVPFCMTVEAE
ALGCEVDWGTKDIQPSVTSHPFKKLEDVEKLPDDFLERGRIPTVLEAIKILKEKYGEEVPVIGGMTGPAS
LASHLAGVENFLKWLIKKPEKVREFLEFLTEACIEYAKAQLEAGADIITIADPTASPELISPEFYEEFAL
PYHKKIVKELHGCPTILHICGNTTPILEYIAQCGFDGISVDEKVDVKTAKEIVGGRAALIGNVSPSQTLL
NGTPEDVKAEARKCLEDGVDILAPGCGIAPRTPLANLKAMVEARKE
>gnl|CDD|239424 cd03308, CmuA_CmuC_like, CmuA_CmuC_like: uncharacterized protein family similar to uroporphyrinogen decarboxylase (URO-D) and the methyltransferases CmuA and CmuC
LYQERVQRLKDAIEGKKPDRVPILSQFTEWFIQYAGMTLKEAQWDTDKLEEAYDKVLKDFDFDITPGSAS
LRPPSFYQALGSKNFKMSSGGFLQHPEVYEYMEADEYDEFIADPYDFIVEKILPRIYKELAEDPAEKSLA
LAKAAAAFVDYNNTNGPIGAKLAEKEYGTPLNAGGVSEAPFDIIGDYLRGFKGISIDLRRRPEKVAEACE
AVTPLMIKMGTATAPAPYPGPVFTPIPLHLPPFLRPKQFEKFYWPSFKKVVEGLAARGQRIFLFFEGDWE
RYLEYLQELPKGKTVGLFEYGDPKKVKEKLGDKKCIAGGFPTTLLKYGTPEECIDYVKELLDTLAPGGGF
IFGTDKPIISADDAKPENLIAVIEFVRE
>gnl|CDD|239425 cd03309, CmuC_like, CmuC_like. Proteins similar to the putative corrinoid methyltransferase CmuC. Its function has been inferred from sequence similarity to the methyltransferases CmuA and MtaA. Mutants of Methylobacterium sp. disrupted in cmuC and purU appear deficient in some step of chloromethane metabolism
LEAIKGGPDRLVIDIGTTNLTGVRPAAVAGAERGVASAAPYVTGLSGKKDWFGLGSWFEPGFGYFPVDDE
EDEVVDDITKWKDYVKPPDIQHPLDWQAPARADLQSLDRNDLVIDVPLPGGVFERFRLRMSMEDALMALY
EEPEAAHELFDYLTDAKLKLYERRIKHLEPDLLVYHDDLGSQKGSFISPATFREFILPRMQRIFDFLRSN
TSALIVHHSCGAAASLVPSMAEMGVDSWNVVMTANNTAELRRLLGDKVVLAGAIDDVALDTATWPEEDAR
GVAKAAAECAPIHPFISAPTAGLPFSIFPEVLRRVSAFLDV
>gnl|CDD|239426 cd03310, CIMS_like, CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers both the N-and C-terminal barrel, and some single-barrel sequences, mostly from Archaea. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate
LATGIGSYPLPDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQLGDDMIGRFLEV
LVDLETGTRFFDNNFFYRPPEAKIEAFLPLELDYLEEVAEAYKEALKVKVVVTGPLTLALLAFLPNGEPD
AYEDLAKSLAEFLREQVKELKNRGIVVVQIDEPSLGAVGAGAFEDLEIVDAALEEVSLKSGGDVEVHLCA
PLDYEALLELGVDVIGFDAAALPSKYLEDLKKLLRIGVRTLILGLVVTDNEAKGRNAWKEIERLEKLVRR
LEEPGEVLDEILYLTPDCGLAFLPPQEARRKLALLAEAARE
>gnl|CDD|239427 cd03311, CIMS_C_terminal_like, CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers the C-terminal barrel, and a few single-barrel sequences most similar to the C-terminal barrel. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Sidechains from both barrels contribute to the binding of the folate substrate
PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLE
RLDGFEFTGWVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLTHPKPLKGILTGPVTIPSPSFVRFR
GYYPSREELAMDLALALREEIRDLYDAGCRYIQIDEPALAEGLPLEPDDLAADYLKWANEALADRPDDTQ
IHTHICYGNFRSTWAAEGGYEPIAEYIFELDVDVFFLEYDNSRAGGLEPLKELPYDKKVGLGVVDVKSPE
VESPEEVKDRIEEAAKYVPLEQLWVSPDCGFATRERGNALTKLENMVKAALV
>gnl|CDD|239428 cd03312, CIMS_N_terminal_like, CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers the N-terminal barrel, and a few single-barrel sequences most similar to the N-terminal barrel. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate
KTHILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDT
SVLLGAIPERFGALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEY
LEAKALGINTKPVLLGPVTFLKLSKAKGGGFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDL
PEEWLAAFKRAYEELAKAAPGLKLLLATYFGSLGENLDLLASLPVDGLHLDLVRGPENLEAVLKAGFADK
VLSAGVVDGRNIWRADLAASLALLETLAAILGDRLVVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQK
LEELALLARA
>gnl|CDD|239429 cd03313, enolase, Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways. The reaction is facilitated by the presence of metal ions
KIKAREILDSRGNPTVEVEVTTEDGGVGRAAVPSGASTGEHEAVELRDGDKSRYLGKGVLKAVKNVNEII
APALIGMDVTDQRAIDKLLIELDGTPNKSKLGANAILGVSLAVAKAAAAALGLPLYRYLGGLAAYVLPVP
MFNVINGGAHAGNKLDFQEFMIVPVGAPSFSEALRMGAEVYHTLKKVLKKKGGLLATNVGDEGGFAPNLS
SNEEALDLLVEAIEKAGYEPGKKIAIALDVAASEFYDEGKYVYDSDEGKKLTSEELIDYYKELVKKYPIV
SIEDPFDEDDWEGWAKLTAKLGDKIQIVGDDLFVTNPERLKKGIEKKAANALLIKVNQIGTLTETIEAIK
LAKKNGYGVVVSHRSGETEDTFIADLAVALGAGQIKTGAPCRSERTAKYNQLLRIEEE
>gnl|CDD|239430 cd03314, MAL, Methylaspartate ammonia lyase (3-methylaspartase, MAL) is a homodimeric enzyme, catalyzing the magnesium-dependent reversible alpha,beta-elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to mesaconic acid. This reaction is part of the main catabolic pathway for glutamate. MAL belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion
KIVDVLATPGLGEAISVMLVLEDGQVAVGDCAAVQYSGAGGRDPLFLAADFIPVIEKVIAPALVGRDVAN
FRPAAAVLDKMRLDGNRLHTAIRYGVSQALLDAVALAQRRTMAEVLCDEYGLPLADEPVPIFAQSGDDRY
INVDKMILKGADVLPHALINNVEEKGPKGEKLLEYVKWLSDRIRKLGRPGYHPILHIDVYGTIGQAFDPD
PDRAADYLATLEEAAAPFPLRIEGPMDAGSREAQIERMAALRAELDRRGVGVRIVADEWCNTLEDIRDFA
DAGAAHMVQIKTPDLGGIDNTIDAVLYCKEHGVGAYLGGSCNETDISARVTVHVALATRADQMLAKPGMG
VDEGLMIVTNEMNRTLALL
>gnl|CDD|239431 cd03315, MLE_like, Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and residues that can function as general acid/base catalysts, a Lys-X-Lys motif and another conserved lysine. Despite these conserved residues, the members of the MLE subgroup, like muconate lactonizing enzyme, o-succinylbenzoate synthase (OSBS) and N-acylamino acid racemase (NAAAR), catalyze different reactions
VEAIPVRLPLKRPLKWASGTLTTADHVLLRLHTDDGLVGWAEATKAAVDMALWDLWGKRLGVPVYLLLGG
YRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVGRDPARDVAVVAALREAVGDDAELRVDANRGW
TPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAFTPHDAFRELALGAADAVNIK
TAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAVTLPGEL
>gnl|CDD|239432 cd03316, MR_like, Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. Members of the MR subgroup are mandelate racemase, D-glucarate/L-idarate dehydratase (GlucD), D-altronate/D-mannonate dehydratase, D-galactonate dehydratase (GalD), D-gluconate dehydratase (GlcD), and L-rhamnonate dehydratase (RhamD)
KITDVETFVLRVPLPEPGGAVTWRNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIEDLLAPLLIGRDPL
DIERLWEKLYRRLFWRGRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGGYDDSP
EELAEEAKRAVAEGFTAVKLKVGGPDSGGEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLAR
ALEEYDLFWFEEPVPPDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEA
KKIAALAEAHGVRVAPHGAGGPIGLAASLHLAAALPNFGILEYHLDDLPLREDLFKNPPEIEDGYVTVPD
RPGLGVE
>gnl|CDD|239433 cd03317, NAAAR, N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of N-acylamino acids. NAAARs act on a broad range of N-acylamino acids rather than amino acids. Enantiopure amino acids are of industrial interest as chiral building blocks for antibiotics, herbicides, and drugs. NAAAR is a member of the enolase superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion
IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVAFEGPFYTEETNATAWHILKDYLLPL
LLGREFSHPEEVSERLAPIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGTRDSIPVGVSIGIQDDVEQ
LLKQIERYLEEGYKRIKLKIKPGWDVEPLKAVRERFPDIPLMADANSAYTLADIPLLKRLDEYGLLMIEQ
PLAADDLIDHAELQKLLKTPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGI
PVWCGGMLESGIGRAHNVALASLPNFTYPGDISASSRYFEEDIITPPFELENGIISVPTGPGIGVTVDRE
ALKK
>gnl|CDD|239434 cd03318, MLE, Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis,cis-muconate (CCM) to muconolactone (ML) in the catechol branch of the beta-ketoadipate pathway. This pathway is used in soil microbes to breakdown lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes (Cl-MLEs). MLEs are members of the enolase superfamily characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion
KIEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTPGGPAWGGESPETIKAIIDRY
LAPLLIGRDATNIGAAMALLDRAVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLAS
GDTERDIAEAEEMLEAGRHRRFKLKMGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPR
LEAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQ
KVAAIAEAAGIALYGGTMLESSIGTAASAHLFATLPSLPFGCELFGPLLLAEDLLEEPLAYRDGELHVPT
GPGLGVRLDEDKVRR
>gnl|CDD|239435 cd03319, L-Ala-DL-Glu_epimerase, L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion
KISLRPERLPLKRPFTIARGSRTEAENVIVEIELDGITGYGEAAPTPRVTGETVESVLAALKSVRPALIG
GDPRLEKLLEALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAA
AAKKAAKRGFPLLKIKLGGDLEDDIERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELGVELIEQ
PVPAGDDDGLAYLRDKSPLPIMADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGL
KVMVGCMVESSLSIAAAAHLAAAKADFVDLDGPLLL
>gnl|CDD|239436 cd03320, OSBS, o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 4-(2'-carboxyphenyl)-4-oxobutyrate (o-succinylbenzoate or OSB), a reaction in the menaquinone biosynthetic pathway. Menaquinone is an essential cofactor for anaerobic growth in eubacteria and some archaea. OSBS belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion
ARLYPYSLPLSRPLGTSRGRLTRRRGLLLRLEDLTGPVGWGEIAPLPLAFGIESALANLEALLVGFTRPR
NRIPVNALLPAGDAAALGEAKAAYGGGYRTVKLKVGATSFEEDLARLRALREALPADAKLRLDANGGWSL
EEALAFLEALAAGRIEYIEQPLPPDDLAELRRLAAGVPIALDESLRRLDDPLALAAAGALGALVLKPALL
GGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALPPLPAACGLGT
>gnl|CDD|239437 cd03321, mandelate_racemase, Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that interconverts the enantiomers of mandelic acid. MR is the first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid and allows this pathway to utilize either enantiomer of mandelate. MR belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion
VLITGLRARAVNVPMQYPVHTSVGTVATAPLVLIDLATDEGVTGHSYLFTYTPAALKSLKQLLDDMAALL
VGEPLAPAELERALAKRFRLLGYTGLVRMAAAGIDMAAWDALAKVHGLPLAKLLGGNPRPVQAYDSHGLD
GAKLATERAVTAAEEGFHAVKTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALD
QEGLTWIEEPTLQHDYEGHARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRA
SALAEQAGIPMSSHLFQEISAHLLAVTPTAHWLEYVDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREKA
VRKYL
>gnl|CDD|239438 cd03322, RspA, The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose putative targets are homoserine lactone (HSL)-derivative. They are part of the mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subfamily share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and catalytic residues, a partially conserved Lys-X-Lys motif and a conserved histidine-aspartate dyad
KITAIEVIVTCPGRNFVTLKITTDQGVTGLGDATLNGRELAVKAYLREHLKPLLIGRDANRIEDIWQYLY
RGAYWRRGPVTMNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQ
GYRAIRVQLPKLFEAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIR
QHTATPLAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPTDLSPVG
MAAALHLDLWVPNFGIQEYMRHAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKFPYVPRYLPV
ARLEDGTVHNW
>gnl|CDD|239439 cd03323, D-glucarate_dehydratase, D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to form 5-keto-4-deoxy-D-glucarate (5-KDG), the initial reaction of the catabolic pathway for (D)-glucarate. GlucD belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion
KITEMRVTPVAGHDSPLLNLSGAHEPFFTRNIVELTDDNGNTGVGESPGGAEALEALLEAARSLVGGDVF
GAYLAVLESVRVAFADRDAGGRGLQTFDLRTTVHVVTAFEVALLDLLGQALGVPVADLLGGGQRDSVPFL
AYLFYKGDRHKTDLPYPWFRDRWGEALTPEGVVRLARAAIDRYGFKSFKLKGGVLPGEEEIEAVKALAEA
FPGARLRLDPNGAWSLETAIRLAKELEGVLAYLEDPCGGREGMAEFRRATGLPLATNMIVTDFRQLGHAI
QLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNNHLGISLAMMTHVAAAAPGLITACDTHWIW
QDGQVITGEPLRIKDGKVAVPDKPGLGVELDRDKLAKAHELYQRL
>gnl|CDD|239440 cd03324, rTSbeta_L-fuconate_dehydratase, Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also encodes rTS alpha whose mRNA is complementary to thymidylate synthase mRNA. rTS beta expression is associated with the production of small molecules that appear to mediate the down-regulation of thymidylate synthase protein by a novel intercellular signaling mechanism. A member of this family, from Xanthomonas, has been characterized to be a L-fuconate dehydratase. rTS beta belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion
IKITALEVRDVRFPTSLELDGSDAMNPDPDYSAAYVVLRTDAAGLKGHGLTFTIGRGNEIVCAAIEALAH
LVVGRDLESIVADMGKFWRRLTSDSQLRWIGPEKGVIHLATAAVVNAVWDLWAKAEGKPLWKLLVDMTPE
ELVSCIDFRYITDALTPEEALEILRRGQPGKAAREADLLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQ
GFTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSPDDI
LGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVCP
HAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYSIEMK
>gnl|CDD|239441 cd03325, D-galactonate_dehydratase, D-galactonate dehydratase catalyses the dehydration of galactonate to 2-keto-3-deoxygalactonate (KDGal), as part of the D-galactonate nonphosphorolytic catabolic Entner-Doudoroff pathway. D-galactonate dehydratase belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion
KITKIETFVVPPRWLFVKIETDEGVVGWGEPTVEGKARTVEAAVQELEDYLIGKDPMNIEHHWQVMYRGG
FYRGGPVLMSAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFT
AVKMNATEELQWIDTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEP
VLPENVEALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVA
LAPHCPLGPIALAASLHVDASTPNFLIQEQSLGIHYNEGDDLLDYLVDPEVFDMENGYVKLPTGPGLGIE
ID
>gnl|CDD|239442 cd03326, MR_like_1, Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown
RIVAIREKAIPLSSPIANAYVDFSGLTTSLVAVVTDVVRDGRPVVGYGFDSIGRYAQGGLLRERFIPRLL
AAAPDSLLDDAGGNLDPARAWAAMMRNEKPGGHGERAVAVGALDMAVWDAVAKIAGLPLYRLLARRYGRG
QADPRVPVYAAGGYYYPGDDLGRLRDEMRRYLDRGYTVVKIKIGGAPLDEDLRRIEAALDVLGDGARLAV
DANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADHYDGPIATGENLFSLQDARNLLRYGGM
RPDRDVLQFDPGLSYGLPEYLRMLDVLEAHGWSRRRFFPHGGHLMSLHIAAGLGLGGNESYPDVFQPFGG
FADGCKVENGYVRLPDAPGIGFEGKAELAAEMREL
>gnl|CDD|239443 cd03327, MR_like_2, Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown
KIKSVRTRVGWLFVEIETDDGTVGYANTTGGPVACWIVDQHLARFLIGKDPSDIEKLWDQMYRATLAYGR
KGIAMAAISAVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAYASGLYPTDLDELPDEAKEYLKEGYRGMK
MRFGYGPSDGHAGLRKNVELVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDD
IEGYAELKKATGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHA
SQIYNYHFIMSEPNSPFAEYLPNSPDEVGNPLFYYIFLNEPVPVNGYFDLSDKPGFGLELN
>gnl|CDD|239444 cd03328, MR_like_3, Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown
AVERVEARAYTVPTDAPEADGTLAWDATTLVLVEVRAGGRTGLGYTYADAAAAALVDGLLAPVVEGRDAL
DPPAAWEAMQRAVRNAGRPGVAAMAISAVDIALWDLKARLLGLPLARLLGRAHDSVPVYGSGGFTSYDDD
RLREQLSGWVAQGIPRVKMKIGRDPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGV
TWFEEPVSSDDLAGLRLVRERGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAA
LAAAHHVDLSAHCAPALHAHVACAVPRLRHLEWFHDHVRIERMLFDGAPDPSGGALRPDLSRPGLGLELR
AR
>gnl|CDD|239445 cd03329, MR_like_4, Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown
KITDVEVTVFEYPTQPVSFDGGHHHPGPAGTRKLALLTIETDEGAKGHAFGGRPVTDPALVDRFLKKVLI
GQDPLDRERLWQDLWRLQRGLTDRGLGLVDIALWDLAGKYLGLPVHRLLGGYREKIPAYASTMVGDDLEG
LESPEAYADFAEECKALGYRAIKLHPWGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGR
ALEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEHSRGALESRADWVLAGATDFLRADVNLVGGITG
AMKTAHLAEAFGLDVELHGNGAANLHVIAAIRNTRYYERGLLHPSQKYDVYAGYLSVLDDPVDSDGFVHV
PKGPGLGVEIDFDYIERN
>gnl|CDD|394879 cd03330, Macro_Ttha0132-like, Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein Ttha0132. Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response. This family is composed of uncharacterized proteins containing a stand-alone macrodomain, similar to Thermus thermophilus hypothetical protein Ttha0132
RLIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMRKGPIRVGEAVETGAGKLPAKY
VIHAAVMGMPGRSSEESIRDATRNALAKAEELGLESVAFPAIGTGVGGFPVEEVARIMLEEIKKCDPPLL
EEVRLYR
>gnl|CDD|394880 cd03331, Macro_Poa1p-like_SNF2, macrodomain, Poa1p-like family, SNF2 subfamily. Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this subfamily contain a C-terminal macrodomain that show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. In addition, they also contain an SNF2 domain, defined by the presence of seven motifs with sequence similarity to DNA helicases. SNF2 proteins have the capacity to use the energy released by their DNA-dependent ATPase activity to stabilize or perturb protein-DNA interactions and play important roles in transcriptional regulation, maintenance of chromosome integrity and DNA repair
DINYVSGDVTHPQTTSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIP
VDDKESRSGGRDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYG
TERLIRKHLASR
>gnl|CDD|239448 cd03332, LMO_FMN, L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer
YQREIYLAGLLGRRPDLPVDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGV
TERDLSVELFGRTLAAPLLLAPIGVQELFHPDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPR
WFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLGWRPRDLDLGYLPFLRGIGIANYFSDPVFRKKL
AEPVGEDPEAPPPMEAAVARFVSVFSGPSLTWEDLAFLREWTDLPIVLKGILHPDDARRAVEAGVDGVVV
SNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGRPYAYGLALGGED
GVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL
>gnl|CDD|239449 cd03333, chaperonin_like, chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains
RELLLQVATTSLNSKLSSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKG
YASPYMPKRLENAKILLLDCPLEYVVIAEKGIDDLALHYLAKAGIMAVRRVKKEDLERIARATGATIVSS
LEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE
>gnl|CDD|239450 cd03334, Fab1_TCP, TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins
RALLAQLLKDEGISNDESWLDILLPLVWKAASNVKPDVRAGDDMDIRQYVKIKKIPGGSPSDSEVVDGVV
FTKNVAHKRMPSKIKNPRILLLQGPLEYQRVENKLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSV
SRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLTSPKLGTCESFRVRTYVEEHGRSKTLM
FFEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAAYHLKLETSFLADEF
>gnl|CDD|239451 cd03335, TCP1_alpha, TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin
GERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVEL
AQLQDKEVGDGTTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHLSISVDNLGKESL
INVAKTSMSSKIIGADSDFFANMVVDAILAVKTTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNC
TRASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLT
TGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLANLEGEETFDPSYLGEAEEVVQERIGD
DELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVETALSIYLENFAT
TLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPDKKHLKWYGLDLINGKVRDN
LEAGVLEPTVSKIKSLKFATEAAITILRIDDLIKLNP
>gnl|CDD|239452 cd03336, TCP1_beta, TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin
ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGRSGGVTVTNDGATILKSIGVDNPA
AKVLVDISKVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSS
DEEAFREDLLNIARTTLSSKILTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLL
DKKIGVNQPKRIENAKILIANTPMDTDKIKIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCF
INRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLI
RFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPG
KKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVGDMKELGITESFKVK
RQVLLSASEAAEMILRVDDIIKCAPRK
>gnl|CDD|239453 cd03337, TCP1_gamma, TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin
PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHP
AAKSMIELSRTQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVD
VNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDAVKTVAVEENGRKKEIDIKRYAKVEKIPGGEIEDSRV
LDGVMLNKDVTHPKMRRRIENPRIVLLDCPLEYLVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIAR
ACGATIVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAM
AVARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTE
LRAKHAQGENSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIVSG
>gnl|CDD|239454 cd03338, TCP1_delta, TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin
TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVEL
SKAQDIEAGDGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLI
KSATTSLNSKVVSQYSSLLAPIAVDAVLKVIDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKAS
KKAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQK
SILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDHFTEDKLGSADLVEEVSLGDGKI
VKITGVKNPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEIEIALQLSEWARTL
TGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNILEENVVQPLL
VSTSAITLATETVRMILKIDDIVLA
>gnl|CDD|239455 cd03339, TCP1_epsilon, TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin
DEYGRPFIIVREQEKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILE
KMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLE
EIADKIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLSVADLERKDVNFELIKVEGKVGGRL
EDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMV
EQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLSPEKLGKAGLV
REISFGTTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEISC
SLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHLGIDCLGRGTN
DMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV
>gnl|CDD|239456 cd03340, TCP1_eta, TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin
PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHP
AAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNID
KEDKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGV
AFKKTFSYAGFEQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKS
GANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVG
GERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYS
RTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKWYGVDINNEGIADNFEAFVW
EPSLVKINALTAATEAACLILSVDETIKNPKS
>gnl|CDD|239457 cd03341, TCP1_theta, TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin
RHYSGLEEAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMA
SQMQEEEIGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEE
VSKALKTAIASKQYGNEDFLSPLVAEACISVLPENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREPE
GSVKRVKKAKVAVFSCPFDIGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRL
GAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDG
RFVPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNK
SAGVDIESGDEGTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMAK
>gnl|CDD|239458 cd03342, TCP1_zeta, TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin
LNPKAEVLRRGQALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASM
IARAATAQDDITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTD
RELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDH
GARHPDMPKRVENAYILTCNVSLEYEKTEVNSGFFYSVVINQKGIDPPSLDMLAKEGILALRRAKRRNME
RLTLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIR
DGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQET
LVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRAGR
>gnl|CDD|239459 cd03343, cpn60, cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. Archaeal cpn60 (thermosome), together with TF55 from thermophilic bacteria and the eukaryotic cytosol chaperonin (CTT), belong to the type II group of chaperonins. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis
VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPA
AKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDP
DDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVAEKRDGKYVVDLDNIKIEKKTGGSVDDTELIRG
IVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGA
NVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDD
KMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVEIELAKRLREYARS
VGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVIEPL
RVKKQAIKSATEAATMILRIDDVIAAK
>gnl|CDD|239460 cd03344, GroEL, GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis
KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQL
VKEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEE
IAQVATISANGDEEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEV
ELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGD
RRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIRKQI
EETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEEGIVPGGGVALLRAS
PALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATGEYVDMIEAGI
IDPTKVVRSALQNAASVASLLLTTEALVVD
>gnl|CDD|239461 cd03345, eu_TyrOH, Eukaryotic tyrosine hydroxylase (TyrOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH) and eukaryotic tryptophan hydroxylase (TrpOH). TyrOH catalyzes the conversion of tyrosine to L-dihydroxyphenylalanine (L-DOPA), the rate-limiting step in the biosynthesis of the catecholamines dopamine, noradrenaline, and adrenaline
WFPRHISELDKCHHLVTKYEPDLDLDHPGFSDKVYRERRKLIAEIAFQYKHGDPIPRVEYTAEEIATWKE
VYKTLKDLHATHACKEYLDAFQLLEKECGYSEDRIPQLEDVSEFLKERTGFQLRPVAGLLSARDFLASLA
FRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADPTFAQFSQDIGLASLGASDEEIEKLSTLYWFTV
EFGLCKENGELKAYGAGLLSSYGELLHALSDEPEHRPFDPAATAVQPYQDQTYQPIYFVSESFSDAKDKL
RNYASTMKRPFSVRYDPY
>gnl|CDD|239462 cd03346, eu_TrpOH, Eukaryotic tryptophan hydroxylase (TrpOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH) and eukaryotic tyrosine hydroxylase (TyrOH). TrpOH oxidizes L-tryptophan to 5-hydroxy-L-tryptophan, the rate-limiting step in the biosynthesis of serotonin (5-hydroxytryptamine), a widely distributed hormone and neurotransmitter
PWFPKKISDLDKCANRVLMYGSELDADHPGFKDNVYRKRRKYFADVAMNYKHGDPIPRVEYTEEEIKTWG
TVYRELNRLYPTHACREYLKNLPLLEKHCGYREDNIPQLEDVSRFLKERTGFTIRPVAGYLSPRDFLAGL
AFRVFHCTQYVRHSSDPFYTPEPDTCHELLGHVPLLADPSFAQFSQEIGLASLGASDEDIQKLATCYFFT
VEFGLCKQDGQLKVYGAGLLSSIGELKHALSGEAKVKPFDPKVTCKQECLITTFQEAYFVSESFEEAKEK
MREFAKT
>gnl|CDD|239463 cd03347, eu_PheOH, Eukaryotic phenylalanine-4-hydroxylase (eu_PheOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic phenylalanine-4-hydroxylase (pro_PheOH), eukaryotic tyrosine hydroxylase (TyrOH) and eukaryotic tryptophan hydroxylase (TrpOH). PheOH catalyzes the first and rate-limiting step in the metabolism of the amino acid L-phenylalanine (L-Phe), the hydroxylation of L-Phe to L-tyrosine (L-Tyr). It uses (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) as the physiological electron donor. The catalytic activity of the tetrameric enzyme is tightly regulated by the binding of L-Phe and BH4 as well as by phosphorylation. Mutations in the human enzyme are linked to a severe variant of phenylketonuria
PWFPRTIQDLDRFANQILSYGAELDADHPGFKDPVYRARRKEFADIAYNYKHGQPIPRVEYTEEEKKTWG
TVFRELKSLYPTHACYEYNHVFPLLEKNCGFSEDNIPQLEDVSNFLQTCTGFRLRPVAGLLSSRDFLAGL
AFRVFHSTQYIRHPSKPMYTPEPDICHELLGHVPLFADPSFAQFSQEIGLASLGAPDEYIEKLATVYWFT
VEFGLCKQGGSIKAYGAGLLSSFGELQYCLSDKPELLPFEPEKTAVTKYPITEFQPLYYVAESFEDAKEK
LRNFAATIPRPFSVRYNPYTQRIEVL
>gnl|CDD|239464 cd03348, pro_PheOH, Prokaryotic phenylalanine-4-hydroxylase (pro_PheOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes the eukaryotic proteins, phenylalanine-4-hydroxylase (eu_PheOH), tyrosine hydroxylase (TyrOH) and tryptophan hydroxylase (TrpOH). PheOH catalyzes the hydroxylation of L-Phe to L-tyrosine (L-Tyr). It uses (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) as the physiological electron donor
DVPDEQGQIDYTPEEHAVWRTLYERQAKLLPGRACDAFLEGLEKLGLPTDRIPDFADVSERLKAATGWTV
VAVPGLIPDDEFFEHLANRRFPVTNFIRRPEELDYLQEPDIFHDIFGHVPMLTNPVFADFMQAYGKGGLK
ATGLEDRALLARLYWYTVEFGLIQEPGGLRIYGAGILSSPGETLYALESPDPNRIPFDLERVMRTPYRID
SFQPTYFVIDSFEQLYDA
>gnl|CDD|100040 cd03349, LbH_XAT, Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients
NISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIGLGGNHPTDWVSTYPFYIFGGEWEDDAKFDDWPS
KGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERLLALK
WWDWP
>gnl|CDD|100041 cd03350, LbH_THP_succinylT, 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs
GRRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEP
LQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETGEIYYGRVPPGSVVVAGSLP
>gnl|CDD|100042 cd03351, LbH_UDP-GlcNAc_AT, UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region
MIHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLK
YKGEPTRLEIGDNNTIREFVTIHRGTAQGGGVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVE
IGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALK
RAYRILYRSGLTLEEALEELEEEAPDSPEVEELVDFIRSSKRGI
>gnl|CDD|100043 cd03352, LbH_LpxD, UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X)
SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI
GSDGFGFAPDGGGWVKIPQLGGVIIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGENCL
IAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHREWL
>gnl|CDD|100044 cd03353, LbH_GlmU_C, N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer
GVTLIDPETTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVI
GNGATVGPFAHLRPGTVLGEGVHIGNFVEIKKSTIGEGSKANHLSYLGDAEIGEGVNIGAGTITCNYDGV
NKHRTVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIARARQ
>gnl|CDD|100045 cd03354, LbH_SAT, Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain
TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKIL
GNITIGDNVKIGANAVVTKDVPANSTVVGVP
>gnl|CDD|100046 cd03356, LbH_G1P_AT_C_like, Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity
LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCI
IGDDVVVED
>gnl|CDD|100047 cd03357, LbH_MAT_GAT, Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X)
LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFY
ANFNCTILDVAPVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIG
DNSVIGAGSVVTKDIPANVVAAGNPARVI
>gnl|CDD|100048 cd03358, LbH_WxcM_N_like, WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity
IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTV
KRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG
>gnl|CDD|100049 cd03359, LbH_Dynactin_5, Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity
YIETASGNKVSRKSVICGSQNIVLNGKTIIQSDVIIRGDLATVSIGRYCILSEGCVIRPPFKKFSKGVAF
FPLHIGDYVFIGENCVVNAAQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSGRPAR
FIGELPECTQELMEEETKEYY
>gnl|CDD|100050 cd03360, LbH_AT_putative, Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation
IIGAGGHARVVADILEADSGYEVVGFLDDDPELKGTEGLGLPVGLDELLLLYPPPDDEFVVAIGDNKLRR
KLAEKLLAAGYRFATLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVH
IAPGVVLSGGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP
>gnl|CDD|173781 cd03361, TOPRIM_TopoIA_RevGyr, TopoIA_RevGyr : The topoisomerase-primase (TORPIM) domain found in members of the type IA family of DNA topoisomerases (Topo IA) similar to the ATP-dependent reverse gyrase found in archaea and thermophilic bacteria. Type IA DNA topoisomerases remove (relax) negative supercoils in the DNA by: cleaving one strand of the DNA duplex, covalently linking to the 5' phosphoryl end of the DNA break and, allowing the other strand of the duplex to pass through the gap. Reverse gyrase is also able to insert positive supercoils in the presence of ATP and negative supercoils in the presence of AMPPNP. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). For topoisomerases the conserved glutamate is believed to act as a general base in strand joining and, as a general acid in strand cleavage. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function
TALMIVESPNKARTIANFFGRPSVRRLGGLVVYEVSTGDGVLMITASGGHVYDLVTKEGGHGVVEDDGRY
VPVYDSIKRCRDCGYQFTEDSDKCPRCGSENIDDKLETLEALRELALEVDEVLIATDPDTEGEKIAWDVY
LALRPYNKNIKRAEFHEVTRRAILEALRNP
>gnl|CDD|173782 cd03362, TOPRIM_TopoIA_TopoIII, TOPRIM_TopoIA_TopoIII: The topoisomerase-primase (TORPIM) domain found in members of the type IA family of DNA topoisomerases (Topo IA) similar to topoisomerase III. Type IA DNA topoisomerases remove (relax) negative supercoils in the DNA by: cleaving one strand of the DNA duplex, covalently linking to the 5' phosphoryl end of the DNA break and, allowing the other strand of the duplex to pass through the gap. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). For topoisomerases the conserved glutamate is believed to act as a general base in strand joining and, as a general acid in strand cleavage. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function
MVLIIAEKPSVAKAIAKILGGGSKKKGKGRYYEFYGEGGGYVVTWASGHLLELDFPEEYDPWDKVWPLED
PLFPAPFKLKVDKGKKKQFKVLKKLAKRADEIVIATDADREGELIGREILEYAKCVKRKPVKRAWFSSLT
PKAIRRAFKNL
>gnl|CDD|173783 cd03363, TOPRIM_TopoIA_TopoI, TOPRIM_TopoIA_TopoI: The topoisomerase-primase (TOPRIM) domain found in members of the type IA family of DNA topoisomerases (Topo IA) similar to Escherichia coli DNA topoisomerase I. Type IA DNA topoisomerases remove (relax) negative supercoils in the DNA by: cleaving one strand of the DNA duplex, covalently linking to the 5' phosphoryl end of the DNA break and, allowing the other strand of the duplex to pass through the gap. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). For topoisomerases the conserved glutamate is believed to act as a general base in strand joining and, as a general acid in strand cleavage. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function
KKLVIVESPAKAKTIKKYLGKEYEVLASVGHIRDLPKKGLGVDGEDDGFEPKYVVIPGKKKVVKELKKLA
KKADEIYLATDPDREGEAIAWHLAEVLKLKKNVKRVVFNEITKEAIKEALKNP
>gnl|CDD|173784 cd03364, TOPRIM_DnaG_primases, TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase domain found in the active site regions of proteins similar to Escherichia coli DnaG. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. E. coli DnaG is a single subunit enzyme
KKVILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKL
GLNVRVLTL
>gnl|CDD|173785 cd03365, TOPRIM_TopoIIA, TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in proteins of the type IIA family of DNA topoisomerases similar to Saccharomyces cerevisiae Topoisomerase II. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. These proteins also catenate/ decatenate duplex rings. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in strand joining and as a general acid in strand cleavage by topisomerases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function
CTLILTEGDSAKALAVAGLSVVGRDYYGVFPLRGKLLNVREASHKQIMENAEIQNIKKILGLQHGKSDYE
STKSLRYGRLMIMTDQDHDGSHIKGLLINFIHSFWPSLLKIPGFLVEFIT
>gnl|CDD|173786 cd03366, TOPRIM_TopoIIA_GyrB, TOPRIM_TopoIIA_GyrB: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in proteins of the type IIA family of DNA topoisomerases similar to the Escherichia coli GyrB subunit. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. These proteins also catenate/ decatenate duplex rings. DNA gyrase is more effective at relaxing supercoils than decatentating DNA. DNA gyrase in addition inserts negative supercoils in the presence of ATP. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general base in strand joining and as a general acid in strand cleavage by topisomerases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function
SELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIGEDFDLEKL
RYHKIIIMTDADVDGAHIRTLLLTFFFRYMRPLIENGHVYIAQP
>gnl|CDD|239465 cd03367, Ribosomal_S23, S12-like family, 40S ribosomal protein S23 subfamily; S23 is located at the interface of the large and small ribosomal subunits of eukaryotes, adjacent to the decoding center. It interacts with domain III of the eukaryotic elongation factor 2 (eEF2), which catalyzes the translocation of the growing peptidyl-tRNA to the P site to make room for the next aminoacyl-tRNA at the A (acceptor) site. Through its interaction with eEF2, S23 may play an important role in translocation. Also members of this subfamily are the archaeal 30S ribosomal S12 proteins. Prokaryotic S12 is essential for maintenance of a pretranslocation state and, together with S13, functions as control element for the rRNA- and tRNA-driven movements of translocation. S12 and S23 are also implicated in translation accuracy. Antibiotics such as streptomycin bind S12/S23 and cause the ribosome to misread the genetic code
RYKKRHLGTKYKADPLGGAPHAKGIVLEKVGVEAKQPNSAIRKCVRVQLIKNGKKITAFVPGDGCLNFID
ENDEVLVAGFGRKGRAVGDIPGVRFKVVKVNGVSLLALFKGKKEK
>gnl|CDD|239466 cd03368, Ribosomal_S12, S12-like family, 30S ribosomal protein S12 subfamily; S12 is located at the interface of the large and small ribosomal subunits of prokaryotes, chloroplasts and mitochondria, where it plays an important role in both tRNA and ribosomal subunit interactions. S12 is essential for maintenance of a pretranslocation state and, together with S13, functions as a control element for the rRNA- and tRNA-driven movements of translocation. Antibiotics such as streptomycin bind S12 and cause the ribosome to misread the genetic code
TINQLIRKGRKKKKKKSKSPALEGCPQKKGVCLKVYTTTPKKPNSALRKVARVRLSNGKEVTAYIPGEGH
NLQEHSVVLVRGGRVKDLPGVRYHIVRGVLDLAGVKNR
>gnl|CDD|213269 cd03369, ABCC_NFT1, ATP-binding cassette domain 2 of NFT1, subfamily C. Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate
WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI
DISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRVSEGGLNLSQGQRQLLCLARAL
LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP
>gnl|CDD|380327 cd03370, nitroreductase, uncharacterized nitroreductase family proteins. Nitroreductase family containing Thermus thermophilus NADH oxidase and other, uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer
VKEAIESRRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQAAAYGQAQVTSA
PAVIVIYSDMEDALANLEETIHPGLSEERRQREAAGLRGAFGKMSVEQRGQWGLAQANIALGFLLLAAQS
LGYDTSPMLGFDPEKVKALLGLPEHVTIAALVALGKPAEEGYPHHRHSLER
>gnl|CDD|239468 cd03371, TPP_PpyrDC, Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors
REDAIEIVLSRAPATAAVVSTTGMTSRELFELRDRPGGGHAQDFLTVGSMGHASQIALGIALARPDRKVV
CIDGDGAALMHMGGLATIGGLAPANLIHIVLNNGAHDSVGGQPTVSFDVSLPAIAKACGYRAVYEVPSLE
ELVAALAKALAADGPAFIEVKVRPGSRSDLGRPTTSPIENKERFMAFL
>gnl|CDD|239469 cd03372, TPP_ComE, Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors
RRDAIKTLIADLKDELVVSNIGFPSKELYAAGDRPLNFYMLGSMGLASSIGLGLALAQPRKVIVIDGDGS
LLMNLGALATIAAEKPKNLIIVVLDNGAYGSTGNQPTHAGKKTDLEAVAKACGLDNVATVASEEAFEKAV
EQALDGPSFIHVKIKPGNTDVPNIPRDPVEIKNRFMEAL
>gnl|CDD|239470 cd03375, TPP_OGFOR, Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity
WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDL
TVIVVSGDGDLAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNP
LALALAAGATFVARGFSGDIKQLKEIIKKAIQHKGFSFVEVLSPCPTFPLGVF
>gnl|CDD|239471 cd03376, TPP_PFOR_porB_like, Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of proteins similar to the beta subunit (porB) of the Helicobacter pylori four-subunit pyruvate ferredoxin oxidoreductase (PFOR), which are also found in archaea and some hyperthermophilic bacteria. PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The 36-kDa porB subunit contains the binding sites for the cofactors, TPP and a divalent metal cation, which are required for activity
FAPGHRACAGCGAALALRHVLKALGPDTVVVNPTGCLEVITTPYPYTAWRVPWIHVAFENAAAVASGIEA
ALKALGRGKDITVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTT
PVGKVSFGKKQPKKDLPLIMAAHNIPYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPCPTGWRFDPS
KTIEIARLAVETGFWPLYEYENGKF
>gnl|CDD|239472 cd03377, TPP_PFOR_PNO, Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of proteins similar to the single subunit pyruvate ferredoxin oxidoreductase (PFOR) of Desulfovibrio Africanus, present in bacteria and amitochondriate eukaryotes. This subfamily also includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). These enzymes are dependent on TPP and a divalent metal cation as cofactors. PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The PFOR from cyanobacterium Anabaena (NifJ) is required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO
PLFEFSGACAGCGETPYVKLLTQLFGDRMVIANATGCSSIYGGSAPTTPYTTNAKGRGPAWANSLFEDNA
EFGLGMRLAVDQRRERARELVQKLIEKIGDEELKTLLNAWLATEDDIEESRERVAKLKPLLAAEKDELAK
ELLSLADYLVKKSVWIIGGDGWAYDIGYGGLDHVLASGENVNILVLDTEVYSNTGGQASKATPLGAVAKF
AAAGKRTGKKDLGMIAMSYGNVYVAQIALGANDNQTLKAFREAEAYDGPSLIIAYSPCIAHGIKGGMTKS
QEQQKLAVESGYWPLYRYNPRLVEEGKNPLQLDSKEPDGPVEEFLNNENRFAALKKANPERAEQLFEQLQ
ADAKERYKRYKRLAA
>gnl|CDD|239473 cd03378, beta_CA_cladeC, Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes
PDEALERLKEGNKRFVSGKPLHPDQDLARRRELAKGQKPFAVILSCSDSRVPPEIIFDQGLGDLFVVRVA
GNIVDDDVLGSLEYAVEVLGVPLVVVLGHESCGAVAAAAVRANVKATVAKLRSRSPIIAELVAAGKLKIV
GAYYDLDTGKVEFL
>gnl|CDD|239474 cd03379, beta_CA_cladeD, Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes
PARKLAIVTCMDARLDPEKALGLKLGDAKVIRNAGGRVTDDAIRSLVVSVYLLGTREIIVIHHTDCGMLT
FTDEELKEKMKERGIAEAYGGIDKEFWFLGFDDLEESVREDVERIRNHPLIPDDVPVHGYVYDVKTGKLT
EV
>gnl|CDD|239475 cd03380, PAP2_like_1, PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium chloroperoxidases and vanadium bromoperoxidases
GAKAFSLPGPAAGYLPTSGTPDLPPPPPALSAAYAADLAEVKALGALQSTARTTAQTALAAFDADGGDPP
PHYANAFSIALGTPGLSEERTPRLYALLARALTDAGIATWDAKYHYNRPRPFVAIRLQWLPICTPEEGTP
KHPSYPSGHATFGGAAALVLAELFPERAAELLARAAEAGNSRVVAGVHWPSDVEAGRILGEAIAAALLA
>gnl|CDD|239476 cd03381, PAP2_glucose_6_phosphatase, PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts glucose-6-phosphate into free glucose and is active in the lumen of the endoplasmic reticulum, where it is bound to the membrane. The generation of free glucose is an important control point in metabolism, and stands at the end of gluconeogenesis and the release of glucose from glycogen. Deficiency of glucose-6-phosphatase leads to von Gierke's disease
LFLIVFPLCGHLSQSVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVHETDYYSNSSVPKIEQFPLTCET
GPGSPSGHAMGTTAVLLVMVTALLSHLAGRKRSRFLRVMLWLVFWGVQLAVCLSRIYLAAHFPHQVIAGV
ISGIAVAETFSHIRYIYSASLKRYVLITFFLFGFALGFYLLLKWLGVDLLWSLEKAFKWCERPEWVHIDT
TPFASLLRNLGTLLGLGLALNSSMY
>gnl|CDD|239477 cd03382, PAP2_dolichyldiphosphatase, PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a membrane-associated protein located in the endoplasmic reticulum and hydrolyzes dolichyl pyrophosphate, as well as dolichylmonophosphate at a low rate. The enzyme is necessary for maintaining proper levels of dolichol-linked oligosaccharides and protein N-glycosylation, and might play a role in re-utilization of the glycosyl carrier lipid for additional rounds of lipid intermediate biosynthesis after its release during protein N-glycosylation reactions
FSLTHVLYDPGDLLSFLLAYLSLLPVAILVGYATLILFRRELEAIYLFIGLLANEALNYVLKRIIKEPRP
CSGAYFVRSGYGMPSSHSQFMGFFAVYLLLFIYLRLGRLNSLVSRFLLSLGLLLLALLVSYSRVYLGYHT
VSQVVVGAIVGILLGILWF
>gnl|CDD|239478 cd03383, PAP2_diacylglycerolkinase, PAP2_like proteins, diacylglycerol_kinase like sub-family. In some prokaryotes, PAP2_like phosphatase domains appear fused to E. coli DAGK-like trans-membrane diacylglycerol kinase domains. The cellular function of these architectures remains to be determined
VLAMIGESPPHVTFVSLLIVIIVVVILKAYFGRGTPLEGGMPSGHAAIAFSIATAISLITNNPIISILSV
LLAVMVAHSRVEMKIHTMWEVVVGAILGALITLLIFKIF
>gnl|CDD|239479 cd03384, PAP2_wunen, PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid phosphatases. Wunen is a drosophila protein expressed in the central nervous system, which provides repellent activity towards primordial germ cells (PGCs), controls the survival of PGCs and is essential in the migration process of these cells towards the somatic gonadal precursors
RLYRFVGVFLFGLFATQLLTDLGKYVTGRLRPHFLDVCKPNYTDLTCSLDHQYIADCTCCTGDPDLIREA
RLSFPSGHASLSMYAAVFLALYLQARLKLRGSRLLRPLLQFLLLALALYVGLSRISDYKHHWSDVLAGAL
LGSVIALFLV
>gnl|CDD|239480 cd03385, PAP2_BcrC_like, PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as bacitracin transport permeases, as it was suspected that they form the permease component of an ABC transporter system. It was shown, however, that BcrC from Bacillus subtilis posesses undecaprenyl pyrophosphate (UPP) phospatase activity, and it is hypothesized that it competes with bacitracin for UPP, increasing the cell's resistance to bacitracin
LDALAIFIAEYLIYILPLLLVVLWLWGGEKQRKVVLFATIAVAVALLINYIIGLLYFHPRPFVVGLGHNL
LPHAADSSFPSDHTTLFFSIAFSLLLRRRKWAGWILLILALLVAWSRIYLGVHYPLDMLGAALVAVLSAL
LVFQ
>gnl|CDD|239481 cd03386, PAP2_Aur1_like, PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of inositol phosphate to ceramide, an essential step in yeast sphingolipid synthesis, and is the target of several antifungal compounds such as aureobasidin
PALEILLYEGFLSIYLESNLQRHIPLDPLAWFPYGSLHFLVPLALLAWLFLFRPPGTLRRFRRALGLANL
LGLLIYLLFPTAPPRYEPPYGLILLVLLMYGSAGYTSGFGGFDNPFNAFPSLHVAWAVLAALFLWRHRRR
LLRWLAVLWPLLIWLSTLYLGNHYFIDLVGGIALALLSFYLARRVR
>gnl|CDD|239482 cd03388, PAP2_SPPase1, PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an intracellular enzyme located in the endoplasmic reticulum, which regulates the level of sphingosine-1-phosphate (S1P), a bioactive lipid. S1P acts as a second messenger in the cell, and extracellularly by binding to G-protein coupled receptors of the endothelial differentiation gene family
PFLDYYFAFTALLGTHTFYILFLPFLFWNGDPYVGRDLVVVLALGMYIGQFIKDLFCLPRPSSPPVVRLT
MSSAALEYGFPSTHAMNATAISFYLLIYLYDRYQYPFVLGLILALFYSTLVCLSRIYMGMHSVLDVIAGS
LIGVLILLFRF
>gnl|CDD|239483 cd03389, PAP2_lipid_A_1_phosphatase, PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from Francisella novicida selectively dephosphorylates lipid A at the 1-position. Lipid A is the membrane-anchor component of lipopolysaccharides (LPS), the major constituents of the outer membrane in many gram-negative bacteria
SYFYLDRPLALYIKALDGRILAGFFRTITDFGKSGWYLIPSLLLFLLFRFGDLRGLSAPSRARFPKAAWA
GLFLFATVALSGILVNLLKFIIGRARPKLLFDDGLYGFDPFHADYAFTSFPSGHSATAGAAAAALALLFP
RYRWAFILLALLIAFSRVIVGAHYPSDVIAGSLLGAVTALALYQRF
>gnl|CDD|239484 cd03390, PAP2_containing_1_like, PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. Most likely membrane-associated phosphatidic acid phosphatases. Plant members of this group are constitutively expressed in many tissues and exhibit both diacylglycerol pyrophosphate phosphatase activity as well as phosphatidate (PA) phosphatase activity, they may have a more generic housekeeping role in lipid metabolism
PSISYPFAESETVPTWLLVIISVGIPLLVIILISLFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAG
RPRPDFLARCFPDGGTPSDTLVGIDICCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFDP
RGSSWRLLLALLPLLLAILVAVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY
>gnl|CDD|239485 cd03391, PAP2_containing_2_like, PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to eukaryota, lacks functional characterization and may act as a membrane-associated phosphatidic acid phosphatase
GVCARETSSWGPVRPLVKLLELSGHGIPWLAGTISCLWISSSPAGQEVLVNLLLGLLLDIITVAILKALV
RRRRPAYNSPDMLDYVAVDKYSFPSGHASRAAFVARFLLNHLVLAVPLRVLLVLWATVVGISRVLLGRHH
VLDVLAGAFLGYLEALLVE
>gnl|CDD|239486 cd03392, PAP2_like_2, PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase
AVVVQAGWLTAFDQSVLSLLRSLRTPLLTAFMTAITFLGSPAVLLIIVLLLALLLLLKRRRRAALFLLLA
LLGGGALNTLLKLLVQRPRPPLHLLVPEGGYSFPSGHAMGATVLYGFLAYLLARRLPRRRVRILLLILAA
ILILLVGLSRLYLGVHYPSDVLAGWLLGLAWLALLILLYRRL
>gnl|CDD|239487 cd03393, PAP2_like_3, PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria and archaea, lacks functional characterization and may act as a membrane-associated lipid phosphatase
IVLSLIYWLVDKRLGRYLGLALCASGYLNAALKEVFKIPRPFTYDGIQAIYEESAGGYGFPSGHAQTSAT
FWGSLMLHVRKKWFTLIGVVLVVLISFSRLYLGVHWPSDVIGGVLIGLLVLVLGE
>gnl|CDD|239488 cd03394, PAP2_like_5, PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase
DREGLLILAEAAALTAAVTEGLKFAVGRARPDGSNNGYRSFPSGHTASAFAAATFLQYRYGWRWYGIPAY
ALASLVGASRVVANRHWLSDVLAGAAIGILVGYLVT
>gnl|CDD|239489 cd03395, PAP2_like_4, PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase
LLEQIDVWLFLLLNGTLVHPLLDDLMPFLTGKKLSVPIFLLLALFILFRKGPIGLLILLLVLLAVGFADQ
LASGFLKPLVARLRPCNALDGVRLVVLGDQGGSYSFASSHAANSFALALFIWLFFRRGLFSPVLLLWALL
VGYSRVYVGVHYPGDVIAGALIGIISGLLFYLLFSWL
>gnl|CDD|239490 cd03396, PAP2_like_6, PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which mainly contains bacterial proteins, lacks functional characterization and may act as a membrane-associated lipid phosphatase
LPGLDLWVAGLFYDAGGGVFPFPLRHSWILETLLHLGGRLLSIALAVLLLALALLFFRRKRLRRRRRALL
LLILVIGLGLLVVAILKSHWGRPRPWDLTEFGGDAPYTPLFSGPSNGCGKGCSFPSGHASAGFALLALYF
LFRRRRPRLARLVLAAGLALGALMGLARMARGAHFLSDVLWSLLLVWLIALLLYRLI
>gnl|CDD|239491 cd03397, PAP2_acid_phosphatase, PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes catalyze phosphomonoester hydrolysis, with optimal activity in low pH conditions. They are secreted into the periplasmic space, and their physiological role remains to be determined
LLLLSAGAPASQQPAPSATIRALPASGYLPPVGATPDSLDLLPPPPAAGSAAFAADLAAYLAARALRGTP
RWALATTDADLSFPGAANAFSCALGEERTPELYRLLRRVLEDAGSATYPAKKYYNRPRPFVLNDEPICTP
PDESGLAKDGSYPSGHTAAGYAWALILAELVPERADEILARGSEYGQSRIVCGVHWPSDVMGGRIMAAAL
VAALLADPAFAADLAAARAELR
>gnl|CDD|239492 cd03398, PAP2_haloperoxidase, PAP2, haloperoxidase_like subfamily. Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles
GTVKPFSLPSGSQFRPPPPPALGSAEYAAQLAEVKTLGGARSTSRTARQTAIAAFWADGPTPPGHWNQIA
RILAARPGLSLFRTARLFAAVNAAMTDAGIAAWDAKYHYRRWRPVTAIRLADTDGNPATEADPYWLPLAG
TPPHPSYPSGHATFAGAAATVLKALFGSDKVPDTVSEPDEGGPSTGVTRVWAELNELADEVAISRVYAGV
HFRSDDAAGAALGEQIGAAALA
>gnl|CDD|259798 cd03399, SPFH_flotillin, Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. The flotillin (reggie) like proteins are lipid raft-associated. Individual proteins of this SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. In addition, microdomains formed from flotillin proteins may be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and interact with a variety of proteins. They may play a role in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and in cancer invasion, and metastasis
FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAERFLGKSTEEIRELV
KETLEGHLRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAA
EVKKD
>gnl|CDD|259799 cd03401, SPFH_prohibitin, Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology
FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLY
RPDPEKLPELYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVD
DVLITNIDFPDEYEKAIEAKQVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ
>gnl|CDD|259800 cd03402, SPFH_like_u2, Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome
VVGIILLGGFFVVQPNEAAVLTLFGRYRGTVRRPGLRWVNPFYRKKRVSLRVRNFESEPLKVNDANGNPI
EIAAVVVWRVVDTAKAVFDVDDYEEFVSIQSEAALRRVASRYPYDSFEDGEPSLRGNSDEVSEELRRELQ
ERLAVAGVEVIEARITHLAYAPEIAQAMLQRQQASAIIAARQTIVEGAVGMVEMALARLEERGVVELDEE
RKAALVSNLLVVLCSERGAQP
>gnl|CDD|259801 cd03403, SPFH_stomatin, Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. Stomatin (or band 7) is widely expressed and, highly expressed in red blood cells. It localizes predominantly to the plasma membrane and to intracellular vesicles of the endocytic pathway, where it is present in higher order homo-oligomeric complexes (of between 9 and 12 monomers). Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and, is implicated in trafficking of Glut1 glucose transporters. This subgroup found in animals, also contains proteins similar to Caenorhabditis elegans MEC-2. MEC-2 interacts with MEC-4, which is part of the degenerin channel complex required for response to gentle body touch
PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRS
TRLLAQTTLRNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAE
AAREARAKVIAAEGEQNASRALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID
>gnl|CDD|259802 cd03404, SPFH_HflK, High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection
LILLLLLLVWLLSGFYTVDPGERGVVLRFGKYVRTVGPGLHWKLPFPIEVVEKVNVTQVRSVEIGFRVPE
ESLMLTGDENIVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEGRAEIAAD
VRELLQEILDRYDLGIEIVQVQLQDADPPEEVQDAFDDVNAARQDKERLINEAQAYANEVIPRARGEAAR
IIQEAEAYKAEVVARAEGDAARFLALLAEYRKAPEVTRERLYLETMEEVLSNASKV
>gnl|CDD|259803 cd03405, SPFH_HflC, High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection
SVFIVDETEQAVVLQFGKPVRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYAR
WRITDPLRFYQSVGGEEGAESRLDDIVDSALRNEIGKRTLAEVVSGGRDELMEEILEQANEEAKEYGIEV
VDVRIKRIDLPEEVSESVYERMRAERERIAAEYRAEGEEEAEKIRAEADRERTVILAEAYREAEEIRGEG
DAEAARIYAEAYGKDPEFYSFYRSLEAYRASFKGKTTLL
>gnl|CDD|259804 cd03406, SPFH_like_u3, Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome
ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIY
FDRIEVVNRLDKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQAD
LNKMAPGLEIIAVRVTKPKIPEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVA
KIQMQQKIMEKEAEKKISEIEDEMHLAREKARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKI
YFGNDIPNMFLDN
>gnl|CDD|259805 cd03407, SPFH_like_u4, Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome
CVSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDVRVETKTKDNVFVTLVVSVQYRVV
PEKVYDAFYKLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVT
DIEPDASVKAAMNEINAAQRLREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVDGLRESIE
DFQEAVPGVSSKEVMDLLLITQYFDTLKEVGKSSKSSTVFLPHGPGGVSDISAQIRAGM
>gnl|CDD|259806 cd03408, SPFH_like_u1, Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome
VIRWKGPDNEIKNGSQLIVREGQAAIFVNEGKVADVFGPGGHTLTTNNIPFLTTLKGWKFGFESPFKAEV
YFVNTKEILDIKWGTPNPIPYRDPEYGIPVRLRAFGTYSFRVTDPALFLTEVVGTQGTFTTDEIEEQLRS
EIVQALKDAIAELSISGLDLALEANLDELSAALKEKLAPEFEKYGLELTSFGIESISLPEEVQKRIDKRA
SMAALGD
>gnl|CDD|239503 cd03409, Chelatase_Class_II, Class II Chelatase: a family of ATP-independent monomeric or homodimeric enzymes that catalyze the insertion of metal into protoporphyrin rings. This family includes protoporphyrin IX ferrochelatase (HemH), sirohydrochlorin ferrochelatase (SirB) and the cobaltochelatases, CbiK and CbiX. HemH and SirB are involved in heme and siroheme biosynthesis, respectively, while the cobaltochelatases are associated with cobalamin biosynthesis. Excluded from this family are the ATP-dependent heterotrimeric chelatases (class I) and the multifunctional homodimeric enzymes with dehydrogenase and chelatase activities (class III)
GLLVVGHGSPYKDPYKKDIEAQAHNLAESLPDFPYYVGFQSGLGPDTEEAIRELAEEGYQRVVIVPLAPV
SGDEVFYDIDSEIGLVRKQVGEPLGEKLTRG
>gnl|CDD|239504 cd03411, Ferrochelatase_N, Ferrochelatase, N-terminal domain: Ferrochelatase (protoheme ferrolyase or HemH) is the terminal enzyme of the heme biosynthetic pathway. It catalyzes the insertion of ferrous iron into the protoporphyrin IX ring yielding protoheme. This enzyme is ubiquitous in nature and widely distributed in bacteria and eukaryotes. Recently, some archaeal members have been identified. The oligomeric state of these enzymes varies depending on the presence of a dimerization motif at the C-terminus
TAVLLVNLGGPESLEDVRPFLKNFLSDRRVIELPRPLRPILAGIILPRRPPKVAKNYKKIGGGSPLNEIT
RAQAEALEKALDERGIDVKVYLAMRYGPPSIEEALEELKADGVDRIVVLPLYPQYSASTTGSYLDEVERA
LKKLRPAPELRVIRSFYDH
>gnl|CDD|239505 cd03412, CbiK_N, Anaerobic cobalamin biosynthetic cobalt chelatase (CbiK), N-terminal domain. CbiK is part of the cobalt-early path for cobalamin biosynthesis. It catalyzes the insertion of cobalt into the oxidized form of precorrin-2, factor II (sirohydrochlorin), the second step of the anaerobic branch of vitamin B12 biosynthesis. CbiK belongs to the class II family of chelatases and is a homomeric enzyme that does not require ATP for its enzymatic activity
KAILLVSFGTSYPTAEKTIDAIEDKVRAAFPDYEVRWAFTSRMIRKKLKKRGIEVDTPEEALAKLAADGY
TEVIVQSLHIIPGEEYEKLKREVDAFKKGFKKIKLGRPLLYSPEDYEEVAAALKDQI
>gnl|CDD|239506 cd03413, CbiK_C, Anaerobic cobalamin biosynthetic cobalt chelatase (CbiK), C-terminal domain. CbiK is part of the cobalt-early path for cobalamin biosynthesis. It catalyzes the insertion of cobalt into the oxidized form of precorrin-2, factor II (sirohydrochlorin), the second step of the anaerobic branch of vitamin B12 biosynthesis. CbiK belongs to the class II family of chelatases, and is a homomeric enzyme that does not require ATP for its enzymatic activity
EAVVFMGHGTDHPSNAVYAALEYVLREEDPANVFVGTVEGYPGLDDVLAKLKKAGIKKVTLMPLMLVAGD
HAHNDMAGDEPDSWKSILEAAGIKVETVLKGLG
>gnl|CDD|239507 cd03414, CbiX_SirB_C, Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), C-terminal domain. SirB catalyzes the ferro-chelation of sirohydrochlorin to siroheme, the prosthetic group of sulfite and nitrite reductases. CbiX is a cobaltochelatase, responsible for the chelation of Co2+ into sirohydrochlorin, an important step in the vitamin B12 biosynthetic pathway. CbiX often contains a C-terminal histidine-rich region that may be important for metal delivery and/or storage, and may also contain an iron-sulfur center. Both CbiX and SirB are found in a wide range of bacteria
TAVVLVGRGSSDPDANADVAKIARLLEEGTGFARVETAFAAATRPSLPEALERLRALGARRVVVLPYLLF
TGVLMDRIEEQVAELAAEPGIEFVLAPPLGPHPELAEALLERVREAL
>gnl|CDD|239508 cd03415, CbiX_CbiC, Archaeal sirohydrochlorin cobalt chelatase (CbiX) single domain. Proteins in this subgroup contain a single CbiX domain N-terminal to a precorrin-8X methylmutase (CbiC) domain. CbiX is a cobaltochelatase, responsible for the chelation of Co2+ into sirohydrochlorin, while CbiC catalyzes the conversion of cobalt-precorrin 8 to cobyrinic acid by methyl rearrangement. Both CbiX and CbiC are involved in vitamin B12 biosynthesis
TAIIIITHGSRRNTFNEDMEEWAAYLERKLGVPVYLTYNEYAEPNWRDLLNELLSEGYGHIIIALAFLGR
GNHVARDIMGELGVSRFYKWVMSKYGGKEILVYVTEPLADSPLVKLALFYRVKRA
>gnl|CDD|239509 cd03416, CbiX_SirB_N, Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), N-terminal domain. SirB catalyzes the ferro-chelation of sirohydrochlorin to siroheme, the prosthetic group of sulfite and nitrite reductases. CbiX is a cobaltochelatase, responsible for the chelation of Co2+ into sirohydrochlorin, an important step in the vitamin B12 biosynthetic pathway. CbiX often contains a C-terminal histidine-rich region that may be important for metal delivery and/or storage, and may also contain an iron-sulfur center. Both are found in a wide range of bacteria. This subgroup also contains single domain proteins from archaea and bacteria which may represent the ancestral form of class II chelatases before domain duplication occurred
ALLLVGHGSRDPRAAEALEALAERLRERLPGDEVELAFLELAEPSLAEALDELAAQGATRIVVVPLFLLA
GGHVKEDIPAALAAARARHPGVRIRYAPPLG
>gnl|CDD|239510 cd03418, GRX_GRXb_1_3_like, Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -_ GSH reductase -_ GSH -_ GRX -_ protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3, which are members of this subfamily
KVEIYTKPNCPYCVRAKALLDKKGVDYEEIDVDGDPALREEMINRSGGRRTVPQIFIGDVHIGGCDDLYA
LERKG
>gnl|CDD|239511 cd03419, GRX_GRXh_1_2_like, Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -_ GSH reductase -_ GSH -_ GRX -_ protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3
PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDL
MALHKSGKLVKL
>gnl|CDD|239512 cd03420, SirA_RHOD_Pry_redox, SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown function. Other domains include RHOD (rhodanese homology domain), and Pry_redox (pyridine nucleotide-disulphide oxidoreductase) as well as a C-terminal domain that corresponds to COG2210. This fold is referred to as a two-layered alpha/beta sandwich, structurally similar to that of translation initiation factor 3
EVDACGLQCPGPILKLKKEIDKLQDGEQLEVKASDPGFARDAQAWCKSTGNTLISLETEKGKVKAVIEK
>gnl|CDD|239513 cd03421, SirA_like_N, SirA_like_N, a protein of unknown function with an N-terminal SirA-like domain. The SirA, YedF, YeeD protein family is present in bacteria as well as archaea. SirA (also known as UvrY, and YhhP) belongs to a family of a two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding
TIDARGLACPQPVIKTKKALELEAGGEIEVLVDNEVAKENVSRFAESRGYEVSVEEKGGEFEITITK
>gnl|CDD|239514 cd03422, YedF, YedF is a bacterial SirA-like protein of unknown function. SirA (also known as UvrY, and YhhP) belongs to a family of a two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding
RLDLRGEPCPYPAIATLEALPSLKPGEILEVISDCPQSINNIPIDARNHGYKVLAIEQSGPTIRYLIQK
>gnl|CDD|239515 cd03423, SirA, SirA (also known as UvrY, and YhhP) belongs to a family of two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is thought to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding
ILDTRGLRCPEPVMMLHKKVRKMKPGDTLLVLATDPSTTRDIPKFCTFLGHELLAQETEDEPYRYLIRK
>gnl|CDD|467530 cd03424, NUDIX_ADPRase_Nudt5_UGPPase_Nudt14, ADP-ribose pyrophosphatase, UDP-glucose pyrophosphatase, and similar proteins. ADP-ribose pyrophosphatase (ADPRase) (NUDIX (Nucleoside diphosphate-linked moiety X)) motif 5; Nudt5) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as nucleoside diphosphate-linked moiety X)) motif 14; Nudt14) hydrolyzes the pyrophosphate of the nucleoside diphosphate sugar to generate glucose-1-P and UMP. In mammals, UDP-glucose is the glucosyl donor for the synthesis of the storage polysaccharide glycogen. UGPPase, as a regulator of UDP-glucose, could play a regulatory role, but it has been shown to prefer ADP-ribose over UDP-glucose. Like other members of the NUDIX hydrolase superfamily, it requires a divalent cation, such as Mg2+, for its activity. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site
HPGAVAVLAITDDGKVVLVRQYRHPVGRVLLELPAGKIDPGEDPEEAARRELEEETGYTAGDLELLGSFY
PSPGFSDERIHLFLAEDLTPVSEQALDEDEFIEVVLVPLEEALEMIEDGEITDAKTLAALLLAL
>gnl|CDD|467531 cd03425, NUDIX_MutT_NudA_like, MutT pyrophosphohydrolase. The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides
IEVVAAIIVDDGRVLIAQRPEGKHLAGLWEFPGGKVEPGETPEQALVRELREELGIEVEVGEPLGTVEHD
YPDFHVRLHVYLCTLWSGEPQLLEHQELRWVTPEELDDLDWLPADIPIVEALL
>gnl|CDD|467532 cd03426, NUDIX_CoAse_Nudt7, coenzyme A pyrophosphatase and similar proteins. Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1), also called nucleoside diphosphate-linked moiety X)) motif 7, is a member of the NUDIX hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved NUDIX fold and requires a single divalent cation for catalysis. In addition to a signature NUDIX motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules
RRAAVLIPLVEGDGELHVLLTKRASHLRSHPGQIAFPGGKREPGDESPVETALRETEEEIGLPPESVEVL
GRLDPLYTPSGFVVTPFVGLLDDPPPLRPNPDEVAEVFTVPLSFLLDPEPRRYETFLRSGPRGTYRVPFY
PYEGYVIWGLTARILSEL
>gnl|CDD|467533 cd03427, NUDIX_MTH1_Nudt1, MutT homolog-1 (MTH1). MutT homolog-1 (MTH1; EC 3.6.1.-), also called nucleoside diphosphate-linked moiety X)) motif 1 (Nudt1), is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases
KLTTLVFVLRGDDRVLLGLKKRGFGAGKWNGFGGKVEPGETIEEAAVRELEEEAGLTATELEKVGRLKFE
FPDDPEAMDVHVFRADSWTGEPQETEEMRPQWFDLDDIPYDKMWPDDRLWLPLLLEGKKFKGRFDF
>gnl|CDD|467534 cd03428, NUDIX_Ap4A_Nudt2, diadenosine tetraphosphate. Diadenosine tetraphosphate (Ap4A; EC 3.6.1.17), also called NUDIX (nucleoside diphosphate-linked moiety X)) motif 2/Nudt2, is a member of the NUDIX hydrolase superfamily. Ap4A hydrolases are well represented in a variety of prokaryotic and eukaryotic organisms. Phylogenetic analysis reveals two distinct subgroups where plant enzymes fall into one subfamily and fungi/animals/archaea enzymes, represented by this subfamily, fall into another. Bacterial enzymes are found in both subfamilies. Ap4A is a potential by-product of aminoacyl tRNA synthesis, and accumulation of Ap4A has been implicated in a range of biological events, such as DNA replication, cellular differentiation, heat shock, metabolic stress, and apoptosis. Ap4A hydrolase cleaves Ap4A asymmetrically into ATP and AMP. It is important in the invasive properties of bacteria and thus presents a potential target for inhibition of such invasive bacteria. Besides the signature NUDIX motif (G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val) that functions as a metal binding and catalytic site, and a required divalent cation, Ap4A hydrolase is structurally similar to the other members of the NUDIX hydrolase superfamily with some degree of variation. Several regions in the sequences are poorly defined and substrate and metal binding sites are only predicted based on kinetic studies
KEKSAGAIIYRRDNGEIEFLLLQHSYGGHWDFPKGHVEPGESELETALRETKEETGLTVDDLPPGFRETL
TYSFKEGVEKTVVYFLAELTPDVEVKLSEEHQDYKWLPYEEALQLLTYENIKELLKEANEYL
>gnl|CDD|467535 cd03429, NUDIX_NADH_pyrophosphatase_Nudt13, NADH pyrophosphatase. NADH pyrophosphatase, also known as NUDIX (nucleoside diphosphate linked moiety X)) motif 13/Nudt13, is thought to have NADH pyrophosphatase activity, be involved in NADH metabolic process and NADP catabolic process, catalyzing the cleavage of NADH into reduced nicotinamide mononucleotide (NMNH) and AMP, and located in mitochondrion. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity. Members of this family are also recognized by the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. A block of 8 conserved amino acids downstream of the NUDIX motif is thought to give NADH pyrophosphatase its specificity for NADH. NADH pyrophosphatase forms a dimer
DPAVIVLVTNGEDKILLARQPRWPPGRYSLLAGFVEPGETLEEAVRREVKEEVGLRVKNVRYVGSQPWPF
PSSLMLGFTAEADSGEITVDDDELEDARWFSRDELPEALFLPPPGSIARRLIRAWL
>gnl|CDD|467536 cd03430, NUDIX_GDPMH_NudD, GDP-mannose glycosyl hydrolase. GDP-mannose glycosyl hydrolase, also known as GDP-mannose mannosyl hydrolase/GDPMH, is a member of the NUDIX hydrolase superfamily. This class of enzymes is unique from other members of the superfamily in two aspects. First, it contains a modified NUDIX signature sequence. The slight changes to the conserved sequence motif, GX5EX7REUXEEXGU, where U = I, L or V), are believed to contribute to the removal of all magnesium binding sites but one, retaining only the metal site that coordinates the pyrophosphate of the substrate. Secondly, it is not a pyrophosphatase that substitutes at a phosphorus; instead, it hydrolyzes nucleotide sugars such as GDP-mannose to GDP and mannose, cleaving the phosphoglycosyl bond by substituting at a carbon position. GDP-mannose provides mannosyl components for cell wall synthesis and is required for the synthesis of other glycosyl donors (such as GDP-fucose and colitose) for the cell wall. The importance of GDP-sugar hydrolase activities is thus closely related to the regulation of cell wall biosynthesis. Enzymes in this family are believed to regulate the concentration of GDP-mannose and GDP-glucose in the bacterial cell wall
LPEEDFKTVVENTPLVSIDLIIRNEDGEILLGKRNNRPAQGYWFVPGGRILKNETLDDAFKRIAREELGL
EVTINAAEFLGVYEHFYDDNFSGEDFSTHYVVLAYRLKLDEGLLLLPDDQHDEYRWFTIDELLANDDVHP
YTKAYF
>gnl|CDD|467537 cd03431, NUDIX_DNA_Glycosylase_C-MutY, C-terminal domain of DNA glycosylase. DNA glycosylase (MutY in bacteria and hMYH in humans) is responsible for repairing misread A*oxoG residues to C*G by removing the inappropriately paired adenine base from the DNA backbone. It belongs to the NUDIX hydrolase superfamily and is important for the repair of various genotoxic lesions. Enzymes belonging to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity. They are also recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V). However, DNA glycosylase does not seem to contain this signature motif. DNA glycosylase consists of 2 domains: the N-terminal domain contains the catalytic properties of the enzyme and the C-terminal domain affects substrate (oxoG) binding and enzymatic turnover. The C-terminal domain is highly similar to MutT, based on secondary structure and topology, despite low sequence identity. MutT sanitizes the nucleotide precursor pool by hydrolyzing oxo-dGTP to oxo-dGMO and inorganic pyrophosphate. The similarity strongly suggests that the two proteins share a common evolutionary origin
VPERYFTVLVLRDGGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALLGLLAEELLLILEPLGEVKHV
FSHFRLHITVYLVELPEAPPAAPDEGRWVDLEELDEYALPAPMRKLLE
>gnl|CDD|239524 cd03440, hot_dog, The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis
FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEV
VRVGRSSVTVEVEVRNEDGKLVATATATFV
>gnl|CDD|239525 cd03441, R_hydratase_like, (R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. The structure of the monomer includes a five-strand antiparallel beta-sheet wrapped around a central alpha helix, referred to as a hot dog fold. The active site lies within a substrate-binding tunnel formed by the homodimer. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit
GELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTDGANL
GSQSVRFLAPVFPGDTLRVEVEVLGKRPSKGRGVVTVRTEARNQGGEVVLSGEATVL
>gnl|CDD|239526 cd03442, BFIT_BACH, Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy
VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVV
ELSARVVYTGRTSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPVP
>gnl|CDD|239527 cd03443, PaaI_thioesterase, PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ)
LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRP
ARGGDLTARARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV
>gnl|CDD|239528 cd03444, Thioesterase_II_repeat1, Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene
LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASASASLDHAIWFHRPFRADDWLLYE
QRSPRAGNGRGLVEGRIFTRDGELVASVAQEGLL
>gnl|CDD|239529 cd03445, Thioesterase_II_repeat2, Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene
DRFRGVSPPVPPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRS
FATRRVRAVQNGKVIFTATASFQR
>gnl|CDD|239530 cd03446, MaoC_like, MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but without the N-terminal PutA domain. This protein family has a hot-dog fold similar to that of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit
YFEDFEIGQVFESVGRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQRLG
VFERTVVAFYGIDNLRFLNPVFIGDTIRAEAEVVEKEEKDGEDAGVVTRRIEVVNQRGEVVQSGEMSLLV
>gnl|CDD|239531 cd03447, FAS_MaoC, FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and 17-beta-hydroxysteriod dehydrogenase (HSD)
RSGGASLTITAPASNEPYARVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRALVETWAADNDRSRV
RSFTASFVGMVLPNDELEVRLEHVGMVDGRKVIKVEARNEETGELVLRGEAEVEQP
>gnl|CDD|239532 cd03448, HDE_HSD, HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), and Hydratase-Dehydrogenase-Epimerase (HDE) proteins. Other enzymes with this fold include MaoC dehydratase, and the fatty acid synthase beta subunit
PDRAPDAVVEIPTSPDQALLYRLSGDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAARAVLEAFADGDPA
RFKAIKVRFSSPVFPGETLRTEMWKEGNRVIFQTKVVERDVVVLSNGAALLA
>gnl|CDD|239533 cd03449, R_hydratase, (R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain
LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGT
IYLSQSLRFLRPVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVVIEGEAVVLA
>gnl|CDD|239534 cd03450, NodN, NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. Rhizobium and related species form nodules on the roots of their legume hosts, a symbiotic process that requires production of Nod factors, which are signal molecules involved in root hair deformation and meristematic cell division. The nodulation gene products, including NodN, are involved in producing the Nod factors, however the role played by NodN is unclear
TFASLADLAALVGQELGVSDWVTVDQERIDQFADATGDHQWIHVDPERAAAEPFGGTIAHGFLTLSLLPA
LTPQLFRVEGVKMGVNYGLDKVRFPAPVPVGSRVRGRFTLLSVEELKGGGVQVTLEVTVEIEGEDKPACV
AEWISRLYF
>gnl|CDD|239535 cd03451, FkbR2, FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved family of proteins found in prokaryotes and archaea but not in eukaryotes. FkbR2 has sequence similarity to (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The function of FkbR2 is unknown
GLYFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSV
NDTSLTAVANLGYDEVRFPAPVFHGDTLYAESEVLSKRESKSRPDAGIVTVRTVGYNQDGEPVLSFERTA
LVPKRG
>gnl|CDD|239536 cd03452, MaoC_C, MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory protein. Orthologs of MaoC include PaaZ [Escherichia coli] and PaaN [Pseudomonas putida], which are putative ring-opening enzymes involved in phenylacetic acid degradation. The C-terminal domain of MaoC has sequence similarity to (R)-specific enoyl-CoA hydratase,Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. MaoC also has an N-terminal PutA domain like that found in the E. coli PutA proline dehydrogenase and other members of the aldehyde dehydrogenase family
NLEQLRPGDSLLTHRRTVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYFVLSAAAGLFVDPA
PGPVLANYGLENLRFLEPVYPGDTIQVRLTCKRKIPRDGQDYGVVRWDAEVTNQNGELVASYDILTLVAK
KG
>gnl|CDD|239537 cd03453, SAV4209_like, SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot dog fold that is similar to those of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit
VGDELPPLTPPVSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVGDPGRV
VSFGVRFTKPVPVPDTLTCTGIVVEKTVADGEDALTVTVDATDQAGGKKVLGRAIVA
>gnl|CDD|239538 cd03454, YdeM, YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown function. YdeM has sequence similarity to the hot-dog fold of (R)-specific enoyl-CoA hydratase. Other enzymes with this fold include the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit
FEDLVIGQRFTSGSYTVTEEEIIAFAREFDPQPFHLDEEAAKESLFGGLAASGWHTAAITMRLLVDAGLS
GSASGGSPGIDELRWPRPVRPGDTLSVEVEVLDKRPSRSRPDRGIVTLRSETLNQRGEVVLTFEATVLVR
>gnl|CDD|239539 cd03455, SAV4209, SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The alpha- and gamma-proteobacterial members of this CD have, in addition to a hot dog fold, an N-terminal extension
GDELPRLSIPPDPTLLFRYSAATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTDWAGPDARVK
SFAFRLGAPLYAGDTLRFGGRVTAKRDDEVVTVELWARNSEGDHVMAGTATVA
>gnl|CDD|239540 cd03457, intradiol_dioxygenase_like, Intradiol dioxygenase supgroup. Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of catecholate derivatives to citric acid cycle intermediates. They break the catechol C1-C2 bond and utilize Fe3+, as opposed to the extradiol-cleaving enzymes which break the C2-C3 or C1-C6 bond and utilize Fe2+ and Mn+. The family contains catechol 1,2-dioxygenases and protocatechuate 3,4-dioxygenases. The specific function of this subgroup is unknown
EVTEGPYYVDGELVRSDITEGQPGVPLTLDLQVVDVATCCPPPNAAVDIWHCDATGVYSGYSAGGGGGED
TDDETFLRGVQPTDADGVVTFTTIFPGWYPGRATHIHFKVHPDATSATSGGNVAHTGQLFFDEDLIEEVY
ATPPYNSNTNARTSNADDGIFSDGGAAGMLPTVELLGGSVSDGLFAWI
>gnl|CDD|239541 cd03458, Catechol_intradiol_dioxygenases, Catechol intradiol dioxygenases can be divided into several subgroups according to their substrate specificity for catechol, chlorocatechols and hydroxyquinols. Almost all members of this family are homodimers containing one ferric ion (Fe3+) per monomer. They belong to the intradiol dioxygenase family, a family of mononuclear non-heme iron intradiol-cleaving enzymes that catalyze the oxygenation of catecholates to aliphatic acids via the cleavage of aromatic rings
RLKQIMARLVRHLHDFIREVELTEDEWMAGVDFLNRVGQAGDDKRNEFILLSDVLGLESLVDEINHRKDT
GGTESTILGPFYVAGAPEVDNGATIDDDTADGEPLFVHGTVTDTDGKPLAGATVDVWHADPDGFYSQQDP
DQPEFNLRGKFRTDEDGRYRFRTIRPVPYPIPPDGPTGELLEALGRHPWRPAHIHFMVSAPGYRTLTTQI
YFEGDPYLDDDAVFAVKDSLIVDFVPVEDGTGVPGPFAELDFDFVL
>gnl|CDD|239542 cd03459, 3,4-PCD, Protocatechuate 3,4-dioxygenase (3,4-PCD) catalyzes the oxidative ring cleavage of 3,4-dihydroxybenzoate to produce beta-carboxy-cis,cis-muconate. 3,4-PCDs are large aggregates of 12 protomers, each composed of an alpha- and beta-subunit and an Fe3+ ion bound in the beta-subunit at the alpha-beta-subunit interface. 3,4-PCD is a member of the aromatic dioxygenases which are non-heme iron intradiol-cleaving enzymes that break the C1-C2 bond and utilize Fe3+
NDLTRKGGGEAIGERIILEGRVLDGDGRPVPDALVEIWQADAAGRYRHPRDSHRAPLDPNFTGFGRVLTD
ADGRYRFRTIKPGAYPWRNGAWRAPHIHVSVFARGLLERLVTRLYFPGDPANAADPVLASVPEERRETLI
ARRDGSDGALAYRFDIVL
>gnl|CDD|239543 cd03460, 1,2-CTD, Catechol 1,2 dioxygenase (1,2-CTD) catalyzes an intradiol cleavage reaction of catechol to form cis,cis-muconate. 1,2-CTDs is homodimers with one catalytic non-heme ferric ion per monomer. They belong to the aromatic dioxygenase family, a family of mononuclear non-heme iron intradiol-cleaving enzymes that catalyze the oxygenation of catecholates to aliphatic acids via the cleavage of aromatic rings
EVQALLKAAAGLDTAGGNPRVKQIVHRLLSDLFKAIDDLDITPDEFWSGVDYLNDLGQAGEAGLLAAGLG
FEHFLDLRMDAADAAAGITGGTPRTIEGPLYVAGAPESDGFARLDDGSDDDGETLVMHGTVTDTDGKPVP
GAKVEVWHANSKGFYSHFDPTQSPFNLRRSIITDADGRYRFRSIMPSGYGVPPGGPTQQLLNALGRHGNR
PAHIHFFVSAPGHRKLTTQINIEGDPYIWDDFAFATREGLIPEVVEVEDAAALKQYGLDGPFAEIAFDFQ
LQ
>gnl|CDD|239544 cd03461, 1,2-HQD, Hydroxyquinol 1,2-dioxygenase (1,2-HQD) catalyzes the ring cleavage of hydroxyquinol (1,2,4-trihydroxybenzene), a intermediate in the degradation of a large variety of aromatic compounds including some polychloro- and nitroaromatic pollutants, to form 3-hydroxy-cis,cis-muconates. 1,2-HQD blongs to the aromatic dioxygenase family, a family of mononuclear non-heme intradiol-cleaving enzymes
QNLTEAVIASMGPTTDPRLKEIMASLVRHLHDFAREVRLTEDEWMAGIDFLTETGQICDDKRNEFILLSD
VLGLSSLVDAINHRKPSGATESTVLGPFYREDAPEYENGASIVQGADGEPCFVHGRVTDTDGKPLPGATV
DVWQADPNGLYDVQDPDQPEFNLRGKFRTDEDGRYAFRTLRPTPYPIPTDGPVGKLLKAMGRHPMRPAHI
HFMVTAPGYRTLVTQIFDSGDPYLDSDAVFGVKDSLVVDFVPVEDDDAPGRLVPGADLELEYDFVLA
>gnl|CDD|239545 cd03462, 1,2-CCD, chlorocatechol 1,2-dioxygenases (1,2-CCDs) (type II enzymes) are homodimeric intradiol dioxygenases that degrade chlorocatechols via the addition of molecular oxygen and the subsequent cleavage between two adjacent hydroxyl groups. This reaction is part of the modified ortho-cleavage pathway which is a central oxidative bacterial pathway that channels chlorocatechols, derived from the degradation of chlorinated benzoic acids, phenoxyacetic acids, phenols, benzenes, and other aromatics into the energy-generating tricarboxylic acid pathway
MNNRVKAVVGDIVDAIRDVLLKHEVTYDEYRAGVQYLIKVGEAGEWPLLLDVFFNSTIEEVKARKRRGST
SAIEGPYFIENAPFVDGKLKTYDDDDHKPLLFRGTVKDLAGAPVAGAVIDVWHSTPDGKYSGFHPNIPED
YYRGKIRTDEDGRYEVRTTVPVPYQIPNDGPTGALLEAMGGHSWRPAHVHFKVRADGYETLTTQLYFEGG
EWVDDDCCNGVKPELILPEVKEDGVRVMTYDFVLEPA
>gnl|CDD|239546 cd03463, 3,4-PCD_alpha, Protocatechuate 3,4-dioxygenase (3,4-PCD), alpha subunit. 3,4-PCD catalyzes the oxidative ring cleavage of 3,4-dihydroxybenzoate to produce beta-carboxy-cis,cis-muconate. 3,4-PCDs are large aggregates of 12 protomers, each composed of an alpha- and beta-subunit and an Fe3+ ion bound in the beta-subunit at the alpha-subunit-beta-subunit interface. 3,4-PCD is a member of the aromatic dioxygenases which are non-heme iron intradiol-cleaving enzymes that break the C1-C2 bond and utilize Fe3+
LGETPSQTVGPYVHIGLPPTREGGNDLVPPDTAGERITLEGRVYDGDGAPVPDAMLEIWQADAAGRYAHP
ADSRRRLDPGFRGFGRVATDADGRFSFTTVKPGAVPGRDGAGQAPHINVWVFARGLLKHLFTRIYFPDEE
ANAADPVLALVPEERRATLIAKREGDGAYRFDIRLQGEGETVFFD
>gnl|CDD|239547 cd03464, 3,4-PCD_beta, Protocatechuate 3,4-dioxygenase (3,4-PCD), beta subunit. 3,4-PCD catalyzes the oxidative ring cleavage of 3,4-dihydroxybenzoate to produce beta-carboxy-cis,cis-muconate. 3,4-PCDs are large aggregates of 12 protomers, each composed of an alpha- and beta-subunit and an Fe3+ ion bound in the beta-subunit at the alpha-subunit-beta-subunit interface. 3,4-PCD is a member of the aromatic dioxygenases which are non-heme iron intradiol-cleaving enzymes that break the C1-C2 bond and utilize Fe3+
RDTEAHPPALTPDYKSSVLRSPKQPLISIPHTLSELTGPVFGHDDLGPLDNDLTRNHNGEPIGERIIVHG
RVLDEDGRPVPNTLVEIWQANAAGRYRHKRDQHDAPLDPNFGGAGRTLTDDDGYYRFRTIKPGAYPWGNH
PNAWRPAHIHFSLFGPSFATRLVTQMYFPGDPLIPHDPIYNSIPDEAARQRLIARFDLSATQPEWALGYR
FDIVLRGRRA
>gnl|CDD|239548 cd03465, URO-D_like, The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane
AAALNGEKPDRVPVGPLLHGGAAEFIGISLKEYYTDPELGAEAQIALYKKFGPDAIKVFSDLFVEAEAFG
AEIRYPEDDTPSVEGPLIEDEEEDDDLLPPDPGDSPRLPELLEAIRLLKEELGDRVPVIGAVGGPFTLAS
LLMGASKFLMLLYTDPELVHKLLEKCTEFIIRYADALIEAGADGIYISDPWASSSILSPEDFKEFSLPYL
KKVFDAIKALGGPVIHHNCGDTAPILELMADLGADVFSIDVTVDLAEAKKKVGDKACLMGNLDPIDVLLN
GSPEEIKEEVKELLEKLLKGGGGYILSSGCEIPPDTPIENIKAMIDAVRE
>gnl|CDD|239549 cd03466, Nitrogenase_NifN_2, Nitrogenase_nifN_2: A subgroup of the NifN subunit of the NifEN complex: NifN forms an alpha2beta2 tetramer with NifE. NifN and nifE are structurally homologous to nitrogenase MoFe protein beta and alpha subunits respectively. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of the MoFe protein. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to the NifEN complex where it is further processed to FeMoco. The nifEN bound precursor of FeMoco has been identified as a molybdenum-free, iron- and sulfur- containing analog of FeMoco. It has been suggested that this nifEN bound precursor also acts as a cofactor precursor in nitrogenase systems which require a cofactor other than FeMoco: i.e. iron-vanadium cofactor (FeVco) or iron only cofactor (FeFeco). This group also contains the Clostidium fused NifN-NifB protein
VNATINPCKICMPMGASMAFKGIEGCMPLLHGSQGCSTYIRRHMARHYNEPVDIASSSLNEETTVYGGEK
NLKKGLKNVIEQYNPEVIGIATTCLSETIGEDVPRIIREFREEVDDSEPKIIPASTPGYGGTHVEGYDTA
VRSIVKNIAVDPDKIEKINVIAGMMSPADIREIKEILREFGIEYILLPDTSETLDGPFWGEYHRLPSGGT
PISEIKGMGGAKATIELGMFVDHGLSAGSYLEEEFGIPNYRLPLPIGLRATDEFMSLLSKLTGKPIPEKY
TRERGRLLDAMIDAHKYNFGRKAAIYGEPDFVVAITRFVLENGMVPVLIATGSESKKLKEKLEEDLKEYV
EKCVILDGADFFDIESYAKELKIDVLIGNSYGRRIAEKLGIPLIRIGFPIHDRLGGQRIRSLGYEGSIEL
VDRITNTIL
>gnl|CDD|239550 cd03467, Rieske, Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis
WVVVGALSELPPGGGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDL
RTGEVVSGPAPRPLPKYPVKVEGDGVVW
>gnl|CDD|176458 cd03468, PolY_like, DNA Polymerase Y-family. Y-family DNA polymerases are a specialized subset of polymerases that facilitate translesion synthesis (TLS), a process that allows the bypass of a variety of DNA lesions. Unlike replicative polymerases, TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. The active sites of TLS polymerases are large and flexible to allow the accomodation of distorted bases. Expression of Y-family polymerases is often induced by DNA damage and is believed to be highly regulated. TLS is likely induced by the monoubiquitination of the replication clamp PCNA, which provides a scaffold for TLS polymerases to bind in order to access the lesion. Because of their high error rates, TLS polymerases are potential targets for cancer treatment and prevention
LALWFPRLPLDALLRNRPADDEAPLAVVERKKAGRILACNAAARAAGVRPGMPLAEALALCPNLQVVEYD
PEADARALQELALWLLRFTPLVALDGPDGLLLDVTGCLHLFGGEDALAASLRAALATLGLSARAGIADTP
GAAWLLARAGGGRGVLRREALAAALVLLAPLPVAALRLPPETVELLARLGLRTLGDLAALPRAELARRFG
LALLLRLDQAYGRDPEPLLFSPPPPAFDFRLELQLEEPIARGLLFPLRRLLEQLCAFLALRGLGARRLSL
TLFREDGRVTRVLVGLARPSRDDLPLLRLLRERLERLALPRGIAPVRLLALTAEP
>gnl|CDD|239551 cd03469, Rieske_RO_Alpha_N, Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha subunit; The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The oxygenase component may contain alpha and beta subunits, with the beta subunit having a purely structural function. Some oxygenase components contain only an alpha subunit. The oxygenase alpha subunit has two domains, an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from the reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Reduced pyridine nucleotide is used as the initial source of two electrons for dioxygen activation
WYFVGHSSELPEPGDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARLCEGRGGNAGRLVCPYHGWTY
DLDGKLVGVPREEGFPGFDKEKLGLRTVPVEEWGGLIFVNLDPDAPPL
>gnl|CDD|239552 cd03470, Rieske_cytochrome_bc1, Iron-sulfur protein (ISP) component of the bc(1) complex family, Rieske domain; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. The bc(1) complex is a multisubunit enzyme found in many different organisms including uni- and multi-cellular eukaryotes, plants (in their mitochondria) and bacteria. The cytochrome bc(1) and b6f complexes are central components of the respiratory and photosynthetic electron transport chains, respectively, which carry out similar core electron and proton transfer steps. The bc(1) and b6f complexes share a common core structure of three catalytic subunits: cyt b, the Rieske ISP, and either a cyt c1 in the bc(1) complex or cyt f in the b6f complex, which are arranged in an integral membrane-bound dimeric complex. While the core of the b6f complex is similar to that of the bc(1) complex, the domain arrangement outside the core and the complement of prosthetic groups are strikingly different
PVEVDLSKIEEGQLITVEWRGKPVFIRRRTPEEIAEAKAVDLSLLDDPDPAANRVRSGKPEWLVVIGICT
HLGCVPTYRAGDYGGFFCPCHGSHYDASGRIRKGPAPLNLEVPPYKFLSDTTIVIG
>gnl|CDD|239553 cd03471, Rieske_cytochrome_b6f, Iron-sulfur protein (ISP) component of the b6f complex family, Rieske domain; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. The cytochrome b6f complex from Mastigocladus laminosus, a thermophilic cyanobacterium, contains four large subunits, including cytochrome f, cytochrome b6, the Rieske ISP, and subunit IV; as well as four small hydrophobic subunits, PetG, PetL, PetM, and PetN. Rieske ISP, one of the large subunits of the cytochrome bc-type complexes, is involved in respiratory and photosynthetic electron transfer. The core of the chloroplast b6f complex is similar to the analogous respiratory cytochrome bc(1) complex, but the domain arrangement outside the core and the complement of prosthetic groups are strikingly different
VAAKDALGNDIKVSKWLATHNPGDRSLVQGLKGDPTYLIVEEDKTIANYGINAVCTHLGCVVPWNAAENK
FKCPCHGSQYDATGKVVRGPAPLSLALVHATVDDDKVVLSPWTETDFRTGEKPWWK
>gnl|CDD|239554 cd03472, Rieske_RO_Alpha_BPDO_like, Rieske non-heme iron oxygenase (RO) family, Biphenyl dioxygenase (BPDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of BPDO and similar proteins including cumene dioxygenase (CumDO), nitrobenzene dioxygenase (NBDO), alkylbenzene dioxygenase (AkbDO) and dibenzofuran 4,4a-dioxygenase (DFDO). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. BPDO degrades biphenyls and polychlorinated biphenyls (PCB's) while CumDO degrades cumene (isopropylbenzene), an aromatic hydrocarbon that is intermediate in size between ethylbenzene and biphenyl. NBDO catalyzes the initial reaction in nitrobenzene degradation, oxidizing the aromatic rings of mono- and dinitrotoluenes to form catechol and nitrite. NBDO belongs to the naphthalene subfamily of ROs. AkbDO is involved in alkylbenzene catabolism, converting o-xylene to 2,3- and 3,4-dimethylphenol and ethylbenzene to cis-dihydrodiol. DFDO is involved in dibenzofuran degradation
LERVFARSWLLLGHETHIPKAGDYLTTYMGEDPVIVVRQKDGSIRVFLNQCRHRGMRICRSDAGNAKAFT
CTYHGWAYDTAGNLVNVPFEKEAFCDGLDKADWGPLQARVETYKGLIFANWDAEAPDL
>gnl|CDD|239555 cd03473, Rieske_CMP_Neu5Ac_hydrolase_N, Cytidine monophosphate-N-acetylneuraminic acid (CMP Neu5Ac) hydroxylase family, N-terminal Rieske domain; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. CMP Neu5Ac hydroxylase is the key enzyme for the synthesis of N-glycolylneuraminic acid (NeuGc) from N-acetylneuraminic acid (Neu5Ac), NeuGc and Neu5Ac are members of a family of cell surface sugars called sialic acids. All mammals except humans have both NeuGc variants on their cell surfaces. In humans, the gene encoding CMP Neu5Ac hydroxylase has a mutation within its coding region that abolishes NeuGc production
QTAETVLSLSPEEVANLKEGINFFRNKEDGKKYIIYKSKSELKACKNQCKHQGGLFIKDIEDLDGRTVRC
TKHNWKLDVSTMKYVNPPDSFCQDELVVEYDEDGGLL
>gnl|CDD|239556 cd03474, Rieske_T4moC, Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. T4mo is a four-protein complex that catalyzes the NADH- and O2-dependent hydroxylation of toluene to form p-cresol. T4mo consists of an NADH oxidoreductase (T4moF), a diiron hydroxylase (T4moH), a catalytic effector protein (T4moD), and a Rieske ferredoxin (T4moC). T4moC contains a Rieske domain and functions as an obligate electron carrier between T4moF and T4moH. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes
FTKVCSLDDVWEGEMELVDVDGEEVLLVAPEGGEFRAFQGICPHQEIPLAEGGFDGGVLTCRAHLWQFDA
DTGEGLNPRDCRLARYPVKVEGGDILVDTEGVLPLFAH
>gnl|CDD|239557 cd03475, Rieske_SoxF_SoxL, SoxF and SoxL family, Rieske domain; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. SoxF is a subunit of the terminal oxidase supercomplex SoxM in the plasma membrane of Sulfolobus acidocaldarius that combines features of a cytochrome bc(1) complex and a cytochrome. The Rieske domain of SoxF has a 12 residue insertion which is not found in eukaryotic and bacterial Rieske proteins and is thought to influence the redox properties of the iron-sulfur cluster. SoxL is a Rieske protein which may be part of an archaeal bc-complex homologue whose physiological function is still unknown. SoxL has two features not seen in other Rieske proteins; (i) a significantly greater distance between the two cluster-binding sites and (ii) an unexpected Pro -_ Asp substitution at one of the cluster binding sites. SoxF and SoxL are found in archaea and in bacteria
GFPKYLLVNIKGGQQQLQVNSPKIYLFAYPLTNEPCFLLNLGASSGQPVVEIPNPVKYPGTGGQYTWPGG
VGPNKSIVAFSAICQHLGCQPPPIVSYPSYYPPDKAPGLASKGAVIHCCCHGSTYDPYKGGVVLTGPAPR
PLPAVILEYDSSTDDLYAVGTLGPEFSNGIP
>gnl|CDD|239558 cd03476, Rieske_ArOX_small, Small subunit of Arsenite oxidase (ArOX) family, Rieske domain; ArOX is a molybdenum/iron protein involved in the detoxification of arsenic, oxidizing it to arsenate. It consists of two subunits, a large subunit similar to members of the DMSO reductase family of molybdenum enzymes and a small subunit with a Rieske-type [2Fe-2S] cluster. The large subunit of ArOX contains the molybdenum site at which the oxidation of arsenite occurs. The small subunit contains a domain homologous to the Rieske domains of the cytochrome bc(1) and cytochrome b6f complexes as well as naphthalene 1,2-dioxygenase. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer
YPAVKVANLSQLSPGQPVTFNYPDESSPCVLVKLGVPVPGGVGPDNDIVAFSALCTHMGCPLTYDPSNKT
FVCPCHFSQFDPARGGQMVSGQATQNLPQIVLEYDEASGDIYAVGVQGLIYGRYSN
>gnl|CDD|239559 cd03477, Rieske_YhfW_C, YhfW family, C-terminal Rieske domain; YhfW is a protein of unknown function with an N-terminal DadA-like (glycine/D-amino acid dehydrogenase) domain and a C-terminal Rieske domain. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. It is commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. YhfW is found in bacteria, some eukaryotes and archaea
DITDIEDLAPGEGGVVNIGGKRLAVYRDEDGVLHTVSATCTHLGCIVHWNDAEKSWDCPCHGSRFSYDGE
VIEGPAVSGLKPADDAPIDNK
>gnl|CDD|239560 cd03478, Rieske_AIFL_N, AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family show similarity to human AIFL, containing an N-terminal Rieske domain and a C-terminal pyridine nucleotide-disulfide oxidoreductase domain (Pyr_redox). The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. AIFL shares 35% homology with human AIF (apoptosis-inducing factor), mainly in the Pyr_redox domain. AIFL is predominantly localized to the mitochondria. AIFL induces apoptosis in a caspase-dependent manner
AVVCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRT
GDIEDAPALDSLPCYEVEVEDGRVY
>gnl|CDD|239561 cd03479, Rieske_RO_Alpha_PhDO_like, Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of PhDO and similar proteins including 3-chlorobenzoate 3,4-dioxygenase (CBDO), phenoxybenzoate dioxygenase (POB-dioxygenase) and 3-nitrobenzoate oxygenase (MnbA). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. PhDO and CBDO are two-component RO systems, containing oxygenase and reductase components. PhDO catalyzes the dihydroxylation of phthalate to form the 4,5-dihydro-cis-dihydrodiol of phthalate (DHD). CBDO, together with CbaC dehydrogenase, converts the environmental pollutant 3CBA to protocatechuate (PCA) and 5-Cl-PCA, which are then metabolized by the chromosomal PCA meta (extradiol) ring fission pathway. POB-dioxygenase catalyzes the initial catabolic step in the angular dioxygenation of phenoxybenzoate, converting mono- and dichlorinated phenoxybenzoates to protocatechuate and chlorophenols. These phenoxybenzoates are metabolic products formed during the degradation of pyrethroid insecticides
DNELLTRVGPGTPMGELLRRYWQPVALSSELTEDGQPVRVRLLGEDLVAFRDTSGRVGLLDEHCPHRGAS
LVFGRVEECGLRCCYHGWKFDVDGQCLEMPSEPPDSQLKQKVRQPAYPVRERGGLVWAYMGPAEEAPEFP
RYDW
>gnl|CDD|239562 cd03480, Rieske_RO_Alpha_PaO, Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of a small subfamily of enzymes found in plants as well as oxygenic cyanobacterial photosynthesizers including LLS1 (lethal leaf spot 1, also known as PaO) and ACD1 (accelerated cell death 1). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. PaO expression increases upon physical wounding of plant leaves and is thought to catalyze a key step in chlorophyll degradation. The Arabidopsis-accelerated cell death gene ACD1 is involved in oxygenation of PaO
PEPAGGSDSDKFDWREVWYPVAYVEDLDPSRPTPFTLLGRDLVIWWDRNSQQWRAFDDQCPHRLAPLSEG
RIDEEGCLECPYHGWSFDGSGSCQRIPQAAEGGKAHTSPRACVASLPTAVRQGLLFVWPGEPENAKAT
>gnl|CDD|239563 cd03481, TopoIIA_Trans_ScTopoIIA, TopoIIA_Trans_ScTopoIIA: Transducer domain, having a ribosomal S5 domain 2-like fold, of the type found in proteins of the type IIA family of DNA topoisomerases similar to Saccharomyces cerevisiae Topo IIA. S. cerevisiae Topo IIA is a homodimer encoded by a single gene. The type IIA enzymes are the predominant form of topoisomerase and are found in some bacteriophages, viruses and archaea, and in all bacteria and eukaryotes. All type IIA topoisomerases are related to each other at amino acid sequence level, though their oligomeric organization sometimes differs. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. TopoIIA enzymes also catenate/ decatenate duplex rings. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes
KSFKDYVKLYLKDANKEDGPPPPVVYEPVNDRWEVAVALSDGQFQQVSFVNSIATTKGGTHVDYVADQIV
KKLDEVVKKKNKGGINVKPFQVKNHLWIFVNCLIENPSFDSQTKETLTTKPKSFGSKCELSEKFLKKAVK
SGIVESVLSWAKF
>gnl|CDD|239564 cd03482, MutL_Trans_MutL, MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to Escherichia coli MutL. EcMutL belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from the ATP-binding site to the DNA breakage/reunion regions of the enzymes. It has been suggested that during initiation of DNA mismatch repair in E. coli, the mismatch recognition protein MutS recruits MutL in the presence of ATP. The MutS(ATP)-MutL ternary complex formed, then recruits the latent endonuclease MutH. Prokaryotic MutS and MutL are homodimers
KLQRLADILGEDFAEQALAIDEEAGGLRLSGWIALPTFARSQADIQYFYVNGRMVRDKLISHAVRQAYSD
VLHGGRHPAYVLYLELDPAQVDVNVHPAKHEVRFRDSRLVHDFIYHAVKKALA
>gnl|CDD|239565 cd03483, MutL_Trans_MLH1, MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to yeast and human MLH1 (MutL homologue 1). This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. MLH1 forms heterodimers with PMS2, PMS1 and MLH3. These three complexes have distinct functions in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Roles for hMLH1-hPMS1 or hMLH1-hMLH3 in MMR have not been established. Cells lacking hMLH1 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 causes predisposition to HNPCC, Muir-Torre syndrome and Turcot syndrome (HNPCC variant). Mutation in hMLH1 accounts for a large fraction of HNPCC families
STKDNIRSVYGAAVANELIEVEISDDDDDLGFKVKGLISNANYSKKKIIFILFINNRLVECSALRRAIEN
VYANYLPKGAHPFVYLSLEIPPENVDVNVHPTKREVHFLNEEEIIERIQKLVEDKLS
>gnl|CDD|239566 cd03484, MutL_Trans_hPMS_2_like, MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to human PSM2 (hPSM2). hPSM2 belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. Included in this group are proteins similar to yeast PMS1. The yeast MLH1-PMS1 and the human MLH1-PMS2 heterodimers play a role in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Cells lacking hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hPMS2 causes predisposition to HPNCC and Turcot syndrome
DIKDNIINVFGGKVIKGLIPINLELDVNPTKEELDSDEDLADSEVKITGYISKPSHGCGRSSSDRQFFYI
NGRPVDLKKVAKLINEVYKSFNSRQYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSEL
FE
>gnl|CDD|239567 cd03485, MutL_Trans_hPMS_1_like, MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to human PSM1 (hPSM1) and yeast MLH2. hPSM1 and yMLH2 are members of the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. PMS1 forms a heterodimer with MLH1. The MLH1-PMS1 complex functions in meiosis. Loss of yMLH2 results in a small but significant decrease in spore viability and a significant increase in gene conversion frequencies. A role for hMLH1-hPMS1 in DNA mismatch repair has not been established. Mutation in hMLH1 accounts for a large fraction of Lynch syndrome (HNPCC) families, however there is no convincing evidence to support hPMS1 having a role in HNPCC predisposition
DHKEALARVLGTAVAANMVPVQSTDEDPQISLEGFLPKPGSDVSKTKSDGKFISVNSRPVSLGKDIGKLL
RQYYSSAYRKSSLRRYPVFFLNILCPPGLVDVNIEPDKDDVLLQNKEAVLQAVENLLESLYG
>gnl|CDD|239568 cd03486, MutL_Trans_MLH3, MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to yeast and human MLH3 (MutL homologue 3). MLH3 belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. MLH1 forms heterodimers with MLH3. The MLH1-MLH3 complex plays a role in meiosis. A role for hMLH1-hMLH3 in DNA mismatch repair (MMR) has not been established. It has been suggested that hMLH3 may be a low risk gene for colorectal cancer; however there is little evidence to support it having a role in classical HNPCC
SILSVFKQIYGLVLAQKLKEVSAKFQEYEVSGYISSEGHYSKSFQFIYVNGRLYLKTRFHKLINKLFRKT
SAVAKNKSSPQSKSSRRGKRSQESYPVFVLNITCPASEYDLSQEPSKTIIEFKDWKTLLPLILEVVKSFL
K
>gnl|CDD|239569 cd03487, RT_Bac_retron_II, RT_Bac_retron_II: Reverse transcriptases (RTs) in bacterial retrotransposons or retrons. The polymerase reaction of this enzyme leads to the production of a unique RNA-DNA complex called msDNA (multicopy single-stranded (ss)DNA) in which a small ssDNA branches out from a small ssRNA molecule via a 2'-5'phosphodiester linkage. Bacterial retron RTs produce cDNA corresponding to only a small portion of the retron genome
KKNGGFRTIYAPKPELKAIQRKILSNLLSKLPVHDAAHGFVKGRSIITNAKPHCGAKYVLKLDIKDFFPS
ITFERVRGVFRSLGYFSPDVATILAKLCTYNGHLPQGAPTSPALSNLVFRKLDERLSKLAKSNGLTYTRY
ADDITFSSNKKLKEALDKLLEIIRSILSEEGFKINKSKTRISSKGSRQIVTGLVVNNGKPSLPRKEKRKI
RALL
>gnl|CDD|239570 cd03488, Topoisomer_IB_N_htopoI_like, Topoisomer_IB_N_htopoI_like : N-terminal DNA binding fragment found in eukaryotic DNA topoisomerase (topo) IB proteins similar to the monomeric yeast and human topo I. Topo I enzymes are divided into: topo type IA (bacterial) and type IB (eukaryotic). Topo I relaxes superhelical tension in duplex DNA by creating a single-strand nick, the broken strand can then rotate around the unbroken strand to remove DNA supercoils and, the nick is religated, liberating topo I. These enzymes regulate the topological changes that accompany DNA replication, transcription and other nuclear processes. Human topo I is the target of a diverse set of anticancer drugs including camptothecins (CPTs). CPTs bind to the topo I-DNA complex and inhibit religation of the single-strand nick, resulting in the accumulation of topo I-DNA adducts. This family may represent more than one structural domain
KWTTLEHNGPVFAPPYEPLPKNVKFYYDGKPVKLSPEAEEVATFYAKMLEHDYATKEIFQKNFFKDFKKV
MTKEEKVIIKDFSKCDFTQMFAYFKAQKEEKKAMSKEEKKAIKAEKEKLEEEYGFCILDGHKEKVGNFRI
EPPGLFRGRGAHPKTGKLKRRIMPEDIIINIGKDAKVPEPPPGHKWKEVRHDNTVTWLASWTENINGSIK
YVMLN
>gnl|CDD|239571 cd03489, Topoisomer_IB_N_LdtopoI_like, Topoisomer_IB_N_LdtopoI_like: N-terminal DNA binding fragment found in eukaryotic DNA topoisomerase (topo) IB proteins similar to the heterodimeric topo I from Leishmania donvanni. Topo I enzymes are divided into: topo type IA (bacterial) and type IB (eukaryotic). Topo I relaxes superhelical tension in duplex DNA by creating a single-strand nick, the broken strand can then rotate around the unbroken strand to remove DNA supercoils and, the nick is religated, liberating topo I. These enzymes regulate the topological changes that accompany DNA replication, transcription and other nuclear processes. Human topo I is the target of a diverse set of anticancer drugs including camptothecins (CPTs). CPTs bind to the topo I-DNA complex and inhibit re-ligation of the single-strand nick, resulting in the accumulation of topo I-DNA adducts. In addition to differences in structure and some biochemical properties, Trypanosomatid parasite topo I differ from human topo I in their sensitivity to CPTs and other classical topo I inhibitors. Trypanosomatid topo I play putative roles in organizing the kinetoplast DNA network unique to these parasites. This family may represent more than one structural domain
RWTTLVHNGVLFPPPYKPHGIPILYNGQPFDMTPEEEEVATMFAVMKEHDYYRKEVFRRNFFESWREILD
KRHHPIRKLELCDFTPIYEWHLREKEKKKSRTKEEKKALKEEKDKEAEPYMWCVWDGVKEQVANFRVEPP
GLFRGRGEHPKMGKLKKRIQPEDITINIGKGAPIPECPAGHKWKEVKHDNTVTWLAMWRDPIAGNFKYVM
LA
>gnl|CDD|239572 cd03490, Topoisomer_IB_N_1, Topoisomer_IB_N_1: A subgroup of the N-terminal DNA binding fragment found in eukaryotic DNA topoisomerase (topo) IB. Topo IB proteins include the monomeric yeast and human topo I and heterodimeric topo I from Leishmania donvanni. Topo I enzymes are divided into: topo type IA (bacterial) and type IB (eukaryotic). Topo I relaxes superhelical tension in duplex DNA by creating a single-strand nick, the broken strand can then rotate around the unbroken strand to remove DNA supercoils and, the nick is religated, liberating topo I. These enzymes regulate the topological changes that accompany DNA replication, transcription and other nuclear processes. Human topo I is the target of a diverse set of anticancer drugs including camptothecins (CPTs). CPTs bind to the topo I-DNA complex and inhibit religation of the single-strand nick, resulting in the accumulation of topo I-DNA adducts. In addition to differences in structure and some biochemical properties, Trypanosomatid parasite topos I differ from human topo I in their sensitivity to CPTs and other classical topo I inhibitors. Trypanosomatid topos I have putative roles in organizing the kinetoplast DNA network unique to these parasites. This family may represent more than one structural domain
QWKYLEHNGMIFTPPYVPHNVPIMYKGETIHLPPNLEEIATYWAQSMGTNYETKEKFCKNFWKVFVNSFE
KDHKFIRRCKLSDADFSLIKNHLEEEKEKKKNLNKEEKEAKKKERAKREYPFNYALVDWIREKVSSNKLE
PPGLFKGRGEHPKQGLLKSRIFPEDVILNISKDAPVPKVTNFMEGHSWKDIYHDNSVTWLAYYKDSINDQ
FKYMFLS
>gnl|CDD|239573 cd03493, SQR_QFR_TM, Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) family, transmembrane subunits; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol, while QFR catalyzes the reverse reaction. SQR, also called succinate dehydrogenase or Complex II, is part of the citric acid cycle and the aerobic respiratory chain, while QFR is involved in anaerobic respiration with fumarate as the terminal electron acceptor. SQRs may reduce either high or low potential quinones while QFRs oxidize only low potential quinols. SQR and QFR share a common subunit arrangement, composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit(s) containing the electron donor/acceptor (quinol or quinone). The reversible reduction of quinone is an essential feature of respiration, allowing the transfer of electrons between respiratory complexes. SQRs and QFRs can be classified into five types (A-E) according to the number of their hydrophobic subunits and heme groups. This classification is consistent with the characteristics and phylogeny of the catalytic and iron-sulfur subunits. Type E proteins, e.g. non-classical archael SQRs, contain atypical transmembrane subunits and are not included in this hierarchy. The heme and quinone binding sites reside in the transmembrane subunits. Although succinate oxidation and fumarate reduction are carried out by separate enzymes in most organisms, some bifunctional enzymes that exhibit both SQR and QFR activities exist
ILHRITGVALLLFLPLHLLGLLALLGGPYAFAEVVAFLSSPLGKLLYLLLLLALLYHALNGIRHLIWDYG
KGLELKLRKALGYAVLALSVLLTVLLLF
>gnl|CDD|239574 cd03494, SQR_TypeC_SdhD, Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. E. coli SQR, a member of this subfamily, reduces the high potential quinine, ubiquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are classified as Type C SQRs because they contain two transmembrane subunits and one heme group. SdhD and SdhC are the two transmembrane proteins of bacterial SQRs. They contain heme and quinone binding sites. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes
DWLVQRVTAVIMALYTIFLVGFLLASPPLTYEAWSGLFSSLWMKIFTLLALLALLLHAWIGLWDILTDYV
KPAGLRLLLQVLIILVLFGYLIWGIQILW
>gnl|CDD|239575 cd03495, SQR_TypeC_SdhD_like, Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) subunit-like; composed of predominantly uncharacterized bacterial proteins with similarity to the E. coli SdhD subunit. One characterized protein is the respiratory Complex II SdhD subunit of the only eukaryotic member, Reclinomonas americana. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. It is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. E. coli SQR is classified as Type C SQRs because it contains two transmembrane subunits and one heme group. The SdhD and SdhC subunits are membrane anchor subunits containing heme and quinone binding sites. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes
HHWWAQRVTAVALVPLVLWFVFSVALLLGASYAEVVAWLAHPFNAILLILTLVSAFYHARLGMQVVIEDY
VHSEGLRLALIIAVKLFAIATAAAGIFAIL
>gnl|CDD|239576 cd03496, SQR_TypeC_CybS, SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Eukaryotic SQRs reduce high potential quinones such as ubiquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are classified as Type C SQRs because they contain two transmembrane subunits and one heme group. CybS and CybL are the two transmembrane proteins of eukaryotic SQRs. They contain heme and quinone binding sites. CybS is the eukaryotic homolog of the bacterial SdhD subunit. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the transmembrane subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes. Mutations in human Complex II result in various physiological disorders including hereditary paraganglioma and pheochromocytoma tumors. The gene encoding for the SdhD subunit is classified as a tumor suppressor gene
LHGSYHWTFERILAVSLLPLTPAAFFAPGLSPVMDAALAAALLLHSHWGFESCIIDYVPKRVGGKLHKLA
MYLLYAGSALSLAGLYYFNTNDVGLTKAVKKLWS
>gnl|CDD|239577 cd03497, SQR_TypeB_1_TM, Succinate:quinone oxidoreductase (SQR) Type B subfamily 1, transmembrane subunit; composed of proteins similar to Bacillus subtilis SQR. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Bacillus subtilis SQR reduces low potential quinones such as menaquinone. SQR is also called succinate dehydrogenase (Sdh) or Complex II and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are classified as Type B as they contain one transmembrane subunit and two heme groups. The heme and quinone binding sites reside on the transmembrane subunit. The transmembrane subunit of Bacillus subtilis SQR is also called Sdh cytochrome b558 subunit. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit containing the electron acceptor (quinone). The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes
RNEFIIRRLHSLLGVVPIGLFLIEHLLTNSSAASGPEGFNAAVNFMHSLPGLLLIEIFGIFLPLLFHAIY
GIYIAFTAKSNTGRYDYFRNWMYTLQRITGIILLVFIAWHVWHTRFAEALGHVDIQTPEAGEANLSAMRN
ALASPLMLIFYIIGVLAAVFHFANGLWTFLITWGITVSPRSQRVSTYVCLLVFVVVSFMGVAAIWAF
>gnl|CDD|239578 cd03498, SQR_TypeB_2_TM, Succinate:quinone oxidoreductase (SQR)-like Type B subfamily 2, transmembrane subunit; composed of proteins with similarity to the SQRs of Geobacter metallireducens and Corynebacterium glutamicum. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. C. glutamicum SQR reduces low potential quinones such as menaquinone. SQR is also called succinate dehydrogenase (Sdh) or Complex II and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are classified as Type B as they contain one transmembrane subunit and two heme groups. The heme and quinone binding sites reside in the transmembrane subunit. The transmembrane subunit of members of this subfamily is also called Sdh cytochrome b558 subunit based on the Bacillus subtilis protein. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit containing the electron acceptor (quinone). The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes. Proteins in this subfamily from G. metallireducens and G. sulfurreducens are bifunctional enzymes with SQR and QFR activities
KKVLMALTGLFLVLFLLVHLLGNLKIFFGPEAFNAYAEFLHTLNPLLWIARLVLLVAAVLHIVFGLQLTI
RNRAARPVRYAVKNRKKLASLASRTMIWSGLIILLFIILHLLDFTFGVVGPVSPPMGVGRGDVYELLVAS
FQQPWIAALYVLAMVALGLHLSHGFWSAFQTLGLNNPRYRPALKAVGRVVAILIAGGFISIPLLILFGL
>gnl|CDD|239579 cd03499, SQR_TypeC_SdhC, Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase C (SdhC) subunit; composed of bacterial SdhC and eukaryotic large cytochrome b binding (CybL) proteins. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this family reduce high potential quinones such as ubiquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Proteins in this subfamily are classified as Type C SQRs because they contain two transmembrane subunits and one heme group. The heme and quinone binding sites reside in the transmembrane subunits. The SdhC or CybL protein is one of the two transmembrane subunits of bacterial and eukaryotic SQRs. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes
RPLSPHLTIYRPPLTAILSILHRITGVALFLGLPLLLWWLLASLSSPESFESVSALLGSWLGKLVLFGLT
WALFYHLLNGIRHLIWDLGKGLELKTVYKSGYAVLVLSVVLTVLLGI
>gnl|CDD|239580 cd03500, SQR_TypeA_SdhD_like, Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase D (SdhD)-like subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this subfamily reduce low potential quinones such as menaquinone and thermoplasmaquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are similar to the Thermoplasma acidophilum SQR and are classified as Type A because they contain two transmembrane subunits as well as two heme groups. Although there are no structures available for this subfamily, the presence of two hemes has been proven spectroscopically for T. acidophilum. The two membrane anchor subunits are similar to the SdhD and SdhC subunits of bacterial SQRs, which contain heme and quinone binding sites. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes
ESLAWLFQRITGVFLVFLLAGHFWVQHMDNGGDVIDFAFVANRLASPLWKVWDLLLLVLALLHGGNGLRN
ILLDYVRRPRLRRAVKGLLYVAGLLLIVLGTYVIFA
>gnl|CDD|239581 cd03501, SQR_TypeA_SdhC_like, Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase C (SdhC)-like subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this subfamily reduce low potential quinones such as menaquinone and thermoplasmaquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are similar to the Thermoplasma acidophilum SQR and are classified as Type A because they contain two transmembrane subunits as well as two heme groups. Although there are no structures available for this subfamily, the presence of two hemes has been proven spectroscopically for T. acidophilum. The two membrane anchor subunits are similar to the SdhD and SdhC subunits of bacterial SQRs, which contain heme and quinone binding sites. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes
MWAWVLHRITGVVILFYLFLHVLDLSSLRRGPETYNAVIATYKSPIFKLGEFGLVAAVVFHALNGIRLIL
VDFGSGGPRYQRQLFYIVLVLTVVLIVAAGY
>gnl|CDD|239582 cd03505, Delta9-FADS-like, The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl CoA desaturases found in various eukaryotes including vertebrates, insects, higher plants, and fungi. The delta-9 acyl-lipid desaturases are found in a wide range of bacteria. These enzymes play essential roles in fatty acid metabolism and the regulation of cell membrane fluidity. Acyl-CoA desaturases are the enzymes involved in the CoA-bound desaturation of fatty acids. Mammalian stearoyl-CoA delta-9 desaturase is a key enzyme in the biosynthesis of monounsaturated fatty acids, and in yeast, the delta-9 acyl-CoA desaturase (OLE1) reaction accounts for all de nova unsaturated fatty acid production in Saccharomyces cerevisiae. These non-heme, iron-containing, ER membrane-bound enzymes are part of a three-component enzyme system involving cytochrome b5, cytochrome b5 reductase, and the delta-9 fatty acid desaturase. This complex catalyzes the NADH- and oxygen-dependent insertion of a cis double bond between carbons 9 and 10 of the saturated fatty acyl substrates, palmitoyl (16:0)-CoA or stearoyl (18:0)-CoA, yielding the monoenoic products palmitoleic (16:l) or oleic (18:l) acids, respectively. In cyanobacteria, the biosynthesis of unsaturated fatty acids is initiated by delta 9 acyl-lipid desaturase (DesC) which introduces the first double bond at the delta-9 position of a saturated fatty acid that has been esterified to a glycerolipid. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXXH, HXXHH, and H/QXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the rat stearoyl CoA delta-9 desaturase. Some eukaryotic (Fungi, Euglenozoa, Mycetozoa, Rhodophyta) desaturase domains have an adjacent C-terminal cytochrome b5-like domain
SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDT
DGDPHSPKRGFWFSHVGWLGGLLRIVLVLHATWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHN
NHHAFPGDARNGLKWYQIDPTKWVIRLLEKLGLAWDLK
>gnl|CDD|239583 cd03506, Delta6-FADS-like, The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: delta-4, delta-5, delta-6, delta-8, delta-8-sphingolipid, and delta-11 desaturases found in vertebrates, higher plants, fungi, and bacteria. These desaturases are required for the synthesis of highly unsaturated fatty acids (HUFAs), which are mainly esterified into phospholipids and contribute to maintaining membrane fluidity. While HUFAs may be required for cold tolerance in bacteria, plants and fish, the primary role of HUFAs in mammals is cell signaling. These enzymes are described as front-end desaturases because they introduce a double bond between the pre-exiting double bond and the carboxyl (front) end of the fatty acid. Various substrates are involved, with both acyl-coenzyme A (CoA) and acyl-lipid desaturases present in this CD. Acyl-lipid desaturases are localized in the membranes of cyanobacterial thylakoid, plant endoplasmic reticulum (ER), and plastid; and acyl-CoA desaturases are present in ER membrane. ER-bound plant acyl-lipid desaturases and acyl-CoA desaturases require cytochrome b5 as an electron donor. Most of the eukaryotic desaturase domains have an adjacent N-terminal cytochrome b5-like domain. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXH, HXX(X)HH, and Q/HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase
LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHNVHHAYTNILGHDPD
IDTLPLLARSEPAFGKDQKKRFLHRYQHFYFFPLLALLLLAFLVVQLAGGLWLAVVFQLNHFGMPVEDPP
GESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPKVAPLVRELCKKHGL
>gnl|CDD|239584 cd03507, Delta12-FADS-like, The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane enzymes, delta-12 acyl-lipid desaturases, oleate 12-hydroxylases, omega3 and omega6 fatty acid desaturases, and other related proteins, found in a wide range of organisms including higher plants, green algae, diatoms, nematodes, fungi, and bacteria. The expression of these proteins appears to be temperature dependent: decreases in temperature result in increased levels of fatty acid desaturation within membrane lipids subsequently altering cell membrane fluidity. An important enzyme for the production of polyunsaturates in plants is the oleate delta-12 desaturase (Arabidopsis FAD2) of the endoplasmic reticulum. This enzyme accepts l-acyl-2-oleoyl-sn-glycero-3-phosphocholine as substrate and requires NADH:cytochrome b oxidoreductase, cytochrome b, and oxygen for activity. FAD2 converts oleate(18:1) to linoleate (18:2) and is closely related to oleate 12-hydroxylase which catalyzes the hydroxylation of oleate to ricinoleate. Plastid-bound desaturases (Arabidopsis delta-12 desaturase (FAD6), omega-3 desaturase (FAD8), omega-6 desaturase (FAD6)), as well as, the cyanobacterial thylakoid-bound FADSs require oxygen, ferredoxin, and ferredoxin oxidoreductase for activity. As in higher plants, the cyanobacteria delta-12 (DesA) and omega-3 (DesB) FADSs desaturate oleate (18:1) to linoleate (18:2) and linoleate (18:2) to linolenate (18:3), respectively. Omega-3 (DesB/FAD8) and omega-6 (DesD/FAD6) desaturases catalyze reactions that introduce a double bond between carbons three and four, and carbons six and seven, respectively, from the methyl end of fatty acids. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXX(X)HH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homologue, stearoyl CoA desaturase. Mutation of any one of four of these histidines in the Synechocystis delta-12 acyl-lipid desaturase resulted in complete inactivity
RSLFRSLSYLAPDILLLALLALAASLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVG
HILHSPLLVPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRLPYRLYRNPFLMLSLGWPYYLL
LNVLLYYLIPYLVVNAWLVLITYLQHTFPDIPWYRADEWNFAQAGLLGTVDRDYGGWLNWLTHIIGTHVA
HHLFPRIPHYNL
>gnl|CDD|239585 cd03508, Delta4-sphingolipid-FADS-like, The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the integral-membrane enzymes, dihydroceramide Delta-4 desaturase, involved in the synthesis of sphingosine; and the human membrane fatty acid (lipid) desaturase (MLD), reported to modulate biosynthesis of the epidermal growth factor receptor; and other related proteins. These proteins are found in various eukaryotes including vertebrates, higher plants, and fungi. Studies show that MLD is localized to the endoplasmic reticulum. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase
ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNL
AFGKPLWNRLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQP
FFYALRPLFVRPKPPTRLEVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFT
GKGQETYSYYGPLNLLTFNVGYHNEHHDFPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNV
GPYSRVKRK
>gnl|CDD|239586 cd03509, DesA_FADS-like, Fatty acid desaturase protein family subgroup, a delta-12 acyl-lipid desaturase-like, DesA-like, yet uncharacterized subgroup of membrane fatty acid desaturase proteins found in alpha-, beta-, and gamma-proteobacteria. Sequences of this domain family appear to be structurally related to membrane fatty acid desaturases and alkane hydroxylases. They all share in common extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase
EWPTWALIAVCYGGWLAVVFLLARLPLPLATLLLIPLAALHSSLQHELLHGHPTRSRWVNEALGYPPLAL
WYPYTRYRDTHLAHHRDEDLTDPGDDPESNYLSPEQWARLPRWQRALLRANNTLLGRLILGPPLGLIAFA
RDEFRALRAGDRAALRAWLLHAALLAPLLAWLQLSAGIPWWAYLLAVYYPALSLAKIRTFLEHRAHERPR
GRTVINEAGGPLRLLFLNNNLHVVHHDLPTLPWYDLPRLYRARRDAYLRRNGGFVYRGYGELFRRHAWRA
KDPPVHPF
>gnl|CDD|239587 cd03510, Rhizobitoxine-FADS-like, This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in Bradyrhizobium japonicum USDA110, and other related proteins. Dihydrorhizobitoxine desaturase is reported to be involved in the final step of rhizobitoxine biosynthesis. This domain family appears to be structurally related to the membrane fatty acid desaturases and the alkane hydroxylases. They all share in common extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXX(X)HH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase
DWLVIAAAVALALAWPNWLAYLLAVLLIGARQRALAILMHDAAHGLLFRNRRLNDFLGNWLAAVPIFQSL
AAYRRSHLKHHRHLGTEDDPDLALYLLLWLVPLLTVFPLIGRIREIAEHAGVPADEDPDARNTRTTFGGW
IERLLFAPHNINYHLEHHLFPAVPFYNLPKAHRIL
>gnl|CDD|239588 cd03511, Rhizopine-oxygenase-like, This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine (3-O-methyl-scyllo-inosamine, 3-O-MSI) oxygenase, and other related proteins. It has been proposed that MocD, MocE (Rieske-like ferredoxin), and MocF (ferredoxin reductase) under the regulation of MocR, act in concert to form a ferredoxin oxygenase system that demethylates 3-O-MSI to form scyllo-inosamine. This domain family appears to be structurally related to the membrane fatty acid desaturases and the alkane hydroxylases. They all share in common extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase
LPRQELKQLMQRSDAPGLLDTALWLGALAVSGILIAWTWGSWWALPAFLVYGVLYAALFARWHECVHGTA
FATRWLNDAVGQIAGLMILLPPDFFRWSHARHHRYTQIPGRDPELAVPRPPTLREYLLALSGLPYWWGKL
RTVFRHAFGAVSEAEKPFIPAEERPKVVREARAMLAVYAGLIALSLYLGSPLLVLVWGLPLLLGQPILRL
FLLAEHGGCPEDANDLRNTRTTLTNPPLRFLYWNMPYHAEHHMYPSVPFHALPKLHELIKDDLPVPYPGY
IAVYR
>gnl|CDD|239589 cd03512, Alkane-hydroxylase, Alkane hydroxylase is a bacterial, integral-membrane di-iron enzyme that shares a requirement for iron and oxygen for activity similar to that of the non-heme integral-membrane acyl coenzyme A (CoA) desaturases and acyl lipid desaturases. The alk genes in Pseudomonas oleovorans encode conversion of alkanes to acyl CoA. The alkane omega-hydroxylase (AlkB) system is responsible for the initial oxidation of inactivated alkanes. It is a three-component system comprising a soluble NADH-rubredoxin reductase (AlkT), a soluble rubredoxin (AlkG), and the integral membrane oxygenase (AlkB). AlkB utilizes the oxygen rebound mechanism to hydroxylate alkanes. This mechanism involves homolytic cleavage of the C-H bond by an electrophilic metal-oxo intermediate to generate a substrate-based radical. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. The active site structure of AlkB is not known, however, spectroscopic and genetic evidence points to a nitrogen-rich coordination environment located in the cytoplasm with as many as eight histidines coordinating the two iron ions and a carboxylate residue bridging the two metals. Like all other members of this superfamily, there are eight conserved histidines seen in the histidine cluster motifs: HXXXH, HXXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase. Also included in this CD are terminal alkane hydroxylases (AlkM), xylene monooxygenase hydroxylases (XylM), p-cymene monooxygenase hydroxylases (CymAa), and other related proteins
AWAWLGLLFITVLIPLLDALLGLDLSNPPEEPPLEKDRYYRWLLYLLLPLQFALLFLGVWAVSTGDLSAL
EKVGLILSLGLLSGVIGINTAHELIHRRSRLERWLGKLLLASLLYGHFAIEHVRGHHRYVATPEDPATAR
RGESFYRFLPRALVGSFRSAWKLEKKRLRRKGRSPWSPRNEVLRYLALAVALLALAAALGGLAGLLFLLI
QAFYAKSLLELVNYIEHYGLLRKKLANGRYEPVGPRHSWNSNHIVSNLLLFNLQRHSDHHAHPTRPYQAL
RPFPEAPQLPSGYPVMALLALIPPLWRRVMDPRV
>gnl|CDD|239590 cd03513, CrtW_beta-carotene-ketolase, Beta-carotene ketolase/oxygenase (CrtW, also known as CrtO), the carotenoid astaxanthin biosynthetic enzyme, initially catalyzes the addition of two keto groups to carbons C4 and C4' of beta-carotene. Carotenoids are important natural pigments produced by many microorganisms and plants. Astaxanthin is reported to be an antioxidant, an anti-cancer agent, and an immune system stimulant. A number of bacteria and green algae can convert beta-carotene into astaxanthin by using several ketocarotenoids as intermediates and CrtW and a beta-carotene hydroxylase (CrtZ). CrtW initially converts beta-carotene to canthaxanthin via echinenone, and CrtZ initially mediates the conversion of beta-carotene to zeaxanthin via beta-cryptoxanthin. After a few more intermediates are formed, CrtW and CrtZ act in combination to produce astaxanthin. Sequences of this domain family appear to be structurally related to membrane fatty acid desaturases and alkane hydroxylases. They all share in common extensive hydrophobic regions that are capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase
GLTLAGLIIAAWLASHVHALFFPRGSISLLLIAAVVLLQTFLHTGLFIIAHDAMHGSLAPGNPRLNRAIG
RLCLFLYAGFSYDRLLRKHHLHHRHPGTAKDPDFHKGNPSGFLPWYLHFMSNYFGWRQLAILAAVWLLLL
GLGSAPLANLLLFWALPLILSSLQLFYFGTWLPHRPGRGGFADRHRARSSRLSPVLSFLTCYHFGYHHEH
HLSPSTPWWRLPELR
>gnl|CDD|239591 cd03514, CrtR_beta-carotene-hydroxylase, Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the addition of hydroxyl groups to the beta-ionone rings of beta-carotene to form zeaxanthin and is found in bacteria and red algae. Carotenoids are important natural pigments; zeaxanthin and lutein are the only dietary carotenoids that accumulate in the macular region of the retina and lens. It is proposed that these carotenoids protect ocular tissues against photooxidative damage. CrtR does not show overall amino acid sequence similarity to the beta-carotene hydroxylases similar to CrtZ, an astaxanthin biosynthetic beta-carotene hydroxylase. However, CrtR does show sequence similarity to the green alga, Haematococcus pluvialis, beta-carotene ketolase (CrtW), which converts beta-carotene to canthaxanthin. Sequences of the CrtR_beta-carotene-hydroxylase domain family, as well as, the CrtW_beta-carotene-ketolase domain family appear to be structurally related to membrane fatty acid desaturases and alkane hydroxylases. They all share in common extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase
LLFLISMALVWLSTWGYVISYLPLWVCFILNTLSLHLAGTVIHDASHKAASRNRWINELIGHVSAFFLGF
PFPVFRRVHMQHHAHTNDPEKDPDHFLLEWLVARSLFITLLVIAILFGFLWELLNLWFLPALIVGTYLAL
FFDWLPHHPFEETQRWDNSRVYPSKLLNPLIMGQNYHLVHHLWPSIPWYRYPEAYYANKPLLDARGC
>gnl|CDD|239592 cd03515, Link_domain_TSG_6_like, This is the extracellular link domain of the type found in human TSG-6. The link domain is a hyaluronan (HA)-binding domain. TSG-6 is the protein product of tumor necrosis factor-stimulated gene-6. TSG-6 is up-regulated in inflammatory lesions and in the ovary during ovulation. It has a strong anti-inflammatory and chondroprotective effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. Also included in this group are the stabilins: stabilin-1 (FEEL-1, CLEVER-1) and stabilin-2 (FEEL-2). Stabilin-2 functions as the major liver and lymph node-scavenging receptor for HA and related glycosaminoglycans. Stabilin-2 is a scavenger receptor with a broad range of ligands including advanced glycation end (AGE) products, acetylated low density lipoprotein and procollagen peptides. In contrast, stabilin-1 does not bind HA, but binds acetylated low density lipoprotein and AGEs with lower affinity. As AGEs accumulate in vascular tissues during aging and diabetes, these receptors may be implicated in the pathologies of these states. Both stabilins are present in the early endocytic pathway in hepatic sinusoidal epithelium associating with clathrin/AP-2. Stabilin-1 is expressed in macrophages. Stabilin-2 is absent from the latter. In macrophages: stabilin-1 is involved in trafficking between early/sorting endosomes and the trans-Golgi network. Stabilin-1 has also been implicated in angiogenesis and possibly leucocyte trafficking. Both stabilins bind gram-positive and gram-negative bacteria. TSG-6 and stabilins contain a single link module which supports high affinity binding to HA
GVFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGF
GHVGIVDYGPRLNLSERWDAYCY
>gnl|CDD|239593 cd03516, Link_domain_CD44_like, This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It also plays an important role in arteriogenesis. The functional HA-binding domain of CD44 is an extended domain comprised of a single link module flanked with N-and C- extensions. These extensions are essential for folding and for functional activity. This group also contains the cell surface retention sequence (CRS) binding protein-1 (CRSBP-1) and lymph vessel endothelial receptor-1 (LYVE-1). CRSBP-1 is a cell surface binding protein for the CRS motif of PDGF-BB (platelet-derived growth factor-BB) and is responsible for the cell surface retention of PDGF-BB in SSV-transformed cells. CRSBP-1 may play a role in autocrine regulation of cell growth mediated by CRS containing growth regulators. LYVE-1 is preferentially expressed on the lymphatic endothelium and is used as a molecular marker for the detection and characterization of lymphatic vessels in tumors
ITCRIMGVFLVEKNGRYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPN
PLCGKNGTGVYILNSNLSSRYDAYCYNSSDTWINSCLPEILTTDDPIFITQTATDGTRYNVSGSTHSSPS
STYP
>gnl|CDD|239594 cd03517, Link_domain_CSPGs_modules_1_3, Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan. In addition, it is found in the first link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. In addition, aggrecan contains a second globular domain (G2) which contains link modules 3 and 4. G2 appears to lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes
VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYG
DMDGFPGVRNYGVRDPDELYDVYCY
>gnl|CDD|239595 cd03518, Link_domain_HAPLN_module_1, Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes
VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGG
KRTVPGLRSYGERDKMLSRYDAFCF
>gnl|CDD|239596 cd03519, Link_domain_HAPLN_module_2, Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes
GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKFHGLDRCDAGWLADGSVRYPISRPRPRCGPLE
PGVRSFGFPDKKHKLYGVYCY
>gnl|CDD|239597 cd03520, Link_domain_CSPGs_modules_2_4, Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes
EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLP
GVRTLYRFPNQTGFPDPHSRFDAYCF
>gnl|CDD|239598 cd03521, Link_domain_KIAA0527_like, Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, it is highly similar to the link domain. The link domain is a hyaluronan-binding (HA) domain. KIAA0527 contains a single link module. The KIAA0527 gene was originally cloned from human brain tissue
KLFVLELENGSQGLGLRAARQSCASLGARLASAAELRRAVVECFFSACARGWLADGTVGTTVCNPVVAEA
LKAVDVKVEIETNPIPFAHYNALCI
>gnl|CDD|239599 cd03522, MoeA_like, MoeA_like. This domain is similar to a domain found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. There this domain is presumed to bind molybdopterin. The exact function of this subgroup is unknown
GAILAHDITRIGPGEFKGRAFKKGHVLTAEDIAALLAAGKEHVYVARLEPGDVHEDEAAARLAAALAGDG
LRLSEPAEGRVNLFAERAGLLKVDVEALDALNAIDAITLATLHNNTPVEAGQMVATVKIIPLAVPEALVE
RAEALARDGPLLRVAPFRPLRVGLIVTGSEVYGGRIEDKFGPVLRARLAALGVELVEQVIVPHDEAAIAA
AIAEALEAGAELLILTGGASVDPDDVTPAAIRAAGGEVIRYGMPVDPGNLLLLGYLGGVPVIGLPGCARS
PKLNGFDLVLPRLLAGERVTRADIAAMGVGGL
>gnl|CDD|239600 cd03523, NTR_like, NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in netrins, complement proteins, tissue inhibitors of metalloproteases (TIMP), and procollagen C-proteinase enhancers (PCOLCE), amongst others. In netrins, the domain plays a role in controlling axon branching in neural development, while the common function of these modules in TIMPs appears to be binding to metzincins. A subset of this family is also known as the C345C domain because it occurs as a C-terminal domain in complement C3, C4 and C5. In C5, the domain interacts with various partners during the formation of the membrane attack complex
KAFCKSDYVVRAKIKEIKEENDDVKYEVKIIKIYKTGKAKADKADLRFYYTAPACCPCHPILNPGREYLI
MGKEEDSQGGLVLDPLSFVEPWSPLSLRQDRRLRE
>gnl|CDD|239601 cd03524, RPA2_OBF_family, RPA2_OBF_family: A family of oligonucleotide binding (OB) folds with similarity to the OB fold of the single strand (ss) DNA-binding domain (DBD)-D of human RPA2 (also called RPA32). RPA2 is a subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). RPA contains six OB folds, which are involved in ssDNA binding and in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. This family also includes OB folds similar to those found in Escherichia coli SSB, the wedge domain of E. coli RecG (a branched-DNA-specific helicase), E. coli ssDNA specific exodeoxyribonuclease VII large subunit, Pyrococcus abyssi DNA polymerase II (Pol II) small subunit, Sulfolobus solfataricus SSB, and Bacillus subtilis YhaM (a 3'-to-5'exoribonuclease). It also includes the OB folds of breast cancer susceptibility gene 2 protein (BRCA2), Oxytricha nova telomere end binding protein (TEBP), Saccharomyces cerevisiae telomere-binding protein (Cdc13), and human protection of telomeres 1 protein (POT1)
TIVGIVVAVEEIRTEGKVLIFTLTDGTGGTIRVTLFGELAEELENLLKEGQVVYIKGKVKKFRGRLQLIV
ESIEL
>gnl|CDD|239602 cd03526, SQR_QFR_TypeB_TM, Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) Type B subfamily, transmembrane subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol, while QFR catalyzes the reverse reaction. SQR, also called succinate dehydrogenase or Complex II, is part of the citric acid cycle and the aerobic respiratory chain, while QFR is involved in anaerobic respiration with fumarate as the terminal electron acceptor. SQR and QFR share a common subunit arrangement, composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Type B proteins contain one transmembrane subunit and two heme groups. The heme and quinone binding sites reside in the transmembrane subunits. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit containing the electron donor/acceptor (quinol or quinone). The reversible reduction of quinone is an essential feature of respiration, allowing the transfer of electrons between respiratory complexes
LDWLQSATGLFLGLFMIGHLFFNSTILLGDNVMNWVAKKFELLPIVVSFLAAFIFAVFIAHAFLGVRKFP
IYRQALTFKTHKDLMHGDTTLWWIQAMTGFAMLFFGSVHLYIMMTQAQPDRTIGFVMSSNRMSSEWMWPL
YIVLLFAVELHGSVGLYSFAVTWGWFDGETPDKSRANLKKLKTLMSAFLSVLGLLTFGA
>gnl|CDD|239603 cd03527, RuBisCO_small, Ribulose bisphosphate carboxylase/oxygenase (Rubisco), small subunit. Rubisco is a bifunctional enzyme catalyzes the initial steps of two opposing metabolic pathways: photosynthetic carbon fixation and the competing process of photorespiration. Rubisco Form I, present in plants and green algae, is composed of eight large and eight small subunits. The nearly identical small subunits are encoded by a family of nuclear genes. After translation, the small subunits are translocated across the chloroplast membrane, where an N-terminal signal peptide is cleaved off. While the large subunits contain the catalytic activities, it has been shown that the small subunits are important for catalysis by enhancing the catalytic rate through inducing conformational changes in the large subunits
RTFETFSYLPPLTDEQIAKQIDYIISNGWAPCLEFTEPEHYDNRYWTMWKLPMFGCTDPAQVLREIEACR
KAYPDHYVRVVGFDNYKQSQCMSFIVHRP
>gnl|CDD|239604 cd03528, Rieske_RO_ferredoxin, Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the Rieske ferredoxin component of some three-component RO systems including biphenyl dioxygenase (BPDO) and carbazole 1,9a-dioxygenase (CARDO). The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The ferredoxin component contains either a plant-type or Rieske-type [2Fe-2S] cluster. The Rieske ferredoxin component in this family carries an electron from the RO reductase component to the terminal RO oxygenase component. BPDO degrades biphenyls and polychlorinated biphenyls. BPDO ferredoxin (BphF) has structural features consistent with a minimal and perhaps archetypical Rieske protein in that the insertions that give other Rieske proteins unique structural features are missing. CARDO catalyzes dihydroxylation at the C1 and C9a positions of carbazole. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes
WVRVCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLR
TGKALSLPATEPLKTYPVKVEDGDVYVD
>gnl|CDD|239605 cd03529, Rieske_NirD, Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium. Members include bacterial and fungal proteins. The bacterial NirD contains a single Rieske domain while fungal proteins have a C-terminal Rieske domain in addition to several other domains. The fungal NirD is involved in nutrient acquisition, functioning at the soil/fungus interface to control nutrient exchange between the fungus and the host plant. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. The Rieske [2Fe-2S] cluster is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In this family, only a few members contain these residues. Other members may have lost the ability to bind the Rieske [2Fe-2S] cluster
WQTVCALDDLPPGSGVAALVGDTQIAIFRLPGREVYAVQNMDPHSRANVLSRGIVGDIGGEPVVASPLYK
QHFSLKTGRCLEDEDVSVATFPVRVEDGEVYVK
>gnl|CDD|239606 cd03530, Rieske_NirD_small_Bacillus, Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar to the Bacillus subtilis small subunit of assimilatory nitrite reductase containing a Rieske domain. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium
WIDIGALEDIPPRGARKVQTGGGEIAVFRTADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDL
ETGEAQGPDEGCVRTFPVKVEDGRVYLG
>gnl|CDD|239607 cd03531, Rieske_RO_Alpha_KSH, The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase component of 3-ketosteroid 9-alpha-hydroxylase (KSH). The terminal oxygenase component of KSH is a key enzyme in the microbial steroid degradation pathway, catalyzing the 9 alpha-hydroxylation of 4-androstene-3,17-dione (AD) and 1,4-androstadiene-3,17-dione (ADD). KSH is a two-component class IA monooxygenase, with terminal oxygenase (KshA) and oxygenase reductase (KshB) components. KSH activity has been found in many actino- and proteo- bacterial genera including Rhodococcus, Nocardia, Arthrobacter, Mycobacterium, and Burkholderia
GWHCLGLARDFRDGKPHGVEAFGTKLVVFADSDGALNVLDAYCRHMGGDLSQGTVKGDEIACPFHDWRWG
GDGRCKAIPYARRVPPLARTRAWPTLERNGQLFVWHDPEGNPPPP
>gnl|CDD|239608 cd03532, Rieske_RO_Alpha_VanA_DdmC, Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and dicamba O-demethylase oxygenase (DdmC) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Vanillate-O-demethylase is a heterodimeric enzyme consisting of a terminal oxygenase (VanA) and reductase (VanB) components. This enzyme reductively catalyzes the conversion of vanillate into protocatechuate and formaldehyde. Protocatechuate and vanillate are important intermediate metabolites in the degradation pathway of lignin-derived compounds such as ferulic acid and vanillin by soil microbes. DDmC is the oxygenase component of a three-component dicamba O-demethylase found in Pseudomonas maltophila, that catalyzes the conversion of a widely used herbicide called herbicide dicamba (2-methoxy-3,6-dichlorobenzoic acid) to DCSA (3,6-dichlorosalicylic acid)
FPRNAWYVAAWADELGDKPLARTLLGEPVVLYRTQDGRVAALEDRCPHRSAPLSKGSVEGGGLVCGYHGL
EFDSDGRCVHMPGQERVPAKACVRSYPVVERDALIWIWMGDAALAD
>gnl|CDD|239609 cd03535, Rieske_RO_Alpha_NDO, Rieske non-heme iron oxygenase (RO) family, Nathphalene 1,2-dioxygenase (NDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. NDO is a three-component RO system consisting of a reductase, a ferredoxin, and a hetero-hexameric alpha-beta subunit oxygenase component. NDO catalyzes the oxidation of naphthalene to cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene (naphthalene cis-dihydrodiol) with the consumption of O2 and NAD(P)H. NDO has a relaxed substrate specificity and can oxidize almost 100 substrates. Included in its varied activities are the enantiospecific cis-dihydroxylation of polycyclic aromatic hydrocarbons and benzocycloalkenes, benzylic hydroxylation, N- and O-dealkylation, sulfoxidation and desaturation reactions
RAWVFLGHESEIPNAGDYVVRYIGDDSFIVCRDEDGEIRAMFNSCRHRGMQVCRAEMGNTSHFRCPYHGW
TYRNTGRLVGVPAQQEAYGGGFDKSQWGLRPAPNLDSYNGLIFGSLDPKAPSL
>gnl|CDD|239610 cd03536, Rieske_RO_Alpha_DTDO, This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit (DitA) of diterpenoid dioxygenase (DTDO). DTDO is a novel aromatic-ring-hydroxylating dioxygenase found in Pseudomonas and other proteobacteria that degrades dehydroabietic acid (DhA). Specifically, DitA hydroxylates 7-oxodehydroabietic acid to 7-oxo-11,12-dihydroxy-8, 13-abietadien acid. The ditA1 and ditA2 genes encode the alpha and beta subunits of the oxygenase component of DTDO while the ditA3 gene encodes the ferredoxin component of DTDO. The organization of the genes encoding the various diterpenoid dioxygenase components, the phylogenetic distinctiveness of both the alpha subunit and the ferredoxin component, and the unusual iron-sulfur cluster of the ferredoxin all suggest that this enzyme belongs to a new class of aromatic ring-hydroxylating dioxygenases
WVLLGHESEIPNKGDFMVRDMGSDSVIVARDKDGEIHVSLNVCPHRGMRISTTDGGNTQIHVCIYHGWAF
RPNGDFIGAPVEKECMHGKMRTKAELGLHKARVTLYGGLIFATWNIDGPSFED
>gnl|CDD|239611 cd03537, Rieske_RO_Alpha_PrnD, This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of aminopyrrolnitrin oxygenase (PrnD). PrnD is a novel Rieske N-oxygenase that catalyzes the final step in the pyrrolnitrin biosynthetic pathway, the oxidation of the amino group in aminopyrrolnitrin to a nitro group, forming the antibiotic pyrrolnitrin. The biosynthesis of pyrrolnitrin is one of the best examples of enzyme-catalyzed arylamine oxidation. Although arylamine oxygenases are widely distributed within the microbial world and used in a variety of metabolic reactions, PrnD represents one of only two known examples of arylamine oxygenases or N-oxygenases involved in arylnitro group formation, the other being AurF involved in aureothin biosynthesis
AASWYVAMRSDDLKDKPTELTLFGRPCVAWRGATGRAVVMDRHCSHLGANLADGRVKDGCIQCPFHHWRY
DEQGQCVHIPGHSTAVRRLEPVPRGARQPTLVTAERYGYVWVWYGSPQPLHPL
>gnl|CDD|239612 cd03538, Rieske_RO_Alpha_AntDO, Rieske non-heme iron oxygenase (RO) family, Anthranilate 1,2-dioxygenase (AntDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. AntDO converts anthranilate to catechol, a naturally occurring compound formed through tryptophan degradation and an important intermediate in the metabolism of many N-heterocyclic compounds such as indole, o-nitrobenzoate, carbazole, and quinaldine
HKDVYTDPEIFALEMERLFGNAWIYVGHESQVPNPGDYITTRIGDQPVVMVRHTDGSVHVLYNRCPHKGT
KIVSDGCGNTGKFFRCPYHAWSFKTDGSLLAIPLKKGYEGTGFDPSHADKGMQRVGAVDIYRGFVFARLS
PSGPDF
>gnl|CDD|239613 cd03539, Rieske_RO_Alpha_S5H, This alignment model represents the N-terminal rieske iron-sulfur domain of the oxygenase alpha subunit (NagG) of salicylate 5-hydroxylase (S5H). S5H converts salicylate (2-hydroxybenzoate), a metabolic intermediate of phenanthrene, to gentisate (2,5-dihydroxybenzoate) as part of an alternate pathway for naphthalene catabolism. S5H is a multicomponent enzyme made up of NagGH (the oxygenase components), NagAa (the ferredoxin reductase component), and NagAb (the ferredoxin component). The oxygenase component is made up of alpha (NagG) and beta (NagH) subunits
WCYVGLEAEIPNPGDFKRTLIGERSVIMTRDPDGGINVVENVCAHRGMRFCRERNGNAKDFVCPYHQWNY
SLKGDLQGVPFRRGVKKDGKVNGGMPKDFKTKDHGLTKLKVATRGGVVFASFDHDVESF
>gnl|CDD|239614 cd03541, Rieske_RO_Alpha_CMO, Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. CMO is a novel RO found in certain plants which catalyzes the first step in betaine synthesis. CMO is not found in animals or bacteria. In these organisms, the first step in betaine synthesis is catalyzed by either the membrane-bound choline dehydrogenase (CDH) or the soluble choline oxidase (COX)
GWQVAGYSDQVKEKNQYFTGRLGNVEYVVCRDGNGKLHAFHNVCTHRASILACGSGKKSCFVCPYHGWVY
GLDGSLTKATQATGIQNFNPKELGLVPLKVAEWGPFVLISVDRSLSEK
>gnl|CDD|239615 cd03542, Rieske_RO_Alpha_HBDO, Rieske non-heme iron oxygenase (RO) family, 2-Halobenzoate 1,2-dioxygenase (HBDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. HBDO catalyzes the double hydroxylation of 2-halobenzoates with concomitant release of halogenide and carbon dioxide, yielding catechol
WVYLAHESQIPNNNDYFTTTIGRQPVVITRDKDGELNAFINACSHRGAMLCRRKQGNKGTFTCPFHGWTF
SNTGKLLKVKDPKTAGYPEGFNCDGSHDLTKVARFESYRGFLFGSLNADVAPL
>gnl|CDD|239616 cd03545, Rieske_RO_Alpha_OHBDO_like, Rieske non-heme iron oxygenase (RO) family, Ortho-halobenzoate-1,2-dioxygenase (OHBDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of OHBDO, salicylate 5-hydroxylase (S5H), terephthalate 1,2-dioxygenase system (TERDOS) and similar proteins. ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. OHBDO converts 2-chlorobenzoate (2-CBA) to catechol as well as 2,4-dCBA and 2,5-dCBA to 4-chlorocatechol, as part of the chlorobenzoate degradation pathway. Although ortho-substituted chlorobenzoates appear to be particularly recalcitrant to biodegradation, several strains utilize 2-CBA and the dCBA derivatives as a sole carbon and energy source. S5H converts salicylate (2-hydroxybenzoate), a metabolic intermediate of phenanthrene, to gentisate (2,5-dihydroxybenzoate) as part of an alternate pathway for naphthalene catabolism. S5H is a multicomponent enzyme made up of NagGH (the oxygenase components), NagAa (the ferredoxin reductase component), and NagAb (the ferredoxin component). The oxygenase component is made up of alpha (NagG) and beta (NagH) subunits. TERDOS is present in gram-positive bacteria and proteobacteria where it converts terephthalate (1,4-dicarboxybenzene) to protocatechuate as part of the terephthalate degradation pathway. The oxygenase component of TERDOS, called TerZ, is a hetero-hexamer with 3 alpha (TerZalpha) and 3 beta (TerZbeta) subunits
RVPYKVFTDRAYFDREQERIFRGKTWSYVGLEAEIPNAGDFKSTFVGDTPVVVTRAEDGSLHAWVNRCAH
RGALVCRERRGNDGSLTCVYHQWAYDLKGNLKGVPFRRGLKGQGGMPKDFDMKQHGLEKLRVETVGGLVF
ASFSDEVEPL
>gnl|CDD|239617 cd03548, Rieske_RO_Alpha_OMO_CARDO, Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole 1,9a-dioxygenase (CARDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. OMO catalyzes the NADH-dependent oxidation of the N-heterocyclic aromatic compound 2-oxoquinoline to 8-hydroxy-2-oxoquinoline, the second step in the bacterial degradation of quinoline. OMO consists of a reductase component (OMR) and an oxygenase component (OMO) that together function to shuttle electrons from the reduced pyridine nucleotide to the active site of OMO, where O2 activation and 2-oxoquinoline hydroxylation occurs. CARDO, which contains oxygenase (CARDO-O), ferredoxin (CARDO-F) and ferredoxin reductase (CARDO-R) components, catalyzes the dihydroxylation at the C1 and C9a positions of carbazole. The oxygenase component of OMO and CARDO contain only alpha subunits arranged in a trimeric structure
YQPYIDAKWGFRNHWYPALFSHELEEGEPKGIQLCGEPILLRRVDGKVYALKDRCLHRGVPLSKKPECFT
KGTITCWYHGWTYRLDDGKLVTILANPDDPLIGRTGLKTYPVEEAKGMIFVFVGDGDYADPPPLAH
>gnl|CDD|239618 cd03556, L-fucose_isomerase, L-fucose isomerase (FucIase); FucIase converts L-fucose, an aldohexose, to its ketose form, which prepares it for aldol cleavage (similar to the isomerization of glucose during glycolysis). L-fucose (or 6-deoxy-L-galactose) is found in blood group determinants as well as in various oligo- and polysaccharides, and glycosides in mammals, bacteria and plants
PKIGIRPTIDGRRGGVRESLEEQTMNMAKAAAKLIEENLKYADGEPVECVIADTTIGRVAEAAACAEKFT
RENVGATITVTPCWCYGSETMDMDPNTPKAIWGFNGTERPGAVYLAAVLAGHAQKGIPAFGIYGHDVQEA
DDTTIPEDVKEKILRFARAAIAVASMRGKSYLSIGSVSMGIAGSIVDPNFFEEYLGMRVESVDMTEIIRR
MDEEIYDPEEYEKALAWTKENCKEGEDENEKNDQKKREQKDKDWEFVVKMAIIIRDLMYGNEKLADLGFE
EEALGHNAIAAGFQGQRQWTDFYPNGDFPEAILNTSFDWNGIREPFVFATENDSLNGVSMLFGHLLTNKA
QIFADVRTYWSPEAVKRVTGKELTGLAKNGIIHLINSGAAALDGTGQAKDKDGNPTMKEFWNLTEEDVQA
CLAATDWCPANREYFRGGGFSSRFLTEGEMPVTMIRLNLIKGLGPVLQIAEGYTVELPEDVHDILDKRTD
PTWPTTWFAPRLTGKGAFKDVYDVMNNWGANHGAITHGHIGADLITLASMLRIPVCMHNVPEEKIFRPNA
WNAFGMDLEGADYRACQLYGPLYK
>gnl|CDD|239619 cd03557, L-arabinose_isomerase, L-Arabinose isomerase (AI) catalyzes the isomerization of L-arabinose to L-ribulose, the first reaction in its conversion into D-xylulose-5-phosphate, an intermediate in the pentose phosphate pathway, which allows L-arabinose to be used as a carbon source. AI can also convert D-galactose to D-tagatose at elevated temperatures in the presence of divalent metal ions. D-tagatose, rarely found in nature, is of commercial interest as a low-calorie sugar substitute
YEVWFVTGSQHLYGEEALKQVAAHSREIVDGLNASGKLPVKIVFKPVLTTPDEILAVCREANADDNCAGV
ITWMHTFSPAKMWIAGLTALQKPLLHLHTQFNREIPWDTIDMDFMNLNQSAHGDREFGFIGSRMRIPRKV
VVGHWQDPEVHEKIGDWMRAAAGWADSRHLKVARFGDNMRNVAVTEGDKVEAQIQFGWSVNGYGVGDLVA
RVDAVSDSDVDALVDEYEALYDLAPELKDGGERRASLREAARIELGLRRFLEDGGFTAFTTTFEDLHGLK
QLPGLAVQRLMAEGYGFGAEGDWKTAALVRAMKVMSAGLPGGTSFMEDYTYHFEPGNELVLGAHMLEVCP
SIAAAKPRLEVHPLGIGGKEDPARLVFTGKAGPAVNASLVDMGNRFRLVVNEVDAVEPPEDLPNLPVARA
LWKPEPDLKTAAEAWILAGGAHHTVFSTAVTAEQLEDFAEMAGIELVVIDEDTNLRQFKKELRW
>gnl|CDD|349787 cd03558, LGIC_ECD, extracellular domain (ECD) of Cys-loop neurotransmitter-gated ion channels (also known as ligand-gated ion channel (LGIC)). This superfamily contains the extracellular domain (ECD) of Cys-loop neurotransmitter-gated ion channels, which include nicotinic acetylcholine receptor (nAChR), serotonin 5-hydroxytryptamine receptor (5-HT3), type-A gamma-aminobutyric acid receptor (GABAAR) and glycine receptor (GlyR). These ligand-gated ion channels (LGICs) are found across metazoans and have close homologs in bacteria. They are vital for communication throughout the nervous system. GABAAR and GlyR are anionic channels, both mediating fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR receptor pore, resulting in hyperpolarization of the neuron. nAChR is a non-selective cation channel that is permeable to Na+ and K+, and some subunit combinations are also permeable to Ca2+. Na+ enters and K+ exits to allow net flow of positively charged ions inward. 5-HT3, a cation-selective channel, binds serotonin and is permeable to Na+, K+, and Ca2+. It mediates neuronal depolarization and excitation within the central and peripheral nervous systems. These ligand-gated chloride channels are critical not only for maintaining appropriate neuronal activity, but have long been important therapeutic targets: benzodiazepines, barbiturates, some intravenous and volatile anaesthetics, alcohol, strychnine, picrotoxin, and ivermectin all derive their biological activity from acting on the inhibitory half of the Cys-loop receptor family. The ECD contains the ligand binding sites for these receptors
VTVTVNISLAQLISVDEVNMDYTTNVFLRQSWIDKRLAYSPADYGGVDSLRLPSEQIWLPDLVFYNNKDA
DFVTTDNVLIRLSPDGTVLYSPRAILKSACPMDLKRFPFDQQNCTMKLESWTYDTTDIELVWDSERPDQA
DFLELPEWDIVEKRGRYCTVVYNTGIYSDITYRFRLKRQ
>gnl|CDD|349850 cd03559, LGIC_TM, transmembrane domain of Cys-loop neurotransmitter-gated ion channels. This superfamily contains the transmembrane domain of Cys-loop neurotransmitter-gated ion channels, which include nicotinic acetylcholine receptor (nAChR), serotonin 5-hydroxytryptamine receptor (5-HT3), type-A gamma-aminobutyric acid receptor (GABAAR), and glycine receptor (GlyR). These ligand-gated ion channels (LGICs) are found across metazoans and have close homologs in bacteria. They are vital for communication throughout the nervous system where the sign of synaptic connections (excitatory or inhibitory) is determined by the charge of the ions that flow through these channels. In general, channels that conduct positive ions are excitatory, whereas channels that conduct negative ions are inhibitory. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. GABAAR and GlyR are anionic channels, both mediating fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR receptor pore, resulting in hyperpolarization of the neuron. nAChR is a non-selective cation channel that is permeable to Na+ and K+, and some subunit combinations are also permeable to Ca2+. Na+ enters and K+ exits to allow net flow of positively charged ions inward. 5-HT3, a cation-selective channel, binds serotonin and is permeable to Na+, K+, and Ca2+. It mediates neuronal depolarization and excitation within the central and peripheral nervous systems. These ligand-gated chloride channels are critical not only for maintaining appropriate neuronal activity, but have long been important therapeutic targets: benzodiazepines, barbiturates, some intravenous and volatile anaesthetics, alcohol, strychnine, picrotoxin, and ivermectin all derive their biological activity from acting on the inhibitory half of the Cys-loop receptor family
YYAVSLLLPSILIMVVSWVGFWLPPDSGERVSFKITLLLTYSVFLIIVSDTLPATPYTPLIDVYFVVCMA
LLFIALLETIFIVRLVHKQDRVGYVIDRLLRRIFPLAFLAYSIVLV
>gnl|CDD|340765 cd03561, VHS, VHS (Vps27/Hrs/STAM) domain family. The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It has a superhelical structure similar to that of the ARM (Armadillo) repeats and is present at the N-termini of proteins involved in intracellular membrane trafficking. There are four general groups of VHS domain containing proteins based on their association with other domains. The first group consists of proteins of the STAM/EAST/Hbp family, which has the domain composition of VHS-SH3-ITAM. The second consists of proteins with a FYVE domain C-terminal to VHS. The third consists of GGA proteins with a domain composition of VHS-GAT (GGA and TOM)-GAE (Gamma-Adaptin Ear) domain. The fourth consists of proteins with a VHS domain alone or with domains other than those mentioned above. In GGA proteins, VHS domains are involved in cargo recognition in trans-Golgi, thereby having a general membrane targeting/cargo recognition role in vesicular trafficking
VEELVEKATSESLTEPDWALNLEICDLVNSDPAQAKDAVRALRKRLQSKNPKVQLLALTLLETLVKNCGA
PFHSEVASRDFLQELVKLVKKKKTSPEVREKALALIQEWAEAFQGDGRLPLFYDTYQQLRR
>gnl|CDD|340766 cd03562, CID, CID (CTD-Interacting Domain) family. The CTD-Interacting Domain (CID) is present in several eukaryotic RNA-processing factors including yeast proteins, Pcf11 and Nrd1, and vertebrate proteins, CTD-associated factors 8 (SCAF8) and Regulation of nuclear pre-mRNA domain-containing proteins (such as RPRD1 and RPRD2). Pcf11 is a conserved and essential subunit of the yeast cleavage factor IA, which is required for polyadenylation-dependent 3'-RNA processing and transcription termination. Nrd1 is implicated in polyadenylation-independent 3'-RNA processing. CID binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase (Pol) II (RNAP II). During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices
KAFNSKLEELSDLSQQSITTLTKWAIHHIKHSRPIVTVIEREIRKCKPNRKLTFLYLIDSIIRNSKRKGP
EFTKDFSPVIVELFKHVYSETDEDCKKKLGRVLSIWEERNVFENSVLEQLKQA
>gnl|CDD|340767 cd03564, ANTH_N, ANTH (AP180 N-Terminal Homology) domain family, N-terminal region. The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains
LDVAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHALAKRLHKKNWIVVLKTLIVIHRLLREG
SPSFLEELLRYSGHIFNLSNFKDDSSPEAWDLSAFIRRYARYLEERLECF
>gnl|CDD|340768 cd03565, VHS_Tom1_like, VHS (Vps27/Hrs/STAM) domain of Tom1 subfamily. This subfamily is composed of Tom1 (Target of myb1 - retroviral oncogene) protein, Tom1L1 (Tom1-like1), Tom1L2 (Tom1-like2), and similar proteins. Proteins belonging to this subfamily are characterized by the presence of a VHS (Vps27p/Hrs/Stam) domain in the N-terminal portion followed by a GAT (GGA and Tom) domain. They are novel regulators for post-Golgi trafficking and signaling. Yeast do not contain homologous proteins of the Tom1 subfamily, suggesting these proteins have evolved to accommodate more complex cellular processes. Tom1 is essential for the negative regulation of Interleukin-1 and Tumor Necrosis Factor-induced signaling pathways. The VHS domain has a superhelical structure similar to the structure of the ARM repeats and is present at the very N-termini of proteins. It is a right-handed superhelix of eight alpha helices. The VHS domain has been found in a number of proteins, some of which have been implicated in intracellular trafficking and sorting
PVGQLIERATDSGLSSEDWALNMEICDMINETDDGPKDAIKAIKKRLSTNAGKNHTVVMYTLTLLETCVK
NCGHRFHVLVANKDFLQELVKLIGPKNDPPTIVQEKVLSLIQSWADAFRGQPDLQEVVKVYQELKAKG
>gnl|CDD|340769 cd03567, VHS_GGA_metazoan, VHS (Vps27/Hrs/STAM) domain of metazoan GGA (Golgi-localized, Gamma-ear-containing, Arf-binding) proteins. GGA (Golgi-localized, Gamma-ear-containing, Arf-binding) comprises a subfamily of ubiquitously expressed, monomeric, motif-binding cargo/clathrin adaptor proteins involved in membrane trafficking between the Trans-Golgi Network (TGN) and endosomes. Jawed vertebrates contain as many as three GGA proteins: GGA1, GGA2, and GGA3. The VHS domain has a superhelical structure similar to the structure of the ARM (Armadillo) repeats and is present at the N-termini of proteins. GGA proteins have a multidomain structure consisting of an N-terminal VHS domain linked by a short proline-rich linker to a GAT (GGA and TOM) domain, which is followed by a long flexible linker to the C-terminal appendage, GAE (Gamma-Adaptin Ear) domain. The VHS domain of GGA proteins binds to the acidic-cluster dileucine (DxxLL) motif found on the cytoplasmic tails of cargo proteins trafficked between the Trans-Golgi Network and the endosomal system
SLEYLLNKATNPFNTEEDWEAIDAFCDRVNKEPEGPQIAVRLLAHKIQSPNEKEALRALTVLEACVKNCG
PRFHSEVGKFRFLNELIKLVSPKYLGNRTPEEVKQKIIELLYSWTRSLPHEPKIKEAYDMLKKQGIIKE
>gnl|CDD|340770 cd03568, VHS_STAM, VHS (Vps27/Hrs/STAM) domain of the STAM (Signal Transducing Adaptor Molecule) subfamily. STAM (Signal Transducing Adaptor Molecule) subfamily members have at their N-termini a VHS domain, which is involved in cytokine-mediated intracellular signal transduction and has a superhelical structure similar to the structure of ARM (Armadillo) repeats, followed by a Ubiquitin-Interacting Motif (UIM) and a SH3 (Src Homology 3) domain, which is a well-established protein-protein interaction domain, and a GAT (GGA and TOM) domain. At the C-termini of most vertebrate STAMs, an Immunoreceptor Tyrosine-based Activation Motif (ITAM) is present, which mediates the binding of HRS (hepatocyte growth factor-regulated tyrosine kinase substrate) in endocytic and exocytic machineries. STAM is a component of the ESCRT (Endosomal Sorting Complex Required for Transport)-0 machinery and together with Hrs, functions to bind and sequester cargoes for downstream sorting into intralumenal vesicles. Jawed vertebrates have two STAM subfamily members, STAM1 and STAM2
FDQDVEKATSEKNTSENWSLILDICDKVGRSPNGAKDCLKSIMKRLNHKDPHVALQALTLLDACVKNCGK
IFHLEVCSRDFESELRKLLTKSHPKVAEKLKELLKKWAEEEFKDDPQLSLIPSLYKKLKAEG
>gnl|CDD|340771 cd03569, VHS_Hrs, VHS (Vps27/Hrs/STAM) domain of Hepatocyte growth factor-regulated tyrosine kinase substrate, Hrs. Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) plays a role in at least three vesicle trafficking events: exocytosis, endocytosis, and endosome to lysosome trafficking. Hrs is involved in promoting rapid recycling of endocytosed signaling receptors to the plasma membrane. Together with STAM or STAM2, it comprises the ESCRT (Endosomal Sorting Complex Required for Transport)-0 machinery, which functions to bind and sequester cargoes for downstream sorting into intralumenal vesicles. Hrs contains an N-terminal VHS domain, which has a superhelical structure similar to the structure of ARM (Armadillo) repeats, a FYVE (Fab1p, YOTB, Vac1p, and EEA1) zinc finger domain, a Double Ubiquitin-Interacting Motif (DUIM), a P(S/T)XP motif that recruit ESCRT-I, a GAT (GGA and TOM) domain, and a short peptide motif near the C-terminus that recruits clathrin
SNFDKLLDKATSQLLLEPDWESILQICDLIRQGDVTPKYAVSAIKKKLNDQNPHVALYALQVLESVVKNC
GTPVHDEVATKEFMEELRDLVKTTTSENVRNKILELIQAWAHAFRNEPKYKIVQDTYNIMKMEGYKFP
>gnl|CDD|340772 cd03571, ENTH, Epsin N-Terminal Homology (ENTH) domain family. The Epsin N-Terminal Homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, contributing to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding
LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGS
ERVVDEFRDNLYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED
>gnl|CDD|340773 cd03572, ENTH_like_Tepsin, Epsin N-Terminal Homology (ENTH)-like domain of AP-4 complex accessory subunit Tepsin and similar domains. This family is composed of proteins containing an ENTH-like domain including vertebrate AP-4 complex accessory subunit Tepsin and Arabidopsis thaliana VHS domain-containing protein At3g16270. Tepsin is also called ENTH Domain-containing protein 2 (ENTHD2), Epsin for AP-4, or Tetra-epsin. It associates with the adapter-like complex 4 (AP-4), a heterotetramer composed of two large adaptins (epsilon and beta), a medium adaptin (mu) and a small adaptin (sigma), which forms a non-clathrin coat on vesicles departing the Trans-Golgi Network. The Epsin N-Terminal Homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding
DRPLLDKATSDDDEPTPGYLLEEIAKLTRSSPGSCQELLDYLLKRLKKSSPHVKLKALRIIKHLCQKGSP
EFRRELQRNSAAIRECTSYRGPPDPLHGDALYKAVREAAQELLEALFSD
>gnl|CDD|239629 cd03574, NTR_complement_C345C, NTR/C345C domain; The NTR domains that are found in the C-termini of complement C3, C4 and C5, are also called C345C domains. In C5, the domain interacts with various partners during the formation of the membrane attack complex, a fundamental process in the mammalian defense against infection. It's role in component C3 and C4 is not well understood
CPICKRELSDTCENLLDKACTSVDYVYKVKVTSVEEEAGFRIYKARVTEVIKSGSDDVQNGNARRTFIIR
ESCDCPLRLKEGRHYLIMGSDGAFYDDRNGEDRYQYVLDSNTWVEEWPTDSKCRNERQQAACDKLKKFEE
SMVLQGC
>gnl|CDD|239630 cd03575, NTR_WFIKKN, NTR domain, WFIKKN subfamily; WFIKKN proteins contain a C-terminal NTR domain and are putative secreted proteins which may be multivalent protease inhibitors that act on serine proteases as well as metalloproteases. Human WFIKKN and a related protein sharing the same domain architecture were observed to have distinct tissue expression patterns. WFIKKN is also referred to as growth and differentiation factor-associated serum protein-1 (GASP-1). It inhibits the activity of mature myostatin, a specific regulator of skeletal muscle mass and a member of the TGFbeta superfamily
VPSLCRSDFAIVGRLTELTEELDSGHARVTLEEVLKDEKMGLKFFGTEPLEVTLLNMDWSCPCPNITAGE
GPLIIMGDVHDGMAVLQPDSYVRASSERRVRKLREVLHK
>gnl|CDD|239631 cd03576, NTR_PCOLCE, NTR domain, PCOLCE subfamily; Procollagen C-endopeptidase enhancers (PCOLCEs) are extracellular matrix proteins that enhance the activity of procollagen C-proteases, by binding to the procollagen I C-peptide. They contain a C-terminal NTR domain, which have been suggested to possess inhibitory functions towards specific serine proteases but not towards metzincins, which are inhibited by the related TIMPs
PTAALCQQKCRRTGTLESNYCSSEFVITGTVISMTRGPGSLHATVSIIKLYKEGRLAITQAGKTMSVKIT
VVCKQCPLLRRGLNYILMGQVDEEGRGVIPPESFVMLYKTKHQKLLAALSNKKC
>gnl|CDD|239632 cd03577, NTR_TIMP_like, NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential regulators of extracellular matrix turnover and remodeling. They form complexes with matrix metalloproteases (MMPs) and inactivate them irreversibly by non-covalently binding their active zinc-binding sites. This group contains domains similar to the TIMP NTR domain, which binds MMPs. Members of this group may or may not function as MMP inhibitors
CSCMPQHPQEKYCQADFVIKVKVLKKKLDGAGLNIRYTIEIKKVYKGSEKSLLPITIYTPSDDSACGIPL
LEGKEYLIAGKVEDGALHTTLCDGVAPWDDLTKEQKRGLKGLYKKG
>gnl|CDD|239633 cd03578, NTR_netrin-4_like, NTR domain, Netrin-4-like subfamily; composed of the C-terminal NTR domains of netrin-4 (beta netrin) and similar proteins. Netrins are secreted proteins that function as tropic cues in the direction of axon growth and cell migration during neural development. Netrin-4 is a basement membrane component that is important in neural, kidney and vascular development. It may also be involved in regulating the outgrowth and shape of epithelial cells during lung branching morphogenesis
AKVFCGMKYAYVIKIKVLSAHDKGTHAEVNVKIKKVLKSTKLKLSRGKRTLYPESWTSRGCTCPILNPGL
EYLVAGHEDVRTGRLIVNMKSFVQHWKPSLGRKVMEILKRE
>gnl|CDD|239634 cd03579, NTR_netrin-1_like, NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called domain C in the context of C. elegans netrin UNC-6. Netrins are secreted proteins that function as tropic cues in the direction of axon growth and cell migration during neural development. These proteins may be chemoattractive to some neurons and chemorepellant for others. In the case of netrin-1, attraction and repulsion responses are mediated by the DCC and UNC-5 receptor families. The biological activities of C. elegans UNC-6, which may either attract or repel migrating cells or axons, are mediated by its different domains. The C-terminal NTR domain of UNC-6 has been shown to inhibit axon branching activity
LKKYCKKDYAVQAQVLSRETAGEWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVGKSYL
LLGKDEDSPERGGLILDKRSLVIEWRDEWARRLRRFQRRERRGKC
>gnl|CDD|239635 cd03580, NTR_Sfrp1_like, NTR domain, Secreted frizzled-related protein (Sfrp) 1-like subfamily; composed of proteins similar to human Sfrp1, Sfrp2 and Sfrp5. Sfrps are soluble proteins containing an NTR domain C-terminal to a cysteine-rich Frizzled domain. They show diverse functions and are thought to work in Wnt signaling indirectly, as modulators or antagonists by binding Wnt ligands, and directly, via the Wnt receptor, Frizzled. They participate in regulating the patterning along the anteroposterior axis in vertebrates. Human Sfrp1 has been found frequently to be downregulated in breast cancer and is associated with disease progression and poor prognosis
PKVCPPCENEEESAKTLLDNFCASDFALKVKIKEISYENGDRKVIGEKKKEILKQGPLKKKDLKKLVLWL
KNGANCPCPQLDNLNGVYLVMGRKVDGKLLLTSIYKWQKKNKEFKRAVRKWKKHKC
>gnl|CDD|239636 cd03581, NTR_Sfrp3_like, NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins similar to human Sfrp3 and Sfrp4. Sfrps are soluble proteins containing an NTR domain C-terminal to a cysteine-rich Frizzled domain. They show diverse functions and are thought to work in Wnt signaling indirectly, as modulators or antagonists by binding Wnt ligands, and directly, via the Wnt receptor, Frizzled. They participate in regulating the patterning along the anteroposterior axis in vertebrates. Human Sfrp3 may suppress the growth and invasiveness of androgen-independent prostate cancer cells
KTYLKNNYNYVIRAKVKEVKRGCHEVTAVVEVKEILKSSLVNIPRDTVTLYTNSGCLCPPLTPNEEYIIM
GYEDEERSRLLLVEGSLAEKWKDRLGKKVKRWDQKLQHQRR
>gnl|CDD|239637 cd03582, NTR_complement_C5, NTR/C345C domain, complement C5 subfamily; The NTR domain found in complement C5 is also known as C345C because it occurs at the C-terminus of complement C3, C4 and C5. Complement C5 is activated by C5 convertase, which itself is a complex between C3b and C3 convertase. The small cleavage fragment, C5a, is the most important small peptide mediator of inflammation, and the larger active fragment, C5b, initiates late events of complement activation. The NTR/C345C domain is important in the function of C5 as it interacts with enzymes that convert C5 to the active form, C5b. The domain has also been found to bind to complement components C6 and C7, and may specifically interact with their factor I modules
CVAAQCQCFAAACDVTITAARRKSETCKEQIAYAYKVMIKSSAAEGDFVTYKATVLDVLKNGQAELEKDS
EVTLVKKATCTSVELQEGQQYLIMGKEALKIRLNRSFRYRYPLDSEAWIEWWPTDTGCPECQDFLNQLDD
FAEDLQLMGC
>gnl|CDD|239638 cd03583, NTR_complement_C3, NTR/C345C domain, complement C3 subfamily; The NTR domain found in complement C3 is also known as the C345C domain because it occurs at the C-terminus of complement C3, C4 and C5. Complement C3 plays a pivotal role in the activation of the complement systems, as all pathways (classical, alternative, and lectin) result in the processing of C3 by C3 convertase. The larger fragment, activated C3b, contains the NTR/C345C domain and binds covalently, via a reactive thioester, to cell surface carbohydrates including components of bacterial cell walls and immune aggregates. The smaller cleavage product, C3a, acts independently as a diffusible signal to mediate local inflammatory processes. The structure of C3 shows that the NTR/C345C domain is located in an exposed position relative to the rest of the molecule. The function of the domain in complement C3 is poorly understood
CAEENCSMQKKGDKVTNDERIDKACEPGVDYVYKVKLVNVELSDSYDIYTMEILQVIKEGTDEGPEGKTR
TFISHPKCREALNLKEGKDYLIMGLSSDLWRIKDKYSYVIGKDTWIEYWPTEDECQDEENQKLCLDLAEF
SEQLTVFGC
>gnl|CDD|239639 cd03584, NTR_complement_C4, NTR/C345C domain, complement C4 subfamily; The NTR domain found in complement C4 is also known as the C345C domain because it occurs at the C-terminus of complement C3, C4 and C5. Complement C4 is a key player in the activation of the component classical pathway. C4 is cleaved by activated C1 to yield C4a anaphylatoxin, and the larger fragment C4b, an essential component of the C3- and C5-convertase enzymes. C4b binds covalently to the surface of pathogens through a reactive thioester. The role of the NTR/C345C domain in C4 (C4b) is unclear
CQCAEGGCPKQKSTFSKEITKTDRFDFACYSPRVDYAYVVKVLNISEKSNFELYETSITDVLQTTGDVSV
KPEETRVFLKRLSCKLELKKGKEYLIMGKDGATSDSNGHMQYLLDSKTWVEKIPSEKRCKATRNRSACKQ
LNEFLKEYKINGC
>gnl|CDD|239640 cd03585, NTR_TIMP, NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential regulators of extracellular matrix turnover and remodeling. They form complexes with matrix metalloproteases (MMPs) and inactivate them irreversibly by non-covalently binding their active zinc-binding sites. The levels of activated membrane-type MMPs, MMPs, and free TIMPs determine the balance between matrix degradation and matrix formation or stabilization. Consequently, TIMPs play roles in processes that require the remodeling and degradation of connective tissue, such as development, morphogenesis, wound healing, as well as in various diseases and pathological states such as tumor cell metastasis, arthritis, and artherosclerosis. Most TIMPs bind to a variety of MMPs. TIMP-1 and TIMP-2 appear to be multifunctional proteins with diverse biological action. They may exhibit growth factor-like activity and can inhibit angiogenesis. TIMP-3 has been implicated in apoptosis
CSCAPVHPQQAFCNSDIVIRAKIVGEKEVDSGNDYGNPIKRIQYEIKQIKMFKGFDKDKDIQYIYTPASS
SLCGVKLDVNGKKEYLISGKVEGGKVHITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCFV
SSPNECLWTDWLSEKSINGHQAKHYACIKRSDGSCSWYRGGAP
>gnl|CDD|176459 cd03586, PolY_Pol_IV_kappa, DNA Polymerase IV/Kappa. Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion synthesis (TLS) polymerase. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Known primarily as Pol IV in prokaryotes and Pol kappa in eukaryotes, this polymerase has a propensity for generating frameshift mutations. The eukaryotic Pol kappa differs from Pol IV and Dpo4 by an N-terminal extension of ~75 residues known as the "N-clasp" region. The structure of Pol kappa shows DNA that is almost totally encircled by Pol kappa, with the N-clasp region augmenting the interactions between DNA and the polymerase. Pol kappa is more resistant than Pol eta and Pol iota to bulky guanine adducts and is efficient at catalyzing the incorporation of dCTP. Bacterial pol IV has a higher error rate than other Y-family polymerases
IHIDMDAFYASVEQRDNPELKGKPVAVGGSSDRGVVSTASYEARKFGVRSAMPIFQAKKLCPNLIFVPPR
FDKYREVSRQIMEILREYTPLVEPLSIDEAYLDVTDYVRLFGSATEIAKEIRARIREETGLTASAGIAPN
KFLAKIASDLNKPNGLTVIPPEDVEEFLAPLPVRKIPGVGKVTAEKLKELGIKTIGDLAKLDVELLKKLF
GKSGRRLYELARGIDNRPVEPDRERKSIGVERTFSEDLTDPEELLEELLELAEELAERLRKRGLKGRTVT
VKLKYADFSTRTRSRTLPEPTDDAEDIYELALELLEELLDGRPIRLLGVRLSGL
>gnl|CDD|239641 cd03587, SOCS, SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region of CIS/SOCS family proteins (in combination with a SH2 domain), ASBs (ankyrin repeat-containing proteins with a SOCS box), SSBs (SPRY domain-containing proteins with a SOCS box), and WSBs (WD40 repeat-containing proteins with a SOCS box), as well as, other miscellaneous proteins. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
NPRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLYK
>gnl|CDD|153058 cd03588, CLECT_CSPGs, C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins. CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity
CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFR
WSDGHPLQFENWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG
>gnl|CDD|153059 cd03589, CLECT_CEL-1_like, C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds
CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFSIPGLIAHLVSIHSQEENDFVYDLFESSRGPDTPYGLW
IGLHDRTSEGPFEWTDGSPVDFTKWAGGQPDNYGGNEDCVQMWRRGDAGQSWNDMPCDAVFPYICKM
>gnl|CDD|153060 cd03590, CLECT_DC-SIGN_like, C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices
CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGE
WKWVDGTPLNSSKTFWHPGEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK
>gnl|CDD|153061 cd03591, CLECT_collectin_like, C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis
EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGP
LTYTNWKPGEPNNAGGGEDCVEMYTSGKWNDVACNLTRLFVCEF
>gnl|CDD|153062 cd03592, CLECT_selectins_like, C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors
WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYYWIDGNDINNEGTWVDTDKKE
LEYKNWAPGEPNNGRNENCLEIYIKDNGKWNDEPCSKKKSAICYT
>gnl|CDD|153063 cd03593, CLECT_NK_receptors_like, C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs). CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro
CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPW
KWIDGSPLNNLFNIRGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK
>gnl|CDD|153064 cd03594, CLECT_REG-1_like, C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro
CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYGPGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHD
PQQSRGWEWSDGSKLDYRSWDRNPPYARGGYCAELSRSTGFLKWNDANCEERNPFICKY
>gnl|CDD|153065 cd03595, CLECT_chondrolectin_like, C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton
QRICRRGTEKPCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGDFWIG
LRRSSQYNVTSSACSSLYYWLDGSISTFRNWYVDEPSCGSEVCVVMYHQPSAPAGQGGPYLFQWNDDNCN
MKNNFICKY
>gnl|CDD|153066 cd03596, CLECT_tetranectin_like, C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells
CLKGTKIHKKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGNWEVWLGINDMVA
EGKWVDVNGSPISYFNWEREITAQPDGGKRENCVALSSSAQGKWFDEDCRREKPYVCEF
>gnl|CDD|153067 cd03597, CLECT_attractin_like, C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells
CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMTKQKLTPWVGLRK
INVSYWCWEDMSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER
>gnl|CDD|153068 cd03598, CLECT_EMBP_like, C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP
GRCYRFVKSPRTFRDAQVICRRCYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGRCRRFSWV
DGSVWNYAYWAPGQPGNRRGHCVELCTRGGHWRRAHCKLRRPFICSY
>gnl|CDD|153069 cd03599, CLECT_DGCR2_like, C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS). CLECT_DGCR2_like: C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DGS is also known velo-cardio-facial syndrome (VCFS). DGS is a genetic abnormality that results in malformations of the heart, face, and limbs and is associated with schizophrenia and depressive disorders. DGCR2 is a candidate for involvement in the pathogenesis of DGS since the DGCR2 gene lies within the minimal DGS critical region (MDGRC) of 22q11, which when deleted gives rise to DGS, and the DGCR2 gene is in close proximity to the balanced translocation breakpoint in a DGS patient having a balanced translocation
CPSGWHHYEGTASCYKVYLSGENYWDAVQTCQKVNGSLATFTTDQELQFILAQEWDFDERVFGRKDQCKF
WVGYQYVITNRNHSLEGRWEVAYKGSMEVFLPPEPIFATGMSTNDNVFCAQLQCFQIPSLRERGLHSWHA
ENCYEKSSFLCKR
>gnl|CDD|153070 cd03600, CLECT_thrombomodulin_like, C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors
CVSDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGRHGRGSLRLWIGLQREPRQ
CSDPSLPLRGFSWVTGDQDTDFSNWLQEPAGTCTSPRCVALSAAGSTPDNLKWKDGPCSARADGYLCKFS
F
>gnl|CDD|153071 cd03601, CLECT_TC14_like, C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein
YEILCSDETMNYAKAGAFCRSRGMRLASLAMRDSEMRDAILAFTLVKGHGYWVGADNLQDGEYDFLWNDG
VSLPTDSDLWAPNEPSNPQSRQLCVQLWSKYNLLDDEYCGRAKRVICEK
>gnl|CDD|153072 cd03602, CLECT_1, C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer
RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDSWRWSDGSESSF
RNWNTFQPFGQGDCATMYSSGRWYAALCSALKPFICYD
>gnl|CDD|153073 cd03603, CLECT_VCBS, A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer
HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGASWIGASDAATEGTWKWSDGEEST
YTNWGSGEPHNNGGGNEDYAAINHFPGISGKWNDLANSYNTLGYVIEW
>gnl|CDD|467538 cd03670, NUDIX_ADPRase_Nudt9, ADP-ribose pyrophosphatase. ADP-ribose pyrophosphatase (ADPRase;EC 3.6.1.13, also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 9/Nudt9, catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). ADPRase-m is also known as NUDT9. It can be distinugished from the cytosolic ADPRase by a N-terminal target sequence unique to mitochondrial ADPRase. NUDT9 functions as a monomer
NPIGRTGLSGRGLLGRWGPNHAADPIITRWKRDADGGNVERSGKKVLEFVAIKRKDDGEWAIPGGFVDPG
EKVSDTLKREFYEEALNSLEEPEIEELLEELFKDGVEIYKGYVDDPRNTDNAWMETVAVNFHDEFGKGVG
LLKLEAGDDAGKVKWMDVTSDLNLYASHSDLLREVAKSH
>gnl|CDD|467539 cd03671, NUDIX_Ap4A_hydrolase_plant_like, plant diadenosine tetraphosphate (Ap4A) hydrolase and similar proteins. Diadenosine tetraphosphate (Ap4A) hydrolase is a member of the NUDIX hydrolase superfamily. Members of this family are well represented in a variety of prokaryotic and eukaryotic organisms. Phylogenetic analysis reveals two distinct subgroups where plant enzymes fall into one group (represented by this subfamily) and fungi/animals/archaea enzymes fall into another. Bacterial enzymes are found in both subfamilies. Ap4A is a potential by-product of aminoacyl tRNA synthesis, and accumulation of Ap4A has been implicated in a range of biological events, such as DNA replication, cellular differentiation, heat shock, metabolic stress, and apoptosis. Ap4A hydrolase cleaves Ap4A asymmetrically into ATP and AMP. It is important in the invasive properties of bacteria and thus presents a potential target for the inhibition of such invasive bacteria. Besides the signature NUDIX motif (G[X5]E[X7]REUXEEXGU where U is Ile, Leu, or Val), Ap4A hydrolase is structurally similar to the other members of the NUDIX hydrolase superfamily with some degree of variations. Several regions in the sequences are poorly defined and substrate and metal binding sites are only predicted based on kinetic studies
PYRPNVGIVLFNRDGQVLVGRRIDVPGAWQFPQGGIDEGEDPEEAALRELYEETGLSPEDVEIIAETPDW
LTYDLPEDLIRKGWGGKYRGQKQKWFLFRFTGDDSEINLDTHEHPEFDAWRWVDLEELPDLVVPFKRDVY
RQVLKEF
>gnl|CDD|467540 cd03672, NUDIX_Dcp2p_Nudt20, mRNA decapping enzyme 2. mRNA decapping enzyme 2 (Dcp2p; EC 3.6.1.62), nucleoside diphosphate linked moiety X))-type motif 20/Nudt20, is required for degradation of mRNAs, both in normal mRNA turnover, and in nonsense-mediated mRNA decay (NMD). Its catalytic subunit, and Dcp1p are the two components of the decapping enzyme complex. Decapping is a key step in both general and nonsense-mediated 5'-_3' mRNA-decay pathways. Dcp2p contains an all-alpha helical N-terminal domain and a C-terminal domain which has the NUDIX fold. While decapping is not dependent on the N-terminus of Dcp2p, it does affect its efficiency. Dcp1p binds the N-terminal domain of Dcp2p stimulating the decapping activity of Dcp2p. Decapping permits the degradation of the transcript and is a site of numerous control inputs. It is responsible for nonsense-mediated decay as well as AU-rich element (ARE)-mediated decay. In addition, it may also play a role in the levels of mRNA. Enzymes belonging to the NUDIX hydrolase superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V)
VPVRGAILLNEDLDKVLLVKGWKSNSSWGFPKGKINKDESDADCAIREVYEETGFDISDLINDKDYIELT
INGQRVRLYIIPGVPEDTPFEPQTRKEISKIEWFDIDDLPKNKKKKGKNSNKFYMVNPFVKPLKKWIKKR
KQKK
>gnl|CDD|467541 cd03673, NUDIX_Ap6A_hydrolase, diadenosine hexaphosphate (Ap6A) hydrolase. Diadenosine hexaphosphate (Ap6A) hydrolase is a member of the NUDIX hydrolase superfamily. Ap6A hydrolase specifically hydrolyzes diadenosine polyphosphates, but not ATP or diadenosine triphosphate, and it generates ATP as the product. Ap6A, the most preferred substrate, hydrolyzes to produce two ATP molecules, which is a novel hydrolysis mode for Ap6A. These results indicate that Ap6A hydrolase is a diadenosine polyphosphate hydrolase. It requires the presence of a divalent cation, such as Mn2+, Mg2+, Zn2+, and Co2+, for activity. Members of the NUDIX hydrolase superfamily are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site
VEAAGGVVWRGRGGGGEVLLIHRPRYDDWSLPKGKLEPGETPEEAAVREVEEETGLRVRLGRPLGTTRYT
YTRKGKGILKKVHYWLMRALGGEFLPQPEEEIDEVRWLPPDEARRLLTYPSDREVLDAALE
>gnl|CDD|467542 cd03674, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
HFTASAFVVNPDRGKVLLVHHRKLGRWLQPGGHVEPDEDPLEAALREAREETGLDVELLSPLSPDPLDID
VHPIPANPGEPAHLHLDVRYLAVADGDEALRKSDESSDVRWFPLDELEELSMDPNLRKLL
>gnl|CDD|467543 cd03675, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. Contains a crystal structure of the NUDIX hydrolase from Nitrosomonas europaea, which has an unknown function. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
VTVAAVVERDGRFLLVEEETDGRLVLNQPAGHLEPGESLLEAAIRETLEETGWEVEPTALLGIYQWTAPD
NGVTYLRFAFAGELLEHLPDQPLDSGIIRAHWLTLEEILALQARLRSPLVLRCIEDYLAGQRYPLSLI
>gnl|CDD|467544 cd03676, NUDIX_Tnr3_like, thiamine diphosphokinase Tnr3 from Schizosaccharomyces pombe and similar proteins. Tnr3 is a bifunctional enzyme composed of a C-terminal thiamine pyrophosphokinase domain, which transfers pyrophosphate from ATP to thiamine and an N-terminal NUDIX hydrolase domain that converts oxidized derivatives of thiamine diphosphate (oxothiamine and oxythiamine) to their respective monophosphates. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belong to this superfamily requires a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
LFGIVTYGVHLNGYVRDGDGLRLWVARRSATKATYPGKLDNLVAGGVPAGESPLETLVREAEEEAGLPED
LARQARPAAGRVSYFYRSDEGGLQPEVLYVYDLELPEDFVPKPQDGEVESFELMSVDEVLEALRAGEFKP
NCALVMLDFLIRH
>gnl|CDD|239649 cd03677, MM_CoA_mutase_beta, Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, Beta subunit-like subfamily; contains bacterial proteins similar to the beta subunit of MCMs from Propionbacterium shermanni and Streptomyces cinnamonensis, which are alpha/beta heterodimers. For P. shermanni MCM, it is known that only the alpha subunit binds coenzyme B12 and substrates. The role of the beta subunit is unclear. MCM catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA. The reaction proceeds via radical intermediates beginning with a substrate-induced homolytic cleavage of the Co-C bond of coenzyme B12 to produce cob(II)alamin and the deoxyadenosyl radical. MCM plays an important role in the conversion of propionyl-CoA to succinyl-CoA during the degradation of propionate for the Krebs cycle. Methylobacterium extorquens MCM participates in the glyoxylate regeneration pathway. In M. extorquens, MCM forms a complex with MeaB; MeaB may protect MCM from irreversible inactivation. In some bacteria, MCM is involved in the reverse metabolic reaction, the rearrangement of succinyl-CoA to methylmalonyl-CoA. Examples include P. shermanni MCM during propionic acid fermentation and Streptomyces MCM in polyketide biosynthesis
FPPVSREAWKAKVEKDLKGAPFEERLVWKTYDGITIKPLYTREDAAPLPPVPEGAAPGGWDVCQRIDVPD
AAEANEAALADLERGATALWLVLDNAGCSPEDLARLLEGVDLDLAPVYLDAGFLSLAAAAALLALVEDRK
ALAGSLGLDPLGALARTGSLFLEPDLARLAELAARSAPGLRAITVDAVPYHNAGATAAQELAYALAAAVE
YLRALTEAGLDVEEAARQIEFRLAVGSDQFLEIAKLRALRLLWARIAEAYGVPEARAARIHARTSRRNKT
RYDPYVNMLRTTTEAFSAGLGGADSITVLPFDAALGLPDDFARRIARNTQLILKEESHLGRVADPAGGSY
YIESLTDQLAEKAWELFQEIEAAGGFVAALESGLIQKKIAESAAKRQKALATRKKPLTGVNEYPNLEEKP
LERL
>gnl|CDD|239650 cd03678, MM_CoA_mutase_1, Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, unknown subfamily 1; composed of uncharacterized bacterial proteins containing a C-terminal MCM domain. MCM catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA. The reaction proceeds via radical intermediates beginning with a substrate-induced homolytic cleavage of the Co-C bond of coenzyme B12 to produce cob(II)alamin and the deoxyadenosyl radical. MCM plays an important role in the conversion of propionyl-CoA to succinyl-CoA during the degradation of propionate for the Krebs cycle. In some bacteria, MCM is involved in the reverse metabolic reaction, the rearrangement of succinyl-CoA to methylmalonyl-CoA. Members of this subfamily also contain an N-terminal coenzyme B12 binding domain followed by a domain similar to the E. coli ArgK membrane ATPase
ILAHWPEKKQRYSGDEYVYKVRGKEIRTELTTESLSGLKIPKVALPRFQDWGEILRWLLRENVPGEFPFT
AGVFPFKRTGEDPTRMFAGEGTPERTNRRFHYLSEGMPAKRLSTAFDSVTLYGEDPDPRPDIYGKIGNSG
VSVATLDDMKKLYSGFDLCAPNTSVSMTINGPAPMLLAFFLNTAIDQQVEKFRRENGIRAETLRSVRGTV
QADILKEDQAQNTCIFSTEFALRMMGDIQEYFIAHQVRNFYSVSISGYHIAEAGANPITQLAFTLANGFT
YVEYYLSRGMHIDDFAPNLSFFFSNGLDPEYAVIGRVARRIWARAMREKYGANERSQMLKYHIQTSGRSL
HAQEIDFNDIRTTLQALYAIYDNCNSLHTNAYDEAITTPTEESVRRALAIQLIINRELGLAKNENPLQGS
FIIEELTDLVEEAVLAEFERISERGGVLGAMETGYQRNKIQEESLYYESLKHDGELPIIGVNTFRSPNGD
PTILP
>gnl|CDD|239651 cd03679, MM_CoA_mutase_alpha_like, Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, Alpha subunit-like subfamily; contains proteins similar to the alpha subunit of Propionbacterium shermanni MCM, as well as human and E. coli MCM. Members of this subfamily contain an N-terminal MCM domain and a C-terminal coenzyme B12 binding domain. MCM catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA. The reaction proceeds via radical intermediates beginning with a substrate-induced homolytic cleavage of the Co-C bond of coenzyme B12 to produce cob(II)alamin and the deoxyadenosyl radical. MCM plays an important role in the conversion of propionyl-CoA to succinyl-CoA during the degradation of propionate for the Krebs cycle. In higher animals, MCM is involved in the breakdown of odd-chain fatty acids, several amino acids, and cholesterol. Methylobacterium extorquens MCM participates in the glyoxylate regeneration pathway. In M. extorquens, MCM forms a complex with MeaB; MeaB may protect MCM from irreversible inactivation. In some bacteria, MCM is involved in the reverse metabolic reaction, the rearrangement of succinyl-CoA to methylmalonyl-CoA. Examples include P. shermanni MCM during propionic acid fermentation, E.coli MCM in a pathway for the conversion of succinate to propionate and Streptomyces MCM in polyketide biosynthesis. Sinorhizobium meliloti strain SU47 MCM plays a role in the polyhydroxyalkanoate degradation pathway. P. shermanni and Streptomyces cinnamonensis MCMs are alpha/beta heterodimers. It has been shown for P. shermanni MCM that only the alpha subunit binds coenzyme B12 and substrates. Human MCM is a homodimer with two active sites. Mouse and E.coli MCMs are also homodimers. In humans, impaired activity of MCM results in methylmalonic aciduria, a disorder of propionic acid metabolism
LPEWAELAAKALKGREPEGLNWHTPEGIPVKPLYTADDLDDMEHLDTLPGIPPFVRGPYATMYTFRPWTI
RQYAGFSTAEESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVVGDVGKAGVAIDSVEDMKILFDGI
PLDKMSVSMTMNGAVLPILAFYIVAAEEQGVPPEKLTGTIQNDILKEFMVRNTYIYPPEPSMRIIADIFA
YTSKNMPKFNSISISGYHMQEAGATADLELAYTLADGLEYIRTGLKAGLDIDEFAPRLSFFWGIGMNFFM
EIAKLRAARLLWAKLVKQFGPKNPKSLALRTHSQTSGWSLTEQDPYNNVVRTCIEAMAAVFGGTQSLHTN
ALDEAIALPTDFSARIARNTQLILQEETGITKVVDPWGGSYYMESLTDDLAEKAWALIQEIEELGGMAKA
IESGIPKLRIEEAAARRQARIDSGREVIVGVNKYRLDHEEPLDVLKIDNTAVRAEQIARLKKLRAERDPE
AVQAALDALTEAAETGEGNLLALAVDAARARATVGEISDALEKVFG
>gnl|CDD|239652 cd03680, MM_CoA_mutase_ICM_like, Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, isobutyryl-CoA mutase (ICM)-like subfamily; contains archaeal and bacterial proteins similar to the large subunit of Streptomyces cinnamonensis coenzyme B12-dependent ICM. ICM from S. cinnamonensis is comprised of a large and a small subunit. The holoenzyme appears to be an alpha2beta2 heterotetramer with up to 2 molecules of coenzyme B12 bound. The small subunit binds coenzyme B12. ICM catalyzes the reversible rearrangement of n-butyryl-CoA to isobutyryl-CoA, intermediates in fatty acid and valine catabolism, which in S. cinnamonensis can be converted to methylmalonyl-CoA and used in polyketide synthesis
RKEWEEETLAPWLKKFPERKEKFTTLSGIPVKRVYTPADLPEDDYLEDIGYPGEYPFTRGVYPTMYRGRL
WTMRQFAGFGTAEETNKRFKYLLEQGQTGLSVAFDLPTLMGYDSDHPMAEGEVGKVGVAIDTLADMEILF
DGIPLDKVSTSMTINPPAAILLAMYIAVAEKQGVPLEKLRGTIQNDILKEYIAQKEWIFPPEPSVRLVTD
IIEYCAKNVPKWNPISISGYHIREAGATAVQELAFTLADGIAYVEAVLERGLDVDEFAPRLSFFFNSHND
FFEEIAKFRAARRIWAKIMKERFGAKNPRSMMLRFHTQTAGASLTAQQPENNIVRTALQALAAVLGGTQS
LHTNSFDEALALPTEEAVRIALRTQQIIAYESGVADVVDPLGGSYYVEALTDEIEEEAWKYIDKIDAMGG
MIKAIEDGYFQREIADAAYKYQKEIESGERIVVGVNKFVVEEEPPIILLKVDDEVEERQIERLKEVRAER
DNAKVQEALDALRKAAEDEENLMPYIIEAVKAYATLGEICDVLREVFG
>gnl|CDD|239653 cd03681, MM_CoA_mutase_MeaA, Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, MeaA-like subfamily; contains various methylmalonyl coenzyme A (CoA) mutase (MCM)-like proteins similar to the Streptomyces cinnamonensis MeaA, Methylobacterium extorquens MeaA and Streptomyces collinus B12-dependent mutase. Members of this subfamily contain an N-terminal MCM domain and a C-terminal coenzyme B12 binding domain. S. cinnamonensis MeaA is a putative B12-dependent mutase which provides methylmalonyl-CoA precursors for the biosynthesis of the monensin polyketide via an unknown pathway. S. collinus B12-dependent mutase may be involved in a pathway for acetate assimilation
PWIIRTYAGHSTAEESNELYRKNLAKGQTGLSVAFDLPTQTGYDSDHILAKGEVGKVGVPINHLGDMRIL
FNQIPLEQMNTSMTINATAMWLLSLYVAVAEEQGADVTALQGTTQNDIIKEYLSRGTYIFPPAPSLRLIV
DMIEYCLKNIPKWNPMNICSYHLQEAGATPVQELAFALATAIAVLDAVRDRNCFPEDEFEDVVSRISFFV
NAGIRFVEEMCKMRAFTELWDEITRDRYGIKDAKYRRFRYGVQVNSLGLTEQQPENNVWRILIEMLAVTL
SKDARARAVQLPAWNEALGLPRPWDQQWSLRMQQVLAYETDLLEYDDLFDGSKVVEAKVEALKEEARAEL
QRILDMGGAVQAIENGYMKSQLVKSNAERLARIENNEMVIVGVNKWQEGEPSPLTTD
>gnl|CDD|239654 cd03682, ClC_sycA_like, ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it facilitates acid resistance in acidic soil. Mutation of this gene (sycA) in Rhizobium tropici CIAT899 causes serious deficiencies in nodule development, nodulation competitiveness, and N2 fixation on Phaseolus vulgaris plants, due to its reduced ability for acid resistance. This family is part of the ClC chloride channel superfamiy. These proteins catalyse the selective flow of Cl- ions across cell membranes and Cl-/H+ exchange transport. These proteins share two characteristics that are apparently inherent to the entire ClC chloride channel superfamily: a unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge
LALLIGLLVGSASALFLWSLDWATEFREAHPWLLPFLPLAGLLIGYLYQKFGKNSEKGNNLIIEEIHGPE
EGIPLRMAPLVLFGTVLTHLFGGSAGREGTAVQMGGSLADAFGRVFKLPEEDRRILLIAGIAAGFAAVFG
TPLAGAIFALEVLVLGRLRYSALIPCLVAAIVADWVSHALGLEHTHYHIVFIPTLDPLLFVKVILAGIIF
GLAGRLFAELLHFLKKLLKKRIKNPYLRPFVGGLLIILLVYLLGSRRYLGLGTPLIEDSFFGGTVYPYDW
LLKLIFTVITLGAGFKGGEVTPLFFIGATLGNALAPILGLPVSLLAALGFVAVFAGATNTPLACIIMGIE
LFGAENAPYFFIACLVAYLFSGHTGIYG
>gnl|CDD|239655 cd03683, ClC_1_like, ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ClC-1 is expressed in skeletal muscle and its mutation leads to both recessively and dominantly-inherited forms of muscle stiffness or myotonia. ClC-K is exclusively expressed in kidney. Similarly, mutation of ClC-K leads to nephrogenic diabetes insipidus in mice and Bartter's syndrome in human. These proteins belong to the ClC superfamily of chloride ion channels, which share the unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge. This domain is found in the eukaryotic halogen ion (Cl-, Br- and I-) channel proteins, that perform a variety of functions including cell volume regulation, regulation of intracelluar chloride concentration, membrane potential stabilization, charge compensation necessary for the acidification of intracellular organelles and transepithelial chloride transport
DWLFLALLGILMALISIAMDFAVEKLLNARRWLYSLLTGNSLLQYLVWVAYPVALVLFSALFCKYISPQA
VGSGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGPFVHISSIVAALLSKLTTFFSGI
YENESRRMEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAFTFRLLAVFFSDQ
ETITALFKTTFFVDFPFDVQELPIFALLGIICGLLGALFVFLHRKIVRFRRKNRLFSKFLKRSPLLYPAI
VALLTAVLTFPFLTLFLFIVVKFVLTALAITLPVPAGIFMPVFVIGAALGRLVGEIMAVLFPEGIRGGIS
NPIGPGGYAVVGAAAFSGAVTHTVSVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQPSIYDSIIKIKK
LPYLPD
>gnl|CDD|239656 cd03684, ClC_3_like, ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 was initially cloned from rat kidney. Expression of ClC-3 produces outwardly-rectifying Cl currents that are inhibited by protein kinase C activation. It has been suggested that ClC-3 may be a ubiquitous swelling-activated Cl channel that has very similar characteristics to those of native volume-regulated Cl currents. The function of ClC-4 is unclear. Studies of human ClC-4 have revealed that it gives rise to Cl currents that rapidly activate at positive voltages, and are sensitive to extracellular pH, with currents decreasing when pH falls below 6.5. ClC-4 is broadly distributed, especially in brain and heart. ClC-5 is predominantly expressed in the kidney, but can be found in the brain and liver. Mutations in the ClC-5 gene cause certain hereditary diseases, including Dent's disease, an X-chromosome linked syndrome characterised by proteinuria, hypercalciuria, and kidney stones (nephrolithiasis), leading to progressive renal failure. These proteins belong to the ClC superfamily of chloride ion channels, which share the unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge. This domain is found in the eukaryotic halogen ion (Cl- and I-) channel proteins, that perform a variety of functions including cell volume regulation, the membrane potential stabilization, transepithelial chloride transport and charge compensation necessary for the acidification of intracellular organelles
GIAIGLIAGLIDIIASWLSDLKEGYCNYIIYVLLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFII
RGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNIISRLFPKYRRNEAKRREILSAAAAAGVA
VAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLVLFEVEYDRDWHYFELIPF
ILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTELLELLFNEC
EPGDDNSLCCYRDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGALFGRIVGILVE
QLAYSYPDSIFFACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVMVS
KWVADAIGKEGIYDAHIHLNGYPFL
>gnl|CDD|239657 cd03685, ClC_6_like, ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. Proteins in this family are ubiquitous in eukarotes and their functions are unclear. They are expressed in intracellular organelles membranes. This family belongs to the ClC superfamily of chloride ion channels, which share the unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge. ClC chloride ion channel superfamily perform a variety of functions including cellular excitability regulation, cell volume regulation, membrane potential stabilization, acidification of intracellular organelles, signal transduction, and transepithelial transport in animals
ESLDYEVIENDLFREEWRKRKKKQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYIE
KGRLFTAFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSV
SGGLALGKEGPMIHIGACIAAGLSQGGSTSLRLDFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGV
LFSLEEVASFWNQALTWRTFFSSMIVTFTLNFFLSGCNSGKCGLFGPGGLIMFDGSSTKYLYTYFELIPF
MLIGVIGGLLGALFNHLNHKVTRFRKRINHKGKLLKVLEALLVSLVTSVVAFPQTLLIFFVLYYFLACWT
FGIAVPSGLFIPMILIGAAYGRLVGILLGSYFGFTSIDPGLYALLGAAAFLGGVMRMTVSLTVILLELTN
NLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFLHNGFPVV
>gnl|CDD|239658 cd03687, Dehydratase_LU, Dehydratase large subunit. This family contains the large (alpha) subunit of B12-dependent glycerol dehydratases (GDHs) and B12-dependent diol dehydratases (DDHs). GDH is isofunctional with DDH. These enzymes can each catalyze the conversion of 1,2-propanediol, glycerol, and 1,2-ethanediol to the corresponding aldehydes via a coenzyme B12 (adenosylcobalamin)-dependent radical mechanism. Both enzymes exhibit a subunit composition of alpha2beta2gamma2. The enzymes differ in substrate specificity; glycerol is the preferred substrate for GDH and 1,2-propanediol for DDH. GDH shows almost equal affinity for both (R) and (S)-isomers while DDH prefers the (S) isomer. GDH plays a key role in the dihydroxyacetone (DHA) pathway and DDH in the anaerobic degradation of 1,2-diols. The radical mechanism has been well studied for Klebsiella oxytoca DDH and involves binding of 1,2-propanediol to the enzyme to induce hemolytic cleavage of the Co-C5' bond of the coenzyme to form cob(II)alamin and the adenosyl radical. Hydrogen abstraction from the substrate follows producing a substrate generated radical and 5'-deoxyadenosine. Rearrangement to the product radical is then followed by abstraction of a hydrogen atom from 5'-deoxyadenosine to produce the hydrated propionaldehyde and regenerate the adenosyl radical. After the Co-C5' bond is reformed and the hydrated aldehyde dehydrated, the process is complete. GDH has a higher affinity for coenzyme B12 than DDH. Both GDH and DDH are activated by various monovalent cations with K+, NH4+, and Rb+ being the most effective. However, DDH differs from GDH in that it is partially active with Cs+ and Na+. In general, the alpha and beta subunits for both enzymes are on different chains. However, for a subset of the GDHs, alpha and beta subunits appear to be on a single chain
VLAKRPVNQDGFVKEWPEEGLIAMESPNDPKPSIKIVNGRVVELDGKPVADFDMIDHFIARYGINLERAE
EAMALDSVKLARMLVDPNVPREEIVRLTTAMTPAKLVEVVSQMNVVEMMMAMQKMRARRTPSNQAHVTNV
KDNPVQIAADAAEAAARGFDEQETTVAVARYAPFNAIALLVGSQVGRPGVLTQCSLEEATELRLGMRGLT
SYAETISVYGTEPVFTDGDDTPWSKAFLASAYASRGLKMRFTSGSGSEVLMGYAEGKSMLYLESRCIYIT
KAAGVQGLQNGGVSCIGVTAAVPSGIRAVLAENLIASMLDLECASGNDQTFSHSDIRRTARTLMQLLPGT
DFIFSGYSAVPNYDNMFAGSNFDAEDFDDYNVLQRDLKVDGGLRPVTEEEVIAVRNKAARAIQAVFRELG
LPPITDEEVEAATYAHGSKDMPERNPVEDIKAAEEIINRNITGLDVVKALARGGFTDEAENILNMLKQRL
TGDYLQTSAIIDDDFQVLSAVNDPNDYAGPGTGYRLSGERWEEIKNIPGALDPNE
>gnl|CDD|293889 cd03688, eIF2_gamma_II, Domain II of the gamma subunit of eukaryotic translation initiation factor 2. This subfamily represents domain II of the gamma subunit of eukaryotic translation initiation factor 2 (eIF2-gamma) found in eukaryota and archaea. eIF2 is a G protein that delivers the methionyl initiator tRNA to the small ribosomal subunit and releases it upon GTP hydrolysis after the recognition of the initiation codon. eIF2 is composed of three subunits, alpha, beta and gamma. Subunit gamma shows strongest conservation, and it confers both tRNA binding and GTP/GDP binding
DLDKPPRMIVIRSFDVNKPGTEVDDLKGGVIGGSLIQGVLKVGDEIEIRPGIVVKKGGKTTCRPIFTKIV
SLFAEGNDLEEAVPGGLIGVGTKLDPTLTKADRLVGQVVGEPG
>gnl|CDD|293890 cd03689, RF3_II, Domain II of bacterial Release Factor 3. This subfamily represents domain II of bacterial Release Factor 3 (RF3). Termination of protein synthesis by the ribosome requires two release factor (RF) classes. The class II RF3 is a GTPase that removes class I RFs (RF1 or RF2) from the ribosome after release of the nascent polypeptide. RF3 in the GDP state binds to the ribosomal class I RF complex, followed by an exchange of GDP for GTP and release of the class I RF. Sequence comparison of class II release factors with elongation factors shows that prokaryotic RF3 is more similar to EF-G whereas eukaryotic eRF3 is more similar to eEF1A, implying that their precise function may differ
FSGFVFKIQANMDPKHRDRIAFLRVCSGKFERGMKVKHVRTGKEVRLSNATTFMAQDRETVEEAYPGDII
GLPNHGTFQIGDTFTEG
>gnl|CDD|293891 cd03690, Tet_II, Domain II of ribosomal protection proteins Tet(M) and Tet(O). This subfamily represents domain II of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to domain II of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA
ESELSGTVFKIEYDPKGERLAYLRLYSGTLRLRDSVRVSGEEEKIKITELRTFENGELVKVDRVYAGDIA
ILVGLKSLRVGDVLGD
>gnl|CDD|293892 cd03691, BipA_TypA_II, Domain II of BipA. BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu
FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLERVEVEEAEAGDIV
AIAGLEDITIGDTICDPEVPEPLP
>gnl|CDD|293893 cd03692, mtIF2_IVc, C2 subdomain of domain IV in mitochondrial translation initiation factor 2. This model represents the C2 subdomain of domain IV of mitochondrial translation initiation factor 2 (mtIF2) which adopts a beta-barrel fold displaying a high degree of structural similarity with domain II of the translation elongation factor EF-Tu. The C-terminal part of mtIF2 contains the entire fMet-tRNAfmet binding site of IF-2 and is resistant to proteolysis. This C-terminal portion consists of two domains, IF2 C1 and IF2 C2. IF2 C2 has been shown to contain all molecular determinants necessary and sufficient for the recognition and binding of fMet-tRNAfMet. Like IF2 from certain prokaryotes such as Thermus thermophilus, mtIF2lacks domain II which is thought to be involved in binding of E.coli IF-2 to 30S subunits
GEAEVRAVFKISKVGTIAGCYVTEGKIKRNAKVRVLRDGEVIYEGKISSLKRFKDDVKEVKKGYECGITL
ENFNDIKEGDIIEA
>gnl|CDD|293894 cd03693, EF1_alpha_II, Domain II of elongation factor 1-alpha. This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression
TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFN
VKGVSVKDIKRGDVAGDSKND
>gnl|CDD|293895 cd03694, GTPBP_II, Domain II of the GTPBP family of GTP binding proteins. This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution
FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKFRPVTVKSIHRNRQPVDRARAGQSASFA
LKKIKRESLRKGMVLVS
>gnl|CDD|293896 cd03695, CysN_NodQ_II, Domain II of the large subunit of ATP sulfurylase. This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha
FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLEDE
IDVSRGDLIVR
>gnl|CDD|293897 cd03696, SelB_II, Domain II of elongation factor SelB. This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation
FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGV
DAKELERGFVLSE
>gnl|CDD|293898 cd03697, EFTU_II, Domain II of elongation factor Tu. Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP
FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLR
GVKKEDVERGMVLAKPG
>gnl|CDD|293899 cd03698, eRF3_II_like, Domain II of the eukaryotic class II release factor-like proteins. This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression
PFRLSIDDKYKSPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEETDWAIAGDTVTLRLRG
IEVEDIQPGDILSS
>gnl|CDD|293900 cd03699, EF4_II, Domain II of Elongation Factor 4 (EF4). Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis
LRALIFDSWYDPYRGVVVLVRVFDGTLKKGDKIRFMATGKEYEVLEVGVFTPKMVPTDELSAGEVGYIIA
GIKSVKDARVGDTITL
>gnl|CDD|293901 cd03700, EF2_snRNP_like_II, Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein. This subfamily represents domain II of elongation factor (EF) EF-2 found in eukaryotes and archaea, and the C-terminal portion of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of U5-116 kD/Snu114p
LMVYSSKMVPTSDKGRFYAFGRVFAGTVHAGQKVRILGPNYTPGKKEDLRIKAIQRLWLMMGRYVEEIND
VPAGNIVGLVGIDQFLQKTGTTTTI
>gnl|CDD|293902 cd03701, IF2_IF5B_II, Domain II of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5. This family represents domain II of prokaryotic Initiation Factor 2 (IF2) and its archaeal and eukaryotic homologue aeIF5B. IF2, the largest initiation factor, is an essential GTP binding protein. In E. coli, three natural forms of IF2 exist in the cell, IF2alpha, IF2beta1, and IF2beta2. Disruption of the eIF5B gene (FUN12) in yeast causes a severe slow-growth phenotype, associated with a defect in translation. eIF5B has a function analogous to prokaryotic IF2 in mediating the joining of the 60S ribosomal subunit. The eIF5B consists of three N-terminal domains (I, II, II) connected by a long helix to domain IV. Domain I is a G domain, domain II and IV are beta-barrels and domain III has a novel alpha-beta-alpha sandwich fold. The G domain and the beta-barrel domain II display a similar structure and arrangement to the homologous domains in EF1A, eEF1A and aeIF2gamma
EPRGVILEVKLDKGAGITIDMLVQEGTLRVGDTIVAGESKDVIYTRIRALLDPDPLEEMESRKKGNKRKE
VGAASGVKILGFGQELPHAGDPLEVV
>gnl|CDD|293903 cd03702, IF2_mtIF2_II, Domain II of bacterial and mitochondrial Initiation Factor 2. This family represents domain II of bacterial Initiation Factor 2 (IF2) and its eukaryotic mitochondrial homolog mtIF2. IF2, the largest initiation factor, is an essential GTP binding protein. In E. coli, three natural forms of IF2 exist in the cell, IF2alpha, IF2beta1, and IF2beta2. Bacterial IF-2 is structurally and functionally related to eukaryotic mitochondrial mtIF-2
LARGVVIESKLDKGRGPVATVLVQNGTLKVGDILVAGTTYGKVRAMIDDNGKRIKEAGPSTPVEILGLNG
VPQAGDKFIVVDSEKEAREIAEKRQE
>gnl|CDD|293904 cd03703, aeIF5B_II, Domain II of archaeal and eukaryotic Initiation Factor 5. This family represents domain II of archaeal and eukaryotic IF5B. aIF5B and eIF5B are homologs of prokaryotic Initiation Factor 2 (IF2). Disruption of the eIF5B gene (FUN12) in yeast causes a severe slow-growth phenotype, associated with a defect in translation. eIF5B has a function analogous to prokaryotic IF2 in mediating the joining of joining of 60S subunits. The eIF5B consists of three N-terminal domains (I, II, II) connected by a long helix to domain IV. Domain I is a G domain, domain II and IV are beta-barrels and domain III has a novel alpha-beta-alpha sandwich fold. The G domain and the beta-barrel domain II display a similar structure and arrangement to the homologous domains of EF1A, eEF1A and aeIF2gamma
PGKGTVLEVKEEEGLGTTIDVILYDGTLREGDTIVVGGLNGPIVTKVRALLKPKPLKEMRVKSRFIHVKE
VVAAAGVKIAAPDLEKAIAGSPLRVVGNEDEIEELIEEVME
>gnl|CDD|294003 cd03704, eRF3_C_III, C-terminal domain of eRF3. This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions: N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils
PVVTEFEAQIVILDLLKSIITAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIAR
LETARPICLETFKDFPQLGRFTLRDEGKTIAIGKVLKL
>gnl|CDD|294004 cd03705, EF1_alpha_III, Domain III of Elongation Factor 1. Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 is composed of four subunits: the alpha chain, which binds GTP and aminoacyl-tRNAs; the gamma chain that probably plays a role in anchoring the complex to other cellular components; and the beta and delta (or beta') chains. This model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha)
KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKM
VPTKPLCVETFSEYPPLGRFAVRDMRQTVAVGVI
>gnl|CDD|294005 cd03706, mtEFTU_III, Domain III of mitochondrial EF-TU (mtEF-TU). mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors
KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVL
EKGQRFTLREGGRTIGTGVVTKL
>gnl|CDD|294006 cd03707, EFTU_III, Domain III of Elongation Factor (EF) Tu. EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively
KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIAL
EEGLRFAIREGGRTVGAGVV
>gnl|CDD|294007 cd03708, GTPBP_III, Domain III of the GP-1 family of GTPases. This family includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in the cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution
RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVLRTGDRALVRFRFLYRPEYLREGQR
LIFREGRTKGIGTVTKV
>gnl|CDD|239680 cd03709, lepA_C, lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized in the cytoplasmic membrane. LepA is ubiquitous in Bacteria and Eukaryota (e.g. Saccharomyces cerevisiae GUF1p), but is missing from Archaea. LepA exhibits significant homology to elongation factors (EFs) Tu and G. The function(s) of the proteins in this family are unknown. The N-terminal domain of LepA is homologous to a domain of similar size found in initiation factor 2 (IF2), and in EF-Tu and EF-G (factors required for translation in Escherichia coli). Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including S. cerevisiae GUF1) originated within the bacterial LepA family. LepA has never been observed in archaea, and eukaryl LepA is organellar. LepA is therefore a true bacterial GTPase, found only in the bacterial lineage
EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIVYDFFDKLKSISKGYASLD
YELIGYRESD
>gnl|CDD|239681 cd03710, BipA_TypA_C, BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of the elongation factors EF-G and EF-2. A member of the ribosome binding GTPase superfamily, BipA is widely distributed in bacteria and plants. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and, is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion
EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNH
VFDGYEPYK
>gnl|CDD|239682 cd03711, Tet_C, Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to the C terminal domains of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA
EPYLRFELEVPQDALGRAMSDLAKMGATFEDPQIKGDEVTLEGTIPVATSQDYQSELPSYTHGEGVLETE
FKGYRPCH
>gnl|CDD|239683 cd03713, EFG_mtEFG_C, EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational elongation factor (EF) EF-G. Included in this group is the C-terminus of mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2) proteins. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homologue of mtEFG2, MEF2
EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRGGWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTME
FSHYEEVP
>gnl|CDD|239684 cd03714, RT_DIRS1, RT_DIRS1: Reverse transcriptases (RTs) occurring in the DIRS1 group of retransposons. Members of the subfamily include the Dictyostelium DIRS-1, Volvox carteri kangaroo, and Panagrellus redivivus PAT elements. These elements differ from LTR and conventional non-LTR retrotransposons. They contain split direct repeat (SDR) termini, and have been proposed to integrate via double-stranded closed-circle DNA intermediates assisted by an encoded recombinase which is similar to gamma-site-specific integrase
VDLKDAYFHIPILPRSRDLLGFAWQGETYQFKALPFGLSLAPRVFTKVVEALLAPLRLLGVRIFSYLDDL
LIIASSIKTSEAVLRHLRATLLANLGFTLNLEKSKLGPTQRITFLGLEL
>gnl|CDD|239685 cd03715, RT_ZFREV_like, RT_ZFREV_like: A subfamily of reverse transcriptases (RTs) found in sequences similar to the intact endogenous retrovirus ZFERV from zebrafish and to Moloney murine leukemia virus RT. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses. These elements can be divided into two major groups. One group contains retroviruses and DNA viruses whose propagation involves an RNA intermediate. They are grouped together with transposable elements containing long terminal repeats (LTRs). The other group, also called poly(A)-type retrotransposons, contain fungal mitochondrial introns and transposable elements that lack LTRs. Phylogenetic analysis suggests that ZFERV belongs to a distinct group of retroviruses
PVNQKQYPLPREAREGITPHIQELLEAGILVPCQSPWNTPILPVKKPGGNDYRMVQDLRLVNQAVLPIHP
AVPNPYTLLSLLPPKHQWYTVLDLANAFFSLPLAPDSQPLFAFEWEGQQYTFTRLPQGFKNSPTLFHEAL
ARDLAPFPLEHEGTILLQYVDDLLLAADSEEDCLKGTDALLTHLGELGYKVSPKKAQICRAEVKFLGVVW
>gnl|CDD|239686 cd03716, SOCS_ASB_like, SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB (SPRY domain-containing SOCS box proteins) protein families. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence of a variable number of repeats. SSB proteins contain a central SPRY domain and a C-terminal SOCS. Recently, it has been shown that all four SSB proteins interact with the MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF), and that SSB-1, SSB-2, and SSB-4 interact with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain
STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE
>gnl|CDD|239687 cd03717, SOCS_SOCS_like, SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. These intracellular proteins regulate the responses of immune cells to cytokines. Identified as negative regulators of the cytokine-JAK-STAT pathway, they seem to play a role in many immunological and pathological processes. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. Related SOCS boxes are also present in Rab40-like proteins and insect proteins of unknown function that also contain a NEUZ (domain in neuralized proteins) domain
TSVRSLQHLCRFVIRQCTRRDLIDQLPLPRRLKDYLKEY
>gnl|CDD|239688 cd03718, SOCS_SSB1_4, SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB1 and SSB4 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF) and also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
PEPLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLLYQ
>gnl|CDD|239689 cd03719, SOCS_SSB2, SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB2 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF). SSB2, like SSB4 and SSB1, also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
AEPHSLLHLSRLCVRHALGDTRLGQVSALPLPPAMKRYLLYQ
>gnl|CDD|239690 cd03720, SOCS_ASB1, SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
GNPRSLLSLCRIAVRRALGKQRLSLICSLPLPDPIKKFLLHE
>gnl|CDD|239691 cd03721, SOCS_ASB2, SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ
>gnl|CDD|239692 cd03722, SOCS_ASB3, SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ABS3 has been shown to be negative regulator of TNF-R2-mediated cellular responses to TNF-alpha by direct targeting of tumor necrosis factor receptor II (TNF-R2) for ubiquitination and proteasome-mediated degradation. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
ASVPSLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSDVLRMY
>gnl|CDD|239693 cd03723, SOCS_ASB4_ASB18, SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Asb4 was identified as imprinted gene in mice. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
GTPRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEPEGVLY
>gnl|CDD|239694 cd03724, SOCS_ASB5, SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB5 has been implicated in the initiation of arteriogenesis. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
ATPSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFLQYR
>gnl|CDD|239695 cd03725, SOCS_ASB6, SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB6 interacts with the adaptor protein APS and recruits elongin B/C to the insulin receptor signaling complex. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
SYPPPLKHLCRVFIRLCLRPWPVDVKVKALPLPDRLKWYLLPEH
>gnl|CDD|239696 cd03726, SOCS_ASB7, SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
RQPRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKHKFDD
>gnl|CDD|239697 cd03727, SOCS_ASB8, SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB8 is highly transcribed in skeletal muscle and in lung carcinoma cell lines. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
SAPGTLKALARYAVRRSLGVQYLPEAVKQLPLPRSVKEYLLLL
>gnl|CDD|239698 cd03728, SOCS_ASB_9_11, SOCS (suppressors of cytokine signaling) box of ASB9 and 11 proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
EGPPSLMQLCRLCIRKCFGRKQHHKIHKLHLPEPLKHFLLYR
>gnl|CDD|239699 cd03729, SOCS_ASB13, SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
STPLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSYN
>gnl|CDD|239700 cd03730, SOCS_ASB14, SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
TNPRSLKHLCRLKIRACMGRLRLRCPVFMSFLPLPNRLKAYILYKEYDLYGQGIFTG
>gnl|CDD|239701 cd03731, SOCS_ASB15, SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB15 is expressed predominantly in skeletal muscle and participates in the regulation of protein turnover and muscle cell development by stimulating protein synthesis and regulating differentiation of muscle cells. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
ENPRPLKHLCRLKIRKLMGLQKLQQPSSMKKLPLPPALKRYILYKEYDLYGQELKL
>gnl|CDD|239702 cd03733, SOCS_WSB_SWIP, SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily contains WSB-1 (SOCS-box-containing WD-40 protein), part of an E3 ubiquitin ligase for the thyroid-hormone-activating type 2 iodothyronine deiodinase (D2), and SWiP-1 (SOCS box and WD-repeats in Protein), a WD40-containing protein that is expressed in embryonic structures of chickens and regulated by Sonic Hedgehog (Shh), as well as, their isoforms WSB-2 and SWiP-2. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
RVVSSLQHLCRMALRRVMTTQQVLALPIPKKMKEFLTYR
>gnl|CDD|239703 cd03734, SOCS_CIS1, SOCS (suppressors of cytokine signaling) box of CIS (cytokine-inducible SH2 protein) 1-like proteins. Together with the SOCS proteins, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. CIS1, like SOCS1 and SOCS3, is involved in the down-regulation of the JAK/STAT pathway. CIS1 binds to cytokine receptors at STAT5-docking sites, which prohibits recruitment of STAT5 to the receptor signaling complex and results in the down-regulation of activation by STAT5
SSARSLQHLCRLVINRLVTDVDCLPLPRRMADYLRQYPFQL
>gnl|CDD|239704 cd03735, SOCS_SOCS1, SOCS (suppressors of cytokine signaling) box of SOCS1-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. SOCS1, like CIS1 and SOCS3, is involved in the down-regulation of the JAK/STAT pathway. SOCS1 has a dual function as a direct potent JAK kinase inhibitor and as a component of an E3 ubiquitin-ligase complex recruiting substrates to the protein degradation machinery
VRVRPLQELCRKSIVATFGRENLARIPLNPVLKDYLKSFPFQI
>gnl|CDD|239705 cd03736, SOCS_SOCS2, SOCS (suppressors of cytokine signaling) box of SOCS2-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. SOCS2 has recently been shown to regulate neuronal differentiation by controlling expression of a neurogenic transcription factor, Neurogenin-1. SOCS2 binds to GH receptors and inhibits the activation of STAT5b induced by GH. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
TSTPSLQHLCRITINKCTRQIQELPLPTRLKDYLTEYTYHV
>gnl|CDD|239706 cd03737, SOCS_SOCS3, SOCS (suppressors of cytokine signaling) box of SOCS3-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. SOCS3, like CIS1 and SOCS1, is involved in the down-regulation of the JAK/STAT pathway. SOCS3 inhibits JAK activity indirectly through recruitment to the cytokine receptors. SOCS3 has been shown to play an essential role in placental development and a non-essential role in embryo development. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
SSVSTLQHLCRKTVNGHLDSYEKRTQLPLPIKEFLDQYDAPL
>gnl|CDD|239707 cd03738, SOCS_SOCS4, SOCS (suppressors of cytokine signaling) box of SOCS4-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
TFPFSLQHICRTVICNCTTYDGIDALPIPSSMKLYLKEYHYKSKVRVLRIDAPEQQ
>gnl|CDD|239708 cd03739, SOCS_SOCS5, SOCS (suppressors of cytokine signaling) box of SOCS5-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. SOCS5 inhibits Th2 differentiation by inhibiting IL-4 signaling. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
TFPFSLQYICRAVICRCTTYDGIDALPLPSMLQDFLKEYHYKQKVRVRWLEREPIKK
>gnl|CDD|239709 cd03740, SOCS_SOCS6, SOCS (suppressors of cytokine signaling) box of SOCS6-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
MQVRSLQYLCRFVIRQYTRIDLIQKLPLPNKMKGYLLEKHY
>gnl|CDD|239710 cd03741, SOCS_SOCS7, SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. SOCS7 is important in the functioning of neuronal cells. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
KNVQSLQHLCRFVIRKLVRRDHIPALPLPRRLIDYLREKHYYSEQLEVY
>gnl|CDD|239711 cd03742, SOCS_Rab40, SOCS (suppressors of cytokine signaling) box of Rab40-like proteins. Rab40 is part of the Rab family of small GTP-binding proteins that form the largest family within the Ras superfamily. Rab proteins regulate vesicular trafficking pathways, behaving as membrane-associated molecular switches. Rab40 is characterized by a SOCS box c-terminal to the GTPase domain. The SOCS boxes interact with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
NKVLSLQDLCCRAIVSCTPVYLIDKLPLPVSIKSHLKSFAMAN
>gnl|CDD|239712 cd03743, SOCS_SSB4, SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB4 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF). SSB4, like SSB2 and SSB1, also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
PEPLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYLQYQ
>gnl|CDD|239713 cd03744, SOCS_SSB1, SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB1 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF), both the absence and the presence of HGF and enhances the HGF-MET-induced mitogen-activated protein kinases Erk-transcription factor Elk-1-serum response elements (SRE) pathway. SSB1, like SSB2 and SSB4, also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
PEPLPLMDLCRRSVRLALGRERLSEIHTLPLPASLKNYLLYQ
>gnl|CDD|239714 cd03745, SOCS_WSB2_SWIP2, SOCS (suppressors of cytokine signaling) box of WSB2/SWiP2-like proteins. This family consists of WSB-2 (SOCS-box-containing WD-40 protein) and SWiP-2 (SOCS box and WD-repeats in Protein). No functional information is available for WSB2 or SWiP-2, but limited information is available for the isoforms WSB-1 and SWiP-1. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
RVLPSLRHLCRKALRHFLTTYQVLALPIPKKMKEFLTYR
>gnl|CDD|239715 cd03746, SOCS_WSB1_SWIP1, SOCS (suppressors of cytokine signaling) box of WSB1/SWiP1-like proteins. This subfamily contains WSB-1 (SOCS-box-containing WD-40 protein), part of an E3 ubiquitin ligase for the thyroid-hormone-activating type 2 iodothyronine deiodinase (D2) and SWiP-1 (SOCS box and WD-repeats in Protein), a WD40-containing protein that is expressed in embryonic structures of chickens and regulated by Sonic Hedgehog (Shh). The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions
RQVASLQHLCRMAIRRVMPTQQVKELPIPSKLLEFLTYRT
>gnl|CDD|239716 cd03747, Ntn_PGA_like, Penicillin G acylase (PGA) belongs to a family of beta-lactam acylases that includes cephalosporin acylase (CA) and aculeacin A acylase. PGA and CA are crucial for the production of backbone chemicals like 6-aminopenicillanic acid and 7-aminocephalosporanic acid (7-ACA), which can be used to synthesize semi-synthetic penicillins and cephalosporins, respectively. While both PGA and CA have a conserved Ntn (N-terminal nucleophile) hydrolase fold and the structural similarity at their active sites is very high, their sequence similarity is low
SNNWAVAGERTASGKPLLANDPHLPLSGPSIWYEAHLSGPGLDVTGATLPGLPGIVIGHNGRIAWGHTNS
YADVVDLYREKLDPEDPTRYRYDGEWRPLETRTETIKVKGGADVELTVRRTRHGPVISDDGGAAAAYALL
RWAGLDEDATLDALLALNRARNWDEFRAALARFGAPSQNLVYADRDGNIGYVANGRVPIRPNGNDGSLPL
PGWDGEYDWDGYLPFEELPQVINPPSGYVVNANNRPWPANYPYPLGSGYWAPPYRAQRIRRLLEAKEKFT
VEDMQAIQLDWVQAVEFGDGPSARGVVDFGDS
>gnl|CDD|239717 cd03748, Ntn_PGA, Penicillin G acylase (PGA) is the key enzyme in the industrial production of beta-lactam antibiotics. PGA hydrolyzes the side chain of penicillin G and related beta-lactam antibiotics releasing 6-amino penicillanic acid (6-APA), a building block in the production of semisynthetic penicillins. PGA is widely distributed among microorganisms, including bacteria, yeast and filamentous fungi but it's in vivo role remains unclear
SNMWIVGPEKAQDGSAILINGPQFGWYNPAYTYGIGLHGAGFDVVGNTPFAYPFILFGHNGHIAWGATAG
FGDVVDIFAEKLNPENPSQYLHNGKWKTMEKRKETITVKGQAPVEMTVYRTVHGPVVQFDETQHTAYSKA
RAWDGYELQSLMAWTKQTKAKNWEEWLDQASKQALTINWYYADKDGNIGYVHTGFYPVRQSGHDPRLPVP
GTGEMDWKGLLPFAENPKVYNPKQGYIANWNNKPAKGYPNTLFAFYWGSADRVQEIDNRLEARDKLTAQQ
IWDINRTTSYADLNNRYFLPFLQVAAQGLPANDNRVYLVETLEAWDGMNEDEDDGGYYDAPGSALFDAWL
NEMLKRTLMDEVPAPFDKWYSATGYRTGQNPANWRMPAKAMTFREKNFLGIPQAYASETRAIEEYQNRGT
ENNMIVFDEKGVSACDVVPPGQSGFVAPDGTPSPHYEDQLKLYENFGCKPLWFTKDDVRANATSVETL
>gnl|CDD|239718 cd03749, proteasome_alpha_type_1, proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIA
GLTADARVLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLF
QTCPSGNYFEYKATSIGARSQSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEQELTIKNVSIAIV
G
>gnl|CDD|239719 cd03750, proteasome_alpha_type_2, proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMV
YSGMGPDFRVLVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGGPY
LYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYNEDLELEDAIHTAILTLKEGFEGQMTEKNIEIGICGE
TKGFRLLTPAEIKDYLA
>gnl|CDD|239720 cd03751, proteasome_alpha_type_3, proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
GTGYDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHI
GIAVAGLLADGRHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSD
GPQLYMIEPSGVSYGYFGCAIGKGKQAAKTELEKLKFSELTCREAVKEAAKIIYIVHDEIKDKAFELELS
WV
>gnl|CDD|239721 cd03752, proteasome_alpha_type_4, proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHI
ACAVAGITSDANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKH
YGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMDSTKLTSEKLEF
ATL
>gnl|CDD|239722 cd03753, proteasome_alpha_type_5, proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCA
MSGLIADARTLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGKKAMSRPFGVALLIAGVD
ENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVEL
ATV
>gnl|CDD|239723 cd03754, proteasome_alpha_type_6, proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIG
CVMTGMIADSRSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEEL
GPQLYKCDPAGYFAGYKATAAGVKEQEATNFLEKKLKKKPDLIESYEETVELAISCLQTVLSTDFKATEI
EVGVV
>gnl|CDD|239724 cd03755, proteasome_alpha_type_7, proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLA
FAGLTADARVLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTP
RLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQSGSKNIELAVM
>gnl|CDD|239725 cd03756, proteasome_alpha_archeal, proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
GYDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGA
ATSGLVADARVLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGGP
RLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEEAIELALKALYAALEENETPENVEIAYVT
V
>gnl|CDD|239726 cd03757, proteasome_beta_type_1, proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKAR
IKMYKYSHNKEMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSA
SSLIQPLLDNQVGRKNQNNVERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLR
KD
>gnl|CDD|239727 cd03758, proteasome_beta_type_2, proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMR
NGYELSPKAAANFTRRELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCL
SILDRYYKPDMTVEEALELMKKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL
>gnl|CDD|239728 cd03759, proteasome_beta_type_3, proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYR
LREEREIKPKTFSSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGCPSIPSDFVVSGTASEQL
YGMCESLWRPDMEPDELFETISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK
>gnl|CDD|239729 cd03760, proteasome_beta_type_4, proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDEC
LDDGHSLSPKEIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYL
ALPLLREAWEKKPDLTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP
>gnl|CDD|239730 cd03761, proteasome_beta_type_5, proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRN
KERISVAAASKLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLD
SGYRYDLSVEEAYDLARRAIYHATHRDAYSGGNVNLYHVREDGWRKIS
>gnl|CDD|239731 cd03762, proteasome_beta_type_6, proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIEL
GEPPLVKTAASLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVD
ANYKPGMTLEECIKFVKNALSLAMSRDGSSGGVIRLVIITKDGVERKF
>gnl|CDD|239732 cd03763, proteasome_beta_type_7, proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNT
GRKPRVVTALTMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLED
RYKPDMTEEEAKKLVCEAIEAGIFNDLGSGSNVDLCVITKDGVEYLRNY
>gnl|CDD|239733 cd03764, proteasome_beta_archeal, Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme for non-lysosomal protein degradation in both the cytosol and the nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are both members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRR
GRPMSIKALATLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLE
DEYKEDMTVEEAKKLAIRAIKSAIERDSASGDGIDVVVITKDGYKELE
>gnl|CDD|239734 cd03765, proteasome_beta_bacterial, Bacterial proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each
TYCLGIKLDAGLVFASDSRTNAGVDNISTYRKMFVFSVPGERVIVLLTAGNLATTQAVISLLQRDLEDPE
ETNLLNAPTMFDAARYVGETLREVQEQDREALKKAGIDFSASFILGGQIKGEEPRLFLIYPQGNFIEATP
DTPFLQIGETKYGKPILDRVITPDTSLEDAAKCALVSMDSTMRSNLSVGPPLDLLVYERDSLQVGHYRRI
EEDDPYFAMIRKAWSEALREAFDQLP
>gnl|CDD|239735 cd03766, Gn_AT_II_novel, Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its function has not yet been determined. The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer
MCGILCSVSPSGPHINSSLLSEELLPNLRNRGPDYLSTRQLSVTNWTLLFTSSVLSLRGDHVTRQPLVDQ
STGNVLQWNGELYNIDGVEDEENDTEVIFELLANCSSESQDILDVLSSIEGPFAFIYYDASENKLYFGRD
CLGRRSLLYKLDPNGFELSISSVSGSSSGSGFQEVLAGGIY
>gnl|CDD|239736 cd03767, SR_Res_par, Serine recombinase (SR) family, Partitioning (par)-Resolvase subfamily, catalytic domain; Serine recombinases catalyze site-specific recombination of DNA molecules by a concerted, four-strand cleavage and rejoining mechanism which involves a transient phosphoserine linkage between DNA and the enzyme. They are functionally versatile and include resolvases, invertases, integrases, and transposases. This subgroup is composed of proteins similar to the E. coli resolvase found in the par region of the RP4 plasmid, which encodes a highly efficient partitioning system. This protein is part of a complex stabilization system involved in the resolution of plasmid dimers during cell division. Similar to Tn3 and other resolvases, members of this family may contain a C-terminal DNA binding domain
IRAYLRASTDEQDATRAKESLEAFATERGFYIAGFYVENASGAKLDRPELFRLLDDAQSGDVLLVEQIDR
LSRLPLDDWETLKASIAAKGLRVVSLDLPTSHSALAAEDNDFTGRILSAINDMLLDLLAAMARKDYEDRR
ERQKQG
>gnl|CDD|239737 cd03768, SR_ResInv, Serine Recombinase (SR) family, Resolvase and Invertase subfamily, catalytic domain; members contain a C-terminal DNA binding domain. Serine recombinases catalyze site-specific recombination of DNA molecules by a concerted, four-strand cleavage and rejoining mechanism which involves a transient phosphoserine linkage between DNA and the enzyme. They are functionally versatile and include resolvases, invertases, integrases, and transposases. Resolvases and invertases affect resolution or inversion and comprise a major phylogenic group. Resolvases (e.g. Tn3, gamma-delta, and Tn5044) normally recombine two sites in direct repeat causing deletion of the DNA between the sites. Invertases (e.g. Gin and Hin) recombine sites in inverted repeat to invert the DNA between the sites. Cointegrate resolution with gamma-delta resolvase requires the formation of a synaptosome of three resolvase dimers bound to each of two res sites on the DNA. Also included in this subfamily are some putative integrases including a sequence from bacteriophage phi-FC1
VIGYARVSTDDQSLERQLEALKAAGECDKIFEEKGSGGKKERPELQKLLEDLREGDTLVVTKLDRLGRST
KDLLEIVEELREKGVSLRSLTEGIDTSTPSGKLMLTILGAFAEFERELIRERTKEG
>gnl|CDD|239738 cd03769, SR_IS607_transposase_like, Serine Recombinase (SR) family, IS607-like transposase subfamily, catalytic domain; members contain a DNA binding domain with homology to MerR/SoxR located N-terminal to the catalytic domain. Serine recombinases catalyze site-specific recombination of DNA molecules by a concerted, four-strand cleavage and rejoining mechanism which involves a transient phosphoserine linkage between DNA and the enzyme. They are functionally versatile and include resolvases, invertases, integrases, and transposases. This subfamily is composed of proteins that catalyze the transposition of insertion sequence (IS) elements such as IS607 from Helicobacter and IS1535 from Mycobacterium, and similar proteins from other bacteria and several archaeal species. IS elements are DNA segments that move to new sites in prokaryotic and eukaryotic genomes causing insertion mutations and gene rearrangements
TVLYARVSSHDQKDDLERQIERLEAYATAQGWIVEVIKDIGSGLNEKRKGLLKLLEDVLAGKVERVVITY
KDRLARFGFELLEELFKAYGVEIVVINQEENEELEQELVEDLIEIITSFSARLYGKRSHKKKKL
>gnl|CDD|239739 cd03770, SR_TndX_transposase, Serine Recombinase (SR) family, TndX-like transposase subfamily, catalytic domain; composed of large serine recombinases similar to Clostridium TndX and TnpX transposases. Serine recombinases catalyze site-specific recombination of DNA molecules by a concerted, four-strand cleavage and rejoining mechanism which involves a transient phosphoserine linkage between DNA and the enzyme. They are functionally versatile and include resolvases, invertases, integrases, and transposases. TndX mediates the excision and circularization of the conjugative transposon Tn5397 from Clostridium difficile. TnpX is responsible for the movement of the nonconjugative chloramphenicol resistance elements of the Tn4451/3 family. Mobile genetic elements such as transposons are important vehicles for the transmission of virulence and antibiotic resistance in many microorganisms
TALYCRLSRDDDLDGESNSIENQKAILEEYAKENGLENIRHYIDDGFSGTTFDRPGFNRMIEDIEAGKID
IVIVKDMSRLGRNYLKVGLYMEILFPKKGVRFIAINDGVDSADGDDDFIPFKNILNEWYAKDISRKIKAS
>gnl|CDD|239740 cd03771, MATH_Meprin, Meprin family, MATH domain; Meprins are multidomain, highly glycosylated extracellular metalloproteases, which are either anchored to the membrane or secreted into extracellular spaces. They are expressed in renal and intestinal brush border membranes, leukocytes, and cancer cells, and are capable of cleaving growth factors, cytokines, extracellular matrix proteins, and biologically active peptides. Meprin proteases are composed of two related subunits, alpha and beta, which form homo- or hetro-complexes where the basic unit is a disulfide-linked dimer. Despite their similarity, the two subunits differ in their ability to self-associate, in proteolytic processing during biosynthesis and in substrate specificity. Both subunits are synthesized as membrane spanning proteins, however, the alpha subunit is cleaved during biosynthesis and loses its transmembrane domain. Meprin beta forms homodimers or heterotetramers while meprin alpha oligomerizes into large complexes containing 10-100 subunits. Both alpha and beta subunits contain a catalytic astacin (M12 family) protease domain followed by the adhesion or interaction domains MAM, MATH and AM. The MATH and MAM domains provide symmetrical intersubunit disulfide bonds necessary for the dimerization of meprin subunits. The MATH domain may also be required for folding of an activable zymogen
CPEAVWRVRNFSQLLETTPKGTKIYSPRFYSPEGYAFQVGLYPNGTESYPGYTGLYFHLCSGENDDVLEW
PCPNRQATMTLLDQDPDIQQRMSNQRSFTTDPSMTSSDNGEYFWDRPSKVGSYDTDTNGCTCYRGPGYGW
STFISHSRLRRRDFLKGDDLIILLDFE
>gnl|CDD|239741 cd03772, MATH_HAUSP, Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, N-terminal MATH (TRAF-like) domain; composed of proteins similar to human HAUSP, an enzyme that specifically catalyzes the deubiquitylation of p53 and MDM2, hence playing an important role in the p53-MDM2 pathway. It contains an N-terminal TRAF-like domain and a C-terminal catalytic protease (C19 family) domain. The tumor suppressor p53 protein is a transcription factor that responds to many cellular stress signals and is regulated primarily through ubiquitylation and subsequent degradation. MDM2 is a RING-finger E3 ubiquitin ligase that promotes p53 ubiquitinylation. p53 and MDM2 bind to the same site in the N-terminal TRAF-like domain of HAUSP in a mutually exclusive manner. HAUSP also interacts with the Epstein-Barr nuclear antigen 1 (EBNA1) protein of the Epstein-Barr virus (EBV), which efficiently immortalizes infected cells predisposing the host to a variety of cancers. EBNA1 plays several important roles in EBV latent infection and cellular transformation. It binds the same pocket as p53 in the HAUSP TRAF-like domain. Through interactions with p53, MDM2 and EBNA1, HAUSP plays a role in cell proliferation, apoptosis and EBV-mediated immortalization
SEATFSFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRNYPDRNPHQKSVGFFLQCNAESDSTSWSCHAQ
AVLRIINYKDDEPSFSRRISHLFFSKENDWGFSNFMTWSEVTDPEKGFIEDDTITLEVYVQADAPHG
>gnl|CDD|239742 cd03773, MATH_TRIM37, Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal protein and is a member of the tripartite motif (TRIM) protein subfamily, also known as the RING-B-box-coiled-coil (RBCC) subfamily of zinc-finger proteins. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction and hepatomegaly. TRIM37, similar to other TRIMs, contains a cysteine-rich, zinc-binding RING-finger domain followed by another cysteine-rich zinc-binding domain, the B-box, and a coiled-coil domain. TRIM37 is autoubiquitinated in a RING domain-dependent manner, indicating that it functions as an ubiquitin E3 ligase. In addition to the tripartite motif, TRIM37 also contains a MATH domain C-terminal to the coiled-coil domain. The MATH domain of TRIM37 has been shown to interact with the TRAF domain of six known TRAFs in vitro, however, it is unclear whether this is physiologically relevant. Eleven TRIM37 mutations have been associated with Mulibrey nanism so far. One mutation, Gly322Val, is located in the MATH domain and is the only mutation that does not affect the length of the protein. It results in the incorrect subcellular localization of TRIM37
IPPYDSATFTLENFSTLRQSADPVYSDPLNVDGLCWRLKVYPDGNGEVRGNFLSVFLELCSGLGEASKYE
YRVEMVHQANPTKNIKREFASDFEVGECWGYNRFFRLDLLINEGYLLPENDTLILRFSVRPP
>gnl|CDD|239743 cd03774, MATH_SPOP, Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to human SPOP. SPOP was isolated as a novel antigen recognized by serum from a scleroderma patient, whose overexpression in COS cells results in a discrete speckled pattern in the nuclei. It contains an N-terminal MATH domain and a C-terminal BTB (also called POZ) domain. Together with Cul3, SPOP constitutes an ubiquitin E3 ligase which is able to ubiquitinate the PcG protein BMI1, the variant histone macroH2A1 and the death domain-associated protein Daxx. Therefore, SPOP may be involved in the regulation of these proteins and may play a role in transcriptional regulation, apoptosis and X-chromosome inactivation. Cul3 binds to the BTB domain of SPOP whereas Daxx and the macroH2A1 nonhistone region have been shown to bind to the MATH domain. Both MATH and BTB domains are necessary for the nuclear speckled accumulation of SPOP. There are many proteins, mostly uncharacterized, containing both MATH and BTB domains from C. elegans and plants which are excluded from this family
KVVKFCYMWTISNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSE
VRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQD
>gnl|CDD|239744 cd03775, MATH_Ubp21p, Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with similarity to Ubp21p of fission yeast. Ubp21p is a deubiquitinating enzyme that may be involved in the regulation of the protein kinase Prp4p, which controls the formation of active spliceosomes. Members of this family are similar to human HAUSP (Herpesvirus-associated ubiquitin-specific protease) in that they contain an N-terminal MATH domain and a C-terminal catalytic protease (C19 family) domain. HAUSP is also an ubiquitin-specific protease that specifically catalyzes the deubiquitylation of p53 and MDM2. The MATH domain of HAUSP contains the binding site for p53 and MDM2. Similarly, the MATH domain of members in this family may be involved in substrate binding
QSFTWRIKNWSELEKKVHSPKFKCGGFEWRILLFPQGNSQTGGVSIYLEPHPEEEEKAPLDEDWSVCAQF
ALVISNPGDPSIQLSNVAHHRFNAEDKDWGFTRFIELRKLAHRTPDKPSPFLENGELNITVYVR
>gnl|CDD|239745 cd03776, MATH_TRAF6, Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF6 subfamily, TRAF domain, C-terminal MATH subdomain; composed of proteins with similarity to human TRAF6, including the Drosophila protein DTRAF2. TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF6 is the most divergent in its TRAF domain among the mammalian TRAFs. In addition to mediating TNFR family signaling, it is also an essential signaling molecule of the interleukin-1/Toll-like receptor superfamily. Whereas other TRAF molecules display similar and overlapping TNFR-binding specificities, TRAF6 binds completely different sites on receptors such as CD40 and RANK. TRAF6 serves as a molecular bridge between innate and adaptive immunity and plays a central role in osteoimmunology. DTRAF2, as an activator of nuclear factor-kappaB, plays a pivotal role in Drosophila development and innate immunity. TRAF6 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors
GIYVWKIKNFSNLRRSMEAGSPVVIHSPGFYTSPPGYKLCARLNLSLPEARCPNYISLFVHLMQGENDSH
LDWPFQGTITLTLLDQSEPRQNIHETMMSKPELLAFQRPTTDRNPKGFGYVEFAHIEDLLQRGFVKNDTL
LIKIEVN
>gnl|CDD|239746 cd03777, MATH_TRAF3, Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF3 subfamily, TRAF domain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF3 was first described as a molecule that binds the cytoplasmic tail of CD40. However, it is not required for CD40 signaling. More recently, TRAF3 has been identified as a key regulator of type I interferon (IFN) production and the mammalian innate antiviral immunity. It mediates IFN responses in Toll-like receptor (TLR)-dependent as well as TLR-independent viral recognition pathways. It is also a key element in immunological homeostasis through its regulation of the anti-inflammatory cytokine interleukin-10. TRAF3 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors
TGLLESQLSRHDQMLSVHDIRLADMDLRFQVLETASYNGVLIWKIRDYKRRKQEAVMGKTLSLYSQPFYT
GYFGYKMCARVYLNGDGMGKGTHLSLFFVIMRGEYDALLPWPFKQKVTLMLMDQGSSRRHLGDAFKPDPN
SSSFKKPTGEMNIASGCPVFVAQTVLENGTYIKDDTIFIKVIVDTS
>gnl|CDD|239747 cd03778, MATH_TRAF2, Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF2 subfamily, TRAF domain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF2 associates with the receptors TNFR-1, TNFR-2, RANK (which mediates differentiation and maturation of osteoclasts) and CD40 (which is important for the proliferation and activation of B cells), among others. It regulates distinct pathways that lead to the activation of nuclear factor-kappaB and Jun NH2-terminal kinases. TRAF2 also indirectly associates with death receptors through its interaction with TRADD (TNFR-associated death domain protein). It is involved in regulating oxidative stress or ROS-induced cell death and in the preconditioning of cells by sublethal stress for protection from subsequent injury. TRAF2 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors
AXADLEQKVLEXEASTYDGVFIWKISDFARKRQEAVAGRIPAIFSPAFYTSRYGYKMCLRIYLNGDGTGR
GTHLSLFFVVMKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPDVTSSSFQRPVNDMNIASGCPLFC
PVSKXEAKNSYVRDDAIFIKAIVD
>gnl|CDD|239748 cd03779, MATH_TRAF1, Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF1 subfamily, TRAF domain, C-terminal MATH subdomain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF1 expression is the most restricted among the TRAFs. It is found exclusively in activated lymphocytes, dendritic cells and certain epithelia. TRAF1 associates, directly or indirectly through heterodimerization with TRAF2, with the TNFR family receptors TNFR-2, CD30, RANK, CD40 and LMP1, among others. It also binds the intracellular proteins TRADD, TANK, TRIP, RIP1, RIP2 and FLIP. TRAF1 is unique among the TRAFs in that it lacks a RING domain, which is critical for the activation of nuclear factor-kappaB and Jun NH2-terminal kinase. Studies on TRAF1-deficient mice suggest that TRAF1 has a negative regulatory role in TNFR-mediated signaling events. TRAF1 contains one zinc finger and one TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors
GTFLWKITDVSQKQRESSHGRDVSLCSPAFYTAKYGYKVCLRLYLNGDGAGKGTHISLFFVIMKGEYDAL
LPWPFRHKVTFMLLDQNNREHVIDAFRPDLSSASFQRPVSDMNVASGCPLFFPLKKLQSPKHAYCKDDTI
YIKCVVD
>gnl|CDD|239749 cd03780, MATH_TRAF5, Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF5 subfamily, TRAF domain, C-terminal MATH subdomain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF5 was identified as an activator of nuclear factor-kappaB and a regulator of lymphotoxin-beta receptor and CD40 signaling. Its interaction with CD40 is indirect, involving hetero-oligomerization with TRAF3. In addition, TRAF5 has been shown to associate with other TNFRs including CD27, CD30, OX40 and GITR (glucocorticoid-induced TNFR). It plays a role in modulating Th2 immune responses (driven by OX40 costimulation) and T-cell activation (triggered by GITR). It is also involved in osteoclastogenesis. TRAF5 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors
GKLIWKVTDYKMKKKEAVDGHTVSIFSQPFYTSRCGYRLCARAYLNGDGSGKGTHLSLYFVVMRGEFDSL
LQWPFRQRVTLMLLDQSGKKNHIMETFKADPNSSSFKRPDGEMNIASGCPRFVAHSVLENAKNTYIKDDT
LFLKVAVD
>gnl|CDD|239750 cd03781, MATH_TRAF4, Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF4 subfamily, TRAF domain, C-terminal MATH subdomain; composed of proteins with similarity to human TRAF4, including the Drosophila protein DTRAF1. TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF4 is highly expressed during embryogenesis, especially in the central and peripheral nervous system. Studies using TRAF4-deficient mice show that TRAF4 is required for neurogenesis, as well as the development of the trachea and the axial skeleton. In addition, TRAF4 augments nuclear factor-kappaB activation triggered by GITR (glucocorticoid-induced TNFR), a receptor expressed in T-cells, B-cells and macrophages. It also participates in counteracting the signaling mediated by Toll-like receptors through its association with TRAF6 and TRIF. DTRAF1 plays a pivotal role in the development of eye imaginal discs and photosensory neuron arrays in Drosophila. TRAF4 contains a RING finger domain, seven zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors
GTLLWKITDYSRKLQEAKGRDNLELFSPPFYTHRYGYKLQVSAFLNGNGSGEGSHLSVYIRVLPGEYDNL
LEWPFSHRITFTLLDQSDPSLSKPQHITETFTPDPTWKNFQKPSASRLDESTLGFGYPKFISHEDLKKRN
YIKDDAIFLRASVE
>gnl|CDD|239751 cd03782, MATH_Meprin_Beta, Meprin family, Beta subunit, MATH domain; Meprins are multidomain extracellular metalloproteases capable of cleaving growth factors, cytokines, extracellular matrix proteins, and biologically active peptides. They are composed of two related subunits, alpha and beta, which form homo- or hetro-complexes where the basic unit is a disulfide-linked dimer. The beta subunit is a type I membrane protein, which forms homodimers or heterotetramers (alpha2beta2 or alpha3beta). Meprin beta shows preference for acidic residues at the P1 and P1' sites of its substrate. Among its best substrates are growth factors and chemokines such as gastrin and osteopontin. Both alpha and beta subunits contain a catalytic astacin (M12 family) protease domain followed by the adhesion or interaction domains MAM, MATH and AM. The MATH and MAM domains provide symmetrical intersubunit disulfide bonds necessary for the dimerization of meprin subunits. The MATH domain may also be required for folding of an activable zymogen
CPEHIWHIRNFTQLLATTPPNGKIYSPPFLSSTGYSFQVGLYLNGTDDYPGNLAIYLHLTSGPNDDQLQW
PCPWQQATMMLLDQHPDIRQRMSNQRSVTTDPNMTSTDSDEYFWDDPRKVGSEVTDTDGSTFYRGPGYGT
SAFITHLRLRSRDFIKGDDVIFLLTME
>gnl|CDD|239752 cd03783, MATH_Meprin_Alpha, Meprin family, Alpha subunit, MATH domain; Meprins are multidomain extracellular metalloproteases capable of cleaving growth factors, cytokines, extracellular matrix proteins, and biologically active peptides. They are composed of two related subunits, alpha and beta, which form homo- or hetro-complexes where the basic unit is a disulfide-linked dimer. The alpha subunit is synthesized as a membrane spanning protein, however, it is cleaved during biosynthesis and loses its transmembrane domain. It oligomerizes into large complexes, containing 10-100 subunits (dimers that associate noncovalently), which are secreted as latent proteases and can move through extracellular spaces in a nondestructive manner. This allows delivery of the concentrated protease to sites containing activating enzymes, such as sites of inflammation, infection or cancerous growth. Meprin alpha shows preference for small or hydrophobic residues at the P1 and P1' sites of its substrate. Both alpha and beta subunits contain a catalytic astacin (M12 family) protease domain followed by the adhesion or interaction domains MAM, MATH and AM. The MATH and MAM domains provide symmetrical intersubunit disulfide bonds necessary for the dimerization of meprin subunits. The MATH domain may also be required for folding of an activable zymogen
CPNAVWRVRNFSQILENTTKGDVLQSPRFYSPEGYGYGVSLYPLSNESDYSGNYTGLYFHLCSGENDAVL
EWPALNRQAIITVLDQDPDVRLRMSSSRSFTTDKSQTSSAINGTLRWDRPSRVGTYDTSCDCFRGIDFGW
STFISHSQLRRRSFLKNDDLIIFVDFE
>gnl|CDD|340817 cd03784, GT1_Gtf-like, UDP-glycosyltransferases and similar proteins. This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics
MRILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFNFADLVEAAGLTFVPVGDDPDELELDSETNLG
PDSLLELLRRLLKAADELLDDLLAALRSSWKPDLVIADPFAYAGPLVAEELGIPSVRLFTGPATLLSAYL
HPFGVLNLLLSSLLEPELFLDPLLEVLDRLRERLGLPPFSLVLLLLRLVPPLYVIGPTFPSLPPDRPRLP
SVLGGLRIVPKNGPLPDELWEWLDKQPPRSVVYVSFGSMVRDLPEELLELIAEALASLGQRFLWVVGPDP
LGGLERLPDNVLVVKWVPQDELLAHPAVGAFVTHGGWNSTLEALYAGVPMVVVPLFADQPNNAARVEELG
AGVELDKDELTAEELAKAVREVLEDESYRRAAELLAELREEDGAPSAADVVERL
>gnl|CDD|340818 cd03785, GT28_MurG, undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase. MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility
KILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKA
PFKLLKGLRQARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAV
SFPETKKYFPAAKVVVTGNPVREEILNLRKELKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLER
GIQVIHQTGKGDYDEVKKLYEDLGINVKVFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPY
PYAADDHQEANARALEKAGAAIVIDQEELTPEVLAEAILDLLNDPERLKKMAEAAKKLAKPDAAERIADL
>gnl|CDD|340819 cd03786, GTB_UDP-GlcNAc_2-Epimerase, UDP-N-acetylglucosamine 2-epimerase and similar proteins. Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility
KILTVTGTRPEAIKLAPVLRALKKDPGLELVLVVTGQHLDMLLGVLFFFILFLIKPDYDLDLMGDNQTLG
AKTGGLLIGLEEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSFDLGMPEEENRHRIDK
LSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALLSAALRIRDELVLSKLGLLEKKYILVTLHRREN
VDSGERLEELLEALEELAEKYDLIVVYPNHPRTRPRIREVGLKFLGGLPNIRLIDPLGYLDLVLLKKRAK
LVLTDSGGIQEEASFLGKPVLVLRDRTERPERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRMSAINP
YGDGNASERIVDILE
>gnl|CDD|340820 cd03788, GT20_TPS, trehalose-6-phosphate synthase. Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a glycosyltransferase that catalyses the synthesis of alpha,alpha-1,1-trehalose-6-phosphate from glucose-6-phosphate using a UDP-glucose donor. It is a key enzyme in the trehalose synthesis pathway. Trehalose is a nonreducing disaccharide present in a wide variety of organisms and may serve as a source of energy and carbon. It is characterized most notably in insect, plant, and microbial cells. Its production is often associated with a variety of stress conditions, including desiccation, dehydration, heat, cold, and oxidation. This family represents the catalytic domain of the TPS. Some members of this domain family coexist with a C-terminal trehalose phosphatase domain
RLIVVSNRLPVTLERDDDGEVEFRRSAGGLVTALKGLLKSTGGLWVGWPGIEADEEESDQVVSPELLEEY
NVVPVFLSDEDFEGYYNGFSNSVLWPLFHYLLPLPDGRFEREWWEAYVRVNQAFADAVVEVYRPGDLIWV
HDYHLLLLPQMLRERLPDARIGFFLHIPFPSSEIFRCLPWREEILRGLLGADLIGFQTFEYARHFLSCCS
RLLGLETTSAGGVEYGGRRVRVGAFPIGIDPDRFRRLAASPEVQERARELRERYKGKKLIVGVDRLDYTK
GIPEKLLAFERFLERYPEWRGKVVLVQVAVPSRTDVEEYQELRREVEELVGRINGRFGTLDWTPVVYLHQ
SLDREELLALYRAADVALVTSLRDGMNLVAKEYVACQRDNPGVLILSEFAGAASELDGAILVNPWDIEEV
AEAINRALTMSPEERKERHQKLRKYVETHDVQAWANSFLDDLA
>gnl|CDD|340821 cd03789, GT9_LPS_heptosyltransferase, lipopolysaccharide heptosyltransferase and similar proteins. Lipopolysaccharide heptosyltransferase (2.4.99.B6) is involved in the biosynthesis of lipooligosaccharide (LOS). Lipopolysaccharide (LPS) is a major component of the outer membrane of gram-negative bacteria. LPS heptosyltransferase transfers heptose molecules from ADP-heptose to 3-deoxy-D-manno-octulosonic acid (KDO), a part of the inner core component of LPS. This family also contains lipopolysaccharide 1,2-N-acetylglucosaminetransferase EC 2.4.1.56 and belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility
KILVIRLSALGDVVLTTPLLRALKKAYPDAKITVVVGPGYAELLELNPYIDEVIPDDKRRRAGLRGRRKL
LRELRARKYDLVIDLHSSLRSALLLLLSGAPRRIGFDREKRRFLLNHPVKPLVVIPPGASGPAKRWPAER
FAELADRLADEGYRVVLFGGPAEEELAEEIAAALGARVVNLAGKTSLRELAALLARADLVVGNDSGPMHL
AAALGTPTVALFGPTDPARTGPYGSNHVVVRADLPCSPCCPKRECPRGDHKCMRDITPEEVIEAIRR
>gnl|CDD|340822 cd03791, GT5_Glycogen_synthase_DULL1-like, Glycogen synthase GlgA and similar proteins. This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms
KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEVKVGGRGEEV
GVFELPVDGVDYYFLDNPEFFDRPGLPGPPGYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTA
LVPAYLKTRYRGPGFKKIKTVFTIHNLAYQGLFPLDTLAELGLPPELFHIDGLEFYGQINFLKAGIVYAD
RVTTVSPTYAKEILTPEYGEGLDGVLRARAGKLSGILNGIDYDEWNPATDKLIPANYSANDLEGKAENKA
ALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGK
VAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYDPETGEGTGF
VFEDYDAEALLAALRRALALYRNPELWRKLQKNAMKQDFSWDKSAKEYLELYRS
>gnl|CDD|340823 cd03792, GT4_trehalose_phosphorylase, trehalose phosphorylase and similar proteins. Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases
KVAHFSSTPQGGGVAEILHALVPLMRELGLDVRWYVIKGRPEFFNITKKFHNILQGVDKPELSEEDKEIY
LEWIEENASRYPLLDGDADVVVIHDPQPALLPKIKKKRDRKWIWRCHIDISTPLTEPQPRVWDFLWNYIE
GYDLFVFHPPEFVPPQVPPPKFYIPPSIDPLSGKNKDLSPADIRYYLEKPFVIDPERPYILQVARFDPSK
DPLGVIDAYKLFKRRAEEPQLVICGHGAVDDPEGSVVYEEVMEYAGDDHDIHVLRLPPSDQEINALQRAA
TVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAVRILRLLTDPELRRKM
GLAAREHVRDNFLITGNLRAWLYLIAKL
>gnl|CDD|340824 cd03793, GT3_GSY2-like, glycogen synthase GSY2 and similar proteins. Glycogen synthase, which is most closely related to the GT3 family of glycosyltransferases, catalyzes the transfer of a glucose molecule from UDP-glucose to a terminal branch of a glycogen molecule, a rate-limit step of glycogen biosynthesis. GSY2, the member of this family in S. cerevisiae, has been shown to possess glycogen synthase activity
NRFLFEVAWEVANKVGGIYTVIKSKAPVTVEEYGDNYCLIGPYNEATARTEVEILEPGNRPLRAALQSMR
SRGIKVHFGRWLIEGYPKVILFDIGSAAWKLDEWKGELWELCSIGIPWNDRETNDAIVFGYLVAWFLGEF
AAQFDPQPAVVAHFHEWQAGVGLILCRKRKVDVATIFTTHATLLGRYLCAGSVDFYNNLDSFDVDKEAGK
RGIYHRYCIERAAAHCAHVFTTVSEITAYEAEHLLKRKPDIVTPNGLNVVKFSAMHEFQNLHAQSKEKIN
EFVRGHFYGHLDFDLDKTLYFFTAGRYEFSNKGADMFIESLARLNYLLKVNGSETTVVAFIIMPAKTNNF
NVESLKGQAVTKQLKDTVNTVKEKIGKRIFESCLKGKLPDPEELLSKEDLVMLKRRIFALQRQSLPPIVT
HNMLDDANDPILNHIRRIQLFNSPEDRVKVIFHPEFLSSTNPLLGLDYEEFVRGCHLGVFPSYYEPWGYT
PAECTVMGIPSITTNLSGFGCFMEEHIEDPKSYGIYIVDRRFKSPDESVQQLTQYMYEFCQQSRRQRIIQ
RNRTERLSDLLDWRYLGRFYRKARQLALRR
>gnl|CDD|340825 cd03794, GT4_WbuB-like, Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase
KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGATETKDGIRVIRVKLGPIK
KNGLIRRLLNYLSFALAALLKLLVREERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLIA
LGVLKKGSLLKLLKKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPKDELRK
KLGLDDKFVVVYAGNIGKAQGLETLLEAAERLKRRPDIRFLFVGDGDEKERLKELAKARGLDNVTFLGRV
PKEEVPELLSAADVGLVPLKDNPANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPE
ALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRLL
>gnl|CDD|340826 cd03795, GT4_WfcD-like, Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes
KVLHVFKFYYPDIGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIRIHRVKSFLNVASTPFS
PSYIKRFKKLAKEYDIIHYHFPNPLADLLLFFSGAKKPVVVHWHSDIVKQKKLLKLYKPLMTRFLRRADR
IIATSPNYVETSPTLREFKNKVRVIPLGIDKNVYNIPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLI
EAAQYLNYPIVIGGEGPLKPDLEAQIELNLLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVLRSEAFGIVL
LEAMMCGKPVISTNIGTGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFT
AEKMK
>gnl|CDD|340827 cd03796, GT4_PIG-A-like, phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder
RICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVITHAYGNRVGVRYLTNGLKVYYLPFKVFYNQSTL
PTLFSTFPLLRNILIRERIQIVHGHQAFSSLAHEALFHARTLGLKTVFTDHSLFGFADASSILTNKLLRF
SLADIDHVICVSHTSKENTVLRASLDPRIVSVIPNAVDSSDFTPDPSKPDPNKITIVVISRLVYRKGIDL
LVGIIPRICKKHPNVRFIIGGDGPKRIELEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTE
AFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPDPEDIVRKLEEAISILRTGKHDPWSFHNRVKK
MYSWEDVARRTEKVYDRILSTPNRPFLERLKRYYNCGPIAGKIFCLLA
>gnl|CDD|340828 cd03798, GT4_WlbH-like, Bordetella parapertussis WlbH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS
VLILTNIYPNANSPGRGIFVRRQVRALSRRGVDVEVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLK
PRLRLLAPLRAPSLAKLLKRRRRGPPDLIHAHFAYPAGFAAALLARLYGVPYVVTEHGSDINVFPPRSLL
RKLLRWALRRAARVIAVSKALAEELVALGVPRDRVDVIPNGVDPARFQPEDRGLGLPLDAFVILFVGRLI
PRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVF
VLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALAEPYLRELGE
AARARVAERFSWVKAADRIAAAYRDV
>gnl|CDD|340829 cd03799, GT4_AmsK-like, Erwinia amylovora AmsK and similar proteins. This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor
KIAFIVDEFPVLSETFILNQITGLIDRGHEVDIYAVNPGDLVKRHPDVEKYNVPSLNLLYAIVGLNKKGA
YDIIHCQFGPLGALGALLRRLKVLKGKLVTSFRGYDISMYVILEGNKVYPQLFAQGDLFLPNCELFKHRL
IALGCDEKKIIVHRSGIDCNKFRFKPRYLPLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQI
IGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTAADGDQDGPPNTLKEAMAMG
LPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDINKLNDEL
>gnl|CDD|340830 cd03800, GT4_sucrose_synthase, sucrose-phosphate synthase and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light
RIALISVHGSPLAQPGGADTGGQNVYVLELARALAELGYQVDIFTRRISPADPEVVEIAPGARVIRVPAG
PPEYLPKEELWPYLEEFADGLLRFIAREGGRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHSLGRVKYR
HLGAQDTYHPSLRITAEEQILEAADRVIASTPQEADELISLYGADPSRINVVPPGVDLERFFPVDRAEAR
RARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGGPSDDPLSMDREELAELAEELG
LIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLV
DPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQLLT
>gnl|CDD|340831 cd03801, GT4_PimA-like, phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea
KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRL
LRELRPLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLARAEALLRR
ADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLL
LEALAKLLRRGPDVRLVIVGGDGPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGF
GLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAE
RFSWERVAERLLDLYR
>gnl|CDD|340832 cd03802, GT4_AviGT4-like, UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue
RIAQVSPPRGPVPPGKYGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSAPLVAVIPRALRLDPIPQESK
LAELLEALEVQLRASDFDVIHNHSYDWLPPFAPLIGTPFVTTLHGPSIPPSLAIYAAEPPVNYVSISDAQ
RAATPPIDYLTVVHNGLDPADYRFQPDPEDYLAFLGRIAPEKGLEDAIRVARRAGLPLKIAGKVRDEDYF
YYLQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQ
HGETGFLVDSVEEMAEAIANIDRIDRAACRRYAEDRFSAARMADRYEALYRKV
>gnl|CDD|340833 cd03804, GT4_WbaZ-like, mannosyltransferase WbaZ and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity
KVAIVHDWLVNYGGAERVLEALLELFPQADIYTLVDFLDKDDRLFIRGKKVRTSFIQKLPKAKRKYRKYL
PLMPLAIEQFDLSGYDLVISSSHAVAKGVLTRPDQLHVCYVHSPIRYAWDLYHQYLAESGLGKGIKSLLA
SLFLHYLRLWDVRTAQRVDLFIANSQFVARRIKKFYGRESTVIYPPVDTDAFAPAADKEDYYLTASRLVP
YKRIDLAVEAFNELPKRLVVIGDGPDLDRLRAMASPNVEFLGYQPDEVLKELLSKARAFVFAAEEDFGIV
PVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEFEQNFDRFKPQAIRANAERFSRAR
FRQEIR
>gnl|CDD|340834 cd03805, GT4_ALG2-like, alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans
LRVAFLHPDLGIGGAERLVVDAALALQSRGHEVTIYTSHHDPSHCFEETKDGTLPVRVRGDWLPRSIFGR
FHALCAYLRMLYLALYLLLFSGEKYDVFIVDQVSACVPLLKLFRPSKILFYCHFPDQLLAQRKSLLKRLY
RKPFDWLEEFTTGMADQIVVNSNFTAGVFKKTFPSLAKNPPEVLYPCVDTDSFDSTSEDPDPGDLIAKSN
KKFFLSINRFERKKNIALAIEAFAKLKQKLPEFENVRLVIAGGYDPRVAENVEYLEELQRLAEELLNVED
QVLFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEPT
PEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAERL
>gnl|CDD|340835 cd03806, GT4_ALG11-like, alpha-1,2-mannosyltransferase ALG11 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides
ITVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFF
LLKYRKLVEAKTYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPT
ISTDMLNKVRSREASYNNDSTIARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKR
NIKPSIVYPPCDTEELTKLPIDEKTRENQILSIAQFRPEKNHPLQLRAFAELLKRLPESIRSNPKLVLIG
SCRNEEDKERVEALKLLAKELILEDSVEFVVDAPYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLI
PLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILTLSEEERLQRREAARSSAERFSDEEFERD
>gnl|CDD|340836 cd03807, GT4_WbnK-like, Shigella dysenteriae WbnK and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis
KVAHVITGLNVGGAETMLLRLLEHMDKSRFEHVVISLTGDGVLGEELLAAGVPVVCLGLSSGKDPGVLLR
LAKLIRKRNPDVVHTWMYHADLIGGLAAKLAGGVKVIWSVRSSNIPQRLTRLVRKLCLLLSKFSPATVAN
SSAVAEFHQEQGYAKNKIVVIYNGIDLFKLSPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLR
AAALLVETHPDLRLLLVGRGPERPNLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNA
LLEAMACGLPVVATDVGGAAELVDDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSI
DAMVRRYETLYY
>gnl|CDD|340837 cd03808, GT4_CapM-like, capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides
KILFIVNVDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKELGVKVIDIPILRRGINPLKDLKAL
FKLYKLLKKEKPDIVHCHTPKPGILGRLAARLAGVPKVIYTVHGLGFVFTEGKLLRLLYLLLEKLALLFT
DKVIFVNEDDRDLAIKKGIIKKKKTVLIPGSGVDLDRFQYSPESLPSEKVVFLFVARLLKDKGIDELIEA
AKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSL
LEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDE
EKVVNKLL
>gnl|CDD|340838 cd03809, GT4_MtfB-like, glycosyltransferases MtfB, WbpX, and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide
KILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELA
LLRWLQILLPKKDKPDLLHSPHNTAPLLLKGCPQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPISLRRAD
AIITVSEATRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERL
LKAFALLKKQGGDLKLVIVGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYE
GFGLPVLEAMACGTPVIASNISVLPEVAGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKK
FSWEKTAEKTLE
>gnl|CDD|340839 cd03811, GT4_GT28_WabH-like, family 4 and family 28 glycosyltransferases similar to Klebsiella WabH. This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core
KILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLK
AILKLKRILKRAKPDVVISFLGFATYIVAKLAAARSKVIAWIHSSLSKLYYLKKKLLLKLKLYKKADKIV
CVSKGIKEDLIRLGPSPPEKIEVIYNPIDIDRIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAF
AKLRKKYPDVKLVILGDGPLREELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLL
EAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEAVFREYT
I
>gnl|CDD|340840 cd03812, GT4_CapH-like, capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1)
KILHIVGGMNVGGIETFLMNLYRKLDKSKIEFDFLATSDDKGEYDEELEELGGKIFYIPPKKKNIIKYFI
KLLKLIKKEKYDIVHVHGSSSNGIILLLAAKAGVPVRIAHSHNTKDSSIKLRKIRKNVLKKLIERLSTKY
LACSEDAGEWLFGEVENGKFKVIPNGIDIEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLI
DIFEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPL
VAVEAQASGLPCLLSDTITKECDITNNVEFLPLNETPSTWAEKILKLIKRKRRINKEINKEKKELGYDDE
SLELTLL
>gnl|CDD|340841 cd03813, GT4-like, glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes
DIGLLLEGTYPYVRGGVSSWVHQLITGLPEHEFAVYFIGGREETYGEIKYEIPPNVVHVEEHPLWERLDD
GSFSGGSSQKANLENLEREGTQLEEGQPILEADRFAIDLLRESELKRDGSLTDFLYSKASWDILLEAYLE
YCTEPSFLDYFWTLRNMLLPLFKLAIAADDLPEADLYHSVSTGYAGLLGALARHRRGIPFLLTEHGIYTR
ERKIEILQSTWIMGYIKKLWIRFFERLGKLAYQQADKIISLYEGNRRRQIRLGADPDKTRVIPNGIDIQR
FAPAREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIGPEDEDPEYAQECKRLVASL
GLENKVKFLGFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIYGADDALGQAG
LVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL
>gnl|CDD|340842 cd03814, GT4-like, glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes
RIALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVAPGPFDEAESAEGRVVSVPSFPLPFYPEYRLAL
PLPRRVRRLIKEFQPDIIHIATPGPLGLAALRAARRLGLPVVTSYHTDFPEYLSYYTLGPLSWLAWAYLR
WFHNPFDTTLVPSPSIARELEGHGFERVRLWPRGVDTELFHPSRRDAALRRRLGPPGRPLLLYVGRLAPE
KNLEALLDADLPLAASPPVRLVVVGDGPARAELEARGPDVIFTGFLTGEELARAYASADVFVFPSRTETF
GLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAER
YSWEAFLDNLLDYYA
>gnl|CDD|340843 cd03816, GT33_ALG1-like, chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins. This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik
PKKKRVCVLVLGDIGRSPRMQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPTKNKLPF
LLFAPLKVLLQALSLLWLLYELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLG
ENHPLVRLAKWYEKTFGRMADAHLCVTKAMQRDLQQFENWNIRATVLYDRPPSHFRPIPLEEKHELFLEL
ALFRELAEGAVSYKEGRPALLVSSTSWTPDEDFSILLDALKAYESSAATEPALLPSLLCIITGKGPLKEM
YLELIKELKLKKVTIRTPWLSAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIG
ELVKHGVNGLVFGDSEELAEQLIDLLSDFDRGKLNVLKKGAQEESENRWDENWDRVAGPLF
>gnl|CDD|340844 cd03817, GT4_UGDG-like, UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol
KIAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEEVVRYRSFSIPIRKYHRQHIPF
PFKKAVIDRIKELGPDIIHTHTPFSLGKLGLRIARKLKIPIVHTYHTMYEDYLHYIPKGKLLVKAVVRKL
VRRFYNHTDAVIAPSEKIKDTLREYGVKGPIEVIPNGIDLDKFEKPLNTEERRKLGLPPDEPILLYVGRL
AKEKNIDFLLRAFAELKKEPNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLF
VFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDETLAEKLLHLRENLELLRKLSK
NAEISAREFAFAKSVEKLYEEV
>gnl|CDD|340845 cd03818, GT4_ExpC-like, Rhizobium meliloti ExpC and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II)
NILFVHQNFPGQFKHLARHLARQPGNEVTFLTRRNDQGIPGVRPVRYRPFRGVASPLEGHRYVRDFEEGV
LRGQAVLRALLALKREGFRPDVVVGHPGWGEALFVKDVFPDVPLIGYCEYYYRAEGADVGFDPEFPLDLM
IRCRLRNRNIALLLSLEQADLGVTPTRWQRSLFPAAYRDRISVIHDGVDTDRLAPDPAARLRLLNGTELK
AGDPVITYVARNLEPYRGFHVFMRALPRIQARRPDARVVVVGGDGVSYGSPPPDGGSWKQKMLAELGVDL
ERVHFVGKVPYDQYVRLLQLSDAHVYLTYPFVLSWSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDF
FDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCLARYLA
>gnl|CDD|340846 cd03819, GT4_WavL-like, Vibrio cholerae WavL and similar sequences. This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core
ILMLTPALEIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGIGLPGLKVPLLRALLGNVRLAR
LIRRERIDLIHAHSRAPAWLGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVRARGDRVIAVSELVRDH
LIEALGVDPERIRVIPNGVDTDRFPPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDE
PDFRLLVAGDGPERDEIRRLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGT
PVVATDVGGAREIVVHGRTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAALTEAVRELLLRV
>gnl|CDD|340847 cd03820, GT4_AmsD-like, amylovoran biosynthesis glycosyltransferase AmsD and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran
KIAIVIPSISNAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYELDDNIKIKNLGDRKYSHFKLLL
KYFKKVRRLRKYLKNNKPDVVISFRTSLLTFLALIGLKSKLIVWEHNNYEAYNKGLRRLLLRRLLYKRAD
KIVVLTEADKLKKYKQPNSNVVVIPNPLSFPSEEPSTNLKSKRILAVGRLTYQKGFDLLIEAWALIAKKH
PDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGL
PIISFDCPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAERFSIEKIIKQWE
E
>gnl|CDD|340848 cd03821, GT4_Bme6-like, Brucella melitensis Bme6 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide
KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEENGRYIPPQDGFASIPLLRQG
AGRTDFSPGLPNWLRRNLREYDVVHIHGVWTYTSLAACKLARRRGIPYVVSPHGMLDPWALQQKHWKKRI
ALHLIERRNLNNAALVHFTSEQEADELRRFGLEPPIAVIPNGVDIPEFDPGLRDRRKHNGLEDRRIILFL
GRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYA
SADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAGCGVVVDPNVSSLAEALAEALRDPADRK
RLGEMARRARQVEENFSWEAVAGQLGE
>gnl|CDD|340849 cd03822, GT4_mannosyltransferase-like, mannosyltransferases of glycosyltransferase family 4 and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides
KIAVLGTLPPRKCGIATYTDDLVEGLRKGGPVVIVVIVSPQDEILKDDDFEVPNEIKSWNSNEYFRLLDH
LNFKKPDVVHIQHEFGIFGGKYGLYALGLLLHLRIPVITTLHTVLDLSDPGKQALKVLFRIATLSERVVV
MAPISRFLLVRIKLIPAVNIEVIPHGVPEVPQDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALP
ELKAEFPDVRLVIAGELHPSLARYEGERYRKAAIEELGLQDHVDFHNNFLPEEEVPRYISAADVVVLPYL
NTEQSSSGTLSYAIACGKPVISTPLRHAEELLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAY
AYARAMTWESIADRYLRLFN
>gnl|CDD|340850 cd03823, GT4_ExpE7-like, glycosyltransferase ExpE7 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II)
KILLVNSLYPPQRVGGAEISVHDLAEALVAEGHEVAVLTAGVGPPGQATVARSVVRYRRAPDETLPLALK
RRGYELFETYNPGLRRLLARLLEDFRPDVVHTHNLSGLGASLLDAARDLGIPVVHTLHDYWLLCPRQFLF
KKGGDAVLAPSRFTANLHEANGLFSARISVIPNAVEPDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLV
EAFKRLPREDIELVIAGHGPLSDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPFGLVVRE
AIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEE
YLKLYRD
>gnl|CDD|340851 cd03825, GT4_WcaC-like, putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis
MKVLHINTVDLSGGAARAAYRLHQALLAYGIDSTMLVGRKKNLISKPEFIEADIIHLHWIHGGYLSLKAL
FKLLRRKPVVWTLHDMWPFTGGCHYPMECEGWKTGCGNCPNLNSYPPAKKDLSRQLFRRKREALAKKRLT
IVAPSRWLADMVRRSPLLKGLPVVVIPNGIDTEIFAPVDKAKARKRLGIPQDKKVILFGAESVTKPRKGF
DELIEALKLLATKDDLLLVVFGKNDPQIVILPFDIISLGYIDDDEQLVDIYSAADLFVHPSLADNLPNTL
LEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQ
RVQAQRYLELYKDL
>gnl|CDD|239753 cd03829, Sina, Seven in absentia (Sina) protein family, C-terminal substrate binding domain; composed of the Drosophila Sina protein, the mammalian Sina homolog (Siah), the plant protein SINAT5, and similar proteins. Sina, Siah and SINAT5 are RING-containing proteins that function as E3 ubiquitin ligases, acting either as single proteins or as a part of multiprotein complexes. Sina is expressed in many cells in the developing eye but is essential specifically for R7 photoreceptor cell development. Sina cooperates with Phyllopod (Phyl), Ebi and the E2 ubiquitin-conjugating enzyme Ubcd1 to catalyze the ubiquitination and subsequent degradation of Tramtrack (Ttk88); Ttk88 is a transcriptional repressor that blocks photoreceptor differentiation. Similarly, the mammalian homologue Siah1 cooperates with SIP (Siah-interacting protein), Ebi and the adaptor protein Skp1, to target beta-catenin for ubiquitination and degradation via a p53-dependent mechanism. SINAT5 targets NAC1 for ubiquitin-mediated degradation resulting in the downregulation of auxin, a hormone that controls many aspects of plant development. Other targets of Sina family proteins include c-Myb, synaptophysin, group 1 glutamate receptors, promyelocytic leukemia protein, alpha-synuclein, synphilin-1 and alpha-ketoglutarate dehydrogenase, among others. Sina proteins also bind proteins that are not targets for ubiquitination such as Phyl, adenomatous polyposis coli, VAV, BAG-1 and Dab-1. Siah binds to a consensus motif, PXAXVXP, which is present in Siah-binding proteins. Siah is a dimeric protein consisting of an N-terminal RING domain, two zinc finger motifs and a C-terminal substrate-binding domain (SBD); this SBD contains an eight-stranded antiparallel beta-sandwich fold similar to the MATH (meprin and TRAF-C homology) domain
VTTLQGEDIVFLATDINLPGATDWVMMQSCFGHHFMLVLEKQELYEGHQQFFAFVQLIGTEKQAENFTYR
LELNGNRRRLTWEATPRSIREGHASVIDNSDCLVFDTSIAQLFSENGNLGINVTISG
>gnl|CDD|349428 cd03855, M14_ASTE, Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily. Peptidase M14 Succinylglutamate desuccinylase (ASTE, also known as N-succinyl-L-glutamate amidohydrolase, N2-succinylglutamate desuccinylase, and SGDS; EC 3.5.1.96) belongs to the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily of the M14 family of metallocarboxypeptidases. This group includes succinylglutamate desuccinylase that catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway. It hydrolyzes N-succinyl-L-glutamate to succinate and L-glutamate
DFLALTLSGSEPAEGELAAVSNGTRVRWLATGVLELTPAASASKSVVLSAGIHGNETAPIEILDQLINDL
IRGELALAHRLLFIFGNPPAIRQGKRFIEENLNRLFSGRHSKLPPSYETARAAELEQAVADFFAKASGEV
RWHLDLHTAIRGSKHEQFAVYPFLEGRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTV
ELGKVRPFGQNDLSQFAAIDQALRALISG
>gnl|CDD|349429 cd03856, M14_Nna1-like, Peptidase M14-like domain of ATP/GTP binding proteins, cytosolic carboxypeptidases and related proteins. Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP), and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This subfamily includes the human AGTPBP-1 and AGBL -2, -3, -4, and -5, and the mouse Nna1/CCP-1 and CCP -2 through -6. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Nna1 is widely expressed in the developing and adult nervous systems, including cerebellar Purkinje and granule neurons, miral cells of the olfactory bulb and retinal photoreceptors. Nna1 is also induced in axotomized motor neurons. Mutations in Nna1 cause Purkinje cell degeneration (pcd). The Nna1 CP domain is required to prevent the retinal photoreceptor loss and cerebellar ataxia phenotypes of pcd mice, and a functional zinc-binding domain is needed for Nna-1 to support neuron survival in these mice. Nna1-like proteins from the different phyla are highly diverse, but they all contain a characteristic N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain
HYARWLNLIATQPLVQLLEIGVTEQGREIQALQSLRTERSDDKSWLFLIARQHPGETTGAWVFFGFLDQL
LSDDDPAQQLRAEYNFYIIPMVNPDGVARGHWRTNSRGMDLNRDWHAPDALLSPETYAVAAALAERVQSP
EGVVLALDLHGDNRNVFLTGPDNKDESTNHNPDKLNSLLTETDRRLPDYNTEASPGDNPGGTVGKQWIAD
VYQITHSVTLEVGDNTDRSVASSRYTPGEIELVAKTAATALL
>gnl|CDD|349430 cd03857, M14-like, Peptidase M14-like domain; uncharacterized subfamily. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
TVLLAAQIHGNETTGTEALMELIRDLASESDEAAKLLDNIVILLVPQLNPDGAELFVNFYLDSMNGLPGT
RYNANGIDLNRDHVKLTQPETQAVAENFIHWWPDIFIDLHEQVGASIPYPTPPDAPNYNLVDLRSDAENG
QEHIRLIAGEGSGELGKYFSPMRGGFDDSTGGNGIGRTSGFHGAISILFEVPGQPNYYRRVSG
>gnl|CDD|349431 cd03858, M14_CP_N-E_like, Peptidase M14 carboxypeptidase subfamily N/E-like. Carboxypeptidase (CP) N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes eight members, of which five (CPN, CPE, CPM, CPD, CPZ) are considered enzymatically active, while the other three are non-active (CPX1, PCX2, ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily, enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form; rather, they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition, all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation
HHNYEELEEFLKQVAKRYPNITRLYSIGKSVEGRELWVLEISDNPGVHEPGEPEFKYVANMHGNEVVGRE
LLLLLAEYLCENYGKDPRVTQLVNSTRIHIMPSMNPDGYEKAQEGDCGGLIGRNNANGVDLNRNFPDQFF
QVYSDNNPRQPETKAVMNWLESIPFVLSANLHGGALVANYPYDDTRSGKSTEYSPSPDDAVFRMLARSYS
DAHPTMSMGKPCCCDDDENFPNGITNGAAWYSVSGGMQDFNYLHTNCFEITLELGCCKYPPASELPKYWE
DNKRSLLNFLEQ
>gnl|CDD|349432 cd03859, M14_CPT, Peptidase M14 Carboxypeptidase T subfamily. Peptidase M14-like domain of carboxypeptidase (CP) T (CPT), CPT belongs to the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPT has moderate similarity to CPA and CPB, and exhibits dual-substrate specificity by cleaving C-terminal hydrophobic amino acid residues like CPA and C-terminal positively charged residues like CPB. CPA and CPB are M14 family peptidases but do not belong to this CPT group. The substrate specificity difference between CPT and CPA and CPB is ascribed to a few amino acid substitutions at the substrate-binding pocket while the spatial organization of the binding site remains the same as in all Zn-CPs. CPT has increased thermal stability in presence of Ca2+ ions, and two disulfide bridges which give an additional stabilization factor
DGGYHTYAELVAELDQLAAEYPEITKLISIGKSVEGRPIWAVKISDNPDEDEDEPEVLFMGLHHAREWIS
LEVALYFADYLLENYGTDPRITNLVDNREIWIIPVVNPDGYEYNRETGGGRLWRKNRRPNNGNNPGSDGV
DLNRNYGYHWGGDNGGSSPDPSSETYRGPAPFSEPETQAIRDLVESHDFKVAISYHSYGELVLYPWGYTS
DAPTPDEDVFEELAEEMASYNGGGYTPQQSSDLYPTNGDTDDWMYGEKGIIAFTPELGPEFYPFYPPPSQ
IDPLAEENLPAA
>gnl|CDD|349433 cd03860, M14_CP_A-B_like, Peptidase M14 carboxypeptidase subfamily A/B-like. The Peptidase M14 Carboxypeptidase (CP) A/B subfamily is one of two main M14 CP subfamilies defined by sequence and structural homology, the other being the N/E subfamily. CPs hydrolyze single, C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1, CPA2, CPA3, CPA4, CPA5, CPA6, CPB, CPO and CPU. CPA1, CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 is detected in hormone-regulated tissues, and is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues, and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle, suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor, PCPU, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues
YHPLDDIVQWLDDLAAAFPDNVEIFTIGKSYEGRDITGIHIWGSGGKGGKPAIVIHGGQHAREWISTSTV
EYLAHQLLSGYGSDATITALLDKFDFYIIPVVNPDGYVYTWTTDRLWRKNRQPTGGSSCVGIDLNRNWGY
KWGGPGASTNPCSETYRGPSAFSAPETKALADFINALAAGQGIKGFIDLHSYSQLILYPYGYSCDAVPPD
LENLMELALGAAKAIRAVHGTTYTVGPACSTLYPASGSSLDWAYDVAKIKYSYTIELRDTGTYGFLLPPE
QILPTGEETWAGVKYLADFI
>gnl|CDD|349434 cd03862, M14-like, Peptidase M14-like domain; uncharacterized subfamily. A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
PVVGLVGGVHGLERIGTQVILAFLRSLLARLKWDKLLQELLEEVRLVVIPIVNPGGMALKTRSNPNGVDL
MRNAPVEAVEKVPFLVGGQRISPHLPWYRGRNGLETESQALIRYVNEHLLESKMSISLDCHSGFGLVDRI
WFPYAHTTEPFPNLAEIFALIQLFRTSYPHHFLYRFEPQSRSYTTHGDLWDYLYDEHQSQQPSGIFLPLT
LEMGSWLWVKKNPRQIFRKHGIFNPIKAHRQQRIL
>gnl|CDD|349435 cd03863, M14_CPD_II, Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain II subgroup. The second carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; EC 3.4.17.22), domain II. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, while the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans-Golgi network and immature secretory vesicles, but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans-Golgi network, such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down -regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop
IQPVDFRHHHFSDMEIFLRRYANEYPSITRLYSVGKSVELRELYVMEISDNPGVHEPGEPEFKYIGNMHG
NEVVGRELLLNLIEYLCKNFGTDPEVTDLVQNTRIHIMPSMNPDGYEKSQEGDRGGTVGRNNSNNYDLNR
NFPDQFFQITDPPQPETLAVMSWLKTYPFVLSANLHGGSLVVNYPFDDDEQGLATYSKSPDDAVFQQLAL
SYSKENSKMYQGSPCKELYPNEYFPHGITNGAQWYNVPGGMQDWNYLNTNCFEVTIELGCVKYPKAEELP
KYWEQNRRSLLQFIKQ
>gnl|CDD|349436 cd03864, M14_CPN, Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase N subgroup. Peptidase M14 Carboxypeptidase N (CPN, also known as kininase I, creatine kinase conversion factor, plasma carboxypeptidase B, arginine carboxypeptidase, and protaminase; EC 3.4.17.3) is an extracellular glycoprotein synthesized in the liver and released into the blood, where it is present in high concentrations. CPN belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPN plays an important role in protecting the body from excessive buildup of potentially deleterious peptides that normally act as local autocrine or paracrine hormones. It specifically removes C-terminal basic residues. As CPN can cleave lysine more avidly than arginine residues it is also called lysine carboxypeptidase. CPN substrates include peptides found in the bloodstream, such as kinins (e.g. bradykinin, kalinin, met-lys-bradykinin), complement anaphylatoxins and creatine kinase MM (CK-MM). By removing just one amino acid, CPN can alter peptide activity and receptor binding. For example Bradykinin, a nine-residue peptide released from kiningen in response to tissue injury which is inactivated by CPN, anaphylatoxins which are regulated by CPN by the cleaving and removal of their C-terminal arginines resulting in a reduction in their biological activities of 10-100-fold, and creatine kinase MM, a cytosolic enzyme that catalyzes the reversible transfer of a phosphate group from ATP to creatine, and is regulated by CPN by the cleavage of C-terminal lysines. Like the other N/E subfamily members, two surface loops surrounding the active-site groove restrict access to the catalytic center, thus restricting larger protein carboxypeptidase inhibitors from inhibiting CPN
HHRYDDLVRALYAVQNECPYITRIYSIGRSVEGRHLYVLEFSDNPGIHEPLEPEFKYVGNMHGNEVLGRE
LLIQLSEFLCEEYRNGNERITRLIQDTRIHILPSMNPDGYEVAARQGPEFNGYLVGRNNANGVDLNRNFP
DLNTLMYYNEKYGGPNHHLPLPDNWKSQVEPETLAVIQWMQNYNFVLSANLHGGAVVANYPYDKSREPRV
RGFRRTAYSPTPDDKLFQKLAKTYSYAHGWMHKGWNCGDYFDEGITNGASWYSLSKGMQDFNYLHTNCFE
ITLELSCDKFPPEEELEREWLGNREALISYMEQ
>gnl|CDD|349437 cd03865, M14_CPE, Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase E subgroup. Peptidase M14 Carboxypeptidase (CP) E (CPE, also known as carboxypeptidase H, and enkephalin convertase; EC 3.4.17.10) belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPE is an important enzyme responsible for the proteolytic processing of prohormone intermediates (such as pro-insulin, pro-opiomelanocortin, or pro-gonadotropin-releasing hormone) by specifically removing C-terminal basic residues. In addition, it has been proposed that the regulated secretory pathway (RSP) of the nervous and endocrine systems utilizes membrane-bound CPE as a sorting receptor. A naturally occurring point mutation in CPE reduces the stability of the enzyme and causes its degradation, leading to an accumulation of numerous neuroendocrine peptides that result in obesity and hyperglycemia. Reduced CPE enzyme and receptor activity could underlie abnormal placental phenotypes from the observation that CPE is down-regulated in enlarged placentas of interspecific hybrid (interspecies hybrid placental dysplasia, IHPD) and cloned mice
YHRYPELREALVSVWLQCPAISRIYTVGRSFEGRELLVIEVSDNPGEHEPGEPEFKYVGNMHGNEAVGRE
LLIFLAQYLCNEYQKGNETIINLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFP
DLDRIVYVNEKEGGPNNHLLKNMKKAVDQNTKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETR
SGSAHEYSSCPDDAIFQSLARAYSSLNPAMSDPNRPPCRKNDDDSSFVDGTTNGGAWYSVPGGMQDFNYL
SSNCFEITVELSCEKFPPEETLKGYWEDNKNSLINYIEQ
>gnl|CDD|349438 cd03866, M14_CPM, Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase M subgroup. Peptidase M14 Carboxypeptidase (CP) M (CPM) belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPM is an extracellular glycoprotein, bound to cell membranes via a glycosyl-phosphatidylinositol on the C-terminus of the protein. It specifically removes C-terminal basic residues such as lysine and arginine from peptides and proteins. The highest levels of CPM have been found in human lung and placenta, but significant amounts are present in kidney, blood vessels, intestine, brain, and peripheral nerves. CPM has also been found in soluble form in various body fluids, including amniotic fluid, seminal plasma and urine. Due to its wide distribution in a variety of tissues, it is believed that it plays an important role in the control of peptide hormones and growth factor activity on the cell surface and in the membrane-localized degradation of extracellular proteins, for example it hydrolyses the C-terminal arginine of epidermal growth factor (EGF) resulting in des-Arg-EGF which binds to the EGF receptor (EGFR) with an equal or greater affinity than native EGF. CPM is a required processing enzyme that generates specific agonists for the B1 receptor
YHNQEQMETYLKDVNKNYPSITHLHSIGKSVEGRDLWVLVLGRFPTKHRIGIPEFKYVANMHGDEVVGRE
LLLHLIEFLVTSYGSDPVITRLINSTRIHIMPSMNPDGFEATKKPDCYYTKGRYNKNGYDLNRNFPDAFE
ENNVQRQPETRAVMDWIKNETFVLSANLHGGALVASYPFDNGNSGTGQLGYYSVSPDDDVFIYLAKTYSY
NHTNMYKGIECSNSQSFPGGITNGYQWYPLQGGMQDYNYVWGQCFEITLELSCCKYPPEETLPQFWNDNR
VALIEYIKQ
>gnl|CDD|349439 cd03867, M14_CPZ, Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase Z subgroup. Peptidase M14-like domain of carboxypeptidase (CP) Z (CPZ), CPZ belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPZ is a secreted Zn-dependent enzyme whose biological function is largely unknown. Unlike other members of the N/E subfamily, CPZ has a bipartite structure, which consists of an N-terminal cysteine-rich domain (CRD) whose sequence is similar to Wnt-binding proteins, and a C-terminal CP catalytic domain that removes C-terminal Arg residues from substrates. CPZ is enriched in the extracellular matrix and is widely distributed during early embryogenesis. That the CRD of CPZ can bind to Wnt4 suggests that CPZ plays a role in Wnt signaling
HHSYSQMVRVLKKTAARCAHIARTYSIGRSFEGKDLLVIEFSSNPGQHELLEPEVKYIGNMHGNEVVGRE
MLIYLAQYLCSEYLLGNPRIQTLINTTRIHLLPSMNPDGYEVAAEEGAGYNGWTSGRQNAQNLDLNRNFP
DLTSEAYRLARTRGARLDHIPIPQSYWWGKVAPETKAVMKWMRSIPFVLSASLHGGDLVVSYPYDFSKHP
LEEKMFSPTPDEKMFKLLAKAYADAHPMMSDRSENRCGGNFLKRGGIINGAEWYSFTGGMADFNYLHTNC
FEVTVELGCEKFPPEEELYTIWQENKEALLNFMEM
>gnl|CDD|349440 cd03868, M14_CPD_I, Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain I subgroup. The first carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; EC 3.4.17.22), domain I. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. This Domain I family contains two contiguous surface cysteines that may become palmitoylated and target the enzyme to membranes, thus regulating intracellular trafficking. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans Golgi network and immature secretory vesicles, but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans Golgi network, such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down-regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop. In D. melanogaster, the CPD variant 1B short (DmCPD1Bs) is necessary and sufficient for viability of the fruit fly
YHNYDELTDLLHKLAETYPNIAKLHSIGKSVQGRELWVLEISDNVNRREPGKPMFKYVANMHGDETVGRQ
LLIYLAQYLLENYGKDERVTRLVNSTDIHLMPSMNPDGFENSKEGDCSGDPGYGGRENANNVDLNRNFPD
QFEDSDDRLLEGRQPETLAMMKWIVENPFVLSANLHGGSVVASYPFDDSPSHIECGVYSKSPDDAVFRHL
AHTYADNHPTMHKGNNCCEDSFKDGITNGAEWYDVPGGMQDFNYVHSNCFEITLELSCCKYPPASELPKE
WDNNKEALLSYMEQ
>gnl|CDD|349441 cd03869, M14_CPX_like, Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup. Peptidase M14-like domain of carboxypeptidase (CP)-like protein X (CPX), CPX forms a distinct subgroup of the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Proteins belonging to this subgroup include CP-like protein X1 (CPX1), CP-like protein X2 (CPX2), and aortic CP-like protein (ACLP) and its isoform adipocyte enhancer binding protein-1 (AEBP1). AEBP1 is a truncated form of ACLP, which may arise from alternative splicing of the gene. These proteins are inactive towards standard CP substrates because they lack one or more critical active site and substrate-binding residues that are necessary for activity. They may function as binding proteins rather than as active CPs or display catalytic activity toward other substrates. Proteins in this subgroup also contain an N-terminal discoidin domain. The CP domain is important for the function of AEBP1 as a transcriptional repressor. AEBP1 is involved in several biological processes including adipogenesis, macrophage cholesterol homeostasis, and inflammation. In macrophages, AEBP1 promotes the expression of IL-6, TNF-alpha, MCP-1, and iNOS whose expression is tightly regulated by NF-kappaB activity. ACLP, a secreted protein that associates with the extracellular matrix, is essential for abdominal wall development and contributes to dermal wound healing
HHNYKDMRQLMKVVNEMCPNITRIYNIGKSYQGLKLYAMEISDNPGEHEVGEPEFRYVAGAHGNEVLGRE
LLLLLMQFLCQEYLAGNPRIRHLVEETRIHLLPSVNPDGYEKAYEAGSELGGWSLGRWTSDGIDINHNFP
DLNSLLWEAEDRKWVPRKVPNHHIPIPEWYLSENATVAPETRAVIAWMEKIPFVLGGNLQGGELVVSYPY
DMTRTPWKTQEYTPTPDDHVFRWLAYSYASTHRLMTDASRRPCHTEDFQKEDGTVNGASWHTVAGSMNDF
SYLHTNCFELSIYLGCDKFPHESELPEEWENNRESLLVFMEQ
>gnl|CDD|349442 cd03870, M14_CPA, Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A subgroup. Peptidase M14 Carboxypeptidase (CP) A (CPA) belongs to the A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPA enzymes generally favor hydrophobic residues. A/B subfamily enzymes are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The procarboxypeptidase A (PCPA) is produced by the exocrine pancreas and stored as a stable zymogen in the pancreatic granules until secretion into the digestive tract occurs. This subfamily includes CPA1, CPA2 and CPA4 forms. Within these A forms, there are slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA4, detected in hormone-regulated tissues, is thought to play a role in prostate cancer
FNYAAYHTLEEIYFWMDNLVAEHPNLVSKLQIGSSFENRPMYVLKFSTGGEERPAIWIDAGIHSREWVTQ
ASAIWTAEKIVSDYGKDPSITSILDTMDIFLEIVTNPDGYVFTHSSNRLWRKTRSVNPGSLCIGVDPNRN
WDAGFGGPGASSNPCSETYHGPHANSEVEVKSIVDFIQSHGNFKAFISIHSYSQLLMYPYGYTVEKAPDQ
EELDEVAKKAVKALASLHGTEYKVGSISTTIYQASGSSIDWAYDNGIKYAFTFELRDTGRYGFLLPANQI
IPTAEETWLALKTIMEHVRDH
>gnl|CDD|349443 cd03871, M14_CPB, Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase B subgroup. Peptidase M14 Carboxypeptidase B (CPB) belongs to the carboxypeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Carboxypeptidase B (CPB) enzymes only cleave the basic residues lysine or arginine. A/B subfamily enzymes are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The procarboxypeptidase B (PCPB) is produced by the exocrine pancreas and stored as stable zymogen in the pancreatic granules until secretion into the digestive tract occurs. PCPB has been reported to be a good serum marker for the diagnosis of acute pancreatitis and graft rejection in pancreas transplant recipients. this subfamily also includes thrombin activatable fibrinolysis inhibitor (TAFIa), a carboxypeptidase that stabilizes fibrin clots by removing C-terminal arginines and lysines from partially degraded fibrin. Inhibition of TAFIa stimulates the degradation of fibrin clots and may help in prevention of thrombosis
HSYEKYNNWETIEAWTEQVASKNPDLVSRSQIGTTFEGRPIYLLKVGKPGSNKKAIFMDCGFHAREWISP
AFCQWFVREAVRTYGKEKIMTKLLDRLDFYILPVLNIDGYVYTWTKNRMWRKTRSPNAGSSCIGTDPNRN
FNAGWCTVGASSNPCSETYCGSAPESEKETKALANFIRNNLSSIKAYLTIHSYSQMLLYPYSYTYKLAPN
HEELNSIAKGAVKELSSLYGTKYTYGPGATTIYPAAGGSDDWAYDQGIKYSFTFELRDKGRYGFLLPESQ
IKPTCEETMLAVKYIANYVL
>gnl|CDD|349444 cd03872, M14_CPA6, Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A6 subgroup. Carboxypeptidase (CP) A6 (CPA6, also known as CPAH; EC 3.4.17.1), belongs to the carboxypeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPA6 prefers large hydrophobic C-terminal amino acids as well as histidine, while peptides with a penultimate glycine or proline are very poorly cleaved. Several neuropeptides are processed by CPA6, including Met- and Leu-enkephalin, angiotensin I, and neurotensin. CPA6 converts enkephalin and neurotensin into forms known to be inactive toward their receptors, but converts inactive angiotensin I into the biologically active angiotensin II. Thus, CPA6 plays a possible role in the regulation of neuropeptides in the extracellular environment within the olfactory bulb where it is highly expressed. It is also broadly expressed in embryonic tissue, being found in neuronal tissues, bone, skin as well as the lateral rectus eye muscle. A disruption in the CPA6 gene is linked to Duane syndrome, a defect in the abducens nerve/lateral rectus muscle connection
VYHSLEEIESWMFYMNKTHSDLVHMFSIGKSYEGRSLYVLKLGKRSRSYKKAVWIDCGIHAREWIGPAFC
QWFVKEAINSYQTDPAMKKMLNQLYFYVMPVFNVDGYHYSWTNDRFWRKTRSKNSRFQCRGVDANRNWKV
KWCDEGASLHPCDDTYCGPFPESEPEVKAVAQFLRKHRKHVRAYLSFHAYAQMLLYPYSYKYATIPNFGC
VESAAHNAVNALQSAYGVRYRYGPASSTLYVSSGSSMDWAYKNGIPYAFAFELRDTGYFGFLLPEGLIKP
TCTETMLAVKNITMHLLKKC
>gnl|CDD|349870 cd03873, Zinc_peptidase_like, Zinc peptidases M18, M20, M28, and M42. Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues)
NLIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKE
NGFKPKGTIVVAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDATAGPILQKGVVIRNPLVDALRKA
AREVGGKPQRASVIGGGTDGRLFAELGIPGVTLGPPGDKGAHSPNEFLNLDDLEKATKVY
>gnl|CDD|349871 cd03874, M28_PMSA_TfR_like, M28 Zn-peptidase Transferrin Receptor-like family. Peptidase M28 family; Transferrin Receptor (TfR) and prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase or GCP-II) subfamily. TfR and PSMA are homodimeric type II transmembrane proteins containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). In TfR, it contains a binding site for the transferrin molecule and has 28% identity to membrane glutamate carboxypeptidase II (mGCP-II or PSMA). The PA domain is inserted between the first and second strands of the central beta sheet in the protease-like domain. TfR1 is widely expressed, and is a key player in the uptake of iron-loaded transferrin (Tf) into cells. The TfR1 homodimer binds two molecules of Tf and the complex is then internalized. TfR1 may also participate in cell growth and proliferation. TfR2 binds Tf but with a significantly lower affinity than TfR1. It is expressed chiefly in hepatocytes, hematopoietic cells, and duodenal crypt cells; its expression overlaps with that of hereditary hemochromatosis protein (HFE). TfR2 is involved in iron homeostasis; in humans, mutations in TfR2 are associated with a form of hemochromatosis (HFE3). PSMA is over-expressed predominantly in prostate cancer (PCa) as well as in the neovasculature of most solid tumors, but not in the vasculature of normal tissues. PSMA is considered a biomarker for PCa and possibly for use as an imaging and therapeutic target. The extracellular domain of PSMA possesses two unique enzymatic functions: N-acetylated, alpha-linked acidic dipeptidase (NAALADase) which cleaves terminal glutamate from the neurodipeptide N-acetyl-aspartyl-glutamate (NAAG), and folate hydrolase (FOLH) which cleaves the terminal glutamates from gamma-linked polyglutamates (carboxypeptidase). A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants. While related in sequence to peptidase M28 GCP-II, TfR lacks the metal ion coordination centers and protease activity
YARKLVDLAKIKEDLEYLSSMPHMAGTKGDAALAKYIENSFKNNGLFEVELEEYSPITNVVGKIEGIEQP
DRAIIIGAHRDSWGYGAGYPNSGTAVLLEIARLFQQLKKKFGWKPLRTIYFISWDGSEFGLAGSTELGED
RKASLKDEVYAYINIDQLVIGNSELDVDAHPLLQSLFRKASKKVKFPGNEDWWKHSPNAKVSNLHQYGDW
TPFLNHLGIPVAVFSFKNDRNASYPINSSYDTFEWLEKFLDPDFELHSTLAEFVGLLVLSLAEDPLLP
>gnl|CDD|349872 cd03875, M28_Fxna_like, M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1. Peptidase family M28; Endoplasmic reticulum metallopeptidase 1 (ERMP1; Felix-ina, FXNA or Fxna peptidase; KIAA1815) subfamily. ERMP1 is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organization of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolyzed has not yet been determined. Another member of this subfamily is the 24-kDa vacuolar protein (VP24) which is probably involved in the formation of intravacuolar pigmented globules (cyanoplasts) in highly anthocyanin-containing vacuoles; however, the biological function of the C-terminal region which includes the putative transmembrane metallopeptidase domain is unknown
PGGFSLERAWEDLQVLISIGPHPYGSHNNDKVRDYLLARVEEIKERANANGLEVEVQDDTGSGSFNFLSS
GMTLVYFEVTNIVVRISGKNSNSLPALLLNAHFDSVPTSPGATDDGMGVAVMLEVLRYLSKSGHQPKRDI
IFLFNGAEENGLLGAHAFITQHPWAKNVRAFINLEAAGAGGRAILFQTGPPWLVEAYYSAAKHPFASVIA
QDVFQSGLIPSDTDYRVFRDYGGLPGLDIAFYKNRYVYHTKYDTADHISRGSLQHMGDNLLALLRYLANS
SELENDSEYRGGPAVFFDLLGLFFVYY
>gnl|CDD|349873 cd03876, M28_SGAP_like, M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins. Peptidase family M28; Streptomyces griseus Aminopeptidase (SGAP, Leucine aminopeptidase (LAP), aminopeptidase S, Mername-AA022 peptidase) subfamily. SGAP is a di-zinc exopeptidase with high preference towards large hydrophobic amino-terminal residues, with Leu being the most efficiently cleaved. It can accommodate all except Pro and Glu residues in the P1' position. It is a monomeric (30 kDa), calcium-activated and calcium-stabilized enzyme; its activation by calcium correlates with substrate specificity and it has thermal stability only in the presence of calcium. Although SGAP contains a calcium binding site, it is not conserved in many members of this subfamily. SGAP is present in the extracellular fluid of S. griseus cultures
DITVDNLMAHLQQLQDIADANGGNRAFGSPGYNASVDYVKNELKAAGYYDVTLQPFTSLYRTTYNVIAET
KGGDPNNVVMLGAHLDSVSAGPGINDNGSGSAALLEVALALAKFKVKNAVRFAWWTAEEFGLLGSKFYVN
NLSSEERSKIRLYLNFDMIASPNYGYFIYDGDGSAFNLTGPPGSAEIERLFEAYFTSLGLPSTPTEFDGR
SDYAPFIEAGIPAGGLFTGAEGIKTEEQAALWGGTAGVAYDPCYHQACDTIDNINRTALLRNADAIAHAV
ATYARSTEG
>gnl|CDD|349874 cd03877, M28_like, M28 Zn-peptidase, many containing a protease-associated (PA) domain insert. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Some proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution
GHNVVGVLEGSDLPDETIVIGAHYDHLGIGGGDSGDKIYNGADDNASGVAAVLELARYFAKQKTPKRSIV
FAAFTAEEKGLLGSKYFAENPKFPLDKIVAMLNLDMIGRLGRSKDVYLIGSGSSELENLLKKANKAAGRV
LSKDPLPEWGFFRSDHYPFAKAGVPALYFFTGLHDDYHKPSDDYEKIDYEGMARVVNLIYQLLRGL
>gnl|CDD|349875 cd03879, M28_AAP, M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase. Peptidase family M28; Aeromonas (Vibrio) proteolytica aminopeptidase (AAP; leucine aminopeptidase from Vibrio proteolyticus; Bacterial leucyl aminopeptidase; E.C. 3.4.11.10) subfamily. AAP is a small (32kDa), heat stable leucine aminopeptidase and is active as a monomer. Similar forms of the enzyme have been isolated from Escherichia coli and Staphylococcus thermophilus. Leucine aminopeptidases, in general, play important roles in many biological processes such as protein catabolism, hormone degradation, regulation of migration and cell proliferation, as well as HIV infection and proliferation. AAP is a broad-specificity enzyme, utilizing two zinc(II) ions in its active site to remove N-terminal amino acids, with preference for large hydrophobic amino acids in the P1 position of the substrate, Leu being the most efficiently cleaved. It can accommodate all residues, except Pro, Asp and Glu in the P1' position
PITHQATVNSLLPQLSKSNMQDTLESLTSFNNRYYKSQTGVESAEWLLDQVQAIIASSGRSGATVEQFTH
SFPQPSIIATIPGSEKSDEIVVIGAHQDSINGSNPSNGRAPGADDDGSGTVTILEALRVLLESGFQPKNT
IEFHWYAAEEGGLLGSQAIATQYKSEGKNVKAMLQLDMTGYVKPGSAEDIGLITDYTDSNLTQFLKQLID
EYLPIPYGDTKCGYACSDHASWTKAGYPAAFPFESAFEDYNPYIHTTNDTLDNSGLSFDHMLEFAKLALA
FAVELG
>gnl|CDD|349876 cd03880, M28_QC_like, M28 Zn-peptidase glutaminyl cyclase. Peptidase M28 family, glutaminyl cyclase (QC; EC 2.3.2.5) subfamily. QC is involved in N-terminal glutamine cyclization of many endocrine peptides and is typically abundant in brain tissue. N-terminal glutamine residue cyclization is an important post-translational event in the processing of numerous bioactive proteins, including neuropeptides, hormones, and cytokines during their maturation in the secretory pathway. The N-terminal pGlu protects them from exopeptidase degradation and/or enables them to have proper conformation for binding to their receptors. QCs are highly conserved from yeast to human. In humans, several genetic diseases, such as osteoporosis, appear to result from mutations of the QC gene. N-terminal glutamate cyclization into pyroglutamate (pGlu) is a reaction that may be related to the formation of several plaque-forming peptides, such as amyloid-(A) peptides and collagen-like Alzheimer amyloid plaque component, which play a pivotal role in Alzheimer's disease
STLRHLPELSDDNEHFNNLLAPILIPRVPGSPGHREVRNFIIDFLKSLLAGWTVELDNFTEKTPIGEVTF
TNIIATLNPPAKRYLVLACHYDSKYFPEGEFIGATDSAVPCAMLLYLARSLDAALTRKWPKSKKSDLGLQ
LIFFDGEEAFEEWSDTDSLYGSRHLAAKWESTPYPPGSRYSGRLDRIDLLVLLDLLGAPNPTFPSYFPNT
HGWYKRLADIEKRLRKLGLLESHPSERKYFQPHSKYTPDIEDDHIPFLERGVPVLHLIPSPFPSVWHTLD
DDEENLDYPTIRNWNKILRVFVAEY
>gnl|CDD|349877 cd03881, M28_Nicastrin, M28 Zn-peptidase nicastrin, a main component of gamma-secretase complex. Peptidase M28 family, nicastrin subfamily. Nicastrin is a main component of the gamma-secretase complex, which also contains presenilin, Pen-2 and Aph-1. Its extracellular domain sequence resembles aminopeptidases, but certain catalytic residues are not conserved. It is mainly localized to the endoplasmic reticulum and Golgi. It is highly glycosylated (Mr 120 kDa) and is essential for substrate recognition of the N-terminus of gamma-secretase substrates derived from APP and Notch. Nicastrin facilitates substrate cleavage by the catalytic presenilin subunit in the gamma-secretase complex. One conserved glutamate is especially important, probably because this residue forms an ion pair with the amino terminus of the substrate. This substrate-binding domain is often called the DAP domain (named after DYIGS, the amino acid stretch that modulates amyloid precursor protein (APP) processing, and Peptidase homologous region). The sequence of the substrate N-terminus is apparently not critical for the interaction, but a free amino group is. Thus, nicastrin can be considered a kind of gatekeeper for the gamma-secretase complex: type I membrane proteins that have not shed their ectodomains cannot interact properly with nicastrin and do not gain access to the active site. Dysfunction of gamma-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1)
RSLNGTHQIGCQSNLSGEIGCSHLGVNSQEDLDLVLSKSPHPPYSVLQQVVLDPNLFNRDNVLSLKSKKK
INGVLVLISKTSPLKGFSPDSRCPNAQFGLYSNSNYNWNPNGNGLMYEDFPFPIFYLEDSTETQVLEKCY
EDFNKPVNGSTPLYPLCGMELDSFMSAAINTETCLRRGSIPEKFCDPLGGYNVWSSLPPINTSWEVKTSK
KIVLVAARMDSTSFFRDVAPGADSSLSGFVALLAAAEALKKVDGKGSLKRNVVFAFFNGESWGYIGSSRF
VYDMENGKFPTYGSKDDLFFFPISFENIDTILEVGQVGLALGAKLYAHTDGVSTNSSVTQQLLDALSNSL
KSLAFTILSAPASSPGLPPSSLMSFLRADPNIPGVVLTDHDKAFTNKYYHSIYDDAENVNVDTASSVAEV
ASVVARSLYTLAGGNTTRFVGYFLANLTGTVTNATNDVCQNPCKNVDEVCIGAGTSRLGECVKSTTRYSP
ALSPAFKFNEPSDWMSTNRYSTWTESFWI
>gnl|CDD|349878 cd03882, M28_nicalin_like, M28 Zn-Peptidase Nicalin, Nicastrin-like protein. Peptidase M28 family, Nicalin (nicastrin-like protein) subfamily. Nicalin is distantly related to Nicastrin, a component of the Alzheimer's disease-associated gamma-secretase, and forms a complex with Nomo (nodal modulator) pM5. Similar to Nicastrin, Nicalin lacks the amino-acid conservation required for catalytically active aminopeptidases. Functional studies in zebrafish embryos and cultured human cells reveal that nicalin and Nomo collaborate to antagonize the Nodal/TGFbeta signaling pathway. Thus, nicastrin and nicalin are both associated with protein complexes involved in cell fate decisions during early embryonic development
FMELEAELLNTKTNVPVYFAPENEELLSIYEDVKSSSAAAQSAAEVLIRSLSANGFKIVVSGNSPKAISD
WKITTIEGRLTGLGDGEKLPTIVIVAHYDTFGVAPWLSSGADSNGSGVAALLELMRLFSRLYSNPRTRAK
YNLLFLLTGGGKLNYQGTKHWLESNLDHFLDNVEFVLCLDSIGSKDSDLYLHVSKPPKEGTHIQQFLEEL
KSVAKAPDKNLTVVHKKINLADTKLAWEHERFSIKRLPAFTLSHLESHRSPLRNSIFDTRSSVDEDKLKR
NTKIIAEALARYIYNL
>gnl|CDD|349879 cd03883, M28_Pgcp_like, M28 Zn-Peptidase Plasma glutamate carboxypeptidase. Peptidase M28 family; Plasma glutamate carboxypeptidase (PGCP; blood plasma glutamate carboxypeptidase; EC 3.4.17.21) subfamily. PGCP is a 56kDa glutamate carboxypeptidase that is mainly produced in mammalian placenta and kidney, the majority of which is thought to be secreted into the bloodstream. Similar proteins are also found in other species, including bacteria. These proteins contain protease-associated (PA) domain inserts between the first and second strands of the central beta sheet in the protease-like domain. The PA domains may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. The exact physiological substrates of PGCP are unknown, although this enzyme may play an important role in the hydrolysis of circulating peptides. Its closest homolog encodes an important brain glutamate carboxypeptidase II (NAALADase) identical to the prostate-specific membrane antigen (PSMA), which serves as a marker for prostatic cancer metastasis. Hypermethylation of PGCP gene has been associated with human bronchial epithelial (HBE) cell immortalization and lung cancer. PGCP also provides an attractive target for serological analysis in hepatitis C virus (HCV)-induced hepatocellular carcinoma (HCC) patients
SYKKVAKQIIQTALNGSLKQAYDRLAYLVDTFGPRLSGSENLEKAIDWLYAKLQNDGFDKVHEEPVEVPH
WVRGEESATLLEPRPQKLAILGLGGSVGTPVEGIEAEVVVVFSFEELQAKADEVKGKIVVYNQPFKGYGE
TVKYRGQGAVEAAKYGAVAVLIRSITPFSIYSPHTGIMRYQDGVTKIPAAAITVEDAEMLSRMAARGQKI
VIELKMEAKTYPDATSRNVIAEITGSKYPDEVVLVGGHLDSWDVGTGAMDDGGGVAISWEALKLIKDLGL
KPKRTIRVVLWTGEEQGLVGAKAYAEAHKDELENHVFAMESDIGTFTPYGLQFTGSDTARAIVKEVMKLL
SPLGITQVLPKAGVGPDISFLKAAGVPGASLIQDNSDYFDYHHTAGDTMDVMDPKQLDQNVAAWASLAYV
IADMD
>gnl|CDD|349880 cd03884, M20_bAS, M20 Peptidase beta-alanine synthase, an amidohydrolase. Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders
LWDRLEELAAIGATPAGGVTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVGNLFGRLEGTDPDAPPVLT
GSHLDTVPNGGRYDGILGVLAGLEALRALKEAGIRPRRPIEVVAFTNEEGSRFPPSMLGSRAFAGTLDLE
ELLSLRDADGVSLAEALKAIGYDGDRPASARRPGDIKAYVELHIEQGPVLEEEGLPIGVVTGIAGQRWLE
VTVTGEAGHAGTTPMALRRDALLAAAELILAVEEIALEHGDDLVATVGRIEVKPNAVNVIPGEVEFTLDL
RHPDDAVLDAMVERIRAEAEAIAAERGVEVEVERLWDSPPVPFDPELVAALEAAAEALGLSYRRMPSGAG
HDAMFMARICPTAMIFVPSRDGISHNPAEYTSPEDLAAGVQVLLHALL
>gnl|CDD|349881 cd03885, M20_CPDG2, M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme. Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells
MLDLLERLVNIESGTYDKEGVDRVAELLAEELEALGFTVERRPLGEFGDHLIATFKGTGGKRVLLIGHMD
TVFPEGTLAFRPFTVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRE
LIEEEAKGADYVLVFEPARADGNLVTARKGIGRFRLTVKGRAAHAGNAPEKGRSAIYELAHQVLALHALT
DPEKGTTVNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTLVPGTSVELTGGLNRP
PMEETPASRRLLARAQEIAAELGLTLDWEATGGGSDANFTAALGVPTLDGLGPVGGGAHTEDEYLELDSL
VPRIKLLARLLM
>gnl|CDD|349882 cd03886, M20_Acy1, M20 Peptidase Aminoacylase 1 family. Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay
LIALRRDLHQHPELSFEEFRTAARIAEELRELGLEVRTGVGGTGVVATLKGGGPGPTVALRADMDALPIQ
EETGLPFASKHEGVMHACGHDGHTAMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPGGAKAMIEEGVLEN
PGVDAAFGLHVWPGLPVGTVGVRSGALMASADEFEITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVVS
RELDPLEPAVVTVGKFHAGTAFNVIPDTAVLEGTIRTFDPEVREALEARIKRLAEGIAAAYGATVELEYG
YGYPAVINDPELTELVREAAKELLGEEAVVEPEPVMGSEDFAYYLEKVPGAFFWLGAGEPDGENPGLHSP
TFDFDEDALPIGAALLAELAL
>gnl|CDD|349883 cd03887, M20_Acy1L2, M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family. Peptidase M20 family, Aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase) subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine)
DEHAEELIELSRDIHDNPELGYEEYKAHDLLTDFLEELGFDVTRGAYGLETAFRAEYGSGKGGPTVAFLA
EYDALPGIGHACGHNLIATASVAAALALKAALKALGLPGTVVVLGTPAEEGGGGKIDLIKAGAFDDVDIA
LMVHPGPKDVAGPKSLAVSKLRVEFHGKAAHAAAAPWEGINALDAAVLAYNNISALRQQLKPTVRVHGII
TEGGKAPNIIPDYAEAEFYVRAPTLKELEELTERVIACFEGAALATGCEVEIEELEGYYDELLPNKTLAN
IYAENMEALGEEVLDGDEGVGSGSTDFGNVSYVVPGIHPYFGIPPPGAANHTPEFAEAAGTEEAHEAALK
AAKALAMTAL
>gnl|CDD|349884 cd03888, M20_PepV, M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides. Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme
EEIDKYKDEILEDLKELVAIPSVRDEATEGAPFGEGPRKALDKFLDLAKRLGFKTKNIDNYAGYAEYGEG
EEVLGILGHLDVVPAGEGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIF
GTDEETGWKCIEHYFEHEEYPDFGFTPDAEFPVINGEKGIVTVDLTFKIDDDKGYRLISIKGGEATNMVP
DKAEAVIPGKDKEELALSAATDLKGNIEIDDGGVELTVTGKSAHASAPEKGVNAITLLAKFLAELNKDGN
DKDFIKFLAKNLHEDYNGKKLGINFEDEVMGELTLNPGIITLDDGKLELGLNVRYPVGTSAEDIIKQIEE
ALEKYGVEVEGHKHQKPLYVPKDSPLVKTLLKVYEEQTGKEGEPVAIGGGTYARELPNGVAFGPEFPGQK
DTMHQANEFIPIDDLIKALAIYAEAIYEL
>gnl|CDD|349885 cd03890, M20_pepD, M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide. Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear
PKIVWKYFEEISKIPRPSGNEKQISDFLVKFAKKLGLEVIQDEVGNVIIRKPATPGYENAPPVILQGHMD
MVCEKNADSEHDFEKDPIKLRIDGDWLKATGTTLGADNGIGVAYALAILEDKDIEHPPLEVLFTVDEETG
MTGALGLDPSLLKGKILLNLDSEEEGELTVGCAGGIDVTITLPIEREEAEGGYTGLKITVKGLKGGHSGV
DIHKGRANANKLMARLLYELAKELDFRLVSINGGTKRNAIPREAVAVIAVPAEDVEALKKLIKKLEKALK
AEYAGTDPNLKIEVEKVETPKVVLSEASTDKLLDLLNALPNGVQRMSPDIEGLVETSLNLGIVKTKEDEI
KVTCSVRSSVDSGKDELANKLESLAKLAGAEVEFSGDYPGWEPNPDSPLLDLMVEVYKELYGKEPEVTAI
HAGLECGLIKEKYPDLDMISFGPTIRDVHSPDERVEISSVERFWDLLVEILKEL
>gnl|CDD|349886 cd03891, M20_DapE_proteobac, M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase. Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE
LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFGGVKNLWARRGTGGPHLCFAGHTDVVPPGD
LEGWSSDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKV
LEWLKARGEKIDYCIVGEPTSEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAEL
TATVLDEGNEFFPPSSLQITNIDVGNGATNVIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDL
EWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELSTSGGTSDARFIASYGCPVVEFGLVNATIHKVNERV
SVADLEKLTDIYERIL
>gnl|CDD|349887 cd03892, M20_peptT, M20 Peptidase T specifically cleaves tripeptides. Peptidase M20 family, Peptidase T (peptT; tripeptide aminopeptidase; tripeptidase) subfamily. PepT acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein
LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDEHGYVTATLPANVDKDVPTI
GFIAHMDTAPDNSGKNVKPQIIENYDGGDIVLNESGIVLSPAEFPELKNYKGQTLITTDGTTLLGADDKA
GIAEIMTALEYLIEHPEIKHGDIRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAAS
ATITITGVNVHPGTAKGKMVNALLLAADFHSMLPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDF
DRDGFEARKELIKEIAKKLNAKYGEGRVELEIKDQYYNMKEKIEPHMHIVDLAKEAMEALGIEPIVKPIR
GGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIVKIAEL
>gnl|CDD|349888 cd03893, M20_Dipept_like, M20 Dipeptidases. Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation
LQTLAELVAIPSVSAQPDRREELRRAAEWLADLLRRLGFTVEIVDTSNGAPVVFAEFPGAPGAPTVLLYG
HYDVQPAGDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEES
GSPSLDQLVEAHRDLLAADAIVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLDHDLHSGLYGGVVPDPM
TALAQLLASLRDETGRILVPGLYDAVRELPEEEFRLDAGVLEEVEIIGGTTGSVAERLWTRPALTVLGID
GGFPGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLEAHLEKHAPSGAKVTVSYVEGGMPWRSDPSDPA
YQAAKDALRTAYGVEPPLTREGGSIPFISVLQEFPQAPVLLIGVGDPDDNAHSPNESLRLGNYKEGTQAE
AALLYS
>gnl|CDD|349889 cd03894, M20_ArgE, M20 Peptidase acetylornithine deacetylase. Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved
ELLARLVAFDTVSRNSNLALIEYVADYLAALGVKSRRVPVPEGGKANLLATLGPGGEGGLLLSGHTDVVP
VDGQKWSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLI
AALAARGGRPDAAIVGEPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADR
LAPGLRDPPFDPPYPTLNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPEAG
IEVEPLFEVPGLETDEDAPLVRLAAALAGDNKVRTVAYGTEAGLFQRAGIPTVVCGPGSIAQAHTPDEFV
ELEQLDRCEEFLRRLIA
>gnl|CDD|349890 cd03895, M20_ArgE_DapE-like, M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases. Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE
AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDRWEIDVEKLKHHPGFSPVAVDYAGAPNVVGTHRPR
GETGRSLILNGHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAAD
VHFQSVVEEECTGNGALAALMRGYRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAI
EKAMHLIQALQELEREWNARKKSHPHFSDHPHPINFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEE
ARREIEECVADAAATDPWLSNHPPEVEWNGFQAEGYVLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTD
GRFFVLYGDIPALCYGPGSRDAHGFDESVDLESLRKITKTIALFIAEWCG
>gnl|CDD|349891 cd03896, M20_PAAh_like, M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins. Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329
VDTAIELGEIPAPTFREGARADLVAEWMADLGLGDVERDGRGNVVGRLRGTGGGPALLFSAHLDTVFPGD
TPATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEGLGDLRGARYLLSAHG
ARLDYFVVAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAPYVPKTTF
AAIRGGGGTSVNRIANLCSMYLDIRSNPDAELADVQREVEAVVSKLAAKHLRVKARVKPVGDRPGGEAQG
TEPLVNAAVAAHREVGGDPRPGSSSTDANPANSLGIPAVTYGLGRGGNAHRGDEYVLKDDMLKGAKAYLM
LAAALCG
>gnl|CDD|175976 cd04009, C2B_Munc13-like, C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins. C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology
PYGVLTVKAYYRASEQSLRVEILNARNLLPLDSNGSSDPFVKVELLPRHLFPDVPTPKTQVKKKTLFPLF
DESFEFNVPPEQCSVEGALLLFTVKDYDLLGSNDFEGEAFLPLNDIPGVEDTSSAQGFGPLPQ
>gnl|CDD|175977 cd04010, C2B_RasA3, C2 domain second repeat present in RAS p21 protein activator 3 (RasA3). RasA3 are members of GTPase activating protein 1 (GAP1), a Ras-specific GAP, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA3 contains an N-terminal C2 domain, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
KLSVRVIECSDLALKNGTCDPYASVTLIYSNKKQDTKRTKVKKKTNNPQFDEAFYFDVTIDSSPEKKQFE
MPEEDAEKLELRVDLWHASMGGGDVFLGEVRIPLRGLDLQAGSHQAWYFLQPREEKSTPPGTRSSKDNSL
GSLRLKIN
>gnl|CDD|175978 cd04011, C2B_Ferlin, C2 domain second repeat in Ferlin. Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology
PQDFQVRVRVIEARQLVGGNIDPVVKVEVGGQKKYTSVKKGTNCPFYNEYFFFNFHESPDELFDKIIKIS
VYDSRSLRSDTLIGSFKLDVGTVYDQPDHAFLRKWLLLTDP
>gnl|CDD|175979 cd04012, C2A_PI3K_class_II, C2 domain first repeat present in class II phosphatidylinositol 3-kinases (PI3Ks). There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a N-terminal C2 domain, a PIK domain, and a kinase catalytic domain. Unlike class I and class III, class II PI3Ks have additionally a PX domain and a C-terminal C2 domain containing a nuclear localization signal both of which bind phospholipids though in a slightly different fashion. Class II PIK3s act downstream of receptors for growth factors, integrins, and chemokines. PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
REASTVTDLLSVTVSSLHRIPPTWVQSFEDFYLSCSLYHGGRLLCSPVTTKPVKITKSFFPRVVWDEWIE
FPIPVCQLPRESRLVLTLYGTTSSPDGGSNKQRMGPEELGWVSLPLFDFRGVLRQGSLLLGLWPPSKDNP
LGPAPPPLFEQPDRVILQIDFPSSAFDVIFP
>gnl|CDD|175980 cd04013, C2_SynGAP_like, C2 domain present in Ras GTPase activating protein (GAP) family. SynGAP, GAP1, RasGAP, and neurofibromin are all members of the Ras-specific GAP (GTPase-activating protein) family. SynGAP regulates the MAP kinase signaling pathway and is critical for cognition and synapse function. Mutations in this gene causes mental retardation in humans. SynGAP contains a PH-like domain, a C2 domain, and a Ras-GAP domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVIT
VNLYRESDKKKKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGNGKSGGKEGKGESPSIRIKARYQS
TRVLPL
>gnl|CDD|175981 cd04014, C2_PKC_epsilon, C2 domain in Protein Kinase C (PKC) epsilon. A single C2 domain is found in PKC epsilon. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1 (alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology
MFTGTLKIKICEAVDLKPTDWSTRHAVPKKGSQLLDPYVSIDVDDTHIGKTSTKPKTNSPVWNEEFTTEV
HNGRNLELTVFHDAAIGPDDFVANCTISFEDLIQRGSGSFDLWVDLEPQGKLHVKIELKGSA
>gnl|CDD|175982 cd04015, C2_plant_PLD, C2 domain present in plant phospholipase D (PLD). PLD hydrolyzes terminal phosphodiester bonds in diester glycerophospholipids resulting in the degradation of phospholipids. In vitro PLD transfers phosphatidic acid to primary alcohols. In plants PLD plays a role in germination, seedling growth, phosphatidylinositol metabolism, and changes in phospholipid composition. There is a single Ca(2+)/phospholipid-binding C2 domain in PLD. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
AAVLLHGTLDVTIYEADNLPNMDMFSEKLRRFFSKLVGCSEPTLKRPSSHRHVGKITSDPYATVDLAGAR
VARTRVIENSENPVWNESFHIYCAHYASHVEFTVKDNDVVGAQLIGRAYIPVEDLLSGEPVEGWLPILDS
NGKPPKPGAKIRVSLQFT
>gnl|CDD|175983 cd04016, C2_Tollip, C2 domain present in Toll-interacting protein (Tollip). Tollip is a part of the Interleukin-1 receptor (IL-1R) signaling pathway. Tollip is proposed to link serine/threonine kinase IRAK to IL-1Rs as well as inhibiting phosphorylation of IRAK. There is a single C2 domain present in Tollip. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
VGRLSITVVQAKLVKNYGLTRMDPYCRIRVGHAVYETPTAYNGAKNPRWNKTIQCTLPEGVDSIYIEIFD
ERAFTMDERIAWTHITIPESVFNGETLDDWYSLSGKQGEDKEGMINLVFSY
>gnl|CDD|175984 cd04017, C2D_Ferlin, C2 domain fourth repeat in Ferlin. Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the fourth C2 repeat, C2D, and has a type-II topology
FQLRAYIYQARDLLAADKSGLSDPFARVSFLNQSQETEVIKETLSPTWDQTLIFDEVELYGSPEEIAQNP
PLVVVELFDQDSVGKDEFLGRSVAKPLVKLDLEEDFPPKLQWFPIYKGGQSAGELLAAFELIEVT
>gnl|CDD|175985 cd04018, C2C_Ferlin, C2 domain third repeat in Ferlin. Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology
RFIFKIYRAEDLPQMDSGIMANVKKAFLGEKKELVDPYVEVSFAGQKVKTSVKKNSYNPEWNEQIVFPEM
FPPLCERIKIQIRDWDRVGNDDVIGTHFIDLSKISNSGDEGFLPTFGPSFVNLYGSPREYSLLDDHQDLN
EGLGEGVAYRG
>gnl|CDD|175986 cd04019, C2C_MCTP_PRT_plant, C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset. MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology
YLRVTVIEAQDLVPSDKNRVPEVFVKAQLGNQVLRTRPSQTRNGNPSWNEELMFVAAEPFEDHLILSVED
RVGPNKDEPLGRAVIPLNDIERRVDDRPVPSRWFSLERPGGAMEQKKKRKFASRIHLRLCLDGGYHVLDE
STHYSSDLRP
>gnl|CDD|175987 cd04020, C2B_SLP_1-2-3-4, C2 domain second repeat present in Synaptotagmin-like proteins 1-4. All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
RGELKVALKYVPPESEGALKSKKPSTGELHVWVKEAKNLPALKSGGTSDSFVKCYLLPDKSKKSKQKTPV
VKKSVNPVWNHTFVYDGVSPEDLSQACLELTVWDHDKLSSNDFLGGVRLGLGTGKSYGQAVDWMDSTGEE
ILLWQKMLDNPNSWVEGTLPLR
>gnl|CDD|175988 cd04021, C2_E3_ubiquitin_ligase, C2 domain present in E3 ubiquitin ligase. E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPPKKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSH
HTLKADVLLGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD
>gnl|CDD|175989 cd04022, C2A_MCTP_PRT_plant, C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset. MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology
KLVVEVVDAQDLMPKDGQGSSSAYVELDFDGQKKRTRTKPKDLNPVWNEKLVFNVSDPSRLSNLVLEVYV
YNDRRSGRRRSFLGRVRISGTSFVPPSEAVVQRYPLEKRGLFSRVRGEIGLKVYITD
>gnl|CDD|175990 cd04024, C2A_Synaptotagmin-like, C2 domain first repeat present in Synaptotagmin-like proteins. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
GVLRVHVVEAKDLAAKDRSGKGKSDPYAILSVGAQRFKTQTIPNTLNPKWNYWCEFPIFSAQNQLLKLIL
WDKDRFAGKDYLGEFDIALEEVFADGKTGQSDKWITLKSTRPGKTSVVSGEIHLQFSW
>gnl|CDD|175991 cd04025, C2B_RasA1_RasA4, C2 domain second repeat present in RasA1 and RasA4. RasA1 and RasA4 are GAP1s (GTPase activating protein 1s), Ras-specific GAP members, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. Both proteins contain two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
RLRCHVLEARDLAPKDRNGTSDPFVRVFYNGQTLETSVVKKSCYPRWNEVFEFELMEGADSPLSVEVWDW
DLVSKNDFLGKVVFSIQTLQQAKQEEGWFRLLPDPRAEEESGGNLGSLRLKVR
>gnl|CDD|175992 cd04026, C2_PKC_alpha_gamma, C2 domain in Protein Kinase C (PKC) alpha and gamma. A single C2 domain is found in PKC alpha and gamma. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1(alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology
RGRIYLKISVKDNKLTVEVREAKNLIPMDPNGLSDPYVKLKLIPDPKNETKQKTKTIKKTLNPVWNETFT
FDLKPADKDRRLSIEVWDWDRTTRNDFMGSLSFGVSELIKMPVDGWYKLLNQEEGEYYNVP
>gnl|CDD|175993 cd04027, C2B_Munc13, C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins. C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology
AKISITVVCAQGLIAKDKTGTSDPYVTVQVGKTKKRTKTIPQNLNPVWNEKFHFECHNSSDRIKVRVWDE
DDDIKSRLKQKFTRESDDFLGQTIIEVRTLSGEMDVWYNLEKRTDKSAVSGAIRLHI
>gnl|CDD|175994 cd04028, C2B_RIM1alpha, C2 domain second repeat contained in Rab3-interacting molecule (RIM) proteins. RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology and do not bind Ca2+
LGPGQLVGRQVLASPSMGDIQLGLYDKKGQLEVEVIRARGLVQKPGSKVLPAPYVKVYLLEGKKCIAKKK
TKIARKTLDPLYQQQLVFDVSPTGKTLQVIVWGDYGRMDKKVFMGVAQILLDDLDLSNLVIGWYKLFPTS
SLVDPT
>gnl|CDD|175995 cd04029, C2A_SLP-4_5, C2 domain first repeat present in Synaptotagmin-like proteins 4 and 5. All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. SHD of Slp (except for the Slp4-SHD) function as a specific Rab27A/B-binding domain. In addition to Slp, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp4/granuphilin promotes dense-core vesicle exocytosis. The C2A domain of Slp4 is Ca2+ dependent. Slp5 mRNA has been shown to be restricted to human placenta and liver suggesting a role in Rab27A-dependent membrane trafficking in specific tissues. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
SGEILFSLSYDYKTQSLNVHVKECRNLAYGDEAKKRSNPYVKTYLLPDKSRQSKRKTSIKRNTTNPVYNE
TLKYSISHSQLETRTLQLSVWHYDRFGRNTFLGEVEIPLDSWNFDSQHEECLPLH
>gnl|CDD|175996 cd04030, C2C_KIAA1228, C2 domain third repeat present in uncharacterized human KIAA1228-like proteins. KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology
PLGRIQLTIRYSSQRQKLIVTVHKCRNLPPCDSSDIPDPYVRLYLLPDKSKSTRRKTSVKKDNLNPVFDE
TFEFPVSLEELKRRTLDVAVKNSKSFLSREKKLLGQVLIDLSDLDLSKGFTQWYDLT
>gnl|CDD|175997 cd04031, C2A_RIM1alpha, C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins. RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology and do not bind Ca2+
ITGRIQIQLWYDKVTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLPDRSEKSKRRTKTVKKTLNPEWNQ
TFEYSNVRRETLKERTLEVTVWDYDRDGENDFLGEVVIDLADALLDDEPHWYPLQ
>gnl|CDD|175998 cd04032, C2_Perforin, C2 domain of Perforin. Perforin contains a single copy of a C2 domain in its C-terminus and plays a role in lymphocyte-mediated cytotoxicity. Mutations in perforin leads to familial hemophagocytic lymphohistiocytosis type 2. The function of perforin is calcium dependent and the C2 domain is thought to confer this binding to target cell membranes. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
SARDNCPCVCSSSPNVNSNCCPTRRGLATLTVTVLRATGLWGDYFTSTDGYVKVFFGGQEKRTEVIWNNN
NPRWNATFDFGSVELSPGGKLRFEVWDRDNGWDDDLLGTCSVVPEAGVHEDSCQLNH
>gnl|CDD|175999 cd04033, C2_NEDD4_NEDD4L, C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated 4 (NEDD4) and NEDD4-like (NEDD4L/NEDD42). Nedd4 and Nedd4-2 are two of the nine members of the Human Nedd4 family. All vertebrates appear to have both Nedd4 and Nedd4-2 genes. They are thought to participate in the regulation of epithelial Na+ channel (ENaC) activity. They also have identical specificity for ubiquitin conjugating enzymes (E2). Nedd4 and Nedd4-2 are composed of a C2 domain, 2-4 WW domains, and a ubiquitin ligase Hect domain. Their WW domains can bind PPxY (PY) or LPSY motifs, and in vitro studies suggest that WW3 and WW4 of both proteins bind PY motifs in the key substrates, with WW3 generally exhibiting higher affinity. Most Nedd4 family members, especially Nedd4-2, also have multiple splice variants, which might play different roles in regulating their substrates. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
ILRVKVLAGIDLAKKDIFGASDPYVKISLYDPDGNGEIDSVQTKTIKKTLNPKWNEEFFFRVNPREHRLL
FEVFDENRLTRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL
>gnl|CDD|176000 cd04035, C2A_Rabphilin_Doc2, C2 domain first repeat present in Rabphilin and Double C2 domain. Rabphilin is found neurons and in neuroendrocrine cells, while Doc2 is found not only in the brain but in tissues, including mast cells, chromaffin cells, and osteoblasts. Rabphilin and Doc2s share highly homologous tandem C2 domains, although their N-terminal structures are completely different: rabphilin contains an N-terminal Rab-binding domain (RBD),7 whereas Doc2 contains an N-terminal Munc13-1-interacting domain (MID). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
LGTLEFTLLYDPANSALHCTIIRAKGLKAMDANGLSDPYVKLNLLPGASKATKLRTKTVHKTRNPEFNET
LTYYGITEEDIQRKTLRLLVLDEDRFGNDFLGETRIPLKKLKPNQTKQFNICL
>gnl|CDD|176001 cd04036, C2_cPLA2, C2 domain present in cytosolic PhosphoLipase A2 (cPLA2). A single copy of the C2 domain is present in cPLA2 which releases arachidonic acid from membranes initiating the biosynthesis of potent inflammatory mediators such as prostaglandins, leukotrienes, and platelet-activating factor. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members of this cd have a type-II topology
LLTVRVLRATNITKGDLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETFEFRIQSQVKNVLELTV
MDEDYVMDDHLGTVLFDVSKLKLGEKVRVTFSLNPQGKEELEVEFLLEL
>gnl|CDD|176002 cd04037, C2E_Ferlin, C2 domain fifth repeat in Ferlin. Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the fifth C2 repeat, C2E, and has a type-II topology
LVRVYVVRARNLQPKDPNGKSDPYLKIKLGKKKINDRDNYIPNTLNPVFGKMFELEATLPGNSILKISVM
DYDLLGSDDLIGETVIDLEDRFFSKHRATCGLPPTYEESGPNQWRDSLKPSGIL
>gnl|CDD|176003 cd04038, C2_ArfGAP, C2 domain present in Arf GTPase Activating Proteins (GAP). ArfGAP is a GTPase activating protein which regulates the ADP ribosylation factor Arf, a member of the Ras superfamily of GTP-binding proteins. The GTP-bound form of Arf is involved in Golgi morphology and is involved in recruiting coat proteins. ArfGAP is responsible for the GDP-bound form of Arf which is necessary for uncoating the membrane and allowing the Golgi to fuse with an acceptor compartment. These proteins contain an N-terminal ArfGAP domain containing the characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) and C-terminal C2 domain. C2 domains were first identified in Protein Kinase C (PKC). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
LGLLKVRVVRGTNLAVRDFTSSDPYVVLTLGNQKVKTRVIKKNLNPVWNEELTLSVPNPMAPLKLEVFDK
DTFSKDDSMGEAEIDLEPLVEAAKLDHLRDTPGGTQIKKVLPSVENCLASESHITWKDGKIVQDLVLKLR
NVESG
>gnl|CDD|176004 cd04039, C2_PSD, C2 domain present in Phosphatidylserine decarboxylase (PSD). PSD is involved in the biosynthesis of aminophospholipid by converting phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn). There is a single C2 domain present and it is thought to confer PtdSer binding motif that is common to PKC and synaptotagmin. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
GVVFMEIKSITDLPPLKNMTRTGFDMDPFVIISFGRRVFRTSWRRHTLNPVFNERLAFEVYPHEKNFDIQ
FKVLDKDKFSFNDYVATGSLSVQELLNAAPQPDPETGL
>gnl|CDD|176005 cd04040, C2D_Tricalbin-like, C2 domain fourth repeat present in Tricalbin-like proteins. 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the fifth C2 repeat, C2E, and has a type-II topology
LTVDVISAENLPSADRNGKSDPFVKFYLNGEKVFKTKTIKKTLNPVWNESFEVPVPSRVRAVLKVEVYDW
DRGGKDDLLGSAYIDLSDLEPEETTELTLPLDGQGGGKLGAVFLP
>gnl|CDD|176006 cd04041, C2A_fungal, C2 domain first repeat; fungal group. C2 domains were first identified in Protein Kinase C (PKC). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
GVLVVTIHRATDLPKADFGTGSSDPYVTASFAKFGKPLYSTRIIRKDLNPVWEETWFVLVTPDEVKAGER
LSCRLWDSDRFTADDRLGRVEIDLKELIEDRNWMGRREDGF
>gnl|CDD|176007 cd04042, C2A_MCTP_PRT, C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP). MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence, three C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology
QLDIHLKEGRNLAARDRGGTSDPYVKFKYGGKTVYKSKTIYKNLNPVWDEKFTLPIEDVTQPLYIKVFDY
DRGLTDDFMGSAFVDLSTLELNKPTEVKLKLEDPNSDEDLGYISLVVTLTP
>gnl|CDD|176008 cd04043, C2_Munc13_fungal, C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group. C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology
HLFTIRIVRAENLKADSSNGLSDPYVTLVDTNGKRRIAKTRTIYDTLNPRWDEEFELEVPAGEPLWISAT
VWDRSFVGKHDLCGRASLKLDPKRFGDDGLPREIWLDLDTQGRLLLRVSMEGERDD
>gnl|CDD|176009 cd04044, C2A_Tricalbin-like, C2 domain first repeat present in Tricalbin-like proteins. 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology
IGVLAVTIKSARGLKGSDIIGGTVDPYVTFSISNRRELARTKVKKDTSNPVWNETKYILVNSLTEPLNLT
VYDFNDKRKDKLIGTAEFDLSSLLQNPEQENLTKNLLRNGKPVGELNYDLRFFP
>gnl|CDD|176010 cd04045, C2C_Tricalbin-like, C2 domain third repeat present in Tricalbin-like proteins. 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology
GVLRLHIRKANDLKNLEGVGKIDPYVRVLVNGIVKGRTVTISNTLNPVWDEVLYVPVTSPNQKITLEVMD
YEKVGKDRSLGSVEINVSDLIKKNEDGKYVEYDDEEERLKRLLSLKGVKG
>gnl|CDD|176011 cd04046, C2_Calpain, C2 domain present in Calpain proteins. A single C2 domain is found in calpains (EC 3.4.22.52, EC 3.4.22.53), calcium-dependent, non-lysosomal cysteine proteases. Caplains are classified as belonging to Clan CA by MEROPS and include six families: C1, C2, C10, C12, C28, and C47. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
PQVVTQVHVHSAEGLSKQDSGGGADPYVIIKCEGESVRSPVQKDTLSPEFDTQAIFYRKKPRSPIKIQVW
NSNLLCDEFLGQATLSADPNDSQTLRTLPLRKRGRDAAGEVPGTISVKVTSSDDLT
>gnl|CDD|176012 cd04047, C2B_Copine, C2 domain second repeat in Copine. There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
DVVELQFSGKKLDKKDFFGKSDPFLEISRQSEDGTWVLVYRTEVIKNTLNPVWKPFTIPLQKLCNGDYDR
PIKIEVYDYDSSGKHDLIGEFETTLDELLKSSPLEFELIN
>gnl|CDD|176013 cd04048, C2A_Copine, C2 domain first repeat in Copine. There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
PKVELSISCRNLLDKDVLSKSDPFVVVYVKTGGSGQWVEIGRTEVIKNNLNPDFVTTFTVDYYFEEVQKL
RFEVYDVDSKSKDLSDHDFLGEAECTLGEIVSSPGQKLTLPLKGGKGKGT
>gnl|CDD|176014 cd04049, C2_putative_Elicitor-responsive_gene, C2 domain present in the putative elicitor-responsive gene. In plants elicitor-responsive proteins are triggered in response to specific elicitor molecules such as glycolproteins, peptides, carbohydrates and lipids. A host of defensive responses are also triggered resulting in localized cell death. Antimicrobial secondary metabolites, such as phytoalexins, or defense-related proteins, including pathogenesis-related (PR) proteins are also produced. There is a single C2 domain present here. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-II topology
GTLEVLLISAKGLQDTDFLGKIDPYVIIQCRTQERKSKVAKGDGRNPEWNEKFKFTVEYPGWGGDTKLIL
RIMDKDNFSDDDFIGEATIHLKGLFEEGVEPGTAELVPAKYNVVLEDDTYKGEI
>gnl|CDD|176015 cd04050, C2B_Synaptotagmin-like, C2 domain second repeat present in Synaptotagmin-like proteins. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
LLFVYLDSAKNLPLAKSTKEPSPYVELTVGKTTQKSKVKERTNNPVWEEGFTFLVRNPENQELEIEVKDD
KTGKSLGSLTLPLSELLKEPDLTLDQPFPLDNSGP
>gnl|CDD|176016 cd04051, C2_SRC2_like, C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins. SRC2 production is a response to pathogen infiltration. The initial response of increased Ca2+ concentrations are coupled to downstream signal transduction pathways via calcium binding proteins. SRC2 contains a single C2 domain which localizes to the plasma membrane and is involved in Ca2+ dependent protein binding. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
TLEITIISAEDLKNVNLFGKMKVYAVVWIDPSHKQSTPVDRDGGTNPTWNETLRFPLDERLLQQGRLALT
IEVYCERPSLGDKLIGEVRVPLKDLLDGASPAGELRFLSYQLRRPSGKPQGVLNF
>gnl|CDD|176017 cd04052, C2B_Tricalbin-like, C2 domain second repeat present in Tricalbin-like proteins. 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology
KGLDTSESKTGLLSPYAELYLNGKLVYTTRVKKKTNNPSWNASTEFLVTDRRKSRVTVVVKDDRDRHDPV
LGSVSISLNDLIDATSVGQQWFPLSGNGQGRIRISALWKPV
>gnl|CDD|176018 cd04054, C2A_Rasal1_RasA4, C2 domain first repeat present in RasA1 and RasA4. Rasal1 and RasA4 are both members of GAP1 (GTPase activating protein 1). Rasal1 responds to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. RasA4 suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. Both of these proteins contains two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
SLYIRIVEGKNLPAKDITGSSDPYCIVKVDNEVIIRTATVWKTLNPFWGEEYTVHLPPGFHTVSFYVLDE
DTLSRDDVIGKVSLTREVISAHPRGIDGWMNLTEVDPDEEVQGEIHLELSV
>gnl|CDD|173788 cd04056, Peptidases_S53, Peptidase domain in the S53 family. Members of the peptidases S53 (sedolisin) family include endopeptidases and exopeptidases sedolisin, kumamolysin, and (PSCP) Pepstatin-insensitive Carboxyl Proteinase. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase
GYTPADLAALYNIPPLGYTGSGQTIGIIEFGGGYYNPSDLQTFFQLFGLPAPTVFIVVVIGGGNAPGTSS
GWGGEASLDVEYAGAIAPGANITLYFAPGTVTNGPLLAFLAAVLDNPNLPSVISISYGEPEQSLPPAYAQ
RVCNLFAQAAAQGITVLAASGDSGAGGCGGDGSGTGFSVSFPASSPYVTAVGGTTLYTGGTGSSAESTVW
SSEGGWGGSGGGFSNYFPRPSYQSGAVLGLPPSGLYNGSGRGVPDVAANADPGTGYLVVVNGQWYLVGGT
SAAAPLFAGLIALINQARLAAGKPPLGFLNPLLYQLAATAPSAFNDITSGNNGGCGGAGYPAGPGWDPVT
GLGTPNFAKLL
>gnl|CDD|173789 cd04059, Peptidases_S8_Protein_convertases_Kexins_Furin-like, Peptidase S8 family domain in Protein convertases. Protein convertases, whose members include furins and kexins, are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad that is not homologous to trypsin. Kexins are involved in the activation of peptide hormones, growth factors, and viral proteins. Furin cleaves cell surface vasoactive peptides and proteins involved in cardiovascular tissue remodeling in the TGN, at cell surface, or in endosomes but rarely in the ER. Furin also plays a key role in blood pressure regulation though the activation of transforming growth factor (TGF)-beta. High specificity is seen for cleavage after dibasic (Lys-Arg or Arg-Arg) or multiple basic residues in protein convertases. There is also strong sequence conservation
PNDPLFPYQWYLKNTGQAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFN
DNDPDPTPRYDDDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYID
IYSNSWGPDDDGKTVDGPGPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVS
AVTANGVRASYSEVGSSVLASAPSGGSGNPEASIVTTDLGGNCNCTSSHNGTSAAAPLAAGVIALMLEAN
PNLTWRDVQHILALTAR
>gnl|CDD|173790 cd04077, Peptidases_S8_PCSK9_ProteinaseK_like, Peptidase S8 family domain in ProteinaseK-like proteins. The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K
WGLDRISQRDLPLDGTYYYDSSTGSGVDVYVLDTGIRTTHVEFGGRAIWGADFVGGDPDSDCNGHGTHVA
GTVGGKTYGVAKKANLVAVKVLDCNGSGTLSGIIAGLEWVANDATKRGKPAVANMSLGGGASTALDAAVA
AAVNAGVVVVVAAGNSNQDACNYSPASAPEAITVGATDSDDARASFSNYGSCVDIFAPGVDILSAWIGSD
TATATLSGTSMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLATK
>gnl|CDD|271144 cd04078, CBM36_xylanase-like, Carbohydrate Binding Module family 36 (CBM36); appended mainly to glycoside hydrolase family 11 (GH11) domains; xylan binding. This family includes carbohydrate binding module family 36 (CBM36) most of which appear appended to glycoside hydrolase family 11 (GH11) domains. These CBMs are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH11 catalytic modules with their dedicated, insoluble substrates. GH11 domains have xylanase (endo-1,4-beta-xylanase) activity which catalyzes the hydrolysis of beta-1,4 bonds of xylan, the major component of hemicelluloses, to generate xylooligosaccharides and xylose. This family includes XynB from Dictyoglomus thermophilum Rt46B.1 and Xyn11A from Pseudobutyrivibrio xylanivorans Mz5T. Xyn11A is a multicatalytic enzyme with an N-terminal GH11 domain, a CBM36 domain, and a C-terminal putative NodB-like polysaccharide deacetylase which is predicted to be an acetyl esterase involved in debranching activity in the xylan backbone. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. Consistent with its structural and sequence similarity to CBM6, CBM36 binds xylan, but only at binding site I, and in a calcium-dependent manner; the latter suggests its potential application in affinity labeling
ATRVECENMTLGGPYAGKISSPFNGVALYANNDYVSYTQYFANSNHTFSLRGCSNNNNTARVDLRIGGQT
VGTFYFTGTYPTVQTISNITHATGNQTVELIVTADNGTWDVYVDYLEIS
>gnl|CDD|271145 cd04079, CBM6_agarase-like, Carbohydrate Binding Module 6 (CBM6); appended mainly to glycoside hydrolase (GH) family 16 alpha- and beta agarases. This family includes carbohydrate binding module 6 (CBM6) domains that are appended mainly to glycoside hydrolase (GH) family 16 agarases. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the activity of alpha- and beta-agarase catalytic modules which are involved in the hydrolysis of 1,4-beta-D-galactosidic linkages. These CBM6s bind specifically to the non-reducing end of agarose chains, recognizing only the first repeat of the disaccharide, and directing the appended catalytic modules to areas of the plant cell wall attacked by beta-agarases. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. This family includes three tandem CBM6s from the Saccharophagus degradans agarase Aga86E, and three tandem CBM6s from Vibrio sp. strain PO-303 AgaA; in both these proteins these are appended to a GH16 domain. Vibrio AgaA also contains a Big-2-like protein-protein interaction domain. This family also includes two tandem CBM6s from an endo-type beta-agarase from a deep-sea Microbulbifer-like isolate, which are appended to a GH16 domain, and two of three CBM6s of Alteromonas agarilytica AgaA alpha-agarase, which are appended to a GH96 domain
GGTIVIEAESFTATGGTFDDGPDGVSGYSVNGGTAINYVNTGDYADYTVNVPEAGTYSVEYLIGTPVSGA
AIELLVDGNSVATTAVPNTGGWDNFQALTLASTVNLTAGTHTIRLTAAGSNDWQWNLDKFTLTK
>gnl|CDD|271146 cd04080, CBM6_cellulase-like, Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including GH5 (cellulase). This family includes carbohydrate binding module 6 (CBM6) domains that are appended to several glycoside hydrolase (GH) domains, including GH5 (cellulase) and GH16, as well as to coagulation factor 5/8 carbohydrate-binding domains. CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. The CBM6s are appended to GHs that display a diversity of substrate specificities. For some members of this family information is available about the specific substrates of the appended GH domains. It includes the CBM domains of various enzymes involved in cell wall degradation including, an extracellular beta-1,3-glucanase from Lysobacter enzymogenes encoded by the gluC gene (its catalytic domain belongs to the GH16 family), the tandem CBM domains of Pseudomonas sp. PE2 beta-1,3(4)-glucanase A (its catalytic domain also belongs to GH16), and a family 6 CBM from Cellvibrio mixtus Endoglucanase 5A (CmCBM6) which binds to the beta1,4-beta1,3-mixed linked glucans lichenan, and barley beta-glucan, cello-oligosaccharides, insoluble forms of cellulose, the beta1,3-glucan laminarin, and xylooligosaccharides, and the CBM6 of Fibrobacter succinogenes S85 XynD xylanase, appended to a GH10 domain, and Cellvibrio japonicas Cel5G appended to a GH5 (cellulase) domain. GH5 (cellulase) family includes enzymes with several known activities such as endoglucanase, beta-mannanase, and xylanase, which are involved in the degradation of cellulose and xylans. GH16 family includes enzymes with lichenase, xyloglucan endotransglycosylase (XET), and beta-agarase activities. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. For CmCBM6 it has been shown that these two binding sites have different ligand specificities
IPGRIEAEDYDLGGEGVAYHDTTPGNEGGYYRNDGVDIETTSDTGGGYNVGWIDAGEWLEYTVNVPEAGT
YTVSFRVASPSGGGSLSLEVDGGTVLGTVDVPNTGGWQTWQTVTTTVVLLPAGTHTLRLVFVGGGFNLNW
FEFT
>gnl|CDD|271147 cd04081, CBM35_galactosidase-like, Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. This family includes carbohydrate binding module family 35 (CBM35); these are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. Examples of proteins which contain CBM35s belonging to this family includes the CBM35 of an exo-beta-1,3-galactanase from Phanerochaete chrysosporium 9 (Pc1,3Gal43A) which is appended to a GH43 domain, and the CBM35 domain of two bifunctional proteins with beta-L-arabinopyranosidase/alpha-D-galactopyranosidase activities from Fusarium oxysporum 12S, Foap1 and Foap2 (Fo/AP1 and Fo/AP2), that are appended to GH27 domains. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). Some CBM35s bind their ligands in a calcium-dependent manner. In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates, while family GH27 includes alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases
TSYEAEAATLTGSAAAVSCSCGCSGGGAVGVGGGGNGGTVTFNNVTASAAGTYTLTIDYINGDVNDRNAT
VSVNGGAAQRVAFPPTGGWNTPGSVTVLVDLKAGSNTITFSNSGGWAPDIDRITV
>gnl|CDD|271148 cd04082, CBM35_pectate_lyase-like, Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. This family includes carbohydrate binding module family 35 (CBM35) domains that are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. Included in this family are CBM35s of pectate lyases, including pectate lyase 10A from Cellvibrio japonicas, these enzymes release delta-4,5-anhydrogalaturonic acid (delta4,5-GalA) from pectin, thus identifying a signature molecule for plant cell wall degradation. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. Some CBM35s bind their ligands in a calcium-dependent manner, especially those binding uronic acids
LTYQAEDASVDQGVIESNHAGYTGSGFVNTDNAVGSYIEWTVNAPTAGTYTLTFRYANGSTSNRPADISV
NGNTVAATLSFPSTGAWTTWATSSVTVPLNAGTNTIRLTATTAEGLPNIDYLTV
>gnl|CDD|271149 cd04083, CBM35_Lmo2446-like, Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446. This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes. Some CBM35 domains belonging to this family are appended to glycoside hydrolase (GH) family domains, including glycoside hydrolase family 31 (GH31), for example the CBM35 domain of Lmo2446, an uncharacterized protein from Listeria monocytogenes EGD-e. These CBM35s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. GH31 has a wide range of hydrolytic activities such as alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, or alpha-1,4-glucan lyase, cleaving a terminal carbohydrate moiety from a substrate that may be a starch or a glycoprotein. Most characterized GH31 enzymes are alpha-glucosidases
TRYEAENAALSGGAVVNTDHAGYSGTGFVDGFATAGASVTFTVNVPAAGTYTLTLRYANGTGSAKTLSLY
VNGTKVKQVSLPSTGSWDTWGTATETVTLRAGTNTIELRYDAGDSGNVNLDNITV
>gnl|CDD|271150 cd04084, CBM6_xylanase-like, Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 and GH43 xylanase domains. This family includes carbohydrate binding module 6 (CBM6) domains that are appended mainly to glycoside hydrolase (GH) family domains, including GH3, GH11, and GH43 domains. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. Examples of proteins having CMB6s belonging to this family are Microbispora bispora GghA, a 1,4-beta-D-glucan glucohydrolase (GH3); Clostridium thermocellum xylanase U (GH11), and Penicillium purpurogenum ABF3, a bifunctional alpha-L-arabinofuranosidase/xylobiohydrolase (GH43). GH3 comprises enzymes with activities including beta-glucosidase (hydrolyzes beta-galactosidase) and beta-xylosidase (hydrolyzes 1,4-beta-D-xylosidase). GH11 family comprises enzymes with xylanase (endo-1,4-beta-xylanase) activity which catalyze the hydrolysis of beta-1,4 bonds of xylan, the major component of hemicelluloses, to generate xylooligosaccharides and xylose. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold
SRVEAETYADSSGVKTEATGDGGVYVGAIDNGDWIAFKNVDFGSGATSFTARVASAGAGGTIEVRLDSPD
GPLIGTLEVPNTGGWQTWTTVSAPVTGVTGVHDLYLVFKGGGGDLFNLDWFQF
>gnl|CDD|271151 cd04085, delta_endotoxin_C, delta-endotoxin C-terminal domain may be associated with carbohydrate binding functionality. Delta-endotoxin C-terminal domain (delta endotoxin domain III) is part of the activated region of delta endotoxins, which are insecticidal toxins produced during sporulation by Bacillus species of bacteria. The activated endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain (I) is involved in membrane insertion and pore formation, while the second and third domains (II and III) are involved in receptor binding. Domain III structurally resembles the carbohydrate binding domain 6 (CBM6) and it is possible that insect specificity is determined by protein-protein or protein-carbohydrate interactions mediated by both domains II and III of the toxin. Delta-endotoxins are of great interest for development of new bioinsecticides and in the control of mosquitoes
TKSELTRNNTIYPDKITQIPAVKAYSLGNGSSVIKGPGFTGGDLVKLTSNGGGSLKVTVTNSLSQKYRIR
IRYASNTNGTLSVSGGGTTTNSFNFPSTMSSGDNLTYNSFKYVEFPTTFTFNSSSSTIEITIQNSSSGGE
VYIDKIEFIPVD
>gnl|CDD|271152 cd04086, CBM35_mannanase-like, Carbohydrate Binding Module 35 (CBM35); appended to several carbohydrate binding enzymes, including several glycoside hydrolase (GH) family 26 mannanase domains. This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes, including periplasmic component of ABC-type sugar transport system involved in carbohydrate transport and metabolism, and several glycoside hydrolase (GH) domains, including GH26. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. Examples of proteins having CMB35s belonging to this family are mannanase A from Clostridium thermocellum (GH26), Man26B from Paenibacillus sp. BME-14 (GH26), and the multifunctional Cel44C-Man26A from Paenibacillus polymyxa GS01 (which has two GH domains, GH44 and GH26). GH26 mainly includes mannan endo-1,4-beta-mannosidase which hydrolyzes 1,4-beta-D-linkages in mannans, galacto-mannans, glucomannans, and galactoglucomannans, but displays little activity towards other plant cell wall polysaccharides. A few proteins belonging to this family have additional CBM3 domains; these CBM3s are not found in the CBM6-CBM35-CBM36_like superfamily
ITYEAEDGTLTGVTVATSRSGYSGTGYVTGFDDDGDSLTFTVNVPEAGLYDLVIRYAAPYGDKENNLYVN
GTSVGEISFPATTKFTEVSAGKVLLNAGENTITIENSWGWYDIDYITVT
>gnl|CDD|239754 cd04087, PTPA, Phosphotyrosyl phosphatase activator (PTPA) is also known as protein phosphatase 2A (PP2A) phosphatase activator. PTPA is an essential, well conserved protein that stimulates the tyrosyl phosphatase activity of PP2A. It also reactivates the serine/threonine phosphatase activity of an inactive form of PP2A. Together, PTPA and PP2A constitute an ATPase. It has been suggested that PTPA alters the relative specificity of PP2A from phosphoserine/phosphothreonine substrates to phosphotyrosine substrates in an ATP-hydrolysis-dependent manner. Basal expression of PTPA is controlled by the transcription factor Yin Yang1 (YY1). PTPA has been suggested to play a role in the insertion of metals to the PP2A catalytic subunit (PP2Ac) active site, to act as a chaperone, and more recently, to have peptidyl prolyl cis/trans isomerase activity that specifically targets human PP2Ac
DIIAFIQDLSESVQGKPLSDEIPVSENIEKLVEILDQLDALIDETPPIDQPSRFGNKAFRTWHDKLEEEL
PSLLEELLPEELDEAVNELSYYLLESFGNSTRIDYGTGHELNFLAFLCCLFKLGILTEEDYGAIVLRVFN
RYLELVRRLQLTYRLEPAGSHGVWGLDDYQFLPFIFGSAQLINHKPLKPKSILDPEIVEEYKKDYLYLSC
IAFINKVKTGPFAEHSPMLWDISGVPTWSKVNQGLIKMYKAEVLSKFPVVQHFLFG
>gnl|CDD|293905 cd04088, EFG_mtEFG_II, Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation factors G1 and G2. This family represents the domain II of bacterial Elongation factor G (EF-G)and mitochondrial Elongation factors G1 (mtEFG1) and G2 (mtEFG2). During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2
FSALVFKTMADPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHGKKREEVEELGAGDIGAVV
GLKDTRTGDTLCD
>gnl|CDD|293906 cd04089, eRF3_II, Domain II of the eukaryotic class II release factor. In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils
PLRMPILDKYKDMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVE
EEDISPGFVLCS
>gnl|CDD|293907 cd04090, EF2_II_snRNP, Domain II of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component. This subfamily includes domain II of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p. This domain is homologous to domain II of the eukaryotic translational elongation factor EF-2. U5-116 kD is a GTPase which is a component of the spliceosome complex which processes precursor mRNAs to produce mature mRNAs
LVVHVTKLYSSSDGGSFWALGRIYSGTLRKGQKVKVLGENYSLEDEEDMTVCTVGRLWILGARYKYEVNS
APAGNWVLIKGIDQSIVKTATITS
>gnl|CDD|293908 cd04091, mtEFG1_II_like, Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG2s are not present in this group
FVGLAFKLEEGRFGQLTYMRVYQGVLRKGDTIYNVRTGKKVRVPRLVRMHSDEMEDIEEVYAGDICALFG
IDCASGDTFTD
>gnl|CDD|293909 cd04092, mtEFG2_II_like, Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG1s are not present in this group
LCALAFKVIHDPQRGPLVFVRVYSGTLKAGSNVYNTTTGKKERISRLLKMHADQTEEVDSLSAGNIGVIT
GLKVTSTGDTLVS
>gnl|CDD|294008 cd04093, HBS1_C_III, C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1). This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome
PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVV
EIELERPIPLETFKDNKELGRFVLRRGGETIAAGIVTEI
>gnl|CDD|294009 cd04094, eSelB_III, Domain III of eukaryotic and archaeal elongation factor SelB. This model represents the domain III of archaeal and eukaryotic selenocysteine (Sec)-specific eukaryotic elongation factor (eEFSec or eSelB), which is homologous to domain III of EF-Tu. SelB is a specialized translation elongation factor responsible for the co-translational incorporation of selenocysteine into proteins by recoding of a UGA stop codon in the presence of a downstream mRNA hairpin loop, called Sec insertion sequence (SECIS) element
TVTAAIALVCKISFFKGSIKSKSKFHITVGHQTVMARVTFFSDPGKDETEEDESAEFVEDEDESLEEAKP
GSEQYALLEFEKPVAAPPGDLFIGSRLDTDPHSNTCRLAFYGRV
>gnl|CDD|294010 cd04095, CysN_NoDQ_III, Domain III of the large subunit of ATP sulfurylase (ATPS). This model represents domain III of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and is homologous to domain III of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD and CysN. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N- and C-termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha
EVSDQFEATLVWMDEKPLQPGRRYLLKHGTRTVRARVTEIDYRIDVNTLEREPADTLALNDIGRVTLRLA
EPLAFDPYAENRATGSFILIDRLTNATVAAGMI
>gnl|CDD|239763 cd04096, eEF2_snRNP_like_C, eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor 2 (eEF-2) and a homologous domain of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and, its yeast counterpart Snu114p. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. In complex with GTP, EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome
EPIYLVEIQCPEDALGKVYSVLSKRRGHVLSEEPKEGTPLFEIKAYLPVIESFGFETDLRSATSGQAFPQ
LVFSHWEIVP
>gnl|CDD|239764 cd04097, mtEFG1_C, mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in eukaryotes. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s) mtEFG2s are not present in this group
EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGEDEFTLEAEVPLNDMFGYSTELRSMTQGKGEFSME
FSRYAPVP
>gnl|CDD|239765 cd04098, eEF2_C_snRNP, eEF2_C_snRNP: This family includes a C-terminal portion of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and, its yeast counterpart Snu114p. This domain is homologous to the C-terminal domain of the eukaryotic translational elongation factor EF-2. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. In complex with GTP, EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome
EPIYEVEITCPADAVSAVYEVLSRRRGHVIYDTPIPGTPLYEVKAFIPVIESFGFETDLRVHTQGQAFCQ
SVFDHWQIVP
>gnl|CDD|239766 cd04100, Asp_Lys_Asn_RS_N, Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages
EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEFFEEAEKLRTESVVGVTGTVVKRPEGNLAT
GEIELQAEELEVLSK
>gnl|CDD|206688 cd04101, RabL4, Rab GTPase-like family 4 (Rab-like4). RabL4 (Rab-like4) subfamily. RabL4s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL4 lacks a prenylation site at the C-terminus. The specific function of RabL4 remains unknown
AQCAVVGDPAVGKSALVQMFHSDGATFQKNYTMTTGCDLVVKTVPVPDTSDSVELFIFDSAGQELFSDMV
ENVWEQPAVVCVVYDVTNEVSFNNCSRWINRVRTHSHGLHTPGVLVGNKCDLTDRREVDAAQAQALAQAN
TLKFYETSAKEGVGYEAPFLSLARAFH
>gnl|CDD|206689 cd04102, RabL3, Rab GTPase-like family 3 (Rab-like3). RabL3 (Rab-like3) subfamily. RabL3s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL3 lacks a prenylation site at the C-terminus. The specific function of RabL3 remains unknown
VKVLVLGDSGVGKSSLVHLLCKNQVLGNPSWTVGCSVDVRHHTYGEGTPEEKTFYVELWDVGGSVGSAES
VKSTRAVFYNQINGIIFVHDLTNKKSSQNLYRWSLEALNRDTFPAGLLVTNGDYDSEQFAGNPVPLLVIG
TKLDQIPEAKRNWVLTRTAFLSEDFNAEEINLDCTNGRLLAAGSSNAVKLSRFFDKVIEKRYFS
>gnl|CDD|133303 cd04103, Centaurin_gamma, Centaurin gamma (CENTG) GTPase. The centaurins (alpha, beta, gamma, and delta) are large, multi-domain proteins that all contain an ArfGAP domain and ankyrin repeats, and in some cases, numerous additional domains. Centaurin gamma contains an additional GTPase domain near its N-terminus. The specific function of this GTPase domain has not been well characterized, but centaurin gamma 2 (CENTG2) may play a role in the development of autism. Centaurin gamma 1 is also called PIKE (phosphatidyl inositol (PI) 3-kinase enhancer) and centaurin gamma 2 is also known as AGAP (ArfGAP protein with a GTPase-like domain, ankyrin repeats and a Pleckstrin homology domain) or GGAP. Three isoforms of PIKE have been identified. PIKE-S (short) and PIKE-L (long) are brain-specific isoforms, with PIKE-S restricted to the nucleus and PIKE-L found in multiple cellular compartments. A third isoform, PIKE-A was identified in human glioblastoma brain cancers and has been found in various tissues. GGAP has been shown to have high GTPase activity due to a direct intramolecular interaction between the N-terminal GTPase domain and the C-terminal ArfGAP domain. In human tissue, AGAP mRNA was detected in skeletal muscle, kidney, placenta, brain, heart, colon, and lung. Reduced expression levels were also observed in the spleen, liver, and small intestine
LKLGIVGNLRSGKSALVHRYLTGSYVQLESPEGGRFKKEVLVDGQSHLLLIRDEGGAPDAQFAGWVDAVI
FVFSLEDEASFQTVYRLYHQLSSYRNISEIPLILVGTQDAISASNPRVIDDARARQLCADMKRCSYYETC
ATYGLNVERVFQEAAQKI
>gnl|CDD|206690 cd04104, p47_IIGP_like, p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1. The p47 GTPase family consists of several highly homologous proteins, including IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1. They are found in higher eukaryotes where they play a role in immune resistance against intracellular pathogens. p47 proteins exist at low resting levels in mouse cells, but are strongly induced by Type II interferon (IFN-gamma). ITGP is critical for resistance to Toxoplasma gondii infection and in involved in inhibition of Coxsackievirus-B3-induced apoptosis. TGTP was shown to limit vesicular stomatitis virus (VSV) infection of fibroblasts in vitro. IRG-47 is involved in resistance to T. gondii infection. LRG-47 has been implicated in resistance to T. gondii, Listeria monocytogenes, Leishmania, and mycobacterial infections. IIGP1 has been shown to localize to the ER and to the Golgi membranes in IFN-induced cells and inflamed tissues. In macrophages, IIGP1 interacts with hook3, a microtubule binding protein that participates in the organization of the cis-Golgi compartment
PLNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPD
DYLEEMKFSEYDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQ
IRDNCLENLQEAGVSEPPVFLVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN
>gnl|CDD|206691 cd04105, SR_beta, Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP). Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer
PTVLLLGPSDSGKTALFTKLTTGKVRSTVTSIEPNVASFYSNSSKGKKLTLVDVPGHEKLRDKLLEYLKA
SLKAIVFVVDSATFQKNIRDVAEFLYDILTDLEKIKNKIPILIACNKQDLFTAKPAKKIKELLEKEINTL
RESRSKSLESLDGDDGSKDTLGDKGGKDFEFDQLEGEVDFVEGSVKKSKGGIDDIEEWIDEL
>gnl|CDD|133306 cd04106, Rab23_like, Rab GTPase family 23 (Rab23)-like. Rab23-like subfamily. Rab23 is a member of the Rab family of small GTPases. In mouse, Rab23 has been shown to function as a negative regulator in the sonic hedgehog (Shh) signaling pathway. Rab23 mediates the activity of Gli2 and Gli3, transcription factors that regulate Shh signaling in the spinal cord, primarily by preventing Gli2 activation in the absence of Shh ligand. Rab23 also regulates a step in the cytoplasmic signal transduction pathway that mediates the effect of Smoothened (one of two integral membrane proteins that are essential components of the Shh signaling pathway in vertebrates). In humans, Rab23 is expressed in the retina. Mice contain an isoform that shares 93% sequence identity with the human Rab23 and an alternative splicing isoform that is specific to the brain. This isoform causes the murine open brain phenotype, indicating it may have a role in the development of the central nervous system. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
IKVIVVGNGNVGKSSMIQRFVKGIFTKDYKKTIGVDFLEKQIFLRQSDEDVRLMLWDTAGQEEFDAITKA
YYRGAQACILVFSTTDRESFEAIESWKEKVEAECGDIPMVLVQTKIDLLDQAVITNEEAEALAKRLQLPL
FRTSVKDDFNVTELFEYLAEKC
>gnl|CDD|206692 cd04107, Rab32_Rab38, Rab GTPase families 18 (Rab18) and 32 (Rab32). Rab38/Rab32 subfamily. Rab32 and Rab38 are members of the Rab family of small GTPases. Human Rab32 was first identified in platelets but it is expressed in a variety of cell types, where it functions as an A-kinase anchoring protein (AKAP). Rab38 has been shown to be melanocyte-specific. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins
FKVLVIGDLGVGKTSIIKRYVHGVFSQHYKATIGVDFALKVIEWDPNTVVRLQLWDIAGQERFGGMTRVY
YKGAVGAIIVFDVTRPSTFEAVLKWKADLDSKVTLPNGEPIPALLLANKCDLKKERLAKDPEQMDQFCKE
NGFIGWFETSAKENINIEEAMRFLVKNILKNDKGLQSPEPDEDNVIDLKQETTTSKSKSCC
>gnl|CDD|206693 cd04108, Rab36_Rab34, Rab GTPase families 34 (Rab34) and 36 (Rab36). Rab34/Rab36 subfamily. Rab34, found primarily in the Golgi, interacts with its effector, Rab-interacting lysosomal protein (RILP). This enables its participation in microtubular dynenin-dynactin-mediated repositioning of lysosomes from the cell periphery to the Golgi. A Rab34 (Rah) isoform that lacks the consensus GTP-binding region has been identified in mice. This isoform is associated with membrane ruffles and promotes macropinosome formation. Rab36 has been mapped to human chromosome 22q11.2, a region that is homozygously deleted in malignant rhabdoid tumors (MRTs). However, experimental assessments do not implicate Rab36 as a tumor suppressor that would enable tumor formation through a loss-of-function mechanism. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins
SKVIVVGDLSVGKTCLINRFCKDVFDKNYKATIGVDFEMERFEVLGVPFSLQLWDTAGQERFKCIASTYY
RGAQAIIIVFDLTDVASLEHTRQWLEDALKENDPSSVLLFLVGTKKDLSSPAQYALMEQDAIKLAREMKA
EYWAVSALTGENVRDFFFRVASLTFELGCC
>gnl|CDD|206694 cd04109, Rab28, Rab GTPase family 28 (Rab28). Rab28 subfamily. First identified in maize, Rab28 has been shown to be a late embryogenesis-abundant (Lea) protein that is regulated by the plant hormone abcisic acid (ABA). In Arabidopsis, Rab28 is expressed during embryo development and is generally restricted to provascular tissues in mature embryos. Unlike maize Rab28, it is not ABA-inducible. Characterization of the human Rab28 homolog revealed two isoforms, which differ by a 95-base pair insertion, producing an alternative sequence for the 30 amino acids at the C-terminus. The two human isoforms are presumably the result of alternative splicing. Since they differ at the C-terminus but not in the GTP-binding region, they are predicted to be targeted to different cellular locations. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins
IKIVVLGDGASGKTSLIRRFAQEGFGKSYKQTIGLDFFSRRITLPGSLNVTLQVWDIGGQQIGGKMLDKY
IYGAQAVCLVYDITNSQSFENLEDWLSVVKKVNEESETKPKMVLVGNKTDLEHNRQVTAEKHARFAQEND
MESIFVSAKTGDRVFLCFQRIAAELLGVKLSQAELEQSQRVVKADVSRYSERTLREPVSRSVNKRSNSMC
AVM
>gnl|CDD|133310 cd04110, Rab35, Rab GTPase family 35 (Rab35). Rab35 is one of several Rab proteins to be found to participate in the regulation of osteoclast cells in rats. In addition, Rab35 has been identified as a protein that interacts with nucleophosmin-anaplastic lymphoma kinase (NPM-ALK) in human cells. Overexpression of NPM-ALK is a key oncogenic event in some anaplastic large-cell lymphomas; since Rab35 interacts with N|PM-ALK, it may provide a target for cancer treatments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins
RDYDHLFKLLIIGDSGVGKSSLLLRFADNTFSGSYITTIGVDFKIRTVEINGERVKLQIWDTAGQERFRT
ITSTYYRGTHGVIVVYDVTNGESFVNVKRWLQEIEQNCDDVCKVLVGNKNDDPERKVVETEDAYKFAGQM
GISLFETSAKENINVEEMFNCITELVLRAKKDNLAKQQQQQQNDVVKLPKNSKRKKRCC
>gnl|CDD|133311 cd04111, Rab39, Rab GTPase family 39 (Rab39). Found in eukaryotes, Rab39 is mainly found in epithelial cell lines, but is distributed widely in various human tissues and cell lines. It is believed to be a novel Rab protein involved in regulating Golgi-associated vesicular transport during cellular endocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins
YQFRLIVIGDSTVGKSSLLKRFTEGRFAEVSDPTVGVDFFSRLIEIEPGVRIKLQLWDTAGQERFRSITR
SYYRNSVGVLLVFDITNRESFEHVHDWLEEARSHIQPHRPVFILVGHKCDLESQRQVTREEAEKLAKDLG
MKYIETSARTGDNVEEAFELLTQEIYERIKRGELCALDGWDGVKSGFPAGRAFSLEERSPTFASPEKSCC
C
>gnl|CDD|206695 cd04112, Rab26, Rab GTPase family 26 (Rab26). Rab26 subfamily. First identified in rat pancreatic acinar cells, Rab26 is believed to play a role in recruiting mature granules to the plasma membrane upon beta-adrenergic stimulation. Rab26 belongs to the Rab functional group III, which are considered key regulators of intracellular vesicle transport during exocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins
FKVMLVGDSGVGKTCLLVRFKDGAFLAGSFIATVGIQFTNKVVTVDGVKVKLQIWDTAGQERFRSVTHAY
YRDAHALLLLYDVTNKSSFDNIRAWLTEILEYAQSDVVIMLLGNKADMSGERVVKREDGERLAKEYGVPF
METSAKTGLNVELAFTAVAKELKHRSVEQPDEPKFKIQDYVEKQKKSSGCC
>gnl|CDD|206696 cd04113, Rab4, Rab GTPase family 4 (Rab4). Rab4 subfamily. Rab4 has been implicated in numerous functions within the cell. It helps regulate endocytosis through the sorting, recycling, and degradation of early endosomes. Mammalian Rab4 is involved in the regulation of many surface proteins including G-protein-coupled receptors, transferrin receptor, integrins, and surfactant protein A. Experimental data implicate Rab4 in regulation of the recycling of internalized receptors back to the plasma membrane. It is also believed to influence receptor-mediated antigen processing in B-lymphocytes, in calcium-dependent exocytosis in platelets, in alpha-amylase secretion in pancreatic cells, and in insulin-induced translocation of Glut4 from internal vesicles to the cell surface. Rab4 is known to share effector proteins with Rab5 and Rab11. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
FKFLIIGSAGTGKSCLLHQFIENKFKQDSNHTIGVEFGSRVVNVGGKSVKLQIWDTAGQERFRSVTRSYY
RGAAGALLVYDITSRESFNALTNWLTDARTLASPDIVIILVGNKKDLEDDREVTFLEASRFAQENGLLFL
ETSALTGENVEEAFLKCARSI
>gnl|CDD|133314 cd04114, Rab30, Rab GTPase family 30 (Rab30). Rab30 subfamily. Rab30 appears to be associated with the Golgi stack. It is expressed in a wide variety of tissue types and in humans maps to chromosome 11. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
MEDYDFLFKIVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEIKGEKIKLQIWDTAGQERFR
SITQSYYRSANALILTYDITCEESFRCLPEWLREIEQYANNKVITILVGNKIDLAERREVSQQRAEEFSD
AQDMYYLETSAKESDNVEKLFLDLACRLI
>gnl|CDD|133315 cd04115, Rab33B_Rab33A, Rab GTPase family 33 includes Rab33A and Rab33B. Rab33B/Rab33A subfamily. Rab33B is ubiquitously expressed in mouse tissues and cells, where it is localized to the medial Golgi cisternae. It colocalizes with alpha-mannose II. Together with the other cisternal Rabs, Rab6A and Rab6A', it is believed to regulate the Golgi response to stress and is likely a molecular target in stress-activated signaling pathways. Rab33A (previously known as S10) is expressed primarily in the brain and immune system cells. In humans, it is located on the X chromosome at Xq26 and its expression is down-regulated in tuberculosis patients. Experimental evidence suggests that Rab33A is a novel CD8+ T cell factor that likely plays a role in tuberculosis disease processes. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
RIFKIIVIGDSNVGKTCLTYRFCAGRFPERTEATIGVDFRERTVEIDGERIKVQLWDTAGQERFRKSMVQ
HYYRNVHAVVFVYDVTNMASFHSLPSWIEECEQHSLPNEVPRILVGNKCDLREQIQVPTDLAQRFADAHS
MPLFETSAKDPSENDHVEAIFMTLAHKLKS
>gnl|CDD|206697 cd04116, Rab9, Rab GTPase family 9 (Rab9). Rab9 is found in late endosomes, together with mannose 6-phosphate receptors (MPRs) and the tail-interacting protein of 47 kD (TIP47). Rab9 is a key mediator of vesicular transport from late endosomes to the trans-Golgi network (TGN) by redirecting the MPRs. Rab9 has been identified as a key component for the replication of several viruses, including HIV1, Ebola, Marburg, and measles, making it a potential target for inhibiting a variety of viruses. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
GKSSLLKVILLGDGGVGKSSLMNRYVTNKFDTQLFHTIGVEFLNKDLEVDGHFVTLQIWDTAGQERFRSL
RTPFYRGSDCCLLTFSVDDSQSFQNLSNWKKEFIYYADVKEPESFPFVILGNKIDIPERQVSTEEAQAWC
RDNGDYPYFETSAKDATNVAAAFEEAVRRV
>gnl|CDD|206698 cd04117, Rab15, Rab GTPase family 15 (Rab15). Rab15 colocalizes with the transferrin receptor in early endosome compartments, but not with late endosomal markers. It codistributes with Rab4 and Rab5 on early/sorting endosomes, and with Rab11 on pericentriolar recycling endosomes. It is believed to function as an inhibitory GTPase that regulates distinct steps in early endocytic trafficking. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
FRLLLIGDSGVGKTCLLCRFTDNEFHSSHISTIGVDFKMKTIEVDGIKVRIQIWDTAGQERYQTITKQYY
RRAQGIFLVYDISSERSYQHIMKWVSDVDEYAPEGVQKILIGNKADEEQKRQVGDEQGNKLAKEYGMDFF
ETSACTNKNIKESFTRLTELVLQA
>gnl|CDD|133318 cd04118, Rab24, Rab GTPase family 24 (Rab24). Rab24 is distinct from other Rabs in several ways. It exists primarily in the GTP-bound state, having a low intrinsic GTPase activity; it is not efficiently geranyl-geranylated at the C-terminus; it does not form a detectable complex with Rab GDP-dissociation inhibitors (GDIs); and it has recently been shown to undergo tyrosine phosphorylation when overexpressed in vitro. The specific function of Rab24 still remains unknown. It is found in a transport route between ER-cis-Golgi and late endocytic compartments. It is putatively involved in an autophagic pathway, possibly directing misfolded proteins in the ER to degradative pathways. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins
VKVVMLGKESVGKTSLVERYVHHRFLVGPYQNTIGAAFVAKRMVVGERVVTLGIWDTAGSERYEAMSRIY
YRGAKAAIVCYDLTDSSSFERAKFWVKELQNLEEHCKIYLCGTKSDLIEQDRSLRQVDFHDVQDFADEIK
AQHFETSSKTGQNVDELFQKVAEDFVSRANNQMNTEKGVDLGQKKNSYFYSCC
>gnl|CDD|133319 cd04119, RJL, Rab GTPase family J-like (RabJ-like). RJLs are found in many protists and as chimeras with C-terminal DNAJ domains in deuterostome metazoa. They are not found in plants, fungi, and protostome metazoa, suggesting a horizontal gene transfer between protists and deuterostome metazoa. RJLs lack any known membrane targeting signal and contain a degenerate phosphate/magnesium-binding 3 (PM3) motif, suggesting an impaired ability to hydrolyze GTP. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization
IKVISMGNSGVGKSCIIKRYCEGRFVSKYLPTIGIDYGVKKVSVRNKEVRVNFFDLSGHPEYLEVRNEFY
KDTQGVLLVYDVTDRQSFEALDSWLKEMKQEGGPHGNMENIVVVVCANKIDLTKHRAVSEDEGRLWAESK
GFKYFETSACTGEGVNEMFQTLFSSIVD
>gnl|CDD|206699 cd04120, Rab12, Rab GTPase family 12 (Rab12). Rab12 was first identified in canine cells, where it was localized to the Golgi complex. The specific function of Rab12 remains unknown, and inconsistent results about its cellular localization have been reported. More recent studies have identified Rab12 associated with post-Golgi vesicles, or with other small vesicle-like structures but not with the Golgi complex. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins
LQVIIIGSRGVGKTSLMERFTDDTFCEACKSTVGVDFKIKTVELRGKKIRLQIWDTAGQERFNSITSAYY
RSAKGIILVYDITKKETFDDLPKWMKMIDKYASEDAELLLVGNKLDCETDREITRQQGEKFAQQITGMRF
CEASAKDNFNVDEIFLKLVDDILKKMPLDILRNELSNSILSLQPEPEIPPELPPPRPHVRCC
>gnl|CDD|133321 cd04121, Rab40, Rab GTPase family 40 (Rab40) contains Rab40a, Rab40b and Rab40c. The Rab40 subfamily contains Rab40a, Rab40b, and Rab40c, which are all highly homologous. In rat, Rab40c is localized to the perinuclear recycling compartment (PRC), and is distributed in a tissue-specific manor, with high expression in brain, heart, kidney, and testis, low expression in lung and liver, and no expression in spleen and skeletal muscle. Rab40c is highly expressed in differentiated oligodendrocytes but minimally expressed in oligodendrocyte progenitors, suggesting a role in the vesicular transport of myelin components. Unlike most other Ras-superfamily proteins, Rab40c was shown to have a much lower affinity for GTP, and an affinity for GDP that is lower than for GTP. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins
KAYDYLLKFLLVGDSDVGKGEILASLQDGSTESPYGYNMGIDYKTTTILLDGRRVKLQLWDTSGQGRFCT
IFRSYSRGAQGIILVYDITNRWSFDGIDRWIKEIDEHAPGVPKILVGNRLHLAFKRQVATEQAQAYAERN
GMTFFEVSPLCNFNITESFTELARIVLMRHGRPPQSPPQNCSRNSCKIS
>gnl|CDD|133322 cd04122, Rab14, Rab GTPase family 14 (Rab14). Rab14 GTPases are localized to biosynthetic compartments, including the rough ER, the Golgi complex, and the trans-Golgi network, and to endosomal compartments, including early endosomal vacuoles and associated vesicles. Rab14 is believed to function in both the biosynthetic and recycling pathways between the Golgi and endosomal compartments. Rab14 has also been identified on GLUT4 vesicles, and has been suggested to help regulate GLUT4 translocation. In addition, Rab14 is believed to play a role in the regulation of phagocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
YIFKYIIIGDMGVGKSCLLHQFTEKKFMADCPHTIGVEFGTRIIEVNGQKIKLQIWDTAGQERFRAVTRS
YYRGAAGALMVYDITRRSTYNHLSSWLTDARNLTNPNTVIFLIGNKADLEAQRDVTYEEAKQFADENGLL
FLECSAKTGENVEDAFLETAKKIYQN
>gnl|CDD|133323 cd04123, Rab21, Rab GTPase family 21 (Rab21). The localization and function of Rab21 are not clearly defined, with conflicting data reported. Rab21 has been reported to localize in the ER in human intestinal epithelial cells, with partial colocalization with alpha-glucosidase, a late endosomal/lysosomal marker. More recently, Rab21 was shown to colocalize with and affect the morphology of early endosomes. In Dictyostelium, GTP-bound Rab21, together with two novel LIM domain proteins, LimF and ChLim, has been shown to regulate phagocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
FKVVLLGEGRVGKTSLVLRYVENKFNEKHESTTQASFFQKTVNIGGKRIDLAIWDTAGQERYHALGPIYY
RDADGAILVYDITDADSFQKVKKWIKELKQMRGNNISLVIVGNKIDLERQRVVSKSEAEEYAKSVGAKHF
ETSAKTGKGIEELFLSLAKRMI
>gnl|CDD|133324 cd04124, RabL2, Rab GTPase-like family 2 (Rab-like2). RabL2 (Rab-like2) subfamily. RabL2s are novel Rab proteins identified recently which display features that are distinct from other Rabs, and have been termed Rab-like. RabL2 contains RabL2a and RabL2b, two very similar Rab proteins that share _ 98% sequence identity in humans. RabL2b maps to the subtelomeric region of chromosome 22q13.3 and RabL2a maps to 2q13, a region that suggests it is also a subtelomeric gene. Both genes are believed to be expressed ubiquitously, suggesting that RabL2s are the first example of duplicated genes in human proximal subtelomeric regions that are both expressed actively. Like other Rab-like proteins, RabL2s lack a prenylation site at the C-terminus. The specific functions of RabL2a and RabL2b remain unknown. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization
VKIILLGDSAVGKSKLVERFLMDGYEPQQLSTYALTLYKHNAKFEGKTILVDFWDTAGQERFQTMHASYY
HKAHACILVFDVTRKITYKNLSKWYEELREYRPEIPCIVVANKIDLDPSVTQKKFNFAEKHNLPLYYVSA
ADGTNVVKLFQDAIKLAVSYK
>gnl|CDD|133326 cd04126, Rab20, Rab GTPase family 20 (Rab20). Rab20 is one of several Rab proteins that appear to be restricted in expression to the apical domain of murine polarized epithelial cells. It is expressed on the apical side of polarized kidney tubule and intestinal epithelial cells, and in non-polarized cells. It also localizes to vesico-tubular structures below the apical brush border of renal proximal tubule cells and in the apical region of duodenal epithelial cells. Rab20 has also been shown to colocalize with vacuolar H+-ATPases (V-ATPases) in mouse kidney cells, suggesting a role in the regulation of V-ATPase traffic in specific portions of the nephron. It was also shown to be one of several proteins whose expression is upregulated in human myelodysplastic syndrome (MDS) patients. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins
LKVVLLGDMNVGKTSLLHRYMERRFKDTVSTVGGAFYLKQWGPYNISIWDTAGREQFHGLGSMYCRGAAA
VILTYDVSNVQSLEELEDRFLGLTDTANEDCLFAVVGNKLDLTEEGALAGQEKDAGDRVSPEDQRQVTLE
DAKAFYKRINKYKMLDEDLSPAAEKMCFETSAKTGYNVDELFEYLFNLVLPLILAQRAEANRTQGTVNLP
NPKRSKSKCC
>gnl|CDD|206700 cd04127, Rab27A, Rab GTPase family 27a (Rab27a). The Rab27a subfamily consists of Rab27a and its highly homologous isoform, Rab27b. Unlike most Rab proteins whose functions remain poorly defined, Rab27a has many known functions. Rab27a has multiple effector proteins, and depending on which effector it binds, Rab27a has different functions as well as tissue distribution and/or cellular localization. Putative functions have been assigned to Rab27a when associated with the effector proteins Slp1, Slp2, Slp3, Slp4, Slp5, DmSlp, rabphilin, Dm/Ce-rabphilin, Slac2-a, Slac2-b, Slac2-c, Noc2, JFC1, and Munc13-4. Rab27a has been associated with several human diseases, including hemophagocytic syndrome (Griscelli syndrome or GS), Hermansky-Pudlak syndrome, and choroidermia. In the case of GS, a rare, autosomal recessive disease, a Rab27a mutation is directly responsible for the disorder. When Rab27a is localized to the secretory granules of pancreatic beta cells, it is believed to mediate glucose-stimulated insulin secretion, making it a potential target for diabetes therapy. When bound to JFC1 in prostate cells, Rab27a is believed to regulate the exocytosis of prostate- specific markers. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
YDYLIKLLALGDSGVGKTTFLYRYTDNKFNPKFITTVGIDFREKRVVYNSQGPDGTSGKAFRVHLQLWDT
AGQERFRSLTTAFFRDAMGFLLMFDLTSEQSFLNVRNWMSQLQAHAYCENPDIVLIGNKADLPDQREVSE
RQARELADKYGIPYFETSAATGQNVEKAVETLLDLIMKRM
>gnl|CDD|206701 cd04128, Spg1, Septum-promoting GTPase (Spg1). Spg1p. Spg1p (septum-promoting GTPase) was first identified in the fission yeast S. pombe, where it regulates septum formation in the septation initiation network (SIN) through the cdc7 protein kinase. Spg1p is an essential gene that localizes to the spindle pole bodies. When GTP-bound, it binds cdc7 and causes it to translocate to spindle poles. Sid4p (septation initiation defective) is required for localization of Spg1p to the spindle pole body, and the ability of Spg1p to promote septum formation from any point in the cell cycle depends on Sid4p. Spg1p is negatively regulated by Byr4 and cdc16, which form a two-component GTPase activating protein (GAP) for Spg1p. The existence of a SIN-related pathway in plants has been proposed. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization
LKIGLLGDAQIGKTSLMVKYVEGEFDEEYIQTLGVNFMEKTISIRGTEITFSIWDLGGQREFINMLPLVC
KDAVAILFMFDLTRKSTLNSIKEWYRQARGFNKTAIPILVGTKYDLFADLPPEEQEEITKQARKYAKAMK
APLIFCSTSHSINVQKIFKFVLAKVFDLPLTIPEILTVGEPI
>gnl|CDD|206702 cd04129, Rho2, Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases). Rho2 is a fungal GTPase that plays a role in cell morphogenesis, control of cell wall integrity, control of growth polarity, and maintenance of growth direction. Rho2 activates the protein kinase C homolog Pck2, and Pck2 controls Mok1, the major (1-3) alpha-D-glucan synthase. Together with Rho1 (RhoA), Rho2 regulates the construction of the cell wall. Unlike Rho1, Rho2 is not an essential protein, but its overexpression is lethal. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for proper intracellular localization via membrane attachment. As with other Rho family GTPases, the GDP/GTP cycling is regulated by GEFs (guanine nucleotide exchange factors), GAPs (GTPase-activating proteins) and GDIs (guanine nucleotide dissociation inhibitors)
RRKLVIVGDGACGKTSLLYVFTLGEFPEEYHPTVFENYVTDCRVDGKPVQLALWDTAGQEEYERLRPLSY
SKAHVILIGFAIDTPDSLENVRTKWIEEVRRYCPNVPVILVGLKKDLRQEAVAKGNYATDEFVPIQQAKL
VARAIGAKKYMECSALTGEGVDDVFEAATRAALLVRKSGKEEPGANCCII
>gnl|CDD|133330 cd04130, Wrch_1, Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42. Wrch-1 (Wnt-1 responsive Cdc42 homolog) is a Rho family GTPase that shares significant sequence and functional similarity with Cdc42. Wrch-1 was first identified in mouse mammary epithelial cells, where its transcription is upregulated in Wnt-1 transformation. Wrch-1 contains N- and C-terminal extensions relative to cdc42, suggesting potential differences in cellular localization and function. The Wrch-1 N-terminal extension contains putative SH3 domain-binding motifs and has been shown to bind the SH3 domain-containing protein Grb2, which increases the level of active Wrch-1 in cells. Unlike Cdc42, which localizes to the cytosol and perinuclear membranes, Wrch-1 localizes extensively with the plasma membrane and endosomes. The membrane association, localization, and biological activity of Wrch-1 indicate an atypical model of regulation distinct from other Rho family GTPases. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
LKCVLVGDGAVGKTSLIVSYTTNGYPTEYVPTAFDNFSVVVLVDGKPVRLQLCDTAGQDEFDKLRPLCYP
DTDVFLLCFSVVNPSSFQNISEKWIPEIRKHNPKAPIILVGTQADLRTDVNVLIQLARYGEKPVSQSRAK
ALAEKIGACEYIECSALTQKNLKEVFDTAILAG
>gnl|CDD|206703 cd04131, Rnd, Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8. The Rnd subfamily contains Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8. These novel Rho family proteins have substantial structural differences compared to other Rho members, including N- and C-terminal extensions relative to other Rhos. Rnd3/RhoE is farnesylated at the C-terminal prenylation site, unlike most other Rho proteins that are geranylgeranylated. In addition, Rnd members are unable to hydrolyze GTP and are resistant to GAP activity. They are believed to exist only in the GTP-bound conformation, and are antagonists of RhoA activity. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
RCKIVLVGDSQCGKTALLQVFAKDSFPENYVPTVFENYTASFEVDKQRIELSLWDTSGSPYYDNVRPLSY
PDSDAVLICFDISRPETLDSVLKKWKGEVREFCPNTPVLLVGCKSDLRTDLSTLTELSNKRQIPVSHEQG
RNLAKQIGAAAYVECSAKTSENSVRDVFEMATLACL
>gnl|CDD|206704 cd04132, Rho4_like, Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like. Rho4 is a GTPase that controls septum degradation by regulating secretion of Eng1 or Agn1 during cytokinesis. Rho4 also plays a role in cell morphogenesis. Rho4 regulates septation and cell morphology by controlling the actin cytoskeleton and cytoplasmic microtubules. The localization of Rho4 is modulated by Rdi1, which may function as a GDI, and by Rga9, which is believed to function as a GAP. In S. pombe, both Rho4 deletion and Rho4 overexpression result in a defective cell wall, suggesting a role for Rho4 in maintaining cell wall integrity. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins
DLKVKIVVVGDGGCGKTCLLMVYAQGSFPEEYVPTVFENYVTTLQVPNGKIIELALWDTAGQEDYDRLRP
LSYPDVDVILICYSVDNPTSLDNVEDKWYPEVNHFCPGTPIVLVGLKTDLRKDKNSVSKLRAQGLEPVTP
EQGESVAKSIGAVAYIECSAKLMENVDEVFDAAINVALSKSGRAARKKKKKKKCVIL
>gnl|CDD|206705 cd04133, Rop_like, Rho-related protein from plants (Rop)-like. The Rop (Rho-related protein from plants) subfamily plays a role in diverse cellular processes, including cytoskeletal organization, pollen and vegetative cell growth, hormone responses, stress responses, and pathogen resistance. Rops are able to regulate several downstream pathways to amplify a specific signal by acting as master switches early in the signaling cascade. They transmit a variety of extracellular and intracellular signals. Rops are involved in establishing cell polarity in root-hair development, root-hair elongation, pollen-tube growth, cell-shape formation, responses to hormones such as abscisic acid (ABA) and auxin, responses to abiotic stresses such as oxygen deprivation, and disease resistance and disease susceptibility. An individual Rop can have a unique function or an overlapping function shared with other Rop proteins; in addition, a given Rop-regulated function can be controlled by one or multiple Rop proteins. For example, Rop1, Rop3, and Rop5 are all involved in pollen-tube growth; Rop2 plays a role in response to low-oxygen environments, cell-morphology, and root-hair development; root-hair development is also regulated by Rop4 and Rop6; Rop6 is also responsible for ABA response, and ABA response is also regulated by Rop10. Plants retain some of the regulatory mechanisms that are shared by other members of the Rho family, but have also developed a number of unique modes for regulating Rops. Unique RhoGEFs have been identified that are exclusively active toward Rop proteins, such as those containing the domain PRONE (plant-specific Rop nucleotide exchanger). Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
FIKCVTVGDGAVGKTCMLISYTSNTFPTDYVPTVFDNFSANVVVDGNTVNLGLWDTAGQEDYNRLRPLSY
RGADVFLLAFSLISKASYENVLKKWIPELRHYAPGVPIVLVGTKLDLRDDKQFFADHPGAVPITTAQGEE
LRKQIGAAAYIECSSKTQQNVKAVFDAAIKVVL
>gnl|CDD|206706 cd04134, Rho3, Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases). Rho3 is a member of the Rho family found only in fungi. Rho3 is believed to regulate cell polarity by interacting with the diaphanous/formin family protein For3 to control both the actin cytoskeleton and microtubules. Rho3 is also believed to have a direct role in exocytosis that is independent of its role in regulating actin polarity. The function in exocytosis may be two-pronged: first, in the transport of post-Golgi vesicles from the mother cell to the bud, mediated by myosin (Myo2); second, in the docking and fusion of vesicles to the plasma membrane, mediated by an exocyst (Exo70) protein. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins
RKVVVLGDGACGKTSLLNVFTRGYFPQVYEPTVFENYIHDIFVDGLAVELSLWDTAGQEEFDRLRSLSYA
DTHVIMLCFSVDNPDSLENVESKWLAEIRHHCPGVKLVLVALKCDLREPRNERDRGTHTISYEEGLAVAK
RINACRYLECSAKLNRGVNEAFTEAARVALNARPPHPHSRACTIA
>gnl|CDD|206707 cd04135, Tc10, Rho GTPase TC10 (Tc10). TC10 is a Rho family protein that has been shown to induce microspike formation and neurite outgrowth in vitro. Its expression changes dramatically after peripheral nerve injury, suggesting an important role in promoting axonal outgrowth and regeneration. TC10 regulates translocation of insulin-stimulated GLUT4 in adipocytes and has also been shown to bind directly to Golgi COPI coat proteins. GTP-bound TC10 in vitro can bind numerous potential effectors. Depending on its subcellular localization and distinct functional domains, TC10 can differentially regulate two types of filamentous actin in adipocytes. TC10 mRNAs are highly expressed in three types of mouse muscle tissues: leg skeletal muscle, cardiac muscle, and uterus; they were also present in brain, with higher levels in adults than in newborns. TC10 has also been shown to play a role in regulating the expression of cystic fibrosis transmembrane conductance regulator (CFTR) through interactions with CFTR-associated ligand (CAL). The GTP-bound form of TC10 directs the trafficking of CFTR from the juxtanuclear region to the secretory pathway toward the plasma membrane, away from CAL-mediated DFTR degradation in the lysosome. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
LKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLGLYDTAGQEDYDRLRPLSYP
MTDVFLICFSVVNPASFQNVKEEWVPELKEYAPNVPYLLIGTQIDLRDDPKTLARLNDMKEKPITVEQGQ
KLAKEIGACCYVECSALTQKGLKTVFDEAIIAIL
>gnl|CDD|206708 cd04136, Rap_like, Rap-like family consists of Rap1, Rap2 and RSR1. The Rap subfamily consists of the Rap1, Rap2, and RSR1. Rap subfamily proteins perform different cellular functions, depending on the isoform and its subcellular localization. For example, in rat salivary gland, neutrophils, and platelets, Rap1 localizes to secretory granules and is believed to regulate exocytosis or the formation of secretory granules. Rap1 has also been shown to localize in the Golgi of rat fibroblasts, zymogen granules, plasma membrane, and microsomal membrane of the pancreatic acini, as well as in the endocytic compartment of skeletal muscle cells and fibroblasts. Rap1 localizes in the nucleus of human oropharyngeal squamous cell carcinomas (SCCs) and cell lines. Rap1 plays a role in phagocytosis by controlling the binding of adhesion receptors (typically integrins) to their ligands. In yeast, Rap1 has been implicated in multiple functions, including activation and silencing of transcription and maintenance of telomeres. Rap2 is involved in multiple functions, including activation of c-Jun N-terminal kinase (JNK) to regulate the actin cytoskeleton and activation of the Wnt/beta-catenin signaling pathway in embryonic Xenopus. A number of effector proteins for Rap2 have been identified, including isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) and Traf2- and Nck-interacting kinase (TNIK), and the RalGEFs RalGDS, RGL, and Rlf, which also interact with Rap1 and Ras. RSR1 is the fungal homolog of Rap1 and Rap2. In budding yeasts, it is involved in selecting a site for bud growth, which directs the establishment of cell polarization. The Rho family GTPase Cdc42 and its GEF, Cdc24, then establish an axis of polarized growth. It is believed that Cdc42 interacts directly with RSR1 in vivo. In filamentous fungi such as Ashbya gossypii, RSR1 is a key regulator of polar growth in the hypha. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
EYKLVVLGSGGVGKSALTVQFVQGIFVDKYDPTIEDSYRKQIEVDCQQCMLEILDTAGTEQFTAMRDLYI
KNGQGFALVYSITAQQSFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVSKEEGQNLARQWGNCP
FLETSAKSKINVDEIFYDLVRQIN
>gnl|CDD|206709 cd04137, RheB, Ras Homolog Enriched in Brain (RheB) is a small GTPase. Rheb (Ras Homolog Enriched in Brain) subfamily. Rheb was initially identified in rat brain, where its expression is elevated by seizures or by long-term potentiation. It is expressed ubiquitously, with elevated levels in muscle and brain. Rheb functions as an important mediator between the tuberous sclerosis complex proteins, TSC1 and TSC2, and the mammalian target of rapamycin (TOR) kinase to stimulate cell growth. TOR kinase regulates cell growth by controlling nutrient availability, growth factors, and the energy status of the cell. TSC1 and TSC2 form a dimeric complex that has tumor suppressor activity, and TSC2 is a GTPase activating protein (GAP) for Rheb. The TSC1/TSC2 complex inhibits the activation of TOR kinase through Rheb. Rheb has also been shown to induce the formation of large cytoplasmic vacuoles in a process that is dependent on the GTPase cycle of Rheb, but independent of the TOR kinase, suggesting Rheb plays a role in endocytic trafficking that leads to cell growth and cell-cycle progression. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins
QRKIAVLGSRSVGKSSLTVQFVEGHFVESYYPTIENTFSKIITYKGQEYHLEIVDTAGQDEYSILPQKYS
IGIHGYILVYSVTSRKSFEVVKVIYDKILDMLGKESVPIVLVGNKSDLHMERQVSAEEGKKLAESWGAAF
LESSAKENENVEEAFELLIEEIEKVENPLPPGQKSKCSVM
>gnl|CDD|133338 cd04138, H_N_K_Ras_like, Ras GTPase family containing H-Ras,N-Ras and K-Ras4A/4B. H-Ras/N-Ras/K-Ras subfamily. H-Ras, N-Ras, and K-Ras4A/4B are the prototypical members of the Ras family. These isoforms generate distinct signal outputs despite interacting with a common set of activators and effectors, and are strongly associated with oncogenic progression in tumor initiation. Mutated versions of Ras that are insensitive to GAP stimulation (and are therefore constitutively active) are found in a significant fraction of human cancers. Many Ras guanine nucleotide exchange factors (GEFs) have been identified. They are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active (GTP-bound) Ras interacts with several effector proteins that stimulate a variety of diverse cytoplasmic signaling activities. Some are known to positively mediate the oncogenic properties of Ras, including Raf, phosphatidylinositol 3-kinase (PI3K), RalGEFs, and Tiam1. Others are proposed to play negative regulatory roles in oncogenesis, including RASSF and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYM
RTGEGFLCVFAINSRKSFEDIHTYREQIKRVKDSDDVPMVLVGNKCDLAARTVSTRQGQDLAKSYGIPYI
ETSAKTRQGVEEAFYTLVREIR
>gnl|CDD|206710 cd04139, RalA_RalB, Ral (Ras-like) family containing highly homologous RalA and RalB. The Ral (Ras-like) subfamily consists of the highly homologous RalA and RalB. Ral proteins are believed to play a crucial role in tumorigenesis, metastasis, endocytosis, and actin cytoskeleton dynamics. Despite their high sequence similarity (_80% sequence identity), nonoverlapping and opposing functions have been assigned to RalA and RalBs in tumor migration. In human bladder and prostate cancer cells, RalB promotes migration while RalA inhibits it. A Ral-specific set of GEFs has been identified that are activated by Ras binding. This RalGEF activity is enhanced by Ras binding to another of its target proteins, phosphatidylinositol 3-kinase (PI3K). Ral effectors include RLIP76/RalBP1, a Rac/cdc42 GAP, and the exocyst (Sec6/8) complex, a heterooctomeric protein complex that is involved in tethering vesicles to specific sites on the plasma membrane prior to exocytosis. In rat kidney cells, RalB is required for functional assembly of the exocyst and for localizing the exocyst to the leading edge of migrating cells. In human cancer cells, RalA is required to support anchorage-independent proliferation and RalB is required to suppress apoptosis. RalA has been shown to localize to the plasma membrane while RalB is localized to the intracellular vesicles. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
HKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQLNILDTAGQEDYAAIRDNYFR
SGEGFLLVFSITDMESFTALAEFREQILRVKEDDNVPLLLVGNKCDLEDKRQVSVEEAANLAEQWGVNYV
ETSAKTRANVDKVFFDLVREIRQ
>gnl|CDD|206711 cd04140, ARHI_like, A Ras homolog member I (ARHI). ARHI (A Ras homolog member I) is a member of the Ras family with several unique structural and functional properties. ARHI is expressed in normal human ovarian and breast tissue, but its expression is decreased or eliminated in breast and ovarian cancer. ARHI contains an N-terminal extension of 34 residues (human) that is required to retain its tumor suppressive activity. Unlike most other Ras family members, ARHI is maintained in the constitutively active (GTP-bound) state in resting cells and has modest GTPase activity. ARHI inhibits STAT3 (signal transducers and activators of transcription 3), a latent transcription factor whose abnormal activation plays a critical role in oncogenesis. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
DYRVVVFGAGGVGKSSLVLRFVKGTFRESYIPTIEDTYRQVISCSKSICTLQITDTTGSHQFPAMQRLSI
SKGHAFILVYSITSKQSLEELKPIYELICEIKGNNLEKIPIMLVGNKCDESPSREVSSSEGAALARTWNC
AFMETSAKTNHNVQELFQELLNLEK
>gnl|CDD|206712 cd04141, Rit_Rin_Ric, Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related protein which interacts with calmodulin (Ric). Rit (Ras-like protein in all tissues), Rin (Ras-like protein in neurons) and Ric (Ras-related protein which interacts with calmodulin) form a subfamily with several unique structural and functional characteristics. These proteins all lack a the C-terminal CaaX lipid-binding motif typical of Ras family proteins, and Rin and Ric contain calmodulin-binding domains. Rin, which is expressed only in neurons, induces neurite outgrowth in rat pheochromocytoma cells through its association with calmodulin and its activation of endogenous Rac/cdc42. Rit, which is ubiquitously expressed in mammals, inhibits growth-factor withdrawl-mediated apoptosis and induces neurite extension in pheochromocytoma cells. Rit and Rin are both able to form a ternary complex with PAR6, a cell polarity-regulating protein, and Rac/cdc42. This ternary complex is proposed to have physiological function in processes such as tumorigenesis. Activated Ric is likely to signal in parallel with the Ras pathway or stimulate the Ras pathway at some upstream point, and binding of calmodulin to Ric may negatively regulate Ric activity
REYKIVMLGAGGVGKSAVTMQFISHSFPDYHDPTIEDAYKTQARIDNEPALLDILDTAGQAEFTAMRDQY
MRCGEGFIICYSVTDRHSFQEASEFKELITRVRLTEDIPLVLVGNKVDLEQQRQVTTEEGRNLAREFNCP
FFETSAALRFYIDDAFHGLVREIRRKESMPAL
>gnl|CDD|133342 cd04142, RRP22, Ras-related protein on chromosome 22 (RRP22) family. RRP22 (Ras-related protein on chromosome 22) subfamily consists of proteins that inhibit cell growth and promote caspase-independent cell death. Unlike most Ras proteins, RRP22 is down-regulated in many human tumor cells due to promoter methylation. RRP22 localizes to the nucleolus in a GTP-dependent manner, suggesting a novel function in modulating transport of nucleolar components. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Like most Ras family proteins, RRP22 is farnesylated
VRVAVLGAPGVGKTAIVRQFLAQEFPEEYIPTEHRRLYRPAVVLSGRVYDLHILDVPNMQRYPGTAGQEW
MDPRFRGLRNSRAFILVYDICSPDSFHYVKLLRQQILETRPAGNKEPPIVVVGNKRDQQRHRFAPRHVLS
VLVRKSWKCGYLECSAKYNWHILLLFKELLISATTRGRSTHPALRLQGALHRERCSIM
>gnl|CDD|133343 cd04143, Rhes_like, Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1). This subfamily includes Rhes (Ras homolog enriched in striatum) and Dexras1/AGS1 (activator of G-protein signaling 1). These proteins are homologous, but exhibit significant differences in tissue distribution and subcellular localization. Rhes is found primarily in the striatum of the brain, but is also expressed in other areas of the brain, such as the cerebral cortex, hippocampus, inferior colliculus, and cerebellum. Rhes expression is controlled by thyroid hormones. In rat PC12 cells, Rhes is farnesylated and localizes to the plasma membrane. Rhes binds and activates PI3K, and plays a role in coupling serpentine membrane receptors with heterotrimeric G-protein signaling. Rhes has recently been shown to be reduced under conditions of dopamine supersensitivity and may play a role in determining dopamine receptor sensitivity. Dexras1/AGS1 is a dexamethasone-induced Ras protein that is expressed primarily in the brain, with low expression levels in other tissues. Dexras1 localizes primarily to the cytoplasm, and is a critical regulator of the circadian master clock to photic and nonphotic input. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins
YRMVVLGASKVGKTAIVSRFLGGRFEEQYTPTIEDFHRKLYSIRGEVYQLDILDTSGNHPFPAMRRLSIL
TGDVFILVFSLDNRESFEEVCRLREQILETKSCLKNKTKENVKIPMVICGNKADRDFPREVQRDEVEQLV
GGDENCAYFEVSAKKNSNLDEMFRALFSLAKLPNEMSPSLHRKISVQYGDALHKKSRGGSRKRKEGDACG
AVAPFARRPSVHSDLRYIRSKSTGGGQSKDKERCQIQ
>gnl|CDD|133344 cd04144, Ras2, Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases). The Ras2 subfamily, found exclusively in fungi, was first identified in Ustilago maydis. In U. maydis, Ras2 is regulated by Sql2, a protein that is homologous to GEFs (guanine nucleotide exchange factors) of the CDC25 family. Ras2 has been shown to induce filamentous growth, but the signaling cascade through which Ras2 and Sql2 regulate cell morphology is not known. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins
KLVVLGDGGVGKTALTIQLCLNHFVETYDPTIEDSYRKQVVVDGQPCMLEVLDTAGQEEYTALRDQWIRE
GEGFILVYSITSRSTFERVERFREQIQRVKDESAADVPIMIVGNKCDKVYEREVSTEEGAALARRLGCEF
IEASAKTNVNVERAFYTLVRALRQQRQGGQGPKGGPTKKKEKKKRKCVIM
>gnl|CDD|133345 cd04145, M_R_Ras_like, R-Ras2/TC21, M-Ras/R-Ras3. The M-Ras/R-Ras-like subfamily contains R-Ras2/TC21, M-Ras/R-Ras3, and related members of the Ras family. M-Ras is expressed in lympho-hematopoetic cells. It interacts with some of the known Ras effectors, but appears to also have its own effectors. Expression of mutated M-Ras leads to transformation of several types of cell lines, including hematopoietic cells, mammary epithelial cells, and fibroblasts. Overexpression of M-Ras is observed in carcinomas from breast, uterus, thyroid, stomach, colon, kidney, lung, and rectum. In addition, expression of a constitutively active M-Ras mutant in murine bone marrow induces a malignant mast cell leukemia that is distinct from the monocytic leukemia induced by H-Ras. TC21, along with H-Ras, has been shown to regulate the branching morphogenesis of ureteric bud cell branching in mice. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
PTYKLVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCEIDGQWARLDILDTAGQEEFSAMREQY
MRTGEGFLLVFSVTDRGSFEEVDKFHTQILRVKDRDEFPMILVGNKADLEHQRQVSREEGQELARQLKIP
YIETSAKDRVNVDKAFHDLVRVIR
>gnl|CDD|206713 cd04146, RERG_RasL11_like, Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like families. RERG (Ras-related and Estrogen- Regulated Growth inhibitor) and Ras-like 11 are members of a novel subfamily of Ras that were identified based on their behavior in breast and prostate tumors, respectively. RERG expression was decreased or lost in a significant fraction of primary human breast tumors that lack estrogen receptor and are correlated with poor clinical prognosis. Elevated RERG expression correlated with favorable patient outcome in a breast tumor subtype that is positive for estrogen receptor expression. In contrast to most Ras proteins, RERG overexpression inhibited the growth of breast tumor cells in vitro and in vivo. RasL11 was found to be ubiquitously expressed in human tissue, but down-regulated in prostate tumors. Both RERG and RasL11 lack the C-terminal CaaX prenylation motif, where a = an aliphatic amino acid and X = any amino acid, and are localized primarily in the cytoplasm. Both are believed to have tumor suppressor activity
KIAVLGASGVGKSALTVRFLTKRFIGEYEPNLESLYSRQVTIDGEQVSLEIQDTPGQQQNEDPESLERSL
RWADGFVLVYSITDRSSFDVVSQLLQLIREIKKRDGEIPVILVGNKADLLHSRQVSTEEGQKLALELGCL
FFEVSAAENYLEVQNVFHELCREVRR
>gnl|CDD|206714 cd04147, Ras_dva, Ras - dorsal-ventral anterior localization (Ras-dva) family. Ras-dva subfamily. Ras-dva (Ras - dorsal-ventral anterior localization) subfamily consists of a set of proteins characterized only in Xenopus leavis, to date. In Xenopus Ras-dva expression is activated by the transcription factor Otx2 and begins during gastrulation throughout the anterior ectoderm. Ras-dva expression is inhibited in the anterior neural plate by factor Xanf1. Downregulation of Ras-dva results in head development abnormalities through the inhibition of several regulators of the anterior neural plate and folds patterning, including Otx2, BF-1, Xag2, Pax6, Slug, and Sox9. Downregulation of Ras-dva also interferes with the FGF-8a signaling within the anterior ectoderm. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins
RLVFMGAAGVGKTALIQRFLYDTFEPKHRRTVEELHSKEYEVAGVKVTIDILDTSGSYSFPAMRKLSIQN
GDAFALVYSVDDPESFEEVKRLREEILEVKEDKFVPIVVVGNKIDSLAERQVEAADALSTVELDWNNGFV
EASAKDNENVTEVFKELLQQANLPSWLSPALRRRRESAPSEIQRRPPMNKTNSCSVS
>gnl|CDD|206715 cd04148, RGK, Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases. RGK subfamily. The RGK (Rem, Rem2, Rad, Gem/Kir) subfamily of Ras GTPases are expressed in a tissue-specific manner and are dynamically regulated by transcriptional and posttranscriptional mechanisms in response to environmental cues. RGK proteins bind to the beta subunit of L-type calcium channels, causing functional down-regulation of these voltage-dependent calcium channels, and either termination of calcium-dependent secretion or modulation of electrical conduction and contractile function. Inhibition of L-type calcium channels by Rem2 may provide a mechanism for modulating calcium-triggered exocytosis in hormone-secreting cells, and has been proposed to influence the secretion of insulin in pancreatic beta cells. RGK proteins also interact with and inhibit the Rho/Rho kinase pathway to modulate remodeling of the cytoskeleton. Two characteristics of RGK proteins cited in the literature are N-terminal and C-terminal extensions beyond the GTPase domain typical of Ras superfamily members. The N-terminal extension is not conserved among family members; the C-terminal extension is reported to be conserved among the family and lack the CaaX prenylation motif typical of membrane-associated Ras proteins. However, a putative CaaX motif has been identified in the alignment of the C-terminal residues of this CD
YRVVLLGDSGVGKSSLANIFTAGVYEDSAYEASGDDTYERTVSVDGEEATLVVYDHWEQEDGMWLEDSCM
QVGDAYVIVYSVTDRSSFEKASELRIQLRRARQAEDIPIILVGNKSDLVRSREVSVQEGRACAVVFDCKF
IETSAALQHNVDELFEGIVRQVRLRRDSKEKNTRRMASRKRRESITKKAKRFLSKIVAKNNKGMAFKQKS
KSCHDLSVL
>gnl|CDD|206716 cd04149, Arf6, ADP ribosylation factor 6 (Arf6). Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins localize to the plasma membrane, where they perform a wide variety of functions. In its active, GTP-bound form, Arf6 is involved in cell spreading, Rac-induced formation of plasma membrane ruffles, cell migration, wound healing, and Fc-mediated phagocytosis. Arf6 appears to change the actin structure at the plasma membrane by activating Rac, a Rho family protein involved in membrane ruffling. Arf6 is required for and enhances Rac formation of ruffles. Arf6 can regulate dendritic branching in hippocampal neurons, and in yeast it localizes to the growing bud, where it plays a role in polarized growth and bud site selection. In leukocytes, Arf6 is required for chemokine-stimulated migration across endothelial cells. Arf6 also plays a role in down-regulation of beta2-adrenergic receptors and luteinizing hormone receptors by facilitating the release of sequestered arrestin to allow endocytosis. Arf6 is believed to function at multiple sites on the plasma membrane through interaction with a specific set of GEFs, GAPs, and effectors. Arf6 has been implicated in breast cancer and melanoma cell invasion, and in actin remodelling at the invasion site of Chlamydia infection
LSKLFGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLW
RHYYTGTQGLIFVVDSADRDRIDEARQELHRIINDREMRDALLLVFANKQDLPDAMKPHEIQEKLGLTRI
RDRNWYVQPSCATSGDGLYEGLTWLSSN
>gnl|CDD|206717 cd04150, Arf1_5_like, ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5). The Arf1-Arf5-like subfamily contains Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Arfs1-5 are soluble proteins that are crucial for assembling coat proteins during vesicle formation. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned. Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins. Humans, but not rodents and other lower eukaryotes, lack Arf2. Human Arf3 shares 96% sequence identity with Arf1 and is believed to generally function interchangeably with Arf1. Human Arf4 in the activated (GTP-bound) state has been shown to interact with the cytoplasmic domain of epidermal growth factor receptor (EGFR) and mediate the EGF-dependent activation of phospholipase D2 (PLD2), leading to activation of the activator protein 1 (AP-1) transcription factor. Arf4 has also been shown to recognize the C-terminal sorting signal of rhodopsin and regulate its incorporation into specialized post-Golgi rhodopsin transport carriers (RTCs). There is some evidence that Arf5 functions at the early-Golgi and the trans-Golgi to affect Golgi-associated alpha-adaptin homology Arf-binding proteins (GGAs)
MRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQG
LIFVVDSNDRERIGEAREELQRMLNEDELRDAVLLVFANKQDLPNAMSAAEVTDKLGLHSLRNRNWYIQA
TCATSGDGLYEGLDWLSNN
>gnl|CDD|206718 cd04151, Arl1, ADP ribosylation factor 1 (Arf1). Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi complex, where it is believed to recruit effector proteins to the trans-Golgi network. Like most members of the Arf family, Arl1 is myristoylated at its N-terminal helix and mutation of the myristoylation site disrupts Golgi targeting. In humans, the Golgi-localized proteins golgin-97 and golgin-245 have been identified as Arl1 effectors. Golgins are large coiled-coil proteins found in the Golgi, and these golgins contain a C-terminal GRIP domain, which is the site of Arl1 binding. Additional Arl1 effectors include the GARP (Golgi-associated retrograde protein)/VFT (Vps53) vesicle-tethering complex and Arfaptin 2. Arl1 is not required for exocytosis, but appears necessary for trafficking from the endosomes to the Golgi. In Drosophila zygotes, mutation of Arl1 is lethal, and in the host-bloodstream form of Trypanosoma brucei, Arl1 is essential for viability
RILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAI
IYVVDSTDRDRLGISKSELHAMLEEEELKDAVLLVFANKQDMPGALSEAEVAEKLGLSELKDRTWQIFKT
SATKGEGLDEGMDWLVNT
>gnl|CDD|206719 cd04152, Arl4_Arl7, Arf-like 4 (Arl4) and 7 (Arl7) GTPases. Arl4 (Arf-like 4) is highly expressed in testicular germ cells, and is found in the nucleus and nucleolus. In mice, Arl4 is developmentally expressed during embryogenesis, and a role in somite formation and central nervous system differentiation has been proposed. Arl7 has been identified as the only Arf/Arl protein to be induced by agonists of liver X-receptor and retinoid X-receptor and by cholesterol loading in human macrophages. Arl7 is proposed to play a role in transport between a perinuclear compartment and the plasma membrane, apparently linked to the ABCA1-mediated cholesterol secretion pathway. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily
FQSLHIVMLGLDSAGKTTVLYRLKFNEFVNTVPTKGFNTEKIKVSLGNAKGVTFHFWDVGGQEKLRPLWK
SYTRCTDGIVFVVDSVDVERMEEAKTELHKITKFSENQGVPVLVLANKQDLPNALPVSEVEKLLALHELS
SSTPWHVQPACAIIGEGLQEGLEKLYEMILKRRKMLRQQKKKR
>gnl|CDD|133353 cd04153, Arl5_Arl8, Arf-like 5 (Arl5) and 8 (Arl8) GTPases. Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like Arl4 and Arl7, are localized to the nucleus and nucleolus. Arl5 is developmentally regulated during embryogenesis in mice. Human Arl5 interacts with the heterochromatin protein 1-alpha (HP1alpha), a nonhistone chromosomal protein that is associated with heterochromatin and telomeres, and prevents telomere fusion. Arl5 may also play a role in embryonic nuclear dynamics and/or signaling cascades. Arl8 was identified from a fetal cartilage cDNA library. It is found in brain, heart, lung, cartilage, and kidney. No function has been assigned for Arl8 to date
LLFSSLWSLFFPRKEYKVIIVGLDNAGKTTILYQFLLGEVVHTSPTIGSNVEEIVYKNIRFLMWDIGGQE
SLRSSWNTYYTNTDAVILVIDSTDRERLPLTKEELYKMLAHEDLRKAVLLVLANKQDLKGAMTPAEISES
LGLTSIRDHTWHIQGCCALTGEGLPEGLDWIASR
>gnl|CDD|206720 cd04154, Arl2, Arf-like 2 (Arl2) GTPase. Arl2 (Arf-like 2) GTPases are members of the Arf family that bind GDP and GTP with very low affinity. Unlike most Arf family proteins, Arl2 is not myristoylated at its N-terminal helix. The protein PDE-delta, first identified in photoreceptor rod cells, binds specifically to Arl2 and is structurally very similar to RhoGDI. Despite the high structural similarity between Arl2 and Rho proteins and between PDE-delta and RhoGDI, the interactions between the GTPases and their effectors are very different. In its GTP bound form, Arl2 interacts with the protein Binder of Arl2 (BART), and the complex is believed to play a role in mitochondrial adenine nucleotide transport. In its GDP bound form, Arl2 interacts with tubulin- folding Cofactor D; this interaction is believed to play a role in regulation of microtubule dynamics that impact the cytoskeleton, cell division, and cytokinesis
LLTILRKTKQKEREMRILMLGLDNAGKTTILKKFNGEDISTISPTLGFNIKTLEYNGYKLNIWDVGGQKS
LRSYWRNYFESTDALIWVVDSSDRARLEDCKRELQKLLVEERLAGATLLIFANKQDLPGALSPEEIREVL
ELDSIKSHHWRIFGCSAVTGENLLDGIDWLVDD
>gnl|CDD|206721 cd04155, Arl3, Arf-like 3 (Arl3) GTPase. Arl3 (Arf-like 3) is an Arf family protein that differs from most Arf family members in the N-terminal extension. In is inactive, GDP-bound form, the N-terminal extension forms an elongated loop that is hydrophobically anchored into the membrane surface; however, it has been proposed that this region might form a helix in the GTP-bound form. The delta subunit of the rod-specific cyclic GMP phosphodiesterase type 6 (PDEdelta) is an Arl3 effector. Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis via interactions with retinitis pigmentosa 2 (RP2). It has been proposed that RP2 functions in concert with Arl3 to link the cell membrane and the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery. In mice, the absence of Arl3 is associated with abnormal epithelial cell proliferation and cyst formation
LLSILRKLKPSSRQEVRILLLGLDNAGKTTILKQLASEDISHITPTQGFNIKNVQADGFKLNVWDIGGQR
KIRPYWRNYFENTDVLIYVIDSADRKRFEEAGQELVELLEEEKLAGVPVLVFANKQDLLTAAPAEEVAEA
LNLHDIRDRSWHIQACSAKTGEGLQEGMNWVCKN
>gnl|CDD|133356 cd04156, ARLTS1, Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11). ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer
QVLLLGLDSAGKSTLLYKLKHAELVTTIPTVGFNVEMLQLEKHLSLTVWDVGGQEKMRTVWKCYLENTDG
LVYVVDSSDEARLDESQKELKHILKNEHIKGVPVVLLANKQDLPGALTAEEITRRFKLKKYCSDRDWYVQ
PCSAVTGEGLAEAFRKLASF
>gnl|CDD|206722 cd04157, Arl6, Arf-like 6 (Arl6) GTPase. Arl6 (Arf-like 6) forms a subfamily of the Arf family of small GTPases. Arl6 expression is limited to the brain and kidney in adult mice, but it is expressed in the neural plate and somites during embryogenesis, suggesting a possible role for Arl6 in early development. Arl6 is also believed to have a role in cilia or flagella function. Several proteins have been identified that bind Arl6, including Arl6 interacting protein (Arl6ip), and SEC61beta, a subunit of the heterotrimeric conducting channel SEC61p. Based on Arl6 binding to these effectors, Arl6 is also proposed to play a role in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. At least three specific homozygous Arl6 mutations in humans have been found to cause Bardet-Biedl syndrome, a disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily
NILVLGLDNSGKTTIINQLKPSNAQSQNIVPTVGFNVESFKKGNLSFTAFDMSGQGKYRGLWEHYYKNIQ
GIIFVIDSSDRLRMVVAKDELELLLNHPDIKHRRIPILFYANKMDLPDALTAVKITQLLCLENIKDKPWH
IFASSALTGEGLDEGVDWLQAQ
>gnl|CDD|206723 cd04158, ARD1, (ADP-ribosylation factor domain protein 1 (ARD1). ARD1 (ADP-ribosylation factor domain protein 1) is an unusual member of the Arf family. In addition to the C-terminal Arf domain, ARD1 has an additional 46-kDa N-terminal domain that contains a RING finger domain, two predicted B-Boxes, and a coiled-coil protein interaction motif. This domain belongs to the TRIM (tripartite motif) or RBCC (RING, B-Box, coiled-coil) family. Like most Arfs, the ARD1 Arf domain lacks detectable GTPase activity. However, unlike most Arfs, the full-length ARD1 protein has significant GTPase activity due to the GAP (GTPase-activating protein) activity exhibited by the 46-kDa N-terminal domain. The GAP domain of ARD1 is specific for its own Arf domain and does not bind other Arfs. The rate of GDP dissociation from the ARD1 Arf domain is slowed by the adjacent 15 amino acids, which act as a GDI (GDP-dissociation inhibitor) domain. ARD1 is ubiquitously expressed in cells and localizes to the Golgi and to the lysosomal membrane. Two Tyr-based motifs in the Arf domain are responsible for Golgi localization, while the GAP domain controls lysosomal localization
RVVTLGLDGAGKTTILFKLKQDEFMQPIPTIGFNVETVEYKNLKFTIWDVGGKHKLRPLWKHYYLNTQAV
VFVIDSSHRDRVSEAHSELAKLLTEKELRDALLLIFANKQDVAGALSVEEMTELLSLHKLCCGRSWYIQG
CDARSGMGLYEGLDWLSRQLVAAGVLDVA
>gnl|CDD|206724 cd04159, Arl10_like, Arf-like 9 (Arl9) and 10 (Arl10) GTPases. Arl10-like subfamily. Arl9/Arl10 was identified from a human cancer-derived EST dataset. No functional information about the subfamily is available at the current time, but crystal structures of human Arl10b and Arl10c have been solved
EITLVGLQNSGKTTLVNVIASGQFSEDTIPTVGFNMRKVTKGNVTIKVWDLGGQPRFRSMWERYCRGVNA
IVYVVDAADREKLEVAKNELHDLLEKPSLEGIPLLVLGNKNDLPGALSVDELIEQMNLKSITDREVSCYS
ISAKEKTNIDIVLDWLIKH
>gnl|CDD|206725 cd04160, Arfrp1, Arf-related protein 1 (Arfrp1). Arfrp1 (Arf-related protein 1), formerly known as ARP, is a membrane-associated Arf family member that lacks the N-terminal myristoylation motif. Arfrp1 is mainly associated with the trans-Golgi compartment and the trans-Golgi network, where it regulates the targeting of Arl1 and the GRIP domain-containing proteins, golgin-97 and golgin-245, onto Golgi membranes. It is also involved in the anterograde transport of the vesicular stomatitis virus G protein from the Golgi to the plasma membrane, and in the retrograde transport of TGN38 and Shiga toxin from endosomes to the trans-Golgi network. Arfrp1 also inhibits Arf/Sec7-dependent activation of phospholipase D. Deletion of Arfrp1 in mice causes embryonic lethality at the gastrulation stage and apoptosis of mesodermal cells, indicating its importance in development
CVLILGLDNAGKTTFLEQTKTKFSKNYKGLNPSKITPTVGLNIGTIEVGKARLMFWDLGGQEELRSLWDK
YYAESHGVIYVIDSTDRERFNESKSAFEKVINNEALEGVPLLVLANKQDLPDALSVAEIKEVFDDCIALI
GRRDCLVQPVSALEGEGVEEGIEWLVDC
>gnl|CDD|133361 cd04161, Arl2l1_Arl13_like, Arl2-like protein 1 (Arl2l1) and Arl13. Arl2l1 (Arl2-like protein 1) and Arl13 form a subfamily of the Arf family of small GTPases. Arl2l1 was identified in human cells during a search for the gene(s) responsible for Bardet-Biedl syndrome (BBS). Like Arl6, the identified BBS gene, Arl2l1 is proposed to have cilia-specific functions. Arl13 is found on the X chromosome, but its expression has not been confirmed; it may be a pseudogene
TLLTVGLDNAGKTTLVSALQGEIPKKVAPTVGFTPTKLRLDKYEVCIFDLGGGANFRGIWVNYYAEAHGL
VFVVDSSDDDRVQEVKEILRELLQHPRVSGKPILVLANKQDKKNALLGADVIEYLSLEKLVNENKSLCHI
EPCSAIEGLGKKIDPSIVEGLRWLLAA
>gnl|CDD|133362 cd04162, Arl9_Arfrp2_like, Arf-like 9 (Arl9)/Arfrp2-like GTPase. Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first identified as part of the Human Cancer Genome Project. It maps to chromosome 4q12 and is sometimes referred to as Arfrp2 (Arf-related protein 2). This is a novel subfamily identified in human cancers that is uncharacterized to date
QILVLGLDGAGKTSLLHSLSSERSLESVVPTTGFNSVAIPTQDAIMELLEIGGSQNLRKYWKRYLSGSQG
LIFVVDSADSERLPLARQELHQLLQHPPDLPLVVLANKQDLPAARSVQEIHKELELEPIARGRRWILQGT
SLDDDGSPSRMEAVKDLLSQLINL
>gnl|CDD|206726 cd04163, Era, E. coli Ras-like protein (Era) is a multifunctional GTPase. Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA
FKSGFVAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHKPKKKLGE
RMVKAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVKDKEDLLPLLEKLKEL
HPFAEIFPISALKGENVDELLEYIVEYL
>gnl|CDD|206727 cd04164, trmE, trmE is a tRNA modification GTPase. TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance
REGIKVVIAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVIEEEIDLGGIPVRLIDTAGLRETEDEIEK
IGIERAREAIEEADLVLLVVDASEGLDEEDLEILELPAKKPVIVVLNKSDLLSDAEGISELNGKPIIAIS
AKTGEGIDELKEALLELAG
>gnl|CDD|206728 cd04165, GTPBP1_like, GTP binding protein 1 (GTPBP1)-like family includes GTPBP2. Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM
RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLNLFRHKHEVESGRTSSVSNDILGFDSDGEVVNYPDNH
LGELDVEICEKSSKVVTFIDLAGHERYLKTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVP
VFVVVTKIDMTPANVLQETLKDLKRLLKSPGVRKLPVPVKSKDDVVLSASNLSSGRVVPIFQVSNVTGEG
LDLLRRFLNLLPPR
>gnl|CDD|206729 cd04166, CysN_ATPS, CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex. CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN
RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAALERSKSSGTQGEKLDLALLVDGLQAEREQGITIDVAY
RYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNK
MDLVDYDEEVFEEIKADYLAFAASLGIEDITFIPISALEGDNVVSRSENMPWYKGPTLLEHLETVEIAS
>gnl|CDD|206730 cd04167, Snu114p, Snu114p, a spliceosome protein, is a GTPase. Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs
RNVCIAGHLHHGKTSLLDMLIEQTHKRTPSVKLGWKPLRYTDTRKDEQERGISIKSNPISLVLEDSKGKS
YLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDRLILEL
KLPPTDAYYKLRHTIDEINNYIASFSTTEGFLVSPELGNVLFASSKFGFCFTLESFAKKYGLVDSILSHI
PSP
>gnl|CDD|206731 cd04168, TetM_like, Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins. Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB
NIGILAHVDAGKTTLTESLLYTSGAIRELGSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIID
TPGHMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEI
KEKLSPDIVPMQKVGLYPNICDTNNIDDEQIETVAEGNDELLEKYLSGGPLEELELDNELSARIQKASLF
PVYHGSALKGIGIDELLEGITNLFPTS
>gnl|CDD|206732 cd04169, RF3, Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria. Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts
RRRTFAIISHPDAGKTTLTEKLLLFGGAIQEAGAVKARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKG
CVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDP
LELLDEIENELGIDCAPMTWPIGMGKDFKGVYDRYDKEIYLYERGAGGAIKAPEETKGLDDPKLDELLGE
DLAEQLREELELVEGAGPEFDKELFLAGELTPVFFGSALNNFGVQELLDAFVKLAPAP
>gnl|CDD|206733 cd04170, EF-G_bact, Elongation factor G (EF-G) family. Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members
NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDGNTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLID
TPGYADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAAL
REAFGRPVVPIQLPIGEGDEFTGVVDLLSEKAYRYDPGEPSVEIEIPEELKEKVAEAREELLEAVAETDE
ELMEKYLEEGELTEEELRAGLRRALRAGLIVPVFFGSALTGIGVRRLLDALVELAPSP
>gnl|CDD|206734 cd04171, SelB, SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome. SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea
IIGTAGHIDHGKTTLIKALTGIETDRLPEEKKRGITIDLGFAYLDLPDGKRLGFIDVPGHEKFVKNMLAG
AGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDEDRLELVEEEILELLAGTFLADA
PIFPVSSVTGEGIEELKNYLDELAEPQSKD
>gnl|CDD|206735 cd04172, Rnd3_RhoE_Rho8, Rnd3/RhoE/Rho8 GTPases. Rnd3/RhoE/Rho8 subfamily. Rnd3/RhoE/Rho8 is a member of the novel Rho subfamily Rnd, together with Rnd1/Rho6 and Rnd2/Rho7. Rnd3/RhoE is known to bind the serine-threonine kinase ROCK I. Unphosphorylated Rnd3/RhoE associates primarily with membranes, but ROCK I-phosphorylated Rnd3/RhoE localizes in the cytosol. Phosphorylation of Rnd3/RhoE correlates with its activity in disrupting RhoA-induced stress fibers and inhibiting Ras-induced fibroblast transformation. In cells that lack stress fibers, such as macrophages and monocytes, Rnd3/RhoE induces a redistribution of actin, causing morphological changes in the cell. In addition, Rnd3/RhoE has been shown to inhibit cell cycle progression in G1 phase at a point upstream of the pRb family pocket protein checkpoint. Rnd3/RhoE has also been shown to inhibit Ras- and Raf-induced fibroblast transformation. In mammary epithelial tumor cells, Rnd3/RhoE regulates the assembly of the apical junction complex and tight junction formation. Rnd3/RhoE is underexpressed in prostate cancer cells both in vitro and in vivo; re-expression of Rnd3/RhoE suppresses cell cycle progression and increases apoptosis, suggesting it may play a role in tumor suppression. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
NQNVKCKIVVVGDSQCGKTALLHVFAKDCFPENYVPTVFENYTASFEIDTQRIELSLWDTSGSPYYDNVR
PLSYPDSDAVLICFDISRPETLDSVLKKWKGEIQEFCPNTKMLLVGCKSDLRTDVSTLVELSNHRQTPVS
YDQGANMAKQIGAATYIECSALQSENSVRDIFHVATLACVNK
>gnl|CDD|206736 cd04173, Rnd2_Rho7, Rnd2/Rho7 GTPases. Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1/Rho6 and Rnd3/RhoE/Rho8. Rnd2/Rho7 is transiently expressed in radially migrating cells in the brain while they are within the subventricular zone of the hippocampus and cerebral cortex. These migrating cells typically develop into pyramidal neurons. Cells that exogenously expressed Rnd2/Rho7 failed to migrate to upper layers of the brain, suggesting that Rnd2/Rho7 plays a role in the radial migration and morphological changes of developing pyramidal neurons, and that Rnd2/Rho7 degradation is necessary for proper cellular migration. The Rnd2/Rho7 GEF Rapostlin is found primarily in the brain and together with Rnd2/Rho7 induces dendrite branching. Unlike Rnd1/Rho6 and Rnd3/RhoE/Rho8, which are RhoA antagonists, Rnd2/Rho7 binds the GEF Pragmin and significantly stimulates RhoA activity and Rho-A mediated cell contraction. Rnd2/Rho7 is also found to be expressed in spermatocytes and early spermatids, with male-germ-cell Rac GTPase-activating protein (MgcRacGAP), where it localizes to the Golgi-derived pro-acrosomal vesicle. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins
RCKIVVVGDTQCGKTALLHVFAKDNYPESYVPTVFENYTASFEIDKHRIELNMWDTSGSSYYDNVRPLAY
PDSDAVLICFDISRPETLDSVLKKWQGETQEFCPNAKLVLVGCKLDMRTDLSTLRELSKQRLIPVTHEQG
SLLARQLGAVAYVECSSRMSENSVRDVFHVTTLASVRREHPSLKRSTSRRGLKRISQQPLRPVTENTPEI
RKDRAKSCTIM
>gnl|CDD|206737 cd04174, Rnd1_Rho6, Rnd1/Rho6 GTPases. Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2/Rho7 and Rnd3/RhoE/Rho8. Rnd1/Rho6 binds GTP but does not hydrolyze it to GDP, indicating that it is constitutively active. In rat, Rnd1/Rho6 is highly expressed in the cerebral cortex and hippocampus during synapse formation, and plays a role in spine formation. Rnd1/Rho6 is also expressed in the liver and in endothelial cells, and is upregulated in uterine myometrial cells during pregnancy. Like Rnd3/RhoE/Rho8, Rnd1/Rho6 is believed to function as an antagonist to RhoA. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
MKERRNPQPLVVRCKLVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFENYTACLETEEQRVELSLWDTSG
SPYYDNVRPLCYSDSDAVLLCFDISRPEIFDSALKKWRAEILDYCPSTRILLIGCKTDLRTDLSTLMELS
NQKQAPISYEQGCAMAKQLGAEAYLECSAFTSEKSIHSIFRTASLLCINKLSPLAKKSPVRSLSKRLLHL
PSRSELISSTFKKEKAKSCSVM
>gnl|CDD|133375 cd04175, Rap1, Rap1 family GTPase consists of Rap1a and Rap1b isoforms. The Rap1 subgroup is part of the Rap subfamily of the Ras family. It can be further divided into the Rap1a and Rap1b isoforms. In humans, Rap1a and Rap1b share 95% sequence homology, but are products of two different genes located on chromosomes 1 and 12, respectively. Rap1a is sometimes called smg p21 or Krev1 in the older literature. Rap1 proteins are believed to perform different cellular functions, depending on the isoform, its subcellular localization, and the effector proteins it binds. For example, in rat salivary gland, neutrophils, and platelets, Rap1 localizes to secretory granules and is believed to regulate exocytosis or the formation of secretory granules. Rap1 has also been shown to localize in the Golgi of rat fibroblasts, zymogen granules, plasma membrane, and the microsomal membrane of pancreatic acini, as well as in the endocytic compartment of skeletal muscle cells and fibroblasts. High expression of Rap1 has been observed in the nucleus of human oropharyngeal squamous cell carcinomas (SCCs) and cell lines; interestingly, in the SCCs, the active GTP-bound form localized to the nucleus, while the inactive GDP-bound form localized to the cytoplasm. Rap1 plays a role in phagocytosis by controlling the binding of adhesion receptors (typically integrins) to their ligands. In yeast, Rap1 has been implicated in multiple functions, including activation and silencing of transcription and maintenance of telomeres. Rap1a, which is stimulated by T-cell receptor (TCR) activation, is a positive regulator of T cells by directing integrin activation and augmenting lymphocyte responses. In murine hippocampal neurons, Rap1b determines which neurite will become the axon and directs the recruitment of Cdc42, which is required for formation of dendrites and axons. In murine platelets, Rap1b is required for normal homeostasis in vivo and is involved in integrin activation. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
EYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYM
KNGQGFVLVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWGCAF
LETSAKAKINVNEIFYDLVRQINR
>gnl|CDD|133376 cd04176, Rap2, Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c. The Rap2 subgroup is part of the Rap subfamily of the Ras family. It consists of Rap2a, Rap2b, and Rap2c. Both isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) and Traf2- and Nck-interacting kinase (TNIK) are putative effectors of Rap2 in mediating the activation of c-Jun N-terminal kinase (JNK) to regulate the actin cytoskeleton. In human platelets, Rap2 was shown to interact with the cytoskeleton by binding the actin filaments. In embryonic Xenopus development, Rap2 is necessary for the Wnt/beta-catenin signaling pathway. The Rap2 interacting protein 9 (RPIP9) is highly expressed in human breast carcinomas and correlates with a poor prognosis, suggesting a role for Rap2 in breast cancer oncogenesis. Rap2b, but not Rap2a, Rap2c, Rap1a, or Rap1b, is expressed in human red blood cells, where it is believed to be involved in vesiculation. A number of additional effector proteins for Rap2 have been identified, including the RalGEFs RalGDS, RGL, and Rlf, which also interact with Rap1 and Ras. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation
EYKVVVLGSGGVGKSALTVQFVSGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYI
KNGQGFIVVYSLVNQQTFQDIKPMRDQIVRVKGYEKVPIILVGNKVDLESEREVSSAEGRALAEEWGCPF
METSAKSKTMVNELFAEIVRQMN
>gnl|CDD|133377 cd04177, RSR1, RSR1/Bud1p family GTPase. RSR1/Bud1p is a member of the Rap subfamily of the Ras family that is found in fungi. In budding yeasts, RSR1 is involved in selecting a site for bud growth on the cell cortex, which directs the establishment of cell polarization. The Rho family GTPase cdc42 and its GEF, cdc24, then establish an axis of polarized growth by organizing the actin cytoskeleton and secretory apparatus at the bud site. It is believed that cdc42 interacts directly with RSR1 in vivo. In filamentous fungi, polar growth occurs at the tips of hypha and at novel growth sites along the extending hypha. In Ashbya gossypii, RSR1 is a key regulator of hyphal growth, localizing at the tip region and regulating in apical polarization of the actin cytoskeleton. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins
DYKIVVLGAGGVGKSALTVQFVQNVFIESYDPTIEDSYRKQVEIDGRQCDLEILDTAGTEQFTAMRELYI
KSGQGFLLVYSVTSEASLNELGELREQVLRIKDSDNVPMVLVGNKADLEDDRQVSREDGVSLSQQWGNVP
FYETSARKRTNVDEVFIDLVRQIICVIM
>gnl|CDD|206753 cd04178, Nucleostemin_like, A circularly permuted subfamily of the Ras GTPases. Nucleostemin (NS) is a nucleolar protein that functions as a regulator of cell growth and proliferation in stem cells and in several types of cancer cells, but is not expressed in the differentiated cells of most mammalian adult tissues. NS shuttles between the nucleolus and nucleoplasm bidirectionally at a rate that is fast and independent of cell type. Lowering GTP levels decreases the nucleolar retention of NS, and expression of NS is abruptly down-regulated during differentiation prior to terminal cell division. Found only in eukaryotes, NS consists of an N-terminal basic domain, a coiled-coil domain, a GTP-binding domain, an intermediate domain, and a C-terminal acidic domain. Experimental evidence indicates that NS uses its GTP-binding property as a molecular switch to control the transition between the nucleolus and nucleoplasm, and this process involves interaction between the basic, GTP-binding, and intermediate domains of the protein
DVILEVLDARDPLGCRCPQVERAVLVLGPNKKLVLVLNKIDLVPKENVEKWLKYLRNEFPTVAFKASTQQ
QKKNLSRKSKKVKASDDLLSSSACLGADALLKLLKNYARNKGIKTSITVGVVGYPNVGKSSVINSLKRSR
ACNVGATPGVTKSMQEVHLDKHVKLLDSPGV
>gnl|CDD|133022 cd04179, DPM_DPG-synthase_like, DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily
VVIPAYNEEENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAA
VRAGFKAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGAGMPLLRRLGSRLFNFLI
RLLLGVRISDTQSGFRLFRREVLEALLSLLESNGFEFGLELLVGA
>gnl|CDD|133023 cd04180, UGPase_euk_like, Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes. This family includes UDP-Glucose Pyrophosphorylase (UDPase) and UDPGlcNAc pyrophosphorylase enzymes. The two enzymes share significant sequence and structure similarity. UDP-Glucose Pyrophosphorylase catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from Glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids, glycoproteins, and proteoglycans . UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1P from PPi and UDPGlcNAc, which is a key precursor of N- and O-linked glycosylations and is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker anchoring a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis
VAVVLLAGGLGTRLGKDGPKSSTDVGLPSGQCFLQLIGEKILTLQEIDLYSCKIPEQLMNSKYTHEKTQC
YFEKINQKNSYVITFMQGKLPLKNDDDARDPHNKTKCHLFPCGHGDVVLALIHSGHLNKLLEKGYRYIHF
IGVDNLLVKVADPLFIGIAIQNRKAINQKVVPKTRNEESGGYRIANINGRVQLLEYDQIKKLLKQKMVNN
QIPKDIDDAPFFLFNTNNLINFLVEFKDRVDDIIEFTDDIVGVMVHRAEEFAPVKN
>gnl|CDD|133024 cd04181, NTP_transferase, NTP_transferases catalyze the transfer of nucleotides onto phosphosugars. Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides
AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGV
NIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSRYG
VVELDDDGRVTRFVEKPTLPESNLANAGIYIFEPEILDYIPEILPRGEDELTDAIPLLIEEGKVYGYPVD
GYWLDIG
>gnl|CDD|133025 cd04182, GT_2_like_f, GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families
IAAIILAAGRSSRMGGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINP
DWEEGMSSSLAAGLEALPADADAVLILLADQPLVTAETLRALIDAFREDGAGIVAPVYQGRRGHPVLFPR
SLFPELLALSGDKGARSLLRAHPDRVVVEVDDPGVLIDIDTPEDLR
>gnl|CDD|133026 cd04183, GT2_BcE_like, GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule. GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds
IIIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICRDEHNTKFHLDESLKLLAP
NATVVELDGETLGAACTVLLAADLIDNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHPRW
SYVKLDENGRVIETAEKEPISDLATAGLYYFKSGSLFVEAAKKMIRKDDSVNGEFYISPLYNELILDGKK
VGIYLIDKDDYHSFGTPEDLE
>gnl|CDD|133027 cd04184, GT2_RfbC_Mx_like, Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis. The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds
PLISIVMPVYNTPEKYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGG
ISAATNSALELATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSEPFFKPDWS
PDLLLSQNYIGHLLVYRRSLVRQVGGFREGFEGAQDYDLVLRVSEHTDRIAHIPRVLYHWRA
>gnl|CDD|133028 cd04185, GT_2_like_b, Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families
AVVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLDNIVYLRLPENLGGAGGFYE
GVRRAYELGYDWIWLMDDDAIPDPDALEKLLAYADKDNPQFLAPLVLDPDGSFVGVLISRRVVEKIGLPD
KEFFIWGDDTEYTLRASKAGPGIYVPDAVVVHKTAINKGSSAVVNIDPPWKLYYGVRNRIYL
>gnl|CDD|133029 cd04186, GT_2_like_c, Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families
IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGI
REAKGDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIVGPKVSGAFLLVRREVFEEVGGFDEDFFLYYED
VDLCLRARLAGYRVLYVPQAVIYHHG
>gnl|CDD|133030 cd04187, DPM1_like_bac, Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily
IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQA
ALLAGLDHARGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKESWLKRLTSKLFYRLINKLS
GVDIPDNGGDFRLMDRKVVDALLLLPERHRFLRGLIAWVGF
>gnl|CDD|133031 cd04188, DPG_synthase, DPG_synthase is involved in protein N-linked glycosylation. UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate
VVIPAYNEEKRLPPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLTLPKNRGK
GGAVRAGMLAARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHLASAAVVKRSWLRNLLGRG
FNFLVRLLLGLGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGS
K
>gnl|CDD|133032 cd04189, G1P_TT_long, G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase. This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose
MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRF
GVRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAEVEDPRR
FGVAVVDDGRIVRLVEKPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGY
SIVTGWWKDTGTPEDLLEANRLLLDK
>gnl|CDD|133033 cd04190, Chitin_synth_C, C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin. Chitin synthase, also called UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyltransferase, catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of GlcNAc residues formed by covalent beta-1,4 linkages. Chitin is an important component of the cell wall of fungi and bacteria and it is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases. Studies with fungi have revealed that most of them contain more than one chitin synthase gene. At least five subclasses of chitin synthases have been identified
VCVTMYNEDEEELARTLDSILKNDYPFCARGGDSWKKIVVCVIFDGAIKKNRGKRDSQLWFFNYFCRVLF
PDDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMYQVFEYAISHWLDKAFE
SVFGFVTCLPGCFSMYRIEALKGDNGGKGPLLDYAYLTNTVDSLHKKNNLDLGEDRILCTLLLKAGPKRK
YLYVPGAVAETDVPETFVELLSQRRRWINSTIAN
>gnl|CDD|133034 cd04191, Glucan_BSP_MdoH, Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan. Periplasmic Glucan Biosynthesis protein MdoH is a glucosyltransferase that catalyzes the elongation of beta-1,2 polyglucose chains of glucan, requiring a beta-glucoside as a primer and UDP-glucose as a substrate. Glucans are composed of 5 to 10 units of glucose forming a highly branched structure, where beta-1,2-linked glucose constitutes a linear backbone to which branches are attached by beta-1,6 linkages. In Escherichia coli, glucans are located in the periplasmic space, functioning as regulator of osmolarity. It is synthesized at a maximum when cells are grown in a medium with low osmolarity. It has been shown to span the cytoplasmic membrane
TAIVMPVYNEDPARVFAGLRAMYESLAKTGLADHFDFFILSDTRDPDIWLAEEAAWLDLCEELGAQGRIY
YRRRRENTGRKAGNIADFCRRWGSRYDYMVVLDADSLMSGDTIVRLVRRMEANPRAGIIQTAPKLIGAET
LFARLQQFANRLYGPVFGRGLAAWQGGEGNYWGHNAIIRVAAFMEHCALPVLPGRPPFGGHILSHDFVEA
ALMRRAGWEVRLAPDLEGSYEECPPTLIDFLKRDRRWCQGNLQH
>gnl|CDD|133035 cd04192, GT_2_like_e, Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families
VVIAARNEAENLPRLLQSLSALDYPKEKFEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNSRVSISGK
KNALTTAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFKGKSLLAKFQRLDWLSLL
GLIAGSFGLGKPFMCNGANMAYRKEAFFEVGGFEGNDHIASGDDELLLAKVASKYPKVAYLKNPEALVTT
QPVTSWKELLNQRKRWASK
>gnl|CDD|133036 cd04193, UDPGlcNAc_PPase, UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc. UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1 to PPi and UDPGlcNAc. UDP-N-acetylglucosamine (UDPGlcNAc), the activated form of GlcNAc, is a key precursor of N- and O-linked glycosylations. It is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker which anchors a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis. Human UAP has two isoforms, resulting from alternative splicing of a single gene and differing by the presence or absence of 17 amino acids. UDPGlcNAc pyrophosphorylase shares significant sequence and structure conservation with UDPglucose pyrophosphorylase
KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKK
VPIPWYIMTSEATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLY
KALQTAGILEDMKKRGIKYIHVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDG
KPQVVEYSEISDELAEKRDADGELQYNAGNIANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGL
VKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLKNAD
>gnl|CDD|133037 cd04194, GT8_A4GalT_like, A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS
MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFK
FFPATTDHISYATYYRLLIPDLLPDYDKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKKRK
RRLGGYDDGSYFNSGVLLINLKKWREENITEKLLELIKEYGGRLIYPDQDILNAVLKDKILYLPPRYNFQ
TGFYYLLKKKSKEEQELEEARKNPVIIHYTGSDKPWNK
>gnl|CDD|133038 cd04195, GT2_AmsE_like, GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis. AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds
SVLMSVYIKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGK
ALNEGLKHCTYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRRLPTSHDDI
LKFARRRSPFNHPTVMFRKSKVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVKAR
>gnl|CDD|133039 cd04196, GT_2_like_d, Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families
AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNLGVARN
FESLLQAADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELVDENGNPIGESFFEYQKIKPG
TSFNNLLFQNVVTGCTMAFNRELLELALPFPDADVIMHDWWLALLASAFGKVVFLDEPLILYRQHGNNVV
GANK
>gnl|CDD|133040 cd04197, eIF-2B_epsilon_N, The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2. N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex
LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWS
KPKSSLMIVIIIMSEDCRSLGDALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERRKKDKNAIMT
MVLKEASPPHRTRRTGEEFVIAVDPKTSRLLHYEELPGSKYRSITDLPSELLGSNSEVEIRHDLLDCHID
ICSPDVL
>gnl|CDD|133041 cd04198, eIF-2B_gamma_N, The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2. N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex
FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPL
NLKQKLDEVTIVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPV
SSEQKGGKGKSKKADERDVIGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFK
RWVL
>gnl|CDD|259862 cd04199, CuRO_1_ceruloplasmin_like, Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins. This family includes the first, third, and fifth cupredoxin domains of ceruloplasmin and similar proteins including the first, third and fifth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. It functions in copper transport, amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. Human Factor VIII facilitates blood clotting by acting as a cofactor for factor IXa. Factor VIII and IXa forms a complex in the presence of Ca+2 and phospholipids that converts factor X to the activated form Xa
RHYYIAAEEIDWDYAPSGLAEKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGP
TIRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEES
GPTKGDPACLTWAYYSHVDLEKDINSGLIGPLLICKK
>gnl|CDD|259863 cd04200, CuRO_2_ceruloplasmin_like, Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins. This family includes the second, fourth and sixth cupredoxin domains of ceruloplasmin and similar proteins, including the second, fourth, and sixth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. Ceruloplasmin also functions in copper transport, amine oxidase and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. Human Factor VIII facilitates blood clotting by acting as a cofactor for factor IXa Factor VIII and IXa forms a complex in the presence of Ca+2 and phospholipids that converts factor X to the activated form Xa
DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRW
HLLGMGNEVDVHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFL
V
>gnl|CDD|259864 cd04201, CuRO_1_CuNIR_like, Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase. Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center, which serves as the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis. The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles two domain nitrite reductase in both sequence homology and structure similarity. It consists of two domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of larger laccases
KVEVDMETVEKTMQLDDGVEYRYWTFDGDIPGPMLRVREGDTVELHFSNNPSSTMPHNIDFHAATGAGGG
AGATFIAPGETSTFSFKATQPGLYVYHCAVAPVPMHIANGMYGLILVEPK
>gnl|CDD|259865 cd04202, CuRO_D2_2dMcoN_like, The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins. This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. The biological function of McoN has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals
DRDYTLVLQEWFVDPGTTPMPPEGMDFNYFTINGKSFPATPPLVVKEGDRVRIRLINLSMDHHPMHLHGH
FFLVTATDGGPIPGSAPWPKDTLNVAPGERYDIEFVADNPGDWMFHCHKLHHAMNGMGGGMMTLIGYE
>gnl|CDD|259866 cd04203, Cupredoxin_like_3, Uncharacterized subfamiy of Cupredoxin. Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. Majority of family members contain multiple cupredoxin domain repeats: ceruloplamin and coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, and spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase and the periplasmic domain of cytochrome c oxidase subunit II. Proteins of this uncharacterized subfamily contain a single cupredoxin domain
VVKITLNDDYFNPNVITVPINEKTTLILHNKGQKSEETETIKKLGIDVVVESEEINITVKPLSPGTYELI
CRYHLLGXEGKVIV
>gnl|CDD|259867 cd04204, Pseudoazurin_like, Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin. The Pseudocyanin-like family of copper-binding proteins (or blue (type 1) copper domain) is a family of small proteins that bind a single copper atom and are characterized by an intense electronic absorption band near 600 nm. Pseudoazurin (PAz) has been identified as a electron donor in the denitrification pathway. For example, PAz acts as an electron donor to cytochrome c peroxidase and N2OR from Paracoccus pantotrophus (Pp), and to the copper containing nitrite reductase (NiR) that catalyzes the second step of denitrification. Plastocyanin is found in cyanobacteria, higher plants, and some algae where it plays a role in photosynthesis. Plastocyanin is responsible for transporting electrons from PSII to PSI. This family also includes halocyanins found in halophilic archaea such as Natronomonas pharaonis (Natronobacterium pharaonis) and amicyanin found in bacteria Paracoccus denitrificans
VVVKMGADNGAMAFEPAAIRVDAGETVEFVNTGGGPHNVVFDKEIVPDGDAEFESDRVDEEGFTYEQTFD
EPGVYGYYCTPHRGAGMVGTVI
>gnl|CDD|259868 cd04205, CuRO_2_LCC_like, Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
RVLLLSDWYHDSAEDVLAGYMPNSFGNEPVPDSLLINGRGRFNCSMAVCNSGCPLPVITVEPGKTYRLRL
INAGSFASFNFAIDGHNMTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKADQPPGNYWIRASADGRTFDE
GGNPNGTAILRY
>gnl|CDD|259869 cd04206, CuRO_1_LCC_like, Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins
REYELTITETTVNPDGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNLPNEPTSIHWHGLRQPGTNDGD
GVAGLTQCPIPPGESFTYRFTVDDQAGTFWYHSHVGGQRADGLYGPLIVE
>gnl|CDD|259870 cd04207, CuRO_3_LCC_like, Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 2, 4, and 6 of the 6-domain MCO ceruloplasmin and similar proteins
DRTRRLVLSQTGAPDGTTRWVINGMPFKEGDANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFWV
LGSGGGPFDAPLNLTNPPWRDTVLVPPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVFE
>gnl|CDD|259871 cd04208, CuRO_2_CuNIR, Cupredoxin domain 2 of Copper-containing nitrite reductase. Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center in the protein. The type 2 copper center of a copper nitrite reductase is the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis
VDREYYLVQSELYTGGDDGGVGLFDYAKMLDEKPDYVVFNGRVFAYTGTNPLQAKVGERVRIYVVNAGPN
LTSSFHVIGGIFDRVYPEGSNPNNPLRGVQTVLVPPGGGAIVEFTFPVPGNYALVDHALSRAEKGALGVL
KVE
>gnl|CDD|259872 cd04210, Cupredoxin_like_1, Uncharacterized Cupredoxin-like subfamily. Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins because they have an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. Majority of family members contain multiple cupredoxin domain repeats; ceruloplasmin and coagulation factors V/VIII have six repeats; Laccase, ascorbate oxidase, and spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase and the periplasmic domain of cytochrome c oxidase subunit II
QEIKISLGNAANALRFFPDQLEFEAGKRYKLHLHNPSQLKHYFTAKDFADAIWTRKVDAGGVEIKGAIRE
LELKPGAEAEWQFVPLKTGKYDLRCTIPGHAEAGMTGQITI
>gnl|CDD|259873 cd04211, Cupredoxin_like_2, Uncharacterized Cupredoxin-like subfamily. Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins because they have an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. Majority of family members contain multiple cupredoxin domain repeats; ceruloplasmin and coagulation factors V/VIII have six repeats; Laccase, ascorbate oxidase, and spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase and the periplasmic domain of cytochrome c oxidase subunit II
TRTIEVTMSDTMRFTPDSIQVKQGETVRFVVTNNGKIPHEFVIGTAAELKEHAEMMRKHPGMEHDEPNMV
SLAPGKSGEIVWTFTKAGTFEFACLIPGHYEAGMVGKVTV
>gnl|CDD|259874 cd04212, CuRO_UO_II, The cupredoxin domain of Ubiquinol oxidase subunit II. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved
LEIQVVSLDWKWLFIYPEQGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLI
ADKPGTYQGLSANYSGEGFSDMKFKVLAV
>gnl|CDD|259875 cd04213, CuRO_CcO_Caa3_II, The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I
ALTIEVTGHQWWWEFRYPDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNR
LWLQADEPGVYRGQCAEFCGASHALMRFKVIAL
>gnl|CDD|259876 cd04214, PAD_N, N-terminal non-catalytic domain of protein-arginine deiminase. The N-terminal non-catalytic domain of protein-arginine deiminase has a cupredoxin-like fold, but lacks the Cu binding site. PAD (protein-arginine deiminase) and protein L-arginine iminohydrolase catalyze the conversion of protein arginine residues to citrulline residues post-translationally in a process called citrullination. The modification plays crucial regulatory roles in development and cell differentiation
LRLDTGSRTHAVCVLGTETTLDIYGSAPAGATSFSVKASPGVVVDVAHSPPAKKEPTGLWPWPLDTDVEV
TMTMKAASKEVNDSKVRVSYYGPKEDAPLGKAVLYLTG
>gnl|CDD|259877 cd04215, Nitrosocyanin, Nitrosocyanin (NC) is a mononuclear red copper protein. Nitrosocyanin (NC) is isolated from the ammonia oxidizing bacterium Nitrosomonas europaea. Nitrosocyanin exhibits remote sequence homology to classic blue copper proteins; its spectroscopic and electrochemical properties are different. The structure of NC is a trimer of single domain cupredoxins. Nitroscocyanin may mediate electron transfer. It could have a novel role as a nitric oxide dehydrogenase or a nitric oxide reductase in the oxidation of ammonia
FVVVGNAYDTTIPELNVEGVTVKNIRAFNVLNEPETLKVKKGDVVKITVENKSPISEGFSIDAFGVQEVI
KAGETKTISFRADKAGAFTIWCQLHPKNIHLPGVLNV
>gnl|CDD|259878 cd04216, Phytocyanin, Phytocyanins are plant blue or type I copper proteins. Phytocyanins are plant blue or type I copper proteins. They are involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Phytocyanins are classified into four groups: stellacyanin, plantacyanin, uclacyanin and early nodulin groups. Stellacyanin appears to be associated with the plant cell wall; it may be involved in oxidative reactions to build polymeric material making up the cell wall. Plantacyanin is shown to play a role in reproduction in Arabidopsis. Plantacyanins may also be stress-related proteins and may be involved in plant defense responses. The early nodulin-like protein (OsENODL1) from Oryza sativa is expressed specifically at the late developmental stage of the seeds
TDYTVGDSNGWDLPVNYTAWASGKTFRVGDSLVFNYNAGAHSVVEVNEADYDSCDTSNPINTYTSGNDSV
TLTKPGTRYFICGVPGHCQSGMKLAINV
>gnl|CDD|259879 cd04217, Cupredoxin_Fibrocystin-L_like, Cupredoxin domain of PKHDL1, a homolog of the autosomal recessive polycystic kidney disease protein. One member of this family is Fibrocystin-L, a homolog of the autosomal recessive polycystic kidney disease protein PKHD1. Human fibrocystin-L is predicted to be a large receptor protein (466 kDa) with a signal peptide, a single transmembrane domain and a short cytoplasmic tail. Fibrocystin-L is widely expressed at a low level in most tissues but is up-regulated specifically in T lymphocytes following activation signals. It may play roles in immunity
TNAGKDLVRGLGYVISPSELEINVGDTVTWHNFKRPKGRIVLVSEEGLFEDQTLYYGKAFSYTFTEPGTY
YFSVKDVPEMKGTINV
>gnl|CDD|259880 cd04218, Pseudoazurin, Pseudoazurin (Paz) is a type I blue copper electron-transfer protein. Pseudoazurin (PAz) has been identified as an electron donor to the denitrification pathway. For example, PAz acts as an electron donor to cytochrome c peroxidase and N2OR from Paracoccus pantotrophus (Pp), and to the copper containing nitrite reductase (NiR) that catalyzes the second step of denitrification. It has been shown that pseudoazurin dramatically enhances the reaction profile of nitrite reduction by Paracoccus pantotrophus cytochrome cd1 and facilitates release of the product nitric oxide. The ability of this small redox protein to interact with a multitude of structurally different partners has been attributed to the hydrophobic character of the binding surface
EHEVKMLNKGAGGAMVFEPAFLRAEPGDTVTFVPTDKSHNAASIKGMLPEGAEPFKGKINEEITVTFEKE
GVYGYKCTPHYGMGMVGLIQVGDPVNLEAAKSVKHPGRAKKRFEALF
>gnl|CDD|259881 cd04219, Plastocyanin, Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to PSI. Plastocyanin is a small copper-containing protein found in cyanobacteria, higher plants, and some algae, where it plays a role in photosynthesis. The two photosystems that are primarily responsible for photosynthesis are photosystem I (PSI) and photosystem II (PSII). The flow of electrons begins in PSII, which acts as a proton pump. Plastocyanin is responsible for transporting electrons from PSII to PSI
ATVKMGSDSGALVFEPKELTVKAGDTVEFVNNKGGPHNVVFDEDAVPSAVDAAALSHKDLLNAPGETFSV
TFPAPGTYTFYCEPHRGAGMVGKITVQ
>gnl|CDD|259882 cd04220, Halocyanin, Halocyanin is an archaea blue (type I) copper redox protein. Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronomonas pharaonis (Natronobacterium pharaonis). Halocyanin may serve as a mobile electron carrier at a peripheral membrane protein. The copper-binding domain is present only once in some halocyanins and is duplicated in others
TVTVGVGMNGGFAFDPAAIRVSPGTTVTWEWTGEGGGHNVVAYEDPITAFDSGSTDSSEGETYEHTFEET
GEYRYVCVPHEALGMKGAIVVE
>gnl|CDD|259883 cd04221, MauL, Methylamine utilization protein MauL. MauL is one of the products from the methylamine utilization gene cluster in Methylobacterium extorquens AM1. Mutants generated by insertions in mauL were not able to grow on methylamine or any other primary amine as carbon sources. MauL belongs to the blue or type I copper protein family. They are involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form
SAEVKQKDKEFEPHVLVIKPGDTVSFPNSDDIRHNVYSFSPAKIFELLDQPPGTTKDVVLFDKAGVVVVG
CNIHPIMRAWILV
>gnl|CDD|259884 cd04222, CuRO_1_ceruloplasmin, The first cupredoxin domain of Ceruloplasmin. Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first cupredoxin domain of ceruloplasmin
REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVW
LGFLGPILKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTW
TVPEEQAPTKADANCLTRIYHSHIDAPKDIASGLIGPLIICKK
>gnl|CDD|259885 cd04223, N2OR_C, The C-terminal cupredoxin domain of Nitrous-oxide reductase. Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain
KVEVYMTAIRSHFTPDIIEVKEGDEVTVHLTNLEQDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPG
VYPYYCTEFCSALHLEMQGYLIVEP
>gnl|CDD|259886 cd04224, CuRO_3_ceruloplasmin, The third cupredoxin domain of Ceruloplasmin. Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the third cupredoxin domain of ceruloplasmin
GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKH
RSKEEEHLGILGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGSHVSPGETF
TYEWTVPEGVGPTNQDPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK
>gnl|CDD|259887 cd04225, CuRO_5_ceruloplasmin, The fifth cupredoxin domain of Ceruloplasmin. Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the fifth cupredoxin domain of ceruloplasmin
RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAE
EEHLGILGPLIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVED
SNCISWAYYSTVDQIKDLYSGLIGPLVICRR
>gnl|CDD|259888 cd04226, CuRO_1_FV_like, The first cupredoxin domain of coagulation factor VIII and similar proteins. Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 1 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom
REYYIAAQNIDWDYTPQSEELRLKRSEQSFKKIVYREYEEGFKKEKPADLSSGLLGPTLRAEVGDTLIVH
FKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYI
YYSHVNMVRDFNSGLIGALLICKKG
>gnl|CDD|259889 cd04227, CuRO_3_FVIII_like, The third cupredoxin domain of coagulation factor VIII and similar proteins. Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 3 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins
QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGIL
GPLLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMPIGPGETFGYMWELTAED
GPTEEDPRCLTRLYQSTVDPERDLASGLIGPLLICKK
>gnl|CDD|259890 cd04228, CuRO_5_FVIII_like, The fifth cupredoxin domain of coagulation factor VIII and similar proteins. Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 5 of unprocessed Factor VIII or the first cupredoxin domain of the light chain of circulating Factor VIII, and similar proteins
IRHYFIAAVEVLWDYGMQRPQHFLRARDPNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILG
PYIRAEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRAEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDC
KAWAYFSNVDLEKDLHSGLIGPLIICKTG
>gnl|CDD|259891 cd04229, CuRO_1_Ceruloplasmin_like_1, cupredoxin domain of ceruloplasmin homologs. Uncharacterized subfamily of ceruloplasmin homologous proteins. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. Ceruloplasmin also functions in copper transport, amine oxidase and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first domain of the triplicated units
RTYYIAAEEVDWDYAPSGKNKCCLGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLG
ILGPVIRAEVGDTIKVVFKNNLDEFPVNMHPHGGLYSKDNEGTTDGAGDVVAPGETYTYRWIVPEDAGPG
PGDPSSRLWLYHSHVDVFAHTNAGLVGPIIVTSKG
>gnl|CDD|259892 cd04230, Sulfocyanin, Sulfocyanin is a blue copper protein in archaebacterium Sulfolobus acidocaldarius. Sulfocyanin is a blue copper protein with a putative membrane anchoring hydrophobic motif at the N-terminus. It may substitute for cytochrome C in electron transfer reactions in archaea
KITLPYNPSNKTVFLYLVVLSSGPTFNFNGTSFGQMHIYIPAGWNVIVKFTNQESLPHNLILVQNDTATP
NSPDISSDGKILLYVGASSSNYTTSGISSGQSASGSIGLISAGYYWLACGILGHAESGMWAVLIVSSNVT
VPY
>gnl|CDD|259893 cd04231, Rusticyanin, Rusticyanin is a cupredoxin in archaea and proteobacteria. Rusticyanin is a copper-containing protein which is involved in electron-transfer. The members of this family are found in archaea and proteobacteria. It is a cupredoxin, or blue-copper protein due to its color. Rusticyanin, extracted from the bacteria Thiobacillus ferrooxidans is redox active down to PH 2.0 and the acid-stable cytochrome c is the primary acceptor of the electron. This organism can grow on Fe2+ as its sole energy source. Rusticyanin is thought to be a principal component in the iron respiratory electron transport chain of T. ferrooxidans
TITYSSKTVHLVVLAVLPGFPFPSFEIDGLINPTLVIPAGATVHITVINTDKGFYHSFIITSKGPPYPYM
PMPDQPGIVAMMPFLPPANGGQFYYYEFNWTPNSPGTYWYLCTYPGHAATGMYGKII
>gnl|CDD|259894 cd04232, CuRO_1_CueO_FtsP, The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins. CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. FtsP does not contain any copper binding sites
KPFTLTAQKGETEFLPGKKTATWGYNGSYLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDGG
PHQPIAPGQTWSPTFTIDQPAATLWYHPHTHGKTAEQVYRGLAGLFIIED
>gnl|CDD|259895 cd04233, Auracyanin, Auracyanins A and B and similar proteins. This subfamily includes both auracyanins A and B from the photosynthetic bacterium Chloroflexus aurantiacus and similar proteins. Auracyanins A and B are very similar blue copper proteins with 38% sequence identity and are homologous to the bacterial redox protein Azurin. However, auracyanin A is expressed only when C. aurantiacus cells are grown in light, whereas auracyanin B is expressed in both dark and light conditions. Thus, auracyanin A may function as a redox partner in photosynthesis, while auracyanin B may function in aerobic respiration
ATTITIKAVPGELKFDKTRLTVKAGSKVTLTFENPDDMPHNLVIVKPGSLEKVGEAALAMGADGPAKNYV
PDSPDVLAATPLVNPGETETLTFTAPTEPGTYPYVCTYPGHWAIMKGVLIV
>gnl|CDD|239767 cd04234, AAK_AK, AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the N-terminal catalytic domain of aspartokinase (4-L-aspartate-4-phosphotransferase;). AK is the first enzyme in the biosynthetic pathway of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. It also catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. One mechanism for the regulation of this pathway is by the production of several isoenzymes of aspartokinase with different repressors and allosteric inhibitors. Pairs of ACT domains are proposed to specifically bind amino acids leading to allosteric regulation of the enzyme. In Escherichia coli, three different aspartokinase isoenzymes are regulated specifically by lysine, methionine, and threonine. AK-HSDHI (ThrA) and AK-HSDHII (MetL) are bifunctional enzymes that consist of an N-terminal AK and a C-terminal homoserine dehydrogenase (HSDH). ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. The third isoenzyme, AKIII (LysC), is monofunctional and is involved in lysine synthesis. The three Bacillus subtilis isoenzymes, AKI (DapG), AKII (LysC), and AKIII (YclM), are feedback-inhibited by meso-diaminopimelate, lysine, and lysine plus threonine, respectively. The E. coli lysine-sensitive AK is described as a homodimer, whereas, the B. subtilis lysine-sensitive AK is described as a heterodimeric complex of alpha- and beta- subunits that are formed from two in-frame overlapping genes. A single AK enzyme type has been described in Pseudomonas, Amycolatopsis, and Corynebacterium. The fungal aspartate pathway is regulated at the AK step, with L-Thr being an allosteric inhibitor of the Saccharomyces cerevisiae AK (Hom3). At least two distinct AK isoenzymes can occur in higher plants, one is a monofunctional lysine-sensitive isoenzyme, which is involved in the overall regulation of the pathway and can be synergistically inhibited by S-adenosylmethionine. The other isoenzyme is a bifunctional, threonine-sensitive AK-HSDH protein. Also included in this CD is the catalytic domain of the Methylomicrobium alcaliphilum ectoine AK, the first enzyme of the ectoine biosynthetic pathway, found in this bacterium, and several other halophilic/halotolerant bacteria
MVVQKFGGTSVASAERIKRVADIIKAYEKGNRVVVVVSAMGGVTDLLIELALLLSFGERLSARLLAAALR
DRGIKARSLDARQAGITTDDNHGAARIIEISYERLKELLAEIGKVPVVTGFIGRNEDGEITTLGRGGSDY
SAAALAAALGADEVEIWTDVDGIYTADPRIVPEARLIPEISYDEALELAYFGAKVLHPRAVEPARKANIP
IRVKNTFNPEAPGTLIT
>gnl|CDD|239768 cd04235, AAK_CK, AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and carbamoyl phosphate (CP) utilization with the production of ATP from ADP and CP. Both CK (this CD) and nonhomologous CP synthetase synthesize carbamoyl phosphate, an essential precursor of arginine and pyrimidine bases, in the presence of ATP, bicarbonate, and ammonia. CK is a homodimer of 33 kDa subunits and is a member of the Amino Acid Kinase Superfamily (AAK)
RIVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQNEAAAEKVPA
YPLDVCGAMSQGMIGYMLQQALDNELPKRGIDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEEL
AAEKGWTFKEDAGRGYRRVVPSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGGLKGVEAVIDK
DLASALLAEEINADLLVILTDVDNVYINFGKPNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFV
ESGGKKAIITSLENAEAALEGKAGTVIV
>gnl|CDD|239769 cd04236, AAK_NAGS-Urea, AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the urea cycle found in animals. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate; NAG is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Ureogenic NAGS activity is dependent on the concentration of glutamate (substrate) and arginine (activator). Domain architecture of ureogenic NAGS consists of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal DUF619 domain. Members of this CD belong to the protein superfamily, the Amino Acid Kinase Family (AAKF)
IYRDVKAFLHQKGGDPREARYWLTQFQIAMPNDWPAFAVLEVDHSVFRSLEMVQSLSFGLAFLQRMDMKL
LVVMGLSAPDGTNMSDLELQAARSRLVKDCKTLVEALQANSAAAHPLFSGESVLQAEEPEPGASKGPSVS
VDTELLQWCLGSGHIPLVCPIGETSSGRSVSLDSSEVTTAIAKALQPIKVIFLNRSGGLRDQKHKVLPQV
HLPADLPSLSDAEWLSETEQNRIQDIATLLNALPSMSSAVITSAETLLTELFSHKGSGTLF
>gnl|CDD|239770 cd04237, AAK_NAGS-ABP, AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the arginine-biosynthesis pathway (ABP) found in gamma- and beta-proteobacteria and higher plant chloroplasts. Domain architecture of these NAGS consisted of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal NAG synthase, acetyltransferase (ArgA) domain. Both bacterial and plant sequences in this CD have a conserved N-terminal extension; a similar sequence in the NAG kinases of the cyclic arginine-biosynthesis pathway has been implicated in feedback inhibition sensing. Plant sequences also have an N-terminal chloroplast transit peptide and an insert (approx. 70 residues) in the C-terminal region of ArgB. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK)
QFVDWFREAAPYINAHRGKTFVIAFGGEAVAHPNFDNIVHDIALLHSLGIRLVLVHGARPQIDQRLAERG
LEPRYHRGLRITDAAALECVKEAAGAVRLEIEALLSMGLPNSPMAGARIRVVSGNFVTARPLGVVDGVDF
GHTGEVRRIDADAIRRQLDQGSIVLLSPLGYSPTGEVFNLSMEDVATAVAIALKADKLIFLTDGPGLLDD
DGELIRELTAQEAEALLETGALLTNDTARLLQAAIEACRGGVPRVHLISYAEDGALLLELFTRDGVGTLI
>gnl|CDD|239771 cd04238, AAK_NAGK-like, AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the Escherichia coli and Pseudomonas aeruginosa type NAGKs which catalyze the phosphorylation of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in bacteria and photosynthetic organisms using either the acetylated, noncyclic (NC), or non-acetylated, cyclic (C) route of ornithine biosynthesis. Also included in this CD is a distinct group of uncharacterized (UC) bacterial and archeal NAGKs. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK)
VVIKYGGSAMKDEELKEAFADDIVLLKQVGINPVIVHGGGPEINELLKRLGIESEFVNGLRVTDKETMEI
VEMVLAGKVNKELVSLLNRAGGKAVGLSGKDGGLIKAEKKEEKDIDLGFVGEVTEVNPELLETLLEAGYI
PVIAPIAVDEDGETYNVNADTAAGAIAAALKAEKLILLTDVPGVLDDPGSLISELTPKEAEELIEDGVIS
GGMIPKVEAALEALEGGVRKVHIIDGRVPHSLLLELFTDEGIGTMI
>gnl|CDD|239772 cd04239, AAK_UMPK-like, AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays a key role in pyrimidine nucleotide biosynthesis. Regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinases of E. coli (Ec) and Pyrococcus furiosus (Pf) are known to function as homohexamers, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Also included in this CD are the alpha and beta subunits of the Mo storage protein (MosA and MosB) characterized as an alpha4-beta4 octamer containing an ATP-dependent, polynuclear molybdenum-oxide cluster. These and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK)
RIVLKLSGEALAGEGGGIDPEVLKEIAREIKEVVDLGVEVAIVVGGGNIARGYIAAARGMPRATADYIGM
LATVMNALALQDALEKLGVKTRVMSAIPMQGVAEPYIRRRAIRHLEKGRIVIFGGGTGNPGFTTDTAAAL
RAEEIGADVLLKATNVDGVYDADPKKNPDAKKYDRISYDELLKKGLKVMDATALTLCRRNKIPIIVFNGL
KPGNLLRALKGEHVGTLIE
>gnl|CDD|239773 cd04240, AAK_UC, AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few bacteria. Sequences in this CD are members of the Amino Acid Kinase (AAK) superfamily
VVKIGGSLIREAVRLLRWLKTLSGGGVVIVPGGGPFADVVRRYQERKGLSDAAAHWMAILAMEQYGYLLA
DLEPRLVARTLAELTDVLERGKIAILLPYRLLLDTDPLPHSWEVTSDSIAAWLAKKLGAKRLVIVTDVDG
IYEKDGKLVNEIAAAELLGETSVDPAFPRLLTKYGIRCYVVNGDDPERVLAALRGREGVGTRI
>gnl|CDD|239774 cd04241, AAK_FomA-like, AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar proteins found in a wide range of organisms. Together, the fomA and fomB genes in the fosfomycin biosynthetic gene cluster of Streptomyces wedmorensis confer high-level fosfomycin resistance. FomA and FomB proteins converted fosfomycin to fosfomycin monophosphate and fosfomycin diphosphate in the presence of ATP and a magnesium ion, indicating that FomA and FomB catalyzed phosphorylations of fosfomycin and fosfomycin monophosphate, respectively. FomA and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK)
MIILKLGGSVITDKDRPETIREENLERIARELAEAIDEKLVLVHGGGSFGHPKAKEYGLPDGDGSFSAEG
VAETHEAMLELNSIVVDALLEAGVPAVSVPPSSFFVTENGRIVSFDLEVIKELLDRGFVPVLHGDVVLDE
GGGITILSGDDIVVELAKALKPERVIFLTDVDGVYDKPPPDAKLIPEIDVGSLEDILAALGSAGTDVTGG
MAGKIEELLELARRGIEVYIFNGDKPENLYRALLGNFIGTRI
>gnl|CDD|239775 cd04242, AAK_G5K_ProB, AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (and, in mammals, ornithine) biosynthesis. G5K is subject to feedback allosteric inhibition by proline or ornithine. In microorganisms and plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia. Microbial G5K generally consists of two domains: a catalytic G5K domain and one PUA (pseudo uridine synthases and archaeosine-specific transglycosylases) domain, and some lack the PUA domain. G5K requires free Mg for activity, it is tetrameric, and it aggregates to higher forms in a proline-dependent way. G5K lacking the PUA domain remains tetrameric, active, and proline-inhibitable, but the Mg requirement and the proline-triggered aggregation are greatly diminished and abolished, respectively, and more proline is needed for inhibition. Although plant and animal G5Ks are part of a bifunctional polypeptide, delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR; ProA); bacterial and yeast G5Ks are monofunctional single-polypeptide enzymes. In this CD, all three domain architectures are present: G5K, G5K+PUA, and G5K+G5PR
RIVVKVGSSLLTDEDGGLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLGLEKRPKTLPEKQAL
AAVGQSLLMALYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEEIR
FGDNDRLSALVAGLVNADLLILLSDVDGLYDKNPRENPDAKLIPEVEEITDEIEAMAGGSGSSVGTGGMR
TKLKAARIATEAGIPVVIANGRKPDVLLDILAGEAVGTLFL
>gnl|CDD|239776 cd04243, AAK_AK-HSDH-like, AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK- homoserine dehydrogenase (HSDH). These aspartokinases are found in such bacteria as E. coli (AKI-HSDHI, ThrA and AKII-HSDHII, MetL) and in higher plants (Z. mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains, located C-terminal to the AK catalytic domain, were shown to be involved in allosteric activation. Also included in this CD is the catalytic domain of the aspartokinase (AK) of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. In E. coli, LysC is reported to be a homodimer of 50 kD subunits. Also included in this CD is the catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine
MKVLKFGGTSVASAERIRRVADIIKSRASSPVLVVVSALGGVTNRLVALAELAASGDDAQAIVLQEIRER
HLDLIKELLSGESAAELLAALDSLLERLKDLLEGIRLLGELSDKTRAEVLSFGELLSSRLMSAYLQEQGL
PAAWLDARELLLTDDGFLNAVVDLKLSKERLAQLLAEHGKVVVTQGFIASNEDGETTTLGRGGSDYSAAL
LAALLDAEEVEIWTDVDGVYTADPRKVPDARLLKELSYDEAMELAYFGAKVLHPRTIQPAIRKNIPIFIK
NTFNPEAPGTLIS
>gnl|CDD|239777 cd04244, AAK_AK-LysC-like, AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive AK isoenzyme found in higher plants. The lysine-sensitive AK isoenzyme is a monofunctional protein. It is involved in the overall regulation of the aspartate pathway and can be synergistically inhibited by S-adenosylmethionine. Also included in this CD is an uncharacterized LysC-like AK found in Euryarchaeota and some bacteria. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP
RLVMKFGGTSVGSAERIRHVADLVGTYAEGHEVVVVVSAMGGVTDRLLLAAEAAVSGRIAGVKDFIEILR
LRHIKAAKEAISDEEIAEVESIIDSLLEELEKLLYGIAYLGELTPRSRDYIVSFGERLSAPIFSAALRSL
GIKARALDGGEAGIITDDNFGNARPLPATYERVRKRLLPMLEDGKIPVVTGFIGATEDGAITTLGRGGSD
YSATIIGAALDADEIWIWKDVDGVMTADPRIVPEARTIPRLSYAEAMELAYFGAKVLHPRTVEPAMEKGI
PVRVKNTFNPEAPGTLIT
>gnl|CDD|239778 cd04245, AAK_AKiii-YclM-BS, AAK_AKiii-YclM-BS: Amino Acid Kinase Superfamily (AAK), AKiii-YclM-BS; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine plus threonine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in Bacilli (Bacillus subtilis YclM) and Clostridia species. Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. In Bacillus subtilis (BS), YclM is reported to be a single polypeptide of 50 kD. The Bacillus subtilis 168 AKIII is induced by lysine and repressed by threonine, and it is synergistically inhibited by lysine and threonine
MKVVKFGGSSLASAEQFQKVKAIVKADPERKIVVVSAPGKRFKDDTKVTDLLILYAEAVLAGEDTESIFE
AIVDRYAEIADELGLPMSILEEIAEILENLANLDYANPDYLLDALKARGEYLNAQLMAAYLNYQGIDARY
VIPKDAGLVVTDEPGNAQILPESYQKIKKLRDSDEKLVIPGFYGYSKNGDIKTFSRGGSDITGAILARGF
QADLYENFTDVDGIYAANPRIVANPKPISEMTYREMRELSYAGFSVFHDEALIPAIEAGIPINIKNTNHP
EAPGTLIV
>gnl|CDD|239779 cd04246, AAK_AK-DapG-like, AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the diaminopimelate-sensitive aspartokinase isoenzyme AKI (DapG), a monofunctional enzymes found in Bacilli (Bacillus subtilis 168), Clostridia, and Actinobacteria bacterial species, as well as, the catalytic AK domain of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis 168, the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related isoenzymes. In Bacillus subtilis, the regulation of the diaminopimelate-lysine biosynthetic pathway involves dual control by diaminopimelate and lysine, effected through separate diaminopimelate- and lysine-sensitive aspartokinase isoenzymes. The role of the AKI isoenzyme is most likely to provide a constant level of aspartyl-beta-phosphate for the biosynthesis of diaminopimelate for peptidoglycan synthesis and dipicolinate during sporulation. The B. subtilis 168 AKII is induced by methionine, and repressed and inhibited by lysine. In Corynebacterium glutamicum and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and threonine. Also included in this CD are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinase isoenzyme types found in Pseudomonas, C. glutamicum, and Amycolatopsis lactamdurans. The B. subtilis AKI is tetrameric consisting of two alpha and two beta subunits; the alpha (43 kD) and beta (17 kD) subunit formed by two in-phase overlapping genes. The alpha subunit contains the AK catalytic domain and two ACT domains. The beta subunit contains two ACT domains. The B. subtilis 168 AKII aspartokinase is also described as tetrameric consisting of two alpha and two beta subunits. Some archeal aspartokinases in this group lack recognizable ACT domains
IIVQKFGGTSVADIERIKRVAERIKKAVKKGYQVVVVVSAMGGTTDELIGLAKEVSPRPSPRELDMLLST
GEQISAALLAMALNRLGIKAISLTGWQAGILTDDHHGNARIIDIDPKRILEALEEGDVVVVAGFQGVNED
GEITTLGRGGSDTTAVALAAALKADRCEIYTDVDGVYTADPRIVPKARKLDVISYDEMLEMASLGAKVLH
PRSVELAKKYNVPLRVRSSFSENPGTLIT
>gnl|CDD|239780 cd04247, AAK_AK-Hom3, AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal catalytic domain of the aspartokinase HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae and other related AK domains. Aspartokinase, the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and in fungi, is responsible for the production of threonine, isoleucine and methionine. S. cerevisiae has a single aspartokinase isoenzyme type, which is regulated by feedback, allosteric inhibition by L-threonine. Recent studies show that the allosteric transition triggered by binding of threonine to AK involves a large change in the conformation of the native hexameric enzyme that is converted to an inactive one of different shape and substantially smaller hydrodynamic size
GWVVQKFGGTSVGKFPDNIADDIVKAYLKGNKVAVVCSARSTGTKAEGTTNRLLQAADEALDAQEKAFHD
IVEDIRSDHLAAARKFIKNPELQAELEEEINKECELLRKYLEAAKILSEISPRTKDLVISTGEKLSCRFM
AAVLRDRGVDAEYVDLSHIVDLDFSIEALDQTFYDELAQVLGEKITACENRVPVVTGFFGNVPGGLLSQI
GRGYTDLCAALCAVGLNADELQIWKEVDGIFTADPRKVPTARLLPSITPEEAAELTYYGSEVIHPFTMEQ
VIKARIPIRIKNVENPRGEGTVIYPD
>gnl|CDD|239781 cd04248, AAK_AK-Ectoine, AAK_AK-Ectoine: Amino Acid Kinase Superfamily (AAK), AK-Ectoine; this CD includes the N-terminal catalytic domain of the aspartokinase of the ectoine (1,4,5,6-tetrahydro-2-methyl pyrimidine-4-carboxylate) biosynthetic pathway found in Methylomicrobium alcaliphilum, Vibrio cholerae, and other various halotolerant or halophilic bacteria. Bacteria exposed to hyperosmotic stress accumulate organic solutes called 'compatible solutes' of which ectoine, a heterocyclic amino acid, is one. Apart from its osmotic function, ectoine also exhibits a protective effect on proteins, nucleic acids and membranes against a variety of stress factors. de novo synthesis of ectoine starts with the phosphorylation of L-aspartate and shares its first two enzymatic steps with the biosynthesis of amino acids of the aspartate family: aspartokinase and L-aspartate-semialdehyde dehydrogenase. The M. alcaliphilum and the V. cholerae aspartokinases are encoded on the ectABCask operon
LTVEKIGGTSMSAFGAVLDNIILKPDSDLYGRVFVVSAYSGVTNALLEHKKTGAPGIYQHFVDADEAWRE
ALSALKQAMLKINEAFADIGLDVEQADAFIGARIQDARACLHDLARLCSSGYFSLAEHLLAARELLASLG
EAHSAFNTALLLQNRGVNARFVDLSGWRDSGDMTLDERISEAFRDIDPRDELPIVTGYAKCAEGLMREFD
RGYSEMTFSRIAVLTGASEAIIHKEFHLSSADPKLVGEDKARPIGRTNYDVADQLANLGMEAIHPKAAKG
LRQAGIPLRVKNTFEPDHPGTLIT
>gnl|CDD|239782 cd04249, AAK_NAGK-NC, AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis using the acetylated, noncyclic route of ornithine biosynthesis. There are two variants of this pathway. In one, typified by the pathway in Escherichia coli, glutamate is acetylated by acetyl-CoA and acetylornithine is deacylated hydrolytically. In this pathway, feedback inhibition by arginine occurs at the initial acetylation of glutamate and not at the phosphorylation of NAG by NAGK. Homodimeric NAGK-NC are members of the Amino Acid Kinase Superfamily (AAK)
LVIKLGGALLETEAALEQLFSALSEYQQQHNRQLVIVHGGGCVVDELLKKLNFPSEKKNGLRVTPKEQIP
YITGALAGTANKQLMAQAIKAGLKPVGLSLADGGMTAVTQLDPELGAVGKATANDPSLLNDLLKAGFLPI
ISSIGADDQGQLMNVNADQAATAIAQLLNADLVLLSDVSGVLDADKQLISELNAKQAAELIEQGVITDGM
IVKVNAALDAAQSLRRGIDIASWQYPEQLTALLAGEPVGTKI
>gnl|CDD|239783 cd04250, AAK_NAGK-C, AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK)
VLIEALPYIQKFRGKTVVIKYGGNAMKDEELKESFARDIVLLKYVGINPVVVHGGGPEINEMLKKLGIES
EFVNGLRVTDEETMEIVEMVLVGKVNKEIVSLINRAGGKAVGLSGKDGNLIKAKKKDATVIEEIIDLGFV
GEVTEVNPELLETLLEAGYIPVIAPVGVGEDGETYNINADTAAGAIAAALKAEKLILLTDVAGVLDDPND
PGSLISEISLKEAEELIADGIISGGMIPKVEACIEALEGGVKAAHIIDGRVPHSLLLEIFTDEGIGTMI
>gnl|CDD|239784 cd04251, AAK_NAGK-UC, AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar to Escherichia coli and Pseudomonas aeruginosa NAGKs which catalyze the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis. These uncharacterized domain sequences are found in some bacteria (Deinococci and Chloroflexi) and archea and belong to the Amino Acid Kinase Superfamily (AAK)
IVVKIGGSVVSDLDKVIDDIANFGERLIVVHGGGNYVNEYLKRLGVEPKFVTSPSGIRSRYTDKETLEVF
VMVMGLINKKIVARLHSLGVKAVGLTGLDGRLLEAKRKEIVRVNERGRKMIIRGGYTGKVEKVNSDLIEA
LLDAGYLPVVSPVAYSEEGEPLNVDGDRAAAAIAAALKAERLILLTDVEGLYLDGRVIERITVSDAESLL
EKAGGGMKRKLLAAAEAVEGGVREVVIGDARADSPISSALNGGGTVI
>gnl|CDD|239785 cd04252, AAK_NAGK-fArgBP, AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway (fArgBP). The nuclear-encoded, mitochondrial polyprotein precursor with an N-terminal NAGK (ArgB) domain (this CD), a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-Acetylglutamate Phosphate Reductase, NAGPR). The precursor is cleaved in the mitochondria into two distinct enzymes (NAGK-DUF619 and NAGPR). Native molecular weights of these proteins indicate that the kinase is an octamer whereas the reductase is a dimer. This CD also includes some gamma-proteobacteria (Xanthomonas and Xylella) NAG kinases with an N-terminal NAGK (ArgB) domain (this CD) and a C-terminal DUF619 domain. The DUF619 domain is described as a putative distant homolog of the acetyltransferase, ArgA, predicted to function in NAG synthase association in fungi. Eukaryotic sequences have an N-terminal mitochondrial transit peptide. Members of this NAG kinase domain CD belong to the Amino Acid Kinase Superfamily (AAK)
AVIKVGGAIIEDDLDELAASLSFLQHVGLYPIVVHGAGPQLNEELEAAGVEPEYVDGLRVTDPETLAVAR
KVFLEENLKLVEALERNGARARPITSGVFEAEYLDKDKYGLVGKITGVNKAPIEAAIRAGYLPILTSLAE
TPSGQLLNVNADVAAGELARVLEPLKIVFLNETGGLLDGTGKKISAINLDEEYDDLMKQPWVKYGTKLKI
KEIKELLDTLPRSSSVSITSPDDLQKELFTHSGAGTLI
>gnl|CDD|239786 cd04253, AAK_UMPK-PyrH-Pf, AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase (uridylate kinase) enzymes that catalyze UMP phosphorylation and play a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of Pyrococcus furiosus (Pf) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs (this CD) appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK)
RIVISLGGSVLAPEKDADFIKEYANVLRKISDGHKVAVVVGGGRLAREYISVARKLGASEAFLDEIGIMA
TRLNARLLIAALGDAYPPVPTSYEEALEAMFTGKIVVMGGTEPGQSTDAVAALLAERLGADLLINATNVD
GVYSKDPRKDPDAKKFDRLSADELIDIVGKSSWKAGSNEPFDPLAAKIIERSGIKTIVVDGRDPENLERA
LKGEFVGTIIE
>gnl|CDD|239787 cd04254, AAK_UMPK-PyrH-Ec, UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of E. coli (Ec) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial and chloroplast UMPKs (this CD) have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK)
KRVLLKLSGEALAGENGFGIDPEVLNRIAREIKEVVDLGVEVAIVVGGGNIFRGASAAEAGMDRATADYM
GMLATVINALALQDALESLGVKTRVMSAIPMQGVAEPYIRRRAIRHLEKGRVVIFAGGTGNPFFTTDTAA
ALRAIEINADVILKATKVDGVYDADPKKNPNAKRYDHLTYDEVLSKGLKVMDATAFTLCRDNNLPIVVFN
INEPGNLLKAVKGEGVGTLIS
>gnl|CDD|239788 cd04255, AAK_UMPK-MosAB, AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA and MosB) which are related to uridine monophosphate kinase (UMPK) enzymes that catalyze the phosphorylation of UMP by ATP, yielding UDP, and playing a key role in pyrimidine nucleotide biosynthesis. The Mo storage protein from the nitrogen-fixing bacterium, Azotobacter vinelandii, is characterized as an alpha4-beta4 octamer containing a polynuclear molybdenum-oxide cluster which is ATP-dependent to bind Mo and pH-dependent to release Mo. These and related bacterial sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK)
HVESPLMGESLVDKELTKRLAGKEQFRLLPDLNVVKIGGQSIIDRGAEAVLPLVEEIVALRPEHKLLILT
GGGTRARHVYSIGLDLGMPTGVLAKLGASVSEQNAEMLATLLAKHGGSKVGHGDLLQLPTFLKAGRAPVI
SGMPPYGLWEHPAEEGRIPPHRTDVGAFLLAEVIGARNLIFVKDEDGLYTADPKKNKKAEFIPEISAAEL
LKKDLDDLVLERPVLDLLQNARHVKEVQIVNGLVPGNLTRALRGEHVGTIIR
>gnl|CDD|239789 cd04256, AAK_P5CS_ProBA, AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR, ProA), the first and second enzyme catalyzing proline (and, in mammals, ornithine) biosynthesis. G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, and is subject to feedback allosteric inhibition by proline or ornithine. In plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia
SRSELKHAKRIVVKLGSAVVTREDECGLALGRLASIVEQVSELQSQGREVILVTSGAVAFGKQRLRHEIL
LSSSMRQTLKSGQLKDMPQMELDGRACAAVGQSGLMALYEAMFTQYGITVAQVLVTKPDFYDEQTRRNLN
GTLEELLRLNIIPIINTNDAVSPPPEPDEDLQGVISIKDNDSLAARLAVELKADLLILLSDVDGLYDGPP
GSDDAKLIHTFYPGDQQSITFGTKSRVGTGGMEAKVKAALWALQGGTSVVITNGMAGDVITKILEGKKVG
TFFT
>gnl|CDD|239790 cd04257, AAK_AK-HSDH, AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - homoserine dehydrogenase (HSDH). These aspartokinases are found in bacteria (E. coli AKI-HSDHI, ThrA and E. coli AKII-HSDHII, MetL) and higher plants (Z. mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains, located C-terminal to the AK catalytic domain, were shown to be involved in allosteric activation
MKVLKFGGTSLANAERIRRVADIILNAAKQEQVAVVVSAPGKVTDLLLELAELASSGDDAYEDILQELES
KHLDLITELLSGDAAAELLSALGNDLEELKDLLEGIYLLGELPDSIRAKVLSFGERLSARLLSALLNQQG
LDAAWIDARELIVTDGGYLNAVVDIELSKERIKAWFSSNGKVIVVTGFIASNPQGETTTLGRNGSDYSAA
ILAALLDADQVEIWTDVDGVYSADPRKVKDARLLPSLSYQEAMELSYFGAKVLHPKTIQPVAKKNIPILI
KNTFNPEAPGTLIS
>gnl|CDD|239791 cd04258, AAK_AKiii-LysC-EC, AAK_AKiii-LysC-EC: Amino Acid Kinase Superfamily (AAK), AKiii-LysC-EC: this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive aspartokinase isoenzyme AKIII. AKIII is a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. In E. coli, LysC is reported to be a homodimer of 50 kD subunits
MVVAKFGGTSVADYAAMLRCAAIVKSDASVRLVVVSASAGVTNLLVALADAAESGEEIESIPQLHEIRAI
HFAILNRLGAPEELRAKLEELLEELTQLAEGAALLGELSPASRDELLSFGERMSSLLFSEALREQGVPAE
WFDVRTVLRTDSRFGRAAPDLNALAELAAKLLKPLLAGTVVVTQGFIGSTEKGRTTTLGRGGSDYSAALL
AEALHAEELQIWTDVAGIYTTDPRICPAARAIKEISFAEAAEMATFGAKVLHPATLLPAIRKNIPVFVGS
SKDPEAGGTLIT
>gnl|CDD|239792 cd04259, AAK_AK-DapDC, AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. Aspartokinase is the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine
WVVLKFGGTSVSSRARWDTIAKLAQKHLNTGGQPLIVCSALSGISNKLEALIDQALLDEHHSLFNAIQSR
HLNLAEQLEVDADALLANDLAQLQRWLTGISLLKQASPRTRAEVLALGELMSTRLGAAYLEAQGLKVKWL
DARELLTATPTLGGETMNYLSARCESEYADALLQKRLADGAQLIITQGFIARNAHGETVLLGRGGSDTSA
AYFAAKLQAARCEIWTDVPGLFTANPHEVPHARLLKRLDYDEAQEIATMGAKVLHPRCIPPARRANIPMV
VRSTERPELSGTLIT
>gnl|CDD|239793 cd04260, AAK_AKi-DapG-BS, AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the diaminopimelate-sensitive aspartokinase isoenzyme AKI (DapG), a monofunctional class enzyme found in Bacilli (Bacillus subtilis 168), Clostridia, and Actinobacteria bacterial species. In Bacillus subtilis, the regulation of the diaminopimelate-lysine biosynthetic pathway involves dual control by diaminopimelate and lysine, effected through separate diaminopimelate- and lysine-sensitive aspartokinase isoenzymes. AKI activity is invariant during the exponential and stationary phases of growth and is not altered by addition of amino acids to the growth medium. The role of this isoenzyme is most likely to provide a constant level of aspartyl-beta-phosphate for the biosynthesis of diaminopimelate for peptidoglycan synthesis and dipicolinate during sporulation. The B. subtilis AKI is tetrameric consisting of two alpha and two beta subunits; the alpha (43 kD) and beta (17 kD) subunit formed by two in-phase overlapping genes. The alpha subunit contains the AK catalytic domain and two ACT domains. The beta subunit contains two ACT domains
IIVQKFGGTSVSTKERREQVAKKVKQAVDEGYKPVVVVSAMGRKGDPYATDTLINLVYAENSDISPRELD
LLMSCGEIISAVVLTSTLRAQGLKAVALTGAQAGILTDDNYSNAKIIKVNPKKILSALKEGDVVVVAGFQ
GVTEDGEVTTLGRGGSDTTAAALGAALNAEYVEIYTDVDGIMTADPRVVPNARILDVVSYNEVFQMAHQG
AKVIHPRAVEIAMQANIPIRIRSTMSENPGTLIT
>gnl|CDD|239794 cd04261, AAK_AKii-LysC-BS, AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis 168, and the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related sequences. In B. subtilis 168, the regulation of the diaminopimelate (Dap)-lysine biosynthetic pathway involves dual control by Dap and lysine, effected through separate Dap- and lysine-sensitive aspartokinase isoenzymes. The B. subtilis 168 AKII is induced by methionine, and repressed and inhibited by lysine. Although Corynebacterium glutamicum is known to contain a single aspartokinase isoenzyme type, both the succinylase and dehydrogenase variant pathways of DAP-lysine synthesis operate simultaneously in this organism. In this organism and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and theronine. Also included in this CD are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinases found in Pseudomons, C. glutamicum, and Amycolatopsis lactamdurans. B. subtilis 168 AKII, and the C. glutamicum, Streptomyces clavuligerus and A. lactamdurans aspartokinases are described as tetramers consisting of two alpha and two beta subunits; the alpha (44 kD) and beta (18 kD) subunits formed by two in-phase overlapping polypeptides
LIVQKFGGTSVASIERIKRVAERIKKRKKKGNQVVVVVSAMGGTTDELIELAKEISPRPPARELDVLLST
GEQVSIALLAMALNRLGIKAISLTGWQAGILTDGHHGKARIIDIDPDRIRELLEEGDVVIVAGFQGINED
GDITTLGRGGSDTSAVALAAALGADRCEIYTDVDGVYTADPRIVPKARKLDEISYDEMLEMASLGAKVLH
PRSVELAKKYGVPLRVLSSFSEEPGTLIT
>gnl|CDD|176265 cd04263, DUF619-NAGK-FABP, DUF619 domain of N-acetylglutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway. DUF619-NAGK-FABP: DUF619 domain of N-acetylglutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway (FABP). The nuclear-encoded, mitochondrial polyprotein precursor (ARG5,6) consists of an N-terminal NAGK (ArgB) domain, a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-Acetylglutamate Phosphate Reductase, NAGPR). The precursor is cleaved into two distinct enzymes (NAGK-DUF619 and NAGPR) in the mitochondria. Native molecular weights of these proteins indicate that the kinase is an octamer whereas the reductase is a dimer. Arg5,6 catalyzes the second reaction of arginine biosynthesis; the phosphorylation of the gamma-carboxyl group of NAG to produce N-acetylglutamylphosphate (NAGP) which is subsequently converted to ornithine in two more steps. It also binds and regulates the promoters of nuclear and mitochondrial genes, and may possibly regulate precursor mRNA metabolism. The DUF619 domain function has yet to be characterized
ASYFDELKERPFKAYGDEPMEVLAIVLPPSGEVATLATFTITKSGWLNNVADNIFTAIKKDHPKLVWTVR
EDDENLKWHFEKADGSFTRNGKVLFWYG
>gnl|CDD|176266 cd04264, DUF619-NAGS, DUF619 domain of various N-acetylglutamate Synthases of the fungal arginine-biosynthetic pathway and urea cycle found in humans and fish. DUF619-NAGS: This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present in C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. The DUF619 domain function has yet to be characterized
PDYIDRLQRLHAIYLSEGYNAAAIVTYEGVNNGVPYLDKFAVSSSAQGEGTSDALWRRLRRDFPKLFWRS
RKTNPINPWYFKRSDGSFKNGQWKVFWYG
>gnl|CDD|176267 cd04265, DUF619-NAGS-U, DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans and fish. This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present in C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. The DUF619 domain function has yet to be characterized
PDYFDSLQGRLHTIYLSEGYNAAAIVTNEEVDGVPYLDKFAVSSSAQGEGTGEALWRRLRRDFPKLFWRS
RSTNPINPWYFKRCDGSFKNGHWTVFWYG
>gnl|CDD|176268 cd04266, DUF619-NAGS-FABP, DUF619 domain of N-acetylglutamate Synthase of the fungal arginine-biosynthetic pathway. DUF619-NAGS-FABP: This family includes the DUF619 domain of N-acetylglutamate synthase (NAGS) of the fungal arginine-biosynthetic pathway (FABP). This NAGS (also known as arginine-requiring protein 2 or ARG2) consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. NAGS catalyzes the formation of NAG from acetylcoenzyme A and L-glutamate. The DUF619 domain, yet to be characterized, is predicted to function in NAGS association in fungi
EKYLDRLKNSLATVIIAGDYEGAAILTWEGPDGSTPEKIAYLDKFAVLPKAQGSDGIADILFNAMLDGFP
NELIWRSRKDNPVNKWYFERSVGVLKLSGSQWKLFWTG
>gnl|CDD|239795 cd04267, ZnMc_ADAM_like, Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions
REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSD
ASNTLNSFSFWRAEGPIRHDNAVLLTAQDFIEGDILGLAYVGSMCNPYSSVGVVEDTGFTLLTALTMAHE
LGHNLGAEHDGGDELAFECDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD
>gnl|CDD|239796 cd04268, ZnMc_MMP_like, Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases
KKPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYNDGTWSYGPSQVDP
LTGEILLARVYLYSSFVEYSGARLRNTAEHELGHALGLRHNFAASDRDDNVDLLAEKGDTSSVMDYAPSN
FSIQLGDGQKYTIGPYDIAAIKKLY
>gnl|CDD|239797 cd04269, ZnMc_adamalysin_II_like, Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions
KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETL
NRFLDWKRSNLLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELG
HNLGMEHDDGGCTCGRSTCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN
>gnl|CDD|239798 cd04270, ZnMc_TACE_like, Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha
NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVD
PGNKFYNKSFPNWGVEKFLVKLLLEQFSDDVCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYY
SNGKKKYLNTGLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDIAECAPGESQGGNYIMYARATSGD
KENNKKFSPCSKKSISKVLEVKSNSCFVERSQSF
>gnl|CDD|239799 cd04271, ZnMc_ADAM_fungal, Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined
QVALIGVAADCSYTKSFGSVEEARRNILNNVNSASQLYESSFNISLGLRNLTISDASCPSTAVDSAPWNL
PCNSRIDIDDRLSIFSQWRGQQPDDGNAFWTLMTACPSGSEVGVAWLGQLCRTGASDQGNETVAGTNVVV
RTSNEWQVFAHEIGHTFGAVHDCTSGTCSDGSVGSQQCCPLSTSTCDANGQYIMNPSSSSGITEFSPCTI
GNICSLLGRNPVRTSCLS
>gnl|CDD|239800 cd04272, ZnMc_salivary_gland_MPs, Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods
VYPELFVVVDYDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKSPRIRLLLVGITISKDPDFEPYIHPINY
GYIDAAETLENFNEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLQTGTGGYAYVGGACTENRVAMGEDTP
GSYYGVYTMTHELAHLLGAPHDGSPPPSWVKGHPGSLDCPWDDGYIMSYVVNGERQYRFSQCSQRQIRNV
FRRLGASCLH
>gnl|CDD|239801 cd04273, ZnMc_ADAMTS_like, Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix
RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQ
KSLKSFCRWQKKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSS
AFTIAHELGHVLGMPHDGDGNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL
>gnl|CDD|239802 cd04275, ZnMc_pappalysin_like, Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved
SIVIPVYFHVIYNNSAVSGGNISDAQITDQIDVLNDDYSGLNAGVDLGIEFVLAGTTRTVNSAWPVFAGS
GTEDAMKSALRKGGYKYLNIYVANFLGGGLLGYATFPDSLVSLAFITDGVVINPSSLPGGSAAPYNLGDT
ATHEVGHWLGLYHTFQGGSPCCTTGDYVADTPAEASPSYGCPAGRDTCPGQPGLDPIHNYMDYSDDSCMN
EFTPGQVTRMRSYLD
>gnl|CDD|239803 cd04276, ZnMc_MMP_like_2, Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin
AALSEPKEPIVYYLDNTFPEKYRDAIREGVLYWNKAFEKAGFKNAIIVKVLPDDADPGDIRYNVIRWIHS
PNGGWAYGPSVVDPRTGEILKADVILYSGFLRQDQLWYEDLLAASLRYLLAHEVGHTLGLRHNFKASSDG
SNEELEDPLGTKEKGATSSVMDYPPPNVAAQGEDQGDYYPPTIGPYDKWAIEYGYTP
>gnl|CDD|239804 cd04277, ZnMc_serralysin_like, Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides
DTTLTYSFSNTGGPYSYGYGREEDTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNSGADIRFGNS
SDPDGNTAGYAYYPGSGSGTAYGGDIWFNSSYDTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGGDPVP
PTYALDSREYTVMSYNSGYGNGASAGGGYPQTPMLLDIAALQYLYG
>gnl|CDD|239805 cd04278, ZnMc_MMP, Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases)
KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDGYPFDG
PGGTLAHAFFPGGIGGDIHFDDDEQWTLGSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP
KFKLSQDDIRGIQALYG
>gnl|CDD|239806 cd04279, ZnMc_MMP_like_1, Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin
KSPIRVYIDPTPAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNPEEDNDADIVIFFDRPPPVGGAGGGL
ARAGFPLISDGNRKLFNRTDINLGPGQPRGAENLQAIALHELGHALGLWHHSDRPEDAMYPSQGQGPDGN
PTLSARDVATLKRLYG
>gnl|CDD|239807 cd04280, ZnMc_astacin_like, Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to yield the active protease domain, which is consequently always found at the N-terminus in multi-domain architectures. This family includes: astacin, a digestive enzyme from Crayfish; meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain, proteins involved in (bone) morphogenesis, tolloid from drosophila, and the sea urchin SPAN protein, which may also play a role in development
NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKGSGCWSYVGRVGGRQVVSLGS
GCFSLGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYG
PTAFSKNGKPTIVPKDPGYQIIGQREGLSFLDIKKINKMY
>gnl|CDD|239808 cd04281, ZnMc_BMP1_TLD, Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) and TLD (tolloid)-like metalloproteases play vital roles in extracellular matrix formation, by cleaving precursor proteins such as enzymes, structural proteins, and proteins involved in the mineralization of the extracellular matrix. The drosophila protein tolloid and its Xenopus homologue xolloid cleave and inactivate Sog and chordin, respectively, which are inhibitors of Dpp (the Drosophila decapentaplegic gene product) and its homologue BMP4, involved in dorso-ventral patterning
AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVG
RRGNGPQAISIGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSL
GEPYDFDSIMHYARNTFSRGMFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP
>gnl|CDD|239809 cd04282, ZnMc_meprin, Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted extracellular proteases, which cleave a variety of targets, including peptides such as parathyroid hormone, gastrin, and cholecystokinin, cytokines such as osteopontin, and proteins such as collagen IV, fibronectin, casein and gelatin. Meprins may also be able to release proteins from the cell surface. Closely related meprin alpha- and beta-subunits form homo- and hetero-oligomers; these complexes are found on epithelial cells of the intestine, for example, and are also expressed in certain cancer cells
ENDADEGIDQDIFEINLGAGLDLFEGDILLDEGQSRNGLIGDTYRWPFPIPYILDDSLDLNAKGVILKAF
EMYRLKSCVDFKPYEGESNYIFFFKGSGCWSMVGDQQGGQNLSIGAGCDYKATVEHEFLHALGFYHEQSR
SDRDDYVKIWWDQILSGREHNFNKYDDSFSTDLNTPYDYESVMHYSPFSFNKGASEPTITTKIPEFNDII
GQRLDFSDIDLERLNRMYNC
>gnl|CDD|239810 cd04283, ZnMc_hatching_enzyme, Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted by teleost embryos to digest the egg envelope or chorion. In some teleosts, the hatching enzyme may be a system consisting of two evolutionary related metalloproteases, high choriolytic enzyme and low choriolytic enzyme (HCE and LCE), which may have different substrate specificities and cooperatively digest the chorion
NGIVYVPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVSL
QKQGCMYKGIIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNNLGTPYDYSSVMHYG
RYAFSINGKPTIVPIPDPNVPIGQRQGMSNLDILRINKLYNC
>gnl|CDD|340852 cd04299, GT35_Glycogen_Phosphorylase-like, proteins similar to glycogen phosphorylase. This family is most closely related to the oligosaccharide phosphorylase domain family and other unidentified sequences. Oligosaccharide phosphorylase catalyzes the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism
LSELAYNLWWSWNPEAQELFRDLDPELWEETGHNPVKLLGEVSPARLEALAKDPGFLGRLERVSEDYTDY
LRAPTWFQRSDRGPSLAAYFSMEFGLHEALPIYSGGLGVLAGDHLKSASDLGVPLVGVGLLYRHGYFRQS
LDSDGWQQELYPELDPGQLPLEPVRDANGEPVRVTVELPDRRVHARVWRAQVGRVPLYLLDTDVEENSED
DRKITDRLYGGDQELRIQQEILLGIGGIRALRALGIKPDVFHLNEGHAAFLGLERIRELVAEGLDFDEAL
ELVRASTLFTTHTPVPAGIDRFPPDLVDRYLGGYPELLGLSRDEFLALGREDPPDPGEPFNMAVLALRLS
QRANGVSKLHGEVSREMFSNLWPGYPPEEVPIGHVTNGVHTPTWVSPEMRELYDRYLGREWRERPTLEDI
WEAVDQIPDEELWEVRNTLRKRLVEFVRERLREQWLRNGAGPAEIAELDNALDPNVLTIGFARRFATYKR
ATLLLRDPERLARILNNPERPVQFVFAGKAHPHDEGGKALIREIVRFSREPDFRGRIIFLEDYDMQLARH
LVQGVDVWLNNPRRPLEASGTSGMKAALNGGLNLSVLDGWWAEGYDGKNGWAIGDERVYPDTEAQDAAEA
AALYDLLENEIIPLFYERDAKGIPQGWVEMVRRSLRTLGPRFSAGRMVRDYTEKYYLPAAKRFRTLARNQ
NARARELAAWKERVRKAWPTVSISSVEAGLPADAELGEELTVTVRVDLGGLRPEDVRVELVAGRGDDGGQ
IVDPVV
>gnl|CDD|340853 cd04300, GT35_Glycogen_Phosphorylase, glycogen phosphorylase and similar proteins. This is a family of oligosaccharide phosphorylases. It includes yeast and mammalian glycogen phosphorylases, plant starch/glucan phosphorylase, as well as the maltodextrin phosphorylases of bacteria. The members of this family catalyze the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism. The allosteric control mechanisms of yeast and mammalian members of this family are different from that of bacterial members. The members of this family belong to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility
KKSFVRHLEYTLGKDREEATPQDLYQALAYSVRDRLIERWNETQQYYYEKDPKRVYYLSLEFLMGRLLGN
NLLNLGLYDEVREALAELGLDLEDLEEEEPDAALGNGGLGRLAACFLDSMATLGLPAWGYGIRYEYGLFK
QKIVDGYQVELPDYWLRYGNPWEIRRPEVSVPVRFGGRVEEVPDGGRLRVRWVDGETVLAVPYDTPIPGY
GTNTVNTLRLWSAKASDEFDLEAFNEGDYIRAVEQKNRAENISRVLYPNDSTYEGKELRLKQQYFFVSAS
LQDIIRRFKKSHGPLSEFPDKVAIQLNDTHPALAIPELMRILVDEEGLSWDEAWDITTKTFAYTNHTVLP
EALEKWPVELFEKLLPRHLQIIYEINRRFLDEVRAKYPGDVDRIRRMSIIEEGKQVRMAHLAIVGSHSVN
GVAALHTEILKTTVLKDFYELYPEKFNNKTNGITPRRWLLQANPGLAALITETIGDDWVTDLDQLKKLEP
FADDPEFLEEWAAIKQANKARLAAYIKETTGVEVNPNSIFDVQVKRIHEYKRQLLNILHIIYLYLRIKEG
PPADFVPRTVIFGGKAAPGYYLAKLIIKLINAVADVVNNDPDVGDKLKVVFLPNYNVSLAEKIIPAADLS
EQISTAGKEASGTGNMKFMLNGALTIGTLDGANVEIAEEVGEENIFIFGLTAEEVEALRKNGYYPADYYE
NDPRLKRVLDQIISGTFSPGDPDEFRPLVDSLLNGNDEYLVLADFESYVDAQEKVDALYRDQEEWARKSI
LNIARSGKFSSDRTIREYAKDIWNV
>gnl|CDD|173926 cd04301, NAT_SF, N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate. NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included
FLVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE
>gnl|CDD|319798 cd04302, HAD_5NT, haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065. 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFRELLPFDEEEAQRAVDAYRE
YYKEKGLFENEVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLDGSRVHKA
DVIRYALDTLGIAPEQAVMIGDRKHDIIGARANGIDSIGVLYGYGSEDELEEAGATYIVETPAELLELL
>gnl|CDD|319799 cd04303, HAD_PGPase, phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase PGP/CbbZ. Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LIIFDFDGTLADSFPWFLSILNQLAARHGFKTVDEEEIEQLRQLSSREILKQLGVPLWKLPLIAKDFRRL
MAEAAPELALFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFAVIEGSSLFGKAKKIRRV
LRRTKITAAQVIYVGDETRDIEAARKVGLAFAAVSWGYAKPEVLKALAPDHMLEDPEDLIQ
>gnl|CDD|319800 cd04305, HAD_Neu5Ac-Pase_like, human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases. N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
AIIFDLDDTLLPGAKELLEELKKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIF
DYALNQLGVKPEETLMVGDSLESDILGAKNAGIKTVWFN
>gnl|CDD|319801 cd04309, HAD_PSP_eu, phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase. Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFRDALRKRLAIINPTKEQVDEFLEEHP
PRLTPGVEELVSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSR
SGGKAKVIEQLKEKHHYKRVIMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF
>gnl|CDD|239811 cd04316, ND_PkAspRS_like_N, ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes
HYSAEITPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISV
TGTVKAEPKAPNGVEIIPEEIEVLSEAKTPLPLDPTGK
>gnl|CDD|239812 cd04317, EcAspRS_like_N, EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS
RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEAPEFELAEKLRNESVIQV
TGKVRARPEGTVNPKLPTGEIEVVASELEVLNKAKTLPFEIDDDVNVSEELRLKYRYLDLRRPKM
>gnl|CDD|239813 cd04318, EcAsnRS_like_N, EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli asparaginyl-tRNA synthetase (AsnRS) and, in Arabidopsis thaliana and Saccharomyces cerevisiae mitochondrial (mt) AsnRS. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. S. cerevisiae mtAsnRS can charge E.coli tRNA with asparagines. Mutations in the gene for S. cerevisiae mtAsnRS has been found to induce a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system
EVTVNGWVRSVRDSKKISFIELNDGSCLKNLQVVVDKELTNFKEILKLSTGSSIRVEGVLVKSPGAKQPF
ELQAEKIEVLGE
>gnl|CDD|239814 cd04319, PhAsnRS_like_N, PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose
KVTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSKDLNEEAYREAKKVGIESSVIVEGAVKADPRAPGGA
EVHGEKLEIIQNVEFFPITEDASDEFLLDVRHL
>gnl|CDD|239815 cd04320, AspRS_cyto_N, AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis
EVLIRARVHTSRAQGAKLAFLVLRQQGYTIQGVLAASAEGVSKQMVKWAGSLSKESIVDVEGTVKKPEEP
IKSCTQQDVELHIEKIYVVSEAAEPLPFQLED
>gnl|CDD|239816 cd04321, ScAspRS_mt_like_N, ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae mitochondrial (mt) aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this fungal group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Mutations in the gene for S. cerevisiae mtAspRS result in a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system
KVTLNGWIDRKPRIVKKLSFADLRDPNGDIIQLVSTAKKDAFSLLKSITAESPVQVRGKLQLKEAKSSEK
NDEWELVVDDIQTLNA
>gnl|CDD|239817 cd04322, LysRS_N, LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These enzymes are homodimeric class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Included in this group are E. coli LysS and LysU. These two isoforms of LysRS are encoded by distinct genes which are differently regulated. Eukaryotes contain 2 sets of aaRSs, both of which encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Saccharomyces cerevisiae cytoplasmic and mitochondrial LysRSs have been shown to participate in the mitochondrial import of the only nuclear-encoded tRNA of S. cerevisiae (tRNAlysCUU). The gene for human LysRS encodes both the cytoplasmic and the mitochondrial isoforms of LysRS. In addition to their housekeeping role, human lysRS may function as a signaling molecule that activates immune cells and tomato LysRS may participate in a root-specific process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging
EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFEDFKKLLDLGDIIGVTGTPFKTKTGEL
SIFVKEFTLLSKSLRPLPEKFHGLTDVETRYRQRYLDL
>gnl|CDD|239818 cd04323, AsnRS_cyto_like_N, AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages
RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTEFYDAKSLTQESSVEVTGEVKEDPRAKQAPG
GYELQVDYLEIIGE
>gnl|CDD|239819 cd04327, ZnMc_MMP_like_3, Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin
KLWRNGTVLRIAFLGGPDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGDGYWSYVGTDALL
IGADAPTMNLGWFTDDTPDPEFSRVVLHEFGHALGFIHEHQSPAANIPWDKEAVYAYFSGPPNWDRETVI
NHNVFAKLDDGDVAYSPYDPDSIMHYPFPGSLTLDGEEVPPNRTLSDKDKAFMRLLYP
>gnl|CDD|239820 cd04328, RNAP_I_Rpa43_N, RNAP_I_Rpa43_N: Rpa43, N-terminal ribonucleoprotein (RNP) domain. Rpa43 is a subunit of eukaryotic RNA polymerase (RNAP) I that is homologous to Rpb7 of eukaryotic RNAP II, Rpc25 of eukaryotic RNP III, and RpoE of archaeal RNAP. Rpa43 has two domains, an N-terminal RNP domain and a C-terminal oligonucleotide-binding (OB) domain. Rpa43 heterodimerizes with Rpa14 and this heterodimer has genetic and biochemical characteristics similar to those of the Rpb7/Rpb4 heterodimer of RNAP II. In addition, the Rpa43/Rpa14 heterodimer binds single-stranded RNA, as is the case for the Rpb7/Rpb4 and the archaeal E/F complexes. The position of Rpa43/Rpa14 in the three-dimensional structure of RNAP I is similar to that of Rpb4/Rpb7, which forms an upstream interface between the C-terminal domain of Rpb1 and the transcription factor IIB (TFIIB), recruiting pol II to the pol II promoter. Rpb43 binds Rrn3, an rDNA-specific transcription factor, functionally equivalent to TFIIB, involved in recruiting RNAP I to the pol I promoter
LGAGPYSCFETLTVSLYVSLAPKYLGNPLTGIKAQLLNPLLKYSPKLKGVVLAYSNIKLLEGELAKIVDD
SPFIFVWISADFLVFRPKI
>gnl|CDD|239821 cd04329, RNAP_II_Rpb7_N, RNAP_II_Rpb7_N: Rpb7, N-terminal ribonucleoprotein (RNP) domain. Rpb7 is a subunit of eukaryotic RNA polymerase (RNAP) II that is homologous to Rpc25 of RNAP III, RpoE of archaeal RNAP, and Rpa43 of eukaryotic RNAP I. Rpb7 heterodimerizes with Rpb4 and this heterodimer binds the 10-subunit core of RNAP II, forming part of the floor of the DNA-binding cleft. Rpb7 has two domains, an N-terminal RNP domain and a C-terminal oligonucleotide-binding (OB) domain, both of which bind single-stranded RNA. Rpb7 is thought to interact with the nascent RNA strand as it exits the RNAP II complex during transcription elongation. The Rpb7/Rpb4 heterodimer is also thought to serve as an upstream interface between the C-terminal domain of Rpb1 and the transcription factor IIB (TFIIB), recruiting pol II to the pol II promoter
FFKIELEHNILLHPSYFGPNLKEYLEQKLLEEVEGTCTGDYGYIIAVTDIDDIGEGKILPGTGSVEFPVK
YKAIVFKPFK
>gnl|CDD|239822 cd04330, RNAP_III_Rpc25_N, RNAP_III_Rpc25_N: Rpc25, N-terminal ribonucleoprotein (RNP) domain. Rpc25 is a subunit of eukaryotic RNA polymerase (RNAP) III and is homologous to Rpa43 of eukaryotic RNAP I, Rpb7 of eukaryotic RNAP II, and RpoE of archaeal RNAP. Rpc25 has two domains, an N-terminal RNP domain and a C-terminal oligonucleotide-binding (OB) domain, both of which are thought to bind single-stranded RNA. Rpc25 heterodimerizes with Rpc17 and plays an important role in transcription initiation. RNAP III transcribes diverse structural and catalytic RNAs including 5S ribosomal RNAs, tRNAs, and a small number of snRNAs involved in RNA and protein synthesis
FILSEIEDTVRIPPSQFSRPLNDAIEDELNKKYANKVIQNVGLCICLYDILEVEDGYILPGDGASHYKVT
FRMVVFRPFV
>gnl|CDD|239823 cd04331, RNAP_E_N, RNAP_E_N: RpoE, N-terminal ribonucleoprotein (RNP) domain. RpoE (subunit E) is a subunit of the archaeal RNA polymerase (RNAP) that is homologous to Rpb7 of eukaryotic RNAP II, Rpc25 of eukaryotic RNAP III, and Rpa43 of eukaryotic RNAP I. RpoE heterodimerizes with RpoF, another RNA polymerase subunit. RpoE has an elongated two-domain structure that includes an N-terminal RNP domain and a C-terminal oligonucleotide-binding (OB) domain. Both domains of RpoE bind single-stranded RNA
YKLVELEDVVRVPPELFGEDLEEAVLEILKEKYEGRLDKDLGKIVSVLDVKDVGEGKIVHGDGAVYHEVR
FDALVFKPEL
>gnl|CDD|239824 cd04332, YbaK_like, YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, ProX, and PrdX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express an INS homolog in trans (e.g. YbaK, ProX, or PrdX)
EYLEYEHTPGAKTIEEAAEALGVPPGQIAKTLVLKDDKGGLVLVVVPGDHELDLKKLAKALGAKKLRLAS
EEELEELTGCEPGGVGPFGLKKGVPVVVDESLLELEDVYVGAGERGADLHLSPADLLRLLGEAEVA
>gnl|CDD|239825 cd04333, ProX_deacylase, This CD, composed mainly of bacterial single-domain proteins, includes the Thermus thermophilus (Tt) YbaK-like protein, a homolog of the trans-acting Escherichia coli YbaK Cys-tRNA(Pro) deacylase and the Agrobacterium tumefaciens ProX Ala-tRNA(Pro) deacylase and also the cis-acting prolyl-tRNA synthetase-editing domain (ProRS-INS). While ProX and ProRS-INS hydrolyze misacylated Ala-tRNA(Pro), the E. coli YbaK hydrolyzes misacylated Cys-tRNA(Pro). A few CD members are N-terminal, YbaK-ProX-like domains of an uncharacterized protein with a C-terminal, predicted Fe-S protein domain
VERVRAFLAARGLDLEVIELPESTRTAALAAEALGCEPGQIAKSLVFRVDDEPVLVVTSGDARVDNKKFK
ALFGEKLKMADAEEVRELTGFAIGGVCPFGHPEPLPVYLDESLKRFDEVWAAAGTPNAAFRLTPDELERL
TGAEWVDV
>gnl|CDD|239826 cd04334, ProRS-INS, INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA synthetase (ProRS) however, this CD is not exclusively bacterial. It is also found at the N-terminus of the eukaryotic/archaea-like ProRS's of yeasts and single-celled parasites. ProRS catalyzes the attachment of proline to tRNA(Pro); proline is first activated by ATP, and then transferred to the acceptor end of tRNA(Pro). ProRS can inadvertently process noncognate amino acids such as alanine and cysteine, and to avoid such errors, in post-transfer editing, the INS domain deacylates mischarged Ala-tRNA(Pro), thus ensuring the fidelity of translation. Misacylated Cys-tRNA(Pro) is not edited by ProRS. In addition to the INS editing domain, the prokaryote-like ProRS protein contains catalytic and anticodon-binding domains which form a dimeric interface
DCDYAANIEKAESLPPAAERPAPPKELEKVATPGQKTIEELAEFLGVPPSQTVKTLLVKADGEEELVAVL
LRGDHELNEVKLENLLGAAPLELASEEEIEAATGAPPGFIGPVGLKKIPIIADRSVADLKNFVCGANEDD
YHYVNVNWGRDFPLPEVADL
>gnl|CDD|239827 cd04335, PrdX_deacylase, This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and Clostridium sticklandii PrdX) and eukaryotic (Plasmodium falciparum N-terminal ProRS editing domain) sequences. The C. sticklandii PrdX protein, a homolog of the YbaK and ProX proteins, and the prolyl-tRNA synthetase-editing domain (ProRS-INS), specifically hydrolyzes Ala-tRNA(Pro). In this CD, many of the eukaryotic editing domains are N-terminal and cis-acting, expressed from a multidomain ProRS, however, similar to the bacterial PrdX, the mammalian, amphibian, and echinoderm PrdX-like proteins are trans-acting, single-domain proteins
EDELLALLDELGIAYETVEHPPVFTVEEADEVLGELPGAHTKNLFLKDKKGRLYLVTALHDKKVDLKALS
KQLGASRLSFASEERLEEKLGVTPGSVTPFALINDKENDVQVVLDKDLLEEERVGFHPLTNTATVGISTE
DLLKFLEATGHEPTVV
>gnl|CDD|239828 cd04336, YeaK, YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. The YbaK-like domain family includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, and ProX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express a single-domain INS homolog such as YbaK, ProX, or PrdX which supplies the function of INS in trans
FERLQELLNTNGARFRVLDHPPEGTSEEVAAIRGTELGQGAKALLCKVKDGSRRFVLAVLPADKKLDLKA
VAAAVGGKKADLASPEEAEELTGCVIGAVPPFSFDPKLKLIADPSLLDRGDEIAFNAGRLDASVVLDTAD
YLRIARPLVLQFT
>gnl|CDD|239829 cd04337, Rieske_RO_Alpha_Cao, Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the plastid-envelope inner and thylakoid membranes, that catalyzes the conversion of chlorophyllide a to chlorophyllide b. CAO is found not only in plants but also in chlorophytes and prochlorophytes. This domain represents the N-terminal rieske domain of the oxygenase alpha subunit. ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Cao is closely related to several other plant RO's including Tic 55, a 55 kDa protein associated with protein transport through the inner chloroplast membrane; Ptc 52, a novel 52 kDa protein isolated from chloroplasts; and LLS1/Pao (Lethal-leaf spot 1/pheophorbide a oxygenase)
SRVLGSSLELEPGLRNFWYPVEFSKDLKMDTMVPFELFGQPWVLFRDEDGTPGCIRDECAHRACPLSLGK
VIEGRIQCPYHGWEYDGDGECTKMPSTKCLNVGIAALPCMEQDGMIWVWPGDDPPAALP
>gnl|CDD|239830 cd04338, Rieske_RO_Alpha_Tic55, Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport through the plant inner chloroplast membrane. This domain represents the N-terminal Rieske domain of the Tic55 oxygenase alpha subunit. Tic55 is closely related to the oxygenase alpha subunits of a small subfamily of enzymes found in plants as well as oxygenic cyanobacterial photosynthesizers including LLS1 (lethal leaf spot 1, also known as PaO), Ptc52, and ACD1 (accelerated cell death 1). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis
SEFETPENVAEYDWREEWYPLYLLKDVPTDAPLGLSVYDEPFVLFRDQNGQLRCLEDRCPHRLAKLSEGQ
LIDGKLECLYHGWQFGGEGKCVKIPQLPADAKIPKNACVKSYEVRDSQGVVWMWMSEATPPDEE
>gnl|CDD|239831 cd04365, IlGF_relaxin_like, IlGF_like family, relaxin_like subgroup, specific to vertebrates. Members include a number of active peptides including (pro)relaxin, mammalian Leydig cell-specific insulin-like peptide (gene INSL3), early placenta insulin-like peptide (ELIP; gene INSL4), and insulin-like peptides 5 (INSL5) and 6 (INSL6). Members of this subgroup are widely expressed in testes (INSL3, INSL6), decidua, placenta, prostate, corpus luteum, brain (various relaxins), GI tract, and kidney (INSL5) where they serve a variety of functions in parturition and development. Typically, the active forms of these peptide hormones are composed of two chains (A and B) linked by two disulfide bonds; the arrangement of four cysteines is conserved in the "A" chain: Cys1 is linked by a disulfide bond to Cys3, Cys2 and Cys4 are linked by interchain disulfide bonds to cysteines in the "B" chain. This alignment contains both chains, plus the intervening linker region, arranged as found in the propeptide form. Propeptides are cleaved to yield two separate chains linked covalently by the two disulfide bonds
VVKLCGRELVRAVIEICGGSRWRRLGLDTHSRKKRQFSRGLSEKCCKVGCTKEELAKLC
>gnl|CDD|239832 cd04366, IlGF_insulin_bombyxin_like, IlGF_like family, insulin_bombyxin_like subgroup. Members include a number of peptides including insulin, insulin-like growth factors I and II, insect prothoracicotropic hormone (bombyxin), locust insulin-related peptide (LIRP), molluscan insulin-related peptides 1 to 5 (MIP), and C. elegans insulin-like peptides. With the exception of insulin-like growth factors, the active forms of these peptide hormones are composed of two chains (A and B) linked by two disulfide bonds; the arrangement of four cysteines is conserved in the "A" chain: Cys1 is linked by a disulfide bond to Cys3, Cys2 and Cys4 are linked by interchain disulfide bonds to cysteines in the "B" chain. This alignment contains both chains, plus the intervening linker region, arranged as found in the propeptide form. Propeptides are cleaved to yield two separate chains linked covalently by the two disulfide bonds
YCGRHLADTLALLCSEYNSPRRGIVDECCRKSCTLDELLSYC
>gnl|CDD|239833 cd04367, IlGF_insulin_like, IlGF_like family, insulin_like subgroup, specific to vertebrates. Members include a number of peptides including insulin and insulin-like growth factors I and II, which play a variety of roles in controlling processes such as metabolism, growth and differentiation, and reproduction. On a cellular level they affect cell cycle, apoptosis, cell migration, and differentiation. With the exception of the insulin-like growth factors, the active forms of these peptide hormones are composed of two chains (A and B) linked by two disulfide bonds; the arrangement of four cysteines is conserved in the "A" chain: Cys1 is linked by a disulfide bond to Cys3, Cys2 and Cys4 are linked by interchain disulfide bonds to cysteines in the "B" chain. This alignment contains both chains, plus the intervening linker region, arranged as found in the propeptide form. Propeptides are cleaved to yield two separate chains linked covalently by the two disulfide bonds
VNQHLCGSHLVDALYLVCGDRGFFYTPKRRRDVEDPLVPQEQAAGLQPQAQEEIKRKRGIVEQCCHNICS
LYQLENYCN
>gnl|CDD|239834 cd04368, IlGF, IlGF, insulin_like growth factors; specific to vertebrates. Members include a number of peptides including insulin-like growth factors I and II, which play a variety of roles in controlling processes such as growth, differentiation, and reproduction. On a cellular level they affect cell cycle, apoptosis, cell migration, proliferation, and differentiation. Typically, the active forms of these peptide hormones are single chains cross-linked by three disulfide bonds
GPETLCGGELVDTLQFVCGDRGFYFSKPTGYGSSRRRPNRGIVEECCFRSCDLRLLEMYCAKPKKSE
>gnl|CDD|99922 cd04369, Bromodomain, Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine
LKKKLRSLLDALKKLKRDLSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLI
FSNAKTYNGPGSPIYKDAKKLEKLFEKLL
>gnl|CDD|239835 cd04370, BAH, BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). BAH domains have first been described as domains found in the polybromo protein and Yeast Rsc1/Rsc2 (Remodeling of the Structure of Chromatin). They also occur in mammalian DNA methyltransferases and the MTA1 subunits of histone deacetylase complexes. A BAH domain is also found in Yeast Sir3p and in the origin receptor complex protein 1 (Orc1p), where it was found to interact with the N-terminal lobe of the silence information regulator 1 protein (Sir1p), confirming the initial hypothesis that BAH plays a role in protein-protein interactions
GITYEVGDSVYVEPDDSIKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPFALRRELFLSDH
LDEIPVESIIGKCKVLFVSEFEGLKQRPNKIDTDDFFCRLAYDPTTKEFKALE
>gnl|CDD|239836 cd04371, DEP, DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first discovered. The function of this domain is still not clear, but it is believed to be important for the membrane association of the signaling proteins in which it is present. New studies show that the DEP domain of Sst2, a yeast RGS protein is necessary and sufficient for receptor interaction
DLVRIMLDSDSGVPIKDRKYHLKTYPNCFTGSELVDWLLDNLEAITREEAVELGQALLKHGLIHHVSDDK
HTFRDSYALYR
>gnl|CDD|239837 cd04372, RhoGAP_chimaerin, RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADISATVYPD
INVITGALKLYFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVT
LHEKDNKMNAENLGIVFGPTLMRPPEDSALTTLNDMRYQILIVQLLITNEDVLF
>gnl|CDD|239838 cd04373, RhoGAP_p190, RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p190-like proteins. p190, also named RhoGAP5, plays a role in neuritogenesis and axon branch stability. p190 shows a preference for Rho, over Rac and Cdc42, and consists of an N-terminal GTPase domain and a C-terminal GAP domain. The central portion of p190 contains important regulatory phosphorylation sites. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGVPLANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDFTVNA
VAGALKSFFSELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNS
KVNLMTSENLSICFWPTLMRPDFTSMEALSATRIYQTIIETFIQQ
>gnl|CDD|239839 cd04374, RhoGAP_Graf, RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase regulator associated with focal adhesion kinase); Graf is a multi-domain protein, containing SH3 and PH domains, that binds focal adhesion kinase and influences cytoskeletal changes mediated by Rho proteins. Graf exhibits GAP activity toward RhoA and Cdc42, but only weakly activates Rac1. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
MDGKEPVYHSPGRLQSEVEGEAQLDDIGFKFVRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGLDPK
TSTPGDVDLDNSEWEIKTITSALKTYLRNLPEPLMTYELHNDFINAAKSENLESRVNAIHSLVHKLPEKN
REMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEETVAAIMDIKFQNIVVEILIEN
>gnl|CDD|239840 cd04375, RhoGAP_DLC1, RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
DKNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQ
QAYDVADMLKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDV
AANSQENQMTATNLAVCLAPSLFHLNTSRRENSSPARRMQRKKSLGKPDQKELSENKAAHQCLAYMIEEC
NTLFMVPKEM
>gnl|CDD|239841 cd04376, RhoGAP_ARHGAP6, RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP6-like proteins. ArhGAP6 shows GAP activity towards RhoA, but not towards Cdc42 and Rac1. ArhGAP6 is often deleted in microphthalmia with linear skin defects syndrome (MLS); MLS is a severe X-linked developmental disorder. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
SLNPIARQVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKE
FFRDMPDPLLPRELYTAFIGTALLEPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHAADSIDEDG
QEVSGNKMTSLNLATIFGPNLLHKQKSGEREFVQASLRIEESTAIINVVQTMIDNYEELFMVSPEL
>gnl|CDD|239842 cd04377, RhoGAP_myosin_IX, RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in class IX myosins. Class IX myosins contain a characteristic head domain, a neck domain, a tail domain which contains a C6H2-zinc binding motif and a RhoGAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGVSLSSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVI
TSVLKQWLRELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEE
VNRMSANALAIVFAPCILRCPDTADPLQSLQDVSKTTTCVETLIKE
>gnl|CDD|239843 cd04378, RhoGAP_GMIP_PARG1, RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein) and PARG1 (PTPL1-associated RhoGAP1). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHD
ISSVLKLFLRQLPEPLILFRLYNDFIALAKEIQRDTEEDKAPNTPIEVNRIIRKLKDLLRQLPASNYNTL
QHLIAHLYRVAEQFEENKMSPNNLGIVFGPTLIRPRPGDADVSLSSLVDYGYQARLVEFLITN
>gnl|CDD|239844 cd04379, RhoGAP_SYD1, RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in SYD-1_like proteins. Syd-1, first identified and best studied in C.elegans, has been shown to play an important role in neuronal development by specifying axonal properties. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGVPLSRLVEREGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEELY
PDINVITGVLKDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHLTLSIIDCLPLSAKATLLLLLDH
LSLVLSNSERNKMTPQNLAVCFGPVLMFCSQEFSRYGISPTSKMAAVSTVDFKQHIEVLHYLLQIWP
>gnl|CDD|239845 cd04380, RhoGAP_OCRL1, RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FITVTGVYLPSCFGSSLETLIRLPDPGIRNLIDQLELGDNPDYSEVPLSIPKEIWRLVDYLYTRGLAQEG
LFEEPGLPSEPGELLAEIRDALDTGSPFNSPGSAESVAEALLLFLESLPDPIIPYSLYERLLEAVANNEE
DKRQVIRISLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRAGGKERRAERDRKR
AFIEQFLLND
>gnl|CDD|239846 cd04381, RhoGap_RalBP1, RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in RalBP1 proteins, also known as RLIP, RLIP76 or cytocentrin. RalBP1 plays an important role in endocytosis during interphase. During mitosis, RalBP1 transiently associates with the centromere and has been shown to play an essential role in the proper assembly of the mitotic apparatus. RalBP1 is an effector of the Ral GTPase which itself is an effector of Ras. RalBP1 contains a RhoGAP domain, which shows weak activity towards Rac1 and Cdc42, but not towards Ral, and a Ral effector domain binding motif. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGASLSLAVERSRCHDGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLEEYE
PPTVASLLKQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVI
AQELETKMNIQNISIVLSPTVQISNRLLYALLTHCQELFGNV
>gnl|CDD|239847 cd04382, RhoGAP_MgcRacGAP, RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in MgcRacGAP proteins. MgcRacGAP plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling. ii) after phosphorylation by aurora B MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain a N-terminal C1-like domain, and a C-terminal RhoGAP domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
IGTGELADFDPSTSPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIH
VICGCLKDFLRSLKEPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQS
PECKMDINNLARVFGPTIVGYSVPNPDPMTILQDTVRQPRVVERLLEIPSDYW
>gnl|CDD|239848 cd04383, RhoGAP_srGAP, RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
KLFNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADDQNDH
DINSVAGVLKLYFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHL
SQFSDENMMDPYNLAICFGPTLMPVPEGQDQVSCQAHVNELIKTIIIH
>gnl|CDD|239849 cd04384, RhoGAP_CdGAP, RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVDGIYRLSGIASNIQRLRHEFDSEQIPDLTKDVYIQ
DIHSVSSLCKLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRL
AKYCSITNMHAKNLAIVWAPNLLRSKQIESACFSGTAAFMEVRIQSVVVEFILNH
>gnl|CDD|239850 cd04385, RhoGAP_ARAP, RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
DGPALEDQQLTDNDIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLREGEYTVH
DVADVLKRFLRDLPDPLLTSELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKH
SDENQMSVHNLALVFGPTLFQTDEHSVGQTSHEVKVIEDLIDNY
>gnl|CDD|239851 cd04386, RhoGAP_nadrin, RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEF
YSDPHAVASALKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLS
KLAQKSDENKMSPSNIAIVLAPNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV
>gnl|CDD|239852 cd04387, RhoGAP_Bcr, RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSEMDV
NAIAGTLKLYFRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAE
REEVNKMSLHNLATVFGPTLLRPSEKESKIPTNTMTDSWSLEVMSQVQVLLYFLQL
>gnl|CDD|239853 cd04388, RhoGAP_p85, RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in the p85 isoforms of the regulatory subunit of the class IA PI3K (phosphatidylinositol 3'-kinase). This domain is also called Bcr (breakpoint cluster region protein) homology (BH) domain. Class IA PI3Ks are heterodimers, containing a regulatory subunit (p85) and a catalytic subunit (p110) and are activated by growth factor receptor tyrosine kinases (RTKs); this activation is mediated by the p85 subunit. p85 isoforms, alpha and beta, contain a C-terminal p110-binding domain flanked by two SH2 domains, an N-terminal SH3 domain, and a RhoGAP domain flanked by two proline-rich regions. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
TLPDLTEQFSPPDVAPPLLIKLVEAIEKKGLESSTLYRTQSSSSLTELRQILDCDAASVDLEQFDVAALA
DALKRYLLDLPNPVIPAPVYSEMISRAQEVQSSDEYAQLLRKLIRSPNLPHQYWLTLQYLLKHFFRLCQS
SSKNLLSARALAEIFSPLLFRFQPASSDSPEFHIRIIEVLITSEWNERQAAPALPPKPPK
>gnl|CDD|239854 cd04389, RhoGAP_KIAA1688, RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGSSLEEIMDRQKEKYPELKLPWILTFLSEKVLALGGFQTEGIFRVPGDIDEVNELKLRVDQWDYPLSGL
EDPHVPASLLKLWLRELEEPLIPDALYQQCISASEDPDKAVEIVQKLPIINRLVLCYLINFLQVFAQPEN
VAHTKMDVSNLAMVFAPNILRCTSDDPRVIFENTRKEMSFLRTLIEH
>gnl|CDD|239855 cd04390, RhoGAP_ARHGAP22_24_25, RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDS
DTDVHTVASLLKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRF
LDEVQSNSSVNKMSVQNLATVFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF
>gnl|CDD|239856 cd04391, RhoGAP_ARHGAP18, RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP18-like proteins. The function of ArhGAP18 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
LFGVPLSTLLERDQKKVPGSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKFYEGTFL
WDQVKQHDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEF
LQKVVDHEEKNKMNLWNVAMIMAPNLFPPRGKHSKDNESLQEEVNMAAGCANIMRLLIRYQDLLWTVPSF
LINQVR
>gnl|CDD|239857 cd04392, RhoGAP_ARHGAP19, RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP19-like proteins. The function of ArhGAP19 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGAPLTEEGIAQIYQLIEYLEKNLRVEGLFRKPGNSARQQELRDLLNSGTDLDLESGGFHAHDCATVLKG
FLGELPEPLLTHAHYPAHLQIADLCQFDEKGNKTSAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQ
TAKHEDKNKMSADNLALLFTPHLICPRNLTPEDLHENAQKLNSIVTFMIKHSQKLFKAPAYLREDARA
>gnl|CDD|239858 cd04393, RhoGAP_FAM13A1a, RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of FAM13A1, isoform a-like proteins. The function of FAM13A1a is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by up several orders of magnitude
KVFGVPLQELQQAGQPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEA
DVCSAASLLRLFLQELPEGLIPASLQIRLMQLYQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSN
VASQHHENRMTAENLAAVFGPDVFHVYTDVEDMKEQEICSRIMAKLLEN
>gnl|CDD|239859 cd04394, RhoGAP-ARHGAP11A, RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP11A-like proteins. The mouse homolog of human ArhGAP11A has been detected as a gene exclusively expressed in immature ganglion cells, potentially playing a role in retinal development. The exact function of ArhGAP11A is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
VFGVPLHSLPHSTVPEYGNVPKFLVDACTFLLDHLSTEGLFRKSGSVVRQKELKAKLEGGEACLSSALPC
DVAGLLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQR
CSENKMDSSNLAVIFAPNLFQSEEGGEKMSSSTEKRLRLQAAVVQTLIDNASNIGIVPDFIL
>gnl|CDD|239860 cd04395, RhoGAP_ARHGAP21, RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
TFGVPLDDCPPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQDPRW
RDVNVVSSLLKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKT
VADNSEVNKMEPRNLAIVFGPTLVRTSDDNMETMVTHMPDQCKIVETLIQHYDWFF
>gnl|CDD|239861 cd04396, RhoGAP_fSAC7_BAG7, RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal SAC7 and BAG7-like proteins. Both proteins are GTPase activating proteins of Rho1, but differ functionally in vivo: SAC7, but not BAG7, is involved in the control of Rho1-mediated activation of the PKC-MPK1 pathway. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
VFGVSLEESLKYASVAISIVDEDGEQYVYGYIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIF
STPPDYGKSFDWDGYTVHDAASVLRRYLNNLPEPLVPLDLYEEFRNPLRKRPRILQYMKGRINEPLNTDI
DQAIKEYRDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGILSHPDHEMDPKEYKLS
RLVVEFLIEHQDKFL
>gnl|CDD|239862 cd04397, RhoGAP_fLRG1, RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGVPLEILVEKFGADSTLGVGPGKLRIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPT
EVPDLSKENPVQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEV
LFSFLKWVSSFSHIDEETGSKMDIHNLATVITPNILYSKTDNPNTGDEYFLAIEAVNYLIENNEEFCEVP
DEL
>gnl|CDD|239863 cd04398, RhoGAP_fRGD1, RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD1-like proteins. Yeast Rgd1 is a GAP protein for Rho3 and Rho4 and plays a role in low-pH response. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLISPEDYE
SDIHSVASLLKLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLAR
IKEHESVNRMSVNNLAIIWGPTLMNAAPDNAADMSFQSRVIETLLDNAYQIF
>gnl|CDD|239864 cd04399, RhoGAP_fRGD2, RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGVDLETRCRLDKKVVPLIVSAILSYLDQLYPDLINDEVRRNVWTDPVSLKETHQLRNLLNKPKKPDKEV
IILKKFEPSTVASVLKLYLLELPDSLIPHDIYDLIRSLYSAYPPSQEDSDTARIQGLQSTLSQLPKSHIA
TLDAIITHFYRLIEITKMGESEEEYADKLATSLSREILRPIIESLLTIGDKHGYKFFRDLLTHKDQIFSE
LK
>gnl|CDD|239865 cd04400, RhoGAP_fBEM3, RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
IFGSPLEEAVELSSHKYNGRDLPSVVYRCIEYLDKNRAIYEEGIFRLSGSASVIKQLKERFNTEYDVDLF
SSSLYPDVHTVAGLLKLYLRELPTLILGGELHNDFKRLVEENHDRSQRALELKDLVSQLPQANYDLLYVL
FSFLRKIIEHSDVNKMNLRNVCIVFSPTLNIPAGIFVLFLTDFDCIFGGI
>gnl|CDD|239866 cd04401, RhoGAP_fMSB1, RhoGAP_fMSB1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal MSB1-like proteins. Msb1 was originally identified as a multicopy suppressor of temperature sensitive cdc42 mutation. Msb1 is a positive regulator of the Pkc1p-MAPK pathway and 1,3-beta-glucan synthesis, both pathways involve Rho1 regulation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
VSAESVKGLIHNITEELKSRGLDTPLLFLPFRPELSPDKVRSLINSFFPSQNGQLQGTAELLDELRYADP
HTLILVLKWIWSRLPGSKVIWWEVYEEFKARERRSNYPADAFLDLLPQCLSSPAHASILYDFFDLLSSIA
AHSSVNGMSGRKLSKMAGPWAFGKPTGATGPPSFQEGLDAWVRAANATEHLFLAYLRS
>gnl|CDD|239867 cd04402, RhoGAP_ARHGAP20, RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
LFGQPLSNICEDDNLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVEVDLKAEPVLLLA
SVLKDFLRNIPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSET
NKMDAFNLAVCIAPSLLWPPASSELQNEDLKKVTSLVQFLIENCQEIFGEDI
>gnl|CDD|239868 cd04403, RhoGAP_ARHGAP27_15_12_9, RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15, 12 and 9-like proteins; This subgroup of ARHGAPs are multidomain proteins that contain RhoGAP, PH, SH3 and WW domains. Most members that are studied show GAP activity towards Rac1, some additionally show activity towards Cdc42. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLDLDDSKWEDI
HVITGALKLFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIE
HGEKNRMTTQNLAIVFGPTLLRPEQETGNIAVHMVYQNQIVELILLE
>gnl|CDD|239869 cd04404, RhoGAP-p50rhoGAP, RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
LPTQQFGVSLQFLKEKNPEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEPVDFD
QYEDVHLPAVILKTFLRELPEPLLTFDLYDDIVGFLNVDKEERVERVKQLLQTLPEENYQVLKYLIKFLV
QVSAHSDQNKMTNSNLAVVFGPNLLWAKDASMSLSAINPINTFTKFLLDHQDEIF
>gnl|CDD|239870 cd04405, RhoGAP_BRCC3-like, RhoGAP_BRCC3-like: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of BRCC3-like proteins. This subgroup also contains two groups of closely related proteins, BRCC3 and DEPDC7, which both contain a C-terminal RhoGAP-like domain and an N-terminal DEP (Disheveled, Egl-10, and Pleckstrin) domain. The function(s) of BRCC3 and DEPDC7 are unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
LSPEVVEEIWKEQTLIRLLQLVGLPLLEELLDPALVNPKHISYNMDPDVYTSNYLDREVVKLFSKSQLDH
WLLSAMDCLANWPDQLVVDVSRPLYSQHDMLSGFKRLLFKTIAKYYGQLKEPLLTFHLFDIFVGILELLG
NGKEEVALEALQLCLLLLPPASRRELRRLLRFMARAAKNDMPRLHKEIENRMLVKQTFSRAILCSKDLDE
GLADLLVLFLMDHHQDIFKVPGSLH
>gnl|CDD|239871 cd04406, RhoGAP_myosin_IXA, RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXA. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGVELSRLTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVI
ASVFKQWLRDLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEE
TNRMSANALAIVFAPCILRCPDTTDPLQSVQDISKTTTCVELIVCE
>gnl|CDD|239872 cd04407, RhoGAP_myosin_IXB, RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAI
TGLLKQWLRELPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEED
VNRMSPNALAIVFAPCLLRCPDSSDPLTSMKDVAKTTTCVEMLIKE
>gnl|CDD|239873 cd04408, RhoGAP_GMIP, RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHD
ITSVLKHFLKELPEPVLPFQLYDDFIALAKELQRDSEKAAESPSIVENIIRSLKELLGRLPVSNYNTLRH
LMAHLYRVAERFEDNKMSPNNLGIVFGPTLLRPLVGGDVSMICLLDTGYQAQLVEFLISN
>gnl|CDD|239874 cd04409, RhoGAP_PARG1, RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude
FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHD
ISNVLKLYLRQLPEPLILFRLYNEFIGLAKESQHVNETQEAKKNSDKKWPNMCTELNRILLKSKDLLRQL
PAPNYNTLQFLIVHLHRVSEQAEENKMSASNLGIIFGPTLIRPRPTDATVSLSSLVDYPHQARLVELLIT
Y
>gnl|CDD|319870 cd04410, DMSOR_beta-like, Beta subunit of the DMSO Reductase (DMSOR) family. This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system
LVVDLDRCIGCGTCEVACKQEHGLRPGPDWSRIKVIEGGGLERAFLPVSCMHCEDPPCVKACPTGAIYKD
EDGIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG
>gnl|CDD|100108 cd04411, Ribosomal_P1_P2_L12p, Ribosomal protein P1, P2, and L12p. Ribosomal proteins P1 and P2 are the eukaryotic proteins that are functionally equivalent to bacterial L7/L12. L12p is the archaeal homolog. Unlike other ribosomal proteins, the archaeal L12p and eukaryotic P1 and P2 do not share sequence similarity with their bacterial counterparts. They are part of the ribosomal stalk (called the L7/L12 stalk in bacteria), along with 28S rRNA and the proteins L11 and P0 in eukaryotes (23S rRNA, L11, and L10e in archaea). In bacterial ribosomes, L7/L12 homodimers bind the extended C-terminal helix of L10 to anchor the L7/L12 molecules to the ribosome. Eukaryotic P1/P2 heterodimers and archaeal L12p homodimers are believed to bind the L10 equivalent proteins, eukaryotic P0 and archaeal L10e, in a similar fashion. P1 and P2 (L12p, L7/L12) are the only proteins in the ribosome to occur as multimers, always appearing as sets of dimers. Recent data indicate that most archaeal species contain six copies of L12p (three homodimers), while eukaryotes have two copies each of P1 and P2 (two heterodimers). Bacteria may have four or six copies (two or three homodimers), depending on the species. As in bacteria, the stalk is crucial for binding of initiation, elongation, and release factors in eukaryotes and archaea
MEYVAAYLLLHKGGKELTEDKIKELLSAAGAEIEPERVKLFLSALNGKNIDEVISKGKELMSSQAAAAAA
PAATAAATAEPAEKAEEAKEEEEEEEDEDFGFGLF
>gnl|CDD|239875 cd04412, NDPk7B, Nucleoside diphosphate kinase 7 domain B (NDPk7B): The nm23-H7 class of nucleoside diphosphate kinase (NDPk7) consists of an N-terminal DM10 domain and two functional catalytic NDPk modules, NDPk7A and NDPk7B. The function of the DM10 domain, which also occurs in multiple copies in other proteins, is unknown. NDPk7 is predominantly expressed in testes, although appreciable amount are also found in liver, heart, brain, ovary, small intestine and spleen. The nm23-H7 gene is located in or near the hereditary prostrate cancer susceptibility locus. Nm23-H7 may be involved in the development of colon and gastric carcinoma, the latter possibly in a type-specific manner
NCTVCIIKPHAVSHGLLGEILQQILDEGFEITALQMFNLTRANAEEFLEVYKGVVPELPAMVDELTSGPC
IALEIAGENAVKTFREFCGPFDPEIAKQLRPNTLRARYGKDKVQNAVHCTDLPEDGPLELKFFF
>gnl|CDD|239876 cd04413, NDPk_I, Nucleoside diphosphate kinase Group I (NDPk_I)-like: NDP kinase domains are present in a large family of structurally and functionally conserved proteins from bacteria to humans that generally catalyze the transfer of gamma-phosphates of a nucleoside triphosphate (NTP) donor onto a nucleoside diphosphate (NDP) acceptor through a phosphohistidine intermediate. The mammalian nm23/NDP kinase gene family can be divided into two distinct groups. The group I genes encode proteins that generally have highly homologous counterparts in other organisms and possess the classic enzymatic activity of a kinase. This group includes vertebrate NDP kinases A-D (Nm23- H1 to -H4), and its counterparts in bacteria, archea and other eukaryotes. NDP kinases exist in two different quaternary structures; all known eukaryotic enzymes are hexamers, while some bacterial enzymes are tetramers, as in Myxococcus. They possess the NDP kinase active site motif (NXXH[G/A]SD) and the nine residues that are most essential for catalysis
ERTLVIIKPDGVQRGLIGEIISRFERKGLKIVALKMLQLTEELAEEHYAEHKGKPFFPELVEFMTSGPVV
AMVLEGENAVKTVRKLMGATNPADAAPGTIRGDFALSIGRNIVHGSDSVESAEREIALWF
>gnl|CDD|239877 cd04414, NDPk6, Nucleoside diphosphate kinase 6 (NDP kinase 6, NDPk6, NM23-H6; NME6; Inhibitor of p53-induced apoptosis-alpha, IPIA-alpha): The nm23-H6 gene encoding NDPk6 is expressed mainly in mitochondria, but also found at a lower level in most tissues. NDPk6 has all nine residues considered crucial for enzyme structure and activity, and has been found to have NDP kinase activity. It may play a role in cell growth and cell cycle progression. The nm23-H6 gene locus has been implicated in a variety of malignant tumors
QLTLALIKPDAVAHPLALEAVRQLILSNGFTIVRKKELRWTTEDAERFYAEHKGKFFYDRLVSFMTSGPS
WALILAHENAIKTWRALMGPTKVFRARASAPDSIRGLYGLTDTRNATHGSDSPASAQREIALFFP
>gnl|CDD|239878 cd04415, NDPk7A, Nucleoside diphosphate kinase 7 domain A (NDPk7A): The nm23-H7 class of nucleoside diphosphate kinase (NDPk7) consists of an N-terminal DM10 domain and two functional catalytic NDPk modules, NDPk7A and NDPk7B. The function of the DM10 domain, which also occurs in multiple copies in other proteins, is unknown. NDPk7 is predominantly expressed in testes, although appreciable amount are also found in liver, heart, brain, ovary, small intestine and spleen. The nm23-H7 gene is located in or near the hereditary prostrate cancer susceptibility locus. Nm23-H7 may be involved in the development of colon and gastric carcinoma, the latter possibly in a type-specific manner
EKTLALIKPDAYSKIGKIIQIIEDAGFTITKAKMTKLSRKEAQDFYAEHQSKPFYNELVQFMTSGPIVAM
ELVGDDAISEWRKLLGPTNSSVARSDAPNSIRALFGTDGTRNAAHGSDSVASAARELEFFF
>gnl|CDD|239879 cd04416, NDPk_TX, NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 (TXNDC6) and Sptrx-2 (TXNDC3) are fusion proteins of Group II N-terminal thioredoxin domains followed by one or three NDP kinase domains, respectively. Sptrx-2, which has a tissue specific distribution in human testis, has been considered as a member of the nm23 family (nm23-H8) and exhibits a high homology with sea urchin IC1 (intermediate chain-1) protein, a component of the sperm axonemal outer dynein arm complex. Txl-2 is mainly represented in close association with microtubules within tissues with cilia and flagella such as seminiferous epithelium (spermatids) and lung airway epithelium, suggesting possible role in control of microtubule stability and maintenance
EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLI
LVLSKENAVEEWRELMGPTDPEEAKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF
>gnl|CDD|239880 cd04418, NDPk5, Nucleoside diphosphate kinase homolog 5 (NDP kinase homolog 5, NDPk5, NM23-H5; Inhibitor of p53-induced apoptosis-beta, IPIA-beta): In human, mRNA for NDPk5 is almost exclusively found in testis, especially in the flagella of spermatids and spermatozoa, in association with axoneme microtubules, and may play a role in spermatogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. It belongs to the nm23 Group II genes and appears to differ from the other human NDPks in that it lacks two important catalytic site residues, and thus does not appear to possess NDP kinase activity. NDPk5 confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes, including glutathione peroxidase 5 (Gpx5)
ERTLAIIKPDAVHKAEEIEDIILESGFTIVQKRKLQLSPEQCSDFYAEHYGKMFFPHLVAYMSSGPIVAM
VLARHNAISYWKELLGPTNSLKAKETHPDSLRAIYGTDDLRNAVHGSDSFSSAEREIRFMFP
>gnl|CDD|341228 cd04433, AFD_class_I, Adenylate forming domain, Class I, also known as the ANL superfamily. This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVV
LLPKFDPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGI
KLVNGYGLTETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWN
NPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPD
PEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID
>gnl|CDD|271198 cd04434, LanC_like, Cyclases involved in the biosynthesis of lantibiotics, and similar proteins. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions
YHGAAGIALFLLELYRATGDKEYLDEAKEGADYLLARLEGLGEPLSGASLYSGLSGLLWALLELYEDLGD
EKLLDALLDLLDDIALEAKEVWWSGNDLILGDAGIILYLLYAAEKTGDEKYKELAAKIGDFLLQAAEELD
NGGNWGLPKGSIYPGFAHGTAGIAYALARLYEETGDEDFLDAAKEGAEYLEAIAVGDEDGFLIPLPDEKD
LFYLGWCHGPAGTALLFYELYKATGDLDLADELLEGIIKTGAPEKLSPGFWNNLCLCHGTAGVLEHLLYV
YRLTGDEREYAKRLADKLLGRATRNGEGLRWYQAWTGPGRVDASLGLMVGAAGIASALLKLLRAETKARP
L
>gnl|CDD|239882 cd04435, DEP_fRom2, DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange factor) Rom2-like proteins. Rom2-like proteins share a common domain architecture, containing, beside the RhoGEF domain, a DEP, a PH (pleckstrin homology) and a CNH domain. Rom2, a yeast GEF for Rho1 and Rho2, is involved in mediating stress response via the Ras-cAMP pathway and also plays a role in mediating resistance to sphingolipid disturbances
LLSRVALQLRDKIPLGDHTKDGITYRNSFTGKDAVTTIQGIIRTSDRNLALLLGRSLDAQKFFHDVTYDH
RLRDSVDEVYRF
>gnl|CDD|239883 cd04436, DEP_fRgd2, DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGAP (GTPase-activator protein) Rgd2-like proteins. Rgd2-like proteins share a common domain architecture, containing, beside the RhoGAP domain, a DEP and a FCH (Fes/CIP4 homology) domain. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5
SLKELLAAMLKEIPLADYKVPILGTYQNTSSGSEIVSWLQENMPEKDLDAAEAFGQDLLNQGFLRLVGGV
GSTFVNSSKFQYQW
>gnl|CDD|239884 cd04437, DEP_Epac, DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange proteins directly activated by cAMP) proteins are GEFs (guanine-nucleotide-exchange factors) for the small GTPases, Rap1 and Rap2. They are directly regulated by cyclic AMP, a second messenger that plays a role in the control of diverse cellular processes, such as cell adhesion and insulin secretion. Epac-like proteins share a common domain architecture, containing RasGEF, DEP and CAP-effector (cAMP binding) domains. The DEP domain is involved in membrane localization
AGRALRNAILSDAPHLIRDRKYHLRTYRQCCVGTELVDWLLQQSPCVQSRSQAVGMWQVLLEEGVLLHVD
QELHFQDKYQFYRFSDDECSPAPLEKREAEEELQEAVTLLSQLGPDALLRMILRK
>gnl|CDD|239885 cd04438, DEP_dishevelled, DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in dishevelled-like proteins. Dishevelled-like proteins play a key role in the transduction of the Wnt signal from the cell surface to the nucleus, which in turn is an important regulatory pathway for cellular development and growth. They contain an N-terminal DIX domain, a central PDZ domain, and a C-terminal DEP domain
NGIPRVMRRPDSGLEIKDRMWLKITIPNSFIGSDLVDWLLSHVEGLTDRREARKYASSLLKLGYIRHTVN
KITFSEQCYYVFGD
>gnl|CDD|239886 cd04439, DEP_1_P-Rex, DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in P-Rex-like proteins. The P-Rex family is the guanine-nucleotide exchange factor (GEF) for the small GTPase Rac that contains an N-terminal RhoGEF domain, two DEP and PDZ domains. Rac-GEF activity is stimulated by phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3), a lipid second messenger, and by the G beta-gamma subunits of heterotrimeric G proteins. The DEP domains are not involved in mediating these stimuli, but may be of importance for basal and stimulated levels Rac-GEF activity
GEKLYKMMCKQGSLIKDRRRKLSTFPKCFLGNEFVSWLLEIGEISKPEEGVNLGQALLENGIIHHVSDKH
QFKNEQVLYRF
>gnl|CDD|239887 cd04440, DEP_2_P-Rex, DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in P-Rex-like proteins. The P-Rex family is the guanine-nucleotide exchange factor (GEF) for the small GTPase Rac that contains an N-terminal RhoGEF domain, two DEP and PDZ domains. Rac-GEF activity is stimulated by phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3), a lipid second messenger, and the G beta-gamma subunits of heterotrimeric G proteins. The DEP domains are not involved in mediating these stimuli, but may be of importance for basal and stimulated levels Rac-GEF activity
EMEDIMSKGVRLYCRLHSLFTPVVKDRDYHLKTYKSVVPASKLVDWLLAQGDCRTREEAVILGVGLCNNG
FMHHVLEKSEFKDEPLLFRFYAD
>gnl|CDD|239888 cd04441, DEP_2_DEP6, DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in DEP6-like proteins. DEP6 proteins contain two DEP and a PDZ domain. Their function is unknown
FMRGQRLYEKLMSTENSILQVREEEGVKYERTFVGSEFIDWLLQEGEAESRREAVQLCRRLLEHGIIQHV
SNKHHFFDSNLLYQF
>gnl|CDD|239889 cd04442, DEP_1_DEP6, DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins contain two DEP and a PDZ domain. Their function is unknown
TGEQLRLRLHEAKVIKDRRHHLRTYPNCFVGKELIDWLIEHKEASDRETAIKIMQKLLDHSIIHHVCDEH
KEFKDAKLFYRF
>gnl|CDD|239890 cd04443, DEP_GPR155, DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like proteins, also known as PGR22, contain an N-terminal permease domain, a central transmembrane region and a C-terminal DEP domain. They are orphan receptors of the class B G protein-coupled receptors. Their function is unknown
CEQFVRYHLDQCRQDIVKDRRCGLRTYKGVFCGCDLVSWLIEVGLAQDRGEAVLYGRRLLQGGVLQHITN
EHHFRDENLLYRF
>gnl|CDD|239891 cd04444, DEP_PLEK2, DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in pleckstrin 2-like proteins. Pleckstrin 2 is found in a wide variety of cell types, which suggest a more general role in signaling than pleckstrin 1. Pleckstrin-like proteins contain a central DEP domain, flanked by 2 PH (pleckstrin homology) domains
SLHRIVDKMHDSSTGIRHSPNMEQGSTYKKTFLGSALVDWLISNSFAASRLEAVTLASMLMEENFLRPVG
VRSMGAIRSGDLAEQFLDDSTALYTFAESYKKKGSSKEE
>gnl|CDD|239892 cd04445, DEP_PLEK1, DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in pleckstrin 1-like proteins. Pleckstrin 1 plays a role in cell spreading and reorganization of actin cytoskeleton in platelets and leukocytes. Its activity is highly regulated by phosphorylation, mainly by protein kinase C. Pleckstrin-like proteins contain a central DEP domain, flanked by 2 PH (pleckstrin homology) domains
NLSALYLSMKDPEKGIKELNLEKDKKVFNHCFTGSCVIDWLVSNQSVRNRQEGLMLASSLLNEGYLQPAG
DTSKNAADGLAENPFLDNPDAFYYFPDSG
>gnl|CDD|239893 cd04446, DEP_DEPDC4, DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC4-like proteins. DEPDC4 is a DEP domain containing protein of unknown function
WNSIIDALQTQVEVKKRRHNLKSYHDCFLGSEAVDVVLAHLMQNKYFGDVDVPRAKAVRLCQALMDCRVF
EAVGTKVFKKKKRAVFEDSSSSLYR
>gnl|CDD|239894 cd04447, DEP_BRCC3, DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in BBRC3-like proteins. BBRC3, also known as DEPDC1B, is a DEP containing protein of unknown function
KLWNEVTELFRAGMPLRKHRQHFKSYENCFTASEAVDWLHELLRSNSNFGPEVTRQQTVQLLKKFLKNHV
IEDIKGRWGKEDLEDNNHLYRF
>gnl|CDD|239895 cd04448, DEP_PIKfyve, DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange factor) PIKfyve-like proteins. PIKfyve contains N-terminal Fyve finger and DEP domains, a central chaperonin-like domain and a C-terminal PIPK (phosphatidylinositol phosphate kinase) domain. PIKfyve-like proteins are important phosphatidylinositol (3)-monophosphate (PtdIns(3)P)-5-kinases, producing PtdIns(3,5)P2, which plays a major role in multivesicular body (MVB) sorting and control of retrograde traffic from the vacuole back to the endosome and/or Golgi. PIKfyve itself has been shown to be play a role in regulating early-endosome-to-trans-Golgi network (TGN) retrograde trafficking
DLWEKICRSSTGIEFQDHRYRLRTYTNCILGKELVNWLIRQGKAATRVQAIAIGQALLDAGWIECVSDDD
LFRDEYALYKP
>gnl|CDD|239896 cd04449, DEP_DEPDC5-like, DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in human also known as KIAA0645, is a DEP domain containing protein of unknown function
LAEIAEAMRDPSGIGIFDRSWHKGLPSNCFIGSEAVSWLINNFEDVDTREEAVELGQELMNEGLIEHVSG
RHPFLDGFYFYYI
>gnl|CDD|239897 cd04450, DEP_RGS7-like, DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in RGS (regulator of G-protein signaling) proteins of the subfamily R7. This subgroup contains RGS7, RGS6, RGS9 and RGS11. They share a common domain architecture, containing, beside the RGS domain, a DEP domain and a GGL (G-protein gamma subunit-like) domain. RGS proteins are GTPase-activating (GAP) proteins of heterotrimeric G proteins by increasing the rate of GTP hydrolysis of the alpha subunit. The fungal homologs, like yeast Sst2, share a related common domain architecture, containing RGS and DEP domains. Sst2 has been identified as the principal regulator of mating pheromone signaling and recently the DEP domain of Sst2 has been shown to be necessary and sufficient to mediate receptor interaction
DSVGQMQDSEVGVRMRTEKSFLTTVPYAFTGKAIVQWLMDCTDVVDPSEALEIAALFVKYGLITPVSDHR
SLLKPDETLYRFQAPYFW
>gnl|CDD|239898 cd04451, S1_IF1, S1_IF1: Translation Initiation Factor IF1, S1-like RNA-binding domain. IF1 contains an S1-like RNA-binding domain, which is found in a wide variety of RNA-associated proteins. Translation initiation includes a number of interrelated steps preceding the formation of the first peptide bond. In Escherichia coli, the initiation mechanism requires, in addition to mRNA, fMet-tRNA, and ribosomal subunits, the presence of three additional proteins (initiation factors IF1, IF2, and IF3) and at least one GTP molecule. The three initiation factors influence both the kinetics and the stability of ternary complex formation. IF1 is the smallest of the three factors. IF1 enhances the rate of 70S ribosome subunit association and dissociation and the interaction of 30S ribosomal subunit with IF2 and IF3. It stimulates 30S complex formation. In addition, by binding to the A-site of the 30S ribosomal subunit, IF1 may contribute to the fidelity of the selection of the initiation site of the mRNA
IEMEGVVTEALPNAMFRVELENGHEVLAHISGKMRMNYIRILPGDRVKVELSPYDLTKGRIVYR
>gnl|CDD|239899 cd04452, S1_IF2_alpha, S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Eukaryotic and archaeal Initiation Factor 2 (e- and aIF2, respectively) are heterotrimeric proteins with three subunits (alpha, beta, and gamma). IF2 plays a crucial role in the process of translation initiation. The IF2 gamma subunit contains a GTP-binding site. The IF2 beta and gamma subunits together are thought to be responsible for binding methionyl-initiator tRNA. The ternary complex consisting of IF2, GTP, and the methionyl-initiator tRNA binds to the small subunit of the ribosome, as part of a pre-initiation complex that scans the mRNA to find the AUG start codon. The IF2-bound GTP is hydrolyzed to GDP when the methionyl-initiator tRNA binds the AUG start codon, at which time the IF2 is released with its bound GDP. The large ribosomal subunit then joins with the small subunit to complete the initiation complex, which is competent to begin translation. The IF2a subunit is a major site of control of the translation initiation process, via phosphorylation of a specific serine residue. This alpha subunit is well conserved in eukaryotes and archaea but is not present in bacteria. IF2 is a cold-shock-inducible protein
PEEGELVVVTVKSIADMGAYVSLLEYGNIEGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVDKEKGYI
DLSKKR
>gnl|CDD|239900 cd04453, S1_RNase_E, S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential endoribonuclease in the processing and degradation of RNA. In addition to its role in mRNA degradation, RNase E has also been implicated in the processing of rRNA, and the maturation of tRNA, 10Sa RNA and the M1 precursor of RNase P. RNase E associates with PNPase (3' to 5' exonuclease), Rhl B (DEAD-box RNA helicase) and enolase (glycolytic enzyme) to form the RNA degradosome. RNase E tends to cut mRNA within single-stranded regions that are rich in A/U nucleotides. The N-terminal region of RNase E contains the catalytic site. Within the conserved N-terminal domain of RNAse E and RNase G, there is an S1-like subdomain, which is an ancient single-stranded RNA-binding domain. S1 domain is an RNA-binding module originally identified in the ribosomal protein S1. The S1 domain is required for RNA cleavage by RNase E. RNase G is paralogous to RNase E with an N-terminal catalytic domain that is highly homologous to that of RNase E. RNase G not only shares sequence similarity with RNase E, but also functionally overlaps with RNase E. In Escherichia coli, RNase G is involved in the maturation of the 5' end of the 16S rRNA. RNase G plays a secondary role in mRNA decay
PNREPIVGNIYLGRVKKIVPGLQAAFVDIGLGKNGFLHLSDILPAYFKKHKKIAKLLKEGQEILVQVVKE
PIGTKGPRLTTNISLPGR
>gnl|CDD|239901 cd04454, S1_Rrp4_like, S1_Rrp4_like: Rrp4-like, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Rrp4 protein, and Rrp40 and Csl4 proteins, also represented in this group, are subunits of the exosome complex. The exosome plays a central role in 3' to 5' RNA processing and degradation in eukarytes and archaea. Its functions include the removal of incorrectly processed RNA and the maintenance of proper levels of mRNA, rRNA and a number of small RNA species. In Saccharomyces cerevisiae, the exosome includes nine core components, six of which are homologous to bacterial RNase PH. These form a hexameric ring structure. The other three subunits (RrP4, Rrp40, and Csl4) contain an S1 RNA binding domain and are part of the "S1 pore structure"
RYLPDVGDIVIGIVTEVNSRFWKVDILSRGTARLEDSSATEKDKKEIRKSLQPGDLILAKVISLGDDMNV
LLTTADNELGVI
>gnl|CDD|239902 cd04455, S1_NusA, S1_NusA: N-utilizing substance A protein (NusA), S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. NusA is a transcription elongation factor containing an N-terminal catalytic domain and three RNA binding domains (RBD's). The RBD's include one S1 domain and two KH domains that form an RNA binding surface. DNA transcription by RNA polymerase (RNAP) includes three phases - initiation, elongation, and termination. During initiation, sigma factors bind RNAP and target RNAP to specific promoters. During elongation, N-utilization substances (NusA, B, E, and G) replace sigma factors and regulate pausing, termination, and antitermination. NusA is cold-shock-inducible
DREGEIVTGIVKRVDRGNVIVDLGKVEAILPKKEQIPGESYRPGDRIKAYVLEVRKTSKGPQIILSR
>gnl|CDD|239903 cd04456, S1_IF1A_like, S1_IF1A_like: Translation initiation factor IF1A-like, S1-like RNA-binding domain. IF1A is also referred to as eIF1A in eukaryotes and aIF1A in archaea. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. IF1A is essential for translation initiation. eIF1A acts synergistically with eIF1 to mediate assembly of ribosomal initiation complexes at the initiation codon and maintain the accuracy of this process by recognizing and destabilizing aberrant preinitiation complexes from the mRNA. Without eIF1A and eIF1, 43S ribosomal preinitiation complexes can bind to the cap-proximal region, but are unable to reach the initiation codon. eIF1a also enhances the formation of 5'-terminal complexes in the presence of other translation initiation factors. This protein family is only found in eukaryotes and archaea
QQIVRVLRMLGNNRHEVECADGQRRLVSIPGKLRKNIWIKRGDFLIVDPIEEGEDVKADIIFVYCKDHVR
SLKKEGFL
>gnl|CDD|239904 cd04457, S1_S28E, S1_S28E: S28E, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. S28E protein is a component of the 30S ribosomal subunit. S28E is highly conserved among archaea and eukaryotes. S28E may control precursor RNA splicing and turnover in mRNA maturation process but its function in the ribosome is largely unknown. The structure contains an OB-fold found in many oligosaccharide and nucleic acid binding proteins. This implies that S28E might be involved in protein synthesis
KLAEVIKVLGRTGSRGEVTQVRVEFMDDKGRSIIRNVKGPVREGDILMLLETEREARRLR
>gnl|CDD|239905 cd04458, CSP_CDS, Cold-Shock Protein (CSP) contains an S1-like cold-shock domain (CSD) that is found in eukaryotes, prokaryotes, and archaea. CSP's include the major cold-shock proteins CspA and CspB in bacteria and the eukaryotic gene regulatory factor Y-box protein. CSP expression is up-regulated by an abrupt drop in growth temperature. CSP's are also expressed under normal condition at lower level. The function of cold-shock proteins is not fully understood. They preferentially bind poly-pyrimidine region of single-stranded RNA and DNA. CSP's are thought to bind mRNA and regulate ribosomal translation, mRNA degradation, and the rate of transcription termination. The human Y-box protein, which contains a CSD, regulates transcription and translation of genes that contain the Y-box sequence in their promoters. This specific ssDNA-binding properties of CSD are required for the binding of Y-box protein to the promoter's Y-box sequence, thereby regulating transcription
VTGTVKWFDDEKGFGFITPDDGGEDVFVHISALEGDGFRSLEEGDRVEFELEEGDKGPQAVNVRL
>gnl|CDD|239906 cd04459, Rho_CSD, Rho_CSD: Rho protein cold-shock domain (CSD). Rho protein is a transcription termination factor in most bacteria. In bacteria, there are two distinct mechanisms for mRNA transcription termination. In intrinsic termination, RNA polymerase and nascent mRNA are released from DNA template by an mRNA stem loop structure, which resembles the transcription termination mechanism used by eukaryotic pol III. The second mechanism is mediated by Rho factor. Rho factor terminates transcription by using energy from ATP hydrolysis to forcibly dissociate the transcripts from RNA polymerase. Rho protein contains an N-terminal S1-like domain, which binds single-stranded RNA. Rho has a C-terminal ATPase domain which hydrolyzes ATP to provide energy to strip RNA polymerase and mRNA from the DNA template. Rho functions as a homohexamer
GSGVLEILPDGFGFLRSSGYNYLPGPDDIYVSPSQIRRFNLRTGDTVVGQIRPPKEGERYFALLKVEA
>gnl|CDD|239907 cd04460, S1_RpoE, S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. RpoE is subunit E of archaeal RNA polymerase. Archaeal cells contain a single RNA polymerase made up of 12 subunits, which are homologous to the 12 subunits (RPB1-12) of eukaryotic RNA polymerase II. RpoE is homologous to Rpa43 of eukaryotic RNA polymerase I, RPB7 of eukaryotic RNA polymerase II, and Rpc25 of eukaryotic RNA polymerase III. RpoE is composed of two domains, the N-terminal RNP (ribonucleoprotein) domain and the C-terminal S1 domain. This S1 domain binds ssRNA and ssDNA. This family is classified based on the C-terminal S1 domain. The function of RpoE is not fully understood. In eukaryotes, RPB7 and RPB4 form a heterodimer that reversibly associates with the RNA polymerase II core
EVVEGEVVEVVDFGAFVRIGPVDGLLHISQIMDDYISYDPKNKRLIGEETKRVLKVGDVVRARIVAVSLK
ERRPRESKIGLTMRQPGLGKLEWIEEEKA
>gnl|CDD|239908 cd04461, S1_Rrp5_repeat_hs8_sc7, S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 repeat 7 (sc7)-like domains. Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in S. cerevisiae Rrp5 and 14 S1 repeats in H. sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 8 and S. cerevisiae S1 repeat 7. Rrp5 is found in eukaryotes but not in prokaryotes or archaea
KEGTLPTNFSDLKPGMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVT
SVDEEKQRFLLSL
>gnl|CDD|239909 cd04462, S1_RNAPII_Rpb7, S1_RNAPII_Rpb7: Eukaryotic RNA polymerase II (RNAPII) Rpb7 subunit C-terminal S1 domain. RNAPII is composed of 12 subunits (Rpb1-12). Rpb4 and Rpb7 form a heterodimer that associate with the RNAPII core. Rpb7 is a homolog of the Rpc25 of RNA polymerase III, RpoE of the archaeal RNA polymerase, and Rpa43 of eukaryotic RNA polymerase I. Rpb7 has two domains, an N-terminal ribonucleoprotein (RNP) domain and a C-terminal S1 domain, both of which bind single-stranded RNA. It is possible that the S1 domain interacts with the nascent RNA transcript, assisted by the RNP domain. In yeast, Rpb4/Rpb7 is necessary for promoter-directed transcription initiation. They also play a role in regulating transcription-coupled repair in the Rad26-dependent pathway, in efficient mRNA export, and in transcription termination
KGEVVDAIVTSVNKTGFFAEVGPLSIFISRHLIPSDMEFDPNASPPCFTSNEDIVIKKDTEVRLKIIGTR
VDATDIFAIGTIKDDYLG
>gnl|CDD|239910 cd04463, S1_EF_like, S1_EF_like: EF-like, S1-like RNA-binding domain. The EF-like superfamily contains the bacterial translation elongation factor P and its archeal and eukaryotic homologs, aIF5A and eIF5A. All proteins in this superfamily contain an S1 domain, which binds RNA or single-stranded DNA and often interacts with the ribosome. Hex-1, the SI-like domain of which is also found in this group, is structurally homologous to eIF5A and might have evolved from an ancestral eIF5A through gene duplication
RELQVLDIQGSKPVTMDLETYEVVQVPPPVDQSFESFEPGEVVLVDTRTGQYVGV
>gnl|CDD|239911 cd04465, S1_RPS1_repeat_ec2_hs2, S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain.While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 2 of the Escherichia coli and Homo sapiens RPS1 (ec2 and hs2, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog
GEIVEGKVTEKVKGGLIVDIEGVRAFLPASQVDLRPVEDLDEYVGKELKFKIIEIDRERNNIVLSRR
>gnl|CDD|239912 cd04466, S1_YloQ_GTPase, S1_YloQ_GTPase: YloQ GTase family (also known as YjeQ and CpgA), S1-like RNA-binding domain. Proteins in the YloQ GTase family bind the ribosome and have GTPase activity. The precise role of this family is unknown. The protein structure is composed of three domains: an N-terminal S1 domain, a central GTPase domain, and a C-terminal zinc finger domain. This N-terminal S1 domain binds ssRNA. The central GTPase domain contains nucleotide-binding signature motifs: G1 (walker A), G3 (walker B) and G4 motifs. Experiments show that the bacterial YloQ and YjeQ proteins have low intrinsic GTPase activity. The C-terminal zinc-finger domain has structural similarity to a portion of the DNA-repair protein Rad51. This suggests a possible role for this GTPase as a regulator of translation, perhaps as a translation initiation factor. This family is classified based on the N-terminal S1 domain
MEGLIIKAIGGFYYVETEDGKIYECRLRGKFRKDKNPPAVGDRVEFEPEDDGEGVIEEILPRKNLLIR
>gnl|CDD|239913 cd04467, S1_aIF5A, S1_aIF5A: Archaeal translation Initiation Factor 5A (aIF5A), S1-like RNA-binding domain. aIF5A is a homolog of eukaryotic eIF5A. IF5A is the only protein known to have the unusual amino acid hypusine. Hypusine is a post-translationally modified lysine and is essential for IF5A function. In yeast, eIF5A interacts with components of the 80S ribosome and translation elongation factors 2 (eEF2) in a hypusine-dependent manner. This C-terminal S1 domain resembles the cold-shock domain which binds RNA. Moreover, IF5A prefers binding to the actively translating ribosome. This evidence suggests that IF5A plays a role in translation elongation instead of translation initiation as previously proposed
IERKTGQVLSIMGDVVQLMDLETYETFEVPIPEEIKDKLEPGKEVEYWESMGKRKID
>gnl|CDD|239914 cd04468, S1_eIF5A, S1_eIF5A: Eukaryotic translation Initiation Factor 5A (eIF5A), S1-like RNA-binding domain. eIF5A is an evolutionarily conserved protein found in eukaryotes. eIF5A is the only protein known to have the unusual amino acid hypusine. Hypusine is essential for eIF5A function and is a post-translationally modified lysine. eIF5A interacts with components of the 80S ribosome and translation elongation factors 2 (eEF2) in a hypusine-dependent manner. This C-terminal S1 domain resembles the oligonucleotides-binding fold (OB fold) which binds RNA. Moreover, eIF5A prefers binding to the actively translating ribosome. This evidence suggests that eIF5A plays a role in translation elongation instead of translation initiation as previously proposed
VKRTEYQLIDIDDGFLSLMDDDGETREDLKLPEGELGKEIREKFDEGKDVLVTVLSAMGEEQAVAVKEA
>gnl|CDD|239915 cd04469, S1_Hex1, S1_Hex1: Hex1, S1-like RNA-binding domain. Hex1 protein is the major component of the Woronin body in filamentous fungi. The Woronin body is a dense vesicle and plays a vital role in filamentous fungi cell integrity. When cell damage occurs, Woronin bodies seal the septal pore to prevent further cytoplasmic bleeding. Hex1 protein self-assembles to form the solid core of the Woronin body vesicle. The Hex1 sequence and structure are similar to eukaryotic initiation factor 5A (eIF5A), suggesting they share a common ancestor during evolution. All members of the EF superfamily to which Hex1 belongs, contain an S1 domain, which has been shown to bind RNA or single-stranded DNA and often interacts with the ribosome
VFKQYRVLDIQDGSIVAMTETGDVKQGLPVIDQSNLWTRLKTAFESGRGSVRVLVVNDGGRELVVDMKVV
HGSRL
>gnl|CDD|239916 cd04470, S1_EF-P_repeat_1, S1_EF-P_repeat_1: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. EF-P stimulates the peptidyltransferase activity in the prokaryotic 70S ribosome. EF-P enhances the synthesis of certain dipeptides with N-formylmethionyl-tRNA and puromycine in vitro. EF-P binds to both the 30S and 50S ribosomal subunits. EF-P binds near the streptomycine binding site of the 16S rRNA in the 30S subunit. EF-P interacts with domains 2 and 5 of the 23S rRNA. The L16 ribosomal protein of the 50S or its N-terminal fragment are required for EF-P mediated peptide bond synthesis, whereas L11, L15, and L7/L12 are not required in this reaction, suggesting that EF-P may function at a different ribosomal site than most other translation factors. EF-P is essential for cell viability and is required for protein synthesis. EF-P is mainly present in bacteria. The EF-P homologs in archaea and eukaryotes are the initiation factors aIF5A and eIF5A, respectively. EF-P has 3 domains (domains I, II, and III). Domains II and III are S1-like domains. This CD includes domain II (the first S1 domain of EF_P). Domains II and III have structural homology to the eIF5A domain C, suggesting that domains II and III evolved by duplication
EEREMQYLYKDGDNYVFMDTETYEQIELPKEALGDAAKFLKEGMEVIVLFYNGEPIGVELP
>gnl|CDD|239917 cd04471, S1_RNase_R, S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, which is a homolog of RNase II. RNase R degrades RNA with secondary structure having a 3' overhang of at least 7 nucleotides. RNase R and PNPase play an important role in the degradation of RNA with extensive secondary structure, such as rRNA, tRNA, and certain mRNA which contains repetitive extragenic palindromic sequences. The C-terminal S1 domain binds ssRNA
VGEEFDGVISGVTSFGLFVELDNLTVEGLVHVSTLGDDYYEFDEENHALVGERTGKVFRLGDKVKVRVVR
VDLDRRKIDFELV
>gnl|CDD|239918 cd04472, S1_PNPase, S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a polyribonucleotide nucleotidyl transferase that degrades mRNA. It is a trimeric multidomain protein. The C-terminus contains the S1 domain which binds ssRNA. This family is classified based on the S1 domain. PNPase nonspecifically removes the 3' nucleotides from mRNA, but is stalled by double-stranded RNA structures such as a stem-loop. Evidence shows that a minimum of 7-10 unpaired nucleotides at the 3' end, is required for PNPase degradation. It is suggested that PNPase also dephosphorylates the RNA 5' end. This additional activity may regulate the 5'-dependent activity of RNaseE in vivo
GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELSDERVEKVEDVLKVGDEVKVKVIEVDDRGRISLSR
>gnl|CDD|239919 cd04473, S1_RecJ_like, S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of this family is not fully understood. In Escherichia coli, RecJ degrades single-stranded DNA in the 5'-3' direction and participates in homologous recombination and mismatch repair
IVYVLDPACTMEDLEVGKLYKGKVNGVAKYGVFVDLNDHVRGLIHRSNLLRDYEVGDEVIVQVTDIPENG
NIDLIPV
>gnl|CDD|239920 cd04474, RPA1_DBD_A, RPA1_DBD_A: A subfamily of OB folds corresponding to the second OB fold, the ssDNA-binding domain (DBD)-A, of human RPA1 (also called RPA70). RPA1 is the large subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). In addition to DBD-A, RPA1 contains three other OB folds: DBD-B, DBD-C, and RPA1N. The major DNA binding activity of human RPA (hRPA) and Saccharomyces cerevisiae RPA (ScRPA) is associated with DBD-A and DBD-B of RPA1. RPA1 DBD-C is involved in trimerization. The ssDNA-binding mechanism is believed to be multistep and to involve conformational change. Although ScRPA and the hRPA have similar ssDNA-binding properties, they differ functionally. Antibodies to hRPA do not cross-react with ScRPA, and null mutations in the ScRPA subunits are not complemented by corresponding human genes. Also, ScRPA cannot support Simian virus 40 (SV40) DNA replication in vitro, whereas human RPA can
PISSLNPYQNKWTIKARVTNKSDIRTWSNARGEGKLFSFDLLDEDGGEIRATFFNDAVDKFYDLLEVGKV
YYISKGSVKVANKKFNTLKNDYEITFNRDTSIIE
>gnl|CDD|239921 cd04475, RPA1_DBD_B, RPA1_DBD_B: A subfamily of OB folds corresponding to the third OB fold, the ssDNA-binding domain (DBD)-B, of human RPA1 (also called RPA70). RPA1 is the large subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). In addition to DBD-B, RPA1 contains three other OB folds: DBD-A, DBD-C, and RPA1N. The major DNA binding activity of human RPA (hRPA) and Saccharomyces cerevisiae RPA (ScRPA) is associated with RPA1 DBD-A and DBD-B. RPA1 DBD-C is involved in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. Although ScRPA and the hRPA have similar ssDNA-binding properties, they differ functionally. Antibodies to hRPA do not cross-react with ScRPA, and null mutations in the ScRPA subunits are not complemented by corresponding human genes. Also, ScRPA cannot support Simian virus 40 (SV40) DNA replication in vitro, whereas human RPA can
IVDVIGVVKSVGPVTTITTKSTGRELDKREITLVDESGHSVELTLWGEQAELFDGSENPVIAIKGVKVSE
FNGKSLSTGSSSTIIINPDIPEAHKLRGWYD
>gnl|CDD|239922 cd04476, RPA1_DBD_C, RPA1_DBD_C: A subfamily of OB folds corresponding to the C-terminal OB fold, the ssDNA-binding domain (DBD)-C, of human RPA1 (also called RPA70). RPA1 is the large subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). In addition to DBD-C, RPA1 contains three other OB folds: DBD-A, DBD-B, and RPA1N. The major DNA binding activity of RPA is associated with RPA1 DBD-A and DBD-B. RPA1 DBD-C is involved in DNA binding and trimerization. It contains two structural insertions not found to date in other OB-folds: a zinc ribbon and a three-helix bundle. RPA1 DBD-C also contains a Cys4-type zinc-binding motif, which plays a role in the ssDNA binding function of this domain. It appears that zinc itself may not be required for ssDNA binding
IAEIKEENLGEGEKPDYFTVKATIVFIKPDNWWYPACPGCNKKVVEEGNGTYRCEKCNKSVPNPEYRYIL
SLNVADHTGEAWLTLFDEVAEQIFGKSAEELLELKEEDPDAFPDAIQDLVGKTFLFRVSVKEETYNDEGR
IRYTVVKVAPVDYKKESKRLIQSIEK
>gnl|CDD|239923 cd04477, RPA1N, RPA1N: A subfamily of OB folds corresponding to the N-terminal OB-fold domain of human RPA1 (also called RPA70). RPA1 is the large subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). RPA1N is known to specifically interact with the p53 tumor suppressor, DNA polymerase alpha, and transcription factors. In addition to RPA1N, RPA1 contains three other OB folds: ssDNA-binding domain (DBD)-A, DBD-B, and DBD-C
GALAAIFNGEDRSNVIKPVLQVLNIKKIDSSNGSSERYRILLSDGVYYVQAMLATQLNPLVESGQLQRGS
IIRLKRFICNVIKGKRILIILDLEVVQ
>gnl|CDD|239924 cd04478, RPA2_DBD_D, RPA2_DBD_D: A subfamily of OB folds corresponding to the OB fold of the central ssDNA-binding domain (DBD)-D of human RPA2 (also called RPA32). RPA2 is a subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). The major DNA binding activity of RPA is associated with RPA1 DBD-A and DBD-B; RPA2 DBD-D is a weak ssDNA-binding domain. RPA2 DBD-D is also involved in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. N-terminal to human RPA2 DBD-D is a domain containing all the known phosphorylation sites of RPA. Human RPA2 is phosphorylated in a cell cycle dependent manner in response to DNA damage. RPA2 interacts physically with menin; the gene encoding menin is a tumor suppressor gene disrupted in multiple endocrine neoplasia type I. This subfamily also includes RPA2 from Cryptosporidium parvum (CpRPA2). CpRPA2 is an SSB, which can be phosphorylated by DNA-PK in vitro
QVTLVGVVRNVEEQSTNITYTIDDGTGTIEVRQWLDDDNDDSSEVEPIEEGTYVRVFGNLKSFQGKKSIM
AFSIRPVTDFNEVTYHLLEVIYVHL
>gnl|CDD|239925 cd04479, RPA3, RPA3: A subfamily of OB folds similar to human RPA3 (also called RPA14). RPA3 is the smallest subunit of Replication protein A (RPA). RPA is a nuclear ssDNA binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). RPA3 is believed to have a structural role in assembly of the RPA heterotrimer
PTPRINGAMLSQFVGKTVRIVGKVEKVDGDSLTLISSDGVNVTVELNRPLDLPISGYVEVIGKVSPDLTI
RVLSYIDFGDDFDMDLYNELVKLSHKFKNLF
>gnl|CDD|239926 cd04480, RPA1_DBD_A_like, RPA1_DBD_A_like: A subgroup of uncharacterized plant OB folds with similarity to the second OB fold, the ssDNA-binding domain (DBD)-A, of human RPA1 (also called RPA70). RPA1 is the large subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). In addition to DBD-A, RPA1 contains three other OB folds: DBD-B, DBD-C, and RPA1N. The major DNA binding activity of RPA is associated with DBD-A and DBD-B of RPA1. RPA1 DBD-C is involved in trimerization. The ssDNA-binding mechanism is believed to be multistep and to involve conformational change
KICVRVLRLWDVYNNASGESLEMVLVDEKGNRIHATIPKRLAAKFRPLLKEGKWYTISNFEVAPNTGSYR
PTDHPYKIKFMSDTVV
>gnl|CDD|239927 cd04481, RPA1_DBD_B_like, RPA1_DBD_B_like: A subgroup of uncharacterized, plant OB folds with similarity to the third OB fold, the ssDNA-binding domain (DBD)-B, of human RPA1 (also called RPA70). RPA1 is the large subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). In addition to DBD-B, RPA1 contains three other OB folds: DBD-A, DBD-C, and RPA1N. The major DNA binding activity of RPA is associated with RPA1 DBD-A and DBD-B. RPA1 DBD-C is involved in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change
DVIGVIVDVGPLEELPPVNKPSRKLDFEIRDLSDERLKCTLWGEYAEEFDAKFQSAGNGEPVVAVLRFWK
IKEYKGPKSLSNSFGASKVYINPDIPEVPEIKMSLK
>gnl|CDD|239928 cd04482, RPA2_OBF_like, RPA2_OBF_like: A subgroup of uncharacterized archaeal OB folds with similarity to the OB fold of the central ssDNA-binding domain (DBD)-D of human RPA2 (also called RPA32). RPA2 is a subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). The major DNA binding activity of RPA is associated with RPA1 DBD-A and DBD-B; RPA2 DBD-D is a weak ssDNA-binding domain. RPA2 DBD-D is also involved in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. N-terminal to human RPA2 DBD-D is a domain containing all the known phosphorylation sites of RPA. Human RPA2 is phosphorylated in a cell cycle dependent manner in response to DNA damage
YRVTGKVVEEPRTIEGGHVFFKISDGTGEIDCAAYEPTKEFRDVVRLLIPGDEVTVYGSVRPGTTLNLEK
LRVIRLARLYERENPVCPKCG
>gnl|CDD|239929 cd04483, hOBFC1_like, hOBFC1_like: A subfamily of OB folds similar to that found in human OB fold containing protein 1 (hOBFC1). Members of this group belong to the Replication protein A subunit 2 (RPA2) family of OB folds. RPA is a nuclear ssDNA binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). The OB fold domain of RPA2 has dual roles in ssDNA binding and trimerization
DILGTVVSRRERETFYSFGVDDGTGVVNCVCWKNLSYAEVSSRSDAARILKSALMALKQAKVLEIGDLLR
VRGSIRTYRGEREINASVVYKV
>gnl|CDD|239930 cd04484, polC_OBF, polC_OBF: A subfamily of OB folds corresponding to the N-terminal OB-fold nucleic acid binding domain of Bacillus subtilis type C replicative DNA polymerase III alpha subunit (polC). Replication in B. subtilis and Staphylococcus aureus requires two different polymerases, polC and DnaE. The holoenzyme is thought to include the two different polymerases. At the B. subtilis replication fork, polC appears to be involved in leading strand synthesis and DnaE in lagging strand synthesis
NVVVEGEVFDLEIRELKSGRKILTFKVTDYTSSITVKKFLRKDEKDKEELKSKGDWVRVRGKVQYDTFSK
ELVLMINDIEEI
>gnl|CDD|239931 cd04485, DnaE_OBF, DnaE_OBF: A subfamily of OB folds corresponding to the C-terminal OB-fold nucleic acid binding domain of Thermus aquaticus and Escherichia coli type C replicative DNA polymerase III alpha subunit (DnaE). The DNA polymerase holoenzyme of E. coli contains two copies of this replicative polymerase, each of which copies a different DNA strand. This group also contains Bacillus subtilis DnaE. Replication in B. subtilis and Staphylococcus aureus requires two different type C polymerases, polC and DnaE, both of which are thought to be included in the DNA polymerase holoenzyme. At the B. subtilis replication fork, polC appears to be involved in leading strand synthesis and DnaE in lagging strand synthesis
TVAGLVTSVRRRRTKKGKRMAFVTLEDLTGSIEVVVFPETYEKYRDLLKEDALLLVEGKVERRDGGLRLI
AERIEDLEDARERL
>gnl|CDD|239932 cd04486, YhcR_OBF_like, YhcR_OBF_like: A subfamily of OB-fold domains similar to the OB folds of Bacillus subtilis YhcR. YhcR is a sugar-nonspecific nuclease, which is active in the presence of Ca2+ and Mn2+. It cleaves RNA endonucleolytically, producing 3'-monophosphate nucleosides. YhcR appears to be the major Ca2+ activated nuclease of B. subtilis. YhcR may be localized in the cell wall
TVEGVVTAVFSGGGLGGFYIQDEDGDGDPATSEGIFVYTGSGADVAVGDLVRVTGTVTEYYGLTQLTAVS
AIEVLGSG
>gnl|CDD|239933 cd04487, RecJ_OBF2_like, RecJ_OBF2_like: A subfamily of OB folds corresponding to the second OB fold (OBF2) of archaeal-specific proteins with similarity to eubacterial RecJ. RecJ is an ssDNA-specific exonuclease. Although the overall sequence similarity of these proteins to eubacterial RecJ proteins is marginal, they appear to carry motifs, which have been shown to be essential for nuclease function in Escherichia coli RecJ. In addition to this OB fold, most proteins in this subfamily contain: i) an N-terminal OB fold belonging to a different domain family (the ribosomal S1-like RNA-binding family); and ii) a domain, C-terminal to OBF2, characteristic of DHH family proteins. DHH family proteins include E. coli RecJ, and are predicted to have a phosphoesterase function
VHIEGEVVQIKQTSGPTIFTLRDETGTVWAAAFEEAGVRAYPEVEVGDIVRVTGEVEPRDGQLQIEVESL
EVL
>gnl|CDD|239934 cd04488, RecG_wedge_OBF, RecG_wedge_OBF: A subfamily of OB folds corresponding to the OB fold found in the N-terminal (wedge) domain of Escherichia coli RecG. RecG is a branched-DNA-specific helicase, which catalyzes the interconversion of a DNA replication fork to a four-stranded (Holliday) junction in vivo and in vitro. This interconversion provides a route to repair stalled forks. The RecG monomer contains three domains. The N-terminal domain is named for its wedge structure, and may provide the specificity of RecG for binding branched-DNA structures. During the reversal of fork to Holliday junction, the wedge domain is fixed at the junction of the fork where the leading and lagging strand duplex arms meet, and is thought to promote the unwinding of the nascent leading and lagging strands. In order to form the Holliday junction, these nascent strands would be annealed, and the parental strands reannealed. The wedge domain may also be a processivity factor of RecG on these branched chain substrates
TVEGTVVSVEVVPRRGRRRLKVTLSDGTGTLTLVFFNFQPYLKKQLPPGTRVRVSGKVKRFRGGLQIVHP
EYELL
>gnl|CDD|239935 cd04489, ExoVII_LU_OBF, ExoVII_LU_OBF: A subfamily of OB folds corresponding to the N-terminal OB-fold domain of Escherichia coli exodeoxyribonuclease VII (ExoVII) large subunit. E. coli ExoVII is composed of two non-identical subunits. E. coli ExoVII is a single-strand-specific exonuclease which degrades ssDNA from both 3-prime and 5-prime ends. ExoVII plays a role in methyl-directed mismatch repair in vivo. ExoVII may also guard the genome from mutagenesis by removing excess ssDNA, since the build up of ssDNA would lead to SOS induction and PolIV-dependent mutagenesis
RVWVEGEISNLKRPSSGHLYFTLKDEDASIRCVMWRSNARRLGFPLEEGMEVLVRGKVSFYEPRGGYQLI
VEEIEPAG
>gnl|CDD|239936 cd04490, PolII_SU_OBF, PolII_SU_OBF: A subfamily of OB folds corresponding to the OB fold found in Pyrococcus abyssi DNA polymerase II (PolII) small subunit. PolII is a family D DNA polymerase, having a 3-prime to 5-prime exonuclease activity. P. abyssi PolII is heterodimeric. The large subunit appears to be the polymerase, and the small subunit may be the exonuclease. The small subunit contains a calcineurin-like phosphatase superfamily domain C-terminal to this OB-fold domain
EVSIIGMVNDVRSTKNGHRIVELEDTTGRITVLLTKDKEELFEEAEDILPDEVIGVSGTVSKDGGLIFAD
EIFRPDVPR
>gnl|CDD|239937 cd04491, SoSSB_OBF, SoSSB_OBF: A subfamily of OB folds similar to the OB fold of the crenarchaeote Sulfolobus solfataricus single-stranded (ss) DNA-binding protein (SSoSSB). SSoSSB has a single OB fold, and it physically and functionally interacts with RNA polymerase. In vitro, SSoSSB can substitute for the basal transcription factor TBP, stimulating transcription from promoters under conditions in which TBP is limiting, and supporting transcription when TBP is absent. SSoSSB selectively melts the duplex DNA of promoter sequences. It also relieves transcriptional repression by the chromatin Alba. In addition, SSoSSB activates reverse gyrase activity, which involves DNA binding, DNA cleavage, strand passage and ligation. SSoSSB stimulates all these steps in the presence of the chromatin protein, Sul7d. SSoSSB antagonizes the inhibitory effect of Sul7d on reverse gyrase supercoiling activity. It also physically and functionally interacts with Mini-chromosome Maintenance (MCM), stimulating the DNA helicase activity of MCM
SVEGKVLSISEPREFTRDGSEGKVQSGLVGDETGTIRFTLWDEKAADDLEPGDVVRIENAYVREFNGRLE
LSVGKNSEIEKL
>gnl|CDD|239938 cd04492, YhaM_OBF_like, YhaM_OBF_like: A subfamily of OB folds similar to that found in Bacillus subtilis YhaM and Staphylococcus aureus cmp-binding factor-1 (SaCBF1). Both these proteins are 3'-to-5'exoribonucleases. YhaM requires Mn2+ or Co2+ for activity and is inactive in the presence of Mg2+. YhaM also has a Mn2+ dependent 3'-to-5'single-stranded DNA exonuclease activity. SaCBF is also a double-stranded DNA binding protein, binding specifically to cmp, the replication enhancer found in S. aureus plasmid pT181. Proteins in this group combine an N-terminal OB fold with a C-terminal HD domain. The HD domain is found in metal-dependent phosphohydrolases
DGFFLIKSKELRTAKNGKPYLALTLQDKTGEIEAKLWDASEEDEEKFKPGDIVHVKGRVEEYRGRLQLKI
QRIRLVTEEDGVD
>gnl|CDD|239939 cd04493, BRCA2DBD_OB1, BRCA2DBD_OB1: A subfamily of OB folds corresponding to the first OB fold (OB1) of the 800-amino acid C-terminal ssDNA binding domain (DBD) of BRCA2 (breast cancer susceptibility gene 2) protein, called BRCA2DBD. BRCA2 participates in homologous recombination-mediated repair of double-strand DNA breaks. It stimulates the displacement of Replication protein A (RPA), the most abundant eukaryotic ssDNA binding protein. It also facilitates filament formation. Mutations that map throughout the BRCA2 protein are associated with breast cancer susceptibility. BRCA2 is a large nuclear protein and its most conserved region is the C-terminal BRCA2DBD. BRCA2DBD binds ssDNA in vitro, and is composed of five structural domains, three of which are OB folds (OB1, OB2, and OB3). BRCA2DBD OB2 and OB3 are arranged in tandem, and their mode of binding can be considered qualitatively similar to two OB folds of RPA1, DBD-A and DBD-B (the major DBDs of RPA). BRCA2DBD OB1 binds DNA weakly
ASRLMVLCVSGINSEERLSPHMPIIELTDGWYSIRAQLDPPLTNLVRKGKLRVGQKLRICGAELLGSANP
CSPLEAPDSVRLKINANSTRRARWDARLGF
>gnl|CDD|239940 cd04494, BRCA2DBD_OB2, BRCA2DBD_OB2: A subfamily of OB folds corresponding to the second OB fold (OB2) of the 800-amino acid C-terminal ssDNA binding domain (DBD) of BRCA2 (breast cancer susceptibility gene 2) protein, called BRCA2DBD. BRCA2 participates in homologous recombination-mediated repair of double-strand DNA breaks. It stimulates the displacement of Replication protein A (RPA), the most abundant eukaryotic ssDNA binding protein. It also facilitates filament formation. Mutations that map throughout the BRCA2 protein are associated with breast cancer susceptibility. BRCA2 is a large nuclear protein and its most conserved region is the C-terminal BRCA2DBD. BRCA2DBD binds ssDNA in vitro, and is composed of five structural domains, three of which are OB folds (OB1, OB2, and OB3). BRCA2DBD OB2 and OB3 are arranged in tandem, and their mode of binding can be considered qualitatively similar to two OB folds of RPA1, DBD-A and DBD-B (the major DBDs of RPA)
PLSSLYDSGGLVGCVDVIILRVYPLQWVEKTSEGGSVFRSERAEEREARLHAQRQQKKLEALFSKIQEEF
EKEEEDNNQRRPRSRTRTRQNVTDLQDGAELYEALEAAADPSFLEAELSEEQLEALSNYQQLQNEKKQAR
LQEEFRKAVEEALKEEGLSKRDVTPVWKLRVTDYRSKPEKSGLLSIWRPTEDLRSLLTEGKRYRIYGLAT
SNSKKRSGNEEVQLTATKKTRYQPLPVSQRELFQPFQPRKA
>gnl|CDD|239941 cd04495, BRCA2DBD_OB3, BRCA2DBD_OB3: A subfamily of OB folds corresponding to the third OB fold (OB3) of the 800-amino acid C-terminal ssDNA binding domain (DBD) of BRCA2 (breast cancer susceptibility gene 2) protein, called BRCA2DBD. BRCA2 participates in homologous recombination-mediated repair of double-strand DNA breaks. It stimulates the displacement of Replication protein A (RPA), the most abundant eukaryotic ssDNA binding protein. It also facilitates filament formation. Mutations that map throughout the BRCA2 protein are associated with breast cancer susceptibility. BRCA2 is a large nuclear protein and its most conserved region is the C-terminal BRCA2DBD. BRCA2DBD binds ssDNA in vitro, and is composed of five structural domains, three of which are OB folds (OB1, OB2, and OB3). BRCA2DBD OB2 and OB3 are arranged in tandem, and their mode of binding can be considered qualitatively similar to two OB folds of RPA1, DBD-A and DBD-B (the major DBDs of RPA)
DTVGVVISVGKPIEGKFPAVYLADECLNLLCVKFWSSLEQYAYEDVVKRRVLLAASNLQWRTESTSGVPT
LFAGEYSTFSANPKESHLQEEFNNLKHLIE
>gnl|CDD|239942 cd04496, SSB_OBF, SSB_OBF: A subfamily of OB folds similar to the OB fold of ssDNA-binding protein (SSB). SSBs bind with high affinity to ssDNA. They bind to and protect ssDNA intermediates during DNA metabolic pathways. All bacterial and eukaryotic SSBs studied to date oligomerize to bring together four OB folds in their active state. The majority (e.g. Escherichia coli SSB) have a single OB fold per monomer, which oligomerize to form a homotetramer. However, Deinococcus and Thermus SSB proteins have two OB folds per monomer, which oligomerize to form a homodimer. Mycobacterium tuberculosis SSB varies in quaternary structure from E. coli SSB. It forms a dimer of dimers having a unique dimer interface, which lends the protein greater stability. Included in this group are OB folds similar to Escherichia coli PriB. E.coli PriB is homodimeric with each monomer having a single OB fold. It does not appear to form higher order oligomers. PriB is an essential protein for the replication restart at forks that have stalled at sites of DNA damage. It also plays a role in the assembly of primosome during replication initiation at the bacteriophage phiX174 origin. PriB physically interacts with SSB and binds ssDNA with high affinity
VILIGRLGKDPELRYTPSGTPVARFSLAVNRRRKDRDEEEEETDWIRVVAFGKLAENAAKYLKKGDLVYV
EGRLRTRSWEDKDGQKRYGTEVVADRIEFL
>gnl|CDD|239943 cd04497, hPOT1_OB1_like, hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection of telomeres 1 protein (hPOT1), the single OB fold of the N-terminal domain of Schizosaccharomyces pombe POT1 (SpPOT1), and the first OB fold of the N-terminal domain of the alpha subunit (OB1Nalpha) of Oxytricha nova telomere end binding protein (OnTEBP). POT1 proteins recognize single-stranded (ss) 3-prime ends of the telomere. A 3-prime ss overhang is conserved in ciliated protozoa, yeast, and mammals. SpPOT1 is essential for telomere maintenance. It binds specifically to the ss G-rich telomeric sequence (GGTTAC) of S. pombe. hPOT1 binds specifically to ss telomeric DNA repeats ending with the sequence GGTTAG. Deletion of the S. pombe pot1+ gene results in a rapid loss of telomere sequences, chromosome mis-segregation and chromosome circularization. hPOT1 is implicated in telomere length regulation. The hPOT1 monomer consists of two closely connected OB folds (OB1-OB2) which cooperate to bind telomeric ssDNA. OB1 makes more extensive contact with the ssDNA than OB2. OB2 protects the 3' end of the ssDNA. A second OB fold has not been predicted in S. pombe POT1. OnTEBP binds the extreme 3-prime end of telomeric DNA. It is heterodimeric and contains four OB folds - three in the alpha subunit (two in the N-terminal domain and one in the C-terminal domain) and one in the beta subunit. OB1Nalpha, together with the second OB fold of the N-terminal domain of OnTEBP alpha subunit and the beta subunit OB fold, forms a deep cleft that binds ssDNA
YKYTPLSSALKESGGSVNVIGVVVDAGPPVRSKGTDYCCTLTITDPSLANSDGLTVKLFRPNEESLPIVK
VGDIILLRRVKIQSYNGKPQGISNDRGSSWAVFRGDDGVVPIPQQSSKPVEFGPEEEPSVEELRKWAS
>gnl|CDD|239944 cd04498, hPOT1_OB2, hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of telomeres 1 protein (hPOT1). POT1 proteins bind to the single-stranded (ss) 3-prime ends of the telomere. hPOT1 binds specifically to ss telomeric DNA repeats ending with the sequence GGTTAG. The hPOT1 monomer consists of two closely connected OB folds (OB1-OB2) which cooperate to bind telomeric ssDNA. OB1 makes more extensive contact with the ssDNA than OB2. OB2 protects the 3' end of the ssDNA. hPOT1 is implicated in telomere length regulation
YFDLLCQLLSVVETDSSSTLLKVWDGTKFPPPLRKVKVEDDVVLEGDRSLKHREEGGKQLTIDILVYDNH
VELAKSLKPGDFVRIYNVHAKSYSSKNEHDENDHLHFHLVHGGTEYGRGIRVL
>gnl|CDD|239945 cd04501, SGNH_hydrolase_like_4, Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid
MRVVCLGDSITYGYPVGPEASWVNLLAEFLGKEVINRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTN
DIIVNTSLEMIKDNIRSMVELAEANGIKVILASPLPVDDYPWKPQWLRPANKLKSLNRWLKDYARENGLL
FLDFYSPLLDERNVGLKPGLLTDGLHPSREGYRVMAPLAEKAL
>gnl|CDD|239946 cd04502, SGNH_hydrolase_like_7, Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid
GILFYGSSSIRLWDTLADDLAPLPVVNRGFGGSTLADCLHYFDRLVLPYQPRRVVLYAGDNDLASGRTPE
EVLRDFRELVNRIRAKLPDTPIAIISIKPSPARWALRPKIRRFNALLKELAETRPNLTYIDVASPMLDAD
GKPRAELFQEDGLHLNDAGYALWRKVIKPAL
>gnl|CDD|239947 cd04506, SGNH_hydrolase_YpmR_like, Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. This subfamily contains sequences similar to Bacillus YpmR
KIVALGDSLTEGVGDETGKGGYVGRLDKLIETKTVKKVTVQNFGVSGDRSDQLLKRLKTKKVQKELKKAD
VITITIGGNDLMQVLEKNFLSLDVEDFKKAEETYQNNLKKIFKEIRKLNPDAPIFLVGLYNPFYVYFPNI
TEINDIVNDWNEASQKLASQYKNAYFVPIFDLFSDGQNKYLLTSDHFHPNDKGYQLIADRVFKA
>gnl|CDD|410449 cd04508, Tudor_SF, Tudor domain superfamily. The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain
GDRVEAKWSDDGQWYPATVVAVNDDGKYTVLFDDGNEEEVSEDDIRP
>gnl|CDD|380490 cd04509, PBP1_ABC_transporter_GPCR_C-like, Family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems. This CD includes members of the family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems. The family C GPCR includes glutamate/glycine-gated ion channels such as the NMDA receptor, G-protein-coupled receptors, metabotropic glutamate, GABA-B, calcium sensing, pheromone receptors, and atrial natriuretic peptide-guanylate cyclase receptors. The glutamate receptors that form cation-selective ion channels, iGluR, can be classified into three different subgroups according to their binding-affinity for the agonists NMDA (N-methyl-D-asparate), AMPA (alpha-amino-3-dihydro-5-methyl-3-oxo-4-isoxazolepropionic acid), and kainate. L-glutamate is a major neurotransmitter in the brain of vertebrates and acts through either mGluRs or iGluRs. mGluRs subunits possess seven transmembrane segments and a large N-terminal extracellular domain. ABC-type leucine-isoleucine-valine binding protein (LIVBP) is a bacterial periplasmic binding protein that has homology with the amino-terminal domain of the glutamate-receptor ion channels (iGluRs). The extracellular regions of iGluRs are made of two PBP-like domains in tandem, a LIVBP-like domain that constitutes the N terminus (included in this model) followed by a domain related to lysine-arginine-ornithine-binding protein (LAOBP) that belongs to the type 2 periplasmic binding fold protein superfamily. The uncharacterized periplasmic components of various ABC-type transport systems are also included in this family
KVGVLFAVHGKGPSGVPCGDIVAQYGIQRFEAMEQALDDINADPNLLPNNTLGIVIYDDCCDPKQALEQS
NKFVNDLIQKDTSDVRCTNGEPPVFVKPEGIKGVIGHLCSSVTIPVSNILELFGIPQITYAATAPELSDD
RGYQLFLRVVPLDSDQAPAMADIVKEKVWQYVSIVHDEGQYGEGGARAFQDGLKKGGLCIAFSDGITAGE
KTKDFDRLVARLKKENNIRFVVYFGYHPEMGQILRAARRAGLVGKFQFMGSDGWANVSLSLNIAEESAEG
LITIKPKVWFVIAALYADAPGRYDIF
>gnl|CDD|467545 cd04511, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
PKIVVGCLPEWEGKVLLCRRAIEPRKGYWTLPAGFMELGETTEQGAARETREEAGARVEIGSLYAVYSLP
HISQVYIIFRARLLSPDFSPGPESLEVRLFDEEEIPWDELAFPSVRWALKHYF
>gnl|CDD|271334 cd04512, Ntn_Asparaginase_2_like, L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily. This family includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2 enzymes. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue. The family is circularly permuted relative to other NTN-hydrolase families
SLIVHGGAGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGE
VEMDAAIMDGKTLNAGAVAGVKGVKNPISLARAVMEKTPHVLLVGEGAERFAREHGHGTVGAVARDAQGN
LAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAE
AAIDYLRRRVGGEGGLIVVDPDGRLGAAHNTPGMAFAYI
>gnl|CDD|271335 cd04513, Glycosylasparaginase, Glycosylasparaginase and similar proteins. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoproteins. This enzyme is an amidase located inside lysosomes. Mutation of this gene in humans causes a genetic disorder known as aspartylglycosaminuria (AGU). The glycosylasparaginase precursor undergoes autoproteolysis through an N-O or N-S acyl rearrangement of the peptide bond, which leads to the cleavage of a peptide bond between an Asp and a Thr. This proteolysis step generates an exposed N-terminal catalytic threonine and activates the enzyme
LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMD
VGAVAALRRIKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFW
KNVVPDPSKSCSSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGL
YADNEVGAAAATGDGDIMMRFLPSYQAVELMRQGMSPQEACEDAIRRIAKKYPKDFEGAVVAVNKAGEYG
AACNGEGFSYAVRT
>gnl|CDD|271336 cd04514, Taspase1_like, Taspase 1 (threonine aspartase 1) and similar proteins. Taspase1 catalyzes the cleavage of the mix lineage leukemia (MLL) nuclear protein and transcription factor TFIIA. Taspase1 is a threonine aspartase, a member of the Ntn hydrolase superfamily and the type 2 asparaginase family. A threonine residue acts as the active site nucleophile in both endopeptidease and protease activities to cleave polypeptide substrates after an aspartate residue. The Taspase1 proenzyme undergoes autoproteolysis into alpha and beta subunits. The N-terminal residue of the beta subunit is a threonine which is the active catalytic residue. The active enzyme is a heterotetramer
FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDG
TVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKEQRKPLSLGRVPPMFLVGEGAREWAKSKGIITD
TVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLA
RRCAERLYHSTRREESDEDEILRSFIESDFMGHPGVKNSPSAGAIGVLAVKKTRSGVELYFAHNTDSFAL
ASMSSSDRKPKCVMSRLPGNGSIAQGGRKIRLR
>gnl|CDD|341214 cd04515, Alpha_kinase, Alpha kinase family. The alpha kinase family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional serine/threonine protein kinases. The family contains myosin heavy chain kinases, elongation factor-2 kinases, and bifunctional ion channel kinases. These kinases are implicated in a large variety of cellular processes such as protein translation, Mg2+/Ca2+ homeostasis, intracellular transport, cell migration, adhesion, and proliferation. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions
EIEVLRLISVTDLKWTTEETTVRVAKKKPFAQGAMREAFKAKDLDSKGKKYVAKRFKRIGDPEENLEDLF
DELRMQALAQYLAKEFNARAKSKNLIAPKINFVDPFVVKLGDRDDPGKVVFLVEPFLEGKFVKYNNNNGM
VNDEDLGETAQAFSHFTYERSGGQLLVTDLQGVGLVLTDPQIHTVDGGGFGLGNLGEEGIKRFFKTHKCN
EIC
>gnl|CDD|239952 cd04516, TBP_eukaryotes, eukaryotic TATA box binding protein (TBP): Present in archaea and eukaryotes, TBPs are transcription factors that recognize promoters and initiate transcription. TBP has been shown to be an essential component of three different transcription initiation complexes: SL1, TFIID and TFIIIB, directing transcription by RNA polymerases I, II and III, respectively. TBP binds directly to the TATA box promoter element, where it nucleates polymerase assembly, thus defining the transcription start site. TBP's binding in the minor groove induces a dramatic DNA bending while its own structure barely changes. The conserved core domain of TBP, which binds to the TATA box, has a bipartite structure, with intramolecular symmetry generating a saddle-shaped structure that sits astride the DNA
VPKIQNIVATVNLGCKLDLKKIALRARNAEYNPKRFAAVIMRIREPKTTALIFSSGKMVCTGAKSEDDSK
LAARKYARIIQKLGFPAKFTDFKIQNIVGSCDVKFPIRLEGLAHAHKQFSSYEPELFPGLIYRMVKPKIV
LLIFVSGKIVLTGAKSREEIYQAFENIYPILLQF
>gnl|CDD|239953 cd04517, TLF, TBP-like factors (TLF; also called TLP, TRF, TRP), which are found in most metazoans. TLFs and TBPs have well-conserved core domains; however, they only share about 60% similarity. TLFs, like TBPs, interact with TFIIA and TFIIB, which are part of the basal transcription machinery. Yet, in contrast to TBPs, TLFs seem not to interact with the TATA-box and even have a negative effect on the transcription of TATA-containing promoters. Recent results indicate that TLFs are involved in the transcription via TATA-less promoters
LDILIVNVVCQFSLRCHIDLRKLALAGRNVEYNPRYPKVTMRLREPRATASVWSSGKITITGATSEEEAK
QAARRAARLLQKLGFKVVRFSNFRVVNVLATCSMPFPIRLDELAAKNRSSASYEPELHPGVVYRITGPRA
TLSIFSTGSVTVTGARSMEDVREAVEKIYPIVFE
>gnl|CDD|239954 cd04518, TBP_archaea, archaeal TATA box binding protein (TBP): TBPs are transcription factors present in archaea and eukaryotes, that recognize promoters and initiate transcription. TBP has been shown to be an essential component of three different transcription initiation complexes: SL1, TFIID and TFIIIB, directing transcription by RNA polymerases I, II and III, respectively. TBP binds directly to the TATA box promoter element, where it nucleates polymerase assembly, thus defining the transcription start site. TBP's binding in the minor groove induces a dramatic DNA bending while its own structure barely changes. The conserved core domain of TBP, which binds to the TATA box, has a bipartite structure, with intramolecular symmetry generating a saddle-shaped structure that sits astride the DNA
SLKIENIVASVDLGQELDLEKVAAELPNAEYNPDQFPGLVYRLEDPKIAALIFRSGKMVCTGAKSVEDLH
RAVKEIIKKLKDYGIKVIEKPEIKVQNIVASADLGREVNLDAIAIGLPNAEYEPEQFPGLVYRLDEPKVV
LLLFSSGKMVITGAKSEEDAKRAVEKLLSRLKEL
>gnl|CDD|213328 cd04519, RasGAP, Ras GTPase Activating Domain. RasGAP functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin, among others. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP exhibit no similarity at their amino acid sequence level. RasGTPases function as molecular switches in a large number of signaling pathways. They are in the on state when bound to GTP, and in the off state when bound to GDP. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator
EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKNPNTLFR
GNSLATKLLDQYMKLVGQEYLKETLSPLIREILESKESCEIDTKLPVGEDLEENLENLLELVNKLVDRIL
SSLDRLPPELRYVFKILREFLAERFPEEPDEAYQAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRNL
TLISKVLQSLANGVEFGDKEPFMKPLNDFIKSNKPKLKQFLDELSS
>gnl|CDD|341359 cd04582, CBS_pair_ABC_OpuCA_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
EDAATPTPTVRPSTPLSDALGIMDDADSRYLVVVDADGRPLGYVTRRDARGASGTCGDFAHPFKATVPVD
ENLRVVLSRMYEHNTSWLPVVDEDGRYAGEVTQDSIADYLS
>gnl|CDD|341360 cd04583, CBS_pair_ABC_OpuCA_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
ITNPVTITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIEDINRNYRKAKKVGEIMERDVFTVKED
SLLRDTVDRILKRGLKYVPVVDEQGRLVGLVTRASLVDIV
>gnl|CDD|341361 cd04584, CBS_pair_AcuB_like, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain. The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
LVKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKATSLSIYELNYL
LSKIPVKDIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDILRAFI
>gnl|CDD|341362 cd04586, CBS_pair_BON_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLRREEPGTEPRRVWWLDALLESP
ERLAEEYVKAHGRTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLRA
>gnl|CDD|341363 cd04587, CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
LMSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRLVGIVTDRDLRNRVVAEGLDPDTPVSEIMTPPP
VTIDADALVFEALLLMLERNIHHLPVVDDGRVVGVVTATDLMRL
>gnl|CDD|341364 cd04588, CBS_pair_archHTH_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
SKDLITLKPDATIKDAAKLLSENNIHGAPVVDDGKLVGIVTLTDIAKALAEGKENAKVKDIMTKDVITID
KDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILKV
>gnl|CDD|341365 cd04589, CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
YLHPPLFVDAETSIREATRLMKENGADSLLVRDGDGRVGIVTRTDLRDAVVLDGQPVDTPVGEIATFPLI
SVEPDDFLFNALLLMTRHRVKRVVVREGEEIVGVLEQTDLLSF
>gnl|CDD|341366 cd04590, CBS_pair_CorC_HlyC_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLDLRA
LLRPPLFVPETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE
>gnl|CDD|341367 cd04591, CBS_pair_voltage-gated_CLC_euk_bac, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
TAEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEADLRPIMDPSP
FTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA
>gnl|CDD|341368 cd04592, CBS_pair_voltage-gated_CLC_euk_bac, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIQRFLKRAKADNEDPKTILVSSIC
TRNGGYCRGLWTCTPDMDLLTAKMLMEARGINQLPVVKRGGEERRRRVVGLLDRDSID
>gnl|CDD|341369 cd04594, CBS_pair_voltage-gated_CLC_archaea, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in archaea. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in archaea. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
KIRDIKVSAYDTVERALKIMRENNLLSLPVVDNDSNFLGAVYLRDIENKSPGKVGKYVVRGSPYVTPTSS
LEEAWEIMMRNKSRWVAVVEKGKFLGIITLDDLLEAY
>gnl|CDD|341370 cd04595, CBS_pair_DHH_polyA_Pol_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
SSPVKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDVDKAKHHGLGHAPVKGYMSTNVITID
PDTSLEEAQELMVEHDIGRLPVVEEGKLVGIVTRSDVLRY
>gnl|CDD|341371 cd04596, CBS_pair_DRTGG_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
LEETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIGKEDDTPIEKVMTKNPITVKPKT
SVASAAHMMIWEGIELLPVVDENRKLLGVISRQDVLKA
>gnl|CDD|341372 cd04597, CBS_pair_inorgPPase, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here
DLEYDKVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDIARTVDYIMTKDNLIVFKEDDY
LDEVKEIMLNTNFRNYPVVDENNKFLGTISRKHLIN
>gnl|CDD|341373 cd04598, CBS_pair_GGDEF_EAL, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
LLEEAPPVSPDTTNDEVYELFEENPDLHALPVVDNGRPVGLINRHQFLDRLATPYGRELYGKRPCSLFMD
KDPLVVDADTPIEELSQLATSRDQRYLYDGFIITENGRYLGVGTGRDLLRA
>gnl|CDD|341374 cd04599, CBS_pair_GGDEF_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
MTRNPITISPLDSVARAAALMERQRIGGLPVVENGKLVGIITSRDVRRAHPNRLVADAMSRNVVTISPEA
SLWEAKELMEEHGIERLVVVEEGRLVGIITKSTLYLE
>gnl|CDD|341375 cd04600, CBS_pair_HPP_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKHADLDPPRGLRGRLRRTLGLR
RDRPETVGDIMTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLIAALYR
>gnl|CDD|341376 cd04601, CBS_pair_IMPDH, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
ITDPVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIRFETDLSTPVSEVMTPDERLVTAP
EGITLEEAKEILHKHKIEKLPIVDDNGELVGLITRKDIEK
>gnl|CDD|341377 cd04603, CBS_pair_KefB_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the KefB (Kef-type K+ transport systems) domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the KefB (Kef-type K+ transport systems) domain which is involved in inorganic ion transport and metabolism. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
NLQLVFVNKNEPLREIIKKITELNARAIVIVNNNMSVLGQITVSDLLEIGPSQYETLTAYDLILVPLIRV
NCDAPITDLLRKFRETDPPIIAVIDDESKFIGTIYERELLKY
>gnl|CDD|341378 cd04604, CBS_pair_SIS_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
LLLRVSDLMHTGDELPLVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLRRALEKGLDILNL
PAKDVMTRNPKTISPDALAAEALELMEEHKITVLPVVDEDGKPVGILHLHDLLR
>gnl|CDD|341379 cd04605, CBS_pair_arch_MET2_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
LVEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVALKKDSLEEIMTRN
VITARPDEPIELAARKMEKHNISALPVVDDDRRVIGIITSDDISRL
>gnl|CDD|341380 cd04606, CBS_pair_Mg_transporter, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
DSAGRLMTTEFVAVRPDWTVEEALEYLRRLAPDPETIYYIYVVDEDRRLLGVVSLRDLLLADPDTKVSDI
MDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLDVI
>gnl|CDD|341381 cd04607, CBS_pair_NTP_transferase_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
NWKKVLVSPDTTIREAIEVIDKGALQIALVVDENRKLLGTVTDGDIRRGLLKGLSLDAPVEEVMNKNPIT
ASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDDLLA
>gnl|CDD|341382 cd04608, CBS_pair_CBS, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
DLIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVS
KAMYKQFKQVDLDTPLGALSRILERDHFALVVDGQGKVLGIVTRIDLLNY
>gnl|CDD|341383 cd04610, CBS_pair_ParBc_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
MTRDVITVSPDDTVKDVIKLIKETGHDGFPVVDDGKVVGYVTAKDLLGKDDDEKVSEIMSRDTVVADPDM
DITDAARVIFRSGISKLPVVDDEGNLVGIITNMDVIRS
>gnl|CDD|341384 cd04611, CBS_pair_GGDEF_PAS_repeat2, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 2. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
YLRLREVGSAMNRSPLVLPGDASLAEAARRMRSHRADAAVIECPDGGLGILTERDLVRFIARHPGNTPVG
ELASRPLLTVGAEDSLIHARDLLIDHRIRHLAVVDEDGQVTGLLGFADLLAGVEHEYLQDL
>gnl|CDD|341385 cd04613, CBS_pair_voltage-gated_CLC_bac, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in bacteria. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
MPRKVTVLPEGMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGVLFEEELWDLVVVKDLATTDV
ITVTPDDDLYTALLKFTSTNLDQLPVVDDDDPGKVLGMLSRRDVIAAYN
>gnl|CDD|341386 cd04614, CBS_pair_arch2_repeat2, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Inosine monophosphate (IMP) dehydrogenases and related proteins including IMP dehydrogenase IX from Methanothermobacter. IMP dehydrogenase is an essential enzyme in the de novo biosynthesis of Guanosine monophosphate (GMP), catalyzing the NAD-dependent oxidation of IMP to xanthosine monophosphate (XMP). The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
YAGKGVVPVWDETPLPVALRAMRLANVPAAPVLDSEGKLVGIVTERDLIDVSRIVESEEESGMSIADDED
EWSWEGIRDVMSLYYPTSNVELPDKPVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGEGDLAG
MLRDVDLLKA
>gnl|CDD|341387 cd04617, CBS_pair_CcpN, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
DIMSVPVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKDLLKATLGGQDLEKTPVSMIMTRM
PNIVTVTPDDSVLEAARKLIEHEIDSLPVVEKEDGKLKVVGRITKTNITRLFVEL
>gnl|CDD|341388 cd04618, CBS_euAMPK_gamma-like_repeat1, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in AMP-activated protein kinase gamma-like proteins, repeat 1. AMP-activated protein kinase (AMPK) plays multiple roles in the body's overall metabolic balance and response to exercise, nutritional stress, hormonal stimulation, and the glucose-lowering drugs metformin and rosiglitazone. AMPK consists of a catalytic alpha subunit and two non-catalytic subunits, beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers. This cd contains 2 tandem repeats of the CBS domains found in the gamma subunits of AMPK. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQM
EELEEHTIETWREIERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK
>gnl|CDD|341389 cd04620, CBS_two-component_sensor_histidine_kinase_repeat1, 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 1. This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
LEQAIDRHPLTVSPDTPVIEAIALMSQTRSSCCLLSEDSIITEARSSCVLVVENQQLVGIFTERDVVRLT
ASGIDLSGVTIAEVMTQPVITLKESEFQDIFTVLSLLRQHQIRHLPIVDDQGQLVGLITPESLRQV
>gnl|CDD|341390 cd04622, CBS_pair_HRP1_like, CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds. Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
MTRDVVTVSPDTTLREAARLMRDLDIGALPVCEGDRLVGMVTDRDIVVRAVAEGKDPNTTTVREVMTGDV
VTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDLAVE
>gnl|CDD|341391 cd04623, CBS_pair_bac_euk, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and eukaryotes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
GRDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRDV
VTCTPDDTVEECMALMTERRIRHLPVVEDGKLVGIVSIGDVVK
>gnl|CDD|341392 cd04629, CBS_pair_bac, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCEPGGTVADYMST
EVLTVSPDTSIVDLAQLFLKNKPRRYPVVEDGKLVGQISRRDVLRA
>gnl|CDD|341393 cd04630, CBS_pair_bac, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
VRDVMKTNVVTIDGLATVREALQLMKEHNVKSLIVEKRHEHDAYGIVTYTDILKKVIAEDRDPDLVNVYE
IMTKPAISVSPDLDIKYAARLMARFNLKRAPVIENNELIGIVSMTDLVLD
>gnl|CDD|341394 cd04631, CBS_archAMPK_gamma-repeat2, CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins. Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here
VVEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVTSTDIMRYLGSGEAFEKLKTGNIH
EVLNVPISSIMKRDIITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIITERDILRAI
>gnl|CDD|341395 cd04632, CBS_pair_arch1_repeat2, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
TEEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVRPGTKTRGGDRGGEKERML
DLPVYDIMSSPVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA
>gnl|CDD|341396 cd04638, CBS_pair_arch2_repeat1, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
MTKDVVTVTLPGTRDDVLEILKKKAISGVPVVKKETGKLVGIVTRKDLLRNPDEEQIALLMSRDPITISP
DDTLSEAAELMLEHNIRRVPVVDDDKLVGIVTVADLVRA
>gnl|CDD|341397 cd04639, CBS_pair_peptidase_M50, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
DAMVTEFPIVDADLTLREFADDYLIGKKSWREFLVTDEAGRLVGLITVDDLRAIPTSQWPDTPVRELMKP
LEEIPTVAADQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDIIELL
>gnl|CDD|341398 cd04640, CBS_pair_proteobact, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in proteobacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
DFRRVPPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGEKPLKIVQERGIPREELLV
ADVMTPRDKLEALDYEDVAHARVGDVVETLKASGRQHALVVDRDEDGRQEVRGIFSASQIARQ
>gnl|CDD|341399 cd04641, CBS_euAMPK_gamma-like_repeat2, CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase. The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHR
SEDFEGVHTCTLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV
>gnl|CDD|341400 cd04643, CBS_pair_bac, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
DFLIPAEKVAHVQDTNNLEHALLVLTKSGYSRIPVLDKDYKLVGLISLSMILDAILGLERIEFEKLSELK
VEEVMNTDVPTVSPDDDLEEVLHLLVDHPFLCVVDEDGYFLGIITRREILKAVNKLLHEF
>gnl|CDD|100051 cd04645, LbH_gamma_CA_like, Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain
EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVG
HGAVLHGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAE
LRESAEHYVELAK
>gnl|CDD|100052 cd04646, LbH_Dynactin_6, Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity
KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTIVNKKPKDPAEPKPMIIG
SNNVFEVGCKCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADCLRRTQTD
RPKPQTLQLDFLRKILPNYHHLKK
>gnl|CDD|100053 cd04647, LbH_MAT_like, Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form
NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVTSAPIVIGDDVWIGAN
VVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI
>gnl|CDD|100054 cd04649, LbH_THP_succinylT_putative, Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP succinyltransferase), C-terminal left-handed parallel alpha-helix (LbH) domain: This group is composed of mostly uncharacterized proteins containing an N-terminal domain of unknown function and a C-terminal LbH domain with similarity to THP succinyltransferase LbH. THP succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is trimeric and displays the left-handed parallel alpha-helix (LbH) structural motif encoded by the hexapeptide repeat motif
GVRIADADRVRLGAYLAEGTTVMHEGFVNFNAGTLGNCMVEGRISSGVIVGKGSDVGGGASIMGTLSGGG
NNVISIGKRCLLGANSGIGISLGDNCIVEAGLYVTAGTKVTLPDNEEFEKNVVKARELSGKNGLLFRRNS
QSGKVEA
>gnl|CDD|100055 cd04650, LbH_FBP, Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group
PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDHGYPTEIGDYVTI
GHNAVVHGAKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTEEEIE
WIKKNAEEYVELAE
>gnl|CDD|100056 cd04651, LbH_G1P_AT_C, Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization
PPYIGRRGEVKNSLVSEGCIISGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVV
IPDGVVIGGDPEEDRARFYVTEDGIVVVGKGMVI
>gnl|CDD|100057 cd04652, LbH_eIF2B_gamma_C, eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange
LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLV
GSGYRVEAGTE
>gnl|CDD|240015 cd04657, Piwi_ago-like, Piwi_ago-like: PIWI domain, Argonaute-like subfamily. Argonaute is the central component of the RNA-induced silencing complex (RISC) and related complexes. The PIWI domain is the C-terminal portion of Argonaute and consists of two subdomains, one of which provides the 5' anchoring of the guide RNA and the other, the catalytic site for slicing
PYLKEFGISVSKEMITVPGRVLPPPKLKYGDSSKTVPPRNGSWNLRGKKFLEGGPIRSWAVLNFAGPRRS
REERADLRNFVDQLVKTVIGAGINITTAIASVEGRVEELFAKLKQAKGEGPQLVLVILPKKDSDIYGRIK
RLADTELGIHTQCVLAKKVTKKGNPQYFANVALKINLKLGGINHSLEPDIRPLLTKEPTMVLGADVTHPS
PGDPAGAPSIAAVVASVDWHLAQYPASVRLQSHRQEIIDDLESMVRELLRAFKKATGKLPERIIYYRDGV
SEGQFAQVLNEELPAIRKACAKLYPGYKPKITFIVVQKRHHTRFFPTDEDDADGKNGNVPPGTVVDRGIT
HPREFDFYLCSHAGIQGTARPTHYHVLWDEIGFTADELQTLTYNLCYTYARCTRSVSIPPPAYYAHLAAA
RARCYL
>gnl|CDD|240016 cd04658, Piwi_piwi-like_Euk, Piwi_piwi-like_Euk: PIWI domain, Piwi-like subfamily found in eukaryotes. This domain is found in Piwi and closely related proteins, where it is believed to perform a crucial role in germline cells, via RNA silencing. RNA silencing refers to a group of related gene-silencing mechanisms mediated by short RNA molecules, including siRNAs, miRNAs, and heterochromatin-related guide RNAs. The mechanism in Piwi is believed to be similar to that in Argonaute, the central component of the RNA-induced silencing complex (RISC). The PIWI domain is the C-terminal portion of Argonaute and consists of two subdomains, one of which provides the 5' anchoring of the guide RNA and the other, the catalytic site for slicing
NLMKELAEHTKLNPKERYDTIRQFIQRIQKNPSVQELLKKWGIELDSNPLKIQGRVLPPEQIIMGNVFVY
ANSNADWKREIRNQPLYDAVNLNNWVLIYPSRDQREAESFLQTLKQVAGPMGIQISPPKIIKVKDDRIET
YIRALKDAFRSDPQLVVIILPGNKKDLYDAIKKFCCVECPVPSQVITSRTLKKKKNLRSIASKIALQINA
KLGGIPWTVEIPPFILKNTMIVGIDVYHDTITKKKSVVGFVASLNKSITKWFSKYISQVRGQEEIIDSLG
KSMKKALKAYKKENKKLPSRIIIYRDGVGDGQLKKVKEYEVPQIKKAIKQYSENYSPKLAYIVVNKRINT
RFFNQGGNNFSNPPPGTVVDSEITKPEWYDFFLVSQSVRQGTVTPTHYNVLYDTTGLKPDHLQRLTYKLC
HLYYNWSGSIRVPAPCQYAHKLAFLVGQ
>gnl|CDD|240017 cd04659, Piwi_piwi-like_ProArk, Piwi_piwi-like_ProArk: PIWI domain, Piwi-like subfamily found in Archaea and Bacteria. RNA silencing refers to a group of related gene-silencing mechanisms mediated by short RNA molecules, including siRNAs, miRNAs, and heterochromatin-related guide RNAs. The central component of the RNA-induced silencing complex (RISC) and related complexes is Argonaute. The PIWI domain is the C-terminal portion of Argonaute and consists of two subdomains, one of which provides the 5' anchoring of the guide RNA and the other, the catalytic site for slicing. This domain is also found in closely related proteins, including the Piwi subfamily, where it is believed to perform a crucial role in germline cells, via a similar mechanism
PTLEFGNGGSVKISRTGLLLKNYGPYDVPSKARREIRVAIIGTSELIGLIAALIGKLLQYLPKFPGFGGG
NKNALGKNKISVFRLDLNRSAQAEAIIEAVDLALSESSQGVDVVIVVLPEDLKELPEEFDLYDRLKAKLL
RLGIPTQFVREDTLKNRQDLAYVAWNLALALYAKLGGIPWKLDADSDPADLYIGIGFARSRDGEVRVTGC
AQVFDSDGLGLILRGAPIEEPTEDRSPADLKDLLKRVLEGYRESHRGRDPKRLVLHKDGRFTDEEIEGLK
EALEELGIKVDLVEVIKSGPHRLFRFGTYPNGFPPRRGTYVKLSDDEGLLWTHGSVPKYNTYPGMGTPRP
LLLRRHSGNTDLEQLASQILGLTKLNWNSFQFYSRLPVTIHYADRVAKLLKRLS
>gnl|CDD|240018 cd04660, nsLTP_like, nsLTP_like: Non-specific lipid-transfer protein (nsLTP)-like subfamily; composed of predominantly uncharacterized proteins with similarity to nsLTPs, including Medicago truncatula MtN5, the root-specific Phaseolus vulgaris PVR3, Antirrhinum majus FIL1, and Lilium longiflorum LIM3. Plant nsLTPs are small, soluble proteins that facilitate the transfer of fatty acids, phospholipids, glycolipids, and steroids between membranes. The MtN5 gene is induced during root nodule development. FIL1 is thought to be important in petal and stamen formation. The LIM3 gene is induced during the early prophase stage of meiosis in lily microsporocytes
CNMDLDLLAECQPYVTGPNPPPPPSRECCAALRRADLPCLCRYKTSLVLQIIDPDKAVYLPAKCGLPLPP
SSC
>gnl|CDD|467546 cd04661, NUDIX_MRP_L46, Mitochondrial ribosomal protein L46. Mitochondrial ribosomal protein L46 (MRP L46) is a component of the large subunit (39S) of the mammalian mitochondrial ribosome and a member of the NUDIX hydrolase superfamily. MRPs are thought to be involved in the maintenance of the mitochondrial DNA. In general, members of the NUDIX hydrolase superfamily require a divalent cation, such as Mg2+ or Mn2+, for activity and contain the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. MRP L46 appears to contain a modified NUDIX motif
RISAAVILSRLPEADEKNDRKSLERKLDRTLYLLVKQKKGKGPWQFPQGDVEEGETLREAAERGLRELGG
DNMNTWFVGNAPIGVYKYKYPKKTKEFGYKSFFLKGRFMPGQKKGVSDFAWLTKEELKEYVDPEYWKSVK
KM
>gnl|CDD|467547 cd04662, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
TSAGLLLYRRRDGGLEVLLVHPGGPFWARKDEGAWSIPKGEVEPGEDPLAAARREFEEETGFPAPGPFIP
LGEVRQKSGKVVHAWAVEGDLDPAAIVSNTFELEWPPRSGRRQEFPEVDRAAWFPLEEAREKLVKGQRPF
LDRLLAA
>gnl|CDD|467548 cd04663, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
RKVCAYVTRGRNRELLVFEHPDFPEAGLQVPKGTVEPGESPEEAALRELAEETGLTGARVVVDLGSHDEG
FEELHQRWFFHLCLAGEPPERWEHHETDDGEGGGLRFEFFWVPLAAAPPRLAAGFGAALELL
>gnl|CDD|467549 cd04664, NUDIX_DHNTPase_like, dihydroneopterin hydrolase. DHNTP pyrophosphatase (DHNTPase) catalyzes the hydrolysis of dihydroneopterin triphosphate (DHNTP) to dihydroneopterin monophosphate (DHNMP) and pyrophosphate,the second step in the pterin branch of the folate synthesis pathway in bacteria. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
FSVLVVIYRKDEEGEVLLLKRTDDGGFWQSVTGGIEDGETPWQAALRELKEETGLDPLELQLIDLNVSNF
YEIFDDWRPGVTVNTEHVFAVEVPEEQPIRLSPEHTDYRWLPYEEAAELLFWPSNREALREL
>gnl|CDD|467550 cd04665, NUDIX_RppH, RNA pyrophosphohydrolase. The initiation of mRNA degradation often requires deprotection of its 5' end. In eukaryotes, the 5'-methylguanosine (cap) structure is principally removed by the NUDIX family decapping enzyme Dcp2, yielding a 5'-monophosphorylated RNA that is a substrate for 5' exoribonucleases. In bacteria, the 5'-triphosphate group of primary transcripts is also converted to a 5' monophosphate by a NUDIX protein called RNA pyrophosphohydrolase (RppH), allowing access to both endo- and 5' exoribonucleases. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
KHVVVIARYKGKWLFTRHKERRGWEFPGGKREPGETIEEAARRELYEETGAVIFELKPLGQYSVHGKGQE
FFGAVYYAEVKSFEPILPYFETAEVRLFDELPEFSLTYPDIQPHLLEKLKE
>gnl|CDD|467551 cd04666, NUDIX_DIPP2_like_Nudt4, diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase type 2 and similar proteins. Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase type 2 (DIPP2), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 4; Nudt4, and other proteins including DIPP1/Nudt3, DIPP3a;APS2/Nudt10 and DIPP3beta;APS1/Nudt11. DIPP regulates the turnover of diphosphoinositol polyphosphates. The turnover of these high-energy diphosphoinositol polyphosphates represents a molecular switching activity with important regulatory consequences. Molecular switching by diphosphoinositol polyphosphates may contribute to regulating intracellular trafficking. Several alternatively spliced transcript variants have been described, but the full-length nature of some variants has not been determined. Isoforms DIPP2alpha and DIPP2beta are distinguishable from each other solely by DIPP2beta possessing one additional amino acid due to intron boundary skidding in alternate splicing. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
LQAGALPYRITKGELEVLLITSRKTGRWILPKGGPEKGETPAEAAAREAWEEAGVRGKVLKRPLGVYRYR
KRLKGRGLPCRVHVFPLEVTEELDDWPEKHERKRRWFSPEEAAELVDEPELRELLRRL
>gnl|CDD|467552 cd04667, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
RRATVICRRGDRILLVARRGGRWLLPGGKIEPGESPLEAAIRELKEETGLAALSLLYLFEHEGPHKLHHV
FLAEAPDGGRPRPGNEIARCRWVSADQLRDLNLSRATRLIVRRYLRR
>gnl|CDD|467553 cd04669, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
VRAVLVIYDDDKLLLIRRTKPGEEYYVFPGGGIEPGETPEEAALREAVEELGLDVAVTLITLILRVLNDG
TQHYFLARVITGSFGLGTGPEFERPERGTYEPVWVPLTALPALNLRPPEL
>gnl|CDD|467554 cd04670, NUDIX_ASFGF2_Nudt6, Antisense Basic Fibroblast Growth Factor. Antisense Basic Fibroblast Growth Factor (ASFGF2; EC 3.6.1.-), also known as nucleoside diphosphate-linked moiety X)) motif 6/Nudt6, and similar proteins including peroxisomal coenzyme A diphosphatase/Nudt7 and mitochondrial coenzyme A diphosphatase/Nudt8. The Nudt6 gene overlaps and lies on the opposite strand from FGF2 gene, and is thought to be the FGF2 antisense gene. The two genes are independently transcribed, and their expression shows an inverse relationship, suggesting that this antisense transcript may regulate FGF2 expression. This gene has also been shown to have hormone-regulatory and antiproliferative actions in the pituitary that are independent of FGF2 expression. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
HQVGVGGLVINENNEVLVVQEKYGGPGGWKLPGGLVDPGEDIGEAAVREVFEETGIDTEFVSILGFRHQH
PGRFGKSDLYFVCRLRPLSDEEIKICPEEIAEAKWMPLEEYLKQPNVSQINKLVAKLLLEC
>gnl|CDD|467555 cd04671, NUDIX_8DGDPP_Nudt18, 8-oxo-DGDP phosphatase. 8-oxo-DGDP phosphatase (8DGDPP; EC 3.6.1.55), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 18/Nudt18; 2-hydroxy-DADP phosphatase; 7,8-dihydro-8-oxoguanine phosphatase, hydrolyzes 8-oxo-7,8-dihydroguanine (8-oxo-Gua)-containing deoxyribo- and ribonucleoside diphosphates to the monophosphates. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
YVVAAVIINEQGEVLMIQEAKRSCRGKWYLPAGRVEPGESIVEAAKREVKEETGLKCEPSTLLSVEEAGG
SWYRFVFTGNITGGKLKTPADADSESLQAFWIDDISTKLPLRAHDILRLIERARQYRRKL
>gnl|CDD|467556 cd04672, NUDIX_CDP-Chase_like, CDP-Choline Pyrophosphatase and similar proteins. Members include: CDP-Choline Pyrophosphatase, ADP-ribose pyrophosphatase, and UDP-X diphosphatase. CDP-choline pyrophosphatase catalyzes the hydrolysis of CDP-choline to produce CMP and phosphocholine. ADP-ribose pyrophosphatase catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. UDP-X diphosphatase hydrolyzes UDP-N-acetylmuramic acid and UDP-N-acetylmuramoyl-L-alanine. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
PKVDVRAAVFKDGKILLVREKSDGRWTLPGGWADVGLSPAENAVKEVREESGYEVRARKLLAVFDRNKGG
HPPSPFHVYKLFFLCELIGGEAQTSIETSEVGFFALDDLPPLSLGRVTPEQIERLFEH
>gnl|CDD|467557 cd04673, NUDIX_ADPRase, ADP-ribose pyrophosphatase. ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). ADPRase-m is also known as NUDT9. It can be distinugished from the cytosolic ADPRase by a N-terminal target sequence unique to mitochondrial ADPRase. NUDT9 functions as a monomer
IVAVGAVVFRDGRVLLVRRGNPPDAGLWSFPGGKVELGETLEDAALRELREETGLEAEVVGLLTVVDVIE
RDEAGRVRFHYVILDFLAEWVSGEPVAGDDALDARWFSLEELDGLPLTPGTRDVLERA
>gnl|CDD|467558 cd04674, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
RNPLPVVVALLPVRDGLLVIRRGIEPGHGELALPGGYIEYGETWQEAAVRELREETGVEADAAEVRLFAV
RSAPDGTLLIFGLLPERPVADLPPFAPTDEATEWVVLTEPVELAFPLH
>gnl|CDD|467559 cd04676, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
DYLKNLRAKIGNELLFTPSVAAVILNEDGRILLQRKGGLGLWSLPAGAIEPGEHPAEAVIREVREETGLL
VKPTRLLGVFGGKEFRYTYPNGDQVEYTVIAFKCVVTGGTLNAIDGETSELRYFSRTQMPTLALPYPDEI
FFIG
>gnl|CDD|467560 cd04677, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
LRKLVGHRPLILVGAAVIILNEQGRILLQKRTDTGDWGLPGGAMELGESLEETARREVFEETGLTVEELE
LLGVYSGKDLYYTYPNGDEVYNVTAVYLVRDVSGELKVDDEESLELRFFSLDELPENINPQHRDVIE
>gnl|CDD|467561 cd04678, NUDIX_MTH2_Nudt15, MutT homolog 2. MutT Homolog 2 (MTH2; EC 3.6.1.9), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 15/Nudt15, may catalyze the hydrolysis of nucleoside diphosphates, triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP, and prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP. MTH2 may also play a role in DNA synthesis and cell cycle progression by stabilizing PCNA. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
PRVGVGVIVLNDDGKVLLGRRKGSHGAGTWALPGGHLEFGESFEECAAREVLEETGLEIRNVRFLTVTND
VFEEEGKHYVTIFVLAEVDDGEPEENMEPDKCEGWEWFSWDELPPLRPLFLPLANLLE
>gnl|CDD|467562 cd04679, NUDIX_MutT_Nudt1, MutT homolog-1 and similar proteins. MutT homolog-1 (MTH1), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 1/Nudt1, is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases
PRVGCGAAILDDGRLLLVLRLRAPEAGHWGLPGGKVDWLETVEDAVRREILEELGLEIELTRLLCVVDQI
DAADGEHWVAPVYLAEIFSGEPRLMEPEKHGGIGWFALDALPQPLTVATRDALEAL
>gnl|CDD|467563 cd04680, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
LGVRAIVLDDAGRVLLVRHTYVPGWYLPGGGVDKGETAEEAARRELREEAGVVLTGPPRLFGVYFNRRVS
PRDHVALYRVREFEQTEPPEPNGEIAEAGFFALDALPEDTTPATRRRLAEL
>gnl|CDD|467564 cd04681, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
YFHNVAAAVGVIIRNEGEILFVRRAKEPGKGKLDLPGGFVDPGESAEEALRRELREELGLKIPKLRYLCS
LPNTYLYKGITYKTCDLFFTAELDEKPKLKKAEDEVAELEWLDLEEIEPEKLAFPSIRKAVERYI
>gnl|CDD|467565 cd04682, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
SGAKLALFLGDKLLTILRDDKPGIPFPNLWDLPGGGREGDETPFACVLRELREELGLALPEDRLVWERVY
PSNHNPGRQSWFFVARLPADEVDAIRFGDEGQEWALMPVDDFLAHPDAVPHFQ
>gnl|CDD|467566 cd04683, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
VDVHLLLVRGDEVLLLRRANTGYDDGWWHLPAGHVEAGETVRAAAVREAKEELGVEIDPEDLRLVHTMHR
RSDGGRERIDFFFRATRWSGEPRNREPDKCAELRWFPLDALPENTVPYVRAALEAIRAGEPYSEHGW
>gnl|CDD|467567 cd04684, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. Contains a crystal structure of the NUDIX hydrolase from Enterococcus faecalis, which has an unknown function. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
PVFGEKLEGLNYKDRPGAYAVIFNDEGKVLLVQTPNGGYFLPGGGIEPGETPEEALHREVLEETGWEIEI
GEFLGNASRYFYSPDYDRYYLNIGYFYLAELVRKVSEPTEEDHELVWLPPEEAADLLKHEHHRWAVAKWL
>gnl|CDD|467568 cd04685, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
RAARVLLLDPDGRVLLFRFHDPDDPGRSWWFTPGGGVEPGESPEQAAVRELREETGLRLEPDDLGGPVWR
RRAVFDFSGETVRQDERFFLVRVPAFEVDTAGWTDLERAVIDGHRWWSLAELAATGETVYPRDLAELL
>gnl|CDD|467569 cd04686, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
HFGVYGIIIRNDKLLLIRKTRGPYQGRYDLPGGSQEFGESLEDALKREFAEETGMTVTSYDNLGVYDFFV
PWSDKELGDVHHIGVFYDVELLDNNISELLQFEGQDSLGAVWIPLQDLTELNSSPLVLKA
>gnl|CDD|467570 cd04688, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
FNIRVAAIIIRDGKVLLARGEDDDYYRLPGGRVEFGETSEDALVREFKEELGVEVEVVRLLFVVENFFTY
DGKPFHEIGFYYLVELSDEALYEQDIFFLEEDGEKLEFRWIPLEELDEIDLYPEFLKELL
>gnl|CDD|467571 cd04689, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
RHIARAIVVDDQNRFYFVVVVRDDDFGKGTLIETAGGGVEENENLEEAIRRELKEELGVEVDILCKIGIV
SDYYNLIHRHNINNYYLCKIKSFGDKNLTDYEIEDFHLSTLKLSYEEAVKEYEKCSNTRLGRLIANRELP
VLKKA
>gnl|CDD|467572 cd04690, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
IVKAAVIIIKDGRLLLVRKRGTDAFYLPGGKREPGETPLQALVRELKEELGLDLDPDSLRFLGTFEAPAA
NEPGTTVRMTCFTADYDGEPQPAAEIEELRWLDPADPDDDRLAPLLREIVLPL
>gnl|CDD|467573 cd04691, NUDIX_ADPRase, ADP-ribose pyrophosphatase and similar proteins. ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). ADPRase-m is also known as NUDT9. It can be distinugished from the cytosolic ADPRase by a N-terminal target sequence unique to mitochondrial ADPRase. NUDT9 functions as a monomer
WLGVGGVVVKEGKVLLVKRAYGPGKGRWTLPGGFVEEGETLDEAIVREVLEETGIDAKPVGIIGVRSGVI
RDGKSDNYVVFLLEYVGGEPKPDERENSEAGFLTLEEALANEDIADMSRELI
>gnl|CDD|467574 cd04692, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
LDIVDEDGRPIGVATRSEVHRQGLWHRTVHVWLVNPEEGRLLLQKRSANKDDFPGLWDISAAGHIDAGET
YEEAAVRELEEELGLTVSPEDLIFLGVIREEVIGGDFIDNEFVHVYLYETDRPLEEFKLQPEEVAGVVFV
DL
>gnl|CDD|467575 cd04693, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
ELWDLYDENRNKTGRTHRRGEPLPEGEYHLVVHVWIFNSDGEILIQQRSPDKKGFPGMWEASTGGSVLAG
ETSLEAAIRELKEELGIDLDADELRPILTIRFDNGFDDIYLFRKDVDIEDLTLQKEEVQDVKWVTLEEIL
EMIESGEFIPYQKYRLE
>gnl|CDD|467576 cd04694, NUDIX_Nudt17, nucleoside diphosphate-linked moiety X)) motif 17. Nucleoside diphosphate-linked moiety X)) motif 17 (EC 3.6.1.-) encoded by the NUDT17 gene on chromosome 1q21.1 and encodes an enzyme thought to hydrolyse some nucleoside diphosphate derivatives. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
VDVGVVVLIEDSDDRVLLTRRAKHMRTFPGVWVPPGGHVELGESLLEAGLRELQEETGLEVSDIQSLSLL
GLWESVYPTLLSIGLPKRHHIVVYYLVKLSESHENQEQLKLQEDEVDAAVWLPKSLLAKLLEAED
>gnl|CDD|467577 cd04696, NUDIX_NudI, NUDIX hydrolase subfamily. Nucleoside triphosphatase NudI catalyzes the hydrolysis of nucleoside triphosphates, with a preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and dCTP). It is a members of the NUDIX hydrolase superfamily which catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
QRTIVCPLIENEGCYLLCKMADDRGVFPGQWALSGGGVEPGERIEEALRREIREELGEQLILSDITPWTF
RDDIRIKTYPDGRQEEIYMIYLIFDCVSANRDVCINDEFQDYAWVKPADLANYDLNVATRVTLA
>gnl|CDD|467578 cd04697, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
VDIVDENNEVVGAATRAEMRRQKLIHRATYIVVRNAAGRLLVQKRTMDKDYCPGYLDPATGGVVGAGESY
EENARRELEEELGIDGVPLRPLFTFYYEDDRSRVWGALFECVYDGPLKLQPEEVAEVDWMSEDEILQAAR
GEEFTPDGRVALERYLA
>gnl|CDD|467579 cd04699, NUDIX_MutT_Nudt1, MutT homolog-1 and similar proteins. MutT homolog-1 (MTH1), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 1/Nudt1, is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases
FPVSVKGVIFDNGRVLLLRRSRAGAGEWELPGGRLEPGESPEEALKREVKEETGLDVSVGELLDTWTFEL
DPDKGVFIVTYLCRLVGGEVTLSDEHEEYEWVTPEELAELELPEGYRR
>gnl|CDD|467580 cd04700, NUDIX_DR1025_like, DR1025 and similar proteins. DR1025 from Deinococcus radiodurans, a member of the NUDIX hydrolase superfamily, show nucleoside triphosphatase and dinucleoside polyphosphate pyrophosphatase activities. Like other enzymes belonging to this superfamily, it requires a divalent cation, in this case Mg2+, for its activity. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. In general, substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
MQHGERTHVPVTLRAAGVVLLNERGDILLVQEKGISGHPEKAGLWHIPSGAVEDGENPQDAAVREACEET
GLRVRLVKFLGAYLGRFPDGVLVLRHVWLAEPEPGQVLAPAFTDEIAEASFVSREEFAQLYAAGQIRMYH
TKLFYAD
>gnl|CDD|271337 cd04701, Asparaginase_2, Bacterial/fungal L-Asparaginase type 2. L-Asparaginase hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzyme undergoes an autoproteolytic cleavage into alpha and beta subunits to expose a threonine residue which becomes the N-terminal residue of the beta subunit. The threonine residue plays a central role in hydrolase activity. Some asparaginases can also hydrolyze L-glutamine and are termed glutaminase-asparaginase. This is a member of the Ntn-hydrolase superfamily, and this subfamily covers mostly bacterial and fungal enzymes
ALAIHGGAGTISRANLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVF
TRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELVPQGTV
GAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWAVAVSGTGNGDSFIRVAAARDVAARMR
YKGLSLAEAAKEVVGPGGELGEGEGGIIAIDARGNVAMPFNCGGMYRAWIDEDG
>gnl|CDD|271338 cd04702, ASRGL1_like, Metazoan L-Asparaginase type 2. ASRGL1 and similar proteins constitute a subfamily of the L-Asparaginase type 2-like enzymes. The wider family includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2 enzymes. The proenzymes undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue. ASRGL1, or asparaginase-like 1, has been cloned from mammalian testis cDNA libraries. It has been identified as a sperm antigen that may induce the production of autoantibodies following obstruction of the male reproductive tract, e.g. vasectomy
KPVIVVHGGAGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNAD
GEVEMDASIMDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTE
RARERLEKFKKEKGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNL
VGAVSTTGHGESIMKVNLARLILFHMEQGKTAEEAAELALAYMKSRVKGLGGLIVVSKTGDWGAKFTSKR
MAWAAVKDG
>gnl|CDD|271339 cd04703, Asparaginase_2_like_1, Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family. The wider family of Asparaginase 2-like enzymes includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue
MAVLVHGGAGSDPERQDGLERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMD
AAVMTSGGAFGAVAAIEGVKNPVLVARAVMETSPHVLLAGDGAVRFARRLGYPDGCDTVGAVARDGGKFA
AAVSTGGTSPALRGRVGDVPIIGAGFYAGPKGAVAATGIGEEIAKRLLARRVYRWIETGLSLQAAAQRAI
DEFDDGVAVGVIAVSRRGEAGIASNTAMAWAIA
>gnl|CDD|153093 cd04704, PLA2_bee_venom_like, PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. Bee venom PLA2 has fewer conserved disulfide bridges than most canonical PLA2s
FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQC
LKNVNDSTSNQVGKIYFNVLQVPCFEL
>gnl|CDD|153094 cd04705, PLA2_group_III_like, PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers
TRLTSERRGLEKTGAIASSPDVSPFLSEGEFKEPDRCCWKHKQCPGHIIPPFSSDGHHNFHLHSVSHCDC
DSRLKDCLRLSSSSRVGPTCSHLLGTTCFN
>gnl|CDD|153095 cd04706, PLA2_plant, PLA2_plant: Plant-specific sub-family of Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. This sub-family does not appear to have a conserved active site and metal-binding loop
ISVPEECSRTCESYFCSGPPFLRYGKYCGPGYSGCPGERPCDDLDACCMTHDACVQAKKNDYLSLECNEK
FKNCVRRFRKARKPTFEGNKCIVTFVIPVITVVMDAALIASKLGKRP
>gnl|CDD|153096 cd04707, otoconin_90, otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites
QLGEMLKCLTGRCPREFEDYGCYCGQEGEGLPVDELDRCCFQHRCCLEQASEMGCLQDRKLSTEVTCVDH
KPKCEGVSVCEKLLCTCDKTAAECMAAAHFNSSLNSLDVSSCPGQVP
>gnl|CDD|240059 cd04708, BAH_plantDCM_II, BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5)-methyltransferases (DCM) from plants. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
FVYDGVTYSVGDFLYVSPDAFAEEERERATFKAGRNVGLKAFVVCQVLEIVVEKESKQADVASTQVKVRR
FYRPEDVSPEKAYASDIREVYYSEDTLTVPVEAVEGKCEVRKKSDLPDSDAPVIFEHVFFCELLYDPAKG
SLKQLPPNIKEEAYSTGASDSALRKRKGKGKGDSESDSEAPVKAPKENRLATLDIFAGCGGL
>gnl|CDD|240060 cd04709, BAH_MTA, BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The Metastasis-associated protein MTA1 is part of the NURD (nucleosome remodeling and deacetylating) complex and plays a role in cellular transformation and metastasis. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
ANMYRVGDYVYFESSPNNPYLIRRIEELNKTARGHVEAKVVCYYRRRDIPDSLYQLADQHRRELEEKSDD
LTPKQRHQLRHRELFLSRQVETLPATHIRGKCSVTLLNDTESARSYLAREDTFFYSLVYDPEQKTLLADQ
GEIRVGPSYQAKLPDLQPFPSPDG
>gnl|CDD|240061 cd04710, BAH_fungalPHD, BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
VGSLVLKNGELLKVNDHIYMSSEPPGEPYYIGRIMEFVPKHEFPSGIHARVFPASYFQVRLNWYYRPRDI
SRRVVADSRLLYASMHSDICPIGSVRGKCTVRHRDQIPDLEEYKKRPNHFYFDQLFDRYILRYYD
>gnl|CDD|240062 cd04711, BAH_Dnmt1_II, BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5)-methyltransferases from Bilateria, Dnmt1 and similar proteins. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
DEDLYPEYYRKSSDYIKGSNLDAPEPFRIGRIKEIFCAKRSNGKPNESDIKLRINKFYRPENTHKGFKAT
YHADINMLYWSDEEATVDFSAVQGRCTVEYGEDLPESVQEYSGGGPDRFYFLEAYNAKTKSFEDPPN
>gnl|CDD|240063 cd04712, BAH_DCM_I, BAH, or Bromo Adjacent Homology domain, as present in DNA (Cytosine-5)-methyltransferases (DCM) 1. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
IHGLTIRVGDVVSVERDDADSTTKWNDDHRWLPLVQFVEYMKKGSDGSKMFHGRWLYRGCDTVLGNYANE
RELFLTNECTCLELDLLSTEIKGVHKVDWSGTPWGKGLPEFFVRQSYYWPERGAFTSLKR
>gnl|CDD|240064 cd04713, BAH_plant_3, BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
TGKGKKKKCHYTSFEKDGNKYRLEDCVLLVPEDDQKPYIAIIKDIYKQEEGSLKLEVQWLYRPEEIEKKK
GGNWKAEDPRELFYSFHRDEVPAESVLHPCKVAFVPKGKQIPLRKGHSGFIVRRVYDNVNKKLWKLTDQD
YEDERQ
>gnl|CDD|240065 cd04714, BAH_BAHCC1, BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQD
ENSVQTIEHKCYVLTFAEYERLARVKKKPQDGVDFYYCAGTYNPDTGMLKC
>gnl|CDD|240066 cd04715, BAH_Orc1p_like, BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of Saccharomyces cerevisiae Orc1p and similar proteins. Orc1 is part of the Yeast Sir1-origin recognition complex, the Orc1p BAH doman functions in epigenetic silencing. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
EFKWGVKRGEGGKKKDGQFYRSFTYDGVEYRLYDDVYVHNGDSEPYIGKIIKIYETAIDSGKKKVKVIWF
FRPSEIRMELKGEPKRHINEVFLACGRGEGLANINLLESIIGKCNVVCISEDFRNPQPSDGIPTSADFLF
PCNFDVGRCVIVDKYDDKI
>gnl|CDD|240067 cd04716, BAH_plantDCM_I, BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5)-methyltransferases (DCM) from plants. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
GITYNLGDDAYVQGGEGEEPFICKITEFFEGTDGKTYFTAQWFYRAEDTVIERQATNHDKKRVFYSEIKN
DNPLDCLISKVKILQVPPNVGTKRKKPNSEKCDYYYDMEYCVPYSTFQTLRN
>gnl|CDD|240068 cd04717, BAH_polybromo, BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human polybromo protein (BAF180) is a component of the SWI/SNF chromatin-remodeling complex PBAF. It is thought that polybromo participates in transcriptional regulation. Saccharomyces cerevisiae RSC1 and RSC2 are part of the 15-subunit nucleosome remodeling RSC complex. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
GLQYRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEETFHEPTRKFYKNEVFKSPLYE
TVPVEEIVGKCAVMDVKDYIKGRPTEISEEDVYVCESRYNESAKSFKKIKT
>gnl|CDD|240069 cd04718, BAH_plant_2, BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
GFHLCCLRPPLKEVPEGDWICPFCEVEKSGQSAMPQLPPTSRSACEKLLSGDLWLARIEKLWEENGTYWY
AARWYTLPEETHMGRQPHNLRRELYLTNDFADIEMECILRHCSVKCPKEFRDASNDGDDVFLCEYEYDVH
WQSFKRLA
>gnl|CDD|240070 cd04719, BAH_Orc1p_animal, BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces cerevisiae Orc1p. Orc1 is part of the Yeast Sir1-origin recognition complex. The Orc1p BAH doman functions in epigenetic silencing. In vertebrates, a similar ORC protein complex exists, which has been shown essential for DNA replication in Xenopus laevis. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
ALTIEVGDFVLIEGEDADGPDVARILHLYEDGNEDDDPKRAIVQWFSRPSEVPKNKRKLLGREPHSQEVF
FYSRSSCDNDIDAETIIGKVRVEPVEPKTDLPETKKKTGGPLFVKRYWDTKTFRSLDS
>gnl|CDD|240071 cd04720, BAH_Orc1p_Yeast, BAH, or Bromo Adjacent Homology domain, as present in Orc1p, which again is part of the Saccharomyces cerevisiae Sir1-origin recognition complex, and as present in Sir3p. The Orc1p BAH doman functions in epigenetic silencing. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
LKDLKGWQIIITDEKGNGIDERNRRGETRRSRRRPRQAKRKIFLARDSDGLELSVGDTILVKDDVANSPS
VYLIHEIRLNTLNNEVELWVMWFLRWFEINPARYYKQFDPEFRSESNKNELYLTAELSEIKLKDIIDKAN
VLSESEFNDLSTDDKNGERTFFCRYACEPDGEEFVWIDI
>gnl|CDD|240072 cd04721, BAH_plant_1, BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
FCRNGVTISVHDFVYVLSEEEDRYVAYIEDLYEDKKGSKMVKVRWFHTTDEVGAALSPDSVNPREIFLSP
NLQVISVECIDGLATVLTREHYEKFQSVPKNSSELQAYFCYRQIDNNKVKPFDITQLRGY
>gnl|CDD|240073 cd04722, TIM_phosphate_binding, TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN
VILALLAGGPSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAA
AAVDIAAAAARAAGADGVEIHGAVGYLAREDLELIRELREAVPDVKVVVKLSPTGELAAAAAEEAGVDEV
GLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS
>gnl|CDD|240074 cd04723, HisA_HisF, Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria
RIIPVIDLKDGVVVHGVGGDRDNYRPITSNLCSTSDPLDVARAYKELGFRGLYIADLDAIMGRGDNDEAI
RELAAAWPLGLWVDGGIRSLENAQEWLKRGASRVIVGTETLPSDDDEDRLAALGEQRLVLSLDFRGGQLL
KPTDFIGPEELLRRLAKWPEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKL
GASGALVASALHDGGLTLEDVVR
>gnl|CDD|240075 cd04724, Tryptophan_synthase_alpha, Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 alpha and 2 beta subunits) that catalyzes the last two steps of L-tryptophan biosynthesis. Alpha and beta subunit catalyze two distinct reactions which are both strongly stimulated by the formation of the complex. The alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P). Indole is then channeled to the active site of the beta subunit, a PLP-dependent enzyme that catalyzes a replacement reaction to convert L-serine into L-tryptophan
ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKE
IRKKNTIPIVLMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTT
PDERIKKIAELASGFIYYVSRTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKYAD
GVIVGSALVKIIEEGGEEEALEALKELAESLK
>gnl|CDD|240076 cd04725, OMP_decarboxylase_like, Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates orotidine 5'-monophosphate (OMP) to form uridine 5'-phosphate (UMP), an essential step in the pyrimidine biosynthetic pathway. In mammals, UMP synthase contains two domains: the orotate phosphoribosyltransferase (OPRTase) domain that catalyzes the transfer of phosphoribosyl 5'-pyrophosphate (PRPP) to orotate to form OMP, and the orotidine-5'-phosphate decarboxylase (ODCase) domain that decarboxylates OMP to form UMP
LIVALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELGFLVFLDLKLGDIPNTVAAAAE
ALLGLGADAVTVHPYGGSDMLKAALEAAEEKGKGLFAVTVLSSPGALDLQEGIPGSLEDLVERLAKLARE
AGVDGVVCGATEPEALRRALGPDFLILTPGIGAQGSGDDQKRGGTPEDAIRAGADYIVVGRPITQAADPV
AAAEAI
>gnl|CDD|240077 cd04726, KGPDC_HPS, 3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates
PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEA
EMAFKAGADIVTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAKLLKLGVDIVILHRGIDAQA
AGGWWPEDDLKKVKKLLGVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF
>gnl|CDD|240078 cd04727, pdxS, PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings
RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMA
KVRIGHFVEAQILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKG
EAGTGNVVEAVRHMRAVNGEIRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPAD
AALMMQLGADGVFVGSGIFKSENPEKRARAIVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQ
ERG
>gnl|CDD|240079 cd04728, ThiG, Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH)
LTIGGKTFSSRLLLGTGKYPSPAIMKEAIEASGAEIVTVALRRVNIGDPGGESFLDLLDKSGYTLLPNTA
GCRTAEEAVRTARLAREALGTDWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFTVLPYCTDDPVLAKRL
EDAGCAAVMPLGSPIGSGQGLLNPYNLRIIIERADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKA
KDPVAMARAFKLAVEAGRLAYLAGRMPKRDYASASSPL
>gnl|CDD|240080 cd04729, NanE, N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates
MKLLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRD
YPDSEVYITPTIEEVDALAAAGADIIALDATDRPRPDGETLAELIKRIHEEYNCLLMADISTLEEALNAA
KLGFDIIGTTLSGYTEETAKTEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAIT
RPEHITGWF
>gnl|CDD|240081 cd04730, NPD_like, 2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN
IRYPIIQAPMAGVSTPELAAAVSNAGGLGFIGAGYLTPEALRAEIRKIRALTDKPFGVNLLVPSSNPDFE
ALLEVALEEGVPVVSFSFGPPAEVVERLKAAGIKVIPTVTSVEEARKAEAAGADALVAQGAEAGGHRGTF
DIGTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESGASPAYKQALLAATAE
DTVLTRAFSGRPARGLGALWAGQGVG
>gnl|CDD|240082 cd04731, HisF, The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria
KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEV
FIPLTVGGGIRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGGYEVYT
HGGRKPTGLDAVEWAKEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVE
AFEEGGADAALAASIFHFGEYTIAELKEYLAER
>gnl|CDD|240083 cd04732, HisA, HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene
IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVK
AVGIPVQVGGGIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDGKVATKGW
LETSEVSLEELAKRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKE
LGVAGVIVGKALYEGKITLEEALA
>gnl|CDD|240084 cd04733, OYE_like_2_FMN, Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase
LGQPLTLPNGATLPNRLAKAAMSERLADGRGLPTPELIRLYRRWAEGGIGLIITGNVMVDPRHLEEPGII
GNVVLESGEDLEAFREWAAAAKANGALIWAQLNHPGRQSPAGLNQNPVAPSVALDPGGLGKLFGKPRAMT
EEEIEDVIDRFAHAARLAQEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIR
AAVGPGFPVGIKLNSADFQRGGFTEEDALEVVEALEEAGVDLVELSGGTYESPAMAGAKKESTIAREAYF
LEFAEKIRKVTKTPLMVTGGFRTRAAMEQALASGAVDGIGLARPLALEPDLPNKLLAG
>gnl|CDD|240085 cd04734, OYE_like_3_FMN, Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. One member of this subgroup, the Sinorhizobium meliloti stachydrine utilization protein stcD, has been idenified as a putative N-methylproline demethylase
LLSPLQLGHLTLRNRIVSTAHATNYAEDGLPSERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNA
SDDEIIPGFRRLAEAVHAHGAVIMIQLTHLGRRGDGDGSWLPPLAPSAVPEPRHRAVPKAMEEEDIEEII
AAFADAARRCQAGGLDGVELQAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFI
VGIRISGDEDTEGGLSPDEALEIAARLAAEGLIDYVNVSAGSYYTLLGLAHVVPSMGMPPGPFLPLAARI
KQAVDLPVFHAGRIRDPAEAEQALAAGHADMVGMTRAHIADPHLVAKAREGREDDIRPCIGCN
>gnl|CDD|240086 cd04735, OYE_like_4_FMN, Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase
LFEPFTLKNGVTLKNRFVMAPMTTYSSNPDGTITDDELAYYQRRAGGVGMVITGATYVSPSGIGFEGGFS
ADDDSDIPGLRKLAQAIKSKGAKAILQIFHAGRMANPALVPGGDVVSPSAIAAFRPGAHTPRELTHEEIE
DIIDAFGEATRRAIEAGFDGVEIHGANGYLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDK
HADKDFILGYRFSPEEPEEPGIRMEDTLALVDKLADKGLDYLHISLWDFDRKSRRGRDDNQTIMELVKER
IAGRLPLIAVGSINTPDDALEALETGADLVAIGRGLLVDPDWVEKIKEGREDEINLEIDPDDLEELKIPP
ALW
>gnl|CDD|240087 cd04736, MDH_FMN, Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO)
EDYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIA
PTGLNGAFWPNGDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDLWFQLYVVHRELAELLVKRALAA
GYTTLVLTTDVAVNGYRERDLRNGFAIPFRYTPRVLLDGILHPRWLLRFLRNGMPQLANFASDDAIDVEV
QAALMSRQMDASFNWQDLRWLRDLWPHKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEA
LAEIVAATYKPVLIDSGIRRGSDIVKALALGANAVLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLAL
IGCPDIASLTP
>gnl|CDD|240088 cd04737, LOX_like_FMN, L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO)
KSLDIINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIK
LKTPIIMAPIAAHGLAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYMSKDDGFN
RSLLDRAKAAGAKAIILTADATVGGNREADIRNKFQFPFGMPNLNHFSEGTGKGKGISEIYAAAKQKLSP
ADIEFIAKISGLPVIVKGIQSPEDADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPII
FDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVKRTF
L
>gnl|CDD|240089 cd04738, DHOD_2_like, Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors
RPLLFLLDPETAHRLAIRALKLGLGPPLLLLLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLA
LGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRGGPLGVNIGKNKD
TPLEDAVEDYVIGVRKLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLGKKVPLLVKIA
PDLSDEELEDIADVALEHGVDGIIATNTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGK
IPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEGPGLVKRIKREL
>gnl|CDD|240090 cd04739, DHOD_like, Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive
DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLPSLFEEQIEREAQELDRFLTYGSSFAEA
LSYFPEYGRYNLGPEEYLELIRRAKRAVSIPVIASLNGVSAGGWVDYARQIEEAGADALELNIYALPTDP
DISGAEVEQRYLDILRAVKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRFYQPDIDLETLEV
VPNLLLSSPAEIRLPLRWIAILSGRVKASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTL
LAGLEAWMEEHGYESVQQLRGSMSQKNVPDPAAFERAQYMKALSS
>gnl|CDD|240091 cd04740, DHOD_1B_like, Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively
SVELAGLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPGGMLNAIGLQ
NPGVEAFLEELLPWLREFGTPVIASIAGSTVEEFVEVAEKLADAGADAIELNISCPNVKGGGMAFGTDPE
AVAEIVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINTLKGMAIDIETRKPILGNVTGGL
SGPAIKPIALRMVYQVYKAVEIPIIGVGGIASGEDALEFLMAGASAVQVGTANFVDPEAFKEIIEGLEAY
LDEEGIKSIEELVGLA
>gnl|CDD|240092 cd04741, DHOD_1A_like, Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively
VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPN
LGLDYYLEYIRTISDGLPGSAKPFFISVTGSAEDIAAMYKKIAAHQKQFPLAMELNLSCPNVPGKPPPAY
DFDATLEYLTAVKAAYSIPVGVKTPPYTDPAQFDTLAEALNAFACPISFITATNTLGNGLVLDPERETVV
LKPKTGFGGLAGAYLHPLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGP
KVFARIEKELEDIW
>gnl|CDD|240093 cd04742, NPD_FabD, 2-Nitropropane dioxygenase (NPD)-like domain, associated with the (acyl-carrier-protein) S-malonyltransferase FabD. NPD is part of the nitroalkaneoxidizing enzyme family, that catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDPs are members of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN
LGDRSFKEDYGLRYAYVAGAMARGIASAELVVAMGKAGMLGFFGAGGLPLDEVEQAIERIQAALGNGEPY
GVNLIHSPDEPELEEGLVDLFLRHGVRVVEASAFMQLTPALVRYRAKGLRRDADGRVQIANRIIAKVSRP
EVAEAFMSPAPERILKKLLAEGKITEEQAELARRVPVADDITVEADSGGHTDNRPLSVLLPTIIRLRDEL
AARYGYRRPIRVGAAGGIGTPEAAAAAFALGADFIVTGSINQCTVEAGTSDAVKDLLQKAGVQDTAYAPA
ADMFELGAKVQVLKRGTLFPARANKLYELYRRYDSLEEIPAKTRKQLEKKYFKRSFDEVWEETRAYFPER
DPAQIERAERNPKHKMALIFRWYLGLSSRWALEGDEERKVDYQIWCGPALGAFNQWVKGTYLEDWRNR
>gnl|CDD|240094 cd04743, NPD_PKS, 2-Nitropropane dioxygenase (NPD)-like domain, associated with polyketide synthases (PKS). NPD is part of the nitroalkaneoxidizing enzyme family, that catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDPs are members of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN
TRYPIVQGPMTRVSDVAEFAVAVAEGGGLPFIALALMRGEQVKALLEETAELLGDKPWGVGILGFVDTEL
RAAQLAVVRAIKPTFALIAGGRPDQARALEAIGISTYLHVPSPGLLKQFLENGARKFIFEGRECGGHVGP
RSSFVLWESAIDALLAANGPDKAGKIHLLFAGGIHDERSAAMVSALAAPLAERGAKVGVLMGTAYLFTEE
AVSAGAILPTFQDQAIAATRTALLETGPGHATRCVVSPFVDEFRATRRRMAREGVSGEEIKERLEALNVG
RLRLASKGVSRNPDGSRRAVEVSEEEQRKEGMYMIGQVAT
>gnl|CDD|100058 cd04745, LbH_paaY_like, paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity
PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIHGFPGQDTVLEENGHI
GHGAILHGCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSDEEVA
WKTRGTKEYQQLAAR
>gnl|CDD|240095 cd04747, OYE_like_5_FMN, Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase
LFTPFTLKGLTLPNRIVMAPMTRSFSPGGVPGQDVAAYYRRRAAGGVGLIITEGTAVDHPAASGDPNVPR
FHGEDALAGWKKVVDEVHAAGGKIAPQLWHVGAMRKLGTPPFPDVPPLSPSGLVGPGKPVGREMTEADID
DVIAAFARAAADARRLGFDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGP
DFPIILRFSQWKQQDYTARLADTPDELEALLAPLVDAGVDIFHCSTRRFWEPEFEGSELNLAGWTKKLTG
LPTITVGSVGLDGDFIGAFAGDEGASPASLDRLLERLERGEFDLVAVGRALLSDPAWVAKVREGRLDELI
PFSRAALATLY
>gnl|CDD|240096 cd04748, Commd, COMM_Domain, a family of domains found at the C-terminus of HCarG, the copper metabolism gene MURR1 product, and related proteins. Presumably all COMM_Domain containing proteins are located in the nucleus and the COMM domain plays a role in protein-protein interactions. Several family members have been shown to bind and inhibit NF-kappaB. Murr1/Commd1 is a protein involved in copper homeostasis, which has also been identified as a regulator of the human delta epithelial sodium channel. HCaRG, a nuclear protein that might be involved in cell proliferation, is negatively regulated by extracellular calcium concentration, and its basal mRNA levels are higher in hypertensive animals
LLTENKAEIEELLSKQSLSLPQLVDFDWRLDVQISSSSLAKVKQPTILVQLKLQVGDNNSSEKICFEMTK
EELQNFLNKLKKIKAQL
>gnl|CDD|240097 cd04749, Commd1_MURR1, COMM_Domain containing protein 1, also called Murr1. Murr1/Commd1 is a protein involved in copper homeostasis, which has also been identified as a regulator of the human delta epithelial sodium channel. The COMM Domain is found at the C-terminus of a variety of proteins; presumably all COMM_Domain containing proteins are located in the nucleus and the COMM domain plays a role in protein-protein interactions. Several family members have been shown to bind and inhibit NF-kappaB
LSGLLNGIAQKEYYGNAEITEELLRSELYPEDPLEEFRALHNKMRGLLKSIASADMDINQLEAFLTAQTK
KQGGITSLQAAVIAKFWKVHKKKIRESLLAQSRWENSLRGLSWRVDLKTQSRHIAQINSPVAIVELELGK
TGQESEFVCLEFDEAKVNRVLKQLAEIQESLDAL
>gnl|CDD|240098 cd04750, Commd2, COMM_Domain containing protein 2. The COMM Domain is found at the C-terminus of a variety of proteins; presumably all COMM_Domain containing proteins are located in the nucleus and the COMM domain plays a role in protein-protein interactions. Several family members have been shown to bind and inhibit NF-kappaB
EFCKLAIEFLFKGINQKKYEGAARKLEVEVETVQHGVEALVYLLIESTKLKLSERDFQDSIEFLGFSDDL
NEILLQLYESNRKEIRNILKELSPDLPHYHNLEWRLDVQIASRSLRSQVKPVITMKLHLEDENKKIETHL
LQTDPANLVHLTQTLEQALQESKTLH
>gnl|CDD|240099 cd04751, Commd3, COMM_Domain containing protein 3. The COMM Domain is found at the C-terminus of a variety of proteins; presumably all COMM_Domain containing proteins are located in the nucleus and the COMM domain plays a role in protein-protein interactions. Several family members have been shown to bind and inhibit NF-kappaB
EIFAKQYQKKKEVLENKLKSIGISFPHITDVNWRLDYVVSSKHLGKVNQPIYLIQLSTENGENKPDINFT
CTLEQLQDLVNKLKDAAKNIERAAQ
>gnl|CDD|240100 cd04752, Commd4, COMM_Domain containing protein 4. The COMM Domain is found at the C-terminus of a variety of proteins; presumably all COMM_Domain containing proteins are located in the nucleus and the COMM domain plays a role in protein-protein interactions. Several family members have been shown to bind and inhibit NF-kappaB
ISSVKMKLLCAQVLKDLLGEGIDYEKVLKLTADAKFESGDVKASIAVLSFILSSAAKYNVDGESLSSELQ
QLGLPKEHATSLCRSYEEKQSKLQESLRANSLRLSRLESVDWRVDYILSSSELQEVNEPLVQLRLKVRNA
DTGEITPHPFSVSADKFRVLLAELKQAQTLMETL
>gnl|CDD|240101 cd04753, Commd5_HCaRG, COMM_Domain containing protein 5, also called HCaRG (hypertension-related, calcium-regulated gene). HCaRG is a nuclear protein that might be involved in cell proliferation; it is negatively regulated by extracellular calcium concentration, and its basal mRNA levels are higher in hypertensive animals. The COMM Domain is found at the C-terminus of a variety of proteins; presumably all COMM_Domain containing proteins are located in the nucleus and the COMM domain plays a role in protein-protein interactions. Several family members have been shown to bind and inhibit NF-kappaB
ELRIPEELITDLASVVYGQRRPLLESGALQKGVRLPHLEDFKWRVDVAISTSSLSRVLQPSILMEMKLSD
GKSHRFEVPVAKFHELRYNVALILKEMNDLEKRSILKIQD
>gnl|CDD|240102 cd04754, Commd6, COMM_Domain containing protein 6. The COMM Domain is found at the C-terminus of a variety of proteins; presumably all COMM_Domain containing proteins are located in the nucleus and the COMM domain plays a role in protein-protein interactions. Several family members have been shown to bind and inhibit NF-kappaB
DQQGKLLTASDSVDQVLNIGQLVDFKWKLGMAVSSDTCRSLNSPYVAVTLKVADPSGQVVTKSFEMTIPE
FQNFSRQFKEMAAVLE
>gnl|CDD|240103 cd04755, Commd7, COMM_Domain containing protein 7. The COMM Domain is found at the C-terminus of a variety of proteins; presumably all COMM_Domain containing proteins are located in the nucleus and the COMM domain plays a role in protein-protein interactions. Several family members have been shown to bind and inhibit NF-kappaB
IQNLNQLSEQQFSRLTEILFEFLLEPKESERLLNQLDEFAGENGISLGPLKNIVKSILLVPNGALKRNLT
AEQLREDLIQLGLSEEKASYFSEQWKQHYSTLSRSAVGQTLMVNQLVDMEWKFGVTAGSSELQKVGSIFL
QLKLVVRKGNQTENVYMELTLPQFYSFLHEMERAKASLEC
>gnl|CDD|240104 cd04756, Commd8, COMM_Domain containing protein 8. The COMM Domain is found at the C-terminus of a variety of proteins; presumably all COMM_Domain containing proteins are located in the nucleus and the COMM domain plays a role in protein-protein interactions. Several family members have been shown to bind and inhibit NF-kappaB
TPPELINLLPVAQIVKLLHRVVDGVCGRAYPRYQDYSAIWSLEEWTEVLESLATLFKQAVGKNSNDEEAK
AQLSDLSSSHQEALLKCVKSRKEEIRQALVNKTNSISSAQLQDFDWQLKLALSSDKLSSLQEPLLNLDLD
VKENGILKPVSIEMNKEELQNLISSLEAANKVVLQL
>gnl|CDD|240105 cd04757, Commd9, COMM_Domain containing protein 9. The COMM Domain is found at the C-terminus of a variety of proteins; presumably all COMM_Domain containing proteins are located in the nucleus and the COMM domain plays a role in protein-protein interactions. Several family members have been shown to bind and inhibit NF-kappaB
FHSNLKNLLTKIILENRDKWRSEASENQISLPKLVDHDWRVDIKTSSDSLGRMAVPTCLLQMKIQEAPSL
CGLLPPLSTLTMELSKETLDTMLDGLGRIRDQLSAVAQ
>gnl|CDD|240106 cd04758, Commd10, COMM_Domain containing protein 10. The COMM Domain is found at the C-terminus of a variety of proteins; presumably all COMM_Domain containing proteins are located in the nucleus and the COMM domain plays a role in protein-protein interactions. Several family members have been shown to bind and inhibit NF-kappaB
IKEAVSLINSIDTEKFPRLLSRLFQKLHLKAERSFSEEEEEKLQEAFKLLSQDLKLLLETISFILEQAAY
HNLKPSNLQQQLRNILLLEDKASAFVNAWEAEGEDVLEKLRSRILAPNQLEDVSWRLNLQMSSSTQAKLK
SPLAVLELGVTSEDGNLEKINLEFNHEELLEFYNQLESIQEQLDSL
>gnl|CDD|212498 cd04759, Rib_hydrolase, ADP-ribosyl cyclase, also known as cyclic ADP-ribose hydrolase or CD38. ADP-ribosyl cyclase (EC:3.2.2.5) synthesizes the second messenger cyclic-ADP ribose (cADPR), which in turn releases calcium from internal stores. Mammals possess two membrane proteins, CD38 and BST-1/CD157, which exhibit ADP-ribosyl cyclase activity, as well as intracellular soluble ADP-ribose cyclases. CD38 is involved in differentiation, adhesion, and cell proliferation, and has been implicated in diseases such as AIDS, diabetes, and B-cell chronic lymphocytic leukemia. The extramembrane domain of CD38 acts as a multifunctional enzyme, and can synthesize cADPR from NAD+, hydrolyze NAD+ and cADPR to ADPR, as well as catalyze the exchange of the nicotinamide group of NADP+ with nicotinic acid under acidic conditions, to yield NAADP+ (nicotinic acid-adenine dinucleotide phosphate), a metabolite involved in Ca2+ mobilization from acidic stores
GTTPNLKEIFLGRCYDYQALHNPEEREVDCSKLWNAFEKAFAFKDPCNVTPEDYDPFFNLAPQTIPCDKT
LFWSGTYDLVHSYTKVLRRFFTLEDTLPGYLLNGLTWCGQKDSSGINYTSCPTWEECSNNAVDAFWKRAS
ARFAEQASGDVHVMLNGSRAGGAYNNNSTFGSVELPNLNPPKVTKLNIYVVHDLEGNPRESCGSGSLKEL
QNDLKSKNITFTCIDNPRPVRHLQCIKNPNSPEC
>gnl|CDD|240107 cd04760, BAH_Dnmt1_I, BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5)-methyltransferases from Bilateria, Dnmt1 and similar proteins. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions
GEELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIGGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDM
ALSSIHGKVNVIYKAPSENWSMEGGMDEEDEIFEDDGKTFFYQKWYDPECARFE
>gnl|CDD|133389 cd04761, HTH_MerR-SF, Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily. Helix-turn-helix (HTH) transcription regulator MerR superfamily, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
YTIGELAKLTGVSPSTLRYYERIGLLSPARTEGGYRLYSDADLERLRLI
>gnl|CDD|133390 cd04762, HTH_MerR-trunc, Helix-Turn-Helix DNA binding domain of truncated MerR-like proteins. Proteins in this family mostly have a truncated helix-turn-helix (HTH) MerR-like domain. They lack a portion of the C-terminal region, called Wing 2 and the long dimerization helix that is typically present in MerR-like proteins. These truncated domains are found in response regulator receiver (REC) domain proteins (i.e., CheY), cytosine-C5 specific DNA methylases, IS607 transposase-like proteins, and RacA, a bacterial protein that anchors chromosomes to cell poles
LTTKEAAELLGVSPSTLRRWVKEGKLKAIRTPGGHRRFPEEDLERLLGI
>gnl|CDD|133391 cd04763, HTH_MlrA-like, Helix-Turn-Helix DNA binding domain of MlrA-like transcription regulators. Helix-turn-helix (HTH) transcription regulator MlrA (merR-like regulator A) and related proteins, N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. Its close homolog, CarA from Myxococcus xanthus, is involved in activation of the carotenoid biosynthesis genes by light. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Many MlrA-like proteins in this group appear to lack the long dimerization helix seen in the N-terminal domains of typical MerR-like proteins
YTIGEVALLTGIKPHVLRAWEREFGLLKPQRSDGGHRLFNDADIDRILEIKRWIDNGVQVSKVKKLLS
>gnl|CDD|133392 cd04764, HTH_MlrA-like_sg1, Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators. Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 1). The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Many MlrA-like proteins in this group appear to lack the long dimerization helix seen in the N-terminal domains of typical MerR-like proteins
YTIKEVSEIIGVKPHTLRYYEKEFNLYIPRTENGRRYYTDEDIELLKKIKTLLEKGLSIKEIKEILN
>gnl|CDD|133393 cd04765, HTH_MlrA-like_sg2, Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators. Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 2), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules
FSIGEVAEILGLPPHVLRYWETEFPQLKPVKRAGGRRYYRPKDVELLLLIKHLLYEKGYTIEGAKQALKE
DGAAAIREEEAEERLPSIRAELLDLRDQL
>gnl|CDD|133394 cd04766, HTH_HspR, Helix-Turn-Helix DNA binding domain of the HspR transcription regulator. Helix-turn-helix (HTH) transcription regulator HspR, N-terminal domain. Heat shock protein regulators (HspR) have been shown to regulate expression of specific regulons in response to high temperature or high osmolarity in Streptomyces and Helicobacter, respectively. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules
VYVISVAAELSGMHPQTLRLYERLGLLSPSRTDGGTRRYSERDIERLRRIQRLTQELGVNLAGVKRILEL
EEELAELRAELDELRARLRRE
>gnl|CDD|133395 cd04767, HTH_HspR-like_MBC, Helix-Turn-Helix DNA binding domain of putative HspR-like transcription regulators. Putative helix-turn-helix (HTH) transcription regulator HspR-like proteins. Unlike the characterized HspR, these proteins have a C-terminal domain with putative metal binding cysteines (MBC). Heat shock protein regulators (HspR) have been shown to regulate expression of specific regulons in response to high temperature or high osmolarity in Streptomyces and Helicobacter, respectively. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules
LYPIGVVAELLNIHPETLRIWERHGLIKPARRNGQRLYSNNDLKRLRFIKKLINEKGLNIAGVKQILSMY
PCWSIRDCDEGGRKSKTEIINFPKPCWKEEGTYCCISFDKDLLCSDCEVY
>gnl|CDD|133396 cd04768, HTH_BmrR-like, Helix-Turn-Helix DNA binding domain of BmrR-like transcription regulators. Helix-turn-helix (HTH) BmrR-like transcription regulators (TipAL, Mta, SkgA, BmrR, and BltR), N-terminal domain. These proteins have been shown to regulate expression of specific regulons in response to various toxic substances, antibiotics, or oxygen radicals in Bacillus subtilis, Streptomyces, and Caulobacter crescentus. They are comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain HTH motifs that mediate DNA binding, while the C-terminal domains are often unrelated and bind specific coactivator molecules. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements
LTIGEFAKLAGVSIRTLRHYDDIGLFKPAKIAENGYRYYSYAQLYQLQFILFLRELGFSLAEIKELLDTE
MEELTAMLLEKKQAIQQKIDRLQQLE
>gnl|CDD|133397 cd04769, HTH_MerR2, Helix-Turn-Helix DNA binding domain of MerR2-like transcription regulators. Helix-turn-helix (HTH) transcription regulator MerR2 and related proteins. MerR2 in Bacillus cereus RC607 regulates resistance to organomercurials. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
MYIGELAQQTGVTIKAIRLYEEKGLLPSPKRSGNYRVYDAQHVECLRFIKEARQLGFTLAELKAIFAGHE
GRAVLPWPHLQQALEDKKQEIRAQITELQQLLARLDAFEASLKDAL
>gnl|CDD|133398 cd04770, HTH_HMRTR, Helix-Turn-Helix DNA binding domain of Heavy Metal Resistance transcription regulators. Helix-turn-helix (HTH) heavy metal resistance transcription regulators (HMRTR): MerR1 (mercury), CueR (copper), CadR (cadmium), PbrR (lead), ZntR (zinc), and other related proteins. These transcription regulators mediate responses to heavy metal stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
MKIGELAKAAGVSPDTIRYYERIGLLPPPQRSENGYRLYGEADLARLRFIRRAQALGFSLAEIRELLSLR
DDGAAPCAEVRALLEEKLAEVEAKIAELQALRAELAGLLSACDGDESVICPIL
>gnl|CDD|133399 cd04772, HTH_TioE_rpt1, First Helix-Turn-Helix DNA binding domain of the regulatory protein TioE. Putative helix-turn-helix (HTH) regulatory protein, TioE, and related proteins. TioE is part of the thiocoraline gene cluster, which is involved in the biosynthesis of the antitumor thiocoraline from the marine actinomycete, Micromonospora. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Proteins in this family are unique within the MerR superfamily in that they are composed of just two adjacent MerR-like N-terminal domains; this CD contains the N-terminal or first repeat (rpt1) of these tandem MerR-like domain proteins
YRTVDLARAIGLSPQTVRNYESLGLIPPAERTANGYRIYTDKHIAALRAYRALLPGYGYRVAQRIMRAVH
AGIVASALALVDAAHALLQRYRQQLDQEL
>gnl|CDD|133400 cd04773, HTH_TioE_rpt2, Second Helix-Turn-Helix DNA binding domain of the regulatory protein TioE. Putative helix-turn-helix (HTH) regulatory protein, TioE, and related proteins. TioE is part of the thiocoraline gene cluster, which is involved in the biosynthesis of the antitumor thiocoraline from the marine actinomycete, Micromonospora. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Proteins in this family are unique within the MerR superfamily in that they are composed of just two adjacent MerR-like N-terminal domains; this CD mainly contains the C-terminal or second repeat (rpt2) of these tandem MerR-like domain proteins
MTIGELAHLLGVPPSTLRHWEKEGLLSPDREPETGYRVYDPSDVRDARLIHLLRRGGYLLEQIATVVEQL
RHAGGTEALAAALEQRRVALTQRGRAMLDAAAALAAYL
>gnl|CDD|133401 cd04774, HTH_YfmP, Helix-Turn-Helix DNA binding domain of the YfmP transcription regulator. Helix-turn-helix (HTH) transcription regulator, YfmP, and related proteins; N-terminal domain. YfmP regulates the multidrug efflux protein, YfmO, and indirectly regulates the expression of the Bacillus subtilis copZA operon encoding a metallochaperone, CopZ, and a CPx-type ATPase efflux protein, CopA. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules
YKVDEVAKRLGLTKRTLKYYEEIGLVSPERSEGRYRLYSEEDLKRLERILRLREVLGFSLQEVTHFLERP
LEPVDGGHRYSAESLREIHDALAQQV
>gnl|CDD|133402 cd04775, HTH_Cfa-like, Helix-Turn-Helix DNA binding domain of Cfa-like transcription regulators. Putative helix-turn-helix (HTH) MerR-like transcription regulators; the HTH domain of Cfa, a cyclopropane fatty acid synthase, and other related methyltransferases, as well as, the N-terminal domain of a conserved, uncharacterized ~172 a.a. protein. Based on sequence similarity of the N-terminal domain, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
MYTIGQMSRKFGVSRSTLLYYESIGLIPSARSEANYRLYSEADLSRLEKIVFLQAGGLPLEEIAGCLAQP
HVQAILEERLQSLNREIQRLRQQQQVLAAILG
>gnl|CDD|133403 cd04776, HTH_GnyR, Helix-Turn-Helix DNA binding domain of the regulatory protein GnyR. Putative helix-turn-helix (HTH) regulatory protein, GnyR, and other related proteins. GnyR belongs to the gnyRDBHAL cluster, which is involved in acyclic isoprenoid degradation in Pseudomonas aeruginosa. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules
YTISELAREFDVTPRTLRFYEDKGLLSPERRGQTRVYSRRDRARLKLILRGKRLGFSLEEIRELLDLYDP
PGGNRKQLEKMLEKIEKRRAELEQQRRDIDAALAELDAAEERCRERLA
>gnl|CDD|133404 cd04777, HTH_MerR-like_sg1, Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily. Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 1), N-terminal domain. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
MKIGKFAKKNNITIDTVRHYIDLGLLIPEKKGGQYFFDEKCQDDLEFILELKGLGFSLIEIQKIFSYKRL
TKSRTHEDQDYYKSFLKNKKDELEKEIEDLKKAIQKL
>gnl|CDD|133405 cd04778, HTH_MerR-like_sg2, Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily. Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 2). Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
EYRIDDLARAAGTTVRNVRAYQDRGLLPPPRRRGRVAIYNDSHLARLRLINQLLERGYTLAHIAELLAAW
EQGRDLGDVLGLQAAIDGPWSTEEPGTALLAELQSEFGDERALARAVALGLLEPDGDRVLVPSPRLLEAL
AELVDAGIPLRAVLDLVAAVRRHADDVAERFVDAVGERIHAREGGLLPRPADVDEIAQVVQRYRPLARDA
VEAELDQAL
>gnl|CDD|133406 cd04779, HTH_MerR-like_sg4, Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily. Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 4). Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
YRIGQLAHLAGVSKRTIDYYTNLGLLTPERSDSNYRYYDETALDRLQLIEHLKGQRLSLAEIKDQLEEVQ
RSDKEQREVAQEVQLVCDQIDGLEHRLKQLKPIASQTDRAQRMKMTKELSQQVLTLIQSLTLLL
>gnl|CDD|133407 cd04780, HTH_MerR-like_sg5, Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily. Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 5), N-terminal domain. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
MRMSELSKRSGVSVATIKYYLREGLLPEGRRLAPNQAEYSEAHVERLRLIRALQQEGGLPISQIKEVLDA
IADASLPSTLLALAVQRFGLEEPNV
>gnl|CDD|133408 cd04781, HTH_MerR-like_sg6, Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily. Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 6) with at least two conserved cysteines present in the C-terminal portion of the protein. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
LDIAEVARQSGLPASTLRYYEEKGLIASIGRRGLRRQYDPQVLDRLALIALGRAAGFSLDEIQAMLSHDG
KPPIDRQLLKAKAAELDQQIQRLQAMRELLRHVAQCPAPSHLDCPTFQRL
>gnl|CDD|133409 cd04782, HTH_BltR, Helix-Turn-Helix DNA binding domain of the BltR transcription regulator. Helix-turn-helix (HTH) multidrug-efflux transporter transcription regulator, BltR (BmrR-like transporter) of Bacillus subtilis, and related proteins; N-terminal domain. Blt, like Bmr, is a membrane protein which causes the efflux of a variety of toxic substances and antibiotics. These regulators are comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the C-terminal domains are often unrelated and bind specific coactivator molecules. They share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements
FTTGEFAKLCGISKQTLFHYDKIGLFKPEIVKENGYRYYTLEQFEQLDIILLLKELGISLKEIKDYLDNR
NPDELIELLKKQEKEIKEEIEELQKIK
>gnl|CDD|133410 cd04783, HTH_MerR1, Helix-Turn-Helix DNA binding domain of the MerR1 transcription regulator. Helix-turn-helix (HTH) transcription regulator MerR1. MerR1 transcription regulators, such as Tn21 MerR and Tn501 MerR, mediate response to mercury exposure in eubacteria. These proteins are comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain winged HTH motifs that mediate DNA binding, while the C-terminal domains have three conserved cysteines that define a mercury binding site. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements
LTIGELAKAAGVNVETIRYYQRRGLLPEPPRPEGGYRRYPEETVTRLRFIKRAQELGFTLDEIAELLELD
DGTDCSEARELAEQKLAEVDEKIADLQRMRASLQELVSQCAATKNNVSCPIIAALE
>gnl|CDD|133411 cd04784, HTH_CadR-PbrR, Helix-Turn-Helix DNA binding domain of the CadR and PbrR transcription regulators. Helix-turn-helix (HTH) CadR and PbrR transcription regulators including Pseudomonas aeruginosa CadR and Ralstonia metallidurans PbrR that regulate expression of the cadmium and lead resistance operons, respectively. These proteins are comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the C-terminal domains have three conserved cysteines which form a putative metal binding site. Some members in this group have a histidine-rich C-terminal extension. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements
MKIGELAKKTGCSVETIRYYEKEGLLPAPARSANNYRLYDEEHLERLLFIRRCRSLDMSLDEIRTLLQLQ
DDPEASCAEVNALIDEHLAHVRARIAELQALEKQLQALRERCDGARTIEECGILQGL
>gnl|CDD|133412 cd04785, HTH_CadR-PbrR-like, Helix-Turn-Helix DNA binding domain of the CadR- and PbrR-like transcription regulators. Helix-turn-helix (HTH) CadR- and PbrR-like transcription regulators. CadR and PbrR regulate expression of the cadmium and lead resistance operons, respectively. These proteins are comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the C-terminal domains have three conserved cysteines which comprise a putative metal binding site. Some members in this group have a histidine-rich C-terminal extension. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements
LSIGELARRTGVNVETIRYYESIGLLPEPARTAGGYRLYGAAHVERLRFIRRARDLGFSLEEIRALLALS
DRPDRSCAEADAIARAHLADVRARIADLRRLEAELKRMVAACSGGRVADCRIIEAL
>gnl|CDD|133413 cd04786, HTH_MerR-like_sg7, Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily. Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 7) with a conserved cysteine present in the C-terminal portion of the protein. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
MKIGELAKRSGMAASRIRFYEAEGLLSSVERSANGYRDYPPETVWVLEIISSAQQAGFSLDEIRQLLPAD
ASNWQHDELLAALERKVADIEALEARLAQNKAQLLVLIDLIESKPDEMDCADNARRVMARL
>gnl|CDD|133414 cd04787, HTH_HMRTR_unk, Helix-Turn-Helix DNA binding domain of putative Heavy Metal Resistance transcription regulators. Putative helix-turn-helix (HTH) heavy metal resistance transcription regulators (HMRTR), unknown subgroup. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to heavy metal stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules, such as, metal ions, drugs, and organic substrates. This subgroup lacks one of the conserved, metal-binding cysteines seen in the MerR1 group
MKVKELANAAGVTPDTVRFYTRIGLLRPTRDPVNGYRLYSEKDLSRLRFILSARQLGFSLKDIKEILSHA
DQGESPCPMVRRLIEQRLAETERRIKELLKLRDRMQQAVSQWQQMPDGAPDGHSICHLIESFV
>gnl|CDD|133415 cd04788, HTH_NolA-AlbR, Helix-Turn-Helix DNA binding domain of the transcription regulators NolA and AlbR. Helix-turn-helix (HTH) transcription regulators NolA and AlbR, N-terminal domain. In Bradyrhizobium (Arachis) sp. NC92, NolA is required for efficient nodulation of host plants. In Xanthomonas albilineans, AlbR regulates the expression of the pathotoxin, albicidin. These proteins are putatively comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the C-terminal domains are often unrelated and bind specific coactivator molecules. They share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements
WKIGELARRTGLSVRTLHHYDHIGLLSPSQRTEGGHRLYDRADIRRLHQIIALRRLGFSLREIGRALDGP
DFDPLELLRRQLARLEEQLELATRLR
>gnl|CDD|133416 cd04789, HTH_Cfa, Helix-Turn-Helix DNA binding domain of the Cfa transcription regulator. Putative helix-turn-helix (HTH) MerR-like transcription regulator; the N-terminal domain of Cfa, a cyclopropane fatty acid synthase and other related methyltransferases. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
MYTISELAEKAGISRSTLLYYEKLGLITGTRNANGYRLYPDSDLQRLLLIQQLQAGGLSLKECLACLQGK
LTRSLLLERLSSLAEQIARKQQARDLLAALLG
>gnl|CDD|133417 cd04790, HTH_Cfa-like_unk, Helix-Turn-Helix DNA binding domain of putative Cfa-like transcription regulators. Putative helix-turn-helix (HTH) MerR-like transcription regulator; conserved, Cfa-like, unknown proteins (~172 a.a.). The N-terminal domain of these proteins appears to be related to the HTH domain of Cfa, a cyclopropane fatty acid synthase. These Cfa-like proteins have a unique C-terminal domain with conserved histidines (motif HXXFX7HXXF). Based on sequence similarity of the N-terminal domains, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates
MLTISQLARQFGLSRSTLLYYERIGLLSPSARSESNYRLYGERDLERLEQICAYRSAGVSLEDIRSLLQQ
PGDDATDVLRRRLAELNREIQRLRQQQRAIATLLKQPTLLKEQRLVTKEKWVAILKAAGMDEADMRRWHI
EFEKMEPEAHQEFLQSLGIPEDEIERIRAWSK
>gnl|CDD|271199 cd04791, LanC_SerThrkinase, Lanthionine synthetase C-like domain associated with serine/threonine kinases. Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown
GGLNVAYGAAGVLLALHRAGGAVPEELEDWLVRRALRDLSLPPGLYDGLAGIAWVLYELGRREEAERLLD
RALALPLDSLDPSLYSGLAGIGLALLHLARATGDPEFLERAARIAERLAARLREDDPGVYWNDAGAVRAG
LLHGWSGIALFLLRLYEATGDPAYLDLAERALRKDLARCVEDDDGALLQVDEGNRLLPYLCSGSAGIGLV
LLRYLRHRGDDRYRELLEGIARAVRSRFTVQPGLFHGLAGLGLALLDLAAALGDPRYRAAAERHARLLNL
HALPRDGGIAFPGDQLLRLSTDLATGSAGVLLALLRLLHGGRSWLPL
>gnl|CDD|271200 cd04792, LanM-like, Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins. LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB
RTLVLELNVARLEGLLEGETPEERYEYFIEELLSDEGLLELFDEYPVLARLLVTKIRNWVEAIAELLQRL
AADRPELRETFLIGAELGKLTSIELGLGDTHNGGRSVAILTFASGLKLVYKPRSLAIDAAFNELLAWLNS
KGIPLPLRTPKVLDRDGYGWVEFVEHEPCADEEEVERFYRRAGALLALLYLLNGTDLHFENLIASGEHPV
LIDLETLFHPRLPSSDSDNATDEANDKLADSVLRTGLLPTWGFGGGDGGGVDISGLGGGEGQLPPRKVPV
IVNIGTDDMRLEREEVTLPPAKNLPRLNGEIVSPKDYVEDIIEGFREVYRLLLKNKEELLAPLGPLFAGL
KVRVVLRPTQVYAKLLRESTHPDYLRDALDRERLLDRLWLLSEEKPSLKPIIESEIADLLQGDIPYFTTR
PDSRDLIDSDGRVIPDFFEKSGLDRVIERLRNLSEEDLERQLWLIRASLANWIGLDLSDDGEWELSPLGA
DLYDGLSGIALFLAALAALTGDEKYRDLARKALRPLRKLLRDLAADPRSLGIGGFTGLGSILYALSHLAR
LLGDPELLEDALELADLLTEAIIEDEELDIIGGSAGAILVLLALYERTGDERALELAIACGDHLLKNAVE
NDGGARWKTPASSRPLTGFAHGAAGIAWALLRLAAVTGDERYLEAAKEALAYERSLFDPEEGNWPDRRKR
NNSFSAAWCHGAAGIGLARLGLLKILNDDEIEEEIEKALETTLKYGFGNNDSLCHGDLGNLELLLVAAKL
LGDPELQEEAEELAAIVLNRAEEAGGWLCGLPTGVESPGLMTGLSGIGYGLLRLAAPDKLPSVLLL
>gnl|CDD|271201 cd04793, LanC, Cyclases involved in the biosynthesis of lantibiotics. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthinoine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as precursor peptides and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans) in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. Also contains SpaC (the cyclase involved in the biosynthesis of subtilin), NisC, and homologs
SLSSGLPGIALLLSELARLTPDEGWDEKAHQYLEAAIEELNSAGLSLSLFSGLAGLAFALLALSRNGGRY
QNLLSELNEYIDELAEDRLAEAIAREGISPGEYDVISGLSGIGRYLLERPPPADDLLEEILDYLVDLTEP
IIEGGEKVPWPELQPSESEKKAYPSGHFNLGLAHGIAGPLALLALALRRGIEVPGQREAIERIADWLLKW
RQDDDEGWWPTIVFPEELSNGRPPPVPSRDAWCYGDPGIARALLLAGKALGDPELQELAEEALLAALRRP
DELTGLISPTLCHGYAGLLQIARRMYRDTGEPALLAAAEELIDKLLDLYDPDLPFGFYDTGGSITPLDDP
GLLEGAAGIALALLSAITDKEPDWDRA
>gnl|CDD|271202 cd04794, euk_LANCL, Eukaryotic Lanthionine synthetase C-like protein. This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 and LANCL2 (testes-specific adriamycin sensitivity protein) were thought to be peptide-modifying enzyme components in eukaryotic cells. Both proteins are produced in large quantities in the brain and testes and may have role in the immune surveillance of these organs. More recently, they have been associated with signal transduction processes and insulin sensitization. In particular, LANCL2 has been shown to bind abscisic acid (ABA), and this interaction may play a role in signaling pathways triggered by ABA, such as in human granulocytes and rat insulinoma cells. This eukaryotic LANCL family also includes Arabidopsis GCR2
LYTGAAGIAYMFLRLSEQGPDLKALSEDYLELALEYIEASLTELARKGSSRISFLCGDAGILALAAVIYH
ALGDSERDEEFLEQLLELAKEALPLDDGPDELLYGRAGYLYALLFLRKHLGESLEISDAVIKKLVDAILE
SGRQGAKDYRSPPPLMYEWHGKEYLGAAHGLAGILYMLLQAPPLLQIPSLAPLIKETLDYLLSLQFPSGN
WPSSLGERSRSDRLVQWCHGAPGVVYLLAKAYKVFLDPKYLEAAIRAGELVWERGLLRKGPGLCHGIAGN
AYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLTGARTPDRPYSLFEGLAGTACFLADLLQGPRKARFP
>gnl|CDD|240112 cd04795, SIS, SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars
IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLLRKGDVVIALSYSGRTEELLAALEIA
KELGIPVIAITDALAVS
>gnl|CDD|341401 cd04801, CBS_pair_peptidase_M50, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
DIMTPEVVTVTPEMTVSELLDRMFEEKHLGYPVVENGRLVGIVTLEDIRKVPEVEREATRVRDVMTKDVI
TVSPDADAMEALKLMSQNNIGRLPVVEDGELVGIISRTDLMRA
>gnl|CDD|240117 cd04813, PA_1, PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. Proteins in this subgroup contain a RING-finger (Really Interesting New Gene) domain C-terminal to this PA domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins in this group contain a C-terminal RING-finger domain. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases: such as hSPPL2a and 2b, ii) various E3 ubiquitin ligases similar to human GRAIL (gene related to anergy in lymphocytes) protein, iii) various proteins containing a RING finger motif such as Arabidopsis ReMembR-H2 protein, iv) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), v) various plant vacuolar sorting receptors such as Pisum sativum BP-80, vi) prostate-specific membrane antigen (PSMA), vii) yeast aminopeptidase Y viii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, ix) various subtilisin-like proteases such as Cucumisin from the juice of melon fruits, and x) human TfR (transferrin receptor) 1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup
PLIGGRYASFSPILNPHLRGSYKVSPTDACSLQEHAEIDGKVALVLRGGCGFLDKVMWAQRRGAKAVIVG
DDEPGRGLITMFSNGDTDNVTIPAMFTSRTSYHLLSSLLPKSLILES
>gnl|CDD|240118 cd04814, PA_M28_1, PA_M28_1: Protease-associated (PA) domain, peptidase family M28, subfamily-1. A subfamily of PA-domain containing proteins belonging to the peptidase family M28. Family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following members of the peptidase family M28: i) prostate-specific membrane antigen (PSMA), ii) yeast aminopeptidase Y, and ii) human TfR (transferrin receptor)1 and human TfR2. The proteins listed above belong to other subfamilies, relatively little is known about proteins in this subfamily
PLAQIAIRAAMLNVDAVAIKDAPLVFVGYGIKAPELSWDDYAGLDVKGKVVVVLRNDPQGEPGAGDFGGK
AMTYYGRWTYKYEEAARHGAAGVLIVHELAPASYGWATWKNPAKVHPNLEAAIQRAVAVDLFEASDGLTF
DL
>gnl|CDD|240119 cd04815, PA_M28_2, PA_M28_2: Protease-associated (PA) domain, peptidase family M28, subfamily-2. A subfamily of PA-domain containing proteins belonging to the peptidase family M28. Family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following members of the peptidase family M28: i) prostate-specific membrane antigen (PSMA), ii) yeast aminopeptidase Y, and ii) human TfR (transferrin receptor)1 and human TfR2. The proteins listed above belong to other subfamilies; relatively little is known about proteins in this subfamily
LAILALGGSVATPPEGITAEVVVVKSFDELKAAPAGAVKGKIVFFNQPMVRTQTGSGYGPTVAYRRRGAV
EAAKKGAVAVLIRSIGTDSHRSPHTGMMSYDDGVPKIPAAAISVEDADMLERLAARGKPIRVNL
>gnl|CDD|240120 cd04816, PA_SaNapH_like, PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
VFVVSLSYSPSTPPGGVTAPLVPLDPERPAGCDASDYDGLDVKGAIVLVDRGGCPFADKQKVAAARGAVA
VIVVNNSDGGGTAGTLGAPNIDLKVPVGVITKAAGAALRRRLGAGETLELDA
>gnl|CDD|240121 cd04817, PA_VapT_like, PA_VapT_like: Protease-associated domain containing proteins like VapT from Vibrio metschnikovii strain RH530. This group contains various PA domain-containing proteins similar to V. metschnikovii VapT, including the serine alkaline protease SapSh from the psychotroph Shewanella strain Ac10 and the Apa1 protease from the psychrotroph Pseudoalteromonas Sp. As-11. VapT is a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease showing high activity over a broad pH range and temperature. SapSh has a high level of protease activity at low temperatures. Apa1 is also cold-adapted. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate
EITAGGSTYFARGVVPHNRLIASGTSYASMPVTGSATGSLYYCGTSGGSYICGGMAGKICLIERGGNSKS
VYPEIDKVKACQNAGAIAAIVYSNAALAGLQNPFLVDTNNDTTIPSVSVDRADGQALLAALGQSTTVST
>gnl|CDD|240122 cd04818, PA_subtilisin_1, PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. A subgroup of PA domain-containing subtilisin-like proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following subtilisin-like proteases: i) melon cucumisin, ii) Arabidopsis thaliana Ara12, iii) Alnus glutinosa ag12, iv) members of the tomato P69 family, and v) tomato LeSBT2. However, these proteins belong to other subtilisin-like subgroups. Relatively little is known about proteins in this subgroup
VSAGFGPALTNVTADVVLAGAAPASNTDGCTAFTNAAAFAGKIALIDRGTCNFTVKVLNAQNAGAIAVIV
ANNVAGGAPITMGGDDPDITIPAVMISQADGDALKAALAAGGTVTVTL
>gnl|CDD|240123 cd04819, PA_2, PA_2: Protease-associated (PA) domain subgroup 2. A subgroup of PA-domain containing proteins. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins in this group contain a C-terminal RING-finger domain. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases: such as hSPPL2a and 2b, ii) various E3 ubiquitin ligases similar to human GRAIL (gene related to anergy in lymphocytes) protein, iii) various proteins containing a RING finger motif such as Arabidopsis ReMembR-H2 protein, iv) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), v) various plant vacuolar sorting receptors such as Pisum sativum BP-80, vi) prostate-specific membrane antigen (PSMA), vii) yeast aminopeptidase Y viii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, ix) various subtilisin-like proteases such as Cucumisin from the juice of melon fruits, and x) human TfR (transferrin receptor) 1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup
CALSGGDLAFDAIALPRSPSGEAKGEPVDAGYGLPKDFDGLDLEGKIAVVKRDDPDVDRKEKYAKAVAAG
AAAFVVVNTVPGVLPATGDEGTEDGPPSPIPAASVSGEDGLRLARVAERNDTLVLRV
>gnl|CDD|240124 cd04820, PA_M28_1_1, PA_M28_1_1: Protease-associated (PA) domain, peptidase family M28, subfamily-1, subgroup 1. A subgroup of PA-domain containing proteins belonging to the peptidase family M28. Family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following members of the peptidase family M28: i) prostate-specific membrane antigen (PSMA), ii) yeast aminopeptidase Y, and ii) human TfR (transferrin receptor)1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup
VPLTLGKDLLIGASAAEPAASVEAPLVFVGYGLVAPELGHDDYAGLDVKGKIVVVLSGGPAGIPSEEGAH
AHSSNEKARYAAKAGAIGMITLTTPRSEKIRPWERSVNYADGPSMTWADAAGAAFDRAPGLKSSAPL
>gnl|CDD|240125 cd04821, PA_M28_1_2, PA_M28_1_2: Protease-associated (PA) domain, peptidase family M28, subfamily-1, subgroup 2. A subgroup of PA-domain containing proteins belonging to the peptidase family M28. Family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following members of the peptidase family M28: i) prostate-specific membrane antigen (PSMA), ii) yeast aminopeptidase Y, and ii) human TfR (transferrin receptor)1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup
SLDQGQDVVAWTRTGQDEVSLKDSPLVFVGYGIVAPEYGWDDYKGLDVKGKTVVILVNDPGFATPDSGLF
NGKAMTYYGRWTYKYEEAARQGAAGALIVHETEPASYGWSVVQSSWTGEQFDLVRANPGAPRVKVEGWIQ
RDAAVKLFALAGLDLDE
>gnl|CDD|240126 cd04822, PA_M28_1_3, PA_M28_1_3: Protease-associated (PA) domain, peptidase family M28, subfamily-1, subgroup 3. A subgroup of PA-domain containing proteins belonging to the peptidase family M28. Family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following members of the peptidase family M28: i) prostate-specific membrane antigen (PSMA), ii) yeast aminopeptidase Y, and ii) human TfR (transferrin receptor)1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup
KTLELEKDFVPFAFSRSGAVTAPVVFAGYGITAPELGYDDYAGLDVKGKIVLVLRHEPQEDDANSRFNGP
GLTRHAGLRYKATNARRHGAAAVIVVNGPNSHSGDADRLPRFGGTAPQRVDIAAADPWFTAAEAAGKDLT
SLQMASFAGDA
>gnl|CDD|240127 cd04823, ALAD_PBGS_aspartate_rich, Porphobilinogen synthase (PBGS), which is also called delta-aminolevulinic acid dehydratase (ALAD), catalyzes the condensation of two 5-aminolevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (PBG), which is the second step in the biosynthesis of tetrapyrroles, such as heme, vitamin B12 and chlorophyll. This reaction involves the formation of a Schiff base link between the substrate and the enzyme. PBGSs are metalloenzymes, some of which have a second, allosteric metal binding site, beside the metal ion binding site in their active site. Although PBGS is a family of homologous enzymes, its metal ion utilization at catalytic site varies between zinc and magnesium and/or potassium. PBGS can be classified into two groups based on differences in their active site metal binding site. All of PBGS_aspartate_rich contain an aspartate rich metal binding site with the general sequence DXALDX(Y/F)X3G(H/Q)DG. They also contain an allosteric magnesium binding sequence RX~164DX~65EXXXD and are activated by magnesium and/or potassium, but not by zinc. PBGSs_aspartate_rich are found in some bacterial species and photosynthetic organisms such as vascular plants, mosses and algae, but not in archaea
TRPRRNRRTDALRRLVRETTLSPDDLILPLFVHEGENQREPIPSMPGVFRLSIDELLKEAEEAVDLGIPA
VALFPVTPPELKSEDGSEAYNPDNLVCRAIRAIKEAFPELGIITDVALDPYTSHGHDGIVRDGGILNDET
VEVLCKQALVQAEAGADIVAPSDMMDGRIGAIREALDAEGFTNVSILSYAAKYASAFYGPFRDALGSAPR
KGDKKTYQMDPANSREALREVALDIAEGADMVMVKPGMPYLDIIRRVKDEFGVPTFAYQVSGEYAMLKAA
AQNGWLDEDKVMLESLLAFKRAGADGILTYFAKEAAEWLR
>gnl|CDD|240128 cd04824, eu_ALAD_PBGS_cysteine_rich, Porphobilinogen synthase (PBGS), which is also called delta-aminolevulinic acid dehydratase (ALAD), catalyzes the condensation of two 5-aminolevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (PBG), which is the second step in the biosynthesis of tetrapyrroles, such as heme, vitamin B12 and chlorophyll. This reaction involves the formation of a Schiff base link between the substrate and the enzyme. PBGSs are metalloenzymes, some of which have a second, allosteric metal binding site, beside the metal ion binding site in their active site. Although PBGS is a family of homologous enzymes, its metal ion utilization at catalytic site varies between zinc and magnesium and/or potassium. PBGS can be classified into two groups based on differences in their active site metal binding site. The eukaryotic PBGSs represented by this model, which contain a cysteine-rich zinc binding motif (DXCXCX(Y/F)X3G(H/Q)CG), require zinc for their activity, they do not contain an additional allosteric metal binding site and do not bind magnesium
HSGYAHPLLRQWQSERTLTKSNLIYPIFITDNPDAKQPIDSLPGINRYGVNRLEEFLRPLVAKGLRSVIL
FGVPLKPGKDDRSGSAADDEDGPVIQAIKLIREEFPELLIACDVCLCEYTSHGHCGILYEDGTINNEASV
KRLAEVALAYAKAGAHIVAPSDMMDGRVRAIKQALIQAGLGNKVSVMSYSAKFASCLYGPFRDAACSAPS
FGDRRCYQLPPGARGLALRAVERDVSEGADMIMVKPGTPYLDIVREAKDKHPDLPLAVYHVSGEYAMLHA
AAEAGAFDLKRAVLEAMTGFRRAGADIIITYFTPELLDWL
>gnl|CDD|173791 cd04842, Peptidases_S8_Kp43_protease, Peptidase S8 family domain in Kp43 proteases. Kp43 proteases are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Kp43 is topologically similar to kexin and furin both of which are proprotein convertases, but differ in amino acids sequence and the position of its C-terminal barrel. Kp43 has 3 Ca2+ binding sites that differ from the corresponding sites in the other known subtilisin-like proteases. KP-43 protease is known to be an oxidation-resistant protease when compared with the other subtilisin-like proteases
GLGLTGKGQIVGVADTGLDTNHCFFYDPNFNKTNLFHRKIVRYDSLSDTKDDVDGHGTHVAGIIAGKGND
SSSISLYKGVAPKAKLYFQDIGDTSGNLSSPPDLNKLFSPMYDAGARISSNSWGSPVNNGYTLLARAYDQ
FAYNNPDILFVFSAGNDGNDGSNTIGSPATAKNVLTVGASNNPSVSNGEGGLGQSDNSDTVASFSSRGPT
YDGRIKPDLVAPGTGILSARSGGGGIGDTSDSAYTSKSGTSMATPLVAGAAALLRQYFVDGYYPTKFNPS
AALLKALLINSAR
>gnl|CDD|173792 cd04843, Peptidases_S8_11, Peptidase S8 family domain, uncharacterized subfamily 11. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
GINARYAWTKPGGSGQGVTFVDIEQGWNLNHEDLVGNGITLISGLTDQADSDHGTAVLGIIVAKDNGIGV
TGIAHGAQAAVVSSTRVSNTADAILDAADYLSPGDVILLEMQTGGPNNGYPPLPVEYEQANFDAIRTATD
LGIIVVEAAGNGGQDLDAPVYNRGPILNRFSPDFRDSGAIMVGAGSSTTGHTRLAFSNYGSRVDVYGWGE
NVTTTGYGDLQDLGGENQDYTDSFSGTSSASPIVAGAAASIQGIAKQKGGTPLTPIEMRELLTATGT
>gnl|CDD|173793 cd04847, Peptidases_S8_Subtilisin_like_2, Peptidase S8 family domain in Subtilisin-like proteins. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
PIVCVLDSGINRGHPLLAPALAEDDLDSDEPGWTADDLGHGTAVAGLALYGDLTLPGNGLPRPGCRLESV
RVLPPNGENDPELYGDITLRAIRRAVIQNPDIVRVFNLSLGSPLPIDDGRPSSWAAALDQLAAEYDVLFV
VSAGNLGDDDAADGPPRIQDDEIEDPADSVNALTVGAITSDDDITDRARYSAVGPAPAGATTSSGPGSPG
PIKPDVVAFGGNLAYDPSGNAADGDLSLLTTLSSPSGGGFVTVGGTSFAAPLAARLAAGLFAELPELSPE
TIRALLIHSAE
>gnl|CDD|173794 cd04848, Peptidases_S8_Autotransporter_serine_protease_like, Peptidase S8 family domain in Autotransporter serine proteases. Autotransporter serine proteases belong to Peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Autotransporters are a superfamily of outer membrane/secreted proteins of gram-negative bacteria. The presence of these subtilisin-like domains in these autotransporters are may enable them to be auto-catalytic and may also serve to allow them to act as a maturation protease cleaving other outer membrane proteins at the cell surface
TGAGVKVGVIDSGIDLSHPEFAGRVSEASYYVAVNDAGYASNGDGDSHGTHVAGVIAAARDGGGMHGVAP
DATLYSARASASAGSTFSDADIAAAYDFLAASGVRIINNSWGGNPAIDTVSTTYKGSAATQGNTLLAALA
RAANAGGLFVFAAGNDGQANPSLAAAALPYLEPELEGGWIAVVAVDPNGTIASYSYSNRCGVAANWCLAA
PGENIYSTDPDGGNGYGRVSGTSFAAPHVSGAAALLAQKFPWLTADQVRQTLLTTAT
>gnl|CDD|173795 cd04852, Peptidases_S8_3, Peptidase S8 family domain, uncharacterized subfamily 3. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
YQLHTTRSPDFLGLPGAWGGSLLGAANAGEGIIIGVLDTGIWPEHPSFADVGGGPYPHTWPGDCVTGEDF
NPFSCNNKLIGARYFSDGYDAYGGFNSDGEYRSPRDYDGHGTHTASTAAGNVVVNASVGGFAFGTASGVA
PRARIAVYKVCWPDGGCFGSDILAAIDQAIADGVDVISYSIGGGSPDPYEDPIAIAFLHAVEAGIFVAAS
AGNSGPGASTVPNVAPWVTTVAASTLKPDIAAPGVDILAAWTPEGADPGDARGEDFAFISGTSMASPHVA
GVAALLKSAHPDWSPAAIKSALMTTAY
>gnl|CDD|173796 cd04857, Peptidases_S8_Tripeptidyl_Aminopeptidase_II, Peptidase S8 family domain in Tripeptidyl aminopeptidases_II. Tripeptidyl aminopeptidases II are member of the peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Tripeptidyl aminopeptidase II removes tripeptides from the free N terminus of oligopeptides as well as having endoproteolytic activity. Some tripeptidyl aminopeptidases have been shown to cleave tripeptides and small peptides, e.g. angiotensin II and glucagon, while others are believed to be involved in MHC I processing
GLLPKKETGALRFLQKYPEYDGRGVLIAILDTGVDPGAPGLQVTTDGKPKIIDIIDCTGSGDVDTSTVVT
PDDGGIIGGLTGRKLKIPASWKNPSGKYHVGIKNAYDEKKYEDPGPVYDCVVFHDGEHWRAVIDTSETGD
LDSCTVLTNYREEREYATFGEQDLLNYSVNIYDDGNLLSIVTDSGAHGTHVAGIAAAHFPEEPERNGVAP
GAQIVSIKIGDTRLGSMETGTALVRAMIAAIETKCDLINMSYGEATHWPNSGRIIELMNEAVNKHGVIFV
SSAGNNGPALSTVGAPGGTTSSVIGVGAYVSPEMMAAEYSLREKLPGNQYTWSSRGPTADGALGVSISAP
GGAIASVPNWTLQGSQLMNGTSMSSPNACGGIALLLSGLKAEGIPYTPYSVRRALENTAKKL
>gnl|CDD|240129 cd04859, Prim_Pol, Prim_Pol: Primase-polymerase (primpol) domain of the type found in bifunctional replicases from archaeal plasmids, including ORF904 protein of the crenarchaeal plasmid pRN1 from Sulfolobus islandicus (pRN1 primpol). These primpol domains belong to the archaeal/eukaryal primase (AEP) superfamily. This group includes archaeal plasmids and bacteriophage AEPs. The ORF904 protein is a multifunctional protein having ATPase, primase and DNA polymerase activity, and may play a role in the replication of the archaeal plasmid. The pRN1 primpol domain exhibits DNA polymerase and primase activities; a cluster of active site residues (three acidic residues, and a histidine) is required for both these activities. For pRN1 primpol, the primase activity prefers dNTPs to rNTPs; incorporation of dNTPs requires rNTP as cofactor. The pRN1 primpol contains an unusual zinc-binding stem, which is not conserved in other members of this group
FAVIPLDPGSKRPLIKGWPKDAATTDPEQIEAWWRDGPDANIGLRTGPSGLVVIDIDVKHDGAAALAALA
ELGKLPPLTLTVRTGSGGRHLYFRVPDGVPVKSVKGKGGPGIDIRGGGGYVVAPPSVHPGGGYYVWKSTV
DPAPAPEWLLDL
>gnl|CDD|240130 cd04860, AE_Prim_S, AE_Prim_S: primase domain similar to that found in the small subunit of archaeal and eukaryotic (A/E) DNA primases. Primases are DNA-dependent RNA polymerases which synthesis the short RNA primers required for DNA replication. In addition to its catalytic role in replication, DNA primase may play a role in coupling replication to DNA damage repair and in checkpoint control during S phase. In eukaryotes, this small catalytically active primase subunit (p50) and a larger primase subunit (p60), referred to jointly as the core primase, associate with the B subunit and the DNA polymerase alpha subunit in a complex, called Pol alpha-pri. The function of the larger primase subunit is unclear. Included in this group are Pfu41 and Pfu46, these two proteins comprise the primase complex of the archaea Pyrococcus furiosus; Pfu41 and Pfu46 have sequence identity to the eukaryotic p50 and p60 primase proteins respectively. Pfu41 preferentially uses dNTPs as substrate. Pfu46 regulates the primase activity of Pfu41
PSLFRYYYLNYGLEIPDYLENREFGFTLFDGVYIRHLSFSSAEELRKYLLRNVPRAVYSSSAYYRKPSAK
GEKGWLGRELVFDIDADDYDDVRTCCSGATICEKCWKFAKEAVKILDDILREDFGFKHILWVFSGRRGYH
VWVCDEKARKLDSDERREIVDYLNGIGLNEDKIKKVKVNLGRPLHPGIRRALIDENVTKDINRLLRLPFS
LHGKTGLIVVPIDPNELDKFDP
>gnl|CDD|240131 cd04861, LigD_Pol_like, LigD_Pol_like: Polymerase (Pol) domain of bacterial LigD proteins similar to Pseudomonas aeruginosa (Pae) LigD. The LigD Pol domain belongs to the archaeal/eukaryal primase (AEP) superfamily. In prokaryotes, LigD along with Ku is required for non-homologous end joining (NHEJ)-mediated repair of DNA double-strand breaks (DSB). NHEJ-mediated DNA DSB repair is error-prone. PaeLigD is monomeric, containing an N-terminal phosphoesterase module, a central polymerase (Pol) domain, and a C-terminal ATP-dependent ligase domain. Mycobacterium tuberculosis (Mt)LigD, also found in this group, is monomeric and contains the same modules but these are arranged differently: an N-terminal Pol domain, a central phosphoesterase module, and a C-terminal ligase domain. It has been suggested that LigD Pol contributes to NHEJ-mediated DNA DSB repair in vivo, by filling in short 5'-overhangs with ribonucleotides; the filled in termini would then be sealed by the associated LigD ligase domain, resulting in short stretches of RNA incorporated into the genomic DNA. The PaeLigD Pol domain in vitro, in a manganese-dependent fashion, catalyzes templated extensions of 5'-overhang duplex DNA, and nontemplated single-nucleotide additions to blunt-end duplex DNA; it preferentially adds single ribonucleotides at blunt DNA ends. PaeLigD Pol adds a correctly paired rNTP to the DNA primer termini more rapidly than it does a correctly paired dNTP; it has higher infidelity as an RNA polymerase than it does as a DNA polymerase, which is in keeping with the mutagenic property of NHEJ-mediated DNA DSB repair. The MtLigD Pol domain similarly is stimulated by manganese, is error-prone, and prefers adding rNTPs to dNTPs in vitro. The MtLigD Pol domain has been shown to prefer DNA gapped substrates containing a 5'-phosphate group at the gap
KGDLADYYAAVAPYMLPHLRGRPLTLVRYPDGIDGESFFQKHAPAGAPDWVRTVEVESEGGTINYLLVND
AAGLVWLANLGAIELHPWLSRADDLERPDRLVFDLDPGPGVPFEDVVEAALLLRELLDELGLESFPKTSG
GKGLHVYVPLAPRYTWDEVRAFAKALARELARRLPDLFTAEMAKAKRGGKIFVDYLQNARGKTTVAPYSV
RARPGAPVSTPLTWDEL
>gnl|CDD|240132 cd04862, PaeLigD_Pol_like, PaeLigD_Pol_like: Polymerase (Pol) domain of bacterial LigD proteins similar to Pseudomonas aeruginosa (Pae) LigD. The LigD Pol domain belongs to the archaeal/eukaryal primase (AEP) superfamily. In prokaryotes, LigD along with Ku is required for non-homologous end joining (NHEJ)-mediated repair of DNA double-strand breaks (DSB). NHEJ-mediated DNA DSB repair is error-prone. PaeLigD is monomeric, containing an N-terminal phosphoesterase module, a central polymerase (Pol) domain, and a C-terminal ATP-dependent ligase domain. It has been suggested that LigD Pol contributes to NHEJ-mediated DNA DSB repair in vivo, by filling in short 5'-overhangs with ribonucleotides; the filled in termini would then be sealed by the associated LigD ligase domain, resulting in short stretches of RNA incorporated into the genomic DNA. The PaeLigD Pol domain in vitro, in a manganese-dependent fashion, catalyzes templated extensions of 5'-overhang duplex DNA, and nontemplated single-nucleotide additions to blunt-end duplex DNA; it preferentially adds single ribonucleotides at blunt DNA ends. PaeLigD Pol adds a correctly paired rNTP to the DNA primer termini more rapidly than it does a correctly paired dNTP; it has higher infidelity as an RNA polymerase than it does as a DNA polymerase, which is in keeping with the mutagenic property of NHEJ-mediated DNA DSB repair
KLDLARYYAAVAPWMLPHLAGRPLSLVRCPDGIGGECFFQKHAGAGLPPGVEQLEIEESGGTEPYLYIED
AEGLLALVQMGVLEFHTWGARIDRLERPDRIVFDLDPGPGVPWKAVVEAALLVRELLDELGLESFVKTSG
GKGLHVVVPLAPRAGWDEVKAFAKALAQHLARTNPDRFVATMGKAKRVGKIFIDYLRNGRGATAVAPYSV
RARPGAPVSVPVTWDEL
>gnl|CDD|240133 cd04863, MtLigD_Pol_like, MtLigD_Pol_like: Polymerase (Pol) domain of bacterial LigD proteins similar to Mycobacterium tuberculosis (Mt)LigD. The LigD Pol domain belongs to the archaeal/eukaryal primase (AEP) superfamily. In prokaryotes, LigD along with Ku is required for non-homologous end joining (NHEJ)-mediated repair of DNA double-strand breaks (DSB). NHEJ-mediated DNA DSB repair is error-prone. MtLigD is monomeric and contains an N-terminal Pol domain, a central phosphoesterase module, and a C-terminal ligase domain. It has been suggested that LigD Pol contributes to NHEJ-mediated DNA DSB repair in vivo, by filling in short 5'-overhangs with ribonucleotides; the filled in termini would then be sealed by the associated LigD ligase domain, resulting in short stretches of RNA incorporated into the genomic DNA. The MtLigD Pol domain is stimulated by manganese, is error-prone, and prefers adding rNTPs to dNTPs in vitro. The MtLigD Pol domain has been shown to prefer DNA gapped substrates containing a 5'-phosphate group at the gap
KGDVLDYYARVAPVLLPHLAGRPVTRKRWPDGVDGPFFFEKNCPSGAPDWLPTAEVRSEGSGTLTYPLVN
DLATLAWAANLAALELHVPQWTVDADGNPGPPDRLVFDLDPGEPAGLVECARVALWLRDRLAALGLASFP
KTSGSKGLHLYVPLDGPVSSDQTKEFAKALARELEREHPDLVVSRMTKSLRAGKVFVDWSQNDAAKTTIA
PYSLRAREVPTVATPVTWDEV
>gnl|CDD|240134 cd04864, LigD_Pol_like_1, LigD_Pol_like_1: Polymerase (Pol) domain of mostly bacterial LigD proteins similar to Pseudomonas aeruginosa (Pae) LigD, subgroup 1. The LigD Pol domain belongs to the archaeal/eukaryal primase (AEP) superfamily. In prokaryotes, LigD along with Ku is required for non-homologous end joining (NHEJ)-mediated repair of DNA double-strand breaks (DSB). NHEJ-mediated DNA DSB repair is error-prone. It has been suggested that LigD Pol contributes to NHEJ-mediated DNA DSB repair in vivo, by filling in short 5'-overhangs with ribonucleotides; the filled in termini would then be sealed by the associated LigD ligase domain, resulting in short stretches of RNA incorporated into the genomic DNA. The Pol domains of PaeLigD and Mycobacterium tuberculosis (Mt)LigD are stimulated by manganese, are error-prone, and prefer adding rNTPs to dNTPs in vitro; however PaeLigD and MtLigD belong to other subgroups, proteins in this subgroup await functional characterization
KGDLVDYYRAVAPVMLPHVRGRPITLERFPDGIGKPGFYQKEAPEHFPDWIERVEVPKRGDGGSVHHVLC
DDAATLVYLADQASITPHVWLSRADDLEHPDLMVFDLDPSADDIEAVRTAALAVRELLDELGLPSFVKTT
GSRGFHVVVPLDGRGDFDDVRAFAAEAADALAKRDPDLLTTEARKAKRGDRVFLDIGRNAYGQTAVAPYA
VRARPGAPVAAPITWAEL
>gnl|CDD|240135 cd04865, LigD_Pol_like_2, LigD_Pol_like_2: Polymerase (Pol) domain of bacterial LigD proteins similar to Pseudomonas aeruginosa (Pae) LigD, subgroup 2. The LigD Pol domain belongs to the archaeal/eukaryal primase (AEP) superfamily. In prokaryotes, LigD along with Ku is required for non-homologous end joining (NHEJ)-mediated repair of DNA double-strand breaks (DSB). NHEJ-mediated DNA DSB repair is error-prone. It has been suggested that LigD Pol contributes to NHEJ-mediated DNA DSB repair in vivo, by filling in short 5'-overhangs with ribonucleotides; the filled in termini would then be sealed by the associated LigD ligase domain, resulting in short stretches of RNA incorporated into the genomic DNA. The Pol domains of PaeLigD and Mycobacterium tuberculosis (Mt)LigD are stimulated by manganese, are error-prone, and prefer adding rNTPs to dNTPs in vitro; however PaeLigD and MtLigD belong to other subgroups, proteins in this subgroup await functional characterization
KRDLIRYYRAVAPYLLPYLRDRPLVLKRYPDGIDGKGFYQKDVPAGAPDWLRTVRITSESGRTINYLIVQ
DPAALLWLANLGCIELHPWPSRAGDLDHPDELVIDLDPQPGTSFEDVVEVALLVREVLDELGLRGYPKTS
GARGLHIYVPIAPRYTFEEVRRFAELLAREVERRLPDLATTERWKKERGGRVYLDYLQNARGKTLAAPYS
VRPLPGAPVSTPLEWEEL
>gnl|CDD|240136 cd04866, LigD_Pol_like_3, LigD_Pol_like_3: Polymerase (Pol) domain of bacterial LigD proteins similar to Pseudomonas aeruginosa (Pae) LigD, subgroup 3. The LigD Pol domain belongs to the archaeal/eukaryal primase (AEP) superfamily. In prokaryotes, LigD along with Ku is required for non-homologous end joining (NHEJ)-mediated repair of DNA double-strand breaks (DSB). NHEJ-mediated DNA DSB repair is error-prone. It has been suggested that LigD Pol contributes to NHEJ-mediated repair DSB repair in vivo, by filling in short 5'-overhangs with ribonucleotides; the filled in termini would then be sealed by the associated LigD ligase domain, resulting in short stretches of RNA incorporated into the genomic DNA. The Pol domains of PaeLigD and Mycobacterium tuberculosis (Mt)LigD are stimulated by manganese, are error-prone, and prefer adding rNTPs to dNTPs in vitro; however PaeLigD and MtLigD belong to other subgroups, proteins in this subgroup await functional characterization
KIDYLHYLQEVSPYMLPFLKDRALTVIRYPHGIRGESFFQKNKPDYAPEFVETVMLDEINYIVCNNLETL
VWLGNQLALELHIPFQTIESNKPSEIVFDLDPPSRDHFSLAVEAANLLKEILDALGLTSFVKTSGNKGLQ
VYIPLPDNKFTYDETRLFTEFIAEYLCQQFPELFTTERLKKNRHNRLYLDYVQHAEGKTIIAPYSARGNE
LGTVAAPLYWEEV
>gnl|CDD|340516 cd04867, TGS_YchF_OLA1, TGS (ThrRS, GTPase and SpoT) domain found in the YchF/OLA1 family proteins. The YchF/Ola1 family includes bacterial ribosome-binding ATPase YchF as well as its human homolog Obg-like ATPase 1 (OLA1), both of which belong to the Obg family of GTPases, and are novel ATPases that bind and hydrolyze ATP more efficiently than GTP. They have been associated with various cellular processes and pathologies, including DNA repair, tumorigenesis, and apoptosis, in addition to the regulation of the oxidative stress response. OLA1 is also termed DNA damage-regulated overexpressed in cancer 45 (DOC45), or GTP-binding protein 9 (GTPBP9). It is over-expressed in several human malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus. It is linked to the cellular stress response and tumorigenesis, and may also serve as a valuable tumor marker. Members in this family contain a central Obg-type G (guanine nucleotide-binding) domain, flanked by a coiled-coil domain and this TGS (ThrRS, GTPase, SpoT) domain of unknown function
LNLITFFTAGPDEVRAWTIRKGTKAPQAAGVIHTDFEKGFIRAEVIKYDDLKELGSEAAAKEAGKYRQEG
KDYVVQDGDIIHFKF
>gnl|CDD|153140 cd04868, ACT_AK-like, ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). This CD includes each of two ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). Typically, AK consists of two ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. Aspartokinase is the first enzyme in the pathway of the biosynthesis of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. One mechanism for the regulation of this pathway is by the production of several isoenzymes of aspartokinase with different repressors and allosteric inhibitors. Pairs of ACT domains are proposed to specifically bind amino acids leading to allosteric regulation of the enzyme. In Escherichia coli (EC), three different aspartokinase isoenzymes are regulated specifically by lysine, methionine, and threonine. AK-HSDHI (ThrA) and AK-HSDHII (MetL) are bifunctional enzymes that consist of an N-terminal AK and a C-terminal homoserine dehydrogenase (HSDH). ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. The third isoenzyme, AKIII (LysC), is monofunctional and is involved in lysine synthesis. The three Bacillus subtilis (BS) isoenzymes, AKI (DapG), AKII (LysC), and AKIII (YclM), are feedback inhibited by meso-diaminopimelate, lysine, and lysine plus threonine, respectively. The E. coli lysine-sensitive AK is described as a homodimer, whereas, the B. subtilis lysine-sensitive AK is described as is a heterodimeric complex of alpha- and beta- subunits that are formed from two in-frame overlapping genes. A single AK enzyme type has been described in Pseudomonas, Amycolatopsis, and Corynebacterium, and apparently, unique to cyanobacteria, are aspartokinases with two tandem pairs of ACT domains, C-terminal to the catalytic domain. The fungal aspartate pathway is regulated at the AK step, with L-Thr being an allosteric inhibitor of the Saccharomyces cerevisiae AK (Hom3). At least two distinct AK isoenzymes can occur in higher plants, a monofunctional lysine-sensitive isoenzyme, which is involved in the overall regulation of the pathway and can be synergistically inhibited by S-adenosylmethionine. The other isoenzyme is a bifunctional, threonine-sensitive AK-HSDH protein. Also included in this AK family CD are the ACT domains of the Methylomicrobium alcaliphilum AK; the first enzyme of the ectoine biosynthetic pathway found in this bacterium and several other halophilic/halotolerant bacteria. Members of this CD belong to the superfamily of ACT regulatory domains
AKVSIVGVGMRGTPGVAAKIFSALAEAGINVDMISQSESEVNISFTVDESDLEKAVKALH
>gnl|CDD|153141 cd04869, ACT_GcvR_2, ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, and other related domains. This CD includes the second of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, and other related domains. The glycine cleavage enzyme system in Escherichia coli provides one-carbon units for cellular methylation reactions. This enzyme system, encoded by the gcvTHP operon and lpd gene, catalyzes the cleavage of glycine into CO2 + NH3 and transfers a one-carbon unit to tetrahydrofolate, producing 5,10-methylenetetrahydrofolate. The gcvTHP operon is activated by the GcvA protein in response to glycine and repressed by a GcvA/GcvR interaction in the absence of glycine. It has been proposed that the co-activator glycine acts through a mechanism of de-repression by binding to GcvR and preventing GcvR from interacting with GcvA to block GcvA's activator function. Evidence also suggests that GcvR interacts directly with GcvA rather than binding to DNA to cause repression. Members of this CD belong to the superfamily of ACT regulatory domains
VVEVVGNDRPGIVHEVTQFLAQRNINIEDLSTETYSAPMSGTPLFKAQATLALPAGTDLDALREELEELC
DDLNVDISLEP
>gnl|CDD|153142 cd04870, ACT_PSP_1, CT domains found N-terminal of phosphoserine phosphatase (PSP, SerB). The ACT_PSP_1 CD includes the first of the two ACT domains found N-terminal of phosphoserine phosphatase (PSP, SerB). PSPs belong to the L-2-haloacid dehalogenase-like protein superfamily. PSP is involved in serine metabolism; serine is synthesized from phosphoglycerate through sequential reactions catalyzed by 3-phosphoglycerate dehydrogenase (SerA), 3-phosphoserine aminotransferase (SerC), and SerB. Members of this CD belong to the superfamily of ACT regulatory domains
LITVTGPDRPGLTSALTEVLAAHGVRILDVGQAVIHGRLSLGILVQIPDSADSEALLKDLLFKAHELGLQ
VRFEP
>gnl|CDD|153143 cd04871, ACT_PSP_2, ACT domains found N-terminal of phosphoserine phosphatase (PSP, SerB). The ACT_PSP_2 CD includes the second of the two ACT domains found N-terminal of phosphoserine phosphatase (PSP, SerB). PSPs belong to the L-2-haloacid dehalogenase-like protein superfamily. PSP is involved in serine metabolism; serine is synthesized from phosphoglycerate through sequential reactions catalyzed by 3-phosphoglycerate dehydrogenase (SerA), 3-phosphoserine aminotransferase (SerC), and SerB. Members of this CD belong to the superfamily of ACT regulatory domains
IVTLLGRPLTAEQLAAVTRVVADQGLNIDRIRRLSGRVPLEEQDDSPKACVEFSVRGQPADLEALRAALL
ELASELNVDIAFQR
>gnl|CDD|153144 cd04872, ACT_1ZPV, ACT domain proteins similar to the yet uncharacterized Streptococcus pneumoniae ACT domain protein. This CD, ACT_1ZPV, includes those single ACT domain proteins similar to the yet uncharacterized Streptococcus pneumoniae ACT domain protein (pdb structure 1ZPV). Members of this CD belong to the superfamily of ACT regulatory domains
KAVITVVGKDRVGIVAGVSTKLAELNVNILDISQTIMDGYFTMIMIVDISESNLDFAELQEELEELGKEL
GVKIRIQHEDIFKAMHRI
>gnl|CDD|153145 cd04873, ACT_UUR-ACR-like, ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD. This ACT domain family, ACT_UUR_ACR-like, includes the two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the four ACT domains of a novel protein composed almost entirely of ACT domain repeats (the ACR protein) and like proteins. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. This CD also includes the first of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein and related domains, as well as, the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains
TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPERIARLEEALEDAL
>gnl|CDD|153146 cd04874, ACT_Af1403, N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid binding protein, Af1403, and related domains. This CD includes the N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid binding protein, Af1403, from Archaeoglobus fulgidus and other related archeal ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains
IALSIIAEDKPGVLRDLTGVIAEHGGNITYTQQFIEREGKARIYMELEGVGDIEELVEELRSLPIVREVE
IH
>gnl|CDD|153147 cd04875, ACT_F4HF-DF, N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase). This CD includes the N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase) which catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formyl-FH4 hydrolase generates the formate that is used by purT-encoded 5'-phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase, a hexamer which is activated by methionine and inhibited by glycine, is proposed to regulate the balance FH4 and C1-FH4 in response to changing growth conditions. Members of this CD belong to the superfamily of ACT regulatory domains
ILTLSCPDRPGIVAAVSGFLAEHGGNIVESDQFVDPDSGRFFMRVEFELEGFDLSREALEAAFAPVAAEF
DMDW
>gnl|CDD|153148 cd04876, ACT_RelA-SpoT, ACT domain found C-terminal of the RelA/SpoT domains. ACT_RelA-SpoT: the ACT domain found C-terminal of the RelA/SpoT domains. Enzymes of the Rel/Spo family enable bacteria to survive prolonged periods of nutrient limitation by controlling guanosine-3'-diphosphate-5'-(tri)diphosphate ((p)ppGpp) production and subsequent rRNA repression (stringent response). Both the synthesis of (p)ppGpp from ATP and GDP(GTP), and its hydrolysis to GDP(GTP) and pyrophosphate, are catalyzed by Rel/Spo proteins. In Escherichia coli and its close relatives, the metabolism of (p)ppGpp is governed by two homologous proteins, RelA and SpoT. The RelA protein catalyzes (p)ppGpp synthesis in a reaction requiring its binding to ribosomes bearing codon-specified uncharged tRNA. The major role of the SpoT protein is the breakdown of (p)ppGpp by a manganese-dependent (p)ppGpp pyrophosphohydrolase activity. Although the stringent response appears to be tightly regulated by these two enzymes in E. coli, a bifunctional Rel/Spo protein has been discovered in most gram-positive organisms studied so far. These bifunctional Rel/Spo homologs (rsh) appear to modulate (p)ppGpp levels through two distinct active sites that are controlled by a reciprocal regulatory mechanism ensuring inverse coupling of opposing activities. In studies with the Streptococcus equisimilis Rel/Spo homolog, the C-terminal domain appears to be involved in this reciprocal regulation of the two opposing catalytic activities present in the N-terminal domain, ensuring that both synthesis and degradation activities are not coinduced. Members of this CD belong to the superfamily of ACT regulatory domains
IRVEAIDRPGLLADITTVIAEEKINILSVNTRTDDDGLATIRLTLEVRDLEHLARIMRKLRQIPGVIDVR
R
>gnl|CDD|153149 cd04877, ACT_TyrR, N-terminal ACT domain of the TyrR protein. ACT_TyrR: N-terminal ACT domain of the TyrR protein. The TyrR protein of Escherichia coli controls the expression of a group of transcription units (TyrR regulon) whose gene products are involved in the biosynthesis or transport of the aromatic amino acids. Binding to specific DNA sequences known as TyrR boxes, the TyrR protein can either activate or repress transcription at different sigma70 promoters. Its regulatory activity occurs in response to intracellular levels of tyrosine, phenylalanine and tryptophan. The TyrR protein consists of an N-terminal region important for transcription activation with an ATP-independent aromatic amino acid binding site (contained within the ACT domain) and is involved in dimerization; a central region with an ATP binding site, an ATP-dependent aromatic amino acid binding site and is involved in hexamerization; and a helix turn helix DNA binding C-terminal region. In solution, in the absence of cofactors or in the presence of phenylalanine alone, the TyrR protein exists as a dimer. However, in the presence of ATP and tyrosine the TyrR protein self-aggregates to form a hexamer. Members of this CD belong to the superfamily of ACT regulatory domains
MRLEITCEDRLGITQEVLDLLVEHNIDLRGIEIDPKGRIYLNFPTIEFEKLQTLMPEIRRIDGVEDVKTV
PYMP
>gnl|CDD|153150 cd04878, ACT_AHAS, N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid synthase (AHAS). ACT_AHAS: N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid synthase (AHAS). AHAS catalyses the first common step in the biosynthesis of the three branched-chain amino acids. The first step involves the condensation of either pyruvate or 2-ketobutyrate with the two-carbon hydroxyethyl fragment derived from another pyruvate molecule, covalently bound to the coenzyme thiamine diphosphate. Bacterial AHASs generally consist of regulatory and catalytic subunits. The effector (valine) binding sites are proposed to be located in two symmetrically related positions in the interface between a pair of N-terminal ACT domains with the C-terminal domain of IlvH contacting the catalytic dimer. Plants Arabidopsis and Oryza have tandem IlvH subunits; both the first and second ACT domain sequences are present in this CD. Members of this CD belong to the superfamily of ACT regulatory domains
HTLSVLVENEPGVLNRISGLFARRGFNIESLTVGPTEDPGISRITIVVEGDDDVIEQIVKQLNKLVDVLK
VS
>gnl|CDD|153151 cd04879, ACT_3PGDH-like, ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH). ACT_3PGDH-like: The ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with or without an extended C-terminal (xct) region found in various bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback controlled by the end product L-serine in an allosteric manner. In the Escherichia coli homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. This CD also includes the C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillus, and Treponema species. LSD enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in E. coli, and other Enterobacteriales, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains
RLLIVHKDVPGVIGKVGTILGEHGINIAAMQVGRKEKGGIAYMVLDVDSPVPEEVLEELKALPGIIRVRL
I
>gnl|CDD|153152 cd04880, ACT_AAAH-PDT-like, ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH). ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH): Phenylalanine hydroxylases (PAH), tyrosine hydroxylases (TH) and tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. This family of enzymes shares a common catalytic mechanism, in which dioxygen is used by an active site containing a single, reduced iron atom to hydroxylate an unactivated aromatic substrate, concomitant with a two-electron oxidation of tetrahydropterin (BH4) cofactor to its quinonoid dihydropterin form. Eukaryotic AAAHs have an N-terminal ACT (regulatory) domain, a middle catalytic domain and a C-terminal domain which is responsible for the oligomeric state of the enzyme forming a domain-swapped tetrameric coiled-coil. The PAH, TH, and TPH enzymes contain highly conserved catalytic domains but distinct N-terminal ACT domains and differ in their mechanisms of regulation. One commonality is that all three eukaryotic enzymes appear to be regulated, in part, by the phosphorylation of serine residues N-terminal of the ACT domain. Also included in this CD are the C-terminal ACT domains of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme found in plants, fungi, bacteria, and archaea. The P-protein of Escherichia coli (CM-PDT) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains
SLVFSLKNKPGALAKALKVFAERGINLTKIESRPSRKGLWEYEFFVDFEGHIDDPDVKEALEELKRVTED
VKVLG
>gnl|CDD|153153 cd04881, ACT_HSDH-Hom, ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) and related domains. The ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) encoded by the hom gene of Bacillus subtilis and other related sequences. HSDH reduces aspartate semi-aldehyde to the amino acid homoserine, one that is required for the biosynthesis of Met, Thr, and Ile from Asp. Neither the enzyme nor the aspartate pathway is found in the animal kingdom. This mostly bacterial HSDH group has a C-terminal ACT domain and is believed to be involved in enzyme regulation. A C-terminal deletion in the Corynebacterium glutamicum HSDH abolished allosteric inhibition by L-threonine. Members of this CD belong to the superfamily of ACT regulatory domains
YYLRLTVKDKPGVLAKITGILAEHGISIESVIQKEADGGETAPVVIVTHETSEAALNAALAEIEALDAVQ
GVPSVIRVE
>gnl|CDD|153154 cd04882, ACT_Bt0572_2, C-terminal ACT domain of a novel protein composed of just two ACT domains. Included in this CD is the C-terminal ACT domain of a novel protein composed of just two ACT domains, as seen in the yet uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related proteins. Members of this CD belong to the superfamily of ACT regulatory domains
VLAVEVPDKPGGLHEILQILSEEGINIEYMYAFVEKKGGKALLIFRTEDIEKAIEVLQERGVELV
>gnl|CDD|153155 cd04883, ACT_AcuB, C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB. This CD includes the C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB. AcuB is putatively involved in the anaerobic catabolism of acetoin, and related proteins. Studies report the induction of AcuB by nitrate respiration and also by fermentation. Since acetoin can be secreted and later serve as a source of carbon, it has been proposed that, during anaerobic growth when other carbon sources are exhausted, the induction of the AcuB protein results in acetoin catabolism. AcuB-like proteins have two N-terminal tandem CBS domains and a single C-terminal ACT domain. Members of this CD belong to the superfamily of ACT regulatory domains
SSQIEVRVPDRPGQLADIAAIFKDRGVNIVSVLVYPSKEEDNKILVFRVQTMNPRPIIEDLRRAGYEVLW
PN
>gnl|CDD|153156 cd04884, ACT_CBS, C-terminal ACT domain of the cystathionine beta-synthase (CBS) domain protein found in Thermotoga maritima, Tm0935, and delta proteobacteria. This CD includes the C-terminal ACT domain of the cystathionine beta-synthase (CBS) domain protein found in Thermotoga maritima, Tm0935, and delta proteobacteria. This protein has two N-terminal tandem CBS domains and a single C-terminal ACT domain. The CBS domain is found in a wide range of proteins, often in tandem arrangements and together with a variety of other functional domains. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Members of this CD belong to the superfamily of ACT regulatory domains
RFTFLLEDKPGTLKPVVDTLREFNARIISILTAFEDAPDGMRRVFIRVTPMDRSKENELIEELKAKFTVV
YW
>gnl|CDD|153157 cd04885, ACT_ThrD-I, Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase). This CD includes each of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains
FAVTFPERPGALKKFLELLGPPRNITEFHYRNQGGDEARVLVGIQVPDREDLAELKERLEALGYPYVD
>gnl|CDD|153158 cd04886, ACT_ThrD-II-like, C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains. This CD includes the C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains. The Escherichia coli tdcB gene product, ThrD-II, anaerobically catalyzes the pyridoxal phosphate-dependent dehydration of L-threonine and L-serine to ammonia and to alpha-ketobutyrate and pyruvate, respectively. Tetrameric ThrD-II is subject to allosteric activation by AMP, inhibition by alpha-keto acids, and catabolite inactivation by several metabolites of glycolysis and the citric acid cycle. Also included in this CD are N-terminal ACT domains present in smaller (~170 a.a.) archaeal proteins of unknown function. Members of this CD belong to the superfamily of ACT regulatory domains
LRVELPDRPGQLAKLLAVIAEAGANIIEVSHDRAFKTLPLGEVEVELTLETRGAEHIEEIIAALREAGYD
VRR
>gnl|CDD|153159 cd04887, ACT_MalLac-Enz, ACT_MalLac-Enz CD includes the N-terminal ACT domain of putative NAD-dependent malic enzyme 1, Bacillus subtilis YqkI and related domains. The ACT_MalLac-Enz CD includes the N-terminal ACT domain of putative NAD-dependent malic enzyme 1, Bacillus subtilis YqkI, a malolactic enzyme (MalLac-Enz) which converts malate to lactate, and other related ACT domains. The yqkJ product is predicted to convert malate directly to lactate, as opposed to related malic enzymes that convert malate to pyruvate. Members of this CD belong to the superfamily of ACT regulatory domains
TLRLELPNRPGMLGRVTTAIGEAGGDIGAIDLVEQGRDYTVRDITVDAPSEEHAETIVAAVRALPEVKVL
SVSD
>gnl|CDD|153160 cd04888, ACT_PheB-BS, C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway protein described in Bacillus subtilis (BS) PheB (PheB-BS) and related domains. This CD includes the C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway protein described in Bacillus subtilis (BS) PheB (PheB-BS) and other related ACT domains. In B. subtilis, the upstream gene of pheB, pheA encodes prephenate dehydratase (PDT). The presumed product of the pheB gene is chorismate mutase (CM). The deduced product of the B. subtilis pheB gene, however, has no significant homology to the CM portion of the bifunctional CM-PDT of Escherichia coli. The presence of an ACT domain lends support to the prediction that these proteins function as a phenylalanine-binding regulatory protein. Members of this CD belong to the superfamily of ACT regulatory domains
VTLSLLLEHRPGVLSKVLNTIAQVRGNVLTINQNIPIHGRANVTISIDTSTMNGDIDELLEELREIDGVE
KVELVG
>gnl|CDD|153161 cd04889, ACT_PDH-BS-like, C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate. Included in this CD is the C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate, found in Bacillus subtilis (BS) and other Firmicutes, Deinococci, and Bacteroidetes. PDH is the first enzyme in the aromatic amino acid pathway specific for the biosynthesis of tyrosine. This enzyme is feedback inhibited by tyrosine in B. subtilis and other microorganisms. Both phenylalanine and tryptophan have been shown to be inhibitors of this activity in B. subtilis. Bifunctional chorismate mutase-PDH (TyrA) enzymes such as those seen in Escherichia coli do not contain an ACT domain. Also included in this CD is the N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains as seen in the uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains
LSVFVENKPGRLAEVTEILAEAGINIKAISIAETRGEFGILRLIFSDPERAKEVLK
>gnl|CDD|153162 cd04890, ACT_AK-like_1, ACT domains found C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). This CD includes the first of two ACT domains found C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and is the first enzyme in the pathway of the biosynthesis of the aspartate family of amino acids, lysine, threonine, methionine, and isoleucine. This CD, includes the first ACT domain of the Escherichia coli (EC) isoenzyme, AKIII (LysC) and the Arabidopsis isoenzyme, asparate kinase 1, both enzymes monofunctional and involved in lysine synthesis, as well as the the first ACT domain of Bacillus subtilis (BS) isoenzyme, AKIII (YclM), and of the Saccharomyces cerevisiae AK (Hom3). Also included are the first ACT domains of the Methylomicrobium alcaliphilum AK, the first enzyme of the ectoine biosynthetic pathway. Members of this CD belong to the superfamily of ACT regulatory domains
TAIEIFDQLMNGEVGFLRKIFEILEKHGISVDLIPTSENSVTLYLDDSLLPKKLKRLLAELE
>gnl|CDD|153163 cd04891, ACT_AK-LysC-DapG-like_1, ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII and related proteins. This CD includes the N-terminal of the two ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis (BS) strain 168, and the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, as well as, the first and third, of four, ACT domains present in cyanobacteria AK. Also included are the N-terminal of the two ACT domains of the diaminopimelate-sensitive aspartokinase isoenzyme AKI found in Bacilli (Bacillus subtilis strain 168), Clostridia, and Actinobacteria bacterial species. Members of this CD belong to the superfamily of ACT regulatory domains
AQVTIKGVPDKPGVAAKIFSALAEAGINVDMIVQSVSRGGTTDISFTVPKSDLEKALAILE
>gnl|CDD|153164 cd04892, ACT_AK-like_2, ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). This CD includes the second of two ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). The exception in this group, is the inclusion of the first ACT domain of the bifunctional aspartokinase - homoserine dehydrogenase-like enzyme group (ACT_AKi-HSDH-ThrA-like_1) which includes the monofunctional, threonine-sensitive, aspartokinase found in Methanococcus jannaschii and other related archaeal species. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. AK is the first enzyme in the pathway of the biosynthesis of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. One mechanism for the regulation of this pathway is by the production of several isoenzymes of AK with different repressors and allosteric inhibitors. Pairs of ACT domains are proposed to specifically bind amino acids leading to allosteric regulation of the enzyme. In Escherichia coli (EC), three different AK isoenzymes are regulated specifically by lysine, methionine, and threonine. AK-HSDHI (ThrA) and AK-HSDHII (MetL) are bifunctional enzymes that consist of an N-terminal AK and a C-terminal homoserine dehydrogenase (HSDH). ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. The third isoenzyme, AKIII (LysC), is monofunctional and is involved in lysine synthesis. The three Bacillus subtilis (BS) isoenzymes, AKI (DapG), AKII (LysC), and AKIII (YclM), are feedback inhibited by meso-diaminopimelate, lysine, and lysine plus threonine, respectively. The E. coli lysine-sensitive AK is described as a homodimer, whereas, the B. subtilis lysine-sensitive AK is described as is a heterodimeric complex of alpha- and beta- subunits that are formed from two in-frame overlapping genes. A single AK enzyme type has been described in Pseudomonas, Amycolatopsis, and Corynebacterium, and apparently, unique to cyanobacteria, are AKs with two tandem pairs of ACT domains, C-terminal to the catalytic domain. The fungal aspartate pathway is regulated at the AK step, with L-Thr being an allosteric inhibitor of the Saccharomyces cerevisiae AK (Hom3). At least two distinct AK isoenzymes can occur in higher plants, a monofunctional lysine-sensitive isoenzyme, which is involved in the overall regulation of the pathway and can be synergistically inhibited by S-adenosylmethionine. The other isoenzyme is a bifunctional, threonine-sensitive AK-HSDH protein. Also included in this CD are the ACT domains of the Methylomicrobium alcaliphilum AK; the first enzyme of the ectoine biosynthetic pathway found in this bacterium and several other halophilic/halotolerant bacteria. Members of this CD belong to the superfamily of ACT regulatory domains
ALVSVVGAGMRGTPGVAARIFSALAEAGINIIMISQGSSEVNISFVVDEDDADKAVKALHEEFFL
>gnl|CDD|153165 cd04893, ACT_GcvR_1, ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, and other related domains. This CD includes the first of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, and other related domains. The glycine cleavage enzyme system in Escherichia coli provides one-carbon units for cellular methylation reactions. This enzyme system, encoded by the gcvTHP operon and lpd gene, catalyzes the cleavage of glycine into CO2 + NH3 and transfers a one-carbon unit to tetrahydrofolate, producing 5,10-methylenetetrahydrofolate. The gcvTHP operon is activated by the GcvA protein in response to glycine and repressed by a GcvA/GcvR interaction in the absence of glycine. It has been proposed that the co-activator glycine acts through a mechanism of de-repression by binding to GcvR and preventing GcvR from interacting with GcvA to block GcvA's activator function. Evidence also suggests that GcvR interacts directly with GcvA rather than binding to DNA to cause repression. Members of this CD belong to the superfamily of ACT regulatory domains
HLVISALGTDRPGILNELTRAVSESGCNILDSRMAILGTEFALTMLVEGSWDAIAKLEAALPGLARRLDL
TLMMKRT
>gnl|CDD|153166 cd04894, ACT_ACR-like_1, ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). This CD includes the N-terminal ACT domain of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) have been described, however, the ACR-like sequences in this CD are distinct from those characterized. This CD includes the Oryza sativa ACR-like protein (Os05g0113000) encoded on chromosome 5 and the Arabidopsis thaliana predicted gene product, At2g39570. Members of this CD belong to the superfamily of ACT regulatory domains
SVITINCPDKTGLGCDLCRIILEFGLNITRGDDSTDGRWCYIVFWVVPRPPSIKVRWDLLKNRLMSACP
>gnl|CDD|153167 cd04895, ACT_ACR_1, ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). This CD includes the N-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains
CTLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGT
SR
>gnl|CDD|153168 cd04896, ACT_ACR-like_3, ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). This CD includes the third ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) have been described, however, the ACR-like sequences in this CD are distinct from those characterized. This CD includes the Oryza sativa ACR-like protein (Os05g0113000) encoded on chromosome 5 and the Arabidopsis thaliana predicted gene product, At2g39570. Members of this CD belong to the superfamily of ACT regulatory domains
TLLQIRCVDQKGLLYDILRTSKDCNIQISYGRFSSKVKGYREVDLFIVQSDGKKIMDPKKQAALCARLRE
EMVCP
>gnl|CDD|153169 cd04897, ACT_ACR_3, ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). This CD includes the third ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains
YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEA
AIERR
>gnl|CDD|153170 cd04898, ACT_ACR-like_4, ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). This CD includes the C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) have been described, however, the ACR-like sequences in this CD are distinct from those characterized. This CD includes the Oryza sativa ACR-like protein (Os05g0113000) encoded on chromosome 5 and the Arabidopsis thaliana predicted gene product, At2g39570. Members of this CD belong to the superfamily of ACT regulatory domains
NPVELSGKGRPRVFYDITLALKKLGICIFSAEIGRHSTGDRQWEVYRVLLLEHDRLKLGGRQRSKVVDRV
TKTLMGW
>gnl|CDD|153171 cd04899, ACT_ACR-UUR-like_2, C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD and related domains. This ACT domain family, ACT_ACR-UUR-like_2, includes the second of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the second and fourth ACT domains of a novel protein composed almost entirely of ACT domain repeats, the ACR protein. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. Members of this CD belong to the superfamily of ACT regulatory domains
TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPERQEALRAALGEAL
>gnl|CDD|153172 cd04900, ACT_UUR-like_1, ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD and related domains. This ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD is the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains
GTEVFIYTPDRPGLFARIAGALDQLGLNILDARIFTTRDGYALDTFVVLDPDGEPIGERERLARIREALE
DAL
>gnl|CDD|153173 cd04901, ACT_3PGDH, C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in fungi and bacteria. The C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in fungi and bacteria. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In Escherichia coli, the SerA 3PGDH is feedback-controlled by the end product L-serine in an allosteric manner. In the homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. Members of this CD belong to the superfamily of ACT regulatory domains
RILHIHKNVPGVLGQINTILAEHNINIAAQYLQTRGEIGYVVIDIDSEVSEELLEALRAIPGTIRVRLL
>gnl|CDD|153174 cd04902, ACT_3PGDH-xct, C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH). The C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with an extended C-terminal (xct) region from bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback-controlled by the end product L-serine in an allosteric manner. Some 3PGDH enzymes have an additional domain formed by an extended C-terminal region. This additional domain introduces significant asymmetry to the homotetramer. Adjacent ACT (regulatory) domains interact, creating two serine-binding sites, however, this asymmetric arrangement results in the formation of two different and distinct domain interfaces between identical domains in the asymmetric unit. How this asymmetry influences the mechanism of effector inhibition is still unknown. Members of this CD belong to the superfamily of ACT regulatory domains
MLVVRNTDRPGVIGKVGTILGEAGINIAGMQVGRDEPGGEALMVLSVDEPVPDEVLEELRALPGILSAKV
VEL
>gnl|CDD|153175 cd04903, ACT_LSD, C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit. The C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillis, and Treponema species. These enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in Escherichia coli, and other enterobacterials, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains
TLIVVHKDKPGAIAKVTSVLADHEINIAFMRVSRKEKGDQALMVIEVDQPIDEEVIEEIKKIPNIHQVIL
I
>gnl|CDD|153176 cd04904, ACT_AAAH, ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH). ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH): Phenylalanine hydroxylases (PAH), tyrosine hydroxylases (TH) and tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. This family of enzymes shares a common catalytic mechanism, in which dioxygen is used by an active site containing a single, reduced iron atom to hydroxylate an unactivated aromatic substrate, concomitant with a two-electron oxidation of tetrahydropterin (BH4) cofactor to its quinonoid dihydropterin form. PAH catalyzes the hydroxylation of L-Phe to L-Tyr, the first step in the catabolic degradation of L-Phe; TH catalyses the hydroxylation of L-Tyr to 3,4-dihydroxyphenylalanine, the rate limiting step in the biosynthesis of catecholamines; and TPH catalyses the hydroxylation of L-Trp to 5-hydroxytryptophan, the rate limiting step in the biosynthesis of 5-hydroxytryptamine (serotonin) and the first reaction in the synthesis of melatonin. Eukaryotic AAAHs have an N-terminal ACT (regulatory) domain, a middle catalytic domain and a C-terminal domain which is responsible for the oligomeric state of the enzyme forming a domain-swapped tetrameric coiled-coil. The PAH, TH, and TPH enzymes contain highly conserved catalytic domains but distinct N-terminal ACT domains (this CD) and differ in their mechanisms of regulation. One commonality is that all three eukaryotic enzymes are regulated in part by the phosphorylation of serine residues N-terminal of the ACT domain. Members of this CD belong to the superfamily of ACT regulatory domains
TSLIFSLKEEVGALARALKLFEEFGVNLTHIESRPSRRNGSEYEFFVDCEVDRGDLDQLISSLRRVVADV
NILS
>gnl|CDD|153177 cd04905, ACT_CM-PDT, C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme. The C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme, found in plants, fungi, bacteria, and archaea. The P-protein of E. coli (CM-PDT, PheA) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains
KTSIVFTLPNKPGALYDVLGVFAERGINLTKIESRPSKGGLWEYVFFIDFEGHIEDPNVAEALEELKRLT
EFVKVLGSYP
>gnl|CDD|153178 cd04906, ACT_ThrD-I_1, First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase). This CD includes the first of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains
EALLAVTIPERPGSFKKFCELIGPRNITEFNYRYADEKDAHIFVGVSVANGAEELAELLEDLKSAGYEVV
DLSDDELAKTHLRYM
>gnl|CDD|153179 cd04907, ACT_ThrD-I_2, Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase). This CD includes the second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains
ERLFRFEFPERPGALKKFLNELLPKWNITLFHYRNQGSDYGRVLVGIQVPDADLDELKERLDALGYPYQE
ETDNPAYKLFL
>gnl|CDD|153180 cd04908, ACT_Bt0572_1, N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains. Included in this CD is the N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains as seen in the uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related ACT domains. These tandem ACT domain proteins belong to the superfamily of ACT regulatory domains
IKQLSVFLENKPGRLAAVTEILSEAGINIRALSIADTSEFGILRLIVSDPDKAKEALKEAGFAVKL
>gnl|CDD|153181 cd04909, ACT_PDH-BS, C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH). The C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate, found in Bacillus subtilis (BS) and other Firmicutes, Deinococci, and Bacteroidetes. PDH is the first enzyme in the aromatic amino acid pathway specific for the biosynthesis of tyrosine. This enzyme is feedback-inhibited by tyrosine in B. subtilis and other microorganisms. Both phenylalanine and tryptophan have been shown to be inhibitors of this activity in B. subtilis. Bifunctional chorismate mutase-PDH (TyrA) enzymes such as those seen in Escherichia coli do not contain an ACT domain. Members of this CD belong to the superfamily of ACT regulatory domains
FYDLYVDVPDEPGVIAEVTQILGDAGISIKNIEILEIREGIGGILRISFKTQEDRERAKEILKEAGYEV
>gnl|CDD|153182 cd04910, ACT_AK-Ectoine_1, ACT domains located C-terminal to the catalytic domain of the aspartokinase of the ectoine (1,4,5,6-tetrahydro-2-methyl pyrimidine-4-carboxylate) biosynthetic pathway. This CD includes the first of two ACT domains located C-terminal to the catalytic domain of the aspartokinase of the ectoine (1,4,5,6-tetrahydro-2-methyl pyrimidine-4-carboxylate) biosynthetic pathway found in Methylomicrobium alcaliphilum, Vibrio cholerae, and various other halotolerant or halophilic bacteria. Bacteria exposed to hyperosmotic stress accumulate organic solutes called 'compatible solutes' of which ectoine, a heterocyclic amino acid, is one. Apart from its osmotic function, ectoine also exhibits a protective effect on proteins, nucleic acids and membranes against a variety of stress factors. de novo synthesis of ectoine starts with the phosphorylation of L-aspartate and shares its first two enzymatic steps with the biosynthesis of amino acids of the aspartate family: aspartokinase and L-aspartate-semialdehyde dehydrogenase. The M. alcaliphilum and the V. cholerae aspartokinases are encoded on the ectABCask operon. Members of this CD belong to the superfamily of ACT regulatory domains
VFALEVFDQDMVGEVGYDLEILELLQRFKVSIIAKDTNANTITHYLAGSLKTIKRLTEDLENRFPNAEIT
V
>gnl|CDD|153183 cd04911, ACT_AKiii-YclM-BS_1, ACT domains located C-terminal to the catalytic domain of the lysine plus threonine-sensitive aspartokinase isoenzyme AKIII. This CD includes the first of two ACT domains located C-terminal to the catalytic domain of the lysine plus threonine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in Bacilli (Bacillus subtilis (BS) YclM) and Clostridia species. Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. Bacillus subtilis YclM is reported to be a single polypeptide of 50 kD. AKIII from Bacillus subtilis strain 168 is induced by lysine and repressed by threonine and it is synergistically inhibited by lysine and threonine. Members of this CD belong to the superfamily of ACT regulatory domains
FCSIYISKYLMNREVGFGRKLLSILEDNGISYEHMPSGIDDISIIIRDNQLTDEKEQKILAEIKEELHPD
EIEIIH
>gnl|CDD|153184 cd04912, ACT_AKiii-LysC-EC-like_1, ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII. This CD includes the first of two ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in bacteria (Escherichia coli (EC) LysC) and plants, (Zea mays Ask1, Ask2, and Arabidopsis thaliana AK1). Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. Like the A. thaliana AK1 (AK1-AT), the E. coli AKIII (LysC) has two bound feedback allosteric inhibitor lysine molecules at the dimer interface located between the ACT1 domain of two subunits. The lysine-sensitive plant isoenzyme is synergistically inhibited by S-adenosylmethionine. A homolog of this group appears to be the Saccharomyces cerevisiae AK (Hom3) which clusters with this group as well. Members of this CD belong to the superfamily of ACT regulatory domains
ITLLNIKSNRMLGAHGFLAKVFEIFAKHGLSVDLISTSEVSVSLTLDPTKNLSDQLLLDALVKDLSQIGD
VEVEE
>gnl|CDD|153185 cd04913, ACT_AKii-LysC-BS-like_1, ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis (BS) strain 168 and related proteins. This CD includes the N-terminal of the two ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis (BS) strain 168, and the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related sequences. In B. subtilis 168, the regulation of the diaminopimelate (Dap)-lysine biosynthetic pathway involves dual control by Dap and lysine, effected through separate Dap- and lysine-sensitive aspartokinase isoenzymes. The B. subtilis 168 AKII is induced by methionine and repressed and inhibited by lysine. Although Corynebacterium glutamicum is known to contain a single aspartokinase, both the succinylase and dehydrogenase variant pathways of DAP-lysine synthesis operate simultaneously in this organism. In corynebacteria and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and threonine. Conserved residues in the ACT domains have been shown to be involved in this concerted feedback inhibition. Also included in this CD are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinases found in Pseudomonas aeruginosa, C. glutamicum, and Amycolatopsis lactamdurans. B. subtilis 168 AKII, and the C. glutamicum, Streptomyces clavuligerus and A. lactamdurans aspartokinases are described as tetramers consisting of two alpha and two beta subunits; the alpha (44 kD) and beta (18 kD) subunits formed by two in-phase overlapping polypeptides. This CD includes the first ACT domain C-terminal to the AK catalytic domain of the alpha subunit and the first ACT domain of the beta subunit that lacks the AK catalytic domain. Unlike the C. glutamicum AK beta subunit, which is involved in feedback regulation, the B. subtilis AKII beta subunit is not. Cyanobacteria aspartokinases are unique to this CD and they have a unique domain architecture with two tandem pairs of ACT domains, C-terminal to the catalytic AK domain. In this CD, the first and third cyanobacteria AK ACT domains are present. Members of this CD belong to the superfamily of ACT regulatory domains
QAKITLRGVPDKPGVAAKIFGALAEANINVDMIVQNVSRDGTTDISFTVPKSDLKKALAVLEKLKKELGA
EEVEY
>gnl|CDD|153186 cd04914, ACT_AKi-DapG-BS_1, ACT domains of the diaminopimelate-sensitive aspartokinase (AK) isoenzyme AKI. This CD includes the N-terminal of the two ACT domains of the diaminopimelate-sensitive aspartokinase (AK) isoenzyme AKI, a monofunctional class enzyme found in Bacilli (Bacillus subtilis (BS) strain 168), Clostridia, and Actinobacteria, bacterial species. In B. subtilis, the regulation of the diaminopimelate-lysine biosynthetic pathway involves dual control by diaminopimelate and lysine, effected through separate diaminopimelate- and lysine-sensitive aspartokinase isoenzymes. AKI activity is invariant during the exponential and stationary phases of growth and is not altered by addition of amino acids to the growth medium. The role of this isoenzyme is most likely to provide a constant level of aspartyl-beta-phosphate for the biosynthesis of diaminopimelate for peptidoglycan synthesis and dipicolinate during sporulation. The B. subtilis AKI is tetrameric consisting of two alpha and two beta subunits; the alpha (43 kD) and beta (17 kD) subunit formed by two in-phase overlapping genes. The alpha subunit contains the AK catalytic domain and two ACT domains. The beta subunit contains two ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains
VTQIKVKAKDNENDLQQRVFKALANAGISVDLINVSPEEVIFTVDGEVAEKAVDILEKMGLDPSVRE
>gnl|CDD|153187 cd04915, ACT_AK-Ectoine_2, ACT domains located C-terminal to the catalytic domain of the aspartokinase of the ectoine (1,4,5,6-tetrahydro-2-methyl pyrimidine-4-carboxylate) biosynthetic pathway. This CD includes the second of two ACT domains located C-terminal to the catalytic domain of the aspartokinase of the ectoine (1,4,5,6-tetrahydro-2-methyl pyrimidine-4-carboxylate) biosynthetic pathway found in Methylomicrobium alcaliphilum, Vibrio cholerae, and various other halotolerant or halophilic bacteria. Bacteria exposed to hyperosmotic stress accumulate organic solutes called 'compatible solutes' of which ectoine, a heterocyclic amino acid, is one. Apart from its osmotic function, ectoine also exhibits a protective effect on proteins, nucleic acids and membranes against a variety of stress factors. de novo synthesis of ectoine starts with the phosphorylation of L-aspartate and shares its first two enzymatic steps with the biosynthesis of amino acids of the aspartate family: aspartokinase and L-aspartate-semialdehyde dehydrogenase. The M. alcaliphilum and the V. cholerae aspartokinases are encoded on the ectABCask operon. Members of this CD belong to the superfamily of ACT regulatory domains
RVAIVSVIGRDLSTPGVLARGLAALAEAGIEPIAAHQSMRNVDVQFVVDRDDYDNAIKALHAALVE
>gnl|CDD|153188 cd04916, ACT_AKiii-YclM-BS_2, ACT domains located C-terminal to the catalytic domain of the lysine plus threonine-sensitive aspartokinase isoenzyme AKIII. This CD includes the second of two ACT domains located C-terminal to the catalytic domain of the lysine plus threonine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in Bacilli (Bacillus subtilis (BS) YclM) and Clostridia species. Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. B. subtilis YclM is reported to be a single polypeptide of 50 kD. AKIII from B. subtilis strain 168 is induced by lysine and repressed by threonine and it is synergistically inhibited by lysine and threonine. Members of this CD belong to the superfamily of ACT regulatory domains
LALIMVVGEGMKNTVGVSARATAALAKAGINIRMINQGSSEISIMIGVHNEDADKAVKAIYEEFFN
>gnl|CDD|153189 cd04917, ACT_AKiii-LysC-EC_2, ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII. This CD includes the second of two ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in bacteria (Escherichia coli (EC) LysC). Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. The E. coli AKIII (LysC) binds two feedback allosteric inhibitor lysine molecules at the dimer interface located between the ACT1 domain of two subunits. The second ACT domain (ACT2), this CD, is not involved in the binding of heterotrophic effectors. Members of this CD belong to the superfamily of ACT regulatory domains
LALVALIGNDISETAGVEKRIFDALEDINVRMICYGASNHNLCFLVKEEDKDEVVQRLHSRLFE
>gnl|CDD|153190 cd04918, ACT_AK1-AT_2, ACT domains located C-terminal to the catalytic domain of a monofunctional, lysine-sensitive, plant aspartate kinase 1 (AK1). This CD includes the second of two ACT domains located C-terminal to the catalytic domain of a monofunctional, lysine-sensitive, plant aspartate kinase 1 (AK1), which can be synergistically inhibited by S-adenosylmethionine (SAM). This isoenzyme is found in higher plants, Arabidopsis thaliana (AT) and Zea mays, and also in Chlorophyta. In its inactive state, Arabidopsis AK1 binds the effectors lysine and SAM (two molecules each) at the interface of two ACT1 domain subunits. The second ACT domain (ACT2), this CD, does not interact with an effector. Members of this CD belong to the superfamily of ACT regulatory domains
RSIISLIGNVQRSSLILERAFHVLYTKGVNVQMISQGASKVNISLIVNDSEAEGCVQALHKSFFE
>gnl|CDD|153191 cd04919, ACT_AK-Hom3_2, ACT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3. This CD includes the second of two ACT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae, and other related ACT domains. AK is the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and in fungi, is responsible for the production of threonine, isoleucine and methionine. S. cerevisiae has a single AK, which is regulated by feedback, allosteric inhibition by L-threonine. Recent studies shown that the allosteric transition triggered by binding of threonine to AK involves a large change in the conformation of the native hexameric enzyme that is converted to an inactive one of different shape and substantially smaller hydrodynamic size. Members of this CD belong to the superfamily of ACT regulatory domains
LAILSLVGKHMKNMIGIAGRMFTTLADHRINIEMISQGASEINISCVIDEKDAVKALNIIHTNLLE
>gnl|CDD|153192 cd04920, ACT_AKiii-DAPDC_2, ACT domains of a bifunctional AKIII (LysC)-like aspartokinase/meso-diaminopimelate decarboxylase (DAPDC). This CD includes the second of two ACT domains of a bifunctional AKIII (LysC)-like aspartokinase/meso-diaminopimelate decarboxylase (DAPDC) bacterial protein. Aspartokinase (AK) is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. The lysA gene encodes the enzyme DAPDC, a pyridoxal-5'-phosphate (PLP)-dependent enzyme which catalyzes the final step in the lysine biosynthetic pathway converting meso-diaminopimelic acid (DAP) to l-lysine. Tandem ACT domains are positioned centrally with the AK catalytic domain N-terminal and the DAPDC domains C-terminal. Members of this CD belong to the superfamily of ACT regulatory domains
AAVSLVGRGIRSLLHKLGPALEVFGKKPVHLVSQAANDLNLTFVVDEDQADGLCARLHFQLIE
>gnl|CDD|153193 cd04921, ACT_AKi-HSDH-ThrA-like_1, ACT domains of the bifunctional enzyme aspartokinase (AK) - homoserine dehydrogenase (HSDH). This CD includes the first of two ACT domains of the bifunctional enzyme aspartokinase (AK) - homoserine dehydrogenase (HSDH). The ACT domains are positioned between the N-terminal catalytic domain of AK and the C-terminal HSDH domain found in bacteria (Escherichia coli (EC) ThrA) and higher plants (Zea mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. HSDH is the first committed reaction in the branch of the pathway that leads to Thr and Met. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains were shown to be involved in allosteric activation. Also included in this CD is the first of two ACT domains of a tetrameric, monofunctional, threonine-sensitive, AK found in Methanococcus jannaschii and other related archaeal species. Members of this CD belong to the superfamily of ACT regulatory domains
VALINIEGTGMVGVPGIAARIFSALARAGINVILISQASSEHSISFVVDESDADKALEALEEEFALEIKA
GLIKPIEVEK
>gnl|CDD|153194 cd04922, ACT_AKi-HSDH-ThrA_2, ACT domains of the bifunctional enzyme aspartokinase (AK) - homoserine dehydrogenase (HSDH). This CD includes the second of two ACT domains of the bifunctional enzyme aspartokinase (AK) - homoserine dehydrogenase (HSDH). The ACT domains are positioned between the N-terminal catalytic domain of AK and the C-terminal HSDH domain found in bacteria (Escherichia coli (EC) ThrA) and higher plants (Zea mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. HSDH is the first committed reaction in the branch of the pathway that leads to Thr and Met. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains were shown to be involved in allosteric activation. Members of this CD belong to the superfamily of ACT regulatory domains
LSILALVGDGMAGTPGVAATFFSALAKANVNIRAIAQGSSERNISAVIDEDDATKALRAVHERFFL
>gnl|CDD|153195 cd04923, ACT_AK-LysC-DapG-like_2, ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis (BS) strain 168 and related domains. This CD includes the C-terminal of the two ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis (BS) strain 168, and the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, as well as, the second and fourth, of four, ACT domains present in cyanobacteria AK. Also included are the C-terminal of the two ACT domains of the diaminopimelate-sensitive aspartokinase isoenzyme AKI found in Bacilli (B. subtilis strain 168), Clostridia, and Actinobacteria bacterial species. Members of this CD belong to the superfamily of ACT regulatory domains
AKVSIVGAGMRSHPGVAAKMFKALAEAGINIEMISTSEIKISCLVDEDDAEKAVRALHEAFEL
>gnl|CDD|153196 cd04924, ACT_AK-Arch_2, ACT domains of a monofunctional aspartokinase found mostly in Archaea species (ACT_AK-Arch_2). Included in this CD is the second of two ACT domains of a monofunctional aspartokinase found mostly in Archaea species (ACT_AK-Arch_2). The first or N-terminal ACT domain of these proteins cluster with the ThrA-like ACT 1 domains (ACT_AKi-HSDH-ThrA-like_1) which includes the threonine-sensitive archaeal Methanococcus jannaschii aspartokinase ACT 1 domain. Members of this CD belong to the superfamily of ACT regulatory domains
VAVVAVVGSGMRGTPGVAGRVFGALGKAGINVIMISQGSSEYNISFVVAEDDGWAAVKAVHDEFGL
>gnl|CDD|153197 cd04925, ACT_ACR_2, ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). This CD includes the second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains
TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDN
VLRG
>gnl|CDD|153198 cd04926, ACT_ACR_4, C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). This CD includes the C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains
GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPA
CL
>gnl|CDD|153199 cd04927, ACT_ACR-like_2, Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). This CD includes the second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) have been described, however, the ACR-like sequences in this CD are distinct from those characterized. This CD includes the Oryza sativa ACR-like protein (Os05g0113000) encoded on chromosome 5 and the Arabidopsis thaliana predicted gene product, At2g39570. Members of this CD belong to the superfamily of ACT regulatory domains
FLLKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTPDGRVLDLFFITDARELLHTKKRREETYDYLRAV
LGDSMI
>gnl|CDD|153200 cd04928, ACT_TyrKc, Uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and other related ACT domains. This CD includes a novel, yet uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and other related ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains
MHEITFAAGDKPKLLSQLSSLLGDLGLNIAEAHAFSTDDGLALDIFVVTGWKRGETAALGHALQKEID
>gnl|CDD|153201 cd04929, ACT_TPH, ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. TPH catalyses the hydroxylation of L-Trp to 5-hydroxytryptophan, the rate limiting step in the biosynthesis of 5-hydroxytryptamine (serotonin) and the first reaction in the synthesis of melatonin. Very little is known about the role of the ACT domain in TPH, which appears to be regulated by phosphorylation but not by its substrate or cofactor. Members of this CD belong to the superfamily of ACT regulatory domains
TSVIFSLKNEVGGLAKALKLFQELGINVVHIESRKSKRRSSEFEIFVDCECDQRRLDELVQLLKREVASV
NMNT
>gnl|CDD|153202 cd04930, ACT_TH, ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tyrosine hydroxylases (TH). ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tyrosine hydroxylases (TH). TH catalyses the hydroxylation of L-Tyr to 3,4-dihydroxyphenylalanine, the rate limiting step in the biosynthesis of catecholamines (dopamine, noradrenaline and adrenaline), functioning as hormones and neurotransmitters. The enzyme is not regulated by its amino acid substrate, but instead by phosphorylation at several serine residues located N-terminal of the ACT domain, and by feedback inhibition by catecholamines at the active site. Members of this CD belong to the superfamily of ACT regulatory domains
KQSLIEDARKEREDASLTEDAEDDLDSEVFEEKEGKAVPQKATLLFSLKEGFSSLSRILKVFETFEAKIH
HLESRPSRKEGGDLEVLVRCEVHRSDLLQLISSLRQVAEDVRLTA
>gnl|CDD|153203 cd04931, ACT_PAH, ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, phenylalanine hydroxylases (PAH). ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, phenylalanine hydroxylases (PAH). PAH catalyzes the hydroxylation of L-Phe to L-Tyr, the first step in the catabolic degradation of L-Phe. In PAH, an autoregulatory sequence, N-terminal of the ACT domain, extends across the catalytic domain active site and regulates the enzyme by intrasteric regulation. It appears that the activation by L-Phe induces a conformational change that converts the enzyme to a high-affinity and high-activity state. Modulation of activity is achieved through inhibition by BH4 and activation by phosphorylation of serine residues of the autoregulatory region. The molecular basis for the cooperative activation process is not fully understood yet. Members of this CD belong to the superfamily of ACT regulatory domains
ESSYIEENSNKNGVISLIFSLKEEVGALAKVLRLFEEKDINLTHIESRPSRLNKDEYEFFINLDKKSAPA
LDPIIKSLRNDIGATVHELS
>gnl|CDD|153204 cd04932, ACT_AKiii-LysC-EC_1, ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII. This CD includes the first of two ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in bacteria (Escherichia coli (EC) LysC). Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. The E. coli AKIII (LysC) binds two feedback allosteric inhibitor lysine molecules at the dimer interface located between the ACT1 domain of two subunits. Members of this CD belong to the superfamily of ACT regulatory domains
QTLVTLKSPNMLHAQGFLAKVFGILAKHNISVDLITTSEISVALTLDNTGSTSDQLLTQALLKELSQICD
VKVEE
>gnl|CDD|153205 cd04933, ACT_AK1-AT_1, ACT domains located C-terminal to the catalytic domain of a monofunctional, lysine-sensitive, plant aspartate kinase 1 (AK1). This CD includes the first of two ACT domains located C-terminal to the catalytic domain of a monofunctional, lysine-sensitive, plant aspartate kinase 1 (AK1), which can be synergistically inhibited by S-adenosylmethionine. This isoenzyme is found in higher plants, Arabidopsis thaliana (AT) and Zea mays, and also in Chlorophyta. Like the Escherichia coli AKIII (LysC), Arabidopsis AK1 binds two feedback allosteric inhibitor lysine molecules at the dimer interface located between the ACT1 domain of two subunits. A loop in common is involved in the binding of both Lys and S-adenosylmethionine providing an explanation for the synergistic inhibition by these effectors. Members of this CD belong to the superfamily of ACT regulatory domains
VTMLDITSTRMLGQYGFLAKVFSIFETLGISVDVVATSEVSISLTLDPSKLWSRELIQQELDHVVEELEK
DAVVNLLV
>gnl|CDD|153206 cd04934, ACT_AK-Hom3_1, CT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae, and other related ACT domains. This CD includes the first of two ACT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae, and other related ACT domains. AK is the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and in fungi, is responsible for the production of threonine, isoleucine and methionine. S. cerevisiae has a single AK, which is regulated by feedback, allosteric inhibition by L-threonine. Recent studies shown that the allosteric transition triggered by binding of threonine to AK involves a large change in the conformation of the native hexameric enzyme that is converted to an inactive one of different shape and substantially smaller hydrodynamic size. Members of this CD belong to the superfamily of ACT regulatory domains
ILVINIHSNKKSLSHGFLARIFAILDKYRLSVDLISTSEVHVSMALHMENAEDTNLDAAVKDLQKLGTVD
ILH
>gnl|CDD|153207 cd04935, ACT_AKiii-DAPDC_1, ACT domains of a bifunctional AKIII (LysC)-like aspartokinase/meso-diaminopimelate decarboxylase (DAPDC) bacterial protein. This CD includes the first of two ACT domains of a bifunctional AKIII (LysC)-like aspartokinase/meso-diaminopimelate decarboxylase (DAPDC) bacterial protein. Aspartokinase (AK) is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. The lysA gene encodes the enzyme DAPDC, a pyridoxal-5'-phosphate (PLP)-dependent enzyme which catalyzes the final step in the lysine biosynthetic pathway converting meso-diaminopimelic acid (DAP) to l-lysine. Tandem ACT domains are positioned centrally with the AK catalytic domain N-terminal and the DAPDC domains C-terminal. Members of this CD belong to the superfamily of ACT regulatory domains
IRLVSMETLGMWQQVGFLADVFAPFKKHGVSVDLVSTSETNVTVSLDPDPNGLDPDVLDALLDDLNQICR
VKIIE
>gnl|CDD|153208 cd04936, ACT_AKii-LysC-BS-like_2, ACT domains of the lysine-sensitive, aspartokinase (AK) isoenzyme AKII of Bacillus subtilis (BS) strain 168 and related domains. This CD includes the C-terminal of the two ACT domains of the lysine-sensitive, aspartokinase (AK) isoenzyme AKII of Bacillus subtilis (BS) strain 168, and the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related sequences. In B. subtilis strain 168, the regulation of the diaminopimelate (Dap)-lysine biosynthetic pathway involves dual control by Dap and lysine, effected through separate Dap- and lysine-sensitive AK isoenzymes. The B. subtilis strain 168 AKII is induced by methionine and repressed and inhibited by lysine. Although C. glutamicum is known to contain a single AK, both the succinylase and dehydrogenase variant pathways of DAP-lysine synthesis operate simultaneously in this organism. In corynebacteria and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and threonine. Conserved residues in the ACT domains have been shown to be involved in this concerted feedback inhibition. Also included in this CD are the AKs of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single AKs found in Pseudomons, C. glutamicum, and Amycolatopsis lactamdurans. B. subtilis strain 168 AKII, and the C. glutamicum, Streptomyces clavuligerus and A. lactamdurans AKs are described as tetramers consisting of two alpha and two beta subunits; the alpha (44 kD) and beta (18 kD) subunits formed by two in-phase overlapping polypeptides. This CD includes the second ACT domain C-terminal to the AK catalytic domain of the alpha subunit and the second ACT domain of the beta subunit that lacks the AK catalytic domain. Unlike the C. glutamicum AK beta subunit, which is involved in feedback regulation, the B. subtilis AKII beta subunit is not. Cyanobacteria AKs are unique to this CD and they have a unique domain architecture with two tandem pairs of ACT domains, C-terminal to the catalytic AK domain. In this CD, the second and fourth cyanobacteria AK ACT domains are present. Members of this CD belong to the superfamily of ACT regulatory domains
AKVSIVGAGMRSHPGVAAKMFEALAEAGINIEMISTSEIKISCLIDEDDAEKAVRALHEAFEL
>gnl|CDD|153209 cd04937, ACT_AKi-DapG-BS_2, ACT domains of the diaminopimelate-sensitive aspartokinase (AK) isoenzyme AKI. This CD includes the C-terminal of the two ACT domains of the diaminopimelate-sensitive aspartokinase (AK) isoenzyme AKI, a monofunctional class enzyme found in Bacilli (Bacillus subtilis (BS) strain 168), Clostridia, and Actinobacteria bacterial species. In B. subtilis, the regulation of the diaminopimelate-lysine biosynthetic pathway involves dual control by diaminopimelate and lysine, effected through separate diaminopimelate- and lysine-sensitive AK isoenzymes. AKI activity is invariant during the exponential and stationary phases of growth and is not altered by addition of amino acids to the growth medium. The role of this isoenzyme is most likely to provide a constant level of aspartyl-beta-phosphate for the biosynthesis of diaminopimelate for peptidoglycan synthesis and dipicolinate during sporulation. The BS AKI is tetrameric consisting of two alpha and two beta subunits; the alpha (43 kD) and beta (17 kD) subunit formed by two in-phase overlapping genes. The alpha subunit contains the AK catalytic domain and two ACT domains. The beta subunit contains two ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains
CAKVTIIGSRIRGVPGVMAKIVGALSKEGIEILQTADSHTTISCLVSEDDVKEAVNALHEAFEL
>gnl|CDD|340517 cd04938, TGS_Obg, TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family. The Obg family of GTPases function has been implicated in cellular processes as diverse as sporulation, stress response, control of DNA replication, and ribosome assembly. It consists of several subfamilies such as DRG and YchF with TGS domain. The TGS domain is named after the various RNA-binding multidomain ThrRS, GTPase, and SpoT/RelA proteins in which this domain occurs. The TGS domain of Obg-like GTPases such as those present in DRG (developmentally regulated GTP-binding protein), and GTP-binding proteins Ygr210 and YchF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions
GLIPVYPVKNIQTFTNGSGNSVFRDCVLVKKGTTVKDFANKIHTDLEKGFINAEGIGGRRLEGEDYILQD
NDVVKFT
>gnl|CDD|240137 cd04939, PA2301, PA2301 is an uncharacterized Pseudomonas aeruginosa protein with a YbaK-like domain of unknown function. The YbaK-like domain family includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, and ProX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express a single-domain INS homolog such as YbaK, ProX, or PrdX which supplies the function of INS in trans
GVLVFAIDPELADTAAFCARYGFGLEDSANCVVVAGKRGGEERYAACVVLATTRADVNGVVKRRLGARKA
SFAPMETAVELTGMEYGGITPVGLPAGWPILVDSAVAERPAVVIGSGVRRSKLLLPGAALAELPGAEVL
>gnl|CDD|340854 cd04946, GT4_AmsK-like, amylovoran biosynthesis glycosyltransferase AmsK and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea
TLVLLTNSFPGIKGETFIEEEIRYLSKSFLKIYILPLHVKKVRRCVPSNNIEISNSLKITSFLKKIFRAL
SLFSLVFYKEIWIKDKPRSGSFLLLYYFLIASFLSKHRVLALLQFVSIFGQGTVVYSYWLNHTALGLGLL
KDEYYRDVVISRAHRYDLYEDQYGSYYLPLREYLVSYLDAVFLISKEGKDYLQKCYPAYKEKIFVSRLGV
SDKEQYSKVKKEGDLRLVSCSSIVPVKRIDLIIETLNSLCVAHPSICISWTHIGGGPLKERLEKLAENKL
ENVKVNFTGEVSNKEVKQLYKENDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGL
LLDKDPTPNEIVSSIMKFYLDGGDYKTMKISARECWEERFNAEVNYSKFAN
>gnl|CDD|340855 cd04949, GT4_GtfA-like, accessory Sec system glycosyltransferase GtfA and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria
YFVINNLIGWASSGIEYAQINRLKLFKEHTRPYKIIFLNEQELFAFFIEQLNLQKGDIFISDRPTLTGQV
ILNTKGPAKKGAVLHNEHVKNNDDPEHSLIKNFYKYVFENLNKYDAIIVSTEQQKQDLSERFNKYPPIFT
IPVGYVDQLDTAESNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLI
EELHLEDNVFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKYGPSELIEDGENG
YLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAEKYSTENVMEKW
>gnl|CDD|340856 cd04950, GT4_TuaH-like, teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins. Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility
MAQHPDLLILSHDWWGFLFQRPQHLMLALAKLGHRVLFVEEPGNRDESRTISPTGRIWDRVWKFLVKKLG
RPARVGLTPDFSAFLLRSLLDALLADSRLGFRRVVLWYYTPMTLLFSDHLQASLVVYDCMDELAAFPGMP
PELIEQERRLIKRADVVFTTSPALYEAKRPLHENVHPIPNGVDVEHFAAARQPLDDPIDLREIPGPVLGF
FGAIDEKLDFDLIEELAKARPQWNFVFIGPVVKIDPSSLPRAPNIHWLGPKPYKELPAYLAGFDVALLPF
ALNEYTRFISPLKLFEYLAAGKPVVATSIPSVVRFYGEAVLCGDDPDEFSAAIEKALALKGDARDKRLAR
ALARQESWDERARAMEEALQEGG
>gnl|CDD|340857 cd04951, GT4_WbdM_like, LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria
KILYVITGLGLGGAEKQTVLLADQMFIRGHDVNIVYLTGEVEVKPLNNNIIIYNLGMDKNPRSLLKALLK
LKKIISAFKPDVVHSHMFHANIFARFLRMLYPIPLLICTAHNKNEGGRIRMFIYRLTDFLCDITTNVSRE
ALDEFIAKKAFSKNKSVPVYNGIDLNKFKKDINVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAI
SELILSKNDFKLLIAGDGPLRNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVA
EAMACERPVVATDAGGVAEVVGDHNYVVPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFSINTI
VNEWERLYSG
>gnl|CDD|340858 cd04955, GT4-like, glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in certain bacteria and Archaea
HIFIIGSRGLPAKYGGFETFVEKLTERQQSDNIKYHVACLSENSKQQHFEYNGADCFYVKVPKIGPARAI
AYDIAALNYALKYIKEQNIKNPIFYILACRIGPFIAPYIKKIHKLGGKLFVNPDGLEWKRAKWSLPVRKY
WKFSESLMVKHADLLICDSKNIEKYIRKEYGKSNTTFIAYGTDTLKSSLSDEDEKVREWYKEKGVKPGKY
YLIVGRFVPENNYETMIREFMKSSTKRDLVIITNVEGNAYYELLLKKTAFDHDERIKFVGTVYDQELLKY
IRENAFAYLHGHEVGGTNPSLLEALGSTDLNLLLDVGFNREVAEDAALYWKKEPLASLIDEVDNLNPDEI
SDLGKKAKQRIEEAYTWEKIVDEYEELFL
>gnl|CDD|340859 cd04962, GT4_BshA-like, N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes
MKIGIVCYPSYGGSGVVATELGLELAERGHEVHFISSAIPFRLNLYSGNIFFHEVEVPNYPLFEYPPYTL
ALASKIVEVAKEHKLDVLHAHYAIPHASCAYLAREILGEKIPIVTTLHGTDITLVGYDPSLQPAVRFSIN
KSDRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKPAGALKRRLLAPPDEKVVIHVSNFRPVKR
IDDVVRVFARVRRKIPAKLLLVGDGPERVPAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKE
SFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRA
AERFDPERIVPQYEAYYRRL
>gnl|CDD|409356 cd04967, IgI_1_Contactin, First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains. The members here are composed of the first immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains
GPVFEEQPDDTIFPEDSDEKKVALNCRARANPVPSYRWLMNGTEIDLESDYRYSLVDGTLVISNPSKAKD
AGHYQCLATNTVGSVLSREATLQFGY
>gnl|CDD|409357 cd04968, IgI_3_Contactin, Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains
PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRKVDGSPSSQWEITTSEPVLEIPNVQFEDEGTYEC
EAENSRGKDTVQGRIIVQ
>gnl|CDD|409358 cd04969, Ig5_Contactin, Fifth immunoglobulin (Ig) domain of contactin. The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma
PDFELNPVKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDGSLKIKNVTKSDEGKY
TCFAVNFFGKANSTGSLSV
>gnl|CDD|409359 cd04970, Ig6_Contactin, Sixth immunoglobulin (Ig) domain of contactin. The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma
DATRITLAPSNADITVGENATLQCHASHDPTLDLTFTWSFNGVPIDLEKIEGHYRRRYGKDSNGDLEIVN
AQLKHAGRYTCTAQTVVDSDSASATLVVRGPP
>gnl|CDD|409360 cd04971, IgI_TrKABC_d5, Fifth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB, and TrkC; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the fifth domain of Trk receptors TrkA, TrkB, and TrkC, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors. They are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkA, TrkB, and TrkC share significant sequence homology and domain organization. The first three domains are leucine-rich domains while the fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrkA, TrkB, and TrkC mediate the trophic effects of the neurotrophin Nerve Growth Factor (NGF) family. TrkA is recognized by NGF. TrkB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. TrkC is recognized by NT-3. NT-3 is promiscuous as in some cell systems it activates TrkA and TrkB receptors. TrkA is a receptor found in all major NGF targets, including the sympathetic, trigeminal, and dorsal root ganglia, cholinergic neurons of the basal forebrain, and the striatum. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. The TrkC gene is expressed throughout the mammalian nervous system. This group belongs to the I-set of IgSF domains
APVIVRLEEPELRHHWCIPFTVRGNPKPTLTWYHNGAVLNESDYIRTEIHYEAATPTEYHGCLKFDNPTH
VNNGNYTLVASNEYGQDSKSISAHFM
>gnl|CDD|409361 cd04972, Ig_TrkABC_d4, Fourth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB, and TrkC. The members here are composed of the fourth domain of Trk receptors TrkA, TrkB, and TrkC, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors. They are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkA, TrkB, and TrkC share significant sequence homology and domain organization. The first three domains are leucine-rich domains while the fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrkA, TrkB, and TrkC mediate the trophic effects of the neurotrophin Nerve Growth Factor (NGF) family. TrkA is recognized by NGF. TrKB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. TrkC is recognized by NT-3. NT-3 is promiscuous as in some cell systems it activates TrkA and TrkB receptors. TrkA is a receptor found in all major NGF targets, including the sympathetic, trigeminal, and dorsal root ganglia, cholinergic neurons of the basal forebrain, and the striatum. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. The TrkC gene is expressed throughout the mammalian nervous system
TLKIQMPNASVDVGDDVLLQCQVEGQGLEQAGWILTELEQSATVMKSGSLPSLGLTLANVTSDLNRKNVT
CWAENDVGRAEVSVQVNV
>gnl|CDD|409362 cd04973, IgI_1_FGFR, First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the first immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for all FGFs
PTLPPEAPPTYQISEVESYSAHPGDLLQLRCRLRDDVQSINWTKDGVQLGENNRTRITGEEVQIKDAVPR
DSGLYACVTSSPSGSDTTYFSVNV
>gnl|CDD|409363 cd04974, IgI_3_FGFR, Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
PILQAGLPANQTVVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKYGPDGLPYVTVLKVAGVNTTGEENT
LTISNVTFDDAGEYICLAGNSIGLSFHSAWLT
>gnl|CDD|409364 cd04975, IgI_4_SCFR_like, Fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR), and similar domains; member of the I-set of IgSF domains. The members here are composed of the fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR). In addition to SCFR, this group also includes the fourth Ig domain of macrophage colony stimulating factor receptor (M-CSF-R). SCFR, also called receptor tyrosine kinase KIT or proto-oncogene c-Kit, contains an extracellular component having five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. SCFR and its ligand SCF are critical for normal hematopoiesis, mast cell development, melanocytes, and gametogenesis. SCF binds to the second and third Ig-like domains of SCFR, this fourth Ig-like domain participates in SCFR dimerization, which follows ligand binding. Deletion of this fourth SCFR Ig-like domain abolishes the ligand-induced dimerization of SCFR and completely inhibits signal transduction. M-CSF-R, also called proto-oncogene c-Fms, acts as cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, such as macrophages and monocytes. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
GYINLSSEQNLTVEVNVGENLDLIVEVEAYPKPEHQNWTYMGPFFTDKWEDLPNSENESTYRYVSTLHLT
RLKGSEAGTYTFLASNSDVNAALAFEVYLNY
>gnl|CDD|409365 cd04976, IgI_VEGFR, Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members, VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic, and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
FITVKHRKQQVLEATAGKRSVRLPMKVKAYPPPEVVWYKDGLPLTEKARYLTRHSLIIKEVTEEDTGNYT
ILLSNKQSNVFKNLTATLVV
>gnl|CDD|409366 cd04977, IgI_1_NCAM-1_like, First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar domains; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-nonNCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
LQVKIIPSYAEISVGESKFFLCKVSGDAKNINWVSPNGEKVLTKHGNLKVVNHGSVLSSLTIYNANINDA
GIYKCVATNGKGTESEATVKLDIIQ
>gnl|CDD|409367 cd04978, Ig4_L1-NrCAM_like, Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth
YWIIEPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDGRTLIFSNLQPNDTAVYQ
CNASNVHGYLLANAFLHVL
>gnl|CDD|409368 cd04979, Ig_Semaphorin_C, Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins. The members here are composed of the immunoglobulin (Ig)-like domain in semaphorins. Semaphorins are transmembrane protein that have important roles in a variety of tissues. Functionally, semaphorins were initially characterized for their importance in the development of the nervous system and in axonal guidance. Later they have been found to be important for the formation and functioning of the cardiovascular, endocrine, gastrointestinal, hepatic, immune, musculoskeletal, renal, reproductive, and respiratory systems. Semaphorins function through binding to their receptors and transmembrane semaphorins also serves as receptors themselves. Although molecular mechanism of semaphorins is poorly understood, the Ig-like domains may be involved in ligand binding or dimerization
TSFKQISVKEGDTVILSCSVKSNNAPVTWIHNGKKVPRYRSPRLVLKTERGLLIRSAQEADAGVYECHSG
ERVLGSTLRSVTLHVLER
>gnl|CDD|409369 cd04980, IgV_L_kappa, Immunoglobulin (Ig) light chain, kappa type, variable (V) domain. The members here are composed of the immunoglobulin (Ig) light chain, kappa type, variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains
IVMTQSPASLSVSPGERVTISCKASQSISSNYLAWYQQKPGQAPKLLIYYASTLHSGVPSRFSGSGSGTD
FTLTISSVEPEDAAVYYCQQGYTFPYTFGGGTKLEI
>gnl|CDD|409370 cd04981, IgV_H, Immunoglobulin (Ig) heavy chain (H), variable (V) domain. The members here are composed of the immunoglobulin (Ig) heavy chain (H), variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which can associate with any of the heavy chains. This family includes alpha, gamma, delta, epsilon, and mu heavy chains
QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITR
DTSKSTAYLQLNSLTSEDTAVYYCARGLGGYGYSYFDYWGQGTTVTVS
>gnl|CDD|409371 cd04982, IgV_TCR_gamma, Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain. The members here are composed of the immunoglobulin (Ig) variable (V) domain of the gamma chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigens as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain the standard Ig superfamily V-set AGFCC'C"/DEB domain topology
LEQPQLSITREESKSVTISCKVSGIDFSTTYIHWYRQKPGQALERLLYVSSTSAVRKDSGKTKNKFEARK
DVGKSTSTLTITNLEKEDSATYYCAYWESGSGYYIKVFGSGTKLIVT
>gnl|CDD|409372 cd04983, IgV_TCR_alpha, Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins. The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology
VTQSPQSLSVQEGENVTLNCNYSTSTFYYLFWYRQYPGQGPQFLIYISSDSGNKKKGRFSATLDKSRKSS
SLHISAAQLSDSAVYFCALSESGGTGKLTFGKGTRLTVE
>gnl|CDD|409373 cd04984, IgV_L_lambda, Immunoglobulin (Ig) lambda light chain variable (V) domain. The members here are composed of the immunoglobulin (Ig) light chain, lambda type, variable (V) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology
VLTQPSSLSVSPGETVTITCTGSSGNISGNYVNWYQQKPGSAPRYLIYEDKHRPSGIPDRFSGSKSGNTA
SLTISGAQTEDEADYYCQVWDSNSYVFGGGTKLTV
>gnl|CDD|409374 cd04985, IgC1_CH1_IgADEGM, CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, delta, epsilon, gamma, and mu chains; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the first immunoglobulin constant-1 set domain of alpha, delta, epsilon, gamma, and mu heavy chains. This domain is found on the Fab antigen-binding fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. This group belongs to the C1-set of IgSF domains, which are classical Ig-like domains resembling the antibody constant domain. C1-set domains are found almost exclusively in molecules involved in the immune system, such as in immunoglobulin light and heavy chains, in the major histocompatibility complex (MHC) class I and II complex molecules, and in various T-cell receptors
APTVFPLQSATKSQSNGPVALGCLISDYFPESITVSWQKNTNSITSGFTRTFPVVLRSGGDYSCSSQLTV
PLQEWNSGEVYKCQVQHSASNSKQEKDV
>gnl|CDD|409375 cd04986, IgC1_CH2_IgA, CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin heavy alpha chain; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the second immunoglobulin constant-1 set domain (IgC) of alpha heavy chains. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. This group belongs to the C1-set of IgSF domains, which are classical Ig-like domains resembling the antibody constant domain. C1-set domains are found almost exclusively in molecules involved in the immune system, such as in immunoglobulin light and heavy chains, in the major histocompatibility complex (MHC) class I and II complex molecules, and in various T-cell receptors
QPRLSLQRPALEDLLLGSNASLTCTLSGLKDPEGATFTWEPSGGKEAIQGPPERDSCGCYSVSSVLPGCA
EPWNSGDTFSCTVTHPESKGTLTATI
>gnl|CDD|240138 cd05005, SIS_PHI, Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI
MEYLSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGETTT
PAIGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGEHKS
IQPLGTLFEQSALVFLDAVIAKLMEELGVSEEEMKKRHA
>gnl|CDD|240139 cd05006, SIS_GmhA, Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh)
FQESIQLKEALLELLAEAIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEKERPGLPAIA
LTTDTSILTAIANDYGYEEVFSRQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGG
KLLELADIEIHVPSDDTPRIQEVHLLIGHILCELVEE
>gnl|CDD|240140 cd05007, SIS_Etherase, N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate
RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASE
LPPTFGTPPERVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRY
ARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNL
MVDVRATNEKLRERAIRIVMEATGVSRDEAEAALEQAGGDVKTAILM
>gnl|CDD|240141 cd05008, SIS_GlmS_GlmD_1, SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction
RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAK
EKGAKTVAITNVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA
>gnl|CDD|240142 cd05009, SIS_GlmS_GlmD_2, SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction
EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAP
EDRLEEKLESLIKEVKARGAKVIVITDDGDAKDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGI
DPDKPRNLAKSVT
>gnl|CDD|240143 cd05010, SIS_AgaS_like, AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many phosphosugar isomerases and phosphosugar binding proteins. AgaS is a putative isomerase in Escherichia coli. It is similar to the glucosamine-6-phosphate synthases (GlmS) which catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source
VVYLGSGPLAGLAREAALKVLELTAGKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLL
KELRRDGIAARVIAISPESDAGIEDNSHYYLPGSRDLDDVYLAFPYILYAQLFALFNSIALGLTPDNPCP
SGTVNRVVQGV
>gnl|CDD|240144 cd05013, SIS_RpiR, RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate
EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFS
GETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA
>gnl|CDD|240145 cd05014, SIS_Kpsf, KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway
GKVVVTGVGKSGHIARKIAATLSSTGTPAFFLHPTEALHGDLGMVTPGDVVIAISNSGETDELLNLLPHL
KRRGAPIIAITGNPNSTLAKLSDVVLDLPVEEEACPLGLAPTTSTTAMLALGDALAVA
>gnl|CDD|240146 cd05015, SIS_PGI_1, Phosphoglucose isomerase (PGI) contains two SIS (Sugar ISomerase) domains. This classification is based on the alignment of the first SIS domain. PGI is a multifunctional enzyme which as an intracellular dimer catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. As an extracellular protein, PGI also has functions equivalent to neuroleukin (NLK), autocrine motility factor (AMF), and maturation factor (MF). Evidence suggests that PGI, NLK, AMF, and MF are closely related or identical. NLK is a neurotrophic growth factor that promotes regeneration and survival of neurons. The dimeric form of NLK has isomerase function, whereas its monomeric form carries out neurotrophic activity. AMF is a cytokine that stimulates cell migration and metastasis. MF mediates the differentiation of human myeloid leukemic HL-60 cells to terminal monocytic cells
RAELERIKEFAEKVRSGKKITDVVVIGIGGSDLGPRAVYEALKPYFKGGLRLHFVSNVDPDDLAELLKKL
DPETTLFIVISKSGTTLETLANARLAREWLEEAGGDDLAKHFVAITDNGSGLLKKAGIEGLNTFEIPDWV
GGRFSVLSSVGGLPLALA
>gnl|CDD|240147 cd05016, SIS_PGI_2, Phosphoglucose isomerase (PGI) contains two SIS (Sugar ISomerase) domains. This classification is based on the alignment of the second SIS domain. PGI is a multifunctional enzyme which as an intracellular dimer catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. As an extracellular protein, PGI also has functions equivalent to neuroleukin (NLK), autocrine motility factor (AMF), and maturation factor (MF). Evidence suggests that PGI, NLK, AMF, and MF are closely related or identical. NLK is a neurotrophic growth factor that promotes regeneration and survival of neurons. The dimeric form of NLK has isomerase function, whereas its monomeric form carries out neurotrophic activity. AMF is a cytokine that stimulates cell migration and metastasis. MF mediates the differentiation of human myeloid leukemic HL-60 cells to terminal monocytic cells
KTHALLPYSQRLERFPAWLQQLDMESNGKSVTRDGEDYPTGPIPWGAPGTNDQHSFFQLIHQGTKDKPVD
FIAVKKPQNDVLDYLAGKTLHDLLLANCLATREALMFPGGRPSNTIVLPELTPYTLGALLALYEHKTAVQ
GALLGINPFDQPGVELGKKLAKKI
>gnl|CDD|240148 cd05017, SIS_PGI_PMI_1, The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain
NIVILGMGGSGIGGDLLESLLLDEAKIPVYVVKDYTLPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERG
AKIVAITSGGKLLEMAREHGVPVIIIPKGLQPRAAFPYLFTALLNILNK
>gnl|CDD|176853 cd05018, CoxG, Carbon monoxide dehydrogenase subunit G (CoxG). CoxG has been shown, in Oligotropha carboxidovorans, to anchor the carbon monoxide (CO) dehydrogenase to the cytoplasmic membrane. The gene encoding CoxG is part of the Cox cluster (coxBCMSLDEFGHIK) located on a low-copy-number, circular, megaplasmid pHCG3. This cluster includes genes encoding subunits of CO dehydrogenase and several accessory components involved in the utilization of CO. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands
MKISGEFRIPAPPEEVWAALNDPEVLARCIPGCESLEKIGPNEYEATVKLKVGPVKGTFKGKVELSDLDP
PESYTITGEGKGGAGFVKGTARVTLEPDGGGTRLTYTADAQVGGKLAQLGSRLIDGAARKLINQFFENLA
SKIG
>gnl|CDD|240149 cd05022, S-100A13, S-100A13: S-100A13 domain found in proteins similar to S100A13. S100A13 is a calcium-binding protein belonging to a large S100 vertebrate-specific protein family within the EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A13 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100A13 is involved in the cellular export of interleukin-1 (IL-1) and of fibroblast growth factor-1 (FGF-1), which plays an important role in angiogenesis and tissue regeneration. Export is based on the CuII-dependent formation of multiprotein complexes containing the S100A13 protein. Assembly of these complexes occurs near the inner surface of the plasma membrane. Binding of two Ca(II) ions per monomer triggers key conformational changes leading to the creation of two identical and symmetrical Cu(II)-binding sites on the surface of the protein, close to the interface between the two monomers. These Cu(II)-binding sites are unique among the S100 proteins, which are reported to bind Cu(II) or Zn(II) ions in addition to Ca(II) ions. In addition, the three-dimensional structure of S100A13 differs significantly from those of other S100 proteins; the hydrophobic pocket that largely contributes to protein-protein interactions in other S100 proteins is absent in S100A13. The structure of S100A13 contains a large patch of negatively charged residues flanked by dense cationic clusters, formed mostly from positively charged residues from the C-terminal end, which plays major role in binding FGF-1
TELEKAIETLVSNFHKASVKGGKESLTASEFQELLTQQLPHLLKDVEGLEEKMKNLDVNQDSKLSFEEFW
ELIGELAKAVKGEKHLEKQ
>gnl|CDD|240150 cd05023, S-100A11, S-100A11: S-100A11 domain found in proteins similar to S100A11. S100A11 is a member of the S-100 domain family within EF-hand Ca2+-binding proteins superfamily. Note that the S-100 hierarchy, to which this S-100A11 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins exhibit unique patterns of tissue- and cell type-specific expression and have been implicated in the Ca2+-dependent regulation of diverse physiological processes, including cell cycle regulation, differentiation, growth, and metabolic control . S100 proteins have also been associated with a variety of pathological events, including neoplastic transformation and neurodegenerative diseases such as Alzheimer's, usually via over expression of the protein. S100A11 is expressed in smooth muscle and other tissues and involves in calcium-dependent membrane aggregation, which is important for cell vesiculation . As is the case for many other S100 proteins, S100A11 is homodimer, which is able to form a heterodimer with S100B through subunit exchange. Ca2+ binding to S100A11 results in a conformational change in the protein, exposing a hydrophobic surface that interacts with target proteins. In addition to binding to annexin A1 and A6 S100A11 also interacts with actin and transglutaminase
PTETERCIESLIAVFQKYAGKDGDSYQLSKTEFLSFMNTELASFTKNQKDPGVLDRMMKKLDLNSDGQLD
FQEFLNLIGGLAVACHESF
>gnl|CDD|240151 cd05024, S-100A10, S-100A10: A subgroup of the S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of the S100 family of EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A10 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. A unique feature of S100A10 is that it contains mutation in both of the calcium binding sites, making it calcium insensitive. S100A10 has been detected in brain, heart, gastrointestinal tract, kidney, liver, lung, spleen, testes, epidermis, aorta, and thymus. Structural data supports the homo- and hetero-dimeric as well as hetero-tetrameric nature of the protein. S100A10 has multiple binding partners in its calcium free state and is therefore involved in many diverse biological functions
SELEHSMEKMMLTFHKFAGEKNYLNRDDLQKLMEKEFSEFLKNQNDPMAVDKIMKDLDDCRDGKVGFQSF
FSLIAGLLIACNDYYVKHMKQ
>gnl|CDD|240152 cd05025, S-100A1, S-100A1: S-100A1 domain found in proteins similar to S100A1. S100A1 is a calcium-binding protein belonging to a large S100 vertebrate-specific protein family within the EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A1 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. As is the case with many other members of S100 protein family, S100A1 is implicated in intracellular and extracellular regulatory activities, including interaction with myosin-associated twitchin kinase, actin-capping protein CapZ, sinapsin I, and tubulin. Structural data suggests that S100A1 proteins exist within cells as antiparallel homodimers, while heterodimers with S100A4 and S100B also has been reported. Upon binding calcium S100A1 changes conformation to expose a hydrophobic cleft which is the interaction site of S100A1 with its more that 20 known target proteins
GSELETAMETLINVFHAHSGKEGDKYKLSKKELKDLLQTELSDFLDAQKDADAVDKIMKELDENGDGEVD
FQEFVVLVAALTVACNNFFWEN
>gnl|CDD|240153 cd05026, S-100Z, S-100Z: S-100Z domain found in proteins similar to S100Z. S100Z is a member of the S100 domain family within the EF-hand Ca2+-binding proteins superfamily. Note that the S-100 hierarchy, to which this S-100Z group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately.S100 proteins exhibit unique patterns of tissue- and cell type-specific expression and have been implicated in the Ca2+-dependent regulation of diverse physiological processes, including cell cycle regulation, differentiation, growth, and metabolic control. S100Z is normally expressed in various tissues, with its highest level of expression being in spleen and leukocytes. The function of S100Z remains unclear. Preliminary structural data suggests that S100Z is homodimer, however a heterodimer with S100P has been reported. S100Z is capable of binding calcium ions. When calcium binds to S110Z, the protein experiences a conformational change, which exposes hydrophobic surfaces on the protein. In comparison with their normal tissue counterparts, S100Z gene expression appears to be deregulated in some tumor tissues
MPTQLEGAMDTLIRIFHNYSGKEGDRYKLSKGELKELLQRELTDFLSSQKDPMLVDKIMNDLDSNKDNEV
DFNEFVVLVAALTVACNDFFQEQ
>gnl|CDD|240154 cd05027, S-100B, S-100B: S-100B domain found in proteins similar to S100B. S100B is a calcium-binding protein belonging to a large S100 vertebrate-specific protein family within the EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100B group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100B is most abundant in glial cells of the central nervous system, predominately in astrocytes. S100B is involved in signal transduction via the inhibition of protein phoshorylation, regulation of enzyme activity and by affecting the calcium homeostasis. Upon calcium binding the S100B homodimer changes conformation to expose a hydrophobic cleft, which represents the interaction site of S100B with its more than 20 known target proteins. These target proteins include several cellular architecture proteins such as tubulin and GFAP; S100B can inhibit polymerization of these oligomeric molecules. Furthermore, S100B inhibits the phosphorylation of multiple kinase substrates including the Alzheimer protein tau and neuromodulin (GAP-43) through a calcium-sensitive interaction with the protein substrates
SELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDSDGDGECDF
QEFMAFVAMVTTACHEFF
>gnl|CDD|240155 cd05029, S-100A6, S-100A6: S-100A6 domain found in proteins similar to S100A6. S100A6 is a member of the S100 domain family within EF-hand Ca2+-binding proteins superfamily. Note that the S-100 hierarchy, to which this S-100A6 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins exhibit unique patterns of tissue- and cell type-specific expression and have been implicated in the Ca2+-dependent regulation of diverse physiological processes, including cell cycle regulation, differentiation, growth, and metabolic control . S100A6 is normally expressed in the G1 phase of the cell cycle in neuronal cells. The function of S100A6 remains unclear, but evidence suggests that it is involved in cell cycle regulation and exocytosis. S100A6 may also be involved in tumorigenesis; the protein is overexpressed in several tumors. Ca2+ binding to S100A6 leads to a conformational change in the protein, which exposes a hydrophobic surface for interaction with target proteins. Several such proteins have been identified: glyceraldehyde-3-phosphate dehydrogenase, annexins 2, 6 and 11 and Calcyclin-Binding Protein (CacyBP)
MASPLDQAIGLLVAIFHKYSGREGDKNTLSKKELKELIQKELTIGSKLQDAEIAKLMEDLDRNKDQEVNF
QEYVTFLGALALIYNEAL
>gnl|CDD|240156 cd05030, calgranulins, Calgranulins: S-100 domain found in proteins belonging to the Calgranulin subgroup of the S100 family of EF-hand calcium-modulated proteins, including S100A8, S100A9, and S100A12 . Note that the S-100 hierarchy, to which this Calgranulin group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. These proteins are expressed mainly in granulocytes, and are involved in inflammation, allergy, and neuritogenesis, as well as in host-parasite response. Calgranulins are modulated not only by calcium, but also by other metals such as zinc and copper. Structural data suggested that calgranulins may exist in multiple structural forms, homodimers, as well as hetero-oligomers. For example, the S100A8/S100A9 complex called calprotectin plays important roles in the regulation of inflammatory processes, wound repair, and regulating zinc-dependent enzymes as well as microbial growth
TELEKAIETIINVFHQYSVRKGHPDTLYKKEFKQLVEKELPNFLKKEKNQKAIDKIFEDLDTNQDGQLSF
EEFLVLVIKVGVAAHEKS
>gnl|CDD|240157 cd05031, S-100A10_like, S-100A10_like: S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of the S100 family of EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A1_like group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. A unique feature of S100A10 is that it contains mutation in both of the calcium binding sites, making it calcium insensitive. S100A10 has been detected in brain, heart, gastrointestinal tract, kidney, liver, lung, spleen, testes, epidermis, aorta, and thymus. Structural data supports the homo- and hetero-dimeric as well as hetero-tetrameric nature of the protein. S100A10 has multiple binding partners in its calcium free state and is therefore involved in many diverse biological functions
SELEHAMESLILTFHRYAGKDGDKNTLSRKELKKLMEKELSEFLKNQKDPMAVDKIMKDLDQNRDGKVNF
EEFVSLVAGLSIACEEYYVKHMKK
>gnl|CDD|173625 cd05032, PTKc_InsR_like, Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
WELPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHH
VVRLLGVVSTGQPTLVVMELMAKGDLKSYLRSRRPEAENNPGLGPPTLQKFIQMAAEIADGMAYLAAKKF
VHRDLAARNCMVAEDLTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVV
LWEMATLAEQPYQGLSNEEVLKFVIDGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLKD
>gnl|CDD|270629 cd05033, PTKc_EphR, Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IDASYVTIEKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRL
EGVVTKSRPVMIVTEYMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVN
SDLVCKVSDFGLSRRLEDSEATYTTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYW
DMSNQDVIKAVEDGYRLPPPMDCPSALYQLMLDCWQKDRNERPTFSQIVSTLDKMI
>gnl|CDD|270630 cd05034, PTKc_Src_like, Catalytic domain of Src kinase-like Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KKLGAGQFGEVWMGVWNGTTKVAVKTLKPGTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTE
LMSKGSLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLAR
LIEDDEYTAREGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGY
RMPKPPGCPDELYDIMLQCWKKEPEERPTFEYLQSFLE
>gnl|CDD|270631 cd05035, PTKc_TAM, Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LKLGKILGEGEFGSVMEAQLKQDDGSQLKVAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVC
FTASDLNKPPSPMVILPFMKHGDLHSYLLYSRLGGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLA
ARNCMLDENMTVCVADFGLSRKIYSGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIAT
RGQTPYPGVENHEIYDYLRNGNRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENIL
>gnl|CDD|270632 cd05036, PTKc_ALK_LTK, Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KEVPRKNLTLIRALGQGAFGEVYEGTVSGMPGDPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPN
IVRCIGVCFQRLPRFILLELMAGGDLKSFLRENRPRPEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHR
DIAARNCLLTCKGPGRVAKIGDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVL
LWEIFSLGYMPYPGKSNQEVMEFVTSGGRMDPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILERLNY
>gnl|CDD|270633 cd05037, PTK_Jak_rpt1, Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases. The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ITFHEHLGQGTFTNIYDGILREVGDGRVQEVEVLLKVLDSDHRDISESFFETASLMSQISHKHLVKLYGV
CVADENIMVQEYVRYGPLDKYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGL
DGYPPFIKLSDPGVPITVLSREERVDRIPWIAPECLRNLQANLTIAADKWSFGTTLWEICSGGEEPLSAL
SSQEKLQFYEDQHQLPAPDCAELAELIMQCWTYEPTKRPSFRAILRDLN
>gnl|CDD|270634 cd05038, PTKc_Jak_rpt2, Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases. The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FEERHLKFIKQLGEGHFGSVELCRYDPLGDNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVK
YKGVCESPGRRSLRLIMEYLPSGSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNI
LVESEDLVKISDFGLAKVLPEDKEYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGD
PSQSPPALFLRMIGIAQGQMIVTRLLELLKSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILII
DRLR
>gnl|CDD|270635 cd05039, PTKc_Csk_like, Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
WAINKKDLKLGELIGKGEFGDVMLGDYRGQKVAVKCLKDDSTAAQAFLAEASVMTTLRHPNLVQLLGVVL
EGNGLYIVTEYMAKGSLVDYLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNV
AKVSDFGLAKEASSNQDGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVP
HVEKGYRMEAPEGCPPEVYKVMKNCWELDPAKRPTFKQLREKLEHI
>gnl|CDD|270636 cd05040, PTKc_Ack_like, Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EKLGDGSFGVVRRGEWTTPSGKVIQVAVKCLKSDVLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSS
PLMMVTELAPLGSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIG
DFGLMRALPQNEDHYVMQEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQI
LEKIDKEGERLERPDDCPQDIYNVMLQCWAHKPADRPTFVALRDFLPE
>gnl|CDD|270637 cd05041, PTKc_Fes_like, Catalytic domain of Fes-like Protein Tyrosine Kinases. Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions
EKIGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMI
VMELVPGGSLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGM
SREEEDGEYTVSDGLKQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIE
SGYRMPAPELCPEAVYRLMLQCWAYDPENRPSFSEIYNELQ
>gnl|CDD|270638 cd05042, PTKc_Aatyk, Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QEIGNGWFGKVLLGEIYSGTSVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPY
LLVMEFCDLGDLKAYLRSEREHERGDSDTRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVK
IGDYGLAHSRYKEDYIETDDKLWFPLRWTAPELVTEFHDRLLVVDQTKYSNIWSLGVTLWELFENGAQPY
SNLSDLDVLAQVVREQDTKLPKPQLELPYSDRWYEVLQFCWLSPEQRPAAEDVHLLLTY
>gnl|CDD|270639 cd05043, PTK_Ryk, Pseudokinase domain of Ryk (Receptor related to tyrosine kinase). Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IAVSRERVTLSDLLQEGTFGRIFHGILRDEKGKEEEVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLL
PILHVCIEDGEKPMVLYPYMNWGNLKLFLQQCRLSEANNPQALSTQQLVHMALQIACGMSYLHRRGVIHK
DIAARNCVIDDELQVKITDNALSRDLFPMDYHCLGDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWE
LMTLGQTPYVEIDPFEMAAYLKDGYRLAQPINCPDELFAVMACCWALDPEERPSFQQLVQCLTDFHAQL
>gnl|CDD|270640 cd05044, PTKc_c-ros, Catalytic domain of the Protein Tyrosine Kinase, C-ros. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KFLGSGAFGEVFEGTAKDILGDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLD
NDPQYIILELMEGGDLLSYLRAARPTAFTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVS
SKDYRERVVKIGDFGLARDIYKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQ
QPYPARNNLEVLHFVRAGGRLDQPDNCPDDLYELMLRCWSTDPEERPSFARILEQLQN
>gnl|CDD|173631 cd05045, PTKc_RET, Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NLVLGKTLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYG
ACSQDGPLLLIVEYAKYGSLRSFLRESRKVGPSYLGSDGNRNSSYLDNPDERALTMGDLISFAWQISRGM
QYLAEMKLVHRDLAARNVLVAEGRKMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQS
DVWSFGVLLWEIVTLGGNPYPGIAPERLFNLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADIS
KELEKMMVKS
>gnl|CDD|133178 cd05046, PTK_CCK4, Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4. CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
AFPRSNLQEITTLGRGEFGEVFLAKAKGIEEEGGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNV
VRLLGLCREAEPHYMILEYTDLGDLKQFLRATKSKDEKLKPPPLSTKQKVALCTQIALGMDHLSNARFVH
RDLAARNCLVSSQREVKVSLLSLSKDVYNSEYYKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWE
VFTQGELPFYGLSDEEVLNRLQAGKLELPVPEGCPSRLYKLMTRCWAVNPKDRPSFSELVSALGE
>gnl|CDD|270641 cd05047, PTKc_Tie, Catalytic domain of Tie Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGY
LYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAA
RNILVGENYVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGT
PYCGMTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLE
>gnl|CDD|270642 cd05048, PTKc_Ror, Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EIPLSAVRFLEELGEGAFGKVYKGELLGPSSEESAISVAIKTLKENASPKTQQDFRREAELMSDLQHPNI
VCLLGVCTKEQPQCMLFEYMAHGDLHEFLVRHSPHSDVGVSSDDDGTASSLDQSDFLHIAIQIAAGMEYL
SSHHYVHRDLAARNCLVGDGLTVKISDFGLSRDIYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVW
SFGVVLWEIFSYGLQPYYGYSNQEVIEMIRSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEIHTRL
RTW
>gnl|CDD|270643 cd05049, PTKc_Trk, Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HIKRDTIVLKRELGEGAFGKVFLGECYNLEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENI
VKFYGVCTEGDPLLMVFEYMEHGDLNKFLRSHGPDAAFLASEDSAPGELTLSQLLHIAVQIASGMVYLAS
QHFVHRDLATRNCLVGTNLVVKIGDFGMSRDIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSF
GVVLWEIFTYGKQPWFQLSNTEVIECITQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQE
>gnl|CDD|133181 cd05050, PTKc_Musk, Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EYPRNNIEYVRDIGQGAFGRVFQARAPGLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDHPNI
VKLLGVCAVGKPMCLLFEYMAYGDLNEFLRHRSPRAQCSLSHSTSSARKCGLNPLPLSCTEQLCIAKQVA
AGMAYLSERKFVHRDLATRNCLVGENMVVKIADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYT
TESDVWAYGVVLWEIFSYGMQPYYGMAHEEVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFA
SINRILQR
>gnl|CDD|270644 cd05051, PTKc_DDR, Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EFPREKLEFVEKLGEGQFGEVHLCEANGLSDLTSDDFIGNDNKDEPVLVAVKMLRPDASKNAREDFLKEV
KIMSQLKDPNIVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGASATNSKTLSYGTLLYMATQI
ASGMKYLESLNFVHRDLATRNCLVGPNYTIKIADFGMSRNLYSGDYYRIEGRAVLPIRWMAWESILLGKF
TTKSDVWAFGVTLWEILTLCKEQPYEHLTDEQVIENAGEFFRDDGMEVYLSRPPNCPKEIYELMLECWRR
DEEDRPTFREIHLFLQR
>gnl|CDD|270645 cd05052, PTKc_Abl, Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
WEIERTDITMKHKLGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGV
CTREPPFYIITEFMPYGNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGEN
HLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGID
LSQVYELLEKGYRMERPEGCPPKVYELMRACWQWNPSDRPSFAEIHQALETMF
>gnl|CDD|270646 cd05053, PTKc_FGFR, Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LPLDPEWELPRDRLTLGKPLGEGAFGQVVKAEAVGLDNKPNEVVTVAVKMLKDDATEKDLSDLVSEMEMM
KMIGKHKNIINLLGACTQDGPLYVVVEYASKGNLREFLRARRPPGEEASPDDPRVPEEQLTQKDLVSFAY
QVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDR
VYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRP
TFKQLVEDLDRILT
>gnl|CDD|270647 cd05054, PTKc_VEGFR, Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KWEFPRDRLKLGKPLGRGAFGKVIQASAFGIDKSATCRTVAVKMLKEGATASEHKALMTELKILIHIGHH
LNVVNLLGACTKPGGPLMVIVEFCKFGNLSNYLRSKREEFVPYRDKGARDVEEEEDDDELYKEPLTLEDL
ICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPE
SIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQMDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHG
EPKERPTFSELVEKLGDL
>gnl|CDD|133186 cd05055, PTKc_PDGFR, Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YEVRWKVIESINGNEYVYIDPTQLPYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYGLSKSDAVMKVAV
KMLKPTAHSSEREALMSELKIMSHLGNHENIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKRESFLTL
EDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWM
APESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPGMPVDSKFYKLIKEGYRMAQPEHAPAEIYDIMKTC
WDADPLKRPTFKQIVQLIGKQL
>gnl|CDD|133187 cd05056, PTKc_FAK, Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YEIQREDITLGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIV
KLIGVITENPVWIVMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV
SSPDCVKLGDFGLSRYMEDESYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQ
GVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQLSDILQEEK
>gnl|CDD|270648 cd05057, PTKc_EGFR_like, Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LRIVKETELEKGKVLGSGAFGTVYKGVWIPEGEKVKIPVAIKVLREETGPKANEEILDEAYVMASVDHPH
LVRLLGICLSSQVQLITQLMPLGCLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNV
LVKTPNHVKITDFGLAKLLDVDEKEYHAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAK
PYEGIPAVEIPDLLEKGERLPQPPICTIDVYMVLVKCWMIDAESRPTFKELANEFSKMARDPQRYLVIQ
>gnl|CDD|270649 cd05058, PTKc_Met_Ron, Catalytic domain of the Protein Tyrosine Kinases, Met and Ron. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EVIGKGHFGCVYHGTLIDSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEG
SPLVVLPYMKHGDLRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVA
DFGLARDIYDKEYYSVHNHTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFD
ITVYLLQGRRLLQPEYCPDPLYEVMLSCWHPKPEMRPTFSELVSRISQIFST
>gnl|CDD|173637 cd05059, PTKc_Tec_like, Catalytic domain of Tec-like Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IDPSELTFLKELGSGQFGVVHLGKWRGKIDVAIKMIKEGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTK
QRPIFIVTEYMANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVK
VSDFGLARYVLDDEYTSSVGTKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEV
VEHISQGYRLYRPHLAPTEVYTIMYSCWHEKPEERPTFKILLSQLT
>gnl|CDD|270650 cd05060, PTKc_Syk_like, Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KELGHGNFGSVRKGVYLMKSGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEPL
MLVMELAPLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFG
MSRALGAGSDYYRATTAGRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAM
LESGERLPRPEECPQEIYSIMLSCWKYRPEDRPTFSELESTFRRDPE
>gnl|CDD|133192 cd05061, PTKc_InsR, Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
WEVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHH
VVRLLGVVSKGQPTLVVMELMAHGDLKSYLRSLRPEAENNPGRPPPTLQEMIQMAAEIADGMAYLNAKKF
VHRDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVV
LWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLH
PSFPEVSF
>gnl|CDD|133193 cd05062, PTKc_IGF-1R, Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
WEVAREKITMSRELGQGSFGMVYEGIAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHH
VVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPEMENNPVQAPPSLKKMIQMAGEIADGMAYLNANKF
VHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVV
LWEIATLAEQPYQGMSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIKE
>gnl|CDD|133194 cd05063, PTKc_EphR_A2, Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K)
EIHPSHITKQKVIGAGEFGEVFRGILKMPGRKEVAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIR
LEGVVTKFKPAMIITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILV
NSNLECKVSDFGLSRVLEDDPEGTYTTSGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERP
YWDMSNHEVMKAINDGFRLPAPMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKLL
>gnl|CDD|133195 cd05064, PTKc_EphR_A10, Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ELDNKSIKIERILGTGRFGELCRGCLKLPSKRELPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVR
LEGVITRGNTMMIVTEYMSNGALDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLV
NSDLVCKISGFRRLQEDKSEAIYTTMSGKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYW
DMSGQDVIKAVEDGFRLPAPRNCPNLLHQLMLDCWQKERGERPRFSQIHSILSKMV
>gnl|CDD|173638 cd05065, PTKc_EphR_B, Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IDVSCVKIEEVIGAGEFGEVCRGRLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHL
EGVVTKSRPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVN
SNLVCKVSDFGLSRFLEDDTSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGER
PYWDMSNQDVINAIEQDYRLPPPMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKMI
>gnl|CDD|270651 cd05066, PTKc_EphR_A, Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IDASCIKIEKVIGAGEFGEVCSGRLKLPGKREIPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHL
EGVVTRSKPVMIVTEYMENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVN
SNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPY
WEMSNQDVIKAIEEGYRLPAPMDCPAALHQLMLDCWQKDRNERPKFEQIVSILDKLI
>gnl|CDD|270652 cd05067, PTKc_Lck_Blk, Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAIKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAV
VTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTL
SCKIADFGLARLIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTN
PEVIQNLERGYRMPRPDNCPEELYQLMRLCWKERPEDRPTFEYLRSVLEDFFTA
>gnl|CDD|270653 cd05068, PTKc_Frk_like, Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DQWEIDRKSLKLLRKLGSGQFGEVWEGLWNNTTPVAVKTLKPGTMDPEDFLREAQIMKKLRHPKLIQLYA
VCTLEEPIYIITELMKHGSLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGEN
NICKVADFGLARVIKVEDEYEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGM
TNAEVLQQVERGYRMPCPPNCPPQLYDIMLECWKADPMERPTFETLQWKLEDFFVND
>gnl|CDD|270654 cd05069, PTKc_Yes, Catalytic domain of the Protein Tyrosine Kinase, Yes. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K)
GLAKDAWEIPRESLRLDVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLV
PLYAVVSEEPIYIVTEFMGKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANIL
VGDNLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPY
PGMVNREVLEQVERGYRMPCPQGCPESLHELMKLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQPGDN
>gnl|CDD|270655 cd05070, PTKc_Fyn, Catalytic domain of the Protein Tyrosine Kinase, Fyn. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase
KDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLY
AVVSEEPIYIVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGN
GLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGM
NNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPG
>gnl|CDD|270656 cd05071, PTKc_Src, Catalytic domain of the Protein Tyrosine Kinase, Src. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLY
AVVSEEPIYIVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGE
NLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGM
VNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL
>gnl|CDD|270657 cd05072, PTKc_Lyn, Catalytic domain of the Protein Tyrosine Kinase, Lyn. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
AWEIPRESIKLVKKLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAV
VTKEEPIYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSES
LMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMS
NSDVMSALQRGYRMPRMENCPDELYDIMKTCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQ
>gnl|CDD|270658 cd05073, PTKc_Hck, Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
WEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVK
LHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILV
SASLVCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYP
GMSNPEVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDF
>gnl|CDD|270659 cd05074, PTKc_Tyro3, Catalytic domain of the Protein Tyrosine Kinase, Tyro3. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LKDVLIQEQQFTLGRMLGKGEFGSVREAQLKSEDGSFQKVAVKMLKADIFSSSDIEEFLREAACMKEFDH
PNVIKLIGVSLRSRAKGRLPIPMVILPFMKHGDLHTFLLMSRIGEEPFTLPLQTLVRFMIDIASGMEYLS
SKNFIHRDLAARNCMLNENMTVCVADFGLSKKIYSGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWA
FGVTMWEIMTRGQTPYAGVENSEIYNYLIKGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLE
LIWG
>gnl|CDD|270660 cd05075, PTKc_Axl, Catalytic domain of the Protein Tyrosine Kinase, Axl. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KLALGKTLGEGEFGSVMEGQLNQDDSVLKVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVC
LQNTESEGYPSPVVILPFMKHGDLHSFLLYSRLGDCPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLA
ARNCMLNENMNVCVADFGLSKKIYNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIAT
RGQTPYPGVENSEIYDYLRQGNRLKQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILKDLP
>gnl|CDD|270661 cd05076, PTK_Tyk2_rpt1, Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ITQLSHLGQGTRTNIYEGRLLVEGSGEPEEDKELVPGRDRGQELRVVLKVLDPSHHDIALAFFETASLMS
QVSHTHLVFVHGVCVRGSENIMVEEFVEHGPLDVWLRKEKGHVPMAWKFVVARQLASALSYLENKNLVHG
NVCAKNILLARLGLEEGTSPFIKLSDPGVGLGVLSREERVERIPWIAPECVPGGNSLSTAADKWGFGATL
LEICFNGEAPLQSRTPSEKERFYQRQHRLPEPSCPELATLISQCLTYEPTQRPSFRTILRDLT
>gnl|CDD|270662 cd05077, PTK_Jak1_rpt1, Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IVQGEHLGRGTRTQIYAGILNYKDDDEDEGYSYEKEIKVILKVLDPSHRDISLAFFETASMMRQVSHKHI
VLLYGVCVRDVENIMVEEFVEFGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNI
LLAREGIDGECGPFIKLSDPGIPITVLSRQECVERIPWIAPECVEDSKNLSIAADKWSFGTTLWEICYNG
EIPLKDKTLAEKERFYEGQCMLVTPSCKELADLMTHCMNYDPNQRPFFRAIMRDIN
>gnl|CDD|270663 cd05078, PTK_Jak2_rpt1, Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2. Jak2 is widely expressed in many tissues. It is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LIFNESLGQGTFTKIFKGIRREVGDYGQLHETEVLLKVLDKAHRNYSESFFEAASMMSQLSHKHLVLNYG
VCVCGDENILVQEYVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEEKTLVHGNVCAKNILLIRE
EDRKTGNPPFIKLSDPGISITVLPKDILLERIPWVPPECIENPKNLSLATDKWSFGTTLWEICSGGDKPL
SALDSQRKLQFYEDRHQLPAPKWTELANLINNCMDYEPDHRPSFRAIIRDLN
>gnl|CDD|173644 cd05079, PTKc_Jak1_rpt2, Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVK
YKGICTEDGGNGIKLIMEFLPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNV
LVESEHQVKIGDFGLTKAIETDKEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCD
SESSPMTLFLKMIGPTHGQMTVTRLVRVLEEGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGF
EAIL
>gnl|CDD|270664 cd05080, PTKc_Tyk2_rpt2, Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FHKRYLKKIRDLGEGHFGKVSLYCYDPTNDGTGEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVK
YKGCCSEQGGKSLQLIMEYVPLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLL
DNDRLVKIGDFGLAKAVPEGHEYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSS
QSPPTKFLEMIGIAQGQMTVVRLIELLERGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILKT
VHE
>gnl|CDD|270665 cd05081, PTKc_Jak3_rpt2, Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FEERHLKYISQLGKGNFGSVELCRYDPLGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKY
RGVSYGPGRRSLRLVMEYLPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNIL
VESEAHVKIADFGLAKLLPLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDK
SCSPSAEFLRMMGCERDVPALCRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLD
MLW
>gnl|CDD|133213 cd05082, PTKc_Csk, Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
WALNMKELKLLQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQAFLAEASVMTQLRHSNLVQLLGVIVE
EKGGLYIVTEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNV
AKVSDFGLTKEASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVP
RVEKGYKMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQLREQLEHI
>gnl|CDD|270666 cd05083, PTKc_Chk, Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
WLLNLQKLTLGEIIGEGEFGAVLQGEYMGQKVAVKNIKCDVTAQAFLEETAVMTKLQHKNLVRLLGVILH
NGLYIVMELMSKGNLVNFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAK
ISDFGLAKVGSMGVDNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAV
EKGYRMEPPEGCPPDVYSIMTSCWEAEPGKRPSFKKLREKLEKE
>gnl|CDD|270667 cd05084, PTKc_Fes, Catalytic domain of the Protein Tyrosine Kinase, Fes. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GERIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIY
IVMELVQGGDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFG
MSREEEDGVYAATGGMKQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAV
EQGVRLPCPENCPDEVYRLMEQCWEYDPRKRPSFSTVHQDLQ
>gnl|CDD|270668 cd05085, PTKc_Fer, Catalytic domain of the Protein Tyrosine Kinase, Fer. Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells
GELLGKGNFGEVYKGTLKDKTPVAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYI
VMELVPGGDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGM
SRQEDDGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEK
GYRMSAPQRCPEDIYKIMQRCWDYNPENRPKFSELQKELAA
>gnl|CDD|270669 cd05086, PTKc_Aatyk2, Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YIQEIGNGWFGKVLLGEIYTGTSVARVVVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAI
PYLLVFEFCDLGDLKTYLANQQEKLRGDSQIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLT
VKVGDYGIGFSRYKEDYIETDDKKYAPLRWTAPELVTSFQDGLLAAEQTKYSNIWSLGVTLWELFENAAQ
PYSDLSDREVLNHVIKERQVKLFKPHLEQPYSDRWYEVLQFCWLSPEKRPTAEEVHRLLTY
>gnl|CDD|270670 cd05087, PTKc_Aatyk1, Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YLKEIGHGWFGKVFLGEVNSGLSSTQVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVT
PYLLVMEFCPLGDLKGYLRSCRAAESMAPDPLTLQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLT
VKIGDYGLSHCKYKEDYFVTADQLWVPLRWIAPELVDEVHGNLLVVDQTKQSNVWSLGVTIWELFELGNQ
PYRHYSDRQVLTYTVREQQLKLPKPQLKLSLAERWYEVMQFCWLQPEQRPTAEEVHLLLSY
>gnl|CDD|133219 cd05088, PTKc_Tie2, Catalytic domain of the Protein Tyrosine Kinase, Tie2. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YPVLEWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNI
INLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYL
SQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYG
VLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM
LEERKTYVNTTLYEKFTYAGIDC
>gnl|CDD|270671 cd05089, PTKc_Tie1, Catalytic domain of the Protein Tyrosine Kinase, Tie1. Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development
WEDIKFEDVIGEGNFGQVIKAMIKKDGLKMNAAIKMLKEFASENDHRDFAGELEVLCKLGHHPNIINLLG
ACENRGYLYIAIEYAPYGNLLDFLRKSRVLETDPAFAKEHGTASTLTSQQLLQFASDVAKGMQYLSEKQF
IHRDLAARNVLVGENLVSKIADFGLSRGEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWE
IVSLGGTPYCGMTCAELYEKLPQGYRMEKPRNCDDEVYELMRQCWRDRPYERPPFSQISVQLSRMLEARK
AYVNMALFENFTYAGID
>gnl|CDD|270672 cd05090, PTKc_Ror1, Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ELPLSAVRFMEELGECAFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIV
CLLGVVTQEQPVCMLFEFMNQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYL
SSHFFVHKDLAARNILVGEQLHVKISDLGLSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIW
SFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDIHARL
RSW
>gnl|CDD|270673 cd05091, PTKc_Ror2, Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KEINLSAVRFMEELGEDRFGKVYKGHLFGTAPGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPN
IVCLLGVVTKEQPMSMIFSYCSHGDLHEFLVMRSPHSDVGSTDDDKTVKSTLEPADFLHIVTQIAAGMEY
LSSHHVVHKDLATRNVLVFDKLNVKISDLGLFREVYAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDI
WSYGVVLWEVFSYGLQPYCGYSNQDVIEMIRNRQVLPCPDDCPAWVYTLMLECWNEFPSRRPRFKDIHSR
LRTW
>gnl|CDD|270674 cd05092, PTKc_TrkA, Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HIKRRDIVLKWELGEGAFGKVFLAECHNLLPEQDKMLVAVKALKEATESARQDFQREAELLTVLQHQHIV
RFYGVCTEGEPLIMVFEYMRHGDLNRFLRSHGPDAKILDGGEGQAPGQLTLGQMLQIASQIASGMVYLAS
LHFVHRDLATRNCLVGQGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSF
GVVLWEIFTYGKQPWYQLSNTEAIECITQGRELERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHSRLQA
>gnl|CDD|270675 cd05093, PTKc_TrkB, Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIV
KFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNRPAELTQSQMLHIAQQIAAGMVYLASQH
FVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGV
VLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLA
KASPVYLD
>gnl|CDD|270676 cd05094, PTKc_TrkC, Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIV
KFYGVCGDGDPLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIATQIASGMVYLA
SQHFVHRDLATRNCLVGANLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWS
FGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILH
ALGKATP
>gnl|CDD|270677 cd05095, PTKc_DDR2, Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K)
EFPRKLLTFKEKLGEGQFGEVHLCEAEGMEKFMDKDFALEVSENQPVLVAVKMLRADANKNARNDFLKEI
KIMSRLKDPNIIRLLAVCITDDPLCMITEYMENGDLNQFLSRQQPEGQLALPSNALTVSYSDLRFMAAQI
ASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKF
TTASDVWAFGVTLWETLTFCREQPYSQLSDEQVIENTGEFFRDQGRQTYLPQPALCPDSVYKLMLSCWRR
DTKDRPSFQEIHTLLQE
>gnl|CDD|133227 cd05096, PTKc_DDR1, Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KFPRGHLLFKEKLGEGQFGEVHLCEVVNPQDLPTLQFPFNVRKGRPLLVAVKILRPDANKNARNDFLKEV
KILSRLKDPNIIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHHLDDKEENGNDAVPPAHCLPAISYSSL
LHVALQIASGMKYLSSLNFVHRDLATRNCLVGENLTIKIADFGMSRNLYAGDYYRIQGRAVLPIRWMAWE
CILMGKFTTASDVWAFGVTLWEILMLCKEQPYGELTDEQVIENAGEFFRDQGRQVYLFRPPPCPQGLYEL
MLQCWSRDCRERPSFSDIHAFLTE
>gnl|CDD|133228 cd05097, PTKc_DDR_like, Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EFPRQQLRLKEKLGEGQFGEVHLCEAEGLAEFLGEGAPEFDGQPVLVAVKMLRADVTKTARNDFLKEIKI
MSRLKNPNIIRLLGVCVSDDPLCMITEYMENGDLNQFLSQREIESTFTHANNIPSVSIANLLYMAVQIAS
GMKYLASLNFVHRDLATRNCLVGNHYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMAWESILLGKFTT
ASDVWAFGVTLWEMFTLCKEQPYSLLSDEQVIENTGEFFRNQGRQIYLSQTPLCPSPVFKLMMRCWSRDI
KDRPTFNKIHHFLRE
>gnl|CDD|270678 cd05098, PTKc_FGFR1, Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEME
MMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGMEYCYNPSHNPEEQLSSKDLVSC
AYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALF
DRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQ
RPTFKQLVEDLDRIVALTSNQE
>gnl|CDD|133230 cd05099, PTKc_FGFR4, Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LPLDPKWEFPRDRLVLGKPLGEGCFGQVVRAEAYGIDKSRPDQTVTVAVKMLKDNATDKDLADLISEMEL
MKLIGKHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDYTFDITKVPEEQLSFKDLVSCA
YQVARGMEYLESRRCIHRDLAARNVLVTEDNVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFD
RVYTHQSDVWSFGILMWEIFTLGGSPYPGIPVEELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQR
PTFKQLVEALDKVLAAVSEEYLDLSMPFEQYSPS
>gnl|CDD|173652 cd05100, PTKc_FGFR3, Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LPADPKWELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDKPNKPVTVAVKMLKDDATDKDLSDLVSEMEM
MKMIGKHKNIINLLGACTQDGPLYVLVEYASKGNLREYLRARRPPGMDYSFDTCKLPEEQLTFKDLVSCA
YQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFD
RVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQR
PTFKQLVEDLDRVLTVTSTDEYLDLSVPFEQYSPGCPDSPSSCSSGDDSVFAHD
>gnl|CDD|270679 cd05101, PTKc_FGFR2, Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DAPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATE
KDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPE
EQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRL
PVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMM
MRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEE
>gnl|CDD|270680 cd05102, PTKc_VEGFR3, Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QWEFPRDRLRLGKVLGHGAFGKVVEASAFGIDKSSSCETVAVKMLKEGATASEHKALMSELKILIHIGNH
LNVVNLLGACTKPNGPLMVIVEFCKYGNLSNFLRAKREGFSPYRERSPRTRSQVRSMVEAVRADRRSRQG
SDRVASFTESTSSTNQPRQEVDDLWQSPLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNV
VKICDFGLARDIYKDPDYVRKGSARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQI
NEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKERPTFSDLVEILGDLLQEN
>gnl|CDD|270681 cd05103, PTKc_VEGFR2, Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHH
LNVVNLLGACTKPGGPLMVIVEFCKFGNLSAYLRSKRSEFVPYKTKGARFRQGKDYVGDISVDLKRRLDS
ITSSQSSASSGFVEEKSLSDVEEEEAGQEDLYKDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNI
LLSENNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGAS
PYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQAN
>gnl|CDD|270682 cd05104, PTKc_Kit, Catalytic domain of the Protein Tyrosine Kinase, Kit. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YEIQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRDRLRFGKTLGAGAFGKVVEATAYGLAKADSAMTVAV
KMLKPSAHSTEREALMSELKVLSYLGNHINIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRDSFICP
KFEDLAEAALYRNLLHQREMACDSLNEYMDMKPSVSYVVPTKADKRRGVRSGSYVDQDVTSEILEEDELA
LDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNYVVKGNARLPV
KWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMPVDSKFYKMIKEGYRMDSPEFAPSEMYDIM
RSCWDADPLKRPTFKQIVQLIEQQL
>gnl|CDD|173653 cd05105, PTKc_PDGFR_alpha, Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKV
AVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDNFL
SRHPEKPKKDLDIFGINPADESTRSYVILSFENKGDYMDMKQADTTQYVPMLEIKEASKYSDIQRSNYDR
PASYKGSNDSEVKNLLSDDGSEGLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICD
FGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMIVDSTFY
NKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESLLPS
>gnl|CDD|133237 cd05106, PTKc_CSF-1R, Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KPKYEIRWKIIEAAEGNNYTFIDPTQLPYNEKWEFPRDNLQFGKTLGAGAFGKVVEATAFGLGKEDNVLR
VAVKMLKASAHTDEREALMSELKILSHLGQHKNIVNLLGACTHGGPVLVITEYCCYGDLLNFLRKKAETF
LNFVMALPEISETSSDYKNITLEKKYIRSDSGFSSQGSDTYVEMRPVSSSSSQSSDSKDEEDTEDSWPLD
LDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIMNDSNYVVKGNARLPVKW
MAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGILVNSKFYKMVKRGYQMSRPDFAPPEIYSIMKM
CWNLEPTERPTFSQISQLIQRQLG
>gnl|CDD|133238 cd05107, PTKc_PDGFR_beta, Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YEIRWKVIESVSSDGHEYIYVDPMQLPYDSAWEMPRDNLVLGRTLGSGAFGRVVEATAHGLSHSQSTMKV
AVKMLKSTARSSEKQALMSELKIMSHLGPHLNIVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFL
QYYLDKNRDDGSLISGGSTPLSQRKSHVSLGSESDGGYMDMSKDESADYVPMQDMKGTVKYADIESSNYE
SPYDQYLPSAPERTRRDTLINESPALSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKI
CDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQ
FYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDLLT
>gnl|CDD|270683 cd05108, PTKc_EGFR, Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPH
VCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNV
LVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSK
PYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQG
DERMHLPSPTDSNFYRALMDEEDMDDVVDADEY
>gnl|CDD|270684 cd05109, PTKc_HER2, Catalytic domain of the Protein Tyrosine Kinase, HER2. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
MRILKETELKKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPY
VCRLLGICLTSTVQLVTQLMPYGCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNV
LVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAK
PYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVDEFSRMARDPSRFVVIQ
>gnl|CDD|173655 cd05110, PTKc_HER4, Catalytic domain of the Protein Tyrosine Kinase, HER4. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LRILKETELKRVKVLGSGAFGTVYKGIWVPEGETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPH
LVRLLGVCLSPTIQLVTQLMPHGCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNV
LVKSPNHVKITDFGLARLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGK
PYDGIPTREIPDLLEKGERLPQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQRYLVIQG
DDRMKLPSPNDSKFFQNLLDEED
>gnl|CDD|173656 cd05111, PTK_HER3, Pseudokinase domain of the Protein Tyrosine Kinase, HER3. HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ARIFKETELRKLKVLGSGVFGTVHKGIWIPEGDSIKIPVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAY
IVRLLGICPGASLQLVTQLLPLGSLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNV
LLKSPSQVQVADFGVADLLYPDDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAE
PYAGMRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYLVIK
>gnl|CDD|133243 cd05112, PTKc_Itk, Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IDPSELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLE
QAPICLVFEFMEHGCLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVK
VSDFGMTRFVLDDQYTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEV
VEDINAGFRLYKPRLASTHVYEIMNHCWKERPEDRPSFSLLLRQLA
>gnl|CDD|173657 cd05113, PTKc_Btk_Bmx, Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTK
QRPIFIITEYMANGCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVK
VSDFGLSRYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSET
VEHVSQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILLSNIL
>gnl|CDD|270685 cd05114, PTKc_Tec_Rlk, Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
INPSELTFMKELGSGLFGVVRLGKWRAQYKVAIKAIREGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQ
QKPIYIVTEFMENGCLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVK
VSDFGMTRYVLDDQYTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEV
VEMVSRGHRLYRPKLASKSVYEVMYSCWHEKPEGRPTFADLLRTITEIAE
>gnl|CDD|270686 cd05115, PTKc_Zap-70, Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KRDNLLIDEVELGSGNFGCVKKGVYKMRKKQIDVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMI
GVCEAEALMLVMEMASGGPLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQ
HYAKISDFGLSKALGADDSYYKARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKK
MKGPEVMSFIEQGKRMDCPAECPPEMYALMSDCWIYKWEDRPNFLTVEQRMRTYYYSIA
>gnl|CDD|133247 cd05116, PTKc_Syk, Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GELGSGNFGTVKKGYYQMKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAESW
MLVMEMAELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFG
LSKALRADENYYKAQTHGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQM
IEKGERMECPAGCPPEMYDLMKLCWTYDVDERPGFAAVELRLRNYYY
>gnl|CDD|270687 cd05117, STKc_CAMK, The catalytic domain of CAMK family Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFED
DKNLYLVMELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSP
IKIIDFGLAKIFEEGEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELF
EKILKGKYSFDSPEWKNVSEEAKDLIKRLLVVDPKKRLTAAEALNHPW
>gnl|CDD|270688 cd05118, STKc_CMGC, Catalytic domain of CMGC family Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLKHLNDVEGHPNIVKLLDVFEH
RGGNHLCLVFELMGMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQ
LKLADFGLARSFTSPPYTPYVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQL
AKIVRLLGTPEALDLLSKMLKYDPAKRITASQALAHPYF
>gnl|CDD|270689 cd05119, RIO, Catalytic domain of the atypical protein serine kinases, RIO kinases. RIO kinases are atypical protein serine kinases present in archaea, bacteria and eukaryotes. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. RIO kinases contain a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. Most organisms contain at least two RIO kinases, RIO1 and RIO2. A third protein, RIO3, is present in multicellular eukaryotes. In yeast, RIO1 and RIO2 are essential for survival. They function as non-ribosomal factors necessary for late 18S rRNA processing. RIO1 is also required for proper cell cycle progression and chromosome maintenance. The biological substrates for RIO kinases are still unknown. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K)
IGGVISTGKEANVFYADGVFDGKPVACAVKIYRIETSEFDKVDEYLYGDERFDYRRISPKEKVFIWTEKE
FRNLERAKEAGVSVPQPYTYEKNVLLXEFIGEDELPAPTLVELGRELKELDVEGIFNDVVENVKRLYQEA
ELVHADLSEYNILYIDKVYFIDFGQAVTLRHPGAESYLERDVRNIIRFFSKY
>gnl|CDD|270690 cd05120, APH_ChoK_like, Aminoglycoside 3'-phosphotransferase and Choline Kinase family. This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K)
ISVKLIKEGGDNKVYLLGDPREYVLKIGPPRLKKDLEKEAAMLQLLAGKLSLPVPKVYGFGESDGWEYLL
MERIEGETLSEVWPRLSEEEKEKIADQLAEILAALHRIDSSVLTHGDLHPGNILVKPDGKLSGIIDWEFA
GYGPPAFDYAAALRDWTE
>gnl|CDD|270691 cd05121, ABC1_ADCK3-like, Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and similar proteins. This family is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. Eukaryotes contain at least two more ABC1/ADCK3-like proteins: in humans, these are the putative atypical protein kinases named ADCK1 and ADCK2. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Eight of these plant ABC1 kinase subfamilies (ABC1K1-8) are specific for photosynthetic organisms. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family
KLQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEII
EADLRILRRLARLLERLSPLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVYVPKVYP
ELSTRRVLVMEYIDGVKLTDLEALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIA
LLDFGMVGRLDPETREALADLLLALVNGDAEGLAEAL
>gnl|CDD|270692 cd05122, PKc_STE, Catalytic domain of STE family Protein Kinases. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKD
ELWIVMEFCSGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLI
DFGLSAQLSDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIA
TNGPPGLRNPKKWSKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI
>gnl|CDD|270693 cd05123, STKc_AGC, Catalytic domain of AGC family Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase
LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYL
VLDYVPGGELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLA
KELSSDGDRTYTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPL
KFPEYVSPEAKSLISGLLQKDPTKRLGSGGAEEIKAHPFF
>gnl|CDD|270694 cd05124, AFK, Catalytic domain of Actin-Fragmin Kinase. AFK is found in slime molds, ciliates, and flowering plants. It catalyzes the transfer of the gamma-phosphoryl group from ATP specifically to threonine residues in the actin-fragmin complex. The phosphorylation sites are located at a minor contact site for DNase I and at an actin-actin contact site. Fragmin is an actin-binding protein that functions as a regulator of the microfilament system. It interferes with the growth of F-actin by severing actin filaments and capping their ends. The phosphorylation of the actin-fragmin complex inhibits its nucleation activity and results in calcium-dependent capping activity. Thus, AFK plays a role in regulating actin polymerization. The AFK catalytic domain is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SIEAVDRSGSGSSGVFFVETEEEGAVVVKGSPTIAQEVFASKLAEILGVPTPQMRVLSWSSPEWKEMSRA
LLEASENDDVLELKIALELDRAFLLIMEYVPGGTLFNMGPHRAYFSGPKGEERLIQLGRIIALDIFINNF
DRLPLIIWDNRGNPSNLLFYEINGWYEVLIDSNITCLDNDSFTIYGRDVITLLKLLLFSPGTESQQIARM
RDYIIKYLNIDLGESAIQQGIALGLKSIVK
>gnl|CDD|240161 cd05125, Mth938_2P1-like, Mth938_2P1-like domain. This model contains sequences that are similar to 2P1, a partially characterized nuclear protein, which is homologous to E3-3 from rat and known to be alternatively spliced. Its function is unknown. This family is part of the Mth938 family, for which structures, but no functional data are available
NYIDAYSENGFRLNNNKVIGSGAILPKEVFSWNVSSFEDITEESLSLFELLEPRPEILVIGTGRKSRPLS
PELRKYFKKLGIAVEVVDTRNACATFNFLAEEGRRVAAALIPPG
>gnl|CDD|240162 cd05126, Mth938, Mth938 domain. Mth938 is a hypothetical protein encoded by the Methanobacterium thermoautotrophicum (Mth) genome. This protein crystallizes as a dimer, although it is monomeric in solution, with one disulfide bond in each monomer. The function of the protein has not been determined
EIESTSFGSITVGGETYEHDIVVYPDGSRARRWKELSKKTGTSHGLQPEELEELLEEGVEVIVIGTGQSG
ALKVPPETVEKLEKRGVEVLVLPTEEAVKRYNELAGKGRRVLAVIHV
>gnl|CDD|213329 cd05127, RasGAP_IQGAP_like, Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins. This family represents IQ motif containing GTPase activating protein (IQGAP) which associated with the Ras GTP-binding protein. A primary function of IQGAP proteins is to modulate cytoskeletal architecture. There are three known IQGAP family members: IQGAP1, IQGAP2 and IQGAP3. Human IQGAP1 and IQGAP2 share 62% identity. IQGAPs are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP is an essential regulator of cytoskeletal function. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity, the protein actually lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite of their similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3, only present in mammals, regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton
ASNRREEYLLLKLFKTALREEIESKVSLPEDIVTGNPTVIKLVVNYNRGPRGQKYLRELLGPVVKEILDD
DDLDLETDPVDIYKAWINQEESRTGEPSKLPYDVTREQALKDPEVRKRLIEHLEKLRAITDKFLTAITES
LDKMPYGMRYIAKVLKEALREKFPDAPEEEILKIVGNLLYYRYMNPAIVAPEAFDIIDLSVGGQLSPLQR
RNLGSIAKVLQQAASGKLFGGENPYLSPLNPYISESHEKFKKFFLEACTVPEAEEHFNIDEYSDLTMLTK
PTIYISLQEIFATHKLLLEHQDEIAPDPDDPLRELLDDLGPAPTIESLLGS
>gnl|CDD|213330 cd05128, RasGAP_GAP1_like, Ras-GTPase Activating Domain of GAP1 and similar proteins. The GAP1 family of Ras GTPase-activating proteins includes GAP1(m) (or RASA2), GAP1_IP4BP (or RASA3), Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), and Ras GTPase activating-like proteins (RASAL) or RASAL1. The members are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin homology domain that is associated with a Bruton's tyrosine kinase motif. While this domain structure is conserved, a small change in the function of each individual domain and the interaction between domains has a marked effect on the regulation of each protein
QYYEPLLNLLLESLDVPPFTASAVYLLEELVKVDKDDVARPLVRIFLHHGQIVPLLRALASREISKTQDP
NTLFRGNSLASKCMDEFMKLVGMQYLHETLKPVIDEIFSEKKSCEIDPSKLKDGEVLETNLANLRGYVER
VFKAITSSARRCPTLMCEIFSDLRESAAQRFPDNEDVPYTAVSGFIFLRFFAPAILNPKLFGLREEHPDP
QTARTLTLISKTIQTLGNLGSSSSGLGVKEAYMSPLYERFTDEQHVDAVKKFLDRISSV
>gnl|CDD|213331 cd05129, RasGAP_RAP6, Ras-GTPase Activating Domain of Rab5-activating protein 6. Rab5-activating protein 6 (RAP6) is an endosomal protein with a role in the regulation of receptor-mediated endocytosis. RAP6 contains a Vps9 domain, which is involved in the activation of Rab5, and a Ras GAP domain (RGD). Rab5 is a small GTPase required for the control of the endocytic route, and its activity is regulated by guanine nucleotide exchange factor, such as Rabex5, and GAPs, such as RN-tre. Human Rap6 protein is localized on the plasma membrane and on the endosome. RAP6 binds to Rab5 and Ras through the Vps9 and RGD domains, respectively
DAYKLLGYQLSHYGEFLRILRENPQLLAECLARGEKLSLEQTQNVIQTIVTSLYGNCIMPEDERLLLQLL
RELMELQLKKSDNPRRLLRKGSCAFSRVFKLFTELLFSAKLYLTAALHKPIMQVLVDDEIFLETDPQKAL
CRFSPAEQEKRFGEEGTPEQQRKLQQYRAEFLSRLVALVNKFISSLRQSVYCFPQSLRWIVRQLRKILTR
SGDDEEAEARALCTDLLFTNFICPAIVNPEQYGIISDAPISEVARHNLMQVAQILQVLALTEFESPDPRL
KELLSKFDKDCVSAFLDVVIVGRAVETPPPSSSALLEGSRTAVLITESDLATLVEFLRSVKTGDEEKEDQ
MALDNLLKNLPPASP
>gnl|CDD|213332 cd05130, RasGAP_Neurofibromin, Ras-GTPase Activating Domain of neurofibromin. Neurofibromin is the product of the neurofibromatosis type 1 gene (NF1) and shares a region of similarity with catalytic domain of the mammalian p120RasGAP protein and an extended similarity with the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2. Neurofibromin has been shown to function as a GAP (GTPase-activating protein) which inhibits low molecular weight G proteins such as Ras by stimulating their intrinsic GTPase activity. NF1 is a common genetic disorder characterized by various symptoms ranging from predisposition for the development of tumors to learning disability or mental retardation. Loss of neurofibromin activity can be correlated to the increase in Ras-GTP concentration in neurofibromas of NF1 of patients, supporting the notion that unregulated Ras signaling may contribute to their development
ETVLADRFERLVELVTMMGDDGELPIAMALANVVPCSQMDELARVLVTLFDSKHLLYQLLWNMFSKEVEL
ADSMQTLFRGNSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEWVSYEVDPTRLEGNENLEENQRNL
LQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRFPNSGLGAVGSAIFLRFINPAIVSPYEYGILDRE
PPPRVKRGLKLMSKILQNIANHVLFTKEAHMLPFNDFLRNHFEAGRRFFSSIASDCGAVDGPSSKYLSFI
NDANVLALHRLLWNNQEKIGQYLASSRDHKAVGRRPFDKMATLLAYLGPPGH
>gnl|CDD|213333 cd05131, RasGAP_IQGAP2, Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2. IQGAP2 is a member of the IQGAP family that contains a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeat, a single WW domain, four IQ motifs which mediate interactions with calmodulin, and a Ras-GTPase-activating protein (GAP)-related domain that binds Rho family GTPases. IQGAP2 and IQGAP3 play important roles in the regulation of the cytoskeleton for axon outgrowth in hippocampal neurons and are thought to stay in a common regulatory pathway. The results of RNA interference studies indicated that IQGAP3 partially compensates functions of IQGAP2, but has lesser ability than IQGAP2 to promote axon outgrowth in hippocampal neuron. Moreover, IQGAP2 is required for the cadherin-mediated cell-to-cell adhesion in Xenopus laevis embryos
DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLL
APVVKEIIEDKSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVT
DKVLGSIFSSLDLIPYGMRYIAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMT
AGGQIHSEQRRNLGSVAKVLQHAASNKLFEGENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNID
EYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQNDLLHELLKDLGEVPDVESFLGEGTVDPNDPN
KENTLSQLG
>gnl|CDD|213334 cd05132, RasGAP_GAPA, Ras-GTPase Activating Domain of GAPA. GAPA is an IQGAP-related protein and is predicted to bind to small GTPases, which are yet to be identified. IQGAP proteins are integral components of cytoskeletal regulation. Results from truncated GAPAs indicated that almost the entire region of GAPA homologous to IQGAP is required for cytokinesis in Dictyostelium. More members of the IQGAP family are emerging, and evidence suggests that there are both similarities and differences in their function
EIDSLLQTVMFTLYGNQYESREEHLLLSMFQSVLTYEFDETTEFGSLLRANTAVSRMMTTYTRRGPGQSY
LKTVLADRINDLISLKDLNLEINPLKVYEQMINDIELDTGLPSNLPRGITPEEAAENPAVQNIIEPRLEM
LEEITNSFLEAIINSLDEVPYGIRWICKQIRSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYM
LVDGKPSDNTRRTLTLIAKLLQNLANKPSYSKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELD
QYIALSKKDLSINITLNEIYNTHSLLVKHLAELAPDHNDHLRLILQELGPAPPQVPRKENRTIELPLYSR
WE
>gnl|CDD|213335 cd05133, RasGAP_IQGAP1, Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1. IQGAP1 is a homodimeric protein that is widely expressed among vertebrate cell types from early embryogenesis. Mammalian IQGAP1 protein is the best characterized member of the IQGAP family, and contains several protein-interacting domains. Human IQGAP1 is most similar to mouse Iqgap1 (94% identity) and has 62% identity to human IQGAP2. IQGAP1 binds and cross-links actin filaments in vitro and has been implicated in Ca2+/calmodulin signaling, E-cadherin-dependent cell adhesion, cell motility, and invasion. Yeast IQGAP homologs have a role in the recruitment of actin filaments, are components of the spindle pole body, and are required for actomyosin ring assembly and cytokinesis. Furthermore, IQGAP1 over-expression has also been detected in gastric and colorectal carcinomas and gastric cancer cell lines
DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQIL
APVVKEIMDDKSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVT
DKFLSAIISSVDKIPYGMRFIAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLS
AGGQLTTDQRRNLGSIAKMLQHAASNKMFLGDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVD
EYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHNDPIHELLDDLGEVPTIESLIGENPGPPGDPN
RETLAKTEVSLTLTNKFDVPGDENAEMDAR
>gnl|CDD|213336 cd05134, RasGAP_RASA3, Ras-GTPase Activating Domain of RASA3. RASA3 (or GAP1_IP4BP) is a member of the GAP1 family and has been shown to specifically bind 1,3,4,5-tetrakisphosphate (IP4). Thus, RASA3 may function as an IP4 receptor. The members of GAP1 family are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. Purified RASA3 stimulates GAP activity on Ras with about a five-fold lower potency than p120RasGAP, but shows no GAP-stimulating activity at all against Rac or Rab3A
SEYYSPLRDLLLKSADVEPVSASAAHILGEVCREKQEAAIPLVRLFLHYGKIVPFISAIASAEVNRTQDP
NTIFRGNSLTSKCIDETMKLAGMHYLQVTLKPIIDEICQEHKPCEIDPVKLKDGENLENNRENLRQYVDR
IFRVITKSGVSCPTVMCDIFFSLRESAAKRFQVDPDVRYTAVSSFIFLRFFAPAILSPNLFQLTPHHPDP
QTSRTLTLISKTIQTLGSLSKSKSANFKESYMAAFYDYFNEQKYADAVKNFLDLISSSG
>gnl|CDD|213337 cd05135, RasGAP_RASAL, Ras-GTPase Activating Domain of RASAL1 and similar proteins. Ras GTPase activating-like protein (RASAL) or RASAL1 is a member of the GAP1 family, and a Ca2+ sensor responding in-phase to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. It contains a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL, like Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to receptor-mediated elevation in the concentration of intracellular free Ca2+, a translocation that activates its ability to function as a RasGAP. However, unlike RASAL4, RASAL undergoes an oscillatory translocation to the plasma membrane that occurs in synchrony with repetitive Ca2+ spikes
PSQYYQPLIDLLVESVQSPAEAEDSTPLAMLEEVTTGESRQDVATKLVKIFLGQGLVVPFLDYLNTREVG
RTTDPNTLFRSNSLASKSMEQFMKVVGMPYLHEVLKPVINRIFEEKKYVELDPCKIDLNRTRRISFKGSL
SEAQVRESSLELLQGYLGSIIDAIVGSVDQCPPVMRVAFKQLHKRVEERFPEAEHQDVKYLAISGFLFLR
FFAPAILTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNLGLQLGQGKEQWMAPLHPFILQSVARVKDFL
DRLIDID
>gnl|CDD|213338 cd05136, RasGAP_DAB2IP, Ras-GTPase Activating Domain of DAB2IP and similar proteins. The DAB2IP family of Ras GTPase-activating proteins includes DAB2IP, nGAP, and Syn GAP. Disabled 2 interactive protein, (DAB2IP; also known as ASK-interacting protein 1 (AIP1)), is a member of the GTPase-activating proteins, down-regulates Ras-mediated signal pathways, and mediates TNF-induced activation of ASK1-JNK signaling pathways. The mechanism by which TNF signaling is coupled to DAB2IP is not known
RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVD
RLDDEHLIFRGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSASLSRNQANLR
RSVELAWCKILSSHCVFPRELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEY
PSERAARNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYID
LGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITEALRNP
>gnl|CDD|213339 cd05137, RasGAP_CLA2_BUD2, Ras-GTPase Activating Domain of CLA2/BUD2. CLA2/BUD2 functions as a GTPase-activating protein (GAP) for BUD1/RSR1 and is necessary for proper bud-site selection in yeast. BUD2 has sequence similarity to the catalytic domain of RasGAPs, and stimulates the hydrolysis of BUD1-GTP to BUD1-GDP. Elimination of Bud2p activity by mutation causes a random budding pattern with no growth defect. Overproduction of Bud2p also alters the budding pattern
KVRLDENVVLPSKNYKPLEELLHNFDLGLTLQIAELVPGDKLERLSEILLDIFQASGREDEWFMALVEDE
IDGIDKSTSKNKDMGKSSNNEANLLFRGNSLLTKSLEKYMRRIGKEYLEKSIGDVIRKICEENKDCEVDP
SRVKESDSIEKEEDLEENWENLISLTEEIWNSIYITSNDCPPELRKILKHIRAKVEDRYGDFLRTVTLNS
VSGFLFLRFFCPAILNPKLFGLLKDHPRPRAQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLTTHRE
ELKDYIDKITGIKLDFTPKILPLSYSTPIRILGRLPPLSREGLPTLPYLIDKYRRLAELVSLWTDANPES
ESVSNS
>gnl|CDD|240163 cd05140, Barstar_AU1054-like, Barstar_AU1054-like contains uncharacterized sequences similar to the uncharacterized, predicted RNAase inhibitor AU1054 found in Burkholderia cenocepacia. This is a subfamily of the Barstar family of RNAase inhibitors. Barstar is an intracellular inhibitor of barnase, an extracellular ribonuclease of Bacillus amyloliquefaciens. Barstar binds tightly to the barnase active site and sterically blocks it thus inhibiting its potentially lethal RNase activity inside the cell. Barstar also binds and inhibits a ribonuclease called RNase Sa (produced by Streptomyces aureofaciens) which belongs to the same enzyme family as does barnase
ITIDLSDITSERELHELLKECLGFPGWYGCNWDAFWDAITGLVSMPPVLRFVGWSQFKRRLPRDAELLKE
CLDDMQEEYPQIAARV
>gnl|CDD|240164 cd05141, Barstar_evA4336-like, Barstar_evA4336-like contains uncharacterized sequences similar to the uncharacterized, predicted RNAase inhibitor evA4336 found in Azoarcus sp. EvN1. This is a subfamily of the Barstar family of RNAase inhibitors. Barstar is an intracellular inhibitor of barnase, an extracellular ribonuclease of Bacillus amyloliquefaciens. Barstar binds tightly to the barnase active site and sterically blocks it thus inhibiting its potentially lethal RNase activity inside the cell. Barstar also binds and inhibits a ribonuclease called RNase Sa (produced by Streptomyces aureofaciens) which belongs to the same enzyme family as does barnase
IVLDLSGIADKAALLDALAAALDFPSWFGHNWDALADCLTDLSWWPAEGYVLVLRDGDALRAADPEDFAT
LLEILRDAADE
>gnl|CDD|240165 cd05142, Barstar, Barstar is an intracellular inhibitor of barnase, an extracellular ribonuclease of Bacillus amyloliquefaciens. Barstar binds tightly to the barnase active site and sterically blocks it thus inhibiting its potentially lethal RNase activity inside the cell. Barstar also binds and inhibits a ribonuclease called RNase Sa (produced by Streptomyces aureofaciens) which belongs to the same enzyme family as does barnase
KVVIDGEEIRSIEDLHQILKKELALPEYYGENLDALWDCLTGWVELPLTIEWKNFEQSKQRLGNYAESLL
QVFAEAEEEGGDLKFNV
>gnl|CDD|240166 cd05143, Barstar_SaI14_like, Barstar_SaI14_like contains sequences that are similar to SaI14, an RNAase inhibitor, which are members of the Barstar family. Barstar is an intracellular inhibitor of barnase, an extracellular ribonuclease of Bacillus amyloliquefaciens. Barstar binds tightly to the barnase active site and sterically blocks it thus inhibiting its potentially lethal RNase activity inside the cell. The sequences in this subfamily are mostly uncharacterized, but believed to have a similar function and role
YVIDGASINTLADFFCEIGEAINGEGGYFGPNLDALADCLRGGYGAPDDGPFRLVWRNHAHSRTALGEDE
TARQLELRLAEPHPINEE
>gnl|CDD|270695 cd05144, RIO2_C, C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase. RIO2 is present in archaea and eukaryotes. It contains an N-terminal winged helix (wHTH) domain and a C-terminal RIO kinase catalytic domain. The wHTH domain is primarily seen in DNA-binding proteins, although some wHTH domains may be involved in RNA recognition. RIO2 is essential for survival and is necessary for rRNA cleavage during 40S ribosomal subunit maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO2 kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K)
ISSVGNQIGVGKESDVYLALDEDGNPVVLKFHRLGRTSFRKVKRKRDYLKHRKHASWLYLSRLAAEKEFA
ALKALYEEGFPVPKPIDWNRHAVVMELIDGYPLYQVRLLEDPEEVLDEILELIVKLAKHGLIHGDFSEFN
ILVDEDEKITVIDFPQMVSTSHPNAEEYFDRDVECIIKFFRRK
>gnl|CDD|270696 cd05145, RIO1_like, Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar proteins. RIO1 is present in archaea, bacteria and eukaryotes. In addition, RIO3 is present in multicellular eukaryotes. Both RIO1 and RIO3 are associated with precursors of 40S ribosomal subunits, just like RIO2. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. The specific function of RIO3 is unknown. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K)
LGGVISTGKEANVYLARGGDGEPVAVKIYRTSTSSFKKMAKYIEGDPRFESRRRGNRRKLIFAWARKEFR
NLKRLYEAGVRVPEPIAVYRNVLVMEFIGDDGSPAPRLKDVELEEEDAEELYEQVVEQMRRMYCKAGLVH
GDLSEYNILYYDGKPVIIDVSQAVTLDHPNAEEFLRRDIRNINRFFSRK
>gnl|CDD|270697 cd05146, RIO3_euk, Catalytic domain of the atypical protein serine kinase, RIO3 kinase. RIO3 is present only in multicellular eukaryotes. It is associated with precursors of 40S ribosomal subunits, just like RIO1 and RIO2. Its specific function is still unknown. Like RIO1 and RIO2, it may be involved in ribosomal subunit processing and maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO3 kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K)
VNGCISTGKEAVVFHANGGSMEEVLLPPECAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSKQNPRKIIRL
WAEKEMHNLKRMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMY
NECHLVHADLSEYNILWHEGKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR
>gnl|CDD|270698 cd05147, RIO1_euk, Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase. RIO1 is present in archaea, bacteria and eukaryotes. This subfamily is composed of RIO1 proteins from eukaryotes. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. It is associated with precursors of 40S ribosomal subunits, just like RIO2. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K)
INGCISTGKEANVYHATTKNGGELAIKVYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVKTWAEKEM
RNLKRLNQAGIPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLV
HADLSEYNLLYHKGKVYIIDVSQSVEHDHPHALEFLRRDCVNVNDFFRKK
>gnl|CDD|133248 cd05148, PTKc_Srm_Brk, Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
WERPREEFTLERKLGSGYFGEVWEGLWKNRVRVAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAV
CSVGEPVYIITELMEKGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGED
LVCKVADFGLARLIKEDVYLSSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNN
HEVYDQITAGYRMPCPAKCPQEIYKIMLECWAAEPEDRPSFKALREELDNI
>gnl|CDD|270699 cd05150, APH, Aminoglycoside 3'-phosphotransferase. APH catalyzes the transfer of the gamma-phosphoryl group from ATP to aminoglycoside antibiotics such as kanamycin, streptomycin, neomycin, and gentamicin, among others. The aminoglycoside antibiotics target the 30S ribosome and promote miscoding, leading to the production of defective proteins which insert into the bacterial membrane, resulting in membrane damage and the ultimate demise of the bacterium. Phosphorylation of the aminoglycoside antibiotics results in their inactivation, leading to bacterial antibiotic resistance. The APH gene is found on transposons and plasmids and is thought to have originated as a self-defense mechanism used by microorganisms that produce the antibiotics. The APH subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K)
YRWEPDTIGESGARVYRLDGGGPVLYLKTAPAGYAYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLL
TTALPGRDAASLEPLLDPERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDEDDFDEE
RQGRTAEELLAELEATRPAEEDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLREN
LGGEEYAERFLDAYGIDAPDPERLAYYRLLDEFF
>gnl|CDD|270700 cd05151, ChoK-like, Choline Kinase and similar proteins. This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K)
ITIEPLKGGLTNKNYLVEVAGKKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEVIYFDPETGVKIT
EFIEGATLLTNDFSDPENLERIAALLRKLHSSPLEDLVLCHNDLVPGNFLLDDDRLYLIDWEYAGMNDPL
FDLAALFSENNL
>gnl|CDD|270701 cd05152, MPH2', Macrolide 2'-Phosphotransferase. MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K)
LALAAKHGLDLKPATLRLNESGLDFQVAFARDTEGRRWVLRIPRRPDVSERLEAEKKVLDLVTPHLPFAV
PDWRIHTPELIAYPLLPGVPAATIDPEIQNYVWNWDPLAPPPVFARSLGKALAALHSIPADLAAAAGLPV
YTAEEVRARMAARMDRVKETFGVPPALLARWQAWLADDSLWPFHTVLVHGDLHPGHILVDEDGRVTGLID
WTEAKVGDPADDFAWHYAAFGEEALERLLDAYEKAGGEVWPRMLEHIIELAAAYPLTIALFALDSG
>gnl|CDD|270702 cd05153, HomoserineK_II, Type II Homoserine Kinase. This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K)
DEELAEFLAHYDLGELLSFEGIAAGIENTNYFVTTTDGRYVLTLFEKRRSAAELPFELELLDHLAQAGLP
VPRPLADKDGELLGELNGKPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFPPPRPNPRGLAWW
KPLAERLKARLDLLAADDRALLEDELARLQALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYD
PLLYDLAIALNDWCFDDDGKLDPERAKALLAGYQSVRPLTEEEKAALPLLLRAAALRFWLSRLYDFHLPR
EGALVTPKDPDEFLRRLRQR
>gnl|CDD|270703 cd05154, ACAD10_11_N-like, N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins. This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K)
LAVRRLSGGASNETYLVDAGGDGGGRRLVLRRPPPGGLLPSAHDLEREYRVLRALAGTGVPVPRVLALCE
DPSVLGAPFYVMERVDGRVLPDPLPRPDLSPEERRALARSLVDALAALHSVDPAALGLADLGRPEGYLER
QVDRWRRQLEAAATDPPPALEEALRWLRANLPADGRPVLVHGDFRLGNLLFDPDGRVTAVLDWELATLGD
PLEDLAWLLARWWRPGDPPGLAAPTRLPGFPSREELLARYEEAS
>gnl|CDD|270704 cd05155, APH_ChoK_like_1, Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase. This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). These proteins catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates, such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides, and macrolides leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K)
PILPVASSGWDNATFRLGDDLAVRLPRRAWAAELLEKEQRWLPRLAPRLPLPVPVPLALGKPGAGYPWPW
SVYRWLEGETAADAPLADPAAAAEDLARFLAALHAIDPAGPPNPGRGNPLRGRDLAVRDAEEALAALAGL
LDVAAARALWERALAAPAWAGPPVWLHGDLHPGNLLVRDGRLSAVIDFGDLGVGDPACDLAIAWTLFDAA
ARAAFRAALGVDDATWARARGWAL
>gnl|CDD|270705 cd05156, ChoK_euk, Euykaryotic Choline Kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC) and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. Along with PCho, it is involved in malignant transformation through Ras oncogenes in various human cancers such as breast, lung, colon, prostate, neuroblastoma, and hepatic lymphoma. In mammalian cells, there are three ChoK isoforms (A-1, A-2, and B) which are active in homo- or heterodimeric forms. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K)
FGIKTITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGI
FPGGRLEEFIPSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEP
TKPSKQLELLLSYDLAKELGWLRSLLESTPSPVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYCSYN
YRGFDLANHFCEWAYDYTVPEPPYFKINPENYPTREQQLHFIRAYLDEQYKDKTNDLTEERSKEEEKLLL
EVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARLDAYFKQKE
>gnl|CDD|270706 cd05157, ETNK_euk, Euykaryotic Ethanolamine kinase. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate, and displays negligible activity towards N-methylated derivatives of Etn. The Drosophila ETNK is implicated in development and neuronal function. Mammals contain two ETNK proteins, ETNK1 and ETNK2. ETNK1 selectively increases Etn uptake and phosphorylation, as well as PtdEtn synthesis. ETNK2 is found primarily in the liver and reproductive tissues. It plays a critical role in regulating placental hemostasis to support late embryonic development. It may also have a role in testicular maturation. ETNK is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K)
IKVKRITGGITNALYKVTYPSGDTPKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGR
VEEFLPGRTLTPEDLRDPKISRLIARRLAELHSIVPLGEIEGKKKPILWTTIRKWLDLAPEVFEDEKNKE
KKLEKVDLERLRKELEWLEKWLESLEKSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIAN
HFCEWAGFYCVLDYSRYPTKEEQRNFLRAYLESLDGLPGGEEVSEEEVEKLYNEVNLFRLASHLFWGLWA
LIQAAISSIDFDYLGYAKERLDEYWGD
>gnl|CDD|176646 cd05160, DEDDy_DNA_polB_exo, DEDDy 3'-5' exonuclease domain of family-B DNA polymerases. The 3'-5' exonuclease domain of family-B DNA polymerases. This domain has a fundamental role in reducing polymerase errors and is involved in proofreading activity. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. This domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The exonuclease domain of family B polymerase also contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation. Members include Escherichia coli DNA polymerase II, some eubacterial phage DNA polymerases, nuclear replicative DNA polymerases (alpha, delta, epsilon and zeta), and eukaryotic viral and plasmid-borne enzymes. Nuclear DNA polymerases alpha and zeta lack the four conserved acidic metal-binding residues. Family-B DNA polymerases are predominantly involved in DNA replication and DNA repair
VLSFDIETTPPVGGPEPDRDPIICITYADSFDGVKVVFLLKTSTVGDDIEFIDGIEVEYFADEKELLKRF
FDIIREYDPDILTGYNIDDFDLPYLLKRAEALGIKLTDGIYRRSGGEKSSGSTERIAVKGRVVFDLLAAY
KRDFKLKSYTLDAVAEELLGEGKEKVDGEIIEDAEWEEDPERLIEYNLKDAELTLQILE
>gnl|CDD|438958 cd05162, PWWP, PWWP (Pro-Trp-Trp-Pro) domain. The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids and is composed of a five-stranded antiparallel beta-barrel followed by a helical region. It is found in numerous proteins that are involved in cell division, growth, and differentiation. Most PWWP-domain proteins seem to be nuclear, often DNA-binding, proteins that function as transcription factors regulating a variety of developmental processes. PWWP domains specifically recognize DNA and histone methylated lysines at the level of the nucleosome. Based on the fact that other regions of PWWP-domain proteins are responsible for nuclear localization and DNA-binding, is likely that the PWWP domain acts as a site for protein-protein binding interactions, influencing chromatin remodeling and thereby regulating transcriptional processes. Some PWWP-domain proteins have been linked to cancer or other diseases; some are known to function as growth factors
GDLVWAKLKGYPWWPARVVDPEELPEEVGKKKKKGGVLVQFFGDNDYAWVKSKNIKPFEEGFKKEFKKKK
KKSKKFKKAVEEAEEA
>gnl|CDD|270707 cd05163, PIKK_TRRAP, Pseudokinase domain of TRansformation/tRanscription domain-Associated Protein. TRRAP belongs to the the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. It contains a FATC (FRAP, ATM and TRRAP, C-terminal) domain and has a large molecular weight. Unlike most PIKK proteins, however, it contains an inactive PI3K-like pseudokinase domain, which lacks the conserved residues necessary for ATP binding and catalytic activity. TRRAP also contains many motifs that may be critical for protein-protein interactions. TRRAP is a common component of many histone acetyltransferase (HAT) complexes, and is responsible for the recruitment of these complexes to chromatin during transcription, replication, and DNA repair. TRRAP also exists in non-HAT complexes such as the p400 and MRN complexes, which are implicated in ATP-dependent remodeling and DNA repair, respectively. The TRRAP pseudokinase domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
IARFLPRVEIVRRHGTCYRRLTIRGHDGSKYPFLVQTPSARHSRREERVMQLFRLLNRVLERKKETRRRN
LQFHVPIVVPLSPQVRLVEDDPSYISLQDIYEKLEILNEIQSKMVPETILSNYFLRTMPSPSDLWLFRKQ
FTLQLALSSFMTYVLSLGNRTPHRILISRSTGNVFMTDFLPSINSQGPLLDNNEPVPFRLTPNIQHFIGP
IGVEGLLTSSMMAIARALTEPEYDLEQYLSLFVRDELISWHK
>gnl|CDD|270708 cd05164, PIKKc, Catalytic domain of Phosphoinositide 3-kinase-related protein kinases. PIKK subfamily members include ATM (Ataxia telangiectasia mutated), ATR (Ataxia telangiectasia and Rad3-related), TOR (Target of rapamycin), SMG-1 (Suppressor of morphogenetic effect on genitalia-1), and DNA-PK (DNA-dependent protein kinase). PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). They show strong preference for phosphorylating serine/threonine residues followed by a glutamine and are also referred to as (S/T)-Q-directed kinases. They all contain a FATC (FRAP, ATM and TRRAP, C-terminal) domain. PIKKs have diverse functions including cell-cycle checkpoints, genome surveillance, mRNA surveillance, and translation control. The PIKK catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
IASFDPRVRILASLQKPKKITILGSDGKEYPFLVKGDDDLRKDERVMQLFQLLNTLLEKDKETRKRNLTI
RTYSVVPLSSQSGLIEWVDNTTTLKPVLKKWFNETFPDPTQWYEARSNYTKSTAVMSMVGYIIGLGDRHL
ENILIDTKTGEVVHIDFGMIFNKGKTLPVPEIVPFRLTRNIINGMGPTGVEGLFRKSCEQVLRVFRKHKD
KLITFLDTFLYD
>gnl|CDD|270709 cd05165, PI3Kc_I, Catalytic domain of Class I Phosphoinositide 3-kinase. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. In vitro, they can also phosphorylate the substrates PtdIns and PtdIns(4)P. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
LKSLSRQVEALNKLKKLSDILKEKKKSKEKVKKLLKECLKQKFYDEALQNFQSPLNPSHKLGELIIEKCK
VMDSKKRPLWLVFENADPLALSGEDIKIIFKNGDDLRQDMLTLQIIRIMDNIWKEEGLDLRMLPYGCLST
GDNVGLIEVVRNAKTIANIQKKKGKVATLAFNKDSLHKWLKEKNKTGEKYDRAIEEFTLSCAGYCVATYV
LGIGDRHSDNIMVKENGQLFHIDFGHFLGNFKKKFGIKRERVPFVLTHDFVYVIARGQDNTKSEEFQEFQ
ELCEKAYLILRRHGNLFISLFSMMLSTGIPELTSVKDIEYLRKTLALDKTEEEALKYFRKKFNEALKGSW
TTKVNWFFHNVKH
>gnl|CDD|270710 cd05166, PI3Kc_II, Catalytic domain of Class II Phosphoinositide 3-kinase. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PtdIns as a substrate to produce PtdIns(3)P, but can also phosphorylate PtdIns(4)P. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a Phox homology (PX) domain, and a second C2 domain at the C-terminus. They are activated by a variety of stimuli including chemokines, cytokines, lysophosphatidic acid (LPA), insulin, and tyrosine kinase receptors. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
REEFLKQHVLVQALTSIAEKVKSAKDSARENALRRELEQLASFLLENSFRLPLDPALEVTGVDVRSCSYF
NSNALPLKLVFRNADPRAEPISVIFKVGDDLRQDMLTLQLIRIMDKIWLQEGLDLKMITFRCVPTGNKRG
MVELVPEAETLREIQTEHGLTGSFKDRPLADWLQKHNPSELEYEKAVENFIRSCAGYCVATYVLGICDRH
NDNIMLKTSGHLFHIDFGKFLGDAQMFGNFKRDRVPFVLTSDMAYVINGGDKPSSRFQLFVDLCCQAFNI
IRKNSNLLLNLLSLMLSSGIPGVTQDDLRYVQDALLPELTDAEATAHFTRMIEESLSSKFTQLNFFIHNL
AQ
>gnl|CDD|270711 cd05167, PI4Kc_III_alpha, Catalytic domain of Type III Phosphoinositide 4-kinase alpha. PI4Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 4-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) to generate PtdIns(4)P, the major precursor in the synthesis of other phosphoinositides including PtdIns(4,5)P2, PtdIns(3,4)P2, and PtdIns(3,4,5)P3. Two isoforms of type III PI4K, alpha and beta, exist in most eukaryotes. PI4KIIIalpha is a 220 kDa protein found in the plasma membrane and the endoplasmic reticulum (ER). The role of PI4KIIIalpha in the ER remains unclear. In the plasma membrane, it provides PtdIns(4)P, which is then converted by PI5Ks to PtdIns(4,5)P2, an important signaling molecule. Vertebrate PI4KIIIalpha is also part of a signaling complex associated with P2X7 ion channels. The yeast homolog, Stt4p, is also important in regulating the conversion of phosphatidylserine to phosphatidylethanolamine at the ER and Golgi interface. Mammalian PI4KIIIalpha is highly expressed in the nervous system. The PI4K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
VVLGIDYKSGKPLQSAAKAPFLVTFKVKDCGVDELEHEGTESEATKEVWQAAIFKVGDDCRQDMLALQLI
SLFKNIFEEVGLDLYLFPYRVVATGPGCGVIEVIPNSKSRDQIGRETDNGLYEYFLSKYGDESTPAFQKA
RRNFIKSMAGYSLVSYLLQIKDRHNGNIMIDDDGHIIHIDFGFIFEISPGGNLGFESAPFKLTKEMVDLM
GGSMESEPFKWFVELCVRGYLAVRPYAEAIVSLVELMLDSGLPCFRGQTIKNLRERFALEMSEREAANFM
IKLIADSYLKIRTKGYDMFQYYQNGIP
>gnl|CDD|270712 cd05168, PI4Kc_III_beta, Catalytic domain of Type III Phosphoinositide 4-kinase beta. PI4Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 4-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) to generate PtdIns(4)P, the major precursor in the synthesis of other phosphoinositides including PtdIns(4,5)P2, PtdIns(3,4)P2, and PtdIns(3,4,5)P3. Two isoforms of type III PI4K, alpha and beta, exist in most eukaryotes. PI4KIIIbeta (also called Pik1p in yeast) is a 110 kDa protein that is localized to the Golgi and the nucleus. It is required for maintaining the structural integrity of the Golgi complex (GC), and is a key regulator of protein transport from the GC to the plasma membrane. PI4KIIIbeta also functions in the genesis, transport, and exocytosis of synaptic vesicles. The Drosophila PI4KIIIbeta is essential for cytokinesis during spermatogenesis. The PI4K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
SAAAFGESWEEKKERIRKSSPYGHLPGWDLRSVIVKSGDDLRQELLAMQLIKQFQRIFEEAGLPLWLRPY
EILVTSSDSGLIETIPDTVSIDSLKKRFPNFTSLLDYFERTFGDPNSERFKEAQRNFVESLAAYSLVCYL
LQIKDRHNGNILLDSEGHIIHIDFGFMLSNSPGGLGFETAPFKLTQEYVEVMGGLESDMFRYFKTLMIQG
FLALRKHADRIVLLVEIMQQGSKLPCFFGGGEFTIEQLRERFKLNLTEEECAQFVDSLIDKSLNNWRTRQ
YDNFQYLTNGIL
>gnl|CDD|270713 cd05169, PIKKc_TOR, Catalytic domain of Target of Rapamycin. TOR contains a rapamycin binding domain, a catalytic domain, and a FATC (FRAP, ATM and TRRAP, C-terminal) domain at the C-terminus. It is also called FRAP (FK506 binding protein 12-rapamycin associated protein). TOR is a central component of the eukaryotic growth regulatory network. It controls the expression of many genes transcribed by all three RNA polymerases. It associates with other proteins to form two distinct complexes, TORC1 and TORC2. TORC1 is involved in diverse growth-related functions including protein synthesis, nutrient use and transport, autophagy and stress responses. TORC2 is involved in organizing cytoskeletal structures. TOR is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The TOR catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
ISSFDPTLEVITSKQRPRKLTIVGSDGKEYKFLLKGHEDLRLDERVMQLFGLVNTLLKNDSETSRRNLSI
QRYSVIPLSPNSGLIGWVPGCDTLHSLIRDYREKRKIPLNIEHRLMLQMAPDYDNLTLIQKVEVFEYALE
NTPGDDLRRVLWLKSPSSEAWLERRTNFTRSLAVMSMVGYILGLGDRHPSNIMLDRLTGKVIHIDFGDCF
EVAMHREKFPEKVPFRLTRMLVNAMEVSGVEGTFRSTCEDVMRVLRENKDSLMAVLEAFVHDPLISWRL
>gnl|CDD|270714 cd05170, PIKKc_SMG1, Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1. SMG-1 plays a critical role in the mRNA surveillance mechanism known as non-sense mediated mRNA decay (NMD). NMD protects the cells from the accumulation of aberrant mRNAs with premature termination codons (PTCs) generated by genome mutations and by errors during transcription and splicing. SMG-1 phosphorylates Upf1, another central component of NMD, at the C-terminus upon recognition of PTCs. The phosphorylation/dephosphorylation cycle of Upf1 is essential for promoting NMD. In addition to its catalytic domain, SMG-1 contains a FATC (FRAP, ATM and TRRAP, C-terminal) domain at the C-terminus. SMG-1 is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The SMG-1 catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
IQSVGSTVTVLPTKTKPKKLVFLGSDGKRYPYLFKGLEDLHLDERIMQFLSIVNAMLASDNEHRRRRYRA
RHYSVTPLGPRSGLIQWVDGATPLFSLYKRWQQRRAAAQAQKNQDSGSTPPPVPRPSELFYNKLKPALKA
AGIRKSTSRREWPLEVLRQVLEELVAETPRDLLARELWCSSPSSAEWWRVTQRFARSLAVMSMIGYIIGL
GDRHLDNILVDLSTGEVVHIDYNVCFEKGKRLRVPEKVPFRLTQNIEHALGPTGVEGTFRLSCEQVLKIL
RKGRETLLTLLEAFVYDPLVDWTA
>gnl|CDD|270715 cd05171, PIKKc_ATM, Catalytic domain of Ataxia Telangiectasia Mutated. ATM is critical in the response to DNA double strand breaks (DSBs) caused by radiation. It is activated at the site of a DSB and phosphorylates key substrates that trigger pathways that regulate DNA repair and cell cycle checkpoints at the G1/S, S phase, and G2/M transition. Patients with the human genetic disorder Ataxia telangiectasia (A-T), caused by truncating mutations in ATM, show genome instability, increased cancer risk, immunodeficiency, compromised mobility, and neurodegeneration. A-T displays clinical heterogeneity, which is correlated to the degree of retained ATM activity. ATM contains a FAT (FRAP, ATM and TRRAP) domain, a catalytic domain, and a FATC domain at the C-terminus. It is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The ATM catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
ISRFEDTFTLAGGINLPKIITCIGSDGKKYKQLVKGGDDLRQDAVMEQVFELVNQLLKRDKETRKRKLRI
RTYKVVPLSPRSGVLEFVENTIPLGEYLVGASSKSGAHARYRPKDWTASTCRKKMREKAKASAEERLKVF
DEICKNFKPVFRHFFLEKFPDPSDWFERRLAYTRSVATSSIVGYILGLGDRHLNNILIDQKTGELVHIDL
GIAFEQGKLLPIPETVPFRLTRDIVDGMGITGVEGVFRRCCEETLRVLRENKEALLTILEVLLYDPLYSW
TV
>gnl|CDD|270716 cd05172, PIKKc_DNA-PK, Catalytic domain of DNA-dependent protein kinase. DNA-PK is comprised of a regulatory subunit, containing the Ku70/80 subunit, and a catalytic subunit, which contains a NUC194 domain of unknown function, a FAT (FRAP, ATM and TRRAP) domain, a catalytic domain, and a FATC domain at the C-terminus. It is part of a multi-component system involved in non-homologous end joining (NHEJ), a process of repairing double strand breaks (DSBs) by joining together two free DNA ends of little homology. DNA-PK functions as a molecular sensor for DNA damage that enhances the signal via phosphorylation of downstream targets. It may also act as a protein scaffold that aids the localization of DNA repair proteins to the site of DNA damage. DNA-PK also plays a role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. DNA-PK is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The DNA-PK catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
IVGFDPRVLVLSSKRRPKRITIRGSDEKEYKFLVKGGEDLRQDQRIQQLFDVMNNILASDPACRQRRLRI
RTYQVIPMTSRLGLIEWVDNTTPLKEILENDLLRRALLSLASSPEAFLALRSNFARSLAAMSICGYILGI
GDRHLSNFLVDLSTGRLIGIDFGHAFGSATQFLPIPELVPFRLTRQLLNLLQPLDARGLLRSDMVHVLRA
LRAGRDLLLATMDVFVKEPLLDWQK
>gnl|CDD|270717 cd05173, PI3Kc_IA_beta, Catalytic domain of Class IA Phosphoinositide 3-kinase beta. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kbeta can be activated by G-protein-coupled receptors. Deletion of PI3Kbeta in mice results in early lethality at around day three of development. PI3Kbeta plays an important role in regulating sustained integrin activation and stable platelet agrregation, especially under conditions of high shear stress. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They associate with a regulatory subunit of the p85 family and are activated by tyrosine kinase receptors. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
MKVLSKQVEALNKLKTLNSLIKLNAVKLSKAKGKEAMHTCLRQSAYREALSDLQSPLNPSIILSELNVEK
CKYMDSKMKPLWIVYNNKLFGGDSLGIIFKNGDDLRQDMLTLQILRLMDTLWKEAGLDLRIVPYGCLATG
DRSGLIEVVSSAETIADIQLNSSNVAAAAAFNKDALLNWLKEYNSGDDLERAIEEFTLSCAGYCVATYVL
GIGDRHSDNIMVRKNGQLFHIDFGHILGNFKSKFGIKRERVPFILTYDFIHVIQQGKTGNTEKFGRFRQY
CEDAYLILRKNGNLFITLFALMLTAGLPELTSVKDIQYLKDSLALGKSEEEALKQFRQKFDEALRESWTT
KVNWMAHTVRKD
>gnl|CDD|270718 cd05174, PI3Kc_IA_delta, Catalytic domain of Class IA Phosphoinositide 3-kinase delta. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kdelta is mainly expressed in immune cells and plays an important role in cellular and humoral immunity. It plays a major role in antigen receptor signaling in B-cells, T-cells, and mast cells. It regulates the differentiation of peripheral helper T-cells and controls the development and function of regulatory T-cells. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They associate with a regulatory subunit of the p85 family and are activated by tyrosine kinase receptors. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
THHMKVLMKQGEALSKMKALNDFVKVSSQKATKPQTKEMMHVCMKQETYMEALSHLQSPLDPSIILEEVC
VDQCTFMDSKMKPLWIMYSSEEAGAGNVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCL
STGDKTGLIEVVLHSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGDALDQAIEEFTLSCAGYCVAT
YVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERF
RGYCERAYTILRRHGLLFLHLFALMKAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRES
WKTKVNWLAHNVSKDN
>gnl|CDD|270719 cd05175, PI3Kc_IA_alpha, Catalytic domain of Class IA Phosphoinositide 3-kinase alpha. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kalpha plays an important role in insulin signaling. It also mediates physiologic heart growth and provides protection from stress. Activating mutations of PI3Kalpha is associated with diverse forms of cancer at high frequency. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They associate with a regulatory subunit of the p85 family and are activated by tyrosine kinase receptors. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
CGMYLKHLSRQVEAMEKLINLTDILKQEKKDETQKVQMKFLVEQMRRPDFMDALQGFLSPLNPAHQLGNL
RLEECRIMSSAKRPLWLNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRML
PYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRSCAGY
CVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDFLIVISKGAQECTKT
REFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIAYIRKTLALDKTEQEALEYFMKQMN
DAHHGGWTTKMDWIFHTIKQ
>gnl|CDD|270720 cd05176, PI3Kc_C2_alpha, Catalytic domain of Class II Phosphoinositide 3-kinase alpha. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. The class II alpha isoform, PI3K-C2alpha, plays key roles in clathrin assembly and clathrin-mediated membrane trafficking, insulin signaling, vascular smooth muscle contraction, and the priming of neurosecretory granule exocytosis. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PtdIns as a substrate to produce PtdIns(3)P, but can also phosphorylate PtdIns(4)P. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a Phox homology (PX) domain, and a second C2 domain at the C-terminus. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
REELEKQTRLVQLLGRVAEKVRQASGSARQVALQDGMERVQSFFQKNKCRLPLSPSLVAKELNIKACSFF
SSNAVPLKVALVNADPLGEEINVMFKVGEDLRQDMLALQMIKIMDKIWLQEGLDLRMVIFKCLSTGKDRG
MVELVPSSDTLRKIQVEYGVTGSFKDKPLAEWLRKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRH
NDNIMLRSTGHMFHIDFGKFLGHAQMFGSFKRDRAPFVLTSDMAYVINGGEKPTIRFQLFVDLCCQAYNL
IRKHTNLFLNLLSLMLSSGLPELTGIQDLKYVFDALQPQTTDAEATIFFTRLIESSLGSVATKFNFFIHN
LAQ
>gnl|CDD|270721 cd05177, PI3Kc_C2_gamma, Catalytic domain of Class II Phosphoinositide 3-kinase gamma. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. The class II gamma isoform, PI3K-C2gamma, is expressed in the liver, breast, and prostate. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PtdIns as a substrate to produce PtdIns(3)P, but can also phosphorylate PtdIns(4)P. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a Phox homology (PX) domain, and a second C2 domain at the C-terminus. It's biological function remains unknown. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases
NKEFSKETKLISILIDAAEKVKTASDTRRKEVLKREASRLEDFFQDVVSCCLPLNPALRVKGIDADACSY
FTSNAAPLKISFINANPLAKNISIIFKTGDDLRQDMLVLQIVRVMDNIWLQEGLDMQMIIYRCLSTGKTQ
GLVQMVPDAVTLAKIHRESGLIGPLKENTIEKWFHMHNKLKEDYDKAVRNFFHSCAGWCVVTFILGVCDR
HNDNIMLTHSGHMFHIDFGKFLGHAQTFGSIKRDRAPFIFTSEMEYFITEGGKKPQRFQRFVELCCRAYN
IVRKHSQLLLNLLEMMLHAGLPELKDIQDLKYVYNNLRPQDTDLEATSYFTKKIKESLECFPVKLNNLIH
TLAQ
>gnl|CDD|176178 cd05188, MDR, Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family. The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc
EVLVRVEAAGLCGTDLHIRRGGYPPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGCGTCEL
CRELCPGGGILGEGLDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPGDTVLV
LGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLTGGGGADVVIDAVG
GPETLAQALRLLRPGGRIVVVGGTSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALDLL
>gnl|CDD|133449 cd05191, NAD_bind_amino_acid_DH, NAD(P) binding domain of amino acid dehydrogenase-like proteins. Amino acid dehydrogenase(DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and are found in glutamate, leucine, and phenylalanine DHs (DHs), methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts
ATAAGAVALLKAAGKVTNKSLKGKTVVVLGAGEVGKGIAKLLADEGGKKVVLCDRDILVTATPAGVPVLE
EATAKINEGAVVIDLA
>gnl|CDD|467613 cd05192, GAPDH-like_N, N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like family. The GAPDH-like family includes glyceraldehyde-3-phosphate dehydrogenase (GAPDH), native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs), 2,4-diaminopentanoate dehydrogenase (DAPDH), meso-diaminopimelate D-dehydrogenase (meso-DAPDH), and dihydrodipicolinate reductase (DHDPR). GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. nat-AmDHs catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. They play important roles in the efficient asymmetric synthesis of alpha-chiral amines. DAPDH is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). DHDPR catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). It could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. The model corresponds to the N-terminal NAD(P)-binding domain of GAPDH-like family proteins. It contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft
IRVAINGFGRIGRIVFRAIADQDDLDVVAINDRRDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGD
IPTIVVVLNELAKSAGATVVSNANETSYSPQVVDLVRAI
>gnl|CDD|187536 cd05193, AR_like_SDR_e, aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs. This subgroup contains aldehyde reductase and flavonoid reductase of the extended SDR-type and related proteins. Proteins in this subgroup have a complete SDR-type active site tetrad and a close match to the canonical extended SDR NADP-binding motif. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
VLVTGASGFVASHVVEQLLERGYKVRATVRDPSKVKKVNHLLDLDAKPGRLELAVADLTDEQSFDEVIKG
CAGVFHVATPVSFSSKDPNEVIKPAIGGTLNALKAAAAAKSVKRFVLTSSAGSVLIPKPNVEGIVLDEKS
WNLEEFDSDPKKSAWVYAASKTLAEKAAWKFADENNIDLITVIPTLTIGTIFDSETPSSSGWAMSLITGN
EGVSPALALIPPGYYVHVVDICLAHIGCLELPIARGRYICTAGNFDWNTLLKTLRKKYPSYTFPTDFPDQ
GQDLSKFSSAKLLEI
>gnl|CDD|176179 cd05195, enoyl_red, enoyl reductase of polyketide synthase. Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding
DEVEVEVKAAGLNFRDVLVALGLLPGDETPLGLECSGIVTRVGSGVTGLKVGDRVMGLAPGAFATHVRVD
ARLVVKIPDSLSFEEAATLPVAYLTAYYALVDLARLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATV
GSEEKREFLRELGGPVDHIFSSRDLSFADGILRATGGRGVDVVLNSLSGELLRASWRCLAPFGRFVEIGK
RDILSNSKLGMRPFLRNVSFSSVDLDQLARERPELLRELLREVLELLEAGVLKPLPPTVVPSASEIDAFR
LMQSGKHIGKVVL
>gnl|CDD|133425 cd05197, GH4_glycoside_hydrolases, Glycoside Hydrases Family 4. Glycoside hydrolases cleave glycosidic bonds to release smaller sugars from oligo- or polysaccharides. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by GH4 glycoside hydrolases. Other organisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. GH4 family members include 6-phospho-beta-glucosidases, 6-phospho-alpha-glucosidases, alpha-glucosidases/alpha-glucuronidases (only from Thermotoga), and alpha-galactosidases. They require two cofactors, NAD+ and a divalent metal (Mn2+, Ni2+, Mg2+), for activity. Some also require reducing conditions. GH4 glycoside hydrolases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
VKIAIIGGGSSFTPELVSGLLKTPEELPISEVTLYDIDEERLDIILTIAKRYVEEVGADIKFEKTMDLED
AIIDADFVINQFRVGGLTYREKDEQIPLKYGVIGQETVGPGGTFSGLRQIPYVLDIARKXEKLSPDAWYL
NFTNPAGEVTEAVRRYVPPEKAVGLCNVPIGVMEIVAKLLGESEEKVDWQYAGLNHGIWLNRVRYNGGDV
TPKLDEWVEEKSKDWKTENPFVDQLSPAAIDFYRFYGVLPNPYLRYYLSWDKXRKLEADKEITWKTRADE
VGKVEKELFEVYKFIKENPSVVELIKRGGRKYSEAAIPLIRALLNDNGARFVVNTRNNGAIANIDDDVVV
EVPCLVDKNGPHPIKVGPLDRFVKGLLRQRKMRERLALEAFLTGDIQIALEALYRDPLVPSDEQAKKILE
EILEA
>gnl|CDD|240622 cd05198, formate_dh_like, Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family. Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
KVLVLEPLFPPEALEALEATGFEVIVADDLLADELEALLADADALIVSSTTPVTAEVLAKAPKLKFIQVA
GAGVDNIDLDAAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWGWLWAGFPGYELEG
KTVGIVGLGRIGQRVAKRLQAFGMKVLYYDRTRKPEPEEDLGFRVVSLDELLAQSDVVVLHLPLTPETRH
LINEEELALMKPGAVLVNTARGGLVDEDALLRALKSGKIAGAALDVFEPEPLPADHPLLELPNVILTPHI
AGYTEEARERMAEIAVENLERF
>gnl|CDD|240623 cd05199, SDH_like, Saccharopine Dehydrogenase like proteins. Saccharopine Dehydrogenase (SDH) and related proteins, including bifunctional lysine ketoglutarate reductase/SDH enzymes and N(5)-(carboxyethyl)ornithine synthases. SDH catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SDH is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of related structure. Bifunctional lysine ketoglutarate reductase/SDH protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases
KIGIIREGKTPPDRRVPLTPEQCKELQAKYPGVEIFVQPSPVRCFKDEEYRAAGIEVVEDLSDCDILLGV
KEVPIEQLIPNKTYFFFSHTIKKQPYNRKLLQTILEKNITLIDYEVLVDEQGKRVIAFGRYAGIVGAYNG
LRAYGKKTGLFDLKRAHECSDLEELIAELKKVGLPPPKIVITGSGRVGSGAAEVLKALGIKEVSPEDFLT
VADILINGHYWDKRAPRLFTKEDLKKPDFKIRVIADVTCDIHGSIPSTLRASTIADPVYDYDPTTNKEVA
FSSPDSITVMAVDNLPCELPRDASEDFGEQLIKSVLPEL
>gnl|CDD|133450 cd05211, NAD_bind_Glu_Leu_Phe_Val, NAD(P) binding domain of glutamate dehydrogenase, leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase. Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NAD(P)+. This subfamily includes glutamate, leucine, phenylalanine, and valine DHs. Glutamate DH is a multi-domain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia assimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. As in other NAD+-dependent DHs, monomers in this family have 2 domains separated by a deep cleft. Here the c-terminal domain contains a modified NAD-binding Rossmann fold with 7 rather than the usual 6 beta strands and one strand anti-parrallel to the others. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts
ATGYGVVVAMKAAMKHLGDSLEGLTVAVQGLGNVGWGLAKKLAEEGGKVLAVSDPDGYIYDPGITTEELI
NYAVALGGSARVKVQDYFPGEAILGLDVDIFAPCALGNVIDLENAKKLKAKVVAEGANNPTTDEALRILH
ERGIVVAPDIVANAGGVIVSYFEWVQNLQRLSWDAEEVRSKLEQVMTDIHNGVFAISERDGVTMRAAANI
LAFERIA
>gnl|CDD|133451 cd05212, NAD_bind_m-THF_DH_Cyclohyd_like, NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and methylene-tetrahydrofolate dehydrogenase/cyclohydrolase. NAD(P) binding domains of methylene-tetrahydrofolate dehydrogenase (m-THF DH) and m-THF DH/cyclohydrolase bifunctional enzymes (m-THF DH/cyclohydrolase). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, mono-functional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express a monofunctional DH. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts
GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVH
DADVVVVGSPKPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR
>gnl|CDD|133452 cd05213, NAD_bind_Glutamyl_tRNA_reduct, NADP-binding domain of glutamyl-tRNA reductase. Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts
ILVIGLSHKTAPVELREKLAFSEEELKEALRRLLEKPGISEAVLLSTCNRVELYLVGDNFHKLADELEEL
LAELLNEPELREYLYVGRGQDAVRHLFRVASGLDSMVVGETQILGQVKNAYKLAKEAGTSGKLLNRLFQK
AIKVGKRVRTETGISRGAVSISSAAVELAEKIFGNLKGKKVLVIGAGEMGELAAKHLAAKGVAEITIANR
TYERAEELAKELGGNAVPLDELLELLNEADVVISATGAPHYAKIVERAMKKRSGKPRLIVDLAVPRDIEP
EVGELEGVRLYTIDDLEEVVEENLERREKEA
>gnl|CDD|467614 cd05214, GAPDH_I_N, N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins. GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (EC 1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose
IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKI
KVFAERDPAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDDDPTIVMGVNHDKYDAD
DKIISNASNEWGYSNRVVDLAEYV
>gnl|CDD|187537 cd05226, SDR_e_a, Extended (e) and atypical (a) SDRs. Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
ILILGATGFIGRALARELLEQGHEVTLLVRNTKRLSKEDQEPVAVVEGDLRDLDSLSDAVQGVDVVIHLA
GAPRDTRDFCEVDVEGTRNVLEAAKEAGVKHFIFISSLGAYGDLHEETEPSPSSPYLAVKAKTEAVLREA
SLPYTIVRPGVIYGDLARAIANAVVTPGKKNETFNA
>gnl|CDD|187538 cd05227, AR_SDR_e, aldehyde reductase, extended (e) SDRs. This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
LVLVTGATGFIASHIVEQLLKAGYKVRGTVRSLSKSAKLKALLKAAGYNDRLEFVIVDDLTAPNAWDEAL
KGVDYVIHVASPFPFTGPDAEDDVIDPAVEGTLNVLEAAKAAGSVKRVVLTSSVAAVGDPTAEDPGKVFT
EEDWNDLTISKSNGLDAYIASKTLAEKAAWEFVKENKPKFELITINPGYVLGPSLLADELNSSNELINKL
LDGKLPAIPPNLPFGYVDVRDVADAHVRALESPEAAGQRFIVSAGPFSFQEIADLLREEFPQLTAPFPAP
NPLMLSILVKFDNRKSEELLG
>gnl|CDD|187539 cd05228, AR_FR_like_1_SDR_e, uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs. This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
ILVTGATGFLGSNLVRALLAQGYRVRALVRSGSDAVLLDGLPVEVVEGDLTDAASLAAAMKGCDRVFHLA
AFTSLWAKDRKELYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALGGPPDGRIDETTPWNERPFPNDYYR
SKLLAELEVLEAAAEGLDVVIVNPSAVFGPGDEGPTSTGLDVLDYLNGKLPAYPPGGTSFVDVRDVAEGH
IAAMEKGRRGERYILGGENLSFKQLFETLAEITGVKPPRRTIPPWLLKAVAALSELKARLTGKPPLLTPR
TARVLRRNYLYSSDKARRELGYSPRPLEEALRDTLAWL
>gnl|CDD|187540 cd05229, SDR_a3, atypical (a) SDRs, subgroup 3. These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
TAHVLGASGPIGREVARELRRRGWDVRLVSRSGSKLAWLPGVEIVAADAMDASSVIAAARGADVIYHCAN
PAYTRWEELFPPLMENVVAAAEANGAKLVLPGNVYMYGPQAGSPITEDTPFQPTTRKGRIRAEMEERLLA
AHAKGDIRALIVRAPDFYGPGAINSWLGAALFAILQGKTAVFPGNLDTPHEWTYLPDVARALVTLAEEPD
AFGEAWHLPGAGAITTRELIAIAARAAGRPPKVRVIPKWTLRLAGLFDPLMREIVEMMYLWEEPFILDSS
KLEATFGEIPHTPLDEAIRQTL
>gnl|CDD|187541 cd05230, UGD_SDR_e, UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs. UGD catalyzes the formation of UDP-xylose from UDP-glucuronate; it is an extended-SDR, and has the characteristic glycine-rich NAD-binding pattern, TGXXGXXG, and active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
KRILITGGAGFLGSHLCDRLLEDGHEVICVDNFFTGRKRNIEHLIGHPNFEFIRHDVTEPLYLEVDQIYH
LACPASPVHYQYNPIKTLKTNVLGTLNMLGLAKRVGARVLLASTSEVYGDPEVHPQPESYWGNVNPIGPR
SCYDEGKRVAETLCMAYHRQHGVDVRIARIFNTYGPRMHPNDGRVVSNFIVQALRGEPITVYGDGTQTRS
FQYVSDLVEGLIRLMNSDYFGGPVNLGNPEEFTILELAELVKKLTGSKSEIVFLPLPEDDPKRRRPDISK
AKELLGWEPKVPLEEGLRRTIEYFR
>gnl|CDD|187542 cd05231, NmrA_TMR_like_1_SDR_a, NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs. Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
ILVTGATGRIGSKVATTLLEAGRPVRALVRSDERAAALAARGAEVVVGDLDDPAVLAAALAGVDAVFFLA
PPAPTADARPGYVQAAEAFASALREAGVKRVVNLSSVGADPESPSGLIRGHWLMEQVLNWAGLPVVHLRP
AWFMENLLSQAPSIRKAGVLALPFPGDGRLPPIATDDIARVAAKLLLDPEWHGHRVYELTGPEDLTMNEI
AAALSRVLGRPVRYVPVPEEQWEATLLSLGFSPEMAQHLSEMARAFNEG
>gnl|CDD|187543 cd05232, UDP_G4E_4_SDR_e, UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
KVLVTGANGFIGRALVDKLLSRGEEVRIAVRNAENAEPSVVLAELPDIDSFTDLFLGVDAVVHLAARVHV
MNDQGADPLSDYRKVNTELTRRLARAAARQGVKRFVFLSSVKVNGEGTVGAPFDETDPPAPQDAYGRSKL
EAERALLELGASDGMEVVILRPPMVYGPGVRGNFARLMRLIDRGLPLPPGAVKNRRSLVSLDNLVDAIYL
CISLPKAANGTFLVSDGPPVSTAELVDEIRRALGKPTRLLPVPAGLLRFAAKLLGKRAVIQRLFGSLQYD
PEKTQNELGWRPPISLEEGLQET
>gnl|CDD|212491 cd05233, SDR_c, classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALGGNAVAVQADVSDEEDVEALVEEALE
EFGRLDILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPL
PGQAAYAASKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIPLGRLGTPEE
VAEAVVFLASDEASYITGQVIPVD
>gnl|CDD|187545 cd05234, UDP_G4E_2_SDR_e, UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of archaeal and bacterial proteins, and has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
RILVTGGAGFIGSHLVDRLLEEGNEVVVVDNLSSGRRENIEPEFENKAFRFVKRDLLDTADKVAKKDGDT
VFHLAANPDVRLGATDPDIDLEENVLATYNVLEAMRANGVKRIVFASSSTVYGEAKVIPTPEDYPPLPIS
VYGASKLAAEALISAYAHLFGFQAWIFRFANIVGPRSTHGVIYDFINKLKRNPNELEVLGDGRQRKSYLY
VSDCVDAMLLAWEKSTEGVNIFNLGNDDTISVNEIAEIVIEELGLKPRFKYSGGDRGWKGDVPYMRLDIE
KLKALGWKPRYNSEEAVRKTVRELL
>gnl|CDD|187546 cd05235, SDR_e1, extended (e) SDRs, subgroup 1. This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
TVLLTGATGFLGAYLLRELLKRKNVSKIYCLVRAKDEEAALERLIDNLKEYGLNLWDELELSRIKVVVGD
LSKPNLGLSDDDYQELAEEVDVIIHNGANVNWVYPYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSV
FSAEEYNALDDEESDDMLESQNGLPNGYIQSKWVAEKLLREAANRGLPVAIIRPGNIFGDSETGIGNTDD
FFWRLLKGCLQLGIYPISGAPLDLSPVDWVARAIVKLALNESNEFSIYHLLNPPLISLNDLLDALEEKGY
SIKEVSYEEW
>gnl|CDD|187547 cd05236, FAR-N_SDR_e, fatty acyl CoA reductases (FARs), extended (e) SDRs. SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
KSVLITGATGFLGKVLLEKLLRSCPDIGKIYLLIRGKSGQSAEERLRELLKDKLFDRGRNLNPLFESKIV
PIEGDLSEPNLGLSDEDLQTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKLKAFVH
VSTAYVNGDRQLIEEKVYPPPADPEKLIDILELMDDLELERATPKLLGGHPNTYTFTKALAERLVLKERG
NLPLVIVRPSIVGATLKEPFPGWIDNFNGPDGLFLAYGKGILRTMNADPNAVADIIPVDVVANALLAAAA
YSGVRKPRELEVYHCGSSDVNPFTWGEAEELINQYLKKNP
>gnl|CDD|187548 cd05237, UDP_invert_4-6DH_SDR_e, UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs. UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
KGKTILVTGGAGSIGSELVRQILKFGPKKLIVFDRDENKLHELVRELRSRFPHDKLRFIIGDVRDKERLR
RAFKERGPDIVFHAAALKHVPSMEDNPEEAIKTNVLGTKNVIDAAIENGVEKFVCISTDKAVNPVNVMGA
TKRVAEKLLLAKNEYSSSTKFSTVRFGNVLGSRGSVLPLFKKQIKKGGPLTVTDPDMTRFFMTIPEAVDL
VLQACILGDGGGIFLLDMGPPVKILDLAEALIELLGYEPYEDIPIFFTGLRPGEKLYEELVTEEETLDTE
HFKILGA
>gnl|CDD|187549 cd05238, Gne_like_SDR_e, Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs. Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
MKVLITGASGFVGQRLAERLLSDVPNERLILIDVVSPKAPSGAPRVTQIAGDLAVPALIEALANGRPDVV
FHLAAIVSGGAEADFDLGYRVNVDGTRNLLEALRKNGPKPRFVFTSSLAVYGLPLPNPVTDHTALDPASS
YGAQKAMCELLLNDYSRRGFVDGRTLRLPTVCVRPGRPNKAASAFASTIIREPLVGEEAGLPVAEQLRYW
LKSVATAVANFVHAAELPAEKFGPRRDLTLPGLSVTVGEELRALIPVAGLPALMLITFEPDEEIKRIVFG
WPTRFDATRAQSLGFVADSSLAAGL
>gnl|CDD|187550 cd05239, GDP_FS_SDR_e, GDP-fucose synthetase, extended (e) SDRs. GDP-fucose synthetase (aka 3, 5-epimerase-4-reductase) acts in the NADP-dependent synthesis of GDP-fucose from GDP-mannose. Two activities have been proposed for the same active site: epimerization and reduction. Proteins in this subgroup are extended SDRs, which have a characteristic active site tetrad and an NADP-binding motif [AT]GXXGXXG, that is a close match to the archetypical form. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
KILVTGHRGLVGSAIVRVLARRGYENVVFRTSKELDLTDQEAVRAFFEKEKPDYVIHLAAKVGGIVANMT
YPADFLRDNLLINDNVIHAAHRFGVKKLVFLGSSCIYPDLAPQPIDESDLLTGPPEPTNEGYAIAKRAGL
KLCEAYRKQYGCDYISVMPTNLYGPHDNFDPENSHVIPALIRKFHEAKLRGGKEVTVWGSGTPRREFLYS
DDLARAIVFLLENYDEPIIVNVGSGVEISIRELAEAIAEVVGFKGEIVFDTSKPDGQPRKLLDVSKLRAL
GWFPFTPLEQGIRETYEWYL
>gnl|CDD|187551 cd05240, UDP_G4E_3_SDR_e, UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs. Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
ILVTGAAGGLGRLLARRLAASPRVIGVDGLDRRRPPGSPPKVEYVRLDIRDPAAADVFREREADAVVHLA
FILDPPRDGAERHRINVDGTQNVLDACAAAGVPRVVVTSSVAVYGAHPDNPAPLTEDAPLRGSPEFAYSR
DKAEVEQLLAEFRRRHPELNVTVLRPATILGPGTRNTTRDFLSPRRLPVPGGFDPPFQFLHEDDVARALV
LAVRAGATGIFNVAGDGPVPLSLVLALLGRRPVPLPSPLPAALAAARRLGLRPLPPEQLDFLQYPPVMDT
TRARVELGWQPKHTSAEVLRDFRRAV
>gnl|CDD|187552 cd05241, 3b-HSD-like_SDR_e, 3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs. Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
SVLVTGGSGFFGERLVKQLLERGGTYVRSFDIAPPGEALSAWQHPNIEFLKGDITDRNDVEQALSGADCV
FHTAAIVPLAGPRDLYWEVNVGGTQNVLDACQRCGVQKFVYTSSSSVIFGGQNIHNGDETLPYPPLDSDM
YAETKAIAEIIVLEANGRDDLLTCALRPAGIFGPGDQGLVPILFEWAEKGLVKFVFGRGNNLVDFTYVHN
LAHAHILAAAALVKGKTISGQTYFITDAEPHNMFELLRPVWKALGFGSRPKIRLSGPLAYCAALLSELVS
FMLGPYFVFSPFYVRALVTPMYFSIAKAQKDLGYAPRYSNEEGLIETLNWY
>gnl|CDD|187553 cd05242, SDR_a8, atypical (a) SDRs, subgroup 8. This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
KIVITGGTGFIGRALTRRLTAAGHEVVVLSRRPGKAEGLAEVITWDGLSLGPWELPGADAVINLAGEPIA
CRRWTEANKKEILSSRIESTRVLVEAIANAPAPPKVLISASAVGYYGHSGDEVLTENSPSGKDFLAEVCK
AWEKAAQPASELGTRVVILRTGVVLGPDGGALPKMLLPFRLGLGGPLGSGRQWMSWIHIDDLVRLIEFAI
ENPDLSGPVNAVAPNPVTNAEFTKALGRALHRPAGLPVPAFALKLGFGEMRAELLLKGQRVLPERLLDAG
FQFRYPDLEEALEELL
>gnl|CDD|187554 cd05243, SDR_a5, atypical (a) SDRs, subgroup 5. This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
KVLVVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEKLEAAGAEVVVGDLTDAESLAAALEGIDAVISA
AGSGGKGGPRTEAVDYDGNINLIDAAKKAGVKRFVLVSSIGADKPSHPLEALGPYLDAKRKAEDYLRASG
LDYTIVRPGGLTDDPAGTGRVVLGGDGTRLDGPISRADVAEVLAEALDTPAAIGKTFELGGGD
>gnl|CDD|187555 cd05244, BVR-B_like_SDR_a, biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs. Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
KIAIIGATGRTGSAIVREALARGHEVTALVRDPAKLPAEHEKLKVVQGDVLDLEDVKEALEGQDAVISAL
GTRNDLSPTTLHSEGTRNIVSAMKAAGVKRLIVVGGAGSLDDRPKVTLVLDTLLFPPALRRVAEDHARML
KVLRESGLDWTAVRPPALFDGGATGGYYRVELLVDAKGGSRISRADLAIFMLDELETPEHVRKRPTI
>gnl|CDD|187556 cd05245, SDR_a2, atypical (a) SDRs, subgroup 2. This subgroup contains atypical SDRs, one member is identified as Escherichia coli protein ybjT, function unknown. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that generally matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
VLVTGATGYVGGRLVPRLLQEGHQVRALVRSPEKLADRPWSERVTVVRGDLEDPESLRAALEGIDTAYYL
VHSMGSGGDFEEADRRAARNFARAARAAGVKRIIYLGGLIPKGEELSPHLRSRAEVGEILRAGGVPVTEL
RAAVIIGSGSASFEMVRYLVERLPVMITPRWVNTPCQPIAIRDVLEYLVAALDRPATAGETFEIGGPDVL
SYKDMMERFAEVRGLRRWILPVPVLTPRLSSLWVGLVTPVPNSIARPLIEGLKHDVVVDDDRARDLFPVR
LIPFPDAVERALR
>gnl|CDD|187557 cd05246, dTDP_GD_SDR_e, dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs. This subgroup contains dTDP-D-glucose 4,6-dehydratase and related proteins, members of the extended-SDR family, with the characteristic Rossmann fold core region, active site tetrad and NAD(P)-binding motif. dTDP-D-glucose 4,6-dehydratase is closely related to other sugar epimerases of the SDR family. dTDP-D-dlucose 4,6,-dehydratase catalyzes the second of four steps in the dTDP-L-rhamnose pathway (the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose) in the synthesis of L-rhamnose, a cell wall component of some pathogenic bacteria. In many gram negative bacteria, L-rhamnose is an important constituent of lipopoylsaccharide O-antigen. The larger N-terminal portion of dTDP-D-Glucose 4,6-dehydratase forms a Rossmann fold NAD-binding domain, while the C-terminus binds the sugar substrate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
MKILVTGGAGFIGSNFVRYLLNKYPDYKIINLDKLTYAGNLENLEDVSSSPRYRFVKGDICDAELVDRLF
EEEKIDAVIHFAAESHVDRSISDPEPFIRTNVLGTYTLLEAARKYGVKRFVHISTDEVYGDLLDDGEFTE
TSPLAPTSPYSASKAAADLLVRAYHRTYGLPVVITRCSNNYGPYQFPEKLIPLFILNALDGKPLPIYGDG
LNVRDWLYVEDHARAIELVLEKGRVGEIYNIGGGNELTNLELVKLILELLGKDESLITYVKDRPGHDRRY
AIDSSKIRRELGWRPKVSFEEGLRKTVRWYLENRW
>gnl|CDD|187558 cd05247, UDP_G4E_1_SDR_e, UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
KVLVTGGAGYIGSHTVVELLEAGYDVVVLDNLSNGHREALPRIEKIRIEFYEGDIRDRAALDKVFAEHKI
DAVIHFAALKAVGESVQKPLKYYDNNVVGTLNLLEAMRAHGVKNFVFSSSAAVYGEPETVPITEEAPLNP
TNPYGRTKLMVEQILRDLAKAPGLNYVILRYFNPAGAHPSGLIGEDPQIPNNLIPYVLQVALGRREKLAI
FGDDYPTPDGTCVRDYIHVVDLADAHVLALEKLENGGGSEIYNLGTGRGYSVLEVVEAFEKVSGKPIPYE
IAPRRAGDPASLVADPSKAREELGWKPKRDLEDMCEDAWNWQS
>gnl|CDD|187559 cd05248, ADP_GME_SDR_e, ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs. This subgroup contains ADP-L-glycero-D-mannoheptose 6-epimerase, an extended SDR, which catalyzes the NAD-dependent interconversion of ADP-D-glycero-D-mannoheptose and ADP-L-glycero-D-mannoheptose. This subgroup has the canonical active site tetrad and NAD(P)-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
MIIVTGGAGFIGSNLVKALNERGITDILVVDNLSNGEKFKNLVGLKIADYIDKDDFKDWVRKGDENFKIE
AIFHQGACSDTTETDGKYMMDNNYQYTKELLHYCLEKKIRFIYASSAAVYGNGSLGFAEDIETPNLRPLN
VYGYSKLLFDQWARRHGKEVLSQVVGLRYFNVYGPREYHKGRMASVVFHLFNQIKAGEKVKLFKSSDGYA
DGEQLRDFVYVKDVVKVNLFFLENPSVSGIFNVGTGRARSFNDLASATFKALGKEVKIEYIDFPEDLRGK
YQSFTEADISKLRAAGYTKEFHSLEEGVKDYVKNYLA
>gnl|CDD|187560 cd05250, CC3_like_SDR_a, CC3(TIP30)-like, atypical (a) SDRs. Atypical SDRs in this subgroup include CC3 (also known as TIP30) which is implicated in tumor suppression. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine rich NAD(P)-binding motif that resembles the extended SDRs, and have an active site triad of the SDRs (YXXXK and upstream Ser), although the upstream Asn of the usual SDR active site is substituted with Asp. For CC3, the Tyr of the triad is displaced compared to the usual SDRs and the protein is monomeric, both these observations suggest that the usual SDR catalytic activity is not present. NADP appears to serve an important role as a ligand, and may be important in the interaction with other macromolecules. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
KTALVLGATGLVGKHLLRELLKSPYYSKVTAIVRRKLTFPEAKEKLVQIVVDFERLDEYLEAFQNPDVGF
CCLGTTRKKAGSQENFRKVDHDYVLKLAKLAKAAGVQHFLLVSSLGADPKSSFLYLKVKGEVERDLQKLG
FERLTIFRPGLLLGERQESRPGERLAQKLLRILSPLGFPKYKPIPAETVAKAMVKAALKESSNKVEILEN
KEIL
>gnl|CDD|187561 cd05251, NmrA_like_SDR_a, NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) SDRs. NmrA and HSCARG like proteins. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
ILVFGATGKQGGSVVRALLKDPGFKVRALTRDPSSPAAKALAAPGVEVVQGDLDDPESLEAALKGVYGVF
LVTDFWEAGGEDEIAQGKNVVDAAKRAGVQHFVFSSVPDVEKLTLAVPHFDSKAEVEEYIRASGLPATIL
RPAFFMENFLTPPAPQKMEDGTLTLVLPLDPDTKLPMIDVADIGPAVAAIFKDPAKFNGKTIELAGDELT
PEEIAAAFSKVLGKPVTYVQVEEWLRENGYAL
>gnl|CDD|187562 cd05252, CDP_GD_SDR_e, CDP-D-glucose 4,6-dehydratase, extended (e) SDRs. This subgroup contains CDP-D-glucose 4,6-dehydratase, an extended SDR, which catalyzes the conversion of CDP-D-glucose to CDP-4-keto-6-deoxy-D-glucose. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
FWQGKRVLVTGHTGFKGSWLSLWLQELGAKVIGYSLDPPTNPNLFELANLDNKISSTRGDIRDLNALREA
IREYEPEIVFHLAAQPLVRLSYKDPVETFETNVMGTVNLLEAIRETGSVKAVVNVTSDKCYENKEWGWGY
RENDPLGGHDPYSSSKGCAELIISSYRNSFFNPENYGKHGIAIASARAGNVIGGGDWAEDRIVPDCIRAF
EAGERVIIRNPNAIRPWQHVLEPLSGYLLLAEKLYERGEEYAEAWNFGPDDEDAVTVLELVEAMARYWGE
DARWDLDGNSHPHEANLLKLDCSKAKTMLGWRPRWNLEETLEFTVAWYKEWLSGED
>gnl|CDD|187563 cd05253, UDP_GE_SDE_e, UDP glucuronic acid epimerase, extended (e) SDRs. This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
MKILVTGAAGFIGFHVAKRLLERGDEVVGIDNLNDYYDVRLKEARLELLGKSGGFKFVKGDLEDREALRR
LFKDHEFDAVIHLAAQAGVRYSLENPHAYVDSNIVGFLNLLELCRHFGVKHLVYASSSSVYGLNTKMPFS
EDDRVDHPISLYAATKKANELMAHTYSHLYGIPTTGLRFFTVYGPWGRPDMALFLFTKAILEGKPIDVFN
DGNMSRDFTYIDDIVEGVVRALDTPAKPNPNWDAEAPDPSTSSAPYRVYNIGNNSPVKLMDFIEALEKAL
GKKAKKNYLPMQKGDVPETYADISKLQRLLGYKPKTSLEEGVKRFVEWYKEN
>gnl|CDD|187564 cd05254, dTDP_HR_like_SDR_e, dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs. dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
KILITGATGMLGRALVRLLKERGYEVIGTGRSRASLFKLDLTDPDAVEEAIRDYKPDVIINCAAYTRVDK
CESDPELAYRVNVLAPENLARAAKEVGARLIHISTDYVFDGKKGPYKEEDAPNPLNVYGKSKLLGEVAVL
NANPRYLILRTSWLYGELKNGENFVEWMLRLAAERKEVNVVHDQIGSPTYAADLADAILELIERNSLTGI
YHLSNSGPISKYEFAKLIADALGLPDVEIKPITSSEYPLPARRPANSSLDCSKLEELGGIKPPDWKEALR
>gnl|CDD|187565 cd05255, SQD1_like_SDR_e, UDP_sulfoquinovose_synthase (Arabidopsis thaliana SQD1 and related proteins), extended (e) SDRs. Arabidopsis thaliana UDP-sulfoquinovose-synthase (SQD1), an extended SDR, catalyzes the transfer of SO(3)(-) to UDP-glucose in the biosynthesis of plant sulfolipids. Members of this subgroup share the conserved SDR catalytic residues, and a partial match to the characteristic extended-SDR NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
MKVLILGGDGYCGWPTALHLSKRGHEVCIVDNLVRRRIDVELGLESLTPIASIHERLRAWKELTGKTIEF
YVGDACDYEFLAELLASHEPDAVVHFAEQRSAPYSMIDREHANYTQHNNVIGTLNLLFAIKEFDPDCHLV
KLGTMGEYGTPNIDIPEGYITIEHNGRRDTLPYPKQAGSWYHLSKVHDSHNIMFACKAWGIRITDLNQGV
VYGTKTEETEADERLINRFDYDGVFGTVLNRFCVQAAIGHPLTVYGKGGQTRGFISIRDTVQCLELALEN
PAKAGEYRVFNQFTEQFSVGELAEMVAEAGSKLGLDVKVEHLPNPRVEAEEHYYNAKNTKLLDLGLEPHY
LSESLLDSILNFAVKYADRVDEKRILPKVLWK
>gnl|CDD|187566 cd05256, UDP_AE_SDR_e, UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs. This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
RVLVTGGAGFIGSHLVERLLERGHEVIVLDNLSTGKKENLPEVKPNVKFIEGDIRDDELVEFAFEGVDYV
FHQAAQASVPRSIEDPIKDHEVNVLGTLNLLEAARKAGVKRFVYASSSSVYGDPPYLPKDEDHPPNPLSP
YAVSKYAGELYCQVFARLYGLPTVSLRYFNVYGPRQDPNGGYAAVIPIFIERALKGEPPTIYGDGEQTRD
FTYVEDVVEANLLAATAGAGGEVYNIGTGKRTSVNELAELIREILGKELEPVYAPPRPGDVRHSLADISK
AKKLLGWEPKVSFEEGLRLTVEWF
>gnl|CDD|187567 cd05257, Arna_like_SDR_e, Arna decarboxylase_like, extended (e) SDRs. Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
NVLVTGADGFIGSHLTERLLREGHEVRALDIYNSFNSWGLLDNAVHDRFHFISGDVRDASEVEYLVKKCD
VVFHLAALIAIPYSYTAPLSYVETNVFGTLNVLEAACVLYRKRVVHTSTSEVYGTAQDVPIDEDHPLLYI
NKPRSPYSASKQGADRLAYSYGRSFGLPVTIIRPFNTYGPRQSARAVIPTIISQRAIGQRLINLGDGSPT
RDFNFVKDTARGFIDILDAIEAVGEIINNGSGEEISIGNPAVELIVEELGEMVLIVYDDHREYRPGYSEV
ERRIPDIRKAKRLLGWEPKYSLRDGLRETIEWFKDQ
>gnl|CDD|187568 cd05258, CDP_TE_SDR_e, CDP-tyvelose 2-epimerase, extended (e) SDRs. CDP-tyvelose 2-epimerase is a tetrameric SDR that catalyzes the conversion of CDP-D-paratose to CDP-D-tyvelose, the last step in tyvelose biosynthesis. This subgroup is a member of the extended SDR subfamily, with a characteristic active site tetrad and NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
MRVLITGGAGFIGSNLARFFLKQGWEVIGFDNLMRRGSFGNLAWLKANREDGGVRFVHGDIRNRNDLEDL
FEDIDLIIHTAAQPSVTTSASSPRLDFETNALGTLNVLEAARQHAPNAPFIFTSTNKVYGDLPNYLPLEE
LETRYELAPEGWSPAGISESFPLDFSHSLYGASKGAADQYVQEYGRIFGLKTVVFRCGCLTGPRQFGTED
QGWVAYFLKCAVTGKPLTIFGYGGKQVRDVLHSADLVNLYLRQFQNPDRRKGEVFNIGGGRENSVSLLEL
IALCEEITGRKMESYKDENRPGDQIWYISDIRKIKEKPGWKPERDPREILAEIYAWI
>gnl|CDD|187569 cd05259, PCBER_SDR_a, phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs. PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
KIAIAGATGTLGGPIVSALLASPGFTVTVLTRPSSTSSNEFQPSGVKVVPVDYASHESLVAALKGVDAVI
SALGGAAIGDQLKLIDAAIAAGVKRFIPSEFGVDYDRIGALPLLDLFDEKRDVRRYLRAKNAGLPWTYVS
TGMFLDYLLEPLFGVVDLANRTATIYGDGETKFAFTTLEDIGRAVARALTHPDRTLNRVVFVAGDVVTQN
ELIALVERVTGRKFERTYVSEEELLEELIEAAPAGLLNYVIAFLHGLGIGGGDVEKSDAEYLGLKVETVE
EL
>gnl|CDD|187570 cd05260, GDP_MD_SDR_e, GDP-mannose 4,6 dehydratase, extended (e) SDRs. GDP-mannose 4,6 dehydratase, a homodimeric SDR, catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway. These proteins have the canonical active site triad and NAD-binding pattern, however the active site Asn is often missing and may be substituted with Asp. A Glu residue has been identified as an important active site base. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
RALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSFNTDRIDHLYINKDRITLHYGDLTDSSSLRRAIEK
VRPDEIYHLAAQSHVKVSFDDPEYTAEVNAVGTLNLLEAIRILGLDARFYQASSSEEYGKVQELPQSETT
PFRPRSPYAVSKLYADWITRNYREAYGLFAVNGRLFNHEGPRRGETFVTRKITRQVARIKAGLQPVLKLG
NLDAKRDWGDARDYVEAYWLLLQQGEPDDYVIATGETHSVREFVELAFEESGLTGDIEVEIDPRYFRPTE
VDLLLGDPSKAREELGWKPEVSFEELVREMLDADLE
>gnl|CDD|187571 cd05261, CAPF_like_SDR_e, capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs. This subgroup of extended SDRs, includes some members which have been identified as capsular polysaccharide assembling proteins, such as Staphylococcus aureus Cap5F which is involved in the biosynthesis of N-acetyl-l-fucosamine, a constituent of surface polysaccharide structures of S. aureus. This subgroup has the characteristic active site tetrad and NAD-binding motif of extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
MKILITGAKGFIGKNLIARLKEQKDDDIFFYDRESDESELDDFLQGADFIFHLAGVNRPKDEAEFESGNV
GLTERLLDALTRNGKKPPILLSSSIQAALDNPYGKSKLAAEELLQEYARETGAPVYIYRLPNVFGKWCRP
NYNSAVATFCYNIARDLPIQINDPAAELTLVYIDDVVDELIQLLEGAPTYSGGFDQVLPVYKVTVGEIAE
LLYKFKESRDTLILPNVGTGFDRALYSTYLSYLPPESF
>gnl|CDD|187572 cd05262, SDR_a7, atypical (a) SDRs, subgroup 7. This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
MKVFVTGATGFIGSAVVRELVAAGHEVVGLARSDAGAAKLEAAGAQVHRGDLEDLDILRKAAAEADAVIH
LAFTHDFDNFAQACEVDRRAIEALGEALRGTGKPLIYTSGIWLLGPTGGQEEDEEAPDDPPTPAARAVSE
AAALELAERGVRASVVRLPPVVHGRGDHGFVPMLIAIAREKGVSAYVGDGKNRWPAVHRDDAARLYRLAL
EKGKAGSVYHAVAEEGIPVKDIAEAIGRRLGVPVVSIPAEEAAAHFGWLAMFVALDQPVSSQKTRRRLGW
KPQQPSLLEDL
>gnl|CDD|187573 cd05263, MupV_like_SDR_e, Pseudomonas fluorescens MupV-like, extended (e) SDRs. This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
VFVTGGTGFLGRHLVKRLLENGFKVLVLVRSESLGEAHERIEEAGLEADRVRVLEGDLTQPNLGLSAAAS
RELAGKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTAYVAGNREGNIRETEL
NPGQNFKNPYEQSKAEAEQLVRAAATQIPLTVYRPSIVVGDSKTGRIEKIDGLYELLNLLAKLGRWLPMP
GNKGARLNLVPVDYVADAIVYLSKKPEANGQIFHLTDPTPQTLREIADLFKSAFLSPGLLVLLMNEPNAS
LPNALRRSLLNLP
>gnl|CDD|187574 cd05264, UDP_G4E_5_SDR_e, UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs. This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
RVLIVGGNGFIGSHLVDALLEEGPQVRVFDRSIPPYELPLGGVDYIKGDYENRADLESALVGIDTVIHLA
STTNPATSNKNPILDIQTNVAPTVQLLEACAAAGIGKIIFASSGGTVYGVPEQLPISESDPTLPISSYGI
SKLAIEKYLRLYQYLYGLDYTVLRISNPYGPGQRPDGKQGVIPIALNKILRGEPIEIWGDGESIRDYIYI
DDLVEALMALLRSKGLEEVFNIGSGIGYSLAELIAEIEKVTGRSVQVIYTPARTTDVPKIVLDISRARAE
LGWSPKISLEDGLEKTWQWI
>gnl|CDD|187575 cd05265, SDR_a1, atypical (a) SDRs, subgroup 1. Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
MKILIIGGTRFIGKALVEELLAAGHDVTVFNRGRTKPDLPEGVEHIVGDRNDRDALEELLGGEDFDVVVD
TIAYTPRQVERALDAFKGRVKQYIFISSASVYLKPGRVITESTPLREPDAVGLSDPWDYGRGKRAAEDVL
IEAAAFPYTIVRPPYIYGPGDYTGRLAYFFDRLARGRPILVPGDGHSLVQFIHVKDLARALLGAAGNPKA
IGGIFNITGDEAVTWDELLEACAKALGKEAEIVHVEEDFL
>gnl|CDD|187576 cd05266, SDR_a4, atypical (a) SDRs, subgroup 4. Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
VLILGCGYLGQRLARQLLAQGWQVTGTTRSPEKLAADRPAGVTPLAADLTQPGLLADVDHLVISLPPPAG
SYRGGYDPGLRALLDALAQLPAVQRVIYLSSTGVYGDQQGEWVDETSPPNPSTESGRALLEAEQALLALG
SKPTTILRLAGIYGPGRHPLRRLAQGTGRPPAGNAPTNRIHVDDLVGALAFALQRPAPGPVYNVVDDLPV
TRGEFYQAAAELLGLPPPPFIPFAFLREGKRVSNDRLKAEL
>gnl|CDD|187577 cd05267, SDR_a6, atypical (a) SDRs, subgroup 6. These atypical SDR family members of unknown function have only a partial match to a prototypical glycine-rich NAD(P)-binding motif consensus, GXXG, which conserves part of the motif of extended SDR. Furthermore, they lack the characteristic active site residues of the SDRs. This subgroup is related to phenylcoumaran benzylic ether reductase, an NADPH-dependent aromatic alcohol reductase. One member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
KKVLILGANGEIAREATTMLLENSNVELTLFLRNAHRLLHLKSARVTVVEGDALNSDDLKAAMRGQDVVY
ANLGGTDLDQQAENVVQAMKAVGVKRLIWTTSLGIYDEVPGKFGEWNKEFIGNYLAPYRKSAAVIENSDL
DYTLLRPAWLTNNDEIDYELTPKGEAFKGTEVSRKSVADLITDIINHPDYHVRESIGINKPGT
>gnl|CDD|187578 cd05269, TMR_SDR_a, triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs. TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
ILVTGATGKLGTAVVELLLAKVASVVALVRNPEKAKAFAADGVEVRQGDYDDPETLERAFEGVDRLLLIS
PSDLEDRIQQHKNFIDAAKQAGVKHIVYLSASGADEDSPFLLARDHGATEKYLEASGIPYTILRPGWFMD
NLLEFLPSILEEGTIYGPAGDGKVAFVDRRDIAEAAAAALTEPGHEGKVYNLTGPEALSYAELAAILSEA
LGKPVRYVPVSPDEAARELLAAGLPEGFAALLASLYAAIRKGELAVVSDDVEKLTGRPPRSL
>gnl|CDD|187579 cd05271, NDUFA9_like_SDR_a, NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs. This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
MVVTVFGATGFIGRYVVNRLAKRGSQVIVPYRCEAYARRLLVMGDLGQVLFVEFDLRDDESIRKALEGSD
VVINLVGRLYETKNFSFEDVHVEGPERLAKAAKEAGVERLIHISALGADANSPSKYLRSKAEGEEAVREA
FPEATIVRPSVVFGREDRFLNRFAKLLAFLPFPPLIGGGQTKFQPVYVGDVAEAIARALKDPETEGKTYE
LVGPKVYTLAELVELLRRLGGRKRRVLPLPLWLARLIARVKLLLLLPEPPLTRDQLERLKTDN
>gnl|CDD|187580 cd05272, TDH_SDR_e, L-threonine dehydrogenase, extended (e) SDRs. This subgroup contains members identified as L-threonine dehydrogenase (TDH). TDH catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. This group is distinct from TDHs that are members of the medium chain dehydrogenase/reductase family. This group has the NAD-binding motif and active site tetrad of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
RILITGGLGQIGSELAKLLRKRYGKDNVIASDIRKPPAHVVLSGPFEYLDVLDFKSLEEIVVNHKITWII
HLAALLSAVGEKNPPLAWDVNMNGLHNVLELAREHNLRIFVPSTIGAFGPTTPRNNTPDDTIQRPRTIYG
VSKVAAELLGEYYHHKFGVDFRSLRYPGIISYDTLPGGGTTDYAVQIFYEALKKGKYTCYLKPDTRLPMM
YMPDALRATIELMEAPAEKLKHRRTYNITAMSFTPEEIAAEIKKHIPEFQITYEVDPRRQAIADSWPMSL
DDSNARKDWGWKHKYDLDSMVKDMLEKL
>gnl|CDD|187581 cd05273, GME-like_SDR_e, Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs. This subgroup of NDP-sugar epimerase/dehydratases are extended SDRs; they have the characteristic active site tetrad, and an NAD-binding motif: TGXXGXX[AG], which is a close match to the canonical NAD-binding motif. Members include Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME) which catalyzes the epimerization of two positions of GDP-alpha-D-mannose to form GDP-beta-L-galactose. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
QRALVTGAGGFIGSHLAERLKAEGHYVRGADWKSPEHMTQPTDDDEFHLVDLREMENCLKATEGVDHVFH
LAADMGGMGYIQSNHAVIMYNNTLINFNMLEAARINGVERFLFASSACVYPEFKQLETTVVRLREEDAWP
AEPQDAYGWEKLATERLCQHYNEDYGIETRIVRFHNIYGPRGTWDGGREKAPAAMCRKVATAKDGDRFEI
WGDGLQTRSFTYIDDCVEGLRRLMESDFGEPVNLGSDEMVSMNELAEMVLSFSGKPLEIIHHTPGPQGVR
GRNSDNTLLKEELGWEPNTPLEEGLRITYFWIKEQIEAEKAKTSDVSL
>gnl|CDD|187582 cd05274, KR_FAS_SDR_x, ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs. Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
TLAALAWQAGALSLLAVAPACGAADAVLALAALLALVAALLAAYASTGPPLWLVTRGAEAVSADDVAALA
QAALWGLLRVLALEHPELWGGLVDLDAADAADEAAALAALLAGAPGEDELALRGGQRLVPRLVRAPAAAL
ELAAAPGGLDGTYLITGGLGGLGLLVARWLAARGARHLVLLSRRGPAPRAAARAALLRAGGARVSVVRCD
VTDPAALAALLAELAAGGPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLHELTPDLPLDFFV
LFSSVAALLGGAGQAAYAAANAFLDALAAQRRRRGLPATSVQWGAWAGGGMAAAAALRARLARSGLGPLA
PAEALEALEALLASDAPQAVVASVD
>gnl|CDD|176180 cd05276, p53_inducible_oxidoreductase, PIG3 p53-inducible quinone oxidoreductase. PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MKAIVIKEPGGPEVLELGEVPKPAPGPGEVLIRVAAAGVNRADLLQRQGLYPPPPGASDILGLEVAGVVV
AVGPGVTGWKVGDRVCALLAGGGYAEYVVVPAGQLLPVPEGLSLVEAAALPEVFFTAWQNLFQLGGLKAG
ETVLIHGGASGVGTAAIQLAKALGARVIATAGSEEKLEACRALGADVAINYRTEDFAEEVKEATGGRGVD
VILDMVGGDYLARNLRALAPDGRLVLIGLLGGAKAELDLAPLLRKRLTLTGSTLRSRSLEEKAALAAAFR
EHVWPLFASGRIRPVIDKVFPLEEAAEAHRRMESNEHIGKIVL
>gnl|CDD|176181 cd05278, FDH_like, Formaldehyde dehydrogenases. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit
MKALVYLGPGKIGLEEVPDPKIQGPHDAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVG
SDVKRLKPGDRVSVPCITFCGRCRFCRRGYHAHCENGLWGWKLGNRIDGGQAEYVRVPYADMNLAKIPDG
LPDEDALMLSDILPTGFHGAELAGIKPGSTVAVIGAGPVGLCAVAGARLLGAARIIAVDSNPERLDLAKE
AGATDIINPKNGDIVEQILELTGGRGVDCVIEAVGFEETFEQAVKVVRPGGTIANVGVYGKPDPLPLLGE
WFGKNLTFKTGLVPVRARMPELLDLIEEGKIDPSKLITHRFPLDDILKAYRLFDNKPDGCIKVVIRP
>gnl|CDD|176182 cd05279, Zn_ADH1, Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding
CKAAVLWEKGKPLSIEEIEVAPPKAGEVRIKVVATGVCHTDLHVIDGKLPTPLPVILGHEGAGIVESIGP
GVTTLKPGDKVIPLFGPQCGKCKQCLNPRPNLCSKSRGTNGRGLMSDGTSRFTCKGKPIHHFLGTSTFAE
YTVVSEISLAKIDPDAPLEKVCLIGCGFSTGYGAAVNTAKVTPGSTCAVFGLGGVGLSVIMGCKAAGASR
IIAVDINKDKFEKAKQLGATECINPRDQDKPIVEVLTEMTDGGVDYAFEVIGSADTLKQALDATRLGGGT
SVVVGVPPSGTEATLDPNDLLTGRTIKGTVFGGWKSKDSVPKLVALYRQKKFPLDELITHVLPFEEINDG
FDLMRSGESIRTILT
>gnl|CDD|176183 cd05280, MDR_yhdh_yhfp, Yhdh and yhfp-like putative quinone oxidoreductases. Yhdh and yhfp-like putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
FKALVVEEQDGGVSLFLRTLPLDDLPEGDVLIRVHYSSLNYKDALAATGNGGVTRNYPHTPGIDAAGTVV
SSDDPRFREGDEVLVTGYDLGMNTDGGFAEYVRVPADWVVPLPEGLSLREAMILGTAGFTAALSVHRLED
NGQTPEDGPVLVTGATGGVGSIAVAILAKLGYTVVALTGKEEQADYLKSLGASEVLDREDLLDESKKPLL
KARWAGAIDTVGGDVLANLLKQTKYGGVVASCGNAAGPELTTTVLPFILRGVSLLGIDSVNCPMELRKQV
WQKLATEWKPDLLEIVVREISLEELPEAIDRLLAGKHRGRTVVKI
>gnl|CDD|176184 cd05281, TDH, Threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria) and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose
MKAIVKTKAGPGAELVEVPVPKPGPGEVLIKVLAASICGTDVHIYEWDEWAQSRIKPPLIFGHEFAGEVV
EVGEGVTRVKVGDYVSAETHIVCGKCYQCRTGNYHVCQNTKILGVDTDGCFAEYVVVPEENLWKNDKDIP
PEIASIQEPLGNAVHTVLAGDVSGKSVLITGCGPIGLMAIAVAKAAGASLVIASDPNPYRLELAKKMGAD
VVINPREEDVVEVKSVTDGTGVDVVLEMSGNPKAIEQGLKALTPGGRVSILGLPPGPVDIDLNNLVIFKG
LTVQGITGRKMFETWYQVSALLKSGKVDLSPVITHKLPLEDFEEAFELMRSGKCGKVVLYP
>gnl|CDD|176645 cd05282, ETR_like, 2-enoyl thioester reductase-like. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain
VVYTQFGEPLPLVLELVSLPIPPPGPGEVLVRMLAAPINPSDLITISGAYGSRPPLPAVPGNEGVGVVVE
VGSGVSGLLVGQRVLPLGGEGTWQEYVVAPADDLIPVPDSISDEQAAMLYINPLTAWLMLTEYLKLPPGD
WVIQNAANSAVGRMLIQLAKLLGFKTINVVRRDEQVEELKALGADEVIDSSPEDLAQRVKEATGGAGARL
ALDAVGGESATRLARSLRPGGTLVNYGLLSGEPVPFPRSVFIFKDITVRGFWLRQWLHSATKEAKQETFA
EVIKLVEAGVLTTPVGAKFPLEDFEEAVAAAEQPGRGGKVLLT
>gnl|CDD|176186 cd05283, CAD1, Cinnamyl alcohol dehydrogenases (CAD). Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
KGYAARDASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGS
KVTKFKVGDRVGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKYPDGTITQGGYADHIVVDERFVFKIP
EGLDSAAAAPLLCAGITVYSPLKRNGVGPGKRVGVVGIGGLGHLAVKFAKALGAEVTAFSRSPSKKEDAL
KLGADEFIATKDPEAMKKAAGSLDLIIDTVSASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGR
KSVAGSLIGGRKETQEMLDFAAEHGIKPWVEVIPMDGINEALERLEKGDVRYRFVLD
>gnl|CDD|176187 cd05284, arabinose_DH_like, D-arabinose dehydrogenase. This group contains arabinose dehydrogenase (AraDH) and related alcohol dehydrogenases. AraDH is a member of the medium chain dehydrogenase/reductase family and catalyzes the NAD(P)-dependent oxidation of D-arabinose and other pentoses, the initial step in the metabolism of d-arabinose into 2-oxoglutarate. Like the alcohol dehydrogenases, AraDH binds a zinc in the catalytic cleft as well as a distal structural zinc. AraDH forms homotetramers as a dimer of dimers. AraDH replaces a conserved catalytic His with replace with Arg, compared to the canonical ADH site. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MKAARLYEYGKPLRLEDVPVPEPGPGQVLVRVGGAGVCHSDLHVIDGVWGGILPYKLPFTLGHENAGWVE
EVGSGVDGLKEGDPVVVHPPWGCGTCRYCRRGEENYCENARFPGIGTDGGFAEYLLVPSRRLVKLPRGLD
PVEAAPLADAGLTAYHAVKKALPYLDPGSTVVVIGVGGLGHIAVQILRALTPATVIAVDRSEEALKLAER
LGADHVLNASDDVVEEVRELTGGRGADAVIDFVGSDETLALAAKLLAKGGRYVIVGYGGHGRLPTSDLVP
TEISVIGSLWGTRAELVEVVALAESGKVKVEITKFPLEDANEALDRLREGRVTGRAVLVP
>gnl|CDD|176188 cd05285, sorbitol_DH, Sorbitol dehydrogenase. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit
AAVLHGPGDLRLEERPIPEPGPGEVLVRVRAVGICGSDVHYYKHGRIGDFVVKEPMVLGHESAGTVVAVG
SGVTHLKVGDRVAIEPGVPCRTCEFCKSGRYNLCPDMRFAATPPVDGTLCRYVNHPADFCHKLPDNVSLE
EGALVEPLSVGVHACRRAGVRPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAKELGATH
TVNVRTEDTPESAEKIAELLGGKGPDVVIECTGAESCIQTAIYATRPGGTVVLVGMGKPEVTLPLSAASL
REIDIRGVFRYANTYPTAIELLASGKVDVKPLITHRFPLEDAVEAFETAAKGKKGVIKVVIEG
>gnl|CDD|176189 cd05286, QOR2, Quinone oxidoreductase (QOR). Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 2-haloacrylate reductase, a member of this subgroup, catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR, Burkholderia 2-haloacrylate reductase does not act on the quinones 1,4-benzoquinone and 1,4-naphthoquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
KAVRIHKTGGPEVLEYEDVPVPEPGPGEVLVRNTAIGVNFIDTYFRSGLYPLPLPFVLGVEGAGVVEAVG
PGVTGFKVGDRVAYAGPPGAYAEYRVVPASRLVKLPDGISDETAAALLLQGLTAHYLLRETYPVKPGDTV
LVHAAAGGVGLLLTQWAKALGATVIGTVSSEEKAELARAAGADHVINYRDEDFVERVREITGGRGVDVVY
DGVGKDTFEGSLDSLRPRGTLVSFGNASGPVPPFDLLRLSKGSLFLTRPSLFHYIATREELLARAAELFD
AVASGKLKVEIGKRYPLADAAQAHRDLESRKTTGKLLLIP
>gnl|CDD|176190 cd05288, PGDH, Prostaglandin dehydrogenases. Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES
SNRQVVLAKRPEGPPPPDDFELVEVPLPELKDGEVLVRTLYLSVDPYMRGWMSDAKSYSPPVQLGEPMRG
GGVGEVVESRSPDFKVGDLVSGFLGWQEYAVVDGASGLRKLDPSLGLPLSAYLGVLGMTGLTAYFGLTEI
GKPKPGETVVVSAAAGAVGSVVGQIAKLLGARVVGIAGSDEKCRWLVEELGFDAAINYKTPDLAEALKEA
APDGIDVYFDNVGGEILDAALTLLNKGGRIALCGAISQYNATEPPGPKNLGNIITKRLTMQGFIVSDYAD
RFPEALAELAKWLAEGKLKYREDVVEGLENAPEAFLGLFTGKNTGKLVV
>gnl|CDD|176191 cd05289, MDR_like_2, alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases. Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MKAVRIHEYGGPEVLELADVPTPEPGPGEVLVKVHAAGVNPVDLKIREGLLKAAFPLTLPLIPGHDVAGV
VVAVGPGVTGFKVGDEVFGMTPFTRGGAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQALFELG
GLKAGQTVLIHGAAGGVGSFAVQLAKARGARVIATASAANADFLRSLGADEVIDYTKGDFERAAAPGGVD
AVLDTVGGETLARSLALVKPGGRLVSIAGPPPAEQAAKRRGVRAGFVFVEPDGEQLAELAELVEAGKLRP
VVDRVFPLEDAAEAHERLESGHARGKVVL
>gnl|CDD|133426 cd05290, LDH_3, A subgroup of L-lactate dehydrogenases. L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed of some bacterial LDHs from firmicutes, gammaproteobacteria, and actinobacteria. Vertebrate LDHs are non-allosteric, but some bacterial LDHs are activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenase, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
KLVVIGAGHVGSAVLNYALALGLFSEIVLIDVNEGVAEGEALDFHHATALTYSTNTKIRAGDYDDCADAD
IIVITAGPSIDPGNTDDRLDLAQTNAKIIREIMGNITKVTKEAVIILITNPLDIAVYIAATEFDYPANKV
IGTGTMLDTARLRRIVADKYGVDPKNVTGYVLGEHGSHAFPVWSLVNIAGLPLDELEALFGKEPIDKDEL
LEEVVQAAYDVFNRKGWTNAGIAKSASRLIKAILLDERSILPVCTLLSGEYGLSDVALSLPTVIGAKGIE
RVLEIPLDEWELEKLHKSAKAIRETIE
>gnl|CDD|133427 cd05291, HicDH_like, L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases. L-2-hydroxyisocapronate dehydrogenase (HicDH) catalyzes the conversion of a variety of 2-oxo carboxylic acids with medium-sized aliphatic or aromatic side chains. This subfamily is composed of HicDHs and some bacterial L-lactate dehydrogenases (LDH). LDHs catalyze the last step of glycolysis in which pyruvate is converted to L-lactate. Bacterial LDHs can be non-allosteric or may be activated by an allosteric effector such as fructose-1,6-bisphosphate. Members of this subfamily with known structures such as the HicDH of Lactobacillus confusus, the non-allosteric LDH of Lactobacillus pentosus, and the allosteric LDH of Bacillus stearothermophilus, show that they exist as homotetramers. The HicDH-like subfamily is part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
RKVVIIGAGHVGSSFAYSLVNQGIADELVLIDINEEKAEGEALDLEDALAFLPSPVKIKAGDYSDCKDAD
IVVITAGAPQKPGETRLDLLEKNAKIMKSIVPKIKASGFDGIFLVASNPVDVITYVVQKLSGLPKNRVIG
TGTSLDTARLRRALAEKLNVDPRSVHAYVLGEHGDSQFVAWSTVTVGGKPLLDLLKEGKLSELDLDEIEE
DVRKAGYEIINGKGATYYGIATALARIVKAILNDENAILPVSAYLDGEYGEKDVYIGVPAIIGRNGVEEV
IELDLTEEEQEKFEKSADIIKENIKK
>gnl|CDD|133428 cd05292, LDH_2, A subgroup of L-lactate dehydrogenases. L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed predominantly of bacterial LDHs and a few fungal LDHs. Bacterial LDHs may be non-allosteric or may be activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
MKVAIVGAGFVGSTTAYALLLRGLASEIVLVDINKAKAEGEAMDLAHGTPFVKPVRIYAGDYADCKGADV
VVITAGANQKPGETRLDLLKRNVAIFKEIIPQILKYAPDAILLVVTNPVDVLTYVAYKLSGLPPNRVIGS
GTVLDTARFRYLLGEHLGVDPRSVHAYIIGEHGDSEVAVWSSANIGGVPLDEFCKLCGRPFDEEVREEIF
EEVRNAAYEIIERKGATYYAIGLALARIVEAILRDENSVLTVSSLLDGQYGIKDVALSLPCIVGRSGVER
VLPPPLSEEEEEALRASAEVLKEAIESL
>gnl|CDD|133429 cd05293, LDH_1, A subgroup of L-lactate dehydrogenases. L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed of eukaryotic LDHs. Vertebrate LDHs are non-allosteric. This is in contrast to some bacterial LDHs that are activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
KPRNKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDKLKGEAMDLQHGSAFLKNPKIEADKDYSVTA
NSKVVIVTAGARQNEGESRLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHR
VIGSGCNLDSARFRYLIAERLGVAPSSVHGWIIGEHGDSSVPVWSGVNVAGVRLQDLNPDIGTDKDPEKW
KEVHKQVVDSAYEVIKLKGYTSWAIGLSVADLVDAILRNTGRVHSVSTLVKGLHGIEDEVFLSLPCILGE
NGITHVIKQPLTEEEQEKLQKSADTLWEVQKQ
>gnl|CDD|133430 cd05294, LDH-like_MDH_nadp, A lactate dehydrogenases-like structure with malate dehydrogenase enzymatic activity. The LDH-like MDH proteins have a lactate dehyhydrogenase-like (LDH-like) structure and malate dehydrogenase (MDH) enzymatic activity. This subgroup is composed of some archaeal LDH-like MDHs that prefer NADP(H) rather than NAD(H) as a cofactor. One member, MJ0490 from Methanococcus jannaschii, has been observed to form dimers and tetramers during crystalization, although it is believed to exist primarilly as a tetramer in solution. In addition to its MDH activity, MJ0490 also possesses fructose-1,6-bisphosphate-activated LDH activity. Members of this subgroup have a higher sequence similarity to LDHs than to other MDHs. LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)- binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenase, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
MKVSIIGASGRVGSATALLLAKEDVVKEINLISRPKSLEKLKGLRLDIYDALAAAGIDAEIKISSDLSDV
AGSDIVIITAGVPRKEGMSRLDLAKKNAKIVKKYAKQIAEFAPDTKILVVTNPVDVMTYKALKESGFDKN
RVFGLGTHLDSLRFKVAIAKHFNVHISEVHTRIIGEHGDSMVPLISSTSIGGIPIKRFPEYKDFDVEKIV
ETVKNAGQNIISLKGGSEYGPASAISNLVRTIANDERRILTVSTYLEGEIDGIRDVCIGVPVKLGKNGIE
EIVPIEMDDDEREAFRKSAEIVKKYTREV
>gnl|CDD|133431 cd05295, MDH_like, Malate dehydrogenase-like. These MDH-like proteins are related to other groups in the MDH family but do not have conserved substrate and cofactor binding residues. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. Members of this subgroup are uncharacterized MDH-like proteins from animals. They are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
RADCPYYAKAELLADYLQKNLPDFRVHKIVKHPDEWEDWLQDLCKKNGWSHKRSPIIWRELLDRGGKGLL
LGGCNEFLEYAESYYGITSSMMSEEMTVIAEENLETHIEVEKEEEELRSKINPLQVCITNASAPLCYHLI
PSLASGEVFGMEEEISIHLLDSPENLEKLKGLVMEVEDLAFPLLRGISVTTDLDVAFKDAHVIVLLDDFL
IKEGEDLEGCIRSRVAICQLYGPLIEKNAKEDVKVIVAGRTFLNLKTSILIKYAPSIPRKNIIAVARLQE
NRAKALLARKLNVNSAGIKDVIVWGNIGGNTYIDLSKARVYRYDSAIWGPPNYSRPVLELVHDSKWINGE
FVATLKSLSSSLNHEAAISPAHAIATTLSYWYHGSPPGEIFSLGVISEGWYGIPEGIVFSMPVKFQNGSW
EVVTDLELSEILREVLKRITSDLIQEKLVALG
>gnl|CDD|133432 cd05296, GH4_P_beta_glucosidase, Glycoside Hydrolases Family 4; Phospho-beta-glucosidase. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases such as the phospho-beta-glucosidases. Other organisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. The 6-phospho-beta-glucosidase from Thermotoga maritima hydrolylzes cellobiose 6-phosphate (6P) into glucose-6P and glucose, in an NAD+ and Mn2+ dependent fashion. The Escherichia coli 6-phospho-beta-glucosidase (also called celF) hydrolyzes a variety of phospho-beta-glucosides including cellobiose-6P, salicin-6P, arbutin-6P, and gentobiose-6P. Phospho-beta-glucosidases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
MKLTIIGGGSSYTPELIEGLIRRYEELPVTELVLVDIDEEEKLEIVGALAKRMVKKAGLPIKVHLTTDRR
EALEGADFVFTQIRVGGLEARALDERIPLKHGVIGQETTGAGGFAKALRTIPVILDIAEDVEELAPDAWL
INFTNPAGIVTEAVLRHTGDRVIGLCNVPIGLQRRIAELLGVDPEDVFIDYAGLNHLGWLRRVLLDGEDV
LPELLEDLAALLSFEEGLLFGPELLRALGALPNEYLRYYYQTDEALEEILEAAGTRGEVVKEVEKELFEL
YKDPNLDEKPKELEKRGGAGYSEAALALISAIYNDKGDIHVVNVRNNGAIPGLPDDAVVEVPCVVDADGA
HPLPVGPLPPAILGLIQQVKAYERLTIEAAVEGDRDLALLALALHPLVPSVSVAKKLLDELLEAHKEYL
>gnl|CDD|133433 cd05297, GH4_alpha_glucosidase_galactosidase, Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases. Glucosidases cleave glycosidic bonds to release glucose from oligosaccharides. Alpha-glucosidases and alpha-galactosidases release alpha-D-glucose and alpha-D-galactose, respectively, via the hydrolysis of alpha-glycopyranoside bonds. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases such as the alpha-glucosidases. Other organsisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. Alpha-glucosidases and alpha-galactosidases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
IKIAFIGAGSVVFTKNLVGDLLKTPELSGSTIALMDIDEERLETVEILAKKIVEELGAPLKIEATTDRRE
ALDGADFVINTIQVGGHEYTETDFEIPEKYGYYQTVGDTSGPGGIFRALRTIPVLLDIARDIEELCPDAW
LLNYANPMAELTWALNRYTPIKTVGLCHGVQGTAEQLAKLLGEPPEEVDYQVAGINHMAWLLKFEYNGED
LYPLLDEWIEEGSEEWDQLSPVRFDMYRRYGLFPTESSEHLSEYVPHYRKETKKIWYGEFNEDEYGGRDE
EQGWEWYEERLKLILAEIDKEELDPVKRSGEYASPIIEALVTGKPRRINGNVPNNGLIPNLPDDVVVEVP
ALVDRNGIHPEKIGPLPPQLAALIRPRINVQELAVEAALTGDRELLYQALMLDPLTKAELQLEEIWDEVD
ELP
>gnl|CDD|133434 cd05298, GH4_GlvA_pagL_like, Glycoside Hydrolases Family 4; GlvA- and pagL-like glycosidases. Bacillus subtilis GlvA and Clostridium acetobutylicum pagL are 6-phospho-alpha-glucosidase, catalyzing the hydrolysis of alpha-glucopyranoside bonds to release glucose from oligosaccharides. The substrate specificities of other members of this subgroup are unknown. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP_PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases, which include 6-phospho-beta-glucosidases, 6-phospho-alpha-glucosidases, alpha-glucosidases/alpha-glucuronidases (only from Thermotoga), and alpha-galactosidases. Members of this subfamily are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others
FKIVIAGGGSTYTPGIVKSLLDRKEDFPLRELVLYDIDAERQEKVAEAVKILFKENYPEIKFVYTTDPEE
AFTDADFVFAQIRVGGYAMREQDEKIPLKHGVVGQETCGPGGFAYGLRSIGPMIELIDDIEKYSPDAWIL
NYSNPAAIVAEALRRLFPNARILNICDMPIAIMDSMAAILGLDRKDLEPDYFGLNHFGWFTKIYDKQGED
LLPKLREHVKENGYLPPDSDEEHRDPSWNDTFANAKDMMADFPDYLPNTYLQYYLYPDYMVEHSNPNYTR
ANEVMDGREKRVFEECRKIIETGTAEGSTFHVDVHGEYIVDLAASIAYNTKERFLVIVENNGAIPNLPDD
AMVEVPAYIGSNGPEPLVVGKIPTFYKGLMEQQVAYEKLLVEAYLEGSYQKALQAFTLNRTVPSAKVAKE
VLDDLIEANKGYWPELK
>gnl|CDD|240624 cd05299, CtBP_dh, C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related repressor. The transcriptional corepressor CtBP is a dehydrogenase with sequence and structural similarity to the d2-hydroxyacid dehydrogenase family. CtBP was initially identified as a protein that bound the PXDLS sequence at the adenovirus E1A C terminus, causing the loss of CR-1-mediated transactivation. CtBP binds NAD(H) within a deep cleft, undergoes a conformational change upon NAD binding, and has NAD-dependent dehydrogenase activity
PKVVITDYDFPDLDIEREVLEEAGVELVDAQSRTEDELIEAAADADALLVQYAPVTAEVIEALPRLKVIV
RYGVGVDNVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTVGGPIRRL
RGLTLGLVGFGRIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGVRVVSLDELLARSDVVSLHCPLTPET
RHLIDAEALALMKPGAFLVNTARGGLVDEAALARALKSGRIAGAALDVLEEEPPPADSPLLSAPNVILTP
HAAWYSEESLAELRRKAAEEVVRVLRGEPPRN
>gnl|CDD|240625 cd05300, 2-Hacid_dh_1, Putative D-isomer specific 2-hydroxyacid dehydrogenase. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants
MKILVLSPLDDEHLERLRAAAPGAELRVVTAEELTEELADADVLLGNPPLPELLPAAPRLRWIQSTSAGV
DALLFPELLERDVVLTNARGIFGPPIAEYVLGYMLAFARKLPRYARNQAERRWQRRGPVRELAGKTVLIV
GLGDIGREIARRAKAFGMRVIGVRRSGRPAPPVVDEVYTPDELDELLPEADYVVNALPLTPETRGLFNAE
RFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEEEPLPADSPLWDLPNVIITPHISGDSP
SYPERVVEIFLENLRRYLAGEPLLNVVDKDRGY
>gnl|CDD|240626 cd05301, GDH, D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH). D-glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase, HPR) catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. In humans, HPR deficiency causes primary hyperoxaluria type 2, characterized by over-excretion of L-glycerate and oxalate in the urine, possibly due to an imbalance in competition with L-lactate dehydrogenase, another formate dehydrogenase (FDH)-like enzyme. GDH, like FDH and other members of the D-specific hydroxyacid dehydrogenase family that also includes L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase, typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form, despite often low sequence identity. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
PKVLVTRRLPEEALALLREGFEVEVWDEDRPLPREELLEAAKGADGLLCTLTDKIDAELLDAAPPLKVIA
NYSVGYDHIDVDAAKARGIPVTNTPDVLTDATADLAFALLLAAARRVVEGDRFVRAGEWKGWSPTLLLGT
DLHGKTLGIVGMGRIGQAVARRAKGFGMKILYHNRSRKPEAEEELGARYVSLDELLAESDFVSLHCPLTP
ETRHLINAERLALMKPTAILINTARGGVVDEDALVEALKSGKIAGAGLDVFEPEPLPADHPLLTLPNVVL
LPHIGSATVETRTAMAELAADNLLAVLAG
>gnl|CDD|240627 cd05302, FDH, NAD-dependent Formate Dehydrogenase (FDH). NAD-dependent formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of a formate anion to carbon dioxide coupled with the reduction of NAD+ to NADH. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family have 2 highly similar subdomains of the alpha/beta form, with NAD binding occurring in the cleft between subdomains. NAD contacts are primarily to the Rossmann-fold NAD-binding domain which is inserted within the linear sequence of the more diverse flavodoxin-like catalytic subdomain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production from C1 compounds such as methanol, and in the stress responses of plants. NAD-dependent FDH is useful in cofactor regeneration in asymmetrical biocatalytic reduction processes, where FDH irreversibly oxidizes formate to carbon dioxide, while reducing the oxidized form of the cofactor to the reduced form
AKIVCVLYDDGEHGYKPPNLLGCVENELGLRKWLESQGHELVVTSDKDGPDSELEKHLPDADVVISTPFH
PAYMTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGH
EQAIEGGWNVADVVKRAYDLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHRLPEEVEKELGLTRHA
DLEDMVSKCDVVTINCPLHPETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDV
WFPQPAPKDHPWRTMPNNAMTPHISGTTLDAQARYAAGTKEILERFFEGEPFRPEYLIVQGGKLAGKG
>gnl|CDD|240628 cd05303, PGDH_2, Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains. Phosphoglycerate dehydrogenase (PGDH) catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDH comes in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence
MKILITDGIDEIAIEKLEEAGFEVDYEPLIAKEELLEKIKDYDVLIVRSRTKVTKEVIDAAKNLKIIARA
GVGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLGKWNKKKYKGIELRGK
TLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDEQAVELGVKTVSLEELLKNSDFISLHVPLTPETKHM
INKKELELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDVFENEPPPGSKLLELPNVSLTPHIGA
STKEAQERIGEELANKIIEFL
>gnl|CDD|240629 cd05304, Rubrum_tdh, Rubrum transdehydrogenase NAD-binding and catalytic domains. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain
MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEELAQADIV
LKVRPPSEEEVALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGY
KAVLEAANHLPRFFPMLMTAAGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGA
KFVEVDVEEDAEGAGGYAKELSEEFLAKQRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGS
VIVDLAAEQGGNCELTVPGETVVTNGVTIIGPTNLPSRLPTQASQLYAKNLLNFLELLVKDDGELTLDLE
DEIVRGTLVTHDG
>gnl|CDD|240630 cd05305, L-AlaDH, Alanine dehydrogenase NAD-binding and catalytic domains. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms
MKIGIPKEIKNQENRVALTPAGVAELVAAGHEVLVEKGAGLGSGFSDEEYSEAGAEIVPTAEEVWAKADL
IVKVKEPLPEEYDLLREGQILFTYLHLAADKELTEALLEKKVTAIAYETIEDEDGSLPLLAPMSEIAGRL
AVQIGAEYLEKPNGGRGVLLGGVPGVPPAKVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDI
FGGRVTTLYSNPANLEEALKEADLVIGAVLIPGAKAPKLVTEEMVKTMKPGSVIVDVAIDQGGCFETSRP
TTHDNPTYVVHGVIHYCVPNMPGAVPRTSTLALTNATLPYLLKLANKGLEEALLEDPGLAKGLNTYKGKL
TNKAVAEAF
>gnl|CDD|133453 cd05311, NAD_bind_2_malic_enz, NAD(P) binding domain of malic enzyme (ME), subgroup 2. Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists primarily of archaeal and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts
QHGTAIVTLAGLLNALKLVGKKIEEVKIVINGAGAAGIAIARLLLAAGAKPENIVVVDSKGVIYEGREDD
LNPDKNEIAKETNPEKTGGTLKEALKGADVFIGVSRPGVVKKEMIKKMAKDPIVFALANPVPEIWPEEAK
EAGADIVATGRSDFPNQVNNVLGFPGIFRGALDVRATKITEEMKLAAAEAIADLAEEEVLGEEYIIPTPF
DPRVVPRVATAVAKAA
>gnl|CDD|133454 cd05312, NAD_bind_1_malic_enz, NAD(P) binding domain of malic enzyme (ME), subgroup 1. Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists of eukaryotic and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts
IQGTAAVALAGLLAALRITGKPLSDQRILFLGAGSAGIGIADLIVSAMVREGLSEEEARKKIWLVDSKGL
LTKDRKDLTPFKKPFARKDEEKEGKSLLEVVKAVKPTVLIGLSGVGGAFTEEVVRAMAKSNERPIIFALS
NPTSKAECTAEDAYKWTDGRALFASGSPFPPVEYNGKTYVPGQGNNAYIFPGIGLGAILSGARHITDEMF
LAAAEALASLVTDEELARGRLYPPLSNIREISAQIAVAVAKYAYEEGLATRYPPPEDLEEYVKSQMWEP
>gnl|CDD|133455 cd05313, NAD_bind_2_Glu_DH, NAD(P) binding domain of glutamate dehydrogenase, subgroup 2. Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. Glutamate DH is a multidomain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia asimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha -beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts
TGKGLSWGGSLIRPEATGYGLVYFVEEMLKDRNETLKGKRVAISGSGNVAQYAAEKLLELGAKVVTLSDS
KGYVYDPDGFTGEKLAELKEIKEVRRGRVSEYAKKYGTAKYFEGKKPWEVPCDIAFPCATQNEVDAEDAK
LLVKNGCKYVAEGANMPCTAEAIEVFRQAGVLFAPGKAANAGGVAVSGLEMSQNSQRLSWTAEEVDAKLK
DIMKNIHDACAETAKKYGDPPDLVAGANIAGFLKVADAMLAQGV
>gnl|CDD|187583 cd05322, SDH_SDR_c_like, Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs. Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADATNEQSVIAL
SKGVDEIFKRVDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIQGRIIQINS
KSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLGNLLKSPMFQSLLPQYAKKLGIKESEV
EQYYIDKVPLKRGCDYQDVLNMLLFYASPKASYCTGQSINITGGQVM
>gnl|CDD|187584 cd05323, ADH_SDR_c_like, insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs. This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKK
AIEKFGRVDILINNAGILDEKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIG
SVAGLYPAPQFPVYSASKHGVVGFTRSLADLLEYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLPSAPTQ
SPEVVAKAIVYLIEDDEKNGAIWIVDGGKLIEIE
>gnl|CDD|187585 cd05324, carb_red_PTCR-like_SDR_c, Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs. PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAAD
FVEEKYGGLDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGL
GSLTSAYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGGKAPKTPEEGAETPVYLALLPPDG
EPTGKFFSDKKVVPW
>gnl|CDD|187586 cd05325, carb_red_sniffer_like_SDR_c, carbonyl reductase sniffer-like, classical (c) SDRs. Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
VLITGASRGIGLELVRQLLARGNNTVIATCRDPSAATELAALGASHSRLHILELDVTDEIAESAEAVAER
LGDAGLDVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSI
GDNTSGGWYSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAKNKGPITPEESVAGLLK
VIDNLNEEDSGKFLDYDGTEIPW
>gnl|CDD|187587 cd05326, secoisolariciresinol-DH_like_SDR_c, secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs. Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
RLDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVHCDVTVEADVRAAV
DTAVARFGRLDIMFNNAGVLGAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVAS
VAGVVGGLGPHAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGVEDEAIEEAVRGAA
NLKGTALRPEDIAAAVLYLASDDSRYVSGQNLVVDGGLT
>gnl|CDD|212492 cd05327, retinol-DH_like_SDR_c_like, retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs. Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13, and -14, dehydrogenase/reductase SDR family member (DHRS)-12, -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNAKVEVIQLDLSSLASVRQF
AEEFLARFPRLDILINNAGIMAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAH
RAGPIDFNDLDLENNKEYSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSFFL
LYKLLRPFLKKSPEQGAQTALYAATSPELEGVSGKYFSDCKIKMSSSEALDEELAEKLW
>gnl|CDD|187589 cd05328, 3alpha_HSD_SDR_c, alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs. Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
TIVITGAASGIGAATAELLEDAGHTVIGIDLREADVIADLSTPEGRAAAIADVLARCSGVLDGLVNCAGV
GGTTVAGLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGWAQDKLELAKALAAGTEARAVALA
EHAGQPGYLAYAGSKEALTVWTRRRAATWLYGAGVRVNTVAPGPVETPILQAFLQDPRGGESVDAFVTPM
GRRAEPDEIAPVIAFLASDAASWINGANLFVDGGLDASMR
>gnl|CDD|187590 cd05329, TR_SDR_c, tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs. This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
RWNLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSER
QELMDTVASHFGGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVF
ISSVAGVIAVPSGAPYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLDKVIER
TPLKRFGEPEEVAALVAFLCMPAASYITGQIIAVDGGLTAN
>gnl|CDD|187591 cd05330, cyclohexanol_reductase_SDR_c, cyclohexanol reductases, including levodione reductase, classical (c) SDRs. Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPDAEVLLIKADVSDEAQVE
AYVDATVEQFGRIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNT
ASVGGIRGVGNQSGYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSLKQLGPENPEEAGE
EFVSVNPMKRFGEPEEVAAVVAFLLSDDAGYVNAAVVPIDGGQSYKY
>gnl|CDD|187592 cd05331, DH-DHB-DH_SDR_c, 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs. 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPID
ALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAY
GASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQRTLWHDEDGAAQVIAGVPEQFRLGIPLGKIAQ
PADIANAVLFLASDQAGHITMHDLVVDGGATLGA
>gnl|CDD|187593 cd05332, 11beta-HSD1_like_SDR_c, 11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs. Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDMSDLEDAEQ
VVEEALKLFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSS
IAGKIGVPFRTAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGDGSMSAKMDDTTA
NGMSPEECALEILKAIALRKREVFYARQVPLLAVYLRQLFPGLFDWL
>gnl|CDD|187594 cd05333, BKR_SDR_c, beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs. This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEK
VEAEFGPVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGL
IGNPGQANYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTP
EEVANAVAFLASDDASYITGQVLHVNGGMY
>gnl|CDD|187595 cd05334, DHPR_SDR_c_like, dihydropteridine reductase (DHPR), classical (c) SDRs. Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAENEEADASIIVLDSDSFTEQAKQVVASVARLSGKVD
ALICVAGGWAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLSGGLLVLTGAKAALEPTPGMIGYG
AAKAAVHQLTQSLAAENSGLPAGSTANAILPVTLDTPANRKAMPDADFSSWTPLEFIAELILFWASGAAR
PKSGSLIPVVT
>gnl|CDD|187596 cd05337, BKR_1_SDR_c, putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR. This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
RPVAIVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALL
DQAWEDFGRLDCLVNNAGIAVRPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRFDGPHRS
IIFVTSINAYLVSPNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDELIAA
GLVPIRRWGQPEDIAKAVRTLASGLLPYSTGQPINIDGGLSMRRL
>gnl|CDD|187597 cd05338, DHRS1_HSDL2-like_SDR_c, human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs. This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver, a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDNGSAKSLPGTIEETAEEIEAAGGQALPIV
VDVRDEDQVRALVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVK
AGQGHILNISPPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIETPAATELSGGS
DPARARSPEILSDAVLAILSRPAAERTGLVVIDEEL
>gnl|CDD|187598 cd05339, 17beta-HSDXI-like_SDR_c, human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs. 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKI
KKEVGDVTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLI
SPAGLADYCASKAAAVGFHESLRLELKAYGKPGIKTTLVCPYFINTGMFQGVKTPRPLLAPILEPEYVAE
KIVRAILTNQQMLYLPFYAYFLPILKRTLPTPV
>gnl|CDD|187599 cd05340, Ycik_SDR_c, Escherichia coli K-12 YCIK-like, classical (c) SDRs. Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
LLNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFILDLLTCTSEN
CQQLAQRIAVNYPRLDGVLHNAGLLGDVCPLSEQNPQVWQDVXQVNVNATFMLTQALLPLLLKSDAGSLV
FTSSSVGRQGRANWGAYAVSKFATEGLXQVLADEYQQRNLRVNCINPGGTRTAMRASAFPTEDPQKLKTP
ADIMPLYLWLMGDDSRRKTGMTFDAQ
>gnl|CDD|187600 cd05341, 3beta-17beta-HSD_like_SDR_c, 3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs. This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
NRLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVV
DTAREAFGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIE
GLVGDPALAAYNASKGAVRGLTKSAALECATQGYGIRVNSVHPGYIYTPMTDELLIAQGEMGNYPNTPMG
RAGEPDEIAYAVVYLASDESSFVTGSELVVDGGYTAG
>gnl|CDD|187601 cd05343, Mgc4172-like_SDR_c, human Mgc4172-like, classical (c) SDRs. Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
MERWRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFPYQCDLSNEEQ
ILSMFSAIRTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVDDGHI
ININSMSGHRVPPVSVFHFYAATKHAVTALTEGLRQELREAKTHIRATSISPGLVETEFAFKLHDNDPEK
AAATYESIPCLKPEDVANAVLYVLSTPPHVQIHDILLRPT
>gnl|CDD|187602 cd05344, BKR_like_SDR_like, putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR. This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVE
KAGDAFGRVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTV
KEPEPNLVLSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTERVRRLLEARAEKEGISVEEAEKEV
ASQIPLGRVGKPEELAALIAFLASEKASYITGQAILVDGGLTR
>gnl|CDD|187603 cd05345, BKR_3_SDR_c, putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR. This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMV
EAALSKFGRLDILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIAST
AGLRPRPGLTWYNASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMGEDTPENRAKFRATIP
LGRLSTPDDIANAALYLASDEASFITGVALEVDGGRCI
>gnl|CDD|187604 cd05346, SDR_c5, classical (c) SDR, subgroup 5. These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRESIEAALE
NLPEEFRDIDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIA
GRYPYAGGNVYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSLVRFHGDKEKADKVYEGVEPL
TPEDIAETILWVASRPAHVNINDIEIMPVNQASAGHIHR
>gnl|CDD|187605 cd05347, Ga5DH-like_SDR_c, gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs. Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
FSLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIK
AAVEAIEEDFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINIC
SLLSELGGPPVPAYAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVADPEFNDDILKRIP
AGRWGQPEDLVGAAVFLASDASDYVNGQIIFVDGGWLA
>gnl|CDD|187606 cd05348, BphB-like_SDR_c, cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs. cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
WLKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVA
RCVERFGKLDCFIGNAGIWDYSTSLVDIPEEKLDEAFDELFHINVKGYILGAKAALPALYATEGSVIFTV
SNAGFYPGGGGPLYTASKHAVVGLVKQLAYELAPHIRVNGVAPGGMVTDLRGPASLGQGETSISTPPLDD
MLKSILPLGFAPEPEDYTGAYVFLASRGDNRPATGTVINYDGGMGVR
>gnl|CDD|187607 cd05349, BKR_2_SDR_c, putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR. This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAK
NHFGPVDTIVNNALIDFPFDPDQRKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGT
NLFQNPVVPYHDYTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDASAATPKEVFDAIAQTTPLG
KVTTPQDIADAVLFFASPWARAVTGQNLVVDGGLVM
>gnl|CDD|187608 cd05350, SDR_c6, classical (c) SDR, subgroup 6. These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELE
AELGGLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRG
LPGAAAYSASKAALSSLAESLRYDVKKRGIRVTVINPGFIDTPLTANMFTMPFLMSVEQAAKRIYKAIKK
GAAEPTFPWRLAVPLRLLKLLPERLRRRL
>gnl|CDD|187609 cd05351, XR_like_SDR_c, xylulose reductase-like, classical (c) SDRs. Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser)
MELDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPGIEPVCVDLSDWDATEEA
LGSVGPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVPGSIVNVSSQASQ
RALTNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNWSDPEKAKKMLNRIPLGKFA
EVEDVVNAILFLLSDKSSMTTGSTLPVDGGFLAS
>gnl|CDD|187610 cd05352, MDH-like_SDR_c, mannitol dehydrogenase (MDH)-like, classical (c) SDRs. NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser)
LDLFSLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQ
ESVEKTFKQIQKDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSL
IITASMSGTIVNRPQPQAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWE
SYIPLKRIALPEELVGAYLYLASDASSYTTGSDLIIDGGYTC
>gnl|CDD|187611 cd05353, hydroxyacyl-CoA-like_DH_SDR_c-like, (3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs. Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGDRKGSGKSSSAADKVVDEIKAAGGKAVANYD
SVEDGEKIVKTAIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFG
RIINTSSAAGLYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPAAGSRMTETVMPEDLFDALK
PEYVAPLVLYLCHESCEVTGGLFEVGAGWIGKLRWERSGG
>gnl|CDD|187612 cd05354, SDR_c7, classical (c) SDR, subgroup 7. These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
IKDKTVLVTGANRGIGKAFVESLLAHGAKKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAA
QAKDVDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKN
FPAMGTYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAGGPKESPETVAEAVLKALKAGE
FHVFPDEMAKQVKEAYQSFPKNVVA
>gnl|CDD|187613 cd05355, SDR_c1, classical (c) SDR, subgroup 1. These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
PGIEAKMDPLPDFGEKSYKGSGKLKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAEETKK
LIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFGKLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFS
MFYLTKAALPHLKKGSSIINTTSVTAYKGSPHLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIW
TPLIPSSFPEEKVSEFGSQVPMGRAGQPAEVAPAYVFLASQDSSYVTGQVLHVNGGEIIN
>gnl|CDD|187614 cd05356, 17beta-HSD1_like_SDR_c, 17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs. This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSAGDDIYERI
EKELEGLDIGILVNNVGISHSIPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSF
AGLIPTPLLATYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLFVPSPEQFVRSAL
NTLGLSKRTTGYWSHALQGWVARLVPEWI
>gnl|CDD|187615 cd05357, PR_SDR_c, pteridine reductase (PR), classical (c) SDRs. Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVA
AAFRAFGRCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMT
DRPLTGYFAYCMSKAALEGLTRSAALELAPNIRVNGIAPGLILLPEDMDAEYRENALRKVPLKRRPSAEE
IADAVIFLLDSNYITGQIIKVDGG
>gnl|CDD|187616 cd05358, GlcDH_SDR_c, glucose 1 dehydrogenase (GlcDH), classical (c) SDRs. GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVA
LFQSAIKEFGTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIKGKIINMS
SVHEKIPWPGHVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRADLLSLIP
MGRIGEPEEIAAAAAWLASDEASYVTGTTLFVDGGMTLYPSFQ
>gnl|CDD|187617 cd05359, ChcA_like_SDR_c, 1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs. This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAV
KERFGRLDVLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIR
ALPNYLAVGTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDALAHFPNREDLLEAAAANTPAGRVGT
PQDVADAVGFLCSDAARMITGQTLVVDGGLSI
>gnl|CDD|187618 cd05360, SDR_c3, classical (c) SDR, subgroup 3. These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
QVVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADT
AVERFGRIDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGY
RSAPLQAAYSASKHAVRGFTESLRAELAHDGAPISVTLVQPTAMNTPFFGHARSYMGKKPKPPPPIYQPE
RVAEAIVRAAEHPRREVKVGDPA
>gnl|CDD|187619 cd05361, haloalcohol_DH_SDR_c-like, haloalcohol dehalogenase, classical (c) SDRs. Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
MSIALVTHARHFAGPASAEALTEDGYTVVCHDASFADAAERQAFESENPGTKALSEQKPEELVDAVLQAG
GAIDVLVSNDYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLA
YNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSPTYFPTSDWENNPELRERVKRDVPLGRLGR
PDEMGALVAFLASRRADPITGQFFAFAGGYLP
>gnl|CDD|187620 cd05362, THN_reductase-like_SDR_c, tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs. 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVAR
LFDAAEKAFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDGGRIINISSSL
TAAYTPNYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAVEGYAKMSPLGRL
GEPEDIAPVVAFLASPDGRWVNGQVIRANGGYV
>gnl|CDD|187621 cd05363, SDH_SDR_c, Sorbitol dehydrogenase (SDH), classical (c) SDR. This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAA
LVDRWGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRGGKIINMASQAG
RRGEALVGVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGVDAKFARYENRPRGEKKRLV
GEAVPFGRMGRAEDLTGMAIFLASTDADYIVAQTYNVDGGNWMS
>gnl|CDD|187622 cd05364, SDR_c11, classical (c) SDR, subgroup 11. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEKKILLVVADLTEEEGQ
DRIISTTLAKFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVS
SVAGGRSFPGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMGMPEEQYIKFLSRAK
ETHPLGRPGTVDEVAEAIAFLASDASSFITGQLLPVDGGRHLM
>gnl|CDD|187623 cd05365, 7_alpha_HSDH_SDR_c, 7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs. This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKAT
VSQFGGITILVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSE
NKNVRIAAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASVLTPEIERAMLKHTPLGRLGE
PEDIANAALFLCSPASAWVSGQVLTVSGGGVQ
>gnl|CDD|187624 cd05366, meso-BDH-like_SDR_c, meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs. 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAGYNAVAVGADVTDKDDVEAL
IDQAVEKFGSFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHGGKIINASS
IAGVQGFPNLGAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGEIAGKPEGEGF
AEFSSSIPLGRLSEPEDVAGLVSFLASEDSDYITGQTILVDGGMVYR
>gnl|CDD|187625 cd05367, SPR-like_SDR_c, sepiapterin reductase (SPR)-like, classical (c) SDRs. Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
VIILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQELKEELRPGLRVTTVKADLSDAAGVEQLLEA
IRKLDGERDLLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLKKTVVNVSSGA
AVNPFKGWGLYCSSKAARDMFFRVLAAEEPDVRVLSYAPGVVDTDMQREIRETSADPETRSRFRSLKEKG
ELLDPEQSAEKLANLLEKDKFESGAHVDYYD
>gnl|CDD|187626 cd05368, DHRS6_like_SDR_c, human DHRS6-like, classical (c) SDRs. Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P)
DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERGPGITTRVLDVTDKEQVAALAKEEGR
IDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVPNR
FVYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEALKAFAARQPLGRLATP
EEVAALAVYLASDESAYVTGTAVVIDGGWSL
>gnl|CDD|187627 cd05369, TER_DECR_SDR_a, Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR. TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIQCDVRDPEAVEA
AVDETLKEFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGGSILNIS
ATYAYTGSPFQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKKMIERV
PLGRLGTPEEIANLALFLLSDAASYINGTTLVVDGGQWL
>gnl|CDD|187628 cd05370, SDR_c2, classical (c) SDR, subgroup 2. Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
MKLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPNIHTIVLDVGDAESVEALAE
ALLSEYPNLDILINNAGIQRPIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSG
LAFVPMAANPVYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGGTPRKMPLDEFV
DEVVAGLERGREEIRVGM
>gnl|CDD|187629 cd05371, HSD10-like_SDR_c, 17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs. HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKLGDNCRFVPVDVTSEKDVKAALALAK
AKFGRLDIVVNCAGIAVAAKTYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPDQGGERGV
IINTASVAAFEGQIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAK
QVPFPSRLGDPAEYAHLVQHIIENPYLNGEVIRLDGAIRMPP
>gnl|CDD|187630 cd05372, ENR_SDR, Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR. This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
GKRILITGIANDRSIAWGIAKALHEAGAELAFTYQPEALRKRVEKLAERLGESALVLPCDVSNDEEIKEL
FAEVKKDWGKLDGLVHSIAFAPKVQLKGPFLDTSRKGFLKALDISAYSLVSLAKAALPIMNPGGSIVTLS
YLGSERVVPGYNVMGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKTLAASGITGFDKMLEYSEQRAP
LGRNVTAEEVGNTAAFLLSDLSSGITGEIIYVDGGYHIMG
>gnl|CDD|187631 cd05373, SDR_c10, classical (c) SDR, subgroup 10. This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDL
IEEEIGPLEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASL
RGRAGFAAFAGAKFALRALAQSMARELGPKGIHVAHVIIDGGIDTDFIRERFPKRDERKEEDGILDPDAI
AEAYWQLHTQPRSAWTHELDLRPWVETF
>gnl|CDD|187632 cd05374, 17beta-HSD-like_SDR_c, 17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs. 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIE
RFGRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPT
PFLGPYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGSALEDPEISPYAPERKEIKEN
AAGVGSNPGDPEKVADVIVKALTSESPPLRYFLGSDAL
>gnl|CDD|349398 cd05379, CAP_bacterial, Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins. Little is known about bacterial and archaeal members of the CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Studies of eukaryotic proteins show that CAP domains have several functions, including the binding of cholesterol, lipids and heparan sulfate. This group includes Borrelia burgdorferi outer surface protein BB0689, which does not bind to cholesterol, lipids, or heparan sulfate, and whose function is unknown
EQEVLELINEYRAKAGLPPLSWDPRLEKAAQDHAEDMAANGYFSHTGPDGSSDRAARAGYWYRGAGENIA
YGQGSAEEAVNQWINSPGHRANILDPDFTEIGVGVAYNSSGGTYWTQVFG
>gnl|CDD|349399 cd05380, CAP_euk, Eukaryotic CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins. The CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain is found mainly in eukaryotes. This family includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), and allergen 5 from vespid venom
RQEILDAHNELRSKVAKGKLKGLPPAANMPKLKWDCELAKLAQNWAKTCVFAHSPCRNTGGVGQNLASVS
SSGKDLKELIEDAVNAWFDELKDYGFGSNPNNNFNSGIGHFTQMVWAKTTKVGCAVARCPKGGGNKTYVV
CNYS
>gnl|CDD|349400 cd05381, CAP_PR-1, CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of pathogenesis-related protein 1 (PR-1) family proteins. Members of pathogenesis-related protein 1 (PR-1) family are among the most abundantly produced proteins in plants on pathogen attack. They are considered hallmarks of hypersensitive response/defense pathways and may act as anti-fungal agents or be involved in cell wall loosening
PQDFLDAHNQARAAVGVPPLVWDDTLAAYAQKYANQRRGDCSLVHSNGPYGENLFWGSGDNWSPADAVKS
WVDEKPYYDYASNTCVGGKMCGHYTQVVWRNSTRLGCARVVCDNNGGTFVICNYDPPGNYIGERPY
>gnl|CDD|349401 cd05382, CAP_GAPR1-like, CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of Golgi-associated plant pathogenesis-related protein 1 and similar proteins. Golgi-associated plant pathogenesis related protein 1 (GAPR1), also called Golgi-associated PR-1 protein or glioma pathogenesis-related protein 2 (GLIPR-2), forms amyloid-like fibrils in the presence of liposomes containing acidic phospholipids. It has been identified in mice as an up-regulated protein in kidney fibrosis, and is involved in epithelial to mesenchymal transition and in generating a pool of myofibroblasts contributing to fibrosis. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others
VFQKECLKAHNEYRALHGAPPLKLDKELSKEAQKWAEKLASSGTLQHSSPSSYGENLAYFSGSGYDLTGE
EAVDSWYNEIKNYNFNKPGFQSGTGHFTQVVWKSSTELGVGVAKSKDGCVYVVARYSPAGNV
>gnl|CDD|349402 cd05383, CAP_CRISP, CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory proteins. Cysteine-rich secretory proteins (CRISPs) are two-domain proteins with an evolutionary diverse and structurally conserved N-terminal CAP domain and a C-terminal cysteine-rich domain, which is comprised of a hinge and an ICR (ion channel regulator) region. CRISPs are involved in response to pathogens, fertilization, and sperm maturation. One member, Tex31 from the venom duct of Conus textile, has been shown to possess proteolytic activity sensitive to serine protease inhibitors. CRISP-1 has been shown to mediate gamete fusion by binding to the egg surface. Other members of the CRISP family secreted in the testis (CRISP2), epididymis (CRISP3-4), or during ejaculation (CRISP3), are also involved in sperm-egg interaction, supporting the existence of a functional redundancy and cooperation between homolog proteins ensuring the success of fertilization. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1) and allergen 5 from vespid venom, among others
KVQQEIVDLHNALRRSVNPPASNMLKMSWNPEAAENAQRWANRCNFTHSPPNGRTIPGIRCGENIFMSSY
PASWSEVIQAWYDEYKDFKYGVGAKPPGSVTGHYTQVVWYSSYLVGCAVAYCPSQGSLKYFYVCQYCPA
>gnl|CDD|349403 cd05384, CAP_PRY1-like, CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of pathogen-related yeast 1 (PRY1) protein and similar fungal proteins. PRY1, also called pathogenesis-related protein 1, is a yeast protein that is up-regulated in core ESCRT mutants. It is a secreted protein required for efficient export of lipids such as acetylated sterols, and acts in detoxification of hydrophobic compounds. This PRY1-like group also contains fruiting body proteins SC7/14 from Schizophyllum commune. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others
SFASSILDAHNKKRALHGTQPLTWNDTLAEYAQDYADSYDCSGNLVHSGGPYGENLALGYSSGAAAVDAW
YDEISDYDYSNPGFSESTGHFTQLVWKSTTQVGCAYKDCGGAWGLYIVCEYDPAGNVIG
>gnl|CDD|349404 cd05385, CAP_GLIPR1-like, CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of glioma pathogenesis-related protein 1 and similar proteins. Glioma pathogenesis-related protein 1 (GLIPR1) is also called related to testes-specific, vespid, and pathogenesis protein 1 (RTVP-1). The GLIPR1 gene has been identified as a p53 target gene and was shown to be methylated and down-regulated in prostate cancer. It is a novel broad-spectrum tumor suppressor whose proapoptotic properties are exerted in part through ROS-JNK signaling. GLIPR1 is composed of a signal peptide that directs its secretion, a CAP domain, and a transmembrane domain. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others
AFIDECVRIHNELRSKVSPPAANMRYMSWDKALAKTARAWARKCKFSHNICLKEPGKCHPNFTTLGENIW
LGSIFSFSVESAITSWYNEVKDYNFKTNSCSRVCGHYTQVVWADSYKVGCAVHVCPNGGGFFSGSSSAIF
VCNYGPAG
>gnl|CDD|349771 cd05386, TraL, transfer origin protein TraL. The transfer origin protein TraL is member of the SIMIBI superfamily which contains a ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. The specific function of TraL protein is unknown
KIHFVLQGKGGVGKSVIASLLAQYLIDKGQPVSCIDTDPVNKTFAGYKALNVQRINIIDNDEIIQSKFDQ
LVEQFLAEDGTVVIDTGASTFLPLMNYLIDNDVPDLLKDMGKEVVIHTVINGGQALDDTINGLQTLLDQF
KDNAKVVVWLNEYFG
>gnl|CDD|349772 cd05387, BY-kinase, bacterial tyrosine-kinase. Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity
EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLP
NEPGLSEVLSGQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVL
AVADALILAPLVDGVLLVVRAGKTRRREVKEALERLEQAGAKVLGVVLNK
>gnl|CDD|349773 cd05388, CobB_N, N-terminal domain of cobyrinic acid a,c-diamide synthase. Cobyrinic acid a,c-diamide synthase (CobB, CbiA). Biosynthesis of cobalamin (vitamin B12) requires more than two dozen different enzymes. CobB catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinic acid, via the formation of a phosphorylated intermediate, using glutamine or ammonia as the nitrogen source. CobB is comprised of two protein domains: the C-terminal glutaminase domain and the N-terminal ATP-binding domain. The glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. It belongs to the triad class of glutamine amidotransferases. This classification is based on the N-terminal domain which catalyzes the ultimate synthesis of the diamide product by using energy from the hydrolysis of ATP and ammonia transferred from the C-terminal domain
PRIVIAGTSSGSGKTTITLGLMRALARRGLRVQPFKVGPDYIDPGFHEAATGRPSRNLDSWMMGEDGVRE
LFARAAGGADVAIIEGVMGLYDGRDTDSDEGSTAELARLLGAPVLLVLDCKGMARSAAAIVKGYKEFDPD
LNLAGVILNRVGSPRHAELLKEAIEEYTGIPVLGYLPRDDELTLPERHLGLVP
>gnl|CDD|349774 cd05389, CobQ_N, N-terminal domain of cobyric acid synthase. Cobyric acid synthase (CobQ, CbiP) N-terminal domain. CobQ plays a role in the cobalamin (vitamin B12) biosynthesis pathway. CobQ catalyzes the ATP-dependent amidation of adenosyl-cobyrinic acid a,c-diamide at carboxylates positions b, d, e, and g to produce cobyric acid using glutamine or ammonia as the nitrogen source. The C-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. Ammonia is translocated via an intramolecular tunnel to the N-terminal domain for the synthesis of cobyric acid
KSIMVQGTASDVGKSTLVAALCRILKRRGYRVAPFKAQNMSLNSFVTKDGGEIGRAQAVQAEAAGVEPSV
DMNPVLLKPKGDFKSQVIVMGKPIGDMDAREYYEYKGRLAPAVLESLDRLAAEYDLVVIEGAGSPAEINL
RDRDIVNMGMARAADAPVILVADIDRGGVFASLYGTLALLPEEERKLVKGVVINKFRGDRSLLEPGIEML
EERTGVPVLGVLP
>gnl|CDD|349775 cd05390, HypB, nickel incorporation protein HypB. HypB is one of numerous accessory proteins required for the maturation of nickel-dependent hydrogenases, like carbon monoxide dehydrogenase or urease. HypB is a GTP-binding protein and has GTP hyrolase activity. It forms homodimer and is capable of binding two nickel ions and two zinc ions. The active site is located on the dimer interface. Energy from hydrolysis of GTP is used to insert nickels into hydrogenases
ILDKNDRLADENREHFEEHGVLALNLMSSPGSGKTTLLERTIDALKDELKIAVIEGDLETDNDAERIRAT
GVPAIQINTGGACHLDADMVARALHDLDLDELDLLFIENVGNLVCPAEFDLGEHKNVVLLSVTEGDDKPL
KYPLMFQVADVVLINKIDLLPYFDFDVEKAKEDIKKLNPNAPIIEVSAKTGEGMEAWIDWLRE
>gnl|CDD|213340 cd05391, RasGAP_p120GAP, Ras-GTPase Activating Domain of p120. p120GAP is a negative regulator of Ras that stimulates hydrolysis of bound GTP to GDP. Once the Ras regulator p120GAP, a member of the GAP protein family, is recruited to the membrane, it is transiently immobilized to interact with Ras-GTP. The down-regulation of Ras by p120GAP is a critical step in the regulation of many cellular processes, which is disrupted in approximately 30% of human cancers. p120GAP contains SH2, SH3, PH, calcium- and lipid-binding domains, suggesting its involvement in a complex network of cellular interactions in vivo
MEKIMPEEEYSELKELILQKELHVVYALAHVCGQDRTLLASILLRIFRHEKLESLLLRTLNDREISMEDE
ATTLFRATTLASTLMEQYMKATATPFVHHALKDTILKILESKQSCELNPSKLEKNEDVNTNLEHLLNILS
ELVEKIFMAAEILPPTLRYIYGCLQKSVQQKWPTNTTVRTRVVSGFVFLRLICPAILNPRMFNIISETPS
PTAARTLTLVAKSLQNLANLVEFGAKEPYMEGVNPFIKKNKERMIMFLDELGNVPELPDTTEHSRTDLSR
DLAALHEICVAHSDELRTLSNERGALKKLLAVTELLQQKQNQYTQSNR
>gnl|CDD|213341 cd05392, RasGAP_Neurofibromin_like, Ras-GTPase Activating Domain of proteins similar to neurofibromin. Neurofibromin-like proteins include the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2, the closest homolog of neurofibromin, which is responsible for the human autosomal dominant disease neurofibromatosis type I (NF1). The RasGAP Ira1/2 proteins are negative regulators of the Ras-cAMP signaling pathway and conserved from yeast to human. In yeast Ras proteins are activated by GEFs, and inhibited by two GAPs, Ira1 and Ira2. Ras proteins activate the cAMP/protein kinase A (PKA) pathway, which controls metabolism, stress resistance, growth, and meiosis. Recent studies showed that the kelch proteins Gpb1 and Gpb2 inhibit Ras activity via association with Ira1 and Ira2. Gpb1/2 bind to a conserved C-terminal domain of Ira1/2, and loss of Gpb1/2 results in a destabilization of Ira1 and Ira2, leading to elevated levels of Ras2-GTP and uninhibited cAMP-PKA signaling. Since the Gpb1/2 binding domain on Ira1/2 is conserved in the human neurofibromin protein, the studies suggest that an analogous signaling mechanism may contribute to the neoplastic development of NF1
KKSEAYDELLELLIEDPQLLLAIAEVCPSSEVDLLAQSLLNLFETRNRLLPLISWLIEDEISHTSRAADL
FRRNSVATRLLTLYAKSVGNKYLRKVLRPLLTEIVDNKDYFEVEKIKPDDENLEENADLLMKYAQMLLDS
ITDSVDQLPPSFRYICNTIYESVSKKFPDAALIAVGGFLFLRFICPAIVSPESENLLDPPPTPEARRSLI
LIAKVLQNIANGVLFSLKEPYLESLNEFLKKNSDRIQQFLSEVSTIPPTDPIFDESDEEPITADLRYLHK
FLYLHFLEIRKEVLKGSSSQGSDKELVETFKLIDEIL
>gnl|CDD|213342 cd05394, RasGAP_RASA2, Ras-GTPase Activating Domain of RASA2. RASA2 (or GAP1(m)) is a member of the GAP1 family of Ras GTPase-activating proteins that includes GAP1_IP4BP (or RASA3), CAPRI, and RASAL. In vitro, RASA2 has been shown to bind inositol 1,3,4,5-tetrakisphosphate (IP4), the water soluble inositol head group of the lipid second messenger phosphatidylinositol 3,4,5-trisphosphate (PIP3). In vivo studies also demonstrated that RASA2 binds PIP3, and it is recruited to the plasma membrane following agonist stimulation of PI 3-kinase. Furthermore, the membrane translocation is a consequence of the ability of its pleckstrin homology (PH) domain to bind PIP3
SACYTSLRNLLLKSPDVKPISASAAHILGEICRDKYDAVLPLVRLLLHHNKLVPFVAAVAALDLKDTQEA
NTIFRGNSLATRCLDEMMKIVGKHYLKVTLKPVLDEICESPKPCEIDPIKLKEGDNVENNKENLRYYVDK
VFFSIVKSSMSCPTLMCDVFRSLRHLAVKRFPNDPHVQYSAVSSFVFLRFFAVAVVSPHTFQLRPHHPDA
QTSRTLTLISKTIQTLGSWGSLSKSKLSSFKETFMCDFFKMFQEEKYIEKVKKFLDEISSTE
>gnl|CDD|213343 cd05395, RasGAP_RASA4, Ras-GTPase Activating Domain of RASA4. Ras GTPase activating-like 4 protein (RASAL4), also known as Ca2+ -promoted Ras inactivator (CAPRI), is a member of the GAP1 family. Members of the GAP1 family are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL4, like RASAL, is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to a receptor-mediated elevation in the concentration of intracellular free Ca2+ ([Ca2+]i). However, unlike RASAL, RASAL4 does not sense oscillations in [Ca2+]i
PSSHYQPLVQLLCQEVKLGHQAGPVQLISLIDETTTAECRQEVATNLVKLFLGQGLAKEFLDLLFQLELD
KTTEPNTLFRSNSLASKSMESFLKVAGMQYLHSVLGPTINRVFEEKKYVELDPSKVEIKDVGCSGLHRIQ
TESEVIEQSAQLLQSYLGELLSAISKSVKYCPAVIRATFRQLFKRVQERFPENQHQNVKFIAVTSFLCLR
FFSPAIMSPKLFHLREKHADARTSRTLLLLAKAVQNVGNMDTLASRAKEAWMAPLQPAIQQGVAQLKDFI
TKLVDIE
>gnl|CDD|188647 cd05396, An_peroxidase_like, Animal heme peroxidases and related proteins. A diverse family of enzymes, which includes prostaglandin G/H synthase, thyroid peroxidase, myeloperoxidase, linoleate diol synthase, lactoperoxidase, peroxinectin, peroxidasin, and others. Despite its name, this family is not restricted to metazoans: members are found in fungi, plants, and bacteria as well
QLNARTPYLDGSSIYGSNPDVARALRTFKGGLLKTNEVKGPSYGTELLPFNNPNPSMGTIGLPPTRCFIA
GDPRVNENLLLLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFT
DPRDDLVLLFPDPDVVPYVLSEFFTAAYRFGHSLVPEGVDRIDENGQPKEIPDVPLKDFFFNTSRSILSD
TGLDPLLRGFLRQPAGLIDQNVDDVMFLFGPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSF
QDILTDPELAKKLAELYGDPDDVDLWVGGLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFG
KSGKEELEKLISLADIICLN
>gnl|CDD|143387 cd05397, NT_Pol-beta-like, Nucleotidyltransferase (NT) domain of DNA polymerase beta and similar proteins. This superfamily includes the NT domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of Class I and Class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, and Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. The Escherichia coli CCA-adding enzyme belongs to this superfamily but is not included as this enzyme lacks the N-terminal helix conserved in the remainder of the superfamily. In the majority of the Pol beta-like superfamily NTs, two carboxylates, Dx[D/E], together with a third more distal carboxylate coordinate two divalent metal cations that are essential for catalysis. These divalent metal ions are involved in a two-metal ion mechanism of nucleotide addition. Two of the three catalytic carboxylates are found in Rel-Spo enzymes, with the second carboxylate of the DXD motif missing. Evidence supports a single-cation synthetase mechanism for Rel-Spo enzymes
EELLDIIKERLKKLVPGYEIVVYGSLVRGLLKKSSDIDLACVRVDIRDW
>gnl|CDD|143388 cd05398, NT_ClassII-CCAase, Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes. CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This Class II group is comprised mainly of eubacterial and eukaryotic enzymes and includes Bacillus stearothermophilus CCAase, Escherichia coli poly(A) polymerase I, human mitochondrial CCAase, and Saccharomyces cerevisiae CCAase (CCA1). CCA-adding enzymes have a single catalytic pocket, which recognizes both ATP and CTP substrates. Included in this subgroup are CC- and A-adding enzymes from various ancient species of bacteria such as Aquifex aeolicus; these enzymes collaborate to add CCA to tRNAs. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are fairly well conserved in this family. Escherichia coli CCAase is related to this group but has not been included in this alignment as this enzyme lacks the N-terminal helix conserved in the remainder of the NT superfamily
TPELLKLLRELKKALGYEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAEALFKKIGGRVVGLGEEFGT
ATVVINGLTIDVATLRTETYTDPGRRPPVVGFTIEEDLLRRDFTINAMAYDLDDGELIDPFGGLKDLEN
>gnl|CDD|143389 cd05399, NT_Rel-Spo_like, Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases. This family includes the catalytic domains of Escherichia coli ppGpp synthetase (RelA), ppGpp synthetase/hydrolase (SpoT), and related proteins. RelA synthesizes (p)ppGpp in response to amino-acid starvation and in association with ribosomes. (p)ppGpp triggers the bacterial stringent response. SpoT catalyzes (p)ppGpp synthesis under carbon limitation in a ribosome-independent manner. It also catalyzes (p)ppGpp degradation. Gram-negative bacteria have two enzymes involved in (p)ppGpp metabolism while most Gram-positive organisms have a single Rel-Spo enzyme (Rel), which both synthesizes and degrades (p)ppGpp. The Arabidopsis thaliana Rel-Spo proteins, At-RSH1,-2, and-3 appear to regulate a rapid (p)ppGpp-mediated response to pathogens and other stresses. This catalytic domain is found in association with an N-terminal HD domain and a C-terminal metal dependent phosphohydrolase domain (TGS). Some Rel-Spo proteins also have a C-terminal regulatory ACT domain. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition.Two of the three catalytic carboxylates are found in Rel-Spo enzymes, with the second carboxylate of the DXD motif missing. Evidence supports a single-cation synthetase mechanism
KAALEEIADLLRDAGIIGRVASVSGRVKSPYSIYEKLRRKGKDLPILDEITDLVGVRVVLLFVDDCYRVL
DLLHSLFKVIPGRVKDYIAEPKENGYQSLHLVVRGPEDKAGVLIEIQIRTILMHAWAEL
>gnl|CDD|143390 cd05400, NT_2-5OAS_ClassI-CCAase, Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I CCA-adding enzyme. In vertebrates, 2-5OASs are induced by interferon during the innate immune response to protect against RNA virus infections. In the presence of an RNA activator, 2-5OASs catalyze the oligomerization of ATP into 2-5A. 2-5A activates endoribonuclease L, which leads to degradation of the viral RNA. 2-5OASs are also implicated in cell growth control, differentiation, and apoptosis. This family includes human OAS1, -2, -3, and OASL. CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This class I group includes the archaeal Sulfolobus shibatae and Archeoglobus fulgidus CCA-adding enzymes. It belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this family
PLEEAKERYREIREALKESLSELAGRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSFAEYGPAELLD
ELGEALKEYYGANEEVKAQHRSVTVKFKGQGFHVDVVPAFEADSGSKYGSVPDRDGGSWVDRNPKHHAEL
LRR
>gnl|CDD|143391 cd05401, NT_GlnE_GlnD_like, Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), and similar proteins. Escherichia coli GlnD and -E participate in the Glutamine synthetase (GS)/Glutamate synthase (GOGAT) pathway for the assimilation of ammonium nitrogen. In nitrogen sufficiency, GlnE adenylates GS, reducing GS activity; when nitrogen is limiting, GlnE deadenylates GS-AMP, restoring GS activity. When nitrogen is limiting, GlnD uridylylates the nitrogen regulatory protein PII to PII-UTP, and in nitrogen sufficiency, it removes the modifying groups. The activity of Escherichia coli GlnE is modulated by PII-proteins. PII-UMP promotes GlnE deadenylation activity, and PII promotes GlnE adenylation activity. Escherichia coli GlnE has two separate NT domains. The N-terminal NT domain catalyzes the deadenylylation of GS, and the C-terminal NT domain the adenylylation reaction. The majority of proteins in this family contain a C-terminal NT domain which is associated with a cystathionine beta-synthase (CBS) domain pair and a CAP_ED (cAMP receptor protein effector) domain. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved
RAKLRQLRRILRRDLLGGASIRAISRALSDLADALLRRALELALAELGKGPPPVPFALLALGSYGRGELN
PSSDQDLLLLYDDDGDEVAAYFEELAERLIKILSEAGGPYCLGDVMLRPPGWRRSLAEWLDAARDWLTEP
GRLWERTALLDARPVAGDRALAEELRRRIRER
>gnl|CDD|143392 cd05402, NT_PAP_TUTase, Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases. Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved
KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPNHRVDREDFLRKLAKLLKKSGEVV
EVEPIINARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV
>gnl|CDD|143393 cd05403, NT_KNTase_like, Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. S. aureus KNTase is a plasmid encoded enzyme which confers resistance to a wide range of aminoglycoside antibiotics which have a 4'- or 4''-hydroxyl group in the equatorial position, such as kanamycin A. This enzyme transfers a nucleoside monophosphate group from a nucleotide (ATP,GTP, or UTP) to the 4'-hydroxyl group of kanamycin A. This enzyme is a homodimer, having two NT active sites. The nucleotide and antibiotic binding sites of each active site include residues from each monomer. Included in this subgroup is Escherichia coli AadA5 which confers resistance to the antibiotic spectinomycin and is a putative aminoglycoside-3'-adenylyltransferase. It is part of the aadA5 cassette of a class 1 integron. This subgroup also includes Haemophilus influenzae HI0073 which forms a 2:2 heterotetramer with an unrelated protein HI0074. Structurally HI0074 is related to the substrate-binding domain of S. aureus KNTase. The genes encoding HI0073 and HI0074 form an operon. Little is known about the substrate specificity or function of two-component NTs. The characterized members of this subgroup may not be representive of the function of this subgroup. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, co-ordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this subgroup
EEILEEILEILRELLGGVEKVYLFGSYARGDARPDSDIDLLVIFDDPLDPLELARLLEELELLLGRPVDL
VVLNALELELLLRILIEGEGIYL
>gnl|CDD|176102 cd05466, PBP2_LTTR_substrate, The substrate binding domain of LysR-type transcriptional regulators (LTTRs), a member of the type 2 periplasmic binding fold protein superfamily. This model and hierarchy represent the the substrate-binding domain of the LysR-type transcriptional regulators that form the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, oxidative stress responses, nodule formation of nitrogen-fixing bacteria, synthesis of virulence factors, toxin production, attachment and secretion, to name a few. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate-binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLRIGASPSIAAYLLPPLLAAFRQRYPGVELSLVEGGSSELLEALLEGELDLAIVALPVDDPGLESEPLF
EEPLVLVVPPDHPLAKRKSVTLADLADEPLILFERGSGLRRLLDRAFAEAGFTPNIALEVDSLEAIKALV
AAGLGIALLPESAVEELADGGLVVLPLEDPPLSRTIGLVWRKGRYLSPAARAFLELL
>gnl|CDD|119437 cd05467, CBM20, The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
QVRFQVRCTTQFGQSVYVVGSHPELGNWDPAKALRLNTSNSYPLWTGEIPLPAPEGQVIEYKYVIVDDDG
NVQWESGSNRVLTVPSTSSLIVVDDW
>gnl|CDD|176472 cd05468, pVHL, von Hippel-Landau (pVHL) tumor suppressor protein. von Hippel-Landau (pVHL) protein, the gene product of VHL, is a critical regulator of the ubiquitous oxygen-sensing pathway. It is conserved throughout evolution, as its homologs are found in organisms ranging from mammals to the Drosophila melanogaster, Anopheles gambiae insects and the Caenorhabditis elegans nematode. pVHL acts as the substrate recognition component of an E3 ubiquitin ligase complex. Several proteins have been identified as pVHL-binding proteins that are subject to ubiquitin-mediated proteolysis; the best characterized putative substrates are the alpha subunits of the hypoxia-inducible factor (HIF1alpha, HIF2alpha, and HIF3alpha). In addition to HIF degradation, pVHL has been implicated to be involved in HIF independent cellular processes. Germline VHL mutations cause renal cell carcinomas, hemangioblastomas and pheochromocytomas in humans. pVHL can bind to and direct the proper deposition of fibronectin and collagen IV within the extracellular matrix. It works to stabilize microtubules and foster the maintenance of primary cilium. It also has been reported to promote the stabilization and activation of p53 in a HIF-independent manner and, in neuronal cells, promote apoptosis by down-regulation of Jun-B
RSVNSRVPSTVRFVNRTDRPVELYWIDYDGKPVSYGTLQPGETVRQNTYVGHPWLFRDAETGEKLLVNRK
EVFVPSPWRVGRPIDGNGTLPVTSLDERCLQLVRSLVPEDVRGLEIRVPRSLYEDLDIEPTLPRDLQRLL
S
>gnl|CDD|100112 cd05469, Transthyretin_like, Transthyretin_like. This domain is present in the transthyretin-like protein (TLP) family which includes transthyretin (TTR) and a transthyretin-related protein called 5-hydroxyisourate hydrolase (HIUase). TTR and HIUase are homotetrameric proteins with each subunit consisting of eight beta-strands arranged in two sheets and a short alpha-helix. The central channel of the tetramer contains two independent binding sites, each located between a pair of subunits. TTR transports thyroid hormones and retinol in the blood serum of vertebrates while HIUase catalyzes the second step in a three-step ureide pathway. TTRs are highly conserved and found only in vertebrates while the HIUases are found in a wide range of bacterial, plant, fungal, slime mold and vertebrate organisms
CPLMVKVLDAVRGSPAANVAIKVFRKTADGSWEIFATGKTNEDGELHGLITEEEFXAGVYRVEFDTKSYW
KALGITPFHEYAEVVFTANDSGHRHYTIALLLSPFSYSTTAVV
>gnl|CDD|133137 cd05470, pepsin_retropepsin_like, Cellular and retroviral pepsin-like aspartate proteases. This family includes both cellular and retroviral pepsin-like aspartate proteases. The cellular pepsin and pepsin-like enzymes are twice as long as their retroviral counterparts. The cellular pepsin-like aspartic proteases are found in mammals, plants, fungi and bacteria. These well known and extensively characterized enzymes include pepsins, chymosin, rennin, cathepsins, and fungal aspartic proteases. Several have long been known to be medically (rennin, cathepsin D and E, pepsin) or commercially (chymosin) important. The eukaryotic pepsin-like proteases contain two domains possessing similar topological features. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except in the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The eukaryotic pepsin-like proteases have two active site ASP residues with each N- and C-terminal lobe contributing one residue. While the fungal and mammalian pepsins are bilobal proteins, retropepsins function as dimers and the monomer resembles structure of the N- or C-terminal domains of eukaryotic enzyme. The active site motif (Asp-Thr/Ser-Gly-Ser) is conserved between the retroviral and eukaryotic proteases and between the N-and C-terminal of eukaryotic pepsin-like proteases. The retropepsin-like family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements; as well as eukaryotic DNA-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. Retropepsin is synthesized as part of the POL polyprotein that contains an aspartyl-protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A) and A2 (retropepsin family)
IEIGIGTPPQTFNVLLDTGSSNLWVPSVDCQSLAIYSHSSYDDPSASSTYSDNGCTFSITYGTGSLSGGL
STDTVSIGDIEVVGQAFGCATDEPGATFLPALFDGILGL
>gnl|CDD|133138 cd05471, pepsin_like, Pepsin-like aspartic proteases, bilobal enzymes that cleave bonds in peptides at acidic pH. Pepsin-like aspartic proteases are found in mammals, plants, fungi and bacteria. These well known and extensively characterized enzymes include pepsins, chymosin, renin, cathepsins, and fungal aspartic proteases. Several have long been known to be medically (renin, cathepsin D and E, pepsin) or commercially (chymosin) important. Structurally, aspartic proteases are bilobal enzymes, each lobe contributing a catalytic Aspartate residue, with an extended active site cleft localized between the two lobes of the molecule. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. Most members of the pepsin family specifically cleave bonds in peptides that are at least six residues in length, with hydrophobic residues in both the P1 and P1' positions. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap.The enzymes are mostly secreted from cells as inactive proenzymes that activate autocatalytically at acidic pH. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
YYGEITIGTPPQKFSVIFDTGSSLLWVPSSNCTSCSCQKHPRFKYDSSKSSTYKDTGCTFSITYGDGSVT
GGLGTDTVTIGGLTIPNQTFGCATSESGDFSSSGFDGILGLGFPSLSVDGVPSFFDQLKSQGLISSPVFS
FYLGRDGDGGNGGELTFGGIDPSKYTGDLTYTPVVSNGPGYWQVPLDGISVGGKSVISSSGGGGAIVDSG
TSLIYLPSSVYDAILKALGAAVSSSDGGYGVDCSPCDTLPDITFTFLWILGDVFLRNYYTVFDLDNNRIG
FAP
>gnl|CDD|133139 cd05472, cnd41_like, Chloroplast Nucleoids DNA-binding Protease, catalyzes the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase. Chloroplast Nucleoids DNA-binding Protease catalyzes the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) in senescent leaves of tobacco. Antisense tobacco with reduced amount of CND41 maintained green leaves and constant protein levels, especially Rubisco. CND41 has DNA-binding as well as aspartic protease activities. The pepsin-like aspartic protease domain is located at the C-terminus of the protein. The enzyme is characterized by having two aspartic protease catalytic site motifs, the Asp-Thr-Gly-Ser in the N-terminal and Asp-Ser-Gly-Ser in the C-terminal region. Aspartic proteases are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe may be evolved from the other through ancient gene-duplication event. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
EYVVTVGLGTPARDQTVIVDTGSDLTWVQCQPCCLYQVSYGDGSYTTGDLATDTLTLGSSDVVPGFAFGC
GHDNEGLFGGAAGLLGLGRGKLSLPSQTASSYGGVFSYCLPDRSSSSSGYLSFGAAASVPAGASFTPMLS
NPRVPTFYYVGLTGISVGGRRLPIPPASFGAGGVIIDSGTVITRLPPSAYAALRDAFRAAMAAYPRAPGF
SILDTCYDLSGFRSVSVPTVSLHFQGGADVELDASGVLYPVDDSSQVCLAFAGTSDDGGLSIIGNVQQQT
FRVVYDVAGGRIGFAPGGC
>gnl|CDD|133140 cd05473, beta_secretase_like, Beta-secretase, aspartic-acid protease important in the pathogenesis of Alzheimer's disease. Beta-secretase also called BACE (beta-site of APP cleaving enzyme) or memapsin-2. Beta-secretase is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths in peripheral nerve cells. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. Beta-secretase is a member of pepsin family of aspartic proteases. Same as other aspartic proteases, beta-secretase is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The enzymes specifically cleave bonds in peptides which have at least six residues in length with hydrophobic residues in both the P1 and P1' positions. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap. The enzymes are mostly secreted from cells as inactive proenzymes that activate autocatalytically at acidic pH. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
GQGYYIEMLIGTPPQKLNILVDTGSSNFAVAAAPHPFIHTYFHRELSSTYRDLGKGVTVPYTQGSWEGEL
GTDLVSIPKGPNVTFRANIAAITESENFFLNGSNWEGILGLAYAELARPDSSVEPFFDSLVKQTGIPDVF
SLQMCGAGLPVNGSASGTVGGSMVIGGIDPSLYKGDIWYTPIREEWYYEVIILKLEVGGQSLNLDCKEYN
YDKAIVDSGTTNLRLPVKVFNAAVDAIKAASLIEDFPDGFWLGSQLACWQKGTTPWEIFPKISIYLRDEN
SSQSFRITILPQLYLRPVEDHGTQLDCYKFAISQSTNGTVIGAVIMEGFYVVFDRANKRVGFAVSTCAEH
DGFRTSEIEGPFST
>gnl|CDD|133141 cd05474, SAP_like, SAPs, pepsin-like proteinases secreted from pathogens to degrade host proteins. SAPs (Secreted aspartic proteinases) are secreted from a group of pathogenic fungi, predominantly Candida species. They are secreted from the pathogen to degrade host proteins. SAP is one of the most significant extracellular hydrolytic enzymes produced by C. albicans. SAP proteins, encoded by a family of 10 SAP genes. All 10 SAP genes of C. albicans encode preproenzymes, approximately 60 amino acid longer than the mature enzyme, which are processed when transported via the secretory pathway. The mature enzymes contain sequence motifs typical for all aspartyl proteinases, including the two conserved aspartate residues other active site and conserved cysteine residues implicated in the maintenance of the three-dimensional structure. Most Sap proteins contain putative N-glycosylation sites, but it remains to be determined which Sap proteins are glycosylated. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA). The overall structure of Sap protein conforms to the classical aspartic proteinase fold typified by pepsin. SAP is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe may be evolved from the other through ancient gene-duplication event. More recently evolved enzymes have similar three-dimensional structures, however their amino acid sequences are more divergent except for the conserved catalytic site motif. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
TYYSAELSVGTPPQKVTVLLDTGSSDLWVPDFSISYGDGTSASGTWGTDTVSIGGATVKNLQFAVANSTS
SDVGVLGIGLPGNEATYGTGYTYPNFPIALKKQGLIKKNAYSLYLNDLDASTGSILFGGVDTAKYSGDLV
TLPIVNDNGGSEPSELSVTLSSISVNGSSGNTTLLSKNLPALLDSGTTLTYLPSDIVDAIAKQLGATYDS
DEGLYVVDCDAKDDGSLTFNFGGATISVPLSDLVLPASTDDGGDGACYLGIQPSTSDYNILGDTFLRSAY
VVYDLDNNEISLAQA
>gnl|CDD|133142 cd05475, nucellin_like, Nucellins, plant aspartic proteases specifically expressed in nucellar cells during degradation. Nucellins are important regulators of nucellar cell's progressive degradation after ovule fertilization. This degradation is a characteristic of programmed cell death. Nucellins are plant aspartic proteases specifically expressed in nucellar cells during degradation. The enzyme is characterized by having two aspartic protease catalytic site motifs, the Asp-Thr-Gly-Ser in the N-terminal and Asp-Ser-Gly-Ser in the C-terminal region, and two other regions nearly identical to two regions of plant aspartic proteases. Aspartic proteases are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe may be evolved from the other through ancient gene-duplication event. Although the three-dimensional structures of the two lobes are very similar, the amino acid sequences are more divergent, except for the conserved catalytic site motif
GYYYVTINIGNPPKPYFLDIDTGSDLTWLQCDAPCTGCQCDYEIEYADGGSSMGVLVTDIFSLKLTNGSR
AKPRIAFGCGYDQQGPLLNPPPPTDGILGLGRGKISLPSQLASQGIIKNVIGHCLSSNGGGFLFFGDDLV
PSSGVTWTPMRRESQKKHYSPGPASLLFNGQPTGGKGLEVVFDSGSSYTYFNAQAYFKPLTLKFGKGWRT
RLLEIPPENYLIISEKGNVCLGILNGSEIGLGNTNIIGDISMQGLMVIYDNEKQQIGWVRSDC
>gnl|CDD|133143 cd05476, pepsin_A_like_plant, Chroloplast Nucleoids DNA-binding Protease and Nucellin, pepsin-like aspartic proteases from plants. This family contains pepsin like aspartic proteases from plants including Chloroplast Nucleoids DNA-binding Protease and Nucellin. Chloroplast Nucleoids DNA-binding Protease catalyzes the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) in senescent leaves of tobacco and Nucellins are important regulators of nucellar cell's progressive degradation after ovule fertilization. Structurally, aspartic proteases are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The enzymes specifically cleave bonds in peptides which have at least six residues in length with hydrophobic residues in both the P1 and P1' positions. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap. The enzymes are mostly secreted from cells as inactive proenzymes that activate autocatalytically at acidic pH
EYLVTLSIGTPPQPFSLIVDTGSDLTWTQCCSYEYSYGDGSSTSGVLATETFTFGDSSVSVPNVAFGCGT
DNEGGSFGGADGILGLGRGPLSLVSQLGSTGNKFSYCLVPHDDTGGSSPLILGDAADLGGSGVVYTPLVK
NPANPTYYYVNLEGISVGGKRLPIPPSVFAIDSDGSGGTIIDSGTTLTYLPDPAYPDLTLHFDGGADLEL
PPENYFVDVGEGVVCLAILSSSSGGVSILGNIQQQNFLVEYDLENSRLGFAPADC
>gnl|CDD|133144 cd05477, gastricsin, Gastricsins, asparate proteases produced in gastric mucosa. Gastricsin is also called pepsinogen C. Gastricsins are produced in gastric mucosa of mammals. It is synthesized by the chief cells in the stomach as an inactive zymogen. It is self-converted to a mature enzyme under acidic conditions. Human gastricsin is distributed throughout all parts of the stomach. Gastricsin is synthesized as an inactive progastricsin that has an approximately 40 residue prosequence. It is self-converting to a mature enzyme being triggered by a drop in pH from neutrality to acidic conditions. Like other aspartic proteases, gastricsin are characterized by two catalytic aspartic residues at the active site, and display optimal activity at acidic pH. Mature enzyme has a pseudo-2-fold symmetry that passes through the active site between the catalytic aspartate residues. Structurally, aspartic proteases are bilobal enzymes, each lobe contributing a catalytic aspartate residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe may be evolved from the other through ancient gene-duplication event. Although the three-dimensional structures of the two lobes are very similar, the amino acid sequences are more divergent, except for the conserved catalytic site motif. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
DMSYYGEISIGTPPQNFLVLFDTGSSNLWVPSVLCQSQACTNHTKFNPSQSSTYSTNGETFSLQYGSGSL
TGIFGYDTVTVQGIIITNQEFGLSETEPGTNFVYAQFDGILGLAYPSISAGGATTVMQGMMQQNLLQAPI
FSFYLSGQQGQQGGELVFGGVDNNLYTGQIYWTPVTSETYWQIGIQGFQINGQATGWCSQGCQAIVDTGT
SLLTAPQQVMSTLMQSIGAQQDQYGQYVVNCNNIQNLPTLTFTINGVSFPLPPSAYILQNNGYCTVGIEP
TYLPSQNGQPLWILGDVFLRQYYSVYDLGNNQVGFATA
>gnl|CDD|133145 cd05478, pepsin_A, Pepsin A, aspartic protease produced in gastric mucosa of mammals. Pepsin, a well-known aspartic protease, is produced by the human gastric mucosa in seven different zymogen isoforms, subdivided into two types: pepsinogen A and pepsinogen C. The prosequence of the zymogens are self cleaved under acidic pH. The mature enzymes are called pepsin A and pepsin C, correspondingly. The well researched porcine pepsin is also in this pepsin A family. Pepsins play an integral role in the digestion process of vertebrates. Pepsins are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe may be evolved from the other through ancient gene-duplication event. More recently evolved enzymes have similar three-dimensional structures, however their amino acid sequences are more divergent except for the conserved catalytic site motif. Pepsins specifically cleave bonds in peptides which have at least six residues in length with hydrophobic residues in both the P1 and P1' positions. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
EPLTNYLDMEYYGTISIGTPPQDFTVIFDTGSSNLWVPSVYCSSQACSNHNRFNPRQSSTYQSTGQPLSI
QYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFFYYAPFDGILGLAYPSIASSGATPVFDNMMSQ
GLVSQDLFSVYLSSNGQQGSVVTFGGIDPSYYTGSLNWVPVTAETYWQITVDSVTINGQVVACSGGCQAI
VDTGTSLLVGPSSDIANIQSDIGASQNQNGEMVVNCSSISSMPDVVFTINGVQYPLPPSAYILQDQGSCT
SGFQSMGLGELWILGDVFIRQYYSVFDRANNKVGLAP
>gnl|CDD|133146 cd05479, RP_DDI, RP_DDI; retropepsin-like domain of DNA damage inducible protein. The family represents the retropepsin-like domain of DNA damage inducible protein. DNA damage inducible protein has a retropepsin-like domain and an amino-terminal ubiquitin-like domain and/or a UBA (ubiquitin-associated) domain. This CD represents the retropepsin-like domain of DDI
QNAMEHHPESFGKVPMLYINVEINGVPVKAFVDSGAQMTIMSKACAEKCGLMRLIDKRFQGIAKGVGTQK
ILGRIHLAQVKIGNLFLPCSFTVLEDDDVDFLIGLDMLKRHQCVIDLKENVLRI
>gnl|CDD|133147 cd05480, NRIP_C, NRIP_C; putative nuclear receptor interacting protein. Proteins in this family have been described as probable nuclear receptor interacting proteins. The C-terminal domain of this family is homologous to the retroviral aspartyl protease domain. The domain is structurally related to one lobe of the pepsin molecule. The conserved active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A
VSCQCAGKELRALVDTGCQYNLISAACLDRLGLKERVLKAKAEEEAPSLPTSVKVIGQIERLVLQLGQLT
VECSAQVVDDNEKNFSLGLQTLKSLKCVINLEK
>gnl|CDD|133148 cd05481, retropepsin_like_LTR_1, Retropepsins_like_LTR; pepsin-like aspartate protease from retrotransposons with long terminal repeats. Retropepsin of retrotransposons with long terminal repeats are pepsin-like aspartate proteases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A
LDMKINGKQSVKFQLDTGATCNVLPLRWLKSLTPDKDPELRPSPVRLTAYGGSTIPVEGGVKLKCRYRNP
KYNLTFQVVKEEGPPLLGAKACE
>gnl|CDD|133149 cd05482, HIV_retropepsin_like, Retropepsins, pepsin-like aspartate proteases. This is a subfamily of retropepsins. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A
LTLYINGKLFEGLLDTGADVSIIAENDWPKNWPIQPAPSNLTGIGGAITPSQSSVLLLEIDGEGHLGTIL
VYVLSLPVNLWGRDILS
>gnl|CDD|133150 cd05483, retropepsin_like_bacteria, Bacterial aspartate proteases, retropepsin-like protease family. This family of bacteria aspartate proteases is a subfamily of retropepsin-like protease family, which includes enzymes from retrovirus and retrotransposons. While fungal and mammalian pepsin-like aspartate proteases are bilobal proteins with structurally related N- and C-termini, this family of bacteria aspartate proteases is half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate proteases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A
GHFVVPVTINGQPVRFLLDTGASTTVISEELAERLGLPLTLGGKVTVQTANGRVRAARVRLDSLQIGGIT
LRNVPAVVLPGDALGVDGLLGMDFLR
>gnl|CDD|133151 cd05484, retropepsin_like_LTR_2, Retropepsins_like_LTR, pepsin-like aspartate proteases. Retropepsin of retrotransposons with long terminal repeats are pepsin-like aspartate proteases. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A
KTVTLLVNGKPLKFQLDTGSAITVISEKTWRKLGSPPLKPTKKRLRTATGTKLSVLGQILVTVKYGGKTK
VLTLYVVKNEGLNLLGRDWLD
>gnl|CDD|133152 cd05485, Cathepsin_D_like, Cathepsin_D_like, pepsin family of proteinases. Cathepsin D is the major aspartic proteinase of the lysosomal compartment where it functions in protein catabolism. It is a member of the pepsin family of proteinases. This enzyme is distinguished from other members of the pepsin family by two features that are characteristic of lysosomal hydrolases. First, mature Cathepsin D is found predominantly in a two-chain form due to a posttranslational cleavage event. Second, it contains phosphorylated, N-linked oligosaccharides that target the enzyme to lysosomes via mannose-6-phosphate receptors. Cathepsin D preferentially attacks peptide bonds flanked by bulky hydrophobic amino acids and its pH optimum is between pH 2.8 and 4.0. Two active site aspartic acid residues are essential for the catalytic activity of aspartic proteinases. Like other aspartic proteinases, Cathepsin D is a bilobed molecule; the two evolutionary related lobes are mostly made up of beta-sheets and flank a deep active site cleft. Each of the two related lobes contributes one active site aspartic acid residue and contains a single carbohydrate group. Cathepsin D is an essential enzyme. Mice deficient for proteinase cathepsin D, generated by gene targeting, develop normally during the first 2 weeks, stop thriving in the third week and die in a state of anorexia in the fourth week. The mice develop atrophy of ileal mucosa followed by other degradation of intestinal organs. In these knockout mice, lysosomal proteolysis was normal. These results suggest that vital functions of cathepsin D are exerted by limited proteolysis of proteins regulating cell growth and/or tissue homeostasis, while its contribution to bulk proteolysis in lysosomes appears to be non-critical. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
PEPLSNYMDAQYYGVITIGTPPQSFKVVFDTGSSNLWVPSKKCSWTNIACLLHNKYDSTKSSTYKKNGTE
FAIQYGSGSLSGFLSTDTVSVGGVSVKGQTFAEAINEPGLTFVAAKFDGILGMGYSSISVDGVVPVFYNM
VNQKLVDAPVFSFYLNRDPSAKEGGELILGGSDPKHYTGNFTYLPVTRKGYWQFKMDSVSVGEGEFCSGG
CQAIADTGTSLIAGPVDEIEKLNNAIGAKPIIGGEYMVNCSAIPSLPDITFVLGGKSFSLTGKDYVLKVT
QMGQTICLSGFMGIDIPPPAGPLWILGDVFIGKYYTEFDLGNNRVGFAT
>gnl|CDD|133153 cd05486, Cathespin_E, Cathepsin E, non-lysosomal aspartic protease. Cathepsin E is an intracellular, non-lysosomal aspartic protease expressed in a variety of cells and tissues. The protease has proposed physiological roles in antigen presentation by the MHC class II system, in the biogenesis of the vasoconstrictor peptide endothelin, and in neurodegeneration associated with brain ischemia and aging. Cathepsin E is the only A1 aspartic protease that exists as a homodimer with a disulfide bridge linking the two monomers. Like many other aspartic proteases, it is synthesized as a zymogen which is catalytically inactive towards its natural substrates at neutral pH and which auto-activates in an acidic environment. The overall structure follows the general fold of aspartic proteases of the A1 family, it is composed of two structurally similar beta barrel lobes, each lobe contributing an aspartic acid residue to form a catalytic dyad that acts to cleave the substrate peptide bond. The catalytic Asp residues are contained in an Asp-Thr-Gly-Ser/thr motif in both N- and C-terminal lobes of the enzyme. The aspartic acid residues act together to allow a water molecule to attack the peptide bond. One aspartic acid residue (in its deprotonated form) activates the attacking water molecule, whereas the other aspartic acid residue (in its protonated form) polarizes the peptide carbonyl, increasing its susceptibility to attack. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
YFGQISIGTPPQNFTVIFDTGSSNLWVPSIYCTSQACTKHNRFQPSESSTYVSNGEAFSIQYGTGSLTGI
IGIDQVTVEGITVQNQQFAESVSEPGSTFQDSEFDGILGLAYPSLAVDGVTPVFDNMMAQNLVELPMFSV
YMSRNPNSADGGELVFGGFDTSRFSGQLNWVPVTVQGYWQIQLDNIQVGGTVIFCSDGCQAIVDTGTSLI
TGPSGDIKQLQNYIGATATDGEYGVDCSTLSLMPSVTFTINGIPYSLSPQAYTLEDQSDGGGYCSSGFQG
LDIPPPAGPLWILGDVFIRQYYSVFDRGNNRVGFAP
>gnl|CDD|133154 cd05487, renin_like, Renin stimulates production of angiotensin and thus affects blood pressure. Renin, also known as angiotensinogenase, is a circulating enzyme that participates in the renin-angiotensin system that mediates extracellular volume, arterial vasoconstriction, and consequently mean arterial blood pressure. The enzyme is secreted by the kidneys from specialized juxtaglomerular cells in response to decreases in glomerular filtration rate (a consequence of low blood volume), diminished filtered sodium chloride and sympathetic nervous system innervation. The enzyme circulates in the blood stream and hydrolyzes angiotensinogen secreted from the liver into the peptide angiotensin I. Angiotensin I is further cleaved in the lungs by endothelial bound angiotensin converting enzyme (ACE) into angiotensin II, the final active peptide. Renin is a member of the aspartic protease family. Structurally, aspartic proteases are bilobal enzymes, each lobe contributing a catalytic Aspartate residue, with an extended active site cleft localized between the two lobes of the molecule. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap. The enzymes are mostly secreted from cells as inactive proenzymes that activate autocatalytically at acidic pH. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
LTNYLDTQYYGEIGIGTPPQTFKVVFDTGSSNLWVPSSKCSPLYTACVTHNLYDASDSSTYKENGTEFTI
HYASGTVKGFLSQDIVTVGGIPVTQMFGEVTALPAIPFMLAKFDGVLGMGYPKQAIGGVTPVFDNIMSQG
VLKEDVFSVYYSRDSSHSLGGEIVLGGSDPQHYQGDFHYINTSKTGFWQIQMKGVSVGSSTLLCEDGCTA
VVDTGASFISGPTSSISKLMEALGAKERLGDYVVKCNEVPTLPDISFHLGGKEYTLSSSDYVLQDSDFSD
KLCTVAFHAMDIPPPTGPLWVLGATFIRKFYTEFDRQNNRIGFALA
>gnl|CDD|133155 cd05488, Proteinase_A_fungi, Fungal Proteinase A, aspartic proteinase superfamily. Fungal Proteinase A, a proteolytic enzyme distributed among a variety of organisms, is a member of the aspartic proteinase superfamily. In Saccharomyces cerevisiae, targeted to the vacuole as a zymogen, activation of proteinases A at acidic pH can occur by two different pathways: a one-step process to release mature proteinase A, involving the intervention of proteinase B, or a step-wise pathway via the auto-activation product known as pseudo-proteinase A. Once active, S. cerevisiae proteinase A is essential to the activities of other yeast vacuolar hydrolases, including proteinase B and carboxypeptidase Y. The mature enzyme is bilobal, with each lobe providing one of the two catalytically essential aspartic acid residues in the active site. The crystal structure of free proteinase A shows that flap loop is atypically pointing directly into the S(1) pocket of the enzyme. Proteinase A preferentially hydrolyzes hydrophobic residues such as Phe, Leu or Glu at the P1 position and Phe, Ile, Leu or Ala at P1'. Moreover, the enzyme is inhibited by IA3, a natural and highly specific inhibitor produced by S. cerevisiae. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
VPLTNYLNAQYFTDITLGTPPQKFKVILDTGSSNLWVPSVKCGSIACFLHSKYDSSASSTYKANGTEFKI
QYGSGSLEGFVSQDTLSIGDLTIKKQDFAEATSEPGLAFAFGKFDGILGLAYDTISVNKIVPPFYNMINQ
GLLDEPVFSFYLGSSEEDGGEATFGGIDESRFTGKITWLPVRRKAYWEVELEKIGLGDEELELENTGAAI
DTGTSLIALPSDLAEMLNAEIGAKKSWNGQYTVDCSKVDSLPDLTFNFDGYNFTLGPFDYTLEVSGSCIS
AFTGMDFPEPVGPLAIVGDAFLRKYYSVYDLGNNAVGLAK
>gnl|CDD|133156 cd05489, xylanase_inhibitor_I_like, TAXI-I inhibits degradation of xylan in the cell wall. Xylanase inhibitor-I (TAXI-I) is a member of potent TAXI-type inhibitors of fungal and bacterial family 11 xylanases. Plants developed a diverse battery of defense mechanisms in response to continual challenges by a broad spectrum of pathogenic microorganisms. Their defense arsenal includes inhibitors of cell wall-degrading enzymes, which hinder a possible invasion and colonization by antagonists. Xylanases of fungal and bacterial pathogens are the key enzymes in the degradation of xylan in the cell wall. Plants secrete proteins that inhibit these degradation glycosidases, including xylanase. Surprisingly, TAXI-I displays structural homology with the pepsin-like family of aspartic proteases but is proteolytically nonfunctional, because one or more residues of the essential catalytic triad are absent. The structure of the TAXI-inhibitor, Aspergillus niger xylanase I complex, illustrates the ability of tight binding and inhibition with subnanomolar affinity and indicates the importance of the C-terminal end for the differences in xylanase specificity among different TAXI-type inhibitors. This family also contains pepsin-like aspartic proteinases homologous to TAXI-I. Unlike TAXI-I, they have active site aspartates and are functionally active. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
YTITPLKGAVPLVLDLAGPLLWSTCDAGHSSTYQTVPCSSSVCSLANRYHCPGTCGGAPGPGCGNNTCTA
HPYNPVTGECATGDLTQDVLSANTTDGSNPLLVVIFNFVFSCAPSLLLKGLPPGAQGVAGLGRSPLSLPA
QLASAFGVARKFALCLPSSPGGPGVAIFGGGPYYLFPPPIDLSKSLSYTPLLTNPRKSGEYYIGVTSIAV
NGHAVPLNPTLSANDRLGPGGVKLSTVVPYTVLRSDIYRAFTQAFAKATARIPRVPAAAVFPELCYPASA
LGNTRLGYAVPAIDLVLDGGGVNWTIFGANSMVQVKGGVACLAFVDGGSEPRPAVVIGGHQMEDNLLVFD
LEKSRLGFSSSL
>gnl|CDD|133157 cd05490, Cathepsin_D2, Cathepsin_D2, pepsin family of proteinases. Cathepsin D is the major aspartic proteinase of the lysosomal compartment where it functions in protein catabolism. It is a member of the pepsin family of proteinases. This enzyme is distinguished from other members of the pepsin family by two features that are characteristic of lysosomal hydrolases. First, mature Cathepsin D is found predominantly in a two-chain form due to a posttranslational cleavage event. Second, it contains phosphorylated, N-linked oligosaccharides that target the enzyme to lysosomes via mannose-6-phosphate receptors. Cathepsin D preferentially attacks peptide bonds flanked by bulky hydrophobic amino acids and its pH optimum is between pH 2.8 and 4.0. Two active site aspartic acid residues are essential for the catalytic activity of aspartic proteinases. Like other aspartic proteinases, Cathepsin D is a bilobed molecule; the two evolutionary related lobes are mostly made up of beta-sheets and flank a deep active site cleft. Each of the two related lobes contributes one active site aspartic acid residue and contains a single carbohydrate group. Cathepsin D is an essential enzyme. Mice deficient for proteinase cathepsin D, generated by gene targeting, develop normally during the first 2 weeks, stop thriving in the third week and die in a state of anorexia in the fourth week. The mice develop atrophy of ileal mucosa followed by other degradation of intestinal organs. In these knockout mice, lysosomal proteolysis was normal. These results suggest that vital functions of cathepsin D are exerted by limited proteolysis of proteins regulating cell growth and/or tissue homeostasis, while its contribution to bulk proteolysis in lysosomes appears to be non-critical. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
NYMDAQYYGEIGIGTPPQTFTVVFDTGSSNLWVPSVHCSLLDIACWLHHKYNSSKSSTYVKNGTEFAIQY
GSGSLSGYLSQDTVSIGGLQVEGQLFGEAVKQPGITFIAAKFDGILGMAYPRISVDGVTPVFDNIMAQKL
VEQNVFSFYLNRDPDAQPGGELMLGGTDPKYYTGDLHYVNVTRKAYWQIHMDQVDVGSGLTLCKGGCEAI
VDTGTSLITGPVEEVRALQKAIGAVPLIQGEYMIDCEKIPTLPVISFSLGGKVYPLTGEDYILKVSQRGT
TICLSGFMGLDIPPPAGPLWILGDVFIGRYYTVFDRDNDRVGFAK
>gnl|CDD|99923 cd05491, Bromo_TBP7_like, Bromodomain; TBP7_like subfamily, limited to fungi. TBP7, or TAT-binding protein homolog 7, is a yeast protein of unknown function that contains AAA-superfamily ATP-ase domains and a bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine
LKKFRQPIIDELQRKYLKFEKPPTEDAFVRPDNENNEERPYEIAKDKQGVDTILETASGKKFYNMDLDTI
EERLWNGYYATPKDFLKDIKRIVRDAKTIGDRERLLKANEMFANAELDI
>gnl|CDD|99924 cd05492, Bromo_ZMYND11, Bromodomain; ZMYND11_like sub-family. ZMYND11 or BS69 is a ubiquitously expressed nuclear protein that has been shown to associate with chromatin. It interacts with chromatin remodeling factors and might play a role in chromatin remodeling and gene expression. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
LNCLLKFIVSRMKSWLPPDTTNRAIVLNKRGKATKLPKRRRLIHTHLDVADIQEKINSEKYTSLEEFKAD
ALLLLHNTAIFHGADSEQYDAARWLYRDTCHDLRELRLC
>gnl|CDD|99925 cd05493, Bromo_ALL-1, Bromodomain, ALL-1 like proteins. ALL-1 is a vertebrate homologue of Drosophila trithorax and is often affected in chromosomal rearrangements that are linked to acute leukemias, such as acute lymphocytic leukemia (ALL). Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine
ELEELLDSRTKSHLLRCGPKPPALLPETEESLPGRKSPVTPEVLQGLLSSEVKQEELPPLDLEAVGKKLE
AGFYTSVLDFSDDIVKIIQAALNSEGGQPEIKKANSMAKSFFIKLMESVFPWFNSEDPKLW
>gnl|CDD|99926 cd05494, Bromodomain_1, Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine
DYEALERVLRELKRHRRNEDAWPFLEPVNPPRRGAPDYRDVIKRPMSFGTKVNNIVETGARDLEDLQIVQ
EDPADKQIDDEGRRSPSNIYAVEALEQLIVFQCKQVKGLKQKRH
>gnl|CDD|99927 cd05495, Bromo_cbp_like, Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDD
VWLMFDNAWLYNRKTSRVYKYCTKLAEVFEQEIDPVMQ
>gnl|CDD|99928 cd05496, Bromo_WDR9_II, Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
YDESDWKKQCKELVNLMWDCEDSEPFRQPVDLLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDV
RLIFSNSKSYTPNKRSRIYSMTLRLSALFEEHIKKIISDWKSALKRNEK
>gnl|CDD|99929 cd05497, Bromo_Brdt_I_like, Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
RHTNQLQYLLKVVLKALWKHKFAWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQ
DFNTMFTNCYIYNKPGDDVVLMAQTLEKLFLQKLAQM
>gnl|CDD|99930 cd05498, Bromo_Brdt_II_like, Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
QLKFCSGILKELFSKKHKAYAWPFYKPVDPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADV
RLMFSNCYKYNPPDHPVHAMARKLQDVFEDRW
>gnl|CDD|99931 cd05499, Bromo_BDF1_2_II, Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
ELKFCEEVLKELMKPKHSAYNWPFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDV
RLIFKNCYTFNPEGTDVYMMGHQLEEVFNDKW
>gnl|CDD|99932 cd05500, Bromo_BDF1_2_I, Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
MTKHQHKFLLSSIRSLKRLKDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTAD
FNLMVDNCLTFNGPEHPVSQMGKRLQAAFEKHL
>gnl|CDD|99933 cd05501, Bromo_SP100C_like, Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major component of PML-SP100 nuclear bodies (NBs), which are poorly understood. It is covalently modified by SUMO-1 and may play a role in processes at the chromatin level. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
PEELLKCEFLLLKVYCMSKSGFFISKPYYIRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFH
NHKLFYKDDDFGQVGITLEKKFEKNFKEVFAI
>gnl|CDD|99934 cd05502, Bromo_tif1_like, Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or corepressors to modulate transcription. Vertebrate Tif1-gamma, also labeled E3 ubiquitin-protein ligase TRIM33, plays a role in the control of hematopoiesis. Its homologue in Xenopus laevis, Ectodermin, has been shown to function in germ-layer specification and control of cell growth during embryogenesis. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
LSPIDQRKCERLLLELYCHELSLPFHEPVSPSVPNYYKIIKTPMDLSLIRKKLQPKSPQHYSSPEEFVAD
VRLMFKNCYKFNEEDSEVAQAGKELELFFEEQLKEILPD
>gnl|CDD|99935 cd05503, Bromo_BAZ2A_B_like, Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B (BAZ2B) were identified as a novel human bromodomain gene by cDNA library screening. BAZ2A is also known as Tip5 (Transcription termination factor I-interacting protein 5) and hWALp3. The proteins may play roles in transcriptional regulation. Human Tip5 is part of a complex termed NoRC (nucleolar remodeling complex), which induces nucleosome sliding and may play a role in the regulation of the rDNA locus. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
DLALCETILDEMEAHEDAWPFLEPVNTKLVPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFD
NCETFNEDDSEVGRAGHNMRKFFEKRW
>gnl|CDD|99936 cd05504, Bromo_Acf1_like, Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was identified as a novel human bromodomain gene by cDNA library screening. The Drosophila homologue, Acf1, is part of the CHRAC (chromatin accessibility complex) and regulates ISWI-induced nucleosome remodeling. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
RRRSEGRHHGPLNLSALEQLLVEIVKHKDSWPFLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLA
EEFLSDIQLVFSNCFLYNPEHTSVYKAGTRLQRFFIKRCRKLGLP
>gnl|CDD|99937 cd05505, Bromo_WSTF_like, Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The Williams-Beuren syndrome deletion transcript 9 is a putative transcriptional regulator. WSTF was found to play a role in vitamin D-mediated transcription as part of two chromatin remodeling complexes, WINAC and WICH. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
ELQKCEEILSKILKYRFSWPFREPVTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFS
NAEKYYENGSYVLSCMRKTEQCCVNLL
>gnl|CDD|99938 cd05506, Bromo_plant1, Bromodomain, uncharacterized subfamily specific to plants. Might function as a global transcription factor. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
VMKQCGTLLRKLMKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLT
FANAMRYNPPGNDVHTMAKELLKIFETRW
>gnl|CDD|99939 cd05507, Bromo_brd8_like, Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with the thyroid hormone receptor in a ligand-dependent fashion and enhances thyroid hormone-dependent activation from thyroid response elements. Brd8 is thought to be a nuclear receptor coactivator. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
YRAWKKAILLVYRTLASHRYASVFLKPVTEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLL
MFQNAIMYNSSDHDVYLMAVEMQREVMSQIQQLL
>gnl|CDD|99940 cd05508, Bromo_RACK7, Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) was identified as a potential tumor suppressor genes, it shares domain architecture with BS69/ZMYND11; both have been implicated in the regulation of cellular proliferation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
VDQLSKLLKFALERMKQPGAEPFLKPVDLEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWI
LHNAIIYNGGDHKLTQAAKAIVKICEQEM
>gnl|CDD|99941 cd05509, Bromo_gcn5_like, Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates acetylation of histones at lysine residues; such acetylation is generally correlated with the activation of transcription. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
PLYTQLKKVLDSLKNHKSAWPFLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIF
DNCRLYNGPDTEYYKCANKLEKFFWKKLKEL
>gnl|CDD|99942 cd05510, Bromo_SPT7_like, Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, and SLIK. SAGA is involved in the RNA polymerase II-dependent transcriptional regulation of about 10% of all yeast genes. The SPT7 bromodomain has been shown to weakly interact with acetylated histone H3, but not H4. The human representative of this subfamily is cat eye syndrome critical region protein 2 (CECR2). Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
ERIGQEEFYESLDKVLNELKTYTEHSTPFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFV
DDLNLIWKNCLLYNSDPSHPLRRHANFMKKKAEHLLKLIPDI
>gnl|CDD|99943 cd05511, Bromo_TFIID, Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, a large multi-domain complex, which initiates the assembly of the transcription machinery. TAFII250 contains two bromodomains that specifically bind to acetylated histone H4. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
LSFILDEIVNELKNLPDSWPFHTPVNKKKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVD
NSVLYNGPDSVYTKKAKEMLELAEELLAEREEKLTQLEKNIN
>gnl|CDD|99944 cd05512, Bromo_brd1_like, Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein assumed to be a transcriptional regulator. BRD1 has been implicated with brain development and susceptibility to schizophrenia and bipolar affective disorder. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
PLEVLLRKTLDQLQEKDTAEIFSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLII
NNCLAYNAKDTIFYRAAVRLRDQGGAIL
>gnl|CDD|99945 cd05513, Bromo_brd7_like, Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown to inhibit cell growth and the progression of the cell cycle by regulating cell-cycle genes at the transcriptional level. BRD7 has been identified as a gene involved in nasopharyngeal carcinoma. The protein interacts with acetylated histone H3 via its bromodomain. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
PLQKALEQLIRQLQRKDPHGFFAFPVTDFIAPGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMC
ENAMKYNKPDTIYYKAAKKLLHSGMKIL
>gnl|CDD|99946 cd05515, Bromo_polybromo_V, Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine
MQQKLWELYNAVKNYTDGRGRRLSLIFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSD
FVLMFDNACKYNEPDSQIYKDALTLQKVLLETKRE
>gnl|CDD|99947 cd05516, Bromo_SNF2L2, Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
ELTKKMNKIVDVVIKYKDSDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEK
DVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQKI
>gnl|CDD|99948 cd05517, Bromo_polybromo_II, Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine
LKQILEQLLEAVMTATDPSGRLISELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKD
LDLMVKNAKTFNEPGSQVYKDANAIKKIFTAKK
>gnl|CDD|99949 cd05518, Bromo_polybromo_IV, Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine
RKKRMLALFLYVLEYREGSGRRLCDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDD
FKLMFRNARHYNEEGSQVYEDANILEKVLKEKR
>gnl|CDD|99950 cd05519, Bromo_SNF2, Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in transcriptional activation, it is the catalytic component of the SWI/SNF ATP-dependent chromatin remodeling complex. The protein is essential for the regulation of gene expression (both positive and negative) of a large number of genes. The SWI/SNF complex changes chromatin structure by altering DNA-histone contacts within the nucleosome, which results in a re-positioning of the nucleosome and facilitates or represses the binding of gene-specific transcription factors. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
LKAAMLEIYDAVLNCEDETGRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLED
FHLMFANARTYNQEGSIVYEDAVEMEKAFKKKY
>gnl|CDD|99951 cd05520, Bromo_polybromo_III, Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine
SSNPLWQLYDTIRNARNNQGQLLAEPFLKLPSKRKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEAD
LNLMFENAKRYNVPNSRIYKDAEKLQKLMQAKK
>gnl|CDD|99952 cd05521, Bromo_Rsc1_2_I, Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
KLSKKLKPLYDGIYTLKEENGIEIHPIFNVLPLRKDYPDYYKIIKNPLSLNTVKKRLPHYTNAQEFVNDL
AQIPWNARLYNTKGSVIYKYALILEKYINDVIIPNL
>gnl|CDD|99953 cd05522, Bromo_Rsc1_2_II, Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
PYEARIKNILKGLRKERDENGRLLTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLN
DLNLMFENAKLYNENDSQEYKDAVLLEKEARLLA
>gnl|CDD|99954 cd05524, Bromo_polybromo_I, Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine
LDPIAVCQELYDTIRNYKSEDGRILCESFIRVPKRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLT
ADFELLINNAKAYYKPDSPEHKDACKLWELFLSARNEVLSGGE
>gnl|CDD|99955 cd05525, Bromo_ASH1, Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the trithorax-group in Drosophila melanogaster, an epigenetic transcriptional regulator of HOX genes. Drosophila ASH1 has been shown to methylate specific lysines in histones H3 and H4. Mammalian ASH1 has been shown to methylate histone H3. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
ARLAQVLKEICDAIITYKDSNGQSLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFD
SDMLKVFRNAEKYYGRKSPIGRDVCRLRKAYYQAKH
>gnl|CDD|99956 cd05526, Bromo_polybromo_VI, Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine
QLLVQELLATLFVSVMNHQDEEGRCYSDSLAELPELAVDGVGPKKIPLTLDIIKRNVDKGRYRRLDKFQE
DMFEVLERARRLSRTDSEIYEDAVELQQFFIKIRDELCKN
>gnl|CDD|99957 cd05528, Bromo_AAA, Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. The structure(2DKW) in this alignment is an uncharacterized protein predicted from analysis of cDNA clones from human fetal liver
LRELRLFLRDVLKRLASDKRFNAFTKPVDEEEVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDL
IVTNALEYNPDRDPADKLIRSRACELRDEVHAMIEAELDPLF
>gnl|CDD|99958 cd05529, Bromo_WDR9_I_like, Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine
LYNPLSSEWELFDPGWEQPHIRDEERERLISGLDKLLLSLQLEIAEYFEYPVDLRAWYPDYWNRVPVPMD
LETIRSRLENRYYRSLEALRHDVRLILSNAETFNEPNSEIAKKAKRLSDWLLRILSSL
>gnl|CDD|99913 cd05530, POLBc_B1, DNA polymerase type-B B1 subfamily catalytic domain. Archaeal proteins that are involved in DNA replication are similar to those from eukaryotes. Some archaeal members also possess multiple family B DNA polymerases (B1, B2 and B3). So far there is no specific function(s) has been assigned for different members of the archaea type B DNA polymerases. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family B DNA polymerases are support independent gene duplications during the evolution of archaeal and eukaryotic family B DNA polymerases
QTSTQAIIKGKKYRGAIVLEPPPGIFFNVVVLDFASLYPSIIKVWNLSYETVNCPHCECKTNEVPEVGHW
VCKKRPGITSQIIGLLRDLRVKIYKKKAKDKSLDEEMRQWYDVVQSAMKVFINASYGVFGAENFPLYCPP
VAESTTALGRYIITSTIKKARELGLKVLYGDTDSLFLWNPPQEQLEDLVEWVEKELGLDLELDKEYRYVV
FSGLKKNYLGVTKDGSVDIKGLLGKKRNTPEFVKELFYEVIEILSAVNSPEDFEKAREKIRDIVKGVYKR
LKKKEYTLDQLAFKVMLSKPPEEYTKNTPQHVKAARQLEKYGRNVEAGDIISYVKVKGKEGVKPVQLARL
DEVDVEKYVEIMRSTLEQILGA
>gnl|CDD|99914 cd05531, POLBc_B2, DNA polymerase type-B B2 subfamily catalytic domain. Archaeal proteins that are involved in DNA replication are similar to those from eukaryotes. Some archaeal members also possess multiple family B DNA polymerases (B1, B2 and B3). So far there is no specific function(s) has been assigned for different members of the archaea type B DNA polymerases. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family B DNA polymerases are support independent gene duplications during the evolution of archaeal and eukaryotic family B DNA polymerases
LLLADRGGLVFQPEPGLYENVAQIDFSSMYPSIIVKYNISPETINCRCCECRDHVYLGHRICLKRRGFLP
EVLEPLLERRLEYKRLKKEEDPYAGRQKALKWILVTSFGYLGYKNAKFGRIEVHEAITAYGRKILLRAKE
IAEEMGFRVLHGIVDSLWIQGRGDIEELAREIEERTGIPLKLEGHYDWIVFLPERDGLGAPNRYFGRLSD
GEMKVRGIELRRRDTPPFVKKFQEEALDILASAKTPEELLKLREEALDLFRRYLQRLREGDLEDLIIEKK
ISKRSSEYKVLASTALKALRAKGVSVVPGMKIEYIVRDGKRPVPDLGNDEGYDTKYYRELLERAAEELLF
PL
>gnl|CDD|99915 cd05532, POLBc_alpha, DNA polymerase type-B alpha subfamily catalytic domain. Three DNA-dependent DNA polymerases type B (alpha, delta, and epsilon) have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase (Pol) alpha is almost exclusively required for the initiation of DNA replication and the priming of Okazaki fragments during elongation. In most organisms no specific repair role, other than check point control, has been assigned to this enzyme. Pol alpha contains both polymerase and exonuclease domains, but lacks exonuclease activity suggesting that the exonuclease domain may be for structural purposes only
KKKKKAKYAGGLVLEPKKGLYDKFILLLDFNSLYPSIIQEYNICFTTVDRADPDDEDDEEPPLPPSDQEK
GILPRIIRKLVERRRQVKKLMKSEKDPDKKAQLDIRQLALKLTANSMYGCLGFSYSRFYAKPLAALITSK
GREILQKTKDLVEKMNLEVIYGDTDSIMINTGTTDYEEAKKLGNKIKKEVNKSYKKLEIDIDGVFKRLLL
LKKKKYAALKVVDDDKGKLKKEVKGLDIVRRDWCPLSKEIGNYVLDQILSDKSREDIVENIHEYLRKINE
DLRNGKIPLEKFIITKQLTKNPEEYPDKKSLPHVQVALRMNKRGRKVKAGDTIPYIICKDGSSKSLADRA
YHPDEVKKNENLKIDIEYYLSQQILPPISRLCEPIEGTDAVRLAECLGLD
>gnl|CDD|99916 cd05533, POLBc_delta, DNA polymerase type-B delta subfamily catalytic domain. Three DNA-dependent DNA polymerases type B (alpha, delta, and epsilon) have been identified as essential for nuclear DNA replication in eukaryotes. Presently, no direct data is available regarding the strand specificity of DNA polymerase during DNA replication in vivo. However, mutation analysis supports the hypothesis that DNA polymerase delta is the enzyme responsible for both elongation and maturation of Okazaki fragments on the lagging strand
EQYEGATVIEPIKGYYDVPIATLDFASLYPSIMMAHNLCYTTLLNKNTAKKLPPEDYIKTPNGDYFVKSS
VRKGLLPEILEELLAARKRAKKDLKEETDPFKKAVLDGRQLALKISANSVYGFTGATVGKLPCLEISSSV
TSFGRQMIEKTKKLVEEKYTKANGYSHDAKVIYGDTDSVMVKFGVSDVEEAMKLGKEAAEYVSKKFIKPI
KLEFEKVYFPYLLINKKRYAGLLWTNPDKHDKMDTKGIETVRRDNCLLVQNVVETCLNKILIERDVEGAI
EFVKGVISDLLQNKIDISLLVITKALTKTADDYAGKQAHVELAERMRKRDPGSAPNVGDRVPYVIIKGAK
GAKAYEKAEDPIYVLENNIPIDTQYYLENQLSKPLLRIFEPIL
>gnl|CDD|99917 cd05534, POLBc_zeta, DNA polymerase type-B zeta subfamily catalytic domain. DNA polymerase (Pol) zeta is a member of the eukaryotic B-family of DNA polymerases and distantly related to DNA Pol delta. Pol zeta plays a major role in translesion replication and the production of either spontaneous or induced mutations. Apart from its role in translesion replication, Pol zeta also appears to be involved in somatic hypermutability in B lymphocytes, an important element for the production of high affinity antibodies in response to an antigen
GSQFRVESMLLRLAKPENYILPSPSRQQVAQQRALECLPLVMEPESGFYSDPVIVLDFQSLYPSIMIAYN
YCYSTCLGRVEELNGGGKFGFLGVKLYLPPPPLDLLLLKDDVTISPNGVMFVKKSVRKGILPKMLEEILD
TRIMVKKAMKKYKDDKKLQRILDARQLALKLLANVTYGYTAASFSGRMPCVEIADSIVQTGRETLERAIE
LIESTPKWGAKVVYGDTDSLFVLLPGRTKEEAFKIGKEIAEAVTAANPSPIKLKFEKVYHPCVLVTKKRY
VGYKYESPDQTEPTFDAKGIETVRRDGCPAVQKILEKSLRILFETKDLSTVKSYLQRQWSKLLQGRVSIQ
DFIFAKEVRLGTYKEGATLPAGAIVALRRMEKDPRAEPQYGERVPYVVVRGEPGSRLIDLVVSPEEFLAD
PSLRLDAEYYITKQIIPALDRLFNLVGVDVQ
>gnl|CDD|99918 cd05535, POLBc_epsilon, DNA polymerase type-B epsilon subfamily catalytic domain. Three DNA-dependent DNA polymerases type B (alpha, delta, and epsilon) have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase (Pol) epsilon has been proposed to play a role in elongation of the leading strand during DNA replication. Pol epsilon might also have a role in DNA repair. The structure of pol epsilon is characteristic of this family with the exception that it contains a large c-terminal domain with an unclear function. Phylogenetic analyses indicate that Pol epsilon is the ortholog to the archaeal Pol B3 rather than to Pol alpha, delta, or zeta. This might be because pol epsilon is ancestral to both archaea and eukaryotes DNA polymerases type B
GHLLESETYVGGHVEALESGVFRSDIPCRFKLDPDAIQELLQNVDETLRFAIEVEGKIPLDQVENFEEVR
EEILEKLQSLRDNPKRSEKPLIYHLDVAAMYPNIILTNRLQPDAIVDEDVCAACDFNKPGKTCQRRMEWA
WRGEYFPASRGEYERIKQQLESEKFPPLFPGGPPKSFHELSPEEQAEELKKRLKDYSRKVYKKTHVTKEE
ERSTTICQRENPFYVDTVRAFRDRRYEYKGLHKVWKKKLEAAKAAGDAAEIKEAKKMVVLYDSLQLAHKC
ILNSFYGYVMRKGSRWYSMEMAGIVCYTGANIIQMARELVEQIGRPLELDTDGIWCILPKSFPENFTFKT
KNGKKVTISYPCVMLNHLVHKKFTNDQYQELVDPSTGTYETRSENSIFFEVDGPYKAMILPASKEEGKLL
KKRYAVFNEDGSLAELKGFEVKRRGELQLIKIFQSEVFDAFLKGSTLEECYAAVAAVANYWLDVLDSKGE
NLDDEELFELISENRSMSKKLEEYGNQKSTSITTAKRLAEFLGDQMVKDKGLSCKYIISKKPEGSPVTER
AIPVAIFQAEPEVRKHYLRKWLKDPSDEDLDIRDIIDWDYYIERLGSTIQKIITIPAALQG
>gnl|CDD|99919 cd05536, POLBc_B3, DNA polymerase type-B B3 subfamily catalytic domain. Archaeal proteins that are involved in DNA replication are similar to those from eukaryotes. Some members of the archaea also possess multiple family B DNA polymerases (B1, B2 and B3). So far there is no specific function(s) has been assigned for different members of the archaea type B DNA polymerases. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family B DNA polymerases are support independent gene duplications during the evolution of archaeal and eukaryotic family B DNA polymerases. Structural comparison of the thermostable DNA polymerase type B to its mesostable homolog suggests several adaptations to high temperature such as shorter loops, disulfide bridges, and increasing electrostatic interaction at subdomain interfaces
RESYEGGIVLEPEKGLHENIVVLDFSSLYPSIMIKYNISPDTLVREGCEDCDVEPQVGHKFRKDPPGFIP
SVLEDLLEERRRIKEKMKKLDPESEEYKLLDERQRAIKILANSFYGYMGWANARWYCKECAEAVTAWGRE
YIKTTIKIAEEKGFKVIYGDTDSLFVKIDGADAVKKKVKKLLKYINEELPLELEIEKFYKRGFFVTKKRY
AGLTEDGKIDVVGLEVVRRDWSEIAKETQARVLEAILKEGDVEEAVKIVKEVIEKLKRGEVPPEKLVIWK
QLTKDLSEYKATGPHVAAAKKLAKRGYKVRPGTKIGYVIVKGSGKISDRAYPYDMVDEKHKYDAEYYIDN
QVLPAVLRILEAFGYKEEDLK
>gnl|CDD|99920 cd05537, POLBc_Pol_II, DNA polymerase type-II subfamily catalytic domain. Bacteria contain five DNA polymerases (I, II, III, IV and V). DNA polymerase II (Pol II) is a prototype for the B-family of polymerases. The role of Pol II in a variety of cellular activities, such as repair of DNA damaged by UV irradiation or oxidation has been proven by genetic studies. DNA polymerase III is the main enzyme responsible for replication of the bacterial chromosome; however, In vivo studies have also shown that Pol II is able to participate in chromosomal DNA replication with larger role in lagging-strand replication
ISSPGGYVMDSKPGLYKNVLVLDFKSLYPSIIRTFLIDPLGLIEGLKAPDPEDLIPGFLGARFSREKHIL
PDLIARLWAARDEAKREKNAPLSQAIKIIMNSFYGVLGSTGCRFFDPRLASSITLRGHEIMKQTRAWIEQ
QGYQVIYGDTDSTFVWLGEELDAAEAQAIGKELASQINQWWAQKLKEEFGLESFLEIEFETHYSRFFMPT
IRGSDEGSKKRYAGLKSTDGGDELVFKGLETVRSDWTPLARQFQKELYERVFNDEPYEGFIKETVEELLA
GELDELLVYRKRLRRPLSEYTKNVPPHVQAARLADQINRELGRPRQYQWIEYVITVNGPEPLEYRTSPLD
YQHYIDKQLKPIADSILPFLG
>gnl|CDD|99921 cd05538, POLBc_Pol_II_B, DNA polymerase type-II B subfamily catalytic domain. Bacteria contain five DNA polymerases (I, II, III, IV and V). DNA polymerase II (Pol II) is a prototype for the B-family of polymerases. The role of Pol II in a variety of cellular activities, such as repair of DNA damaged by UV irradiation or oxidation has been proved by genetic studies. DNA polymerase III is the main enzyme responsible for replication of the bacterial chromosome; however, In vivo studies have also shown that Pol II is able to participate in chromosomal DNA replication with larger role in lagging-strand replication
GKFEGGYAYVFITGVLGPIVHADVASLYPSIMLAYRICPARDSLGIFLALLKYLVELRLAAKESARAAAR
PAERDAFKAKQAAFKVLINSFYGYLGTGLHAFSDPEAAAEVTRLGRELLKLMIRWLRRRGATPVEVDTDG
IYFIPPNGVDTEDEEEELVRELSSTLPKGITVEFDGRYRAMFSYKIKNYALLDYDGKLIVKGSAFRSRGI
EPFLREFLREAVRLLLQGDGAGVHDLYEDYLRRLRSHELPISDLARTETLKESPEEYLQKVRAGKRNPAA
AYEIALARPREWRAGDRVTYYVSGTGKGVSVYENCRLVADYDPAHPDENTGFYAERLLQLAARLLPF
>gnl|CDD|349776 cd05540, UreG, urease accessory protein UreG. UreG is one of the four accessory proteins of urease. Urease is an enzyme which catalyzes the decomposition of urea to form ammonia and carbon dioxide. Bacterial urease is a trimer of three subunits which are encoded by genes ureA, ureB, and ureC. Up to four accessory proteins (ureD, ureE, ureF, and ureG) are required for urease catalytical function. UreG may play an important role in nickel incorporation of the urease metallocenter. UreG is a member of the Fer4_NifH superfamily which contains an ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion
LTVGIGGPVGSGKTALVEALCRALRDKYSIAVVTNDIYTKEDAEFLIRNGALPEERIRGVETGGCPHTAI
REDASMNLAAIEELTAKFPDLDLLLVESGGDNLAATFSPELADYIIYVIDVAGGDKIPRKGGPGITQSDL
LVINKTDLAPYVGADLDVMERDAKKMRGGGPFVFTNLKTDVGLDEVIDWIL
>gnl|CDD|349405 cd05559, CAP_PI16_HrTT-1, CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor 16 and HrTT-1 protein. Human peptidase inhibitor 16 (PI16) is also called cysteine-rich secretory protein 9 (CRISP-9) or PSP94-binding protein. Mouse PI16 is also called cysteine-rich protease inhibitor. PI16 is predominantly expressed by cardiac fibroblasts and is exposed to the interstitium via a glycophosphatidylinositol (-GPI) membrane anchor. It suppresses the activation of the chemokine chemerin in the myocardium, which may be a part of the cardiac stress response. At high endothelial shear stress, PI16 is an inflammation-regulated inhibitor of matrix metalloproteinase 2 (MMP2). Also included in this subfamily is the HrTT-1 protein, a tail-tip epidermis marker in ascidians. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others
KKLLVDLHNQYRSQVSPSAANMLKMTWDTELEALAKAYARKCIWEHNPDRGRVGENLFASTGKPLDVELA
VEDWHNEKEYYNFETKTCAPGKMCGHYTQVVWANTEKIGCGSYFCETLEGVEWENATLLVCNYE
>gnl|CDD|240187 cd05560, Xcc1710_like, Xcc1710_like family, specific to proteobacteria. Xcc1710 is a hypothetical protein from Xanthomonas campestris pv. campestris str. ATCC 33913, similar to Mth938, a hypothetical protein encoded by the Methanobacterium thermoautotrophicum (Mth) genome. Their three-dimensional structures have been determined, but their functions are unknown
TITAYGDGYVEINDQRYEHSLIVTPDELITDWPVARFEDLTAAHFEALLALQPEVILLGTGERQRFPPPA
LLAPLLARGIGVEVMDTQAACRTYNILMGEGRRVVAALL
>gnl|CDD|173797 cd05561, Peptidases_S8_4, Peptidase S8 family domain, uncharacterized subfamily 4. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
VRVGMIDTGIDTAHPALSAVVIARLFFAGPGAPAPSAHGTAVASLLAGAGAQRPGLLPGADLYGADVFGR
AGGGEGASALALARALDWLAEQGVRVVNISLAGPPNALLAAAVAAAAARGMVLVAAAGNDGPAAPPLYPA
AYPGVIAVTAVDARGRLYREANRGAHVDFAAPGVDVWVAAPGGGYRYVSGTSFAAPFVTAALALLLQASP
LAPDDARARLAATAKDLGPPGRDPVFGYG
>gnl|CDD|173798 cd05562, Peptidases_S53_like, Peptidase domain in the S53 family. Members of the peptidase S53 (sedolisin) family include endopeptidases and exopeptidases. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase
GVDGTGIKIGVISDGFDGLGDAADDQASGDLPGNVNVLGDLDGGSGGGDEGRAMLEIIHDIAPGAELAFH
TAGGGELDFAAAIRALAAAGADIIVDDIGYLNEPFFQDGPIAQAVDEVVASPGVLYFSSAGNDGQSGSIF
GHAAAPGAIAVGAVDYGNTPAFGSDPAPGGTPSSFDPVGIRLPTPEVRQKPDVTAPDGVNGTVDGDGDGP
PNFFGTSAAAPHAAGVAALVLSANPGLTPADIRDALRSTALDMGEPGYDNASGSGLVDADRAVAA
>gnl|CDD|99905 cd05563, PTS_IIB_ascorbate, PTS_IIB_ascorbate: subunit IIB of enzyme II (EII) of the L-ascorbate-specific phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). In this system, EII is an L-ascorbate-specific permease with two cytoplasmic subunits (IIA and IIB) and a transmembrane channel IIC subunit. Subunits IIA, IIB, and IIC are encoded by the sgaA, sgaB, and sgaT genes of the E. coli sgaTBA operon. In some bacteria, the IIB (SgaB) domain is fused C-terminal to the IIA (SgaT) domain. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include ascorbate, chitobiose/lichenan, lactose, galactitol, mannitol, fructose, and a sensory system with similarity to the bacterial bgl system
KILAVCGSGLGSSLMLKMNVEKVLKELGIEAEVEHTDLGSAKASSADIIVTSKDLASLLADGGAKVIGLK
NIMDKNEIKEKLLEAL
>gnl|CDD|99906 cd05564, PTS_IIB_chitobiose_lichenan, PTS_IIB_chitobiose_lichenan: subunit IIB of enzyme II (EII) of the N,N-diacetylchitobiose-specific and lichenan-specific phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). In these systems, EII is either a lichenan- or an N,N-diacetylchitobiose-specific permease with two cytoplasmic domains (IIA and IIB) and a transmembrane channel IIC domain. In the chitobiose system, these subunits are expressed as separate proteins from chbA, chbB, and chbC of the chb operon (formerly the cel (cellulose) operon). In the lichenan system, these subunits are expressed from licA, licB, and licC of the lic operon. The lic operon of Bacillus subtilis is required for the transport and degradation of oligomeric beta-glucosides, which are produced by extracellular enzymes on substrates such as lichenan or barley glucan. The lic operon is transcribed from a gammaA-dependent promoter and is inducible by lichenan, lichenan hydrolysate, and cellobiose. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include chitobiose/lichenan, ascorbate, lactose, galactitol, mannitol, fructose, and a sensory system with similarity to the bacterial bgl system
KILLVCSAGMSTSILVKKMKKAAEKRGIDAEIEAVPESELEEYIDDADVVLLGPQVRYMLDEVKKKAAEY
GIPVAVIDMMDYGMMNGEKVLKQALK
>gnl|CDD|99907 cd05565, PTS_IIB_lactose, PTS_IIB_lactose: subunit IIB of enzyme II (EII) of the lactose-specific phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) found in Firmicutes as well as Actinobacteria. In this system, EII is a lactose-specific permease with two cytoplasmic domains (IIA and IIB) and a transmembrane channel IIC domain. The IIC and IIB domains are expressed as a single protein from the lac operon. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include lactose, chitobiose/lichenan, ascorbate, galactitol, mannitol, fructose, and a sensory system with similarity to the bacterial bgl system
LNVLVLCAGGGTSGLLANALNKGAKERGVPLEAAAGAYGSHYDMIPDYDLVILAPQMASYYDELKKDTDR
LGIKLVTTTGKQYIELTRDPDGALKFVLN
>gnl|CDD|99908 cd05566, PTS_IIB_galactitol, PTS_IIB_galactitol: subunit IIB of enzyme II (EII) of the galactitol-specific phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). In this system, EII is a galactitol-specific permease with two cytoplasmic domains (IIA and IIB) and a transmembrane channel IIC domain that are expressed on three distinct polypeptide chains, in contrast to other PTS sugar transporters. The three genes encoding these subunits (gatA, gatB, and gatC) comprise the gatCBA operon. Galactitol PTS permease takes up exogenous galactitol, releasing the phosphate ester into the cytoplasm in preparation for oxidation and further metabolism via a modified glycolytic pathway called the tagatose-6-phosphate glycolytic pathway. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include galactitol, chitobiose/lichenan, ascorbate, lactose, mannitol, fructose, and a sensory system with similarity to the bacterial bgl system
KKILVACGTGVATSTVVASKVKELLKENGIDVKVEQCKIAEVPSLLDDADLIVSTTKVPEDYGIPVINGL
PFLTGIGEDKVYEEILEAL
>gnl|CDD|99909 cd05567, PTS_IIB_mannitol, PTS_IIB_mannitol: subunit IIB of enzyme II (EII) of the mannitol-specific phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). In this system, EII is a mannitol-specific permease with two cytoplasmic domains (IIA and IIB) and a transmembrane channel IIC domain. The IIA, IIB, and IIC domains are expressed from the mtlA gene as a single protein, also known as the mannitol PTS permease, the mtl transporter, or MtlA. MtlA is only functional as a dimer with the dimer contacts occuring between the IIC domains. MtlA takes up exogenous mannitol releasing the phosphate ester into the cytoplasm in preparation for oxidation to fructose-6-phosphate by the NAD-dependent mannitol-P dehydrogenase (MtlD). The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include mannitol, chitobiose/lichenan, ascorbate, lactose, galactitol, fructose, and a sensory system with similarity to the bacterial bgl system
KKIVFACDAGMGSSAMGASVLRKKLKKAGLEIPVTNSAIDELPSDADLVVTHASLTDRAKKKAPQAQHLS
VDNFLNTPEYDELIERL
>gnl|CDD|99910 cd05568, PTS_IIB_bgl_like, PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory systems composed of a membrane-bound sugar-sensor (similar to BglF) and a transcription antiterminator (similar to BglG) which regulate expression of genes involved in sugar utilization. The domain architecture of the IIB-containing protein includes a region N-terminal to the IIB domain which is homologous to the BglG transcription antiterminator with an RNA-binding domain followed by two homologous domains, PRD1 and PRD2 (PTS Regulation Domains). C-terminal to the IIB domain is a domain similar to the PTS IIA domain. In this system, the BglG-like region and the IIB and IIA-like domains are all expressed together as a single multidomain protein. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include this sensory system with similarity to the bacterial bgl system, chitobiose/lichenan, ascorbate, lactose, galactitol, mannitol, and fructose systems
KKALVVCPSGIGTSRLLKSKLKKLFPEIEIIDVISLRELEEVDLDDYDLIISTVPLEDTDKPVIVVSPIL
TEEDIKKIRKFIKKL
>gnl|CDD|99911 cd05569, PTS_IIB_fructose, PTS_IIB_fructose: subunit IIB of enzyme II (EII) of the fructose-specific phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). In this system, EII (also referred to as FruAB) is a fructose-specific permease made up of two proteins (FruA and FruB) each containing 3 domains. The FruA protein contains two tandem nonidentical IIB domains and a C-terminal IIC transmembrane domain. Both IIB domains of FruA are included in this alignment. The FruB protein (also referred to as diphosphoryl transfer protein) contains a IIA domain, a domain of unknown function, and an Hpr-like domain called FPr (fructose-inducible HPr). This familiy also includes the IIB domains of several fructose-like PTS permeases including the Frv permease encoded by the frvABXR operon, the Frw permease encoded by the frwACBD operon, the Frx permease encoded by the hrsA gene, and the Fry permease encoded by the fryABC (ypdDGH) operon. FruAB takes up exogenous fructose, releasing the 1-phosphate ester in to the cytoplasm in preparation for metabolism primarily via glycolysis. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include fructose, chitobiose/lichenan, ascorbate, lactose, galactitol, mannitol, and a sensory system with similarity to the bacterial bgl system
IVAVTACPTGIAHTYMAAEALEKAAKKLGWEIKVETQGSLGIENELTAEDIAEADAVILAADVPVDDERF
AGKRVYEVSVAEAIKDAEAVIERALA
>gnl|CDD|270722 cd05570, STKc_PKC, Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALANRHPFLTGLHACFQTEDR
LYFVMEYVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADF
GMCKEGIWGGNTTSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILN
DEVLYPRWLSREAVSILKGLLTKDPARRLGCGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPR
DTSNFDPEFTSESPRLTPVDSDLLTNIDQEEFRGFSYI
>gnl|CDD|270723 cd05571, STKc_PKB, Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K
KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRL
CFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFG
LCKEEISYGATTKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILME
EVRFPSTLSPEAKSLLAGLLKKDPKKRLGGGPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETD
TRYFDEEFTAESVELTPPDRGDLLGLEEEERPHFEQFSYSAS
>gnl|CDD|270724 cd05572, STKc_cGK, Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYM
LMEYCLGGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFA
KKLGSGRKTWTFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDPMKIYNIILKGI
DKIEFPKYIDKNAKNLIKQLLRRNPEERLGYLKGGIRDIKKHKWFEGFDWEG
>gnl|CDD|270725 cd05573, STKc_ROCK_NDR_like, Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADSPWIVRLHYAF
QDEDHLYLVMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHI
KLADFGLCTKMNKSGDRESYLNDSVNTLFQDNVLARRRPHKQRRVRAYSAVGTPDYIAPEVLRGTGYGPE
CDWWSLGVILYEMLYGFPPFYSDSLVETYSKIMNWKESLVFPDDPDVSPEAIDLIRRLLCDPEDRLGSAE
EIKAHPFFKGIDWENLRESPPPFVPELSSPTDTSNFDDFEDDLLLSEYLSNGSPLLGKGKQLAFVGFTFK
>gnl|CDD|270726 cd05574, STKc_phototropin_like, Catalytic domain of Phototropin-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASF
QTSTHLCFVMDYCPGGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESG
HIMLTDFDLSKQSSVTPPPVRKSLRKGSRRSSVKSIEKETFVAEPSARSNSFVGTEEYIAPEVIKGDGHG
SAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNILKKELTFPESPPVSSEAKDLIRKLLVKDPSKRLGSK
RGASEIKRHPFFRGVNWALIRNMTPPIIPRPDDPID
>gnl|CDD|270727 cd05575, STKc_SGK, Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLLKNVKHPFLVGLHYSFQTKDK
LYFVLDYVNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDF
GLCKEGIEPSDTTSTFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILH
KPLRLRTNVSPSARDLLEGLLQKDRTKRLGSGNDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLD
LRNIDPEFTREPVPASVGKSADSVAVSASVQEADNAFDGFSYV
>gnl|CDD|270728 cd05576, STKc_RPK118_like, Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EELKAFRVLGVIDKVLLVMDTRTQETFILKGLRKSSEYSRERKTIIPRCVPNMVCLRKYIISEESVFLVL
QHAEGGKLWSYLSKFLNDKEIHQLFADLDERLAAASRFYIPEECIQRWAAEMVVALDALHREGIVCRDLN
PNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIENMYCAPEVGGISEETEACDWWSLGALLFELLTGKALV
ECHPAGINTHTTLNIPEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF
>gnl|CDD|270729 cd05577, STKc_GRK, Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCL
VLTLMNGGDLKYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLG
LAVEFKGGKKIKGRVGTHGYMAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRR
TLEMAVEYPDSFSPEARSLCEGLLQKDPERRLGCRGGSADEVKEHPFFRSLNWQRLEAGMLEPPFVPD
>gnl|CDD|270730 cd05578, STKc_Yank1, Catalytic domain of the Serine/Threonine Kinase, Yank1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HFQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQ
DEEDMYMVVDLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVH
ITDFNIATKLTDGTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEI
RAKFETASVLYPAGWSEEAIDLINKLLERDPQKRLGDLSDLKNHPYF
>gnl|CDD|270731 cd05579, STKc_MAST_like, Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ISRGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYL
VMEYLPGGDLYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLS
KVGLVRRQIKLSIQKKSNGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHA
ETPEEIFQNILNGKIEWPEDPEVSDEAKDLISKLLTPDPEKRLGAKGIEEIKNHPFFKGIDW
>gnl|CDD|270732 cd05580, STKc_PKA_like, Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSF
QDDRNLYMVMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHI
KITDFGFAKRVKDRTYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKI
LEGKIRFPSFFDPDAKDLIKRLLVVDLTKRLGNLKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRG
PGDTSNFDKY
>gnl|CDD|270733 cd05581, STKc_PDK1, Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTF
QDESKLYFVLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHI
KITDFGTAKVLGPDSSPESTKGDADSQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQ
MLTGKPPFRGSNEYLTFQKIVKLEYEFPENFPPDAKDLIQKLLVLDPSKRLGVNENGGYDELKAHPFF
>gnl|CDD|270734 cd05582, STKc_RSK_N, N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEG
KLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTD
FGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMIL
KAKLGMPQFLSPEAQSLLRALFKRNPANRLGAGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRP
DDTFYFDPEFTSRTPKDSPGVPPSANAHQLFRGFSFV
>gnl|CDD|270735 cd05583, STKc_MSK_N, N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VLGTGAYGKVFLVRKVGGHDAGKLYAMKVLKKATIVQKAKTAEHTMTERQVLEAVRQSPFLVTLHYAFQT
DAKLHLILDYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVL
TDFGLSKEFLPGENDRAYSFCGTIEYMAPEVVRGGSDGHDKAVDWWSLGVLTYELLTGASPFTVDGERNS
QSEISKRILKSHPPIPKTFSAEAKDFILKLLEKDPKKRLGAGPRGAHEIKEHPFFKGL
>gnl|CDD|270736 cd05584, STKc_p70S6K, Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LKVLGKGGYGKVFQVRKTTGSDKGKIFAMKVLKKASIVRNQKDTAHTKAERNILEAVKHPFIVDLHYAFQ
TGGKLYLILEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVK
LTDFGLCKESIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTID
KILKGKLNLPPYLTNEARDLLKKLLKRNVSSRLGSGPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLL
QSEEDVSQFDSKFTKQTPVDSPDDSTLSESANQVFQGFTYVAP
>gnl|CDD|270737 cd05585, STKc_YPK1_like, Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLY
LVLAFINGGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGL
CKLNMKDDDKTNTFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEP
LRFPDGFDRDAKDLLIGLLNRDPTKRLGYNGAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSN
FDEEFTREKPIDSVVDDSHLSESVQQQFEGWSY
>gnl|CDD|270738 cd05586, STKc_Sck1_like, Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILVRTALDESPFIVGLKFSFQTPTD
LYLVTDYMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDF
GLSKADLTDNKTTNTFCGTTEYLAPEVLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIA
FGKVRFPKDVLSDEGRSFVKGLLNRNPKHRLGAHDDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSD
TDVSNFDPEFTNASLLNANIVPWAQRPGLPGATSTPLSPSVQANFRGFTF
>gnl|CDD|270739 cd05587, STKc_cPKC, Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMD
RLYFVMEYVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIAD
FGMCKEGIFGGKTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIM
EHNVSYPKSLSKEAVSICKGLLTKHPAKRLGCGPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSP
RDAENFDKEFTKEPPVLTPTDKLVIMNIDQSEFEGFSFVN
>gnl|CDD|270740 cd05588, STKc_aPKC, Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTESR
LFFVIEFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDY
GMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDIVGSSDNPDQNTE
DYLFQVILEKPIRIPRSLSVKAASVLKGFLNKNPAERLGCHPQTGFADIQSHPFFRTIDWEQLEQKQVTP
PYKPRIESERDLENFDPQFTNEPVQLTPDDPDVIEKIDQSEFEGFEYV
>gnl|CDD|270741 cd05589, STKc_PKN, Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVNSARHPFLVNLFAC
FQTPEHVCFVMEYAAGGDLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYV
KIADFGLCKEGMGFGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVF
DSIVNDEVRYPRFLSTEAISIMRRLLRKNPERRLGASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPT
IKSPEDVSNFDEEFTSEKPVLTPPKEPRPLTEEEQALFKDFDYVAD
>gnl|CDD|270742 cd05590, STKc_nPKC_eta, Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDR
LFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADF
GMCKEGIFNGKTTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILN
DEVVYPTWLSQDAVDILKAFMTKNPTMRLGSLTLGGEEAILRHPFFKELDWEKLNRRQIEPPFRPRIKSR
EDVSNFDPDFIKEDPVLTPIEESLLPMINQDEFRNFSYTAPEL
>gnl|CDD|270743 cd05591, STKc_nPKC_epsilon, Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAAKHPFLTALHSCFQTKDR
LFFVMEYVNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADF
GMCKEGILNGKTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH
DDVLYPVWLSKEAVSILKAFMTKNPAKRLGCVASQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKIKT
KRDANNFDQDFTKEEPVLTPVDPAVIKQINQEEFRGFSFVN
>gnl|CDD|270744 cd05592, STKc_nPKC_theta_like, Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALASQHPFLTHLFCTFQTESH
LFFVMEYLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADF
GMCKENIYGENKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICN
DTPHYPRWLTKEAASCLSLLLERNPEKRLGVPECPAGDIRDHPFFKTIDWDKLERREIDPPFKPKVKSAN
DVSNFDPDFTMEKPVLTPVDKKLLASMDQEQFKGFSFTNP
>gnl|CDD|270745 cd05593, STKc_PKB_gamma, Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLK
NTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRD
LKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC
GRLPFYNQDHEKLFELILMEDIKFPRTLSADAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFTGVNWQ
DVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE
>gnl|CDD|270746 cd05594, STKc_PKB_alpha, Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SPSDNSGAEEMEVSLTKPKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVA
HTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDY
LHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWW
GLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIM
QHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMETVDNERRPHFPQFS
YSASAT
>gnl|CDD|173686 cd05595, STKc_PKB_beta, Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRL
CFVMEYANGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFG
LCKEGITDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILME
EIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVD
TRYFDDEFTAQSITITPPDRYDSLDLLESDQRTHFPQFSYSAS
>gnl|CDD|270747 cd05596, STKc_ROCK, Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NKNIENFLNRYEKPVNEITKLRMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDS
AFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMVMDYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDA
IHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDKDGLVRSDTAVGTPDYISPEVLKSQGGDGVYGRE
CDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHKNSLQFPDDVEISKDAKSLICAFLTDREVRLGRNG
IEEIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNFDDIEEDETPEETFPVPKAFVGNHLPFVGFT
YS
>gnl|CDD|270748 cd05597, STKc_DMPK_like, Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAF
QDENYLYLVMDYYCGGDLLTLLSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGH
IRLADFGSCLKLREDGTVQSSVAVGTPDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYA
ESLVETYGKIMNHKEHFSFPDDEDDVSEEAKDLIRRLICSRERRLGQNGIDDFKKHPFFEGIDWDNIRDS
TPPYIPEVTSPTDTSNFDVDDDDLRHTDSLPPPSNAAFSGLHLPFVGFTYT
>gnl|CDD|270749 cd05598, STKc_LATS, Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILAEADNEWVVKLYYSF
QDKENLYFVMDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHI
KLTDFGLCTGFRWTHDSKYYLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTP
AETQLKVINWRTTLKIPHEANLSPEAKDLILRLCCDAEDRLGRNGADEIKAHPFFAGIDWEKLRKQKAPY
IPTIRHPTDTSNFDPVDPEKLRSSDEEPTTPNDPDNGKHPEHAFYEFTFRRFF
>gnl|CDD|270750 cd05599, STKc_NDR_like, Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSF
QDEENLYLIMEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHI
KLSDFGLCTGLKKSHLAYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCR
KIMNWRETLVFPPEVPISPEAKDLIERLLCDAEHRLGANGVEEIKSHPFFKGVDWDHIRERPAPILPEVK
SILDTSNFDEFEEVDLQIPSSPEAGKDSKELKSKDWVFIGYTYK
>gnl|CDD|270751 cd05600, STKc_Sid2p_like, Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LRKRRTRLKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNS
PWLVKLLYAFQDPENVYLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPE
NFLIDSSGHIKLTDFGLASGTLSPKKIESMKIRLEEVKNTAFLELTAKERRNIYRAMRKEDQNYANSVVG
SPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSGSTPNETWANLYHWKKTLQRPVYTDPDLEFN
LSDEAWDLITKLITDPQDRLQSPEQIKNHPFFKNIDWDRLREGSKPPFIPELESEIDTSYFDDFNDEADM
AKYKDVHEKQKSLEGSGKNGGDNGNRSLFVGFTFRH
>gnl|CDD|270752 cd05601, STKc_CRIK, Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKANSPWITKLQYAF
QDSENLYLVMEYHPGGDLLSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGH
IKLADFGSAAKLSSDKTVTSKMPVGTPDYIAPEVLTSMNGGSKGTYGVECDWWSLGIVAYEMLYGKTPFT
EDTVIKTYSNIMNFKKFLKFPEDPKVSESAVDLIKGLLTDAKERLGYEGLCCHPFFSGIDWNNLRQTVPP
FVPTLTSDDDTSNFDEFEPKKTRPSYENFNKSKGFSGKDLPFVGFTFT
>gnl|CDD|270753 cd05602, STKc_SGK1, Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NPHAKPSDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFL
VGLHFSFQTTDKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENIL
LDSQGHIVLTDFGLCKENIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYS
RNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRTKRLGAKDDFTEIKNHIFFSPINWDDLINKKIT
PPFNPNVSGPNDLRHFDPEFTDEPVPNSIGQSPDSILVTASIKEAAEAFLGFSYAPPMD
>gnl|CDD|270754 cd05603, STKc_SGK2, Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEK
LYFVLDYVNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDF
GLCKEGMEPEETTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILH
KPLHLPGGKTVAACDLLQGLLHKDQRRRLGAKADFLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPAD
LRHFDPEFTQEAVPHSVGRTPDLTASSSSSSSAFLGFSYAP
>gnl|CDD|270755 cd05604, STKc_SGK3, Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTD
KLYFVLDFVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTD
FGLCKEGISNSDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENIL
HKPLVLRPGISLTAWSILEELLEKDRQLRLGAKEDFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPD
DISNFDAEFTEEMVPYSVCVSSDYSIVNASVLEADDAFVGFSYAPP
>gnl|CDD|270756 cd05605, STKc_GRK4_like, Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYE
TKDALCLVLTIMNGGDLKFHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGH
VRISDLGLAVEIPEGETIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKR
EEVDRRVKEDQEEYSEKFSEEAKSICSQLLQKDPKTRLGCRGEGAEDVKSHPFFKSINFKRLEAGLLEPP
FVPDP
>gnl|CDD|270757 cd05606, STKc_beta_ARK, Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGGDCPFIVCMTYAFQTP
DKLCFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRIS
DLGLACDFSKKKPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDR
MTLTMNVELPDSFSPELKSLLEGLLQRDVSKRLGCLGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIPP
>gnl|CDD|270758 cd05607, STKc_GRK7, Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DKYFYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYA
FETKTHLCLVMSLMNGGDLKYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDN
GNCRLSDLGLAVEVKEGKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKV
SKEELKRRTLEDEVKFEHQNFTEEAKDICRLFLAKKPENRLGSRTNDDDPRKHEFFKSINFPRLEAGLID
PPFVPD
>gnl|CDD|270759 cd05608, STKc_GRK1, Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DWFLDFRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAF
QTKTDLCLVMTIMNGGDLRYHIYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDD
DGNVRISDLGLAVELKDGQTKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGE
KVENKELKQRILNDSVTYSEKFSPASKSICEALLAKDPEKRLGFRDGNCDGLRTHPFFRDINWRKLEAGI
LPPPFVPD
>gnl|CDD|270760 cd05609, STKc_MAST, Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFE
TKRHLCMVMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIK
LTDFGLSKIGLMSLTTNLYEGHIEKDTREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLV
GCVPFFGDTPEELFGQVISDEIEWPEGDDALPDDAQDLITRLLQQNPLERLGTGGAEEVKQHPFFQDLDW
>gnl|CDD|270761 cd05610, STKc_MASTL, Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PSIEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKSPFIVHLY
YSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNE
GHIKLTDFGLSKVTLNRELNMMDILTTPSMAKPKNDYSRTPGQVLSLISSLGFNTPTPYRTPKSVRRGAA
RVEGERILGTPDYLAPELLLGKPHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGE
EELSVNAQNAIEILLTMDPTKRAGLKELKQHPLFHGVDWENLQNQTMPFIPQPDDETDTSYFEARNNAQ
>gnl|CDD|270762 cd05611, STKc_Rim15_like, Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKD
YLYLVMEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTD
FGLSRNGLEKRHNKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILS
RRINWPEEVKEFCSPEAVDLINRLLCMDPAKRLGANGYQEIKSHPFFKSINWD
>gnl|CDD|270763 cd05612, STKc_PRKX_like, Catalytic domain of PRKX-like Protein Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTE
HDQRFLYMLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHI
KLTDFGFAKKLRDRTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKI
LAGKLEFPRHLDLYAKDLIKKLLVVDRTRRLGNMKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSH
DGDTSNFDDYPE
>gnl|CDD|270764 cd05613, STKc_MSK1_N, N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NFELLKVLGTGAYGKVFLVRKVSGHDAGKLYAMKVLKKATIVQKAKTAEHTRTERQVLEHIRQSPFLVTL
HYAFQTDTKLHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDS
SGHVVLTDFGLSKEFLLDENERAYSFCGTIEYMAPEIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTV
DGEKNSQAEISRRILKSEPPYPQEMSALAKDIIQRLLMKDPKKRLGCGPNGADEIKKHPFFQKINWDDLA
AKKVPAPFKP
>gnl|CDD|270765 cd05614, STKc_MSK2_N, N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NFELLKVLGTGAYGKVFLVRKVSGHDANKLYAMKVLRKAALVQKAKTVEHTRTERNVLEHVRQSPFLVTL
HYAFQTDAKLHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDS
EGHVVLTDFGLSKEFLTEEKERTYSFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTLE
GEKNTQSEVSRRILKCDPPFPSFIGPVARDLLQKLLCKDPKKRLGAGPQGAQEIKEHPFFKGLDWEALAL
RKVNPPFRPSIRSELDVGNFAEEFTNLEPVYSPAGTPPSGARVFQGYSFIAP
>gnl|CDD|270766 cd05615, STKc_cPKC_alpha, Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SNNLDRVRLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKP
PFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLD
NVMLDSEGHIKIADFGMCKEHMVEGVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPP
FDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKHPAKRLGCGPEGERDIREHAFFRRIDWDKLEN
REIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQADFEGFSYVNPQFVHPSL
>gnl|CDD|270767 cd05616, STKc_cPKC_beta, Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCF
QTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHI
KIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELF
QSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPK
ACGRNAENFDRFFTRHPPVLTPPDQEVIRNIDQSEFEGFSFVN
>gnl|CDD|270768 cd05617, STKc_aPKC_zeta, Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFE
QASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYR
DLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMM
AGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCQPQTGFSDIKSH
TFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSEPVQLTPDDEDVIKRIDQSEFEGFEYINPLL
LSTEETV
>gnl|CDD|270769 cd05618, STKc_aPKC_iota, Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EKEAMNSRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTE
KHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHER
GIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVL
MFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHPQTG
FADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGF
EYINPLLMSAEECV
>gnl|CDD|270770 cd05619, STKc_nPKC_theta, Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KLTIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTH
LFCTFQTKENLFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLD
KDGHIKIADFGMCKENMLGDAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQD
EEELFQSIRMDNPFYPRWLEKEAKDILVKLFVREPERRLGVRGDIRQHPFFREINWEALEEREIEPPFKP
KVKSPFDCSNFDKEFLNEKPRLSFADRALINSMDQNMFRNFSFVNPKMERL
>gnl|CDD|173710 cd05620, STKc_nPKC_delta, Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEH
LFFVMEFLNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADF
GMCKENVFGDNRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRV
DTPHYPRWITKESKDILEKLFERDPTRRLGVVGNIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSN
FDREFLSEKPRLSYSDKNLIDSMDQSAFAGFSFINP
>gnl|CDD|270771 cd05621, STKc_ROCK2, Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVNKIRELQMKAEDYDVVKVIGRGAFGEVQL
VRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLV
NLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETGMVHCD
TAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLNFPDD
VEISKHAKNLICAFLTDREVRLGRNGVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDIDTSNFDDIE
DDKGDVETFPIPKAFVGNQLPFVGFTYYR
>gnl|CDD|270772 cd05622, STKc_ROCK1, Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
STGESFETRFEKIDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRM
KAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFY
AFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH
LKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYAD
SLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDT
VAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYSNRRYL
>gnl|CDD|270773 cd05623, STKc_MRCK_alpha, Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain
EVRLRQLEQLILDGPGQTNGQCFSVETLLDILICLYDECSNSPLRREKNILEYLEWAKPFTSKVKQMRLH
KEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQWITTLHYA
FQDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNG
HIRLADFGSCLKLMEDGTVQSSVAVGTPDYISPEILQAMEDGKGKYGPECDWWSLGVCMYEMLYGETPFY
AESLVETYGKIMNHKERFQFPTQVTDVSENAKDLIRRLICSREHRLGQNGIEDFKNHPFFVGIDWDNIRN
CEAPYIPEVSSPTDTSNFDVDDDCLKNCETMPPPTHTAFSGHHLPFVGFTYTSSCVLSD
>gnl|CDD|270774 cd05624, STKc_MRCK_beta, Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain
AKVRLKKLEQLLLDGPQRNESALSVETLLDVLVCLYTECSHSPLRRDKYVSEFLEWAKPFTQLVKEMQLH
RDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYA
FQDENYLYLVMDYYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNG
HIRLADFGSCLKMNDDGTVQSSVAVGTPDYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPFY
AESLVETYGKIMNHEERFQFPSHVTDVSEEAKDLIQRLICSRERRLGQNGIEDFKKHAFFEGLNWENIRN
LEAPYIPDVSSPSDTSNFDVDDDVLRNPEILPPSSHTGFSGLHLPFVGFTYTTESCFSD
>gnl|CDD|270775 cd05625, STKc_LATS1, Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSF
QDKDNLYFVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHI
KLTDFGLCTGFRWTHDSKYYQSGDHLRQDSMDFSNEWGDPENCRCGDRLKPLERRAARQHQRCLAHSLVG
TPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEAS
DLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSDLRQQSAPYIPKITHPTDTSNFDPVDPDKLWSDDD
KEGNVNDTLNGWYKNGKHPEHAFYEFTFRRFF
>gnl|CDD|173715 cd05626, STKc_LATS2, Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SMFVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSF
QDKDNLYFVMDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHI
KLTDFGLCTGFRWTHNSKYYQKGSHIRQDSMEPSDLWDDVSNCRCGDRLKTLEQRATKQHQRCLAHSLVG
TPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQPPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAV
DLITKLCCSAEERLGRNGADDIKAHPFFSEVDFSSDIRTQPAPYVPKISHPMDTSNFDPVEEESPWNDAS
GDSTRTWDTLCSPNGKHPEHAFYEFTFRRFF
>gnl|CDD|270776 cd05627, STKc_NDR2, Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYS
FQDKRNLYLIMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGH
VKLSDFGLCTGLKKAHRTEFYRNLTHNPPSDFSFQNMNSKRKAETWKKNRRQLAYSTVGTPDYIAPEVFM
QTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKVMNWKETLVFPPEVPISEKAKDLILRFCTDAE
NRIGSNGVEEIKSHPFFEGVDWEHIRERPAAIPIEIKSIDDTSNFDDFPESDILQPAPNTTEPDYKSKDW
VFLNYTYKRFEGLTQR
>gnl|CDD|270777 cd05628, STKc_NDR1, Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSF
QDKLNLYLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHV
KLSDFGLCTGLKKAHRTEFYRNLNHSLPSDFTFQNMNSKRKAETWKRNRRQLAFSTVGTPDYIAPEVFMQ
TGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMNWKETLIFPPEVPISEKAKDLILRFCCEWEH
RIGAPGVEEIKTNPFFEGVDWEHIRERPAAIPIEIKSIDDTSNFDEFPDSDILKPSVAVSNHPETDYKNK
DWVFINYTYKRFEGLTARGAIPSYMK
>gnl|CDD|270778 cd05629, STKc_NDR_like_fungal, Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSF
QDAQYLYLIMEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHI
KLSDFGLSTGFHKQHDSAYYQKLLQGKSNKNRIDNRNSVAVDSINLTMSSKDQIATWKKNRRLMAYSTVG
TPDYIAPEIFLQQGYGQECDWWSLGAIMFECLIGWPPFCSENSHETYRKIINWRETLYFPDDIHLSVEAE
DLIRRLITNAENRLGRGGAHEIKSHPFFRGVDWDTIRQIRAPFIPQLKSITDTSYFPTDELEQVPEAPAL
KQAAPAQQEESVELDLAFIGYTYKRFD
>gnl|CDD|270779 cd05630, STKc_GRK6, Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYE
TKDALCLVLTLMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGH
IRISDLGLAVHVPEGQTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKR
EEVERLVKEVPEEYSEKFSPQARSLCSMLLCKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPP
FKPDP
>gnl|CDD|173720 cd05631, STKc_GRK4, Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
TFRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYE
TKDALCLVLTIMNGGDLKFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGH
IRISDLGLAVQIPEGETVRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKR
EEVDRRVKEDQEEYSEKFSEDAKSICRMLLTKNPKERLGCRGNGAAGVKQHPIFKNINFKRLEANMLEPP
FCPDP
>gnl|CDD|270780 cd05632, STKc_GRK5, Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYA
YETKDALCLVLTIMNGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDY
GHIRISDLGLAVKIPEGESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKV
KREEVDRRVLETEEVYSAKFSEEAKSICKMLLTKDPKQRLGCQEEGAGEVKRHPFFRNMNFKRLEAGMLD
PPFVPDPRAVYCKDVLDIEQFSTVKGVNLDQTD
>gnl|CDD|270781 cd05633, STKc_GRK3, Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFI
VCMTYAFHTPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL
LDEHGHVRISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQH
KTKDKHEIDRMTLTVNVELPDSFSPELKSLLEGLLQRDVSKRLGCHGRGAQEVKEHSFFKGIDWQQVYLQ
KYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDSDQELYKNFPLVISERWQQEVAETVYEAVN
>gnl|CDD|100059 cd05635, LbH_unknown, Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity
PGAVLDAEDGPIYIGKDAVIEPFAVIEGPVYIGPGSRVKMGARIYGNTTIGPTCKIGGEVEDSIIEGYSN
KQHDGFLGHSYLGSWCNLGAGTNNSDLKNNY
>gnl|CDD|100060 cd05636, LbH_G1P_TT_C_like, Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity
KDEIEGTVEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKN
SIIMDGTKVPHLNYVGDSVLGENVNLGAGTITANLRFDDKPVKVRLKGERVDTGRRKLGAIIGDGVKTGI
NVSLNPGVKIGPGSWVYPGCVVR
>gnl|CDD|240188 cd05637, SIS_PGI_PMI_2, The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the second SIS domain
NPAKELALELAGRIPIIYGSTLYEPAAYRFKNQLNENAKYPAFYEELPEANHNEIVGWESPLSALPLAVI
LSDEDDHVRIKLRIVITKFEEGGIPYEVIESVGASPLARLLSLIYLGDLASVYLALLRGVDP
>gnl|CDD|193517 cd05638, M42, M42 Peptidases, also known as glutamyl aminopeptidase family. Peptidase M42 family proteins, also known as glutamyl aminopeptidases (GAP), are co-catalytic metallopeptidases, found in archaea and bacteria. They typically bind two zinc or cobalt atoms and include cellulase and endo-1,4-beta-glucanase (endoglucanase). Some of the enzymes exhibit typical aminopeptidase specificity, whereas others are also capable of N-terminal deblocking activity, i.e. hydrolyzing acylated N-terminal residues. GAP removes glutamyl residues from the N-terminus of peptide substrates, but is also effective against aspartyl and, to a lesser extent, seryl residues. Lactococcus lactis glutamyl aminopeptidase (PepA; aminopeptidase A) has high thermal stability and aids growth of the organism in milk. Pyrococcus horikoshii contain a thermostable de-blocking aminopeptidase member of this family, used commercially for N-terminal protein sequencing
ELLKELVEIPAISGYEAKIRNFIIEEIKDWVDEVKVDGLGNLILTLKEENAPRVLIAAHXDEVGFXVTEI
KPDGRLRVSPIGGVRPNSVEGQRVKIETRKGKTIPGVIGSVPPHLHVYDAGKAKPDWKDIVVDIGARSKE
EVEELGIRPGDFVVFDPRFQVLESKYIKSRALDDRVSVYILLELIKRLQDAELPAEVYFVASVQEEVGLR
GASTSTEAVEPDVALAVDXGAAGDGFAGQAKIGKGPSIRAKDSSGIYHPALRRWLETLAKENGIEYQVDI
YPYGGTDAGAAHLTGFGVPTLAIGVPIRYIHSFAERTHERDILHTEALLYAL
>gnl|CDD|349892 cd05639, M18, M18 peptidase aminopeptidase family. Peptidase M18 aminopeptidase family is widely distributed in bacteria and eukaryotes, but only the yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized to date. Yeast aminopeptidase I is active only in its dodecameric form with broad substrate specificity, acting on N-terminal leucine and most other amino acids. In contrast, the mammalian aspartyl aminopeptidase is highly selective for hydrolysis of N-terminal Asp or Glu residues from peptides. These enzymes have two catalytic zinc ions at the active site
AKELIDFXSKSPTPFHAVAEIARRLDEAGFVPLEEFSDWGDEXGGKYYATRNGSAIIAFRVGDDLRAERG
FNLVGAHTDSPCLRVKPNPLIEDEGFAQFGVEYYGGILKYHWLDRDLEIAGRLFKKDKGELESILVHIGD
DPVFRIPDLAPHLDKEANEISEKNKEENLXPIIGTIPPSEEEKEAVKTNHLKILNEXLGILAGVTEEDFV
SMELELVDTQSAREVGXDDEFIFAPRLDDRLCCFAALRALLSANPDKSIGVTLYDNEEIGSDSNQGAKGR
FLEKVLRRILKXQGDSPFALDEVIENSSVISADVAHAVNPNYKDVHDLNHAPKLNYGPVLKKNSNQRYAT
NAEFVALVREVANEQGVPVQVFTLRNDDGCGGTIGPILASQRGSRVIDLGPAQLAMHSIREIAGSADLFE
TVKAFRGFFE
>gnl|CDD|349893 cd05640, M28_like, M28 Zn-peptidase; uncharacterized subfamily. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions
LRAHLEQLVRMERNPHDPSAFLAAAAEYIAQELVGSGYNVTSHFFSHQEGVYANLIADLPGSYSQDKLIL
IGAHYDTVPGSPGADDNASGVAALLELARLLATLDPNHTLRFVAFDLEEYPFFARGLMGSHAYAEDLLRP
LTPIVGMLSLEMIGYYDPFPHSQAYPAGFELHFYPHMGDFIAVVGRLRSRKLVRAFKRAFRMLSDFPVES
LNLPFNGPGVPPFRRSDHSSFWDHGYPAIMVTDTAFYRNPQYHLPCDTPDTLNYKFLTRVTAGLAAGLAD
L
>gnl|CDD|349894 cd05642, M28_like, M28 Zn-peptidase-like; uncharacterized subfamily. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions
QLPDDELQAILSEVDPKRIEATIRKLVSFGTRHTLSTQTDPTRGIGAARDWIAEEFREYAAASGGRMTVE
VPSYVQGPASRIPFPVNISNVVATLKGSEDPDRVYVVSGHYDSRVSDVMDYESDAPGANDDASGVAVSME
LARIFAKHRPKATIVFTAVAGEEQGLYGSTFLAQTYRNNSVNVEGMLNNDIVGSSTGDDGTKDPHTIRLF
AQGTPAVESSEQAESRLSIGGENDSPARNLGRFIAEVASNAFTDMKVALIYRLDRYLRGGDHRPFLEAGY
PAVRFTEPNENYAHQHQDVRTEDGTVYGDLIEFVDFDYIARVAKVNLAAMWSLANAPGMPRNVTIDT
>gnl|CDD|349895 cd05643, M28_like, M28 Zn-peptidase-like. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They typically have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This protein subfamily conserves some of the metal-coordinating residues of the typically co-catalytic M28 family which might suggest binding of a single metal ion
AFETVSFISRYHRVQGSRGYVKAAEEVKELLEELGLEAKLISDIYDGGERILTPQSPISWELIEGELNET
LPILYAIIGKETPPEIAFVAHLCHPKPGANDNASGSALLLEVARVLAKLILNRPKRGICFLWVPEYTGTA
AYFAQHPDRLKKIIAVINLDMVGEDQTKTGSTLMLVPTPLSFPSYLNEELAQKLSNFTGSSLPAVRYGKE
PYEGGSDHDVFSDPGIPAVMFNTWPDRYYHTSDDTPDKLDPETLKNVGAAVLLTAYALANGEEEMAEQLA
KGYARKYLGE
>gnl|CDD|381731 cd05644, M28_like, M28 Zn-peptidase-like, uncharacterized subfamily. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They typically have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. Proteins in this subfamily conserve some of the metal-coordinating residues of the typically co-catalytic M28 family, and appear to bind a single metal (Zn) ion
YNLACRLFPICRSITGDGVRATLDILKDHIPELEIHEVPSGTKVFDWTVPDEWNIRDAYIRNPDGEKVID
FKDNNLHVVGYSEPVDKTLPLDELQPHLHTLPEQPDAIPYVTSYYKRRWGFCLSHNQRDKLPEGDYEVVI
DSTLADGSLTYGEYVLPGESEDEVLLSTYICHPSLANDNLSGPVLATFLAKWLASRERRYSYRFVFAPET
IGSITYLSRNLEHLKKHVKAGFVLTCVGDDGAYSYKPSRRGNALIDRVALHVLKHCAPGFKAYSFLPRGS
DERQYCSPGFDLPVGSLMRSKYGTYPEYHTSADNLDFISPEGLADSFQTLLEAIDVLENN
>gnl|CDD|349897 cd05645, M20_peptidase_T, M20 Peptidase T specifically cleaves tripeptides. Peptidase M20 family, Peptidase T (PepT; tripeptide aminopeptidase; tripeptidase) subfamily and similar proteins. PepT acts only on tripeptide substrates, and is thus termed a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein
LLERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEKGTLIATLPANVDGDIPAI
GFISHVDTSPDGSGKNVNPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKA
GLAEIFTALAVLKEKNIPHGDIEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASV
NIKIVGNNVHPGTAKGVGVNALSLAARIHAEVPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFD
RKQFEARKRKXKEIAKKVGKGLHPDCYIELVIEDSYYNFREKVVEHPHILDIAQQAARDCGITPELKPIR
GGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIVRIAEL
>gnl|CDD|349898 cd05646, M20_AcylaseI_like, M20 Aminoacylase-I like subfamily. Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB
EDPAVTRFREYLRINTVHPNPDYDACVEFLKRQADELGLPVRVIEVVPGKPVVVLTWEGSNPELPSILLN
SHTDVVPVFEEKWTHDPFSAHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEE
IGGHDGMEKFVKTEEFKKLNVGFALDEGLASPTEEYRVFYGERSPWWVVITAPGTPGHGSKLLENTAGEK
LRKVIESIMEFRESQKQRLKSNPNLTLGDVTTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEK
QIDEWCAEAGRGVTYEFEQKSPEKDPTSLDDSNPWWAAFKKAVKEMGLKLKPEIFPAATDSRYIRALGIP
ALGFSPMNNTPILLHDHNEFLNEDVFLRGIEIYEKIIPALA
>gnl|CDD|349899 cd05647, M20_DapE_actinobac, M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase. Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE
PIELTAALVDIPSVSGNEKPIADEIEAALRTLPHLEVIRDGNTVVARTERGLASRVILAGHLDTVPVAGN
LPSRVEEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLTLIFYDCEEVAAELNGLGRLAEEHPEWL
AADFAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLAAYEPRTVNIDGLT
YREGLNAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEIEVTDLSPGALPGLDH
PVARDLIEAVGGKVRAKYGWTDVARFSALGIPAVNFGPGDPLLAHKRDEQVPVEQITACAAILRRWL
>gnl|CDD|349900 cd05649, M20_ArgE_DapE-like, M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases. Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE
TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGFDEVEIDPMGNVIGYIGGGKKKILFDGHIDTVGIGNID
NWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLRDFAYTILVAGTVQEEDCDGVCWQYIS
KADKIKPDFVVSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFPE
APFLGRGTLTVTDIFSTSPSRCAVPDSCRISIDRRLTVGETWEGCLEEIRALPAVKKYGDDVAVSMYNYD
RPSYTGEVYESERYFPTWLLPEDHELVKALLEAYKALFGARPLIDKWTFSTNGVSIMGRAGIPCIGFGPG
AENQAHAPNEYTWKEDLVRCAAGYAAIPTSY
>gnl|CDD|349901 cd05650, M20_ArgE_DapE-like, M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases. Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE
EEIIELERDLIRIPAVNPESGGEGEKEKADYLEKKLREYGFYTLERYDAPDERGIIRPNIVAKIPGGNDK
TLWIISHLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLF
VADEEDGSEYGIQYLLNKFDLFKKDDLIIVPDFGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGIN
AFVAASNFALELDELLHEKFDEKDDLFNPPYSTFEPTKKEANVPNVNTIPGYDVFYFDCRVLPTYKLDEV
LKFVNKIISDFENSYGAGITYEIVQKEQAPPATPEDSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLR
KKGYPAVVWSTLDETAHQPNEYIRISHIVKDAKVFAEML
>gnl|CDD|349902 cd05651, M20_ArgE_DapE-like, M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases. Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE
EAIELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRKGNNVWAENGHFDEGKPTLLLNSHHDTVKPN
AGWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGPLNYNLIYAASAEEEISGKNGIESLLP
HLPPLDLAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAARNEGDNAIYKALDDIQWLRDFRFDKVSPLL
GPVKMTVTQINAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLKSEIKPRSFRLNSSAIPPDHPI
VQAAIAAGRTPFGSPTLSDQALMPFPSVKIGPGDSSRSHTADEFIELSEIEEGIDIYIELL
>gnl|CDD|349903 cd05652, M20_ArgE_DapE-like_fungal, M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases. Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal, and have been inferred by similarity as being related to both ArgE and DapE
LLSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKQPVENKDRFNVYAYPGSSRQPRVLLTSHIDTV
PPFIPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGDGMKAFNDLG
LNTWDAVIFGEPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPSSELLG
PTTLNIGRISGGVAANVVPAAAEASVAIRLAAGPPEVKDIVKEAVAGILTDTEDIEVTFTSGYGPVDLDC
DVDGFETDVVAYGTDIPYLKGDHKRYLYGPGSILVAHGPDEAITVSELEEAVEGYKKLIL
>gnl|CDD|349904 cd05653, M20_ArgE_LysK, M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase. Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved
QDAVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEAGNAVGGAGSGPPDVLLLGHIDTVPGEI
PVRVEGGVLYGRGAVDAKGPLAAMILAASALNEELGARVVVAGLVDEEGSSKGARELVRRGPRPDYIIIG
EPSGWDGITLGYRGSLLVKIRCEGRSGHSSSPERNAAEDLIKKWLEVKKWAEGYNVGGRDFDSVVPTLIK
GGESSNGLPQRAEATIDLRLPPRLSPEEAIALATALLPTCELEFIDDTEPVKVSKNNPLARAFRRAIRKQ
GGKPRLKRKTGTSDMNVLAPLWTVPIVAYGPGDSTLDHTPNEHIELAEIERAAAVLKGALEEL
>gnl|CDD|349905 cd05654, M20_ArgE_RocB, M20 Peptidase arginine utilization protein, RocB. Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases
ERLEQLLKSLVSWPSVTGTEGERSFADFLKEILKELPYFKENPSHVWQLLPPDDLGRRNVTALVKGKKPS
KRTIILISHFDTVGIEDYGELKDIAFDPDELTKAFSEYVEELDEEVREDLLSGEWLFGRGTMDMKSGLAV
HLALLEQASEDEDFDGNLLLMAVPDEEVNSRGMRAAVPALLELKKKHDLEYKLAINSEPIFPQYDGDQTR
YIYTGSIGKILPGFLCYGKETHVGEPFAGINANLMASEITARLELNADLCEKVEGEITPPPVCLKQKDLK
ESYSVQTPVRAVAYFNLFLHKKTAKELMELLRKIAEKAAEETIKAIYEEYKKYCKRPEVKLPAKVRVLTY
EELYKYAKRRFGDGFEAAIEEAEKKRAEELDDRMISIQIVDALFILCKEKGPAIVLFYAPPYYPANYLDE
NDPLLKECIEEAKAKAAEKYGEAFEVKNYFPGISDLSYLGLDDAKSGIDSFKDNTPGWGRIYSIPFKEIK
ALNIPVLNLGPYGKDAHKWTERVYKPYAFEVLPELISKIIKTLL
>gnl|CDD|349906 cd05656, M42_Frv, M42 Peptidase, endoglucanases. Peptidase M42 family, Frv (Frv Operon Protein; Endo-1 4-Beta-Glucanase; Cellulase Protein; Endoglucanase; Endo-1 4-Beta-Glucanase Homolog; Glucanase; EC. 3.2.1.4) subfamily. Frv is a co-catalytic metallopeptidase, found in archaea and bacteria, including Pyrococcus horikoshii tetrahedral shaped phTET1 (DAPPh1; FrvX; PhDAP aminopeptidase; PhTET aminopeptidase; deblocking aminopeptidase), phTET2 (DAPPh2) and phTET3 (DAPPh3), Haloarcula marismortui TET (HmTET) as well as Bacillus subtilis YsdC. All of these exhibit aminopeptidase and deblocking activities. The HmTET is a broad substrate aminopeptidase capable of degrading large peptides. PhTET2, which shares 24% identity with HmTET, is a cobalt-activated peptidase and possibly a deblocking aminopeptidase, assembled as a 12-subunit tetrahedral dodecamer, while PhTET1 can be alternatively assembled as a tetrahedral dodecamer or as an octahedral tetracosameric structure. The active site in such a self-compartmentalized complex is located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers. PhTET2 cleaves polypeptides by a nonprocessive mechanism, preferring N-terminal hydrophobic or uncharged polar amino acids. Streptococcus pneumoniae PepA (SpPepA) also forms dodecamer with tetrahedral architecture, and exhibits selective substrate specificity to acidic amino acids with the preference to glutamic acid, with the substrate binding S1 pocket containing an Arg allows electrostatic interactions with the N-terminal acidic residue in the substrate. The YsdC gene is conserved in a number of thermophiles, archaea and pathogenic bacterial species; the closest structural homolog is Thermotoga maritima FrwX (34% identity), which is annotated as either a cellulase or an endoglucanase, and is possibly involved in polysaccharide biosynthesis or degradation
ELLKKLTEAPGPSGYEEEVRDVIKEELKPYVDEVKVDGLGNLIARKKGKGEAPKVMIAAHMDEIGFMVTH
IDDDGFLRFEPIGGWDPQVLLGQRVRILTDKGEVPGVIGSKPPHLLKPEERKKVPKIDDLFIDIGASSKE
EAAEMGVRVGDPVVPDTEFTELGGNRVVGKALDNRAGCAVLLEVLRELKDEELPNDLYFVATVQEEVGLR
GAKTAAFRIDPDIAIAVDVTIAGDTPGIKHKGEVKLGKGPVIRIGDRSLIPHPKLREFLIETAEKNNIPY
QLEVSPGGGTDAGAIHLTREGVPTAVISIPARYIHSPVEVVDLRDVENAVKLLTALI
>gnl|CDD|349907 cd05657, M42_glucanase_like, M42 Peptidase, endoglucanase-like subfamily. Peptidase M42 family, glucanase (endo-1,4-beta-glucanase or endoglucanase)-like subfamily. Proteins in this subfamily are co-catalytic metallopeptidases, found in archaea and bacteria. They show similarity to cellulase and endo-1,4-beta-glucanase (endoglucanase) which typically bind two zinc or cobalt atoms. Some of the enzymes exhibit typical aminopeptidase specificity, whereas others are also capable of N-terminal deblocking activity, i.e. hydrolyzing acylated N-terminal residues. Many of these enzymes are assembled either as tetrahedral dodecamers or as octahedral tetracosameric structures, with the active site located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers
YLLDLLKELLAIPSPTGYTDEAVRYLKKELEGLGVETELTNKGALIATIPGKDSRKARALSAHVDTLGAI
VKEIKPDGRLRLTPIGGFAWNSAEGENVTIITRDGKTYTGTVLPLKASVHVYGDAPEAQERTWDNMEVRL
DEKVKSKEDVLALGIRVGDFVAFDPRPEVTESGFIKSRHLDDKASVAILLALARALKENKLKLPVDTHFL
FSNYEEVGHGASFAPPEDTDELLAVDMGPVGPGQNSDEYTVSICAKDSGGPYDYHLRKRLVNLAERNGID
YQVDVYPFYGSDASAALRAGHDVRHALIGPGVDASHGYERTHIDGIEATARLLIAYL
>gnl|CDD|349908 cd05658, M18_DAP, M18 peptidase aspartyl aminopeptidase. Peptidase M18 family, aspartyl aminopeptidase (DAP; EC 3.4.11.21) subfamily, is widely distributed in bacteria and eukaryotes. DAP cleaves only unblocked N-terminal acidic amino-acid residues. It is a cytosolic enzyme and is highly conserved; for example, the human enzyme has 51% identity to an aspartyl aminopeptidase-like protein in Arabidopsis thaliana. The mammalian DAP is highly selective for hydrolysis of N-terminal aspartate or glutamate residues from peptides. Unlike glutamyl aminopeptidase (M42), DAP does not cleave simple aminoaryl-arylamide substrates. Although there is lack of understanding of the function of this enzyme, it is thought to act in concert with other aminopeptidases to facilitate protein turnover because of their restricted specificities for the N-terminal aspartic and glutamic acid, which cannot be cleaved by any other aminopeptidases. The mammalian aspartyl aminopeptidase is possibly contributing to the catabolism of peptides, including those produced by the proteasome. It may also trim the N-terminus of peptides that are intended for the MHC class I system. In humans, DAP has been implicated in the specific function of converting angiotensin II to the vasoactive angiotensin III within the brain. Saccharomyces cerevisiae aminopeptidase I (Ape1) is involved in protein degradation in vacuoles (the yeast lysosomes) where it is transported by the unique cytoplasm-to-vacuole targeting (Cvt) pathway under vegetative growth conditions and by the autophagy pathway during starvation. Its N-terminal propeptide region, which mediates higher-order complex formation, serves as a scaffolding cargo critical for the assembly of the Cvt vesicle for vacuolar delivery. Pseudomonas aeruginosa aminopeptidase (PaAP) shows that its activity is dependent on Co2+ rather than Zn2+, and is thus a cocatalytic cobalt peptidase rather than a zinc-dependent peptidase
AKEFLDFLNASPSPFHAVAECKERLEAAGFVELSERDNWNLKPGGKYYVTRNGSSLIAFAVGGKFKPGNG
FRIVGAHTDSPCLKVKPNSKKEKEGYLQLGVETYGGGLWHTWFDRDLGLAGRVIVKDGDGKLESKLVDID
RPILRIPNLAIHLDRDVNEGFKPNKETHLVPIIGTTASKELEKTAKSASLAGKHHPLLLKLIAKELGVKP
EDILDFDLCLYDTQPAAIGGANDEFIFSPRLDNLLSSFAALQALLDSSEDNADDPNIRVVALFDNEEVGS
LSAQGADSPLLEDVLERISSALGGDPEAFERAIAKSFLLSADMAHAVHPNYPEKHEPNHRPVLNKGPVIK
VNANQRYATDAVTAALLRELAKKAGVPLQEFVVRNDSPCGSTIGPILASRLGIRTVDIGIPQLSMHSIRE
MCGTKDVYYLIKLFKAFFE
>gnl|CDD|349909 cd05659, M18_API, M18 peptidase aminopeptidase I. Peptidase M18 family, aminopeptidase I (vacuolar aminopeptidase I; polypeptidase; Leucine aminopeptidase IV; LAPIV; aminopeptidase III; aminopeptidase yscI; EC 3.4.11.22) subfamily. Aminopeptidase I is widely distributed in bacteria and eukaryotes, but only the yeast enzyme has been characterized to date. It is a vacuolar enzyme, synthesized as a cytosolic proform, and proteolytically matured upon arrival in the vacuole. The pro-aminopeptidase I (proAPI) does not enter the vacuole via the secretory pathway. In non-starved cells, it uses the cytoplasm to vacuole targeting (cvt) pathway and in cells starved for nitrogen, it is targeted to the vacuole via autophagy. Yeast aminopeptidase I is active only in its dodecameric form with broad substrate specificity, acting on all aminoacyl and peptidyl derivatives that contain a free alpha-amino group; this is in contrast to the highly selective M18 mammalian aspartyl aminopeptidase. N-terminal leucine and most other hydrophobic amino acid residues are the best substrates while glycine and charged amino acid residues in P1 position are cleaved much more slowly. This enzyme is strongly and specifically activated by zinc (Zn2+) and chloride (Cl-) ions
TEKEEIEALSESYKDFLSKAKTERECVKEIIKRAKEAGFISLEDVIEGRGLKAGDKVYAVNRGKSVALFR
IGKDPLEQGMNIIGAHIDSPRLDLKPNPLYEESGLAFFKTHYYGGIKKYQWLAIPLAIHGVIFKKDGTKV
EINIGEDENDPVFTISDLLPHLAKEQMKKKMSEAIEGENLNILVGSIPLEGEEEEKEPVKLNILKILNEK
YGIEEEDFVSAEIEVVPAGPARDVGLDRSLIGGYGQDDRICAYTALEAILEAENPEKTAIVLFVDKEEIG
STGNTGMKSRFFENTVAEIIALWGEYSELKVRRALANSRMLSADVSAAFDPNYPSVHEKRNAAYLGYGVV
FNKYTGSRGKYGANDANAEFVARLRKILNENGVIWQTAELGKVDQGGGGTIAKILAEYGMDVIDCGPAVL
SMHAPFEIASKADLYEAYLAYKAFLE
>gnl|CDD|349910 cd05660, M28_like_PA, M28 Zn-peptidase containing a protease-associated (PA) domain insert. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate
VKFLASDEFEGRAPGSEGEKKTVDYLAEQFKELGLKPAGSDGSYLQAVPLVSKIEYSTSHNVVAILPGSK
LPDEYIVLSAHWDHLGIGPPIGGDEIYNGAVDNASGVAAVLELARVFAAQDQRPKRSIVFLAVTAEEKGL
LGSRYYAANPIFPLDKIVANLNIDMIGRIGPTKDVLLIGSGSSELENILKEAAKAVGRVVDYDPNPENGS
FYRSDHYNFAKKGVPVLFFFGGYDLGDGGKKLAKAYLHTDYHKPADDVTEKWDYEGAAEDTKLIYATAWE
LANSEERPNW
>gnl|CDD|349911 cd05661, M28_like_PA, M28 Zn-peptidase containing a PA domain insert. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate
AKALHQITKRVDAENAYNHIRFLSQAIGVAGTPEELKAARYIEQQLKSLGYEVEVQPFTSHNVIATKKPD
NNKNNNDIIIVTSHYDSVVKAPGANDNASGTAVTLELARVFKKVKTDKELRFIAFGAEENGLLGSKYYVA
SLSEDEIKRTIGVFNLDMVGTSDAKAGDLYAYTIDGKPNLVTDSGAAASKRLSGVLPLVQQGSSDHVPFH
EAGIPAALFIHMDPETEPVEPWYHTPNDTVENISKERLDNALDIVGTAVYQA
>gnl|CDD|349912 cd05662, M28_like, M28 Zn-Peptidases. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins that do not contain a protease-associated (PA) domain
RLLADVKILSSDKFEGRKTGTKGAAKTRAYIIERFKQIGLLPWGDRFEHPFSYTKRFSTRQGVNVLAVIK
GSEPPTKWRVVSAHYDHLGIRGGKIYNGADDNASGVAALLALAEYFKKHPPKHNVIFAATDAEEPGLRGS
YAFVEALKVPRAQIELNINLDMISRPERNELYVEGASQFPQLTSILENVKGTCIKALHPKDTDGSIGSID
WTRASDHYPFHKAKIPWLYFGVEDHPDYHKPTDDFETIDQEFFAAVVESAVQLFKIDD
>gnl|CDD|349913 cd05663, M28_like_PA_PDZ_associated, M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ domain. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution
VGYLTSDELEGRLTGTKGEKLAADYIAQRFEELGLEPGLDNGTYFQPFEFTTGTGRNVIGVLPGKGDVAD
ETVVVGAHYDHLGYGGEGSLARGDESLIHNGADDNASGVAAMLELAAKLVDSDTSLALSRNLVFIAFSGE
ELGLLGSKHFVKNPPFPIKNTVYMINMDMVGRLRDNKLIVQGTGTSPGWEQLVQARNKATGFKLILDPTG
YGPSDHTSFYLDDVPVLHFFTGAHSDYHRPSDDSDKLNYDGMADIADFAVRIISAL
>gnl|CDD|349914 cd05664, M20_Acy1-like, M20 Peptidase aminoacylase 1 subfamily. Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine)
PDLEDLYKDFHAHPELSFQEHRTAAKIAEELRKLGFEVTTGIGGTGVVAVLRNGEGPTVLLRADMDALPV
EENTGLPYASTVRMKDWDGKEVPVMHACGHDMHVAALLGAARLLVEAKDAWSGTLIAVFQPAEETGGGAQ
AMVDDGLYDKIPKPDVVLAQHVMPGPAGTVGTRPGRFLSAADSLDITIFGRGGHGSMPHLTIDPVVMAAS
IVTRLQTIVSREVDPQEFAVVTVGSIQAGSAENIIPDEAELKLNVRTFDPEVREKVLNAIKRIVRAECAA
SGAPKPPEFTYTDSFPATVNDEDATARLAAAFREYFGEDRVVEVPPVSASEDFSILATAFGVPSVFWFIG
GIDPQRWAKAVKQKGKEIPGNHSPLFAPVIEPTLRTGVEALTVAALAFL
>gnl|CDD|349915 cd05665, M20_Acy1_IAAspH, M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase. Peptidase M20 family, bacterial and archaeal aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage
EQLVRWRRDFHRYPESGWTEFRTASLIADYLEELGYELKLGREVINADFRMGLPDDETLAAAFERAREQG
ADEELLEKMEGGFTGVVATLDTGRPGPTIALRFDIDAVDVTESEDDSHRPFKEGFASRNDGCMHACGHDG
HTAIGLGLAHALAQLKDSLSGTIKLIFQPAEEGVRGARAMAEAGVVDDVDYFLASHIGFGVPSGEVVCGP
DNFLATTKLDARFTGVSAHAGAAPEDGRNALLAAATAALNLHAIPRHGEGATRINVGVLGAGEGRNVIPA
SAELQVETRGETTAINEYMFEQAQRVIKGAATMYGVTVEIRTMGEAISAESDPELVALLREQAARVPGVQ
AVIDSAAFGGSEDATLLMARVQENGGKASYVIFGTELAAGHHNEEFDFDEAVLAIAVELLTRAVL
>gnl|CDD|349916 cd05666, M20_Acy1-like, M20 Peptidase aminoacylase 1 subfamily. Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine)
DELTAWRRDLHAHPELGFEEHRTSALVAEKLREWGIEVHRGIGGTGVVGVLRGGDGGRAIGLRADMDALP
IQEATGLPYASTHPGKMHACGHDGHTTMLLGAARYLAETRNFDGTVHFIFQPAEEGGGGAKAMIEDGLFE
RFPCDAVYGLHNMPGLPAGKFAVRPGPMMASADTFEITIRGKGGHAAMPHLGVDPIVAAAQLVQALQTIV
SRNVDPLDAAVVSVTQIHAGDAYNVIPDTAELRGTVRAFDPEVRDLIEERIREIADGIAAAYGATAEVDY
RRGYPVTVNDAEETAFAAEVAREVVGAENVDTDVRPSMGSEDFAFMLEARPGAYVFLGNGDGEGGCPLHN
PGYDFNDAILPIGASYWVRLVER
>gnl|CDD|349917 cd05667, M20_Acy1-like, M20 Peptidase aminoacylase 1 subfamily. Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine)
VEAAIQQVEPKVIEWRRDFHQNPELSNREFRTAALIAKELKSLGIEVRTGIAKTGVVGILKGGKPGPVIA
LRADMDALPVEEKTGLPFASKVKTTYLGQTVGVMHACGHDAHVAILLGAAEVLAANKDKIKGTVMFIFQP
AEEGPPEGEEGGAKLMLKEGAFKDYKPEAIFGLHVGSGLPSGQLGYRSGPIMASADRFRITVKGKQTHGS
RPWDGIDPIMASAQIIQGLQTIISRRIDLTKEPAVISIGKINGGTRGNIIPEDAEMVGTIRTFDPEMRED
IFARLKTIAEHIAKAYGATAEVEFANGYPVTYNDPALTAKMLPTLQKAVGKADLVVLPPTQTGAEDFSFY
AEQVPGMFFFLGGTPAGQEPATAPPNHSPYFIVDESALKTGVKAHIQLVLDYL
>gnl|CDD|349918 cd05668, M20_Acy1-like, M20 Peptidase aminoacylase 1 subfamily. Peptidase M20 family, uncharacterized subfamily of bacterial uncharacterized proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine)
IAELSTFRHTLHRYPELSGQEKETAKRILAFFEPLSPDEVLTGLGGHGVAFIFEGKAEGPTVLFRCELDA
LPIEEENDFAHRSKIQGKSHLCGHDGHMAIVSGLGMELSQNRPQKGKVILLFQPAEETGEGAAAVIADPK
FKEIQPDFAFALHNLPGLELGQIAVKKGPFNCASRGMIIRLKGRTSHAAHPEAGVSPAEAMAKLIVALPA
LPDAMPKFTLVTVIHAKLGEAAFGTAPGEATVMATLRAHTNETMEQLVAEAEKLVQQIADAYGLGVSLEY
TEVFAATHNHPEAWALGNQAAKNLGLPTKHIRIPFRWSEDFGQFGSVAKTALFVLGSGEDQPQLHNPDFD
FPDELIPTGVAIFKEIIQQLH
>gnl|CDD|349919 cd05669, M20_Acy1_YxeP-like, M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2. Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs
AFYQQLIEWRRYLHQHPELSNQEFETTKKIRRWLEEKGIRILDLPLKTGVVAEIGGGGPIIALRADIDAL
PIEEETGLPYASQNKGVMHACGHDFHTASLLGAAVLLKEREAELKGTVRLIFQPAEETGAGAKKVIEAGA
LDDVSAIFGFHNKPDLPVGTIGLKSGALMAAVDRFEIEIAGKGAHAAKPENGVDPIVAASQIINALQTIV
SRNISPLESAVVSVTRIHAGNTWNVIPDSAELEGTVRTFDAEVRQLVKERFEQIVEGIAAAFGAKIEFKW
HSGPPAVINDEELTDLASEVAAQAGYEVVHAEPSLGGEDFAFYQQKIPGVFAFIGSNGTYELHHPAFNPD
EEALPVAADYFAELAERLLEH
>gnl|CDD|349920 cd05670, M20_Acy1_YkuR-like, M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins. Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs
ELIKIRRDLHQIPELGLEEFKTQAYLLDVIAKLPQDNLEIKTWCETGILVYVEGSNPERTIGYRADIDAL
PIEEETGLPFASKHPGVMHACGHDGHMTIALGLLEYFAQHQPKDNLLFIFQPAEEGPGGAKRMYESGVFG
KWRPDEIYGLHVNPDLPVGTIATRSGTLFAGTSELHIDFIGKSGHAAYPHNANDMVVAAANFVTQLQTIV
SRNVDPIDGAVVTIGKIHAGTARNVIAGTAHLEGTIRTLTQEMMELVKQRVRDIAEGIELAFDCEVKVDL
GQGYYPVENDPDLTTEFIDFMKKADGVNFVEAEPAMTGEDFGYLLKKIPGTMFWLGVDSPYGLHSATLNP
DEEAILFGVNAYKGFLK
>gnl|CDD|349921 cd05672, M20_ACY1L2-like, M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily. Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. This subfamily includes Staphylococcus aureus antibiotic resistance factor HmrA that has been shown to participate in methicillin resistance mechanisms in vivo in the presence of beta-lactams. Aminoacylase 1 (ACY1) proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine)
IDELADELRELSRDIHDNPELGFEEYKAHDLLTDFLEEHGFTVTRGAYGLETAFRAEYGSSGGPTVGFLA
EYDALPGIGHACGHNLIATASVAAALALKEALKALGLPGKVVVLGTPAEEGGGGKIDLIKAGAFDDVDAA
LMVHPGPRDVAGVPSLAVDKLTVEFHGKSAHAAAAPWEGINALDAAVLAYNAISALRQQLKPTWRIHGII
TEGGKAPNIIPDYAEARFYVRAPTRKELEELRERVIACFEGAALATGCTVEIEEDEPPYADLRPNKTLAE
IYAENMEALGEEVIDDPEGVGTGSTDMGNVSYVVPGIHPYFGIPTPGAANHTPEFAEAAGTEEAHEAALK
AAKALAMTAL
>gnl|CDD|349922 cd05673, M20_Acy1L2_AbgB, M20 Peptidase Aminoacylase 1-like protein 2 aminobenzoyl-glutamate utilization protein B subfamily. Peptidase M20 family, ACY1L2 aminobenzoyl-glutamate utilization protein B (AbgB) subfamily. This group contains mostly bacterial amidohydrolases, including gene products of abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate is a natural end product of folate catabolism, and its utilization is initiated by the abg region gene product, AbgT, by enabling uptake of its into the cell in a concentration-dependent, saturable manner. It is subsequently cleaved by AbgA and AbgB (sometimes referred to as AbgAB)
IEEKRAQLTDLSDKIWEFPELSFEEFRSAALLKEALEEEGFTVERGVAGIPTAFVASYGSGGPVIAILGE
YDALPGLSQEAGVAERKPVEPGANGHGCGHNLLGTGSLGAAIAVKDYMEENNLAGTVRFYGCPAEEGGSG
KTFMVRDGVFDDVDAAISWHPASFNGVWSTSSLANISVKFKFKGISAHAAAAPHLGRSALDAVELMNVGV
NYLREHMIPEARVHYAITNGGGAAPNVVPAFAEVWYYIRAPKMEAAEELYDRVDKIAKGAAMMTETEVEY
EFISGCYNLLPNRALAEAMYENMEEVGPPKFTEEEKAFAKEIQRTLTSEDIASVSAALLEQGTEPKPLHD
FLAPLYPKEQPNAGSTDVGDVSWVVPTAQCHVACWAIGTPGHTWQNVAQGKTPIAHKGMLLAAKVMAMTA
LDLLTDPELLAEAKAEF
>gnl|CDD|349923 cd05674, M20_yscS, M20 Peptidase, carboxypeptidase yscS. Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure
IERLSGAVQIPTVSFDDMPPIDEDERWDAFYKFHDYLEKTFPLVHKTLKVEVVNEYGLLYTWEGSDPSLK
PLLLMAHQDVVPVNPETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTIIL
AFGHDEEVGGERGAGAIAELLLERYGVDGLAAILDEGGAVLEGVFLGVPFALPGVAEKGYMDVEITVHTP
GGHSSVPPKHTGIGILSEAVAALEANPFPPKLTPGNPYYGMLQCLAEHSPLPPRSLKSNLWLASPLLKAL
LASELLSTSPLTRALLRTTQAVDIINGGVKINALPETATATVNHRIAPGSSVEEVLEHVKNLIADIAVKY
GLGLSAFGGDVIYSTNGTKLLTSLLSPEPSPVSSTSSPVWQLLAGTIRQVFEQFGEDLVVAPGIMTGNTD
TRHYWNLTKNIYRFTPIRLNPEDLGRIHGVNERISIDDYLETVAFYYQLIQ
>gnl|CDD|349924 cd05675, M20_yscS_like, M20 Peptidase, carboxypeptidase yscS-like. Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis
VDLLQELIRIDTTNSGDGTGSETRAAEVLAARLAEAGIQTEIFVVESHPGRANLVARIGGTDPSAGPLLL
LGHIDVVPADASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEE
AGGENGAKWLVDNHPELFDGATFALNEGGGGSLPVGKGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRPTD
DNAITRLAEALRRLGAHNFPVRLTDETAYFAQMAELAGGEGGALMLTAVPVLDPALAKLGPSAPLLNAML
RNTASPTMLDAGYATNVLPGRATAEVDCRILPGQSEEEVLDTLDKLLGDPDVSVEAVHLEPATESPLDSP
LVDAMEAAVQAVDPGAPVVPYMSPGGTDAKYFRRLGIPGYGFAPLFLPPELDYTGLFHGVDERVPVESLY
FGVRFLDRLVK
>gnl|CDD|349925 cd05676, M20_dipept_like_CNDP, M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase. Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine
VFKYIDEHQDEFIERLREAVAIQSVSADPEKRPELIRMMEWAAERLEKLGFKVELVDIGTQTLPDGEELP
LPPVLLGRLGSDPSKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEA
YQKLGQELPVNLKFCFEGMEESGSEGLDELIEARKDTFFSDVDYVCISDNYWLGKKKPCLTYGLRGICYF
FIEVEGPNKDLHSGVFGGSVHEPMTDLIALMSSLVDSDGKILIPGIYDAVAPLTEEEWELYEKIDFDMEE
YREDIGVRRLLYDNKEELLMHRWRYPSLSIHGIEGAFSGPGAKTVIPAKVIGKFSIRLVPNMDPEVVEKQ
VTDYLEKVFAELKSPNKLKVYMGHGGKPWVADPDHPNYKAARKATKRVFGVEPDLTREGGSIPITLTFQE
ATGKNVMLLPIGAADDGAHSQNEKINRRNYIEGTKLLAAYFHELSKL
>gnl|CDD|349926 cd05677, M20_dipept_like_DUG2_type, M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats. Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex
MLNTLSEFIAFQTVSQSPTTENAEDSRRCAIFLRQLFKKLGATNCLLLPSGPGTNPIVLATFSGNSSDAK
RKRILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQEGELDNDVVFL
IEGEEESGSPGFKEVLRKNKELIGDIDWILLSNSYWLDDNIPCLNYGLRGVIHATIVVSSDKPDLHSGVD
GGVLREPTADLIKLLSKLQDPDGRILIPHFYDPVKPLTEAERARFTAIAETALIHEDTTVDSLIAKWRKP
SLTVHTVKVSGPGNTTVIPKSASASVSIRLVPDQDLDVIKQDLTDYIQSCFAELKSQNHLDIEVLNEAEP
WLGDPDNPAYQILREAVTAAWGVEPLYIREGGSIPTIRFLEKEFNAPAVQLPCGQSSDNAHLDNERLRIK
NLYKMREILSRVFNRL
>gnl|CDD|349927 cd05678, M20_dipept_like, uncharacterized M20 dipeptidase. Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine
SYREHRELVSIPNDATDEEEMRKNVDWLEQAFRKRGFKTSQLPTSGLPLLLAEKPISDARKTVLFYMHLD
GQPVDPSKWDQKSPYTPVLKRKDAAGNWEEINWDAIFSNLDPEWRVFARAAADDKGPIMMMLAALDALKA
GGIAPKFNVKIILDSEEEKGSPSLPKAVKEYKELLAADALIIMDGPAHATNKPTLTFGCRGIATATLTTY
GAKVPQHSGHYGNYAPNPAFRLSSLLASMKDDTGKVTIPGFYDGISIDEETQKILAAVPDDEESINKRLG
IAQTDKVGRNYQEALQYPSLNVRGMESGWKGDKVRTIIPEIAEAEIDIRLVPESDGPYLLDLVKAHIEKQ
GYFVTDRAPTDEERLAHDKIAKFTYRNGADAFRTDINSPIGNWLRKALTDEFGEEPIQIRMMGGTVPIAP
FVNVLDIPAIIVPMVNMDNNQHSPNENLRIGNIRTGIRTCYAILTH
>gnl|CDD|349928 cd05679, M20_dipept_like, uncharacterized M20 dipeptidase. Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine
FDSGAFLAELARRVAVPTESQEPARKPELRAYLDQEMRPRFERLGFTVHIHDNPVAGRAPFLIAERIEDP
SLPTLLIYGHGDVVPGYEGRWRDGRDPWTVTVWGERWYGRGTADNKGQHSINMAALRQVLEARGGKLGFN
VKFLIEMGEEMGSPGLRAFCFSHREALKADLFIASDGPRLAADRPTMFLGSRGGLNFELRVNLREGGHHS
GNWGGLLANPGIILANAIASLVDGKGRIKLPALKPAHLPNSVRSALADVEVGGGPDDPSIDPWWGEPGLT
AAERVFGWNTLEVLAFKTGNPDAPVNAIPGHAEAICQIRFVVGTDPDTFIPAVRAHLDANGFDGVEVTAS
QMVFAATRLDPDSPWVGWALASLQKTTGKKPALLPNLGGSLPNDVFSEVLGLPTLWVPHSYPACSQHAPN
EHILAPVMREALRVMAGLFWDLGEDGPR
>gnl|CDD|349929 cd05680, M20_dipept_like, uncharacterized M20 dipeptidase. Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine
LEELFELLRIPSVSADPAHKGDVRRAAEWLADKLTEAGFEHTEVLPTGGHPLVYAEWLGAPGAPTVLVYG
HYDVQPPDPLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEI
GSPSLPAFLEENAERLAADVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNRDLHSGSYGGAVPNPA
NALARLLASLHDEDGRVAIPGFYDDVRPLTDAEREAWAALPFDEAAFKASLGVPALGGEAGYTTLERLWA
RPTLDVNGIWGGYQGEGSKTVIPSKAHAKISMRLVPGQDPDAIADLLEAHLRAHAPPGVTLSVKPLHGGR
PYLVPTDHPALQAAERALEEAFGKPPVFVREGGSIPIVALFEKVLGIPTVLMGFGLPDDAIHAPNEKFRL
ECFHKGIEAIAHLLARL
>gnl|CDD|349930 cd05681, M20_dipept_Sso-CP2, uncharacterized M20 dipeptidase. Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus
YLEDLRDLLKIPSVSAQGRGIPETADFLKEFLRRLGAEVEIFETDGNPIVYAEFNSGDAKTLLFYNHYDV
QPAEPLELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPN
LEKFVAEHADLLKADGCIWEGGGKNPKGRPQISLGVKGIVYVELRVKTADFDLHSSYGAIVENPAWRLVQ
ALNSLRDEDGRVLIPGFYDDVRPLSEAERALIDTYDFDPEELRKTYGLKRPLQVEGKDPLRALFTEPTCN
INGIYSGYTGEGSKTILPSEAFAKLDFRLVPDQDPAKILSLLRKHLDKNGFDDIEIHDLLGEKPFRTDPD
APFVQAVIESAKEVYGQDPIVLPNSAGTGPMYPFYDALEVPVVAIGVGNAGSNAHAPNENIRIADYYKGI
EHTEELLRN
>gnl|CDD|349931 cd05682, M20_dipept_dapE, uncharacterized M20 dipeptidase. Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila
EILPALSDYIRIPNQSPLFDPEWATNGLLEKAANLIADWVKAQNIKGAKVEVVELEGRTPLLFVEIPGTE
QDDDTVLLYGHMDKQPPFTGWDEGLGPTKPVIRGDKLYGRGGADDGYAIFASLTAIKALQEQGIPHPRCV
VLIEACEESGSADLPFYLDKLKERIGNVDLVVCLDSGCGNYEQLWLTTSLRGVLGGDLTVQVLNEGVHSG
DASGIVPSSFRILRQLLSRIEDENTGEVKLDEQHCDIPAHRYEQAKKIAEILGEAVYEEFPFVSGVQPVT
TDLVQLYLNRTWKPQLSVTGADGLPPASTAGNVLRPETTLKLSLRLPPTVDAEKASAALKKLLETDPPYN
AKVTFKSDGAGSGWNAPLLSPWLAKALNEASQLFFGKPAAYQGEGGSIPFMNMLGEKFPKAQFIVTGVLG
PKSNAHGPNEFLHIPYTKKLTACVAYVLADH
>gnl|CDD|349932 cd05683, M20_peptT_like, M20 Peptidase T like enzymes specifically cleave tripeptides. Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein
NEDRLINTFLELVQIDSETLHEKEISKVLKKKFENLGLSVIEDDAGKTTGGGAGNLICTLKADKEEVPKI
LFTSHMDTVTPGINVKPPQIADGYIYSDGTTILGADDKAGIAAILEAIRVIKEKNIPHGQIQFVITVGEE
SGLVGAKALDPELIDADYGYALDSEGDVGTIIVGAPTQDKINAKIYGKTAHAGTSPEKGISAINIAAKAI
SNMKLGRIDEETTANIGKFQGGTATNIVTDEVNIEAEARSLDEEKLDAQVKHMKETFETTAKEKGAHAEV
EVETSYPGFKINEDEEVVKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERI
PIEDLYDTAVLVVEIIKE
>gnl|CDD|240189 cd05684, S1_DHX8_helicase, S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH (Asp-Glu-Ala-His) box polypeptide. The DEAH-box RNA helicases are thought to play key roles in pre-mRNA splicing and DHX8 facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. DHX8 is also known as HRH1 (human RNA helicase 1) in Homo sapiens and PRP22 in Saccharomyces cerevisiae
GKIYKGKVTSIMDFGCFVQLEGLKGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVISIQNGKISLS
MKDVDQDTG
>gnl|CDD|240190 cd05685, S1_Tex, S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has been characterized in Bordetella pertussis and Pseudomonas aeruginosa. The tex gene is essential in Bortella pertusis and is named for its role in toxin expression. Tex has two functional domains, an N-terminal domain homologous to the Escherichia coli maltose repression protein, which is a poorly defined transcriptional factor, and a C-terminal S1 RNA-binding domain. Tex is found in prokaryotes, eukaryotes, and archaea
GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIDEERGRISLS
>gnl|CDD|240191 cd05686, S1_pNO40, S1_pNO40: pNO40, S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function with an N-terminal S1 RNA binding domain, a CCHC type zinc finger, and clusters of basic amino acids representing a potential nucleolar targeting signal. pNO40 was identified through a yeast two-hybrid interaction screen of a human kidney cDNA library using the pinin (pnn) protein as bait. pNO40 is thought to play a role in ribosome maturation and/or biogenesis
PALYQIFKGEVASVTEYGAFVKIPGCRKQGLVHKSHMSSCRVDDPSEVVDVGEKVWVKVIGREMKDKMKL
SLS
>gnl|CDD|240192 cd05687, S1_RPS1_repeat_ec1_hs1, S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 1 of the Escherichia coli and Homo sapiens RPS1 (ec1 and hs1, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog
GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDPIENGEDEVKVGDEVEVYVLRVEDEEGNVVLSKR
>gnl|CDD|240193 cd05688, S1_RPS1_repeat_ec3, S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 3 (ec3) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog
EGDVVEGTVKSITDFGAFVDLGGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG
>gnl|CDD|240194 cd05689, S1_RPS1_repeat_ec4, S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 4 (ec4) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog
YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRIS
LG
>gnl|CDD|240195 cd05690, S1_RPS1_repeat_ec5, S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 5 (ec5) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog
GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG
>gnl|CDD|240196 cd05691, S1_RPS1_repeat_ec6, S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 6 (ec6) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog
GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIK
AKE
>gnl|CDD|240197 cd05692, S1_RPS1_repeat_hs4, S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 4 (hs4) of the H. sapiens RPS1 homolog. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog
GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVLSIDARGRISLSIK
>gnl|CDD|240198 cd05693, S1_Rrp5_repeat_hs1_sc1, S1_Rrp5_repeat_hs1_sc1: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 1 (hs1) and S. cerevisiae S1 repeat 1 (sc1). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
LSEGMLVLGQVKEITKLDLVISLPNGLTGYVPITNISDAYTERLEELDEESEEEDDEEELPDLEDLFSVG
QLVRCKVVSLDKSKSGKKRIELSLEPELVN
>gnl|CDD|240199 cd05694, S1_Rrp5_repeat_hs2_sc2, S1_Rrp5_repeat_hs2_sc2: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 2 (hs2) and S. cerevisiae S1 repeat 2 (sc2). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
DLVEGMVLSGCVSSVEDHGYILDIGIPGTTGFLPKKDAGNFSKLKVGQLLLCVVEKVKDDGRVVSLSADP
SKVS
>gnl|CDD|240200 cd05695, S1_Rrp5_repeat_hs3, S1_Rrp5_repeat_hs3: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 3 (hs3). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
GMLVNARVKKVLSNGLILDFLSSFTGTVDFLHLDPEKSSKSTYKEGQKVRARILYVDPSTKVVGLS
>gnl|CDD|240201 cd05696, S1_Rrp5_repeat_hs4, S1_Rrp5_repeat_hs4: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 4 (hs4). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
GAVVDSVKVTKVEPDLGAVFELKDGLLGFVHISHLSDDKVPSDTGPFKAGTTHKARIIGYSPMDGLLQLS
L
>gnl|CDD|240202 cd05697, S1_Rrp5_repeat_hs5, S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 5 (hs5) and S. cerevisiae S1 repeat 5 (sc5). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
GQVVKGTIRKLRPSGIFVKLSDHIKGLVPPMHLADVRLKHPEKKFKPGLKVKCRVLSVEPERKRLVLTL
>gnl|CDD|240203 cd05698, S1_Rrp5_repeat_hs6_sc5, S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 6 (hs6) and S. cerevisiae S1 repeat 5 (sc5). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
GLKTHGTIVKVKPNGCIVSFYNNVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK
>gnl|CDD|240204 cd05699, S1_Rrp5_repeat_hs7, S1_Rrp5_repeat_hs7: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 7 (hs7). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
GKLVDARVLKKTLNGLEVAILPEEIRAFLPTMHLSDHVSNCPLLWHCLQEGDTIPNLMCLSNYKGRIILT
KK
>gnl|CDD|240205 cd05700, S1_Rrp5_repeat_hs9, S1_Rrp5_repeat_hs9: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes Homo sapiens S1 repeat 9 (hs9). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
GDQLKLVVQDVTEDGSVMFSGGQVSGLTVLASRYHKEGVNVTPGCKLKAVILHVDFVKSQVHVSL
>gnl|CDD|240206 cd05701, S1_Rrp5_repeat_hs10, S1_Rrp5_repeat_hs10: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 10 (hs10). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
DSRHTAIVQHADKDFAIVSLATTGDLAAFPTRSHLNDTFRFDSEKLSVGQCLDVTLKDPNCLAGGPLLA
>gnl|CDD|240207 cd05702, S1_Rrp5_repeat_hs11_sc8, S1_Rrp5_repeat_hs11_sc8: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 11 (hs11) and S. cerevisiae S1 repeat 8 (sc8). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
GDLVKAKVKSVKPTQLNVQLADNVHGRIHVSEVFDEWPDGKNPLSKFKIGQKIKARVIGGHDAKTHRFLP
>gnl|CDD|240208 cd05703, S1_Rrp5_repeat_hs12_sc9, S1_Rrp5_repeat_hs12_sc9: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 12 (hs12) and S. cerevisiae S1 repeat 9 (sc9). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
GQEVTGFVNNVSKEFVWLTISPDVKGRIPLLDLSDDVSVLEHPEKKFPIGQALKAKVVGVDKEHKLLRLS
ARG
>gnl|CDD|240209 cd05704, S1_Rrp5_repeat_hs13, S1_Rrp5_repeat_hs13: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 13 (hs13). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
LEEGAVTLGMVTKVIPHSGLTVQLPFGKTGLVSIFHLSDSYTENPLEGFKPGKIVRCCILSKKDGKYQLS
LR
>gnl|CDD|240210 cd05705, S1_Rrp5_repeat_hs14, S1_Rrp5_repeat_hs14: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 14 (hs14). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
IKEGQLLRGYVSSVTKQGVFFRLSSSIVGRVLFQNVTKYFVSDPSLYNKYLPEGKLLTAKVLSVNSEKNL
VELS
>gnl|CDD|240211 cd05706, S1_Rrp5_repeat_sc10, S1_Rrp5_repeat_sc10: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes S. cerevisiae S1 repeat 10 (sc10). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
LKVGDILPGRVTKVNDRYVLVQLGNKVTGPSFITDALDDYSEALPYKFKKNDIVRACVLSVDVPNKKIAL
SLR
>gnl|CDD|240212 cd05707, S1_Rrp5_repeat_sc11, S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes S. cerevisiae S1 repeat 11 (sc11). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
GDVVRGFVKNIANNGVFVTLGRGVDARVRVSELSDSYLKDWKKRFKVGQLVKGKIVSIDPDNGRIEMT
>gnl|CDD|240213 cd05708, S1_Rrp5_repeat_sc12, S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes S. cerevisiae S1 repeat 12 (sc12). Rrp5 is found in eukaryotes but not in prokaryotes or archaea
KVGQKIDGTVRRVEDYGVFIDIDGTNVSGLCHKSEISDNRVADASKLFRVGDKVRAKVLKIDAEKKRISL
GLKASYF
>gnl|CDD|100078 cd05709, S2P-M50, Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of this family use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. The domain core structure appears to contain at least three transmembrane helices with a catalytic zinc atom coordinated by three conserved residues contained within the consensus sequence HExxH, together with a conserved aspartate residue. The S2P/M50 family of RIP proteases is widely distributed; in eukaryotic cells, they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum (ER) stress responses. In sterol-depleted mammalian cells, a two-step proteolytic process releases the N-terminal domains of sterol regulatory element-binding proteins (SREBPs) from membranes of the ER. These domains translocate into the nucleus, where they activate genes of cholesterol and fatty acid biosynthesis. It is the second proteolytic step that is carried out by the SREBP Site-2 protease (S2P) which is present in this CD superfamily. Prokaryotic S2P/M50 homologs have been shown to regulate stress responses, sporulation, cell division, and cell differentiation. In Escherichia coli, the S2P homolog RseP is involved in the sigmaE pathway of extracytoplasmic stress responses, and in Bacillus subtilis, the S2P homolog SpoIVFB is involved in the pro-sigmaK pathway of spore formation. Some of the subfamilies within this hierarchy contain one or two PDZ domain insertions, with putative regulatory roles, such as the inhibition of substrate cleavage as seen by the RseP PDZ domain
LAFILALLISVTVHELGHALVARRLGVKVARFSGGFTLNPLKHGDPYGIILIPLGGYAKPVGENPRAFKK
PRWQRLLVALAGPLANLLLALLLLLLLLLLGGLPPAPVGQAASSGLANLLAFLALINLNLAVFNLLPIPP
LDGGRILRALLEAIRGRVEERLEAYGFAILLGLLLLLLLN
>gnl|CDD|240214 cd05710, SIS_1, A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars
NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFA
KEKGATVIGLTDDEDSPLAKLADYVIVYGFEIDAVEEKYLLLYMLALRLL
>gnl|CDD|409376 cd05711, IgC2_D2_LILR_KIR_like, Second immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors, Natural killer inhibitory receptors (KIRs) and similar domains; member of Immunoglobulin Constant-2 set of IgSF domains. The members here are composed of the second immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors (LILRs), Natural killer inhibitory receptors (KIRs, also known as also known as cluster of differentiation (CD) 158), and similar proteins. This group includes LILRB1 (also known as LIR-1), LILRA5 (also known as LIR9), an activating natural cytotoxicity receptor NKp46, the immune-type receptor glycoprotein VI (GPVI), and the IgA-specific receptor Fc-alphaRI (also known as cluster of differentiation (CD) 89). LILRs are a family of immunoreceptors expressed on expressed on T and B cells, on monocytes, dendritic cells, and subgroups of natural killer (NK) cells. The human LILR family contains nine proteins (LILRA1-3, and 5, and LILRB1-5). From functional assays, and as the cytoplasmic domains of various LILRs, for example LILRB1, LILRB2 (also known as LIR-2), and LILRB3 (also known as LIR-3) contain immunoreceptor tyrosine-based inhibitory motifs (ITIMs), it is thought that LIR proteins are inhibitory receptors. Of the eight LIR family proteins, only LILRB1, and LILRB2, show detectable binding to class I MHC molecules; ligands for the other members have yet to be determined. The extracellular portions of the different LIR proteins contain different numbers of Ig-like domains for example, four in the case of LILRB1, and LILRB2, and two in the case of LILRB4 (also known as LIR-5). The activating natural cytotoxicity receptor NKp46 is expressed in natural killer cells, and is organized as an extracellular portion having two Ig-like extracellular domains, a transmembrane domain, and a small cytoplasmic portion. GPVI, which also contains two Ig-like domains, participates in the processes of collagen-mediated platelet activation and arterial thrombus formation. Fc-alphaRI is expressed on monocytes, eosinophils, neutrophils, and macrophages; it mediates IgA-induced immune effector responses such as phagocytosis, antibody-dependent cell-mediated cytotoxicity and respiratory burst. Killer cell immunoglobulin-like receptors (KIRs; also known as CD158 for human KIR) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. KIRs are a family of highly polymorphic activating and inhibitory receptors that serve as key regulators of human NK cell function. The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The major ligands for KIR are MHC class I (HLA-A, -B or -C) molecules
KPFLSAHPGPVVPSGENVTLQCHSRIGFDRFILYKEGRSPLLQFHGSGFQASFPLGPVTPAHAGTYRCYG
SYNHSPYEWSAPSDPLEIVV
>gnl|CDD|409377 cd05712, IgV_CD33, Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic acid-binding Ig-like lectins). The members here are composed of the immunoglobulin (Ig) domain at the N-terminus of Cluster of Differentiation (CD) 33 and related Siglecs (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains, an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains, followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11
WGLQMPKSVTVQEGLCVLIPCSFSYPADYWVSNPVHGYWYRGGPYPKYRPPVATNNRTREVHESTQGRFR
LLGDPGKKNCSLSISDARPEDSGKYFFRVERGDSNKYSYLSNQLSLTVT
>gnl|CDD|409378 cd05713, IgV_MOG_like, Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM)
FSVIGPTEPILALVGEDAELPCHLSPKMSAEHMEVRWFRSQFSPVVHLYRDGQDQEEEQMPEYRGRTELL
KDAIAEGSVALRIHNVRPSDEGQYTCFFRSGSFYEEATLELKVA
>gnl|CDD|409379 cd05714, Ig_CSPGs_LP_like, Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage link protein (LP), and similar domains. The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in chondroitin sulfate proteoglycans (CSPGs) and human cartilage link protein (LP). Included in this group are the CSPGs aggrecan, versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. There is considerable evidence that HA-binding CSPGs are involved in developmental processes in the central nervous system. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes
EAESAKVFSHLGGNVTLPCKFYRDPTAFGSGIHKIRIKWTKLTSDSGYLKEVDVLVAMGNVVYHKKTYGG
RVSVPLKPGSDSDASLVITDLTASDYGLYRCEVIEGIEDDQDVVALDVQGVVF
>gnl|CDD|409380 cd05715, IgV_P0-like, Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins. The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain
MEVYTPRELNVLNGSDVRLTCTFTSCYTVGDAFSVTWTYQPEGGNTTESMFHYSKGKPYILKVGRFKDRV
SWAGNPSKKDASIVISNLQFSDNGTYTCDVKNPPDIVGGHGEIRLYV
>gnl|CDD|409381 cd05716, IgV_pIgR_like, Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others
SVGPEVVTGVEGGSVTIQCPYPPKYASSRKYWCKWGSEGCQTLVSSEGVVPGGRISLTDDPDNGVFTVTL
NQLRKEDAGWYWCGVGDDGDRGLTVQVKLV
>gnl|CDD|409382 cd05717, IgV_1_Necl_like, First (N-terminal) immunoglobulin (Ig)-like domain of the nectin-like molecules; member of the V-set of Ig superfamily (IgSF) domains. The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 (CADM3)), Necl-2 (CADM1), Necl-3 (CADM2), and similar proteins. At least five nectin-like molecules have been identified (Necl-1 to Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1, Necl-2, and Necl-3 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue, and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues and is a putative tumour suppressor gene which is downregulated in aggressive neuroblastoma. Necl-3 accumulates in central and peripheral nervous system tissue and has been shown to selectively interact with oligodendrocytes. This group also contains Class-I MHC-restricted T-cell-associated molecule (CRTAM), whose expression pattern is consistent with its expression in Class-I MHC-restricted T-cells
PHTQDVTVVEGETLTLKCQVSLRDDSSLQWLNPNGQTIYFNDKRALRDSRYQLLNHSASELSISVSNVTL
SDEGVYTCLHYTDPVSTKKVTVTV
>gnl|CDD|409383 cd05718, IgV_1_PVR_like, First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains. The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226)
QRVQVPTEVTGFLGGSVTLPCSLTSPGTTKITQVTWMKIGAGSSQNVAVFHPQYGPSVPNPYAERVEFLA
ARLGLRNATLRIRNLRVEDEGNYICEFATFPQGNRQGTTWLRV
>gnl|CDD|409384 cd05719, IgC1_2_PVR_like, Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (Necl-5)) and similar proteins. Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), these result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted, while CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the second Ig-like domain of nectin-1, also known as poliovirus receptor related protein(PVRL)1 or CD111
PTNSLEGGPALLIGGEPTLVATCISANGKPPASVTWETDLKGEASTTQVRGSNGTVTVTSRYRLVPSREA
DGQPLTCVVEHPSLEKDQRISVTLNV
>gnl|CDD|409385 cd05720, IgV_CD8_alpha, Immunoglobulin (Ig)-like variable (V) domain of Cluster of Differentiation (CD) 8 alpha chain. The members here are composed of the immunoglobulin (Ig)-like variable domain of the Cluster of Differentiation (CD) 8 alpha. The CD8 glycoprotein plays an essential role in the control of T-cell selection, maturation, and the T-cell receptor (TCR)-mediated response to peptide antigen. CD8 is comprised of alpha and beta subunits and is expressed as either an alpha/alpha or alpha/beta dimer. Both dimeric isoforms can serve as a coreceptor for T cell activation and differentiation, however they have distinct physiological roles, different cellular distributions, unique binding partners, etc. Each CD8 subunit is comprised of an extracellular domain containing a V-type Ig-like domain, a single pass transmembrane portion, and a short intracellular domain. The Ig domain of CD8 alpha binds to antibodies. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology
FRMSPRKRDAQLGQKVELVCEVLNSVPQGCSWLFQPRGSAPQPTFLLYLSSSNKTKWAEGLDSKRFSGSR
SGSSYVLTLKDFRKEDEGYYFCSVISNSVLYFSSFVPVFL
>gnl|CDD|409386 cd05721, IgV_CTLA-4, Immunoglobulin Variable (IgV) domain of cytotoxic T lymphocyte-associated antigen 4 (CTLA-4). The members here are composed of the variable(v)-type immunoglobulin (Ig) domain found in cytotoxic T lymphocyte-associated antigen 4 (CTLA-4). CTLA-4 is involved in the regulation of T cell response, acting as an inhibitor of intracellular signaling. CTLA-4 is similar to CD28, a T cell co-receptor protein that recognizes the B7 proteins (CD80 and CD86). CD28 binding of the B7 proteins occurs after the presentation of antigen to the T cell receptor (TCR) via the peptide-MHC complex on the surface of an antigen presenting cell (APC). CTLA-4 also binds the B7 molecules with a higher affinity than does CD28. The B7/CTLA-4 interaction generates inhibitory signals down-regulating the response, and may prevent T cell activation by weak TCR signals. CD28 and CTLA-4 then elicit opposing signals in the regulation of T cell responsiveness and homeostasis. T cell activation leads to increased CTLA-4 gene expression and trafficking of CTLA-4 protein to the cell surface. CTLA-4 is not detected on the T-cell surface until 24 hours after activation. Covalent dimerization of CTLA-4 has been shown to be required for its high binding avidity, although each CTLA-4 monomer contains a binding site for CD80 and CD86
HVAQPAVVLASSRGVASFVCEYASSGNATEVRVTVLRQADSQMTEVCAATYTMGNELTFLDDSICTGTSS
GNQVNLTIQGLRAMDTGLYICKVELMYPPPYYVGMGNGTQIYVID
>gnl|CDD|409387 cd05722, IgI_1_Neogenin_like, First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
ELYFLSEPSDIVAMRGGPVVLNCSAESDPPPKIEWKKDGVLLNLVSDERRQQLPNGSLLITSVVHSKHNK
PDEGFYQCVAQNESLGSIVSRTARVTV
>gnl|CDD|409388 cd05723, IgI_4_Neogenin_like, Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
LKKPSNIYAHESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHNLQVLGLVKSDEGFYQCIAE
NDVGNAQASAQLII
>gnl|CDD|409389 cd05724, IgI_2_Robo, Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
RVEPSDTQVAVGEMAVLECSPPRGHPEPTVSWRKDGQPLNLDNERVRIVDDGNLLIAEARKSDEGTYKCV
ATNMVGERESRAARLSV
>gnl|CDD|409390 cd05725, IgI_3_Robo, Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEILDDHSLKIRKVTAGDMGSYTCVAEN
MVGKIEASATLTV
>gnl|CDD|409391 cd05726, IgI_4_Robo, Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains. Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
QFVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNLLFPYQPPQPSSRFSVSPTGDLTITNVQRS
DVGYYICQALNVAGSILAKAQLEVTDVL
>gnl|CDD|409392 cd05727, Ig2_Contactin-2-like, Second Ig domain of the neural cell adhesion molecule contactin-2, and similar domains. The members here are composed of the second Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes
ERDEVKVKEGWGVVLFCDPPPHYPDLSYRWLLNEFPNFIPEDGRRFVSQTNGNLYIAKVEASDRGNYSCF
VSSPSSTKSVFSKFIPLR
>gnl|CDD|143205 cd05728, Ig4_Contactin-2-like, Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains. The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes
EWLKVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAGDLRITKLSLSDSGMYQCVA
ENKHGTIYASAELAV
>gnl|CDD|409393 cd05729, IgI_2_FGFR_like, Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains. The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors
PRFTDTEKMEEREHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWSLIIERAIP
RDKGKYTCIVENEYGSINHTYDVDV
>gnl|CDD|143207 cd05730, IgI_3_NCAM-1, Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains. The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain
PPTIRARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNEDGSEMTILDVDKLDE
AEYTCIAENKAGEQEAEIHLKVFAK
>gnl|CDD|409394 cd05731, Ig3_L1-CAM_like, Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains. The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin
SESSTMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGRTKFENFNKTLKIENVSEADSGEYQCTASNT
MGSARHTISVTVE
>gnl|CDD|409395 cd05732, IgI_NCAM-1_like, Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins. The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains
VQPKITYLENQTAVELEQITLTCEAEGDPIPEITWRRATRGISFEEGDLDGRIVVRGHARVSSLTLKDVQ
LTDAGRYDCEASNRIGGDQQSMYLEV
>gnl|CDD|409396 cd05733, IgI_L1-CAM_like, Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the first immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lacks a C" strand
PTITEQSPKDYIVDPRDNITIKCEAKGNPQPTFRWTKDGKFFDPAKDPRVSMRRRSGTLVIDNHNGGPED
YQGEYQCYASNELGTAISNEIRLV
>gnl|CDD|409397 cd05734, Ig_DSCAM, Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM). The members here are composed of the immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion
PPRFVVQPNDQDGIYGKAVVLNCSADGYPPPTIVWKHSKGSGVPQFQHIVPLNGRIQLLSNGSLLIKHVL
EEDSGYYLCKVSNDVGADISKSMYLTV
>gnl|CDD|409398 cd05735, Ig_DSCAM, Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM). The members here are composed of the immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion
KIPAMITSYPNTTLATKGQKKEMSCTAHGEKPIIVRWEKEDTIINPSEMSRYLVTTKEVGDEVISTLQIL
PTVREDSGFFSCHAINSYGEDRGIIQLTVQE
>gnl|CDD|409399 cd05736, IgI_2_Follistatin_like, Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling
PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGA
YTCIAKNEGGVDEDISSLFVEDS
>gnl|CDD|319300 cd05737, IgI_Myomesin_like_C, C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity
ARVLGGLPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVYFTINGVSSEDS
GKYGLVVKNKYGSETSDVTVSV
>gnl|CDD|409400 cd05738, IgI_2_RPTP_IIa_LAR_like, Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; member of the I-set of IgSF domains. The members here are composed of the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains
IIDMGPQLKVVEKARTATMLCAASGNPDPEISWFKDFLPVDTATSNGRIKQLRSGALQIENSEESDQGKY
ECVATNSAGTRYSAPANLYVR
>gnl|CDD|409401 cd05739, IgI_3_RPTP_IIa_LAR_like, Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F (also known as LAR), type IIa; member of the I-set of IgSF domains. The members here are composed of the third immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains. Included in this group is Drosophila LAR (DLAR)
SIPPSNHEVMPGGSVNLTCVAVGAPMPYVKWMKGGEELTKEDEMPVGRNVLELTNIYESANYTCVAISSL
GMIEATAQVTVK
>gnl|CDD|409402 cd05740, IgI_hCEACAM_2_4_6_like, Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) domains 2, 4, and 6, and similar domains. The members here are composed of the second, fourth, and sixth immunoglobulin (Ig)-like domains in human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. The CEA family is a group of anchored or secreted glycoproteins expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions; it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface
KPFISSNNSNPVEDKDAVTLTCEPETQNTSYLWWFNGQSLPVTPRLTLSNGNRTLTLLNVTREDAGAYQC
EISNPVSANRSDPVTLDVI
>gnl|CDD|409403 cd05741, IgV_CEACAM_like, Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) and similar proteins. The members here are composed of the immunoglobulin (Ig)-like domain in carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) and related domains. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions: it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two (D1, D4) or four (D1-D4) Ig-like domains on the cell surface. This family corresponds to the D1 Ig-like domain. Also belonging to this group is the N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family, CD84-like family. The SLAM family is a group of immune-cell specific receptors that can regulate both adaptive and innate immune responses. SLAM family proteins are organized as an extracellular domain with having two or four Ig-like domains, a single transmembrane segment, and a cytoplasmic region having Tyr-based motifs. The extracellular domain is organized as a membrane-distal Ig variable (IgV) domain that is responsible for ligand recognition and a membrane-proximal truncated Ig constant-2 (IgC2) domain
SSEQFYGAEGKNVLLLVPNLQTPLKSVSWYKGKQVSRNDEIAEYENSSDEFRAGSAFSGREYIYTNGSLL
IQNITLSDTGFYTLESTNIGGKTESATFQLHV
>gnl|CDD|409404 cd05742, IgI_VEGFR_like, Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and similar proteins; member of the I-set of IgSF domains. The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and related proteins. The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1) and VEGFR-3 (Flt-4). VEGF-A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF; VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic, and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth. This group also contains alpha-type platelet-derived growth factor receptor precursor (PDGFR)-alpha (CD140a), and PDGFR-beta (CD140b). PDGFRs alpha and beta have an extracellular component with five Ig-like domains, a transmembrane segment, and a cytoplasmic portion that has protein tyrosine kinase activity
SDLELSPNAEPTVLPQGETLVLNCTANVNLNEVVDFQWTYPSEKEGKLALLKPDIKVDWSEPGEFVSTLT
IPEATLKDSGTYTCAARSGVMKKEKQTSVSVH
>gnl|CDD|143220 cd05743, Ig_Perlecan_like, Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins. The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities
GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGMVFG
IPDGILTV
>gnl|CDD|409405 cd05744, IgI_Myotilin_C_like, Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAG
IYTCIARNRAGENSFNAELVV
>gnl|CDD|143222 cd05745, Ig3_Peroxidasin, Third immunoglobulin (Ig)-like domain of peroxidasin. The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self
EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVA
QLTV
>gnl|CDD|143223 cd05746, Ig4_Peroxidasin, Fourth immunoglobulin (Ig)-like domain of peroxidasin. The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self
VQIPCSAQGDPEPTITWNKDGVQVTESGKFHISPEGYLAIRDVGVADQGRYECVARNTIGYASVSMVLS
>gnl|CDD|143224 cd05747, IgI_Titin_like, Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
TLPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSD
EGNYTVVVENSEGKQEAQFTLT
>gnl|CDD|409406 cd05748, Ig_Titin_like, Immunoglobulin (Ig)-like domain of titin and similar proteins. The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains
TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNS
AGEKSATINVKV
>gnl|CDD|409407 cd05749, IgI_2_Axl_Tyro3_like, Second immunoglobulin (Ig)-like domain of Axl/Tyro3 family receptor tyrosine kinases (RTKs); member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the second immunoglobulin (Ig)-like domain in the Axl/Tyro3 family of receptor tyrosine kinases (RTKs). This family includes Axl (also known as Ark, Ufo, and Tyro7), Tyro3 (also known as Sky, Rse, Brt, Dtk, and Tif), and Mer (also known as Nyk, c-Eyk, and Tyro12). Axl/Tyro3 family receptors have an extracellular portion with two Ig-like domains followed by two fibronectin-types III (FNIII) domains, a membrane-spanning single helix, and a cytoplasmic tyrosine kinase domain. Axl, Tyro3, and Mer are widely expressed in adult tissues, though they show higher expression in the brain, lymphatic and vascular systems, and testis. Axl, Tyro3, and Mer bind the vitamin K dependent protein Gas6 with high affinity, and in doing so activate their tyrosine kinase activity. Axl/Gas6 signaling may play a part in cell adhesion processes, prevention of apoptosis, and cell proliferation
HFTVEPEDLAVTANTPFNLTCQAVGPPEPVEILWWQGGSPLGGPPAPSPSVLNVPGLNETTKFSCEAHNA
KGLTSSRTATVT
>gnl|CDD|409408 cd05750, Ig_Pro_neuregulin, Immunoglobulin (Ig)-like domain in neuregulins. The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage
PKLKEMKSQTVQEGSKLVLKCEATSENPSPRYRWFKDGKELNRKRPKNIKIRNKKKNSELQINKAKLEDS
GEYTCVVENILGKDTVTGNVTV
>gnl|CDD|409409 cd05751, IgC2_D1_LILR_KIR_like, First immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors (LILRs), Natural killer inhibitory receptors (KIRs) and similar domains; member of Immunoglobulin Constant-2 set of IgSF domains. The members here are composed of the first immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors (LILRs) and Natural killer inhibitory receptors (KIRs, also known as also known as cluster of differentiation (CD) 158), and similar proteins. This group includes LILRB1 (also known as LIR-1), LILRA5 (also known as LIR9), an activating natural cytotoxicity receptor NKp46, the immune-type receptor glycoprotein VI (GPVI), and the IgA-specific receptor Fc-alphaRI (also known as cluster of differentiation (CD) 89). LILRs are a family of immunoreceptors expressed on expressed on T and B cells, on monocytes, dendritic cells, and subgroups of natural killer (NK) cells. The human LILR family contains nine proteins (LILRA1-3, and 5, and LILRB1-5). From functional assays, and as the cytoplasmic domains of various LILRs, for example LILRB1, LILRB2 (also known as LIR-2), and LILRB3 (also known as LIR-3) contain immunoreceptor tyrosine-based inhibitory motifs (ITIMs), it is thought that LIR proteins are inhibitory receptors. Of the eight LIR family proteins, only LILRB1, and LILRB2, show detectable binding to class I MHC molecules; ligands for the other members have yet to be determined. The extracellular portions of the different LIR proteins contain different numbers of Ig-like domains for example, four in the case of LILRB1, and LILRB2, and two in the case of LILRB4 (also known as LIR-5). The activating natural cytotoxicity receptor NKp46 is expressed in natural killer cells, and is organized as an extracellular portion having two Ig-like extracellular domains, a transmembrane domain, and a small cytoplasmic portion. GPVI, which also contains two Ig-like domains, participates in the processes of collagen-mediated platelet activation and arterial thrombus formation. Fc-alphaRI is expressed on monocytes, eosinophils, neutrophils, and macrophages; it mediates IgA-induced immune effector responses such as phagocytosis, antibody-dependent cell-mediated cytotoxicity and respiratory burst. Killer cell immunoglobulin-like receptors (KIRs; also known as CD158 for human KIR) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. KIRs are a family of highly polymorphic activating and inhibitory receptors that serve as key regulators of human NK cell function. The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The major ligands for KIR are MHC class I (HLA-A, -B or -C) molecules
KPFIWAEPSSVIPLEKSVTIRCQGTPEAFLYQLEKEGNSTETVIPKKPQKKAEFIIPHMNSRTAGRYRCR
YRKGAGWSEPSDLLELVV
>gnl|CDD|409410 cd05752, Ig1_FcgammaR_like, First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains. The members here are composed of the first immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity
AVVSLDPPWTTVFQGEKVTLTCQGFYSPEQNSTQWYHNGTLISSTSSSYRIVAATVNDSGEYRCQTQGSS
LSDPVHLEV
>gnl|CDD|409411 cd05753, Ig2_FcgammaR_like, Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains. The members here are composed of the second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity
WLLLQAPSAVVFEGEPLTLRCHGWKDKKVHKVTYYKDGKALKFSYENSNFSIPQATLSDSGSYHCSGTVR
IKRRSSESVNITV
>gnl|CDD|409412 cd05754, IgI_Perlecan_like, Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
IQVTVEEPRSQEVRPGADVSFICRAKSKSPAYTLVWTRVNGTLPSRAMDFNGILTIRNVQLSDAGTYVCT
GSNMLDTDEATATLY
>gnl|CDD|409413 cd05755, IgC2_2_ICAM-1_like, Second immunoglobulin (Ig)-like C2-set domain of intercellular cell adhesion molecule 1 (ICAM-1), and similar domains. The members here are composed of the second immunoglobulin (Ig)-like domain of intercellular cell adhesion molecule 1 (ICAM-1; also known as domain of cluster of differentiation (CD) 54) and similar proteins. During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. ICAM-1 may be involved in organ targeted tumor metastasis. The interaction of ICAM-1 with leukocyte function-associated antigen-1 (LFA-1) plays a part in leukocyte-endothelial cell recognition. This group also contains ICAM-2 which also interacts with LFA-1. Transmigration of immature dendritic cells across resting endothelium is dependent on the interaction of ICAM-2 with, yet unidentified, ligand(s) on the dendritic cells. ICAM-1 has five Ig-like domains and ICAM-2 has two. ICAM-1 may also act as host receptor for viruses and parasites. The structures of this group show that the second Ig domain lacks a D strand and thus belonging to the C2-set of the IgSF
PPERVELTPLPSWQPVGKNFTLRCRVPGGAPRASLTLVLLRGNETLHRETFGGAAPAPQPAEATFTVLAR
REDHGANFSCLAELDLRPQGLNLFHNHSAPR
>gnl|CDD|409414 cd05756, Ig1_IL1R_like, First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains. The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta
DEWGEDIKILVVLEGEPDVIKCPLFPNFLAQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALL
EDSGNYYCVVRNSTYCSKVSISLEVV
>gnl|CDD|409415 cd05757, Ig2_IL1R-like, Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains. The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2
PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCK
FTYTHNGKQYNVTRTISLTVTE
>gnl|CDD|319310 cd05758, IgI_5_KIRREL3-like, Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar domains; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (also known as Neph1), Kirrel2 (also known as Neph3), and Drosophila RST (also known as irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development
GPPIITAEATQPAILGEKARLECLVFSSPPPDRIVWSWDEGFLESGSSGRFSVETFPTEPGVISVLHISG
TQRSDFQTSFNCSAWNRFGEGTAIVSLG
>gnl|CDD|409416 cd05759, IgI_2_KIRREL3-like, Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar domains; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development
DPVIEGGPVISLQAGVPYNLTCRARGAKPAAEIIWFRDGEQLEGAVYSKELLKDGKRETTVSTLLITPSD
LDTGRTFTCRARNEAIPNGKETSITLDV
>gnl|CDD|409417 cd05760, Ig2_PTK7, Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7. The members here are composed of the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines
PVVLKHPASAAEIQPSSRVTLRCHIDGHPRPTYQWFRDGTPLSDGQGNYSVSSKERTLTLRSAGPDDSGL
YYCCAHNAFGSVCSSQNFTLSIIDE
>gnl|CDD|409418 cd05761, IgI_2_Necl-1-4, Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of the I-set of Ig superfamily domains. The members here are composed of the second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 or CADM3), Necl-2 (also known as CADM1), Necl-3 (also known as CADM2) and Necl-4 (also known as CADM4). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues, and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression
LGVPEKPVITGFTSPVVEGDEITLTCTTSGSKPAADIRWFKNDKELKGVKEVQESGAGKTFTVTSTLRFR
VDRDDDGVAVICRVDHESLTSTPKQTQQVLEV
>gnl|CDD|409419 cd05762, IgI_8_hMLCK_like, Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains. The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II
PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCG
CYTLEVENKLGSRQAQVNLTVVDKPDPPA
>gnl|CDD|409420 cd05763, IgI_LRIG1-like, Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains. The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains
SFTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGV
YSCTAQNSAGSISANATLTVL
>gnl|CDD|409421 cd05764, IgI_SALM5_like, Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains. This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand
PLITRHTHELRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNSSRTLVYDNGTLDILITTVKDTGAFT
CIASNPAGEATARVELHI
>gnl|CDD|409422 cd05765, IgI_3_WFIKKN-like, Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKQVPGKENLIMRPNHVRGNVVVTNIGQLVIYNAQP
QDAGLYTCTARNSGGLLRANFPLSV
>gnl|CDD|409423 cd05766, IgC1_MHC_II_beta, Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class II beta chain. MHC class II molecules play a key role in the initiation of the antigen-specific immune reponse. These molecules have been shown to be expressed constitutively on the cell surface of professional antigen-presenting cells (APCs), including B-lymphocytes, monocytes, and macrophages in both humans and mice. The expression of these molecules has been shown to be induced in nonprofessional APCs such as keratinocyctes and they are also expressed on the surface of activated human T cells and on T cells from other species. The MHC II molecules present antigenic peptides to CD4(+) T-lymphocytes. These peptides derive mostly from proteolytic processing via the endocytic pathway of antigens internalized by the APC. These peptides bind to the MHC class II molecules in the endosome before they are transported to the cell surface. MHC class II molecules are heterodimers, comprised of two similarly-sized membrane-spanning chains, alpha and beta. Each chain has two globular domains (N- and C-terminal) and a membrane-anchoring transmembrane segment. The two chains form a compact four-domain structure. The peptide-binding site is a cleft in the structure
RVQPSVKVSPTKTGPLEHPNLLVCSVTGFYPAEIEVKWFRNGQEETAGVVSTELIPNGDWTFQILVMLET
TPRRGDVYTCQVEHSSLQSPLTVDWR
>gnl|CDD|409424 cd05767, IgC1_MHC_II_alpha, Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin (Ig) domain of the major histocompatibility complex (MHC) class II alpha chain. MHC class II molecules play a key role in the initiation of the antigen-specific immune reponse. These molecules have been shown to be expressed constitutively on the cell surface of professional antigen-presenting cells (APCs), including B-lymphocytes, monocytes, and macrophages in both humans and mice. The expression of these molecules has been shown to be induced in nonprofessional APCs such as keratinocyctes, and they are also expressed on the surface of activated human T cells and on T cells from other species. The MHC II molecules present antigenic peptides to CD4(+) T-lymphocytes. These peptides derive mostly from proteolytic processing via the endocytic pathway, of antigens internalized by the APC. These peptides bind to the MHC class II molecules in the endosome before they are transported to the cell surface. MHC class II molecules are heterodimers, comprised of two similarly-sized membrane-spanning chains, alpha and beta. Each chain had two globular domains (N- and C-terminal), and a membrane-anchoring transmembrane segment. The two chains form a compact four-domain structure. The peptide-binding site is a cleft in the structure
VPPEVTVFPKSPVELGEPNTLICFVDNFFPPVINVTWLRNGQPVTDGVSETVFLPREDHSFRKFSYLPFT
PSEGDIYDCRVEHWGLEEPLLKHWE
>gnl|CDD|409425 cd05768, IgC1_CH3_IgAGD_CH4_IgAEM, CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, and delta chains, and CH4 domain (fourth constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, epsilon, and mu chains; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the third and fourth immunoglobulin constant domain (IgC) of alpha, delta, gamma and alpha, epsilon, and mu heavy chains, respectively. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns
PSVYLLPPPEEELSLNETVTLTCLVKGFYPEDIFVSWLQNGEPLPSADYKTTAPVPESDGSFFVYSKLNV
STADWNSGDVFSCVVGHEALPLQFTQKSIDKSPGK
>gnl|CDD|409426 cd05769, IgC1_TCR_beta, T cell receptor (TCR) beta chain constant immunoglobulin domain; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the T cell receptor (TCR) beta chain constant immunoglobulin domain. TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. This group includes the variable domain of the beta chain. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The antigen binding site is formed by the variable domains of the alpha and beta chains, located at the N-terminus of each chain. Alpha/beta TCRs recognize antigens differently from gamma/delta TCRs
TPPTVALFPPSEAEIRNKRKATLVCLATGFYPDHVSLSWKVNGKEVKDGVATDPQALRENTSTYSLSSRL
RVSATEWFNPRNTFTCIVKFYGGTDTDTWTQGIAGPVTCGVSAEEL
>gnl|CDD|409427 cd05770, IgC1_beta2m, Class I major histocompatibility complex (MHC) beta-2-microglobulin; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin-like domain in beta-2-microglobulin (beta2m). Beta2m is the non-covalently bound light chain of the human class I major histocompatibility complex (MHC-I). Beta2m is structured as a beta-sandwich domain composed of two facing beta-sheets (four stranded and three stranded), that is typical of the C-type immunoglobulin superfamily. This structure is stabilized by an intramolecular disulfide bridge connecting two Cys residues in the facing beta-sheets. In vivo, MHC-I continuously exposes beta2m on the cell surface, where it may be released to plasmatic fluids, transported to the kidneys, degraded, and finally excreted
STPKVQVYSRFPAENGKPNVLNCYVSGFHPPDIEIRLLKNGVKIEDVEQSDLSFSKDWTFYLLKYTEFTP
TKGDEYACRVRHNTLSEPKIYKWD
>gnl|CDD|409428 cd05771, IgC1_Tapasin_R, Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin-like domain on Tapasin-R. Tapasin is a V-C1 (variable-constant) immunoglobulin superfamily molecule present in the endoplasmic reticulum (ER), where it links MHC class I molecules to the transporter associated with antigen processing (TAP). Tapasin-R is a tapasin-related protein that contains similar structural motifs to Tapasin, with some marked differences, especially in the V domain, transmembrane and cytoplasmic regions. The majority of Tapasin-R is located within the ER; however, there may be some expression of Tapasin-R at the cell surface. Tapasin-R lacks an obvious ER retention signal
PRVRLSPKNLVKPDLPQTLSCHIAGYYPLDVDVEWLREEPGGSESQVSRDGVSLSSHRQSVDGTYSISSY
LTLEPGTENRGATYTCRVTHVSLEEPLSVS
>gnl|CDD|409429 cd05772, IgC1_SIRP_domain_2, Signal-regulatory protein (SIRP) immunoglobulin-like domain 2; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin (Ig)-like domain in Signal-Regulatory Protein (SIRP), domain 2 (C1 repeat 1). The SIRPs belong to the "paired receptors" class of membrane proteins that comprise several genes coding for proteins with similar extracellular regions, but very different transmembrane/cytoplasmic regions with different (activating or inhibitory) signaling potentials. They are commonly on NK cells, but are also on many myeloid cells. Their extracellular region contains three Immunoglobulin superfamily domains, a single V-set and two C1-set IgSF domains. Their cytoplasmic tails contain either ITIMs or transmembrane regions that have positively charged residues that allow an association with adaptor proteins, such as DAP12/KARAP, containing ITAMs. There are 3 distinct SIRP members: alpha, beta, and gamma. SIRP alpha (also known as CD172a or SRC homology 2 domain-containing protein tyrosine phosphatase substrate 1/Shps-1) is a membrane receptor that interacts with a ligand CD47 expressed on many cells and gives an inhibitory signal through immunoreceptor tyrosine-based inhibition motifs in the cytoplasmic region that interact with phosphatases SHP-1 and SHP-2. SIRP beta has a short cytoplasmic region and associates with a transmembrane adapter protein DAP12 containing immunoreceptor tyrosine-based activation motifs to give an activating signal. SIRP gamma contains a very short cytoplasmic region lacking obvious signaling motifs, but also binds CD47, but with much less affinity
KPSQPLVSGPSGRATPGQTVSFTCKSHGFSPRDITLKWFKNGNELSALQTTVFPEGDSVSYSVSSTVQVV
LTKDDVHSQLTCEVAHVTLQAPLRGTANLSDI
>gnl|CDD|143250 cd05773, IgC1_hNephrin_like, Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin-like domain in human nephrin and similar proteins. Nephrin is an integral component of the slit diaphragm and is a central component of the glomerular ultrafilter. Nephrin plays a structural role and has a role in signaling. Nephrin is a transmembrane protein having a short intracellular portion, an extracellular portion comprised of eight Ig-like domains, and one fibronectin type III-like domain. The extracellular portions of nephrin from neighboring foot processes of separate podocyte cells may interact with each other, and in association with other components of the slit diaphragm form a porous molecular sieve within the slit pore. The intracellular portion of nephrin is associated with linker proteins, which connect nephrin to the actin cytoskeleton. The intracellular portion is tyrosine phosphorylated, and mediates signaling from the slit diaphragm into the podocytes
VRFAPDLQKGPQLRKVASRGDGSSDANLVCQAQGVPRVQFRWAKNGVPLDLGNPRYEETTEHTGTVHTSI
LTIINVSAALDYALFTCTAHNSLGEDSLDIQLVSTSRPD
>gnl|CDD|409430 cd05774, IgV_CEACAM_D1, First immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM). The members here are composed of the immunoglobulin (Ig)-like domain 1 in carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) proteins. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions: it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two (D1, D4) or four (D1-D4) Ig-like domains on the cell surface
LTIELVPPQVAEGENVLLLVHNLPENLLAYAWYKGKTVSPNFLIASYIISTNSSTPGPAYSGRETIYPNG
SLLIQNVTQKDTGFYTLQTITADLQTEQASVHLQV
>gnl|CDD|409431 cd05775, IgV_CD2_like_N, N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains. The members here are composed of the N-terminal immunoglobulin (Ig)-like domain (or domain 1) of T-cell surface antigen Clusters of Differentiation (CD) 2 and similar proteins. CD2 is a T-cell specific surface glycoprotein and is critically important for mediating adhesion between T cells and antigen-presenting cells or between cytolytic T cells and target cells. CD2 is located on chromosome 1 at 1p13 in humans and on chromosome 3 in mice. CD2 contains an extracellular domain with two or Ig-like domains, a single transmembrane segment, and a cytoplasmic region rich in proline and basic residues
SSGEVYGALGGNVTLTISSLQDDIDEIKWKKTKDKIVEWENNIGPTYFGSFKDRVLLDKESGSLTIKNLT
KEDSGTYELEITSTNGKVLSSKFTLEVL
>gnl|CDD|99819 cd05776, DNA_polB_alpha_exo, inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase alpha, a family-B DNA polymerase. The 3'-5' exonuclease domain of eukaryotic DNA polymerase alpha. DNA polymerase alpha is a family-B DNA polymerase with a catalytic subunit that contains a DnaQ-like 3'-5' exonuclease domain. It is one of the three DNA-dependent type B DNA polymerases (delta and epsilon are the other two) that have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase alpha is almost exclusively required for the initiation of DNA replication and the priming of Okazaki fragments during elongation. It associates with DNA primase and is the only enzyme able to start DNA synthesis de novo. The catalytic subunit contains both polymerase and 3'-5' exonuclease domains, but only exhibits polymerase activity. The 3'-5' exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, without the four conserved acidic residues that are crucial for metal binding and catalysis. This explains why in most organisms, that no specific repair role, other than check point control, has been assigned to this enzyme. The exonuclease domain may have a structural role
PPLTVMSLSIKTVLNSKTNKNEIVMISMLVHRNVSLDKPTPPPPFQSHTCTLTRPLGRSPPPDLFEKNAK
KKKTKVRIFENERALLNFFLAKLQKIDPDVLVGHDLEGFDLDVLLSRIQELKVPHWSRIGRLKRSVWPKK
KGGGKFGERELTAGRLLCDTYLSAKELIRCKSYDLTELSQQVLGIERQDIDPEEILNMYNDSESLLKLLE
HTEKDAYLILQLMFKLNILPLTKQ
>gnl|CDD|99820 cd05777, DNA_polB_delta_exo, DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase delta, a family-B DNA polymerase. The 3'-5' exonuclease domain of eukaryotic DNA polymerase delta. DNA polymerase delta is a family-B DNA polymerase with a catalytic subunit that contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain. It is one of the three DNA-dependent type B DNA polymerases (alpha and epsilon are the other two) that have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase delta is the enzyme responsible for both elongation and maturation of Okazaki fragments on the lagging strand. It is also implicated in mismatch repair (MMR) and base excision repair (BER). The catalytic subunit displays both polymerase and 3'-5' exonuclease activities. The exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues necessary for metal binding and catalysis. The exonuclease domain of family B polymerase also contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation
WSKIAPLRILSFDIECAGRKGVFPEPEKDPVIQIANVVTRQGEGEPFIRNIFTLKTCAPIVGAQVFSFET
EEELLLAWRDFVQEVDPDIITGYNICNFDLPYLLERAKALKLNTFPFLGRIKNIKSTIKDTTFSSKQMGT
RETKEINIEGRIQFDLLQVIQRDYKLRSYSLNSVSAHFLGEQKEDVHYSIITDLQNGNPETRRRLAVYCL
KDAYLPLRLLDKLMCLVNYI
>gnl|CDD|99821 cd05778, DNA_polB_zeta_exo, inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta, a family-B DNA polymerase. The 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta. DNA polymerase zeta is a family-B DNA polymerase which is distantly related to DNA polymerase delta. It plays a major role in translesion replication and the production of either spontaneous or induced mutations. In addition, DNA polymerase zeta also appears to be involved in somatic hypermutability in B lymphocytes, an important element for the production of high affinity antibodies in response to an antigen. The catalytic subunit contains both polymerase and 3'-5' exonuclease domains, but only exhibits polymerase activity. The DnaQ-like 3'-5' exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, without the four conserved acidic residues that are crucial for metal binding and catalysis
HQHLTILSLEVHVNTRGDLLPDPEFDPISAIFYCIDDDVSPFILDANKVGVIIVDELKSNASNGRIRSGL
SGIPVEVVESELELFEELIDLVRRFDPDILSGYEIQRSSWGYLIERAAALGIDDLLDEISRVPSDSNGKF
GDRDDEWGYTHTSGIKIVGRHILNVWRLMRSELALTNYTLENVVYHVLHQRIPLYSNKTLTEWYKSGSAS
ERWRVLEYYLKRVRLNLEILD
>gnl|CDD|99822 cd05779, DNA_polB_epsilon_exo, DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase epsilon, a family-B DNA polymerase. The 3'-5' exonuclease domain of eukaryotic DNA polymerase epsilon. DNA polymerase epsilon is a family-B DNA polymerase with a catalytic subunit that contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain. It is one of the three DNA-dependent type B DNA polymerases (alpha and delta are the other two) that have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase epsilon plays a role in elongating the leading strand during DNA replication. It is also involved in DNA repair. The catalytic subunit contains both polymerase and 3'-5' exonuclease activities. The N-terminal exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and are involved in metal binding and catalysis. DNA polymerase epsilon also carries a unique large C-terminal domain with an unknown function. Phylogenetic analyses indicate that it is orthologous to the archaeal DNA polymerase B3 rather than to the eukaryotic alpha, delta, or zeta polymerases. The exonuclease domain of family-B polymerases contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation
DPRVLAFDIETTKLPLKFPDAETDQIMMISYMIDGQGYLIVNREIVSEDIEDFEYTPKPEYEGPFKVFNE
PDEKALLQRFFEHIREVKPHIIVTYNGDFFDWPFVEARAAIHGLSMEEEIGFRKDSEGEYKSRYIIHMDC
FRWVKRDSYLPQGSQGLKAVTKAKLGYDPVELDPEDMVPLAREDPQTLASYSVSDAVATYYLYM
>gnl|CDD|99823 cd05780, DNA_polB_Kod1_like_exo, DEDDy 3'-5' exonuclease domain of Pyrococcus kodakaraensis Kod1 and similar archaeal family-B DNA polymerases. The 3'-5' exonuclease domain of archaeal family-B DNA polymerases with similarity to Pyrococcus kodakaraensis Kod1, including polymerases from Desulfurococcus (D. Tok Pol) and Thermococcus gorgonarius (Tgo Pol). Kod1, D. Tok Pol, and Tgo Pol are thermostable enzymes that exhibit both polymerase and 3'-5' exonuclease activities. They are family-B DNA polymerases. Their amino termini harbor a DEDDy-type DnaQ-like 3'-5' exonuclease domain that contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and are involved in metal binding and catalysis. The exonuclease domain of family B polymerases contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation. Members of this subfamily show similarity to eukaryotic DNA polymerases involved in DNA replication. Some archaea possess multiple family-B DNA polymerases. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family-B DNA polymerases support independent gene duplications during the evolution of archaeal and eukaryotic family-B DNA polymerases
EDLKILSFDIEVLNHEGEPNPEKDPIIMISFADEGGNKVITWKKFDLPFVEVVKTEKEMIKRFIEIVKEK
DPDVIYTYNGDNFDFPYLKKRAEKLGIELDLGRDGSEIKIQRGGFNNASEIKGRIHVDLYPVARRTLNLT
RYTLERVYEELFGIEKEDVPGEEIAEAWDSGENLERLFRYSMEDAKYTYEIGKEF
>gnl|CDD|99824 cd05781, DNA_polB_B3_exo, DEDDy 3'-5' exonuclease domain of Sulfurisphaera ohwakuensis DNA polymerase B3 and similar archaeal family-B DNA polymerases. The 3'-5' exonuclease domain of archaeal proteins with similarity to Sulfurisphaera ohwakuensis DNA polymerase B3. B3 is a family-B DNA polymerase. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. B3 exhibits both polymerase and 3'-5' exonuclease activities. This exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and are involved in metal binding and catalysis. The exonuclease domain of family B polymerases also contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation. Archaeal proteins that are involved in DNA replication are similar to those from eukaryotes. Some archaea possess multiple family-B DNA polymerases. B3 is mainly found in crenarchaea. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family B-DNA polymerases support independent gene duplications during the evolution of archaeal and eukaryotic family-B DNA polymerases
PDLKTLAFDIEVYSKYGTPNPRRDPIIVISLATSNGDVEFILAEGLDDRKIIREFVKYVKEYDPDIIVGY
NSNAFDWPYLVERARVLGVKLDVGRRGGSEPSTGVYGHYSITGRLNVDLYDFAEEIPEVKVKTLENVAEY
LGVMKKSERVLIEWYRIYEYWDDEKKRDILLKYNRDDARSTYGLAEKL
>gnl|CDD|99825 cd05782, DNA_polB_like1_exo, Uncharacterized bacterial subgroup of the DEDDy 3'-5' exonuclease domain of family-B DNA polymerases. A subfamily of the 3'-5' exonuclease domain of family-B DNA polymerases. This subfamily is composed of uncharacterized bacterial family-B DNA polymerases. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. This exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are involved in metal binding and catalysis. The exonuclease domain of family-B DNA polymerases has a fundamental role in proofreading activity. It contains a beta hairpin structure that plays an important role in active site switching in the event of a nucleotide misincorporation. Family-B DNA polymerases are predominantly involved in DNA replication and DNA repair
ILVFDIETVPDVDLGRRLYLLLELDDLEVLEKRFAQRLEKSGSDFLPLPFHKVVSISALYRDDDGGFLKV
RTLDGADEKELLEDFFQLIEKKNPRLVSFNGRGFDLPVLHLRALIHGVSAPAYFDLGNKDWNYRNRYSER
HLDLMDLLAFYGARARASLDLLAKLLGIPGKMDVDGSQVWELYAEGKLDEIAEYCETDVLNTYLLYLR
>gnl|CDD|99826 cd05783, DNA_polB_B1_exo, DEDDy 3'-5' exonuclease domain of Sulfolobus solfataricus DNA polymerase B1 and similar archaeal family-B DNA polymerases. The 3'-5' exonuclease domain of Sulfolobus solfataricus DNA polymerase B1 and similar archaeal proteins. B1 is a family-B DNA polymerase. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. B1displays thermostable polymerase and 3'-5' exonuclease activities. This exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and are involved in metal binding and catalysis. The exonuclease domain of family-B polymerases also contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation. Family-B DNA polymerases from thermophilic archaea are unique in that they are able to recognize the presence of uracil in the template strand, leading to the stalling of DNA synthesis. This is an additional safeguard mechanism against increased levels of deaminated bases during genome duplication at high temperatures. S. solfataricus B1 also interacts with DNA polymerase Y and may contribute to genome stability mechanisms
PIPKLKRIAIDIEVYTPIKGRIPDPKTAEYPVISVALAGSDGLKRVLVLKREGVEGLEGLLPEGAEVEFF
DSEKELIREAFKIISEYPIVLTFNGDNFDLPYLYNRALKLGIPKEEIPIYLKRDYATLKHGIHIDLYKFF
SNRAIQVYAFGNKYREYTLDAVAKALLGEGKVELEKNISELNLYELAEYNYRDAELTLELTTFN
>gnl|CDD|99827 cd05784, DNA_polB_II_exo, DEDDy 3'-5' exonuclease domain of Escherichia coli DNA polymerase II and similar bacterial family-B DNA polymerases. The 3'-5' exonuclease domain of Escherichia coli DNA polymerase II (Pol II) and similar bacterial proteins. Pol II is a family-B DNA polymerase. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. This exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and are involved in metal binding and catalysis. The exonuclease domain has a fundamental role in the proofreading activity of polII. It contains a beta hairpin structure that plays an important role in active site switching in the event of a nucleotide misincorporation. Pol II is involved in a variety of cellular activities, such as the repair of DNA damaged by UV irradiation or oxidation. It plays a pivotal role in replication-restart, a process that bypasses DNA damage in an error-free manner. Pol II is also involved in lagging strand synthesis
PKLKVVSLDIETSMDGELYSIGLYGEGQERVLMVGDPEDDAPDNIEWFADEKSLLLALIAWFAQYDPDII
IGWNVINFDLRLLQRRAEAHGLPLRLGRGGSPLNWRQSGKPGQGFLSLPGRVVLDGIDALKTATYHFESF
SLENVAQELLGEGKLIHDVDDRGAEIERLFREDKLALARYNLQDCELVWRIFE
>gnl|CDD|99828 cd05785, DNA_polB_like2_exo, Uncharacterized bacterial subgroup of the DEDDy 3'-5' exonuclease domain of family-B DNA polymerases. A subfamily of the 3'-5' exonuclease domain of family-B DNA polymerases. This subfamily is composed of uncharacterized bacterial family-B DNA polymerases. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. This exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are involved in metal binding and catalysis. The exonuclease domain of family-B DNA polymerases has a fundamental role in proofreading activity. It contains a beta hairpin structure that plays an important role in active site switching in the event of a nucleotide misincorporation. Family-B DNA polymerases are predominantly involved in DNA replication and DNA repair
FKGMTFDDLRRLQLDIETYSLPGFFFSNPDRGDDRIIIVALRDNRGWEEVLHAEDAAEKELLEELVAIIR
ERDPDVIEGHNIFRFDLPYLRRRCRRHGVPLAIGRDGSIPRQRPSRFRFAERLIDYPRYDIPGRHVIDTY
FLVQLFDVSSRDLPSYGLKAVAKHFGLASPDRTYIDGRQIAEVWRSDPARLLAYALDDVRETEGLAA
>gnl|CDD|100061 cd05787, LbH_eIF2B_epsilon, eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange
VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSL
ISFGVVIGD
>gnl|CDD|240215 cd05789, S1_Rrp4, S1_Rrp4: Rrp4 S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Rrp4 protein is a subunit of the exosome complex. The exosome plays a central role in 3' to 5' RNA processing and degradation in eukarytes and archaea. Its functions include the removal of incorrectly processed RNA and the maintenance of proper levels of mRNA, rRNA and a number of small RNA species. In Saccharomyces cerevisiae, the exosome includes nine core components, six of which are homologous to bacterial RNase PH. These form a hexameric ring structure. The other three subunits (RrP4, Rrp40, and Csl4) contain an S1 RNA binding domain and are part of the "S1 pore structure"
RYIPEVGDVVIGRVTEVGFKRWKVDINSPYDAVLPLSEVNLPRTDEDELNMRSYLDEGDLIVAEVQSVDS
DGSVSLHTRSLKYGKL
>gnl|CDD|240216 cd05790, S1_Rrp40, S1_Rrp40: Rrp40 S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Rrp4 protein is a subunit of the exosome complex. The exosome plays a central role in 3' to 5' RNA processing and degradation in eukarytes and archaea. Its functions include the removal of incorrectly processed RNA and the maintenance of proper levels of mRNA, rRNA and a number of small RNA species. In Saccharomyces cerevisiae, the exosome includes nine core components, six of which are homologous to bacterial RNase PH. These form a hexameric ring structure. The other three subunits (RrP4, Rrp40, and Csl4) contain an S1 RNA binding domain and are part of the "S1 pore structure"
RYVPAKGDHVIGIVVAKAGDFFKVDIGGSEPASLSYLAFEGATKRNRPNLNVGDLVYARVVKANRDMEPE
LSCVDSSGKADGFGPL
>gnl|CDD|240217 cd05791, S1_CSL4, S1_CSL4: CSL4, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. ScCSL4 protein is a subunit of the exosome complex. The exosome plays a central role in 3' to 5' RNA processing and degradation in eukarytes and archaea. Its functions include the removal of incorrectly processed RNA and the maintenance of proper levels of mRNA, rRNA and a number of small RNA species. In S. cerevisiae, the exosome includes nine core components, six of which are homologous to bacterial RNase PH. These form a hexameric ring structure. The other three subunits (RrP4, Rrp40, and Csl4) contain an S1 RNA binding domain and are part of the "S1 pore structure"
LVLPKVGSIVIARVTRINPRFAKVDILCVGGRPLKESFRGVIRKEDIRATEKDKVEMYKCFRPGDIVRAK
VISLGDASSYYLSTAENELGVV
>gnl|CDD|240218 cd05792, S1_eIF1AD_like, S1_eIF1AD_like: eukaryotic translation initiation factor 1A domain containing protein (eIF1AD)-like, S1-like RNA-binding domain. eIF1AD is also known as MGC11102 protein. Little is known about the function of eIF1AD. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins, including translation initiation factor IF1A (also referred to as eIF1A in eukaryotes). eIF1A is essential for translation initiation. eIF1A acts synergistically with eIF1 to mediate assembly of ribosomal initiation complexes at the initiation codon and maintain the accuracy of this process by recognizing and destabilizing aberrant preinitiation complexes from the mRNA. Without eIF1A and eIF1, 43S ribosomal preinitiation complexes can bind to the cap-proximal region, but are unable to reach the initiation codon. eIF1a also enhances the formation of 5'-terminal complexes in the presence of other translation initiation factors
QQIVRVLGSKGNNLHEVETPNGSRYLVSMPTKFRKNIWIKRGDFVLVEPIEEGDKVKAEIVKILTRDHVK
YIKEEGLW
>gnl|CDD|240219 cd05793, S1_IF1A, S1_IF1A: Translation initiation factor IF1A, also referred to as eIF1A in eukaryotes and aIF1A in archaea, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. IF1A is essential for translation initiation. eIF1A acts synergistically with eIF1 to mediate assembly of ribosomal initiation complexes at the initiation codon and maintain the accuracy of this process by recognizing and destabilizing aberrant preinitiation complexes from the mRNA. Without eIF1A and eIF1, 43S ribosomal preinitiation complexes can bind to the cap-proximal region, but are unable to reach the initiation codon. eIF1a also enhances the formation of 5'-terminal complexes in the presence of other translation initiation factors. This protein family is only found in eukaryotes and archaea
EEYGQVEKMLGNGRLEVRCFDGKKRLCRIRGKMRKRVWINEGDIVLVAPWDFQDDKADIIYKYTPDEVRW
LKRKGEL
>gnl|CDD|240220 cd05794, S1_EF-P_repeat_2, S1_EF-P_repeat_2: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. EF-P stimulates the peptidyltransferase activity in the prokaryotic 70S ribosome. EF-P enhances the synthesis of certain dipeptides with N-formylmethionyl-tRNA and puromycine in vitro. EF-P binds to both the 30S and 50S ribosomal subunits. EF-P binds near the streptomycine binding site of the 16S rRNA in the 30S subunit. EF-P interacts with domains 2 and 5 of the 23S rRNA. The L16 ribosomal protein of the 50S or its N-terminal fragment are required for EF-P mediated peptide bond synthesis, whereas L11, L15, and L7/L12 are not required in this reaction, suggesting that EF-P may function at a different ribosomal site than most other translation factors. EF-P is essential for cell viability and is required for protein synthesis. EF-P is mainly present in bacteria. The EF-P homologs in archaea and eukaryotes are the initiation factors aIF5A and eIF5A, respectively. EF-P has 3 domains (domains I, II, and III). Domains II and III are S1-like domains. This CD includes domain III (the second S1 domain of EF_P). Domains II and III of have structural homology to the eIF5A domain C, suggesting that domains II and III evolved by duplication
VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER
>gnl|CDD|240221 cd05795, Ribosomal_P0_L10e, Ribosomal protein L10 family, P0 and L10e subfamily; composed of eukaryotic 60S ribosomal protein P0 and the archaeal P0 homolog, L10e. P0 or L10e forms a tight complex with multiple copies of the small acidic protein L12(e). This complex forms a stalk structure on the large subunit of the ribosome. The stalk is known to contain the binding site for elongation factors G and Tu (EF-G and EF-Tu, respectively); however, there is disagreement as to whether or not L10 is involved in forming the binding site. The stalk is believed to be associated with GTPase activities in protein synthesis. In a neuroblastoma cell line, L10 has been shown to interact with the SH3 domain of Src and to activate the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott-Aldrich Syndrome Protein (WASP) and the WASP-interacting protein (WIP). These eukaryotic and archaeal P0 sequences have an additional C-terminal domain homologous with acidic proteins P1 and P2
EWKKEYVEKLTELLKSYPKVLIVDADNVGSKQLQKIRRSLRGKAEILMGKNTLIRRALRNLGDENPELEK
LLPYLKGNVGFIFTNGDPFEIRKILEENKVPAPAKPGAIAPCDVVVPAGPTGMPPGPTSFFQALGIPTKI
EKGKIEIISDVVVVKKGEKVGASEATLLNKLNIKP
>gnl|CDD|240222 cd05796, Ribosomal_P0_like, Ribosomal protein L10 family, P0-like protein subfamily; composed of uncharacterized eukaryotic proteins with similarity to the 60S ribosomal protein P0, including the Saccharomyces cerevisiae protein called mRNA turnover protein 4 (MRT4). MRT4 may be involved in mRNA decay. P0 forms a tight complex with multiple copies of the small acidic protein L12(e). This complex forms a stalk structure on the large subunit of the ribosome. It occupies the L7/L12 stalk of the ribosome. The stalk is known to contain the binding site for elongation factors EF-G and EF-Tu; however, there is disagreement as to whether or not P0 is involved in forming the binding site. The stalk is believed to be associated with GTPase activities in protein synthesis. In a neuroblastoma cell line, P0 has been shown to interact with the SH3 domain of Src and to activate the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott-Aldrich Syndrome Protein (WASP) and the WASP-interacting protein (WIP). Some eukaryotic P0 sequences have an additional C-terminal domain homologous with acidic proteins P1 and P2
ELKQKLVENIREAVDKYKYIYVFSVDNMRNNKLKDIRQEWKDSRFFFGKNKVMQVALGRTPEDEYKPNLH
KLSKYLKGQVGLLFTNEPPEEVIEYFDSYSEPDFARAGSIATETVTLPEGPLEQFPHSMEPQLRKLGLPT
KLKKGVITLEADYVVCEEGKVLT
>gnl|CDD|240223 cd05797, Ribosomal_L10, Ribosomal protein L10 family, L10 subfamily; composed of bacterial 50S ribosomal protein and eukaryotic mitochondrial 39S ribosomal protein, L10. L10 occupies the L7/L12 stalk of the ribosome. The N-terminal domain (NTD) of L10 interacts with L11 protein and forms the base of the L7/L12 stalk, while the extended C-terminal helix binds to two or three dimers of the NTD of L7/L12 (L7 and L12 are identical except for an acetylated N-terminus). The L7/L12 stalk is known to contain the binding site for elongation factors G and Tu (EF-G and EF-Tu, respectively); however, there is disagreement as to whether or not L10 is involved in forming the binding site. The stalk is believed to be associated with GTPase activities in protein synthesis. In a neuroblastoma cell line, L10 has been shown to interact with the SH3 domain of Src and to activate the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott-Aldrich Syndrome Protein (WASP) and the WASP-interacting protein (WIP). These bacteria and eukaryotic sequences have no additional C-terminal domain, present in other eukaryotic and archaeal orthologs
NREKKEEIVAELKEKLKEAKSVVVADYRGLTVAQLTELRKELREAGVKLKVVKNTLAKRALEGTGFEDLD
DLLKGPTAIAFSEEDPVAAAKVLKDFAKENKKLEIKGGVVEGKVLDAEEVKALAKLPSREELLAQLLGLL
QAPATKLVRVLNAPASK
>gnl|CDD|240224 cd05798, SIS_TAL_PGI, SIS_TAL_PGI: Transaldolase (TAL)/ Phosphoglucose isomerase (PGI). This group represents the SIS (Sugar ISomerase) PGI domain, of a multifunctional protein (TAL-PGI) having both TAL and PGI activities. TAL_PGI contains an N-terminal TAL domain and a C-terminal PGI domain. TAL catalyzes the reversible conversion of sedoheptulose-7-phosphate (S7P) and glyceraldehyde-3-phosphate (G3P), to fructose-6-phosphate (F6P) and erythrose-4-phosphate (E4P). PGI catalyzes the reversible isomerization of F6P to glucose-6-phosphate (G6P). It has been suggested for Gluconobacter oxydans TAL_PGI that this enzyme generates E4P and G6P directly from S7P and G3P. G. oxydans TAL_PGI contributes to increased xylitol production from D-arabitol. As xylitol is an alternative natural sweetner to sucrose, the microbial conversion of D-arabitol to xylitol is of interest to food and pharmaceutical industries
DKVTIIASPGIASLGAWLEQLIAESTGKEGKGIIPVDGEPLGDPAVYGDDRVFVYLRLAGEADADQEEAL
LALEAAGHPVIRIDLDDAYDLGQEFFRWEMATAVAGAVLGINPFDQPDVEASKIETRRL
>gnl|CDD|100092 cd05799, PGM2, This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model
RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRHNSREFAELTAAVLA
ANGIKVYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAV
LEPLDIKFEEALDSGLIKYIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAG
FTNVIVVEEQAEPDPDFPTVKFPNPEEPGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLL
TGNEIGALLADYLLEQRKEKGKLPKNPVIVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESG
GKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAYLKAQGKTLLDRLDELYEKYGYYKEKTISITFE
GKEGPEKIKAIMDRLRNNPNVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGKKTLEEAEKKLDALKK
>gnl|CDD|100093 cd05800, PGM_like2, This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model
IKFGTDGWRGIIAEDFTFENVRRVAQAIADYLKEEGGGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDV
YLSDRPVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLE
ARAEGLIETIDPKPDYLEALRSLVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPL
FGGIPPEPIEKNLGELAEAVKEGGADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENKGLRGP
VVKTVSTTHLIDRIAEKHGLPVYETPVGFKYIAEKMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLL
EAVAKTGKPLSELVAELEEEYGPSYYDRIDLRLTPAQKEAILEKLKNEPPLSIAGGKVDEVNTIDGVKLV
LEDGSWLLIRPSGTEPLLRIYAEAPSPEKVEALLDAGKKLA
>gnl|CDD|100094 cd05801, PGM_like3, This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model
PRLITAYYTLKPDPSNPAQRVAFGTSGHRGSSLKGSFNEAHILAISQAICDYRKSQGITGPLFLGKDTHA
LSEPAFISALEVLAANGVEVIIQQNDGYTPTPVISHAILTYNRGRTEGLADGIVITPSHNPPEDGGFKYN
PPHGGPADTDITRWIEKRANALLANGLKGVKRIPLEAALASGYTHRHDFVTPYVADLGNVIDMDAIRKSG
LRLGVDPLGGASVPYWQPIAEKYGLNLTVVNPKVDPTFRFMTLDHDGKIRMDCSSPYAMAGLLKLKDKFD
LAFANDPDADRHGIVTPSAGLMNPNHYLSVAIDYLFTHRPLWNKSAGVGKTLVSSSMIDRVAAALGRKLY
EVPVGFKWFVDGLLDGSLGFGGEESAGASFLRRDGTVWTTDKDGIIMCLLAAEILAVTGKDPGQLYQELT
ERFGEPYYARIDAPATPEQKARLKKLSPEQVTATELAGDPILAKLTRAPGNGASIGGLKVTTANGWFAAR
PSGTEDVYKIYAESFLSEEHLKKIQKEAQEIV
>gnl|CDD|100095 cd05802, GlmM, GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model
LFGTDGIRGVANEPLTPELALKLGRAAGKVLGKGGGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLL
LGVIPTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKELELPPTGEK
IGRVYRIDDARGRYIEFLKSTFPKDLLSGLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNINV
NCGSTHPESLQKAVLENGADLGIAFDGDADRVIAVDEKGNIVDGDQILAICARDLKERGRLKGNTVVGTV
MSNLGLEKALKELGIKLVRTKVGDRYVLEEMLKHGANLGGEQSGHIIFLDHSTTGDGLLTALQLLAIMKR
SGKSLSELASDMKLYPQVLVNVRVKDKKALLENPRVQAAIAEAEKELGGEGRVLVRPSGTEPLIRVMVEG
EDEELVEKLAEELA
>gnl|CDD|100096 cd05803, PGM_like4, This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate guanyltransferase domain in a protein of unknown function that is found in both prokaryotes and eukaryotes. This domain belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model
IISISGIRGIVGEGLTPEVITRYVAAFATWQPERTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVID
LGIAPTPTVQVLVRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEEVLSCAEAGSAQKAGYDQ
LGEVTFSEDAIAEHIDKVLALVDVDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGL
FPHTPEPLPENLTQLCAAVKESGADVGFAVDPDADRLALVDEDGRPIGEEYTLALAVDYVLKYGGRKGPV
VVNLSTSRALEDIARKHGVPVFRSAVGEANVVEKMKEVDAVIGGEGNGGVILPDVHYGRDSLVGIALVLQ
LLAASGKPLSEIVDELPQYYISKTKVTIAGEALERLLKKLEAYFKDAEASTLDGLRLDSEDSWVHVRPSN
TEPIVRIIAEAPTQDEAEALADRFI
>gnl|CDD|100115 cd05804, StaR_like, StaR_like; a well-conserved protein found in bacteria, plants, and animals. A family member from Streptomyces toyocaensis, StaR is part of a gene cluster involved in the biosynthesis of glycopeptide antibiotics (GPAs), specifically A47934. It has been speculated that StaR could be a flavoprotein hydroxylating a tyrosine sidechain. Some family members have been annotated as proteins containing tetratricopeptide (TPR) repeats, which may at least indicate mostly alpha-helical secondary structure
ADPDFALGHAAAALLLLLGGERPAAAAKAAAAAQALAARATERERAHVEALSAWIAGDLPKALALLEQLL
DDYPRDLLALKLHLGAFGLGDFSGMRDHVARVLPLWAPENPDYWYLLGMLAFGLEEAGQYDRAEEAARRA
LELNPDDAWAVHAVAHVLEMQGRFKEGIAFMESWRDTWDCSSMLRGHNWWHLALFYLERGDYEAALAIYD
THIAPSAESDPALDLLDAASLLWRLELAGHVDVGDRWEDLADYAAWHFPDHGLAFNDLHAALALAGAGDK
DALDKLLAALKGRASSADDNKQPARDVGLPLAEALYAFAEGNYATALELLGPVRDDLARIGGSHAQRDVF
EQTLI
>gnl|CDD|100097 cd05805, MPG1_transferase, GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose pyrophosphorylase, is a bifunctional enzyme with both phosphomannose isomerase (PMI) activity and GDP-mannose phosphorylase (GMP) activity. The protein contains an N-terminal NTP transferase domain, an L-beta-H domain, and a C-terminal PGM-like domain that belongs to the alpha-D-phosphohexomutase superfamily. This subfamily is limited to bacteria and archaea. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this group appear to lack conserved residues necessary for metal binding and catalytic activity. Other members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model
LFGGRGVSGLINVDITPEFATRLGAAYGSTLPPGSTVTVSRDASRASRMLKRALISGLLSTGVNVRDLGA
LPLPVARYAIRFLGASGGIHVRTSPDDPDKVEIEFFDSRGLNISRAMERKIENAFFREDFRRAHVDEIGD
ITEPPDFVEYYIRGLLRALDTSGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVILNARLDEDAPRTD
TERQRSLDRLGRIVKALGADFGVIIDPNGERLILVDEAGRVISDDLLTALVSLLVLKSEPGGTVVVPVTA
PSVIEQLAERYGGRVIRTKTSPQALMEAALENVVLAGDGDGGFIFPEFHPGFDAIAALVKILEMLARTNI
SLSQIVDELPRFYVLHKEVPCPWEAKGRVMRRLIEEAPDKSIELIDGVKIYEDDGWVLVLPDADEPLCHI
YAEGSDQERAEELTEFYVEKV
>gnl|CDD|99881 cd05806, CBM20_laforin, Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Laforin, encoded by the EPM2A gene, is a dual-specificity phosphatase that dephosphorylates complex carbohydrates. Mutations in the gene encoding laforin result in Lafora disease, a fatal autosomal recessive neurodegenerative disorder characterized by the presence of intracellular deposits of insoluble, abnormally branched, glycogen-like polymers, known as Lafora bodies, in neurons, muscle, liver, and other tissues. The molecular basis for the formation of these Lafora bodies is unknown. Laforin is one of the only phosphatases that contains a carbohydrate-binding module. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
MLFRFGVVLTFADRDTELLVLGSRPELGSWDPQRAVPMRPARKALSPQEPSLWLGEVELSEPGSEDTFWY
KFLKREAGALIWEGNGPHHDRCCVYDSSNLVDGVYCLPVGHW
>gnl|CDD|99882 cd05807, CBM20_CGTase, CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
DQVSVRFVVNNATTQLGENVYLVGNVHELGNWDPSKAIGPFFNQVVYQYPNWYYDVSVPAGTTIEFKFIK
KNGDNTVTWESGSNHTYTAPSSTTGTIRVNW
>gnl|CDD|99883 cd05808, CBM20_alpha_amylase, Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
VAVTFNVTATTVWGQNVYVVGNVPELGNWSPANAVALSAATYPVWSGTVDLPAGTAIEYKYIKKDGSGTV
TWESGPNRTATTPASGTLTLNDTWR
>gnl|CDD|99884 cd05809, CBM20_beta_amylase, Beta-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Beta-amylase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 14, which hydrolyzes the alpha-1,4-glucosidic bonds of starch, yielding beta-maltose from the nonreducing end of the substrate. Beta-amylase is found in both plants and microorganisms, however the plant members lack a C-terminal CBM20 domain and are not included in this group. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
TPVPQTFVVKNVPTTIGETVYITGSRAELGNWDTKQYPIQLYYNSHSNDWRGTVHLPAGRNIEFKAIKKS
KDGTNKSWQGGQQSWYPVPLGTTSYTSSW
>gnl|CDD|99885 cd05810, CBM20_alpha_MTH, Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Alpha-MTH, also known as maltotetraose-forming exo-amylase or G4-amylase, is an exo-amylase found in bacteria that degrades starch from its non-reducing end. Most alpha-MTHs have, in addition to the C-terminal CBM20 domain, an N-terminal glycosyl hydrolase family 13 catalytic domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
VSVTFSCNNGTTQLGQSVYVVGNVPQLGNWSPADAVKLDPTAYPTWSGSISLPASTNVEWKCLKRNETNP
TAGVQWQGGGNNQLTTGNSTASTSGSF
>gnl|CDD|99886 cd05811, CBM20_glucoamylase, Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
CATATTVAVTFNERVTTSYGENIKIVGSIPQLGNWDTSSAVALSASQYTSSNPLWSVTIPLPAGTSFEYK
FIRKESDGSVTWESDPNRSYTVPSGCGTTATVDDSW
>gnl|CDD|99887 cd05813, CBM20_genethonin_1, Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 is a human skeletal muscle protein with no known function. It contains a C-terminal CBM20 domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
VNVTFRVHYITHSDAQLVAVTGDHEELGSWHSYIPLQYVKDGFWSASVSLPVDTHVEWKFVLVENGQVTR
WEECSNRLLETGHEDKIVHKWWGCH
>gnl|CDD|99888 cd05814, CBM20_Prei4, Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
CRVTFRVFASELAPGEVVAVVGSLPVLGNWQPEKAVPLEKEDDDCNLWKASIELPRGVDFQYRYFVAVVL
NDSGPCQVIVRKWETHLQPRSIKPLEEERLNDDDKFGIYDGVEQVDRGWL
>gnl|CDD|99889 cd05815, CBM20_DPE2_repeat1, Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 1. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 starch binding domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal carbohydrate-binding domains. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
TLSFKLPYYTQWGQSLLICGSDPLLGSWNVKKGLLLKPSHQGDVLVWSGSISVPPGFSSEYNYYVVDDRK
SVLRSESGEKRKLVLPEGLQGGESVELRDLW
>gnl|CDD|99890 cd05816, CBM20_DPE2_repeat2, Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 2. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal CBM20 domains. Included in this group are PDE2-like proteins from Dictyostelium, Entamoeba, and Bacteroides. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
VVQFKILCPYVPKGQSVYVTGSSPELGNWDPQKALKLSDVGFPIWEADIDISKDSFPFEYKYIIANKDSG
VVSWENGPNRELSAPSLKGESSTLIVSDG
>gnl|CDD|99891 cd05817, CBM20_DSP, Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This CBM20 domain is located at the N-terminus of a protein tyrosine phosphatase of unknown function found in slime molds and ciliated protozoans. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
MVTFKIHYPTQFGEAVYISGNCNQLGNWNPSKAKRMQWNEGDLWTVDVGIPESVYIEYKYFVSNYDDPNT
VLWESGPNRVLRTNHQILLIWNHRKVKFNC
>gnl|CDD|99892 cd05818, CBM20_water_dikinase, Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in the chloroplast-encoded phosphoglucan water dikinase, one of two enzymes involved in the phosphorylation of plant starches. In addition to the CBM20 domain, phosphoglucan water dikinase contains a C-terminal pyruvate binding domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
KVKLQVRLDHQVKFGEHVAILGSTKELGSWKKKVPMNWTENGWVCDLELDGGELVEYKFVIVKRDGSVIW
EGGNNRVLELPKEGNFEIVCHW
>gnl|CDD|271320 cd05819, NHL, NHL repeat unit of beta-propeller proteins. The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats
GTGPGELNNPQGIAVDSSGNIYVADTGNNRIQVFDPDGNFITSFGSFGSGDGQFNEPAGVAVDSDGNLYV
ADTGNHRIQKFDPDGNFLASFGGSGDGDGEFNGPRGIAVDSSGNIYVADTGNHRIQKFDPDGEFLTTFGS
GGSGPGQFNGPTGVAVDSDGNIYVADTGNHRIQVFDPDGNFLTTFGSTGTGPGQFNYPTGIAVDSDGNIY
VADSGNNRVQVFDPDGAGFGGNGNFLGSDGQFNRPSGLAVDSDGNLYVADTGNNRIQVF
>gnl|CDD|99893 cd05820, CBM20_novamyl, Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1,4-alpha-maltohydrolase, and AcbD), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Novamyl has a five-domain structure similar to that of cyclodextrin glucanotransferase (CGTase). Novamyl has a substrate-binding surface with an open groove which can accommodate both cyclodextrins and linear substrates. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch
KQIPVIFTVQNTPETAPGEFLYLTGSVPELGNWSTSTDQAVGPLLCPNWPDWFVVASVPAGTYIEFKFLK
APADGTGTWEGGSNHAYTTPSGGTGTVTVTWQR
>gnl|CDD|100113 cd05821, TLP_Transthyretin, Transthyretin (TTR) is a 55 kDa protein responsible for the transport of thyroid hormones and retinol in vertebrates. TTR distributes the two thyroid hormones T3 (3,5,3'-triiodo-L-thyronine) and T4 (Thyroxin, or 3,5,3',5'-tetraiodo-L-thyronine), as well as retinol (vitamin A) through the formation of a macromolecular complex that includes each of these as well as retinol-binding protein. Misfolded forms of TTR are implicated in the amyloid diseases familial amyloidotic polyneuropathy and senile systemic amyloidosis. TTR forms a homotetramer with each subunit consisting of eight beta-strands arranged in two sheets and a short alpha-helix. The central channel of the tetramer contains two independent binding sites, each located between a pair of subunits, which differ in their ligand binding affinity. A negative cooperativity has been observed for the binding of T4 and other TTR ligands. A fraction of plasma TTR is carried in high density lipoproteins by binding to apolipoprotein AI (apoA-I). TTR is able to proteolytically process apoA-I by cleaving its C-terminus; therefore TTR has protease activity in addition to its function in protein transport
GGGDSKCPLMVKVLDAVRGSPAANVAVKVFKKTADGSWEPFASGKTTETGEIHGLTTDEQFTEGVYKVEF
DTKAYWKKLGISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSN
>gnl|CDD|100114 cd05822, TLP_HIUase, HIUase (5-hydroxyisourate hydrolase) catalyzes the second step in a three-step ureide pathway in which 5-hydroxyisourate (HIU), a product of the uricase (urate oxidase) reaction, is hydrolyzed to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). HIUase has high sequence similarity with transthyretins and is a member of the transthyretin-like protein (TLP) family. HIUase is distinguished from transthyretins by a conserved signature motif at its C-terminus that forms part of the active site. In HIUase, this motif is YRGS, while transthyretins have a conserved TAVV sequence in the same location. Most HIUases are cytosolic but in plants and slime molds, they are peroxisomal based on the presence of N-terminal periplasmic localization sequences. HIUase forms a homotetramer with each subunit consisting of eight beta-strands arranged in two sheets and a short alpha-helix. The central channel of the tetramer contains two independent binding sites, each located between a pair of subunits
GPLSTHVLDTATGKPAAGVAVTLYRLDGNGWTLLATGVTNADGRCDDLLPPGAQLAAGTYKLTFDTGAYF
AARGQESFYPEVEVRFTITDPTEHYHVPLLLSPFGYSTYRGS
>gnl|CDD|100062 cd05824, LbH_M1P_guanylylT_C, Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity
LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVT
VLGDDVTIKD
>gnl|CDD|100063 cd05825, LbH_wcaF_like, wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms
PWNLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAFPLITAPIVIGDGAWVAAEAF
VGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV
>gnl|CDD|320675 cd05826, Sortase_B, Sortase domain found in class B sortases. Class B sortases are membrane-bound cysteine transpeptidases broadly distributed in Gram-positive bacteria (mainly present in Firmicutes and Actinobacteria). They can have radically distinct functions. Some members of this group attach haemoproteins to the peptidoglycan of the cell wall, while others assemble pili, which are multi-subunit hair-like fibres that extend from the cell surface to promote microbial adhesion and biofilm formation. In transpeptidation reaction, the surface protein substrate is cleaved at a conserved cell wall-sorting signal (Class B sortases normally recognize the consensus NP[Q/K][T/S][N/G/S][D/A] motif), and covalently linked to peptidoglycan for display on the bacterial surface. The prototypical sortase B protein from Staphylococcus aureus (named Sa-SrtB) cleaves surface protein precursors between threonine and asparagine at a conserved NPQTN motif with subsequent covalent linkage to pentaglycine cross-bridges. It is required for anchoring the heme-iron binding surface protein IsdC to the cell wall envelope. SrtB contains an N-terminal hydrophobic region that functions as a signal peptide/transmembrane domain. At the C terminus, it contains an essential cysteine residue within the catalytic TLXTC signature sequence, where X is usually a serine. Genes encoding SrtB and its targets are generally clustered in the same locus. The prototypical class B sortase involved in pilus biogenesis is pilus-specific sortase C2 from Streptococcus pyogenes (named Sp-SrtC2) that anchors a surface protein containing a QVPTGV motif to the cell wall, as well as polymerizes the major pilin subunit Tee3/FctA and attaches the minor tip pilin Cpa. The linkage of Cpa to Tee3 by SrtC2 requires the VPPTG motif in the cell wall-sorting signal of Cpa. The family also includes SrtB enzymes from Bacillus anthracis (named Ba-SrtB) and Clostridium difficile (named Cd-SrtB). Ba-SrtB is thought to recognize the NPKTG motif, and attaches surface proteins to meso-diaminopimelic acid (mDAP) cross-bridges. Cd-SrtB does not play an essential role in pathogenesis. It cleaves short [SP]PXTG motif-containing peptides between the threonine and glycine residues and then covalently anchors the threonine residue to a nucleophile such as glycine or mDAP, but not to the peptidoglycan of C. difficile, suggesting a novel association of sortase activity with cyclic diGMP (c-diGMP)-mediated regulation to control levels of cell wall anchoring and secretion of putative adhesion molecules
PDIVGWIYIPGTNIDYPVVQGKDNEYYLNHDFDGEYSLAGSIFLDYRNSPDFSDRNTIIYGHNMKNGSMF
GDLKKYKDEDFFKEHPYIYLYTPDGKYKYEIFAVYVTDADDDYYQTDFSDDEEFQEYLDEIKERSLYDTG
VDVTEGDKILTLSTCSYEFDNGRLVVVAKL
>gnl|CDD|320676 cd05827, Sortase_C, Sortase domain found in class C sortases. Class C sortases are membrane-bound cysteine transpeptidases broadly distributed in Gram-positive bacteria (mainly present in Firmicutes and Actinobacteria). They function as pilin polymerases responsible for the assembly of pili, which are multi-subunit hair-like fibres that extend from the cell surface to promote microbial adhesion and biofilm formation. First, one or more class C sortases form the long thin shaft of the pilus through linking together pilin subunits via isopeptide bonds. The base of the pilus is then anchored to the cell wall by a housekeeping sortase or, in some cases, the class C sortase itself. Depending upon the organism both the number and type of sortase enzymes involved varies, and in some cases, accessory factors appear to be needed. In three-component spaA pilus from Corynebacterium diphtheriae, the prototypical class C sortase (named Cd-SrtA) catalyzes polymerization of the SpaA-type pilus, consisting of the shaft pilin SpaA, tip pilin SpaC and minor pilin SpaB. The pilus shaft is then attached to the cell wall by a housekeeping class E sortase, Cd-SrtF. In the absence of Cd-SrtF, Cd-SrtA attaches the pilus to the cell wall, albeit at a reduced rate. Cd-SrtA can recognize two distinct sorting signals (LPLTG in SpaA and SpaC, and LAFTG in SpaB) and it can employ lysine residues that originate from different proteins (either Lys190 within the pilin motif of SpaA or Lys139 in SpaB). However, Cd-SrtA cannot be able to polymerize the major pilin subunit SpaH, even though it contains LPLTG motif. In two-component pili of prototypical Bacillus cereus, the class C sortase (named Bc-SrtD) cleaves related sorting signals within a major pilin protein BcpA (LPVTG) and a minor tip pilin BcpB (IPNTG), and catalyzes a transpeptidation that joins the threonine residues in each signal to the side-chain of Lys162 in BcpA (located within a pilin motif). Unlike the SpaA pilus in C. diphtheriae, in B. cereus Bc-SrtD is unable to covalently attach the pilus to the cell wall without the help of the housekeeping sortase
DGVIGYLEIPKIDVDLPIYHGTSEEVLAKGAGHLEGTSLPVGGKGTHSVIAGHRGLPNATLFTDLDKLKK
GDKFYITVLGETLAYKVDDIKVILPDDTDKLKIQPGKDLVTLLTCTPYGINTHRLLVTGER
>gnl|CDD|320677 cd05828, Sortase_D_1, Sortase domain found in subfamily 1 of the class D family of sortases. Class D sortases are cysteine transpeptidases distributed in Gram-positive bacteria (mainly present in Firmicutes). The prototypical subfamily 1 of class D sortase from Bacillus anthracis (named Ba-SrtC) covalently attaches proteins bearing a noncanonical LPNTA sorting signal, such as the BasH and BasI proteins, to the peptidoglycan of the cell wall that facilitate sporulation. BasH is exclusively anchored to the forespore cell wall envelope, while BasI is attached to the diaminopimelic acid moiety of the peptidoglycan of predivisional cells. Ba-SrtC lacks the N-terminal signal peptide and membrane anchor. The family also includes many class D sortase homologs from Gram-negative bacteria, but the functions of these enzymes are unknown
GEPVARLSIPRLGLDLPVLEGTSGEALAFGPGHLPGSALPGEGGNVVIAGHRDTHFRFLKDLKVGDEITL
ETSGGTYTYRVTETRIVDADDTSVLLPTDEETLTLVTCYPFDALGSAPLRYVVYAEL
>gnl|CDD|320678 cd05829, Sortase_F, Sortase domain found in the class F family of sortases. Class F sortases are mainly present in Actinobacteria, Chlorobacteria and Firmicutes. Their functions are largely unknown
ASAPVRLSIPAIGVDAPVVPVGLDADGAMPVPPDPDRAGWYRGGPAPGEAGTAVIAGHVDSGGGPGVFAR
LGDLRPGDEVTVTRADGTTATFRVTSVETYPKDDLPTDEVFGPTGPPRLRLITCGGAFDRGTGSYEDNVV
VYAE
>gnl|CDD|320679 cd05830, Sortase_E, Sortase domain found in the class E family of sortases. Class E sortases are membrane-bound cysteine transpeptidases distributed in Gram-positive bacteria (mainly present in Actinobacteria). Genes encoding class A and E sortases are never found in the same organism, and similar to class A sortases, the genes encoding class E sortases are not positioned adjacent to genes encoding potential protein substrates, suggesting a housekeeping sortase function of class E sortases in some high G + C Gram-positive bacteria. Similar to class A sortase, class E sortases are capable of anchoring a large number of functionally distinct surface proteins containing a cell wall sorting signal to an amino group located on the bacterial cell wall. They recognize an LAXTG sorting signal, instead of the canonical LPXTG motif processed by class A sortases. The prototypical class E sortase from Corynebacterium diphtheria (named Cd-SrtF) is a non-polymerization sortase that is not required for pilus polymerization, and proceeds to complete the assembly process by anchoring the polymer to the cell wall peptidoglycan. Moreover, in Streptomyces coelicolor, one or both of Staphylococcus aureus SrtA homologs may function as class E sortase responsible for the cell wall anchoring of the long chaplin proteins (ChpA-C) containing an LAXTG sorting signal, which presumably mediate aerial hyphae formation. The family also includes some class E sortase homologs from Gram-negative and Archaebacterial species, but the functions of these enzymes are unknown
GEAFAVLYIPRFIDLDRPVVEGTSEVLLRRGVGHYPGTALPGEVGNFAIAGHRTTYGAPFRDLDELRPGD
PIVVETAGGWYVYRVTSTEIVSPDDVEVLAPVPGQPGAPPGRRLLTLTTCHPPGSSAERLIVHAE
>gnl|CDD|100109 cd05831, Ribosomal_P1, Ribosomal protein P1. This subfamily represents the eukaryotic large ribosomal protein P1. Eukaryotic P1 and P2 are functionally equivalent to the bacterial protein L7/L12, but are not homologous to L7/L12. P1 is located in the L12 stalk, with proteins P2, P0, L11, and 28S rRNA. P1 and P2 are the only proteins in the ribosome to occur as multimers, always appearing as sets of heterodimers. Recent data indicate that eukaryotes have four copies (two heterodimers), while most archaeal species contain six copies of L12p (three homodimers) and bacteria may have four or six copies (two or three homodimers), depending on the species. Experiments using S. cerevisiae P1 and P2 indicate that P1 proteins are positioned more internally with limited reactivity in the C-terminal domains, while P2 proteins seem to be more externally located and are more likely to interact with other cellular components. In lower eukaryotes, P1 and P2 are further subdivided into P1A, P1B, P2A, and P2B, which form P1A/P2B and P1B/P2A heterodimers. Some plant species have a third P-protein, called P3, which is not homologous to P1 and P2. In humans, P1 and P2 are strongly autoimmunogenic. They play a significant role in the etiology and pathogenesis of systemic lupus erythema (SLE). In addition, the ribosome-inactivating protein trichosanthin (TCS) interacts with human P0, P1, and P2, with its primary binding site located in the C-terminal region of P2. TCS inactivates the ribosome by depurinating a specific adenine in the sarcin-ricin loop of 28S rRNA
ELACTYAALILHDDGIEITADNINALLKAAGVNVEPYWPGLFAKALEGKDIKDLLSNVGGGGGGAAPAAA
AAAAAAAAAEAKKEEKKEEEEEESDDDMGFGLF
>gnl|CDD|100110 cd05832, Ribosomal_L12p, Ribosomal protein L12p. This subfamily includes archaeal L12p, the protein that is functionally equivalent to L7/L12 in bacteria and the P1 and P2 proteins in eukaryotes. L12p is homologous to P1 and P2 but is not homologous to bacterial L7/L12. It is located in the L12 stalk, with proteins L10, L11, and 23S rRNA. L12p is the only protein in the ribosome to occur as multimers, always appearing as sets of dimers. Recent data indicate that most archaeal species contain six copies of L12p (three homodimers), while eukaryotes have four copies (two heterodimers), and bacteria may have four or six copies (two or three homodimers), depending on the species. The organization of proteins within the stalk has been characterized primarily in bacteria, where L7/L12 forms either two or three homodimers and each homodimer binds to the extended C-terminal helix of L10. L7/L12 is attached to the ribosome through L10 and is the only ribosomal protein that does not directly interact with rRNA. Archaeal L12p is believed to function in a similar fashion. However, hybrid ribosomes containing the large subunit from E. coli with an archaeal stalk are able to bind archaeal and eukaryotic elongation factors but not bacterial elongation factors. In several mesophilic and thermophilic archaeal species, the binding of 23S rRNA to protein L11 and to the L10/L12p pentameric complex was found to be temperature-dependent and cooperative
MEYIYAALLLHYAGKEINEENLKKVLEAAGIEVDEARVKALVAALEEVNIDEAIKKAAVAAAAAAPAAAA
AAAAEEKAEEKEEEKKKEEEKEEEEEEALAGLGALF
>gnl|CDD|100111 cd05833, Ribosomal_P2, Ribosomal protein P2. This subfamily represents the eukaryotic large ribosomal protein P2. Eukaryotic P1 and P2 are functionally equivalent to the bacterial protein L7/L12, but are not homologous to L7/L12. P2 is located in the L12 stalk, with proteins P1, P0, L11, and 28S rRNA. P1 and P2 are the only proteins in the ribosome to occur as multimers, always appearing as sets of heterodimers. Recent data indicate that eukaryotes have four copies (two heterodimers), while most archaeal species contain six copies of L12p (three homodimers). Bacteria may have four or six copies of L7/L12 (two or three homodimers) depending on the species. Experiments using S. cerevisiae P1 and P2 indicate that P1 proteins are positioned more internally with limited reactivity in the C-terminal domains, while P2 proteins seem to be more externally located and are more likely to interact with other cellular components. In lower eukaryotes, P1 and P2 are further subdivided into P1A, P1B, P2A, and P2B, which form P1A/P2B and P1B/P2A heterodimers. Some plants have a third P-protein, called P3, which is not homologous to P1 and P2. In humans, P1 and P2 are strongly autoimmunogenic. They play a significant role in the etiology and pathogenesis of systemic lupus erythema (SLE). In addition, the ribosome-inactivating protein trichosanthin (TCS) interacts with human P0, P1, and P2, with its primary binding site in the C-terminal region of P2. TCS inactivates the ribosome by depurinating a specific adenine in the sarcin-ricin loop of 28S rRNA
MKYVAAYLLAVLGGNASPSAADVKKILGSVGVEVDDEKLNKVISELEGKDVEELIAAGKEKLASVPAGAG
GAAPAAAAAAAAAAAAKKEEKKEESEEESDDDMGFGLFD
>gnl|CDD|438959 cd05834, PWWP_HRP, PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family. The HRP family includes hepatoma-derived growth factor (HDGF), and HDGF-related proteins (HRPs). HDGF, also called high mobility group protein 1-like 2 (HMG-1L2), is a heparin-binding protein that acts as a transcriptional repressor with mitogenic activity for fibroblasts. It is a prognostic factor in several types of cancer. HDGFL1 is also called PWWP domain-containing protein 1 (PWWP1). Its biological function remains unclear. HDGFL2, also called HDGF-related protein 2 (HRP-2), or hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. HDGFL3, also called HDGF-related protein 3 (HRP-3), enhances DNA synthesis and may play a role in cell proliferation. The family also includes PC4 and SFRS1-interacting protein (PSIP) and similar proteins. PSIP, also called CLL-associated antigen KW-7, dense fine speckles 70 kDa protein (DFS 70), lens epithelium-derived growth factor (LEDGF), or transcriptional coactivator p75/p52, acts as a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Members of the HRP family contains a PWWP domain, which is necessary for DNA binding
FKPGDLVFAKVKGYPPWPARIDEIPEGAKIPKNKYPVFFYGTHETAFLKPKDLFPYEENKEKYGKPRKRK
GFNEGLWEIENN
>gnl|CDD|438960 cd05835, PWWP_DNMT3, PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family. The DNMT3 family includes DNMT3A and DNMT3B, which are required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNMT3A, also called DNA methyltransferase HsaIIIA, DNA MTase HsaIIIA, or M.HsaIIIA, modifies DNA in a non-processive manner and also methylates non-CpG sites. It may preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. DNMT3A is recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. DNMT3B, also called DNA methyltransferase HsaIIIB, DNA MTase HsaIIIB, or M.HsaIIIB, may preferentially methylate nucleosomal DNA within the nucleosome core region. DNMT3B may function as a transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Members of this family contains a PWWP domain that is responsible for establishing DNA methylation patterns during embryogenesis and gametogenesis. In tumorigenesis, DNA methylation by DNMT3B is known to play a role in the inactivation of tumor suppressor genes. In addition, a point mutation in the PWWP domain of DNMT3B has been identified in patients with ICF (immunodeficiency, centromeric instability, and facial anomalie) syndrome, a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA
KIGDLVWAKLKGSPWWPGIVVSHKDCGQKPPAEGSVWVFWFGDHKVSEVPLDKILPFAEFFNKFYISKNS
SKLYKKAVYEALKEAAERS
>gnl|CDD|438961 cd05836, PWWP_GLYR1, PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins. GLYR1, also called 3-hydroxyisobutyrate dehydrogenase-like protein, cytokine-like nuclear factor N-PAC, nuclear protein NP60, or nuclear protein of 60 kDa, is a putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. It recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). GLYR1 enhances the activity of MAP2K4 and MAP2K6 kinases to phosphorylate p38-alpha. In addition to the PWWP domain, GLYR1 also contains an AT-hook and a C-terminal NAD-binding domain. The PWWP domain specifically recognizes DNA and histone methylated lysines
FKIGDLVWAKMKGFPPWPGKIVNPPPDLKKPPRKKKMHCVYFFGSENYAWIEDENIKPYEEFKEEMLKSK
KSAGFKDAVEAIEEYI
>gnl|CDD|438962 cd05837, PWWP_MSH6, PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins. MSH6, also called G/T mismatch-binding protein (GTBP or GTMBP), MutS protein homolog 6, or MutS-alpha 160 kDa subunit (p160), is a mismatch repair protein homologous to bacterial MutS. It is a component of the post-replicative DNA mismatch repair system (MMR). It heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, it forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Mutations in MSH6 have been linked to increased cancer susceptibility, particularly in hereditary nonpolyposis colorectal cancer in humans. MSH6 contains a PWWP domain, but its role in MSH6 remains unclear. MSH6 orthologs found in Saccharomyces cerevisiae, Caenorhabditis elegans, and Arabidopsis thaliana lack the PWWP domain. PWWP domains typically recognize DNA and histone methylated lysines
FSPGDLVWAKLEGYPWWPSLVCNHPTTGFHKKFGKKGEVHVQFFDDPPSRAWVKAKNVKPFTGSDDKEFQ
KGGMFFSKDPKWKKAVKEADKALKLSVEERLKL
>gnl|CDD|438963 cd05838, PWWP_NSD_rpt2, second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins. The nuclear receptor binding SET domain (NSD) protein family consists of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising in suppressing cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play nonredundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). This model corresponds to the second PWWP domain. The family also includes Drosophila melanogaster maternal-effect sterile 4 (dMes4) that may act as a histone-lysine N-methyltransferase required for wing morphogenesis. The PWWP domain specifically recognizes DNA and histone methylated lysines
LYGDIVWVKLGNYRWWPAEILHPREVPDNIQSLPHPPGEFPVRFFGSHDYYWVHRGRVFLFEEGDKGSKE
KSKKSLDKSFKRALKEANEAFRELKA
>gnl|CDD|438964 cd05839, PWWP_BRPF, PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family. The BRPF family of proteins includes BRPF1, BRD1/BRPF2, and BRPF3. They are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, C2HC5HC2H, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PHD finger binds to lysine 4 of histone H3 (K4H3), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties
LEPGDLVWAKCRGYPWYPAEIVDPKDPKEGNGVPIPVPPDRVLKKSNEKLYLVLFFDAKRTWGWLPRNKL
RPLGVDEELDKLKLSEAKKSKRRKEVRKAYERACKH
>gnl|CDD|438965 cd05840, PWWP_ScIOC4-like, PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar proteins. ScIOC4 functions as a component of the ISW1B complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing. The family also includes Schizosaccharomyces pombe PWWP domain-containing proteins 1 and 2 (SpPDP1 and SpPDP2). SpPDP1 associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20. Members of this family contain a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines
GDLVLAKVKGYPPWPAMVLPEELLPKNVLKAKKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPLTKEEID
KFLSKSKRKNKDLIEAYEVALEPP
>gnl|CDD|438966 cd05841, PWWP_BS69-like, PWWP domain found in protein BS69, protein kinase C-binding protein 1 (PRKCBP1) and similar proteins. Protein BS69, also called zinc finger MYND domain-containing protein 11 (ZMYND11 or ZMY11), is a ubiquitously expressed nuclear protein acting as a transcriptional co-repressor in association with various transcription factors. It was originally identified as an adenovirus 5 E1A-binding protein that inhibits E1A transactivation, as well as c-Myb transcription. BS69 is a multi-domain protein, containing bromo, plant homeodomain (PHD), proline-tryptophan-tryptophan-proline (PWWP), and MYeloid translocation protein 8, Nervy and DEAF-1 (MYND) domains. The specific role of the PWWP domain within BS69 is not clearly identified, but BS69 functions in chromatin remodeling, consistent with other PWWP-containing proteins. PRKCBP1, also called cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor. They form a RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a PHD finger, a bromodomain, and a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines
KPCPVVHPLVWVKLDGFPFWPAKVMGTKDGQVDVRFFGDYDRAWLPSKNVTLHTREIVSTLPDSSESKDK
RTLKKAIKELERHIALLRQ
>gnl|CDD|320682 cd05843, Peptidase_M48_M56, Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral membrane metallopeptidases. This family contains peptidase M48 (also known as Ste24 peptidase, Ste24p, Ste24 endopeptidase, a-factor converting enzyme, AFC1), M56 (also known as BlaR1 peptidase) as well as a novel family called minigluzincins. Peptidase M48 belongs to Ste24 endopeptidase family. Members of this family include Ste24 protease (peptidase M48A), protease htpX homolog (peptidase M48B), or CAAX prenyl protease 1, and mitochondrial metalloendopeptidase OMA1 (peptidase M48C). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. The Ste24p contains multiple membrane spans, a zinc metalloprotease motif (HEXXH), and a COOH-terminal ER retrieval signal (KKXX). Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Ste24p has limited homology to HtpX family of prokaryotic proteins; HtpX proteins, also part of the M48 peptidase family, are smaller and homology is restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins; HtpX then undergoes self-degradation and collaborates with FtsH to eliminate these misfolded proteins. Peptidase M56 includes zinc metalloprotease domain in MecR1 and BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain beta-lactam antibiotics in MRSA. Also included are a novel family of related proteins that consist of the soluble minimal scaffold similar to the catalytic domains of the integral-membrane metallopeptidase M48 and M56, thus called minigluzincins
LKKIRQEILLSAGAFPLDKVVVVPGSVPNAFFTGGANKRVVLTTALLELLSEEELAAVIAHELGHFKAHE
YQADNVGARLFGKNELDAALLKLI
>gnl|CDD|340860 cd05844, GT4-like, glycosyltransferase family 4 proteins. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility
TVGIYRTVLLPVSETFIREQASGLRRYRPTFVGCRRLAPAPFDGVALRALGGSGPLRWLRQMAQRLLGWS
APRLGGAAGLAPALVHAHFGRDGVYALPLARALGVPLVVTFHGFDITTSRAWLAASPGWPSQFQRHRRAL
QRPAALFVAVSGFIRDRLLARGLPAERIHVHYIGIDPAKFAPRDPAERAPTILFVGRLVEKKGCDVLIEA
FRRLAARHPTARLVIAGDGPLRPALQALAAALGRVRFLGALPHAEVQDWMRRAEIFCLPSVTAASGDSEG
LGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVC
EQFDIRVQTAKLEAI
>gnl|CDD|409432 cd05845, IgI_2_L1-CAM_like, Second immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the second immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins. L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1 that involves abnormalities of axonal growth. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
KEKIDPVEVEEGDPVVLPCNPPKGAPPPRIYWMNSSLEHITQDERVSMGQNGDLYFSNVMEQDSHPDYIC
HAHFPGTRTIVQKEPITLKVL
>gnl|CDD|409433 cd05846, IgV_1_MRC-OX-2_like, First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains. The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion
VVVHTGDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGL
NSTSITIWNVTLEDEGCYKCLFNTFPDGIKSGTACLTV
>gnl|CDD|409434 cd05847, IgC1_CH2_IgE, CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the second constant domain of the heavy chain of immunoglobulin E (IgE). The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta, and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). The different classes of antibodies vary in their heavy chains; the IgE class has the epsilon type. This domain (Cepsilon2) of IgE is in place of the flexible hinge region found in IgG
PTVQILHSSCASTLTSETIQLLCLISGYTPSTIEVEWLVDGQVATLSAASTAPQKEEGGTFSTTSKLNVT
QEDWKSGKTYTCKVTHQGTTFEAHTKK
>gnl|CDD|409435 cd05848, IgI_1_Contactin-5, First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains. The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord. This group belongs to the I-set of IgSF domains
GPVFVQEPDDAIFPTDSDEKKVILNCEARGNPVPTYRWLRNGTEIDTESDYRYSLIDGNLIISNPSEVKD
SGRYQCLATNSIGSILSREALLQFAY
>gnl|CDD|409436 cd05849, IgI_1_Contactin-1, First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains. The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains
GPVFEEQPIDTIYPEESTEGKVSVNCRARANPFPIYKWRKNNLDIDLTNDRYSMVGGNLVINNPDKYKDA
GRYVCIVSNIYGKVRSREATLSFGY
>gnl|CDD|409437 cd05850, IgI_1_Contactin-2, First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains. The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module by contacts between IG domains 1 and 4, and domains 2 and 3. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-2 is also expressed in retinal amacrine cells in the developing chick retina, corresponding to the period of formation and maturation of AC processes. This group belongs to the I-set of IgSF domains
YGPVFEEQPSSTLFPEGSAEEKVTLACRARASPPATYRWKMNGTELKMEPDSRYRLVAGNLVISNPVKAK
DAGSYQCLASNRRGTVVSREASLRFGF
>gnl|CDD|143259 cd05851, IgI_3_Contactin-1, Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains
PADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKILEPMPATAEISMSGAVLKIFNIQPEDEGTYEC
EAENIKGKDKHQARVYVQ
>gnl|CDD|409438 cd05852, Ig5_Contactin-1, Fifth immunoglobulin (Ig) domain of contactin-1. The members here are composed of the fifth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma
PTFEFNPMKKKILAAKGGRVIIECKPKAAPKPKFSWSKGTELLVNNSRISIWDDGSLEILNITKLDEGSY
TCFAENNRGKANSTGVLSV
>gnl|CDD|409439 cd05853, Ig6_Contactin-4, Sixth immunoglobulin (Ig) domain of contactin-4. The members here are composed of the sixth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-4. Contactins are neural cell adhesion molecules, and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. Highest expression of contactin-4 is in testes, thyroid, small intestine, uterus, and brain. Contactin-4 plays a role in the response of neuroblastoma cells to differentiating agents, such as retinoids. The contactin 4 gene is associated with cerebellar degeneration in spinocerebellar ataxia type 16
DPTRVMVPPSSMDVTVGESIVLPCQVSHDHSLDIVFTWSFNGHLIDFQKDGDHFERVGGQDSAGDLMIRS
IQLKHAGKYVCMVQTSVDKLSAAADLIVRGPP
>gnl|CDD|409440 cd05854, Ig6_Contactin-2, Sixth immunoglobulin (Ig) domain of contactin-2. The members here are composed of the sixth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module by contacts between IG domains 1 and 4, and domains 2 and 3. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-2 is also expressed in retinal amacrine cells (AC) in the developing chick retina, corresponding to the period of formation and maturation of AC processes
DATKITLAPSSADINQGENLTLQCHASHDPTMDLTFTWSLDDFPIDLDKPNGHYRRMEVKETIGDLVIVN
AQLSHAGTYTCTAQTVVDSASASATLVVRGPP
>gnl|CDD|409441 cd05855, IgI_TrkB_d5, Fifth domain (immunoglobulin-like) of Trk receptor TrkB; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the fifth domain of Trk receptor, TrkB, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors, which mediate the trophic effects of the neurotrophin Nerve Growth Factor (NGF) family. Trks are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkB shares significant sequence homology and domain organization with TrkA and TrkC. The first three domains are leucine-rich domains while the fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrKB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. In some cell systems NT-3 can activate TrkA and TrkB receptors. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. This group belongs to the I-set of IgSF domains
PPTITFLELPTRDHHWCIPFTVKGNPKPTLQWFHEGAILNESEYICTKIHVINNTEYHGCLQLDNPTHLN
NGIYTLVAKNEYGEDEKNVSAHFM
>gnl|CDD|409442 cd05856, IgI_2_FGFRL1-like, Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains. The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors
PRFTQPAKMRRRVIARPVGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKKKKWTLSLKNLKPEDS
GKYTCHVSNRAGEINATYKVDV
>gnl|CDD|409443 cd05857, IgI_2_FGFR, Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains. The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans
PYWTNPEKMEKKLHAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVP
SDKGNYTCVVENEYGSINHTYHLDV
>gnl|CDD|409444 cd05858, IgI_3_FGFR2, Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
PILQAGLPANTSVVVGTDAEFVCKVYSDAQPHIQWLKHVEKNGSKYGPDGLPYVEVLKTAGVNTTDKEIE
VLYLRNVTFEDAGEYTCLAGNSIGISHHSAWLTVL
>gnl|CDD|409445 cd05859, Ig4_PDGFR, Fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR). The members here are composed of the fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR; also known as cluster of differentiation (CD) 140a) alpha and beta. PDGF is a potent mitogen for connective tissue cells. PDGF-stimulated processes are mediated by three different PDGFs (PDGF-A,PDGF-B, and PDGF-C). PDGFR alpha binds to all three PDGFs, whereas the PDGFR beta binds only to PDGF-B. PDGF alpha is organized as an extracellular component having five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. In mice, PDGFR alpha and PDGFR beta are essential for normal development
GFIALKPTFGQLEFANLHEVKEFVVEVEAYPPPQIRWLKDNRTLIENLTEITTSTRNVQETRYVSKLKLI
RAKEEDSGLYTALAQNEDAVKSYTFALQIQV
>gnl|CDD|409446 cd05860, IgI_4_SCFR, Fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR); member of the I-set of IgSF domains. The members here are composed of the fourth Immunoglobulin (Ig)-like domain in stem cell factor receptor (SCFR). SCFR is organized as an extracellular component having five IG-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. SCFR and its ligand SCF are critical for normal hematopoiesis, mast cell development, melanocytes, and gametogenesis. SCF binds to the second and third Ig-like domains of SCFR. This fourth Ig-like domain participates in SCFR dimerization, which follows ligand binding. Deletion of this fourth domain abolishes the ligand-induced dimerization of SCFR and completely inhibits signal transduction. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
GFINITPVDNTTIFVNAGENLDLRVEYEAYPKPEHQVWIYMNETLTNTSDHYVKSKTEGNNRYVSELHLT
RLKGTEGGIYTFLVSNSDASASVTFNVYVKT
>gnl|CDD|409447 cd05861, IgI_PDGFR-alphabeta, Immunoglobulin (Ig)-like domain of platelet-derived growth factor (PDGF) receptors (R), alpha and beta; member of the I-set of IgSF domains. The members here are composed of the immunoglobulin (Ig)-like domain of platelet-derived growth factor (PDGF) receptors (R), alpha (also known as cluster of differentiation (CD) 140a), and beta (also known as CD140b). PDGF is a potent mitogen for connective tissue cells. PDGF-stimulated processes are mediated by three different PDGFs (PDGF-A,PDGF-B, and PDGF-C). PDGFRalpha binds to all three PDGFs, whereas the PDGFRbeta binds only to PDGF-B. PDGFRs alpha and beta have similar organization: an extracellular component with five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. In mice, PDGFRalpha and PDGFRbeta are essential for normal development
SSINVEMEAVKTVVRQGETITLMCIVIGNEVVDLEWTYPGKESGRGIEPVEEFKVPPYHLVYTLTIPSAT
LEDSGTYECAVTEATNDHQDEKKINITVH
>gnl|CDD|409448 cd05862, IgI_VEGFR, Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); member of the I-set of IgSF domains. The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members, VEGFR-1 (also known as Flt-1), VEGFR-2 (also known as KDR or Flk-1) and VEGFR-3 (also known as Flt-4). VEGF_A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF, VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-2 and -1 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth
YDVQLSPPKPVELLVGEKLVLNCTARTELNVGVDFQWDYPGKKEQRRASVRRRRKQQSSEATEFSSTLTI
DNVTLSDKGLYTCAASSGPMFKKNSTSVIVHE
>gnl|CDD|409449 cd05863, IgI_VEGFR-3, Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3); member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-3 (Flt-4) binds two members of the VEGF family (VEGF-C and VEGF-D) and is involved in tumor angiogenesis and growth. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
PFISVEWRKGPVIEATAGDELVKLPVKVAAYPPPEFQWYKDGKLISGKHSPHSLQIKDVTEASAGTYTLV
LWNSAAGLEKRISLELIV
>gnl|CDD|409450 cd05864, IgI_VEGFR-2, Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-2 (KDR/Flk-1) is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A; VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGF-A also interacts with VEGFR-1, which it binds more strongly than VEGFR-2. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
FIALGSGMESLVEAKVGERVRIPVKYLGYPPPEIKWYKNGIPIESNHTIKAGHVLTIMEVTEKDAGNYTV
VLTNPISKEKQRHTFSLVV
>gnl|CDD|409451 cd05865, IgI_1_NCAM-1, First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
LQVDIVPSQGEISVGESKFFLCQVAGEAKDKDISWFSPNGEKLTPNQQRISVVRNDDYSSTLTIYNANID
DAGIYKCVVSNEDEGESEATVNVKIFQ
>gnl|CDD|409452 cd05866, IgI_1_NCAM-2, First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2 (OCAM/mamFas II, RNCAM). NCAM-2 is organized similarly to NCAM-1, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
LQVSISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIVSSQRVVVQKEGVRSRLTIYNANIEDAGI
YRCQATDAKGQTQEATVVLEIYQ
>gnl|CDD|409453 cd05867, Ig4_L1-CAM_like, Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM
YWTRRPQSHLYGPGETARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHVSSGALILTDVQPSDTAVYQ
CEARNRHGNLLANAHVHVV
>gnl|CDD|409454 cd05868, Ig4_NrCAM, Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). The members here are composed of the fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). NrCAM belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six IG-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. NrCAM is primarily expressed in the nervous system
YWITAPTNLVLSPGEDGTLICRANGNPKPSISWLTNGVPIEIAPTDPSRKVDGDTIIFSKVQERSSAVYQ
CNASNEYGYLLANAFVNVL
>gnl|CDD|143277 cd05869, IgI_NCAM-1, Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1). The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains
AKPKITYVENQTAMELEEQITLTCEASGDPIPSITWRTSTRNISSEEKTLDGHIVVRSHARVSSLTLKYI
QYTDAGEYLCTASNTIGQDSQSMYLEV
>gnl|CDD|143278 cd05870, IgI_NCAM-2, Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2). The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains
VQPHIIQLKNETTVENGAATLSCKAEGEPIPEITWKRASDGHTFSEGDKSPDGRIEVKGQHGESSLHIKD
VKLSDSGRYDCEAASRIGGHQKSMYLDI
>gnl|CDD|409455 cd05871, Ig_Sema3, Immunoglobulin (Ig)-like domain of class III semaphorin Sema3. The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G
NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYT
CQAVEHGFSQTLVKIRLHVIEP
>gnl|CDD|409456 cd05872, Ig_Sema4B_like, Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B. The members here are composed of the immunoglobulin (Ig)-like domain of Sema4B and similar proteins. Sema4B is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4B has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4B has been shown to preferentially regulate the development of the postsynaptic specialization at the glutamatergic synapses. This cytoplasmic domain includes a PDZ-binding motif upon which the synaptic localization of Sem4B is dependent. Sema4B is a ligand of CLCP1. CLCP1 was identified in an expression profiling analysis, which compared a highly metastic lung cancer subline with its low metastic parental line. Sema4B was shown to promote CLCP1 endocytosis and their interaction is a potential target for therapeutic intervention of metastasis
LPVKFRTVVAGADVVLPCQLRSNLASPVWLFNGTPLNAQFSYLRLGTDGLLILVTSPEHSGTYRCYSEEE
GFQQLVASYSLNVVEQ
>gnl|CDD|409457 cd05873, Ig_Sema4D_like, Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins. The members here are composed of the immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins. Sema4D is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4D has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4D plays a part in the development of GABAergic synapses. Sema4D in addition is an immune semaphorin. It is abundant on resting T cells; its expression is weak on resting B cells and antigen presenting cells (APCs), but is upregulated by various stimuli. The receptor used by Sema4D in the immune system is CD72. Sem4D enhances the activation of B cells and DCs through binding CD72, perhaps by reducing CD72s inhibitory signals. The receptor used by Sema4D in the non-lymphatic tissues is plexin-B1. Sem4D is anchored to the cell surface but its extracellular domain can be released from the cell surface by a metalloprotease-dependent process. Sem4D may mediate its effects in its membrane-bound form and/or its cleaved form
GDPRQRTFKLGGNAELKCSPKSNLARVVWKFQGKVLKAESPKYGLYGDGLLIFNASEADAGRYQCLSVEK
SKAKTFFQTVAKYVLEV
>gnl|CDD|409458 cd05874, IgI_NrCAM, Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the first immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule). NrCAM belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. NrCAM is primarily expressed in the nervous system
PTITHQSPKDYIVDPRENIVIQCEAKGKPPPSFSWTRNGTHFDIDKDPKVTMKPNTGTLVINIMNGEKAE
AYEGVYQCTARNERGAAVSNNIVIR
>gnl|CDD|409459 cd05875, IgI_hNeurofascin_like, Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the first immunoglobulin (Ig)-like domain of human neurofascin (NF). NF belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and a cytoplasmic domain. NF has many alternatively spliced isoforms having different temporal expression patterns during development. NF participates in axon subcellular targeting and synapse formation, however little is known of the functions of the different isoforms. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lacks a C" strand
PTITKQSAKDYIVDPRDNILIECEAKGNPVPTFHWTRNGKFFNVAKDPRVSMRRRSGTLVIDFRGGGRPE
DYEGEYQCFARNKFGTALSNKIRLQ
>gnl|CDD|409460 cd05876, Ig3_L1-CAM, Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM
SSSSLVALRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQNHNKTLQLLNVGESDDGEYVCLAENS
LGSARHAYYVTVE
>gnl|CDD|409461 cd05877, Ig_LP_like, Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains. The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes
ETVQAKVFSHRGGNVTLPCRYHYEPELSAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFL
RRADDLDASLVITDLRLEDYGRYRCEVIDGLEDESVVVALRLRGVVF
>gnl|CDD|409462 cd05878, Ig_Aggrecan_like, Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core protein (CSPG). The members here are composed of the immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core proteins (CSPGs). Included in this group are the Ig domains of other CSPGs: versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes
IPQSSPVRVLLGTSVTLPCYFIDPPHPVTPSTAPLAPRIKWSKVSVDGKKEKEVVLLVATEGRVRVNSAY
QGRVSLPNYPAIPSDATLEVQSLRASDSGLYRCEVMHGIEDSQDTVELVVKGVVF
>gnl|CDD|409463 cd05879, IgV_P0, Immunoglobulin (Ig)-like domain of protein zero (P0). The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin
IVVYTDREVYGTVGSDVTLSCSFWSSEWISDDISFTWHYQPDGSRDAISIFHYGKGQPYIDNVGPFKERI
EWVGNPSRKDGSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVTLYV
>gnl|CDD|409464 cd05880, IgV_EVA1, Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1. The members here are composed of the immunoglobulin (Ig) domain of epithelial V-like antigen 1 (EVA 1). EVA is also known as myelin protein zero-like 2. EVA is an adhesion molecule and may play a role in the structural organization of the thymus and early lymphocyte development
IEVYTSKEVEAVNGTDVRLKCTFSSSAPIGDTLVITWNFRPLDGGREESVFYYHKRPYPPPDGRFKGRVV
WDGNIMRRDASILIWQLQPTDNGTYTCQVKNPPDVHGPIGEIRLRV
>gnl|CDD|409465 cd05881, IgV_1_Necl-2, First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule 2; member of the V-set of Ig superfamily (IgSF) domains. The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of nectin-like molecule-2, Necl-2 (also known as cell adhesion molecule 1 (CADM1), SynCAM1, IGSF4A, Tslc1, sgIGSF, and RA175). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 - Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region, belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-2 has Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-2 is expressed in a wide variety of tissues and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma
LVTEDVTVVEGEVATISCRVKNSDDSVIQLLNPNRQTIYFRDFRPLKDSRFQLVNFSSSELRVSLTNVSI
SDEGRYFCQLYTDPPQEAYTTITV
>gnl|CDD|143290 cd05882, IgV_1_Necl-1, First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule-1 (Necl-1); member of the V-set of Ig superfamily (IgSF) domains. The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of nectin-like molecule-1, Necl-1 (also known as celll adhesion molecule 3 (CADM3), SynCAM2, or IGSF4). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 - Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 has Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons
QPVTQDETVAVGGTVTLKCGVKEHDNSSLQWSNTAQQTLYFGEKRALRDNRIQLVKSTPTELIISISNVQ
LSDEGEYTCSIFTMPVRTAKATVTV
>gnl|CDD|409466 cd05883, IgI_2_Necl-2, Second immunoglobulin (Ig)-like domain of nectin-like molecule 2 (Necl-2); member of the I-set of Ig superfamily domains. The members here are composed of the second immunoglobulin (Ig)-like domain of nectin-like molecule 2 (Necl-2; also known as cell adhesion molecule 1 (CADM1)). Nectin-like molecules (Necls) have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. Necl-2 has Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is expressed in a wide variety of tissues and is a putative tumour suppressor gene which is downregulated in aggressive neuroblastoma. Ig domains are likely to participate in ligand binding and recognition
LVPPRNLVIDIQKDTAVEGEEIELNCTAMASKPAATIRWFKGNKELTGKSEVEEWYSRMFTVTSQLMLKV
TKEDDGVPVICLVDHPAVKDLQTQRYLEV
>gnl|CDD|409467 cd05884, IgI_2_Necl-3, Second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3); member of the I-set of Ig superfamily domains. The members here are composed of the second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3; also known as cell adhesion molecule 2 (CADM2)). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Ig domains are likely to participate in ligand binding and recognition
VLGVPEKPQISGFTSPVMEGDHIQLTCKTSGSKPAADIRWFKNDKEVKDVKYLKAEDANRKTFTVSSSLD
FHVDRDDDGVAITCRVDHESLTATPQIAMQVLEI
>gnl|CDD|409468 cd05885, IgI_2_Necl-4, Second immunoglobulin (Ig)-like domain of nectin-like molecule-4 (Necl-4); member of the I-set of Ig superfamily domains. The members here are composed of the second immunoglobulin (Ig)-like domain of nectin-like molecule-4 (Necl-4; also known as cell adhesion molecule 4 (CADM4)). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1-Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. Ig domains are likely to participate in ligand binding and recognition. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. In injured peripheral nerve cells, the mRNA signal for both Necl-4 and Necl-5 was observed to be elevated. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression
LVAPENPVVEVREQAVEGGEVELSCLVPRSRPAATLRWYRDRKELKGVSSGQENGKVWSVASTVRFRVDR
KDDGGIVICEAQNQALPSGHSKQTQYVLDV
>gnl|CDD|409469 cd05886, IgV_1_Nectin-1_like, First immunoglobulin variable (IgV) domain of nectin-1, and similar domains. The members here are composed of the first immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1 (PVRL1) or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. In addition nectins heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls), nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D
QTVQVNDSMSGFIGTDVVLHCSFANPLPSVKITQVTWQKSTNGSKQNVAIYNPSMGVSVLPPYRERVTFL
NPSFTDGTIRLSRLELEDEGVYICEFATFPTGNRESQLNLTVM
>gnl|CDD|409470 cd05887, IgV_1_Nectin-3_like, First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains. The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis
GPIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGISIQGEYQGRVSFKNYS
LNDATITLHNVGFSDSGKYICKAVTFPLGNAQSSTTVTVL
>gnl|CDD|409471 cd05888, IgV_1_Nectin-4_like, First immunoglobulin (Ig) domain of nectin-4, and similar domains. The members here are composed of the first immunoglobulin (Ig) domain of nectin-4 (also known as poliovirus receptor related protein 4 or LNIR receptor). Nectin-4 belongs to the nectin family, which is comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example nectin-4 trans-interacts with nectin-1. Nectin-4 has also been shown to interact with the actin filament-binding protein, afadin. Unlike the other nectins, which are widely expressed in adult tissues, nectin-4 is mainly expressed during embryogenesis, and is not detected in normal adult tissue or in serum. Nectin-4 is re-expressed in breast carcinoma, and patients having metastatic breast cancer have a circulating form of nectin-4 formed from the ectodomain
DVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQEIALLHSKYGLHVFPAYEGRVEQPPPPRPA
DGSVLLRNAVQADEGEYECRVSTFPAGNFQAELRLRVL
>gnl|CDD|409472 cd05889, IgV_1_DNAM-1_like, First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains. The members here are composed of the first immunoglobulin (Ig) domain of DNAX accessory molecule 1 (DNAM-1, also known as CD226). DNAM-1 is a transmembrane protein having two Ig-like domains. It is an adhesion molecule which plays a part in tumor-directed cytotoxicity and adhesion in natural killer (NK) cells and T lymphocytes. It has been shown to regulate the NK cell killing of several tumor types, including myeloma cells and ovarian carcinoma cells. DNAM-1 interacts specifically with poliovirus receptor (PVR; CD155) and nectin -2 (CD211), other members of the Ig superfamily. DNAM-1 is expressed in most peripheral T cells, NK cells, monocytes and a subset of B lymphocytes
LVEEVLWDTSVPLSENMSLECVYPSTGILTQVEWTKIGGQKDNIAVYHPTHGMHIRKPYAGRVYFLNSTM
ASNNMSLSFRNASEDDVGYYSCSLYTYPQGSWEKVIQVVQS
>gnl|CDD|143298 cd05890, IgC1_2_Nectin-1_like, Second immunoglobulin (Ig) domain of nectin-1, and similar domains; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the second immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1, or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectin-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D
PTNRMEGTTAVLRAKKGQDDKVLVATCTSANGKPPSVVSWDTRLKGEAEFQEIRNPNGTVTVISRYRLVP
SREAHQQSLACIVNYHMDRFTDSLTLNV
>gnl|CDD|143299 cd05891, IgI_M-protein_C, C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers
GKVIGGLPDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKYASLTIKGVTSEDS
GKYSINVKNKYGGETVDVTVSV
>gnl|CDD|409473 cd05892, IgI_Myotilin_C, C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRICLLIQNANKKDA
GWYTVSAVNEAGVVSCNARLDV
>gnl|CDD|409474 cd05893, IgI_1_Palladin_C, First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTCSLHTTASTLDDD
GNYTIMAANPQGRISCTGRLMV
>gnl|CDD|409475 cd05894, Ig_C5_MyBP-C, C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain
AENTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTIT
VTNPVGEDHASLFVKV
>gnl|CDD|409476 cd05895, Ig_Pro_neuregulin-1, Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival
PKLKEMKSQEVAAGSKLVLRCETSSEYPSLRFKWFKNGKEINRKNKPENIKIQKKKKKSELRINKASLAD
SGEYMCKVSSKLGNDSASANVTI
>gnl|CDD|409477 cd05896, Ig1_IL1RAPL-1_like, First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory protein-like 1 (IL1RAPL-1), and similar domains. The members here are composed of the first immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory protein-like 1 (IL1RAPL-1). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. IL1RAPL is encoded by a gene on the X-chromosome, this gene is wholly or partially deleted in multiple cases of non-syndromic intellectual disability. This group also contains IL1RAPL-2 which is also encoded by a gene on the X-chromosome and is a candidate for another non-syndromic intellectual disability loci
TDWSVDLKKYMVLAGEPVRIKCALFYGYIRTNYSMAQSAGLSLMWYKSSGPGDFEEPIIFDGVRMSKEED
SIWFRPAELQDSGLYTCVLRNSTYCMKVSMSLTVA
>gnl|CDD|409478 cd05897, Ig2_IL1R2_like, Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar domains. The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds the IL-1 receptor, type II (IL1R2) represented in this group. Mature IL1R2 consists of three IG-like domains, a transmembrane domain, and a short cytoplasmic domain. It lacks the large cytoplasmic domain of mature IL1R1 and does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta
ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYY
TCKLTFTHEGKKYNITRSIELRIVK
>gnl|CDD|409479 cd05898, IgI_5_KIRREL3, Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 protein; member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 protein (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1). These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development. Neph1 and 2 may mediate axonal guidance and synapse formation in certain areas of the CNS. In the kidney they participate in the formation of the slit diaphragm
GPPIISSEQVQYAVRGERGKVKCFIGSTPPPDRIAWAWKENVLESGTLERYTVERTSTGSGVLSTLTINN
IMEADFQTHYNCTAWNSFGSGTAIIQLE
>gnl|CDD|409480 cd05899, IgV_TCR_beta, Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain. The members here are composed of the immunoglobulin (Ig) variable domain of the beta chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. This group includes the variable domain of the alpha chain of alpha/beta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology
VTQSPRYLIKRRGQSVTLRCSQKSGHDNMYWYRQDPGKGLQLLFYSYGGGLNEEGDLPGDRFSASRPSLT
RSSLTIKSAEPEDSAVYLCASSLGGGADEAYFGPGTRLTV
>gnl|CDD|409481 cd05900, Ig_Aggrecan, Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan. The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggrecan has a wide distribution in connective tissue and extracellular matrices. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes
IPLESPLRVVLGSSLLIPCYFQDPIAKDPGAPTVAPLSPRIKWSFISKEKESVLLVATEGKVRVNTEYLD
RVSLPNYPAIPSDATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF
>gnl|CDD|409482 cd05901, Ig_Versican, Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican. The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Like aggrecan, versican has a wide distribution in connective tissue and extracellular matrices. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes
VRKSSRVHGSLSGSVVLPCRFSTLPTLPPSYNITSEFLRIKWTKIQVDKNGKDHKETTVLVAQNGIIKIG
QEYMGRVSVPSHPEDQGDASLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSGVVF
>gnl|CDD|409483 cd05902, Ig_Neurocan, Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan. The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Unlike aggrecan which is widely distributed in connective tissue and extracellular matrices, neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes
RVTAPPVRRPLSSSVLLPCVFTLPPSASSPPEGPRIKWTKLSTSGGQQQRPVLVARDNVVRVAKAFQGRV
SLPGYPKNRYNASLVLSRLRYSDSGTYRCEVVLGINDEQDTVPLEVTGVVF
>gnl|CDD|341229 cd05903, CHC_CoA_lg, Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase). Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA
RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILR
RAKAKVFVVPERFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVA
SPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRL
RTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTG
ATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIP
VLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVAKQYWPERLVHVD
DLPRTPSGKVQKFRLRE
>gnl|CDD|341230 cd05904, 4CL, 4-Coumarate-CoA Ligase (4CL). 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids
LPTDLPLDSVSFLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEF
PVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSD
LLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPM
FHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQI
MSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPETG
ESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQV
APAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVD
AIPKSPSGKILRKEL
>gnl|CDD|341231 cd05905, Dip2, Disco-interacting protein 2 (Dip2). Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent
AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPI
EPPDISQQLGFLLGTCKVRVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKW
GPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCL
LSVYSGHHTILIPPELMKTNPLLWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMC
MVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRVNPFICWQGTSGPEPSRVYLDMRALRHGVVRLD
ERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTR
LSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRVHPYRGR
CAVFSITGLVVVVAEQPPGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQA
FLAGKLHPIYV
>gnl|CDD|341232 cd05906, A_NRPS_TubE_like, The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
PLHRPEGAPRTLLELLLRAAERGPTKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQ
FDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSG
LPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDV
FLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEE
IEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCSGVIYSRSFPTYDHSQA
LEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD
NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDAL
SETLRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQRSKLKAAFEAG
>gnl|CDD|341233 cd05907, VL_LC_FACS_like, Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases. This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (_C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions
GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIA
YILNDSEAKALFVEDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHV
FERRAGLYVPLLAGARIYFASSAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAVG
GRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADDGE
ILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENAL
KASPLISQAVVIGDGRPFLVALIVPDPEALEAWAEEHGIAYTDVAELAANPAVRAEIEAAVEAANARLSR
YEQIKKFLLLPEPFTIENGELTPTLKLKRPVI
>gnl|CDD|341234 cd05908, A_NRPS_MycA_like, The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA). The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
PEGIIFILGDKKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPV
SIGSNEEHKLKLNKVWNTLKNPYLITEEEVLCELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILN
STEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIVSSPNFGY
KYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEASVGASLPKA
QSPFKTITLGRRHVTHGEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNV
TPGYYNNPEATAKVFTDDGWLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGR
VVACGVNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGGWQINEVLPIRRIPKTTSGKVKRYEL
AQRYQSGEF
>gnl|CDD|341235 cd05909, AAS_C, C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas). Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases
EDTLGTSLTYRKLLTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLREL
RACIKLAGIKTVLTSKQFIEKLKLHHLFDVEYDARIVYLEDLRAKISKADKCKAFLAGKFPPKWLLRIFG
VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLP
LLSGIKVVFHPNPLDYKKIPELIYDKKATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQE
FQEKFGIRILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPN
VMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNE
VAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKNAGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA
>gnl|CDD|341236 cd05910, FACL_like_1, Uncharacterized subfamily of fatty acid CoA ligase (FACL). Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions
SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCL
QEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFG
PALGLTSVIPDMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAP
VPIALAARLRKMLSDEAEILTPYGATEALPVSSIGSRELLATTTAATSGGAGTCVGRPIPGVRVRIIEID
DEPIAEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFC
GRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELRALA
KDYPHTQRIGRFLIHPSFPVDIRHNAKIFREKLAVWA
>gnl|CDD|341237 cd05911, Firefly_Luc_like, Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL). This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light
AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYT
ADELAHQLKISKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPP
LKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLAS
LLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQE
LLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGP
QVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVA
DAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRGGVVFVDEIPKSASGKIL
>gnl|CDD|341238 cd05912, OSB_CoA_lg, O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE). O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center
SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLK
DSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSV
IYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILLGGGPAPKPLLEQCK
EKGIPVYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVGEILLKGPNVTKGYL
NRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIP
DDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ
>gnl|CDD|341239 cd05913, PaaK, Phenylacetate-CoA ligase (also known as PaaK). PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence
EEIETMSRDELDALQLARLKWTVRHAYENVPFYRRKFAAAGIDPDDIKSLDDLRKLPFTTKEDLRDNYPF
GLFAVPREKVVRIHASSGTTGKPTVVGYTKNDLDVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGF
HYGAERLGALVIPAGGGNTERQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPRELSLKVGIFGAEPW
TEEMRKRIERRLGIKAYDIYGLTEIIGPGVAFECEEKDGLHIWEDHFIPEIIDPETGEPVPPGEVGELVF
TTLTKEAMPLIRYRTRDITRLLPGPCPCGRTHRRIDRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGP
HYQLILTRQEHLDELTIKVEVRPEADDDEKLEALKQRLERHIKSVLGVTVEVELVEPGSLPRSEGKAKRV
IDKRK
>gnl|CDD|341240 cd05914, LC_FACL_like, Uncharacterized subfamily of fatty acid CoA ligase (FACL). The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions
LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADE
VHHILNHSEAKAIFVSDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLH
HIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPKLTLKKFKFK
LAKKINNRKIRKLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPN
RIRLGSAGKVIDGVEVRIDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEG
YLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPDFLDVKALKQRNIID
AIKWEVRDKVNQKVPNYKKISKVKIVKEEFEKTPKGKIKRFLY
>gnl|CDD|213283 cd05915, ttLC_FACS_like, Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles. This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS
LERAAALFGRKEVVSRLHTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVP
GMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEA
LGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNA
WCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGS
AAPRSLIARFERMGVEVRQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEG
RPVPKDGKALGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGE
WISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVF
AEEIPRTSAGKFLKRALRE
>gnl|CDD|341241 cd05917, FACL_like_2, Uncharacterized subfamily of fatty acid CoA ligase (FACL). Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions
PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGA
TMVFPSPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIE
VMNMKDVTIAYGMTETSPVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYS
VMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSD
VQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR
>gnl|CDD|341242 cd05918, A_NRPS_SidN3_like, The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS). The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVL
KAGGAFVPLDPSHPLQRLQEILQDTGAKVVLTSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGR
ALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPSVARLLD
PEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVD
PDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQEGSGRGRRLYRTGDLVRYNPDGS
LEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGD
SLFLEPSDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS
>gnl|CDD|341243 cd05919, BCL_like, Benzoate CoA ligase (BCL) and similar adenylate forming enzymes. This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP
KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLH
PDDYAYIARDCEARLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSA
KMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSL
RLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHT
IPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPV
EVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVD
ELPRTATGKLQRFKLR
>gnl|CDD|341244 cd05920, 23DHB-AMP_lg, 2,3-dihydroxybenzoate-AMP ligase. 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system
EFARRYRAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVV
QLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDRHAGFDHRALARELAESIPE
VALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACPGVLGTLLAGGRV
VLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLG
CTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGRPMSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYY
RAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAM
PDELLGERSCAFVVLRDPPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL
>gnl|CDD|341245 cd05921, FCS, Feruloyl-CoA synthetase (FCS). Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily
LAHWARQAPDRTWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAA
MYAGVPAAPVSPAYSLMSQDLAKLKHLFELLKPGLVFAQDAAPFARALAAIFPLGTPLVVSRNAVAGRGA
ISFAELAATPPTAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPV
LVDWLPWNHTFGGNHNFNLVLYNGGTLYIDDGKPMPGGFEETLRNLREISPTVYFNVPAGWEMLVAALEK
DEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALAVATVGERIPMMAGLGATETAPTATFTHWPTERSGLI
GLPAPGTELKLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLADPDDPAKGLVFDG
RVAEDFKLASGTWVSVGPLRARAVAACAPLVHDAVVAGEDRAEVGALVFPDLLACRRLVGLQEASDAEVL
RHAKVRAAFRDRLAALNGEATGSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYADT
P
>gnl|CDD|341246 cd05922, FACL_like_6, Uncharacterized subfamily of fatty acid CoA ligase (FACL). Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions
LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGG
RIVLADAGAADRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQ
NLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGL
AGVPSTYAMLTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPER
ILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLAR
RDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKIDPKDV
LRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR
>gnl|CDD|341247 cd05923, CBAL, 4-Chlorobenzoate-CoA ligase (CBAL). CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions
QTVFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIAL
LALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGP
LIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFA
VLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMP
DAVLERVNQHLPGEKVNIYGTTEAMNSLYMRDARTGTEMRPGFFSEVRIVRIGGSPDEALANGEEGELIV
AAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRH
PGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRASELADFKRPRRYFFLDELPKNAMNKVLR
RQL
>gnl|CDD|341248 cd05924, FACL_like_5, Uncharacterized subfamily of fatty acid CoA ligase (FACL). Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions
RSADDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHG
TGSWTAFGGLLGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLSSLFAIS
SGGALLSPEVKQGLLELVPNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVVLDDDGRVVPPG
SGGVGWIARRGHIPLGYYGDEAKTAETFPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFP
EEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEI
ERSPAGKADYRWAK
>gnl|CDD|341249 cd05926, FACL_fum10p_like, Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis. FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis
PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLN
PAYKKAEFEFYLADLGSKLVLTPKGELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNA
KSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLL
STLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPA
VLEALEATFGAPVLEAYGMTEAAHQMTSNPLPPGPRKPGSVGKPVGVEVRILDEDGEILPPGVVGEICLR
GPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPA
VLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRK
VAE
>gnl|CDD|341250 cd05927, LC-FACS_euk, Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS). The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells
GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEA
IEYILNHAEISIVFCDAGVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIV
SNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIKALKPTVFP
GVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLML
TGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAK
DPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAP
EKIENIYARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKGGGTGSFEELCKNPEVKKAILEDLV
RLGKENGLKGFEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMYK
>gnl|CDD|341251 cd05928, MACS_euk, Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM). MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12
VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRV
AVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKT
KLLVSEKSRDGWLNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYW
LDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRML
VQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASP
PYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWF
MGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQLTKELQ
QHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW
>gnl|CDD|341252 cd05929, BACL_like, Bacterial Bile acid CoA ligases and similar proteins. Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp
LEARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPA
YKSSRAPRAEACAIIEIKAAALVCGLFTGGGALDGLEDYEAAEGGSPETPIEDEAAGWKMLYSGGTTGRP
KGIKRGLPGGPPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLR
LIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTE
GQGLTIINGEEWLTHPGSVGRAVLGKVHILDEDGNEVPPGEIGEVYFANGPGFEYTNDPEKTAAARNEGG
WSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQ
PAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD
>gnl|CDD|341253 cd05930, A_NRPS, The adenylation domain of nonribosomal peptide synthetases (NRPS). The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPS
YPAERLAYILEDSGAKLVLTDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQF
TSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL
RLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLD
ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDD
QVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYM
VPSAFVVLDALPLTPNGKVDRKAL
>gnl|CDD|341254 cd05931, FAAL, Fatty acyl-AMP ligase (FAAL). FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin
RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLY
AGAIAVPLPPPTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAAD
WPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLL
TPLYSGGPSVLMSPAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRDEDLEGLDLSSWRVALNGA
EPVRPATLRRFAEAFAPFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLRVDRDALAGRAVAVAADDPA
ARELVSCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLR
TGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPGCVAAFSVPDDGEERLVVVAEVE
RGADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD
>gnl|CDD|341255 cd05932, LC_FACS_bac, Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase. The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions
GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTI
RYVLEHSESKALFVGKLDDWKAMAPGVPEGLISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLA
TLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFA
ESLDTFVEDVQRARPTLFFSVPRLWTKFQQGVQDKIPQQKLNLLLKIPVVNSLVKRKVLKGLGLDQCRLA
GCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISEDGEILVRSP
ALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRV
EMVCVIGSGLPAPLALVVLSEEARLRADAFARAELEASLRAHLARVNSTLDSHEQLAGIVVVKDPWSIDN
GILTPTLKIKRNVLEKAY
>gnl|CDD|341256 cd05933, ACSBG_like, Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS). This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions
KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPE
ACQYVAETSEANILVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEKEPNLYSWDEFMELGRSIPDEQL
DAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQ
ILDIWLPIKVGGQVYFAQPDALKGTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWA
KGVGLETNLKLMGGESPSPLFYRLAKKLVFKKVRKALGLDRCQKFFTGAAPISRETLEFFLSLNIPIMEL
YGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWGRHVFMGYLNMEDKTEEAIDED
GWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGDKRKFLSMLLTL
KCEVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQKWV
ILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY
>gnl|CDD|341257 cd05934, FACL_DitJ_like, Uncharacterized subfamily of fatty acid CoA ligase (FACL). Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins
GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYI
IDHSGAQLVVVDPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVS
VLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPEL
HEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGL
RGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPA
VREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQ
LR
>gnl|CDD|341258 cd05935, LC_FACS_like, Putative long-chain fatty acid CoA ligase. The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters
SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILN
DSGAKVAVVGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGF
VGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAP
MPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIPXFGVDARVIDIETGRELPPNEVGE
IVVRGPQIFKGYWNRPEETEESFIEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEA
KLYKHPAIXEVCVISVPDERVGEEVKAFIVLRPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRS
ASGKILWRLL
>gnl|CDD|341259 cd05936, FC-FACS_FadD_like, Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD. This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions
LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGAL
KAGAVVVPLNPLYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVP
KGAMLTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLK
EIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETS
PVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGW
LRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL
KEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR
>gnl|CDD|341260 cd05937, FATP_chFAT1_like, Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi. Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus
FEGKTWTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPL
IHCLKLSGSRFVIVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHG
TAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGN
GLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQVVLVKMDPETD
DPIRDPKTGFCVRAPVGEPGEMLGRVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDA
DGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESSAVPTEF
TKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP
>gnl|CDD|341261 cd05938, hsFATP2a_ACSVL_like, Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis
FEGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSL
LHCFRCCGAKVLVVAPELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRAH
VTIKSPALYIYTSGTTGLPKAARISHLRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELG
ATCVLKPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRF
GPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPG
LLVAKITQQSPFLGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVA
TTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQD
SLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTPDIY
>gnl|CDD|341262 cd05939, hsFATP4_like, Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins. Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis
DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHC
ITVSKAKALIFNLLDPLLTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAF
GMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQ
PPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVY
PIRLIKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFKKGDSA
FLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIV
DPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGYDP
>gnl|CDD|341263 cd05940, FATP_FACS, Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes. Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis
DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHC
LNVSSAKHLVVDAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVG
WSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLRPDI
WEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLALVKYDLESGEPIRDAEGRCI
KVPRGEPGLLISRINPLEPFDGYTDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFR
WKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARP
LFLRLQPEMEITGTFKQQKVDLRNEGFDP
>gnl|CDD|341264 cd05941, MCS, Malonyl-CoA synthetase (MCS). MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility
DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPS
YPLAELEYVITDSEPSLVLDPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLH
HVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAA
AERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDE
ETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSG
GYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELKEWAKQRLAPYKRPRR
LILVDELPRNAMGKVNKKELRK
>gnl|CDD|341265 cd05943, AACS, Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS). AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol
MDAFRRWVNARHGLSLADYAALHRWSVDDPGAFWAAVWDFSGVRGSKPYDVVVVSGRIMPGARWFPGARL
NYAENLLRHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAM
LATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVVP
YTVAAGQPDLSKIAKALTLEDFLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLK
EHILHCDLRPGDRLFYYTTCGWMMWNWLVSGLAVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAK
YLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKPDVLLASISGGTDIISCFVGGNPLLP
VYRGEIQCRGLGMAVEAFDEEGKPVWGEKGELVCTKPFPSMPVGFWNDPDGSRYRAAYFAKYPGVWAHGD
WIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVE
LDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRPVKNAGALANPESLDLF
>gnl|CDD|341266 cd05944, FACL_like_4, Uncharacterized subfamily of fatty acid CoA ligase (FACL). Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions
SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGA
HVVLAGPAGYRNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRAR
FEDATGLPVVEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLLRDCAPDEVGEICV
AGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPA
VAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKP
ALRADAIHR
>gnl|CDD|341267 cd05945, DltA, D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins. This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP
LDASSPAERIREILDAAKPALLIADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDV
FLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTP
ESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGYAKPG
AKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRAYRTGDLVRLEADGLLFYRG
RLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTKAIKAELAER
LPPYMIPRRFVYLDELPLNANGKIDRKAL
>gnl|CDD|341268 cd05958, ABCL, 2-aminobenzoate-CoA ligase (ABCL). ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer
RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLL
RPKELAYILDKARITVALCAHALTASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDD
RFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGP
DLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD
DEGNPVPDGTIGRLAVRGPTGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNI
APPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIE
FVTELPRTATGKLQRFALR
>gnl|CDD|341269 cd05959, BCL_4HBCL, Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase). Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process
EKYNAATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTA
FLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAG
ALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFS
AAKLFFAYGLGNSLTFPLSVGATTVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLS
SLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDG
GDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVS
PFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVF
VDELPKTATGKIQRFKLR
>gnl|CDD|341270 cd05966, ACS, Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme). Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation
EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHLKERGDKV
AIIWEGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVF
AGFSAESLADRINDAQCKLVITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTGGEVPMTEGRDL
WWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTA
DIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKH
DLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIE
PAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGR
VDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRK
EIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEEELGDTSTLAD
>gnl|CDD|341271 cd05967, PrpE, Propionyl-CoA synthetase (PrpE). EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency
YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILDNSNPPFTRWFVGGRLNTCYNALDRHVEAGRGDQIAL
IYDSPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGG
FAAKELASRIDDAKPKLIVTASCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQVPADLTKPGRDL
DWSELLAKAEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASD
VGWVVGHSYIVYGPLLHGATTVLYEGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYIK
KYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEPLPIKAGSPGKPVPGY
QVQVLDEDGEPVGPNELGNIVIKLPLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIM
GRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELVAL
VREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDPSVLDEI
>gnl|CDD|341272 cd05968, AACS_like, Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase. This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms
MASLGIPDLEAFLERSAEDNAWFWGEFVKDVGIEWYEPPYQTLDLSGGKPWAAWFVGGRMNIVEQLLDKW
LADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIG
GIVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFT
PAKGRDLSYDEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDL
LTWFTDLGWMMGPWLIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAP
VNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEISGGILGNVLIKPIKPSSFNGPVP
GMKADVLDESGKPARPEVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYIL
GRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERV
ADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKELGDLSSLENP
>gnl|CDD|341273 cd05969, MACS_like_4, Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS). This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria
YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLEN
SEAKVLITTEELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPG
WVTGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLR
FIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNE
LPPGTKGILALKPGWPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG
PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEF
VDNLPKTRSGKIMRRVLKAKEL
>gnl|CDD|341274 cd05970, MACS_AAE_MA_like, Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like. MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids
YEDFHNNFSINVPENFNFAYDVVDAMAKEYPDKLALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIG
KGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEIEKAAP
ECPSKPKLVWVGDPVPEGWIDFRKLIKNASPDFERPTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTYP
LGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTF
CAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEP
KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDAEKTAEVWHDGYYHTGDAA
WMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPS
EELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD
>gnl|CDD|341275 cd05971, MACS_like_3, Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS). MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria
KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEAL
EYRLSNSGASALVTDGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPADW
AWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLR
AIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTP
LPPGEVGEIAVELPDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIG
PAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEF
VNELPRTATGKIRRRELRA
>gnl|CDD|341276 cd05972, MACS_like, Medium-chain acyl-CoA synthetase (MACS or ACSM). MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes
WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEA
AGAKAIVTDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSS
FFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRLVVSAGEPLN
PEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAI
KLPPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEH
PAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGK
IRRVELRD
>gnl|CDD|341277 cd05973, MACS_like_2, Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS). MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria
LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRT
SGARLVVTDAANRHKLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGW
AYGLYYAITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRV
SSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDEL
GPGEPGRLAIDIANSPLMWFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPF
DVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVD
ELPKTPSGKIQRFLLRR
>gnl|CDD|341278 cd05974, MACS_like_1, Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS). MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria
VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDR
GGAVYAAVDENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWNISSPGWAKH
AWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREVVGAGE
PLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVAL
DLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVL
IEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFAELPKTIS
GKIRRVELRRRE
>gnl|CDD|99716 cd05992, PB1, The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants
VRVKVKYGGEIRRFVVVSRSISFEDLRSKIAEKFGLDAVSFKLKYPDEDGDLVTISSDEDLEEAIEEARR
SGSKKLRLFVF
>gnl|CDD|100076 cd06006, R3H_unknown_2, R3H domain of a group of fungal proteins with unknown function. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner
CQQIESTLRKFINDKSKRSLRFPPMRSPQRAFIHELAKDYGLYSESQDPEPKRSVFVKK
>gnl|CDD|100077 cd06007, R3H_DEXH_helicase, R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may function as ATP-dependent DNA or RNA helicases. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner
RIAINKALEDFRASDNEEYEFPSSLTNHERAVIHRLCRKLGLKSKSKGKGSNRRLSVYK
>gnl|CDD|100116 cd06008, NF-X1-zinc-finger, Presumably a zinc binding domain, which has been shown to bind to DNA in the human nuclear transcriptional repressor NF-X1. The zinc finger can be characterized by the pattern C-X(1-6)-H-X-C-X3-C(H/C)-X(3-4)-(H/C)-X(1-10)-C. The NF-X1 zinc finger co-occurs with atypical RING-finger and R3H domains. Human NF-X1 is involved in the transcriptional repression of major histocompatibility complex class II genes. The drosophila homolog encoded by stc (shuttle craft) plays a role in embryonic development, and the Arabidopsis homologue AtNFXL1 has been shown to function in the response to trichothecene and other defense mechanisms
CGEVCGKPLPCGNHKCEQLCHEGPCPPCPETVKKKCRCGKTTKEVPCGE
>gnl|CDD|276963 cd06059, Tubulin, The tubulin superfamily and related homologs. The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins. Also included in this group is the mitochondrial Misato/DML1 protein family, involved in mitochondrial fusion and in mitochondrial distribution and morphology
EIITIQVGQCGNQIGDRFWELARAVLVDMEEGVINEVLKGPLGQLFDPNQFVTGVSGAGNNWAVGYYVYG
PKYIESILDRIRKQVEKCDSLQGFFILHSLGGGTGSGLGSYLLELLEDEYPKVYRFTFSVFPSPDDDNVI
TSPYNSVLALNHLTEHADCVLPIDNEALYDICNRQPATLDIDFPPFDDMNNLVAQLLSSLTSSLRFEGSL
NVDLNEITTNLVPFPRLHFLLPSLSPLTSANDVTLEPLTLDQLFSDLFSKDNQLVGCDPRHGTYLACALL
LRGKVFSLSDVRRNIDRIKPKLKFISWNPDGFKVGLCSVPPVGQKYSLLFLSNNTSIASTFERLIERFDK
LYKRKAFLHHYTGEGMEEGDFSEARESLANLIQEYQE
>gnl|CDD|276964 cd06060, misato, Misato segment II tubulin-like domain. Human Misato shows similarity with Tubulin/FtsZ family of GTPases and is localized to the the outer membrane of mitochondria. It has a role in mitochondrial fusion and in mitochondrial distribution and morphology. Mutations in its Drosophila homolog (misato) lead to irregular chromosome segregation during mitosis. Deletion of the budding yeast homolog DML1 is lethal and unregulate expression of DML1 leads to mitochondrial dispersion and abnormalities in cell morphology. The Misato/DML1 protein family is conserved from yeast to human, but its exact function is still unknown
REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPPDHDVHDVLFREGETLQGEETYTPRLLLVDLKGS
LGSLRKEGALYEEPDDDSSESQWWGDVETHVQEPIEKNEFQQDLEEEETYQVELESQSTAEDGDKVYLLE
ESVRVWSDYLRVYYHPRSINVLNEYQHDSEFNPFDNFSQGEELFSDLEELEEFEDRLRFFVEECDSLQGF
QILVDTDDGFGGVAAKLLENLRDEYGKKSILTPGLSPASPPDPDSQRRIKRLLNDALSLSSLSEHSSLFV
PLSLPSLLWRKPGWPRTFPHLDYSSPYHTSAVLAAALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAAL
SLALPFPLLLGSSLLDSLQDLLGDLSLTPSCQNETDVFAQSVVLRGIPESRLKSPLQPRSPASRCSSVEE
VLEGYLQCTFPGSSSAVTTLPQPLPVPTPFPSIFSPSLGRKGFLLDDSRPASLDVESVPVLASLQSSSAL
GPLLEELASEVEKLGLRKLHEFLGGGGLERDEFKESLEELLSLADCYGD
>gnl|CDD|100037 cd06061, PurM-like1, AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain
KIGKLPPEFLKRLILKNLGADRDEVLVGPGGGEDAAVVDFGGKVLVVSTDPITGAGKDAGWLAVHIAAND
IATSGARPRWLLVTLLLPPGTDEEELKAIMREINEAAKELGVSIVGGHTEVTPGVTRPIISVTAIGKGEK
DKLVTPSGAKPGDDIVMTKGAGIEGTAILANDFEEELKKRLSEEELREAAKLFYKISVVKEALIAAEAGV
TAMHDATEGGILGALWEVAEASGVGLRIEKDKIPIRQETKEICEALGIDPLRLISSGTLLITVPPEKGDE
LVDALEEAGIPASVIGKI
>gnl|CDD|99873 cd06062, H2MP_MemB-H2up, Endopeptidases belonging to membrane-bound hydrogenases group. These hydrogenases transfer electrons from H2 to a cytochrome that is bound to a membrane-located complex coupling electron transfer to transmembrane proton translocation. Endopeptidase HybD from E. coli is well studied in this group. Maturation of [NiFe] hydrogenases include proteolytic processing of large subunit, assembly with other subunits, and formation of the nickel metallocenter. Hydrogenase maturation endopeptidase (HybD) cleaves a short C-terminal peptide after a His or an Arg residue in the large subunit (pre-HybC) of hydrogenase 2 (hyb operon) in E. coli. This cleavage is nickel dependent. A variety of endopeptidases belong to this group that are similar in function and sequence homology. They include such proteins as HynC, HoxM, and HupD
ILVLGIGNILLADEGIGVHAVERLEENYSFPENVELIDGGTLGLELLPYIEEADRLIIVDAVDAGGPPGT
VYRFEGEDVPAFLSAKLSAHQVGLLEVLALAELLGDLPPEIVLIGVQPESIEWGLELSPEVAAALPTAIE
AVLAEL
>gnl|CDD|99874 cd06063, H2MP_Cyano-H2up, This group of endopeptidases include HupW enzymes that are specific to the cyanobacterial hydrogenase and are involved in the C-terminal cleavage of the hydrogenase large subunit precursor protein. Cyanobacterial nickel-iron (NiFe)-hydrogenases are found exclusively in the N2-fixing strains and are encoded by hup (hydrogen uptake) genes. These uptake hydrogenases are heterodimers with a large (hupL) and small subunit (hupS) and catalyze the consumption of the H2 produced during N2 fixation. Sequence similarity shows that the putative metal-binding resides are well conserved in this group of hydrogen maturation proteases. This group also includes such proteins as the hydrogenase III from Aquifex aeolicus
LTIIGCGNLNRGDDGVGPILIRRLQAYLLPPHVRLVDCGTAGMEVMFRARGAKQLIIIDASSTGSEPGAV
FEVPGEELEALPEPSYNLHDFRWDHALAAGRKIFGDDFPKDVTVYLIEAKSLDFGLELSPPVKQAAERVA
EMIIKE
>gnl|CDD|99875 cd06064, H2MP_F420-Reduc, Endopeptidases belonging to F420-reducing hydrogenases group. These hydrogenases from methanogens are encoded by the fru, frc, or frh genes. Sequence comparison indicates that fruD and frcD gene products from Methanococcus voltae are similar to HycI protease of Escherichia coli and are putatively involved in the C-terminal processing of large subunits (FruA and FrcA respectively). FrhD (F420 reducing hydrogenase delta subunit) enzyme belongs to the gene cluster of 8-hydroxy-5-deazaflavin (F420) reducing hydrogenase (FRH) from the thermophilic methanogen Methanobacterium thermoautotrophicum delta H. FrhD subunit is putatively involved in the processing of the coenzyme F420 hydrogenase-processing. It is similar to those frhD genes found in Methanomicrobia and Methanobacteria. It is different from the FrhD conserved domain found in methyl viologen-reducing hydrogenase and F420-non-reducing hydrogenase iron-sulfur subunit D
LVVGCGNILFGDDGFGPAVIEELEKLELLPDNVQVIDAGTGAPHLLFTLLDEESKPKKIIIVDAIDFGLE
PGTLKKISVDELPPGKYYDFDAHSWPLADPLHELKDKYGIEIVVIGCQPKRVPEPDVEPGLSEEVEKAVP
KAVEIILEEL
>gnl|CDD|99876 cd06066, H2MP_NAD-link-bidir, Endopeptidases that belong to the bidirectional NAD-linked hydrogenase group. This group of endopeptidases are highly specific carboxyl-terminal protease (HoxW protease) which releases a 24-amino-acid peptide from HoxH prior to progression of subunit assembly. These bidirectional hydrogenases are heteropentamers encoded by the hox (hydrogen oxidation) genes, in which complex HoxEFU shows the diaphorase activity, and HoxYH constitutes the NiFe-hydrogenase
LVIGYGNPLRGDDGLGPAVAERIEEWLLPGVEVLAVHQLTPELAEDLAGADRVIFIDASLGGSPAPFRIV
RLEPRRDSSFTSHALSPAALLALAQALYGHAPPAWLLTIPGYNFELGEPLSPAAEAALAAALELLRKLL
>gnl|CDD|99877 cd06067, H2MP_MemB-H2evol, Endopeptidases belonging to membrane-bound hydrogen evolving hydrogenase group. In hydrogenase 3 from E coli, the maturation of the large subunit (HycE) requires the cleavage of a C-terminal peptide by the endopeptidase HycI, before the final formation of the [NiFe] metallocenter. HycI protease is a monomer and lacks characteristic signature motifs of serine, zinc, cysteine, or acid proteases and thus its cleavage reaction is not inhibited by conventional inhibitors of serine and metalloproteases. Such hydrogenases as those from Methanosarcina barkeri (EchCE) and Rhodospirillum rubrum (CooLH) also belong to this group of membrane-bound hydrogen evolving hydrogenase. Sequence comparison of the large subunits from related hydrogenase indicates that in contrast to EchE (358 amino acids) and CooH (361 amino acids), the large subunit HycE (569 amino acids) contains an extra carboxy-terminal stretch of 32 amino acids that is cleaved during the maturation process. In the absence of this C-terminal stretch, there is no homolog of endopeptidase HycI found in these two related hydrogenase
VLLGVGNELRGDDGAGPLLAEKLEDLPNPNWLVIDGGTVPENFTGKIREEKPDLIVIVDAADMGLEPGEI
RIIDPEEIAEYFFSTHTLPLSILIDYLRESTGAEVIFLGIQPENLEFGEPLSPEVKDAAEELAKLL
>gnl|CDD|99878 cd06068, H2MP_like-1, Putative [NiFe] hydrogenase-specific C-terminal protease. Sequence comparison shows similarity to hydrogenase specific C-terminal endopeptidases, also called Hydrogen Maturation Proteases (H2MP). Maturation of [FeNi] hydrogenases includes formation of the nickel metallocenter, proteolytic processing and assembly with other subunits. Hydrogenase maturation endopeptidases are responsible for the proteolytic processing, liberating a short C-terminal peptide by cleaving after a His or an Arg residue, e.g., HycI (E. coli) is involved in processing of HypE (the large subunit of hydrogenases 3). This cleavage is nickel dependent
LVAGVGNIFLGDDGFGVEVARRLRPRQLPPGVRVADFGIRGIHLAYELLDGYDTLILVDAVPRGGEPGTL
YVIELEDVDAAPELLDAHGMNPDAVLALLRALGGTPPRVVVVGCEPADVDEGIGLSEPVAAAVPEAVRLV
RDVV
>gnl|CDD|99879 cd06070, H2MP_like-2, Putative [NiFe] hydrogenase-specific C-terminal protease. Sequence comparison shows similarity to hydrogenase specific C-terminal endopeptidases, also called Hydrogen Maturation Proteases (H2MP). Maturation of [FeNi] hydrogenases includes formation of the nickel metallocenter, proteolytic processing and assembly with other subunits. Hydrogenase maturation endopeptidases are responsible for the proteolytic processing, liberating a short C-terminal peptide by cleaving after a His or an Arg residue, e.g., HycI (E. coli) is involved in processing of HypE (the large subunit of hydrogenases 3). This cleavage is nickel dependent
LIIGVGNRLYGDDGFGSCLAEALEQCGAPVFDGGLDGFGLLSHLENYDIVIFIDVAVIDEDVGVFKITPE
PASVAEQISFETDAHRLGPAHLLLLLKSSGRRPKAYIVGVKPESIEFARGLSEAVIARAEKALEELKKLL
>gnl|CDD|100117 cd06071, Beach, BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in a family of proteins conserved throughout eukaryotes. This group contains human lysosomal trafficking regulator (LYST), LPS-responsive and beige-like anchor (LRBA) and neurobeachin. Disruption of LYST leads to Chediak-Higashi syndrome, characterized by severe immunodeficiency, albinism, poor blood coagulation and neurologic problems. Neurobeachin is a candidate gene linked to autism. LBRA seems to be upregulated in several cancer types. It has been shown that the BEACH domain itself is important for the function of these proteins
TKKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERL
QLLKERYESDSDDSDPPFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWRSAS
ENPSDVKELIPEFYYLPEFFLNINKFDFGKQDGEKVNDVELPPWAKSPEEFIRKHREALESEYVSKNLHH
WIDLIFGYKQRGEEAVKAKNVFHPLTYEGSVDLDSIDVEREAIEAQINNFGQTPVQLFTKPHPKR
>gnl|CDD|438967 cd06080, PWWP_MUM1-like, PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins. MUM-1, also called PWWP domain-containing DNA repair factor 3A (PWWP3A), or protein expandere (EXPAND1), is a melanoma-associated antigen (MAA) that belongs to the mutated or aberrantly expressed type of MAAs, along with antigens such as CDK4, beta-catenin, gp100-in4, p15, and N-acetylglucosaminyltransferase V. It is highly expressed in several types of human cancers and involved in the DNA damage response pathway by contributing to the maintenance of chromatin architecture. MUM-1 is recruited to the vicinity of DNA breaks by TP53BP1 and plays an accessory role to facilitate damage-induced chromatin changes and promoting chromatin relaxation. It is required for efficient DNA repair and cell survival following DNA damage. This subfamily also includes mutated melanoma-associated antigen 1-like protein 1 (MUM1L1), also called MUM1-like protein 1, or PWWP domain-containing DNA repair factor 3B (PWWP3B). Its biological function remains unclear. The PWWP domain specifically recognizes DNA and histone methylated lysines
FSKGDIVWAKYRKYPYWPAVVKSVYKKPKKASVLFLELPPEKKGIKVSLKKLKPFDCKEKEELLEEGKES
PYSEDFKEAVELAEDYLIKK
>gnl|CDD|240505 cd06081, KOW_Spt5_1, KOW domain of Spt5, repeat 1. Spt5, an eukaryotic ortholog of NusG, contains multiple KOW motifs at its C-terminus. Spt5 is involved in transcription elongation and termination. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. KOW_Spt5 domains play critical roles in recruitment of multiple other eukaryotic transcription elongation and RNA biogenesis factors and additionally are involved in the binding of the eukaryotic Spt5 proteins to RNA polymerases
GSWVRIKRGIYKGDLAQVDEVDENGNRVVVKLIPRIDY
>gnl|CDD|240506 cd06082, KOW_Spt5_2, KOW domain of Spt5, repeat 2. Spt5, an eukaryotic ortholog of NusG, contains multiple KOW motifs at its C-terminus. Spt5 is involved in transcription elongation and termination. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. KOW_Spt5 domains play critical roles in recruitment of multiple other eukaryotic transcription elongation and RNA biogenesis factors and additionally are involved in the binding of the eukaryotic Spt5 proteins to RNA polymerases
FQPGDNVEVIEGELKGLQGKVESVDGDIVTIMPKHEDLKEPLEFPAKELRK
>gnl|CDD|240507 cd06083, KOW_Spt5_3, KOW domain of Spt5, repeat 3. Spt5, an eukaryotic ortholog of NusG, contains multiple KOW motifs at its C-terminus. Spt5 is involved in transcription elongation and termination. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. KOW_Spt5 domains play critical roles in recruitment of multiple other eukaryotic transcription elongation and RNA biogenesis factors and additionally are involved in the binding of the eukaryotic Spt5 proteins to RNA polymerases
HFKVGDHVKVISGRHEGETGLVVKVEDDVVTVFSDLTMRELKVFPRDLQLS
>gnl|CDD|240508 cd06084, KOW_Spt5_4, KOW domain of Spt5, repeat 4. Spt5, an eukaryotic ortholog of NusG, contains multiple KOW motifs at its C-terminus. Spt5 is involved in transcription elongation and termination. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. KOW_Spt5 domains play critical roles in recruitment of multiple other eukaryotic transcription elongation and RNA biogenesis factors and additionally are involved in the binding of the eukaryotic Spt5 proteins to RNA polymerases
GDTVKVVDGPYKGRQGTVLHIYRGTLFLHSREVTENGGIFVVR
>gnl|CDD|240509 cd06085, KOW_Spt5_5, KOW domain of Spt5, repeat 5. Spt5, an eukaryotic ortholog of NusG, contains multiple KOW motifs at its C-terminus. Spt5 is involved in transcription elongation and termination. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. KOW_Spt5 domains play critical roles in recruitment of multiple other eukaryotic transcription elongation and RNA biogenesis factors and additionally are involved in the binding of the eukaryotic Spt5 proteins to RNA polymerases
GRDPLIGKTVRIRKGPYKGYIGIVKDATGTTARVELHSKNKTITVDRSRLAV
>gnl|CDD|240510 cd06086, KOW_Spt5_6, KOW domain of Spt5, repeat 6. Spt5, an eukaryotic ortholog of NusG, contains multiple KOW motifs at its C-terminus. Spt5 is involved in transcription elongation and termination. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. KOW_Spt5 domains play critical roles in recruitment of multiple other eukaryotic transcription elongation and RNA biogenesis factors and additionally are involved in the binding of the eukaryotic Spt5 proteins to RNA polymerases
EHLEPVPPEKGDRVKVIKGEDRGSTGELISIDGADGIVKMDSDGDIKILPMNFLAKLV
>gnl|CDD|240511 cd06087, KOW_RPS4, KOW motif of Ribosomal Protein S4 (RPS4). RPS4 plays a critical role in the core assembly of the small ribosomal subunit with a KOW motif at its C-terminal. RPS4 also acts as a general transcription antiterminator factor and regulates ribosomal RNA expression level. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. RPS4 deficiency in human has been associated with Turner syndrome. Archeae RPS4 (RPS4e) showed substantial identity to the eukaryotic equivalents RPS4, but the archaeal proteins formed a different complex from the eukaryotic proteins
FEEGNLAMVTGGRNVGRVGVIKEIERHKGSFDIVHVKDAAGNEFATRLSNVFVIG
>gnl|CDD|240512 cd06088, KOW_RPL14, KOW motif of Ribosomal Protein L14. RPL14 is a component of the large ribosomal subunit in both archaea and eukaryotes with KOW motif at its N terminal. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. Auto-antibodies to RPL14 in humans have been associated with systemic lupus erythematosus . Although RPL14 is well conserved, it is not found in all archaea, and therefore it is presumably not essential
VEIGRVVLSKAGRDKGKLYVIVDIIDENVVLVDGPLRTGVKPKKKNLKHLQLTDFVIDIPRGARTKGVKK
ANEKLR
>gnl|CDD|240513 cd06089, KOW_RPL26, KOW motif of Ribosomal Protein L26. RPL26 and its bacterial paralogs RPL24 have a KOW motif at their N terminal. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. RPL26 makes a very minor contributions to the biogenesis, structure, and function of 60s ribosomal subunits. However, RPL24 is essential to generate the first intermediate during 50s ribosomal subunits assembly. RPL26 have an extra-ribosomal function to enhances p53 translation after DNA damage
GDEVQVIRGKDKGKQGKVLKVDRKKNRVIVEGVNVVKKHVKPSQENPQGGIIEVEAPIHISNVML
>gnl|CDD|240514 cd06090, KOW_RPL27, KOW motif of eukaryotic Ribosomal Protein L27. RPL27e has a KOW motif at its N terminal. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4
KPGKVVIVLSGRYAGKKAVIVKNNDEGTKDRPYGHALVAGIDRYPRKVTKKMSKKKIAKRSKVKPFVKVV
NYNHLMPTRYSVD
>gnl|CDD|240515 cd06091, KOW_NusG, NusG contains an NGN domain at its N-terminus and KOW motif at its C-terminus. KOW_NusG motif is one of the two domains of N-Utilization Substance G (NusG) a transcription elongation and Rho-termination factor in bacteria and archaea. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. The eukaryotic ortholog of NusG is Spt5 with multiple KOW motifs at its C-terminus
EVDFEVGDTVRIISGPFAGFEGKVEEIDEEKGKVKVLVEMFGRETPVELDFDQVEK
>gnl|CDD|132768 cd06093, PX_domain, The Phox Homology domain, a phosphoinositide binding module. The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting
SVSIPDYEKVKDGGKKYVVYIIEVTTQGGEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNLD
PEFIEERRKQLEQYLQSLLNHPELRNSEELKEFLEL
>gnl|CDD|133158 cd06094, RP_Saci_like, RP_Saci_like, retropepsin family. Retropepsin on retrotransposons with long terminal repeats (LTR) including Saci-1, -2 and -3 of Schistosoma mansoni. Retropepsins are related to fungal and mammalian pepsins. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A
LHVRDRTSGLRFLVDTGAAVSVLPASSTKKSLKPSPLTLQAANGTPIATYGTRSLTLDLGLRRPFAWNFV
VADVPHPILGADFLQHYGL
>gnl|CDD|133159 cd06095, RP_RTVL_H_like, Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements. This family includes aspartate proteases from retroelements with LTR (long terminal repeats) including the RTVL_H family of human endogenous retrovirus-like elements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A
VTITVEGVPIVFLVDTGATHSVLKSDLGPKQELSTTSVLIRGVSGQSQQPVTTYRTLVDLGGHTVSHSFL
VVPNCPDPLLGRDLLS
>gnl|CDD|133160 cd06096, Plasmepsin_5, Plasmepsins are a class of aspartic proteinases produced by the plasmodium parasite. The family contains a group of aspartic proteinases homologous to plasmepsin 5. Plasmepsins are a class of at least 10 enzymes produced by the plasmodium parasite. Through their haemoglobin-degrading activity, they are an important cause of symptoms in malaria sufferers. This family of enzymes is a potential target for anti-malarial drugs. Plasmepsins are aspartic acid proteases, which means their active site contains two aspartic acid residues. These two aspartic acid residue act respectively as proton donor and proton acceptor, catalyzing the hydrolysis of peptide bond in proteins. Aspartic proteinases are composed of two structurally similar beta barrel lobes, each lobe contributing an aspartic acid residue to form a catalytic dyad that acts to cleave the substrate peptide bond. The catalytic Asp residues are contained in an Asp-Thr-Gly-Ser/thr motif in both N- and C-terminal lobes of the enzyme. There are four types of plasmepsins, closely related but varying in the specificity of cleavage site. The name plasmepsin may come from plasmodium (the organism) and pepsin (a common aspartic acid protease with similar molecular structure). This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
YAYYFIDIFIGNPPQKQSLILDTGSSSLSFPCSQCKNCGIHMEPPYNLNNSITSSILYCDCNKCCYCLSC
LNNKCEYSISYSEGSSISGFYFSDFVSFESYLNSNSEKESFKKIFGCHTHETNLFLTQQATGILGLSLTK
NNGLPTPIILLFTKRPKLKKDKIFSICLSEDGGELTIGGYDKDYTVRNSSIGNNKVSKIVWTPITRKYYY
YVKLEGLSVYGTTSNSGNTKGLGMLVDSGSTLSHFPEDLYNKINNFFPTITIIFENNLKIDWKPSSYLYK
KESFWCKGGEKSVSNKPILGASFFKNKQIIFDLDNNRIGFVESNCP
>gnl|CDD|133161 cd06097, Aspergillopepsin_like, Aspergillopepsin_like, aspartic proteases of fungal origin. The members of this family are aspartic proteases of fungal origin, including aspergillopepsin, rhizopuspepsin, endothiapepsin, and rodosporapepsin. The various fungal species in this family may be the most economically important genus of fungi. They may serve as virulence factors or as industrial aids. For example, Aspergillopepsin from A. fumigatus is involved in invasive aspergillosis owing to its elastolytic activity and Aspergillopepsins from the mold A. saitoi are used in fermentation industry. Aspartic proteinases are a group of proteolytic enzymes in which the scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in a DT(S)G motif at the active site. They have a similar fold composed of two beta-barrel domains. Between the N-terminal and C-terminal domains, each of which contributes one catalytic aspartic residue, there is an extended active-site cleft capable of interacting with multiple residues of a substrate. Although members of the aspartic protease family of enzymes have very similar three-dimensional structures and catalytic mechanisms, each has unique substrate specificity. The members of this family has an optimal acidic pH (5.5) and cleaves protein substrates with similar specificity to that of porcine pepsin A, preferring hydrophobic residues at P1 and P1' in the cleave site. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
YLTPVKIGTPPQTLNLDLDTGSSDLWVFSSETPAAQQGGHKLYDPSKSSTAKLLPGATWSISYGDGSSAS
GIVYTDTVSIGGVEVPNQAIELATAVSASFFSDTASDGLLGLAFSSINTVQPPKQKTFFENALSSLDAPL
FTADLRKAAPGFYTFGYIDESKYKGEISWTPVDNSSGFWQFTSTSYTVGGDAPWSRSGFSAIADTGTTLI
LLPDAIVEAYYSQVPGAYYDSEYGGWVFPCDTTLPDLSFAVFSILGDVFLKAQYVVFDVGGPKLGFAP
>gnl|CDD|133162 cd06098, phytepsin, Phytepsin, a plant homolog of mammalian lysosomal pepsins. Phytepsin, a plant homolog of mammalian lysosomal pepsins, resides in grains, roots, stems, leaves and flowers. Phytepsin may participate in metabolic turnover and in protein processing events. In addition, it highly expressed in several plant tissues undergoing apoptosis. Phytepsin contains an internal region consisting of about 100 residues not present in animal or microbial pepsins. This region is thus called a plant specific insert. The insert is highly similar to saponins, which are lysosomal sphingolipid-activating proteins in mammalian cells. The saponin-like domain may have a role in the vacuolar targeting of phytepsin. Phytepsin, as its animal counterparts, possesses a topology typical of all aspartic proteases. They are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe has probably evolved from the other through a gene duplication event in the distant past. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA)
VALKNYLDAQYFGEIGIGTPPQKFTVIFDTGSSNLWVPSSKCYFSIACYFHSKYKSSKSSTYKKNGTSAS
IQYGTGSISGFFSQDSVTVGDLVVKNQVFIEATKEPGLTFLLAKFDGILGLGFQEISVGKAVPVWYNMVE
QGLVKEPVFSFWLNRNPDEEEGGELVFGGVDPKHFKGEHTYVPVTRKGYWQFEMGDVLIGGKSTGFCAGG
CAAIADSGTSLLAGPTTIVTQINSAVDCNSLSSMPNVSFTIGGKTFELTPEQYILKVGEGAAAQCISGFT
ALDVPPPRGPLWILGDVFMGAYHTVFDYGNLRVGFAE
>gnl|CDD|99853 cd06099, CS_ACL-C_CCL, Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) from citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. Some CS proteins function as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. CCL cleaves citryl-CoA (CiCoA) to AcCoA and OAA. ACLs catalyze an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA; they do this in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate CiCoA, and c) the hydrolysis of CiCoA to produce citrate and CoA. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL
SYAENFLYMLGGEEPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGG
ANEAVLKMLEEIGTPKNEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGDDPMFE
LAAELEKIAEEVLYEKKLYPNVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPR
SEY
>gnl|CDD|99854 cd06100, CCL_ACL-C, Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CCL cleaves citryl-CoA (CiCoA) to acetyl-CoA (AcCoA) and oxaloacetate (OAA). ACL catalyzes an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. ACL may be required for fruiting body maturation in the filamentous fungus Sordaria macrospore. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL; the first enzyme is citryl-CoA synthetase (CCS) which is not included in this group. Chlorobium limicola ACL is an example of a two-subunit type ACL. It is comprised of a large and a small subunit; it has been speculated that the large subunit arose from a fusion of the small subunit of the two subunit CCS with CCL. The small ACL subunit is a homolog of the larger CCS subunit. Mammalian ACL is of the single-subunit type and may have arisen from the two-subunit ACL by another gene fusion. Mammalian ACLs are homotetramers; the ACLs of C. limicola and Arabidopsis are a heterooctomers (alpha4beta4). In cancer cells there is a shift in energy metabolism to aerobic glycolysis, the glycolytic end product pyruvate enters a truncated TCA cycle generating citrate which is cleaved in the cytosol by ACL. Inhibiting ACL limits the in-vitro proliferation and survival of these cancer cells, reduces in vivo tumor growth, and induces differentiation
GYDLSDLIGKISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATPSAHAARLTASAGPEDLQSAVA
AGLLGIGDRFGGAGEGAARLFKEAVDSGDALDAAAAEFVAEYRAAKKRIPGFGHPVHKNPDPRVPRLLEL
ARELGPAGPHLDYALAVEKALTAAKGKPLPLNVDGAIAAILLDLGFPPGALRGLFVLGRSPGLIAHALEE
KRLGQPLYRHPWDDIEY
>gnl|CDD|99855 cd06101, citrate_synt, Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and form homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria
PGLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELPSYAENFLYMLGGEEPDPE
FAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPKNE
PAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKGLDPMFELAAELEKIAPEVLYEKKL
YPNVDFYSGVLYKAMGFPTELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRAEY
>gnl|CDD|99856 cd06102, citrate_synt_like_2, Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria
RGRRPRAAVAAAALDWGEPVLESAITLITEGRLFYRGRDAVELAETATLEEVAALLWDGDEAARLLRLLA
AALLGAAPSDAPVHRRLARAWGLDPAAADLLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAA
LSGPRHGGATARVEALLDEALRAGDAEAAVRERLRRGEALPGFGHPLYPDGDPRAAALLAALRPLGPAAP
PAARALIEAARALTGARPNIDFALAALTRALGLPAGAAFALFALGRSAGWIAHALEQRAQGKLIRPRARY
VG
>gnl|CDD|99857 cd06103, ScCS-like, Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). This group includes three S. cerevisiae CS proteins, ScCit1,-2,-3. ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA; in addition to having activity with AcCoA, it plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. ScCit3 is a mitochondrial CS and functions in the metabolism of PrCoA; it is a dual specificity CS and 2MCS, having similar catalytic efficiency with both AcCoA and PrCoA. The pattern of expression of the ScCIT3 gene follows that of the ScCIT1 gene and its expression is increased in the presence of a ScCIT1 deletion. Included in this group is the Tetrahymena 14 nm filament protein which functions as a CS in mitochondria and as a cytoskeletal component in cytoplasm and Geobacter sulfurreducens (GSu) CS. GSuCS is dimeric and eukaryotic-like; it lacks 2MCS activity and is inhibited by ATP. In contrast to eukaryotic and other prokaryotic CSs, GSuCIT is not stimulated by K+ ions. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS
LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQ
ELLPKADGGGEPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLSAAI
LALQSESKFAKAYAEGKINKTTYWEYVYEDAMDLIAKLPVVAAKIYRRKYRKGGEIGAIDSKLDWSANFA
HMLGYEDEEFTDLMRLYLTLHSDHEGGNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKW
LLKMQKELGKDVSDEELEKYIWDTLNSGRVVPGYGHAVLRKTDPRFTCQREFALKHLPDDPLFKLVAQCY
KIIPGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTEPQYYTVLFGVSRALGVLAQLVWSRALGLPIERPKS
MSTEGL
>gnl|CDD|99858 cd06105, ScCit1-2_like, Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA. In addition to its CS function, ScCit1 plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. Chicken and pig heart CS, two Arabidopsis thaliana (Ath) CSs, CSY4 and -5, and Aspergillus niger (An) CS also belong to this group. Ath CSY4 has a mitochondrial targeting sequence; AthCSY5 has no identifiable targeting sequence. AnCS encoded by the citA gene has both an N-terminal mitochondrial import signal and a C-terminal peroxisiomal target sequence; it is not known if both these signals are functional in vivo. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS
LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQ
KLLPKAPGGEEPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAI
TALNSESKFAKAYAEGIHKSKYWEYVYEDSMDLIAKLPCVAAKIYRNLYRGGKIIAIDSNLDWSANFANM
LGYTDPQFTELMRLYLTIHSDHEGGNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLT
KLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPLFKLVSQLYKI
VPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGVLSQLIWDRALGLPLERPKSVS
TDGLEKL
>gnl|CDD|99859 cd06106, ScCit3_like, Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase (2MCS) catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxaloacetate (OAA) to form 2-methylcitrate and CoA. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with OAA to form citrate and CoA, the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit3 is mitochondrial and functions in the metabolism of PrCoA; it is a dual specificity CS and 2MCS, having similar catalytic efficiency with both AcCoA and PrCoA. The pattern of expression of the ScCIT3 gene follows that of the major mitochondrial CS gene (CIT1, not included in this group) and its expression is increased in the presence of a CIT1 deletion. This group also contains Aspergillus nidulans 2MCS; a deletion of the gene encoding this protein results in a strain unable to grow on propionate. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS
LKEALKEVIPAKREQLKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQ
KELPKAPIGGEMLPESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLSIGV
AALNHDSKFAAAYEKGIKKTEYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLGKIDPEVDWSYNFTS
MLGYGDNLDFVDLLRLYIALHGDHEGGNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRW
ILEMQKNIGSKATDQDIRDYLWKTLKSGRVVPGYGHAVLRKPDPRFTALMEFAQTRPELENDPVVQLVQK
LSEIAPGVLTEHGKTKNPFPNVDAASGVLFYHYGIREFLYYTVIFGVSRALGPLTQLVWDRILGLPIERP
KSLSLEGL
>gnl|CDD|99860 cd06107, EcCS_AthCS-per_like, Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs, including EcCS, are strongly and specifically inhibited by NADH through an allosteric mechanism. Included in this group is an NADH-insensitive type II Acetobacter acetii CS which has retained many of the residues used by EcCS for NADH binding. C. aurantiacus is a gram-negative thermophilic green gliding bacterium; its CS belonging to this group may be a type I CS. It is not inhibited by NADH or 2-oxoglutarate and is inhibited by ATP. Both gram-positive and gram-negative bacteria are found in this group. This group also contains three Arabidopsis peroxisomal CS proteins, CYS-1, -2, and -3 which participate in the glyoxylate cycle. AthCYS1, in addition to a peroxisomal targeting sequence, has a predicted secretory signal peptide; it may be targeted to both the secretory pathway and the peroxisomes and perhaps is located in the extracellular matrix. AthCSY1 is expressed only in siliques and specifically in developing seeds. AthCSY2 and 3 are active during seed germination and seedling development and are thought to participate in the beta-oxidation of fatty acids
GLRVYDPGYLNTAVCESSITYIDGDKGILLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRL
SEHMMVPESVHRLIQTFPRDAHPMGILCAGLSALSAFYPEAIPAHTGDLYQNNPEVRDKQIIRTLAKMPT
IAAAAYCHRIGRPFVYPRANLSYIENFLYMMGYVDQEPYEPNPRLARALDRLWILHADHEMNCSTSAARH
TGSSLADPISCMAAAIAALYGPLHGGANEAALKMLREIGTPENVPAFIERVKNGKRRLMGFGHRVYKNYD
PRAKVIREILHEVLTEVEKDPLLKVAMELERIALEDEYFVSRKLYPNVDFYSGFIYKALGFPPEFFTVLF
AVARTSGWMAHWREMMEDPLQRIWRPRQVYTG
>gnl|CDD|99861 cd06108, Ec2MCS_like, Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxalacetate (OAA) to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and OAA to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group contains proteins similar to the E. coli 2MCS, EcPrpC. EcPrpC is one of two CS isozymes in the gram-negative E. coli. EcPrpC is a dimeric (type I) CS; it is induced during growth on propionate and prefers PrCoA as a substrate though it has partial CS activity with AcCoA. This group also includes Salmonella typhimurium PrpC and Ralstonia eutropha (Re) 2-MCS1 which are also induced during growth on propionate and prefer PrCoA as substrate, but can also use AcCoA. Re 2-MCS1 can use butyryl-CoA and valeryl-CoA at a lower rate. A second Ralstonia eutropha 2MCS, Re 2-MCS2, which is induced on propionate is also found in this group. This group may include proteins which may function exclusively as a CS, those which may function exclusively as a 2MCS, or those with dual specificity which functions as both a CS and a 2MCS
GGLAGVVAGQTAISTVGKGGKGLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRL
PAALKTVLELIPKDSHPMDVMRTGCSMLGCLEPENEFSQQYEIAIRLLAIFPSILLYWYHYSHSGKRIET
ETDEDSIAGHFLHLLHGKKPGELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRG
PLHGGANEAAMELIERFKSPEEAEQGLLEKLERKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGGDPL
LYQISERIEEVMWEEKKLFPNLDFYSASAYHFCGIPTELFTPIFVMSRVTGWAAHIMEQRANNRLIRPSA
DYIGPEPRPFVPI
>gnl|CDD|99862 cd06109, BsCS-I_like, Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains proteins similar to BsCS-I, one of two CS isozymes in the gram-positive B. subtilis. The majority of CS activity in B. subtilis is provided by the other isozyme, BsCS-II (not included in this group). BsCS-I has a lower catalytic activity than BsCS-II, and has a Glu in place of a key catalytic Asp residue. This change is conserved in other members of this group. For E. coli CS (not included in this group), site directed mutagenesis of the key Asp residue to a Glu converts the enzyme into citryl-CoA lyase which cleaves citryl-CoA to AcCoA and OAA. A null mutation in the gene encoding BsCS-I (citA) had little effect on B. subtilis CS activity or on sporulation. However, disruption of the citA gene in a strain null for the gene encoding BsCS-II resulted in a sporulation deficiency, a characteristic of strains defective in the Krebs cycle. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. Many of the gram-negative species represented in this group have a second CS isozyme which is in another group
PGLEGVVAAETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARAL
PDVVAALLPALAGLDPMDALRALLALLPDSPDLATALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAA
DYLRMLTGEPPSEAHVRALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGP
VLDMLDAIGTPENAEAWLREALARGERLMGFGHRVYRVRDPRADVLKAAAERLGAPDERLEFAEAVEQAA
LALLREYKPGRPLETNVEFYTALLLEALGLPREAFTPTFAAGRTAGWTAHVLEQARTGRLIRPQSRYVG
>gnl|CDD|99863 cd06110, BSuCS-II_like, Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains proteins similar to BsCS-II, the major CS of the gram-positive bacterium Bacillus subtilis. A mutation in the gene which encodes BsCS-II (citZ gene) has been described which resulted in a significant loss of CS activity, partial glutamate auxotrophy, and a sporulation deficiency, all of which are characteristic of strains defective in the Krebs cycle. Streptococcus mutans CS, found in this group, may participate in a pathway for the anaerobic biosynthesis of glutamate. This group also contains functionally uncharacterized CSs of various gram-negative bacteria. Some of the gram-negative species represented in this group have a second CS isozyme found in another group. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS
KGLEGVIAADSKISYIDGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAEREL
PAEIIDLLKLLPKDAHPMDVLRTAVSALALYDPEADDMSREANLRKAIRLIAKMPTIVAAFHRIRNGLEP
VAPDPDLSHAANFLYMLTGEKPSEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGAL
KGPLHGGANERVMKMLLEIGSVDNVAAYVKDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRRLGKETGE
PKWYEMSEAIEQAMRDEKGLNPNVDFYSASVYYMLGIPVDLFTPIFAISRVSGWCAHILEQYFNNRLIRP
RAEYVG
>gnl|CDD|99864 cd06111, DsCS_like, Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2-methylcitrate synthase (2MCS) catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. DsCS, compared with CS from the hyperthermophile Pyrococcus furiosus (not included in this group), has an increase in the size of surface loops, a higher proline content in the loop regions, a more accessible active site, and a higher number of intramolecular ion pairs. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. For example, included in this group are Corynebacterium glutamicum (Cg) PrpC1 and -2, which are only synthesized during growth on propionate-containing medium, can use PrCoA, AcCoA and butyryl-CoA as substrates, and have comparable catalytic activity with AcCoA as the major CgCS (GltA, not included in this group)
KGLAGVVADTTAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRL
DRNLLSLIASLPKNCHPMDVLRTAVSVLGAEDSETDDSSPDANLAKAIRLLAQLPTVVAADIRRRKGLDP
IPPDSDLGIAENFLHMCFGEVPSPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGAL
KGPLHGGANEAVMHMMLEIDDPEKAAQWMLDALARKEKVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDG
QKWLAMYDALEDAMVAAKGIKPNLDFPAGPAYYLMGFDIDFFTPIFVMARITGWTAHIMEQRADNALIRP
LSEYNGPEQRPV
>gnl|CDD|99865 cd06112, citrate_synt_like_1_1, Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism
YIPGLAGVPAAESSISYIDGKNGILEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHR
RVKYNIRDMMKCFPETGHPMDMLQATVAALGMFYPKPEVLKPNPDYIDAATVKLIAKMPTLVAMWARIRN
GDDPIEPRPDLDYAENFLYMLFGEEPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSA
IGTLSGPLHGGANEDVLEMLEEIGSPENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFA
KMGELSKLYEIALEVERLCEELLGHKGVYPNVDFYSGIVYKELGIPADLFTPIFAVARVAGWLAHWKEQL
GDNRIFRPTQIYIGEIDRKYVPL
>gnl|CDD|99866 cd06113, citrate_synt_like_1_2, Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) a carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) hydrolysis of citryl-CoA to produce citrate and CoA. CSs are found in two structural types: type I (homodimeric) and type II CSs (homohexameric). Type II CSs are unique to gram-negative bacteria. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria. Type I CS is active as a homodimer, both subunits participating in the active site. Type II CS is a hexamer of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria
RGLRNEDGTGVLAGLTNISDVVGYKIIDGEKVPCPGKLYYRGYDVEDLVNGAQKENRFGFEETAYLLLFG
YLPNKEELEEFCEILSSYRTLPDNFVEDVILKAPSKDIMNKLQRSVLALYSYDDKPDDISLENVLRQSIQ
LIARLPTIAVYAYQAKRHYYDGESLYIHHPQPELSTAENILSMLRPDKKYTELEAKLLDLCLVLHAEHGG
GNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIKENVKDWTDEDEVRAYLRKILN
KEAFDKSGLIYGMGHAVYTLSDPRAVVLKKYARSLAKEKGREEEFALYERIERLAPEVIAEERGIGKTVC
ANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLNSGRIIRPAYKYVG
>gnl|CDD|99867 cd06114, EcCS_like, Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs including EcCS are strongly and specifically inhibited by NADH through an allosteric mechanism. Included in this group is an NADH-insensitive type II Acetobacter acetii CS which has retained many of the residues used by EcCS for NADH binding
LPVLEGTEGEKVIDISSLRKKTGVFTYDPGFMNTASCESAITYIDGEKGILRYRGYPIEQLAEKSSFLEV
CYLLLYGELPTAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVNALSAFYPDSLDVNDPE
QRELAAIRLIAKVPTIAAMAYRYSIGQPFIYPDNDLSYVENFLHMMFAVPYEPYEVDPVVVKALDTILIL
HADHEQNASTSTVRMVGSSGANLFASISAGIAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAKAKDKN
DPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGKDDPLLEIAMELEEIALKDDYFIERKLYPNVDFYS
GIILRALGIPTEMFTVLFALGRTPGWIAQWREMHEDPELKIGRPRQLYTG
>gnl|CDD|99868 cd06115, AthCS_per_like, Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains three Arabidopsis peroxisomal CS proteins, CYS1, -2, and -3 which are involved in the glyoxylate cycle. AthCYS1, in addition to a peroxisomal targeting sequence, has a predicted secretory signal peptide; it may be targeted to both the secretory pathway and the peroxisomes and is thought to be located in the extracellular matrix. AthCSY1 is expressed only in siliques and specifically in developing seeds. AthCSY2 and 3 are active during seed germination and seedling development and are thought to participate in the beta-oxidation of fatty acids
DHGTVKATDFKKIKAGKDDKGLRLYDPGYLNTAVVRSKISYIDGDKGILRYRGYPIEELAEKSTFLEVAY
LLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHDAHPMGMLVSAISALSAFHPEANPALAGQDI
YKNKQVRDKQIVRILGKAPTIAAAAYRRRAGRPPNLPSQDLSYTENFLYMLDSLGERKYKPNPRLARALD
ILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRMLAEIGTVENIPAFIEG
VKNRKRKLSGFGHRVYKNYDPRAKIIKKLADEVFEIVGKDPLIEIAVALEKAALSDEYFVKRKLYPNVDF
YSGLIYRAMGFPTDFFPVLFAIPRMAGYLAHWRESLDDPDTKIMRPQQLYTGVWLRHYVP
>gnl|CDD|99869 cd06116, CaCS_like, Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group is similar to gram-negative Escherichia coli (Ec) CS (type II, gltA) and Arabidopsis thaliana (Ath) peroxisomal (Per) CS. However EcCS and AthPerCS are not found in this group. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. C. aurantiacus is a gram-negative thermophilic green gliding bacterium, its CS belonging to this group may be a type I CS; it is not inhibited by NADH or 2-oxoglutarate and is inhibited by ATP. Both gram-positive and gram-negative bacteria are found in this group
GLMTYDPAYLNTASCKSAITYIDGEKGILRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDI
TRHTMTHENLKKFMDGFRYDAHPMGILISSVAALSTFYPEAKNIGDEEQRNKQIIRLIGKMPTIAAFAYR
HRLGLPYVLPDNDLSYTGNFLSMLFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRAD
PYTAVAAAVAALYGPLHGGANEAVLRMLQQIGSPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIK
KIADEVFEATGRNPLLDIAVELEKIALEDEYFISRKLYPNVDFYSGLIYQALGFPTEAFTVLFAIPRTSG
WLAQWIEMLRDPEQKIARPRQVYTGPRDRDYVPI
>gnl|CDD|99870 cd06117, Ec2MCS_like_1, Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxalacetate (OAA) to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and OAA to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group contains proteins similar to the E. coli 2MCS, EcPrpC. EcPrpC is one of two CS isozymes in the gram-negative E. coli. EcPrpC is a dimeric (type I) CS; it is induced during growth on propionate and prefers PrCoA as a substrate, but has a partial CS activity with AcCoA. This group also includes Salmonella typhimurium PrpC and Ralstonia eutropha (Re) 2-MCS1 which are also induced during growth on propionate, prefer PrCoA as substrate, but can also can use AcCoA. Re 2-MCS1 at a low rate can use butyryl-CoA and valeryl-CoA. A second Ralstonia eutropha 2MCS is also found in this group, Re 2-MCS2, which is induced on propionate. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS
VALSGVAAGNTALCTVGRSGNDLHYRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGL
PANVKTALEQLPAAAHPMDVMRTGVSVLGCVLPEKEDHPVSGARDIADRLMASLGSILLYWYHYSHNGKR
IEVETDDDSIGGHFLHLLHGEKPSESWEKAMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGA
LRGPKHGGANEVAFEIQQRYESADEAEADIRRRVENKEVVIGFGHPVYTIADPRNQVIKEVAKQLSKEGG
DMKMFDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGVPTAMFTPLFVIARTTGWSAHIIEQRQDGKIIR
PSANYTGPEDLKFVPI
>gnl|CDD|99871 cd06118, citrate_synt_like_1, Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism
PGLEGVKAKETSISYIDGDEGILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRAL
PEHVVEILDLLPKNAHPMDVLRTAVSALGSFDPFARDKSPEARYEKAIRLIAKLPTIAANIYRNREGLEI
IAPDPDLSYAENFLYMLFGEEPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAAL
KGPLHGGANEAVLKMLLEIGTPENVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKGD
DKLFEIAEELEEIALEVLGEKGIYPNVDFYSGVVYKALGFPTELFTPLFAVSRAVGWLAHIIEYRENNQR
LIRPRAEY
>gnl|CDD|380376 cd06121, cupin_YML079wp, Saccharomyces cerevisiae YML079wp and related proteins, cupin domain. This family includes eukaryotic, bacterial, and archaeal proteins homologous to YML079wp, a Saccharomyces cerevisiae cupin-like protein of unknown function that structurally resembles plant seed storage and ligand-binding proteins (canavalin, glycinin, auxin binding protein) as well as the bacterial RmlC epimerase. YML079wp is non-essential in yeast and localizes to the nucleus and cytoplasm. The presence of a hydrophobic ligand within a well-conserved binding pocket inside the cupin beta-barrel and sequence similarity with bacterial epimerases suggests a possible biochemical function for YML079wp and its homologs. Also included in this family are Shewanella oneidensis So0799, Agrobacterium fabrum Atu3615 and Branchiostoma belcheri Bbduf985. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer
AEELIEKLGLEPHPEGGYFRETYRSPETVPTPRDGGERPASTAIYYLLTPGDFSAFHRLKSDEIWHFHAG
DPLELHLLDPDGTYETVVLGPDLAAGERPQVVVPAGTWQAAELLGGGGYALVGCTVAPGFDFEDFELGDR
EELLAKYPQHAEL
>gnl|CDD|380377 cd06122, cupin_TTHA0104, Thermus thermophilus TTHA0104 and related proteins, cupin domain. This family contains bacterial proteins including TTHA0104 (also called TT1209), a putative antibiotic synthesis protein from Thermus thermophilus. TTHA0104 is a cupin-like protein. The cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin (cupa is the Latin term for small barrel)
YFKDLRDHARFSPEKMQKITLFESERLFCDLYCLEPGQSQKVHAHAGSDKVYFVLEGEGRFTVGDEEREL
GAGEAVLAPAGVPHGVRNTGAERLVLLVFMAP
>gnl|CDD|380378 cd06123, cupin_HAO, 3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain. 3-Hydroxyanthranilate-3,4-dioxygenase (HAO or 3HAO) is a non-heme iron-dependent extradiol dioxygenase that catalyzes the oxidative ring opening of 3-hydroxyanthranilate (3-HAA) in the final enzymatic step of the kynurenine biosynthetic pathway in which tryptophan is converted to quinolinate, an endogenous neurotoxin, making HAO a target for pharmacological downregulation. Quinolate is also the universal de novo precursor to the pyridine ring of nicotinamide adenine dinucleotide. The enzyme forms homodimers, with two metal binding sites per molecule. One of the bound metal ions occupies the proposed ferrous-coordinated active site, which is located in a conserved double-strand beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
KWIEENRHLLKPPVGNKLLWQDSDFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEPGKFKDVVI
KEGEIFLLPARVPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHCDDLGTQLKPAIEE
FFASEELRTCKPC
>gnl|CDD|380379 cd06124, cupin_NimR-like_N, AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain. This family contains mostly bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included in this family is Escherichia coli HTH-type transcriptional regulator NimR (also called YeaM) that negatively regulates expression of the nimT operon and its own expression. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
VLARAADYPAGHRTPWHSHPWGQLLYASSGVMTVETEDGRWLVPPQRAVWIPAGVEHSVRMLGAVELRSL
YIDPEAAAGLPAEPCVLAVSPLLRE
>gnl|CDD|176647 cd06125, DnaQ_like_exo, DnaQ-like (or DEDD) 3'-5' exonuclease domain superfamily. The DnaQ-like exonuclease superfamily is a structurally conserved group of 3'-5' exonucleases, which catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. It is also called the DEDD superfamily, after the four invariant acidic residues present in the catalytic site of its members. The superfamily consists of DNA- and RNA-processing enzymes such as the proofreading domains of DNA polymerases, other DNA exonucleases, RNase D, RNase T, Oligoribonuclease and RNA exonucleases (REX). The DnaQ-like exonuclease domain contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, which are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The conservation patterns of the three motifs may vary among different subfamilies. DnaQ-like exonucleases are classified as DEDDy or DEDDh exonucleases depending on the variation of motif III as YX(3)D or HX(4)D, respectively. The significance of the motif differences is still unclear. Almost all RNase families in this superfamily are present only in eukaryotes and bacteria, but not in archaea, suggesting a later origin, which in some cases are accompanied by horizontal gene transfer
IAIDTEATGLDGAVHEIIEIALADVNPEDTAVIDLKDILRDKPLAILVGHNGSFDLPFLNNRCAELGLKY
PLLAGSWIDTIKLAADDVENTLQITA
>gnl|CDD|176648 cd06127, DEDDh, DEDDh 3'-5' exonuclease domain family. DEDDh exonucleases, part of the DnaQ-like (or DEDD) exonuclease superfamily, catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. These proteins contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDh exonucleases are classified as such because of the presence of specific Hx(4)D conserved pattern at the ExoIII motif. The four conserved acidic residues are clustered around the active site and serve as ligands for the two metal ions required for catalysis. Most DEDDh exonucleases are the proofreading subunits (epsilon) or domains of bacterial DNA polymerase III, the main replicating enzyme in bacteria, which functions as the chromosomal replicase. Other members include other DNA and RNA exonucleases such as RNase T, Oligoribonuclease, and RNA exonuclease (REX), among others
VVFDTETTGLDPKKDRIIEIGAVKVDGGIEIVERFETLVNPGRPIPPEATAIHGITDEMLADAPPFEEVL
PEFLEFLGGRVLVAHNASFDLRFLNRELRRLGGPPLPNPWIDTLRLARRLLPGLRSHRLGLLLAERYGIP
LEGAHRALADALATAELLL
>gnl|CDD|176649 cd06128, DNA_polA_exo, DEDDy 3'-5' exonuclease domain of family-A DNA polymerases. The 3'-5' exonuclease domain of family-A DNA polymerases has a fundamental role in reducing polymerase errors and is involved in proofreading activity. Family-A DNA polymerases contain a DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-B DNA polymerases. The exonuclease domain contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, which are clustered around the active site and contain four invariant acidic residues that serve as ligands for the two metal ions required for catalysis. The Klenow fragment (KF) of Escherichia coli Pol I, the Thermus aquaticus (Taq) Pol I, and Bacillus stearothermophilus (BF) Pol I are examples of family-A DNA polymerases. They are involved in nucleotide excision repair and in the processing of Okazaki fragments that are generated during lagging strand synthesis. The N-terminal domains of BF Pol I and Taq Pol I resemble the fold of the 3'-5' exonuclease domain of KF without the proofreading activity of KF. The four critical metal-binding residues are not conserved in BF Pol I and Taq Pol I, and they are unable to bind metals necessary for exonuclease activity
APVAAFGTETDSLDNISANLVGLAFAIEGVAAYIPVAHDYALELLKPLLEDEKALKVGQNLKYDRVILAN
YGIELRGIAFDTMLEAYLLDPVAGRHDMDSLAERWLKEKTITFEEIAGKGLTFNQIALEEAGEYAAEDAA
VTLQLHLKMWP
>gnl|CDD|176650 cd06129, RNaseD_like, DEDDy 3'-5' exonuclease domain of RNase D, WRN, and similar proteins. The RNase D-like group is composed of RNase D, WRN, and similar proteins. They contain a DEDDy-type, DnaQ-like, 3'-5' exonuclease domain that contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. RNase D is involved in the 3'-end processing of tRNA precursors. RNase D-like proteins in eukaryotes include yeast Rrp6p, human PM/Scl-100 and Drosophila melanogaster egalitarian (Egl) protein. WRN is a unique DNA helicase possessing exonuclease activity. Mutation in the WRN gene is implicated in Werner syndrome, a disease associated with premature aging and increased predisposition to cancer. Yeast Rrp6p and the human Polymyositis/scleroderma autoantigen 100kDa (PM/Scl-100) are exosome-associated proteins involved in the degradation and processing of precursors to stable RNAs. Egl is a component of an mRNA-binding complex which is required for oocyte specification. The Egl subfamily does not possess a completely conserved YX(3)D pattern at the ExoIII motif
ALSSLCEDLSMDGDVIAFDMEWPPGRRYYGEVALIQLCVSEEKCYLFDPLSLSVDWQGLKMLLENPSIVK
ALHGIEGDLWKLLRDFGEKLQRLFDTTIAANLKGLPERWSLASLVEHFLGKTLDKSISCADWSYRPLTED
QKLYAAADVYALLIIYTKLRN
>gnl|CDD|99834 cd06130, DNA_pol_III_epsilon_like, an uncharacterized bacterial subgroup of the DEDDh 3'-5' exonuclease domain family with similarity to the epsilon subunit of DNA polymerase III. This subfamily is composed of uncharacterized bacterial proteins with similarity to the epsilon subunit of DNA polymerase III (Pol III), a multisubunit polymerase which is the main DNA replicating enzyme in bacteria, functioning as the chromosomal replicase. The Pol III holoenzyme is a complex of ten different subunits, three of which (alpha, epsilon, and theta) compose the catalytic core. The Pol III epsilon subunit, encoded by the dnaQ gene, is a DEDDh-type 3'-5' exonuclease which is responsible for the proofreading activity of the polymerase, increasing the fidelity of DNA synthesis. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The epsilon subunit of Pol III also functions as a stabilizer of the holoenzyme complex
FVAIDFETANADRASACSIGLVKVRDGQIVDTFYTLIRPPTRFDPFNIAIHGITPEDVADAPTFPEVWPE
IKPFLGGSLVVAHNASFDRSVLRAALEAYGLPPPPYQYLCTVRLARRVWPLLPNHKLNTVAEHLGIELNH
HDALEDARACAEILLA
>gnl|CDD|99835 cd06131, DNA_pol_III_epsilon_Ecoli_like, DEDDh 3'-5' exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III and similar proteins. This subfamily is composed of the epsilon subunit of Escherichia coli DNA polymerase III (Pol III) and similar proteins. Pol III is the main DNA replicating enzyme in bacteria, functioning as the chromosomal replicase. It is a holoenzyme complex of ten different subunits, three of which (alpha, epsilon, and theta) compose the catalytic core. The Pol III epsilon subunit, encoded by the dnaQ gene, is a DEDDh-type 3'-5' exonuclease which is responsible for the proofreading activity of the polymerase, increasing the fidelity of DNA synthesis. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The epsilon subunit of Pol III also functions as a stabilizer of the holoenzyme complex
QIVLDTETTGLDPREGHRIIEIGCVELINRRLTGNTFHVYINPERDIPEEAFKVHGITDEFLADKPKFAE
IADEFLDFIRGAELVIHNASFDVGFLNAELSLLGLGKKIIDFCRVIDTLALARKKFPGKPNSLDALCKRF
GIDNSHRTLHGALLDAELLAEVYLELT
>gnl|CDD|99836 cd06133, ERI-1_3'hExo_like, DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and similar proteins. This subfamily is composed of Caenorhabditis elegans ERI-1, human 3' exonuclease (3'hExo), Drosophila exonuclease snipper (snp), and similar proteins from eukaryotes and bacteria. These are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. ERI-1 has been implicated in the degradation of small interfering RNAs (RNAi). 3'hExo participates in the degradation of histone mRNAs. Snp is a non-essential exonuclease that efficiently degrades structured RNA and DNA substrates as long as there is a minimum of 2 nucleotides in the 3' overhang to initiate degradation. Snp is not a functional homolog of either ERI-1 or 3'hExo
YLVIDFEATCWEGNSKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVD
NAPSFPEVLKEFLEWLGKNGKYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYGLKKR
TGLSKALEYLGLEFEGRHHRGLDDARNIARILKRLL
>gnl|CDD|99837 cd06134, RNaseT, DEDDh 3'-5' exonuclease domain of RNase T. RNase T is a DEDDh-type DnaQ-like 3'-5' exoribonuclease E implicated in the 3' maturation of small stable RNAs and 23srRNA, and in the end turnover of tRNA. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. RNase T is related to the proofreading domain of DNA polymerase III. Despite its important role, RNase T is mainly found only in gammaproteobacteria. It is speculated that it might have originated from DNA polymerase III at the time the gamma division of proteobacteria diverged from other bacteria. RNase T is a homodimer with the catalytic residues of one monomer contacting a large basic patch on the other monomer to form a functional active site
RFRGFLPVVVDVETGGFNPQTDALLEIAAVTLEMDEQGNLYPDETFHFHILPFEGANLDPAALEFNGIDP
FHPFRFAVDEKEALKEIFKPIRKALKAQGCTRAILVGHNAHFDLGFLNAAVARCKIKRNPFHPFSTFDTA
TLAGLAYGQTVLAKACQAAGIEFDNKEAHSALYDTQKTAELFCKIVNRW
>gnl|CDD|99838 cd06135, Orn, DEDDh 3'-5' exonuclease domain of oligoribonuclease and similar proteins. Oligoribonuclease (Orn) is a DEDDh-type DnaQ-like 3'-5' exoribonuclease that is responsible for degrading small oligoribonucleotides to mononucleotides. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. Orn is essential for Escherichia coli survival. The human homolog, also called Sfn (small fragment nuclease), is able to hydrolyze short single-stranded RNA and DNA oligomers. It plays a role in cellular nucleotide recycling
LVWIDLEMTGLDPEKDRILEIACIITDGDLNIIAEGPELVIHQPDEVLDGMDEWCTEMHTKSGLTERVRA
STVTLAQAEAELLEFIKKYVPKGKSPLAGNSVHQDRRFLDKYMPELEEYLHYRILDVSSIKELARRWYPE
IYRKAPKKKGTHRALDDIRESIAELKYYRENIF
>gnl|CDD|99839 cd06136, TREX1_2, DEDDh 3'-5' exonuclease domain of three prime repair exonuclease (TREX)1, TREX2, and similar proteins. Three prime repair exonuclease (TREX)1 and TREX2 are closely related DEDDh-type DnaQ-like 3'-5' exonucleases. They contain three conserved sequence motifs known as ExoI, II, and III, with a specific Hx(4)D conserved pattern at ExoIII. These motifs contain four conserved acidic residues that participate in coordination of divalent metal ions required for catalysis. Both proteins play a role in the metabolism and clearance of DNA. TREX1 is the major 3'-5' exonuclease activity detected in mammalian cells. Mutations in the human TREX1 gene can cause Aicardi-Goutieres syndrome (AGS), which is characterized by perturbed innate immunity and presents itself as a severe neurological disease. TREX1 degrades ssDNA generated by aberrant replication intermediates to prevent checkpoint activation and autoimmune disease. There are distinct structural differences between TREX1 and TREX2 that point to different biological roles for these proteins. The main difference is the presence of about 70 amino acids at the C-terminus of TREX1. In addition, TREX1 has a nonrepetitive proline-rich region that is not present in the TREX2 protein. Furthermore, TREX2 contains a conserved DNA binding loop positioned adjacent to the active site that has a sequence distinct from the corresponding loop in TREX1. Truncations in the C-terminus of human TREX1 cause autosomal dominant retinal vasculopathy with cerebral leukodystrophy (RVCL), a neurovascular syndrome featuring a progressive loss of visual acuity combined with a variable neurological picture
FVFLDLETTGLPKHNRPEITELCLVAVHRDHLLNTSRDKPALPRVLDKLSLCFNPGRAISPGASEITGLS
NDLLEHKAPFDSDTANLIKLFLRRQPKPICLVAHNGNRFDFPILRSELERLGTKLPDDILCVDSLPAFRE
LDQSLGSLYKRLFGQEPKNSHTAEGDVLALLKCALHK
>gnl|CDD|99840 cd06137, DEDDh_RNase, DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonucleases PAN2, RNA exonuclease (REX)-1,-3, and -4, ISG20, and similar proteins. This group is composed of eukaryotic exoribonucleases that include PAN2, RNA exonuclease 1 (REX1 or Rex1p), REX3 (Rex3p), REX4 (or Rex4p), ISG20, and similar proteins. They are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. PAN2 is the catalytic subunit of poly(A) nuclease (PAN), a Pab1p-dependent 3'-5' exoribonuclease which plays an important role in the posttranscriptional maturation of pre-mRNAs. REX proteins are required for the processing and maturation of many RNA species, and ISG20 is an interferon-induced antiviral exonuclease with a strong preference for single-stranded RNA
VALDCEMVGLADGDSEVVRISAVDVLTGEVLIDSLVRPSVRVTDWRTRFSGVTPADLEEAAKAGKTIFGW
EAARAALWKFIDPDTILVGHSLQNDLDALRMIHTRVVDTAILTREAVKGPLAKRQWSLRTLCRDFLGLKI
QGGGEGHDSLEDALAAREVVL
>gnl|CDD|99841 cd06138, ExoI_N, N-terminal DEDDh 3'-5' exonuclease domain of Escherichia coli exonuclease I and similar proteins. This subfamily is composed of the N-terminal domain of Escherichia coli exonuclease I (ExoI) and similar proteins. ExoI is a monomeric enzyme that hydrolyzes single stranded DNA in the 3' to 5' direction. It plays a role in DNA recombination and repair. It primarily functions in repairing frameshift mutations. The N-terminal domain of ExoI is a DEDDh-type DnaQ-like 3'-5 exonuclease containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The ExoI structure is unique among DnaQ family enzymes in that there is a large distance between the two metal ions required for catalysis and the catalytic histidine is oriented away from the active site
LFYDYETFGLNPSFDQILQFAAIRTDENFNEIEPFNIFCRLPPDVLPSPEALIVTGITPQQLLKEGLSEY
EFIAKIHRLFNTPGTCIVGYNNIRFDDEFLRFAFYRNLYDPYTWEWKNGNSRWDLLDVVRAYYALRPDGI
VWPKNDDGKPSFKLEDLAQANGIEHSNAHDALSDVEATIALAK
>gnl|CDD|176651 cd06139, DNA_polA_I_Ecoli_like_exo, DEDDy 3'-5' exonuclease domain of Escherichia coli DNA polymerase I and similar bacterial family-A DNA polymerases. Escherichia coli-like Polymerase I (Pol I), a subgroup of family-A DNA polymerases, contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain in the same polypeptide chain as the polymerase domain. The exonuclease domain contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The 3'-5' exonuclease domain of DNA polymerases has a fundamental role in reducing polymerase errors and is involved in proofreading activity. E. coli DNA Pol I is involved in genome replication but is not the main replicating enzyme. It is also implicated in DNA repair
ELEKAKVFAFDTETTSLDPMQAELVGISFAVEPGEAYYIPLGHDYGGEQLPREEVLAALKPLLEDPSIKK
VGQNLKFDLHVLANHGIELRGPAFDTMLASYLLNPGRRRHGLDDLAERYLGHKTISFEDLVGKGKKQITF
DQVPLEKAAEYAAEDADITLRLYELLKPKLKEEPGLLELYEEIEMPLIPVLAE
>gnl|CDD|176652 cd06140, DNA_polA_I_Bacillus_like_exo, inactive DEDDy 3'-5' exonuclease domain of Bacillus stearothermophilus DNA polymerase I and similar family-A DNA polymerases. Bacillus stearothermophilus-like Polymerase I (Pol I), a subgroup of the family-A DNA polymerases, contains an inactive DnaQ-like 3'-5' exonuclease domain in the same polypeptide chain as the polymerase region. The exonuclease-like domain of these proteins possess the same fold as the Klenow fragment (KF) of Escherichia coli Pol I, but does not contain the four critical metal-binding residues necessary for activity. The function of this domain is unknown. It might act as a spacer between the polymerase and the 5'-3' exonuclease domains. Some members of this subgroup, such as those from Bacillus sphaericus and Thermus aquaticus, are thermostable DNA polymerases
RLADEVALYVELLGENYHTADIIGLALANGGGAYYIPLELALLDLAALKEWLEDEKIPKVGHDAKRAYVA
LKRHGIELAGVAFDTMLAAYLLDPTRSSYDLADLAKRYLGRELPSDEEVYGKGAKFAVPDEEVLAEHLAR
KAAAIARLAPKLEEELEENEQLELYYEVELPLAEVLAE
>gnl|CDD|176653 cd06141, WRN_exo, DEDDy 3'-5' exonuclease domain of WRN and similar proteins. WRN is a unique RecQ DNA helicase exhibiting an exonuclease activity. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. Mutations in the WRN gene cause Werner syndrome, an autosomal recessive disorder associated with premature aging and increased susceptibility to cancer and type II diabetes. WRN interacts with key proteins involved in DNA replication, recombination, and repair. It is believed to maintain genomic stability and life span by participating in DNA processes. WRN is stimulated by Ku70/80, an important regulator of genomic stability
TDSAQDAEEAVKELLGKEKVVGFDTEWRPSFRKGKRNKVALLQLATESRCLLFQLAHMDKLPPSLKQLLE
DPSILKVGVGIKGDARKLARDFGIEVRGVVDLSHLAKRVGPRRKLVSLARLVEEVLGLPLSKPKKVRCSN
WEARPLSKEQILYAATDAYASLELYRKLLA
>gnl|CDD|176654 cd06142, RNaseD_exo, DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins. Ribonuclease (RNase) D is a bacterial enzyme involved in the maturation of small stable RNAs and the 3' maturation of tRNA. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. In vivo, RNase D only becomes essential upon removal of other ribonucleases. Eukaryotic RNase D homologs include yeast Rrp6p, human PM/Scl-100, and the Drosophila melanogaster egalitarian protein
ELEDLCERLASAGVIAVDTEFMRLNTYYPRLCLIQISTGGEVYLIDPLAIGDLSPLKELLADPNIVKVFH
AAREDLELLKRDFGILPQNLFDTQIAARLLGLGDSVGLAALVEELLGVELDKGEQRSDWSKRPLTDEQLE
YAALDVRYLLPLYEKLKEELEEEGRLEWAEEECELLLD
>gnl|CDD|99846 cd06143, PAN2_exo, DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2. PAN2 is the catalytic subunit of poly(A) nuclease (PAN), a Pab1p-dependent 3'-5' exoribonuclease which plays an important role in the posttranscriptional maturation of pre-mRNAs. PAN catalyzes the deadenylation of poly(A) tails, which are initially synthesized to default lengths of 70 to 90, to mRNA-specific lengths of 55 to 71. Pab1p and PAN also play a role in the export and decay of mRNA. PAN2 contains a DEDDh-type DnaQ-like 3'-5' exonuclease domain with three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis
VAIDAEFVKLKPEETEIRSDGTKSTIRPSQMSLARVSVVRGEGELEGVPFIDDYISTTEPVVDYLTRFSG
IKPGDLDPKTSSKNLTTLKSAYLKLRLLVDLGCIFVGHGLAKDFRVINIQVPKEQVIDTVELFHLPGQRK
LSLRFLAWYLLGEKIQSETHDSIEDARTALKLYR
>gnl|CDD|99847 cd06144, REX4_like, DEDDh 3'-5' exonuclease domain of RNA exonuclease 4, XPMC2, Interferon Stimulated Gene product of 20 kDa, and similar proteins. This subfamily is composed of RNA exonuclease 4 (REX4 or Rex4p), XPMC2, Interferon (IFN) Stimulated Gene product of 20 kDa (ISG20), and similar proteins. REX4 is involved in pre-rRNA processing. It controls the ratio between the two forms of 5.8S rRNA in yeast. XPMC2 is a Xenopus gene which was identified through its ability to correct a mitotic defect in fission yeast. The human homolog of XPMC2 (hPMC2) may be involved in angiotensin II-induced adrenal cell cycle progression and cell proliferation. ISG20 is an IFN-induced antiviral exonuclease with a strong preference for single-stranded RNA and minor activity towards single-stranded DNA. These proteins are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. REX proteins function in the processing and maturation of many RNA species, similar to the function of Escherchia coli RNase T
VALDCEMVGVGPDGSESALARVSIVNEDGNVVYDTYVKPQEPVTDYRTAVSGIRPEHLKDAPDFEEVQKK
VAELLKGRILVGHALKNDLKVLKLDHPKKLIRDTSKYKPLRKTAKGKSPSLKKLAKQLLGLDIQEGEHSS
VEDARAAMRLYR
>gnl|CDD|99848 cd06145, REX1_like, DEDDh 3'-5' exonuclease domain of RNA exonuclease 1, -3 and similar eukaryotic proteins. This subfamily is composed of RNA exonuclease 1 (REX1 or Rex1p), REX3 (or Rex3p), and similar eukaryotic proteins. In yeast, REX1 and REX3 are required for 5S rRNA and MRP (mitochondrial RNA processing) RNA maturation, respectively. They are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. REX1 is the major exonuclease responsible for pre-tRNA trail trimming and may also be involved in nuclear CCA turnover. REX proteins function in the processing and maturation of many RNA species, similar to the function of Escherichia coli RNase T
FALDCEMCYTTDGLELTRVTVVDENGKVVLDELVKPDGEIVDYNTRFSGITEEMLENVTTTLEDVQKKLL
SLISPDTILVGHSLENDLKALKLIHPRVIDTAILFPHPRGPPYKPSLKNLAKKYLGRDIQQGEGGHDSVE
DARAALELVK
>gnl|CDD|176655 cd06146, mut-7_like_exo, DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins. The mut-7 subfamily is composed of Caenorhabditis elegans mut-7 and similar proteins found in plants and metazoans. Mut-7 is implicated in posttranscriptional gene silencing. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs, termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis
IHIVDSEEELEALLLALSLEAGRVVGIDSEWKPSFLGDSDPRVAILQLATEDEVFLLDLLALENLESEDW
DRLLKRLFEDPDVLKLGFGFKQDLKALSASYPALKCMFERVQNVLDLQNLAKELQKSDMGRLKGNLPSKT
KGLADLVQEVLGKPLDKSEQCSNWERRPLREEQILYAALDAYCLLEVFDKLLE
>gnl|CDD|99850 cd06147, Rrp6p_like_exo, DEDDy 3'-5' exonuclease domain of yeast Rrp6p, human polymyositis/scleroderma autoantigen 100kDa, and similar proteins. Yeast Rrp6p and its human homolog, the polymyositis/scleroderma autoantigen 100kDa (PM/Scl-100), are exosome-associated proteins involved in the degradation and processing of precursors to stable RNAs. Both proteins contain a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. The motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. PM/Scl-100, an autoantigen present in the nucleolar compartment of the cell, reacts with autoantibodies produced by about 50% of patients with polymyositis-scleroderma overlap syndrome
DETPLTFVDTEEKLEELVEKLKNCKEIAVDLEHHSYRSYLGFTCLMQISTREEDYIVDTLKLRDDMHILN
EVFTDPNILKVFHGADSDIIWLQRDFGLYVVNLFDTGQAARVLNLPRHSLAYLLQKYCNVDADKKYQLAD
WRIRPLPEEMIKYAREDTHYLLYIYDRLRNELLERANALAPNLLESVLNCSR
>gnl|CDD|99851 cd06148, Egl_like_exo, DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins. The Egalitarian (Egl) protein subfamily is composed of Drosophila Egl and similar proteins. Egl is a component of an mRNA-binding complex which is required for oocyte specification. Egl contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. The motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The conservation of this subfamily throughout eukaryotes suggests that its members may be part of ancient RNA processing complexes that are likely to participate in the regulated processing of specific mRNAs. Some members of this subfamily do not have a completely conserved YX(3)D pattern at the ExoIII motif
KEAIIHLKKQKVIGLDCEGVNLGRKGKLCLVQIATRTGQIYLFDILKLGSIVFINGLKDILESKKILKVI
HDCRRDSDALYHQYGIKLNNVFDTQVADALLQEQETGGFNPDRVISLVQLLDKYLYISISLKEDVKKLMR
EDPKFWALRPLTEDMIRYAALDVLCLLPLYYAMLDALISKFLKAVFKYLNTERNLSE
>gnl|CDD|99852 cd06149, ISG20, DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar proteins. Interferon (IFN) Stimulated Gene product of 20 kDa (ISG20) is an IFN-induced antiviral exonuclease with a strong preference for single-stranded RNA and minor activity towards single-stranded DNA. It was also independently identified by its response to estrogen and was called HEM45 (human estrogen regulated transcript). ISG20 is a DEDDh-type DnaQ-like 3'-5' exonuclease containing three conserved sequence motifs termed ExoI, ExoII and ExoIII with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. ISG20 may be a major effector of innate immunity against pathogens including viruses, bacteria, and parasites. It is located in promyelocytic leukemia (PML) nuclear bodies, sites for oncogenic DNA viral transcription and replication. It may carry out its function by degrading viral RNAs as part of the IFN-regulated antiviral response
VAIDCEMVGTGPGGRESELARCSIVNYHGDVLYDKYIRPEGPVTDYRTRWSGIRRQHLVNATPFAVAQKE
ILKILKGKVVVGHAIHNDFKALKYFHPKHMTRDTSTIPLLNRKAGFPENCRVSLKVLAKRLLHRDIQVGR
QGHSSVEDARATMELYK
>gnl|CDD|100007 cd06150, YjgF_YER057c_UK114_like_2, This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site
ARMSQAVVHNGTVYLAGQVADDTSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNA
VWDAWVPPGHAPARACVEAKLADPGYLVEIVVTAA
>gnl|CDD|100008 cd06151, YjgF_YER057c_UK114_like_3, This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site
IAQAVEVPAGAATIYLSGTVPAVVNASAPKGSPARYGDTETQTISVLKRIETILQSQGLTMGDVVKMRVF
LVADPALDGKMDFAGFMKAYRQFFGTAEQPNKPARSTLQVAGLVNPGWLVEIEVVA
>gnl|CDD|100009 cd06152, YjgF_YER057c_UK114_like_4, YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site
LHYSQAVRIGDRIEISGQGGWDPDTGKIPEDLEEEIDQAFDNVELALKAAGGKGWEQVYKVNSYHVDIKN
EEAFGLMVENFKKWMPNHQPIWTCVGVTALGLPGMRVEIEVDAI
>gnl|CDD|100010 cd06153, YjgF_YER057c_UK114_like_5, This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site
FSRATLLAAGGRTHLFISGTASIVGHGTVHPGDVEAQTRETLENIEALLEAAGRGGGAQFLADLLRLKVY
LRDREDLPAVRAILAARLGPAVPAVFLQADVCRPDLLVEIEAVA
>gnl|CDD|100011 cd06154, YjgF_YER057c_UK114_like_6, This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site
ISSGSPWEEQAGYSRAVRVGNWVFVSGTTGYDYDGMVMPGDAYEQTRQCLEIIEAALAEAGASLEDVVRT
RMYVTDIADFEAVGRAHGEVFGDIRPAATMVVVSLLVDPEMLVEIEVTA
>gnl|CDD|100012 cd06155, eu_AANH_C_1, A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine nucleotide alpha hydrolase (AANH)-like domain located N-terminal to two distinctly different YjgF-YER057c-UK114-like domains. This CD contains the first of these domains. The YjgF-YER057c-UK114 protein family is a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site
LSQNRTGGLLWISNVTASESDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYG
TFFDKPNPPSRVCVECGLPEGCDVQLSCVAA
>gnl|CDD|100013 cd06156, eu_AANH_C_2, A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine nucleotide alpha hydrolase (AANH)-like domain located N-terminal to two distinctly different YjgF-YER057c-UK114-like domains. This CD contains the second of these domains. The YjgF-YER057c-UK114 protein family is a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site
YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVLSLQHLERVAKAMNVQWVLAAVCYVTDESSVPIA
RSAWSKYCSELDLEDESRNESDDVNPPLVIVVVPELPRGALVEWQGIA
>gnl|CDD|132726 cd06157, NR_LBD, The ligand binding domain of nuclear receptors, a family of ligand-activated transcription regulators. Ligand-binding domain (LBD) of nuclear receptor (NR): Nuclear receptors form a superfamily of ligand-activated transcription regulators, which regulate various physiological functions in metazoans, from development, reproduction, to homeostasis and metabolism. The superfamily contains not only receptors for known ligands but also orphan receptors for which ligands do not exist or have not been identified. The members of the family include receptors of steroids, thyroid hormone, retinoids, cholesterol by-products, lipids and heme. With few exceptions, NRs share a common structural organization with a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
ELLCELATRDLLLIVEWAKSIPGFRELPLEDQIVLLKSFWLELLVLDLAYRSYKNGLSLLLAPNGGHTDD
DKEDEMKLLLKGELIRLLFEFVNPLRALKLDDEEYALLKAIVLFSPDRKESLEDRKIVEELQERLLEALQ
DYLRKNYPEEAPSRFAKLLLLLPSLRKL
>gnl|CDD|100079 cd06158, S2P-M50_like_1, Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group includes bacterial, eukaryotic, and Archaeal S2P/M50s homologs with a minimal core protein and no PDZ domains
ILIVIIAVLLAITLHEFAHAYVAYRLGDPTARRAGRLTLNPLAHIDPIGTIILPLLLPFLFGWAKPVPVN
PRNFKNPRRGMLLVSLAGPLSNLLLALLFALLLRLLPAFGGVVASFLFLMLAYGVLINLVLAVFNLLPIP
PLDGSKILAALLPRRLAEAYARLEPYGFLILLALLFTGILG
>gnl|CDD|100080 cd06159, S2P-M50_PDZ_Arch, Uncharacterized Archaeal homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group appears to be limited to Archaeal S2P/M50s homologs with additional putative N-terminal transmembrane spanning regions, relative to the core protein, and either one or two PDZ domains present
YLALILFLIYWILISILRKRGILEYNISTYGPFLMLRTKKGRGFIDKLARPKRFWRAFGNIGIPIAFVGM
IFMLLLILLSAIIILSGPPAPLNAPRNVLVIPGVNIFIPLPYGIIALVVGVVVHELSHGILARVEGIKVK
SGGLLLLIIPPGAFVEPDEEELNKADRRIRLRIFAAGVTANFVVALIAFALFFLYWIFWINFLLGLFNCL
PAIPLDGGHVFRDLLEALLRRFPSEKAERVVNAITYYLSSLVLLSLLFMIFGP
>gnl|CDD|100081 cd06160, S2P-M50_like_2, Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group includes bacterial, eukaryotic, and Archaeal S2P/M50s homologs with additional putative N- and C-terminal transmembrane spanning regions, relative to the core protein, and no PDZ domains
LLLLVLTLLTTLLVGAWLSGNDVPGNPLLLLQGLPFALALLAILGIHEMGHYLAARRHGVKASLPYFIPF
PFIGTFGAFIRMRSPIPNRKALFDIALAGPLAGLLLALPVLIIGLAVAGWVGLLVTALNLLPVGQLDGGH
IVRALFGRRVAALIGIGLLVALGLLALYLSFSIWLLWALLLLI
>gnl|CDD|100082 cd06161, S2P-M50_SpoIVFB, SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates intramembrane proteolysis (RIP), and is involved in the pro-sigmaK pathway of bacterial spore formation. SpoIVFB (sporulation protein, stage IV cell wall formation, F locus, promoter-distal B) is one of 4 proteins involved in endospore formation; the others are SpoIVFA (sporulation protein, stage IV cell wall formation, F locus, promoter-proximal A), BofA (bypass-of-forespore A), and SpoIVB (sporulation protein, stage IV cell wall formation, B locus). SpoIVFB is negatively regulated by SpoIVFA and BofA and activated by SpoIVB. It is thought that SpoIVFB, SpoIVFA, and BofA are located in the mother-cell membrane that surrounds the forespore and that SpoIVB is secreted from the forespore into the space between the two where it activates SpoIVFB
IILHHSWFLLLLLIAILLGPGVGPVAWLLGLLEALLLFLSVLLHELGHALVARRYGIRVRSITLLPFGGV
AELEEEPETPKEEFVIALAGPLVSLLLAGLFYLLYLLLPGGGPLSSLLEFLAQVNLILGLFNLLPALPLD
GGRVLRALLWRRTGYRRATRIAARIGQLFAILLVVLGLFLLFLGLGNLWLLLIALFIYLAAEAELRRA
>gnl|CDD|100083 cd06162, S2P-M50_PDZ_SREBP, Sterol regulatory element-binding protein (SREBP) Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50A), regulates intramembrane proteolysis (RIP) of SREBP and is part of a signal transduction mechanism involved in sterol and lipid metabolism. In sterol-depleted mammalian cells, a two-step proteolytic process releases the N-terminal domains of SREBPs from membranes of the endoplasmic reticulum (ER). These domains translocate into the nucleus, where they activate genes of cholesterol and fatty acid biosynthesis. The first cleavage occurs at Site-1 within the ER lumen to generate an intermediate that is subsequently released from the membrane by cleavage at Site-2, which lies within the first transmembrane domain. It is the second proteolytic step that is carried out by the SREBP Site-2 protease (S2P) which is present in this CD family. This group appears to be limited to eumetazoan proteins and contains one PDZ domain
LVVVVVGGWGVVYFFDTFLKSSSCMKYPYEAFLKNTGLSISPFHIRWHTTAFNRLFYRWGRAKPRLLYLW
FSLGVVFGVLAMFLSVFLLGKTLMQTLSQMMASSPAVANEQVLQVVVPGVNLPLSQLGYYFTALLISGVV
HEMGHGVAAVREQVRVNGFGIFFFIIYPGAYVDLFTDHLNLISPVQQLRIFCAGVWHNFVLGLVGYLLLI
ETFLKYLISLSGALAVINAVPCFALDGQWILSTFLEATLVSVIVQKDKRDLIGFFILLVGSLLLAAN
>gnl|CDD|100084 cd06163, S2P-M50_PDZ_RseP-like, RseP-like Site-2 proteases (S2P), zinc metalloproteases (MEROPS family M50A), cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. In Escherichia coli, the S2P homolog RseP is involved in the sigmaE pathway of extracytoplasmic stress responses. Also included in this group are such homologs as Bacillus subtilis YluC, Mycobacterium tuberculosis Rv2869c S2P, and Bordetella bronchiseptica HurP. Rv2869c S2P appears to have a role in the regulation of prokaryotic lipid biosynthesis and membrane composition and YluC of Bacillus has a role in transducing membrane stress. This group includes bacterial and eukaryotic S2P/M50s homologs with either one or two PDZ domains present. PDZ domains are believed to have a regulatory role. The RseP PDZ domain is required for the inhibitory reaction that prevents cleavage of its substrate, RseA
ILAFILVLGILIFVHELGHFLVAKLFGVKVEEFSIGFGPKLFSFKKGETEYSISAIPLGGYVKMLGEDPE
EEADPEDDPRSFNSKPVWQRILIVFAGPLANFLLAIVLFAVLLSFLALLSINLGILNLLPIPALDGGHLL
FLLIEAIRGRPLSEKVEEIIQTIGFALLLGLMLFVTFNDIVR
>gnl|CDD|100085 cd06164, S2P-M50_SpoIVFB_CBS, SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates intramembrane proteolysis (RIP), and is involved in the pro-sigmaK pathway of bacterial spore formation. In this subgroup, SpoIVFB (sporulation protein, stage IV cell wall formation, F locus, promoter-distal B) contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain. SpoIVFB is one of 4 proteins involved in endospore formation; the others are SpoIVFA (sporulation protein, stage IV cell wall formation, F locus, promoter-proximal A), BofA (bypass-of-forespore A), and SpoIVB (sporulation protein, stage IV cell wall formation, B locus). SpoIVFB is negatively regulated by SpoIVFA and BofA and activated by SpoIVB. It is thought that SpoIVFB, SpoIVFA, and BofA are located in the mother-cell membrane that surrounds the forespore and that SpoIVB is secreted from the forespore into the space between the two where it activates SpoIVFB. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown
GRIFGIPIRLHPSWLLILALIAWSFGPGVFPAVPPALGAVAWLLGLAAALLLFASVLLHELGHSLVARRY
GIPVRSITLFLFGGVARLEREPETPGQEFVIAIAGPLVSLVLALLFLLLSLALPGSGAGPLGVLLGYLAL
INLLLAVFNLLPAFPLDGGRVLRALLWRRTGDYLKATRIAAWVGRGFAVLLIILGLLSLFLNLLGGLWLI
LIAWFLYIGAGAEARQA
>gnl|CDD|320680 cd06165, Sortase_A, Sortase domain found in class A sortases. Class A sortases are membrane-bound cysteine transpeptidases distributed in Gram-positive bacteria (mainly present in Firmicutes). They perform a housekeeping role in the cell as members of this group are capable of anchoring a large number of functionally distinct surface proteins containing a cell wall sorting signal to an amino group located on the bacterial cell wall. They do so by catalyzing a transpeptidation reaction in which the surface protein substrate is cleaved at a conserved cell wall-sorting signal (Class A sortases recognize a canonical LPXTG motif, X can be any amino acid), and covalently linked to peptidoglycan for display on the bacterial surface. The prototypical sortase A protein from Staphylococcus aureus (named Sa-SrtA) cleaves the amide bond between threonine and glycine residues of the canonical LPXTG motif in a wide range of protein substrates with diverse functions that can promote bacterial adhesion, nutrient acquisition, host cell invasion, and immune evasion. Next, it catalyzes a transpeptidation reaction by which the proteins are covalently linked to the peptidoglycan precursor lipid II. SrtA is therefore affects the ability of a pathogen to establish successful infection. SrtA contains an N-terminal hydrophobic segment, a linker region and an extra-cellular C-terminal catalytic domain. The hydrophobic segment functions as both a signal peptide for secretion and a stop-transfer signal for membrane anchoring. The catalytic domain contains the catalytic TLXTC signature sequence where X is usually a valine, isoleucine or a threonine. The gene encoding SrtA is generally not located in the same gene cluster as its substrates while the gene encoding SrtB is usually clustered in the same locus as its substrate
LNVIGAIAIPSVGINLPIFKGLSNENLLVGAGTMKPNQKMGKGNYVLAGHNMGDGGLLFSPLQNLKKGDK
IYLTDLKKVYEYKVTSKKVVDPTDVDVLDDTKGKPLLTLITCDDPTDTTKRIVVQGE
>gnl|CDD|320681 cd06166, Sortase_D_2, Sortase domain found in subfamily 2 of the class D family of sortases. Class D sortases are cysteine transpeptidases distributed in Gram-positive bacteria (mainly present in Firmicutes). They anchor surface proteins bearing a cell wall sorting signal to peptidoglycans of the bacterial cell wall envelope, which is responsible for spore formation under anaerobic conditions. This involves a transpeptidation reaction in which the surface protein substrate is cleaved at the cell wall sorting signal and covalently linked to peptidoglycan for display on the bacterial surface. The prototypical subfamily 2 of class D sortase from Clostridium perfringens (named Cp-SrtD) recognizes the LPQTGS signal motif for transpeptidation. Its catalytic activity is in a metal cation- and temperature- dependent manner. The presence of magnesium appears to enhance Cp-SrtD catalysis towards the LPQTGS signal motif
GGVIGILEIPKIDLKLPILEGATEENLKYGVGHFEGTAMPGEGGNFAIAGHRSYTYGRFFNRLDELKIGD
EIIVTTKNGTYTYKVTEIFIVEPTDVSVLDPTEGKKEITLITCTPINPTHRLIVKAE
>gnl|CDD|350201 cd06167, PIN_LabA-like, PIN domain of Synechococcus elongatus LabA (low-amplitude and bright) and related proteins. The LabA-like PIN domain family includes Synechococcus elongatus PCC 7942 LabA which participates in cyanobacterial circadian timing. It is required for negative feedback regulation of the autokinase/autophosphatase KaiC, a central component of the circadian clock system. In particular, LabA seems necessary for KaiC-dependent repression of gene expression. This family also includes the N-terminal domain of limkain b1, a human autoantigen associated with cytoplasmic vesicles. Other members are the LabA-like PIN domains of human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into this family
GVLVDADNCSNGFGALILRRYAGLFLQMGFEKYANINAQPLLVPPSNNRGFTVIRVAAKRKDAADVALVR
QAGRLAYTGAPDTVVLVSGDKLDFSDLIEKAKEAGLNVIVVGP
>gnl|CDD|212486 cd06168, LSMD1, LSM domain containing 1. The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. LSMD1 proteins have a single Sm-like domain structure. Sm-like proteins exist in archaea as well as prokaryotes, forming heptameric and hexameric ring structures similar to those found in eukaryotes
RLKLRKLLGRTLRVTLTDGRVLVGTFVCTDKDGNIILSNAEEYRKPSDLGAEEPRSLGLVMVPGKHIVSI
EVD
>gnl|CDD|132884 cd06169, BMC, Bacterial Micro-Compartment (BMC) domain. Bacterial micro-compartments are primitive protein-based organelles that sequester specific metabolic pathways in bacterial cells. The prototypical bacterial microcompartment is the carboxysome shell, a bacterial polyhedral organelle which increase the efficiency of CO2 fixation by encapsulating RuBisCO and carbonic anhydrase. They can be divided into two types: alpha-type carboxysomes (alpha-cyanobacteria and proteobacteria) and beta-type carboxysomes (beta-cyanobacteria). In addition to these proteins there are several homologous shell proteins including those found in pdu organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol and eut organelles involved in the cobalamin-dependent degradation of ethanolamine. Structure evidence shows that several carboxysome shell proteins and their homologs (Csos1A, CcmK1,2,4, and PduU) exist as hexamers which might further assemble into extended, tightly packed layers hypothesized to represent the flat facets of the polyhedral organelles outer shell. Although it has been suggested that other homologous proteins in this family might also form hexamers and play similar functional roles in the construction of their corresponding organelle outer shell at present no experimental evidence directly supports this view
ALGLLEVRGLAAAIVAADAAVKAADVELVGIERAGGGGLVTLIIRGDVSAVKAAVEAAEQAA
>gnl|CDD|99777 cd06170, LuxR_C_like, C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix motif and binds DNA. Proteins belonging to this group are response regulators; some act as transcriptional activators, others as transcriptional repressors. Many are active as homodimers. Many are two domain proteins in which the DNA binding property of the C-terminal DNA binding domain is modulated by modifications of the N-terminal domain. For example in the case of Lux R which participates in the regulation of gene expression in response to fluctuations in cell-population density (quorum-sensing), a signaling molecule, the pheromone Acyl HSL (N-acyl derivatives of homoserine lactone), binds to the N-terminal domain and leads to LuxR dimerization. For others phophorylation of the N-terminal domain leads to multimerization, for example Escherichia coli NarL and Sinorhizobium melilot FixJ. NarL controls gene expression of many respiratory-related operons when environmental nitrate or nitrite is present under anerobic conditions. FixJ is involved in the transcriptional activation of nitrogen fixation genes. The group also includes small proteins which lack an N-terminal signaling domain, such as Bacillus subtilis GerE. GerE is dimeric and acts in conjunction with sigmaK as an activator or a repressor modulating the expression of various genes in particular those encoding the spore-coat. These LuxR family regulators may share a similar organization of their target binding sites. For example the LuxR dimer binds the lux box, a 20bp inverted repeat, GerE dimers bind two 12bp consensus sequences in inverted orientation having the central four bases overlap, and the NarL dimer binds two 7bp inverted repeats separated by 2 bp
LTPREREVLRLLAEGKTNKEIADILGISEKTVKTHLRNIMRKLGVKSRTQLVAYAIR
>gnl|CDD|100119 cd06171, Sigma70_r4, Sigma70, region (SR) 4 refers to the most C-terminal of four conserved domains found in Escherichia coli (Ec) sigma70, the main housekeeping sigma, and related sigma-factors (SFs). A SF is a dissociable subunit of RNA polymerase, it directs bacterial or plastid core RNA polymerase to specific promoter elements located upstream of transcription initiation points. The SR4 of Ec sigma70 and other essential primary SFs contact promoter sequences located 35 base-pairs upstream of the initiation point, recognizing a 6-base-pair -35 consensus TTGACA. Sigma70 related SFs also include SFs which are dispensable for bacterial cell growth for example Ec sigmaS, SFs which activate regulons in response to a specific signal for example heat-shock Ec sigmaH, and a group of SFs which includes the extracytoplasmic function (ECF) SFs and is typified by Ec sigmaE which contains SR2 and -4 only. ECF SFs direct the transcription of genes that regulate various responses including periplasmic stress and pathogenesis. Ec sigmaE SR4 also contacts the -35 element, but recognizes a different consensus (a 7-base-pair GGAACTT). Plant SFs recognize sigma70 type promoters and direct transcription of the major plastid RNA polymerase, plastid-encoded RNA polymerase (PEP)
RERLEEALDKLPEREREVILLRFGEGLSYEEIAEILGISRSTVRQRLHRALKKLR
>gnl|CDD|340862 cd06172, MFS_LacY, LacY proton/sugar symporter family of the Major Facilitator Superfamily of transporters. LacY proton/sugar family (also called LacY/RafB family) symporters are integral membrane proteins responsible for the transport of specific beta-glucosides into the cell accompanied by the import of a proton. Members include lactose permease (LacY), raffinose permease (RafB), and sucrose permease, which facilitate the transport of beta-galactosides, raffinose, and sucrose, respectively. The prototypical member, LacY, contains 12 transmembrane helices connected by hydrophilic loops with both N and C termini on the cytoplasmic face. The LacY/RafB permease family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
YWKFSLFFFLFFFIWSASFSFFPIWLTQINHLSGSETGIVFSANSLFALLFQPVYGLISDKLGLKKHLLW
FISGLLVLFGPFFIFVYGPLLQSNILLGAIVGGIYLGFAFLAGCGAIESYIERVSRRFNFEYGRARMWGS
LGWALAAFFAGILFNINPNINFWLGSGFALILLLLLLFAKPEDSDTAAAAGANASSVSLKDVLELFRMPK
FWFFILFVIGVSCFYDVFDQQFPPYFTSLFATPEQGNRVFGYLNSAQVFLEAGMMFLAPLIVNRIGAKNG
LLLAGTIMAVRIIGSGLATSPLEISILKLLHAFEVPLLLVSIFKYITSHFDTRLSATLYLVGFQFAKQLG
AVVLSPLAGNLYDSIGFQQTYLVLGGIVLVFTLISVFTL
>gnl|CDD|340863 cd06173, MFS_MefA_like, Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
FRLLWLAQLLSALGDWIFTVALPWLVLQLTGSALLVGLVLAAFFLPFLLFSPFAGVLADRFDRRRLLILA
DLLRALLAAVLALLALLGSLSLWLLLVLAFLLGIASAFFGPARQALLPELVPKEQLVRANALNSLATQLA
RIIGPALGGLLVALLGPGGAFAINALSFLLSALLLLFIRRPPPAAPGESSSLLLRDLREGLRYLRRSPLL
RLLLLALALFALLGGALTVLLPLLAKEVLGGGAAGYGLLLAAFGVGALLGALLLGRLSKRRRRGRLLLIG
ALLLGLALLVLGLSPSLWLLLAALFLLGLAGGLFNVPLNTLLQLRVPDELRGRVFSVYNALNSGAMPLGA
LLAGLLADALGLSAVFLLAGALLLLAALLLLLL
>gnl|CDD|349949 cd06174, MFS, Major Facilitator Superfamily. The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated
LLLGFFLTGLARGLISPLLPALLQSFGLSASQLGLLFALFSLGYALLQPLAGLLADRFGRRPVLLLGLLL
FALGALLFAFAPSFWLLLLGRFLLGLGSGLIDPAVLALIADLFPERERGRALGLLQAFGSVGGILGPLLG
GILASSLGFGWRAVFLIAAALALLAAILLLLVVPDPPESARAKNEEASSKSVLKLLKRVLKNPGLWLLLL
AIFLVNLAYYSFSTLLPLFLLDLGGLSVAVAGLLLSLFGLAGALGSLLLGLLSDRLIGRKPLLLIGLLLM
ALGLALLLLAPSLLLLLLLLLLLGFGLGGLLPLSFALIAELFPPEIRGTAFGLLNTFGFLGGAIGPLLAG
FLLAATFGLTGAFLVLAVLLLLAAILLL
>gnl|CDD|340865 cd06175, MFS_POT, Proton-coupled oligopeptide transporter (POT) family of the Major Facilitator Superfamily of transporters. The Proton-coupled oligopeptide transporter (POT) family is present across all major kingdoms of life and is known by a variety of names. It is referred to as the Nitrate transporter/Peptide transporter (NRT1/PTR) family (NPF) in plants, and in addition to POT, it is also known as the Peptide transporter (PepT/PTR) or Solute Carrier 15 (SLC15) family in animals. Members of this family are proton-driven symporters involved in nitrogen acquisition in the form of di- and tripeptides. Plant members transport other nitrogenous ligands including nitrate, the plant hormone auxin, and glucosinolate compounds that are important for seed defense. POT proteins exhibit substrate multispecificity, with one transporter able to recognize as many as 8,400 types of di/tripeptides and certain peptide-like drugs. The POT family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
CAMILLIELCERFTFYGIGANLVPFLTGALGLGNAQAANVVLNFLGTSYVTPLFGGWIADTFLGRYRTIL
IGAAIYAVGVAILTVSTIPPGLRPLRCNPSHCEQASGIQLTGFYAALYLIALGTGGVKANVSPLGADQFD
ERGPSKTQSFFNWFYFCINVGSLLAMLGTPYIQDNVGWAAAYGIPFVAILLALVVFEVKQLLRALPLFAF
CILFWTVYAQMTTSYVLQALTLVRSTGLFTIPPASMQAFNPILLLLLIPVLDKVVYPLIRRYGVGLSPLT
KIGLGFFFGSLSMFVAGFLELKRLNTAHAHGPVVTTSPLSFWWQIPQYLLLGIGEILVSITGLEFAYREA
PKSMKGFIMGLLLLTSGFGSFFGSVLVTLVSKPTDGAHIADDLNKGVLTNFFFLLAVLAALNFLIFLLVS
RK
>gnl|CDD|349950 cd06176, MFS_BCD_PucC-like, Bacteriochlorophyll delivery (BCD) family, also called PucC family, of the Major Facilitator Superfamily. The bacteriochlorophyll delivery (BCD) family, also called PucC family, is composed of the PucC protein and related proteins including LhaA (also called ORF477 and F1696) and bacteriochlorophyll synthase 44.5 kDa chain (also called ORF428). These proteins are found in photosynthetic organisms. Rhodobacter capsulatus LhaA and PucC are implicated in light-harvesting complex 1 and 2 (LH1 and LH2) assembly. PucC may function to shepherd or sequester LH2 alpha and beta proteins to facilitate proper assembly, as well as deliver bacteriochlorophyll a to nascent LH2 complexes. The BCD family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RILRLGLFQVALGMMVVLTTGTLNRVMIVELGLPATLVGLLIALHYLVAPLRVWIGHRSDTHPLRGYRRT
PYIWLGMLLLALGLALAPFAALLLAGAAFWLGLALAVLAFLLYGIGVGAAGTAFLALLADLTPEERRPRA
VTVVWTMLILGIIVTAIVFGRLLDPYSPERLIQVFQIVALVALLLALLALWGVERRRSRAALAAEEAPPE
TFREALRLLWASPQARRFFIFLFLSTLALFMQDVILEPFGGEVFGMSVGETTRLTAIWGGGTLLGMLLAG
FLLSRRLGKKRTAALGCLLSALGFLLLALAGLLGNPWLFRPGVFLLGLGNGLFTVGALTLMMDLTGEGTA
GLFMGLWGAAQALARGLGTLLGGALRDLLRALFGSPALAYGLVFLLEAVLLLVALLLLR
>gnl|CDD|340866 cd06177, MFS_NHS, Nucleoside:H(+) symporter family of the Major Facilitator Superfamily of transporters. The prototypical members of the Nucleoside:H(+) symporter (NHS) family are Escherichia coli nucleoside permease NupG and xanthosine permease. Nucleoside:H(+) symporters are proton-driven transporters that facilitate the import of nucleosides across the cytoplasmic membrane. NupG is a broad-specificity transporter of purine and pyrimidine nucleosides. Xanthosine permease is involved in the uptake of xanthosine and other nucleosides such as inosine, adenosine, cytidine, uridine and thymidine. The NHS family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RLSVMMFLQFFIWGAWLVTLGGYMGSTLGFTGAQIGAVYSTTGIAAIIMPFFLGIIADRFFAAEKVLAVL
HLIGAAALFYAATVTDFSVFFWVMLLYSLCYMPTLALTNSIAFSNLEDPVKDFPPIRVWGTIGWIAAGWP
VGFLGWEASNLQFYIAAGASLLLGLYSLTLPHTPPKKAGKGVSKRSLLGLDAFVLLKNPFFAVFFIFSFL
LGAPLQFYYTFANPFLNDFGMIVKNPAGIMSLGQISEILFMLAIPFFLKRLGIKKVMLIGMLAWVLRFGL
FAYGDPSPGVWMLVLSIILHGVCYDFFFVTGYIYVDKKAPKDIRASAQGLFMLMTNGVGALVGSILSGKV
VDKFTTVEGTKDWQTIWLVPAIYALVLAILFALFFR
>gnl|CDD|340867 cd06178, MFS_unc93-like, Uncharacterized Unc-93-like proteins of the Major Facilitator Superfamily of transporters. This subfamily consists of uncharacterized proteins, mainly from fungi and plants, with similarity to Caenorhabditis elegans uncoordinated protein 93 (also called putative potassium channel regulatory protein unc-93). Unc-93 acts as a regulatory subunit of a multi-subunit potassium channel complex that may function in coordinating muscle contraction in C. elegans. The unc93-like subfamily belongs to the Unc-93 family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
TQVVLVGLVCFCCPGMFNALTGLGGGGQVDPTVANNANTALYATFAVFGFFGGGIFNLLGPRLTLAFGGT
GYPLYAGSLLSYNHVQNQGFVIFAGAILGIGAGLLWTAQGAIMLSYPTENQKGRFIAIFWVIFNLGGVIG
SLIPFGLNYHSTSATVNDATYIAFIVLMAVGAVLALLLLDPPKVVRKDGGRVAAIKSATWVSEELKLLLK
LFKDPKMLLLFPAFFASNWFYTYQFNGVNGYLFNLRTRSLNNVLYWGAQMFGAYVIGYLLDAKFMSRRTR
AFIGLAIVFVIGMAIWGGGLAFQLSYTRDDVKPTPKIDDKTGRRYAGPFVLYLFYGILDAIYQTYVYWTM
GALSNDPRKLARYAGFYKGIQSAGAAIAWRLDALKVSYMTQLIICWVLLAVGLPLASPVIYFYKK
>gnl|CDD|340868 cd06179, MFS_TRI12_like, Fungal trichothecene efflux pump (TRI12) of the Major Facilitator Superfamily of transporters. This family includes Fusarium sporotrichioides trichothecene efflux pump (TRI12), which may play a role in F. sporotrichioides self-protection against trichothecenes. TRI12 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
AALCLAYFAQLFGVTLPAAVLPFIVADLGPSSNSTWISTAWSLAQAVLGPIVGRLSDLFGRRWFFIGGNL
LGVVGSIVAGTAKSVNMLIGGQALIGIGAGTQGLGAAVASELVPNKYRGLVQGVVNLVASPGSALGPLIA
GALVEANAAGWRWIFYINAIFNALALILLFFFYHPPPRPQLHGSSTRQKLKRLDWVGLFLLIAGLVLFLL
GLSWGGNPYPWSSAHVIAPLVIGGVLLIAFGLYEWKGTKDGLLPPRLLFRGRNFALILIVAFVEGMIFYS
LNIFWPQQISLLFTTDPLKAGLYQLPFGLGTLFGAILAGLLLTKIKHIKWQLVAGFVLFTAFLALLALIT
PDNKALAIAFSVLAGIGIGGPLVLAIVIVQLSVPPEDIGTASGLLGSARALGGAVGTAIFTSILSNRLSK
NLPARVAPAALEAGLPASSLPALLGALASGNIAALTAVPGINPEIIAAATAALKQAYADSFRYVWYAAIP
FGVVAIIAALFLRDIDSYMTDHVDARLE
>gnl|CDD|340869 cd06180, MFS_YjiJ, Uncharacterized protein YjiJ and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of Escherichia coli YjiJ and other uncharacterized proteins. They belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LAGALALAVAMGIGRFAYTPLLPLMLAELGLSYAQAGWIATANYAGYLVGALLASFLRRRGRARRLIRGG
LLLTVLLLAAMALTSGFAALLALRFLAGAASAFVFVFGSNLVLHHATAAGRGHLIGLLFAGVGLGIALSG
LLVPAGLGGGLSWRAGWLALALLSAVLLLLSFLLLRRGPSAPTEASAAESAPGLNRPLWRLALAYGLFGF
GYIITATFLPLIARETGAGSLLAGLLWSLFGLAAVPSCFLWGALSDRWGTRRALAANLLVQAVGVLLPLL
SPGPAGLVLSAVLFGGTFMAITALVMALARELAPPAAPRALALMTASFGVGQILGPLLAGWLADATGGFA
PALILAAAALVVAALLALLVL
>gnl|CDD|198409 cd06181, BI-1-like, BAX inhibitor (BI)-1/YccA-like protein family. Mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. Their broad tissue distribution and high degree of conservation suggests an important regulatory role. This superfamily also contains the lifeguard(LFG)-like proteins and other subfamilies which appear to be related by common descent and also function as inhibitors of apoptosis. In plants, BI-1 like proteins play a role in pathogen resistance. A prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes
STKDFLRKVYMILALQLLLTAATATAFTVCDPGWYWSPALMGLLTSMLALMATAAMIRAKMPVNLILLFG
FTGLMGYVVGPLLFFYGPTILLRALGGTALVFFGLTVYALQARKDFLFLGGPLMAGLGFLLLSFLLNTFF
YSPWLHLVAAAVGLVLFCGFLLYDTQLIIHKAEVGPEDYINACISLYLDIINIFIRLLTILA
>gnl|CDD|99779 cd06182, CYPOR_like, NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal ferredoxin reducatase (FNR)- like FAD and NAD binding module, an FMN-binding domain, and an additional conecting domain (inserted within the FAD binding region) that orients the FNR and FMN binding domains. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2, which then transfers two electrons and a proton to NADP+ to form NADPH
AITVNRKLTPPDSPRSTRHLEFDLSGNSVLKYQPGDHLGVIPPNPLQPRYYSIASSPDVDPGEVHLCVRV
VSYEAPAGRIRKGVCSNFLAGLQLGAKVTVFIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLQERAAL
RANGKARGPAWLFFGCRNFASDYLYREELQEALKDGALTRLDVAFSREQAEPKVYVQDKLKEHAEELRRL
LNEGAHIYVCGDAKSMAKDVEDALVKIIAKAGGVDESDAEEYLKELEDEGRYVEDVW
>gnl|CDD|99780 cd06183, cyt_b5_reduct_like, Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH
FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYP
GGKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLY
ANRTEEDILLREELDELAKKHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPPPSEDTLVLVCGPP
PMIEGAVKGLLKELGYKKDNVFKF
>gnl|CDD|99781 cd06184, flavohem_like_fad_nad_binding, FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling
GGWRGFRPFVVARKVAESEDITSFYLEPADGGPLPPFLPGQYLSVRVKLPGLGYRQIRQYSLSDAPNGDY
YRISVKREPGGLVSNYLHDNVKVGDVLEVSAPAGDFVLDEASDRPLVLISAGVGITPMLSMLEALAAEGP
GRPVTFIHAARNSAVHAFRDELEELAARLPNLKLHVFYSEPEAGDREEDYDHAGRIDLALLRELLLPADA
DFYLCGPVPFMQAVREGLKALGVPAERIHYEVFGPGE
>gnl|CDD|99782 cd06185, PDR_like, Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal
VRIRDEAPDIRSFELEAPDGAPLPAFEPGAHIDVHLPNGLVRQYSLCGDPADRDRYRIAVLREPASRGGS
RYMHELLRVGDELEVSAPRNLFPLDEAARRHLLIAGGIGITPILSMARALAARGADFELHYAGRSREDAA
FLDELAALPGDRVHLHFDDEGGRLDLAALLAAPPAGTHVYVCGPEGMMDAVRAAAAALGWPEARLHFERF
A
>gnl|CDD|99783 cd06186, NOX_Duox_like_FAD_NADP, NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation
IATVELLPDSDVIRLTIPKPKPFKWKPGQHVYLNFPSLLSFWQSHPFTIASSPEDEQDTLSLIIRAKKGF
TTRLLRKALKSPGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSRTRR
VKLVWVVRDREDLEWFLDELRAAQELEVDGEIEIYVTRVVVCGPPGLVDDVRNAVAKKGGTGVEFHEESF
>gnl|CDD|99784 cd06187, O2ase_reductase_like, The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate
VVSVERLTHDIAVVRLQLDQPLPFWAGQYVNVTVPGRPRTWRAYSPANPPNEDGEIEFHVRAVPGGRVSN
ALHDELKVGDRVRLSGPYGTFYLRRDHDRPVLCIAGGTGLAPLRAIVEDALRRGEPRPVHLFFGARTERD
LYDLEGLLALAARHPWLRVVPVVSHEEGAWTGRRGLVTDVVGRDGPDWADHDIYICGPPAMVDATVDALL
ARGAPPERIHFDKF
>gnl|CDD|99785 cd06188, NADH_quinone_reductase, Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain of this group typically contains an iron-sulfur cluster binding domain
PEEVLGAKKWECTVISNDNVATFIKELVLKLPSGEEIAFKAGGYIQIEIPAYEIAYADFDVAEKYRADWD
KFGLWQLVFKHDEPVSRAYSLANYPAEEGELKLNVRIATPPPGNSDIPPGIGSSYIFNLKPGDKVTASGP
FGEFFIKDTDREMVFIGGGAGMAPLRSHIFHLLKTLKSKRKISFWYGARSLKELFYQEEFEALEKEFPNF
KYHPVLSEPQPEDNWDGYTGFIHQVLLENYLKKHPAPEDIEFYLCGPPPMNSAVIKMLDDLGVPRENIAF
DDF
>gnl|CDD|99786 cd06189, flavin_oxioreductase, NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD
CKVESIEPLNDDVYRVRLKPPAPLDFLAGQYLDLLLDDGDKRPFSIASAPHEDGEIELHIRAVPGGSFSD
YVFEELKENGLVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGSKRPIHLYWGARTEED
LYLDELLEAWAEAHPNFTYVPVLSEPEEGWQGRTGLVHEAVLEDFPDLSDFDVYACGSPEMVYAARDDFV
EKGLPEENFFSDAF
>gnl|CDD|99787 cd06190, T4MO_e_transfer_like, Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family
LVDVRELTHDVAEFRFALDGPADFLPGQYALLALPGVEGARAYSMANLANASGEWEFIIKRKPGGAASNA
LFDNLEPGDELELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSDRPVDLFYGGRTPS
DLCALDELSALVALGARLRVTPAVSDAGSGSAAGWDGPTGFVHEVVEATLGDRLAEFEFYFAGPPPMVDA
VQRMLMIEGVVPFDQIHFDRFV
>gnl|CDD|99788 cd06191, FNR_iron_sulfur_binding, Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR was intially identified as a chloroplast reductase activity catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methnae assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H)
LRVAEVRSETPDAVTIVFAVPGPLQYGFRPGQHVTLKLDFDGEELRRCYSLCSSPAPDEISITVKRVPGG
RVSNYLREHIQPGMTVEVMGPQGHFVYQPQPPGRYLLVAAGSGITPLMAMIRATLQTAPESDFTLIHSAR
TPADMIFAQELRELADKPQRLRLLCIFTRETLDSDLLHGRIDGEQSLGAALIPDRLEREAFICGPAGMMD
AVETALKELGMPPERIHTERF
>gnl|CDD|99789 cd06192, DHOD_e_trans_like, FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH
IVKKEQLEPNLVLLTIKAPLAARLFRPGQFVFLRNFESPGLERIPLSLAGVDPEEGTISLLVEIRGPKTK
LIAELKPGEKLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAKKLAANGNKVTVLAGAKKAKEEFL
DEYFELPADVEIWTTDDGELGLEGKVTDSDKPIPLEDVDRIIVAGSDIMMKAVVEALDEWLQLIKASVSN
NSPMCCGIGICGACTIETKHGVKRLCKDGPVFR
>gnl|CDD|99790 cd06193, siderophore_interacting, Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H)
VVRVERLTPHMRRITLGGPDLAGFPSDGPDQHVKLLFPDPGQAPPVLPVLGRRRWPPEEPRPVMRTYTVR
RFDPEAGELDIDFVLHGDEGPASRWAASAQPGDTLGIAGPGGSFLPPPDADWYLLAGDETALPAIAAILE
ELPADARGTALIEVPDAADEQPLPAPAGVEVTWLHRGGAEAGELALLAVRALAPPAGDGYVWIAGEAGAV
RALRRHLREERGVPRAQVYASGYWR
>gnl|CDD|99791 cd06194, FNR_N-term_Iron_sulfur_binding, Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH
VVSLQRLSPDVLRVRLEPDRPLPYLPGQYVNLRRAGGLARSYSPTSLPDGDNELEFHIRRKPNGAFSGWL
GEEARPGHALRLQGPFGQAFYRPEYGEGPLLLVGAGTGLAPLWGIARAALRQGHQGEIRLVHGARDPDDL
YLHPALLWLAREHPNFRYIPCVSEGSQGDPRVRAGRIAAHLPPLTRDDVVYLCGAPSMVNAVRRRAFLAG
APMKRIYADPFE
>gnl|CDD|99792 cd06195, FNR1, Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH
TVLKRRDWTDDLFSFRVTRDIPFRFQAGQFTKLGLPNDDGKLVRRAYSIASAPYEENLEFYIILVPDGPL
TPRLFKLKPGDTIYVGKKPTGFLTLDEVPPGKRLWLLATGTGIAPFLSMLRDLEIWERFDKIVLVHGVRY
AEELAYQDEIEALAKQYNGKFRYVPIVSREKENGALTGRIPDLIESGELEEHAGLPLDPETSHVMLCGNP
QMIDDTQELLKEKGFSKNHRRKPGNITVEKY
>gnl|CDD|99793 cd06196, FNR_like_1, Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH
HTVTLLSIEPVTHDVKRLRFDKPEGYDFTPGQATEVAIDKPGWRDEKRPFTFTSLPEDDVLEFVIKSYPD
HDGVTEQLGRLQPGDTLLIEDPWGAIEYKGPGVFIAGGAGITPFIAILRDLAAKGKLEGNTLIFANKTEK
DIILKDELEKMLGLKFINVVTDEKDPGYAHGRIDKAFLKQHVTDFNQHFYVCGPPPMEEAINGALKELGV
PEDSIVFE
>gnl|CDD|99794 cd06197, FNR_like_2, FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and have a variety of physiological functions in a variety of organisms including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H)
IKSEVITPTLTRFTFELSPPDVVGKWTPGQYITLDFSSELDSGYSHMADDDPQSLNDDFVRTFTVSSAPP
HDPATDEFEITVRKKGPVTGFLFQVARRLREQGLEVPVLGVGGEFTLSLPGEGAERKMVWIAGGVGITPF
LAMLRAILSSRNTTWDITLLWSLREDDLPLVMDTLVRFPGLPVSTTLFITSEVYLCGPPALEKAVLEWLE
GKKVHRESFA
>gnl|CDD|99795 cd06198, FNR_like_3, NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH
ARVTEVRPTTTLTLEPRGPALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGRLRFTIKALGDYTRRL
AERLKPGTRVTVEGPYGRFTFDDRRARQIWIAGGIGITPFLALLEALAARGDARPVTLFYCVRDPEDAVF
LDELRALAAAAGVVLHVIDSPSDGRLTLEQLVRALVPDLADADVWFCGPPGMADALEKGLRALGVPARRF
HYERFE
>gnl|CDD|99796 cd06199, SiR, Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain
TVLENRLLTGPGSEKETRHIELDLEGSGLSYEPGDALGVYPTNDPALVDELLAALGLSGDEPVSTVGGGT
LPLREALIKHYEITTLLLALLESYAADTGALELLALAALEAVLAFAELRDVLDLLPIPPARLTAEELLDL
LRPLQPRLYSIASSPKAVPDEVHLTVAVVRYESHGRERKGVASTFLADRLKEGDTVPVFVQPNPHFRLPE
DPDAPIIMVGPGTGIAPFRAFLQEREATGAKGKNWLFFGERHFATDFLYQDELQQWLKDGVLTRLDTAFS
RDQAEKVYVQDRMREQGAELWAWLEEGAHFYVCGDAKRMAKDVDAALLDIIATEGGMDEEEAEAYLKELK
KEKRYQRDVY
>gnl|CDD|99797 cd06200, SiR_like1, Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH
WRLQARVLLNPGSQGAPLWRLRLTPPDAGAQWQAGDIAEIGPRHPLPHREYSIASLPADGALELLVRQVR
HADGGLGLGSGWLTRHAPIGASVALRLRENPGFHLPDDGRPLILIGNGTGLAGLRSHLRARARAGRHRNW
LLFGERQAAHDFFCREELEAWQAAGHLARLDLAFSRDQAQKRYVQDRLRAAADELRAWVAEGAAIYVCGS
LQGMAPGVDAVLDEILGEEAVEALLAAGRYRRDVY
>gnl|CDD|99798 cd06201, SiR_like2, Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH
GWPPLLPLETIDRQSTQAFARWGRDLGEALGLDLPLDHKKRLPRTKALELVERKDYGAAVQAPTAILRFK
PAKRKLSGKGLPSFEAGDLLGILPPGSDVPRFYSLASSSSDGFLEICVRKHPGGLCSGYLHGLKPGDTIK
AFIRPNPSFRPAKGAAPVILIGAGTGIAPLAGFIRANAARRPMHLYWGGRDPASDFLYEDELDQYLADGR
LTQLHTAFSRTPDGAYVQDRLRADAERLRRLIEDGAQIMVCGSRAMAQGVAAVLEEILAPQPLSLDELKL
QGRYAEDVY
>gnl|CDD|99799 cd06202, Nitric_oxide_synthase, The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses with a heme-containing N-terminal oxidase domain. The reductase portion is similar in structure to NADPH dependent cytochrome-450 reductase (CYPOR), having an inserted connecting sub-domain within the FAD binding portion of FNR. NOS differs from CYPOR in a requirement for the cofactor tetrahydrobiopterin and unlike most CYPOR is dimeric. Nitric oxide synthase produces nitric oxide in the conversion of L-arginine to L-citruline. NOS has been implicated in a variety of processes including cytotoxicity, anti-inflamation, neurotransmission, and vascular smooth muscle relaxation
KVISRQNLQSPKSSRSTILVKLDTNGAQELHYQPGDHVGIFPANRPELVDALLDRLHDAPPPDQVIKLEV
LEERSTALGIIKTWTPHERLPPCTLRQALTRYLDITTPPTPQLLQLLATLATDEKDKERLEVLGKGSSEY
EDWKWYKNPNILEVLEEFPSLQVPASLLLTQLPLLQPRYYSISSSPDMYPGEIHLTVAVVSYRTRDGQGP
VHHGVCSTWLNGLTPGDTVPCFVRSAPSFHLPEDPSVPVIMVGPGTGIAPFRSFWQQRQYDLRMSEDPGK
KFGDMTLFFGCRNSTIDDIYKEETEEAKNKGVLTEVYTALSREPGKPKTYVQDLLKEQAESVYDALVREG
GHIYVCGDVTMAEDVSQTIQRILAEHGNMSAEEAEEFILKLRDENRYHEDIFGVTL
>gnl|CDD|99800 cd06203, methionine_synthase_red, Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for the regeneration of methionine from homocysteine, as well as the coversion of methyltetrahydrofolate to tetrahydrofolate. In MSR, electrons are transferred from NADPH to FAD to FMN to cob(II)alamin. MSR resembles proteins of the cytochrome p450 family including nitric oxide synthase, the alpha subunit of sulfite reductase, but contains an extended hinge region. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPORs resemble ferredoxin reductase (FNR) but have a connecting subdomain inserted within the flavin binding region, which helps orient the FMN binding doamin with the FNR module. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH
PISSAKKLTEGDDVKTVVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVV
PNTKKKNAKVPVHIPKVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDF
VRKRGLSLLDLLEAFPSCRPPLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPAKGLCTSWLE
SLCLSASSHGVKVPFYLRSSSRFRLPPDDLRRPIIMVGPGTGVAPFLGFLQHREKLKESHTETVFGEAWL
FFGCRHRDRDYLFRDELEEFLEEGILTRLIVAFSRDENDGSTPKYVQDKLEERGKKLVDLLLNSNAKIYV
CGDAKGMAKDVRDTFVDILSKELGLDKLEAKKLLARLRKEDRYLEDVW
>gnl|CDD|99801 cd06204, CYPOR, NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH
DAKNPFLAPVAVSRELFTGSDRSCLHIEFDISGSGIRYQTGDHLAVWPTNPSEEVERLLKVLGLDDRDTV
ISLKSLDEPASKKVPFPCPTTYRTALRHYLDITAPVSRQVLAALAQFAPDPEEKERLLKLASEGKDEYAK
WIVEPHRNLLEVLQDFPSAKPTPPPFDFLIELLPRLQPRYYSISSSSKVHPNRIHITAVVVKYPTPTGRI
IKGVATNWLLALKPALNGEKPPTPYYLSGPRKKGGGSKVPVFVRRSNFRLPTKPSTPVIMIGPGTGVAPF
RGFIQERAALKESGKKVGPTLLFFGCRHPDEDFIYKDELEEYAKLGGLLELVTAFSREQPKKVYVQHRLA
EHAEQVWELINEGAYIYVCGDAKNMARDVEKTLLEILAEQGGMTETEAEEYVKKLKTRGRYQEDVW
>gnl|CDD|99802 cd06206, bifunctional_CYPOR, These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase (CYPOR). NADPH cytochrome p450 reductase serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH
TVVENRELTAPGVGPSKRHLELRLPDGMTYRAGDYLAVLPRNPPELVRRALRRFGLAWDTVLTISASGSA
TGLPLGTPISVSELLSSYVELSQPATRRQLAALAEATRCPDTKALLERLAGEAYAAEVLAKRVSVLDLLE
RFPSIALPLATFLAMLPPMRPRQYSISSSPLVDPGHATLTVSVLDAPALSGQGRYRGVASSYLSSLRPGD
SIHVSVRPSHSAFRPPSDPSTPLIMIAAGTGLAPFRGFLQERAALLAQGRKLAPALLFFGCRHPDHDDLY
RDELEEWEAAGVVSVRRAYSRPPGGGCRYVQDRLWAEREEVWELWEQGARVYVCGDGRMAPGVREVLKRI
YAEKDERGGGSDDEEAEEWLEELRNKGRYATDVF
>gnl|CDD|99803 cd06207, CyPoR_like, NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH
KVTENKRLTPADYDRSTRHIEFDLGGSGLSYETGDNLGIYPENSDALVDEFLARLGLDGDDVVRVEPNEQ
QRGKPPFPEPISVRQLLKKFLDIFGKPTKKFLKLLSQLATDEEEKEDLYKLASREGRTEYKRYEKYTYLE
VLKDFPSVRPTLEQLLELCPLIKPRYYSISSSPLKNPNEVHLLVSLVSWKTPSGRSRYGLCSSYLAGLKV
GQRVTVFIKKSSFKLPKDPKKPIIMVGPGTGLAPFRAFLQERAALLAQGPEIGPVLLYFGCRHEDKDYLY
KEELEEYEKSGVLTTLGTAFSRDQPKKVYVQDLIRENSDLVYQLLEEGAGVIYVCGSTWKMPPDVQEAFE
EILKKHGGGDEELAEKKIEELEERGRYVVEAW
>gnl|CDD|99804 cd06208, CYPOR_like_FNR, These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but lack the FAD-binding region connecting sub-domain. Ferredoxin-NADP+ reductase (FNR) is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins, such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2, which then transfers two electrons and a proton to NADP+ to form NADPH. CYPOR serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases, sulfite reducatase, and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal FNR-like FAD and NAD binding module, an FMN-binding domain, and an additional connecting domain (inserted within the FAD binding region) that orients the FNR and FMN -binding domains. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH
NLYKPKNPLIGKVVSNTRLTGPDAPGEVCHIVIDHGGKLPYLEGQSIGIIPPGTDAKNGKPHKLRLYSIA
SSRYGDDGDGKTLSLCVKRLVYTDPETDETKKGVCSNYLCDLKPGDDVQITGPVGKTMLLPEDPNATLIM
IATGTGIAPFRSFLRRLFREKHADYKFTGLAWLFFGVPNSDSLLYDDELEKYPKQYPDNFRIDYAFSREQ
KNADGGKMYVQDRIAEYAEEIWNLLDKDNTHVYICGLKGMEPGVDDALTSVAEGGLAWEEFWESLKKKGR
WHVEVY
>gnl|CDD|99805 cd06209, BenDO_FAD_NAD, Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group
TFEATVTEVERLSDSTIGLTLELDEAGALAFLPGQYVNLQVPGTDETRSYSFSSAPGDPRLEFLIRLLPG
GAMSSYLRDRAQPGDRLTLTGPLGSFYLREVKRPLLMLAGGTGLAPFLSMLDVLAEDGSAHPVHLVYGVT
RDADLVELDRLEALAERLPGFSFRTVVADPDSWHPRKGYVTDHLEAEDLNDGDVDVYLCGPPPMVDAVRS
WLDEQGIEPANFYYEKFT
>gnl|CDD|99806 cd06210, MMO_FAD_NAD_binding, Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water
VREAEIVAVDRVSSNVVRLRLQPDDAEGAGIAAEFVPGQFVEIEIPGTDTRRSYSLANTPNWDGRLEFLI
RLLPGGAFSTYLETRAKVGQRLNLRGPLGAFGLRENGLRPRWFVAGGTGLAPLLSMLRRMAEWGEPQEAR
LFFGVNTEAELFYLDELKRLADSLPNLTVRICVWRPGGEWEGYRGTVVDALREDLASSDAKPDIYLCGPP
GMVDAAFAAAREAGVPDEQVYLEKFL
>gnl|CDD|99807 cd06211, phenol_2-monooxygenase_like, Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases
LLNVKDFEGTVVEIEDLTPTIKGVRLKLDEPEEIEFQAGQYVNLQAPGYEGTRAFSIASSPSDAGEIELH
IRLVPGGIATTYVHKQLKEGDELEISGPYGDFFVRDSDQRPIIFIAGGSGLSSPRSMILDLLERGDTRKI
TLFFGARTRAELYYLDEFEALEKDHPNFKYVPALSREPPESNWKGFTGFVHDAAKKHFKNDFRGHKAYLC
GPPPMIDACIKTLMQGRLFERDIYYEKF
>gnl|CDD|99808 cd06212, monooxygenase_like, The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate
FVGTVVAVEALTHDIRRLRLRLEEPEPIKFFAGQYVDITVPGTEETRSFSMANTPADPGRLEFIIKKYPG
GLFSSFLDDGLAVGDPVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGA
RTARDLFYLEEIAALGEKIPDFTFIPALSESPDDEGWSGETGLVTEVVQRNEATLAGCDVYLCGPPPMID
AALPVLEMSGVPPDQIFYDKFT
>gnl|CDD|99809 cd06213, oxygenase_e_transfer_subunit, The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate while mono-oxygenases add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate
IRGTIVAQERLTHDIVRLTVQLDRPIAYKAGQYAELTLPGLPAARSYSFANAPQGDGQLSFHIRKVPGGA
FSGWLFGADRTGERLTVRGPFGDFWLRPGDAPILCIAGGSGLAPILAILEQARAAGTKRDVTLLFGARTQ
RDLYALDEIAAIAARWRGRFRFIPVLSEEPADSSWKGARGLVTEHIAEVLLAATEAYLCGPPAMIDAAIA
VLRALGIAREHIHADRF
>gnl|CDD|99810 cd06214, PA_degradation_oxidoreductase_like, NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation oxidoreductase. PA oxidoreductases of E. coli hydroxylate PA-CoA in the second step of PA degradation. Members of this group typically fuse a ferredoxin reductase-like domain with an iron-sulfur binding cluster domain. Ferredoxins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal portion may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH
FHPLTVAEVVRETADAVSITFDVPEELRDAFRYRPGQFLTLRVPIDGEEVRRSYSICSSPGDDELRITVK
RVPGGRFSNWANDELKAGDTLEVMPPAGRFTLPPLPGARHYVLFAAGSGITPVLSILKTALAREPASRVT
LVYGNRTEASVIFREELADLKARYPDRLTVIHVLSREQGDPDLLRGRLDAAKLNALLKNLLDATEFDEAF
LCGPEPMMDAVEAALLELGVPAERIHRELFT
>gnl|CDD|99811 cd06215, FNR_iron_sulfur_binding_1, Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH
LRCVKIIQETPDVKTFRFAAPDGSLFAYKPGQFLTLELEIDGETVYRAYTLSSSPSRPDSLSITVKRVPG
GLVSNWLHDNLKVGDELWASGPAGEFTLIDHPADKLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSA
RSPADIIFADELEELARRHPNFRLHLILEQPAPGAWGGYRGRLNAELLALLVPDLKERTVFVCGPAGFMK
AVKSLLAELGFPMSRFHQESF
>gnl|CDD|99812 cd06216, FNR_iron_sulfur_binding_2, Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH
FVDFYLELINPLWSARELRARVVAVRPETADMVTLTLRPNRGWPGHRAGQHVRLGVEIDGVRHWRSYSLS
SSPTQEDGTITLTVKAQPDGLVSNWLVNHLAPGDVVELSQPQGDFVLPDPLPPRLLLIAAGSGITPVMSM
LRTLLARGPTADVVLLYYARTREDVIFADELRALAAQHPNLRLHLLYTREELDGRLSAAHLDAVVPDLAD
RQVYACGPPGFLDAAEELLEAAGLADRLHTERF
>gnl|CDD|99813 cd06217, FNR_iron_sulfur_binding_3, Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH
WRVLRVTEIIQETPTVKTFRLAVPDGVPPPFLAGQHVDLRLTAIDGYTAQRSYSIASSPTQRGRVELTVK
RVPGGEVSPYLHDEVKVGDLLEVRGPIGTFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVPFRL
LYSARTAEDVIFRDELEQLARRHPNLHVTEALTRAAPADWLGPAGRITADLIAELVPPLAGRRVYVCGPP
AFVEAATRLLLELGVPRDRIRTEAF
>gnl|CDD|99814 cd06218, DHOD_e_trans, FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster
VLSNREIADDIYRLVLEAPEIAAAAKPGQFVMLRVPDGSDPLLRRPISIHDVDPEEGTITLLYKVVGKGT
RLLSELKAGDELDVLGPLGNGFDLPDDDGKVLLVGGGIGIAPLLFLAKQLAERGIKVTVLLGFRSADDLF
LVEEFEALGAEVYVATDDGSAGTKGFVTDLLKELLAEARPDVVYACGPEPMLKAVAELAAERGVPCQVSL
EERMACGIGACLGCVVKTKDDEGGYKRVCKDGPVFD
>gnl|CDD|99815 cd06219, DHOD_e_trans_like1, FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD, forming FADH2 via a semiquinone intermediate, and then transfers a hydride ion to convert NADP+ to NADPH
YKILEKEELAPNVKLFEIEAPLIAKKAKPGQFVIVRADEKGERIPLTIADWDPEKGTITIVVQVVGKSTR
ELATLEEGDKIHDVVGPLGKPSEIENYGTVVFVGGGVGIAPIYPIAKALKEAGNRVITIIGARTKDLVIL
EDEFRAVSDELIITTDDGSYGEKGFVTDPLKELIESGEKVDLVIAIGPPIMMKAVSELTRPYGIPTVVSL
NPIMVDGTGMCGACRVTVGGETKFACVDGPEFDAHKVD
>gnl|CDD|99816 cd06220, DHOD_e_trans_like2, FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster
VTIKEVIDETPTVKTFVFDWDFDFKPGQFVMVWVPGVDEIPMSLSYIDGPNSITVKKVGEATSALHDLKE
GDKLGIRGPYGNGFELVGGKVLLIGGGIGIAPLAPLAERLKKAADVTVLLGARTKEELLFLDRLRKSDEL
IVTTDDGSYGFKGFVTDLLKELDLEEYDAIYVCGPEIMMYKVLEILDERGVRAQFSLERYMKCGIGICGS
CCIDPTGLRVCRDGPVFDGEQLK
>gnl|CDD|99817 cd06221, sulfite_reductase_like, Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+
IVEVVDETEDIKTFTLRLEDDDEELFTFKPGQFVMLSLPGVGEAPISISSDPTRRGPLELTIRRVGRVTE
ALHELKPGDTVGLRGPFGNGFPVEEMKGKDLLLVAGGLGLAPLRSLINYILDNREDYGKVTLLYGARTPE
DLLFKEELKEWAKRSDVEVILTVDRAEEGWTGNVGLVTDLLPELTLDPDNTVAIVCGPPIMMRFVAKELL
KLGVPEEQIWVSLERRMKCGVGKCGHCQIGPKYVCKDGPVFSY
>gnl|CDD|259998 cd06222, RNase_H_like, Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of spliceosomal protein Prp8. Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication. RNase H inhibitors have been explored as anti-HIV drug targets since RNase H inactivation inhibits reverse transcription. This model also includes the Prp8 domain IV, which adopts the RNase fold but shows low sequence homology; domain IV is implicated in key spliceosomal interactions
INVDGSCRGNPGPAGIGGVLRDHEGGWLGGFALKIGAPTALEAELLALLLALELALDLGYLKVIIESDSK
YVVDLINSGSFKWSPNILLIEDILLLLSRFWSVKISHVPREGNQVADALAK
>gnl|CDD|206754 cd06223, PRTases_typeI, Phosphoribosyl transferase (PRT)-type I domain. Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22
AGRLLAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLELPLGGDVK
GKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGDPVYSLFT
>gnl|CDD|100121 cd06224, REM, Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also called REM domain (Ras exchanger motif). This domain is common in nucleotide exchange factors for Ras-like small GTPases and is typically found immediately N-terminal to the RasGef (Cdc25-like) domain. REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyrosine-kinase mediated signalling to Ras, RasGRP1-4, RasGRF1,2, CNrasGEF, and RAP-specific nucleotide exchange factors, to name a few
TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAPPENLEYNDWDKKKSKPIRLRV
LNVLRTWVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKLLRKLLKL
>gnl|CDD|381743 cd06225, HAMP, Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established
TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL
>gnl|CDD|349445 cd06226, M14_CPT_like, Peptidase M14-like domain of an uncharacterized group of Peptidase M14 Carboxypeptidase T (CPT)-like proteins. Peptidase M14-like domain of an uncharacterized group of Peptidase M14 Carboxypeptidase T (CPT)-like proteins. This group belongs to the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPT exhibits dual-substrate specificity by cleaving C-terminal hydrophobic amino acid residues and C-terminal positively charged residues. However, CPT does not belong to this CPT-like group
DIRALKLTNKQATPPGEKPKFFMMAAIHAREYTTAELVARFAEDLVAGYGTDADATWLLDYTELHLVPQV
NPDGRKIAETGLLWRKNTNTTPCPASSPTYGVDLNRNSSFKWGGAGAGGSACSETYRGPSAASEPETQAI
ENYVKQLFPDQRGPGLTDPAPDDTSGIYIDIHSYGNLVLYPWGWTGTPAPNAAGLRTLGRKFAYFNGYTP
QQAVALYPTDGTTDDFAYGTLGVAAYTFELGTAFFESCSYFENTILPDNLPALYYAA
>gnl|CDD|349446 cd06227, M14-CPA-like, Peptidase M14 carboxypeptidase A-like domain; uncharacterized subfamily. A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
KPRVLLVFGEHARELISVESALRLLRQLCGGLQEPAASALRELAREILDNVELKIIPNANPDGRRLVESG
DYCWRGNENGVDLNRNWGVDWGKGEKGAPSEEYPGPKPFSEPETRALRDLALSFKPHAFVSVHSGMLAIY
TPYAYSASVPRPNRAADMDDLLDVVAKASCGDCTVGSAGKLVGYLADGTAMDYMYGKLKVPYSFTFEIYG
DSGKARCFDCFNPF
>gnl|CDD|349447 cd06228, M14-like, Peptidase M14-like domain; uncharacterized subfamily. A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
PGVYFIGGVHAREWGSPDILIYFAADLLEAYTNNTGLTYGGKTFTAAQVKSILENVDLVVFPLVNPDGRW
YSQTSESMWRKNRNPASAGDGGSCIGVDINRNFDFLWDFPRYFDPGRVPASTSPCSETYHGPSAFSEPET
RNVVWLFDAYPNIRWFVDVHSASELILYSWGDDENQSTDPAMNFLNPAYDGKRGIAGDTRYREFIPSDDR
TIAVNLANRMALAIAAVRGRVYTVQQAFGLYPTSGASDDYAYSRHFVNPAKRKVYGFTIEWGTEFQPAYS
EMENIIRDVSAGLV
>gnl|CDD|349448 cd06229, M14_Endopeptidase_I, Peptidase M14 carboxypeptidase family-like domain of Endopeptidase I. Peptidase M14-like domain of Gamma-D-glutamyl-L-diamino acid endopeptidase 1 (also known as Gamma-D-glutamyl-meso-diaminopimelate peptidase I, and Endopeptidase I (ENP1); EC 3.4.19.11). ENP1 is a member of the M14 family of metallocarboxypeptidases (MCPs), and is classified as belonging to subfamily C. However it has an exceptional type of activity of hydrolyzing the gamma-D-Glu-(L)meso-diaminopimelic acid (gamma-D-Glu-Dap) bond of L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid and L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid(L)-D-Ala peptides. ENP1 has a different substrate specificity and cellular role than MpaA (MpaA does not belong to this group). ENP1 hydrolyzes the gamma-D-Glu-Dap bond of MurNAc-tripeptide and MurNAc-tetrapeptide, as well as the amide bond of free tripeptide and tetrapeptide. ENP1 is active on spore cortex peptidoglycan, and is produced at stage IV of sporulation in forespore and spore integuments
VLYNASFHAREYITTLLLMKFIEDYAKAYVNKSYIRGKDVGELLNKVTLHIVPMVNPDGVEISQNGSNAI
NPYYLRLVAWNKKGTDFTGWKANIRGVDLNRNFPAGWEKEKRLGPKAPGPRDYPGKEPLSEPETKAMAAL
TRQNDFDLVLAYHSQGEEIYWGYNGLEPEESKAMAEKFASVSGYEPVEAEAIDSYGGFKDWFIYEFKKPS
FTIETGKGNNPLPISQFDEIYEKNKGVL
>gnl|CDD|349449 cd06230, M14_ASTE_ASPA_like, Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily. The Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily belongs to the M14 family of metallocarboxypeptidases (MCPs), and includes ASTE, which catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) which cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD
LLILAGVHGDEYEGVEAIRRLLAELDPSELKGTVVLVPVANPPAFEAGTRYTPLDGLDLNRIFPGDPDGS
PTERLAHELTELILKHADALIDLHSGGTGRLVPYAILDYDSDAREKSRELARAFGGTPVIWGGDPPGGTP
VAAARSAGIPAITVELGGGGRLRAERLERYLRGIRNV
>gnl|CDD|349450 cd06231, M14_REP34-like, Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34). This family includes Francisella tularensis protein rapid encystment phenotype 34 (REP34) which is a zinc-containing monomeric protein demonstrating carboxypeptidase B-like activity. REP34 possesses a novel topology with its substrate binding pocket deviating from the canonical M14 peptidases with a possible catalytic role for a conserved tyrosine and distinct S1' recognition site. Thus, REP34, identified as an active carboxypeptidase and a potential key F. tularensis effector protein, may help elucidate a mechanistic understanding of F. tularensis infection of phagocytic cells. A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
SYLRDVAERLGARRFKVRELGEVGYQGYPLFALKSPNPRGDKPRVLISAGIHGDEPAGVEALLRFLESLA
EKYLRRVNLLVLPCVNPWGFERNTRENADGIDLNRSFLKDSPSPEVRALMEFLASLGRFDLHLDLHEDWD
SDGFYLYELGPALKAGRDGLQAVDAVIPPDPISLTIDGSPAPDGVILRPDDPAERPGWPFAIYLVANGAV
RTYTTETPSDFPLERRVAAHLAAIRTALE
>gnl|CDD|349451 cd06232, M14-like, Peptidase M14-like domain; uncharacterized subfamily. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
YEARSYQGRDIWAREFTEPSTSEFVSQAKLSLYKPTILISARHHANEVSSTNAALRLAELLATDPPEILK
KVNLVIIPLENPDGYALHEELQKDNPEHKLHAARYNALGDEYAYEYFNDDPRFPEAEVRPRAWERWLPDI
HVDLHGYPSHEWVQPFSGYAPRGFRSYWLPRGLFYGYFPYLDDEAYPGGELAEELAEAITKALNQDPALA
AFNRRWYDRYRKYAVKWGPKVFPLEYYKPVLIYWSIFRQHRYLSARYPQITPVELITEVADETAYG
>gnl|CDD|349452 cd06233, M14-like, Peptidase M14-like domain; uncharacterized subfamily. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
LVITSGTHGVEGFAGSAIQLAFLEELLPSLLPADTGVLLVHALNPYGMAHLRRVNENNVDLNRNFLVDFS
APLPNNPGYDELDPLLNPRSPPSLALLSFLLKLLKLIAKHGMAALKQALLGGQYEHPDGLFYGGRAPEWS
RRTLREILREHLAGARKVVHIDLHTGLGPRGKLTLIFSSPDDSARARLEEWFGGEVVDWGGDDADFYAVT
GDLTDYLGKLALPDAEVLGVTLEFGTLPSIAVLRALRAE
>gnl|CDD|349453 cd06234, M14_PaCCP-like, Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases similar to Pseudomonas aerugnosa CCP (PaCCP). A bacterial subgroup of the Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP)-like proteins. This subgroup includes PaCCP from Pseudomonas aeruginosa, a carboxypeptidase homologous to M14D subfamily of human CCPs. Structural complexes with well-known inhibitors of metallocarboxypeptidases indicate that PaCCP might only possess C-terminal hydrolase activity against cellular substrates of particular specificity. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins (such as alpha-tubulin in eukaryotes) to remove a C-terminal tyrosine. Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain
YSYERHLDLVARAQASPGVRLEVLGQTLDGRDIDLLTIGDPGTGKKKVWIIARQHPGETMAEWFMEGLLD
RLLDEDDPVSRALLEKAVFYVVPNMNPDGSVRGNLRTNAAGVNLNREWANPSLERSPEVFAVRQAMDATG
VDFFLDVHGDEALPYNFIAGAEGIPSWTPRLAALEAAFKAALAAASPDFQTEHGYPPDAPGEANLTIASN
WVAERFGCLAMTLEMPFKDNANNPDPGTGWSPERSKRLGASVLDAL
>gnl|CDD|349454 cd06235, M14_AGTPBP-like, Peptidase M14-like domain of human Nna1/AGTPBP-1, AGBL2 -5, and related proteins. Subgroup of the Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP), and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This eukaryotic subgroup includes the human Nna1/AGTPBP-1 and AGBL -2, -3, -4, and -5, and the mouse Nna1/CCP-1 and CCP -2 through -6. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Nna1 is widely expressed in the developing and adult nervous systems, including cerebellar Purkinje and granule neurons, miral cells of the olfactory bulb and retinal photoreceptors. Nna1 is also induced in axotomized motor neurons. Mutations in Nna1 cause Purkinje cell degeneration (pcd). The Nna1 CP domain is required to prevent the retinal photoreceptor loss and cerebellar ataxia phenotypes of pcd mice, and a functional zinc-binding domain is needed for Nna-1 to support neuron survival in these mice. Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain
IYFEREVLCHSLDGRKLDLLTITSPNNKKLGPYPREFAGKKVVFLSGRVHPGETPASFVMKGFLDFLLSN
DPRAQLLREHFVFKIVPMLNPDGVIRGNYRCSLNGFNLNRHYKNPDPELHPTIYGAKKVIDYLQKTYKRR
VLMYCDFHGHSSKSNGFMYGNSFPDTVQFHWNMVFPKILSLNAPDFFSSSCCSFGVMKSKEGTGRVVFGR
RLIHSHSYTLESTFFSNNRGNIDGACGYTEENLEDLGYSVASTLLD
>gnl|CDD|349455 cd06236, M14_AGBL5_like, Peptidase M14-like domain of ATP/GTP binding protein (AGBL)-5 and related proteins. Peptidase M14-like domain of ATP/GTP binding protein_like (AGBL)-5, and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This eukaryotic subgroup includes the human AGBL5 and the mouse cytosolic carboxypeptidase (CCP)-5. ATP/GTP binding protein (AGTPBP-1/Nna1)-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Mutations in AGTPBP-1/Nna1 cause Purkinje cell degeneration (pcd). AGTPBP-1/Nna1 however does not belong to this subgroup. AGTPBP-1/Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain
KSPESDIYYHRELLCYSLEGRRVDLLTITSCHGVTEEREERLPNLFPDTSKPRPHKFEGKKVVFISARVH
PGETPSSFVFNGFLEFLLRPDDPRAIALRRLFVFKLIPMLNPDGVARGHYRTDTRGVNLNRVYLNPDPEL
HPSIYAAKALLFYIDLHAHASKRGCFIYGNALEDEEQQVENLLYPKLISLNSAHFDFDACNFSEKNMYSR
DKRDGLSKEGSGRVALYKATGIVHSYTLECNYHFEDVGRALAVALLDMLGCNP
>gnl|CDD|349456 cd06237, M14_Nna1-like, Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; uncharacterized bacterial subgroup. A bacterial subgroup of the Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP),-like proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins (such as alpha-tubulin in eukaryotes) to remove a C-terminal tyrosine. Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain
ADYDAWIDSLAKKPFVKRSTIGKSVEGRPIEALTIGNPDSKELVVLLGRQHPPEVTGALAMQAFVETLLA
DTELAKAFRARFRVLVVPLLNPDGVDLGHWRHNAGGVDLNRDWGPFTQPETRAVRDFLLELVEEPGGKVV
FGLDFHSTWEDVFYTQPDDEKTNPPGFTPDWLAAIEERLPGYEVNIKPSHNPGRPTSKNWFYDTFGAPAV
TYEVGDETPRDLIRRKARVAAEELMELLL
>gnl|CDD|349457 cd06238, M14-like, Peptidase M14-like domain; uncharacterized subgroup. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
PAILWMGYSIHGNELSGSEAAMQVAYHLAAGQDEATRALLENTVIVIDPNQNPDGRERFVNWFNQNRGAV
GDPDPQSMEHNEPWPGGRTNHYLFDLNRDWLAQTQPESRARAAAIHRWRPQVVVDFHEMGTDQTFFFPPP
AEPVNPLIPRQQLRWTKRFGSDHAAAFDSYGWSYFTREVFDLFYPGYGDSYPSYLGAIGMLYEQGSSRGL
AQERTDG
>gnl|CDD|349458 cd06239, M14-like, Peptidase M14-like domain; uncharacterized subgroup. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
KVLLWSQMHGNEPTGTEALLDLISYLRRERQEFEKILERLTLVAIPMLNPDGAELFTRHNAEGIDLNRDA
RALQTPESRALKAVLDSFSPKFAFNLHDQRSIFGVGGTGKPASLSLLAPAADEEREDNPSREKARKLIAS
ILEELEKIIPGQVARFDDSFYPRAFGDWFQELGIPTILIETGAYPNDYSRERVR
>gnl|CDD|349459 cd06240, M14-like, Peptidase M14-like domain; uncharacterized subgroup. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
KAVVWIDGGLHATEVAGSQMLPELAYRLATSDDEEVRRILDNVILLLVPSANPDGQDLVVDWYMRYKDTP
KEGSRLPWLYQKYVGHDNNRDWYMLNMQETRNVARVLYEEWFPQVLYDHHQTGPAGPRIFVPPFRDPINP
NIDPLVIRGSNALGAAMATRLAAEGKPGVISNAVYDTWWPGYLRTTAYFHNIIGILTEIAGNATPSPIPF
VP
>gnl|CDD|349460 cd06241, M14-like, Peptidase M14-like domain; uncharacterized subgroup. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
KPVVLIQAGIHPGEVEGKEASLMLLRDIAQGGKKHLLDNLILLFVPIFNADGNDRRSKGNRPNQNGPLEV
GWRTNAQGLDLNRDFMKLEAPETRALAKLFNQWDPDLFIDTHTTDGSDHQYDLTYAFSQNPAGDPGLSAY
VRDVFLPAVSAALERKGHLPLPGIDGNDGGDPSKGWYTYTHHPRYSTGYGGLRNRMSILVETYSLKPFKQ
RVLAT
>gnl|CDD|349461 cd06242, M14-like, Peptidase M14-like domain; uncharacterized subgroup. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
KPTVLLVGQQHGNEPAGREAALALARDLAFGDDARELLEKVNVLVVPRANPDGRAANTRGNANGVDLNRD
HLLLSTPETRALARVLRDYRPEVVIDAHEFGGVTGDFTLARYDVLWPRATNLNIDPGLRALSRELVLDEV
EKALEAAGFRSDPYGTTITNPVGRIIHNGLTLRILRNAAGLRNAVSFLIESRLGIGLGRENFRRRVASQL
LALRSFLRTA
>gnl|CDD|349462 cd06243, M14_CP_Csd4-like, Peptidase M14 carboxypeptidase Csd4 and similar proteins. This family includes peptidase M14 carboxypeptidase Csd4 from H. pylori which has been shown to be DL-carboxypeptidase with a modified zinc binding site containing a glutamine residue in place of a conserved histidine. It is an archetype of a new carboxypeptidase subfamily with a domain arrangement that differs from this family of peptide-cleaving enzymes. Csd4 plays a role in trimming uncrosslinked peptidoglycan peptide chains by cleaving the amide bond between meso-diaminopimelate and iso-D-glutamic acid in truncated peptidoglycan side chains. It acts as a cell shape determinant, similar to Campylobacter jejuni Pgp1. The M14 family of metallocarboxypeptidases (MCPs), also known as funnelins, are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
EDIEKPFTRLEGREPGPTLLIIGGIQGDEPGGFLAADLLADLYLVKGNVIVVPRLNFPSILRNHRGLNGD
MNRKFAALDKKDPEYKTIQEIKSLIADFRPDVVLHLHDGSGFYRPNYVDAMRNPKRWGQSIIIDQDRYKT
AKFINLLAIAKNVIERINAHILDPKYKYHLKNTRTFSGDSDHKEMRKALTFYALKQKKPAFAIEASKSLP
LAEKIYYHLQAIEGFLN
>gnl|CDD|349463 cd06244, M14-like, Peptidase M14-like domain; uncharacterized subgroup. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
VPIVYNNIHGNEVEGVDALLEFLEMLATEPNVTYNTLVKYYKVENVDLEVKDLLDDVFFIVVPTENPDGR
VANTRTNANGFDLNRDNAYQTQPETRAMQELISKWNPVTFLDMHGYVEGFLIEPCTPPHNPNFEYDLIAK
NMLAQGEAMGRAAIANNKLYNSYEIPARDYLKKDPGGPSWKEGWDDMSPAYTPMYAMLHGAIGHTVEVPA
LNEDTTDAMVYAA
>gnl|CDD|349464 cd06245, M14_CPD_III, Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain III subgroup. The third carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; EC 3.4.17.22), domain III. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans-Golgi network and immature secretory vesicles, but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans-Golgi network, such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down -regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop
YHSYKQLSKFLRGLNSNYPTITNLTSLGQSVEKRDIWVLEIGNKPNESEPSEPKILFVGGIHGNAPVGTE
LLLLLAHFLCHNYKKDSAITKLLNRTRIHIVPSLNPDGAEKAEEKKCTSKIGEKNANGVDLDTDFESNAN
NRSGAAQPETKAIMDWLKEKDFTLSVALDGGSLVVTYPYDKPVQTVENKETLKHLAKVYANNHPTMHAGD
PGCCSNSDENFTNGVIRASEWHSHKGSMLDFSYKFGSCPEITVYTSCCYFPPAEELLTLWAEHKKSLLSM
IVE
>gnl|CDD|349465 cd06246, M14_CPB2, Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase B2 subgroup. Peptidase M14 Carboxypeptidase (CP) B2 (CPB2, also known as plasma carboxypeptidase B, carboxypeptidase U, and CPU), belongs to the carboxpeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPB2 enzyme displays B-like activity; it only cleaves the basic residues lysine or arginine. It is produced and secreted by the liver as the inactive precursor, procarboxypeptidase U or PCPB2, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). It circulates in plasma as a zymogen bound to plasminogen, and the active enzyme, TAFIa, inhibits fibrinolysis. It is highly regulated, increased TAFI concentrations are thought to increase the risk of thrombosis and coronary artery disease by reducing fibrinolytic activity while low TAFI levels have been correlated with chronic liver disease
YYEQYHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSGKEQTAKNAIWIDCGIHAREWISP
AFCLWFIGHASYFYGIIGQHTNLLNLVDFYVMPVVNVDGYDYSWKKNRMWRKNRSKHANNRCIGTDLNRN
FDAGWCGKGASSDSCSETYCGPYPESEPEVKAVASFLRRHKDTIKAYISMHSYSQMVLFPYSYTRNKSKD
HDELSLLAKEAVTAIRKTSRNRYTYGPGAETIYLAPGGSDDWAYDLGIKYSFTFELRDRGTYGFLLPPSY
IKPTCNEALLAVKKIALHVI
>gnl|CDD|349466 cd06247, M14_CPO, Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase O subgroup. Peptidase M14 carboxypeptidase (CP) O (CPO, also known as metallocarboxypeptidase C; EC 3.4.17.) belongs to the carboxypeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPO has not been well characterized as yet, and little is known about it. Based on modeling studies, CPO has been suggested to have specificity for acidic residues rather than aliphatic/aromatic residues as in A-like enzymes or basic residues as in B-like enzymes. It remains to be demonstrated that CPO is functional as an MCP
YTKYHPMDEIYQWMDQMQEKNSEVVSQHYLGQTYEKRPMYYLKIGWPSDKPKKIIWMDCGIHAREWIAPA
FCQWFVKEILQNYKTDSRLNKLLKNLDFYVLPVLNIDGYIYSWTTDRLWRKSRSPHNNGTCYGTDLNRNF
NSQWCSIGASRNCCSIIFCGTGPESEPETKAVADLIEKKKSDILCYLTIHSYGQLILLPYGYTKEPSPNH
EEMMEVGEKAAAALKEKHGTSYRVGSSADILYSNSGSSRDWARDIGIPFSYTFELRDTGTYGFVLPEDQI
QPTCEETMEAVMSIIEYV
>gnl|CDD|349467 cd06248, M14_CP_insect, Peptidase M14 carboxypeptidase subfamily A/B-like. This family includes peptidase M14 carboxypeptidases found specifically in insects, including B-type carboxypeptidase of H. zea (CPBHz, insect gut carboxypeptidase-3) that is insensitive to potato carboxypeptidase inhibitor (PCI) in corn earworm, and midgut procarboxypeptidase A (PCPAHa, insect gut carboxypeptidase-1) from Helicoverpa armigera larva, a devastating pest of crops. PCPAHa preferentially cleaves aliphatic and aromatic residues. The peptidase M14 Carboxypeptidase (CP) A/B subfamily is one of two main M14 CP subfamilies defined by sequence and structural homology, the other being the N/E subfamily. CPs hydrolyze single, C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1, CPA2, CPA3, CPA4, CPA5, CPA6, CPB, CPO and CPU. CPA1, CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 is detected in hormone-regulated tissues, and is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues, and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle, suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor, PCPU, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues
YHSLDEIDEYLDGLAEESPDVVTVVEGGYTFEGRPIKYVRIRSTNSEDTSKPTIMIEGGINPREWISPPA
ALYAIHKLVEDVETQSDLLNNFDWIILPVANPDGYVFTHTNDREWTKNRSTNSNPLGQICFGVNINRNFD
YQWNPVLSSESPCSELYAGPSAFSEAESRAIRDILHEHGNRIHLYISFHSGGSFILYPWGYDGSTSSNAR
QLHLAGVAAAAAISSNNGRPYVVGQSSVLLYRAAGTSSDYAMGIAGIDYTYELPGYSSGDPFYVPPAYIE
QVVREAWEGIVVGARAA
>gnl|CDD|349468 cd06250, M14_PaAOTO_like, Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like subfamily; subgroup includes Pseudomonas aeruginosa AotO. An uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the the M14 family of metallocarboxypeptidases. This subgroup includes Pseudomonas aeruginosa AotO and related proteins. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD. The gene encoding P. aeruginosa AotO was characterized as part of an operon encoding an arginine and ornithine transport system, however it is not essential for arginine and ornithine uptake
ERIPLDSPAPGTERSLTVFRFGGAGAGPKVYIQAALHADELPGNLVIHHLLERLKALEAAGRIKGEIVLV
PQANPIGLSQKIGGYHQGRFDLATGDNFNRNFPDLAKAVAARVEERLGDDAAANVALIRAALKEALDALP
PRTELQRLKLTLLRLALDADIVLDLHCDDEALRHLYTPPALWPAAEDLAAALGAPAVLLADNSGGGAFDE
AFSKPWLRLAEAFPGAPIPLACFSATVELRGQADVDDELARADAEGILRFLAARGVI
>gnl|CDD|349469 cd06251, M14_ASTE_ASPA-like, Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup. A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD
VPVLVARGAKPGPTLLLTAAIHGDELNGIEVIQRLLEDLDPSKLRGTLIAIPVVNPLGFENNSRYLPDDG
RDLNRSFPGSEKGSLASRLAHLLWNEIVKKADYVIDLHTASTGRTNLPYVRADLRDPESRRMAEAFGAPV
IVDDPGEDGSLRGAAVELGIPAITVELGEALRFDEDIIRRGVEGVLNVLRHLGML
>gnl|CDD|349470 cd06252, M14_ASTE_ASPA-like, Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup. A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD
PGKQAGFLRLPLSDDRSAWGAIPIPITVINNGSGPTVLLTGGNHGDEYEGPIALRRLARDLDPEDVRGRL
IIVPALNLPAVRAGTRTSPLDGGNLNRAFPGDADGTPTERIAHFLETVLLPRADAVIDLHSGGSSLDFVP
CAAVHLLPDPAQRARSLALAEAFGAPLSVVVDNVDAPGTLDSAAERAGKIFVSTELGGGGTVTPAALRIA
ERGVLNVLIHLGVL
>gnl|CDD|349471 cd06253, M14_ASTE_ASPA-like, Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup. A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD
LESPFREPLEVKGFRFGGGNAEPRIAIVAGIHGDELNGLYVCSRLIRFLKELEEGGYKLKGKVLVIPAVN
PLGINSGTRFWPFDNLDMNRMFPGYNKGETTERIAAALFEDLKGADYGIDLHSSNDFLREIPQVRVIESG
AQDLLPLAKFLGLDVVWVHPASTVDTGTLAYNWNEWGTKALVLEMGVGMRIDKEYCEQLFEGILRFLLKM
G
>gnl|CDD|349472 cd06254, M14_ASTE_ASPA-like, Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup. A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD
PVTLINGAKPGPTLLITAGIHGGEYPGILAAIRLARELDPADVKGTLIIVHIANVSGFEARTPFVVPEDG
KNLNRVFPGDPDGTLTERIAYFLTREIISRADFLIDLHGGDANEALTPFVYYPGGASEEVNDISRAAAQA
LGLPYIVISSSEKGTGYYSYAALRGIPSILVERGGLGTCDEEDVQAHKDGIKNLLRHL
>gnl|CDD|349473 cd06255, M14_ASTE_ASPA-like, Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup. A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD
VGELASGAPVTIPVIVVRGAKPGPCLWINGAVHGDELNGPLAALELFRELDPAQLSGTLVATPIANPLAF
QGRQKFSPQDGEDLDQSFPGDPDGLITERMAHALFSEVKEVADYLIDFHTGGTPFDANPYTVYKLFPESG
PVEEKRLLRLARAFGVHANCRVDVSGAGGELPGNTAGALDYQCMAQGIPAFMVELGGGGRAEEEAVRFAA
RGLRNLLRYLGML
>gnl|CDD|349474 cd06256, M14_ASTE_ASPA-like, Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup. A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD
LLDQLPDGLLDCPAAELLENLPGPTLIHLPGRRPRPLFVSTLLHGNEPTGLRAVQRLLKTGQAPLPRTLL
LFIGNVDAAKAGVRRLPGQPDYNRCWPGPFETPEGRLAAAVLERLDTLRPFASIDIHNNTGKNPHYACVN
RLDAAHLRLASLFSRTLVYFTRPLGVLSEALAALCPAVTVECGKPGDAEGEEHAAEGLDAFLHL
>gnl|CDD|99751 cd06257, DnaJ, DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification
DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD
>gnl|CDD|341049 cd06258, M3_like, M3-like Peptidases, zincin metallopeptidases, include M2_ACE, M3A, M3B_PepF, and M32 families. The peptidase M3-like family, also called neurolysin-like family, is part of the "zincin" metallopeptidases, and includes the M2, M3 and M32 families of metallopeptidases. The M2 angiotensin converting enzyme (ACE, EC 3.4.15.1) is a membrane-bound, zinc-dependent dipeptidase that catalyzes the conversion of the decapeptide angiotensin I to the potent vasopressor octapeptide angiotensin II. The M3 family is subdivided into two subfamilies: the widespread M3A, which comprises a number of high-molecular mass endo- and exopeptidases from bacteria, archaea, protozoa, fungi, plants and animals, and the small M3B, whose members are enzymes primarily from bacteria. Well-known mammalian/eukaryotic M3A endopeptidases are the thimet oligopeptidase (TOP; endopeptidase 3.4.24.15), neurolysin (alias endopeptidase 3.4.24.16), and the mitochondrial intermediate peptidase. The first two are intracellular oligopeptidases, which act only on relatively short substrates of less than 20 amino acid residues, while the latter cleaves N-terminal octapeptides from proteins during their import into the mitochondria. The M3A subfamily also contains several bacterial endopeptidases, called oligopeptidases A, as well as a large number of bacterial carboxypeptidases, called dipeptidyl peptidases (Dcp; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). M3B subfamily consists of oligopeptidase F (PepF) which hydrolyzes peptides containing 7-17 amino acid residues with fairly broad specificity. Peptidases in the M3 family contain the HEXXH motif that forms part of the active site in conjunction with a C-terminally-located Glutamic acid (Glu) residue. A single zinc ion is ligated by the side-chains of the two Histidine (His) residues, and the more C-terminal Glu. Most of the peptidases are synthesized without signal peptides or propeptides, and function intracellularly. There are similarities to the thermostable carboxypeptidases from Pyrococcus furiosus carboxypeptidase (PfuCP), and Thermus aquaticus (TaqCP), belonging to peptidase family M32. Little is known about function of this family, including carboxypeptidases Taq and Pfu
LNSREEKYSKAASLAHWDHDTNIGTEERAAALEEASTLLSEFAEEDSLVALALVEPELSEPLNEEYKRLV
EKIQKLGKAAGAIPKELFKEYNTLLSDFSKLWELRPLLEKLVELRNQAARLLGYEDPYDALLDLYEAGYS
TEVVEQDFEELKQAIPLLYKELHAIQRPKLHRDYGFYYIPKFDVTSAMLKQKFDAEWMFEGALWFLQELG
LEPGPLLTWERLDLYAPLGKVCHAFATDFGRKDVRITTNYTVTRDDILTTHHEFGHALYELQYRTRFAFL
GNGASLGFHESQSQFLENSVGTFKHLYSKHLLSGPQMDDESEEKFLLARLLDKVTFLPHIILVDKWEWAV
FSGEIPKKPDLPSWWNLLYKEYLGVPPVPRDETYTDGWAQFHHWAGYDGYYIRYALGQVYAFQFYEKLCE
DAGHEGKCDIGNFDEAGQKLREILRLGGSRPPTELLKNATGKEPNIASFLLHI
>gnl|CDD|99750 cd06259, YdcF-like, YdcF-like. YdcF-like is a large family of mainly bacterial proteins, with a few members found in fungi, plants, and archaea. Escherichia coli YdcF has been shown to bind S-adenosyl-L-methionine (AdoMet), but a biochemical function has not been idenitified. The family also includes Escherichia coli sanA and Salmonella typhimurium sfiX, which are involved in vancomycin resistance; sfiX may also be involved in murein synthesis
DAIVVLGGGVNGDGPSPILAERLDAAAELYRAGPAPKLIVSGGQGPGEGYSEAEAMARYLIELGVPAEAI
LLEDRSTNTYENARFSAELLRERGIRSVLLVTSAYHMPRALLIFRKAGLDVEVVPAPTDFYSLSSALRLL
RLALREYLGL
>gnl|CDD|411709 cd06260, DUF820-like, Uncharacterized PDDEXK family nuclease. The Domain of unknown function 820 (DUF820) family is composed of hypothetical proteins that are greatly expanded in cyanobacteria. The proteins are found sporadically in other bacteria. They have been predicted to belong to the PD-(D/E)xK superfamily of nucleases, which includes very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI
VRLELIDGELIAMSPAGGRHGRIALNLARLLAAWLRERLGRVFASDTGVRLPDDGSVREPDVAVVCGERL
PDLGIDKFFPGAPDLVVEVLSPSTRYRDLGDKLELYARAGVPEYWLVDPEERTVEVYRLEDGEAYVLVGG
ETLSGESVLPGLELR
>gnl|CDD|119394 cd06261, TM_PBP2, Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters which generally bind type 2 PBPs. These types of transporters consist of a PBP, two TMs, and two cytoplasmic ABC ATPase subunits, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. For these transporters the ABCs and TMs are on independent polypeptide chains. These systems transport a diverse range of substrates. Most are specific for a single substrate or a group of related substrates; however some transporters are more promiscuous, transporting structurally diverse substrates such as the histidine/lysine and arginine transporter in Enterobacteriaceae. In the latter case, this is achieved through binding different PBPs with different specificities to the TMs. For other promiscuous transporters such as the multiple-sugar transporter Msm of Streptococcus mutans, the PBP has a wide substrate specificity. These transporters include the maltose-maltodextrin, phosphate and sulfate transporters, among others
LLNTLLLALIATLLALVLGLLLGIILARKRGKLDRLLRRIIDLLLSLPSLVLGLLLVLLFGVLLGWGILP
GLGLPALILALLLIAPFARLIRRAALESIPKDLVEAARALGASPWQIFRRIILPLALPPILTGLVLAFAR
ALGEFALVSFLGGGEAPGPGTGLLLIFAILFPGDLGVAAAVALILLLLSL
>gnl|CDD|293792 cd06262, metallo-hydrolase-like_MBL-fold, mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site
KRLPVGPLQTNCYLVSDEEGEAILIDPGAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPG
APVYIHEADAELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEE
GVLFTGDTLFAGSIGRTDLPGGDPEQLIESIKKLLLLLPDDTVVYPGH
>gnl|CDD|99706 cd06263, MAM, Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region
CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPR
SSHCLSFWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSG
SRGDIALDDISLSPGPC
>gnl|CDD|119387 cd06265, RNase_A_canonical, Canonical RNase A family includes all vertebrate homologues to the bovine pancreatic ribonuclease A (RNase A) that contain the catalytic site, necessary for RNase activity. In the human genome 8 RNases, refered to as "canonical" RNases, have been identified, pancreatic RNase (RNase 1), Eosinophil Derived Neurotoxin (SEDN/RNASE 2), Eosinophil Cationic Protein (ECP/RNase 3), RNase 4, Angiogenin (RNase 5), RNase 6 or k6, the skin derived RNase (RNase 7) and RNase 8. The eight human genes are all located in a cluster on chromosome 14. Canonical RNase A enzymes have special biological activities; for example, some stimulate the development of vascular endothelial cells, dendritic cells, and neurons, are cytotoxic/anti-tumoral and/or anti-pathogenic. RNase A is involved in endonucleolytic cleavage of 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates. The catalytic mechanism is a transphosphorylation of P-O 5' bonds on the 3' side of pyrimidines and subsequent hydrolysis to generate 3' phosphate groups. The canonical RNase A family proteins have a conserved catalytic triad (two histidines and one lysine). They also share 6 to 8 cysteines that form three to four disulfide bonds. Two disulfide bonds that are close to the N and C termini contribute most significantly to conformational stability. Angiogenin or RNAse 5 has been implicated in tumor-associated angiogenesis. Comparative analysis in mammals and birds indicates that the whole family may have originated from a RNase 5-like gene. This hypothesis is supported by the fact that only RNase 5-like RNases have been reported outside the mammalian class. The RNase 5 group would therefore be the most ancient form of this family, and all other members would have arisen during mammalian evolution
TRYQKFLRQHVDPPRTGIRYCNVMMRRRNMTKGRCKPVNTFIHESFADVRAVCTNPNVTCKNGRNNCHKS
NSPFPVTDCNLTGGSRYPNCRYRGTPSTRKIVVACENGVPVHLDG
>gnl|CDD|259999 cd06266, RNase_HII, Ribonuclease H (RNase H) type II family (prokaryotic RNase HII and HIII, and eukaryotic RNase H2/HII). This family contains ribonucleases HII (RNases H2) which include bacterial RNase HII and HIII, and eukaryotic and archaeal RNase H2/HII. RNase H2 cleaves RNA sequences that are part of RNA/DNA hybrids or that are incorporated into DNA, thereby preventing genomic instability and the accumulation of aberrant nucleic acid which can induce Aicardi-Goutieres syndrome, a severe autoimmune disorder in humans. Ribonuclease H (RNase H) is classified into two families, type I (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type II (prokaryotic RNase HII and HIII, and eukaryotic RNase H2/HII). RNase H endonucleolytically hydrolyzes an RNA strand when it is annealed to a complementary DNA strand in the presence of divalent cations. The enzyme can be found in bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes, but no prokaryotic genome contains the combination of only RNase HI and HIII. Despite a lack of evidence for homology from sequence comparisons, type I and type II RNase H share a common fold and similar steric configurations of the four acidic active-site residues, suggesting identical or very similar catalytic mechanisms. It appears that type I and type II RNases H also have overlapping functions in cells, as over-expression of Escherichia coli RNase HII can complement an RNase HI deletion phenotype in E. coli
AGVDEAGRGCVAGPVVVAAVYCEKEDRLRALGVKDSKQLSPAKRERLADEIMEKVAVAVGVLSPEEIDLY
MAAKNINNATKLAYNRALENLSVKPEFVLVDGKGIEPEYLSRELEEILGVRVTCLVKADSKSPLVAAASI
IAKVFRDREMEELHRKYGLFGSGYYADPETLEELRKNIVLGRIPPCVRLSFET
>gnl|CDD|380491 cd06267, PBP1_LacI_sugar_binding-like, ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain
TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDEL
LEELLAAGIPVVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRD
ALAEAGLPVDPELVVEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVV
GFDDIPLAALLTPPLTTVRQPAYEMGRAAAELLLERIEGEEEPPRRIVLPTELV
>gnl|CDD|380492 cd06268, PBP1_ABC_transporter_LIVBP-like, periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. They are mostly present in archaea and eubacteria, and are primarily involved in scavenging solutes from the environment. ABC-type transporters couple ATP hydrolysis with the uptake and efflux of a wide range of substrates across bacterial membranes, including amino acids, peptides, lipids and sterols, and various drugs. These systems are comprised of transmembrane domains, nucleotide binding domains, and in most bacterial uptake systems, periplasmic binding proteins (PBPs) which transfer the ligand to the extracellular gate of the transmembrane domains. These PBPs bind their substrates selectively and with high affinity. Members of this group include ABC-type Leucine-Isoleucine-Valine-Binding Proteins (LIVBP), which are homologous to the aliphatic amidase transcriptional repressor, AmiC, of Pseudomonas aeruginosa. The uncharacterized periplasmic components of various ABC-type transport systems are included in this group
KIGVVVPLTGPYADYGEEILRGVALAVEEINAAGGINGRKLELVIADDQGDPETAVAVARKLVDDDKVLA
VVGHYSSSVTLAAAPIYQEAGIPLISPGSTAPELTEGGGPYVFRTVPSDAMQAAALADYLAKKLKGKKVA
ILYDDYDYGKSLADAFKKALKALGGEIVAEEDFPLGTTDFSAQLTKIKAAGPDVLFLAGYGADAANALKQ
ARELGLKLPILGGDGLYSPELLKLGGEAAEGVVVAVPWHPDSPDPPKQAFVKAYKKKYGGPPSWRAATAY
DATQALAGDRVQQPVLVV
>gnl|CDD|380493 cd06269, PBP1_glutamate_receptors-like, ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as natriuretic peptide receptors (NPRs), and N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of ionotropic glutamate receptors. This CD represents the ligand-binding domain of the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the ionotropic glutamate receptors, all of which are structurally similar and related to the periplasmic-binding fold type 1 family. The family C GPCRs consists of metabotropic glutamate receptor (mGluR), a calcium-sensing receptor (CaSR), gamma-aminobutyric acid receptor (GABAbR), the promiscuous L-alpha-amino acid receptor GPR6A, families of taste and pheromone receptors, and orphan receptors. Truncated splicing variants of the orphan receptors are not included in this CD. The family C GPCRs are activated by endogenous agonists such as amino acids, ions, and sugar based molecules. Their amino terminal ligand-binding region is homologous to the bacterial leucine-isoleucine-valine binding protein (LIVBP) and a leucine binding protein (LBP). The ionotropic glutamate receptors (iGluRs) have an integral ion channel and are subdivided into three major groups based on their pharmacology and structural similarities: NMDA receptors, AMPA receptors, and kainate receptors. The family of membrane bound guanylyl cyclases is further divided into three subfamilies: the ANP receptor (GC-A)/C-type natriuretic peptide receptor (GC-B), the heat-stable enterotoxin receptor (GC-C)/sensory organ specific membrane GCs such as retinal receptors (GC-E, GC-F), and olfactory receptors (GC-D and GC-G)
TIGALLPVHDYLESGAKVLPAFELALSDVNSRPDLLPKTTLGLAIRDSECNPTQALLSACDLLAAAKVVA
ILGPGCSASAAPVANLARHWDIPVLSYGATAPGLSDKSRYAYFLRTVPPDSKQADAMLALVRRLGWNKVV
LIYSDDEYGEFGLEGLEELFQEKGGLITSRQSFDENKDDDLTKLLRNLRDTEARVIILLASPDTARSLML
EAKRLDMTSKDYVWFVIDGEASSSDEHGDEARQAAEGAITVTLIFPVVKEFLKFSMELKLKSSKRKQGLN
EEYELNNFAAFFYDAVLADRPGQFSIINLQYTEAGDYRKVGTWDSEGGLNMS
>gnl|CDD|380494 cd06270, PBP1_GalS-like, ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism. Ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalS is a dimeric protein like GalR,and its major role is in regulating expression of the high-affinity galactose transporter encoded by the mgl operon, whereas GalR is the exclusive regulator of galactose permease, the low-affinity galactose transporter. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are homologous to the periplasmic sugar binding of ABC-type transport systems
TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEE
LILIAEKIPPLVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRD
ALAEAGIPLDPSLIIEGDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVI
GFDDVPLARYLSPKLTTVHYPIEEMAQAAAELALNLAYGEPLPISHEFTPTLIERD
>gnl|CDD|380495 cd06271, PBP1_AglR_RafR-like, ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. Ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
VIALVFPVTETELNGTVSEXVSGITEEAGTTGYHLLVWPFEEAESXVPIRDLVETGSADGVILSEIEPND
PRVQFLTKQNFPFVAHGRSDXPIGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSPHDRRLQGY
VRAXRDAGLTGYPLDADTTLEAGRAAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIG
KDSAPFLGAMITPPLTTVHAPIAEAGRELAKALLARIDGEDPETLQVLVQPSLS
>gnl|CDD|380496 cd06272, PBP1_hexuronate_repressor-like, ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators. Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGLYWPSVGERVALTRLLSGINEAISKQGYNINLSICPYKVGHLCTAKGLFSENRFDGVIVFGISDSDI
EYLNKNKPKIPIVLYNRESPKYSTVNVDNEKAGRLAVLLLIQKGHKSIAYIGNPNSNRNQTLRGKGFIET
CEKHGIHLSDSIIDSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVS
YDNIPQEARSDPPLTVVGVPIEKIAEESLRLILKLIEGRENEIQQLILYPELIFRE
>gnl|CDD|380497 cd06273, PBP1_LacI-like, ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPEL
FELLEQRQVPYVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDRARARLAGIR
DALAERGLELPEERVVEAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSI
TGFDDLELAAHLSPPLTTVRVPAREIGELAARYLLALLEGGPPPKSVELETELIVRES
>gnl|CDD|380498 cd06274, PBP1_FruR, ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs. Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDI
YYLCQAAGLPVVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELPSTAERIRGFRA
ALAEAGITEGDDWILAEGYDRESGYQLMAELLARLGGLPQALFTSSLTLLEGVLRFLRERLGAIPSDLVL
GTFDDHPLLDFLPNPVDSVRQDHDEIAEHAFELLDALIEGQPEPGVIIIPPELI
>gnl|CDD|380499 cd06275, PBP1_PurR, ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. Ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric PurR belongs to the LacI-GalR family of transcription regulators and is activated to bind to DNA operator sites by initially binding either of high affinity corepressors, hypoxanthine or guanine. PurR is composed of two functional domains: aan N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the purine transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDD
AELLAALRSIPVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFR
RALAEAGIEVPPSWIVEGDFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISI
IGYDDIELARYFSPALTTIHQPKDELGELAVELLLDRIENKREEPQSIVLEPELIERES
>gnl|CDD|380500 cd06277, PBP1_LacI-like, ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIRLIIYSDNGDGVVNETPFFSELIDGIEREARKYGYNLLISSVDIGDDFDEILKELTDDQSSGIILLGT
ELEEKQIKLFQDVSIPVVVVDNYFEDLNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEER
RRGFRKAMRELGLSEDPEPEFVVSVGPEGAYKDMKALLDTGPKLPTAFFAENDIIALGCIKALQEAGIRV
PEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKIKDPDGGTLKILVSTKLVERGS
>gnl|CDD|380501 cd06278, PBP1_LacI-like, ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVDDALRQLLQYRVDGVIVTSATLSSELA
EECARRGIPVVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAA
LAELGLPPPAVEAGDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGLVVPEDISVVGF
DDIPMAAWPSYDLTTVRQPIEEMAEAAVDLLLERIENPETPPERRVLPGELVERGS
>gnl|CDD|380502 cd06279, PBP1_LacI-like, ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria. This group includes the ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding
AIGVLLPDDLSYAFSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAVRNAAVDGFIVYGLSDDDP
AVAALRRRGLPLVVVDGPAPPGIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRLDRGRERGPVSAERL
AAATNSVARERLAGYRDALEEAGLDLDDVPVVEAPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGA
LRAARERGLRVPEDLSVTGFDDIPEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGAPPRPVILPTELV
VRAS
>gnl|CDD|380503 cd06280, PBP1_LacI-like, ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding
TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRE
LKRLLKHGIPIVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYRE
ALAEAGIPVDESLIFEGDSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVV
GFDDSDWFEIVDPPLTVVAQPAYEIGRIAAQLLLERIEGQGEEPRRIVLPTELIIR
>gnl|CDD|380504 cd06281, PBP1_LacI-like, ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEDDPE
LAAALARLDIPVVLIDRDLPGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKA
AFAAAGLPPDPDLVRLGSFSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVV
SIGDSDLAELHDPPITAIRWDLDAVGRAAAELLLDRIEGPPAGPPRRIVVPTELILRDSC
>gnl|CDD|380505 cd06282, PBP1_LacI-like, ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQGSE
ALELLEEEGVPYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDFSASDRARLRYQGY
RDALKEAGLKPIPIVEVDFPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVI
GFDGIAIGELLTPTLATVVQPSRDMGRAAADLLLAEIEGESPPTSIRLPHHLREGGS
>gnl|CDD|380506 cd06283, PBP1_RegR_EndR_KdgR-like, ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR. Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNNDA
YLELAQKGLPVVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGISTRRERLQGFL
DALARYNIEGDVYVIEIEDTEDLQQALAAFLSQHDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLC
GFDDWDWADLIGPGITTIRQPTYEIGKAAAEILLERIEGDSGEPKEIELPSELIIR
>gnl|CDD|380507 cd06284, PBP1_LacI-like, ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group includes the ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding
TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAEL
LSELSKRYPIVQCCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRA
LAEAGLPVDEDLIIEGDFSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIG
FDDIEFAEMFSPSLTTIRQPRYEIGETAAELLLEKIEGEGVPPEHIILPHELIVRES
>gnl|CDD|380508 cd06285, PBP1_LacI-like, ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPD
LQELAARGVPVVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRR
ALAEAGLPVPDERIVPGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVV
GFDDIPLAAFLPPPLTTVRQPKYEMGRRAAELLLQLIEGGGRPPRSITLPPELVVREST
>gnl|CDD|380509 cd06286, PBP1_CcpB-like, ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species. This group includes the ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species. Catabolite control protein B (CcpB) is 30% identical in sequence to CcpA which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. Like CcpA, the DNA-binding protein CcpB exerts its catabolite-repressing effect by a mechanism dependent on the presence of HPr(Ser-P), the small phosphocarrier proteins of the phosphoenolpyruvate-sugar phosphotransferase system, but with a less significant degree
TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIITSRENDWEV
IEPYAKYGPIVLCEETDSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLGRPESSSASTQARLKAYQD
VLGEHGLSLREEWIFTNCHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVI
GFDNQPISELLNLTTIDQPLEEMGKEAFELLLSQLESKEPTKKELPSKLIER
>gnl|CDD|380510 cd06287, PBP1_LacI-like, ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
AIALISSMPFAIAGGASRLGFMMEVAAAAAEEALEHDLALVLVPPLHHVSMLDALDVDGAIVVEPTVEDP
ILARLRQRGVPVVSIGRAPGTDEPVPYVDLQSAATARLLLEHLHGAGARQVALLTGSSRRNSSLESEAAY
LRFAQEYGTTPVVYKVPESEGERAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMV
VTRYDGIRARTADPPLTAVDLHLDRVARTAIDLLFASLSGEERSVEVGPAPELVVRAS
>gnl|CDD|380511 cd06288, PBP1_sucrose_transcription_regulator, ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors. This group includes the ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGLITDDIATTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHREV
TLPPELTDIPLVLLNCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRA
ALAEAGIPYDPSLVVHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVV
GFDNQELAAYLRPPLTTVALPYYEMGRRAAELLLDGIEGEPPEPGVIRVPCPLIERES
>gnl|CDD|380512 cd06289, PBP1_MalI-like, ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria. This group includes the ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria. They are members of the LacI-GalR family of repressor proteins which are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPAAGTTAE
LLRRLKAWGIPVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFR
AALAEAGLPLDESLIVPGPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAV
VGFDDVPEAALWTPPLTTVSVHPREIGRRAARLLLRRIEGPDTPPERIIIEPRLVVRE
>gnl|CDD|380513 cd06290, PBP1_LacI-like, ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEEL
LKLLAEGIPVVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRA
LEDAGLEVDPRLIVEGDFTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIG
FDDLPFSKYTTPPLTTVRQPLYEMGKTAAEILLELIEGKGRPPRRIILPTELVIRES
>gnl|CDD|380514 cd06291, PBP1_Qymf-like, ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs. This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEE
YKKLNIPIVSIDRYLSEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKE
AGIEYEIIEIDENDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDG
IEISELLYPELTTIRQPIEEMAKEAVELLLKLIEGEEIEESRIVLPVELIERET
>gnl|CDD|380515 cd06292, PBP1_AglR_RafR-like, Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the repressors specific raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins highly similar to DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR). Members of this group belong to the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
LIGYVVPELPGGFSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLASTRH
DDPRVRYLHEAGVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLA
GYRAALEEAGLPFDPGLVVEGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRD
VSVVGFDDSPLAAFTHPPLTTVRQPIDEIGRAVVDLLLAAIEGNPSEPREILLQPELVVRESS
>gnl|CDD|380516 cd06293, PBP1_LacI-like, ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSH
LARLRARGTAVVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARA
AVAEAGLDPDEVVRELSAPDANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVS
VVGYDDLPFAAAANPPLTTVRQPSYELGRAAADLLLDEIEGPGHPHEHVVFQPELVVRSS
>gnl|CDD|380517 cd06294, PBP1_MalR-like, ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors. This group includes the ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGLVLPSSAEELFQNPFFSEVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRGRRVDGFILLYSK
EDDPLIEYLKEEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRL
QGYKQALKEAGLPLDDDYILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPE
DVSIISFNNSPLAELASPPLTSVDINPYELGREAAKLLINLLEGPESLPKNVIVPHELI
>gnl|CDD|380518 cd06295, PBP1_CelR, ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. This group includes the ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. The binding of CelR to the celE promoter is inhibited specifically by cellobiose. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
QRSRTIAVVVPMDPHGDQSITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQLARLLDSGRADGLIVL
GQGLDHDALRELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEVAD
RLQGYRDALAEAGLEADPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISV
PGDVAVVGYDDIPLAAYFRPPLTTVRQDLALAGRLLVEKLLALIAGEPVTSSMLPVELVVRES
>gnl|CDD|380519 cd06296, PBP1_CatR-like, ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation. This group includes the ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation. This group belongs to the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQ
LRLLRSAGIPFVLIDPVGEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYR
AALAEAGIAVDPDLVREGDFTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSV
IGFDDTPPARWTSPPLTTVHQPLREMGAVAVRLLLRLLEGGPPDARRIELATELVVRGST
>gnl|CDD|380520 cd06297, PBP1_CcpA_TTHA0807, ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs. Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators
TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMASLDLTELF
EEVIVPTEKPVVLIDANSMGYDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFTETVFREREQGF
LEALNKAGRPISSSRMFRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVA
VIGFDGQPWAASPGLTTVRQPVEEMGEAAAKLLLKRLNEYGGPPRSLKFEPELIVRES
>gnl|CDD|380521 cd06298, PBP1_CcpA, ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation. Ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators
TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEI
REEFKRSPVPVVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYINNDKKLQGYK
RALEEAGLEFNEPLIFEGDYDYDSGYELYEELLESGEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEII
GFDNTRYATMSRPQLTSINQPLYDIGAVAMRLLTKLMNKEEVEETIVKLPHSIIWRQS
>gnl|CDD|380522 cd06299, PBP1_LacI-like, ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum produces significant amounts of L-glutamate directly from cheap sugar and ammonia. This group includes the ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum which has a unique ability to produce significant amounts of L-glutamate directly from cheap sugar and ammonia. This regulatory protein is a member of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEG
LQALIAQGLPVVFVDREVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFR
AALTAAGIPIDEELVAFGDFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSL
ISFDDVPWFELLSPPLTVIAQPVERIGRRAVELLLALIENGGRATSIRVPTELIPRES
>gnl|CDD|380523 cd06300, PBP1_ABC_sugar_binding-like, periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily. Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail
TIGLSNTYAGNSWREQMIASLKADAAQSGQKGLVKELIVANSNGDATEQIAQIRNLIDQGVDAIIINPSS
PTALNAVIEQAADAGIPVVAFDGAVTSPDAYNVSNDQVEWGRLGAKWLFEALGGKGNVLVVRGIAGAPAS
ADRHAGVKEALAEYPGIKVVGEVFGGWDEATAQTAMLDFLATHPQVDGVWTQGGEDTGVLQAFQQAGRPP
VPIVGGDENGFAKQWWKHPKKGLTGAAVWPPPAIGAAGLEVALRLLEGQGPKPQSVLLPPPLITNDDAKA
WYKDDCPDDFSSWPEPPVDILG
>gnl|CDD|380524 cd06301, PBP1_rhizopine_binding-like, periplasmic binding proteins specific to rhizopines. Periplasmic binding proteins specific to rhizopines, which are simple sugar-like compounds produced in the nodules induced by the symbiotic root nodule bacteria, such as Rhizobium and Sinorhizobium. Rhizopine-binding-like proteins from other bacteria are also included. Two inositol based rhizopine compounds are known to date: L-3-O-methly-scyllo-inosamine (3-O-MSI) and scyllo-inosamine. Bacterial strains that can metabolize rhizopine have a greater competitive advantage in nodulation and rhizopine synthesis is regulated by NifA/NtrA regulatory transcription activators which are maximally expressed at the onset of nitrogen fixation in bacteroids. The members of this group belong to the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily
IKIGVSMQNFSDEFLTYLRDAIEAYAKEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDA
SAPAVDAAADAGIPLVYVNREPDSKPKGVAFVGSDDIESGELQMEYLAKLLGGKGNIAILDGVLGHEAQI
LRTEGNKDVLAKYPGMKIVAEQTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKD
DILVAGIDATPDALKAMKAGRLDATVFQDAAGQGETAVDVAVKAAKGEEVESDIWIPFELVT
>gnl|CDD|380525 cd06302, PBP1_LsrB_Quorum_Sensing-like, periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs. Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling
KIAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYTGPTQADAAQQVQIVENLIAQGVDAIAVSPNDADAL
APVLKKAKDAGIKVITWDSDAPPSARDYFVNQADDEGLGEALVDSLAKEIGGKGKVAILSGSLTATNLNA
WIKAMKEYLKSKYPDIELVDTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTG
KVAVTGIGLPNTARPYLKDGSVKEGVLWDPAKLGYLTVYAAYQLLKGKGFTEDSDDVGTGGKVKVDVAGG
EILLGPPLVFTKDNVD
>gnl|CDD|380526 cd06303, PBP1_LuxPQ_Quorum_Sensing, periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs. Periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs from other bacteria. The members of this group are highly homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea, and that are members of the type 1 periplasmic binding protein superfamily. The Vibrio harveyi AI-2 receptor consists of two polypeptides, LuxP and LuxQ: LuxP is a periplasmic binding protein that binds AI-2 by clamping it between two domains, LuxQ is an integral membrane protein belonging to the two-component sensor kinase family. Unlike AI-2 bound to the LsrB receptor in Salmonella typhimurium, the Vibrio harveyi AI-2 signaling molecule has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LuxPQ to control light production as well as its motility behavior
EQRQLTEDFSERVRAPPVPAEVTQKRPVKIAVVYPGLQVSDYWRRSIVSFRKRLDELGIKYQLDEFFTRP
GAEIRLQALQIREMLKSDPDYLIFTLDALRHRRFVEILLDSGKPKLILQNITTPLRDWDNHQPLLYVGFD
HAEGSRMLAKHFIKIFPEEGKYAILYLTEGYVSDQRGDTFIDEVARHSNLELVSAYYTDFDRESAREAAR
ALLARHPDLDFIYACSTDIALGAIDALQELGRETDIMINGWGGGSAELDALQKGGLDVTVMRMNDDNGIA
MAEAIKLDLEGREVPTVYAGDFELVTKGDSPERIEALKKR
>gnl|CDD|380527 cd06304, PBP1_BmpA_Med_PnrA-like, periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and various putative lipoproteins from other bacteria. Periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and various putative lipoproteins from other bacteria. These outer membrane proteins include Med, a cell-surface localized protein regulating the competence transcription factor gene comK in Bacillus subtilis, and PnrA, a periplasmic purine nucleoside binding protein of an ATP-binding cassette (ABC) transport system in Treponema pallidum. All contain the type 1 periplasmic sugar-binding protein-like fold
KVALILPGPINDGGWNQAAYEGLKKAAKELGIEVAYSENVPPADAERVLRDYASQGYDLIIGHGFQFEDA
AKEVAPEFPDTKFVVISGNVTAAPNVASYDFKEEEGGYLAGALAALMTKTGKVGFVGGMEIPPIKRLLAG
FEAGAKAVNPDAKVLVAYTGSWDDVAKAKEAALAMIAQGADVIFGAANAAGLGVIEAAKEKGVYAIGNVS
DQNSLAPDTVVTSVVWDMDPAIYAAVKDVKAGTFGGGVYEYGLKEGGVGLAP
>gnl|CDD|380528 cd06305, PBP1_methylthioribose_binding-like, similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. Proteins similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. The sugar-binding domain of the periplasmic proteins in this group is also homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR), DNA-binding transcriptional repressors such as LacI and GalR
TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALD
PKLKKALDAGIPVVTFDTDSQVPGVNNITQDDYALGTLSLGQLVKDLNGEGNIAVFNVFGVPPLDKRYDI
YKAVLKANPGIKKIVAELGDVTPNTAADAQTQVEALLKKYPEGGIDAIWAAWDEPAKGAVQALEEAGRTD
IKVYGVDISNQDLELMADEGSPWVATAAQDPALIGTVAVRNVARKLAGEDLPDKYSLVPVLIT
>gnl|CDD|380529 cd06306, PBP1_TorT-like, TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport
KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEAGGYTNLSKQISQLEDCVASGADAILLGAISFDG
LDPKVAEAAAAGIPVIDLVNGIDSPKVAARVLVDFYDMGYLAGEYLVEHHPGKPVKVAWFPGPAGAGWAE
DREKGFKEALAGSNVEIVATKYGDTGKAVQLNLVEDALQAHPDIDYIVGNAVAAEAAVGALREAGLTGKV
KVVSTYLTPGVYRGIKRGKILAAPSDQPVLQGRIAVDQAVRALEGKPVPKHVGPPILVV
>gnl|CDD|380530 cd06307, PBP1_sugar_binding, periplasmic sugar-binding domain of uncharacterized transport systems. Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes
RFGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRIHFVDSLDPEALAAALRRLAAGCDGVALVAPDHP
LVRAAIDELAARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRFLGRRPGKVLVILGSHRFRGH
EEREAGFRSVLRERFPDLTVLEVLEGLDDDELAYELLRELLARHPDLVGIYNAGGGNEGIARALREAGRA
RRVVFIGHELTPETRRLLRDGTIDAVIDQDPELQARRAIEVLLAHLGGKGPAPPQPPIPIEIITR
>gnl|CDD|380531 cd06308, PBP1_sensor_kinase-like, periplasmic binding domain of two-component sensor kinase signaling systems. Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail
VIGFSQCSLNDPWRAAMNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADAL
TPVVKKAYDAGIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDR
HKGFLEAIAKYPGIKIVASQDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREKEI
KIIGVDGLPEAGEKAVKDGILAATFLYPTGGKEAIEAALKILNGEKVPKEIVLPTPLI
>gnl|CDD|380532 cd06309, PBP1_galactofuranose_YtfQ-like, periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems. Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally
TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWD
PVLKEAKDAGIPVILVDRTIDGEDGSLYVTFIGSDFVEEGRRAAEWLVKNYKGGKGNVVELQGTAGSSVA
IDRSKGFREVIKKHPNIKIVASQSGNFTREKGQKVMENLLQAGPGDIDVIYAHNDDMALGAIQALKEAGL
KPGKDVLVVGIDGQKDALEAIKAGELNATVECNPLFGPTAFDTIAKLLAGEKVPKLIIVEERLFDKDNAA
EELEP
>gnl|CDD|380533 cd06310, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate-binding protein such as CUT2. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSED
LVDPLKDAKDKGIPVIVIDSGIKGDAYLSYIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQ
REEGFKEYLKKHPGGIKVLASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSG
QIKIVGFDSQEELLDALKNGKIDALVVQNPYEIGYEGIKLALKLLKGEEVPKNIDTGAELIT
>gnl|CDD|380534 cd06311, PBP1_ABC_sugar_binding-like, periplasmic sugar-binding domain of uncharacterized ABC-type transport systems. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
TIGISIPSADHGWTAGVAYYAEKQAKELADLEYKLVTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELT
VAAQKAKDAGIPVVNFDRGLNVLIYDLYVAGDNPGMGVVSAEYIGKKLGGKGNVVVLEVPSSGSVNEERV
AGFKEVIKGNPGIKILAMQAGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRTDIKV
MTGGGGSQEYFKRIMDGDPIWPASATYSPAMIADAIKLAVLILKGGKTVEKEVIIPSTLV
>gnl|CDD|380535 cd06312, PBP1_ABC_sugar_binding-like, periplasmic sugar-binding domain of uncharacterized ABC-type transport systems. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
TIYVISHGSPSDPFWSVVKKGAKDAAKDLGVTVQYLGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDA
LEPALKRAVAAGIPVIAINSGDDRSKERLGALTYVGQDEYLAGQAAGERALEAGPKNALCVNHEPGNPGL
EARCKGFADAFKGAGILVELLDVGGDPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGK
VKIGTFDLSPETLEAIKDGKILFAIDQQPYLQGYLAVVFLYLYKRYGTLPPPEPILTGPGFV
>gnl|CDD|380536 cd06313, PBP1_ABC_ThpA_XypA, periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems. This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge
KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALA
PAVEKAKEAGIPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGPIGQSAQIDRG
KGIENVLKKYPDIKVLAEQTANWSRDEAMSLMENWLQAYGDEIDGIIAQNDDMALGALQAVKAAGRDDIP
VVGIDGIEDALQAVKSGELIATVLQDAEAQGKGAVEVAVDAVKGEGVEKKYYIPFVLVTKDNVDDYL
>gnl|CDD|380537 cd06314, PBP1_tmGBP, periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs. Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP)
TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAV
TPVINKAADKGIPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNER
IQGFKDALKGSPGIEIVDPLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVGKV
KIVGFDTLPETLQGIKDGVIAATVGQRPYEMGYLSVKLLYKLLKGGKPVPDVIDTGVDVVT
>gnl|CDD|380538 cd06315, PBP1_ABC_sugar_binding-like, periplasmic sugar-binding domain of uncharacterized ABC-type transport systems. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
KTIAYVASDLRNGGVLGVGRGVKEAAAALGWKVDVLDGGGTVTGRLAALNQALALKPDGIILGGDDAVEL
QEPLKKAVKAGIPVVGWHAAASPGPIPELGLFTNITTDPREVAETAAALVIAQSGGKAGVVIFTDSRYAI
ATAKANAMKKAIEACSGCKVLEYVDIPIADTAQRMPKLIRSLLQRYGDRWTHTLAINDLYFDFAAPALRA
AGVEADPVNISAGDGSPSAYDRIRAGEYQVATVAEPLTLQGWQLVDELNRALAGEPPSGYVQPVHLVT
>gnl|CDD|380539 cd06316, PBP1_ABC_sugar_binding-like, periplasmic sugar-binding domain of uncharacterized ABC-type transport systems. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
KVAIAMHTTGSDWSRLQVAGIKDTFEELGIEVVAVTDANFDPAKQITDLETLIALKPDIIISIPVDPVAT
AAAYKKVADAGIKLVFMDNVPDGLEAGKDYVSVVSSDNRGNGQIAAELLAEAIGGKGKVGIIYHDADFYA
TNQRDKAFKDTLKEKYPDIKIVAEQGFADPNDAEEVASAMLTANPDIDGIYVSWDTPALGVISALRAAGR
SDIKITTVDLGTEIALDMAKGGNVKGIGAQRPYDQGVAEALAAALALLGKEVPPFIGVPPLAVTKDNLLE
AWKQIFKTDPPAEV
>gnl|CDD|380540 cd06317, PBP1_ABC_sugar_binding-like, periplasmic sugar-binding domain of uncharacterized ABC-type transport systems. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSI
PAIKRASEAGIPVIAYDAVIPSDFQAAQVGVDNLEGGKEIGKYAADYIKAELGGQAKIGVVGALSSLIQN
QRQKGFEEALKANPGVEIVATVDGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQG
KIKVFGWDLTKQAIFLGIDEGVLQAVVQQDPEKMGYEAVKAAVKAIKGEDVEKTIDVPPTIVTKENVDQF
R
>gnl|CDD|380541 cd06318, PBP1_ABC_D-talitol-like, periplasmic D-talitol-binding protein of an ABC transport system and similar proteins. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLT
PAVKAAKAAGIPVITVDSALDPSANVATQVGRDNKQNGVLVGKEAAKALGGDPGKIIELSGDKGNEVSRD
RRDGFLAGVNEYQLRKYGKSNIKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALK
AAGMLDKVKVAGADGQKEALKLIKDGKYVATGLNDPDLLGKTAVDTAAKVVKGEESFPEFTYTPTALITK
DN
>gnl|CDD|380542 cd06319, PBP1_ABC_sugar_binding-like, periplasmic sugar-binding domain of uncharacterized ABC-type transport systems. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAP
TVLDLANEAKIPVVIADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKENGWGGGSVGIIAIPQSRVNG
QARTAGFEDALEEAGVEEVALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRT
GDILVVGFDGDPEALDLIKDGKLDGTVAQQPFGMGARAVELAIQALNGDNTVEKEIYLPVLLVTSENV
>gnl|CDD|380543 cd06320, PBP1_allose_binding, periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding
KIGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTN
LIPPIEKANKKGIPVINLDDAVDADALKKAGGKVTSFIGTDNVAAGALAAEYIAEKLPGGGKVAIIEGLP
GNAAAEARTKGFKETFKKAPGLKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVK
AAGKTGKVLVVGTDGIPEAKKSIKAGELTATVAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALITKD
NVD
>gnl|CDD|380544 cd06321, PBP1_ABC_sugar_binding-like, periplasmic sugar-binding domain of uncharacterized ABC-type transport systems. This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAG
IEPAIKRAKDAGIIVVAVDVAAEGADATVTTDNVQAGYLACEYLVEQLGGKGKVAIIDGPPVSAVIDRVN
GCKEALAEYPGIKLVDDQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDDIVIT
SVDGSPEAVAALKREGSPFIATAAQDPYDMARKAVELALKILNGQEPAPELVLIPSTLVT
>gnl|CDD|380545 cd06322, PBP1_ABC_sugar_binding-like, periplasmic sugar-binding domain of uncharacterized ABC-type transport systems. This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIV
PAIEAANEAGIPVFTVDVKADGAKVVTHVGTDNYAGGKLAGEYALKALLGGGGKIAIIDYPEVESVVLRV
NGFKEAIKKYPNIEIVAEQPGDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDKIK
VIGFDGNPEAIKAIAKGGKIKADIAQQPDKIGQETVEAIVKYLAGETVEKEILIPPKLYT
>gnl|CDD|380546 cd06323, PBP1_ribose_binding, periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis D-ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group belong to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability
TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVS
PAVEEANEAGIPVITVDRSVTGGKVVSHIASDNVAGGEMAAEYIAKKLGGKGKVVELQGIPGTSAARERG
KGFHNAIAKYPKINVVASQTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKDVIV
VGFDGTPDAVKAVKDGKLAATVAQQPEEMGAKAVETADKYLKGEKVPKKIPVPLKLVT
>gnl|CDD|380547 cd06324, PBP1_ABC_sugar_binding-like, periplasmic sugar-binding domain of uncharacterized ABC-type transport systems. This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
RVVFINPGKEDEPFWQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEELLARPPKPDYLILVNEKGV
APELLELAEQAKIPVFLINNDLTDEERALLGKPREKFKYWLGSIVPDNEQAGYLLAKALIKAARKKSDDG
KIRVLAISGDKSTPASILREQGLRDALAEHPDVTLLQIVYANWSEDEAYQKTEKLLQRYPDIDIVWAAND
AMALGAIDALEEAGLKPGKDVLVGGIDWSPEALQAVKDGELTASVGGHFLEGAWALVLLYDYHHGIDFAA
GTSVQLKPMLAITRDNVAQYLKLFGDDNWPKIDFRQF
>gnl|CDD|380548 cd06325, PBP1_ABC_unchar_transporter, type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally
RIGILQFGSHPALDAAREGFRDGLRELGYVEGKNVEIEYRNAQGDPERLPQIAAELVALKPDVIVAIGTP
AAQAAKAATKTIPIVFAAVTDPVGAGLVASLARPGGNVTGVSDLEPVGKRLELLKELLPNAKRVGVLYNP
GEPNSVAQLEELEAAAKKLGLELVEVPVSSPADIEQAFASLAGKVADALYVPTDNTVASARPRIAALALK
ARIPVIYSDREFVEAGALMSYGPDYYDLGRQAARYVDRILKGAKPADLPVEQPTKFELVINLKTAKALGL
TI
>gnl|CDD|380549 cd06326, PBP1_ABC_ligand_binding-like, periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally, however
IVIGQSAPLSGPLAELGREYLAGAKAYFDQVNAAGGINGRKIRLVTLDDGYDPARTVENTRQLIEQDKVV
ALFGYVGTANVEAVLPLLEEAGVPLVGPLTGADSLREPGNPYVFHVRASYADEVEKIVRHLATLGLKRIA
VVYQDDPFGKEGLAAAEAALAARGLEPVATAAVARNAADVAAAAAALAAAKPQAVVLIAAGKAAAAFIKA
LRAAGGAAQFYGLSVVGAAALAKALGDAARGVVVSQVVPNPWSTTLPLVREYQAAMKAAGPKEPSYASLE
GYIAARVLVEALRRAGRNPTRESLVAALESLGRLDLGGFTVDFSPGNHTGSRFVDLTVI
>gnl|CDD|380550 cd06327, PBP1_SBP-like, periplasmic substrate-binding domain of active transport proteins (substrate binding proteins or SBPs). Periplasmic substrate-binding domain of active transport proteins found in gram-negative, gram-positive bacteria, and archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids
RIGVLTDLSGVYADLSGPGSVEAAKMAVEDFGGKVLGRPIEVVSADHQNKPDVASAIAREWYDRDGVDAI
VDVPNSAVALAVQKLAKEKKKIAIVTGAGSSDLTGKACSPYGVHWAYDTYALARGTVKALVKQGGKSWFF
ITADYAFGHSLEADATAAVKAAGGKVVGSVRHPLGTTDFSSFLLQAQASGADVIALANAGADLVNAVKQA
REFGLTDGGQKLAALLLFITDIHALGLDAAQGLYLTTAFYWDRDDATRAWAKRFFARTGKMPTMLQAGVY
SAVLHYLKAVKAAGTDDADAVVAKMREMPVNDFFAKNGRIRADGRVVHDMYLVQVK
>gnl|CDD|380551 cd06328, PBP1_SBP-like, periplasmic substrate-binding domain of active transport proteins (substrate binding proteins or SBPs). Periplasmic substrate-binding domain of active transport proteins found in gram-negative and gram-positive bacteria. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids
KIGVITSLTGPLAAYGKQTERGFELGLEYATDGTMEVDGRKIEVIVKDDQGDPDTAKAAATELIGDDGVD
ILVGTVSSAVALALAPVAEQNKKILIVGPAAADSITGENWNKYTFRTSRNSWQDAIAGAKALADPLGKSV
AFLAQDYAFGQDGVAAFKKALEAKGGKIVGEELVPVTTTDFTPYLQRILDAKPDVLFVAWAGTGALTLWQ
QLADQGVLDDIKVVTGGPDIATLAALGDALPGIEGLTYYYYGLPKNPVNDWLVKAHKERYNAPPDLFTAG
GFAAAQAVVRALEKAGGDTDVEKLIAALEGLTFETPKGKMTIRAEDHQALQPMYIV
>gnl|CDD|380552 cd06329, PBP1_SBP-like, periplasmic substrate-binding domain of active transport proteins (substrate binding proteins or SBPs). Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids
KIAFIDPLSGPFASVGEIYLKGLQFAIEEINAGGGLLGRKIELVPFDNKGSPQEALIQLKKAIDQGIRFV
LQGNSSAVAGALIDAIEKHNQRNPDKRVLFLNYGAEAPELTGAKCSFWHFRFDANADMKMAALADYMKKD
GSIKKVYLINQDYSFGRDVAAAAKKNLKKKRPDIEIVGEDLHPLGKVKDFSPYIAKIKASGADTVITGNW
GNDLTLLMKAARDSGLKAPFYTYYADGPGAPAAIGEAGVGRLVAVAYWHPNPKTPELEKFAEAFRAKYGR
YPDFNIGRTYMGVEMLAAAIKKAGSTDPEKVAKALEGLSFDTPGGPVTMRADDHQAIQPLYIS
>gnl|CDD|380553 cd06330, PBP1_As_SBP-like, periplasmic substrate-binding domain of active transport proteins. Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea that is predicted to be involved in the efflux of toxic compounds. Members of this subgroup include proteins from Herminiimonas arsenicoxydans, which is resistant to arsenic (As) and various heavy metals such as cadmium and zinc. Moreover, they show significant sequence similarity to the cluster of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa
KIGVITPLSGAAAVYGEPARNGAELAVEEINAAGGILGRKIELVVRDDKGKPDEAVRAARELVLQEGVDF
LIGTISSGVALAVAPVAEELKVLFIATDAATDRLTEENFNPYVFRTSPNTYMDAVAAALYAAKKPPDVKR
WAGIGPDYEYGRDSWAAFKAALKKLKPDVEVVGELWPKLGATDYTAYITALLAAKPDGVFSSLWGGDLVT
FVKQAKPYGLFDKTKVVSGLGGGSEVLQALGKEMPEGLIGGGRYPFGWPDTPLNKAFVEAYRAKYGEYPT
YWAYEAYAAVMALKAAIEKAGSTDTDKVIAALEGLTFDTPGGKITIRAEDHQAVQPVVVGTT
>gnl|CDD|380554 cd06331, PBP1_AmiC-like, type 1 periplasmic components of amide-binding protein (AmiC) and the active transport system for short-chain and urea (FmdDEF). This group includes the type 1 periplasmic components of amide-binding protein (AmiC) and the active transport system for short-chain and urea (FmdDEF), found in bacteria and Archaea. AmiC controls expression of the amidase operon by a ligand-triggered conformational switch. In the absence of ligand or presence of butyramide (repressor), AmiC (the ligand sensor and negative regulator) adopts an open conformation and inhibits the transcription antitermination function of AmiR by direct protein-protein interaction. In the presence of inducing ligands such as acetamide, AmiC adopts a closed conformation which disrupts a silencing AmiC-AmiR complex and the expression of amidase and other genes of the operon is induced. FmdDEF is predicted to be an ATP-dependent transporter and closely resembles the periplasmic binding protein and the two transmembrane proteins present in various hydrophobic amino acid-binding transport systems
KIGLLTPLSGPASVYGRAIANGAELAVEEINAAGGVLGRPVELVVEDDASDPATAVAAARRLIQQDKVDA
IVGPITSATRNAVAPVAERAKVPLLYPTFYEGGECSPYLFCFGEVPNQQLDPLIPWLMEEYGKKFYLIGS
DYVWPRTMNDAARRVIEAHGGEVVGEEYLPLGTTDFSSVIEKIKASGADVVLSTLVGADAVTFLKQFAAA
GLRRKVRIAALLFDENTLAGLGAEAAEGIYSVLSYFQSLDTPENKAFVAAYRKKFGEDAPPITSLSEAAY
EAVHLYAAAVEKAGSTDPEAVIAALPGVSFDGPQGPVTMDPDNHHVRLNLYIA
>gnl|CDD|380555 cd06332, PBP1_aromatic_compounds-like, type 1 periplasmic binding proteins of active transport systems predicted to be involved in transport of aromatic compounds such as 2-nitrobenzoic acid and alkylbenzenes. This group includes the type 1 periplasmic binding proteins of active transport systems that are predicted to be involved in transport of aromatic compounds such as 2-nitrobenzoic acid and alkylbenzenes; their substrate specificities are not well characterized, however. Members also exhibit close similarity to active transport systems for short chain amides and/or urea found in bacteria and archaea
KIGLLAPLTGPFAALGEDMVRGFELALEEVGGEVAGRKVELVVEDDAGDPDTAVTKARKLVEQDKVDVLI
GPLSGDEGLAVAPYAKEPGVPFINPVAGADDLTQRAKAPNFFRTSFTGSQWSAPLGDYAYKELGYKKVAT
IGSDYAFGYEQAAGFKRGFEAAGGEVVQEIWVPLGTTDFSPYIAQIPSADDAVFAFLGGADAVRFLKQYR
EFGLKDKIPLIGGGTTVDESVLPAMGDAALGIISASHYAEGLDNPENKKFVAAYKKKFGKLPSLYAAGGY
DGAQAILEALEAVGGDVSDKQALAAALRKVKFDSPRGPFSFDENRNPVQNVYIREV
>gnl|CDD|380556 cd06333, PBP1_ABC_RPA1789-like, type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, RPA1791-1793), involved in active transport of lignin-derived aromatic substrates, and its close homologs. This group includes RPA1789 (CouP) from Rhodopseudomonas palustris and its close homologs in other bacteria. RPA1789 (CouP) is the periplasmic binding-protein component of an ABC system (CouPSTU; RPA1789, RPA1791-1793) that is involved in the active transport of lignin-derived aromatic substrates. Members of this group has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP)
KIGAILSLTGPAASLGIPERNAVELLVEQINAAGGINGRKLELIVYDDESDPTKAVTNARKLIEEDKVDA
IIGPSTTGESLAVAPIAEEAKVPLISLAGAAAIVEPVRKWVFKTPQSDSLVAEAILDYMKKKGIKKVALL
GDSDAYGQSGRAALKKLAPEYGIEIVADERFARTDTDMTAQLTKIRAAKPDAVLVWASGPPAALVAKNLR
QLGYKGPIYQSHGAANQDFIKLAGKAAEGVILPAGKLLVADQLPDSDPQKKVLLEFVKAYEAKYGEGPST
FAGHAYDALLLLVEAIEPAGGTDRAALRDALENTKGLVGVTGVYNFSPTDHNGLDPDSLVMV
>gnl|CDD|380557 cd06334, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters, such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally
KIGLLTDLTGPTADVGKPYAQGVRDYLNYVNEEGGINGVKIELEECDTGYKVPRAVACYKRLKAQDGVVA
ILGWGTGDTEALAPRVAKDKIPYISASYGRSLADDGKVFPYNFFVGATYSSQARALLKYIAQEWGGKLKG
PKVAFVYHDSPFGREPIPALKAYAKELGFEVVAEQVPSPGALDATAQWLRIRRAGPDYVIIQGTGGSVAV
IIKDAKRLGLKTKFIGNIWGGDEDLIKLAGDAAEGYVGVSPFAFGTDDPPGKEIVEEVAKKGKGDGPEEV
GTVYYNRGWATAMLAVEAIRRADKAGGGTGLGNKLKAGLERLKDFDLGGLAPPVTFTPTDHRGGGVVRIY
QWDGGKWVPV
>gnl|CDD|380558 cd06335, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters, such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally
KIGVIGPLTGPSAELGESARRGVELAVEEINAAGGILGRKIELVERDDEANPTKAVQNAQELIDKEKVVA
IIGPTNSGVALATIPILQEAKIPLIIPVATGTAITKPPAKPRNYIFRVAASDTLQADFLVDYAVKKGFKK
IAILHDTTGYGQGGLKDVEAALKKRGITPVATESFKIGDTDMTPQLLKAKDAGADVILVYGLGPDLAQIL
KAMEKLGWKVPLVGSWGLSMPNFIELAGPLAEGTIMTQTFIEDYLTPRAKKFIDAYKKKYGTDRIPSPVS
AAQGYDAVYLLAAAIKQAGSTDGKKIRAALENLKGYVGGVKTYNKPFSKTDHEALDVSMVVLGYWKDG
>gnl|CDD|380559 cd06336, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions. This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, their ligand specificity has not been determined experimentally
KIGFLGPLSGPAAAWGLPMLRGLELAADEINAAGGIKVGGKKYKVEVVSYDDKYTPAEAVAAARRLVSQD
GVKFIFGPGGSAIAAAVQPVTERNKVLLLTAAFSDPILGPDNPLLFRIPPTPYEYAPPFIKWLKKNGPIK
TVALIAPNDATGKDWAAAFVAAWKAAGGEVVAEEFYDRGTTDFYPVLTKILALKPDALDLGGSSPGPAGL
IIKQARELGFKGPFVSEGGAKADEILKEVGGEAAEGFIGVLPADDDPIASPGAKAFVERYKKKYGEPPNS
ESALFYDAAYILVKAMEKAGTVDDTKKIRAALAMLSPDETLFGKLKWGGKEIYGINHQLLVPVVV
>gnl|CDD|380560 cd06337, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters, such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally
KIGRVSPLTGPLAAFGEADPWVLEQIREAFADGGIKVGGKKYPVEIVVRDSQSDPNRAGEAARDLILRDK
VDLMLASGTPDTVNPVADQCEANGVPCISTDAPWQAWFFGRGGDPAKGFKWTFHFFWGLEDIAANFLGMW
DQVPTNKVVGLLWPNDPDGTAFADAFLGLPAAAGYTLVDPGRFPPGTDDFSSIINAFKKAGVEIVTGVMI
PPDFATFWRQAAQQGFKPKVVTIGKALLFPSAVAALGDLGDGLSTEVWWSPAHPFKSSLTGQTAAELADA
YEKATGKQWTQPLGYAHALFEVAVDALKRAGSPDDEAVRAALADTDLDTIVGPVDFTSGPVPNVAKTPLV
GGQW
>gnl|CDD|380561 cd06338, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT); however, their ligand specificity has not been determined experimentally
KIGASLSLTGPFAGEGKAQKRGYELWVEDVNAAGGVKGGGKKRPVELVYYDDQSDPATAVRLYEKLITED
KVDLLLGPYSSGLTLAAAPVAEKYGIPMIAGGAASDSIFERGYKYVFGVLPPASDYAKGLLDLLAELGPK
PKTVAIVYEDDPFGKEVAEGAREAAKKAGLEVVYDESYPPGTTDFSPLLTKVKAANPDILLVGGYPPDAI
TLVRQMKELGYNPKAFFLTVGPAFPAFREALGKDAEGVLGPSQWEPSLPYKVFPGAKEFVKAYKEKFGEE
PSYHAAAAYAAGQVLQQAIEKAGSLDPEKVRDALASLDFDTVYGPIKFDETGLQIGKPMVVVQWQGG
>gnl|CDD|380562 cd06339, PBP1_YraM_LppC_lipoprotein-like, periplasmic binding component of lipoprotein LppC, an immunodominant antigen. This subgroup includes periplasmic binding component of lipoprotein LppC, an immunodominant antigen, whose molecular function is not characterized. Members of this subgroup are predicted to be involved in transport of lipid compounds, and they are sequence similar to the family of ABC-type hydrophobic amino acid transporters (HAAT)
RIALLLPLSGPYAAAGQAIRDGIELALFDAGGSRPELRVYDTGGPEGAAAAYQQAVAEGADLIIGPLLKS
SVAALAAAAQALGVPVLALNNDESATAGPGLFQFGLSPEDEARQAARYAVQQGLRRFAVLAPDNAYGQRV
ANAFREAWQALGGTVVAVESYDPDETDFSAAIRRLLGVDQSEARIRQLGELLEFEPRRRQDFDAIFLPAG
PEQARLIAPQLAFYGAGDVPLLGTSLWYSGKLNLLRDPDLNGAWFADPPWLLSPRAFPLRYRLAYGWPPP
RLAALGYDAYRLAARLARLGGGLTPGAGFSGLTGLLRLDPDGRIERQLAWA
>gnl|CDD|380563 cd06340, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, their ligand specificity has not been determined experimentally
KIGVLYPLSGPLALIGQEAKRGAELAVDEINAAGGIKSLGGAKIELVVADTQSDPEVAASEAERLITQEG
VVAIIGAYSSSVTLAASQVAERYGVPFVTASAVADEITERGFKYVFRTAPTASQFAEDAVDFLKELAKKK
GKKIKKVAIIYEDSAFGTSVAKGLKKAAKKAGLEVVLDEPYPAGATDLSSEVLKLKAAKPDVVFATSYTN
DAILLLRTMKELGFKPKAIIGVGGGYSDPEFLKALGKDAEGVFSVVPWSPDLAKKKPGAKEVNERYKKKY
GEDMTGHAARAYTAAWVLADALERAGSTDPEAIRAAAALTLDIPEGLIMPGGGVKFDEKGQNVLARPVVV
QW
>gnl|CDD|380564 cd06341, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally
KIGLIYPDTGPGAASFSAARAGAEARFGLANAAGGINGRKVEYVWCDDQSDPATNLQAARQLVEDEKVFA
LVGSSSAASGSANDYLAQAGIPVVGGAGVSVWCFRNMFSNFFSLGGGGSTTTYGQYAAALGGTKAAVVVT
DIPAASQQLAQQLAASLRAAGVEVVGTAPYAAAAPDYTAVAQAAKAAGADAVVGVLDPDVAARVLKAARA
QGLDLKVALSPSGYDPSVLAAYGAALAGVSVASTFLPFEADTPAVKAYRAAMAKYAPELQDPLQQFALSG
YIAADLFVRGLEAAGGCPTRAAFIKALRDVKDYDAGGLLPPGDFTANPGLPSTCYAFVRV
>gnl|CDD|380565 cd06342, PBP1_ABC_LIVBP-like, type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active transport systems involved in the transport of all three branched chain aliphatic amino acids (leucine, isoleucine and valine). This subgroup includes the type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active transport systems that are involved in the transport of all three branched chain aliphatic amino acids (leucine, isoleucine and valine). This subgroup also includes a leucine-specific binding protein (or LivK), which is very similar in sequence and structure to leucine-isoleucine-valine binding protein (LIVBP). ABC-type active transport systems are transmembrane proteins that function in the transport of diverse sets of substrates across extra- and intracellular membranes, including carbohydrates, amino acids, inorganic ions, dipeptides and oligopeptides, metabolic products, lipids and sterols, and heme, to name a few
KIGVAGPLTGPNAALGQDIRNGAELAVDEINAKGGGLGFKIELVAQDDACDPAQAVAAAQKLVADGVVAV
IGHYNSGAAIAAAPIYAEAGIPMISPSATNPKLTEQGYKNFFRVVGTDDQQGPAAADYAAKTLKAKRVAV
IHDGTAYGKGLADAFKKALKALGGTVVGREGITPGTTDFSALLTKIKAANPDAVYFGGYYPEAGLLLRQL
REAGLKAPFMGGDGIVSPDFIKAAGDAAEGVYATTPGAPPEKLPAAKAFLKAYKAKFGEPPGAYAAYAYD
AAQVLLAAIEKAGSTDRAAVAAALRATDFDGVTGTISFDAKGDLTGPAFTVYQV
>gnl|CDD|380566 cd06343, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however its ligand specificity has not been determined experimentally
GVTDDEIKIGTSLPLSGPAAAYGKPVRAGAAAYFDEVNAAGGINGRKIELIVEDDGYDPARAVAAVRKLV
EQDKVFAIVGGLGTPTNLAVRPYLNEAGVPQLFPATGASALSPPPKPYTFGVQPSYEDEGRILADYIVET
LPAAKVAVLYQNDDFGKDGLEGLKEALKAYGLEVVAEETYEPGDTDFSSQVLKLKAAGADVVVLGTLPKE
AAAALKEAAKLGWKPTFLGSSVSADPTTLAKAGGDAAEGVYSASYLKDPTDADDPAVKEFREAYKKYFPD
DPPNAYALYGYAAAQVFVEALKRAGKDLTREGLIKALESLKDFDDGGPGPPVTFSPDDHRGIESMYLVQV
DGGKW
>gnl|CDD|380567 cd06344, PBP1_ABC_HAAT-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of hydrophobic amino acids or peptides. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of hydrophobic amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally
DIVIGVAWPFAPDGDLFLEGVELAVEEINAAGGVLGRKIRLVEYDDEASVDKGLAIAQRFADNPDVVAVI
GHRSSYVAIPASIIYERAGLLMLSPGATAPKLTQHGFKYIFRNIPSDEDIARQLARYAARQGYKRIVIYY
DDDSYGKGLANAFEEEARELGITIVDRRSYSSDEEDFRRLLSKWKALDFFDAIFLAGSMPEGAEFIKQAR
ELGIKVPIIGGDGLDSPELIEIAGKAAEGVVVATVFDPDDPRPEVRAFVEAFRKKYGREPDVWAAQGYDA
VKLLAEAIEKAGSTVPAKIASALRFLENWEGVTGTYSFDANGDVVGKAIYFK
>gnl|CDD|380568 cd06345, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally
KIGVLGPLSAPAGEAMERGAELAVEEINAAGGILGRKVELVVADTQGKPEDGVAAAERLITEDKVDAIVG
GFRSEVVLAAMEVAAEYKVPFIVTGAASPAITKKVKKDYEKYKYVFRVGPNNSYLGATVAEFLKDLLVEK
LGFKKVAILAEDAAWGRGIAEALKKLLPEAGLEVVGVERFPTGTTDFTPILSKIKASGADVIVTIFSGPG
GILLVKQWAELGVPAPLVGINVPAQDPEFWENTGGAGEYEITLAFAAPKAKVTPKTKPFVDAYKKKYGEA
PNYTAYTAYDAIYILAEAIERAGSTDPDALVKALEKTDYEGVRGRIKFDKKDEYPHDVKYGPGYVTGLIF
QWQDGG
>gnl|CDD|380569 cd06346, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally
KIGALLPLTGPLASLGPPMLAAAELAVEEINAAGGVLGKKVELVVEDSQTDPTAAVDAARKLVDVEGVPA
IVGAASSGVTLAVASVAVPNGVVQISPSSTSPALTTLEDKGYVFRTAPSDALQGVVLAQLAAERGFKKVA
VIYVNNDYGQGLADAFKKAFEALGGTVTASVPYEPGQTSYRAELAQAAAGGPDALVLIGYPEDGATILRE
ALELGLDFTPWIGTDGLKSDDLVEAAGAEALEGMLGTAPGSPGSPAYEAFAAAYKAEYGDDPGPFAANAY
DAVMLLALAYEGASGPIDFDENGDVAGPYEIWKV
>gnl|CDD|380570 cd06347, PBP1_ABC_LivK_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally
KIGVIGPLTGEAAAYGQPALNGAELAVDEINAAGGILGKKIELIVYDNKSDPTEAANAAQKLIDEDKVVA
IIGPVTSSIALAAAPIAQKAKIPMITPSATNPLVTKGGDYIFRACFTDPFQGAALAKFAYEELGAKKAAV
LYDVSSDYSKGLAKAFKEAFEKLGGEIVAEETYTSGDTDFSAQLTKIKAANPDVIFLPGYYEEAALIIKQ
ARELGITAPILGGDGWDSPELLELGGDAVEGVYFTTHFSPDDPSPEVQEFVKAYKAKYGEPPNAFAALGY
DAVMLLADAIKRAGSTDPEAIRDALAKTKDFEGVTGTITFDPNGNPIKPAVILE
>gnl|CDD|380571 cd06348, PBP1_ABC_HAAT-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally
KIGVALSLTGPGALYGQSQKNGAQLAVEEINAAGGVGGVKIELIVEDTAGDPEQAINAFQKLINQDKVLA
ILGPTLSSEAFAADPIAQQAKVPVVGISNTAPGITDIGPYIFRNSLPEDKVIPPTVKAAKKKYGIKKVAV
LYDQDDAFTVSGTKVFPAALKKNGVEVLDTETFQTGDTDFSAQLTKIKALNPDAIVISALAQEGALIVKQ
ARELGLKGPIVGGNGFNSPDLIKLAGKAAEGVIVGSAWSPDNPDPKNQAFVAAYKEKYGKEPDQFAAQAY
DAAYILAEAIKKAGSTTDRADLRDALARILIAKDFEGPLGPFSFDADRDGIQPPVVLIVKDG
>gnl|CDD|380572 cd06349, PBP1_ABC_HAAT-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally
KIGVSGPLTGDNAEYGQQFKNGVELAVDEINAAGGVNGRKLELVVYDDQGDPKEAVNIAQKFVSDDKVVA
VIGDFSSSCSMAAAPIYEEAGLVQISPTASHPDFTKGGDYVFRNSPTQAVEAPFLADYAVKKLGAKKIAI
IYLNTDWGVSAADAFKKAAKALGGEIVATEAYLPGTKDFSAQITKIKNANPDAIYLAAYYNDAALIAKQA
RQLGWDVQIFGSSSLYSPEFIELAGDAAEGVYLSSPFFPESPDPEVKEFVKAYKAKYGEDPDDFAARAYD
AVNILAEAIEKAGTDREAIRDALANIKDFSGLTGTITFDENGDVLKSLTILVVKDGKF
>gnl|CDD|380573 cd06350, PBP1_GPCR_family_C-like, ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory transmission on the cellular surface through initial binding of glutamate; categorized into ionotropic glutamate receptors (iGluRs) and metabotropic glutamate receptors (mGluRs). Ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory transmission on the cellular surface through initial binding of glutamate and are categorized into ionotropic glutamate receptors (iGluRs) and metabotropic glutamate receptors (mGluRs). The metabotropic glutamate receptors (mGluR) are key receptors in the modulation of excitatory synaptic transmission in the central nervous system. The mGluRs are coupled to G proteins and are thus distinct from the iGluRs which internally contain ligand-gated ion channels. The mGluR structure is divided into three regions: the extracellular region, the seven-spanning transmembrane region and the cytoplasmic region. The extracellular region is further divided into the ligand-binding domain (LBD) and the cysteine-rich domain. The LBD has sequence similarity to the LIVBP, which is a bacterial periplasmic protein (PBP), as well as to the extracellular region of both iGluR and the gamma-aminobutyric acid (GABA)b receptor. iGluRs are divided into three main subtypes based on pharmacological profile: NMDA, AMPA, and kainate receptors. All family C GPCRs have a large extracellular N terminus that contain a domain with homology to bacterial periplasmic amino acid-binding proteins
IIGGLFPVHYRDDADFCCCGILNPRGVQLVEAMIYAIEEINNDSSLLPNVTLGYDIRDTCSSSSVALESS
LEFLLDNGIKLLANSNGQNIGPPNIVAVIGAASSSVSIAVANLLGLFKIPQISYASTSPELSDKIRYPYF
LRTVPSDTLQAKAIADLLKHFNWNYVSTVYSDDDYGRSGIEAFEREAKERGICIAQTIVIPENSTEDEIK
RIIDKLKSSPNAKVVVLFLTESDARELLKEAKRRNLTGFTWIGSDGWGDSLVILEGYEDVLGGAIGVVPR
SKEIPGFDDYLKSYAPYVIDAVYATVKFDENGDGNGGYDIVNLQRTGTGNYEYVEVGTWDSNSGGLSLNS
>gnl|CDD|380574 cd06351, PBP1_iGluR_N_LIVBP-like, N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NMDA, AMPA, and kainate receptor subtypes of ionotropic glutamate receptors (iGluRs). N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NMDA, AMPA, and kainate receptor subtypes of ionotropic glutamate receptors (iGluRs). While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Glutamate mediates the majority of excitatory synaptic transmission in the central nervous system via two broad classes of ionotropic receptors characterized by their response to glutamate agonists: N-methyl-aspartate (NMDA) and non-NMDA receptors. NMDA receptors have intrinsically slow kinetics, are highly permeable to Ca2+, and are blocked by extracellular Mg2+ in a voltage-dependent manner. On the other hand, non-NMDA receptors have faster kinetics, are weakly permeable to Ca2+, and are not blocked by extracellular Mg2+. While non-NMDA receptors typically mediate excitatory synaptic responses at resting membrane potentials, NMDA receptors contribute to several forms of synaptic plasticity and are suggested to play an important role in the development of synaptic pathways
HIGFIFEVNNEPAAKAFEVAVTYLKKNINTRYGLSVQYDSIEANKSNAFVLLEAICNKYATGTPALILDT
TKSSINSLTSALGAPHISASYGQQGDLRQWRDLDEAKQKYLLQVRPPEALRSIVLHLNITNAWIKFVDSY
DMEHYKSLLQNIQTRAVQNNVIVAIAKVGKREREEQLDINNFFILGTLQSIRMVLEVRPAYFERNFAWHA
ITQNEVEISSQSDNAHIMFMNPMAYDILLETVYRDRLGLTRTTYNLNENPMVQQFIQRWVRLDEREFPEA
KNAELQLSSAFYFDLALRSALAFKETGYGTFDLQSTQPFNGHSFMKFEMDINVRKIRGWSEYESVNSK
>gnl|CDD|380575 cd06352, PBP1_NPR_GC-like, ligand-binding domain of membrane guanylyl-cyclase receptors. Ligand-binding domain of membrane guanylyl-cyclase receptors. Membrane guanylyl cyclases (GC) have a single membrane-spanning region and are activated by endogenous and exogenous peptides. This family can be divided into three major subfamilies: the natriuretic peptide receptors (NPRs), sensory organ-specific membrane GCs, and the enterotoxin/guanylin receptors. The binding of peptide ligands to the receptor results in the activation of the cytosolic catalytic domain. Three types of NPRs have been cloned from mammalian tissues: NPR-A/GC-A, NPR-B/ GC-B, and NPR-C. In addition, two of the GCs, GC-D and GC-G, appear to be pseudogenes in humans. Atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP) are produced in the heart, and both bind to the NPR-A. NPR-C, also termed the clearance receptor, binds each of the natriuretic peptides and can alter circulating levels of these peptides. The ligand binding domain of the NPRs exhibits strong structural similarity to the type 1 periplasmic binding fold protein family
KVGVLAPSNSQSLPVGYARSAPAIDIAIERINSEGLLLPGFNFEFTYRDSCCDESEAVGAAADLIYKRNV
DVFIGPACSAAADAVGRLATYWNIPIITWGAVSASFLDKSRYPTLTRTSPNSLSLAEALLALLKQFNWKR
AAIIYSDDDSKCFSIANDLEDALNQEDNLTISYYEFVEVNSDSDYSSILQEAKKRARIIVLCFDSETVRQ
FMLAAHDLGMTNGEYVFIFIELFKDGFGGNSTDGWERNDGRDEDAKQAYESLLVISLSRPSNPEYDNFSK
EVKARAKEPPFYCYDASEEEVSPYAAALYDAVYLYALALNETLAEGGNYRNGTAIAQRMWNRTFQGITGP
VTIDSNGDRDPDYALLDLDPSTGKFVVVLTYDGTSNGLVVV
>gnl|CDD|380576 cd06353, PBP1_Med-like, periplasmic binding domain of the basic membrane lipoprotein Med in Bacillus and its close homologs from other bacteria and Archaea. Periplasmic binding domain of the basic membrane lipoprotein Med in Bacillus and its close homologs from other bacteria and Archaea. Med, a cell-surface localized protein, which regulates the competence transcription factor gene comK in Bacillus subtilis, lacks the DNA binding domain when compared with structures of transcription regulators from the LacI family. Nevertheless, Med has significant overall sequence homology to various periplasmic substrate-binding proteins. Moreover, the structure of Med shows a striking similarity to PnrA, a periplasmic nucleoside binding protein of an ATP-binding cassette transport system. Members of this group contain the type 1 periplasmic sugar-binding protein-like fold
KVGLLVEGTISDQGWGSKAYKGLLNIEEKFGVDVEYKENIDSEEKIEEAVEELVEKGVNLIFGHGREFGE
YFNEIAPDYPDVHFVSFNGEAKHDNVTSIHFDGYAMGYFAGMLAAHMTKTNKVGVIAAFPWQPEVEGFEE
GVKYVSPEAKVLVRFVNDWDDGEKAMELAQELISQGVDVVYPAGDGFNVEVIEQAKEDGLYAIGYIDDQS
YIGPNTVLTSTVQDVPQLYEAIANQFNEGELTPGNITYDFNDGVVSLGPF
>gnl|CDD|380577 cd06354, PBP1_PrnA-like, periplasmic binding domain of basic membrane lipoprotein, PnrA, in Treponema pallidum and its homologs from other bacteria and Archaea. Periplasmic binding domain of basic membrane lipoprotein, PnrA, in Treponema pallidum and its homologs from other bacteria and Archaea. The PnrA lipoprotein, also known as Tp0319 or TmpC, represents a novel family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC) transport system (pnrABCDE). It shows a striking structural similarity to another basic membrane lipoprotein Med which regulates the competence transcription factor gene, comK, in Bacillus subtilis. The members of PnrA-like subgroup are likely to have similar nucleoside-binding functions and a similar type 1 periplasmic sugar-binding protein-like fold
KVALVTDSGGIGDKSFNQSAWEGLQRAAKELGIKVKYLESKSDADYEPNLRALADEGYDLIITVGFAMAD
AVEEAAKANPDTKFIIIDATVDETPPNVRSIVFREEEAAFLAGYLAALMTKTGKVGFIGGMDIPPVRRFE
DGFAAGAKYANPDIVVDVTVIGTYAGSFNDPAKGKAIAQEMIDQGADVIFAAAGGTGLGVIEAAKEAGKY
AIGVDVDQNYLAPGNVLTSVVKRVDVAVYDAIKDLVNGKFGGGVIVLGLAEGGVGLAP
>gnl|CDD|380578 cd06355, PBP1_FmdD-like, periplasmic component (FmdD) of an active transport system for short-chain amides and urea (FmdDEF). This group includes the periplasmic component (FmdD) of an active transport system for short-chain amides and urea (FmdDEF), found in Methylophilus methylotrophus, and its homologs from other bacteria. FmdD, a type 1 periplasmic binding protein, is induced by short-chain amides and urea and repressed by excess ammonia, while FmdE and FmdF are hydrophobic transmembrane proteins. FmdDEF is predicted to be an ATP-dependent transporter and closely resembles the periplasmic binding protein and the two transmembrane proteins present in various hydrophobic amino acid-binding transport systems
KVGILHSLSGTMAISERPLVDATLLAIDEINAAGGLLGRKIEPVIEDGASDWPTFAEKAEKLITQDKVAV
IFGCWTSASRKAVLPVIEKYNGLLFYPVQYEGLEQSPNIVYTGATPNQQILPAIDWLLENLGKRFFLVGS
DYVFPRTANKIIRDQLKALGGEVVGEEYVPLGGTDFDAIVAKIKAFKPDVIVNTLNGDSNIAFFKQLAAA
GITASDLPVLSFSVSEAELRAIGPEELAGHYAAWNYFQSLDTPENQAFVEAFKAKYGADRVTSDPMEAAY
LGVYLWAQAVEKAGSFDPDAVRAALKGQSFEAPGGTVTVDPENHHLWKPVRIGKVQADGQFDIVWSS
>gnl|CDD|380579 cd06356, PBP1_amide_urea_BP-like, periplasmic component (FmdD) of an active transport system for short-chain amides and urea (FmdDEF). This group includes the type 1 periplasmic-binding proteins that are predicted to have a function similar to that of an active transport system for short chain amides and/or urea in bacteria and Archaea, by sequence comparison and phylogenetic analysis
KIGSIFDLSGGLNIYGKPMVHAMKLAVEEINAAGGLLGRQIELVAYDTQSDMQKYTQYAQQLILRDKVDV
VFGGITSASREAIRPILRRNKILYFYNTQYEGGVCDKNTFCTGSTPEQQVSPLIEWAIKKYGKKVYIIAA
DYNFGQISADWVKKYAKKNGGEVVGEEFFPLDVTDFGPTIQKIQAAKPDFVVSLLVGGNHISFYRQWAAA
GLKKKIPIVSTVFGAGNEHKVLSPPELEGMYVSYSYFEELDTPANKAFVAKWRAKYGDEPYINQEAVGVY
NAVYLWAEAVEKAGSTEREAVIAALESGISFDGPSGTVTVDPKSHHAIQNVYLA
>gnl|CDD|380580 cd06357, PBP1_AmiC, periplasmic binding domain of amidase (AmiC) that belongs to the type 1 periplasmic binding fold protein family. This group includes the periplasmic binding domain of amidase (AmiC) that belongs to the type 1 periplasmic binding fold protein family. AmiC controls expression of the amidase operon by the ligand-triggered conformational switch. In the absence of ligand or presence of butyramide (repressor), AmiC (the ligand sensor and negative regulator) adopts an open conformation and inhibits the transcription antitermination function of AmiR by direct protein-protein interaction. In the presence of inducing ligands such as acetamide, AmiC adopts a closed conformation which disrupts a silencing AmiC-AmiR complex and the expression of amidase and other genes of the operon are induced
RVGLLFSQTGVTAIIEQSMLNGALLAIEEINAAGGVNGRPIEPVVYDPASDPDRYRELAERLLLEDGVRH
IFGCYTSASRKAVLPVVERHNALLWYPTPYEGFEYSPNVIYTGAVPNQHLLPLARYLLAHFGKRVFLVGS
NYVYPWESNRVARELIEASGGEVVGERYVPLGDTDFAEIIEEIKSLKPDVVFSTLVGDSIYAFYRAYAEA
GLDPADMPIASLTTSEAEVAAIGAEAAAGHYTSAPYFQSIDTPENRAFVEAYRARFGDDAVTSAVAEAAY
FQVHLLARAIERAGSDDPEAIRAALYGQEFDAPQGPVRIDPDNNHTWLTPRIGRANADGQFDIVWESDEP
VAPDPYL
>gnl|CDD|380581 cd06358, PBP1_NHase, type 1 periplasmic-binding protein of the nitrile hydratase (NHase) system that selectively converts nitriles to corresponding amides. This group includes the type 1 periplasmic-binding protein of the nitrile hydratase (NHase) system that selectively converts nitriles to corresponding amides, which are subsequently converted by amidases to yield free carboxylic acids and ammonia. NHases from bacteria and fungi have been purified and characterized. In Rhodococcus sp., the nitrile hydratase operon consists of six genes encoding NHase regulator 2, NHase regulator 1, amidase, NHase alpha subunit, NHase beta subunit, and NHase activator. The operon produces a constitutive hydratase that has a broad substrate spectrum: aliphatic and aromatic nitriles, mononitriles and dinitriles, hydroxynitriles and amino-nitriles, and a constitutive amidase of equally low substrate specificity. NHases are metalloenzymes containing either cobalt or iron, and therefore can be classified into two subgroups: ferric NHases and cobalt NHases
RIGLLIPLSGPAGLWGPSCEACAELAAAEINAAGGILGREVELVLIDAGGPPAEVAAAARRLVDDGAVDA
IVGMHTSAVRQALANAVGGRVPYVYTPLYEGGERTPGVYAIGETPEEQLRPALRWLADERRVRRWFLVGN
DYVWPRASHAAARRYIARLGGEVVGERFVPLGEDDFERVLARIRASRPDAVLISLVGQDAVDFNRAFAAA
GLAGRILRLSPAIDENVLLAIGADATENLYSASGYFASLRTAANLAFLERYHAAFGDRAPPLNALGESCY
EGVHFLAALARRAGSLDVRALAAAAEGLTYESPRGAVTLRGRHARQPVYLARA
>gnl|CDD|380582 cd06359, PBP1_Nba-like, type 1 periplasmic binding component of active transport systems predicted to be involved in 2-nitrobenzoic acid degradation pathway. This group includes the type 1 periplasmic binding component of active transport systems that are predicted to be involved in 2-nitrobenzoic acid degradation pathway; their substrate specificities are not well characterized
KIGFITTLSGPAAVLGQDMRDGFNLALEQLGGKLGGLPVEVVVEDDQLKPDVAKQAAERLIERDKVDFVT
GIIFSNVMLAVVKPVVDSKVFYISANAGPSDLAGKGCNPNFFVTSWQNDQLHEAAGKYANDKGYKRVYLL
APNYQAGKDALAGFKRTYKGEVVGEIYTPLGQLDFSAELAQIRAAKPDAVFAFYPGGMGVNFVKQYAQAG
LKKKIPLYTVGTLDDEDLLPAMGDAALGVLSVSQWSPDLDNPENKRFVAAFRKKYGRPPSNYAAQGYDAA
LLIDAAVKAVGGDLSDKDALRAALRKADFKSVRGAFRFNNNQFPIQDFYLREV
>gnl|CDD|380583 cd06360, PBP1_alkylbenzenes-like, type 1 periplasmic binding component of active transport systems predicted be involved in anaerobic biodegradation of alkylbenzenes such as toluene and ethylbenzene. This group includes the type 1 periplasmic binding component of active transport systems that are predicted be involved in anaerobic biodegradation of alkylbenzenes such as toluene and ethylbenzene; their substrate specificity is not well characterized, however
KIGVLLPLTGPLAVNGEDVRDGFELYFDEIGNQVAGRKIELIVEDDEGKPDVGLTKARKLVERDKVHVLA
GIVSSAVAYAVRDYVVEQKIPLVISNAGAAPLTQELASPYIFRTSFSNGQYDAPFGQYAYEKLGYRRIAV
MASDYAAGHEQAGAFARTFKQAGGKVVQEIYPPLGTADFAPYLARIQQDAADAVWAFFAGADAIRFVKQY
DEYGLKGKLPLVGIGGLVDDAILPEQGDAALGIVSYLHYSAALDTPENKAFVQAYRKKYGRDPGLYAEGG
YVAARAIAEALEAVKGNVEDKEAFLEALRKVRFEAPRGPFRFDPYQQAVVTTYIRRVEKVDGKLVNVVID
RIPDVDQ
>gnl|CDD|380584 cd06361, PBP1_GPC6A-like, ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a broad-spectrum amino acid-sensing receptor. This family includes the ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a broad-spectrum amino acid-sensing receptor, and its fish homolog, the 5.24 chemoreceptor. GPRC6A is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into cellular responses
IIGGLFPIHEKVLDLHDRPTKPQIFICTGFDLRGFLQSLAMIHAIEMINNSTLLPGIKLGYEIYDTCSDV
TKALQATLRLLSKFNSSNELLECDYTDYVPPVKAVIGASYSEISIAVARLLNLQLIPQISYESSAPILSD
KLRFPSFLRTVPSDFHQTKAMAKLISHFGWNWVGIIYTDDDYGRSALESFIIQAEAENVCIAFKEVLPAY
LSDPTMNVRINDTIQTIQSSSQVNVVVLFLKPSLVKKLFKEVIERNISKIWIASDNWSTAREILKMPNIN
KVGKILGFTFKSGNISSFHNYLKNLLIYSIQLAVTAIANALRKLCCERGCQDPTAFQPWELLKELKKVTF
TDDGETYHFDANGDLNTGYDLILWKEDNGHMTFTIVAEYDLQNDVFIFTNN
>gnl|CDD|380585 cd06362, PBP1_mGluR, ligand binding domain of metabotropic glutamate receptors (mGluR). Ligand binding domain of the metabotropic glutamate receptors (mGluR), which are members of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into cellular responses. mGluRs bind to glutamate and function as an excitatory neurotransmitter; they are involved in learning, memory, anxiety, and the perception of pain. Eight subtypes of mGluRs have been cloned so far, and are classified into three groups according to their sequence similarities, transduction mechanisms, and pharmacological profiles. Group I is composed of mGlu1R and mGlu5R that both stimulate PLC hydrolysis. Group II includes mGlu2R and mGlu3R, which inhibit adenylyl cyclase, as do mGlu4R, mGlu6R, mGlu7R, and mGlu8R, which form group III
GDINLGGLFPVHERSSSGECCGEIREERGIQRLEAMLFAIDEINSRPDLLPNITLGFVILDDCSSDTTAL
EQALHFIRDSLLSQESAGFCQCSDDPPNLDESFQFYDVVGVIGAESSSVSIQVANLLRLFKIPQISYAST
SDELSDKERYPYFLRTVPSDSFQAKAIVDILLHFNWTYVSVVYSEGSYGEEGYKAFKKLARKAGICIAES
ERISQDSDEKDYDDVIQKLLQKKNARVVVLFADQEDIRGLLRAAKRLGASGRFIWLGSDGWGTNIDDLKG
NEDVALGALTVQPYSEEVPRFDDYFKSLTPSNNTRNPWFREFWQELFQCSFRPSRENSCNDDKLLINKSE
GYKQESKVSFVIDAVYAFAHALHKMHKDLCPGDTGLCQDLMKCIDGSELLEYLLNVSFTGEAGGEIRFDE
NGDGPGRYDIMNFQRNNDGSYEYVRVGVWDQYTQKLSLND
>gnl|CDD|380586 cd06363, PBP1_taste_receptor, ligand-binding domain of the T1R taste receptor. Ligand-binding domain of the T1R taste receptor. The T1R is a member of the family C receptors within the G-protein coupled receptor superfamily, which also includes the metabotropic glutamate receptors, GABAb receptors, the calcium-sensing receptor (CaSR), the V2R pheromone receptors, and a small group of uncharacterized orphan receptors
FRLPGDYLLGGLFPLHELTSTLPHRPPEPTDCSCDRFNLHGYHLAQAMRFAVEEINNSSDLLPGVTLGYE
IFDTCSDAVNFRPTLSFLSQNGSHDIEVQCNYTNYQPRVVAVIGPDSSELALTTAKLLGFFLMPQISYGA
SSEELSNKLLYPSFLRTVPSDKYQVEAMVQLLQEFGWNWVAFLGSDDEYGQDGLQLFSEKAANTGICVAY
QGLIPTDTDPKPKYQDILKKINQTKVNVVVVFAPKQAAKAFFEEVIRQNLTGKVWIASEAWSLNDTVTSL
PGIQSIGTVLGFAIQTGTLPGFQEFIYAFAFSVYAAVYAVAHALHNLLGCNSGACPKGRVVYPWQLLEEL
KKVNFTLLNQTIRFDENGDPNFGYDIVQWIWNNSSWTFEVVGSYSTYPIQLTINESKIKWHTKDSPVP
>gnl|CDD|380587 cd06364, PBP1_CaSR, ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors within the G-protein coupled receptor superfamily. Ligand-binding domain of the CaSR calcium-sensing receptor, which is a member of the family C receptors within the G-protein coupled receptor superfamily. CaSR provides feedback control of extracellular calcium homeostasis by responding sensitively to acute fluctuations in extracellular ionized Ca2+ concentration. This ligand-binding domain has homology to the bacterial leucine-isoleucine-valine binding protein (LIVBP) and a leucine binding protein (LBP). CaSR is widely expressed in mammalian tissues and is active in tissues that are not directly involved in extracellular calcium homeostasis. Moreover, CaSR responds to aromatic, aliphatic, and polar amino acids, but not to positively charged or branched chain amino acids, which suggests that changes in plasma amino acid levels are likely to modulate whole body calcium metabolism. Additionally, the family C GPCRs includes at least two receptors with broad-spectrum amino acid-sensing properties: GPRC6A which recognizes basic and various aliphatic amino acids, its gold-fish homolog the 5.24 chemoreceptor, and a specific taste receptor (T1R) which responds to aliphatic, polar, charged, and branched amino acids, but not to aromatic amino acids
IIGGLFPIHFRPVSPDPDFTTEPHSPECEGFNFRGFRWAQTMIFAIEEINNSPDLLPNITLGYRIYDSCA
TISKALRAALALVNGQEETNLDERCSGGPPVAAVIGESGSTLSIAVARTLGLFYIPQVSYFASCACLSDK
KQFPSFLRTIPSDYYQSRALAQLVKHFGWTWVGAIASDDDYGRNGIKAFLEEAEKLGICIAFSETIPRTY
SQEKILRIVEVIKKSTAKVIVVFSSEGDLEPLIKELVRQNITGRQWIASEAWITSSLLATPEYFPVLGGT
IGFAIRRGEIPGLKEFLLRVHPSKSPSNPFVKEFWEETFNCSLSSSSKSNSSSSSRPPCTGSENLENVQN
PYTDVSQLRISYNVYKAVYAIAHALHDLLQCEPGKGPFSNGSCADIKKVEPWQLLYYLKHVNFTTKFGEE
VYFDENGDPVASYDIINWQLSDDGTIQFVTVGYYDASAPSGEELVINESKILW
>gnl|CDD|380588 cd06365, PBP1_pheromone_receptor, Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within the G-protein coupled receptor superfamily. Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within the G-protein coupled receptor superfamily, which also includes the metabotropic glutamate receptor, the GABAb receptor, the calcium-sensing receptor (CaSR), the T1R taste receptor, and a small group of uncharacterized orphan receptors
IIGGVFPIHTFSEGKKKDFKEPPSPLLCFRFSIKYYQHLLAFLFAIEEINKNPDLLPNITLGFHIYDSCS
SERLALESSLSILSGNSEPIPNYSCREQRKLVAFIGDLSSSTSVAMARILGLYKYPQISYGAFDPLLSDK
VQFPSFYRTVPSDTSQSLAIVQLLKHFGWTWVGLIISDDDYGEQFSQDLKKEMEKNGICVAFVEKIPTNS
SLKRIIKYINQIIKSSANVIIIYGDTDSLLELLFRLWEQLVTGKVWITTSQWDISTLPFEFYLNLFNGTL
GFSQHSGEIPGFKEFLQSVHPSKYPEDIFLKTLWESYFNCKWPDQNCKSLQNCCGNESLETLDVHSFDMT
MSRLSYNVYNAVYAVAHALHEMLLCQPKTGPGNCSDRRNFQPWQLHHYLKKVQFTNPAGDEVNFDEKGDL
PTKYDILNWQIFPNGTGTKVKVGTFDPSAPSGQQLIINDSMIEW
>gnl|CDD|380589 cd06366, PBP1_GABAb_receptor, ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb receptor or GABAbR). GABAa receptors are members of the ionotropic receptor superfamily which includes alpha-adrenergic and glycine receptors. The GABAb receptor is a member of a receptor superfamily which includes the mGlu receptors. The GABAb receptor is coupled to G alpha-i proteins, and activation causes a decrease in calcium, an increase in potassium membrane conductance, and inhibition of cAMP formation. The response is thus inhibitory and leads to hyperpolarization and decreased neurotransmitter release, for example
YIGGLFPLSGSKGWWGGAGILPAAEMALEHINNRSDILPGYNLELIWNDTQCDPGLGLKALYDLLYTPPP
KVMLLGPGCSSVTEPVAEASKYWNLVQLSYAATSPALSDRKRYPYFFRTVPSDTAFNPARIALLKHFGWK
RVATIYQNDEVFSSTAEDLEELLEEANITIVATESFSSEDPTDQLENLKEKDARIIIGLFYEDAARKVFC
EAYKLGMYGPKYVWILPGWYDDNWWDVPDNDVNCTPEQMLEALEGHFSTELLPLNPDNTKTISGLTAQEF
LKEYLERLSNSNYTGSPYAPFAYDAVWAIALALNKTIEKLAEYNKTLEDFTYNDKEMADLFLEAMNSTSF
EGVSGPVSFDSKGDRLGTVDIEQLQGGSYVKVGLYDPNADSLLLLNESSIVWPG
>gnl|CDD|380590 cd06367, PBP1_iGluR_NMDA, N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptors. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptors. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. The function of the NMDA subtype receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer comprising two NR1 and two NR2 (A, B, C, and D) or NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain
PSVNIGAILGTKKEVAIKDEAEKDDFHHHFTLPVQLRVELVTMPEPDPKSIITRICDLLSDSKVQGVVFS
DDTDQEAIAQILDFIAAQTLTPVLGLHGRSSMIMADKSEHSMFLQFGPPIEQQASVMLNIMEEYDWYIVS
LVTTYFPGYQDFVNKLRSTIENSGWELEEVLQLDMSLDDGDSKLQAQLKKLQSPEARVILLYCTKEEATY
VFEVAASVGLTGYGYTWLVGSLVAGTDTVPAEFPTGLISLSYDEWYNLPARIRDGVAIVATAASEMLSEH
EQIPDPPSSCVNNQEIRKYTGPMLKRYLINVTFEGRDLSFSEDGYQMHPKLVIILLNNERKWERVGKWKD
SSLIMND
>gnl|CDD|380591 cd06368, PBP1_iGluR_non_NMDA-like, N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA (N-methyl-D-aspartate) subtypes of ionotropic glutamate receptors. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA (N-methyl-D-asparate) subtypes of ionotropic glutamate receptors. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Glutamate mediates the majority of excitatory synaptic transmission in the central nervous system via two broad classes of ionotropic receptors, characterized by their response to glutamate agonists: N-methyl-D-aspartate (NMDA) and non-NMDA receptors. NMDA receptors have intrinsically slow kinetics, are highly permeable to Ca2+, and are blocked by extracellular Mg2+ in a voltage-dependent manner. Non-NMDA receptors have faster kinetics, are most often only weakly permeable to Ca2+, and are not blocked by extracellular Mg2+. While non-NMDA receptors typically mediate excitatory synaptic responses at resting membrane potentials, NMDA receptors contribute several forms of synaptic plasticity and are thought to play an important role in the development of synaptic pathways. Non-NMDA receptors include alpha-amino-3-hydroxy-5-methyl-4-isoxazole proprionate (AMPA) and kainate receptors
KIGAIFNEVNDAHERAAFRYAVERLNTNIVKLAYFRITYSIEAIDSNSHFDATDKACDLLEKGVVAIVGP
SSSDSNNALQSICDALDVPHITVHDDPRLSKSQYSLSLYPRNQLSQAVSDLLKYWRWKRFVLVYDDDDRL
RRLQELLEAARFSKRFVSVRKVDLDYKTLDETPLLKRKDCSLFSRILIDLSPEKAYTFLLQALEMGMTIE
LYHYFLTTMDLSLLLDLELFRYNHANITGFQLVDNNSMYKEDINRLAFNWSRFRQHIKIESNLRGPPYEA
ALMFDAVLLLADAFRRTGDLRFNGTGLRSNFTLRILELGYGGLRKIGFWDSNTRLAMNL
>gnl|CDD|380592 cd06369, PBP1_GC_C_enterotoxin_receptor, ligand-binding domain of the membrane guanylyl cyclase C. Ligand-binding domain of the membrane guanylyl cyclase C (GC-C or StaR). StaR is a key receptor for the STa (Escherichia coli Heat Stable enterotoxin), a potent stimulant of intestinal chloride and bicarbonate secretion that cause acute secretory diarrhea. The catalytic domain of the STa/guanylin receptor type membrane GC is highly similar to those of the natriuretic peptide receptor (NPR) type and sensory organ-specific type membrane GCs (GC-D, GC-E and GC-F). The GC-C receptor is mainly expressed in the intestine of most vertebrates, but is also found in the kidney and other organs. Moreover, GC-C is activated by guanylin and uroguanylin, endogenous peptide ligands synthesized in the intestine and kidney. Consequently, the receptor activation results in increased cGMP levels and phosphorylation of the CFTR chloride channel and secretion
YTINVIMLNDSAFPWSLKNVKGAVNEGLEIVRARLAEAGLNVTINATFEYFNTTLYRSRGCRSSTCEGVE
KLKKLSNTGRLGCVVLGPTCTYATFQMYSVTFNLGYPLISAGSFGLSCDYKENLTRLLSPARKLMYFFVN
FWKENDFPFKTSSWRTAYVYKNQTNTEDCFWYLNALEAGVSYFSNKLRFKEVLRTEEELQKILMDQNRKS
NVIIMCGSPEDLKTLKGIRAVAEDIVIILVDLFNDVYFTNTTSPDYMKNVLVLTLPPTNSYSISPFSTDL
SLLNNDYAAAYLDGVLLFGHVLKKFLESNEAMQTMKFIHAFRNITFEGALGPVTLDSYGDRDVNLSLLYT
SVDTNKYKVLLTYDTHNNKTKPMDTSPTFIW
>gnl|CDD|380593 cd06370, PBP1_SAP_GC-like, Ligand-binding domain of membrane bound guanylyl cyclases. Ligand-binding domain of membrane bound guanylyl cyclases (GCs), which are known to be activated by sperm-activating peptides (SAPs), such as speract or resact. These ligand peptides are released by a range of invertebrates to stimulate the metabolism and motility of spermatozoa and are also potent chemoattractants. These GCs contain a single transmembrane segment, an extracellular ligand binding domain, and intracellular protein kinase-like and cyclase catalytic domains. GCs of insect and nematodes, which exhibit high sequence similarity to the speract receptor are also included in this model
ITIGYLTPYSGAGSYDRQGRVISGAITLAVDDVNNDPNLLPGHTLSFVWNDTRCDELLSIRAMTELWKRG
VSAFIGPGCTCATEARLAAAFNLPMISYKCADPEVSDKSLYPTFARTIPPDSQISKSVIALLKHFNWNKV
SIVYENETKWSKIADTIKELLELNNIEINHEEYFPDPYPYTTSHGNPFDKIVEETKEKTRIYVFLGDYSL
LREFMYYAEDLGLLDNGDYVVIGVELDQYDVDDPAKYPNFLSGDYTKNDTKEALEAFRSVLIVTPSPPTN
PEYEKFTKKVKEYNKLPPFNFPNPEGIEKTKEVPIYAAYLYDAVMLYARALNETLAEGGDPRDGTAIISK
IRNRTYESIQGFDVYIDENGDAEGNYTLLALKPNKGTNDGSYGLHPVGTF
>gnl|CDD|380594 cd06371, PBP1_sensory_GC_DEF-like, ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are specifically expressed in sensory tissues. This group includes the ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are specifically expressed in sensory tissues. They share a similar topology with an N-terminal extracellular ligand-binding domain, a single transmembrane domain, and a C-terminal cytosolic region that contains kinase-like and catalytic domains. GC-D is specifically expressed in a subpopulation of olfactory sensory neurons. GC-E and GC-F are colocalized within the same photoreceptor cells of the retina and have important roles in phototransduction. Unlike the other family members, GC-E and GC-F have no known extracellular ligands. Instead, they are activated under low calcium conditions by guanylyl cyclase activating proteins called GCAPs. GC-D expressing neurons have been implicated in pheromone detection and GC-D is phylogenetically more similar to the Ca2+-regulated GC-E and GC-F than to receptor GC-A, -B and -C which are activated by peptide ligands. Moreover, these olfactory GCs and retinal GCs share characteristic sequence similarity in a regulatory domain that is involved in the binding of GCAPs, suggesting GC-D activity may be regulated by an unknown extracellular ligand and intracellular Ca2+. Rodent GC-D-expressing neurons have been implicated in pheromone detection and were recently shown to respond to atmospheric CO2 which is an olfactory stimulus for many invertebrates and regulates some insect innate behavior, such as the location of food and hosts
KVGVVGPWTCDPIFAKALPDLAARLAVSRINKDPSLDLGYWFDYVILPEDCETSKALAAFSSAEGRASGF
VGPVNPGYCEAASLLAQEWDKALFSWGCVNHELNSYPTFARTLPPPADVLYTVLRYFRWAHVAVVSSPQD
LWVETGRELASALRARGLPVGLVTSMEPSDSGAREALKRIRDADRVRVVIMCMHSVLIGGEEQRTLLEAA
HDMGLTDGSYVFVPYDTLLYSLPYKHEPYAVLRNNSKLRRAYDAVLTITMESPEGSFYEAFRRAQERGEL
PSDLDPEQVSPLFGTIYNSIYLLAGAVENARAAGGGVSGASLARHARNAQFPGFNQLLRTDSGGNGQPSY
VILDTDGKGWRLFPTYTLDMTTGLLRFLG
>gnl|CDD|380595 cd06372, PBP1_GC_G-like, Ligand-binding domain of membrane guanylyl cyclase G. This group includes the ligand-binding domain of membrane guanylyl cyclase G (GC-G) which is a sperm surface receptor and might function, similar to its sea urchin counterpart, in the early signaling event that regulates the Ca2+ influx/efflux and subsequent motility response in sperm. GC-G appears to be a pseudogene in human. Furthermore, in contrast to the other orphan receptor GCs, GC-G has a broad tissue distribution in rat, including lung, intestine, kidney, and skeletal muscle
TVGFQAPWNLSHPFSAQRLGSAIQLAVDKVNSEPSLLGNYSLDFVYTDCGCNAKESLGAFIDQVQKENIS
ALFGPACPEAAEVTGLLASEWNIPMFGFVGQSPKLDDRDVYDTYVKLVPPLQRIGEVLVKTLQFFGWTHV
AMFGGSSATSTWDKVDELWKSVENQLKFNFNVTAKVKYDTSNPDLLQENLRYISSVARVIVLICSSEDAR
SILLEAEKLGLMDGEYVFFLLQQFEDSFWKEVLNDEKNQVFLKAYEMVFLIAQSSYGTYGYSDFRKQVHQ
KLRRAPFYSSISSEDQVSPYSAYLHDAVLLYAMGLKEMLKDGKDPRDGRALLQTLRGYNQTTFYGITGLV
YLDVQGERHMDYSVYDLQKSGNQSLFVPVLHYDSFQKTIR
>gnl|CDD|380596 cd06373, PBP1_NPR-like, Ligand binding domain of natriuretic peptide receptor (NPR) family. Ligand binding domain of natriuretic peptide receptor (NPR) family which consists of three different subtypes: type A natriuretic peptide receptor (NPR-A, or GC-A), type B natriuretic peptide receptors (NPR-B, or GC-B), and type C natriuretic peptide receptor (NPR-C). There are three types of natriuretic peptide (NP) ligands specific to the receptors: atrial NP (ANP), brain or B-type NP (BNP), and C-type NP (CNP). The NP family is thought to have arisen through gene duplication during evolution and plays an essential role in cardiovascular and body fluid homeostasis. ANP and BNP bind mainly to NPR-A, while CNP binds specifically to NPR-B. Both NPR-A and NPR-B have guanylyl cyclase catalytic activity and produces intracellular secondary messenger cGMP in response to peptide-ligand binding. Consequently, the NPR-A activation results in vasodilation and inhibition of vascular smooth muscle cell proliferation. NPR-C acts as the receptor for all the three members of NP family, and functions as a clearance receptor. Unlike NPR-A and -B, NPR-C lacks an intracellular guanylyl cyclase domain and is thought to exert biological actions by sequestration of released natriuretic peptides and/or inhibition of adenylyl cyclase
TLAVLLPQDDSYPFSLAKVLPAIELALRRVERRGFLPGWRFQVHYRDTKCSDTLAPLAAVDLYCAKKVDV
FLGPVCEYALAPVARYAGHWNVPVLTAGGLAAGFDDKTEYPLLTRMGGSYVKLGEFVLTLLRHFGWRRVA
LLYHDNLRRKAGNSNCYFTLEGIFNALTGERDSIHKSFDEFDETKDDFEILLKRVSNSARIVILCASPDT
VREIMLAAHELGMINGEYVFFNIDLFSSSSKGARPWYRENDTDERNEKARKAYRALLTVTLRRPDSPEYR
NFSEEVKERAKEKYNYFTYGDEEVNSFVGAFHDAVLLYALALNETLAEGGSPRNGTEITERMWNRTFEGI
TGNVSIDANGDRNADYSLLDMNPVTGKFEVVANYFGNSKQLEPV
>gnl|CDD|380597 cd06374, PBP1_mGluR_groupI, ligand binding domain of the group I metabotropic glutamate receptor. Ligand binding domain of the group I metabotropic glutamate receptor, a family containing mGlu1R and mGlu5R, all of which stimulate phospholipase C (PLC) hydrolysis. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes
RLVARMPGDIIIGALFPVHHQPPLKKVFSRKCGEIREQYGIQRVEAMFRTLDKINKDPNLLPNITLGIEI
RDSCWYSPVALEQSIEFIRDSVASVEDEKDTQNTPDPTPLSPPENRKPIVGVIGPGSSSVTIQVQNLLQL
FHIPQIGYSATSIDLSDKSLYKYFLRVVPSDYLQARAMLDIVKRYNWTYVSTVHTEGNYGESGIEAFKEL
AAEEGICIAHSDKIYSNAGEEEFDRLLRKLMNTPNKARVVVCFCEGETVRGLLKAMRRLNATGHFLLIGS
DGWADRKDVVEGYEDEAAGGITIKIHSPEVESFDEYYFNLKPETNSRNPWFREFWQHRFDCRLPGHPDEN
PYFKKCCTGEESLLGNYVQDSKLGFVINAIYAMAHALHRMQEDLCGGYSVGLCPAMLPINGSLLLDYLLN
VSFVGVSGDTIMFDENGDPPGRYDIMNFQKTGEGSYDYVQVGSWKNGSLKMDDE
>gnl|CDD|380598 cd06375, PBP1_mGluR_groupII, ligand binding domain of the group II metabotropic glutamate receptor. Ligand binding domain of the group II metabotropic glutamate receptor, a family that contains mGlu2R and mGlu3R, all of which inhibit adenylyl cyclase. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes
IKLEGDLVLGGLFPVHEKGEGMEECGRINEDRGIQRLEAMLFAIDRINRDPHLLPGVRLGVHILDTCSRD
TYALEQSLEFVRASLTKVDDSEYMCPDDGSYAIQEDSPLPIAGVIGGSYSSVSIQVANLLRLFQIPQISY
ASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRNICI
ATAEKVGRSADRKSFDGVIRELLQKPNARVVVLFTRSDDARELLAAAKRLNASFTWVASDGWGAQESIVK
GSEDVAEGAITLELASHPIPDFDRYFQSLTPYNNHRNPWFRDFWEQKFQCSLQNKSQAASVSDKHLSIDS
SNYEQESKIMFVVNAVYAMAHALHNMQRTLCPNTTRLCDAMRSLDGKKLYKDYLLNVSFTAPFPPADAGS
EVKFDAFGDGLGRYNIFNYQRAGGSYGYRYKGVGKWANSLDL
>gnl|CDD|380599 cd06376, PBP1_mGluR_groupIII, ligand-binding domain of the group III metabotropic glutamate receptor. Ligand-binding domain of the group III metabotropic glutamate receptor, a family which contains mGlu4R, mGluR6R, mGluR7, and mGluR8; all of which inhibit adenylyl cyclase. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes
IRVEGDITLGGLFPVHARGLAGVPCGEIKKEKGIHRLEAMLYALDQINSDPDLLPNVTLGARILDTCSRD
TYALEQSLTFVQALIQKDTSDVRCTNGDPPVFVKPEKVVGVIGASASSVSIMVANILRLFQIPQISYAST
APELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGNYGEKGVESFVQISREAGGVCIAQ
SEKIPRERRTGDFDKIIKRLLETPNARAVVIFADEDDIRRVLAAAKRANKTGHFLWVGSDSWGAKISPVL
QQEDVAEGAITILPKRASIEGFDAYFTSRTLENNRRNVWFAEFWEENFNCKLTSSGSKKEDTLRKCTGQE
RIGRDSGYEQEGKVQFVVDAVYAMAHALHNMNKDLCPGYRGLCPEMEPAGGKKLLKYIRNVNFNGSAGTP
VMFNKNGDAPGRYDIFQYQTTNGSNYGYRLIGQWTDELQLNIEDMQW
>gnl|CDD|380600 cd06377, PBP1_iGluR_NMDA_NR3, N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR3 subunit of NMDA receptor family. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NR3 subunit of NMDA receptor family. The ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer composed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain
VLKRIGHTVRLGALLPHPWFTRGRAGAALAVDLPTGLLPYNLSLEVVVAAPWARDPASLTRSLCHSVVVQ
GVAALLAFPQSRGELLQLDFLSAALEIPVVSILRREFPRPLRSQNPFHLQLDLQSSLESLEDVLVSLLQA
NSWEDVSLLLCQPWDPTSFLLLWQNNSQFHLGTVLNLSVLDESDLQRSLQQHLESLKDPSPAIVMFGCDA
ARARRVFEAAPPGGLPEFHWLLGTPLPVEELPTEGLPPGLLALGETSRPSLEAYVQDAVELVARALSSAA
LVHPELALLPATVNCNDLKTGGSESSGQYLSRFLANTSFQGRTGTVWVTGSSQVHSERHFKVWSLRRDPL
GAPTWATVGSWQDGKLDMEPGAW
>gnl|CDD|380601 cd06378, PBP1_iGluR_NMDA_NR2, N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR2 subunit of NMDA receptor family. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NR2 subunit of NMDA receptor family. The ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer composed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain
PSLNIAVILPGTSFEVRIRSRLEPDAFHGLPFEVSPITVLMNDTNPKSILTQICDLLSGRKVHGIVFEDD
TDQEAVAQILDFISLQTYLPILGISGGSANVLLDKEEGSTFLQLGPSIEQQATVMLNILEEYDWHQFSVV
TSLFPGYRDFVDAIRSTIDNSFVGWELQDVLTLDMSNDGSDAKTLRQLKKIEAQVILLYCTKEEAQYIFE
AAEEAGLTGYGYVWIVPSLVLGNTDPPPAEFPVGLISVHFDTWDYSLRARVRDGVAIIATGAEAMLSEHG
FLPEPKSDCYAPNETREPANETLHRYLINVTWEGRDLSFNEDGYLVNPELVIINLNRERLWEKVGKWESG
SLQMKY
>gnl|CDD|380602 cd06379, PBP1_iGluR_NMDA_NR1, N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor. The ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer ccomposed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. When co-expressed with NR1, the NR3 subunits form receptors that are activated by glycine alone and therefore can be classified as excitatory glycine receptors. NR1/NR3 receptors are calcium-impermeable and unaffected by ligands acting at the NR2 glutamate-binding site
KIFNIGAVLSSPKHEEIFREAVNEVNAHSHLPRKITLNATSITLDPNPIRTALSVCEDLIASQVYAVIVS
HPPTPSDLSPTSVSYTAGFYRIPVIGISARDSAFSDKNIHVSFLRTVPPYSHQADVWAEMLRHFEWKQVI
VIHSDDQDGRALLGRLETLAETKDIKIEKVIEFEPGEKNFTSLLEEMKELQSRVILLYASEDDAEIIFRD
AAMLNMTGAGYVWIVTEQALAASNVPDGVLGLQLIHGKNESAHIRDSVSVVAQAIRELFRSSENITDPPV
DCRDDTNIWKSGQKFFRVLKSVKLSDGRTGRVEFNDKGDRIGAEYDIINVQNPRKLVQVGIYVGSQRPTK
SLLSLNDRKIIWPG
>gnl|CDD|380603 cd06380, PBP1_iGluR_AMPA, N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor, a member of the glutamate-receptor ion channels (iGluRs). AMPA receptors are the major mediators of excitatory synaptic transmission in the central nervous system. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. AMPA receptors consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important roles in mediating the rapid excitatory synaptic current
PIGAIFDSGEDQVQTAFRYAIDRHNSNNNNRFRLFPLTERIDITNADSFSVSRAICSQLSRGVFAIFGSS
DASSLNTIQSYSDTFHMPYITPSFPKNEPSDSNPFELSLRPSYIEAIVDLIRHYGWKKVVYLYDSDEGLL
RLQQLYDYLKEKSNISVRVRRVRNVNDAYEFLRTLRELDREKEDKRIVLDLSSERYQKILEQIVEDGMNR
RNYHYLLANLDFLDLDLERFLHGGVNITGFQLVDTNNKTVKDFLQRWKKLDPREYPGAGTDTIPYEAALA
VDAVLVIAEAFQSLLRQNDDIFRFTFHGELYNNGSKGIDCDPNPPLPWEHGKAIMKALKKVRFEGLTGNV
QFDDFGQRKNYTLDVIELTSNRGLRKIGTWSEGDGFLLGE
>gnl|CDD|380604 cd06381, PBP1_iGluR_delta-like, N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of an orphan family of delta receptors, GluRdelta1 and GluRdelta2. This CD represents the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of an orphan family of delta receptors, GluRdelta1 and GluRdelta2. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Although the delta receptors are a member of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetic analysis shows that both GluRdelta1 and GluRalpha2 are more homologous to non-NMDA receptors. GluRdelta2 was shown to function as an AMPA-like receptor by mutation analysis. Moreover, targeted disruption of GluRdelta2 gene caused motor coordination impairment, Purkinje cell maturation, and long-term depression of synaptic transmission. It has been suggested that GluRdelta2 is the receptor for cerebellin 1, a glycoprotein of the Clq, and the tumor necrosis factor family which is secreted from cerebellar granule cells. Furthermore, recent studies have shown that the orphan GluRdelta1 plays an essential role in high-frequency hearing and ionic homeostasis in the basal cochlea and that the locus encoding GluRdelta1 may be involved in congenial or acquired high-frequency hearing loss in humans
HIGAIFEENAAKDDRVFQLAVSDLSLNDDILQSEKITYSIKVIEANNPFQAVQEACDLMTQGILALVTST
GCASANALQSLTDAMHIPHLFVQRNPGGSPRTACHLNPSPDGEAYTLASRPPVRLNDVMLRLVTELRWQK
FVMFYDSEYDIRGLQSFLDQASRLGLDVSLQKVDKNISHVFTSLFTTMKTEELNRYRDTLRRAILLLSPQ
GAHSFINEAVETNLASKDSHWVFVNEEISDPEILDLVHSALGRMTVVRQIFPSAKDNQKCFRNNHRISSL
LCDPQEGYLQMLQISNLYLYDSVLMLANAFHRKLEDRKWHSMASLNCIRKSTKPWNGGRSMLDTIKKGHI
TGLTGVMEFREDSSNPYVQFEILGTTYSETFGKDMRKLATWDSEKGLNGSL
>gnl|CDD|380605 cd06382, PBP1_iGluR_Kainate, N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate receptors. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate receptors, non-NMDA ionotropic receptors which respond to the neurotransmitter glutamate. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Kainate receptors have five subunits, GluR5, GluR6, GluR7, KA1 and KA2, which are structurally similar to AMPA and NMDA subunits of ionotropic glutamate receptors. KA1 and KA2 subunits can only form functional receptors with one of the GluR5-7 subunits. Moreover, GluR5-7 can also form functional homomeric receptor channels activated by kainate and glutamate when expressed in heterologous systems. Kainate receptors are involved in excitatory neurotransmission by activating postsynaptic receptors and in inhibitory neurotransmission by modulating release of the inhibitory neurotransmitter GABA through a presynaptic mechanism. Kainate receptors are closely related to AMAP receptors. In contrast of AMPA receptors, kainate receptors play only a minor role in signaling at synapses and their function is not well defined
RIGGIFDEDDEDLEIAFKYAVDRINRERTLPNTKLVPDIERVPRDDSFEASKKVCELLEEGVAAIFGPSS
PSSSDIVQSICDALEIPHIETRWDPKESNRDTFTINLYPDPDALSKAYADLVKSLNWKSFTILYEDDEGL
IRLQELLKLPKPKDIPITVRQLDPGDDYRPVLKEIKKSGETRIILDCSPDRLVDVLKQAQQVGMLTEYYH
YILTNLDLHTLDLEPFKYSGANITGFRLVDPENPEVKNVLKDWSKREKEGFNKDIGPGQITTETALMYDA
VNLFANALKEGLTGPIKFDEEGQRTDFKLDILELTEGGLVKVGTWNPTDGLNITR
>gnl|CDD|380606 cd06383, PBP1_iGluR_AMPA_Like, N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of uncharacterized AMPA-like receptors. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of uncharacterized AMPA-like receptors. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. AMPA receptors consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important roles in mediating the rapid excitatory synaptic current
NILIINEEDNSLANKAFKAAQSYLKKNPTLGLVLGNVIVVTNNGSDAKVTLDKVCSEYDTSIDAKKPPHI
VLDTTMSGVSSETVKSFTRALGLPTISASYGQEGDLRQWRNLDPNQKKYLVQVMPPADIIPEAIRSIVSM
QNITNAAILFDDSFVMDHKYKSLLQNIPTRHVITKIKTDGKEIRNQLRRLRDLDIVNFFVLGRMDTIKKV
LDAAAKKNYFGRKYAWYAITKDEGNISCGCKNASIVFVKPTPNTGNRDRLSLLKTTYSLNGTPELDSAFY
FDLFLRTFLAIKSMLKGGKWPDDMEYITCDEYNETNTPVRNLLDLRKAFTEVSMTPTFAPQMILKSNGHS
YMQFEMDINAVNIKNGRSVSSKELGTWKA
>gnl|CDD|380607 cd06384, PBP1_NPR_B, ligand-binding domain of type B natriuretic peptide receptor. Ligand-binding domain of type B natriuretic peptide receptor (NPR-B). NPR-B is one of three known single membrane-spanning natriuretic peptide receptors that have been identified. Natriuretic peptides are family of structurally related but genetically distinct hormones/paracrine factors that regulate blood volume, blood pressure, ventricular hypertrophy, pulmonary hypertension, fat metabolism, and long bone growth. In mammals there are three natriuretic peptides: ANP, BNP, and CNP. Like NPR-A (or GC-A), NPR-B (or GC-B) is a transmembrane guanylyl cyclase, an enzyme that catalyzes the synthesis of cGMP. NPR-B is the predominant natriuretic peptide receptor in the brain. The rank of order activation of NPR-B by natriuretic peptides is CNP__ANP_BNP. Homozygous inactivating mutations in human NPR-B cause a form of short-limbed dwarfism known as acromesomelic dysplasia type Maroteaux
TVAVVLPENNLSYAWAWPRVFPALRMAVDALQRKGKLLRGYTVNLLFHSSELQGACSEYVAPLMAVDLKL
YHDPDVLFGPGCVYPAASVGRFASHWRLPLITAGAVAFGFSSKDEHYRTTVRTGPSAPKLGEFVSHLHSH
FNWTSRAALLYHDLKTDDRPYYFIIEGVFLALDGENLTVEHVPYDDQENGDPREAIHFIKANGRIVYICG
PLEMLHEIMLQAQRENLTNGDYVFFYLDVFGESLRDDDTRPAEKPSSDIQWQDLREAFKTVLVITYKEPD
NPEYQEFQRELIARAKQEFGVQLNPSLMNLIAGCFYDGVLLYAQALNETLREGGSQKDGLNIVEKMQDRR
FWGVTGLVSMDKNNDRDTDFNLWAMTDHESGQYEVVAHYNGAEKQIVWT
>gnl|CDD|380608 cd06385, PBP1_NPR_A, Ligand-binding domain of type A natriuretic peptide receptor. Ligand-binding domain of type A natriuretic peptide receptor (NPR-A). NPR-A is one of three known single membrane-spanning natriuretic peptide receptors that regulate blood volume, blood pressure, ventricular hypertrophy, pulmonary hypertension, fat metabolism, and long bone growth. In mammals there are three natriuretic peptides: ANP, BNP, and CNP. NPR-A is highly expressed in kidney, adrenal, terminal ileum, adipose, aortic, and lung tissues. The rank order of NPR-A activation by natriuretic peptides is ANP_BNP__CNP. Single allele-inactivating mutations in the promoter of human NPR-A are associated with hypertension and heart failure
TLAVVLPLTNTSYPWAWPRVGPAVELALERVNARPDLLPGWHVRTVLGSSENKEGVCSDSTAPLVAVDLK
FEHHPAVFLGPGCVYTAAPVARFTAHWRVPLLTAGAPALGFGVKDEYALTTRTGPSHKKLGEFVARLHRR
YGWERRALLVYADRKGDDRPCFFAVEGLYMQLRRRLNITVDDLVFNEDEPLNYTELLRDIRQKGRVIYVC
CSPDTFRKLMLQAWREGLCGEDYAFFYIDIFGASLQSGQFPDPQRPWERGDADDNSAREAFQAVKIITYK
EPDNPEYKEFLKQLKTEAMEMFNFTVEDGLMNLIAASFHDGVLLYAHAVNETLAHGGTVTNGSAITQRMW
NRSFYGVTGYVKIDENGDRETDFSLWDMDPETGAFQIVSNYNGTSKELMAVPGRKIHW
>gnl|CDD|380609 cd06386, PBP1_NPR_C, ligand-binding domain of type C natriuretic peptide receptor. Ligand-binding domain of type C natriuretic peptide receptor (NPR-C). NPR-C is found in atrial, mesentery, placenta, lung, kidney, venous tissue, aortic smooth muscle, and aortic endothelial cells. The affinity of NPR-C for natriuretic peptides is ANP_CNP_BNP. The extracellular domain of NPR-C is about 30% identical to NPR-A and NPR-B. However, unlike the cyclase-linked receptors, it contains only 37 intracellular amino acids and no guanylyl cyclase activity. Major function of NPR-C is to clear natriuretic peptides from the circulation or extracellular surroundings through constitutive receptor-mediated internalization and degradation
QKIEVLVLLPKDNSYLFSLTRVRPAIEYALRSVEGNGLLPPGTRFNVAYEDSDCGNRALFSLVDRVAQKR
AKPDLILGPVCEYAAAPVARLASHWNLPMLSAGALAAGFSHKDSEYSHLTRVAPAYAKMGEMFLALFRHH
HWSRAFLVYSDDKLERNCYFTLEGVHEVFQEEGLHTSIYSFDETKDLDLEEIVRNIQASERVVIMCASSD
TIRSIMLVAHRHGMTNGDYAFFNIELFNSSSYGNGSWKRGDKHDFEAKQAYSSLQTVTLLRTVKPEFEKF
SMEVKSSVQKQGLNDEDYVNMFVEGFHDAILLYALALHEVLRNGYSKKDGGKIIQQTWNRTFEGIAGQVS
IDANGDRYGDFSVIAMTDVEAGTQEVIGDYFGKEGRFEMRP
>gnl|CDD|380610 cd06387, PBP1_iGluR_AMPA_GluR3, N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR3 subunit of the AMPA receptor. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR3 subunit of the AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor. The AMPA receptor is a member of the glutamate-receptor ion channels (iGluRs) which are the major mediators of excitatory synaptic transmission in the central nervous system. AMPA receptors are composed of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current. Furthermore, this N-terminal domain of the iGluRs has homology with LIVBP, a bacterial periplasmic binding protein, as well as with the structurally related glutamate-binding domain of the G-protein-coupled metabotropic receptors (mGluRs)
SIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGF
YDQMSMNTLTSFCGALHTSFITPSFPTDADVQFVIQMRPALKGAILSLLAHYKWEKFVYLYDTERGFSIL
QAIMEAAVQNNWQVTARSVGNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYH
YMLANLGFTDILLERVMHGGANITGFQIVNNENPMVQQFLQRWVRLDEREFPEAKNAPLKYTSALTHDAI
LVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTID
VYEMKPSGSRKAGYWNEYERFVPFS
>gnl|CDD|380611 cd06388, PBP1_iGluR_AMPA_GluR4, N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR4 subunit of the AMPA receptor. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR4 subunit of the AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor. The AMPA receptor is a member of the glutamate-receptor ion channels (iGluRs) which are the major mediators of excitatory synaptic transmission in the central nervous system. AMPA receptors are composed of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current. Furthermore, this N-terminal domain of the iGluRs has homology with LIVBP, a bacterial periplasmic binding protein, as well as with the structurally related glutamate-binding domain of the G-protein-coupled metabotropic receptors (mGluRs)
QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGL
YDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNRFVFLYDTDRGYSIL
QAIMEKAGQNGWQVSAICVENFNDASYRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHY
IIANLGFKDISLERFMHGGANVTGFQLVDFNTPMVTKLMQRWKKLDQREYPGSETPPKYTSALTYDGVLV
MAETFRNLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVF
ELKSTGPRKVGYWNDMDKLVLIQ
>gnl|CDD|380612 cd06389, PBP1_iGluR_AMPA_GluR2, N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit of the AMPA receptor. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit of the AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor. The AMPA receptor is a member of the glutamate-receptor ion channels (iGluRs) which are the major mediators of excitatory synaptic transmission in the central nervous system. AMPA receptors are composed of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current. Furthermore, this N-terminal domain of the iGluRs has homology with LIVBP, a bacterial periplasmic binding protein, as well as with the structurally related glutamate-binding domain of the G-protein-coupled metabotropic receptors (mGluRs)
QIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSV
NTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDS
AAEKKWQVTAINVGNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYII
ANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYTSALTYDAVQVM
TEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIME
LKTNGPRKIGYWSEVDKMVVTL
>gnl|CDD|380613 cd06390, PBP1_iGluR_AMPA_GluR1, N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit of the AMPA receptor. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit of the AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor. The AMPA receptor is a member of the glutamate-receptor ion channels (iGluRs) which are the major mediators of excitatory synaptic transmission in the central nervous system. AMPA receptors are composed of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current. Furthermore, this N-terminal domain of the iGluRs has homology with LIVBP, a bacterial periplasmic binding protein, as well as with the structurally related glutamate-binding domain of the G-protein-coupled metabotropic receptors (mGluRs)
QIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYTFCSQFSKGVYAIFGFYERRTVN
MLTSFCGALHVCFITPSFPVDTSNQFVLQLRPELQDALISVIEHYKWQKFVYIYDADRGLSVLQKVLDTA
AEKNWQVTAVNILTTTEEGYRMLFQDLDKKKERLVVVDCESERLNAILGQIVKLEKNGIGYHYILANLGF
MDIDLTKFKESGANVTGFQLVNYTDTIPARIMQQWKNSDSRDLPRVDWKRPKYTSALTYDGVKVMAEAFQ
SLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDG
IRKIGYWNEDDKLVPAA
>gnl|CDD|380614 cd06391, PBP1_iGluR_delta_2, N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 receptor of an orphan glutamate receptor family. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 receptor of an orphan glutamate receptor family. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Although the delta receptors are a member of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetic analysis shows that both GluRdelta1 and GluRalpha2 are closer related to non-NMDA receptors. GluRdelta2 was shown to function as an AMPA-like receptor by mutation analysis. Moreover, targeted disruption of GluRdelta2 gene caused motor coordination impairment, Purkinje cell maturation, and long-term depression of synaptic transmission. It has been suggested that GluRdelta2 is the receptor for cerebellin 1, a glycoprotein of the Clq and tumor necrosis factor family that is secreted from cerebellar granule cells
HIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSI
GCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNDVILRVVTEYAWQK
FIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPA
TAKSFITEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISS
SLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKWHSMASLSCIRKNSKPWQGGRSMLETIKKGG
VSGLTGLLEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNGSL
>gnl|CDD|380615 cd06392, PBP1_iGluR_delta_1, N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta1 receptor of an orphan glutamate receptor family. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta1 receptor of an orphan glutamate receptor family. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Although the delta receptors are a member of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetic analysis shows that both GluRdelta1 and GluRalpha2 may be closer related to non-NMDA receptors. In contrast to GluRdelta2, GluRdelta1 is expressed in many areas in the developing CNS, including the hippocampus and the caudate putamen. Furthermore, recent studies have shown that the orphan GluRdelta1 plays an essential role in high-frequency hearing and ionic homeostasis in the basal cochlea and that the locus encoding GluRdelta1 may be involved in congenial or acquired high-frequency hearing loss in humans
HIGAIFEENAAKDDRVFQLAVSDLSLNDDILQSEKITYSIKVIEANNPFQAVQEACDLMTQGILALVTST
GCASANALQSLTDAMHIPHLFVQRNSGGSPRTACHLNPSPEGEEYTLAARPPVRLNDVMLKLVTELRWQK
FIVFYDSEYDIRGLQSFLDQASRLGLDVSLQKVDRNISRVFTNLFTTMKTEELNRYRDTLRRAILLLSPR
GAQSFINEAVETNLASKDSHWVFVNEEISDPEILELVHSALGRMTVIRQIFPLSKDNNQRCMRNNHRISS
LLCDPQEGYLQMLQVSNLYLYDSVLMLANAFHRKLEDRKWHSMASLNCIRKSTKPWNGGRSMLDTIKKGH
ITGLTGVMEFREDGANPYVQFEILGTSYSETFGKDVRRLATWDSEKGLNGSL
>gnl|CDD|380616 cd06394, PBP1_iGluR_Kainate_KA1_2, N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 subunits of Kainate receptor. N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 subunits of Kainate receptor. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. There are five types of kainate receptors, GluR5, GluR6, GluR7, KA1, and KA2, which are structurally similar to AMPA and NMDA subunits of ionotropic glutamate receptors. KA1 and KA2 subunits can only form functional receptors with one of the GluR5-7 subunits. Moreover, GluR5-7 can also form functional homomeric receptor channels activated by kainate and glutamate when expressed in heterologous systems. Kainate receptors are involved in excitatory neurotransmission by activating postsynaptic receptors and in inhibitory neurotransmission by modulating release of the inhibitory neurotransmitter GABA through a presynaptic mechanism. Kainate receptors are closely related to AMPA receptors. In contrast of AMPA receptors, kainate receptors play only a minor role in signaling at synapses and their function is not well defined
SLRMAAILDDQTVCGRGERLALALAREQINSIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVS
VLGPSSSPASASTVSHICGEKEIPHIKVGPEETPRLQYLRFASVSLYPSNEDISLAVSRILKSFNYPSAS
LICAKAECLLRLEELVRQFLISKETLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLILKKASE
LGMTSAFYKYILTTMDFPLLHLDGIVDDQSNILGFSMFNTSHPFYLEFVRSLNMSWRENCDASTYPGPAL
SSALMFDAVHVVVSAVRELNRSQEIGVKPLSCTSAQIWQHGTSLMNYLRMVEYDGLTGRVEFNSKGQRTN
YTLRILEKSRQGHREIGVWYSNRTLAMNA
>gnl|CDD|99717 cd06395, PB1_Map2k5, PB1 domain is essential part of the mitogen-activated protein kinase kinase 5 (Map2k5, alias MEK5) one of the key member of the signaling kinases cascade which involved in angiogenesis and early cardiovascular development. The PB1 domain of Map2k5 interacts with the PB1 domain of another members of kinase cascade MEKK2 (or MEKK3). A canonical PB1-PB1 interaction, involving heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. The Map2k5 protein contains a type I PB1 domain
LVIRIKIPNGGAVDWTVQSGPQLLFRDVLDVIGQVLPEATTTAFEYEDEDGDRITVRSDEEMKAMLSYYC
STVMEQQVNGQLIEPLQIFPR
>gnl|CDD|99718 cd06396, PB1_NBR1, The PB1 domain is an essential part of NBR1 protein, next to BRCA1, a scaffold protein mediating specific protein-protein interaction with both titin protein kinase and with another scaffold protein p62. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. The NBR1 protein contains a type I PB1 domain
VNLKVTYNGESQSFLVSDSENTTWASVEAMVKVSFGLNDIQIKYVDEENEEVSVNSQGEYEEALKSAVRQ
GNLLQMNVYEH
>gnl|CDD|99719 cd06397, PB1_UP1, Uncharacterized protein 1. The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions
TQFKSSFLGDTRRIVFPDIPTWEALASKLENLYNLPEIKVGVTYIDNDNDEITLSSNKELQDFYRLSHRE
STEVIKLNVNDL
>gnl|CDD|99720 cd06398, PB1_Joka2, The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with sulfur stress inducible UP9 protein. The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants
LVVKVKYGGTLRRFTFPVAENQLDLNMDGLREKVEELFSLSPDADLSLTYTDEDGDVVTLVDDNDLTDAI
QYFCSGSRLNPLRIDVTVDYD
>gnl|CDD|99721 cd06399, PB1_P40, The PB1 domain is essential part of the p40 adaptor protein which plays an important role in activating phagocyte NADPH oxidase during phagocytosis. The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. The PB1 domain of p40 represents a type I PB1 domain which interacts with the PB1 domain of oxidase activator p67 which belong to type II PB1 domain. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants
NWLRCYYYEDTISTIRDIAVEEDLSSTPLLKDLLELTRREFQREDIALNYRDAEGDLIRLLSDEDVALMV
RQSRGLPSQKRLFPWKLHITHK
>gnl|CDD|99722 cd06401, PB1_TFG, The PB1 domain found in TFG protein, an oncogenic gene product and fusion partner to nerve growth factor tyrosine kinase receptor TrkA and to the tyrosine kinase ALK. The PB1 domain is a modular domain mediating specific protein-protein interaction in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. The PB1 domains of TFG represent a type I/II PB1 domain. The physiological function of TFG remains unknown
LILKAQLGDDIRRIPIHNEDITYDELLLMMQRVFRGKLGSSDDVLIKYKDEDGDLITIFDSSDLSFAIQC
SRILKLTLFVN
>gnl|CDD|99723 cd06402, PB1_p62, The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) involved in cell signaling, receptor internalization, and protein turnover. The PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants
LTVKAYLLGKDANAEIRRFAIDEDVSTSYEYLVEKVAAVFPSLRGKNFQLFWKDEEGDLVAFSSDEELVM
ALGSLNDDTFRIYIKEK
>gnl|CDD|99724 cd06403, PB1_Par6, The PB1 domain is an essential part of Par6 protein which in complex with Par3 and aPKC proteins is crucial for establishment of apical-basal polarity of animal cells. The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The Par6 protein contains a type II PB1 domain
VEVKSKFDAEFRRFSLDRNKPGKFEDFYKLLEHLHHIPNVDFLIGYTDPHGDLLPINNDDNFLKALSSAN
PLLRIFIQRR
>gnl|CDD|99725 cd06404, PB1_aPKC, PB1 domain is an essential modular domain of the atypical protein kinase C (aPKC) which in complex with Par6 and Par3 proteins is crucial for establishment of apical-basal polarity of animal cells. PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The aPKC protein contains a type I/II PB1 domain
VRVKAAYNGDIMITSIDPSISLEELCNEVRDMCRFHNDQPFTLKWIDEEGDPCTISSQMELEEAFRLYEL
NKDSELNIHVFPG
>gnl|CDD|99726 cd06405, PB1_Mekk2_3, The PB1 domain is present in the two mitogen-activated protein kinase kinases MEKK2 and MEKK3 which are two members of the signaling kinase cascade involved in angiogenesis and early cardiovascular development. The PB1 domain of MEKK2 (and/or MEKK3) interacts with the PB1 domain of another member of the kinase cascade Map2k5. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The MEKK2 and MEKK3 proteins contain a type II PB1 domain
VRIKFEHNGEKRIIQFPRPVKFKDLQQKVTTAFGQPMDLHYTNNELLIPLKNQEDLDRAIELLDRSPHMK
SLRILLSAP
>gnl|CDD|99727 cd06406, PB1_P67, A PB1 domain is present in p67 proteins which forms a signaling complex with p40, a crucial step for activation of NADPH oxidase during phagocytosis. PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes . A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The p67 proteins contain a type II PB1 domain
DSYVVKVHFKYTVAIQVARGLSYATLLQKISSKLELPAEHITLSYKSEASGEDVILSDTNMEDVWSQAKD
GCLTLWCTLT
>gnl|CDD|99728 cd06407, PB1_NLP, A PB1 domain is present in NIN like proteins (NLP), a key enzyme in a process of establishment of symbiosis betweeen legumes and nitrogen fixing bacteria (Rhizobium). The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes like osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants
VRVKATYGEEKIRFRLPPSWGFTELKQEIAKRFKLDDMSAFDLKYLDDDEEWVLLTCDADLEECIDVYRS
SGSHTIRLLVHA
>gnl|CDD|99729 cd06408, PB1_NoxR, The PB1 domain is present in the Epichloe festucae NoxR protein (NADPH oxidase regulator), a key regulator of NADPH oxidase isoform, NoxA. NoxA is essential for growth control of the fungal endophyte in plant tissue in the process of symbiotic interaction between a fungi and its plant host. The Epichloe festucae p67(phox)-like regulator, NoxR, dispensable in culture but essential in plants for the symbiotic interaction. Plants infected with a noxR deletion mutant show severe stunting and premature senescence, whereas hyphae in the meristematic tissues show increased branching leading to increased fungal colonization of pseudostem and leaf blade tissue. The PB1 domain is a modular domain mediating specific protein-protein interactions which a play role in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants
RKIRVKVHAQDDTRYIMIGPDTGFADFEDKIRDKFGFKRRLKIKMKDDGDMITMGDQDDLDMAIDTARSE
ARKQGSDMGKLEIWVM
>gnl|CDD|99730 cd06409, PB1_MUG70, The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in meiosis and harbors a PB1 domain. The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domains depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic amino acid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants
FAFKFKDPKGRVHRFRLRPSESLEELRTLISQRLGDDDFETHLYALSYVDDEGDIVLITSDSDLVAAVLV
ARSAGLKKLDLHLHYP
>gnl|CDD|99731 cd06410, PB1_UP2, Uncharacterized protein 2. The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions
LCSYGGRILPRPPDGQLRYVGGETRIVSVDRSISFKELVSKLSELFGAGVVVTLKYQLPDEDLDALISVS
NDEDLKNMMEEYDRLSGGSARLRVFLF
>gnl|CDD|99732 cd06411, PB1_p51, The PB1 domain is present in the p51 protein, a homolog of the p67 protein. p51 plays an important role in NADPH oxidase activation during phagosytosis. The PB1 domain is a modular domain mediating specific protein-protein interaction in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants
VTVQCAFTVALRAPRGADVSSLRALLSQALPQQAQRGQLSYRAPGEDGHWVPISGEESLQRAWQDVADGP
RGLQLQCR
>gnl|CDD|119374 cd06412, GH25_CH-type, CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases
VPGIDVSGHQGSVDWSGAAANGARFAYVKATEGTSYTNPRFSSQYNGAYNAGLIRGAYHFALPDQSSGAA
QADYFLDHGGGWSPDGRTLPGVLDLEYNPYGATCYGLSPAQMVSWIKDFSDTYKARTGRDPVIYTTTSWW
NQCTGNSAGFANHPLWLARYGSSPGALPAGWSAWTFWQYSDSGPFPGDQNVFNGSRASL
>gnl|CDD|119375 cd06413, GH25_muramidase_1, Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues
YPVRGIDVSHHQGDIDWARVRAQGVSFAYIKATEGGDHVDKRFAENWRGARAAGLPRGAYHFFTFCRSGA
EQAANFIRNVPKDPGALPPVVDVEWNGNSATCPSAEEVLAELQVFLDALEAHYGKRPIIYTTYDFYDDYL
KGEFPDYPLWIRSVAGHPRLYEDRPWTFWQYTNRGRVPGIEGDVDLNVFNG
>gnl|CDD|119376 cd06414, GH25_LytC-like, The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes
KKGIDVSEWQGDIDWKKVKASGVDFAIIRAGYGGYGELQEDKYFEENIKGAKAAGIPVGVYFYSYAVTVA
EAREEAEFVLRLIKGYKLSYPVYYDLEDETQLGAGLSKDQRTDIANAFCETIEAAGYYPGIYANLSWLTN
KLDDERLSKYDVWVAQYGNSPTYPGNYGMWQYTSSGSVPGISGNVDLNYCY
>gnl|CDD|119377 cd06415, GH25_Cpl1-like, Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin encoded by the pneumococcal bacteriophage Cp-1, which cleaves the glycosidic N-acetylmuramoyl-(beta1,4)-N-acetylglucosamine bonds of the pneumococcal glycan chain, thus acting as an enzymatic antimicrobial agent (an enzybiotic) against streptococcal infections. Cpl-1 belongs to the CP family of lysozymes (CPL lysozymes) which includes the Cpl-7 lysin. Cpl-1 has a glycosyl hydrolase family 25 (GH25) catalytic domain with an irregular (beta/alpha)5-beta3 barrel and a C-terminal cell wall-anchoring module formed by six similar choline-binding repeats (ChBr's). The ChBr's facilitate the anchoring of Cpl-1 to the choline-containing teichoic acid of the pneumococcal cell wall. Other members of this domain family have an N-terminal CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain similar to that of the firmicute CHAP lysins and associated with endopeptidase activity. The Cpl-7 lysin is also included here as is LysB of Lactococcus phage, and the Mur lysin of Lactobacillus phage
DYGVDVASYQGTDLTAYGQAGAKFAIVKISEGTNYVNPKASAQVSSAIANGKMTGGYHFARFGGSVSQAK
YEADYFLNSAQQAGLPKGSYLALDYEQGSGNSKAANTSAILAFMDTIKDAGYKPMLYSYKPLLLNNVDYS
QIIAKYPNSLWVAAYPTYGVQDTPDFNYFPSMDGVAIWQFTSNWRGGGVDGNITLL
>gnl|CDD|119378 cd06416, GH25_Lys1-like, Lys-1 is a lysozyme encoded by the Caenorhabditis elegans lys-1 gene. This gene is one of a several lysozyme genes upregulated upon infection by the Gram-negative bacterial pathogen Serratia marcescens. Lys-1 contains a glycosyl hydrolase family 25 (GH25) catalytic domain. This family also includes Lys-5 from Caenorhabditis elegans
ILGVDISQPTSVSTFQCLKNNGYSFAIIRAYRSNGSFDPNSVTNIKNARAAGLSTDVYFFPCINCCGSAA
GQVQTFLQYLKANGIKYGTVWIDIEQNPCQWSSDVASNCQFLQELVSAAKALGLKVGIYSSQYDWSQIFG
SSYTCNFSSLPLWYAHYDNNPNFSDFSPFGGWTKPTMKQYSGTTTVCGVSVDLNVY
>gnl|CDD|119379 cd06417, GH25_LysA-like, LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis
MNGIDVSSWQSRIVTTVVPADFVIVKATQGTGYVNPSWRSQAAQAIAAGKLLGLYHYANGGNAIAEADYF
LNNIKGYVGKAVLVLDWESYQNSAWGNSAWARQWVNRVHELTGVWPMVYVSKSVTRQINWSVRADCGLWV
AQYASNNPTGYQSQAGPWNAAWSGETIHQYTSNGSLNGYNGPLDLNLFYGDREQW
>gnl|CDD|119380 cd06418, GH25_BacA-like, BacA is a bacterial lysin from Enterococcus faecalis that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. BacA is homologous to the YbfG and YkuG lysins of Bacillus subtilis. BacA has a C-terminal catalytic glycosyl hydrolase family 25 (GH25) domain and an N-terminal peptidoglycan-binding domain comprised of three alpha helices which is similar to a domain found in matrixins
LLVSTGDTTRTGWACDTATQPTDARAQTLKAAGYGIVGRYLTGSPGGCLSKNLTATELETITAAGLKVFP
IYQGGGYSLDYFGYEQGVKDARDAVAAARALGFPPGTIIYFAVDFDALDDEVTEVILPYFRGWNDALHEA
GYRIGIYGSRNVCSRVLAAAAGLAVVSFVADMSTGFSGNLGYPLPKDWAFDQIAEYTIGSGGGAIPIDTN
AA
>gnl|CDD|119381 cd06419, GH25_muramidase_2, Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues
PALSNYPVLGVQLSQDDGYIDFNSLQSNGISFVYLRATQGASYFDDNFLSNFSRAQGTGLSVGVIHTFSF
SSTAAAQYRYFIRKVGNNTGNLPIAIYVSYYGDYNPDTKKSTQKLGLLVQLLEQHYNQSVIIRGTPAVLK
QVVKALKQLKYWLIEDKLKGQGSKNQFWQYTANGKVKSGGNSAELPLAVF
>gnl|CDD|133042 cd06420, GT2_Chondriotin_Pol_N, N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase. Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix
LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIKHVWQEDEGFRKAKI
RNKAIAAAKGDYLIFIDGDCIPHPDFIADHIELAEPGVFLSGSRVLLNEKLTERGIRGCNMSFWKKDLLA
VNGFDEEFTGWGGEDSELVARLLNSGIKFRKLKFAAIVFHLW
>gnl|CDD|133043 cd06421, CESA_CelA_like, CESA_CelA_like are involved in the elongation of the glucan chain of cellulose. Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end
PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEYGYRYLTRPDNRH
AKAGNLNNALAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDWLADGAPNE
QELFYGVIQPGRDRWGAAFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAG
LAPETLAAYIKQRLRWARGMLQIL
>gnl|CDD|133044 cd06422, NTP_transferase_like_1, NTP_transferase_like_1 is a member of the nucleotidyl transferase family. This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase
KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRFGL
RITISDEPDELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHN
GVGDFSLDADGRLRRGGGGAVAPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWF
DVGTPERLLAA
>gnl|CDD|133045 cd06423, CESA_like, CESA_like is the cellulose synthase superfamily. The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan
IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGAL
NAGLRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRL
GRRAQSALGGVLVLSGAFGAFRREALREVGGWDEDTLTED
>gnl|CDD|133046 cd06424, UGGPase, UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose. UGGPase: UDP-Galactose/Glucose Pyrophosphorylase catalyzes the reversible production of UDP-Glucose/UDP-Galactose and pyrophosphate (PPi) from Glucose-1-phosphate/Galactose-1-phosphate and UTP. Its dual substrate specificity distinguishes it from the single substrate enzyme UDP-glucose pyrophosphorylase. It may play a key role in the galactose metabolism in raffinose oligosaccharide (RFO) metabolizing plants. RFO raffinose is a major photoassimilate and is a galactosylderivative of sucrose (Suc) containing a galactose (Gal) moiety. Upon arriving at the sink tissue, the Gal moieties of the RFOs are initially removed by alpha-galactosidase and then are phosphorylated to Gal-1-P. Gal-1-P is converted to UDP-Gal. The UDP-Gal is further metabolized to UDP-Glc via an epimerase reaction. The UDP-Glc can be directly utilized in cell wall metabolism or in Suc synthesis. However, for the Suc synthesis UDP-Glc must be further metabolized to Glc-1-P. This can be carried out either by the UGPase in the reverse direction or by the dual substrate PPase itself operating in the reverse direction. According to the latter possibility, the three-step pathway of Gal-1-P to Glc-1-P could be carried out by a single PPase, functioning sequentially in reverse directions separated by the epimerase reaction
AVFVLVAGGLGERLGYSGIKIGLPVELTTNTTYLQYYLNYIRAFQEASKKGEKMEIPFVIMTSDDTHSKT
LKLLEENNYFGLEKDQVHILKQEKVFCLIDNDAHLALDPDNTYSILTKPHGHGDVHTLLYNSGLLKKWIE
AGYKWLVFFQDTNALAFKAIPAVLGVSATKSLDMNSLTVPRKPKEAIGALCKLTKNNGKSMTINVEYNQL
DPLLRASGKDDGDVDDKTGFSPFPGNINQLVFSLGPYMDELEKTKGAIPEFINPKYKDATKTAFKSPTRL
ECMMQDIPLLFEEDYRVGFTVLDRWLCFSPVKNNL
>gnl|CDD|133047 cd06425, M1P_guanylylT_B_like_N, N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation
MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKK
LGIKITFSIETEPLGTAGPLALARDLLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVED
PSKYGVVVHDENTGRIERFVEKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAY
ELPGFWMDIGQPKDFLKGMSLYL
>gnl|CDD|133048 cd06426, NTP_transferase_like_2, NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family. This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase
VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGV
NISYVREDKPLGTAGALSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVREYEVQVPYGV
VETEGGRITSIEEKPTHSFLVNAGIYVLEPEVLDLIPKNEFFDMPDLIEKLIKEGKKVGVFPIHEYWLDI
GRPEDYEKAN
>gnl|CDD|133049 cd06427, CESA_like_2, CESA_like_2 is a member of the cellulose synthase superfamily. The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, Glucan Biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of glucan
PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAARALRLPSIFRVVVVPPSQPR
TKPKACNYALAFARGEYVVIYDAEDAPDPDQLKKAVAAFARLDDKLACVQAPLNYYNARENWLTRMFALE
YAAWFDYLLPGLARLGLPIPLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTTLE
EANNALGNWIRQRSRWIKGYMQTWLVHMRNP
>gnl|CDD|133050 cd06428, M1P_guanylylT_A_like_N, N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase. N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation
AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFYPESVFSDFISDAQQ
EFNVPIRYLQEYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEA
SREQASNYGCIVEDPSTGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNRE
GRAEVIRLEQDVLTPLAGSGKLYVYKTDDFWSQIKTAGSAIYANRLY
>gnl|CDD|133051 cd06429, GT8_like_1, GT8_like_1 represents a subfamily of GT8 with unknown function. A subfamily of glycosyltransferase family 8 with unknown function: Glycosyltransferase family 8 comprises enzymes with a number of known activities; lipopolysaccharide galactosyltransferase lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase and inositol 1-alpha-galactosyltransferase. It is classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed
IHVVIFSDNRLAAAVVINSSISNNKDPSNLVFHIVTDNQNYGAMRSWFDLNPLKIATVKVLNFDDFKLLG
KVKVDSLMQLESEADTSNLKQRKPEYISLLNFARFYLPELFPKLEKVIYLDDDVVVQKDLTELWNTDLGG
GVAGAVETSWNPGVNVVNLTEWRRQNVTETYEKWMELNQEEEVTLWKLITLPPGLIVFYGLTSPLDPSWH
VRGLGYNYGIRPQDIKAAAVLHFNGNMKPWLRTAIPSYKELWEKYLS
>gnl|CDD|133052 cd06430, GT8_like_2, GT8_like_2 represents a subfamily of GT8 with unknown function. A subfamily of glycosyltransferase family 8 with unknown function: Glycosyltransferase family 8 comprises enzymes with a number of known activities; lipopolysaccharide galactosyltransferase lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase and inositol 1-alpha-galactosyltransferase. It is classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed
MHLAVVACGERLEETLTMLKSAIVFSQKPLRFHIFAEDQLKQSFKEKLDDWPELIDRKFNYTLHPITFPS
GNAAEWKKLFKPCAAQRLFLPSLLPDVDSLLYVDTDILFLRPVEEIWSFLKKFNSTQLAAMAPEHEEPNI
GWYNRFARHPYYGKTGVNSGVMLMNLTRMRRKYFKNDMTPVGLRWEEILMPLYKKYKLKITWGDQDLINI
IFHHNPEMLYVFPCHWNYRPDHCMYGSNCKAAEEEGVFILHGNRGVYHSDKQPAFRAVYEAIREYTFGDD
LHQSLLRPLELSLQLTVHTYCGKA
>gnl|CDD|133053 cd06431, GT8_LARGE_C, LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis. The catalytic domain of LARGE is a putative glycosyltransferase. Mutations of LARGE in mouse and human cause dystroglycanopathies, a disease associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. LARGE needs to both physically interact with alpha-dystroglycan and function as a glycosyltransferase in order to stimulate alpha-dystroglycan hyperglycosylation. LARGE localizes to the Golgi apparatus and contains three conserved DxD motifs. While two of the motifs are indispensible for glycosylation function, one is important for localization of th eenzyme. LARGE was originally named because it covers approximately large trunck of genomic DNA, more than 600bp long. The predicted protein structure contains an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif, and two putative catalytic domains. This catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis
IHVAIVCAGYNASRDVVTLVKSVLFYRRNPLHFHLITDEIARRILATLFQTWMVPAVEVSFYNAEELKSR
VSWIPNKHYSGIYGLMKLVLTEALPSDLEKVIVLDTDITFATDIAELWKIFHKFTGQQVLGLVENQSDWY
LGNLWKNHRPWPALGRGFNTGVILLDLDKLRKMKWESMWRLTAERELMSMLSTSLADQDIFNAVIKQNPF
LVYQLPCAWNVQLSDHTRSEQCYRDVSDLKVIHWNSPKKLRVKNKHVEFFRNLYLTFLEYDGNLLRRELF
>gnl|CDD|133054 cd06432, GT8_HUGT1_C_like, The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family. C-terminal domain of glycoprotein glucosyltransferase (UGT). UGT is a large glycoprotein whose C-terminus contains the catalytic activity. This catalytic C-terminal domain is highly homologous to Glycosyltransferase Family 8 (GT 8) and contains the DXD motif that coordinates donor sugar binding, characteristic for Family 8 glycosyltransferases. GT 8 proteins are retaining enzymes based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. The non-catalytic N-terminal portion of the human UTG1 (HUGT1) has been shown to monitor the protein folding status and activate its glucosyltransferase activity
INIFSVASGHLYERFLRIMMLSVMKNTKSPVKFWFIKNFLSPQFKEFLPEMAKEYGFEYELVTYKWPRWL
HKQTEKQRIIWGYKILFLDVLFPLNVDKVIFVDADQIVRTDLKELMDMDLKGAPYGYTPFCDSRKEMDGF
RFWKQGYWKSHLRGRPYHISALYVVDLKRFRRIAAGDRLRGQYQQLSQDPNSLANLDQDLPNNMQHQVPI
FSLPQEWLWCETWCSDESKKKAKTIDLCNNPLTKEPKL
>gnl|CDD|133055 cd06433, GT_2_WfgS_like, WfgS and WfeV are involved in O-antigen biosynthesis. Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families
SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKG
IALATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLLYGM
PICHQATFFRRSLFEKYGGFDESYRIAADYDLLLRLLLAGKIFKYLPEVLAAFRLGGVSSTS
>gnl|CDD|133056 cd06434, GT2_HAS, Hyaluronan synthases catalyze polymerization of hyaluronan. Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate
DVTVIIPVYDEDPDVFRECLRSILRQKPLEIIVVTDGDDEPYLSILSQTVKYGGIFVITVPHPGKRRALA
EGIRHVTTDIVVLLDSDTVWPPNALPEMLKPFEDPKVGGVGTNQRILRPRDSKWSFLAAEYLERRNEEIR
AAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEFTNETFMGRRLNAGDDRFLTRYVLSHGYKTVYQYTSEA
YTETPENYKKFLKQQLRWSRSNWRS
>gnl|CDD|133057 cd06435, CESA_NdvC_like, NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response
SIHVPCYEEPPEMVKETLDSLAALDYPNFEVIVIDNNTKDEALWKPVEAHCAQLGERFRFFHVEPLPGAK
AGALNYALERTAPDAEIIAVIDADYQVEPDWLKRLVPIFDDPRVGFVQAPQDYRDGEESLFKRMCYAEYK
GFFDIGMVSRNERNAIIQHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLI
PDTFEAFKKQRFRWAYGAVQILKKHW
>gnl|CDD|133058 cd06436, GlcNAc-1-P_transferase, N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine. N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase
VLVPCLNEEAVIQRTLASLLRNKPNFLVLVIDDASDDDTAGIVRLAITDSRVHLLRRHLPNARTGKGDAL
NAAYDQIRQILIEEGADPERVIIAVIDADGRLDPNALEAVAPYFSDPRVAGTQSRVRMYNRHKNLLTILQ
DLEFFIIIAATQSLRALTGTVGLGGNGQFMRLSALDGLIGEEPWSDSLLED
>gnl|CDD|133059 cd06437, CESA_CaSu_A2, Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex. Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal
PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQGVNIKHVRRAD
RTGYKAGALAEGMKVAKGEYVAIFDADFVPPPDFLQKTPPYFADPKLGFVQTRWGHINANYSLLTRVQAM
SLDYHFTIEQVARSSTGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVV
PAELPASMSAYRSQQHRWSKGP
>gnl|CDD|133060 cd06438, EpsO_like, EpsO protein participates in the methanolan synthesis. The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier
ILIPAHNEEAVIGNTVRSLKAQDYPRELYRIFVVADNCTDDTAQVARAAGATVLERHDPERRGKGYALDF
GFRHLLNLADDPDAVVVFDADNLVDPNALEELNARFAAGARVVQAYYNSKNPDDSWITRLYAFAFLVFNR
LRPLGRSNLGLSCQLGGTGMCFPWAVLRQAPWAAHSLTEDLEF
>gnl|CDD|133061 cd06439, CESA_like_1, CESA_like_1 is a member of the cellulose synthase (CESA) superfamily. This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins
TYFGYPLLLKLLARLRPKPPSLPDPAYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRDRLEIIVVSDGS
TDGTAEIAREYADKGVKLLRFPERRGKAAALNRALALATGEIVVFTDANALLDPDALRLLVRHFADPSVG
AVSGELVIVDGGGSGSGEGLYWKYENWLKRAESRLGSTVGANGAIYAIRRELFRPLPADTINDDFVLPLR
IARQGYRVVYEPDAVAYEEVAEDGSEEFRRRVRIAAGNLQA
>gnl|CDD|133062 cd06442, DPM1_like, DPM1_like represents putative enzymes similar to eukaryotic DPM1. Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily
IIIPTYNERENIPELIERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAY
IEGFKAARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLA
RLLLGRKVSDPTSGFRAYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLG
GKEIVEYLKGLLRL
>gnl|CDD|176473 cd06444, DNA_pol_A, Family A polymerase primarily fills DNA gaps that arise during DNA repair, recombination and replication. DNA polymerase family A, 5'-3' polymerase domain. Family A polymerase functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. DNA-dependent DNA polymerases can be classified into six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaeota polymerase II (class D), human polymerase beta (class X), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerases are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I, mitochondrial polymerase gamma, and several bacteriophage polymerases including those from odd-numbered phage (T3, T5, and T7). Prokaryotic polymerase I (pol I) has two functional domains located on the same polypeptide; a 5'-3' polymerase and a 5'-3' exonuclease. Pol I uses its 5' nuclease activity to remove the ribonucleotide portion of newly synthesized Okazaki fragments and the DNA polymerase activity to fill in the resulting gap. The structure of these polymerases resembles in overall morphology a cupped human right hand, with fingers (which bind an incoming nucleotide and interact with the single-stranded template), palm (which harbors the catalytic amino acid residues and also binds an incoming dNTP) and thumb (which binds double-stranded DNA) subdomains
DELLLELLGPRPAEGLRPAELELLAHPAVPLLLEYKKLAKLWSANGWPWLDQWVRDGRFHPEYVPGGTVT
GRWASRGGNAQQIPRRDPLGRDIRQAFVADPGWTLVVADASQLELRVLAALSGDEALAEAFGRGGDLYTA
TASAMFGVPVGGGERQHAKIANLGAMYGATSGISARLLAQLRRISTKEAAALIELFFSRFPAFPKAMEYV
EDAARRGERGGYVRTLLGRRSPPPDIRWTEVVSDPAAASRARRVRRAAGRFARNFVVQGTAADWAKLAMV
ALRRRLEELALDARLVFFVHDEVVLHCPKEEAEAVAAIVREAAEQAVRLLFGSVPVRFPVKIGVVWR
>gnl|CDD|119438 cd06445, ATase, The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT and MGMT) reverses O6-alkylation DNA damage by transferring O6-alkyl adducts to an active site cysteine irreversibly, without inducing DNA strand breaks. ATases are specific for repair of guanines with O6-alkyl adducts, however human ATase is not limited to O6-methylguanine, repairing many other adducts at the O6-position of guanine as well. ATase is widely distributed among species. Most ATases have N- and C-terminal domains. The C-terminal domain contains the conserved active-site cysteine motif (PCHR), the O6-alkylguanine binding channel, and the helix-turn-helix (HTH) DNA-binding motif. The active site is located near the recognition helix of the HTH motif. While the C-terminal domain of ATase contains residues that are necessary for DNA binding and alkyl transfer, the function of the N-terminal domain is still unknown. Removal of the N-terminal domain abolishes the activity of the C-terminal domain, suggesting an important structural role for the N-terminal domain in orienting the C-terminal domain for proper catalysis. Some ATase C-terminal domain homologs are either single-domain proteins that lack an N-terminal domain, or have a tryptophan substituted in place of the acceptor cysteine (i.e. the motif PCHR is replaced by PWHR). ATase null mutant mice are viable, fertile, and have a normal lifespan
FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLER
KRELLELEG
>gnl|CDD|107207 cd06446, Trp-synth_B, Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions
PALEELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYLGGAKIYLKREDLNHTGAHKINNA
LGQALLAKRMGKKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPS
GSGTLKDAISEAIRDWVTNVEDTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACV
GGGSNAAGLFYPFINDKDVKLIGVEAGGCGLETGGHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSIS
AGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKLLARTEGIIPALESSHAIAYAIKLAKKLGKEKVI
VVNLSGRGDKDLQTV
>gnl|CDD|107208 cd06447, D-Ser-dehyd, D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- or D-serine to pyruvate and ammonia. D-serine dehydratase serves as a detoxifying enzyme in most E. coli strains where D-serine is a competitive antagonist of beta-alanine in the biosynthetic pathway to pentothenate and coenzyme A. D-serine dehydratase is different from other pyridoxal-5'-phosphate-dependent enzymes in that it catalyzes alpha, beta-elimination reactions on amino acids
IFWKNPNYGKPAEALAPLSREDIFDAEARLKRFAPYIAKVFPETAASHGIIESPLLPIPRMKQALEKLYH
QPIKGRLLLKADSHLPISGSIKARGGIYEVLKHAEKLALEHGLLTLEDDYSKLASEKFRKLFSQYSIAVG
STGNLGLSIGIMAAALGFKVTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCYFV
DDENSRDLFLGYAVAASRLKAQLAELGIKVDAEHPLFVYLPCGVGGAPGGVAFGLKLIFGDNVHCFFAEP
THSPCMLLGMATGLHDKISVQDIGIDNRTAADGLAVGRPSGLVGKLMEPLLSGIYTVEDDELYRLLAMLK
DSENIEVEPSAAAGFTGPAQVLSEAEGKRYVRLGYRMENATHIVWATGGSMVPE
>gnl|CDD|107209 cd06448, L-Ser-dehyd, Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L-, D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia
KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNECVHVVCSSGGNAGLAAAYAA
RKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREELAENDPGPVYVHPFDDPLIWEGH
SSMVDEIAQQLQSQEKVDAIVCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTL
PKITSVATSLGAKTVSSQALEYAQEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKIL
DLQLEVLLTPLDNVVVVVCGGSNITLEQLKEYKKQL
>gnl|CDD|107210 cd06449, ACCD, Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia
TPIQYLPRLSEHLGGKVEIYAKRDDCNSGLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVA
AVAAKLGLKCVLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGFDIGIRKSFEEAAEEVEAKGGKP
YVIPAGGSEHPLGGLGYVGFVLEIAQQEEELGFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDAS
AKPEKTKAQVLRIAQAKLAEEGLEVKEEDVVLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGK
SMQGMIDLVRNGEFKEGSKVLFIHLGG
>gnl|CDD|99743 cd06450, DOPA_deC_like, DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine
FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESN
LLALLAARDRARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAID
EDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSI
SVDPHKYGLVPLGCSAVLVRALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLSL
VCFRLKPSVKLDELNYDLSDRLNERGGWHVPATTLGGPNVLRFVVTNPLTTRDDADALLEDIERA
>gnl|CDD|99744 cd06451, AGAT_like, Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway
LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNL
LEPGDKVLVGVNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVL
NPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIKKK
TKPKGFYFDLLLLLKYWGEGYSYPHTPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGL
KLLAKPELRSPTVTAVLVPEGVDGDEVVRRLMKRYNIEIAGGLGPTAGKVFRIGHMGEATREDVLGVLSA
LEEALK
>gnl|CDD|99745 cd06452, SepCysS, Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface
FINIDPIQRGGRLTPEARKALIEWGDGYSVCDFCRGRLDEIEKPPIKDFHHDLAEFLGMDEARVTPGARE
GKFAVMHSLCEKGDWVVVDGLAHYTSYVAAERAGLNVREVPNTGHPEYHITPEGYAEVIEEVKDEFGKPP
ALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHKSMAASAPIG
VLATTEEWADIVFRTSQMFKIKEVELLGCTLRGAPLVTLMASFPHVKERVKRWDEEVEKARWFVAELEKI
EGIKQLGEKPKNHDLMFFETPSFDEIAKKHKRRGYFLYSELKKRGIHGIKPGLTRYFKLSTYGLTWEQVE
YVVDAFKEIAE
>gnl|CDD|99746 cd06453, SufS_like, Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine
VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNT
TEAINLVAYGLGRANKPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERT
KLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGV
LYGKEELLEEMPPYGGGGEMIEEVSFEETTYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHE
HELTAYALERLSEIPGVRVYGDAEDRAGVVSFNLEGIHPHDVATILDQYGIAVRAGHHCAQPLMRRLGVP
GTVRASFGLYNTEEEIDALVEAL
>gnl|CDD|99747 cd06454, KBL_like, KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life
KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSG
YAANDGVLSTLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRPYGKKLIVTEG
VYSMDGDIAPLPELVDLAKKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGY
IAGSKELIDYLRSYARGFIFSTSLPPAVAAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGS
PSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG
>gnl|CDD|341050 cd06455, M3A_TOP, Peptidase M3 thimet oligopeptidase (TOP), also includes neurolysin. Peptidase M3 Thimet oligopeptidase (TOP; PZ-peptidase; endo-oligopeptidase A; endopeptidase 24.15; soluble metallo-endopeptidase; EC 3.4.24.15) family also includes neurolysin (endopeptidase 24.16, microsomal endopeptidase, mitochondrial oligopeptidase M, neurotensin endopeptidase, soluble angiotensin II-binding protein, thimet oligopeptidase II) which hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. TOP and neurolysin are neuropeptidases expressed abundantly in the testis, but are also found in the liver, lung and kidney. They are involved in the metabolism of neuropeptides under 20 amino acid residues long and cleave most bioactive peptides at the same sites, but recognize different positions on some naturally occurring and synthetic peptides; they cleave at distinct sites on the 13-residue bioactive peptide neurotensin, which modulates central dopaminergic and cholinergic circuits. TOP has been shown to degrade peptides released by the proteasome, limiting the extent of antigen presentation by major histocompatibility complex class I molecules, and has been associated with amyloid protein precursor processing
LATADEIIAEAKAVLDAIAALPPEDATFENTLLPLDEAENELSDASGPLTFLQSVSPDKEVRDASSEAEK
KLSAFSIELSMREDLYRLVKAVYDKNEKKLDAESRRLLEKLLRDFRRNGLGLPDEKRERLKELKKEISEL
SIEFSKNLNEDNTGIWFTEEELEGVPEDFLDRLKKDDDGKYKVTLKYPDYFPVMKYAKNPETRKRMYLAF
ENRAYPENVPLLEEIVALRDELARLLGYKSHADYVLEDRMAKTPEAVEAFLDDLREKLKPLAEKELAELL
ALKKEDLPEAGLPGKLYPWDLAYYSRLLKKEEYSVDEEKIREYFPLEHVVDGMLDIYEELFGLRFEEVDG
APVWHPDVRLYAVWDDDTGEFLGYLYLDLFPREGKYGHAANFPLQPGFTKPDGSRQYPVTALVCNFPKPT
ADKPSLLKHDEVVTLFHEFGHAMHDLLSRTKYARFHGTSVERDFVEAPSQMLENWCWDPEVLKRLSKHYK
TGEPLPDELIEKLIKSRNFNSGLFYLRQLFLALFDLALHTPDSHEALDLTKLWNELREEITLIPGPPEGT
HGYASFGHLMGGYDAGYYGYLWSEVFAADMFYTFFKADPLNPEVGRRYRDKVLEPGGSRDEMELLEDFLG
REPNSDAFLKEL
>gnl|CDD|341051 cd06456, M3A_DCP, Peptidase family M3, dipeptidyl carboxypeptidase (DCP). Peptidase family M3 dipeptidyl carboxypeptidase (DCP; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). This metal-binding M3A family also includes oligopeptidase A (OpdA; EC 3.4.24.70). DCP cleaves dipeptides off the C-termini of various peptides and proteins, the smallest substrate being N-blocked tripeptides and unblocked tetrapeptides. DCP from Escherichia coli is inhibited by the anti-hypertensive drug captopril, an inhibitor of the mammalian angiotensin converting enzyme (ACE, also called peptidyl dipeptidase A). OpdA may play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. It can also cleave N-acetyl-L-Ala. This family also includes Arabidopsis thaliana organellar oligopeptidase OOP (At5g65620), which plays a role in targeting peptide degradation in mitochondria and chloroplasts; it degrades peptide substrates that are between 8 to 23 amino acid residues, and shows a weak preference for hydrophobic residues (F/L) at the P1 position
EHFVPAIEEAIAEQRAEIEAIEANPEPPTFENTIEPLERAGEPLDRVWGVFSHLNSVNNSDELRAAYEEV
LPLLSAHSDAIGQNEALFARVKALYDSREALGLDPEQKRLLEKTLRDFVLSGAALSEEKKERLAEINEEL
SELSTKFSQNVLDATNAFSLVITDEAELAGLPESALAAAAEAAKARGKGGWLFTLDAPSYQPFLTYCDNR
ELREKVYRAYVTRASDGGEFDNSPIIEEILALRAEKAKLLGYKNYAEYSLATKMAKSPEAVLEFLEDLAE
KAKPAAEKELAELQAFAKEEGGGDKLEPWDWAYYAEKLRKEKYDLDEEELRPYFPLDRVLEGLFELAERL
YGITFKERDDVPVWHPDVRVYEVFDADGELLGLFYLDLYARPGKRGGAWMDSFRSRSRLLDSGQLPVAYL
VCNFTPPAGGKPALLSHDEVETLFHEFGHALHHLLTDVDYPSVSGTNVVWDFVELPSQFMENWAWEPEVL
KLYARHYETGEPLPDELIEKLLAARNFNAGFATLRQLAFALLDLALHSLYDPEAPEDVDAFEREVLKEYG
VLPPIPPRRRSCSFSHIFSGGYAAGYYSYLWAEVLAADAFSAFEEAGGFNRETGRRFRDTILSRGGSRDP
MELFRAFRGRDPDIDALLRRRGL
>gnl|CDD|341052 cd06457, M3A_MIP, Peptidase M3 mitochondrial intermediate peptidase (MIP). Peptidase M3 mitochondrial intermediate peptidase (MIP; EC 3.4.24.59) belongs to the widespread subfamily M3A, that shows similarity to Thimet oligopeptidase (TOP). It is one of three peptidases responsible for the proteolytic processing of both nuclear and mitochondrial encoded precursor polypeptides targeted to various subcompartments of the mitochondria. It cleaves intermediate-size proteins initially processed by mitochondrial processing peptidase (MPP) to yield a processing intermediate with a typical N-terminal octapeptide that is sequentially cleaved by MIP to mature-size protein. MIP cleaves precursor proteins of respiratory components, including subunits of the electron transport chain and tri-carboxylic acid cycle enzymes, and components of the mitochondrial genetic machinery, including ribosomal proteins, translation factors, and proteins required for mitochondrial DNA metabolism. It has been suggested that the human MIP (HMIP polypeptide (gene symbol MIPEP) may be one of the loci predicted to influence the clinical manifestations of Friedreich's ataxia (FRDA), an autosomal recessive neurodegenerative disease caused by the lack of human frataxin. These proteins are enriched in cysteine residues, two of which are highly conserved, suggesting their importance to stability as well as in formation of metal binding sites, thus playing a role in MIP activity
GLFGLPGLTSPSGFQRLARETLARCEDLVDRILNDDSPNESRKVVKLLDDLSDTLCRVIDLAEFVRNVHP
DPEFVEAAEEAYEELSEYMNELNTNTGLYDALKRVLEDPEIVASLTEEERRVAKLLLRDFEKSGIHLPEE
KRKKFVELSSEILSLGREFLQNASAPDEEVRKKVYLAYHSSSEEQEEVLEELLKARAELAQLLGFPSYAH
RALRDKMAKSPENVLSFLETLSDSLRPKAEKELEELRKLKRKHEGLSSPTLMPWDRDYYTGLLRAQARSS
DASELSPYFSLGTVMEGLSRLFSRLYGIRLVPVPTQPGEVWHPDVRKLEVVHETEGLLGTIYCDLFERPG
KPPGAAHFTIRCSRRLDDDDLGDGGSYQLPVVVLVCNFPPPSGSSPTLLSHSEVETLFHEMGHAMHSMLG
RTRYQHVSGTRCATDFVELPSILMEHFASDPRVLSLFARHYRTGEPLPEELLEKLCASKKLFSALETQQQ
ILYALLDQVLHSEDPLDSSFDSTDILAELQNEYGLLPYVPGTAWQLRFGHLVGYGATYYSYLFDRAIASK
IWQKLFAKDPLSREAGERLREEVLKHGGGRDPWEMLADLLGEEELAEGLVEAM
>gnl|CDD|341053 cd06459, M3B_PepF, Peptidase family M3B, oligopeptidase F (PepF). Peptidase family M3B oligopeptidase F (PepF; Pz-peptidase B; EC 3.4.24.-) is mostly bacterial and includes oligoendopeptidase F from Lactococcus lactis. This enzyme hydrolyzes peptides containing between 7 and 17 amino acids with fairly broad specificity. The PepF gene is duplicated in L. lactis on the plasmid that bears it, while a shortened second copy is found in Bacillus subtilis. Most bacterial PepFs are cytoplasmic endopeptidases; however, the Bacillus amyloliquefaciens PepF oligopeptidase is a secreted protein and may facilitate the process of sporulation. Specifically, the yjbG gene encoding the homolog of the PepF1 and PepF2 oligoendopeptidases of Lactococcus lactis has been identified in Bacillus subtilis as an inhibitor of sporulation initiation when over-expressed from a multicopy plasmid
PEQASFQEALDEFRQAGSQELQQEALKRINELRRRPSTLANLDHIRHTIDTNDEFYKKELTFFDELEPAV
KEDVNDALRALPSSPVPYRQYLRLARRQLAHYLTPDEEKVLVELLEKENVAADEYTKLIASVKIMDFEFE
GEERTLSQVYAQPYLESPDRAVRQRASEARFEGLKEYEKTLAALYNELVHVRTAIARKRGYDSFLELGLA
NNGYNADXVEGLRDIVKTNIVVLAKFLREKQRLLGLEKLYFYDVYAPLPGANTPKGTADEAVDLVRQSFE
PLSPEYAREAFRYFTHRWVDAVANPGKRSGGYCTYIYDYKHPYVLMNFTGTSGDVSTLAHELGHAFHQYF
SRKYQIPLNAWYPLELAEIASTFNELLLSDWLLKFFGSPEEKKYLLAHKLDDLFAFLFRQVAVAEFEHAV
YENREXGGALRKSVLRSIEKAVQPEFDGDDVTLDLDRGIFWARQPHFYTDPFYVYDYTFGQVCALQFYKR
ALEDGASAARDYVDLLRSGGSRPPLELAKSAGLDLSTDGPWQSAVGFIE
>gnl|CDD|341054 cd06460, M32_Taq, Peptidase family M32, which includes thermostable carboxypeptidases TaqCP, PfuCP and FisCP. Peptidase family M32 is a subclass of metallocarboxypeptidases, distributed mainly in bacteria and archaea, whose members contain a HEXXH motif that participates in coordinating a divalent cation such as Zn2+ or Co2+. It includes the thermostable carboxypeptidases (E.C. 3.4.17.19) from Thermus aquaticus (TaqCP) and Pyrococcus furiosus (PfuCP), which have broad specificities toward a wide range of C-terminal substrates that include basic, aromatic, neutral and polar amino acids. These enzymes have a similar fold to the M3 peptidases such as neurolysin and the M2 angiotensin converting enzyme (ACE). The keratin-degrading extremophilic eubacterium Fervidobacterium islandicum M32 carboxypeptidase (FisCP) plays an important role in cellular metabolism, and significantly enhances the degradation of native chicken feathers. It has been shown to mainly cleave the C-termini of peptides with a basic amino acid sequence. Novel M32 peptidases from some eukaryotes: protozoa Trypanosoma cruzi, a causative agent of Chagas' disease, and Leishmania major, a parasite that causes leishmaniasis, have been identified, thus making these enzymes an attractive potential target for drug development against these organisms
LLKEIAALEHALALLGWDQETMMPPGGAEARAEQLATLSGLAHELLTSPELGELLEELEEEEDELDDDEK
ANVRELRREYDRATKIPAELVEEYARLTSEAEAAWREAREENDFALFAPYLEKIVELKREEAEYLGYEKH
PYDALLDEYEPGMTVAELDALFAELKEELVPLLKKILESGKPPDDSFLEGPFPVEKQRALSRELLEALGF
DFDRGRLDESAHPFTTGFGPGDVRITTRYDENDFLSALFSTIHETGHALYEQGLPPELRGTPLGGGASMG
IHESQSRFWENQVGRSRAFWEFLYPKLQEHFPEQLKDVSLEEFYRAVNRVEPSLIRVEADELTYPLHIIL
RYEIEKALINGELEVDDLPEAWNEKMKEYLGITPPNDAEGVLQDVHWSGGSFGYFPTYALGNLYAAQLFA
AMKKDLPDLDEQIARGDFAPIRDWLRENIHQHGSLYTPDELLKRATGEPLNPKYFLDYLEEKYS
>gnl|CDD|341055 cd06461, M2_ACE, Peptidase family M2, angiotensin converting enzyme (ACE). Peptidase family M2 angiotensin converting enzyme (ACE, EC 3.4.15.1) is a membrane-bound, zinc-dependent dipeptidase that catalyzes the conversion of the decapeptide angiotensin I to the potent vasopressor octapeptide angiotensin II, by removing two C-terminal amino acids. There are two forms of the enzyme in humans, the ubiquitous somatic ACE and the sperm-specific germinal ACE, both encoded by the same gene through transcription from alternative promoters. Somatic ACE has two tandem active sites with distinct catalytic properties, whereas germinal ACE, the function of which is largely unknown, has just a single active site. Recently, an ACE homolog, ACE2, has been identified in humans that differs from ACE; it preferentially removes carboxy-terminal hydrophobic or basic amino acids and appears to be important in cardiac function. ACE homologs (also known as members of the M2 gluzincin family) have been found in a wide variety of species, including those that neither have a cardiovascular system nor synthesize angiotensin. ACE is well-known as a key part of the renin-angiotensin system that regulates blood pressure and ACE inhibitors are important for the treatment of hypertension
FLEEYNEEASKLYNRSAEAQWNYETNITDENLQALLEASLELSKFVKEAAENAKKFDWQDFLDPDLKRQL
KLLSRLGVAALDEEDLEELNELLSEMEKIYSTAKVCPYDNPSCCCLLLEPDLTNILATSRDYDELLYAWK
GWRDAVGKKMRPLYEEYVELSNEAARLNGFADAGEYWRSSYEMDEFEEELERLWEQIKPLYEQLHAYVRR
KLRKKYGDDVIPKDGPIPAHLLGNMWAQSWSNIYDLVVPYPDKPSLDVTPELKKQNYTAKKMFKLAEEFF
TSLGLPPLPKSFWEKSMFEKPPDREVVCHASAWDFYNGDDFRIKMCTEVTMEDFLTVHHEMGHIQYYMAY
KDQPVLFREGANPGFHEAIGDTIALSVSTPKHLKRLGLLDDNVDDEEADINFLLKQALDKIAFLPFGYLL
DKWRWDVFSGEIPPDEYNEAWWELREKYQGIVPPVPRSEEDFDPGAKYHIPANTPYIRYFLSTILQFQFH
KALCKAAGHTGPLHKCDIYGSKEAGKKLKKMLSLGSSKPWPDALEELTGERELDASPLLEYFQPLYDWLK
EEN
>gnl|CDD|119396 cd06462, Peptidase_S24_S26, The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal peptidase families. The S24 LexA protein domains include: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The S26 type I signal peptidase (SPase) family also includes mitochondrial inner membrane protease (IMP)-like members. SPases are essential membrane-bound proteases which function to cleave away the amino-terminal signal peptide from the translocated pre-protein, thus playing a crucial role in the transport of proteins across membranes in all living organisms. All members in this superfamily are unique serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases
FALRVEGDSMEPTIPDGDLVLVDKSSYEPKRGDIVVFRLPGGELTVKRVIGLPGEGHYFLLGDNPNSPDS
RIDGPPELDIVGVV
>gnl|CDD|107220 cd06463, p23_like, Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells
WYQTLDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGKEYLLEGELFGPIDPEESKWTVEDRKIEIT
LKKKEPGEWWPRLE
>gnl|CDD|107221 cd06464, ACD_sHsps-like, Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps
DVYETDDAYVVEADLPGFKKEDIKVEVEDGVLTISGEREEEEEEEENYLRRERSYGSFSRSFRLPEDVDP
DKIKASLENGVLTITLPK
>gnl|CDD|107222 cd06465, p23_hB-ind1_like, p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. hB-ind1 participates in signaling by the small GTPase Rac1. It binds to Rac1 and enhances different Rac1 effects including activation of nuclear factor (NF) kappaB and activation of c-Jun N-terminal kinase (JNK). hB-ind1 also plays a part in the RNA replication and particle production of Hepatitis C virus (HCV) through its interaction with heat shock protein Hsp90, HCV nonstructural protein 5A (NS5A), and the immunophilin FKBP8. hB-ind1 is upregulated in the outer layer of Chinese hamster V79 cells grown as multicell spheroids, versus in the same cells grown as monolayers. This group includes the Saccharomyces cerevisiae Sba1, a co-chaperone of the Hsp90. Sba1 has been shown to be is required for telomere length maintenance, and may modulate telomerase DNA-binding activity
PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGGGGKKYEFDLEFYKEIDPEESKYKVTGRQI
EFVLRKKEAGEYWPRLTKEKGKLPWLKVDFDKWVDEDE
>gnl|CDD|107223 cd06466, p23_CS_SGT1_like, p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of Skp1). Sgt1 interacts with multiple protein complexes and has the features of a cochaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. ScSgt1 is needed for the G1/S and G2/M cell-cycle transitions, and for assembly of the core kinetochore complex (CBF3) via activation of Ctf13, the F-box protein. Binding of Hsp82 (a yeast Hsp90 homologue) to ScSgt1, promotes the binding of Sgt1 to Skp1 and of Skp1 to Ctf13. Some proteins in this group have an SGT1-specific (SGS) domain at the extreme C-terminus. The ScSgt1-SGS domain binds adenylate cyclase. The hSgt1-SGS domain interacts with some S100 family proteins, and studies suggest that the interaction of hSgt1 with Hsp90 and Hsp70 may be regulated by S100A6 in a Ca2+ dependent fashion. This group also includes the p23_like domains of Melusin and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). Melusin is a vertebrate protein which interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells
DWYQTDTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGSEYQLELDLFGPIDPEQSKVSVLPTKVEI
TLKKAEPGSWPSLE
>gnl|CDD|107224 cd06467, p23_NUDC_like, p23_like domain of NUD (nuclear distribution) C and similar proteins. Aspergillus nidulas (An) NUDC is needed for nuclear movement. AnNUDC is localized at the hyphal cortex, and binds NUDF at spindle pole bodies (SPBs) and in the cytoplasm at different stages in the cell cycle. At the SPBs it is part of the dynein molecular motor/NUDF complex that regulates microtubule dynamics. Mammalian(m) NUDC associates both with the dynein complex and also with an anti-inflammatory enzyme, platelet activating factor acetylhydrolase I, PAF-AH(I) complex, through binding mNUDF, the regulatory beta subunit of PAF-AH(I). mNUDC is important for cell proliferation both in normal and tumor tissues. Its expression is elevated in various cell types undergoing mitosis or stimulated to proliferate, with high expression levels observed in leukemic cells and tumors. For a leukemic cell line, human NUDC was shown to activate the thrombopoietin (TPO) receptor (Mpl) by binding to its extracellular domain, and promoting cell proliferation and differentiation. This group also includes the human broadly immunogenic tumor associated antigen, CML66, which is highly expressed in a variety of solid tumors and in leukemias. In normal tissues high expression of CML66 is limited to testis and heart
YSWTQTLDEVTVTIPLPEGTKSKDVKVEITPKHLKVGVKGGEPLLDGELYAKVKVDESTWTLEDGKLLEI
TLEKRNEGEWWPSLV
>gnl|CDD|107225 cd06468, p23_CacyBP, p23_like domain found in proteins similar to Calcyclin-Binding Protein(CacyBP)/Siah-1-interacting protein (SIP). CacyBP/SIP interacts with S100A6 (calcyclin), with some other members of the S100 family, with tubulin, and with Siah-1 and Skp-1. The latter two are components of the ubiquitin ligase that regulates beta-catenin degradation. The beta-catenin gene is an oncogene participating in tumorigenesis in many different cancers. Overexpression of CacyBP/SIP, in part through its effect on the expression of beta-catenin, inhibits the proliferation, tumorigenicity, and invasion of gastric cancer cells. CacyBP/SIP is abundant in neurons and neuroblastoma NB2a cells. An extensive re-organization of microtubules accompanies the differentiation of NB2a cells. CacyBP/SIP may contribute to NB2a cell differentiation through binding to and increasing the oligomerization of tubulin. CacyBP/SIP is also implicated in differentiation of erythroid cells, rat neonatal cardiomyocytes, in mouse endometrial events, and in thymocyte development
ITKYAWDQSDKFVKIYITLKGVHQLPKENIQVEFTERSFELKVHDLNGKNYRFTINRLLKKIDPEKSSFK
VKTDRIVITLAKKKEKKWESLT
>gnl|CDD|107226 cd06469, p23_DYX1C1_like, p23_like domain found in proteins similar to dyslexia susceptibility 1 (DYX1) candidate 1 (C1) protein, DYX1C1. The human gene encoding this protein is a positional candidate gene for developmental dyslexia (DD), it is located on 15q21.3 by the DYX1 DD susceptibility locus (15q15-21). Independent association studies have reported conflicting results. However, association of short-term memory, which plays a role in DD, with a variant within the DYX1C1 gene has been reported. Most proteins belonging to this group contain a C-terminal tetratricopeptide repeat (TPR) protein binding region
WSQTDEDVKISVPLKGVKTSKVDIFCSDLYLKVNFPPYLFELDLAAPIDDEKSSAKIGNGVLVFTLVKKE
PGIWEALC
>gnl|CDD|107227 cd06470, ACD_IbpA-B_like, Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins IbpA and IbpB, and similar proteins. IbpA and IbpB are 16 kDa small heat shock proteins (sHsps). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. IbpA and IbpB are produced during high-level production of various heterologous proteins, specifically human prorenin, renin and bovine insulin-like growth factor 2 (bIGF-2), and are strongly associated with inclusion bodies containing these heterologous proteins. IbpA and IbpB work as an integrated system to stabilize thermally aggregated proteins in a disaggregation competent state. The chaperone activity of IbpB is also significantly elevated as the temperature increases from normal to heat shock. The high temperature results in the disassociation of 2-3-MDa IbpB oligomers into smaller approximately 600-kDa structures. This elevated activity seen under heat shock conditions is retained for an extended period of time after the temperature is returned to normal. IbpA also forms multimers
PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEENEEREYLHRGIAKRAFERSFNLAD
HVKVKGAELENGLLTIDLER
>gnl|CDD|107228 cd06471, ACD_LpsHSP_like, Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to Lactobacillus plantarum (Lp) small heat shock proteins (sHsp) HSP 18.5, HSP 18.55 and HSP 19.3. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Transcription of the genes encoding Lp HSP 18.5, 18.55 and 19.3 is regulated by a variety of stresses including heat, cold and ethanol. Early growing L. plantarum cells contain elevated levels of these mRNAs which rapidly fall of as the cells enter stationary phase. Also belonging to this group is Bifidobacterium breve (Bb) HSP20 and Oenococcus oenis (syn. Leuconostoc oenos) (Oo) HSP18. Transcription of the gene encoding BbHSP20 is strongly induced following heat or osmotic shock, and that of the gene encoding OoHSP18 following heat, ethanol or acid shock. OoHSP18 is peripherally associated with the cytoplasmic membrane
MKTDIKETDDEYIVEADLPGFKKEDIKLDYKDGYLTISAKRDESKDEKDKKGNYIRRERYYGSFSRSFYL
PNVDEEEIKAKYENGVLKITLPK
>gnl|CDD|107229 cd06472, ACD_ScHsp26_like, Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein (Hsp)26 and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. ScHsp26 is temperature-regulated, it switches from an inactive to a chaperone-active form upon elevation in temperature. It associates into large 24-mers storage forms which upon heat shock disassociate into dimers. These dimers initiate the interaction with non-native substrate proteins and re-assemble into large globular assemblies having one monomer of substrate bound per dimer. This group also contains Arabidopsis thaliana (Ath) Hsp15.7, a peroxisomal matrix protein which can complement the morphological phenotype of S. cerevisiae mutants deficient in Hsps26. AthHsp15.7 is minimally expressed under normal conditions and is strongly induced by heat and oxidative stress. Also belonging to this group is wheat HSP16.9 which differs in quaternary structure from the shell-type particles of ScHsp26, it assembles as a dodecameric double disc, with each disc organized as a trimer of dimers
RVDWKETPEAHVFKADVPGVKKEDVKVEVEDGRVLRISGERKKEEEKKGDDWHRVERSSGRFVRRFRLPE
NADADEVKAFLENGVLTVTVPK
>gnl|CDD|107230 cd06475, ACD_HspB1_like, Alpha crystallin domain (ACD) found in mammalian small (s)heat shock protein (Hsp)-27 (also denoted HspB1 in human) and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Hsp27 shows enhanced synthesis in response to stress. It is a molecular chaperone which interacts with a large number of different proteins. It is found in many types of human cells including breast, uterus, cervix, platelets and cancer cells. Hsp27 has diverse cellular functions including, chaperoning, regulation of actin polymerization, keratinocyte differentiation, regulation of inflammatory pathways in keratinocytes, and protection from oxidative stress through modulating glutathione levels. It is also a subunit of AUF1-containing protein complexes. It has been linked to several transduction pathways regulating cellular functions including differentiation, cell growth, development, and apoptosis. Its activity can be regulated by phosphorylation. Its unphosphorylated state is a high molecular weight aggregated form (100-800kDa) composed of up to 24 subunits, which forms as a result of multiple interactions within the ACD, and is required for chaperone function and resistance to oxidative stress. Upon phosphorylation these large aggregates rapidly disassociate to smaller oligomers and chaperone activity is modified. High constitutive levels of Hsp27 have been detected in various cancer cells, in particular those of carcinoma origin. Over-expression of Hsp27 has a protective effect against various diseases-processes, including Huntington's disease. Mutations in Hsp27 have been associated with a form of distal hereditary motor neuropathy type II and Charcot-Marie-Tooth disease type 2
GMSEIRQTADRWKVSLDVNHFAPEELVVKTKDGVVEITGKHEEKQDEHGFVSRCFTRKYTLPPGVDPTAV
TSSLSPDGILTVEAPI
>gnl|CDD|107231 cd06476, ACD_HspB2_like, Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB2/heat shock 27kDa protein 2 and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. HspB2 is preferentially and constitutively expressed in skeletal muscle and heart. HspB2 shows homooligomeric activity and forms aggregates in muscle cytosol. Although its expression is not induced by heat shock, it redistributes to the insoluble fraction in response to heat shock. In the mouse heart, HspB2 plays a role in maintaining energetic balance, by protecting cardiac energetics during ischemia/reperfusion, and allowing for increased work during acute inotropic challenge. hHspB2 [previously also known as myotonic dystrophy protein kinase (DMPK) binding protein (MKBP)] is selectively up-regulated in skeletal muscles from myotonic dystrophy patients. The ACD of hHspB2 binds the DMPK kinase domain. In vitro, hHspB2 enhances the kinase activity of DMPK and confers thermoresistance. The hHspB2 gene lies less than 1kb from the 5 prime end of the related alphaB (HspB4)-crystallin gene, with the opposite transcription direction. These two genes may share regulatory elements for their expression
QVESEDDKYQVFLDVCHFTPDEITVRTVDNLLEVSARHPQRMDRHGFVSREFTRTYILPMDVDPLLVRAS
LSHDGILCIQAPR
>gnl|CDD|107232 cd06477, ACD_HspB3_Like, Alpha crystallin domain (ACD) found in mammalian HspB3, also known as heat-shock protein 27-like protein (HSPL27, 17-kDa) and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. HspB3 is expressed in adult skeletal muscle, smooth muscle, and heart, and in several other fetal tissues. In muscle cells HspB3 forms an oligomeric 150 kDa complex with myotonic dystrophy protein kinase-binding protein (MKBP/ HspB2), this complex may comprise one of two independent muscle-cell specific chaperone systems. The expression of HspB3 is induced during muscle differentiation controlled by the myogenic factor MyoD. HspB3 may also interact with Hsp22 (HspB8)
DQEEGKPMFQILLDVVQFRPEDIIIQVFEGWLLIKGQHGVRMDEHGFISRSFTRQYQLPDGVEHKDLSAM
LCHDGILVVETKD
>gnl|CDD|107233 cd06478, ACD_HspB4-5-6, Alpha-crystallin domain found in alphaA-crystallin (HspB4), alphaB-crystallin (HspB5), and the small heat shock protein (sHsp) HspB6, also known as Hsp20. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. Only trace amounts of HspB4 are found in tissues other than the lens. HspB5 on the other hand is also expressed constitutively in other tissues including brain, heart, and type I and type IIa skeletal muscle fibers, and in several cancers including gliomas, renal cell carcinomas, basal-like and metaplastic breast carcinomas, and head and neck cancer. HspB5's functions include effects on the apoptotic pathway and on metastasis. Phosphorylation of HspB5 reduces its oligomerization and anti-apoptotic activities. HspB5 is protective in demyelinating disease such as multiple sclerosis (MS), being a negative regulator of inflammation. In early active MS lesions it is the most abundant gene transcript and an autoantigen, the immune response against it would disrupt its function and worsen inflammation and demyelination. Given as therapy for ongoing demyelinating disease it may counteract this effect. It is an autoantigen in the pathogenesis of various other inflammatory disorders including Lens-associated uveitis (LAU), and Behcet's disease. Mutations in HspB5 have been associated with diseases including dominant cataract and desmin-related myopathy. Mutations in HspB4 have been associated with Autosomal Dominant Congenital Cataract (ADCC). HspB6 (Hsp20) is ubiquitous and is involved in diverse functions including regulation of glucose transport and contraction of smooth muscle, in platelet aggregation, in cardioprotection, and in the prevention of apoptosis. It interacts with the universal scaffolding and adaptor protein 14-3-3, and also with the proapoptotic protein Bax
EVRLDKDRFSVNLDVKHFSPEELSVKVLGDFVEIHGKHEERQDEHGFISREFHRRYRLPPGVDPAAITSS
LSADGVLTISGPR
>gnl|CDD|107234 cd06479, ACD_HspB7_like, Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB7, also known as cardiovascular small heat shock protein (cvHsp), and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. HspB7 is a 25-kDa protein, preferentially expressed in heart and skeletal muscle. It binds the cytoskeleton protein alpha-filamin (also known as actin-binding protein 280). The expression of HspB7 is increased during rat muscle aging. Its expression is also modulated in obesity implicating this protein in this and related metabolic disorders. As the human gene encoding HspB7 is mapped to chromosome 1p36.23-p34.3 it is a positional candidate for several dystrophies and myopathies
GNVKTLGDTYQFAVDVSDFSPEDIIVTTSNNQIEVHAEKLASDGTVMNTFTHKCQLPEDVDPTSVSSSLG
EDGTLTIKARR
>gnl|CDD|107235 cd06480, ACD_HspB8_like, Alpha-crystallin domain (ACD) found in mammalian 21.6 KDa small heat shock protein (sHsp) HspB8, also denoted as Hsp22 in humans, and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. A chaperone complex formed of HspB8 and Bag3 stimulates degradation of protein complexes by macroautophagy. HspB8 also forms complexes with Hsp27 (HspB1), MKBP (HspB2), HspB3, alphaB-crystallin (HspB5), Hsp20 (HspB6), and cvHsp (HspB7). These latter interactions may depend on phosphorylation of the respective partner sHsp. HspB8 may participate in the regulation of cell proliferation, cardiac hypertrophy, apoptosis, and carcinogenesis. Point mutations in HspB8 have been correlated with the development of several congenital neurological diseases, including Charcot Marie tooth disease and distal motor neuropathy type II
GGPPEPRNPPPNSSEPWKVCVNVHSFKPEELTVKTKDGFVEVSGKHEEQQKEGGIVSKNFTKKIQLPPEV
DPVTVFASLSPEGLLIIEAPQ
>gnl|CDD|107236 cd06481, ACD_HspB9_like, Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB9 and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Human (h) HspB9 is expressed exclusively in the normal testis and in various tumor samples and is a cancer/testis antigen. hHspB9 interacts with TCTEL1 (T-complex testis expressed protein -1), a subunit of dynein. hHspB9 and TCTEL1 are co-expressed in similar cells within the testis and in tumor cells. Included in this group is Xenopus Hsp30, a developmentally-regulated heat-inducible molecular chaperone
EGKDGKEGFSLKLDVRGFSPEDLSVRVDGRKLVVTGKREKKNEDEKGSFSYEYQEFVREAQLPEHVDPEA
VTCSLSPSGHLHIRAPR
>gnl|CDD|107237 cd06482, ACD_HspB10, Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB10, also known as sperm outer dense fiber protein (ODFP), and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Human (h) HspB10 occurs exclusively in the axoneme of sperm cells and may have a cytoskeletal role
LAASCDSSNVLASVDVCGFEPDQVKVKVKDGKVQVSAERENRYDCLGSKKYSYMNICKEFSLPPGVDEKD
VTYSYGLGSVVKIETPC
>gnl|CDD|107238 cd06488, p23_melusin_like, p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related proteins. Melusin's tail domain interacts with the cytoplasmic domain of beta1-A and beta1-D isoforms of beta1 integrin, it does not bind other integrin beta subunits. Melusin is a muscle-specific protein expressed in skeletal and cardiac muscles but not in smooth muscle or other tissues. It is needed for heart hypertrophy following mechanical overload. The integrin-binding portion of this domain appears to be sequestered in the full length melusin protein, Ca2+ may modulate the protein's conformation exposing this binding site. This group includes Chordc1, also known as Chp-1, which is conserved from vertebrates to humans. Mammalian Chordc1 interacts with the heat shock protein (HSP) Hsp90 and is implicated in circadian and/or homeostatic mechanisms in the brain. The N-terminal portions of proteins belonging to this group contain two cysteine and histidine rich domain (CHORD) domains
CRHDWHQTGSHVVVSVYAKNSNPELSVVEANSTVLTIHIVFEGNKEFQLDIELWGVIDVEKSSVNMLPTK
VEIKLRKAEPGSWAKLE
>gnl|CDD|107239 cd06489, p23_CS_hSgt1_like, p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related proteins. hSgt1 is a co-chaperone which has been shown to be elevated in HEp-2 cells as a result of stress conditions such as heat shock. It interacts with the heat shock proteins (HSPs) Hsp70 and Hsp90, and it expression pattern is synchronized with these two Hsps. The interaction with HSP90 has been shown to involve the hSgt1_CS domain, and appears to be required for correct kinetochore assembly and efficient cell division. Some proteins in this subgroup contain a tetratricopeptide repeat (TPR) HSP-binding domain N-terminal to this CS domain, and most proteins in this subgroup contain a Sgt1-specific (SGS) domain C-terminal to the CS domain. The SGS domain interacts with some S100 family proteins. Studies suggest that S100A6 modulates in a Ca2+ dependent manner the interactions of hSgt1 with Hsp90 and Hsp70. The yeast Sgt1 CS domain is not found in this subgroup
DWYQTESQVVITILIKNVKPEDVSVEFEKRELSATVKLPSGNDYSLKLHLLHPIVPEQSSYKILSTKIEI
KLKKTEAIRWSKLE
>gnl|CDD|107240 cd06490, p23_NCB5OR, p23_like domain found in NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR) and similar proteins. NCB5OR is widely expressed in human organs and tissues and is localized in the ER (endoplasmic reticulum). It appears to play a critical role in maintaining viable pancreatic beta cells. Mice homozygous for a targeted knockout (KO) of the gene encoding NCB5OR develop an early-onset nonautoimmune diabetes phenotype with a non-inflammatory beta-cell deficiency. The role of NCB5OR in beta cells may be in maintaining or regulating their redox status. Proteins in this group in addition contain an N-terminal cytochrome b5 domain and a C-terminal cytochrome b5 oxidoreductase domain. The gene encoding NCB5OR has been considered as a positional candidate for type II diabetes and other diabetes subtypes related to B-cell dysfunction, however variation in its coding region does not appear not to be a major contributor to the pathogenesis of these diseases
YDWFQTDSEVTIVVYTKSKGNPADIVIVDDQQRELRVEIILGDKSYLLHLDLSNEVQWPCEVRISTETGK
IELVLKKKEPEKWTSLG
>gnl|CDD|107241 cd06492, p23_mNUDC_like, p23-like NUD (nuclear distribution) C-like domain of mammalian(m) NUDC and similar proteins. Mammalian(m) NUDC associates both with the dynein complex and also with an anti-inflammatory enzyme, platelet activating factor acetylhydrolase I, PAF-AH(I) complex, through binding mNUDF, the regulatory beta subunit of PAF-AH(I). mNUDC is important for cell proliferation both in normal and tumor tissues. Its expression is elevated in various cell types undergoing mitosis or stimulated to proliferate, with high expression levels observed in leukemic cells and tumors. For a leukemic cell line, human NUDC was shown to activate the thrombopoietin (TPO) receptor (Mpl) by binding to its extracellular domain, and promoting cell proliferation and differentiation
YRWTQTLSEVELKVPFKVSFRLKGKDVVVDIQRKHLKVGLKGQPPIIDGELYNEVKVEESSWLIEDGKVV
TVNLEKINKMEWWSRLV
>gnl|CDD|107242 cd06493, p23_NUDCD1_like, p23_NUDCD1: p23-like NUD (nuclear distribution) C-like domain found in human NUD (nuclear distribution) C domain-containing protein 1, NUDCD1 (also known as CML66), and similar proteins. NUDCD1/CML66 is a broadly immunogenic tumor associated antigen, which is highly expressed in a variety of solid tumors and in leukemias. In normal tissues high expression of NUDCD1/CML66 is limited to testis and heart
YYWQQTEEDLTLTIRLPEDTTKEDIRIKFLPDHISIALKDQAPLLEGKLYSSIDHESSTWIIKENKSLEV
SLIKKDEGPTWPELV
>gnl|CDD|107243 cd06494, p23_NUDCD2_like, p23-like NUD (nuclear distribution) C-like found in human NUDC domain-containing protein 2 (NUDCD2) and similar proteins. Little is known about the function of the proteins in this subgroup
VPCKTPWGCWYQTMDEVFIEVNVPPGTRAKDVKCKLGSRDISLAVKGQEVLKGKLFDSVVADECTWTLED
RKLIRIVLTKSNRDAGNCWKSLL
>gnl|CDD|107244 cd06495, p23_NUDCD3_like, p23-like NUD (nuclear distribution) C-like domain found in human NUDC domain-containing protein 3 (NUDCD3) and similar proteins. Little is known about the function of the proteins in this subgroup
GAVRENYTWSQDYTDVEVRVPVPKDVVKGRQVSVDLQSSSIRVSVRDGGGEKVLMEGEFTHKINTENSLW
SLEPGKCVLLSLSKCSEVWWNAVLKGEEEIDI
>gnl|CDD|107245 cd06497, ACD_alphaA-crystallin_HspB4, Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaA-crystallin (HspB4, 20kDa). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. Only trace amounts of HspB4 are found in tissues other than the lens. HspB5 does not belong to this group. Mutations inHspB4 have been associated with Autosomal Dominant Congenital Cataract (ADCC). The chaperone-like functions of HspB4 are considered important for maintaining lens transparency and preventing cataract
GISEVRSDRDKFTIYLDVKHFSPEDLTVKVLDDYVEIHGKHSERQDDHGYISREFHRRYRLPSNVDQSAI
TCSLSADGMLTFSGPK
>gnl|CDD|107246 cd06498, ACD_alphaB-crystallin_HspB5, Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaB-crystallin (HspB5, 20kDa). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. HspB4 does not belong to this group. HspB5 shows increased synthesis in response to stress. HspB5 is also expressed constitutively in other tissues including brain, heart, and type I and type IIa skeletal muscle fibers, and in several cancers including gliomas, renal cell carcinomas, basal-like and metaplastic breast carcinomas, and head and neck cancer. Its functions include effects on the apoptotic pathway and on metastasis. Phosphorylation of HspB5 reduces its oligomerization and anti-apoptotic activities. HspB5 is protective in demyelinating disease such as multiple sclerosis (MS), being a negative regulator of inflammation. In early active MS lesions it is the most abundant gene transcript and an autoantigen, the immune response against it would disrupt its function and worsen inflammation and demyelination. Given as therapy for ongoing demyelinating disease it may counteract this effect. It is an autoantigen in the pathogenesis of various other inflammatory disorders including Lens-associated uveitis (LAU), and Behcet's disease. Mutations in HspB5 have been associated with diseases including dominant cataract and desmin-related myopathy
EMRLEKDKFSVNLDVKHFSPEELKVKVLGDFIEIHGKHEERQDEHGFISREFQRKYRIPADVDPLTITSS
LSPDGVLTVCGPRK
>gnl|CDD|133460 cd06499, GT_MraY-like, Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine:polyprenol phosphate D-N-acetylhexosamine-1-phosphate transferases. They catalyze the transfer of a D-N-acetylhexosamine 1-phosphate to a membrane-bound polyprenol phosphate, which is the initiation step of protein N-glycosylation in eukaryotes and peptidoglycan biosynthesis in bacteria. One member, D-N-acetylhexosamine 1-phosphate transferase (GPT) is a eukaryotic enzyme, which is specific for UDP-GlcNAc as donor substrate and dolichol-phosphate as the membrane bound acceptor. The bacterial members MraY, WecA, and WbpL/WbcO utilize undecaprenol phosphate as the acceptor substrate, but use different UDP-sugar donor substrates. MraY-type transferases are highly specific for UDP-N-acetylmuramate-pentapeptide, whereas WecA proteins are selective for UDP-N-acetylglucosamine (UDP-GlcNAc). The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic endproducts implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The eukaryotic reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for N-glycosylation. The prokaryotic reactions lead to the formation of polyprenol-linked oligosaccharides involved in bacterial cell wall and peptidoglycan assembly. Archaeal and eukaryotic enzymes may use the same substrates and are evolutionarily closer than the bacterial enzyme. Archaea possess the same N-glycosylation pathway as eukaryotes. A glycosyl transferase gene Mv1751 in M. voltae encodes for the enzyme that carries out the first step in the pathway, the attachment of GlcNAc to a dolichol lipid carrier in the membrane. A lethal mutation in the alg7 (GPT) gene in Saccharomyces cerevisiae was successfully complemented with Mv1751, the archaea gene
PTPTMGGLAILLGFLLGVLLYIPHSNTLILLALLSGLVAGIVGFIDDLLGLKVELSEREKLLLQILAALF
LLLIGGGHTTVTTPLGFVLDLGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLSGQ
TTSALLFIILAGACLGFLYFNFYPAKIFMGDTGSYFLGAAYAAVA
>gnl|CDD|99748 cd06502, TA_like, Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway
DFRSDTVTGPTPEMLEAMAAANVGDDVYGEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHTQP
GGSVICHETAHIYTDEAGAPEFLSGVKLLPVPGENGKLTPEDLEAAIRPRDDIHFPPPSLVSLENTTEGG
TVYPLDELKAISALAKENGLPLHLDGARLANAAAALGVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNR
DFIARARRRRKQAGGGMRQSGFLAAAGLAALENDLWLRRLRHDHEMARRLAEALEELGGLESEVQTNIVL
LDPVEANAVFVELSKEAIERRGEGVLFYAWGEGGVRFVTHWDTTEEDVDELLSALKAV
>gnl|CDD|349951 cd06503, ATP-synt_Fo_b, F-type ATP synthase, membrane subunit b. Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens
TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEI
IEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG
>gnl|CDD|119382 cd06522, GH25_AtlA-like, AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain
KDVVDVSSNNGIMSVADYNKLKNYGVKAVIVKLTEGTTYRNPYAASQIANAKAAGLKVSAYHYAHYTSAA
DAQAEARYFANTAKSLGLSKNTVMVADMEDSSSSGNATANVNAFWQTMKAAGYKNTDVYTSASWLNSRAD
TSTLGAKRVWVAQYPYNPSSNNLWNTNYGAWQWTSQAHFPGRSGGFDVSIDY
>gnl|CDD|119383 cd06523, GH25_PlyB-like, PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues
AIVDISEWQGPINWDYDTLSKQLDLVIIRVQYGSNYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADAK
AEARDFYNRANKKPTFYVLDVEVTSMSDMNAGVQAFISELRRLGAKKVGLYIGHHFYTTFNLAVSKFDAI
WIPAYGSNPGTYPYDLWQYTDSGYLPGISGNVDLNRL
>gnl|CDD|119384 cd06524, GH25_YegX-like, YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins
FGIDVSHYQGKIDWQKVKAKVKDSPVAFVFIKATEGVDIVDPDFPTNWEGAKEAGIIRGAYHFYRPNSDP
KQQADNFLNTVKLLGPGDLPPVLDVEWDGRKSSAKQIQEGVLEWLDAVEKATGVKPIIYTNPSFWTDYLT
DSSFSEYPLWIADYNPRRKKVPPNESKKWLLWQYSDSGKVPGISGAVDLNVFNG
>gnl|CDD|119385 cd06525, GH25_Lyc-like, Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues
KGIDISNWQGNINFNAVKDSGVEVVYIKATEGTTFVDSYFNENYNGAKAAGLKVGFYHFLVGTSNPEEQA
ENFYNTIKGKKMDLKPALDVEVNFGLSKDELNDYVLRFIEEFEKLSGLKVGIYTYTSFINNNLDSRLSSY
PLWIANYGVSPPSSNGIWNSWVGFQYSETGRVNGVSGSVDLDEF
>gnl|CDD|107247 cd06526, metazoan_ACD, Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps
VVNDDDEKFQVTLDVKGFKPEELKVKVSDNKLVVEGKHEEREDEHGYVSREFTRRYQLPEGVDPDSVTSS
LSSDGVLTIEAPK
>gnl|CDD|132725 cd06528, RNAP_A'', A'' subunit of Archaeal RNA Polymerase (RNAP). Archaeal RNA polymerase (RNAP), like bacterial RNAP, is a large multi-subunit complex responsible for the synthesis of all RNAs in the cell. The relative positioning of the RNAP core is highly conserved between archaeal RNAP and the three classes of eukaryotic RNAPs. In archaea, the largest subunit is split into two polypeptides, A' and A'', which are encoded by separate genes in an operon. Sequence alignments reveal that the archaeal A'' subunit corresponds to the C-terminal one-third of the RNAPII largest subunit (Rpb1). In subunit A'', several loops in the jaw domain are shorter. The RNAPII Rpb1 interacts with the second-largest subunit (Rpb2) to form the DNA entry and RNA exit channels in addition to the catalytic center of RNA synthesis
PLLKEKLEEVLKEHGLTLSEAEEIIKEVLREYLRSLIEPGEAVGIVAAQSIGEPGTQMTLRTFHYAGVAE
INVTLGLPRLIEIVDARKEPSTPTMTIYLEEEYKYDREKAEEVARKIEETTLENLAEDISIDLFNMRITI
ELDEEMLEDRGITVDDVLKAIEKLKKGKVGEEGDVTLIVLKAEEPSIKELRKLAEKILNTKIKGIKGIKR
VIVRKEEDEYVIYTEGSNLKAVLKVEGVDPTRTTTNNIHEIEEVLGIEAARNAIINEIKRTLEEQGLDVD
IRHIMLVADIMTYDGEVRQIGRHGIAGEKPSVLARAAFEVTVKHLLDAAVRGEVDELRGVIENIIVGQPI
PLGTGDVELTMDP
>gnl|CDD|119397 cd06529, S24_LexA-like, Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response
FALRVKGDSMEPTIPDGDLVLVDPSDTPRDGDIVVARLDGELTVKRLQRRGGGRLRLISDNPAYPPIEID
EEELEIVGVVG
>gnl|CDD|119398 cd06530, S26_SPase_I, The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidase I, which is the most intensively studied, has two N-terminal transmembrane segments inserted in the plasma membrane and a hydrophilic, C-terminal catalytic region that is located in the periplasmic space. Although the bacterial signal peptidase I is monomeric, signal peptidases of eukaryotic cells commonly function as oligomeric complexes containing two divergent copies of the catalytic monomer. These are the IMP1 and IMP2 signal peptidases of the mitochondrial inner membrane that remove leader peptides from nuclear- and mitochondrial-encoded proteins. Also, two components of the endoplasmic reticulum signal peptidase in mammals (18-kDa and 21-kDa) belong to this family and they process many proteins that enter the ER for retention or for export to the Golgi apparatus, secretory vesicles, plasma membranes or vacuole. An atypical member of the S26 SPase type I family is the TraF peptidase which has the remarkable activity of producing a cyclic protein of the Pseudomonas pilin system. The type I signal peptidases are unique serine proteases that utilize a serine/lysine catalytic dyad mechanism in place of the classical serine/histidine/aspartic acid catalytic triad mechanism
EPVVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSPGDPGKPIIKRVIGYFVLGDNRNNSLDS
RYWGPVPEDDIVGKV
>gnl|CDD|133474 cd06532, Glyco_transf_25, Glycosyltransferase family 25 [lipooligosaccharide (LOS) biosynthesis protein] is a family of glycosyltransferases involved in LOS biosynthesis. The members include the beta(1,4) galactosyltransferases: Lgt2 of Moraxella catarrhalis, LgtB and LgtE of Neisseria gonorrhoeae and Lic2A of Haemophilus influenzae. M. catarrhalis Lgt2 catalyzes the addition of galactose (Gal) to the growing chain of LOS on the cell surface. N. gonorrhoeae LgtB and LgtE link Gal-beta(1,4) to GlcNAc (N-acetylglucosamine) and Glc (glucose), respectively. The genes encoding LgtB and LgtE are two genes of a five gene locus involved in the synthesis of gonococcal LOS. LgtE is believed to perform the first step in LOS biosynthesis
KIFVINLDRSTDRRERMEAQLAALGLDFEFFDAVDGKDLSEEELAALYDALFLPRYGRPLTPGEIGCFLS
HYKLWQKIVESNLEYALILEDDAILDPDGTAGYLVSRKGAKKLLAALEPIDLPVDVFL
>gnl|CDD|119439 cd06533, Glyco_transf_WecG_TagA, The glycosyltransferase WecG/TagA superfamily contains Escherichia coli WecG, Bacillus subtilis TagA and related proteins. E. coli WecG is believed to be a UDP-N-acetyl-D-mannosaminuronic acid transferase, and is involved in enterobacterial common antigen (eca) synthesis. B. subtilis TagA plays a key role in the Wall Teichoic Acid (WTA) biosynthetic pathway, catalyzing the transfer of N-acetylmannosamine to the C4 hydroxyl of a membrane-anchored N-acetylglucosaminyl diphospholipid to make ManNAc-beta-(1,4)-GlcNAc-pp-undecaprenyl. This is the first committed step in this pathway. Also included in this group is Xanthomonas campestris pv. campestris GumM, a glycosyltransferase participating in the biosynthesis of the exopolysaccharide xanthan
LNSADLVLPDGIGVVWAARLLGGPLPERVTGSDLMPALLELAAQKGLRVFLLGAKPEVLEKAAERLRARY
PGLKIVGYHHGYFGPEEEEEIIERINASGADILFVGLGAPKQELWIARHKDRLPVPVAIGVGGSFDFLAG
TVKRAPKWMQKLGLEWLYRLLQEPRRLWRRY
>gnl|CDD|143395 cd06534, ALDH-SF, NAD(P)+-dependent aldehyde dehydrogenase superfamily. The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group
AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLAD
KLGGPELPSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAE
LLQEAGLPPGVVNVVPGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIV
DEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDEFVEKLVTVLVDVDPDMPIAQEEIFGPVLPV
IRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFGGVKNSGIGRE
GGPYGLEEYTRTKTVVI
>gnl|CDD|119368 cd06535, CIDE_N_CAD, CIDE_N domain of CAD nuclease. The CIDE_N (cell death-inducing DFF45-like effector, N-terminal) domain is found at the N-terminus of CAD nuclease (caspase-activated DNase/DNA fragmentation factor, DFF40) and its inhibitor, ICAD(DFF45). These proteins are associated with the chromatin condensation and DNA fragmentation events of apoptosis; the CIDE_N domain is thought to regulate the activity of CAD/DFF40 and ICAD/DFF45 during apoptosis. In normal cells, DFF exists in the nucleus as a heterodimer composed of CAD/DFF40 as a latent nuclease and its chaperone and inhibitor subunit ICAD/DFF45. Apoptotic activation of caspase-3 results in the cleavage of DFF45/ICAD and the release of active DFF40/CAD nuclease
KPKCVKIRSLNSAQKYGVAAKNLKELLRKGCRLLQLPCAGSRLCLYEDGTEVTEEYFPTLPDNTELVLLT
PGQSWQG
>gnl|CDD|119369 cd06536, CIDE_N_ICAD, CIDE_N domain of ICAD. The CIDE_N (cell death-inducing DFF45-like effector, N-terminal) domain is found at the N-terminus of the CAD nuclease (caspase-activated DNase/DNA fragmentation factor, DFF40) and its inhibitor, ICAD (DFF45). These proteins are associated with the chromatin condensation and DNA fragmentation events of apoptosis; the CIDE_N domain is thought to regulate the activity of the CAD/DFF40 and ICAD/DFF45 during apoptosis. In normal cells, DFF exists in the nucleus as a heterodimer composed of CAD/DFF40 as a latent nuclease and its chaperone and inhibitor subunit ICAD/DFF45. Apoptotic activation of caspase-3 results in the cleavage of DFF45/ICAD and release of active DFF40/CAD nuclease
ELKPCVVCNVSRQKQHGVAASSLEELRIKACESLGFDSSSAPITLVLAEDGTIVEDEDYFLCLPPNTKFV
LLAENEKWAP
>gnl|CDD|119370 cd06537, CIDE_N_B, CIDE_N domain of CIDE-B proteins. The CIDE_N (cell death-inducing DFF45-like effector, N-terminal) domain is found at the N-terminus of the CIDE (cell death-inducing DFF45-like effector) proteins. These proteins are associated with the chromatin condensation and DNA fragmentation events of apoptosis; the CIDE_N domain is thought to regulate the activity of the CAD/DFF40, ICAD/DFF45 and CIDE nucleases during apoptosis. The CIDE protein family includes 3 members: CIDE-A, CIDE-B, and FSP27(CIDE-C). Based on sequence similarity with DFF40 and DFF45, CIDE proteins were initially characterized as mitochondrial activators of apoptosis. However, strong metabolic phenotypes of mice lacking CIDE-A and CIDE-B indicated that this family may play critical roles in energy balance
PQRPFRVCDHKRTVRKGLTAASLQELLAKALETLLLSGVLTLVLEEDGTAVDSEDFFELLEDDTCLMVLE
QGQSWSPKSGM
>gnl|CDD|119371 cd06538, CIDE_N_FSP27, CIDE_N domain of FSP27 proteins. The CIDE-N (cell death-inducing DFF45-like effector, N-terminal) domain is found in the FSP27/CIDE-C protein, which has been identified as a n adipocyte lipid droplet protein that negatively regulates lipolysis and promotes triglyceride accumulation. The CIDE protein family includes 3 members: CIDE-A, CIDE-B, and FSP27(CIDE-C). Based on sequence similarity with DFF40 and DFF45, CIDE proteins were initially characterized as mitochondrial activators of apoptosis. The CIDE-N domain of FSP27 is sufficient to increase apoptosis in vitro when overexpressed
RPRPFRVSNADRSLRKGIMADSLEDLLNKVLDALLLDCISSLVLDEDGTGVDTEEFFQALADNTVFMVLG
KGQKWKPPT
>gnl|CDD|119372 cd06539, CIDE_N_A, CIDE_N domain of CIDE-A proteins. The CIDE_N (cell death-inducing DFF45-like effector, N-terminal) domain is found at the N-terminus of the CIDE (cell death-inducing DFF45-like effector) proteins. These proteins are associated with the chromatin condensation and DNA fragmentation events of apoptosis; the CIDE_N domain is thought to regulate the activity of the CAD/DFF40, ICAD/DFF45, and CIDE nucleases during apoptosis. The CIDE protein family includes 3 members: CIDE-A, CIDE-B, and FSP27(CIDE-C). Based on sequence similarity with DFF40 and DFF45, the CIDE proteins were initially characterized as mitochondrial activators of apoptosis. However, strong metabolic phenotypes of mice lacking CIDE-A and CIDE-B indicated that this family may play critical roles in energy balance
PARPFRVSNHDRSSRRGVMASSLQELISKTLDALVITSGLVTLVLEEDGTVVDTEEFFQTLGDNTHFMVL
EKGQKWTP
>gnl|CDD|119343 cd06541, ASCH, ASC-1 homology or ASCH domain, a small beta-barrel domain found in all three kingdoms of life. ASCH resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation. The domain has been named after the ASC-1 protein, the activating signal cointegrator 1 or thyroid hormone receptor interactor protein 4 (TRIP4). ASC-1 is conserved in many eukaryotes and has been suggested to participate in a protein complex that interacts with RNA. It has been shown that ASC-1 mediates the interaction between various transciption factors and the basal transcriptional machinery
VLMFGDRYGQLVVSGRKTIEIRSLDIYEQLPKAGDYLIILDGQQPLAIAEVVKVEIMPMVNELSEEQEQA
EGEGDLTLLYELKEHAAFFKEELAPDMLLYAISFE
>gnl|CDD|119359 cd06542, GH18_EndoS-like, Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B
PISFGYFEVWDDKGASLQESLLNLPDSVDMVSLFAANINLDAATAVQFLLTNKETYIRPLQAKGTKVLLS
ILGNHLGAGFANNLSDAAAKAYAKAIVDTVDKYGLDGVDFDDEYSGYGKNGTSQPSNEAFVRLIKELRKY
MGPTDKLLTIDGYGQALSNDGEEVSPYVDYVIYQYYGSSSSSTQRNWNTNSPKIPPEKMVYTESFEEENG
GNSGSSAEQYARWTPAKGGKGGIGTYALDRDYYRPYDSAVSKALK
>gnl|CDD|119360 cd06543, GH18_PF-ChiA-like, PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus furiosus with a glycosyl hydrolase family 18 (GH18) catalytic domain as well as a cellulose-binding domain. Members of this domain family are found not only in archaea but also in eukaryotes and prokaryotes. PF-ChiA exhibits hydrolytic activity toward both colloidal and crystalline (beta/alpha) chitins at high temperature
TVFAPYVDVTLNPPPDLTTYAAATGVKAFTLAFIVASGGCKPAWGGSYPLDQGGWIKSDIAALRAAGGDV
IVSFGGASGTPLATSCTSADQLAAAYQKVIDAYGLTHLDFDIEGGALTDTAAIDRRAQALALLQKEYPDL
KISFTLPVLPTGLTPDGLNVLEAAAANGVDLDTVNIMTMDYGSSAGSQDMGAAAISAAESLHDQLKDLYP
KLSDAELWAMIGVTPMIGVNDVGSEVFTLADAQTLVDFAKEKGLGRLSMWSLNRDRPCPGGGASPTATCS
GVQQQDYDFSKIFA
>gnl|CDD|119361 cd06544, GH18_narbonin, Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons with unknown function. Narbonin has a glycosyl hydrolase family 18 (GH18) domain without the conserved catalytic residues and with no known enzymatic activity. Narbonin amounts to up to 3% of the total seed globulins of mature seeds and was thought to be a storage protein but was found to degrade too slowly during germination. This family also includes the VfNOD32 nodulin from Vicia faba
LFREYIGADFNGVTFSDVPINPKVEFHFILSFAIDYDTESNPTNGKFNPYWDTENLTPEAVKSIKAQHPN
VKVVISIGGRGVQNNPTPFDPSNVDSWVSNAVSSLTSIIQTYNLDGIDIDYEHFPADPDTFVECIGQLIT
ELKNNGVIKVASIAPSEDAEQSHYLALYNAYGDYIDYVNYQFYNYGVPTTVAKYVEFYDEVANNYPGKKV
LASFSTDGEDGANIPGEIFIGGCKRLKKNGSLPGVFIWNADDS
>gnl|CDD|119362 cd06545, GH18_3CO4_chitinase, The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an uncharacterized bacterial member of the family 18 glycosyl hydrolases with homologs found in Flavobacterium, Stigmatella, and Pseudomonas
VVGYLPNYDDLNALSPTIDFSKLTHINLAFANPDANGTLNANPVRSELNSVVNAAHAHNVKILISLAGGS
PPEFTAALNDPAKRKALVDKIINYVVSYNLDGIDVDLEGPDVTFGDYLVFIRALYAALKKEGKLLTAAVS
SWNGGAVSDSTLAYFDFINIMSYDATGPWWGDNPGQHSSYDDAVNDLNYWNERGLASKDKLVLGLPFYGY
GFYYNGIPTIRNKVAFAKQNYGGVMIWELSQDASGENSLLNAI
>gnl|CDD|119363 cd06546, GH18_CTS3_chitinase, GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen Coccidioides posadasii. CTS3 has a chitinase-like glycosyl hydrolase family 18 (GH18) domain; and has homologs in bacteria as well as fungi
RLVIYYQTTHPSNGDPISSLLLVTEKGIALTHLIVAALHINDDGNIHLNDHPPDHPRFTTLWTELAILQS
SGVKVMGMLGGAAPGSFSRLDDDDEDFERYYGQLRDMIRRRGLDGLDLDVEEPMSLDGIIRLIDRLRSDF
GPDFIITLAPVASALTGGEANLSGFDYRELEQARGDKIDFYNAQFYNGFGSMSSPSDYDAIVAQGWDPER
IVIGLLTNPDNGQGFVPFDTLSSTLSTLRQRYPNFGGVMGWEYFNA
>gnl|CDD|119364 cd06547, GH85_ENGase, Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of N-glycosylproteins. The beta-1,4-glycosyl bond located between two N-acetylglucosamine residues is hydrolyzed such that N-acetylglucosamine 1 remains with the protein and N-acetylglucosamine 2 forms the reducing end of the released glycan. ENGase is a key enzyme in the processing of free oligosaccharides in the cytosol of eukaryotes. Oligosaccharides formed in the lumen of the endoplasmic reticulum are transported into the cytosol where they are catabolized by cytosolic ENGases and other enzymes, possibly to maximize the reutilization of the component sugars. ENGases have an eight-stranded alpha/beta barrel topology and are classified as a family 85 glycosyl hydrolase (GH85) domain. The GH85 ENGases are sequence-similar to the family 18 glycosyl hydrolases, also known as GH18 chitinases. An ENGase-like protein is also found in bacteria and is included in this alignment model
LVCHDMMGGYTSDRPSQGSNSFNAYTFSYWQYVDTFVYFSHSAVTIPPADWINAAHRNGVPVLGTFIFEW
TGQVEWLEDFLKKDEDGSFPVADKLVEVAKYYGFDGWLINIETELGDAEKAKRLIAFLRYLKAKLHENVP
GSLVIWYDSMTEDGKLSWQNELNSKNKPFFDVCDGIFLNYWWTEESLERSVQLAEGLGRSPYDVYVGVDV
WGRGTKGGGGWNSDKALDEIKKAGLSVALFAPGWTYESFEEPDFFVKNESRFGESGDPFLTNDDKFWSGL
ATYVPEKSPITSLPFVTNFNTGSGYAFYVNGKKVSDSPWNNLSLQDILPTYRWIVSSNG
>gnl|CDD|119365 cd06548, GH18_chitinase, The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel
VVGYFTNWGIYGRNYFVTDDIPADKLTHINYAFADIDGDGGVVTSDDEAADEAAQSVDGGADTDDQPLKG
NFGQLRKLKQKNPHLKILLSIGGWTWSGGFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGSGG
APGNVARPEDKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFINLMTYD
FHGAWSNTTGHHSNLYASPADPPGGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWTGYTRYWDEVAKAP
YLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD
>gnl|CDD|119366 cd06549, GH18_trifunctional, GH18 domain of an uncharacterized family of bacterial proteins, which share a common three-domain architecture: an N-terminal glycosyl hydrolase family 18 (GH18) domain, a glycosyl transferase family 2 domain, and a C-terminal polysaccharide deacetylase domain
IALAFYTPWDDASFASLKRHAPRLDWLVPEWLNLTGPEGRIDVFVDPQGVAIIAAAKAHPKVLPLVQNIS
GGAWDGKNIARLLADPSARAKFIANIAAYLERNQADGIVLDFEELPADDLPKYVAFLSELRRRLPAQGKQ
LTVTVPADEADWNLKALARNADKLILMAYDEHYQGGAPGPIASQDWFESNLAQAVKKLPPEKLIVALGSY
GYDWTKGGNTKAISSEAAWLLAAHASAAVKFDDKASNATYFFYDDEGVSHEVWMLDAVTLFNQLKAVQRL
GPAGVALWRLGSEDPGLW
>gnl|CDD|119348 cd06550, TM_ABC_iron-siderophores_like, Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters involved in the uptake of siderophores, heme, vitamin B12, or the divalent cations Mg2+ and Zn2+. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The TMs are bundles of alpha helices that transverse the cytoplasmic membrane multiple times. The two ABCs bind and hydrolyze ATP and drive the transport reaction. Each TM has a prominent cytoplasmic loop which contacts an ABC and represents a conserved motif. The two TMs form either a homodimer (e.g. in the case of the BtuC subunits of the Escherichia coli BtuCD vitamin B12 transporter), a heterodimer (e.g. the TroC and TroD subunits of the Treponema pallidum general transition metal transporter, TroBCD), or a pseudo-heterodimer (e.g. the FhuB protein of the E. coli ferrichrome transporter, FhuBC). FhuB contains two tandem TMs which associate to form the pseudo-heterodimer. Both FhuB TMs are found in this hierarchy
LLAALLVGAALAVSGAILQSLTRNRLASPSILGISHGALLGVVLALLLGIGLSNYALGAFAFAGALAIAL
LVLLLASRGGLSPSKLILIGIVLSAFFSAGVILISLLSDDSLQDLNIWLFGSILGVTWEDLLILLIILLL
VLLLLLLLSRKLNLLTFDEDLAKSLGINVNLLRLLLLLLVALLVVAAVALVGVILFVGLIAPHLARRLFG
RSHRYLLPLSALLGAILLLLGDLLSRTLLPSELPVGPVTALLGAPYFLYLL
>gnl|CDD|153244 cd06551, LPLAT, Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis. Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene)
FRYLLLNFFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLILFLLLERGLRRDVYGLMDEELLERYPFF
TRLGAFSVDRDSPRSAAKSLKYVARLLSKPGSVVWIFPEGTRTRRDKRPLQFKPGVAHLAEKAGVPIVPV
ALRYTFELFEQFPEIFVRIGPPIPYAETALGEELAAELANRLTRLLD
>gnl|CDD|119344 cd06552, ASCH_yqfb_like, ASC-1 homology domain, subfamily similar to Escherichia coli Yqfb. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation
RILFFERYEEAILSGKKTATIRDGGESHLKPGDVVEVHTGERIFGEAEITSVEEKTLGELTDEDARQEGF
PSLEELKEALKEIYPGLKDDDEVYVIEFRL
>gnl|CDD|119345 cd06553, ASCH_Ef3133_like, ASC-1 homology domain, subfamily similar to Enterococcus faecalis Ef3133. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation
YEAWAFGDSPELADELAALVLAGKKTATCSALALYEAEEEPLPKVGDYSIILDGQGKPVCIIETTEVEVV
PFNDVTEEFAYAEGEGDRSLEYWRKAHEAFFTRELEEAGKEFTEDMLVVCERFEVVY
>gnl|CDD|119346 cd06554, ASCH_ASC-1_like, ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation. The domain has been named after the ASC-1 protein, the activating signal cointegrator 1 or thyroid hormone receptor interactor protein 4 (TRIP4). ASC-1 is conserved in many eukaryotes and has been suggested to participate in a protein complex that interacts with RNA. It has been shown that ASC-1 mediates the interaction between various transciption factors and the basal transcriptional machinery
MKALSIHQPWASLIVRGIKRIEGRSWATNYRGRLWIHASAKLPTKLDIEEVEEFYRILYKLDIELPTGYP
TGCLLGCVDVVDCLTQEEYREQYPWGKSEESPYAWVLANPRPL
>gnl|CDD|119347 cd06555, ASCH_PF0470_like, ASC-1 homology domain, subfamily similar to Pyrococcus furiosus Pf0470. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation
HEMGLEEEPFELIKSGKKTIEIRLNDEKRQQIKVGDKILFNDLDTGQQLLVKVVDIRKYDSFRELLEEEG
LEKVGPGVDSIEEGVKDTYKIYSKEQEKKYGVLAIEIRV
>gnl|CDD|119341 cd06556, ICL_KPHMT, Members of the ICL/PEPM_KPHMT enzyme superfamily catalyze the formation and cleavage of either P-C or C-C bonds. Typical members are phosphoenolpyruvate mutase (PEPM), phosphonopyruvate hydrolase (PPH), carboxyPEP mutase (CPEP mutase), oxaloacetate hydrolase (OAH), isocitrate lyase (ICL), 2-methylisocitrate lyase (MICL), and ketopantoate hydroxymethyltransferase (KPHMT)
LWLLQKYKQEKERFATLTAYDYSMAKQFADAGLNVMLVGDSQGMTVAGYDDTLPYPVNDVPYHVRAVRRG
APLALIVADLPFGAYGAPTAAFELAKTFMRAGAAGVKIEGGEWHIETLQMLTAAAVPVIAHTGLTPQSVN
TSGGDEGQYRGDEAGEQLIADALAYAPAGADLIVMECVPVELAKQITEALAIPLAGIGAGSGTDGQFLVL
ADAFGITGGHIPKFAKNFHAETGDIRAAAR
>gnl|CDD|119342 cd06557, KPHMT-like, Ketopantoate hydroxymethyltransferase (KPHMT) is the first enzyme in the pantothenate biosynthesis pathway. Ketopantoate hydroxymethyltransferase (KPHMT) catalyzes the first committed step in the biosynthesis of pantothenate (vitamin B5), which is a precursor to coenzyme A and is required for penicillin biosynthesis
IPDLQKMKKAGEKIVMLTAYDYPTAKLADEAGVDVILVGDSLGMVVLGYDSTLPVTLDEMIYHTRAVRRG
APRALVVADMPFGSYQTSPEQALRNAARLMKEAGADAVKLEGGAEVAETIRALVDAGIPVMGHIGLTPQS
VNQLGGYKVQGKTEEEAERLLEDALALEEAGAFALVLECVPAELAKEITEALSIPTIGIGAGPDCDGQVL
VWHDMLGLSPGFKPKFVKRYADLGELIREAVKAYVEEVKSGSFP
>gnl|CDD|119339 cd06558, crotonase-like, Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole
VLVERDGGVATITLNRPEKRNALSLEMLDELAAALDEAEADPDVRVVVLTGAGKAFCAGADLKELAALSD
AGEEARAFIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGG
GTQRLPRLVGPARARELLLTGRRISAEEALELGLVDEVVPDEELLAAALELARRL
>gnl|CDD|143472 cd06559, Endonuclease_V, Endonuclease_V, a DNA repair enzyme that initiates repair of nitrosative deaminated purine bases. Endonuclease_V (EndoV) is an enzyme that can initiate repair of all possible deaminated DNA bases. EndoV cleaves the DNA strand containing lesions at the second phosphodiester bond 3' to the lesion using Mg2+ as a cofactor. EndoV homologs are conserved throughout all domains of life from bacteria to humans. EndoV is encoded by the nfi gene and nfi null mutant mice have a phenotype prone to cancer. The ability of endonuclease V to recognize mismatches and abnormal replicative DNA structures suggests that the enzyme plays an important role in DNA metabolism. The details of downstream processing for the EndoV pathway remain unknown
LEEARKLQEELAKKVVLEDLGPGEVRLVAGVDVSYKKDGDLAVAAAVVLDYPDLEVVETAVAVGEVTFPY
IPGLLAFREGPPLLEALEKLKTKPDLLLVDGHGIAHPRRFGLASHLGVLLDLPTIGVAKSLLVGDGEEPG
EERGSFTPLYDDGEVVGAALRTRDGVKPVYVSPGHRIDLETAVELVLKCCKGYRLPEPTRLADLLSRE
>gnl|CDD|143473 cd06560, PriL, Archaeal/eukaryotic core primase: Large subunit, PriL. Primases synthesize the RNA primers required for DNA replication. Primases are grouped into two classes, bacteria/bacteriophage and archaeal/eukaryotic. The proteins in the two classes differ in structure and the replication apparatus components. The DNA replication machinery of archaeal organisms contains only the core primase, a simpler arrangement compared to eukaryotes. Archaeal/eukaryotic core primase is a heterodimeric enzyme consisting of a small catalytic subunit (PriS) and a large subunit (PriL). Although the catalytic activity resides within PriS, the PriL subunit is essential for primase function as disruption of the PriL gene in yeast is lethal. PriL is composed of two structural domains. Several functions have been proposed for PriL, such as the stabilization of PriS, involvement in the initiation of synthesis, the improvement of primase processivity, and the determination of product size
TLLDLIASSIAVERAIERVREALEGKIIESPELEDSVENEVLSFYIARVLVAALDDSILTRRFARAEAKI
AEERLRKESEEDLLEIAIELGYLKPDELIGIEVGIEDLPYKIPVSDYLKLAARLRGDKWRLVNRILRNGY
VYLTKEELLRLLREAIRERLLDGLPL
>gnl|CDD|132880 cd06561, AlkD_like, A new structural DNA glycosylase. This domain represents a new and uncharacterized structural superfamily of DNA glycosylases that form an alpha-alpha superhelix fold that are not belong to the identified five structural DNA glycosylase superfamilies (UDG, AAG/MNPG, MutM/Fpg and helix-hairpin-helix). DNA glycosylases removing alkylated base residues have been identified in all organisms investigated and may be universally present in nature. DNA glycosylases catalyze the first step in Base Excision Repair (BER) pathway by cleaving damaged DNA bases within double strand DNA to produce an abasic site. The resulting abasic site is further processed by AP endonuclease, phosphodiesterase, DNA polymerases, and DNA ligase functions to restore the DNA to an undamaged state. All glycosylase examined to date utilize a similar strategy for binding DNA and base flipping despite their structural diversity
EKMKKFMKNLGPGDPFLGVRTPDLRKIAKEFKKEDKLEEDHELAEALWHEEIREAQYLALDLLDKKELKE
EDLERFEPWIEYIDNWDLVDSLCANLLGKLLYAEPELDLLEEWAKSENEWVRRAAIVLLLRLIKKETDFD
LLLEIIERLLHDEEYFVQKAVGWALREYGKKDPERVIAFLEKNGLSMPRLTLRYAIE
>gnl|CDD|119332 cd06562, GH20_HexA_HexB-like, Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself
FPHRGLLLDTSRHFLSVDSIKRTIDAMAYNKLNVLHWHITDSQSFPLESPSYPELSKKGAYSPSEVYTPE
DVKEIVEYARLRGIRVIPEIDTPGHTGSWGQGYPELLTGCYAVWRKYCPEPPCGQLNPTNPKTYDFLKTL
FKEVSELFPDKYFHLGGDEVNFNCWNSNPEIQKFMKKNNGTDYSDLESYFIQRALDIVRSLGKTPIVWEE
VFDNGVYLLPKDTIVQVWGGSDELKNVLAAGYKVILSSYDFWYLDCGFGGWVGPGNDWCDPYKNWPRIYS
GTPEQKKLVLGGEACMWGEQVDDTNLDQRLWPRASALAERLWSGPSDTNLTDAEPRLVEFRCRLVRRG
>gnl|CDD|119333 cd06563, GH20_chitobiase-like, The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself
FSWRGLMLDVSRHFFPVDEVKRFIDLMALYKLNVFHWHLTDDQGWRIEIKKYPKLTEVGAWRGPTEIGLP
QGGGDGTPYGGFYTQEEIREIVAYAAERGITVIPEIDMPGHALAALAAYPELGCTGGPGSVVSVQGVVSN
VLCPGKPETYTFLEDVLDEVAELFPSPYIHIGGDEVPKGQWEKSPACQARMKEEGLKDEHELQSYFIKRV
EKILASKGKKMIGWDEILEGGLPPNATVMSWRGEDGGIKAAKQGYDVIMSPGQYLYLDYAQSKGPDEPAS
WAGFNTLEKVYSFEPVPGGLTPEQAKRILGVQANLWTEYIPTPERVEYMAFPRLLALAEVAWTPPEKKDW
EDFRKRL
>gnl|CDD|119334 cd06564, GH20_DspB_LnbB-like, Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself
EVRGFMLDVGRKYYSMDFLKDIIKTMSWYKMNDLQLHLNDNLIFNLDDMSTTVNNATYASDDVKSGNNYY
NLTANDGYYTKEEFKELIAYAKDRGVNIIPEIDSPGHSLAFTKAMPELGLKNPFSKYDKDTLDISNPEAV
KFVKALFDEYLDGFNPKSDTVHIGADEYAGDAGYAEAFRAYVNDLAKYVKDKGKTPRVWGDGIYYKGDTT
VLSKDVIINYWSYGWADPKELLNKGYKIINTNDGYLYIVPGAGYYGDYLNTEDIYNNWTPNKFGGTNATL
PEGDPQILGGMFAIWNDDSDAGISEVDIYDRIFPALPAFAEKTWGG
>gnl|CDD|119335 cd06565, GH20_GcnA-like, Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself
FRGVHLDLKRNAVPKVSYLKKLLRLLALLGANGLLLYYEDTFPYEGEPEVGRMRGAYTKEEIREIDDYAA
ELGIEVIPLIQTLGHLEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIEEMIRQVLELHPSKYIHIGMD
EAYDLGRGRSLRKHGNLGRGELYLEHLKKVLKIIKKRGPKPMMWDDMLRKLSIEPEALSGLPKLVTPVVW
DYYADLDEHDRPIGLWKKYGSVFAVAWGASAWKGATPPNDKHLENIKSWLKAAKKNGVQGILLTGWGDYG
HEAVLCELLPGLIPSLALALG
>gnl|CDD|143475 cd06567, Peptidase_S41, C-terminal processing peptidase family S41. Peptidase family S41 (C-terminal processing peptidase or CTPase family) contains very different subfamilies; it includes photosystem II D1 C-terminal processing protease (CTPase), interphotoreceptor retinoid-binding protein IRBP and tricorn protease (TRI). CTPase and TRI both contain the PDZ domain while IRBP, although being very similar to the tail-specific protease domain, lacks the PDZ insertion domain and hydrolytic activity. These serine proteases have distinctly different active sites: in CTPase, the active site consists of a serine/lysine catalytic dyad while in tricorn core protease, it is a tetrad (serine, histidine, serine, glutamate). CPases with different substrate specificities in different species include processing of D1 protein of the photosystem II reaction center in higher plants and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein; and others such as tricorn protease (TRI) act as a carboxypeptidase, involved in the degradation of proteasomal products. CTPase homolog IRBP, secreted by photoreceptors into the interphotoreceptor matrix, having arisen in the early evolution of the vertebrate eye, promotes the release of all-trans retinol from photoreceptors and facilitates its delivery to the retinal pigment epithelium
FDEAWRLLRENYYDPHGVDWDALRDRYVDLLDAVDDRELLAGALNGMLGELGDPHSRYLTIGYIRIPSFS
AESTAEELREALAELKKGVKGLILDLRNNPGGLLSAAVELASLFLPKGKIVVTTRRRGGNETEYVAPGGG
SLYDGPLVVLVNEGSASASEIFAGALQDLGRATLVGERTFGKGSVQTVFPLLDGSALKLTTAKYYTPSGR
SIEGKGVEPDIEVP
>gnl|CDD|119336 cd06568, GH20_SpHex_like, A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases
FAYRGLMLDVARHFFTVAEVKRYIDLLALYKLNVLHLHLTDDQGWRIEIKSWPKLTEIGGSTEVGGGPGG
YYTQEDYKDIVAYAAERHITVVPEIDMPGHTNAALAAYPELNCDGKAKPLYTGIEVGFSSLDVDKPTTYE
FVDDVFRELAALTPGPYIHIGGDEAHSTPHDDYAYFVNRVRAIVAKYGKTPVGWQEIARADLPAGTVAQY
WSDRAPDADAAAALDKGAKVILSPADKAYLDMKYDADSPLGLTWAGPVEVREAYDWDPAAYGPGVPDEAI
LGVEAPLWTETIRNLDDLEYMAFPRLAGVAEIGWSPQEARDWDDYKVRL
>gnl|CDD|119337 cd06569, GH20_Sm-chitobiase-like, The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself
DAPRFEYRGMHLDVARNFHSKETVLKLLDQMAAYKLNKLHLHLTDDEGWRLEIPGLPELTEVGAKRCHDL
SETTCLLPQLGSGPDTNNSGSGYYSRADYIEILKYAKARHIEVIPEIDMPGHARAAIKAMEARYRKLMAA
GKPAEAEEYRLSDPADTSQYLSVQFYTDNVINPCMPSTYRFVDKVIDEIARMHQEAGQPLTTIHFGGDEV
PEGAWGGSPACKAQLFAKEGSVKDVEDLKDYFFERVSKILKAHGITLAGWEDGLLGKDTTNVDGFATPYV
WNNVWGWGYWGGEDRAYKLANKGYDVVLSNATNLYFDFPYEKHPEERGYYWAGRFVDTKKVFSFMPDNLY
ANAEVTRDGDPIDDTALNGKVRLTLEGPKNILGLQGQLWSETIRTDEQLEYMVFPRLLALAERAWHKAPW
EADYQDTAVRKAALNADWNQFANTL
>gnl|CDD|119338 cd06570, GH20_chitobiase-like_1, A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This subgroup lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself
FPWRGLLIDVSRHFIPVAVIKRQLDAMASVKLNVFHWHLTDDQGFRIESKKYPKLQQKASDGLYYTQEQI
REVVAYARDRGIRVVPEIDVPGHASAIAVAYPELASGPGPYVIERGWGVFEPLLDPTNEETYTFLDNLFG
EMAELFPDEYFHIGGDEVDPKQWNENPRIQAFMKEHGLKDAAALQAYFNQRVEKILSKHGKKMIGWDEVL
HPDLPKNVVIQSWRGHDSLGEAAKAGYQGILSTGYYIDQPQPAAYHYRVDPMILGGEATMWAELVSEETI
DSRLWPRTAAIAERLWSAQDVRDEDDMYRRL
>gnl|CDD|119330 cd06571, Bac_DnaA_C, C-terminal domain of bacterial DnaA proteins. The DNA-binding C-terminal domain of DnaA contains a helix-turn-helix motif that specifically interacts with the DnaA box, a 9-mer motif that occurs repetitively in the replication origin oriC. Multiple copies of DnaA, which is an ATPase, bind to 9-mers at the origin and form an initial complex in which the DNA strands are being separated in an ATP-dependent step
IELIIEAVAEYFGISVEDLRSKSRKKEIALARQIAMYLARELTGLSLPEIGRAFGGRDHSTVLHAVRKIE
ELLEEDPELKEDVEELEKKL
>gnl|CDD|119329 cd06572, Histidinol_dh, Histidinol dehydrogenase, HisD, E.C 1.1.1.23. Histidinol dehydrogenase catalyzes the last two steps in the L-histidine biosynthesis pathway, which is conserved in bacteria, archaea, fungi, and plants. These last two steps are (i) the NAD-dependent oxidation of L-histidinol to L-histidinaldehyde, and (ii) the NAD-dependent oxidation of L-histidinaldehyde to L-histidine. In most fungi and in the unicellular choanoflagellate Monosiga bevicollis, the HisD domain is fused with units that catalyze the second and third biosynthesis steps in this same pathway
VEETVREIIEDVRERGDEALLEYTEKFDGVELESLRVSEEEIDAAYAAVDPELKEAIELAAENIRAFHEA
QLPKDWEVETEPGVVLGQRYRPIERVGLYVPGGTAPYPSTVLMLAIPAKVAGVKEIVVVTPPRKDGKINP
AILAAAKLAGVDEIYKVGGAQAIAALAYGTETIPKVDKIVGPGNIYVTAAKRLVSGDVGIDMPAGPSEVL
VIADETANPEFVAADLLSQAEHDPDSQAILVTTSEELAEAVEEEVERQLAELPRREIAAKSLLDYGAIIL
VDDLEEAIELANEYAPEHLELQTEDPEELLEKIRNAGSIFLGPYTPEALGDYAAGPNHVLPTGGTARFYS
GLSVDDFLKRITVQEYSKEGLRALAPAVATLAEAEGLEAH
>gnl|CDD|119325 cd06573, PASTA, PASTA domain. This domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. It is a small globular fold consisting of 3 beta-sheets and an alpha-helix. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain
EVPDLVGISKKDLEEQLYDLLKLDASGSGNKVVKQSPEAGTKVAEGSTIRIYL
>gnl|CDD|119320 cd06574, TM_PBP1_branched-chain-AA_like, Transmembrane subunit (TM) of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters which are involved in the uptake of branched-chain amino acids (AAs), as well as TMs of transporters involved in the uptake of monosaccharides including ribose, galactose, and arabinose. These transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. This group includes Escherichia coli LivM and LivH, two TMs which heterodimerize to form the translocation pathway of the E. coli branched-chain AA LIV-1/LS transporter. This transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) and LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine. Included in this group are proteins from transport systems that contain a single TM which homodimerizes to generate the transmembrane pore; for example E. coli RbsC, AlsC, and MglC, the TMs of the high affinity ribose transporter, the D-allose transporter and the galactose transporter, respectively. The D-allose transporter may also to be involved in low affinity ribose transport
GLIYAILALGVYIVFRILGFPDLTVDGSFPLGAAVAAILIVAGYNPWLALIAAILAGAAAGLVTGFLHTR
LKINGLLAGILIMIGLYSINLRIMGGPNIPLGTRDTLLGLLLLFGISGTLSIPVVLLLIVLLVLFLVIWF
LRTKLGLAMRATGDNPDMARSLGINVDRTRILGLVISNALAALGGALYAQYQGFADVNMGIGTGVIGLAA
VIIGGAIVGRRTIKASILGVIIGAILYRIALALALGSGLIPSDLKLITAGVIVLVL
>gnl|CDD|119326 cd06575, PASTA_Pbp2x-like_2, PASTA domain of PBP2x-like proteins, second repeat. Penicillin-binding proteins (PBPs) are the major targets for beta-lactam antibiotics, like penicillins and cephalosporins. Beta-lactam antibiotics specifically inhibit transpeptidase activity by acylating the active site serine. PBPs catalyze key steps in the synthesis of the peptidoglycan, such as the interconnecting of glycan chains (polymers of N-glucosamine and N-acetylmuramic acid residues) and the cross-linking (transpeptidation) of short stem peptides, which are attached to glycan chains. Peptidoglycan is essential in cell division and protects bacteria from osmotic shock and lysis. PBP2x is one of the two monofunctional high molecular mass PBPs in Streptococcus pneumoniae and has been seen as the primary PBP target in beta-lactam-resistant strains. The PASTA domain is found at the C-termini of several PBPs and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain
TMPDLTGWSKRDALKLLELLGLKVKFSGSGYVVSQSIAPGTKVKKGTTITVTLK
>gnl|CDD|119327 cd06576, PASTA_Pbp2x-like_1, PASTA domain of PBP2x-like proteins, first repeat. Penicillin-binding proteins (PBPs) are the major targets for beta-lactam antibiotics, like penicillins and cephalosporins. Beta-lactam antibiotics specifically inhibit transpeptidase activity by acylating the active site serine. PBPs catalyze key steps in the synthesis of the peptidoglycan, such as the interconnecting of glycan chains (polymers of N-glucosamine and N-acetylmuramic acid residues) and the cross-linking (transpeptidation) of short stem peptides, which are connected to glycan chains. Peptidoglycan is essential in cell division and protects bacteria from osmotic shock and lysis. PBP2x is one of the two monofunctional high molecular mass PBPs in Streptococcus pneumoniae and has been seen as the primary PBP target in beta-lactam-resistant strains. The PASTA domain is found at the C-termini of several PBPs and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain
KVPDVTGKSVEEAKKELKEAGLQPVVIGNGKKVKKQSPKPGEKVLEGSKVLLYTD
>gnl|CDD|119328 cd06577, PASTA_pknB, PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain
TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS
>gnl|CDD|119440 cd06578, HemD, Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole (linear) to uroporphyrinogen-III, the fourth step in the biosynthesis of heme. This ubiquitous enzyme is present in eukaryotes, bacteria and archaea. Mutations in the human uroporphyrinogen-III synthase gene cause congenital erythropoietic porphyria, a recessive inborn error of metabolism also known as Gunther disease
VLVTRPRPQADELAALLEALGAEVLELPLIEIEPLDDAELDAALADLDEYDWLIFTSPNAVEAFFEALEE
LGLRALAGLKIAAVGPKTAEALREAGLTADFVPEEGDSEGLLELLELQDGKGKRILRPRGGRAREDLAEA
LRERGAEVDEVEVYRTVPPDLDAELLELLEEGAIDAVLFTSPSTVRNLLELLGKEGRALLKNVKIAAIGP
RTAEALRELGLKVVIVAESPTLEALLEAL
>gnl|CDD|119321 cd06579, TM_PBP1_transp_AraH_like, Transmembrane subunit (TM) of Escherichia coli AraH and related proteins. E. coli AraH is the TM of a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of the monosaccharide arabinose. This group also contains E. coli RbsC, AlsC, and MglC, which are TMs of other monosaccharide transporters, the ribose transporter, the D-allose transporter and the galactose transporter, respectively. The D-allose transporter may also be involved in low affinity ribose transport. These transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. Proteins in this subgroup have a single TM which homodimerizes to generate the transmembrane pore
AAVLGILALGMTLVIITGGIDLSVGSVAALSAVVAALLLVNAGLPIPLAILAALAVGALIGLLNGLLVAY
LRIPPFIVTLGTMFILRGLALLITGGRPISGLPPLFSFFLGGGLILGIPVPVLIALAVALVAWFLLRRTR
FGRYLYAVGGNPEAARLSGINVRRVKILAYVLSGLLAGLAGILLAARLGSAQPTAGNGYELDAIAAVVLG
GTSLTGGRGSVLGTLLGALLLGVLNNGLNLLGVSSFWQQIVKGAILLLAVALD
>gnl|CDD|119322 cd06580, TM_PBP1_transp_TpRbsC_like, Transmembrane subunit (TM) of Treponema pallidum (Tp) RbsC-1, RbsC-2 and related proteins. This is a functionally uncharacterized subgroup of TMs which belong to a larger group of TMs of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters, which are mainly involved in the uptake of branched-chain amino acids (AAs) or in the uptake of monosaccharides including ribose, galactose, and arabinose, and which generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction
ATPLILAALGVAISFRAGVFNIGLEGQMLLGAFAAALVALYLGLPATGSLPLGLLAAALAGALWALLPAL
LKAKLGVNEVISGLMLNYIALGLTSYLLLLALLLVILVWLLLYRTRFGLRLRAVGENPRAARYAGINVKR
VRLLAMLISGALAGLAGAYLVLGVQGRFTEGMSAGYGFIAIAVALLGRWNPLGILLAALLFGALEAGGIA
LQRSGGVPSELVQVLPGIIVLFVL
>gnl|CDD|119323 cd06581, TM_PBP1_LivM_like, Transmembrane subunit (TM) of Escherichia coli LivM and related proteins. LivM is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivM forms a heterodimer with another TM, LivH, to generate the transmembrane pore. LivH is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine
ILIYAILALGLNLLLGYAGQLSLGHAAFFGIGAYTAALLATRLGLPFWLALLAAGLVAALVGLLLGLPAL
RLRGVYFAIATLAFAEIVRLLALNWSSLTGGSNGLSGIPPPLLGGLLLSSPLAFYYLVLAVLLLVLLLLR
RLVRSPFGRALRAIRENEVAAEALGINVTRYKLLAFALSAALAGLAGALYAHYLGFVSPESFGFALSIEL
LLMVVLGGLGSLLGPVLGAALLVLLPELLRSLGPGLRLLVFGLLLILVVLFLPRGLVG
>gnl|CDD|119324 cd06582, TM_PBP1_LivH_like, Transmembrane subunit (TM) of Escherichia coli LivH and related proteins. LivH is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivH forms a heterodimer with another TM, LivM, to generate the transmembrane pore. LivM is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine
GLALGAIYALIALGLTLIFGVTGVINFAHGEFYMLGAYVAYTLLVALGLPFWLALLLALLVAALLGVLLE
RLVLRPLRGAPLLTLLITFGGLLILLQGLLLIFGGDPRVPPPPLLSGSVELGGVTIPPYRLFIIAVALVL
LAALYLFLRRTRLGRAIRAVAQNPEAARLLGINVRRVFALTFALGAALAGLAGVLLAPITGVSPTMGLLL
LLKAFAAVVLGGLGSIPGAVVGGLLLGLAESLAAAYLSSGYKDAVAFVLLILVLLVRPQGLF
>gnl|CDD|133475 cd06583, PGRP, Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity
PVKYVVIHHTANPNCYTAAAAVRYLQNYHMRGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGNYNSYSI
GIELIGNFDGGPPTAAQLEALAELLAYLVKRYGIPPDYRIVGHRDVSPGTECPGDA
>gnl|CDD|132915 cd06586, TPP_enzyme_PYR, Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes. Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit
AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTG
LLNAINGLADAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRT
AYASQGPVVVRLPR
>gnl|CDD|319898 cd06587, VOC, vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases
HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLGPGLRLALLEGPEPERPGGGGLFHLAFEVDDV
DEVDERLREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF
>gnl|CDD|319899 cd06588, PhnB_like, Escherichia coli PhnB and similar proteins. The Escherichia coli phnB gene is found next to an operon of fourteen genes (phnC-to-phnP) related to the cleavage of carbon-phosphorus (C-P) bonds in unactivated alkylphosphonates, supporting bacterial growth on alkylphosphonates as the sole phosphorus source. It was originally considered part of that operon. PhnB appears to play no direct catalytic role in the usage of alkylphosphonate. Although many of the proteins in this family have been annotated as 3-demethylubiquinone-9 3-methyltransferase enzymes by automatic annotation programs, the experimental evidence for this assignment is lacking. In Escherichia coli, the gene coding 3-demethylubiquinone-9 3-methyltransferase enzyme is ubiG, which belongs to the AdoMet-MTase protein family. PhnB-like proteins adopt a structural fold similar to bleomycin resistance proteins, glyoxalase I, and type I extradiol dioxygenases
ITPYLWFNGNAEEALEFYAEVFPGGEILSLTRYGEGPPDFPEGDEGKVMHAEFTLGGQTLMASDDGPGFP
FTFGNAISLSVDCDSQEEADRLFEKLSEGGEVLMPLQETFWGARYGWVKDKFGVSWQIN
>gnl|CDD|269876 cd06589, GH31, glycosyl hydrolase family 31 (GH31). GH31 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite -1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively
GRPPLLPKWALGFWNSRYGYYSEDEVEELVDRYREEGIPLDGFVLDSDWMDWGGNWGGFTWNREKFPDPK
GMIDELHDKGVKLGLIVKPRLRDWWWENIKKLLLEQGVDGWWTDMGEPLPFDDATFHNGGKAQKIHNAYP
LNMAEATYEGQKKTFPNKRPFILSRSGYAGAQRYPAIWSGDNTTTWDSLAFQIRAGLSASLSGVGYWGHD
IGGFTGGDPDKELYTRWVQFGAFSPIFRLHGDNSPRDKEPWVYGEEALAIFRKYL
>gnl|CDD|260000 cd06590, RNase_HII_bacteria_HIII_like, Bacterial type 2 ribonuclease, HII and HIII-like. This family includes type 2 RNases H from several bacteria, such as Bacillus subtilis, which have two different RNases, HII and HIII. RNases HIII are distinguished by having a large (70-90 residues) N-terminal extension of unknown function. In addition, the active site of RNase HIII differs from that of other RNases H; replacing the fourth residue (aspartate) of the acidic "DEDD" motif with a glutamate. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes; however, no prokaryotic genomes contain the combination of both RNase HI and HIII. This mutual exclusive gene inheritance might be the result of functional redundancy of RNase HI and HIII in prokaryotes. Ribonuclease (RNase) H is classified into two families, type I (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type II (prokaryotic RNase HII and HIII, archaeal RNase HII and eukaryotic RNase H2/HII). RNase H endonucleolytically hydrolyzes an RNA strand when it is annealed to a complementary DNA strand in the presence of divalent cations, in DNA replication or repair
HIGSDEVGKGDYFGPLVVAAVYVDKEDIEFLKELGVKDSKKLTDKKIIKLAPKIKEKIPYSLLVLDPEKY
NELYAKGKNLNKLKAWLHNQAIENLLKKKKKPKFILIDQFASEKVYYNYLKKEKIKKIPLYFETKAESKD
LAVAAASILARYAFLEEMDKLSKEYGMKLPKGASAKVDQAAAEIVKKYGKEELKKVAKLHFKNTKKI
>gnl|CDD|269877 cd06591, GH31_xylosidase_XylS, xylosidase XylS-like. XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in prokaryotes, eukaryotes, and archaea, that catalyzes the release of alpha-xylose from the non-reducing terminal side of the alpha-xyloside substrate. XylS has been characterized in Sulfolobus solfataricus where it hydrolyzes isoprimeverose, the p-nitrophenyl-beta derivative of isoprimeverose, and xyloglucan oligosaccharides, and has transxylosidic activity. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. The XylS family corresponds to subgroup 3 in the Ernst et al classification of GH31 enzymes
GKAPMLPKWALGFWQSKERYKTQEELLEVAREYRERGIPLDVIVQDWFYWTEQGWGDMKFDPERFPDPKG
MVDELHKMNVKLMISVWPTFGPGSENYKELDEKGLLLRTNRGNGGFGGGTAFYDATNPEAREIYWKQLKD
NYFDKGIDAWWLDATEPELDPYDFDNYDGRTALGPGAEVGNAYPLMHAKGIYEGQRATGPDKRVVILTRS
AFAGQQRYGAAVWSGDISSSWETLRRQIPAGLNFGASGIPYWTTDIGGFFGGDPEPGEDDPAYRELYVRW
FQFGAFCPIFRSHGTRPPREPNEIWSYGEEAYDILVKYIKLR
>gnl|CDD|269878 cd06592, GH31_NET37, glucosidase NET37. NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31), it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein
RPPIWSTWAEYKYNINQEKVLEYAEEIRANGFPPSVIEIDDGWQTYYGDFEFDPEKFPDPKGMIDKLHEM
GFRVTLWVHPFINPDSPNFRELRDKGYLVKEDSGGPPLIVKWWNGYGAVLDFTNPEARDWFKERLRELQE
DYGIDGFKFDAGEASYLPADPATFPSGLNPNEYTTLYAELAAEFGLLNEVRSGWKSQGLPLFVRMSDKDS
HWGYWNGLRSLIPTALTQGLLGYPFVLPDMIGGNAYGNFPPDKELYIRWLQLSAFMPAMQFSVAPWRNYD
EEVVDIARKLAKLREKLLPYIYELAAEAVDTGEPIIRPLWWIAPEDEEALTIDDQFLLGDDILVAPVLEK
GARSRDVYLPKGRW
>gnl|CDD|269879 cd06593, GH31_xylosidase_YicI, alpha-xylosidase YicI-like. YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) enzyme that catalyzes the release of an alpha-xylosyl residue from the non-reducing end of alpha-xyloside substrates such as alpha-xylosyl fluoride and isoprimeverose. YicI forms a homohexamer (a trimer of dimers). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. The YicI family corresponds to subgroup 4 in the Ernst et al classification of GH31 enzymes
GRPPLPPAWSFGLWLSRSFYYSEEEVLEVADGMRERGIPCDVIHLDCFWMKEDWWCDFEWDEERFPDPEG
MIARLKEKGFKVCLWINPYISQDSPLFKEAAEKGYLVKNPDGSPWHQWDGWQPGMGIIDFTNPEAVAWYK
EKLKRLLDMGVDVIKTDFGERIPEDAVYYDGSDGRKMHNLYPLLYNKAVYEATKEVKGEEAVLWARSAWA
GSQRYPVHWGGDSESTFEGMAASLRGGLSLGLSGFGFWSHDIGGFEGTPSPELYKRWTQFGLLSSHSRLH
GSTPREPWEYGEEALDVVRKFAKLRYRL
>gnl|CDD|269880 cd06594, GH31_glucosidase_YihQ, alpha-glucosidase YihQ-like. YihQ is a bacterial alpha-glucosidase with a conserved glycosyl hydrolase family 31 (GH31) domain that catalyzes the release of an alpha-glucosyl residue from the non-reducing end of alpha-glucoside substrates such as alpha-glucosyl fluoride. Orthologs of YihQ that have not yet been functionally characterized are present in plants and fungi. YihQ has sequence similarity to other GH31 enzymes such as CtsZ, a 6-alpha-glucosyltransferase from Bacillus globisporus, and YicI, an alpha-xylosidase from Echerichia coli. These latter two belong to different GH31 subfamilies than YihQ. In bacteria, YihQ (along with YihO) is important for bacterial O-antigen capsule assembly and translocation
GRQPPLPDWVYDGAILGLQGGTDKVLEVLEQLLAAGVPVAAVWLQDWVGTRKTSFGKRLWWNWEWDEELY
PGWDELVKELKEQGIRVLGYINPFLANVGPLYSYKEAEEKGYLVKNKTGEPYLVDFGEFDAGLVDLTNPE
ARRWFKEVIKENMIDFGLSGWMADFGEYLPFDAVLHSGEDAALYHNRYPELWARLNREAVEEAGKEGEIV
FFMRSGYTGSPRYSTLFWAGDQNVDWSRDDGLKSVIPGALSSGLSGFSLTHSDIGGYTTLFNPLVGYKRS
KELLMRWAEMAAFTPVMRTHEGNRPDDNAQFYSDAETLAHFARMA
>gnl|CDD|269881 cd06595, GH31_u1, glycosyl hydrolase family 31 (GH31); uncharacterized subgroup. This family represents an uncharacterized GH31 enzyme subgroup found in bacteria and eukaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein
TGKPPLIPRYALGNWWSRYWAYSDDDILDLVDNFKRNEIPLSVLVLDMDWHITDKKYKNGWTGYTWNKEL
FPDPKGFLDWLHERGLRVGLNLHPAEGIRPHEEAYAEFAKYLGIDPAKIIPIPFDVTDPKFLDAYFKLLI
HPLEKQGVDFWWLDWQQGKDSPLAGLDPLWWLNHYHYLDSGRNGKRRPLILSRWGGLGSHRYPIGFSGDT
EVSWETLAFQPYFTATAANVGYSWWSHDIGGHKGGIEDPELYLRWVQFGVFSPILRLHSDKGPYYKREPW
LWDAKTFEIAKDYLRLRHRLIPYL
>gnl|CDD|269882 cd06596, GH31_CPE1046, Clostridium CPE1046-like. CPE1046 is an uncharacterized Clostridium perfringens protein with a glycosyl hydrolase family 31 (GH31) domain. The domain architecture of CPE1046 and its orthologs includes a C-terminal fibronectin type 3 (FN3) domain and a coagulation factor 5/8 type C domain in addition to the GH31 domain. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein
LTGKPVLLPEWALYLGDADCYNRDYWVKVPGGISLNGEPGNTTDDARAVADKYKEHDMPLGWFLPNDGYG
CGYGQLDSTVANLKELGFETGLWTQSGLRDIAKEVGDAGVRALKTDVAWVGAGYSFALNGVEDAADGIEN
NSNARPFIWTVDGWAGTQRYAVIWTGDQSGSWEYIRFHIPTYIGSGLSGQAYATSDVDGIFGGSPETYTR
DLQWKAFTPVLMNMSGWAANDKQPWVFGEPYTSINRKYLKLKMRLMPYIYTYAREASVTGLPMVRAMFLE
YPNDPTAYGTATQYQFMWGPDFLVAPVYQNTAAGNDVRNGIYLPAGTWIDYWTG
>gnl|CDD|269883 cd06597, GH31_transferase_CtsY, CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like. CtsY is a bacterial 3-alpha-isomaltosyltransferase, first identified in Arthrobacter globiformis, that produces cyclic tetrasaccharides together with a closely related enzyme CtsZ. CtsY and CtsZ both have a glycosyl hydrolase family 31 (GH31) catalytic domain; CtsZ belongs to a different subfamily. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein
GRAALPPKWAFGHWVSANEWNSQAEVLELVEEYLAYDIPVGAVVIEAWSDEATFYIFNDATGKWPDPKGM
IDSLHEQGIKVILWQTPVVKTDGTDHAQKSNDYAEAIAKGYYVKNGDGTPYIPEGWWFGGGSLIDFTNPE
AVAWWHDQRDYLLDELGIDGFKTDGGEPYWGEDLIFSDGKKGREMRNEYPNLYYKAYFDYIREIGNDGVL
FSRAGDSGAQRYPIGWVGDQDSTFEGLQSALKAGLSAAWSGYPFWGWDIGGFSGPLPTAELYLRWTQLAA
FSPIMQNHSEKNHRPWSEERRWNVAERTGDPEVLDIYRKYVKLRME
>gnl|CDD|269884 cd06598, GH31_transferase_CtsZ, CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like. CtsZ is a bacterial 6-alpha-glucosyltransferase, first identified in Arthrobacter globiformis, that produces cyclic tetrasaccharides together with a closely related enzyme CtsY. CtsZ and CtsY both have a glycosyl hydrolase family 31 (GH31) catalytic domain; CtsY belongs to a different subfamily. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein
GRPPLPPKWAFGLWQSEFGYDNWAEVDELVDTLRQKDFPLDGVVLDLYWFGGIIASPDGPMGDLDWDRKA
FPDPAKMIADLKQQGVGTILIEEPYVLKNSDEYDELVKKGLLAKDKAGKPEPTLFNFWFGEGGMIDWSDP
EARAWWHDRYKDLIDMGVAGWWTDLGEPEMHPPDMVHADGDAADVHNIYNLLWAKSIYDGYQRNFPEQRP
FIMSRSGTAGSQRYGVIPWSGDIGRTWGGLASQINLQLHMSLSGIDYYGSDIGGFARGETLDPELYTRWF
QYGAFDPPVRPHGQNLCNPETAPDREGTKAINRENIKLRYQLLPYYYSLAYR
>gnl|CDD|269885 cd06599, GH31_glycosidase_Aec37, E.coli Aec37-like. Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family represented by Escherichia coli protein Aec37. The gene encoding Aec37 (aec-37) is located within a genomic island (AGI-3) isolated from the extraintestinal avian pathogenic Escherichia coli strain BEN2908. The function of Aec37 and its orthologs is unknown; however, deletion of a region of the genome that includes aec-37 affects the assimilation of seven carbohydrates, decreases growth rate of the strain in minimal medium containing galacturonate or trehalose, and attenuates the virulence of E. coli BEN2908 in chickens. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein
GRPALPPRWSLGYLGSTMYYTEAPDAQEQILDFIDTCREHDIPCDGFHLSSGYTSIEDGKRYVFNWNKDK
FPDPKAFFRKFHERGIRLVANIKPGLLTDHPHYDELAEKGAFIKDDDGGEPAVGRFWGGGGSYLDFTNPE
GREWWKEGLKEQLLDYGIDSVWNDNNEYEIWDDDAACCGFGKGGPISELRPIQPLLMARASREAQLEHAP
NKRPFVISRSGCAGIQRYAQTWSGDNRTSWKTLKYNIAMGLGMSLSGVANYGHDIGGFAGPAPEPELFVR
WVQNGIFQPRFSIHSWNTDNTVTEPWMYPEATPAIREAI
>gnl|CDD|269886 cd06600, GH31_MGAM-like, maltase-glucoamylase (MGAM)-like. This family includes the following closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), lysosomal acid alpha-glucosidase (GAA), neutral alpha-glucosidase C (GANC), the alpha subunit of neutral alpha-glucosidase AB (GANAB), and alpha-glucosidase II. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII). GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. Alpha-glucosidase II is a GH31 enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This family also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source. The MGAM-like family corresponds to subgroup 1 in the Ernst et al classification of GH31 enzymes
GRPALPPYWAFGYHQSRYSYYDQDKVVEVVDIMQEAGIPYDVMWLDIDYMDSYKDFTWDPVRFPEPKKFV
DELHKNGQKLVTIVDPGITREWWAGLISEFLYSQGIDGIWIDMNEPSNFYKVHNLYGFYEAMATAEGLRT
SHNERPFILSRSTFAGSQKYAAHWTGDNTASWDDLKLSIPLVLGLSLSGIPFVGADIGGFAGDTSEELLV
RWYQLGAFYPFSRSHKATDTKDQEPVLFPEYYKESVREILELRYKL
>gnl|CDD|269887 cd06601, GH31_lyase_GLase, alpha-1,4-glucan lyase. GLases (alpha-1,4-glucan lyases) are glycosyl hydrolase family 31 (GH31) enzymes that degrade alpha-1,4-glucans and maltooligosaccharides via a nonhydrolytic pathway to yield 1,5-D-anhydrofructose from the nonreducing end. GLases cleave the bond between C1 and O1 of the nonreducing sugar residue of alpha-glucans to generate a monosaccharide product with a double bond between C1 and C2. This family corresponds to subgroup 2 in the Ernst et al classification of GH31 enzymes
GRSRMKPRYVFGYHQGCYGYSSRESLEVVVQSYRDANIPLDGLHIDVDFQDNYRTFTTSKDKFPNPKEMF
SNLHAQGFKCSTNITPIITDPYIGGVNYGGGLGSPGFYPDLGRPEVREWWGQQYKYLFDMGLEMVWQDMT
TPAIAPHKINGYGDMKTFPLRLLVTDDSVKNEHTYKPAATLWNLYAYNLHKATYHGLNRLNARPNRRNFI
IGRGGYAGAQRFAGLWTGDNASTWDFLQINIPQVLNLGLSGVPISGSDIGGFASGSDENEGKWCDPELLI
RWVQAGAFLPWFRNHYDRYIKKKQQEKLYEPYYYYEPVLPICRKYVELRYRLMQVFYDAMYENTQNG
>gnl|CDD|269888 cd06602, GH31_MGAM_SI_GAA, maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase. This subgroup includes the following three closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), and lysosomal acid alpha-glucosidase (GAA), also known as acid-maltase. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end, and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII)
GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPLDVQWNDIDYMDRYRDFTLDPVNFPGLPAFV
DDLHANGQHYVPILDPGISANESGGYPPYDRGLEMDVFIKNDDGSPYVGKVWPGYTVFPDFTNPNTQEWW
TEEIKDFHDQVPFDGLWIDMNEPSNFCTGSCGNSPNAPGCPDNKLNNPPYVPNNLGGGSLSDKTICMDAV
HYDGGLHYDVHNLYGLSEAIATYKALKEIFPGKRPFIISRSTFPGSGKYAGHWLGDNYSTWEDMRYSIPG
MLEFNLFGIPMVGADICGFNGNTTEELCARWMQLGAFYPFSRNHNDIGAIDQEPYVWGPSVADASRKALL
IRYSLLPYLYTLFYRAH
>gnl|CDD|269889 cd06603, GH31_GANC_GANAB_alpha, neutral alpha-glucosidase C, neutral alpha-glucosidase AB. This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae
GTPPLPPLFALGYHQCRWNYNDQEDVLEVDANFDEHDIPYDVIWLDIEHTDGKRYFTWDKKKFPDPKKMQ
EKLASKGRKLVTIVDPHIKRDDDYFVYKEAKEKDYFVKDSDGKDFEGWCWPGSSSWPDFLNPEVRDWWAS
LFSYDKYKGSTENLYIWNDMNEPSVFNGPEITMPKDAIHYGGVEHRDVHNIYGLYMHMATFEGLLKRSNG
KKRPFVLTRSFFAGSQRYGAVWTGDNMATWEHLKISIPMLLSLSIAGIPFVGADVGGFFGNPDEELLVRW
YQAGAFYPFFRAHAHIDTKRREPWLFGEETTEIIREAIRLRYRLLPYWYTLFYEASRTGLPIMRPLWYEF
PEDESTFDIDDQFMLGDSLLVKPVVEEGATSVTVYLPGGEVWYDYFTGQRVTGGGTKTVPVPLDSIPVFQ
RGGSIIPRKERVRRSSKLMRNDPYTLVVALDENGEAEGELYLDDGES
>gnl|CDD|269890 cd06604, GH31_glucosidase_II_MalA, Alpha-glucosidase II-like. Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a glycosyl hydrolase family 31 (GH31) enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This subgroup also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source
GRPPLPPKWALGYQQSRWSYYPEEEVREVAKGFRERDIPCDAIYLDIDYMDGYRVFTWDKERFPDPKELI
KELHEQGFRLVTIVDPGVKVDPGYEVYEEGLENDYFVKDPDGELYVGKVWPGKSVFPDFTNPEVREWWGD
LYKELVDLGVDGIWNDMNEPAVFNAPGGTTMPLDAVHRLDGGKITHEEVHNLYGLLMARATYEGLRRLRP
NKRPFVLSRAGYAGIQRYAAIWTGDNSSSWEHLRLSIPMLLNLGLSGVPFVGADIGGFAGDPSPELLARW
YQLGAFFPFFRNHSAKGTRDQEPWAFGEEVEEIARKAIELRYRLLPYLYTLFYEAHETG
>gnl|CDD|270782 cd06605, PKc_MAPKK, Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYS
EGDISICMEYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKHKIIHRDVKPSNILVNSRGQVK
LCDFGVSGQLVDSLAKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMMIF
ELLSYIVDEPPPLLPSGKFSPDFQDFVSQCLQKDPTERPSYKELMEHPFIKRYEY
>gnl|CDD|270783 cd06606, STKc_MAPKKK, Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERT
ENTLNIFLEYVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKL
ADFGCAKRLAEIATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNPVAA
LFKIGSSGEPPPIPEHLSEEAKDFLRKCLQRDPKKRPTADELLQHPFL
>gnl|CDD|270784 cd06607, STKc_TAO, Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KIFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCY
LREHTAWLVMEYCLGSASDIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTV
KLADFGSASLVCPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALY
HIAQNDSPTLSSGEWSDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVTR
>gnl|CDD|270785 cd06608, STKc_myosinIII_N_like, N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LPDPAGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILRKFSNHPNIATFYG
AFIKKDPPGGDDQLWLVMEYCGGGSVTDLVKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIK
GQNILLTEEAEVKLVDFGVSAQLDSTLGRRNTFIGTPYWMAPEVIACDQQPDASYDARCDVWSLGITAIE
LADGKPPLCDMHPMRALFKIPRNPPPTLKSPEKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI
>gnl|CDD|270786 cd06609, STKc_MST3_like, Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLK
GSKLWIIMEYCGGGSVLDLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLA
DFGVSGQLTSTMSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLI
PKNNPPSLEGNKFSKPFKDFVELCLNKDPKERPSAKELLKHKFIKKAKKTSYLTLLIERIKKWK
>gnl|CDD|270787 cd06610, STKc_OSR1_SPAK, Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVV
GDELWLVMPLLSGGSLLDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGS
VKIADFGVSASLATGGDRTRKVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYSKY
PPMKVLMLTLQNDPPSLETGADYKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF
>gnl|CDD|132942 cd06611, STKc_SLK_like, Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VNPNDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYEA
YFYENKLWILIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDG
DVKLADFGVSAKNKSTLQKRDTFIGTPYWMAPEVVACETFKDNPYDYKADIWSLGITLIELAQMEPPHHE
LNPMRVLLKILKSEPPTLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQSDNKAIKDLLAE
>gnl|CDD|132943 cd06612, STKc_MST1_2, Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKN
TDLWIVMEYCGAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKL
ADFGVSGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFM
IPNKPPPTLSDPEKWSPEFNDFVKKCLVKDPEERPSAIQLLQHPFI
>gnl|CDD|270788 cd06613, STKc_MAP4K3_like, Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRD
KLWIVMEYCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLAD
FGVSAQLTATIAKRKSFIGTPYWMAPEVAAVERKGGYDGKCDIWALGITAIELAELQPPMFDLHPMRALF
LIPKSNFDPPKLKDKEKWSPDFHDFIKKCLTKNPKKRPTATKLLQHPFV
>gnl|CDD|270789 cd06614, STKc_PAK, Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDE
LWVVMEYMDGGSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLAD
FGFAAQLTKEKSKRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLIT
TKGIPPLKNPEKWSPEFKDFLNKCLVKDPEKRPSAEELLQHPFLK
>gnl|CDD|132946 cd06615, PKc_MEK, Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYS
DGEISICMEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKHKIMHRDVKPSNILVNSRGEIK
LCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKELEAMF
GRPVSEGEAKESHRPVSGHPPDSPRPMAIFELLDYIVNEPPPKLPSGAFSDEFQDFVDKCLKKNPKERAD
LKELTKHPFIKRAELEEVDFAGWVCSTM
>gnl|CDD|270790 cd06616, PKc_MKK4, Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YEFTAEDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDCPYIVKF
YGALFREGDCWICMELMDISLDKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKEELKIIHRDVKPSN
ILLDRNGNIKLCDFGISGQLVDSIAKTRDAGCRPYMAPERIDPSASRDGYDVRSDVWSLGITLYEVATGK
FPYPKWNSVFDQLTQVVKGDPPILSNSEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIKMYEERN
VDVAAYVQKIL
>gnl|CDD|173729 cd06617, PKc_MKK3_6, Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQKRLLMDLDISMRSVDCPYTVTFYGALF
REGDVWICMEVMDTSLDKFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHSKLSVIHRDVKPSNVLINRN
GQVKLCDFGISGYLVDSVAKTIDAGCKPYMAPERINPELNQKGYDVKSDVWSLGITMIELATGRFPYDSW
KTPFQQLKQVVEEPSPQLPAEKFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFELHLSKNTDVASFVSL
ILG
>gnl|CDD|270791 cd06618, PKc_MKK7, Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GYLTIDGKKYKADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDVVLKS
HDCPYIVKCYGYFITDSDVFICMELMSTCLDKLLKRIQGPIPEDILGKMTVSIVKALHYLKEKHGVIHRD
VKPSNILLDESGNVKLCDFGISGRLVDSKAKTRSAGCAAYMAPERIDPPDNPKYDIRADVWSLGISLVEL
ATGQFPYRNCKTEFEVLTKILNEEPPSLPPNEGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYET
AEVDVASWFQDVMAE
>gnl|CDD|132950 cd06619, PKc_MKK5, Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QDIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFV
ENRISICTEFMDGGSLDVYRKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFG
VSTQLVNSIAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNQGSLMPLQLLQ
CIVDEDPPVLPVGQFSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQYNDGNAEVVSMWVCRALEERR
>gnl|CDD|270792 cd06620, PKc_Byr1_like, Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DLKNQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYG
AFLNENNNIIICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVHRIIHRDIKPSNILVNS
KGQIKLCDFGVSGELINSIADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDD
DGYNGPMGILDLLQRIVNEPPPRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVRASDV
DLRAWA
>gnl|CDD|270793 cd06621, PKc_Pek1_like, Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLD
EQDSSIGIAMEYCEGGSLDSIYKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTR
KGQVKLCDFGVSGELVNSLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPP
LGPIELLSYIVNMPNPELKDEPENGIKWSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKKKVNMA
KFVKQVW
>gnl|CDD|132953 cd06622, PKc_PBS2_like, Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFI
EGAVYMCMEYMDAGSLDKLYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEHNIIHRDVKPTNVLVNGNG
QVKLCDFGVSGNLVASLAKTNIGCQSYMAPERIKSGGPNQNPTYTVQSDVWSLGLSILEMALGRYPYPPE
TYANIFAQLSAIVDGDPPTLPSGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNADVDMAEWVT
GALKRK
>gnl|CDD|132954 cd06623, PKc_MAPKK_plant_like, Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYK
EGEISIVLEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKRHIIHRDIKPSNLLINSKGEVK
IADFGISKVLENTLDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFE
LMQAICDGPPPSLPAEEFSPEFRDFISACLQKDPKKRPSAAELLQHPFIKKADN
>gnl|CDD|270794 cd06624, STKc_ASK, Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LEYEYEYDESGERVVLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQY
LGSVSEDGFFKIFMEQVPGGSLSALLRSKWGPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVL
VNTYSGVVKISDFGTSKRLAGINPCTETFTGTLQYMAPEVIDKGQRGYGPPADIWSLGCTIIEMATGKPP
FIELGEPQAAMFKVGMFKIHPEIPESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL
>gnl|CDD|270795 cd06625, STKc_MEKK3_like, Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NWKQGKLLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEVKALECEIQLLKNLQHERIVQYYGC
LQDEKSLSIFMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGN
VKLGDFGASKRLQTICSSTGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPM
AAIFKIATQPTNPQLPPHVSEDARDFLSLIFVRNKKQRPSAEELLSHSFV
>gnl|CDD|270796 cd06626, STKc_MEKK4, Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RWQRGNKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVH
REEVYIFMEYCQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKL
GDFGSAVKLKNNTTTMAPGEVNSLVGTPAYMAPEVITGNKGEGHGRAADIWSLGCVVLEMATGKRPWSEL
DNEWAIMYHVGMGHKPPIPDSLQLSPEGKDFLSRCLESDPKKRPTASELLDHPFI
>gnl|CDD|270797 cd06627, STKc_Cdc7_like, Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKT
KDSLYIILEYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKL
ADFGVATKLNEVEKDENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFR
IVQDDHPPLPENISPELRDFLLQCFQKDPTLRPSAKELLKHPWL
>gnl|CDD|270798 cd06628, STKc_Byr2_like, Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KWIKGALIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKDRKKSMLDALQREIALLRELQHENIVQ
YLGSSSDANHLNIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVD
NKGGIKISDFGISKKLEANSLSTKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTH
PFPDCTQMQAIFKIGENASPTIPSNISSEARDFLEKTFEIDHNKRPTADELLKHPFL
>gnl|CDD|270799 cd06629, STKc_Bck1_like, Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FKWVKGELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRADSRQKTVVDALKSEIDTLKDLDHPNI
VQYLGFEETEDYFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNIL
VDLEGICKISDFGISKKSDDIYGNNGATSMQGSVFWMAPEVIHSQGQGYSAKVDIWSLGCVVLEMLAGRR
PWSDDEAIAAMFKLGNKRSAPPVPEDVNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL
>gnl|CDD|270800 cd06630, STKc_MEKK1, Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HWLKGPLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQEEVVEAIREEIRMMARLNHPNIVRMLG
ATQHKSHFNIFVEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTG
QRLRIADFGAAARLASKGTGAGEFQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNA
EKISNHLALIFKIASATTPPPIPEHLSPGLRDVTLRCLELQPEDRPPARELLKHPVFT
>gnl|CDD|270801 cd06631, STKc_YSK4, Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IQWKKGNVLGKGAYGTVYCGLTSTGQLIAVKQVELDTSDKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLG
TCLEDNVVSIFMEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNG
VIKLIDFGCAKRLCINLSSGSQSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWA
DMNPMAAIFAIGSGRKPVPRLPDKFSPEARDFVHACLTRDQDERPSAEQLLKHPFI
>gnl|CDD|270802 cd06632, STKc_MEKK1_plant, Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RWQKGQLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGT
EREEDNLYIFLEYVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGV
VKLADFGMAKHVEAFSFAKSFKGSPYWMAPEVIMQKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVA
AIFKIGNSGELPPIPDHLSPDAKDFIRLCLQRDPEDRPTASQLLEHPFV
>gnl|CDD|270803 cd06633, STKc_TAO3, Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RKGVLKDPEIADLFYKDDPEEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIK
EVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSH
NMIHRDIKAGNILLTEPGQVKLADFGSASIASPANSFVGTPYWMAPEVILAMDEGQYDGKVDIWSLGITC
IELAERKPPLFNMNAMSALYHIAQNDSPTLQSNEWTDSFRGFVDYCLQKIPQERPSSAELLRHDFVRRER
PPRVLIDLIQRTKDAVRELDNLQYRKMKKILFQ
>gnl|CDD|270804 cd06634, STKc_TAO2, Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DPEVAELFFKDDPEKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQ
KLRHPNTIEYRGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRD
VKAGNILLTEPGLVKLGDFGSASIMAPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAER
KPPLFNMNAMSALYHIAQNESPALQSGHWSEYFRNFVDSCLQKIPQDRPTSDVLLKHRFLLRERPPTVIM
DLIQRTKDAVRELDNLQYRKMKKILFQE
>gnl|CDD|270805 cd06635, STKc_TAO1, Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PSTSRAGSLKDPDIAELFFKEDPEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQ
DIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEIEIAAITHGALQGLAY
LHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSL
GITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHMFV
LRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQ
>gnl|CDD|270806 cd06636, STKc_MAP4K4_6_N, N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RSLDDIDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYS
HHRNIATYYGAFIKKSPPGHDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAH
KVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIW
SLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPKLKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHP
FI
>gnl|CDD|270807 cd06637, STKc_TNIK, Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LRDPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYG
AFIKKNPPGMDDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQ
NVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDFKSDLWSLGITAIEMA
EGAPPLCDMHPMRALFLIPRNPAPRLKSKKWSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRDQPNERQ
VRIQLKDHIDRTKKKR
>gnl|CDD|132969 cd06638, STKc_myosinIIIA_N, N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FPLSGKTIIFDSFPDPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKA
LSDHPNVVKFYGMYYKKDVKNGDQLWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAYILHEALMGLQHL
HVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQLDSTYDARC
DVWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVSDL
LQHVFI
>gnl|CDD|270808 cd06639, STKc_myosinIIIB_N, N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LYGLFPYNSSMLGLESLADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYN
ILRSLPNHPNVVKFYGMFYKADQYVGGQLWLVLELCNGGSVTELVKGLLKCGQRLDEAMISYILYGALLG
LQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSARLRRNTSVGTPFWMAPEVIACEQQYDYSY
DARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRNPPPTLLNPEKWCRGFSHFISQCLIKDFEKRPS
VTHLLEHPFIK
>gnl|CDD|132971 cd06640, STKc_MST4, Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DPEELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGS
YLKGTKLWIIMEYLGGGSALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDV
KLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVL
FLIPKNNPPTLVGDFSKPFKEFIDACLNKDPSFRPTAKELLKHKFIVKNAKKTSYLTELIDRFKRWK
>gnl|CDD|270809 cd06641, STKc_MST3, Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGS
YLKDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEV
KLADFGVAGQLTDTQIKRNXFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVL
FLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRYKRWK
>gnl|CDD|270810 cd06642, STKc_STK25, Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DPEELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGS
YLKGTKLWIIMEYLGGGSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDV
KLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVL
FLIPKNSPPTLEGQHSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRYTKKTSFLTELIDRYKRWK
>gnl|CDD|270811 cd06643, STKc_SLK, Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LNPEDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDA
FYYENNLWILIEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDG
DIKLADFGVSAKNTRTLQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGVTLIEMAQIEPPHHE
LNPMRVLLKIAKSEPPTLAQPSRWSPEFKDFLRKCLEKNVDARWTTSQLLQHPFVSVLVSNKPLRELIAE
AKA
>gnl|CDD|132975 cd06644, STKc_STK10, Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YEHVRRDLDPNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPY
IVKLLGAFYWDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGN
VLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQ
IEPPHHELNPMRVLLKIAKSEPPTLSQPSKWSMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSVTSNRP
LRELVAEAKAEV
>gnl|CDD|270812 cd06645, STKc_MAP4K3, Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GLDLSRRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNI
VAYFGSYLRRDKLWICMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANIL
LTDNGHVKLADFGVSAQITATIAKRKSFIGTPYWMAPEVAAVERKGGYNQLCDIWAVGITAIELAELQPP
MFDLHPMRALFLMTKSNFQPPKLKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFVTQ
>gnl|CDD|270813 cd06646, STKc_MAP4K5, Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DILRRNPQHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVA
YFGSYLSREKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLT
DNGDVKLADFGVAAKITATIAKRKSFIGTPYWMAPEVAAVEKNGGYNQLCDIWAVGITAIELAELQPPMF
DLHPMRALFLMSKSNFQPPKLKDKTKWSSTFHNFVKISLTKNPKKRPTAERLLTHLFV
>gnl|CDD|270814 cd06647, STKc_PAK_I, Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SVGDPKKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYL
DSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDG
SVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLR
ALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHPFLK
>gnl|CDD|270815 cd06648, STKc_PAK_II, Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SPGDPRSDLDNFVKIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDYQHPNIVEMY
SSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDG
RVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQ
AMKRIRDNEPPKLKNLHKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFLA
>gnl|CDD|132980 cd06649, PKc_MEK2, Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ELKDDDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYG
AFYSDGEISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNSR
GEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKEL
EAIFGRPVVDGEEGEPHSISPRPRPPGRPVSGHGMDSRPAMAIFELLDYIVNEPPPKLPNGVFTPDFQEF
VNKCLIKNPAERADLKMLMNHTFIKRSEVEEVDFAGWLCKTLRLNQPSTPT
>gnl|CDD|270816 cd06650, PKc_MEK1, Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYG
AFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSR
GEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKEL
ELMFGCQVEGDAAETPPRPRTPGRPLSSYGMDSRPPMAIFELLDYIVNEPPPKLPSGVFSLEFQDFVNKC
LIKNPAERADLKQLMVHAFIKRSDAEEVDFAGWLCSTIG
>gnl|CDD|270817 cd06651, STKc_MEKK3, Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KSPSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEVSALECEIQLLKNLQHER
IVQYYGCLRDRAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGA
NILRDSAGNVKLGDFGASKRLQTICMSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTE
KPPWAEYEAMAAIFKIATQPTNPQLPSHISEHARDFLGCIFVEARHRPSAEELLRHPFAQL
>gnl|CDD|270818 cd06652, STKc_MEKK2, Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PTNWRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESPETSKEVNALECEIQLLKNLLHERIVQYY
GCLRDPQERTLSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRD
SVGNVKLGDFGASKRLQTICLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA
EFEAMAAIFKIATQPTNPQLPAHVSDHCRDFLKRIFVEAKLRPSADELLRHTFV
>gnl|CDD|270819 cd06653, STKc_MEKK3_like_u1, Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PVNWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETSKEVNALECEIQLLKNLRHDRIVQYY
GCLRDPEEKKLSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRD
SAGNVKLGDFGASKRIQTICMSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWA
EYEAMAAIFKIATQPTKPQLPDGVSDACRDFLRQIFVEEKRRPTAEFLLRHPFV
>gnl|CDD|270820 cd06654, STKc_PAK1, Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILV
MRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHR
DIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMI
EGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLS
SLTPLIAAAKEATKNN
>gnl|CDD|132986 cd06655, STKc_PAK2, Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIINEILVM
KELKNPNIVNFLDSFLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRD
IKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE
GEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSS
LTPLILAAKEAMKSNR
>gnl|CDD|132987 cd06656, STKc_PAK3, Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3. Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation
DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVM
RENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRD
IKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE
GEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSS
LTPLIIAAKEAIKNSSR
>gnl|CDD|132988 cd06657, STKc_PAK4, Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SHEQFRAALQMVVDPGDPRTYLDNFIKIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVI
MRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHR
DIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMV
DGEPPYFNEPPLKAMKMIRDNLPPKLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPS
CIVPLMRQNRMR
>gnl|CDD|132989 cd06658, STKc_PAK5, Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RVSHEQFRAALQLVVSPGDPREYLDSFIKIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEV
VIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVI
HRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIE
MIDGEPPYFNEPPLQAMRRIRDNLPPRVKDSHKVSSVLRGFLDLMLVREPSQRATAQELLQHPFLKLAGP
PSCIVPLMRQYR
>gnl|CDD|270821 cd06659, STKc_PAK6, Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VTHEQFKAALRMVVDQGDPRQLLENYVKIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNEVV
IMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIH
RDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEM
VDGEPPYFSDSPVQAMKRLRDSPPPKLKNSHKASPVLRDFLERMLVRDPQERATAQELLDHPFLLQTGLP
ECLVPLIQQYRKRTSTC
>gnl|CDD|381296 cd06660, AKR_SF, Aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others
SRLGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNRDDVVIATKGGH
PPGGDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNW
SAERLAEALAYAKAHGLPGFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARGPAQLALAWLLS
QPFVTVPIVGARSPEQLEENLA
>gnl|CDD|119400 cd06661, GGCT_like, GGCT-like domains, also called AIG2-like family. Gamma-glutamyl cyclotransferase (GGCT) catalyzes the formation of pyroglutamic acid (5-oxoproline) from dipeptides containing gamma-glutamyl, and is a dimeric protein. In Homo sapiens, the protein is encoded by the gene C7orf24, and the enzyme participates in the gamma-glutamyl cycle. Hereditary defects in the gamma-glutamyl cycle have been described for some of the genes involved, but not for C7orf24. The synthesis and metabolism of glutathione (L-gamma-glutamyl-L-cysteinylglycine) ties the gamma-glutamyl cycle to numerous cellular processes; glutathione acts as a ubiquitous reducing agent in reductive mechanisms involved in protein and DNA synthesis, transport processes, enzyme activity, and metabolism. AIG2 (avrRpt2-induced gene) is an Arabidopsis protein that exhibits RPS2- and avrRpt2-dependent induction early after infection with Pseudomonas syringae pv maculicola strain ES4326 carrying avrRpt2. avrRpt2 is an avirulence gene that can convert virulent strains of P. syringae to avirulence on Arabidopsis thaliana, soybean, and bean. The family also includes bacterial tellurite-resistance proteins (trgB); tellurium (Te) compounds are used in industrial processes and had been used as antimicrobial agents in the past. Some members have been described proteins involved in cation transport (chaC)
LFVYGTLMDGEVLHARLGRALFLGPATLKGYRLVFGGGSGYPGLVPGPGARVWGELYEVDPEDLARLDAF
EGVPGGYRREEVEVELEDGEGVEAWVYVA
>gnl|CDD|119401 cd06662, SURF1, SURF1 superfamily. Surf1/Shy1 has been implicated in the posttranslational steps of the biogenesis of the mitochondrially-encoded Cox1 subunit of cytochrome c oxidase (complex IV). Cytochrome c oxidase (complex IV), the terminal electron-transferring complex of the respiratory chain, is an assemblage of nuclear and mitochondrially-encoded subunits. Its assembly is mediated by nuclear encoded assembly factors, one of which is Surf1/Shy1. Mutations in human Surf1 are a major cause of Leigh syndrome, a severe neurodegenerative disorder
LVGLGFWQLQRAEWKEALIARIEARLAAPPVPLPELLAPPLEDLEYRRVTVTGTFLPEKEVLLDNRTRDG
RPGYEVLTPFRLDDGRTVLVNRGWVPADADRPALPAVAPPTGEVTVTGRLRPPEPRGLFLPPNDPAANPW
QNRDLEAMAQALGLPLVPLVLQLASGAPPGLPRPWPPPVMIPNKHLGYAVQWFALAAAALVL
>gnl|CDD|133456 cd06663, Biotinyl_lipoyl_domains, Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue
TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPL
VKI
>gnl|CDD|143480 cd06664, IscU_like, Iron-sulfur cluster scaffold-like proteins. IscU_like and NifU_like proteins. IscU and NifU function as a scaffold for the assembly of [2Fe-2S] clusters before they are transferred to apo target proteins. They are highly conserved and play vital roles in the ISC and NIF systems of Fe-S protein maturation. NIF genes participate in nitrogen fixation in several isolated bacterial species. The NifU domain, however, is also found in bacteria that do not fix nitrogen, so it may have wider significance in the cell. Human IscU interacts with frataxin, the Friedreich ataxia gene product, and incorrectly spliced IscU has been shown to disrupt iron homeostasis in skeletal muscle and cause myopathy
LYSEIILDHYRNPRNVGRLEDADGTGEVGNPLCGDEITLYLKVEDGRITDAKFQGFGCAISIASASLLTE
LIKGKTLDEALKLLNKDIAMLDGKEELAALAGVGLPPARIHCALLAWKALKAA
>gnl|CDD|467154 cd06665, PDZ1_PDZ3_bazooka-like, PDZ domain 1 and PDZ domain 3 of Drosophila bazooka (DmPar3), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 and 3 of Drosophila bazooka (DmPar3), and related domains. The Par complex comprises atypical protein kinase C (aPKC) and two scaffolding proteins, Par3 (Bazooka (Baz) in Drosophila) and Par6; bazooka (DmPar3) has three central PDZ domains. Both PDZ1 and PDZ3 domains, but not PDZ2, in bazooka (DmPar3) engage in a canonical interaction with the PDZ domain-binding motif in Par6. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This bazooka-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
DGEMLLIINEYGSPLGLTALPDKEHGGGLLVQHVEPGSRAERGRLRRDDRILEINGIKLIGLTESQVQEQ
LRRALESSELRVRVLRG
>gnl|CDD|467155 cd06667, PDZ2_MUPP1-like, PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
EVIELVNDGSGLGFGIVGGKSTGVVVKTILPGGVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQC
GSHVRLVVAR
>gnl|CDD|467156 cd06668, PDZ4_MUPP1-like, PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
EIVVAQLSKFSESSGLGISLEGTVDVEVRGHHYIRSILPEGPVGRNGKLFSGDELLEVNGIQLLGLSHKE
VVSILKELPPPVRLVCCR
>gnl|CDD|467157 cd06669, PDZ5_MUPP1-like, PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
LAMWSDEVTVIELEKGDRGLGFSILDYQDPLDPSETVIVIRSLVPGGVAEQDGRLLPGDRLVFVNDVSLE
NASLDEAVQALKSAPPGTVRIGVAKPLP
>gnl|CDD|467158 cd06670, PDZ6_MUPP1-like, PDZ domain 6 of multi-PDZ-domain protein 1 (MUPP1) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 6 of multi-PDZ-domain protein 1 (MUPP1). MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ6 domain is therefore absent from PATJ. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ6 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
SSLERTITIVKGNSSLGITVSADKDGNGCIVKSIIHGGAVSRDGRISVGDFIVSINNESLRNVTNAQARA
ILRRASLVGTDISITYI
>gnl|CDD|467159 cd06671, PDZ7_MUPP1-PD6_PATJ-like, PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated tight junction) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of MUPP1 and PDZ domain 6 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
PPRRVELWREPGKSLGISIVGGRVMGSRLSNGEEIRGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLR
NATHEEAVEAIRNAGNPVVFLVQSLI
>gnl|CDD|467160 cd06672, PDZ8_MUPP1-PDZ7_PATJ-PDZ2_INAD-like, PDZ domain 8 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 7 of protein-associated tight junction (PATJ), PDZ domain 2 of Drosophila melanogaster inactivation-no-after-potential D (INAD), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 8 of MUPP1, PDZ domain 7 of PATJ, and PDZ domain 2 of Drosophila melanogaster INAD, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. It contains 5 PDZ domains arranged in tandem (PDZ1-PDZ5) which independently bind various proteins. INAD PDZ2 binds eye-specific protein kinase C. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ8 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
LHLIELEKGSSGLGLSLAGNKDRSRMSVFVVGIDPDGAAGKDGRIQVGDELLEINGQVLYGRSHLNASAI
IKSAPSKVKIVFLR
>gnl|CDD|467161 cd06673, PDZ10_MUPP1-PDZ8_PATJ-like, PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated tight junction) and similar domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 10 of MUPP1, PDZ domain 8 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ10 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
GRETTIEINKGKKGLGLSIVGGSDTLLGAIIIHEVYEDGAAAKDGRLWAGDQILEVNGEDLRKATHDEAI
NVLRQTPQKVRLLVYR
>gnl|CDD|467162 cd06674, PDZ11_MUPP1-PDZ9_PATJ-like, PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ (protein-associated tight junction) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 11 of MUPP1, PDZ domain 9 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ11 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
YDIFTVELQKKPGRGLGLSIVGKRNDTGVFVSDIVKGGAADADGRLMQGDQILSVNGEDVRNASQEAAAA
LLKCAQGKVRLEVGRLK
>gnl|CDD|467163 cd06675, PDZ12_MUPP1-like, PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight junction (PATJ, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 12 of MUPP1, PDZ domain 10 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like PDZ12 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RTVEIKRGPQDSLGISIAGGVGSPLGDVPVFIAMIQPNGVAAQTGKLKVGDRIVSINGQSTDGLTHSEAV
NLLKNASGTIILQVVA
>gnl|CDD|467164 cd06676, PDZ13_MUPP1-like, PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 13 of MUPP1. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ13 domain is therefore absent from PATJ. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ13 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
TITLERGSDGLGFSIVGGFGSPHGDLPIYVKTVFEKGAAAEDGRLKRGDQILAVNGESLEGVTHEEAVNI
LKKTKGTVTLTVL
>gnl|CDD|467165 cd06677, PDZ1_LNX1_2-like, PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
GEITTIEIHRSDPYEELGISIVGGNDTPLINIVIQEVYRDGVIARDGRLLPGDQILEVNGVDISNVTHSQ
ARSVLRQPCPVLRLTVLRE
>gnl|CDD|467166 cd06678, PDZ2_LNX1_2-like, PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
LHVTLNKRDGEQLGIKLVRKKDEPGVFILDLLEGGLAARDGRLKSDDRVLAINGQDLRHGTPEQAAQIIQ
ASGERVHFVVSR
>gnl|CDD|467167 cd06679, PDZ3_LNX1_2-like, PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
KTVTIKKEPSESLGISVAGGRGSRRGDLPIYVTNVQPDGCLGRDGRIKKGDVLLSINGISLTNLSHSEAV
AVLKASAASSSIVLKVLE
>gnl|CDD|467168 cd06680, PDZ4_LNX1_2-like, PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2)and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
KDITLRRSSSGSLGFSIVGGYEESHGNQPFFVKSIVPGTPAYNDGRLKCGDIILAVNGVSTVGMSHAALV
PLLKEQRGRVTLTVVSWPG
>gnl|CDD|467169 cd06681, PDZ2_GRIP1-2-like, PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
KTVEVTLEKEGNSFGFVIRGGAHEDRNKSRPLTVTHVRPGGPADREGTIKPGDRLLSVDGISLHGATHAE
AMSILKQCGQEATLLIEYD
>gnl|CDD|467170 cd06682, PDZ5_GRIP1-2-like, PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family domain PDZ5 is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
FHVKLPKRSGVGLGITISAPKNRKPGDPLIISDVKKGSVAHRTGTLEPGDKLLAIDNIRLDNCSMEDAAQ
ILQQAEDIVKLKIRK
>gnl|CDD|467171 cd06683, PDZ6_GRIP1-2-like, PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ6 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
AIIYTVELKRYGGPLGITISGTEEPFDPIVISGLTEGGLAERTGAIHVGDRILAINGESLRGKPLSEAIH
LLQNAGDTVTLKISR
>gnl|CDD|467172 cd06684, PDZ3_GRIP1-2-like, PDZ domain 3 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
GPLLVEIEKTPGSSLGITLSTSTHRNKQVIVIDSIKPASIADRCGALHVGDHILSIDGTSVEHCSLAEAT
QLLASNSGDQVKLEILP
>gnl|CDD|467173 cd06685, PDZ7_GRIP1-2-like, PDZ domain 7 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
LELHKVTLYKDSDTEDFGFSVSDGLYEKGVYVNAIRPGGPADLSGLQPYDRILQVNHVRTRDFDCCLVVP
LIAESGDKLELVVSR
>gnl|CDD|467174 cd06686, PDZ4_GRIP1-2-like, PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
QVVHTETTEVILRGDPLKGFGIQLQGGVFATETLSSPPLISFIEPDSPAERCGVLQVGDRVLSINGIPTE
DRTLEEANQLLRDSASKVTLEIEFDVAES
>gnl|CDD|467175 cd06687, PDZ1_GRIP1-2-like, PDZ domain 1 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
TVVELIKKEGSTLGLTVSGGIDKDGKPRVSNLRPGGIAARSDQLNVGDYIKSVNGIRTTKLRHDEIISLL
KNVGERVVLEVEY
>gnl|CDD|467176 cd06689, PDZ1_MUPP1-like, PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
EFEQAIQSMAQGRQVEYIELEKPESGGLGFSVVGLKSENRGELGIFVQEIQPGSVAARDGRLKENDQILA
INGQPLDQSISHQQAIAILQQAKGSVELVVAR
>gnl|CDD|467177 cd06690, PDZ_Radil-like, PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Radil (also known as protein KIAA1849) and related domains. Radil is required for cell adhesion and migration of neural crest precursors during development. Radil is a component of a Rasip1-Radil-ARHGAP29 complex at endothelial cell-cell junctions. Rap1, via its effectors Radil and Rasip1 and their binding partner ArhGAP29, controls the endothelial barrier by decreasing Rho-mediated radial tension on cell-cell junctions. ArhGAP29 binds the Radil PDZ domain. The Radil PDZ domain also binds kinesin family protein 14 (KIF14); KIF14 negatively regulates Rap1-mediated inside-out integrin activation by tethering Radil on microtubules. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Radil-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
EDVFVVELERGPKGLGLGLIDGLHTPLRSPGIYIRTLVPDSPAARDGRLRLGDRILAVNGTSLVGADYQS
AMDLIRTSGDKLRFLVAK
>gnl|CDD|467178 cd06691, PDZ1_Par3-like, PDZ domain 1 of partitioning defective 3 (Par3), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP) and related domains; Drosophila bazooka PDZ1 belongs to a different PDZ family. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par3 and the Par complex include: Par-3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par3 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
LDDMTKTVELSNDGGPLGIHVVPFSSSLSGRTLGLLIRGIEEGSRAERDGRFQENDCIVEINGVDLIDKS
FEQAQDIFRQAMRSPEVKLHVVPAANRE
>gnl|CDD|467179 cd06692, PDZ1_GgSTXBP4-like, PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, and related domains. Gallus gallus STXBP4 isoform X1 contains 2 PDZ domains (PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This STXBP4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
IEFSDCSKGLGIKIIGGYRENTGEEFGIFIKRILPGGLAATDGRLKEGDLILEVNGESLQGVTNERAVSI
LRSASASNHMSLLIARDE
>gnl|CDD|467180 cd06694, PDZ1_PTPN13_FRMPD2-like, PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
EIVIVTLKKDPQKGLGFTIVGGENSGSLDLGIFVKSIIPGGPADKDGRIKPGDRIIAINGQSLEGKTHHA
AVEIIQNAPDKVELIISQPKSV
>gnl|CDD|467181 cd06695, PDZ3_PTPN13_FRMPD2-like, PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
TFEVKLTKGSSGLGFSFLGGENNSPEDPFSGLVRIKKLFPGQPAAESGLIQEGDVILAVNGEPLKGLSYQ
EVLSLLRGAPPEVTLLLCRP
>gnl|CDD|467182 cd06696, PDZ4_PTPN13-like, PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)] and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
EVELEVTLTKSEKGSLGFTVTKGKDDNGCYIHDIVQDPAKSDGRLRPGDRLIMVNGVDVTNMSHTEAVSL
LRAAPKEVTLVLGRA
>gnl|CDD|467183 cd06697, PDZ5_PTPN13-like, PDZ domain 5 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), Protein-tyrosine phosphatase 1E (PTP-E1), and Protein-tyrosine phosphatase (PTPL1)] and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
HLLPDITLTCHPGQLGLKLTGGSDSKYQVIYVLEIVPGSAAAEEGSLQPLDIIHYINGVSTQGMTLEDAV
RALEASLPTVVLKATRD
>gnl|CDD|467184 cd06698, PDZ1_hSTXBP4-PDZ2_GgSTXBP4-like, PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus uncharacterized STXBP4 isoform X1, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus uncharacterized STXBP4 isoform X1, and related domains. Human STXBP4 (also known as Synip) includes a single PDZ domain, a coiled-coil domain, and a WW domain (named for its two conserved tryptophans); Gallus gallus STXBP4 isoform X1 contains 2 PDZ domains (PDZ1 and PDZ2). Human STXBP4 plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane: insulin induces the dissociation of the STXBP4 and STX4 complex liberating STX4 to interact with Vamp2, and to form the SNARE complex thereby promoting vesicle fusion. It may also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose. Human STXBP4 is also known to physically associate with a prominent isoform of TP63 (deltaNp63alpha 9) whose overexpression promotes squamous cell carcinoma development, and in doing so prevents degradation of this isoform by the Cdc20-APC/C complex, Itch, and RACK1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This STXBP4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
GIQLITVAKSTGLGLSIVGGINRPEGPMVFIQEVIPGGDCYKDGRLRPGDQLVSINKESLIGVTLEEAKS
ILTRAKLRSESNVEIAFIR
>gnl|CDD|467185 cd06701, PDZ4_Scribble-like, PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
PPGLQELTIVKEPGEKLGISIRGGAKGHAGNPLDPTDEGIFISKINPDGAAARDGRLKVGQRILEVNGQS
LLGATHQEAVRILRSVGDTLTLLVCDGY
>gnl|CDD|467186 cd06702, PDZ3_Scribble-like, PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
EEIHLVKAGGPLGLSIVGGSDHSSHPFGVDEPGIFISKVIPDGAAAKSGLRIGDRILSVNGKDLRHATHQ
EAVSALLSPGQEIKLLVRH
>gnl|CDD|467187 cd06703, PDZ2_Scribble-like, PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
ETITTTLIRDGKGLGFSIAGGKGSTPFRDGDEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARH
DQAVALLTSSSPTITLVVEREA
>gnl|CDD|467188 cd06704, PDZ1_Scribble-like, PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
LTITIERQTGGLGISIAGGKGSTPYKGDDEGIFISRVTEGGPAAKAGVRVGDKLLEVNGVDLVDADHHEA
VEALKNSGNTVTMVVLR
>gnl|CDD|467189 cd06705, PDZ_MAST, PDZ domain of the microtubule-associated serine-threonine (MAST) protein kinase family. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST family kinases, including MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain; MAST family member MASTL is a shorter protein lacking the PDZ domain. The PDZ domain gives the MAST family the capacity to scaffold its own kinase activity. These kinases are implicated in the inhibition of neurite outgrowth and regeneration in cultured cells. Their binding partners include microtubules, beta2-syntrophin, TNF receptor-associated factor 6 (TRAF6), cAMP-regulated phosphoprotein (ARPP-16), and PTEN. This family also includes Caenorhabditis elegans KIN-4 MAST kinase, a key longevity factor acting through binding PTEN phosphatase, and Drosophila Drop out which regulates dynein-dependent transport during embryonic development. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
LKPPIVIKKGPRGFGFTLRAIRVYIGDSDVYTVHHLVTAVEEGSPAYEAGLRPGDLITHVNGEPVQGLLH
TQVVQLILKGGNKVSIRATPLEK
>gnl|CDD|467190 cd06706, PDZ_PTPN3-4-like, PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein phosphatase non-receptor type 4 (PTNP4), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PTPN3, PTPN4 and related domains. PTPN3 (also known as protein-tyrosine phosphatase H1, PTP-H1) has a tumor-suppressive or a tumor-promoting role in many cancers. It serves as a specific phosphatase for the MAP kinase p38gamma; the two interact via their PDZ domains and cooperate to promote Ras-induced oncogenesis. Interaction partners of the PTPN3 PDZ domain include p38gamma and human papillomavirus E6 oncoprotein. PTPN4 (also known as protein-tyrosine phosphatase MEG1) plays a role in immunity, learning, synaptic plasticity or cell homeostasis. p38gamma is also an interaction partner of the PTPN4 PDZ domain: PTPN4 regulates neuronal cell homeostasis by protecting neurons against apoptosis; binding of the C terminus of p38gamma to the PDZ domain of PTPN4, antagonizes the catalytic autoinhibition of PTPN4, leading to cell apoptosis. Other interaction partners of the PTPN4 PDZ domain include glutamate receptor subunit GluN2A, and RABV strain G protein, among others. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQV
VMFIKASRERHSGELVLLVR
>gnl|CDD|467191 cd06707, PDZ_GIPC, PDZ domain of GIPC family proteins. GIPC1/GIPC (GAIP/RGS19-interacting protein), GIPC2, and GIPC3 (also known as C19orf64) constitute the GIPC family. These proteins contain an N-terminal GIPC-homology 1 (GH1) domain, a central PDZ domain, and a C-terminal GH2 domain. GIPC proteins function as adaptor molecules that assemble RTKs, GPCRs, integrins, transmembrane proteins and cytoplasmic signaling regulators as cargoes of MYO6-dependent endocytic transport. Mutations in the Gipc1 and Gipc2 genes have been linked to cancer, while mutations in the Gipc3 gene cause nonsyndromic hearing loss. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GIPC family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
KGQPKEIEVTKSEDALGLTITDNGAGYAFIKRIKEGSIMDKVPAICVGDHIEKINGESLVGCRHYEVARM
LKEIPIGETFTLRLVEPKK
>gnl|CDD|467192 cd06708, PDZ_nNOS-like, PDZ domain of neuronal nitric oxide synthase (nNOS), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of nNOS, and related domains. nNOS produces a key signaling molecule, nitric oxide (NO), which has diverse functions throughout the body and acts as a neurotransmitter and intracellular signaling molecule in the central and peripheral nervous system. nNOS is concentrated at synaptic junctions in the brain and motor endplates in skeletal muscle. The PDZ domain of neuronal nitric oxide synthase (nNOS) interacts with the PDZ domain of alpha1-syntrophin (in muscle cells) and with the second PDZ domain of Disks large homolog 4 (Dlg4, also known as PSD-95), and nitric oxide synthase 1 adaptor protein NOS1AP in neurons. Dlg4 binds NMDA receptors, and nNOS, forming a complex in neurons. NOS1AP competes with Dgl4 for the nNOS PDZ domain and prevents the coupling of nNos activation with NMDA receptor-mediated calcium influx. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This nNOS-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
NVISVRLFKRKVGGLGFLVKQRVCKPPVIISDLIRGGAAEQSGLVQVGDIILAVNGRPLVDVSYESALEV
LRSIPSETPVVLILRGPEGFTTHLETTFTGDGTPKTVRVT
>gnl|CDD|467193 cd06709, PDZ_SYNJ2BP-like, PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNJ2BP, and related domains. SYNJ2BP (also known as mitochondrial outer membrane protein 25, OMP25) regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Binding partners of the SYNJ2BP PDZ domain include activin type II receptors (ActR-II), and SYNJ2. SYNJ2BP interacts with the PDZ binding motif of the Notch Delta-like ligand 1 (DLL1) and DLL4, promoting Delta-Notch signaling, and inhibiting sprouting angiogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNJ2BP-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
EEITLKRGPSGLGFNIVGGTDQPYIPNDSGIYVAKIKEDGAAAIDGRLQEGDKILEINGQSLENLTHQDA
VELFRNAGEDVKLKVQ
>gnl|CDD|467194 cd06710, PDZ_RGS12-like, PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RTVEIARGRAGYGFTISGQAPCVLSCVVRGSPADVAGLKAGDQILAVNGINVSKASHEDVVKLIGKCTGV
LRLVIA
>gnl|CDD|467195 cd06711, PDZ_RGS3-like, PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS3, and related domains. RGS3 down-regulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. It downregulates G-protein-mediated release of inositol phosphates and activation of MAP kinases. In Eph/ephrin signaling, RGS3 binds via its PDZ domain to the cytoplasmic C terminus of Eph receptor tyrosine kinase EphB. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
LQITIQRGKDGFGFTICDDSPVRVQAVDPGGPAEQAGLQQGDTVLQINGQPVERSKCVELAHAIRNCPSE
IILLVWR
>gnl|CDD|467196 cd06712, PDZ_rhophilin-like, PDZ domain of rhophilin-1, rhophilin-2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This rhophilin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
PRTVHLTKEEGGFGFTLRGDSPVQVASVDPGSCAAEAGLKEGDYIVSVGGVDCKWSKHSEVVKLLKSAGE
EGLELQVV
>gnl|CDD|467197 cd06713, PDZ_tamalin_CYTIP-like, PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This tamalin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
SQRRTIILEKQDNETFGFEIQTYGLHHKNSNEVEMCTYVCRVHEDSPAYLAGLTAGDVILSVNGVSVEGA
SHQEIVELIRSSGNTLRLETL
>gnl|CDD|467198 cd06714, PDZ_RIM-like, PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RIM, RIM2, piccolo and related domains. RIM proteins and Gallus gallus protein piccolo (also called aczonin) are involved in neurotransmitter release at presynaptic active zones, the site of vesicle fusion. A protein complex containing RIM proteins positions synaptic vesicles containing synaptotagmin at the active zone. RIM proteins simultaneously activate docking and priming of synaptic vesicles and recruit Ca2+-channels to active zones, thereby connecting primed synaptic vesicles to Ca2+-channels. RIM binding to vesicular Rab proteins (Rab3 and Rab27 isoforms) mediates vesicle docking; RIM binding to Munc13 activates vesicle priming; RIM binding to the Ca2+-channel, both directly and indirectly via RIM-BP, recruits the Ca2+-channels. The RIM PDZ domain interacts with the C-termini of N- and P/Q-type voltage-gated Ca2+-channels. RIM1, RIM2 and piccolo also participate in regulated exocytosis through binding cAMP-GEFII (cAMP-binding protein-guanidine nucleotide exchange factor II). The piccolo PDZ domain binds cAMP-GEFII. RIM2 also plays a role in dendrite formation by melanocytes. Caenorhabditis elegans RIM (also known as unc-10) may be involved in the regulation of defecation and daumone response. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
DFLIGRIILQRDPKDGSVSGNGLGLKVVGGKMTESGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGIS
LQGKTFEEVQDIISQSKGEVELVVS
>gnl|CDD|467199 cd06715, PDZ1-PDZRN4-like, PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PDZRN4, PDZRN3-B, and related domains. PDZRN4 (also known as ligand of numb protein X 4, and SEMACAP3-like protein) contains an N-terminal RING domain and two tandem repeat PDZ domains. It is involved in the progression of cancer, including human liver cancer and breast cancer, and may contribute to the tumorigenesis of rectal adenocarcinoma. Danio rerio PDZRN3-B may participate in neurogenesis: the first PDZ domain of Danio rerio Pdzrn3 interacts with Kidins220 (Kinase D-interacting substrate 220 kD, also named Ankyrin Repeat-Rich Membrane Spanning), a crucial mediator of signal transduction in neural tissues. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZRN4-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
KPFTVVLHRENGSLGFNIIGGRPCENNQEGSSSEGIYVSKIVENGPAADEGGLQVHDRIIEVNGKDLSKA
THEEAVEAFRTAKEPIVVQVLR
>gnl|CDD|467200 cd06716, PDZ2-PDZRN4-like, PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PDZRN4, PDZRN3-B, and related domains. PDZRN4 (also known as ligand of numb protein X 4, and SEMACAP3-like protein) contains an N-terminal RING domain and two tandem repeat PDZ domains. It is involved in the progression of cancer, including human liver cancer and breast cancer, and may contribute to the tumorigenesis of rectal adenocarcinoma. Danio rerio PDZRN3-B may participate in neurogenesis: the first PDZ domain of Danio rerio Pdzrn3 interacts with Kidins220 (Kinase D-interacting substrate 220 kD, also named Ankyrin Repeat-Rich Membrane Spanning), a crucial mediator of signal transduction in neural tissues. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZRN4-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
IEYEEVTLKRSNSQEKLGLTLCYRTDDEEDTGIYVSEVDPNSIAAKDGRIREGDQILQINGVDVQNREEA
IALLSEEEKSITLLVARP
>gnl|CDD|467201 cd06717, PDZ_Dishevelled-like, PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of DVL1-3, and related domains. The dishevelleds (DVL1, 2 and 3 in humans) act downstream of Frizzled (FZD) receptors in both the canonical and non-canonical WNT signaling pathway; they bind the cytoplasmic C-terminus of frizzled family members and transduce the Wnt signal to down-stream effectors. They bind to several proteins known to modulate Wnt signaling. Binding partners of the DVL1 PDZ domain include nucleoredoxin (NXN), Van Gogh-like (VANGL1), Wnt receptor RYK, Dapper 1 (DACT1), Frizzled7 (FZD7), transmembrane protein 88 (TMEM88), Daple (dishevelled-associating protein with a high frequency of leucines), also known as Ccdc88c), and cysteine-rich protein Idax. The DVL2 PDZ domain has been shown to bind the nuclear export signal sequence of the DVL2 protein. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This DVL-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
TVTLNMEKVNFLGISIVGQSNERGDGGIYVGSIMKGGAVAADGRIEPGDMILQVNDISFENMSNDDAVRV
LREAVHKPGPITLTVAK
>gnl|CDD|467202 cd06718, PDZ_Par6-like, PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F (RhoGAP100F), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Par6 (also known as PAR6 or Par-6), RhoGAP100F, and related domains. Par6 is part of a conserved machinery that directs metazoan cell polarity, a process necessary for the function of diverse cell types. Par6 forms a cell polarity-regulatory complex with atypical protein kinase C (aPKC) and Par3. Par6 can also directly associate with PALS1 (proteins associated with Lin7, also known as Stardust) providing a link between the Par3/aPKC/Par6 complex and the PALS1-PATJ (protein-associated TJ) complex. Binding partners of the Par6-PDZ domain include Par3, PALS1/Stardust; leucine-rich repeat-containing protein netrin-G ligand-2 (NGL-2), human crumbs (CRB3) involve in the morphogenesis of the tight junctions in mammalian epithelial cells, and PAR-6 co-operates with the Par6 semi-CRIB domain to bind CDC42. CDC42 regulates the Par6 PDZ domain through an allosteric CRIB-PDZ transition. Drosophila RhoGAP100F, also known as synapse defective protein 1 homolog (syd-1 homolog), is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound form. The RhoGAP100F-PDZ domain binds the neurexin C terminus to control synapse formation at the Drosophila neuromuscular junction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par6-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RRVELIKPPGKPLGFYIRDGNGVERVPGIFISRLVLGSLADSTGLLAVGDEILEVNGVEVTGKSLDDVTD
MMVAPTRLIITVKP
>gnl|CDD|467617 cd06719, PDZ2-4_Nma111p-like, second and fourth PDZ domains (PDZ2 and 4) of Saccharomyces cerevisiae pro-apoptotic serine protease Nma111p and related domains. Second and fourth PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens 1)) domains of the HtrA-type protease Saccharomyces cerevisiae Nma11p (also known as Ynm3p), and related domains. Nma111p is a nuclear serine protease which mediates apoptosis through proteolysis of the apoptotic inhibitor Bir1p. Nma111p is composed of two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminus of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands (A-F) and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. One permutation places beta-strand A at the C-terminus, another permutation places both beta-strands A and B at the C-terminus. This Nma111p-like family PDZ2 and PDZ4 domains show similarity to permuted PDZ domains
RFVEVAGATFHDLSYQQARSYAIPVRGVYVSEASGSFKLAGGISKGWIITSVNNQPTPNLDTFIEVMKTI
PDNSRVRVR
>gnl|CDD|467203 cd06720, PDZ1_APBA1_3-like, PDZ domain 1 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, APBA3, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of APBA1, APBA2, APBA3, and related domains. The APBA/X11/Mint protein family includes three members: neuron specific APBA1 (also known as X11alpha and Mint1) and APBA2 (also known as X11beta and Mint2), and the ubiquitously expressed APBA3 (also known as (X12gamma and Mint3). They are involved in regulating neuronal signaling, trafficking and plasticity. They contain two PDZ domains (PDZ1 and PDZ2) which bind a variety of proteins: Arf GTPases (APBA1 and APBA2 PDZ2) and neurexin (APBA1 and APBA2 PDZ1 and 2), which are involved in vesicle docking and exocytosis; alpha1B subunit of N-type Ca2+ channel (APBA1 PDZ1) that is involved in ion channels; KIF17 (APBA1 PDZ1) that is involved in transport and traffic; and Alzheimer's disease related proteins such as APP (APBA3 PDZ2), CCS (APBA1 PDZ2), NF-kappa-B/p65 (APBA2 PDZ2), presenilin-1 (APBA1 and APBA2 PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This APBA1,2,3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F
KEVVVEKQKGEILGVVIVESGWGSLLPTVVVANMMPGGPAARSGKLNIGDQIMSINGTSLVGLPLSTCQA
IIKNLKNQTKVKLTVV
>gnl|CDD|467204 cd06721, PDZ1_syntenin-like, PDZ domain 1 of syntenin-1, syntenin-2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of syntenin-1, syntenin-2, and related domains. Syntenins are implicated in various cellular processes such as trafficking, signaling, and cancer metastasis. They bind to signaling and adhesion molecules, such as syndecans, neurexins, ephrin B, and phospholipid PIP2. Through its tandem PDZ domains (PDZ1 and PDZ2), syntenin links syndecans to other cell surface receptors and kinases, such as E-cadherin and ephrin-B, establishing signaling crosstalk. During syndecan binding, syntenin PDZ2 serves as a high-affinity domain, and PDZ1, also necessary for binding, acts as a complementary, low-affinity domain; this is also the case for syntenin binding to proto-oncogene c-Src. The syntenin PDZ domain-PIP2 interaction controls Arf6-mediated syndecan recycling through endosomal compartments; both PDZ1 and PDZ2 interact with PIP2. Different binding partners and downstream regulators of syntenin1 PDZ domains, such as to proto-oncogene c-Src, mitogen-activated protein kinase (MAPK), and focal adhesion kinase (FAK), have been identified that promote the progression and invasion of a variety of cancers, such as melanoma, glioblastoma multiforme and breast cancer. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This syntenin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F
REVILCKDQDGKIGLRVKSIDKGVFVQLVQANSPAALAGLRFGDQILQINGENVAGWSSDKAHKVLKKAS
PERITLAVR
>gnl|CDD|467205 cd06722, PDZ_PICK1-like, PDZ domain of PICK1 (protein interacting with C-kinase 1) and similar domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PICK1, and related domains. PICK1 (also known as PRKCA-binding protein and protein kinase C-alpha-binding protein) plays a key role in regulating trafficking of binding partners by altering either their subcellular targeting and/or surface expression. PICK1 plays a role in synaptic plasticity by regulating the trafficking and internalization of amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptors; the PICK1-PDZ domain binds the AMPA receptor subunits. The PICK1 PDZ domain also binds glutamate transporters, Eph receptors, metabotropic glutamate receptors, and ASICs (acid-sensing ion channels), among others. Clustering and synaptic targeting of PICK1 requires direct interaction between the PDZ domain and lipid membranes. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PICK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F
GTVTLKKDAQNLIGISIGGGAPYCPCLYIVQVFDNTPAAKDGTLAAGDEIVGVNGKSVKGKTKVEVAKMI
QAVKGEVTIHYNKL
>gnl|CDD|467206 cd06723, PDZ1_Dlg1-2-4-like, PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
YEEITLERGNSGLGFSIAGGTDNPHIGDDPSIYITKIIPGGAAAADGRLRVNDIILRVNDVDVRNVTHSV
AVEALKEAGSIVRLYVKRR
>gnl|CDD|467207 cd06724, PDZ2_Dlg1-2-4-like, PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
EIKLVKGPKGLGFSIAGGVGNQHIPGDNGIYVTKIIEGGAAQKDGRLQVGDKLLAVNDVSLEEVTHEEAV
AALKNTSDVVYLKVA
>gnl|CDD|467208 cd06726, PDZ_MPP-like, PDZ domain of membrane palmitoylated proteins (MPPs), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1-7 (also known as MAGUK p55 subfamily members 1-7), and related domains. MPPs comprise a subfamily of a larger group of multidomain proteins, namely, membrane-associated guanylate kinases (MAGUKs). MPPs form diverse protein complexes at the cell membranes, which are involved in a wide range of cellular processes, including establishing proper cell structure, polarity and cell adhesion. MPPs have only one PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RLVEFEKARDEPLGATIKMEEDSVIVARILHGGMAHRSGLLHVGDEILEINGIPVSGKTVDELQKLLSSL
SGSVTFKLIP
>gnl|CDD|467209 cd06727, PDZ1_ZO1-like, PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins, and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ZO family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
HTVTLHRAPGFGFGIAVSGGRDNPHFQSGDTSIVISDVLKGGPAEGKLQENDRVVSVNGVSMENVEHSFA
VQILRKCGKTANITVKR
>gnl|CDD|467210 cd06728, PDZ2_ZO1-like_ds, PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and ZO-3, and related domains; form domain-swapping dimers. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins, and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ZO family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
LKVTLTKSRKNDEYGLRLGSRIFVKEITPDSLAAKDGNLQEGDIILKINGTPVENLSLSEAKKLIEKSKD
KLQLVVLRD
>gnl|CDD|467211 cd06729, PDZ3_ZO1-like_domain, PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins, and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ZO family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
DTRLVSFRKGGSVGLRLAGGNDVGIFVAGVQEGSPAEKQGLQEGDQILKVNGVDFRNLTREEAVLFLLDL
PKGEEVTILAQS
>gnl|CDD|467212 cd06730, PDZ0_MAGI-1_3-like, PDZ domain 0 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 0 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ0 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
KVHECVVSRGPDGELNLEIRGGAENGQFPYLGEVKEDKVVYKSGKLHPGELLLEVNGTPVSGLTLRDVLA
VIKHCKEPVRLKTVK
>gnl|CDD|467213 cd06731, PDZ1_MAGI-1_3-like, PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
LIRTSLKKSARGFGFTIIGGDEPDEFLQIKSVVPDGPAALDGKLRTGDVLVSVNDTCVLGYTHADVVKLF
QSIPIGQSVNLEVCR
>gnl|CDD|467214 cd06732, PDZ2_MAGI-1_3-like, PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
PELVTVPIVKGPMGFGFTIADSPQGQRVKQILDPQRCRGLQEGDLIVEINGQNVQNLSHAQVVDVLKECP
KGSEVTLLVQRG
>gnl|CDD|467215 cd06733, PDZ3_MAGI-1_3-like, PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
ELTVFLRRQETGFGFRILGGTEEGSQVSIGAIVPGGAADLDGRLRTGDELLSVDGVNVVGASHHKVVDLM
GNAARNGQVNLTVRR
>gnl|CDD|467216 cd06734, PDZ4_MAGI-1_3-like, PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
PYDVTLTRRENEGFGFVIISSVNKKSGSKIGRIIPGSPADRCGQLKVGDRILAVNGISILNLSHGDIVNL
IKDSGLSVTLTIVP
>gnl|CDD|467217 cd06735, PDZ5_MAGI-1_3-like, PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5, and belongs to this MAGI1,2,3-like family. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
YYSVELERGPKGFGFSIRGGREYNNMPLYVLRLAEDGPAQRDGRLRVGDQILEINGESTQGMTHAQAIEL
IRSGGSVVRLLLRR
>gnl|CDD|467218 cd06736, PDZ_CARD11_CARD14-like, PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CARD11, CARD14, and related domains. CARD11 (also known as CARD-containing MAGUK protein 1, CARMA1, Bimp3) and CARD14 (also known as CARD-containing MAGUK protein 2, CARMA2, Bimp2) belong to the CARD-containing membrane-associated guanylate kinase (MAGUK) protein family. They play several crucial biological functions, including regulation of immune response and inflammation. The CARD11-Bcl10-MALT1 (CBM) complex bridges T cell receptor signaling to the canonical IkappaB kinase (IKK)/NF-kappaB pathway. CARD14 can form an analogous biochemical complex to activate NF-kappaB during specialized immunity. The CBM complex of CARD14/CARMA2 may bind with TRAF6 and get involved in IL-17 pathways in keratinocytes. The preponderance of protein interactions occurs through the N-terminal half of CARD11 that includes the CARD, LATCH, and coiled-coil domains; the C-terminal PDZ-SH3-MAGUK region binds the adhesion and degranulation-promoting adapter protein (ADAP) and aryl hydrocarbon receptor interacting protein (AIP). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This CARD11 and CARD14-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
TITFQGDSLLSQITIIGGNRTGIFIHSVQPGSAAEKAGLREGTQLLLLEGCIRGERQSVSLEDCTKEEAH
WTLQR
>gnl|CDD|467219 cd06737, PDZ1_harmonin, PDZ domain 1 of harmonin isoforms a, b, and c, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
KLRLVRLDRRGPESLGFSVRGGLEHGCGLFVSHVSPGSQADNKGLRVGDEIVRINGYSISQCTHEEVINL
IKTKKTVSLKVRHVG
>gnl|CDD|467220 cd06738, PDZ2_harmonin, PDZ domain 2 of harmonin isoforms a, b, and c, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
KEKKVFISLVGTRGLGCSISSGPTQKPGIFISNVKPGSLAEEVGLEVGDQIVEVNGTSFTNVDHKEAVMA
LKSSRHLTITVR
>gnl|CDD|467221 cd06739, PDZ3_harmonin, PDZ domain 3 of harmonin isoforms a and b, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of harmonin isoforms a and b, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RQVRLLRIKKNGPLDLALEGGIDSPLGGKIVVSAVYEGGAADKHGGIVKGDQIMMVNGKSLTDVTLAEAE
AALQRAMNSGGDWIDLVIAVAPPK
>gnl|CDD|467222 cd06740, PDZ1_FL-whirlin, PDZ domain 1 of the full-length isoform of whirlin and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
VRQVTLKRSKSHEGLGFSIRGGAEHGVGIYVSLVEPGSLAEKEGLRVGDQILRVNDVSFEKVTHAEAVKI
LRVSKKLVLSVR
>gnl|CDD|467223 cd06741, PDZ2_FL-whirlin, PDZ domain 2 of the full-length isoform of whirlin and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
ERKVNLVVEDGQSLGLMIRGGAEYGLGIYVTGVDPGSVAENAGLKVGDQILEVNGRSFLDITHDEAVKIL
KSSKHLIMTVKDVG
>gnl|CDD|467224 cd06742, PDZ3_FL-whirlin-like, PDZ domain 3 of the full-length isoform of whirlin, PDZ domain 1 of the short isoform of whirlin, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of the full-length isoform of whirlin, PDZ domain 1 of the short isoform of whirlin, and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
TLLVRIKKTKPTLGIAIEGGANTKQPLPRVINIQRGGSAHNCGGLKVGHVILEVNGTSLRGLEHREAARL
IAEAFKNKSRDYIEFLVTEFN
>gnl|CDD|467225 cd06743, PDZ1_L-delphilin-like, PDZ domain 1 of delphilin (L-delphilin isoform), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
PATNQGWPEAFGFSIGGSGPCYILSVEEGSSAHAAGLQPGDQILELDGQDVSSLSCEAIIALARRCPSVP
PSLGVV
>gnl|CDD|467226 cd06744, PDZ2_L-delphilin-like, PDZ domain 2 of delphilin (L-delphilin isoform), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which it is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
TVRVYRGNGSFGFTLRGHAPVYIESVDPGSAAERAGLKPGDRILFLNGLDVRNCSHDKVVSLLQGSGSMP
TLVVE
>gnl|CDD|467227 cd06745, PDZ_SIPA1-like, PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SIPA1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F
ELTLRRNGLGQLGFHVNYEGFVTEVERFGFAWQAGLRQGSRLVEICKVPVATLTHEQMIDLLRTSVKVKV
TVI
>gnl|CDD|467228 cd06746, PDZ_SHANK1_3-like, PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SHANK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F
DSIIDPRTVVLQKGDKGFGFVLRGAKAVGPILEFTPTPAFPALQYLESVDPGGVADKAGLKKGDFLLEIN
GEDVVKASHEQVVNLIRQSGNTLVLKVVTVT
>gnl|CDD|467229 cd06747, PDZ_MYO18-like, PDZ domain of MYO18A protein, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MYO18 protein and related domains. MYO18 (also known as myosin XVIIIA, KIAA0216, MysPDZ), a member of the myosin superfamily, is involved in regulating cell protrusion and migration, and Golgi trafficking and morphology, and is required for myoblast adhesion and muscle integrity. The MYO18A/MRCK/LRAP35a complex regulates actomyosin retrograde flow in cell protrusion and migration; the PtdIns(4)P/GOLPH3/MYO18A/F-actin complex is a hub for signals that regulate Golgi trafficking function. The MYO18A PDZ domain binds p190Rho-guanine nucleotide exchange factor (p190RhoGEF), Golgin45, and leucine repeat adaptor protein 1 (Lurap1, also known as Lrap35a). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MYO18-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F
EITLKRQPTGDFGFSLRRGTIVERGPDDGQELKRTVHFAEPGAGTKNLATGLLPGDRLIEVNGVNVENAS
RDEIIEMIRKSGDTVTLKVQ
>gnl|CDD|467230 cd06748, PDZ_CNK1_2_3-like, PDZ domain of connector enhancer of kinase suppressor of ras 1 (CNK1), CNK2, CNK3, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CNK1 (also known as connector enhancer of KSR 1 (CNKSR1), CNK homolog protein 1, connector enhancer of KSR-like), CNK2 (also known as CNKSR2, CNK homolog protein 2), and CNK3 (also known as CNKSR3, CNK homolog protein 3, CNKSR family member 3, maguin-like). CNK proteins modulate Ras-mediated signaling, acting downstream of Ras as a scaffold for the Raf/MEK/ERK kinase cascade. They also modulate signaling mediated via Rho family small GTPases, through interactions with various guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs), and modulate the insulin signaling pathway through interactions with the Arf guanine nucleotide exchange factors. CNK proteins also regulate cell proliferation and migration by acting as scaffolds for the PI3K/Akt and JNK signaling cascades. CNK2 plays a role in the molecular processes that govern morphology of the postsynaptic density (PSD), and influences subcellular localization of the regulatory NCK-interacting kinase TNIK. TNIK binds a region of CNK2 including the PDZ and the DUF domain; this region also binds the kinase MINK1. CNK2 may also influence the membrane localization of MINK1. CNK3 plays a part in transepithelial sodium transport; it coordinates assembly of an epithelial sodium channel (ENaC)-regulatory complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This CNK1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F
ELVQLTNKKPEEGLGLEIKSTYNGLHVITGTKENSPADRCGKIHAGDEVIQVNYQTVVGWQLKNLVRALR
EDPHGVTLTLK
>gnl|CDD|467231 cd06749, PDZ_densin_erbin-like, PDZ domain of densin, erbin, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of densin, erbin, and related domains. Densin (also known as leucine-rich repeat-containing protein 7, LRRC7, densin-180, protein LAP1) and erbin (also known as densin-180-like protein, Erbb2-interacting protein, protein LAP2) belong to the LAP (leucine-rich repeat and PDZ domain) family of scaffolding proteins that play roles in the maintenance of cell shape and apical-basal polarity. Densin and erbin are components of the excitatory postsynaptic compartment and are regulators of dendritic morphology and postsynaptic structure. The densin PDZ domain binds CaV1.3 alpha1 subunit, delta-catenin, and MAGUIN-1. Binding partners of the erbin PDZ domain include ErbB receptor tyrosine kinase ErbB2, HTLV-1 Tax1, Cav1.3 Ca2+channels, and constituents of the cadherin:catenin cell adhesion complex, in particular delta-catenin, p0071 and ARVCF. The erbin PDZ domain binds Smad3, a transductor of the TGFbeta pathway, possibly by a novel interface of binding. Erbin and two other LAP proteins (scribble and lano) redundantly regulate epithelial polarity and apical adhesion complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This densin and erbin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
IRVRIEKNPGLGFSISGGIGSQGNPFRPDDDGIFVTKVQPDGPASKLLQPGDKILEVNGYDFVNIEHGQA
VSLLKSFQNTVDLVVER
>gnl|CDD|467232 cd06750, PDZ_shroom2_3_4-like, PDZ domain of shroom2, shroom3, shroom4, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of shroom2, shroom3, shroom4, and related domains. Shroom family proteins shroom2 (also known as apical-like protein; protein APXL), shroom3 (also known as shroom-related protein), and shroom4 (also known as second homolog of apical protein) are essential regulators of cell morphology during animal development; they regulate cell architecture by directing the subcellular distribution and activation of Rho kinase (ROCK), which results in the localized activation of non-muscle myosin. The interaction between shroom and ROCK is mediated by the shroom domain 2 (SD2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This shroom2,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
QLIEVQLQGGAPWGFTLKGGLEHGEPLVISKIEEGGKAASVGKLQVGDEVVNINGVPLSGSRQEAIQLVK
GSHKTLKLVVRR
>gnl|CDD|467233 cd06751, PDZ3_PDZD7-like, PDZ domain 3 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of the Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa and can also form homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the third PDZ domain of the canonical isoform of PDZD7- isoform 1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD7-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
LLTVELSKMKQSLGISISGGIESKVQPVVKIEKIFPGGAAALSGNLKAGYELVSVDGESLQQVTHQQAVD
IIRRAYSNKSKEPMEIVVK
>gnl|CDD|467234 cd06752, PDZ_PDZD11-like, PDZ domain of PDZ domain-containing protein 11, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZD11, and related domains. PDZD11 (also known as ATPase-interacting PDZ protein, plasma membrane calcium ATPase-interacting single-PDZ protein, PMCA-interacting single-PDZ protein, PISP) is involved in the dynamic assembly of apical junctions (AJs). It is recruited by PLEKHA7 to AJs to promote the efficient junctional recruitment and stabilization of nectins, and the efficient early phases of assembly of AJs in epithelial cells. The PDZD11 PDZ domain binds nectin-1 and nectin-3. PDZD11 also binds to a PDZ binding motif located in the C-terminal tail of the human sodium-dependent multivitamin transporter, to the cytoplasmic tail of the Menkes copper ATPase ATP7A, and to the cytoplasmic tail of all plasma membrane Ca2+-ATPase b-splice variants. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD11-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RTVVLKRPPGEQLGFNIRGGKASGLGIFISKVIPDSDAHRLGLKEGDQILSVNGVDFEDIEHSEAVKVLK
TAREIQMRVRYFP
>gnl|CDD|467235 cd06753, PDZ_PDLIM-like, PDZ domain of PDZ-LIM family proteins, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDLIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
SVTLSGPAPWGFRLQGGKDFNQPLTISRVTPGGKAAQANLRPGDVILAINGESTEGMTHLEAQNKIKAAT
GSLSLTLER
>gnl|CDD|467236 cd06754, PDZ_LIMK-like, PDZ domain of LIM Kinase (LIMK) family, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the LIMK protein family, and related domains. The LIMK family is composed of LIMK1 and LIMK2, which are common downstream effectors of several signalization pathways and function as signaling nodes that control cytoskeleton dynamics through the phosphorylation of cofilin family proteins. They also control microtubule dynamics. The LIMK1 PDZ domain binds tubulin and nischarin. LIMK1 also binds a carboxy-terminal motif of membrane type 1-matrix metalloproteinase (MT1-MMP, also known as MMP14) having features of a PDZ domain-binding site; MT1-MMP is a major protease involved in dissemination of carcinoma cells during cancer progression. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LIMK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
PHSVTLVSIPPTPEGKRGFSVSVEKGCSEHSHTVRVSELDPMHLSPDLKSLHVGDRILEVNGTPVRDLSL
EEIDDLIQSTSKTLQLTIEHDP
>gnl|CDD|467237 cd06755, PDZ_RapGEF2_RapGEF6-like, PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange factor 6, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Rap guanine nucleotide exchange factor 2 (RapGEF2, also named RA-GEF-1, PDZ-GEF1, CNrasGEF and nRapGEP) and Rap guanine nucleotide exchange factor 6 (RapGEF6, also named RA-GEF-2 and PDZ-GEF2). RapGEF2 and RapGEF6 constitute a subfamily of guanine nucleotide exchange factors (GEFs) for RAP small GTPases that is characterized by the possession of the PDZ and Ras/Rap-associating domains. They activate Rap small GTPases, by catalyzing the release of GDP from the inactive GDP-bound forms, thereby accelerating GTP loading to yield the active GTP-bound forms. The PDZ domain of RapGEF6 (also known as PDZ-GEF2) binds junctional adhesion molecule A (JAM-A). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RapGEF2 and RapGEF6 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RTVTLTRPSRESPLHFSLLGGSEKGFGIFVSKVEKGSKAAEAGLKRGDQILEVNGQNFENITLKKALEIL
RNNTHLSITVKTN
>gnl|CDD|467238 cd06756, PDZ_ARHGAP21_23-like, PDZ domain of ARHGAP21 and ARHGAP23, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ARHGAP21, ARHGAP23, and related domains. This subfamily includes the GAPs (GTPase activating proteins): ARHGAP21 (Rho GTPase-activating protein 21; also known as Rho GTPase-activating protein 10, Rho-type GTPase-activating protein 21) and ARHGAP23 (Rho GTPase-activating protein 23; also known as Rho-type GTPase-activating protein 23). GAPs deactivate Rho GTPases by accelerating GTP hydrolysis. ARHGAP21/23 interact with a planar cell polarity (PCP) protein Pk1 to regulate a lateral signaling pathway in migrating cells. The ARHGAP21 PDZ domain binds claudin-2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ARHGAP21-23-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
PKTVTLQRTSQGFGFTLRHFIVYPPESAVHESLKDEENGNRGGKQRSRLEPMDTIFVKQVKEGGPAHQAG
LCTGDRIVKVNGESVIGKTYSQVIALIQNSDSTLELSVM
>gnl|CDD|467239 cd06758, PDZ2_PDZD2-like, PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains, and is expressed at exceptionally high levels in the pancreas and certain cancer tissues such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RVWKMHLLKEKGGLGIQITGGKGSKRGDIGIFVAGVEEGGSADRDGRLKKGDELLMINGQSLIGLSHQEA
VAILRSSASPVQLVIASK
>gnl|CDD|467240 cd06759, PDZ3_PDZD2-PDZ1_hPro-IL-16-like, PDZ domain 3 of PDZ domain containing 2 (PDZD2), PDZ domain 1 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the first PDZ domain (PDZ1) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16; 1332 amino-acid protein). Precursor IL-16 is cleaved to produce pro-IL-16 and mature IL-16 (derived from the C-terminal 121 AA). Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
STIVLMKGAGGKGLGFSIVGGRDSPRGPMGIYVKTIFPGGAAAEDGRLKEGDEILEVNGESLQGLTHQEA
IQKFKQIKKGLVVLTVR
>gnl|CDD|467241 cd06760, PDZ4_PDZD2-PDZ2_hPro-IL-16-like, PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the second PDZ domain (PDZ2) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16; 1332 amino-acid protein). Precursor IL-16 is cleaved to produce pro-IL-16 and mature IL-16 (derived from the C-terminal 121 AA). Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
DRIIMEVTLNKEPGVGLGIGLCCLPLENDIPGIFIHHLSPGSVAHMDGRLRRGDQILEINGTSLRNVTLN
EAYAILSQCKPGPVTLIISR
>gnl|CDD|467242 cd06761, PDZ5_PDZD2-like, PDZ domain 5 of PDZ domain containing 2 (PDZD2), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
TETINLTRRENESFGLDLEIQATPLKVLVTGLRPGGAAERESMGKLTAGDEIVSINGTPVSAMSYQETCH
LMQNLPKSLTLEVQK
>gnl|CDD|467243 cd06762, PDZ6_PDZD2-PDZ3_hPro-IL-16-like, PDZ domain 6 of PDZ domain containing 2 (PDZD2), PDZ domain 3 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 6 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the third PDZ domain (PDZ3) of human pro-interleukin-16 (isoform 1, also known as nPro-IL-16). Precursor IL-16 is cleaved to produce pro-IL-16 and C-terminal mature IL-16. Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ6 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
IHVVVLHKEEGSGLGFSLAGGSDLENKSITVHRVFPSGLAAQEGTIQKGDRILSINGKSLKGVTHGDALS
VLKQARLPKVAVVVIR
>gnl|CDD|467244 cd06763, PDZ7_PDZD2-PDZ4_hPro-IL-16-like, PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of PDZD2, also known as KIAA0300, PIN-1, PAPIN, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family include the PDZ domain of the secreted mature form of human interleukin-16 (IL-16); this is the fourth PDZ domain (PDZ4) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16). Precursor IL-16 is cleaved to produce pro-IL-16 and C-terminal mature IL-16. Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
AVTVELEKGSAGLGFSLEGGKGSPLGDRPLTIKRIFKGGAAEQSGVLQVGDEILQINGTSLQGLTRFEAW
NIIKSLPEGPVTLLIR
>gnl|CDD|467245 cd06764, PDZ1_DLG5-like, PDZ domain 1 of Discs Large 5 (Dlg5) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
EWETETVEFEKVRDDMDLKALGFDIAGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLT
NKDKKQAIQAVLNGGGVINMVVRRR
>gnl|CDD|467246 cd06765, PDZ2_DLG5-like, PDZ domain 2 of Discs Large 5 (Dlg5) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PSZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
HINLSGQKDSGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSL
SLMKVFP
>gnl|CDD|467247 cd06766, PDZ4_DLG5-like, PDZ domain 4 of Discs Large 5 (Dlg5) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPDGLVPGDLILEYNSVDMRNKTAEEAYLEML
KPAETVTLKVQ
>gnl|CDD|467248 cd06767, PDZ3_DLG5-like, PDZ domain 3 of Discs Large 5 (Dlg5) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
EEPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILR
QCGDTITMLVQY
>gnl|CDD|467249 cd06768, PDZ_NHERF-like, PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This NHERF-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RLCHLVKGPEGYGFNLHAEKGRPGHFIREVDPGSPAERAGLKDGDRLVEVNGENVEGESHEQVVEKIKAS
GNQVTLLVVD
>gnl|CDD|467250 cd06769, PDZ_FRMPD1_3_4-like, PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of FRMPD1, FRMPD3, FRMPD4, and related domains. FRMPD1 (also known as FERM domain-containing protein 2, FRMD2), inhibits the malignant phenotype of lung cancer by activating the Hippo pathway via interaction with WWC3; the FRMPD1 PDZ domain binds WWC3. FRMPD3 is a target gene of the neuron-specific transcription factor NPAS4 that is involved in synaptic plasticity. FRMPD4 (also known as PDZ domain-containing protein 10, PDZD10, PDZK10, PSD-95-interacting regulator of spine morphogenesis, and Preso) regulates dendritic spine morphogenesis, and mGluR1/5 signaling; the FRMPD4 PDZ domain binds PAK-interacting exchange factor-beta (betaPix). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This FRMPD1,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
TVEIQRDAVLGFGFVAGSERPVVVRSVTPGGPSEGKLLPGDQILKINNEPVEDLPRERVIDLIRECKDSI
VLTVL
>gnl|CDD|467619 cd06775, cpPDZ_MBTPS2-like, circularly permuted PDZ domain of membrane-bound transcription factor site-2 protease (MBTPS2, also known as S2P) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MBTPS2, also known as sterol regulatory element-binding protein (SREBP) Site-2 protease (S2P), and related domains. MBTPS2 is a zinc metalloprotease (MEROPS family M50A). In the Golgi, it catalyzes the second step in the proteolytic activation of sterol regulatory element-binding proteins (SREBPs), releasing the transcriptionally active N-terminal domain of SREBP, which then enters the nucleus and activates genes encoding the low density lipoprotein (LDL) receptor and enzymes for cholesterol and fatty acid biosynthesis. MBTPS2 also mediates the second step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF6. ATF6 is a membrane-bound transcription factor that activates genes in the endoplasmic reticulum (ER) stress response. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. One permutation places beta-strand A on the C-terminus, another permutation places both beta-strands A and B on the C-terminus
IYCAGVWHNFVLVLVALLVLFLLPFLLSPFYYTGSGVVVTEVVENSPVSGPRGLFVGDVITSINDCPVTS
VEDWMKCLEEVSKSPQSGYCVSADFLQQLDTSSRVYK
>gnl|CDD|467620 cd06777, cpPDZ_DegS, circularly permuted PDZ domain of DegS serine endoprotease. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Escherichia coli DegS and related domains. DegS (also known as Site-1 protease DegS, S1P protease DegS, and Site-1-type intramembrane protease) participates in the activation of the sigma(E) extracytoplasmic stress response. Initially, there is an accumulation of misfolded membrane proteins (OMPs) in the periplasm which bind by their YXF motif to the DegS PDZ domain, activating DegS-catalyzed cleavage of the RseA periplasmic domain and making RseA a substrate for cleavage by another membrane protease RseP. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This DegS family PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus
RGYLGITLSEIPPAMARGGGIDQLQGALVKGVSPDSPAAKAGIQVGDIILQFDNKPVISVLELMDLVAEI
RPGTVIPVVVLRDGKQLTLEVTI
>gnl|CDD|467621 cd06779, cpPDZ_Deg_HtrA-like, permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping serine proteases and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Deg/HtrA-type serine proteases that participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. Typically, these proteases have an N-terminal serine protease domain and at least one C-terminal PDZ domain that recognizes substrates, and in some cases activates the protease function. An exception is yeast Nma11p which has two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. HtrA-type proteases include the human HtrA1-4 and MBTPS2, tricorn protease, DegS, DegP and C-terminal processing peptidase, cyanobacterial serine proteases Hhoa, HhoB, and HtrA, and yeast Nma11p. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-termini of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This Deg/HtrA family PDZ domain is a circularly permuted PDZ domain which places beta-strand A at the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus
RPYLGIEMENISPLLAKELGLPVNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAALDTK
KPGDSLNLTILRDGKTLTVTV
>gnl|CDD|467622 cd06781, cpPDZ_BsHtra-like, circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and YyxA and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Bacillus subtilis HtrA/YkdA, HtrB/YvtA and YyxA/YycK, and related domains. HtrA-type serine proteases participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. HtrA, HtrB, and YyxA have a single transmembrane domain at the N-terminus and a PDZ domain at the C-terminus. Expression of htrA and htrB genes is induced both by heat shock and by secretion stress (by a common) mechanism; yyxA is neither heat shock nor secretion stress inducible. HtrA and HtrB may have overlapping cellular functions; YyxA may have a cellular function distinct from the other two proteases or have the same function but under different conditions. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This BsHtrA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus
RPSLGISMVDLSDVPEYEQQSLKLPSNVNKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLRQ
ILYSHKVGDTVKVTIYRDGKEKTLNIKL
>gnl|CDD|467623 cd06782, cpPDZ_CPP-like, circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CPP (also known as tail-specific protease, PRC protein, Protease Re, and Photosystem II D1 protein processing peptidase), and related domains. CPP belongs to the peptidase S41A family. It cleaves a C-terminal 11 residue peptide from the precursor form of penicillin-binding protein 3, and may have a role in protecting bacterium from thermal and osmotic stresses. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This CPP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus
FGGIGIEIGKDDDGYLVVVSPIPGGPAEKAGIKPGDVIVAVDGESVRGMSLDEVVKLLRGPKGTKVKLTI
RRGGEGEPRDVTLTREKI
>gnl|CDD|467624 cd06785, cpPDZ_HtrA-like, circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine proteases and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of HtrA family serine proteases including human HtrA1, HtrA2 (mitochondrial), HtrA3, and HtrA4, and related domains. These proteases are key enzymes associated with pregnancy. Their diverse biological functions include cell growth proliferation, migration and apoptosis. They are also implicated in disorders including Alzheimer's, Parkinson's, arthritis and cancer. HtrA1 (also known as high-temperature requirement A serine peptidase 1, L56, and serine protease 11) substrates include extracellular matrix proteins, proteoglycans, and insulin-like growth factor (IGF)-binding proteins. HtrA1 also inhibits signaling by members of the transforming growth factor beta (TGF-beta) family. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This HtrA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus
KRYIGIRMLTLTPSLLEELKQRNPDFPDVSSGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSDVY
EAVKSGSSLLVVVRRGNEDLLLTVTPEE
>gnl|CDD|467625 cd06786, cpPDZ1_ScNma111-like, circularly permuted first PDZ domain (PDZ1) of Saccharomyces cerevisiae pro-apoptotic serine protease Nma111p and related domains. First PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the HtrA-type protease Saccharomyces cerevisiae Nma111p (also known as Ynm3p), and related domains. Nma111p is a nuclear serine protease which mediates apoptosis through proteolysis of the apoptotic inhibitor Bir1p. Nma111p is composed of two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This ScNma111-like PDZ1 domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation places both beta-strands A and B on the C-terminus
CRRLGLTPETEAAVRKAFPSETGMLVAETVLPEGPADGKLEEGDVLISVNGELITQFIRLEEILDENVGK
TVELVVQRGGEEITVTITV
>gnl|CDD|467626 cd06787, cpPDZ_AthDEGP7-like, circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 7 (DEGP7) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Arabidopsis thaliana putative protease DEGP7 (also known as DegP protease 7, DEG7), and related domains. DEGP7 belongs to the HtrA family of housekeeping proteases. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This AtDEGP7-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus
ARSFGLSDKWVQALVKKDPVRRQVLRVKGCLAGSKAENALEQGDMVLAINGEPVTCFRDVERACQVLKTG
DSSDGPLNLTVFRQGQEVDVVV
>gnl|CDD|467251 cd06789, PDZ_AFDN-like, PDZ domain of afadin (AFDN), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of afadin (AFDN, also known as ALL1-fused gene from chromosome 6 protein (AF6) and MLLT4), and related domains. AFDN belongs to the adhesion system, probably together with the E-cadherin-catenin system, that plays a role in the organization of homotypic, interneuronal, and heterotypic cell-cell adherens junctions. The AFDN PDZ domain interaction partners include poliovirus receptor-related protein PRR2/nectin, the junctional adhesion molecule (JAM), the breakpoint-cluster-region protein (BCR), connexin36 (Cx36), and a subset of Eph-related receptor tyrosine kinases; it can also bind low molecular weight ligands, in competition with a natural peptide ligand. Other AFDN-binding proteins have been identified. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This AFDN family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
PEIITVTLKKVGNGMGLSIVAAKGAGQDKLGIYIKSVVKGGAADLDGRLQAGDQLLSVDGHSLVGLSQER
AAELMTKTGSVVTLEVAKQ
>gnl|CDD|467252 cd06790, PDZ_neurabin-like, PDZ domain of neurabin-1 and neurabin-2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of neurabin-1 (also known as protein phosphatase 1 regulatory subunit 9A) and neurabin-2 (also known as spinophilin, and protein phosphatase 1 regulatory subunit 9B), and related domains. Neurabin-1 and neurabin-2 are neuronal scaffolding proteins that play important roles in the regulation of synaptic transmission through their ability to interact with and target protein phosphatase 1 (PP1) to dendritic spines where PP1 dephosphorylates and inactivates glutamate receptors. Neurabin-2 interacts with multiple other synaptic proteins, including synaptic signaling and scaffolding proteins (e.g., GluN1 and SAPAP3) and cytoskeletal proteins (e.g., neurofilament medium polypeptide, NF-M). Neurabin-1 and neurabin-2 also binds F-actin. Other binding partners of neurabin-1 include adenosine A1 receptor (A1R), SAD-1 kinase and 70 kDa ribosomal protein S6 kinase (p70-S6K). This PDZ domain is immediately C-terminal to the PP1 binding domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This neurabin-like PDZ domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
DLFPVELEKGSEGLGISIIGMGVGADAGLEKLGIFVKTVTEGGAAQRDGRIQVNDQIVEVDGISLVGVTQ
AFAASVLRNTSGTVRFLIGR
>gnl|CDD|467253 cd06791, PDZ3_MUPP1-like, PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
ETFEVELVKDEQGLGITIAGYVGEKASGELSGIFVKSIIPGSAADQDGRIQVNDQIIAVDGVNLQGFTNQ
EAVEVLRNTGQVVHLTLAR
>gnl|CDD|467254 cd06792, PDZ2-PTPN13_FRMPD2-like, PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and similar domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of human PTPN13, and related domains. PTPN13, also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1), negatively regulates FAS-mediated apoptosis and NGFR-mediated pro-apoptotic signaling, and may also regulate phosphoinositide 3-kinase (PI3K) signaling. It contains 5 PDZ domains; interaction partners of its second PDZ domain (PDZ2) include the Fas receptor (TNFRSF6) and thyroid receptor-interacting protein 6 (TRIP6). The second PDZ (PDZ2) domain, but not PDZ1 or PDZ3, of FRMPD2 binds to GluN2A and GluN2B, two subunits of N-methyl-d-aspartic acid (NMDA) receptors. Other binding partners of the FRMPDZ2 PDZ2 domain include NOD2, and catenin family members, delta catenin (CTNND2), armadillo repeat gene deleted in velo-cardio-facial syndrome (ARVCF) and p0071 (also known as plakophilin 4; PKP4). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
DVFEVELSKKDGSLGISVTGGINTSVRHGGIYVKSLVPGGAAEQDGRIQKGDRLLEVNGVSLEGVTHKQA
VECLKNAGQVVTLVLER
>gnl|CDD|467255 cd06793, PDZ2_APBA1_3-like, PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, APBA3, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of APBA1, APBA2, APBA3, and related domains. The APBA/X11/Mint protein family includes three members: neuron specific APBA1 (also known as X11alpha and Mint1) and APBA2 (also known as X11beta and Mint2), and the ubiquitously expressed APBA3 (also known as X12gamma and Mint3). They are involved in regulating neuronal signaling, trafficking, and plasticity. They contain two PDZ domains (PDZ1 and PDZ2) which bind a variety of proteins: Arf GTPases (APBA1 and APBA2 PDZ2) and neurexin (APBA1 and APBA2 PDZ1 and 2) which are involved in vesicle docking and exocytosis; alpha1B subunit of N-type Ca2+ channel (APBA1 PDZ1) that is involved in ion channels; KIF17 (APBA1 PDZ1) that is involved in transport and traffic; and Alzheimer's disease related proteins, APP (APBA3 PDZ2), CCS (APBA1 PDZ2), NF-kappa-B/p65 (APBA2 PDZ2), presenilin-1 (APBA1 and APBA2 PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This APBA1,3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
PVTTVLIRRPDLKYQLGFSVQNGIICSLLRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVQLLSNSVG
EIHMKTMP
>gnl|CDD|467256 cd06794, PDZ2_syntenin-like, PDZ domain 2 of syntenin-1, syntenin-2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of syntenin-1, syntenin-2, and related domains. Syntenins are implicated in various cellular processes such as trafficking, signaling, and cancer metastasis. They bind to signaling and adhesion molecules, such as syndecans, neurexins, ephrin B, and phospholipid PIP2. Through its tandem PDZ domains (PDZ1 and PDZ2) syntenin links syndecans to other cell surface receptors and kinases, such as E-cadherin and ephrin-B, establishing signaling crosstalk. During syndecan binding, syntenin PDZ2 serves as a high-affinity domain, and PDZ1, also necessary for binding, acts as a complementary, low-affinity domain; this is also the case for syntenin binding to proto-oncogene c-Src. The syntenin PDZ domain-PIP2 interaction controls Arf6-mediated syndecan recycling through endosomal compartments; both PDZ1 and PDZ2 interact with PIP2. Different binding partners and downstream regulators of syntenin1 PDZ domains, such as to proto-oncogene c-Src, mitogen-activated protein kinase (MAPK), and focal adhesion kinase (FAK), have been identified that promote the progression and invasion of a variety of cancers, such as melanoma, glioblastoma multiforme, and breast cancer. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This syntenin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F
RPFERTITMHKDSTGHVGFVFKNGKITSIVKDSSAARNGLLTDHQLCEVNGQNVIGLKDKEIADILATAG
RVVTITIM
>gnl|CDD|467257 cd06795, PDZ3_Dlg1-2-4-like, PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila Dlg1, human Dlg1, 2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197; SAP-97), Dlg2 (also known as channel-associated protein of synapse-110; postsynaptic density protein 93, PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95; synapse-associated protein 90, SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling, regulating surface expression of NMDA receptors in dorsal horn neurons of the spinal cord; it interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. The Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development; postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
EPRKIVLHKGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQAAAAL
KNAGQTVTIIAQYKPEEYSRF
>gnl|CDD|467258 cd06796, PDZ_Lin-7-like, PDZ domain of protein Lin-7 and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Lin-7 (also known as LIN-7 or LIN7), and related domains. Lin-7 targets and organize protein complexes to epithelial and synaptic plasma membranes. There are three mammalian Lin-7 homologs: Lin-7A (protein lin-7 homolog A, also known as mammalian lin-seven protein 1 (MALS-1), vertebrate lin-7 homolog 1 (Veli-1), tax interaction protein 33); Lin-7B (also known as MALS-2, Veli-2); and Lin-7C (also known as MALS-3, Veli-3). Lin-7 is involved in localization of the Let-23 growth factor receptor to the basolateral membrane of epithelial cells, in tight junction localization of insulin receptor substrate p53 (IRSp53), in retaining gamma-aminobutyric (GABA) transporter (BGT-1) at the basolateral surface of epithelial cells, and in regulating recruitment of neurotransmitter receptors to the postsynaptic density (PSD). The Lin7 PDZ domain binds Let-23, BGT and beta-catenin, and NMDA (N-methyl-D-aspartate) receptor NR2B. Lin-7 also binds to the PDZ binding motif located in the C-terminal tail of Rhotekin, an effector protein for small GTPase Rho. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Lin-7-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
HPRVVELPKTEEGLGFNVMGGKEQNSPIYISRIIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVEL
LKAAQGSVKLVVRYTP
>gnl|CDD|467259 cd06798, PDZ_MPP5-like, PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP5, Drosophila Stardust, and related domains. MPP5 (also known as MAGUK p55 subfamily member 1, protein associated with Lin-7 1 or PALS1) and Drosophila Stardust are membrane-associated guanylate kinase (MAGUK)-like proteins that serve as signaling and scaffolding proteins, linking different proteins critical to the formation and maintenance of tight junctions (TJ) and apical-basal polarity. Apical-basal polarity determinants cluster in complexes; in particular, the Crumbs complex (Crb, MPP5, and PATJ) and the PAR/aPKC-complex (PAR-3, PAR-6, aPKC) determine the apical plasma membrane domain. Within the Crumbs complex, Crb is stabilized in the plasma membrane by MPP5, which in turn recruits PATJ and Lin-7 to the complex. MPP5 also links the Crumbs complex with the PAR/aPKC-complex. The Drosophila homolog of the Crumbs complex is the (CRB)-Stardust (Sdt)-Discs Lost (Dlt) complex. MPP5 also acts as an interaction partner for SARS-CoV envelope protein E, which results in delayed formation of TJs and dysregulation of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP5-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
KIVRIEKTREPLGATVRNEGDSVIISRIVKGGAAEKSGLLHEGDEILEINGIEIRGKDVNEVCDLLADMH
GTLTFLLIP
>gnl|CDD|467260 cd06799, PDZ_MPP3-MPP4-MPP7-like, PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP3, MPP4, and MPP7, and related domains. MPP3 (also known as MAGUK p55 subfamily member 3, erythrocyte membrane protein p55, or EMP55), MPP4 (also known as MAGUK p55 subfamily member 4 or Discs large homolog 6), and MPP7 (also known as MAGUK p55 subfamily member 7) are membrane-associated guanylate kinase (MAGUK)-like proteins. MPP3 is part of a cell adhesion protein complex including tumor suppressor CADM1 and actin-binding protein 4.1B. Participation in the Crumbs cell polarity complex has also been demonstrated for MPP7 in epithelial cells, and for MPP3 and MPP4 in the retina. MPP4 is needed for proper localization of plasma membrane calcium ATPases and maintenance of calcium homeostasis at the rod photoreceptor synaptic terminals. Binding partners of the MPP3 PDZ domain include nectin-3, serotonin 5-hydroxytryptamine, 5-HT(2C) receptor, and a cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1); fragments of MPP4 having the PDZ domain bind CRB (PDZ-SH3-GUK) and GABA transporter GAT1 (PDZ-SH3). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
KIVRLVKNNEPLGATIKRDEKTGAIVVARIMRGGAADRSGLIHVGDELREVNGISVEGKDPEEVIQILAN
SQGPITFKLIP
>gnl|CDD|467261 cd06800, PDZ_GOPC-like, PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GOPC and related domains. GOPC, also known as PIST (PDZ domain protein interacting specifically with TC10), FIG (fused in glioblastoma), and CAL (CFTR-associated ligand), regulates the trafficking of a wide array of proteins, including small GTPases, receptors, and cell surface molecules such as cadherin 23 and CFTR. It may regulate CFTR chloride currents and acid-sensing ASIC3 currents by modulating cell surface expression of both channels, and may play a role in autophagy. Interaction partners of the GOPC PDZ domains include: FZD5, FZD8, ASIC3, CFTR, MUC3, ARFRP1, Ggamma13, neuroligin, and Stargazin. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GOPC-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RKVLLSKEPHEGLGISITGGKEHGVPILISEIHEGQPADRCGGLYVGDAILSVNGIDLRDAKHKEAVTIL
SQQRGEITLEVVY
>gnl|CDD|467262 cd06801, PDZ_syntrophin-like, PDZ domain of syntrophins, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of syntrophins (including alpha-1-syntrophin, beta-1-syntrophin, beta-2-syntrophin, gamma-1-syntrophin, and gamma-2-syntrophin), and related domains. Syntrophins play a role in recruiting various signaling molecules into signaling complexes and help provide appropriate spatiotemporal regulation of signaling pathways. They function in cytoskeletal organization and maintenance; as components of the dystrophin-glycoprotein complex (DGC), they help maintain structural integrity of skeletal muscle fibers. They link voltage-gated sodium channels to the actin cytoskeleton and the extracellular matrix, and control the localization and activity of the actin reorganizing proteins such as PI3K, PI(3,4)P2 and TAPP1. Through association with various cytoskeletal proteins within the cells, they are involved in processes such as regulation of focal adhesions, myogenesis, calcium homeostasis, and cell migration. They also have roles in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This syntrophin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RTVRVVKQDVGGLGISIKGGAEHKMPILISKIFKGQAADQTGQLFVGDAILSVNGENLEDATHDEAVQAL
KNAGDEVTLTVKY
>gnl|CDD|143484 cd06808, PLPDE_III, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes. The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity
IRHNYRRLREAAPAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQ
VSELEDAAEQGVIVVTVDSLEELEKLEEAALKAGPPARVLLRIDTGDENGKFGVRPEELKALLERAKELP
HLRLVGLHTHFGSADEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQELPLGTFIIVEPG
R
>gnl|CDD|143485 cd06810, PLPDE_III_ODC_DapDC_like, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate Decarboxylases, and Related Enzymes. This family includes eukaryotic ornithine decarboxylase (ODC, EC 4.1.1.17), diaminopimelate decarboxylase (DapDC, EC 4.1.1.20), plant and prokaryotic biosynthetic arginine decarboxylase (ADC, EC 4.1.1.19), carboxynorspermidine decarboxylase (CANSDC), and ODC-like enzymes from diverse bacterial species. These proteins are fold type III PLP-dependent enzymes that catalyze essential steps in the biosynthesis of polyamine and lysine. ODC and ADC participate in alternative pathways of the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. ODC catalyzes the direct synthesis of putrescine from L-ornithine, while ADC converts L-arginine to agmatine, which is hydrolysed to putrescine by agmatinase in a pathway that exists only in plants and bacteria. DapDC converts meso-2,6-diaminoheptanedioate to L-lysine, which is the final step of lysine biosynthesis. CANSDC catalyzes the decarboxylation of carboxynorspermidine, which is the last step in the synthesis of norspermidine. The PLP-dependent decarboxylases in this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Prokaryotic ornithine, lysine and biodegradative arginine decarboxylases are fold type I PLP-dependent enzymes and are not included in this family
TPFYVYDLDIIRAHYAALKEALPSGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPE
RIIFTGPAKSVSEIEAALASGVDHIVVDSLDELERLNELAKKLGPKARILLRVNPDVSAGTHKISTGGLK
SKFGLSLSEARAALERAKELDLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGG
LGIPYDEQPLDFEEYAALINPLLKKYFPNDPGVTLILEPGRYIVAQAGVLVTRVVAVKVNGGRFFAVVDG
GMNHSFRPALAYDAYHPITPLKAPGPDEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYG
FSESSNFNSHPRPAEYLV
>gnl|CDD|143486 cd06811, PLPDE_III_yhfX_like, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme yhfX. This subfamily is composed of the uncharacterized protein yhfX from Escherichia coli K-12 and similar bacterial proteins. These proteins are homologous to bacterial alanine racemases (AR), which are fold type III PLP-dependent enzymes containing an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. It catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. Members of this subfamily may act as PLP-dependent enzymes
MFLEALLKRNPALIEAALTLHQSGAIPPDTYVIDLDQIEENARLLAETAEKYGIELYFMTKQFGRNPFLA
RALLEAGIPGAVAVDFKEARALHEAGLPLGHVGHLVQIPRHQVPAVLAMRPEVITVYSLEKAREISDAAV
ELGRVQDVLLRVYGDEDTLYPGQEGGFPLEELPAVLAAIKALPGIRIAGLTSFPCFLYDEEQGDIAPTPN
LFTLLKAKELLEKRGIEILQLNAPSATSCATLPLLAEYGVTHGEPGHALTGTTPLHAVGDQPEKPAMVYV
SEVSHTFGGHSYCYGGGFYRRSHLKNALVGTDPDDASAHRAELLDPENIDYYGTLDGPEFAVGDTVIMAF
RTQIFVTRSDVALVSGIASGKPRLVGIYDSQG
>gnl|CDD|143487 cd06812, PLPDE_III_DSD_D-TA_like_1, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase, Unknown Group 1. This subfamily is composed of uncharacterized bacterial proteins with similarity to eukaryotic D-serine dehydratases (DSD) and D-threonine aldolases (D-TA). DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. DSD and D-TA are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on their similarity to AR, it is possible members of this family also form dimers in solution
LAALDTPFLLLDEARMDRNIARLRQRLSRLGVRLRPHLKTAKSLEVARRLLAAGASPATVSTLKEAEAFA
EAGYRDILYAVGIAPAKLPRVLALRRQGVNLTILLDSVEQAQAVAAFSRQHGVRFPVLIEIDCDGHRGGI
APDSDALLEIARILHDGGAELRGVLTHAGESYACRTPEALAAAAEQERAAAVRAAERLRAAGLPCPVVSV
GSTPTAHFAEDLTGVTEVRAGVYVFFDLVMAGIGVCGLDDIALSVVTTVIGHQPEKGWILIDAGWMALSR
DRGTARQAVDQGYGLVCDVAGSPLPGLIVTSTNQEHGIIALRGGSDLSLPDLPIGTRLRILPNHACATAA
QHDHYHVLDGEGVVQATWSRINGW
>gnl|CDD|143488 cd06813, PLPDE_III_DSD_D-TA_like_2, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase, Unknown Group 2. This subfamily is composed of uncharacterized bacterial proteins with similarity to eukaryotic D-serine dehydratases (DSD) and D-threonine aldolases (D-TA). DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. DSD and D-TA are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on their similarity to AR, it is possible members of this family also form dimers in solution
RYREAFAGLDAPFAFVDLDALDANAADLVRRAGGKPIRVASKSVRCRALLRRVLAAPGFQGVMAFTLAEA
LWLARQGFDDILVAYPSVDRAALRELAADPKLGATITLMVDSVEHLDLLDAVAAPMRVEVRVCIDIDASL
RFGGLHFGVRRSPLHTPAQALALAKAIAARPGLRLVGLMGYEAQIAGVGDSVPGKRVKSAVIRLLKKRSI
KELAERRAAVVAALRAEGEDLEFVNGGGTGSLESTAADAVVTEVTAGSGLYAPALFDHYRSFQPEPAAGF
ALPVVRRPAPGIVTCLGGGYIASGPAGKDRLPVPWLPAGLKLLPLEGAGEVQTPLTGPAAERLGIGDPVW
FRHAKAGELCERFNELHLVRGGEIVGTVPTYRGEGQCF
>gnl|CDD|143489 cd06814, PLPDE_III_DSD_D-TA_like_3, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase, Unknown Group 3. This subfamily is composed of uncharacterized bacterial proteins with similarity to eukaryotic D-serine dehydratases (DSD) and D-threonine aldolases (D-TA). DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. DSD and D-TA are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on their similarity to AR, it is possible members of this family also form dimers in solution
ALKQAGIGEPTLLLDKDRLDHNIDLLREHLAGSLAYRIVAKSLPSPPLLRHIMKRAGTRRLMVFHQPFLN
AVAKAFPDADILLGKPMPVAAAARFYRQLTGSAFRPARQLQWLIDTPERLAQYRALARSLGLTLRINLEL
DVGLHRGGFADPQTLPKALTAIDAPPRLRFSGLMGYEPHVAKLPGLISPAKARAAAMARYQAFVALARAH
LGAHTQKLTLNTGGSPTYRLYEGDGPVNEVSAGSALVKPTDFDLPALEDHQPALFIATPVLKVLDALEIP
GLPGLGRLLPLWNPNRRRAYFIYGGNWKADPVSPAGLRYNGLYGRSSNQEMLNGSASSQLKVDDYVFLRP
TQSEAVLLQFGDILVVRGGQIIDRWPVLP
>gnl|CDD|143490 cd06815, PLPDE_III_AR_like_1, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1. This subfamily is composed of uncharacterized bacterial proteins with similarity to bacterial alanine racemases (AR), which are fold type III PLP-dependent enzymes containing an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. It catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. Members of this subfamily may act as PLP-dependent enzymes
YPRLEINLSKIRHNAKVLVELCKSRGIEVTGVTKVVCGDPEIAEALLEGGITHLADSRIENLKKLKDLGI
SGPKMLLRIPMLSEVEDVVKYADISLNSELETIKALSEEAKKQGKIHKIILMVDLGDLREGVLPEDLLDF
VEEILKLPGIELVGIGTNLGCYGGVLPTEENMGKLVELKEEIEKEFGIKLPIISGGNSASLPLLLKGELP
GGINQLRIGEAILLGRETTYNEPIPGLYQDAFTLEAEIIEIKEKPSVPIGEIGLDAFGNKPEFEDRGIRK
RAILAIGRQDVDPDGLTPVDNGIEILGASSDHLILDITDSDRDYKVGDEIRFNLDYGALLRAMTSPYVEK
VYI
>gnl|CDD|143491 cd06817, PLPDE_III_DSD, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Eukaryotic D-Serine Dehydratase. This subfamily is composed of chicken D-serine dehydratase (DSD, EC 4.3.1.18) and similar eukaryotic proteins. Chicken DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. It is a fold type III PLP-dependent enzyme with similarity to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as dimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Experimental data suggest that chicken DSD also exists as dimers. Sequence comparison and biochemical experiments show that chicken DSD is distinct from the ubiquitous bacterial DSDs coded by dsdA gene, mammalian L-serine dehydratases (LSD) and mammalian serine racemase (SerRac), which are fold type II PLP-dependent enzymes
LSDLPTPALVIDRAKFKRNCERMLQRAKALGVKFRPHVKTHKTLEGTRLQLGEGRPSRGIVVSTLAEAEF
LLPLGEEGRVDDILYGLPVPPSKLPRLAELSKKLGHLRVMVDNPEQLDFLEQFQPLKSGKKWSVFIKVDC
GTHRAGVPPESEDAKELIQKLEKASEAVELFGFYSHAGHSYSSRSAEDAKEVLREEIEAVLTAAKKLKSI
QGDRKLTLSVGATPTAHAAEALVLIPAPSLSGLLELHAGNYPFYDLQQVATGLCSEEDIAVFVLAEVISV
YPKRNEALVNAGVLALSREPSRIYGGFGRVIPWPGPIPGHPEWYLVRLSQEHGILQPRDGDLDFKRLKVG
SKVRIIPQHACITAAMFPVYYVVDSGDIVVDVWVPWKGW
>gnl|CDD|143492 cd06818, PLPDE_III_cryptic_DSD, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bacterial Cryptic D-Serine Dehydratase. This subfamily is composed of Burkholderia cepacia cryptic D-serine dehydratase (cryptic DSD), which is also called D-serine deaminase, and similar bacterial proteins. Members of this subfamily are fold type III PLP-dependent enzymes with similarity to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as dimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on similarity, it is possible cryptic DSDs may also form dimers. Cryptic DSDs are distinct from the ubiquitous bacterial DSDs coded by the dsdA gene, mammalian L-serine dehydratases (LSD) and mammalian serine racemase (SerRac), which are fold type II PLP-dependent enzymes. At present, the enzymatic and biochemical properties of cryptic DSDs are still poorly understood. Typically, DSDs catalyze the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia
VSLPLLVLDASALAHNLAWMQAFAAAHGVKLAPHGKTTMAPQLFRRQLEAGAWGITVATVAQARVALAFG
VRRVLLANQLVGKANLRRLAALLAADPDFEFFCLVDSVDNVRALAAFFAALERPLNVLIELGVPGGRTGV
RTEAEALALADAIAASPALRLAGVEGYEGVAAHDDSEETLAAVRAFLARAVDLARRLAERGLFPDRELIL
TAGGSAWFDLVAEALAALALDGPVTLVLRSGCYVTHDHGIYRRAQQALRARDPLSLAGALRPALEIWAYV
QSRPEPGLAILGMGKRDVAFDAGLPVPLRVFRPGGGVVRLPDGWEVTALNDQHAFLRLPPESPLAVGDVI
AFGISHPCTTFDKWRVILLVDDDYRVVDAVTT
>gnl|CDD|143493 cd06819, PLPDE_III_LS_D-TA, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase. Low specificity D-threonine aldolase (Low specificity D-TA, EC 4.3.1.18), encoded by dtaAS gene from Arthrobacter sp. strain DK-38, is the prototype of this subfamily. Low specificity D-TAs are fold type III PLP-dependent enzymes that catalyze the interconversion between D-threonine/D-allo-threonine and glycine plus acetaldehyde. Both PLP and divalent cations (eg. Mn2+) are required for catalytic activity. Members of this subfamily show similarity to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on its similarity to AR, it is possible that low specificity D-TAs also form dimers in solution. Experimental data show that the monomeric form of low specificity D-TAs exhibit full catalytic activity
PLAEIDTPALVLDLDALERNIKRMAAFAKAHGVRLRPHAKTHKCPAIARRQIAAGAVGVCCQKLSEAEVM
AAAGIRDILITNEVVGPAKIARLAALARRAPLIVCVDHPDNVRALAAAAVEAGVRLDVLVEIDVGQGRCG
VPPGEAALALARTIAALPGLRFAGLQAYHGHLQHIRDYEERRAAIAEAAEALQATRDALEAAGLPCEIVT
GGGTGTYEFEAASGVYTELQAGSYVFMDADYGDNEDEGGAPPFENALFVLTTVISANAPGRAVVDAGLKS
LSVDSGLPKVAGRPGLSYVRAGDEHGIVELEDGAAPLKIGDRLELVPGHCDPTVNLHDWYVGVRGGVVED
VWPISARG
>gnl|CDD|143494 cd06820, PLPDE_III_LS_D-TA_like, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine Aldolase-like. This subfamily is composed of uncharacterized bacterial proteins with similarity to low specificity D-threonine aldolase (D-TA), which is a fold type III PLP-dependent enzyme that catalyzes the interconversion between D-threonine/D-allo-threonine and glycine plus acetaldehyde. Both PLP and divalent cations (eg. Mn2+) are required for catalytic activity. Low specificity D-TAs show similarity to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on its similarity to AR, it is possible that low specificity D-TAs also form dimers in solution. Experimental data show that the monomeric form of low specificity D-TAs exhibit full catalytic activity
LDTPALLIDLDRLERNIARMQAYADAHGLSLRPHIKTHKSPEIARLQLAAGAIGITVATVGEAEVMADAG
LSDIFIAYPIVGRQKLERLRALAERVTLSVGVDSAEVARGLAEVAEGAGRPLEVLVEVDSGMNRCGVQTP
EDAVALARAIASAPGLRFRGIFTYPGHSYAPGALEEAAADEAEALLAAAGILEEAGLEPPVVSGGSTPTL
WRSHEVPGITEIRPGTYIFNDASQVALGACTLDDCALTVLATVVSRPTAERAVLDAGSKALTSDRGTGTT
GYGHLLEYPDARIVGLSEEHGVIDLSGCDALPRVGDRVRVVPNHACVVVNLVDEVYLVDGGEVVETWPVA
ARG
>gnl|CDD|143495 cd06821, PLPDE_III_D-TA, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase. D-threonine aldolase (D-TA, EC 4.3.1.18) reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Its activity is present in several genera of bacteria but not in fungi. It requires PLP and a divalent cation such as Co2+, Ni2+, Mn2+, or Mg2+ as cofactors for catalytic activity and thermal stability. Members of this subfamily show similarity to bacterial alanine racemase (AR), a fold type III PLP-dependent enzyme which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on its similarity to AR, it is possible that low specificity D-TAs also form dimers in solution. Experimental data show that the monomeric form of low specificity D-TAs exhibit full catalytic activity
IKNTDEIISPALAVYPDRIEENIRRMIRMAGDPQRLRPHVKTHKMAEIVRLQLEAGITKFKCATIAEAEM
LAEAGAPDVLLAYPLVGPNIERFLELAKKYPGTRFSALVDDLEAAEALSAAAGSAGLTLSVLLDVNTGMN
RTGIAPGEDAEELYRAIATLPGLVLAGLHAYDGHHRNTDLAEREAAADAAYKPVLALREALEAAGLPVPE
LVAGGTPSFPFHAAYTDVECSPGTFVLWDAGYGSKLPDLGFKPAALVVTRVISHPTAGRVTLDLGHKAVA
SDPPLPRVCLLGLPDAEPVGHSEEHLVLETPEAARPEIGDVLYGIPRHICPTVALYDEALVVRDGRIVGT
WPVAARNRRIT
>gnl|CDD|143496 cd06822, PLPDE_III_YBL036c_euk, Pyridoxal 5-phosphate (PLP)-binding TIM barrel domain of Type III PLP-Dependent Enzymes, Eukaryotic YBL036c-like proteins. This subfamily contains mostly uncharacterized eukaryotic proteins with similarity to the yeast hypothetical protein YBL036c, which is homologous to a Pseudomonas aeruginosa gene that is co-transcribed with a known proline biosynthetic gene. YBL036c is a single domain monomeric protein with a typical TIM barrel fold. It binds the PLP cofactor and has been shown to exhibit amino acid racemase activity. The YBL036c structure is similar to the N-terminal domain of the fold type III PLP-dependent enzymes, bacterial alanine racemase and eukaryotic ornithine decarboxylase, which are two-domain dimeric proteins. The lack of a second domain in YBL036c may explain limited D- to L-alanine racemase or non-specific racemase activity. Some members of this subfamily are also referred to as PROSC (Proline synthetase co-transcribed bacterial homolog)
LIANLKRIRQAVKRASKKLPASKPRLVAVSKTKPAELIKEAYDAGQRHFGENYVQELIEKAPDLPIDIKW
HFIGHLQSNKVKKLLKVPNLYMVETVDSEKLADKLNKAWEKLGEREPLKVMVQVNTSGEESKSGLEPSEA
VELVKHIIEECPNLKFSGLMTIGSFGYSLSSGPNPDFLCLVDCRKKVCEKLGINPDDLELSMGMSADFEH
AIEMGSTNVRVGSAIFG
>gnl|CDD|143497 cd06824, PLPDE_III_Yggs_like, Pyridoxal 5-phosphate (PLP)-binding TIM barrel domain of Type III PLP-Dependent Enzymes, Yggs-like proteins. This subfamily contains mainly uncharacterized proteobacterial proteins with similarity to the hypothetical Escherichia coli protein YggS, a homolog of yeast YBL036c, which is homologous to a Pseudomonas aeruginosa gene that is co-transcribed with a known proline biosynthetic gene. Like yeast YBL036c, Yggs is a single domain monomeric protein with a typical TIM-barrel fold. Its structure, which shows a covalently-bound PLP cofactor, is similar to the N-terminal domain of the fold type III PLP-dependent enzymes, bacterial alanine racemase and eukaryotic ornithine decarboxylase, which are two-domain dimeric proteins. YggS has not been characterized extensively and its biological function is still unkonwn
NIAENLAQVKQRIAQAAKQAGRDPSSVQLLAVSKTKPADAIREAYAAGQRHFGENYVQEALEKIEALRDL
QDIEWHFIGPIQSNKTKLIAENFDWVHSVDRLKIAKRLNDQRPAGLPPLNVCIQVNISGEDSKSGVAPED
AAELAEAISQLPNLRLRGLMAIPAPTDDEAAQRAAFKRLRQLFDQLKKQYPDLDTLSMGMSGDLEAAIAA
GSTMVRIGTAIFGA
>gnl|CDD|143498 cd06825, PLPDE_III_VanT, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins. This subfamily is composed of Enterococcus gallinarum VanT and similar proteins. VanT is a membrane-bound serine racemase (EC 5.1.1.18) that is essential for vancomycin resistance in Enterococcus gallinarum. It converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. The C-terminal region of this protein contains a PLP-binding TIM-barrel domain followed by beta-sandwich domain, which is homologous to the fold type III PLP-dependent enzyme, bacterial alanine racemase (AR). AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. On the basis of this similarity, it has been suggested that dimer formation of VanT is required for its catalytic activity, and that it catalyzes the racemization of serine in a mechanistically similar manner to that of alanine by bacterial AR. Some biochemical evidence indicates that VanT also exhibits alanine racemase activity and plays a role in the racemization of L-alanine. VanT contains a unique N-terminal transmembrane domain, which may function as an L-serine transporter. VanT serine racemases are not related to eukaryotic serine racemases, which are fold type II PLP-dependent enzymes
RAWLEIDLSALEHNVKEIKRLLPSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREA
GIKGEILILGYTPPVRAKELKKYSLTQTLISEAYAEELSKYAVNIKVHLKVDTGMHRLGESPEDIDSILA
IYRLKNLKVSGIFSHLCVSDSLDEDDIAFTKHQIACFDQVLADLKARGIEVGKIHIQSSYGILNYPDLKY
DYVRPGILLYGVLSDPNDPTKLGLDLRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYA
DGYPRSLSNQKAYVLINGKRAPIIGNICMDQLMVDVTDIPEVKEGDTATLIGQDGDEELSADEVARNAHT
ITNELLSRIGERVKRIYK
>gnl|CDD|143499 cd06826, PLPDE_III_AR2, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2. This subfamily is composed of bacterial alanine racemases (EC 5.1.1.1) with similarity to Yersinia pestis and Vibrio cholerae alanine racemase (AR) 2. ARs catalyze the interconversion between L- and D-alanine, an essential component of the peptidoglycan layer of bacterial cell walls. These proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity
NAWLEISTGAFENNIKLLKKLLGGNTKLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREA
GFTGKILRVRTATPSEIEDALAYNIEELIGSLDQAEQIDSLAKRHGKTLPVHLALNSGGMSRNGLELSTA
QGKEDAVAIATLPNLKIVGIMTHFPVEDEDDVRAKLARFNEDTAWLISNAKLKREKITLHAANSFATLNV
PEAHLDMVRPGGILYGDTPPSPEYKRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDG
YRRSFSNKAHVLINGQRVPVVGKVSMNTVMVDVTDIPGVKAGDEVVLFGKQGGAEITAAEIEEGSGTILA
ELYTLWGQTNPRVYV
>gnl|CDD|143500 cd06827, PLPDE_III_AR_proteobact, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases. This subfamily is composed mainly of proteobacterial alanine racemases (EC 5.1.1.1), fold type III PLP-dependent enzymes that catalyze the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. hese proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity
PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGIT
KPILLLEGFFSADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQ
RLKASPNVASIVLMTHFACADEPDSPGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIM
LYGASPFADKSGADLGLKPVMTLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPS
GTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKVGDPVELWGKGLPVDEVAAAAGTIGYELLCRLTPRVP
RVYV
>gnl|CDD|143501 cd06828, PLPDE_III_DapDC, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase. Diaminopimelate decarboxylase (DapDC, EC 4.1.1.20) participates in the last step of lysine biosynthesis. It converts meso-2,6-diaminoheptanedioate to L-lysine. It is a fold type III PLP-dependent enzyme that contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. DapDC exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity
YGTPLYVYDEATIRENYRRLKEAFSGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGF
PPERIVFTGNGKSDEELELALELGILRINVDSLSELERLGEIAPELGKGAPVALRVNPGVDAGTHPYIST
GGKDSKFGIPLEQALEAYRRAKELPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFL
DLGGGLGIPYRDEDEPLDIEEYAEAIAEALKELCEGGPDLKLIIEPGRYIVANAGVLLTRVGYVKETGGK
TFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEGETEKVDVVGPICESGDVFAKDRELPEVEEGDLLAIHD
AGAYGYSMSSNYNSRPRPAEVLV
>gnl|CDD|143502 cd06829, PLPDE_III_CANSDC, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase. Carboxynorspermidine decarboxylase (CANSDC) catalyzes the decarboxylation of carboxynorspermidine, the last step in the biosynthesis of norspermidine. It is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. Based on this similarity, CANSDC may require homodimer formation and the presence of the PLP cofactor for its catalytic activity
TPCYVLDEAKLRRNLEILKRVQERSGAKILLALKAFSMWSVFPLIREYLDGTTASSLFEARLGREEFGGE
VHTYSPAYRDDEIDEILRLADHIIFNSLSQLERFKDRAKAAGISVGLRINPEYSEVETDLYDPCAPGSRL
GVTLDELEEEDLDGIEGLHFHTLCEQDFDALERTLEAVEERFGEYLPQLKWLNLGGGHHITRPDYDVDRL
IALIKRFKEKYGVEVYLEPGEAVALNTGYLVATVLDIVENGMPIAILDASATAHMPDVLEMPYRPPIRGA
GEPGEGAHTYRLGGNSCLAGDVIGDYSFDEPLQVGDRLVFEDMAHYTMVKTNTFNGVRLPSIAIRD
>gnl|CDD|143503 cd06830, PLPDE_III_ADC, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase. This subfamily includes plants and biosynthetic prokaryotic arginine decarboxylases (ADC, EC 4.1.1.19). ADC is involved in the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. It catalyzes the decarboxylation of L-arginine to agmatine, which is then hydrolyzed to putrescine by agmatinase. ADC is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. Homodimer formation and the presence of both PLP and Mg2+ cofactors may be required for catalytic activity. Prokaryotic ADCs (biodegradative), which are fold type I PLP-dependent enzymes, are not included in this family
RGYGLPLLLRFPDILRHRIERLNAAFAKAIEEYGYKGKYQGVYPIKVNQQREVVEEIVKAGKRYNIGLEA
GSKPELLAALALLKTPDALIICNGYKDDEYIELALLARKLGHNVIIVIEKLSELDLILELAKKLGVKPLL
GVRIKLASKGSGKWQESGGDRSKFGLTASEILEVVEKLKEAGMLDRLKLLHFHIGSQITDIRRIKSALRE
AARIYAELRKLGANLRYLDIGGGLGVDYDGSRSSSDSSFNYSLEEYANDIVKTVKEICDEAGVPHPTIVT
ESGRAIVAHHSVLIFEVLGVKRLADWYFCNFSLFQSLPDSWAIDQLFPIMPLHRLNEKPTRRAVLGDITC
DSDGKIDSFIDPPDILPTLPLHPLRKDEPYYLGFFLVGAYQEILGDLHNLFGDTNAVHV
>gnl|CDD|143504 cd06831, PLPDE_III_ODC_like_AZI, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme Inhibitor. Antizyme inhibitor (AZI) is homologous to the fold type III PLP-dependent enzyme ODC but does not retain any decarboxylase activity. Like ODC, AZI is presumed to exist as a homodimer. Antizyme is a regulatory protein that binds directly to the ODC monomer to block its active site, leading to its degradation by the 26S proteasome. AZI binds to Antizyme with a higher affinity than ODC, preventing the formation of the Antizyme-ODC complex. Thus, AZI blocks the ability of Antizyme to promote ODC degradation, which leads to increased ODC enzymatic activity and polyamine levels. AZI also prevents the degradation of other proteins regulated by Antizyme, such as cyclin D1
DNYIYEHTLTGKNAFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEM
ALVQELGVSPENIIYTNPCKQASQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEE
MNMKFGTTLKNCRHLLECAKELDVQIVGVKFHVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIG
GGFTGSEIQLEEVNHVIRPLLDVYFPEGSGIQIIAEPGSYYVSSAFTLAVNVIAKKAVENDKHLSSVEKN
GSDEPAFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNV
GDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDWYEMQDAG
>gnl|CDD|143505 cd06836, PLPDE_III_ODC_DapDC_like_1, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with similarity to Ornithine and Diaminopimelate Decarboxylases. This subfamily contains uncharacterized proteins with similarity to ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases. Homodimer formation and the presence of the PLP cofactor may be required for catalytic activity
VHPAVGLYDLDGFRALVARLTAAFPAPVLHTFAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFP
PERIVFDSPAKTRAELREALELGVAINIDNFQELERIDALVAEFKEASSRIGLRVNPQVGAGKIGALSTA
TATSKFGVALEDGARDEIIDAFARRPWLNGLHVHVGSQGCELSLLAEGIRRVVDLAEEINRRVGRRQITR
IDIGGGLPVNFESEDITPTFADYAAALKAAVPELFDGRYQLVTEFGRSLLAKCGTIVSRVEYTKSSGGRR
IAITHAGAQVATRTAYAPDDWPLRVTVFDANGEPKTGPEVVTDVAGPCCFAGDVLAKERALPPLEPGDYV
AVHDTGAYYFSSHSSYNSLPRPAVYGVRT
>gnl|CDD|143506 cd06839, PLPDE_III_Btrk_like, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase. This subfamily is composed of Bacillus circulans BtrK decarboxylase and similar proteins. These proteins are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases, eukaryotic ornithine decarboxylases and diaminopimelate decarboxylases. BtrK is presumed to function as a PLP-dependent decarboxylase involved in the biosynthesis of the aminoglycoside antibiotic butirosin. Homodimer formation and the presence of the PLP cofactor may be required for catalytic activity
LADAYGTPFYVYDRDRVRERYAALRAALPPAIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALE
AGVPPEKILFAGPGKSDAELRRAIEAGIGTINVESLEELERIDALAEEHGVVARVALRINPDFELKGSGM
KMGGGPSQFGIDVEELPAVLARIAALPNLRFVGLHIYPGTQILDADALIEAFRQTLALALRLAEELGLPL
EFLDLGGGFGIPYFPGETPLDLEALGAALAALLAELGDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKVS
RGETFLVTDGGMHHHLAASGNFGQVLRRNYPLAILNRMGGEERETVTVVGPLCTPLDLLGRNVELPPLEP
GDLVAVLQSGAYGLSASPLAFLSHPAPAEVLV
>gnl|CDD|143507 cd06840, PLPDE_III_Bif_AspK_DapDC, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase/Diaminopimelate Decarboxylase. Bifunctional aspartate kinase/diaminopimelate decarboxylase (AspK/DapDC, EC 4.1.1.20/EC 2.7.2.4) typically exists in bacteria. These proteins contain an N-terminal AspK region and a C-terminal DapDC region, which contains a PLP-binding TIM-barrel domain followed by beta-sandwich domain, characteristic of fold type III PLP-dependent enzymes. Members of this subfamily have not been fully characterized. Based on their sequence, these proteins may catalyze both reactions catalyzed by AspK and DapDC. AspK catalyzes the phosphorylation of L-aspartate to produce 4-phospho-L-aspartate while DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine
RDALLRLAPDVGPCYVYDLETVRARARQVSALKAVDSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELD
LVLKLFPDLDPRRVLFTPNFAARSEYEQALELGVNVTVDNLHPLREWPELFRGREVILRIDPGQGEGHHK
HVRTGGPESKFGLDVDELDEARDLAKKAGIIVIGLHAHSGSGVEDTDHWARHGDYLASLARHFPAVRILN
VGGGLGIPEAPGGRPIDLDALDAALAAAKAAHPQYQLWMEPGRFIVAESGVLLARVTQIKHKDGVRFVGL
ETGMNSLIRPALYGAYHEIVNLSRLDEPPAGNADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYG
FCMASTYNLREPAEEVVL
>gnl|CDD|143508 cd06841, PLPDE_III_MccE_like, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE. This subfamily is composed of uncharacterized proteins with similarity to Escherichia coli MccE, a hypothetical protein that is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Most members of this subfamily share the same domain architecture as ODC and DapDC. A few members, including Escherichia coli MccE, contain an additional acetyltransferase domain at the C-terminus
LLESYGSPFFVFDEDALRENYRELLGAFKKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYEL
ALKLGVPGKRIIFNGPYKSKEELEKALEEGALINIDSFDELERILEIAKELGRVAKVGIRLNMNYGNNVW
SRFGFDIEENGEALAALKKIQESKNLSLVGLHCHVGSNILNPEAYSAAAKKLIELLDRLFGLELEYLDLG
GGFPAKTPLSLAYPQEDTVPDPEDYAEAIASTLKEYYANKENKPKLILEPGRALVDDAGYLLGRVVAVKN
RYGRNIAVTDAGINNIPTIFWYHHPILVLRPGKEDPTSKNYDVYGFNCMESDVLFPNVPLPPLNVGDILA
IRNVGAYNMTQSNQFIRPRPAVYLIDNNG
>gnl|CDD|143509 cd06842, PLPDE_III_Y4yA_like, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA. This subfamily is composed of the hypothetical Rhizobium sp. protein Y4yA and similar uncharacterized bacterial proteins. These proteins are homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases
LVALVEAYGSPLNVLFPQTFRENIAALRAVLDRHGVDGRVYFARKANKSLALVRAAAAAGIGVDVASLAE
LRQALAAGVRGDRIVATGPAKTDEFLWLAVRHGATIAVDSLDELDRLLALARGYTTGPARVLLRLSPFPA
SLPSRFGMPAAEVRTALERLAQLRERVRLVGFHFHLDGYSAAQRVAALQECLPLIDRARALGLAPRFIDI
GGGFPVSYLADAAEWEAFLAALTEALYGYGRPLTWRNEGGTLRGPDDFYPYGQPLVAADWLRAILSAPLP
QGRTIAERLRDNGITLALEPGRALLDQCGLTVARVAFVKQLGDGNHLIGLEGNSFSACEFSSEFLVDPLL
IPAPEPTTDGAPIEAYLAGASCLESDLITRRKIPFPRLPKPGDLLVFPNTAGYQMDFLESRFHRHPLPRR
VVV
>gnl|CDD|143510 cd06843, PLPDE_III_PvsE_like, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE. This subfamily is composed of PvsE from Vibrio parahaemolyticus and similar proteins. PvsE is a vibrioferrin biosynthesis protein which is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. It has been suggested that PvsE may be involved in the biosynthesis of the polycarboxylate siderophore vibrioferrin. It may catalyze the decarboxylation of serine to yield ethanolamine. PvsE may require homodimer formation and the presence of the PLP cofactor for activity
PLCAYVYDLAALRAHARALRASLPPGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPDA
PLIFGGPGKTDSELAQALAQGVERIHVESELELRRLNAVARRAGRTAPVLLRVNLALPDLPSSTLTMGGQ
PTPFGIDEADLPDALELLRDLPNIRLRGFHFHLMSHNLDAAAHLALVKAYLETARQWAAEHGLDLDVVNV
GGGIGVNYADPEEQFDWAGFCEGLDQLLAEYEPGLTLRFECGRYISAYCGYYVTEVLDLKRSHGEWFAVL
RGGTHHFRLPAAWGHNHPFSVLPVEEWPYPWPRPSVRDTPVTLVGQLCTPKDVLARDVPVDRLRAGDLVV
FPLAGAYGWNISHHDFLMHPHPERIYL
>gnl|CDD|132911 cd06844, STAS, Sulphate Transporter and Anti-Sigma factor antagonist domain found in the C-terminal region of sulphate transporters as well as in bacterial and archaeal proteins involved in the regulation of sigma factors. The STAS (Sulphate Transporter and Anti-Sigma factor antagonist) domain is found in the C-terminal region of sulphate transporters as well as in bacterial and archaeal proteins involved in the regulation of sigma factors, like anti-anti-sigma factors and "stressosome" components. The sigma factor regulators are involved in protein-protein interaction which is regulated by phosphorylation
VPLEKVDDYWVVRLEGELDHHSVEQFKEELLHNITNVAGKTIVIDISALEFMDSSGTGVLLERSRLAEAV
GGQFVLTGISPAVRITLTESGLDKGXATAL
>gnl|CDD|132900 cd06845, Bcl-2_like, Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This alignment model spans what have been described as Bcl-2 homology regions BH1, BH2, BH3, and BH4. Many members of this family have an additional C-terminal transmembrane segment. Some homologous proteins, which are not included in this model, may miss either the BH4 (Bax, Bak) or the BH2 (Bcl-X(S)) region, and some appear to only share the BH3 region (Bik, Bim, Bad, Bid, Egl-1). This family is involved in the regulation of the outer mitochondrial membrane's permeability and in promoting or preventing the release of apoptogenic factors, which in turn may trigger apoptosis by activating caspases. Bcl-2 and the closely related Bcl-X(L) are anti-apoptotic key regulators of programmed cell death. They are assumed to function via heterodimeric protein-protein interactions, binding pro-apoptotic proteins such as Bad (BCL2-antagonist of cell death), Bid, and Bim, by specifically interacting with their BH3 regions. Interfering with this heterodimeric interaction via small-molecule inhibitors may prove effective in targeting various cancers. This family also includes the Caenorhabditis elegans Bcl-2 homolog CED-9, which binds to CED-4, the C. Elegans homolog of mammalian Apaf-1. Apaf-1, however, does not seem to be inhibited by Bcl-2 directly
DEITRRLARDYLRYRLGEPETPNSPLPSGSPPSEVAETLRRVGDELEEKHRRLFENMCRQLNISPDNAYE
VFQEVARELFEDGGINWGRIVALFAFGGRLAVKCVEQGLPELVRSIAEWTSDFLEENLADWIQENGGWDG
FVEF
>gnl|CDD|185704 cd06846, Adenylation_DNA_ligase_like, Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases. ATP-dependent polynucleotide ligases catalyze the phosphodiester bond formation of nicked nucleic acid substrates using ATP as a cofactor in a three step reaction mechanism. This family includes ATP-dependent DNA and RNA ligases. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent DNA ligases have a highly modular architecture, consisting of a unique arrangement of two or more discrete domains, including a DNA-binding domain, an adenylation or nucleotidyltransferase (NTase) domain, and an oligonucleotide/oligosaccharide binding (OB)-fold domain. The adenylation domain binds ATP and contains many active site residues. Together with the C-terminal OB-fold domain, it comprises a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases including eukaryotic GRP-dependent mRNA-capping enzymes. The catalytic core contains both the active site as well as many DNA-binding residues. The RNA circularization protein from archaea and bacteria contains the minimal catalytic unit, the adenylation domain, but does not contain an OB-fold domain. This family also includes the m3G-cap binding domain of snurportin, a nuclear import adaptor that binds m3G-capped spliceosomal U small nucleoproteins (snRNPs), but doesn't have enzymatic activity
PQLLNPILEEALSEYDEQDEYYVQEKYDGKRALIVALNGGVFAISRTGLEVPLPSILIPGRELLTLKPGF
ILDGELVVENREVANPKPTYYAFDVVPLSGVGLRDLPYSDRFAYLKSLLKEFEGLDPVKLVPLENAPSYD
ETLDDLLEKLKKKGKEGLVFKHPDAPYKGRPGSSGNQLKLKP
>gnl|CDD|467022 cd06847, HFD_SUPT7L, histone-fold domain found in Suppressor of Ty 7-like (SUPT7L) and similar proteins. SUPT7L, also called STAGA complex 65 subunit gamma, adenocarcinoma antigen ART1, SPTF-associated factor 65 gamma, or STAF65gamma, is the ortholog of yeast SPT7 in mammalian cells. It is highly similar to yeast SPT7 but lacks the N-terminal SPT7 bromodomain. SUPT7L is a protein component specific to STAGA (SPT3-TAF9-GCN5 Acetyltransferase)-type complexes. It plays an essential role for the integrity of the STAGA complex
DEESVRQLLRKSVAAILAHAGFDSASESALEVLTDVLDEFLRKFTRLLRSAVDREALSGETGFPDILERV
LHEMGIGGISSLHEYY
>gnl|CDD|133457 cd06848, GCS_H, Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue
YTKDHEWVKVEGDGIATVGITDYAQDLLGDIVFVELPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVV
EVNEALLDNPELINSDPYGEGWLVKI
>gnl|CDD|133458 cd06849, lipoyl_domain, Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue
TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQV
IAVI
>gnl|CDD|133459 cd06850, biotinyl_domain, The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine
EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI
>gnl|CDD|133461 cd06851, GT_GPT_like, This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and archaeal GPT-like glycosyltransferases. Eukaryotic GPT catalyzes the transfer of GlcNAc-1-P from UDP-GlcNAc to dolichol-P to form GlcNAc-P-P-dolichol. The reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for eukaryotic N-linked glycosylation. GPT activity has been identified in all eukaryotic cells examined to date. Evidence for the existence of the N-glycosylation pathway in archaea has emerged and genes responsible for the pathway have been identified. A glycosyl transferase gene Mv1751 in M. voltae encodes for the enzyme that carries out the first step in the pathway, the attachment of GlcNAc to a dolichol lipid carrier in the membrane. A lethal mutation in the alg7 (GPT) gene in Saccharomyces cerevisiae was successfully complemented with Mv1751, the archaeal gene, indicating eukaryotic and archaeal enzymes may use the same substrates and are evolutionarily closer than the bacterial enzyme, which uses a different substrate
TGKDMNKKGNVMIPEPGGISILIGFVASEITLIFFPFLSFPHFPISEILAALITSVLGFSVGIIDDRLTM
GGWFKPVALAFAAAPILLLGAYDSNLDFPLFGGSVKIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFT
TIISFALAISLLVQQNYEIGIACLCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAILGEVEKIA
AVAFIPAIINFFL
>gnl|CDD|133462 cd06852, GT_MraY, Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the formation of the first lipid intermediate in the synthesis of bacterial cell wall peptidoglycan. It catalyzes the formation of undecaprenyl-pyrophosphoryl-N-acetylmuramoyl-pentapeptide from UDP-MurNAc-pentapeptide and undecaprenyl-phosphate. It is an integral membrane protein with possibly ten transmembrane domains
GPKSHLKKAGTPTMGGILFILAILISTLLWADLDSPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSA
RQKLLLQFLIAIVFALLLYYFNGSGTLITLPFFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAA
GVSIIVALALAIIAYLAGNAVFLAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQ
ELLLLIIGGVFVIEALSVILQVGSFKLTGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL
>gnl|CDD|133463 cd06853, GT_WecA_like, This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. WecA is an UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate (Und-P) GlcNAc-1-phosphate transferase that catalyzes the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate molecule and N-acetylglucosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylglucosamine precursor. WecA participates in the biosynthesis of O antigen LPS in many enteric bacteria and is also involved in the biosynthesis of enterobacterial common antigen. A conserved short sequence motif and a conserved arginine at a cytosolic loop of this integral membrane protein were shown to be critical in recognition of substrate UDP-N-acetylglucosamine
RKVHKGPIPRLGGLAIFLGFLLALLLALLFPFFLLPELLGLLAGATIIVLLGLLDDLFDLSPKVKLLGQI
LAALIVVFGGGVILSLLGPFGGGIILLGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAIL
ALLNGQVLVALLALALAGALLGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGTQKSSTAISPVVPLLI
LAVPLFDTLFVIIRRLLRGRSPFQADRDHLHHRLLRLGL
>gnl|CDD|133464 cd06854, GT_WbpL_WbcO_like, The members of this subfamily catalyze the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate (Und-P) molecule and N-acetylhexosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylhexosamine precursor. The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic end products implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The subgroup of bacterial UDP-HexNAc:polyprenol-P HexNAc-1-P transferases includes the WbcO protein from Yersinia enterocolitica and the WbpL protein from Pseudomonas aeruginosa. These transferases initiate LPS O-antigen biosynthesis. Similar to other GlcNAc/MurNAc-1-P transferase family members, WbpL is a highly hydrophobic protein possessing 11 predicted transmembrane segments
LLDIPNERSSHTKPTPRGGGIAFVLAFLLALLLAAAAGPLNDLSYLLLLIGLLLLAAVGFIDDLRSLSPK
IRLLVQLLAAALALYALGPLTSLLLNFLPPWLIALLLLLAIVWIINLYNFMDGIDGLAGGEALVVFLALA
LLGYLAGEPALALLALALAGALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLLALSGQSPWAWLLLL
SPFLVDATVTLLRRLLRGENIFQAHRKHLYQRLARAGKSHRKV
>gnl|CDD|133465 cd06855, GT_GPT_euk, UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from UDP-GlcNAc to dolichol-P to form GlcNAc-P-P-dolichol. The reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for eukaryotic N-glycosylation. GPT activity has been identified in all eukaryotic cells examined to date. A series of six conserved motifs designated A through F, ranging in length from 5 to 13 amino acid residues, has been identified in this family. They have been determined to be important for stable expression, substrate binding, or catalytic activities
IPKFGPLFIKAGLYGIDLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFLKDFPHDKLVEYLSALLSIC
CMTFLGFADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVPLRPLLGTLIDLGILYYVYMILLAV
FCTNSINIYAGINGLEVGQSLVIALSILLYNLLELNGSSGSMTLDAHLFSLYLLLPFIAVSLALLYYNWY
PSKVFVGDTFTYFAGMVFAVVGILGHFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLL
EPS
>gnl|CDD|133466 cd06856, GT_GPT_archaea, UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT catalyzes the transfer of GlcNAc-1-P from UDP-GlcNAc to dolichol-P to form GlcNAc-P-P-dolichol. The reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for eukaryotic N-linked glycosylation. Evidence for the existence of the N-glycosylation pathway in archaea has emerged and genes responsible for the pathway have been identified. A glycosyl transferase gene Mv1751 in M. voltae encodes for the enzyme that carries out the first step in the pathway, the attachment of GlcNAc to a dolichol lipid carrier in the membrane. A lethal mutation in the alg7 (GPT) gene in Saccharomyces cerevisiae was successfully complemented with Mv1751, the archaea gene, indicating that eukaryotic and archaeal enzymes may use the same substrates and are evolutionarily closer than the bacterial enzyme, which uses a different substrate
VGRDVHKPGKPEVPEMGGIAVLLGFSLGLLFLSALTHSVEALALLITSLLAGLIGLLDDILGLSQSEKVL
LTALPAIPLLVLKAGNPLTSLPIGGRVLGILYYLLIVPLGITGASNAFNMLAGFNGLEAGMGIIILLALA
IILLINGDYDALIIALILVAALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLLPYV
IDFLLKLRSKGGGKEHREKPTKVLEDGTLYPPPDKSSLLTLRLLLRKGPMTEKEVVLVLWALEALLGILA
>gnl|CDD|271356 cd06857, SLC5-6-like_sbd, Solute carrier families 5 and 6-like; solute binding domain. This superfamily includes the solute-binding domain of SLC5 proteins (also called the sodium/glucose cotransporters or solute sodium symporters), SLC6 proteins (also called the sodium- and chloride-dependent neurotransmitter transporters or Na+/Cl--dependent transporters), and nucleobase-cation-symport-1 (NCS1) transporters. SLC5s co-transport Na+ with sugars, amino acids, inorganic ions or vitamins. SLC6s include Na+/Cl--dependent plasma membrane transporters for the monoamine neurotransmitters serotonin, dopamine, and norepinephrine, and the amino acid neurotransmitters GABA and glycine. NCS1s are essential components of salvage pathways for nucleobases and related metabolites; their known substrates include allantoin, uracil, thiamine, and nicotinamide riboside. Members of this superfamily are important in human physiology and disease. They contain a functional core of 10 transmembrane helices (TMs): an inverted structural repeat, TMs1-5 and TMs6-10; TMs numbered to conform to the SLC6 Aquifex aeolicus LeuT
FDLILACIGLALGLANFIRFPQMTYSYGGAFILPYIVLSIIVGIPLLVLELSMGQFSGIGFISMWRCSPF
FKGLGVVSLFLSFLLLIYYTYLAALALVYIINLYYWILALGLFLIWVTIYGIFFRGLKSIGKLIVIAVIV
LLVLLLVLTVRALFLEGAGASEGLNKGGTPDFMELNNSGIWTAATIQVFFSLGAGWGSVITIASFCLFKK
NAQRDALIAAFLNLIASIIFVGLIGIAAGVLSFDPQNMVVLGLLNSLYLTFIASPQAISSLAGSNLWAFL
YYAALLLAGLSSMATITNTVAQSLFDEFRRKLKTGVIDTALIVVLLVAAVIFLVLGLRILFLTDKQLVGT
SVVPLLLILLLVVFWIYGRERIQRDIEFMLGPVGSIVWFWLWVIAPAILVIILVWAA
>gnl|CDD|132769 cd06859, PX_SNX1_2_like, The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex
FEISVTDPVKVGDGMSAYVVYRVTTKTNLPDFKKSEFSVLRRYSDFLWLYERLVEKYPGRIVPPPPEKQA
VGRFKVKFEFIEKRRAALERFLRRIAAHPVLRKDPDFRLFLESD
>gnl|CDD|132770 cd06860, PX_SNX7_30_like, The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. This subfamily consists of SNX7, SNX30, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of the sorting nexins in this subfamily has yet to be elucidated
LFITVDNPEKHVTTLETYITYRVTTKTTRSEFDSSEYSVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHS
VKGLLDRFSPEFVATRMRALHKFLNRIVEHPVLSFNEHLKVFLTAK
>gnl|CDD|132771 cd06861, PX_Vps5p, The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. The PX domain of Vps5p binds phosphatidylinositol-3-phosphate (PI3P). Similar to SNX1, Vps5p contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1
FEITVGDPHKVGDLTSAHTVYTVRTRTTSPNFEVSSFSVLRRYRDFRWLYRQLQNNHPGVIVPPPPEKQS
VGRFDDNFVEQRRAALEKMLRKIANHPVLQKDPDFRLFLESE
>gnl|CDD|132772 cd06862, PX_SNX9_18_like, The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX9, SNX18, and similar proteins. They contain an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1
YHCTVTNPKKESKFKGLKSFIAYQITPTHTNVTVSRRYKHFDWLYERLVEKYSCIAIPPLPEKQVTGRFE
EDFIEKRRERLELWMNRLARHPVLSQSEVFRHFLTCTDEKDWKSGKRKAEKDELV
>gnl|CDD|132773 cd06863, PX_Atg24p, The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation protein. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The yeast Atg24p is a sorting nexin (SNX) which is involved in membrane fusion events at the vacuolar surface during pexophagy. This is facilitated via binding of Atg24p to phosphatidylinositol 3-phosphate (PI3P) through its PX domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway
LECLVSDPQKELDGSSDTYISYLITTKTNLPSFSRKEFKVRRRYSDFVFLHECLSNDFPACVVPPLPDKH
RLEYITGDRFSPEFITRRAQSLQRFLRRISLHPVLSQSKILHQFLESS
>gnl|CDD|132774 cd06864, PX_SNX4, The phosphoinositide binding Phox Homology domain of Sorting Nexin 4. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It shows a similar domain architecture as SNX1-2, among others, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. SNX4 is implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and the long form of the leptin receptor
MEITVTEAEKRTGGSAMNLKETYTVYLIETKIVEHESEEGLSKKLSSLWRRYSEFELLRNYLVVTYPYVI
VPPLPEKRAMFMWQKLSSDTFDPDFVERRRAGLENFLLRVAGHPELCQDKIFLEFLTHE
>gnl|CDD|132775 cd06865, PX_SNX_like, The phosphoinositide binding Phox Homology domain of SNX-like proteins. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. This subfamily is composed of uncharacterized proteins, predominantly from plants, with similarity to sorting nexins. A few members show a similar domain architecture as a subfamily of sorting nexins, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit is known to determine specific membrane localization
KITVSDPKKEQEPSRVPLGGPPYISYKVTTRTNIPSYTHGEFTVRRRFRDVVALADRLAEAYRGAFVPPR
PDKSVVESQVMQSAEFIEQRRVALEKYLNRLAAHPVIGLSDELRVFLTLQ
>gnl|CDD|132776 cd06866, PX_SNX8_Mvp1p_like, The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles
DTVTVELVPEKKGLFLKHVEYEVSSKRFKSTVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGSADRE
FLEARRRGLSRFLNLVARHPVLSEDELVRTFLTEP
>gnl|CDD|132777 cd06867, PX_SNX41_42, The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX41 and SNX42 (also called Atg20p) form dimers with SNX4, and are required in protein recycling from the sorting endosome (post-Golgi endosome) back to the late Golgi in yeast
PIQIVDAGKSSEGGSGSYIVYVIRLGGSEVKRRYSEFESLRKNLTRLYPTLIIPPIPEKHSLKDYAKKPS
KAKNDAKIIERRKRMLQRFLNRCLQHPILRNDIVFQKFLDPN
>gnl|CDD|132778 cd06868, PX_HS1BP3, The phosphoinositide binding Phox Homology domain of HS1BP3. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Hematopoietic lineage cell-specific protein-1 (HS1) binding protein 3 (HS1BP3) associates with HS1 proteins through their SH3 domains, suggesting a role in mediating signaling. It has been reported that HS1BP3 might affect the IL-2 signaling pathway in hematopoietic lineage cells. Mutations in HS1BP3 may also be associated with familial Parkinson disease and essential tremor. HS1BP3 contains a PX domain, a leucine zipper, motifs similar to immunoreceptor tyrosine-based inhibitory motif and proline-rich regions. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes
GLDLTVPEYQEIRGKTSSGHVLYQIVVVTRLAAFKSAKHKEEDVVQFMVSKKYSEFEELYKKLSEKYPGT
ILPPLPRKALFVSESDIRERRAAFNDFMRFISKDEKLANCPELLEFLGVK
>gnl|CDD|132779 cd06869, PX_UP2_fungi, The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins. The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction
NGWDINVVAVRVTETAGRLSSKKAYFVNRSKHHYEFIIRVRREGEEYRTIYVARRYSDFKKLHHDLKKEF
PGKKLPKLPHKDKLPREKLRLSLRQYLRSLLKDPEVAHSSILQEFLTSD
>gnl|CDD|132780 cd06870, PX_CISK, The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity
SCPSVSIPSSDEDREKKKRFTVYKVVVSVGRSSWFVFRRYAEFDKLYESLKKQFPASNLKIPGKRLFGNN
FDPDFIKQRRAGLDEFIQRLVSDPKLLNHPDVRAFLQMD
>gnl|CDD|132781 cd06871, PX_MONaKA, The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. MONaKA (Modulator of Na,K-ATPase) binds the plasma membrane ion transporter, Na,K-ATPase, and modulates its enzymatic and ion pump activities. It modulates brain Na,K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes
LLDDTVPLTCVIEASQNIQSHTEYIIRVQRGPSPENSWQVIRRYNDFDLLNASLQISGISLPLPPKKLIG
NMDREFIAERQQGLQNYLNVILMNPILASCLPVKKFLDPNNYSANFTEIA
>gnl|CDD|132782 cd06872, PX_SNX19_like_plant, The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins. The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized plant proteins containing an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some sorting nexins (SNXs). This is the same domain architecture found in SNX19. SNX13 and SNX14 also contain these three domains but also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction
LSCRVLGAEIVKSGSKSFAVYSVAVTDNENETWVVKRRFRNFETLHRRLKEVPKYNLELPPKRFLSSSLD
GAFIEERCKLLDKYLKDLLVIEKVAESHEVWSFLSAR
>gnl|CDD|132783 cd06873, PX_SNX13, The phosphoinositide binding Phox Homology domain of Sorting Nexin 13. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome
DKFKLTAVIINTGIVKEHGKTYAVYAISVTRIYPNGQEESWHVYRRYSDFHDLHMRLKEKFPNLSKLSFP
GKKTFNNLDRAFLEKRRKMLNQYLQSLLNPEVLDANPGLQEIVLDFLEPG
>gnl|CDD|132784 cd06874, PX_KIF16B_SNX23, The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway
IKITIPRYVLRGQGKDEHFEFEVKITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKS
ERVAKERRRQLETYLRNFFSVCLKLPACPLYPKVGRTLSKATLCDFSPFFRKGVFEN
>gnl|CDD|132785 cd06875, PX_IRAS, The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected. The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway
EPETKIRIPSAETVEGYTVYIIEVKVGSVEWTVKHRYSDFAELHDKLVAEHKVDKDLLPPKKLIGNKSPS
FVEKRRKELEIYLQTLLSFFQKTMPRELAHFLDFHKYEIIGLTQNL
>gnl|CDD|132786 cd06876, PX_MDM1p, The phosphoinositide binding Phox Homology domain of yeast MDM1p. The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway
ELQRQQYMVQENDNSLYGRTRVSIQSYISDVEEEGKEFVVYLIEVQRLNNDDQSSGWVVARRYSEFLELH
KYLKKRYPGVLKLDFPQKRKISLKYSKTLLVEERRKALEKYLQELLKIPEVCEDEEFRKFLSQ
>gnl|CDD|132787 cd06877, PX_SNX14, The phosphoinositide binding Phox Homology domain of Sorting Nexin 14. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs
SAWRVSIPYVEMRRDPSNGERIYVFCIEVERNDRRAKGHEPQHWSVLRRYNEFYVLESKLTEFHGEFPDA
PLPSRRIFGPKSYEFLESKREIFEEFLQKLLQKPELRGSELLYDFLSPN
>gnl|CDD|132788 cd06878, PX_SNX25, The phosphoinositide binding Phox Homology domain of Sorting Nexin 25. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs
RWCEHLGKWRANIQSAEVTVEDDKEVPLYVIVVHVSEVGLNEDESISSGWVVTRKLSEFHDLHRKLKECS
SWLKKVELPSLSKKWFKSIDKKFLDKSKNQLQKYLQFILEDETLCQSEALYSFLSPS
>gnl|CDD|132789 cd06879, PX_UP1_plant, The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins. The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction
YCVFIPSWVVLPKSKESDGKAINPKVGNMSVVYSEYQPLNNAVDKFYRVQVGVQSPEGITTMRGVLRRFN
DFLKLHTDLKKLFPKKKLPAAPPKGLLRMKNRALLEERRHSLEEWMGKLLSDIDLSRSVPVASFLELE
>gnl|CDD|132790 cd06880, PX_SNX22, The phosphoinositide binding Phox Homology domain of Sorting Nexin 22. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known
IEVSIPSYRLEVDESEKPYTVFTIEVLVNGRRHTVEKRYSEFHALHKKLKKSIKTPDFPPKRVRNWNPKV
LEQRRQGLEAYLQGLLKINELPKQLLDFLGVRHFPSLPKS
>gnl|CDD|132791 cd06881, PX_SNX15_like, The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily have similarity to sorting nexin 15 (SNX15), which contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein. Other members of this subfamily contain an additional C-terminal kinase domain, similar to human RPK118, which binds sphingosine kinase and the antioxidant peroxiredoxin-3 (PRDX3). RPK118 may be involved in the transport of proteins such as PRDX3 from the cytoplasm to its site of function in the mitochondria
WSRSFTVTDTRRHKKGYTEYKITSKVFSRSVPEDVSEVVVWKRYSDFKKLHRELSRLHKQLYLSGSFPPF
PKGKYFGRFDAAVIEERRQAILELLDFVGNHPALYQSSAFQQFFEEA
>gnl|CDD|132792 cd06882, PX_p40phox, The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase. The PX domain is a phosphoinositide binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p40phox contains an N-terminal PX domain, a central SH3 domain that binds p47phox, and a C-terminal PB1 domain that interacts with p67phox. It is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. The PX domain is a phospholipid-binding module involved in the membrane targeting of proteins. The p40phox PX domain binds to PI3P, an abundant lipid in phagosomal membranes, playing an important role in the localization of NADPH oxidase. The PX domain of p40phox is also involved in protein-protein interaction
DVAVSATIADIEEKRGFTNYYVFVIEVKTKGGSKYLIYRRYRQFFALQSKLEERFGPEAGSSAYDCTLPT
LPGKIYVGRKAEIAERRIPLLNRYMKELLSLPVWVLMDEDVRLFFYQTESDSE
>gnl|CDD|132793 cd06883, PX_PI3K_C2, The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are also involved in the regulation of clathrin-mediated membrane trafficking as well as ATP-dependent priming of neurosecretory granule exocytosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. Class II PI3Ks include three vertebrate isoforms (alpha, beta, and gamma), the Drosophila PI3K_68D, and similar proteins
EVSVFGFQKRYSPEKYYIYVVKVTRENQTEPSFVFRTFEEFQELHNKLSLLFPSLKLPSFPARVVLGRSH
IKQVAERRKIELNSYLKSLFNASPEVAESDLVYTFFHPL
>gnl|CDD|132794 cd06884, PX_PI3K_C2_68D, The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases similar to the Drosophila PI3K_68D protein. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. PI3K_68D is a novel PI3K which is widely expressed throughout the Drosophila life cycle. In vitro, it has been shown to phosphorylate PI and PI4P. It is involved in signaling pathways that affect pattern formation of Drosophila wings
IVRVTVVGFQKRYDPEKYYVYVVEVTRENQASPQHVFRTYKEFLELYQKLCRKFPLAKLHPLSTGSHVGR
SNIKSVAEKRKQDIQQFLNSLFKMAEEVSHSDLVYTFFHPL
>gnl|CDD|132795 cd06885, PX_SNX17_31, The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Members of this subfamily include sorting nexin 17 (SNX17), SNX31, and similar proteins. They contain an N-terminal PX domain followed by a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX17 is known to regulate the trafficking and processing of a number of proteins. It binds some members of the low-density lipoprotein receptor (LDLR) family such as LDLR, VLDLR, ApoER2, and others, regulating their endocytosis. It also binds P-selectin and may regulate its lysosomal degradation. SNX17 is highly expressed in neurons. It binds amyloid precursor protein (APP) and may be involved in its intracellular trafficking and processing to amyloid beta peptide, which plays a central role in the pathogenesis of Alzheimer's disease. The biological function of SNX31 is unknown
HFSIPDTQELSDEGGSTYVAYNIHINGVLHCSVRYSQLHGLNEQLKKEFGNRKLPPFPPKKLLPLTPAQL
EERRLQLEKYLQAVVQDPRIANSDIFNSFLLNAQ
>gnl|CDD|132796 cd06886, PX_SNX27, The phosphoinositide binding Phox Homology domain of Sorting Nexin 27. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX27 contains an N-terminal PDZ domain followed by a PX domain and a Ras-Associated (RA) domain. It binds G protein-gated potassium (Kir3) channels, which play a role in neuronal excitability control, through its PDZ domain. SNX27 downregulates Kir3 channels by promoting their movement in the endosome, reducing surface expression and increasing degradation. SNX27 also associates with 5-hydroxytryptamine type 4 receptor (5-HT4R), cytohesin associated scaffolding protein (CASP), and diacylglycerol kinase zeta, and may play a role in their intracellular trafficking and endocytic recycling. The SNX27 PX domain preferentially binds to phosphatidylinositol-3-phosphate (PI3P) and is important for targeting to the early endosome
KRSVPISIPDYKHVEQNGEKFVVYNIYMAGRQLCSRRYREFANLHQNLKKEFPDFQFPKLPGKWPFSLSE
QQLDARRRGLEQYLEKVCSIRVIGESDIMQDFLSDE
>gnl|CDD|132797 cd06887, PX_p47phox, The phosphoinositide binding Phox Homology domain of the p47phox subunit of NADPH oxidase. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p47phox is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox), which plays a key role in the ability of phagocytes to defend against bacterial infections. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p47phox is required for activation of NADH oxidase and plays a role in translocation. It contains an N-terminal PX domain, two Src Homology 3 (SH3) domains, and a C-terminal domain that contains PxxP motifs for binding SH3 domains. The PX domain of p47phox is unique in that it contains two distinct basic pockets on the membrane-binding surface: one preferentially binds phosphatidylinositol-3,4-bisphosphate [PI(3,4)P2] and is analogous to the PI3P-binding pocket of p40phox, while the other binds anionic phospholipids such as phosphatidic acid or phosphatidylserine. Simultaneous binding in the two pockets results in increased membrane affinity. The PX domain of p47phox is also involved in protein-protein interaction
IRHIALLGFEKRFVPSQHYVYMFLVKWQDLSEKLVYRRFTEIYEFHKTLKEMFPIEAGDINKENRIIPHL
PAPKWFDGQRAAENRQGTLTEYCSTLLSLPPKISRCPHVLDFFKVRPD
>gnl|CDD|132798 cd06888, PX_FISH, The phosphoinositide binding Phox Homology domain of Five SH protein. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Five SH (FISH), also called Tks5, is a scaffolding protein and Src substrate that is localized in podosomes, which are electron-dense structures found in Src-transformed fibroblasts, osteoclasts, macrophages, and some invasive cancer cells. FISH contains an N-terminal PX domain and five Src homology 3 (SH3) domains. FISH binds and regulates some members of the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. It is required for podosome formation, degradation of the extracellular matrix, and cancer cell invasion. This subfamily also includes proteins with a different number of SH3 domains than FISH, such as Tks4, which contains four SH3 domains instead of five. The Tks4 adaptor protein is required for the formation of functional podosomes. It has overlapping, but not identical, functions as FISH. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction
VKDVKVIDVEKRRAPSKHYVYIINVTWSDGSSNVIYRRYSKFFDLQMQLLDKFPIEGGQKDPSQRIIPFL
PGKILFRRSHIRDVAVKRLKPIDEYCKALVRLPPHISQCDEVLRFFEAK
>gnl|CDD|132799 cd06889, PX_NoxO1, The phosphoinositide binding Phox Homology domain of Nox Organizing protein 1. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Nox Organizing protein 1 (NoxO1) is a critical regulator of enzyme kinetics of the nonphagocytic NADPH oxidase Nox1, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Nox1 is expressed in colon, stomach, uterus, prostate, and vascular smooth muscle cells. NoxO1, a homolog of the p47phox subunit of phagocytic NADPH oxidase, is involved in targeting activator subunits (such as NoxA1) to Nox1. It is co-localized with Nox1 in the membranes of resting cells and directs the subcellular localization of Nox1. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of NoxO1 preferentially binds phosphatidylinositol-3,5-bisphosphate [PI(3,5)P2], PI5P, and PI4P
SPRHPVDVQGVGVMQKRRHKTYMFSVLWSDGSELFVYRSLEEFRKLHKQLKEKFPVEAGLLRSSDRVLPK
FKDAPSLGSLKGSTSRSLARLKLLETYCQELLRLDEKVSRSPEVIQFFAPQ
>gnl|CDD|132800 cd06890, PX_Bem1p, The phosphoinositide binding Phox Homology domain of Bem1p. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily bear similarity to Saccharomyces cerevisiae Bem1p, containing two Src Homology 3 (SH3) domains at the N-terminus, a central PX domain, and a C-terminal PB1 domain. Bem1p is a scaffolding protein that is critical for proper Cdc42p activation during bud formation in yeast. During budding and mating, Bem1p migrates to the plasma membrane where it can serve as an adaptor for Cdc42p and some other proteins. Bem1p also functions as an effector of the G1 cyclin Cln3p and the cyclin-dependent kinase Cdc28p in promoting vacuolar fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of Bem1p specifically binds phosphatidylinositol-4-phosphate (PI4P)
VSASVESVLLEDNRYWYRVRATLSDGKTRYLCRYYQDFYKLHIALLDLFPAEAGRNSSKRILPYLPGPVT
DVVNDSISLKRLNDLNEYLNELINLPAYIQTSEVVRDFFANR
>gnl|CDD|132801 cd06891, PX_Vps17p, The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps17p. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Vsp17p forms a dimer with Vps5p, the yeast counterpart of human SNX1, and is part of the retromer complex that mediates the transport of the carboxypeptidase Y receptor Vps10p from endosomes to Golgi. Similar to Vps5p and SNX1, Vps17p harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit helps determine specific membrane localization
EQPSQPESRKILTSNRRELEPERKKPKYFLRVRVTGIERNKSKDPIIRFDVTTNLPTFRSSTYKDVRRTY
EEFQKLFKYLNGANPETFVPALPLPSTSYGSNNEEDARKLKANLQRWFNRVCSDPILIRDEELRFFIESD
>gnl|CDD|132802 cd06892, PX_SNX5_like, The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Members of this subfamily include SNX5, SNX6, and similar proteins. They contain a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p
SSLQVDISDALSERDKVKFTVHTKTTLPTFQKPEFSVTRQHEEFVWLHDTLVENEDYAGLIIPPAPPKPD
FDASREKLQKLGEGEGSMTKEEFEKMKQELEAEYLAIFKKTVAMHEVFLRRLASHPVLRNDANFRVFLEY
E
>gnl|CDD|132803 cd06893, PX_SNX19, The phosphoinositide binding Phox Homology domain of Sorting Nexin 19. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX19 contains an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. These domains are also found in SNX13 and SNX14, which also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNX19 interacts with IA-2, a major autoantigen found in type-1 diabetes. It inhibits the conversion of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to PI(3,4,5)P3, which leads in the decrease of protein phosphorylation in the Akt signaling pathway, resulting in apoptosis. SNX19 may also be implicated in coronary heart disease and thyroid oncocytic tumors
NIRIPKTITAKEYKGTGTHPYTLYTVQYETILDVQSEQNPNAASEQPLATHTVNRRFREFLTLQTRLEEN
PKFRKIMNVKGPPKRLFDLPFGNMDKDKIEARRGLLETFLRQLCSIPEISNSEEVQEFLAYG
>gnl|CDD|132804 cd06894, PX_SNX3_like, The phosphoinositide binding Phox Homology domain of Sorting Nexin 3 and related proteins. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily is composed of SNX3, SNX12, and fungal Grd19. Grd19 is involved in the localization of late Golgi membrane proteins in yeast. SNX3/Grp19 associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer
FLEIDVVNPQTHGVGKKRFTDYEVRMRTNLPVFKKKESSVRRRYSDFEWLRSELERDSKIVVPPLPGKAL
KRQLPFRGDDGIFEEEFIEERRKGLETFINKVAGHPLAQNEKCLHMFLQEETI
>gnl|CDD|132805 cd06895, PX_PLD, The phosphoinositide binding Phox Homology domain of Phospholipase D. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Phospholipase D (PLD) catalyzes the hydrolysis of the phosphodiester bond of phosphatidylcholine to generate membrane-bound phosphatidic acid and choline. Members of this subfamily contain PX and Pleckstrin Homology (PH) domains in addition to the catalytic domain. PLD activity has been detected in viruses, bacteria, yeast, plants, and mammals, but the PX domain is not present in PLDs from viruses and bacteria. PLDs are implicated in many cellular functions like signaling, cytoskeletal reorganization, vesicular transport, stress responses, and the control of differentiation, proliferation, and survival. Vertebrates contain two PLD isozymes, PLD1 and PLD2. PLD1 is located mainly in intracellular membranes while PLD2 is associated with plasma membranes. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction
GEPIKARITDVERSGTTRHLLNPNLYTIELQHGQFTWTIKRRYKHFQELHQALKLYRALLRIPLPTRRHK
EERLSLKRSRKPEREKKNRRLPSLPALPDILVSEEQLDSRKKQLENYLQNLLKIPDYRNHPETLEFLEVS
>gnl|CDD|132806 cd06896, PX_PI3K_C2_gamma, The phosphoinositide binding Phox Homology Domain of the Gamma Isoform of Class II Phosphoinositide 3-Kinases. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. The class II gamma isoform, PI3K-C2gamma, is expressed in the liver, breast, and prostate. It's biological function remains unknown. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction
RATILGFSKKSSNLYLVQVTQSCNLVSLTEKSFEQFSELHSQLQKQFPSLALPEFPHWWHLPFTDSDHKR
VRDLNHYLEQLLSGSREVANSDCVLSFFLSE
>gnl|CDD|132807 cd06897, PX_SNARE, The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction
LEISIPTTSVSPKPYTVYNIQVRLPLRSYTVSRRYSEFVALHKQLESEVGIEPPYPLPPKSWFLSTSSNP
KLVEERRVGLEAFLRALLNDEDSRWRNSPAVKEFLNLP
>gnl|CDD|132808 cd06898, PX_SNX10, The phosphoinositide binding Phox Homology domain of Sorting Nexin 10. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX10 may be involved in the regulation of endosome homeostasis. Its expression induces the formation of giant vacuoles in mammalian cells
SVEVRDPRTHKEDDWGSYTDYEIFLHTNSMCFTLKTSCVRRRYSEFVWLRNRLQKNALLIQLPSLPPKNL
FGRFNNEGFIEERQQGLQDFLEKVLQTPLLLSDSRLHLFLQTQ
>gnl|CDD|173887 cd06899, lectin_legume_LecRK_Arcelin_ConA, legume lectins, lectin-like receptor kinases, arcelin, concanavalinA, and alpha-amylase inhibitor. This alignment model includes the legume lectins (also known as agglutinins), the arcelin (also known as phytohemagglutinin-L) family of lectin-like defense proteins, the LecRK family of lectin-like receptor kinases, concanavalinA (ConA), and an alpha-amylase inhibitor. Arcelin is a major seed glycoprotein discovered in kidney beans (Phaseolus vulgaris) that has insecticidal properties and protects the seeds from predation by larvae of various bruchids. Arcelin is devoid of monosaccharide binding properties and lacks a key metal-binding loop that is present in other members of this family. Phytohaemagglutinin (PHA) is a lectin found in plants, especially beans, that affects cell metabolism by inducing mitosis and by altering the permeability of the cell membrane to various proteins. PHA agglutinates most mammalian red blood cell types by binding glycans on the cell surface. Medically, PHA is used as a mitogen to trigger cell division in T-lymphocytes and to activate latent HIV-1 from human peripheral lymphocytes. Plant L-type lectins are primarily found in the seeds of leguminous plants where they constitute about 10% of the total soluble protein of the seed extracts. They are synthesized during seed development several weeks after flowering and transported to the vacuole where they become condensed into specialized vesicles called protein bodies. L-type lectins have a dome-shaped beta-barrel carbohydrate recognition domain with a curved seven-stranded beta-sheet referred to as the "front face" and a flat six-stranded beta-sheet referred to as the "back face". This domain homodimerizes so that adjacent back sheets form a contiguous 12-stranded sheet and homotetramers occur by a back-to-back association of these homodimers. Though L-type lectins exhibit both sequence and structural similarity to one another, their carbohydrate binding specificities differ widely
LSFNFNGFSSDQSNLTLQGDATISSNGALQLTNDTSPASSVGRALYSKPVRLWDSTTGKVASFSTSFSFS
ITPPNPSLGGDGLAFFLAPTDSLPPASSGGYLGLFNSSNNGNSSNHIVAVEFDTFQNPEFGDPDDNHVGI
DVNSLVSVKAGYWDDDGGKLKSGKPMQAWIDYDSSSKRLSVTLAYSGVAKPKKPLLSYPVDLSKVLPEEV
YVGFSASTGLLTELHYILSWSFSSNG
>gnl|CDD|173888 cd06900, lectin_VcfQ, VcfQ bacterial pilus biogenesis protein, lectin domain. This family includes bacterial proteins homologous to the VcfQ (also known as MshQ) bacterial pilus biogenesis protein. VcfQ is encoded by the vcfQ gene of the type IV pilus gene cluster of Vibrio cholerae and is essential for type IV pilus assembly. VcfQ has a Laminin G-like domain as well as an L-type lectin domain
QCFSDNFDRPSLGNDWVVISSGGSFTPQVVNNRLRLTDASGNQATAVTLQRLFPSAGNYVEVEFDYYAYG
SGGNGADGVALVLSDASVTPQAGAFGGSLGYAQRNDGVPGFAGGWLGIGLDEYGNFSNPNEGRNGFSGRR
PQSVTVRGSGSGYTGYKYITGTGVLPPGIDNNSTSTPAPGHRYRITIDSTNGDNAWLSVERDIGNGGAYF
VVILTFDALAEQNQDAIPENFYLSFTGSTGGSTNTHEIDNFQVCA
>gnl|CDD|173889 cd06901, lectin_VIP36_VIPL, VIP36 and VIPL type 1 transmembrane proteins, lectin domain. The vesicular integral protein of 36 kDa (VIP36) is a type 1 transmembrane protein of the mammalian early secretory pathway that acts as a cargo receptor transporting high mannose type glycoproteins between the Golgi and the endoplasmic reticulum (ER). Lectins of the early secretory pathway are involved in the selective transport of newly synthesized glycoproteins from the ER to the ER-Golgi intermediate compartment (ERGIC). The most prominent cycling lectin is the mannose-binding type1 membrane protein ERGIC-53, which functions as a cargo receptor to facilitate export of glycoproteins from the ER. L-type lectins have a dome-shaped beta-barrel carbohydrate recognition domain with a curved seven-stranded beta-sheet referred to as the "front face" and a flat six-stranded beta-sheet referred to as the "back face". This domain homodimerizes so that adjacent back sheets form a contiguous 12-stranded sheet and homotetramers occur by a back-to-back association of these homodimers. Though L-type lectins exhibit both sequence and structural similarity to one another, their carbohydrate binding specificities differ widely
YLKREHSLIKPYQGVGSSMPLWDFLGSTMVTSQYIRLTPDHQSKQGSIWNRVPCYLRDWEMHVHFKVHGS
GKNLFGDGFAIWYTKERMQPGPVFGSKDNFHGLAIFFDTYSNQNGEHEHVHPYISAMVNNGSLSYDHDRD
GTHTELAGCSAPFRNKDHDTFVAIRYSKGRLTVMTDIDGKNEWKECFDVTGVRLPTGYYFGASAATGDLS
DNHDIISMKLYELDVEETPEEEEIDWSKIVPSVSYLKP
>gnl|CDD|173890 cd06902, lectin_ERGIC-53_ERGL, ERGIC-53 and ERGL type 1 transmembrane proteins, N-terminal lectin domain. ERGIC-53 and ERGL, N-terminal carbohydrate recognition domain. ERGIC-53 and ERGL are eukaryotic mannose-binding type 1 transmembrane proteins of the early secretory pathway that transport newly synthesized glycoproteins from the endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC). ERGIC-53 and ERGL have an N-terminal lectin-like carbohydrate recognition domain (represented by this alignment model) as well as a C-terminal transmembrane domain. ERGIC-53 functions as a 'cargo receptor' to facilitate the export of glycoproteins with different characteristics from the ER, while the ERGIC-53-like protein (ERGL) which may act as a regulator of ERGIC-53. In mammals, ERGIC-53 forms a complex with MCFD2 (multi-coagulation factor deficiency 2) which then recruits blood coagulation factors V and VIII. Mutations in either MCFD2 or ERGIC-53 cause a mild form of inherited hemophilia known as combined deficiency of factors V and VIII (F5F8D). In addition to the lectin and transmembrane domains, ERGIC-53 and ERGL have a short N-terminal cytoplasmic region of about 12 amino acids. ERGIC-53 forms disulphide-linked homodimers and homohexamers. ERGIC-53 and ERGL are sequence-similar to the lectins of leguminous plants. L-type lectins have a dome-shaped beta-barrel carbohydrate recognition domain with a curved seven-stranded beta-sheet referred to as the "front face" and a flat six-stranded beta-sheet referred to as the "back face". This domain homodimerizes so that adjacent back sheets form a contiguous 12-stranded sheet and homotetramers occur by a back-to-back association of these homodimers. Though L-type lectins exhibit both sequence and structural similarity to one another, their carbohydrate binding specificities differ widely
RRFEYKYSFKGPHLAQKDGTVPFWSHGGDAIASLEQVRLTPSLRSKKGSVWTKNPFSFENWEVEVTFRVT
GRGRIGADGLAIWYTKERGEEGPVFGSSDKWNGVGIFFDSFDNDGKKNNPAILVVGNDGTKSYDHQNDGL
TQALGSCLRDFRNKPYPVRAKITYYQNVLTVSINNGFTPNKDDYELCTRVENMVLPPNGYFGVSAATGGL
ADDHDVLSFLTFSLT
>gnl|CDD|173891 cd06903, lectin_EMP46_EMP47, EMP46 and EMP47 type 1 transmembrane proteins, N-terminal lectin domain. EMP46 and EMP47, N-terminal carbohydrate recognition domain. EMP46 and EMP47 are fungal type-I transmembrane proteins that cycle between the endoplasmic reticulum and the golgi apparatus and are thought to function as cargo receptors that transport newly synthesized glycoproteins. EMP47 is a receptor for EMP46 responsible for the selective transport of EMP46 by forming hetero-oligomerization between the two proteins. EMP46 and EMP47 have an N-terminal lectin-like carbohydrate recognition domain (represented by this alignment model) as well as a C-terminal transmembrane domain. EMP46 and EMP47 are 45% sequence-identical to one another and have sequence homology to a class of intracellular lectins defined by ERGIC-53 and VIP36. L-type lectins have a dome-shaped beta-barrel carbohydrate recognition domain with a curved seven-stranded beta-sheet referred to as the "front face" and a flat six-stranded beta-sheet referred to as the "back face". This domain homodimerizes so that adjacent back sheets form a contiguous 12-stranded sheet and homotetramers occur by a back-to-back association of these homodimers. Though L-type lectins exhibit both sequence and structural similarity to one another, their carbohydrate binding specificities differ widely
LNKDLSLPNLLKISPNGKLIPNWQTSGNPKLESGRIILTPPGNQRGSLWLKKPLSLKDEWTIEWTFRSTG
PEGRSGGGLNFWLVKDGNADVGTSSIYGPSKFDGLQLLIDNNGGSGGSLRGFLNDGSKDYKNEDVDSLAF
GSCLFAYQDSGVPSTIRLSYDALNSLFKVQVDNRLCFQTDKVQLPQGGYRFGITAANADNPESFEILKLK
VWNGL
>gnl|CDD|349475 cd06904, M14_MpaA-like, Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins. Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A (MpaA) and related proteins. MpaA is a member of the M14 family of metallocarboxypeptidases (MCPs), however it has an exceptional type of activity, it hydrolyzes the gamma-D-glutamyl-meso-diaminopimelic acid (gamma-D-Glu-Dap) bond in murein peptides. MpaA is specific for cleavage of the gamma-D-Glu-Dap bond of free murein tripeptide; it may also cleave murein tetrapeptide. MpaA has a different substrate specificity and cellular role than endopeptidase I, ENP1 (ENP1 does not belong to this group). MpaA works on free murein peptide in the recycling pathway
EKVYGTSVKGRPILAYKFGPGSRARILIIGGIHGDEPEGVSLVEHLLRWLKNHPASGDFHIVVVPCLNPD
GLAAGTRTNANGVDLNRNFPTKNWEPDARKPKDPRYYPGPKPASEPETRALVELIERFKPDRIISLHAPY
LVNYDGPAKSLLAEKLAQATGYPVVGDVGYTPGSLGTYAGIERNIPVITLELPEAVSIDELWQDLKRALI
EAIK
>gnl|CDD|349476 cd06905, M14-like, Peptidase M14-like domain; uncharacterized subfamily. A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism
LAFDRYYTYAELTARLKALAEAYPNLVRLESIGKSYEGRDIWLLTITNGETGPADEKPALWVDGNIHGNE
VTGSEVALYLAEYLLTNYGKDPEITRLLDTRTFYILPRLNPDGAEAYKLKTERSGRSSPRDDDRDGDGDE
DGPEDLNGDGLITQMRVKDPTGTWKVDPDDPRLMVDREKGEKGFYRLYPEGIDNDGDGRYNEDGPGGVDL
NRNFPYNWQPFYVQPGAGPYPLSEPETRAVADFLLAHPNIAAVLTFHTSGGMILRPPGTGPDSDMPPADR
RVYDAIGKKGVELTGYPVSSVYKDFYTVPGGPLDGDFFDWAYFHLGIPSFSTELWDLPEFAGKKKEGTVE
EAERLRWAD
>gnl|CDD|349477 cd06906, M14_Nna1, Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases. Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP), and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This eukaryotic subgroup includes the mouse Nna1/CCP-1, and -4 proteins, and the human Nna1/AGTPBP-1 protein. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Nna1 is widely expressed in the developing and adult nervous systems, including cerebellar Purkinje and granule neurons, miral cells of the olfactory bulb and retinal photoreceptors. Nna1 is also induced in axotomized motor neurons. Mutations in Nna1 cause Purkinje cell degeneration (pcd). The Nna1 CP domain is required to prevent the retinal photoreceptor loss and cerebellar ataxia phenotypes of pcd mice, and a functional zinc-binding domain is needed for Nna-1 to support neuron survival in these mice. Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain
SQIYYRQQTLCETLGGNSCPVLTITAMPESNNEEHICQFRNRPYIFLSARVHPGESNASWVMKGTLDFLL
SSSPAAQSLRESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRRWLNPNPELHPTIYHTKGLLQYLRSIGR
LPLVYCDYHGHSRKKNVFMYGCSPKESWSHGDTNNPSGDIVEDLGYRTLPKLLSHFAPAFSLSSCSFVVE
KSKESTARVVVWREIGVLRSYTMESTYCGCDQGKYKGLHIGTRELEEMGARFCEALLRLKR
>gnl|CDD|349478 cd06907, M14_AGBL2-3_like, Peptidase M14-like domain of ATP/GTP binding protein AGBL-2 and AGBL-3, and related proteins. Peptidase M14-like domain of ATP/GTP binding protein_like (AGBL)-2, and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This subgroup includes the human AGBL-2, and -3, and the mouse cytosolic carboxypeptidase (CCPs)-2, and -3. ATP/GTP binding protein (AGTPBP-1/Nna1)-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Mutations in AGTPBP-1/Nna1 cause Purkinje cell degeneration (pcd). AGTPBP-1/Nna1 however does not belong to this subgroup. AGTPBP-1/Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain
RSQYCKRRVLCRTLAGNSVYVLTITSPSSNPEEAKAKKAVVLTARVHPGETNASWMMKGFLDFLTGSSPD
AKLLRDNFVFKIVPMLNPDGVIVGNYRCSLAGRDLNRNYKTPLKESFPTIWHTKMMIKRLLEEREVILYC
DLHGHSRKQNVFMYGCENRKNPEKPLKERVFPLMLSKNAPDKFSFESCKFKVQKSKEGTGRVVMWREGIL
NSYTLEATFCGSTLGRRKGTHFNTLDFEAMGYHFCDTLLDYC
>gnl|CDD|349479 cd06908, M14_AGBL4_like, Peptidase M14-like domain of ATP/GTP binding protein AGBL-4 and related proteins. Peptidase M14-like domain of ATP/GTP binding protein_like (AGBL)-4, and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This eukaryotic subgroup includes the human AGBL4 and the mouse cytosolic carboxypeptidase (CCP)-6. ATP/GTP binding protein (AGTPBP-1/Nna1)-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Mutations in AGTPBP-1/Nna1 cause Purkinje cell degeneration (pcd). AGTPBP-1/Nna1 however does not belong to this subgroup. AGTPBP-1/Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain
NFFTRELLGKSVQQRRLDLLTITDPVNKHLTVEKKKKVVFITARVHPGETPSSFVCQGLIDFLVSNHPVA
KVLRDHLVFKIVPMLNPDGVFLGNYRCSLMGFDLNRHWHEPSPWAHPTLYAVKNLLRELDNDPTVQLDFY
IDIHAHSTLMNGFMYGNIYDDVYRFERQAVFPKLLCQNAEDFSLSNTVFNRDPVKAGTGRRFLGGLLDDT
ANCYTLEVSFYSYRLSDSSSATPYTEEGYMKLGRNMARALLDYY
>gnl|CDD|349480 cd06909, M14_ASPA, Peptidase M14 Aspartoacylase (ASPA) subfamily. Aspartoacylase (ASPA) belongs to the Succinylglutamate desuccinylase/aspartoacylase subfamily of the M14 family of metallocarboxypeptidases. ASPA (also known as aminoacylase 2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD
KRVAIVGGTHGNELTGVYLVKHWLKNPELIERKSFEVHPLLANPRAVEQCRRYIDTDLNRCFSLENLSSA
PSSLPYEVRRAREINQILGPKGNPACDFIIDLHNTTSNMGITLILSSSDDFTLKLAAYLQQRLPPVRVLL
HESPSKESPFLRSVAKHGFTIEVGPVPQGVLRADIFEQTRKLVKAILDFI
>gnl|CDD|349481 cd06910, M14_ASTE_ASPA-like, Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup. A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD
DISPYKTGNTGIDYVHRFDSGQPGPHVMINALTHGNEICGAIALDWLLKNGVRPLRGRLTFCFANVEAYE
RFDPARPTASRFVDEDLNRVWGPELLDGPEQSIELRRARELRPVVDTVDYLLDIHSMQEKVPPLALAGDK
EKGRALARRVGSPAHLLIDAGHAEGLRLRDYAGFGDPSSPKNALLVECGQHWERSAVVVALDITLRFL
>gnl|CDD|132874 cd06911, VirB9_CagX_TrbG, VirB9/CagX/TrbG, a component of the type IV secretion system. VirB9 is a component of the type IV secretion system, which is employed by pathogenic bacteria to export virulence proteins directly from the bacterial cytoplasm into the host cell. Unlike the more common type III secretion system, type IV systems evolved from the conjugative apparatus, which is used to transfer DNA between cells. VirB9 was initially identified as an essential virulence gene on the Agrobacterium tumefaciens Ti plasmid. In the pilin-like conjugative structure, VirB9 appears to form a stabilizing complex in the outer membrane, by interacting with the lipoprotein VirB7. The heterodimer has been shown to stabilize other components of the type IV system. This alignment model spans the C-terminal domain of VirB9. CagX is a component of the Helicobacter pylori cag PAI-encoded type IV secretion system. Some other members of this family are involved in conjugal transfer to T-DNA of plant cells
PGPLNFDYSISGSAAIKPVRVFDDGRFTYFQFPPNAELPAIFVVDPDGKESLVNYRVEGNYIVVDGVAPK
LVLRLGDEVVRIVNKG
>gnl|CDD|133467 cd06912, GT_MraY_like, This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like family. This family contains both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine:polyprenol phosphate D-N-acetylhexosamine-1-phosphate transferases, which catalyze the transfer of a D-N-acetylhexosamine 1-phosphate to a membrane-bound polyprenol phosphate. This is the initiation step of protein N-glycosylation in eukaryotes and peptidoglycan biosynthesis in bacteria. The three bacterial members MraY, WecA, and WbpL/WbcO, utilize undecaprenol phosphate as the acceptor substrate, but use different UDP-sugar donor substrates. MraY-type transferases are highly specific for UDP-N-acetylmuramate-pentapeptide, whereas WecA proteins are selective for UDP-N-acetylglucosamine (UDP-GlcNAc). The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic end products implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The prokaryotic enzyme-catalyzed reactions lead to the formation of polyprenol-linked oligosaccharides involved in bacterial cell wall and peptidoglycan assembly
DGIQKFHTRPTPRIGGVAIFLGLLAGLLLLSLLSGSLLLLLLLAALPAFLAGLLEDITKRVSPRIRLLAT
FLSALLAVWLLGASITRLDLPGLDLLLSFPPFAIIFTIFAVAGVANAFNIIDGFNGLASGVAIISLLSLA
LVAFQVGDTDLAFLALLLAGALLGFLIFNFPFGKIFLGDGGAYLLGFLLAWLA
>gnl|CDD|133063 cd06913, beta3GnTL1_like, Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine . This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified
IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPK
GVGYAKNQAIAQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLT
REQLLTQVYTSHGPTVIMPTWFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRY
HPGATTHSV
>gnl|CDD|133064 cd06914, GT8_GNT1, GNT1 is a fungal enzyme that belongs to the GT 8 family. N-acetylglucosaminyltransferase is a fungal enzyme that catalyzes the addition of N-acetyl-D-glucosamine to mannotetraose side chains by an alpha 1-2 linkage during the synthesis of mannan. The N-acetyl-D-glucosamine moiety in mannan plays a role in the attachment of mannan to asparagine residues in proteins. The mannotetraose and its N-acetyl-D-glucosamine derivative side chains of mannan are the principle immunochemical determinants on the cell surface. N-acetylglucosaminyltransferase is a member of glycosyltransferase family 8, which are, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed, retaining glycosyltransferases
YAYVNYATNADYLCNALILFEQLRRLGSKAKLVLLVPETLLDRNLDDFVRRDLLLARDKVIVKLIPVIIA
SGGDAYWAKSLTKLRAFNQTEYDRIIYFDSDSIIRHPMDELFFLPNYIKFAAPRAYWKFASHLMVIKPSK
EAFKELMTEILPAYLNKKNEYDMDLINEEFYNSKQLFKPSVLVLPHRQYGLLTGEFREKLHKSFLSNAQH
LYEKWDPDDVFKESKVIHFSDSPLPKPWNYNNLEDIYCIEKIYCKMVKPRLEDDCRACDLWNSLYADF
>gnl|CDD|133065 cd06915, NTP_transferase_WcbM_like, WcbM_like is a subfamily of nucleotidyl transferases. WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars
AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGI
RIYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPDASRYG
NVTVDGDGRVIAFVEKGPGAAPGLINGGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGFEVDGYF
IDIGIPEDYARAQ
>gnl|CDD|143512 cd06916, NR_DBD_like, DNA-binding domain of nuclear receptors is composed of two C4-type zinc fingers. DNA-binding domain of nuclear receptors is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. It interacts with a specific DNA site upstream of the target gene and modulates the rate of transcriptional initiation. Nuclear receptors form a superfamily of ligand-activated transcription regulators, which regulate various physiological functions, from development, reproduction, to homeostasis and metabolism in animals (metazoans). The family contains not only receptors for known ligands but also orphan receptors for which ligands do not exist or have not been identified. NRs share a common structural organization with a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD). Most nuclear receptors bind as homodimers or heterodimers to their target sites, which consist of two hexameric half-sites. Specificity is determined by the half-site sequence, the relative orientation of the half-sites and the number of spacer nucleotides between the half-sites. However, a growing number of nuclear receptors have been reported to bind to DNA as monomers
CAVCGDKASGYHYGVLTCEGCKGFFRRSVRRNLEYTCPAGGNCVIDKRNRNRCQACRLKKCLAVGMRKEA
VR
>gnl|CDD|270822 cd06917, STKc_NAK1_like, Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SLYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDVSDIQKEVALLSQLKLGQPKNIIKYYGS
YLKGPSLWIIMDYCEGGSIRTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNV
KLCDFGVAASLNQNSSKRSTFVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPYSDVDALRA
VMLIPKSKPPRLEGNGYSPLLKEFVAACLDEEPKDRLSADELLKSKWIKQHSKTPTSVLKELISRYN
>gnl|CDD|132994 cd06919, Asp_decarbox, Aspartate alpha-decarboxylase or L-aspartate 1-decarboxylase, a pyruvoyl group-dependent decarboxylase in beta-alanine production. Decarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalyzed by the enzyme L-aspartate decarboxylase (ADC), EC:4.1.1.11 which requires a pyruvoyl group for its activity. The pyruvoyl cofactor is covalently bound to the enzyme. The protein is synthesized as a proenzyme and cleaved via self-processing at Gly23-Ser24 to yield an alpha chain (C-terminal fragment) and beta chain (N-terminal fragment), and the pyruvoyl group. Beta-alanine is required for the biosynthesis of pantothenate, in which the enzyme plays a critical regulatory role. The active site of the tetrameric enzyme is located at the interface of two subunits, with a Lysine and a Histidine from the beta chain of one subunit forming the active site with residues from the alpha chain of the adjacent subunit. This alignment model spans the precursor (or both beta and alpha chains) of aspartate decarboxylase
LRTMLKSKIHRATVTEADLNYEGSITIDEDLLEAAGILPYEKVLVVNVNNGARFETYVIPGERGSGVICL
NGAAARLGQPGDRVIIMAYALMDEEEAEGHKPKVVLVDEKN
>gnl|CDD|132993 cd06920, NEAT, NEAr Transport domain, a component of cell surface proteins. NEAr Transporter (NEAT) domain; used by pathogenic bacteria to to scavenge heme-iron from host hemoproteins. The NEAT domain is a component of cell surface proteins (iron regulated surface determinants, or Isd, such as IsdA and IsdC) in various gram-positive bacteria, and may be arranged in tandem repeats
DGTYTVNFKVLKEGTDEPSMANGYLNKPAKLTVKNGKKYVTLTLKNSDWMKNFKVEVNGGNKDVVVVKDD
NSNNTRTVKFEVPDLDSKINAKVHVVVMGINYDHKYDVRLKFDTSSI
>gnl|CDD|211312 cd06921, ChtBD1_GH19_hevein, Hevein or Type 1 chitin binding domain subfamily co-occuring with family 19 glycosyl hydrolases or with barwin domains. This subfamily includes Hevein, a major IgE-binding allergen in natural rubber latex. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements
EQCGRQAGGALCPGGLCCSQWGWCGSTDDYCGDGCQSQCG
>gnl|CDD|211313 cd06922, ChtBD1_GH18_1, Hevein or Type 1 chitin binding domain subfamily that co-occurs with family 18 glycosyl hydrolases. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements
PGTCSPTQPCKGGCCNKDGVCGFGPDYCGADVCISNCD
>gnl|CDD|211314 cd06923, ChtBD1_GH16, Hevein or Type 1 chitin binding domain subfamily that co-occurs with family 16 glycosyl hydrolases. This subfamily includes Saccharomyces cerevisiae Utr2p, also known as Crh2p, which participates in the cross-linking of chitin to beta(1-3)- and beta(1-6) glucan in the cell wall, and S. cerevisiae Crr1p, a putative transglycosidase which is needed for proper spore wall assembly. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements
ITCNETSQCPEEWPCCSQYGECGTGPYCLGGCNPRYSFSLDSCMPMP
>gnl|CDD|132902 cd06926, RNAP_II_RPB11, RPB11 subunit of Eukaryotic RNA polymerase II. The eukaryotic RPB11 subunit of RNA polymerase (RNAP) II is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. At least three distinct RNAP complexes are found in eukaryotic nuclei: RNAP I, RNAP II, and RNAP III. RNAP II is responsible for the synthesis of mRNA precursor. The RPB11 subunit heterodimerizes with the RPB3 subunit, and together with RPB10 and RPB12, anchors the two largest subunits, RPB1 and RPB2, and stabilizes their association
PEGEKKITEKKDTKVPNAATFTINKEDHTLGNLLRMQLLKDPNVLFAGYKVPHPLEHKIELRIQTDGSIT
PKEALKNAITDLISELSLLKEEF
>gnl|CDD|132903 cd06927, RNAP_L, L subunit of Archaeal RNA polymerase. The archaeal L subunit of RNA polymerase (RNAP) is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. A single distinct RNAP complex is found in archaea, which may be responsible for the synthesis of all RNAs. The archaeal RNAP harbors homologues of all eukaryotic RNAP II subunits with two exceptions (RPB8 and RPB9). The 12 archaeal subunits are designated by letters and can be divided into three functional groups that are engaged in: (I) catalysis (A'/A", B'/B" or B); (II) assembly (L, N, D and P); and (III) auxiliary functions (F, E, H and K). The assembly of the two largest archaeal RNAP subunits that provide most of the enzyme's catalytic functions depends on the presence of the archaeal D/L heterodimer
LKVIEKEDNELELEIEGEDHTLLNLLKEELLRDPGVKVASYDIEHPLLSNPVLKIKTDGGVDPLEALKEA
AKRLIDLCEEFLD
>gnl|CDD|132904 cd06928, RNAP_alpha_NTD, N-terminal domain of the Alpha subunit of Bacterial RNA polymerase. The bacterial alpha subunit of RNA polymerase (RNAP) consists of two independently folded domains: an amino-terminal domain (alphaNTD) and a carboxy-terminal domain (alphaCTD). AlphaCTD is not required for RNAP assembly but interacts with transcription activators. AlphaNTD is essential in vivo and in vitro for RNAP assembly and basal transcription. It is similar to the eukaryotic RPB3/AC40/archaeal D subunit, and contains two subdomains: one subdomain is similar the eukaryotic Rpb11/AC19/archaeal L subunit which is involved in dimerization; and the other is an inserted beta sheet subdomain. The alphaNTDs of plant plastid RNAP (PEP) are also included in this subfamily. PEP is largely responsible for the transcription of photosynthetic genes and is closely related to the multi-subunit bacterial RNAP, which is a large multi-subunit complex responsible for the synthesis of all bacterial RNAs. The bacterial RNAP core enzyme consists of four subunits (beta', beta, alpha and omega). All residues in the alpha subunit that is involved in dimerization or in the interaction with other subunits are located within alphaNTD
SKVENKRENYGRFVIEPLERGQGTTLGNALRRVLLSSLPGAAITAVKIEGVLHEFSTIPGVREDVLEILL
NLKEIVFKSDSEDEPQVLRLKVKGPGVVTAADIELPSGVEIVNPDQYIATLTEDASLEMELRIEKGRGYV
PAEENKSEEKPIGFIPIDAIFSPVRKVNYSVESTRVGQRTDYEKLILEIWTNGSISPEEALAQAAKILIN
HFSPF
>gnl|CDD|132727 cd06929, NR_LBD_F1, Ligand-binding domain of nuclear receptor family 1. Ligand-binding domain (LBD) of nuclear receptor (NR) family 1: This is one of the major subfamily of nuclear receptors, including thyroid receptor, retinoid acid receptor, ecdysone receptor, farnesoid X receptor, vitamin D receptor, and other related receptors. Nuclear receptors form a superfamily of ligand-activated transcription regulators, which regulate various physiological functions, from development, reproduction, to homeostasis and metabolism in animals (metazoans). The family contains not only receptors for known ligands but also orphan receptors for which ligands do not exist or have not been identified. NRs share a common structural organization with a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
QEKFDHFTEIMTVAIRRVVEFAKRIPGFRELSQEDQIALLKGGCFEILLLRSATLYDPEKNSLTFGDGKG
NSRDVLLNGGFGEFIEPLFEFAEKMNKLQLDDNEYALLTAIVLFSPDRPGLQDVDTVEKLQERLLEALQR
YLKVNHPDAPQMFAKLLKKLTELRTLNELHAELL
>gnl|CDD|132728 cd06930, NR_LBD_F2, Ligand-binding domain of nuclear receptor family 2. Ligand-binding domain (LBD) of nuclear receptor (NR) family 2: This is one of the major subfamily of nuclear receptors, including some well known nuclear receptors such as glucocorticoid receptor (GR), mineralocorticoid receptor (MR), estrogen receptor (ER), progesterone receptor (PR), and androgen receptor (AR), other related receptors. Nuclear receptors form a superfamily of ligand-activated transcription regulators, which regulate various physiological functions, from development, reproduction, to homeostasis and metabolism in animals (metazoans). The family contains not only receptors for known ligands but also orphan receptors for which ligands do not exist or have not been identified. NRs share a common structural organization with a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
PESLCELADRVLFKTVDWAKNLPAFRNLPLDDQLTLLQNSWAELLLLGLAQRSVHFELSELLLPSPLLVI
LTEREALLGLAELVQRLQELLSKLRSLQLDPKEYACLKAIVLFNPDLPGLKNQQQVEELQEKAQQALQEY
IRKRYPQQPARFAKLLLRLPELRSI
>gnl|CDD|132729 cd06931, NR_LBD_HNF4_like, The ligand binding domain of heptocyte nuclear factor 4, which is explosively expanded in nematodes. The ligand binding domain of hepatocyte nuclear factor 4 (HNF4) like proteins: HNF4 is a member of the nuclear receptor superfamily. HNF4 plays a key role in establishing and maintenance of hepatocyte differentiation in the liver. It is also expressed in gut, kidney, and pancreatic beta cells. HNF4 was originally classified as an orphan receptor, but later it is found that HNF4 binds with very high affinity to a variety of fatty acids. However, unlike other nuclear receptors, the ligands do not act as a molecular switch for HNF4. They seem to constantly bind to the receptor, which is constitutively active as a transcription activator. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, HNF4 has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD). The LBD domain is also responsible for recruiting co-activator proteins. More than 280 nuclear receptors are found in C. ele gans, most of which are originated from an explosive burst of duplications of HNF4
SISVLLQAEALSRQQSSPIPTCSGDIRPKKIASINDVCESMKQQLLVLVEWAKYIPAFCELPLDDQVALL
RAHAGEHLLLGVARRSMPYKDILLLGNDLIIPRHCPEPEISRVANRILDELVLPLRDLNIDDNEYACLKA
IVFFDPDAKGLSDPQKIKRLRFQVQVSLEDYINDRQYDSRGRFGELLLLLPTLQSITWQMIEQIQFARLF
GVAKIDNLLQEM
>gnl|CDD|132730 cd06932, NR_LBD_PPAR, The ligand binding domain of peroxisome proliferator-activated receptors. The ligand binding domain (LBD) of peroxisome proliferator-activated receptors (PPAR): Peroxisome proliferator-activated receptors (PPARs) are members of the nuclear receptor superfamily of ligand-activated transcription factors. PPARs play important roles in regulating cellular differentiation, development and lipid metabolism. Activated PPAR forms a heterodimer with the retinoid X receptor (RXR) that binds to the hormone response element located upstream of the peroxisome proliferator responsive genes and interacts with co-activators. There are three subtypes of peroxisome proliferator activated receptors, alpha, beta (or delta), and gamma, each with a distinct tissue distribution. Several essential fatty acids, oxidized lipids and prostaglandin J derivatives can bind and activate PPAR. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, PPAR has a central well conserved DNA binding domain (DBD), a variable N-terminal regulatory domain, a flexible hinge a nd a C-terminal ligand binding domain (LBD)
ADLRALAKHLYVAYLKQFPLTKAKARKILTGKTTDHAPFVIYDIESLKLNKDGQPQEKTIRIRLFQRCQV
RSVETIRELTEFAKSLPGFRNLDLNDQVTLLKYGVHEVIFTMLASLYNKDGLLFPEGNGYVTREFLESLR
KPFCDIMEPKFEFAEKFNALELTDSELALFCAVIILSPDRPGLINRKPVERIQEHVLQALELQLKKNHPD
SPQLFAKLLQKMVDLRQLVTDHVQMVQQIKKTETDASLPPLLQEIYKDM
>gnl|CDD|132731 cd06933, NR_LBD_VDR, The ligand binding domain of vitamin D receptors, a member of the nuclear receptor superfamily. The ligand binding domain of vitamin D receptors (VDR): VDR is a member of the nuclear receptor (NR) superfamily that functions as classical endocrine receptors. VDR controls a wide range of biological activities including calcium metabolism, cell proliferation and differentiation, and immunomodulation. VDR is a high affinity receptor for the biologically most active Vitamin D metabolite, 1alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)2D3). The binding of the ligand to the receptor induces a conformational change of the ligand binding domain (LBD) with consequent dissociation of corepressors. Upon ligand binding, VDR forms heterodimer with the retinoid X receptor (RXR) that binds to vitamin D response elements (VDREs), recruits coactivators. This leads to the expression of a large number of genes. Approximately 200 human genes are considered to be primary targets of VDR and even more genes are regulated indirectly. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, VDR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
LSDEQQKIIDILLEAHHKTYDTTYSDFNKFRPPVRLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTAED
QIALLKSSAIEVIMLRSNQSFSLDDMSWTCGSPDFKYKVSDVTKAGHSLELLEPLVKFQVGLKKLNLHEE
EHVLLMAICILSPDRPGVQDHALIEAIQDRLSDTLQTYIRCRHPPPGSRLLYAKMIQKLADLRSLNEEHS
KQYRSLSFQPEHSMKLTPLVLEVFGNEI
>gnl|CDD|132732 cd06934, NR_LBD_PXR_like, The ligand binding domain of xenobiotic receptors:pregnane X receptor and constitutive androstane receptor. The ligand binding domain of xenobiotic receptors: This xenobiotic receptor family includes pregnane X receptor (PXR), constitutive androstane receptor (CAR) and other related nuclear receptors. They function as sensors of toxic byproducts of cell metabolism and of exogenous chemicals, to facilitate their elimination. The nuclear receptor pregnane X receptor (PXR) is a ligand-regulated transcription factor that responds to a diverse array of chemically distinct ligands, including many endogenous compounds and clinical drugs. The ligand binding domain of PXR shows remarkable flexibility to accommodate both large and small molecules. PXR functions as a heterodimer with retinoic X receptor-alpha (RXRa) and binds to a variety of response elements in the promoter regions of a diverse set of target genes involved in the metabolism, transport, and elimination of these molecules from the cell. Constitutive androstane receptor (CAR) is a closest mammalian relative of PXR, which has also been proposed to function as a xenosensor. CAR is activated by some of the same ligands as PXR and regulates a subset of common genes. The sequence homology and functional similarity suggests that the CAR gene arose from a duplication of an ancestral PXR gene. Like other nuclear receptors, xenobiotic receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
LTPEQEELIRELVGAHTKTFDTTFSQFKQFRPPFSLLPHFADLTTYMIKQIIKFAKDLPYFRSLPIEDQI
SLLKGATFEICQIRFNTVFNEETGTWECGPLTYCIEDAARAGFQQLLLEPLLRFHYTLRKLQLQEEEYVL
MQAMSLFSPDRPGVTQHDVIDQLQEKMALTLKSYIDSKRPGPEKRFLYPKILACLTELRTINEEYTKQIL
HIQDIQPMATPLMQEI
>gnl|CDD|132733 cd06935, NR_LBD_TR, The ligand binding domain of thyroid hormone receptor, a members of a superfamily of nuclear receptors. The ligand binding domain (LBD) of thyroid hormone receptors: Thyroid hormone receptors are members of a superfamily of nuclear receptors. Thyroid hormone receptors (TR) mediate the actions of thyroid hormones, which play critical roles in growth, development, and homeostasis in mammals. They regulate overall metabolic rate, cholesterol and triglyceride levels, and heart rate, and affect mood. TRs are expressed from two separate genes (alpha and beta) in human and each gene generates two isoforms of the receptor through differential promoter usage or splicing. TRalpha functions in the heart to regulate heart rate and rhythm and TRbeta is active in the liver and other tissues. The unliganded TRs function as transcription repressors, by binding to thyroid hormone response elements (TRE) predominantly as homodimers, or as heterodimers with retinoid X-receptors (RXR), and being associated with a complex of proteins containing corepressor proteins. Ligand binding promotes corepressor dissociation and binding of a coactivator to activate transcription. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, TR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
DEEWELIRTVTEAHVATNAQGSHWKQKRKFLPEDIGQAPIVSAPDGDKVDLEAFSHFTKIITPAITRVVD
FAKKLPMFTELPCEDQIILLKGCCMEIMSLRAAVRYDPESETLTLSGEMAVTREQLKNGGLGVVSDAIFD
LGVSLSSFNLDDTEVALLQAVLLMSSDRPGLACVERIEKLQDSFLLAFEHYINYRKHHVPHFWPKLLMKV
TDLRMIGACHASRFLHMKVECPTELFPPLFLEV
>gnl|CDD|132734 cd06936, NR_LBD_Fxr, The ligand binding domain of Farnesoid X receptor:a member of the nuclear receptor superfamily of ligand-activated transcription factors. The ligand binding domain (LBD) of Farnesoid X receptor: Farnesoid X receptor (FXR) is a member of the nuclear receptor superfamily of ligand-activated transcription factors. FXR is highly expressed in the liver, the intestine, the kidney, and the adrenals. FXR plays key roles in the regulation of bile acid, cholesterol, triglyceride, and glucose metabolism. Evidences show that it also regulates liver regeneration. Upon binding of ligands, such as bile acid, an endogenous ligand, FXRs bind to FXR response elements (FXREs) either as a monomer or as a heterodimer with retinoid X receptor (RXR), and regulate the expression of various genes involved in bile acid, lipid, and glucose metabolism. There are two FXR genes (FXRalpha and FXRbeta) in mammals. A single FXRalpha gene encodes four isoforms resulting from differential use of promoters and alternative splicing. FXRbeta is a functional receptor in mice, rats, rabbits and dogs, but is a pseudogene in humans and primates. Like other members of the nuclear receptor (NR) superfamily, farnesoid X receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
QEQQTLLDYIVDAYQKQRIPQEITKKLLQEEFSPEENFLILTEMATSHVQVLVEFTKGLPGFETLDHEDQ
IALLKGSAVEAMFLRSAQIYNKKLPAGHADLLEERIRSSGISDEFITPMFNFYKSMGELKMTQEEYALLT
AITILFPDRPYLKDKEAVEKLQEPLLDLLQKFCKLYHPEDPQHFACLLGRLTELRTLNHHHAEMLMSWKV
NDHKFTPLLCE
>gnl|CDD|132735 cd06937, NR_LBD_RAR, The ligand binding domain (LBD) of retinoic acid receptor (RAR), a members of the nuclear receptor superfamily. The ligand binding domain (LBD) of retinoic acid receptor (RAR): Retinoic acid receptors are members of the nuclear receptor (NR) superfamily of ligand-regulated transcription factors. RARs mediate the biological effect of retinoids, including both naturally dietary vitamin A (retinol) metabolites and active synthetic analogs. Retinoids play key roles in a wide variety of essential biological processes, such as vertebrate embryonic morphogenesis and organogenesis, differentiation and apoptosis, and homeostasis. RARs function as heterodimers with retinoic X receptors by binding to specific RAR response elements (RAREs) found in the promoter regions of retinoid target genes. In the absence of ligand, the RAR-RXR heterodimer recruits the corepressor proteins NCoR or AMRT, and associated factors such as histone deacetylases or DNA-methyltransferases, leading to an inactive condensed chromatin structure, preventing transcription. Upon ligand binding, the corepressors are released, and coactivator complexes such as histone acetyltransferase or histone arginine methyltransferases are recruited to activate transcription. There are three RAR subtypes (alpha, beta, gamma), originating from three distinct genes. For each subtype, several isoforms exist that differ in their N-terminal region, allowing retinoids to exert their pleiotropic effects. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, retinoic acid receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
DLITKVRKAHQETFPSLCQLGKYTTNSSADQRVRLDLGLWDKFSELSTKCIIKIVEFAKRLPGFTTLTIA
DQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLEMDDTE
IGLLSAICLICGDRQDLEEPDRVEKLQEPLLEALKIYARKRRPDKPHMFPKMLMKITDLRSISAKGAERV
ITLKMEIPGPMPPLISEMLEN
>gnl|CDD|132736 cd06938, NR_LBD_EcR, The ligand binding domain (LBD) of the Ecdysone receptor, a member of the nuclear receptors super family. The ligand binding domain (LBD) of the ecdysone receptor: The ecdysone receptor (EcR) belongs to the superfamily of nuclear receptors (NRs) of ligand-dependent transcription factors. Ecdysone receptor is present only in invertebrates and regulates the expression of a large number of genes during development and reproduction. ECR functions as a heterodimer by partnering with ultraspiracle protein (USP), the ortholog of the vertebrate retinoid X receptor (RXR). The natural ligands of ecdysone receptor are ecdysteroids#the endogenous steroidal hormones found in invertebrates. In addition, insecticide bisacylhydrazine used against pests has shown to act on EcR. EcR must be dimerised with a USP for high-affinity ligand binding to occur. The ligand binding triggers a conformational change in the C-terminal part of the EcR ligand-binding domain that leads to transcriptional activation of genes controlled by EcR. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, ec dysone receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
QEELINRLVYYQEEFEQPSEEDLKRITEHPQNDEDQSDMRFRHITEMTILTVQLIVEFAKRLPGFDKLSR
EDQITLLKACSSEVMMLRVARRYDAKTDSIVFANNQPYTRDSYRKAGMGDSAEDLFRFCRAMCSMKVDNA
EYALLTAIVIFSDRPGLLQPKKVEKIQEIYLEALRAYVDNRRPPSQRVIFAKLLSILTELRTLGNQNSEM
CFSLKLKNRKLPPFLAEIWDV
>gnl|CDD|132737 cd06939, NR_LBD_ROR_like, The ligand binding domain of Retinoid-related orphan receptors, of the nuclear receptor superfamily. The ligand binding domain (LBD) of Retinoid-related orphan receptors (RORs): Retinoid-related orphan receptors (RORs) are transcription factors belonging to the nuclear receptor superfamily. RORs are key regulators of many physiological processes during embryonic development. RORs bind as monomers to specific ROR response elements (ROREs) consisting of the consensus core motif AGGTCA preceded by a 5-bp A/T-rich sequence. Transcription regulation by RORs is mediated through certain corepressors, as well as coactivators. There are three subtypes of retinoid-related orphan receptors (RORs), alpha, beta, and gamma that differ only in N-terminal sequence and are distributed in distinct tissues. RORalpha plays a key role in the development of the cerebellum, particularly in the regulation of the maturation and survival of Purkinje cells. RORbeta expression is largely restricted to several regions of the brain, the retina, and pineal gland. RORgamma is essential for lymph node organogenesis. Recently, it has been su ggested that cholesterol or a cholesterol derivative is the natural ligand of RORalpha. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, retinoid-related orphan receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
DELEHLAQNICKAHLETCQYLREELQQLRWKTFSQEEILAYQNKSREEMWQLCAEKITEAIQYVVEFAKR
IPGFMELCQNDQIVLLKAGSLEVVLVRMSRAFNPSNNTVLFDGKYAPIDLFKSLGCDDLISAVFDFAKSL
CELKLTEDEIALFSALVLISADRPGLQEKRKVEKLQQKIELALRHVLQKNHGDDTILTKLLAKMPTLRAL
CSLHMEKLQKFKQSYPDIVHLEFPPLYKELF
>gnl|CDD|132738 cd06940, NR_LBD_REV_ERB, The ligand binding domain of REV-ERB receptors, members of the nuclear receptor superfamily. The ligand binding domain (LBD) of REV-ERB receptors: REV-ERBs are transcriptional regulators belonging to the nuclear receptor superfamily. They regulate a number of physiological functions including the circadian rhythm, lipid metabolism, and cellular differentiation. The LBD domain of REV-ERB is unusual in the nuclear receptor family by lacking the AF-2 region that is responsible for coactivator interaction. REV-ERBs act as constitutive repressors because of their inability to bind coactivators. REV-ERB receptors can bind to two classes of DNA response elements as either a monomer or heterodimer, indicating functional diversity. When bound to the DNA, they recruit corepressors (NcoR/histone deacetylase 3) to the promoter, resulting in repression of the target gene. The porphyrin heme has been demonstrated to function as a ligand for REV-ERB. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, REV-ERB receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
SPYVDPPKSGHEIWEEFSMSFTPAVREVVEFAKRIPGFRDLSQHDQVTLLKAGTFEVLMVRFASLFDAKE
RSVTFLSGQKYSVDDLHSMGAGDLLNSMFDFSEKLNSLQLSDEEMGLFTAVVLVSADRSGLENVNLVEAL
QETLIRALRTLIAKNHPNEPSIFTKLLLKLPDLRTLNNLHSEKLLAFKV
>gnl|CDD|132739 cd06941, NR_LBD_DmE78_like, The ligand binding domain of Drosophila ecdysone-induced protein 78, a member of the nuclear receptor superfamily. The ligand binding domain (LBD) of Drosophila ecdysone-induced protein 78 (E78) like: Drosophila ecdysone-induced protein 78 (E78) is a transcription factor belonging to the nuclear receptor superfamily. E78 is a product of the ecdysone-inducible gene found in an early late puff locus at position 78C during the onset of Drosophila metamorphosis. Two isoforms of E78, E78A and E78B, are expressed from two nested transcription units. An E78 orthologue from the Platyhelminth Schistosoma mansoni (SmE78) has also been identified. It is the first E78 orthologue known outside of the molting animals--the Ecdysozoa. SmE78 may be involved in transduction of an ecdysone signal in S. mansoni, consistent with its function in Drosophila. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, E78-like receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
IWLWQQLSEALTPSVQRVVEFAKRIPGFCDLSQDDQLLLIKAGFFEVWLVRISRLINSKSGSITFDDGIS
ISRQQLDIIYDSDFVKALFEFSDSFNSLGLSDTEVALFCAVVLLSPDRIGLSEPKKVAILQDRVLEALKV
QVSRNRPAEAQLFASLLMKIPELRSIGAKHQMHLDWYRVNWPLLRLPPLFAEIYD
>gnl|CDD|132740 cd06942, NR_LBD_Sex_1_like, The ligand binding domain of Caenorhabditis elegans nuclear hormone receptor Sex-1 protein. The ligand binding domain (LBD) of Caenorhabditis elegans nuclear hormone receptor Sex-1 protein like: Sex-1 protein of C. elegans is a transcription factor belonging to the nuclear receptor superfamily. Sex-1 plays pivotal role in sex fate of C. elegans by regulating the transcription of the sex-determination gene xol-1, which specifies male (XO) fate when active and hermaphrodite (XX) fate when inactive. The Sex-1 protein directly represses xol-1 transcription by binding to its promoter. However, the active ligand for Sex-1 protein has not yet been identified. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, Sex-1 like receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
LNAWGHFAHEFEMHIQEIVQFVKSIPGFNQLSGEDRAQLLKGNMFPLYLLRLSRDYNNEGTVLCDFRPVE
FASLLSQLLHGKLIDEMLQFANKILTLNLTNAELALLCAAELLQPDSLGIQLEETAKSNLQLSVLFQFLK
SVLFKDGEDTEQRLQKLFDILNRLRNMNKEHQNILADRDKRSNLQLPPLYL
>gnl|CDD|132741 cd06943, NR_LBD_RXR_like, The ligand binding domain of the retinoid X receptor and Ultraspiracle, members of nuclear receptor superfamily. The ligand binding domain of the retinoid X receptor (RXR) and Ultraspiracle (USP): This family includes two evolutionary related nuclear receptors: retinoid X receptor (RXR) and Ultraspiracle (USP). RXR is a nuclear receptor in mammalian and USP is its counterpart in invertebrates. The native ligand of retinoid X receptor is 9-cis retinoic acid (RA). RXR functions as a DNA binding partner by forming heterodimers with other nuclear receptors including CAR, FXR, LXR, PPAR, PXR, RAR, TR, and VDR. RXRs can play different roles in these heterodimers. It acts either as a structural component of the heterodimer complex, required for DNA binding but not acting as a receptor or as both a structural and a functional component of the heterodimer, allowing 9-cis RA to signal through the corresponding heterodimer. In addition, RXR can also form homodimers, functioning as a receptor for 9-cis RA, independently of other nuclear receptors. Ultraspiracle (USP) plays similar roles as DNA binding partner of other nuclear rec eptors in invertebrates. USP has no known high-affinity ligand and is thought to be a silent component in the heterodimeric complex with partner receptors. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, RXR and USP have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
DMPIERILEAELAVEPKSEAVAMVPPEYRDPVSNICQAADKQLFQLVEWAKRIPHFSELPLDDQVILLRA
GWNELLIAAFAHRSIAVKDGILLATGLHLHRNSAHQAGVGAIFDRILTELVVKMRDLKMDRTELGCLRAI
ILFNPDVKGLKSRQEVESLREKVYASLEEYCRQKHPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFK
>gnl|CDD|132742 cd06944, NR_LBD_Ftz-F1_like, The ligand binding domain of FTZ-F1 like nuclear receptors. The ligand binding domain of FTZ-F1 like nuclear receptors: This nuclear receptor family includes at least three subgroups of receptors that function in embryo development and differentiation, and other processes. FTZ-F1 interacts with the cis-acting DNA motif of ftz gene, which required at several stages of development. Particularly, FTZ-F1 genes are strongly linked to steroid biosynthesis and sex-determination; LRH-1 is a regulator of bile-acid homeostasis, steroidogenesis, reverse cholesterol transport and the initial stages of embryonic development. SF-1 is an essential regulator of endocrine development and function and is considered a master regulator of reproduction; SF-1 functions cooperatively with other transcription factors to modulate gene expression. Phospholipids have been identified as potential ligand for LRH-1 and steroidogenic factor-1 (SF-1). However, the ligand for FTZ-F1 has not yet been identified. Most nuclear receptors function as homodimer or heterodimers. However, LRH-1 and SF-1 bind to DNA as a monomer. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, receptors in this family have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
VPLLILELLQCEPDERQVQARIFALLQQETYNRGEELDTFGLMCKMADQTLFSIVEWARNSVFFKELKVD
DQMKLLQNCWSELLVLDHIYRQVHHGKEDSILLVTGQEVDLSTLASQAGLGLSSLVDRAQELVNKLRELQ
FDRQEFVCLKFLILFNPDVKGLENRQLVESVQEQVNAALLDYTLCNYPQQTDKFGQLLLRLPEIRAISMQ
AEEYLYYKHLNGEVPCNNLLIEMLHAK
>gnl|CDD|132743 cd06945, NR_LBD_Nurr1_like, The ligand binding domain of Nurr1 and related nuclear receptor proteins, members of nuclear receptor superfamily. The ligand binding domain of nuclear receptor Nurr1_like: This family of nuclear receptors, including Nurr1, Nerve growth factor-induced-B (NGFI-B) and DHR38 are involved in the embryo development. Nurr1 is a transcription factor that is expressed in the embryonic ventral midbrain and is critical for the development of dopamine (DA) neurons. Structural studies have shown that the ligand binding pocket of Nurr1 is filled by bulky hydrophobic residues, making it unable to bind to ligands. Therefore, it belongs to the class of orphan receptors. However, Nurr1 forms heterodimers with RXR and can promote signaling via its partner, RXR. NGFI-B is an early immediate gene product of embryo development that is rapidly produced in response to a variety of cellular signals including nerve growth factor. It is involved in T-cell-mediated apoptosis, as well as neuronal differentiation and function. NGFI-B regulates transcription by binding to a specific DNA target upstream of its target genes and regulating the rate of tr anscriptional initiation. Another group of receptor in this family is DHR38. DHR38 is the Drosophila homolog to the vertebrate NGFI-B-type orphan receptor. It interacts with the USP component of the ecdysone receptor complex, suggesting that DHR38 might modulate ecdysone-triggered signals in the fly, in addition to the ECR/USP pathway. Nurr1_like proteins exhibit a modular structure that is characteristic for nuclear receptors; they have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
PVSLITALVRAHVDSTPRKTDLDYSKIQENVDPVPPKPDSQQVQQFYDLLTGSVDVIRQWAEKIPGFKDL
HREDQDLLLESAFLELFVLRLAYRSNPVDGKLVFCNGLVLHRLQCVRGFGEWLDSILAFSSSLQSLLLDD
ISAFCCLALLLLITERHGLKEPKKVEELQNKIISCLRDHVTSNYPGQDKPNRLSKLLLKLPELRTLSKKG
LQRIFFLKLEDLLPPPPLIDKRFLDTLPF
>gnl|CDD|132744 cd06946, NR_LBD_ERR, The ligand binding domain of estrogen receptor-related nuclear receptors. The ligand binding domain of estrogen receptor-related receptors (ERRs): The family of estrogen receptor-related receptors (ERRs), a subfamily of nuclear receptors, is closely related to the estrogen receptor (ER) family, but it lacks the ability to bind estrogen. ERRs can interfere with the classic ER-mediated estrogen signaling pathway, positively or negatively. ERRs share target genes, co-regulators and promoters with the estrogen receptor (ER) family. There are three subtypes of ERRs: alpha, beta and gamma. ERRs bind at least two types of DNA sequence, the estrogen response element and another site, originally characterized as SF-1 (steroidogenic factor 1) response element. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, ERR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
ILSHLLVAEPDKLFAMPDPALPDSDIKALTTLSDLADRELVVIIGWAKHIPGFSSLSLNDQMSLLQSAWM
EILTLGVVFRSLPFNGELVFAEDFILDEELAREAGLLELYSACLQLVRRLQRLRLEKEEYVLLKALALAN
SDSVHIEDVEAVRQLRDALLEALSDYEAGRHPGEAPRRAGQLLLTLPLLRQTDGKARRFFYGVKREGKVP
MHKLFLEMLEA
>gnl|CDD|132745 cd06947, NR_LBD_GR_Like, Ligand binding domain of nuclear hormone receptors:glucocorticoid receptor, mineralocorticoid receptor, progesterone receptor, and androgen receptor. The ligand binding domain of GR_like nuclear receptors: This family of NRs includes four distinct, but closely related nuclear hormone receptors: glucocorticoid receptor (GR), mineralocorticoid receptor (MR), progesterone receptor (PR), and androgen receptor (AR). These four receptors play key roles in some of the most fundamental physiological functions such as the stress response, metabolism, electrolyte homeostasis, immune function, growth, development, and reproduction. The NRs in this family use multiple signaling pathways and share similar functional mechanisms. The dominant signaling pathway is via direct DNA binding and transcriptional regulation of target genes. Another mechanism is via protein-protein interactions, mainly with other transcription factors such as nuclear factor-kappaB and activator protein-1, to regulate gene expression patterns. Both pathways can up-regulate or down-regulate gene expression and require ligand activation of the receptor and recruitment of other cofactors such as chaperone proteins and coregulator proteins. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, GR, MR, PR, and AR share the same modular structure with a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
SLLSVLEAIEPEVVYAGYDNSQPDTTARLLSSLNRLGERQLVSVVKWAKALPGFRNLHLDDQMTLIQYSW
MSLMVFALGWRSYKHVNSQMLYFAPDLVFNEQRMHQSAMYSLCLGMRQISQEFVRLQVTYEEFLCMKVLL
LLSTIPKDGLKSQAAFDEMRMNYIKELRKAIVKREKNSSQSWQRFYQLTKLLDSMHDLVKNLLQFCFYTF
IQSHALSVEFPEMLVEIISDQLPKVLSGNVKPLYFH
>gnl|CDD|132746 cd06948, NR_LBD_COUP-TF, Ligand binding domain of chicken ovalbumin upstream promoter transcription factors, a member of the nuclear receptor family. The ligand binding domain of chicken ovalbumin upstream promoter transcription factors (COUP-TFs): COUP-TFs are orphan members of the steroid/thyroid hormone receptor superfamily. They are expressed in many tissues and are involved in the regulation of several important biological processes, such as neurogenesis, organogenesis, cell fate determination, and metabolic homeostasis. In mammals two isoforms named COUP-TFI and COUP-TFII have been identified. Both genes show an exceptional homology and overlapping expression patterns, suggesting that they may serve redundant functions. Although COUP-TF was originally characterized as a transcriptional activator of the chicken ovalbumin gene, COUP-TFs are generally considered to be repressors of transcription for other nuclear hormone receptors, such as retinoic acid receptor (RAR), thyroid hormone receptor (TR), vitamin D receptor (VDR), peroxisome proliferator activated receptor (PPAR), and hepatocyte nuclear factor 4 (HNF4). Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, COUP-TFs have a central well cons erved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
YLSSYISLLLRAEPYPTSRYGSQCQPNNIMGIDNICELAARLLFSAVEWARNIPFFPDLQVTDQVALLRL
SWSELFVLNAAQCCMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEFSCLKA
IVLFTSDACGLSDPAHIESLQEKSQCALEEYVRTQYPNQPTRFGKLLLRLPSLRTVSSSVIEQLFFVRLV
GKTPIETLIRDMLLSGSSFVWPYLPG
>gnl|CDD|132747 cd06949, NR_LBD_ER, Ligand binding domain of Estrogen receptor, which are activated by the hormone 17beta-estradiol (estrogen). The ligand binding domain (LBD) of Estrogen receptor (ER): Estrogen receptor, a member of nuclear receptor superfamily, is activated by the hormone estrogen. Estrogen regulates many physiological processes including reproduction, bone integrity, cardiovascular health, and behavior. The main mechanism of action of the estrogen receptor is as a transcription factor by binding to the estrogen response element of target genes upon activation by estrogen and then recruiting coactivator proteins which are responsible for the transcription of target genes. Additionally some ERs may associate with other membrane proteins and can be rapidly activated by exposure of cells to estrogen. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, ER has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD). The C-terminal LBD also contains AF-2 activation motif, the dimerization motif, and part of the nuclear localization region. Estrogen receptor has been linked to aging, cancer, obesity and other diseases
LSAEQLISALLEAEPPHIYSEYDPTRPFTEASLMMLLTNLADRELVHMINWAKKIPGFVDLSLHDQVHLL
ESAWLELLMLGLVWRSMEHPGKLLFAPDLLLDRNQGSCVEGMVEIFDMLLATASRFRELQLQREEYVCLK
AIILLNSSVYTFLLESLESRRQVQRLLDKITDALVHACSKRGLSLQQQSRRLAQLLLILSHIRHVSNKGM
EHLYSMKCKNVVPLYDLLLEMLDAH
>gnl|CDD|132748 cd06950, NR_LBD_Tlx_PNR_like, The ligand binding domain of Tailless-like proteins, orphan nuclear receptors. The ligand binding domain of the photoreceptor cell-specific nuclear receptor (PNR) like family: This family includes photoreceptor cell-specific nuclear receptor (PNR), Tailless (TLX), and related receptors. TLX is an orphan receptor that is expressed by neural stem/progenitor cells in the adult brain of the subventricular zone (SVZ) and the dentate gyrus (DG). It plays a key role in neural development by promoting cell cycle progression and preventing apoptosis in the developing brain. PNR is expressed only in the outer layer of retinal photoreceptor cells. It may be involved in the signaling pathway regulating photoreceptor differentiation and/or maintenance. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, TLX and PNR have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
GEEIDVAQPTPKRPPFPYGTISSYEVSPESVCESAARLLFMAVKWAKSIPAFSTLPFRDQLILLEESWSE
LFLLGAAQWSLPLDSCPLLAVPGLSPDNTEAERTFLSEVRALQETLSRFRQLRVDATEFACLKAIVLFKP
ETRGLKDPAQVEALQDQAQLMLNKHIRTRYPTQPARFGKLLLLLPSLRFISSSTIEELFFKKTIGN
>gnl|CDD|132749 cd06951, NR_LBD_Dax1_like, The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain. The ligand binding domain of DAX1-like proteins: This orphan nuclear receptor family includes DAX1 (dosage-sensitive sex reversal adrenal hypoplasia congenita critical region on chromosome X gene 1) and the Small Heterodimer Partner (SHP). Both receptors have a typical ligand binding domain, but lack the DNA binding domain, typical to almost all of the nuclear receptors. They function as a transcriptional coregulator by directly interacting with other nuclear receptors. DAX1 and SHP can form heterodimers with each other, as well as with many other nuclear receptors. In addition, DAX1 can also form homodimers. DAX1 plays an important role in the normal development of several hormone-producing tissues. SHP has shown to regulate a variety of target genes
ATAPHRLASCHQHRPVQLCAPQMVCRAASQVLLKTIRFVRNLPCFTYLPPDDQLRLLRRSWAPLLLLGLA
QDKVPFDTVEVPAPSILCEILTGAEMHWGGTPPPTLTMPPCIPLADVQDIQQFLMKCWSLDLDCKEYAYL
KGAVLFTPVPPLLCPHYIEALQKEAQQALNEHTMMTRPLEQLRSARLLLMLSLLRGIKTEPVTELFFRPI
IGNVSMDDVLLQ
>gnl|CDD|132750 cd06952, NR_LBD_TR2_like, The ligand binding domain of the orphan nuclear receptors TR4 and TR2. The ligand binding domain of the TR4 and TR2 (human testicular receptor 4 and 2): TR4 and TR2 are orphan nuclear receptors. Several isoforms of TR4 and TR2 have been isolated in various tissues. TR2 is abundantly expressed in the androgen-sensitive prostate. TR4 transcripts are expressed in many tissues, including central nervous system, adrenal gland, spleen, thyroid gland, and prostate. The expression of TR2 is negatively regulated by androgen, retinoids, and radiation. The expression of both mouse TR2 and TR4 is up-regulated by neurocytokine ciliary neurotrophic factor (CNTF) in mouse. It has shown that human TR2 binds to a wide spectrum of natural hormone response elements (HREs) with distinct affinities suggesting that TR2 may cross-talk with other gene expression regulation systems. The genes responding to TR2 or TR4 include genes that are regulated by retinoic acid receptor, vitamin D receptor, peroxisome proliferator-activated receptor. TR4/2 binds to HREs as a dimer. Like other members of the nuclea r receptor (NR) superfamily of ligand-activated transcription factors, TR2-like receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
LLTDVHVAFKLQMPSPMPSYLNVHYICESASRLLFLSIHWARSIPAFQALGAETQTSLVRACWPELFTLG
LAQCSQQLSLPTILAAIINHLQTSIQQDKLSADKVKQVMEHINKLQEFVNSMQKLDVDDHEYAYLKAIVL
FSPDHPGQELRQQIEKLQEKALMELRDYVGKTYPEDEYRLSKLLLRLPPLRSLSPAITEELFFAGLIGNV
QIDSVIPYILRM
>gnl|CDD|132751 cd06953, NR_LBD_DHR4_like, The ligand binding domain of orphan nuclear receptor Ecdysone-induced receptor DHR4. The ligand binding domain of Ecdysone-induced receptor DHR4: Ecdysone-induced orphan receptor DHR4 is a member of the nuclear receptor family. DHR4 is expressed during the early Drosophila larval development and is induced by ecdysone. DHR4 coordinates growth and maturation in Drosophila by mediating endocrine response to the attainment of proper body size during larval development. Mutations in DHR4 result in shorter larval development which translates into smaller and lighter flies. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, DHR4 has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
QLLVAEDLEPLITPMLIEDGATVDQAELFALLCRLGDELLFRQIQWTKKLPFFTELSIKDHTHLLTTKWA
ELILLSTITVASLQNLGLLQDCLSKYLPSEDELERFGDEGGEVVERLTYLLAKFRQLKVSNEEYVCLKVI
NFLNQDIDGLTNASQLESLQKRYWYVLQDFTELNYPNQPNRFSDLLSCLPEIRAAAGKLLHSKLFYLPLL
FKA
>gnl|CDD|132752 cd06954, NR_LBD_LXR, The ligand binding domain of Liver X receptors, a family of nuclear receptors of ligand-activated transcription factors. The ligand binding domain of Liver X receptors: Liver X receptors (LXRs) belong to a family of nuclear receptors of ligand-activated transcription factors. LXRs operate as cholesterol sensors which protect from cholesterol overload by stimulating reverse cholesterol transport from peripheral tissues to the liver and its excretion in the bile. Oxidized cholesterol derivatives or oxysterols were identified as specific ligands for LXRs. Upon ligand binding a conformational change leads to recruitment of co-factors, which stimulates expression of target genes. Among the LXR target genes are several genes involved in cholesterol efflux from peripheral tissues such as the ATP-binding-cassette transporters ABCA1, ABCG1 and ApoE. There are two LXR isoforms in mammals, LXRalpha and LXRbeta. LXRalpha is expressed mainly in the liver, intestine, kidney, spleen, and adipose tissue, whereas LXRbeta is ubiquitously expressed at lower level. Both LXRalpha and LXRbeta function as heterodimers with the retinoid X receptor (RX R) which may be activated by either LXR ligands or 9-cis retinoic acid, a specific RXR ligand. The LXR/RXR complex binds to a liver X receptor response element (LXRE) in the promoter region of target genes. LXR has typical NR modular structure with a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and the ligand binding domain (LBD) at the C-terminal
QREMIEQLVAAQQQCNKRSFEDVPKVTPWPEGQDPQSREARQQRFAHFTELAILSVQEIVDFAKQLPGFL
TLTREDQIALLKASTIEVMLLETARRYNPESEAITFLKDFPYSRDDFARAGLQVEFINPIFEFSKSMREL
QLDDAEYALLIAINIFSADRPNVQDHHRVERLQETYVEALHSYIKIKRPSDRLMFPRMLMKLVSLRTLSS
VHSEQVFALRLQDKKLPPLLSEIWDV
>gnl|CDD|143513 cd06955, NR_DBD_VDR, DNA-binding domain of vitamin D receptors (VDR) is composed of two C4-type zinc fingers. DNA-binding domain of vitamin D receptors (VDR) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. VDR interacts with a VDR response element, a direct repeat of GGTTCA DNA site with 3 bp spacer upstream of the target gene, and modulates the rate of transcriptional initiation. VDR is a member of the nuclear receptor (NR) superfamily that functions as classical endocrine receptors. VDR controls a wide range of biological activities including calcium metabolism, cell proliferation and differentiation, and immunomodulation. VDR is a high-affinity receptor for the biologically most active Vitamin D metabolite, 1alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)2D3). The binding of the ligand to the receptor induces a conformational change of the ligand binding domain (LBD) with consequent dissociation of corepressors. Upon ligand binding, VDR forms a heterodimer with the retinoid X receptor (RXR) that binds to vitamin D response elements (VDREs), recruits coactivators. This leads to the expression of a large number of genes. Approximately 200 human genes are considered to be primary targets of VDR and even more genes are regulated indirectly. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, VDR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
FDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCV
DIGMMKEFILTDEEVQRKREMILKRKEEEALKESLRP
>gnl|CDD|143514 cd06956, NR_DBD_RXR, DNA-binding domain of retinoid X receptor (RXR) is composed of two C4-type zinc fingers. DNA-binding domain of retinoid X receptor (RXR) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. RXR functions as a DNA binding partner by forming heterodimers with other nuclear receptors including CAR, FXR, LXR, PPAR, PXR, RAR, TR, and VDR. All RXR heterodimers preferentially bind response elements composed of direct repeats of two AGGTCA sites with a 1-5 bp spacer. RXRs can play different roles in these heterodimers. RXR acts either as a structural component of the heterodimer complex, required for DNA binding but not acting as a receptor, or as both a structural and a functional component of the heterodimer, allowing 9-cis RA to signal through the corresponding heterodimer. In addition, RXR can also form homodimers, functioning as a receptor for 9-cis RA, independently of other nuclear receptors. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, RXR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
HICAICGDRASGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLIDKRQRNRCQYCRYQKCLAMGMKR
EAVQEER
>gnl|CDD|143515 cd06957, NR_DBD_PNR_like_2, DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) like is composed of two C4-type zinc fingers. The DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) nuclear receptor-like family is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. PNR interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. This family includes nuclear receptor Tailless (TLX), photoreceptor cell-specific nuclear receptor (PNR) and related receptors. TLX is an orphan receptor that plays a key role in neural development by regulating cell cycle progression and exit of neural stem cells in the developing brain. PNR is expressed only in the outer layer of retinal photoreceptor cells. It may be involved in the signaling pathway regulating photoreceptor differentiation and/or maintenance. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, PNR-like receptors have a central well-conserved DNA-binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
CKVCGDKSYGKHYGVYCCDGCSCFFKRSVRKGIIYTCIAGNGNCVVDKARRNWCPFCRLQKCFAVGMNRA
AVQEERGPRKLR
>gnl|CDD|143516 cd06958, NR_DBD_COUP_TF, DNA-binding domain of chicken ovalbumin upstream promoter transcription factors (COUP-TFs) is composed of two C4-type zinc fingers. DNA-binding domain of chicken ovalbumin upstream promoter transcription factors (COUP-TFs) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. COUP-TFs are orphan members of the steroid/thyroid hormone receptor superfamily. They are expressed in many tissues and are involved in the regulation of several important biological processes, such as neurogenesis, organogenesis, cell fate determination, and metabolic homeostasis. COUP-TFs homodimerize or heterodimerize with retinoid X receptor (RXR) and a few other nuclear receptors and bind to a variety of response elements that are composed of imperfect AGGTCA direct or inverted repeats with various spacings. COUP-TFs are generally considered to be repressors of transcription for other nuclear hormone receptors such as retinoic acid receptor (RAR), thyroid hormone receptor (TR), vitamin D receptor (VDR), peroxisome proliferator activated receptor (PPAR), and hepatocyte nuclear factor 4 (HNF4). Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, COUP-TFs have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
CVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLTYTCRGNRNCPIDQHHRNQCQYCRLKKCLKVGMRREA
VQR
>gnl|CDD|143517 cd06959, NR_DBD_EcR_like, The DNA-binding domain of Ecdysone receptor (EcR) like nuclear receptor family is composed of two C4-type zinc fingers. The DNA-binding domain of Ecdysone receptor (EcR) like nuclear receptor family is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. EcR interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. This family includes three types of nuclear receptors: Ecdysone receptor (EcR), Liver X receptor (LXR) and Farnesoid X receptor (FXR). The DNA binding activity is regulated by their corresponding ligands. The ligands for EcR are ecdysteroids; LXR is regulated by oxidized cholesterol derivatives or oxysterols; and bile acids control FXR's activities. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, EcR-like receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
NCVVCGDKASGFHYGVLSCEGCKGFFRRSVTKGAVYACKFGNKCEMDMYMRRKCQECRLRKCKAAGMRPD
CLL
>gnl|CDD|143518 cd06960, NR_DBD_HNF4A, DNA-binding domain of heptocyte nuclear factor 4 (HNF4) is composed of two C4-type zinc fingers. DNA-binding domain of hepatocyte nuclear factor 4 (HNF4) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. HNF4 interacts with a DNA site, composed of two direct repeats of AGTTCA with 1 bp spacer, which is upstream of target genes and modulates the rate of transcriptional initiation. HNF4 is a member of the nuclear receptor superfamily. HNF4 plays a key role in establishing and maintenance of hepatocyte differentiation in the liver. It is also expressed in gut, kidney, and pancreatic beta cells. HNF4 was originally classified as an orphan receptor, but later it is found that HNF4 binds with very high affinity to a variety of fatty acids. However, unlike other nuclear receptors, the ligands do not act as a molecular switch for HNF4. They seem to constantly bind to the receptor, which is constitutively active as a transcription activator. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, HNF4 has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
CAVCGDRATGKHYGVLSCNGCKGFFRRSVRKNRTYTCRFGGNCVVDKDKRNACRYCRFKKCLEVGMDPEA
VQNERD
>gnl|CDD|143519 cd06961, NR_DBD_TR, DNA-binding domain of thyroid hormone receptors (TRs) is composed of two C4-type zinc fingers. DNA-binding domain of thyroid hormone receptors (TRs) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. TR interacts with the thyroid response element, which is a DNA site with direct repeats of the consensus sequence 5'-AGGTCA-3' separated by one to five base pairs, upstream of target genes and modulates the rate of transcriptional initiation. Thyroid hormone receptor (TR) mediates the actions of thyroid hormones, which play critical roles in growth, development, and homeostasis in mammals. They regulate overall metabolic rate, cholesterol and triglyceride levels, and heart rate, and affect mood. TRs are expressed from two separate genes (alpha and beta) in human and each gene generates two isoforms of the receptor through differential promoter usage or splicing. TRalpha functions in the heart to regulate heart rate and rhythm and TRbeta is active in the liver and other tissues. The unliganded TRs function as transcription repressors, by binding to thyroid hormone response elements (TRE) predominantly as homodimers, or as heterodimers with retinoid X-receptors (RXR), and being associated with a complex of proteins containing corepressor proteins. Ligand binding promotes corepressor dissociation and binding of a coactivator to activate transcription. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, TR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
PCVVCGDKATGYHYRCITCEGCKGFFRRTVQKKLSYSCKGEGKCEIDKVTRNQCQECRFKKCIAVGMAKD
LVLDDRKRGAKRKLI
>gnl|CDD|143520 cd06962, NR_DBD_FXR, DNA-binding domain of Farnesoid X receptor (FXR) family is composed of two C4-type zinc fingers. DNA-binding domain of Farnesoid X receptor (FXR) family is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. FXR interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. FXR is a member of the nuclear receptor family of ligand activated transcription factors. Bile acids are endogenous ligands for FXRs. Upon binding of a ligand, FXR binds to FXR response element (FXRE), which is an inverted repeat of TGACCT spaced by one nucleotide, either as a monomer or as a heterodimer with retinoid X receptor (RXR), to regulate the expression of various genes involved in bile acid, lipid, and glucose metabolism. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, FXR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
EELCVVCGDKASGYHYNALTCEGCKGFFRRSITKNAVYKCKNGGNCEMDMYMRRKCQECRLRKCKEMGML
AECLLTEIQCKSKR
>gnl|CDD|143521 cd06963, NR_DBD_GR_like, The DNA binding domain of GR_like nuclear receptors is composed of two C4-type zinc fingers. The DNA binding domain of GR_like nuclear receptors is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. It interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. This family of NRs includes four types of nuclear hormone receptors: glucocorticoid receptor (GR), mineralocorticoid receptor (MR), progesterone receptor (PR), and androgen receptor (AR). The receptors bind to common DNA elements containing a partial palindrome of the core sequence 5'-TGTTCT-3' with a 3bp spacer. These four receptors regulate some of the most fundamental physiological functions such as the stress response, metabolism, electrolyte homeostasis, immune function, growth, development, and reproduction. The NRs in this family have high sequence homology and share similar functional mechanisms. The dominant mechanism of function is by direct DNA binding and transcriptional regulation of target genes . The GR, MR, PR, and AR exhibit same modular structure. They have a central highly conserved DNA binding domain (DBD), a non-conserved N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
CLICGDEASGCHYGVLTCGSCKVFFKRAAEGQHNYLCAGRNDCIIDKIRRKNCPACRLRKCYQAGMTLGA
RKL
>gnl|CDD|143522 cd06964, NR_DBD_RAR, DNA-binding domain of retinoic acid receptor (RAR) is composed of two C4-type zinc fingers. DNA-binding domain of retinoic acid receptor (RAR) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. RAR interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. RARs mediate the biological effect of retinoids, including both natural dietary vitamin A (retinol) metabolites and active synthetic analogs. Retinoids play key roles in a wide variety of essential biological processes, such as vertebrate embryonic morphogenesis and organogenesis, differentiation and apoptosis, and homeostasis. RAR function as a heterodimer with retinoic X receptor by binding to specific RAR response elements (RAREs), which are composed of two direct repeats of the consensus sequence 5'-AGGTCA-3' separated by one to five base pair and found in the promoter regions of retinoid target genes. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, retinoic acid receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
PRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEV
GMSKESVRNDRNKKK
>gnl|CDD|143523 cd06965, NR_DBD_Ppar, DNA-binding domain of peroxisome proliferator-activated receptors (PPAR) is composed of two C4-type zinc fingers. DNA-binding domain of peroxisome proliferator-activated receptors (PPAR) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. PPAR interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. Peroxisome proliferator-activated receptors (PPARs) are members of the nuclear receptor superfamily of ligand-activated transcription factors. PPARs play important roles in regulating cellular differentiation, development and lipid metabolism. Activated PPAR forms a heterodimer with the retinoid X receptor (RXR) that binds to the hormone response elements, which are composed of two direct repeats of the consensus sequence 5'-AGGTCA-3' separated by one to five base pair located upstream of the peroxisome proliferator responsive genes, and interacts with co-activators. Several essential fatty acids, oxidized lipids and prostaglandin J derivatives can bind and activate PPAR. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, PPAR has a central well conserved DNA binding domain (DBD), a variable N-terminal regulatory domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
ECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLVYKPCDLSCKIHKKSRNKCQYCRFQKCLNVGMSHNA
IRFGRMPRVEKEKL
>gnl|CDD|143524 cd06966, NR_DBD_CAR, DNA-binding domain of constitutive androstane receptor (CAR) is composed of two C4-type zinc fingers. DNA-binding domain (DBD) of constitutive androstane receptor (CAR) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. CAR DBD interacts with CAR response element, a perfect repeat of two AGTTCA motifs with a 4 bp spacer upstream of the target gene, and modulates the rate of transcriptional initiation. The constitutive androstane receptor (CAR) is a ligand-regulated transcription factor that responds to a diverse array of chemically distinct ligands, including many endogenous compounds and clinical drugs. It functions as a heterodimer with RXR. The CAR/RXR heterodimer binds many common response elements in the promoter regions of a diverse set of target genes involved in the metabolism, transport, and ultimately, elimination of these molecules from the body. CAR is a closest mammalian relative of PXR and is activated by some of the same ligands as PXR and regulates a subset of common genes. The sequence homology and functional similarity suggests that the CAR gene arose from a duplication of an ancestral PXR gene. Like other nuclear receptors, CAR has a central well conserved DNA binding domain, a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain
KICGVCGDKALGYNFNAITCESCKAFFRRNALKNKEFKCPFNESCEINVVTRRFCQKCRLDKCFAIGMKK
EWIMSEEDKSEKRQKIEENRAKKR
>gnl|CDD|143525 cd06967, NR_DBD_TR2_like, DNA-binding domain of the TR2 and TR4 (human testicular receptor 2 and 4) is composed of two C4-type zinc fingers. DNA-binding domain of the TR2 and TR4 (human testicular receptor 2 and 4) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. TR2 and TR4 interact with specific DNA sites upstream of the target gene and modulate the rate of transcriptional initiation. TR4 and TR2 are orphan nuclear receptors; the physiological ligand is as yet unidentified. TR2 is abundantly expressed in the androgen-sensitive prostate. TR4 transcripts are expressed in many tissues, including central nervous system, adrenal gland, spleen, thyroid gland, and prostate. It has been shown that human TR2 binds to a wide spectrum of natural hormone response elements (HREs) with distinct affinities suggesting that TR2 may cross-talk with other gene expression regulation systems. The genes responding to TR2 or TR4 include genes that are regulated by retinoic acid receptor, vitamin D receptor, and peroxisome proliferator-activated receptor. TR4/2 binds to HREs as dimers. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, TR2-like receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
QPVELCVVCGDKASGRHYGAVSCEGCKGFFKRSIRKNLGYSCRGSKDCVINKHHRNRCQYCRLQKCLAMG
MKSDSVQCERKPIDVSR
>gnl|CDD|143526 cd06968, NR_DBD_ROR, DNA-binding domain of Retinoid-related orphan receptors (RORs) is composed of two C4-type zinc fingers. DNA-binding domain of Retinoid-related orphan receptors (RORs) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. ROR interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. RORS are key regulators of many physiological processes during embryonic development. RORs bind as monomers to specific ROR response elements (ROREs) consisting of the consensus core motif AGGTCA preceded by a 5-bp A/T-rich sequence. There are three subtypes of retinoid-related orphan receptors (RORs), alpha, beta, and gamma, which differ only in N-terminal sequence and are distributed in distinct tissues. RORalpha plays a key role in the development of the cerebellum particularly in the regulation of the maturation and survival of Purkinje cells. RORbeta expression is largely restricted to several regions of the brain, the retina, and pineal gland. RORgamma is essential for lymph node organogenesis. Recently, it has been suggested that cholesterol or a cholesterol derivative are the natural ligands of RORalpha. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, retinoid-related orphan receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
AQIEVIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQNNVSYSCPRQKNCLIDRTNRNRCQHCRLQKCLA
LGMSRDAVKFGRMSKKQRDSLYAEV
>gnl|CDD|143527 cd06969, NR_DBD_NGFI-B, DNA-binding domain of the orphan nuclear receptor, nerve growth factor-induced-B. DNA-binding domain (DBD) of the orphan nuclear receptor, nerve growth factor-induced-B (NGFI-B) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. NGFI-B interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. NGFI-B is a member of the nuclear-steroid receptor superfamily. NGFI-B is classified as an orphan receptor because no ligand has yet been identified. NGFI-B is an early immediate gene product of embryo development that is rapidly produced in response to a variety of cellular signals including nerve growth factor. It is involved in T-cell-mediated apoptosis, as well as neuronal differentiation and function. NGFI-B regulates transcription by binding to a specific DNA target upstream of its target genes and regulating the rate of transcriptional initiation. NGFI-B binds to the NGFI-B response element (NBRE) 5'-(A/T)AAAGGTCA as a monomer. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, NGFI-B has a central well-conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
GLCAVCGDNAACQHYGVRTCEGCKGFFKRTVQKNAKYVCLANKNCPVDKRRRNRCQYCRFQKCLQVGMVK
EVVRT
>gnl|CDD|143528 cd06970, NR_DBD_PNR, DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) is composed of two C4-type zinc fingers. DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. PNR interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. PNR is a member of the nuclear receptor superfamily of the ligand-activated transcription factors. PNR is expressed only in the outer layer of retinal photoreceptor cells. It may be involved in the signaling pathway regulating photoreceptor differentiation and/or maintenance. It most likely binds to DNA as a homodimer. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, PNR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
KGLNPGLLCRVCGDTSSGKHYGIYACNGCSGFFKRSVRRKLIYRCQAGTGMCPVDKAHRNQCQACRLKKC
LQAGMNKDAVQNERQPRNTAQV
>gnl|CDD|133477 cd06971, PgpA, Phosphatidylglycerophosphatase A; a bacterial membrane-associated enzyme involved in lipid metabolism. Phosphatidylglycerophosphatase A domain represents a family of bacterial membrane-associated enzymes involved in lipid metabolism. The prototype of this CD is a putative Phosphatidylglycerophosphatase A (PGPase A) from Listeria monocytogenes. PGPase A (EC: 3.1.3.27), encoded by the gene pgpA, specifically catalyzes the formation of phosphatidylglycerol from phosphatidyl glycerophosphate (PGP). It requires Mg2+ for activity and is inhibited by sulfhydryl agents and freezing/thawing. PGPase B encoded from pgpB is not included in this family, which also acts on phosphatidic acid (PA) and lysophosphatidic acid (LPA). Aside from PGPase A and B, evidence shows that there is another PGPase existing in E. coli. Thus, PGPase A is not essential for PGPase activity in E. coli
AHFLATGFGSGLSPIAPGTFGSLAALPLELLLSELGKVLLELLALLLAFLLGIWAAEKTLKDLGVHDPGE
IVIDEVVGQWIALLIVPFGWLWGLLAFLLFRFFDIVKPGPIGWLDRKVKGGLGVMLDDILAGLYAALVLR
LLL
>gnl|CDD|132992 cd06974, TerD_like, Uncharacterized proteins involved in stress response, similar to tellurium resistance terD. Tellurium resistance terD like proteins. This family is composed of uncharacterized proteins involved in stress response, such as the tellurium resistance proteins, chemical-damaging agent resistance proteins, and general stress proteins from a variety of organisms. The tellurium resistance proteins are homologous terA,-D,-E,-F,-Z,-X gene products, which confer tellurium resistance mediated by plasmids. Currently, the biochemical mechanism of tellurium resistance remains unknown. The family also contains several ter gene homologues, YceC, YceD, YceE, for which there is no clear evidence for any involvement in the tellurium resistance. A putative cAMP-binding protin CABP1 shows a significant similarity to the terD protein and is also included in this family
LSKVRVGLGWDPGSTGGGIDLDLSAFLLDADGKVRGDADVVFYNQLSSPDGAVRLSGDNRTGGDGDDETI
TVDLDRLPPDIRRIVFTVTIYEGQPFGQVENAFVRLVDAGGNTELARYDLTEDSGETALILAELYRRNGE
WKFRAVGQGFNGGLAALATHYG
>gnl|CDD|380380 cd06975, cupin_BacB, Bacillus subtilis bacilysin and related proteins, cupin domain. Bacilysin (BacB, also known as AerE in Microcystis aeruginosa) is a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. It is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa
KTIKLETGVELQFFVGSWTEIMLSYIPPGAKMPLHQHREEQIGMILNGELEMTVGGEEQELEPLGDVYYA
PPNVPHGAVNPSDETAVLLDIKR
>gnl|CDD|380381 cd06976, cupin_MtlR-like_N, AraC/XylS family transcriptional regulators similar to MtlR, N-terminal cupin domain. MtlR is a Pseudomonas fluorescens protein that acts as a transcriptional regulator of the mannitol utilization genes. It has an N-terminal cupin domain (represented by this alignment) and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
SSFRVRRHDYPYFPAPWHFHPEYELTLIVKGSGTRFVGDHIGNFEPGDLVLIGPNLPHTWKSDEEYGEDL
RARAIVIQFSEDF
>gnl|CDD|380382 cd06977, cupin_RhaR_RhaS-like_N, HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain. Members of this family contain an N-terminal cupin domain and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain, including the HTH-type transcription activators RhaS and RhaR. RhaS and RhaR respond to the availability of L-rhamnose and activate transcription of the operons in the Escherichia coli L-rhamnose catabolic regulon. The E. coli RhaR protein activates expression of the rhaSR operon in the presence of its effector, L-rhamnose. The resulting RhaS protein (plus L-rhamnose) activates expression of the L-rhamnose catabolic operon rhaBAD as well as the transport operon rhaT. These proteins bind DNA as dimers, via their HTH motifs. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
NQPVAVEPRAPQEPFPEHTHDFHEIVIVTKGSGIHVLNGHPYRITAGDVFYIRPDDRHSYESVDDLCLTN
ILFRPERLFLFLDWLDTLPGYLAHQFQSHWRLNSSTLREIRQLIDQLESELEERDAGSELMAEALFLQLL
VLLSRHR
>gnl|CDD|380383 cd06978, cupin_EctC, L-ectoine synthase, cupin domain. Ectoine synthase (EctC; also known as L-ectoine synthase or N-acetyldiaminobutyrate dehydratase; EC 4.2.1.108) is a cupin-like bacterial protein that converts N'-acetyldiaminobutyric acid to ectoine, in the last step of the L-ectoine biosynthetic pathway, via a cyclo-condensation reaction and using iron as the cofactor. Ectoines are potent microbial stress protectants, primarily synthesized by bacteria but also found in a few obligate halophilic protists and archaea, based on the ectoine biosynthetic ectABC gene. In halophilic eubacteria, the osmolytic ectoines enable the organisms to adapt to a wide range of salt concentrations by adjusting the cytoplasmic solute pool to the osmolarity of the surrounding environment. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
IVRSLEEIIGTERDVDGGNWTSRRLLLAKDGMGFSLHDTTIYAGTETRLWYKNHLEAVYCIEGEGEVEDL
ATGEVHPIEPGTLYALDKHDRHILRAHTDMRLVCVFNPPLT
>gnl|CDD|380384 cd06979, cupin_RemF-like, Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain. RemF cyclase is a manganese-containing polyketide cyclase present in bacteria that is involved in the biosynthesis of resistomycin, the aromatic pentacyclic metabolite in Streptomyces resistomycificus. Structure of this enzyme shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold that forms a homodimer. It contains an unusual octahedral zinc-binding site in a large hydrophobic pocket that may represent the active site. The zinc ion, coordinated to four histidine side chains and two water molecules, could act as a Lewis acid in the aldol condensation reaction catalyzed by RemF, reminiscent of class II aldolases
TTELRFLDTKDGTADRFDLFEFEVSPNAGMPPPHYHEDWEETIYGLEGSVTLTLPGKTVEVGPGDSIFIP
RGEVHGFVNRSGGPTCRLCVLAP
>gnl|CDD|380385 cd06980, cupin_bxe_c0505, uncharacterized protein bxe_c0505, cupin domain. This family includes mostly bacterial proteins homologous to bxe_c0505, a Burkholderia xenovorans protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
GLRAFFEYRDLGIAEATGGRVGAHVIRATGGGEGPTGWHYHDCDFQMVYVLKGWVKFEFEGGGEVRLEAG
DCVYQPPGIRHNVLDYSDDLELLEITSPAEFGTVE
>gnl|CDD|380386 cd06981, cupin_reut_a1446, Cupriavidus pinatubonensis reut_a1446 and related proteins, cupin domain. This family includes bacterial and some eukaryotic proteins homologous to reut_a1446, a Cupriavidus pinatubonensis protein of unknown function that may be related to mannose-6-phosphate isomerase. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
MGNLFDNLPDDLPEELFETLLENGGVRIERIVSTGQASPPGFWYDQDEDEWVLLLQGEAELEFEDGEEVE
LKPGDYLLIPAHCRHRVAWTSPEPPTIWLAVHY
>gnl|CDD|380387 cd06982, cupin_BauB-like, Pseudomonas aeruginosa BauB and related proteins, cupin domain. This family includes bacterial proteins homologous to beta-alanine degradation protein BauB from Pseudomonas aeruginosa, which is involved in the degradation of beta-alanine. Also included are Rhodopseudomonas palustris Rpa4178 and Bordetella pertussis Bp2299, which are both proteins with unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
QAVPTVQIDNERVRVTRWRFPPGAETGWHRHEYDYVVVPLTDGTLTIEDPDGERTASLLAGGVSYRRPAG
VEHNVINAGDAEVVFVEIELK
>gnl|CDD|380388 cd06983, cupin_dsy2733, Desulfitobacterium hafniense dsy2733 and related proteins, cupin domain. This family includes bacterial proteins homologous to dsy2733, a Desulfitobacterium hafniense protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
SMALSNSDNVQISLFAFADGESVSEEEYFGDTLYYVLEGEAEITIGDEKHRLKAGDVLAVPAGVLHAIGG
LGAFKLLQITV
>gnl|CDD|380389 cd06984, cupin_Moth_1897, uncharacterized Methanocaldococcus jannaschii Moth_1897 and related proteins, cupin domain. This family includes archaeal and bacterial proteins homologous to Moth_1897, a Methanocaldococcus jannaschii protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
KARKLYDTEHAQIVHITLKPGESLKKHITPVDVFFYVLEGEGIVEIGEEKQEVEADTLIESPANIPHCLY
NESDADLRVLVIK
>gnl|CDD|380390 cd06985, cupin_BF4112, Bacteroides fragilis BF4112 and related proteins, cupin domain. This family includes archaeal and bacterial proteins homologous to BF4112, a Bacteroides fragilis protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
GKVFLKEALGLTGAEISFNSLPAGAAVPFVHSHKENEEIYIILKGKGEFQVDGEVFPVKEGSVIRVAPDG
KRSWRNTSDEPLIYICIQAKEGSLEQYTITD
>gnl|CDD|380391 cd06986, cupin_MmsR-like_N, AraC/XylS family transcriptional regulators similar to MmsR, N-terminal cupin domain. This family contains bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included is MmsR, a bacterial transcriptional regulator thought to positively regulate the expression of the mmsAB operon. The mmsAB operon contains two structural genes involved in valine metabolism: mmsA which encodes methylmalonate-semialdehyde dehydrogenase, and mmsB which encodes 3-hydroxyisobutyrate dehydrogenase. The cupin domain of members of this subfamily does not contain a metal binding site
ISSDLYLTDCGYEPCEPGHSYGPAVRDYYILHYVLSGKGTFSVNGKTYHLKAGQGFLIPPGEPHSYGADE
DDPWTYYWIGFSGS
>gnl|CDD|380392 cd06987, cupin_MAE_RS03005, Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain. This family includes bacterial and some eukaryotic proteins homologous to MAE_RS03005, a Microcystis aeruginosa protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
DYEAFRISPGDTNRLALLFDPEGDGVPFTVVVEIFDPGGRTPPNTHPAAHEMFFVLAGEGRAYCDGQRVP
LRPGDALVVPPGSEHVIENTGSGRLYCLTLMVPNEGFAELIRSGIPAELDDE
>gnl|CDD|380393 cd06988, cupin_DddK, Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain. This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
PFGGAWCVVRPGTTSTPHSHHEYEIFIVISGKGIVVVDGEREPVKAGDVVYIPPGTEHYVKNDGDEDFEF
YSIWWD
>gnl|CDD|380394 cd06989, cupin_DRT102, Arabidopsis thaliana DRT102 and related proteins, cupin domain. This family includes bacterial and eukaryotic proteins homologous to DNA-damage-repair/toleration protein DRT102 found in Arabidopsis thaliana. DRT102 may be involved in DNA repair from UV damage. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
PPGAKAAVLEGDPSKPGPFVVRLKFPAGYKIPPHTHPDDERVTVISGTFYLGMGDKFDEAKAKALPAGSF
FTLPAGTPHFAWAKDEETVVQVTGEGP
>gnl|CDD|380395 cd06990, cupin_DUF861, domain of unknown function DUF 861, cupin domain. This family contains proteins which seem to be specific to bacteria and some fungi. The function of this family is unknown but contains a cupin domain without a metal binding site. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin (cupa is the Latin term for small barrel)
DSPDETRTFPKGKVEVVRLGGVTVGRATFEPGWRWSEHVKPIAGTDSCQAPHVGYVLSGRLRVRMDDGTE
LEFGPGDVYVIPPGHDAWVVGDEPVVALDFA
>gnl|CDD|380396 cd06991, cupin_TcmJ-like, TcmJ monooxygenase and related proteins, cupin domain. This family includes TcmJ, a subunit of the tetracenomycin (TCM) polyketide synthase (PKS) type II complex in Streptomyces glaucescens. TcmJ is a quinone-forming monooxygenase involved in the modification of aromatic polyketides synthesized by polyketide synthases of types II and III. Orthologs of TcmJ include the Streptomyces BenD (benastatin biosynthetic pathway), the Streptomyces olivaceus ElmJ (polyketide antibiotic elloramycin biosynthetic pathway), the Actinomadura hibisca PdmL (pradimicin biosynthetic pathway), the Streptomyces cyaneus CurC (curamycin biosynthetic pathway), the Streptomyces rishiriensis Lct30 (lactonamycin biosynthetic pathway), and the Streptomyces WhiE II (spore pigment polyketide biosynthetic pathway). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
RGGDLRILLSPKTVGATSGFMGTLTLAPGERVSEHYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLV
PRGVRHRLENAGDEPARLVFHLSPLAPRPELGHVD
>gnl|CDD|380397 cd06992, cupin_GDO-like_C, gentisate 1,2-dioxygenase, 1-hydroxy-2-naphthoate dioxygenase, and salicylate 1,2-dioxygenase bicupin aromatic ring-cleaving dioxygenases, C-terminal cupin domain. This model represents the C-terminal cupin domains of three closely related bicupin aromatic ring-cleaving dioxygenases: gentisate 1,2-dioxygenase (GDO), salicylate 1,2-dioxygenase (SDO), and 1-hydroxy-2-naphthoate dioxygenase (NDO). GDO catalyzes the cleavage of the gentisate (2,5-dihydroxybenzoate) aromatic ring, a key step in the gentisate degradation pathway allowing soil bacteria to utilize 2,5-xylenol, 3,5-xylenol, and m-cresol as sole carbon and energy sources. NDO catalyzes the cleavage of 1-hydroxy-2-naphthoate as part of the bacterial phenanthrene degradation pathway. SDO is a ring cleavage dioxygenase from Pseudaminobacter salicylatoxidans that oxidizes salicylate to 2-oxohepta-3,5-dienedioic acid via a novel ring fission mechanism. SDO differs from other known GDO's and NDO's in its unique ability to oxidatively cleave many different salicylate, gentisate, and 1-hydroxy-2- naphthoate substrates with high catalytic efficiency. The active site of this enzyme is located in the N-terminal domain but could be influenced by changes in the C-terminal domain, which lacks the strictly conserved metal-binding residues found in other cupin domains and is thought to be an inactive vestigial remnant
GVALEYVNPTTGGPVMPTIGAFMQLLRAGFSTRPHRSTASAVYHVVEGSGRTVIGGKTFEWEPGDVFVVP
SWAWHSHEADSEDAVLFSFSDRPVQEALG
>gnl|CDD|380398 cd06993, cupin_CENP-C_C, centromere-binding protein CENP-C, C-terminal cupin domain. This family includes centromeric protein C (CENP-C; known as Mif2 in budding yeast and centromere protein 3 or cnp3 in fission yeast), which is an inner kinetochore centromere (CEN)-binding protein found in fungi and metazoans. CENP-C is a component of the CENP-A nucleosome-associated complex (NAC) that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. CENP-C localizes to the inner kinetochore plates adjacent to the centromeric DNA and is known to have DNA-binding ability. CENP-C, along with CENP-H, provides a platform onto which the mitotic kinetochore is assembled and thus plays a critical role in the structuring of kinethocore chromatin. The cupin domain at the C-terminus forms a homodimer which is part of an enhanceosome-like structure that nucleates kinetochore assembly in budding yeast. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
DFFASGMLELPPGGEKPLKNSKDNTYVFYVIQGAVEVTLHETTFVVTKGCSFQVPRGNYYSIKNIGNKEA
RLFFVQS
>gnl|CDD|380399 cd06995, cupin_YkgD-like_N, AraC/XylS family transcriptional regulators similar to Escherichia coli YkgD, N-terminal cupin domain. This family contains mostly bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included in this family is YkgD, an uncharacterized Escherichia coli protein thought to be a transcriptional regulator. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
DALDRLIQLANVQGRLDLRCQLQGDWQLDHPAGPLGEARFHIVLQGECRLELPGGESLTLSPGDVVLLPQ
GSAHRLHSGSNKDAAVPPTLSSDGLLPLRRNGGGGEDLDMLCGR
>gnl|CDD|380400 cd06996, cupin_Lmo2851-like_N, AraC/XylS family transcriptional regulators similar to Listeria monocytogenes Lmo2851 protein, N-terminal cupin domain. This family contains bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included is Listeria monocytogenes Lmo2851 protein, whose function is unknown. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
FPILSNKYFFKNKDIYIRKHNRFADYPLHTHNFLEINYMYSGSCTQIVNGQEITLKEGDLLLLDQGSTHS
IKALGEDDILINIIFRN
>gnl|CDD|380401 cd06997, cupin_MelR-like_N, AraC/XylS family transcriptional regulators similar to Escherichia coli MelR, N-terminal cupin domain. This family contains bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators, including Escherichia coli MelR, a transcription factor that controls melibiose utilization. MelR is encoded by the melR gene and is essential for melibiose-dependent triggering of the melAB operon that encodes products needed for melibiose catabolism and transport. Expression of melR is autoregulated by MelR, which represses the melR promoter by binding to a target that overlaps the transcript start. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
LQIEHRQPHIMPTPHWHGQVEVNIPFDGDVEYLINEHAVSLNAGHIGLFWGGLPHQLTDTGDCAIMAIFN
LPLHHFFS
>gnl|CDD|380402 cd06998, cupin_D-LI-like, sugar isomerase such as lyxose isomerase, cupin domain. This family includes D-lyxose isomerase (D-LI; EC 5.3.1.15) homologous to YdaE from the sigma B regulon of Bacillus subtilis and to pathogenic Escherichia coli O157 z5688 D-lyxose isomerase (EcSI or Z5688), both having highly similar active sites. YdaE may have a synergistic role with ydaD, an NAD(P)-dependent alcohol dehydrogenase, in the adaptation to environment stresses, while EcSI has D-lyxose/D-mannose activity. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
DKLMIVHPGQFCPPHHHGRKTESYEVRLGEMEVFYSPTPSAESGVELLNALPKGRERSYETLTSYVRLRP
GPKFVMPPKHLHAFRAPPDSVPLVVREVSS
>gnl|CDD|380403 cd06999, cupin_HpaA-like_N, AraC/XylS family transcriptional regulators similar to HpaA, N-terminal cupin domain. Members of this family contain an N-terminal cupin domain and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain, similar to Escherichia coli 4-hydroxyphenylacetate catabolism regulatory protein HpaA (also known as 4HPA). HpaA is encoded by the hpaA gene which is located upstream of hpaBC. It is activated by 4-HPA, 3-HPA and phenylacetate, and represents a member of the AraC/XylS family of regulators that recognizes aromatic effectors. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
IPTYALYGESAAAPTPDFLHCETIAARSRLHDWEIAPHRHADLFQVLYIESGGGEVRLDGRTHPLSAPAL
VVVPPGVVHGFRFSPDTDGHVLTLADPL
>gnl|CDD|380404 cd07000, cupin_HGO_N, homogentisate 1,2-dioxygenase and related proteins, N-terminal cupin domain. This family includes homogentisate 1,2-dioxygenase (also known as homogentisate oxygenase, homogentisic acid oxidase, homogentisicase, HGO, HGD, HGDO, or HmgA; EC 1.13.11.5), which is involved in the metabolic degradation of phenylalanine and tyrosine. It catalyzes the crucial aromatic ring opening reaction, utilizing nonheme Fe2+ to incorporate both atoms of molecular oxygen into homogentisate (2,5-dihydroxyphenylacetate) to yield 4-maleylacetoacetate as part of the homogentisate pathway. HGO deficiency caused by critical mutations and polymorphic sites, causes the metabolic disease alkaptonuria (AKU), a rare disorder of autosomal recessive inheritance. Homogentisate accumulation causes insoluble ochronotic pigments to deposit in connective tissues, resulting in degenerative arthritis. These enzymes are found in prokaryotes, eukaryotes, and archaea. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
LRWKPFPIPEEPTDFVDGLRTICGAGDPAARHGLAIHVYAANKSMDDRAFYNSDGDFLIVPQQGTLRIQT
EFGKLEVEPGEIAVIPRGIRFRVELPDGPARGYICEVYG
>gnl|CDD|380405 cd07001, cupin_YbfI-like_N, AraC/XylS family transcriptional regulators similar to Bacillus subtilis YbfI, N-terminal cupin domain. This family contains bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators, including YbfI, an uncharacterized Bacillus subtilis. In Pseudomonas putida, this protein is thought to regulate the expression of phenylserine aldolase. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
DYEAYHFKGIMQKSFPNHFHDFYVIGFIESGQRTLFCEGKEYTVEPGDLLLINPRDVHSCIQISGRRLDY
ERINIW
>gnl|CDD|380406 cd07002, cupin_SznF-like_C, Streptomyces achromogenes SznF and related proteins, C-terminal cupin domain. This family includes bacterial proteins similar to Streptomyces achromogenes SznF, containing an N-terminal helical region that mediates dimerization, a central heme oxygenase domain, and a C-terminal cupin domain. SznF is a metalloenzyme that catalyzes an oxidative rearrangement of the guanidine group of N(omega)-methyl-L-arginine to generate an N-nitrosourea product, during the biosynthesis of streptozotocin, an N-nitrosourea natural product and an approved cancer chemotherapeutic. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold generally capable of homodimerization. However, in SznF, the cupin domain is not involved in dimerization
PEYKDLHDPIKERVKAGKVNIPVARLVEPRGELSVTHVHDGDELCHVVSGTMRFVSGLGSSTILNAGEGV
VIKRNRLHGALILSEECVYEIYSIGD
>gnl|CDD|380407 cd07003, cupin_YobQ-like_N, Bacillus subtilis YobQ and related proteins, N-terminal cupin domain. This family includes bacterial proteins homologous to Bacillus subtilis YobQ and Photobacterium leiognathi LumQ, both uncharacterized proteins thought to be DNA-binding proteins that may function as AraC/XylS family transcriptional regulators. YobQ has an N-terminal cupin beta barrel domain (represented by this alignment model) and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
RTYSHDQSSHSHEHAQLVLPLSGSLELEVEGRGSRVKPDIGLYIPPNAEHRFAGSSDNRCLVLDLP
>gnl|CDD|380408 cd07005, cupin_WbuC-like, Escherichia coli WbuC and related proteins, cupin domain. This family includes bacterial proteins homologous to WbuC, an Escherichia coli protein of unknown function with a cupin beta barrel fold. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
RRRAHLNLHESPDDPVQRMLNALQPGTYVRPHRHPDPPKWELFVVLRGRIAVLIFDDDGTVTERVILGAG
GGVFGIEIPPGTWHTVVALEPDTVIFEVKEGPYDPATDKDFAPW
>gnl|CDD|380409 cd07006, cupin_XcTcmJ-like, Xanthomonas campestris XcTcmJ and related proteins, cupin domain. This family includes bacterial and archaeal proteins homologous to plant pathogen Xanthomonas campestris tetracenomycin polyketide synthesis protein XcTcmJ, a protein encoded by the tcmJ gene. XcTcmJ is annotated as being involved in tetracenomycin polyketide biosynthesis. Also included is Xc5357 from a different strain of X. campestris. Structure studies show that binding of zinc induces conformational changes and serves a functional role in this cupin protein. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
FRVLAGTERSQAATMVLAPGDTEGGPDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEAGETHE
IRNTGDEPLKTLNFYVPPA
>gnl|CDD|380410 cd07007, cupin_CapF-like_C, Staphylococcus aureus CapF and related proteins, C-terminal cupin domain. This family contains cupin domains of proteins homologous to Staphylococcus aureus CapF (also known as WbjC in Pseudomonas aeruginosa and FnlB in Escherichia coli). CapF is a bifunctional metalloenzyme produced by certain pathogenic bacteria and is essential in the biosynthetic path of capsular polysaccharide (CP), a mucous layer on the surface of bacterium that facilitates immune evasion and infection. Thus, CapF is an antibacterial/therapeutic target. In S. aureus, enzymes CapE, CapF and CapG catalyze the sequential transformation of UDP-D-GlcNAc in the CP precursor UDP-L-FucNAc via the intermediate compound UDP-N-acetyl-L-talosamine (UDP-L-TalNAc). CapF consists of two domains; the C-terminal cupin domain catalyzes the epimerization of the compound produced by the upstream enzyme CapE, and the N-terminal short-chain dehydrogenase/reductase (SDR) domain catalyzes the reduction of the compound afforded by the cupin domain, requiring one equivalent of NADPH. The cupin domain is crucial for catalyzing the first chemical reaction, and also important for the stability of the enzyme. Similarly, in P. aeruginosa, WbjC, WbjB and WbjD enzymes synthesize UDP-N-acetyl-L-fucosamine, a precursor of the lipopolysacharide component L-fucosamine. The cupin domains contain a conserved "jelly roll-like" beta-barrel fold
RGSFTEFLKTPDSGQFSVSTTKPGITRGNHYHHTKNEKFLVIKGKALIRFRHIGTDEIIEYYVSGDKPEV
VDIPPGYTHNITNVGDDDLVTLFWANEIFDPNNPDTYFE
>gnl|CDD|380411 cd07008, cupin_yp_001338853-like, Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain. This family includes bacterial proteins homologous to Klebsiella pneumoniae yp_001338853.1, an uncharacterized conserved protein with double-stranded beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
RIFDVAEFVQFSDEEPIRSVITETDDSAIVVWHVKPGQEIAAHIHPHGQDTWIVLSGEGEYLLGDGQTVP
IKAGDIVIAPAGQVHGARNTGDEPLVFVSVV
>gnl|CDD|380412 cd07009, cupin_BLL0285-like, Bradyrhizobium japonicum BLL0285 and related proteins, cupin domain. This family includes bacterial proteins homologous to BLL0285, a Bradyrhizobium japonicum protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
SVVFTVLPVGWVGDWHEAPAPQWVITLSGRWEVETMDGTRFEMGPGDVLFGEDQGAKDADGGTGHLSGLV
GDEPCRRMIVQ
>gnl|CDD|380413 cd07010, cupin_PMI_type_I_N_bac, Phosphomannose isomerase in bacteria and archaea, N-terminal cupin domain. This subfamily contains type I phosphomannose isomerase (PMI; E.C. 5.3.1.8; also known as mannose-6-phosphate isomerase) found in many bacteria (e.g. Bacillus subtilis) and archaea. PMI catalyzes the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P), the first committed step in the synthesis of mannosylated glycoproteins. The active site, located within the N-terminal jelly roll-like beta-barrel cupin fold, contains a single essential zinc atom and forms a deep, open cavity large enough to contain M6P or F6P. PMI type I also has a C-terminal beta-barrel fold which has diverged considerably from the N-terminal domain and is not included here. This subfamily does not contain an alpha helical domain that exists in eukaryotic and some prokaryotic PMIs. F6P is a substrate for glycolysis and gluconeogenesis, while M6P is a substrate for production of activated mannose donor guanosine 5'-diphosphate D-mannose, an important precursor of mannosylated biomolecules such as glycoproteins, bacterial exopolysaccharides and fungal cell wall components. PMI is also essential for survival, virulence and possibly pathogenicity of some bacteria and protozoan parasites, as well as for cell wall integrity of certain yeasts. Thus, PMI is a potential target against fungal infections causing serious illness or death
PILKERVWGGRRLKELFGKPPPDEPIGESWEVSPLLVKLLDAAERLSVQVHPDDEYARKHENEPFGKTEA
WYILDAEPGAKIYLGFKEGVTREEFEKAIDDGDIEELLNKVPVKPGDFFYIPAGTVHAIGAGILVLEIQQ
NSDITYRLYDWGRLDLDGKPRELHLEKALDVID
>gnl|CDD|380414 cd07011, cupin_PMI_type_I_N, type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain. This subfamily contains type I phosphomannose isomerase (PMI; E.C. 5.3.1.8; also known as mannose-6-phosphate isomerase) found in eukaryotes and some bacteria such as Salmonella enterica. PMI catalyzes the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P), the first committed step in the synthesis of mannosylated glycoproteins. The active site, located within the N-terminal jelly roll-like beta-barrel cupin fold, contains a single essential zinc atom and forms a deep, open cavity large enough to contain M6P or F6P. PMI type I also has a C-terminal beta-barrel fold which has diverged considerably from the N-terminal domain and is not included here. This subfamily contains an alpha helical domain that is found in eukaryotic and some prokaryotic PMIs but is not present in their archaeal counterparts. F6P is a substrate for glycolysis and gluconeogenesis, while M6P is a substrate for production of activated mannose donor guanosine 5'-diphosphate D-mannose, an important precursor of mannosylated biomolecules such as glycoproteins, bacterial exopolysaccharides and fungal cell wall components. PMI is also essential for survival, virulence and possibly pathogenicity of some bacteria and protozoan parasites, as well as for cell wall integrity of certain yeasts. Thus, PMI is a potential target against fungal infections causing serious illness or death
LKNAVQNYAWGSKGAISLLARGGGKIPEGKPYAELWMGTHLPFLFKVLSAAKPLSIQAHPDKEQAEKLFA
REPENYKDPNHKPEMAIALTPFEALCGFRPLEEILALLERVPPELRELLGQEDAEQSKEGLKALFSALLT
LDSDEEALAALVARLRARPKSEELDEAEELVLRLAEQYPGDPGVFAALLLNLVTLKPGEAIFLPAGEPHA
YLSGDGVECMANSDNVVRAGLTPKHVDVDELLRMLDY
>gnl|CDD|270234 cd07012, PBP2_Bug_TTT, Bug (Bordetella uptake gene) protein family of periplasmic solute-binding receptors; contains the type 2 periplasmic binding fold. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) proteins present in a number of bacterial species, but mainly in proteobacteria. In eubacteria, at least three families of periplasmic binding-protein dependent transporters are known: the ATP-binding cassette (ABC) transporters, the tripartite ATP-independent periplasmic transporters, and the tripartite tricarboxylate transporters (TTT). Bug proteins are the PBP components of the TTT. Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter
YPSKPIRLVVPFPAGGGTDVVARLLAEALSKELGQPVVVENKPGAGGAIGAAAVARAAPDGYTLLLGSSG
TLTINPLLYKKLYDPLKDFTPVALLATDPLVLVVNADSPYKTLAELVAAAKANPGKLTYGSAGAGSSSHL
AGELLAQAAGIKLTHVPYKGGAPALTDLLGGQVDAAFDSLSEALPQIKAGKLRALAVTSPERLPLLPDVP
TLAEQGLPDFEVSSWRGLFAPAGTPPEVVAKLNAALAKALADPEVRERLAALGLEPVYLTPAEFAAFLRA
ETARWGKLIKA
>gnl|CDD|132924 cd07013, S14_ClpP, Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease. Clp protease (caseinolytic protease; ClpP; Peptidase S14) is a highly conserved serine protease present throughout in bacteria and eukaryota, but seems to be absent in archaea, mollicutes and some fungi. Clp proteases are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. Additionally, they are implicated in the control of cell growth, targeting DNA-binding protein from starved cells. ClpP has also been linked to the tight regulation of virulence genes in the pathogens Listeria monocytogenes and Salmonella typhimurium. This enzyme belong to the family of ATP-dependent proteases; the functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP, although the proteolytic subunit alone does possess some catalytic activity. Active site consists of the triad Ser, His and Asp; some members have lost all of these active site residues and are therefore inactive, while others may have one or two large insertions. ClpP seems to prefer hydrophobic or non-polar residues at P1 or P1' positions in its substrate. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function
REIMLTGEVEDISANQFAAQLLFLGAVNPEKDIYLYINSPGGDVFAGMAIYDTIKFIKADVVTIIDGLAA
SMGSVIAMAGAKGKRFILPNAMMMIHQPWGGTLGDATDMRIYADLLLKVEGNLVSAYAHKTGQSEEELHA
DLERDTWLSAREAVEYGFADTI
>gnl|CDD|132925 cd07014, S49_SppA, Signal peptide peptidase A. Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): SppA is an intramembrane enzyme found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Unlike the eukaryotic functional homologs that are proposed to be aspartic proteases, site-directed mutagenesis and sequence analysis have shown these bacterial, archaeal and thylakoid SppAs to be ClpP-like serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain, cleaving peptide bonds in the plane of the lipid bilayer. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad (both residues absolutely conserved within bacteria, chloroplast and mitochondrial signal peptidase family members) and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. In addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members, the E. coli SppA contains an amino-terminal domain (sometimes referred to as 67K type). Others, including sohB peptidase, protein C, protein 1510-N and archaeal signal peptide peptidase, do not contain the amino-terminal domain (sometimes referred to as 36K type). Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain. This family also contains homologs that either have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for the catalytic activity of peptidases
VVFANGVIVDGEESSSDTQGNVSGDTTAAQIRDARLDPKVKAIVLRVNSPGGSVTASEVIRAELAAARAA
GKPVVASGGGNAASGGYWISTPANYIVANPSTLVGSIGIFGVQLADQLSIENGYKRFITLVADNRHSTPE
QQIDKIAQGGVWTGQDAKANGLVDSLGSFDDAVAKLA
>gnl|CDD|132926 cd07015, Clp_protease_NfeD, Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease. Nodulation formation efficiency D (NfeD; stomatin operon partner protein, STOPP; DUF107) is a member of membrane-anchored ClpP-class proteases. Currently, more than 300 NfeD homologs have been identified - all of which are bacterial or archaeal in origin. Majority of these genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named STOPP (stomatin operon partner protein). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 (1510-N or PH1510-N) from Pyrococcus horikoshii has been shown to possess serine protease activity and has a Ser-Lys catalytic dyad, preferentially cleaving hydrophobic substrates. Difference in oligomeric form and catalytic residues between 1510-N (forming a dimer) and ClpP (forming a tetradecamer) shows a possible functional difference: 1510-N is likely to have a regulatory function while ClpP is involved in protein quality control
VYVAQIKGQITSYTYDQFDRYITIAEQDNAEAIIIELDTPGGRADAAGNIVQRIQQSKIPVIIYVYPPGA
SAASAGTYIALGSHLIAMAPGTSIGACRPILGYSQNGSIIEAPPKITNYFIAYIKSLAQESGRNATIAEE
FITKDLSLTPEEALKYGVIEVVARDINELLKK
>gnl|CDD|132927 cd07016, S14_ClpP_1, Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease. Clp protease (caseinolytic protease; ClpP; Peptidase S14) is a highly conserved serine protease present throughout in bacteria and eukaryota, but seems to be absent in archaea, mollicutes and some fungi. This subfamily only contains bacterial sequences. Clp proteases are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth, targeting DNA-binding protein from starved cells. ClpP has also been linked to the tight regulation of virulence genes in the pathogens Listeria monocytogenes and Salmonella typhimurium. This enzyme belong to the family of ATP-dependent proteases; the functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP, although the proteolytic subunit alone does possess some catalytic activity. Active site consists of the triad Ser, His and Asp; some members have lost all of these active site residues and are therefore inactive, while others may have one or two large insertions. ClpP seems to prefer hydrophobic or non-polar residues at P1 or P1' positions in its substrate. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function
AEIYIYGDIGSDWGVTAKEFKDALDALGDDSDITVRINSPGGDVFAGLAIYNALKRHKGKVTVKIDGLAA
SAASVIAMAGDEVEMPPNAMLMIHNPSTGAAGNADDLRKAADLLDKIDESIANAYAEKTGLSEEEISALM
DAETWLTAQEAVELGFADEI
>gnl|CDD|132928 cd07017, S14_ClpP_2, Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease. Clp protease (caseinolytic protease; ClpP; Peptidase S14) is a highly conserved serine protease present throughout in bacteria and eukaryota, but seems to be absent in archaea, mollicutes and some fungi. Clp proteases are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth, targeting DNA-binding protein from starved cells. ClpP has also been linked to the tight regulation of virulence genes in the pathogens Listeria monocytogenes and Salmonella typhimurium. This enzyme belong to the family of ATP-dependent proteases; the functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP, although the proteolytic subunit alone does possess some catalytic activity. Active site consists of the triad Ser, His and Asp; some members have lost all of these active site residues and are therefore inactive, while others may have one or two large insertions. ClpP seems to prefer hydrophobic or non-polar residues at P1 or P1' positions in its substrate. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function
DIYSRLLKERIIFLGGPIDDEVANLIIAQLLYLESEDPKKPIYLYINSPGGSVTAGLAIYDTMQYIKPPV
STICLGLAASMGALLLAAGTKGKRYALPNSRIMIHQPLGGAGGQASDIEIQAKEILRLRRRLNEILAKHT
GQPLEKIEKDTDRDRYMSAEEAKEYGLIDKI
>gnl|CDD|132929 cd07018, S49_SppA_67K_type, Signal peptide peptidase A (SppA) 67K type, a serine protease, has catalytic Ser-Lys dyad. Signal peptide peptidase A (SppA; Peptidase S49; Protease IV) 67K type: SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Members in this subfamily contain an amino-terminal domain in addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members (sometimes referred to as 67K type), similar to E. coli and Arabidopsis thaliana SppA peptidases. Unlike the eukaryotic functional homologs that are proposed to be aspartic proteases, site-directed mutagenesis and sequence analysis have shown that members in this subfamily, mostly bacterial, are serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad (both residues absolutely conserved within bacteria, chloroplast and mitochondrial signal peptidase family members) and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain
LVLDLSGSLVEQPPPSPPLLLGGGESSELSLRDLLEALEKAAEDDRIKGIVLDLDGLSGGLAKLEELRQA
LERFRASGKPVIAYADGYSQGQYYLASAADEIYLNPSGSVELTGLSAETLFFKGLLDKLGVEVQVFRVGE
YKSAVEPFTRDDMSPEAREQTQALLDSLWDQYLADVAASRGLSPDALEALIDLGGDSAEEALEAGLVDGL
AYRDELEARLKE
>gnl|CDD|132930 cd07019, S49_SppA_1, Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad. Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): SppAs in this subfamily are found in all three domains of life and are involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Site-directed mutagenesis and sequence analysis have shown these bacterial, archaeal and thylakoid SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad (both residues absolutely conserved within bacteria, chloroplast and mitochondrial signal peptidase family members) and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. In addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members, the E. coli SppA contains an amino-terminal domain, similar to Arabidopsis thaliana SppA1 peptidase. Others, including sohB peptidase, protein C and archaeal signal peptide peptidase, do not contain the amino-terminal domain. Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain
SIGVVFANGAIVDGEETQGNVGGDTTAAQIRDARLDPKVKAIVLRVNSPGGSVTASEVIRAELAAARAAG
KPVVVSAGGAAASGGYWISTPANYIVANPSTLTGSIGIFGVITTVENSLDSIGVHTDGVSTSPLADVSIT
RALPPEAQLGLQLSIENGYKRFITLVADARHSTPEQIDKIAQGHVWTGQDAKANGLVDSLGDFDDAVAKA
A
>gnl|CDD|132931 cd07020, Clp_protease_NfeD_1, Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease. Nodulation formation efficiency D (NfeD; stomatin operon partner protein, STOPP; DUF107) is a member of membrane-anchored ClpP-class proteases. Currently, more than 300 NfeD homologs have been identified - all of which are bacterial or archaeal in origin. Majority of these genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named STOPP (stomatin operon partner protein). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 (1510-N or PH1510-N) from Pyrococcus horikoshii has been shown to possess serine protease activity and has a Ser-Lys catalytic dyad, preferentially cleaving hydrophobic substrates. Difference in oligomeric form and catalytic residues between 1510-N (forming a dimer) and ClpP (forming a tetradecamer) shows a possible functional difference: 1510-N is likely to have a regulatory function while ClpP is involved in protein quality control
VYVLEINGAITPATADYLERAIDQAEEGGADALIIELDTPGGLLDSTREIVQAILASPVPVVVYVYPSGA
RAASAGTYILLAAHIAAMAPGTNIGAAHPVAIGGGGGSDPVMEKKILNDAVAYIRSLAELRGRNAEWAEK
AVRESLSLTAEEALKLGVIDLIAADLNELLKKLDGRTVKVAGKEVTL
>gnl|CDD|132932 cd07021, Clp_protease_NfeD_like, Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease. Nodulation formation efficiency D (NfeD; stomatin operon partner protein, STOPP; DUF107) is a member of membrane-anchored ClpP-class proteases. Currently, more than 300 NfeD homologs have been identified - all of which are bacterial or archaeal in origin. Majority of these genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named STOPP (stomatin operon partner protein). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 (1510-N or PH1510-N) from Pyrococcus horikoshii has been shown to possess serine protease activity and has a Ser-Lys catalytic dyad, preferentially cleaving hydrophobic substrates. Difference in oligomeric form and catalytic residues between 1510-N (forming a dimer) and ClpP (forming a tetradecamer) shows a possible functional difference: 1510-N is likely to have a regulatory function while ClpP is involved in protein quality control
VYVIPIEGEIDPGLAAFVERALKEAKEEGADAVVLDIDTPGGRVDSALEIVDLILNSPIPTIAYVNDRAA
SAGALIALAADEIYMAPGATIGAAEPIPGDGNGAADEKVQSYWRAKMRAAAEKKGRDPDIAEAMVDKDIE
VPGVGIKGGELLTLTADEALKVGYAEGIAGSLDELLVK
>gnl|CDD|132933 cd07022, S49_Sppa_36K_type, Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad. Signal peptide peptidase A (SppA; Peptidase S49; Protease IV) 36K type: SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Members in this subfamily are all bacterial and include sohB peptidase and protein C. These are sometimes referred to as 36K type since they contain only one domain, unlike E. coli SppA that also contains an amino-terminal domain. Site-directed mutagenesis and sequence analysis have shown these SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases
GVAVIPVHGVLVPRGSWLEASSGLTSYEGIAAAIRAALADPDVRAIVLDIDSPGGEVAGVFELADAIRAA
RAGKPIVAFVNGLAASAAYWIASAADRIVVTPTAGVGSIGVVASHVDQSKALEKAGLKVTLIFAGAHKVD
GNPDEPLSDEARARLQAEVDALYAMFVAAVARNRGLSAAAVRATEGGVFRGQEAVAAGLADAVGTLDDAL
AALA
>gnl|CDD|132934 cd07023, S49_Sppa_N_C, Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad. Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. This subfamily contains members with either a single domain (sometimes referred to as 36K type), such as sohB peptidase, protein C and archaeal signal peptide peptidase, or an amino-terminal domain in addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members (sometimes referred to as 67K type), similar to E. coli and Arabidopsis thaliana SppA peptidases. Site-directed mutagenesis and sequence analysis have shown these SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain
KIAVIDIEGTISDGGGIGADSLIEQLRKAREDDSVKAVVLRINSPGGSVVASEEIYREIRRLRKAKKPVV
ASMGDVAASGGYYIAAAADKIVANPTTITGSIGVIGQGPNLEELLDKLGIERDTIKSGPGKDKGSPDRPL
TEEERAILQALVDDIYDQFVDVVAEGRGMSGERLDKLADGRVWTGRQALELGLVDELGGLDDAIAKAA
>gnl|CDD|132882 cd07025, Peptidase_S66, LD-Carboxypeptidase, a serine protease, includes microcin C7 self immunity protein. LD-carboxypeptidase (Muramoyltetrapeptide carboxypeptidase; EC 3.4.17.13; Merops family S66; initially described as Carboxypeptidase II) family also includes the microcin c7 self-immunity protein (MccF) as well as uncharacterized proteins including hypothetical proteins. LD-carboxypeptidase hydrolyzes the amide bond that links the dibasic amino acids to C-terminal D-amino acids. The physiological substrates of LD-carboxypeptidase are tetrapeptide fragments (such as UDP-MurNAc-tetrapeptides) that are produced when bacterial cell walls are degraded; they contain an L-configured residue (L-lysine or meso-diaminopimelic acid residue) as the penultimate residue and D-alanine as the ultimate residue. A possible role of LD-carboxypeptidase is in peptidoglycan recycling whereby the resulting tripeptide (precursor for murein synthesis) can be reconverted into peptidoglycan by attachment of preformed D-Ala-D-Ala dipeptides. Some enzymes possessing LD-carboxypeptidase activity also act as LD-transpeptidase by replacing the terminal D-Ala with another D-amino acid. MccF contributes to self-immunity towards microcin C7 (MccC7), a ribosomally encoded peptide antibiotic that contains a phosphoramidate linkage to adenosine monophosphate at its C-terminus. Its possible biological role is to defend producer cells against exogenous microcin from re-entering after having been exported. It is suggested that MccF is involved in microcin degradation or sequestration in the periplasm
IGIVAPSSPIDEEERLERAIARLESLGLEVVVGPHVLARDGYLAGTDEERAADLNAAFADPEIKAIWCAR
GGYGANRLLPYLDYDLIRANPKIFVGYSDITALHLALYAKTGLVTFHGPMLASLFGPGTLDYTTVLRLLA
LLSGEQSSEDLEWPLNPPLRTLRPGKAEGRLIGGNLTVLASLLGTPYLPDTEGKILFLEDVGEPPYRIDR
MLTQLKLAGVLDKVAGIILGRFTDCEDNDDFGYTLEEVLKEVLGDLGIPVLYGLPIGHTPPNLTLPLGAE
AE
>gnl|CDD|197305 cd07026, Ribosomal_L20, Ribosomal protein L20. The ribosomal protein family L20 contains members from eubacteria, as well as their mitochondrial and plastid homologs. L20 is an assembly protein, required for the first in-vitro reconstitution step of the 50S ribosomal subunit, but does not seem to be essential for ribosome activity. L20 has been shown to partially unfold in the absence of RNA, in regions corresponding to the RNA-binding sites. L20 represses the translation of its own mRNA via specific binding to two distinct mRNA sites, in a manner similar to the L20 interaction with 23S ribosomal RNA
RGVVARKRRKKILKLAKGFRGRRSRLFRTAKQAVMKALAYAYRDRKQKKRDFRRLWITRINAAAREHGLS
YSRFIHGLKKANILLNRKVLAQLAILDPKAFKALVE
>gnl|CDD|132905 cd07027, RNAP_RPB11_like, RPB11 subunit of RNA polymerase. The eukaryotic RPB11 subunit of RNA polymerase (RNAP), as well as its archaeal (L subunit) and bacterial (alpha subunit) counterparts, is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. At least three distinct RNAP complexes are found in eukaryotic nuclei: RNAP I, RNAP II, and RNAP III, for the synthesis of ribosomal RNA precursor, mRNA precursor, and 5S and tRNA, respectively. A single distinct RNAP complex is found in prokaryotes and archaea, which may be responsible for the synthesis of all RNAs. The assembly of the two largest eukaryotic RNAP subunits that provide most of the enzyme's catalytic functions depends on the presence of RPB3/RPB11 heterodimer subunits. This is also true for the archaeal (D/L subunits) and bacterial (alpha subunit) counterparts
LRIISKEKNSVTVEMENEDHTLGNLLREELLKDDQVDFARYYIKHPVIDKIQIRIQTKSGIKPKDALKRA
VNKLSKLYEHLGT
>gnl|CDD|132906 cd07028, RNAP_RPB3_like, RPB3 subunit of RNA polymerase. The eukaryotic RPB3 subunit of RNA polymerase (RNAP), as well as its archaeal (D subunit) and bacterial (alpha subunit) counterparts, is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. At least three distinct RNAP complexes are found in eukaryotic nuclei: RNAP I, RNAP II, and RNAP III, for the synthesis of ribosomal RNA precursor, mRNA precursor, and 5S and tRNA, respectively. A single distinct RNAP complex is found in prokaryotes and archaea, which may be responsible for the synthesis of all RNAs. The RPB3 subunit is similar to the bacterial RNAP alpha subunit in that it contains two subdomains: one subdomain is similar to the eukaryotic Rpb11/AC19/archaeal L subunit which is involved in dimerization; and the other is an inserted beta sheet subdomain. The assembly of the two largest eukaryotic RNAP subunits that provide most of the enzyme's catalytic functions depends on the presence of RPB3/RPB11 heterodimer subunits. This is also true for the archaeal (D/L subunits) and bacterial (alpha subunit) counterparts
PQVKIREADKDNVDFILSGVDLAMANALRRVMIAEVPTMAVDSVEVETNTSVLADEILAHRLGLIPLQSM
DILQLYRSPEEDCECEDHCDKCSVVLTLQAFAESESTTNVYSKDLVIVSNLMGRNIGHPIIQDILICKLR
KGQEIKLTCVAKKGIGKEHAKFGPVAAIEFRYDPVADTYIMNVESVGSLPPDQVVVEAIKTLQKKVASIL
LA
>gnl|CDD|132907 cd07029, RNAP_I_III_AC19, AC19 subunit of Eukaryotic RNA polymerase (RNAP) I and RNAP III. The eukaryotic AC19 subunit of RNA polymerase (RNAP) I and RNAP III is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. At least three distinct RNAP complexes are found in eukaryotic nuclei: RNAP I, RNAP II, and RNAP III. RNAP I is responsible for the synthesis of ribosomal RNA precursor, while RNAP III functions in the synthesis of 5S and tRNA. The AC19 subunit is the equivalent of the RPB11 subunit of RNAP II. The RPB11 subunit heterodimerizes with the RPB3 subunit, and together with RPB10 and RPB12, anchors the two largest subunits, RPB1 and RPB2, and stabilizes their association. The homology of AC19 to RPB11 suggests a similar function. The AC19 subunit is likely to associate with the RPB3 counterpart, AC40, to form a heterodimer, which stabilizes the association of the two largest subunits of RNAP I and RNAP III
VEGEGTDESCATFVFYGEDHTLGNSLRYVIMKNPEVEFCGYSIPHPSENKINLRIQTKGGEPAVDVLKKG
LEDLEQICDHILSTF
>gnl|CDD|132908 cd07030, RNAP_D, D subunit of Archaeal RNA polymerase. The D subunit of archaeal RNA polymerase (RNAP) is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. A single distinct RNAP complex is found in archaea, which may be responsible for the synthesis of all RNAs. The archaeal RNAP harbors homologues of all eukaryotic RNAP II subunits with two exceptions (RPB8 and RPB9). The 12 archaeal subunits are designated by letters and can be divided into three functional groups that are engaged in: (I) catalysis (A'/A", B'/B" or B); (II) assembly (L, N, D and P); and (III) auxiliary functions (F, E, H and K). The D subunit is equivalent to the RPB3 subunit of eukaryotic RNAP II. It contains two subdomains: one subdomain is similar the eukaryotic Rpb11/AC19/archaeal L subunit which is involved in dimerization, and the other is an inserted beta sheet subdomain. The assembly of the two largest archaeal RNAP subunits that provide most of the enzyme's catalytic functions depends on the presence of the archaeal D/L heterodimer
MEIEVLELDDDRARFVLEGVPPAFANAIRRAIISEVPTLAIDDVNIYENTSVLFDEMLAHRLGLIPLRTD
LDLYKYRSECSCGGAGCPLCTVTLTLSVEGPGTVYSGDLKSSDPDVKPVYDNIPIVKLGKGQKLVLEAYA
RLGRGKEHAKWQPTTACGYKYYPVIEIDEDCDGCGKCVEECPRGVLELEEGKVVVEDLEDCSLCKLCERA
CDAGAIRVGWDEDRFIFEVESDGSLPPKEILLEALRILKEKADELIEAL
>gnl|CDD|132909 cd07031, RNAP_II_RPB3, RPB3 subunit of Eukaryotic RNA polymerase II. The eukaryotic RPB3 subunit of RNA polymerase (RNAP) II is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. At least three distinct RNAP complexes are found in eukaryotic nuclei: RNAP I, RNAP II, and RNAP III. RNAP II is responsible for the synthesis of mRNA precursor. The RPB3 subunit is similar to the bacterial RNAP alpha subunit in that it contains two subdomains: one subdomain is similar the eukaryotic Rpb11/AC19/archaeal L subunit which is involved in dimerization, and the other is an inserted beta sheet subdomain. The RPB3 subunit heterodimerizes with the RPB11 subunit, and together with RPB10 and RPB12, anchors the two largest subunits, RPB1 and RPB2, and stabilizes their association
PRVEITELTDDKVKFILENTDLSVANSLRRVMIAEVPTLAIDLVEIEENTSVLHDEFIAHRLGLIPLTSD
DVDEFLYYSRDCDCDEFCDKCSVELTLDVKCTGDQTREVTSRDLVSSGPKVNDVVPVPIRNDSEDNGEED
GILIVKLRKGQELKLRCIAKKGIGKEHAKWSPTAAVTFEYDPDNALRHTDYWYLEDEDKEWPKSENACIE
EPPEKDALFDIDAKPDKFYFNVESTGALPPEQIVLSGLEILKKKLADLQLQLSEE
>gnl|CDD|132910 cd07032, RNAP_I_II_AC40, AC40 subunit of Eukaryotic RNA polymerase (RNAP) I and RNAP III. The eukaryotic AC40 subunit of RNA polymerase (RNAP) I and RNAP III is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. At least three distinct RNAP complexes are found in eukaryotic nuclei: RNAP I, RNAP II, and RNAP III. RNAP I is responsible for the synthesis of ribosomal RNA precursor, while RNAP III functions in the synthesis of 5S and tRNA. The AC40 subunit is the equivalent of the RPB3 subunit of RNAP II. The RPB3 subunit is similar to the bacterial RNAP alpha subunit in that it contains two subdomains: one subdomain is similar the eukaryotic Rpb11/AC19/archaeal L subunit which is involved in dimerization; and the other is an inserted beta sheet subdomain. The RPB3 subunit heterodimerizes with the RPB11 subunit, and together with RPB10 and RPB12, anchors the two largest subunits, RPB1 and RPB2, and stabilizes their association. The homology of AC40 to RPB3 suggests a similar function. The AC40 subunit is likely to associate with the RPB11 counterpart, AC19, to form a heterodimer, which stabilizes the association of the two largest subunits of RNAP I and RNAP III
FKIEIISLSDEELEFDLIGVDASIANAFRRILLAEVPTMAIEKVYIYNNTSVIQDEVLAHRLGLIPIKAD
PRLFEYREDSDDEPTEENTLVFELKVKCTRNPNAPKDSTDPDELYINHKVYSGDLKWVPIGSQEKRFADN
PIRPVHPDILIAKLRPGQEIDLELHCVKGIGKDHAKFSPVATASYRLLPEITLLKPITGEDAEKLQKCFP
PGVIDIEEVKGKKKAVVANPRKDTLSREVLRHEEFKDKVELGRVRDHFIFSIESTGALPPDVLFLEAIKI
LKEKCRKLLEE
>gnl|CDD|132916 cd07033, TPP_PYR_DXS_TK_like, Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins. Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids
KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTF
SFFLQRAYDQIRHDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAAL
EAALEYDGPVYIRLPR
>gnl|CDD|132917 cd07034, TPP_PYR_PFOR_IOR-alpha_like, Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase alpha subunit (IOR-alpha), and related proteins. Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain, of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit (IOR-alpha), and related proteins, subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzyme Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit. This subfamily includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate
GNEAVARGALAAGVDVVAAYPITPSTEIAETLAKAVLGELGGVVVQAESEHAAAEAAIGASAAGARAMTA
TSGPGLNLMAEALYLAAGAELPLVIVVAQRPGPSTGLPKPDQSDLMAARYGGHPWPVLAPSSVQEAFDLA
LEAFELAEKYRLPVIVLSDG
>gnl|CDD|132918 cd07035, TPP_PYR_POX_like, Pyrimidine (PYR) binding domain of POX and related proteins. Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway
DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPG
LTNAVTGLANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRI
ALSGRPGPVALDLPK
>gnl|CDD|132919 cd07036, TPP_PYR_E1-PDHc-beta_like, Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins. Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids
QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRP
IVEIMFADFALPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVA
PSTPYDAKGLLKAAIRDDDPVIFLEHK
>gnl|CDD|132920 cd07037, TPP_PYR_MenD, Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins. Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone)
QALVEELKRLGVRDVVISPGSRSAPLALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGT
AVANLLPAVVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPEDDDDLWYLLRL
ANRAVLEALSAPPGPVHLNLPF
>gnl|CDD|132921 cd07038, TPP_PYR_PDC_IPDC_like, Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins. Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions
EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKGLGALVTTYGVG
ELSALNGIAGAYAEHVPVVHIVGAPSTKAQASGLLLHHTLGDGDFDVFLKMFEEITCAAARLTDPENAAE
EIDRVLRTALRESRPVYIEIPR
>gnl|CDD|132922 cd07039, TPP_PYR_POX, Pyrimidine (PYR) binding domain of POX. Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate
TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGS
SGPGAIHLLNGLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDR
AIRTAIAKRGVAVLILPGDVQDAP
>gnl|CDD|132716 cd07040, HP, Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction. Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed
VLYLVRHGEREPNAEGRFTGWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGL
FEGLPVEVDPRARVLNALLELLARHLLDGKNVLIVSHGGTIRALLAALLGLSDEEILSLNLPNGSILVLE
LDECGGKYVRLLN
>gnl|CDD|132912 cd07041, STAS_RsbR_RsbS_like, Sulphate Transporter and Anti-Sigma factor antagonist domain of the "stressosome" complex proteins RsbS and RsbR, regulators of the bacterial stress activated alternative sigma factor sigma-B by phosphorylation. The STAS (Sulphate Transporter and Anti-Sigma factor antagonist) domain of proteins related to RsbS and RsbR which are part of the "stressosome" complex that plays an important role in the regulation of the bacterial stress activated alternative sigma factor sigma-B. During stress conditions RsbS and RsbR are phosphorylated which leads to the release of RsbT, an activator of of the RsbU phosphatase, which in turn activates RsbV which leads to the release and activation of sigma factor B. RsbS is a single domain protein (STAS domain), while RsbR-like proteins have a well-conserved C-terminal STATS domain and a variable N-terminal domain. The STAS domain is also found in the C- terminal region of sulphate transporters and anti-anti-sigma factors
STPIIPVWDGVLVLPLIGDLDDERAEQLQERLLEAISRRRARGVIIDLTGVPVIDSAVARHLLRLARALR
LLGARTILTGIRPEVAQTLVELGIDLSGIRTAATLQQAL
>gnl|CDD|132913 cd07042, STAS_SulP_like_sulfate_transporter, Sulphate Transporter and Anti-Sigma factor antagonist domain of SulP-like sulfate transporters, plays a role in the function and regulation of the transport activity, proposed general NTP binding function. The SulP family is a large and diverse family of anion transporters, with members from eubacteria, plants, fungi, and mammals. They contain 10 to 14 transmembrane helices which form the catalytic core of the protein and a C-terminal extension, the STAS (Sulphate Transporter and AntiSigma factor antagonist) domain which plays a role in the function and regulation of the transport activity. The STAS domain is found in the C-terminal region of sulphate transporters and bacterial anti-sigma factor antagonists. It has been suggested that this domain may have a general NTP binding function
YPLAEEPPGVLIYRIDGPLFFGNAEYFKDRLLRLVDEDPPLKVVILDLSAVNFIDSTAAEALEELVKDLR
KRGVELYLAGLNPQVRELLERAGLLDEIGEENFFPTL
>gnl|CDD|132914 cd07043, STAS_anti-anti-sigma_factors, Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key regulators of anti-sigma factors by phosphorylation. Anti-anti-sigma factors play an important role in the regulation of several sigma factors and their corresponding anti-sigma factors. Upon dephosphorylation they bind the anti-sigma factor and induce the release of the sigma factor from the anti-sigma factor. In a feedback mechanism the anti-anti-sigma factor can be inactivated via phosphorylation by the anti-sigma factor. Well studied examples from Bacillus subtilis are SpoIIAA (regulating sigmaF and sigmaC which play an important role in sporulation) and RsbV (regulating sigmaB involved in the general stress response). The STAS domain is also found in the C- terminal region of sulphate transporters and stressosomes
ITVEERGGVLVVRLSGELDAATAPELREALEELLAEGPRRLVLDLSGVTFIDSSGLGVLLGAYKRARAAG
GRLVLVNVSPAVRRVLELTGLDRLFPIYP
>gnl|CDD|132871 cd07044, CofD_YvcK, Family of CofD-like proteins and proteins related to YvcK. CofD is a 2-phospho-L-lactate transferase that catalyzes the last step in the biosynthesis of coenzyme F(420)-0 (F(420) without polyglutamate) by transferring the lactyl phosphate moiety of lactyl(2)diphospho-(5')guanosine (LPPG) to 7,8-didemethyl-8-hydroxy-5-deazariboflavin ribitol (F0). F420 is a hydride carrier, important for energy metabolism of methanogenic archaea, as well as for the biosynthesis of other natural products, like tetracycline in Streptomyces. F420 and some of its precursors are also utilized as cofactors for enzymes, like DNA photolyase in Mycobacterium tuberculosis. YvcK from Bacillus subtilis is a member of a family of mostly uncharacterized proteins and has been proposed to play a role in carbon metabolism, since its function is essential for growth on intermediates of the Krebs cycle and pentose phosphate pathway. Both families appear to have a conserved phosphate binding site, but have different substrate binding residues conserved within each family
VVVFGGGTGLPVLLRGLKEFPVEITAIVTVADDGGSSGELRNXQDIPPPGDLRNVLVALSDQEDRLEQLF
QYRKEEGINEGLGHSLGNLAIAGXTSITGDFTDAIVELSKVFNIKGNILPSSDDPVSLHAEXEDGTIVHG
ESFIPKGEKKIDRVFLTPVDEASPSREVLEAIEKADNIVIGPGSLYTSILPNISVPGIREALKKTXAKKV
YVSNIXTQPGETDEYTSSDHAEALQRHLGRPFIDVVLVDEEDRSDEVXNSYRFDELVPVEVDFFALKRLG
CRVISADFLXEENGGSRHNSKELSEIIVE
>gnl|CDD|132885 cd07045, BMC_CcmK_like, Carbon dioxide concentrating mechanism K (CcmK)-like proteins, Bacterial Micro-Compartment (BMC) domain. Bacterial micro-compartments are primitive protein-based organelles that sequester specific metabolic pathways in bacterial cells. The prototypical bacterial microcompartment is the carboxysome shell, a bacterial polyhedral organelle which increase the efficiency of CO2 fixation by encapsulating RuBisCO and carbonic anhydrase. They can be divided into two types: alpha-type carboxysomes (alpha-cyanobacteria and proteobacteria) and beta-type carboxysomes (beta-cyanobacteria). Potential functional differences between the two types are not yet fully understood. In addition to these proteins there are several homologous shell proteins including those found in pdu organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol and eut organelles involved in the cobalamin-dependent degradation of ethanolamine. Structure evidence shows that several carboxysome shell proteins and their homologs (Csos1A, CcmK1,2,4, and PduU) exist as hexamers which might further assemble into extended, tightly packed layers hypothesized to represent the flat facets of the polyhedral organelles outer shell. Although it has been suggested that other homologous proteins in this family might also form hexamers and play similar functional roles in the construction of their corresponding organelle outer shells at present no experimental evidence directly supports this view
ALGLIETRGLVAAIEAADAALKAANVTLVGYEKVGGGLVTVKITGDVAAVKAAVEAGAAAAERIGELVSS
HVIPRPHDEVEKIL
>gnl|CDD|132886 cd07046, BMC_PduU-EutS, 1,2-propanediol utilization protein U (PduU)/ethanolamine utilization protein S (EutS), Bacterial Micro-Compartment (BMC) domain. PduU encapsulates several related enzymes within a shell composed of a few thousand protein subunits. PduU exists as a hexamer which might further assemble into the flat facets of the polyhedral outer shell of the pdu organelle. This proteinaceous noncarboxysome microcompartment is involved in coenzyme B12-dependent degradation of 1,2-propanediol. The core of PduU is related to the typical BMC domain and its natural oligomeric state is a cyclic hexamer. Unlike other typical BMC domain proteins, the 3D topology of PduU reveals a circular permuted variation on the typical BMC fold which leads to several unique features. The exact functions related to those unique features are still not clear. Another difference is the presence of a deep cavity on one side of the hexamer as well as an intermolecular six-stranded beta barrel that seems to block the central pore that is present in other BMC domain proteins. EutS proteins included in this CD are sequence homologs of PduU. They are encoded within eut operon and may be required for the formation of the outer shell of bacterial eut polyhedral organelles which are involved in the cobalamin-dependent degradation of ethanolamine. Although it has been suggested that EutS might also form hexamers and play similar functional roles in the construction of the eut organelle outer shell at present no experimental evidence directly supports this view
QRIIQEYVPGKQITLAHLIANPDPEIYQKLGLNPGVDEAIGILTITPSEAAIIAADIATKAADVEIGFLD
RFSGALVITGDVSEVESALEAVVDYLRETLGFTVCPITKT
>gnl|CDD|132887 cd07047, BMC_PduB_repeat1, 1,2-propanediol utilization protein B (PduB), Bacterial Micro-Compartment (BMC) domain repeat 1. PduB proteins are homologs of the carboxysome shell protein. They are encoded within the pdu operon and might be required for the formation of the outer shell of the bacterial pdu polyhedral organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduB might form hexamers and further assemble into the flat facets of the polyhedral outer shell of pdu organelles at present no experimental evidence directly supports this view. PduB proteins contain two tandem BMC domains repeats. This CD contains repeat 1 (the first BMC domain of PduB)
TEFVGTAIGDTIGLVIANVDPLLLEKMKLDKKYRSIGILGARTGAGPQIMAADEAVKATNTEVISIELPR
DTKGGAGHGSLILFGAEDVSDVRRAVEVALSETEKTFGDVYGSEAGHIELQYTARASYALNKAF
>gnl|CDD|132888 cd07048, BMC_PduB_repeat2, 1,2-propanediol utilization protein B (PduB), Bacterial Micro-Compartment (BMC) domain repeat 2. PduB proteins are homologs of the carboxysome shell protein. They are encoded within the pdu operon and might be required for the formation of the outer shell of the bacterial pdu polyhedral organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduB might form hexamers and further assemble into the flat facets of the polyhedral outer shell of the pdu organelles at present no experimental evidence directly supports this view. PduB proteins contain two tandem BMC domains repeats. This CD contains repeat 2 (the second BMC domain of PduB)
AFGIIVGAPAAIGLLMADTALKAANVDIVGYASPSGGTSFSNEVILTISGDSGAVRQALIAAREVGLQLL
>gnl|CDD|132889 cd07049, BMC_EutL_repeat1, ethanolamine utilization protein S (EutS), Bacterial Micro-Compartment (BMC) domain repeat 1. EutL proteins are homologs of the carboxysome shell protein. They are encoded within the eut operon and might be required for the formation of the outer shell of the bacterial eut polyhedral organelles which are involved in the cobalamin-dependent degradation of ethanolamine. Although it has been suggested that EutL might form hexamers and further assemble into the flat facets of the polyhedral outer shell of the eut organelles at present no experimental evidence directly supports this view. EutL proteins contain two tandem BMC domains. This CD includes domain 1 (the first BMC domain of EutL)
VLAVKVIPNVDPDLAKELSLPPHHRSLGIITADSDDVTYTALDEATKAAEVEVVYARSFYAGAAHASTPL
AGEVIGILAGPSPAEVRSGLNAAIDFIENEAYF
>gnl|CDD|132890 cd07050, BMC_EutL_repeat2, ethanolamine utilization protein S (EutS), Bacterial Micro-Compartment (BMC) domain repeat 2. EutL proteins are homologs of the carboxysome shell protein. They are encoded within the eut operon and might be required for the formation of the outer shell of the bacterial eut polyhedral organelles which are involved in the cobalamin-dependent degradation of ethanolamine. Although it has been suggested that EutL might form hexamers and further assemble into the flat facets of the polyhedral outer shell of eut organelles at present no experimental evidence directly supports this view. EutL proteins contain two tandem BMC domains. This CD includes domain 2 (the second BMC domain of EutL)
RTGSYLSKTAGIAEGEALAYLIAPPLEAMYGLDAALKAADVELATFFPPPSETNFGGALLTGSQSACKAA
CNAFAEAVLEIAANPRE
>gnl|CDD|132891 cd07051, BMC_like_1_repeat1, Bacterial Micro-Compartment (BMC)-like domain 1 repeat 1. BMC-like domains exist in cyanobacteria, proteobacteria, and actinobacteria and are homologs of the carboxysome shell proteins. They might be encoded from putative organelles involved in unknown metabolic process. Although it has been suggested that these carboxysome shell protein homologs form hexamers and further assemble into the flat facets of the polyhedral bacterial organelles shell at present no experimental evidence exists to directly support this view. Proteins in this CD contain two tandem BMC domains. This CD includes repeat 1 (the first BMC domain of BMC like 1 proteins)
ELRTYVFIDRLQPQLAAYMGTVSQGFLPVAGDASLWIEVAPGLAIHRVTDIALKAANVRPGVQVVERQFG
LLELHSRSQSEVLAAGDAVLDALGLTEEDRLKPKILSSQII
>gnl|CDD|132892 cd07052, BMC_like_1_repeat2, Bacterial Micro-Compartment (BMC)-like domain 1 repeat 2. BMC-like domains exist in cyanobacteria, proteobacteria, and actinobacteria and are homologs of the carboxysome shell proteins. They might be encoded from putative organelles involved in unknown metabolic process. Although it has been suggested that these carboxysome shell protein homologs form hexamers and further assemble into the flat facets of the polyhedral bacterial organelles shell at present no experimental evidence exists to directly support this view. Proteins in this CD contain two tandem BMC domains. This CD includes repeat 2 (the second BMC domain of BMC like 1 proteins)
HAQLINRNRRGSMLLPGQSLFVLEVEPAAYASLAANEAEKAAPITLVDVRMVGAFGRLYLSGTEADVRAA
RDAAIAALE
>gnl|CDD|132893 cd07053, BMC_PduT_repeat1, 1,2-propanediol utilization protein T (PduT), Bacterial Micro-Compartment (BMC) domain repeat 1. PduT proteins are homologs of the carboxysome shell protein. They are encoded within the pdu operon and might be required for the formation of the outer shell of the bacterial pdu polyhedral organelles which are involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduT might form hexamers and further assemble into the flat facets of the polyhedral outer shell of pdu organelles at present no experimental evidence directly supports this view. PduT proteins contain two tandem BMC domains repeats. This CD contains repeat 1 (the first BMC domain of PduT) as well as carboxysome shell protein sequence homolog, EutM protein, are also included in this CD. They too might exist as hexamers and might play similar functional roles in the construction of the eut organelle outer shell which still remains poorly understood
AIGLLELNSIAKGIEAADAMLKAANVELVLAKTICPGKYIIIVSGDVGAVQAAVDAGKEIGGKYVVDSFV
LPNVHP
>gnl|CDD|132894 cd07054, BMC_PduT_repeat2, 1,2-propanediol utilization protein T (PduT), Bacterial Micro-Compartment (BMC) domain repeat 2. PduT proteins are homologs of the carboxysome shell protein. They are encoded within the pdu operon and might be required for the formation of the outer shell of the bacterial pdu polyhedral organelles which are involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduT might form hexamers and further assemble into the flat facets of the polyhedral outer shell of pdu organelles, at present no experimental evidence directly supports this view. PduT proteins contain two tandem BMC domains repeats. This CD contains repeat 2 (the second BMC domain of PduT) as well as carboxysome shell protein sequence homolog, EutM protein, are also included in this CD. They too might exist as hexamers and might play similar functional roles in the construction of the eut organelle outer shell which still remains poorly understood
ALGVIETFSVASGIVAADAALKAADVQLIEIRLAMGIGGKSFVVLTGDVSAVEAAVEAAEAVVGEKGLLV
DSVVIPSP
>gnl|CDD|132895 cd07055, BMC_like_2, Bacterial Micro-Compartment (BMC)-like domain 2. BMC like 2 domains exist in cyanobacteria, proteobacteria, and actinobacteria and are homologs of carboxysome shell proteins. They might be encoded from putative organelles involved in unknown metabolic process. Although it has been suggested that these carboxysome shell protein homologs form hexamers and further assemble into the flat facets of the polyhedral bacterial organelles shell at present no experimental evidence exists to directly support this view
AIGLMQGKVIDMIYAADIAEKASGVFVSDIFGSCPQHMITLAIFGETSAVELAMREIEEDA
>gnl|CDD|132896 cd07056, BMC_PduK, 1,2-propanediol utilization protein K (PduK), Bacterial Micro-Compartment (BMC) domain repeat 1l. PduK proteins are homologs of the carboxysome shell protein. They are encoded within the pdu operon and might be required for the formation of the outer shell of the bacterial pdu polyhedral organelles which are involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduK might form hexamers and further assemble into the flat facets of the polyhedral outer shell of pdu organelles at present no experimental evidence directly supports this view
SLGLLEVSGLSGAIVVADRMAKTANVRLLGLENTKGSGWMTVKISGDVAAVNAAIEAGKQTAGASDGYVA
STVIARP
>gnl|CDD|132897 cd07057, BMC_CcmK, Carbon dioxide concentrating mechanism (CcmK); Bacterial Micro-Compartment (BMC) domain. CcmK1-4 and CcmL proteins found in Synechocystis sp. strain PCC 6803 make up the beta carboxysome shell. These CcmK proteins have been shown to form hexameric units, while the CcmL proteins have been shown to form pentameric units. Together these proteins further assemble into the flat facets of the polyhedral carboxysome shell. The structures suggest that the central pores and the gaps between hexamers limit the transport of metabolites into and out of the the carboxysome
AVGMIETLGFPAVLAAADAMVKAARVTLVGYEKIGSGRCTVIVRGDVAEVKAAVEAGIEAAERVHGGEVL
SHTIIPRPHENLEAVLPI
>gnl|CDD|132898 cd07058, BMC_CsoS1, Carboxysome Shell 1 (CsoS1); Bacterial Micro-Compartment (BMC) domain. The cso operon in Halothiobacillus neapolitanus contains the genes involved in alpha carboxysome function including those for the carboxysome shell proteins: CsoS1A, CsoS1B, and CsoS1C. CsoS1A has been shown to form hexameric units which further assemble into the flat facets of the polyhedral carboxysome shell. The structures suggest that the central pores and the gaps between hexamers limit the transport of metabolites into and out of the the carboxysome. Although it has been suggested that other homologous proteins, CsoS1B and CsoS1C, in this family might also form hexamers and play similar functional roles in the construction of carboxysome outer shell at present no experimental evidence directly supports this view
GIALGMIETRGLVPAIEAADAMTKAAEVRLIGRQFVGGGYVTVLVRGETGAVNAAVRAGADACERVGDGL
VAAHIIARVHSEVENILP
>gnl|CDD|132899 cd07059, BMC_PduA, 1,2-propanediol utilization protein A (PduA), Bacterial Micro-Compartment (BMC) domain. PduA is encoded within the 1,2-propanediol utilization (pdu) operon along with other homologous carboxysome shell proteins PduB, B', J, K, T, and U. PduA is thought to be required for the formation of the outer shell of bacterial pdu polyhedral organelles which are involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduA might form hexamers and further assemble into the flat facets of the polyhedral outer shell of pdu organelles, like PduU does, at present no experimental evidence directly supports this view
ALGMIETKGLVGAIEAADAMVKAANVTLVGKEQIGGGLVTVMVRGDVGAVKAATDAGAAAAERVGELVSV
HVIPRPHTEVEKILP
>gnl|CDD|349952 cd07060, SPOUT_MTase, SPOUT superfamily of SAM-dependent RNA methyltransferases. The SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, also known as class IV methyltransferase family, is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot. Members of the SPOUT superfamily that have been characterized functionally are involved in post-transcriptional RNA modification by catalyzing methylation of the 2-OH group of ribose, the N-1 atom of guanosine 37 in tRNA, or the N-3 atom of uridine 1498 in 16S rRNA
RIVIDEKKIPEKVDKIIRAALAEYAKRLSIYGIVTLSSEGFAVKISELEISGGSNIAFVIGGEYGGLEES
ARALADEPISISSMTLSAELAATILLEQL
>gnl|CDD|132717 cd07061, HP_HAP_like, Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His residue which is phosphorylated during the reaction. Catalytic domain of HAP (histidine acid phosphatases) and phytases (myo-inositol hexakisphosphate phosphohydrolases). The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. Functions in this subgroup include roles in metabolism, signaling, or regulation, for example Escherichia coli glucose-1-phosphatase functions to scavenge glucose from glucose-1-phosphate and the signaling molecules inositol 1,3,4,5,6-pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) are in vivo substrates for eukaryotic multiple inositol polyphosphate phosphatase 1 (Minpp1). Phytases scavenge phosphate from extracellular sources and are added to animal feed while prostatic acid phosphatase (PAP) has been used for many years as a serum marker for prostate cancer. Recently PAP has been shown in mouse models to suppress pain by functioning as an ecto-5prime-nucleotidase. In vivo it dephosphorylates extracellular adenosine monophosphate (AMP) generating adenosine,and leading to the activation of A1-adenosine receptors in dorsal spinal cord
ELEQVQVLSRHGDRYPGELTPFGRQQAFELGRYFRQRYGELLLLHSYNRSDLYIRSSDSQRTLQSAQAFL
AGLFPPDGWQPIAVHTIPEEEDDVSNLFDLCAYETVAKGYSAPFCDLFTEEEWVKLEYLNDLKFYYGYGP
GNPLARAQGSPLLNELLARLTNGPSGSQTFPLDRKLYLYFSHDTTILPLLTALGLFDFAEPLPPDFLRGF
SESDYPPFAARLVFELWRCPGDGESYVRVLVN
>gnl|CDD|132883 cd07062, Peptidase_S66_mccF_like, Microcin C7 self-immunity protein determines resistance to exogenous microcin C7. Microcin C7 self-immunity protein (mccF): MccF, a homolog of the LD-carboxypeptidase family, mediates resistance against exogenously added microcin C7 (MccC7), a ribosomally-encoded peptide antibiotic that contains a phosphoramidate linkage to adenosine monophosphate at its C-terminus. The plasmid-encoded mccF gene is transcribed in the opposite direction to the other five genes (mccA-E) and is required for the full expression of immunity but not for production. The catalytic triad residues (Ser, His, Glu) of LD-carboxypeptidase are also conserved in MccF, strongly suggesting that MccF shares the hydrolytic activity with LD-carboxypeptidases. Substrates of MccF have not been deduced, but could likely be microcin C7 precursors. The possible role of MccF is to defend producer cells against exogenous microcin from re-entering after having been exported. It is suggested that MccF is involved in microcin degradation or sequestration in the periplasm
DTIAVVSPSSGIPGELPHRLERAKKRLENLGFEVVEGPNALKGDKYLSASPEERAEELMAAFADPSIKAI
IPTIGGDDSNELLPYLDYELIKKNPKIFIGYSDITALHLAIYKKTGLVTYYGPNLLDFFGEDEELLDYTL
QLFLKALFEKEQIESTPPDSWTDERDDWEEDEKTRWRRPGYWVLQGKGKVEGRLIGGCLDTLLLLAGTPY
MPDPYKLEGKILFLETSELSPATVERALRQLKLAGVFDKISGIIFGRPQDEEDKGTEETYEDILLEVLGD
LDIPIVYDVDFGHTPPQLTLPIGAKAEV
>gnl|CDD|132881 cd07064, AlkD_like_1, A new structural DNA glycosylase containing HEAT-like repeats. This domain represents a new and uncharacterized structural superfamily of DNA glycosylases that form an alpha-alpha superhelix fold that are not belong to the identified five structural DNA glycosylase superfamilies (UDG, AAG/MNPG, MutM/Fpg and helix-hairpin-helix). DNA glycosylases removing alkylated base residues have been identified in all organisms investigated and may be universally present in nature. DNA glycosylases catalyze the first step in Base Excision Repair (BER) pathway by cleaving damaged DNA bases within double strand DNA to produce an abasic site. The resulting abasic site is further processed by AP endonuclease, phosphodiesterase, DNA polymerases, and DNA ligase functions to restore the DNA to an undamaged state. All glycosylase examined to date utilize a similar strategy for binding DNA and base flipping despite their structural diversity. The known structures for members of this family, AlkC and AlkD from Bacillus cereus, are distant homologues and are composed of six variant HEAT (Huntington/Elongation/ A subunit/Target of rapamycin) repeats. HEAT motifs are ~45-amino acid sequences that form antiparallel alpha-helices, which are packed by a conserved hyrophobic interface and are tandemly repeated to form superhelical alpha-structures. AlkD and AlkC are specific for removal of 3-methyladenine (3mA) and 7-methylguanine (7mG) from the DNA by base excision repair. Homologues of AlkC and AlkD were also identified in other organisms
HADPERAAAMKAYMKNQFPFYGIKTPERRALSKPFLKESKLPDKEELWELVLELWQQPEREYQYVAIDLL
RKYKKFLTPEDLPLLEELITTKSWWDTVDSLAKVVGGILLADYPEFEPVMDEWSTDENFWLRRTAILHQL
KYKEKTDTDLLFEIILANLGSKEFFIRKAIGWALREYSKTNPDWVRDFVAAHKLRLSPLSRREALKYL
>gnl|CDD|143549 cd07066, CRD_FZ, CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain. CRD_FZ is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines
KCEPIPLPLCRGLPYNTTRFPNLLGHESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGDRP
IPPCRSLCEEVRDSCEPLMLAFGFPWPEPLDCDRFPDSNEEGLCISPPG
>gnl|CDD|132718 cd07067, HP_PGM_like, Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction. Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG
RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEEL
PGLPVEVDPRLREARVLPALEELIAPHDGKNVLIVSHGGVLRALLAYLLGLSDEDILRLNLPNGSISVLE
LDENGGGVLLLRL
>gnl|CDD|132753 cd07068, NR_LBD_ER_like, The ligand binding domain of estrogen receptor and estrogen receptor-related receptors. The ligand binding domain of estrogen receptor (ER) and estrogen receptor-related receptors (ERRs): Estrogen receptors are a group of receptors which are activated by the hormone estrogen. Estrogen regulates many physiological processes including reproduction, bone integrity, cardiovascular health, and behavior. The main mechanism of action of the estrogen receptor is as a transcription factor by binding to the estrogen response element of target genes upon activation by estrogen and then recruiting coactivator proteins which are responsible for the transcription of target genes. Additionally some ERs may associate with other membrane proteins and can be rapidly activated by exposure of cells to estrogen. ERRs are closely related to the estrogen receptor (ER) family. But, it lacks the ability to bind estrogen. ERRs can interfere with the classic ER-mediated estrogen signaling pathway, positively or negatively. ERRs share target genes, co-regulators and promoters with the estrogen receptor (ER) family. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, ER and ERRs have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
LLSALLVAEPDKLYAMNDPTGPDTEVSLLATLSDLADRELVHIISWAKHIPGFSDLSLNDQMHLLQSAWL
EILMLGLVWRSLPHPGKLVFAPDLLLDREQARVEGLLEIFDMLLQLVRRFRELGLQREEYVCLKAIILAN
SDVRHLEDREAVQQLRDAILDALVDVEAKRHGSQQPRRLAQLLLLLPHLRQASNKGVRHLYSVKCEGKVP
MYKLFLEMLEA
>gnl|CDD|132754 cd07069, NR_LBD_Lrh-1, The ligand binding domain of the liver receptor homolog-1, a member of nuclear receptor superfamily,. The ligand binding domain (LBD) of the liver receptor homolog-1 (LRH-1): LRH-1 belongs to nuclear hormone receptor superfamily, and is expressed mainly in the liver, intestine, exocrine pancreas, and ovary. Most nuclear receptors function as homodimer or heterodimers. However, LRH-1 binds DNA as a monomer, and is a regulator of bile-acid homeostasis, steroidogenesis, reverse cholesterol transport and the initial stages of embryonic development. Recently, phospholipids have been identified as potential ligand for LRH-1 and steroidogenic factor-1 (SF-1). Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, LRH-1 has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
IPHLILELLKCEPDEPQVQAKIMAYLQQEQANRSKHEKLSTFGLMCKMADQTLFSIVEWARSSIFFRELK
VDDQMKLLQNCWSELLILDHIYRQVVHGKEGSIFLVTGQQVDYSIIASQAGATLNNLMSHAQELVAKLRS
LQFDQREFVCLKFLVLFSLDVKNLENFQLVEGVQEQVNAALLDYTMCNYPQQTEKFGQLLLRLPEIRAIS
MQAEEYLYYKHLNGDVPYNNLLIEMLHAKRA
>gnl|CDD|132755 cd07070, NR_LBD_SF-1, The ligand binding domain of nuclear receptor steroidogenic factor 1, a member of nuclear receptor superfamily. The ligand binding domain of nuclear receptor steroidogenic factor 1 (SF-1): SF-1, a member of the nuclear hormone receptor superfamily, is an essential regulator of endocrine development and function and is considered a master regulator of reproduction. Most nuclear receptors function as homodimer or heterodimers, however SF-1 binds to its target genes as a monomer, recognizing the variations of the DNA sequence motif, T/CCA AGGTCA. SF-1 functions cooperatively with other transcription factors to modulate gene expression. Phospholipids have been determined as potential ligands of SF-1. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, SF-1 has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
VPELILQLLQLEPDEDQVRARILGCLQEPQKSRPDQPAPFGLLCRMADQTFISIVDWARRCMVFKELEVA
DQMTLLQNCWSELLVFDHIYRQVQHGKEGSILLVTGQEVELSTVAAQAGSLLHSLVLRAQELVLQLHALQ
LDRQEFVCLKFLILFSLDVKFLNNHSLVKDAQEKANAALLDYTLCHYPHCGDKFQQLLLRLVEVRALSMQ
AKEYLYHKHLGNEMPRNNLLIEMLQAK
>gnl|CDD|132756 cd07071, NR_LBD_Nurr1, The ligand binding domain of Nurr1, a member of conserved family of nuclear receptors. The ligand binding domain of nuclear receptor Nurr1: Nurr1 belongs to the conserved family of nuclear receptors. It is a transcription factor that is expressed in the embryonic ventral midbrain and is critical for the development of dopamine (DA) neurons. Structural studies have shown that the ligand binding pocket of Nurr1 is filled by bulky hydrophobic residues, making it unable to bind to ligands. Therefore, it belongs to the class of orphan receptors. However, Nurr1 forms heterodimers with RXR and can promote signaling via its partner, RXR. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, Nurr1 has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
PVSLISALVRAHVDSNPAMTSLDYSRFQANPDYQMSGDDTQHIQQFYDLLTGSMEIIRGWAEKIPGFTDL
PKADQDLLFESAFLELFVLRLAYRSNPVEGKLIFCNGVVLHRLQCVRGFGEWIDSIVEFSSNLQNMNIDI
SAFSCIAALAMVTERHGLKEPKRVEELQNKIVNCLKDHVTFNNGGLNRPNYLSKLLGKLPELRTLCTQGL
QRIFYLKLEDLVPPPAIIDKLFLDTLPF
>gnl|CDD|132757 cd07072, NR_LBD_DHR38_like, Ligand binding domain of DHR38_like proteins, members of the nuclear receptor superfamily. The ligand binding domain of nuclear receptor DHR38_like proteins: DHR38 is a member of the steroid receptor superfamily in Drosophila. DHR38 interacts with the USP component of the ecdysone receptor complex, suggesting that DHR38 might modulate ecdysone-triggered signals in the fly, in addition to the ECR/USP pathway. At least four differentially expressed mRNA isoforms have been detected during development. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, DHR38 has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
PPVSLITALVRAHVDTSPDFANLDYSQYREPSPLEPPMSEAEKVQQFYSLLTSSIDVIKTFAEKIPGFPD
LCKEDQELLFQSASLELFVLRLAYRTAPEDTKLTFCNGVVLHKQQCQRSFGDWLHAILEFSKSLHAMDID
ISAFACLCALTLITERHGLKEPHKVEQLQMKIISSLRDHVTYNAEAQKKPHYFSRLLGKLPELRSLSVQG
LQRIFYLKLEDLVPAPPLIENMFVASLPF
>gnl|CDD|132758 cd07073, NR_LBD_AR, Ligand binding domain of the nuclear receptor androgen receptor, ligand activated transcription regulator. The ligand binding domain of the androgen receptor (AR): AR is a member of the nuclear receptor family. It is activated by binding either of the androgenic hormones, testosterone or dihydrotestosterone, which are responsible for male primary sexual characteristics and for secondary male characteristics, respectively. The primary mechanism of action of ARs is by direct regulation of gene transcription. The binding of an androgen results in a conformational change in the androgen receptor which causes its transport from the cytosol into the cell nucleus, and dimerization. The receptor dimer binds to a hormone response element of AR-regulated genes and modulates their expression. Another mode of action is independent of their interactions with DNA. The receptors interact directly with signal transduction proteins in the cytoplasm, causing rapid changes in cell function, such as ion transport. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, AR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD). The LBD is not only involved in binding to androgen, but also involved in binding of coactivator proteins and dimerization. A ligand dependent nuclear export signal is also present at the ligand binding domain
IFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSW
MGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALL
LFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLL
IKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFH
>gnl|CDD|132759 cd07074, NR_LBD_PR, Ligand binding domain of the progesterone receptor, a member of the nuclear hormone receptor. The ligand binding domain of the progesterone receptor (PR): PR is a member of the nuclear receptor superfamily of ligand dependent transcription factors, mediating the biological actions of progesterone. PR functions in a variety of biological processes including development of the mammary gland, regulating cell cycle progression, protein processing, and metabolism. When no binding hormone is present the carboxyl terminal inhibits transcription. Binding to a hormone induces a structural change that removes the inhibitory action. After progesterone binds to the receptor, PR forms a dimer and the complex enters the nucleus where it interacts with the hormone response element (HRE) in the promoters of progesterone responsive genes and alters their transcription. In addition, rapid actions of PR that occur independent of transcription, have also been observed in several tissues like brain, liver, mammary gland and spermatozoa. There are two natural PR isoforms called PR-A and PR-B. PR-B has an additional stretc h of 164 amino acids at the N terminus. The extra domain in PR-B performs activation functions by recruiting coactivators that could not be recruited by PR-A. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, PR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD). The LBD is not only involved in binding to progesterone, but also involved in coactivator binding and dimerization
PLINLLMSIEPDVVYAGYDNTKPETPSSLLTSLNQLCERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSW
MSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKALL
LLNTIPLEGLRSQTQFDEMRSSYIRELIKAIGLRQKGVVASSQRFYQLTKLMDNMHDLVKQLHLYCLNTF
IQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK
>gnl|CDD|132760 cd07075, NR_LBD_MR, Ligand binding domain of the mineralocorticoid receptor, a member of the nuclear receptor superfamily. The ligand binding domain of the mineralocorticoid receptor (MR): MR, also called aldosterone receptor, is a member of nuclear receptor superfamily involved in the regulation of electrolyte and fluid balance. The receptor is activated by mineralocorticoids such as aldosterone and deoxycorticosterone as well as glucocorticoids, like cortisol and cortisone. Binding of its ligand results in its translocation to the cell nucleus, homodimerization and binding to hormone response elements (HREs) present in the promoter of MR controlled genes. This results in the recruitment of the coactivators and the transcription of the activated genes. MR is expressed in many tissues and its activation results in the expression of proteins regulating electrolyte and fluid balance. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, MR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD). The LBD, in addition to binding ligand, contains a ligand-dependent activation function-2 (AF-2)
SPVMVLENIEPEIVYAGYDSSKPDTAENLLSTLNRLAGKQMIQVVKWAKVLPGFRNLPLEDQITLIQYSW
MCLSSFALSWRSYKHTNSQFLYFAPDLVFNEERMHQSAMYELCQGMHQISLQFVRLQLTFEEYTIMKVLL
LLSTIPKDGLKSQAAFEEMRTNYIKELRKMVTKAPNNSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTF
RESQALKVEFPAMLVEIISDQLPKVESGNAKPLYFHRK
>gnl|CDD|132761 cd07076, NR_LBD_GR, Ligand binding domain of the glucocorticoid receptor, a member of the nuclear receptor superfamily. The ligand binding domain of the glucocorticoid receptor (GR): GR is a ligand-activated transcription factor belonging to the nuclear receptor superfamily. It binds with high affinity to cortisol and other glucocorticoids. GR is expressed in almost every cell in the body and regulates genes controlling a wide variety of processes including the development, metabolism, and immune response of the organism. In the absence of hormone, the glucocorticoid receptor (GR) is complexes with a variety of heat shock proteins in the cytosol. The binding of the glucocorticoids results in release of the heat shock proteins and transforms it to its active state. One mechanism of action of GR is by direct activation of gene transcription. The activated form of GR forms dimers, translocates into the nucleus, and binds to specific hormone responsive elements, activating gene transcription. GR can also function as a repressor of other gene transcription activators, such as NF-kappaB and AF-1 by directly binding to them, and bloc king the expression of their activated genes. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, GR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD). The LBD also functions for dimerization and chaperone protein association
TLVSLLEVIEPEVLYSGYDSSVPDSTWRIMSTLNMLGGRQVVAAVKWAKAIPGFRNLHLDDQMTLLQYSW
MFLMAFALGWRSYRQSNGNLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLL
LLSTVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNFCFQTF
LDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK
>gnl|CDD|143396 cd07077, ALDH-like, NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family. The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group
ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNI
DTERGITASVGHIQDVLLPDNGETYVRAFPIGVTMHILPSTNPLSGITSALRGIATRNQCIFRPHPSAPF
TNRALALLFQAADAAHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFG
AGNSPVVVDETADEERASGSVHDSKFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETKPL
SKETTPSFDDEALESMTPLECQFRVLDVISAVENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASF
YPNESSKKGRGAFAGKGVERIVTSGMNNIFGAGVGHDALRPLKRLVR
>gnl|CDD|143397 cd07078, ALDH, NAD(P)+ dependent aldehyde dehydrogenase family. The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group
DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYA
GLARRLHGEVIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTAL
LLAELLAEAGLPPGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKS
PLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGP
LISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKD
EEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPSAPFGGVKQSGIGREGGPYG
LEEYTEPKTVTI
>gnl|CDD|143398 cd07079, ALDH_F18-19_ProA-GPR, Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19. Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1)
EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAGLSEALLDRLLLTPER
IEAMAEGLRQVAALPDPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVIL
RGGSEALHSNRALVEIIQEALEEAGLPEDAVQLIPDTDREAVQELLKLDDYIDLIIPRGGAGLIRFVVEN
ATIPVIKHGDGNCHVYVDESADLEMAVRIVVNAKTQRPSVCNALETLLVHRDIAEEFLPKLAEALREAGV
ELRGDEETLAILPGAKPATEEDWGTEYLDLILAVKVVDSLDEAIAHINRYGSGHTEAIVTENYETAERFL
REVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELTTYKYIVRGD
>gnl|CDD|143399 cd07080, ALDH_Acyl-CoA-Red_LuxC, Acyl-CoA reductase LuxC. Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN
TLSAPDLDALIEELRLNRRALAALPVEEIVDFLDRAGKRLLDPDYPLRQQAERLLPTVTGYSEEMLREGL
KRLMALFRRENLERILERELGSPGILDEWVPPGRGGYIRAQPRGLVVHIIAGNVPLLPVWSIVRGLLVKN
VNLLKMSSSDPLTATALLRSLADVDPNHPLTDSISVVYWPGGDAELEERILASADAVVAWGGEEAVKAIR
SLLPPGCRLIDFGPKYSFAVIDREALESEKLAEVADALAEDICRYDQQACSSPQVVFVEKDDDEELREFA
EALAAALERLPRRYPALSLSAAESAKIARARLEAEFYELKGGVSRDLGWTVIISDEIGLEASPLNRTVNV
KPVASLDDVLRPVTPYLQTVGLAPSPAELAELADALAAAGVDRIVALGTMNDFQSGWHHDGMFPLQRLVR
WV
>gnl|CDD|143400 cd07081, ALDH_F20_ACDH_EutE-like, Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins. Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway
LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYN
VYKDEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQR
AATLLLQAAVAAGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGKPAIGVGAGNTP
VVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVILK
NGDVNRDIVGQDAYKIAAAAGLKVPQETRILIGEVTSLAEHEPFAHEKLSPVLAMYRAANFADADAKALA
LKLEGGCGHTSAMYSDNIKAIENMNQFANAMKTSRFVKNGPCSQGGLGDLYNFRGWPSMTLGCGTWGGNS
VSENVGPKHLVNLKTVALR
>gnl|CDD|143401 cd07082, ALDH_F11_NP-GAPDH, NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11. NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants
QFKYLINGEWKESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLEERIDCLHKF
ADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQVRRE
PLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGRE
IGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQ
RCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNG
GGREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKL
ADALEVGTVNINSKCQRGPDHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN
>gnl|CDD|143402 cd07083, ALDH_P5CDH, ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like. ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH
RRAMREALRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKT
WKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEV
VPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFP
PGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDE
TADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQ
EAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDFAEALE
VANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRF
LEMKAVAERF
>gnl|CDD|143403 cd07084, ALDH_KGSADH-like, ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like. ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway
PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARA
FVIYSYRIPHEPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVS
IVMQIMVRLLHYAGLLPPEDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAG
FNWKVLGPDAQAVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWSKTPLVEKLKALLARRKLEDLLLGPV
QTFTTLAMIAHMENLLGSVLLFSGKELKNHSIPSIYGACVASALFVPIDEILKTYELVTEEIFGPFAIVV
EYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADP
RGAGIGGPEAIKLVWRCHAEQA
>gnl|CDD|143404 cd07085, ALDH_F6_MMSDH, Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2. Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD
LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFR
QLLEENLDELARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVV
AGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALL
DHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMA
LSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGV
KVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAAR
KFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW
>gnl|CDD|143405 cd07086, ALDH_F7_AASADH-like, NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins. ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105)
GVIGGEWVGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEAL
RKKKEALGRLVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVI
TAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELL
VHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCT
TTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKR
IDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFR
WLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS
>gnl|CDD|143406 cd07087, ALDH_F3-13-14_CALDH-like, ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins. ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate
AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHA
LKHLKKWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAP
ATSALLAKLIPKYFDPEAVAVVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGK
SPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGR
IINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEF
INSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGNSGMGAYHGKAGFDTFSH
LKSVLK
>gnl|CDD|143407 cd07088, ALDH_LactADH-AldA, Escherichia coli lactaldehyde dehydrogenase AldA-like. Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD
YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLI
RENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGI
LPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAH
PKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAE
RVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEG
EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNE
LEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL
>gnl|CDD|143408 cd07089, ALDH_CddD-AldA-like, Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins. The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD
VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEV
GAPVMTARAMQVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLN
LAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTG
STAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYD
EVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGRPAGLDKGFYVEPT
LFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN
GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY
>gnl|CDD|143409 cd07090, ALDH_F9_TMBADH, NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1. NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis
VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNG
KPIEEARVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPA
LACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKV
MSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVE
RTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLCGGERVVPEDGLENGFYVSPCVLTDC
TDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNIS
PVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG
>gnl|CDD|143410 cd07091, ALDH_F1-2_Ald2-like, ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins. ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences
EQPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRL
LNKLADLIERDRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRRE
PIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPT
AGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFN
QGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATL
LTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDIN
KALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI
>gnl|CDD|143411 cd07092, ALDH_ABALDH-YdcW, Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like. NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency
VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTG
KPLHLVRDDELPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIA
PALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGK
KVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAAL
VEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDD
EIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEM
PHGGFKQSGYGKDLSIYALEDYTRIKHVMV
>gnl|CDD|143412 cd07093, ALDH_F8_HMSADH, Human aldehyde dehydrogenase family 8 member A1-like. In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone
NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTG
KPITLARTRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAP
ALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGR
TIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERF
VERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATILTGGGRPELPDLEGGYFVEPTVITG
LDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLV
RDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI
>gnl|CDD|143413 cd07094, ALDH_F21_LactADH-like, ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins. ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences
LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACE
GGKPIKDARVEVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLV
AHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTG
SAAVGEALRANAGGKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEF
IEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGERDGALFKPTVLEDVPR
DTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRT
DWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI
>gnl|CDD|143414 cd07095, ALDH_SGSD_AstD, N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like. N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate
QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDI
SIKAYHERTGERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVA
ELMVELWEEAGLPPGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGN
NPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFM
GPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLSPGIIDVTDAADVPDEEIFGPLLQVYRYDD
FDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGASSTAPFGGVGLSGNHRPSAYYA
ADYCAYPVASL
>gnl|CDD|143415 cd07097, ALDH_KGSADH-YcbD, Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like. Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group
YRNYIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGD
ELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVG
LITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALV
EHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTA
SSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERL
KRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHF
KRRVEAGVVMVNLPTAGVDYHVPFGGRKGSSYGPREQGEAALEFYTTIKTVYV
>gnl|CDD|143416 cd07098, ALDH_F15-22, Aldehyde dehydrogenase family 15A1 and 22A1-like. Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation
YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGK
TMVDASLGEILVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGP
IIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIG
SPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYD
KLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFP
PTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVA
INDFGVNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTEDR
>gnl|CDD|143417 cd07099, ALDH_DDALDH, Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like. The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid
RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGK
PRADAGLEVLLALEAIDWAARNAPRVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDI
IPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAGVDKVAFTGSVATGR
KVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARL
VAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHD
MDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGI
PALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR
>gnl|CDD|143418 cd07100, ALDH_SSADH1_GabD1, Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like. Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate
IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYY
AENAEAFLADEPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCAL
AIEELFREAGFPEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDP
FIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPL
ARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEE
EAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVKRSGYGRELGRFGIRE
FVNIKTVWV
>gnl|CDD|143419 cd07101, ALDH_SSADH2_GabD2, Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like. Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however, the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s)
EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGK
ARRHAFEEVLDVAIVARYYARRAERLLKPRRRRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAI
PALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADYVMFTGSTATGRV
VAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFV
ARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLGPYFYEPTVLTGVTED
MELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAAAWA
SIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV
>gnl|CDD|143420 cd07102, ALDH_EDX86601, Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601). Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD
ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGR
PIAQAGGEIRGMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPA
LLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAI
QRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVA
VVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALFPEDKAGGAYLAPTVLTNVDH
SMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCDYLDP
ALAWTGVKDSGRGVTLSRLGYDQLTRPKSYHL
>gnl|CDD|143421 cd07103, ALDH_F5_SSADH_GabD, Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like. Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species
VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQG
KPLAEARGEVDYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAP
ALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGK
LLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKL
VERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDD
MLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAE
APFGGVKESGLGREGGKEGLEEYLETKYVSL
>gnl|CDD|143422 cd07104, ALDH_BenzADH-like, ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins. ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences
DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILRE
AAGLPRRPEGEILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVT
GGLLIAEIFEEAGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELG
GNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTV
IGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDD
EEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDEPHVPFGGVKASGGGRFGGPASL
EEFTEWQWITV
>gnl|CDD|143423 cd07105, ALDH_SaliADH, Salicylaldehyde dehydrogenase, DoxF-like. Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD
DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLRE
AASLITQIIGGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRT
HWLIGRVFHEAGLPKGVLNVVTHSPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLE
LGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVLGS
LVSAAAADRVKELVDDALSKGAKLVVGGLADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKD
EEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDEPTLPHGGVKSSGYGRFNGKWG
IDEFTETKWITI
>gnl|CDD|143424 cd07106, ALDH_AldA-AAD23400, Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like. Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD
VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQG
KPLAEAQFEVGGAVAWLRYTASLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALL
AGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMAS
AAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAK
AAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVD
EEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGG
HKQSGIGVEFGIEGLKEYTQTQVINI
>gnl|CDD|143425 cd07107, ALDH_PhdK-like, Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like. Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD
VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCG
NPVSAMLGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAP
LAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAI
MRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVV
ERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGRPEGPALEGGFYVEPTVFADV
TPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRH
FLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL
>gnl|CDD|143426 cd07108, ALDH_MGR_2402, Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like. NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402), and other similar sequences, are present in this CD
VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETG
NALRTQARPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAP
ALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKI
IYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKL
VAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLSTSGATVLRGGPLPGEGPLADGFFVQPTIFS
GVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGG
GQQPGQSYGGFKQSGLGREASLEGMLEHFTQKKTVNI
>gnl|CDD|143427 cd07109, ALDH_AAS00426, Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like. Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD
VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDT
GKPLTQARADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAP
ALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGI
AVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERL
VERFRALRVGPGLEDPDLGPLISAKQLDRVEGFVARARARGARIVAGGRIAEGAPAGGYFVAPTLLDDVP
PDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGG
GIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV
>gnl|CDD|143428 cd07110, ALDH_F10_BADH, Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like. Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine
VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNG
KPLDEAAWDVDDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWK
VAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTA
TGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFL
ERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGARLLCGGRRPAHLEKGYFIAPTVFA
DVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCSQ
PCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQITR
>gnl|CDD|143429 cd07111, ALDH_F16, Aldehyde dehydrogenase family 16A1-like. Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence
YGPAPESAACALAWLDAHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAART
AFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDT
ELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIV
TGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDA
IWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAE
GADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWS
ENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWEPA
>gnl|CDD|143430 cd07112, ALDH_GABALDH-PuuC, Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like. NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD
GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELAL
LETLDMGKPISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLM
AAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFT
GSTEVGRRFLEYSGQSNLKRVWLECGGKSPNIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHES
IKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRVLTETGGFFV
EPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTV
WVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI
>gnl|CDD|143431 cd07113, ALDH_PADH_NahF, Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like. NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate
GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPAERGRILLRLA
DLIEQHGEELAQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIPSMQGERYTAFTRR
EPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA
VGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQ
GQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIV
RGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSK
ALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY
>gnl|CDD|143432 cd07114, ALDH_DhaS, Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like. Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD
SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRD
NGKLIRETRAQVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKL
APALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTET
GRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVE
RLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSGADLGAGYFFEPTIL
ADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTY
RALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI
>gnl|CDD|143433 cd07115, ALDH_HMSADH_HapE, Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like. 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD
TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTG
KPIRAARRLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAP
ALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGR
KIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERF
TSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPE
MRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINTYNRFDPG
SPFGGYKQSGFGREMGREALDEYTEVKSVWVNL
>gnl|CDD|143434 cd07116, ALDH_ACDHII-AcoD, Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like. Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression
YDNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIA
DRMEANLEMLAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVV
GQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLA
SSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFADVMDADDAFFDKALEGFVMFALNQG
EVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLT
GGERNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDG
NTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLVSY
>gnl|CDD|143435 cd07117, ALDH_StaphAldA1, Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like. Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD
YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIA
DIIDENKELLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVV
GQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLL
NHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCA
GSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRL
TENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRAL
RVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL
>gnl|CDD|143436 cd07118, ALDH_SNDH, Gluconobacter oxydans L-sorbosone dehydrogenase-like. Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase
RRSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLE
SGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKL
PFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRV
GKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVA
AVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDV
TPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDG
SPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL
>gnl|CDD|143437 cd07119, ALDH_BADH-GbsA, Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like. Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde
YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIAD
KIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGL
ITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAE
SPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAG
SRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPT
GDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANR
VARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLSPQPIGWF
>gnl|CDD|143438 cd07120, ALDH_PsfA-ACA09737, Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like. Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural
SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDPRLRARVLLELADAFEANAERLARLLALEN
GKILGEARFEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAP
ALAAGCTVVVKPAGQTAQINAAIIRILAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATG
RAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDR
LAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPVTEGLAKGAFLRPTLLEV
DDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNK
LFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL
>gnl|CDD|143439 cd07121, ALDH_EutE, Ethanolamine utilization protein EutE-like. Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source
GVFATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLAA
EKTPGTEDLTTTAWSGDNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVS
AYAVELINKAIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSGKKAIGAGAGN
PPVVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQAEQLLEVV
LLTNKGATPNKKWVGKDASKILKAAGIEVPADIRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIEL
AVELEHGNRHTAIIHSKNVENLTKMARAMQTTIFVKNGPSYAGLGVGGEGYTTFTIAGPTGEGLTSARTF
TRRRRCVLV
>gnl|CDD|143440 cd07122, ALDH_F20_ACDH, Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like. Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway
VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFASEYVYN
DIKDMKTVGVIEEDEEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIE
AAKIMREAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGGPGMVKAAYSSGKPAIGVGPGNVP
AYIDETADIKRAVKDIILSKTFDNGTICASEQSVIVDDEIYDEVRAELKRRGAYFLNEEEKEKLEKALFD
DGGTLNPDIVGKSAQKIAELAGIEVPEDTKVLVAEETGVGPEEPLSREKLSPVLAFYRAEDFEEALEKAR
ELLEYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVNTPSSLGGIGDTYNGLAPSLTLGCGSWGGNSTSD
NVGPKHLLNIKRVAYR
>gnl|CDD|143441 cd07123, ALDH_F4-17_P5CDH, Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17. Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences
PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAAL
VEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLR
FNVKYAEELYAQQPLSSPAGVWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVL
SNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPR
IVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDP
DDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGP
VLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKPTGAVVGQQPFG
GARASGTNDKAGSPLNLLRWVSPRTIKETFVP
>gnl|CDD|143442 cd07124, ALDH_PutA-P5CDH-RocA, Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA. Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis
FRNEPFTDFADEENRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEE
AEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYY
AREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAA
KLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIA
EMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDP
EVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLA
VIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTG
SKAGGPDYLLQFMQPKTVTENF
>gnl|CDD|143443 cd07125, ALDH_PutA-P5CDH, Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA. The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12)), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes
ANSSFVNRIFDLEVPLEALADALKAFDEKEWEAIPIINGEETETGEGAPVIDPADHERTIGEVSLADAED
VDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYY
AAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIA
ARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPILPLIAET
GGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLST
DVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGNGYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKA
EDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAG
GPNYLLRFGNEKTVSLNTTAAGGNPSLL
>gnl|CDD|143444 cd07126, ALDH_F12_P5CDH, Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences
NLVAGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKNPERYLLYGDVSHR
VAHELRKPEVEDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLARSFNVPGDHQGQQSSGYR
WPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGP
TMNKILLEANPRMTLFTGSSKVAERLALELHGKVKLEDAGFDWKILGPDVSDVDYVAWQCDQDAYACSGQ
KCSAQSILFAHENWVQAGILDKLKALAEQRKLEDLTIGPVLTWTTERILDHVDKLLAIPGAKVLFGGKPL
TNHSIPSIYGAYEPTAVFVPLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAV
VSNDIRFLQEVLANTVNGTTYAGIRARTTGAPQNHWFGPAGDPRGAGIGTPEAIRLVWSCHREIITDIG
>gnl|CDD|143445 cd07127, ALDH_PAD-PaaZ, Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like. Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes
ALFDKHRATLDAAVEAIASRGYWSPFPESPSPKIYGETAAAAGKAAFEALLGQRFDLDQPGASGWVGGEV
SPYGVELGVTYPQCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMM
AFQAGGPHAQDRGLEAVAYAWREMSRIPPTAEWEKPQGKHDPLAMEKTFTVVPRGVALVIGCSTFPTWNG
YPGLFASLATGNPVIVKPHPAAILPLAITVQVAREVLAEAGFDPNLVTLAADTPEEPIAQTLATRPEVRI
IDFTGSNAFGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRD
GIQTDDGRKSFDEVAADLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFP
DARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVREHGAMTVGVYSTDPEVVERVQ
EAALDAGVALSINLTGGVFVNQSAAFSDFHGTGANPAANAALTDGAFVANRFRVVQRRR
>gnl|CDD|143446 cd07128, ALDH_MaoC-N, N-terminal domain of the monoamine oxidase C dehydratase. The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH
LQSYVAGQWHAGTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAK
YLMERKEDLYALSAATGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDVEPLSKDGTFVGQHI
LTPRRGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLLPEGALQLICG
SVGDLLDHLGEQDVVAFTGSAATAAKLRAHPNIVARSIRFNAEADSLNAAILGPDATPGTPEFDLFVKEV
AREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATL
LAEAEVVFGGPDRFEVVGADAEKGAFFPPTLLLCDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAAR
GRGSLVASVVTNDPAFARELVLGAAPYHGRLLVLNRDSAKESTGHGSPLPQLVHGGPGRAGGGEELGGLR
GVKHYMQRTAVQGSPTMLTAITG
>gnl|CDD|143447 cd07129, ALDH_KGSADH, Alpha-Ketoglutaric Semialdehyde Dehydrogenase. Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids
VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLF
ADLVREGSWLDARIDPADPDRQPLPRPDLRRMLVPLGPVAVFGASNFPLAFSVAGGDTASALAAGCPVVV
KAHPAHPGTSELVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAA
AARPEPIPFYAELGSVNPVFILPGALAERGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPAGDAFIAAL
AEALAAAPAQTMLTPGIAEAYRQGVEALAAAPGVRVLAGGAAAEGGNQAAPTLFKVDAAAFLADPALQEE
VFGPASLVVRYDDAAELLAVAEALEGQLTATIHGEEDDLALARELLPVLERKAGRLLFNGWPTGVEVCPA
MVHGGPYPATTDPRFTSVGTAAIERFLRPVCYQN
>gnl|CDD|143448 cd07130, ALDH_F7_AASADH, NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B. Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer
GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALR
KKKEALGKLVSLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVIT
AFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALV
KDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTT
TRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVI
DGPGNYVEPTIVEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGP
KGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS
>gnl|CDD|143449 cd07131, ALDH_AldH-CAJ73105, Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like. Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD
NYIGGEWVDSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAE
LLKKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVA
LITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALV
EHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTA
TSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERL
TGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAF
RARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNGHREAGTTALDAFTEWKAVYVDYS
>gnl|CDD|143450 cd07132, ALDH_F3AB, Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins. NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes
AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYA
ISNLPEWMKPEPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSP
ATAKLLAELIPKYLDKECYPVVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGK
SPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGR
IINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEF
INSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMGAYHGKYSFDTFSH
KRSCLVKSLNMEKLNSLRYPPYS
>gnl|CDD|143451 cd07133, ALDH_CALDH_CalB, Coniferyl aldehyde dehydrogenase-like. Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD
QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGHRSRHETLLAEILPSIAGIKH
ARKHLKKWMKPSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFT
PRTSALLAELLAEYFDEDEVAVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGG
KSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPDYTS
IINERHYARLQGLLEDARAKGARVIELNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYD
SLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMGAYHGK
EGFLTFSHAKPVFK
>gnl|CDD|143452 cd07134, ALDH_AlkH-like, Pseudomonas putida Aldehyde dehydrogenase AlkH-like. Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD
RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHA
IKHLKKWMKPKRVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTP
HTSAVIAKIIREAFDEDEVAVFEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGK
SPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPDL
ARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYED
LDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIGSYHGVY
GFKAFSHERAVLR
>gnl|CDD|143453 cd07135, ALDH_F14-YMR110C, Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins. Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD
YTPLDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGV
KNDILHMLKNLKKWAKDEKVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVV
LKPSELTPHTAALLAELVPKYLDPDAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTP
VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGA
NASPDYTRIVNPRHFNRLKSLLDTTKGKVVIGGEMDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIK
VDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGVGDSGYGAYH
GKYGFDTFTHERTVVK
>gnl|CDD|143454 cd07136, ALDH_YwdH-P39616, Bacillus subtilis aldehyde dehydrogenase ywdH-like. Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD
ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYA
IKHLKKWMKPKRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTP
NTSKVIAKIIEETFDEEYVAVVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGK
SPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGR
IINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEI
IKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGVGNSGMGSYHGKYSFDTFSH
KKSILKKSTWFDLPLRYPPYKGKKKKLKK
>gnl|CDD|143455 cd07137, ALDH_F3FHI, Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins. Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress
APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKL
AIKELKKWMAPEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELA
PATSALLAKLIPEYLDTKAIKVIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGG
KCPVIVDSTVDLKVAVRRIAGGKWGCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDL
SRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKI
EESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGESGFGAYHGKFS
FDAFSHKKAVLY
>gnl|CDD|143456 cd07138, ALDH_CddD_SSP0762, Rhodococcus ruber 6-oxolauric acid dehydrogenase-like. The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD
FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEA
YEARADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEERRGNSLVVREPIGVCGLITPW
NWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDV
DMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRML
VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEGLE
RGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRL
RAGQVHINGAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQG
>gnl|CDD|143457 cd07139, ALDH_AldA-Rv0768, Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like. The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD
LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLA
DALEARADELARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGV
VAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYL
VRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCV
ALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGR
PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLA
VARRIRTGTVGVNGFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL
>gnl|CDD|143458 cd07140, ALDH_F1L_FTFDH, 10-formyltetrahydrofolate dehydrogenase, ALDH family 1L. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids
TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRG
RLMYRLADLMEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNL
TLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINIL
PGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGM
SSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGV
KEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDVDGVLQRANDTEYGLAS
GVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIEY
>gnl|CDD|143459 cd07141, ALDH_F1AB_F2_RALDH1, NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like. NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism
NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASE
RGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTY
TRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPG
YGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEA
LFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKE
GAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFT
KDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK
>gnl|CDD|143460 cd07142, ALDH_F2BC, Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like. Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde
VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRI
LLRFADLLEKHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHE
PIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPT
AGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFN
QGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATL
ITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNID
TANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM
>gnl|CDD|143461 cd07143, ALDH_AldA_AN0554, Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like. NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD
GKYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVSGSKR
GRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYT
RHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGY
GRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGI
FFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEG
ATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTN
NINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL
>gnl|CDD|143462 cd07144, ALDH_ALD2-YMR170C, Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like. NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD
GKSYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGEER
GELLDKLADLVEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYT
LHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGY
GAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIM
YNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEG
AKLVYGGEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAV
FTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL
>gnl|CDD|143463 cd07145, ALDH_LactADH_F420-Bios, Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like. NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD
IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIE
VGKPIKQSRVEVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERRIAFTVREPIGVVGAITPFNFPANLF
AHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTG
STAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYD
KFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGGKRDEGSFFPPTVLEN
DTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTR
FRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI
>gnl|CDD|143464 cd07146, ALDH_PhpJ, Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like. Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD
LEVRNPYTGEVVGTVPAGTEEALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGL
CLKDTRYEVGRAADVLRFAAAEALRDDGESFSCDLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHK
IAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVA
VGKAIAATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDL
LVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQRQGALYAPTVLDHVPPDAE
LVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSELS
PFGGVKDSGLGGKEGVREAMKEMTNVKTYSL
>gnl|CDD|143465 cd07147, ALDH_F21_RNP123, Aldehyde dehydrogenase family 21A1-like. Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD
LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLE
AGKPIKDARGEVARAIDTFRIAAEEATRIYGEVLPLDISARGEGRQGLVRRFPIGPVSAITPFNFPLNLV
AHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGS
PAVGWDLKARAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFK
SRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGKRDGALLEPTILEDVPPD
MEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDVPTFRVD
HMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI
>gnl|CDD|143466 cd07148, ALDH_RL0313, Uncharacterized ALDH (RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1. Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD
LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWLPAHERIAILERLADLMEERADELALLIAR
EGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNL
IVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIG
SARVGWMLRSKLAPGTRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADD
FAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTYAPTVLLDP
PRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAF
RVDWMPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI
>gnl|CDD|143467 cd07149, ALDH_y4uC, Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1. Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD
IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALE
AGKPIKDARKEVDRAIETLRLSAEEAKRLAGETIPFDASPGGEGRIGFTIREPIGVVAAITPFNFPLNLV
AHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTG
SPAVGEAIARKAGLKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEF
LERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLTGGKRDGAILEPTVLTDVPP
DMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTFRV
DHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF
>gnl|CDD|143468 cd07150, ALDH_VaniDH_like, Pseudomonas putida vanillin dehydrogenase-like. Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde
FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDE
GGSTYGKAWFETTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKV
AFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAV
GREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVK
KFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKGAKLLTGGKYDGNFYQPTVLTDVTPDM
RIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTILDEAH
VPFGGVKASGFGREGGEWSMEEFTELKWITV
>gnl|CDD|143469 cd07151, ALDH_HBenzADH, NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like. NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD
GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEER
RDEIVEWLIRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPW
NFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPV
PRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRI
IVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAEGNVL
EPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMT
HINDQPVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQH
>gnl|CDD|143470 cd07152, ALDH_BenzADH, NAD-dependent benzaldehyde dehydrogenase II-like. NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids
GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKA
GFEVGAAIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNA
VVLKPDPRTPVSGGVVIARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAG
RHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHL
PVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTYDGLFYRPTVLSGVKPGMPAFDEEIFG
PVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDEPHNPFGGMGAS
GNGSRFGGPANWEEFTQWQWVTV
>gnl|CDD|133478 cd07153, Fur_like, Ferric uptake regulator(Fur) and related metalloregulatory proteins; typically iron-dependent, DNA-binding repressors and activators. Ferric uptake regulator (Fur) and related metalloregulatory proteins are iron-dependent, DNA-binding repressors and activators mainly involved in iron metabolism. A general model for Fur repression under iron-rich conditions is that activated Fur (a dimer having one Fe2+ coordinated per monomer) binds to specific DNA sequences (Fur boxes) in the promoter region of iron-responsive genes, hindering access of RNA polymerase, and repressing transcription. Positive regulation by Fur can be direct or indirect, as in the Fur repression of an anti-sense regulatory small RNA. Some members sense metal ions other than Fe2+. For example, the zinc uptake regulator (Zur) responds to Zn2+, the manganese uptake regulator (Mur) responds to Mn2+, and the nickel uptake regulator (Nur) responds to Ni2+. Other members sense signals other than metal ions. For example, PerR, a metal-dependent sensor of hydrogen peroxide. PerR regulates DNA-binding activity through metal-based protein oxidation, and co-ordinates Mn2+ or Fe2+ at its regulatory site. Fur family proteins contain an N-terminal winged-helix DNA-binding domain followed by a dimerization domain; this CD spans both those domains
PQRLAILEVLLESDGHLTAEEIYERLRKKGPSISLATVYRTLELLEEAGLVREIELGDGKARYELNTDEH
HHHLICTKCGKVIDFEDCPLEELLEELAAKTGFKITSHRLELYGIC
>gnl|CDD|143529 cd07154, NR_DBD_PNR_like, The DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) nuclear receptor-like family. The DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) nuclear receptor-like family is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. PNR interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. This family includes nuclear receptor Tailless (TLX), photoreceptor cell-specific nuclear receptor (PNR) and related receptors. TLX is an orphan receptor that plays a key role in neural development by regulating cell cycle progression and exit of neural stem cells in the developing brain. PNR is expressed only in the outer layer of retinal photoreceptor cells. It may be involved in the signaling pathway regulating photoreceptor differentiation and/or maintenance. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, PNR-like receptors have a central well-conserved DNA-binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
CKVCGDRSSGKHYGVYACDGCSGFFKRSIRRNLLYTCKAGNGSCVVDKARRNQCQACRLKKCLEVSMNKD
AVQ
>gnl|CDD|143530 cd07155, NR_DBD_ER_like, DNA-binding domain of estrogen receptor (ER) and estrogen related receptors (ERR) is composed of two C4-type zinc fingers. DNA-binding domains of estrogen receptor (ER) and estrogen related receptors (ERR) are composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. ER and ERR interact with the palindromic inverted repeat, 5'GGTCAnnnTGACC-3', upstream of the target gene and modulate the rate of transcriptional initiation. ERR and ER are closely related and share sequence similarity, target genes, co-regulators and promoters. While ER is activated by endogenous estrogen, ERR lacks the ability to bind to estrogen. Estrogen receptor mediates the biological effects of hormone estrogen by the binding of the receptor dimer to estrogen response element of target genes. However, ERRs seem to interfere with the classic ER-mediated estrogen responsive signaling by targeting the same set of genes. ERRs and ERs exhibit the common modular structure with other nuclear receptors. They have a central highly conserved DNA binding domain (DBD), a non-conserved N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
CLVCGDIASGYHYGVASCEACKAFFKRTIQGNLGYSCPSTSECEVDKKRRKSCQACRLQKCLKVGMLKEG
VRLDR
>gnl|CDD|143531 cd07156, NR_DBD_VDR_like, The DNA-binding domain of vitamin D receptors (VDR) like nuclear receptor family is composed of two C4-type zinc fingers. The DNA-binding domain of vitamin D receptors (VDR) like nuclear receptor family is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. This domain interacts with specific DNA site upstream of the target gene and modulates the rate of transcriptional initiation. This family includes three types of nuclear receptors: vitamin D receptors (VDR), constitutive androstane receptor (CAR) and pregnane X receptor (PXR). VDR regulates calcium metabolism, cellular proliferation and differentiation. PXR and CAR function as sensors of toxic byproducts of cell metabolism and of exogenous chemicals, to facilitate their elimination. The DNA binding activity is regulated by their corresponding ligands. VDR is activated by Vitamin D; CAR and PXR respond to a diverse array of chemically distinct ligands, including many endogenous compounds and clinical drugs. Like other nuclear receptors, xenobiotic receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
CGVCGDRATGYHFNAMTCEGCKGFFRRSMKRKARFTCPFNGDCEITKDNRRHCQACRLKKCLDIGMKKEM
IL
>gnl|CDD|143532 cd07157, 2DBD_NR_DBD1, The first DNA-binding domain (DBD) of the 2DBD nuclear receptors is composed of two C4-type zinc fingers. The first DNA-binding domain (DBD) of the 2DBD nuclear receptors(NRs) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. NRs interact with specific DNA sites upstream of the target gene and modulate the rate of transcriptional initiation. Theses proteins contain two DBDs in tandem, probably resulted from an ancient recombination event. The 2DBD-NRs are found only in flatworm species, mollusks and arthropods. Their biological function is unknown
QTCQVCGEPAAGFHHGAYVCEACKKFFMRSSNAISFTISECPNGGKCIIDKKNRTKCQACRYRKCLNVGM
SLGGPRYGRRSDISKI
>gnl|CDD|143533 cd07158, NR_DBD_Ppar_like, The DNA-binding domain of peroxisome proliferator-activated receptors (PPAR) like nuclear receptor family. The DNA-binding domain of peroxisome proliferator-activated receptors (PPAR) like nuclear receptor family is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. These domains interact with specific DNA sites upstream of the target gene and modulate the rate of transcriptional initiation. This family includes three known types of nuclear receptors: peroxisome proliferator-activated receptors (PPAR), REV-ERB receptors and Drosophila ecdysone-induced protein 78 (E78). Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, PPAR-like receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
CKVCGDKASGFHYGVHSCEGCKGFFRRTIQHNLTYRRCLNGGKCVIQRKNRNRCQYCRFKKCLSVGMSRN
AVR
>gnl|CDD|143534 cd07160, NR_DBD_LXR, DNA-binding domain of Liver X receptors (LXRs) family is composed of two C4-type zinc fingers. DNA-binding domain of Liver X receptors (LXRs) family is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. LXR interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. LXR operates as cholesterol sensor which protects cells from cholesterol overload by stimulating reverse cholesterol transport from peripheral tissues to the liver and its excretion in the bile. Oxidized cholesterol derivatives or oxysterols were identified as specific ligands for LXRs. LXR functions as a heterodimer with the retinoid X receptor (RXR) which may be activated by either LXR agonist or 9-cis retinoic acid, a specific RXR ligand. The LXR/RXR complex binds to a liver X receptor response element (LXRE) in the promoter region of target genes. The ideal LXRE sequence is a direct repeat-4 (DR-4) DNA fragment consisting of two AGGTCA hexameric half-sites separated by a 4-nucleotide spacer. LXR has typical NR modular structure with a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and the ligand binding domain (LBD) at the C-terminal
EEPPRKRKKGPAPKMLGNEVCSVCGDKASGFHYNVLSCEGCKGFFRRSVIKGAQYVCKNGGKCQMDMYMR
RKCQECRLRKCREAGMREQCVLSEEQIRLKK
>gnl|CDD|143535 cd07161, NR_DBD_EcR, DNA-binding domain of Ecdysone receptor (ECR) family is composed of two C4-type zinc fingers. DNA-binding domain of Ecdysone receptor (EcR) family is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. EcR interacts with highly degenerate pseudo-palindromic response elements, resembling inverted repeats of 5'-AGGTCA-3' separated by 1 bp, upstream of the target gene and modulates the rate of transcriptional initiation. EcR is present only in invertebrates and regulates the expression of a large number of genes during development and reproduction. EcR functions as a heterodimer by partnering with ultraspiracle protein (USP), the ortholog of the vertebrate retinoid X receptor (RXR). The natural ligands of EcR are ecdysteroids, the endogenous steroidal hormones found in invertebrates. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, EcRs have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
EELCLVCGDRASGYHYNALTCEGCKGFFRRSVTKSAVYHCKYGRACEMDMYMRRKCQECRLKKCLSVGMR
PECVVPESQCAIKRREKKQQK
>gnl|CDD|143536 cd07162, NR_DBD_PXR, DNA-binding domain of pregnane X receptor (PXRs) is composed of two C4-type zinc fingers. DNA-binding domain (DBD)of pregnane X receptor (PXR) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. PXR DBD interacts with the PXR response element, a perfect repeat of two AGTTCA motifs with a 4 bp spacer upstream of the target gene, and modulates the rate of transcriptional initiation. The pregnane X receptor (PXR) is a ligand-regulated transcription factor that responds to a diverse array of chemically distinct ligands, including many endogenous compounds and clinical drugs. PXR functions as a heterodimer with retinoic X receptor-alpha (RXRa) and binds to a variety of promoter regions of a diverse set of target genes involved in the metabolism, transport, and ultimately, elimination of these molecules from the body. Like other nuclear receptors, PXR has a central well conserved DNA-binding domain, a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain
ICRVCGDRATGYHFNAMTCEGCKGFFRRAMKRNARLCCPFQKGCVITKSNRRQCQACRLRKCLSIGMKKE
LIMSDEAVEKRRALIKR
>gnl|CDD|143537 cd07163, NR_DBD_TLX, DNA-binding domain of Tailless (TLX) is composed of two C4-type zinc fingers. DNA-binding domain of Tailless (TLX) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. TLX interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. TLX is an orphan receptor that is expressed by neural stem/progenitor cells in the adult brain of the subventricular zone (SVZ) and the dentate gyrus (DG). It plays a key role in neural development by promoting cell cycle progression and preventing apoptosis in the developing brain. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, TLX has a central well conserved DNA-binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
SSRILDIPCKVCGDRSSGKHYGIYACDGCSGFFKRSIRRNRQYVCKSKGQGGCPVDKTHRNQCRACRLKK
CFEVGMNKDAVQHERGPRNSTL
>gnl|CDD|143538 cd07164, NR_DBD_PNR_like_1, DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) like proteins is composed of two C4-type zinc fingers. DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) like proteins is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. PNR interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. PNR is a member of nuclear receptor superfamily of the ligand-activated transcription factors. PNR is expressed only in the outer layer of retinal photoreceptor cells. It may be involved in the signaling pathway regulating photoreceptor differentiation and/or maintenance. It most likely binds to DNA as a homodimer. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, PNR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
CRVCGDRASGKHYGVPSCDGCRGFFKRSIRRNLAYVCKENGSCVVDVARRNQCQACRFKKCLQVNMNRDA
VQHERAPR
>gnl|CDD|143539 cd07165, NR_DBD_DmE78_like, DNA-binding domain of Drosophila ecdysone-induced protein 78 (E78) like is composed of two C4-type zinc fingers. DNA-binding domain of proteins similar to Drosophila ecdysone-induced protein 78 (E78) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. E78 interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. Drosophila ecdysone-induced protein 78 (E78) is a transcription factor belonging to the nuclear receptor superfamily. E78 is a product of the ecdysone-inducible gene found in an early late puff locus at position 78C during the onset of Drosophila metamorphosis. An E78 orthologue from the Platyhelminth Schistosoma mansoni (SmE78) has also been identified. It is the first E78 orthologue known outside of the molting animals--the Ecdysozoa. The SmE78 may be involved in transduction of an ecdysone signal in S. mansoni, consistent with its function in Drosophila. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, E78-like receptors have a central well conserved DNA-binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
CKVCGDKASGYHYGVTSCEGCKGFFRRSIQKQIEYRCLRDGKCEIIRLNRNRCQYCRFKKCLAAGMSKDS
VRYGRIPNRQR
>gnl|CDD|143540 cd07166, NR_DBD_REV_ERB, DNA-binding domain of REV-ERB receptor-like is composed of two C4-type zinc fingers. DNA-binding domain of REV-ERB receptor- like is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. This domain interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. REV-ERB receptors are transcriptional regulators belonging to the nuclear receptor superfamily. They regulate a number of physiological functions including the circadian rhythm, lipid metabolism, and cellular differentiation. REV-ERB receptors bind as a monomer to a (A/G)GGTCA half-site with a 5' AT-rich extension or as a homodimer to a direct repeat 2 element (AGGTCA sequence with a 2-bp spacer), indicating functional diversity. When bound to the DNA, they recruit corepressors (NcoR/histone deacetylase 3) to the promoter, resulting in repression of the target genes. The porphyrin heme has been demonstrated to function as a ligand for REV-ERB receptor. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, REV-ERB receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
GMVVLCKVCGDKASGFHYGVHACEGCKGFFRRSIQQKIQYRKCTKNETCSIMRINRNRCQYCRFKKCLAV
GMSRDAVRFGRIPKREKAR
>gnl|CDD|143541 cd07167, NR_DBD_Lrh-1_like, The DNA-binding domain of Lrh-1 like nuclear receptor family like is composed of two C4-type zinc fingers. The DNA-binding domain of Lrh-1 like nuclear receptor family like is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. This domain interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. This nuclear receptor family includes at least three subgroups of receptors that function in embryo development and differentiation, and other processes. FTZ-F1 interacts with the cis-acting DNA motif of ftz gene, which is required at several stages of development. Particularly, FTZ-F1 regulated genes are strongly linked to steroid biosynthesis and sex-determination; LRH-1 is a regulator of bile-acid homeostasis, steroidogenesis, reverse cholesterol transport and the initial stages of embryonic development; SF-1 is an essential regulator of endocrine development and function and is considered a master regulator of reproduction; SF-1 functions cooperatively with other transcription factors to modulate gene expression. Phospholipids have been identified as potential ligand for LRH-1 and steroidogenic factor-1 (SF-1). However, the ligand for FTZ-F1 has not yet been identified. Most nuclear receptors function as homodimer or heterodimers. However, LRH-1 and SF-1 bind to DNA as monomers. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, receptors in this family have a central well conserved DNA-binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
CPVCGDKVSGYHYGLLTCESCKGFFKRTVQNKKRYTCIENQNCQIDKTQRKRCPYCRFQKCLSVGMKLEA
VRADRMRGGRNKFGPMYKRDRAL
>gnl|CDD|143542 cd07168, NR_DBD_DHR4_like, DNA-binding domain of ecdysone-induced DHR4 orphan nuclear receptor is composed of two C4-type zinc fingers. DNA-binding domain of ecdysone-induced DHR4 orphan nuclear receptor is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. This domain interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. Ecdysone-induced orphan receptor DHR4 is a member of the nuclear receptor family. DHR4 is expressed during the early Drosophila larval development and is induced by ecdysone. DHR4 coordinates growth and maturation in Drosophila by mediating endocrine response to the attainment of proper body size during larval development. Mutations in DHR4 result in shorter larval development which translates into smaller and lighter flies. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, DHR4 has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
DEDESPKLCSICEDKATGLHYGIITCEGCKGFFKRTVQNKRVYTCVGDGRCEITKAQRNRCQYCRFRKCI
RKGMMLAAVREDRMPGGRNS
>gnl|CDD|143543 cd07169, NR_DBD_GCNF_like, DNA-binding domain of Germ cell nuclear factor (GCNF) F1 is composed of two C4-type zinc fingers. DNA-binding domain of Germ cell nuclear factor (GCNF) F1 is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. This domain interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. GCNF is a transcription factor expressed in post-meiotic stages of developing male germ cells. In vitro, GCNF has the ability to bind to direct repeat elements of 5'-AGGTCA.AGGTCA-3', as well as to an extended half-site sequence 5'-TCA.AGGTCA-3'. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, GCNF has a central well conserved DNA-binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
DDRAEQRTCLICGDRATGLHYGIISCEGCKGFFKRSICNKRVYRCSRDKNCVMSRKQRNRCQYCRLLKCL
QMGMNRKAIREDGMPGGRNK
>gnl|CDD|143544 cd07170, NR_DBD_ERR, DNA-binding domain of estrogen related receptors (ERR) is composed of two C4-type zinc fingers. DNA-binding domain of estrogen related receptors (ERRs) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. ERR interacts with the palindromic inverted repeat, 5'GGTCAnnnTGACC-3', upstream of the target gene and modulates the rate of transcriptional initiation. The estrogen receptor-related receptors (ERRs) are transcriptional regulators, which are closely related to the estrogen receptor (ER) family. Although ERRs lack the ability to bind to estrogen and are so-called orphan receptors, they share target genes, co-regulators and promoters with the estrogen receptor (ER) family. By targeting the same set of genes, ERRs seem to interfere with the classic ER-mediated estrogen response in various ways. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, ERR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
TIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKV
GMLKEGVRLDRVRGGRQKYKRRIDAEN
>gnl|CDD|143545 cd07171, NR_DBD_ER, DNA-binding domain of estrogen receptors (ER) is composed of two C4-type zinc fingers. DNA-binding domain of estrogen receptors (ER) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. ER interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. Estrogen receptor is a transcription regulator that mediates the biological effects of hormone estrogen. The binding of estrogen to the receptor triggers the dimerization and the binding of the receptor dimer to estrogen response element, which is a palindromic inverted repeat: 5'GGTCAnnnTGACC-3', of target genes. Through ER, estrogen regulates development, reproduction and homeostasis. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, ER has a central well-conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
KDTHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVG
MMKGGIRRERRG
>gnl|CDD|143546 cd07172, NR_DBD_GR_PR, DNA-binding domain of glucocorticoid receptor (GR) is composed of two C4-type zinc fingers. DNA-binding domains of glucocorticoid receptor (GR) and progesterone receptor (PR) are composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinate a single zinc atom. The DBD from both receptors interact with the same hormone response element (HRE), which is an imperfect palindrome GGTACAnnnTGTTCT, upstream of target genes and modulates the rate of transcriptional initiation. GR is a transcriptional regulator that mediates the biological effects of glucocorticoids and PR regulates genes controlled by progesterone. GR is expressed in almost every cell in the body and regulates genes controlling a wide variety of processes including the development, metabolism, and immune response of the organism. PR functions in a variety of biological processes including development of the mammary gland, regulating cell cycle progression, protein processing, and metabolism. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, GR and PR have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD)
PQKICLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRLRKCLQAGM
NLGARKTK
>gnl|CDD|143547 cd07173, NR_DBD_AR, DNA-binding domain of androgen receptor (AR) is composed of two C4-type zinc fingers. DNA-binding domain of androgen receptor (AR) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. To regulate gene expression, AR interacts with a palindrome of the core sequence 5'-TGTTCT-3' with a 3-bp spacer. It also binds to the direct repeat 5'-TGTTCT-3' hexamer in some androgen controlled genes. AR is activated by the androgenic hormones, testosterone or dihydrotestosterone, which are responsible for primary and for secondary male characteristics, respectively. The primary mechanism of action of ARs is by direct regulation of gene transcription. The binding of androgen results in a conformational change in the androgen receptor which causes its transport from the cytosol into the cell nucleus, and dimerization. The receptor dimer binds to a hormone response element of AR regulated genes and modulates their expression. Another mode of action of androgen receptor is independent of their interactions with DNA. The receptor interacts directly with signal transduction proteins in the cytoplasm, causing rapid changes in cell function, such as ion transport. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, AR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
PPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCFEAG
MTLGARKLKKLG
>gnl|CDD|143580 cd07176, terB, tellurite resistance protein terB. This family contains uncharacterized bacterial proteins involved in tellurium resistance. The prototype of this CD is the Kp-terB protein from Klebsiella pneumoniae, whose 3D structure was recently determined. The biological function of terB and the mechanism responsible for tellurium resistance are unknown
FAEALVALAALVAAADGDIDDAELQAIEALLRSLPVLSGFDRERLIALLDKLLALLRPEGLAALLKAAAK
LLPPELRETAFAVAVDIAAADGEVDPEERAVLEKLYRALGL
>gnl|CDD|143581 cd07177, terB_like, tellurium resistance terB-like protein. This family consists of tellurium resistance terB proteins, N-terminal domain of heat shock DnaJ-like proteins, N-terminal domain of Mo-dependent nitrogenase-like proteins, C-terminal domain of ABC transporter ATP-binding proteins, C-terminal domain of serine/threonine protein kinase, and many hypothetical bacterial proteins. The function of this family is unknown
ALAALLLAAAKADGRVDEEEIAAIEALLRRLPLLDAEERAELIALLEEPLAEAGDLAALAALLKELPDAE
LREALLAALWEVALADGELDPEERALLRRLADAL
>gnl|CDD|143582 cd07178, terB_like_YebE, tellurium resistance terB-like protein, subgroup 3. This family includes several uncharacterized bacterial proteins including an Escherichia coli protein called YebE. Protein sequence homology analysis shows they are similar to tellurium resistance protein terB, but the function of this family is unknown
LLLRAMIAAAKADGHIDEAERARILGELGEAGLDAEERAFLEAELAAPLDPDALAAAVPDPELAAEVYAA
SLLAIDPDTFAERAYLDELAAALGL
>gnl|CDD|143548 cd07179, 2DBD_NR_DBD2, The second DNA-binding domain (DBD) of the 2DBD nuclear receptor is composed of two C4-type zinc fingers. The second DNA-binding domain (DBD) of the 2DBD nuclear receptor (NR) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. NRs interact with specific DNA sites upstream of the target gene and modulate the rate of transcriptional initiation. The proteins contain two DBDs in tandem, probably resulting from an ancient recombination event. The 2DBD-NRs are found only in flatworm species, mollusks and arthropods. Their biological function is unknown
CRVCGGKSSGFHFGALTCEGCKGFFRRTELSSNSYVCPGGQNCAITPATRNACKSCRFRRCLAVGMSKTG
SRIG
>gnl|CDD|260001 cd07180, RNase_HII_archaea_like, Archaeal Ribonuclease HII. This family includes type 2 RNases H from archaea, some of which show broad divalent cation specificity. It is proposed that three of the four acidic residues at the active site are involved in metal binding and the fourth one is involved in the catalytic process in archaea. Most archaeal genomes contain multiple RNase H genes. Despite a lack of evidence for homology from sequence comparisons, type I and type II RNase H share a common fold and similar steric configurations of the four acidic active-site residues, suggesting identical or very similar catalytic mechanisms. It appears that type I and type II RNases H also have overlapping functions in cells, as over-expression of Escherichia coli RNase HII can complement an RNase HI deletion phenotype in E. coli. RNase H is classified into two families, type I (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type II (prokaryotic RNase HII and HIII, archaeal RNase HII and eukaryotic RNase H2/HII). RNase H endonucleolytically hydrolyzes an RNA strand when it is annealed to a complementary DNA strand in the presence of divalent cations, in DNA replication or repair
IGIDEAGRGPVIGPMVVAGVAIDEEDLKRLKSLGVKDSKKLSPKRREELYEEILKSAIDVVVVVVSPEEI
DRRRESMNLNELEAEAFAEIINRLALQPDTVYVDACDVNEERFGRRLRERLNTGVEVVAEHKADAKYPVV
SAASIVAKVERDREIEELKKEYGDFGSGYPSDPKTIEFLREYYREHGEPPPIVRKSWKTVKRLL
>gnl|CDD|260002 cd07181, RNase_HII_eukaryota_like, Eukaryotic RNase HII. This family includes eukaryotic type 2 RNase H (RNase HII or H2) which is active during replication and is believed to play a role in the removal of Okazaki fragment primers and single ribonucleotides in DNA-DNA duplexes. Eukaryotic RNase HII (RNASEH2A) is functional when it forms a heterotrimeric complex with two other accessory proteins (RNASEH2B and RNASEH2C). It is speculated that these accessory subunits are required for correct folding of the catalytic subunit of RNase HII. Mutations in the three subunits of human RNase HII cause the severe genetic neurological disorder Aicardi-Goutieres syndrome. Ribonuclease H (RNase H) is classified into two families, type I (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type II (prokaryotic RNase HII and HIII, and eukaryotic RNase H2/HII). RNase H endonucleolytically hydrolyzes an RNA strand when it is annealed to a complementary DNA strand in the presence of divalent cations, in DNA replication and repair. The enzyme can be found in bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite a lack of evidence for homology from sequence comparisons, type I and type II RNase H share a common fold and similar steric configurations of the four acidic active-site residues, suggesting identical or very similar catalytic mechanisms
LGIDEAGRGPVLGPMVYGCAYCPLSYEEELKKLGFADSKTLTEEQREELFKKIKEDPDNVGWAVRVLSPE
EISAKMLRRSKYNLNEISHDAAIGLIRSVLDKGVNVTEVYVDTVGPPEKYQAKLQKLFPGIKITVSKKAD
SLYPIVSAASIVAKVTRDRALENWQFEEPGIDIDREFGSGYPSDPKTKAWLKKNVDPVFGFPSLVRFSWS
TAKTILEKKAV
>gnl|CDD|260003 cd07182, RNase_HII_bacteria_HII_like, Bacterial Ribonuclease HII-like. This family includes mostly bacterial type 2 RNases H, with some eukaryotic members. Bacterial RNase HII has a role in primer removal based on its involvement in ribonucleotide-specific catalytic activity in the presence of RNA/DNA hybrid substrates. Several bacteria, such as Bacillus subtilis, have two different type II RNases H, RNases HII and HIII; double deletion of these leads to cellular lethality. It appears that type I and type II RNases H also have overlapping functions in cells, as over-expression of Escherichia coli RNase HII can complement an RNase HI deletion phenotype. In Leishmania mitochondria, of the four distinct RNase H genes (H1, HIIA, HIIB, HIIC), HIIC is essential for the survival of the parasite and thus can be a potential target for anti-leishmanial chemotherapy. Ribonuclease H (RNase H) is classified into two families, type I (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type II (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H endonucleolytically hydrolyzes an RNA strand when it is annealed to a complementary DNA strand in the presence of divalent cations, in DNA replication and repair
AGVDEAGRGPLAGPVVAAAVILPPDFPIEGLNDSKKLSEKKREELYEEIKENALAYGIGIASVEEIDELN
ILQATLLAMKRAVEGLKVKPDYVLVDGNRLPPLPIPQEAIVKGDAKSASIAAASILAKVTRDRLMEELDK
EYPEYGFAKHKGYGTKEHLEALKKYGPSPIHRKSFAP
>gnl|CDD|199892 cd07184, E_set_Isoamylase_like_N, N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also called glycogen 6-glucanohydrolase) proteins. E or "early" set domains are associated with the catalytic domain of isoamylase-like proteins at the N-terminal end. Isoamylase is one of the starch-debranching enzymes that catalyze the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen. Isoamylase contains a bound calcium ion, but this is not in the same position as the conserved calcium ion that has been reported in other alpha-amylase family enzymes. The N-terminal domain of isoamylase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and the beta subunit of AMP-activated protein kinase
CKVTFELPAEQGADSVSLVGDFNDWDPQATPMKKLKNGTFSATLDLPAGREYQFRYLIDGERWVNDPEAD
AYAPNGFGEENSVVSV
>gnl|CDD|143586 cd07185, OmpA_C-like, Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane
LITIYFDFGSAELTPEAKPLLDKLAEVLKKNPDAKIRIEGHTDSRGSDAYNQELSERRAEAVADYLVSKG
VDASRITAVGYGESRPIASNDTEEGRAKNRRVEIVI
>gnl|CDD|132872 cd07186, CofD_like, LPPG:FO 2-phospho-L-lactate transferase; important in F420 biosynthesis. CofD is a 2-phospho-L-lactate transferase that catalyzes the last step in the biosynthesis of coenzyme F(420)-0 (F(420) without polyglutamate) by transferring the lactyl phosphate moiety of lactyl(2)diphospho-(5')guanosine (LPPG) to 7,8-didemethyl-8-hydroxy-5-deazariboflavin ribitol (F0). F420 is a hydride carrier, important for energy metabolism of methanogenic archaea, as well as for the biosynthesis of other natural products, like tetracycline in Streptomyces. F420 and some of its precursors are also utilized as cofactors for enzymes, like DNA photolyase in Mycobacterium tuberculosis
IVVLSGGTGGAKLLRGLKRVLDPEELTVVVNTGDDFWLSGLYVSPDLDTVLYTLAGLIDRETGWGIEGDT
FNTLEALERLGGEEWFRLGDRDRATHILRTEMLREGKSLSEVTAELAERLGIKARILPMSDDRVETRVVT
DEGDLHFQEYWVRRRGEPEVRDVRFVGAEEARPAPEVLEAIEDADLVIIGPSNPVTSIGPILALPGIREA
LRDKKAPVVAVSPIIGGKAVSGPAAKLMAALGFEPSAAGVAEIYGDLLDGFVIDEADRALADAIEALGIE
VSRTDTLMTDEEDKIRLAREVLE
>gnl|CDD|132873 cd07187, YvcK_like, family of mostly uncharacterized proteins similar to B.subtilis YvcK. One member of this protein family, YvcK from Bacillus subtilis, has been proposed to play a role in carbon metabolism, since its function is essential for growth on intermediates of the Krebs cycle and the pentose phosphate pathway. In general, this family of mostly uncharacterized proteins is related to the CofD-like protein family. CofD has been characterized as a 2-phospho-L-lactate transferase involved in F420 biosynthesis. This family appears to have the same conserved phosphate binding site as the other family in this hierarchy, but a different substrate binding site
IVAFGGGTGLSTLLRGLKKYTHNLTAIVTVTDDGGSSGRLRRELGIPAPGDIRNRLVALADDESLAQKLF
FLYRRFGDFDLRGHSLGNLILAALTLITGSFAEAILLLSRLLGVRGRVLPVTNDPLHLVAELEDGTIVRG
ESRISHLELGSPIKRVFLEPPDPKANPEALEAIEEADLIVYGPGSLYTSILPNLLVKGIAEAIRASKAPK
VYICNLMTQPGETDGFTLSDHVRALLRHLGEGLLDVVLVNSERPPEEVLRRYEEGSLPVELDEELLEKLG
IRVIEADLLSEESGIRHDPEKLAAALLE
>gnl|CDD|143587 cd07197, nitrilase, Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes. This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy
IAAVQLAPKIGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFESAKEDLDLAEELDGPTLEALAE
LAKELGIYIVAGIAEKDGDKLYNTAVVIDPDGEIIGKYRKIHLFDFGERRYFSPGDEFPVFDTPGGKIGL
LICYDLRFPELARELALKGADIILVPAAWPTARREHWELLLRARAIENGVYVVAANRVGEEGGLEFAGGS
MIVDPDGEVLAEASEEEGILVAELDLDELREARKRWSYLRDRR
>gnl|CDD|132837 cd07198, Patatin, Patatin-like phospholipase. Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes PNPLA (1-9), TGL (3-5), ExoU-like, and SDP1-like subfamilies. There are some additional hypothetical proteins included in this family
LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGA
FPPTGRLLGILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVSDTSKGELWSAVRASSSIPGYFGP
VPLSFRGRRYGDGGLSNNLPVAELGNTINVSP
>gnl|CDD|132838 cd07199, Pat17_PNPLA8_PNPLA9_like, Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17. Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum
ILSLDGGGIRGIIPAEILAELEKRLGKPSRIADLFDLIAGTSTGGIIALGLALGRYSAEELVELYEELGR
KIFPRVLVTAYDLSTGKPVVFSNYDAEEPDDDDDFKLWDVARATSAAPTYFPPAVIESGGDEGAFVDGGV
AANNPALLALAEALRLLAPDKDDILVLSLGTGTSPSSSSSKKASRWGGLGWGRPLLDILMDAQSDGVDQW
LDLLFGSLDSKDNYLRINPPLPGPIPALDDASEANLLALDSAAFELIE
>gnl|CDD|132839 cd07200, cPLA2_Grp-IVA, Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent. Group IVA cPLA2, an 85 kDa protein, consists of two domains: the regulatory C2 domain and the alpha/beta hydrolase PLA2 domain. Group IVA cPLA2 is also referred to as cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (cPLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. A calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. Includes PLA2G4A from chicken, human, and frog
LRFSMALCDEEKEFRQARKMRVREALRKLLGEEGPKVTSLREVPVIALLGSGGGFRAMVGMSGAMKALYD
SGVLDCATYVAGLSGSTWYMSTLYSHPDFPEKGPGEINKELMRNVSSSPLLLLTPQLLKRYTEALWEKKS
SGQPVTFTDFFGMLIGETLIKERMDTKLSDLQEKVNDGQVPLPLFTCLHVKPDVSALMFHDWVEFSPYEI
GMAKYGTFMSPDLFGSKFFMGFLAKKYPENPLHFLMGVWGSAFSILFNRVLGRNSREGRAGKVHNFMLGL
NLNTSYPLSPLSDLATDEPEAAVADADEFERIYEPLDTKSKKIHVVDSGLTFNLPYPLILRPQRGVDLII
SFDFSARPSDSSPPFKELLLAEKWARMNGLPFPPIDFKVFDREGLKECYVFKPKNDDDCPTVIHFVLCNI
NFRNLKAPGVPRETEEEKEFANFDIFDDPETPFSTFNFQYPNQAFDRLHELMEFNTLNNIDVIKDAIRES
IEKRRRNPSRCSVSL
>gnl|CDD|132840 cd07201, cPLA2_Grp-IVB-IVD-IVE-IVF, Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent. Group IVB, IVD, IVE, and IVF cPLA2 consists of two domains: the regulatory C2 domain and alpha/beta hydrolase PLA2 domain. Group IVB, IVD, IVE, and IVF cPLA2 are also referred to as cPLA2-beta, -delta, -epsilon, and -zeta respectively. cPLA2-beta is approximately 30% identical to cPLA2-alpha and it shows low enzymatic activity compared to cPLA2alpha. cPLA2-beta hydrolyzes palmitic acid from 1-[14C]palmitoyl-2-arachidonoyl-PC and arachidonic acid from 1-palmitoyl-2[14C]arachidonoyl-PC, but not from 1-O-alkyl-2[3H]arachidonoyl-PC. cPLA2-delta, -epsilon, and -zeta are approximately 45-50% identical to cPLA2-beta and 31-37% identical to cPLA2-alpha. It's possible that cPLA2-beta, -delta, -epsilon, and -zeta may have arisen by gene duplication from an ancestral gene. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. The calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. It includes PLA2G4B, PLA2G4D, PLA2G4E, and PLA2G4F from humans
LKAEESSEDLDVRLGFDLCAEEQEFLQKRKKVVAAALKKALQLEEDLQEDEVPVVAVMTTGGGTRALTSM
YGSLLGLQKLGLLDCVSYITGLSGSTWTMATLYEDPNWSQKDLEGPIEEARKHVTKSKLGCFSPERLKYY
RQELSEREQEGHKVSFIDLWGLIIESMLHDKKNDHKLSDQREAVSQGQNPLPIYLSLNVKDNLSTQDFRE
WVEFTPYEVGFLKYGAFIPAEDFGSEFFMGRLMKKLPESRICFLQGMWSSIFSLNLLDAWYLATGSEDFW
HRWTRDKVNDIEDEPPLPPRPPERLTTLLTPGGPLSQAFRDFLTSRPTVSQYFNFLRGLQLHNDYLENKG
FSTWKDTHLDAFPNQLTPSEDHLCLVDTAFFINTSYPPLLRPERKVDVILSLNYSLGSQFEPLKQASEYC
SEQGIPFPKIELSPEDQENLKECYVFEDADNPEAPIVLHFPLVNDTFRKYKAPGVERSPEEMAQGGVDVS
SSDSPYATRNLTYTEEDFDKLVKLTSYNVLNNKDLILQALRLAVERKKQRK
>gnl|CDD|132841 cd07202, cPLA2_Grp-IVC, Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent. Group IVC cPLA2, a small 61 kDa protein, is a single domain alpha/beta hydrolase. It lacks a C2 domain; therefore, it has no Ca-dependence. Group IVC cPLA2 is also referred to as cPLA2-gamma. The cPLA2-gamma enzyme is predominantly found in cardiac and skeletal muscles, and to a lesser extent in the brain. Human cPLA2-gamma is approximately 30% identical to cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Includes PLA2G4C protein from human and Pla2g4c protein from mouse
SEVRIAPGLNKEEKAAVVKRRKDVLQSLQKLGINADKAPVIAVLGSGGGLRAMIACLGVLSELDKAGLLD
CVTYLAGVSGSTWCMSSLYTEPDWSTKLQTVEDELKRRLQKVSWDFAYALKKEIQAAKSDNFSLTDFWAY
LVVTTFTKELDESTLSDQRKQSEEGKDPYPIFAAIDKDLSEWKERKTGDPWFEFTPHEAGYPLPGAFVST
THFGSKFENGKLVKQEPERDLLYLRALWGSALADGEEIAKYICMSLWIWGTTYNFLYKHGDIADKPAMRS
RETLHLMDAGLAINSPYPLVLPPVRNTDLILSFDFSEGDPFETIKDTAEYCRKHNIPFPQVDEAKLDQDA
EAPKDFYVFKGENGPVVMHFPLFNKVNCGDQLEDWRKEYRTFQGAYSTDQVRQLLELAKANVKNNKEKIM
SEIRALAGQI
>gnl|CDD|132842 cd07203, cPLA2_Fungal_PLB, Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain. Fungal phospholipase B are Group IV cPLA2 homologs. Aspergillus PLA2 is Ca-dependent, yet it does not contain a C2 domain. PLB deacylates both sn-1 and sn-2 chains of phospholipids and are abundantly expressed in fungi. It shows lysophospholipase (lysoPL) and transacylase activities. The active site residues from cPLA2 are also conserved in PLB. Like cPLA2, PLB also has a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). It includes PLB1 from Schizosaccharomyces pombe, PLB2 from Candida glabrata, and PLB3 from Saccharomyces cerevisiae. PLB1, PLB2, and PLB3 show PLB and lysoPL activities; PLB3 is specific for phosphoinositides
PFNVSCPSDANLIRSASDGLSTNEQEYLEKRRSITNSALKDFLSRANLNGDDDLDSNNSSNGPRIGIAVS
GGGYRAMLTGAGAIAAMDNRTDNATEHGLGGLLQSSTYLSGLSGGSWLVGSLASNNFTSVQDLLADSIWN
LDHSIFNPYGAAIVKTLNYYTNLANEVAQKKDAGFNVSLTDIWGRALSYQLFPALRGGPNLTWSSIRNQS
WFQNAEMPFPIIVADGRYPGETIINLNATVFEFTPYEFGSWDPSLNSFTPTEYLGTNVSNGVPPNGSCVN
GFDNAGFVMGTSSTLFNQFLLQINSTSSPSFIKLIATGFLLDILKENQDIASYIPNPFQGYTYSNSNGTN
PIVDSDYLDLVDGGEDGQNIPLWPLLQPERDVDVIFAFDSSADTDYNWPNGTSLVATYERQFSSQGNNGT
GFPYVPDQNTFVNLGLNDRPTFFGCDGRNLTDLNVDQYTPPLVVYIPNAPWSYNSNISTFKLSYTDSERQ
GMILNGFESATRNNLTNDDEFATCVACAIIRRSLERLNITTPDECQQCFDNYCWNGTIDTTP
>gnl|CDD|132843 cd07204, Pat_PNPLA_like, Patatin-like phospholipase domain containing protein family. Members of this family share a patain domain, initially discovered in potato tubers. PNPLA protein members show non-specific hydrolase activity with a variety of substrates such as triacylglycerol, phospholipids, and retinylesters. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly). Nomenclature of PNPLA family could be misleading as some of the mammalian members of this family show hydrolase, but no phospholipase activity
NLSFSGCGFLGIYHVGVASALREHAPRLLQNARRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARR
RSLGPLHPSFNLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFI
PFYCGLIPPKFRGVRYIDGGLSDNLPILDDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLEN
LYRLNRALFPPSLEILSRMCQQGYLDALRFLER
>gnl|CDD|132844 cd07205, Pat_PNPLA6_PNPLA7_NTE1_like, Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1. Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases
IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRSTDLKALSD
LTIPTAGLLRGDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPP
VKIDGQLLVDGGVLNNLPVDVLRELGADIIIAVDL
>gnl|CDD|132845 cd07206, Pat_TGL3-4-5_SDP1, Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase. Triacylglycerol lipases are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This family includes subfamilies of proteins: TGL3, TGL4, TGL5, and SDP1
LREGLHGNLGNMGNPSLYRHAYFGTKHLIEDYIEEVDLSLEYLALLDTKELSVEEKLDFFRRARHAFGRT
ALMLSGGASLGLFHLGVVKALWEQDLLPRVISGSSAGAIVAALLGTHTDEELIGDLTFQEAYERTGRIIN
ITVAPAEPHQNSRLLNALTSPNVLIWSAVLASCAVPGVFPPVMLMAKNRDGEIVPYLPGRKWVDGSVSDD
LPAKRLARLYNVNHFIVSQTNPHVVPFLQEYSGDITIIPPFSFSNPLKLLSNPSEDELQRLILEGERATW
PKIEMIRTQTRISRTLEE
>gnl|CDD|132846 cd07207, Pat_ExoU_VipD_like, ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2. ExoU, a 74-kDa enzyme, is a potent virulence factor of Pseudomonas aeruginosa. One of the pathogenic mechanisms of P. aeruginosa is to induce cytotoxicity by the injection of effector proteins (e.g. ExoU) using the type III secretion (T3S) system. ExoU is homologus to patatin and also has the conserved catalytic residues of mammalian calcium-independent (iPLA2) and cytosolic (cPLA2) PLA2. In vitro, ExoU cytotoxity is blocked by the inhibitor of cytosolic and Ca2-independent phospholipase A2 (cPLA2 and iPLA2) enzymes, suggesting that phospholipase A2 inhibitors may represent a novel mode of treatment for acute P. aeruginosa infections. ExoU requires eukaryotic superoxide dismutase as a cofactor and cleaves phosphatidylcholine and phosphatidylethanolamine in vitro. VipD, a 69-kDa cytosolic protein, belongs to the members of Legionella pneumophila family and is homologus to ExoU from Pseudomonas. Even though VipD shows high sequence similarity with several functional regions of ExoU (e.g. oxyanion hole, active site serine, active site aspartate), it has been shown to have no phospholipase activity. This family includes ExoU from Pseudomonas aeruginosa and VipD of Legionella pneumophila
NLVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDILKETDFAKLLDSPV
GLLFLLPSLFKEGGLYKGDALEEWLRELLKEKTGNSFATSLLRDLDDDLGKDLKVVATDLTTGALVVFSA
ETTPDMPVAKAVRASMSIPFVFKPVRLAKGDVYVDGGVLDNYPVWLFDGWELST
>gnl|CDD|132847 cd07208, Pat_hypo_Ecoli_yjju_like, Hypothetical patatin similar to yjju protein of Escherichia coli. Patatin-like phospholipase similar to yjju protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins, and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates
LVLEGGGMRGAYTAGVLDAFLEAGIRPFDLVIGVSAGALNAASYLSGQRGRALRINTKYATDPRYLGLRS
LLRTGNLFDLDFLYDELPDGLDPFDFEAFAASPARFYVVATDADTGEAVYFDKPDILDDLLDALRASSAL
PGLFPPVRIDGEPYVDGGLSDSIPVDKAIEDGADKIVVILTRPRGYRKKPSKSSPLAKLLYRKYPNLVEA
LLRRHSRYNETLEFIRRLEAEGKIFVIAPEKPLKVSRLERDPEKLEALYDLGYEDA
>gnl|CDD|132848 cd07209, Pat_hypo_Ecoli_Z1214_like, Hypothetical patatin similar to Z1214 protein of Escherichia coli. Patatin-like phospholipase similar to Z1214 protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates
LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAGGDPEAVERLEKLWRELSREDVFLRG
LLDRALDFDTLRLLAILFAGLVIVAVNVLTGEPVYFDDIPDGILPEHLLASAALPPFFPPVEIDGRYYWD
GGVVDNTPLSPAIDLGADEIIVVSLSDKGRDDRKGTPPTTLIEILPRLFLRSGLDSERIRHNLELGYLDT
LRADS
>gnl|CDD|132849 cd07210, Pat_hypo_W_succinogenes_WS1459_like, Hypothetical patatin similar to WS1459 of Wolinella succinogenes. Patatin-like phospholipase. This family predominantly consists of bacterial patatin glycoproteins. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates
FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPDEMAELLLSLERKDFWMFW
DPPLRGGLLSGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQP
VEIGGRPFVDGGVADRLPFDALRPEIERILYHHVAPRRPWERLNIIGKISRALIRPFRWNLAILSGVIED
VLEPLGPLLLK
>gnl|CDD|132850 cd07211, Pat_PNPLA8, Patatin-like phospholipase domain containing protein 8. PNPLA8 is a Ca-independent myocardial phospholipase which maintains mitochondrial integrity. PNPLA8 is also known as iPLA2-gamma. In humans, it is predominantly expressed in heart tissue. iPLA2-gamma can catalyze both phospholipase A1 and A2 reactions (PLA1 and PLA2 respectively). This family includes PNPLA8 (iPLA2-gamma) from Homo sapiens and iPLA2-2 from Mus musculus
PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEE
LYRKLGKDVFSQNTYISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACVSTQVNRTP
LKPYVFRNYNHPPGTRSHYLGSCKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEAK
LLWPDTPIQCLVSVGTGRYPSSVRLETGGYTSLKTKLLNLIDSATDTERVHTALDDLLPPDVYFRFNPVM
SECVELDETRPEKLDQLQDDTLEYIKRN
>gnl|CDD|132851 cd07212, Pat_PNPLA9, Patatin-like phospholipase domain containing protein 9. PNPLA9 is a Ca-independent phospholipase that catalyzes the hydrolysis of glycerophospholipids at the sn-2 position. PNPLA9 is also known as PLA2G6 (phospholipase A2 group VI) or iPLA2beta. PLA2G6 is stimulated by ATP and inhibited by bromoenol lactone (BEL). In humans, PNPLA9 in expressed ubiquitously and is involved in signal transduction, cell proliferation, and apoptotic cell death. Mutations in human PLA2G6 leads to infantile neuroaxonal dystrophy (INAD) and idiopathic neurodegeneration with brain iron accumulation (NBIA). This family includes PLA2G6 from Homo sapiens and Rattus norvegicus
LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVF
DGSRPYNSEPLEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKNANFLP
PTDPAEQLLWRAARSSGAAPTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVV
SLGTGIIPQTPVNTVDVFRPSNPWELAKTVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFS
PPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR
>gnl|CDD|132852 cd07213, Pat17_PNPLA8_PNPLA9_like1, Patatin-like phospholipase. Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum
KYRILSLDGGGVKGIVQLVLLKRLAEEFPSFLDQIDLFAGTSAGSLIALGLALGYSPRQVLKLYEEVGLK
VFSKSSAGGGAGNNQYFAAGFLKAFAEVFFGDLTLGDLKRKVLVPSFQLDSGKDDPNRRWKPKLFHNFPG
EPDLDELLVDVCLRSSAAPTYFPSYQGYVDGGVFANNPSLCAIAQAIGEEGLNIDLKDIVVLSLGTGRPP
SYLDGANGYGDWGLLQWLPDLLDLFMDAGVDAADFQCRQLLGERYFRLDPVLPANIDLDDNKQIEELVEI
ANTVDLTE
>gnl|CDD|132853 cd07214, Pat17_isozyme_like, Patatin-like phospholipase of plants. Pat17 is an isozyme of patatin cloned from Solanum cardiophyllum. Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue, and Nu = nucleophile). Patatin-like phospholipase are included in this group. Members of this family have also been found in vertebrates
GKFITVLSIDGGGIRGIIPATILEFLEGKLQELDGPDARIADYFDVIAGTSTGGLITAMLTAPNENKRPL
FAAKDIVQFYLENGPKIFPQSTGQFEDDRKKLRSLLGPKYDGVYLHDLLNELLGDTRLSDTLTNVVIPTF
DIKLLQPVIFSSSKAKNDKLTNARLADVCISTSAAPTYFPAHYFTTEDSNGDIREFNLVDGGVAANNPTL
LAISEVTKEIIKDNPFFASIKPLDYKKLLVLSLGTGSAEESYKYNAAAKWGLITWLSENGXTPIIDIFSN
ASSDMVDYHLSVIFQALDSEKNYLRIQDDSLTGTASSVDDATEENLEKLVEIGKKLLKKPVSRVNLETG
>gnl|CDD|132854 cd07215, Pat17_PNPLA8_PNPLA9_like2, Patatin-like phospholipase of bacteria. Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum
RILSIDGGGIRGIIPATILVSVEEKLQKKTGNPEARLADYFDLVAGTSTGGILTCLYLCPNESGRPKFSA
KEALNFYLERGNYIFKKKIWNKIKSRGGFLNEKYSHKPLEEVLLEYFGDTKLSELLKPCLITSYDIERRS
PHFFKSHTAIKNEQRDFYVRDVARATSAAPTYFEPARIHSLTGEKYTLIDGGVFANNPTLCAYAEARKLK
FEQPGKPTAKDMIILSLGTGKNKKSYTYEKVKDWGLLGWAKPLIDIMMDGASQTVDYQLKQIFDAEGDQQ
QYLRIQPELEDADPEMDDASPENLEKLREVGQALAEDHKDQLDEIVDRL
>gnl|CDD|132855 cd07216, Pat17_PNPLA8_PNPLA9_like3, Patatin-like phospholipase. Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum
LNLLSLDGGGVRGLSSLLILKEIMERIDPKEGLDEPPKPCDYFDLIGGTSTGGLIAIMLGRLRMTVDECI
DAYTRLAKKIFSRKRLRLIIGDLRTGARFDSKKLAEAIKVILKELGNDEDDLLDEGEEDGCKVFVCATDK
DVTGKAVRLRSYPSKDEPSLYKNATIWEAARATSAAPTFFDPVKIGPGGRTFVDGGLGANNPIREVWSEA
VSLWEGLARLVGCLVSIGTGTPSIKSLGRSAEGAGLLKGLKDLVTDTEAEAKRFSAEHSELDEEGRYFRF
NVPHGLEDVGLDEYEKMEEIVSLTREYLA
>gnl|CDD|132856 cd07217, Pat17_PNPLA8_PNPLA9_like4, Patatin-like phospholipase. Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum
KKILALDGGGIRGLLSVEILGRIEKDLRTHLDDPEFRLGDYFDFVGGTSTGSIIAACIALGMSVTDLLSF
YTLNGVNMFDKAWLAQRLFLNKLYNQYDPTNLGKKLNTVFPETTLGDDTLRTLLMIVTRNATTGSPWPVC
NNPEAKYNDSDRSDCNLDLPLWQLVRASTAAPTFFPPEVVSIAPGTAFVFVDGGVTTYNNPAFQAFLMAT
AKPYKLNWEVGADNLLLVSVGTGFAPEARPDLKAADMWALDHAKYIPSALMNAANAGQDMVCRVLGECRK
GGLVDREIGTMHVDPNWLGPKLFTYVRYDVSLSRSGLDVLGLSDSQLEAVQKMDAVDQMEELQR
>gnl|CDD|132857 cd07218, Pat_iPLA2, Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2. Calcium-independent phospholipase A2; otherwise known as Group IVA-1 PLA2. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly);mutagenesis experiments confirm the role of this serine as a nucleophile. Some members of this group show triacylglycerol lipase activity (EC 3:1:1:3). Members include iPLA-1, iPLA-2, and iPLA-3 from Aedes aegypti and show acylglycerol transacylase/lipase activity. Also includes putative iPLA2-eta from Pediculus humanus corporis which shows patatin-like phospholipase activity
MNLSFAGCGFLGIYHVGVAVCLKKYAPHLLLNKISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRH
SLGPFSPSFNIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIP
VFSGLLPPKFRGVRYMDGGFSDNLPTLDENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIY
RLVRILFPPRPEVLSSLCQQGFDDALRFLHRNNLI
>gnl|CDD|132858 cd07219, Pat_PNPLA1, Patatin-like phospholipase domain containing protein 1. Members of this family share a patatin domain, initially discovered in potato tubers. Some members of PNPLA1 subfamily do not have the lipase consensus sequence Gly-X-Ser-X-Gly which is essential for hydrolase activity. This family includes PNPLA1 from Homo sapiens and Gallus gallus. Currently, there is no literature available on the physiological role, structure, or enzymatic activity of PNPLA1. It is expressed in various human tissues in low mRNA levels
MEQVFKGDPDTPHSISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGISMDEY
LRVLNVGVAEVRKSFLGPLSPSCKMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSK
EELIEALYCSCFVPVYCGLIPPTYRGVRYIDGGFTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDF
RIFNCSFQFSLENIARMTHALFPPDLMVLHDYYYRGYQDTVLYLRRLNAVYLNSPSKRVIFPRVEVYCQA
LGKECPQRSQPSLQDGQASLEESWQPHLARAPKGDGRGLHDPPLSPPLAAPESTAEWVVESPVSSPASPL
ESSPSLPGSLTDLSPASLPAVHSLPSSTPGLS
>gnl|CDD|132859 cd07220, Pat_PNPLA2, Patatin-like phospholipase domain containing protein 2. PNPLA2 plays a key role in hydrolysis of stored triacylglecerols and is also known as adipose triglyceride lipase (ATGL). Members of this family share a patain domain, initially discovered in potato tubers. ATGL is expressed in white and brown adipose tissue in high mRNA levels. Mutations in PNPLA2 encoding adipose triglyceride lipase (ATGL) leads to neutral lipid storage disease (NLSD) which is characterized by the accumulation of triglycerides in multiple tissues. ATGL mutations are also commonly associated with severe forms of skeletal- and cardio-myopathy. This family includes patatin-like proteins: TTS-2.2 (transport-secretion protein 2.2), PNPLA2 (Patatin-like phospholipase domain-containing protein 2), and iPLA2-zeta (Calcium-independent phospholipase A2) from Homo sapiens
LDSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVA
KEARKRFLGPLHPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALV
CSCFIPVYCGLIPPTLRGVRYVDGGISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQ
FNLRNLYRLSKALFPPEPQVLAEMCKQGYRDALRFLKEN
>gnl|CDD|132860 cd07221, Pat_PNPLA3, Patatin-like phospholipase domain containing protein 3. PNPLA3 is a triacylglycerol lipase that mediates triacylglycerol hydrolysis in adipocytes and is an indicator of the nutritional state. PNPLA3 is also known as adiponutrin (ADPN) or iPLA2-epsilon. Human adiponutrins are bound to the cell membrane of adipocytes and show transacylase, TG hydrolase, and PLA2 activity. This family includes patatin-like proteins: ADPN (adiponutrin) from mammals, PNPLA3 (Patatin-like phospholipase domain-containing protein 3), and iPLA2-epsilon (Calcium-independent phospholipase A2) from Homo sapiens
WSLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSAR
SRNIGILHPSFNLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCF
IPFFSGLIPPSFRGVRYVDGGVSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTE
NLYLLTRALFPPDVKVLGEICLRGYLDAFRFLEENGICNRPQ
>gnl|CDD|132861 cd07222, Pat_PNPLA4, Patatin-like phospholipase domain containing protein 4. PNPLA4, also known as GS2 (gene sequence-2), shows both lipase and transacylation activities. GS2 lipase is expressed in various tissues, predominantly in muscle and adipocytes tissue. It is also expressed in keratinocytes and shows retinyl ester hydrolase, acylglycerol, TG hydrolase, and PLA2 activity. This family includes patatin-like proteins: GS2 from mammals, PNPLA4 (Patatin-like phospholipase domain-containing protein 4), and iPLA2-eta (Calcium-independent phospholipase A2) from Homo sapiens
NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLTAPEKIEECKEFTYKFAEEVR
KQRFGAMTPGYDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCY
VPVYAGLKPVEYKGQKWIDGGFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLA
NLVRLNQALFPPNRRKLESYYQMGFDDAVRFLKKEN
>gnl|CDD|132862 cd07223, Pat_PNPLA5-mammals, Patatin-like phospholipase domain containing protein 5. PNPLA5, also known as GS2L (GS2-like), plays a role in regulation of adipocyte differentiation. PNPLA5 is expressed in brain tissue in high mRNA levels and low levels in liver tissue. There is no concrete evidence in support of the enzymatic activity of GS2L. This family includes patatin-like proteins: GS2L (GS2-like) and PNPLA5 (Patatin-like phospholipase domain-containing protein 5) reported exclusively in mammals
MDFLEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSN
LLGMVKHLERLSLGIFHPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDEL
IQALICTLYFPFYCGIIPPEFRGERYIDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAF
NASFQISTRNFFLGLKCLIPPKPEVVADNCRQGYLDALRFLERRGLTKEPVLWSLVSKEPPAPADGPRDT
GHDQGQKGGLSLNWDVPNVLVKDVPNFEQLSPELEAALKKACTRDFSTWARFCCSVPGKVLTYLLLPCTL
PFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLRLGSPPVTR
>gnl|CDD|132863 cd07224, Pat_like, Patatin-like phospholipase. Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates
GFSFSAAGLLFPYHLGVLSLLIEAGVINETTPLAGASAGSLAAACSASGLSPEEALEATEELAEDCRSNG
TAFRLGGVLRDELDKTLPDDAHERCNRGRIRVAVTQLFPVPRGLLVSSFDSKSDLIDALLASCNIPGYLA
PWPATMFRGKLCVDGGFALFIPPTTAADRTVRVCPFPASRSSIKGQNLDNDDTEDVPYSRRQLLNWALEP
ADDAMLLELFNEGYKDANEWAKE
>gnl|CDD|132864 cd07225, Pat_PNPLA6_PNPLA7, Patatin-like phospholipase domain containing protein 6 and protein 7. Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are 60% identical to each other. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologous to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes PNPLA6 and PNPLA7 from Homo sapiens, YMF9 from Yeast, and Swiss Cheese protein (sws) from Drosophila melanogaster
HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMK
QRAREWAKDMTSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTD
GSLWRYVRASMSLSGYLPPLCDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDA
LSGWWLLWKRWNPLAEKVKVPNMAEIQSRLAYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEIC
EVGYQHGKTVFDGWKRSGVLEKMLQD
>gnl|CDD|132865 cd07227, Pat_Fungal_NTE1, Fungal patatin-like phospholipase domain containing protein 6. These are fungal Neuropathy Target Esterase (NTE), commonly referred to as NTE1. Patatin-like phospholipase. NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. This family includes NTE1 from fungi
RLARRLCGQAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKK
FAGRMASMWRFLSDVTYPFASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWR
YIRASMSLAGLLPPLSDNGSMLLDGGYMDNLPVSPMRSLGIRDIFAVDVGSVDDRTPMDYGDSVSGVWIF
FNRWNPFSSRPNVPSMAEIQSRLTYVSSVKTLEKVKATPGCHYMRPPVQDFDTLDFGKF
>gnl|CDD|132866 cd07228, Pat_NTE_like_bacteria, Bacterial patatin-like phospholipase domain containing protein 6. Bacterial patatin-like phospholipase domain containing protein 6. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. This group includes YCHK and rssA from Escherichia coli as well as Ylbk from Bacillus amyloliquefaciens
IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEWVRSLSQRDVLRLLD
LSASRSGLLKGEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAP
VEHNGRLLVDGGVVNPIPVSVARALGADIVIAVDL
>gnl|CDD|132867 cd07229, Pat_TGL3_like, Triacylglycerol lipase 3. Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG lipase activity of the lipid particle. Triacylglycerol (TAG) lipases are also necessary for the mobilization of TAG stored in lipid particles. TGL3 contains the consensus sequence motif GXSXG, which is found in lipolytic enzymes. This family includes Tgl3p from Saccharomyces cerevisiae
GDILTLLNLLRSGLVRNLGNITSPKLFTRAYAGTKLLIEEYITEVAECLEYVTALQTSPMHSKGFSSQAK
LDFFHDTRQSFGRTALVLQGGSIFGLCHLGVVKALWLRGLLPRIITGTATGALIAALVGVHTDEELLRFL
DGDGIDLSAFNRLRGKKSLGYSGYGWLGTLGRRIQRLLREGYFLDVKVLEEFVRANLGDLTFEEAYARTG
RVLNITVAPSAVSGSPNLLNYLTAPNVLIWSAALASNASSAALYRSVTLLCKDETGSIVPWPPVQVLFFR
SWRGANYSERESPLARLSELFNVNHFIVSQARPYLAPFLSSDLHENIPGPNITLVPELSFSDFLRLFQNP
TTDEIQYWILKGERGVWPALAALRVRCAVEFELDDGYQVLR
>gnl|CDD|132868 cd07230, Pat_TGL4-5_like, Triacylglycerol lipase 4 and 5. TGL4 and TGL5 are triacylglycerol lipases that are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. Tgl4 is a functional ortholog of mammalian adipose TG lipase (ATGL) and is phosphorylated and activated by cyclin-dependent kinase 1 (Cdk1/Cdc28). TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. This family includes TGL4 (STC1) and TGL5 (STC2) from Saccharomyces cerevisiae
LLYLIRTTLSRDLGNMGNVNLYRHSHVGTKKLIERYITEALLTLEYLVDDDEDGLEDRYLLGMLLQTRKN
FGRTALLLSGGGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEIPELLEEFPYGDFNV
FEDPDQEENVLQKLSRFLKYGSWFDISHLTRVMRGFLGDLTFQEAYNRTRRILNITVSPASIYELPRLLN
YITAPNVLIWSAVCASCSVPGVFPSSPLYEKDPKTGEIVPWNPSSVKWIDGSVDNDLPMTRLSEMFNVNH
FIVSQVNPHVVPFLKKSESCVGGEVEDELSARFKRWLNNVTDLAKDEVLHRLQLLSELGIFPNLLTKLRS
VLSQKYSGDITILPELNYSDFPKILKNPTPEFMLDACLRGERATWPKLSRIRNHCAIELALDKAIQYLRA
R
>gnl|CDD|132869 cd07231, Pat_SDP1-like, Sugar-Dependent 1 like lipase. Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This acyl-hydrolase domain is homologus to yeast triacylglycerol lipase 3 and human adipose triglyceride lipase. This family includes SDP1 from Arabidopsis thaliana
LRADLVRNLGNMCNPELHKGRLEVPRLIRDYIAEVKAQLRAVVESDEDELSLEEKLAFFQETRHAFGRTA
LLLSGGAALGTFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEELQSFFRALLGDLTFQEAYDR
TGRILGITVCPPRKSEPPRLLNYLTSPHVVIWSAVAASCAFPGLFEAQELMAKDRFGEIVPYHPPGKVSS
PRRWRDGSLEQDLPMQQLRELFNVNHFIVSQANPHIVPLLRLKKLFAQEWEGDITIVMPITWKQLLKIIQ
NPTPEELRKAAMAGERCTWEKLSAIESNCGIELTLDECVAELR
>gnl|CDD|132870 cd07232, Pat_PLPL, Patain-like phospholipase. Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants and fungi. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates
LRGCVKNNFAGIENGRLYSETYYGTKNLVEEYIDEVEACLKYLRESSQLDLEEKRRLFKRLSTNYGRTAL
CLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVAALLCTRTDEELKQLLVPELARKITACEPPWL
VWIPRWLKTGARFDSVEWARTCCWFTRGSMTFEEAYERTGRILNISVVPADPHSPTILLNYLTSPNCTIW
SAVLASAAVPGILNPVVLMMKDPDGTLIPPFSFGSKWKDGSLRTDIPLKALNTLFNVNFSIVSQVNPHIN
LFFFSSRGSVGRPVSHRKGRGWRGGFLLSALEQYLKLDIKKWLKVLRDLELLPRPLGQDWSQIFLQDFSG
TITIWPRSTLSDFLRILSDPTPEDLERMIHEGQQAAFPKLHFIKNRMRIEKAIEDGR
>gnl|CDD|319900 cd07233, GlxI_Zn, Glyoxalase I that uses Zn(++) as cofactor. This family includes eukaryotic glyoxalase I that prefers the divalent cation zinc as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event
FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIPKDPRTAWVFSREGTLELTH
NWGTENDEDPVYHNGNSDPRGFGHIGIAVDDVYAACERFEELGVKFKKKPDDGKMKGIAFIKDPDGYWIE
IL
>gnl|CDD|319901 cd07235, MRD, Mitomycin C resistance protein (MRD). Mitomycin C (MC) is a naturally occurring antibiotic, and antitumor agent used in the treatment of cancer. Its antitumor activity is exerted primarily through monofunctional and bifunctional alkylation of DNA. MRD binds to MC and functions as a component of the MC exporting system. MC is bound to MRD by a stacking interaction between a His and a Trp. MRD adopts a structural fold similar to bleomycin resistance protein, glyoxalase I, and extradiol dioxygenases; and it has binding sites at an identical location to binding sites in these evolutionarily related enzymes
ISLIAIVVEDMAKSLEFYRKLGFEVPEEADSAPHTEAALPGGIRLALDTEETIRSYDPGWQAPTGGGRFA
IAFLCPTPAEVDAKYAELTGAGYEGHLKPWNAPWGQRYAIVKDPDGNVVDLFA
>gnl|CDD|319902 cd07237, BphC1-RGP6_C_like, C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase. This subfamily contains the C-terminal, catalytic, domain of BphC1-RGP6 and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, and has Fe(II) at the catalytic site. Its C-terminal repeat is represented in this subfamily. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, they belong to a different subfamily of the ED_TypeI_classII_C (C-terminal domain of type I, class II extradiol dioxygenases) family
GGFVTGDQGLGHVVLIVPDVDEALAFYTDVLGFRLSDEIRIPLPPGVTARLHFLHCNGRHHSLAFGAGPG
PKRLHHLMLEVTSLDDVGRAYDRVRKRGIPIAMTLGRHTNDKMLSFYVATPSGFLIEYGWGGRVVDEDWT
VEEYDAPSIWGHK
>gnl|CDD|319903 cd07238, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
RIVANIATADPERAAAFYGDHLGLPLVMDHGWIVTFASPGNAHAQISLAREGGSGTVVPDLSIEVDDVDA
VHARVVAAGLRIEYGPTTEAWGVRRFFVRDPFGRLINILTHV
>gnl|CDD|319904 cd07239, BphC5-RK37_C_like, C-terminal, catalytic domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase). 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). The enzyme contains a N-terminal and a C-terminal domain of similar structure fold, resulting from an ancient gene duplication. BphC belongs to the type I extradiol dioxygenase family, which requires a metal in the active site for its catalytic activity. Polychlorinated biphenyl degrading bacteria demonstrate multiplicity of BphCs. Bacterium Rhodococcus rhodochrous K37 has eight genes encoding BphC enzymes. This family includes the C-terminal domain of BphC5-RrK37. The crystal structure of the protein from Novosphingobium aromaticivorans has a Mn(II)in the active site, although most proteins of type I extradiol dioxygenases are activated by Fe(II)
VPVKLSHVVLNSPDLDKTVAFYEDVLGFRVSDWLGDVMHFLRCNSQHHSIAIARGPHTSLNHVAYEMRSV
DEYMRGSGRLIRSGARKIWGPGRHMAGDNTFSYFLDPHGNVVEYTSELELLDEDWHPHVVDFSEPEVTDQ
WGT
>gnl|CDD|319905 cd07241, VOC_BsYyaH, vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
KIEHVALWTNDLERMKDFYVKYFGAESNDIYHNKKKGFRSYFLTFDSGARLELMSRPDVTDPDKEVERTG
LAHIAFSVGSKEAVDELTERLRADGYAVVGGPRTTGDGYYESVILDPEGNRIEIT
>gnl|CDD|319906 cd07242, VOC_BsYqjT, vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
GVSHVELAVSDLHRSFKWFEWILGLGWKEYDTWSFGPSWKLSGGSLLVVQQTDEFATPEFDRARVGLNHL
AFHAESREAVDELTEKLAKIGGVRTYGDRHPFAGGPPHYAAFCEDPDGIKLELVAP
>gnl|CDD|319907 cd07243, 2_3_CTD_C, C-terminal domain of catechol 2,3-dioxygenase. This subfamily contains the C-terminal, catalytic, domain of catechol 2,3-dioxygenase. Catechol 2,3-dioxygenase (2,3-CTD, catechol:oxygen 2,3-oxidoreductase) catalyzes an extradiol cleavage of catechol to form 2-hydroxymuconate semialdehyde with the insertion of two atoms of oxygen. The enzyme is a homotetramer and contains catalytically essential Fe(II) . The reaction proceeds by an ordered bi-unit mechanism. First, catechol binds to the enzyme, this is then followed by the binding of dioxygen to form a tertiary complex, and then the aromatic ring is cleaved to produce 2-hydroxymuconate semialdehyde. Catechol 2,3-dioxygenase belongs to the type I extradiol dioxygenase family. The subunit comprises the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. This subfamily represents the C-terminal domain
GIAAHRLDHCLLYGERIAETTRFFTDVLGFYLTERVLDPDGGTRVGIFLSCSNKAHDIAFVGYPEDGKLH
HTSFFLESWEDVLKAGDIISKNDVSIDIGPTRHGITRGQTIYFFDPSGNRNETFAGGYIAYPDMPVVTWT
EDQL
>gnl|CDD|319908 cd07244, FosA, fosfomycin resistant protein subfamily FosA. This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases
GINHITLAVSDLERSLAFYVDLLGFKPHVRWDKGAYLTAGDLWLCLSLDPAAEPSPDYTHIAFTVSEEDF
EELSERLRAAGVKIWQENSSEGDSLYFLDPDGHKLELHVGSLESRLASLRE
>gnl|CDD|319909 cd07245, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
LDHVALACPDLERARRFYTDVLGLEEVPRPPFLKFGGAWLYLGGGQQIHLVVEQNPSELPRPEHPGRDRH
PSFSVPDLDALKQRLKEAGIPYTESTSPGGGVTQLFFRDPDGNRLEF
>gnl|CDD|319910 cd07246, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
TTVSPYLVVEDAAAAIAFYKKAFGAEELGRTTQEDGRVGHAELRIGGTVVMVADENPERGALSPTKLGGT
PVIFHLYVEDVDATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP
>gnl|CDD|319911 cd07247, SgaA_N_like, N-terminal domain of Streptomyces griseus SgaA and similar domains. SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein
PVWFELPTTDLERAKAFYGAVFGWTFEDEGDGGGDYALFTAGGGAVGGLMRAPEEVAGAPPGWLIYFAVD
DLDAALARVEAAGGKVVVPPTDIPGGGRFAVFADPEGNRFGLWS
>gnl|CDD|319912 cd07249, MMCE, Methylmalonyl-CoA epimerase (MMCE). MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) interconverts (2R)-methylmalonyl-CoA and (2S)-methylmalonyl-CoA. MMCE has been found in bacteria, archaea, and in animals. In eukaryotes, MMCE is an essential enzyme in a pathway that converts propionyl-CoA to succinyl-CoA, and is important in the breakdown of odd-chain length fatty acids, branched-chain amino acids, and other metabolites. In bacteria, MMCE participates in the reverse pathway for propionate fermentation, glyoxylate regeneration, and the biosynthesis of polyketide antibiotics. MMCE is closely related to glyoxalase I and type I extradiol dioxygenases
LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNTQIELLEPLGEDSPIAKFLDKKGG
GLHHIAFEVDDIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFLHPKDTGGVLIELVE
>gnl|CDD|319913 cd07250, HPPD_C_like, C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase (HmaS). HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of 4-hydroxyphenylpyruvate to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_C_like domain represents the C-terminal domain
LTRIDHVVGNVPDGEMDPAVEWYEKCLGFHRFWEFDDEDIGTEYSGLRSIVLANPNETIKLPLNEPAPGK
RKSQIQEFLDYHGGAGVQHIALNTDDIFATVRALRARGVEFLPPPDAYYDDLRERLDGLLVKEDLDTLKE
LGILVDRDEQGYLLQIFTKPLQDRPTLFFEIIQRRGAGGFGAGNFKALFEAIER
>gnl|CDD|319914 cd07251, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
LITLGVRDLERSARFYEALGWKPNLDPNDGVVFFQLGGTVLALYPRDALAEDAGVSVTGAGFSGVTLAHN
VRSREEVDQLLAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVAYN
>gnl|CDD|319915 cd07252, BphC1-RGP6_N_like, N-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase. This subfamily contains the N-terminal, non-catalytic, domain of BphC1-RGP6 and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of 2,3-dihydroxybiphenyl 1,2-dioxygenases. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, and has Fe(II) at the catalytic site. Its N-terminal repeat is represented in this subfamily. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, they belong to a different family, the ED_TypeI_classII_C (C-terminal domain of type I, class II extradiol dioxygenases) family
RSLGYLGFEVSDLDAWREFATDVLGLQVADDGPDDALYLRMDDRAHRIAVHPGEVDDLAYAGWEVADEAA
LDALAERLEAAGIEVTTGSAELAAERGVLGLIKFTDPSGNPHEIFYGPRE
>gnl|CDD|319916 cd07253, GLOD5, Human glyoxalase domain-containing protein 5 and similar proteins. Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 and similar proteins. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLC
FITETPIDEVLEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY
>gnl|CDD|319917 cd07254, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
KRFHLSLNVTDLERSIRFYSDLFGAEPAKRKADYAKFMLEDPPLNLALLVNDRKEPYGLNHLGIQVDSKE
EVAALKARAEAAGLPVRKEPRTTCCYAVQDKFWLTDPDGNAWEFYATLTE
>gnl|CDD|319918 cd07255, VOC_BsCatE_like_N, N-terminal of Bacillus subtilis CatE like protein. Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
TRIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQVLLVLEAIPDAVLAPRSTTGLYHFAI
LLPDRKALGRALAHLAEHGPLIGAADHGVSEAIYLSDPEGNGIEIYADRPREQW
>gnl|CDD|319919 cd07256, HPCD_C_class_II, C-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD). This subfamily contains the C-terminal, catalytic, domain of HPCD. HPCD catalyses the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. The aromatic ring of 4-hydroxyphenylacetate is opened by this dioxygenase to yield the 3,4-diol product, 2-hydroxy-5-carboxymethylmuconate semialdehyde. HPCD is a homotetramer and each monomer contains two structurally homologous barrel-shaped domains at the N- and C-terminus. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism. Most extradiol dioxygenases contain Fe(II) in their active site, but HPCD can be activated by either Mn(II) or Fe(II). These enzymes belong to the type I class II family of extradiol dioxygenases. The class III 3,4-dihydroxyphenylacetate 2,3-dioxygenases belong to a different superfamily
LLRIDHFNQRVPDVDAGLRYYEDLGFRVSEYTEDDDGETWAAWMHRKGGVHDTALTNGNGPRLHHVAFWV
PEPHNIIQTCDLMAAARYSDRIERGPGRHGVSNAFFLYILDPDGHRIEIYTSDYYTVDPDNPPIKWDVHD
PQRQTWWGAPVPRSWFEEAS
>gnl|CDD|319920 cd07257, THT_oxygenase_C, The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase. This subfamily contains the C-terminal, catalytic, domain of THT oxygenase. THT oxygenase is an extradiol dioxygenase in the 2,4-dinitrotoluene (DNT) degradation pathway. It catalyzes the conversion of 2,4,5-trihydroxytoluene to an unstable ring fission product, 2,4-dihydroxy-5-methyl-6-oxo-2,4-hexadienoic acid. The native protein was determined to be a dimer by gel filtration. The enzyme belongs to the type I family of extradiol dioxygenases which contains two structurally homologous barrel-shaped domains at the N- and C-terminus of each monomer. The active-site metal is located in the C-terminal barrel. Fe(II) is required for its catalytic activity
KLGHVGLEVNDFEATFDWYTKTFGLKPSDVIYLPDGKTVGSFLHLDRGSEYVDHHSFFFAQGPRPKVHHA
AFEVHDFDSQVLGHDWLREKGYKHVWGVGRHILGSQIFDYWFDPSGFIVEHYTDGDLVNADTPIGLHAAG
PETLSQWGPALP
>gnl|CDD|319921 cd07258, PpCmtC_C, C-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC). This subfamily contains the C-terminal, catalytic, domain of PpCmtC. 2,3-dihydroxy-p-cumate-3,4-dioxygenase (CmtC of Pseudomonas putida F1) is a dioxygenase involved in the eight-step catabolism pathway of p-cymene. CmtC acts upon the reaction intermediate 2,3-dihydroxy-p-cumate, yielding 2-hydroxy-3-carboxy-6-oxo-7-methylocta-2,4-dienoate. The CmtC belongs to the type I family of extradiol dioxygenases. Fe2+ was suggested as a cofactor, same as for other enzymes in the family. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism
SHVGLNSTNPERDEDFWTDVCNARVSDRIGDIFLMRVNAIHHTFALGPASSSGIQHINHQVTSIDDVLRS
YYRLKEHDVPIVFGPGRHPTSGARFLYFKGPDGMTFEYSVGVDEIEDEATHRPRQFGFEPESLCMWGA
>gnl|CDD|319922 cd07261, EhpR_like, phenazine resistance protein, EhpR. Phenazine resistance protein (EhpR) in Enterobacter agglomerans confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. EhpR is evolutionarily related to glyoxalase I and type I extradiol dioxygenases
LVILYVDNPERSTEFYRFLLGKEPVESSPTFASFVLSGGAKLGLWSSEEVEPKVAVTGGGAELSFMVPSG
EQVDEVYAEWKAMGIPIIQEPTTMDFGYTFVATDPDGHRLRVCC
>gnl|CDD|319923 cd07262, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
ISHVTIGVNDLERSRAFYDAALAPLGYKRGFEDGGRVGYGLEGGPDFWVTEPFDGEPATAGNGTHVAFAA
PSRAAVDAFHAAALAAGGTDNGAPGLRPHYHPGYYAAYVRDPDGNKIEAVC
>gnl|CDD|319924 cd07263, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
QVMLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRWVTVAPPGSPGTSLLLEPKAHPAQMPQSPEAAGGTP
GILLATDDIDATYERLTAAGVTFVQEPTQMGGGRVANFRDPDGNLFALME
>gnl|CDD|319925 cd07264, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
IAYIVLYVDDFAASLRFYRDVLGLPPRFLHEEGEYAEFDTGETKLALFSRKEMARSGGPDRRGSAFELGF
EVDDVEATVEELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEICEP
>gnl|CDD|319926 cd07265, 2_3_CTD_N, N-terminal domain of catechol 2,3-dioxygenase. This subfamily contains the N-terminal, non-catalytic, domain of catechol 2,3-dioxygenase. Catechol 2,3-dioxygenase (2,3-CTD, catechol:oxygen 2,3-oxidoreductase) catalyzes an extradiol cleavage of catechol to form 2-hydroxymuconate semialdehyde with the insertion of two atoms of oxygen. The enzyme is a homotetramer and contains catalytically essential Fe(II) . The reaction proceeds by an ordered bi-unit mechanism. First, catechol binds to the enzyme, this is then followed by the binding of dioxygen to form a tertiary complex, and then the aromatic ring is cleaved to produce 2-hydroxymuconate semialdehyde. Catechol 2,3-dioxygenase belongs to the type I extradiol dioxygenase family. The subunit comprises the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. This subfamily represents the N-terminal domain
GVLRPGHVQLRVLDLEEAIKHYREVLGLVETGRDDQGRVYLKAWDEYDHHSIILREADTAGLDFMGFKVL
DDADLEQLEARLQAYGVTVTRIPAGELPGVGRRVRFQLPSGHTMELYAEKEY
>gnl|CDD|319927 cd07266, HPCD_N_class_II, N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD). This subfamily contains the N-terminal, non-catalytic, domain of HPCD. HPCD catalyses the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. The aromatic ring of 4-hydroxyphenylacetate is opened by this dioxygenase to yield the 3,4-diol product, 2-hydroxy-5-carboxymethylmuconate semialdehyde. HPCD is a homotetramer and each monomer contains two structurally homologous barrel-shaped domains at the N- and C-terminus. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism. Most extradiol dioxygenases contain Fe(II) in their active site, but HPCD can be activated by either Mn(II) or Fe(II). These enzymes belong to the type I class II family of extradiol dioxygenases. The class III 3,4-dihydroxyphenylacetate 2,3-dioxygenases belong to a different superfamily
DIIRLAHAELVVTDLAASREFYVDTLGLHVTDEDDNAIYLRGVEEFIHHTLVLRKAPEAAVGHLGFRVRD
EADLDKAAAFYKELGLPTEWREEPGQGRTLRVEDPFGFPIEFYLEMDH
>gnl|CDD|319928 cd07267, THT_Oxygenase_N, N-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase. This subfamily contains the N-terminal, non-catalytic, domain of THT oxygenase. THT oxygenase is an extradiol dioxygenase in the 2,4-dinitrotoluene (DNT) degradation pathway. It catalyzes the conversion of 2,4,5-trihydroxytoluene to an unstable ring fission product, 2,4-dihydroxy-5-methyl-6-oxo-2,4-hexadienoic acid. The native protein was determined to be a dimer by gel filtration. The enzyme belongs to the type I family of extradiol dioxygenases which contains two structurally homologous barrel-shaped domains at the N- and C-terminus of each monomer. The active-site metal is located in the C-terminal barrel. Fe(II) is required for its catalytic activity
LTRLAHVVYEHPDLEKAERFLTDFGLIVAYRTGEEIYYRGYGTDPYVYVARKSSRSRFLGAAFVAASRAD
LEKAATLPGASPIEDLEAPGGGKVVTLTDPDGFPVHLVYGQES
>gnl|CDD|319929 cd07268, VOC_EcYecM_like, Escherichia coli YecM and similar proteins, a vicinal oxygen chelate subfamily. Uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily contains Escherichia coli YecM and similar proteins.The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
DLPSFEDKIFELLIKLGLDLKELPIDHIALRVNTNAFAEEWKIGLSQCGELLSDNEINGRPIYLFKLEKP
LQYANQSIDIVELPAPKNKRYPYEGWEHIEIVIPEPPQELVSRSQNLPLLNGLSPIDISLKFSEPKGEKE
RLPNPTVAVSFGKVCIKFHPYSIEEVVASEQ
>gnl|CDD|132809 cd07276, PX_SNX16, The phosphoinositide binding Phox Homology domain of Sorting Nexin 16. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking
DRPIRPPILGYEVMEERARFTVYKIRVENKVGDSWFVFRRYTDFVRLNDKLKQMFPGFRLSLPPKRWFKD
NFDPDFLEERQLGLQAFVNNIMAHKDIAKCKLVREFFCLD
>gnl|CDD|132810 cd07277, PX_RUN, The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains. The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways
INVWIPSVFLRGKGSDAHHVYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNKD
AKFVEERRKRLQVYLRRVVNTLIQTSPELTACPSKETLIKLLPFFGDT
>gnl|CDD|132811 cd07278, PX_RICS_like, The phosphoinositide binding Phox Homology domain of PX-RICS-like proteins. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this family include PX-RICS, TCGAP (Tc10/Cdc42 GTPase-activating protein), and similar proteins. They contain N-terminal PX and Src Homology 3 (SH3) domains, a central Rho GAP domain, and C-terminal extensions. They act as Rho GTPase-activating proteins. PX-RICS is the main isoform expressed during neural development. It is involved in neural functions including axon and dendrite extension, postnatal remodeling, and fine-tuning of neural circuits during early brain development. The PX domain of PX-RICS specifically binds phosphatidylinositol 3-phosphate (PI3P), PI4P, and PI5P. TCGAP is widely expressed in the brain where it is involved in regulating the outgrowth of axons and dendrites and is regulated by the protein tyrosine kinase Fyn. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction
NVDIGSLQVVLSDDGSLKSYKNSGKELVYLVQVQCQGKSWLVKRSYDDFRMLDKHLHQCIYDRKFSQLTE
LPEECIEKREQQNLHQVLSDYLKRLSSIAGNLLNCGPVLNWLEL
>gnl|CDD|132812 cd07279, PX_SNX20_21_like, The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development
LKFEIVSARTVKEGEKKYVVYQLAVVQTGDPDTQPAFIERRYSDFLKLYKALRKQHPQLMAKVSFPRKVL
MGNFSSELIAERSRAFEQFLGHILSIPNLRDSKAFLDFLQGP
>gnl|CDD|132813 cd07280, PX_YPT35, The phosphoinositide binding Phox Homology domain of the fungal protein YPT35. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of YPT35 proteins from the fungal subkingdom Dikarya. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of YPT35 binds to phosphatidylinositol 3-phosphate (PI3P). It also serves as a protein interaction domain, binding to members of the Yip1p protein family, which localize to the ER and Golgi. YPT35 is mainly associated with endosomes and together with Yip1p proteins, may be involved in a specific function in the endocytic pathway
HATDVNVGDYTIVGGDTGGGAYVVWKITIETKDLIGSSIVAYKRYSEFVQLREALLDEFPRHKRNEIPQL
PPKVPWYDSRVNLNKAWLEKRRRGLQYFLNCVLLNPVFGGSPVVKEFLLP
>gnl|CDD|132814 cd07281, PX_SNX1, The phosphoinositide binding Phox Homology domain of Sorting Nexin 1. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX1 is both membrane associated and a cytosolic protein that exists as a tetramer in protein complexes. It can associate reversibly with membranes of the endosomal compartment, thereby coating these vesicles. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 contains a Bin/Amphiphysin/Rvs (BAR) domain C-terminal to the PX domain. The PX domain of SNX1 specifically binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,5)P2, while the BAR domain detects membrane curvature. Both domains help determine the specific membrane-targeting of SNX1, which is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network
LKVSITDPEKIGDGMNAYVVYKVTTQTSLLMFRSKHFTVKRRFSDFLGLYEKLSEKHSQNGFIVPPPPEK
SLIGMTKVKVGKEDSSSAEFLERRRAALERYLQRIVSHPSLLQDPDVREFLEKE
>gnl|CDD|132815 cd07282, PX_SNX2, The phosphoinositide binding Phox Homology domain of Sorting Nexin 2. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX2 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. Similar to SNX1, SNX2 contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX domain of SNX2 preferentially binds phosphatidylinositol-3-phosphate (PI3P), but not PI(3,4,5)P3. Studies on mice deficient with SNX1 and/or SNX2 suggest that they provide an essential function in embryogenesis and are functionally redundant
IEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSRSEFSVRRRFSDFLGLHSKLASKYLHVGYIVPPAPEK
SIVGMTKVKVGKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESS
>gnl|CDD|132816 cd07283, PX_SNX30, The phosphoinositide binding Phox Homology domain of Sorting Nexin 30. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX30 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX30 has yet to be elucidated
LFVTVDDPKKHVCTMETYITYRVTTKTTRTEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFV
VKGVVDRFSEEFVETRRKALDKFLKRIADHPVLSFNEHFNVFLTAK
>gnl|CDD|132817 cd07284, PX_SNX7, The phosphoinositide binding Phox Homology domain of Sorting Nexin 7. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX7 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, SNX30, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX7 has yet to be elucidated
IFITVDEPESHVTAIETFITYRVMTKTSRSEFDSSEFEVRRRYQDFLWLKGRLEEAHPTLIIPPLPEKFV
MKGMVERFNEDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ
>gnl|CDD|132818 cd07285, PX_SNX9, The phosphoinositide binding Phox Homology domain of Sorting Nexin 9. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX9, also known as SH3PX1, is a cytosolic protein that interacts with proteins associated with clathrin-coated pits such as Cdc-42-associated tyrosine kinase 2 (ACK2). It contains an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature. The PX-BAR structural unit helps determine specific membrane localization. Through its SH3 domain, SNX9 binds class I polyproline sequences found in dynamin 1/2 and the WASP/N-WASP actin regulators. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis. Its array of interacting partners suggests that SNX9 functions at the interface between endocytosis and actin cytoskeletal organization
FDCVVADPRKGSKMYGLKSYIEYQLTPTNTNRSVNHRYKHFDWLYERLLVKFGLAIPIPSLPDKQVTGRF
EEEFIKMRMERLQAWMTRMCRHPVISESEVFQQFLNFRDEKEWKTGKRKAEKDETV
>gnl|CDD|132819 cd07286, PX_SNX18, The phosphoinositide binding Phox Homology domain of Sorting Nexin 18. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX18, like SNX9, contains an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature. The PX-BAR structural unit helps determine specific membrane localization. SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1
FQCTIDDPTKQTKFKGMKSYISYKLVPSHTGLQVHRRYKHFDWLYARLAEKFPVISVPHIPEKQATGRFE
EDFISKRRKGLIWWMDHMCSHPVLARCDAFQHFLTCPSTDEKAWKQGKRKAEKDEMV
>gnl|CDD|132820 cd07287, PX_RPK118_like, The phosphoinositide binding Phox Homology domain of RPK118-like proteins. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily bear similarity to human RPK118, which contains an N-terminal PX domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. It also binds the antioxidant peroxiredoxin-3 (PRDX3) and may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. Members of this subfamily also show similarity to sorting nexin 15 (SNX15), which contains PX and MIT domains but does not contain a kinase domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein
LARFYTVTDPRRHPKGYTVYKVTARIVSRKNPEDVQEIVVWKRYSDFKKLHKDLWQIHKNLCRQSELFPP
FAKAKVFGRFDESVIEERRQCAEDLLQFSANIPALYNSSQLEDFFKGG
>gnl|CDD|132821 cd07288, PX_SNX15, The phosphoinositide binding Phox Homology domain of Sorting Nexin 15. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX15 contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. It plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein
YYRFYSVTDPRTHPKGYTEYKVTAQFISKKQPEDVKEVVVWKRYSDLKKLHGELAYTHRNLFRRQEEFPP
FPRAQVFGRFEAAVIEERRNAAEAMLLFTVNIPALYNSPQLKEFFRDG
>gnl|CDD|132822 cd07289, PX_PI3K_C2_alpha, The phosphoinositide binding Phox Homology Domain of the Alpha Isoform of Class II Phosphoinositide 3-Kinases. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. The class II alpha isoform, PI3K-C2alpha, plays key roles in clathrin assembly and clathrin-mediated membrane trafficking, insulin signaling, vascular smooth muscle contraction, and the priming of neurosecretory granule exocytosis. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction
EVSVFTYHKRYNPDKHYIYVVRILREGQIEPSFVFRTFDEFQELHNKLSILFPLWKLPGFPNKMVLGRTH
IKDVAAKRKVELNSYIQSLMNSSTEVAECDLVYTFFHPL
>gnl|CDD|132823 cd07290, PX_PI3K_C2_beta, The phosphoinositide binding Phox Homology Domain of the Beta Isoform of Class II Phosphoinositide 3-Kinases. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. The class II beta isoform, PI3K-C2beta, contributes to the migration and survival of cancer cells. It regulates Rac activity and impacts membrane ruffling, cell motility, and cadherin-mediated cell-cell adhesion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction
DVFLCRHESTFNPSKGYAYVVKVQREGHKEATFVQRTFEEFQELHNKLRLLFPSSKLPSFPSRFVIGRSR
GEAVAERRKEELNGYIWHLIHAPPEVAECDLVYTFFHPL
>gnl|CDD|132824 cd07291, PX_SNX5, The phosphoinositide binding Phox Homology domain of Sorting Nexin 5. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. The PX domain of SNX5 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,4)P2. SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels
PSLQIDIPDALSERDKVKFTVHTKTTLPSFQSPDFSVTRQHEDFIWLHDALIETEDYAGLIIPPAPPKPD
FDGPREKMQKLGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEY
D
>gnl|CDD|132825 cd07292, PX_SNX6, The phosphoinositide binding Phox Homology domain of Sorting Nexin 6. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). SNX6 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs
AALQVDISDALSERDKVKFTVHTKSSLPNFKQNEFSVVRQHEEFIWLHDSFVENEDYAGYIIPPAPPRPD
FDASREKLQKLGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEY
N
>gnl|CDD|132826 cd07293, PX_SNX3, The phosphoinositide binding Phox Homology domain of Sorting Nexin 3. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX3 associates with early endosomes through a PX domain-mediated interaction with phosphatidylinositol-3-phosphate (PI3P). It associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer. SNX3 is required for the formation of multivesicular bodies, which function as transport intermediates to late endosomes. It also promotes cell surface expression of the amiloride-sensitive epithelial Na+ channel (ENaC), which is critical in sodium homeostasis and maintenance of extracellular fluid volume
FLEIDVTNPQTVGVGRGRFTTYEIRLKTNLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAL
FRQLPFRGDDGIFDDSFIEERKQGLEQFLNKVAGHPLAQNERCLHMFLQDEII
>gnl|CDD|132827 cd07294, PX_SNX12, The phosphoinositide binding Phox Homology domain of Sorting Nexin 12. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. The specific function of SNX12 has yet to be elucidated
SNFLEIDIFNPQTVGVGRNRFTTYEVRMRTNLPIFKLKESCVRRRYSDFEWLKNELERDSKIVVPPLPGK
ALKRQLPFRGDEGIFEESFIEERRQGLEQFINKIAGHPLAQNERCLHMFLQDETIDRNYVPG
>gnl|CDD|132828 cd07295, PX_Grd19, The phosphoinositide binding Phox Homology domain of fungal Grd19. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Grd19 is involved in the localization of late Golgi membrane proteins in yeast. Grp19 associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer
FLEIEVRNPKTHGIGRGMFTDYEIVCRTNIPAFKLRVSSVRRRYSDFEYFRDILERESPRVMIPPLPGKI
FTNRFSDEVIEERRQGLETFLQSVAGHPLLQTGSKVLAAFLQDPKF
>gnl|CDD|132829 cd07296, PX_PLD1, The phosphoinositide binding Phox Homology domain of Phospholipase D1. The PX domain is a phosphoinositide binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Phospholipase D (PLD) catalyzes the hydrolysis of the phosphodiester bond of phosphatidylcholine to generate membrane-bound phosphatidic acid and choline. PLDs are implicated in many cellular functions like signaling, cytoskeletal reorganization, vesicular transport, stress responses, and the control of differentiation, proliferation, and survival. PLD1 contains PX and Pleckstrin Homology (PH) domains in addition to the catalytic domain. It acts as an effector of Rheb in the signaling of the mammalian target of rapamycin (mTOR), a serine/threonine protein kinase that transduces nutrients and other stimuli to regulate many cellular processes. PLD1 also regulates the secretion of the procoagulant von Willebrand factor (VWF) in endothelial cells. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of PLD1 specifically binds to phosphatidylinositol-3,4,5-trisphosphate [PI(3,4,5)P3], which enables PLD1 to mediate signals via the ERK1/2 pathway
GCPIKARVLEVERFTSTSDVKKPSLNVYTIELTHGEFTWQVKRKFKHFQELHRELLRYKAFIRIPIPTRS
HTVRRQTIKRGEPRHMPSLPRGAEEEAREEQFSSRRKQLEDYLSKLLKMPMYRNYHATMEFIDVS
>gnl|CDD|132830 cd07297, PX_PLD2, The phosphoinositide binding Phox Homology domain of Phospholipase D2. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Phospholipase D (PLD) catalyzes the hydrolysis of the phosphodiester bond of phosphatidylcholine to generate membrane-bound phosphatidic acid and choline. PLD activity has been detected in viruses, bacteria, yeast, plants, and mammals, but the PX domain is not present in PLDs from viruses and bacteria. PLDs are implicated in many cellular functions like signaling, cytoskeletal reorganization, vesicular transport, stress responses, and the control of differentiation, proliferation, and survival. PLD2 contains PX and Pleckstrin Homology (PH) domains in addition to the catalytic domain. It mediates EGF-dependent insulin secretion and EGF-induced Ras activation by the guanine nucleotide-exchange factor Son of sevenless (Sos). It regulates mast cell activation by associating and promoting the activation of the protein tyrosine kinase Syk. PLD2 also participates in the sphingosine 1-phosphate-mediated pathway that stimulates the migration of endothelial cells, an important factor in angiogenesis. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction
GVPVTAKVENTERYTTGSKVHVCTLYTVRLTHGEFTWTVKKKFKHFQELHRDLYRHKVMLSFLPLGRFAI
QHRQQLEGLTEEMPSLPGTDREASRRTASKPKYLENYLNNLLENSFYRNYHAMMEFLAVS
>gnl|CDD|132831 cd07298, PX_RICS, The phosphoinositide binding Phox Homology domain of PX-RICS. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. RICS is a Rho GTPase-activating protein for cdc42 and Rac1. It is implicated in the regulation of postsynaptic signaling and neurite outgrowth. An N-terminal splicing variant of RICS containing additional PX and Src Homology 3 (SH3) domains, also called PX-RICS, is the main isoform expressed during neural development. PX-RICS is involved in neural functions including axon and dendrite extension, postnatal remodeling, and fine-tuning of neural circuits during early brain development. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of PX-RICS specifically binds phosphatidylinositol 3-phosphate (PI3P), PI4P, and PI5P
NVDFGSIQLSLGEEQNEVMRNGCESKELVYLVQIACQGRSWIVKRSYEDFRVLDKHLHLCIYDRRFSQLP
ELPRSDSLKDSPESVTQMLMAYLSRLSAIAGNKINCGPALTWMEI
>gnl|CDD|132832 cd07299, PX_TCGAP, The phosphoinositide binding Phox Homology domain of Tc10/Cdc42 GTPase-activating protein. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. TCGAP (Tc10/Cdc42 GTPase-activating protein) contains N-terminal PX and Src Homology 3 (SH3) domains, a central Rho GAP domain, and C-terminal proline-rich regions. It is widely expressed in the brain where it is involved in regulating the outgrowth of axons and dendrites and is regulated by the protein tyrosine kinase Fyn. It interacts with cdc42 and TC10beta through its GAP domain and with phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P2] through its PX domain. It is translocated to the plasma membrane in adipocytes in response to insulin and may be involved in the regulation of insulin-stimulated glucose transport. TCGAP has also been named sorting nexins 26 (SNX26). SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. It is unknown whether TCGAP also functions as a SNX
NVDFGSIQLQLSNERSDWTSSSEKDLVFLVQVTCQGRSWMVLRSYEDFRTLDAHLHRCIFDRRFSQLLEL
PPLCEIGDRLQILTPLLSEYLNRLTGIVDSNLNCGPVLTWMEI
>gnl|CDD|132833 cd07300, PX_SNX20, The phosphoinositide binding Phox Homology domain of Sorting Nexin 20. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. The PX domain of SNX20 binds PIs and targets the SNX20/PSGL-1 complex to endosomes. SNX20 may function in the sorting and cycling of PSGL-1 into endosomes
LLFEIPSARIIEQTISKHVVYQIIVIQTGSFDCNKVVIERRYSDFLKLHQELLSDFSEELEDVVFPKKKL
TGNFSEEIIAERRVALRDYLTLLYSLRFVRRSQAFQDFLTHPEL
>gnl|CDD|132834 cd07301, PX_SNX21, The phosphoinositide binding Phox Homology domain of Sorting Nexin 21. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development
LLFEVTDANVVQDAHSKYVLYTIYVIQTGQYDPSPAYISRRYSDFERLHRRLRRLFGGEMAGVSFPRKRL
RKNFTAETIAKRSRAFEQFLCHLHSLPELRASPAFLEFFYLR
>gnl|CDD|143636 cd07302, CHD, cyclase homology domain. Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide
EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAER
AVRAALEMQEALAELNAEREGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQI
LVSEATYELLGDAGFEFEELGEVELKGKSGPVRVYRL
>gnl|CDD|132765 cd07303, Porin3, Eukaryotic porin family that forms channels in the mitochondrial outer membrane. The porin family 3 contains two sub-families that play vital roles in the mitochondrial outer membrane, a translocase for unfolded pre-proteins (Tom40) and the voltage-dependent anion channel (VDAC) that regulates the flux of mostly anionic metabolites through the outer mitochondrial membrane
TYAELGKSARDLFTKGYGGGIKLDVKTKSELEFTSSGSANTETIESTTKVGGSLETKYRWSPYGLTFTEK
WNTDNTLGLEITVEDQLSRGLKSTFDSSFSPNTGKKNAKIKTGYKRINLGCDVDFDIAGPLIRGALVLGY
EGWLAGYQMVFETVSRVTQSNFAVGYKTDYNEFQAHTNVNDGTEFGGSIYHKVNDKLEVGVNLAATAGNS
NTRFGIAAKYQVDPDACFSASVNNSSLVGLGYTQTLKPGIKLTLSALLDHKAGGHKLGLGLEFQ
>gnl|CDD|143612 cd07304, Chorismate_synthase, Chorismase synthase, the enzyme catalyzing the final step of the shikimate pathway. Chorismate synthase (CS; 5-enolpyruvylshikimate-3-phosphate phospholyase; 1-carboxyvinyl-3-phosphoshikimate phosphate-lyase; E.C. 4.2.3.5) catalyzes the seventh and final step in the shikimate pathway: the conversion of 5- enolpyruvylshikimate-3-phosphate (EPSP) to chorismate, a precursor for the biosynthesis of aromatic compounds. This process has an absolute requirement for reduced FMN as a co-factor which is thought to facilitate cleavage of C-O bonds by transiently donating an electron to the substrate, having no overall change its redox state. Depending on the capacity of these enzymes to regenerate the reduced form of FMN, chorismate synthases are divided into two classes: Enzymes, mostly from plants and eubacteria, that sequester CS from the cellular environment, are monofunctiona,l while those that can generate reduced FMN at the expense of NADPH, such as found in fungi and the ciliated protozoan Euglena gracilis, are bifunctional, having an additional NADPH:FMN oxidoreductase activity. Recently, bifunctionality of the Mycobacterium tuberculosis enzyme (MtCS) was determined by measurements of both chorismate synthase and NADH:FMN oxidoreductase activities. Since shikimate pathway enzymes are present in bacteria, fungi and apicomplexan parasites (such as Toxoplasma gondii, Plasmodium falciparum, and Cryptosporidium parvum) but absent in mammals, they are potentially attractive targets for the development of new therapy against infectious diseases such as tuberculosis (TB)
FRVTTFGESHGPALGVVIDGCPAGLPLDEEDIQKELDRRRPGQGRGTTPRIEKDEVEILSGVFEGKTTGT
PIALLIRNKDQRSWDYSMLKTLPRPGHADYTGFLKYGGFDDRRGGGRSSARETAARVAAGAVAKKLLKEF
GIEVVAHVKSIGGIEDEPFDLDEEELLEEAEESPVRCPDPEAEEKMKELIDEAKKEGDSVGGVVEVVATG
VPAGLGSPVFDKLDARLAQALMSIPAVKGVEIGSGFEAARMRGSEVNDEIYYDEGGIKTKTNNAGGILGG
ISNGEPIVFRVAFKPTPSIAKPQKTVDLTGEETELAVKGRHDPCAVPRAVPVVEAMVALVLADA
>gnl|CDD|132766 cd07305, Porin3_Tom40, Translocase of outer mitochondrial membrane 40 (Tom40). Tom40 forms a channel in the mitochondrial outer membrane with a pore about 1.5 to 2.5 nanometers wide. It functions as a transport channel for unfolded protein chains and forms a complex with Tom5, Tom6, Tom7, and Tom22. The primary receptors Tom20 and Tom70 recruit the unfolded precursor protein from the mitochondrial-import stimulating factor (MSF) or cytosolic Hsc70. The precursor passes through the Tom40 channel and through another channel in the inner membrane, formed by Tim23, to be finally translocated into the mitochondrial matrix. The process depends on a proton motive force across the inner membrane and requires a contact site where the outer and inner membranes come close. Tom40 is also involved in inserting outer membrane proteins into the membrane, most likely not via a lateral opening in the pore, but by transfering precursor proteins to an outer membrane sorting and assembly machinery
LPNPGTFEELHREVKEVFPLDFFDGFRLDVNKGLSPHFQVSHSLHLGSSSLTSSYQFGATYVGDKQYPFL
QGDIDNDGNLNARIIHQLGDRLRSKLQAQLQDSKFNMSQLELDYRGDDFTASLKLANPDILNETGIYVAS
YLQSVTPKLALGGELVYQRVPGNGISVLSYAARYTAGNWIASGQLGAQGGLHLSYYRKLSDKLQLGVELE
LNLRTRESTATLGYQYDFRQSRFRGSIDSNGKVSAVLEKRLPLPLSLLLSGELNHVKNDYKFGFGLTIG
>gnl|CDD|132767 cd07306, Porin3_VDAC, Voltage-dependent anion channel of the outer mitochondrial membrane. The voltage-dependent anion channel (VDAC) regulates the flux of mostly anionic metabolites through the outer mitochondrial membrane, which is highly permeable to small molecules. VDAC is the most abundant protein in the outer membrane, and membrane potentials can toggle VDAC between open or high-conducting and closed or low-conducting forms. VDAC binds to and is regulated in part by hexokinase, an interaction that renders mitochondria less susceptible to pro-apoptotic signals, most likely by intefering with VDAC's capability to respond to Bcl-2 family proteins. While VDAC appears to play a key role in mitochondrially induced cell death, a proposed involvement in forming the mitochondrial permeability transition pore, which is characteristic for damaged mitochondria and apoptosis, has been challenged by more recent studies
PPTYFDIGKSAKDLLTKGYNFGAWKLDVKTKTPNGVEFTSTGSKKPDTGKVSGSLEAKYKIKGLTLTQKW
NTDNVLLTEITIEDLLAPGLKLTLDTTFPPNTGKKSGKLKAGYKHDPININADVDLNKGPLVGASAVLGY
KGFLLGAEVVYDTAKSKFTKYNFALGYTNGDFELSLKLNNGKTLRGSYFHKVSPRLAVGAKVTWYSGTNE
TTFAVGGQYALDPDALVKAKVNNDGQLGLSYQHKLRPGVTLTLSAGFDAKNLNQGGHKFGLSLSLK
>gnl|CDD|153271 cd07307, BAR, The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively
KLDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSNTDLGEALEKFGKIQKELEEFR
DQLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDSSKLAEAEEELQEA
KEKYEELREELIEDLNKLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY
>gnl|CDD|173892 cd07308, lectin_leg-like, legume-like lectins: ERGIC-53, ERGL, VIP36, VIPL, EMP46, and EMP47. The legume-like (leg-like) lectins are eukaryotic intracellular sugar transport proteins with a carbohydrate recognition domain similar to that of the legume lectins. This domain binds high-mannose-type oligosaccharides for transport from the endoplasmic reticulum to the Golgi complex. These leg-like lectins include ERGIC-53, ERGL, VIP36, VIPL, EMP46, EMP47, and the UIP5 (ULP1-interacting protein 5) precursor protein. Leg-like lectins have different intracellular distributions and dynamics in the endoplasmic reticulum-Golgi system of the secretory pathway and interact with N-glycans of glycoproteins in a calcium-dependent manner, suggesting a role in glycoprotein sorting and trafficking. L-type lectins have a dome-shaped beta-barrel carbohydrate recognition domain with a curved seven-stranded beta-sheet referred to as the "front face" and a flat six-stranded beta-sheet referred to as the "back face". This domain homodimerizes so that adjacent back sheets form a contiguous 12-stranded sheet and homotetramers occur by a back-to-back association of these homodimers. Though L-type lectins exhibit both sequence and structural similarity to one another, their carbohydrate binding specificities differ widely
FISEHSLSPPFLDDNDGEIGNWTVGGSTVITKNYIRLTPDVPSQSGSLWSRVPIPAKDFEIEVEFSIHGG
SGLGGDGFAFWYTEEPGSDGPLFGGPDKFKGLAIFFDTYDNDGKGFPSISVFLNDGTKSYDYETDGEKLE
LASCSLKFRNSNAPTTLRISYLNNTLKVDITYSEGNNWKECFTVEDVILPSQGYFGFSAQTGDLSDNHDI
LSVHTYEL
>gnl|CDD|213985 cd07309, PHP, Polymerase and Histidinol Phosphatase domain. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. PHP in polymerases has trinuclear zinc/magnesium dependent proofreading activity. It has also been shown that the PHP domain functions in DNA repair. The PHP structures have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel
VDLHTHTVFSDGDHAKLTELVDKAKELGPDALAITDHGNLRGLAEFNTAGKXNHIKAAEAAGIKIIIGSE
VNLTVLAHPVVATSDSHY
>gnl|CDD|143583 cd07311, terB_like_1, tellurium resistance terB-like protein, subgroup 1. This family includes several uncharacterized bacterial proteins. The prototype of this CD is tellurite resistance protein from Nostoc punctiforme that belongs to COG3793. Its precise biological function and its mechanism responsible for tellurium resistance still remains rather poorly understood
ALGASWIFQQTWGFDQIPTNQDKLAYLKALLVCAKGDGVISPEERDWAIGYAAARGGDADMVEELKEYTA
DEDLEEVDFRSPNIKSSRRALLYDAIQVCAADGELSPGEVAAVRKAASLLGISEDEVQKLEEIYFQEASL
RQKRLALLYP
>gnl|CDD|143584 cd07313, terB_like_2, tellurium resistance terB-like protein, subgroup 2. This family includes several uncharacterized bacterial proteins. Protein sequence homology analysis shows they are similar to tellurium resistance protein terB, but the function of this family is unknown
AAAALLVEVARADGEYDEEERAAIDRLLAERFGLDAEEAAELLAEAEALEEEAPDLYEFTSLIKEHFDYE
ERLELVEALWEVAYADGELDEYEEHLIRRVADLL
>gnl|CDD|143585 cd07316, terB_like_DjlA, N-terminal tellurium resistance protein terB-like domain of heat shock DnaJ-like proteins. Tellurium resistance terB-like domain of the DnaJ-like DjlA proteins. This family represents the terB-like domain of DjlA-like proteins, a subgroup of heat shock DnaJ-like proteins. Escherichia coli DjlA is a type III membrane protein with a small N-terminal transmembrane region and DnaJ-like domain on the extreme C-terminus. Overproduction has been shown to activate the RcsC pathway, which regulates the production of the capsular exopolysaccharide colanic acid. The specific function of this domain is unknown
ALFALMGKLAKADGRVSEAEIQAARALMDQMGLDAEARREAIRLFNEGKESDFGLEEYARQFRRACGGRP
ELLLQLLEFLFQIAYADGELSEAERELLRRIARLLG
>gnl|CDD|153371 cd07320, Extradiol_Dioxygenase_3B_like, Subunit B of Class III Extradiol ring-cleavage dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site of the aromatic ring. Intradiol enzymes cleave the aromatic ring between two hydroxyl groups, whereas extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon. Extradiol dioxygenases can be further divided into three classes. Class I and II enzymes are evolutionary related and show sequence similarity, with the two-domain class II enzymes evolving from the class I enzyme through gene duplication. Class III enzymes are different in sequence and structure and usually have two subunits, designated A and B. This model represents the catalytic subunit B of extradiol dioxygenase class III enzymes. Enzymes belonging to this family include Protocatechuate 4,5-dioxygenase (LigAB), 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase (CarB), 4,5-DOPA Dioxygenase, 2,3-dihydroxyphenylpropionate 1,2-dioxygenase, and 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase (HPCD). There are also some family members that do not show the typical dioxygenase activity
LAIIIPHGPALYAAEDTGKTRNDYQPIEISKRIKEKRPDTIIVVSPHHLVIISATAITCAETFETADSGQ
WGRRPVYDVKGDPDLAWEIAEELIKEIPVTIVNEMDGLDHGTLVPLSYIFGDPWDFKVIPLSVGVLVPPF
AKLFEFGKAIRAAVEPSDLRVHVVASGDLSHQLQGDRPSSQSGYYPIAEEFDKYVIDNLEELDPVEFKNM
HQYLTISNATPCGFHPLLILLGALDGKERKDLFTVYGIPSSSTGYAAAIL
>gnl|CDD|153390 cd07321, Extradiol_Dioxygenase_3A_like, Subunit A of Class III extradiol dioxygenases. Extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. There are two major groups of dioxygenases according to the cleavage site of the aromatic ring. Intradiol enzymes cleave the aromatic ring between two hydroxyl groups, whereas extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon. Extradiol dioxygenases can be divided into three classes. Class I and II enzymes are evolutionary related and show sequence similarity, with the two domain class II enzymes evolving from the class I enzyme through gene duplication. Class III enzymes are different in sequence and structure and usually have two subunits, designated A and B, which form a tetramer composed of two copies of each subunit. This model represents subunit A of class III extradiol dioxygenase enzymes. The A subunit is the smaller, non-catalytic subunit. Enzymes that belong to this family include Protocatechuate 4,5-dioxygenase (LigAB) A subunit, 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase (CarB) A subunit, Gallate Dioxygenase and proteins of unknown function
SRYELEKLLEQLLVKPEVKERFKADPEAVLAEYGLTPEEKAALLARDVGALYVLGVNPMLLMHFAIRLGI
PSAEYSA
>gnl|CDD|143474 cd07322, PriL_PriS_Eukaryotic, Eukaryotic core primase: Large subunit, PriL. Primases synthesize the RNA primers required for DNA replication. Primases are grouped into two classes, bacteria/bacteriophage and archaeal/eukaryotic. The proteins in the two classes differ in structure and the replication apparatus components. Archaeal/eukaryotic core primase is a heterodimeric enzyme consisting of a small catalytic subunit (PriS) and a large subunit (PriL). In eukaryotic organisms, a heterotetrameric enzyme formed by DNA polymerase alpha, the B subunit and two primase subunits has primase activity. Although the catalytic activity resides within PriS, the PriL subunit is essential for primase function as disruption of the PriL gene in yeast is lethal. PriL is composed of two structural domains. Several functions have been proposed for PriL such as stabilization of the PriS, involvement in synthesis initiation, improvement of primase processivity, determination of product size and transfer of the products to DNA polymerase alpha
FYDTPPTGNISLEEFEEIAIDRLKLLREIEQLEEERRKDHISHFILRLAYCRSEELRRWFVRQETELFRY
RLELLSLEGLKQFLKSNGLDYQPVSDEEKEELREELLKSASSLKQIKIEATNFYKVPFEEVLDLVRKRRV
FLKKGFAYVPQDELVSLVLSKFRSRLSKALALTARSLPRLEEDDRLLPLLKSLSKSYTGKDYSKNGNGGG
LTLSSIDELSKKSFPLCMRQLHEALRKNHHLKHGGRLQLGLFLKGIGLSLEEALKFWRSEFTKKMDADKF
DKEYAYNIRHNYGKEGKRANYTPYSCSKIISQNPPGPGDCHGCPFRHFDSDSLKQLLQSYGLSDSDIEEI
IDLVKSGHYQLACTKYFELTHPGAESDTGINHPNQYFEES
>gnl|CDD|153396 cd07323, LAM, LA motif RNA-binding domain. This domain is found at the N-terminus of La RNA-binding proteins as well as in other related proteins. Typically, the domain co-occurs with an RNA-recognition motif (RRM), and together these domains function to bind primary transcripts of RNA polymerase III in the La autoantigen (Lupus La protein, LARP3, or Sjoegren syndrome type B antigen, SS-B). A variety of La-related proteins (LARPs or La ribonucleoproteins), with differing domain architecture, appear to function as RNA-binding proteins in eukaryotic cellular processes
LEKIKKQVEYYFSDENLCKDRFLRSLMDDDGWVPLSLLASFNRVKKLTTDVELILEALRDSSVVEVSEDG
TKVRR
>gnl|CDD|320683 cd07324, M48C_Oma1-like, Oma1 peptidase-like, integral membrane metallopeptidase. This family contains peptidase M48 subfamily C (also known as Oma1 peptidase or mitochondrial metalloendopeptidase OMA1), including similar peptidases containing tetratricopeptide (TPR) repeats, as well as uncharacterized proteins such as E. coli bepA (formerly yfgC), ycaL and loiP (formerly yggG), considered to be putative metallopeptidases. Oma1 peptidase is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Homologs of Oma1 are present in higher eukaryotes, eubacteria and archaebacteria, suggesting that Oma1 is the founding member of a conserved family of membrane-embedded metallopeptidases, all containing the zinc metalloprotease motif (HEXXH). M48 peptidases proteolytically remove the C-terminal three residues of farnesylated proteins
YLNRLGDRLAAASGRPDLPYRFFVVDDPSINAFALPGGYIFVTTGLLLLLESEDELAAVLAHEIGHVTLR
HIARQLERYSRDQEREADRLGLQLLARAGYDPRGMARFFERLARQEGLSGSRLPEFLSTHPLTAERIAAL
RA
>gnl|CDD|320684 cd07325, M48_Ste24p_like, M48 Ste24 endopeptidase-like, integral membrane metallopeptidase. This family contains peptidase M48 family Ste24p-like proteins that are as yet uncharacterized, but probably function as intracellular, membrane-associated zinc metalloproteases; they all contain the HEXXH Zn-binding motif, which is critical for Ste24p activity. They likely remove the C-terminal three residues of farnesylated proteins proteolytically and are possibly associated with the endoplasmic reticulum and golgi. Some members also contain ankyrin domains which occur in very diverse families of proteins and mediate protein-protein interactions
LGNSVRVTPRQFPELHALLVEACRILGLKKVPELYVYQSPVLNAFALGFEGRPFIVLNSGLVELLDDDEL
RFVIGHELGHIKSGHVLYRTLLLLLLLLGELIGILLLSSALPLALLAWSRAAEYSADRAGLLVCQDPEAA
IRALMKLAGGSKLLKDVNNIEYFLEEEAQADALDGFFKWLSELLSTHPFLVKRAAELLR
>gnl|CDD|320685 cd07326, M56_BlaR1_MecR1_like, Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase. This family contains peptidase M56, which includes zinc metalloprotease domain in MecR1 as well as BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain ?-lactam antibiotics in MRSA. Both, MecR1 and BlaR1, are transmembrane proteins that consist of four transmembrane helices, a cytoplasmic zinc protease domain, and the soluble C-terminal extracellular sensor domain, and are highly similar in sequence and function. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. All members contain the zinc metalloprotease motif (HEXXH). Homologs of this peptidase domain are also found in a number of other bacterial genome sequences, most of which are as yet uncharacterized
VRRLRRRRRLRRLLLLLLRELRARGGGGVRVVDHDAPLAFCLGGRRPRIVLSTGLLELLSPEELRAVLAH
ERAHLRRRDPLLLLLASALARALPFLPLLRRLAAAYRLLRELAADDAAARRVGPRALASALLKLARAGAP
AAPAGALAFAGAAVNEARIRRLLDP
>gnl|CDD|320686 cd07327, M48B_HtpX_like, HtpX-like membrane-bound metallopeptidase. This family contains peptidase M48 subfamily B, also known as HtpX, which consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX, an integral membrane (IM) metallopeptidase, is widespread in bacteria and archaea, and plays a central role in protein quality control by preventing the accumulation of misfolded proteins in the membrane. Its expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and eliminating them by collaborating with FtsH, a membrane-bound and ATP-dependent protease. HtpX contains the zinc binding motif (HEXXH), has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not. Mutation studies of HtpX-like M48 metalloprotease from Leptospira interrogans (LA4131) has been shown to result in altered expression of a subset of metal toxicity and stress response genes
QYWFSDKLVLRAMGAREVSEEEAPELHAIVERLARRAGLPKPRVAIVDTPMPNAFATGRNPKNAAVAVTT
GLLQLLNEDELEAVLAHELSHIKNRDVLVMTLASLSRYREFAADRGSAKLTGDPLALASALMKISGSMQR
IPKRDLRQVEASAFFIIPPLSGGSLAELFSTHPPTEKRIERLR
>gnl|CDD|320687 cd07328, M48_Ste24p_like, M48 Ste24 endopeptidase-like, integral membrane metallopeptidase. This family contains peptidase M48-like proteins that are as yet uncharacterized, but probably function as intracellular, membrane-associated zinc metalloproteases; they all contain the HEXXH Zn-binding motif, which is critical for Ste24p activity. They likely remove the C-terminal three residues of farnesylated proteins proteolytically and are possibly associated with the endoplasmic reticulum and golgi
ALLKALFPRLARPRGPLVVLTREEAPALFALVDELAAALGAPPPDEVVLTADVNASVTELGLLLGRRGLL
TLGLPLLAALSPEELRAVLAHELGHFANGDTRLGAWILSRRAEYEADRVAARVAGSAAAASALRKLAARR
PSSPDDTHPPLAERLAALGA
>gnl|CDD|320688 cd07329, M56_like, Peptidase M56-like, integral membrane metallopeptidase in bacteria. This family contains peptidase M56, which includes zinc metalloprotease domain in MecR1 as well as BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain beta-lactam antibiotics in MRSA. Both, MecR1 and BlaR1, are transmembrane proteins that consist of four transmembrane helices, a cytoplasmic zinc protease domain, and the soluble C-terminal extracellular sensor domain, and are highly similar in sequence and function. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. All members contain the zinc metalloprotease motif (HEXXH). Homologs of this peptidase domain are also found in a number of other bacterial genome sequences, most of which are as yet uncharacterized
DRLARQADVPPPRVYVVDSDVPNAFAVGRSRGPTVVVTTGLLDLLDDDELEAVLAHELAHLKRRDVLVLL
LFDPLLLLVVGLLLFLSLFIFELLGFFFQPLLFLAFFALLRLAELLADALAVARTSAARRARLTGLPAAL
ASALEKIEDASDRALEAGLVLPALAADASSLEKTDHPPLEERVERLLE
>gnl|CDD|320689 cd07330, M48A_Ste24p, Peptidase M48 CaaX prenyl protease type 1, an integral membrane, Zn-dependent protein. This family of M48 CaaX prenyl protease 1-like family includes a number of well characterized genes such as those found in Taenia solium metacestode (TsSte24p), Arabidopsis (AtSte24), yeast Ste24p and human (Hs Ste24p) as well as several uncharacterized genes such as YhfN, some of which also containing tetratricopeptide (TPR) repeats. All members of this family contain the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. They are thought to be intimately associated with the endoplasmic reticulum (ER), regardless of whether their genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. The gene ZmpSte24, also known as FACE-1 in humans, a member of this family, is involved in the post-translational processing of prelamin A to mature lamin A, a major component of the nuclear envelope. ZmpSte24 deficiency causes an accumulation of prelamin A leading to lipodystrophy and other disease phenotypes while mutations in the protein lead to diseases of lamin processing (laminopathies), such as premature aging disease progeria and metabolic disorders. Some of these mutations map to the peptide-binding site
YPILAALVFLLVFTGLMVLVELPFGWVARFRVEERFGYMRETRSLWSKRTVALLTVGLLVALPVSALLLP
FEEPGGGAWWLGEWLAWLFYLFWRWKLSPFYAQFWKRRSRPLANGELRERIESMMNREGFGCAEILKVEL
SGGSMIHANAYFPGSGKRRRVVVFADALVSLMTPDELLAVIAHELGHVKHHHHLFRLAASQAVSFIVCAL
FILIYPLRFLLNFFARRFEYQADAYAAKLAGADALISALVKLHRDNLTTLTPSRLYSLWHYSHPHAAMRV
AHLLR
>gnl|CDD|320690 cd07331, M48C_Oma1_like, Peptidase M48C, integral membrane endopeptidase. This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer
VRRVAARLIAAAGDDPPQSAGWDWEVHVIDSPEVNAFVLPGGKIFVFTGLLPVAKNDDELAAVLGHEIAH
ALARHSAERMSQQKLLQLLLLLLLAALGASLAGLALGLLGLGAQLGLLLPYSRKQELEADRIGLQLMAKA
GYDPRAAVTFWEKMAAAEGGGKPPEFLSTHPSSETRIEALEELLPEA
>gnl|CDD|320691 cd07332, M48C_Oma1_like, Peptidase M48C Ste24p, integral membrane endopeptidase. This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer
YRYGLPALAELAAPLLPPSVEEKLGEQTLELLDETLLEPSELPAERQAALQQLFARLLAALPLPYPYRLH
FRDSGIGANAFALPGGTIVVTDGLVELAESPEELAAVLAHEIGHVEHRHSLRQLIRSSGLSLLVSLLTGD
VSGLSDLLAGLPALLLSLSYSRDFEREADAFALELLKAAGISPEGLADFFERLEEEHGDGGSLPEWLSTH
PDTEERIEAIRE
>gnl|CDD|320692 cd07333, M48C_bepA_like, Peptidase M48C Ste24p bepA-like, integral membrane protein. This family contains peptidase M48C Ste24p protease bepA (formerly yfgC)-like proteins considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Several members of this family also contain tetratricopeptide (TPR) repeat motifs, which are involved in a variety of functions including protein-protein interactions. BepA has been shown to possess protease activity and is responsible for the degradation of incorrectly folded LptD, an essential outer-membrane protein (OMP) involved in OM transport and assembly of lipopolysaccharide. Overexpression of the bepA protease causes abnormal biofilm architecture
QEVELGKQFAQQIRQQLPLVEDPEVNEYVNRIGQRLAAVSPRPPFPYRFFVVNDDSINAFATPGGYIYVN
TGLILAADNEAELAGVLAHEIGHVVARHIAKQIEKSYSREDEREADQLGLQYLTKAGYDPRGMVSFFKKL
RRKEWFGGSSIPTYLSTHPAPAERIAYLEELIAS
>gnl|CDD|320693 cd07334, M48C_loiP_like, Peptidase M48C Ste24p loiP-like, integral membrane protein. This subfamily contains peptidase M48 Ste24p protease loiP (formerly yggG)-like family are mostly uncharacterized proteins that include E. coli loiP and ycaLG, considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. LoiP has been shown to be a metallopeptidase that cleaves its targets preferentially between Phe-Phe residues. It is upregulated when bacteria are subjected to media of low osmolarity, thus yggG was named LoiP (low osmolarity induced protease). Proper membrane localization of LoiP may depend on YfgC, another putative metalloprotease in this subfamily
AGAKAAKAATLSDEEVKALAAQSAAQMDAKNPVAPANSPYAKRLARLTKGLKSYDGLPLNFKVYLTPDVN
AFAMADGSVRVYSGLMDMMTDDELLGVIGHEIGHVKLGHSKKAMKTAYLTSAARKAAASASGTVGALSDS
QLGALAEKLINAQFSQKQESEADDYGYKFLKKNGYNPQAAVSALEKLAALSGGGKSSLFSSHPDPAKRAE
RIRAR
>gnl|CDD|320694 cd07335, M48B_HtpX_like, Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase. This family contains peptidase M48 subfamily B, also known as HtpX, which consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX, an integral membrane (IM) metallopeptidase, is widespread in bacteria and archaea, and plays a central role in protein quality control by preventing the accumulation of misfolded proteins in the membrane. Its expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and eliminating them by collaborating with FtsH, a membrane-bound and ATP-dependent protease. HtpX contains the zinc binding motif (HEXXH), has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not. Mutation studies of HtpX-like M48 metalloprotease from Leptospira interrogans (LA4131) has been shown to result in altered expression of a subset of metal toxicity and stress response genes
GFGGSFISLLLSKWMAKRAMGVKVIDNPSNEKERWLVETVAELARKAGIKMPEVGIYPSPDVNAFATGPS
RNNSLVAVSTGLLDNMSEDEVEAVLAHEISHIANGDMVTMTLLQGVVNTFVIFLSRIIALIIDSFLSGDE
NGSGIGYFLVVIVLEIVLGILASLVVMWFSRKREFRADAGGAKLTGKEKMIAALERLKQISERPESEDDV
AAAIKISRGSGFLRLFSTHPPLEERIAALE
>gnl|CDD|320695 cd07336, M48B_HtpX_like, Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase. This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not
LTALLLAIGYLIGGQSGMIIALLIALGMNFFSYWFSDKIVLRMYGARPVSEEEAPELYQIVEELARRAGL
PMPKVYIIPSPQPNAFATGRNPEHAAVAVTTGILRLLDKDELEGVLAHELAHIKNRDILISTIAATIAGA
ISMLANMAQWGAIFGGRGGRDRGGNPIGALLLAILAPIAATLIQLAISRSREYLADETGARISGNPLALA
SALEKLERGAQRHPPMEANPATAHLFIVNPLSGGGLAKLFSTHPPTEERIARLRAM
>gnl|CDD|320696 cd07337, M48B_HtpX_like, Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase. This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not
LLLVAILIGISPFGESILRALSGCRIRRGARKPTRRELEEINPELEDKARRLGPDPEKVKLFISDDEYPN
AFALGRNTICVTKGLLDLLDYEELKGILAHELGHLSHKDTDYLLLIFVLLLLAAIWTKLGTLLIFVWIRL
LVMFSSRKAEYRADAFAVKIGYGEGLRSALDQLREYEDAPKGFLAALYSTHPPTEKRIERLEE
>gnl|CDD|320697 cd07338, M48B_HtpX_like, Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase. This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not
IFALIINLIQWLISPYIINWVYRAREPPDPEYPWLQEIVEEVARRAGIKPPKVGIAEDPIPNAFAYGSPL
TGARVAVTRGLLDILNRDELEAVIGHELGHIKHRDVAIMTAIGLIPSIIYYIGRSLLFSGGSSGGRNGGG
ALLAVGIAAFAVYFLFQLLVLGFSRLREYYADAHSAKVTGNGRALQSALAKIAYGYLAEIFSTHPLPAKR
IQALEK
>gnl|CDD|320698 cd07339, M48B_HtpX_like, Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase. This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not
LLLLSPRVSPRLILRLYGARPLSPGDAPELYRLLQELARRAGLPRPPLLYYVPSRVLNAFAVGSRKDAAI
ALTDGLLRRLTLRELAGVLAHEVSHIRNGDLRVMGLADLISRLTSLLSLLGQLLLLLNLPLLLLGEVTIS
WLAILLLILAPTLSTLLQLALSRTREFDADLDAARLTGDPEGLASALAKLERYQGGWWERLLLPGRRVPE
PSLLRTHPPTEERIRRLLA
>gnl|CDD|320699 cd07340, M48B_Htpx_like, Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase. This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not
IYILISYFSGDKIVLAMSGAREITREDEPRLYNVVEELAIAAGLPMPKVYIIDDPAPNAFATGRNPEHAV
IAVTTGLLEKLNRDELEGVIAHELSHIKNYDIRLMTIAVVLVGIIALIADLALRSFFYGGGSRRRRRDGG
GGGALILLILGLVLIILAPIFAQLIQLAISRQREYLADASAVELTRNPEGLISALEKISGDSSPLKVANS
ATAHLNLYFPNPGKKSSFSSLFSTHPPIEERIKRLR
>gnl|CDD|320700 cd07341, M56_BlaR1_MecR1_like, Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase. This family contains peptidase M56, which includes zinc metalloprotease domain in MecR1 as well as BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain ?-lactam antibiotics in MRSA. Both, MecR1 and BlaR1, are transmembrane proteins that consist of four transmembrane helices, a cytoplasmic zinc protease domain, and the soluble C-terminal extracellular sensor domain, and are highly similar in sequence and function. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. All members contain the zinc metalloprotease motif (HEXXH). Homologs of this peptidase domain are also found in a number of other bacterial genome sequences, most of which are as yet uncharacterized
IWLAGALLLLLRLLRGLLRLRRLRRRAEPVPDSLLLELARRLGLRRSVRLSVSALVASPMVVGLFRPVIL
LPEGLLEGSPEELRAILLHELAHIRRRDLLVNLLQRLLEALFWFNPLVWLLSRRLRLERELACDEAVLAA
LGDKEDYAEALLRLAERRSQPPPALALALAGSKSLLKRRIKRILKKK
>gnl|CDD|320701 cd07342, M48C_Oma1_like, M48C peptidase, integral membrane endopeptidase. This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer
TIERGGAPRTVSVPPVPGCAYRVELGNSDGVNAYADGRRVQITSGMMDFAQDDDELALVVAHELAHNILG
HRDRLRANGVAGGLLDGFGGNAAYSREFEIEADYLGLYLMARAGYDIDGAADFWRRLGASHPVGIGRAAT
HPSTAERFAALEKAVAEI
>gnl|CDD|320702 cd07343, M48A_Zmpste24p_like, Peptidase M48 subfamily A, a type 1 CaaX endopeptidase. This family contains peptidase family M48 subfamily A which includes a number of well-characterized genes such as those found in humans (ZMPSTE24, also known as farnesylated protein-converting enzyme 1 or FACE-1 or Hs Ste24), Taenia solium metacestode (TsSte24p), Arabidopsis (AtSte24) and yeast (Ste24p). Ste24p contains the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. It is thought to be intimately associated with the endoplasmic reticulum (ER), regardless of whether its genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. Ste24p is involved in the post-translational processing of prelamin A to mature lamin A, a major component of the nuclear envelope. ZmpSte24 deficiency causes an accumulation of prelamin A leading to lipodystrophy and other disease phenotypes, while mutations in this gene or in that encoding its substrate, prelamin A, result in a series of human inherited diseases known as laminopathies, the most severe of which are Hutchinson Gilford progeria syndrome (HGPS) and restrictive dermopathy (RD) which arise due to unsuccessful maturation of prelamin A. Two forms of mandibuloacral dysplasia, a condition that causes a variety of abnormalities involving bone development, skin pigmentation, and fat distribution, are caused by mutations in two different genes; mutations in the LMNA gene, which normally provides instructions for making lamin A and lamin C, cause mandibuloacral dysplasia with A-type lipodystrophy (MAD-A), and mutations in the ZMPSTE24 gene cause mandibuloacral dysplasia with B-type lipodystrophy (MAD-B). Within cells, these genes are involved in maintaining the structure of the nucleus and may play a role in many cellular processes. Certain HIV protease inhibitors have been shown to inhibit the enzymatic activity of ZMPSTE24, but not enzymes involved in prelamin A processing
YIILLLLVLVYLFELYLSLRQLRHLKRKLPPPPELADVISQEEFEKAQAYSLDKSRFSIVSSLLSLLLLL
LLLLFGLLPLLDLLLRSLGGNEILQSLLFFLLLSLISTLLSLPFSLYSTFVIEEKFGFNKQTLGLFIKDL
LKSLLLSLVLGGPLLALLLWIIKKFGKYWWLYAWLFVVVFSLLLMFIYPTLIAPLFNKFTPLEDGELKTK
IEALAKRAGFPLKKVYVMDGSKRSTHSNAYFTGFGKNKRIVLFDTLLEQLTEDEILAVLAHELGHWKHGH
ILKGLILSQLLLFLGFYLFGLLLNNPSLYRAFGFFGPSDQPALIGFLLLLSPLSFLLSPLMNALSRKFEY
EADAFAVELGYGEALISALVKLSKDNLSNLTPDPLYSAFHYSHPPLLERIAALEK
>gnl|CDD|320703 cd07344, M48_yhfN_like, Peptidase M48 YhfN-like, a novel minigluzincin. M48 YhfN-like protease is considered as a CaaX prenyl protease 1 homolog, with most of the sequences in this family as yet uncharacterized. It contains the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. It is probably associated with the endoplasmic reticulum (ER), regardless of whether its genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. This novel family of related proteins consist of the soluble minimal scaffold similar to the catalytic domains of the integral-membrane metallopeptidase M48 and M56, thus called minigluzincins
AKELLPERVEKYAERLGVKPPKIRIRDMKTRWGSCSSKGNINLNWRLIKAPPEVIDYVVVHELAHLKHMN
HSPRFWALVERYMPDYKERRKWLKEN
>gnl|CDD|320704 cd07345, M48A_Ste24p-like, Peptidase M48 subfamily A-like, putative CaaX prenyl protease. This family contains peptidase family M48 subfamily A-like CaaX prenyl protease 1, most of which are uncharacterized. Some of these contain tetratricopeptide (TPR) repeats at the C-terminus. Proteins in this family contain the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. They are thought to be possibly associated with the endoplasmic reticulum (ER), regardless of whether their genes possess the conventional signal motif (KKXX) in the C-terminal. These proteins putatively remove the C-terminal three residues of farnesylated proteins proteolytically
LSVLALLLFAIDIYALDLKYYLSFIPLFGSSPTLLALLFLLLFLLLLLLVWYAAYPVYKKLFSGLESRRA
YVLSNLRFLLPILLPWLLLSLLQDLLSLLPLAILKNLLSSSLGLLGFLLLFLLLLLLFPPLLIRLIWGCK
PLPPGPLRDRLEAFCRRAGFKVADILVWPLFEGRVATAGVMGILPRFRYILITDALLDSLSPEELEAVLA
HEIGHVKKRHLLLYLLFFLGFILLLALLSLLLSLLLLLLLPLLILLLGSSAEILLTLLLALPLLLLLVLY
FRFVFGFFSRNFERQADLYALRALGSAEPLISALEKIAELSGNSRDKPSWHHFSIAQRIAFLEKCE
>gnl|CDD|349983 cd07346, ABC_6TM_exporters, Six-transmembrane helical domain of the ATP-binding cassette transporters. This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRV
VFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWK
LTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRD
LRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYN
QLQQALASLERI
>gnl|CDD|259818 cd07347, harmonin_N_like, N-terminal protein-binding module of harmonin and similar domains, also known as HHD (harmonin homology domain). This domain is found in harmonin, and similar proteins such as delphilin, and whirlin. These are postsynaptic density-95/discs-large/ZO-1 (PDZ) domain-containing scaffold proteins. Harmonin and whirlin are organizers of the Usher protein network of the inner ear and the retina, delphilin is found at the cerebellar parallel fiber-Purkinje cell synapses. This domain is also found in CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM). CCM2 along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signaling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours; the C-terminal domain of malcavernin represented here has also been refered to as the Karet domain. Harmonin contains a single copy of this domain at its N-terminus which binds specifically to a short internal peptide fragment of the cadherin 23 cytoplasmic domain (a component of the Usher protein network). Whirlin contains two copies of this domain; the first of these has been assayed for interaction with the cytoplasmic domain of cadherin 23 and no interaction could be detected
RRELARLFSEQADQLLTDQERAYVTQALSEYRKGRSVEALVADLFPVLDTPAKLSLLQGLRSLIPPKDQQ
RFDELVAQ
>gnl|CDD|132762 cd07348, NR_LBD_NGFI-B, The ligand binding domain of Nurr1, a member of conserved family of nuclear receptors. The ligand binding domain of Nerve growth factor-induced-B (NGFI-B): NGFI-B is a member of the nuclear#steroid receptor superfamily. NGFI-B is classified as an orphan receptor because no ligand has yet been identified. NGFI-B is an early immediate gene product of the embryo development that is rapidly produced in response to a variety of cellular signals including nerve growth factor. It is involved in T-cell-mediated apoptosis, as well as neuronal differentiation and function. NGFI-B regulates transcription by binding to a specific DNA target upstream of its target genes and regulating the rate of transcriptional initiation. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, NGFI-B has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD)
PVNLIASLVRAHIDSNPSSAKLDYSKFQESVSPLFEKEDASDIQQFYDLLSGSLEVIRKWAEKIPGFSDF
CKEDQELLLESAFVELFILRLAYRSNPEEGKLIFCNGVVLHRTQCVRGFGDWIDSILEFSQSLHRMNLDV
SAFSCLAALVIITDRHGLKEPKRVEELQNRLISCLKEHVSGSASEPQRPNCLSRLLGKLPELRTLCTQGL
QRIFYLKLEDLVPPPPIVDKIFMDTLPF
>gnl|CDD|132763 cd07349, NR_LBD_SHP, The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain. The ligand binding domain of the Small Heterodimer Partner (SHP): SHP is a member of the nuclear receptor superfamily. SHP has a ligand binding domain, but lacks the DNA binding domain, typical to almost all of the nuclear receptors. It functions as a transcriptional coregulator by directly interacting with other nuclear receptors through its AF-2 motif. The closest relative of SHP is DAX1 and they can form heterodimer. SHP is an orphan receptor, lacking an identified ligand
VPRPRQRCLCEQRRRVCLCTPHRTCREASDVLVKTVAFMRNLPSFWQLPPQDQLLLLQNCWGPLFLLGLA
QDRVTFEVAEAPVPSMLKKILLEGQSSSGGSGQPDRPQPSLAAVQWLQCCLNKFWSLDLSPKEYAYLKGT
ILFNPDVPGLTASSHVGHLQQEAQWALCEVLEPLHPQDQGRFARILLTASTLKSIPPSLITDLFFRPIIG
DADIAELLGDML
>gnl|CDD|132764 cd07350, NR_LBD_Dax1, The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain. The ligand binding domain of the DAX1 protein: DAX1 (dosage-sensitive sex reversal adrenal hypoplasia congenita critical region on chromosome X gene 1) is a nuclear receptor with a typical ligand binding domain, but lacks the DNA binding domain. DAX1 plays an important role in the normal development of several hormone-producing tissues. Duplications of the region of the X chromosome containing DAX1 cause dosage sensitive sex reversal. DAX1 acts as a global repressor of many nuclear receptors, including SF-1, LRH-1, ERR, ER, AR and PR. DAX1 can form homodimer and heterodimerizes with its alternatively spliced isoform DAX1A and other nuclear receptors such as SHP, ERalpha and SF-1
PRASGQGCSCGSQRRVTLKSPQVTCKAASAVLVKTLRFVKGVPCFQELPLDDQLVLVRSCWAPLLVLGLA
QDGVDFETVETSEPSMLQRILTTRPPPTSGAEPGEPQALPQMPQAEASHLPSAADIRAIKAFLAKCWSLD
ISTKEYAYLKGTVLFNPDLPGLQCVQYIQGLQWEAQQALNEHVRMIHRGDQARFAKLNIALSLLRAINAN
VIAELFFRPIIGTVNMDDMLLE
>gnl|CDD|259819 cd07353, harmonin_N, N-terminal protein-binding module of harmonin. Harmonin is a postsynaptic density-95/discs-large/ZO-1 (PDZ) domain-containing scaffold protein, which organizes the Usher protein network of the inner ear and the retina. Harmonin contains a single copy of this domain, which is found at the N-terminus of all three harmonin isoform classes (a, b and c), and which preceeds the first PDZ protein-binding domain, PDZ1. This harmonin_N domain binds specifically to a short internal peptide fragment of the cadherin 23 cytoplasmic domain; cadherin 23 is a component of the Usher protein network
ERKVAREFRHKVDLLIENEAEKDALYDALRQYHESMDIPQLIGDLKLVINEPSRLPLFEDIRPLIPLKHQ
VEYDQLTPK
>gnl|CDD|259820 cd07354, HN_L-delphilin-R1_like, first harmonin_N_like domain (repeat 1) of L-delphilin, and related domains. This subgroup contains the first of two harmonin_N_like domains of an alternatively spliced longer variant of mouse delphilin (L-delphilin, isoform 1), and related domains. Delphilin is a scaffold protein which binds the glutamate receptor delta-2 (GRID2) subunit and the monocarboxylate transporter 2 at the cerebellar parallel fiber-Purkinje cell synapses. The N-terminus of L-delphilin contains this harmonin_N_like domain preceded by a postsynaptic density-95/discs-large/ZO-1 (PDZ) protein-binding domain, PDZ1. L-delphilin, in common with the shorter C-terminal isoforms (S-delphilin/delphilin alpha and delphilin beta) has a second harmonin_N_like domain (not belonging to this subgroup) and a second PDZ domain, PDZ2. This first harmonin_N_like domain is a putative protein-binding module based on its sequence similarity to the N-terminal domain of harmonin
RVRKAREFLKKVNEILGDDPEKKERLVEALKQYAADRNVEMLAEALTDILTTEAHRKLLDEIRYFIPNKH
RARFDKLVSQ
>gnl|CDD|259821 cd07355, HN_L-delphilin-R2_like, second harmonin_N_like domain (repeat 2) of L-delphilin, and related domains. This subgroup contains the second of two harmonin_N_like domains of an alternatively spliced longer variant of mouse delphilin (L-delphilin), and related domains. Delphilin is a postsynaptic density-95/discs-large/ZO-1 (PDZ) domain-containing scaffold protein which binds the glutamate receptor delta-2 (GRID2) subunit and the monocarboxylate transporter 2 at the cerebellar parallel fiber-Purkinje cell synapses. This harmonin_N_like domain in L-delphilin follows the second PDZ protein-binding domain, PDZ2; it is also found in the shorter C-terminal isoforms (S-delphilin/delphilin alpha and delphilin beta). It is a putative protein-binding module based on its sequence similarity to the N-terminal domain of harmonin. The first harmonin_N_like domain of L-delphilin belongs to a different subgroup and is missing from S-delphilin
IRVQGRTFKQQLEHLLTSKERYQLCRALERYFQHRNIDTLIVDVYPVLDTPAKQTLWQFILQLLTYEEQE
YCQQKIALFL
>gnl|CDD|259822 cd07356, HN_L-whirlin_R1_like, first harmonin_N_like domain (repeat 1) of the long isoform of whirlin, and related domains. This subgroup contains the first of two harmonin_N_like domains of the long isoform of whirlin, and related domains. Whirlin is a postsynaptic density-95/discs-large/ZO-1 (PDZ) domain-containing scaffold protein which binds various components of the Usher protein network of the inner ear and the retina: erythrocyte protein p55, usherin, VlGR1, and myosin XVa. The long isoform of whirlin contains two harmonin_N_like domains, and three PDZ protein-binding domains, PDZ1-3. This first harmonin_N_like domain precedes PDZ1, and is a putative protein-binding module based on its sequence similarity to the N-terminal domain of harmonin. This first harmonin_N_like domain has been assayed for interaction with the cytoplasmic domain of cadherin 23 (a component of the Usher network and an interacting partner of the harmonin N-domain), however no interaction could be detected. The short whirlin isoform, derived from an alternative start ATG, lacks this first harmonin_N_like domain. The short isoform has in common with the long isoform, the second harmonin_N_like domain (designated repeat 2, not present in this subgroup), and PDZ3
LSANVRNLHVALTKLLSDAEREEFTHCLNCYHKNRNVYDLVQSLKVVLDSPEKRQLFPLLRLVIPRSDQA
LFDQYTSE
>gnl|CDD|259823 cd07357, HN_L-whirlin_R2_like, second harmonin_N_like domain (repeat 2) of the long isoform of whirlin, and related domains. This subgroup contains the second of two harmonin_N_like domains found in the long isoform of whirlin, and related domains. Whirlin is a postsynaptic density-95/discs-large/ZO-1 (PDZ) domain-containing scaffold protein which binds various components of the Usher protein network of the inner ear and the retina: erythrocyte protein p55, usherin, VlGR1, and myosin XVa. The long isoform of whirlin contains two harmonin_N_like domains, and three PDZ protein-binding domains, PDZ1-3. The short whirlin isoform, derived from an alternative start ATG, lacks the first harmonin_N_like domain but has in common with the long isoform, this second harmonin_N_like domain (designated repeat 2, included in this subgroup) and PDZ3. This second harmonin_N_like domain is a putative protein-binding module based on its sequence similarity to the N-terminal domain of harmonin
SSQTAALVEEKARSLLNRSERATLSYYLAEYSSGHLTVDAFVLALFELLNTPEKFSLLSEIRELVAPEDL
DRFDELVLRRE
>gnl|CDD|259824 cd07358, HN_PDZD7_like, harmonin_N_like domain, a protein-binding module of PDZ domain-containing protein 7 and related proteins. Human PDZD7 is a scaffolding protein which associates with the Usher Syndrome protein network, and localizes to the stereocilia Ankle-link. Usher syndrome is the leading cause of genetic deaf-blindness. PDZD7 has a role as in Usher syndrome type 2 (and not in USH1) in humans. Whirlin, Usherin and GRP98 are other USH2 proteins. The latter two form the ankle links and whirlin is thought to be a scaffold for protein interactions at these links. PDZD7, whirlin, and harmonin (an USH1 protein) have a similar domain composition. The domain represented here is a putative protein-binding module based on its sequence similarity to the N-terminal domain of harmonin. Cooperative effects of mutations in PDZD7 and Usherin, and in PDZD7 and GPR98, result in a digenic USH2 phenotype
SSDSLTRLEEMASRLLTSDEVSAILRHCRRYVEERDVEDLVRPLLAILDTPEKLLLLREIRSLIPPSDLG
RFDSMVSP
>gnl|CDD|153372 cd07359, PCA_45_Doxase_B_like, Subunit B of the Class III Extradiol dioxygenase, Protocatechuate 4,5-dioxygenase, and simlar enzymes. This subfamily of class III extradiol dioxygenases consists of a number of proteins with known enzymatic activities: Protocatechuate (PCA) 4,5-dioxygenase (LigAB), 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB), 3-O-Methylgallate Dioxygenase, 2-aminophenol 1,6-dioxygenase, as well as proteins without any known enzymatic activity. These proteins play essential roles in the degradation of aromatic compounds by catalyzing the incorporation of both atoms of molecular oxygen into their preferred substrates. As members of the Class III extradiol dioxygenase family, the enzymes use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. LigAB-like class III enzymes are usually composed of two subunits, designated A and B, which form a tetramer composed of two copies of each subunit. This model represents the catalytic subunit, B
KIVLGIGASHAPGLTGAADPGPDAVRAAVFAAFARIRDRLEAARPDVVVVVGNDHFTNFFLDNMPAFAIG
IADSYEGPDEGWLGIPRAPVPGDADLARHLLAGLVEDGFDVAFSYELRLDHGITVPLHFLDPDNDVPVVP
VLVNCVTPPLPSLRRCYALGRALRRAIESFPGDLRVAVLGTGGLSHWPGGPRHGEINEEFDREFLDLLER
GDLEALLKATTEETLEEAGNGGHEILNWIAAAGALGEAPGEVLYYEPVPEWNTGMGFAVLE
>gnl|CDD|153373 cd07361, MEMO_like, Memo (mediator of ErbB2-driven cell motility) is co-precipitated with the C terminus of ErbB2, a protein involved in cell motility. This subfamily is composed of Memo (mediator of ErbB2-driven cell motility) and similar proteins. Memo is a protein that is co-precipitated with the C terminus of ErbB2, a protein involved in cell motility. It is required for the ErbB2-driven cell mobility and is found in protein complexes with cofilin, ErbB2 and PLCgamma1. However, Memo is not homologous to any known signaling proteins, and its function in ErbB2 signaling is not known. Structural studies show that Memo binds directly to a specific ErbB2-derived phosphopeptide. Memo is homologous to class III nonheme iron-dependent extradiol dioxygenases, however, no metal binding or enzymatic activity can be detected for Memo. This subfamily also contains a few members containing a C-terminal AMMECR1-like domain. The AMMECR1 protein was proposed to be a regulatory factor that is potentially involved in the development of AMME contiguous gene deletion syndrome
PPAVAGSFYPADPEELRRQLEAFLAAAPGPPPKEPPKAIIVPHAGYVYSGPVAAHAYAALDPGKPKRVVI
LGPSHTGYGRGCALSSAGAWETPLGDVPVDRELVEELLKLGGFIVDDELAHEEEHSLEVQLPFLQYLLPD
FKIVPILVGDQSPEAAEALAEALSKYLLDPDTLIVISSDFSHYGPRESAERLDRKAIEAILALDPEGFYE
YLRETGNTACGRGPIAVLLEAAKELGALKAELLDYATSGDVSGDRDSVVGYASAAF
>gnl|CDD|153374 cd07362, HPCD_like, Class III extradiol dioxygenases with similarity to homoprotocatechuate 2,3-dioxygenase, which catalyzes the key ring cleavage step in the metabolism of homoprotocatechuate. This subfamily of class III extradiol dioxygenases consists of two types of proteins with known enzymatic activities; 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase (HPCD) and 2-amino-5-chlorophenol 1,6-dioxygenase. HPCD catalyzes the key ring cleavage step in the metabolism of homoprotocatechuate (hpca), a central intermediate in the bacterial degradation of aromatic compounds. The enzyme incorporates both atoms of molecular oxygen into hpca, resulting in aromatic ring-opening to yield the product alpha-hydroxy-delta-carboxymethyl cis-muconic semialdehyde. 2-amino-5-chlorophenol 1,6-dioxygenase catalyzes the oxidization and subsequent ring-opening of 2-amino-5-chlorophenol, which is an intermediate during p-chloronitrobenzene degradation. The enzyme is probably a heterotetramer composed of two alpha and two beta subunits. Alpha and beta subunits share significant sequence similarity and both belong to this family. Like all Class III extradiol dioxygenases, these enzymes use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon
ELAMLAPHVPSMCHEENPPENQGCLVGAIKGMKEIRKRIEELKPDVILVISCHWMSSSFHHFVDATPRHG
GLTAVECPDLISDVPYDYPGDPELGRLLVEEGQEAGLRVKAVNDPTYIWDYGTVVPLRYLNPNKDIPVVS
ISACWTAASLEESYTWGEVIGKALLESDKRVVFLASGSLSHNLVRGPEAEEGMNHYPSLAEQQMDRRFIQ
LLREGQFQEACNMLPQYARAAGVESGGRHLTVMLGVMQGWGKVAELHGYGPSSGTGNAVMTF
>gnl|CDD|153375 cd07363, 45_DOPA_Dioxygenase, The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine. This subfamily is composed of plant 4,5-DOPA Dioxygenase, the uncharacterized Escherichia coli protein Jw3007, and similar proteins. 4,5-DOPA Dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine (4,5-DOPA). The reaction results in the opening of the cyclic ring between carbons 4 and 5 and producing an unstable seco-DOPA that rearranges to betalamic acid. 4,5-DOPA Dioxygenase is a key enzyme in the biosynthetic pathway of the plant pigment betalain. Homologs of DODA are present not only in betalain-producing plants but also in bacteria and archaea. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon
PVLFISHGSPMLALEDNPATAFLRELGKELPKPKAILVISAHWETRGPTVTASARPETIYDFYGFPPELY
EIQYPAPGSPELAERVAELLKAAGIPARLDPERGLDHGAWVPLKLMYPDADIPVVQLSLPASLDPAEHYA
LGRALAPLRDEGVLIIGSGSSVHNLRALRWGGPAPPPPWALEFDDWLKDALTAGDLDALLDYWEKAPHAR
RAHPTEEHLLPLLVALGAAGGDEARRLHDSIEYGSLSMSSYRF
>gnl|CDD|153376 cd07364, PCA_45_Dioxygenase_B, Subunit B of the Class III extradiol dioxygenase, Protocatechuate 4,5-dioxygenase, which catalyzes the oxidization and subsequent ring-opening of protocatechuate. Protocatechuate 4,5-dioxygenase (LigAB) catalyzes the oxidization and subsequent ring-opening of protocatechuate (or 3,4-dihydroxybenzoic acid, PCA), an intermediate in the breakdown of lignin and other compounds. Protocatechuate 4,5-dioxygenase is an aromatic ring opening dioxygenase belonging to the class III extradiol enzyme family, a group of enyzmes that cleaves aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon using a non-heme Fe(II). LigAB is composed of two subunits, designated A and B, which form a tetramer composed of two copies of each subunit. The B subunit (LigB) is the catalytic subunit of LigAB
MARIIAGVGTSHVPAIGAAMDNGKTDEPYWKPLFKGYQPARDWIKKNKPDVAIIVYNDHASAFDLDIIPT
FAIGTAEEFQPADEGYGPRPVPDVQGHPDLAWHIAQSLILDDFDMTIVNEMDVDHGLTVPLSIMYGQPEA
WPCKVIPLCVNVVQYPQPTGKRCFALGKAIRRAVESYDEDLKVAIWGTGGMSHQLQGERAGLINKEFDNR
FLDKLISDPEGLAKMPHIEYLREAGSEGIELVMWLIMRGALDEQVRELHRFYHVPASNTAYGLLILE
>gnl|CDD|153377 cd07365, MhpB_like, Subunit B of the Class III Extradiol ring-cleavage dioxygenase, 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB), which catalyzes the oxidization and subsequent ring-opening of 2,3-dihydroxyphenylpropionate. 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB) catalyzes the oxidization and subsequent ring-opening of 2,3-dihydroxyphenylpropionate, yielding the product 2-hydroxy-6-oxo-nona-2,4-diene 1,9-dicarboxylate. It is an essential enzyme in the beta-phenylpropionic degradation pathway, in which beta-phenylpropionic is first hydrolyzed to produce 2,3-dihydroxyphenylpropionate. The enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. LigAB-like class III enzymes are usually composed of two subunits, designated A and B, which form a tetramer composed of two copies of each subunit. This model represents the catalytic subunit, B. MhpB is likely to be a tetramer
MTVALICMSHSPLLGFNDPAPEVVAEVDAAFAAARAFVAAFDPELVVLFAPDHYNGFFYDLMPPFCIGTA
ATAVGDYGTLAGPLNVPRDLAEDLARHVLDSGIDVAISHRMQVDHGFTQPLEELFGGLDRYPVIPIFVNS
VAPPLAPMRRARALGEAVGRFLAKLDKRVLFLGSGGLSHDPPVPQLATAPPEVAERLIAGRNPTPEARAA
RQQRVIAAAKAFAAGDSTLMPLNPEWDRAFLDLLASGDLAALDAMTNDEIAAQAGNSAHEVRTWVAAFAA
LAAAGRYRAESRYYRPIPEWIAGFGVMTAE
>gnl|CDD|153378 cd07366, 3MGA_Dioxygenase, Subunit B of the Class III Extradiol ring-cleavage dioxygenase, 3-O-Methylgallate Dioxygenase, which catalyzes the oxidization and subsequent ring-opening of 3-O-Methylgallate. 3-O-Methylgallate Dioxygenase catalyzes the oxidization and subsequent ring-opening of 3-O-Methylgallate (3MGA) between carbons 2 and 3. 3-O-Methylgallate Dioxygenase is a key enzyme in the syringate degradation pathway, in which the syringate is first converted to 3-O-Methylgallate by O-demethylase. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which uses a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. LigAB-like enzymes are usually composed of two subunits, designated A and B, which form a tetramer composed of two copies of each subunit. This model represents the catalytic subunit, B
AEIVAGMATSHGPMLVTPPEQWLHRLEDDRNPSYHWFRGRTWTYEELVAERGDENENQITPEEMAARYAR
CQAALDRLADFIRAARIDVAVIVGDDQKELFDEALLPAFAIYYGDTITNGPRTREQLDRMPPHEAAAGYA
PDEARTYPCHPELARHLIKHTVADGFDVAALDHLPDTVGIPHAFGFIYRRIMGDLVIPVVPVLINTFYPP
NQPSARRCFEFGRAVARAIRSWPGDARVGVIASGGLSHFVIDEEFDRRILDALRNRDAEFLSSLPEAHLQ
SGTSELKNWIAAAGALDDLGLKMTSVDYVPCYRTEAGTGTAMGFVAWR
>gnl|CDD|153379 cd07367, CarBb, CarBb is the B subunit of the Class III Extradiol ring-cleavage dioxygenase, 2-aminophenol 1,6-dioxygenase, which catalyzes the oxidization and subsequent ring-opening of 2-aminophenyl-2,3-diol. CarBb is the B subunit of 2-aminophenol 1,6-dioxygenase (CarB), which catalyzes the oxidization and subsequent ring-opening of 2-aminophenyl-2,3-diol. It is a key enzyme in the carbazole degradation pathway isolated from bacterial strains with carbazole degradation ability. The enzyme is a heterotetramer composed of two A and two B subunits. CarB belongs to the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. Although the enzyme was originally isolated as a meta-cleavage enzyme for 2'-aminobiphenyl-2,3-diol involved in carbazole degradation, it has also shown high specificity for 2,3-dihydroxybiphenyl
MAKIVGAAATSHILMSPKGVEDQAARVVQGMAEIGRRVRESRPDVLVVISSDHLFNINLSLQPPFVVGTA
DSYTPFGDMDIPRELFPGHREFARAFVRQAAEDGFDLAQAEELRPDHGVMVPLLFMGPKLDIPVVPLIVN
INTDPAPSPRRCWALGKVLAQYVEKRRPAGERVAVIAAGGLSHWLGVPRHGEVNEAFDRMFLDLLEGGNG
ERLAGMGNDEILDQAGNGGLEIVNWIMAAAAVEAQSGEKVYYEPMPQWMTGMGGMEFN
>gnl|CDD|153380 cd07368, PhnC_Bs_like, PhnC is a Class III Extradiol ring-cleavage dioxygenase involved in the polycyclic aromatic hydrocarbon (PAH) catabolic pathway. This subfamily is composed of Burkholderia sp. PhnC and similar poteins. PhnC is one of nine protein products encoded by the phn locus. These proteins are involved in the polycyclic aromatic hydrocarbon (PAH) catabolic pathway. PhnC is a member of the class III extradiol dioxygenase family, a group os enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. LigAB-like enzymes are usually composed of two subunits, designated A and B, which form a tetramer composed of two copies of each subunit. This model represents the catalytic subunit, B
MGKIVGGFMMPHDPVMFVTPTAPPAAQREICWHAYAICAERLAALQVTSVVVIGDDHYTLFGTYCLPMYL
IGTGDVDGPYDPLPGLPRAVIENNEPLAHHIMQHGLEYGIDWAVARSFTVDHAATIPIHLAVRPVRAKGK
GMRAIPVYLATGVDPFITSWRAHELGRVIGAAVEAWQGDERVAIIGSGGISHWVGTAEMGAVNEGFDREI
MKLVAQGDLAALIALSDEEILEDGGNGGMEIRNWACAMGALPAARGEVIAYEPVAEWVTGLGFMQLK
>gnl|CDD|153381 cd07369, PydA_Rs_like, PydA is a Class III Extradiol ring-cleavage dioxygenase required for the degradation of 3-hydroxy-4-pyridone (HP). This subfamily is composed of Rhizobium sp. PydA and similar proteins. PydA is required for the degradation of 3-hydroxy-4-pyridone (HP), an intermediate in the Leucaena toxin mimosine degradation pathway. It is a member of the class III extradiol dioxygenase family, a group of enzymes that use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. LigAB-like enzymes are usually composed of two subunits, designated A and B, which form a tetramer composed of two copies of each subunit. This model represents the catalytic subunit, B
MAKIVAAIGMSHAPGALGWPDAPSPDVRARTEEATLKLGRTLTAARPDVIIAFLDDHFENHFRTNMPTIA
IGVAESHSGPADQLMEALRVPKKHYFPGNPEVAEQLLRALVHDSFDCARMGEIEYGNNLLVPWKLMKPDL
DVSVIPIYTNVFSPPLMKYSRAYALGAAVRKAIEDLPDDLRVAFMATGGLSHWPPYWNPNQPETDPFLQR
MKEYQTYGKPVLEKDPNLFVDLAAYEIEMAKKNQWPLNSKHPLVNAAWDRKFLKAYCRGDSEWLKNLTYE
EVEEEGGHGGHEILNWVAVMGAMDGKKAKLLLYEPVLEWICGMAYVDYE
>gnl|CDD|153382 cd07370, HPCD, The Class III extradiol dioxygenase, homoprotocatechuate 2,3-dioxygenase, catalyzes the key ring cleavage step in the metabolism of homoprotocatechuate. 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase (HPCD) catalyzes the key ring cleavage step in the metabolism of homoprotocatechuate (hpca), a central intermediate in the bacterial degradation of aromatic compounds. The enzyme incorporates both atoms of molecular oxygen into hpca, resulting in aromatic ring-opening to yield alpha-hydroxy-delta-carboxymethyl cis-muconic semialdehyde. HPCD is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon
KIVLAAKITHVPTMMLSEQPGPNKGCRQAAIDGLKEIGRRARELGVDTIVVFDTHWLVNAGYHINANARF
SGLFTSNELPHFIADMPYDYAGDPELAHLIAEEATEHGVKTLAHEDPSLPLEYGTLVPMRFMNEDDHFKV
VSVAVWCTHDIEESRRLGEAIRRAIAASDRRVALLASGSLSHRFWPNRELEAHEDPFTISSPFNRQVDLR
VLELWKEGRHAEFLDMLPDYARRCAGEGGMHDTAMLFGALGWDDYDGKAEVVTEYFPSSGTGQVNVWFPV
>gnl|CDD|153383 cd07371, 2A5CPDO_AB, The alpha and beta subunits of the Class III extradiol dioxygenase, 2-amino-5-chlorophenol 1,6-dioxygenase, which catalyzes the oxidization and subsequent ring-opening of 2-amino-5-chlorophenol. This subfamily contains both alpha and beta subunits of 2-amino-5-chlorophenol 1,6-dioxygenase (2A5CPDO), which catalyzes the oxidization and subsequent ring-opening of 2-amino-5-chlorophenol, an intermediate during p-chloronitrobenzene degradation. 2A5CPDO is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. The active enzyme is probably a heterotetramer, composed of two alpha and two beta subunits. Alpha and beta subunits share significant sequence similarity and may have evolved by gene duplication
VSAFLVPGPPLPQLGENVPQWEPRSWAYERAGASLAASRPDVVLVYSTQWIAVLDHHWLTRPRSEGRHVD
ENWPEFGRLDYSINVDVELAEACVEEGRKAGLVTRMMRYPRFPIDTGTITALTLMRPGTDIPPVVISANN
LYLSGEETEGEMDLAGKATRDAGKRVAVLGSGGLSHSHFHEEIDPPKDHIESEEGDKWNRRMLELMEQGD
MSALFELLPQYIKEARADMGSKAFTWMLGAMGYPELAAEVHGYGTVYGSGNAVIEFNL
>gnl|CDD|153384 cd07372, 2A5CPDO_B, The beta subunit of the Class III extradiol dioxygenase, 2-amino-5-chlorophenol 1,6-dioxygenase, which catalyzes the oxidization and subsequent ring-opening of 2-amino-5-chlorophenol. 2-amino-5-chlorophenol 1,6-dioxygenase (2A5CPDO), catalyzes the oxidization and subsequent ring-opening of 2-amino-5-chlorophenol, which is an intermediate during p-chloronitrobenzene degradation. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. The active 2A5CPDO enzyme is probably a heterotetramer, composed of two alpha and two beta subunits. The alpha and beta subunits share significant sequence similarity and may have evolved by gene duplication. This model describes the beta subunit, which contains a putative metal binding site with two conserved histidines; these residues are equivalent to two out of three Fe(II) binding residues present in the catalytic subunit dioxygenase LigB. The alpha subunit does not contain these potential metal binding residues. The 2A5CPDO beta subunit may be the catalytic subunit of the enzyme
GEIISGFLAPHPPHLVYGENPPQNEPRSQGGWEQLRWAYERARESIEALKPDVLLVHSPHWITSVGHHFL
GVPELSGRSVDPIFPNLFRYDFSMNVDVELAEACCEEGRKAGLVTKMMRNPRFRVDYGTITTLHMIRPQW
DIPVVGISANNTPYYLNTKEGLGEMDVLGKATREAIRKTGRRAVLLASNTLSHWHFHEEPAPPEDMSKEH
PETYAGYQWDMRMIELMRQGRMKEVFRLLPQFIEEAFAEVKSGAFTWMHAAMQYPELAAELHGYGTVIGT
GNAVMEWNLVKAGL
>gnl|CDD|153385 cd07373, 2A5CPDO_A, The alpha subunit of the Class III extradiol dioxygenase, 2-amino-5-chlorophenol 1,6-dioxygenase, which catalyzes the oxidization and subsequent ring-opening of 2-amino-5-chlorophenol. 2-amino-5-chlorophenol 1,6-dioxygenase (2A5CPDO) catalyzes the oxidization and subsequent ring-opening of 2-amino-5-chlorophenol, which is an intermediate during p-chloronitrobenzene degradation. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. The active enzyme is probably a heterotetramer, composed of two alpha and two beta subunits. The alpha and beta subunits share significant sequence similarity and may have evolved by gene duplication. This model describes the alpha subunit, which does not contain a potential metal binding site and may not possess catalytic activity
MTIVSAFLVPGSPLPQLRPDVPSWGQFAAATRQAGKALAASRPDVVLVYSTQWFAVLDQQWLTRPRSEGV
HVDENWHEFGELPYDIRSDTALAEACVTACPEHGVHARGVDYDGFPIDTGTITACTLMGIGTEALPLVVA
SNNLYHSGEITEKLGAIAADAAKDQNKRVAVVGVGGLSGSLFREEIDPREDHIANEEDDKWNRRVLKLIE
AGDLPALREAMPVYAKAARVDMGFKHLHWILGALGGKFSGANVLGYGPSYGSGAAVVEFRL
>gnl|CDD|143620 cd07374, CYTH-like_Pase, CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases. CYTH-like superfamily enzymes hydrolyze triphosphate-containing substrates and require metal cations as cofactors. They have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB), and from thiamine triphosphatase. Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. Thiamine triphosphatase is a soluble cytosolic enzyme which converts thiamine triphosphate to thiamine diphosphate. This domain superfamily also contains RNA triphosphatases, membrane-associated polyphosphate polymerases, tripolyphosphatases, nucleoside triphosphatases, nucleoside tetraphosphatases and other proteins with unknown functions
EVERKFRVPDDAVLPLLLGVPGVLGVGEPETVQLRAIYFDTPDLRLARAGLRLRRRTGGADAGWHLKLPG
GISRRTEVRAPLGDAAAVAPLLLAAALVLAVTRGLPLRPVATIETTRTVYRLLDAGGVLAELDLDTVTAR
VLDGGGTQYWREVEVELPDGDEALLDALERRLTA
>gnl|CDD|153408 cd07375, Anticodon_Ia_like, Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains. This domain is found in a variety of class Ia aminoacyl tRNA synthetases, C-terminal to the catalytic core domain. It recognizes and specifically binds to the anticodon of the tRNA. Aminoacyl tRNA synthetases catalyze the transfer of cognate amino acids to the 3'-end of their tRNAs by specifically recognizing cognate from non-cognate amino acids. Members include valyl-, leucyl-, isoleucyl-, cysteinyl-, arginyl-, and methionyl-tRNA synthethases. This superfamily also includes a domain from MshC, an enzyme in the mycothiol biosynthetic pathway
EERLKQARAFLNRLYRLLSFFRKALGGTQPKWDNELLEEADRELLARLQEFIKRTTNALEALDPTTAVQE
LFKFTNELNWYLDELKPALQTEELREAVLAVLRAALVVLTKLLAPFT
>gnl|CDD|143511 cd07376, PLPDE_III_DSD_D-TA_like, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase. This family includes eukaryotic D-serine dehydratases (DSD), cryptic DSDs from bacteria, D-threonine aldolases (D-TA), low specificity D-TAs, and similar uncharacterized proteins. DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Members of this family are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on similarity to AR, it is possible members of this family also form dimers in solution
ALEANISRMAARARASGVRLRPHVKTHKSPELAQRQLAAGARGVTVATLAEAETFAEAGVKDILMAYPLV
GPAAIARLAGLLRQEAEFHVLVDSPEALAALAAFAAAHGVRLRVMLEVDVGGHRSGVRPEEAAALALADA
VQASPGLRLAGVMAYEGHIYGAGGAREGAQARDQAVAAVRAAAAAAERGLACPTVSGGGTPTYQLTAGDR
AVTELRAGSYVFMDTGFDTLGACAQRPAAFRVTTVISRPAPTGRAVLDAGWKASSADTAFIGGGAVLGRP
ELRAVLLSEEHEGRSEPLNTPDLDDLPIGDRVFLVPNHACETVALHDELYVVEGGRVAATWPVFG
>gnl|CDD|153418 cd07377, WHTH_GntR, Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators. This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences
PLYEQIADQLREAILSGELKPGDRLPSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTFVA
>gnl|CDD|277324 cd07378, MPP_ACP5, Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain. Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LRFLVLGDWGGKPNPYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSA
PSLQVPWYLVLGNHDHRGNVSAQIAYTQRPNSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTD
DEASGQPRGPPNKKLAETQLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDA
YLSGHDHNLQHIVDESGTYYVISGAGSKADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIR
FVDSDG
>gnl|CDD|277325 cd07379, MPP_239FB, Homo sapiens 239FB and related proteins, metallophosphatase domain. 239FB (Fetal brain protein 239) is thought to play a role in central nervous system development, but its specific role in unknown. 239FB is expressed predominantly in human fetal brain from a gene located in the chromosome 11p13 region associated with the mental retardation component of the WAGR (Wilms tumor, Aniridia, Genitourinary anomalies, Mental retardation) syndrome. Orthologous brp-like (brain protein 239-like) proteins have been identified in the invertebrate amphioxus group and in vertebrates. 239FB belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLDPEGTD
ILVTHGPPYGHLDLGSSGQRLGCEELLNTVQRVRPKLHVFGHIHEGYGIERVPDTDGETTFVNAS
>gnl|CDD|277326 cd07380, MPP_CWF19_N, Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain. CWF19 cell cycle control protein (also known as CWF19-like 1 (CWF19L1) in Homo sapiens), N-terminal metallophosphatase domain. CWF19 contains C-terminal domains similar to that found in the CwfJ cell cycle control protein. The metallophosphatase domain belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LVCGDVNGRLKALFEKVNTINKKNGPFDALLCVGDFFGDDESDEELEAYKDGSKKVPIPTYFLGGNNGGV
DILLTSEWPKGISKLSKSPFEPDLLISGSDLIAELAKKLKPRYHFAGLEGVFYEREPYRNDSVLEKAEHV
TRFIGLAPV
>gnl|CDD|277327 cd07381, MPP_CapA, CapA and related proteins, metallophosphatase domain. CapA is one of three membrane-associated enzymes in Bacillus anthracis that is required for synthesis of gamma-polyglutamic acid (PGA), a major component of the bacterial capsule. The YwtB and PgsA proteins of Bacillus subtilis are closely related to CapA and are also included in this alignment model. CapA belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LAFVGDVMLGRGVREPILRRYDYSPPFGDVKPLLRNADLAFGNLETPITTRGEEAPKKGFHFRAPPENAD
ALKAAGFDVVSLANNHALDYGEDGLRDTLEALDRAGIDHAGAGRNLAEAGRPAYLEVKGVRVAFLGYTTG
TNGGPEAADAAPGALVNDADEAAILADVAEAKKKADIVIVSLHWGGEYGYEPAPEQRQLARALIDAGADL
VVGHHPHVLQGIEVYKGRLIAYSLGNFVF
>gnl|CDD|277328 cd07382, MPP_DR1281, Deinococcus radiodurans DR1281 and related proteins, metallophosphatase domain. DR1281 is an uncharacterized Deinococcus radiodurans protein with a domain that belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
KILFIGDVVGEPGRNALKKHLPKLKKKYKIDFVIVNGENAAGGKGLTKKIYEELFEAGVDVITMGNHTWD
KKEIYDYLEKEPRILRPANYPPGTPGKGYVVVKLNGKKIAVVNLLGRVFMDPLDNPFRAADKLLEELKEE
TDIIFVDFHAEATSEKIALGFYLDGRVSAVVGTHTHVQTADERILPKGTAYITDVGMTGPYNSVIGVKPE
TAIKRFLTGLPDRFEVAEGDARLCGVIIEIDDETGKAVKIERIQI
>gnl|CDD|277329 cd07383, MPP_Dcr2, Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain. DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
GKFKILQFADLHFGEGEWTCWEGCEADLKTVEFIESVLDEEKPDLVVLTGDLITGENTADDNATSYLDKA
VSPLVERGIPWAATFGNHDGYDWIDPSQVEWFESTSAALKKKYGKNIPSLAFFHIPLPEYREVWNEKGKL
GGINREKVCCQKTNSGFFKALVKRGDVKAVFCGHDHGNDFCGRWKNGIWLCYGRHTGYGGYG
>gnl|CDD|277330 cd07384, MPP_Cdc1_like, Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain. Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. This group also contains Saccharomyces cerevisiae TED1 (Trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), which acts together with Emp24p and Erv25p in cargo exit from the ER, and human MPPE1. The human MPPE1 gene is a candidate susceptibility gene for bipolar disorder. These proteins belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LLIADPQILDETSYPPRPKPALRLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRILDSEEWKEY
LHRFQKIFFLKSPGSLGSIPVIFIPGNHDIGYGGEAVFPEKVDRFEKYFILLTHIPLYRLLDSIKPVLIL
SGHDHDYCEVVHKSSPGSVKEITVKSFSWRMG
>gnl|CDD|277331 cd07385, MPP_YkuE_C, Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain. YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVL
GNHDYYSGDVEVWIAALEKAGITVLRNESVELSRDGATIGLAGSGVDDIGGHGEDLEKALKGLDENDPVI
LLAHNPDAAEEAQRPGVDLVLSGHTHGGQIFPPNYGVLSKLGFPYDSGLYQIGGTTYLYVSRGLGTWGPP
IRLGCPPEITLITL
>gnl|CDD|277332 cd07386, MPP_DNA_pol_II_small_archeal_C, archeal DNA polymerase II, small subunit, C-terminal metallophosphatase domain. The small subunit of the archeal DNA polymerase II contains a C-terminal metallophosphatase domain. This domain is thought to be functionally active because the active site residues required for phosphoesterase activity in other members of this superfamily are intact. The archeal replicative DNA polymerases are thought to possess intrinsic phosphatase activity that hydrolyzes the pyrophosphate released during nucleotide polymerization. This domain belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
AVFISDVHVGSKTFLEDAFEKFVRWLNGEDDSASRVKYLIIAGDLVDGIGVYPGQEEELEILDIYEQYEE
AAEYLSDVPSHIKIIIIPGNHDAVRQAEPQPALPEEIRKLFYPGNVEFLSNPALVKIHGVDVLIYHGRSL
DDVVGLIPGLSYDKPGKAMEELLKRRHLAPIYGGRTPIAPEAEDYLVIDEVPDILHTGHVHVYGVGVYRG
VLLVNSGTWQSQTEFQKMVNINPTPGKVPVVDL
>gnl|CDD|277333 cd07387, MPP_PolD2_C, PolD2 (DNA polymerase delta, subunit 2), C-terminal domain. PolD2 (DNA polymerase delta, subunit 2) is an auxiliary subunit of the eukaryotic DNA polymerase delta (PolD) complex thought to play a regulatory role and to serve as a scaffold for PolD assembly by interacting simultaneously with all of the other three subunits. PolD2 is catalytically inactive and lacks the active site residues required for phosphoesterase activity in other members of this superfamily. PolD2 is also involved in the recruitment of several proteins regulating DNA metabolism, including p21, PDIP1, PDIP38, PDIP46, and WRN. Human PolD consists of four subunits: p125 (PolD1), p50 (PolD2), p66(PolD3), and p12(PolD4). PolD is one of three major replicases in eukaryotes. PolD also plays an essential role in translesion DNA synthesis, homologous recombination, and DNA repair. Within the PolD complex, PolD2 tightly associates with PolD3. PolD2 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
YIALVSGLGLGGDAESILSLQLLVDWLTGQLGDESEQLSASSIVRLIIAGNSLAKSEQGKDSQSKARYLT
KKSSAASVEAVKELDEFLSQLASSVPVDVMPGENDPANFMLPQQPLHRCMFPKSRSYSTLNLVTNPYEFS
VDGVRVLGTSGQNVSDILKYSSKESRLDALESTLRWRHIAPTAPDTLWCYPFTDRDPFILEECPHVYFAG
NQPKFGTKLVEGENGQRVLLVCVPSFSKTGSAVLVNLRTLECEPINF
>gnl|CDD|277334 cd07388, MPP_Tt1561, Thermus thermophilus Tt1561 and related proteins, metallophosphatase domain. This family includes bacterial proteins related to Tt1561 (also known as Aq1956 in Aquifex aeolicus), an uncharacterized Thermus thermophilus protein. The conserved domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets, and is thought to allow for productive metal coordination. However, the active site residues required for phosphoesterase activity in other members of this superfamily are poorly conserved in this functionally uncharacterized family
RRTVRYILATSNPKGDLEALEKFVKLAPDTGADAIALIGNLLPKAAKSRDYAAFFRILSEAHLPTAYVPG
PQDAPIWEYLREAANVELVHPEIRNVHETFTFWRGPYLVAGVGGEIADEGEPEEHEALRYPAWVAEYRLK
ALWELKDYPKIFLFHTPPYHKGLNEQGSHEVAHLIKTHNPLLVLVAGKGQKHELLGASWVVVPGDLSEGE
YSLLDLRARKLETG
>gnl|CDD|277335 cd07389, MPP_PhoD, Bacillus subtilis PhoD and related proteins, metallophosphatase domain. PhoD (also known as alkaline phosphatase D/APaseD in Bacillus subtilis) is a secreted phosphodiesterase encoded by phoD of the Pho regulon in Bacillus subtilis. PhoD homologs are found in prokaryotes, eukaryotes, and archaea. PhoD contains a twin arginine (RR) motif and is transported by the Tat (Twin-arginine translocation) translocation pathway machinery (TatAyCy). This family also includes the Fusarium oxysporum Fso1 protein. PhoD belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
RFAFGSCNGYSPGQFLAYRVIALSKRKPDVFLWLGDQIYEDGPKGLGPLPPHPGHEALTLEEYRERYRQY
KSDPDLQKLLASVPIVGIWDDHDIGDNDGDYPESPKFYARKAAARQAYLEFLPHPNPSPRRIKRGGIYRS
FIFGDLVKLILLDTRTYRVIASGIQILPNDLLEGESDDDLLDSWDGFPHERERLLDLIRLEKPKNVVFLS
GDVHLGEIGRLPSSPPGDGYVLVEVTSSGLTN
>gnl|CDD|277336 cd07390, MPP_AQ1575, Aquifex aeolicus AQ1575 and related proteins, metallophosphatase domain. This family includes bacterial and archeal proteins homologous to AQ1575, an uncharacterized Aquifex aeolicus protein. AQ1575 may play an accessory role in DNA repair, based on the close proximity of its gene to Holliday junction resolvasome genes. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
IYFTSDTHFGHPNVIRYTNRPFDNVEEMNKVIINNWNNTVGPDDIVYHLGDFALGTNKANEALEILSLLN
GHIHLIRGNHDKSLLMYRPLFFESVQQYVRIEHGGRRFYLSHYPYRGPDSPDFDGWLIHGHVHSNSPDEG
PFVYDPRQINVGVEAWDYRPVSLEEIEDLI
>gnl|CDD|277337 cd07391, MPP_PF1019, Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain. This family includes bacterial and archeal proteins homologous to PF1019, an uncharacterized Pyrococcus furiosus protein. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LVIADLHLGYEEELRRQGINLPRRQKERLLERLDRLLEELGPDRLVILGDLKHSFGRVSRQERREVPFFR
LLAKDVDVILIRGNHDGGLEEILSDVNVVVVEGYLLGGYLIFHGHKEPDPLDAKLVIMGHEHPAIKLRDG
VGASRKLPCFLRGEGEDGDVIVLPAFNPLTGGVDI
>gnl|CDD|277338 cd07392, MPP_PAE1087, Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain. PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
ILAISDVHGDVPKLKKIKLKAEEADAVIVAGDITHFGPGEEAIEALNLLLAIGAPVLAVPGNCDTPEVLG
ELNSAGLNIHGKVVEVGGYIFVGVGGSNPTPFNTPFEYSEEEIYSKLGLLNVKLPGRLILVTHAPPYGTA
VDRVSSGVHVGSKAIRKFIEEFQPLLCICGHIHESRGIDKIGNTLVVNPG
>gnl|CDD|277339 cd07393, MPP_DR1119, Deinococcus radiodurans DR1119 and related proteins, metallophosphatase domain. DR1119 is an uncharacterized Deinococcus radiodurans protein with a metallophosphatase domain. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
VFAIADLHLNLDKKTKDMTVFGDEWKNHISKLEENWNNVVSPEDIVLIPGDISWAMNLKEALKDLTWIND
LPGIKILLKGNHDYWWPSKSKARRALEEEFLALKFHKAYIDDKVVVGGTRLWDNPYNCWPIINKQLKEET
LKVEIDERCCQRELERLNFALKAMNELREDKIKILMLHHPPANEDGDINPIFKLILESRVDICLFGHIHT
VPRFYLINGLLGGIRFILVAADYLNFSP
>gnl|CDD|163637 cd07394, MPP_Vps29, Homo sapiens Vps29 and related proteins, metallophosphatase domain. Vps29 (vacuolar sorting protein 29), also known as vacuolar membrane protein Pep11, is a subunit of the retromer complex which is responsible for the retrieval of mannose-6-phosphate receptors (MPRs) from the endosomes for retrograde transport back to the Golgi. Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer complex assembly as well as a phosphatase with specificity for the cytoplasmic tail of the MPR. The retromer includes the following 5 subunits: Vps35, Vps26, Vps29, and a dimer of the sorting nexins Vps5 (Snx1), and Vps17 (Snx2). Vps29 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LVLVIGDLHIPHRAADLPAKFKKLLVPGKIQHVLCTGNLCSKETYDYLKTIAPDVHIVRGDFDENLNYPE
TKVITVGQFKIGLIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAFEHEGKFFINPGSATGAFSP
LDPNVIPSFVLMDIQGSTVVTYVYQLIDGEVKVEKIEY
>gnl|CDD|277340 cd07395, MPP_CSTP1, Homo sapiens CSTP1 and related proteins, metallophosphatase domain. CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
WKGPFYFIQGADPQLGLIKQNNIGNGGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFR
EQQVSDLKDVLSKLDPDIPLVCVCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDP
SKVPELASAQDQWLEEQLQIARESDAKHVVVFQHIPLFLEDPDEEDDYFNIPKSVRRELLDKFKKAGVKA
VFSGHYHRNAGGRYRDLEMVVTSAVGCQLGNDTSGLRVVVVTENKISHRYYSL
>gnl|CDD|277341 cd07396, MPP_Nbla03831, Homo sapiens Nbla03831 and related proteins, metallophosphatase domain. Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
FSFGIIADIQYADIDDGKNLGTRRRYYRNSLGVLERAVEEWNRESNLAFVVQLGDIIDGYNAKDRSKEAL
DAVLSILDRLKGPVHHVLGNHEFYNFPREYLNHLKTLNGEDAYYYSFSPGPGFRFLVLDFVKFNGGIGEE
QLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWNYEEVLAILESYPCVKACFSGHNHEGGYEQD
SHGVHHVTLEGVLETPPDSQAFGTAYVYEDHMVVR
>gnl|CDD|277342 cd07397, MPP_NostocDevT-like, Nostoc DevT and similar proteins, metallophosphatase domain. DevT (Alr4674) is a putative protein phosphatase from Nostoc PCC 7120 (Anabaena PCC 7120). DevT mutants form mature heterocysts, but they are unable to fix N(2) and must be supplied with a source of combined nitrogen in order to survive. Anabaena DevT shows homology to phosphatases of the PPP family and displays a Mn(2+)-dependent phosphatase activity. DevT is constitutively expressed in both vegetative cells and heterocysts, and is not regulated by NtcA. The heterocyst regulator HetR may exert a certain inhibition on the expression of devT. Under diazotrophic growth conditions, DevT protein accumulates specifically in mature heterocysts. The role that DevT plays in a late essential step of heterocyst differentiation is still unknown. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
VRIAIVGDVHGQWDAEDERALRLLQPDLVLFVGDFGNENVQLVRRIASLDLPKAVILGNHDAWYTATRWG
RCPYDRSKGDRVQQQLEILGDEHVGYGRLDFPSLKLSVVGGRPFSKGGGRWLSKRFLSAVYGVISLEESA
QRIADAAKAAPEDHPLIFLAHNGPSGLGSRPEDICGKDWKPPGGDHGDPDLAEAIAQVQAQGRRVPLVVF
GHMHHQLKRGNKGLRMMHVDDRTGTVYLNAAVVPR
>gnl|CDD|277343 cd07398, MPP_YbbF-LpxH, Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain. YbbF/LpxH is an Escherichia coli UDP-2,3-diacylglucosamine hydrolase thought to catalyze the fourth step of lipid A biosynthesis, in which a precursor UDP-2,3-diacylglucosamine is hydrolyzed to yield 2,3-diacylglucosamine 1-phosphate and UMP. YbbF belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LFISDLHLGLRGCRADRLLDFLLVEELDEADALYLLGDIFDLWIGDDSVVWPGAHRALARLLRLADRGTE
VIYVPGNHDFLLGRFFAEALGAILLPEPAEHLELDGKRLLVLHGDQLDTDDRAYQWLRKLGRNPYLQLLF
LNLPLNRRRRIAGLIRRSSAAYLKHKQKKALAIIDVFEEAVARLARHRGVDGVICGHTHRPAIHRLDGIL
YINLGDW
>gnl|CDD|277344 cd07399, MPP_YvnB, Bacillus subtilis YvnB and related proteins, metallophosphatase domain. YvnB (BSU35040) is an uncharacterized Bacillus subtilis protein with a metallophosphatase domain. This family includes bacterial and eukaryotic proteins similar to YvnB. YvnB belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
FTLVWLPDTQYYFELYPDILKAQTEWIVDERENKNIDFVFHTGDVTDHGVDKEWEVAAAAFNVLDDSGVP
YSVLAGNHDLVLALGWGPSDEVLAWANEVLKKHPDRPAILNTHEYMLSDDGRMPEGNIGERIWDELVKKN
PNVFMVLSGHYHPAGRTTLVGDGDAGRDVHQMLANYQGRPEGGQGYLRLLDFDVKKQKVDVKTYSPY
>gnl|CDD|277345 cd07400, MPP_1, Uncharacterized subfamily, metallophosphatase domain. Uncharacterized subfamily of the MPP superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
IAHISDLHFGEERKPEVLELNLLDEINALKPDLVVVTGDLTQRARPAEFEEAREFLDALEPEPVVVVPGN
HDAIVALHHPLLPPPDTGRERNVLLDAGDALKLLKELGVDLVLHGHKHVPAVWNLGLLNGIVVVNAGT
>gnl|CDD|277346 cd07401, MPP_TMEM62_N, Homo sapiens TMEM62, N-terminal metallophosphatase domain. TMEM62 (transmembrane protein 62) is an uncharacterized Homo sapiens transmembrane protein with an N-terminal metallophosphatase domain. TMEM62 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
WFVHLTDIHVSSFHDPNRIQDETFCSNFIDVIKPTLVLITGDLTDNKTGNKLPSYQYQEEWQWKYYNILK
ESSVINKEYLFDIRGNHDLFGIVSFDSQNNYYRKYSNTGRDHSHSFSSTTRFGNYSFIGFDPTIFPGPKR
PFNFFGSLDKKLLDRLEKELEKSKNSKYTIWFGHYPHSLIISPSAKSSSKTFKDLLKKYNVTAYLCGHLH
PLGGEPVHYAGHPIAIITNPKPSHLLAPPSNFNDKSTHIRVLSF
>gnl|CDD|277347 cd07402, MPP_GpdQ, Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain. GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPA
PVYWIPGNHDDRAAMREALPEPPYDDNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAE
APDRPTLIFLHHPPFPLGIPWMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPST
CHQFALDLDDFALDAEAPGPRNLLLHADGI
>gnl|CDD|277348 cd07403, MPP_TTHA0053, Thermus thermophilus TTHA0053 and related proteins, metallophosphatase domain. TTHA0053 is an uncharacterized Thermus thermophilus protein with a domain that belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LVISDQIHPHIYSPRIKENLPDVDLVLAAGDLPIAYLEFVATKLRVPVLFVPGNHGLDVLLTHAPPLGPS
AGEDFAHRGFRAFLLFIRLFRPRYLIHGHTHLLGANPERRHRTPGGTEVINAQGYALLAL
>gnl|CDD|277349 cd07404, MPP_MS158, Microscilla MS158 and related proteins, metallophosphatase domain. MS158 is an uncharacterized Microscilla protein with a metallophosphatase domain. Microscilla proteins MS152, and MS153 are also included in this family. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LQIASDLHLEVEQNLAKLKFFPKVPDADILILAGDIGRLTDAEAWDNFLDLQSFQFEPVYYVPGNHEFYG
GSLDITLDALRMAAQDLSNVHYLNNQEVVLDDVRILGCTLWSDFDPDGEDIVQRKLNDFRGATVVVTHHA
PSPRSTSDNYADGLPKNAAFHVDLKDLILAPPIDLWIHGHTHFNTDYSVGGTRVVSNQLGY
>gnl|CDD|277350 cd07405, MPP_UshA_N, Escherichia coli UshA and related proteins, N-terminal metallophosphatase domain. UshA is a bacterial periplasmic enzyme with UDP-sugar hydrolase and dinucleoside-polyphosphate hydrolase activities associated with its N-terminal metallophosphatase domain, and 5'-nucleotidase activity associated with its C-terminal domain. UshA has been studied in Escherichia coli where it is expressed from the ushA gene as an immature precursor and proteolytically cleaved to form a mature product upon export to the periplasm. UshA hydrolyzes many different nucleotides and nucleotide derivatives and has been shown to degrade external UDP-glucose to uridine, glucose 1-phosphate and phosphate for utilization by the cell. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
ITVLHTNDHHGHFWRNEYGEYGLAAQKTLVDGIRKEVAAEGGSVLLLSGGDINTGVPESDLQDAEPDFRG
MNLVGYDAMAIGNHEFDNPLTVLRQQEKWAKFPLLSANIYQKSTGERLFKPWALFKRQDLKIAVIGLTTD
DTAKIGNPEYFTDIEFRKPADEAKLVIQELQQTEKPDIIIAATHMGHYDNGEHGSNAPGDVEMARALPAG
SLAMIVGGHSQDPVCMAAENKKQVDYVPGTPCKPDQQNGIWIVQAHEWGKYVGRADFEFRNGEMKMVNYQ
LIPVNLK
>gnl|CDD|277351 cd07406, MPP_CG11883_N, Drosophila melanogaster CG11883 and related proteins, N-terminal metallophosphatase domain. CG11883 is an uncharacterized Drosophila melanogaster UshA-like protein with two domains, an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LTILHFNDVYEIAPQDNEPVGGAARFATLRKQFEAENPNPLVLFSGDVFNPSALSTATKGKHMVPVLNAL
GVDVACVGNHDFDFGLDQFQKLIEESNFPWLLSNVFDAETGGPLGNGKEHHIIERNGVKIGLLGLVEEEW
LETLTINPPNVEYRDYIETARELVVELREKGADVIIALTHMRLPNDIRLAQEVPEIDLILGGHDHEYYIE
EINGTLIVKSGTDFRNLSIIDLEVDTGGRKWKVNIRRVDITSSIEED
>gnl|CDD|277352 cd07407, MPP_YHR202W_N, Saccharomyces cerevisiae YHR202W and related proteins, N-terminal metallophosphatase domain. YHR202W is an uncharacterized Saccharomyces cerevisiae UshA-like protein with two domains, an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LPWGQINFLHTTDTHGWLGGHLRDPNYSADYGDFLSFVQHMREIADGKGVDLLLVDTGDLHDGTGLSDAS
DPPGSYTSPIFRMMPYDALTIGNHELYLAEVALLEYEGFVPSWGGRYLASNVDITDDSGLLVPFGSRYAI
FTTKHGVRVLAFGFLFDFKGNANNVTVTPVQDVVQQPWFQNAIKNEDVDLIIVLGHMPVRDPSEFKVLHD
AIRKIFPNTPIQFFGGHSHIRDFTQYDSSSTSLESGRYLETVGWVSFDGPKASDSVLNLSKPNASLSFSR
SYIDFN
>gnl|CDD|277353 cd07408, MPP_SA0022_N, Staphylococcus aureus SA0022 and related proteins, N-terminal metallophosphatase domain. SA0022 is an uncharacterized Staphylococcus aureus UshA-like protein with two putative domains, an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. SA0022 also contains a putative C-terminal cell wall anchor domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
ITILHTNDIHGRYAEEDDVIGMAKLATIKEEERNTILVDAGDAFQGLPISNMSKGEDAAELMNAVGYDAM
TVGNHEFDFGKDQLKKLSKSLNFPFLSSNIYVNGKRVFDASTIVDKNGIEYGVIGVTTPETKTKTHPKNV
EGVEFTDPITSVTEVVAELKGKGYKNYVIICHLGVDSTTQEEWRGDDLANALSNSPLAGKRVIVIDGHSH
TVFENGKQYGNVTYNQTGSYLNNIGKIKLNSDTNLVENIKISNKS
>gnl|CDD|277354 cd07409, MPP_CD73_N, CD73 ecto-5'-nucleotidase and related proteins, N-terminal metallophosphatase domain. CD73 is a mammalian ecto-5'-nucleotidase expressed in endothelial cells and lymphocytes that catalyzes the conversion of 5'-AMP to adenosine in the final step of a pathway that generates adenosine from ATP. This pathway also includes a CD39 nucleoside triphosphate dephosphorylase that mediates the dephosphorylation of ATP to ADP and then to 5'-AMP. These enzymes all have an N-terminal metallophosphatase domain and a C-terminal 5'nucleotidase domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LTILHTNDVHARFEETSPSGGKKCAAAKKCYGGVARVATKVKELRKEGPNVLFLNAGDQFQGTLWYTVYK
GNAVAEFMNLLGYDAMTLGNHEFDDGPEGLAPFLENLKFPVLSANIDASNEPLLAGLLKPSTILTVGGEK
IGVIGYTTPDTPTLSSPGKVKFLDEIEAIQEEAKKLKAQGVNKIIALGHSGYEVDKEIAKKVPGVDVIVG
GHSHTFLYTGPPPSKEKPVGPYPTVVKNPDGRKVLVVQAYAFGKYLGYLDVTFDAKGNVLSWEGNPILL
>gnl|CDD|277355 cd07410, MPP_CpdB_N, Escherichia coli CpdB and related proteins, N-terminal metallophosphatase domain. CpdB is a bacterial periplasmic protein with an N-terminal metallophosphatase domain and a C-terminal 3'-nucleotidase domain. This alignment model represents the N-terminal metallophosphatase domain, which has 2',3'-cyclic phosphodiesterase activity, hydrolyzing the 2',3'-cyclic phosphates of adenosine, guanosine, cytosine and uridine to yield nucleoside and phosphate. CpdB also hydrolyzes the chromogenic substrates p-nitrophenyl phosphate (PNPP), bis(PNPP) and p-nitrophenyl phosphorylcholine (NPPC). CpdB is thought to play a scavenging role during RNA hydrolysis by converting the non-transportable nucleotides produced by RNaseI to nucleosides which can easily enter a cell for use as a carbon source. This family also includes YfkN, a Bacillus subtilis nucleotide phosphoesterase with two copies of each of the metallophosphatase and 3'-nucleotidase domains. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LRILETSDLHGNVLPYDYAKDKPTLPFGLARTATLIKKARAENPNTVLVDNGDLIQGNPLAYYYATIKDG
PIHPLIAAMNALKYDAGVLGNHEFNYGLDYLDRAIKQAKFPVLSANIIDAKTGEPFLPPYVIKEREVGVK
IGILGLTTPQIPVWEKANLIGDLTFQDIVETAKKYVPELRAEGADVVVVLAHGGIEADLEQLTGENGAYD
LAKKVPGIDAIVTGHQHREFPGKVFNGTVNGVPVIEPGSRGNHLGVIDLTLEKTDGKWKVKDSKAELRPT
>gnl|CDD|277356 cd07411, MPP_SoxB_N, Thermus thermophilus SoxB and related proteins, N-terminal metallophosphatase domain. SoxB (sulfur oxidation protein B) is a periplasmic thiosulfohydrolase and an essential component of the sulfur oxidation pathway in archaea and bacteria. SoxB has a dinuclear manganese cluster and is thought to catalyze the release of sulfate from a protein-bound cysteine S-thiosulfonate. SoxB is expressed from the sox (sulfur oxidation) gene cluster, which encodes 15 other sox genes, and has two domains, an N-terminal metallophosphatase domain and a C-terminal 5'-nucleotidase domain. SoxB binds the SoxYZ complex and is thought to function as a sulfate-thiohydrolase. SoxB is closely related to the UshA, YchR, and CpdB proteins, all of which have the same two-domain architecture. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LTLLHITDTHAQLNPHYFREPSNNLGIGSVDFGALARVFGKAGGFAHIATLVDRLRAEVGGKTLLLDGGD
TWQGSGVALLTRGKAMVDIMNLLGVDAMVGHWEFTYGKDRVLELLELLDGPFLAQNIFDEETGDLLFPPY
RIKEVGGLKIGVIGQAFPYVPIANPPSFSPGWSFGIREEELQEHVVKLRRAEGVDAVVLLSHNGMPVDVA
LAERVEGIDVILSGHTHDRVPEPIRGGKTLVVAAGSHGKFVGRVDLKVRDGEIKSFRYELLPV
>gnl|CDD|277357 cd07412, MPP_YhcR_N, Bacillus subtilis YhcR endonuclease and related proteins, N-terminal metallophosphatase domain. YhcR is a Bacillus subtilis sugar-nonspecific endonuclease. It cleaves endonucleolytically to yield nucleotide 3'-monophosphate products, similar to Staphylococcus aureus micrococcal nuclease. YhcR appears to be located in the cell wall, and is thought to be a substrate for a Bacillus subtilis sortase. YhcR is the major calcium-activated nuclease of B. subtilis. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
VQILGINDFHGNLEPTGGAYIGVQGKKYSTAGGIAVLAAYLDEARDGTGNSIIVGAGDMVGASPANSALL
QDEPTVEALNKMGFEVGTLGNHEFDEGLAELLRIINGGCHPTEPTKACQYPYPGAGFPYIAANVVDKKTG
KPLLPPYLIKEIHGVPIAFIGAVTKSTPDIVSPENVEGLKFLDEAETINKYAPELKAKGVNAIVVLIHEG
GSQAPYFGTTACSALSGPIVDIVKKLDPAVDVVISGHTHQYYNCTVGGRLVTQADSYGKAYADVTLTIDP
TTHDIVNKSAENVVV
>gnl|CDD|277358 cd07413, MPP_PA3087, Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain. PA3087 is an uncharacterized protein from Pseudomonas aeruginosa with a metallophosphatase domain that belongs to the phosphoprotein phosphatase (PPP) family. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
YDLIGDVHGCAHTLDRLLDLLGYRLQGGVWRHPRRQALFVGDLIDRGPRIREVLHRVHAMVDAGEALCVM
GNHEFNALAWHTPAPPGSGRQYVREHSPKNARQHKATLDQFEGHDWRDFLGWFQTLPLFLDLGRFRVVHA
CWDERLLKGPEMRLPHGAELTDKDGYTRDFFRVKWWVPPVFVGHYWRRGTPAPIRPNLACLDYSAVKYGK
LAAYRWDGETRL
>gnl|CDD|277359 cd07414, MPP_PP1_PPKL, PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain. PP1 (protein phosphatase type 1) is a serine/threonine phosphatase that regulates many cellular processes including: cell-cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism, transcription and neuronal signaling, through its interaction with at least 180 known targeting proteins. PP1 occurs in all tissues and regulates many pathways, ranging from cell-cycle progression to carbohydrate metabolism. Also included here are the PPKL (PP1 and kelch-like) enzymes including the PPQ, PPZ1, and PPZ2 fungal phosphatases. These PPKLs have a large N-terminal kelch repeat in addition to a C-terminal phosphoesterase domain. The PPP (phosphoprotein phosphatase) family, to which PP1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
DIDSIIERLLEVRGSRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFE
YGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIK
LWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWG
ENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDE
TLMCSFQILKP
>gnl|CDD|277360 cd07415, MPP_PP2A_PP4_PP6, PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain. PP2A-like family of phosphoprotein phosphatases (PPP's) including PP4 and PP6. PP2A (Protein phosphatase 2A) is a critical regulator of many cellular activities. PP2A comprises about 1% of total cellular proteins. PP2A, together with protein phosphatase 1 (PP1), accounts for more than 90% of all serine/threonine phosphatase activities in most cells and tissues. The PP2A subunit in addition to having a catalytic domain homologous to PP1, has a unique C-terminal tail, containing a motif that is conserved in the catalytic subunits of all PP2A-like phosphatases including PP4 and PP6, and has an important role in PP2A regulation. The PP2A-like family of phosphatases all share a similar heterotrimeric architecture, that includes: a 65kDa scaffolding subunit (A), a 36kDa catalytic subunit (C), and one of 18 regulatory subunits (B). The PPP (phosphoprotein phosphatase) family, to which PP2A belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
DLDQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDT
NYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTD
LFDYLPLAALIDGQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGY
LFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQ
FEAAP
>gnl|CDD|277361 cd07416, MPP_PP2B, PP2B, metallophosphatase domain. PP2B (calcineurin) is a unique serine/threonine protein phosphatase in its regulation by a second messenger (calcium and calmodulin). PP2B is involved in many biological processes including immune responses, the second messenger cAMP pathway, sodium/potassium ion transport in the nephron, cell cycle progression in lower eukaryotes, cardiac hypertrophy, and memory formation. PP2B is highly conserved from yeast to humans, but is absent from plants. PP2B is a heterodimer consisting of a catalytic subunit (CnA) and a regulatory subunit (CnB); CnB contains four Ca2+ binding motifs referred to as EF hands. The PPP (phosphoprotein phosphatase) family, to which PP2B belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
PRVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPAN
TRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACME
AFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHFVH
NTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAA
VLKYENNVMNIRQFNCSPHPYWLPN
>gnl|CDD|277362 cd07417, MPP_PP5_C, PP5, C-terminal metallophosphatase domain. Serine/threonine protein phosphatase-5 (PP5) is a member of the PPP gene family of protein phosphatases that is highly conserved among eukaryotes and widely expressed in mammalian tissues. PP5 has a C-terminal phosphatase domain and an extended N-terminal TPR (tetratricopeptide repeat) domain containing three TPR motifs. The PPP (phosphoprotein phosphatase) family, to which PP5 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
YSGPKLEDGKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHG
QFYDLLNIFELNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGF
EGEVKAKYNEQMFNLFSEVFNWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPPDSGLMCELL
WSDPQPQPGRGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQM
GNKGAFIRFKGSDLKPKFTQFEAVPHPNVKPMAYAN
>gnl|CDD|163661 cd07418, MPP_PP7, PP7, metallophosphatase domain. PP7 is a plant phosphoprotein phosphatase that is highly expressed in a subset of stomata and thought to play an important role in sensory signaling. PP7 acts as a positive regulator of signaling downstream of cryptochrome blue light photoreceptors. PP7 also controls amplification of phytochrome signaling, and interacts with nucleotidediphosphate kinase 2 (NDPK2), a positive regulator of phytochrome signalling. In addition, PP7 interacts with heat shock transcription factor HSF and up-regulates protective heat shock proteins. PP7 may also play a role in salicylic acid-dependent defense signaling. The PPP (phosphoprotein phosphatase) family, to which PP7 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
WPDGGALTNEWVHELMSVFEWSSRNLPPSELPSVLPVNVFDSLVLTAHKILHREPNCVRIDVEDVCEVVV
VGDVHGQLHDVLFLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFC
TSMYGFEQEVLTKYGDKGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLFRSPSLPKRKKQKGKNRRVLL
LEPESESLKLGTLDDLMKARRSVLDPPGEGSNLIPGDVLWSDPSLTPGLSPNKQRGIGLLWGPDCTEEFL
EKNNLKLIIRSHEGPDAREKRPGLAGMNKGYTVDHDVESGKLITLFSAPDYPQFQATEERYNNKGAYIIL
QPPDFSDPQFHTFEAVKPRPKANPYYD
>gnl|CDD|277363 cd07419, MPP_Bsu1_C, Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase domain. Bsu1 encodes a nuclear serine-threonine protein phosphatase found in plants and protozoans. Bsu1 has a C-terminal phosphatase domain and an N-terminal Kelch-repeat domain. Bsu1 is preferentially expressed in elongating plant cells. It modulates the phosphorylation state of Bes1, a transcriptional regulator phosphorylated by the glycogen synthase kinase Bin2, as part of a steroid hormone signal transduction pathway. The PPP (phosphoprotein phosphatase) family, to which Bsu1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
IIAHLLKPRGWKPPVERRFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEY
GSPVTEEAGDIEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECI
ERLGEDIRDGDSVWQRINRLFNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEAGSPVVMDL
LWSDPTENDSVLGLRPNAIDPRGTGLIVKFGPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLF
SATNYCGTAGNAGAILVLGRDLVVVPKLIHP
>gnl|CDD|277364 cd07420, MPP_RdgC, Drosophila melanogaster RdgC and related proteins, metallophosphatase domain. RdgC (retinal degeneration C) is a vertebrate serine-threonine protein phosphatase that is required to prevent light-induced retinal degeneration. In addition to its catalytic domain, RdgC has two C-terminal EF hands. Homologs of RdgC include the human phosphatases protein phosphatase with EF hands 1 and -2 (PPEF-1 and -2). PPEF-1 transcripts are present at low levels in the retina, PPEF-2 transcripts and PPEF-2 protein are present at high levels in photoreceptors. The PPP (phosphoprotein phosphatase) family, to which RdgC belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIF
YKNGLPSPENPYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYK
DHGKKILRLLEDVFSWLPLATIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVSTKTEWQQVVDILWSDPK
ATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRG
AYVKLGPQLTPHFVQYQ
>gnl|CDD|163664 cd07421, MPP_Rhilphs, Rhilph phosphatases, metallophosphatase domain. Rhilphs (Rhizobiales/ Rhodobacterales/ Rhodospirillaceae-like phosphatases) are a phylogenetically distinct group of PPP (phosphoprotein phosphatases), found only in land plants. They are named for their close relationship to to PPP phosphatases from alpha-Proteobacteria, including Rhizobiales, Rhodobacterales and Rhodospirillaceae. The PPP (phosphoprotein phosphatase) family, to which the Rhilphs belong, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
PRVVICVGDIHGYISKLNNLWLNLQSALGPSDFASALVIFLGDYCDRGPETRKVIDFLISLPEKHPKQRH
VFLCGNHDFAFAAFLGVLPRPSDGSEFKSTWKEYEKNEEREGWYKGEGFENMHLQGRRWAGKMKVTFNTV
RGEPYKGSIYDARPTFESYGVPHGSSDLIKAVPEEHKKFLRNLVWVHEEDDVCIETEEGLKHCKLIAVHA
GLEKSNSVEEQLKLLRTKDTSIPKIAPLSGRKNVWNIPQELADKKTIVVSGHHGKLHIDGLRLIIDEGGG
FDDRPIAAIVLPSKEIIRDTDNFS
>gnl|CDD|277365 cd07422, MPP_ApaH, Escherichia coli ApaH and related proteins, metallophosphatase domain. ApaH (also known as symmetrically cleaving Ap4A hydrolase and bis(5'nucleosyl)-tetraphosphatase) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases that hydrolyzes the nucleotide-signaling molecule diadenosine tetraphosphate (Ap(4)A) into two ADP and also hydrolyzes Ap(5)A, Gp(4)G, and other extending compounds. Null mutations in apaH result in high intracellular levels of Ap(4)A which correlate with multiple phenotypes, including a decreased expression of catabolite-repressible genes, a reduction in the expression of flagellar operons, and an increased sensitivity to UV and heat. Ap4A hydrolase is important in responding to heat shock and oxidative stress via regulating the concentration of Ap4A in bacteria. Ap4A hydrolase is also thought to play a role in siderophore production, but the mechanism by which ApaH interacts with siderophore pathways in unknown. The PPP (phosphoprotein phosphatase) family, to which ApaH belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, and PrpA/PrpB. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
TYAIGDIQGCYDELQRLLEKINFDPAKDRLWLVGDLVNRGPDSLETLRFVKSLGDSAVVVLGNHDLHLLA
VAAGIKKLKKKDTLDEILEAPDRDELLDWLRHQPLLHRDDELGIVMVHAGIPPQWDIEKALALAREVEAV
LRGDNYRDFLANMYGNEPDRWSDDLEGIDRLRYIINAFTRMRFCTPDGRLDFKCKGSPEEAPAGLRPWFD
VPNRKTRDYTIVFGHWAALGGLTRPNNIIALDTGCVWGGKLTALRLE
>gnl|CDD|277366 cd07423, MPP_Prp_like, Bacillus subtilis PrpE and related proteins, metallophosphatase domain. PrpE (protein phosphatase E) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases and a key signal transduction pathway component controlling the expression of spore germination receptors GerA and GerK in Bacillus subtilis. PrpE is closely related to ApaH (also known symmetrical Ap(4)A hydrolase and bis(5'nucleosyl)-tetraphosphatase). PrpE has specificity for phosphotyrosine only, unlike the serine/threonine phosphatases to which it is related. The Bacilli members of this family are single domain proteins while the other members have N- and C-terminal domains in addition to this phosphatase domain. Pnkp is the end-healing and end-sealing component of an RNA repair system present in bacteria. It is composed of three catalytic modules: an N-terminal polynucleotide 5' kinase, a central 2',3' phosphatase, and a C-terminal ligase. Pnkp is a Mn(2+)-dependent phosphodiesterase-monoesterase that dephosphorylates 2',3'-cyclic phosphate RNA ends. An RNA binding site is suggested by a continuous tract of positive surface potential flanking the active site. The PPP (phosphoprotein phosphatase) family, to which PrpE belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
DIIGDVHGCYDELVELLEKLGYQKKEEGLYVHPEGRKLVFLGDLVDRGPDSIDVLRLVMNMVKAGKALYV
PGNHCNKLYRYLKGRNVQLAHGLETTVEELEALSKEERPEFRERFAEFLESLPSHLVLDGGRLVVAHAGI
KEEMIGRGSKRVRDFCLYGDTTGETDEDGLPVRRDWAKDYRGKALVVYGHTPVPEPRWLNNTINIDTGCV
FGGKLTALRYPEMELVSVPAKQPYA
>gnl|CDD|277367 cd07424, MPP_PrpA_PrpB, PrpA and PrpB, metallophosphatase domain. PrpA and PrpB are bacterial type I serine/threonine and tyrosine phosphatases thought to modulate the expression of proteins that protect the cell upon accumulation of misfolded proteins in the periplasm. The PPP (phosphoprotein phosphatase) family, to which PrpA and PrpB belong, is one of two known protein phosphatase families specific for serine and threonine. This family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
GRDFVVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVLELLKQPWFHAVQGNHEQMAID
ALRGGDDVMWRANGGGWFFDLPDEEAKVLLEKLHHLPIAIEVESRNGKVGIVHADYPFDEYSFGFVEKPE
DEEEALWSRDRLQKSQTQPVAGADAFIFGHTPVPEPLDLGNVYYIDTGGVFDGNLTLVKLQ
>gnl|CDD|277368 cd07425, MPP_Shelphs, Shewanella-like phosphatases, metallophosphatase domain. This family includes bacterial, eukaryotic, and archeal proteins orthologous to the Shewanella cold-active protein-tyrosine phosphatase, CAPTPase. CAPTPase is an uncharacterized protein that belongs to the Shelph (Shewanella-like phosphatase) family of PPP (phosphoprotein phosphatases). The PPP family is one of two known protein phosphatase families specific for serine and threonine. In addition to Shelps, the PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
VAIGDLHGDLDRLRTILKLAGVIDSNDRWIGGDTVVVQTGDILDRGDDEIEILKLLEKLKRQARKAGGKV
ILLLGNHELMNLCGDFRYVHPRGLNEFGGVAKRRYALLSDGGYIGRYLRTHPVVLVVNDILFVHGGLGPL
WSRGYSLETKNGACERSALDKALAKLGVKRMVVGHTPQEGGVVNTLCGGKLIRIDVGMSRGKYGGLPEV
>gnl|CDD|143631 cd07429, Cby_like, Chibby, a nuclear inhibitor of Wnt/beta-catenin mediated transcription, and similar proteins. Chibby(Cby) is a well-conserved nuclear protein that functions as part of the Wnt/beta-catenin signaling pathway. Specifically, Cby binds directly to beta-catenin by interacting with its central region, which harbors armadillo repeats. Cby-beta-catenin interactions may also involve 14-3-3 proteins. By competing with other binding partners of beta-catenin, the Tcf/Lef transcription factors, Cby inhibits transcriptional activation. Cby has been shown to play a role in adipocyte differentiation. The C-terminal region of Cby appears to contain an alpha-helical coiled-coil motif
MPLFGRKFSPKKTPPRKSASLSNLRLLDRSTRQAELGLDYGPIRLKLGGQELVFEDGRWISESGGSSGVS
GREVLRLKKKNQQLEEENNLLKLKIEVLLDMLAETTAE
>gnl|CDD|143632 cd07430, GH15_N, Glycoside hydrolase family 15, N-terminal domain. Members of this family are N-terminal domains uniquely found in bacterial and archaeal glucoamylases and glucodextranases. Glucoamylase (glucan 1,4-alpha-glucosidase; 4-alpha-D-glucan glucohydrolase; amyloglucosidase; exo-1,4-alpha-glucosidase; gamma-amylase; lysosomal alpha-glucosidase; EC 3.2.1.3) hydrolyzes beta-1,4-glucosidic linkages of starch, glycogen and malto-oligosaccharides, releasing beta-D-glucose from the non-reducing end. Glucodextranase (glucan 1,6-alpha-glucosidase; exo-1,6-alpha-glucosidase; EC 3.2.1.70) uses an inverting reaction mechanism to hydrolyze alpha-1,6-glucosidic linkages of dextran and related oligosaccharides, releasing beta-D-glucose from the non-reducing end. These N-terminal domains adopt a structure consisting of antiparallel beta-strands, divided into two beta-sheets, with one sheet wrapped by an extended polypeptide, which appears to stabilize the domain. The function of these domains in the enzymes is as yet unknown. However, it is suggested that domain N of bacterial GA is involved in folding and/or the thermostability of the A domain that forms an (alpha/alpha)6-barrel structure
PGAPGAPPTWTSAAKDGVGTAYEAVSRVWFTLAHGILTEVYYPRIDTPQIRDLQFLVTDGEGFVDEEKRD
TTSTVEYLDPGSLAYRLVNTDKQGRYRLEKEIFTDPDRDVLLMRVRFEALDGGGLRLYVLLAPHLGNTGS
GNTAWVVDHGGRTALVASRGSVALALKASIPFTRASVGYVGVSDGWQDLKRNGRMTWTYDSAGDGNVALT
GELPLGASTEFTLALGFGKTTAEAAATAAASLAAGFEAVLARYNEGWRAY
>gnl|CDD|213986 cd07431, PHP_PolIIIA, Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III. PolIIIAs that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that is responsible for the replication of the DNA duplex. The alpha subunit of DNA polymerase III core enzyme catalyzes the reaction for polymerizing both DNA strands. The PolIIIA PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination, and like other PHP structures, exhibits a distorted (beta/alpha) 7 barrel and coordinates up to 3 metals. Initially, it was proposed that PHP region might be involved in pyrophosphate hydrolysis, but such activity has not been found. It has been shown that the PHP domain of PolIIIA has a trinuclear metal complex and is capable of proofreading activity
AHLHVHSSYSLLDSAIRPEDLVARAKELGYSALALTDRNVLYGAVRFYKACKKAGIKPIIGLELTVEGDG
EPYPLLLLAKNNEGYQNLLRLSTAAMLGEEKDGVPYLDLEELAEAASGLLVVLLGPLLLLLAAEQGLPLV
ATNDVHYLNPEDAFAADVLTAFLAVANTVRIAKECAVEL
>gnl|CDD|213987 cd07432, PHP_HisPPase, Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce histidinol. HisPPase can be classified into two types: the bifunctional HisPPase found in proteobacteria that belongs to the DDDD superfamily and the monofunctional Bacillus subtilis type that is a member of the PHP family. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel
ADLHIHSVFSPDSDMTPEEIVERAIELGLDGIAITDHNTIDGAEEALKEAYKDGLLVIPGVEVTLVVLAH
PDRPSRYGLSDLILKPLIKNGDAIEVNNSRLRYGLNNLAAKRYAELGGLPITGGSDAHT
>gnl|CDD|213988 cd07433, PHP_PolIIIA_DnaE1, Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III DnaE1. PolIIIAs that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that are responsible for the replication of the DNA duplex. PolIIIA core enzyme catalyzes the reaction for polymerizing both DNA strands. dnaE1 is the longest compared to dnaE2 and dnaE3. A unique motif was also identified in dnaE1 and dnaE3 genes
SFVHLRVHSEYSLLDGAVRIKKLVKLAKEDGMPALAITDLSNLFGAVKFYKAASKAGIKPIIGADLNVAN
PDDADEPFRLTLLAQNEQGYKNLTELISRAYLEGQRNGGPHIKLEWLAEYSEGLIALSGGRDGDIGQLLL
EGNPDLAEALLQFLKKIFPDRFYLELQRHGRPEEEAYEHALIDLAYELGLPLVATNDVRFLKPEDFEAHE
ARVCIAEGRTLDDPRRPRRYSPQQYFKSAEEMAELFADLPEAIENTVEIAKRCNVRIELGKPFLPDF
>gnl|CDD|213989 cd07434, PHP_PolIIIA_DnaE2, Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III at DnaE2 gene. PolIIIA DnaE2 plays a role in SOS mutagenesis/translesion synthesis and has dominant effects in determining GC variability in the bacterial genome. PolIIIAs that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that are responsible for the replication of the DNA duplex. PolIIIA core enzyme catalyzes the reaction for polymerizing both DNA strands. PolC PHP is located in a different location compared to dnaE1, 2, and 3. dnaE1 is the longest compared to dnaE2 and dnaE3. A unique motif was also identified in dnaE1 and dnaE3 genes. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. PHP domains found in DnaEs of thermophilic origin exhibit 3'-5' exonuclease activity
YAELHCLSNFSFLRGASHPEELVARAAELGYRALAITDECSLAGVVRAHAAAKELGLKLIVGSELVLADG
TRLVLLARDRAGYGRLCRLITLGRRRAEKGEYRLTLADLLAHAEGLLLILLPPDRLPAAAALLAQLRWLA
RAFPGRLWLALELHLGGDDARRLARLAALAAALGLPLVATGDVLMHSPSRRPLQDVLTAIRLGTTVAEAG
RRLAANAERHLRSPAELARLFLYPPEALAETLEIAARCTFSLDELRYEYP
>gnl|CDD|213990 cd07435, PHP_PolIIIA_POLC, Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III at PolC gene. DNA polymerase III alphas (PolIIIAs) that contain a PHP domain have been classified into four basic groups based on phylogenetic and domain structural analyses: polC, dnaE1, dnaE2, and dnaE3. The PolC group is distinct from the other three and is clustered together. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that are responsible for the replication of the DNA duplex. The alpha subunit of DNA polymerase III core enzyme catalyzes the reaction for polymerizing both DNA strands. PolC PHP is located in different location compare to dnaE1, 2, and 3. The PHP domain has four conserved sequence motifs and and contains an invariant histidine that is involved in metal ion coordination.The PHP domain of PolC is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel. PHP domains found in dnaEs of thermophilic origin exhibit 3'-5' exonuclease activity. In contrast, PolC PHP lacks detectable nuclease activity
RVELHAHTKMSAMDGVTSVKELVKRAAEWGHKAIAITDHGVVQAFPEAYEAAKKNGIKVIYGVEAYLVDP
YHITILVKNQTGLKNLYKLVSLSHTKYFYRVPRIPKSELEKYREGLLIGSACENGELFEAALNKKSDEEL
EEIASFYDYIEIQPLDNYQFLIEKGLIKSEEELKEINKRIIKLGKKLNKPVVATGDVHYLDPEDKIYREI
LLAGQGGGDGRADEQPDLYFRTTDEMLDEFSYLGEEKAYEVVVTNTNKIADMIEDIKP
>gnl|CDD|213991 cd07436, PHP_PolX, Polymerase and Histidinol Phosphatase domain of bacterial polymerase X. The bacterial/archaeal X-family DNA polymerases (PolXs) have a PHP domain at their C-terminus. The bacterial/archaeal PolX core domain and PHP domain interact with each other and together are involved in metal dependent 3'-5' exonuclease activity. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. PolX is found in all kingdoms, however bacterial PolXs have a completely different domain structure from eukaryotic PolXs. Bacterial PolX has an extended conformation in contrast to the common closed 'right hand' conformation for DNA polymerases. This extended conformation is stabilized by the PHP domain. The PHP domain of PolX is structurally homologous to other members of the PHP family that has a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel
ELKDIRGDLHVHTTWSDGRNSIEEMAEAARALGYEYIAITDHSKSLRVANGLSEERLREQIEEIDALNEK
LPGIRILKGIEVDILPDGSLDYPDEVLAELDVVVASVHSGFNQSEEEMTERLLKAIENPHVDILGHPTGR
LLGRREGYEVDMERVIEAAAETGTALEINANPDRLDLDDRHARRAKEAGVKIAINTDAHSTDGLDNMRYG
VGTARRGWLEKEDVLNTLPLEELLKFL
>gnl|CDD|213992 cd07437, PHP_HisPPase_Ycdx_like, Polymerase and Histidinol Phosphatase domain of Ycdx like. PHP Ycdx-like is a stand alone PHP domain similar to Ycdx E. coli protein with an unknown physiological role. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. It has also been shown that the PHP domain functions in DNA repair. The PHP structures have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel. YcdX may be involved in swarming
ILADLHTHTIASGHAYSTIEEMARAAAEKGLKLLGITDHGPAMPGAPHPWYFGNLKVIPREIYGVRILRG
VEANIIDYDGNLDLPERVLKRLDYVIASLHEPCFAPGTKEENTRAYINAMENPYVDIIGHPGNPRYPIDY
EAVVKAAKEYNVLLEINNSSLSPSRKGSRENCREIAELCKKYGVPVIVGSDAHIAYDIGNFDEALELLEE
IGFPEELILNTSPERLLDFLKLR
>gnl|CDD|213993 cd07438, PHP_HisPPase_AMP, Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) AMP bound. The PHP domain of this HisPPase family has an unknown function. It has a second domain inserted in the middle that binds adenosine 5-monophosphate (AMP). The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to give histidinol. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to the other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel
IDLHTHSTASDGTLSPEELVELAKEAGLKVLAITDHDTVAGLEEALAAAKELGIELIPGVEISTEYEGRE
VHILGSPEEAIELIHAAGGVAVLAHPGLYKLSRKKLEELIEELKEAGLDGIEVYHPYHSPEDRERLLELA
KEYGLLVTGGSDFHG
>gnl|CDD|143633 cd07439, FANCE_c-term, Fanconi anemia complementation group E protein, C-terminal domain. Fanconi Anemia (FA) is an autosomal recessive disorder associated with increased susceptibility to various cancers, bone marrow failure, cardiac, renal, and limb malformations, and other characteristics. Cells are highly sensitive to DNA damaging agents. A multi-subunit protein complex, the FA core complex, is responsible for ubiquitination of the protein FANCD2 in response to DNA damage. This monoubiquitination results in a downstream effect on homology-directed DNA repair. FANCE is part of the FA core complex and its C-terminal domain, which is modeled here, has been shown to directly interact with FANCD2. The domain contains a five-fold repeat of a structural unit similar to ARM and HEAT repeats. FANCE appears conserved in metazoa and in plants
AELPSVIQEVLEDIKELLLQEGEWLPSSPDELQFLHSCSPSQMEVLCSQLQLSSLSDQTLLLLCSSLLPL
SPDLSLANAVVFTRHLLLPKLLSLNESASRALVAALASFAKRYPRPFCEALLRPLLQCPHPGPFQAELLC
RLVKECFEPDAVLLLLHQILISPNLVWTEETFTVIQALLNRKPPLSEESFSELVSKLQEQAEAFSKSLKF
AKLLLAVITKYGPQMSPAHKQSLSEALERNKTFLKKSILAALKR
>gnl|CDD|188659 cd07440, RGS, Regulator of G protein signaling (RGS) domain superfamily. The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. While inactive, G-alpha-subunits bind GDP, which is released and replaced by GTP upon agonist activation. GTP binding leads to dissociation of the alpha-subunit and the beta-gamma-dimer, allowing them to interact with effectors molecules and propagate signaling cascades associated with cellular growth, survival, migration, and invasion. Deactivation of the G-protein signaling controlled by the RGS domain accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, which results in the reassociation of the alpha-subunit with the beta-gamma-dimer and thereby inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins are also involved in apoptosis and cell proliferation, as well as modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play important roles in neuronal signals modulation. Some RGS proteins are principal elements needed for proper vision
LRDPYGLEYFRQFLKSEHCEENLEFWLAVEKFKKTTSSDEELKSKAKEIYDKYISKDAPKEINIPESIRE
EIEENLEEPYPDPDCFDEAQEHILNLLEKDSYPRFLKSDLYLK
>gnl|CDD|143550 cd07441, CRD_SFRP3, Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt antagonist. The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), which plays important roles in embryogenesis and postnatal development as an antagonist of Wnt proteins, key players in a number of fundamental cellular processes. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled proteins (Fz), thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. SFRP3 regulates Wnt signaling activity in bone development and homeostasis. It is also involved in the control of planar cell polarity
AASCEPVRIPMCKSMPWNMTKMPNHLHHSTQANAVLAIEQFEGLLGTQCSPDLLFFLCAMYAPICTIDFQ
HEPIKPCKSVCERARAGCEPVLIRYRHTWPESLACEELPVYDRGVCISPEAIVTAE
>gnl|CDD|143551 cd07442, CRD_SFRP4, Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist. The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 4 (SFRP4), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRDs domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs
QGAPCEAVRIPMCRHMPWNITRMPNHLHHSTQENAVLAIEQYEELVDTGCSPVLPFFLCAMYAPICTLEF
LYDPIKPCRSVCQRARDGCEPIMRRYNHSWPESLACDDLPVYDRGVCISPEAIVTDL
>gnl|CDD|143552 cd07443, CRD_SFRP1, Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt activity. The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related protein 1 (SFRP1), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRDs domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. SFRP1 is expressed in many tissues and is involved in the regulation of Wnt signaling in osteoblasts, leading to enhanced trabecular bone formation in adults; it has also been shown to control the growth of retinal ganglion cell axons and the elongation of the antero-posterior axis
YTKPPQCVDIPADLRLCHNVGYKKMVLPNLLDHETMAEVKQQASSWVPLLNKNCHKGTQVFLCSLFAPVC
LDRPVYPCRWLCEAVRDSCEPVMQFFGFYWPEMLKCDKFPEGEVCIAMTPPNAT
>gnl|CDD|143553 cd07444, CRD_SFRP5, Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt activity. The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 5 (SFRP5), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs
YSKQPQCVDIPADLPLCHNVGYKRMRLPNLLEHESMAEVKQQASSWVPLLAKRCHADTQVFLCSLFAPVC
LDRPIYPCRSLCEAVRDSCAPVMESYGFPWPEMLHCHKFPLDNDLCIAVQFGHLQAT
>gnl|CDD|143554 cd07445, CRD_corin_1, One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease . The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the first (N-terminal) CRD
NTSACMNITHSQCQMLPYHSTLKPSLLSVKNMEMEKFLKFFSYLHRLSCYQHIMLFGCSLALPECISDGD
DRHGLLPCRSFCEAAKEGCEPVLGMVNASWPDFLRCSQFRNNTETAVENRALCFSPQQER
>gnl|CDD|143555 cd07446, CRD_SFRP2, Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt activity. The cysteine-rich-domain (CRD) is an essential part of the secreted frizzled related protein 2 (SFRP2), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. As a Wnt antagonist, SFRP2 regulates Nkx2.2 expression in the ventral spinal cord and anteroposterior axis elongation. SFRP2 also has a Wnt-independent function as an enhancer of procollagen cleavage by the TLD proteinases. SFRP2 binds both procollagen and TLD, thus facilitating the enzymatic reaction by bringing together the proteinase and its substrate
KKSNCKPIPANMLLCHGIEYTNMRLPNLLGHETMKEVLQQAGSWIPLVQKQCHPDTKKFLCSLFAPVCLD
DLDEAIQPCRSLCEAVKDGCAPVMSAFGFPWPDMLDCTRFPLDNDLCIPPAGSDHLLP
>gnl|CDD|143556 cd07447, CRD_Carboxypeptidase_Z, Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family. The cysteine-rich-domain (CRD) is an essential part of carboxypeptidase Z, a member of the carboxypeptidase E family of metallocarboxypeptidases. This is a group of Zn-dependent enzymes implicated in the intra- and extracellular processing of proteins. Carboxypeptidase Z removes C-terminal basic amino acid residues from its substrates, particularly arginine. The CRD acts as a ligand-binding domain for Wnts involved in developmental processes. CPZ binds and may process Wnt-4, CPZ has also been found to enhance the induction of the homeobox gene Cdx1. During vertebrate embryogenesis, the CRD of CPZ upregulates Pax3, a Wnt reporter gene essential for patterning of somites and limb development
SATCTDLLLSYCSDVSYTQTTFPNLLGHRSREVTEAGAEYLLLSVLHGLLGGECNPDIRLLGCSVLAPRC
ENDKVIKPCRSTCEALRKRCSHAFDAIQMAWPYFLDCDRFFAGEQEGCYDPLEGLRGD
>gnl|CDD|143557 cd07448, CRD_FZ4, Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor. The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 4 (Fz4) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and the Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Frizzled 4 (Fz4) activates the Ca(2+)/calmodulin-dependent protein kinase II and protein kinase C of the Wnt/Ca(2+) signaling pathway during retinal angiogenesis. Mutations in Fz4 lead to familial exudative vitreoretinopathy (FEVR), a hereditary ocular disorder characterized by failure of the peripheral retinal vascularization. In addition, the interplay between Fz4 and norrin as a receptor-ligand pair plays an important role in vascular development in the retina and inner ear in a Wnt-independent manner
DRRCEPIRIEMCQGLGYNVTRMPNLVGHELQTDAELQLQTFTPLIQYGCSSQLKFFLCSVYVPMCTEKVP
VPIGPCRPLCLSVKKRCLPVLKEFGFPWPEALNCSKFPPQNNHNHMCMEGPGDEEV
>gnl|CDD|143558 cd07449, CRD_FZ3, Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor. The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 3 (Fz3) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz3 plays a vital role in the anterior-posterior guidance of commissural axons. Knockout mice without Fz3 show defects in fiber tracts in the rostral CNS
SLFSCEPITLRMCQDLPYNTTFMPNLLNHYDQQTAALAMEPFHPMVNLECSRDFRPFLCALYAPVCMEYG
RVTLPCRRLCQRAYSECSKLMEMFGVPWPEDMECSRFPDCDEPYPRLVDLSLSGEPT
>gnl|CDD|143559 cd07450, CRD_FZ6, Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor. The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 6 (Fz6) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Frizzled 6 (Fz6) is expressed in the skin and hair follicles and controls hair patterning in mammals using a Fz-dependent tissue polarity system, which is similar to the one that patterns the Drosophila cuticle
SLFTCEPITVPRCLKMPYNMTFFPNLMGHYDQDIAAVEMEPFLPLANLRCSPNVHTFLCQAFVPTCTEQI
HVVRPCRELCEKVYSDCKKLIDTFGISWPEELECDRLQYCDETVPDTADPHTEFSSP
>gnl|CDD|143560 cd07451, CRD_SMO, Cysteine-rich domain of the smoothened receptor (Smo) integral membrane protein. The cysteine-rich domain (CRD) is part of the smoothened receptor (Smo), an integral membrane protein and one of the key players in the Hedgehog (Hh) signaling pathway, critical for development, cell growth and migration, as well as stem cell maintenance. The CRD of Smo is conserved in vertebrates and can also be identified in invertebrates. The precise function of the CRD in Smo is unknown. Mutations in the Drosophila CRD disrupt Smo activity in vivo, while deletion of the CRD in mammalian cells does not seem to affect the activity of overexpressed Smo
RPAKCEPLKNTTCLGSKLPYTYTSLDLVPDSTTQEEVQEKLHLWSGLRNVPKCWAVIQPLLCALYMPKCE
NGKVELPSQEMCQATRGPCKIVENERGWPDFLRCDNDRFPPRGCKNDVRELKFNTSGQCESP
>gnl|CDD|143561 cd07452, CRD_sizzled, Cysteine-rich domain of the sizzled protein. The cysteine-rich domain (CRD) is an essential part of the sizzled protein, which regulates bone morphogenetic protein (Bmp) signaling by stabilizing chordin, and plays a critical role in the patterning of vertebrate and invertebrate embryos. Sizzled also functions in the ventral region as a Wnt inhibitor and modulates canonical Wnt signaling. Sizzled proteins belong to the secreted frizzled-related protein family (SFRP), and have be identified in the genomes of birds, fishes and frogs, but not mammals
FDIGLSTKCVPIPPEMSMCQDVGYSEMRLPNLLGHTSMAEVVPKSADWQTLLHTGCHPHARTFLCSLFAP
VCLDTFIQPCRSMCVAVRDSCAPVLACHGHSWPESLDCDRFPAGEDMCLASLSKEYQYFYKEFPKPACQS
C
>gnl|CDD|143562 cd07453, CRD_crescent, Cysteine-rich domain of the crescent protein. The cysteine-rich domain (CRD) is an essential part of the crescent protein, a member of the secreted frizzled-related protein (SFRP) family, which regulates convergent extension movements (CEMs) during gastrulation and neurulation. Xenopus laevis crescent efficiently forms inhibitory complexes with Wnt5a and Wnt11, but this effect is cancelled in the presence of another member of the SFRP family, Frzb1. A potential role for Crescent in head formation is to regulate a non-canonical Wnt pathway positively in the adjacent posterior mesoderm, and negatively in the overlying anterior neuroectoderm
SPCMRIPKSMALCYDIGYSEMRIPNLLEHETMAEVIQQSSSWLPLLARECHPDARIFLCSLFAPICWDRP
IYPCRSLCEAVRSSCAPLMACYGYPWPEILHCDKFPVDHDLCISPQFIDTLSPERVKPRASCEDC
>gnl|CDD|143563 cd07454, CRD_LIN_17, Cysteine-rich domain (CRD) of LIN_17. A cysteine-rich domain (CRD) is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. The protein lin-17 is involved in cell type specification during Caenorhabditis elegans vulval development
VKGKCIPIDIELCKDLPYNYTYFPNTILHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMCPIGM
PQAVTSCKSVCEQVKADCFSILEEFGIGWPEPLNCAQFPDPPELCMKPTEDEIT
>gnl|CDD|143564 cd07455, CRD_Collagen_XVIII, Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18). The cysteine-rich domain (CRD) is an essential part of the variant 3 of collagen XVIII (V3C18), which regulates major cellular functions such as the differential epithelial morphogenesis of early lung and kidney development. V3C18 is a 170 kD protein, which is proteolotically processed into the CRD-containing 50 kD glucoprotein precursor that binds Wnt3a through its CRD domain and suppresses the Wnt3a-induced stabilization of beta catenin. Full-length V3C18 is unable to inhibit Wnt signaling
PRPRCLPVPSSLPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGG
GPPPPPPPCRQFCEVLQDSCWNLLEGGRLPVACASLPEQEDGYCVLIGPPAEN
>gnl|CDD|143565 cd07456, CRD_FZ5_like, Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5. The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 5 (Fz5) and frizzled 8 (Fz8) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines
KCEEITIPMCKGIGYNMTYMPNQFNHDTQEEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDYDKP
LPPCRSVCERARDGCAPIMRQYGFAWPERMSCDALPEGGDPDNLCMDRNN
>gnl|CDD|143566 cd07457, CRD_FZ9_like, Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9. The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 9 (Fz9) and frizzled 10 (Fz10) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines
GKCERITIPMCQGIGYNMTRMPNLLGHESQSEAAISIHEFAPLVQYGCAEHLRFFLCSLYAPMCTEQVSI
PIPACRSMCEQARDKCSPIMEQFSFSWPDSLDCDRLPRKNDPKDLCMEAPN
>gnl|CDD|143567 cd07458, CRD_FZ1_like, Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1. The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 1 (Fz1), frizzled 2 (Fz2), and frizzled 7 (Fz7) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines
GKCEPITIPLCTDIPYNMTIFPNLLGHTKQEDAGLEVHQFYPLVKVQCSPDLKFFLCSVYAPVCTVLERP
IPPCRSLCESARQGCEALMNKFGFQWPESLDCEKFPVHGAGDLCVGENT
>gnl|CDD|143568 cd07459, CRD_TK_ROR_like, Cysteine-rich domain of tyrosine kinase-like orphan receptors. The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor (Ror) proteins, a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2
GYCQPYRGSVCAKYLGNKSVYVTSKQTQEDIEEQLSAAFTVISTSSDVSPKCQQYALPSLCYYAFPLCDE
GSSTPKPRRICRDECELLENDLCKKEYAIAKRHPLIGHQLLLPDCSSLPSPGSPESSNCIRLGIP
>gnl|CDD|143569 cd07460, CRD_FZ5, Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins. The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 5 (Fz5) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz5 plays critical regulating roles in the yolk sac and placental angiogenesis, in the maturation of the Paneth cell phenotype, in governing the neural potential of progenitors in the developing retina, and in neuronal survival in the parafascicular nucleus
KALVCQEITVPMCKGIGYNLTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLRFFLCSMYTPICLPDY
RKPLPPCRSVCERAKAGCSPLMRQYGFAWPERMNCDRLPVLGDPETLCMDYNRTEAT
>gnl|CDD|143570 cd07461, CRD_FZ8, Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor. The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 8 (Fz8) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Xenopus Fz8 is important in Wnt/beta-catenin signaling pathways controlling the transcriptional activation of target genes Siamois and Xnr3 in the animal caps of late blastula
KELQCQEITVPLCKGIGYNYTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDY
KKPLPPCRSVCERAKAGCAPLMRQYGFPWPDRMRCDLLPEQGNPDTLCMDYNRTD
>gnl|CDD|143571 cd07462, CRD_FZ10, Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor. The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 10 (Fz10) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. The cellular functon of Fz10 is unknown
GEGRCQPIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHSHLKFFLCSLYAPMCTEQV
STPIPACRVMCEQARLKCSPIMEQFNFKWPDSLDCSKLPNKNDPNYLCMEAPNNGTD
>gnl|CDD|143572 cd07463, CRD_FZ9, Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor. The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 9 (Fz9) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz9 may play a signaling role in lymphoid development and maturation, particularly at points where B cells undergo self-renewal prior to further differentiation
RAAKCQPVVIPMCRGIGYNLTRMPNFLGHDSQREAAIKLNEFAPLVEYGCHVHLRFFLCSLYAPMCTDQV
STSIPACRPMCEQARQKCSPIMEQFNFGWPESLDCSRLPTRNDPNALCMEAPENATA
>gnl|CDD|143573 cd07464, CRD_FZ2, Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor. The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 2 (Fz2) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz2 is involved in the Wnt/beta-catenin signaling pathway and in the activation of protein kinase C and calcium/calmodulin-dependent protein kinase (CaM kinase)
DHGFCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSLELRFFLCSMYAPVCTVLE
QAIPPCRSICERARQGCEALMNKFGFQWPERLRCENFPRHGAEQICVGQNHSEDGGP
>gnl|CDD|143574 cd07465, CRD_FZ1, Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor. The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 1 (Fz1) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata
DHGYCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLE
QALPPCRSLCERARQGCEALMNKFGFQWPDTLRCEKFPVHGAGELCVGQNTSESGTP
>gnl|CDD|143575 cd07466, CRD_FZ7, Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor. The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 7 (Fz7) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Xenopus Fz7 is important in Wnt/beta-catenin signaling pathways controlling the transcriptional activation of target genes Siamois and Xnr3 in the animal caps of late blastula
DHGFCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELKFFLCSMYAPVCTVLE
QAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDAS
>gnl|CDD|143576 cd07467, CRD_TK_ROR1, Cysteine-rich domain of tyrosine kinase-like orphan receptor 1. The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor 1 (Ror1), a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2
EDGFCQPYRGIACARFIGNRTIYMESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYC
DETSGMPKPRDLCRDECEILENVLCQTEYIFARSNPMILMRLKLPNCEDLAQPDSPEAANCIRIGIPMAD
PI
>gnl|CDD|143577 cd07468, CRD_TK_ROR2, Cysteine-rich domain of tyrosine kinase-like orphan receptor 2. The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor (Ror2), a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2
KDGFCQPYRGIACARFIGNRTIYVDSLQMQGEIENRITAAFTMIGTSTHLSDQCSQFAIPSFCHFVFPLC
DDRSRTPKPRELCRDECEVLENDLCRQEYNIARSNPLILMQLQLPKCEELPLPESPEAANCMRIGIPVER
>gnl|CDD|143578 cd07469, CRD_TK_ROR_related, Cysteine-rich domain of proteins similar to tyrosine kinase-like orphan receptors. The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor (Ror) proteins, a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands
SAGYCATYRGEVCRAYLSNDALVWFNSSYADPEGLNEQLTTGLWEELIKTVSELCRPAAEKLLCNYAFPE
CHPSGVGPTPKPLCREDCLAVKELFCYKDWALIEENKQRGIYLKSRGHFTLPECESLPSIHADPPACSHI
PLTDLKK
>gnl|CDD|143621 cd07470, CYTH-like_mRNA_RTPase, CYTH-like mRNA triphosphatase (RTPase) component of the mRNA capping apparatus. This subgroup includes fungal and protozoal RTPases. RTPase catalyzes the first step in the mRNA cap formation process, the removal of the gamma-phosphate of triphosphate terminated pre-mRNA. This activity is metal-dependent. The 5'-end of the resulting mRNA diphosphate is subsequently capped with GMP by RNA guanylytransferase, and then further modified by one or more methyltransferases. The mRNA cap-forming activity is an essential step in mRNA processing. The RTPases are not conserved among eukarya. The structure and mechanism of this fungal RTPase domain group is different from that of higher eukaryotes. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel. The RTPase domain of the mimivirus RTPase-GTase fusion mRNA capping enzyme also belongs to this subgroup
KTVAEWLYAYLISLSEESESHLEIEAKLGTIIDKRTGERITLPVSTDIILADRARTRFESNVTESQHKRI
NEFLNELVEESSKKREKLKYEHSRTRDSFYELPNATGKKTKIRVSYDQKTGRVLACIRKRRLADLDIHSP
GSPYDIRISINLELPVPGPNSKITGNGPILTRRKDRLSYTHNAFRIDLTKVTSSEPNQHTEESYEVEVEL
DSKALLDAFDKKDGDSNLLEELVETLLNNARIL
>gnl|CDD|213030 cd07472, HmuY_like, Bacterial proteins similar to Porphyromonas gingivalis HmuY and the C-terminal domain of PARMER_03218. HmuY is a hemophore that scavenges heme from infected hosts and delivers it to the outer membrane receptor HmuR. Related but uncharacterized proteins do not appear to share the specific heme-binding site. The C-terminal domain of PARMER_03128, an uncharacterized protein from Parabacteroides merdae, plus related proteins from Bacteroidetes, appear to be a distantly related family and have been included in this model
DMKRVIILKNAGACYFSIADMAVYTKADVAANAGKIDFVYLYRAKLNIDFNHALVSPSADPEYLPGVTLP
AGVKNKTKIEKVGNLQDDQLARLQYGVYIDDLDFETLDFTGATDYALNLKSEAGAFVETADGKYRAYVYF
NKVNDTKKVMTVSIKRY
>gnl|CDD|173799 cd07473, Peptidases_S8_Subtilisin_like, Peptidase S8 family domain in Subtilisin-like proteins. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
SGDVVVAVIDTGVDYNHPDLKDNMWVNPGEIPGNGIDDDGNGYVDDIYGWNFVNNDNDPMDDNGHGTHVA
GIIGAVGNNGIGIAGVAWNVKIMPLKFLGADGSGTTSDAIKAIDYAVDMGAKIINNSWGGGGPSQALRDA
IARAIDAGILFVAAAGNDGTNNDKTPTYPASYDLDNIISVAATDSNDALASFSNYGKKTVDLAAPGVDIL
STSPGGGYGYMSGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILSSAD
>gnl|CDD|173800 cd07474, Peptidases_S8_subtilisin_Vpr-like, Peptidase S8 family domain in Vpr-like proteins. The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
GKGVKVAVIDTGIDYTHPDLGGPGFPNDKVKGGYDFVDDDYDPMDTRPYPSPLGDASAGDATGHGTHVAG
IIAGNGVNVGTIKGVAPKADLYAYKVLGPGGSGTTDVIIAAIEQAVDDGMDVINLSLGSSVNGPDDPDAI
AINNAVKAGVVVVAAAGNSGPAPYTIGSPATAPSAITVGASTVADVAEADTVGPSSSRGPPTSDSAIKPD
IVAPGVDIMSTAPGSGTGYARMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTAKPLYDSDGVVY
PVSRQGAGRVDALRA
>gnl|CDD|173801 cd07475, Peptidases_S8_C5a_Peptidase, Peptidase S8 family domain in Streptococcal C5a peptidases. Streptococcal C5a peptidase (SCP), is a highly specific protease and adhesin/invasin. The subtilisin-like protease domain is located at the N-terminus and contains a protease-associated domain inserted into a loop. There are three fibronectin type III (Fn) domains at the C-terminus. SCP binds to integrins with the help of Arg-Gly-Asp motifs which are thought to stabilize conformational changes required for substrate binding. Peptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
PLWDKGGYKGEGMVVAVIDSGVDPTHDAFRLDDDSKAKYSEEFEAKKKKAGIGYGKYYNEKVPFAYNYAD
NNDDILDEDDGSSHGMHVAGIVAGNGDEEDNGEGIKGVAPEAQLLAMKVFSNPEGGSTYDDAYAKAIEDA
VKLGADVINMSLGSTAGFVDLDDPEQQAIKRAREAGVVVVVAAGNDGNSGSGTSKPLATNNPDTGTVGSP
ATADDVLTVASANKKVPNPNGGQMSGFSSWGPTPDLDLKPDITAPGGNIYSTVNDNTYGYMSGTSMASPH
VAGASALVKQRLKEKYPKLSGEELVDLVKNLLMNTATPPLDSEDTKTYYSPRRQGAGLIDVAKAIA
>gnl|CDD|173802 cd07476, Peptidases_S8_thiazoline_oxidase_subtilisin-like_protease, Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases. Thiazoline oxidase/subtilisin-like protease is produced by the symbiotic bacteria Prochloron spp. that inhabit didemnid family ascidians. The cyclic peptides of the patellamide class found in didemnid extracts are now known to be synthesized by the Prochloron spp. The prepatellamide is heterocyclized to form thiazole and oxazoline rings and the peptide is cleaved to form the two cyclic patellamides A and C. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution)
LLFAFGGGDPRITIAILDGPVDRTHPCFRGANLTPLFTYAAAACQDGGASAHGTHVASLIFGQPCSSVEG
IAPLCRGLNIPIFAEDRRGCSQLDLARAINLALEQGAHIINISGGRLTQTGEADPILANAVAMCQQNNVL
IVAAAGNEGCACLHVPAALPSVLAVGAMDDDGLPLKFSNWGADYRKKGILAPGENILGAALGGEVVRRSG
TSFAAAIVAGIAALLLSLQLRRGAPPDPLAVRRALLETATPCDPEAAEECERCLAGR
>gnl|CDD|173803 cd07477, Peptidases_S8_Subtilisin_subset, Peptidase S8 family domain in Subtilisin proteins. This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
GVKVAVIDTGIDSSHPDLKLNIVGGANFTGDDNNDYQDGNGHGTHVAGIIAALDNGVGVVGVAPEADLYA
VKVLNDDGSGTYSDIIAGIEWAIENGMDIINMSLGGPSDSPALREAIKKAYAAGILVVAAAGNSGNGDSS
YDYPAKYPSVIAVGAVDSNNNRASFSSTGPEVELAAPGVDILSTYPNNDYAYLSGTSMATPHVAGVAALV
WSKRPELTNAQVRQALNKT
>gnl|CDD|173804 cd07478, Peptidases_S8_CspA-like, Peptidase S8 family domain in CspA-like proteins. GSP (germination-specific protease) converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores. Analysis of an enzyme fraction of GSP showed that it was composed of a gene cluster containing the processed forms of products of cspA, cspB, and cspC which are positioned in a tandem array just upstream of the 5' end of sleC. The amino acid sequences deduced from the nucleotide sequences of the csp genes showed significant similarity and showed a high degree of homology with those of the catalytic domain and the oxyanion binding region of subtilisin-like serine proteases. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
LTGKGVLVGIIDTGIDYLHPEFRNEDGTTRILYIWDQTIPGGPPPGGYYGGGEYTEEIINAALASDNPYD
IVPSRDENGHGTHVAGIAAGNGDNNPDFKGVAPEAELIVVKLKQAKKYLREFYEDVPFYQETDIMLAIKY
LYDKALELNKPLVINISLGTNFGSHDGTSLLERYIDAISRLRGIAVVVGAGNEGNTQHHHSGGIVPNGET
KTVELNVGEGEKGFNLEIWGDFPDRFSVSIISPSGESSGRINPGIGGSESYKFVFEGTTVYVYYYLPEPY
TGDQLIFIRFKNIKPGIWKIRLTGVSITDGRFDAWLPSRGLLSENTRFLEPDPYTTLTIPGTARSVITVG
AYNQNNNSIAIFSGRGPTRDGRIKPDIAAPGVNILTASPGGGYTTRSGTSVAAAIVAGACALLLQWGIVR
GNDPYLYGEKIKTYLIRGARRRPGDEYPNPEWGYG
>gnl|CDD|173805 cd07479, Peptidases_S8_SKI-1_like, Peptidase S8 family domain in SKI-1-like proteins. SKI-1 (type I membrane-bound subtilisin-kexin-isoenzyme) proteins are secretory Ca2+-dependent serine proteinases cleave at nonbasic residues: Thr, Leu, and Lys. SKI-1s play a critical role in the regulation of the synthesis and metabolism of cholesterol and fatty acid metabolism. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
WQLGYTGAGVKVAVFDTGLAKDHPHFRNVKERTNWTNEKTLDDGLGHGTFVAGVIASSREQCLGFAPDAE
IYIFRVFTNNQVSYTSWFLDAFNYAILTKIDVLNLSIGGPDFMDKPFVDKVWELTANNIIMVSAIGNDGP
LYGTLNNPADQMDVIGVGGIDFDDNIARFSSRGMTTWELPGGYGRVKPDIVTYGSGVYGSKLKGGCRALS
GTSVASPVVAGAVALLLSTVPEKRDLINPASMKQALIESATRLPG
>gnl|CDD|173806 cd07480, Peptidases_S8_12, Peptidase S8 family domain, uncharacterized subfamily 12. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
TTSPFTGAGVRVAVLDTGIDLTHPAFAGRDITTKSFVGGEDVQDGHGHGTHCAGTIFGRDVPGPRYGVAR
GAEIALIGKVLGDGGGGDGGILAGIQWAVANGADVISMSLGADFPGLVDQGWPPGLAFSRALEAYRQRAR
LFDALMTLVAAQAALARGTLIVAAAGNESQRPAGIPPVGNPAACPSAMGVAAVGALGRTGNFSAVANFSN
GEVDIAAPGVDIVSAAPGGGYRSMSGTSMATPHVAGVAALWAEALPKAGGRALAALLQARLTAARTTQFA
PGLDLPDRGVGLGLAPA
>gnl|CDD|173807 cd07481, Peptidases_S8_BacillopeptidaseF-like, Peptidase S8 family domain in BacillopeptidaseF-like proteins. Bacillus subtilis produces and secretes proteases and other types of exoenzymes at the end of the exponential phase of growth. The ones that make up this group is known as bacillopeptidase F, encoded by bpr, a serine protease with high esterolytic activity which is inhibited by PMSF. Like other members of the peptidases S8 family these have a Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity
GTGIVVANIDTGVDWTHPALKNKYRGWGGGSADHDYNWFDPVGNTPLPYDDNGHGTHTMGTMVGNDGDGQ
QIGVAPGARWIACRALDRNGGNDADYLRCAQWMLAPTDSAGNPADPDLAPDVINNSWGGPSGDNEWLQPA
VAAWRAAGIFPVFAAGNDGPRCSTLNAPPANYPESFAVGATDRNDVLADFSSRGPSTYGRIKPDISAPGV
NIRSAVPGGGYGSSSGTSMAAPHVAGVAALLWSANPSLIGDVDATEAILTETAR
>gnl|CDD|173808 cd07482, Peptidases_S8_Lantibiotic_specific_protease, Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific proteases. Lantiobiotic (lanthionine-containing antibiotics) specific proteases are very similar in structure to serine proteases. Lantibiotics are ribosomally synthesised antimicrobial agents derived from ribosomally synthesised peptides with antimicrobial activities against Gram-positive bacteria. The proteases that cleave the N-terminal leader peptides from lantiobiotics include: epiP, nsuP, mutP, and nisP. EpiP, from Staphylococcus, is thought to cleave matured epidermin. NsuP, a dehydratase from Streptococcus and NisP, a membrane-anchored subtilisin-like serine protease from Lactococcus cleave nisin. MutP is highly similar to epiP and nisP and is thought to process the prepeptide mutacin III of S. mutans. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values
KVTVAVIDSGIDPDHPDLKNSISSYSKNLVPKGGYDGKEAGETGDINDIVDKLGHGTAVAGQIAANGNIK
GVAPGIGIVSYRVFGSCGSAESSWIIKAIIDAADDGVDVINLSLGGYLIIGGEYEDDDVEYNAYKKAINY
AKSKGSIVVAAAGNDGLDVSNKQELLDFLSSGDDFSVNGEVYDVPASLPNVITVSATDNNGNLSSFSNYG
NSRIDLAAPGGDFLLLDQYGKEKWVNNGLMTKEQILTTAPEGGYAYMYGTSLAAPKVSGALALIIDKNPL
KKPPDEAIRILYNT
>gnl|CDD|173809 cd07483, Peptidases_S8_Subtilisin_Novo-like, Peptidase S8 family domain in Subtilisin_Novo-like proteins. Subtilisins are a group of alkaline proteinases originating from different strains of Bacillus subtilis. Novo is one of the strains that produced enzymes belonging to this group. The enzymes obtained from the Novo and BPN' strains are identical. The Carlsburg and Novo subtilisins are thought to have arisen from a common ancestral protein. They have similar peptidase and esterase activities, pH profiles, catalyze transesterification reactions, and are both inhibited by diispropyl fluorophosphate, though they differ in 85 positions in the amino acid sequence. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin.. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
KTVIVAVLDSGVDIDHEDLKGKLWINKKEIPGNGIDDDNNGYIDDVNGWNFLGQYDPRRIVGDDPYDLTE
KGYGNNDVNGPISDADHGTHVAGIIAAVRDNGIGIDGVADNVKIMPLRIVPNGDERDKDIANAIRYAVDN
GAKVINMSFGKSFSPNKEWVDDAIKYAESKGVLIVHAAGNDGLDLDITPNFPNDYDKNGGEPANNFITVG
ASSKKYENNLVANFSNYGKKNVDVFAPGERIYSTTPDNEYETDSGTSMAAPVVSGVAALIWSYYPNLTAK
EVKQIILESGV
>gnl|CDD|173810 cd07484, Peptidases_S8_Thermitase_like, Peptidase S8 family domain in Thermitase-like proteins. Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values
TPNDPYYSYQWNLDQIGAPKAWDITGGSGVTVAVVDTGVDPTHPDLLKVKFVLGYDFVDNDSDAMDDNGH
GTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDANGSGSLADIANGIRYAADKGAKVINLSLGGGLGST
ALQEAINYAWNKGVVVVAAAGNEGVSSVSYPAAYPGAIAVAATDQDDKRASFSNYGKWVDVSAPGGGILS
TTPDGDYAYMSGTSMATPHVAGVAALLYSQGPLSASEVRDALKKTADDIG
>gnl|CDD|173811 cd07485, Peptidases_S8_Fervidolysin_like, Peptidase S8 family domain in Fervidolysin. Fervidolysin found in Fervidobacterium pennivorans is an extracellular subtilisin-like keratinase. It is contains a signal peptide, a propeptide, and a catalytic region. The tertiary structure of fervidolysin is similar to that of subtilisin. It contains a Asp/His/Ser catalytic triad and is a member of the peptidase S8 (subtilisin and kexin) family. The catalytic triad is similar to that found in trypsin-like proteases, but it does not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values
AAWEFGTGGPGIIVAVVDTGVDGTHPDLQGNGDGDGYDPAVNGYNFVPNVGDIDNDVSVGGGHGTHVAGT
IAAVNNNGGGVGGIAGAGGVAPGVKIMSIQIFAGRYYVGDDAVAAAIVYAADNGAVILQNSWGGTGGGIY
SPLLKDAFDYFIENAGGSPLDGGIVVFSAGNSYTDEHRFPAAYPGVIAVAALDTNDNKASFSNYGRWVDI
AAPGVGTILSTVPKLDGDGGGNYEYLSGTSMAAPHVSGVAALVLSKFPDVFTPEQIRKLLEES
>gnl|CDD|173812 cd07487, Peptidases_S8_1, Peptidase S8 family domain, uncharacterized subfamily 1. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
GKGITVAVLDTGIDAPHPDFDGRIIRFADFVNTVNGRTTPYDDNGHGTHVAGIIAGSGRASNGKYKGVAP
GANLVGVKVLDDSGSGSESDIIAGIDWVVENNEKYNIRVVNLSLGAPPDPSYGEDPLCQAVERLWDAGIV
VVVAAGNSGPGPGTITSPGNSPKVITVGAVDDNGPHDDGISYFSSRGPTGDGRIKPDVVAPGENIVSCRS
PGGNPGAGVGSGYFEMSGTSMATPHVSGAIALLLQANPILTPDEVKCILRDTAT
>gnl|CDD|173813 cd07488, Peptidases_S8_2, Peptidase S8 family domain, uncharacterized subfamily 2. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
RPGKFLWDKNDSKNAPNTLAAVFIRNNPRFGRNNTFDDHATLVASIMGGRDGGLPAVNLYSSAFGIKSNN
GQWQECLEAQQNGNNVKIINHSYGEGLKRDPRAVLYGYALLSLYLDWLSRNYEVINVFSAGNQGKEKEKF
GGISIPTLAYNSIVVGSTDRNGDRFFASDVSNAGSEINSYGRRKVLIVAPGSNYNLPDGKDDFVSGTSFS
APLVTGIIALLLEFYDRQYKKGNNNLIALRALVSSSV
>gnl|CDD|173814 cd07489, Peptidases_S8_5, Peptidase S8 family domain, uncharacterized subfamily 5. gap in seq This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
GVDKLHAEGITGKGVKVAVVDTGIDYTHPALGGCFGPGCKVAGGYDFVGDDYDGTNPPVPDDDPMDCQGH
GTHVAGIIAANPNAYGFTGVAPEATLGAYRVFGCSGSTTEDTIIAAFLRAYEDGADVITASLGGPSGWSE
DPWAVVASRIVDAGVVVTIAAGNDGERGPFYASSPASGRGVIAVASVDSYFSSWGPTNELYLKPDVAAPG
GNILSTYPLAGGGYAVLSGTSMATPYVAGAAALLIQARHGKLSPAELRDLLASTAKPLPWSDGTSALPDL
APVAQQGAGLVNAYKALYATTTLSPSSLSLND
>gnl|CDD|173815 cd07490, Peptidases_S8_6, Peptidase S8 family domain, uncharacterized subfamily 6. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
GVTVAVLDTGVDADHPDLAGRVAQWADFDENRRISATEVFDAGGHGTHVSGTIGGGGAKGVYIGVAPEAD
LLHGKVLDDGGGSLSQIIAGMEWAVEKDADVVSMSLGGTYYSEDPLEEAVEALSNQTGALFVVSAGNEGH
GTSGSPGSAYAALSVGAVDRDDEDAWFSSFGSSGASLVSAPDSPPDEYTKPDVAAPGVDVYSARQGANGD
GQYTRLSGTSMAAPHVAGVAALLAAAHPDLSPEQIKDALTETAY
>gnl|CDD|173816 cd07491, Peptidases_S8_7, Peptidase S8 family domain, uncharacterized subfamily 7. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
LLKRIKVALIDDGVDILDSDLQGKIIGGKSFSPYEGDGNKVSPYYVSADGHGTAMARMICRICPSAKLYV
IKLEDRPSPDSNKRSITPQSAAKAIEAAVEKKVDIISMSWTIKKPEDNDNDINELENAIKEALDRGILLF
CSASDQGAFTGDTYPPPAARDRIFRIGAADEDGGADAPVGDEDRVDYILPGENVEARDRPPLSNSFVTHT
GSSVATALAAGLAALILYCVRLRAIGAEEENESDGSA
>gnl|CDD|173817 cd07492, Peptidases_S8_8, Peptidase S8 family domain, uncharacterized subfamily 8. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
GVRVAVIDSGVDTDHPDLGNLALDGEVTIDLEIIVVSAEGGDKDGHGTACAGIIKKYAPEAEIGSIKILG
EDGRCNSFVLEKALRACVENDIRIVNLSLGGPGDRDFPLLKELLEYAYKAGGIIVAAAPNNNDIGTPPAS
FPNVIGVKSDTADDPKSFWYIYVEFSADGVDIIAPAPHGRYLTVSGNSFAAPHVTGMVALLLSEKPDIDA
NDLKRLLQRLAV
>gnl|CDD|173818 cd07493, Peptidases_S8_9, Peptidase S8 family domain, uncharacterized subfamily 9. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
GITIAVIDAGFPKVHEAFAFKHLFKNLRILGEYDFVDNSNNTNYTDDDHGTAVLSTMAGYTPGVMVGTAP
NASYYLARTEDVASETPVEEDNWVAAAEWADSLGVDIISSSLGYTTFDNPTYSYTYADMDGKTSFISRAA
NIAASKGMLVVNSAGNEGSTQWKGIGAPADAENVLSVGAVDANGNKASFSSIGPTADGRLKPDVMALGTG
IYVINGDGNITYANGTSFSCPLIAGLIACLWQAHPNWTNLQIKEAILKSAS
>gnl|CDD|173819 cd07494, Peptidases_S8_10, Peptidase S8 family domain, uncharacterized subfamily 10. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
PDDLAALLNATRVHQRGITGRGVRVAMVDTGFYAHPFFESRGYQVRVVLAPGATDPACDENGHGTGESAN
LFAIAPGAQFIGVKLGGPDLVNSVGAFKKAISLSPDIISNSWGYDLRSPGTSWSRSLPNALKALAATLQD
AVARGIVVVFSAGNGGWSFPAQHPEVIAAGGVFVDEDGARRASSYASGFRSKIYPGRQVPDVCGLVGMLP
HAAYLMLPVPPGSQLDRSCAAFPDGTPPNDGWGVFSGTSAAAPQVAGVCALMLQANPGLSPERARSLLNK
TARDVTKGASAQGTSAGP
>gnl|CDD|173820 cd07496, Peptidases_S8_13, Peptidase S8 family domain, uncharacterized subfamily 13. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
GVVVAVLDTGVLFHHPDLAGVLLPGYDFISDPAIANDGDGRDSDPTDPGDWVTGDDVPPGGFCGSGVSPS
SWHGTHVAGTIAAVTNNGVGVAGVAWGARILPVRVLGKCGGTLSDIVDGMRWAAGLPVPGVPVNPNPAKV
INLSLGGDGACSATMQNAINDVRARGVLVVVAAGNEGSSASVDAPANCRGVIAVGATDLRGQRASYSNYG
PAVDVSAPGGDCASDVNGDGYPDSNTGTTSPGGSTYGFLQGTSMAAPHVAGVAALMKSVNPSLTPAQIES
LLQST
>gnl|CDD|173821 cd07497, Peptidases_S8_14, Peptidase S8 family domain, uncharacterized subfamily 14. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
GEGVVIAIVDTGVDYSHPDLDIYGNFSWKLKFDYKAYLLPGMDKWGGFYVIMYDFFSHGTSCASVAAGRG
KMEYNLYGYTGKFLIRGIAPDAKIAAVKALWFGDVIYAWLWTAGFDPVDRKLSWIYTGGPRVDVISNSWG
ISNFAYTGYAPGLDISSLVIDALVTYTGVPIVSAAGNGGPGYGTITAPGAASLAISVGAATNFDYRPFYL
FGYLPGGSGDVVSWSSRGPSIAGDPKPDLAAIGAFAWAPGRVLDSGGALDGNEAFDLFGGTSMATPMTAG
SAALVISALKEKEGVGEYDPFLVRTILMSTA
>gnl|CDD|173822 cd07498, Peptidases_S8_15, Peptidase S8 family domain, uncharacterized subfamily 15. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values
VVVAIIDTGVDLNHPDLSGKPKLVPGWNFVSNNDPTSDIDGHGTACAGVAAAVGNNGLGVAGVAPGAKLM
PVRIADSLGYAYWSDIAQAITWAADNGADVISNSWGGSDSTESISSAIDNAATYGRNGKGGVVLFAAGNS
GRSVSSGYAANPSVIAVAATDSNDARASYSNYGNYVDLVAPGVGIWTTGTGRGSAGDYPGGGYGSFSGTS
FASPVAAGVAALILSANPNLTPAEVEDILTST
>gnl|CDD|319802 cd07499, HAD_CBAP, molecular class B acid phosphatases, similar to Escherichia coli AphA. class B acid phosphatases (CBAPs) have been detected in a minority of bacterial species which include a number of major pathogens such as Escherichia coli, Haemophilus influenzae, and Streptococcus pyogenes. This family includes the CBAP Escherichia coli AphA. The purified enzyme is a broad-spectrum nucleotidase highly active against both 3'- and 5'-mononucleotides and monodeoxynucleotides, which can also act as a phosphotransferase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
VAQIAKSLEGKAPIAVGFDIDDTVLFSSPCFYYGKQTFSPDSFDYLKNQKFWDKVNNGWDEFSIPKEIAK
QLIDMHQKRGDQIYFITGRTPGKTDTVTKTLAKDFHIKNMNPVIFAGDKPVQYTKTQYIQKNNISIHYGD
SDNDILAAREAGARGIRVLRAANSTYKPLPKNGGYGEEVLVNSQY
>gnl|CDD|319803 cd07500, HAD_PSP, phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p. This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LIVFDMDSTLIQQEVIDELAAEAGVGEEVAAITERAMRGELDFEESLRERVALLKGLPESVLDEVYERLT
LTPGAEELIQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKLTGKVLGPIVDAQRKAE
TLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIAFHA
>gnl|CDD|319804 cd07501, HAD_MDP-1_like, eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH. This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
PKCLVFDLDYTLWPGVVDEHGIPPFKDRGGKEVSLYPDAQEILKELKERGILLAVASRNNEFDHANEVLE
KLDLKELFDAFEIYPGSKSSHFRKIAKELGIGFDSMVFFDDEPRNREEVSEGGVTCILV
>gnl|CDD|319805 cd07502, HAD_PNKP-C, C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related phosphatases. This family includes the C-terminal domain of the bifunctional enzyme T4 polynucleotide kinase/phosphatase, PNKP. The PNKP phosphatase domain can catalyze the hydrolytic removal of the 3'-phosphoryl of DNA, RNA and deoxynucleoside 3'-monophosphates. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
PKAVIFDLDGTLADTNGRQPYLERRPRDWDAFFEAADHDPPNAPVIELVKESALTGYEIVYLSGRPERYR
RDTLRWLAKHGIPDDALHMRGNADRRKDRRVKLEILRRLIRTRFEVRLLVDDREQVVDMWRRAGFPCLQV
AWGDF
>gnl|CDD|319806 cd07503, HAD_HisB-N, histidinol phosphate phosphatase and related phosphatases. This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
KALFLDRDGVINVDVPYVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKM
RELLASQGVEIDDIYYCPHHPDDGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGI
LV
>gnl|CDD|319807 cd07504, HAD_5NT, haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB. 5'-nucleotidases dephosphorylate nucleoside 5prime-monophosphates. This family includes human 5'-nucleotidase, cytosolic IIIA (cN-IIIA, previously called cN-III; NT5C3A) the main pyrimidine 5'-nucleotidase in erythrocytes which dephosphorylates the pyrimidine nucleotides CMP, UMP, TMP, and the purine 7-methylguanosine monophosphate (m7GM), and possesses phosphotransferase activity. It also includes human 5'-nucleotidase, cytosolic IIIB (cN-IIIB; NT5C3B) which has a strong preference for m7GMP, dephosphorylates CMP and UMP and, with significantly lower efficiency, GMP and AMP, and can also act as a phosphotransferase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
DPTRVEEKICGLVKGGADKLQIISDFDMTLSRFRYNGGRCPTCHNIFDNCKLLTEECRAKLVQLKEKYYP
IEIDPHLTIEEKVPYMEEWWTKSHELLIEQGFQKDAIDQIVAESDIALRDGYEEFFEKLQQHGIPVLIFS
AGLGDIIEEVLRQAGVYHPNVKVVSNFMDFDDNGVLTGFKGPLIHVFNKNESALKNTDYFKQLKGRTNII
LLGDSIGDLRMADGVPNVEHILKIGFLNDKVEELLEKYMDSYDIVLVNDETLDVPNSILQKIL
>gnl|CDD|319808 cd07505, HAD_BPGM-like, beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
AVIFDMDGVLIDTEPLHRQAWQLLERKNALLLELIASEGLKLKPGVVELLDALKAAGIPVAVATSSSRRN
VELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERCLVFEDSLAGIEAAKAAGMTVVA
VPD
>gnl|CDD|319809 cd07506, HAD_like, uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LVLFDIDGTLLPGVREALEALAARPDVVLGLLTGNLEEIARIKLEPFGLDEDFPVGAFGDDHADRNELPP
IAVERARAKTGYAFDPHQVVVIGDTPNDVACARALGARSVAVATG
>gnl|CDD|319810 cd07507, HAD_Pase, haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii mannosyl-3-phosphoglycerate phosphatase and Persephonella marina glucosyl-3-phosphoglycerate phosphatase. This family includes Pyrococcus horikoshii and Thermus thermophilus HB27 mannosyl-3-phosphoglycerate phosphatases (MpgPs) which catalyze the dephosphorylation of alpha-mannosyl-3-phosphoglycerate (MPG) to produce alpha-mannosylglycerate (MG), and Persephonella marina glucosyl-3-phosphoglycerate phosphatase (GpgP) which catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) to produce glucosylglycerate (GG). It also includes Methanococcoides burtonii MpgP protein which is able to dephosphorylate GPG to GG, and MPG to MG. Similar flexibilities in substrate specificity have been confirmed in vitro for the MpgPs from Thermus thermophiles and Pyrococcus horikoshii. Screens with natural substrates have not yet detected activity for another member Escherichia Coli YedP. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
VIFTDLDGTLLDHHTYSFDPARPALERLKERGIPVVPCTSKTRAEVEYLRKELGIEDPFIVENGGAIFIP
RGYFKFPGRCKSEGGYEVIELGKPYREIRAALEKIREETGFKITGFGDLTEEEIAELTGLPRERAALAKE
REYSETIILRSDEEEDEKVLEALEERGLKITKGGRFYHVLGAGADKGKAVAILAALYRQLYEAIVTVGLG
DSPNDLPMLEAVDIAFVVKSLNGKYESVILPGVLKAPAPGPEGWN
>gnl|CDD|319811 cd07508, HAD_Pase_UmpH-like, haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family. Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase, Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LVISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSAKA
TARFLRSRKFGKKVYVLGEEGLKEELRAAGFRIAGGPSKGIETYAELVEHLEDDENVDAVIVGSDFKLNF
AKLRKACRYLRNPGCLFIATAPDRIHPLKDGGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKF
GIDPERVLFVGDRLATDVLFGKACGFQTLLVLTGVTTLEDLQAYIDHELVPDYYADSLAD
>gnl|CDD|319812 cd07509, HAD_PPase, inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP). LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLT
AARQYLEEKGLRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLLLDGAPLIALHKGR
YYKRKDGLALDPGAFVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACG
MRGILVRTGKYRPSDEKKPNVPPDLTADSFADAVDHIL
>gnl|CDD|319813 cd07510, HAD_Pase_UmpH-like, UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase. This subfamily includes the phosphoglycolate phosphatases (human PGP and Arabidopsis thaliana PGLP2) and p-nitrophenylphosphatases (Schizosaccharomyces pombe PHO2 and Saccharomyces PHO13p). It belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
VDTFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGLKEEEIFSS
AYCAARYLRQRLPGPADGKVYVLGGEGLRAELEAAGVAHLGGPDDGLRRAAPKDWLLAGLDPDVGAVLVG
LDEHVNYLKLAKATQYLRDPGCLFVATNRDPWHPLSDGSFIPGTGSLVAALETASGRQAIVVGKPSRFMF
DCISSKFSIDPARTCMVGDRLDTDILFGQNCGLKTLLVLTGVSTLEEALAKLSNDLVPDYYVESLADLLE
LL
>gnl|CDD|319814 cd07511, HAD_like, uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to the uncharacterized human CECR5 (cat eye syndrome critical region protein 5). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
FGFAFDIDGVLVRGKKPIPGAPKALKFLNDNKIPFIFLTNGGGFPESKRADFLSKLLGVEVSPDQVIQSH
SPGKPTELTYDFAEHVLQRQAKRLGKTEPFKYVYMVGDNPMSDIRGANLFDRYVVTGWISILVRTG
>gnl|CDD|319815 cd07512, HAD_PGPase, haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ. Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
AVIFDLDGTLIDSAPDLHAALNAVLAAEGLAPLSLAEVRSFVGHGAPALIRRAFAAAGEDLDGPLHDALL
ARFLDHYEADPPGLTRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQ
RKPDPAPLRAAIRRLGGDVSRALMVGDSETDAATARAAGVPFVLVTFGYRHAPVAELPHDAVFSDFDALP
DLLA
>gnl|CDD|319816 cd07514, HAD_Pase, phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily. Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LIAVDIDGTLTDRRRSIDLRAIEAIRKLEKAGIPVVLVTGNSLPVARALAKYLGLSGPVVAENGGVDKGT
GLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKLL
>gnl|CDD|319817 cd07515, HAD-like, uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
VIAFDADDTLWHNEPIELLPGVREALAALKADYRLVLITKGDLLDQEQKLARSGLSDYFDAVEVVSEKDP
DTYRRVLSRYGIGPERFVMVGNSLRSDILPVLAAGGWGVHIPYELTWKEEADEPDAHPRAA
>gnl|CDD|319818 cd07516, HAD_Pase, phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily. Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDP
TGKEILERLISKEDVKELEEFLRKLGIGINIYTNDDWADTIYEENEDDEIIKPAEILDDLLLPPDEDITK
ILFVGEDEELDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNEN
DLSMLEYAGLGVAMGNAIDEVKEAADYVTLTNNEDGVAKAIEK
>gnl|CDD|319819 cd07517, HAD_HPP, phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily. Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDSYVSYNGQYVFFE
GEVIYKNPLPQELVERLTEFAKEQGHPVSFYGQLLLFEDEEEEQKYEELRPELRFVRWHPLSTDVIPKGG
SKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIADYVTKDVDEDGILKALK
HFG
>gnl|CDD|319820 cd07518, HAD_YbiV-Like, Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily. Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
KLIATDMDGTFLNDDKTYDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVVY
FKFTLNVPDEAAPDIIDELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDG
GNDIEMLKYAGYSYAMENAPEEVKAAAKYVAPSNNENGVLQVIE
>gnl|CDD|319821 cd07519, HAD_PTase, hydrolase domain of the bifunctional HAD hydrolase/UbiA family prenyltransferase proteins and related domains; belongs to the haloacid dehalogenase-like superfamily. This family includes bifunctional enzymes that have both an N-terminal HAD hydrolase domain and a C-terminal UbiA family prenyltransferase domain. The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases (PTases) and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. PTases catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways
PLVVDLDGTLLLPYNAEVLDYIQAARAEGRSIVLATASDQRIADRIAAHLGLFDGVFASDGRLNLKGRNK
ADLLVDRFGEKGFDYAGNSRADLPVWDAAAKAIVV
>gnl|CDD|319822 cd07520, HAD_like, uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LVFVDLDDTLFQTARKLPGHGRLAPATVDKRGNALSYMTPAQTAFVDWLLAGAVLIPVTARSVEAMSRVT
LPFRSWAICSHGGVILTPDGEPDPEWLPRPVGKAQAVRWLLERHLFPGARPTLGFGDSLSDLGFMRLCDW
AGTP
>gnl|CDD|319823 cd07521, HAD_FCP1-like, human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily. Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
KLTLVLDLDETLVHSTWKPVLSEDFKIPVLPDGREHGYYVKKRPGVDEFLERLSKLYEIVIFTAGTRAYA
DPVADKLDPNGLFIDRRLFRDSCVYVDGNYVKDLSKLFRDLSKVVIIDDSPGSYWLQPENAIPI
>gnl|CDD|319824 cd07522, HAD_cN-II, cytosolic 5'-nucleotidase II (cN-II) similar to human NT5DC1 (5'-nucleotidase domain-containing protein 1) and NT5DC2. Cytosolic 5'-nucleotidase II (cN-II), also known as purine 5'-nucleotidase, IMP-GMP specific nucleotidase, or high Km 5prime-nucleotidase, catalyzes the dephosphorylation of 6-hydroxypurine nucleoside monophosphates. It is ubiquitously expressed and likely to play an important role in the regulation of purine nucleotide interconversions and in the regulation of IMP and GMP pools within the cell. It is also acts as a phosphotransferase, catalyzing the reverse reaction, the transfer of a phosphate from a monophosphate substrate to a nucleoside acceptor, to form a nucleoside monophosphate. The nucleoside acceptor is preferentially inosine and deoxyinosine, phosphate donors include any 6-hydroxypurine monophosphate substrate of the nucleotidase reaction. Both the dephosphorylation and phosphotransferase reactions are allosterically activated by adenine-based nucleotides and 2,3-bisphosphoglycerate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
FVNRSLNLEKIKVFGFDMDYTLARYNSPELESLIYDLAKERLVEEKGYPEELLKFDYDPNFPVRGLVFDK
EKGNLLKLDAYGQILRAYHGTRPLSDEEVREIYGSNNTGVRDDESRYYFLNTLFSLPEACLLAQLVDYFD
NNPLESDMSYRSIYQDVRAAVDWVHSKGLLKKKIMQDPERYVLRDPELPLLLSRLREAGKKLFLLTNSDY
SYTNKGMKYLLGGFLPKHRDWRDYFDVVIVDARKPGFFTEGTPFREVDTETGQLKITKVGPLEKGKVYSG
GNLKQFTELLGWRGKEVLYFGDHIYSDILKSKKRHGWRTALIVPELGSLFRTGSNPTYFSSQVERYADLY
TS
>gnl|CDD|319825 cd07523, HAD_YsbA-like, uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA. The specific function of Lactococcus lactis YsbA is unknown. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
NFIWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYAEVPDLEEEYKELEAEY
LAKPILFPGAKAVLRWIKEQGGKNFLMTHRDHSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLL
NKYQLNPEETVMIGDRELDIEAGHNAGISTILF
>gnl|CDD|319826 cd07524, HAD_Pase, phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily. Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
IVFCDFDGTITENDNIIYLMDEFAPPLEEWEALKEGVLSQTLSFREGVGQMFELLPSSLKDEIIEFLEKT
AKIRPGFKEFVAFCQEHGIPFIIVSGGMDFFIEPLLEGLVIEKIAIYCNGSDFSGEQIHIDWPHECDCTN
GCGCCKSSIIRKYSKPRPFIIVIGDSVTDLEAAKEADLVFARDGLILKCEEENLPYPPFETFTDIDIHLQ
L
>gnl|CDD|319827 cd07525, HAD_like, uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
DAFLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTNAPRPAESVVRQLAKLGVPPSTYDAIITSGE
VTRELLAREAGLGRKVYHLGPERDANVLEGLDVVATDDAEKAEFILCTGLYDDETETPEDYRKLLKAAAA
RGLPLICANPDLVVPRGGKLIYCAGALAELYEELGGEVIYFGKPHPPIYDLALARLGRPAKARILAVGDG
LHTDILGANAAGLDSLFVTGGIHRRLAAEAGIKSQIVPDFVIP
>gnl|CDD|319828 cd07526, HAD_BPGM_like, subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH. This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate, and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
DLVIFDCDGVLVDSEVIAARVLVEVLAELGARVLAAFEAELQPIPGAAAALSALTLPFCVASNSSRERLT
HSLGLAGLLAYFEGRIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLVIEDSPTGVRAALAAGMTVFGFT
G
>gnl|CDD|319829 cd07527, HAD_ScGPP-like, subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
ALLFDMDGTLVDSTPAVERAWHKWAKEHGVDPEEVLKVSHGRRAIDVIRKLAPDDADIELVLALETEEPE
SYPEGVIAIPGAVDLLASLPAAGDRWAIVTSGTRALAEARLEAAGLPHPEVLVTADDVKNGKPDPEPYLL
GAKLLGLDPSDCVVFEDAPAGIKAGKAAGARVVAVNTSHDLEQLEAAGADLVVEDLSDISVDGDE
>gnl|CDD|319830 cd07528, HAD_CbbY-like, subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY. This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
ALIFDVDGTLAETEELHRRAFNNAFFAERGLDWYWDRELYGELLRVGGGKERIAAYFEKVGWPESAPKDL
KELIADLHKAKTERYAELIAAGLLPLRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSALLGPERRAI
FDAIAAGDDVAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCIVTPS
>gnl|CDD|319831 cd07529, HAD_AtGPP-like, subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2. This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDE
QQEALAELFMGTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVK
GRGKPAPDIFLVAAKRFNEPPKDPSKCLVFEDSPNGVKAAKAAGMQVVMVPD
>gnl|CDD|319832 cd07530, HAD_Pase_UmpH-like, UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase. Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSAL
ATAQYLAEQLPGAKVYVIGEEGLRTALHEAGLTLTDENPDYVVVGLDRDLTYEKLAEATLAIRNGAKFIA
TNPDLTLPTERGLLPGNGSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAA
GIAAGIDTLLVLTGVTTREDLAKPPYRPTYIVPSLRE
>gnl|CDD|319833 cd07531, HAD_Pase_UmpH-like, UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar phosphatase. Bacillus subtilis AraL is a phosphatase displaying activity towards different sugar phosphate substrates; it is encoded by the arabinose metabolic operon araABDLMNPQ-abfA and may play a role in the dephosphorylation of substrates related to l-arabinose metabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
KGYIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSY
VTARFLAREKPNAKVFVTGEEGLIEELRLAGLEIVDKYDEAEYVVVGSNRKITYELLTKAFRACLRGARY
IATNPDRIFPAEDGPIPDTAAIIGAIEWCTGREPEVVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVD
IAMGKAIGMETALVLTGVTTRENLDRHGYKPDYVLNSIKDLV
>gnl|CDD|319834 cd07532, HAD_PNPase_UmpH-like, UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium falciparum PNPase. Plasmodium falciparum para nitrophenyl phosphate phosphatase (PNPase) catalyzes the dephosphorylation of thiamine monophosphate to thiamine, other substrates on which its active are nucleotides, phosphorylated sugars, pyridoxal-5-phosphate, and paranitrophenyl phosphate. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
EWLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENN
ILSSAAVIADYLKEKGFKKKVYVIGEEGIRKELEEAGIVSCGGDGEDEKDDSMGDFAHNLELDPDVGAVV
VGRDEHFSYPKLMKACNYLRNPDVLFLATNMDATFPGPVGRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQ
ILNFLMKSGVIKPERTLMIGDRLKTDILFANNCGFQSLLVGTGVNSLEDAEKIKKEGDPKKKDLVPDTYL
PSLGHL
>gnl|CDD|319835 cd07533, HAD_like, uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LVIFDWDGTLADSQHNIVAAMTAAFADLGLPVPSAAEVRSIIGLSLDEAIARLLPMATPALVAVAERYKE
AFDILRLLPEHAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADDTPSKP
HPEMLREILAELGVDPSRAVMVGDTAYDMQMAANAGAHAVGVAWGYHSLEDLRSAGADAVVDHFSEL
>gnl|CDD|319836 cd07534, HAD_CAP, molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; belongs to the haloacid dehalogenase-like hydrolase superfamily. Molecular class C acid phosphatases (CAPs) are nonspecific acid phosphatases with generally broad substrate specificity and optimum activity at neutral to acidic pH. Members include Haemophilus influenzae lipoprotein e (P4), Elizabethkingia meningosepticum OlpA, Helicobacter pylori HppA, Enterobacter sp. 4 acid phosphatase PhoI, and Streptococcus pyogenes M1 GAS LppC. Lipoprotein e (P4) exhibits phosphomonoesterase activity with aryl phosphate substrates including nicotinamide mononucleotide (NMN), tyrosine phosphate, phenyl phosphate, p-nitrophenyl phosphate, and 4-methylumbelliferyl phosphate. The role of P4 in NAD+ uptake appears to be the dephosphorylation of NMN to nicotinamide riboside, which is then taken up by the organism. Elizabethkingia meningosepticum OlpA is a broad-spectrum nucleotidase with preference for 5'-nucleotides, it efficiently hydrolyzes nucleotide monophosphates, with a strong preference for 5'-nucleotides and for 3'-AMP; OlpA can also hydrolyze sugar phosphates and beta-glycerol phosphate, although with a lower efficiency. Helicobacter pylori HppA is also a 5' nucleotidase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
SAEYKALYLQAYNLAKMRLDHALKKEKTDKKPAVVLDLDETVLDNSPYQARQVKNGKPFSPETWDKWVQE
AQAKPIPGAVDFLNYANAKGVTIFYVSNRDQKLKAATLKNLKRLGFPQASDDHLLLKTDKSSKESRRQLV
KEKYNIVLLFGDNLGDFGDFTYKKENEDRRALVEKNAEEFGEKFIILPNPMYGSWE
>gnl|CDD|319837 cd07535, HAD_VSP, vegetative storage proteins similar to soybean VSPalpha and VSPbeta proteins; belongs to the haloacid dehalogenase-like superfamily. Soybean [Glycine max (L.) Merr.] vegetative storage protein VSPalpha and VSPbeta levels were identified as storage proteins due to their abundance and pattern of expression in plant tissues, they accumulate to almost one-half the amount of soluble leaf protein when soybean plants are continually depodded. They possess acid phosphatase activity which appears to be low compared to several other plant acid phosphatases, it increases in the leaves of depodded soybean plants, but to no more than 0.1% of the total acid phosphatase activity in these leaves. This acid phosphatase activity has maximal activity at pH 5.0 - 5.5, and can liberate Pi from different substrates such as napthyl acid phosphate, carboxyphenyl phosphate, sugar-phosphates, glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, phosphoenolpyruvate, ATP, ADP, PPi, and short chain polyphosphates; they cleave phosphoenolpyruvate, ATP, ADP, PPI, and polyphosphates most efficiently. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Soybean VSPalpha and VSPbeta lack this active site aspartate, other members of this family have this aspartate and may be more active. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
VEDYMKGGQYLRDSSVKTVNALAYAYSKVLAGDGMDVWIFDIDDTLLSNIPYYKKHGYGGEKFDSTAFDE
WVEKGKAPALPESLKLYNKLLELGFKIFLLSGRDETLRNATVENLKKAGYHGWEHLILRGPDDQGKSAVV
YKSEQRKELEEKGYRIVGNIGDQWSDLLGDPEGDRTFKLPNPMYYI
>gnl|CDD|319838 cd07536, P-type_ATPase_APLT, Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, Neo1p, and human ATP8A2, -9B, -10D, -11B, and -11C. Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. Mammalian ATP11C may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. The yeast Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Human putative ATPase phospholipid transporting 9B, ATP9B, localizes to the trans-golgi network in a CDC50 protein-independent manner. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
DNSISNQKYNVFTFLPGVLYEQFKRFLNLYFLVIACLQFVPALKPGYLYTTWAPLIFILAVTMTKEAIDD
FRRFQRDKEVNKKQLYSKLTGRKVQIKSSDIQVGDIVIVEKNQRIPSDMVLLRTSEPQGSCYVETAQLDG
ETDLKLRVAVSCTQQLPALGDLMKISAYVECQKPQMDIHSFEGNFTLEDSDPPIHESLSIENTLLRASTL
RNTGWVIGVVVYTGKETKLVMNTSNAKNKVGLLDLELNRLTKALFLALVVLSLVMVTLQGFWGPWYGEKN
WYIKKMDTTSDNFGRNLLRFLLLFSYIIPISLRVNLDMVKAVYAWFIMWDENMYYIGNDTGTVARTSTIP
EELGQVVYLLTDKTGTLTQNEMIFKRCHIGGVSYGGQVLSFCILQLLEFTSDRKRMSVIVRDESTGEITL
YMKGADVAISPIVSKDSYMEQYNDWLEEECGEGLRTLCVAKKALTENEYQEWESRYTEASLSLHDRSLRV
AEVVESLERELELLGLTAIEDRLQAGVPETIETLRKAGIKIWMLTGDKQETAICIAKSCHLVSRTQDIHL
LRQDTSRGERAAITQHAHLELNAFRRKHDVALVIDGDSLEVALKYYRHEFVELACQCPAVICCRVSPTQK
ARIVTLLKQHTGRRTLAIGDGGNDVSMIQAADCGVGISGKEGKQASLAADYSITQFRHLGRLLLVHGRNS
YNRSAALGQYVFYKGLIISTIQAVFSFVFGFSGVPLFQGFLMVGYNVIYTMFPVFSLVIDQDVKPESAML
YPQLYKDLQKGRSLNFKTFLGWVLISLYHGGILFY
>gnl|CDD|319839 cd07538, P-type_ATPase, uncharacterized subfamily of P-type ATPase transporters. This subfamily contains P-type ATPase transporters of unknown function. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd2+, and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine
GLTEAEARRRLESGGKNELPQPKKRTLLASILDVLREPMFLLLLAAALIYFVLGDPREGLILLIFVVVII
AIEVVQEWRTERALEALKNLSSPRATVIRDGRERRIPSRELVPGDLLILGEGERIPADGRLLENDDLGVD
ESTLTGESVPVWKRIDGKAMSAPGGWDKNFCYAGTLVVRGRGVAKVEATGSRTELGKIGKSLAEMDDEPT
PLQKQTGRLVKLCALAALVFCALIVAVYGVTRGDWIQAILAGITLAMAMIPEEFPVILTVFMAMGAWRLA
KKNVLVRRAAAVETLGSITVLCVDKTGTLTKNQMEVVELTSLVREYPLRPELRMMGQVWKRPEGAFAAAK
GSPEAIIRLCRLNPDEKAAIEDAVSEMAGEGLRVLAVAACRIDESFLPDDLEDAVFIFVGLIGLADPLRE
DVPEAVRICCEAGIRVVMITGDNPATAKAIAKQIGLDNTDNVITGQELDAMSDEELAEKVRDVNIFARVV
PEQKLRIVQAFKANGEIVAMTGDGVNDAPALKAAHIGIAMGKRGTDVAREASDIVLLDDNFSSIVSTIRL
GRRIYDNLKKAITYVFAIHVPIAGLALLPPLLGLPPLLFPVHVVLLELIIDPTCSIVFEAEPAERDIMRR
PPRPPDEPLFGPRLVIKAILQGA
>gnl|CDD|319840 cd07539, P-type_ATPase, uncharacterized subfamily of P-type ATPase transporters. This subfamily contains P-type ATPase transporters of unknown function. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd2+, and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine
PGLSEEPVAAPSRLPARNLALETATRSGILAVAAQLELPPVALLGLAAGASASTGGGVDAVLIVGVLTVN
AVIGGVQRLRAERALAALLAQQQQPARVVRAPAGRTQTVPAESLVPGDVIELRAGEVVPADARLLEADDL
EVDESALTGESLPVDKQVAPTPGAPLADRACMLYEGTTVVSGQGRAVVVATGPHTEAGRAQSLVAPVETA
TGVQAQLRELTSQLLPLSLGGGAAVTGLGLLRGAPLRQAVADGVSLAVAAVPEGLPLVATLAQLAAARRL
SRRGVLVRSPRTVEALGRVDTICFDKTGTLTENRLRVVQVRPPLAELPFESSRGYAAAIGRTGGGIPLLA
VKGAPEVVLPRCDRRMTGGQVVPLTEADRQAIEEVNELLAGQGLRVLAVAYRTLDAGTTHAVEAVVDDLE
LLGLLGLADTARPGAAALIAALHDAGIDVVMITGDHPITARAIAKELGLPRDAEVVTGAELDALDEEALT
GLVADIDVFARVSPEQKLQIVQALQAAGRVVAMTGDGANDAAAIRAADVGIGVGARGSDAAREAADLVLT
DDDLETLLDAVVEGRTMWQNVRDAVHVLLGGNLGEVMFTLIGTAIGGGAPLNTRQLLLVNLLTDMFPALA
LAVE
>gnl|CDD|319841 cd07541, P-type_ATPase_APLT_Neo1-like, Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human putative APLT, ATP9B. Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as a flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. The yeast Neo1 gene is an essential gene; Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Also included in this sub family is human putative ATPase phospholipid transporting 9B, ATP9B, which localizes to the trans-golgi network in a CDC50 protein-independent manner. Levels of ATP9B, along with levels of other ATPase genes, may contribute to expressivity of and atypical presentations of Hailey-Hailey disease (HHD), and the ATP9B gene has recently been identified as a putative Alzheimer's disease loci. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
SNEVRNQKYNIFTFLPKVLYEQFKFFYNLYFLVVALSQFVPALKIGYLYTYWAPLGFVLAVTMAKEAVDD
IRRRRRDKEQNYEKLTVRGETVEIPSSDIKVGDLIIVEKNQRIPADMVLLRTSEKSGSCFIRTDQLDGET
DWKLRIAVPCTQKLPEEGILNSISAVYAEAPQKDIHSFYGTFTINDDPTSESLSVENTLWANTVVASGTV
IGVVVYTGKETRSVMNTSQPKNKVGLLDLEINFLTKILFCAVLALSIVMVALQGFQGPWYIYLFRFLILF
SSIIPISLRVNLDMAKIVYSWQIEHDKNIPGTVVRTSTIPEELGRIEYLLSDKTGTLTQNEMVFKKLHLG
TVSYGGQNLNYEILQIFPFTSESKRMGIIVREEKTGEITFYMKGADVVMSKIVQYNDWLEEECGNMAREG
LRTLVVAKKKLSEEEYQAFEKRYNAAKLSIHDRDLKVAEVVESLERELELLCLTGVEDKLQEDVKPTLEL
LRNAGIKIWMLTGDKLETATCIAKSSKLVSRGQYIHVFRKVTTREEAHLELNNLRRKHDCALVIDGESLE
VCLKYYEHEFIELACQLPAVVCCRCSPTQKAQIVRLIQKHTGKRTCAIGDGGNDVSMIQAADVGVGIEGK
EGKQASLAADFSITQFSHIGRLLLWHGRNSYKRSAKLAQFVMHRGLIISIMQAVFSSVFYFAPIALYQGF
LMVGYSTIYTMAPVFSLVLDQDVSEELAMLYPELYKELTKGRSLSYKTFFIWVLISIYQGGIIMYGALLL
FDSEFVHIVAISFTALILTELI
>gnl|CDD|319842 cd07542, P-type_ATPase_cation, P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and Saccharomyces cerevisiae Ypk9p. Saccharomyces cerevisiae Yph9p localizes to the yeast vacuole and may play a role in sequestering heavy metal ions, its deletion confers sensitivity for growth for cadmium, manganese, nickel or selenium. Human ATP13A2 (PARK9/CLN12) is a lysosomal transporter with zinc as the possible substrate. Mutation in the ATP13A2 gene has been linked to Parkinson's disease and Kufor-Rakeb syndrome, and to neuronal ceroid lipofuscinoses. ATP13A3/AFURS1 is a candidate gene for oculo auriculo vertebral spectrum (OAVS), being one of nine genes included in a 3q29 microduplication in a patient with OAVS. Mutation in the human ATP13A4 may be involved in a speech-language disorder. This subfamily also includes zebrafish ATP13A2 a lysosome-specific transmembrane ATPase protein of unknown function which plays a crucial role during embryonic development, its deletion is lethal. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
DEQSDRRLIYGPNEIDVPLKSILKLLFKEVLNPFYVFQLFSVILWSSDDYYYYAACIVIISVISIFLSLY
ETRKQSKRLREMVHFTCPVRVIRDGEWQTISSSELVPGDILVIPDNGTLLPCDAILLSGSCIVNESMLTG
ESVPVTKTPLPDESNDSLWSIYSIEDHSKHTLFCGTKVIQTRAYEGKPVLAVVVRTGFNTTKGQLVRSIL
YPKPVDFKFYRDSMKFILFLAIIALIGFIYTLIILILNGESLGEIIIRALDIITIVVPPALPAALTVGII
YAQSRLKKKGIFCISPQRINICGKINLVCFDKTGTLTEDGLDLWGVRPVSGNNFGDLEVFSLDLDLDSSL
PNGPLLRAMATCHSLTLIDGELVGDPLDLKMFEFTGWSLEILRQFPFSSALQRMSVIVKTPGDDSMMAFT
KGAPEMIASLCKPETVPSNFQEVLNEYTKQGFRVIALAYKALESKTWLLQKLSREEVESDLEFLGLIVME
NRLKPETAPVINELNRANIRTVMVTGDNLLTAISVARECGMISPSKKVILIEAVKPEDDDSASLTWTLLL
KGTVFARMSPDQKSELVEELQKLDYTVGMCGDGANDCGALKAADVGISLSEAEASVAAPFTSKVPDISCV
PTVIKEGRAALVTSFSCFKYMALYSLIQFISVLILYSINSNLGDFQFLFIDLVIITPIAVFMSRTGAYPK
LSSKRPPASLVSPPVLVSLLGQIVLILLFQVIGFLIVRQQPWYIPPEPTVDKANTDNSNE
>gnl|CDD|319843 cd07543, P-type_ATPase_cation, P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 (ATP13A1) and Saccharomyces manganese-transporting ATPase 1 Spf1p. Saccharomyces Spf1p may mediate manganese transport into the endoplasmic reticulum (ER); one consequence of deletion of SPF1 is severe ER stress. This subfamily also includes Arabidopsis thaliana MIA (Male Gametogenesis Impaired Anthers) protein which is highly abundant in the endoplasmic reticulum and small vesicles of developing pollen grains and tapetum cells. The MIA gene functionally complements a mutant in the SPF1 from Saccharomyces cerevisiae. The expression of ATP13A1 has been followed during mouse development, ATP13A1 transcript expression showed an increase as development progressed, with the highest expression at the peak of neurogenesis. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
DIAAAKKKYGKNKFDIPVPTFSELFKEHAVAPFFVFQVFCVGLWCLDEYWYYSLFTLFMLVAFEATLVFQ
RMKNLSEFRTMGNKPYTIQVYRDGKWVPISSDELLPGDLVSIGRSAEDNLVPCDLLLLRGSCIVNEAMLT
GESVPLMKEPIEDRDPEDVLDDDGDDKLHVLFGGTKVVQHTPPGKGGLKPPDGGCLAYVLRTGFETSQGK
LLRTILFSTERVTANNLETFIFILFLLVFAIAAAAYVWIEGTKDGRSRYKLFLECTLILTSVVPPELPME
LSLAVNTSLIALAKLYIFCTEPFRIPFAGKVDICCFDKTGTLTSDDLVVEGVAGLNDGKEVIPVSSIEPV
ETILVLASCHSLVKLDDGKLVGDPLEKATLEAVDWTLTKDEKVFPRSKKTKGLKIIQRFHFSSALKRMSV
VASYKDPGSTDLKYIVAVKGAPETLKSMLSDVPADYDEVYKEYTRQGSRVLALGYKELGHLTKQQARDYK
REDVESDLTFAGFIVFSCPLKPDSKETIKELNNSSHRVVMITGDNPLTACHVAKELGIVDKPVLILILSE
EGKSNEWKLIPHVKVFARVAPKQKEFIITTLKELGYVTLMCGDGTNDVGALKHAHVGVALLKLGDASIAA
PFTSKLSSVSCVCHIIKQGRCTLVTTLQMFKILALNCLISAYSLSVLYLDGVKFGDVQATISGLLLAACF
LFISRSKPLETLSKERPLPNIFNLYTILSVLLQFAVHFVSLVYITGEAKELEPPREEVDLEKEFEPSLVN
STVYILSMAQQVATFAVNYKGRPFRESLRENKPL
>gnl|CDD|319844 cd07544, P-type_ATPase_HM, P-type heavy metal-transporting ATPase; uncharacterized subfamily. Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
RKLLAVAALAVIALILCFGLHQPLLAAWIVLIGGVVIALSLLWEMIKTLRRGRYGVDLLAILAIVATLLV
GEYWASLIILLMLTGGEALEDYAQRRASRELTALLDRAPRIAHRLVGGQLEEVPVEEVTVGDRLLVRPGE
VVPVDGEVVSGTATLDESSLTGESKPVSKRPGDRVMSGAVNGDSALTMVATKLAADSQYAGIVRLVKEAQ
ANPAPFVRLADRYAVPFTLLALAIAGVAWAVSGDPVRFAAVLVVATPCPLILAAPVAIVSGMSRSSRRGI
LVKDGGVLEKLARAKTVAFDKTGTLTYGQPKVVDVVPAPGVDADEVLRLAASVEQYSSHVLARAIVAAAR
ERELQLSAVTELTEVPGAGVTGTVDGHEVKVGKLKFVLARGAWAPDIRNRPLGGTAVYVSVDGKYAGAIT
LRDEVRPEAKETLAHLRKAGVERLVMLTGDRRSVAEYIASEVGIDEVRAELLPEDKLAAVKEAPKAGPTI
MVGDGVNDAPALAAADVGIAMGARGSTAASEAADVVILVDDLDRVVDAVAIARRTRRIALQSVLIGMALS
IIGMLIAAFGLIPPVAGALLQEVIDVVSILNALRAL
>gnl|CDD|319845 cd07545, P-type_ATPase_Cd-like, P-type heavy metal-transporting ATPase, similar to Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase. CadA from gram-positive Staphylococcus aureus plasmid pI258 is required for full Cd(2+) and Zn(2+) resistance. This subfamily also includes CadA, from the gram-negative bacilli, Stenotrophomonas maltophilia D457R, which is a cadmium efflux pump acquired as part of a cluster of antibiotic and heavy metal resistance genes from gram-positive bacteria. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
IHFVLGEDALVVIALFLASIVLGGYGLFKKGWRNLIRRNFDMKTLMTIAVIGAALIGEWPEAAMVVFLFA
ISEALEAYSMDRARRSIRSLMDIAPKTALVRRDGQEREVPVAEVAVGDRMIVRPGERIAMDGIIVRGESS
VNQAAITGESLPVEKGVGDEVFAGTLNGEGALEVRVTKPAEDSTIARIIHLVEEAQAERAPTQAFVDRFA
RYYTPVVMAIAALVAIVPPLFFGGAWFTWIYRGLALLVVACPCALVISTPVSIVSAIGNAARKGVLIKGG
VYLEELGRLKTVAFDKTGTLTKGKPVVTDVVVLGGQTEKELLAIAAALEYRSEHPLASAIVKKAEQRGLT
LSAVEEFTALTGRGVRGVVNGTTYYIGSPRLFEELNLSESPALEAKLDALQNQGKTVMILGDGERILGVI
AVADQVRPSSRNAIAALHQLGIKQTVMLTGDNPQTAQAIAAQVGVSDIRAELLPQDKLDAIEALQAEGGR
VAMVGDGVNDAPALAAADVGIAMGAAGTDTALETADIALMGDDLRKLPFAVRLSRKTLAIIKQNIAFALG
IKLIALLLVIPGWLTLWMAVFADMGASLLVTLNSLRLLR
>gnl|CDD|319846 cd07546, P-type_ATPase_Pb_Zn_Cd2-like, P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). Escherichia coli ZntA mediates resistance to toxic levels of selected divalent metal ions. ZntA has the highest selectivity for Pb(2+), followed by Zn(2+) and Cd(2+); it also shows low levels of activity with Cu(2+), Ni(2+), and Co(2+). It is upregulated by the transcription factor ZntR at high zinc concentrations. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
AIAWGLELVNPPLGQWAFIAATLVGLFPIARKAFRLARSGSPFSIETLMTVAAIGALFIGATAEAAMVLL
LFLVGELLEGYAASRARSGVKALMALVPETALREENGERREVPADSLRPGDVIEVAPGGRLPADGELLSG
FASFDESALTGESIPVEKAAGDKVFAGSINVDGVLRIRVTSAPGDNAIDRILHLIEEAEERRAPIERFID
RFSRWYTPAIMAVALLVIVVPPLLFGADWQTWIYRGLALLLIGCPCALVISTPAAITSGLAAAARRGALI
KGGAALEQLGRVTTVAFDKTGTLTRGKPVVTDVVPLTGISEAELLALAAAVEMGSSHPLAQAIVARAQAA
GLTIPPAEEARALVGRGIEGQVDGERVLIGAPKFAADRGTLEVQGRIAALEQAGKTVVVVLANGRVLGLI
ALRDELRPDAAEAVAELNALGIKALMLTGDNPRAAAAIAAELGLDFRAGLLPEDKVKAVRELAQHGPVAM
VGDGINDAPAMKAASIGIAMGSGTDVALETADAALTHNRLGGVAAMIELSRATLANIRQNITIALGLKAV
FLVTTLLGITGLWLAVLADTGATVLVTANALRLLRFR
>gnl|CDD|319847 cd07548, P-type_ATPase-Cd_Zn_Co_like, P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to transport cadmium, zinc and cobalt but not copper out of the cell. Bacillus subtilis CadA/YvgW appears to transport cadmium, zinc and cobalt but not copper, out of the cell. Functions in metal ion resistance and cellular metal ion homeostasis. CadA/YvgW is also important for sporulation in B. subtilis, the significant specific expression of the cadA/yvgW gene during the late stage of sporulation, is controlled by forespore-specific sigma factor, sigma G, and mother cell-specific sigma factor, sigma E. This subfamily also includes Helicobacter pylori CadA an essential resistance pump with ion specificity towards Cd(2+), Zn(2+) and Co(2+), and Zn-transporting ATPase, ZiaA(N) in Synechocystis PCC 6803. Transcription of ziaA is induced by Zn under the control of the Zn responsive repressor ZiaR. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
LIRIIIAIVLFAGALLLKSFLTLSLVLYLIAYLLIGGDVILKAVRNILKGQFFDENFLMSIATLGAFAIG
EYPEAVAVMLFYEVGELFQDLAVERSRKSIKALLDIRPDYANLKRNNELKDVKPEEVQIGDIIVVKPGEK
IPLDGVVLKGESFLDTSALTGESVPVEVKEGSSVLAGFINLNGVLEIKVTKPFKDSAVAKILELVENASA
RKAPTEKFITKFARYYTPIVVFLALLLAVIPPLFSPDGSFSDWIYRALVFLVISCPCALVISIPLGYFGG
IGAASRKGILIKGSNYLEALSQVKTVVFDKTGTLTKGVFKVTEIVPAPGFSKEELLKLAALAESNSNHPI
ARSIQKAYGKMIDPSEIEDYEEIAGHGIRAVVDGKEILVGNEKLMEKFNIEHDEDEIEGTIVHVALDGKY
VGYIVISDEIKEDAKEAIKGLKELGIKNLVMLTGDRKSVAEKVAKKLGIDEVYAELLPEDKVEKVEELKA
ESKGKVAFVGDGINDAPVLARADVGIAMGGLGSDAAIEAADVVLMNDEPSKVAEAIKIARKTRRIVWQNI
ILALGVKAIVLILGALGLATMWEAVFADVGVALLAILNAMRILR
>gnl|CDD|319848 cd07550, P-type_ATPase_HM, P-type heavy metal-transporting ATPase; uncharacterized subfamily. Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
LGLGLSVVATTRFLPPLPVRAAVTLAAAFPVLRRALESLKERRLNVDVLDSLAVLLSLLTGDYLAANTIA
FLLELGELLEDYTARKSEKALLDLLSPQERTVWVERDGVEVEVPADEVQPGDTVVVGAGDVIPVDGTVLS
GEALIDQASLTGESLPVEKREGDLVFASTVVEEGQLVIRAERVGRETRAARIAELIEQSPSLKARIQNYA
ERLADRLVPPTLGLAGLVYALTGDISRAAAVLLVDFSCGIRLSTPVAVLSALNHAARHGILVKGGRALEL
LAKVDTVVFDKTGTLTEGEPEVTAIITFDGRLSEEDLLYLAASAEEHFPHPVARAIVREAEERGIEHPEH
EEVEYIVGHGIASTVDGKRIRVGSRHFMEEEEIILIPEVDELIEDLHAEGKSLLYVAIDGRLIGVIGLSD
PLRPEAAEVIARLRALGGKRIIMLTGDHEQRARALAEQLGIDRYHAEALPEDKAEIVEKLQAEGRTVAFV
GDGINDSPALSYADVGISMRGGTDIARETADVVLLEDDLRGLAEAIELARETMALIKRNIALVVGPNTAV
LAGGVFGLLSPILAAVLHNGTTLLALLNSLRP
>gnl|CDD|319849 cd07551, P-type_ATPase_HM_ZosA_PfeT-like, P-type heavy metal-transporting ATPase, similar to Bacillus subtilis ZosA/PfeT which transports copper, and perhaps zinc under oxidative stress, and perhaps ferrous iron. Bacillus subtilis ZosA/PfeT (previously known as YkvW) transports copper, it may also transport zinc under oxidative stress and may also be involved in ferrous iron efflux. ZosA/PfeT is expressed under the regulation of the peroxide-sensing repressor PerR. It is involved in competence development. Disruption of the zosA/pfeT gene results in low transformability. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
ELIFALLCLALILAGLLLSKLGPQGVPWALFLLAYLIGGYASAKEGIEATLRKKTLNVDLLMILAAIGAA
AIGYWAEGALLIFIFSLSHALEDYAMGRSKRAITALMQLAPETARRIQRDGEIEEVPVEELQIGDRVQVR
PGERVPADGVILSGSSSIDEASITGESIPVEKTPGDEVFAGTINGSGALTVRVTKLSSDTVFAKIVQLVE
EAQSEKSPTQSFIERFERIYVKGVLLAVLLLLLLPPFLLGWTWADSFYRAMVFLVVASPCALVASTPPAT
LSAIANAARQGVLFKGGVHLENLGSVKAIAFDKTGTLTEGKPRVTDVIPAEGVDEEELLQVAAAAESQSE
HPLAQAIVRYAEERGIPRLPAIEVEAVTGKGVTATVDGQTYRIGKPGFFGEVGIPSEAAALAAELESEGK
TVVYVARDDQVVGLIALMDTPRPEAKEAIAALRLGGIKTIMLTGDNERTAEAVAKELGIDEVVANLLPED
KVAIIRELQQEYGTVAMVGDGINDAPALANADVGIAMGAGTDVALETADVVLMKDDLSKLPYAIRLSRKM
RRIIKQNLIFALAVIALLIVANLFGLLNLPLGVVGHEGSTLLVILNGLRLL
>gnl|CDD|319850 cd07552, P-type_ATPase_Cu-like, P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+)-ATPase. Archaeoglobus fulgidus CopB transports Cu(2+) from the cytoplasm to the exterior of the cell using ATP as energy source, it transports preferentially Cu(2+) over Cu(+), it is activated by Cu(2+) with high affinity and partially by Cu(+) and Ag(+). This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
SLILTIPILLLSPMMGTLLPFQVSFPGSDWVVLILATILFFYGGKPFLKGAKDELKSKKPGMMTLIALGI
TVAYVYSVYAFLGNYFGEHGMDFFWELATLIVIMLLGHWIEMKAVMGAGDALKKLAELLPKTAHLVTDGS
IEDVPVSELKVGDVVLVRAGEKIPADGTILEGESSVNESMVTGESKPVEKKPGDEVIGGSVNGNGTLEVK
VTKTGEDSYLSQVMELVAQAQASKSRAENLADKVAGWLFYIALGVGIIAFIIWLILGDLAFALERAVTVL
VIACPHALGLAIPLVVARSTSIAAKNGLLIRNREALERARDIDVVLFDKTGTLTEGKFGVTDVITFDEYD
EDEILSLAAALEAGSEHPLAQAIVSAAKEKGIRPVEVENFENIPGVGVEGTVNGKRYQVVSPKYLKELGL
KYDEELVKRLAQQGNTVSFLIQDGEVIGAIALGDEIKPESKEAIRALKAQGITPVMLTGDNEEVAQAVAE
ELGIDEYFAEVLPEDKAKKVKELQAEGKKVAMVGDGVNDAPALAQADVGIAIGAGTDVAIESADVVLVKS
DPRDIVDFLELAKATYRKMKQNLWWGAGYNVIAIPLAAGVLAPIGIILSPAVGAVLMSLSTVIVAINAMT
LK
>gnl|CDD|319851 cd07553, P-type_ATPase_HM, P-type heavy metal-transporting ATPase; uncharacterized subfamily. Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle
AGACAGNIMLYSFPVYLGMTPDFLVAPFFRWLSSAFALPSMLYCGSYFYGKAWKSAKQGIPHIDLPIALG
IVIGFVVSWYGLIKGDGLVYFDSLSVLVFLMLVGRWLQVVTQERNRNRLADSRLEAPITEIETGSGSRIK
TRADQIKSGDVYLVASGQRVPVDGKLLSEQASIDMSWLTGESLPRIVERGDKVPAGTSLENQAFEIRVEH
SLAESWSGSILQKVEAQEARKTPRDLLADKIIHYFTVIALLIAVAGFGVWLAIDLSIALKVFTSVLIVAC
PCALALATPFTDEIALARLKKKGVLIKNASSLERLSRVRTIVFDKTGTLTRGKSSFVMVNPEGIDRLALR
AISAIEAHSRHPISRAIREHLMAKGLIKAGASELVEIVGKGVSGNSSGSLWKLGSAPDACGIQESGVVIA
RDGRQLLDLSFNDLLRPDSNREIEELKKGGLSIAILSGDNEEKVRLVGDSLGLDPRQLFGNLSPEEKLAW
IESHSPENTLMVGDGANDALALASAFVGIAVAGEVGVSLEAADIYYAGNGIGGIRDLLTLSKQTIKAIKG
LFAFSLLYNLVAIGLALSGWISPLVAAILMPLSSITILGIVWAALGFRSK
>gnl|CDD|143637 cd07556, Nucleotidyl_cyc_III, Class III nucleotidyl cyclases. Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways
PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFA
EDMREAVSALNQSEGNPVRVRIGIHTGPVVVGVIGSRPQYDVWGALVNLASRMESQAKAGQVL
>gnl|CDD|143638 cd07557, trimeric_dUTPase, Trimeric dUTP diphosphatases. Trimeric dUTP diphosphatases, or dUTPases, are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface
AGYDLRLGEDFEGIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLARKGITVHNAGVIDPGYRGEITLE
LYNLGPEPVVIKKGDRIAQLVF
>gnl|CDD|143471 cd07559, ALDH_ACDHII_AcoD-like, Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like. Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences
YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIA
DRIEENLELLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVV
GQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLA
SHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAMDADDDFDDKAEEGQLGFAFNQG
EVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLT
GGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRD
INRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILVSY
>gnl|CDD|143476 cd07560, Peptidase_S41_CPP, C-terminal processing peptidase; serine protease family S41. The C-terminal processing peptidase (CPP, EC 3.4.21.102) also known as tail-specific protease (tsp), the photosystem II D1 C-terminal processing protease (D1P), and other related S41 protease family members are present in this CD. CPP is synthesized as a precursor form with a carboxyl-terminal extension. It specifically recognizes a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. The C-terminal carboxylate group is essential, and proteins where this group is amidated are not substrates. This family of proteases contains the PDZ domain that promotes protein-protein interactions and is important for substrate recognition. The active site consists of a serine/lysine catalytic dyad. The bacterial CCP-1 is believed to be important for the degradation of incorrectly synthesized proteins as well as protection from thermal and osmotic stresses. In E. coli, it is involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II, allowing the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation
LSEALKKLEEVLELIKKNYVDPVDDEKLIEGAIKGMLSSLDPYSRYLTPIGYIRITSFSENTAEELKKAL
KELKKQGMKGLILDLRNNPGGLLDEAVEIADLFLPGGPIVSTKGRNGKREAYASDDGGLYDGPLVVLVNG
GSASASEIVAGALQDNGRAVLVGERTFGKGSVQTVFPLSDGSALKLTTAKYYTPSGRSIQKKGIEPDIEV
P
>gnl|CDD|143477 cd07561, Peptidase_S41_CPP_like, C-terminal processing peptidase-like; serine protease family S41. Bacterial protease homologs of the S41 family related to C-terminal processing peptidase (CPP). CPP-1 is believed to be important for the degradation of incorrectly synthesized proteins as well as protection from thermal and osmotic stresses. CPP is synthesized with an extension on its carboxyl-terminus and specifically recognizes a C-terminal tripeptide, but cleaves at variable distance from the C-terminus. The CPP active site consists of a serine/lysine catalytic dyad. Conservation of these residues is seen in the CPP-like proteins of this group. CPP proteins contain a PDZ domain that promotes protein-protein interactions and is important for substrate recognition however, most of CPP-like proteins only have an internal fragment or lack the PDZ domain
GEYYALEEVNQWIYDVMREWYLWYDDIPALDDLDYFDDPEDFLESLLSEKDGKDRFSYIVDGGKKVGYLV
YNSFTSGYDDELNQAFAEFKAQGVTELVLDLRYNGGGLVSSANLLASLLAPAVALGQVFATLEYNDKRSA
NNEDLLFSSKTLAGGNSLNLSKVYVLTSGSTASASELVINSLKPYMDVVLIGETTYGKNVGSLTFEDDRK
HKWALQPVVFKVVNADGQGDYSNGLTPDIEVNEDSSNLLPLGDPNE
>gnl|CDD|143478 cd07562, Peptidase_S41_TRI, Tricorn protease; serine protease family S41. The tricorn protease (TRI), a member of the S41 peptidase family and named for its tricorn-like shape, exists only in some archaea and eubacteria. It has been shown to act as a carboxypeptidase, involved in the degradation of proteasomal products to preferentially yield di- and tripeptides, with subsequent and final degradations to free amino acid residues by tricorn interacting factors, F1, F2 and F3. Tricorn is a hexameric D3-symmetric protease of 720kD, and can self-associate further into a giant icosahedral capsid structure containing twenty copies of the complex. Each tricorn peptidase monomer consists of five structural domains: a six-bladed beta-propeller and a seven-bladed beta-propeller that limit access to the active site, the two domains (C1 and C2) that carry the active site residues, and a PDZ-like domain (proposed to be important for substrate recognition) between the C1 and C2 domains. The active site tetrad residues are distributed between the C1 and C2 domains, with serine and histidine on C1 and serine and glutamate on C2
EWLQMFDEAWRLVRDNFYDPDMHGVDWDAVRAEYRPLLPRAATRAELADVLNEMLGELNDSHTGVSGLRY
RDWVESNREYVEELSDGRIGYVHIPDMGDDGFAEFLRDLLAEVDKDGLIIDVRFNGGGNVADLLLDFLSR
RRYGYDIPRGGGKPVTYPSGRWRGPVVVLVNEGSASDAEIFAYGFRALGLGPVVGTRTAGGVIISGRYRL
PDGGSLTVPEFGVYLPDGGPLENRGVAPDIEVENTPEDVAAGRDPQLEAAIEELLK
>gnl|CDD|143479 cd07563, Peptidase_S41_IRBP, Interphotoreceptor retinoid-binding protein; serine protease family S41. Interphotoreceptor retinoid-binding protein (IRBP) is a homolog of the S41 protease, C-terminal processing peptidase (CTPase) family. It is thought to facilitate the compartmentalization of the visual cycle that requires poorly soluble and potentially toxic retinoids to cross the aqueous subretinal space between the photoreceptors and the retinal pigment epithelium (RPE). IRBP is secreted by photoreceptors into the interphotoreceptor matrix (IPM) where it is rapidly turned over by a combination of RPE and photoreceptor endocytosis. It is the most abundant soluble protein component of the IPM, consisting of homologous modules, each repeat structure arising through the duplication (as in teleost IRBP) or quadruplication (in tetrapods) of an ancient gene, arisen in the early evolution of the vertebrate eye. IRBP has been shown to promote the release of all-trans retinol from photoreceptors and facilitates its delivery to the RPE. Conversely, IRBP can promote the release of 11-cis-retinal from the RPE, prevent its isomerization in the subretinal space, and transfer it to photoreceptors. In vivo evidence implicates IRBP as a retinoid transporter in the visual cycle, suggesting a critical role for IRBP in cone function essential for human vision. IRBP is a dominant autoimmune antigen in the eye; IRBP proteolysis analysis has proven a useful biomarker for autoimmune uveitis (AU) disorders, a major cause of blindness. This family also includes a chlamydia-secreted protein, designated chlamydia protease-like activity factor (CPAF), known to degrade host proteins, enabling Chlamydia to evade host defenses and replicate
VFEALAKLLEENYAFPEAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQELGDGHLNVSYIGYLRI
DSFGGFEIAAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASYFTDEDKPVHLYTIYKRPGNTT
TELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPVLPFPLPNGLYL
TVPTSRSVDPITGTNWEGVGVPPDIEVPATPGYDDALERA
>gnl|CDD|143588 cd07564, nitrilases_CHs, Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases). Nitrilases (nitrile aminohydrolases, EC:3.5.5.1) hydrolyze nitriles (RCN) to ammonia and the corresponding carboxylic acid. Most nitrilases prefer aromatic nitriles, some prefer arylacetonitriles and others aliphatic nitriles. This group includes the nitrilase cyanide dihydratase (CDH), which hydrolyzes inorganic cyanide (HCN) to produce formate. It also includes cyanide hydratase (CH), which hydrolyzes HCN to formamide. This group includes four Arabidopsis thaliana nitrilases (Ath)NIT1-4. AthNIT1-3 have a strong substrate preference for phenylpropionitrile (PPN) and other nitriles which may originate from the breakdown of glucosinolates. The product of PPN hydrolysis, phenylacetic acid has auxin activity. AthNIT1-3 can also convert indoacetonitrile to indole-3-acetic acid (IAA, auxin), but with a lower affinity and velocity. From their expression patterns, it has been speculated that NIT3 may produce IAA during the early stages of germination, and that NIT3 may produce IAA during embryo development and maturation. AthNIT4 has a strong substrate specificity for the nitrile, beta-cyano-L-alanine (Ala(CN)), an intermediate of cyanide detoxification. AthNIT4 has both a nitrilase activity and a nitrile hydratase (NHase) activity, which generate aspartic acid and asparagine respectively from Ala(CN). NHase catalyzes the hydration of nitriles to their corresponding amides. This subgroup belongs to a larger nitrilase superfamily comprised of belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 1
VKVAAVQAAPVFLDLAATVEKACRLIEEAAANGAQLVVFPEAFIPGYPYWIWFGAPAEGRELFARYYENS
VEVDGPELERLAEAARENGIYVVLGVSERDGGTLYNTQLLIDPDGELLGKHRKLKPTHAERLVWGQGDGS
GLRVVDTPIGRLGALICWENYMPLARYALYAQGEQIHVAPWPDFSPYYLSREAWLAASRHYALEGRCFVL
SACQVVTEEDIPADCEDDEEADPLEVLGGGGSAIVGPDGEVLAGPLPDEEGILYADIDLDDIVEAKLDFD
PVGHYSRPDVFSLTVDR
>gnl|CDD|143589 cd07565, aliphatic_amidase, aliphatic amidases (class 2 nitrilases). Aliphatic amidases catalyze the hydrolysis of short-chain aliphatic amides to form ammonia and the corresponding organic acid. This group includes Pseudomonas aeruginosa (Pa) AmiE, the amidase from Geobacillus pallidus RAPc8 (RAPc8 amidase), and Helicobacter pylori (Hp) AmiE and AmiF. PaAimE and HpAmiE hydrolyze various very short aliphatic amides, including propionamide, acetamide and acrylamide. HpAmiF is a formamidase which specifically hydrolyzes formamide. These proteins belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 2. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. HpAmiE, HpAmiF, and RAPc8 amidase, and PaAimE appear to be homohexameric enzymes, trimer of dimers
VGVAVVQYKVPVLHTKEEVLENAERIADMVEGTKRGLPGMDLIVFPEYSTQGLMYDKWTMDETACTVPGP
ETDIFAEACKEAKVWGVFSIMERNPDHGKNPYNTAIIIDDQGEIVLKYRKLHPWVPIEPWYPGDLGTPVC
EGPKGSKIALIICHDGMYPEIARECAYKGAELIIRIQGYMYPAKDQWIITNKANAWCNLMYTASVNLAGF
DGVFSYFGESMIVNFDGRTLGEGGREPDEIVTAELSPSLVRDARKNWGSENNLYKLGHRGYVAVPGGAAD
CPYTFYKDLVE
>gnl|CDD|143590 cd07566, ScNTA1_like, Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases). Saccharomyces cerevisiae NTA1 functions in the N-end rule protein degradation pathway. It specifically deaminates the N-terminal asparagine and glutamine residues of substrates of this pathway, to aspartate and glutamate respectively, these latter are the destabilizing residues. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 3
RIACLQLNPQIGQVEENLSRAWELLDKTKKRAKLKKPDILVLPELALTGYNFHSLEHIKPYLEPTTSGPS
FEWAREVAKKFNCHVVIGYPEKVDESSPKLYNSALVVDPEGEVVFNYRKSFLYYTDEEWGCEENPGGFQT
FPLPFAKDDDFDGGSVDVTLKTSIGICMDLNPYKFEAPFTDFEFATHVLDNGTELIICPMAWLHSLSPTE
LTVLPQEPDTETVSYWLQRFEPLRAEPLEGTQVVFCNRIGTENDTLYAGSSAVIGIYDGLDSPDGSNGNY
WKLRFDPFLDLKERL
>gnl|CDD|143591 cd07567, biotinidase_like, biotinidase and vanins (class 4 nitrilases). These secondary amidases participate in vitamin recycling. Biotinidase (EC 3.5.1.12) has both a hydrolase and a transferase activity. It hydrolyzes free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin to acceptor molecules such as histones. Biotinidase deficiency in humans is an autosomal recessive disorder characterized by neurological and cutaneous symptoms. This subgroup includes the three human vanins, vanin1-3. Vanins are ectoenzymes, Vanin-1, and -2 are membrane associated, vanin-3 is secreted. They are pantotheinases (EC 3.5.1.92, pantetheine hydrolase), which convert pantetheine, to pantothenic acid (vitamin B5) and cysteamine (2-aminoethanethiol, a potent anti-oxidant). They are potential targets for therapeutic intervention in inflammatory disorders. Vanin-1 deficient mice lacking free cysteamine are less susceptible to intestinal inflammation, and expression of vanin-1 and -3 is induced as part of the inflammatory-regenerative differentiation program of human epidermis. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 4. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer
YIAAVVEHHPILSPDPDALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPD
PEVNWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGT
LIARYRKYNLFGEPGFDVPPEPEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSE
LPFLTAVQIQQAWAYANGVNLLAANYNNPSAGMTGSGIYAGRSGALVYHYDNEPGGKLLVAEVPKLPSRR
PTELEAKVDTSSLPSSLKN
>gnl|CDD|143592 cd07568, ML_beta-AS_like, mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases). This family includes mammalian-like beta-AS (EC 3.5.1.6, also known as beta-ureidopropionase or N-carbamoyl-beta-alanine amidohydrolase). This enzyme catalyzes the third and final step in the catabolic pyrimidine catabolic pathway responsible for the degradation of uracil and thymine, the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the beta-amino acids, beta-alanine and beta-aminoisobutyrate respectively. This family belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 5. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Beta-ASs from this subgroup are found in various oligomeric states, dimer (human), hexamer (calf liver), decamer (Arabidopsis and Zea mays), and in the case of Drosophila melanogaster beta-AS, as a homooctamer assembled as a left-handed helical turn, with the possibility of higher order oligomers formed by adding dimers at either end. Rat beta-AS changes its oligomeric state (hexamer, trimer, dodecamer) in response to allosteric effectors. Eukaryotic Saccharomyces kluyveri beta-AS belongs to a different superfamily
SRIVRVGLIQASNVIPTDAPIEKQKEAMIQKHVTMIREAAEAGAQIVCLQEIFYGPYFCAEQDTKWYEFA
EEIPNGPTTKRFAALAKEYNMVLILPIYEKEQGGTLYNTAAVIDADGTYLGKYRKNHIPHVGGFWEKFYF
RPGNLGYPVFDTAFGKIGVYICYDRHFPEGWRALGLNGAEIVFNPSATVAGLSEYLWKLEQPAAAVANGY
FVGAINRVGTEAPWNIGEFYGSSYFVDPRGQFVASASRDKDELLVAELDLDLIREVRDTWQFYRDRRPET
YGELTKL
>gnl|CDD|143593 cd07569, DCase, N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases). DCase hydrolyses N-carbamyl-D-amino acids to produce D-amino acids. It is an important biocatalyst in the pharmaceutical industry, producing useful D-amino acids for example in the preparation of beta-lactam antibiotics. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 6. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Agrobacterium radiobacter DCase forms a tetramer (dimer of dimers). Some DCases may form trimers
SRQVILAAAQMGPIARAETRESVVARLIALLEEAASRGAQLVVFPELALTTFFPRWYFPDEAELDSFFET
EMPNPETQPLFDRAKELGIGFYLGYAELTEDGGVKRRFNTSILVDKSGKIVGKYRKVHLPGHKEPEPYRP
FQHLEKRYFEPGDLGFPVFRVPGGIMGMCICNDRRWPETWRVMGLQGVELVLLGYNTPTHNPPAPEHDHL
RLFHNLLSMQAGAYQNGTWVVAAAKAGMEDGCDLIGGSCIVAPTGEIVAQATTLEDEVIVADCDLDLCRE
GRETVFNFARHRRPEHYGLIAE
>gnl|CDD|143594 cd07570, GAT_Gln-NAD-synth, Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases (class 7 and 8 nitrilases). Glutamine-dependent NAD synthetases are bifunctional enzymes, which have an N-terminal GAT domain and a C-terminal NAD+ synthetase domain. The GAT domain is a glutaminase (EC 3.5.1.2) which hydrolyses L-glutamine to L-glutamate and ammonia. The ammonia is used by the NAD+ synthetase domain in the ATP-dependent amidation of nicotinic acid adenine dinucleotide. Glutamine aminotransferases are categorized depending on their active site residues into different unrelated classes. This class of GAT domain belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to classes 7 and 8. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase forms a homooctamer
RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEDLLLRPDFLEAAEEALEELAA
ATADLDIAVVVGLPLRHDGKLYNAAAVLQNGKILGVVPKQLLPNYGVFDEKRYFTPGDKPDVLFFKGLRI
GVEICEDLWVPDPPSAELALAGADLILNLSASPFHLGKQDYRRELVSSRSARTGLPYVYVNQVGGQDDLV
FDGGSFIADNDGELLAEAPRFEEDLADVDLDRLRSERRRNSSFLDEEAEIY
>gnl|CDD|143595 cd07571, ALP_N-acyl_transferase, Apolipoprotein N-acyl transferase (class 9 nitrilases). ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 9
LRVALVQGNIPQDEKWDPEQRQATLDRYLDLTRELADEKPDLVVWPETALPFDLQRDPDALARLARAARA
VGAPLLTGAPRREPGGGRYYNSALLLDPGGGILGRYDKHHLVPFGEYVPLRDLLRFLGLLFDLPMGDFSP
GTGPQPLLLGGGVRVGPLICYESIFPELVRDAVRQGADLLVNITNDAWFGDSAGPYQHLAMARLRAIETG
RPLVRAANTGISAVIDPDGRIVARLPLFEAGVLVAEVPLRTGLTPYVRWGDWPLLLLLLL
>gnl|CDD|143596 cd07572, nit, Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases). This subgroup includes mammalian Nit1 and Nit2, the Nit1-like domain of the invertebrate NitFhit, and various uncharacterized bacterial and archaeal Nit-like proteins. Nit1 and Nit2 are candidate tumor suppressor proteins. In NitFhit, the Nit1-like domain is encoded as a fusion protein with the non-homologous tumor suppressor, fragile histidine triad (Fhit). Mammalian Nit1 and Fhit may affect distinct signal pathways, and both may participate in DNA damage-induced apoptosis. Nit1 is a negative regulator in T cells. Overexpression of Nit2 in HeLa cells leads to a suppression of cell growth through cell cycle arrest in G2. These Nit proteins and the Nit1-like domain of NitFhit belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 10
RVALIQMTSTADKEANLARAKELIEEAAAQGAKLVVLPECFNYPGGTDAFKLALAEEEGDGPTLQALSEL
AKEHGIWLVGGSIPERDDDDGKVYNTSLVFDPDGELVARYRKIHLFDVDVPGGISYRESDTLTPGDEVVV
VDTPFGKIGLGICYDLRFPELARALARQGADILTVPAAFTMTTGPAHWELLLRARAIENQCYVVAAAQAG
DHEAGRETYGHSMIVDPWGEVLAEAGEGEGVVVAEIDLDRLEEVRRQIPVLKHRR
>gnl|CDD|143597 cd07573, CPA, N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases). CPA (EC 3.5.1.53, also known as N-carbamoylputrescine amidase and carbamoylputrescine hydrolase) converts N-carbamoylputrescine to putrescine, a step in polyamine biosynthesis in plants and bacteria. This subgroup includes Arabidopsis thaliana CPA, also known as nitrilase-like 1 (NLP1), and Pseudomonas aeruginosa AguB. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 11. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer; P. aeruginosa AugB is a homohexamer, Arabidopsis thaliana NLP1 is a homooctomer
VTVALVQMACSEDPEANLAKAEELVREAAAQGAQIVCLQELFETPYFCQEEDEDYFDLAEPPIPGPTTAR
FQALAKELGVVIPVSLFEKRGNGLYYNSAVVIDADGSLLGVYRKMHIPDDPGYYEKFYFTPGDTGFKVFD
TRYGRIGVLICWDQWFPEAARLMALQGAEILFYPTAIGSEPQEPPEGLDQRDAWQRVQRGHAIANGVPVA
AVNRVGVEGDPGSGITFYGSSFIADPFGEILAQASRDEEEILVAEFDLDEIEEVRRAWPFFRDRRPDLYG
ALTK
>gnl|CDD|143598 cd07574, nitrilase_Rim1_like, Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an N-terminal RimI domain (class 12 nitrilases). Some members of this subgroup are implicated in post-translational modification, as they contain an N-terminal GCN5-related N-acetyltransferase (GNAT) protein RimI family domain. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 12. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer
VRVAAAQYPLRRYASFEEFAAKVEYWVAEAAGYGADLLVFPEYFTMELLSLLPEAIDGLDEAIRALAALT
PDYVALFSELARKYGINIIAGSMPVREDGRLYNRAYLFGPDGTIGHQDKLHMTPFEREEWGISGGDKLKV
FDTDLGKIGILICYDSEFPELARALAEAGADLLLVPSCTDTRAGYWRVRIGAQARALENQCYVVQSGTVG
NAPWSPAVDVNYGQAAVYTPCDFGFPEDGILAEGEPNTEGWLIADLDLEALRRLREEGSVRNLRDWREDL
>gnl|CDD|143599 cd07575, Xc-1258_like, Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases). Uncharacterized subgroup belonging to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup either represents a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. XC1258 is a homotetramer
LKIALIQTDLVWEDPEANLAHFEEKIEQLKEKTDLIVLPEMFTTGFSMNAEALAEPMNGPTLQWMKAQAK
KKGAAITGSLIIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVC
YDLRFPVWSRNTNDYDLLLYVANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVID
PLGEPLAEAEEDEGVLTATLDKEALQEFREKFPFLKDADSFT
>gnl|CDD|143600 cd07576, R-amidase_like, Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases). Pseudomonas sp. MCI3434 R-amidase hydrolyzes (R,S)-piperazine-2-tert-butylcarboxamide to form (R)-piperazine-2-carboxylic acid. It does so with strict R-stereoselectively. Its preferred substrates are carboxamide compounds which have the amino or imino group connected to their beta- or gamma-carbon. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group. It has been suggested that this subgroup represents a new class. Members of the nitrilase superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Native R-amidase however appears to be a monomer
RLALYQGPARDGDVAANLARLDEAAARAAAAGADLLVFPELFLTGYNIGDAVARLAEPADGPALQALRAI
ARRHGIAIVVGYPERAGGAVYNAAVLIDEDGTVLANYRKTHLFGDSERAAFTPGDRFPVVELRGLRVGLL
ICYDVEFPELVRALALAGADLVLVPTALMEPYGFVARTLVPARAFENQIFVAYANRCGAEDGLTYVGLSS
IAGPDGTVLARAGRGEALLVADLDPAALAAARRENPYLADRRPE
>gnl|CDD|143601 cd07577, Ph0642_like, Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases). Uncharacterized subgroup of the nitrilase superfamily. This superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. Pyrococcus horikoshii Ph0642 is a hypothetical protein belonging to this subgroup. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). This subgroup was classified as belonging to class 13, which represents proteins that at the time were difficult to place in a distinct similarity group. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer
KVGYVQFNPKFGEVEKNLKKVESLIKGVEADLIVLPELFNTGYAFTSKEEVASLAESIPDGPTTRFLQEL
ARETGAYIVAGLPERDGDKFYNSAVVVGPEGYIGIYRKTHLFYEEKLFFEPGDTGFRVFDIGDIRIGVMI
CFDWYFPEAARTLALKGADIIAHPANLVLPYCPKAMPIRALENRVFTITANRIGTEERGGETLRFIGKSQ
ITSPKGEVLARAPEDGEEVLVAEIDPRLARDKRINEENDIFKDRRPEFY
>gnl|CDD|143602 cd07578, nitrilase_1_R1, First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). Members of this subgroup have two nitrilase domains. This is the first of those two domains. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer
YKAAAIQFEPEMGEKERNIERLLALCEEAARAGARLIVTPEMATTGYCWYDRAEIAPFVEPIPGPTTARF
AELAREHDCYIVVGLPEVDSRSGIYYNSAVLIGPSGVIGRHRKTHPYISEPKWAADGDLGHQVFDTEIGR
IALLICMDIHFFETARLLALGGADVICHISNWLAERTPAPYWINRAFENGCYLIESNRWGLERGVQFSGG
SCIIEPDGTIQASIDSGDGVALGEIDLDRARHRQFPGELVFTARRPEL
>gnl|CDD|143603 cd07579, nitrilase_1_R2, Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). Members of this subgroup have two nitrilase domains. This is the second of those two domains. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer
RIAVAQFAPTPDIAGNLATIDRLAAEAKATGAELVVFPELALTGLDDPASEAESDTGPAVSALRRLARRL
RLYLVAGFAEADGDGLYNSAVLVGPEGLVGTYRKTHLIEPERSWATPGDTWPVYDLPLGRVGLLIGHDAL
FPEAGRVLALRGCDLLACPAAIAIPFVGAHAGTSVPQPYPIPTGADPTHWHLARVRAGENNVYFAFANVP
DPARGYTGWSGVFGPDTFAFPRQEAAIGDEEGIAWALIDTSNLDSRYPTNVVRRKDLVRMRQPHWYAPL
>gnl|CDD|143604 cd07580, nitrilase_2, Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer
RVACVQFDPRVGDLDANLARSIELIREAADAGANLVVLPELANTGYVFESRDEAFALAEEVPDGASTRAW
AELAAELGLYIVAGFAERDGDRLYNSAVLVGPDGVIGTYRKAHLWNEEKLLFEPGDLGLPVFDTPFGRIG
VAICYDGWFPETFRLLALQGADIVCVPTNWVPMPRPPEGGPPMANILAMAAAHSNGLFIACADRVGTERG
QPFIGQSLIVGPDGWPLAGPASGDEEEILLADIDLTAARRKRIWNSNDVLRDRRPDLY
>gnl|CDD|143605 cd07581, nitrilase_3, Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer
VALAQFASSGDKEENLEKVRRLLAEAAAAGADLVVFPEYTMARFGDGLDDYARVAEPLDGPFVSALARLA
RELGITVVAGMFEPAGDGRVYNTLVVVGPDGEIIAVYRKIHLYDAFGFRESDTVAPGDELPPVVFVVGGV
KVGLATCYDLRFPELARALALAGADVIVVPAAWVAGPGKEEHWETLLRARALENTVYVAAAGQAGPRGIG
RSMVVDPLGVVLADLGEREGLLVADIDPERVEEAREALPVLENRR
>gnl|CDD|143606 cd07582, nitrilase_4, Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer
YTALALQPTCEAAEDRADILANIDRINEQIDAAVGFSGPGLPVRLVVLPEYALQGFPMGEPREVWQFDKA
AIDIPGPETEALGEKAKELNVYIAANAYERDPDFPGLYFNTAFIIDPSGEIILRYRKMNSLAAEGSPSPH
DVWDEYIEVYGYGLDALFPVADTEIGNLGCLACEEGLYPEVARGLAMNGAEVLLRSSSEVPSVELDPWEI
ANRARALENLAYVVSANSGGIYGSPYPADSFGGGSMIVDYKGRVLAEAGYGPGSMVAGAEIDIEALRRAR
ARPGMHNWLKDLRT
>gnl|CDD|143607 cd07583, nitrilase_5, Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer
KIALIQLDIVWGDPEANIERVESLIEEAAAAGADLIVLPEMWNTGYFLDDLYELADEDGGETVSFLSELA
KKHGVNIVAGSVAEKEGGKLYNTAYVIDPDGELIATYRKIHLFGLMGEDKYLTAGDELEVFELDGGKVGL
FICYDLRFPELFRKLALEGAEILFVPAEWPAARIEHWRTLLRARAIENQAFVVACNRVGTDGGNEFGGHS
MVIDPWGEVLAEAGEEEEILTAEIDLEEVAEVRKKIPVFKDRR
>gnl|CDD|143608 cd07584, nitrilase_6, Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer
KVALIQMDSVLGDVKANLKKAAELCKEAAAEGADLICFPELATTGYRPDLLGPKLWELSEPIDGPTVRLF
SELAKELGVYIVCGFVEKGGVPGKVYNSAVVIDPEGESLGVYRKIHLWGLEKQYFREGEQYPVFDTPFGK
IGVMICYDMGFPEVARILTLKGAEVIFCPSAWREQDADIWDINLPARALENTVFVAAVNRVGNEGDLVLF
GKSKILNPRGQVLAEASEEAEEILYAEIDLDAIADYRMTLPYLKDRKP
>gnl|CDD|143609 cd07585, nitrilase_7, Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer
RIALVQFEARVGDKARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVRALSREAEVPDGPSTQALSDL
ARRYGLTILAGLIEKAGDRPYNTYLVCLPDGLVHRYRKLHLFRREHPYIAAGDEYPVFATPGVRFGILIC
YDNHFPENVRATALLGAEILFAPHATPGTTSPKGREWWMRWLPARAYDNGVFVAACNGVGRDGGEVFPGG
AMILDPYGRVLAETTSGGDGMVVADLDLDLINTVRGRRWISFLRARRPELY
>gnl|CDD|143610 cd07586, nitrilase_8, Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer
RVAIAQIDPVLGDVEENLEKHLEIIETARERGADLVVFPELSLTGYNLGDLVYEVAMHADDPRLQALAEA
SGGICVVFGFVEEGRDGRFYNSAAYLEDGRVVHVHRKVYLPTYGLFEEGRYFAPGSHLRAFDTRFGRAGV
LICEDAWHPSLPYLLALDGADVIFIPANSPARGVGGDFDNEENWETLLKFYAMMNGVYVVFANRVGVEDG
VYFWGGSRVVDPDGEVVAEAPLFEEDLLVAELDRSAIRRARFFSPTFRDEDIRLVLSEL
>gnl|CDD|143611 cd07587, ML_beta-AS, mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases). This subgroup includes mammalian-like beta-AS (EC 3.5.1.6, also known as beta-ureidopropionase or N-carbamoyl-beta-alanine amidohydrolase). This enzyme catalyzes the third and final step in the catabolic pyrimidine catabolic pathway responsible for the degradation of uracil and thymine, the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the beta-amino acids, beta-alanine and beta-aminoisobutyrate respectively. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 5. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Beta-ASs from this subgroup are found in various oligomeric states, dimer (human), hexamer (calf liver), decamer (Arabidopsis and Zea mays), and in the case of Drosophila melanogaster beta-AS, as a homooctamer assembled as a left-handed helical turn, with the possibility of higher order oligomers formed by adding dimers at either end. Rat beta-AS changes its oligomeric state (hexamer, trimer, dodecamer) in response to allosteric effectors. Eukaryotic Saccharomyces kluyveri beta-AS belongs to a different superfamily
LEDLLEKHLPPEELKEVKRILYGEEVKPLELPESALDLAKENDFELKGYKFEAAPEQTRPPRIVRVGLIQ
NKIVLPTTAPIAEQREAIHDRIKKIIEAAAMAGVNIICFQEAWTMPFAFCTREKLPWCEFAESAEDGPTT
KFCQELAKKYNMVIVSPILERDEEHGDTIWNTAVVISNSGNVLGKSRKNHIPRVGDFNESTYYMEGNTGH
PVFETQFGKIAVNICYGRHHPLNWLMYGLNGAEIVFNPSATVGALSEPMWPIEARNAAIANSYFTVGINR
VGTEVFPNEFTSGDGKPAHKDFGHFYGSSYVAAPDGSRTPGLSRTRDGLLVAELDLNLCRQVKDKWGFRM
TARYEMYADFLAK
>gnl|CDD|153272 cd07588, BAR_Amphiphysin, The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Amphiphysins function primarily in endocytosis and other membrane remodeling events. They contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. This subfamily is composed of different isoforms of amphiphysin and Bridging integrator 2 (Bin2). Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin and synaptojanin. They function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. Bin2 is mainly expressed in hematopoietic cells and is upregulated during granulocyte differentiation. The N-BAR domains of amphiphysins form a curved dimer with a positively-charged concave face that can drive membrane bending and curvature
QKLGKADETRDEVFDEHVNNFNKQQASANRLQKDLKNYLNSVRAMKQASKTLSETLKELYEPDWPGREHL
ASIFEQLDLLWNDLEEKLSDQVLGPLTAYQSQFPEVKKRIAKRGRKLVDYDSARHNLEALKAKKKVDDQK
LTKAEEELQQAKKVYEELNTELHEELPALYDSRIAFYVDTLQSIFAAESVFHKEIGKVNTKLNDVMDGLA
D
>gnl|CDD|153273 cd07589, BAR_DNMBP, The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin Binding Protein. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. DyNamin Binding Protein (DNMBP), also called Tuba, is a Cdc42-specific Guanine nucleotide Exchange Factor (GEF) that binds dynamin and various actin regulatory proteins. It serves as a link between dynamin function, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. DNMBP contains BAR and SH3 domains as well as a Dbl Homology domain (DH domain), which harbors GEF activity. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of DNMBP may be involved in binding to membranes. The gene encoding DNMBP is a candidate gene for late onset Alzheimer's disease
QTKDKEFDELEKKFGSLEKQVQLVVRNVELYLQHVQESVLVKVLALEVVLDLYPSNHPRLESKWERFRRV
VRGISSKALPEFKSRVRKLVIEPLSSLLKLFSGPQKLIQKRYDKLLDYERYKEKKERGGKVDEELEEAAN
QYEALNAQLKEELPKFNQLTAQLLETCLKSFVELQRDLYDTLLKRAELLPLLDSS
>gnl|CDD|153274 cd07590, BAR_Bin3, The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 3 (Bin3) is widely expressed in many tissues except in the brain. It plays roles in regulating filamentous actin localization and in cell division. In humans, the Bin3 gene is located in chromosome 8p21.3, a region that is implicated in cancer suppression. Homozygous inactivation of the Bin3 gene in mice led to the development of cataracts and an increased likelihood of lymphomas during aging, suggesting a role for Bin3 in lens development and cancer suppression. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
KKPILSKTVDRELEREVQKLQQLESTTKKLYKDMKKYIEAVLALSKAEQRLSQDLASGPLCEDNDELRNL
VEALDSVTTQLDKTVQELVNLIQKTFIEPLKRLRSVFPSVNAAIKRREQSLQEYERLQAKVEKLAEKEKT
GPNLAKLEQAEKALAAARADFEKQNIKLLEELPKFYNGRTDYFQPCFEALIKSQVLYYSQSTKIFTQLAP
NLDNPIEQLTISEQE
>gnl|CDD|153275 cd07591, BAR_Rvs161p, The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 161 and similar proteins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 161 (Rvs161p) and Schizosaccharomyces pombe Hob3 (homolog of Bin3). S. cerevisiae Rvs161p plays a role in regulating cell polarity, actin cytoskeleton polarization, vesicle trafficking, endocytosis, bud formation, and the mating response. It forms a heterodimer with another BAR domain protein Rvs167p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. S. pombe Hob3 is important in regulating filamentous actin localization and may be required in activating Cdc42 and recruiting it to cell division sites. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
KTGQVERTVDREFEFEERRYRTMEKASTKLQKEAKGYLDSLRALTSSQARIAETISSFYGDAGDKDGAML
SQEYKQAVEELDAETVKELDGPYRQTVLDPIGRFNSYFPEINEAIKKRNHKLLDYDAARAKVRKLIDKPS
EDPTKLPRAEKELDEAKEVYETLNDQLKTELPQLVDLRIPYLDPSFEAFVKIQLRFFTEGYERLAQVQRY
LDAQTREDYANGQL
>gnl|CDD|153276 cd07592, BAR_Endophilin_A, The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins, localized at synapses, which interact with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. The BAR domains of endophilin-A1 and A3 form crescent-shaped dimers that can detect membrane curvature and drive membrane bending
EGTKLDDEFLEMERKTDATSKLVEDLIPKTKEYLQPNPAARAKLAMQNTYSKIRGQAKSTKYPQPEGLLG
EVMLKYGRELGEDSNFGQALVEVGEALKQLAEVKDSLDDNVKQNFLDPLQQLQDKDLKEINHHRKKLEGR
RLDYDYKKRKQGKGPDEELKQAEEKFEESKELAENSMFNLLENDVEQVSQLSALVEAQLDYHRQSAEILE
ELQSKLQERISEA
>gnl|CDD|153277 cd07593, BAR_MUG137_fungi, The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated Gene 137 protein and similar proteins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. This subfamily is composed predominantly of uncharacterized fungal proteins with similarity to Schizosaccharomyces pombe Meiotically Up-regulated Gene 137 protein (MUG137), which may play a role in meiosis and sporulation in fission yeast. MUG137 contains an N-terminal BAR domain and a C-terminal SH3 domain, similar to endophilins. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
QKTTLSEEFLELEKEIELRKEGMERLHRSTEAYVEYLSKKKPLLDDKDKCLPVEALGLVMINHGEEFPQD
SEYGSCLSKLGRAHCKIGTLQEEFADRLSDTFLANIERSLAEMKEYHSARKKLESRRLAYDAALTKSQKA
KKEDSRLEEELRRAKAKYEESSEDVEARMVAIKESEADQYRDLTDLLDAELDYHQQSLDVLREVRQSWPS
KSSGS
>gnl|CDD|153278 cd07594, BAR_Endophilin_B, The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain two endophilin-B isoforms. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle
QFTEEKLGTAEKTEYDAHFENLLQRADKTKVWTEKILKQTEAVLQPNPNVRVEDFIYEKLDRKKPDRLSN
LEQLGQAMIEAGNDFGPGTAYGSALIKVGQAQKKLGQAEREFIQTSSSNFLQPLRNFLEGDMKTISKERK
LLENKRLDLDACKTRVKKAKSAEAIEQAEQDLRVAQSEFDRQAEITKLLLEGISSTHANHLRCLRDFVEA
QMTYYAQCYQYMDDLQRQL
>gnl|CDD|153279 cd07595, BAR_RhoGAP_Rich-like, The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of Rho and Rac GTPase activating proteins (GAPs) with similarity to GAP interacting with CIP4 homologs proteins (Rich). Members contain an N-terminal BAR domain, followed by a Rho GAP domain, and a C-terminal prolin-rich region. Vertebrates harbor at least three Rho GAPs in this subfamily including Rich1, Rich2, and SH3-domain binding protein 1 (SH3BP1). Rich1 and Rich2 play complementary roles in the establishment and maintenance of cell polarity. Rich1 is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. Rich2 is a Rac GAP that interacts with CD317 and plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. SH3BP1 is a Rac GAP that inhibits Rac-mediated platelet-derived growth factor (PDGF)-induced membrane ruffling. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of Rich1 has been shown to form oligomers, bind membranes and induce membrane tubulation
DQTVGRAEKTEVLSDELLQIEKRVEAVKDACQNIHKKLISCLQGQSGEDKDKRLKKLPEYGLAQSMLESS
KELPDDSLLGKVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQKKRLSKLVLDMDSA
RSRYNAAHKSSGGQGAAAKVDALKDEYEEAELKLEQCRDALATDMYEFLAKEAEIASYLIDLIEAQREYH
RTALSVLEAVLPELQEQIEQSPSKPVFGQPLEEH
>gnl|CDD|153280 cd07596, BAR_SNX, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEVGGELGEALSKLG
KAAEELSSLSEAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAP
GIKPAKVEELEEELEEAESALEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAE
AWESLLPE
>gnl|CDD|153281 cd07597, BAR_SNX8, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 8. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
DEFTDKKLSEAAKVLLPPDFQEQWANSRERIRRLLESWTKLRVLAERYEKRSQQQAADRAEFARLLNSLG
ELTARLYPWAGDSDTWGDINEGLSSLSKHFQLLSDLSEDEARAEEDGVLEKLKLQLDLLVSLRDLFERHE
KLSLNNIQRLLKRIELNKKKLESLRAKPDVKGAEVDKLEASIIKDKESIANQLNRSWFIRECILEETQLF
QETQFLLTSILQEFVKDEIQYHSELANVWERLVPKL
>gnl|CDD|153282 cd07598, BAR_FAM92, The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92). BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. This group is composed of proteins from the family with sequence similarity 92 (FAM92), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, FAM92A and FAM92B, which may exist in many variants. The Xenopus homolog of FAM92A1, xVAP019, is essential for embryo survival and cell differentiation. FAM92A1 may be involved in regulating cell proliferation and apoptosis. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECL
AALQDYRQAEVERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQIISQA
ESELQKASVDANRSTKELEEQMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEED
L
>gnl|CDD|153283 cd07599, BAR_Rvs167p, The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 167 and similar proteins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 167 (Rvs167p) and Schizosaccharomyces pombe Hob1 (homolog of Bin1). S. cerevisiae Rvs167p plays a role in regulation of the actin cytoskeleton, endocytosis, and sporulation. It forms a heterodimer with another BAR domain protein Rvs161p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. Rvs167p also interacts with the GTPase activating protein (GAP) Gyp5p, which is involved in ER to Golgi vesicle trafficking. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
DEQFEELEKDFKSLEKSLKKLIEQSKAFRDSWRSILTHQIAFAKEFAELYDPIVGPKESVGSHPAPESTL
ARLSRYVKALEELKKELLEELEFFEERVILPAKELKKYIKKIRKTIKKRDHKKLDYDKLQNKLNKLLQKK
KELSLKDEKQLAKLERKLEEAKEEYEALNELLKSELPKLLALADEFLPPLFKSFYYIQLNIYYTLHEYLQ
EFGEPQ
>gnl|CDD|153284 cd07600, BAR_Gvp36, The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 kDa and similar proteins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Proteomic analysis shows that Golgi vesicle protein of 36 kDa (Gvp36) may be involved in vesicular trafficking and nutritional adaptation. A Saccharomyces cerevisiae strain deficient in Gvp36 shows defects in growth, in actin cytoskeleton polarization, in endocytosis, in vacuolar biogenesis, and in the cell cycle. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
VELEQRVDALKLVYKKILKVTKTYENESYDYPPNLTESISDFSKTIGSKVSELSKATSPTEAQKVLLGTP
APAKLPKTLNHALSRAALASSLELKSLEPEDEDPLSKALGKYSDAEEKIAEARLEQDQLIQKEFNAKLRE
TLNTSFQKAHKARKKVEDKRLQLDTARAELKSAEPAEKQEAARVEVETAEDEFVSATEEAVELMKEVLDN
PEPLQLLKELVKAQLAYHKTAAELLEELLSVL
>gnl|CDD|153285 cd07601, BAR_APPL, The Bin/Amphiphysin/Rvs (BAR) domain of Adaptor protein, Phosphotyrosine interaction, PH domain and Leucine zipper containing proteins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Adaptor protein, Phosphotyrosine interaction, PH domain and Leucine zipper containing (APPL) proteins are effectors of the small GTPase Rab5 that function in endosome-mediated signaling. They contain BAR, pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains. They form homo- and hetero-oligomers that are mediated by their BAR domains, and are localized to cytoplasmic membranes. Vertebrates contain two APPL proteins, APPL1 and APPL2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
RSLLNVFEEDALQLSSYMNQLLQACKRVYDAQNELKSATQALSKKLGEYEKQKFELGRDDEILVSTLKQF
SKVVDELSTMHSTLSSQLADTVLHPISQFMESDLAEIMTLKELFKAASNDHDGVLSKYSRLSKKRENTKV
KIEVNDEVYACRKKQHQTAMNYYCALNLLQYKKTTALLEPMIGYLQAQIAFFKMGPEMFTRQTEEFLSDI
NTSVQ
>gnl|CDD|153286 cd07602, BAR_RhoGAP_OPHN1-like, The Bin/Amphiphysin/Rvs (BAR) domain of Oligophrenin1-like Rho GTPase Activating Proteins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of Rho and Rac GTPase activating proteins (GAPs) with similarity to oligophrenin1 (OPHN1). Members contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, and a Rho GAP domain. Some members contain a C-terminal SH3 domain. Vertebrates harbor at least three Rho GAPs in this subfamily including OPHN1, GTPase Regulator Associated with Focal adhesion kinase (GRAF), GRAF2, and an uncharacterized protein called GAP10-like. OPHN1, GRAF and GRAF2 show GAP activity towards RhoA and Cdc42. In addition, OPHN1 is active towards Rac. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domains of OPHN1 and GRAF directly interact with their Rho GAP domains and inhibit their activity. The autoinhibited proteins are able to bind membranes and tubulate liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domains can occur simultaneously
RENLHEHEAELERTNKAIKELIKECKNLISATKNLSKAQRSFAQTLQNFKFECIGETQTDDEIEIAESLK
EFGRLIETVEDERDRMLENAEEQLIEPLEKFRKEQIGGAKEEKKKFDKETEKFCSSLEKHLNLSTKKKEN
QLQEADAQLDMERRNFHQASLEYVFKLQEVQERKKFEFVETLLSFMYGWLTFYHQGHEVAKDFKPYL
>gnl|CDD|153287 cd07603, BAR_ACAPs, The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain containing proteins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of ACAPs (ArfGAP with Coiled-coil, ANK repeat and PH domain containing proteins), which are Arf GTPase activating proteins (GAPs) containing an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, and C-terminal ankyrin (ANK) repeats. Vertebrates contain at least three members, ACAP1, ACAP2, and ACAP3. ACAP1 and ACAP2 are Arf6-specific GAPs, involved in the regulation of endocytosis, phagocytosis, cell adhesion and migration, by mediating Arf6 signaling. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
RASLEQVEADVSELETRLEKLLKLCNGMVDSGKTYVNANSLFVNSLNDLSDYFRDDSLVQNCLNKFIQAL
QEMNNFHTILLDQAQRTVSTQLQNFVKEDIKKVKESKKHFEKISDDLDNALVKNAQAPRSKPQEAEEATN
ILTATRSCFRHTALDYVLQINVLQAKKRHEILSTLLSYMHAQFTFFHQGYDLLEDLEPYM
>gnl|CDD|153288 cd07604, BAR_ASAPs, The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing proteins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of ASAPs (ArfGAP with SH3 domain, ANK repeat and PH domain containing proteins), which are Arf GTPase activating proteins (GAPs) with similarity to ACAPs (ArfGAP with Coiled-coil, ANK repeat and PH domain containing proteins) in that they contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, and ankyrin (ANK) repeats. However, ASAPs contain an additional C-terminal SH3 domain. ASAPs function in regulating cell growth, migration, and invasion. Vertebrates contain at least three members, ASAP1, ASAP2, and ASAP3. ASAP1 and ASAP2 shows GTPase activating protein (GAP) activity towards Arf1 and Arf5. They do not show GAP activity towards Arf6, but is able to mediate Arf6 signaling by binding stably to GTP-Arf6. ASAP3 is an Arf6-specific GAP. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains
RNTVGALEESLEGDRVGLQKLKKAVKAIHNSGLAHVENELQFAEALEKLGSKALSREEEDLGAAFLKFSV
FTKELAALFKNLMQNLNNIIMFPLDSLLKGDLKGSKGDLKKPFDKAWKDYETKASKIEKEKKQLAKEAGM
IRTEITGAEIAEEMEKERRMFQLQMCEYLIKVNEIKTKKGVDLLQHLVEYYHAQNSYFQDGLKVIEHFRP
YIEKL
>gnl|CDD|153289 cd07605, I-BAR_IMD, Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes. Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac
EELNRLTENIYKNIKEQFNPVLRNLIKAGKKYQKALQALSQAAKVFFDALAKIGELASQSRGSQELGEAL
KQIVDTHKSIEASLEQVAKAFHGELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQK
KSQKSGTGKYQEKLDQALEELNDKQKELEAFVSQGLRDALLEERRRYCFLVDKHCSVAKHEIAYHAKAMT
LLSTRLPLWQELC
>gnl|CDD|153290 cd07606, BAR_SFC_plant, The Bin/Amphiphysin/Rvs (BAR) domain of the plant protein SCARFACE (SFC). BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. The plant protein SCARFACE (SFC), also called VAscular Network 3 (VAN3), is a plant ACAP (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein), an Arf GTPase Activating Protein (GAP) that plays a role in the trafficking of auxin efflux regulators from the plasma membrane to the endosome. It is required for the normal vein patterning in leaves. SCF contains an N-terminal BAR domain, followed by a Pleckstrin Homology (PH) domain, an Arf GAP domain, and C-terminal ankyrin (ANK) repeats. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
KQLQELEGSADELRDRSLKLYKGCRKYRDALGEAYDGDSAFAESLEEFGGGHDDPISVAVGGPVMTKFTS
ALREIGSYKEVLRSQVEHMLNDRLAQFADTDLQEVKDARRRFDKASLDYEQARSKFLSLTKDAKPEILAA
AEEDLGTTRSAFETARFDLMNRLHAADARKRVEFLERLSGSMDAHLAFFKSGYELLRQLEPY
>gnl|CDD|153291 cd07607, BAR_SH3P_plant, The Bin/Amphiphysin/Rvs (BAR) domain of the plant SH3 domain-containing proteins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. This group is composed of proteins with similarity to Arabidopsis thaliana SH3 domain-containing proteins 1 (SH3P1) and 2 (SH3P2). SH3P1 is involved in the trafficking of clathrin-coated vesicles. It is localized at the plasma membrane and is associated with vesicles of the trans-Golgi network. Yeast complementation studies reveal that SH3P1 has similar functions to the Saccharomyces cerevisiae Rvs167p, which is involved in endocytosis and actin cytoskeletal arrangement. Members of this group contain an N-terminal BAR domain and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
QKLERLYASTRAAKHFQRDIVRGVEGFISTGSKQLEIGTKLAEDCKKYGSENPSVNTALSRASLHYGSAR
NQMEKERENLHRVLSEQVAEPLRAMVYGAPLEDARHLKQRYDRLRQEVEAQAAEVARRRSKDKESGGNPD
NAAKLQSAESKLDELKSSMNTLGKEATSAMLAVEDQQQQVTLQRLLAMVEAERAYHQRAADILDKLHDE
>gnl|CDD|153292 cd07608, BAR_ArfGAP_fungi, The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized fungal Arf GAP proteins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. This group is composed of uncharacterized fungal proteins containing an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, and an Arf GTPase Activating Protein (GAP) domain. These proteins may play roles in Arf-mediated functions involving membrane dynamics. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
ATLSNLERKTRLLRSYLKRLIKRIVKLIEAQDQLVDLEFNELLSEAKFKNDFNVALDSYFDPFLLNLAFF
LRDVCQDLQLKKIEPLLKIYSINDIKELSDKKKDFEEESKDYYSWLSKYLSNESDKKRPDSKLLAKRKTF
ELSRFDYLNYLQDLHGGRKEQELLSILTKFINQQYDSIALTSNKIDALRPSL
>gnl|CDD|153293 cd07609, BAR_SIP3_fungi, The Bin/Amphiphysin/Rvs (BAR) domain of fungal Snf1p-interacting protein 3. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. This group is composed of mostly uncharacterized fungal proteins with similarity to Saccharomyces cerevisiae Snf1p-interacting protein 3 (SIP3). These proteins contain an N-terminal BAR domain followed by a Pleckstrin Homology (PH) domain. SIP3 interacts with SNF1 protein kinase and activates transcription when anchored to DNA. It may function in the SNF1 pathway. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
ASVNHFDDQVDAIEKWLDGYVSSTKKLYSSLDELERVINSFLSHLLPPLLVSGGVIDQDYTPLALKRFGD
GLKDFWGGVLSALKGNDSLILDPLRSFVKSDIRPYKELRKNFEYYQRKYDSMLARYVAQSKTKEPSSLRE
DAFQLFEARKAYLKASLDLVIAIPQLRLTLDKLLVDIITDLWREKKRTHDDSGSKFDPKWGEEMERIRGW
SEEM
>gnl|CDD|153294 cd07610, FCH_F-BAR, The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein
GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKPESGKTSLGTSWNSLREETESAA
TVHEELSEKLSQLIREPLEKVKEDKEQARKKELAEGEKLKKKLQELWAKLAKKADEEYREQVEKLNPAQS
EYEEEKLNKIQAEQEREEERLEILKDNLKNYINAIKEIPQKIQQELEQSIN
>gnl|CDD|153295 cd07611, BAR_Amphiphysin_I_II, The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin I and II. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Amphiphysins function primarily in endocytosis and other membrane remodeling events. They contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin and synaptojanin. They function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. The N-BAR domain of amphiphysin forms a curved dimer with a positively-charged concave face that can drive membrane bending and curvature. Human autoantibodies to amphiphysin-1 hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Mutations in amphiphysin-2 (BIN1) are associated with autosomal recessive centronuclear myopathy
QKLGKADETKDEQFEEYVQNFKRQETEGTRLQRELRAYLAAIKGMQEASKKLTESLHEVYEPDWYGRDDV
KTIGEKCDLLWEDFHQKLVDGALLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQTSKRKDEGR
IAKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEISVLCHKLYEVMTKLG
E
>gnl|CDD|153296 cd07612, BAR_Bin2, The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 2. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 2 (Bin2) is a BAR domain containing protein that is mainly expressed in hematopoietic cells. It is upregulated during granulocyte differentiation and is thought to function primarily in this lineage. The BAR domain of Bin2 is closely related to the BAR domains of amphiphysins, which function primarily in endocytosis and other membrane remodeling events. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. Unlike amphiphysins, Bin2 does not appear to contain a C-terminal SH3 domain. Amphiphysin I proteins, enriched in the brain and nervous system, function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), function in intracellular vessicle trafficking. Bin2 can form a stable complex with Bin1 in cells but cannot replace the function of Bin1, and thus, appears to harbor a nonredundant function. The N-BAR domain of amphiphysin forms a curved dimer with a positively-charged concave face that can drive membrane bending and curvature
QKLGKTVETKDEQFEQCAMNLNMQQSDGNRLYKDLKAYLNAVKVMHESSKRLSQTLQDIYEPDWDGHEDL
GAIVEGEDLLWNDYEAKLHDQALRTMESYMAQFPDVKERVAKRGRKLVDYDSARHHLEALQNAKKKDDAK
IAKAEEEFNRAQVVFEDINRELREELPILYDSRIGCYVTVFQNISNLRDTFYKEMSKLNHDLYNVMKKLE
D
>gnl|CDD|153297 cd07613, BAR_Endophilin_A1, The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A1 (or endophilin-1) is also referred to as SH3P4 (SH3 domain containing protein 4) or SH3GL2 (SH3 domain containing Grb2-like protein 2). It is localized in presynaptic nerve terminals. It plays many roles in clathrin-dependent endocytosis of synaptic vesicles including early vesicle formation, ubiquitin-dependent sorting of plasma membrane proteins, and regulation of calcium influx into neurons. The BAR domain of endophilin-A1 forms crescent-shaped dimers that can detect membrane curvature and drive membrane bending, while its SH3 domain binds the endocytic proteins, dynamin 1, synaptojanin 1, and amphiphysins
EGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLA
EAMLKFGRELGDECNFGPALGDVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGR
RLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQATQILQ
QVTVKLEDRIREA
>gnl|CDD|153298 cd07614, BAR_Endophilin_A2, The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins, localized at synapses, which interact with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A2 (or endophilin-2) is also referred to as SH3P8 (SH3 domain containing protein 8) or SH3GL1 (SH3 domain containing Grb2-like protein 1). It localizes to presynaptic nerve terminals and forms heterodimers with endophilin-A1 through their BAR domains. Endophilin-A2 binds dynamin 1, synaptojanin 1, and the beta1-adrenergic receptor cytoplasmic tail through its SH3 domain
EGTKLDDDFKEMEKKVDLTSKAVTEVLARTIEYLQPNPASRAKLTMLNTVSKIRGQVKNPGYPQSEGLLG
ETMIRYGKELGDESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCDKDLKEIQHHLKKLEGR
RLDFDYKKKRQGKIPDEELRQAMEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILD
ELAEKLKRRMREA
>gnl|CDD|153299 cd07615, BAR_Endophilin_A3, The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins localized at synapses that interacts with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A3 (or endophilin-3) is also referred to as SH3P13 (SH3 domain containing protein 13) or SH3GL3 (SH3 domain containing Grb2-like protein 3). It regulates Arp2/3-dependent actin filament assembly during endocytosis. It binds N-WASP through its SH3 domain and enhances the ability of N-WASP to activate the Arp2/3 complex. Endophilin-A3 co-localizes with the vesicular glutamate transporter 1 (VGLUT1), and may play an important role in the synaptic release of glutamate
EGTKLDDDFQEMERKIDVTNKVVAELLSKTTEYLQPNPAYRAKLGMLNTVSKIRGQVKTTGYPQTEGLLG
DCMLRYGRELGEESTFGNALLDVGESMKQMAEVKDSLDINVKQNFIDPLQLLQDKDLKEIGHHLKKLEGR
RLDFDYKKKRQGKIPDEEIRQAVEKFEESKELAERSMFNFLENDVEQVSQLSVLIEAALDYHRQSTEILE
DLQSKLQNRISTA
>gnl|CDD|153300 cd07616, BAR_Endophilin_B1, The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B1. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle. Endophilin-B1, also called Bax-interacting factor 1 (Bif-1) or SH3GLB1 (SH3-domain GRB2-like endophilin B1), is localized mainly to the Golgi apparatus. It is involved in the regulation of many biological events including autophagy, tumorigenesis, nerve growth factor (NGF) trafficking, neurite outgrowth, mitochondrial outer membrane dynamics, and cell death. Endophilin-B1 forms homo- and heterodimers (with endophilin-B2) through its BAR domain, which can bind and bend membranes. It interacts with amphiphysin 1 and dynamin 1 through its SH3 domain
QFTEEKFGQAEKTELDAHLENLLSKAECTKHWTEKIMKQTEVLLQPNPNARIEEFVYEKLDRKAPSRMNN
PELLGQYMIDAGNEFGPGTAYGNALIKCGETQKQIGTADRELIQTSAINFLTPLRNFIEGDYKTITKERK
LLQNKRLDLDAAKTRLKKAKVAEARAAAEQELRITQSEFDRQAEITRLLLEGISSTHAHHLRCLNDFVEA
QMTYYAQCYQYMLDLQKQL
>gnl|CDD|153301 cd07617, BAR_Endophilin_B2, The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B2. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain two endophilin-B isoforms. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle. Endophilin-B2, also called SH3GLB2 (SH3-domain GRB2-like endophilin B2), is a cytoplasmic protein that interacts with the apoptosis inducer Bax. It is overexpressed in prostate cancer metastasis and has been identified as a cancer antigen with potential utility in immunotherapy. Endophilin-B2 forms homo- and heterodimers (with endophilin-B1) through its BAR domain, which can bind and bend membranes
QFTEEKLGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTN
AELLGQYMTEAANDFGPGTPYGKTLIKVGETQKRLGAAERDFIHTSSINFLTPLRNFLEGDWKTISKERR
LLQNRRLDLDACKARLKKAEHELRVAQTEFDRQAEVTRLLLEGISSTHVNHLRCLHEFVEAQATYYAQCY
RHMLDLQKQL
>gnl|CDD|153302 cd07618, BAR_Rich1, The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 1 (Rich1) is also called Neuron-associated developmentally-regulated protein (Nadrin) or Rho GTPase activating protein 17 (ARHGAP17). It is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. It may be a component of a sorting mechanism in the recycling of tight junction transmembrane proteins. Rich1 contains an N-terminal BAR domain followed by a Rho GAP domain and a C-terminal proline-rich domain. It interacts with the BAR domain proteins endophilin and amphiphysin through its proline-rich region. The BAR domain of Rich1 forms oligomers and can bind membranes and induce membrane tubulation
NQTVGRAEKTEVLSEDLLQIERRLDTVRSVSHNVHKRLIACFQGQVGTDAEKRHKKLPLTALAQNMQEGS
AQLGEESLIGKMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSA
RGRYNQAHKSSGTNFQAMPSKIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQAD
YHRKALAVIEKVLPEIQAHQDKWMEKPAFGTPLEEH
>gnl|CDD|153303 cd07619, BAR_Rich2, The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 2 (Rich2) is a Rho GTPase activating protein that interacts with CD317, a lipid raft-associated integral membrane protein. It plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. Rich2 contains an N-terminal BAR domain followed by a GAP domain for Rho and Rac GTPases and a C-terminal proline-rich domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
NQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGVDADKRSKKLPLTTLAQCMVEGA
AVLGDDSLLGKMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSS
RTRWQQSSKSSGLSSNLQPTGAKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQ
AEYHRKSLELLQSVLPQIKAHQEAWVEKPSYGKPLEEH
>gnl|CDD|153304 cd07620, BAR_SH3BP1, The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. SH3-domain binding protein 1 (SH3BP1 or 3BP-1) is a Rac GTPase activating protein that inhibits Rac-mediated platelet-derived growth factor (PDGF)-induced membrane ruffling. SH3BP1 contains an N-terminal BAR domain followed by a GAP domain for Rho and Rac GTPases and a C-terminal proline-rich domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
GSLSVSQDATELLTEDLVLVEQRVEPAKKAAQLIHKKLQGCLQSQPGLEAEKRMKKLPLMALSISMAESF
KDFDAESSIRRVLEMCCFMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQFAKLTTDWNSA
KSRSPQAAGRSPRSGGRSEEVGEHQGIRRANKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYAN
YFIRLLELQAEYHKNSLEFLDKNITELKENHSQKEPSVSVSSQRVYG
>gnl|CDD|153305 cd07621, BAR_SNX5_6, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Members of this subfamily include SNX5, SNX6, the mammalian SNX32, and similar proteins. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. The function of SNX32 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
GFLKSISKSADEELLLSGQKDVDEFFEQEKNFLVEYHNRIKDATAKADKMTRKHKDVADSYIKISAALTQ
LATSEPTPLDKFLLKVAETFEKLRKLEGRVASDEDLKLSDTLRYYMRDTQAAKDLLYRRLRCLANYENAN
KNLEKARAKNKDVHAAEAAQQEACEKFESMSESAKQELLDFKTRRVAAFRKNLVELAELEIKHAKAQIQL
LKNCLAALK
>gnl|CDD|153306 cd07622, BAR_SNX4, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 4. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It is also implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and leptin. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
KALNASFRLRNPDKRFEDLKNYSDELQTNLNNLLKVRARLAERLYGVYKIHANYGRVFSEWSAIEKEMGD
GLQKAGHYMDSYAASIDNGLEDEELIADQLKEYLFFADSLRAVCKKHELLQYDLEKAEDALANKKQQGEE
AVKEAKDELNEFVKKALEDVERFKKQKVRDLKEILISYAKLQIKLAKKGLQTWTNIKECLQ
>gnl|CDD|153307 cd07623, BAR_SNX1_2, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. This subfamily consists of SNX1, SNX2, and similar proteins. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
SKITIKMDETDQWFEEKQQQIENLDQQLRKLHASVESLVNHRKELALNTGSFAKSAAMLSNCEEHTSLSR
ALSQLAEVEEKIEQLHGEQADTDFYILAELLKDYIGLIGAIKDVFHERVKVWQNWQNAQQTLTKKREAKA
KLELSGRTDKLDQAQQEIKEWEAKVDRGQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYLESLLNTQQ
QLIKYWEAFLPEAK
>gnl|CDD|153308 cd07624, BAR_SNX7_30, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 7 and 30. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. This subfamily consists of SNX7, SNX30, and similar proteins. The specific functions of SNX7 and SNX30 have not been elucidated. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
RNTSTMYLLKNRSPEFDKMNEYLTLFGEKLGTIERISQRIHKERIEYFDELKEYSPIFQLWSASETELAP
LLEGVSSAVERCTAALEVLLSDHEFVFLPPLREYLLYSDAVKDVLKRRDQFQIEYELSVEELNKKRLELL
KEVEKLQDKLECANADLKADLERWKQNKRQDLKKILLDMAEKQIQYYEQCLAAWEEVLPA
>gnl|CDD|153309 cd07625, BAR_Vps17p, The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps17p. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp17p forms a dimer with Vps5p, the yeast counterpart of human SNX1, and is part of the retromer complex that mediates the transport of the carboxypeptidase Y receptor Vps10p from endosomes to Golgi. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
GLKRKTLKQFAPPYDEYTELAEFRPLVKSIYLTAQDLQEKLLRVSKARKQLSLEEADFGQKLIQLSVEET
HHGLGNLYEKFGKVLTAVGDIDSIQATVDMATLYDGLEWISRDAYVVKEALTNRHLLMRELIQAQQNTKS
KQEAARRLKAKRDINPLKVDEAIRQLEEATKHEHDLSLKLKRITGNMLIERKEWTDWTEEDLQSAIREYT
LRKIEYERKKLSLLERIRLD
>gnl|CDD|153310 cd07626, BAR_SNX9_like, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 9 and Similar Proteins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. This subfamily consists of SNX9, SNX18, SNX33, and similar proteins. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
DVEQQVDAFKKFVKSMDDSVKNLINIAQEQAKKHQGPYKKEYQKIGQAFTSLGTAFELDETPTSVPLTQA
IKHTGQAYEEIGELFAEQPKHDLIPLLDGLHEYKGLLSTFPDIIGVHKGAVQKVKECERLVDEGKMSSAE
LEEVKRRTDVISYALLAEINHFHRERVRDFKSMMRNYLQQQIEFYQKIAAKLEEALAMY
>gnl|CDD|153311 cd07627, BAR_Vps5p, The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
EPDEWFIEKKQYLDSLESQLKQLYKSLELVSSQRKELASATEEFAETLEALSSLELSKSLSDLLAALAEV
QKRIKESLERQALQDVLTLGVTLDEYIRSIGSVRAAFAQRQKLWQYWQSAESELSKKKAQLEKLKRQGKT
QQEKLNSLLSELEEAERRASELKKEFEEVSELIKSELERFERERVEDFRNSVEIYLESAIESQKELIELW
ETFYQR
>gnl|CDD|153312 cd07628, BAR_Atg24p, The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Atg24p. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Atg24p is involved in membrane fusion events at the vacuolar surface during pexophagy. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
KPDKEFLEIREKSDKLDENLTKIDKIFAKVVKRQSDLSVDYADLATQFQKLGSLESGEITEPFKIFSESL
SQFSTSLRVLNKYTDENYLTSLKDLLHYILSLKNLIKLRDQKQLDYEELSDYLLTDEVENAKETSDAFNK
EVLKEYPNFERIKKQEIKDSLGALADGHIDFYQGLVEDWEKVEPK
>gnl|CDD|153313 cd07629, BAR_Atg20p, The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Atg20p. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The function of Atg20p is unknown but it has been shown to interact with Atg11p, which plays a role in linking cargo molecules with vesicle-forming components. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
EPDDEFTDIEAETKKYEQLLHGGMEKVNRRITKRLGDLAEDMADLGGRFNAFSLEEQKSELAEALEKVGQ
AVDSTYLATEALVGSLYYNINEPLSESAQFAGVVRELLKYRKLKHVQYEMTKDSLLESALVAASDDLVIS
STIKQKDLPRFQREREADLREILKNYSKYHKDWAKQNLEAWKEAKAE
>gnl|CDD|153314 cd07630, BAR_SNX_like, The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized Sorting Nexins. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of uncharacterized proteins with similarity to sorting nexins (SNXs), which are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
DVDEFFQKERDMNTKLSANMKEAAEKFLKIVNTEQRLANALGHLSSSLQLCVGLDEASVVALNRLCTKLS
EALEEAKENIEVVAGNNENTLGLTLDLYSRYSESEKDMLFRRTCKLIEFENASKALEKAKPQKKEQAEEA
KKKAETEFEEISSLAKKELERFHRQRVLELQSALVCYAESQIKNAKEAAAVLTKTLEA
>gnl|CDD|153315 cd07631, BAR_APPL1, The Bin/Amphiphysin/Rvs (BAR) domain of Adaptor protein, Phosphotyrosine interaction, PH domain and Leucine zipper containing 1. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Adaptor protein, Phosphotyrosine interaction, PH domain and Leucine zipper containing (APPL) proteins are effectors of the small GTPase Rab5 that function in endosome-mediated signaling. They contain BAR, pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains. They form homo- and hetero-oligomers that are mediated by their BAR domains. Vertebrates contain two APPL proteins, APPL1 and APPL2. APPL1 interacts with diverse receptors (e.g. NGF receptor TrkA, FSHR, adiponectin receptors) and signaling proteins (e.g. Akt, PI3K), and may function as an adaptor linked to many distinct signaling pathways. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
RSLLGVFEEDAAAISNYFNQLFQAMHRIYDAQNELSAATHLTSKLLKEYEKQRFPLGGDDEVMSSTLQQF
SKVIDELSSCHAVLSTQLADAMMFPITQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKRRENEKV
KYEVTEDVYTSRKKQHQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSENLNEQLEEFLTNI
GTSVQ
>gnl|CDD|153316 cd07632, BAR_APPL2, The Bin/Amphiphysin/Rvs (BAR) domain of Adaptor protein, Phosphotyrosine interaction, PH domain and Leucine zipper containing 2. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Adaptor protein, Phosphotyrosine interaction, PH domain and Leucine zipper containing (APPL) proteins are effectors of the small GTPase Rab5 that function in endosome-mediated signaling. They contain BAR, pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains. They form homo- and hetero-oligomers that are mediated by their BAR domains. Vertebrates contain two APPL proteins, APPL1 and APPL2. Both APPL proteins interact with the transcriptional repressor Reptin, acting as activators of beta-catenin/TCF-mediated trancription. APPL2 is essential for cell proliferation. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
RSLLSVFEEDAGTLTDYTNQLLQAMQRVYGAQNEMCLATQQLSKQLLAYEKQNFALGKGDEEVISTLQYF
AKVVDELNVLHSELAKQLADTMVLPIIQFREKDLTEVSTLKDLFGIASNEHDLSMAKYSRLPKKRENEKV
KAEVAKEVAYSRRKQHLSSLQYYCALNALQYRKRVAMLEPMLGYTHGQINFFKKGAELFSKKLDSFLSSV
SDMNQ
>gnl|CDD|153317 cd07633, BAR_OPHN1, The Bin/Amphiphysin/Rvs (BAR) domain of Oligophrenin-1. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Oligophrenin-1 (OPHN1) is a GTPase activating protein (GAP) with activity towards RhoA, Rac, and Cdc42, that is expressed in developing spinal cord and in adult brain areas with high plasticity. It plays a role in regulating the actin cystoskeleton as well as morphology changes in axons and dendrites, and may also function in modulating neuronal connectivity. Mutations in the OPHN1 gene causes X-linked mental retardation associated with cerebellar hypoplasia, lateral ventricle enlargement and epilepsy. OPHN1 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, and a Rho GAP domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
RERLKCYEQELERTNKFIKDVIKDGNALISAIKEYSSAVQKFSQTLQSFQFDFIGDTLTDDEINIAESFK
EFAELLQEVEEERMMMVQNASDLLIKPLENFRKEQIGFTKERKKKFEKDSEKFYSLLDRHVNLSSKKKES
QLQEADLQVDKERQNFYESSLEYVYQIQEVQESKKFDVVEPVLAFLHSLFTSNNLTVELTQDFLPYK
>gnl|CDD|153318 cd07634, BAR_GAP10-like, The Bin/Amphiphysin/Rvs (BAR) domain of Rho GTPase activating protein 10-like. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This group is composed of uncharacterized proteins called Rho GTPase activating protein (GAP) 10-like. GAP10-like may be a GAP with activity towards RhoA and Cdc42. Similar to GRAF and GRAF2, it contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domains of the related proteins GRAF and OPHN1, directly interact with their Rho GAP domains and inhibit theiractivity. The autoinhibited proteins are capable of binding membranes and tubulating liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domain can occur simultaneously
RERLQCHEIELERTNKFIKELIKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLK
EFARLLIAVEEERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILEKHLNLSAKKKES
HLQRADTQIDREHQNFYEASLEYVFKIQEVQEKKKFEFVEPLLAFLQGLFTFYHEGYELAQEFAPYK
>gnl|CDD|153319 cd07635, BAR_GRAF2, The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion 2. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. GTPase Regulator Associated with Focal adhesion kinase 2 (GRAF2), also called Rho GTPase activating protein 10 (ARHGAP10) or PS-GAP, is a GAP with activity towards Cdc42 and RhoA which regulates caspase-activated p21-activated protein kinase-2 (PAK-2p34). GRAF2 interacts with PAK-2p34, leading to its stabilization and decrease of cell death. It is highly expressed in skeletal muscle and also interacts with PKNbeta, which is a target of Rho. GRAF2 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of the related protein GRAF directly interacts with its Rho GAP domain and inhibits its activity. Autoinhibited GRAF is capable of binding membranes and tubulating liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domain can occur simultaneously
RERIRAHEAELERTNRFIKELLKDGKNLIAATKSLSAAQRKFAHSLRDFKFEFIGDAETDDERCIDASLQ
EFSNFLKNLEEQREIMALNVTETLIKPLERFRKEQLGAVKEEKKKFDKETEKNYSLLEKHLNLSAKKKEP
QLQEADVQVEQNRQHFYELSLEYVCKLQEIQERKKFECVEPMLSFFQGVFTFYHQGYELAKDFNHYK
>gnl|CDD|153320 cd07636, BAR_GRAF, The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion kinase. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. GTPase Regulator Associated with Focal adhesion kinase (GRAF), also called Rho GTPase activating protein 26 (ARHGAP26), is a GAP with activity towards RhoA and Cdc42 and is only weakly active towards Rac1. It influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase (FAK), which is a critical component of integrin signaling. GRAF contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of GRAF directly interacts with its Rho GAP domain and inhibits its activity. Autoinhibited GRAF is capable of binding membranes and tubulating liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domain can occur simultaneously
RERLKSHEAELDKTNKFIKELIKDGKSLIAALKNLSSAKRKFADSLNEFKFQCIGDAETDDEICIARSLQ
EFAAVLRNLEDERTRMIENASEVLITPLEKFRKEQIGAAKEAKKKYDKETEKYCAVLEKHLNLSSKKKES
QLHEADSQVDLVRQHFYEVSLEYVFKVQEVQERKMFEFVEPLLAFLQGLFTFYHHGYELAKDFSDFK
>gnl|CDD|153321 cd07637, BAR_ACAP3, The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 3. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ACAP3 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 3), also called centaurin beta-5, is presumed to be an Arf GTPase activating protein (GAP) based on its similarity to the Arf6-specific GAPs ACAP1 and ACAP2. The specific function of ACAP3 is still unknown. ACAP3 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, and C-terminal ankyrin (ANK) repeats. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
RATIDEVETDVVEIEAKLDKLVKLCSGMIEAGKAYATTNKLFVSGIRDLSQQCKKDEMISECLDKFGDSL
QEMVNYHMILFDQAQRSVRQQLHSFVKEDVRKFKETKKQFDKVREDLEIALVKNAQAPRHKPHEVEEATS
TLTITRKCFRHLALDYVLQINVLQAKKKFEILDSMLSFMHAQYTFFQQGYSLLHELDPYM
>gnl|CDD|153322 cd07638, BAR_ACAP2, The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 2. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ACAP2 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 2), also called centaurin beta-2, is an Arf6-specific GTPase activating protein (GAP) which mediates Arf6 signaling. Arf6 is involved in the regulation of endocytosis, phagocytosis, cell adhesion and migration. ACAP2 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, and C-terminal ankyrin (ANK) repeats. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
RAALEDVEGDVAELELKLDKLVKLCIGMIDAGKAFCQANKQFMNGIRDLAQYSSKDAVIETSLTKFSDTL
QEMINYHTILFDQAQRSIKAQLQTFVKEDLRKFKDAKKQFDKVSEEKENALVKNAQVQRNKQHEVEEATN
ILTATRKCFRHIALDYVLQINVLQSKRRSEILKSMLSFMYAHLTFFHQGYDLFSELGPYM
>gnl|CDD|153323 cd07639, BAR_ACAP1, The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 1. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ACAP1 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 1), also called centaurin beta-1, is an Arf6-specific GTPase activating protein (GAP) which mediates Arf6 signaling. Arf6 is involved in the regulation of endocytosis, phagocytosis, cell adhesion and migration. ACAP1 also participates in the cargo sorting and recycling of the transferrin receptor and integrin beta1. It may also play a role in innate immune responses. ACAP1 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, and C-terminal ankyrin (ANK) repeats. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
RAAIEEVEAEVSELETRLEKLVKLGSGMLEGGRHYCAASRAFVDGLCDLAHHGPKDPMMAECLEKFSDGL
NHILDSHAELLEATQFSFKQQLQLLVKEDLRGFRDARKEFERGAESLEAALQHNAETPRRKAQEVEEAAA
ALLGARATFRDRALDYALQINVIEDKKKFDILEFMLQLMEAQASFFQQGHEALSALHQYR
>gnl|CDD|153324 cd07640, BAR_ASAP3, The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 3. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ASAP3 (ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 3) is also known as ACAP4 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 4), DDEFL1 (Development and Differentiation Enhancing Factor-Like 1), or centaurin beta-6. It is an Arf6-specific GTPase activating protein (GAP) and is co-localized with Arf6 in ruffling membranes upon EGF stimulation. ASAP3 is implicated in the pathogenesis of hepatocellular carcinoma and plays a role in regulating cell migration and invasion. ASAP3 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of the related protein ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains
RSTAAALEESLEGDQASLQRIKKIVKAIHNSGLNHVENEEQYTEALENLGNSHLSQNNHELSTGFLNLAV
FTREVTALFKNLVQNLNNIVSFPLDSLLKGQLRDGRLESKKQMEKAWKDYEAKIGKLEKERREKQKQHGL
IRLDMTDTAEDMQRERRNFQLHMCEYLLKAQESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQNLGPFI
EKL
>gnl|CDD|153325 cd07641, BAR_ASAP1, The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 1. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ASAP1 (ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 1) is also known as DDEF1 (Development and Differentiation Enhancing Factor 1), AMAP1, centaurin beta-4, or PAG2. ASAP1 is an Arf GTPase activating protein (GAP) with activity towards Arf1 and Arf5 but not Arf6 However, it has been shown to bind GTP-Arf6 stably without GAP activity. It has been implicated in cell growth, migration, and survival, as well as in tumor invasion and malignancy. It binds paxillin and cortactin, two components of invadopodia which are essential for tumor invasiveness. It also binds focal adhesion kinase (FAK) and the SH2/SH3 adaptor CrkL. ASAP1 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains
RNTVNVLEEALDQDRTALQKVKKSVKAIYNSGQDHVQNEENYAQALDKFGSNFLSRDNPDLGTAFVKFST
LTKELSTLLKNLLQGLSHNVIFTLDSLLKGDLKGVKGDLKKPFDKAWKDYETKFTKIEKEKREHAKQHGM
IRTEITGAEIAEEMEKERRLFQLQMCEYLIKVNEIKTKKGVDLLQNLIKYYHAQCNFFQDGLKTADKLKQ
YIEKL
>gnl|CDD|153326 cd07642, BAR_ASAP2, The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 2. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ASAP2 (ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 2) is also known as DDEF2 (Development and Differentiation Enhancing Factor 2), AMAP2, centaurin beta-3, or PAG3. ASAP2 mediates the functions of Arf GTPases vial dual mechanisms: it exhibits GTPase activating protein (GAP) activity towards class I (Arf1) and II (Arf5) Arfs; and binds class III Arfs (GTP-Arf6) stably without GAP activity. It binds paxillin and is implicated in Fcgamma receptor-mediated phagocytosis in macrophages and in cell migration. ASAP2 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of the related protein ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains
RNTVVAIEEALDVDRTVLYKMKKSVKAIHTSGLAHVENEEQYTQALEKFGSNCVCRDDPDLGSAFLKFSV
FTKELTALFKNLVQNMNNIITFPLDSLLKGDLKGVKGDLKKPFDKAWKDYETKVTKIEKEKKEHAKMHGM
IRTEISGAEIAEEMEKERRFFQLQMCEYLLKVNEIKIKKGVDLLQNLIKYFHAQCNFFQDGLKAVETLKP
SIEKL
>gnl|CDD|153327 cd07643, I-BAR_IMD_MIM, Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis. The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. Members of this subfamily include missing in metastasis (MIM) or metastasis suppressor 1 (MTSS1), metastasis suppressor 1-like (MTSSL) or ABBA (Actin-Bundling protein with BAIAP2 homology), and similar proteins. They contain an N-terminal IMD and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. MIM was originally identified as a missing transcript from metastatic bladder and prostate cancer cells. It is a scaffold protein that functions in a signaling pathway between the PDGF receptor, Src kinases, and actin assembly. It may also function as a cofactor of the Sonic hedgehog (Shh) transcriptional pathway and may participate in tumor development and progression via this pathway. ABBA regulates actin and plasma membrane dynamics to promote the extension of radial glia, which is important in neuronal migration, axon guidance and neurogenesis. The IMD domain of MIM binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac
KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIG
SALTRMCMRHKSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIR
LQKKARKGKGDLQPQLDSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEV
THLQTIMEDLASLTADPHKLP
>gnl|CDD|153328 cd07644, I-BAR_IMD_BAIAP2L2, Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2. The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. This group is composed of uncharacterized proteins known as BAIAP2L2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2). They contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The related proteins, BAIAP2L1 and IRSp53, function as regulators of membrane dynamics and the actin cytoskeleton. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac
DLLYRSTISIYKSIMEQFNPALENLVYLGNNYLRAFHALSEAAEVYFSAIAKIGEQALQSLTSQSLGEIL
IQMSETQRKLSADLEVVFQTFHVDLLQHMDKNTKLDMQFIEDSRRVYELEYRHRAANLEKCMSELWRMER
QRDRNVREMKENVNRLRQSMQAFLKESQRAAELEEKRRYRFLAEKHYLLNNTFLQFQSRARGMLQTRVPS
WKEQP
>gnl|CDD|153329 cd07645, I-BAR_IMD_BAIAP2L1, Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1. The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. BAIAP2L1 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1) is also known as IRTKS (Insulin Receptor Tyrosine Kinase Substrate). It is widely expressed, serves as a substrate for the insulin receptor, and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. BAIAP2L1 expression leads to the formation of short actin bundles, distinct from filopodia-like protrusions induced by the expression of the related protein IRSp53. It contains an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The IMD domain of BAIAP2L1 binds and bundles actin filaments, and binds the small GTPase Rac
DEVNKLTESTYKNVMEQFNPGLRNLINLGKNYEKAVNAMVLAGKAYYDGVAKIGEIAAVSPVSKELGHVL
MEISDVHKKLNDSLEENFKKFHREIIAELERKTDLDVKYMTATLKRYQTEHKNKLDSLEKSQADLKKIRR
KSQGRRNASKYEHKENEYLETVTSRQSDIQKFIADGCREALLEEKRRFCFLVDKHCSFSNHIHYFHQQAA
ELLNSKLPVWQETCSD
>gnl|CDD|153330 cd07646, I-BAR_IMD_IRSp53, Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Insulin Receptor tyrosine kinase Substrate p53. The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. IRSp53 (Insulin Receptor tyrosine kinase Substrate p53) is also known as BAIAP2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2). It is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. One variant (T-form) is expressed exclusively in human breast cancer cells. The gene encoding IRSp53 is a putative susceptibility gene for Gilles de la Tourette syndrome. IRSp53 contains an N-terminal IMD, a CRIB (Cdc42 and Rac interactive binding motif), an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. Its IMD domain binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac
RTEEVNRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALASVTFAAKGYFDALVKMGELASESQGSKELGD
VLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLTAALKKYQTEHRSKGESLEKCQAELKKL
RKKSQGSKNPQKYSDKELQYIEAISNKQGELENYVSDGYKTALTEERRRYCFLVEKQCAVAKNSIAYHSK
GKELLTQKLPSWQQACSDPNKI
>gnl|CDD|153331 cd07647, F-BAR_PSTPIP, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
FTSTTGFDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSKSAGPGDEIGTLKSSWDSLRKETE
NVANAHIQLAQSLREEAEKLEEFREKQKEERKKTEDIMKRSQKNKKELYKKTMKAKKSYEQKCREKDKAE
QAYEKSSSGAQPKEAEKLKKKAAQCKTSAEEADSAYKSSIGCLEDARVEWESEHATACQVFQNMEEERIK
FLRNALWVHCNLGSMQCVKLDEMYEDVRK
>gnl|CDD|153332 cd07648, F-BAR_FCHO, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proteins in this group have been named FCH domain Only (FCHO) proteins. Vertebrates have two members, FCHO1 and FCHO2. These proteins contain an F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
GEKNNGFDVLYHNMKHGQIAVKELADFLRERATIEETYSKALNKLAKQASNSSQLGTFAPLWLVLRVSTE
KLSELHLQLVQKLQELIKDVQKYGEEQHKKHKKVKEEESGTAEAVQAIQTTTAALQKAKEAYHARCLELE
RLRRENASPKEIEKAEAKLKKAQDEYKALVEKYNNIRADFETKMTDSCKRFQEIEESHLRQMKEFLASYA
EVLSENHSAVGQVHEEFKRQVDELTVDKLLRQFVESKGTGTEKPELIEFEE
>gnl|CDD|153333 cd07649, F-BAR_GAS7, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein 7. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Growth Arrest Specific protein 7 (GAS7) is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
NTTVTGFEILLQKQLKGKQMQKEMAEFIRERIKIEEEYAKNLSKLSQSSLAAQEEGTLGEAWAQVKKSLA
DEAEVHLKFSSKLQSEVEKPLLNFRENFKKDMKKLDHHIADLRKQLASRYAAVEKARKALLERQKDLEGK
TQQLEIKLSNKTEEDIKKARRKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTSLELERLEVERIEMIRQHL
CQYTQLRHETDMFNQSTVEPVDQ
>gnl|CDD|153334 cd07650, F-BAR_Syp1p_like, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of yeast Syp1 protein. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Syp1p is associated with septins, a family of GTP-binding proteins that serve as elements of septin filaments, which are required for cell morphogenesis and division. Syp1p regulates cell-cycle dependent septin cytoskeletal dynamics in yeast. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCH domain Only (FCHO) proteins and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
LSPYEATEILRIRLSQIKLVNTELADWLQERRRLERQYVQGLRKLARRNEPLNKSLLGVFQNPWLTIESE
TEFIAASHGELAQRIETDVEEPLRDFATSTEFMNTLDDDQNLSNLAKELDESQKKWDKLKKKHSKASSKA
VSAAVSDLEEARQQWDSQAPFLFELLQAIDEERLNHLKDVLLQFQTHESDYALRTTESAEECMNQLLEFD
TEDEIQRFARKASAGRFA
>gnl|CDD|153335 cd07651, F-BAR_PombeCdc15_like, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
GKNDAGFDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRLEKLSRKSLGGSEEGGLKNSLDTLRLETE
SMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHMEKLLKKKQDQEKYLEKAREKYEADCSKINSY
TLQSQLTWGKELEKNNAKLNKAQSSINSSRRDYQNAVKALRELNEIWNREWKAALDDFQDLEEERIQFLK
SNCWTFANNISTLCVDDDESCERIRS
>gnl|CDD|153336 cd07652, F-BAR_Rgd1, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
LNSDVGLSTLLDRLKQSIASAKEFATFLKKRAAIEEEHARGLKKLARTTLDTYKRPDHKQGSFSNAYHSS
LEFHEKLADNGLRFAKALNEMSDELSSLAKTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADD
LERVKTGDPGKKLKFGLKGNKSAAQHEDELLRKVQAADQDYASKVNAAQALRQELLSRHRPEAVKDLFDL
ILEIDAALRLQYQKYALPNELLVL
>gnl|CDD|153337 cd07653, F-BAR_CIP4-like, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 and similar proteins. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Members of this subfamily typically contain an N-terminal F-BAR domain and a C-terminal SH3 domain. In addition, some members such as FNBP1L contain a central Cdc42-binding HR1 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
TELWDQFDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRKLVKKYLPKKKEEDEYSFSSVKAFRSI
LNEVNDIAGQHELIAENLNSNVCKELKTLISELRQERKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFK
EAEKAKQKYEKADADMNLTKADVEKAKANANLKTQAAEEAKNEYAAQLQKFNKEQRQHYSTDLPQIFDKL
QELDEKRINRTVELLLQAAEIERKVIPIIAKCLDGIKKAGD
>gnl|CDD|153338 cd07654, F-BAR_FCHSD, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains proteins (FCHSD). F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of FCH and double SH3 domain (FCHSD) proteins, so named as they contain an N-terminal F-BAR domain and two SH3 domains at the C-terminus. Vertebrates harbor two subfamily members, FCHSD1 and FCHSD2, which have been characterized only in silico. Their biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
LRHLEQLSKLQAKHQTECDLLEDIRTYSQKKAAIEREYGQALQKLASQFLKREWPGSGELKPEDDRSGYT
VWGAWLEGLDAVAQSRQNRCEAYRRYISEPAKTGRSAKEQQLKKCTEQLQRAQAEVQQTVRELSKSRKTY
FEREQVAHLAREKAADVQAREARSDLSIFQSRTSLQKASVKLSARKAECSSKATAARNDYLLNLAATNAH
QDRYYQTDLPAIIKALDGELYDHLKDFLISLSHTELETAQVIQETFQRLLETSS
>gnl|CDD|153339 cd07655, F-BAR_PACSIN, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
FWEVGNYKRTVKRIEDGHKLCDDLMKMVQERAEIEKAYAKKLKEWAKKWRDLIEKGPEYGTLETAWKGLL
SEAERLSELHLSIRDKLLNDVVEEVKTWQKENYHKSMMGGFKETKEAEDGFAKAQKPWAKLLKKVEKAKK
AYHAACKAEKSAQKQENNAKSDTSLSPDQVKKLQDKVEKCKQEVSKTKDKYEKALEDLNKYNPRYMEDME
QVFDKCQEFEEKRLDFFKEILLSYHRHLDLSTNPSFKAIYRDLQQTII
>gnl|CDD|153340 cd07656, F-BAR_srGAP, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Proteins. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs, all of which are expressed during embryonic and early development in the nervous system but with different localization and timing. srGAPs contain an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
QQLSEQLKCLDLRTEAQVQLLADLQDYFRRRAEIELEYSRSLEKLADRFSSKHKNEKSKREDWSLLSPVN
CWNTLLVQTKQESRDHSTLSDIYSNNLVQRLGQMSEDLQRISKKCREIGSQLHDELLRVLNELQTAMKTY
HTYHAESKSAERKLKEAEKQEEKQEQSPEKKLERSRSSKKIEKEVEKRQAKYSEAKLKCTKARNEYLLNL
AAANATIHKYFVQDLSDLIDCMDLGFHNSLS
>gnl|CDD|153341 cd07657, F-BAR_Fes_Fer, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) and Fer (Fes related) tyrosine kinases. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Fes (feline sarcoma), also called Fps (Fujinami poultry sarcoma), and Fer (Fes related) are cytoplasmic (or nonreceptor) tyrosine kinases that play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Although Fes and Fer show redundancy in their biological functions, they show differences in their expression patterns. Fer is ubiquitously expressed while Fes is expressed predominantly in myeloid and endothelial cells. Fes and Fer contain an N-terminal F-BAR domain, an SH2 domain, and a C-terminal catalytic kinase domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. The F-BAR domain of Fes is critical in its role in microtubule nucleation and bundling
LQGQSGHEALLKRQDAELRLLETMKKYMAKRAKSDREYASTLGSLANQGLKIEAGDDLQGSPISKSWKEI
MDSTDQLSKLIKQHAEALESGTLDKLTLLIKDKRKAKKAYQEERQQIDEQYKKLTDEVEKLKSEYQKLLE
DYKAAKSKFEEAVVKGGRGGRKLDKARDKYQKACRKLHLCHNDYVLALLEAQEHEEDYRTLLLPGLLNSL
QSLQEEFITQWKKILQEYLRYSDLTTD
>gnl|CDD|153342 cd07658, F-BAR_NOSTRIN, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic INducer (NOSTRIN). F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Nitric Oxide Synthase TRaffic INducer (NOSTRIN) is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). NOSTRIN facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of NOSTRIN may be correlated to preeclampsia. NOSTRIN contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. The F-BAR domain of NOSTRIN is necessary and sufficient for its membrane association and is responsible for its subcellular localization
FMGQKGFEELRRYVKQGGDFCKELATVLQERAELELNYAKGLSKLSGKLSKASKSVSGTLSSAWTCVAEE
MESEADIHRNLGSALTEEAIKPLRQVLDEQHKTRKPVENEVDKAAKLLTDWRSEQIKVKKKLHGLARENE
KLQDQVEDNKQSCTKQKMLNKLKKSAEVQDKEDEKLEAKRKKGEESRLKAENEYYTCCVRLERLRLEWES
ALRKGLNQYESLEEERLQHLKHSLSQYLR
>gnl|CDD|153343 cd07659, BAR_PICK1, The Bin/Amphiphysin/Rvs (BAR) domain of Protein Interacting with C Kinase 1. The BAR domain of Arfaptin-like proteins, also called the Arfaptin domain, is a dimerization and lipid binding module that can detect and drive membrane curvature. Protein Interacting with C Kinase 1 (PICK1), also called Protein kinase C-alpha-binding protein, is highly expressed in brain and testes. PICK1 plays a key role in the trafficking of AMPA receptors, which are critical for regulating synaptic strength and may be important in cellular processes involved in learning and memory. PICK1 is also critical in the early stages of spermiogenesis. Mice deficient in PICK1 are infertile and show characteristics of the human disease globozoospermia such as round-headed sperm, reduced sperm count, and severely impaired sperm motility. PICK1 may also be involved in the neuropathogenesis of schizophrenia. PICK1 contains an N-terminal PDZ domain and a C-terminal BAR domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of PICK1 is necessary for its membrane localization and activation
NDGLVKKLEELEQTAELYKGLVEHTKRLLRAFYALSQTHKEFGDLFANIGVREPQPAASEAFTKFGEAHR
SIEKFGIELLKTLKPMLSDLGTYLNKAIPDTKLTIKKYADVKFEYLSYCLKVKEMDDEEYSYAALDEPLY
RVETGNYEYRLILRCRQEARARFAKLRQDVLEKLELLDQKHVQDIVFQLQRFVSALSEYHSDCHELLKEP
DLFPI
>gnl|CDD|153344 cd07660, BAR_Arfaptin, The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin. The BAR domain of Arfaptin-like proteins, also called the Arfaptin domain, is a dimerization and lipid binding module that can detect and drive membrane curvature. Arfaptins are ubiquitously expressed proteins implicated in mediating cross-talk between Rac, a member of the Rho family GTPases, and Arf (ADP-ribosylation factor) small GTPases. Arfaptins bind to GTP-bound Arf1, Arf5, and Arf6, with strongest binding to GTP-Arf1. Arfaptins also bind to Rac-GTP and Rac-GDP with similar affinities. The Arfs are thought to bind to the same surface as Rac, and their binding is mutually exclusive. Mammals contain at least two isoforms of Arfaptin. Arfaptin 1 has been shown to inhibit the activation of Arf-dependent phospholipase D (PLD) and the secretion of matrix metalloproteinase-9 (MMP-9), an enzyme implicated in cancer invasiveness and metastasis. Arfaptin 2 regulates the aggregation of the protein huntingtin, which is implicated in Huntington disease. Arfaptins are single-domain proteins with a BAR-like structure. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
DLELEAQIEVLRDTQRKYESVLRLARALASQFYQMLQTQKALGDAFADLSQKSPELQEEFTYNAETQKLL
CKNGETLLGALNFFVSSLNTLVNKTMEDTLMTVKQYESARIEYDAYRNDLEALNLGPRDAATSARLEEAQ
RRFQAHKDKYEKLRNDVSVKLKFLEENKVKVMHKQLLLFHNAISAYFSGNQKQLEQTLKQF
>gnl|CDD|153345 cd07661, BAR_ICA69, The Bin/Amphiphysin/Rvs (BAR) domain of Islet Cell Autoantigen 69-kDa. The BAR domain of Arfaptin-like proteins, also called the Arfaptin domain, is a dimerization and lipid binding module that can detect and drive membrane curvature. Islet cell autoantigen 69-kDa (ICA69) is a diabetes-associated autoantigen that is highly expressed in brain and beta cells. It is involved in membrane trafficking at the Golgi complex in neurosecretory cells. It is coexpressed with Protein Interacting with C Kinase 1 (PICK1), also a the BAR domain containing protein, in many tissues at different developmental stages. In neurons, ICA69 colocalizes with PICK1 in cell bodies and dendrites but is absent in synapses where PICK1 is enriched. ICA69 contains an N-terminal BAR domain and a conserved C-terminal domain of unknown function. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. ICA69 associates with PICK1 through their BAR domains to form a heterodimer which is involved in regulating the synaptic targeting and surface expression of AMPA receptors. Autoantibodies against ICA69 have been identified in patients with insulin-dependent diabetes mellitus, rheumatoid arthritis, and primary Sjogren's syndrome. ICA69 has also been shown to be released by pancreatic cancer cells
DAELDAKLELFRSVQDTCLELLKIIDNYQERLCILSQEENVLGKFLKEQGKIDKTTAGKMMAATGKALSF
SSQQRLALRVPLLRLYQEVETFRERAIADTLQTIQRMEKCRTEYRAALLWMKSVSQELDPDTYKQLEKFR
KAQAQVRSAKERFDKLKMDVCQKVDLLGASRCNLLSHALVTYQNTLLQFWEKTSRTMATIHEAF
>gnl|CDD|153346 cd07662, BAR_SNX6, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
DFFKNVVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDSSAKSDRMTRSHKSAADDYNRIGSSLYTL
GTQDSTDICKFFLKVSELFDKTRKIEARVAADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANK
ALDKARAKNKDVLQAETTQQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLL
QSCLAVLN
>gnl|CDD|153347 cd07663, BAR_SNX5, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
GFFKNMVKSADEVLFSGVKEVDEFFEQEKTFLVNYYNRIKDSCAKADKMTRSHKNVADDYIHISAALNSV
AAEEPTVIKKYLLKVAELFEKLRKVEDRVASDQDLKLTELLRYYMLNIEAAKDLLYRRARALADYENSNK
ALDKARLKSKDVKQAEAHQQECCQKFEKLSESAKQELISFKRRRVAAFRKNLIEMTELEIKHAKNNVSLL
QSCIDLFK
>gnl|CDD|153348 cd07664, BAR_SNX2, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX2 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
RMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVESLVCHRKELSANTAAFAKSAAMLG
NSEDHTALSRALSQLAEVEEKIDQLHQDQAFADFYLFSELLGDYIRLIAAVKGVFDQRMKCWQKWQDAQV
TLQKKREAEAKLQYANKPDKLQQAKDEIKEWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIK
YLESLVQTQQQLIKYWEAFLPEAK
>gnl|CDD|153349 cd07665, BAR_SNX1, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
KMFNKATDAVSKMTIKMNESDVWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELALNTALFAKSLAMLG
SSEDNTALSRALSQLAEVEEKIEQLHQEQANNDFFLLAELLADYIRLLSAVRGAFDQRMKTWQRWQDAQA
MLQKKREAEARLLWANKPDKLQQAKDEIAEWESRVTQYERDFERISATVRKEVIRFEKEKSKDFKNHIIK
YLETLLHSQQQLVKYWEAFLPEAK
>gnl|CDD|153350 cd07666, BAR_SNX7, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX7 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
HPTLTFNEDFKIFLTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMNEYVEAFSQKI
NVLDKISQRIYKEQREYFEELKEYGPIYTLWSASEEELADSLKGMASCIDRCCKATDKRMKGLSEQLLPV
IHEYVLYSETLMGVIKRRDQIQAELDSKVEALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQN
MQTDLRSAFTDMAENNISYYEECLATWESFLHS
>gnl|CDD|153351 cd07667, BAR_SNX30, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 30. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX30 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
HPVLSFNEHFNVFLTAKDLNAYKKQGIALLSKMGESVKYVTGGYKLRSRPLEFAAIGDYLDTFALKLGTI
DRIAQRIIKEEIEYLVELREYGPVYSTWSGLEGELAEPLEGVSACIGNCSTALEELTEDMTEDFLPVLRE
YILYSESMKNVLKKRDQVQAEYEAKLEAVALRKEERPKVPTDVEKCQDRVECFNADLKADMERWQNNKRQ
DFRQLLMGMADKNIQYYEKCLTAWESIIPL
>gnl|CDD|153352 cd07668, BAR_SNX9, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 9. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX9, also known as SH3PX1, is a cytosolic protein that interacts with proteins associated with clathrin-coated pits such as Cdc-42-associated tyrosine kinase 2 (ACK2). It binds class I polyproline sequences found in dynamin 1/2 and the WASP/N-WASP actin regulators. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis. Its array of interacting partners suggests that SNX9 functions at the interface between endocytosis and actin cytoskeletal organization. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
EAPDLDLVEIEQKCEAVGRFTKAMDDGVKELLTVGQEHWKRCTGPLPKEYQKIGKALQSLATVFSTSGYQ
GETDLNDAITEAGKTYEEIASLVAEQPKKDLHFLMETNHEYKGFLGCFPDIIGAHKGAIEKVKESDKLVA
TSKITLQDKQNMVKRVSTMSYALQAEMNHFHSNRIYDYNSVIRLYLEQQVQFYETIAEKLRQALSRFPVM
>gnl|CDD|153353 cd07669, BAR_SNX33, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 33. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX33 interacts with Wiskott-Aldrich syndrome protein (WASP) and plays a role in the maintenance of cell shape and cell cycle progression. It modulates the shedding and endocytosis of cellular prion protein (PrP(c)) and amyloid precursor protein (APP). BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
PTEHQDLQDVEERVDVFKAFSKKMDDSVLQLSNVASELVRKHLGGFRKEFQKLGNAFQAISHSFQLDPPY
SSEALNNAISHTGRTYEAVGEMFAEQPKNDLFQMLDTLSLYQGLLSNFPDIIHLQKGAFAKVKESQRMSD
EGRMDQDEADGIRKRCRVVGFALQAEMNHFHQRRELDFKQMMQHYLRQQIIFYQRVSQQLEKTLRMY
>gnl|CDD|153354 cd07670, BAR_SNX18, The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 18. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions
PSAVLDLQDVESRIDGFKAFTKKMDESVLQLNHTANEFARKQVTGFKKEYQKVGQSFKGLSQAFELDQQA
FSAGLNQAIAFTGEAYEAIGELFAEQPRQDLDPVMDLLALYQGHLANFPDIIHVQKGALTKVKESKKHVE
EGKMELQKADGIQDRCNIISFATLAEIHHFHKIRVRDFKSQMQHFLQQQIRFFQKVTQKLEEALQKY
>gnl|CDD|153355 cd07671, F-BAR_PSTPIP1, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 1 (PSTPIP1), also known as CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
FTLNTGYEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELVQIARKAGGQTEINTLKASFDQLKQQIE
NIGNSHIQLAGMLREELKSLEEFRERQKEQRKKYEAVMERVQKSKVSLYKKTMESKKTYEQRCREADEAE
QTFERSSSTGNPKQSEKSQNKAKQCRDAATEAERVYKQNIEQLDKARTEWETEHILTCEVFQLQEDDRIT
ILRNALWVHCNHFSMQCVKDDELYEEVRTTLE
>gnl|CDD|153356 cd07672, F-BAR_PSTPIP2, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 2. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2), also known as Macrophage Actin-associated tYrosine Phosphorylated protein (MAYP), is mostly expressed in hematopoietic cells but is also expressed in the brain. It is involved in regulating cell adhesion and motility. Mutations in the gene encoding murine PSTPIP2 can cause autoinflammatory disorders such as chronic multifocal osteomyelitis and macrophage autoinflammatory disease. PSTPIP2 contains an N-terminal F-BAR domain and lacks the PEST motifs and SH3 domain that are found in PSTPIP1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
LTSTGGYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGQTEINTLKRSLDVFKQQI
DNVGQSHIQLAQTLRDEAKKMEDFRERQKLARKKIELIMDAIHKQRAMQFKKTMESKKNYEQKCRDKDEA
EQAVNRNANLVNVKQQEKLFAKLAQSKQNAEDADRLYMQNISVLDKIREDWQKEHVKACEFFEKQECERI
NFFRNAVWTHVNQLSQQCVTSDEMYEEVRK
>gnl|CDD|153357 cd07673, F-BAR_FCHO2, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. The specific function of FCH domain Only 2 (FCHO2) is still unknown. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO1 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
YFLENFWGEKNSGFDVLYHNMKHGQISTKELSDFIRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWD
VFKTSTEKLANCHLELVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQNIQSITQALQKSKENYN
AKCLEQERLKKEGATQREIEKAAVKSKKATESYKLYVEKYALAKADFEQKMTETAQKFQDIEETHLIRIK
EIIGSYSNSVKEIHIQIGQVHEEFINNMANTTVESLIQKFAESKGTGKERPGPIEFEEC
>gnl|CDD|153358 cd07674, F-BAR_FCHO1, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH domain Only 1 (FCHO1) may be involved in clathrin-coated vesicle formation. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO2 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
GEKNAGFDVLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKMASNGSPLGTFAPMWEVFRVSSD
KLALCHLELMRKLNDLIKDINRYGDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQE
RLRREGVPQKELEKAELKTKKAAESLRGSVEKYNRARGDFEQKMLESAQKFQDIEETHLRHMKLLIKGYS
HSVEDTHVQIGQVHEEFKQNVENVGVENLIRKFAESKGTGKERPGPVGFEE
>gnl|CDD|153359 cd07675, F-BAR_FNBP1L, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 1-Like. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FormiN Binding Protein 1-Like (FNBP1L), also known as Toca-1 (Transducer of Cdc42-dependent actin assembly), forms a complex with neural Wiskott-Aldrich syndrome protein (N-WASP). The FNBP1L/N-WASP complex induces the formation of filopodia and endocytic vesicles. FNBP1L is required for Cdc42-induced actin assembly and is essential for autophagy of intracellular pathogens. It contains an N-terminal F-BAR domain, a central Cdc42-binding HR1 domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
TELWDQFDNLDKHTQWGIDFLERYAKFVKERLEIEQNYAKQLRNLVKKYCPKRSSKDEEPRFTSCLSFYN
ILNELNDYAGQREVVAEEMGHRVYGELMRYSHDLKGERKMHLQEGRKAQQYLDMCWKQMDNSKKKFEREC
REAEKAQQSYERLDNDTNATKSDVEKAKQQLNLRTHMADESKNEYAAQLQNFNGEQHKHFYIVIPQIYKQ
LQEMDERRTVKLSECYRGFADSERKVIPIISKCLEGMVLAAK
>gnl|CDD|153360 cd07676, F-BAR_FBP17, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Formin Binding Protein 17 (FBP17), also called FormiN Binding Protein 1 (FNBP1), is involved in dynamin-mediated endocytosis. It is recruited to clathrin-coated pits late in the endocytosis process and may play a role in the invagination and scission steps. FBP17 binds in vivo to tankyrase, a protein involved in telomere maintenance and mitogen activated protein kinase (MAPK) signaling. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
TELWDQFDNLEKHTQWGIEVLEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCRAFL
MTLNEMNDYAGQHEVISENLASQIIVELTRYVQELKQERKSHFHDGRKAQQHIETCWKQLESSKRRFERD
CKEADRAQQYFEKMDADINVTKADVEKARQQAQIRHQMAEDSKAEYSSYLQKFNKEQHEHYYTHIPNIFQ
KIQEMEERRIGRVGESMKTYAEVDRQVIPIIGKCLDGITKAAE
>gnl|CDD|153361 cd07677, F-BAR_FCHSD2, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 2 (FCHSD2). F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH and double SH3 domains 2 (FCHSD2) contains an N-terminal F-BAR domain and two SH3 domains at the C-terminus. It has been characterized only in silico, and its biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
NIQVEQMTKLQAKHQAECKLLEDEREFSQKIAAIESEYAQKEQKLASQYLKSDWRGMKADERADYRSMYT
VWKSFLEGTMQVAQSRINICENYKNLISEPARTVRLYKEQQLKRCVDQLTKIQAELQETVKDLAKGKKKY
FETEQMAHAVREKADIEAKSKLSLFQSRISLQKASVKLKARRSECNSKATHARNDYLLTLAAANAHQDRY
YQTDLVNIMKALDGNVYDHLKDYLMAFSRTELETCQAVQNTFQFLLETSS
>gnl|CDD|153362 cd07678, F-BAR_FCHSD1, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 (FCHSD1). F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH and double SH3 domains 1 (FCHSD1) contains an N-terminal F-BAR domain and two SH3 domains at the C-terminus. It has been characterized only in silico, and its biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
LRFLEQLSILQTKQQRDAELLEDIRSYSKQRAAIEREYGQALQRLASQFLKRDWHRGGNETEMDRSVRTV
WGAWREGTAATGQGRVTRLEAYRRLRDEAGKTGRSAKEQVLKKSTEQLQKAQAELLETVKELSKSKKLYG
QLERVSEVAKEKAADVEARLNKSDHGIFHSKASLQKLSAKFSAQSAEYSQQLQAARNEYLLNLVAANAHL
DHYYQEELPAIMKALDGDLYERLRDPLTSLSHTELEACEVTQEHFHRIEQATS
>gnl|CDD|153363 cd07679, F-BAR_PACSIN2, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 2 (PACSIN2). F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 2 or Syndapin II is expressed ubiquitously and is involved in the regulation of tubulin polymerization. It associates with Golgi membranes and forms a complex with dynamin II which is crucial in promoting vesicle formation from the trans-Golgi network. PACSIN 2 contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
FWEVGNYKRTVKRIDDGHRLCNDLMNCLHERARIEKVYAQQLTEWAKRWRQLVEKGPQYGTVEKAWCALM
SEAEKVSELHLEVKASLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKK
AYHTACKEEKLATSREANSKADPALNPEQLKKLQDKVEKCKQDVLKTKEKYEKSLKELDQTTPQYMENME
QVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKNIYRELEQSIK
>gnl|CDD|153364 cd07680, F-BAR_PACSIN1, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1). F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
FWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIM
TEADKVSELHQEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKK
AYHLACKEEKLAMTREANSKAEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLDDVGKTTPQYMENME
QVFEQCQQFEEKRLVFLKEVLLDIKRHLNLAESSSYAHVYRELEQTIR
>gnl|CDD|153365 cd07681, F-BAR_PACSIN3, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3). F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 3 or Syndapin III is expressed ubiquitously and regulates glucose uptake in adipocytes through its role in GLUT1 trafficking. It also modulates the subcellular localization and stimulus-specific function of the cation channel TRPV4. PACSIN 3 contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
FWEAGNYRRTVKRIEDGYRLCNDLVSCFQERAKIEKGYAQQLSDWARKWRGIVEKGPQYGTLEKAWHAFL
TAAERLSEIHLELRENLVGEDSEKVRAWQKEAFHKQMIGGFRESKEAEEGFRKAQKPWVKKLKEVESSKK
GYHAARKDERTAQTRETHAKADSTVSQEQLRKLQDRVEKCTQEAEKAKEQYEKALEELNRYNPRYMEDME
QAFEICQEAERKRLCFFKEMLLDLHQHLDLSSSDSFHALYRDLHQTIS
>gnl|CDD|153366 cd07682, F-BAR_srGAP2, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Protein 2. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs. srGAP2 is expressed in zones of neuronal differentiation. It plays a role in the regeneration of neurons and axons. srGAP2 contains an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
AQLVEQLKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSP
VNCWNLLLNQVKRESRDHATLSDIYLNNIIPRFVQISEDSGRLFKKSKEVGLQLQEDLMKVLNELYTVMK
TYHMYNADSISAQSKLKEAEKQEEKQMSRSVRQEDRQTPRSPDSTTNIRIEEKHVRRSSVKKIEKMKEKR
QAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDCCDLGYHASLN
>gnl|CDD|153367 cd07683, F-BAR_srGAP1, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Protein 1. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs. srGAP1, also called Rho GTPase-Activating Protein 13 (ARHGAP13), is a Cdc42- and RhoA-specific GAP and is expressed later in the development of CNS (central nervous system) tissues. It is an important downstream signaling molecule of Robo1. srGAP1 contains an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
AQLVEQQKCLEQQTEMRVQLLQDLQDFFRKKAEIESEYSRNLEKLAERFMAKTRSTKDHQQYKKDQNLLS
PVNCWYLLLNQVRRESKDHATLSDIYLNNVIMRFMQISEDSTRMFKKSKEIAFQLHEDLMKVLNELYTVM
KTYHMYHTESISAESKLKEAEKQEEKQIGRSGDPVFHIRLEDRHQRRSSVKKIEKMKEKRQAKYSENKLK
SIKARNEYLLTLEATNASVFKYYIHDLSDLIDCCDLGYHASLN
>gnl|CDD|153368 cd07684, F-BAR_srGAP3, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Protein 3. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs. srGAP3, also called MEGAP (MEntal disorder associated GTPase-Activating Protein), is a Rho GAP with activity towards Rac1 and Cdc42. It impacts cell migration by regulating actin and microtubule cytoskeletal dynamics. The association between srGAP3 haploinsufficiency and mental retardation is under debate. srGAP3 contains an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
TQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIRTSREHQFKKDQQLLSP
VNCWYLVLEQTRRESRDHATLNDIFNNNVIVRLSQISEDVIRLFKKSKEIGLQMHEELLKVTNELYTVMK
TYHMYHAESISAESKLKEAEKQEEKQFNKSGDISSNLLRHEERPQRRSSVKKIEKMKEKRQAKYSENKLK
CTKARNDYLLNLAATNAAVSKYYIHDVSDLIDCCDLGFHASLA
>gnl|CDD|153369 cd07685, F-BAR_Fes, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) tyrosine kinase. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Fes (feline sarcoma), also called Fps (Fujinami poultry sarcoma), is a cytoplasmic (or nonreceptor) tyrosine kinase whose gene was first isolated from tumor-causing retroviruses. It is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells, and plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. Fes kinase has also been implicated as a tumor suppressor in colorectal cancer. It contains an N-terminal F-BAR domain, an SH2 domain, and a C-terminal catalytic kinase domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. The F-BAR domain of Fes is critical in its role in microtubule nucleation and bundling
LWCPQGHAALLRLQDSELRLMEVMKKWMSQRAKSDREYSGMLHHMSAQVEKLDRSQHGALSMLSSPISQS
WAVLVSQTETLSQVLRKHAEDLNAGPLSKLSLLIRDKQQLRKTFSEQWQLLKQEYTKTTQQDIEKLKSQY
RSLAKDSAQAKRKYQEASKDKDRDKAKEKYVKSLWKLYALHNEYVLAVRAAQLHHQHHYQRILPGLLESL
QSLHEEMVLILKEILQEYFEISSLVQE
>gnl|CDD|153370 cd07686, F-BAR_Fer, The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fer (Fes related) tyrosine kinase. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Fer (Fes related) is a cytoplasmic (or nonreceptor) tyrosine kinase expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells. It contains an N-terminal F-BAR domain, an SH2 domain, and a C-terminal catalytic kinase domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules
SDLRNSHEALLKLQDWELRLLETVKKFMALRVKSDKEYASTLQNLCNQVDKESTSQLDYVSNVSKSWLHM
VQQTEQLSKIMKTHAEELNSGPLHRLTMMIKDKQQVKKSYIGVHQQIEAEMYKVTKTELEKLKCSYRQLT
KEVNSAKEKYKDAVAKGKETEKARERYDKATMKLHMLHNQYVLAVKGAQLHQHQYYDFTLPLLLDSLQKM
QEEMIKALKGILDEYSQITSLVTE
>gnl|CDD|409484 cd07687, IgC_TCR_delta, Immunoglobulin (Ig) constant domain of the delta chain of delta/gamma T-cell antigen receptors (TCRs). The members here are composed of the constant domain of the delta chain of delta/gamma T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. The majority of T cells contain alpha-beta TCRs, but a small subset contain gamma-delta TCRs. Alpha-beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma-delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing and MHC independently of the bound peptide. Gamma-delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds
SPSVFVMKNGTNVACLVKNFYPKEVTISLSSSKKIIEFDPAIVISPNGKYSAVKLGKYGDSDSVTCSVQH
SNKTVHSTDF
>gnl|CDD|409485 cd07688, IgC_TCR_alpha, Immunoglobulin (Ig) constant domain the alpha chain of alpha/beta T-cell antigen receptors (TCRs). The members here are composed of the constant domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group includes the variable domain of the alpha chain. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The antigen binding site is formed by the variable domains of the alpha and beta chains, located at the N-terminus of each chain. Alpha/beta TCRs recognize antigens differently from gamma/delta TCRs
EPAVYQLKDPRSSDISVCLFTDFDSQTNVTKSMDSETVFITNKTVLDMKSMDSKSNGAVAWSNQSDFECA
DAFKNTDPFYPSA
>gnl|CDD|409486 cd07689, IgC2_VCAM-1, Immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1) and similar proteins; member of the C2-set of IgSF domains. The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1; also known as Cluster of Differentiation (CD) 106) and similar proteins. During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. The interaction of VCAM-1 binding to the beta1 integrin very late antigen 4 (VLA-4) expressed by lymphocytes and monocytes mediates the adhesion of leucocytes to blood vessel walls, and regulates migration across the endothelium. During metastasis, some circulating cancer cells extravasate to a secondary site by a similar process. VCAM-1 may be involved in organ targeted tumor metastasis and may also act as host receptors for viruses and parasites. VCAM-1 contains seven Ig domains
PKDPEIEMSGPLVAGKPVTVSCSVPDVYPFDRLEIELLKGETLLESKEFLEDMDKKSLETKSLEVTFIPT
IEDTGKVLVCRAKLHIDEMEFEPKQRQSTQE
>gnl|CDD|409487 cd07690, IgV_1_CD4, First immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 4; member of the V-set of IgSF domains. The members here are composed of the first immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 4. CD4 and CD8 are the two primary co-receptor proteins found on the surface of T cells, and the presence of either CD4 or CD8 determines the function of the T cell. CD4 is found on helper T cells, where it is required for the binding of MHC (major histocompatibility complex) class II molecules, while CD8 is found on cytotoxic T cells, where it is required for the binding of MHC class I molecules. CD4 contains four immunoglobulin domains, with the first three included in this hierarchy. The fourth domain has a general Ig architecture, but has slight topological changes in the arrangement of beta strands relative to the other structures in this family and is not specifically included in the hierarchy
KKVVLGKKGDTAELPCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRNLWDQGSFPLI
IKNLKIEDSDTYICEVEDKKEEVELLV
>gnl|CDD|409488 cd07691, IgC1_CD3_gamma_delta, Immunoglobulin (Ig)-like domain of Cluster of Differentiation (CD) 3 gamma and delta chains; member of the C1-set of IgSF domains. The members here are composed of immunoglobulin (Ig)-like domain of Cluster of Differentiation (CD) 3 gamma and delta chains. CD3 is a T cell surface receptor that is associated with alpha/beta T cell receptors (TCRs). The CD3 complex consists of one gamma, one delta, two epsilon, and two zeta chains. The CD3 subunits form heterodimers as gamma/epsilon, delta/epsilon, and zeta/zeta. The gamma, delta, and epsilon chains each contain an extracellular Ig domain, whereas the extracellular domains of the zeta chains are very small and have unknown structure. The CD3 domain participates in intracellular signaling once the TCR has bound an MHC/antigen complex
SVKENEDKVFLKCNSASSITWKKGTEGIEASDKTDLDLGSRINDPRGTYQCKGSENKEKTLQVHYRMCQ
>gnl|CDD|409489 cd07692, IgC1_CD3_epsilon, Immunoglobulin (Ig)-like domain of Cluster of Differentiation (CD) 3 epsilon chain; member of the C1-set of IgSF domains. The members here are composed of the immunoglobulin (Ig)-like domain of Cluster of Differentiation (CD) 3 epsilon chain. CD3 is a T cell surface receptor that is associated with alpha/beta T cell receptors (TCRs). The CD3 complex consists of one gamma, one delta, two epsilon, and two zeta chains. The CD3 subunits form heterodimers as gamma/epsilon, delta/epsilon, and zeta/zeta. The gamma, delta, and epsilon chains each contain an extracellular Ig domain, whereas the extracellular domains of the zeta chains are very small and have unknown structure. The CD3 domain participates in intracellular signaling once the TCR has bound an MHC/antigen complex
YKVSISGTSVELTCPKDFENGIQWKRNDNNEQMKGHNEKYLSLKEFSEMESSGYYQCYATEGNTEAAHYL
YLRAR
>gnl|CDD|409490 cd07693, IgC_1_Robo, First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains. The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site
PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRSHRIVLPSGSLFFLRVVHGRK
GRSDEGVYVCVAHNSLGEAVSRNASLEVA
>gnl|CDD|409491 cd07694, IgC2_2_CD4, Second immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 4; member of the C2-set of IgSF domains. The members here are composed of the second immunoglobulin (Ig) Constant 2 (C2)-set domain of Cluster of Differentiation (CD) 4. CD4 and CD8 are the two primary co-receptor proteins found on the surface of T cells, and the presence of either CD4 or CD8 determines the function of the T cell. CD4 is found on helper T cells, where it is required for the binding of MHC (major histocompatibility complex) class II molecules, while CD8 is found on cytotoxic T cells, where it is required for the binding of MHC class I molecules. CD4 contains four immunoglobulin domains, with the first three included in this hierarchy. The fourth domain has a general Ig architecture, but has slight topological changes in the arrangement of beta strands relative to the other structures in this family and is not specifically included in the hierarchy. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand
FKLTATSSDHVLSGTNLTLTLHGSSNSLPAFKVEWRGPGNKSKQILNQDKKTLNLVQLGPNDSGTWDCIV
SVNSSEKTLKLDIKVLAF
>gnl|CDD|409492 cd07695, IgV_3_CD4, Third immunoglobulin (Ig) Variable (V) domain of Cluster of Differentiation (CD) 4; member of the V-set of IgSF domains. The members here are composed of the third immunoglobulin variable (IgV) domain of Cluster of Differentiation (CD) 4. CD4 and CD8 are the two primary co-receptor proteins found on the surface of T cells, and the presence of either CD4 or CD8 determines the function of the T cell. CD4 is found on helper T cells, where it is required for the binding of MHC (major histocompatibility complex) class II molecules, while CD8 is found on cytotoxic T cells, where it is required for the binding of MHC class I molecules. CD4 contains four immunoglobulin domains, with the first three included in this hierarchy. The fourth domain has a general Ig architecture, but has slight topological changes in the arrangement of beta strands relative to the other structures in this family and is not specifically included in the hierarchy
SEIVYTKVGEQVEFSFPLNFTKEKWKEGGSGELWWQAEGASSSKSWITFSLKNKEVSVKRVTQDPKLQMG
KKLPLDLTLPQVLPQHAGSGNLTLALETGKLEQEVNL
>gnl|CDD|409493 cd07696, IgC1_CH3_IgAEM_CH2_IgG, CH3 domain (third constant Ig domain of heavy chains) in immunoglobulin heavy alpha, epsilon, and mu chains, and CH2 domain (second constant Ig domain of the gheavy chain) in immunoglobulin heavy gamma chain; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the third immunoglobulin constant domain (IgC) of the gamma heavy chains and the second immunoglobulin constant domain (IgC) of alpha, epsilon, and mu heavy chains. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns
VSVFLIPPSPKDLFLTKSAKVTCLVVDLTSIEEVNVTWSREDGNEVLASTTNPEKHYNATLSVVSTLTVC
ADDWDNGKTFKCKVTHPDLPSPIVKSIQ
>gnl|CDD|409494 cd07697, IgC1_TCR_gamma, T cell receptor (TCR) gamma chain constant immunoglobulin domain; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin (Ig) constant (C) domain of the gamma chain of gamma-delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha-beta TCRs, but a small subset contain gamma-delta TCRs. Alpha-beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma-delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing and MHC independently of the bound peptide. Gamma-delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds
SPKPTIFLPSIAETEKQKAGTYLCLLENFFPDVIKIHWREKKSDTILESQEGNTEKTKDTYMKFSWLTVP
KKSLGKEHRCIYKHENNKNGVKQEIIFP
>gnl|CDD|409495 cd07698, IgC1_MHC_I_alpha3, Class I major histocompatibility complex (MHC) alpha chain, alpha3 immunoglobulin domain; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class I alpha chain. Class I MHC proteins bind antigenic peptide fragments and present them to CD8+ T lymphocytes. Class I molecules consist of a transmembrane alpha chain and a small chain called the beta-2-microglobulin. The alpha chain contains three extracellular domains, two of which fold together to form the peptide-binding cleft (alpha1 and alpha2), and one which has an Ig fold (alpha3). Peptide binding to class I molecules occurs in the endoplasmic reticulum (ER) and involves both chaperones and dedicated factors to assist in peptide loading. Class I MHC molecules are expressed on most nucleated cells
DPPKVHVTHHPRSDGESTLRCWALGFYPAEITLTWQRDGEDQTQDMELVETRPNGDGTFQKWAAVVVPSG
EEQRYTCHVQHEGLPEPLTLRW
>gnl|CDD|409496 cd07699, IgC1_L, Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin (Ig) light chain constant (C) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determine the type of immunoglobulin: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains
APSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGVTTSKTEQQSDNTYSMSSYLTLS
SSDWNKHKVYTCEVTHEGLSSTITKSFNR
>gnl|CDD|409497 cd07700, IgV_CD8_beta, Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain. The members here are composed of the immunoglobulin (Ig)-like domain in Cluster of Differentiation (CD) 8 beta. The CD8 glycoprotein plays an essential role in the control of T-cell selection, maturation, and the T-cell receptor (TCR)-mediated response to peptide antigen. CD8 is comprised of alpha and beta subunits and is expressed as either an alpha/alpha or alpha/beta dimer. Both dimeric isoforms can serve as a coreceptor for T cell activation and differentiation, however they have distinct physiological roles, different cellular distributions, unique binding partners, etc. Each CD8 subunit is comprised of an extracellular domain containing a V-type Ig-like domain, a single pass transmembrane portion, and a short intracellular domain. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology
LLQTPGSLLVQTNQTVKMSCEAKTSPKNTRIYWLRQRQAPSKDSHFEFLASWDPSKGIVYGEGVDQEKLI
ILSDSDSSRYILSLMSVKPEDSGTYFCMTVGSPELIFGTGTKLSVV
>gnl|CDD|409498 cd07701, IgV_1_Necl-3, First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule-3; member of the V-set of Ig superfamily (IgSF) domains. The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of nectin-like molecule-3, Necl-3 (also known as cell adhesion molecule 2 (CADM2), SynCAM2, IGSF4D). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 - Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region, belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-3 accumulates in central and peripheral nervous system tissue, and has been shown to selectively interact with oligodendrocytes
FPLTQNVTVVEGGTANLTCRVDQNDNTSLQWSNPAQQTLYFDDKKALRDNRIELVRASWHELSISISDVS
LSDEGQYTCSLFTMPVKTSKAYLTVL
>gnl|CDD|409499 cd07702, IgI_VEGFR-1, Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1); member of the I-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1). VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-1 binds VEGF-A strongly; VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-1 may play an inhibitory role in the function of VEGFR-2 by binding VEGF-A and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis and may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand
FITVKHRKQQVLETFAGQKSYRLSMKVKAFPSPEVIWLKDGLPATEKCARYLTRGYSLIIKDVTEEDAGN
YTILLSIKQSNLFKNLTATLIV
>gnl|CDD|409500 cd07703, IgC1_2_Nectin-2_Necl-5_like, Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; member of the C1-set of the Ig superfamily (IgSF) domains. The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'
PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEA
NGKEVTCKVEHETLEEPQLLPVTLSVR
>gnl|CDD|409501 cd07704, IgC1_2_Nectin-3-4_like, Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related protein 4), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the second immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 or cluster of differentiation (CD) 113) and nectin-4 (poliovirus receptor related protein 4). Nectin-3 and nectin-4 belong to the nectin family comprised of four transmembrane glycoproteins (nectin-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. Nectin-3 has also been shown to form a heterophilic trans-interaction with nectin-1 in ciliary epithelia, establishing the apex-apex adhesion between the pigment and non-pigment cell layers. Nectin-4 has recently been identified in several types of breast carcinoma and can be used as a histological and serological marker for breast cancer
PLVSLNPGPALLIDGGNETLAASCTAETGKPAASVTWETDLGGMESSRTFEHNRTATVTSEYHLVPTRFA
NGRPLTCVVSHPALQQDIRITHILDV
>gnl|CDD|409502 cd07705, IgI_2_Necl-1, Second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1); member of the I-set of Ig superfamily domains. The members here are composed of the second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1; also known as cell adhesion molecule3 (CADM3)). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains is essential to cell-cell adhesion and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues and is a putative tumour suppressor gene which is downregulated in aggressive neuroblastoma. Ig domains are likely to participate in ligand binding and recognition
LGIPQKPQITGYESAFKEKDKAKLRCTSSGSKPAANIKWRKGDQELEGAPTSVQEDGNGKTFTVSSSVEF
QVTREDDGAEITCSVGHESLHDSDRSTSQRIEV
>gnl|CDD|409503 cd07706, IgV_TCR_delta, Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain. The members here are composed of the immunoglobulin (Ig) variable (V) domain of the delta chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing, and MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology
KVTQAQPDVSVQVGEEVTLNCRYETSWTNYYLFWYKQLPSGEMTFLIRQDSSEQNAKSGRYSVNFQKAQK
SISLTISALQLEDSAKYFCALSLPYDTDKLIFGKGTRLTVEP
>gnl|CDD|293793 cd07707, MBL-B1-B2-like, metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B1 MBls include chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I
LSLTQINGPVWVVTDLGSVPSNGLVYNGSKGLVLVDSTWTPKTTKELIKEIEKVSQKPVTEVINTHFHTD
RAGGNAYLKERGAKTVSTALTRDLAKSEWAEIVAFTRKGLPEYPDLGYELPDGVLDGDFNLQFGKVEAFY
PGPAHTPDNIVVYFPQENVLYGGCIIKETDLGNVADADVKEWPTSIERLKKRYRNIKAVIPGHGEVGGPE
LLDHTLDLL
>gnl|CDD|293794 cd07708, MBL-B3-like, metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His)
WPNPFPPFQIAGNTYYVGTDDLAAYLIVTPQGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAH
FDHAGGSAEIKKQTGAKVMAGAEDVSLLLSGGSSDFHYANDSSTYFPQSTVDRAVHDGERVTLGGTVLTA
HATPGHTPGCTTWTMTLKDHGKQYQVVFADSLTVNPGYRLVDNPTYPKIVEDYRHSFAVVEAMRCDILLG
PHPGVFDMKNKYVLLSKGQNNPFVDPGGCKAYAEAKAN
>gnl|CDD|293795 cd07709, flavodiiron_proteins_MBL-fold, catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain. FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain
VEIADDIYWVGVNDWDLRLFEGEYPTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKID
YIVVNHQEPDHSGSLPELLELAPNAKIVCSKKAARFLKHFYPGIDERFVVVKDGDTLDLGKHTLKFIPAP
MLHWPDTMVTYDPEDKILFSGDAFGAHGASGELFDDEVEDYLEEARRYYANIMGPFSKQVRKALEKLEAL
DIKMIAPSHGPIWRKDPGEIIDLYRDWS
>gnl|CDD|293796 cd07710, arylsulfatase_Sdsa1-like_MBL-fold, Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain. Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
GLFEVTDGVYQVRGYDLSNMTFIEGDTGLIIIDTLESAEAAKAALELFRKHTGDKPVKAIIYTHSHPDHF
GGAGGFVEEEDSGKVPIIAPEGFMEEAVSENVLAGNAMSRRAAYQFGALLPKGEKGQVGAGLGPGLSTGT
VGFIPPTITITETGETLTIDGVELEFQHAPGEAPDEMMVWLPDYKVLFCADNVYHTFPNLYTLRGAKYRD
ALAWAKSLDEAISLKAEVLFPSHTWPVWG
>gnl|CDD|293797 cd07711, MBLAC1-like_MBL-fold, uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain. Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
EVKVLVEGYARRDSDGGFRASSTVTLIKDGGKNILVDTGTPWDRDLLLKALAEHGLSPEDIDYVVLTHGH
PDHIGNLNLFPNATVIVGWDICGDSYDDHSLEEGDGYEIDENVEVIPTPGHTPEDVSVLVETEKKGTVAV
AGDLFEREEDLEDPILWDPLSEDPELQEESRKRILALADWIIPGHGPPFK
>gnl|CDD|293798 cd07712, MBLAC2-like_MBL-fold, uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain. Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
LFIEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEEVYVHPA
DAEILAAPDNFETLTWDAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFS
GDVVYDGPLIMDLPHSDLDDYLASLEKLSKLPDEFDKVLPGH
>gnl|CDD|293799 cd07713, DHPS-like_MBL-fold, Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain. This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
KITVLVDNTAGDEGLLAEHGLSLLIETEGKKILFDTGQSGVLLHNAKKLGIDLSDIDAVVLSHGHYDHTG
GLKALLELNPKAPVYAHPDAFEPRYSKRGGGKKGIGIGREELEKAGARLVLVEEPTEIAPGVYLTGEIPR
VTDFEKGNPGLFVKEDGGLVPDDFEDEQALVIDTKKGLVVITGCSHAGIVNILEHAKKLTGGDKIYAVIG
GFHLVGASEERIEKTIAALKELGVEKIYPGHCTGFKAIAALKEALGDKFIPLGVGTVIE
>gnl|CDD|293800 cd07714, RNaseJ_MBL-fold, RNAaseJ, MBL-fold metallo-hydrolase domain. RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIG
ALPYLLPELNVPIYATPLTLALIKKKLEEFKLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLA
IKTPEGTIVHTGDFKFDQTPVDGKPTDLEKLAELGKEGVLLLLSDSVHVSGHASQEDLKLMINLLKPKYF
IPVHGEYRHLVAHAKLAEELGIPEENIFLLENGDVLEL
>gnl|CDD|293801 cd07715, TaR3-like_MBL-fold, MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain. Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
RFWGVRGSIPVPGPDTVRYGGNTSCVEVRAGGELLILDAGTGIRELGNELMKEGPPGEAHLLLSHTHWDH
IQGFPFFAPAYDPGNRIHIYGPHKDGGSLEEVLRRQMSPPYFPVPLEELLAAIEFHDLEPGEPFSIGGVT
VTTIPLNHPGGALGYRIEEDGKSVVYATDTEHYPDDGESDEALLEFARGADLLIHDAQYTDEEYPSKRGW
GH
>gnl|CDD|293802 cd07716, RNaseZ_short-form-like_MBL-fold, uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain. The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
KLTVLGCSGSYPGPGGACSGYLLEADGFRILLDCGSGVLSRLQRYIDPEDLDAVVLSHLHPDHCADLGVL
QYARRYHPRGARKPPLPLYGPAGPAERLAALYGLEDVFDFHPIEPGEPLEIGPFTITFFRTVHPVPCYAM
RIEDGGKVLVYTGDTGYCDELVEFARGADLLLCEA
>gnl|CDD|293803 cd07717, RNaseZ_ZiPD-like_MBL-fold, Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold metallo-hydrolase domain. The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
LTFLGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGL
LSTMSLLGRTEPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEPDPGLVFEDDGFTVTAFPLDHRVP
CFGYRFEEGRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGVKK
LVLTHFSARYKDPEELLKEARAVFPNTILAEDFMTIE
>gnl|CDD|293804 cd07718, RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold, Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase domain. The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEEADEVLRNLKCIFISHLHADH
HLGLIRLLAERKKLFKPPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDL
LSNLLEELGLKSIETVPVIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT
>gnl|CDD|293805 cd07719, arylsulfatase_AtsA-like_MBL-fold, Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain. Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily
RVTLLGTGGPIPDPDRAGPSTLVVVGGRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPA
LLLTAWLAGRKTPLPVYGPPGTRALVDGLLAAYALDIDYRARIGDEGRPDPGALVEVHEIAAGGVVYEDD
GVKVTAFLVDHGPVPPALAYRFDTPGRSVVFSGDTGPSENLIELAKGADLLVH
>gnl|CDD|293806 cd07720, OPHC2-like_MBL-fold, Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain. Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
FKVGDFEVTALSDGTLPLPLDLLLGGAAPEAEAALLAAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGL
FGPTAGKLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLVDAGGKPVFPNAEVHVSEAEWDFWLDDANAAK
APEGAKRFFDAARDRLRPYAAAGRFEDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHHPA
LQFAHPDWTIAFDVDPEQAAATRRRLLDRAAAEGLLVAGAH
>gnl|CDD|293807 cd07721, yflN-like_MBL-fold, uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain. This subgroup includes the uncharacterized Bacillus subtilis yflN protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
GVYQLPLLPPVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALK
EAPGAPVYAHEREAPYLEGEKPYPPPVRLGLLGLLSPLLPVKPVPVDRTLEDGDTLDLAGGLRVIHTPGH
TPGHISLYLEEDGVLIAGDALVTVGGELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG
>gnl|CDD|293808 cd07722, LACTB2-like_MBL-fold, uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain. Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
RVIRILGQNPGPFTLQGTNTYLVGTGKRRILIDTGEGRPSYIPLLKSVLDSEGNATISDILLTHWHHDHV
GGLPDVLDLLRGPSPRVYKFPRPEEDEDPDEDGGDIHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLE
EENALFTGDCVLGHGTAVFEDLAAYMASLKKLLSLGPGRIYPGHGPVI
>gnl|CDD|293809 cd07723, hydroxyacylglutathione_hydrolase_MBL-fold, hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain. hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDA
PVYGPAEDRIPGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGRFFEG
TAEQMYASLQKLLALPDDTLVYCGH
>gnl|CDD|293810 cd07724, POD-like_MBL-fold, ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain. Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAE
RTGAPIVIGEGAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGR
PDLPGEAEGLARQLYDSLQRKLLLLPDETLVYPGHDY
>gnl|CDD|293811 cd07725, TTHA1429-like_MBL-fold, uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain. Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
LYRLSLPLPGPLGHVNVYLLRDGDETTLIDTGLATEEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIG
LAGKLQEKSGATVYILDVTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKITPN
VSLWAVRVEDPLGAYLESLDKLEKLDVDLAYPGHGGPIKDPKAR
>gnl|CDD|293812 cd07726, ST1585-like_MBL-fold, uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain. This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
GIYLIDLGFLGFPGRIASYLLDGEGRPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGG
AGLLAEALPNAKVYVHPRGARHLIDPSKLWASARAVYGDEADRLGGEILPVPEERVIVLEDGETLDLGGR
TLEVIDTPGHAPHHLSFLDEESDGLFTGDAAGVRYPELDVVGPPSTPPPDFDPEAWLESLDRLLSLKPER
IYLTH
>gnl|CDD|293813 cd07727, YmaE-like_MBL-fold, uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain. Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 proteins.Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
GVYYCGFHSEKSFGAASYLILRPEGNILVDSPRYSPPLAKRIEALGGIRYIFLTHRDDVADHAKWAERFG
AKRIIHEDDVNAVTRPDEVIVLWGGDPWELDPDLTLIPVPGHTRGSVVLLYKEKGVLFTGDHLAWSRRRG
WLSAFRYVCWYSWPEQAESVERLADLDFEWVLPGHGRRVHF
>gnl|CDD|293814 cd07728, YtnP-like_MBL-fold, Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain. Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
IKLTWLDGGVTHLDGGAMFGVVPKPLWSKKYPANEKNQIELRTDPILIQYQGKNYLIDAGIGNGKLTEKQ
KRNFGVTEESSIEESLAELGLTPEDIDYVLMTHLHFDHASGLTKVKGEQLVSVFPNATIYVSEIEWEEMR
NPNIRSKNTYWKENWEPIEDQVKTFSDEIEIVPGITMIHTGGHSDGHSIIEIEQGGETAIHMADLMPTHA
HQNPLWVLAYDDYPMTSIEAKEKWLKEGIKNNYWFTFYH
>gnl|CDD|293815 cd07729, AHL_lactonase_MBL-fold, quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain. Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
KLYALDYGTVTVDKSSLFYYGRGPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAADDPGGLELAFPPGVT
EEQTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLAAGYYEDVLAL
DDDLPGGRVRLVDGDYDLFPGVTLIPTPGHTPGHQSVLVRLPEGTVLLAGDAAYTYENLEEGRPPGINYD
PEAALASLERLKALAEREGARVIPGHDP
>gnl|CDD|293816 cd07730, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are annotated as GumP protein
GSCTLPERLVLRGGPLKRVTFPALAFLIEHPTGGKILFDLGYRKDFEEYTPRVPERLYRTPVPLEVEEDV
AEQLAAGGIDPEDIDAVILSHLHWDHIGGLSDFPNARLIVGPGAKEALRPPGYPSGFLPELLPSDFEGRL
VRWEEDDFLWVPLGPFPRALDLFGDGSLYLVDLPGHAPGHLGLLARTTSGTWVFLAGDACHHRIGLLRPS
PLLPLPDLDDGADREAARETLARLRELDAAPDVRVVLAHD
>gnl|CDD|293817 cd07731, ComA-like_MBL-fold, Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain. This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
RVHFLDVGQGDAILIQTPGKTILIDTGPRDSFGEDVVVPYLKARGIKKLDYLILTHPDADHIGGLDAVLK
NFPVKEVYMPGVTHTTKTYEDLLDAIKEKGIPVTPCKAGDRWQLGGVSFEVLSPPKDDYDDLNNNSCVLR
LTYGGTSFLLTGDAEKEAEEELLASGPDLLADVLKVGHH
>gnl|CDD|293818 cd07732, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Includes functionally uncharacterized Enterococcus faecalis EF2904. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
RITIHRGTNEIGGNCIEVETGGTRILLDFGLPLDPESKYFDEVLDFLELGLLPDIVGLYRDPLLLGGLRS
EEDPSVDAVLLSHAHLDHYGLLNYLRPDIPVYMGEATKRILKALLPFFGEGDPVPRNIRVFESGKSFTIG
DFTVTPYLVDHSAPGAYAFLIEAPGKRIFYTGDFRFHGRKPELTEAFVEKAPKNIDVLLMEG
>gnl|CDD|293819 cd07733, YycJ-like_MBL-fold, uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain. Includes the uncharacterized Bacillus subtilis YycJ protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYN
VPIYATAGTLRAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD
LKQRILSDRGH
>gnl|CDD|293820 cd07734, Int9-11_CPSF2-3-like_MBL-fold, Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain. CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
TPLGGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLF
RGFIFRGPIYATHPTVALGRLLLEDYVKSAERIGQDQSLYTPEDIEEALKHIVPLGYGQSIDLFPALSLT
AYNAGHVLGAAMWEIQIYGEKLVYTGDFSNTEDRLLPAASILPPRPDLLITES
>gnl|CDD|293821 cd07735, class_II_PDE_MBL-fold, class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain. Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
FELVVLGCSGGPDEGNTSSFLLDPAGSDGDILLDAGTGVGALSLEEMFNDILFPSQKAAYELYQRIRHYL
ITHAHLDHIAGLPLLSPNDGGQRGSPKTIYGLPETIDALKKHIFNWVIWPDFTSIPSGKYPYLRLEPIEP
EYPIALTGLSVTAFPVSHGVPVSTAFLIRDGGDSFLFFGDTGPDSVSKSPRLDALWRALAPLIPKKLKAI
IIECSFPNSRPDALLYGHLTPKLLAEELAKLAKEVLKGALKGLNVIITH
>gnl|CDD|293822 cd07736, PhnP-like_MBL-fold, phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain. Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAI
LLTHFHMDHVQGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLN
HSKPTFGYLLESGGKRLAYLTDTLGLPEETLEFLKQQQPDVLVLDC
>gnl|CDD|293823 cd07737, YcbL-like_MBL-fold, Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain. This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHY
GVPIIGPHKEDKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNR
ESKLAIVGDVLFKGSIGRTDFPGGNHAQLIASIKEKLLPLGDDVTFIPGH
>gnl|CDD|293824 cd07738, DdPDE5-like_MBL-fold, Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain. Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
TFLGVSHGFDPKGHTSGFIIWINGRGIMVDPPVNSTSYLRQNGISPRLVDHVILTHCHADHDAGTFQKIL
EEEKITLYTTRTINESFLRKYAALTGLPPDFLEELFDFRPVIIGEKTKINGAEFEFDYSFHSIPTIRFKV
SYGGKSIAYSGDTRYDPDGLKSLYEQGILSESRRAFLLRFPWDADVILH
>gnl|CDD|293825 cd07739, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
LQVDVFTAPEISSFPVTSTLIYGETEAVLVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLE
VLLEAFPDAKVVATPAVVAHIKAQLEPKLAFWGPLLGGNAPARLVVPEPLDGDTLTLEGHPLEIVGVGGG
DTDDTTYLWIPSLKTVVAGDVVYNGVHVWLADATTPELRAAWLAALDKIEALNPETVVPGH
>gnl|CDD|293826 cd07740, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
TFLGSGDAFGSGGRLNTCFHVASEAGRFLIDCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPFFL
LDAQFVAKRTRPLTIAGPPGLRERLRRAMEALFPGSSKVPRRFDLEVIELEPGEPTTLGGVTVTAFPVVH
PSGALPLALRLEAAGRVLAYSGDTEWTDALVPLARGADLFICECYFFEKKVPGH
>gnl|CDD|293827 cd07741, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
IIFLGTGGGRFVVITQLRASGGIWIELNGKNIHIDPGPGALVRMCRPKLDPTKLDAIILSHRHLDHSNDA
NVLIEAMTEGGFKKRGTLLAPEDALNGEPVVLLYYHRRKLEEIEILEEGDEYELGGIKIEATRHKHSDPT
TYGFIFRTSDKKIGYISDTRYFEELIEYYSNCDVLIINVTRPRPRKGVDHLSVEDVEKILKEIKPKLAIL
TH
>gnl|CDD|293828 cd07742, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
HHLNCGTMRPPGGDLRLVCHCLLVETDDGLVLVDTGFGLADVADPKRRLGGPFRRLLRPRLDEDETAVRQ
IEALGFDPSDVRHIVLTHLDLDHAGGLADFPHATVHVHAAELDAATSPRTRYERRRYRPQQLAHGPWWVT
YAAGGERWFGFEAVRPLDGLPPEILLVPLPGHTRGHCGVAVRTGDRWLLHAGDAYFHHGELDPLPPPPPP
LRLFQRLLAVDRSARLANLARLRELARDHGDEVEVFCAH
>gnl|CDD|293829 cd07743, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
TYYIPGPTNIGVYVFGDKEALLIDSGLDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTG
CKVYAPKIEKAFIENPLLEPSYLGGAYPPKELRNKFLMAKPSKVDDIIEEGELELGGVGLEIIPLPGHSF
GQIGILTPDGVLFAGDALFGEEVLEKYGIPFLYDVEEQLETLEKLEELDADYYVPGH
>gnl|CDD|143394 cd07749, NT_Pol-beta-like_1, Nucleotidyltransferase (NT) domain of an uncharacterized subgroup of the Pol beta-like NT superfamily. The Pol beta-like NT superfamily includes DNA polymerase beta and other family X DNA Polymerases, as well as Class I and Class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly(A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. Proteins belonging to this subgroup are uncharacterized. In the majority of the Pol beta-like superfamily NTs, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations essential for catalysis. These divalent metal ions are involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this subgroup
IYLRALRKFYERLKNINVNWALTGSLSFALQGVPVEPHDIDIQTDNEGAYEIERIFHEFVNTEVRFSESE
GIRSHFGELQIDGIKVEIMGDVQKRLEDGWWETPVDLNRYKRFVEVEGMKIPVLSLEYEYQAYLKLGRKK
NQIEKAEMLKKYLQQR
>gnl|CDD|143622 cd07750, PolyPPase_VTC_like, Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins VTC-2, -3 and- 4, and similar proteins. Saccharomyces cerevisiae VTC-1, -2, -3, and -4 comprise the membrane-integral VTC complex. VTC-2, -3, and -4 contain polyP polymerase domains. For S. cerevisiae VTC4 it has been shown that this domain generates polyP from ATP by a phosphotransfer reaction releasing ADP. This activity is metal ion-dependent. The ATP gamma phosphate may be cleaved and then transferred to an acceptor phosphate to form polyP. PolyP is ubiquitous. In prokaryotes, it is a store of phosphate and energy. In eukaryotes, polyPs have roles in bone calcification, and osmoregulation, and in phosphate transport in the symbiosis of mycorrhizal fungi and plants. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel
RYERKYLVPASQLEALLAALKPHLRVDEYAGNRDYTIRSLYFDTPDLDLYREKLNGRRRREKVRIRSYGD
SDGLIFLEVKTKRGRVTYKRRLPLSPEDAERLLAGGYFFLLESQDPLAEEFYFRMRYKQLRPVLLVSYRR
EALVSPDGGVRITFDTNLRYRDEDGDLFSGNLGTPILPPDLVILEVKYDGALPLWLADLLSSHGLEPTSF
SKYC
>gnl|CDD|143623 cd07751, PolyPPase_VTC4_like, Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) protein VTC4, and similar proteins. Saccharomyces cerevisiae VTC-1, -2, -3, and -4 comprise the membrane-integral VTC complex. VTC-2,-3, and -4 contain polyP polymerase domains. S. cerevisiae VTC4 belongs to this subgroup. For VTC4 it has been shown that this domain generates polyP from ATP by a phosphotransfer reaction releasing ADP. This activity is metal ion-dependent. The ATP gamma phosphate may be cleaved and then transferred to an acceptor phosphate to form polyP. PolyP is ubiquitous. In prokaryotes, it is a store of phosphate and energy. In eukaryotes, polyPs have roles in bone calcification, and osmoregulation, and in phosphate transport in the symbiosis of mycorrhizal fungi and plants. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel
PPQTFVRRTTKYWVHPRDVVPVKLAILKHLPVLVFNGSKEEEKEKEDVPPRDDSAITSVYFDNENLDLYH
GRLERDEGAELIRLRWYGGMQDTDTVFVERKTHHESWTGEKSVKERFALKEKYVNSFLKGKYTVDKVFRK
LRKEGKKSEAEIEKLEALATEIQYVILKRKLKPVVRTFYRRTAFQLPDDNRVRISLDTELCMIDERGRDG
RRRTTLNDWPFKQLPDNEIVRFPYAVLEVKLQTQEGEEPPEWVEELLNSHLVEEVYKFSKFLHGCATLFP
DKVDSIPYWL
>gnl|CDD|143624 cd07756, CYTH-like_Pase_CHAD, Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain. This subgroup belongs to the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily. Members of this superfamily hydrolyze triphosphate-containing substrates, require metal cations as cofactors, and have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). A number of proteins in this subgroup also contain a C-terminal CHAD (Conserved Histidine Alpha-helical Domain) domain which may participate in metal chelation or act as a phosphor-acceptor. The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB) and from thiamine triphosphatase. Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. Thiamine triphosphatase is a soluble cytosolic enzyme which converts thiamine triphosphate to thiamine diphosphate. This domain superfamily also contains RNA triphosphatases, membrane-associated polyphosphate polymerases, tripolyphosphatases, nucleoside triphosphatases, nucleoside tetraphosphatases and other proteins with unknown functions. Proteins of this subgroup have not been characterized
EIELKLLLPPEDLEALAAHPLLAALAAGRAQTRRLHNTYFDTPDLALRRAGIALRVRREGGQWVQTLKTA
GSVVGGLHQRPEWEVPLPGPAPDLDLASILPDGELLEALAALAALVPLFTTDFERTVWLLRLGGSEIEVA
LDQGEIRAGDRSEPICEIELELKSGDPAALFALARRLAERLPLRLSNRSKAERGYRL
>gnl|CDD|143625 cd07758, ThTPase, Thiamine Triphosphatase. ThTPase is a soluble cytosolic enzyme which converts thiamine triphosphate (ThTP) to thiamine diphosphate. This catalytic activity depends on a divalent metal cofactor, for example Mg++. ThTPase regulates the intracellular concentration of ThTP, maintaining it at a low concentration in vivo. ThTP acts as a messenger in cell signaling in response to cellular stress, and in addition, can phosphorylate proteins in certain tissues. There is another class of membrane-associated enzymes in animal tissues which also convert ThTP to thiamine diphosphate, however they do not belong to this subgroup. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel
LEVERKFRCGPSAEERLRKLGALLELLGRRTFHDTYYDTPDNTLSLNDVWLRQRNGQWELKIPPGGDPPT
AGANTRYEELTGEAAIAAALRKLLGGALPSAGGLGDELANLGLREFASFVTKRESWKLDGAFRVDLDRTD
FGYSVGEVELLVEEEDNEAEVPAALAKIDELISALMERYLWAFKQGRPPGKLTAYL
>gnl|CDD|143626 cd07761, CYTH-like_CthTTM-like, Clostridium thermocellum (Cth)TTM and similar proteins, a subgroup of the CYTH-like superfamily. CthTTM is a metal dependent tripolyphosphatase, nucleoside triphosphatase, and nucleoside tetraphosphatase. It hydrolyzes the beta-gamma phosphoanhydride linkage of triphosphate-containing substrates including tripolyphosphate, nucleoside triphosphates and nucleoside tetraphosphates. These substrates are hydrolyzed, releasing Pi. Mg++ or Mn++ are required for the enzyme's activity. CthTTM appears to have no adenylate cyclase activity. This subgroup consists chiefly of bacterial sequences. Members of the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily have a unique active site located within an eight-stranded beta barrel
MEIERKFLVNELPAGLESYKKVEIRQGYLSINPEVRIRSKGEKYILTVKSGGGLVREEIEIEIDKKEFEH
LLEKTEGNLIEKTRYLIPLEGGLLAELDVFEGRLTGLVYAEVEFPSEEAARAFSPPAWFGKEVTEDPRYK
NKNLAL
>gnl|CDD|143627 cd07762, CYTH-like_Pase_1, Uncharacterized subgroup 1 of the CYTH-like superfamily. Enzymes belonging to the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily hydrolyze triphosphate-containing substrates, require metal cations as cofactors, and have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB) and from thiamine triphosphatase. Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. Thiamine triphosphatase is a soluble cytosolic enzyme which converts thiamine triphosphate to thiamine diphosphate. This domain superfamily also contains RNA triphosphatases, membrane-associated polyphosphate polymerases, tripolyphosphatases, nucleoside triphosphatases, nucleoside tetraphosphatases and other proteins with unknown functions. Proteins of this subgroup are of bacterial origin and have not been characterized
LEIEFKNLLTKEEYEQLKNAFDLKDFFKQTNYYFDTPDFALKKKHSALRIREKEGKAELTLKVPQEVGLL
ETNQPLTLEEAEKLIKGGTLPEGEILDKLKELGIDPSELKLFGSLTTIRAEIPYEGGLLVLDHSLYLGIT
DYELEYEVDDYEAGKKAFLELLKQYNIPYRPAKNKIARFL
>gnl|CDD|143639 cd07765, KRAB_A-box, KRAB (Kruppel-associated box) domain -A box. The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta, KRAB-A interacting protein, and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation
VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL
>gnl|CDD|341447 cd07766, DHQ_Fe-ADH, Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH). This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H
PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVKGVGEKVADSLKKGLAVAIFDFVGENPTFEEVKNAV
ERARAAEADAVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVGPHYN
PDVVFVDTDITKGLPPRQVASGGVDALAHAVELEKVVEAATLAGMGLFESPGLGLAHAIGHALTAFEGIP
HGEAVAVGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPTHLADLGVSKEDIPKLAEKAL
>gnl|CDD|163686 cd07767, MPN, Mpr1p, Pad1p N-terminal (MPN) domains. MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) domains are found in the N-terminal termini of proteins with a variety of functions; they are components of the proteasome regulatory subunits, the signalosome (CSN), eukaryotic translation initiation factor 3 (eIF3) complexes, and regulators of transcription factors. These domains are isopeptidases that release ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. Catalytically active MPN domains contain a metalloprotease signature known as the JAB1/MPN/Mov34 metalloenzyme (JAMM) motif. For example, Rpn11 (also known as POH1 or PSMD14), a subunit of the 19S proteasome lid is involved in the ATP-dependent degradation of ubiquitinated proteins, contains the conserved JAMM motif involved in zinc ion coordination. Poh1 is a regulator of c-Jun, an important regulator of cell proliferation, differentiation, survival and death. JAB1 is a component of the COP9 signalosome (CSN), a regulatory particle of the ubiquitin (Ub)/26S proteasome system occurring in all eukaryotic cells; it cleaves the ubiquitin-like protein NEDD8 from the cullin subunit of the SCF (Skp1, Cullins, F-box proteins) family of E3 ubiquitin ligases. AMSH (associated molecule with the SH3 domain of STAM, also known as STAMBP), a member of JAMM/MPN+ deubiquitinases (DUBs), specifically cleaves Lys 63-linked polyubiquitin (poly-Ub) chains, thus facilitating the recycling and subsequent trafficking of receptors to the cell surface. Similarly, BRCC36, part of the nuclear complex that includes BRCA1 protein and is targeted to DNA damage foci after irradiation, specifically disassembles K63-linked polyUb. BRCC36 is aberrantly expressed in sporadic breast tumors, indicative of a potential role in the pathogenesis of the disease. Some variants of the JAB1/MPN domains lack key residues in their JAMM motif and are unable to coordinate a metal ion. Comparisons of key catalytic and metal binding residues explain why the MPN-containing proteins Mov34/PSMD7, Rpn8, CSN6, Prp8p, and the translation initiation factor 3 subunits f (p47) and h (p40) do not show catalytic isopeptidase activity. It has been proposed that the MPN domain in these proteins has a primarily structural function
LKMFLDAAKSINGKEVIGLLYGSKTKKVLDVDEVIAVPFDEGDKDDNVWFLMYLDFKKLNAGLRIVGWYH
THPKPSCFLSPNDLATHELFQRYFPEKVMIIVDVKPKDLGNSWKCY
>gnl|CDD|466788 cd07768, ASKHA_NBD_FGGY_RBK-like, nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases. The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
YGIGVDVGTSSARAGVYDLYAGLEMAQEPVPYYQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAY
EVKGCGVDATCSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLLDYLGGKISPEM
GVPKLKYFLDEYSHLRDKHFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRLE
HLTTTKNLPSNVPIGTTSGVALPEMAEKMGLHPGTAVVVSCIDAHASWFAVASPHLETSLFMIAGTSSCH
MYGTTISDRIPGVWGPFDTIIDPDYSVYEAGQSATGKLIEHLFESHPCARKFDEALKKGADIYQVLEQTI
RQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQ
NEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQLADSITEADISN
DRKSETFEPLAYRLGADYILLYKLLCVKYHIH
>gnl|CDD|466789 cd07769, ASKHA_NBD_FGGY_GK, nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins. GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDI
AAIGITNQRETTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWI
LDNVPGARERAERGELLFGTIDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSML
PEVRPSSEVFGYTDPEGLGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNG
LLTTIAWQIGGKVTYALEGSIFIAGAAIQWLRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPY
WDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADI
LGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYRGWKKAVE
>gnl|CDD|466790 cd07770, ASKHA_NBD_FGGY_GntK, nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins. GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDA
IGFSSAMHSLLGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEE
RPELFAKAAKFVSIKEYLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEV
LPGLKPEFAERLGLLAGTPVVLGASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWCY
RLDENRWLVGGAINNGGNVLDWLRDTLLLSGDDYEELDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDAR
GAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLV
PEEEEASALGAALLALEALGLISSLEADELVKIGKVVEPDPENHAIYAELYERFKKLY
>gnl|CDD|466791 cd07771, ASKHA_NBD_FGGY_RhaB-like, nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins. Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases
NYLAVDLGASSGRVILGSLDGGKLELEEIHRFPNRPVEINGHLYWDIDRLFDEIKEGLKKAAEQGGDIDS
IGIDTWGVDFGLLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKE
GPELLERADKLLMLPDLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTV
LGTLKPEVAEELGLKGIPVIAVASHDTASAVAAVPAEDEDAAFISSGTWSLIGVELDEPVITEEAFEAGF
TNEGGADGTIRLLKNITGLWLLQECRREWEEEGKDYSYDELVALAEEAPPFGAFIDPDDPRFLNPGDMPE
AIRAYCRETGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADAT
GLPVIAGPVEATAIGNLLVQLIALGEIKSLEEGRELVRNS
>gnl|CDD|466792 cd07772, ASKHA_NBD_FGGY_NaCK-like, nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins. This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
VIAVFDIGKTNKKLLLFDENGEVLAERSTPNPEIEEDGYPCEDVEAIWEWLLDSLAELAKRHRIDAINFT
THGATFALLDENGELALPVYDYEKPIPDEINEAYYAERGPFEETGSPPLPGGLNLGKQLYWLKREKPELF
ARAKTILPLPQYWAWRLTGKAASEITSLGCHTDLWDFEKNEYSSLVKKEGWDKLFPPLRKAWEVLGPLRP
DLARRTGLPKDIPVGCGIHDSNAALLPYLAAGKEPFTLLSTGTWCIAMNPGNDLPLTELDLARDCLYNLD
VFGRPVKTARFMGGREYERLVERIAKSFPQLPSLADLAKLLARGTFALPSFAPGGGPFPGSGGRGVLSAF
PSAEEAYALAILYLALMTDYALDLLGSGVGRIIVEGGFAKNPVFLRLLAALRPDQPVYLSDDSEGTALGA
ALLA
>gnl|CDD|466793 cd07773, ASKHA_NBD_FGGY_FK, nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins. FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAA
ISVSSQGESGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREH
EPEIFAKAAKWLSVADYIAYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTV
IGTVTPEAAEELGLPAGTPVVVGGHDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGGL
SYGHHVPGGYYYLAGSLPGGALLEWFRDLFGGDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDP
DARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRP
IEVPEVPEATALGAALLAGVGAG
>gnl|CDD|466794 cd07775, ASKHA_NBD_FGGY_AI-2K, nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins. AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
YLLALDAGTGSGRAVIFDLEGNQIAVAQREWRHKEVPDVPGSMDFDTEKNWKLICECIREALKKAGIAPK
SIAAISTTSMREGIVLYDNEGEEIWACANVDARAAEEVSELKELYNTLEEEVYRISGQTFALGAIPRLLW
LKNNRPEIYRKAAKITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVE
SGTVIGKVTKEAAEETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMN
IRVNCHVIPDMWQAEGISFFPGLVMRWFRDAFCAEEKEIAERLGIDAYDLLEEMAKDVPPGSYGIMPIFS
DVMNYKNWRHAAPSFLNLDIDPEKCNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGK
LWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAVESLVKWEREYLPNPENHEVYQDLYE
KW
>gnl|CDD|466795 cd07776, ASKHA_NBD_FGGY_SpXK-like, nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins. XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDSDLPEYGTKGGVHRDGDGGEVTSPVLMWVEALDLLLEK
LKAAGFDFSRVKAISGSGQQHGSVYWSKGAESALANLDPSKSLAEQLEGAFSVPDSPIWMDSSTTKQCRE
LEKAVGGPEALAKLTGSRAYERFTGPQIAKIAQTDPEAYENTERISLVSSFLASLLLGRYAPIDESDGSG
MNLMDIRSRKWSPELLDAATAPDLKEKLGELVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAG
LGLEPGDVAVSLGTSDTVFLVLDEPKPGPEGHVFANPVDPGSYMAMLCYKNGSLARERVRDRYAGGSWEK
FNELLESTPPGNNGNLGLYFDEPEITPPVPGGGRRFFGDDGVDAFFDPAVEVRAVVESQFLSMRLHAERL
GSDIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFS
AEEPKLVAEPDPEAAEVYDKLLER
>gnl|CDD|466796 cd07777, ASKHA_NBD_FGGY_SHK, nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins. SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
NVLGIDIGTTSIKAALLDLESGRILESVSRPTPAPISSDDPGRSEQDPEKILEAVRNLIDELPREYLSDV
TGIGITGQMHGIVLWDEDGNPVSPLITWQDQRCSEEFLGGLSTYGEELLPKSGMRLKPGYGLATLFWLLR
NGPLPSKADRAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSG
EIVGTLSSALPKGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKFELSGSVEIRPFFDGR
YLLVAASLPGGRALAVLVDFLREWLRELGGSLSDDEIWEKLDELAESEESSDLSVDPTFFGERHDPEGRG
SITNIGESNFTLGNLFRALCRGIAENLHEMLPRLDLDLSGIERIVGSGGALRKNPVLRRIIEKRFGLPVV
LSEGSEEAAVGAALLA
>gnl|CDD|466797 cd07778, ASKHA_NBD_FGGY_MPA43-like, nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins. This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
VGIGIDVGSTSVRIGIFDYHGTLLATSERPISYKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDYIV
SGIGVSATCSMVVMQRDSDTSYLVPYNVIHEKSNPDQDIIFWMDHRASEETQWLNNILPDDILDYLGGGF
IPEMAIPKLKYLIDLIKEDTFKKLEVFDLHDWISYMLATNLGHSNIVPVNAPPSIGIGIDGSLKGWSKDF
YSKLKISTKVCNVGNTFKEAPPLPYAGIPIGKVNVILASYLGIDKSTVVGHGCIDCYAGWFSTFAAAKTL
DTTLFMVAGTSTCFLYATSSSQVGPIPGIWGPFDQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKS
DANFFETVEEKIDKYERLLGQSIHYLTRHMFFYGDYLGNRTPYNDPNMSGSFIGESTDSSLTDLVLKYIL
ILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNARLLQLLSTVLSKIHIIVPLSDSKYAVVKGAALLG
KAAFLHNQSIEERLISLKNEDQISICASASIVKLVSDETKLAIILRAKYQIMND
>gnl|CDD|466798 cd07779, ASKHA_NBD_FGGY_YgcE-like, nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins. This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDI
AAIGLTSQRSTFVPVDEDGRPLRPAISWQDKRTAKFLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRD
WSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQQCAALGAGVLEPGTASLS
LGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVLEGSINTGGSAVRWFRDEFGQDEVAEKELGVSPYEL
LNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAMEK
AGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVT
DTFEPDPENVAIY
>gnl|CDD|466799 cd07781, ASKHA_NBD_FGGY_L-RBK, nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
YVIGIDFGTQSVRAGLVDLADGEELASAVVPYPTGYIPPRPGWAEQNPADYWEALEEAVRGALAEAGVDP
EDVVGIGVDTTSSTVVPVDEDGNPLAPAILWMDHRAQEEAAEINETAHPALEYYLAYYGGVYSSEWMWPK
ALWLKRNAPEVYDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPGLLKLRE
KLPGEVVPVGEPAGTLTAEAAERLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPK
PVDIPGICGPVPDAVVPGLYGLEAGQSAVGDIFAWFVRLFVPPAEERGDSIYALLSEEAAKLPPGESGLV
ALDWFNGNRTPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAE
KNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPENHAVYEE
LYALYKELYDALGP
>gnl|CDD|466800 cd07782, ASKHA_NBD_FGGY_D-RBK, nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins. The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway
YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQV
KGIGFDATCSLVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPP
KLLWLKENLPETWAKAGHFFDLPDFLTWKATGSLTRSLCSLVCKWTYLAHEGSEGGWDDDFFKEIGLEDL
VEDNFAKIGSVVLPPGEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGTLGADVGGLPCEADPLTR
RLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNEGGQSATGALLDHIIETHPAYPELKEEAKA
AGKSIYEYLNERLEQLAEEKGLPLAYLTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALLYL
ATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAV
ASGDFPSLWDAMAAMSGPGKVVEPNEELKKYHDRKYEVFLKMYEDQREYR
>gnl|CDD|466801 cd07783, ASKHA_NBD_FGGY_SePSK_AtXK1-like, nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins. This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRRVVA
IAVDGTSGTLVLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEP
EVLAKTAKFLHQADWLAGRLTGDRGVTDYNNALKLGYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIG
TLTAEAAEELGLPAGTPVVAGTTDSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSHRH
GDGYWLVGGASNTGGAVLRWFFSDDELAELSAQADPPGPSGLIYYPLPLRGERFPFWDPDARGFLLPRPH
DRAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAALG
AALLAAAGL
>gnl|CDD|198361 cd07786, FGGY_EcGK_like, Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases. This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDI
AAIGITNQRETTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWI
LDNVPGARERAERGELAFGTIDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASML
PEVKPSSEVFGYTDPDLLGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNG
LLTTIAWQLGGKVTYALEGSIFIAGAAVQWLRDGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPY
WDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADI
LGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYAGWKKAVK
>gnl|CDD|466802 cd07792, ASKHA_NBD_FGGY_GK1-3-like, nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins. This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
PLVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGIS
PSDIKAIGITNQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGGKDHFRKKTGLPISTYFSA
VKLRWLLDNVPEVKKAVDDGRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCE
FFGIPMSILPEIRSSSEVYGKIASGPLAGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGE
EPVFSKHGLLTTVAYKLGPDAPPVYALEGSIAIAGAAVQWLRDNLGIISSASEVETLAASVPDTGGVYFV
PAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKN
NLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQISEEERERRYK
RWKKAVERS
>gnl|CDD|466803 cd07793, ASKHA_NBD_FGGY_GK5-like, nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins. The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDI
AAIGISTQRNTFLTWDKKTGKPLHNFITWQDLRAAELCESWNRSLLLKALRGGSKFLHFLTRNKRFLAAS
VLKFSTAHVSIRLLWILQNNPELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLE
WSPILLSLFGIPSSILPEVKDTSGDFGSTDPSIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGT
FIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASDTGTVIDWAKSIGLFDDPSETEDIAESVEDTN
GVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDG
GVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEKIFEPKMDNEKRE
ELYKNWKKAVK
>gnl|CDD|466804 cd07798, ASKHA_NBD_FGGY_YoaC-like, nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins. The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDAKEFDPEELWEKICEAIREALKKAGISPE
DISAVSSTSQREGIVFLDKDGRELYAGPNIDARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAARLLWFK
ENRPEIFERIATVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSG
TVLGTVSEEAARELGLPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLW
TGCHLVPGKWVLESNAGVTGLNYQWLKELLYGDPEDSYEVLEEEASEIPPGANGVLAFLGPQIFDARLSG
LKNGGFLFPTPLSASELTRGDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILAD
VLGKPVLVPEGREASALGAAICAAVGAG
>gnl|CDD|466805 cd07802, ASKHA_NBD_FGGY_EcLyxK-like, nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins. The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDI
AGVGVTGHGNGLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLK
ENEPERYDRIRTVLFCKDWIRYRLTGEISTDYTDAGSSLLDLDTGEYDDELLDLLGIEELKDKLPPLVPS
TEIAGRVTAEAAALTGLPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGS
NSLHADPGLYLIVEASPTSASNLDWFLDTLLGEEKEAGGSDYDELDELIAAVPPGSSGVIFLPYLYGSGA
NPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVARKPETIRLTGGGARSPVWAQIFADVLGL
PVEVPDGEELGALGAAICAAVAAG
>gnl|CDD|466806 cd07804, ASKHA_NBD_FGGY_RrXK-like, nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins. The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEI
AAIGVSGLVPALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIK
RNEPEVFKKTRKFLGAYDYIVYKLTGEYVIDYSSAGNEGGLFDIRKRTWDEELLEALGIDPDLLPELVPS
TEIVGEVTKEAAEETGLAEGTPVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDPRLWL
DYHDIPGTYVLNGGMATSGSLLRWFRDEFAGEEVEAEKSGGDSAYDLLDEEAEKIPPGSDGLIVLPYFMG
ERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQI
VADVTGVPQEYVKDTVGASLGDAFLAGVGVG
>gnl|CDD|466807 cd07805, ASKHA_NBD_FGGY_CvXK-like, nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins. The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDI
AAIAFSGQMQGVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPPSGKDPLAKILWL
KENEPEIYAKTHKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPS
TEVVGELTPEAAAELGLPAGTPVVGGGGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGI
FTLASADPGRYLLAAEQETAGGALEWARDNLGGDEDLGADDYELLDELAAEAPPGSNGLLFLPWLNGERS
PVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILAD
VLGRPVEVPENPQEAGALGAALLAAVGLGLLKSFDEAKALVKVEKVFEPDPENRARYDRLYEVFK
>gnl|CDD|466808 cd07808, ASKHA_NBD_FGGY_EcXK-like, nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins. The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDI
AAIGLTGQMHGLVLLDKNGRPLRPAILWNDQRSAAECEELEARLGDEILIITGNPPLPGFTLPKLLWLKE
NEPEIFARIRKILLPKDYLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTE
IVGTLTPEAAEELGLPEGTPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHT
FPHAVPGKWYAMGVTLSAGLSLRWLRDLFGPDRESFDELDAEAAKVPPGSEGLLFLPYLSGERTPYWDPN
ARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPV
VVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDELYARYRELY
>gnl|CDD|466809 cd07809, ASKHA_NBD_FGGY_BaXK-like, nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins. The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain
LVLGIDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRD
VAAIGISGQMHGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKKCLLVGLNIPARFTASKLLWLK
ENEPEHYARIAKILLPHDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRDLRDLLPEVL
PAGEVAGRLTPEGAEELGLPAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHG
RVATFCDSTGGMLPLINTTNCLTAWTELFRELLGVSYEELDELAAQAPPGAGGLLLLPFLNGERTPNLPH
GRASLVGLTLSNFTRANLARAALEGATFGLRYGLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVP
VVVPETGEGGALGAALQAAWGAG
>gnl|CDD|176854 cd07812, SRPBCC, START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins
VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARFVGGRKGGRRLTLTSEVTEVDPP
RPGRFRVTGGGGGVDGTGEWRLEPEGDGGTRVTYTVEYDPPGPLLKVFALLLAGALKRELAALLRALKAR
L
>gnl|CDD|176855 cd07813, COQ10p_like, Coenzyme Q-binding protein COQ10p and similar proteins. Coenzyme Q-binding protein COQ10p and similar proteins. COQ10p is a hydrophobic protein located in the inner membrane of mitochondria that binds coenzyme Q (CoQ), also called ubiquinone, which is an essential electron carrier of the respiratory chain. Deletion of the gene encoding COQ10p (COQ10 or YOL008W) in Saccharomyces cerevisiae results in respiratory defect because of the inability to oxidize NADH and succinate. COQ10p may function in the delivery of CoQ (Q6 in budding yeast) to its proper location for electron transport. The human homolog, called Q-binding protein COQ10 homolog A (COQ10A), is able to fully complement for the absence of COQ10p in fission yeast. Human COQ10A also has a splice variant COQ10B. COQ10p belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands
YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPES
IEAELVDGPFKHLEGEWRFKPLGENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQL
>gnl|CDD|176856 cd07814, SRPBCC_CalC_Aha1-like, Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human Aha1, and related proteins. This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Micromonospora echinospora CalC, human Aha1, and related proteins. Proteins in this group belong to the SRPBCC domain superfamily of proteins, which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM), by a self sacrificing mechanism which results in inactivation of both CalC and the highly reactive diradical enediyne species. MeCalC can also inactivate two other enediynes, shishijimicin and namenamicin. A crucial Gly of the MeCalC CLM resistance mechanism is not conserved in this subgroup. This family also includes the C-terminal, Bet v1-like domain of Aha1, one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity, and may regulate the dwell time of Hsp90 with client proteins. Aha1 can act as either a positive or negative regulator of chaperone-dependent activation, depending on the client protein, but the mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases
TITIEREFDAPPELVWRALTDPELLAQWFGPTTTAEMDLRVGGRWFFFMTGPDGEEGWVSGEVLEVEPPR
RLVFTWAFSDETPGPETTVTVTLEETGGGTRLTLTHSGFPEEDAEQEAREGMEEGWTGTLDRLKALLEK
>gnl|CDD|176857 cd07815, SRPBCC_PITP, Lipid-binding SRPBCC domain of Class I and Class II Phosphatidylinositol Transfer Proteins. This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of the phosphatidylinositol transfer protein (PITP) family of lipid transfer proteins. This family of proteins includes Class 1 PITPs (PITPNA/PITPalpha and PITPNB/PITPbeta, Drosophila vibrator and related proteins), Class IIA PITPs (PITPNM1/PITPalphaI/Nir2, PITPNM2/PITPalphaII/Nir3, Drosophila RdgB, and related proteins), and Class IIB PITPs (PITPNC1/RdgBbeta and related proteins). The PITP family belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Class III PITPs, exemplified by the Sec14p family, are found in yeast and plants but are unrelated in sequence and structure to Class I and II PITPs and belong to a different superfamily
LIKEFRIVLPLTVEEYQIGQLYMVAKASKEETGSGEGVEVLKNEPYEDENGGKGQYTHKIYHLGSKLPSW
LRALAPKSALTIEEKSWNAYPYCKTVYSCPFFEKFSISIESMHKPDLGTQENAHNLSAEQLAQRKVVVID
IANDSVASKDYKPEEDPKLFKSKKTGRGPLRKGWRKSTKPIMCAYKLVTVDFPYWGLQNKVENFIQKVER
DVFLNYHRQAFCWIDEWFDLTMEDIREFEEETKELLDAKRK
>gnl|CDD|176858 cd07816, Bet_v1-like, Ligand-binding bet_v_1 domain of major pollen allergen of white birch (Betula verrucosa), Bet v 1, and related proteins. This family includes the ligand binding domain of Bet v 1 (the major pollen allergen of white birch, Betula verrucosa) and related proteins. In addition to birch Bet v 1, this family includes other plant intracellular pathogenesis-related class 10 (PR-10) proteins, norcoclaurine synthases (NCSs), cytokinin binding proteins (CSBPs), major latex proteins (MLPs), and ripening-related proteins. It belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Members of this family binds a diverse range of ligands. Bet v 1 can bind brassinosteroids, cytokinins, flavonoids and fatty acids. Hyp-1, a PR-10 from Hypericum perforatum/St. John's wort, catalyzes the condensation of two molecules of emodin to the bioactive naphthodianthrone hypericin. NCSs catalyze the condensation of dopamine and 4-hydroxyphenylacetaldehyde to (S)-norcoclaurine, the first committed step in the biosynthesis of benzylisoquinoline alkaloids such as morphine. The role of MLPs is unclear; however, they are associated with fruit and flower development and in pathogen defense responses. A number of PR-10 proteins in this subgroup, including Bet v 1, have in vitro RNase activity, the biological significance of which is unclear. Bet v 1 family proteins have a conserved glycine-rich P (phosphate-binding)-loop proximal to the entrance of the ligand-binding pocket. However, its conformation differs from that of the canonical P-loop structure found in nucleotide-binding proteins. Several PR-10 members including Bet v1 are allergenic. Cross-reactivity of Bet v 1 with homologs from plant foods results in birch-fruit syndrome
GTLEHEVELKVPAEKLWKAFVLDSHLLPPKLPPVIKSVELLEGDGGPGSIKLITFGPGGKVKYVKERIDA
VDEENKTYKYTVIEGDVLKDGYKSYKVEIKFVPKGDGGCVVKWTIEYEKKGDAEPPEEEIKAGKEKALKM
FKAVEAYL
>gnl|CDD|176859 cd07817, SRPBCC_8, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins
TVEKSITVNVPVEEVYDFWRDFENLPRFMSHVESVEQLDDTRSHWKAKGPAGLSVEWDAEITEQVPNERI
AWRSVEGADPNAGSVRFRPAPGRGTRVTLTIEYEPPGGAEGAAVAGLLGGEPERQLREDLRRFKQLVET
>gnl|CDD|176860 cd07818, SRPBCC_1, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins
DYRVERSIVINAPPEEVFPYVNDLKNWPEWSPWEKLDPDMKRTYSGPDSGVGASYSWEGNDKVGEGEMEI
TESVPNERIEYELRFIKPFEATNDVEFTLEPVGGGTKVTWGMSGELPFPLKLMYLFLDMDKMIGKDFEKG
LANLKAVLEK
>gnl|CDD|176861 cd07819, SRPBCC_2, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins
AIKVSREFEIEAPPAAVMDVLADVEAYPEWSPKVKSVEVLLRDNDGRPEMVRIGVGAYGIKDTYALEYTW
DGAGSVSWTLVEGEGNRSQEGSYTLTPKGDGTRVTFDLTVELTVPLPGFLKRKAEPLVLDEALKGLKKRV
>gnl|CDD|176862 cd07820, SRPBCC_3, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins
LERSTVIPAPIEEVFDFHSRPDNLERLTPPWLEFAVLGRTPGLIYGGARVTYRLRHFGIPQRWTTEITEV
EPPRRFVDEQVSGPFRSWRHTHRFEAIGGGTLMTDRVEYRLPLGPLGRLAAPLVVRRYLERFFAYRH
>gnl|CDD|176863 cd07821, PYR_PYL_RCAR_like, Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid receptors (RCARs), and related proteins. The PYR/PYL/RCAR-like family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. PYR/PYL/RCAR plant proteins are receptors involved in signal transduction. They bind abscisic acid (ABA) and mediate its signaling. ABA is a vital plant hormone, which regulates plant growth, development, and response to environmental stresses. Upon binding ABA, these plant proteins interact with a type 2C protein phosphatase (PP2C), such as ABI1 and ABI2, and inhibit their activity. When ABA is bound, a loop (designated the gate/CL2 loop) closes over the ligand binding pocket, resulting in the weakening of the inactive PYL dimer and facilitating type 2C protein phosphatase binding. In the ABA:PYL1:ABI1 complex, the gate blocks substrate access to the phosphatase active site. A conserved Trp from PP2C inserts into PYL to lock the receptor in a closed formation. This group also contains Methylobacterium extorquens AM1 MxaD. The mxaD gene is located within the mxaFJGIR(S)ACKLDEHB cluster which encodes proteins involved in methanol oxidation. MxaD may participate in the periplasmic electron transport chain for oxidation of methanol. Mutants lacking MxaD exhibit a reduced growth on methanol, and a lower rate of respiration with methanol
AKVTVSVTIDAPADKVWALLSDFGGLHKWHPAVASCELEGGGPGVGAVRTVTLKDGGTVRERLLALDDAE
RRYSYRIVEGPLPVKNYVATIRVTPEGDGGTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALKAALE
>gnl|CDD|176864 cd07822, SRPBCC_4, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins
TISTEIEINAPPEKVWEVLTDFPSYPEWNPFVRSATGLSLALGARLRFVVKLPGGPPRSFKPRVTEVEPP
RRLAWRGGLPFPGLLDGEHSFELEPLGDGGTRFVHRETFSGLLAPLVLLGLGRDLRAGFEAMNEALKARA
E
>gnl|CDD|176865 cd07823, SRPBCC_5, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins
LENEFTVPAPPDRVWALLLDIERVAPCLPGASLTEVEGDDEYKGTVKVKLGPISASFKGTARLLEDDEAA
RRAVLEATGKDARGQGTAEATVTLRLSPAGGGTRVTVDTDLALTGKLAQFGRGGIGDVAGRLLAQFAANL
EARLAA
>gnl|CDD|176866 cd07824, SRPBCC_6, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins
YRFHTVWRIPAPPEAVWDVLVDAESWPDWWPGVERVVELEPGDEAGIGARRRYTWRGLLPYRLRFELRVT
RIEPLSLLEVRASGDLEGVGRWTLAPDGSGTVVRYDWEVRTTKPWMNLLAPLARPVFRWNHRRVMRAGEK
GLARRL
>gnl|CDD|176867 cd07825, SRPBCC_7, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins
QVSVSRTVDAPAEAVFAVLADPRRHPEIDGSGTVREAIDGPRILAVGDVFRMAMRLDGGPYRITNHVVAF
EENRLIAWRPGPAGQEPGGHRWRWELEPIGPGRTRVTETYDWSAVTDLKELLGFPAFPEVQLEASLDRLA
TLAE
>gnl|CDD|176868 cd07826, SRPBCC_CalC_Aha1-like_9, Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins. SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands
EIVITREFDAPRELVFRAHTDPELVKRWWGPRGLTMTVCECDIRVGGSYRYVHRAPDGEEMGFHGVYHEV
TPPERIVQTEEFEGLPDGVALETVTFTELGGRTRLTATSRYPSKEARDGVLASGMEEGMEESYDRLDELL
AS
>gnl|CDD|143640 cd07827, RHD-n, N-terminal sub-domain of the Rel homology domain (RHD). Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal sub-domain, which may be distantly related to the DNA-binding domain found in P53. The C-terminal sub-domain has an immunoglobulin-like fold and serves as a dimerization module that also binds DNA (see cd00102). The RHD is found in NF-kappa B, nuclear factor of activated T-cells (NFAT), the tonicity-responsive enhancer binding protein (TonEBP), and the arthropod proteins Dorsal and Relish (Rel)
PYLEITEQPKQRGHRFRYECEGRSAGSIPGENSTADRKTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHPH
QLVGKTDCRDGVCEVRLGPKNNMTASFNNLGIQCVRKKDVEEALGQRIQLGIDPFMVHKGPEGNASDIDL
NRVRLCFQAFIEDSDGGFTLPLPPVLSNPIYDKK
>gnl|CDD|381185 cd07828, lipocalin_heme-bd-THAP4-like, heme-binding beta-barrel domain of human THAP4, Arabidopsis thaliana nitrobindin, and similar proteins. Proteins in this subfamily use a beta-barrel domain to bind ferric heme. This group also includes the beta-barrel domain of human THAP domain containing 4 (THAP4). The THAP domain is found in proteins involved in transcriptional regulation, cell-cycle control, apoptosis and chromatin modification. Arabidopsis thaliana nitrobindin may reversibly bind nitric oxide (NO) and be involved in NO transport. It also includes the beta-barrel domain of Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
LEPLSWLLGTWRGSGKGGYPTIKDFSYGEEITFSHDGQPFLNYTARTWTLDTGKPMHRESGFLRIKPDGN
KVELLIAHNTGLVEIEEGEVTGNTLELTTDAVARTSFAPEVTAIKRLFGLVDGNTLEYTVDMATAGKPLT
PHLSARLKKV
>gnl|CDD|270823 cd07829, STKc_CDK_like, Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEEGIPSTALREISLLKELKHPNIVKLLDVIHTE
NKLYLVFEYCDQDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLA
DFGLARAFGIPLRTYTHEVVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFK
IFQILGTPTEESWPGVTKLPDYKPTFPKWPKNDLEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHP
YF
>gnl|CDD|270824 cd07830, STKc_MAK_like, Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYSWEECMNLREVKSLRKLNEHPNIVKLKEVFREN
DELYFVFEYMEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKI
ADFGLAREIRSRPPYTDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYK
ICSVLGTPTKQDWPEGYKLASKLGFRFPQFAPTSLHQLIPNASPEAIDLIKDMLRWDPKKRPTASQALQH
PYF
>gnl|CDD|270825 cd07831, STKc_MOK, Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNNLREIQALRRLSPHPNILRLIEVLFDR
KTGRLALVFELMDMNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDILKL
ADFGSCRGIYSKPPYTEYISTRWYRAPECLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAK
IHDVLGTPDAEVLKKFRKSRHMNYNFPSKKGTGLRKLLPNASAEGLDLLKKLLAYDPDERITAKQALRHP
YF
>gnl|CDD|270826 cd07832, STKc_CCRK, Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIKALQACQGHPYVVKLRDVFP
HGTGFVLVFEYMLSSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLK
IADFGLARLFSEEDPRLYSHQVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQ
LAIVLRTLGTPNEKTWPELTSLPDYNKITFPESKGIRLEEIFPDCSPEAIDLLKGLLVYNPKKRLSAEEA
LRHPYFF
>gnl|CDD|270827 cd07833, STKc_CDKL, Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFR
RKGRLYLVFEYVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLK
LCDFGFARALTARPASPLTDYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQ
LYLIQKCLGPLPPSHQELFSSNPRFAGVAFPEPSQPESLERRYPGKVSSPALDFLKACLRMDPKERLTCD
ELLQHPYF
>gnl|CDD|270828 cd07834, STKc_MAPK, Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNVFDDLIDAKRILREIKILRHLKHENIIGLLDILRP
PSPEEFNDVYIVTELMETDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNC
DLKICDFGLARGVDPDEDKGFLTEYVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRD
YIDQLNLIVEVLGTPSEEDLKFISSEKARNYLKSLPKKPKKPLSEVFPGASPEAIDLLEKMLVFNPKKRI
TADEALAHPYLAQLHDPEDEPVAKPPFDFPFFDDEELTIEELKELIYEE
>gnl|CDD|270829 cd07835, STKc_CDK1_CdkB_like, Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGVPSTAIREISLLKELNHPNIVRLLDVVHSE
NKLYLVFEFLDLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKL
ADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLF
RIFRTLGTPDEDVWPGVTSLPDYKPTFPKWARQDLSKVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQH
PYF
>gnl|CDD|143341 cd07836, STKc_Pho85, Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NFKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTE
NKLMLVFEYMDKDLKKYMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELK
LADFGLARAFGIPVNTFSNEVVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQL
LKIFRIMGTPTESTWPGISQLPEYKPTFPRYPPQDLQQLFPHADPLGIDLLHRLLQLNPELRISAHDALQ
HPWF
>gnl|CDD|270830 cd07837, STKc_CdkB_plant, Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGVPSTALREVSLLQMLSQSIYIVRLLDVE
HVEENGKPLLYLVFEYLDTDLKKFIDSYGRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNL
LVDKQKGLLKIADLGLGRAFTIPIKSYTHEIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPL
FPGDSELQQLLHIFRLLGTPNEEVWPGVSKLRDWHEYPQWKPQDLSRAVPDLEPEGVDLLTKMLAYDPAK
RISAKAALQHPYFD
>gnl|CDD|270831 cd07838, STKc_CDK4_6_like, Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEGIPLSTIREIALLKQLESFEHPNVVRLLDVC
HGPRTDRELKLTLVFEHVDQDLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILV
TSDGQVKLADFGLARIYSFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSS
EADQLGKIFDVIGLPSEEEWPRNSALPRSSFPSYTPRPFKSFVPEIDEEGLDLLKKMLTFNPHKRISAFE
ALQHPYF
>gnl|CDD|143344 cd07839, STKc_CDK5, Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHS
DKKLTLVFEYCDQDLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKL
ADFGLARAFGIPVRCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQL
KRIFRLLGTPTEESWPGVSKLPDYKPYPMYPATTSLVNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQ
HPYF
>gnl|CDD|270832 cd07840, STKc_CDK9_like, Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPITAIREIKLLQKLDHPNVVRLKEIVTSK
GSAKYKGSIYMVFEYMDHDLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINND
GVLKLADFGLARPYTKENNADYTNRVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKT
ELEQLEKIFELCGSPTEENWPGVSDLPWFENLKPKKPYKRRLREVFKNVIDPSALDLLDKLLTLDPKKRI
SADQALQHEYF
>gnl|CDD|270833 cd07841, STKc_CDK7, Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKDGINFTALREIKLLQELKHPNIIGLLDV
FGHKSNINLVFEFMETDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGV
LKLADFGLARSFGSPNRKMTHQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDID
QLGKIFEALGTPTEENWPGVTSLPDYVEFKPFPPTPLKQIFPAASDDALDLLQRLLTLNPNKRITARQAL
EHPYFSNDPAPTPPSQLP
>gnl|CDD|270834 cd07842, STKc_CDK8_like, Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KYEIEGCIGRGTYGRVYKAKRKNGKDGKEYAIKKFKGDKEQYTGISQSACREIALLRELKHENVVSLVEV
FLEHADKSVYLLFDYAEHDLWQIIKFHRQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANIL
VMGEGPERGVVKIGDLGLARLFNAPLKPLADLDPVVVTIWYRAPELLLGARHYTKAIDIWAIGCIFAELL
TLEPIFKGREAKIKKSNPFQRDQLERIFEVLGTPTEKDWPDIKKMPEYDTLKSDTKASTYPNSLLAKWMH
KHKKPDSQGFDLLRKLLEYDPTKRITAEEALEHPYF
>gnl|CDD|173741 cd07843, STKc_CDC2L1, Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
CRSVDEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEKEKEGFPITSLREINILLKLQHPNIVTVK
EVVVGSNLDKIYMVMEYVEHDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLN
NRGILKICDFGLAREYGSPLKPYTQLVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGK
SEIDQLNKIFKLLGTPTEKIWPGFSELPGAKKKTFTKYPYNQLRKKFPALSLSDNGFDLLNRLLTYDPAK
RISAEDALKHPYF
>gnl|CDD|270835 cd07844, STKc_PCTAIRE_like, Catalytic domain of PCTAIRE-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
TYKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEHEEGAPFTAIREASLLKDLKHANIVTLHDIIHTK
KTLTLVFEYLDTDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLA
DFGLARAKSVPSKTYSNEVVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDVEDQLH
KIFRVLGTPTEETWPGVSSNPEFKPYSFPFYPPRPLINHAPRLDRIPHGEELALKFLQYEPKKRISAAEA
MKHPYF
>gnl|CDD|173742 cd07845, STKc_CDK10, Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GRCRSVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDNERDGIPISSLREITLLLNLRHPNIVE
LKEVVVGKHLDSIFLVMEYCEQDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLL
LTDKGCLKIADFGLARTYGLPAKPMTPKVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLP
GKSEIEQLDLIIQLLGTPNESIWPGFSDLPLVGKFTLPKQPYNNLKHKFPWLSEAGLRLLNFLLMYDPKK
RATAEEALESSYFKEKPLPCEPEMMPTFP
>gnl|CDD|270836 cd07846, STKc_CDKL2_3, Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFR
RKKRWYLVFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVK
LCDFGFARTLAAPGEVYTDYVATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQL
YHIIKCLGNLIPRHQELFQKNPLFAGVRLPEVKEVEPLERRYPKLSGVVIDLAKKCLHIDPDKRPSCSEL
LHHEFF
>gnl|CDD|270837 cd07847, STKc_CDKL1_4, Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFR
RKRKLHLVFEYCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIK
LCDFGFARILTGPGDDYTDYVATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQL
YLIRKTLGDLIPRHQQIFSTNQFFKGLSIPEPETREPLESKFPNISSPALSFLKGCLQMDPTERLSCEEL
LEHPYF
>gnl|CDD|270838 cd07848, STKc_CDKL5, Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFR
RRGKLYLVFEYVEKNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLK
LCDFGFARNLSEGSNANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQL
FTIQKVLGPLPAEQMKLFYSNPRFHGLRFPAVNHPQSLERRYLGILSGVLLDLMKNLLKLNPTDRYLTEQ
CLNHPAF
>gnl|CDD|270839 cd07849, STKc_ERK1_2_like, Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FDVGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTYCLRTLREIKILLRFKHENIIGILD
IQRPPTFESFKDVYIVQELMETDLYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLN
TNCDLKICDFGLARIADPEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLF
PGKDYLHQLNLILGILGTPSQEDLNCIISLKARNYIKSLPFKPKVPWNKLFPNADPKALDLLDKMLTFNP
HKRITVEEALAHPYLEQYHDPSDEPVAEEPFPFDMELFDDLPKEKLKELIFEEIMR
>gnl|CDD|270840 cd07850, STKc_JNK, Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTP
QKSLEEFQDVYLVMELMDANLCQVIQMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCT
LKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQW
NKIIEQLGTPSDEFMSRLQPTVRNYVENRPKYAGYSFEELFPDVLFPPDSEEHNKLKASQARDLLSKMLV
IDPEKRISVDDALQHPYINVWYDPSEVEAPPPAPYDHSIDEREHTVEEWKELIYKEV
>gnl|CDD|143356 cd07851, STKc_p38, Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FYRQELNKTVWEVPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKH
MKHENVIGLLDVFTPASSLEDFQDVYLVTHLMGADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGII
HRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELL
TGKTLFPGSDHIDQLKRIMNLVGTPDEELLKKISSESARNYIQSLPQMPKKDFKEVFSGANPLAIDLLEK
MLVLDPDKRITAAEALAHPYLAEYHDPEDEPVAPPYDQSFESRDLTVDEWKELVYDEIMNFKP
>gnl|CDD|270841 cd07852, STKc_MAPK15-like, Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IDKHILRRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKIFDAFRNATDAQRTFREIMFLQELNDHPNII
KLLNVIRAENDKDIYLVFEYMETDLHAVIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILL
NSDCRVKLADFGLARSLSQLEEDDENPVLTDYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGK
PLFPGTSTLNQLEKIIEVIGRPSAEDIESIQSPFAATMLESLPPSRPKSLDELFPKASPDALDLLKKLLV
FNPNKRLTAEEALRHPYVAQFHNPADEPSLPGPIVIPLDDNKKLTVDEYRNRLYEEI
>gnl|CDD|173748 cd07853, STKc_NLK, Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DVEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQP
PHIDPFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNC
VLKICDFGLARVEEPDESKHMTQEVVTQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSP
IQQLDLITDLLGTPSLEAMRSACEGARAHILRGPHKPPSLPVLYTLSSQATHEAVHLLCRMLVFDPDKRI
SAADALAHPYLDEGRLRYHTCMCKCCYTTSGGRVYTSDFEPSANPPFDDEYEKNLTSVRQVKEELHQFIL
EQQQGNRVPLCINPQSAAFKSF
>gnl|CDD|143359 cd07854, STKc_MAPK4_6, Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FDLGSRYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSVKHALREIKIIRRLDHDNIVKVYEV
LGPSGSDLTEDVGSLTELNSVYIVQEYMETDLANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDL
KPANVFINTEDLVLKIGDFGLARIVDPHYSHKGYLSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFA
EMLTGKPLFAGAHELEQMQLILESVPVVREEDRNELLNVIPSFVRNDGGEPRRPLRDLLPGVNPEALDFL
EQILTFNPMDRLTAEEALMHPYMSCYSCPFDEPVSLHPFHIEDELDDILLMTEIHSIIYNWD
>gnl|CDD|270842 cd07855, STKc_ERK5, Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FDVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIR
DILRPKVPYADFKDVYVVLDLMESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNL
LVNENCELKIGDFGMARGLCTSPEEHKYFMTEYVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEMLGR
RQLFPGKNYVHQLQLILTVLGTPSQAVINAIGADRVRRYIQNLPNKQPVPWETLYPKADQQALDLLSQML
RFDPSERITVAEALQHPFLAKYHDPDDEPDCAPPFDFDFDAEALTREALKEAIVNE
>gnl|CDD|270843 cd07856, STKc_Sty1_Hog1, Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IFGTVFEITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHEN
IISLSDIFISPLEDIYFVTELLGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNIL
VNENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKD
HVNQFSIITELLGTPPDDVINTICSENTLRFVQSLPKRERVPFSEKFKNADPDAIDLLEKMLVFDPKKRI
SAAEALAHPYLAPYHDPTDEPVADEKFDWSFNDADLPVDTWKVMMYSE
>gnl|CDD|173750 cd07857, STKc_MPK1, Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYELIKELGQGAYGIVCSARNAETSEEETVAIKKITNVFSKKILAKRALRELKLLRHFRGHKNITCLYDM
DIVFPGNFNELYLYEELMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNA
DCELKICDFGLARGFSENPGENAGFMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRKPVF
KGKDYVDQLNQILQVLGTPDEETLSRIGSPKAQNYIRSLPNIPKKPFESIFPNANPLALDLLEKLLAFDP
TKRISVEEALEHPYLAIWHDPDDEPVCQKPFDFSFESEDSMEELRDMIIEEV
>gnl|CDD|143363 cd07858, STKc_TEY_MAPK, Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FEVDTKYVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIAIK
DIMPPPHREAFNDVYIVYELMDTDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLL
LNANCDLKICDFGLARTTSEKGDFMTEYVVTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELLGRKPLFP
GKDYVHQLKLITELLGSPSEEDLGFIRNEKARRYIRSLPYTPRQSFARLFPHANPLAIDLLEKMLVFDPS
KRITVEEALAHPYLASLHDPSDEPVCQTPFSFDFEEDALTEEDIKELIYNEMLAYHP
>gnl|CDD|143364 cd07859, STKc_TDY_MAPK, Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLP
PSRREFKDIYVVFELMESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADC
KLKICDFGLARVAFNDTPTAIFWTDYVATRWYRAPELCGSFFSKYTPAIDIWSIGCIFAEVLTGKPLFPG
KNVVHQLDLITDLLGTPSPETISRVRNEKARRYLSSMRKKQPVPFSQKFPNADPLALRLLERLLAFDPKD
RPTAEEALADPYFKGLAKVEREPSAQPITKLEFEFERRRLTKEDVRELIYREILEYHP
>gnl|CDD|270844 cd07860, STKc_CDK2_3, Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHT
ENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIK
LADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQL
FRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRDLLSQMLHYDPNKRISAKAALA
HPFF
>gnl|CDD|270845 cd07861, STKc_CDK1_euk, Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQ
ENRLYLVFEFLSMDLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVI
KLADFGLARAFGIPVRVYTHEVVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQ
LFRIFRILGTPTEDIWPGVTSLPDYKNTFPKWKKGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKAL
VHPYF
>gnl|CDD|270846 cd07862, STKc_CDK6, Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QQYECVAEIGEGAYGKVFKARDLKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLETFEHPNVVRLF
DVCTVSRTDRETKLTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQN
ILVTSSGQIKLADFGLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFR
GSSDVDQLGKILDVIGLPGEEDWPRDVALPRQAFHSKSAQPIEKFVTDIDELGKDLLLKCLTFNPAKRIS
AYSALSHPYF
>gnl|CDD|143368 cd07863, STKc_CDK4, Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLSTVREVALLKRLEAFDHPNIVRLMDV
CATSRTDRETKVTLVFEHVDQDLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENIL
VTSGGQVKLADFGLARIYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGN
SEADQLGKIFDLIGLPPEDDWPRDVTLPRGAFSPRGPRPVQSVVPEIEESGAQLLLEMLTFNPHKRISAF
RALQHPFF
>gnl|CDD|270847 cd07864, STKc_CDK12, Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
WGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVN
LKEIVTDKQDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHR
DIKCSNILLNNKGQIKLADFGLARLYNSEESRPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGE
LFTKKPIFQANQELAQLELISRLCGSPCPAVWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPTPALDLLD
HMLTLDPSKRCTAEQALNSPWL
>gnl|CDD|270848 cd07865, STKc_CDK9, Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DQVEFPFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGFPITALREIKILQLLKH
ENVVNLIEICRTKATPYNRYKGSIYLVFEFCEHDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKI
LHRDMKAANILITKDGVLKLADFGLARAFSLAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDMWGA
GCIMAEMWTRSPIMQGNTEQHQLTLISQLCGSITPEVWPGVDKLELFKKMELPQGQKRKVKERLKPYVKD
PYALDLIDKLLVLDPAKRIDADTALNHDFF
>gnl|CDD|270849 cd07866, STKc_BUR1, Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FYGCSKLRDYEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDGFPITALREIKILKKLKHPNVV
PLIDMAVERPDKSKRKRGSVYMVTPYMDHDLSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRD
IKAANILIDNQGILKIADFGLARPYDGPPPNPKGGGGGGTRKYTNLVVTRWYRPPELLLGERRYTTAVDI
WGIGCVFAEMFTRRPILQGKSDIDQLHLIFKLCGTPTEETWPGWRSLPGCEGVHSFTNYPRTLEERFGKL
GPEGLDLLSKLLSLDPYKRLTASDALEHPYF
>gnl|CDD|270850 cd07867, STKc_CDC2L6, Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DLFEYEGCKVGRGTYGHVYKAKRKDGKDEKEYALKQIEGTGISMSACREIALLRELKHPNVIALQKVFLS
HSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANI
LVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAEL
LTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYM
EKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF
>gnl|CDD|270851 cd07868, STKc_CDK8, Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YDFKVKLTGERERVEDLFEYEGCKVGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSACREIALLRE
LKHPNVISLQKVFLSHADRKVWLLFDYAEHDLWHIIKFHRASKANKKPVQLPRGMVKSLLYQILDGIHYL
HANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYT
KAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPYHHDQLDRIFNVMGFPADKDWEDIKKMPEHSTLMKD
FRRNTYTNCSLIKYMEKHKVKPDSKAFHLLQKLLTMDPIKRITSEQAMQDPYF
>gnl|CDD|143374 cd07869, STKc_PFTAIRE1, Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHD
IIHTKETLTLVFEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTG
ELKLADFGLARAKSVPSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDI
QDQLERIFLVLGTPNEDTWPGVHSLPHFKPERFTLYSPKNLRQAWNKLSYVNHAEDLASKLLQCFPKNRL
SAQAALSHEYFSDLPPRLWELTD
>gnl|CDD|270852 cd07870, STKc_PFTAIRE2, Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SYLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTK
ETLTFVFEYMHTDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLA
DFGLARAKSIPSQTYSSEVVTLWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVFEQLE
KIWTVLGVPTEDTWPGVSKLPNYKPEWFLPCKPQQLRVVWKRLSRPPKAEDLASQMLMMFPKDRISAQDA
LLHPYF
>gnl|CDD|270853 cd07871, STKc_PCTAIRE3, Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FGKLETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHD
IIHTERCLTLVFEYLDSDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKG
ELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVK
EELHLIFRLLGTPTEETWPGVTSNEEFRSYLFPQYRAQPLINHAPRLDTDGIDLLSSLLLYETKSRISAE
AALRHSYF
>gnl|CDD|143377 cd07872, STKc_PCTAIRE2, Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GFGKMETYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLH
DIVHTDKSLTLVFEYLDKDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINER
GELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTV
EDELHLIFRLLGTPTEETWPGISSNDEFKNYNFPKYKPQPLINHAPRLDTEGIELLTKFLQYESKKRISA
EEAMKHAYFRSLGTRIHSLPESISIFSLK
>gnl|CDD|270854 cd07873, STKc_PCTAIRE1, Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIH
TEKSLTLVFEYLDKDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELK
LADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQL
HFIFRILGTPTEETWPGILSNEEFKSYNYPKYRADALHNHAPRLDSDGADLLSKLLQFEGRKRISAEEAM
KHPYFHSLGERIHKLPD
>gnl|CDD|143379 cd07874, STKc_JNK3, Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLM
KCVNHKNIISLLNVFTPQKSLEEFQDVYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGI
IHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGE
MVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPADSEHN
KLKASQARDLLSKMLVIDPAKRISVDEALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIY
KEVMN
>gnl|CDD|143380 cd07875, STKc_JNK1, Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRA
YRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIK
HLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWS
VGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLF
PADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIE
EWKELIYKEVMDLE
>gnl|CDD|143381 cd07876, STKc_JNK2, Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SEEDSQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRE
LVLLKCVNHKNIISLLNVFTPQKSLEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLH
SAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGC
IMGELVKGSVIFQGTDHIDQWNKVIEQLGTPSAEFMNRLQPTVRNYVENRPQYPGISFEELFPDWIFPSE
SERDKLKTSQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEAEAPPPQIYDAQLEEREHAIEEWK
ELIYKEVMD
>gnl|CDD|143382 cd07877, STKc_p38alpha, Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLL
KHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSAD
IIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAE
LLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLL
EKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVP
>gnl|CDD|143383 cd07878, STKc_p38beta, Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FYRQELNKTVWEVPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKH
MKHENVIGLLDVFTPATSIENFNEVYLVTNLMGADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGII
HRDLKPSNVAVNEDCELRILDFGLARQADDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELL
KGKALFPGNDYIDQLKRIMEVVGTPSPEVLKKISSEHARKYIQSLPHMPQQDLKKIFRGANPLAIDLLEK
MLVLDSDKRISASEALAHPYFSQYHDPEDEPEAEPYDESPENKERTIEEWKELTYEEVSSFKP
>gnl|CDD|143384 cd07879, STKc_p38delta, Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FYREEVNKTVWELPERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKH
MQHENVIGLLDVFTSAVSGDEFQDFYLVMPYMQTDLQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIH
RDLKPGNLAVNEDCELKILDFGLARHADAEMTGYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLT
GKTLFKGKDYLDQLTQILKVTGVPGPEFVQKLEDKAAKSYIKSLPKYPRKDFSTLFPKASPQAVDLLEKM
LELDVDKRLTATEALEHPYFDSFRDADEETEQQPYDDSLENEKLSVDEWKKHIYKEVKSFSP
>gnl|CDD|143385 cd07880, STKc_p38gamma, Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YYRQEVNKTIWEVPDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKH
MKHENVIGLLDVFTPDLSLDRFHDFYLVMPFMGTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGII
HRDLKPGNLAVNEDCELKILDFGLARQTDSEMTGYVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEML
TGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQKLQSEDAKNYVKKLPRFRKKDFRSLLPNANPLAVNVLEK
MLVLDAESRITAAEALAHPYFEEFHDPEDETEAPPYDDSFDEVDQSLEEWKRLTFTEILSFQP
>gnl|CDD|143641 cd07881, RHD-n_NFAT, N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells (NFAT) proteins. Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes that are mainly involved in cell-cell interaction. Upon de-phosphorylation of the nuclear localization signal, NFAT enters the nucleus and acts as a transcription factor; its export from the nucleus is triggered by phosphorylation via export kinases. NFATs play important roles in mediating the immune response, and are found in T cells, B Cells, NK cells, mast cells, and monocytes. NFATs are also found in various non-hematopoietic cell types, where they play roles in development
DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMENKPLTLQMFIGTADDRY
LRPHAFYQVHRITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGR
KNTRVRLVFRVHIPQPSGRVLSLQVASNPIECSQR
>gnl|CDD|143642 cd07882, RHD-n_TonEBP, N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding protein (TonEBP). Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the tonicity-responsive enhancer binding protein (TonEBP), also called NFAT5. Mammalian TonEBP regulates the expression of genes in response to tonicity. It plays a pivotal role in urinary concentrating mechanisms in kidney medulla, by triggering the accumulation of osmolytes that enable renal medullary cells to tolerate high levels of urea and salt
KELKILVQPETQHRARYLTEGSRGSVKDRSQQGFPTVKLEGYNKPVVLQVFVGTDSGRVKPHGFYQACKV
TGRNTTPCEEVDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVII
PRKDGSTLTLQTVSNPILCTQ
>gnl|CDD|143643 cd07883, RHD-n_NFkB, N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light polypeptide gene enhancer in B-cells (NF-kappa B). Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B1 and B2 families of transcription factors, also referred to as class I members of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. Family members include NF-kappa B1 and NF-kappa B2. NF-kappa B1 is commonly referred to as p105 or p50 (proteolytically processed form), while NF-kappa B2 is called p100 or p52 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). p105 and p100 may also act as I-kappa Bs due to their C-terminal ankyrin repeats
PYLEILEQPKQRGFRFRYGCEGPSHGGLPGASSEKNKKSYPTVKICNYQGPARIVVQLVTNSEPPRLHAH
SLVGKHCEDGICTVQVGPKDMTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNPGDLVHVDAEGGGDR
QLTDEEQAEIRQKAKQQAKSMDLSVVRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK
>gnl|CDD|143644 cd07884, RHD-n_Relish, N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish. Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the arthropod Relish protein, in which the RHD domain co-occurs with C-terminal ankyrin repeats. Family members are sometimes referred to as p110 or p68 (proteolytically processed form). Relish is an NF-kappa B-like transcription factor, which plays a role in mediating innate immunity in Drosophila. It is activated via the Imd (immune deficiency) pathway, which triggers phosphorylation of Relish. IKK-dependent proteolytic cleavage of Relish (which involves Dredd) results in a smaller active form (without the C-terminal ankyrin repeats), which is transported into the nucleus and functions as a transactivator
PFLRIVEQPVDKFRFRYKSEMHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQADDNRRKPHV
HKLVGKQGDDDVCDPHDIEVSPEGDYVAMFQNMGIIHTAKKNIPEELYKKKNMNLNQVVLRFQAFAVSAN
GHLRPICPPVYSNPINNLK
>gnl|CDD|143645 cd07885, RHD-n_RelA, N-terminal sub-domain of the Rel homology domain (RHD) of RelA. Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD domain of the RelA family of transcription factors, categorized as a class II member of the NF-kappa B family. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). RelA (also called p65) forms heterodimers with NF-kappa B1 (p50) and B2 (p52). RelA also forms homodimers
PYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINNYTGPGRVRISLVTKDPPHKPHPH
ELVGKDCKDGYYEAELSPDRCIHSFQNLGIQCVKKRDLEQAVSQRIQTNNNPFNVPIEEQRADYDLNAVR
LCFQVTVRDPSGRLLPLPPVLSQPIYDNR
>gnl|CDD|143646 cd07886, RHD-n_RelB, N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral oncogene homolog B (RelB) protein. Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the RelB family of transcription factors, categorized as class II NF-kappa B family members. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). RelB, is unable to homodimerize but is a potent transactivator in a heterodimer with NF-kappa B1 (p50) or B2 (p52). It is involved in the regulation of genes that play roles in inflammatory processes and the immune response
PRLLITEQPKQRGMRFRYECEGRSAGSILGESSTEANKTQPAIEIQNCIGLKEVTVTVCLVWKDPPHRVH
PHGLVGKDCPNGICQVTLNPHSSPRHSFSNLGIQCVRKREIEAAIETRLQLNIDPFKAGSLKNHEEVDMN
VVRLCFQASYRDDDGRKDCLSPVLSEPIYDKK
>gnl|CDD|143647 cd07887, RHD-n_Dorsal_Dif, N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal. Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the arthropod Dorsal and Dif (Dorsal-related immunity factor), and similar proteins. Dorsal and Dif are Rel-like transcription factors, which play roles in mediating innate immunity in Drosophila. They are activated via the Toll pathway. Cytoplasmic Dorsal/Dif are inactivated via forming a complex with Cactus, the Drosophila homologue of mammalian I-kappa B proteins. In response to signals, Cactus is degraded and Dorsal/Dif can be transported into the nucleus, where they act as transcription factors. Dorsal is also an essential gene in establishing the proper dorsal/ventral polarity in the developing embryo
PYVRIVEQPTSRALRFRYECEGRSAGSIPGANSTSEGKTFPTIQVVNYDGRAVVVVSCVTKDEPFRPHPH
NLVGKEGCKKGVCTKKINPTEMRIVFQKLGIQCVKKKDVEESLKLREEINVDPFRTGFDHKDQINSIDLN
VVRLCFQVFLEDENGRFTVPLPPVVSDPIYDKK
>gnl|CDD|143579 cd07888, CRD_corin_2, One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease . The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the second (C-terminal) CRD
QCEPITLELCMNLPYNTTRYPNYLGHRTQKEASISWESSLFPALVQTNCYKYLMFFACTILVPKCDPVTQ
QRIPPCRSLCRNSKERCESVLGIVGLQWPEDTDCAQFPEENSDNQTCLLPDE
>gnl|CDD|143628 cd07890, CYTH-like_AC_IV-like, Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily. This subgroup contains class IV ACs and similar proteins. AC catalyzes the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. cAMP is a key signaling molecule which conveys a variety of signals in different cell types. In prokaryotes, cAMP is a catabolite derepression signal which triggers the expression of metabolic pathways including the lactose operon. Six non-homologous classes of ACs have been identified (I-VI). Class IV ACs are found in this group. In bacteria, the gene encoding Class IV AC has been designated cyaB and the protein as AC2. AC-IV occurs in addition to AC-I in bacterial pathogens such as Yersinia pestis (plague disease). The role of AC-IV is unknown but it has been speculated that it may be a factor in pathogenesis, perhaps providing cAMP for a secondary internal signaling function, or for secretion and uptake into host cells, where it may disrupt normal cellular processes. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel
EVEIKARVDDLEALRERLAALGGAEGGREFQEDIYFDHPDRDLAATDEALRLRRMGDSGKTLLTYKGPKL
DGGPKVREEIETEVADPEAMKEILERLGFGPVGRVKKEREIYLLGQTRVHLDRVEGLGDFVEIEVVLEDI
EEAEEGLGEAAELLGLLEYDEETLSYLEL
>gnl|CDD|143629 cd07891, CYTH-like_CthTTM-like_1, CYTH-like Clostridium thermocellum TTM-like subgroup 1. This subgroup contains the triphosphate tunnel metalloenzyme (TTM) from Clostridium thermocellum (CthTTM) and similar proteins. These are found primarily in bacteria. CthTTM is a metal dependent tripolyphosphatase, nucleoside triphosphatase, and nucleoside tetraphosphatase. It hydrolyzes the beta-gamma phosphoanhydride linkage of triphosphate-containing substrates including tripolyphosphate, nucleoside triphosphates and nucleoside tetraphosphates. These substrates are hydrolyzed, releasing Pi. Mg++ or Mn++ are required for the enzyme's activity. CthTTM appears to have no adenylate cyclase activity. This subgroup consists chiefly of bacterial sequences. These enzymes are members of the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily, which have a unique active site located within an eight-stranded beta barrel
LEIERKFLVKGDAWRALAAKGVRIRQGYLSTDPERTVRVRIAGDRAYLTIKGPTNGLSRYEFEYEIPLAD
AEELLALCEGPVIEKTRYRVPHGGHTWEVDVFHGENAGLVVAEIELPSEDEPFELPDWLGREVTGDPRYY
NASLAKHP
>gnl|CDD|143630 cd07892, PolyPPase_VTC2-3_like, Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins VTC-2, and -3, and similar proteins. Saccharomyces cerevisiae VTC-1, -2, -3, and -4 comprise the membrane-integral VTC complex. VTC-2, -3, and -4 contain polyP polymerase domains. S. cerevisiae VTC-2,and -3 belong to this subgroup. For VTC4 it has been shown that this domain generates polyP from ATP by a phosphotransfer reaction releasing ADP. This activity is metal ion-dependent. The ATP gamma phosphate may be cleaved and then transferred to an acceptor phosphate to form polyP. PolyP is ubiquitous. In prokaryotes, it is a store of phosphate and energy. In eukaryotes, polyPs have roles in bone calcification, and osmoregulation, and in phosphate transport in the symbiosis of mycorrhizal fungi and plants. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel
NSSDDNFKSYKFWVHPDNLMEVKTRILRHLPVLVYNNQSSEDDDDVLGAGSEDPTITTLYFDNPNFDLYN
DKLLKLNEAPTLRLRWTGKLSDKPDIFVEKKTFDENTSSFEEDKLQLKEKYINGFIFGKYKFEKKLQKME
KRGADLENLKKDVENIQDFIRENKLQPVLRAVYTRTAFQIPGDDRIRVSIDSDIAFIREDSFDKDRPIRD
PNDWHRTDIDDSNSNPFKFLRKGEYSKFPYSVLEIKVKESLNKNRKHYEWVNDLTNSHLVKEVPKFSKFV
QGVASLFEEDDKLNILPFWLPDL
>gnl|CDD|153435 cd07893, OBF_DNA_ligase, The Oligonucleotide/oligosaccharide binding (OB)-fold domain is a DNA-binding module that is part of the catalytic core unit of ATP dependent DNA ligases. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP dependent DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains including a DNA-binding domain, an adenylation (nucleotidyltransferase (NTase)) domain, and an oligonucleotide/oligosaccharide binding (OB)-fold domain. The adenylation and C-terminal OB-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core unit contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases. The OB-fold domain contacts the nicked DNA substrate and is required for the ATP-dependent DNA ligase nucleotidylation step. The RxDK motif (motif VI), which is essential for ATP hydrolysis, is located in the OB-fold domain
DTLDLVIVGAYYGKGRRGGGIGAFLCAVYDPERDEFQTICKVGSGFTDEELEELRELLKELKTPEKPPRV
NSIEKPDFWVEPKVVVEVLADEITRSPMHTAGRGEEEEGYALRFPRFVRIRDDKGPEDA
>gnl|CDD|185705 cd07894, Adenylation_RNA_ligase, Adenylation domain of RNA circularization proteins. RNA circularization proteins are capable of circularizing RNA molecules in an ATP-dependent reaction. RNA circularization may protect RNA from exonuclease activity. This model comprises the adenylation domain, the minimal catalytic unit that is common to all members of the ATP-dependent DNA ligase family, and the carboxy-terminal extension of RNA circularization protein that serves as a dimerization module. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation of nicked nucleic acid substrates using the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. The adenylation domain binds ATP and contains many active site residues
EYLRFRKDFKGIERGTVILLNEGEVIRGYPKIGRALLLEPGIKEHFKGPVAVEEKMNGYNVRIVRIGGKV
LAFTRGGFICPFTTDRLRDLIDPEFFDDHPDLVLCGEVVGPENPYVPGSYPEVEDVGFFVFDIRKKNTGR
PLPVEERRELLEKYGLPTVRLFGEFTADEIEELKEIIRELDKEGREGVVLKDPDMRVPPLKYTTSYSNCS
DIRYAFRYPFDLGRDFFFSRIVREGFQSVELGESEEELEERALELGEAILEPLVEAIRKVARGERVYEEF
RLRFRSEETAEEFLEHLRRLGVHIEIVELELEREGGYWVVRFDKVFPSTTDKLRSILEGGLW
>gnl|CDD|185706 cd07895, Adenylation_mRNA_capping, Adenylation domain of GTP-dependent mRNA capping enzymes. RNA capping enzymes transfer GMP from GTP to the 5'-diphosphate end of nascent mRNAs to form a G(5')ppp(5')RNA cap structure. The RNA cap is found only in eukarya. RNA capping is chemically analogous to the first two steps of polynucleotide ligation. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation of nicked nucleic acid substrates using the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. Structural studies reveal a shared structure for DNA ligases and capping enzymes, with a common catalytic core composed of an adenylation or nucleotidyltransferase domain and a C-terminal OB-fold domain containing conserved sequence motifs. The adenylation domain binds ATP and contains many active site residues
EKLSELRRKVAELCPGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGEVYLIDRK
NDVFKVPGLFFPRRKNLEPHHQGTLLDGELVIDKVPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKK
EVIEPRNELLKKGPIDKAKEPFSVRLKDFFPLYKIEKLFEKIIPKLPHENDGLIFTPNDEPYVPGTDKNL
LKWKP
>gnl|CDD|185707 cd07896, Adenylation_kDNA_ligase_like, Adenylation domain of kDNA ligases and similar proteins. The mitochondrial DNA of parasitic protozoans is highly unusual. It is termed the kinetoplast DNA (kDNA) and consists of circular DNA molecules (maxicircles) and several thousand smaller circular molecules (minicircles). This group is composed of kDNA ligase, Chlorella virus DNA ligase, and similar proteins. kDNA ligase and Chlorella virus DNA ligase are the smallest known ATP-dependent ligases. They are involved in DNA replication or repair. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. They have a highly modular architecture consisting of a unique arrangement of two or more discrete domains. The adenylation and the C-terminal oligonucleotide/oligosaccharide binding (OB)-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family, including this group. The adenylation domain binds ATP and contains many of the active-site residues
PELLLAKTYDEGEDISGYLVSEKLDGVRAYWDGKQLLSRSGKPIAAPAWFTAGLPPFPLDGELWIGRGQF
EQTSSIVRSKKPDDEDWRKVKFMVFDLPSAKGPFEERLERLKNLLEKIPNPHIKIVPQIPVKSNEALDQY
LDEVVAAGGEGLMLRRPDAPYETGRSDNLLKLKP
>gnl|CDD|185708 cd07897, Adenylation_DNA_ligase_Bac1, Adenylation domain of putative bacterial ATP-dependent DNA ligases. Bacterial DNA ligases are divided into two broad classes: NAD-dependent and ATP-dependent. All bacterial species have a NAD-dependent DNA ligase (LigA). Some bacterial genomes contain multiple genes for DNA ligases that are predicted to use ATP as their cofactor, including Mycobacterium tuberculosis LigB, LigC, and LigD. This group is composed of predicted bacterial ATP-dependent DNA ligases. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three-step reaction mechanism. The adenylation and C-terminal oligonucleotide/oligosaccharide binding (OB)-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family, including this group. The adenylation domain binds ATP and contains many of the active site residues
ASRPYPFMLAHPLEDDPEDLGDPSDWQAEWKWDGIRGQLIRRGGEVFLWSRGEELITGSFPELLAAAEAL
PDGTVLDGELLVWRDGRPLPFNDLQQRLGRKTVGKKLLAEAPAAFRAYDLLELNGEDLRALPLRERRARL
EALLARLPPPRLDLSPLIAFADWEELAALRAQSRERGAEGLMLKRRDSPYLVGRKKGDWWKWKIDPL
>gnl|CDD|185709 cd07898, Adenylation_DNA_ligase, Adenylation domain of ATP-dependent DNA Ligases. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent ligases are present in many organisms such as viruses, bacteriophages, eukarya, archaea and bacteria. Some organisms express a variety of different ligases which appear to be targeted to specific functions. ATP-dependent DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains including a DNA-binding domain, an adenylation (nucleotidyltransferase (NTase)) domain, and an oligonucleotide/oligosaccharide binding (OB)-fold domain. The adenylation domain binds ATP and contains many of the active-site residues. The adenylation and C-terminal OB-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core unit contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases
IKPMLAHPEESAEAAKAKKPAAAWVEDKYDGIRAQVHKDGGRVEIFSRSLEDITDQFPELAAAAKALPHE
FILDGEILAWDDNRGLPFSELFKRLGRKFRDKFLDEDVPVVLMAFDLLYLNGESLLDRPLRERRQLLEEL
FVEIPGRIRIAPALPVESAEELEAAFARARARGNEGLMLKDPDSPYEPGRRGLAWLKLKKE
>gnl|CDD|185710 cd07900, Adenylation_DNA_ligase_I_Euk, Adenylation domain of eukaryotic DNA Ligase I. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent ligases are present in many organisms such as viruses, bacteriophages, eukarya, archaea and bacteria. Some organisms express a variety of different ligases which appear to be targeted to specific functions. There are three classes of ATP-dependent DNA ligases in eukaryotic cells (I, III and IV). DNA ligase I is required for the ligation of Okazaki fragments during lagging-strand DNA synthesis and for base excision repair (BER). DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains. The adenylation and C-terminal oligonucleotide/oligosaccharide binding (OB)-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The adenylation domain binds ATP and contains many of the active-site residues. DNA ligase I is the main replicative ligase in eukaryotes. The common catalytic core unit comprises six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases
HCKLTPGIPVKPMLAKPTKGVSEVLDRFEDKEFTCEYKYDGERAQIHLLEDGKVKIFSRNLENNTEKYPD
IVAVLPKSLKPSVKSFILDSEIVAYDRETGKILPFQVLSTRKRKDVDANDIKVQVCVFAFDLLYLNGESL
LKKPLRERRELLHSLFKEVPGRFQFATSKDSEDTEEIQEFLEEAVKNNCEGLMVKTLDSDATYEPSKRSH
NWLKLKKDY
>gnl|CDD|185711 cd07901, Adenylation_DNA_ligase_Arch_LigB, Adenylation domain of archaeal and bacterial LigB-like DNA ligases. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent ligases are present in many organisms such as viruses, bacteriophages, eukarya, archaea and bacteria. Bacterial DNA ligases are divided into two broad classes: NAD-dependent and ATP-dependent. All bacterial species have a NAD-dependent DNA ligase (LigA). Some bacterial genomes contain multiple genes for DNA ligases that are predicted to use ATP as their cofactor, including Mycobacterium tuberculosis LigB, LigC, and LigD. This group is composed of archaeal DNA ligases and bacterial proteins similar to Mycobacterium tuberculosis LigB. Members of this group contain adenylation and C-terminal oligonucleotide/oligosaccharide binding (OB)-fold domains, comprising a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The adenylation domain binds ATP and contains many of the active-site residues. The common catalytic core unit comprises six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases
VGRPVRPMLAQRAPSVEEALIKEGGEAAVEYKYDGIRVQIHKDGDEVRIFSRRLEDITNALPEVVEAVRE
LVKAEDAILDGEAVAYDPDGRPLPFQETLRRFRRKYDVEEAAEEIPLTLFLFDILYLDGEDLLDLPLSER
RKILEEIVPETEAILLAPRIVTDDPEEAEEFFEEALEAGHEGVMVKSLDSPYQAGRRGKNWLKVKPD
>gnl|CDD|185712 cd07902, Adenylation_DNA_ligase_III, Adenylation domain of DNA Ligase III. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three-step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent ligases are present in many organisms such as viruses, bacteriophages, eukarya, archaea and bacteria. There are three classes of ATP-dependent DNA ligases in eukaryotic cells (I, III and IV). DNA ligase III is not found in lower eukaryotes and is present both in the nucleus and mitochondria. It has several isoforms; two splice forms, III-alpha and III-beta, differ in their carboxy-terminal sequences. DNA ligase III-beta is believed to play a role in homologous recombination during meiotic prophase. DNA ligase III-alpha interacts with X-ray Cross Complementing factor 1 (XRCC1) and functions in single nucleotide Base Excision Repair (BER). The mitochondrial form of DNA ligase III originates from the nucleolus and is involved in the mitochondrial DNA repair pathway. This isoform is expressed by a second start site on the DNA ligase III gene. DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains. The adenylation and C-terminal oligonucleotide/oligosaccharide binding (OB)-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The adenylation domain binds ATP and contains many active site residues. The common catalytic core unit comprises six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases
KKKLSVRASLMTPVKPMLAEACKSVEDAMKKCPNGMYAEIKYDGERVQVHKQGDNFKFFSRSLKPVLPHK
VAHFKDYIPKAFPHGHSMILDSEVLLVDTKTGKPLPFGTLGIHKKSAFKDANVCLFVFDCLYYNGESLMD
KPLRERRKILEDNMVEIPNRIMLSEMKFVKKADDLSAMIARVIKEGLEGLVLKDLKSVYEPGKRHWLKVK
KDY
>gnl|CDD|185713 cd07903, Adenylation_DNA_ligase_IV, Adenylation domain of DNA Ligase IV. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent ligases are present in many organisms such as viruses, bacteriophages, eukarya, archaea and bacteria. There are three classes of ATP-dependent DNA ligase in eukaryotic cells (I, III and IV). DNA ligase IV is required for DNA non-homologous end joining pathways, including recombination of the V(D)J immunoglobulin gene segments in cells of the mammalian immune system. DNA ligase IV is stabilized by forming a complex with XRCC4, a nuclear phosphoprotein, which is phosphorylated by DNA-dependent protein kinase. DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains. The adenylation and C-terminal oligonucleotide/oligosaccharide binding (OB)-fold domains comprise a catalytic core unit that is common to all members of the ATP-dependent DNA ligase family. The adenylation domain binds ATP and contains many of the active-site residues. The common catalytic unit comprises six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases
KNDLSIELFSPFRPMLAERLNIGYVEIKLLKGKPFYIETKLDGERIQLHKDGNEFKYFSRNGNDYTYLYG
ASLTPGSLTPYIHLAFNPKVKSCILDGEMVVWDKETKRFLPFGTLKDVAKLREVEDSDLQPCFVVFDILY
LNGKSLTNLPLHERKKLLEKIITPIPGRLEVVKRTEASTKEEIEEALNEAIDNREEGIVVKDLDSKYKPG
KRGGGWIKIKPEYLD
>gnl|CDD|185714 cd07905, Adenylation_DNA_ligase_LigC, Adenylation domain of Mycobacterium tuberculosis LigC-like ATP-dependent DNA ligases. Bacterial DNA ligases are divided into two broad classes: NAD-dependent and ATP-dependent. All bacterial species have a NAD-dependent DNA ligase (LigA). Some bacterial genomes contain multiple genes for DNA ligases that are predicted to use ATP as their cofactor, including Mycobacterium tuberculosis LigB, LigC, and LigD. This group is composed of ATP-dependent DNA ligases similar to Mycobacterium tuberculosis LigC. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. Members of this group contain adenylation and C-terminal oligonucleotide/oligosaccharide binding (OB)-fold domains, comprising a catalytic core unit that is common to all members of the ATP-dependent DNA ligase family. The adenylation domain binds ATP and contains many of the active-site residues. The common catalytic core unit comprises six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases
VEPMLARAVDALPEPGGWQYEPKWDGFRCLAFRDGDEVRLQSRSGKPLTRYFPELVAAARALLPPGCVLD
GELVVWRGGRLDFDALQQRIHPAASRVRRLAEETPASFVAFDLLALGGRDLRGRPLRERRAALEALLAGW
GPPLHLSPATTDRAEAREWLEEFEGAGLEGVVAKRLDGPYRPGERAMLKVKHRR
>gnl|CDD|185715 cd07906, Adenylation_DNA_ligase_LigD_LigC, Adenylation domain of Mycobacterium tuberculosis LigD and LigC-like ATP-dependent DNA ligases. Bacterial DNA ligases are divided into two broad classes: NAD-dependent and ATP-dependent. All bacterial species have a NAD-dependent DNA ligase (LigA). Some bacterial genomes contain multiple genes for DNA ligases that are predicted to use ATP as their cofactor, including Mycobacterium tuberculosis LigB, LigC, and LigD. This group is composed of ATP-dependent DNA ligases similar to Mycobacterium tuberculosis LigC. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. Members of this group contain adenylation and C-terminal oligonucleotide/oligosaccharide binding (OB)-fold domains, comprising a catalytic core unit that is common to all members of the ATP-dependent DNA ligase family. The adenylation domain binds ATP and contains many of the active-site residues. The common catalytic core unit comprises six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases. LigD consists of a central ATP-dependent DNA ligase catalytic core unit fused to a C-terminal polymerase domain and an N-terminal 3'-phosphoesterase (PE) module. LigD catalyzes the end-healing and end-sealing steps during non-homologous end joining
IEPMLATLVDEPPDGEDWLYEIKWDGYRALARVDGGRVRLYSRNGLDWTARFPELAEALAALPVRDAVLD
GEIVVLDEGGRPDFQALQNRLRLRRRLARTVPVVYYAFDLLYLDGEDLRGLPLLERKELLEELLPAGSPR
LRVSEHFEGGGAALFAAACELGLEGIVAKRADSPYRSGRRSRDWLKIKCR
>gnl|CDD|153117 cd07908, Mn_catalase_like, Manganese catalase-like protein, ferritin-like diiron-binding domain. This uncharacterized bacterial protein family has a ferritin-like domain similar to that of the manganese catalase protein of Lactobacillus plantarum and the bll3758 protein of Bradyrhizobium japonicum. Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF)
PYPPIKVAGPNPRYAELLLDDYAGTNSELTAISQYIYQHLISEEKYPEIAETFLGIAIVEMHHLEILGQL
IVLLGGDPRYRSSSSDKFTYWTGKYVNYGESIKEMLKLDIASEKAAIAKYKRQAETIKDPYIRALLNRII
LDEKLHIKILEELL
>gnl|CDD|153118 cd07909, YciF, YciF bacterial stress response protein, ferritin-like iron-binding domain. YciF is a bacterial protein of unknown function that is up-regulated when bacteria experience stress conditions, and is highly conserved in a broad range of bacterial species. YciF has a ferritin-like domain. Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF)
HDLFVHELRDLYSAEKQLVKALPKMAKAATSEELKEAFESHLEETEGQVERLEQIFESLGEKPEGKKCKA
MEGLIKEAEELIEETGDSAVLDAALIAAAQKVEHYEIAGYGTLRALAKLLGLDDAADLLQETLDEEKATD
RKLTDLA
>gnl|CDD|153119 cd07910, MiaE, MiaE tRNA-modifying nonheme diiron monooxygenase, ferritin-like diiron-binding domain. MiaE is a nonheme diiron monooxygenase that catalyzes the posttranscriptional allylic hydroxylation of a modified nucleoside in tRNA called 2-methylthio-N-6-isopentenyl adenosine (ms2i6A). ms2i6A is found at position 37, next to the anticodon at the 3' position in almost all eukaryotic and bacterial tRNA's that read codons beginning with uridine. The miaE gene is absent in Escherichia coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species
LFLKSPTPPAWLDAALANLDEILIDHAHCEKKAASSAMSLIFRYPEKPELVEAMSDLAREELQHFEQVLK
IMKKRGIPLGPDSKDPYASGLRKLVRKGEPERLLDRLLVAALIEARSCERFALLAPALPDPELKKFYRGL
LESEARHYELFLDLARKYFDEEDVDARLDELLAAEAEIIA
>gnl|CDD|153120 cd07911, RNRR2_Rv0233_like, Ribonucleotide Reductase R2-like protein, Mn/Fe-binding domain. Rv0233 is a Mycobacterium tuberculosis ribonucleotide reductase R2 protein with a heterodinuclear manganese/iron-carboxylate cofactor located in its metal center. The Rv0233-like family may represent a structural/functional counterpart of the evolutionary ancestor of the RNRR2's (Ribonucleotide Reductase, R2/beta subunit) and the bacterial multicomponent monooxygenases. RNRR2s belong to a broad superfamily of ferritin-like diiron-carboxylate proteins. The RNR protein catalyzes the conversion of ribonucleotides to deoxyribonucleotides and is found in prokaryotes and archaea. The catalytically active form of RNR is a proposed alpha2-beta2 tetramer. The homodimeric alpha subunit (R1) contains the active site and redox active cysteines as well as the allosteric binding sites
GGLNWNSLPMKLFEKGKRKGFWNPADIDFSQDREDWEQLSEEERDLALRLCAGFIAGEEAVTLDLLPLMM
AMAAEGRLEEEMYLTQFLFEEAKHTDFFRRWLDAVGVSDDLSDLHTAVYREPFYEALPYAELRLYLDASP
AAQVRASVTYNMIVEGVLAETGYYAWRTICEKRGILPGMQEGIRRLGDDESRHIAWGTFTCRRLVAADDA
NWDVFEERMNELVPHALGLIDEIFELYDEMPFGLDPDELMQYAVDQFQRRLGYIERARGQPVEEIETDAT
>gnl|CDD|143653 cd07912, Tweety_N, N-terminal domain of the protein encoded by the Drosophila tweety gene and related proteins, a family of chloride ion channels. The protein product of the Drosophila tweety (tty) gene is thought to form a trans-membrane protein with five membrane-spanning regions and a cytoplasmic C-terminus. This N-terminal domain contains the putative transmembrane spanning regions. Tweety has been suggested as a candidate for a large conductance chloride channel, both in vertebrate and insect cells. Three human homologs have been identified and designated TTYH1-3. TTYH2 has been associated with the progression of cancer, and Drosophila melanogaster tweety has been assumed to play a role in development. TTYH2, and TTYH3 bind to and are ubiquinated by Nedd4-2, a HECT type E3 ubiquitin ligase, which most likely plays a role in controlling the cellular levels of tweety family proteins
MYKAPWLVKLLHSLPHLNFTFHRVNSTFNPEDEIYQQSLLILASIPAACLILSLLFLLVYLITRCCDRKP
TEERPRHSICCLKWSLVIATLLCCAAIGVGLYGNDETHDGVVQLTYSLRNANHTVAGIDNQTSDTEASLN
VTVEPQLTNLEDIFDARVNKTDYLQIVQGLQQMATNAAQQLTGIPFWSLVGVSLTKLADQVSLYESYRWL
AYLGLLSLLLVICLVLLVGLARHSRCLLIVFSVCGLFALIISWLSLGLYLASAVALSDFCVDPDDYVRNQ
TPSGLSSDILQYYLTCEPSTTNPFQQRLTESQRALTNMQSQVQGLLREAVFEFPTAEDNLLSLQGDLNST
EINLHQLTALLDCRGLHKDYVEALRGLCYDGLEGLLYLLLFSLLAALLFTILVCVDSHTWIYIRKRDD
>gnl|CDD|153419 cd07914, IGPD, Imidazoleglycerol-phosphate dehydratase. Imidazoleglycerol-phosphate dehydratase (IGPD; EC 4.2.1.19) catalyzes the dehydration of imidazole glycerol phosphate to imidazole acetol phosphate, the sixth step of histidine biosynthesis in plants and microorganisms where the histidine is synthesized de novo. There is an internal repeat in the protein domain that is related by pseudo-dyad symmetry, perhaps as a result of an ancient gene duplication. The apo-form of IGPD exists as a catalytically inactive trimer which, in the presence of specific divalent metal cations such as manganese (Mn2+), cobalt (Co2+), cadmium (Cd2+), nickel (Ni2+), iron (Fe2+) and zinc (Zn2+), assembles to form a biologically active high molecular weight metalloenzyme; a 24-mer with 4-3-2 symmetry. Each 24-mer has 24 active sites, and contains around 1.5 metal ions per monomer, each monomer contributing residues to three separate active sites. IGPD enzymes are monofunctional in fungi, plants, archaea and some eubacteria while they are encoded as bifunctional enzymes in other eubacteria, such that the enzyme is fused to histidinol-phosphate phosphatase, the penultimate enzyme of the histidine biosynthesis pathway. The histidine biosynthesis pathway is a potential target for development of herbicides, and IGPD is a target for the triazole phosphonate herbicides
AEIERKTKETDIEVELNLDGTGKSKIDTGIGFFDHMLTLFARHGGFDLTVKAKGDLEVDDHHTVEDVGIV
LGQALKKALGDKKGIRRYGSALVPMDEALARVAVDLSGRPYLVFDAEFPREKIGDFDTELVEEFFRSFAN
NAGITLHIRVLYGRNDHHIIEAIFKAFARALRQAVAIDGRGGVPSTKGVL
>gnl|CDD|153420 cd07920, Pumilio, Pumilio-family RNA binding domain. Puf repeats (also labelled PUM-HD or Pumilio homology domain) mediate sequence specific RNA binding in fly Pumilio, worm FBF-1 and FBF-2, and many other proteins such as vertebrate Pumilio. These proteins function as translational repressors in early embryonic development by binding to sequences in the 3' UTR of target mRNAs, such as the nanos response element (NRE) in fly Hunchback mRNA, or the point mutation element (PME) in worm fem-3 mRNA. Other proteins that contain Puf domains are also plausible RNA binding proteins. Yeast PUF1 (JSN1), for instance, appears to contain a single RNA-recognition motif (RRM) domain. Puf repeat proteins have been observed to function asymmetrically and may be responsible for creating protein gradients involved in the specification of cell fate and differentiation. Puf domains usually occur as a tandem repeat of 8 domains. This model encompasses all 8 tandem repeats. Some proteins may have fewer (canonical) repeats
SLTLQDIKAGHIVEFAKDQHGSRFLQQKLEEATPEEKELIFDEILPHVVELMVDPFGNYVIQKLFEHGTE
EQRLQLLEKILGHVVRLSLDMYGCRVIQKLLESISEEQISLLVKELRGHVVELVKDQNGNHVIQKCIEKF
PPEDLQFIIDAFKGNCVALSTHPYGCRVIQRCLEHCSEEQREPLLEEILEHALELVQDQFGNYVVQHVLE
LGDPDDTSRIIEKLLGNIVQLSCHKFASNVVEKCLKHASKEERELIIDEILASGNETSALDTLMKDQYGN
YVIQTALDVAKEEQRELLVEAIRPHLPSLRKSPYGKHILAKL
>gnl|CDD|153391 cd07921, PCA_45_Doxase_A_like, Subunit A of the Class III Extradiol dioxygenase, Protocatechuate 4,5-dioxygenase, and similar enzymes. This subfamily includes the A subunit of protocatechuate (PCA) 4,5-dioxygenase (LigAB) and two subfamilies of unknown function. The A subunit is the smaller, non-catalytic subunit of LigAB. PCA 4,5-dioxygenase catalyzes the oxidization and subsequent ring-opening of PCA (or 3,4-dihydroxybenzoic acid), which is an intermediate in the breakdown of lignin and other compounds. PCA 4,5-dioxygenase is one of the aromatic ring opening dioxygenases which play key roles in the degradation of aromatic compounds. As members of the Class III extradiol dioxygenase family, the enzymes use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. LigAB-like class III enzymes are usually composed of two subunits, designated A and B, which form a tetramer composed of two copies of each subunit
GTYVFDAERSRKGYALNKMCMSLNKAENREAFKADEEAYCDKFGLTEEQKQAVLDRDWLRLLELGGNIYY
LLKLAAIDGKSMQDIGAQMTGMTEEEFRAMMVAGGR
>gnl|CDD|153392 cd07922, CarBa, CarBa is the A subunit of 2-aminophenol 1,6-dioxygenase, which catalyzes the oxidization and subsequent ring-opening of 2-aminophenyl-2,3-diol. CarBa is the A subunit of 2-aminophenol 1,6-dioxygenase, which catalyzes the oxidization and subsequent ring-opening of 2-aminophenyl-2,3-diol. 2-aminophenol 1,6-dioxygenase is a key enzyme in the carbazole degradation pathway isolated from bacterial strains with carbazole degradation ability. The enzyme is a heterotetramer composed of two A and two B subunits. CarB belongs to the class III extradiol dioxygenase family, composed of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. Although the enzyme was originally isolated as a meta-cleavage enzyme for 2'-aminobiphenyl-2,3-diol involved in carbazole degradation, the enzyme has also shown high specificity for 2,3-dihydroxybiphenyl
MARYPVNRLIQELFKDPGLIERFQDDPSAVFEEYGLTPAERAALREGTFGALTSIGVHPILQMHYLMYTN
PEMAKHVSIKD
>gnl|CDD|153393 cd07923, Gallate_dioxygenase_C, The C-terminal domain of Gallate Dioxygenase, which catalyzes the oxidization and subsequent ring-opening of gallate. Gallate Dioxygenase catalyzes the oxidization and subsequent ring-opening of gallate, an intermediate in the degradation of the aromatic compound, syringate. The reaction product of gallate dioxygenase is 4-oxalomesaconate. The amino acid sequence of the N-terminal and C-terminal regions of gallate dioxygenase exhibits homology with the sequence of the PCA 4,5-dioxygenase B (catalytic) and A subunits, respectively. This model represents the C-terminal domain, which is similar to the A subunit of PCA 4,5-dioxygenase (or LigAB). The enzyme is estimated to be a homodimer according to the Escherichia coli enzyme. Since enzymes in this subfamily have fused A and B subunits, the dimer interface may resemble the tetramer interface of classical LigAB enzymes. This enzyme belongs to the class III extradiol dioxygenase family, composed of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon
RSVRAYRINRFLHRLIEPAHRERFLEDPEALFDEAGLTEEERTLIRNRDWIGMIRYGVIFFVLEKLAAVV
GVSNLHVYAAMRGESLEEFQKTRN
>gnl|CDD|153394 cd07924, PCA_45_Doxase_A, The A subunit of Protocatechuate 4,5-dioxygenase (LigAB) is the smaller, non-catalytic subunit. The A subunit is the non-catalytic subunit of Protocatechuate (PCA) 4,5-dioxygenase (LigAB), which is composed of A and B subunits that form a tetramer. PCA 4,5-dioxygenase catalyzes the oxidization and subsequent ring-opening of PCA (or 3,4-dihydroxybenzoic acid), which is an intermediate in the breakdown of lignin and other compounds. PCA 4,5-dioxygenase is one of the aromatic ring opening dioxygenases which play key roles in the degradation of aromatic compounds. As a member of the Class III extradiol dioxygenase family, LigAB uses a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon
DKPYDDIPGTYVFDAERARKGYHLNQFCMSLMKAENRERFKADERAYLDKWPMTEEQKQAVLARDYNRML
ALGGNIYYLAKIGATDGLSFQQAAGSMTGMSMEEYRQMMVDGGRSPEGNRS
>gnl|CDD|153395 cd07925, LigA_like_1, The A subunit of Uncharacterized proteins with similarity to Protocatechuate 4,5-dioxygenase (LigAB). The proteins of unknown function in this subfamily are similar to the A subunit of the Protocatechuate (PCA) 4,5-dioxygenase (LigAB). LigAB belongs to the class III extradiol dioxygenase family, composed of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. Dioxygenases play key roles in the degradation of aromatic compounds. PCA 4,5-dioxygenase catalyzes the oxidization and subsequent ring-opening of PCA (or 3,4-dihydroxybenzoic acid), which is an intermediate in the breakdown of lignin and other compounds
GTTLFDGEMARKGYALNKMCFSFNDAANREAFLADEEAYCEKFGLTPEQKQAVRNRDVLRMLEAGGNIYY
LAKLAGILGLNMQDIGGLQTGMSTEEFKAMLVAQGR
>gnl|CDD|143648 cd07927, RHD-n_NFAT_like, N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells (NFAT) proteins and similar proteins. Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes that are mainly involved in cell-cell interaction. Upon de-phosphorylation of the nuclear localization signal, NFAT enters the nucleus and acts as a transcription factor; its export from the nucleus is triggered by phosphorylation via export kinases. NFATs play important roles in mediating the immune response, and are found in T cells, B Cells, NK cells, mast cells, and monocytes. NFATs are also found in various non-hematopoietic cell types, where they play roles in development. This group also contains the N-terminal RHD sub-domain of the non-calcium regulated tonicity-responsive enhancer binding protein (TonEBP), also called NFAT5. Mammalian TonEBP regulates the expression of genes in response to tonicity. It plays a pivotal role in urinary concentrating mechanisms in kidney medulla, by triggering the accumulation of osmolytes that enable renal medullary cells to tolerate high levels of urea and salt
YELRIEVQPEPHHRARYETEGSRGAVKAPSTGGFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYQVHRI
TGKTTTPCKEKIIGNTKVLEIPLEPKNNMTATIDCAGILKLRNADIELRKGETDIKKKNTRARLVFRVHI
PEKDGRIVSLQTASNPIECSQ
>gnl|CDD|153077 cd07930, bacterial_phosphagen_kinase, Phosphagen (guanidino) kinases found in bacteria. Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, such as phosphocreatine (PCr) or phosphoarginine, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. This subfamily is specific to bacteria and lacks an N-terminal domain, which otherwise forms part of the substrate binding site. Most of the catalytic residues are found in the larger C-terminal domain, however, which appears conserved in these bacterial proteins. Their functions have not been characterized
SDIVISSRIRLARNLKGYPFPNKLSEEQAADVLEKVEKALSNIEDKDEFELLKLKDLDPLERQVLVEKHL
ISPELAENKEGGAVIVNEDETVSIMINEEDHLRIQCLLPGLQLEEAYERADKIDDLLEEKLDYAFDEKLG
YLTACPTNVGTGLRASVMLHLPALVLTGQINRILNALSQLGLAVRGLYGEGSEALGNIYQISNQVTLGLS
EEEIIENLESVVRQIIEQEREA
>gnl|CDD|153078 cd07931, eukaryotic_phosphagen_kinases, Phosphagen (guanidino) kinases mostly found in eukaryotes. Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK) or phosphoarginine in the case of arginine kinase, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CK exists in tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial and cytosolic) isoforms. They are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK and AK, the most studied members of this family are also other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK) and hypotaurocyamine kinase (HTK)
LESNKSLLAKYLTPEVYEKLKNRKTASGFTLADVIQSGVDNPDSGVGVYAGDEESYDVFAPLFDPVIEDY
HGGYKPEDKHTSDLDPEKPGLEDLDPRKKYIISTRIRVARNLDGFPLPPGMTKEQRRQIERLMVSALSSL
EGDLKGTYYSLTEMTEEQQQQLIDDHFLFKDGDRFLEAAGENRDWPDGRGIFHNSDKTFLVWVNEEDHLR
IISMQKGGDLKAVFTRLSRALTEIEKSLKEEFAHDPHLGYITSCPTNLGTGMRASVHVKLPNLIKDMDKL
KAIARKLGLQIRGIGGEHSESEGGVVDISNKRRLGFSEVQLVQDMYDGVKKLIEEEKK
>gnl|CDD|153079 cd07932, arginine_kinase_like, Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes. Eukaryotic arginine kinase-like phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphoarginine in the case of arginine kinase (AK), which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. Besides AK, one of the most studied members of this family, this model also represents a phosphagen kinase with different substrate specificity, hypotaurocyamine kinase (HTK)
KLEEELAKLQDAEDCKSLLKKYLTPEVLKKLKDKKTKLGGTLADCIQSGAENLDSGVGIYACDPEAYTVF
ADLFDPVIEDYHGGFKPEDKHPAPDFGDLKNLELGNLDPEGKYVISTRVRCGRSVEGYPFNPCLTKEQYI
EMEEKVKSALETLTGELAGTYYPLTGMDKETQQQLIDDHFLFKEGDRFLQAAGGYRFWPTGRGIFHNDDK
TFLVWVNEEDHLRIISMQKGGDLGAVYKRLVTALKELEKKLPFARDDRLGYLTFCPTNLGTTLRASVHIK
LPKLSKDPPRLKEICEKYNLQVRGTHGEHTESVGGVYDISNKRRLGLTEFEAVKEMQDGVLELIKLEKEL
>gnl|CDD|143649 cd07933, RHD-n_c-Rel, N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel. Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the c-Rel family of transcription factors, categorized as a class II member of the NF-kappa B family. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). c-Rel plays an important role in B cell proliferation and survival
PYVEIFEQPRQRGMRFRYKCEGRSAGSIPGERSTDNNRTYPSIQILNYTGKGKVRITLVTKNEPYKPHPH
DLVGKDCRDGYYEAEFGPERRVLAFQNLGIQCVRRREVKEAIMLRISRGINPFNVPEEQLLQIEEYDLNV
VRLCFQIFLPDEHGNYTTALPPIVSNPIYDNR
>gnl|CDD|143650 cd07934, RHD-n_NFkB2, N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2). Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B2 family of transcription factors, a class I member of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. NF-kappa B2 is commonly referred to as p100 or p52 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). NF-kappa B2 is involved in the alternative NF-kappa B signaling pathway which is activated by few agonists and plays an important role in secondary lymphoid organogenesis, maturation of B-cells, and adaptive humoral immunity. p100 may also act as an I-kappa B due to its C-terminal ankyrin repeats
PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAH
SLVGKHCNESGNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTGPYKLTEAEERELEQ
EAKELKKVMDLSIVRLKFTAYLRDSNGSYTLALKPVISDPIHDSK
>gnl|CDD|143651 cd07935, RHD-n_NFkB1, N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa B1). Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B1 family of transcription factors, a class I member of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. NF-kappa B1 is commonly referred to as p105 or p50 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). NF-kappa B1 is involved in the canonical NF-kappa B signaling pathway which is activated by many agonists and is essential in immune and inflammatory responses, as well as cell survival. p105 is involved in its own specific NF-kappa B signaling pathway which is also implicated in immune and inflammatory responses. p105 may also act as an I-kappa B due to its C-terminal ankyrin repeats. It is also involved in mitogen-activated protein kinase (MAPK) signaling as its degradation leads to the activation of TPL-2, a MAPK kinase kinase which activates ERK pathways
PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAH
SLVGKHCEDGICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAE
GGGDRQLTEREKEIIRQAAVQQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK
>gnl|CDD|153421 cd07936, SCAN, SCAN oligomerization domain. The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix
PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKP
ESGEEAATLAEDLLA
>gnl|CDD|163675 cd07937, DRE_TIM_PC_TC_5S, Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain. This family includes the carboxyltransferase domains of pyruvate carboxylase (PC) and the transcarboxylase (TC) 5S subunit. Transcarboxylase 5S is a cobalt-dependent metalloenzyme subunit of the biotin-dependent transcarboxylase multienzyme complex. Transcarboxylase 5S transfers carbon dioxide from the 1.3S biotin to pyruvate in the second of two carboxylation reactions catalyzed by TC. The first reaction involves the transfer of carbon dioxide from methylmalonyl-CoA to the 1.3S biotin, and is catalyzed by the 12S subunit. These two steps allow a carboxylate group to be transferred from oxaloacetate to propionyl-CoA to yield pyruvate and methylmalonyl-CoA. The catalytic domain of transcarboxylase 5S has a canonical TIM-barrel fold with a large C-terminal extension that forms a funnel leading to the active site. Transcarboxylase 5S forms a homodimer and there are six dimers per complex. In addition to the catalytic domain, transcarboxylase 5S has several other domains including a carbamoyl-phosphate synthase domain, a biotin carboxylase domain, a carboxyltransferase domain, and an ATP-grasp domain. Pyruvate carboxylase, like TC, is a biotin-dependent enzyme that catalyzes the carboxylation of pyruvate to produce oxaloacetate. In mammals, PC has critical roles in gluconeogenesis, lipogenesis, glyceroneogenesis, and insulin secretion. Inherited PC deficiencies are linked to serious diseases in humans such as lactic acidemia, hypoglycemia, psychomotor retardation, and death. PC is a single-chain enzyme and is active only in its homotetrameric form. PC has three domains, an N-terminal biotin carboxylase domain, a carboxyltransferase domain (this alignment model), and a C-terminal biotin-carboxyl carrier protein domain. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM"
ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAGFFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPN
TPLQMLLRGQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICY
TGSPVHTLEYYVKLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVGLPIHLHTHDTSGLAVATY
LAAAEAGVDIVDTAISPLSGGTSQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF
>gnl|CDD|163676 cd07938, DRE_TIM_HMGL, 3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain. 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM"
IVEVGPRDGLQNEKTFIPTEDKIELIDALSAAGLRRIEVTSFVSPKWVPQMADAEEVLAGLPRRPGVRYS
ALVPNLRGAERALAAGVDEVAVFVSASETFSQKNINCSIAESLERFEPVAELAKAAGLRVRGYVSTAFGC
PYEGEVPPERVAEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERFPDEKLALHFHDTRGQALAN
ILAALEAGVRRFDSSVGGLGGCPFAPGATGNVATEDLVYMLEGMGIETGIDLDKLLAAARWISE
>gnl|CDD|163677 cd07939, DRE_TIM_NifV, Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain. FrbC (NifV) of Streptomyces rubellomurinus catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate and CoA, a reaction similar to one catalyzed by homocitrate synthase. The gene encoding FrbC is one of several genes required for the biosynthesis of FR900098, a potent antimalarial antibiotic. This protein is also required for assembly of the nitrogenase MoFe complex but its exact role is unknown. This family also includes the NifV proteins of Heliobacterium chlorum and Gluconacetobacter diazotrophicus, which appear to be orthologous to FrbC. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM"
INDTTLRDGEQAPGVAFSREEKLAIARALDEAGVDEIEVGIPAMGEEEREAIRAIVALGLPARLIVWCRA
VKEDIEAALRCGVTAVHISIPVSDIHLAHKLGKDRAWVLDQLRRLVGRAKDRGLFVSVGAEDASRADPDF
LIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAATDLPLEFHAHNDLGLATANTLAAVRAGATH
VSVTVNGLGERAGNAALEEVVMALKHLYGRDTGIDTTRLPELSQLVARA
>gnl|CDD|163678 cd07940, DRE_TIM_IPMS, 2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain. 2-isopropylmalate synthase (IPMS) catalyzes an aldol-type condensation of acetyl-CoA and 2-oxoisovalerate yielding 2-isopropylmalate and CoA, the first committed step in leucine biosynthesis. This family includes the Arabidopsis thaliana IPMS1 and IPMS2 proteins, the Glycine max GmN56 protein, and the Brassica insularis BatIMS protein. This family also includes a group of archeal IPMS-like proteins represented by the Methanocaldococcus jannaschii AksA protein. AksA catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form trans-homoaconitate, one of 13 steps in the conversion of alpha-ketoglutarate and acetylCoA to alpha-ketosuberate, a precursor to coenzyme B and biotin. AksA also catalyzes the condensation of alpha-ketoadipate or alpha-ketopimelate with acetylCoA to form, respectively, the (R)-homocitrate homologs (R)-2-hydroxy-1,2,5-pentanetricarboxylic acid and (R)-2-hydroxy-1,2,6- hexanetricarboxylic acid. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM"
IFDTTLRDGEQTPGVSLTPEEKLEIARQLDELGVDVIEAGFPAASPGDFEAVKRIAREVLNAEICGLARA
VKKDIDAAAEALKPAKVDRIHTFIATSDIHLKYKLKKTREEVLERAVEAVEYAKSHGLDVEFSAEDATRT
DLDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVPNIKVPISVHCHNDLGLAVANSLAA
VEAGARQVECTINGIGERAGNAALEEVVMALKTRYDYYGVETGIDTEELYETSRLVSR
>gnl|CDD|163679 cd07941, DRE_TIM_LeuA3, Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel domain. Desulfobacterium autotrophicum LeuA3 is sequence-similar to alpha-isopropylmalate synthase (LeuA) but its exact function is unknown. Members of this family have an N-terminal TIM barrel domain that belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM"
IYDTTLRDGTQGEGISFSVEDKLRIARKLDELGVDYIEGGWPGSNPKDTEFFARAKKLKLKHAKLAAFGS
TRRAGVKAEEDPNLQALLEAGTPVVTIFGKSWDLHVTEALGTTLEENLAMIRDSVAYLKSHGREVIFDAE
HFFDGYKANPEYALATLKAAAEAGADWLVLCDTNGGTLPHEIAEIVKEVRERLPGVPLGIHAHNDSGLAV
ANSLAAVEAGATQVQGTINGYGERCGNANLCSIIPNLQLKMGYECLPEENLKKLTELSRFVSE
>gnl|CDD|163680 cd07942, DRE_TIM_LeuA, Mycobacterium tuberculosis LeuA3 and related proteins, N-terminal catalytic TIM barrel domain. Alpha-isopropylmalate synthase (LeuA), a key enzyme in leucine biosynthesis, catalyzes the first committed step in the pathway, converting acetyl-CoA and alpha-ketoisovalerate to alpha-isopropyl malate and CoA. Although the reaction catalyzed by LeuA is similar to that of the Arabidopsis thaliana IPMS1 protein, the two fall into phylogenetically distinct families within the same superfamily. LeuA has and N-terminal TIM barrel catalytic domain, a helical linker domain, and a C-terminal regulatory domain. LeuA forms a homodimer in which the linker domain of one monomer sits over the catalytic domain of the other, inserting residues into the active site that may be important for catalysis. Homologs of LeuA are found in bacteria as well as fungi. This family includes alpha-isopropylmalate synthases I (LEU4) and II (LEU9) from Saccharomyces cerevisiae. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM"
APIWCSVDLRDGNQALAEPMSVEQKLRFFKLLVKIGFKEIEVGFPSASQTDFDFVRELIEEDLIPDDVTI
QVLTQAREDLIERTFEALRGAKKAIVHLYNATSPLQRRVVFGKSKEEIIEIAVDGAKLVKELAAKYPETD
WRFEYSPESFSDTELDFALEVCEAVIDVWQPTPENKIILNLPATVEVATPNVYADQIEWFCRNLSRRESV
IISLHPHNDRGTGVAAAELALLAGADRVEGTLFGNGERTGNVDLVTLALNLYSQGVDPGLDFSDIDEIIR
VVEE
>gnl|CDD|163681 cd07943, DRE_TIM_HOA, 4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain. 4-hydroxy 2-ketovalerate aldolase (Also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. This family includes the Escherichia coli MhpE aldolase, the Pseudomonas DmpG aldolase, and the Burkholderia xenovorans BphI pyruvate aldolase. In Pseudomonas, the DmpG aldolase tightly associates with a dehydrogenase (DmpF) and is inactive without it. HOA has a canonical TIM-barrel fold with a C-terminal extension that forms a funnel leading to the active site. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM"
VYIHDVTLRDGMHAVRHQFTLEQVRAIARALDAAGVPLIEVGHGDGLGGSSLNYGFAAHTDEEYLEAAAE
ALKQAKLGVLLLPGIGTVDDLKMAADLGVDVVRVATHCTEADVSEQHIGAARKLGMDVVGFLMMSHMASP
EELAEQAKLMESYGADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAG
ATRIDGSLAGLGAGAGNTPLEVLVAVLERMGIETGIDLYKLMDAAEDLVRPLM
>gnl|CDD|163682 cd07944, DRE_TIM_HOA_like, 4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain. This family of bacterial enzymes is sequence-similar to 4-hydroxy-2-oxovalerate aldolase (HOA) but its exact function is unknown. This family includes the Bacteroides vulgatus Bvu_2661 protein and belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM"
ILDCTLRDGGYVNNWDFGDEFVKAIYRALAAAGIDYVEIGYRSSPEKEFKGKSAFCDDEFLRRLLGDSKG
NTKIAVMVDYGNDDIDLLEPASGSVVDMIRVAFHKHEFDEALPLIKAIKEKGYEVFFNLMAISGYSDEEL
LELLELVNEIKPDVFYIVDSFGSMYPEDIKRIISLLRSNLDKDIKLGFHAHNNLQLALANTLEAIELGVE
IIDATVYGMGRGAGNLPTELLLDYLNNKFGKKYNLEPVLELIDEYIAPLKKKYEWG
>gnl|CDD|163683 cd07945, DRE_TIM_CMS, Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic TIM barrel domain. Citramalate synthase (CMS) catalyzes the conversion of pyruvate and acetyl-CoA to (R)-citramalate in the first dedicated step of the citramalate pathway. Citramalate is only found in Leptospira interrogans and a few other microorganisms. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM"
MDTTLRDGEQTSGVSFSPSEKLNIAKILLQELKVDRIEVASARVSEGEFEAVQKIIDWAAEEGLLDRIEV
LGFVDGDKSVDWIKSAGAKVLNLLTKGSLKHCTEQLRKTPEEHFADIREVIEYAIKNGIEVNIYLEDWSN
GMRDSPDYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFHAHNDYDLAVANVL
AAVKAGIKGLHTTVNGLGERAGNAPLASVIAVLKDKLKVKTNIDEKRLNRASRLVETFSGKRIPANKPIV
>gnl|CDD|163684 cd07947, DRE_TIM_Re_CS, Clostridium kluyveri Re-citrate synthase and related proteins, catalytic TIM barrel domain. Re-citrate synthase (Re-CS) is a Clostridium kluyveri enzyme that converts acetyl-CoA and oxaloacetate to citrate. In most organisms, this reaction is catalyzed by Si-citrate synthase which is Si-face stereospecific with respect to C-2 of oxaloacetate, and phylogenetically unrelated to Re-citrate synthase. Re-citrate synthase is also found in a few other strictly anaerobic organisms. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM"
IWITDTTFRDGQQARPPYTVEQIVKIYDYLHELGGGSGVIRQTEFFLYTEKDREAVEACLDRGYKFPEVT
GWIRANKEDLKLVKEMGLKETGILMSVSDYHIFKKLKMTREEAMEKYLEIVEEALDHGIKPRCHLEDITR
ADIYGFVLPFVNKLMKLSKESGIPVKIRLCDTLGYGVPYPGASLPRSVPKIIYGLRKDCGVPSENLEWHG
HNDFYKAVANAVAAWLYGASWVNCTLLGIGERTGNCPLEAMVIEYAQLKGNFDGMNLEVITEIAEYFEK
>gnl|CDD|163685 cd07948, DRE_TIM_HCS, Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel domain. Homocitrate synthase (HCS) catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate, the first step in the lysine biosynthesis pathway. This family includes the Yarrowia lipolytica LYS1 protein as well as the Saccharomyces cerevisiae LYS20 and LYS21 proteins. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM"
FKIIDSTLREGEQFANAFFDTEDKIEIAKALDAFGVDYIELTSPAASPQSRADCEAIAKLGLKAKILTHI
RCHMDDARIAVETGVDGVDLVFGTSPFLREASHGKSITEIIESAVEVIEFVKSKGIEVRFSSEDSFRSDL
VDLLRVYRAVDKLGVNRVGIADTVGIATPRQVYELVRTLRGVVSCDIEFHGHNDTGCAIANAYAALEAGA
THIDTTVLGIGERNGITPLGGLIARMYTADPEYVVSKYKLELLPELERLVAD
>gnl|CDD|153386 cd07949, PCA_45_Doxase_B_like_1, The B subunit of unknown Class III extradiol dioxygenases with similarity to Protocatechuate 4,5-dioxygenase. This subfamily is composed of proteins of unknown function with similarity to the B subunit of Protocatechuate 4,5-dioxygenase (LigAB). LigAB belongs to the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. Dioxygenases play key roles in the degradation of aromatic compounds. LigAB-like enzymes are usually composed of two subunits, designated A and B, which form a tetramer composed of two copies of each subunit. This model represents the catalytic subunit, B
MAKIIGGITTSHVPAIGGAIAKGLQQTPYWKPFFDGFPPVHDWLEKAKPDVAVVFYNDHGLNFFLDKMPT
FAVGAAPSYRNADEGWGIPALAPFKGDPELSWHLIESLVEDEFDITTCQEMLVDHACTLPMQLFWPGAEW
PIKVVPVSINTVQHPLPSPKRCFKLGQAIGRAIESYPEDLRVVVLGTGGLSHQLDGERAGFINKDFDRYC
LDKMVDNPEWLTKYSIEELVELAGTQGVEFLMWIAMRGALGDEVREVHRNYHIPISNTAAGTLLLE
>gnl|CDD|153387 cd07950, Gallate_Doxase_N, The N-terminal domain of the Class III extradiol dioxygenase, Gallate Dioxygenase, which catalyzes the oxidization and subsequent ring-opening of gallate. Gallate Dioxygenase catalyzes the oxidization and subsequent ring-opening of gallate, an intermediate in the degradation of the aromatic compound, syringate. The reaction product of gallate dioxygenase is 4-oxalomesaconate. The amino acid sequence of the N-terminal and C-terminal regions of gallate dioxygenase exhibits homology with the sequence of PCA 4,5-dioxygenase B (catalytic) and A subunits, respectively. The enzyme is estimated to be a homodimer according to the Escherichia coli enzyme. LigAB-like enzymes are usually composed of two subunits, designated A and B, which form a tetramer composed of two copies of each subunit. In this subfamily, the subunits A and B are fused to make a single polypeptide chain. The dimer interface for this subfamily may resemble the tetramer interface of classical LigAB enzymes. Gallate Dioxygenase belongs to the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon
MAKIIGGIGSSHTPTIGFAYDKNKQNDPAWAPIFDGYEPVKQWLAEQKPDVLFMVYNDHVTSFFFDHYSA
FALGVGDSYEVADEGGGPRDLPPIRGHAALAQHIAESLVADEFDLTFFQDKPLDHGCFSPLSLLLPHEDG
WPVKVVPLQVGVLQFPLPTARRCYKLGQALRRAIESYPEDLKVAVVGTGGLSHQVHGERAGFNNTEWDME
FLDLIENDPESLAAMTHADYATLGGAEGAEVIMWLIMRGALSDRVRELHRNYYLPSMTGIATLVFEN
>gnl|CDD|153388 cd07951, ED_3B_N_AMMECR1, The N-terminal domain, an extradiol dioxygenase class III subunit B-like domain, of unknown proteins containing a C-terminal AMMECR1 domain. This subfamily is composed of uncharacterized proteins containing an N-terminal domain with similarity to the catalytic B subunit of class III extradiol dioxygenases and a C-terminal AMMECR1-like domain. This model represents the N-terminal domain. Class III extradiol dioxygenases use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon, however, proteins in this subfamily do not contain a potential metal binding site and may not exhibit class III extradiol dioxygenase-like activity. The AMMECR1 protein was proposed to be a regulatory factor that is potentially involved in the development of AMME contiguous gene deletion syndrome
LVPHPPLLVPEVGGGEEAEIAATRAACEAAARRLAAARPDTIVVVSPHAPVFRDAFAISTGGTLRGDFSR
FGAPEVSFGVDLDLELVEEIAGEADKEGLPVGALGERIPELDHGTLVPLYFLRKAGSDGKLVRIGLSGLS
PEELYAFGRALAAAAEELGRRVALIASGDLSHRLTEDAPGGYDPRGPEFDAAIAEALAKGDVDALLALDP
ELAEEAGECGRRSWQVLAGALDGASVKGEVLSYEGPFGVGYLVAVW
>gnl|CDD|153389 cd07952, ED_3B_like, Uncharacterized class III extradiol dioxygenases. This subfamily is composed of proteins of unknown function with similarity to the catalytic B subunit of class III extradiol dioxygenases. Class III extradiol dioxygenases use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. They play key roles in the degradation of aromatic compounds
FIAVIPHGDEIIDPLDEESRKLNEAIKEEGAKNDDPDVLVVITPHGIRLSGHVAVILTEYLEGTLRTNKV
LIRSKYPNDRELANEIYKSARADGIPVLGINFATSSGDNSDFPLDWGELIPLSFLKKRPIVLITPPRLLP
REELVEFGRALGKALEGYEKRVAVIISADHAHTHDPDGPYGYSPDAAEYDAAIVEAIENNDFEALLELDD
ELIEKAKPDSYWQLLILAGILESSPRKSKVLYYEVPTYFGMMVALF
>gnl|CDD|409289 cd07953, PUA, PUA RNA binding domain. The PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, and a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was also found in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in regulating the expression of other genes. It has been shown that the PUA domain acts as an RNA binding domain in at least some of the proteins involved in RNA metabolism
PVVVVDKGAEKAVLNGADLMAPGVVSADGDFKRGDLVRIVSEGGRPLAIGVAEMSSDEMKEELKGIAVRV
LHF
>gnl|CDD|271157 cd07954, AP_MHD_Cterm, C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD). This family corresponds to the C-terminal domain of heterotetrameric AP complexes medium mu subunits and its homologs existing in monomeric stonins, delta-subunit of the heteroheptameric coat protein I (delta-COPI), a protein encoded by a pro-death gene referred as MuD (also known as MUDENG, mu-2 related death-inducing gene), an endocytic adaptor syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related proteins. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. Stonins have been characterized as clathrin-dependent AP-2 mu chain related factors and may act as cargo-specific sorting adaptors in endocytosis. Coat protein complex I (COPI)-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. MuD is distantly related to the C-terminal domain of mu2 subunit of AP-2. It is able to induce cell death by itself and plays an important role in cell death in various tissues. Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress responses. It shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, FCHo1/2, which represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Another mammalian neuronal-specific protein SGIP1 does have a C-terminal MHD and has been classified into this family as well. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15
EVFLDVVEKVNLLISKDGSLLNSEVQGEIALKSFLSGMPEIRLGLNNPDVGIKLDDVSFHPCVRLKRFES
ERVISFIPPDGEFELMSYRTVEPWSILPITIFPVVSEEGSQLEVVITLKLSESLQLTAENVEVHIPLPSG
VTSLKSKPSDGQAKFDPEKNALVWRIKRIPVGGKEQSLSAHVELGSLAHECPEEAPPVSVSFEIPETTGS
GIQVRSLQVFDEKNPGHDPIKWVRYITHTGKYVAR
>gnl|CDD|153409 cd07955, Anticodon_Ia_Cys_like, Anticodon-binding domain of cysteinyl tRNA synthetases and domain found in MshC. This domain is found in cysteinyl tRNA synthetases (CysRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. CysRS catalyzes the transfer of cysteine to the 3'-end of its tRNA. The family also includes a domain of MshC, the rate-determining enzyme in the mycothiol biosynthetic pathway, which is specific to actinomycetes. The anticodon-binding site of CysRS lies C-terminal to this model's footprint and is not shared by MshC
DEVLADAEARLARWRSAVALPDGPDAEALVARLREALADDLDTPKALAALDAWAREALSRGGTDPDAPAL
VRTAVDALLGV
>gnl|CDD|153410 cd07956, Anticodon_Ia_Arg, Anticodon-binding domain of arginyl tRNA synthetases. This domain is found in arginyl tRNA synthetases (ArgRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. ArgRS catalyzes the transfer of arginine to the 3'-end of its tRNA
EEVGVGAVKYQDLSNKRIKDYTFDWERMLSFEGDTGPYLQYAHARLCSILRKAGETIEAEADADLSLLPE
PDERDLILLLAKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPVLGAEEELRNARLALVAAARQV
LANGLDLLGIEAPERM
>gnl|CDD|153411 cd07957, Anticodon_Ia_Met, Anticodon-binding domain of methionyl tRNA synthetases. This domain is found in methionyl tRNA synthetases (MetRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon (CAU). MetRS catalyzes the transfer of methionine to the 3'-end of its tRNA
INSELANNLGNLVNRTLNMASKYFGGVVPEFGGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIME
LARAANKYIDETAPWKLAKEEDPERLATVLYVLLELLRILAILLSPFMPETAEKILDQL
>gnl|CDD|153412 cd07958, Anticodon_Ia_Leu_BEm, Anticodon-binding domain of bacterial and eukaryotic mitochondrial leucyl tRNA synthetases. This domain is found in leucyl tRNA synthetases (LeuRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain. In contrast to other class Ia enzymes, the anticodon is not used as an identity element in LeuRS (with exceptions such as Saccharomyces cerevisiae and some other eukaryotes). No anticodon-binding site can be defined for this family, which includes bacterial and eukaryotic mitochondrial members, as well as LeuRS from the archaeal Halobacteria. LeuRS catalyzes the transfer of leucine to the 3'-end of its tRNA
WSDSGVEGAYRFLNRVWRLVTELAEALAAPAAAAELSEEDKELRRKLHKTIKKVTEDIERLRFNTAIAAL
MELVNALYKYKKKDAQHAAVLREALETLVLLLAPFAPHIAEELWEEL
>gnl|CDD|153413 cd07959, Anticodon_Ia_Leu_AEc, Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases. This domain is found in leucyl tRNA synthetases (LeuRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain. In contrast to other class Ia enzymes, the anticodon is not used as an identity element in LeuRS (with exceptions such as Saccharomyces cerevisiae and some other eukaryotes). No anticodon-binding site can be defined for this family, which includes archaeal and eukaryotic cytoplasmic members. LeuRS catalyzes the transfer of leucine to the 3'-end of its tRNA
FREEEANSAILRLERFYELAEELIETEGELEELTFIDRWLLSRLNRLIKETTEAYENMQFREALKEGLYE
LQNDLDWYRERGGAGMNKDLLRRFIEVWTRLLAPFAPHLAEEIWHEL
>gnl|CDD|153414 cd07960, Anticodon_Ia_Ile_BEm, Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases. This domain is found in isoleucyl tRNA synthetases (IleRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. This family includes bacterial and eukaryotic mitochondrial members. IleRS catalyzes the transfer of isoleucine to the 3'-end of its tRNA
ISDEILKQVAEAYRKIRNTFRFLLGNLNDFDPAKDAVPYEELLELDRYALHRLNELIKEVREAYENYEFH
KVYQALNNFCTVDLSAFYLDIIKDRLYCDAKDSLERRSAQTVLYHILDALLKLLAPILPFTAEEVWEHLP
GEKKEESVFLEDWPELPEEWKDEELEEKWEKLLALRDEVN
>gnl|CDD|153415 cd07961, Anticodon_Ia_Ile_ABEc, Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA synthetases. This domain is found in isoleucyl tRNA synthetases (IleRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. This family includes bacterial, archaeal, and eukaryotic cytoplasmic members. IleRS catalyzes the transfer of isoleucine to the 3'-end of its tRNA
FSEKGVREVVRKVLLPLWNAYRFFVTYANLDGFDPGKDDDAVASLNVLDRWILSRLNSLIKEVTEEMEAY
DLYTAVRALLEFIDELTNWYIRRNRKRFWGEEGDDDKLAAYATLYEVLLTLSRLMAPFTPFITEEIYQNL
RRELGDAPESVHLLDWPEVDESLIDEELEEAMELVREIVELGR
>gnl|CDD|153416 cd07962, Anticodon_Ia_Val, Anticodon-binding domain of valyl tRNA synthetases. This domain is found in valyl tRNA synthetases (ValRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. ValRS catalyzes the transfer of valine to the 3'-end of its tRNA
FDEKRVEGGRNFCNKLWNAARFVLMNLEDDDEPEEDPESLSLADRWILSRLNKTVEEVTEALENYRFSEA
ATALYEFFWNDFCDWYLELVKPRLYGEDEEEKKAARATLYYVLETILRLLHPFMPFITEELWQRL
>gnl|CDD|153417 cd07963, Anticodon_Ia_Cys, Anticodon-binding domain of cysteinyl tRNA synthetases. This domain is found in cysteinyl tRNA synthetases (CysRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. CysRS catalyzes the transfer of cysteine to the 3'-end of its tRNA
DDNLEDARAALERLYTALRGVPPTTVDIDWGEPFAERFIAAMDDDFNTPEALAVLFELAREINRLKKEDI
EKAAALAALLKALGGVLGLLQQDPEAFLQGGTGEGGLSVAEIEALIAQRNQARKAKDWAEADRIRDELAA
QGIILEDSPEGTTWRR
>gnl|CDD|176481 cd07964, RBP-H, Head domain of virus receptor-binding proteins (RBP). Virus receptor-binding proteins (RBPs) are found in lactococcal bacteriophages, as well as in adenoviruses and reoviruses, which invade mammalian cells. Lactococcus lactis is widely used in dairy fermentations and infection of L. lactis by phages greatly impairs the fermentation process. Adenovirus typically infects respiratory tracts with symptoms ranging from the common cold to pneumonia. Onset of viral infections begin with the recognition of host cells through the receptor-binding protein complex located at the distal part of the virion. The RBP has three domains: the N- terminal shoulders domain, the interlaced neck domain, and the C-terminal head domain. Phages recognize their host through an interaction between the RBP head (RBP-H) domain and saccharidic receptors at the host cell surface. Adenovirus recognizes the membrane cofactor protein, CD46, as a cellular receptor
TKTLSLGVGNGIILTLRKKGTLVEVRGYGILVSINAGVTLVGFGSDITAGFTPANQFSLVGHFASSDTSF
HIDIEPPGTITWWGPNNTSTGGTISGTLSYPID
>gnl|CDD|153436 cd07967, OBF_DNA_ligase_III, The Oligonucleotide/oligosaccharide binding (OB)-fold domain of ATP-dependent DNA ligase III is a DNA-binding module that is part of the catalytic core unit. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent ligases are present in many organisms such as viruses, bacteriohages, eukarya, archaea and bacteria. There are three classes of ATP-dependent DNA ligases in eukaryotic cells (I, III and IV). DNA ligase III is not found in lower eukaryotes and is present both in the nucleus and mitochondria. It has several isoforms; two splice forms, III-alpha and III-beta, differ in their carboxy-terminal sequences. DNA ligase III-beta is believed to play a role in homologous recombination during meiotic prophase. DNA ligase III-alpha interacts with X-ray Cross Complementing factor 1 (XRCC1) and functions in single nucleotide Base Excision Repair (BER). The mitochondrial form of DNA ligase III originates from the nucleolus and is involved in the mitochondrial DNA repair pathway. This isoform is expressed by a second start site on the DNA ligase III gene. DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains. The adenylation and C-terminal oligouncleotide/oligosaccharide binding (OB)-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core unit contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases. The OB-fold domain contacts the nicked DNA substrate and is required for the ATP-dependent DNA ligase nucleotidylation step. The RxDK motif (motif VI), which is essential for ATP hydrolysis, is located in the OB-fold domain
MADTADLVVLGAYYGTGSKGGMMSVFLMGCYDPNSKKWCTVTKCGNGHDDATLARLQKELKMVKISKDPS
KVPSWLKCNKSLVPDFIVKDPKKAPVWEITGAEFSKSEAHTADGISIRFPRVTRIRDDKDWKTATSLPE
>gnl|CDD|153437 cd07968, OBF_DNA_ligase_IV, The Oligonucleotide/oligosaccharide binding (OB)-fold domain of ATP-dependent DNA ligase IV is a DNA-binding module that is part of the catalytic core unit. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent ligases are present in many organisms such as viruses, bacteriohages, eukarya, archaea and bacteria. There are three classes of ATP-dependent DNA ligases in eukaryotic cells (I, III and IV). DNA ligase IV is required for DNA non-homologous end joining pathways, including recombination of the V(D)J immunoglobulin gene segments in cells of the mammalian immune system. DNA ligase IV is stabilized by forming a complex with XRCC4, a nuclear phosphoprotein, which is phosphorylated by DNA-dependent protein kinase. DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains. The adenylation and C-terminal oligouncleotide/oligosaccharide binding (OB)-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core unit contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases. The OB-fold domain contacts the nicked DNA substrate and is required for the ATP-dependent DNA ligase nucleotidylation step. The RxDK motif (motif VI), which is essential for ATP hydrolysis, is located in the OB-fold domain
GEDLDLLIIGGYYGEGRRGGKVSSFLCGVAEDDDPESDKPSVFYSFCKVGSGFSDEELDEIRRKLKPHWK
PFDKKAPPSSLLKFGKEKPDVWIEPKDSVVLEVKAAEIVPSDSYKTGYTLRFPRCEKIRYDKDWHDCLTL
>gnl|CDD|153438 cd07969, OBF_DNA_ligase_I, The Oligonucleotide/oligosaccharide binding (OB)-fold domain of ATP-dependent DNA ligase I is a DNA-binding module that is part of the catalytic core unit. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent ligases are present in many organisms such as viruses, bacteriohages, eukarya, archaea and bacteria. There are three classes of ATP-dependent DNA ligases in eukaryotic cells (I, III and IV). This group is composed of eukaryotic DNA ligase I, Sulfolobus solfataricus DNA ligase and similar proteins. DNA ligase I is required for the ligation of Okazaki fragments during lagging-strand DNA synthesis and for base excision repair (BER). ATP dependent DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains including a DNA-binding domain, an adenylation (nucleotidyltransferase (NTase)) domain, and an oligonucleotide/oligosaccharide binding (OB)-fold domain. The adenylation and C-terminal OB-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core unit contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases. The OB-fold domain contacts the nicked DNA substrate and is required for the ATP-dependent DNA ligase nucleotidylation step. The RxDK motif (motif VI), which is essential for ATP hydrolysis, is located in the OB-fold domain
GDTLDLVPIGAYYGKGKRTGVYGAFLLACYDPETEEFQTVCKIGTGFSDEFLEELYESLKEHVIPKKPYR
VDSSLEPDVWFEPKEVWEVKAADLTLSPVHTAAIGLVDEEKGISLRFPRFIRVRDDKKPEDATTSEQIAE
MYKK
>gnl|CDD|153439 cd07970, OBF_DNA_ligase_LigC, The Oligonucleotide/oligosaccharide binding (OB)-fold domain of ATP-dependent DNA ligase LigC is a DNA-binding module that is part of the catalytic core unit. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent ligases are present in many organisms such as viruses, bacteriohages, eukarya, archaea and bacteria. Bacterial DNA ligases are divided into two broad classes: NAD-dependent and ATP-dependent. All bacterial species have a NAD-dependent DNA ligase (LigA). Some bacterial genomes contain multiple genes for DNA ligases that are predicted to use ATP as their cofactor, including Mycobacterium tuberculosis LigB, LigC, and LigD. This group is composed of Mycobacterium tuberculosis LigC and similar bacterial proteins. ATP dependent DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains including a DNA-binding domain, an adenylation (nucleotidyltransferase (NTase)) domain, and an oligonucleotide/oligosaccharide binding (OB)-fold domain. The adenylation and C-terminal OB-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core unit contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases. The OB-fold domain contacts the nicked DNA substrate and is required for the ATP-dependent DNA ligase nucleotidylation step. The RxDK motif (motif VI), which is essential for ATP hydrolysis, is located in the OB-fold domain
RTADCVVGGVRGHKDRPGSLLLGLYDDGGRLRHVGRTSPLAAAERRELAELLEPARAGHPWTGRAPGFPS
RWGTRKSLEWVPVRPELVVEVSADTAEGGGRFRHPLRFLRWRPDKSPEDCTL
>gnl|CDD|153440 cd07971, OBF_DNA_ligase_LigD, The Oligonucleotide/oligosaccharide binding (OB)-fold domain of ATP-dependent DNA ligase LigD is a DNA-binding module that is part of the catalytic core unit. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent ligases are present in many organisms such as viruses, bacteriohages, eukarya, archaea and bacteria. Bacterial DNA ligases are divided into two broad classes: NAD-dependent and ATP-dependent. All bacterial species have a NAD-dependent DNA ligase (LigA). Some bacterial genomes contain multiple genes for DNA ligases that are predicted to use ATP as their cofactor, including Mycobacterium tuberculosis LigB, LigC, and LigD. This group is composed of Mycobacterium tuberculosis LigD and similar bacterial proteins. LigD, or DNA ligase D, catalyzes the end-healing and end-sealing steps during nonhomologous end joining. ATP dependent DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains including a DNA-binding domain, an adenylation (nucleotidyltransferase (NTase)) domain, and an oligonucleotide/oligosaccharide binding (OB)-fold domain. The adenylation and C-terminal OB-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core unit contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases. The OB-fold domain contacts the nicked DNA substrate and is required for the ATP-dependent DNA ligase nucleotidylation step. The RxDK motif (motif VI), which is essential for ATP hydrolysis, is located in the OB-fold domain
RRQEFVIGGYTPPKGSRGGFGSLLLGVYDGGRLVYVGRVGTGFSAATLRELRERLAPLERKTSPFADPPP
ADARGAVWVKPELVAEVEFAEWTPDGRLRHPVFKGLREDKPAAEV
>gnl|CDD|153441 cd07972, OBF_DNA_ligase_Arch_LigB, The Oligonucleotide/oligosaccharide binding (OB)-fold domain of archaeal and bacterial ATP-dependent DNA ligases is a DNA-binding module that is part of the catalytic core unit. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent ligases are present in many organisms such as viruses, bacteriohages, eukarya, archaea and bacteria. Bacterial DNA ligases are divided into two broad classes: NAD-dependent and ATP-dependent. All bacterial species have a NAD-dependent DNA ligase (LigA). Some bacterial genomes contain multiple genes for DNA ligases that are predicted to use ATP as their cofactor, including Mycobacterium tuberculosis LigB, LigC, and LigD. This group is composed of Pyrococcus furiosus DNA ligase, Mycobacterium tuberculosis LigB, and similar archaeal and bacterial proteins. ATP dependent DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains including a DNA-binding domain, an adenylation (nucleotidyltransferase (NTase)) domain, and an oligonucleotide/oligosaccharide binding (OB)-fold domain. The adenylation and C-terminal OB-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core unit contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases. The OB-fold domain contacts the nicked DNA substrate and is required for the ATP-dependent DNA ligase nucleotidylation step. The RxDK motif (motif VI), which is essential for ATP hydrolysis, is located in the OB-fold domain
ETLDLVVIGAEWGEGRRAGLLGSYTLAVRDEETGELVPVGKVATGLTDEELEELTERLRELIIEKFGPVV
SVKPELVFEVAFEEIQRSPRYKSGYALRFPRIVRIRDDKDPDEADTLERVEA
>gnl|CDD|153422 cd07973, Spt4, Transcription elongation factor Spt4. Spt4 is a transcription elongation factor. Three transcription-elongation factors Spt4, Spt5, and Spt6, are conserved among eukaryotes and are essential for transcription via the modulation of chromatin structure. It is known that Spt4, Spt5, and Spt6 are general transcription-elongation factors, controlling transcription both positively and negatively in important regulatory and developmental roles. Spt4 functions entirely in the context of the Spt4-Spt5 heterodimer and it has been found only as a complex to Spt5 in Yeast and Human. Spt4 is a small protein that has zinc finger at the N-terminus. Spt5 is a large protein that has several interesting structural features of an acidic N-terminus, a single NGN domain, five or six KOW domains, and a set of simple C-termianl repeats. Spt4 binds to Spt5 NGN domain. Unlike Spt5, Spt4 is not essential for viability in yeast, however Spt4 is critical for normal function of the Spt4-Spt5 complex. Spt4 homolog is not found in bacteria
RGLRACLLCSLIKTEDQFERDGCPNCEGYLDMKGNHERVYDCTSPNFEGIIALMDPEKSWVARWQRIDKF
VPGIYAISVSGRLPEDIVEELESRGIIY
>gnl|CDD|199899 cd07976, TFIIA_alpha_beta_like, Precursor of TFIIA alpha and beta subunits and similar proteins. Transcription factor II A (TFIIA) is one of the general transcription factors for RNA polymerase II. TFIIA increases the affinity of TATA-binding protein (TBP) for DNA in order to assemble the initiation complex. TFIIA also functions as an activator during development and differentiation, and is involved in transcription from TATA-less promoters. TFIIA is composed of more than one subunit in various organisms. Mammalian TFIIA large subunits (TFIIA alpha and beta) and the smaller subunit (TFIIA gamma) form a heterotrimer. TFIIA alpha and beta are encoded by a single gene (TFIIA_alpha_beta), its protein product is post-translationally processed and cleaved. TOA1 and TOA2 are the two subunits of Yeast TFIIA which correspond to Mammalian TFIIA_alpha_beta and TFIIA gamma, respectively. TOA1 and TOA2 form a heterodimeric protein complex. TFIIA_alpha_beta alone is sufficient for transcription in early embryogenesis, but the cleaved forms, TFIIA alpha and TFIIA beta, represent the vast majority of TFIIA in most differentiated cells. The exact functional differences between cleaved and uncleaved forms are not yet clear. This model also contains paralogs of the canonical TFIIA_alpha_beta, such as the human ALF, which may be involved in gametogenesis and early embryogenesis (and is also subject to proteolytic cleavage)
VSKVYESVIEDVINNVREDFEDEGVDESVLQELKQLWEEKLSQSGAASFPWDPKPETENIVLCQYDKVTR
VKNKWKCTLKDGIMTLNGKDYVFQKATGEFEW
>gnl|CDD|153423 cd07977, TFIIE_beta_winged_helix, TFIIE_beta_winged_helix domain, located at the central core region of TFIIE beta, with double-stranded DNA binding activity. Transcription Factor IIE (TFIIE) beta winged-helix (or forkhead) domain is located at the central core region of TFIIE beta. The winged-helix is a form of helix-turn-helix (HTH) domain which typically binds DNA with the 3rd helix. The winged-helix domain is distinguished by the presence of a C-terminal beta-strand hairpin unit (the wing) that packs against the cleft of the tri-helical core. Although most winged-helix domains are multi-member families, TFIIE beta winged-helix domain is typically found as a single orthologous group. TFIIE is one of the six eukaryotic general transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF and TFIIH) that are required for transcription initiation of protein-coding genes. TFIIE is a heterotetramer consisting of two copies each of alpha and beta subunits. TFIIE beta contains several functional domains, an N-terminal serine-rich region, a central core domain exhibiting a winged-helix structure capable of binding double-stranded DNA, a leucine repeat, a sigma3 region, and a C-terminal domain containing two basic regions. The assembly of transcription preinitiation complex (PIC) includes the general transcription factors and RNA polymerase II (pol II) initiated by the binding of the TBP subunit of TFIID to the TATA box, followed by either the sequential assembly of other general transcription factors and pol II or a preassembled pol II holoenzyme pathway. TFIIE interacts directly with TFIIF, TFIIB, pol II, and promoter DNA. TFIIE recruits TFIIH and regulates its activities. TFIIE and TFIIH are also important for the transition from initiation to elongation
TGSGTHVFTQLAKIVDYMKKRHQHPLTLDEILDYLSLLDIGPKLKEWLKSEALVNNPKIDPKDGTFSFKP
KYNIR
>gnl|CDD|467023 cd07978, HFD_TAF13, histone-fold domain found in transcription initiation factor TFIID subunit 13 (TAF13) and similar proteins. TAF13, also called TATA Binding Protein (TBP) associated factor 13, transcription initiation factor TFIID 18 kDa subunit, TAF(II)18, TAFII-18, or TAFII18, is a component of the DNA-binding general RNA polymerase II transcription factor IID (TFIID) complex that is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TFIID is one of the general transcription factors required for accurate and regulated initiation by RNA polymerase II. It plays a central role in mediating promoter responses to various activators and repressors. TAF13 interacts with TBP, and more strongly with TAF10 and TAF11
LFTKEIRQMMYGFGDVRNPLPETVDLLEEIVIEYITDLLHKAMEVAKLRGSKKISVEDILFLLRKDPKKL
ARVKELL
>gnl|CDD|467024 cd07979, HFD_TAF9, histone-fold domain found in transcription initiation factor TFIID subunit 9 (TAF9) and similar proteins. The family includes TAF9 (also called TATA Binding Protein (TBP) associated factor 9, RNA polymerase II TBP-associated factor subunit G, STAF31/32, transcription initiation factor TFIID 31 kDa subunit, TAFII-31, TAFII31, transcription initiation factor TFIID 32 kDa subunit, TAFII-32, or TAFII32) and TAF9-like (also called transcription initiation factor TFIID subunit 9B, neuronal cell death-related protein 7, DN-7, or transcription-associated factor TAFII31L), which are essential for cell viability. They are involved in transcriptional activation as well as the repression of distinct but overlapping sets of genes. They may have roles in gene regulation associated with apoptosis. Both TAF9 and TAF9-like are TAFs that are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription. TAF9 interacts directly with different transcription factors such as p53, herpes simplex virus activator vp16, and the basal transcription factor TFIIB
PRDAQVIRAILKSMGVTDYEPRVVNQLLEFAYRYTTEVLQDAKVYAEHAGRSQIDEEDVRLAIQSRADHS
FTQPPPRELLLELAAEKNSIPLPPI
>gnl|CDD|259828 cd07980, TFIIF_beta, Transcription initiation factor IIF, beta subunit. The TFIIF-beta subunit, also called RNA Polymerase II-associating Protein 30 (RAP30), forms a heteromeric complex of RAP30/74 (TFIIF, beta/gamma) that is involved in both initiation and elongation of RNA chains by RNA polymerase II. Accurate transcription in vivo requires at least six general transcription initiation factors, in addition to RNA polymerase II. TFIIF-beta binds directly to RNA polymerase II and helps bring polymerase into a pre-initiation complex
DLDLDTSNADRSVWLVKVPKFLSERWSKLDDDGIELGTLRVYKDPPSGKPRVSLTLPENLPENANIPKEY
ELDMTNESVQNTYVFSEKDLPGFKARSQPYYRKSIPKKTALEGRVVHECDCRP
>gnl|CDD|467025 cd07981, HFD_TAF12, histone-fold domain found in transcription initiation factor TFIID subunit 12 (TAF12) and similar proteins. TAF12, also called TATA Binding Protein (TBP) associated factor 12, transcription initiation factor TFIID 20/15 kDa subunits, TAFII-20/TAFII-15, or TAFII20/TAFII15, is a TBP-associated factor (TAF). TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex, and TBP-free TAFII complex (TFTC). TIIFD is multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. TFIID and PCAF are composed of TATA binding protein (TBP) and several TAFs. TBP is not part of TFTC. TAFs are essential for mediating regulation of RNA polymerase transcription. TAF12 interacts with TAF4 and makes a novel histone-like heterodimer that binds DNA and has a core promoter function of a subset of genes. It is important for RAS-induced transformation properties of human colorectal cancer cells; its levels are increased in the cells harboring the RAS mutation. Also, TAF12 interacts with activating transcription factor 7 (ATF7) and contributes to the hypersensitivity of osteoclast (OCL) precursors to 1,25-dihydroxyvitamin D2 (1,25-(OH)2D3; also known as calcitriol) in Paget's disease (PD), a disorder of the bone remodeling process, in which the body absorbs old bone and forms abnormal new bone
NPLLSKRKLQELVREVDPNERLDPDVEELLLQLADDFVDDVVTFACKLAKHRGSDTLEVKDVQLHLERNW
NIRV
>gnl|CDD|467026 cd07982, HFD_TAF10, histone-fold domain found in transcription initiation factor TFIID subunit 10 (TAF10) and similar proteins. TAF10, also called TATA Binding Protein (TBP) associated factor 10, STAF28, transcription initiation factor TFIID 30 kDa subunit, TAF(II)30, TAFII-30, or TAFII30, is a TBP-associated factor (TAF). TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex, and TBP-free TAFII complex (TFTC). TIIFD is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. TFIID and PCAF are composed of TATA binding protein (TBP) and several TAFs. TBP is not part of TFTC. TAF10 regulates genes that are important for cell cycle progression and cell morphology. A lack of TAF10 leads to cell cycle arrest and cell death by apoptosis in mice
KELEEFLEQLEDYTPTIPDEVTQYYLERAGFQTSDPRVVRLISLAAQKFISDIANDALQYCKMRQSAQKK
KGKKGKDKKLVLTMEDLAAALKEYGINV
>gnl|CDD|153245 cd07983, LPLAT_DUF374-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: DUF374. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are the uncharacterized DUF374 phospholipid/glycerol acyltransferases and similar proteins
LRLLYLTLRWRVIGDESADALIAQGEPVILAFWHGRLLLMPYLFRRRKRIAALISRSKDGEIIARVLERL
GIRVVRGSSSRGGAAALREMLRALKDGYNIAITPDGPRGPRYKVKPGVILLARKSGAPIVPVAIAASRAW
RLKSWDRFIIPKPFSRVVIVFGEPIHVPPDADEEELEEYRLELEAALNA
>gnl|CDD|153246 cd07984, LPLAT_LABLAT-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lipid A biosynthesis lauroyl/myristoyl (LABLAT, HtrB) acyltransferases and similar proteins
LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLGYPVTVVYRPLKNPLLDRLITRGRERFG
ARLIPRGGGLRELIRALKKGEIVGILPDQDPGRKGGVFVPFFGRPAATPTGPARLALKTGAPVVPAFAYR
LPGGGYRIEFEPPLENPPSEDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK
>gnl|CDD|153247 cd07985, LPLAT_GPAT, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT. Lysophospholipid acyltransferase (LPLAT) superfamily member: glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB). LPLATs are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. This subgroup includes glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB)
GNSYIGNLSRFDRIEEQLAQGHNVVLLANHQTEADPAVISLLLEKTHPYLAENMIYVAGDRVVSDPLCKP
FSMGRNLLCVHSKKHIDDPPELKEEKMKANLATLKEMQQLLNEGGQLIWVAPSGGRDRPDANGEWYPDPF
DPSAVEMMRLLAQKSRVPTHLYPMALLTYDIMPPPKQVEKEIGEKRAVAFTGVGLAVGEEIDFSAIAATH
KDPEEVREAFSKAAFDSVKRLYNVL
>gnl|CDD|153248 cd07986, LPLAT_ACT14924-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ACT14924. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized phospholipid/glycerol acyltransferases such as the Pectobacterium carotovorum subsp. carotovorum PC1 locus ACT14924 putative acyltransferase, and similar proteins
LDALNVQLEVDVSGLENIPKDGPVVIVANHPFGILDGLILADLLGSVRPDVRILANQLLSKIPELRDLFI
PVDPLEGRAALAKNRESLREALRHLKNGGALIIFPAGRVSTASPPFGRVSDRPWNPFVARLARKAKAPVV
PVYFSGRNSRLFYLAGLIHPTLRTLLLPRELLNKRGKTIRIRVGRPIPPEELARFEDAEELADFLRLHTY
>gnl|CDD|153249 cd07987, LPLAT_MGAT-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this suubgroup are such LPLATs as 2-acylglycerol O-acyltransferase (MGAT), and similar proteins
HRKYFRVYEVRGLENIPDEGPALLVHPHGGLPIDGALLAAAFLLLFPGRLPRALADHFLFPLPGLRDLLR
RLGAVPGSRENCVRLLREGELVLIFPGGAREALKSKREEYYLLWKKRKGFARLALRAGAPIVPVFTFGEE
ELFRVLGDPDGPVGKRLFRLLPLPRRLPLYPVFGEPIVVPRPPIPDPPDEDVEELHQKYIAALRELIEKH
KK
>gnl|CDD|153250 cd07988, LPLAT_ABO13168-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ABO13168. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized phospholipid/glycerol acyltransferases such as the Acinetobacter baumannii ATCC 17978 locus ABO13168 putative acyltransferase, and similar proteins
ARLLLRLSGWRIEGEPPNKPKFVVIGAPHTSNWDFVLGLLAAFALGLKISFLGKHSLFKPPLGPFMRWLG
GIPVDRSRAGGLVEQVVEEFRRREEFVLAIAPEGTRSKVDKWKTGFYHIARGAGVPILLVYLDYKRKTVG
IGPLFEPSGDIEADLAAIRAFYR
>gnl|CDD|153251 cd07989, LPLAT_AGPAT-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins
LRLLLRLLGVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALPRPIRFVAKKELFKIPFLGWLLRLL
GAIPIDRGNGRSAREALREAIEALKEGESVVIFPEGTRSRDGELLPFKSGAFRLAKEAGVPIVPVAISGT
WGSLPKGKKLPRPGRVTVRIGEPIPPEGLELAEEDRKELREKVR
>gnl|CDD|153252 cd07990, LPLAT_LCLAT1-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as Lysocardiolipin acyltransferase 1 (LCLAT1) or 1-acyl-sn-glycerol-3-phosphate acyltransferase and similar proteins
VFLFEWLSGVKVVVYGDEPKLPKERALIISNHRSEVDWLVLWMLADRFGRLGRLKIVLKDSLKYPPLGGW
GWQLGEFIFLKRKWEKDEKTIKRQLKRLKDSPEPFWLLIFPEGTRFTEEKKERSQEFAEKNGLPPLKHVL
LPRTKGFVAILETLRDAVDAVYDVTIAYPDGKPPSEQRLLLGGKPREVHVHVR
>gnl|CDD|153253 cd07991, LPLAT_LPCAT1-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lysophosphatidylcholine acyltransferase 1 (LPCAT-1), glycerol-3-phosphate acyltransferase 3 (GPAT3), and similar sequences
ARVLLFAFGFYVIKVHGKPDPPEAPRIIVANHTSFIDPLILFSDLFPSIVAKKELGKLPFIGTILRALGC
IFVDRSEPKDRKKVVEEIKERATDPNWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFV
DAFWNSSGYSSLMYLFRLLTQPANVLEVEFLPVYTPSEEGEDPKEFANRVRLIMANKLGLPATDWTGEDK
R
>gnl|CDD|153254 cd07992, LPLAT_AAK14816-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown AAK14816-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized glycerol-3-phosphate acyltransferases such as the Plasmodium falciparum locus AAK14816 putative acyltransferase, and similar proteins
VRLLSRVILRIYFRRITVVGRENVPKDGPVIFLGNHPNALIDPLLLAATLRRPVRFLAKADLFKNPLIGW
LLESFGAIPVYRPKDLARGGIGKISNAAVFDAVGEALKAGGAIGIFPEGGSHDRPRLLPLKAGAARMALE
ALEAGQKDVKIVPVGLNYEDKSRFRSRVLVEFGKPISVSAFEEAEASRDVEKKLINQLEAELE
>gnl|CDD|153255 cd07993, LPLAT_DHAPAT-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and similar proteins
FDGVQVNEGQLERLRKAAQEGHPVVLLPTHRSYLDFLLLSFILFSLGLPLPHIAAGENLNIPILGTLLRR
LGAFFIRRSFGKDPLYRAVLQEYVQELLKNGQPLEFFIEGTRSRTGKLLPPKLGLLSVVVEAYLKGSVPD
VLIVPVSISYDRVLEEELYAEELLGPPKPKESLSGLLGASKILRENFGRIRVDFGEPISLREYLG
>gnl|CDD|153424 cd07994, WGR, WGR domain. The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs) as well as the putative Escherichia coli molybdate metabolism regulator and related bacterial proteins, a small family of bacterial DNA ligases, and various other bacterial proteins of unknown function. It has been called WGR after the most conserved central motif of the domain. The domain occurs in single-domain proteins and in a variety of domain architectures, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain
KATLGFQDIGSNKYYKLQLLEDDKENRYWVFRSYGRVGTVIGSTKLEQMPSKEEAEEHFMKLYEEKTGKG
YYP
>gnl|CDD|153431 cd07995, TPK, Thiamine pyrophosphokinase. Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin pyrophosphokinase) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamine) to form the coenzyme thiamine pyrophosphate (TPP). TPP is required for central metabolic functions, and thiamine deficiency is associated with potentially fatal human diseases. The structure of thiamine pyrophosphokinase suggests that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis
ALILLGGPLPDSPLLLKLWKKADLIIAADGGANHLLDLGIVPDLIIGDFDSISPEVLEYYKSKGVEIIHF
PDEKDFTDFEKALKLALERGADEIVILGATGGRLDHTLANLNLLLKYAKDGIKIVLIDEQNEIFLLLPGS
HTLELEEEGKYVSLIPLGEVTGLTLKGLKYPLDNATLSFGSSLGTSNEFTGEKATVSVESGLLLVILS
>gnl|CDD|153425 cd07996, WGR_MMR_like, WGR domain of molybdate metabolism regulator and related proteins. The WGR domain is found in the putative Escherichia coli molybdate metabolism regulator and related bacterial proteins, as well as in various other bacterial proteins of unknown function. It has been called WGR after the most conserved central motif of the domain. The domain appears to occur in single-domain proteins and in a variety of domain architectures, together with ATP-dependent DNA ligase domains, WD40 repeats, leucine-rich repeats, and other domains. It has been proposed to function as a nucleic acid binding domain
MTRLERIDPERNSARFYEIELEGDLFGEWSLVRRWGRIGTKGQSRTKTFDSEEEALKAAEKLIREKLKRG
YREA
>gnl|CDD|153426 cd07997, WGR_PARP, WGR domain of poly(ADP-ribose) polymerases. The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins and histones. Higher eukaryotes contain several PARPs and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. Poly-ADP-ribosylation was thought to be a reversible post-translational covalent modification that serves as a regulatory mechanism for protein substrates. However, it is now known that it plays important roles in many cellular processes including maintenance of genomic stability, transcriptional regulation, energy metabolism, cell death and survival, among others
HVYGDIATVYDATLNQTDISNNNNKFYKIQILESKGPNTYALFTRWGRVGERGQSQLTPFGSLESAIKEF
EKKFKDKTGNEWENRPLFKKQPGKYALVELDY
>gnl|CDD|153427 cd07998, WGR_DNA_ligase, WGR domain of bacterial DNA ligases. The WGR domain is found in a small family of predicted bacterial DNA ligases. It has been called WGR after the most conserved central motif of the domain. The domain typically occurs in together with an ATP-dependent DNA ligase domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain
KSTSLYFQEGNSDKVYEVDLFEVSDDGYVVNFRYGRRGSALREGTKTVAPVTLEAAEKIFDKLVKSKTNK
GYREGEG
>gnl|CDD|153432 cd07999, GH7_CBH_EG, Glycosyl hydrolase family 7. Glycosyl hydrolase family 7 contains eukaryotic endoglucanases (EGs) and cellobiohydrolases (CBHs) that hydrolyze glycosidic bonds using a double-displacement mechanism. This leads to a net retention of the conformation at the anomeric carbon. Both enzymes work synergistically in the degradation of cellulose,which is the main component of plant cell wall, and is composed of beta-1,4 linked glycosyl units. EG cleaves the beta-1,4 linkages of cellulose and CBH cleaves off cellobiose disaccharide units from the reducing end of the chain. In general, the O-glycosyl hydrolases are a widespread group of enzymes that hydrolyze the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycoside hydrolase family 7
PENHPKLTTQQCTKSGGCTTQTTSVVLDANWRWVHDTNGYTCCYGGNWWNATLCPDEATCAKNCALEGAD
YAGTYGVTTSGNSLTLNFVTPDGYKNVGSRVYLLADDSKYQMFKLLGQEFTFDVDMSNLPCGMNGALYLS
EMDADGGMSKYPSNPAGAKYGTGYCDAQCPRDLKFIGGEAGIGGYGSCCNEMDIWEANSRATAFTPHPCT
TPGQYRCSGYSENRYAGVCDKDGCGFNPYRMGNTSFYGPGKTVDTSKPFTVVTQFVTNDGGKLTEIKRLY
IQNGKVIESAVVNIEGIPPGNSITDDFCAAQGTNSFSRLGGLKQMGEALSRGMVLVMSIWDDEGANMLWL
DSGVARGPCPTTSGVPSNIESQQPNASVTFSNIKFG
>gnl|CDD|193574 cd08000, NGN, N-Utilization Substance G (NusG) N-terminal (NGN) domain Superfamily. The N-Utilization Substance G (NusG) and its eukaryotic homolog Spt5 are involved in transcription elongation and termination. NusG contains an NGN domain at its N-terminus and Kyrpides Ouzounis and Woese (KOW) repeats at its C-terminus in bacteria and archaea. The eukaryotic ortholog, Spt5, is a large protein composed of an acidic N-terminus, an NGN domain, and multiple KOW motifs at its C-terminus. Spt5 forms a Spt4-Spt5 complex that is an essential RNA Polymerase II elongation factor. NusG was originally discovered as an N-dependent antitermination enhancing activity in Escherichia coli and has a variety of functions, such as being involved in RNA polymerase elongation and Rho-termination in bacteria. Orthologs of the NusG gene exist in all bacteria, but its functions and requirements are different. The diverse activities suggest that, after diverging from a common ancestor, NusG proteins became specialized in different bacteria
NWYVLFVKTGREEKVEKLLEKRFEANDIEAFVPKKEVPERKRGKIEEVIKPLFPGYVFVETDLSPELYEL
IREVPGVIGILGNGEEPSPVSDEEIEMIL
>gnl|CDD|153428 cd08001, WGR_PARP1_like, WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins. The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of vertebrate PARP-1 and similar proteins, including Arabidopsis thaliana PARP-1 and PARP-3. PARP-1 is the best-studied among the PARPs. It is a widely expressed nuclear chromatin-associated enzyme that possesses auto-mono-ADP-ribosylation (initiation), elongation, and branching activities. PARP-1 is implicated in DNA damage and cell death pathways and is important in maintaining genomic stability and regulating cell proliferation, differentiation, neuronal function, inflammation, and aging
AHVLEEGGNLYSAVLGLVDIQTGTNSYYKLQLLEHDKGNRYWVFRSWGRVGTTIGGNKLEEFSSLEEAKM
AFEELYEEKTGNDFENRKNFKKKPGKFYPLDIDY
>gnl|CDD|153429 cd08002, WGR_PARP3_like, WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins. The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-3 and similar proteins, including Arabidopsis thaliana PARP-2. PARP-3 displays a tissue-specific expression, with highest amounts found in the nuclei of epithelial cells of prostate ducts, salivary glands, liver, pancreas, and in the neurons of terminal ganglia. Unlike PARP-1 and PARP-2, PARP-3 activity is not induced by DNA strand breaks. However, it co-localizes with Polycomb group bodies and is part of complexes making up DNA-PKcs, DNA ligases III and IV, Ku70, and Ku80. PARP-3 is a nuclear protein that may be involved in transcriptional control and responses to DNA damage
VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLESGKEYYVWNRWGRVGEKGQNKLKGPWDSLEGAIKDFEK
KFKDKTKNNWEDRENFVPHPGKYTLIEMDY
>gnl|CDD|153430 cd08003, WGR_PARP2_like, WGR domain of poly(ADP-ribose) polymerases. The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-2 and similar proteins. Similar to PARP-1, PARP-2 is ubiquitously expressed and its activity is induced by DNA strand breaks. It also plays a role in cell differentiation, cell death, and maintaining genomic stability. Studies on mice deficient with PARP-2 shows that it is important in fat storage, T cell maturation, and spermatogenesis
HVYEEGDDVYDAMLNQTNIQQNNNKYYIIQLLEDDAEKIYSVWFRWGRVGKKGQSSLVPCGSDLEQAKSL
FEKKFLDKTKNEWEDRANFEKVAGKYDLLEMDY
>gnl|CDD|381750 cd08010, MltG_like, proteins similar to Escherichia coli YceG/mltG may function as endolytic murein transglycosylases. The gene product of Escherichia coli yceG/mltG has been erroneously annotated as an aminodeoxychorismate lyase. Its overexpression has been reported to cause abnormal biofilm architecture, and it has been reported to be part of a putative five-gene operon. More recently it has been proposed to function as a terminase for peptidoglycan polymerization. The family also includes Streptomyces caeruleus NovB, an uncharacterized member of the novobiocin biosynthetic gene cluster
LKAGRYELSPGMSLAEILERLTSGKTAQVKLTIPEGYTLRQVAKALAKAGGLSEADFLKALRDPAFLKEL
GNPKYPLEGYLFPDTYEVPKGDSAEDILKRMVKRFNEKLEEAWLERAKLPGLTPYEVLTLASIVEKEAGL
DEERPKVAGVFYNRLKKGMPLQSDPTVIYALGKRKGGLITYKDLKIDSPYNTYVNKGLPPGPIANPGRSA
LKAALNPAKTDYLYFVADGDGGHYFSKTLEEHNRNV
>gnl|CDD|349933 cd08011, M20_ArgE_DapE-like, M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases. Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly archaeal, and have been inferred by homology as being related to both ArgE and DapE
VKLLQELVQIPSPNPPGDNTSAIAAYIKLLLEDLGYPVELHEPPEEIYGVVSNIVGGRKGKRLLFNGHYD
VVPAGDGEGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGR
AGTKYLLEKVRIKPNDVLIGEPSGSDNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLY
ELEKTVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSIEEVSFEIKSFYSPTVSNP
DSEIVKKTEEAITEVLGIRPKEVISVGASDARFYRNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKV
HALVA
>gnl|CDD|349934 cd08012, M20_ArgE-related, M20 Peptidases with similarity to acetylornithine deacetylases. Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved
LDEERFVSLLGKLIGESKYLQNNPPQLVPKEDNAGRHVLEALTPYSTENGGPLVIDHVSYVKGRGNIIVE
YPGTVDGKTVSFVGSHMDVVTANPETWEFDPFSLSIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPAL
KRTVVAVFIANEENSEIPGVGVDALVKSGLLDNLKSGPLYWVDSADSQPCIGTGGMVTWKLTATGKLFHS
GLPHKAINALELVMEALAEIQKRFYIDFPPHPKEEVYGFATPSTMKPTQWSYPGGSINQIPGECTICGDC
RLTPFYDVKEVREKLEEYVDDINANIEELPTRGPVSKYVLPAEGLRGRVSLEFDEAAASGVACNLDSPGF
HALCKATSEVVGYVKPYAITGSLPLIRELQDEGFDVQITGYGLMATYHAKNEYCLLSDFQNGFKVLARTI
AQL
>gnl|CDD|349935 cd08013, M20_ArgE_DapE-like, M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases. Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE
DDPVSLTQTLVRINSSNPSLSATGGAGEAEIATYVAAWLAHRGIEAHRIEGTPGRPSVVGVVRGTGGGKS
LMLNGHIDTVTLDGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGLRGDVILAAVADEED
ASLGTQEVLAAGWRADAAIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALE
EYQQELPERPVDPLLGRASVHASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTAILGELAQTV
PNFSYREPRITLSRPPFEVPKEHPFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGA
GLHAKEEWVDVESIRQLREVLSAVVREFC
>gnl|CDD|349936 cd08014, M20_Acy1-like, M20 Peptidase aminoacylase 1 subfamily. Peptidase M20 family, uncharacterized subfamily of uncharacterized bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine)
LVEWRRHLHAHPELSGQEYRTTAFVAERLRDLGLKPKEFPGGTGLVCDIGGKRDGRTVALRADMDALPIQ
EQTGLPYRSTVPGVMHACGHDAHTAIALGAALVLAALEEELPGRVRLIFQPAEETMPGGALDMIRAGALD
GVSAIFALHVDPRLPVGRVGVRYGPITAAADSLEIRIQGEGGHGARPHLTVDLVWAAAQVVTDLPQAISR
RIDPRSPVVLTWGSIEGGRAPNVIPDSVELSGTVRTLDPDTWAQLPDLVEEIVAGICAPYGAKYELEYRR
GVPPVINDPASTALLEAAVREILGEDNVVALAEPSMGGEDFAWYLEHVPGAMARLGVWGGDGTSYPLHHP
DFDVDERAIAIGVRVLAAAAL
>gnl|CDD|349937 cd08015, M28_like, M28 Zn-peptidase-like; uncharacterized subfamily. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions
TYNVIAEIPGSDKKDEVVILGAHLDSWHGATGATDNGAGTAVMMEAMRILKAIGSKPKRTIRVALWGSEE
QGLHGSRAYVEKHFGDPPTMQLQRDHKKISAYFNLDNGTGRIRGIYLQGNLAAYPIFSAWLYPFHDLGAT
TVIERNTGGTDHAAFDAVGIPAFQFIQDPWDYWTRTHHTNRDTYDRLIPEDLKQAAIITASFAYHASSRE
KIVPRKPL
>gnl|CDD|349938 cd08017, M20_IAA_Hyd, M20 Peptidase Indole-3-acetic acid amino acid hydrolase. Peptidase M20 family, plant aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage
LVRVRREIHENPELAFQEHETSALIRRELDALGIPYRYPVAKTGIVATIGSGSPPVVALRADMDALPIQE
LVEWEHKSKVDGKMHACGHDAHVAMLLGAAKLLKARKHLLKGTVRLLFQPAEEGGAGAKEMIKEGALDDV
EAIFGMHVSPALPTGTIASRPGPFLAGAGRFEVVIRGKGGHAAMPHHTVDPVVAASSAVLALQQLVSRET
DPLDSQVVSVTRFNGGHAFNVIPDSVTFGGTLRALTTEGFYRLRQRIEEVIEGQAAVHRCNATVDFSEDE
RPPYPPTVNDERMYEHAKKVAADLLGPENVKIAPPVMGAEDFAFYAEKIPAAFFFLGIRNETAGSVHSLH
SPYFFLDEEVLPVGAALHAAVAERYL
>gnl|CDD|349939 cd08018, M20_Acy1_amhX-like, M20 Peptidase aminoacylase 1 amhX-like subfamily. Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine)
ELKERIVEVFTHLHQIPEISWEEYKTTEYLAKKLEEMGFRVTTFEGGTGVVAEIGSGKPGPVVALRADMD
ALWQEVDGEFKANHSCGHDAHMTMVLGAAELLKKIGLVKKGKLKFLFQPAEEKGTGALKMIEDGVLDDVD
YLFGVHLRPIQELPFGTAAPAIYHGASTFLEGTIKGKQAHGARPHLGINAIEAASAIVNAVNAIHLDPNI
PWSVKMTKLQAGGEATNIIPDKAKFALDLRAQSNEAMEELKEKVEHAIEAAAALYGASIEITEKGGMPAA
EYDEEAVELMEEAITEVLGEEKLAGPCVTPGGEDFHFYTKKKPELKATMIGLGCGLTPGLHHPNMTFDRD
ALENGVKILARAVLK
>gnl|CDD|349940 cd08019, M20_Acy1-like, M20 Peptidase aminoacylase 1 subfamily. Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine)
IIELRRYFHMHPELSLKEERTSKRIKEELDKLGIPYVETGGTGVIATIKGGKAGKTVALRADIDALPVEE
CTDLEYKSKNPGLMHACGHDGHTAMLLGAAKILNEIKDTIKGTVKLIFQPAEEVGEGAKQMIEEGVLEDV
DAVFGIHLWSDVPAGKISVEAGPRMASADIFKIEVKGKGGHGSMPHQGIDAVLAAASIVMNLQSIVSREI
DPLEPVVVTVGKLNSGTRFNVIADEAKIEGTLRTFNPETREKTPEIIERIAKHTAASYGAEAELTYGAAT
PPVINDEKLSKIARQAAIKIFGEDSLTEFEKTTGSEDFSYYLEEVPGVFAFVGSRNEEKGATYPHHHEFF
NIDEDALKLGAALYVQFALDFL
>gnl|CDD|349941 cd08021, M20_Acy1_YhaA-like, M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085. Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity
LEELVDQLEDEMIQWRRHIHQYPELSFEEFETAAYIANELKKLGLEVETNVGGTGVVATLKGGKPGKTVA
LRADMDALPIEEETDLPFKSKNPGVMHACGHDGHTAMLLGAAKVLAENKDEIKGTVRFIFQPAEEVPPGG
AKPMIEAGVLEGVDAVFGLHLWSTLPTGTIAVRPGAIMAAPDEFDITIKGKGGHGSMPHETVDPIVIAAQ
IVTALQTIVSRRVDPLDPAVVTIGTFQGGTSFNVIPDTVELKGTVRTFDEEVREQVPKRIERIVKGICEA
YGASYELEYQPGYPVVYNDPEVTELVKKAAKEVLIGVENVEPQLMMGGEDFSYYLKEVPGCFFFLGAGNE
EKGCIYPHHSPKFDIDESALKIGVKVHVGAVLEL
>gnl|CDD|349942 cd08022, M28_PSMA_like, M28 Zn-peptidase prostate-specific membrane antigen. Peptidase M28 family; prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase II or GCP-II)-like subfamily. PSMA is a homodimeric type II transmembrane protein containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). PSMA is over-expressed predominantly in prostate cancer (PCa) as well as in the neovasculature of most solid tumors, but not in the vasculature of the normal tissues. PSMA is considered a biomarker for PCa and possibly for use as an imaging and therapeutic target. The extracellular domain of PSMA possesses two unique enzymatic functions: N-acetylated, alpha-linked acidic dipeptidase (NAALADase) which cleaves terminal glutamate from the neurodipeptide N-acetyl-aspartyl-glutamate (NAAG), and folate hydrolase (FOLH) which cleaves the terminal glutamates from gamma-linked polyglutamates (carboxypeptidase). A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. Inhibition of GCP-II has been shown to be effective in preclinical models of neurological disorders associated with excessive activation of glutamatergic systems. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants
EKILLDEPDAENIREWLRYYTSGPHLAGTEGNLELAQWTEDKWREFGLDDVELEEYDVPIWNVIGTIRGS
EEPDEYIILGNHRDAWVFGAGDPNSGTAVLLEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGSTEWV
EENADWLQERAVAYLNVDVAVSGSTLRAAGSPLLQNLLREAAKEVQDPDEGATLKYLPSWWDDTGGEIGN
LGSGSDYTPFLDHLGIASIDFGFSGGPTDPYPHYHSNYDSFEWMEKFGDPGFKYHVAIAQVWGLLALRLA
DDPILPF
>gnl|CDD|185693 cd08023, GH16_laminarinase_like, Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans
WSDEFDGDGLPDPSKWTYETGGGGNGNNELQYYTYRPENAYVEDGNLVITARKEPDKGGDGYPYTSGRIT
TKGKFSFTYGRVEARAKLPKGQGTWPAFWMLGENIKYVGWPASGEIDIMEYVGNEPNTVYGTLHGGATND
GNNGSGGSYTLPTDDLSDDFHTYAVEWTPDKITFYVDGKLYFTYTNPNTDNGGQWPFDQPFYLILNLAVG
GNWPGPPDDDTPFPATMEVDYVRVY
>gnl|CDD|185694 cd08024, GH16_CCF, Coelomic cytolytic factor, member of glycosyl hydrolase family 16. Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members
LVFEDDFDSFDLSKWQHEVTAGGGGNGEFQWYTNDRSNSYVRDGKLYIKPTLTADTFGEDFLTLGNGNLD
GLAPWGTCTNNANNGCYRTGNAGGIINPVMSARLRTKNSFSFKYGRVEVRAKLPTGDWLWPAIWMLPRDN
VYGGWPRSGEIDIMESRGNRPLYDGGEAIGINSVGSTLHWGPDPGQNRYTKTTGKRSDSGGDFADDFHTY
GLDWTPDHIRFYVDDRLILTLDVPGQGFWEFGGFSGTPIDNPWAGGGKMAPFDQEFYLILNVAVGGTNGF
FPDGWPGGKPWSNGSPTAMRDFWEARNQWLPTWHGGDDAAMQVDYVKMWQ
>gnl|CDD|153090 cd08025, RNR_PFL_like_DUF711, Uncharacterized proteins with similarity to Ribonucleotide reductase and Pyruvate formate lyase. This subfamily contains Streptococcus pneumoniae Sp0239 and similar uncharacterized proteins. Sp0239 is structurally similar to ribonucleotide reductase (RNR) and pyruvate formate lyase (PFL), which are believed to have diverged from a common ancestor. RNR and PFL possess a ten-stranded alpha-beta barrel domain that hosts the active site, and are radical enzymes. RNRs are found in all organisms and provide the only mechanism by which nucleotides are converted to deoxynucleotides. PFL is an essential enzyme in anaerobic bacteria that catalyzes the conversion of pyruvate and CoA to acteylCoA and formate
EEIIETIEMILEENLDIRTVTLGISLLDCIDPDIDELCENIYEKITSAAKRLVETVEEVSSELGVPIVNK
RISVTPIAILAAGLDAEDYVEIAKTLDKAAKEVGVDFIGGFSALVQKGFTRGDRALIESIPEALASTERV
CSSVNVASTKAGINMDAVKLMGEIIKETAELTKDGIGCAKLVVFANAPEDNPFMAGAFHGVGEPDAVINV
GVSGPGVVKAALEELKGADLEELAEEIKKTAFKITRLGELVGREVSERLGVPFGIVDLSLAPTPAVGDSV
AEILEEMGLERVGTHGTTAALALLNDAVKKGGAMATSRVGGLSGAFIPVSEDAGMIEAVREGALTLEKLE
AMTAVCSVGLDMIAVPGDTPAETISAIIADEMAIGVINNKTTAVRIIPVP
>gnl|CDD|153434 cd08026, DUF326, Cysteine-rich 4 helical bundle widely conserved in bacteria. This functionally uncharacterized protein forms a 4-helical bundle with a bromodomain-like topology. It is present in major bacterial lineages and contains highly conserved cysteines in a repeated pattern, whose sidechains appear buried. Some family members have been (mis)annotated as putative ferredoxins
MQECIDACLACARACEECADACLEEGGVHAMAECIRLDLDCADICRLAANLMSRGSPFAKALCALCAEIC
EACAEECEKHAHEHCQECAEACRRCAEACRKM
>gnl|CDD|153397 cd08028, LARP_3, La RNA-binding domain of La-related protein 3. This domain is found at the N-terminus of the La autoantigen and similar proteins, and co-occurs with an RNA-recognition motif (RRM). Together these domains function to bind primary transcripts of RNA polymerase III at their 3' terminus and protect them from exonucleolytic degradation. Binding is specific for the 3'-terminal UUU-OH motif. The La autoantigen is also called Lupus La protein, LARP3, or Sjoegren syndrome type B antigen (SS-B)
MDDLEKKIIRQIEYYFGDFNLPRDKFLKEQIKEDDGWVPMEVMLKFNRLKSLSSDPEVIAKALKKSKSGL
IEVSEDKTKIRR
>gnl|CDD|153398 cd08029, LA_like_fungal, La-motif domain of fungal proteins similar to the La autoantigen. This domain is found in fungal proteins related to the La autoantigen. A variety of La-related proteins (LARPs or La ribonucleoproteins), with differing domain architecture, appear to function as RNA-binding proteins in eukaryotic cellular processes
PEEIRKQVEFYFSDSNLPTDKFLWTLTGGSNNGWVPIKTIASFKRMRRFQPLEAVVEALRESELLEVSED
GENVRR
>gnl|CDD|153399 cd08030, LA_like_plant, La-motif domain of plant proteins similar to the La autoantigen. This domain is found in plant proteins related to the La autoantigen. A variety of La-related proteins (LARPs or La ribonucleoproteins), with differing domain architecture, appear to function as RNA-binding proteins in eukaryotic cellular processes
TKEKVLRQVEFYFSDSNLPRDDFLLEEVEEDPDGMVSLALICSFSRMRSLLGLGGGKPEDVPEDTLKAVA
EALRTSTLLKVSEDGKRVGR
>gnl|CDD|153400 cd08031, LARP_4_5_like, La RNA-binding domain of proteins similar to La-related proteins 4 and 5. This domain is found in proteins similar to La-related proteins 4 and 5 (LARP4, LARP5). A variety of La-related proteins (LARPs or La ribonucleoproteins), with differing domain architecture, appear to function as RNA-binding proteins in eukaryotic cellular processes
KELLKRQLEYYFSRENLANDAYLLSQMDSDQYVPIWTIANFNKIKKLTTDIDLIVEALRESPNVQVDEKG
EKVRP
>gnl|CDD|153401 cd08032, LARP_7, La RNA-binding domain of La-related protein 7. LARP7 is a component of the 7SK snRNP, a key factor in the regulation of RNA polymerase II transcription. 7SK functionality is dependent on the presence of LARP7, which is thought to stabilize the 7SK RNA by interacting with its 3' end. The release of 7SK RNA from P-TEFb/HEXIM/7SK complexes activates the cyclin-dependent kinase P-TEFb, which in turn phosphorylates the C-terminal domain of RNA pol II and mediates a transition into productive transcription elongation
RVKQLLADIAKQVDFWFGDVNLHKDRFLREQIEKSRDGYIDISLLVSFNKMKKLTTDGKLIARALKNSSV
VELNLEGTRIRR
>gnl|CDD|153402 cd08033, LARP_6, La RNA-binding domain of La-related protein 6. This domain is found in animal and plant proteins related to the La autoantigen. A variety of La-related proteins (LARPs or La ribonucleoproteins), with differing domain architecture, appear to function as RNA-binding proteins in eukaryotic cellular processes
IQKIVKQVEYYFSDENLLKDAFLLKHVRRNKEGYVPIKLIASFKKVKALTRDWRVVAAALRRSSKLVVSE
DGKKVRR
>gnl|CDD|153403 cd08034, LARP_1_2, La RNA-binding domain proteins similar to La-related proteins 1 and 2. This domain is found in proteins similar to vertebrate La-related proteins 1 and 2 (LARP1, LARP2). A variety of La-related proteins (LARPs or La ribonucleoproteins), with differing domain architecture, appear to function as RNA-binding proteins in eukaryotic cellular processes
KEYIKKQIEYYFSVDNLEKDFFLRRKMDPEGYLPIALIASFHRVQALTTDVNLILEALKDSTVVELVDEK
VRC
>gnl|CDD|153404 cd08035, LARP_4, La RNA-binding domain of La-related protein 4. This domain is found in vertebrate La-related protein 4 (LARP4), also known as c-MPL binding protein. La-type domains often co-occur with RNA-recognition motifs (RRMs). A variety of La-related proteins (LARPs or La ribonucleoproteins), with differing domain architecture, appear to function as RNA-binding proteins in eukaryotic cellular processes
RECLKKQLEFCFSRENLSKDLYLISQMDSDQFVPIWTVANMEGIKKLTTDMDLILDVLRSSPMVQVDETG
EKVRP
>gnl|CDD|153405 cd08036, LARP_5, La RNA-binding domain of La-related protein 5. This domain is found in vertebrate La-related protein 5 (LARP5). A variety of La-related proteins (LARPs or La ribonucleoproteins), with differing domain architecture, appear to function as RNA-binding proteins in eukaryotic cellular processes
RELLKKTLEFCLSRENLASDMYLISQMDSDQYVPIMTVANLDHIKKLSTDVDLIVDVLRSLPLVQVDEKG
EKVRP
>gnl|CDD|153406 cd08037, LARP_1, La RNA-binding domain of La-related protein 1. This domain is found in vertebrate La-related protein 1 (LARP1). A variety of La-related proteins (LARPs or La ribonucleoproteins), with differing domain architecture, appear to function as RNA-binding proteins in eukaryotic cellular processes
KDYIKRQIEYYFSVDNLERDFFLRRKMDEDGFLPVTLIASFHRVQALTTDISLIIKALKDSKVVEIIDMK
IRR
>gnl|CDD|153407 cd08038, LARP_2, La RNA-binding domain of La-related protein 2. This domain is found in vertebrate La-related protein 2 (LARP2). A variety of La-related proteins (LARPs or La ribonucleoproteins), with differing domain architecture, appear to function as RNA-binding proteins in eukaryotic cellular processes
KEYIKRQIEYYFSTENLERDFFLRRKMDLQGFLPISLIAGFYRVQALTTNVDLILEALKDSTEVEIVDQK
IRR
>gnl|CDD|185716 cd08039, Adenylation_DNA_ligase_Fungal, Adenylation domain of uncharacterized fungal ATP-dependent DNA ligase-like proteins. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent ligases are present in many organisms such as viruses, bacteriophages, eukarya, archaea and bacteria. This group is composed of uncharacterized fungal proteins with similarity to ATP-dependent DNA ligases. ATP dependent DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains including a DNA-binding domain, an adenylation (nucleotidyltransferase (NTase)) domain, and an oligonucleotide/oligosaccharide binding (OB)-fold domain. The adenylation domain binds ATP and contains many of the active-site residues. The adenylation and C-terminal OB-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core unit contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases. This model characterizes the adenylation domain of this group of uncharacterized fungal proteins. It is not known whether these proteins also contain an OB-fold domain
IGRPKSLKARSIKHCCKMIGSRRMWVETKYDGEYCQIHIDLSKDSSPIRIFSKSGKDSTADRAGVHSIIR
KALRIGKPGCKFSKNCILEGEMVVWSDRQGKIDPFHKIRKHVERSGSFIGTDNDSPPHEYEHLMIVFFDV
LLLDDESLLSKPYSERRDLLESLVHVIPGYAGLSERFPIDFSRSSGYERLRQIFARAIAERWEGLVLKGD
EEPYFDLFLEQGSFSGCWIKLKKDY
>gnl|CDD|153442 cd08040, OBF_DNA_ligase_family, The Oligonucleotide/oligosaccharide binding (OB)-fold domain is a DNA-binding module that is part of the catalytic core unit of ATP dependent DNA ligases. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP dependent DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains including a DNA-binding domain, an adenylation (nucleotidyltransferase (NTase)) domain, and an oligonucleotide/oligosaccharide binding (OB)-fold domain. The adenylation and C-terminal OB-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core unit contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases. The OB-fold domain contacts the nicked DNA substrate and is required for the ATP-dependent DNA ligase nucleotidylation step. The RxDK motif (motif VI), which is essential for ATP hydrolysis, is located in the OB-fold domain
KTAEAVIIGMRAGFGNRSDVMGSLLLGYYGEDGLQAVFSVGTGFSADERRDLWQNLEPLVTSFDDHPVWN
VGKDLSFVPLYPGKVVEVKYFEMGSKDCLRFPVFIGIR
>gnl|CDD|153443 cd08041, OBF_kDNA_ligase_like, The Oligonucleotide/oligosaccharide binding (OB)-fold domain of kDNA ligase-like ATP-dependent DNA ligases is a DNA-binding module that is part of the catalytic core unit. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent ligases are present in many organisms such as viruses, bacteriohages, eukarya, archaea and bacteria. The mitochondrial DNA of parasitic protozoan is highly unusual. It is termed the kinetoplast DNA (kDNA) and consists of circular DNA molecules (maxicircles) and several thousand smaller circular molecules (minicircles). This group is composed of kDNA ligase, Chlorella virus DNA ligase, and similar proteins. kDNA ligase and Chlorella virus DNA ligase are the smallest known ATP-dependent ligases. They are involved in DNA replication or repair. ATP dependent DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains. The adenylation and oligonucleotide/oligosaccharide binding (OB)-fold domains comprise a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core unit contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases. The OB-fold domain contacts the nicked DNA substrate and is required for the ATP-dependent DNA ligase nucleotidylation step. The RxDK motif (motif VI), which is essential for ATP hydrolysis, is located in the OB-fold domain
QDAEARVVGYEEGKGKYEGMLGALVVETKDGIRFKIGSGFSDEQRRNPPPIGSIITYKYQGLTKNGLPRF
PVFLRVR
>gnl|CDD|176269 cd08044, TAF5_NTD2, TAF5_NTD2 is the second conserved N-terminal region of TATA Binding Protein (TBP) Associated Factor 5 (TAF5), involved in forming Transcription Factor IID (TFIID). The TATA Binding Protein (TBP) Associated Factor 5 (TAF5) is one of several TAFs that bind TBP and are involved in forming Transcription Factor IID (TFIID) complex. TAF5 contains three domains, two conserved sequence motifs at the N-terminal and one at the C-terminal region. TFIID is one of seven General Transcription Factors (GTF) (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIID) involved in accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays an important role in the recognition of promoter DNA and assembly of the preinitiation complex. TFIID complex is composed of the TBP and at least 13 TAFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. TAF5 may play a major role in forming TFIID and its related complexes. TAFs from various species were originally named by their predicted molecular weight or their electrophoretic mobility in polyacrylamide gels. A new, unified nomenclature for the pol II TAFs has been suggested to show the relationship between TAF orthologs and paralogs. TAF5 has a paralog gene (TAF5L) which has a redundant function. Several hypotheses are proposed for TAFs functions such as serving as activator-binding sites, core-promoter recognition or a role in essential catalytic activity. C-terminus of TAF5 contains six WD40 repeats that likely form a closed beta propeller structure and may be involved in protein-protein interaction. The first part of the TAF5 N-terminal (TAF5_NTD1) homodimerizes in the absence of other TAFs. The second conserved N-terminal part of TAF5 (TAF5_NTD2) has an alpha-helical domain. One study has shown that TAF5_NTD2 homodimerizes only at high concentration of calcium but not any other metals. No dimerization was observed in other structural studies of TAF_NTD2. Several TAFs interact via histone-fold (HFD) motifs; HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamer. However, TAF5 does not have a HFD motif
PNDYEQAYSKLRKWIESSLDIYKYELSQLLYPIFVHSYLDLVASGHLEEAKSFFERFSGDFEDSHSEDIK
KLSSITTPEHLKENELAKLFRSNKYVIRMSRDAYSLLLRFLESWGGSLLLKILNEHIDIDVRD
>gnl|CDD|467027 cd08045, HFD_TAF4, histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and similar proteins. TAF4, also called TATA Binding Protein (TBP) associated factor 4, RNA polymerase II TBP-associated factor subunit C, TBP-associated factor 4, transcription initiation factor TFIID 130 kDa subunit (TAF(II)130, TAFII-130, TAFII130), or transcription initiation factor TFIID 135 kDa subunit (TAF(II)135, TAFII-135, TAFII135), is a component of the TFIID complex that is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TFIID is one of the general transcription factors required for accurate and regulated initiation by RNA polymerase II. It plays a central role in mediating promoter responses to various activators and repressors. TAF4 potentiates transcriptional activation by the AF-2S of retinoic acid, vitamin D3 and thyroid hormone. TAF4 also acts as a component of the TFTC-HAT complex and some MLL1/MLL complexes. TAF4 interacts with ATF7 and the interaction inhibits ATF7-mediated transactivation
EESFLNPPPLQKKIQKIAKKHGLKEVSPDVLSLLSLAVQERLRDLLEKLIVASKHRVDSEKPDYRYEVTS
DVRRQLKALERLEREEEERRREEERERLLR
>gnl|CDD|173966 cd08047, TAF7, TATA Binding Protein (TBP) Associated Factor 7 (TAF7) is one of several TAFs that bind TBP and is involved in forming Transcription Factor IID (TFIID) complex. The TATA Binding Protein (TBP) Associated Factor 7 (TAF7) is one of several TAFs that bind TBP and are involved in forming the Transcription Factor IID (TFIID) complex. TFIID is one of seven General Transcription Factors (GTF) (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIID) that are involved in accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays an important role in the recognition of promoter DNA and assembly of the preinitiation complex. TFIID complex is composed of the TBP and at least 13 TAFs. TAFs are named after their electrophoretic mobility in polyacrylamide gels in different species. A new, unified nomenclature has been suggested for the pol II TAFs to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs functions such as serving as activator-binding sites, core-promoter recognition or a role in essential catalytic activity. Each TAF, with the help of a specific activator, is required only for expression of subset of genes and is not universally involved for transcription as are GTFs. TAF7 is involved in the regulation of the transition from PIC assembly to initiation and elongation. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. Several TAFs interact via histone-fold (HFD) motifs; the HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers
EEQFILRLPPDVADRLRKAIEEGDSNEKLLSITLFEDSRRAVVRINGQKYPAKLVDLPTIIESHKTLDKK
NLYKTADISQMLIVYEPDDSEKEAKEAKLDKKDKPKKFEYPHGLTPPMKNVRKRRFRKTPSKKIAEIEEV
EKEVKRLLKEDTEAVSVEYEVI
>gnl|CDD|467028 cd08048, HFD_TAF11, histone-fold domain found in transcription initiation factor TFIID subunit 11 (TAF11) and similar proteins. TAF11, also called TATA Binding Protein (TBP) associated factor 11, TFIID subunit p30-beta, or transcription initiation factor TFIID 28 kDa subunit (TAF(II)28, TAFII-28, TAFII28), is a component of the TFIID complex that is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TFIID is one of the general transcription factors required for accurate and regulated initiation by RNA polymerase II. It plays a central role in mediating promoter responses to various activators and repressors. TAF11 interacts with the ligand binding domains of the nuclear receptors for vitamin D3 and thyroid hormone. TAF11 also directly interacts with TFIIA, acting as a bridging factor that stabilizes the TFIIA-TBP-DNA complex
FTEEQLERYEAFRRSKFNKSAIKRLMQSVLGQSVSQNVVIVMAGIAKVFVGELVETARDVQEEWGEATGP
LQPKHLREAYRRLKAEG
>gnl|CDD|176263 cd08049, TAF8, TATA Binding Protein (TBP) Associated Factor 8. The TATA Binding Protein (TBP) Associated Factor 8 (TAF8) is one of several TAFs that bind TBP, and is involved in forming the Transcription Factor IID (TFIID) complex. TFIID is one of seven General Transcription Factors (GTF) (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIID) that are involved in accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays an important role in the recognition of promoter DNA and the assembly of the preinitiation complex. The TFIID complex is composed of the TBP and at least 13 TAFs. TAFs from various species were originally named by their predicted molecular weight or their electrophoretic mobility in polyacrylamide gels. A new, unified nomenclature for the pol II TAFs has been suggested to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs' functions, such as serving as activator-binding sites, involvement in the core-promoter recognition, or a role in the essential catalytic activity of the complex. The mouse ortholog of TAF8 is called taube nuss protein (TBN), and is required for early embryonic development. TBN mutant mice exhibit disturbances in the balance between cell death and cell survival in the early embryo. TAF8 plays a role in the differentiation of preadipocyte fibroblasts to adipocytes; it is also required for the integration of TAF10 into the TAF complex. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. TAF8 is also a component of a small TAF complex (SMAT), which contains TAF8, TAF10 and SUPT7L. Several TAFs interact via histone-fold motifs. The histone fold (HFD) is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamer. TAF8 contains an H4 related histone fold motif, and interacts with several subunits of TFIID, including TBP and the histone-fold protein TAF10. Currently, five HF-containing TAF pairs have been described or suggested to exist in TFIID: TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10
AHIPSWLPPFPDPHTYKRTPTYSERETDPKKLREELASQRRLAEKALLRLQQKT
>gnl|CDD|381749 cd08050, TAF6C, C-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6). This model characterizes the carboxy (C)-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6), which is one of several TAFs that bind TBP and are involved in forming the Transcription Factor IID (TFIID) complex. This C-terminal HEAT repeat domain of TAF6 (TAF6C) is proposed to form a homodimer that effectively bridges the downstream promoter-interacting TAFs (TAF1, -2, and -7) with lobe B of TFIID. This domain influences the TAF6-TAF9 complex, is thus important for TFIID assembly, and may trigger signals from transcriptional effectors. The HEAT domain motif is generally involved in protein/protein interactions, and in A. locustae, the conserved TAF6C domain is formed by five HEAT repeats, tightly packed against each other, defining a single structural domain. TFIID is one of several General Transcription Factors (GTFs), which also include TFIIA, TFIIB, TFIIE, TFIIF and TFIIH, that are involved in the accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays a key role in the recognition of promoter DNA and assembly of the pre-initiation complex. The TFIID complex is composed of the TBP and at least 13 TAFs. TAFs are named after their electrophoretic mobility in polyacrylamide gels in different species. A new, unified nomenclature has been suggested for the pol II TAFs to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs' functions such as serving as activator-binding sites, core-promoter recognition, or a role in essential catalytic activity. These TAFs, with the help of specific activators, are required only for expression of a subset of genes and are not universally involved for transcription, as are GTFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. Several TAFs interact via histone-fold domain (HFD) motifs; the HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers. The minimal HFD contains three alpha-helices linked by two loops and is found in core histones, TAFs and many other transcription factors. TFIID has a histone octamer-like substructure. TAF6 is a shared subunit of histone acetyltransferase complex SAGA and TFIID complexes. The N-terminal HFD of TAF6, interacts with the HFD of TAF9 and makes a novel histone-like heterodimer that is structurally related to histones H4 and H3. TAF6 may also interact with the downstream core promoter element (DPE)
KHVLSKELQLYFEKITEALLGDDEELRKAALASLRTDPGLQPLLPYFVQFIAEGVTKNLRNLALLIYLLR
MVRALLDNPHLFLEPYLHQLLPSVLTCLLAKQLGSRPPTDNHWALRDFAASLLAQICKKYSTSYPTLQPR
ITKTLLKALLDPSKPLTTHYGAIVGLAALGPEAVRALLLPNLKAYLERLESELEDSSSNALKRIEAEKVY
GALLKA
>gnl|CDD|153444 cd08051, gp6_gp15_like, Head-Tail Connector Proteins gp6 and gp15, and similar proteins. Members of this family include the proteins gp6 and gp15 from bacteriophage HK97 and SPP1, respectively. They are critical in the assembly of the connector, a specialized structure that serves as an interface for head and tail attachment, as well as a point at which DNA exits the head during infection by the bacteriophage. They form dodecameric ring structures that comprise the middle ring of the connector, located between the portal protein (attached to the head) and the gp7/gp16 ring (attached to the tail). They are components of the mature phage and the absence or mutation of HK97 gp6 or SPP1 gp15, respectively, result in defective head-tail joining and the absence of mature phage particles. The genome maps of HK97 and SPP1 show that genes encoding gp6 and gp15 are in the same relative position on the genome, located adjacent to the major capsid protein (MCP) gene and in between head and tail genes. Also included in this family is the uncharacterized Bacillus subtilis Yqbg protein, whose gene is part of the unusual genetic element called skin. The Yqbg gene is surrounded with genes similar to genes in the Bacillus subtilis prophage-like element PBSX, which encode for proteins comprising contractile-tailed phage-like particles that are produced upon mitomycin C treatment. Yqbg likely acts as a head-tail connector protein, similar to gp6 and gp15, of the PBSX-like prophage encoded in the skin element
SLFKQQIEFEEDDRDELLTLYAQAAFDYCXRWCDEPFWDAVAADIPAAVKGAVLKVFQFYFEHRGAQSII
KDTTLGEVQLYENAAAERXXFIYR
>gnl|CDD|153445 cd08053, Yqbg, Putative Head-Tail Connector Protein Yqbg from Bacillus subtilis and similar proteins. The uncharacterized Bacillus subtilis Yqbg protein, whose gene is part of the unusual genetic element called skin, shows a similar structure to the connector proteins gp6 and gp15 from bacteriophage HK97 and SPP1, respectively. gp6 and gp15 are critical in the assembly of the connector, a specialized structure that serves as an interface for head and tail attachment, as well as a point at which DNA exits the head during infection by the bacteriophage. They form dodecameric ring structures that comprise the middle ring of the connector, located between the portal protein (attached to the head) and the gp7/gp16 ring (attached to the tail). The Yqbg gene is surrounded with genes similar to genes in the Bacillus subtilis prophage-like element PBSX, which encode for proteins comprising contractile-tailed phage-like particles that are produced upon mitomycin C treatment. Yqbg likely acts as a head-tail connector protein, similar to gp6 and gp15, of the PBSX-like prophage encoded in the skin element
MTYADYEFYTEEYYGKERPEELLKKDILRASAKIDKITFGRFDDLGYPEIPEEVKLAVCALAEYIALIDG
DESSGGGVTSESIGDYSVSYSSGTSGSLAKKDVYNLLLDYLAPTGLLYRGV
>gnl|CDD|153446 cd08054, gp6, Head-Tail Connector Protein gp6 of Bacteriophage HK97 and similar proteins. The bacteriophage HK97 gp6 protein is critical in the assembly of the connector, a specialized structure that serves as an interface for head and tail attachment, as well as a point at which DNA exits the head during infection by the bacteriophage. It forms a dodecameric ring structure that comprises the middle ring of the connector, located between the portal protein (attached to the head) and the gp7 ring (attached to the tail). It is a component of the mature phage and the absence of HK97 gp6 results in defective head-tail joining and the absence of mature phage particles. Although the crystal structure of HK97 gp6 shows an unexpected 13-mer ring, the biological form present in the mature phage is believed to be a dodecamer
TLEEAKAHLRIDHDDDDALIELLIDAAEEYIENYTGRDLDEQTADAEEVPALIKLAVLLLVAHLYENREA
VTDVTASELPFGVESLLAPYR
>gnl|CDD|153447 cd08055, gp15, Head-Tail Connector Protein gp15 of Bacteriophage SPP1 and similar proteins. The bacteriophage SPP1 gp15 protein is critical in the assembly of the connector, a specialized structure that serves as an interface for head and tail attachment, as well as a point at which DNA exits the head during infection by the bacteriophage. It forms a dodecameric ring structure that comprises the middle ring of the connector, located between the portal protein (attached to the head) and the gp16 ring (attached to the tail). Binding of the gp15 and gp16 rings to the portal protein is essential to prevent leakage of packaged DNA. gp15 is a component of the mature phage and its mutation results in defective head-tail joining
EKVKKLLGISLDDNSDDELLEELIEDAIEDVLDYCNQTFLPDPLLPTVVKLAVALYNKLGTEGEISSRSE
GDVSVSYETGLPKSILKGLNPYRRL
>gnl|CDD|163687 cd08056, MPN_PRP8, Mpr1p, Pad1p N-terminal (MPN) domains without isopeptidase activity found in splicing factor Prp8. Members of this family are found in pre-mRNA-processing factor 8 (Prp8) which is a critical splicing factor, interacting with several other spliceosomal proteins, snRNAs, and the pre-mRNA, thus organizing and stabilizing the spliceosome catalytic core. Prp8 is one of the largest and most highly conserved of nuclear proteins, occupying a central position in the catalytic core of the spliceosome. Its C-terminal domain exhibits a JAB1/MPN-like core similar to deubiquitinating enzymes, but does not show catalytic isopeptidase activity, possibly because the putative isopeptidase center is covered by insertions and terminal appendices that are grafted onto this core, thus impairing the metal binding site. It is proposed that this domain is a protein interaction domain instead of a Zn(2+)-dependent metalloenzyme as proposed for some MPN proteins. The DEAD-box protein Brr2 and the GTPase Snu114 bind to the Prp8 C-terminus, a region where mutations in human Prp8 (hPrp8) cause a severe form of the genetic disorder retinitis pigmentosa, RP13, which leads to progressive photoreceptor degeneration in the retina and eventual blindness. At the N-terminus of Prp8, there are several domains, including a highly variable nuclear localization signal (NLS) motif rich in prolines, a conserved RNA recognition motif (RRM), and U5 and U6 snRNA binding sites
FSSKTDWRVRAIAATNLHLRTKNIYVSSDDIKETGYTYILPKNLLKKFISISDLRTQIAGYLYGKSPPDN
PQVKEIRCIVLVPQLGTHQTVTLPQQLPQHEYLEDLEPLGWIHTQPNELPQLSPQDVTTHAKILADNPSW
DGEKTVILTCSFTPGSCSLTAYKLTPEGYEWGKQNKDLGNNTPKGYSPSFYEKVQLLLSDRFLGFFLVPE
DGVWNYNFMGAKHSPNMKYDLKLDIPKEFYHELHRPTHFLQF
>gnl|CDD|163688 cd08057, MPN_euk_non_mb, Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity (non metal-binding); eukaryotic. This family contains MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) domains variants lacking key residues in the JAB1/MPN/Mov34 metalloenzyme (JAMM) motif and are unable to coordinate a metal ion. Comparisons of key catalytic and metal binding residues explain why the MPN-containing proteins Rpn7/PSMD7, Rpn8/PSMD8, CSN6, Prp8p, and the translation initiation factor 3 subunits f and h do not show catalytic isopeptidase activity. It has been proposed that the MPN domain in these proteins has a primarily structural function. Rpn7 is known to be critical for the integrity of the 26S proteasome complex by establishing a correct lid structure. It is necessary for the incorporation/anchoring of Rpn3 and Rpn12 to the lid and essential for viability and normal mitosis. CSN6 is a highly conserved protein complex with diverse functions, including several important intracellular pathways such as the ubiquitin/proteasome system, DNA repair, cell cycle, developmental changes, and some aspects of immune responses. It cleaves ubiquitin-like protein Nedd8 (neural precursor cell expressed, developmentally downregulated 8)) in the cullin 1 in cells. EIF3f s a potent inhibitor of HIV-1 replication as well as an important negative regulator of cell growth and proliferation. EIF3h regulates cell growth and viability, and that over-expression of the gene may provide growth advantage to prostate, breast, and liver cancer cells
VQLHPLVLLNISDHYTRRKYGIKRVIGVLLGYVDGDKIEVTNSFELPFDEEEESIFIDTEYLEKRYNLHK
KVYPQEKIVGWYSIGSNNSNEISKSDNSLHSQFSLISEENPLILILDPSLQSDSEKLEISTFTSAQREEN
GAEITYEIGTEETERIA
>gnl|CDD|163689 cd08058, MPN_euk_mb, Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); eukaryotic. This family contains eukaryotic MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) domains found in proteins with a variety of functions, including AMSH (associated molecule with the Src homology 3 domain (SH3) of STAM), H2A-DUB (histone H2A deubiquitinase), BRCC36 (BRCA1/BRCA2-containing complex subunit 36), as well as Rpn11 (regulatory particle number 11) and CSN5 (COP9 signalosome complex subunit 5). These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity. Rpn11 is responsible for substrate deubiquitination during proteasomal degradation. It is essential for maintaining a correct cell cycle and normal mitochondrial morphology and physiology. CSN5 is critical for nuclear export and the degradation of several tumor suppressor proteins, including p53, p27, and Smad4. Over-expression of CSN5 has been implicated in cancer initiation and progression. AMSH specifically cleaves Lys 63 and not Lys48-linked polyubiquitin (poly-Ub) chains, thus facilitating the recycling and subsequent trafficking of receptors to the cell surface. It is involved in the degradation of EGF receptor (EGFR) and possibly other ubiquitinated endocytosed proteins. BRCC36 is part of the BRCA1/BRCA2/BARD1-containing nuclear complex that displays an E3 ubiquitin ligase activity; it is targeted to DNA damage foci after irradiation. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. It is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene and serves as a marker in prostate tumors
DALLKMLQHAESNTGIEVMGLLCGELTHNEFTDKHVIVPKQSAGPDSCTGENVEELFNVQTGRPLLVVGW
YHSHPTFTAWLSSVDIHTQASYQLMLPEAIAIVVSPKHRNKDTGIFRLT
>gnl|CDD|163690 cd08059, MPN_prok_mb, Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); prokaryotic. This family contains bacterial and archaeal MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These catalytically active domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site
DLLKTILVHAKDAHPDEFCGFLSGSKDNVMDELIFLPFVSGSVSAVIDLAALEIGMKVVGLVHSHPSGSC
RPSEADLSLFTRFGLYHVIVCYPYENSWKCY
>gnl|CDD|163691 cd08060, MPN_UPF0172, Mov34/MPN/PAD-1 family: UPF0172 family of unknown function includes neighbor of COX4 (Noc4p). This family includes Noc4p (neighbor of COX4; neighbor of Cytochrome c Oxidase 4; nucleolar complex associated 4 homolog) which belongs to the family of unknown function, UPF0172, with MPN/JAMM-like domains. Proteins in this family are homologs of the NOC4 gene which is conserved in eukaryotic members including human, dog, mouse, rat, chicken, zebrafish, fruit fly, mosquito, S.pombe, K.lactis, E.gossypii, M.grisea, N.crassa, A.thaliana, and rice. NOC4 highly expressed in the pancreas and moderately in liver, heart, lung, kidney, brain, skeletal muscle, and placenta. This nucleolar protein forms a complex with Nop14p that mediates maturation and nuclear export of 40S ribosomal subunits. This family of eukaryotic MPN-like domains lacks the key residues that coordinate a metal ion and therefore does not show catalytic isopeptidase activity
LSTLAYVKMLLHAAKYPHCAVNGLLLGKKSSGGSVEITDAVPLFHSCLALAPMLEVALALVDAYCKSSGL
VIVGYYQANERLDDSSPSPVAKKIADKIAENFSNACLLMVDNEKLTLDCKGNALVVYKDKGGRWKVKELR
GINLLLWESANEILSALLSSKAYRNLVDFDDHLDDISLDWLN
>gnl|CDD|163692 cd08061, MPN_NPL4, Mov34/MPN/PAD-1 family: nuclear protein localization-4 (Npl4) domain. Npl4p (nuclear protein localization-4) is identical to Hmg-CoA reductase degradation 4 (HRD4) protein and contains a domain that is part of the pfam clan MPN/Mov34-like. Npl4 plays an intermediate role between endoplasmic reticulum-associated degradation (ERAD) substrate ubiquitylation and proteasomal degradation. Npl4p associates with Cdc48p (Cdc48 in yeast and p97 or valosin-containing protein (VCP) in higher eukaryotes), the highly conserved ATPase of the AAA family, via ubiquitin fusion degradation-1 protein (Ufd1p) to form a Cdc48p-Ufd1p-Npl4p complex which then functions in the recognition of several polyubiquitin-tagged proteins and facilitates their presentation to the 26S proteasome for processive degradation. This family of eukaryotic MPN-like domains lacks the key residues that coordinate a metal ion and therefore does not show catalytic isopeptidase activity
TLKRQKYRHVDHVEFDNPSIVEFFLYVFWRKTGQQRIGFLYGRYDEDEDVPLGIKAVVEAIYEPPQEGTP
DGFELLEDPNADTVDAIAAALGLERVGWIFTDLPREDKDGYFLSAEEVILAAKFQLKHPTGKFGSKFVTV
VVTGDKDGQIHFEAYQVSDQAMALVRDGLLLPTKDADELYVREPTLERYVPDVFYSGKDKYGKTKAVPEV
DVEYFLVDVPHGFPLSPSSFKSSDFPIENRPPSLGELQDLDALARYLGKPFLERLSDFHLLLYL
>gnl|CDD|163693 cd08062, MPN_RPN7_8, Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in 19S proteasomal subunits Rpn7 and Rpn8. This family includes lid subunits of the 26 S proteasome regulatory particles, Rpn7 (PSMD7; proteasome 26S non-ATPase subunit 7; p44), and Rpn8 (PSMD8; proteasome 26S non-ATPase subunit 8; p40; Mov34). Rpn7 is known to be critical for the integrity of the 26 S proteasome complex by establishing a correct lid structure. It is necessary for the incorporation/anchoring of Rpn3 and Rpn12 to the lid and essential for viability and normal mitosis. Rpn7 and Rpn8 are ATP-independent components of the 19S regulator subunit, and contain the MPN structural motif on its N-terminal region. However, while they show a typical MPN metalloprotease fold, they lack the canonical JAMM motif, and therefore do not show catalytic isopeptidase activity. It is suggested that Rpn7 function is primarily structural
KKVVVHPLVLLSVVDHYNRVAKGTSKRVVGVLLGSWKKGVLDVTNSFAVPFEEDEKDPSVWFLDHNYLEN
MYGMFKKVNAKEKIVGWYSTGPKLRPNDLDINELFRRYCPNPVLVIIDVRPKDLGLPTEAYIAVEEVHDD
GTPTSKTFVHVPSEIGAEEAEEVGVEHLLRDIKDVTVSTLSTRVTNKLNSLKGLQSKLKEIKDYLQLVVE
GKLPINHQIIYNLQDIFNLLPNLNLPELVKAFAVKTNDQMLVIYLSSLIRSVIALHNLINNKIANKEAEK
>gnl|CDD|163694 cd08063, MPN_CSN6, Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in COP9 signalosome complex subunit 6. CSN6 (COP9 signalosome subunit 6; COP9 subunit 6; MOV34 homolog, 34 kD) is one of the eight subunits of COP9 signalosome, a highly conserved protein complex with diverse functions, including several important intracellular pathways such as the ubiquitin/proteasome system, DNA repair, cell cycle, developmental changes, and some aspects of immune responses. CSN6 is an MPN-domain protein that directly interacts with the MPN+-domain subunit CSN5. It is cleaved during apoptosis by activated caspases. CSN6 processing occurs in CSN/CRL (cullin-RING Ub ligase) complexes and is followed by the cleavage of Rbx1, the direct interaction partner of CSN6. CSN6 cleavage enhances CSN-mediated deneddylating activity (i.e. cleavage of ubiquitin-like protein Nedd8 (neural precursor cell expressed, developmentally downregulated 8)) in the cullin 1 in cells. The cleavage of Rbx1 and increased deneddylation of cullins inactivate CRLs and presumably stabilize pro-apoptotic factors for final apoptotic steps. While CSN6 shows a typical MPN metalloprotease fold, it lacks the canonical JAMM motif, and therefore does not show catalytic isopeptidase activity
LSVKLHPLVILNISDHITRHRAQSQSEPPRVVGALLGQQDGREIEIENSFELKYDTNEDGEIVLDKEFLE
TRLEQFKQVFKDLDFVGWYTTGPGGPTESDLPIHKQILEINESPVLLLLDPEANASGKDLPVTIYESVLE
LVDGEATLRFRELPYTIETGEAERIGVDHVARGGASGSSEKSTVAAHLQAQHNAIKMLNSRVELILEYLK
AVPVGEVPPDHSILRSISALCSRLPVLKSEAFREELLAEYNDVLLVAYLATLTKGCNTLNELVDKFNVVY
DRKGSGRR
>gnl|CDD|163695 cd08064, MPN_eIF3f, Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF3f. Eukaryotic translation initiation factor 3 (eIF3) subunit F (eIF3F; EIF3S5; eIF3-p47; eukaryotic translation initiation factor 3, subunit 5 epsilon, 47kDa; Mov34/MPN/PAD-1 family protein) is an evolutionarily non-conserved subunit of the functional core that comprises eIF3a, eIF3b, eIF3c, eIF3e, eIF3f, and eIF3h, and contains the MPN domain. However, it lacks the canonical JAMM motif, and therefore does not show catalytic isopeptidase activity. It has been shown that eIF3f mRNA expression is significantly decreased in many human tumors including pancreatic cancer and melanoma. EIF3f is a potent inhibitor of HIV-1 replication; it mediates restriction of HIV-1 expression through several factors including the serine/arginine-rich (SR) protein 9G8, and cyclin-dependent kinase 11 (CDK11). EIF3f phosphorylation by CDK11 is important in regulating its function in translation and apoptosis. It enhances its association with the core eIF3 subunits during apoptosis, suggesting that eIF3f may inhibit translation by increasing the binding to the eIF3 complex during apoptosis. Thus, eIF3f may be an important negative regulator of cell growth and proliferation
VRVHPVVLFSILDSYERRNEGQERVIGTLLGTRSEGEVEITNCFAVPHNESEDQVAVDMEYHRTMYELHQ
KVNPKEVIVGWYATGSEITEHSALIHDYYSRECTSYNPIHLTVDTSLDDGKMSIKAYVSSPLGVPGKTLG
SMFVPIPLELLYSEAERVALDLLAKTLASPSRSAPLTSDLEQLEASLEKLQEMLDRVLRYVEDVLAGKVK
ADNAIGRYLMDALTSVPKLDPEEFEKMFNSSLQDLLMVTYLSNLTKTQLALAEKL
>gnl|CDD|163696 cd08065, MPN_eIF3h, Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h. Eukaryotic translation initiation factor 3 (eIF3) subunit h (eIF3h; eIF3 subunit 3; eIF3S3; eIF3-gamma; eIF3-p40) is an evolutionarily non-conserved subunit of the functional core that comprises eIF3a, eIF3b, eIF3c, eIF3e, eIF3f, and eIF3h, and contains the MPN domain. However, it lacks the canonical JAMM motif, and therefore does not show catalytic isopeptidase activity.Together with eIF3e and eIF3f, eIF3h stabilizes the eIF3 complex. Results suggest that eIF3h regulates cell growth and viability, and that over-expression of the gene may provide growth advantage to prostate, breast, and liver cancer cells. For example, EIF3h gene amplification is common in late-stage prostate cancer suggesting that it may be functionally involved in the progression of the disease. It has been shown that coamplification of MYC, a well characterized oncogene involved in cell growth, differentiation, and apoptosis, and EIF3h in patients with non-small cell lung cancer (NSCLC) improves survival if treated with the Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitor (EGFR-TKI), Gefitinib. Plant eIF3h is implicated in translation of specific mRNAs
TSVQIDGLVVLKIIKHCKEELPELVQGQLLGLDVGGTLEVTNCFPFPKSEEDDSDRADEDIADYQLEMMR
LLREVNVDHNHVGWYQSTYLGSFFTRDLIETQYNYQEAIEESVVLVYDPSKTSQGSLSLKAYRLSEKFME
LYKEGKFSTESLREANLTFSNIFEEIPVVIRNSHLVNALLSELEEDSPSSQSDFDRLDLSTNSFLEKNLE
LLMESVDELSQEQGKFNYYQRNLARQQAQIQQWLQKRKAENAQREARGEEPLPEED
>gnl|CDD|163697 cd08066, MPN_AMSH_like, Mov34/MPN/PAD-1 family. AMSH (associated molecule with the Src homology 3 domain (SH3) of STAM (signal-transducing adapter molecule, also known as STAMBP)) and AMSH-like proteins (AMSH-LP) are members of JAMM/MPN+ deubiquitinases (DUBs), with Zn2+-dependent ubiquitin isopeptidase activity. AMSH specifically cleaves Lys 63 and not Lys48-linked polyubiquitin (poly-Ub) chains, thus facilitating the recycling and subsequent trafficking of receptors to the cell surface. AMSH and AMSH-LP are anchored on the early endosomal membrane via interaction with the clathrin coat. AMSH shares a common SH3-binding site with another endosomal DUB, UBPY (ubiquitin-specific protease Y; also known as USP8), the latter being a cysteine protease that does not discriminate between Lys48 and Lys63-linked ubiquitin. AMSH is involved in the degradation of EGF receptor (EGFR) and possibly other ubiquitinated endocytosed proteins. AMSH also interacts with CHMP1, CHMP2, and CHMP3 proteins, all of which are components of ESCRT-III, suggested to be required for EGFR down-regulation. The function of AMSH-LP has not been elucidated; however, it exhibits two fundamentally distinct features from AMSH: first, there is a substitution in the critical amino acid residue in the SH3-binding motif (SBM) in the human AMSH-LP, but not in its mouse ortholog, and lacks STAM-binding ability; second, AMSH-LP lacks the ability to interact with CHMP proteins. It is therefore likely that AMSH and AMSH-LP play different roles on early endosomes
LRQVVVPADLMDKFLQLAEPNTSRNLETCGILCGKLSNNAFFITHLIIPKQSGTSDSCQTTNEEELFDFQ
DQHDLITLGWIHTHPTQTCFLSSVDLHTHCSYQLMLPEAIAIVCAPKYNEFGIFRLTDPPGLDEILNCKK
TGFHPHPKDPPLYEDCGHVIWKDQLKVTVVDLR
>gnl|CDD|163698 cd08067, MPN_2A_DUB, Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase. This family includes histone H2A deubiquitinase (Histone H2A DUB;MYSM1; myb-like, SWIRM and MPN domains 1; 2ADUB; 2A-DUB; KIAA19152ADUB, or KIAA1915/MYSM1), a member of JAMM/MPN+ deubiquitinases (DUBs), with possible Zn2+-dependent ubiquitin isopeptidase activity. It contains the SWIRM (Swi3p, Rsc8p and Moira), and SANT (SWI-SNF, ADA N-CoR, TFIIIB)/Myb domains; the SANT, but not the SWIRM, domain can bind directly to DNA. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. 2A-DUB interacts with p/CAF (p300/CBP-associated factor) in a co-regulatory protein complex, where the status of acetylation of nucleosomal histones modulates its deubiquitinase activity. 2A-DUB is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene; it participates in transcriptional regulation events in androgen receptor-dependent gene activation. In prostate tumors, the levels of uH2A are dramatically decreased, thus 2A-DUB serving as a cancer-related marker
KIQPFKVTVSSNALLLMDFHCHLTTSEVIGYLGGTWDPNTQNLTILQAFPCRSRLTGLDCEMDPVSETEI
RESLESRGLSVVGWYHSHPTFPPNPSLRDIDTQLDYQIMFKGSDSGYEPCVGLICSPYDRRNSTPESQIT
CFWVMPPPENRPNEYGVPMLMSYTVSQDEFLTQDVLKELRWLVEFYR
>gnl|CDD|163699 cd08068, MPN_BRCC36, Mov34/MPN/PAD-1 family: BRCC36, a subunit of BRCA1-A complex. BRCC36 (BRCA1-A complex subunit BRCC36; BRCA1/BRCA2-containing complex subunit 36; BRCA1/BRCA2-containing complex subunit 3; BRCC3; BRISC complex subunit BRCC36; BRCC36 isopeptidase complex; Lys-63-specific deubiquitinase BRCC36) and BRCC36-like domains are members of JAMM/MPN+ deubiquitinases (DUBs), possibly with Zn2+-dependent ubiquitin isopeptidase activity. BRCC36 is part of the BRCA1/BRCA2/BARD1-containing nuclear complex that displays an E3 ubiquitin ligase activity. It is targeted to DNA damage foci after irradiation; RAP80 recruits the Abraxas-BRCC36-BRCA1-BARD1 complex to DNA double strand breaks (DSBs) for DNA repair through specific recognition of Lys 63-linked polyubiquitinated proteins by its tandem ubiquitin-interacting motifs. A new protein, MERIT40 (mediator of RAP80 interactions and targeting 40 kDa), also named NBA1 (new component of the BRCA1 A complex), exists in the same BRCA1-containing complex and is essential for the integrity of the complex. There are studies suggesting that MERIT40/NBA1 ties BRCA1 complex integrity, DSB recognition, and ubiquitin chain activities to the DNA damage response. It has also been shown that BRCA1-containing complex resembles the lid complex of the 26S proteasome
LSKVHLSADVYLVCLTHALSTEKEEVMGLLIGEIEVSKKGEEVAIVHISAVIILRRSDKRKDRVEISPEQ
LSAASTEAERLTEETGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDSGFVGLIFSCFNEDKSTKMG
EVQVTCFQSVQGNKAGQYERIEVPLEIVPTSTISEACLESLVELPEILYQEEEDAYNKALQSCDLDPLTK
IHNGSVYTKSLCHILETISGPLLQLLEARLEQNK
>gnl|CDD|163700 cd08069, MPN_RPN11_CSN5, Mov34/MPN/PAD-1 family: proteasomal regulatory protein Rpn11 and signalosome complex subunit CSN5. This family contains proteasomal regulatory protein Rpn11 (26S proteasome regulatory subunit rpn11; PAD1; POH1; RPN11; PSMD14; Rpn11 subunit of the 19S-proteasome; regulatory particle number 11) and signalosomal CSN5 (COP9 signalosome complex subunit 5; COP9 complex homolog subunit 5; c-Jun activation domain-binding protein-1; CSN5/JAB1; JAB1). COP9 signalosome (CSN) and the proteasome lid are paralogous complexes and their respective subunits CSN5 and Rpn11 are most closely related between the two complexes, both containing the conserved JAMM (JAB1/MPN/Mov34 metalloenzyme) motif involved in zinc ion coordination and providing the active site for isopeptidase activity. Rpn11 is responsible for substrate deubiquitination during proteasomal degradation. It is essential for maintaining a correct cell cycle and normal mitochondrial morphology and physiology; mutations in Rpn11 cause cell cycle and mitochondrial defects, temperature sensitivity and sensitivity to DNA damaging reagents such as UV. It has been shown that the C-terminal region of Rpn11 is involved in the regulation of the mitochondrial fission and tubulation processes. CSN5, one of the eight subunits of CSN, is critical for nuclear export and the degradation of several tumor suppressor proteins, including p53, p27, and Smad4. Its MPN+ domain is critical for the physical interaction of RUNX3 and Jab1. It has been suggested that the direct interaction of CSN5/JAB1 with p27 provides p27 with a leucine-rich nuclear export signal (NES), which is required for binding to chromosomal region maintenance 1 (CRM1), and facilitates nuclear export. The over-expression of CSN5/JAB1 also has been implicated in cancer initiation and progression, including cancer of the lung, pancreas, mouth, thyroid, and breast, suggesting that the oncogenic activity of CSN5 is associated with the down-regulation of RUNX3
PWKPDPDYFEKVYISSLALLKMLKHARAGGPIEVMGLMLGKVDDYTIIVVDVFALPVEGTETRVNAQDEF
QEYMVQYEMLKQTGRPENVVGWYHSHPGYGCWLSGIDVNTQQLNQQLQDPFVAVVVDPIRSLVKGKVVIG
AFRTIPPGYKPLEPRQTTSNIGHLPKPKIEDFGGHNKQYYSLPIEYFKSSLDRKLLLNLWNKYWVNTLSL
SPLLENSNEYTIKQILDLAEKLEKAEQQEERLTGEELDIANVGKLDKARDSSKIHLEE
>gnl|CDD|163701 cd08070, MPN_like, Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding). This family contains archaeal and bacterial MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site
RELLEAILAHAEAEYPEECCGLLLGKGGGVTAIVTEVYPVRNVAESPRRRFEIDPAEQLAAQREARERGL
EVVGIYHSHPDGPARPSETDLRLAWPPGVSYLIVSLAGGAPELRAWRLEGGQFEEEEV
>gnl|CDD|163702 cd08071, MPN_DUF2466, Mov34/MPN/PAD-1 family. Mov34 DUF2466 (also known as DNA repair protein RadC) domain of unknown function contains the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity. However, to date, the name RadC has been misleading and no function has been determined
EDVAEYLREELGDLDQEEFVVLLLDTKNRLIAVETISVGTLNSSLVHPREIFKEALRHNAAAIILAHNHP
SGDPTPSREDIELTKRLKEAGELLGIRLLDHIIVGDGGYFSFR
>gnl|CDD|163703 cd08072, MPN_archaeal, Mov34/MPN/PAD-1 family: archaeal JAB1/MPN/Mov34 metalloenzyme. This family contains only archaeal MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site
ISRDLLDSILEAAKSSHPNEFAALLRGKDGVITELLILPGTESGEVSAVFPLLMLPLDMSIVGSVHSHPS
GSPRPSDADLSFFSKTGLVHIIVGYPYDEDDWRAYDSDGEPVELEVV
>gnl|CDD|163704 cd08073, MPN_NLPC_P60, Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding) found in proteins also containing NlpC/P60 domains. This family contains bacterial MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains at the N-terminus of NlpC/P60 phage tail protein domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site
KLEDAILAHAKAEYPREACGLVVRKGRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPD
GSPAPSEADRAQQEATGLPWIIVSWPEGDLRVFRPVGY
>gnl|CDD|173969 cd08148, RuBisCO_large, Ribulose bisphosphate carboxylase large chain. Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions
VLATYRVHPEATPPEKAAEAIAAESSTGTWTEVPTTQEQLRRVKGRVYSVEELGKRYIVKIAYPVELFEP
GNIPQILTVTAGNLFGLGALEAVRLEDLEFPEEYKKLFPGPKFGIDGIRKLLGVYGRPLVGTIIKPKLGL
NPKYTAEAAYAAALGGLDLIKDDETLTDQPFCPLRDRITEVAAALDRVQEETGEKKLYAVNVTAGTFEII
ERAERALELGANMLMVDVLTAGFSALQALAEDFEIDLPIHVHRAMHGAVTRSKFHGISMLVLAKLLRMAG
GDFIHTGTVVGKMALEREEALGIADALTDDWAGFKRVFPVASGGIHPGLVPGILRDFGIDVILQAGGGIH
GHPDGTVAGARAMRQA
>gnl|CDD|163706 cd08150, catalase_like, Catalase-like heme-binding proteins and protein domains. Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity
GLRGQHFQGTCAFGTFEVLADLKERLRVGLFAEGKVYPAYIRFSNGAGIDDTKPDIRGFAIKFTGVADAG
TLDFVLNNTPVFFIRNTSDYEDFVAEFARSARGEPPLDFIAWYVEKRPEDLPNLLGARSQVPDSYAAARY
FSQVTFAFINGAGKYRVVRSKDNPVDGIPSLEDHELEARPPDYLREELTERLQRGPVVYDFRIQLNDDTD
ATTIDNPTILWPTEHPVEAVAKITIPPPTFTAAQEAFAFNPFTPWHGLLETNDLGPILEVRRRVYTSSQG
LRH
>gnl|CDD|163707 cd08151, AOS, Allene oxide synthase. Allene oxide synthase converts a fatty acid hydroperoxide to an allene oxide, which is an unstable epoxide. In corals, the enzyme is part of a eiconaosid synthesis pathway that is initiated by a lipoxygenase, which generates the fatty acid hydroperoxides in the first step. The structure of allene oxide synthase closely resembles that of catalase, but allene oxide synthase does not have catalase activity
EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESDFPEHAFFTAGKRFPVILRHANI
VGGDDDASLDGRGAALRFLNAGDDDAGPLDLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRGPLAR
YAVWASLRRAPDSYTDLHYYSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPR
LPGDTRPKDYLRNEFRQRLQSPGVRYRLQIQLREVSDDATAVALDCCRPWDEDEHPWLDLAVVRLGAPLP
NDELEKLAFNPGNTPESLGLPLAYCADDYASLGHLRSLVYEISQRLRK
>gnl|CDD|163708 cd08152, y4iL_like, Catalase-like heme-binding proteins similar to the uncharacterized y4iL. Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to Rhizobium sp. NGR234 y4iL, of mostly bacterial origin
GHALRDAHAKSHGCLKAEFTVLDDLPPELAQGLFAEPGTYPAVIRFSNAPGDILDDSVPDPRGMAIKVLG
VPGEKLLPEEDATTQDFVLVNHPVFFARDAKDYLALLKLLARTTSLPDGAKAALSAPLRGALRVLEAAGG
ESPTLKLGGHPPAHPLGETYWSQAPYRFGDYVAKYSVVPASPALPALTGKELDLTDDPDALREALADFLA
ENDAEFEFRIQLCTDLEKMPIEDASVEWPEALSPFVPVATITIPPQDFDSPARQRAFDDNLSFNPWHGLA
EHRPLGSINRARKAVYEASSAFRHE
>gnl|CDD|163709 cd08153, srpA_like, Catalase-like heme-binding proteins similar to the uncharacterized srpA. Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to the Synechococcus elongatus PCC 7942 periplasmic protein srpA, of mostly bacterial origin. The plasmid-encoded srpA is regulated by sulfate, but does not seem to function in its uptake or metabolism
VDALEALFGKHPGFRRNHAKGICVSGTFTPSGAAASLSRAPLFSGGSVPVTGRFSLGGGNPKAPDDAANP
RGMALKFRLPDGEQWRMVMNSFPVFPVRTPEEFLALLKAIAPDATGKPDPAKLKAFLAAHPEAAAFLAWI
KTAPPPASFANTTYYGVNAFYFTNANGKRQPVRWRFVPEDGVKYLSDEEAAKLGPDFLFDELAQRLAQGP
VRWDLVLQLAEPGDPTDDPTKPWPADRKEVDAGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLL
AARSAAYAVSFSRRQ
>gnl|CDD|163710 cd08154, catalase_clade_1, Clade 1 of the heme-binding enzyme catalase. Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 1 catalases are found in bacteria, algae, and plants; they have a relatively small subunit size of 55 to 69 kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. They appear to form tetramers. In eukaryotic cells, catalases are located in peroxisomes
TLTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYT
RASFLQEPGKKTPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMI
HALKPSPVTNIQDPNRIFDFFSHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYH
WKPKQGVKNLTAEEAAEVQGKNFNHATQDLYDAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPE
DQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEPSDDKMLQGRLFSYSDTQRYRLGPNYLQLPI
NAPKAAVHNNQRDGQMNYGHDTSDVNYEPSRLDGLPEAPKYPYSQPPLSGTTQQAPIAKTNNFKQAGERY
RSFSEEEQENLIKNLVVDLSDVNEEIKLRMLSYFSQADPDYGERVAEGL
>gnl|CDD|163711 cd08155, catalase_clade_2, Clade 2 of the heme-binding enzyme catalase. Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 2 catalases are mostly found in bacteria and fungi; they have a large subunit size of 75 to 84 kDa, and bind a heme d group buried deep inside the structure. They appear to form tetramers. In eukaryotic cells, catalases are located in peroxisomes
DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAV
KFYTEEGNYDLVGNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAQSAHDTFWDFVSLQPESAHMVMWAM
SDRAIPRSYRMMEGFGVHTFRLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIE
SGDYPEWELGVQLIDEEDEFKFDFDILDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVV
PGIDFSNDPLLQGRLFSYLDTQLSRLGGPNFHELPINRPVCPVHNNQRDGHMRMTINKGRVNYFPNSLGA
GPPRAASPAEGGFVHYPEKVEGPKIRIRSESFADHYSQARLFWNSMSPVEKEHIISAFTFELSKVETPEI
RERVVDHLANIDEDLAKKVAKGL
>gnl|CDD|163712 cd08156, catalase_clade_3, Clade 3 of the heme-binding enzyme catalase. Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 3 catalases are the most abundant subfamily and are found in all three kingdoms of life; they have a relatively small subunit size of 43 to 75 kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. Clade 3 catalases also bind NADPH as a second redox-active cofactor. They form tetramers, and in eukaryotic cells, catalases are located in peroxisomes
RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFY
TEEGNWDLVGNNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPD
GYRHMNGYGSHTFSLVNAKGERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSW
TLYVQVMPEEDAEKYRFNPFDLTKVWPHKDYPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSP
DKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCPVNNYQRDGAMRVDGNGGGAPNYEPNSFGGPPEDPEY
AEPPLPVSGDADRYNYRDDDDDYTQAGDLYRLVSEDERERLVENIAGHLKGAPEFIQERQVAHFYKADPD
YGERVAKAL
>gnl|CDD|163713 cd08157, catalase_fungal, Fungal catalases similar to yeast catalases A and T. Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. This family of fungal catalases has a relatively small subunit size, and binds a protoheme IX (heme b) group buried deep inside the structure. Fungal catalases also bind NADPH as a second redox-active cofactor. They form tetramers; in eukaryotic cells, catalases are typically located in peroxisomes. Saccharomyces cerevisiae catalase T is found in the cytoplasm, though
LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKG
SADTVRDPRGFAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQNPE
SIHQVMILFSDRGTPASYRSMNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYA
TKDLFEAIERGDYPSWTVYVQVMTPEQAEKLRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQ
AAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPNYQQLPVNRPKTSPVYNPYQRDGPMSVNGNYGG
DPNYVSSILPPTYFKKRVDADGHHENWVGEVVAFLTEITDEDFVQPRALWEVVGKPGQQERFVKNVAGHL
SGAPPEIRKRVYEIFARVNPDLGKRIEKATE
>gnl|CDD|176482 cd08159, APC10-like, APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination. This family contains the single domain protein, APC10, a subunit of the anaphase-promoting complex (APC), as well as the DOC1 domain of multi-domain proteins present in E3 ubiquitin ligases. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC, a multi-protein complex (or cyclosome), is a cell cycle-regulated, E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. APC10-like DOC1 domains such as those present in HECT (Homologous to the E6-AP Carboxyl Terminus) and Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase proteins, HECTD3, and CUL7, respectively, are also included in this hierarchy. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling a SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, Fbx29 F-box protein, and ROC1 (RING-box protein 1) and promotes ubiquitination. CUL7 is a multi-domain protein with a C-terminal cullin domain that binds ROC1 and a centrally positioned APC10/DOC1 domain. HECTD3 contains a C-terminal HECT domain which contains the active site for ubiquitin transfer onto substrates, and an N-terminal APC10 domain which is responsible for substrate recognition and binding. An APC10/DOC1 domain homolog is also present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT domain. Recent studies have shown that the protein complex HERC2-RNF8 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Also included in this hierarchy is an uncharacterized APC10/DOC1-like domain found in a multi-domain protein, which also contains CUB, zinc finger ZZ-type, and EF-hand domains. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here
KCYTASIEVSSNPLPVSRLTDGNYDTYWQSDGSQGSHWIRLFMKKDVLIRVLAIFVDMADSSYMPSLVVV
YGGHSPSDLRELKDVNIRPSNGWVALLEDDTLKCPYIEIRIKRCRSDGIDTRIRGLRLL
>gnl|CDD|380914 cd08161, SET, SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily. The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site
EIRPSTIPGAGFGLFATRDIPKGEVIGLARFINHSCEPNCEFEEVYVGGKPRVFIVALRDIKAGEELTVD
YG
>gnl|CDD|277369 cd08162, MPP_PhoA_N, Synechococcus sp. strain PCC 7942 PhoA and related proteins, N-terminal metallophosphatase domain. Synechococcus sp. strain PCC 7942 PhoA is a large atypical alkaline phosphatase. It is known to be transported across the inner cytoplasmic membrane and into the periplasmic space. In vivo inactivation of the gene encoding PhoA leads to a loss of extracellular, phosphate-regulated phosphatase activity, but does not appear to affect the cells capacity for phosphate uptake. PhoA may play a role in scavenging phosphate during growth of Synechococcus sp. strain PCC 7942 in its natural environment. PhoA belongs to a domain family which includes the bacterial enzyme UshA and several other related enzymes including SoxB, CpdB, YhcR, and CD73. All members have a similar domain architecture which includes an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LQLLHFSDQEAGFQAIEDIPNLSAVLSALYEEAKADNANSLHVSAGDNTIPGPFFDASAEVPSLGAQGRA
DISIQNELGVQAIALGNHEFDLGTDLLAGLIAYSARGNTLGAAFPSLSVNLDFSNDANLAGLVITADGQE
ASTIAGKVAKSCIVDVNGEKVGIVGATTPGLRSISSPGAEKLPGLDFVSGRDEAENLPLESAIIQALVDV
LAANAPDCNKVVLLSHMQQISIEQELADRLSGVDVIVAGGSNTRLVDTNDMLRAGDSSQGVYPLFTTDAD
GNTTLIVNTDGNYKYVGRLVVDFDEEGNVIPYSYDDEVSGVYATD
>gnl|CDD|277370 cd08163, MPP_Cdc1, Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain. Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. Cdc1 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
ALVADPQLVDDHTYPGRPWILNTLTEHFVDQYLRRNWRYLQKQLKPDSTFFLGDLFDGGREWADEYWKKE
YFRFNRIFDPKPLRKMIESLPGNHDIGFGNGVKLPVRQRFESYFGPTSRVIDVGNHTFVIVDTISLSNND
NPQVYQPAREFLHSFEAMKVNSKPRILLTHVPLYRPPNTSCGPLREKKTPLPYGYGYQYQNVLEPSLSES
ILKAINPVAAFSGDDHDYCEVVHEYQFDGKEGSAREITVKSISMAMG
>gnl|CDD|277371 cd08164, MPP_Ted1, Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain. Saccharomyces cerevisiae Ted1 (trafficking of Emp24p/Erv25p-dependent cargo disrupted 1) is a metallophosphatase domain-containing protein which acts together with Emp24p and Erv25p in cargo exit from the ER. Ted1 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LALGDPQIEGDWPITNYGFKGRLDIFGNDYFLGHIYQMMQFRLKPTHVTVLGDLFSSQWITDEEFEKRAD
RYKKRIFGRSDWQVGNISLAARTFENGDILLINIAGNHDVGYAGESTEARISRFEQLFILLTHVPLYKFF
LEGKPGLILTGHDHEGCDYEYPSNPSVTWATSLEESGNGVREYTVRSMMGEFG
>gnl|CDD|277372 cd08165, MPP_MPPE1, human MPPE1 and related proteins, metallophosphatase domain. MPPE1 is a functionally uncharacterized metallophosphatase domain-containing protein. The MPPE1 gene is located on chromosome 18 and is a candidate susceptibility gene for Bipolar disorder. MPPE1 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKM
FRHPSDTPLHVVAGNHDIGFHYEMTTYKVHRFEKVFILLQHYPLYRLLQWLKPRLVLSGHTHSACEVLHY
GGIPEISVPSFSWRNR
>gnl|CDD|277373 cd08166, MPP_Cdc1_like_1, uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain. A functionally uncharacterized subgroup related to the metallophosphatase domain of Saccharomyces cerevisiae Cdc1, S. cerevisiae Ted1 and human MPPE1. Cdc1 is an endoplasmic reticulum-localized transmembrane lipid phosphatase and is a subunit of DNA polymerase delta. TED1 (trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), acts together with Emp24p and Erv25p in cargo exit from the ER. The MPPE1 gene is a candidate susceptibility gene for Bipolar disorder. Proteins in this uncharacterized subgroup belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination
LLVADPQILGYENEKFGLGEISRWDSDRYLAKTYERALWYFKPDIVIFLGDLFDEGIIANDDEYYSYVQR
FIGIFPLKRGKNAIYIPGDNDIGGESEIIIESRVRRFNNYFIMLSHVPLLVEGYLLLKHVVVDLKPDLIF
SGHDHSSFIFIYQRKKPRNVLFTRVSDVDPTYKKLKGQNESVHEIQVPTCSYRMG
>gnl|CDD|173979 cd08168, Cytochrom_C3, Heme-binding domain of the class III cytochrome C family and related proteins. This alignment models heme binding core motifs as encountered in the cytochrome C3 family and related proteins. Cytochrome C3 is a tetraheme protein found in sulfate-reducing bacteria which use either thiosulfate or sulfate as the ultimate electron acceptors. C3 is an integral part of a complex electron transfer chain. The model also contains triheme cytochromes C7 which function in electron transfer during Fe(III) respiration by Geobacter sulfurreducens (PpcA, PpcB, PpcC, PpcD, and PpcE) and four repeated core motifs as found in the 16-heme cytochrome C HmcA of Desulfovibrio vulgaris Hildenborough which plays a role in electron transfer through the membrane following periplasmic oxidation of hydrogen (resulting in sulfate reduction in the cytoplasm)
KGPVPFPHKKHAEALGIDCRTCHHKYEGGKGEPQKCAECHSHDGTDDPDFVSLKDAFHNSCIGCHKEMAK
AGKKTGPVGCAGCHK
>gnl|CDD|341448 cd08169, DHQ-like, Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. This group contains dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. These proteins exhibit the dehydroquinate synthase structural fold. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multi-step reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. 2-epi-5-epi-valiolone synthases catalyze the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications
EYPVFFGEGVFESVNSYIPRDAFDQCLIIVDSGVPDLIVNYLAEYFGYYLEVHVFIIQGGEAYKTFQTVV
EELERAAALHLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKN
LLGAFYPPRAVFADFSFLKTLPFRQVRAGMAELVKMALIADNDFFEFLEDKANSATVYSPEQLEKLINKC
ISLKLDVVVADEDEQGKRRGLNYGHTFGHALELASGYKIPHGEAVAVGMAYAAKIANRLGLLPEHDVSRI
IWLLNKLGLPLDHPLALDPDSLYEYLESDKKSLYGNLGMILLSGVGDG
>gnl|CDD|341449 cd08170, GlyDH, Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site
PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGECSREEIERLA
AIARANGADVVIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNP
DLVLVDTEIIAKAPVRFLVAGMGDALATYFEARACARSGAPNMAGGRPTLAALALAELCYDTLLEYGVAA
KAAVEAGVVTPALEAVIEANTLLSGLGFESGGLAAAHAIHNGLTALPETHHLLHGEKVAFGTLVQLVLEG
RPDEEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRKVAEAACAPGETIHNMPFPVTPEDVVDAILAADA
L
>gnl|CDD|341450 cd08171, GlyDH-like, Glycerol dehydrogenase-like. This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site
LPSYTIGEDAYDAIPKICSPYGKKVVVIGGKKALAAAKPKLRAALEGSGLEITDFIWYGGEATYENVEKL
KANPEVQEADMIFAVGGGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFLKRP
PVHTFIDTEIIAEAPEKYLWAGIGDTLAKYYEVEFSARGDELDHTNALGVAISKMCSEPLLKYGVQALED
CRANKVSDALEQVVLDIIVTTGLVSNLVEPDYNSSLAHALYYGLTTLPQIEEEHLHGEVVSYGVLVLLTV
DGQFEELEKVYAFNKSIGLPTCLADLGLTVEDLEKVLDKALKTKDLRHSPYPITKEMFEEAIKDL
>gnl|CDD|341451 cd08172, GlyDH-like, Glycerol_dehydrogenase-like. This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site
PQEYICEEGALKELPELLSEFGIKRPLIIHGEKSWQAAKPYLPKLFEIEYPVLRYDGECSYEEIDRLAEE
AKEHQADVIIGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYDYFPRSAYL
VLVDPRLLLDSPKDYFVAGIGDTLAKWYEADAILRQLEELPAFLQLARQAAKLCRDILLKDSEQALADLE
AGKLTPAFIKVVETIIALAGMVGGFGDEYGRSAGAHAIHNGLTKLPETHHFLHGEKVAYGILVQLALEGK
WDEIKKLLPFYRRLGLPTSLADLGLTDDTEEALQKIAAFAASPEESIHLLPPDVTAEEVLQAIEKL
>gnl|CDD|341452 cd08173, Gro1PDH, Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya
LPRNVVVGHGAINKIGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEAAEVE
KVKKLIKESKADFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDKPYSIKAKAP
IAIIADTEIISKAPKRLLAAGCGDLISNITAVKDWRLAHRLKGEYYSEYAASLALMSAKLIIENADLIKP
GLEEGVRTVVKALISSGVAMSIAGSSRPASGSEHLFSHALDKLAPGPALHGEQCGVGTIMMAYLHGGDWK
EIREALKKIGAPTTAKELGLDKEIIIEALTIAHKIRPERYTILGDNGLTEEAAERLARITGVI
>gnl|CDD|341453 cd08174, G1PDH-like, Glycerol-1-phosphate dehydrogenase-like. These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion
PLILKIEEGALEHLGKYLADRNQGFGKVAIVTGEGIDELLGEDILESLEEAGEIVTVEENTDNSAEELAE
KAFSLPKVDAIVGIGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKVDGKRKSLGAKMPYGV
IVDLDVIKSAPRRLILAGIGDLISNITALYDWKLAEEKGGEPVDDFAYLLSRTAADSLLNTPGKDIKDDE
FLKELAESLVLSGIAMEIAGSSRPASGSEHLISHALDKLFPGPALHGIQVGLGTYFMSFLQGQRYEEIRD
VLKRTGFPLNPSDLGLTKEEFIEAVKLAPSTRPGRYTILEELDLSEERLKEI
>gnl|CDD|341454 cd08175, G1PDH, Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner. Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer
IKEIVIGEGALKKLPEYLKELFGGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGEGDLIADEA
AVGKVLLELEKDTDLIIAVGSGTINDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPIIVDGVKKTFPAH
APKAIFADLDVLANAPQRMIAAGFGDLLGKYTALADWKLSHLLGGEYYCPEVADLVQEALEKCLDNAEGI
AARDPEAIEALMEALILSGLAMQLVGNSRPASGAEHHLSHYWEMEFLRLGKPPVLHGEKVGVGTLLIAAL
YILEQLPPPEELRELLRKAGAPTTPEDLGIDRDLLRDSLRLAKEIRDRYTVLDLAWDLGL
>gnl|CDD|341455 cd08176, LPO, Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate
NRFVLNPTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPT
IENVMAGVAAYKESGADGIIAVGGGSSIDTAKAIGIIVANPGADVRSLEGVAPTKNPAVPIIAVPTTAGT
GSEVTINYVITDTEKKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELS
DMLALKAIELIAKNLRKAVANPNNVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANA
ILLPYVMEFNAPATGEKYRDIARAMGVDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEA
LAEDALNDVCTPGNPREATKEDIIALYK
>gnl|CDD|341456 cd08177, MAR, Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes. Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer and is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase
PQRVVFGAGTLAELAEELERLGARRALVLSTPRQRALAERVAALLGDRVAGVFDGAVMHVPVEVAERALA
AAREAGADGLVAIGGGSAIGLAKAIALRTGLPIVAVPTTYAGSEMTPIWGETEDGVKTTGRDPRVLPRTV
IYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPSDLEARSDA
LYGAWLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALGGGDAA
GGLYDLARRLGAPTSLRDLGMPEDDIDRAADLALANPYPNPRPVERDALRALLERAW
>gnl|CDD|341457 cd08178, AAD_C, C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD). This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure
KVPPKIYFEPGCLPYLLLELPGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVR
KGLEAMNAFKPDVIIALGGGSAMDAAKIMWLFYEHPETKFEDLAQRFMDIRKRVYKFPKLGKKAKLVAIP
TTSGTGSEVTPFAVITDDKTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVM
ASDYTDGLALQAIKLIFEYLPRSYNNGNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPH
GRANAILLPHVIRYNATDPPTKQAAFPQYKYYVAKERYAEIADLLGLGGKTPEEKVESLIKAIEDLKKDL
GIPTSIREAGIDEADFLAAVDKLAEDAFDDQCTGANPRYPLISELKEILL
>gnl|CDD|341458 cd08179, NADPH_BDH, NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria. NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold
RFFVPRDIYFGEGALEYLKTLKGKRAFIVTGGGSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETV
EKGAEAMREFEPDWIIAIGGGSVIDAAKAMWVFYEYPELTFEDALVPFPLPELRKKARFIAIPSTSGTGS
EVTRASVITDTEKGIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDA
LALGAILDIFENLPKSYNGGKDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAIL
LPYVIEFNSKDPEARARYAALLIGLTDEELVEDLIEAIEELNKKLGIPLSFKEAGIDEDEFFAKLDEMAE
NAMNDACTGTNPRKPTVEEMKELLKAAYY
>gnl|CDD|341459 cd08180, PDD, 1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism. 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold
FSLKTKIYSGEDSLERLKELKGKRVFIVTDPFMVKSGMVDKVTDELDKSNEVEIFSDVVPDPSIEVVAKG
LAKILEFKPDTIIALGGGSAIDAAKAIIYFALKQKGNIKKPLFIAIPTTSGTGSEVTSFAVITDPEKGIK
YPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRA
YRDGDDLEAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEFLIAAIRRLN
KKLGIPSTLKELGIDEEEFEKAIDEMAEAALADRCTATNPRKPTAEDLIELLR
>gnl|CDD|341460 cd08181, PPD-like, 1,3-propanediol dehydrogenase-like (PPD). This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion
FYMPTKVYFGKNCVEKHADELAALGKKALIVTGKHSAKKNGSLDDVTEALEENGIEYFIFDEVEENPSIE
TVEKGAELARKEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDLFQNGKYNPPLPIVAIPTTAGTGSEV
TPYSILTDHEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALA
LEALRLIGECLPNLLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLP
AYLKLCEKQEPEKVDKILKLLGFGSIEEFQKFLNRLLGKKEELSEEELEKYADEAMKAKNKKNTPGNVTK
EDILRIYR
>gnl|CDD|341461 cd08182, HEPD, Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP). Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes
PVKIIFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDALGGRIPVVVFSDFSPNPDLEDLER
GIELFRESGPDVIIAVGGGSVIDTAKAIAALLGSPGENLLLLRTGEKAPEENALPLIAIPTTAGTGSEVT
PFATIWDEAEGKKYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYAL
RAIRLILENLPLLLENLPNLEAREAMAEASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPA
VLRYNAGADDECDDDPRGREILLALGASDPAEAAERLRALLESLGLPTRLSEYGVTAEDLEALAASVNTP
ERLKNNPVRLSEEDLLRLLE
>gnl|CDD|341462 cd08183, Fe-ADH-like, Iron-containing alcohol dehydrogenases-like. This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized
PPRIVFGRGSLQELGELAAELGKRALLVTGRSSLRSGRLARLLEALEAAGIEVALFSVSGEPTVETVDAA
VALAREAGCDVVIAIGGGSVIDAAKAIAALLTNEGSVLDYLEVVGKGRPLTEPPLPFIAIPTTAGTGSEV
TKNAVLSSPEHGVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALA
REGLRLAARSLRRAYEDGEDLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLP
PVLEANLRALREREPDSPALARYRELAGILTGDPDAAAEDGVEWLEELCEELGIPRLSEYGLTEEDFPEI
VEKARGSSSMKGNPIELSDEELLEILE
>gnl|CDD|341463 cd08184, Fe-ADH_KdnB-like, Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis. This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity
VPKYLFGRGSFDQLGELLAERRKSNNDYVVFFIDDVFKGKPLLDRLPLQNGDLLIFVDTTDEPKTDQIDA
LRAQIRAENDKLPAAVVGIGGGSTMDIAKAVSNMLTNPGSAADYQGWDLVKNPGIYKIGVPTLSGTGAEA
SRTAVLTGPEKKLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEK
ALELCRDVFLSDDMMSPENREKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVANCIVFNVLEE
FYPEGVKEFREMLEKQNITLPKGICKDLTDEQYEKMVAVTLIHEKPLTNALGPDWKDILTPEKVTKLF
>gnl|CDD|341464 cd08185, Fe-ADH-like, Iron-containing alcohol dehydrogenases-like. This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized
YYQPTRILFGAGKLNELGEEALRPGKKALIVTGKGSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTT
TVMEGAALAKEEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYIFGGTGKGPPPEKALPIIAIPTTAG
TGSEVDPWAVITNPETKEKKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPF
SDMLALEAIRLVAKYLPRAVKDGSDLEAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHPNIPHGAG
LAALYPAYFEFTIEKAPEKFAFVARAEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWL
AENAMETMGGLFANNPVELTEEDIVEIYE
>gnl|CDD|341465 cd08186, Fe-ADH-like, Iron-containing alcohol dehydrogenase. This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover
KTTLYFGVGAIAKIKDILKDLGIDKVIIVTGRSSYKKSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQA
DEAAKLARDFGADAVIAIGGGSPIDTAKSVAVLLAYGGKTARDLYGFRFAPERALPLVAINLTHGTGSEV
DRFAVATIPEKGYKPGIAYDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLA
KEAIRLIAEYLPRALANPKDLEARYWLLYASMIAGIAIDNGLLHLTHALEHPLSGLKPELPHGLGLALLG
PAVVKYIYKAVPETLADILRPIVPGLKGTPDEAEKAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVELA
FTTPSLDLLLSLAPVEVTEEVVREIYEESL
>gnl|CDD|341466 cd08187, BDH, Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. The butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway in anaerobic micro-organism. Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. Activity in the reverse direction is 50-fold lower than that in the forward direction. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Since members of this superfamily use different divalent ions, preferentially iron or zinc, it has been suggested to be renamed to family III metal-dependent polyol dehydrogenases. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3. The active site of YqhD contains a Zn metal, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions
NFTFYNPTKIIFGKGAIEELGEEIKKYGKKVLLVYGGGSIKKNGLYDRVVASLKEAGIEVVEFGGVEPNP
RLETVREGIELAREENVDFILAVGGGSVIDAAKAIAAGAKYDGDVWDFFTGKAPPEKALPVGTVLTLAAT
GSEMNGGAVITNEETKEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDAPL
QDRLAEGLLRTVIENGPKALKDPDDYEARANLMWAATLALNGLLGAGRGGDWATHAIEHELSALYDITHG
AGLAIVFPAWMRYVLKKKPERFAQFARRVFGIDPGGDDEETALEGIEALEEFFKSIGLPTTLSELGIDEE
DIEEMAEKAVRGGGLGGGFKPLTREDIEEILK
>gnl|CDD|341467 cd08188, PDDH, 1,3-Propanediol (1,3-PD) dehydrogenase. This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity
FRFYIPPVNLFGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPT
VTNVNEGLELFKENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDYEGVDKSKKPGLPLIAINTTAGTA
SEVTRFAVITDEERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTD
ALALEAIRLIAENLPKAVANGKDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAI
LLPHVMEFNLPACPERFADIARALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLL
AENALKDACGPTNPRQATKEDVIAIYR
>gnl|CDD|341468 cd08189, Fe-ADH-like, Iron-containing alcohol dehydrogenases-like. This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized
LPWPEPELFEGAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTI
DNVEEGLALYKENGCDAIIAIGGGSVIDCAKVIAARAANPKKSVRKLKGLLKVRKKLPPLIAVPTTAGTG
SEATIAAVITDPETHEKYAINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETD
EYALEAVKLIFENLPKAYEDGSDLEARENMLLASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAV
VLPHVLEFYGPAAEKRLAELADAAGLGDSGESDSEKAEAFIAAIRELNRRMGIPTTLEELKEEDIPEIAK
RALKEANPLYPVPRIMDRKDCEELLRKV
>gnl|CDD|341469 cd08190, HOT, Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism. This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used
ASNIRFGPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFE
EAIEFAKEGDFDAFVAVGGGSVIDTAKAANLYATHPGDFLDYVNAPIGKGKPVPGPLKPLIAIPTTAGTG
SETTGVAIFDLEELKVKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNARPR
PANPDERPAYQGSNPISDVWAEKAIELIGKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAM
AYPIAGLVKDYRPPGYPVDHPHVPHGLSVALTAPAVFRFTAPACPERHLEAAELLGADTSGASDRDAGEV
LADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLKLNPRPVTEEDLEEIFEDAL
>gnl|CDD|341470 cd08191, Fe-ADH-like, Iron-containing alcohol dehydrogenases-like. This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized
LRSPSRLLFGPGARRALGRVAARLGSRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVST
VADAAAAARAFDPDVVIGLGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEV
TPVAVLTDPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDFPPFPRLDP
DPVYVGKNPLTDLLALEAIRLIGRHLPRAVRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGA
LTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALGVTTAGTSEEAADRAIERVEELLARIGIPTTLAD
LGVTEADLPGLAEKALSVTRLIANNPRPPTEEDLLRILRAAF
>gnl|CDD|341471 cd08192, MAR-like, Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes. Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase
LERVSYGPGAVEALLHELATLGASRVFIVTSKSLATKTDVIKRLEEALGDRHVGVFSGVRQHTPREDVLE
AARAVREAGADLLVSLGGGSPIDAAKAVALALAEDVTDVDQLDALEDGKRIDPNVTGPTLPHIAIPTTLS
GAEFTAGAGATDDDTGHKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFV
DALALKALRLLFEGLPRSKADPEDLEARLKCQLAAWLSLFGLGSGVPMGASHAIGHQLGPLYGVPHGITS
CIMLPAVLRFNAPVNAERQRLIARALGLVTGGLGREAADAADAIDALIRELGLPRTLRDVGVGRDQLEKI
AENALTDVWCRTNPRPITDKDDVLEILESA
>gnl|CDD|341472 cd08193, HVD, 5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene
FQTVPRIICGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEA
VVEAAVEQAREAGADGVIGFGGGSSMDVAKLVALLAGSDQPLDDIYGVGKATGPRLPLILVPTTAGTGSE
VTPISIVTTGETEKKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKKNPISDAL
AREALRLLGANLRRAVEDGSDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVL
PHVLRFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPMLAE
DAMKQTRLLVNNPREVTEEDALAIYQAAL
>gnl|CDD|341473 cd08194, Fe-ADH-like, Iron-containing alcohol dehydrogenases-like. This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions
PRTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVE
EGLALYKEGGCDFIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTR
FTVITDTETDVKMLLKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALS
AIKLIGRNLRRAYADGDDLEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAV
TEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALERLCADLEIPTLREYGIDEEEFEAALDKMAE
DALASGSPANNPRVPTKEEIIELYREAW
>gnl|CDD|341474 cd08195, DHQS, Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway
SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETV
ERIYDFLLEAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGK
NLIGAFYQPKAVLIDPDFLKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIAR
SVEIKADIVEEDEREKGLRAILNFGHTFGHAIESASGYKLLHGEAVAIGMVAAARLSVKLGLLSEEDLER
IRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKIRFVLLKGIGKAVIVDDVSEEEIREAL
>gnl|CDD|341475 cd08196, Fe-ADH-like, iron-containing alcohol dehydrogenases (Fe-ADH)-like. This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized
WSYYQPVKIIFGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVAVFSDVEPNPTVE
NVDKCARLARENGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYLEGKKKIPKKGLPLIAIPTTAGTGS
EVTPVAVLTDKEKGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDA
LALEAAKLVLENLEKAYNNPNDKEAREKMALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALT
LPSFIRLNAEALPGRLDELAKQLGFKDAEELADKIEELKKRIGLRTRLSELGITEEDLEEIVEESFHPNR
ANNNPVEVTKEDLEKLL
>gnl|CDD|341476 cd08197, DOIS, 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose. 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multistep reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. They are important antibacterial agents. DOIS is a homolog of the dehydroquinate synthase which catalyzes the cyclization of 3-deoxy-D-arabino-heputulosonate-7-phosphate to dehydroquinate (DHQ) in the shikimate pathway
LTDIYLGRGILESLLSILEELKADRHFLVTDSNVNDLYGDRLLEGLKKAGIPVELLVVPAGESNKTLSTL
TELAERLIAAGITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGK
NLVGSYYAPLFVFVDTEFLKTLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDL
SIEAKLEVLSNDPYEKKEGLILEYGHTVGHAIELLSGGELSHGEAVAIGMCVAAEISHLLGLLSEEDVDK
HYELLEKIGLPTIIPDGISVEAILEVIRYDNKRGYIKADADTIRMVLLEKLGKPANPDGDYLTPVPEEIV
KEALE
>gnl|CDD|341477 cd08198, DHQS-like, Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis. This family contains dehydroquinate synthase-like proteins. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. The activity of DHQS requires NAD as cofactor. Proteins of this family share sequence similarity and functional motifs with that of dehydroquinate synthase, but the specific function has not been characterized
SYPVCFTHDLFSPDNPLLRALLVRRGPGRRHRVLFVIDSGVAAAHPALVKQIERYFQAHPDRLELVAPPL
IVPGGEAVKNDPALVEEILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQND
SGVGVKNGINFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLERNAAA
LRQRDPDAMEKLIRRCAELHLDHIAASGDPFETGSARPLDFGHWSAHKLEQLSGYALRHGEAVAIGIALD
SLYARLLGLLSREDFDRILALLQNLGLPLWHPLLERDGVLELLDGLEEFREHLGGRLTITLLRGIGVGVE
VHEIDLDLMEEAIDEL
>gnl|CDD|341478 cd08199, EEVS, 2-epi-5-epi-valiolone synthase (EEVS). 2-epi-5-epi-valiolone synthase catalyzes the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications. Validamycin A is an antifungal antibiotic which has a strong trehalase inhibitory activity and has been used to control sheath blight disease in rice caused by Rhizoctonia solani. Acarbose is an alpha-glucosidase inhibitor used for the treatment of type II insulin-independent diabetes. Salbostatin produced by Streptomyces albus also belongs to this family. It exhibits strong trehalase inhibitory activity
SYDVVLVDDLFDPENPTLADAYGRPGRRRLVVVDENVDRLYGARIRAYFAAHGIEATILVLPGGEANKTM
ETVLRIVDALDDFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFG
GHKNRLGAYYPPVATLLDRSFLKTLPRRHIRNGLAEIIKMALVKDAELFELLEEHGAALVETRFFQDEVA
DEIIRRAIQGMLEELAPNLWEHDLERLVDFGHTFSPILEMAAAPELLHGEAVAIDMALSAVLAYRRGLLS
EEELDRILRLMRRLGLPVWHPLCTPDLLWRALEDIVKHRDGLQRLPLPKGIGECVFVNDVTEEELERAL
>gnl|CDD|173828 cd08200, catalase_peroxidase_2, C-terminal non-catalytic domain of catalase-peroxidases. This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear
DPIPAVDYELIDDADIAALKAKILASGLTVSELVSTAWASASTFRNSDKRGGANGARIRLAPQKDWEVNE
PEELAKVLAVLEGIQKEFNESQSGGKKVSLADLIVLGGCAAVEKAAKDAGVDIKVPFTPGRTDATQEQTD
VESFEVLEPKADGFRNYLKKGYRVPPEEMLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRP
GVLTNDFFVNLLDMSTEWKPADEDDGLFEGRDRKTGEVKWTATRVDLVFGSNSELRAVAEVYASDDAQEK
FVKDFVAAWTKVMNLDR
>gnl|CDD|173829 cd08201, plant_peroxidase_like_1, Uncharacterized family of plant peroxidase-like proteins. This is a subgroup of heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX) which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions
WPSQIDELEDILYLQSGYSARGFVAGVTPCTDCAPGPGRQAAAEWLRTAFHDMATHNVDDGTGGLDASIQ
YELDRPENIGSGFNTTLNFFVNFYSPRSSMADLIAMGVVTSVASCGGPVVPFRAGRIDATEAGQAGVPEP
QTDLGTTTESFRRQGFSTSEMIALVACGHTLGGVHSEDFPEIVPPGSVPDTVLQFFDTTIQFDNKVVTEY
LSGTTNNPLVVGPNNTTNSDLRIFSSDGNVTMNELASPDTFQKTCADILQRMID
>gnl|CDD|188876 cd08203, SAM_PNT, Sterile alpha motif (SAM)/Pointed domain. Sterile alpha motif (SAM)/Pointed domain is found in about 40% of transcriptional regulators of ETS family (initially named for Erythroblastosis virus, E26-E Twenty Six). SAM Pointed domain containing proteins of this family additionally have a C-terminal ETS DNA-binding domain. In a few cases, SAM Pointed domain appears as a single domain protein. Members of this group are mostly involved in regulation of embryonic development and growth control in eukaryotes. SAM Pointed domains mediate protein-protein interactions. Depending on the subgroup, they can interact with other SAM Pointed domains forming homo or hetero dimers/oligomers and/or they can recruit a protein kinase to its target which can be a SAM Pointed domain containing protein itself or another protein that has no kinase docking site. Thus, SAM Pointed domains participate in transcriptional regulation and signal transduction. Some genes coding ETS family transcriptional regulators are proto-oncogenes. They are prone to chromosomal translocations resulting in gene fusions. Chimeric proteins with SAM Pointed domains were found in a number of different human tumors including myeloid leukemia, lymphoblastic leukemia, Ewing's sarcoma and primitive neuroectodermal tumor. Members of this family are potential targets for cancer therapy
DPLEWTPEHVQQWLSWVSKKFSLDPIDPDRFPMNGKELCALSKEDFRERAPSRGGDVLASHLALLRK
>gnl|CDD|350058 cd08204, ArfGap, GTPase-activating protein (GAP) for the ADP ribosylation factors (ARFs). ArfGAPs are a family of proteins containing an ArfGAP catalytic domain that induces the hydrolysis of GTP bound to the small guanine nucleotide-binding protein Arf, a member of the Ras superfamily of GTPases. Like all GTP-binding proteins, Arf proteins function as molecular switches, cycling between GTP (active-membrane bound) and GDP (inactive-cytosolic) form. Conversion to the GTP-bound form requires a guanine nucleotide exchange factor (GEF), whereas conversion to the GDP-bound form is catalyzed by a GTPase activating protein (GAP). In that sense, ArfGAPs were originally proposed to function as terminators of Arf signaling, which is mediated by regulating Arf family GTP-binding proteins. However, recent studies suggest that ArfGAPs can also function as Arf effectors, independently of their GAP enzymatic activity to transduce signals in cells. The ArfGAP domain contains a C4-type zinc finger motif and a conserved arginine that is required for activity, within a specific spacing (CX2CX16CX2CX4R). ArfGAPs, which have multiple functional domains, regulate the membrane trafficking and actin cytoskeleton remodeling via specific interactions with signaling lipids such as phosphoinositides and trafficking proteins, which consequently affect cellular events such as cell growth, migration, and cancer invasion. The ArfGAP family, which includes 31 human ArfGAP-domain containing proteins, is divided into 10 subfamilies based on domain structure and sequence similarity. The ArfGAP nomenclature is mainly based on the protein domain structure. For example, ASAP1 contains ArfGAP, SH3, ANK repeat and PH domains; ARAPs contain ArfGAP, Rho GAP, ANK repeat and PH domains; ACAPs contain ArfGAP, BAR (coiled coil), ANK repeat and PH domains; and AGAPs contain Arf GAP, GTP-binding protein-like, ANK repeat and PH domains. Furthermore, the ArfGAPs can be classified into two major types of subfamilies, according to the overall domain structure: the ArfGAP1 type includes 6 subfamilies (ArfGAP1, ArfGAP2/3, ADAP, SMAP, AGFG, and GIT), which contain the ArfGAP domain at the N-terminus of the protein; and the AZAP type includes 4 subfamilies (ASAP, ACAP, AGAP, and ARAP), which contain an ArfGAP domain between the PH and ANK repeat domains
LEELLKLPGNKVCADCGAPDPRWASINLGVFICIRCSGIHRSLGVHISKVRSLTLDSWTPEQVELMKAIG
NARANAYYEANLPPGFKKPTPDSSDEEREQFIRAKY
>gnl|CDD|173970 cd08205, RuBisCO_IV_RLP, Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV. Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions, like for example 2,3-diketo-5-methylthiopentyl-1-phosphate enolase or 5-methylthio-d-ribulose 1-phosphate isomerase
ITATYRIEAPGADAEKKAEAIALEQTVGTWTELPGETEEIRERHVGRVESIEELEESEGKYGRARVTISY
PLDNFGGDLPQLLNTLFGNLSLLPGIKLVDLELPDSLLAAFPGPRFGIEGLRRLLGVHDRPLLGTIIKPS
IGLSPEELAELAYELALGGIDLIKDDELLADQPYAPFEERVRACMEAVRRANEETGRKTLYAPNITGDPD
ELRRRADRAVEAGANALLINPNLVGLDALRALAEDPDLPIMAHPAFAGALSRSPDYGSHFLLLGKLMRLA
GADAVIFPGPGGRFPFSREECLAIARACRRPLGGIKPALPVPSGGMHPGRVPELYRDYGPDVILLAGGGI
LGHPDGAAAGVRAFRQA
>gnl|CDD|173971 cd08206, RuBisCO_large_I_II_III, Ribulose bisphosphate carboxylase large chain, Form I,II,III. Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubico-like proteins (RLP), are missing critical active site residues
TDLLAAFRMTPAEGVDPEEAAAAVAAESSTGTWTTVWTDRLTATERLKAKVYRIDPVPDGQYIAKIAYPL
DLFEEGSVPNLLTSIIGNVFGMKAVKALRLEDFRFPPAYLKTFDGPSFGIQGEREILGKYGRPLLGTIVK
PKLGLSPKEYARVVYEALRGGLDFVKDDENQNSQPFMRFEDRILFVAEAMDKAEAETGEAKGHYLNITAD
TPEEMIKRAEFAKELGSVIVMVDGVTAGWTAIQSARRWCPDNGLALHAHRAGHAAFTRQKNHGISMRVLA
KLARLIGVDHIHTGTVVGKLEGDPSEVKGIADMLREDEVEGDLSRIFFNQDWGGMKPVFPVASGGLHPGR
MPALIEILGDDVILQFGGGTHGHPDGPAAGAKANRQALEAWVQGRILREYAKTHKELAAALEKW
>gnl|CDD|173972 cd08207, RLP_NonPhot, Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria. Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions. The specific function of this subgroup is unknown
RITATYLIETPLDLERAAEVIAGEQSSGTFIALPGETDELKERSAARVESIEELETAAQPSLPRRASGGP
YTRARVTISFPLDNIGTSLPNLLATVAGNLFELRELSGLRLVDLGLPDEFAAAFPGPAFGIAGTRRLTGV
EDRPLIGTIIKPSVGLTPEETAALVRQLAAAGIDFIKDDELLANPPYSPLDERVRAVMRVINDHAQRTGR
KVMYAFNITDDIDEMRRNHDLVVEAGGTCVMVSLNSVGLSGLAALRRHSQLPIHGHRNGWGMLTRSPALG
ISFQAYQKLWRLAGVDHLHVNGLASKFWESDDSVIESARACLTPLGGPDDAAMPVFSSGQWGGQAPPTYR
RLGSVDLLYLAGGGIMAHPDGPAAGVRSLRQAWEAAVAGVPLEEYAKTHPELARAL
>gnl|CDD|173973 cd08208, RLP_Photo, Ribulose bisphosphate carboxylase like proteins from phototrophic bacteria. Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions. The specific function of this subgroup is unknown
DVAGFFASRASLDMEQYLVLDYYLECVGDPETAAAHFCSEQSTAQWRRVGVDEDFRPRFAAKVIDLEVIE
ELEQLSYPVKHSETGPVHACRVTIAHPHGNFGPKIPNLLSAVCGEGTFFSPGVPVVKLMDIHFPETYLAD
FEGPKFGIAGLRERLQAHDRPIFFGVIKPNIGLPPGEFAELGYQSWLGGLDIAKDDEMLADVDWCPLEER
AALLGKARRRAEAETGVPKIYLANITDEVDRLMELHDVAVRNGANALLINAMPVGLSAVRMLRKHAQVPL
IAHFPFIASFSRLEKYGIHSRVMTKLQRLAGLDVVIMPGFGPRMMTPEEEVLECVIACLEPMGPIKPCLP
VPGGSDSALTLQTVYEKVGNVDFGFVPGRGVFGHPMGPKAGAKSIRQAWEAIEAGISIETWAETHPELQA
AVDA
>gnl|CDD|173974 cd08209, RLP_DK-MTP-1-P-enolase, 2,3-diketo-5-methylthiopentyl-1-phosphate enolase. Ribulose bisphosphate carboxylase like proteins (RLPs) similar to B. subtilis YkrW protein, have been identified as 2,3-diketo-5-methylthiopentyl-1-phosphate enolases. They catalyze the tautomerization of 2,3-diketo-5-methylthiopentane 1-phosphate (DK-MTP 1-P). This is an important step in the methionine salvage pathway in which 5-methylthio-D-ribose (MTR) derived from 5'-methylthioadenosine is converted to methionine
IVATYRFPDGADLEKKAEQIAVGLTVGSWTDLPALRQAQLQKHLGEVVSVEELEEGRGVITIAYPLINVS
GDIPALLTTIFGKLSLDGKIKLVDLRLPEEFGRAFPGPKFGIEGIRQRLGVHDRPLLMSIFKGVLGLDLD
DLAEQLREQALGGVDLIKDDEILFDNPLAPALERIRACRPVLQEVYEQTGRRTLYAVNLTGPVFTLKEKA
RRLVEAGANALLFNVFAYGLDVLEALASDPEINVPIFAHPAFAGALYGSPDYGIAASVLLGTLMRLAGAD
AVLFPSPYGSVALSKEEALAIAEALRRGGAFKGVFPVPSAGIHPGLVPQLLRDFGTDVILNAGGGIHGHP
DGAAAGVRAFREAIDAVLAGESLEPAAIPDGPLKSALDKWG
>gnl|CDD|173975 cd08210, RLP_RrRLP, Ribulose bisphosphate carboxylase like proteins (RLPs) similar to R.rubrum RLP. RLP from Rhodospirillum rubrum plays a role in an uncharacterized sulfur salvage pathway and has been shown to catalyze a novel isomerization reaction that converts 5-methylthio-d-ribulose 1-phosphate to a 3:1 mixture of 1-methylthioxylulose 5-phosphate and 1-methylthioribulose 5-phosphate
RFRVTYRLVAASEAEAEARARGIALEQTVEMPLELVPDGYIRDNIVGRVESLEPAGEGSYRARISYSVDT
AGGELTQLLNVLFGNSSLQPGIRLVDFELPPSLLRRFPGPRFGIAGLRALLGIPERPLLCSALKPQGLSA
AELAELAYAFALGGIDIIKDDHGLADQPFAPFEERVKACQEAVAEANAETGGRTLYAPNVTGPPTQLLER
ARFAKEAGAGGVLIAPGLTGLDTFRELAEDFDFLPILAHPAFAGAFVSSGDGISHALLFGTLFRLAGADA
VIFPNYGGRFGFSREECQAIADACRRPMGGLKPILPAPGGGMSVERAPEMVELYGPDVMLLIGGSLLRAG
DDLTENTRAFVEAV
>gnl|CDD|173976 cd08211, RuBisCO_large_II, Ribulose bisphosphate carboxylase large chain, Form II. Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form II is mainly found in bacteria, and forms large subunit oligomers (dimers, tetramers, etc.) that do not include small subunits
DQSSRYADLDLKEEDLIAGGEHVLVAYIMKPKAGYGYLATAAHFAAESSTGTNVEVSTTDDFTRGVDALV
YEIDEARELMKIAYPVELFDRNLTDGRAMVASFLTLIIGNNQGMGDVEYLKMHDFYVPESMLELFDGPSV
NISDMWKVLGRPEVDGGYIAGTIIKPKLGLRPKPFAEACYAFWLGGDFIKNDEPQANQPFCPLKKVIPLV
ADAMRRAQDETGEAKLFSANITADDPDEMIARGEYILEAFGPNAGHVAFLVDGYVAGPAAVTTARRRFPD
QFLHYHRAGHGAVTSPQSKRGYTAFVLSKMARLQGASGIHTGTMGFGKMEGESSDKVIAYMIERDEAQGP
LFNQKWYGMKPTTPIISGGMNALRLPGFFENLGNGNVILTAGGGSFGHIDGPAAGAKSLRQAYDAWKQGV
DVIEYAKEHKELARAFESF
>gnl|CDD|173977 cd08212, RuBisCO_large_I, Ribulose bisphosphate carboxylase large chain, Form I. Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I is the most abundant class, present in plants, algae, and bacteria, and forms large complexes composed of 8 large and 8 small subunits
GYWTPDYQPKDTDILAAFRITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPG
EENQYFAYIAYPLDLFEEGSVANLTTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRL
NKYGRPLLGCTIKPKLGLSAKNYGRVVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAET
GEVKGHYLNVTAGTMEEMYKRAEFAKELGSPIIMHDLLTGFTAIQSLAKWCRDNGMLLHLHRAGHATYDR
QKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVTLGFYDLLRDDYIEKDRSRGIFFTQDWASLPG
VMPVASGGIHVGQMHQLIEIFGDDVVLQFGGGTIGHPWGIAAGATANRVALEAMVQARNEGRDLAREGPE
ILREAAKWSPELAAALETWKDIKFEFESTD
>gnl|CDD|173978 cd08213, RuBisCO_large_III, Ribulose bisphosphate carboxylase large chain, Form III. Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form III is only found in archaea and forms large subunit oligomers (dimers or decamers) that do not include small subunits
DDLIAVFRIEPAEGISIEEAAGRVASESSIGTWTTLATLYPERAEKLKAKAYYFDGLGGSYIVKVAYPLE
LFEEGNMPQLLSSIAGNIFGMKAVKNLRLEDIYFPESYLREFKGPQFGIEGVREILGIKDRPLLGTVPKP
KVGLSPEEHAEVAYEALVGGVDLVKDDENLTSQPFNRFEERAKESLKARDKAEAETGERKAYLANITAPV
REMERRAELVADLGGKYVMIDVVVAGWSALQYLRDLAEDYGLAIHAHRAMHAAFTRNPRHGISMLVLAKL
YRLIGVDQLHIGTAVGKMEGDKEEVLRIADILREQKYKPDEEDFHLAQDWGGIKPVFPVASGGLHPGLVP
DVIDILGKDIVIQVGGGVHGHPDGTRAGAKAVRQAIEAALEGISLDEYAKDHKELARALEKW
>gnl|CDD|270855 cd08215, STKc_Nek, Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEE
NGKLCIVMEYADGGDLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDG
VVKLGDFGISKVLESTTDLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPA
LVYKIVKGQYPPIPSQYSSELRDLVNSMLQKDPEKRPSANEILSSPFI
>gnl|CDD|270856 cd08216, PK_STRAD, Pseudokinase domain of STE20-related kinase adapter protein. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ELLYEIGKCFKGGGVVHLAKHKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVV
DNDLYVVTPLMAYGSCRDLLKTHFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKV
VLSGLRYAYSMVKHGKRQRVVHDFPKSSEKNLPWLSPEVLQQNLLGYNEKSDIYSVGITACELANGVVPF
SDMPATQMLLEKVRGTTPQLLDCSTYPLEEDSMSQSEDSSTEHPNNRDTRDIPYQRTFSEAFHQFVELCL
QRDPELRPSASQLLAHSFFKQCRRSNTSLLDLLKP
>gnl|CDD|270857 cd08217, STKc_Nek2, Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIVRYYDRIVD
RANTTLYIVMEYCEGGDLAQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHNRSVGGGKILHRDLKPAN
IFLDSDNNVKLGDFGLARVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPF
QAANQLELAKKIKEGKFPRIPSRYSSELNEVIKSMLNVDPDKRPSVEELLQLPLI
>gnl|CDD|270858 cd08218, STKc_Nek1, Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEE
NGNLYIVMDYCDGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGII
KLGDFGIARVLNSTVELARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLV
LKIIRGSYPPVPSRYSYDLRSLVSQLFKRNPRDRPSINSILEKPFI
>gnl|CDD|173759 cd08219, STKc_Nek3, Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEAD
GHLYIVMEYCDGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVK
LGDFGSARLLTSPGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLIL
KVCQGSYKPLPSHYSYELRSLIKQMFKRNPRSRPSATTILSRGSL
>gnl|CDD|270859 cd08220, STKc_Nek8, Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLE
DKALMIVMEYAPGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTV
VKIGDFGISKILSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALV
LKIMRGTFAPISDRYSEELRHLILSMLHLDPNKRPTLSEIMAQPII
>gnl|CDD|270860 cd08221, STKc_Nek9, Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HYIPVRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLD
GESLFIEMEYCNGGNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLV
KLGDFGISKVLDSESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLA
VKIVQGEYEDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLERPLL
>gnl|CDD|270861 cd08222, STKc_Nek11, Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEISVGELQPDETVDANREAKLLSKLDHPAIVKFHDS
FVEKESFCIVTEYCEGGDLDDKISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLK
NNVIKVGDFGISRILMGTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNL
LSVMYKIVEGETPSLPDKYSKELNAIYSRMLNKDPALRPSAAEILKIPFI
>gnl|CDD|270862 cd08223, STKc_Nek4, Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEG
EDGFLYIVMGFCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNI
IKVGDLGIARVLESSSDMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSL
VYKILEGKLPPMPKQYSPELGELIKAMLHQDPEKRPSVKRILRQPYI
>gnl|CDD|270863 cd08224, STKc_Nek6_7, Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFI
ENNELNIVLELADAGDLSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITAN
GVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMN
LYSLCKKIEKCEYPPLPADLYSQELRDLVAACIQPDPEKRPDISYVLDVAKR
>gnl|CDD|173765 cd08225, STKc_Nek5, Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQE
NGRLFIVMEYCDGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMV
AKLGDFGIARQLNDSMELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQL
VLKICQGYFAPISPNFSRDLRSLISQLFKVSPRDRPSITSILKRPFL
>gnl|CDD|270864 cd08226, PK_STRAD_beta, Pseudokinase domain of STE20-related kinase adapter protein beta. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ELQVELGKGFCNLTSVYLARHTPTGTLVTVKITNLDNCSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTE
GSWLWVISPFMAYGSARGLLKTYFPEGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLV
SLSGLSHLYSMVTNGQRSKVVYDFPQFSTSVLPWLSPELLRQDLHGYNVKSDIYSVGITACELARGQVPF
QDMRRTQMLLQKLKGPPYSPLDIFPFPELESRMKNSQSGMDSGIGESVATSSMTRTMTSERLQTPSSKTF
SPAFHNLVELCLQQDPEKRPSASSLLSHSFFKQVKEQTQASLLSLLPP
>gnl|CDD|173767 cd08227, PK_STRAD_alpha, Pseudokinase domain of STE20-related kinase adapter protein alpha. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ELLTVIGRGFEDLMTVNLARYKPTGEYVTVRRINLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIA
DNELWVVTSFMAYGSAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKV
YLSGLRSNLSMINHGQRLRVVHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPF
KDMPATQMLLEKLNGTVPCLLDTTTIPAEELTMKPSRSGANSGLGESTTVSTPRPSNGESSSHPYNRTFS
PHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEALPELLRP
>gnl|CDD|270865 cd08228, STKc_Nek6, Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDS
FIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFIT
ATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDK
MNLFSLCQKIEQCDYPPLPTEHYSEKLRELVSMCIYPDPDQRPDIGYVHQIAKQMHVW
>gnl|CDD|270866 cd08229, STKc_Nek7, Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARAD
CIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPEKTVWKYFVQLCSA
LEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSD
IWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDITYV
YDVAKRMHARTA
>gnl|CDD|176192 cd08230, glucose_DH, Glucose dehydrogenase. Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossman fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability
MKAIAVKPGKPGVRVVDIPEPEPTPGEVLVRTLEVGVCGTDREIVAGEYGTAPPGEDFLVLGHEALGVVE
EVGDGSGLSPGDLVVPTVRRPPGKCLNCRIGRPDFCETGEYTERGIKGLHGFMREYFVDDPEYLVKVPPS
LADVGVLLEPLSVVEKAIEQAEAVQKRLPTWNPRRALVLGAGPIGLLAALLLRLRGFEVYVLNRRDPPDP
KADIVEELGATYVNSSKTPVAEVKLVGEFDLIIEATGVPPLAFEALPALAPNGVVILFGVPGGGREFEVD
GGELNRDLVLGNKALVGSVNANKRHFEQAVEDLAQWKYRWPGVLERLITRRVPLEEFAEALTEKPDGEIK
VVIEW
>gnl|CDD|176193 cd08231, MDR_TM0436_like, Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH). This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability
ARAAVLTGPGKPLEIREVPLPDLEPGAVLVRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALG
GGVTTDVAGEPLKVGDRVTWSVGAPCGRCYRCLVGDPTKCENRKKYGHEASCDDPHLSGGYAEHIYLPPG
TAIVRVPDNVPDEVAAPANCALATVLAALDRAGPVGAGDTVVVQGAGPLGLYAVAAAKLAGARRVIVIDG
SPERLELAREFGADATIDIDELPDPQRRAIVRDITGGRGADVVIEASGHPAAVPEGLELLRRGGTYVLVG
SVAPAGTVPLDPERIVRKNLTIIGVHNYDPSHLYRAVRFLERTQDRFPFAELVTHRYPLEDINEALELAE
SGTALKVVIDP
>gnl|CDD|176194 cd08232, idonate-5-DH, L-idonate 5-dehydrogenase. L-idonate 5-dehydrogenase (L-ido 5-DH) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
CVIHAAGDLRVEERPAPEPGPGEVRVRVAAGGICGSDLHYYQHGGFGTVRLREPMVLGHEVSGVVEAVGP
GVTGLAPGQRVAVNPSRPCGTCDYCRAGRPNLCLNMRFLGSAMRFPHVQGGFREYLVVDASQCVPLPDGL
SLRRAALAEPLAVALHAVNRAGDLAGKRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVARAMG
ADETVNLARDPLAAYAADKGDFDVVFEASGAPAALASALRVVRPGGTVVQVGMLGGPVPLPLNALVAKEL
DLRGSFRFDDEFAEAVRLLAAGRIDVRPLITAVFPLEEAAEAFALAADRTRSVKVQLSF
>gnl|CDD|176195 cd08233, butanediol_DH_like, (2R,3R)-2,3-butanediol dehydrogenase. (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit
MKAARYHGRKDIRVEEVPEPPVKPGEVKIKVAWCGICGSDLHEYLDGPIFIPTEGHPHLTGETAPVTLGH
EFSGVVVEVGSGVTGFKVGDRVVVEPTIKCGTCGACKRGLYNLCDSLGFIGLGGGGGGFAEYVVVPAYHV
HKLPDNVPLEEAALVEPLAVAWHAVRRSGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARR
ELAEELGATIVLDPTEVDVVAEVRKLTGGGGVDVSFDCAGVQATLDTAIDALRPRGTAVNVAIWEKPISF
NPNDLVLKEKTLTGSICYTREDFEEVIDLLASGKIDAEPLITSRIPLEDIVEKGFEELINDKEQHVKILV
S
>gnl|CDD|176196 cd08234, threonine_DH_like, L-threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose
MKALVYEGPGELEVEEVPVPEPGPDEVLIKVAACGICGTDLHIYEGEFGAAPPLVPGHEFAGVVVAVGSK
VTGFKVGDRVAVDPNIYCGECFYCRRGRPNLCENLTAVGVTRNGGFAEYVVVPAKQVYKIPDNLSFEEAA
LAEPLSCAVHGLDLLGIKPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAKKLGATETVD
PSREDPEAQKEDNPYGFDVVIEATGVPKTLEQAIEYARRGGTVLVFGVYAPDARVSISPFEIFQKELTII
GSFINPYTFPRAIALLESGKIDVKGLVSHRLPLEEVPEALEGMRSGGALKVVVV
>gnl|CDD|176197 cd08235, iditol_2_DH_like, L-iditol 2-dehydrogenase. Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MKAAVLHGPNDVRLEEVPVPEPGPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGD
GVTGFKVGDRVFVAPHVPCGECHYCLRGNENMCPNYKKFGNLYDGGFAEYVRVPAWAVKRGGVLKLPDNV
SFEEAALVEPLACCINAQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGARKVIVSDLNEFRLEFAKKLG
ADYTIDAAEEDLVEKVRELTDGRGADVVIVATGSPEAQAQALELVRKGGRILFFGGLPKGSTVNIDPNLI
HYREITITGSYAASPEDYKEALELIASGKIDVKDLITHRFPLEDIEEAFELAADGKSLKIVIT
>gnl|CDD|176198 cd08236, sugar_DH, NAD(P)-dependent sugar dehydrogenases. This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex
MKALVLTGPGDLRYEDIPKPEPGPGEVLVKVKACGICGSDIPRYLGTGAYHPPLVLGHEFSGTVEEVGSG
VDDLAVGDRVAVNPLLPCGKCEYCKKGEYSLCSNYDYIGSRRDGAFAEYVSVPARNLIKIPDHVDYEEAA
MIEPAAVALHAVRLAGITLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVARELGADDTIN
PKEEDVEKVRELTEGRGADLVIEAAGSPATIEQALALARPGGKVVLVGIPYGDVTLSEEAFEKILRKELT
IQGSWNSYSAPFPGDEWRTALDLLASGKIKVEPLITHRLPLEDGPAAFERLADREEFSGKVLL
>gnl|CDD|176199 cd08237, ribitol-5-phosphate_DH, ribitol-5-phosphate dehydrogenase. NAD-linked ribitol-5-phosphate dehydrogenase, a member of the MDR/zinc-dependent alcohol dehydrogenase-like family, oxidizes the phosphate ester of ribitol-5-phosphate to xylulose-5-phosphate of the pentose phosphate pathway. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability
MINQVYRLVRPKFFEVTYEEENLREDWVIVRPTYLSICHADQRYYQGNRSPEALKKKLPMALIHEGIGVV
VSDPTGTYKVGTKVVMVPNTPVEKDEIIPENYLPSSRFRSSGYDGFMQDYVFLPPDRLVKLPDNVDPEVA
AFTELVSVGVHAISRFEQIAHKDRNVIGVWGDGNLGYITALLLKQIYPESKLVVFGKHQEKLDLFSFADE
TYLIDDIPEDLAVDHAFECVGGRGSQSAINQIIDYIRPQGTIGLMGVSEYPVPINTRMVLEKGLTLVGSS
RSTREDFERAVELLSRNPEVAEYLRKLVGGVFPVRSINDIHRAFESDLTNSWGKTVMEWEV
>gnl|CDD|176200 cd08238, sorbose_phosphate_red, L-sorbose-1-phosphate reductase. L-sorbose-1-phosphate reductase, a member of the MDR family, catalyzes the NADPH-dependent conversion of l-sorbose 1-phosphate to d-glucitol 6-phosphate in the metabolism of L-sorbose to (also converts d-fructose 1-phosphate to d-mannitol 6-phosphate). The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability
MKTKAWRMYGKGDLRLEKFELPEIADDEILVRVISDSLCFSTWKLALQGSDHKKVPNDLAKEPVILGHEF
AGTILKVGKKWQGKYKPGQRFVIQPALILPDGPSCPGYSYTYPGGLATYHIIPNEVMEQDCLLIYEGDGY
AEASLVEPLSCVIGAYTANYHLQPGEYRHRMGIKPGGNTAILGGAGPMGLMAIDYAIHGPIGPSLLVVTD
VNDERLARAQRLFPPEAASRGIELLYVNPATIDDLHATLMELTGGQGFDDVFVFVPVPELVEEADTLLAP
DGCLNFFAGPVDKNFSAPLNFYNVHYNNTHYVGTSGGNTDDMKEAIDLMAAGKLNPARMVTHIGGLNAAA
ETTLNLPGIPGGKKLIYTQKPLPLTGIEELADKEPEEPAAIVLENGGIWNKEAEEYLLEN
>gnl|CDD|176201 cd08239, THR_DH_like, L-threonine dehydrogenase (TDH)-like. MDR/AHD-like proteins, including a protein annotated as a threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Zinc-dependent ADHs are medium chain dehydrogenase/reductase type proteins (MDRs) and have a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. In addition to alcohol dehydrogenases, this group includes quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MRGAVFPGDRTVELREFPVPVPGPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQGVIPGHEPAGVVVAVG
PGVTHFRVGDRVMVYHYVGCGACRNCRRGWMQLCTSKRAAYGWNRDGGHAEYMLVPEKTLIPLPDDLSFA
DGALLLCGIGTAYHALRRVGVSGRDTVLVVGAGPVGLGALMLARALGAEDVIGVDPSPERLELAKALGAD
FVINSGQDDVQEIRELTSGAGADVAIECSGNTAARRLALEAVRPWGRLVLVGEGGELTIEVSNDLIRKQR
TLIGSWYFSVPDMEECAEFLARHKLEVDRLVTHRFGLDQAPEAYALFAQGESGKVVFVF
>gnl|CDD|176202 cd08240, 6_hydroxyhexanoate_dh_like, 6-hydroxyhexanoate dehydrogenase. 6-hydroxyhexanoate dehydrogenase, an enzyme of the zinc-dependent alcohol dehydrogenase-like family of medium chain dehydrogenases/reductases catalyzes the conversion of 6-hydroxyhexanoate and NAD(+) to 6-oxohexanoate + NADH and H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MKAAAVVEPGKPLEEVEIDTPKPPGTEVLVKVTACGVCHSDLHIWDGGYDLGGGKTMSLDDRGVKLPLVL
GHEIVGEVVAVGPDAADVKVGDKVLVYPWIGCGECPVCLAGDENLCAKGRALGIFQDGGYAEYVIVPHSR
YLVDPGGLDPALAATLACSGLTAYSAVKKLMPLVADEPVVIIGAGGLGLMALALLKALGPANIIVVDIDE
AKLEAAKAAGADVVVNGSDPDAAKRIIKAAGGGVDAVIDFVNNSATASLAFDILAKGGKLVLVGLFGGEA
TLPLPLLPLRALTIQGSYVGSLEELRELVALAKAGKLKPIPLTERPLSDVNDALDDLKAGKVVGRAVLKP
>gnl|CDD|176203 cd08241, QOR1, Quinone oxidoreductase (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MKAVVCKELGGPEDLVLEEVPPEPGAPGEVRIRVEAAGVNFPDLLMIQGKYQVKPPLPFVPGSEVAGVVE
AVGEGVTGFKVGDRVVALTGQGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRRARLQPG
ETVLVLGAAGGVGLAAVQLAKALGARVIAAASSEEKLALARALGADHVIDYRDPDLRERVKALTGGRGVD
VVYDPVGGDVFEASLRSLAWGGRLLVIGFASGEIPQIPANLLLLKNISVVGVYWGAYARREPELLRANLA
ELFDLLAEGKIRPHVSAVFPLEQAAEALRALADRKATGKVVLT
>gnl|CDD|176204 cd08242, MDR_like, Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family, including threonine dehydrogenase. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MKALVLDGGLDLRVEDLPKPEPPPGEALVRVLLAGICNTDLEIYKGYYPFPGVPGHEFVGIVEEGPEAEL
VGKRVVGEINIACGRCEYCRRGLYTHCPNRTVLGIVDRDGAFAEYLTLPLENLHVVPDLVPDEQAVFAEP
LAAALEILEQVPITPGDKVAVLGDGKLGLLIAQVLALTGPDVVLVGRHSEKLALARRLGVETVLPDEAES
EGGGFDVVVEATGSPSGLELALRLVRPRGTVVLKSTYAGPASFDLTKAVVNEITLVGSRCGPFAPALRLL
RKGLVDVDPLITAVYPLEEALEAFERAAEPGALKVLLRP
>gnl|CDD|176205 cd08243, quinone_oxidoreductase_like_1, Quinone oxidoreductase (QOR). NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit
MKAIVIEQPGGPEVLKLREIPIPEPKPGWVLIRVKAFGLNRSEIFTRQGHSPSVKFPRVLGIEAVGEVEE
APGGTFTPGQRVATAMGGMGRTFDGSYAEYTLVPNEQVYAIDSDLSWAELAALPETYYTAWGSLFRSLGL
QPGDTLLIRGGTSSVGLAALKLAKALGATVTATTRSPERAALLKELGADEVVIDDGAIAEQLRAAPGGFD
KVLELVGTATLKDSLRHLRPGGIVCMTGLLGGQWTLEDFNPMDDIPSGVNLTLTGSSSGDVPQTPLQELF
DFVAAGHLDIPPSKVFTFDEIVEAHAYMESNRAFGKVVVL
>gnl|CDD|176206 cd08244, MDR_enoyl_red, Possible enoyl reductase. Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain
MRAIRLHEFGPPEVLVPEDVPDPVPGPGQVRIAVAAAGVHFVDTQLRSGWGPGPFPPELPYVPGGEVAGV
VDAVGPGVDPAWLGRRVVAHTGRAGGGYAELAVADVDSLHPVPDGLDLEAAVAVVHDGRTALGLLDLATL
TPGDVVLVTAAAGGLGSLLVQLAKAAGATVVGAAGGPAKTALVRALGADVAVDYTRPDWPDQVREALGGG
GVTVVLDGVGGAIGRAALALLAPGGRFLTYGWASGEWTALDEDDARRRGVTVVGLLGVQAERGGLRALEA
RALAEAAAGRLVPVVGQTFPLERAAEAHAALEARSTVGKVLLLP
>gnl|CDD|176207 cd08245, CAD, Cinnamyl alcohol dehydrogenases (CAD) and related proteins. Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes, or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
KAAVVHAAGGPLEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGA
GVEGRKVGDRVGVGWLVGSCGRCEYCRRGLENLCQKAVNTGYTTQGGYAEYMVADAEYTVLLPDGLPLAQ
AAPLLCAGITVYSALRDAGPRPGERVAVLGIGGLGHLAVQYARAMGFETVAITRSPDKRELARKLGADEV
VDSGAELDEQAAAGGADVILVTVVSGAAAEAALGGLRRGGRIVLVGLPESPPFSPDIFPLIMKRQSIAGS
THGGRADLQEALDFAAEGKVKPMIETFPLDQANEAYERMEKGDVRFRFVL
>gnl|CDD|176208 cd08246, crotonyl_coA_red, crotonyl-CoA reductase. Crotonyl-CoA reductase, a member of the medium chain dehydrogenase/reductase family, catalyzes the NADPH-dependent conversion of crotonyl-CoA to butyryl-CoA, a step in (2S)-methylmalonyl-CoA production for straight-chain fatty acid biosynthesis. Like enoyl reductase, another enzyme in fatty acid synthesis, crotonyl-CoA reductase is a member of the zinc-dependent alcohol dehydrogenase-like medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES
GTLPPLGVVPEKMYAFAIRPERYGDPAQAIQLEDVPVPELGPGEVLVAVMAAGVNYNNVWAALGEPVSTF
AARQRRGRDEPYHIGGSDASGIVWAVGEGVKNWKVGDEVVVHCSVWDGNDPERAGGDPMFDPSQRIWGYE
TNYGSFAQFALVQATQLMPKPKHLSWEEAAAYMLVGATAYRMLFGWNPNTVKPGDNVLIWGASGGLGSMA
IQLARAAGANPVAVVSSEEKAEYCRALGAEGVINRRDFDHWGVLPDVNSEAYTAWTKEARRFGKAIWDIL
GGREDPDIVFEHPGRATFPTSVFVCDRGGMVVICAGTTGYNHTYDNRYLWMRQKRIQGSHFANDREAAEA
NRLVMKGRIDPCLSKVFSLDETPDAHQLMHRNQHHVGNMAVLV
>gnl|CDD|176209 cd08247, AST1_like, AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast. This group contains members identified in targeting of yeast membrane proteins ATPase. AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast, identified as a multicopy suppressor of pma1 mutants which cause temperature sensitive growth arrest due to the inability of ATPase to target to the cell surface. This family is homologous to the medium chain family of dehydrogenases and reductases. Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES
YKALTFKNNTSPLTITTIKLPLPNCYKDNEIVVKVHAAALNPVDLKLYNSYTFHFKVKEKGLGRDYSGVI
VKVGSNVASEWKVGDEVCGIYPHPYGGQGTLSQYLLVDPKKDKKSITRKPENISLEEAAAWPLVLGTAYQ
ILEDLGQKLGPDSKVLVLGGSTSVGRFAIQLAKNHYNIGTVVGTCSSRSAELNKKLGADHFIDYDAHSGV
KLLKPVLENVKGQGKFDLILDCVGGYDLFPHINSILKPKSKNGHYVTIVGDYKANYKKDTFNSWDNPSAN
ARKLFGSLGLWSYNYQFFLLDPNADWIEKCAELIADGKVKPPIDSVYPFEDYKEAFERLKSNRAKGKVVI
KV
>gnl|CDD|176210 cd08248, RTN4I1, Human Reticulon 4 Interacting Protein 1. Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES
MKAWQIHSYGGIDSLLLLENARIPVIRKPNQVLIKVHAASVNPIDVLMRSGYGRTLLNKKRKPQSCKYSG
IEFPLTLGRDCSGVVVDIGSGVKSFEIGDEVWGAVPPWSQGTHAEYVVVPENEVSKKPKNLSHEEAASLP
YAGLTAWSALVNVGGLNPKNAAGKRVLILGGSGGVGTFAIQLLKAWGAHVTTTCSTDAIPLVKSLGADDV
IDYNNEDFEEELTERGKFDVILDTVGGDTEKWALKLLKKGGTYVTLVSPLLKNTDKLGLVGGMLKSAVDL
LKKNVKSLLKGSHYRWGFFSPSGSALDELAKLVEDGKIKPVIDKVFPFEEVPEAYEKVESGHARGKTVIK
>gnl|CDD|176211 cd08249, enoyl_reductase_like, enoyl_reductase_like. Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain
QKAAVLTGPGGGLLVVVDVPVPKPGPDEVLVKVKAVALNPVDWKHQDYGFIPSYPAILGCDFAGTVVEVG
SGVTRFKVGDRVAGFVHGGNPNDPRNGAFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAALALFQKL
GLPLPPPKPSPASKGKPVLIWGGSSSVGTLAIQLAKLAGYKVITTASPKNFDLVKSLGADAVFDYHDPDV
VEDIRAATGGKLRYALDCISTPESAQLCAEALGRSGGGKLVSLLPVPEETEPRKGVKVKFVLGYTVFGEI
PEDREFGEVFWKYLPELLEEGKLKPHPVRVVEGGLEGVQEGLDLLRKGKVSGEKLVVRL
>gnl|CDD|176212 cd08250, Mgc45594_like, Mgc45594 gene product and other MDR family members. Includes Human Mgc45594 gene product of undetermined function. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES
SFRKLVVHRLSPNFREATSIVDVPVPLPGPGEVLVKNRFVGINASDINFTAGRYDPGVKPPFDCGFEGVG
EVVAVGEGVTDFKVGDAVATMSFGAFAEYQVVPARHAVPVPELKPEVLPLLVSGLTASIALEEVGEMKSG
ETVLVTAAAGGTGQFAVQLAKLAGCHVIGTCSSDEKAEFLKSLGCDRPINYKTEDLGEVLKKEYPKGVDV
VYESVGGEMFDTCVDNLALKGRLIVIGFISGYQSGTGPSPVKGATLPPKLLAKSASVRGFFLPHYAKLIP
QHLDRLLQLYQRGKLVCEVDPTRFRGLESVADAVDYLYSGKNIGKVVVE
>gnl|CDD|176213 cd08251, polyketide_synthase, polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding
EVAPPGPGEVRIQVRAFSLNFGDLLCVRGLYPTMPPYPFTPGFEASGVVRAVGPHVTRLAVGDEVIAGTG
ESMGGHATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFARAGLAKGEHILIQTATGGTGLMAVQL
ARLKGAEIYATASSDDKLEYLKQLGVPHVINYVEEDFEEEIMRLTGGRGVDVVINTLSGEAIQKGLNCLA
PGGRYVEIAMTALKSAPSVDLSVLSNNQSFHSVDLRKLLLLDPEFIADYQAEMVSLVEEGELRPTVSRIF
PFDDIGEAYRYLSDRENIGKVVV
>gnl|CDD|176214 cd08252, AL_MDR, Arginate lyase and other MDR family members. This group contains a structure identified as an arginate lyase. Other members are identified quinone reductases, alginate lyases, and other proteins related to the zinc-dependent dehydrogenases/reductases. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MKAIGFTQPLPITDPDSLIDIELPKPVPGGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKILGWDASGV
VEAVGSEVTLFKVGDEVYYAGDITRPGSNAEYQLVDERIVGHKPKSLSFAEAAALPLTSLTAWEALFDRL
GISEDAENEGKTLLIIGGAGGVGSIAIQLAKQLTGLTVIATASRPESIAWVKELGADHVINHHQDLAEQL
EALGIEPVDYIFCLTDTDQHWDAMAELIAPQGHICLIVDPQEPLDLGPLKSKSASFHWEFMFTRSMFQTP
DMIEQHEILNEVADLLDAGKLKTTLTETLGPINAENLREAHALLESGKTIGKIVLE
>gnl|CDD|176215 cd08253, zeta_crystallin, Zeta-crystallin with NADP-dependent quinone reductase activity (QOR). Zeta-crystallin is a eye lens protein with NADP-dependent quinone reductase activity (QOR). It has been cited as a structural component in mammalian eyes, but also has homology to quinone reductases in unrelated species. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MRAIRYHEFGAPDVLRLGDLPVPTPGPGEVLVRVHASGVNPVDTYIRAGAYPGLPPLPYVPGSDGAGVVE
AVGEGVDGLKVGDRVWLTNLGWGRRQGTAAEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYRALFHRA
GAKAGETVLVHGGSGAVGHAAVQLARWAGARVIATASSAEGAELVRQAGADAVFNYRAEDLADRILAATA
GQGVDVIIEVLANVNLAKDLDVLAPGGRIVVYGSGGLRGTIPINPLMAKEASIRGVLLYTATPEERAAAA
EAIAAGLADGALRPVIAREYPLEEAAAAHEAVESGGAIGKVVLDP
>gnl|CDD|176216 cd08254, hydroxyacyl_CoA_DH, 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members. This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MKAWRFHKGSKGLLVLEEVPVPEPGPGEVLVKVKAAGVCHSDLHILDGGVPTLTKLPLTLGHEIAGTVVE
VGAGVTNFKVGDRVAVPAVIPCGACALCRRGRGNLCLNQGMPGLGIDGGFAEYIVVPARALVPVPDGVPF
AQAAVATDAVLTPYHAVVRAGEVKPGETVLVIGLGGLGLNAVQIAKAMGAAVIAVDIKEEKLELAKELGA
DEVLNSLDDSPKDKKAAGLGGGFDVIFDFVGTQPTFEDAQKAVKPGGRIVVVGLGRDKLTVDLSDLIARE
LRIIGSFGGTPEDLPEVLDLIAKGKLDPQVETRPLDEIPEVLERLHKGKVKGRVVLVP
>gnl|CDD|176217 cd08255, 2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_like, 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members. This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability
DLVLDTALEGLSTGTEKLPLPLPPGYSSVGRVVEVGSGVTGFKPGDRVFCFGPHAERVVVPANLLVPLPD
GLPPERAALTALAATALNGVRDAEPRLGERVAVVGLGLVGLLAAQLAKAAGAREVVGVDPDAARRELAEA
LGPADPVAADTADEIGGRGADVVIEASGSPSALETALRLLRDRGRVVLVGWYGLKPLLLGEEFHFKRLPI
RSSQVYGIGRYDRPRRWTEARNLEEALDLLAEGRLEALITHRVPFEDAPEAYRLLFEDPPECLKVVL
>gnl|CDD|176218 cd08256, Zn_ADH2, Alcohol dehydrogenases of the MDR family. This group has the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenases of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability
MRAVVCHGPQDYRLEEVPVPRPGPGEILVKVEACGICAGDIKCYHGAPSFWGDENQPPYVKPPMIPGHEF
VGRVVELGEGAEERGVKVGDRVISEQIVPCWNCRFCNRGQYWMCQKHDLYGFQNNVNGGMAEYMRFPKEA
IVHKVPDDIPPEDAILIEPLACALHAVDRANIKFDDVVVLAGAGPLGLGMIGAARLKNPKKLIVLDLKDE
RLALARKFGADVVLNPPEVDVVEKIKELTGGYGCDIYIEATGHPSAVEQGLNMIRKLGRFVEFSVFGDPV
TVDWSIIGDRKELDVLGSHLGPYCYPIAIDLIASGRLPTDGIVTHQFPLEDFEEAFELMARGDDSIKVVL
>gnl|CDD|176219 cd08258, Zn_ADH4, Alcohol dehydrogenases of the MDR family. This group shares the zinc coordination sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MKALVKTGPGPGNVELREVPEPEPGPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEV
GPDVEGWKVGDRVVSETTFSTCGRCPYCRRGDYNLCPHRKGIGTQADGGFAEYVLVPEESLHELPENLSL
EAAALTEPLAVAVHAVAERSGIRPGDTVVVFGPGPIGLLAAQVAKLQGATVVVVGTEKDEVRLDVAKELG
ADAVNGGEEDLAELVNEITDGDGADVVIECSGAVPALEQALELLRKGGRIVQVGIFGPLAASIDVERIIQ
KELSVIGSRSSTPASWETALRLLASG
>gnl|CDD|176220 cd08259, Zn_ADH5, Alcohol dehydrogenases of the MDR family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MKAAILHKPNKPLQIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVG
EGVERFKPGDRVILYYYIPCGKCEYCLSGEENLCRNRAEYGEEVDGGFAEYVKVPERSLVKLPDNVSDES
AALAACVVGTAVHALKRAGVKKGDTVLVTGAGGGVGIHAIQLAKALGARVIAVTRSPEKLKILKELGADY
VIDGSKFSEDVKKLGGADVVIELVGSPTIEESLRSLNKGGRLVLIGNVTPDPAPLRPGLLILKEIRIIGS
ISATKADVEEALKLVKEGKIKPVIDRVVSLEDINEALEDLKSGKVVGRIVLK
>gnl|CDD|176221 cd08260, Zn_ADH6, Alcohol dehydrogenases of the MDR family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MRAAVYEEFGEPLEIREVPDPEPPPDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVG
EDVSRWRVGDRVTVPFVLGCGTCPYCRAGDSNVCEHQVQPGFTHPGSFAEYVAVPRADVNLVRLPDDVDF
VTAAGLGCRFATAFRALVHQARVKPGEWVAVHGCGGVGLSAVMIASALGARVIAVDIDDDKLELARELGA
VATVNASEVEDVAAAVRDLTGGGAHVSVDALGIPETCRNSVASLRKRGRHVQVGLTLGEEAGVALPMDRV
VARELEIVGSHGMPAHRYDAMLALIASGKLDPEPLVGRTISLDEAPDALAAMDDYATAGITVITD
>gnl|CDD|176222 cd08261, Zn_ADH7, Alcohol dehydrogenases of the MDR family. This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MKALVCEKPGRLEVVDIPEPVPGAGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGE
GVAGLKVGDRVVVDPYISCGECYACRKGRPNCCENLQVLGVHRDGGFAEYIVVPADALLVPEGLSLDQAA
LVEPLAIGAHAVRRAGVTAGDTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFARELGADDTINV
GDEDVAARLRELTDGEGADVVIDATGNPASMEEAVELVAHGGRVVLVGLSKGPVTFPDPEFHKKELTILG
SRNATREDFPDVIDLLESGKVDPEALITHRFPFEDVPEAFDLWEAPPGGVIKVLIEF
>gnl|CDD|176223 cd08262, Zn_ADH8, Alcohol dehydrogenases of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MRAAVFRDGPLVVRDVPDPEPGPGQVLVKVLACGICGSDLHATAHPEAMVDDAGGPSLMDLGADIVLGHE
FCGEVVDYGPGTERKLKVGTRVTSLPLLLCGQGASCGIGLSPEAPGGYAEYMLLSEALLLRVPDGLSMED
AALTEPLAVGLHAVRRARLTPGEVALVIGCGPIGLAVIAALKARGVGPIVASDFSPERRALALAMGADIV
VDPAADSPFAAWAAELARAGGPKPAVIFECVGAPGLIQQIIEGAPPGGRIVVVGVCMESDNIEPALAIRK
ELTLQFSLGYTPEEFADALDALAEGKVDVAPMVTGTVGLDGVPDAFEALRDPEHHCKILVD
>gnl|CDD|176224 cd08263, Zn_ADH10, Alcohol dehydrogenases of the MDR family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MKAAVLKGPNPPLTIEEIPVPRPKEGEILIRVAACGVCHSDLHVLKGELPFPPPFVLGHEISGEVVEVGP
NVENPYGLSVGDRVVGSFIMPCGKCRYCARGKENLCEDFFAYNRLKGTLYDGTTRLFRLDGGPVYMYSMG
GLAEYAVVPATALAPLPESLDYTESAVLGCAGFTAYGALKHAADVRPGETVAVIGVGGVGSSAIQLAKAF
GASPIIAVDVRDEKLAKAKELGATHTVNAAKEDAVAAIREITGGRGVDVVVEALGKPETFKLALDVVRDG
GRAVVVGLAPGGATAEIPITRLVRRGIKIIGSYGARPRQDLPELVGLAASGKLDPEALVTHKYKLEEINE
AYENLRKGLIHGRAIVE
>gnl|CDD|176225 cd08264, Zn_ADH_like2, Alcohol dehydrogenases of the MDR family. This group resembles the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase family. However, this subgroup does not contain the characteristic catalytic zinc site. Also, it contains an atypical structural zinc-binding pattern: DxxCxxCxxxxxxxC. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MKALVFEKSGIENLKVEDVKDPKPGPGEVLIRVKMAGVNPVDYNVINAVKVKPMPHIPGAEFAGVVEEVG
DHVKGVKKGDRVVVYNRVFDGTCDMCLSGNEMLCRNGGIIGVVSNGGYAEYIVVPEKNLFKIPDSISDEL
AASLPVAALTAYHALKTAGLGPGETVVVFGASGNTGIFAVQLAKMMGAEVIAVSRKDWLKEFGADEVVDY
DEVEEKVKEITKMADVVINSLGSSFWDLSLSVLGRGGRLVTFGTLTGGEVKLDLSDLYSKQISIIGSTGG
TRKELLELVKIAKDLKVKVWKTFKLEEAKEALKELFSKERDGRIL
>gnl|CDD|176226 cd08265, Zn_ADH3, Alcohol dehydrogenases of the MDR family. This group resembles the zinc-dependent alcohol dehydrogenase and has the catalytic and structural zinc-binding sites characteristic of this group. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc
RAAIVDAKWDPRPEYKLTPKEIEGKLTNLGSKVWRYPELRVEDVPVPNLKPDEILIRVKACGICGSDIHL
YETDKDGYILYPGLTEFPVVIGHEFSGVVEKTGKNVKNFEKGDPVTAEEMMWCGMCRACRSGSPNHCKNL
KELGFSADGAFAEYIAVNARYAWEINELREIYSEDKAFEAGALVEPTSVAYNGLFIRGGGFRPGAYVVVY
GAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGADYVFNPTKMRDCLSGEKVMEVTKGWGADIQV
EAAGAPPATIPQMEKSIAINGKIVYIGRAATTVPLHLEVLQVRRAQIVGAQGHSGHGIFPSVIKLMASGK
IDMTKIITARFPLEGIMEAIKAASERTDGKITIL
>gnl|CDD|176227 cd08266, Zn_ADH_like1, Alcohol dehydrogenases of the MDR family. This group contains proteins related to the zinc-dependent alcohol dehydrogenases. However, while the group has structural zinc site characteristic of these enzymes, it lacks the consensus site for a catalytic zinc. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MKAVVIRGHGGPEVLEYGDLPEPEPGPDEVLVRVKAAALNHLDLWVRRGMPGIKLPLPHILGSDGAGVVE
AVGPGVTNVKPGQRVVIYPGISCGRCEYCLAGRENLCAQYGILGEHVDGGYAEYVAVPARNLLPIPDNLS
FEEAAAAPLTFLTAWHMLVTRARLRPGETVLVHGAGSGVGSAAIQIAKLFGATVIATAGSEDKLERAKEL
GADYVIDYRKEDFVREVRELTGKRGVDVVVEHVGAATWEKSLKSLARGGRLVTCGATTGYEAPIDLRHVF
WRQLSILGSTMGTKAELDEALRLVFRGKLKPVIDSVFPLEEAAEAHRRLESREQFGKIVLTP
>gnl|CDD|176228 cd08267, MDR1, Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
VVYTRYGSPEVLLLLEVEVPIPTPKPGEVLVKVHAASVNPVDWKLRRGPPKLLLGRPFPPIPGMDFAGEV
VAVGSGVTRFKVGDEVFGRLPPKGGGALAEYVVAPESGLAKKPEGVSFEEAAALPVAGLTALQALRDAGK
VKPGQRVLINGASGGVGTFAVQIAKALGAHVTGVCSTRNAELVRSLGADEVIDYTTEDFVALTAGGEKYD
VIFDAVGNSPFSLYRASLALKPGGRYVSVGGGPSGLLLVLLLLPLTLGGGGRRLKFFLAKPNAEDLEQLA
ELVEEGKLKPVIDSVYPLEDAPEAYRRLKSGRARGKVVI
>gnl|CDD|176229 cd08268, MDR2, Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MRAVRFHQFGGPEVLRIEELPVPAPGAGEVLIRVEAIGLNRADAMFRRGAYIEPPPLPARLGYEAAGVVE
AVGAGVTGFAVGDRVSVIPAADLGQYGTYAEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGALVELA
GLRPGDSVLITAASSSVGLAAIQIANAAGATVIATTRTSEKRDALLALGAAHVIVTDEEDLVAEVLRITG
GKGVDVVFDPVGGPQFAKLADALAPGGTLVVYGALSGEPTPFPLKAALKKSLTFRGYSLDEITLDPEARR
RAIAFILDGLASGALKPVVDRVFPFDDIVEAHRYLESGQQIGKIVVTP
>gnl|CDD|176230 cd08269, Zn_ADH9, Alcohol dehydrogenases of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability
LTGPGRFEVEEHPRPTPGPGQVLVRVEGCGVCGSDLPAFNQGRPWFVYPAEPGGPGHEGWGRVVALGPGV
RGLAVGDRVAGLSGGAFAEYDLADADHAVPLPSLLDGQAFPGEPLGCALNVFRRGWIRAGKTVAVIGAGF
IGLLFLQLAAAAGARRVIAIDRRPARLALARELGATEVVTDDSEAIVERVRELTGGAGADVVIEAVGHQW
PLDLAGELVAERGRLVIFGYHQDGPRPVPFQTWNWKGIDLINAVERDPRIGLEGMREAVKLIADGRLDLG
SLLTHEFPLEELGDAFEAARRRPDGFIKGVIV
>gnl|CDD|176231 cd08270, MDR4, Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MRALVVDPDAPLRLRLGEVPDPQPAPHEALVRVAAISLNRGELKFAAERPDGAVPGWDAAGVVERAAADG
SGPAVGARVVGLGAMGAWAELVAVPTGWLAVLPDGVSFAQAATLPVAGVTALRALRRGGPLLGRRVLVTG
ASGGVGRFAVQLAALAGAHVVAVVGSPARAEGLRELGAAEVVVGGSELSGAPVDLVVDSVGGPQLARALE
LLAPGGTVVSVGSSSGEPAVFNPAAFVGGGGGRRLYTFFLYDGEPLAADLARLLGLVAAGRLDPRIGWRG
SWTEIDEAAEALLARRFRGKAVLDV
>gnl|CDD|176232 cd08271, MDR5, Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MKAWVLPKPGAALQLTLEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVA
VGAKVTGWKVGDRVAYHASLARGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQALFKKLRIE
AGRTILITGGAGGVGSFAVQLAKRAGLRVITTCSKRNFEYVKSLGADHVIDYNDEDVCERIKEITGGRGV
DAVLDTVGGETAAALAPTLAFNGHLVCIQGRPDASPDPPFTRALSVHEVALGAAHDHGDPAAWQDLRYAG
EELLELLAAGKLEPLVIEVLPFEQLPEALRALKDRHTRGKIVVTI
>gnl|CDD|176233 cd08272, MDR6, Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MKALVLESFGGPEVFELREVPRPQPGPGQVLVRVHASGVNPLDTKIRRGGAAARPPLPAILGCDVAGVVE
AVGEGVTRFRVGDEVYGCAGGLGGLQGSLAEYAVVDARLLALKPANLSMREAAALPLVGITAWEGLVDRA
AVQAGQTVLIHGGAGGVGHVAVQLAKAAGARVYATASSEKAAFARSLGADPIIYYRETVVEYVAEHTGGR
GFDVVFDTVGGETLDASFEAVALYGRVVSILGGATHDLAPLSFRNATYSGVFTLLPLLTGEGRAHHGEIL
REAARLVERGQLRPLLDPRTFPLEEAAAAHARLESGSARGKIVIDV
>gnl|CDD|176234 cd08273, MDR8, Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
NREVVVTRRGGPEVLKVVEADLPEPAAGEVVVKVEASGVSFADVQMRRGLYPDQPPLPFTPGYDLVGRVD
ALGSGVTGFEVGDRVAALTRVGGNAEYINLDAKYLVPVPEGVDAAEAVCLVLNYVTAYQMLHRAAKVLTG
QRVLIHGASGGVGQALLELALLAGAEVYGTASERNHAALRELGATPIDYRTKDWLPAMLTPGGVDVVFDG
VGGESYEESYAALAPGGTLVCYGGNSSLLQGRRSLAALGSLLARLAKLKLLPTGRRATFYYVWRDRAEDP
KLFRQDLTELLDLLAKGKIRPKIAKRLPLSEVAEAHRLLESGKVVGKIVLL
>gnl|CDD|176235 cd08274, MDR9, Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MRAVLLTGHGGLDKLVYRDDVPVPTPAPGEVLIRVGACGVNNTDINTREGWYSTEVDGATDSTGAGEAGW
WGGTLSFPRIQGADIVGRVVAVGEGVDTARIGERVLVDPSIRDPPEDDPADIDYIGSERDGGFAEYTVVP
AENAYPVNSPLSDVELATFPCSYSTAENMLERAGVGAGETVLVTGASGGVGSALVQLAKRRGAIVIAVAG
AAKEEAVRALGADTVILRDAPLLADAKALGGEPVDVVADVVGGPLFPDLLRLLRPGGRYVTAGAIAGPVV
ELDLRTLYLKDLTLFGSTLGTREVFRRLVRYIEEGEIRPVVAKTFPLSEIREAQAEFLEKRHVGKLVLVP
>gnl|CDD|176236 cd08275, MDR3, Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
RAVVLTGFGGLDKLKVEKEALPEPSSGEVRVRVEACGLNFADLMARQGLYDSAPKPPFVPGFECAGTVEA
VGEGVKDFKVGDRVMGLTRFGGYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYYALFELGNLRPGQ
SVLVHSAAGGVGLAAGQLCKTVPNVTVVGTASASKHEALKENGVTHVIDYRTQDYVEEVKKISPEGVDIV
LDALGGEDTRKSYDLLKPMGRLVVYGAANLVTGEKRSWFKLAKKWWNRPKVDPMKLISENKSVLGFNLGW
LFEERELLTEVMDKLLKLYEEGKIKPKIDSVFPFEEVGEAMRRLQSRKNIGKVVLTP
>gnl|CDD|176237 cd08276, MDR7, Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MKAWRLSGGGGLDNLKLVEEPVPEPGPGEVLVRVHAVSLNYRDLLILNGRYPPPVKDPLIPLSDGAGEVV
AVGEGVTRFKVGDRVVPTFFPNWLDGPPTAEDEASALGGPIDGVLAEYVVLPEEGLVRAPDHLSFEEAAT
LPCAGLTAWNALFGLGPLKPGDTVLVQGTGGVSLFALQFAKAAGARVIATSSSDEKLERAKALGADHVIN
YRTTPDWGEEVLKLTGGRGVDHVVEVGGPGTLAQSIKAVAPGGVISLIGFLSGFEAPVLLLPLLTKGATL
RGIAVGSRAQFEAMNRAIEAHRIRPVIDRVFPFEEAKEAYRYLESGSHFGKVVIRV
>gnl|CDD|176238 cd08277, liver_alcohol_DH_like, Liver alcohol dehydrogenase. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding
IKCKAAVAWEAGKPLVIEEIEVAPPKANEVRIKMLATSVCHTDILAIEGFKATLFPVILGHEGAGIVESV
GEGVTNLKPGDKVIPLFIGQCGECSNCRSGKTNLCQKYRANESGLMPDGTSRFTCKGKKIYHFLGTSTFS
QYTVVDENYVAKIDPAAPLEHVCLLGCGFSTGYGAAWNTAKVEPGSTVAVFGLGAVGLSAIMGAKIAGAS
RIIGVDINEDKFEKAKEFGATDFINPKDSDKPVSEVIREMTGGGVDYSFECTGNADLMNEALESTKLGWG
VSVVVGVPPGAELSIRPFQLILGRTWKGSFFGGFKSRSDVPKLVSKYMNKKFDLDELITHVLPFEEINKG
FDLMKSGECIRTVIT
>gnl|CDD|176239 cd08278, benzyl_alcohol_DH, Benzyl alcohol dehydrogenase. Benzyl alcohol dehydrogenase is similar to liver alcohol dehydrogenase, but has some amino acid substitutions near the active site, which may determine the enzyme's specificity of oxidizing aromatic substrates. Also known as aryl-alcohol dehydrogenases, they catalyze the conversion of an aromatic alcohol + NAD+ to an aromatic aldehyde + NADH + H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MKTTAAVVREPGGPFVLEDVELDDPRPDEVLVRIVATGICHTDLVVRDGGLPTPLPAVLGHEGAGVVEAV
GSAVTGLKPGDHVVLSFASCGECANCLSGHPAYCENFFPLNFSGRRPDGSTPLSLDDGTPVHGHFFGQSS
FATYAVVHERNVVKVDKDVPLELLAPLGCGIQTGAGAVLNVLKPRPGSSIAVFGAGAVGLAAVMAAKIAG
CTTIIAVDIVDSRLELAKELGATHVINPKEEDLVAAIREITGGGVDYALDTTGVPAVIEQAVDALAPRGT
LALVGAPPPGAEVTLDVNDLLVSGKTIRGVIEGDSVPQEFIPRLIELYRQGKFPFDKLVTFYPFEDINQA
IADSESGKVIKPVLR
>gnl|CDD|176240 cd08279, Zn_ADH_class_III, Class III alcohol dehydrogenase. Glutathione-dependent formaldehyde dehydrogenases (FDHs, Class III ADH) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding
MRAAVLHEVGKPLEIEEVELDDPGPGEVLVRIAAAGLCHSDLHVVTGDLPAPLPAVLGHEGAGVVEEVGP
GVTGVKPGDHVVLSWIPACGTCRYCSRGQPNLCDLGAGILGGQLPDGTRRFTADGEPVGAMCGLGTFAEY
TVVPEASVVKIDDDIPLDRAALLGCGVTTGVGAVVNTARVRPGDTVAVIGCGGVGLNAIQGARIAGASRI
IAVDPVPEKLELARRFGATHTVNASEDDAVEAVRDLTDGRGADYAFEAVGRAATIRQALAMTRKGGTAVV
VGMGPPGETVSLPALELFLSEKRLQGSLYGSANPRRDIPRLLDLYRAGRLKLDELVTRRYSLDEINEAFA
DMLAGENARGVIV
>gnl|CDD|176241 cd08281, liver_ADH_like1, Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase). NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group contains members identified as zinc dependent alcohol dehydrogenases (ADH), and class III ADG (aka formaldehyde dehydrogenase, FDH). Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also know as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to the corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
MRAAVLRETGAPTPYADSRPLVIEEVELDPPGPGEVLVKIAAAGLCHSDLSVINGDRPRPLPMALGHEAA
GVVVEVGEGVTDLEVGDHVVLVFVPSCGHCRPCAEGRPALCEPGAAANGAGTLLSGGRRLRLRGGEINHH
LGVSAFAEYAVVSRRSVVKIDKDVPLEIAALFGCAVLTGVGAVVNTAGVRPGQSVAVVGLGGVGLSALLG
AVAAGASQVVAVDLNEDKLALARELGATATVNAGDPNAVEQVRELTGGGVDYAFEMAGSVPALETAYEIT
RRGGTTVTAGLPDPEARLSVPALSLVAEERTLKGSYMGSCVPRRDIPRYLALYLSGRLPVDKLLTHRLPL
DEINEGFDRLAAGEAVRQVIL
>gnl|CDD|176242 cd08282, PFDH_like, Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH). Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. PFDH converts 2 molecules of aldehydes to corresponding carboxylic acid and alcohol. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit
MKAVVYGGPGNVAVEDVPDPKIEHPTDAIVRITTTAICGSDLHMYRGRTGAEPGLVLGHEAMGEVEEVGS
AVESLKVGDRVVVPFNVACGRCRNCKRGLTGVCLTVNPGRAGGAYGYVDMGPYGGGQAEYLRVPYADFNL
LKLPDRDGAKEKDDYLMLSDIFPTGWHGLELAGVQPGDTVAVFGAGPVGLMAAYSAILRGASRVYVVDHV
PERLDLAESIGAIPIDFSDGDPVEQILGLEPGGVDRAVDCVGYEARDRGGEAQPNLVLNQLIRVTRPGGG
IGIVGVYVAEDPGAGDAAAKQGELSFDFGLLWAKGLSFGTGQAPVKKYNRQLRDLILAGRAKPSFVVSHV
ISLEDAPEAYARFDKRLETKVVIKP
>gnl|CDD|176243 cd08283, FDH_like_1, Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1. Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit
MKALVWHGKGDVRVEEVPDPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVG
PEVRNLKVGDRVVVPFTIACGECFYCKRGLYSQCDNTNPSAEMAKLYGHAGAGIFGYSHLTGGYAGGQAE
YVRVPFADVGPFKIPDDLSDEKALFLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAE
RVIAIDRVPERLEMARSHLGAETINFEEVDDVVEALRELTGGRGPDVCIDAVGMEAHGSPLHKAEQALLK
LETDRPDALREAIQAVRKGGTVSIIGVYGGTVNKFPIGAAMNKGLTLRMGQTHVQRYLPRLLELIESGEL
DPSFIITHRLPLEDAPEAYKIFDKKEDGCIKVVLKP
>gnl|CDD|176244 cd08284, FDH_like_2, Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2. Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit
MKAVVFKGPGDVRVEEVPIPQIQDPTDAIVKVTAAAICGSDLHIYRGHIPSTPGFVLGHEFVGEVVEVGP
EVRTLKVGDRVVSPFTIACGECFYCRRGQSGRCAKGGLFGYAGSPNLDGAQAEYVRVPFADGTLLKLPDG
LSDEAALLLGDILPTGYFGAKRAQVRPGDTVAVIGCGPVGLCAVLSAQVLGAARVFAVDPVPERLERAAA
LGAEPINFEDAEPVERVREATEGRGADVVLEAVGGAAALDLAFDLVRPGGVISSVGVHTAEEFPFPGLDA
YNKNLTLRFGRCPVRSLFPELLPLLESGRLDLEFLIDHRMPLEEAPEAYRLFDKRKVLKVVLDP
>gnl|CDD|176245 cd08285, NADP_ADH, NADP(H)-dependent alcohol dehydrogenases. This group is predominated by atypical alcohol dehydrogenases; they exist as tetramers and exhibit specificity for NADP(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like other zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric ADHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains; however, they do not have and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit
MKAFAMLGIGKVGWIEKPIPVCGPNDAIVRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGS
EVKDFKPGDRVIVPAITPDWRSVAAQRGYPSQSGGMLGGWKFSNFKDGVFAEYFHVNDADANLAPLPDGL
TDEQAVMLPDMMSTGFHGAELANIKLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVELAKEY
GATDIVDYKNGDVVEQILKLTGGKGVDAVIIAGGGQDTFEQALKVLKPGGTISNVNYYGEDDYLPIPREE
WGVGMGHKTINGGLCPGGRLRMERLASLIEYGRVDPSKLLTHHFFGFDDIEEALMLMKDKPDDLIKPVII
F
>gnl|CDD|176246 cd08286, FDH_like_ADH2, formaldehyde dehydrogenase (FDH)-like. This group is related to formaldehyde dehydrogenase (FDH), which is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. This family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Another member is identified as a dihydroxyacetone reductase. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit
MKALVYHGPGKISWEDRPKPTIQEPTDAIVKMLKTTICGTDLHILKGDVPTVTPGRILGHEGVGVVEEVG
SAVTNFKVGDRVLISCISSCGTCGYCRKGLYSHCESGGWILGNLIDGTQAEYVRIPHADNSLYKLPEGVD
EEAAVMLSDILPTGYECGVLNGKVKPGDTVAIVGAGPVGLAALLTAQLYSPSKIIMVDLDDNRLEVAKKL
GATHTVNSAKGDAIEQVLELTDGRGVDVVIEAVGIPATFELCQELVAPGGHIANVGVHGKPVDLHLEKLW
IKNITITTGLVDTNTTPMLLKLVSSGKLDPSKLVTHRFKLSEIEKAYDTFSAAAKHKALKVIIDF
>gnl|CDD|176247 cd08287, FDH_like_ADH3, formaldehyde dehydrogenase (FDH)-like. This group contains proteins identified as alcohol dehydrogenases and glutathione-dependant formaldehyde dehydrogenases (FDH) of the zinc-dependent/medium chain alcohol dehydrogenase family. The MDR family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit
MRATVIHGPGDIRVEEVPDPVIEEPTDAVIRVVATCVCGSDLWPYRGVSPTRAPAPIGHEFVGVVEEVGS
EVTSVKPGDFVIAPFAISDGTCPFCRAGFTTSCVHGGFWGAFVDGGQGEYVRVPLADGTLVKVPGSPSDD
EDLLPSLLALSDVMGTGHHAAVSAGVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIAMSRHEDRQALAR
EFGATDIVAERGEEAVARVRELTGGVGADAVLECVGTQESMEQAIAIARPGGRVGYVGVPHGGVELDVRE
LFFRNVGLAGGPAPVRRYLPELLDDVLAGRINPGRVFDLTLPLDEVAEGYRAMDERRAIKVLLRP
>gnl|CDD|176248 cd08288, MDR_yhdh, Yhdh putative quinone oxidoreductases. Yhdh putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
FKALVLEKDDGGTSAELRELDESDLPEGDVTVEVHYSTLNYKDGLAITGKGGIVRTFPLVPGIDLAGTVV
ESSSPRFKPGDRVVLTGWGVGERHWGGYAQRARVKADWLVPLPEGLSARQAMAIGTAGFTAMLCVMALED
HGVTPGDGPVLVTGAAGGVGSVAVALLARLGYEVVASTGRPEEADYLRSLGASEIIDRAELSEPGRPLQK
ERWAGAVDTVGGHTLANVLAQTRYGGAVAACGLAGGADLPTTVMPFILRGVTLLGIDSVMAPIERRRAAW
ARLARDLDPALLEALTREIPLADVPDAAEAILAGQVRGRVVVDV
>gnl|CDD|176249 cd08289, MDR_yhfp_like, Yhfp putative quinone oxidoreductases. yhfp putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
FQALVVEKDEDDVSVSVKNLTLDDLPEGDVLIRVAYSSVNYKDGLASIPGGKIVKRYPFIPGIDLAGTVV
ESNDPRFKPGDEVIVTSYDLGVSHHGGYSEYARVPAEWVVPLPKGLTLKEAMILGTAGFTAALSIHRLEE
NGLTPEQGPVLVTGATGGVGSLAVSILAKLGYEVVASTGKADAADYLKKLGAKEVIPREELQEESIKPLE
KQRWAGAVDPVGGKTLAYLLSTLQYGGSVAVSGLTGGGEVETTVFPFILRGVNLLGIDSVECPMELRRRI
WRRLATDLKPTQLLNEIKQEITLDELPEALKQILQGRVTGRTVVKL
>gnl|CDD|176250 cd08290, ETR, 2-enoyl thioester reductase (ETR). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain
AKALVYTEHGEPKEVLQLESYEIPPPGPPNEVLVKMLAAPINPADINQIQGVYPIKPPTTPEPPAVGGNE
GVGEVVKVGSGVKSLKPGDWVIPLRPGLGTWRTHAVVPADDLIKVPNDVDPEQAATLSVNPCTAYRLLED
FVKLQPGDWVIQNGANSAVGQAVIQLAKLLGIKTINVVRDRPDLEELKERLKALGADHVLTEEELRSLLA
TELLKSAPGGRPKLALNCVGGKSATELARLLSPGGTMVTYGGMSGQPVTVPTSLLIFKDITLRGFWLTRW
LKRANPEEKEDMLEELAELIREGKLKAPPVEKVTDDPLEEFKDALANALKGGGGGKQVLVM
>gnl|CDD|176251 cd08291, ETR_like_1, 2-enoyl thioester reductase (ETR) like proteins, child 1. 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain
MKALLLEEYGKPLEVKELSLPEPEVPEPGPGEVLIKVEAAPINPSDLGFLKGQYGSTKALPVPPGFEGSG
TVVAAGGGPLAQSLIGKRVAFLAGSYGTYAEYAVADAQQCLPLPDGVSFEQGASSFVNPLTALGMLETAR
EEGAKAVVHTAAASALGRMLVRLCKADGIKVINIVRRKEQVDLLKKIGAEYVLNSSDPDFLEDLKELIAK
LNATIFFDAVGGGLTGQILLAMPYGSTLYVYGYLSGKLDEPIDPVDLIFKNKSIEGFWLTTWLQKLGPEV
VKKLKKLVKTELKTTFASRYPLALTLEAIAFYSKNMSTGKKLLI
>gnl|CDD|176252 cd08292, ETR_like_2, 2-enoyl thioester reductase (ETR) like proteins, child 2. 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain
MRAAVHTQFGDPADVLEIGEVPKPTPGAGEVLVRTTLSPIHNHDLWTIRGTYGYKPELPAIGGSEAVGVV
DAVGEGVKGLQVGQRVAVAPVHGTWAEYFVAPADGLVPLPDGISDEVAAQLIAMPLSALMLLDFLGVKPG
QWLIQNAAGGAVGKLVAMLAAARGINVINLVRRDAGVAELRALGIGPVVSTEQPGWQDKVREAAGGAPIS
VALDSVGGKLAGELLSLLGEGGTLVSFGSMSGEPMQISSGDLIFKQATVRGFWGGRWSQEMSVEYRKRMI
AELLTLALKGQLLLPVEAVFDLGDAAKAAAASMRPGRAGKVLLR
>gnl|CDD|176253 cd08293, PTGR2, Prostaglandin reductase. Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES
MINKRVVLNSRPGKNGNPVAENFRVEECTLPDELNEGQVLVRTLYLSVDPYMRCRMNEDTGTDYLAPWQL
SQVLDGGGVGVVEESKHQKFAVGDIVTSFNWPWQTYAVLDGSSLEKVDPQLVDGHLSYFLGAVGLPGLTA
LIGIQEKGHITPGANQTMVVSGAAGACGSLAGQIGRLLGCSRVVGICGSDEKCQLLKSELGFDAAINYKT
DNVAERLRELCPEGVDVYFDNVGGEISDTVISQMNENSHIILCGQISQYNKDVPYPPPLPEATEAILKER
NITRERFLVLNYKDKFEEAIAQLSQWVKEGKLKVKETVYEGLENAGEAFQSMMNGGNIGKQIVKV
>gnl|CDD|176254 cd08294, leukotriene_B4_DH_like, 13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 hydroxydehydrogenase activity. Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto- 13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES
VKAKTWVLKKHFDGKPKESDFELVEEELPPLKDGEVLCEALFLSVDPYMRPYSKRLNEGDTMIGTQVAKV
IESKNSKFPVGTIVVASFGWRTHTVSDGKDQPDLYKLPADLPDDLPPSLALGVLGMPGLTAYFGLLEICK
PKAGETVVVNGAAGAVGSLVGQIAKIKGCKVIGCAGSDDKVAWLKELGFDAVFNYKTVSLEEALKEAAPD
GIDCYFDNVGGEFSSTVLSHMNDFGRVAVCGSISTYNDKEPKKGPYVQETIIFKQLKMEGFIVYRWQDRW
PEALKQLLKWIKEGKLKYREHVTEGFENMPQAFIGMLKGENTGKAIVKV
>gnl|CDD|176255 cd08295, double_bond_reductase_like, Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. This group includes proteins identified as the Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. The Arabidopsis enzyme, a member of the medium chain dehydrogenase/reductase family, catalyzes the reduction of 7-8-double bond of phenylpropanal substrates as a plant defense mechanism. Prostaglandins and related eicosanoids (lipid mediators involved in host defense and inflamation) are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. Leukotriene B4 (LTB4) can be metabolized by LTB4 20-hydroxylase in inflamatory cells, and in other cells by bifunctional LTB4 12-HD/PGR. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES
VRNKQVILKAYVTGFPKESDLELRTTKLTLKVPPGGSGDVLVKNLYLSCDPYMRGRMKGHDDSLYLPPFK
PGEVITGYGVAKVVDSGNPDFKVGDLVWGFTGWEEYSLIPRGQDLRKIDHTDVPLSYYLGLLGMPGLTAY
AGFYEVCKPKKGETVFVSAASGAVGQLVGQLAKLKGCYVVGSAGSDEKVDLLKNKLGFDDAFNYKEEPDL
DAALKRYFPNGIDIYFDNVGGKMLDAVLLNMNLHGRIAACGMISQYNLEWPEGVRNLLNIIYKRVKIQGF
LVGDYLHRYPEFLEEMSGYIKEGKLKYVEDIADGLESAPEAFVGLFTGSNIGKQVVKV
>gnl|CDD|176256 cd08296, CAD_like, Cinnamyl alcohol dehydrogenases (CAD). Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADHs), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
YKAVQVTEPGGPLELVERDVPLPGPGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVG
EGVSRWKVGDRVGVGWHGGHCGTCDACRRGDFVHCENGKVTGVTRDGGYAEYMLAPAEALARIPDDLDAA
EAAPLLCAGVTTFNALRNSGAKPGDLVAVQGIGGLGHLAVQYAAKMGFRTVAISRGSDKADLARKLGAHH
YIDTSKEDVAEALQELGGAKLILATAPNAKAISALVGGLAPRGKLLILGAAGEPVAVSPLQLIMGRKSIH
GWPSGTALDSEDTLKFSALHGVRPMVETFPLEKANEAYDRMMSGKARFRVVLT
>gnl|CDD|176257 cd08297, CAD3, Cinnamyl alcohol dehydrogenases (CAD). These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MKAAVVEEFGEKPYEVKDVPVPEPGPGEVLVKLEASGVCHTDLHAALGDWPVKPKLPLIGGHEGAGVVVA
VGPGVSGLKVGDRVGVKWLYDACGKCEYCRTGDETLCPNQKNSGYTVDGTFAEYAIADARYVTPIPDGLS
FEQAAPLLCAGVTVYKALKKAGLKPGDWVVISGAGGGLGHLGVQYAKAMGLRVIAIDVGDEKLELAKELG
ADAFVDFKKSDDVEAVKELTGGGGAHAVVVTAVSAAAYEQALDYLRPGGTLVCVGLPPGGFIPLDPFDLV
LRGITIVGSLVGTRQDLQEALEFAARGKVKPHIQVVPLEDLNEVFEKMEEGKIAGRVVVDF
>gnl|CDD|176258 cd08298, CAD2, Cinnamyl alcohol dehydrogenases (CAD). These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines
MKAMVLEKPGPIEENPLRLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRV
EAVGPGVTRFSVGDRVGVPWLGSTCGECRYCRSGRENLCDNARFTGYTVDGGYAEYMVADERFAYPIPED
YDDEEAAPLLCAGIIGYRALKLAGLKPGQRLGLYGFGASAHLALQIARYQGAEVFAFTRSGEHQELAREL
GADWAGDSDDLPPEPLDAAIIFAPVGALVPAALRAVKKGGRVVLAGIHMSDIPAFDYELLWGEKTIRSVA
NLTRQDGEEFLKLAAEIPIKPEVETYPLEEANEALQDLKEGRIRGAAVL
>gnl|CDD|176259 cd08299, alcohol_DH_class_I_II_IV, class I, II, IV alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group includes alcohol dehydrogenases corresponding to mammalian classes I, II, IV. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction
TAGKVIKCKAAVLWEPKKPFSIEEIEVAPPKAHEVRIKIVATGICRSDDHVVSGKLVTPFPVILGHEAAG
IVESVGEGVTTVKPGDKVIPLFVPQCGKCRACLNPESNLCLKNDLGKPQGLMQDGTSRFTCKGKPIHHFL
GTSTFSEYTVVDEIAVAKIDAAAPLEKVCLIGCGFSTGYGAAVNTAKVTPGSTCAVFGLGGVGLSAIMGC
KAAGASRIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLTEMTDGGVDFSFEVIGRLDTMKAALAS
CHEGYGVSVIVGVPPSSQNLSINPMLLLTGRTWKGAVFGGWKSKDSVPKLVADYMAKKFNLDPLITHTLP
FEKINEGFDLLRSGKSIRTVLTF
>gnl|CDD|176260 cd08300, alcohol_DH_class_III, class III alcohol dehydrogenases. Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding
ITCKAAVAWEAGKPLSIEEVEVAPPKAGEVRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVES
VGEGVTSVKPGDHVIPLYTPECGECKFCKSGKTNLCQKIRATQGKGLMPDGTSRFSCKGKPIYHFMGTST
FSEYTVVAEISVAKINPEAPLDKVCLLGCGVTTGYGAVLNTAKVEPGSTVAVFGLGAVGLAVIQGAKAAG
ASRIIGIDINPDKFELAKKFGATDCVNPKDHDKPIQQVLVEMTDGGVDYTFECIGNVKVMRAALEACHKG
WGTSVIIGVAAAGQEISTRPFQLVTGRVWKGTAFGGWKSRSQVPKLVEDYMKGKIKVDEFITHTMPLDEI
NEAFDLMHAGKSIRTVVK
>gnl|CDD|176261 cd08301, alcohol_DH_plants, Plant alcohol dehydrogenase. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding
ITCKAAVAWEAGKPLVIEEVEVAPPQAMEVRIKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAGIVES
VGEGVTDLKPGDHVLPVFTGECKECRHCKSEKSNMCDLLRINTDRGVMINDGKSRFSINGKPIYHFVGTS
TFSEYTVVHVGCVAKINPEAPLDKVCLLSCGVSTGLGAAWNVAKVKKGSTVAIFGLGAVGLAVAEGARIR
GASRIIGVDLNPSKFEQAKKFGVTEFVNPKDHDKPVQEVIAEMTGGGVDYSFECTGNIDAMISAFECVHD
GWGVTVLLGVPHKDAVFSTHPMNLLNGRTLKGTLFGGYKPKTDLPNLVEKYMKKELELEKFITHELPFSE
INKAFDLLLKGECLRCILH
>gnl|CDD|176720 cd08304, DD, Death Domain Superfamily of protein-protein interaction domains. The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer
RLDLCENLTLEVLQQLKTALKSRIPPDQVEQISAANELLNILESQYNHTLQLLFALFEDLGLHNLARLL
>gnl|CDD|260019 cd08305, Pyrin, Pyrin: a protein-protein interaction domain. The Pyrin domain (or PYD), also called DAPIN or PAAD, is a subfamily of the Death Domain (DD) superfamily and it functions in several signaling pathways. The Pyrin domain is found at the N-terminus of a variety of proteins and serves as a linker that recruits other domains into signaling complexes. Pyrin-containing proteins include NALPs, ASC (Apoptosis-associated speck-like protein containing a CARD), and the interferon-inducible p200 (IFI-200) family of proteins which includes the human IFI-16, myeloid cell nuclear differentiation antigen (MNDA) and absent in melanoma (AIM) 2. NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. ASC and NALPs are involved in the regulation of inflammation. ASC, NALP1 and NALP3 are involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP12 functions as a negative regulator of inflammation. The p200 proteins are involved in the regulation of cell cycle and differentiation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including Caspase activation and recruitment domain (CARD) and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
LLTGLENITDEEFKMFKSLLASELKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLAN
QLQ
>gnl|CDD|260020 cd08306, Death_FADD, Fas-associated Death Domain protein-protein interaction domain. Death domain (DD) found in FAS-associated via death domain (FADD). FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor, FAS, and its DED recruits the initiator caspases, caspase-8 and -10, to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes
LNEAFDVICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALR
DCQLNLVADLVEKKL
>gnl|CDD|260021 cd08307, Death_Pelle, Death domain of the protein kinase Pelle. Death domain (DD) of the protein kinase Pelle from Drosophila melanogaster and similar proteins. In Drosophila, interaction between the DDs of Tube and Pelle is an important component of the Toll pathway, which functions in establishing dorsoventral polarity in embryos and in mediating innate immune responses to pathogens. Tube and Pelle transmit the signal from the Toll receptor to the Dorsal/Cactus complex. Pelle also functions in photoreceptor axon targeting. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
MYIYELPFTERKQLCALLDQDNKWEELAGVMMGYDPDDVEGIRRCCLRGRSPTEELLTKWGNKNHTITEL
FVLLYRMKLYRAMRILKDFVDPKYHVL
>gnl|CDD|260022 cd08308, Death_Tube, Death domain of Tube. Death domains (DDs) similar to the DD in the protein Tube from Drosophila melanogaster. In Drosophila, interaction between the DDs of Tube and Pelle is an important component of the Toll pathway, which functions in establishing dorsoventral polarity in embryos and also in mediating innate immune response to pathogens. Tube and Pelle transmit the signal from the Toll receptor to the Dorsal/Cactus complex. Some members of this subfamily contain a C-terminal kinase domain, like Pelle, in addition to the DD. Tube has no counterpart in vertebrates. It contains an N-terminal DD and a C-terminal region with five copies of the Tube repeat, an 8-amino acid motif. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
NTEIRKLPPSALYKLANILDPGDGWKKLMALIPKKLDDLDEDNYPPKYTSDHIKLIEEAAQKQRRSCTEI
LLEEWGTSGRERPTLRHLLKLLVKAELFRAADYLAVDLLKGEPPARPDSGPAAPIDVE
>gnl|CDD|260023 cd08309, Death_IRAK, Death domain of Interleukin-1 Receptor-Associated Kinases. Death Domains (DDs) found in Interleukin-1 (IL-1) Receptor-Associated Kinases (IRAK1-4) and similar proteins. IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. All four types are involved in signal transduction involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB, and mitogen-activated protein kinase pathways. IRAK1 and IRAK4 are active kinases while IRAK2 and IRAK-M (also called IRAK3) are inactive. In general, IRAKs are expressed ubiquitously, except for IRAK-M which is detected only in macrophages. The insect homologs, Pelle and Tube, are important components of the Toll pathway, which functions in establishing dorsoventral polarity in embryos and also in the innate immune response. Most members have an N-terminal DD followed by a kinase domain. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
TYIRNLPPWVLKRLCKVLDALELAGWRQLASLIPYDQTDVRQIESMKQRGQSPTRELLWDWGTQNATVQD
LVQLLTQLGLFRAADLIT
>gnl|CDD|260024 cd08310, Death_NFkB-like, Death domain of Nuclear Factor-KappaB precursor proteins. Death Domain (DD) of Nuclear Factor-KappaB (NF-kB) precursor proteins. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). Two of these, NF-kB1 and NF-kB2 are produced from the processing of the precursor proteins p105 and p100, respectively. In addition to RHD, p105 and p100 contain ANK repeats and a C-terminal DD. NF-kBs are regulated by the Inhibitor of NF-kB (IkB) Kinase (IKK) complex through classical and non-canonical pathways, which differ in the IKK subunits involved and downstream targets. IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. The precursor proteins p105 and p100 function as IkBs and as NF-kB proteins after being processed by the proteasome. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
TRLRLCKLLDVGKDWRELAELLGLGHLVESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVEL
ID
>gnl|CDD|260025 cd08311, Death_p75NR, Death domain of p75 Neurotrophin Receptor. Death Domain (DD) found in p75 neurotrophin receptor (p75NTR, NGFR, TNFRSF16). p75NTR binds members of the neurotrophin (NT) family including nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), and NT3, among others. It contains an NT-binding extracellular region that bears four cysteine-rich repeats, a transmembrane domain, and an intracellular DD. p75NTR plays roles in the immune, vascular, and nervous systems, and has been shown to promote cell death or survival, and to induce neurite outgrowth or collapse depending on its ligands and co-receptors. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
PPHKQEEVEKLLNAGREGSDWRALAGELGYSAEEIDSFAREADPCRALLTDWSAQDGATLGVLLTALRKI
GRDDIVEILQ
>gnl|CDD|260026 cd08312, Death_MyD88, Death domain of Myeloid Differentation primary response protein MyD88. Death Domain (DD) of Myeloid Differentiation primary response protein 88 (MyD88). MyD88 is an adaptor protein involved in interleukin-1 receptor (IL-1R)- and Toll-like receptor (TLR)-induced activation of nuclear factor-kappaB (NF-kB) and mitogen activated protein kinase pathways that lead to the induction of proinflammatory cytokines. It is a key component in the signaling pathway of pathogen recognition in the innate immune system. MyD88 contains an N-terminal DD and a C-terminal Toll/IL-1 Receptor (TIR) homology domain that mediates interaction with TLRs and IL-1R. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
VRKKLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRPPGATVGNLLEILEELE
RKDVLEDLQ
>gnl|CDD|176729 cd08313, Death_TNFR1, Death domain of Tumor Necrosis Factor Receptor 1. Death Domain (DD) found in tumor necrosis factor receptor-1 (TNFR-1). TNFR-1 has many names including TNFRSF1A, CD120a, p55, p60, and TNFR60. It activates two major intracellular signaling pathways that lead to the activation of the transcription factor NF-kB and the induction of cell death. Upon binding of its ligand TNF, TNFR-1 trimerizes which leads to the recruitment of an adaptor protein named TNFR-associated death domain protein (TRADD) through a DD/DD interaction. Mutations in the TNFRSF1A gene causes TNFR-associated periodic syndrome (TRAPS), a rare disorder characterized recurrent fever, myalgia, abdominal pain, conjunctivitis and skin eruptions. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
LLYTVLDEVPPRRWKEFVRRLGLSDNEIERVELDHRRCRDAQYQMLKVWKERGPRPYATLQHLLSVLRDM
ELVGCAEDIE
>gnl|CDD|260027 cd08315, Death_TRAILR_DR4_DR5, Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors. Death Domain (DD) found in Tumor necrosis factor-Related Apoptosis-Inducing Ligand (TRAIL) Receptors. In mammals, this family includes TRAILR1 (also called DR4 or TNFRSF10A) and TRAILR2 (also called DR5, TNFRSF10B, or KILLER). They function as receptors for the cytokine TRAIL and are involved in apoptosis signaling pathways. TRAIL preferentially induces apoptosis in cancer cells while exhibiting little toxicity in normal cells. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
SFDYFEDIVPFKSWKRLMRALGLSDNEIKLAEANDPGSQEPLYQMLNKWLNKTGRKASVNTLLDALEDLG
LRGAAETIADKLVQSGKF
>gnl|CDD|260028 cd08316, Death_FAS_TNFRSF6, Death domain of FAS or TNF receptor superfamily member 6. Death Domain (DD) found in the FS7-associated cell surface antigen (FAS). FAS, also known as TNFRSF6 (TNF receptor superfamily member 6), APT1, CD95, FAS1, or APO-1, together with FADD (Fas-associating via Death Domain) and caspase 8, is an integral part of the death inducing signalling complex (DISC), which plays an important role in the induction of apoptosis and is activated by binding of the ligand FasL to FAS. FAS also plays a critical role in self-tolerance by eliminating cell types (autoreactive T and B cells) that contribute to autoimmunity. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
DVDLSKHIPDIAEIMGWKDVKKFARKSGISETKIDEIQLDNPNDTAEQKVQLLRAWYQKHGKKGAYRTLI
KTLRKAGKRAKADKIQDIIKKDVS
>gnl|CDD|260029 cd08317, Death_ank, Death domain associated with Ankyrins. Death Domain (DD) associated with Ankyrins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. Ankyrins function as adaptor proteins and they interact, through ANK repeats, with structurally diverse membrane proteins, including ion channels/pumps, calcium release channels, and cell adhesion molecules. They play critical roles in the proper expression and membrane localization of these proteins. In mammals, this family includes ankyrin-R for restricted (or ANK1), ankyrin-B for broadly expressed (or ANK2) and ankyrin-G for general or giant (or ANK3). They are expressed in different combinations in many tissues and play non-overlapping functions. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESA
LKKIGRDDIVEKCE
>gnl|CDD|260030 cd08318, Death_NMPP84, Death domain of Nuclear Matrix Protein P84. Death domain (DD) found in the Nuclear Matrix Protein P84 (also known as HPR1 or THOC1). HPR1/p84 resides in the nuclear matrix and is part of the THO complex, also called TREX (transcription/export) complex, which functions in mRNP biogenesis at the interface between transcription and export of mRNA from the nucleus. Mice lacking THOC1 have abnormal testis development and are sterile. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
QDKPVTSEQIDVLANKLGEQWKTLAPYLEMKDKDIRQIESDSEDMKMRAKQLLVTWQDREGAQATPEILM
TALNAAGLNEIAENLF
>gnl|CDD|260031 cd08319, Death_RAIDD, Death domain of RIP-associated ICH-1 homologous protein with a death domain. Death domain (DD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal Caspase Activation and Recruitment Domain (CARD), which interacts with the caspase-2 CARD, and a C-terminal DD, which interacts with the DD of PIDD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
TDRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLK
AVEVDPSVLQFLL
>gnl|CDD|260032 cd08320, Pyrin_NALPs, Pyrin death domain found in NALP proteins. Pyrin Death Domain found in NALP (NACHT, LRR and PYD domains) proteins including NALP1 (CARD7, NLRP1), NALP3 (NLRP3, Cryopyrin, CIAS1), and NALP12 (NLRP12, Monarch-1), among others. Mammals contains at least 14 NALP proteins, named NALP1-14 (or NLRP1-14). NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. The NBS-LRR family is also referred to as the NLR (Nod-like Receptor) or CATERPILLAR (for CARD, transcription enhancer, R-(purine)-binding, pyrin, lots of LRRs) family. NALP1 contains an additional Caspase activation and recruitment domain (CARD) at the C-terminus. NALP1 and NALP3 are both involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP1-inflammasomes recognize specific substances while NALP3-inflammasomes responds to many diverse triggers. Mutations in the NALP3 gene are associated with a broad spectrum of autoinflammatory disorders including Muckle-Wells Syndrome (MWS), familial cold autoinflammatory syndrome (FCAS), and chronic neurologic cutaneous and articular syndrome (CINCA). NALP12 functions as a negative regulator of inflammation. In general, Pyrin is a subfamily of the Death Domain (DD) superfamily and functions in several signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMN
RTDLCEKARAEMNE
>gnl|CDD|260033 cd08321, Pyrin_ASC-like, Pyrin Death Domain found in ASC. Pyrin Death Domain found in ASC (Apoptosis-associated speck-like protein containing a CARD) and similar proteins. ASC is an adaptor molecule that functions in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. ASC contains two domains from the Death Domain (DD) superfamily, an N-terminal pyrin-like domain and a C-terminal Caspase activation and recruitment domain (CARD). Through these 2 domains, ASC serves as an adaptor for inflammasome integrity and oligomerizes to form supramolecular assemblies. Included in this family is human PYNOD (also known as NLRP10 or NOD8) which via its Pyrin domain suppresses oligomerization of ASC, and ASC-mediated NF-kappaB activation. Other members of this subfamily are associated with ATPase domains and their function remains unknown. In general, Pyrin is a subfamily of the DD superfamily and functions in several signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
RDLLLDALEDLGEEELKKFKWKLRDIPLEGYPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRA
INQNDLAEKLQK
>gnl|CDD|260034 cd08323, CARD_APAF1, Caspase activation and recruitment domain similar to that found in Apoptotic Protease-Activating Factor 1. Caspase activation and recruitment domain (CARD) similar to that found in apoptotic protease-activating factor 1 (APAF-1), which is an activator of caspase-9. APAF-1 contains WD-40 repeats, a CARD, and an ATPase domain. Upon stimulation, APAF-1, together with caspase-9, forms the heptameric 'apoptosome', which leads to the processing and activation of caspase-9, starting a caspase cascade which leads to apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALL
HEGYKDLAALLHDGLP
>gnl|CDD|260035 cd08324, CARD_NOD1_CARD4, Caspase activation and recruitment domain similar to that found in NOD1. Caspase activation and recruitment domain (CARD) found in human NOD1 (CARD4) and similar proteins. NOD1 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD1, as well as NOD2, the N-terminal effector domain is a CARD. Nod1-CARD has been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYIL
QKVADAYIDLRPWLD
>gnl|CDD|260036 cd08325, CARD_CASP1-like, Caspase activation and recruitment domain found in Caspase-1 and related proteins. Caspase activation and recruitment domain (CARD) similar to those found in Caspase-1 (CASP1, ICE) and related proteins, including CARD-only proteins such as ICEBERG or CARD18, INCA (CARD17), CARD16 (COP1, PSEUDO-ICE), CARD8 (DACAR, NDPP1, TUCAN), and CARD12 (NLRC4), as well as ICE-like caspases such as CASP12, CASP5 (ICH-3) and CASP4 (TX, ICH-2). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. CASP1 plays a central role in the cellular response to a wide variety of microbial and non-microbial stimuli, being activated by the inflammasome or the pyroptosome. CARD8 binds itself and the initiator caspase-9, interfering with the binding of APAF-1 and suppressing caspase-9 activation. CARD12 is a Nod-like receptor (NLR) that plays an important role in the innate immune response to Gram-negative bacteria. Caspase-4 (CASP4), -5 (CASP5), and -12 (CASP12) are inflammatory caspases implicated in inflammation and endoplasmic reticulum stress-induced apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
RLKEKRVKFVESVGKGVINGLLDDLLEKNVLNEEEMEKIKEENNTIVDKARVLIDSVTEKGQMAGQIFIQ
HLCNRDKQLSSKL
>gnl|CDD|176740 cd08326, CARD_CASP9, Caspase activation and recruitment domain of Caspase-9. Caspase activation and recruitment domain (CARD) similar to that found in caspase-9 (CASP9, MCH6, APAF3), which interacts with the CARD of apoptotic protease-activating factor 1 (APAF-1). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-9 is the initiator caspase associated with the intrinsic or mitochondrial pathway of apoptosis, induced by many pro-apoptotic signals. Together with APAF-1, it forms the heptameric 'apoptosome' in response to the release of cytochrome c from mitochondria. Activated caspase-9 cleaves and activates downstream effector caspases, like caspase-3, caspase-6, and caspase-7, resulting in apoptosis. In general, CARDs are death domains (DDs) associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
HRQILRRHRARLVEELQPKYLWDHLLSRGVFTPDMIEEIQAAGSRRDQARQLLIDLETRGKQAFPAFLSA
LRETGQTDLAELLR
>gnl|CDD|260037 cd08327, CARD_RAIDD, Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a death domain. Caspase activation and recruitment domain (CARD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal CARD, which interacts with the caspase-2 CARD, and a C-terminal Death domain (DD), which interacts with the DD of PIDD. In general, CARDs are DDs associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
MEPKHKQLLRSQRLELCAELLVDGLIVQYLYQEGILTESHVEEIQSQTTSRRKTLKLLDILPNRGPKAFH
AFLDSLEEFPWVRDKLLLLREEGE
>gnl|CDD|260038 cd08329, CARD_BIRC2_BIRC3, Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2). Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
EEMASDDLSLIRKNRMALFQHLTCVLPILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAA
AEVFRNCLKEIDVVLYRDLFVQKS
>gnl|CDD|260039 cd08330, CARD_ASC_NALP1, Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins. Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. In general, CARDs are death domains (DDs) associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALK
ETNPYLVEDLE
>gnl|CDD|260040 cd08332, CARD_CASP2, Caspase activation and recruitment domain of Caspase-2. Caspase activation and recruitment domain (CARD) similar to that found in caspase-2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Caspase-2 (also known as ICH1, NEDD2, or CASP2) is one of the most evolutionarily conserved caspases, and plays a role in apoptosis, DNA damage response, cell cycle regulation, and tumor suppression. It is localized in the nucleus and exhibits properties of both an initiator and an effector caspase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSA
FCEALRETSQEHLADLL
>gnl|CDD|260041 cd08333, DED_Caspase_8_r1, Death effector domain, repeat 1, of Caspase-8. Death effector domain (DED) found in caspase-8 (CASP8, FLICE), repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
FRKLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALFLALQEKGMLEEGNLSFLKELLFRIGRI
DLLTSHLGVSRE
>gnl|CDD|260042 cd08334, DED_Caspase_8_10_r2, Death effector domain, repeat 2, of initator caspases 8 and 10. Death Effector Domain (DED) found in caspase-8 and caspase-10, repeat 2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis, and they play partially redundant roles. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. They contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
ISPYRVLLYEISEDLTSEDLKSLKFLLSSKLPRRKLEKNKSALDVFVEMEKRGLLSEDNLDELKKILKSL
RPDLAKKINQYKE
>gnl|CDD|260043 cd08336, DED_FADD, Death Effector Domain found in Fas-Associated via Death Domain. Death Effector Domain (DED) found in Fas-Associated via Death Domain (FADD). DEDs comprise a subfamily of the Death Domain (DD) superfamily. FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor and its DED recruits the initiator caspases 8 and 10 to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes
DPFKVLLLEISKSLSDEELESLKFLCKDHIGKRKLEEVQSGLDLFEALEERDKLSPENTAFLRELLKSIG
REDLIRKLEEFE
>gnl|CDD|260044 cd08337, DED_c-FLIP_r1, Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein. Death Effector Domain (DED), repeat 1, similar to that found in FLICE-inhibitory protein (c-FLIP/CASH, also known as Casper/iFLICE/FLAME-1/CLARP/MRIT/usurpin). c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of the Death Inducing Signalling Complex (DISC). At low levels, c-FLIP has been shown to enhance apoptotic signaling by allosterically activating caspase-8. As a modulator of the initiator caspases, c-FLIP regulates life and death in various types of cells and tissues. All members contain two N-terminal DEDs and a C-terminal pseudo-caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
VSAEVLHQVEEELDTDEDEMLLFLCRDAAPDCTTAQLRDALCALNERGKLTLAGLAELLYRVKRFDLLKR
ILHLSKETVE
>gnl|CDD|260045 cd08338, DED_PEA15, Death Effector Domain of Astrocyte phosphoprotein PEA-15. Death Effector Domain (DED) similar to that found in PEA-15 (Astrocyte phosphoprotein PEA-15). PEA-15 is a multifunctional phosphoprotein that modulates signaling pathways, like the ERK MAP kinase cascade by binding to ERK and changing its subcellular localization. It has been implicated in apoptosis, cell proliferation, and glucose metabolism. It does not possess enzymatic activity and mainly acts as an adaptor protein. PEA-15 contains an N-terminal DED domain and a C-terminal disordered region. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes
GEYGSLLQDLTENITSEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLEKHNKLDQDNLSYIEHVFEISR
RPDLLTMVVDYRTK
>gnl|CDD|176750 cd08339, DED_DEDD-like, Death Effector Domain of DEDD and DEDD2. Death Effector Domain (DED) found in DEDD and DEDD2. Both proteins have a single N-terminal DED and a long C-terminal portion with no known domains. DEDD has been shown to block mitotic progression by inhibiting Cdk1 and to be involved in regulating the insulin signaling cascade. DEDD and DEDD2 can bind to themselves, to each other, and to the two tandem DED-containing caspases, caspase-8 and -10. In general, DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes
GLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDYERGMIRSGRDFLLALERQGRCDETNFRQVLQLLRI
ITRHDLLPYVTLKRRRAVCPDLVDKYL
>gnl|CDD|260046 cd08340, DED_c-FLIP_r2, Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein. Death Effector Domain (DED), repeat 2, similar to that found in cellular FLICE-inhibitory protein (c-FLIP/CASH, also known as Casper/iFLICE/FLAME-1/CLARP/MRIT/usurpin). c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of the Death Inducing Signalling Complex (DISC). At low levels, c-FLIP has been shown to enhance apoptotic signaling by allosterically activating caspase-8. As a modulator of the initiator caspases, c-FLIP regulates life and death in various types of cells and tissues. All members contain two N-terminal DEDs and a C-terminal pseudo-caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
SDYRVLMVCVSEELDKSDLRSLIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLLEDCLRNIR
RIDLCKKIQKY
>gnl|CDD|260047 cd08341, DED_Caspase_10_r1, Death effector domain, repeat 1, of Caspase-10. Death effector domain (DED) found in caspase-10, repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-10 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-8 and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
IKFNQQLLIIDENLGVEDIEALKFLCSDLLSNKKLEKVESGHDLFQHLMAEDLLNEEDYFLLAELLYIIR
HHKLLQKLGYTK
>gnl|CDD|319930 cd08342, HPPD_N_like, N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase (HmaS). HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of HPP to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_N_like domain represents the N-terminal domain
FDHVEFYVGNAKQAASYYSTGLGFEPVAYHGLETREKASHVLRQGDIRFVFTSPLSSDAPAADFLAKHGD
GVKDVAFRVEDADAAYERAVARGAKPVAEPVELSDEGGEVVIAAIQGYGDVVHTFVDRKGYKGPFLPGFE
P
>gnl|CDD|319931 cd08343, ED_TypeI_classII_C, C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain. This family contains the C-terminal, catalytic domain of type I, class II extradiol dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site; extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon, whereas intradiol enzymes cleave the aromatic ring between two hydroxyl groups. Extradiol dioxygenases are classified into type I and type II enzymes. Type I extradiol dioxygenases include class I and class II enzymes. These two classes of enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. The extradiol dioxygenases represented in this family are type I, class II enzymes, and are composed of the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. A catalytically essential metal, Fe(II) or Mn(II), presents in all the enzymes in this family
GHVVLCSPDVEASRDFYTDVLGFRVSDRIVDPGVDGGAFLHCDRGTDHHTVALAGGPHPGLHHVAFEVHD
LDDVGRGHDRLREKGYKIEWGPGRHGLGSQVFDYWFDPSGNRVEYYTDGDLVDDDWPPKVHD
>gnl|CDD|319932 cd08344, MhqB_like_N, N-terminal domain of MhqB, a type I extradiol dioxygenase, and similar proteins. This subfamily contains the N-terminal, non-catalytic, domain of Burkholderia sp. NF100 MhqB and similar proteins. MhqB is a type I extradiol dioxygenase involved in the catabolism of methylhydroquinone, an intermediate in the degradation of fenitrothion. The purified enzyme has shown extradiol ring cleavage activity toward 3-methylcatechol. Fe2+ was suggested as a cofactor, the same as most other enzymes in the family. Burkholderia sp. NF100 MhqB is encoded on the plasmid pNF1. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism
HSIDHFALEVPDLEVARRFYEAFGLDVRETGEDLELRAPGNDHVWARLIQGARKRLAYLSFGIFGDDLAR
FAAHLDAAGVALIAAPPGADPDGVWFEDPDGNLLQVRVADKA
>gnl|CDD|319933 cd08345, Fosfomycin_RP, Fosfomycin resistant protein. This family contains three types of fosfomycin resistant protein. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. The three types of fosfomycin resistance proteins, employ different mechanisms to render fosfomycin [(1R,2S)-epoxypropylphosphonic acid] inactive. FosB catalyzes the addition of L-cysteine to the epoxide ring of fosfomycin. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of configuration at C1. FosA catalyzes the addition of glutathione to the antibiotic fosfomycin, making it inactive. Catalytic activities of both FosX and FosA are Mn(II)-dependent, but FosB is activated by Mg(II). Fosfomycin resistant proteins are evolutionarily related to glyoxalase I and type I extradiol dioxygenases
HITLIVRDLEKSTAFLQDIFGAREVYSSGDKTFSLSKEKFFLLGGLWIALMEGESLQERSYTHIAFQIQS
EDFDRYAERLGALGVEMRPPRPRVEGEGRSIYFYDPDNHLFELHTGTL
>gnl|CDD|319934 cd08346, PcpA_N_like, N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins. The N-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases
GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGT
GQISRIGLRVPKGSLSFWAERLEKFGVPHSEVVTRFGEKYLRFEDPDGTRLFLV
>gnl|CDD|319935 cd08347, PcpA_C_like, C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins. The C-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases
GLHGVTLTVREPEETDAFLTNVFGFTEVGEEGDLVRLFAGGNGSGGVVDVLDDPDLPSAQQGYGTVHHVA
FRVADDEEQAAWKERLEELGFDNSGIVDRFYFESLYFREPGGVLFEIATDGPGFTVDEPPEELGEKLKLP
PFLEPRRAEIEAALPPL
>gnl|CDD|319936 cd08348, BphC2-C3-RGP6_C_like, The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases. This subfamily contains Rhodococcus globerulus P6 BphC2-RGP6 and BphC3-RGP6, and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, yielding 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid. This is the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Most type I extradiol dioxygenases are activated by Fe(II). Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, which form hexamers. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, its two domains do not belong to this subfamily
KLAHFVLRTNPEKFEAMVQWYLDILGARIVARNAKGCFLSFDEEHHRIAIFGAPGGAQPPDKRPTRVGLA
HIAFTYASLDDLARNYAQLKERGIKPVWPVNHGVTTSIYYRDPDGNMLEMQVDNFDTPDEATDFMKT
>gnl|CDD|319937 cd08349, BLMA_like, Bleomycin binding protein (BLMA) and similar proteins. BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. As for the larger superfamily, this family contains members with or without domain swapping
IPILPVRDIDKTLAFYVDVLGFEVDYERPPPGYAILSRGGVELHLFEHPGLDPAGSGVAAYIRVEDIDAL
HAELKAAGLPLFGIPRITPIEDKPWGMREFAVVDPDGNLLRFGQ
>gnl|CDD|319938 cd08350, BLMT_like, BLMT, a bleomycin resistance protein encoded on the transposon Tn5, and similar proteins. BLMT is a bleomycin (Bm) resistance protein, encoded by the ble gene on the transposon Tn5. This protein confers a survival advantage to Escherichia coli host cells. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMT has strong binding affinity to Bm and it protects against this lethal compound through drug sequestering. BLMT has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMT is a dimer with two Bm-binding pockets formed at the dimer interface
TDRATPNLPSRDFDATAAFYARLGFQTVYRDDGWMILRRGDLTLEFFPHPDLDPAASWFSCCLRVDDLDA
LYAQWSAAGIPEDTRGIPRLHPPQTQPWGIRMFALIDPDGSLLRLIQN
>gnl|CDD|319939 cd08351, ChaP_like, ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and similar proteins. ChaP is an enzyme involved in the biosynthesis of the potent antitumor agent chartreusin (cha). Cha is an aromatic polyketide glycoside produced by Streptomyces chartreusis. ChaP may play a role as a meta-cleavage dioxygenase in the oxidative rearrangement of the anthracyclic polyketide. ChaP belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases
ITLNHTIVPARDKEASARFLAEILGLPAPPPWGPFAPVRLNNGLTLDFADPRGEIAPQHYAFLVSDDEFD
AILARIRARGLEYWADPQHREPGEINHNDGGRGVYFRDPDGHLLEILT
>gnl|CDD|319940 cd08352, VOC_Bs_YwkD_like, vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins. uncharacterized subfamily of vicinal oxygen chelate (VOC) family contains Bacillus subtilis YwkD and similar proteins. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLALGGYQLELFIKPDAPARPSYPEALG
LRHLAFKVEDVEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE
>gnl|CDD|319941 cd08353, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
IKRMDHVGIVVEDLDAAIAFFTELGLELEGRMTVEGEWADRVVGLDGVRVEIAMLRTPDGHGRLELSKFL
TPAAIPGHRPAPANALGLRHVAFAVDDIDAVVARLRKHGAELVGEVVQYEDSYRLCYVRGPEGIIVELAE
EL
>gnl|CDD|319942 cd08354, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
ILETCLYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGPQVLLVFDPGATSKDVRTGEVPGHGASGHGH
FAFAVPTEELAAWEARLEAKGVPIESYTQWPEGGKSLYFRDPAGNLVELASA
>gnl|CDD|319943 cd08355, TioX_like, Micromonospora sp. TioX and similar proteins. Micromonospora sp. TioX is encoded by a gene of the thiocoraline biosynthetic gene cluster. Thiocoraline is a thiodepsipeptide with potent antitumor activity. TioX may be involved in thiocoraline resistance or secretion. TioX belongs to vicinal oxygen chelate (VOC) superfamily that is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
VVPTLRYRDAVAAIDWLVEAFGFEERMVVPGDEGTIHHAELTFGGGGVMVGSVRDEARPDRPADAGGHGT
QSVYVAVADPDAHYERARAAGAEIVMEPTDTDYGSRDYSARDPEGHLWSFGTY
>gnl|CDD|319944 cd08356, VOC_CChe_VCA0619_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. uncharacterized subfamily of vicinal oxygen chelate (VOC) family contains Vibrio cholerae VCA0619 and similar proteins. The VOC superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
IEIKAFVPAKDFELSKAFYQALGFELASEEGGVAYFRLGDCSFLLQDFYEKEHAENFMMHLLVEDVDAWH
QHVKTLGLAERYGVKVTDPTDQPWGMRDFVLTDPSGVLWRIGQ
>gnl|CDD|319945 cd08357, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and type I ring-cleaving dioxygenases. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
FHLAIPVRDLEAARDFYGDVLGCPEGRSSETWIDFNFFGHQVVAHLVPNYASTSTNAVDGHSVPVPHFGL
ALTVDDFDALAERLKAAGVKFYIEPYVRFEGEPGEQWTMFLLDPSGNALEFKAM
>gnl|CDD|319946 cd08358, GLOD4_N, N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins. Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
RRALHFVFKVGDRNKTIKFYREILGMKVLRHEEFEEGCKAACNGPYDGKWSKTMVGYGPEDDHFVVELTY
NYGIGDYELGNDFLGITIHSKQAVSRAKKHNWPVTQVGDGVYEVKAPGGYKFYLIDK
>gnl|CDD|319947 cd08359, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
QSLGPVIVTEDVAATAAFYVKHFGFRVIFDSDWYVSLRRAERHGFELAIMDGQHGAVPAASQTQSSGLII
NFEVDDADAEYERLTQAGLEFLEPPRDEPWGQRRFIVRDPNGVLIDVIQ
>gnl|CDD|319948 cd08360, MhqB_like_C, C-terminal domain of Burkholderia sp. NF100 MhqB and similar proteins. This subfamily contains the C-terminal, catalytic, domain of Burkholderia sp. NF100 MhqB and similar proteins. MhqB is a type I extradiol dioxygenase involved in the catabolism of methylhydroquinone, an intermediate in the degradation of fenitrothion. The purified enzyme has shown extradiol ring cleavage activity toward 3-methylcatechol. Fe2+ was suggested as a cofactor, the same as most other enzymes in the family. Burkholderia sp. NF100 MhqB is encoded on the plasmid pNF1. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism
PRRLGHVLLFSPDVDRSVDFYRDLLGLKVSDRSFDIIAFMRGAAGSDHHLIAFAKSSATGLHHMSWDVSD
VNEIGIGASQLLRAGYKDGWGLGRHVLGSNYFHYVRDPWGSFVEYSADIDYIPDDSGWVPGDFG
>gnl|CDD|319949 cd08361, PpCmtC_N, N-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC). This subfamily contains the N-terminal, non-catalytic, domain of PpCmtC. 2,3-dihydroxy-p-cumate-3,4-dioxygenase (CmtC of Pseudomonas putida F1) is a dioxygenase involved in the eight-step catabolism pathway of p-cymene. CmtC acts upon the reaction intermediate 2,3-dihydroxy-p-cumate, yielding 2-hydroxy-3-carboxy-6-oxo-7-methylocta-2,4-dienoate. The CmtC belongs to the type I family of extradiol dioxygenases. Fe2+ was suggested as a cofactor, same as other enzymes in the family. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism
MINLHDIRYVRLGTRDLEEAVRFATDILGLELVRREGGAAYFRSDDRDHTLCYFEGDPAEQTSGFEVRDP
AELDAAAAELESAGIAVRRGTAEECEQRRVRAFISFRDPSGNRIELVVRPHHSG
>gnl|CDD|319950 cd08362, BphC5-RrK37_N_like, N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Rhodococcus rhodochrous K37, and similar proteins. 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). The enzyme contains a N-terminal and a C-terminal domain of similar structure fold, resulting from an ancient gene duplication. BphC belongs to the type I extradiol dioxygenase family, which requires a metal in the active site for its catalytic activity. Polychlorinated biphenyl degrading bacteria demonstrate multiplicity of BphCs. Bacterium Rhodococcus rhodochrous K37 has eight genes encoding BphC enzymes. This family includes the N-terminal domain of BphC5-RrK37. The crystal structure of the protein from Novosphingobium aromaticivorans has a Mn(II)in the active site, although most proteins of type I extradiol dioxygenases are activated by Fe(II)
VTHLRYVALGVPDLAAEREFYTEVWGLEEVAEDDDVVYLRAEGSEHHVLRLRQSDENRLDLIAFAAATRA
DVDALAARLAAAGVRILSEPGPLDDPGGGYGFRFFDPDGRTIEVSADVAA
>gnl|CDD|319951 cd08363, FosB, fosfomycin resistant protein subfamily FosB. This subfamily family contains FosB, a fosfomycin resistant protein. FosB is a Mg(2+)-dependent L-cysteine thiol transferase. Fosfomycin inhibits the enzyme UDP-nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosB catalyzes the Mg(II) dependent addition of L-cysteine to the epoxide ring of fosfomycin, (1R,2S)-epoxypropylphosphonic acid, rendering it inactive. FosB is evolutionarily related to glyoxalase I and type I extradiol dioxygenases
INHITFSVSNLNKSIAFYKDVLDAKLLVLGEKTAYFDLNGLWLALNVQEDIPRNEISHSYTHIAFSIDEE
DLDAFKERLKDNGVNILEGRKRDILEGQSIYFTDPDGHLFELHTGTLEDRLEYYKEEKPHM
>gnl|CDD|319952 cd08364, FosX, fosfomycin resistant protein subfamily FosX. This subfamily family contains FosX, a fosfomycin resistant protein. FosX is a Mn(II)-dependent fosfomycin-specific epoxide hydrolase. Fosfomycin inhibits the enzyme UDP-Nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of the configuration at C1 in the presence of Mn(II). The hydrated fosfomycin loses the inhibition activity. FosX is evolutionarily related to glyoxalase I and type I extradiol dioxygenases
IEGISHITFIVKDLDRTAAFLTEIFGAEEVYDSGAETFSLSPEKFFLIGGLWIAIMEGEPLLERSYNHIA
FKVSEGDLDEYRARIKKLGLEIRPPRSRVQGEGRSLYFYDFDNHLFELHTGTLEERLARY
>gnl|CDD|176483 cd08365, APC10-like1, APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination. This model represens the APC10-like DOC1 domain of multi-domain proteins present in E3 ubiquitin ligases. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. APC10/DOC1 domains such as those present in HECT (Homologous to the E6-AP Carboxyl Terminus) and Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase proteins, HECTD3, and CUL7, respectively, are also included here. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling a SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, Fbx29 F-box protein, and ROC1 (RING-box protein 1) and promotes ubiquitination. CUL7 is a multi-domain protein with a C-terminal cullin domain that binds ROC1 and a centrally positioned APC10/DOC1 domain. HECTD3 contains a C-terminal HECT domain which contains the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain which is responsible for substrate recognition and binding. An APC10/DOC1 domain homolog is also present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT domain. Recent studies have shown that the protein complex HERC2-RNF8 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Also included in this hierarchy is an uncharacterized APC10/DOC1-like domain found in a multi-domain protein, which also contains CUB, zinc finger ZZ-type, and EF-hand domains. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here
TKCYVESIEVSSNPADASRLTDGNTSTYWQSDGSQGSHWIRLKMKPDVLVRHLSLAVDATDSSYMPQRVV
VAGGRSASNLQELRDVNIPPSVTGYVTLLEDATISQPYIEIRIKRCRSDGIDTRIHGLRIL
>gnl|CDD|176484 cd08366, APC10, APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination. This model represents the single domain protein APC10, a subunit of the anaphase-promoting complex (APC), which is a multi-subunit E3 ubiquitin ligase. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a vital component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC (also known as the cyclosome), is a cell cycle-regulated E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. In mitosis, the APC initiates sister chromatid separation by ubiquitinating the anaphase inhibitor securin and triggers exit from mitosis by ubiquitinating cyclin B. The C-terminus of APC10 binds to CDC27/APC3, an APC subunit that contains multiple tetratrico peptide repeats. APC10 domains are homologous to the DOC1 domains present in the HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein, and the Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase complex. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here
REIGSLAVWSLSSAKPGNGVDQLRDDSLDTYWQSDGPQPHLINIQFSKKTDISAVALYLDYKLDESYTPS
KISIRAGTSPHDLQEVRTVELEEPNGWVHIPLEDNRDGKPLRTFFLQIAILSNHQNGRDTHIRQIKVYG
>gnl|CDD|176262 cd08367, P53, P53 DNA-binding domain. P53 is a tumor suppressor gene product; mutations in p53 or lack of expression are found associated with a large fraction of all human cancers. P53 is activated by DNA damage and acts as a regulator of gene expression that ultimatively blocks progression through the cell cycle. P53 binds to DNA as a tetrameric transcription factor. In its inactive form, p53 is bound to the ring finger protein Mdm2, which promotes its ubiquitinylation and subsequent proteosomal degradation. Phosphorylation of p53 disrupts the Mdm2-p53 complex, while the stable and active p53 binds to regulatory regions of its target genes, such as the cyclin-kinase inhibitor p21, which complexes and inactivates cdk2 and other cyclin complexes
FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPN
HRQGDDGHTAPNSHVIRCENPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRP
IQLVFTLEDENGNVLGRRVIEVRVCACPGRDRKNEEKAA
>gnl|CDD|259829 cd08368, LIM, LIM is a small protein-protein interaction domain, containing two zinc fingers. LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid)
CAGCGKPIEGRELLRALGKKWHPECFKCAECGKPLGGDSFYEKDGKPYCEKCY
>gnl|CDD|187712 cd08369, FMT_core, Formyltransferase, catalytic core domain. Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis
IVILGSGNIGQRVLKALLSKEGHEIVGVVTHPDSPRGTAQLSLELVGGKVYLDSNINTPELLELLKEFAP
DLIVSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIA
QEVIPISPDDTAGTLYQRLIELGPKLLKEALQK
>gnl|CDD|187727 cd08370, FMT_C_like, Carboxy-terminal domain of Formyltransferase and similar domains. This family represents the C-terminal domain of formyltransferase and similar proteins. This domain is found in a variety of enzymes with formyl transferase and alkyladenine DNA glycosylase activities. The proteins with formyltransferase function include methionyl-tRNA formyltransferase, ArnA, 10-formyltetrahydrofolate dehydrogenase and HypX proteins. Although most proteins with formyl transferase activity contain this C-terminal domain, prokaryotic glycinamide ribonucleotide transformylase (GART), a single domain protein, only contains the core catalytic domain. Thus, the C-terminal domain is not required for formyl transferase catalytic activity and may be involved in substrate binding. Some members of this family have shown nucleic acid binding capacity. The C-terminal domain of methionyl-tRNA formyltransferase is involved in tRNA binding. Alkyladenine DNA glycosylase is a distant member of this family with very low sequence similarity to other members. It catalyzes the first step in base excision repair (BER) by cleaving damaged DNA bases within double-stranded DNA to produce an abasic site and shows ability to bind to DNA
LDAESLERTIRALPYQGARLEIDGERVRLLEAEVVDDVTNEARHSGKILFVDYQCITVATGDGALLITAL
QGL
>gnl|CDD|187740 cd08371, Lumazine_synthase-like, lumazine synthase and riboflavin synthase; involved in the riboflavin (vitamin B2) biosynthetic pathway. This superfamily contains lumazine synthase (6,7-dimethyl-8-ribityllumazine synthase, LS) and riboflavin synthase (RS). Both enzymes play important roles in the riboflavin biosynthetic pathway. Riboflavin is the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) which are essential cofactors for the catalysis of a wide range of redox reactions. These cofactors are also involved in many other processes involving DNA repair, circadian time-keeping, light sensing, and bioluminescence. Riboflavin is biosynthesized in plants, fungi and certain microorganisms; as animals lack the necessary enzymes to produce this vitamin, they acquire it from dietary sources. In the final steps of the riboflavin biosynthetic pathway, LS catalyzes the condensation of the 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy- 2-butanone-4-phosphate to release water, inorganic phosphate and 6,7-dimethyl-8-ribityllumazine (DMRL), and RS catalyzes a dismutation of DMRL which yields riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. In the latter reaction, a four-carbon moiety is transferred between two DMRL molecules serving as donor and acceptor, respectively. Both the LS and RS catalyzed reactions are thermodynamically irreversible and can proceed in the absence of a catalyst. In bacteria and eukaryotes, there are two types of LS: type-I LS forms homo-pentamers or icosahedrally arranged dodecamers of pentamers, type-II LS forms decamers (dimers of pentamers). In archaea LSs and RSs appear to have diverged early in the evolution of archaea from a common ancestor
VGIVDARFNRDIVDALVKGAIAELAELGGNIKIIVVTVPGAYEIPLAAKKLLEKEDYDAVVAIGVVIKGE
TYHFEIVAHEVSRGLMNLQLETDKPVIFGVLTPDNAEEQADERAKRGNKGEEAARAAVE
>gnl|CDD|197306 cd08372, EEP, Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily. This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins
VASYNVNGLNAATRASGIARWVRELDPDIVCLQEVKDSQYSAVALNQLLPEGYHQYQSGPSRKEGYEGVA
ILSKTPKFKIVEKHQYKFGEGDSGERRAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQLKEVLEFLKR
LRQPNSAPVVICGDFNVRPSEVDSENPSSMLRLFVALNLVDSFETLPHAYTFDTYMHNVKSRLDYIFVSK
SLLPSVKSSKILSDAARARIPSDHYPIEVTL
>gnl|CDD|176019 cd08373, C2A_Ferlin, C2 domain first repeat in Ferlin. Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology
LVVSLKNLPGLKGKGDRIAKVTFRGVKKKTRVLENELNPVWNETFEWPLAGSPDPDESLEIVVKDYEKVG
RNRLIGSATVSLQDLVSEGLLEVTEPLLDSNGRPTGATISLEVSYQPPDGAVGGWAD
>gnl|CDD|176020 cd08374, C2F_Ferlin, C2 domain sixth repeat in Ferlin. Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the sixth C2 repeat, C2E, and has a type-II topology
ELRVIVWNTRDVLNDDTNITGEKMSDIYVKGWLDGLEEDKQKTDVHYRSLDGEGNFNWRFVFPFDYLPAE
KKIVVIKKEHFWSLDETEYKIPPKLTLQVWDNDKFSPDDFLGSLELDLSILPRPAKTSKKCGL
>gnl|CDD|176021 cd08375, C2_Intersectin, C2 domain present in Intersectin. A single instance of the C2 domain is located C terminally in the intersectin protein. Intersectin functions as a scaffolding protein, providing a link between the actin cytoskeleton and the components of endocytosis and plays a role in signal transduction. In addition to C2, intersectin contains several additional domains including: Eps15 homology domains, SH3 domains, a RhoGEF domain, and a PH domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. The members here have topology I
EKAYLARSQRASGIGRLMVVIVEGRDLKPCNSNGKSDPYCEVSMGSQEHKTKVVSDTLNPKWNSSMQFFV
KDLEQDVLCITVFDRDFFSPDDFLGRTEIRVADILKETKESKGPITKRLLLHEVPTGEVVVKLDLQ
>gnl|CDD|176022 cd08376, C2B_MCTP_PRT, C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP). MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence, three C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology
VVTIVLVEGKNLPPMDDNGLSDPYVKFRLGNEKYKSKVCSKTLNPQWLEQFDLHLFDDQSQILEIEVWDK
DTGKKDEFIGRCEIDLSALPREQTHSLELELEDGEGSLLLLLTLTG
>gnl|CDD|176023 cd08377, C2C_MCTP_PRT, C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP). MCTPs are involved in Ca2+ signaling at the membrane. The cds in this family contain multiple C2 domains as well as a C-terminal PRT domain. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology
GFLQVKVIRASGLAAADIGGKSDPFCVLELVNARLQTHTIYKTLNPEWNKIFTFPIKDIHDVLEVTVYDE
DKDKKPEFLGKVAIPLLSIKNGERKWYALKDKKLRTRAKGSILLEMDVI
>gnl|CDD|176024 cd08378, C2B_MCTP_PRT_plant, C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset. MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology
YLYVRVVKARGLPANSNDPVVEVKLGNYKGSTKAIERTSNPEWNQVFAFSKDRLQGSTLEVSVWDKDKAK
DDFLGGVCFDLSEVPTRVPPDSPLAPQWYRLEDKKGGRVGGELMLAVWFGT
>gnl|CDD|176025 cd08379, C2D_MCTP_PRT_plant, C2 domain fourth repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset. MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the fourth C2 repeat, C2D, and has a type-II topology
ILEVGILGAQGLDVLRAKDGRGSTDAYCVAKYGPKWVRTRTVEDSSNPRWNEQYTWPVYDPCTVLTVGVF
DNSQSHWKEAVQPDVLIGKVRIRLSTLEDDRVYAHSYPLLSLNPSGVKKMGELECA
>gnl|CDD|176026 cd08380, C2_PI3K_like, C2 domain present in phosphatidylinositol 3-kinases (PI3Ks). C2 domain present in all classes of PI3Ks. PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. In addition some PI3Ks contain a Ras-binding domain and/or a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains members with the first C2 repeat, C2A, and a type-I topology, as well as some with a single C2 repeat
KSLWDINFNLRIKIHGITNINLLDSEDLKLYVRVQLYHGGEPLCPPQSTKKVPFSTSVTWNEWLTFDILI
SDLPREARLCLSIYAVSEPGSKKEVPLGWVNVPLFDYKGKLRQGMITLNLWPGKKTDPRIACTPCNNSNE
NSTRLLIELPEFSKPV
>gnl|CDD|176027 cd08381, C2B_PI3K_class_II, C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks). There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a N-terminal C2 domain, a PIK domain, and a kinase catalytic domain. Unlike class I and class III, class II PI3Ks have additionally a PX domain and a C-terminal C2 domain containing a nuclear localization signal both of which bind phospholipids though in a slightly different fashion. PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
GGQVKLSISYKNGTLFVMVMHAKNLPLLDGSDPDPYVKTYLLPDPQKTTKRKTKVVRKTRNPTFNEMLVY
DGLPVEDLQQRVLQVSVWSHDSLVENEFLGGVCIPLKKLDLSQETEKWYPLG
>gnl|CDD|176028 cd08382, C2_Smurf-like, C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins. A single C2 domain is found in Smurf proteins, C2-WW-HECT-domain E3s, which play an important role in the downregulation of the TGF-beta signaling pathway. Smurf proteins also regulate cell shape, motility, and polarity by degrading small guanosine triphosphatases (GTPases). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have type-II topology
KVRLTVLCADGLAKRDLFRLPDPFAVITVDGGQTHSTDVAKKTLDPKWNEHFDLTVGPSSIITIQVFDQK
KFKKKDQGFLGCVRIRANAVLPLKDTGYQRLDLRKLKKSDNLSVRGKIVVSLS
>gnl|CDD|176029 cd08383, C2A_RasGAP, C2 domain (first repeat) of Ras GTPase activating proteins (GAPs). RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain either a single C2 domain or two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology
SLRLRILEAKNLPSKGTRDPYCTVSLDQVEVARTKTVEKLNPFWGEEFVFDDPPPDVTFFTLSFYNKDKR
SKDRDIVIGKVALSKLDLGQGKDEWFPLTPVDPDSEVQGSVRLRARY
>gnl|CDD|176030 cd08384, C2B_Rabphilin_Doc2, C2 domain second repeat present in Rabphilin and Double C2 domain. Rabphilin is found neurons and in neuroendrocrine cells, while Doc2 is found not only in the brain but in tissues, including mast cells, chromaffin cells, and osteoblasts. Rabphilin and Doc2s share highly homologous tandem C2 domains, although their N-terminal structures are completely different: rabphilin contains an N-terminal Rab-binding domain (RBD),7 whereas Doc2 contains an N-terminal Munc13-1-interacting domain (MID). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
KILVSLMYNTQRRGLIVGIIRCVNLAAMDANGYSDPFVKLYLKPDAGKKSKHKTQVKKKTLNPEFNEEFF
YDIKHSDLAKKTLEITVWDKDIGKSNDYIGGLQLGINAKGERLRHWLDCLKNPDKKIEAWHTL
>gnl|CDD|176031 cd08385, C2A_Synaptotagmin-1-5-6-9-10, C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis as do synaptotagmins 5, 6, and 10. It is distinguished from the other synaptotagmins by having an N-glycosylated N-terminus. Synaptotagmins 5, 6, and 10, members of class 3 synaptotagmins, are located primarily in the brain and localized to the active zone and plasma membrane. They is distinguished from the other synaptotagmins by having disulfide bonds at its N-terminus. Synaptotagmin 6 also regulates the acrosome reaction, a unique Ca2+-regulated exocytosis, in sperm. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
KLGKLQFSLDYDFQSNQLTVGIIQAADLPAMDMGGTSDPYVKVYLLPDKKKKFETKVHRKTLNPVFNETF
TFKVPYSELGNKTLVFSVYDFDRFSKHDLIGEVRVPLLTVDLGHVTEEWRDLES
>gnl|CDD|176032 cd08386, C2A_Synaptotagmin-7, C2A domain first repeat present in Synaptotagmin 7. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
NLGRIQFSVSYDFQESTLTLKILKAVELPAKDFSGTSDPFVKIYLLPDKKHKLETKVKRKNLNPHWNETF
LFEGFPYEKLQQRVLYLQVLDYDRFSRNDPIGEVSLPLNKVDLTEEQTFWKDLKP
>gnl|CDD|176033 cd08387, C2A_Synaptotagmin-8, C2A domain first repeat present in Synaptotagmin 8. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
TRGELHFSLEYDKDMGILNVKLIQARNLQPRDFSGTADPYCKVRLLPDRSNTKQSKIHKKTLNPEFDESF
VFEVPPQELPKRTLEVLLYDFDQFSRDECIGVVELPLAEVDLSEKLDLWRKIQS
>gnl|CDD|176034 cd08388, C2A_Synaptotagmin-4-11, C2A domain first repeat present in Synaptotagmins 4 and 11. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmins 4 and 11, class 4 synaptotagmins, are located in the brain. Their functions are unknown. They are distinguished from the other synaptotagmins by having and Asp to Ser substitution in their C2A domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
KLGTLFFSLRYNSEKKALLVNIIECRDLPAMDEQSGTSDPYVKLQLLPEKEHKVKTRVLRKTRNPVYDET
FTFYGIPYNQLQDLSLHFAVLSFDRYSRDDVIGEVVCPLAGADLLNEGELLVSREIQP
>gnl|CDD|176035 cd08389, C2A_Synaptotagmin-14_16, C2A domain first repeat present in Synaptotagmins 14 and 16. Synaptotagmin 14 and 16 are membrane-trafficking proteins in specific tissues outside the brain. Both of these contain C-terminal tandem C2 repeats, but only Synaptotagmin 14 has an N-terminal transmembrane domain and a putative fatty-acylation site. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium and this is indeed the case here. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
KCGDLDVAFEYDPSARKLTVTVIRAQDIPTKDRGGASSWQVHLVLLPSKKQRAKTKVQRGPNPVFNETFT
FSRVEPEELNNMALRFRLYGVERMRKERLIGEKVVPLSQLNLEGETTVWLTLEP
>gnl|CDD|176036 cd08390, C2A_Synaptotagmin-15-17, C2A domain first repeat present in Synaptotagmins 15 and 17. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
GRLWFSVQYDLEEEQLTVSLIKARNLPPRTKDVAHCDPFVKVCLLPDERRSLQSKVKRKTQNPNFDETFV
FQVSFKELQRRTLRLSVYDVDRFSRHCIIGHVLFPLKDLDLVKGGVVWRDLEP
>gnl|CDD|176037 cd08391, C2A_C2C_Synaptotagmin_like, C2 domain first and third repeat in Synaptotagmin-like proteins. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains either the first or third repeat in Synaptotagmin-like proteins with a type-I topology
GVLRIHVIEAQDLVAKDKFVGGLVKGKSDPYVIVRVGAQTFKSKVIKENLNPKWNEVYEAVVDEVPGQEL
EIELFDEDPDKDDFLGRLSIDLGSVEKKGFIDEWLPLEDVKSGRLHLKLEW
>gnl|CDD|176038 cd08392, C2A_SLP-3, C2 domain first repeat present in Synaptotagmin-like protein 3. All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. SHD of Slp (except for the Slp4-SHD) function as a specific Rab27A/B-binding domain. In addition to Slp, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. Little is known about the expression or localization of Slp3. The C2A domain of Slp3 is Ca2+ dependent. It has been demonstrated that Slp3 promotes dense-core vesicle exocytosis. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
TGEIEFALHYNFRTSCLEITIKACRNLAYGDEKKKKCHPYVKVCLLPDKSHNSKRKTAVKKGTVNPVFNE
TLKYVVEADLLSSRQLQVSVWHSRTLKRRVFLGEVLIPLADWDFEDTDSQRFLWYPLN
>gnl|CDD|176039 cd08393, C2A_SLP-1_2, C2 domain first repeat present in Synaptotagmin-like proteins 1 and 2. All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike Slp3 and Slp4/granuphilin which are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
QGSVQFALDYDPKLRELHVHVIQCQDLAAADPKKQRSDPYVKTYLLPDKSNRGKRKTSVKKKTLNPVFNE
TLRYKVEREELPTRVLNLSVWHRDSLGRNSFLGEVEVDLGSWDWSNTQPTWYPLQ
>gnl|CDD|176040 cd08394, C2A_Munc13, C2 domain first repeat in Munc13 (mammalian uncoordinated) proteins. C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology
MSLLCVLVKKAKLDGAPDKFNTYVTLKVQNVKSTTIAVRGSQPCWEQDFMFEINRLDLGLVIELWNKGLI
WDTLVGTVWIPLSTIRQSNEEGPGEWLTLDSEVNMKNGQIVGTKDPTFHRILLDVRF
>gnl|CDD|176041 cd08395, C2C_Munc13, C2 domain third repeat in Munc13 (mammalian uncoordinated) proteins. C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins.C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology
KVTVKVVAANDLKWQTTGMFRPFVEVNLIGPHLSDKKRKFATKSKNNNWSPKYNETFQFILGNEDDPESY
ELHICVKDYCFARDDRLVGVTVLQLRDIAQAGSCACWLPLGRRIHMDETG
>gnl|CDD|176042 cd08397, C2_PI3K_class_III, C2 domain present in class III phosphatidylinositol 3-kinases (PI3Ks). PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. These are the only domains identified in the class III PI3Ks present in this cd. In addition some PI3Ks contain a Ras-binding domain and/or a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
LEGKVPLLSLSEKLEDPVLRFSGSNVSPNSDLFVTCQVFDDGKPLTLPVQTSYKPFKNRRNWNEWLTLPI
KYSDLPRNSQLAITIWDVSGTGKAVPFGGTTLSLFNKDGTLRRGRQKLRVWPDVEADGSIPTSTGKSPDS
ERDELDRLEKLLKKYERGE
>gnl|CDD|176043 cd08398, C2_PI3K_class_I_alpha, C2 domain present in class I alpha phosphatidylinositol 3-kinases (PI3Ks). PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. The members here are class I, alpha isoform PI3Ks and contain both a Ras-binding domain and a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-I topology
KSLWKINSNLRIKILCATYVNVNDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLDYDIYIPDL
PRSARLCLSICSVKGRKGAKEEHCPLAWGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNP
NKDTPCLELEFDRFSCVV
>gnl|CDD|176044 cd08399, C2_PI3K_class_I_gamma, C2 domain present in class I gamma phosphatidylinositol 3-kinases (PI3Ks). PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. The members here are class I, gamma isoform PI3Ks and contain both a Ras-binding domain and a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-I topology
FTVSLWDCDRKFRVKILGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNTWLEFDIK
IKDLPKGALLNLQIYCGKAPALSSKKSAESPSSESKGKHQLLYYVNLLLIDHRFLLRTGEYVLHMWQISG
KGEDQGSVNADKLTSATNPDKENSMSISILLDNYCHPV
>gnl|CDD|176045 cd08400, C2_Ras_p21A1, C2 domain present in RAS p21 protein activator 1 (RasA1). RasA1 is a GAP1 (GTPase activating protein 1), a Ras-specific GAP member, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA1 contains a C2 domain, a Ras-GAP domain, a pleckstrin homology (PH)-like domain, a SH3 domain, and 2 SH2 domains. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology
RQVRSLQLNVLEAHKLPVKHVPHPYCVISLNEVKVARTKVREGPNPVWSEEFVFDDLPPDVNSFTISLSN
KAKRSKDSEIAEVTVQLSKLQNGQETDEWYPLSSASPLKGGEWGSLRIRARYSHEL
>gnl|CDD|176046 cd08401, C2A_RasA2_RasA3, C2 domain first repeat present in RasA2 and RasA3. RasA2 and RasA3 are GAP1s (GTPase activating protein 1s), Ras-specific GAP members, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA2 and RasA3 are both inositol 1,3,4,5-tetrakisphosphate-binding proteins and contain an N-terminal C2 domain, a Ras-GAP domain, a pleckstrin-homology (PH) domain which localizes it to the plasma membrane, and Bruton's Tyrosine Kinase (BTK) a zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
SLKIKIGEAKNLPPRSGPNKMRDCYCTVNLDQEEVFRTKTVEKSLCPFFGEDFYFEIPRTFRHLSFYIYD
RDVLRRDSVIGKVAIKKEDLHKYYGKDTWFPLQPVDADSEVQGKVHLELRL
>gnl|CDD|176047 cd08402, C2B_Synaptotagmin-1, C2 domain second repeat present in Synaptotagmin 1. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of the class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis. It, like synaptotagmin-2, has an N-glycosylated N-terminus. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
LGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKRTLNPYYNES
FSFEVPFEQIQKVHLIVTVLDYDRIGKNDPIGKVVLGCNATGAELRHWSDMLASPRRPIAQWHTLQ
>gnl|CDD|176048 cd08403, C2B_Synaptotagmin-3-5-6-9-10, C2 domain second repeat present in Synaptotagmins 3, 5, 6, 9, and 10. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 3, a member of class 3 synaptotagmins, is located in the brain and localized to the active zone and plasma membrane. It functions as a Ca2+ sensor for fast exocytosis. It, along with synaptotagmins 5,6, and 10, has disulfide bonds at its N-terminus. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
GELMFSLCYLPTAGRLTLTIIKARNLKAMDITGFSDPYVKVSLMCEGRRLKKKKTSVKKNTLNPTYNEAL
VFDVPPENVDNVSLIIAVVDYDRVGHNELIGVCRVGPNADGQGREHWNEMLANPRKPIAQWHQL
>gnl|CDD|176049 cd08404, C2B_Synaptotagmin-4, C2 domain second repeat present in Synaptotagmin 4. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
RGELLLSLCYQPTTNRLTVVVLKARHLPKMDVSGLADPYVKVNLYYGKKRISKKKTHVKKCTLNPVFNES
FVFDIPSEELEDISVEFLVLDSDRVTKNEVIGRLVLGPKASGSGGHHWKEVCNPPRRQIAEWHMLC
>gnl|CDD|176050 cd08405, C2B_Synaptotagmin-7, C2 domain second repeat present in Synaptotagmin 7. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
RGELLLSLCYNPTANRITVNIIKARNLKAMDINGTSDPYVKVWLMYKDKRVEKKKTVIKKRTLNPVFNES
FIFNIPLERLRETTLIITVMDKDRLSRNDLIGKIYLGWKSGGLELKHWKDMLSKPRQPVAQWHRLK
>gnl|CDD|176051 cd08406, C2B_Synaptotagmin-12, C2 domain second repeat present in Synaptotagmin 12. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 12, a member of class 6 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmins 8 and 13, do not have any consensus Ca2+ binding sites. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
VGEILLSLSYLPTAERLTVVVVKARNLVWDNGKTTADPFVKVYLLQDGRKISKKKTSVKRDDTNPIFNEA
MIFSVPAIVLQDLSLRVTVAESTEDGKTPNVGHVIIGPAASGMGLSHWNQMLASLRKPVAMWHPLR
>gnl|CDD|176052 cd08407, C2B_Synaptotagmin-13, C2 domain second repeat present in Synaptotagmin 13. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 13, a member of class 6 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmins 8 and 12, does not have any consensus Ca2+ binding sites. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
TGEVLLSISYLPAANRLLVVVIKAKNLHSDQLKLLLGIDVSVKVTLKHQNAKLKKKQTKRAKHKINPVWN
EMIMFELPSELLAASSVELEVLNQDSPGQSLPLGRCSLGLHTSGTERQHWEEMLDNPRRQIAMWHQLH
>gnl|CDD|176053 cd08408, C2B_Synaptotagmin-14_16, C2 domain second repeat present in Synaptotagmins 14 and 16. Synaptotagmin 14 and 16 are membrane-trafficking proteins in specific tissues outside the brain. Both of these contain C-terminal tandem C2 repeats, but only Synaptotagmin 14 has an N-terminal transmembrane domain and a putative fatty-acylation site. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium and this is indeed the case here. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
VPELLLGLEYNALTGRLSVEVIKGSNFKNLAMNKAPDTYVKLTLLNSDGQEISKSKTSIRRGQPDPEFKE
TFVFQVALFQLSEVTLMFSVYNKRKMKRKEMIGWFSLGLNSSGEEEEEHWNEMKESKGQQVCRWHTLL
>gnl|CDD|176054 cd08409, C2B_Synaptotagmin-15, C2 domain second repeat present in Synaptotagmin 15. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
LGDIQISLTYNPTLNRLTVVVLRARGLRQLDHAHTSVYVKVSLMIHNKVVKTKKTEVVDGAASPSFNESF
SFKVTSRQLDTASLSLSVMQSGGVRKSKLLGRVVLGPFMYARGKELEHWNDMLSKPKELIKRWHALG
>gnl|CDD|176055 cd08410, C2B_Synaptotagmin-17, C2 domain second repeat present in Synaptotagmin 17. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology
GELLLSLNYLPSAGRLNVDIIRAKQLLQTDMSQGSDPFVKIQLVHGLKLIKTKKTSCMRGTIDPFYNESF
SFKVPQEELENVSLVFTVYGHNVKSSNDFIGRIVIGQYSSGPSETNHWRRMLNSQRTAVEQWHSL
>gnl|CDD|176103 cd08411, PBP2_OxyR, The C-terminal substrate-binding domain of the LysR-type transcriptional regulator OxyR, a member of the type 2 periplasmic binding fold protein superfamily. OxyR senses hydrogen peroxide and is activated through the formation of an intramolecular disulfide bond. The OxyR activation induces the transcription of genes necessary for the bacterial defense against oxidative stress. The OxyR of LysR-type transcriptional regulator family is composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The C-terminal domain also contains the redox-active cysteines that mediate the redox-dependent conformational switch. Thus, the interaction between the OxyR-tetramer and DNA is notably different between the oxidized and reduced forms. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GPLRLGVIPTIAPYLLPRLLPALRQAYPKLRLYLREDQTERLLEKLRSGELDAALLALPVDEPGLEEEPL
FDEPFLLAVPKDHPLAKRKSVTPEDLAGERLLLLEEGHCLRDQALELCRLAGAREQTDFEATSLETLRQM
VAAGLGITLLPELAVPSEELRGDRLVVRPFAEPAPSRTIGLVWRRSSPRAAAFEALAELI
>gnl|CDD|176104 cd08412, PBP2_PAO1_like, The C-terminal substrate-binding domain of putative LysR-type transcriptional regulator PAO1-like, a member of the type 2 periplasmic binding fold protein superfamily. This family includes the C-terminal substrate domain of a putative LysR-type transcriptional regulator from the plant pathogen Pseudomonas aeruginosa PAO1and its closely related homologs. The LysR-type transcriptional regulators (LTTRs) are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of N2 fixing bacteria, and synthesis of virulence factors, to a name a few. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate-binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLRIGCFSTLAPYYLPGLLRRFREAYPGVEVRVVEGNQEELEEGLRSGELDLALTYDLDLPEDIAFEPLA
RLPPYVWLPADHPLAGKDEVSLADLAAEPLILLDLPHSREYFLSLFAAAGLTPRIAYRTSSFEAVRSLVA
NGLGYSLLNDRPYRPWSYDGKRLVRRPLADPVPPLRLGLAWRRGARLTRAARAFVDFA
>gnl|CDD|176105 cd08413, PBP2_CysB_like, The C-terminal substrate domain of LysR-type transcriptional regulators CysB-like contains type 2 periplasmic binding fold. CysB is a transcriptional activator of genes involved in sulfate and thiosulfate transport, sulfate reduction, and cysteine synthesis. In Escherichia coli, the regulation of transcription in response to sulfur source is attributed to two transcriptional regulators, CysB and Cbl. CysB, in association with Cbl, downregulates the expression of ssuEADCB operon which is required for the utilization of sulfur from aliphatic sulfonates, in the presence of cysteine. Also, Cbl and CysB together directly function as transcriptional activators of tauABCD genes, which are required for utilization of taurine as sulfur source for growth. Like many other members of the LTTR family, CysB is composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate-binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
QLTIATTHTQARYVLPPVIAAFRKRYPKVKLSLHQGTPSQIAEMVLKGEADIAIATEALDDHPDLVTLPC
YRWNHCVIVPPGHPLADLGPLTLEDLAQYPLITYDFGFTGRSSIDRAFARAGLEPNIVLTALDADVIKTY
VRLGLGVGIIAEMAYDPQRDADLVALDAGHLFGPNTTRIALRRGTYLRSYAYDFIELF
>gnl|CDD|176106 cd08414, PBP2_LTTR_aromatics_like, The C-terminal substrate binding domain of LysR-type transcriptional regulators involved in the catabolism of aromatic compounds and that of other related regulators, contains type 2 periplasmic binding fold. This CD includes the C-terminal substrate binding domain of LTTRs involved in degradation of aromatic compounds, such as CbnR, BenM, CatM, ClcR and TfdR, as well as that of other transcriptional regulators clustered together in phylogenetic trees, including XapR, HcaR, MprR, IlvR, BudR, AlsR, LysR, and OccR. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate-binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
RLRIGFVGSALYGLLPRLLRRFRARYPDVELELREMTTAEQLEALRAGRLDVGFVRPPPDPPGLASRPLL
REPLVVALPADHPLAARESVSLADLADEPFVLFPREPGPGLYDQILALCRRAGFTPRIVQEASDLQTLLA
LVAAGLGVALVPASVARLQRPGVVYRPLADPPPRSELALAWRRDNASPALRAFLELA
>gnl|CDD|176107 cd08415, PBP2_LysR_opines_like, The C-terminal substrate-domain of LysR-type transcriptional regulators involved in the catabolism of opines and that of related regulators, contains the type 2 periplasmic binding fold. This CD includes the C-terminal substrate-domain of LysR-type transcriptional regulators, OccR and NocR, involved in the catabolism of opines and that of LysR for lysine biosynthesis which clustered together in phylogenetic trees. Opines, such as octopine and nopaline, are low molecular weight compounds found in plant crown gall tumors that are produced by the parasitic bacterium Agrobacterium. There are at least 30 different opines identified so far. Opines are utilized by tumor-colonizing bacteria as a source of carbon, nitrogen, and energy. NocR and OccR belong to the family of LysR-type transcriptional regulators that positively regulates the catabolism of nopaline and octopine, respectively. Both nopaline and octopalin are arginine derivatives. In Agrobacterium tumefaciens, NocR regulates expression of the divergently transcribed nocB and nocR genes of the nopaline catabolism (noc) region. OccR protein activates the occQ operon of the Ti plasmid in response to octopine. This operon encodes proteins required for the uptake and catabolism of octopine. The occ operon also encodes the TraR protein, which is a quorum-sensing transcriptional regulator of the Ti plasmid tra regulon. LysR is the transcriptional activator of lysA gene encoding diaminopimelate decarboxylase, an enzyme that catalyses the decarboxylation of diaminopimelate to produce lysine. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLRIAALPALALSLLPRAIARFRARHPDVRISLHTLSSSTVVEAVLSGQADLGLASLPLDHPGLESEPLA
SGRAVCVLPPGHPLARKDVVTPADLAGEPLISLGRGDPLRQRVDAAFERAGVEPRIVIETQLSHTACALV
AAGLGVAIVDPLTAAGYAGAGLVVRPFRPAIPFEFALVRPAGRPLSRLAQAFIDLL
>gnl|CDD|176108 cd08416, PBP2_MdcR, The C-terminal substrate-binding domian of LysR-type transcriptional regulator MdcR, which involved in the malonate catabolism contains the type 2 periplasmic binding fold. This family includes the C-terminal substrate binding domain of LysR-type transcriptional regulator (LTTR) MdcR that controls the expression of the malonate decarboxylase (mdc) genes. Like other members of the LTTRs, MdcR is a positive regulatory protein for its target promoter and composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins (PBP2). The PBP2 are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate- binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
RLRLGSLYSLTVNTVPRIIMGLKLRRPELDIELTLGSNKDLLKKLKDGELDAILVATPEGLNDPDFEVVP
LFEDDIFLAVPATSPLAASSEIDLRDLKDEKFVTLSEGFATYRGFDEAFEIAGFEPNVVMRVNDIFSLMS
MVSGGVGYALLPGRIADVYEDKVQLIPLAEPYQIRQTIGLVFLRSRERDPNLLALAAEC
>gnl|CDD|176109 cd08417, PBP2_Nitroaromatics_like, The C-terminal substrate binding domain of LysR-type transcriptional regulators that involved in the catabolism of nitroaromatic/naphthalene compounds and that of related regulators; contains the type 2 periplasmic binding fold. This CD includes the C-terminal substrate binding domain of LysR-type transcriptional regulators involved in the catabolism of dinitrotoluene and similar compounds, such as DntR, NahR, and LinR. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. Also included are related LysR-type regulators clustered together in phylogenetic trees, including NodD, ToxR, LeuO, SyrM, TdcA, and PnbR. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TFRIAASDYLEALLLPPLLARLRQEAPGVRLRFVPLDRDDLEEALESGEIDLAIGVFPELPPGLRSQPLF
EDRFVCVARKDHPLAGGPLTLEDYLAAPHVLVSPRGRGHGLVDDALAELGLSRRVALTVPHFLAAPALVA
GTDLIATVPRRLAEALAERLGLRVLPLPFELPPFTVSLYWHPRRDRDPAHRWLRELIAEL
>gnl|CDD|176110 cd08418, PBP2_TdcA, The C-terminal substrate binding domain of LysR-type transcriptional regulator TdcA, which is involved in the degradation of L-serine and L-threonine, contains the type 2 periplasmic binding fold. TdcA, a member of the LysR family, activates the expression of the anaerobically-regulated tdcABCDEFG operon which is involved in the degradation of L-serine and L-threonine to acetate and propionate, respectively. The tdc operon is comprised of one regulatory gene tdcA and six structural genes, tdcB to tdcG. The expression of the tdc operon is affected by several transcription factors including the cAMP receptor protein (CRP), integration host factor (IHF), histone-like protein (HU), and the operon specific regulators TdcA and TcdR. TcdR is divergently transcribed from the operon and encodes a small protein that is required for efficient expression of the Escherichia coli tdc operon. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
KVSIGVSSLIAHTLMPAVINRFKEQFPDVQISIYEGQLSSLLPELRDGRLDFAIGTLPDEMYLKELISEP
LFESDFVVVARKDHPLQGARSLEELLDASWVLPGTRMGYYNNLLEALRRLGYNPRVAVRTDSIVSIINLV
EKADFLTILSRDMGRGPLDSFRLITIPVEEPLPSADYYLIYRKKSRLTPLAEQLVELFRRY
>gnl|CDD|176111 cd08419, PBP2_CbbR_RubisCO_like, The C-terminal substrate binding of LysR-type transcriptional regulator (CbbR) of RubisCO operon, which is involved in the carbon dioxide fixation, contains the type 2 periplasmic binding fold. CbbR, a LysR-type transcriptional regulator, is required to activate expression of RubisCO, one of two unique enzymes in the Calvin-Benson-Bassham (CBB) cycle pathway. All plants, cyanobacteria, and many autotrophic bacteria use the CBB cycle to fix carbon dioxide. Thus, this cycle plays an essential role in assimilating CO2 into organic carbon on earth. The key CBB cycle enzyme is ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO), which catalyzes the actual CO2 fixation reaction. The CO2 concentration affects the expression of RubisCO genes. It has also shown that NADPH enhances the DNA-binding ability of the CbbR. RubisCO is composed of eight large (CbbL) and eight small subunits (CbbS). The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
RLRLAVVSTAKYFAPRLLGAFCRRHPGVEVSLRVGNREQVLERLADNEDDLAIMGRPPEDLDLVAEPFLD
NPLVVIAPPDHPLAGQKRIPLERLAREPFLLREPGSGTRLAMERFFAEHGVTLRVRMELGSNEAIKQAVM
AGLGLSVLSLHTLALELATGRLAVLDVEGFPIRRQWYVVHRKGKRLSPAAQAFLDFL
>gnl|CDD|176112 cd08420, PBP2_CysL_like, C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which activates the transcription of the cysJI operon encoding sulfite reductase, contains the type 2 periplasmic binding fold. CysL, also known as YwfK, is a regular of sulfur metabolism in Bacillus subtilis. Sulfur is required for the synthesis of proteins and essential cofactors in all living organism. Sulfur can be assimilated either from inorganic sources (sulfate and thiosulfate), or from organic sources (sulfate esters, sulfamates, and sulfonates). CysL activates the transcription of the cysJI operon encoding sulfite reductase, which reduces sulfite to sulfide. Both cysL mutant and cysJI mutant are unable to grow using sulfate or sulfite as the sulfur source. Like other LysR-type regulators, CysL also negatively regulates its own transcription. In Escherichia coli, three LysR-type activators are involved in the regulation of sulfur metabolism: CysB, Cbl and MetR. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLRIGASTTIGEYLLPRLLARFRKRYPEVRVSLTIGNTEEIAERVLDGEIDLGLVEGPVDHPDLIVEPFA
EDELVLVVPPDHPLAGRKEVTAEELAAEPWILREPGSGTREVFERALAEAGLDGLDLNIVMELGSTEAIK
EAVEAGLGISILSRLAVRKELELGRLVALPVEGLRLTRPFSLIYHKDKYLSPAAEAFLEFL
>gnl|CDD|176113 cd08421, PBP2_LTTR_like_1, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold. LysR-transcriptional regulators comprise the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
HVRLLANTSAIVEFLPEDLASFLAAHPDVRIDLEERLSADIVRAVAEGRADLGIVAGNVDAAGLETRPYR
TDRLVVVVPRDHPLAGRASVAFADTLDHDFVGLPAGSALHTFLREAAARLGRRLRLRVQVSSFDAVCRMV
AAGLGIGIVPESAARRYARALGLRVVPLDDAWARRRLLLCVRSFDALPPAARALVDHL
>gnl|CDD|176114 cd08422, PBP2_CrgA_like, The C-terminal substrate binding domain of LysR-type transcriptional regulator CrgA and its related homologs, contains the type 2 periplasmic binding domain. This CD includes the substrate binding domain of LysR-type transcriptional regulator (LTTR) CrgA and its related homologs. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis further showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GRLRISAPVSFGRLHLAPLLAEFLARYPDVRLELVLSDRLVDLVEEGFDLAIRIGELPDSSLVARRLGPV
RRVLVASPAYLARHGTPQTPEDLARHRCLGYRLPGRPLRWRFRRGGGEVEVRVRGRLVVNDGEALRAAAL
AGLGIALLPDFLVAEDLASGRLVRVLPDWRPPPLPIYAVYPSRRHLPAKVRAFIDFL
>gnl|CDD|176115 cd08423, PBP2_LTTR_like_6, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold. LysR-transcriptional regulators comprise the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLRVGAFPTAAAALLPPALAALRARHPGLEVRLREAEPPESLDALRAGELDLAVVFDYPVTPPPDDPGLT
RVPLLDDPLDLVLPADHPLAGREEVALADLADEPWIAGCPGSPCHRWLVRACRAAGFTPRIAHEADDYAT
VLALVAAGLGVALVPRLALGARPPGVVVRPLRPPPTRRIYAAVRAGAARRPAVAAALEAL
>gnl|CDD|176116 cd08425, PBP2_CynR, The C-terminal substrate-binding domain of the LysR-type transcriptional regulator CynR, contains the type 2 periplasmic binding fold. CynR is a LysR-like transcriptional regulator of the cyn operon, which encodes genes that allow cyanate to be used as a sole source of nitrogen. The operon includes three genes in the following order: cynT (cyanate permease), cynS (cyanase), and cynX (a protein of unknown function). CynR negatively regulates its own expression independently of cyanate. CynR binds to DNA and induces bending of DNA in the presence or absence of cyanate, but the amount of bending is decreased by cyanate. The CynR of LysR-type transcriptional regulator family is composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins (PBP2). The PBP2 are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GSLRLAMTPTFTAYLIGPLIDRFHARYPGIALSLREMPQERIEAALADDRLDLGIAFAPVRSPDIDAQPL
FDERLALVVGATHPLAQRRTALTLDDLAAEPLALLSPDFATRQHIDRYFQKQGIKPRIAIEANSISAVLE
VVRRGRLATILPDAIAREQPGLCAVALEPPLPGRTAALLRRKGAYRSAAARAFAALA
>gnl|CDD|176117 cd08426, PBP2_LTTR_like_5, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold. LysR-transcriptional regulators comprise the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
RVRVATGEGLAAELLPSLIARFRQRYPGVFFTVDVASTADVLEAVLSGEADIGLAFSPPPEPGIRVHSRQ
PAPIGAVVPPGHPLARQPSVTLAQLAGYPLALPPPSFSLRQILDAAFARAGVQLEPVLISNSIETLKQLV
AAGGGISLLTELAVRREIRRGQLVAVPLADPHMNHRQLELQTRAGRQLPAAASAFLQLL
>gnl|CDD|176118 cd08427, PBP2_LTTR_like_2, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold. LysR-transcriptional regulators comprise the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
RLRLGAIATVLTGLLPRALARLRRRHPDLEVHIVPGLSAELLARVDAGELDAAIVVEPPFPLPKDLVWTP
LVREPLVLIAPAELAGDDPRELLATQPFIRYDRSAWGGRLVDRFLRRQGIRVREVMELDSLEAIAAMVAQ
GLGVAIVPDIAVPLPAGPRVRVLPLGDPAFSRRVGLLWRRSSPRSRLIQALLEAL
>gnl|CDD|176119 cd08428, PBP2_IciA_ArgP, The C-terminal substrate binding domain of LysR-type transcriptional regulator, ArgP (IciA), for arginine exporter (ArgO); contains the type 2 periplasmic binding fold. The inhibitor of chromosomal replication (iciA) protein encoded by Mycobacterium tuberculosis, which is implicated in chromosome replication initiation in vitro, has been identified as arginine permease (ArgP), a LysR-type transcriptional regulator for arginine outward transport, based on the same amino sequence and similar DNA binding targets. Arp has been shown to regulate various targets including DnaA (replication), ArgO (arginine export), dapB (lysine biosynthesis), and gdhA (glutamate biosynthesis). With abundant nutrition, ArgP activates the DnaA gene (to increase replication) and the ArgO (to export redundant molecules). However, when nutrition supply is limited, it is suggested that ArgP might function as an inhibitor of chromosome replication in order to slow replication. This substrate-binding domain has significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLPVAVNADSLATWFLPALAPVLKRERILLDLIVDDEDRTHDLLRDGEVVGCISTQAQPMQGCRSDYLGS
MDYLLVASPDFAARYFPNGLTREALLKAPAVAFNRKDDLHQSFLQQHFGLPPGSYPCHYVPSSEAFVDLA
AQGLAYGMIPELQIEPELASGELIDLAPGHLLRVTLYWHRWNLESGLMKRLSRAL
>gnl|CDD|176120 cd08429, PBP2_NhaR, The C-terminal substrate binding domain of LysR-type transcriptional activator of the nhaA gene, encoding Na+/H+ antiporter, contains the type 2 periplasmic binding fold. NhaR is a positive regulator of the LysR family and is known to be an activator of the nhaA gene encoding a Na(+)/H(+) antiporter. In Escherichia coli, NhaA is the vital antiporter that protects against high sodium stress, and it is essential for growth in high sodium levels, while NhaB becomes essential only if NhaA is not available. The nhaA gene of nhaAR operon is induced by monovalent cations. The nhaR of the operon activates nhaAR, as well as the osmC transcription which is induced at elevated osmolarity. OsmC is transcribed from the two overlapping promoters (osmCp1 and osmP2) and that NhaR is shown to activate only the expression of osmCp1. NhaR also activates the transcription of the pgaABCD operon which is required for production of the biofilm adhesion, poly-beta-1,6-N-acetyl-d-glucosamine (PGA) .Thus, it is suggested that NhaR has an extended role in promoting bacterial survival. This substrate-binding domain has significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
LFRVGVADAVPKSIAYRLLEPAMDLHEPIRLVCREGKLEQLLADLALHRLDMVLADRPMPSSLDVKGYSH
RLGECGVSFFAAPPLAKRLEKPFPASLDEAPLLLPGEDSALRRKLLQWFERQGLRPQIVGEFDDSALMKA
FGQAGAGIFAAPTVIADEVARQYGVVEIGRTDEVVEEFYAISVERRITHPAVVAISEAARSALF
>gnl|CDD|176121 cd08430, PBP2_IlvY, The C-terminal substrate binding of LysR-type transcriptional regulator IlvY, which activates the expression of ilvC gene that encoding acetohydroxy acid isomeroreductase for the biosynthesis of branched amino acids; contains the type 2 periplasmic binding fold. In Escherichia coli, IlvY is required for the regulation of ilvC gene expression that encodes acetohydroxy acid isomeroreductase (AHIR), a key enzyme in the biosynthesis of branched-chain amino acids (isoleucine, valine, and leucine). The ilvGMEDA operon genes encode remaining enzyme activities required for the biosynthesis of these amino acids. Activation of ilvC transcription by IlvY requires the additional binding of a co-inducer molecule (either alpha-acetolactate or alpha-acetohydoxybutyrate, the substrates for AHIR) to a preformed complex of IlvY protein-DNA. Like many other LysR-family members, IlvY negatively auto-regulates the transcription of its own divergently transcribed ilvY gene in an inducer-independent manner. This substrate-binding domain has significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
ELSLYCSVTASYSFLPPILERFRAQHPQVEIKLHTGDPADAIDKVLNGEADIAIAARPDKLPARLAFLPL
ATSPLVFIAPNIACAVTQQLSQGEIDWSRLPFILPERGLARERLDQWFRRRGIKPNIYAQVAGHEAIVSM
VALGCGVGIVPELVLDNSPLKDKVRILEVQPELEPFEVGLCCLKKRLNEPLIKAFWQVA
>gnl|CDD|176122 cd08431, PBP2_HupR, The C-terminal substrate binding domain of LysR-type transcriptional regulator, HupR, which regulates expression of the heme uptake receptor HupA; contains the type 2 periplasmic binding fold. HupR, a member of the LysR family, activates hupA transcription under low-iron conditions in the presence of hemin. The expression of many iron-uptake genes, such as hupA, is regulated at the transcriptional level by iron and an iron-binding repressor protein called Fur (ferric uptake regulation). Under iron-abundant conditions with heme, the active Fur repressor protein represses transcription of the iron-uptake gene hupA, and prevents transcriptional activation via HupR. Under low-iron conditions with heme, the Fur repressor is inactive and transcription of the hupA is allowed. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
ELRIAIDTVLPLQPLYPLIAEFYQLNKATRIRLSEEVLGGTWDALASGRADLVIGATGELPPGGVKTRPL
GEVEFVFAVAPNHPLAKLDGPLDASAIKQYPAIVVADTSRNLPPRSSGLLEGQDRIRVPTMQAKIDAQVL
GLGVGYLPRHLAKPELASGELVEKALEDPRPPQELFLAWRKDQRGKALAWFVQRL
>gnl|CDD|176123 cd08432, PBP2_GcdR_TrpI_HvrB_AmpR_like, The C-terminal substrate domain of LysR-type GcdR, TrPI, HvR and beta-lactamase regulators, and that of other closely related homologs; contains the type 2 periplasmic binding fold. This CD includes the C-terminal substrate domain of LysR-type transcriptional regulators involved in controlling the expression of glutaryl-CoA dehydrogenase (GcdH), S-adenosyl-L-homocysteine hydrolase, cell division protein FtsW, tryptophan synthase, and beta-lactamase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
VLTVSVTPSFAARWLIPRLARFQARHPDIDLRLSTSDRLVDFAREGIDLAIRYGDGDWPGLEAERLMDEE
LVPVCSPALLAGLPLLSPADLARHTLLHDATRPEAWQWWLWAAGVADVDARRGPRFDDSSLALQAAVAGL
GVALAPRALVADDLAAGRLVRPFDLPLPSGGAYYLVYPPGRAESPAVAAFRDWL
>gnl|CDD|176124 cd08433, PBP2_Nac, The C-teminal substrate binding domain of LysR-like nitrogen assimilation control (NAC) protein, contains the type 2 periplasmic binding fold. The NAC is a LysR-type transcription regulator that activates expression of operons such as hut (histidine utilization) and ure (urea utilization), allowing use of non-preferred (poor) nitrogen sources, and represses expression of operons, such as glutamate dehydrogenase (gdh), allowing assimilation of the preferred nitrogen source. The expression of the nac gene is fully dependent on the nitrogen regulatory system (NTR) and the sigma54-containing RNA polymerase (sigma54-RNAP). In response to nitrogen starvation, NTR system activates the expression of nac, and NAC activates the expression of hut, ure, and put (proline utilization). NAC is not involved in the transcription of Sigma70-RNAP operons such as glnA, which directly respond by the NTR system, but activates the transcription of sigma70-RNAP dependent operons such as hut. Hence, NAC allows the coupling of sigma70-RNAP dependent operons to the sigma54-RNAP dependent NTR system. This substrate-binding domain has significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
RVSVGLPPSAASVLAVPLLRAVRRRYPGIRLRIVEGLSGHLLEWLLNGRLDLALLYGPPPIPGLSTEPLL
EEDLFLVGPADAPLPRGAPVPLAELARLPLILPSRGHGLRRLVDEAAARAGLTLNVVVEIDSVATLKALV
AAGLGYTILPASAVAAEVAAGRLVAAPIVDPALTRTLSLATPRDRPLSPAALAVRDLL
>gnl|CDD|176125 cd08434, PBP2_GltC_like, The substrate binding domain of LysR-type transcriptional regulator GltC, which activates gltA expression of glutamate synthase operon, contains type 2 periplasmic binding fold. GltC, a member of the LysR family of bacterial transcriptional factors, activates the expression of gltA gene of glutamate synthase operon and is essential for cell growth in the absence of glutamate. Glutamate synthase is a heterodimeric protein that encoded by gltA and gltB, whose expression is subject to nutritional regulation. GltC also negatively auto-regulates its own expression. This substrate-binding domain has strong homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TVRLGFLHSLGTSLVPDLIRAFRKEYPNVTFELHQGSTDELLDDLKNGELDLALCSPVPDEPDIEWIPLF
TEELVLVVPKDHPLAGRDSVDLAELADEPFVLLSPGFGLRPIVDELCAAAGFTPKIAFEGEEDSTIAGLV
AAGLGVAILPEMTLLNPPGVKKIPIKDPDAERTIGLAWLKDRYLSPAARRFKDFV
>gnl|CDD|176126 cd08435, PBP2_GbpR, The C-terminal substrate binding domain of galactose-binding protein regulator contains the type 2 periplasmic binding fold. Galactose-binding protein regulator (GbpR), a member of the LysR family of bacterial transcriptional regulators, regulates the expression of chromosomal virulence gene chvE. The chvE gene is involved in the uptake of specific sugars, in chemotaxis to these sugars, and in the VirA-VirG two-component signal transduction system. In the presence of an inducing sugar such as L-arabinose, D-fucose, or D-galactose, GbpR activates chvE expression, while in the absence of an inducing sugar, GbpR represses expression. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TVRVGAVPAAAPVLLPPAIARLLARHPRLTVRVVEGTSDELLEGLRAGELDLAIGRLADDEQPPDLASEE
LADEPLVVVARPGHPLARRARLTLADLADYPWVLPPPGTPLRQRLEQLFAAAGLPLPRNVVETASISALL
ALLARSDMLAVLPRSVAEDELRAGVLRELPLPLPTSRRPIGITTRRGGPLSPAARALLDAL
>gnl|CDD|176127 cd08436, PBP2_LTTR_like_3, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold. LysR-transcriptional regulators comprise the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
RLAIGTITSLAAVDLPELLARFHRRHPGVDIRLRQAGSDDLLAAVREGRLDLAFVGLPERRPPGLASREL
AREPLVAVVAPDHPLAGRRRVALADLADEPFVDFPPGTGARRQVDRAFAAAGVRRRVAFEVSDVDLLLDL
VARGLGVALLPASVAARLPGLAALPLEPAPRRRLYLAWSAPPPSPAARAFLELL
>gnl|CDD|176128 cd08437, PBP2_MleR, The substrate binding domain of LysR-type transcriptional regulator MleR which required for malolactic fermentation, contains type 2 periplasmic binidning fold. MleR, a transcription activator of malolactic fermentation system, is found in gram-positive bacteria and belongs to the lysR family of bacterial transcriptional regulators. The mleR gene is required for the expression and induction of malolactic fermentation. This substrate binding domain has significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
KLRFGLPPIIGNYYFPKLAKDLIKTGLMIQIDTYEGGSAELLEQLLQGDLDIALLGSLTPLENSALHSKI
IKTQHFMIIVSKDHPLAKAKKVNFADLKKENFILLNEHFVHPKAFDSLCQQANFQPNIVYRTNDIHILKS
MVRENVGIGFLTDIAVKPDDHLVAIPLLDNEQPTFYISLAHRKDQLLTPAQKKLLDLL
>gnl|CDD|176129 cd08438, PBP2_CidR, The C-terminal substrate binding domain of LysR-like transcriptional regulator CidR, contains the type 2 periplasmic binding fold. This CD includes the substrate binding domain of CidR which positively up-regulates the expression of cidABC operon in the presence of acetic acid produced by the metabolism of excess glucose. The CidR affects the control of murein hydrolase activity by enhancing cidABC expression in the presence of acetic acid. Thus, up-regulation of cidABC expression results in increased murein hydrolase activity. This substrate binding domain has significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
HLRLGLPPLGGSLLFAPLLAAFRQRYPNIELELVEYGGKKVEQAVLNGELDVGITVLPVDEEEFDSQPLC
NEPLVAVLPRGHPLAGRKTVSLADLADEPFILFNEDFALHDRIIDACQQAGFTPNIAARSSQWDFIAELV
AAGLGVALLPRSIAQRLDNAGVKVIPLTDPDLRWQLALIWRKGRYLSHAARAWLALL
>gnl|CDD|176130 cd08439, PBP2_LrhA_like, The C-terminal substrate domain of LysR-like regulator LrhA (LysR homologue A) and that of closely related homologs, contains the type 2 periplasmic binding fold. This CD represents the LrhA subfamily of LysR-like bacterial transcriptional regulators, including LrhA, HexA, PecT, and DgdR. LrhA is involved in control of the transcription of flagellar, motility, and chemotaxis genes by regulating the synthesis and concentration of FlhD(2)C(2), the master regulator for the expression of flagellar and chemotaxis genes. The LrhA protein has strong homology to HexA and PecT from plant pathogenic bacteria, in which HexA and PecT act as repressors of motility and of virulence factors, such as exoenzymes required for lytic reactions. DgdR also shares similar characteristics to those of LrhA, HexA and PecT. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLRIGCPDDYADTILPFLLNRFASVYPRLAIEVVCKRTPRLMEMLERGEVDLALITHPPPGASATILRRS
PTVWYCAAGYILAPGEPLPLALLDEPTLDRRAALAALDAAGIPWRIAYAASSLSGLRAAVRAGLGITART
QEMVPPDLRILGESEGLPPLPDTGYTLCLDPNRPSELAQAFFEAL
>gnl|CDD|176131 cd08440, PBP2_LTTR_like_4, TThe C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold. LysR-transcriptional regulators comprise the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
RVRVAALPSLAATLLPPVLAAFRRRHPGIRVRLRDVSAEQVIEAVRSGEVDFGIGSEPEADPDLEFEPLL
RDPFVLVCPKDHPLARRRSVTWAELAGYPLIALGRGSGVRALIDRALAAAGLTLRPAYEVSHMSTALGMV
AAGLGVAVLPALALPLADHPGLVARPLTEPVVTRTVGLIRRRGRSLSPAAQAFLDLL
>gnl|CDD|176132 cd08441, PBP2_MetR, The C-terminal substrate binding domain of LysR-type transcriptional regulator metR, which regulates the expression of methionine biosynthetic genes, contains type 2 periplasmic binding fold. MetR, a member of the LysR family, is a positive regulator for the metA, metE, metF, and metH genes. The sulfur-containing amino acid methionine is the universal initiator of protein synthesis in all known organisms and its derivative S-adenosylmethionine (SAM) and autoinducer-2 (AI-2) are involved in various cellular processes. SAM plays a central role as methyl donor in methylation reactions, which are essential for the biosynthesis of phospholipids, proteins, DNA and RNA. The interspecies signaling molecule AI-2 is involved in cell-cell communication process (quorum sensing) and gene regulation in bacteria. Although methionine biosynthetic enzymes and metabolic pathways are well conserved in bacteria, the regulation of methionine biosynthesis involves various regulatory mechanisms. In Escherichia coli and Salmonella enterica serovar Typhimurium, MetJ and MetR regulate the expression of methionine biosynthetic genes. The MetJ repressor negatively regulates the E. coli met genes, except for metH. Several of these genes are also under the positive control of MetR with homocysteine as a co-inducer. In Bacillus subtilis, the met genes are controlled by S-box termination-antitermination system. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
RLRIAVECHSCFDWLMPVLDQFRERWPDVELDLSSGFHFDPLPALLRGELDLVITSDPLPLPGIAYEPLF
DYEVVLVVAPDHPLAAKEFITPEDLADETLITYPVERERLDVFRHFLQPAGIEPKRRRTVELTLMILQLV
ASGRGVAALPNWAVREYLDQGLVVARPLGEEGLWRTLYAAVRTEDADQPYLQDFLELA
>gnl|CDD|176133 cd08442, PBP2_YofA_SoxR_like, The C-terminal substrate binding domain of LysR-type transcriptional regulators, YofA and SoxR, contains the type 2 periplasmic binding fold. YofA is a LysR-like transcriptional regulator of cell growth in Bacillus subtillis. YofA controls cell viability and the formation of constrictions during cell division. YofaA positively regulates expression of the cell division gene ftsW, and thus is essential for cell viability during stationary-phase growth of Bacillus substilis. YofA shows significant homology to SoxR from Arthrobacter sp. TE1826. SoxR is a negative regulator for the sarcosine oxidase gene soxA. Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine, which is involved in the metabolism of creatine and choline. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
PLRLGSMETTAAVRLPPLLAAYHARYPKVDLSLSTGTTGALIQAVLEGRLDGAFVAGPVEHPRLEQEPVF
QEELVLVSPKGHPPVSRAEDLAGSTLLAFRAGCSYRRRLEDWLAEEGVSPGKIMEFGSYHAILGCVAAGM
GIALLPRSVLDSLQGRGSVSIHPLPEPFADVTTWLVWRKDSFTAALQAFLDLL
>gnl|CDD|176134 cd08443, PBP2_CysB, The C-terminal substrate domain of LysR-type transcriptional regulator CysB contains type 2 periplasmic binding fold. CysB is a transcriptional activator of genes involved in sulfate and thiosulfate transport, sulfate reduction, and cysteine synthesis. In Escherichia coli, the regulation of transcription in response to sulfur source is attributed to two transcriptional regulators, CysB and Cbl. CysB, in association with Cbl, downregulates the expression of ssuEADCB operon which is required for the utilization of sulfur from aliphatic sulfonates, in the presence of cysteine. Also, Cbl and CysB together directly function as transcriptional activators of tauABCD genes, which are required for utilization of taurine as sulfur source for growth. Like many other members of the LTTR family, CysB is composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
SLYVATTHTQARYVLPPVIKGFIERYPRVSLQMHQGSPTQIAEMVSKGLVDFAIATEALHDYDDLITLPC
YHWNRCVVVKRDHPLADKQSISIEELATYPIVTYTFGFTGRSELDTAFNRAGLTPNIVLTATDADVIKTY
VRLGLGVGVIASMAYDPVDDPDLVIRDARDLFPWSVTKIAFRRGTFLRSYMYDFIQRF
>gnl|CDD|176135 cd08444, PBP2_Cbl, The C-terminal substrate binding domain of LysR-type transcriptional regulator Cbl, which is required for expression of sulfate starvation-inducible (ssi) genes, contains the type 2 periplasmic binding fold. Cbl is a member of the LysR transcriptional regulators that comprise the largest family of prokaryotic transcription factor. Cbl shows high sequence similarity to CysB, the LysR-type transcriptional activator of genes involved in sulfate and thiosulfate transport, sulfate reduction, and cysteine synthesis. In Escherichia coli, the function of Cbl is required for expression of sulfate starvation-inducible (ssi) genes, coupled with the biosynthesis of cysteine from the organic sulfur sources (sulfonates). The ssi genes include the ssuEADCB and tauABCD operons encoding uptake systems for organosulfur compounds, aliphatic sulfonates, and taurine. The genes in these operons encode an ABC-type transport system required for uptake of aliphatic sulfonates and a desulfonation enzyme. Both Cbl and CysB require expression of the tau and ssu genes. Like many other members of the LTTR family, the Cbl is composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
ELTIATTHTQARYALPWVVQAFKEQFPNVHLVLHQGSPEEIASMLANGQADIGIATEALENHPELVSFPY
YDWHHHIIVPVGHPLESITPLTIETIAKWPIITYHGGFTGRSRIDRAFSRAELTPNIVLSALDADVIKTY
VGLGMGIGIVAEMAFEGQRDTNLIKLDTSHLFGKNTTWIALRRGGDLRNFAYRFIELC
>gnl|CDD|176136 cd08445, PBP2_BenM_CatM_CatR, The C-terminal substrate binding domain of LysR-type transcriptional regulators involved in benzoate catabolism; contains the type 2 periplasmic binding fold. This CD includes the C-terminal of LysR-type transcription regulators, BenM, CatM, and CatR, which are involved in the benzoate catabolism. The BenM and CatM are paralogs with overlapping functions. BenM responds synergistically to two effectors, benzoate and cis,cis-muconate, to activate expression of the benABCDE operon which is involved in benzoate catabolism, while CatM responses only to muconate. BenM and CatM share high protein sequence identity and bind to the operator-promoter regions that have similar DNA sequences. In Pseudomonas species, phenolic compounds are converted by different enzymes to central intermediates, such as protocatechuate and catechols. Generally, unsubstituted compounds, such as benzoate, are metabolized by an ortho-cleavage pathway. The catBCA operon encodes three enzymes of the ortho-pathway required for benzoate catabolism: muconate lactonizing enzyme I, muconolactone isomerase, and catechol 1,2-dioxygenase. CatR normally responds to benzoate and cis,cis-muconate, an inducer molecule, to activate transcription of the catBCA operon, whose gene products convert benzoate to catechol. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate-binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
RTFSIGFVPSTLYGLLPELIRRFRQAAPDVEIELIEMTTVQQIEALKEGRIDVGFGRLRIEDPAIRRIVL
REEPLVVALPAGHPLAQEKAPLTLAQLADEPLILYPASPRPSFADQVLSLFRDHGLRPRVIQEVRELQTA
LGLVAAGEGVTLVPASVQRLRRDDVVYRPLLDPDATSPIIMSVRAGDESPYIALILQLIRELY
>gnl|CDD|176137 cd08446, PBP2_Chlorocatechol, The C-terminal substrate binding domain of LysR-type transcriptional regulators involved in the chlorocatechol catabolism, contains the type 2 periplasmic binding fold. This CD includes the substrate binding domain of LysR-type regulators CbnR, ClcR and TfdR, which are involved in the regulation of chlorocatechol breakdown. The chlorocatechol-degradative pathway is often found in bacteria that can use chlorinated aromatic compounds as carbon and energy sources. CbnR is found in the 3-chlorobenzoate degradative bacterium Ralstonia eutropha NH9 and forms a tetramer. CbnR activates the expression of the cbnABCD genes, which are responsible for the degradation of chlorocatechol converted from 3-chlorobenzoate and are transcribed divergently from cbnR. In soil bacterium Pseudomonas putida, the 3-chlorocatechol-degradative pathway is encoded by clcABD operon, which requires the divergently transcribed clcR for activation. TfdR is involved in the activation of tfdA and tfdB gene expression. These genes encode enzymes for the conversion of 2,4-dichlorophenoxyacetic acid and 2,4-dichlorophenol. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GELDVGYFGSAILDTVPRLLRAFLTARPDVTVSLHNMTKDEQIEALRAGRIHIGFGRFYPVEPDIAVENV
AQERLYLAVPKSHPLAARPAVSLADLRNEPLILFPRGGRPSFADEVLGLFRRAGVEPRVAQEVEDVVAAL
ALVAAGFGVCIVPESVAALRWPGVVFRPLADAEAKVPLSCIYRKDDRSPILRAFLDVV
>gnl|CDD|176138 cd08447, PBP2_LTTR_aromatics_like_1, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to regulators involved in the catabolism of aromatic compounds, contains type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type regulator similar to CbnR which is involved in the regulation of chlorocatechol breakdown. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
SLRIGFTAASAYSFLPRLLAAARAALPDVDLVLREMVTTDQIEALESGRIDLGLLRPPFARPGLETRPLV
REPLVAAVPAGHPLAGAERLTLEDLDGQPFIMYSPTEARYFHDLVVRLFASAGVQPRYVQYLSQIHTMLA
LVRAGLGVALVPASASRLRFEGVVFRPLDLPRDVPVELHLAWRRDNDNPALRALLDLI
>gnl|CDD|176139 cd08448, PBP2_LTTR_aromatics_like_2, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to regulators involved in the catabolism of aromatic compounds, contains type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type regulator similar to CbnR which is involved in the regulation of chlorocatechol breakdown. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
RLRIGFVGSMLYRGLPRILRAFRAEYPGIEVALHEMSSAEQIEALLRGELDLGFVHSRRLPAGLSARLLH
REPFVCCLPAGHPLAARRRIDLRELAGEPFVLFSREVSPDYYDQIIALCMDAGFHPKIRHEVRHWLTVVA
LVAAGMGVALVPRSLARAGLAGVRFLPLKGATQRSELYAAWKASAPNPALQAFLAAL
>gnl|CDD|176140 cd08449, PBP2_XapR, The C-terminal substrate binding domain of LysR-type transcriptional regulator XapR involved in xanthosine catabolism, contains the type 2 periplasmic binding fold. In Escherichia coli, XapR is a positive regulator for the expression of xapA gene, encoding xanthosine phosphorylase, and xapB gene, encoding a polypeptide similar to the nucleotide transport protein NupG. As an operon, the expression of both xapA and xapB is fully dependent on the presence of both XapR and the inducer xanthosine. Expression of the xapR is constitutive but not auto-regulated, unlike many other LysR family proteins. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
HLNIGMVGSVLWGGLGPALRRFKRQYPNVTVRFHELSPEAQKAALLSKRIDLGFVRFADTLNDPPLASEL
LWREPMVVALPEEHPLAGRKSLTLADLRDEPFVFLRLANSRFADFLINCCLQAGFTPQITQEVVEPQTLM
ALVAAGFGVALVPESYARLPWPGVRFIPLKQAISADLYAVYHPDSATPVIQAFLALL
>gnl|CDD|176141 cd08450, PBP2_HcaR, The C-terminal substrate binding domain of LysR-type transcriptional regulator HcaR in involved in 3-phenylpropionic acid catabolism, contains the type2 periplasmic binding fold. HcaR, a member of the LysR family of transcriptional regulators, controls the expression of the hcA1, A2, B, C, and D operon, encoding for the 3-phenylpropionate dioxygenase complex and 3-phenylpropionate-2',3'-dihydrodiol dehydrogenase, that oxidizes 3-phenylpropionate to 3-(2,3-dihydroxyphenyl) propionate. Dioxygenases play an important role in protecting the cell against the toxic effects of dioxygen. The expression of hcaR is negatively auto-regulated, as for other members of the LysR family, and is strongly repressed in the presence of glucose. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
VLTIGFLPGAEVQWLPEVLPILREEHPDLDVELSSLFSPQLAEALMRGKLDVAFMRPEIQSDGIDYQLLL
KEPLIVVLPADHRLAGREKIPPQDLAGENFISPAPTAPVLQQVIENYAAQHNIQPNIIQEADNLLSAMSL
VASTLGCALLPLYANNLLPPSVVARPLSGETPTIDLVMGYNKANTSPLLKRFLSRA
>gnl|CDD|176142 cd08451, PBP2_BudR, The C-terminal substrate binding domain of LysR-type transcrptional regulator BudR, which is responsible for activation of the expression of the butanediol operon genes; contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of BudR regulator, which is responsible for induction of the butanediol formation pathway under fermentative growth conditions. Three enzymes are involved in the production of 1 mol of 2,3 butanediol from the condensation of 2 mol of pyruvate with acetolactate and acetoin as intermediates: acetolactate synthetase, acetolactate decarboxylase, and acetoin reductase. In Klebsiella terrigena, BudR regulates the expression of the budABC operon genes, encoding these three enzymes of the butanediol pathway. In many bacterial species, the use of this pathway can prevent intracellular acidification by diverting metabolism from acid production to the formation of neutral compounds (acetoin and butanediol). This substrate-binding domain has significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
RLRVGFTSSAAFHPLVPGLIRRFREAYPDVELTLEEANTAELLEALREGRLDAAFVRPPVARSDGLVLEL
LLEEPMLVALPAGHPLARERSIPLAALADEPFILFPRPVGPGLYDAIIAACRRAGFTPRIGQEAPQMASA
INLVAAGLGVSIVPASMRQLQAPGVVYRPLAGAPLTAPLALAYRRGERSPAVRNFIALV
>gnl|CDD|176143 cd08452, PBP2_AlsR, The C-terminal substrate binding domain of LysR-type trnascriptional regulator AlsR, which regulates acetoin formation under stationary phase growth conditions; contains the type 2 periplasmic binding fold. AlsR is responsible for activating the expression of the acetoin operon (alsSD) in response to inducing signals such as glucose and acetate. Like many other LysR family proteins, AlsR is transcribed divergently from the alsSD operon. The alsS gene encodes acetolactate synthase, an enzyme involved in the production of acetoin in cells of stationary-phase. AlsS catalyzes the conversion of two pyruvate molecules to acetolactate and carbon dioxide. Acetolactate is then converted to acetoin at low pH by acetolactate decarboxylase which encoded by the alsD gene. Acetoin is an important physiological metabolite excreted by many microorganisms grown on glucose or other fermentable carbon sources. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
LLVIGFVGAAIYEFLPPIVREYRKKFPSVKVELRELSSPDQVEELLKGRIDIGFLHPPIQHTALHIETVQ
SSPCVLALPKQHPLASKEEITIEDLRDEPIITVAREAWPTLYDEIIQLCEQAGFRPKIVQEATEYQTVIG
LVSAGIGVTFVPSSAKKLFNLEVAYRKIDQINLNAEWSIAYRKDNHNPLLKHFIHIS
>gnl|CDD|176144 cd08453, PBP2_IlvR, The C-terminal substrate binding domain of LysR-type transcriptional regulator, IlvR, involved in the biosynthesis of isoleucine, leucine and valine; contains type 2 periplasmic binding fold. The IlvR is an activator of the upstream and divergently transcribed ilvD gene, which encodes dihydroxy acid dehydratase that participates in isoleucine, leucine, and valine biosynthesis. As in the case of other members of the LysR family, the expression of ilvR gene is repressed in the presence of its own gene product. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
RLSLAFVSTADYSVLPELVRRFREAYPDVELQLREATSDVQLEALLAGEIDAGIVIPPPGASAPPALAYR
PLLSEPLVLAVPAAWAAEGGAPLALAAVAAEPLVIFPRRIAPAFHDAVTGYYRAAGQTPRIAQEAIQMQT
IISLVSAGMGVALVPASLRNLARPGVVYRELADPAPVLETGLVWRRDDASPVLARFLDLV
>gnl|CDD|176145 cd08456, PBP2_LysR, The C-terminal substrate binding domain of LysR, transcriptional regulator for lysine biosynthesis, contains the type 2 periplasmic binding fold. LysR, the transcriptional activator of lysA encoding diaminopimelate decarboxylase, catalyses the decarboxylation of diaminopimelate to produce lysine. The LysR-transcriptional regulators comprise the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
ELRIAVLPALSQSFLPRAIKAFLQRHPDVTISIHTRDSPTVEQWLSAQQCDLGLVSTLHEPPGIERERLL
RIDGVCVLPPGHRLAVKKVLTPSDLEGEPFISLARTDGTRQRVDALFEQAGVKRRIVVETSYAATICALV
AAGVGVSVVNPLTALDYAAAGLVVRRFSPAVPFEVSLIRPKHRPSSALVAAFSACL
>gnl|CDD|176146 cd08457, PBP2_OccR, The C-terminal substrate-domain of LysR-type transcriptional regulator, OccR, involved in the catabolism of octopine, contains the type 2 periplasmic binding fold. This CD includes the C-terminal substrate-domain of LysR-type transcriptional regulator OccR, which is involved in the catabolism of octopine. Opines are low molecular weight compounds found in plant crown gall tumors produced by the parasitic bacterium Agrobacterium. There are at least 30 different opines identified so far. Opines are utilized by tumor-colonizing bacteria as a source of carbon, nitrogen, and energy. In Agrobacterium tumefaciens, OccR protein activates the occQ operon of the Ti plasmid in response to octopine. This operon encodes proteins required for the uptake and catabolism of octopine, an arginine derivative. The occ operon also encodes the TraR protein, which is a quorum-sensing transcriptional regulator of the Ti plasmid tra regulon. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLRIAAMPALANGFLPRFLAAFLRLRPNLHLSLMGLSSSQVLEAVASGRADLGIADGPLEERQGFLIETR
SLPAVVAVPMGHPLAQLDVVSPQDLAGERIITLENGYLFRMRVEVALGKIGVKRRPIIEVNLSHTALSLV
REGLGIAIIDPATAIGLPLDGIVIRPFDTFIDAGFLVVRAANGPPSTMVDRFIDEF
>gnl|CDD|176147 cd08458, PBP2_NocR, The C-terminal substrate-domain of LysR-type transcriptional regulator, NocR, involved in the catabolism of nopaline, contains the type 2 periplasmic binding fold. This CD includes the C-terminal substrate-domain of LysR-type transcriptional regulator NocR, which is involved in the catabolism of nopaline. Opines are low molecular weight compounds found in plant crown gall tumors produced by the parasitic bacterium Agrobacterium. There are at least 30 different opines identified so far. Opines are utilized by tumor-colonizing bacteria as a source of carbon, nitrogen, and energy. In Agrobacterium tumefaciens, NocR regulates expression of the divergently transcribed nocB and nocR genes of the nopaline catabolism (noc) region. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
SLRVACYTAPALSFMSGVIQTFIADRPDVSVYLDTVPSQTVLELVSLQHYDLGISILAGDYPGLTTEPVP
SFRAVCLLPPGHRLEDKETVHATDLEGESLICLSPVSLLRMQTDAALDSCGVHCNRRIESSLALNLCDLV
SRGMGVGIVDPFTADYYSANPVIQRSFDPVVPYHFAIVLPTDSPPPRLVSEFRAAL
>gnl|CDD|176148 cd08459, PBP2_DntR_NahR_LinR_like, The C-terminal substrate binding domain of LysR-type transcriptional regulators that are involved in the catabolism of dinitrotoluene, naphthalene and gamma-hexachlorohexane; contains the type 2 periplasmic binding fold. This CD includes LysR-like bacterial transcriptional regulators, DntR, NahR, and LinR, which are involved in the degradation of aromatic compounds. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. DntR from Burkholderia species controls genes encoding enzymes for oxidative degradation of the nitro-aromatic compound 2,4-dinitrotoluene. The active form of DntR is homotetrameric, consisting of a dimer of dimers. NahR is a salicylate-dependent transcription activator of the nah and sal operons for naphthalene degradation. Salicylic acid is an intermediate of the oxidative degradation of the aromatic ring in soil bacteria. LinR positively regulates expression of the genes (linD and linE) encoding enzymes for gamma-hexachlorocyclohexane (a haloorganic insecticide) degradation. Expression of linD and linE are induced by their substrates, 2,5-dichlorohydroquinone (2,5-DCHQ) and chlorohydroquinone (CHQ). The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TFRIAMSDIGEMYFLPRLLAALREVAPGVRIETVRLPVDELEEALESGEIDLAIGYLPDLGAGFFQQRLF
RERYVCLVRKDHPRIGSTLTLEQFLAARHVVVSASGTGHGLVEQALREAGIRRRIALRVPHFLALPLIVA
QTDLVATVPERLARLFARAGGLRIVPLPFPLPPFEVKLYWHRRFHRDPGNRWLRQLVAELF
>gnl|CDD|176149 cd08460, PBP2_DntR_like_1, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to DntR, which is involved in the catabolism of dinitrotoluene; contains the type 2 periplasmic binding fold. This CD includes an uncharacterized LysR-type transcriptional regulator similar to DntR, NahR, and LinR, which are involved in the degradation of aromatic compounds. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TFTIRANDGFVAAFGPALLAAVAAEAPGVRLRFVPESDKDVDALREGRIDLEIGVLGPTGPEIRVQTLFR
DRFVGVVRAGHPLARGPITPERYAAAPHVSVSRRGRLHGPIDDALAALGLTRRVVAVVPTFAAALFLARG
SDLIALVPERVTAAARAGLGLRTFPLPLELPAVTVSQAWHPRFDADPAHRWLRECVREVC
>gnl|CDD|176150 cd08461, PBP2_DntR_like_3, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to DntR, which is involved in the catabolism of dinitrotoluene; contains the type 2 periplasmic binding fold. This CD includes an uncharacterized LysR-type transcriptional regulator similar to DntR, NahR, and LinR, which are involved in the degradation of aromatic compounds. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLVIAATDYAQKAILPPLLAALRQEAPGVRVAIRDLESDNLEAQLERGEVDLALTTPEYAPDGLRSRPLF
EERYVCVTRRGHPLLQGPLSLDQFCALDHIVVSPSGGGFAGSTDEALAALGLTRNVVLSVPSFLVVPEIL
AATDMVAFVPSRLVPNLEGLQEVELPLEPPGFDVVMAWHERTHRDPAHRWLRELLAAA
>gnl|CDD|176151 cd08462, PBP2_NodD, The C-terminal substsrate binding domain of NodD family of LysR-type transcriptional regulators that regulates the expression of nodulation (nod) genes; contains the type 2 periplasmic binding fold. The nodulation (nod) genes in soil bacteria play important roles in the development of nodules. nod genes are involved in synthesis of Nod factors that are required for bacterial entry into root hairs. Thirteen nod genes have been identified and are classified into five transcription units: nodD, nodABCIJ, nodFEL, nodMNT, and nodO. NodD is negatively auto-regulates its own expression of nodD gene, while other nod genes are inducible and positively regulated by NodD in the presence of flavonoids released by plant roots. This substrate-binding domain has significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
HFRIIASDYVITVLLPPVIERVAREAPGVRFELLPPDDQPHELLERGEVDLLIAPERFMSDGHPSEPLFE
EEFVCVVWADNPLVGGELTAEQYFSAGHVVVRFGRNRRPSFEDWFLNEYGLKRRVEVVTPSFSSIPPLLV
GTNRIATLHRRLAEQFARRLPLRILPLPFPLPPMREALQWHRYRNNDPGLIWLRELIIEA
>gnl|CDD|176152 cd08463, PBP2_DntR_like_4, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to DntR, which is involved in the catabolism of dinitrotoluene; contains the type 2 periplasmic binding fold. This CD includes an uncharacterized LysR-type transcriptional regulator similar to DntR, NahR, and LinR, which are involved in the degradation of aromatic compounds. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TFRIAAPDYLNALFLPELVARFRREAPGARLEIHPLGPDFDYERALASGELDLVIGNWPEPPEHLHLSPL
FSDEIVCLMRADHPLARRGLMTLDDYLEAPHLAPTPYSVGQRGVIDSHLARLGLKRNIVVTVPYFGLAPY
MLAQSDLVFTTGRHFAEHYAKLLPLAVVDAPIEFPRMRYYQLWHERSHRSPEHRWLRRLVASV
>gnl|CDD|176153 cd08464, PBP2_DntR_like_2, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to DntR, which is involved in the catabolism of dinitrotoluene; contains the type 2 periplasmic binding fold. This CD includes an uncharacterized LysR-type transcriptional regulator similar to DntR, NahR, and LinR, which are involved in the degradation of aromatic compounds. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TFRIGLSDDVESWLAPPLLAALRAEAPGVRLVFRQVDPFNVGDMLDRGEIDLAIGVFGELPAWLKREVLY
TEGYACLFDPQQLSLSAPLTLEDYVARPHVLVSYRGGLRGFVDDALAELGRSRRVVASTPHFAALPALLR
GTPLIATVPARLARAWAAALGLRASPPPLDLPEFPISLLWHARTDNDPALVWLREQIVQA
>gnl|CDD|176154 cd08465, PBP2_ToxR, The C-terminal substrate binding domain of LysR-type transcriptional regulator ToxR regulates the expression of the toxoflavin biosynthesis genes; contains the type 2 periplasmic bindinig fold. In soil bacterium Burkholderia glumae, ToxR regulates the toxABCDE and toxFGHI operons in the presence of toxoflavin as a coinducer. Additionally, the expression of both operons requires a transcriptional activator, ToxJ, whose expression is regulated by the TofI or TofR quorum-sensing system. The biosynthesis of toxoflavin is suggested to be synthesized in a pathway common to the synthesis of riboflavin. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
VFRLAMSDYGARLVLPALMRQLRAEAPGIDLAVSQASREAMLAQVADGEIDLALGVFPELPEELHAETLF
EERFVCLADRATLPASGGLSLDAWLARPHVLVAMRGDAANEIDRALAARGLRRRVALTLPHWGVAPELIA
GTDLILTVARRALDALRLDERLAVFAPPFPIPPFAFQQIWHQRREGDPAHRWLRERIQEA
>gnl|CDD|176155 cd08466, PBP2_LeuO, The C-terminal substrate binding domain of LysR-type transcriptional regulator LeuO, an activator of leucine synthesis operon, contains the type 2 periplasmic binding fold. LeuO, a LysR-type transcriptional regulator, was originally identified as an activator of the leucine synthesis operon (leuABCD). Subsequently, LeuO was found to be not a specific regulator of the leu gene but a global regulator of unrelated various genes. LeuO activates bglGFB (utilization of beta-D-glucoside) and represses cadCBA (lysine decarboxylation) and dsrA (encoding a regulatory small RNA for translational control of rpoS and hns). LeuO also regulates the yjjQ-bglJ operon which coding for a LuxR-type transcription factor. In Salmonella enterica serovar Typhi, LeuO is a positive regulator of ompS1 (encoding an outer membrane), ompS2 (encoding a pathogenicity determinant), and assT, while LeuO represses the expression of OmpX and Tpx. Both osmS1 and osmS2 influence virulence in the mouse model of Salmonella. In Vibrio cholerae, LeuO is involved in control of biofilm formation and in the stringent response. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TFNIAANETLDLLLLPRLLARLKQLAPNISLRESPSSEEDLFEDLRLQEVDLVIDYVPFRDPSFKSELLF
EDELVCVARKDHPRIQGSLSLEQYLAEKHVVLSLRRGNLSALDLLTEEVLPQRNIAYEVSSLLSMLAVVS
QTDLIAIAPRWLADQYAEQLNLQILPLPFKTKPIPLYMVWHKSRERDPAHQWLREQIKQL
>gnl|CDD|176156 cd08467, PBP2_SyrM, The C-terminal substrate binding of LysR-type symbiotic regulator SyrM, which activates expression of nodulation gene NodD3, contains the type 2 periplasmic binding fold. Rhizobium is a nitrogen fixing bacteria present in the roots of leguminous plants, which fixes atmospheric nitrogen to the soil. Most Rhizobium species possess multiple nodulation (nod) genes for the development of nodules. For example, Rhizobium meliloti possesses three copies of nodD genes. NodD1 and NodD2 activate nod operons when Rhizobium is exposed to inducers synthesized by the host plant, while NodD3 acts independent of plant inducers and requires the symbiotic regulator SyrM for nod gene expression. SyrM activates the expression of the regulatory nodulation gene nodD3. In turn, NodD3 activates expression of syrM. In addition, SyrM is involved in exopolysaccharide synthesis. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GFTLAMPDYAEVALLPRLAPRLRERAPGLDLRLCPIGDDLAERGLEQGTIDLAVGRFAVPPDGLVVRRLY
DDGFACLVRHGHPALAQEWTLDDFATLRHVAIAPPGRLFGGIYKRLENLGLKRNVAIAVSSFLTAAATVA
ATDLIATVPRRVATQVAAMLPLRVVPPPVDLGTFPVMLIWHERYQHDPAHRWLRKLIAAA
>gnl|CDD|176157 cd08468, PBP2_Pa0477, The C-terminal substrate biniding domain of an uncharacterized LysR-like transcriptional regulator Pa0477 related to DntR, contains the type 2 periplasmic binding fold. LysR-type transcriptional regulator Pa0477 is related to DntR, which controls genes encoding enzymes for oxidative degradation of the nitro-aromatic compound 2,4-dinitrotoluene. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
RFRFAVTDYTALAVMPRLMARLEELAPSVRLNLVHAEQKLPLDALLAGEIDFALGYSHDDGAEPRLIEER
DWWEDTYVVIASRDHPRLSRLTLDAFLAERHLVVTPWNEDRGVVDQVLEKQGLEREIALQLPNVLNAPFI
VASSDLLMTLPRQAARALAEALPLELFDLPFDMPPYRLKLYSHRQHENSAANQWLIEQLDGL
>gnl|CDD|176158 cd08469, PBP2_PnbR, The C-terminal substrate binding domain of LysR-type transcriptional regulator PnbR, which is involved in regulating the pnb genes encoding enzymes for 4-nitrobenzoate catabolism, contains the type 2 periplasmic binding fold. PnbR is the regulator of one or both of the two pnb genes that encoding enzymes for 4-nitrobenzoate catabolism. In Pseudomonas putida strain, pnbA encodes a 4-nitrobenzoate reductase, which is responsible for catalyzing the direct reduction of 4-nitrobenzoate to 4-hydroxylaminobenzoate, and pnbB encodes a 4-hydroxylaminobenzoate lyase, which catalyzes the conversion of 4-hydroxylaminobenzoate to 3, 4-dihydroxybenzoic acid and ammonium. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
SFVIAANDYVTAVLLPALVRRLETEAPGIDLRIRPVTRLDLAEQLDLGRIDLVIGIFEQIPPRFRRRTLF
DEDEVWVMRKDHPAARGALTIETLARYPHIVVSLGGEEEGAVSGFISERGLARQTEMFDRRALEEAFRES
GLVPRVAVTVPHALAVPPLLADSDMLALLPRSLARAFAERGGLVMKEPPYPPPPVQIRAVWHERHDNDPA
VAWLREMIRDV
>gnl|CDD|176159 cd08470, PBP2_CrgA_like_1, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding domain. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 1. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GLLRITCPVAYGERFIAPLVNDFMQRYPKLEVDIELTNRVVDLVSEGFDLAIRLGRLTDSSLMARRLASR
RHYVCASPAYLERHGTPHSLADLDRHNCLLGTSDHWRFQENGRERSVRVQGRWRCNSGVALLDAALKGMG
LAQLPDYYVDEHLAAGRLVPVLEDYRPPDEGIWALYPHNRHLSPKVRLLVDYLADAL
>gnl|CDD|176160 cd08471, PBP2_CrgA_like_2, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 2. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GLLTVTAPVLFGRLHVLPIITDFLDAYPEVSVRLLLLDRVVNLLEEGVDVAVRIGHLPDSSLVATRVGSV
RRVVCASPAYLARHGTPKHPDDLADHDCIAFTGLSPAPEWRFREGGKERSVRVRPRLTVNTVEAAIAAAL
AGLGLTRVLSYQVAEELAAGRLQRVLEDFEPPPLPVHLVHPEGRLAPAKVRAFVDFAVPRL
>gnl|CDD|176161 cd08472, PBP2_CrgA_like_3, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 3. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GRLRVDVPGSLARLLLIPALPDFLARYPDIELDLGVSDRPVDLIREGVDCVIRVGELADSSLVARRLGEL
RMVTCASPAYLARHGTPRHPEDLERHRAVGYFSARTGRVLPWEFQRDGEEREVKLPSRVSVNDSEAYLAA
ALAGLGIIQVPRFMVRPHLASGRLVEVLPDWRPPPLPVSLLYPHRRHLSPRVRVFVDWVAEL
>gnl|CDD|176162 cd08473, PBP2_CrgA_like_4, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 4. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
PRGTVRVSCPPALAQELLAPLLPRFMAAYPQVRLQLEATNRRVDLIEEGIDVALRVRFPPLEDSSLVMRV
LGQSRQRLVASPALLARLGRPRSPEDLAGLPTLSLGDVDGRHSWRLEGPDGESITVRHRPRLVTDDLLTL
RQAALAGVGIALLPDHLCREALRAGRLVRVLPDWTPPRGIVHAVFPSRRGLLPAVRALIDFL
>gnl|CDD|176163 cd08474, PBP2_CrgA_like_5, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 5. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
PAGTLRINAPRVAARLLLAPLLARFLARYPDIRLELVVDDGLVDIVAEGFDAGIRLGESVEKDMVAVPLG
PPLRMAVVASPAYLARHGTPEHPRDLLNHRCIRYRFPTSGALYRWEFERGGRELEVDVEGPLILNDSDLM
LDAALDGLGIAYLFEDLVAEHLASGRLVRVLEDWSPPFPGGYLYYPSRRRVPPALRAFIDFL
>gnl|CDD|176164 cd08475, PBP2_CrgA_like_6, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 6. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GRLRIDLPVAFGRLCVAPLLLELARRHPELELELSFSDRFVDLIEEGIDLAVRIGELADSTGLVARRLGT
QRMVLCASPAYLARHGTPRTLEDLAEHQCIAYGRGGQPLPWRLADEQGRLVRFRPAPRLQFDDGEAIADA
ALAGLGIAQLPTWLVADHLQRGELVEVLPELAPEGLPIHAVWPRTRHLPPKVRAAVDAL
>gnl|CDD|176165 cd08476, PBP2_CrgA_like_7, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 7. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GRLRVSLPLVGGLLLPVLAAFMQRYPEIELDLDFSDRLVDVIDEGFDAVIRTGELPDSRLMSRRLGSFRM
VLVASPDYLARHGTPETPADLAEHACLRYRFPTTGKLEPWPLRGDGGDPELRLPTALVCNNIEALIEFAL
QGLGIACLPDFSVREALADGRLVTVLDDYVEERGQFRLLWPSSRHLSPKLRVFVDFM
>gnl|CDD|176166 cd08477, PBP2_CrgA_like_8, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 8. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GKLRISAPVTFGSHVLTPALAEYLARYPDVRVDLVLSDRLVDLVEEGFDAAFRIGELADSSLVARPLAPY
RMVLCASPDYLARHGTPTTPEDLARHECLGFSYWRARNRWRLEGPGGEVKVPVSGRLTVNSGQALRVAAL
AGLGIVLQPEALLAEDLASGRLVELLPDYLPPPRPMHLLYPPDRRPTPKLRSFIDFL
>gnl|CDD|176167 cd08478, PBP2_CrgA, The C-terminal substrate binding domain of LysR-type transcriptional regulator CrgA, contains the type 2 periplasmic binding domain. This CD represents the substrate binding domain of LysR-type transcriptional regulator (LTTR) CrgA. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis further showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
PSGLLRVDAATPFVLHLLAPLIAKFRERYPDIELELVSNEGIIDLIERKTDVAIRIGELTDSTLHARPLG
KSRLRILASPDYLARHGTPQSIEDLAQHQLLGFTEPASLNTWPIKDADGNLLKIQPTITASSGETLRQLA
LSGCGIACLSDFMTDKDIAEGRLIPLFAEQTSDVRQPINAVYYRNTALSLRIRCFIDFL
>gnl|CDD|176168 cd08479, PBP2_CrgA_like_9, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 9. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GLLRVNASFGFGRRHIAPALSDFAKRYPELEVQLELTDRPVDLVEEGFDLDIRVGDLPDSSLIARKLAPN
RRILCASPAYLERHGAPASPEDLARHDCLVIRENDEDFGLWRLRNGDGEATVRVRGALSSNDGEVVLQWA
LDGHGIILRSEWDVAPYLRSGRLVRVLPDWQLPDADIWAVYPSRLSRSARVRVFVDFL
>gnl|CDD|176169 cd08480, PBP2_CrgA_like_10, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 10. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GRLRVNASVPFGTHFLLPLLPAFLARYPEILVDLSLTDEVVDLLAERTDVAIRVGPLPDSSLVARKLGES
RRVIVASPSYLARHGTPLTPQDLARHNCLGFNFRRALPDWPFRDGGRIVALPVSGNILVNDGEALRRLAL
AGAGLARLALFHVADDIAAGRLVPVLEEYNPGDREPIHAVYVGGGRLPARVRAFLDFL
>gnl|CDD|176170 cd08481, PBP2_GcdR_like, The C-terminal substrate binding domain of LysR-type transcriptional regulators GcdR-like, contains the type 2 periplasmic binding fold. GcdR is involved in the glutaconate/glutarate-specific activation of the Pg promoter driving expression of a glutaryl-CoA dehydrogenase-encoding gene (gcdH). The GcdH protein is essential for the anaerobic catabolism of many aromatic compounds and some alicyclic and dicarboxylic acids. The structural topology of this substrate-binding domain is most similar to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLELAVLPTFGTRWLIPRLPDFLARHPDITVNLVTRDEPFDFSQGSFDAAIHFGDPVWPGAESEYLMDEE
VVPVCSPALLAGRALAAPADLAHLPLLQQTTRPEAWRDWFEEVGLEVPTAYRGMRFEQFSMLAQAAVAGL
GVALLPRFLIEEELARGRLVVPFNLPLTSDKAYYLVYPEDKAESPPVQAFRDWL
>gnl|CDD|176171 cd08482, PBP2_TrpI, The C-terminal substrate binding domain of LysR-type transcriptional regulator TrpI, which is involved in control of tryptophan synthesis, contains type 2 periplasmic binding fold. TrpI and indoleglycerol phosphate (InGP), are required to activate transcription of the trpBA, the genes for tryptophan synthase. The trpBA is induced by the InGp substrate, rather than by tryptophan, but the exact mechanism of the activation event is not known. This substrate-binding domain of TrpI shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
PLVLSCSGSLLMRWLIPRLPAFQAALPDIDLQLSASDGPVDSLRDGIDAAIRFNDAPWPAGMQVIELFPE
RVGPVCSPSLAPTVPLRQAPAAALLGAPLLHTRSRPQAWPDWAAAQGLAPEKLGTGQSFEHFYYLLEAAV
AGLGVAIAPWPLVRDDLASGRLVAPWGFIETGSHYVLLRPARLRDSRAGALADWL
>gnl|CDD|176172 cd08483, PBP2_HvrB, The C-terminal substrate-binding domain of LysR-type transcriptional regulator HvrB, an activator of S-adenosyl-L-homocysteine hydrolase expression, contains the type 2 periplasmic binding fold. The transcriptional regulator HvrB of the LysR family is required for the light-dependent activation of both ahcY, which encoding the enzyme S-adenosyl-L-homocysteine hydrolase (AdoHcyase) that responsible for the reversible hydrolysis of AdoHcy to adenosine and homocysteine, and orf5, a gene of unknown. The topology of this C-terminal domain of HvrB is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
PLTVTLTPSFASNWLMPRLGSFWAKHPEIELSLLPSADLVDLRPDGIDVAIRYGNGDWPGLESEPLTAAP
FVVVAAPGLLGDRKVDSLADLAGLPWLQERGTNEQRVWLASMGVVPDLERGVTFLPGQLVLEAARAGLGL
SIQARALVEPDIAAGRLTVLFEEEEEGLGYHIVTRPGVLRPAAKAFVRWL
>gnl|CDD|176173 cd08484, PBP2_LTTR_beta_lactamase, The C-terminal substrate-domain of LysR-type transcriptional regulators for beta-lactamase genes, contains the type 2 periplasmic binding fold. This CD includes the C-terminal substrate binding domain of LysR-type transcriptional regulators, BlaA and AmpR, that are involved in control of the expression of beta-lactamase genes. Beta-lactamases are responsible for bacterial resistance to beta-lactam antibiotics such as penicillins. BlaA (a constitutive class A penicillinase) belongs to the LysR family of transcriptional regulators, while BlaB (an inducible class C cephalosporinase or AmpC) can be referred to as a penicillin-binding protein, but it does not act as a beta-lactamase. AmpR regulates the expression of beta-lactamases in many enterobacterial strains and many other gram-negative bacilli. In contrast to BlaA, AmpR acts an activator only in the presence of the beta-lactam inducer. In the absence of the inducer, AmpR acts as a repressor. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
VLTVGAVGTFAVGWLLPRLAEFRQLHPFIDLRLSTNNNRVDIAAEGLDFAIRFGEGAWPGTDATRLFEAP
LSPLCTPELARRLSEPADLANETLLRSYRADEWPQWFEAAGVPPPPINGPVFDSSLLMVEAALQGAGVAL
APPSMFSRELASGALVQPFKITVSTGSYWLTRLKSKPETPAMSAFSQWL
>gnl|CDD|176174 cd08485, PBP2_ClcR, The C-terminal substrate binding domain of LysR-type transcriptional regulator ClcR involved in the chlorocatechol catabolism, contains type 2 periplasmic binding fold. In soil bacterium Pseudomonas putida, the ortho-pathways of catechol and 3-chlorocatechol are central catabolic pathways that convert aromatic and chloroaromaric compounds to tricarboxylic acid (TCA) cycle intermediates. The 3-chlorocatechol-degradative pathway is encoded by clcABD operon, which requires the divergently transcribed clcR and an intermediate of the pathway, 2-chloromuconate, as an inducer for activation. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GELRVAYFGTVVLHTLPLLLRQLLSVAPSATVSLTQMSKNRQIEALDAGTIDIGFGRFYPYQEGVVVRNV
TNERLFLGAQKSRARSFGEQVHCSALRNEPLILFPREGRPSFADEVIGVFKNARVEPKVVAIVEDVNAAM
ALALAGVGVTIVPETVAMISWPDFGFTELVGSKATVPVSCIYRHDHIAPILKTFLNLL
>gnl|CDD|176175 cd08486, PBP2_CbnR, The C-terminal substrate binding domain of LysR-type transcriptional regulator, CbnR, involved in the chlorocatechol catabolism, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of LysR-type regulator CbnR which is involved in the regulation of chlorocatechol breakdown. The chlorocatechol-degradative pathway is often found in bacteria that can use chlorinated aromatic compounds as carbon and energy sources. CbnR is found in the 3-chlorobenzoate degradative bacterium Ralstonia eutropha NH9 and forms a tetramer. CbnR activates the expression of the cbnABCD genes, which are responsible for the degradation of chlorocatechol converted from 3-chlorobenzoate and are transcribed divergently from cbnR. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GELSVAYFGTPIYRSLPLLLRAFLTSTPTATVSLTHMTKDEQVEGLLAGTIHVGFSRFFPRHPGIEIVNI
AQEDLYLAVHRSQSGKFGKTCKLADLRAVELTLFPRGGRPSFADEVIGLFKHAGIEPRIARVVEDATAAL
ALTMAGAASSIVPASVAAIRWPDIAFARIVGTRVKVPISCIFRKEKQPPILARFVEHV
>gnl|CDD|176176 cd08487, PBP2_BlaA, The C-terminal substrate-binding domain of LysR-type trnascriptional regulator BlaA which involved in control of the beta-lactamase gene expression; contains the type 2 periplasmic binding fold. This CD represents the C-terminal substrate binding domain of LysR-type transcriptional regulator, BlaA, that involved in control of the expression of beta-lactamase genes, blaA and blaB. Beta-lactamases are responsible for bacterial resistance to beta-lactam antibiotics such as penicillins. The blaA gene is located just upstream of blaB in the opposite direction and regulates the expression of the blaB. BlaA also negatively auto-regulates the expression of its own gene, blaA. BlaA (a constitutive class A penicllinase) belongs to the LysR family of transcriptional regulators, whereas BlaB (an inducible class C cephalosporinase or AmpC) can be referred to as a penicillin binding protein but it does not act as a beta-lactamase. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
VLTVGAVGTFAVGWLLPRLAEFRQLHPFIELRLRTNNNVVDLATEGLDFAIRFGEGLWPATHNERLLDAP
LSVLCSPEIAKRLSHPADLINETLLRSYRTDEWLQWFEAANMPPIKIRGPVFDSSRLMVEAAMQGAGVAL
APAKMFSREIENGQLVQPFKIEVETGSYWLTWLKSKPMTPAMELFRQWI
>gnl|CDD|176177 cd08488, PBP2_AmpR, The C-terminal substrate domain of LysR-type transcriptional regulator AmpR that involved in control of the expression of beta-lactamase gene ampC, contains the type 2 periplasmic binding fold. AmpR acts as a transcriptional activator by binding to a DNA region immediately upstream of the ampC promoter. In the absence of a beta-lactam inducer, AmpR represses the synthesis of beta-lactamase, whereas expression is induced in the presence of a beta-lactam inducer. The AmpD, AmpG, and AmpR proteins are involved in the induction of AmpC-type beta-lactamase (class C) which produced by enterobacterial strains and many other gram-negative bacilli. The activation of ampC by AmpR requires ampG for induction or high-level expression of AmpC. It is probable that the AmpD and AmpG work together to modulate the ability of AmpR to activate ampC expression. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
VLHVGAVGTFAVGWLLPRLADFQNRHPFIDLRLSTNNNRVDIAAEGLDYAIRFGSGAWHGIDATRLFEAP
LSPLCTPELARQLREPADLARHTLLRSYRADEWPQWFEAAGVGHPCGLPNSIMFDSSLGMMEAALQGLGV
ALAPPSMFSRQLASGALVQPFATTLSTGSYWLTRLQSRPETPAMSAFSAWL
>gnl|CDD|173854 cd08489, PBP2_NikA, The substrate-binding component of an ABC-type nickel import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding domain of nickel transport system, which functions in the import of nickel and in the control of chemotactic response away from nickel. The ATP-binding cassette (ABC) type nickel transport system is comprised of five subunits NikABCDE: the two pore-forming integral inner membrane proteins NikB and NikC; the two inner membrane-associated proteins with ATPase activity NikD and NikE; and the periplasmic nickel binding NikA, the initial nickel receptor. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLTYAWPKDIGDLNPHLYSNQMFAQNMVYEPLVKYGEDGKIEPWLAESWEISEDGKTYTFHLRKGVKFSD
GTPFNAEAVKKNFDAVLANRDRHSWLELVNKIDSVEVVDEYTVRLHLKEPYYPTLNELALVRPFRFLSPK
AFPDGGTKGGVKKPIGTGPWVLAEYKKGEYAVFVRNPNYWGEKPKIDKITVKVIPDAQTRLLALQSGEID
LIYGADGISADAFKQLKKDKGYGTAVSEPTSTRFLALNTASEPLSDLKVREAINYAIDKEAISKGILYGL
EKPADTLFAPNVPYADIDLKPYSYDPEKANALLDEAGWTLNEGDGIREKDGKPLSLELVYQTDNALQKSI
AEYLQSELKKIGIDLNIIGEEEQAYYDRQKDGDFDLIFYRTWGAPYDPHSFLSSMRVPSHADYQAQVGLA
NKAELDALINEVLATTDEEKRQELYDEILTTLHDQAVYIPLTYPRNKAVYNPKVKGVTFSPTQYEIPF
>gnl|CDD|173855 cd08490, PBP2_NikA_DppA_OppA_like_3, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
KTLTVGLPFESTSLDPASDDGWLLSRYGVAETLVKLDDDGKLEPWLAESWEQVDDTTWEFTLRDGVKFHD
GTPLTAEAVKASLERALAKSPRAKGGALIISVIAVDDYTVTITTKEPYPALPARLADPNTAILDPAAYDD
GVDPAPIGTGPYKVESFEPDQSLTLERNDDYWGGKPKLDKVTVKFIPDANTRALALQSGEVDIAYGLPPS
SVERLEKDDGYKVSSVPTPRTYFLYLNTEKGPLADVRVRQALSLAIDREGIADSVLEGSAAPAKGPFPPS
LPANPKLEPYEYDPEKAKELLAEAGWTDGDGDGIEKDGEPLELTLLTYTSRPELPPIAEAIQAQLKKIGI
DVEIRVVEYDAIEEDLLDGDFDLALYSRNTAPTGDPDYFLNSDYKSDGSYNYGGYSNPEVDALIEELRTE
FDPEERAELAAEIQQIIQDDAPVIPVAHYNQVVAVSKRVKGYKVDPTEYY
>gnl|CDD|173856 cd08491, PBP2_NikA_DppA_OppA_like_12, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
DVTIVLPEEPDSLEPCDSSRTAVGRVIRSNVTEPLTEIDPESGTVGPRLATEWEQVDDNTWRFKLRPGVK
FHDGTPFDAEAVAFSIERSMNGKLTCETRGYYFGDAKLTVKAVDDYTVEIKTDEPDPILPLLLSYVDVVS
PNTPTDKKVRDPIGTGPYKFDSWEPGQSIVLSRFDGYWGEKPEVTKATYVWRSESSVRAAMVETGEADLA
PSIAVQDATNPDTDFAYLNSETTALRIDAQIPPLDDVRVRKALNLAIDRDGIVGALFGGQGRPATQLVVP
GINGHNPDLKPWPYDPEKAKALVAEAKADGVPVDTEITLIGRNGQFPNATEVMEAIQAMLQQVGLNVKLR
MLEVADWLRYLRKPFPEDRGPTLLQSQHDNNSGDASFTFPVYYLSEGSQSTFGDPELDALIKAAMAATGD
ERAKLFQEIFAYVHDEIVADIPMFHMVGYTRVSKRLDYKPDIATNSELRLSEI
>gnl|CDD|173857 cd08492, PBP2_NikA_DppA_OppA_like_15, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
GGTLTYALGQDPTCLDPHTLDFYPNGSVLRQVVDSLVYQDPTGEIVPWLAESWEVSDDGTTYTFHLRDGV
TFSDGTPLDAEAVKANFDRILDGSTKSGLAASYLGPYKSTEVVDPYTVKVHFSEPYAPFLQALSTPGLGI
LSPATLARPGEDGGGENPVGSGPFVVESWVRGQSIVLVRNPDYNWAPALAKHQGPAYLDKIVFRFIPEAS
VRVGALQSGQVDVITDIPPQDEKQLAADGGPVIETRPTPGVPYSLYLNTTRPPFDDVRVRQALQLAIDRE
AIVETVFFGSYPAASSLLSSTTPYYKDLSDAYAYDPEKAKKLLDEAGWTARGADGIRTKDGKRLTLTFLY
STGQPQSQSVLQLIQAQLKEVGIDLQLKVLDAGTLTARRASGDYDLALSYYGRADPDILRTLFHSANRNP
PGGYSRFADPELDDLLEKAAATTDPAERAALYADAQKYLIEQAYVVPLYEEPQVVAAAPNVKGF
>gnl|CDD|173858 cd08493, PBP2_DppA_like, The substrate-binding component of an ABC-type dipeptide import system contains the type 2 periplasmic binding fold. This family represents the substrate-binding domain of an ATP-binding cassette (ABC)-type dipeptide import system. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLVYCSEGSPESLDPQLATDGESDAVTRQIYEGLVEFKPGTTELEPGLAESWEVSDDGLTYTFHLRKGVK
FHDGRPFNADDVVFSFNRWLDPNHPYHKVGGGGYPYFYSMGLGSLIKSVEAVDDYTVKFTLTRPDAPFLA
NLAMPFASILSPEYADQLLAAGKPEQLDLLPVGTGPFKFVSWQKDDRIRLEANPDYWGGKAKIDTLVFRI
IPDNSVRLAKLLAGECDIVAYPNPSDLAILADAGLQLLERPGLNVGYLAFNTQKPPFDDPKVRQAIAHAI
NKEAIVDAVYQGTATVAKNPLPPTSWGYNDDVPDYEYDPEKAKALLAEAGYPDGFELTLWYPPVSRPYNP
NPKKMAELIQADLAKVGIKVEIVTYEWGEYLERTKAGEHDLYLLGWTGDNGDPDNFLRPLLSCDAAPSGT
NRARWCNPEFDELLEKARRTTDQAERAKLYKQAQEIIHEDAPWVPIAHSKRLLAVRKNVKGF
>gnl|CDD|173859 cd08494, PBP2_NikA_DppA_OppA_like_6, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLTIGLTLEPTSLDITTTAGAAIDQVLLGNVYETLVRRDEDGKVQPGLAESWTISDDGLTYTFTLRSGVT
FHDGTPFDAADVKFSLQRARAPDSTNADKALLAAIASVEAPDAHTVVVTLKHPDPSLLFNLGGRAGVVVD
PASAADLATKPVGTGPFTVAAWARGSSITLVRNDDYWGAKPKLDKVTFRYFSDPTALTNALLAGDIDAAP
PFDAPELEQFADDPRFTVLVGTTTGKVLLAMNNARAPFDDVRVRQAIRYAIDRKALIDAAWDGYGTPIGG
PISPLDPGYVDLTGLYPYDPDKARQLLAEAGAAYGLTLTLTLPPLPYARRIGEIIASQLAEVGITVKIEV
VEPATWLQRVYKGKDYDLTLIAHVEPDDIGIFADPDYYFGYDNPEFQELYAQALAATDADERAELLKQAQ
RTLAEDAAADWLYTRPNIVVARKGVTGY
>gnl|CDD|173860 cd08495, PBP2_NikA_DppA_OppA_like_8, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLRIAMDIPLTTLDPDQGAEGLRFLGLPVYDPLVRWDLSTADRPGEIVPGLAESWEVSPDGRRWTFTLRP
GVKFHDGTPFDADAVVWNLDRMLDPDSPQYDPAQAGQVRSRIPSVTSVEAIDDNTVRITTSEPFADLPYV
LTTGLASSPSPKEKAGDAWDDFAAHPAGTGPFRITRFVPRERIELVRNDGYWDKRPPKNDKLVLIPMPDA
NARLAALLSGQVDAIEAPAPDAIAQLKSAGFQLVTNPSPHVWIYQLNMAEGPLSDPRVRQALNLAIDREG
LVDLLLGGLAAPATGPVPPGHPGFGKPTFPYKYDPDKARALLKEAGYGPGLTLKLRVSASGSGQMQPLPM
NEFIQQNLAEIGIDLDIEVVEWADLYNAWRAGAKDGSRDGANAINMSSAMDPFLALVRFLSSKIDPPVGS
NWGGYHNPEFDALIDQARVTFDPAERAALYREAHAIVVDDAPWLFVVHDRNPRALSPKVKGF
>gnl|CDD|173861 cd08496, PBP2_NikA_DppA_OppA_like_9, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA can bind peptides of a wide range of lengths (2-35 amino-acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLTIATSADPTSWDPAQGGSGADHDYLWLLYDTLIKLDPDGKLEPGLAESWEYNADGTTLTLHLREGLTF
SDGTPLDAAAVKANLDRGKSTGGSQVKQLASISSVEVVDDTTVTLTLSQPDPAIPALLSDRAGMIVSPTA
LEDDGKLATNPVGAGPYVLTEWVPNSKYVFERNEDYWDAANPHLDKLELSVIPDPTARVNALQSGQVDFA
QLLAAQVKIARAAGLDVVVEPTLAATLLLLNITGAPFDDPKVRQAINYAIDRKAFVDALLFGLGEPASQP
FPPGSWAYDPSLENTYPYDPEKAKELLAEAGYPNGFSLTIPTGAQNADTLAEIVQQQLAKVGIKVTIKPL
TGANAAGEFFAAEKFDLAVSGWVGRPDPSMTLSNMFGKGGYYNPGKATDPELSALLKEVRATLDDPARKT
ALRAANKVVVEQAWFVPLFFQPSVYALSKKVSGL
>gnl|CDD|173862 cd08497, MbnE-like, Methanobactin MbnE, a periplasmic binding protein of the TonB-dependent transport system, and similar proteins. Methanobactin MbnE is a periplasmic binding protein that is involved in the TonB-dependent transport system in bacteria. The function of MbnE is to bind to methanobactin and transport it across the periplasmic space to the TonB receptor on the outer membrane of the cell. The binding of MbnE to methanobactin allows the bacteria to scavenge iron from the environment, which is essential for many biological processes. The evolutionary relationship between MbnE and the ABC transport system is not clear, as they are distinct systems that have evolved separately. However, it is possible that there have been some functional convergences between these systems in terms of nutrient uptake and transport
DFTHFDYVNPDAPKGGTLRLSAPGTFDSLNPFILKGTAAAGLFLLVYETLMTRSPDEPFSLYGLLAESVE
YPPDRSWVTFHLRPEARFSDGTPVTAEDVVFSFETLKSKGPPYYRAYYADVEKVEALDDHTVRFTFKEKA
NRELPLIVGGLPVLPKHWYEGRDFDKKRYNLEPPPGSGPYVIDSVDPGRSITYERVPDYWGKDLPVNRGR
YNFDRIRYEYYRDRTVAFEAFKAGEYDFREENSAKRWATGYDFPAVDDGRVIKEEFPHGNPQGMQGFVFN
TRRPKFQDIRVREALALAFDFEWMNKNLFYGQYTRTRFNLRKALELLAEAGWTVRGGDILVNADGEPLSF
EILLDSPTFERVLLPYVRNLKKLGIDASLRLVDSAQYQKRLRSFDFDMITAAWGQSLSPGNEQRFHWGSA
AADKPGSNNLAGIKDPAVDALIEAVLAADDREELVAAVRALDRVLRAGHYVIPQWYLPYHRVAYWDRFGR
P
>gnl|CDD|173863 cd08498, PBP2_NikA_DppA_OppA_like_2, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLRIALAADPTSLDPHFHNEGPTLAVLHNIYDTLVRRDADLKLEPGLATSWEAVDDTTWRFKLREGVKFH
DGSPFTAEDVVFSLERARDPPSSPASFYLRTIKEVEVVDDYTVDIKTKGPNPLLPNDLTNIFIMSKPWAE
AIAKTGDFNAGRNPNGTGPYKFVSWEPGDRTVLERNDDYWGGKPNWDEVVFRPIPNDATRVAALLSGEVD
VIEDVPPQDIARLKANPGVKVVTGPSLRVIFLGLDQRRDELPAGSPLGKNPLKDPRVRQALSLAIDREAI
VDRVMRGLATPAGQLVPPGVFGGEPLDKPPPYDPEKAKKLLAEAGYPDGFELTLHCPNDRYVNDEAIAQA
VAGMLARIGIKVNLETMPKSVYFPRATKGEADFYLLGWGVPTGDASSALDALLHTPDPEKGLGAYNRGGY
SNPEVDALIEAAASEMDPAKRAALLQEAQEIVADDAAYIPLHQQVLIWAARKGIDLTPRAD
>gnl|CDD|173864 cd08499, PBP2_Ylib_like, The substrate-binding component of an uncharacterized ABC-type peptide import system Ylib contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an uncharacterized ATP-binding cassette (ABC)-type peptide transport system YliB. Although the ligand specificity of Ylib protein is not known, it shares significant sequence similarity to the ABC-type dipeptide and oligopeptide binding proteins. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
DLVIAVLSDATSLDPHDTNDTPSASVQSNIYEGLVGFDKDMKIVPVLAESWEQSDDGTTWTFKLREGVKF
HDGTPFNAEAVKANLDRVLDPETASPRASLFSMIEEVEVVDDYTVKITLKEPFAPLLAHLAHPGGSIISP
KAIEEYGKEISKHPVGTGPFKFESWTPGDEVTLVKNDDYWGGLPKVDTVTFKVVPEDGTRVAMLETGEAD
IAYPVPPEDVDRLENSPGLNVYRSPSISVVYIGFNTQKEPFDDVRVRQAINYAIDKEAIIKGILNGYGTP
ADSPIAPGVFGYSEQVGPYEYDPEKAKELLAEAGYPDGFETTLWTNDNRERIKIAEFIQQQLAQIGIDVE
IEVMEWGAYLEETGNGEEHQMFLLGWSTSTGDADYGLRPLFHSSNWGAPGNRAFYSNPEVDALLDEARRE
ADEEERLELYAKAQEIIWEDAPWVFLYHPETLAGVSKEVKGFYIYPSGGFSLKD
>gnl|CDD|173865 cd08500, PBP2_NikA_DppA_OppA_like_4, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
PKNPLVVTPYESVGQYGGTLNPALADEWGSRDIIGLGYAGLVRYDPDTGELVPNLAESWEVSEDGREFTF
KLREGLKWSDGQPFTADDVVFTYEDIYLNPEIPPSAPDTLLVGGKPPKVEKVDDYTVRFTLPAPNPLFLA
YLAPPDIPTLGPWKLESYTPGERVVLERNPYYWKVDTEGNQLPYIDRIVYQIVEDAEAQLLKFLAGEIDL
QGRHPEDLDYPLLKENEEKGGYTVYNLGPATSTLFINFNLNDKDPVKRKLFRDVRFRQALSLAINREEII
ETVYFGLGEPQQGPVSPGSPYYYPEWELKYYEYDPDKANKLLDEAGLKKKDADGFRLDPDGKPVEFTLIT
NAGNSIREDIAELIKDDWRKIGIKVNLQPIDFNLLVTRLSANEDWDAILLGLTGGGPDPALGAPVWRSGG
SLHLWNQPYPGGGPPGGPEPPPWEKKIDDLYDKGAVELDQEKRKALYAEIQKIAAENLPVIGTVGPLAPV
AVKNRLGNV
>gnl|CDD|173866 cd08501, PBP2_Lpqw, The substrate-binding domain of mycobacterial lipoprotein Lpqw contains type 2 periplasmic binding fold. LpqW is one of key players in synthesis and transport of the unique components of the mycobacterial cell wall which is a complex structure rich in two related lipoglycans, the phosphatidylinositol mannosides (PIMs) and lipoarabinomannans (LAMs). Lpqw is a highly conserved lipoprotein that transport intermediates from a pathway for mature PIMs production into a pathway for LAMs biosynthesis, thus controlling the relative abundance of these two essential components of cell wall. LpqW is thought to have been adapted by the cell-wall biosynthesis machinery of mycobacteria and other closely related pathogens, evolving to play an important role in PIMs/LAMs biosynthesis. Most of periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the LpqW protein. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
ELTVAIDELGPGFNPHSAAGNSTYTSALASLVLPSAFRYDPDGTDVPNPDYVGSVEVTSDDPQTVTYTIN
PEAQWSDGTPITAADFEYLWKAMSGEPGTYDPASTDGYDLIESVEKGDGGKTVVVTFKQPYADWRALFSN
LLPAHLVADEAGFFGTGLDDHPPWSAGPYKVESVDRGRGEVTLVRNDRWWGDKPPKLDKITFRAMEDPDA
QINALRNGEIDAADVGPTEDTLEALGLLPGVEVRTGDGPRYLHLTLNTKSPALADVAVRKAFLKAIDRDT
IARIAFGGLPPEAEPPGSHLLLPGQAGYEDNSSAYGKYDPEAAKKLLDDAGYTLGGDGIEKDGKPLTLRI
AYDGDDPTAVAAAELIQDMLAKAGIKVTVVSVPSNDFSKTLLSGGDYDAVLFGWQGTPGVANAGQIYGSC
SESSNFSGFCDPEIDELIAEALTTTDPDEQAELLNEADKLLWEQAYTLPLYQGPGLVAVKKGLANV
>gnl|CDD|173867 cd08502, PBP2_NikA_DppA_OppA_like_16, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLRVVPQADLRTLDPIVTTAYITRNHGYMIYDTLFGMDANGEPQPQMAESWEVSDDGKTYTFTLRDGLKF
HDGSPVTAADVVASLKRWAKRDAMGQALMAAVESLEAVDDKTVVITLKEPFGLLLDALAKPSSQPAFIMP
KRIAATPPDKQITEYIGSGPFKFVEWEPDQYVVYEKFADYVPRKEPPSGLAGGKVVYVDRVEFIVVPDAN
TAVAALQSGEIDFAEQPPADLLPTLKADPVVVLKPLGGQGVLRFNHLQPPFDNPKIRRAVLAALDQEDLL
AAAVGDPDFYKVCGSMFPCGTPWYSEAGKEGYNKPDLEKAKKLLKEAGYDGEPIVILTPTDYAYLYNAAL
VAAQQLKAAGFNVDLQVMDWATLVQRRAKPDGGWNIFITSWSGLDLLNPLLNTGLNAGKAWFGWPDDPEI
EALRAAFIAATDPAERKALAAEIQKRAYEDVPYIPLGQFTQPTAYRSKLEGL
>gnl|CDD|173868 cd08503, PBP2_NikA_DppA_OppA_like_17, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
PKRGGTLRVAVPGGSTADTLDPHTADSSADYVRGFALYEYLVEIDPDGTLVPDLAESWEPNDDATTWTFK
LRKGVTFHDGKPLTADDVVASLNRHRDPASGSPAKTGLLDVGAIEAVDDHTVRFTLKRPNADFPYLLSDY
HFPIVPAGDGGDDFKNPIGTGPFKLESFEPGVRAVLERNPDYWKPGRPYLDRIEFIDIPDPAARVNALLS
GQVDVINQVDPKTADLLKRNPGVRVLRSPTGTHYTFVMRTDTAPFDDPRVRRALKLAVDREALVETVLLG
YGTVGNDHPVAPIPPYYADLPQREYDPDKAKALLAEAGLPDLEVELVTSDAAPGAVDAAVLFAEQAAQAG
ININVKRVPADGYWSDVWMKKPFSATYWGGRPTGDQMLSLAYRSGAPWNETHWANPEFDALLDAARAELD
EAKRKELYAEMQQILHDEGGIIIPYFRSYLDAHSDKVKGY
>gnl|CDD|173869 cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
QVLNLGIGSEPPTLDPAKATDSASSNVLNNLFEGLYRLDKDGKIVPGLAESWEVSDDGLTYTFHLRKDAK
WSNGDPVTAQDFVYSWRRALDPKTASPYAYLLYPIKNAEAINAGKKPPDELGVKALDDYTLEVTLEKPTP
YFLSLLAHPTFFPVNQKFVEKYGGKYGTSPENIVYNGPFKLKEWTPNDKIVLVKNPNYWDAKNVKLDKIN
FLVIKDPNTALNLFEAGELDIAGLPPEQVILKLKNNKDLKSTPYLGTYYLEFNTKKPPLDNKRVRKALSL
AIDREALVEKVLGDAGGFVPAGLFVPPGTGGDFRDEAGKLLEYNPEKAKKLLAEAGYELGKNPLKLTLLY
NTSENHKKIAEAIQQMWKKNLGVKVTLKNVEWKVFLDRRRKGDFDIARSGWGADYNDPSTFLDLFTSGSG
NNYGGYSNPEYDKLLAKAATETDPEKRWELLAKAEKILLDDAPIIPLYQYVTAYLVKPKVKGLVYNPLGG
YDFKYAYL
>gnl|CDD|173870 cd08505, PBP2_NikA_DppA_OppA_like_18, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
VLYYAFSARPKGLDPAQSYDSYSAEIIEQIYEPLLQYHYLKRPYELVPNTAAAMPEVSYLDVDGSVYTIR
IKPGIYFQPDPAFPKGKTRELTAEDYVYSIKRLADPPLEGVEAVDRYTLRIRLTGPYPQFLYWLAMPFFA
PVPWEAVEFYGQPGMAEKNLTLDWHPVGTGPYMLTENNPNSRMVLVRNPNYRGEVYPFEGSADDDQAGLL
ADAGKRLPFIDRIVFSLEKEAQPRWLKFLQGYYDVSGISSDAFDQALRVSAGGEPELTPELAKKGIRLSR
AVEPSIFYIGFNMLDPVVGGYSKEKRKLRQAISIAFDWEEYISIFRNGRAVPAQGPIPPGIFGYRPGEDG
KPVRYDLELAKALLAEAGYPDGRDGPTGKPLVLNYDTQATPDDKQRLEWWRKQFAKLGIQLNVRATDYNR
FQDKLRKGNAQLFSWGWNADYPDPENFLFLLYGPNAKSGGENAANYSNPEFDRLFEQMKTMPDGPERQAL
IDQMNRILREDAPWIFGFHPKSNGLAHPWVGNYKPNPM
>gnl|CDD|173871 cd08506, PBP2_clavulanate_OppA2, The substrate-binding domain of an oligopeptide binding protein (OppA2) from the biosynthesis pathway of the beta-lactamase inhibitor clavulanic acid contains the type 2 periplasmic binding fold. Clavulanic acid (CA), a clinically important beta-lactamase inhibitor, is one of a family of clavams produced as secondary metabolites by fermentation of Streptomyces clavuligeru. The biosynthesis of CA proceeds via multiple steps from the precursors, glyceraldehyde-3-phosphate and arginine. CA possesses a characteristic (3R,5R) stereochemistry essential for reaction with penicillin-binding proteins and beta-lactamases. Two genes (oppA1 and oppA2) in the clavulanic acid gene cluster encode oligopeptide-binding proteins that are required for CA biosynthesis. OppA1/2 is involved in the binding and transport of peptides across the cell membrane of Streptomyces clavuligerus. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLRLLSSADFDHLDPARTYYADGWQVLRLIYRQLTTYKPAPGAEGTEVVPDLATDTGTVSDDGKTWTYTL
RDGLKFEDGTPITAKDVKYGIERSFAIETPDDKTIVFHLNRPDSDFPYLLALPAAAPVPAEKDTKADYGR
APVSSGPYKIESYDPGKGLVLVRNPHWDAETDPIRDAYPDKIVVTFGLDPETIDQRLQAGDADLALDGDG
VPRAPAAELVEELKARLHNVPGGGVYYLAINTNVPPFDDVKVRQAVAYAVDRAALVRAFGGPAGGEPATT
ILPPGIPGYEDYDPYPTKGPKGDPDKAKELLAEAGVPGLKLTLAYRDTAVDKKIAEALQASLARAGIDVT
LKPIDSATYYDTIANPDGAAYDLFITGWGPDWPSASTFLPPLFDGDAIGPGGNSNYSGYDDPEVNALIDE
ALATTDPAEAAALWAELDRQIMEDAPIVPLVYPKALDLRSSRVTNY
>gnl|CDD|173872 cd08507, PBP2_SgrR_like, The C-terminal solute-binding domain of DNA-binding transcriptional regulator SgrR is related to the ABC-type oligopeptide-binding proteins and contains the type 2 periplasmic-binding fold. A novel family of SgrR transcriptional regulator contains a two-domain structure with an N terminal DNA-binding domain of the winged helix family and a C-terminal solute-binding domain. The C-terminal domain shows strong homology with the ABC-type oligopeptide-binding protein family, a member of the type 2 periplasmic-binding fold protein (PBP2) superfamily that also includes the C-terminal substrate-binding domain of LysR-type transcriptional regulators. SgrR (SugaR transport-related Regulator) is negatively autoregulated and activates transcription of divergent operon SgrS, which encodes a small RNA required for recovery from glucose-phosphate stress. Hence, the small RNA SgrS and SgrR, the transcription factor that controls sgrS expression, are both required for recovery from glucose-phosphate stress. Most of periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
REGKDVLRLPYYRPLPTLDPGTPLRRSESHLVRQIFDGLVRYDEENGEIEPDLAHHWESNDDLTHWTFYL
RKGVRFHNGRELTAEDVVFTLLRLRELESYSWLLSHIEQIESPSPYTVDIKLSKPDPLFPRLLASANASI
LPADILFDPDFARHPIGTGPFRVVENTDKRLVLEAFDDYFGERPLLDEVEIWVVPELYENLVYPPQSTYL
QYEESDSDEQQESRLEEGCYFLLFNQRKPGAQDPAFRRALSELLDPEALIQHLGGERQRGWFPAYGLLPE
WPREKIRRLLKESEYPGEELTLATYNQHPHREDAKWIQQRLAKHGIRLEIHILSYEELLEGDADSMADLW
LGSANFADDLEFSLFAWLLDKPLLRHGCILEDLDALLAQWRNEELAQAPLEEIEEQLVDEAWLLPLFHHW
LTLSFHPSLQGVALNSLGWFDFKSVWFK
>gnl|CDD|173873 cd08508, PBP2_NikA_DppA_OppA_like_1, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLRIGSAADDIRTLDPHFATGTTDKGVISWVFNGLVRFPPGSADPYEIEPDLAESWESSDDPLTWTFKLR
KGVMFHGGYGEVTAEDVVFSLERAADPKRSSFSADFAALKEVEAHDPYTVRITLSRPVPSFLGLVSNYHS
GLIVSKKAVEKLGEQFGRKPVGTGPFEVEEHSPQQGVTLVANDGYFRGAPKLERINYRFIPNDASRELAF
ESGEIDMTQGKRDQRWVQRREANDGVVVDVFEPAEFRTLGLNITKPPLDDLKVRQAIAAAVNVDEVVEFV
GAGVAQPGNSVIPPGLLGEDADAPVYPYDPAKAKALLAEAGFPNGLTLTFLVSPAAGQQSIMQVVQAQLA
EAGINLEIDVVEHATFHAQIRKDLSAIVLYGAARFPIADSYLTEFYDSASIIGAPTAVTNFSHCPVADKR
IEAARVEPDPESRSALWKEAQKKIDEDVCAIPLTNLVQAWARKPALDYGY
>gnl|CDD|173874 cd08509, PBP2_TmCBP_oligosaccharides_like, The substrate binding domain of a cellulose-binding protein from Thermotoga maritima contains the type 2 periplasmic binding fold. This family represents the substrate-binding domain of a cellulose-binding protein from the hyperthermophilic bacterium Thermotoga maritima (TmCBP) and its closest related proteins. TmCBP binds a variety of lengths of beta-1,4-linked glucose oligomers, ranging from two sugar rings (cellobiose) to five (cellopentose). TmCBP is structurally homologous to domains I and III of the ATP-binding cassette (ABC)-type oligopeptide-binding proteins and thus belongs to the type 2 periplasmic binding fold protein (PBP2) superfamily. The type 2 periplasmic binding proteins are soluble ligand-binding components of ABC or tripartite ATP-independent transporters and chemotaxis systems. Members of the PBP2 superfamily function in uptake of a variety of metabolites in bacteria such as amino acids, carbohydrate, ions, and polyamines. Ligands are then transported across the cytoplasmic membrane energized by ATP hydrolysis or electrochemical ion gradient. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLIVGGGTGGTPPSNFNPYAPGGASTAGLVQLIYEPLAIYNPLTGEFIPWLAESWTWSDDFTTLTVTLRK
GVKWSDGEPFTADDVVFTFELLKKYPALDYSGFWYYVESVEAVDDYTVVFTFKKPSPTEAFYFLYTLGLV
PIVPKHVWEKVDDPLITFTNEPPVGTGPYTLKSFSPQWIVLERNPNYWGAFGKPKPDYVVYPAYSSNDQA
LLALANGEVDWAGLFIPDIQKTVLKDPENNKYWYFPYGGTVGLYFNTKKYPFNDPEVRKALALAIDRTAI
VKIAGYGYATPAPLPGPPYKVPLDPSGIAKYFGSFGLGWYKYDPDKAKKLLESAGFKKDKDGKWYTPDGT
PLKFTIIVPSGWTDWMAAAQIIAEQLKEFGIDVTVKTPDFGTYWAALTKGDFDTFDAATPWGGPGPTPLG
YYNSAFDPPNGGPGGSAAGNFGRWKNPELDELIDELNKTTDEAEQKELGNELQKIFAEEMPVIPLFYNPI
WYEYNTKYWTGWPTEENPY
>gnl|CDD|173875 cd08510, PBP2_Lactococcal_OppA_like, The substrate binding component of an ABC-type lactococcal OppA-like transport system contains. This family represents the substrate binding domain of an ATP-binding cassette (ABC)-type oligopeptide import system from Lactococcus lactis and other gram-positive bacteria, as well as its closet homologs from gram-negative bacteria. Oligopeptide-binding protein (OppA) from Lactococcus lactis can bind peptides of length from 4 to at least 35 residues without sequence preference. The oligopeptide import system OppABCDEF is consisting of five subunits: two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and also is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
GGTLKVALVSDSPFKGIFSSELYEDNTDAEIMGFGNEGLFDTDKNYKITDSGAAKFKLDDKAKTVTITIK
DGVKWSDGKPVTAKDLEYSYEIIANKDYTGVRYTDSFKNIVGMEEYHDGKADTISGIKKIDDKTVEITFK
EMSPSMLQSGNGYFEYAEPKHYLKDVPVKKLESSDQVRKNPLGFGPYKVKKIVPGESVEYVPNEYYWRGK
PKLDKIVIKVVSPSTIVAALKSGKYDIAESPPSQWYDQVKDLKNYKFLGQPALSYSYIGFKLGKWDKKKG
ENVMDPNAKMADKNLRQAMAYAIDNDAVGKKFYNGLRTRANSLIPPVFKDYYDSELKGYTYDPEKAKKLL
DEAGYKDVDGDGFREDPDGKPLTINFAAMSGSETAEPIAQYYIQQWKKIGLNVELTDGRLIEFNSFYDKL
QADDPDIDVFQGAWGTGSDPSPSGLYGENAPFNYSRFVSEENTKLLDAIDSEKAFDEEYRKKAYKEWQKY
MNEEAPVIPTLYRYSITPVNKRVKGY
>gnl|CDD|173876 cd08511, PBP2_NikA_DppA_OppA_like_5, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This family represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
GTLRIGLEADPDRLDPALSRTFVGRQVFAALCDKLVDIDADLKIVPQLATSWEISPDGKTLTLKLRKGVK
FHDGTPFDAAAVKANLERLLTLPGSNRKSELASVESVEVVDPATVRFRLKQPFAPLLAVLSDRAGMMVSP
KAAKAAGADFGSAPVGTGPFKFVERVQQDRIVLERNPHYWNAGKPHLDRLVYRPIPDATVRLANLRSGDL
DIIERLSPSDVAAVKKDPKLKVLPVPGLGYQGITFNIGNGPFNDPRVRQALALAIDREAINQVVFNGTFK
PANQPFPPGSPYYGKSLPVPGRDPAKAKALLAEAGVPTVTFELTTANTPTGRQLAQVIQAMAAEAGFTVK
LRPTEFATLLDRALAGDFQATLWGWSGRPDPDGNIYQFFTSKGGQNYSRYSNPEVDALLEKARASADPAE
RKALYNQAAKILADDLPYIYLYHQPYYIAASKKVRGLVPYPDGIVRL
>gnl|CDD|173877 cd08512, PBP2_NikA_DppA_OppA_like_7, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
PKDTLVVATSADINTLDPAVAYEVASGEVVQNVYDRLVTYDGEDTGKLVPELAESWEVSDDGKTYTFHLR
DGVKFHDGNPVTAEDVKYSFERALKLNKGPAFILTQTSLNVPETIKAVDDYTVVFKLDKPPALFLSTLAA
PVASIVDKKLVKEHGKDGDWGNAWLSTNSAGSGPYKLKSWDPGEEVVLERNDDYWGGAPKLKRVIIRHVP
EAATRRLLLERGDADIARNLPPDDVAALEGNPGVKVISLPSLTVFYLALNTKKAPFDNPKVRQAIAYAID
YDGIIDQVLKGQGKPHPGPLPDGLPGGAPDLPPYKYDLEKAKELLAEAGYPNGFKLTLSYNSGNEPREDI
AQLLQASLAQIGIKVEIEPVPWAQLLEAARSREFDIFIGGWGPDYPDPDYFAATYNSDNGDNAANRAWYD
NPELDALIDEARAETDPAKRAALYKELQKIVYDDAPYIPLYQPVEVVAVRKNVKGY
>gnl|CDD|173878 cd08513, PBP2_thermophilic_Hb8_like, The substrate-binding component of ABC-type thermophilic oligopeptide-binding protein Hb8-like import systems, contains the type 2 periplasmic binding fold. This family includes the substrate-binding domain of an ABC-type oligopeptide-binding protein Hb8 from Thermus thermophilius and its closest homologs from other bacteria. The structural topology of this substrate-binding domain is similar to those of DppA from Escherichia coli and OppA from Salmonella typhimurium, and thus belongs to the type 2 periplasmic binding fold protein (PBP2) superfamily. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. The type 2 periplasmic binding proteins are soluble ligand-binding components of ABC or tripartite ATP-independent transporters and chemotaxis systems. Members of the PBP2 superfamily function in uptake of a variety of metabolites in bacteria such as amino acids, carbohydrate, ions, and polyamines. Ligands are then transported across the cytoplasmic membrane energized by ATP hydrolysis or electrochemical ion gradient. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLVIGLSQEPTTLNPLLASGATDAEAAQLLFEPLARIDPDGSLVPVLAEEIPTSENGLSVTFTLRPGVKW
SDGTPVTADDVVFTWELIKAPGVSAAYAAGYDNIASVEAVDDYTVTVTLKKPTPYAPFLFLTFPILPAHL
LEGYSGAAARQANFNLAPVGTGPYKLEEFVPGDSIELVRNPNYWGGKPYIDRVVLKGVPDTDAARAALRS
GEIDLAWLPGAKDLQQEALLSPGYNVVVAPGSGYEYLAFNLTNHPILADVRVRQALAYAIDRDAIVKTLY
GGKATPAPTPVPPGSWADDPLVPAYEYDPEKAKQLLDEAGWKLGPDGGIREKDGTPLSFTLLTTSGNAVR
ERVAELIQQQLAKIGIDVEIENVPASVFFSDDPGNRKFDLALFGWGLGSDPDLSPLFHSCASPANGWGGQ
NFGGYSNPEADELLDAARTELDPEERKALYIRYQDLLAEDLPVIPLYFRNQVSAYKKNLKGV
>gnl|CDD|173879 cd08514, PBP2_AppA_like, The substrate-binding component of the oligopeptide-binding protein, AppA, from Bacillus subtilis contains the type 2 periplasmic-binding fold. This family represents the substrate-binding domain of the oligopeptide-binding protein, AppA, from Bacillus subtilis and its closest homologs from other bacteria and archaea. Bacillus subtilis has three ABC-type peptide transport systems, a dipeptide-binding protein (DppA) and two oligopeptide-binding proteins (OppA and AppA) with overlapping specificity. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and also is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLVLATGGDPSNLNPILSTDSASSEVAGLIYEGLLKYDKDLNFEPDLAESWEVSDDGKTYTFKLRKDVKW
HDGEPLTADDVKFTYKAIADPKYAGPRASGDYDEIKGVEVPDDYTVVFHYKEPYAPALESWALNGILPKH
LLEDVPIADFRHSPFNRNPVGTGPYKLKEWKRGQYIVLEANPDYFLGRPYIDKIVFRIIPDPTTALLELK
AGELDIVELPPPQYDRQTEDKAFDKKINIYEYPSFSYTYLGWNLKRPLFQDKRVRQAITYAIDREEIIDG
LLLGLGEVANGPFSPGTWAYNPDLKPYPYDPDKAKELLAEAGWVDGDDDGILDKDGKPFSFTLLTNQGNP
VREQAATIIQQQLKEIGIDVKIRVLEWAAFLEKVDDKDFDAVLLGWSLGPDPDPYDIWHSSGAKPGGFNF
VGYKNPEVDKLIEKARSTLDREKRAEIYHEWQEILAEDQPYTFLYAPNSLYAVNKRLKGIKPA
>gnl|CDD|173880 cd08515, PBP2_NikA_DppA_OppA_like_10, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
RDTLVIAVQKEPPTLDPYYNTSREGVIISRNIFDTLIYRDPDTGELVPGLATSWKWIDDTTLEFTLREGV
KFHDGSPMTAEDVVFTFNRVRDPDSKAPRGRQNFNWLDKVEKVDPYTVRIVTKKPDPAALERLAGLVGPI
VPKAYYEKVGPEGFALKPVGTGPYKVTEFVPGERVVLEAFDDYWGGKPPIEKITFRVIPDVSTRVAELLS
GGVDIITNVPPDQAERLKSSPGLTVVGGPTMRIGFITFDAAGPPLKDVRVRQALNHAIDRQAIVKALWGG
RAKVPNTACQPPQFGCEFDVDTKYPYDPEKAKALLAEAGYPDGFEIDYYAYRGYYPNDRPVAEAIVGMWK
AVGINAELNVLSKYRALRAWSKGGLFVPAFFYTWGSNGINDASASTSTWFKARDAEFDELLEKAETTTDP
AKRKAAYKKALKIIAEEAYWTPLYQYSQNYGYSKDLNWTP
>gnl|CDD|173881 cd08516, PBP2_NikA_DppA_OppA_like_11, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
TLRFGLSTDPDSLDPHKATAAASEEVLENIYEGLLGPDENGKLVPALAESWEVSDDGLTYTFKLRDGVKF
HNGDPVTAADVKYSFNRIADPDSGAPLRALFQEIESVEAPDDATVVIKLKQPDAPLLSLLASVNSPIIPA
ASGGDLATNPIGTGPFKFASYEPGVSIVLEKNPDYWGKGLPKLDGITFKIYPDENTRLAALQSGDVDIIE
YVPPQQAAQLEEDDGLKLASSPGNSYMYLALNNTREPFDDPKVRQAIAYAIDRDAIVDAAFFGRGTPLGG
LPSPAGSPAYDPDDAPCYKYDPEKAKALLAEAGYPNGFDFTILVTSQYGMHVDTAQVIQAQLAAIGINVE
IELVEWATWLDDVNKGDYDATIAGTSGNADPDGLYNRYFTSGGKLNFFNYSNPEVDELLAQGRAETDEAK
RKEIYKELQQILAEDVPWVFLYWRSQYYAMNKNVQGF
>gnl|CDD|173882 cd08517, PBP2_NikA_DppA_OppA_like_13, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
GGTLNVVVQPEPPSLNPALKSDGPTQLISGKIFEGLLRYDFDLNPQPDLATSWEVSEDGLTYTFKLRPGV
KWHDGKPFTSADVKFSIDTLKEEHPRRRRTFANVESIETPDDLTVVFKLKKPAPALLSALSWGESPIVPK
HIYEGTDILTNPANNAPIGTGPFKFVEWVRGSHIILERNPDYWDKGKPYLDRIVFRIIPDAAARAAAFET
GEVDVLPFGPVPLSDIPRLKALPNLVVTTKGYEYFSPRSYLEFNLRNPPLKDVRVRQAIAHAIDRQFIVD
TVFFGYGKPATGPISPSLPFFYDDDVPTYPFDVAKAEALLDEAGYPRGADGIRFKLRLDPLPYGEFWKRT
AEYVKQALKEVGIDVELRSQDFATWLKRVYTDRDFDLAMNGGYQGGDPAVGVQRLYWSGNIKKGVPFSNA
SGYSNPEVDALLEKAAVETDPAKRKALYKEFQKILAEDLPIIPLVELGFPTVYRKRVKNL
>gnl|CDD|173883 cd08518, PBP2_NikA_DppA_OppA_like_19, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
DELVLAVGSEPETGFNPLLGWGEHGEPLIFSGLLKRDENLNLVPDLATSYKVSDDGLTWTFTLRDDVKFS
DGEPLTAEDVAFTYNTAKDPGSASDILSNLEDVEAVDDYTVKFTLKKPDSTFLDKLASLGIVPKHAYENT
DTYNQNPIGTGPYKLVQWDKGQQVIFEANPDYYGGKPKFKKLTFLFLPDDAAAAALKSGEVDLALIPPSL
AKQGVDGYKLYSIKSADYRGISLPFVPATGKKIGNNVTSDPAIRKALNYAIDRQAIVDGVLNGYGTPAYS
PPDGLPWGNPDAAIYDYDPEKAKKILEEAGWKDGDDGGREKDGQKAEFTLYYPSGDQVRQDLAVAVASQA
KKLGIEVKLEGKSWDEIDPRMHDNAVLLGWGSPDDTELYSLYHSSLAGGGYNNPGHYSNPEVDAYLDKAR
TSTDPEERKKYWKKAQWDGAEDPPWLWLVNIDHLYVVNDGLDGG
>gnl|CDD|173884 cd08519, PBP2_NikA_DppA_OppA_like_20, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
RIVVGTTDKVRTLDPAGAYDLGSWQLLSNLGDTLYTYEPGTTELVPDLATSLPFVSDDGLTYTIPLRQGV
KFHDGTPFTAKAVKFSLDRFIKIGGGPASLLADRVESVEAPDDYTVTFRLKKPFATFPALLATPALTPVS
PKAYPADADLFLPNTFVGTGPYKLKSFRSESIRLEPNPDYWGEKPKNDGVDIRFYSDSSNLFLALQTGEI
DVAYRSLSPEDIADLLLAKDGDLQVVEGPGGEIRYIVFNVNQPPLDNLAVRQALAYLIDRDLIVNRVYYG
TAEPLYSLVPTGFWGHKPVFKEKYGDPNVEKARQLLQQAGYSAENPLKLELWYRSNHPADKLEAATLKAQ
LEADGLFKVNLKSVEWTTYYKQLSKGAYPVYLLGWYPDYPDPDNYLTPFLSCGNGVFLGSFYSNPKVNQL
IDKSRTELDPAARLKILAEIQDILAEDVPYIPLWQGKQYAVAQKNVKGV
>gnl|CDD|173885 cd08520, PBP2_NikA_DppA_OppA_like_21, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction
VLRLADGDGDWGYPSPYTHYPRGPGYVKMSLIFDSLVWKDEKGFIPWLAESWEVSEDGLTYTFHLREGAK
WHDGEPLTAEDVAFTFDYMKKHPYVWVDIELSIIERVEALDDYTVKITLKRPYAPFLEKIATTVPILPKH
IWEKVEDPEKFTGPEAAIGSGPYKLVDYNKEQGTYLYEANEDYWGGKPKVKRLEFVPVSDALLALENGEV
DAISILPDTLAALENNKGFKVIEGPGFWVYRLMFNHDKNPFSDKEFRQAIAYAIDRQELVEKAARGAAAL
GSPGYLPPDSPWYNPNVPKYPYDPEKAKELLKGLGYTDNGGDGEKDGEPLSLELLTSSSGDEVRVAELIK
EQLERVGIKVNVKSLESKTLDSAVKDGDYDLAISGHGGIGGDPDILREVYSSNTKKSARGYDNEELNALL
RQQLQEMDPEKRKELVFEIQELYAEELPMIPLYYPTMYTVHRGKYDGW
>gnl|CDD|176056 cd08521, C2A_SLP, C2 domain first repeat present in Synaptotagmin-like proteins. All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. Slp5 mRNA has been shown to be restricted to human placenta and liver suggesting a role in Rab27A-dependent membrane trafficking in specific tissues. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology
GEIEFSLSYNYKTGSLEVHIKECRNLAYADEKKKRSNPYVKVYLLPDKSKQSKRKTSVKKNTTNPVFNET
LKYHISKSQLETRTLQLSVWHHDRFGRNTFLGEVEIPLDSWDLDSQQSEWYPL
>gnl|CDD|260080 cd08523, Reeler_cohesin_like, Domains similar to the eukaryotic reeler domain and bacterial cohesins. This diverse family summarizes a set of distantly related domains, as revealed by structural similarity
VSLRALGDVQVGTNLEVTLSIDEPVNFAPEIEFTVNLKSNSDLFEEFHATAHNIDPSCDHGTMIDKNDIA
IDVDVRRLSFSWTPAQEVRAKVSLRAEPKAEHVYLSASSEKGDVREIAGTDEGSGEKT
>gnl|CDD|197341 cd08524, Reelin_subrepeat_like, Tandem repeat subunit of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the subrepeats, which directly contact each other in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1). Genetic deficiency of reelin, or ApoER2 and VLDLR, or Dab1, all exhibit the same phenotypes, including ataxia, cortical layer inversion and abnormal positioning patterns
LKDDFDGYPSPDNWLLCPGGKTGTVCGALSSGNALVFNEPYGPRELVTTDLNTNEASFLQFYIGSGCSTP
SYSNQPVLLEYSVDNGASWHLLEEIRADSFSKWRIIILYLPEDAKSGATRFRWWQPNHRGVYQATWAIDN
VLIG
>gnl|CDD|197342 cd08525, Reelin_subrepeat_1, N-terminal subrepeat in the tandem repeat unit of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the N-terminal subrepeat, which directly contacts the C-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
VLLDTFDTLPDSNENWFFYPGGVVKNDCGSTDSALVFTENIGGERYAVTRDLTVNEGYMLQFKINVGCSS
TFSSSNSVMLEYSTDAGLSWHLVQEECLPSSPGCSELHPSSVYESSTFNGWKRITIPLPNATLSSATRFR
WIQYGYTSGVQTWAIDNVYIG
>gnl|CDD|197343 cd08526, Reelin_subrepeat_2, C-terminal subrepeat in the tandem repeat unit of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the C-terminal subrepeat, which directly contacts the N-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
FLKDSFEGSLSSSDNWSLVSGGEVGTGCGVLASGKALYFNGPGLRQLVTVDLDLTNARFVQFYLRIGSKS
QTSTCNPPDSRSEGVLLQYSVNGGITWHLLQELYYDQYSEPRFVSIELPLEARTNGTRFRWWQPSHSGKG
QDQWALDNILIG
>gnl|CDD|270867 cd08528, STKc_Nek10, Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EYAVLELLGSGAFGCVYKVRKKSNGQTLLALKEINMTNPAFGRTEQERDKSVGDIISEVNIIKEQLRHPN
IVRYYKTFLENDRLYIVMELIEGAPLGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHKEKQIVHRDL
KPNNIMLGEDDKVTITDFGLAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTL
QPPFYSTNMLTLATKIVEAEYEPLPEGMYSDDITFVIRSCLTPDPEARPDIVEVSSMISD
>gnl|CDD|270868 cd08529, STKc_FA2-like, Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVD
KGKLNIVMEYAENGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNV
KIGDLGVAKILSDTTNFAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALI
LKIVRGKYPPISASYSQDLSQLIDSCLTKDYRQRPDTTELLRNPSL
>gnl|CDD|270869 cd08530, STKc_CNK2-like, Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLD
GNRLCIVMEYAPFGDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGD
LVKIGDLGISKVLKKNLAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELR
YKVCRGKFPPIPPVYSQDLQQIIRSLLQVNPKKRPSCDKLLQSPAV
>gnl|CDD|188877 cd08531, SAM_PNT-ERG_FLI-1, Sterile alpha motif (SAM)/Pointed domain of ERG (Ets related gene) and FLI-1 (Friend leukemia integration 1) transcription factors. SAM Pointed domain of ERG/FLI-1 subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. The ERG and FLI regulators are involved in endothelial cell differentiation, bone morphogenesis and neural crest development. They are proto-oncogenes implicated in cancer development such as myeloid leukemia, Ewing's sarcoma and erythroleukemia. Members of this subfamily are potential targets for cancer therapy
VPADPLLWTREHVRQWVEWAIKEYSLKDVDVSRFDNIDGKELCRMTRDDFLRLTSAYNGDVLISHLCYLR
QTPLP
>gnl|CDD|188878 cd08532, SAM_PNT-PDEF-like, Sterile alpha motif (SAM)/Pointed domain of prostate-derived ETS factor. SAM Pointed domain of PDEF-like (Prostate-Derived ETS Factor) subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. In human males this activator is highly expressed in the prostate gland and enhances androgen-mediated activation of the PSA promoter though interaction with the DNA binding domain of androgen receptor. PDEF may play a role in prostate cancer development as well as in goblet cell formation and mucus production in the epithelial lining of respiratory and intestinal tracts
IDTTCALLGISPDPYQWSTANVQAWLQWTEHQYRLPPNPPRCFQMNGKTLCALSEEDFVRRAPQGGDTLH
AQLEIWKSAAE
>gnl|CDD|188879 cd08533, SAM_PNT-ETS-1,2, Sterile alpha motif (SAM)/Pointed domain of ETS-1,2 family. SAM Pointed domain of ETS-1,2 family of transcriptional activators is a protein-protein interaction domain. It carries a kinase docking site and mediates interaction between ETS transcriptional activators and protein kinases. This group of transcriptional factors is involved in the Ras/MAP kinase signaling pathway. MAP kinases phosphorylate the transcription factors. Phosphorylated factors then recruit coactivators and enhance transactivation. Members of this group play a role in regulation of different embryonic developmental processes. ETS-1,2 transcriptional activators are proto-oncogenes involved in malignant transformation and tumor progression. They are potential molecular targets for selective cancer therapy
PKDPRQWSETQVAYWLDWAANEFSLEGVNLSNFCMSGRDMCALGKEAFLSLAPPFVGDILWEHLDILQKE
C
>gnl|CDD|176084 cd08534, SAM_PNT-GABP-alpha, Sterile alpha motif (SAM)/Pointed domain of GA-binding protein (GABP) alpha chain. SAM Pointed domain of GA-binding protein (GABP) alpha subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. This type of transcriptional regulators forms heterotetramers containing two alpha and two beta subunits. It interacts with GA repeats (purine rich repeats). GABP transcriptional factors control gene expression in cell cycle control, apoptosis, and cellular respiration. GABP participates in regulation of transmembrane receptors and key hormones especially in myeloid cells and at the neuromuscular junction
AVDSNYRKEQERLKIPYDPMEWTEDHVLHWLQWAVKEFGLTGINLSDWNITGRELCSLTQEEFLQRVPKD
PGDIFWTHLELLRKCKFVS
>gnl|CDD|176085 cd08535, SAM_PNT-Tel_Yan, Sterile alpha motif (SAM)/Pointed domain of Tel/Yan protein. SAM Pointed domain of Tel (Translocation, Ets, Leukemia)/Yan subfamily of ETS transcriptional repressors is a protein-protein interaction domain. SAM Pointed domains of this type of regulators can interact with each other, forming head-to-tail homodimers or homooligomers, and/or interact with SAM Pointed domains of another subfamily of ETS factors forming heterodimers. The oligomeric form is able to block transcription of target genes and is involved in MAPK signaling. They participate in regulation of different processes during embryoniv development including hematopoietic differentiation and eye development. Tel/Yan transcriptional factors are frequent targets of chromosomal translocations resulting in fusions of SAM domain with new neighboring genes. Such chimeric proteins were found in different tumors. Members of this subfamily are potential targets for cancer therapy
LQPRQWSREDVLQWLRWAENEFSLPPIDSNTFEMNGKALCLLTKEDFRYRCPHAGDVLYNLLQHLLKQ
>gnl|CDD|176086 cd08536, SAM_PNT-Mae, Sterile alpha motif (SAM)/Pointed domain of Mae protein homolog. Mae (Modulator of the Activity of ETS) subfamily represents a group of SAM Pointed monodomain proteins. SAM Pointed domain is a protein-protein interaction domain. It can interact with other SAM pointed domains forming head-to-tail heterodimers and also provides a kinase docking site. For example, in Drosophila Mae is required for facilitating phosphorylation of the Yan factor and for blocking phosphorylation of the ETS-2 regulator. Mae interacts with the SAM Pointed domains of Yan and ETS-2. Binding enhances access of the kinase to the Yan phosphorylation site by providing a kinase docking site, or inhibits phosphorylation of ETS-2 by blocking its docking site. This type of factors participates in regulation of kinase signaling particularly during embryogenesis
DPRSWSREHVRTWLRWVSARYQLEVVDLDKFLMNGKGLCLMSLEGFLYRVPVGGKLLYEDFQRRLA
>gnl|CDD|188880 cd08537, SAM_PNT-ESE-1-like, Sterile alpha motif (SAM)/Pointed domain of ESE-1 like ETS transcriptional regulators. SAM Pointed domain of ESE-1-like (Epithelium-Specific ETS) subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. SAM Pointed domain of ESE-1 provides a potential docking site for signaling kinase Pak1 in humans. ESE-1 factors are involved in regulation of gene expression in different types of epithelial cells. ESE-1 is expressed in many different organs including intestine, stomach, pancreas, lungs, kidneys, and prostate. The DNA binding consensus motif for ESE-1 consists of a purine-rich GGA[AT] core sequence. The expression profile of these factors is altered in epithelial cancers if compared to normal tissues. Members of this subfamily are potential targets for cancer therapy
GTTKGSWDQENPQFWSKQNVLEWISYHVEKNKYDASSLDLSYCTMDGLTLCACAKEQLMLVFGPELGDLL
HHSLEELTSRY
>gnl|CDD|188881 cd08538, SAM_PNT-ESE-2-like, Sterile alpha motif (SAM)/Pointed domain of ESE-2 like ETS transcriptional regulators. SAM Pointed domain of ESE-2-like (Epithelium-Specific ETS) subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. It can act as a major transactivator by providing a potential docking site for co-activators. ESE-2 factors are involved in regulation of gene expression in a variety of epithelial (glandular and secretory) cells. ESE-2 mRNA was found in skin keratinocytes, salivary gland, mammary gland, stomach, prostate, and kidneys. The DNA binding consensus motif for ESE-2 consists of a GGA core and AT-rich flanks. The expression profiles of these factors are altered in epithelial cancers. Members of this subfamily are potential targets for cancer therapy
QTACDSYWTSVHPEYWTKRHVWEWLQFCCDQYKLDANCISFCHFNISGLQLCSMTQEEFLDAAGICGEYL
YFILQNIRTHGYSF
>gnl|CDD|188882 cd08539, SAM_PNT-ESE-3-like, Sterile alpha motif (SAM)/Pointed domain of ESE-3 like ETS transcriptional regulators. SAM Pointed domain of ESE-3-like (Epithelium-Specific ETS) subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. It can act as a major transactivator by providing a potential docking site for co-activators. The ESE-3 transcriptional activator is involved in regulation of glandular epithelium differentiation through the MAP kinase signaling cascade. It is found to be expressed in glandular epithelium of prostate, pancreas, salivary gland, and trachea. Additionally, ESE-3 is differentially expressed during monocyte-derived dendritic cells development. DNA binding consensus motif for ESE-3 consists of purine-rich GGAA/T core sequence. The expression profiles of these factors are altered in epithelial cancers. Members of this subfamily are potential targets for cancer therapy
GRQWHEIHPQYWTKFQVWEWLQHLLDTNQLDANCIPFQEFDINGEHLCSMSLQEFTRAAGTAGQLLYSNL
QHLKWNGQ
>gnl|CDD|176090 cd08540, SAM_PNT-ERG, Sterile alpha motif (SAM)/Pointed domain of ERG transcription factor. SAM Pointed domain of ERG subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. It may participate in formation of homodimers or heterodimers with ETS-2, Fli-1, ER81, and Pu-1. However, dimeric forms are inactive and SAM Pointed domain is not essential for dimerization, since ER81 and Pu-1 do not have it. In mouse, a regulator of this type binds the ESET histone H3-specific methyltransferase (human homolog is SETDB1), which leads to modification of the local chromatin structure through histone methylation. ERG regulators are involved in endothelial cell differentiation, bone morphogenesis and neural crest development. The Erg gene is a proto-oncogene. It is a target of chromosomal translocations resulting in fusions with other neighboring genes. Chimeric proteins were found in solid tumors such as myeloid leukemia or Ewing's sarcoma. Members of this subfamily are potential targets for cancer therapy
VPADPTLWSTDHVRQWLEWAVKEYGLPDVDVLLFQNIDGKELCKMTKEDFQRLTPSYNADILLSHLHYLR
ETPLP
>gnl|CDD|188883 cd08541, SAM_PNT-FLI-1, Sterile alpha motif (SAM)/Pointed domain of friend leukemia integration 1 transcription activator. SAM Pointed domain of FLI-1 (Friend Leukemia Integration) subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. The FLI-1 protein participates in regulation of cellular differentiation, proliferation, and survival. The Fli-1 gene was initially described in Friend virus-induced erythroleukemias as a site for virus integration. It is highly expressed in hematopoietic tissues and at lower level in lungs, heart, and ovaries. Fli-1 is a proto-oncogene implicated in Ewing's sarcoma and erythroleukemia. Members of this subfamily are potential targets for cancer therapy
PPNMTTNERRVIVPADPTLWSQDHVRQWLEWAIKEYGLMEIDTSLFQNMDGKELCKMSKEDFLRLTSLYN
TEVLLSHLNYLRESSSSLSYN
>gnl|CDD|176092 cd08542, SAM_PNT-ETS-1, Sterile alpha motif (SAM)/Pointed domain of ETS-1. SAM Pointed domain of ETS-1 subfamily of ETS transcriptional activators is a protein-protein interaction domain. The ETS-1 activator is regulated by phosphorylation. It contains a docking site for the ERK2 MAP (Mitogen Activated Protein) kinase, while the ERK2 phosphorylation site is located in the N-terminal disordered region upstream of the SAM Pointed domain. Mutations of the kinase docking site residues inhibit phosphorylation. ETS-1 activators play a role in a number of different physiological processes, and they are expressed during embryonic development, including blood vessel formation, hematopoietic, lymphoid, neuronal and osteogenic differentiation. The Ets-1 gene is a proto-oncogene involved in progression of different tumors (including breast cancer, meningioma, and prostate cancer). Members of this subfamily are potential molecular targets for selective cancer therapy
ATFSGFTKEQQRLGIPKDPREWTETHVREWVMWAVNEFSLKGVDFQKFCMSGAALCALGKECFLELAPDF
VGDILWEHLEILQKEDPK
>gnl|CDD|188884 cd08543, SAM_PNT-ETS-2, Sterile alpha motif (SAM)/Pointed domain of ETS-2. SAM Pointed domain of ETS-2 subfamily of ETS transcriptional regulators is a protein-protein interaction domain. It contains a docking site for Cdk10 (cyclin-dependent kinase 10), a member of the Cdc2 kinase family. The interaction between ETS-2 and Cdk10 kinase inhibits ETS-2 transactivation activity in mammals. ETS-2 is also regulated by ERK2 MAP kinase. ETS-2, which is phosphorylated by ERK2, can interact with coactivators and enhance transactivation. ETS-2 transcriptional activators are involved in embryonic development and cell cycle control. The Ets-2 gene is a proto-oncogene. It is overexpressed in breast and prostate cancer cells and its overexpression is necessary for transformation of such cells. Members of ETS-2 subfamily are potential molecular targets for selective cancer therapy
DTFSGFSKEQRRLGIPKNPWLWTEQQVCQWLLWATNEFSLVNVNFQQFLMNGQELCNLGKERFLELAPDF
VGDILWEHLEQMIKENQEK
>gnl|CDD|260081 cd08544, Reeler, Reeler, the N-terminal domain of reelin, F-spondin, and a variety of other proteins. This domain is found at the N-terminus of F-spondin, a protein attached to the extracellular matrix, which plays roles in neuronal development and vascular remodelling. The F-spondin reeler domain has been reported to bind heparin. The reeler domain is also found at the N-terminus of reelin, an extracellular glycoprotein involved in the development of the brain cortex, and in a variety of other eukaryotic proteins with different domain architectures, including the animal ferric-chelate reductase 1 or stromal cell-derived receptor 2, a member of the cytochrome B561 family, which reduces ferric iron before its transport from the endosome to the cytoplasm. Also included is the insect putative defense protein 1, which is expressed upon bacterial infection and appears to contain a single reeler domain
ACTDMPVPGHGGDPQTTPSPYSITVSGNTYKPGQTYTVTLSGSRPTPFRGFLLQARDASSNEPVGTFQLP
PDSGTKLLTCCPSGNAVTHTNNSPKTSVTVTWKAPSNGSGCVTFRATVVQSYDVFWVDVLSKTLC
>gnl|CDD|260082 cd08545, YcnI_like, Reeler-like domain of YcnI and similar proteins. YcnI is a copper-responsive gene of Bacillus subtilis. It is homologous to an uncharacterized protein from Nocardia farcinica, which shares a conserved three-dimensional structure with cohesins and the reeler domain. Some members in this YcnI_like family have C-terminal domains (DUF461) that may bind copper
ASAHVTVEPKEAAAGSYYKLTFRVPHGCDGAATTKVRVKLPEGVASVKPQPKPGWTVEVTKDKLAKPYDL
HGKTVTEGVTSVTWTAGDLGPDGQFDEFVLSAKLPPDPGGTLYFPAVQTCSDGGVVRWTEVPAADGHELE
HPAPVLTLTAAA
>gnl|CDD|260083 cd08546, cohesin_like, Cohesin domain, interaction parter of dockerin. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. Cohesin modules are phylogenetically distributed into three groups: type I cohesin-dockerin interactions mediate assembly of a range of dockerin-borne enzymes to the complex, while type-II interactions mediate attachment of the cellulosome complex to the bacterial cell wall. Recently discovered type-III cohesins, such as found in the anchoring scaffoldin ScaE, appears to contribute to increased stability of the elaborate cellulosome complex. While the presence of cohesin and dockerin domains in a genome can be indicative of cellulolytic activity, cohesin domains may occur in a wider range of domain architectures, biological systems, and taxonomic lineages
PTVEIKKDTLTEAVGETVTVEVSIEGAPAGFAGTDLTINYDPNVLEIVGIESGDLATAARLLELKNASKD
PDDGIIRVATASSTGQSGGKDGVLAKIVLRVPAGGKTDLTVAYQSRTTNNGLFTDVDGDEEGLWTHTVEV
IQGN
>gnl|CDD|260084 cd08547, Type_II_cohesin, Type II cohesin domain, interaction partner of dockerin. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type II cohesins; their interactions with dockerin mediate attachment of the cellulosome complex to the bacterial cell wall
ASVSLSAPETDVKVGETFTVTVKVNNATNLAGYDFTLSYDPSVLEFVSVTTGSLSGGGGVIANEDAPPGT
VRVAGSSTGGAGGVSGSGTLATLTFKAKAAGTSTISLTDSNTTLSDADGSTIPTFVGGGLEVVQPE
>gnl|CDD|260085 cd08548, Type_I_cohesin_like, Type I cohesin domain, interaction partner of dockerin. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I cohesins; their interactions with dockerin mediate assembly of a range of dockerin-borne enzymes to the complex
VEVIIGNVSAKAGDTVTVPVTLSNVPSKGIGSCDFVLKYDSSVLEVVSVDAGSIVKNPTANFSSNVDEDG
IIKFLFSDSTGGSYLIKTDGVFATLTFKVKSNAAGGTYAITLSSNGAFSDADLKEISVTFINGKV
>gnl|CDD|341479 cd08549, G1PDH_related, Glycerol-1-phosphate dehydrogenase and related proteins. This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids
PRYTIVGDGAINKIEEILKKLNLKRVLIITGKNTKAKYCRFFYDQLKTVCDIVYYDNIDNLEDELKKYTF
YDCVIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASPIVSLRIPGVKKTFMADAPIAIIADTEII
KKSPRRLLSAGIGDLVSNITAVLDWKLAHKEKGEKYSEFAAILSKTSAKELVSYVLKASDLEEYHRVLVK
ALVGSGIAMAIAGSSRPASGSEHLFSHALDKLKEEYLNINVLHGEQVGVGTIIMSYLHEKENKKLSGLHE
RIKMILKKVGAPTTAKQLGIDEDLIIEALTEAHKIRPRRYTLLDGLSREEA
>gnl|CDD|341480 cd08550, GlyDH-like, Glycerol_dehydrogenase-like. This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized
PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVGEKLEKSLEEAGIDYEVEVFGGECTEENIERLA
EKAKEEGADVIIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSP
DLVLVDTDIIAAAPVRYLAAGIGDTLAKWYEARPSSRGGPDDLALQAAVQLAKLAYDLLLEYGVQAVEDV
RQGKVTPALEDVVDAIILLAGLVGSLGGGGCRTAAAHAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEG
RSEEEIEELIEFLRRLGLPVTLEDLGLELTEEELRKIAEYACDPPDMAHMLPFPVTPEMLAEAILAA
>gnl|CDD|341481 cd08551, Fe-ADH, iron-containing alcohol dehydrogenases (Fe-ADH)-like. This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H
PTRIVFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVE
AAAELAREEGADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTP
NAVITDPETGRKMGIVSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALE
AIRLIGKNLRRAVADGSDLEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYV
MEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAM
KSGRLLSNNPRPLTEEDIREIY
>gnl|CDD|350202 cd08553, PIN_Fcf1-like, VapC-like PIN domain of rRNA-processing proteins, Fcf1 (Utp24, YDR339C), Utp23 (YOR004W), and other eukaryotic homologs. Fcf1 (FAF1-copurifying factor 1, also known as Utp24) and Utp23 (U three-associated protein 23) are essential proteins involved in pre-rRNA processing and 40S ribosomal subunit assembly. Components of the small subunit (SSU) processome, Fcf1 and Utp23 are essential nucleolar proteins that are required for processing of the 18S pre-rRNA at sites A0-A2. The Fcf1 protein was reported to interact with Pmc1p (vacuolar Ca2+ ATPase) and Cor1p (core subunit of the ubiquinol-cytochrome c reductase complex). The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. The subfamily of Fcf1- and Utp23-like homologs have three of the four conserved residues found in S. cerevisiae Fcf1. Some members of the superfamily, including S. cerevisiae Utp23, lack several of these key catalytic residues. Mutation of the remaining conserved putative active site residues seen in Utp23 did not interfere with rRNA maturation and cell viability. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
YQVLVDGNFIHAALQKKIDLKEALPKLLGGKVKLFVTRCVLAELRSLGEDFSGALLAAKRFERRRCNHEE
GPVSAAECILDIIGKNNEEHYFVATQDTELRKKLRKIPGVPLLYINRNVLILE
>gnl|CDD|176489 cd08554, Cyt_b561, Eukaryotic cytochrome b(561). Cytochrome b(561) is a family of endosomal or secretory vesicle-specific electron transport proteins. They are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments. This is an exclusively eukaryotic family. Members of the prokaryotic cytochrome b561 family are not deemed homologous
EFNWHPLLMVIGFVFLMGEALLVYRVFRLLTKRALKLLHAILHLLAFVLGLVGLLAVFLFHNAGGIANLY
SLHSWLGLATVLLFLLQFLSGFVLFLLPLLRLSYRSSLLPFHRFFGLAIFVLAIATILLGI
>gnl|CDD|176498 cd08555, PI-PLCc_GDPD_SF, Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases superfamily. The PI-PLC-like phosphodiesterases superfamily represents the catalytic domains of bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11), glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria, as well as their uncharacterized homologs found in organisms ranging from bacteria and archaea to metazoans, plants, and fungi. PI-PLCs are ubiquitous enzymes hydrolyzing the membrane lipid phosphoinositides to yield two important second messengers, inositol phosphates and diacylglycerol (DAG). GP-GDEs play essential roles in glycerol metabolism and catalyze the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols that are major sources of carbon and phosphate. Both, PI-PLCs and GP-GDEs, can hydrolyze the 3'-5' phosphodiester bonds in different substrates, and utilize a similar mechanism of general base and acid catalysis with conserved histidine residues, which consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81, glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs). The residues essential for enzyme activities and metal binding are not conserved in these sequence homologs, which might suggest that the function of catalytic domains in these proteins might be distinct from those in typical PLC-like phosphodiesterases
VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGILPPTLEEVLELIA
DYLKNPDYTIILSLEIKQDSPEYDEFLAKVLKELRVYFDYDLRGKVVLSSFNALGVDYYNFSSKLIKDTE
LIASANKLGLLSRIWTVNDNNEIINKFLNLGVDGLITDF
>gnl|CDD|176499 cd08556, GDPD, Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and similar proteins. The typical glycerophosphodiester phosphodiesterase domain (GDPD) consists of a TIM barrel and a small insertion domain named the GDPD-insertion (GDPD-I) domain, which is specific for GDPD proteins. This family corresponds to both typical GDPD domain and GDPD-like domain which lacks the GDPD-I region. Members in this family mainly consist of a large family of prokaryotic and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), and a number of uncharacterized homologs. Sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria are also included in this family. GDPD plays an essential role in glycerol metabolism and catalyzes the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols are major sources of carbon and phosphate. Its catalytic mechanism is based on the metal ion-dependent acid-base reaction, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). Both, GDPD related proteins and PI-PLCs, belong to the superfamily of PI-PLC-like phosphodiesterases
IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHDIPTLEEVLELVKGGVGLNIELKE
PTRYPGLEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVPTGLLVDKPPLDPLLAELARALGADA
VNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITDD
>gnl|CDD|176500 cd08557, PI-PLCc_bacteria_like, Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar proteins. This subfamily corresponds to the catalytic domain present in bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and their sequence homologs found in eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Its catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. Eukaryotic homologs in this family are named as phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). They are distinct from the typical eukaryotic phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11), which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, which is closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs. This family also includes a distinctly different type of eukaryotic PLC, glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC), an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG), releasing dimyristyl glycerol (DMG), which may facilitate the evasion of the protozoan to the host's immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs, but not mammalian PI-PLCs
PALLDDLPLSQLSIPGTHNSYAYTIDGNSPIVSKWSKTQDLSITDQLDAGVRYLDLRVAYDPDDGDLYVC
HGLFLLNGQTLEDVLNEVKDFLDAHPSEVVILDLEHEYGGDNGEDHDELDALLRDVLGDPLYRPPVRAGG
WPTLGELRAGKRVLLFYFGGDDSSGGYDWGSLNIQDPYANGTDKLESLKAFLNSALASPRSADFFYVNQA
SLTPGRITIAVAGSLYTVATRANPALYEWLKEDGSGASGPNIVATDFVDVGDLIDAVIRLN
>gnl|CDD|176501 cd08558, PI-PLCc_eukaryota, Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins. This family corresponds to the catalytic domain present in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) and similar proteins. The higher eukaryotic PI-PLCs play a critical role in most signal transduction pathways, controlling numerous cellular events such as cell growth, proliferation, excitation and secretion. They strictly require Ca2+ for the catalytic activity. They display a clear preference towards the hydrolysis of the more highly phosphorylated membrane phospholipids PI-analogues, phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol-4-phosphate (PIP), to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. The eukaryotic PI-PLCs have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains, such as the pleckstrin homology (PH) domain, EF-hand motif, and C2 domain. The catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a linker region. The catalytic mechanism of eukaryotic PI-PLCs is based on general base and acid catalysis utilizing two well conserved histidines and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. The mammalian PI-PLCs consist of 13 isozymes, which are classified into six-subfamilies, PI-PLC-delta (1,3 and 4), -beta(1-4), -gamma(1,2), -epsilon, -zeta, and -eta (1,2). Ca2+ is required for the activation of all forms of mammalian PI-PLCs, and the concentration of calcium influences substrate specificity. This family also includes metazoan phospholipase C related but catalytically inactive proteins (PRIP), which belong to a group of novel inositol trisphosphate binding proteins. Due to the replacement of critical catalytic residues, PRIP does not have PLC enzymatic activity
YQDMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDGPDGEPVVYHGHTLTSKI
LFKDVIEAIKEYAFVTSPYPVILSLENHCSLEQQKKMAQILKEIFGDKLLTPPLDENPVQLPSPEQLKGK
ILIKGKKYHMSSFSETKALKLLKESPEEFVKYNKRQLSRVYPKGTRVDSSNYNPQPFWNAGCQMVALNYQ
TPDLPMQLNQGKFEQN
>gnl|CDD|176502 cd08559, GDPD_periplasmic_GlpQ_like, Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in bacterial and eukaryotic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ. GP-GDEs are involved in glycerol metabolism and catalyze the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. In E. coli, there are two major G3P uptake systems: Glp and Ugp, which contain genes coding for two different GP-GDEs. GlpQ gene from the glp operon codes for a periplasmic phosphodiesterase GlpQ. GlpQ is a dimeric enzyme that hydrolyzes periplasmic glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), to the corresponding alcohols and G3P, which is subsequently transported into the cell through the GlpT transport system. Ca2+ is required for GlpQ enzymatic activity. This subfamily also includes some GP-GDEs in higher plants and their eukaryotic homologs, which show very high sequence similarities with bacterial periplasmic GP-GDEs
PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVAEHFPFRGRKDT
GYFVIDFTLAELKTLRAGSWFNQRYPERAPSYYGGFKIPTLEEVIELAQGLNKSTGRNVGIYPETKHPTF
HKQEGPDIEEKLLEVLKKYGYTGKNDPVFIQSFEPESLKRLRNETPDIPLVQLIDYGDWAETDKKYTYAW
LTTDAGLKEIAKYADGIGPWKSLIIPEDSNGLLVPTDLVKDAHKAGLLVHPYTFRNENLFLAPDFKQDMD
ALYNAAGVDGVFTDFP
>gnl|CDD|176503 cd08560, GDPD_EcGlpQ_like_1, Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic phosphodiesterase (GlpQ) include uncharacterized proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and their hypothetical homologs. Members in this subfamily show high sequence similarity to Escherichia coli periplasmic phosphodiesterase GlpQ, which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols
LKDKLLSCAEKPFRKTDFSIGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSQCDLH
TTTNILAIPELAAKCTQPFTPANATKPASAECCTSDITLAEFKSLCGKMDASNPSATTPEEYQNGTPDWR
TDLYATCGTLMTHKESIALFKSLGVKMTPELKSPSVPMPFDGNYTQEDYAQQMIDEYKEAGVPPSRVWPQ
SFNLDDIFYWIKNEPDFGRQAVYLDDRDDTADFPATWSPSMDELKARGVNIIAPPIWMLVDPDENGKIVP
SEYAKAAKAAGLDIITWTLERSGPLASGGGWYYQTIEDVINNDGDMYNVLDVLARDVGILGIFSDWPATV
TYYANC
>gnl|CDD|176504 cd08561, GDPD_cytoplasmic_ScUgpQ2_like, Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic phosphodiesterases UgpQ2 and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized cytoplasmic phosphodiesterases which predominantly exist in bacteria. The prototype of this family is a putative cytoplasmic phosphodiesterase encoded by gene ulpQ2 (SCO1419) in the Streptomyces coelicolor genome. It is distantly related to the Escherichia coli cytoplasmic phosphodiesterases UgpQ that catalyzes the hydrolysis of glycerophosphodiesters at the inner side of the cytoplasmic membrane to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols
VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRR
LDAGYHFTDDGGRTYPYRGQGIRIPTLEELFEAFPDVRLNIEIKDDGPAAAAALADLIERYGAQDRVLVA
SFSDRVLRRFRRLCPRVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAHA
AGLEVHVWTVNDPAEMRRLLDLGVDGIITDRPDLLLEVL
>gnl|CDD|176505 cd08562, GDPD_EcUgpQ_like, Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic glycerophosphodiester phosphodiesterase UgpQ and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Escherichia coli cytosolic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46), UgpQ, and similar proteins. GP-GDE plays an essential role in the metabolic pathway of E. coli. It catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. E. coli possesses two major G3P uptake systems: Glp and Ugp, which contain genes coding for two distinct GP-GDEs. UgpQ gene from the E. coli ugp operon codes for a cytosolic phosphodiesterase GlpQ, which is the prototype of this family. Various glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), can only be hydrolyzed by UgpQ during transport at the inner side of the cytoplasmic membrane to alcohols and G3P, which is a source of phosphate. In contrast to Ca2+-dependent periplasmic phosphodiesterase GlpQ, cytosolic phosphodiesterase UgpQ requires divalent cations, such as Mg2+, Co2+, or Mn2+, for its enzyme activity
IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQ
LDAGSWFSPEFAGEPIPTLADVLELARELGLGLNLEIKPDPGDEALTARVVAAALRELWPHASKLLLSSF
SLEALRAARRAAPELPLGLLFDTLPADWLELLAALGAVSIHLNYRGLTEEQVKALKDAGYKLLVYTVNDP
ARAAELLEWGVDAIFTDRP
>gnl|CDD|176506 cd08563, GDPD_TtGDE_like, Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermoanaerobacter tengcongensis glycerophosphodiester phosphodiesterase (TtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Despite the fact that most of GDPD family members exist as the monomer, TtGDE can function as a dimeric unit. Its catalytic mechanism is based on the general base-acid catalysis, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). A divalent metal cation is required for the enzyme activity of TtGDE
TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEEL
KKLDAGSWFDEKFTGEKIPTLEEVLDLLKDKDLLLNIEIKTDVIHYPGIEKKVLELVKEYNLEDRVIFSS
FNHESLKRLKKLDPKIKLALLYETGLQDPKDYAKKIGADSLHPDFKLLTEEVVEELKKRGIPVRLWTVNE
EEDMKRLKDLGVDGIITNYP
>gnl|CDD|176507 cd08564, GDPD_GsGDE_like, Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria glycerophosphodiester phosphodiesterase and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative Galdieria sulphuraria glycerophosphodiester phosphodiesterase (GsGDE, EC 3.1.4.46) and its uncharacterized eukaryotic homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols
MVRPIIVGHRGAGCSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHGTEDDTNPDTSIQLDDS
GFKNINDLSLDEITRLHFKQLFDEKPCGADEIKGEKIPTLEDVLVTFKDKLKYNIELKGREVGLGERVLN
LVEKYGMILQVHFSSFLHYDRLDLLKALRPNKLNVPIALLFNEVKSPSPLDFLEQAKYYNATWVNFSYDF
WTEEFVKKAHENGLKVMTYFDEPVNDNEEDYKVYLELGVDCICPNDPVLLVNFLK
>gnl|CDD|176508 cd08565, GDPD_pAtGDE_like, Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (pAtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols
IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKA
LRLRDSFGEKIPTLEEVLALFAPSGLELHVEIKTDADGTPYPGAAALAAATLRRHGLLERSVLTSFDPAV
LTEVRKHPGVRTLGSVDEDMLERLGGELPFLTATALKAHIVAVEQSLLAATWELVRAAVPGLRLGVWTVN
DDSLIRYWLACGVRQLTTDRPDLAL
>gnl|CDD|176509 cd08566, GDPD_AtGDE_like, Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (AtGDE, EC 3.1.4.46) and its uncharacterized eukaryotic homolgoues. Members in this family shows high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. AtGDE exists as a hexamer that is a trimer of dimers, which is unique among current known GDPD family members. However, it remains unclear if the hexamer plays a physiological role in AtGDE enzymatic function
LVVAHRGGWGAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEI
RKLRLKDGDGEVTDEKVPTLEEALAWAKGKILLNLDLKDADLDEVIALVKKHGALDQVIFKSYSEEQAKE
LRALAPEVMLMPIVRDAEDLDEEEARAIDALNLLAFEITFDDLDLPPLFDELLRALGIRVWVNTLGDDDT
AGLDRALSDPREVWGELVDAGVDVIQTDRP
>gnl|CDD|176510 cd08567, GDPD_SpGDE_like, Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi glycerophosphodiester phosphodiesterase and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and similar proteins. The prototype of this CD is a putative GP-GDE from Silicibacter pomeroyi (SpGDE). It shows high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols
FDLQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDITRDPDGAWLPYEGP
ALYELTLAEIKQLDVGEKRPGSDYAKLFPEQIPVPGTRIPTLEEVFALVEKYGNQKVRFNIETKSDPDRD
ILHPPPEEFVDAVLAVIRKAGLEDRVVLQSFDWRTLQEVRRLAPDIPTVALTEETTLGNLPRAAKKLGAD
IWSPYFTLVTKELVDEAHALGLKVVPWTVNDPEDMARLIDLGVDGIITDYPDL
>gnl|CDD|176511 cd08568, GDPD_TmGDE_like, Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermotoga maritime glycerophosphodiester phosphodiesterase (TmGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. TmGDE exists as a monomer that might be the biologically relevant form
IILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELK
KLHPGGELIPTLEEVFRALPNDAIINVEIKDIDAVEPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPD
AKVGLLIGEEEEGFSIPELHEKLKLYSLHVPIDAIGYIGFEKFVELLRLLRKLGLKIVLWTVNDPELVPK
LKGLVDGVITDDVEKI
>gnl|CDD|176512 cd08570, GDPD_YPL206cp_fungi, Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL206cp and uncharacterized hypothetical homologs existing in fungi. The product of S. cerevisiae ORF YPL206c (PGC1), YPL206cp (Pgc1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL206cp is an integral membrane protein with a single GDPD domain following by a short hydrophobic C-terminal tail that may function as a membrane anchor. This protein plays an essential role in the regulation of the cardiolipin (CL) biosynthetic pathway in yeast by removing the excess phosphatidylglycerol (PG) content of membranes via a phospholipase C-type degradation mechanism. YPL206cp has been characterized as a PG-specific phospholipase C that selectively catalyzes the cleavage of PG, not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate. Members in this family are distantly related to S. cerevisiae YPL110cp, which selectively hydrolyzes glycerophosphocholine (GPC), not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate, and has been characterized as a cytoplasmic GPC-specific phosphodiesterase
VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDSTWDELS
HLRTIEEPHQPMPTLKDVLEWLVEHELPDVKLMLDIKRDNDPEILFKLIAEMLAVKPDLDFWRERIILGL
WHLDFLKYGKEVLPGFPVFHIGFSLDYARHFLNYSEKLVGISMHFVSLWGPFGQAFLPELKKNGKKVFVW
TVNTEEDMRYAIRLGVDGVITDDP
>gnl|CDD|176513 cd08571, GDPD_SHV3_plant, Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase (GDPD) domain present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play an important role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens
PLVIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPKRKKTYV
VEGQSTSGIFSFDLTWAEIQTLKPIISNPFSVLFRNPRNDNAGKILTLEDFLTLAKPKSLSGVWINVENA
AFLAEHKGLLSVDAVLTSLSKAGYDQTAKKVYISSPDSSVLKSFKKRVGTKLVFRVLDVDDTEPDTLLSN
LTEIKKFASGVLVPKSYIWPVDSDSFLTPQTSVVQDAHKAGLEVYVSGFANEFVSLAYDYSADPTLEILS
FVGNGNSVDGVITDFPATAARA
>gnl|CDD|176514 cd08572, GDPD_GDE5_like, Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins. GDE5 is widely expressed in mammalian tissues, with highest expression in spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols
LVIGHRGLGKNYASGSLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSKTGSD
EGELIEVPIHDLTLEQLKELGLQHISALKRKALTRKAKGPKPNPWGMDEHDPFPTLQEVLEQVPKDLGFN
IEIKYPQLLEDGEGELTPYFERNAFVDTILAVVFEHAGGRRIIFSSFDPDICIMLRLKQNKYPVLFLTNG
GTNEVEHMDPRRRSLQAAVNFALAEGLLGVVLHAEDLLKNPSLISLVKALGLVLFTYGDDNNDPENVKKQ
KELGVDGVIYDRV
>gnl|CDD|176515 cd08573, GDPD_GDE1, Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE1 and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE1 (also known as MIR16, membrane interacting protein of RGS16) and their metazoan homologs. GDE1 is widely expressed in mammalian tissues, including the heart, brain, liver, and kidney. It shows sequence homology to bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. GDE1 has been characterized as GPI-GDE (EC 3.1.4.44) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate glycerol phosphate and inositol. It functions as an integral membrane-bound glycoprotein interacting with regulator of G protein signaling protein RGS16, and is modulated by G protein-coupled receptor (GPCR) signaling. In addition, GDE1 may interact with PRA1 domain family, member 2 (PRAF2, also known as JM4), which is an interacting protein of the G protein-coupled chemokine receptor CCR5. The catalytic activity, which is dependent on the integrity of the GDPD domain, is required for GDE1 cellular function
IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRK
LNAAAKHRLSSRFPGEKIPTLEEAVKECLENNLRMIFDVKSNSSKLVDALKNLFKKYPGLYDKAIVCSFN
PIVIYKVRKADPKILTGLTWRPWFLSYTDDEGGPRRKSGWKHFLYSMLDVILEWSLHSWLPYFLGVSALL
IHKDDISSAYVRYWRARGIRVIAWTVNTPTEKQYFAKTLNVPYITDSL
>gnl|CDD|176516 cd08574, GDPD_GDE_2_3_6, Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2, GDE3, GDE6-like proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase domain-containing protein subtype 5 (GDE2), subtype 2 (GDE3), subtype 1 (GDE6), and their eukaryotic homologs. Mammalian GDE2, GDE3, and GDE6 show very high sequence similarity to each other and have been classified into the same family. Although they are all transmembrane proteins, based on different pattern of tissue distribution, these enzymes might display diverse cellular functions. Mammalian GDE2 is primarily expressed in mature neurons. It selectively hydrolyzes glycerophosphocholine (GPC) and mainly functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE3 is specifically expressed in bone tissues and spleen. It selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate inositol 1-phosphate (Ins1P) and glycerol and functions as an inducer of osteoblast differentiation. Mammalian GDE6 is predominantly expressed in the spermatocytes of testis, and its specific physiological function has not been elucidated yet
KPALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVADVFPERAHER
ASMFTWTDLQQLNAGQWFLKDDPFWTASSLSESDREEAGNQSIPSLAELLRLAKKHNKSVIFDLRRPPPN
HPYYQSYVNITLDTILASGIPQHQVFWLPDEYRALVRKVAPGFQQVSGRKLPVESLRENGISRLNLEYSQ
LSAQEIREYSKANISVNLYVVNEPWLYSLLWCSGVQSVTTNA
>gnl|CDD|176517 cd08575, GDPD_GDE4_like, Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4-like proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE4 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1)) and similar proteins. Mammalian GDE4 is a transmembrane protein whose cellular function is not elucidated. It is expressed widely, including in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. It is also expressed in the growth cones in neuroblastoma Neuro2a cells, which suggests mammalian GDE4 may play some distinct role from other members of mammalian GDEs family. Also included in this subfamily are uncharacterized mammalian glycerophosphodiester phosphodiesterase domain-containing protein 3 (GDPD3) and similar proteins which display very high sequence homology to mammalian GDE4
PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAEL
PPLDAGYGYTFDGGKTGYPRGGGDGRIPTLEEVFKAFPDTPINIDIKSPDAEELIAAVLDLLEKYKREDR
TVWGSTNPEYLRALHPENPNLFESFSMTRCLLLYLALGYTGLLPFVPIKESFFEIPRPVIVLETFTLGEG
ASIVAALLWWPNLFDHLRKRGIQVYLWVLNDEEDFEEAFDLGADGVMTDSPTKL
>gnl|CDD|176518 cd08576, GDPD_like_SMaseD_PLD, Glycerophosphodiester phosphodiesterase-like domain of spider venom sphingomyelinases D, bacterial phospholipase D, and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase-like domain (GDPD-like) present in sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.4) from spider venom, the Corynebacterium pseudotuberculosis Phospholipase D (PLD)-like protein from pathogenic bacteria, and the Ajellomyces capsulatus H143 PLD-like protein from ascomycetes. Spider SMases D and bacterial PLD proteins catalyze the Mg2+-dependent hydrolysis of sphingomyelin producing choline and ceramide 1-phosphate (C1P), which possess a number of biological functions, such as regulating cell proliferation and apoptosis, participating in inflammatory responses, and playing a key role in phagocytosis. In the presence of Mg2+, SMases D can function as lysophospholipase D and hydrolyze lysophosphatidylcholine (LPC) to choline and lysophosphatidic acid (LPA), which is a multifunctional phospholipid involved in platelet aggregation, endothelial hyperpermeability, and pro-inflammatory responses. Loxosceles spider venoms' SMases D are the principal toxins responsible for dermonecrosis and complement dependent haemolysis induced by spider venom. Due to amino acid substitutions at the entrance to the active-site pocket, some members lack activity. The typical GDPD domain consists of a TIM barrel and a small insertion domain named as the GDPD-insertion (GDPD-I) domain, which is specific for GDPD proteins. Although proteins in this family contain a non-typical GDPD domain which lacks the GDPD-I, their catalytic mechanisms are based on Mg2+-dependent acid-base reactions similar to GDPD proteins. They might be divergent members of the GDPD family. Moreover, this family does not belong to phospholipase D (PLD) superfamily, since it lacks the conserved HKD sequence motif that characterizes the catalytic center of the PLD superfamily. It belongs to the superfamily of PLC-like phosphodiesterases
YAIAHMVNDLEGVDDALDHGANAIEIDVTFWSNGTGWWADHDVPCDCFRGCTAREMFDEILDYRRNGTTP
GFRENLIFVWLDLKNPDLCGECSINAGRDLARKLLEPYWNGGSGARALYGFSIPSITDSRFFKGIRDRLN
SEEAVSGLLDKVGKDFSGNEDLEDIRRVYDYGGDGHIWQSDGITNCLEKYRTCARLREAIKKRDTPGYLG
KVYGWTSDKGSSVRKLLRLGVDGIITNYPKRIIDVLKESEFSGTHRMATYDDNPW
>gnl|CDD|176519 cd08577, PI-PLCc_GDPD_SF_unchar3, Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases. This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues
INAHSHNDYWRKRPLYDALSAGFGSIEADVWLVNGDLLVAHDEVDLSPARTLESLYLDPLLEILDQNNGQ
AYNDPEQPLQLLIDIKTDGESTYPALEEVLKPYIDIGYLSYYDKLVPGPVTVVITGNRPKEEVKSQYPRY
IFFDGRLDEDLPDEQLARLSPMISASFAKFSKWNGKGDTPEDEKEKLKSIIDKAHARGKKVRFWGTPDRP
NVWKTLMELGVDLLNTDD
>gnl|CDD|176520 cd08578, GDPD_NUC-2_fungi, Putative glycerophosphodiester phosphodiesterase domain of ankyrin repeat protein NUC-2 and similar proteins. This subfamily corresponds to a putative glycerophosphodiester phosphodiesterase domain (GDPD) present in Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81. Some uncharacterized NUC-2 sequence homologs are also included in this family. NUC-2 plays an important role in the phosphate-regulated signal transduction pathway in Neurospora crassa. It shows high similarity to a cyclin-dependent kinase inhibitory protein PHO81, which is part of the phosphate regulatory cascade in S. cerevisiae. Both NUC-2 and PHO81 have multi-domain architecture, including an SPX N-terminal domain following by several ankyrin repeats and a putative C-terminal GDPD domain with unknown function. Although the putative GDPD domain displays sequence homology to that of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), the residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in members of this family, which suggests the function of putative GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs
ETYWKSTSGSDTQANKDGNSFVTASSLSGEYLRVKVCVLKDGTPVVAPEWFVPVGGIKLLVSDLTAEQLE
SILDYSLDDLNSEISDMVDLKRLLSSRVVSLETLLELLPPSIQLDIQVLFPTAAEIASIPVKGSPLVDLN
KFIDTVLLVVFDHARYLRHTPGSTRSIVFSSCNPEVCTILNWKQPNFPVFFAMNGLVRNNDTLSFDTPHH
LDSLAVDPQKLNEADPRSRSIKEAVRFAKNNNLLGLILPYSLLNIVPQLVESIKSRGLLLIASGEPESLI
EVAEAGDGINGVVTEDELLF
>gnl|CDD|176521 cd08579, GDPD_memb_like, Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial glycerophosphodiester phosphodiesterases. In addition to a C-terminal GDPD domain, most members in this family have an N-terminus that functions as a membrane anchor
IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKK
LTIGENGHGAKIPSLDEYLALAKGLKQKLLIELKPHGHDSPDLVEKFVKLYKQNLIENQHQVHSLDYRVI
EKVKKLDPKIKTGYILPFNIGNLPKTNVDFYSIEYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAM
GVDGIITDYP
>gnl|CDD|176522 cd08580, GDPD_Rv2277c_like, Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial protein Rv2277c and similar proteins. Members in this subfamily are bacterial homologous of mammalian GDE4, a transmembrane protein whose cellular function has not yet been elucidated
PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQL
ATLNAGYNFKPEGGYPYRGKPVGIPTLEQVLRAFPDTPFILDMKSLPADPQAKAVARVLERENAWSRVRI
YSTNADYQDALAPYPQARLFESRDVTRTRLANVAMAHQCDLPPDSGAWAGFELRRKVTVVETFTLGEGRS
PVQATLWTPAAVDCFRRNSKVKIVLFGINTADDYRLAKCLGADAVMVDSPAAM
>gnl|CDD|176523 cd08581, GDPD_like_1, Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity to Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols
LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDS
LRVAEPARFGSRFAGEPLPSLAAVVQWLAQHPQVTLFVEIKTESLDRFGLERVVDKVLRALPAVAAQRVL
ISFDYDLLALAKQQGGPRTGWVLPDWDDASLAEADELQPDYLFCDKNLLPDTGDLWAGTWKWVIYEVNEP
AEALALAARGVALIETDNI
>gnl|CDD|176524 cd08582, GDPD_like_2, Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity to Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols
VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRK
LDIGSWKGESYKGEKVPTLEEYLAIVPKYGKKLFIEIKHPRRGPEAEEELLKLLKESGLLPEQIVIISFD
AEALKRVRELAPTLETLWLRNYKSPKEDPRPLAKSGGAAGLDLSYEKKLNPAFIKALRDAGLKLNVWTVD
DAEDAKRLIELGVDSITTNRPGR
>gnl|CDD|176525 cd08583, PI-PLCc_GDPD_SF_unchar1, Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases. This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues
LIAHAMGGIDGKTYTNSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHSWDESLLKQLGLPTSKNTKPLS
YEEFKSKKIYGKYTPMDFKDVIDLLKKYPDVYIVTDTKQDDDNDIKKLYEYIVKEAKEVDPDLLDRVIPQ
IYNEEMYEAIMSIYPFKSVIYTLYRQDSIRLDEIIAFCYENGIKAVTISKNYVNDKLIEKLNKAGIYVYV
YTINDLKDAQEYKKLGVYGIYTDFLTE
>gnl|CDD|176526 cd08584, PI-PLCc_GDPD_SF_unchar2, Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases. This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues
IIAHRGNTITALKRTFENFGVETDIRDYGGQLVISHDPFVKNGELLEDWLKEYNHGTLILNIKAEGLELR
LKKLLAEYGITNYFFLDMSVPDIIKYLENGEKRTATRVSEYEPIPTALSLYEKADWVWIDSFTSLWLDND
LILKLLKAGKKICLVSPELHGRDHLAEWEAKQYIEFLKENFDALCTKVPDLW
>gnl|CDD|176527 cd08585, GDPD_like_3, Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity with Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols
WLKDRPIAHRGLHDRDAGIPENSLSAFRAAAEAGYGIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEEL
TAAELRALRLLGTDEHIPTLDEVLELVAGRVPLLIELKSCGGGDGGLERRVLAALKDYKGPAAIMSFDPR
VVRWFRKLAPGIPRGQLSEGSNDEADPAFWNEALLSALFSNLLTRPDFIAYHLDDLPNPFVTLARALLGM
PVIVWTVRTEEDIARLKQYADNIIFEG
>gnl|CDD|176528 cd08586, PI-PLCc_BcPLC_like, Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar proteins. This subfamily corresponds to the catalytic domain present in Bacillus cereus phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and its sequence homologs found in bacteria and eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Their catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This family also includes some uncharacterized eukaryotic homologs, which contains a single TIM-barrel type catalytic domain, X domain. They are similar to bacterial PI-PLCs, and distinct from typical eukaryotic PI-PLCs, which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains, and strictly require Ca2+ for their catalytic activities. The prototype of this family is Bacillus cereus PI-PLC, which has a moderate thermal stability and is active as a monomer
MSALPDDTPLSELSIPGTHDSGALHGGLSSSVQCQDWSIAEQLNAGIRFLDIRLRLIDNNDLAIHHGPFY
QGLTFGDVLNECYSFLDANPSETIIMSLKQEGSGDGNTDSFAEIFKEYLDNYPSYFYYTESKIPTLGEVR
GKIVLLRRFDGDDEGGGYNNGGPDDTLFTINIDNGTLYIQDFYEVSTAEDIEKKWNAIKAHLDKAASNSS
SSNKLYINFTSGSGGGFPLGGGPGKYAEGINPLLYNYLKENNGRGRLGIVIMDFPGADWDLIQLIIGTN
>gnl|CDD|176529 cd08587, PI-PLCXDc_like, Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and similar proteins. This family corresponds to the catalytic domain present in phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD) which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs mainly found in eukaryota. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs and their bacterial homologs contain a single TIM-barrel type catalytic domain, X domain, which is more closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs
PSAIGDLPLRDLVIPGSHDSGMYTINGDSPVGPDQPEFGKIAKGIVRKWSVTQSLSIYDQLEAGIRYFDL
RVAYKPDSENKLYFVHGLYSGEPVDEVLEDVNDFLDEHPKEVVILDFNHFYGMDDKSPEDHEKLVELLED
IFGDKLCPRDSDLLDVTLADLWESGKRVIVFYDDDLASEGPYLWPSPYIPDPWANTDDPQKLIDFLENKL
KERRRPDKFFVLQWILTPQASTIVLGLFSGLLKKLALRANPALLEWLREQLPGQDGPNIILNDFVDLGEF
IDLAIALN
>gnl|CDD|176530 cd08588, PI-PLCc_At5g67130_like, Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its uncharacterized homologs. This subfamily corresponds to the catalytic domain present in Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its uncharacterized homologs. Members in this family show high sequence similarity to bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), which participates in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG)
CNGSPALCDRTYDEYTFLTTHNSFANSEDAFFLAPNQEDDITKQLDDGVRGLMLDIHDANGGLRLCHSVC
GLGDGGPLSDVLREVVDFLDANPNEVVTLFLEDYVSPGPLLRSKLFRVAGLTDLVYVPDAMPWAGSDWPT
LGEMIDANKRLLVFTDNEDVSTEPPGVMYQFDYTVENPFSVGGDDDWSCTVRRGSGPLSRIAPGFRRLFL
MNHFRDVPVPITAANDNNGDGLLLRHLNNCRPAAGGRKPNFVAVDFYNIGDAFEAVDELN
>gnl|CDD|176531 cd08589, PI-PLCc_SaPLC1_like, Catalytic domain of Streptomyces antibioticus phosphatidylinositol-specific phospholipase C1-like proteins. This subfamily corresponds to the catalytic domain present in Streptomyces antibioticus phosphatidylinositol-specific phospholipase C1 (SaPLC1) and similar proteins. The typical bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) catalyzes Ca2+-independent hydrolysis of the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). The catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. In contrast, SaPLC1 is the first known natural Ca2+-dependent bacterial PI-PLC. It is more closely related to the eukaryotic PI-PLCs rather than the typical bacterial PI-PLCs. It participates in PI metabolism to generate myo-inositol-1-phosphate and myo-inositol-1:2-cyclic phosphate simultaneously. SaPLC1 and other members in this subfamily have two Ca2+-chelating amino acid substitutions which convert them from metal-independent enzymes to metal-dependent bacterial PI-PLC. Additionally, SaPLC1 active site utilizes a mechanism of amino acid juxtaposition, swapping amino acid positions, to adapt a calcium binding pocket and maintain more ideal active site geometry to support efficient catalysis
AAAADALRLNQIQVVGTHNSYHKEIDPAELALLAVNPPLAEGLDYSHPPLADQLDSGVRQLELDVWADPE
GGRYAHPLGLAPDDAAVMKKPGWKVSHIPDLDNRNNCVTLEDCLDDVRAWSDAHPGHVPIFIKLELKDGF
SALPGGGVPFTARGPAQLDALIRSVLGDDKLITPDDVRGGAATLDEAVRAGGWPTLSALRGKVLFVLDPG
EEGNPRDLYRTDAPSLRGRAAFGNSEPAQPDAAFPAVNNASAGDPRIRYLVKRGWFVRTRADADTYEART
NDTSRRDAALASGAQIVSTDYPNVAPAIRDYAVPLPGGAAARCN
>gnl|CDD|176532 cd08590, PI-PLCc_Rv2075c_like, Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins. This subfamily corresponds to the catalytic domain present in uncharacterized Mycobacterium tuberculosis Rv2075c and its homologs. Members in this family are more closely related to the Streptomyces antibioticus phosphatidylinositol-specific phospholipase C1(SaPLC1)-like proteins rather than the typical bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). In contrast, SaPLC1-like proteins have two Ca2+-chelating amino acid substitutions which convert them to metal-dependent bacterial PI-PLC. Rv2075c and its homologs have the same amino acid substitutions as well, which might suggest they have metal-dependent PI-PLC activity
QRNLDSNAPLCQAQILGTHNSYNSRAYGYGNRYHGVRYLDPNQELSITDQLDLGARFLELDVHWTTGDLR
LCHGGDHGYLGVCSSEDRLFEDGLNEIADWLNANPDEVVILYLEDHGDGGKDDELNALLNDAFGDLLYTP
SDCDDLQGLPNWPTKEDMLNSGKQVVLATGGGCSGAQGMYNRKEFADTQPSNFRPYPECAFAMGNNTSLV
RVYEDSTNYSSAAGDPGGPFKNGNILNAMDYLKCGVNLVGLDQLNPGRIAAAVWSWA
>gnl|CDD|176533 cd08591, PI-PLCc_beta, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta. This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are four PLC-beta isozymes (1-4). They are activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. The beta-gamma subunits of heterotrimeric G proteins are known to activate the PLC-beta2 and -beta3 isozymes only. Aside from four PLC-beta isozymes identified in mammals, some eukaryotic PLC-beta homologs have been classified into this subfamily, such as NorpA and PLC-21 from Drosophila and PLC-beta from turkey, Xenopus, sponge, and hydra
YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCT
EILFKDVIEAIAETAFKTSEYPVILSFENHCSSKQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSP
NDLKRKILIKNKKLSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSR
IYPKGTRVDSSNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN
>gnl|CDD|176534 cd08592, PI-PLCc_gamma, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma. This family corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-gamma isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-gamma represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C2 domain.The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unique to PI-PLC-gamma, a second PH domain, two SH2 (Src homology 2) regions, and one SH3 (Src homology 3) region is present within this linker region. There are two PI-PLC-gamma isozymes (1-2). They are activated by receptor and non-receptor tyrosine kinases due to the presence of two SH2 and a single SH3 domain within the linker region. Aside from the two PI-PLC-gamma isozymes identified in mammals, some eukaryotic PI-PLC-gamma homologs have been classified with this subfamily
PQDMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDGPDGMPIIYHGHTLTSKI
KFMDVLKTIKEHAFVTSEYPVILSIENHCSLPQQRNMAQAFKEVFGDMLLTQPVDRNADQLPSPNQLKRK
IIIKHKKLFYEMSSFPETKAEKYLNRQKGKIFLKYNRRQLSRVYPKGQRVDSSNYDPVPMWNCGSQMVAL
NFQTPDKPMQLNQALFMLN
>gnl|CDD|176535 cd08593, PI-PLCc_delta, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta. This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This CD corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. Aside from three PI-PLC-delta isozymes identified in mammals, some eukaryotic PI-PLC-delta homologs have been classified to this CD
YQDMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWDGPDGEPIIYHGHTLTSKI
LFKDVIQAIREYAFKVSPYPVILSLENHCSVEQQKVMAQHLKSILGDKLLTQPLDGVLTALPSPEELKGK
ILVKGKKLKLAKELSDLVIYCKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFVRHNKRQLSR
IYPAGLRTDSSNYDPQEMWNVGCQIVALNFQTPGEEMDLNDGLFRQN
>gnl|CDD|176536 cd08594, PI-PLCc_eta, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta. This family corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-eta isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-eta represents a class of neuron-speific PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are two PI-PLC-eta isozymes (1-2), both neuron-specific enzymes. They function as calcium sensors that are activated by small increases in intracellular calcium concentrations. The PI-PLC-eta isozymes are also activated through GPCR stimulation. Aside from the PI-PLC-eta isozymes identified in mammals, their eukaryotic homologs are also present in this family
NQDMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDGPDGEPVVHHGYTLTSKI
LFRDVIETINKYAFIKNEYPVILSIENHCSVQQQKKMAQYLKEILGDKLDLSSVISGDSKQLPSPQSLKG
KILIKGKKWQVSSFSETRAHQIVQQKAAQFLRFNQRQLSRIYPSAYRIDSSNFNPQPYWNAGCQLVALNY
QTEGRMLQLNRAKFRAN
>gnl|CDD|176537 cd08595, PI-PLCc_zeta, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta. This family corresponds to the catalytic domain presenting in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-zeta isozyme. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-zeta represents a class of sperm-specific PI-PLC that has an N-terminal EF-hand domain, a PLC catalytic core domain, and a C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There is one PLC-zeta isozyme (1). PLC-zeta plays a fundamental role in vertebrate fertilization by initiating intracellular calcium oscillations that trigger the embryo development. However, the mechanism of its activation still remains unclear. Aside from PI-PLC-zeta identified in mammals, its eukaryotic homologs have been classified with this family
YQDMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDGADNEPVVYHGYTLTSKI
LFKEVITTVEKYAFEKSDYPVVLSLENHCSTEQQEIMAHYLVSILGEKLLRAPIDDPATGELPSPEALKF
KILVKNKKKIAKALSDLVIYTKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFVGHTQRFITR
IYPKGTRASSSNYNPQEFWNVGCQMVALNFQTLGAPMDLQNGKFLDN
>gnl|CDD|176538 cd08596, PI-PLCc_epsilon, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon. This family corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-epsilon isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-epsilon represents a class of mammalian PI-PLC that has an N-terminal CDC25 homology domain with a guanyl-nucleotide exchange factor (GFF) activity, a pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and two predicted RA (Ras association) domains that are implicated in the binding of small GTPases, such as Ras or Rap, from the Ras family. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There is one PI-PLC-epsilon isozyme (1). PI-PLC-epsilon is activated by G alpha(12/13), G beta gamma, and activated members of Ras and Rho small GTPases. Aside from PI-PLC-epsilon identified in mammals, its eukaryotic homologs have been classified with this family
EEDLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWDGDDGMPIIYHGHTLTTKI
PFKDVVEAINRSAFITSDYPVILSIENHCSLQQQRKMAEIFKTVFGEKLVTKFLFESDFSDDPSLPSPLQ
LKNKILLKNKKAPELSDLVIYCQAVKFPGLSTPKCYHISSLNENAAKRLCRRYPQKLVQHTRCQLLRTYP
AATRIDSSNPNPLIFWLHGLQLVALNYQTDDLPMHLNAAMFEAN
>gnl|CDD|176539 cd08597, PI-PLCc_PRIP_metazoa, Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein. This family corresponds to the catalytic domain present in metazoan phospholipase C related, but catalytically inactive proteins (PRIP), which belong to a group of novel Inositol 1,4,5-trisphosphate (InsP3) binding protein. PRIP has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP do not have PLC enzymatic activity. PRIP consists of two subfamilies, PRIP-1(previously known as p130 or PLC-1), which is predominantly expressed in the brain, and PRIP-2 (previously known as PLC-2), which exhibits a relatively ubiquitous expression. Experiments show both, PRIP-1 and PRIP-2, are involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. In addition, PRIP-2 acts as a negative regulator of B-cell receptor signaling and immune responses
CQDMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDGPNGEPVIYHGHTLTSKI
SFRSVIEAINEYAFVASEYPLILCIENHCSEKQQLVMAQYLKEIFGDKLYTEPPNEGESYLPSPHDLKGK
IIIKGKKLKRRKLCKELSDLVSLCKSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFVNYNKKF
LSRVYPSPMRVDSSNYNPQDFWNCGCQIVAMNYQTPGLMMDLNTGKFLEN
>gnl|CDD|176540 cd08598, PI-PLC1c_yeast, Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C. This family corresponds to the catalytic domain present in a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this CD is protein Plc1p encoded by PLC1 genes from Saccharomyces cerevisiae. Plc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that Plc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like Plc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily
EEDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWDGDDGEPVVTHGYTLTSSV
PFRDVCRAIKKYAFVTSPYPLILSLEVHCDAEQQERMVEIMKETFGDLLVTEPLDGLEDELPSPEELRGK
ILIKVKKESKTPNHIFSLSERSLLKLLKDKRAALDKHNRRHLMRVYPSGTRISSSNFNPLPFWRAGVQMV
ALNWQTYDLGMQLNEAMFAGS
>gnl|CDD|176541 cd08599, PI-PLCc_plant, Catalytic domain of plant phosphatidylinositide-specific phospholipases C. This family corresponds to the catalytic domain present in a group of phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11) encoded by PLC genes from higher plants, which are homologs of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The domain arrangement of plant PI-PLCs is structurally similar to the mammalian PLC-zeta isoform, which lacks the N-terminal pleckstrin homology (PH) domain, but contains EF-hand like motifs (which are absent in a few plant PLCs), a PLC catalytic core domain with X- and Y- highly conserved regions split by a linker sequence, and a C2 domain. However, at the sequence level, the plant PI-PLCs are closely related to the mammalian PLC-delta isoform. Experiments show that plant PLCs display calcium dependent PLC catalytic properties, although they lack some of the N-terminal motifs found in their mammalian counterparts. A putative calcium binding site may be located at the region spanning the X- and Y- domains
HHDMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGGRGDICVLHGGTLTKPV
KFEDCIKAIKENAFTASEYPVIITLENHLSPELQAKAAQILRETLGDKLFYPDSEDLPEEFPSPEELKGK
ILISDKPPVIRNSLSETQLKKVIEGEHPTDLIEFTQKNLLRVYPAGLRITSSNYDPMLAWMHGAQMVALN
MQGYDRPLWLNRGKFRAN
>gnl|CDD|176542 cd08600, GDPD_EcGlpQ_like, Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Escherichia coli periplasmic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46), GlpQ, and similar proteins. GP-GDE plays an essential role in the metabolic pathway of E. coli. It catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. E. coli possesses two major G3P uptake systems: Glp and Ugp, which contain genes coding for two different GP-GDEs. GlpQ gene from the E. coli glp operon codes for a periplasmic phosphodiesterase GlpQ, which is the prototype of this family. GlpQ is a dimeric enzyme that hydrolyzes periplasmic glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), to the corresponding alcohols and G3P, which is subsequently transported into the cell through the GlpT transport system. Ca2+ is required for the enzymatic activity of GlpQ. This family also includes a surface-exposed lipoprotein, protein D (HPD), from Haemophilus influenza Type b and nontypeable strains, which shows very high sequence similarity with E. coli GlpQ. HPD has been characterized as a human immunoglobulin D-binding protein with glycerophosphodiester phosphodiesterase activity. It can hydrolyze phosphatidylcholine from host membranes to produce free choline on the lipopolysaccharides on the surface of pathogenic bacteria
KIIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKRKDG
RYYVIDFTLDELKSLSVTERFDIENGKKVQVYPNRFPLWKSDFKIHTLEEEIELIQGLNKSTGKNVGIYP
EIKAPWFHHQEGKDIAAATLEVLKKYGYTSKNDKVYLQTFDPNELKRIKNELLPKMGMDLKLVQLIAYTD
WGETQEKDPGGWVNYDYDWMFTKGGLKEIAKYADGVGPWYSMIIEEKSSKGNIVLTDLVKDAHEAGLEVH
PYTVRKDALPEYAKDADQLLDALLNKAGVDGVFTDFPD
>gnl|CDD|176543 cd08601, GDPD_SaGlpQ_like, Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46) from Staphylococcus aureus, Bacillus subtilis and similar proteins. Members in this family show very high sequence similarity to Escherichia coli periplasmic phosphodiesterase GlpQ, which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols
NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIERPGPVKDYTLA
EIKQLDAGSWFNKAYPEYARESYSGLKVPTLEEVIERYGGRANYYIETKSPDLYPGMEEKLLATLDKYGL
LTDNLKNGQVIIQSFSKESLKKLHQLNPNIPLVQLLWYGEGAETYDKWLDEIKEYAIGIGPSIADADPWM
VHLIHKKGLLVHPYTVNEKADMIRLINWGVDGMFTNYPDRLKEVLK
>gnl|CDD|176544 cd08602, GDPD_ScGlpQ1_like, Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of putative bacterial and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ, as well as plant glycerophosphodiester phosphodiesterases (GP-PDEs), all of which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. The prototypes of this family include putative secreted phosphodiesterase encoded by gene glpQ1 (SCO1565) from the pho regulon in Streptomyces coelicolor genome, and in plants, two distinct Arabidopsis thaliana genes, AT5G08030 and AT1G74210, coding putative GP-PDEs from the cell walls and vacuoles, respectively
PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHPEFADRKTT
KTVDGVNVTGWFTEDFTLAELKTLRARQRLPYRDQSYDGQFPIPTFEEIIALAKAASAATGRTVGIYPEI
KHPTYFNAPLGLPMEDKLLETLKKYGYTGKKAPVFIQSFEVTNLKYLRNKTDLPLVQLIDDATIPPQDTP
EGDSRTYADLTTDAGLKEIATYADGIGPWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNENTF
LPPDFFGDPYAEYRAFLDAGVDGLFTDFP
>gnl|CDD|176545 cd08603, GDPD_SHV3_repeat_1, Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 1 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play an important role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This family includes domain I, the first GDPD domain of SHV3 and SVLs
PLVIARGGFSGLFPDSSLFAYQFAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPKRKKT
YSVNGVSTKGWFSVDFTLAELQQVTLIQGIFSRTPIFDGQYPISTVEDVVTLAKPEGLWLNVQHDAFYQQ
HNLSMSSYLLSLSKTVKVDYISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSILKNLTF
IKTFASGILVPKSYIWPVDSDQYLQPATSLVQDAHKAGLEVYASGFANDFDISYNYSYDPVAEYLSFVGN
GNFSVDGVLSDFPITASEA
>gnl|CDD|176546 cd08604, GDPD_SHV3_repeat_2, Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 2 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play important an role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This CD includes domain II (the second GDPD domain of SHV3 and SVLs), which is necessary for SHV3 function
PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSKFSNRATTV
PEIGSTSGIFTFDLTWSEIQTLKPAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNKSLSGVLINVE
NAAYLAEKKGLDVVDAVLDALTNAGYDNQTAQKVLIQSTDSSVLAAFKKQISYERVYVVDETIRDASDSS
IEEIKKFADAVVIDRGSVFPVSTSFLTRQTNVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSY
VQGAGVDGFITEFPATAARY
>gnl|CDD|176547 cd08605, GDPD_GDE5_like_1_plant, Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester phosphodiesterase-like proteins similar to mammalian GDE5. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized plant glycerophosphodiester phosphodiesterase (GP-PDE)-like proteins. Members in this family show very high sequence homology to mammalian glycerophosphodiester phosphodiesterase GDE5 and are distantly related to plant GP-PDEs
AVIGHRGLGMNRASHQPSVGPGIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVERGGEV
ESSRIRDLTLAELKALGPQAESTKTSTVALYRKAKDPEPEPWIMDVEDSIPTLEEVFSEVPPSLGFNIEL
KFGDDNKTEAEELVRELRAILAVCKQHAPGRRIMFSSFDPDAAVLLRALQSLYPVMFLTDCGPYTHNDPR
RNSIEAAIQVALEGGLQGIVSEVKVLLRNPTAVSLVKASGLELGTYGKLNNDAEAVERQADLGVDGVIVD
HV
>gnl|CDD|176548 cd08606, GDPD_YPL110cp_fungi, Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL110cp and other uncharacterized fungal homologs. The product of S. cerevisiae ORF YPL110c (GDE1), YPL110cp (Gde1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL110cp has been characterized as a cytoplasmic glycerophosphocholine (GPC)-specific phosphodiesterase that selectively hydrolyzes GPC, not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate. YPL110cp has multi-domain architecture, including not only C-terminal GDPD, but also an SPX N-terminal domain along with several ankyrin repeats, which implies that YPL110cp may mediate protein-protein interactions in a variety of proteins and play a role in maintaining cellular phosphate levels. Members in this family are distantly related to S. cerevisiae YPL206cp, which selectively catalyzes the cleavage of phosphatidylglycerol (PG), not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate, and has been characterized as a PG-specific phospholipase C
SVQVIGHRGLGKNTAERKSLQLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETGTDVPI
HDLTLEQFLHLSRMKYTVDFKKKGFKGNSRGHSIQAPFTTLEELLKKLPKSVGFNIELKYPMLHEAEEEE
VAPVAIELNAFVDTVLEKVFDYGAGRNIIFSSFTPDICILLSLKQPGYPVLFLTEAGKAPDMDVRAASLQ
EAIRFAKQWNLLGLVSAAEPLVMCPRLIQVVKRSGLVCVSYGVLNNDPENAKTQVKAGVDAVIVDSVLAI
RRGLTE
>gnl|CDD|176549 cd08607, GDPD_GDE5, Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester phosphodiesterase GDE5 and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative mammalian GDE5 and similar proteins. Mammalian GDE5 is widely expressed in mammalian tissues, with highest expression in the spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. In addition to C-terminal GDPD domain, all members in this subfamily have a starch binding domain (CBM20) in the N-terminus, which suggests these proteins may play a distinct role in glycerol metabolism
LDVGHRGAGNSYTAASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSDR
DDLLEVPVKDLTYEQLKLLKLFHISALKVKEYKSVEEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWP
QQQKDGSWESELFTYFDRNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQR
YPEFMDLRTRTFEIAVNFAQAEELLGVNLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKEL
GVDGLIYDRI
>gnl|CDD|176550 cd08608, GDPD_GDE2, Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2 and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE2 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 5 (GDPD5)) and their metazoan homologs. Mammalian GDE2 is transmembrane protein primarily expressed in mature neurons. It is a mammalian homolog of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Mammalian GDE2 selectively hydrolyzes glycerophosphocholine (GPC) and has been characterized as GPC-GDE (EC 3.1.4.2) that contributes to osmotic regulation of cellular GPC. Mammalian GDE2 functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE2 also plays a critical role for retinoid-induced neuronal outgrowth. The catalytic activity of GDPD domain is essential for mammalian GDE2 cellular function
KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYED
ASMFNWTDLERLNAGQWFLKDDPFWTAQSLSPSDRKEAGNQSVCSLAELLELAKRYNASVLLNLRRPPPN
HPYHQSWINLTLKTILASGIPQEQVMWTPDWQRKLVRKVAPGFQQTSGEKLPVASLRERGITRLNLRYTQ
ASAQEIRDYSASNLSVNLYTVNEPWLYSLLWCSGVPSVTSDASHVLRKVPFPLWLMPPDEYCLIWITSDL
ISFAVIVGIFIFQKWRLGGIRSYNPEQIMLSAAVRRSSRDVNIMKEKLIFSEINNGVETTDELSLCSDNG
Y
>gnl|CDD|176551 cd08609, GDPD_GDE3, Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE3 and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE3 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 2 (GDPD2), Osteoblast differentiation promoting factor) and their metazoan homologs. Mammalian GDE3 is a transmembrane protein specifically expressed in bone tissues and spleen. It is a mammalian homolog of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Mammalian GDE3 has been characterized as glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate inositol 1-phosphate (Ins1P) and glycerol. Mammalian GDE3 functions as an inducer of osteoblast differentiation. It also plays a critical role for actin cytoskeletal modulation. The catalytic activity of GDPD domain is essential for mammalian GDE3 cellular function
VSAAVYLAPLAICSPCIMEENNLPPKPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVP
FLMHDEGLLRTTNVKDVFPGRDAAGSNNFTWTELKTLNAGSWFLERRPFWTLSSLSEEDRREADNQTVPS
LSELLDLAKKHNVSIMFDLRNENNSHVFYSSFVFYTLETILKLGIPPDKVWWLPDEYRHDVMKMEPGFKQ
VYGRQKEMLMDGGNFMNLPYQDLSALEIKELRKDNVSVNLWVVNEPWLFSLLWCSGVSSVTTNACQLLKD
MSKPIWLLEPNTYLGIWIATDCVSLLLMLWLFLLQ
>gnl|CDD|176552 cd08610, GDPD_GDE6, Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE6 and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE6 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 4 (GDPD4)) and their metazoan homologs. Mammalian GDE6 is a transmembrane protein predominantly expressed in the spermatocytes of testis. Although the specific physiological function of mammalian GDE6 has not been elucidated, its different pattern of tissue distribution suggests it might play a critical role in the completion of meiosis during male germ cell differentiation
LYLIPLGIYSPCIREKETLGPKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMH
DFTLKRTTNIGEVQPESACENPAFFNWDFLSTLNAGKWFVKPRPFYNMKPLSEADKERARNQSIPKLSNF
LRLAEKENKLVIFDLYRPPPKHPYRHTWIRRVLEVILNEVGIEQHLVLWLPAHDRQYVQSVAPGFKQHVG
RKVPIETLLKNNISILNLAYKKLFSNDIRDYKAANIHTNVYVINEPWLFSLAWCSGIHSVTTNNIHLLKQ
LDHPHFFMTPKFYVFMWLLADIISVLFIVLIFCFHW
>gnl|CDD|176553 cd08612, GDPD_GDE4, Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4 and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE4 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1)) and similar proteins. Mammalian GDE4 is a transmembrane protein whose cellular function has not yet been elucidated. It is expressed widely, including in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. It is also expressed in the growth cones in neuroblastoma Neuro2a cells, which suggests GDE4 may play some distinct role from other members of the GDE family
GGYIATSYFLLRNPTLLHKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQV
VVSHDENLLRSCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYCVPKGSDRRIPLLEEVFEAFPDTPINID
IKVENDELIKKVSDLVRKYKREDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIP
IKESFLEIPMPSIFLKTYFPKSMSRLNRFVLFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFE
LGADGVMTDYPTKLREFLDK
>gnl|CDD|176554 cd08613, GDPD_GDE4_like_1, Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of mammalian glycerophosphodiester phosphodiesterase GDE4. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial homologs of mammalian GDE4, a transmembrane protein whose cellular function has not been elucidated yet
LLLAAAGVWLNNTSLLAPPPGGKPKLLAHRGLAQTFDREGVENDTCTAERIDPPTHDYLENTIASMQAAF
DAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELKTLDIGYGYTADGGKTFPFRGKGVG
MMPTLDEVFAAFPDRRFLINFKSDDAAEGELLAEKLATLPRKRLQVLTVYGGDKPIAALRELTPDLRTLS
KASMKDCLIEYLALGWTGYVPDSCRNTTLLIPLNYAPWLWGWPNRFLARMEAAGTRVILVGPYTGGEFSE
GFDTPEDLKRLPEGFTGYIWTNKIEALAP
>gnl|CDD|176555 cd08616, PI-PLCXD1c, Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1. This subfamily corresponds to the catalytic domain present in a group of phosphatidylinositol-specific phospholipase C X domain containing 1 (PI-PLCXD1), 2 (PI-PLCXD2) and 3 (PI-PLCXD3), which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs found in vertebrates. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, members in this group contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs
LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQSVQNLVKVFPCIFKKIVKKWSKTQSLTITEQLEA
GIRYFDLRIATKPKDNDLYFVHGLYGILVKEILEEINDFLTEHPKEVVILDFNHFYGMTEEDHEKLLKMI
KSIFGKKLCPRDPDLLNVTLEYLWEKGYQVIVFYHDPVAKKPPYLWPSDAIPSPWPNTTDPKKLIQFLET
TLKERRPPGFHVSQGILTPDVKTILRHLTSGLLKTLTLRALPKLLEWLRKQEPGSGQGVNIIIADFVDLD
EFIDTVIALN
>gnl|CDD|176556 cd08619, PI-PLCXDc_plant, Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing proteins found in plants. The CD corresponds to the catalytic domain present in uncharacterized plant phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, plant PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of plant PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs
FPGCDFHTDDHKEWMSLSQLKAMDSSLKLRDIVWPGTHDSATNKIGIPKVSRPFARCQSLSIYNQLCSGA
RVLDIRVQEDRRVCHGCLKTYPVDVVLNDIKRFLSETKSEFVILEIRTEYGHEDPPQFDLWLVEQLGDHL
IHQDDSVFSKTLAELLPKRVICIWKPRKSPAPAVGSPLWSSAYLKDNWIDTDLPVTKFESNIKNLLEQPP
QDSRKYFYRVENTVTPQFDNPILCVKPVTRRISQYARLFIPEVFKRGLADRLQIFSLDFIDLDFVDACIG
LTVAR
>gnl|CDD|176557 cd08620, PI-PLCXDc_like_1, Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins. This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs
GSAPAQQPFNRFVLPGAHDAGMNGMTNLSVTQKDNVSTQLALGARYFDFRPGYLWPQTRVLVLLNDLYHQ
HNMIPGQGFDTFLQDVVTFLKANPTEIVVVHITWDGFDNDCARPSAQEVVEALAQALASAKVGYVTSGTV
SDLAASYAQLRQTGKRLIVLFGDADKYDSYSDEDYATSDPQPIIDALNKMLAEGQSGYDYTVLQLQATAS
STKKGLAAAILSGSHAGSPLLATKAMFDSATLPWLRENVLARLGDDPLVVLMNDFVDNATTDVAIALTKQ
R
>gnl|CDD|176558 cd08621, PI-PLCXDc_like_2, Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins. This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs
YEVIKDRPLRHIVMPGTHDSGMSSLTGGLWPVDGNDSNTQTQGLSIYDQLRAGARYFDIRPVITHGGELW
TGHYNGEDASAQGANGESLDDILDEVNRFTDENPGELVILNFSHILNTDNGDGRPFSAEEWEKIFDELEG
INNRCGNIDEEGDLYTQKLSDFIDASGKACVVFIYDGTISSNQGSTPAKGGIYDGPQFTVYDSYSNTDDT
NYMAEDQLAKLRSHRRPSFGDDIFFLLSWTLTPQALTVTGSSIKKLAEEANPALFWKLVDAMSPWSFPNV
VYVDYLGNFGEVLALAIGLN
>gnl|CDD|176559 cd08622, PI-PLCXDc_CG14945_like, Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to phosphatidylinositol-specific phospholipase C, X domain containing. This subfamily corresponds to the catalytic domain present in uncharacterized metazoan Drosophila melanogaster CG14945-like proteins, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs
KKSIGNLRIKDLFIPGTHNSAAYDTNSNANESLVDKYLLTQDLDIWTQLVHGIRYLDLRVGYYPDSPDNF
WINHDLVRIVPLLTVLNDVRNFVQNTGEIVVLDFHRFPVGFHSHPEVHDELISLLRQELGDLILRRSRNY
GWGPTLSEIWARRKRVIICYDHEYFVRESDWLWPPVQQKWGNVQTLDDLKSYLRKLISQPHRFTNPPVSL
MAELTPVPWDIISDRLGNLRKLADIVNRKLTRWYRDEWGYNANIVATDFFLGTNIIDVAIETNLRK
>gnl|CDD|176560 cd08623, PI-PLCc_beta1, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1. This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 1. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta1 is expressed at highest levels in specific regions of the brain. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension
NEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTT
EISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPS
PMDLMYKILVKNKKMSNLVNYIQPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLS
RIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLSMQINMGMYEYN
>gnl|CDD|176561 cd08624, PI-PLCc_beta2, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2. This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 2. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta2 is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins
HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTT
EILFKDAIEAIAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPS
PEDLRGKILIKNKKYEEMSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKR
QMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQTMDLPMQQNMALFEFN
>gnl|CDD|176562 cd08625, PI-PLCc_beta3, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3. This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 3. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta3 is widely expressed at highest levels in brain, liver, and parotid gland. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins
SDDMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTT
EIPFKDVIEAIAESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPS
PQELMGKILVKNKKMSTLVNYIEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPMEFVEYNKKQLS
RIYPKGTRVDSSNYMPQLFWNVGCQMVALNFQTLDLAMQLNMGVFEYN
>gnl|CDD|176563 cd08626, PI-PLCc_beta4, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4. This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 4. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta4 is expressed in high concentrations in cerebellar Purkinje and granule cells, the median geniculate body, and the lateral geniculate nucleus. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension
YQDMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCT
DILFKDVIQAIKDTAFVTSDYPVILSFENHCSKPQQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSP
NKLKRKILIKNKRLSSLVNYAQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSAIEFVNYNKRQMSR
IYPKGTRVDSSNYMPQIFWNAGCQMVSLNFQTPDLGMQLNQGKFEYN
>gnl|CDD|176564 cd08627, PI-PLCc_gamma1, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1. This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-gamma isozyme 1. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-gamma represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unique to PI-PLC-gamma1, a second PH domain, two SH2 (Src homology 2) regions, and one SH3 (Src homology 3) region is present within this linker region. PI-PLC-gamma1 is ubiquitously expressed. It is activated by receptor and non-receptor tyrosine kinases due to the presence of two SH2 and a single SH3 domain within the linker region
PEEMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKI
KFSDVLHTIKEHAFVTSEYPIILSIEDHCSIVQQRNMAQHFKKVFGDMLLTKPVDINADGLPSPNQLKRK
ILIKHKKLYRDMSSFPETKAEKYVNRSKGKKFLQYNRRQLSRIYPKGQRLDSSNYDPLPMWICGSQLVAL
NFQTPDKPMQMNQALFMLG
>gnl|CDD|176565 cd08628, PI-PLCc_gamma2, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2. This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-gamma isozyme 2. PI-PLC is a signaling enzyme that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-gamma represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unique to PI-PLC-gamma2, a second PH domain, two SH2 (Src homology 2) regions, and one SH3 (Src homology 3) region is present within this linker region. PI-PLC-gamma2 is highly expressed in cells of hematopoietic origin. It is activated by receptor and non-receptor tyrosine kinases due to the presence of two SH2 and a single SH3 domain within the linker region. Unlike PI-PLC-gamma1, the activation of PI-PLC-gamma2 may require concurrent stimulation of PI 3-kinase
PQDMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDGPDGKPIIYHGWTRTTKI
KFDDVVQAIKDHAFVTSEYPVILSIEEHCSVEQQRHMAKVFKEVFGDKLLMKPLEASADQLPSPTQLKEK
IIIKHKKLIAIELSDLVVYCKPTSKTKDNLENPDFKEIRSFVETKAPSIIRQKPVQLLKYNRKGLTRVYP
KGQRVDSSNYDPFRLWLCGSQMVALNFQTADKYMQLNHALFSLN
>gnl|CDD|176566 cd08629, PI-PLCc_delta1, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1. This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta1 isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This subfamily corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Unlike PI-PLC-delta 4, PI-PLC-delta1 and 3 possess a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1and 3 from the cell nucleus. Experiments show PI-PLC-delta1 is essential for normal hair formation
YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTFTSKI
LFCDVLRAIRDYAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDGVTTSLPSPEQLKGK
ILLKGKKLKLVPELSDMIIYCKSVHFGGFSSPGTSGQAFYEMASFSESRALRLLQESGNGFVRHNVSCLS
RIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDN
>gnl|CDD|176567 cd08630, PI-PLCc_delta3, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3. This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta3 isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This family corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). Unlike PI-PLC-delta 4, PI-PLC-delta1 and 3 possess a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1 and 3 from the cell nucleus
FQDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKI
LFRDVIQAVRQHAFTASPYPVILSLENHCGLEQQAAMARHLQTILGDMLVTQPLDSLNPEELPSPEELKG
RVLVKGKKLQISPELSALAVYCQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLT
RVYPLGLRMNSANYSPQEMWNSGCQLVALNFQTPGYEMDLNAGRFLVN
>gnl|CDD|176568 cd08631, PI-PLCc_delta4, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4. This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta4 isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This CD corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). Unlike PI-PLC-delta 1 and 3, a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1 and 3 from the cell nucleus, is not present in PI-PLC-delta4. Experiments show PI-PLC-delta4 is required for the acrosome reaction in fertilization
YQDMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDGPNGEPIVYHGHTFTSKI
LFKDVVAAVAQYAFQVSDYPVILSLENHCGVEQQQTMAQHLTEILGEKLLSTTLDGVLPTQLPSPEELRG
KILLKGKKIRLSPELSDCVIYCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEFVQHNTWQLS
RVYPSGLRTDSSNYNPQEMWNAGCQMVALNFQTAGLEMDLNDGLFRQN
>gnl|CDD|176569 cd08632, PI-PLCc_eta1, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1. This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-eta isozyme 1. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-eta represents a class of neuron-speific PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-eta1 is a neuron-specific enzyme and expressed in only nerve tissues such as the brain and spinal cord. It may perform a fundamental role in the brain
NQDMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDGPDGEPVVHHGYTLTSKI
TFRDVIETINKYAFVKNEFPVILSIENHCSIQQQKKIAQYLKEIFGDKLDLSSVLTGDPKQLPSPQLLKG
KILVKGKKLCRDLSDLVVYTNSVAAQDIVDDGSTGNVLSFSETRAHQLVQQKAEQFMTYNQKQLTRIYPS
AYRIDSSNFNPLPYWNVGCQLVALNYQSEGRMMQLNRAKFMVN
>gnl|CDD|176570 cd08633, PI-PLCc_eta2, Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2. This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-eta isozyme 2. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-eta represents a class of neuron-speific PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-eta2 is a neuron-specific enzyme and expressed in the brain. It may in part function downstream of G-protein-coupled receptors and play an important role in the formation and maintenance of the neuronal network in the postnatal brain
NQDMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDGPDGEPIVHHGYTLTSKI
LFKDVIETINKYAFIKNEYPVILSIENHCSVPQQKKMAQYLTEILGDKLDLSSVISNDCTRLPSPEILKG
KILVKGKKLSRALSDLVKYTKSVRVHDIETEATSSWQVSSFSETKAHQILQQKPAQYLRFNQRQLSRIYP
SSYRVDSSNYNPQPFWNAGCQMVALNYQSEGRMLQLNRAKFSAN
>gnl|CDD|176474 cd08637, DNA_pol_A_pol_I_C, Polymerase I functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. Family A polymerase (polymerase I) functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. DNA-dependent DNA polymerases can be classified in six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerase are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I (pol I), mitochondrial polymerase delta, and several bacteriphage polymerases including those from odd-numbered phage (T3, T5, and T7). Prokaryotic Pol Is have two functional domains located on the same polypeptide; a 5'-3' polymerase and 5'-3' exonuclease. Pol I uses its 5' nuclease activity to remove the ribonucleotide portion of newly synthesized Okazaki fragments and DNA polymerase activity to fill in the resulting gap. A combination of phylogenomic and signature sequence-based (or phonetic) approaches is used to understand the evolutionary relationships among bacteria. DNA polymerase I is one of the conserved proteins that is used to search for protein signatures. The structure of these polymerases resembles in overall morphology a cupped human right hand, with fingers (which bind an incoming nucleotide and interact with the single-stranded template), palm (which harbors the catalytic amino acid residues and also binds an incoming dNTP) and thumb (which binds double-stranded DNA) subdomains
DTEYLEELSEELEKELAELEEEIYELAGEEFNINSPKQLGEVLFEKLGLPVGKKTKTGYSTDAEVLEKLA
DEHPIVELILEYRELTKLKSTYVDALPKLINPKTGRIHTSFNQTVTATGRLSSSDPNLQNIPIRTEEGRE
IRKAFVAEEGWVLLSADYSQIELRILAHLSGDEALIEAFKNGEDIHTRTAAEVFGVPPEEVTPEMRRIAK
AVNFGIIYGISAFGLSQQLGISRKEAKEYIDRYFARYPGVKEYMEETVEEAREKGYVETLFGRRRYIPEI
NSKNRNVRAFAERIAINTPIQGTAADIIKLAMIRVHKALKEEGLKARMLLQVHDELVFEVPEEELEEVAA
LVKEEMENAVELSVPLKVDVGVGKNWG
>gnl|CDD|176475 cd08638, DNA_pol_A_theta, DNA polymerase theta is a low-fidelity family A enzyme implicated in translesion synthesis and in somatic hypermutation. DNA polymerase theta is a low-fidelity family A enzyme implicated in translesion synthesis (TLS) and in somatic hypermutation (SHM). DNA-dependent DNA polymerases can be classified in six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerase functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. Pol theta is an exception among family A polymerases and generates processive single base substitutions. Family A polymerase are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I (pol I), mitochondrial polymerase delta, and several bacteriphage polymerases including those from odd-numbered phage (T3, T5, and T7). Prokaryotic Pol Is have two functional domains located on the same polypeptide; a 5'-3' polymerase and 5'-3' exonuclease. Pol I uses its 5' nuclease activity to remove the ribonucleotide portion of newly synthesized Okazaki fragments and DNA polymerase activity to fill in the resulting gap. Polymerase theta mostly has amino-terminal helicase domain, a carboxy-terminal polymerase domain and an intervening space region
GIGFDPEELERQRALLQAKLKELEEEAYRSTSKEVLEQLKRLHPLPKLILEYRKLSKLLTTYVEPLLLLC
KLSSSLQMYRIHPTWNQTGTATGRLSSSEPNLQNVPKDFEIKDAPSPPAGSEGDIPTISLRHAFIPPPGR
VLLSADYSQLELRILAHLSGDPALIELLNSGGDVFKMIAAQWLGKPVEEVTDEERQQAKQLVYGILYGMG
AKSLAEQLGVSEEEAKQFIESFKNAYPGVRRFIRETIERARRNGFVETLTGRRRYLPEINSGNSSERAQA
ERQAVNTVIQGSAADIMKIAMINIHEKLHSLLPNLPAGRARLVLQIHDELLFEVPESDVDEVARIIKRSM
ENAAKLSVPLPVKVSIGKSWGSL
>gnl|CDD|176476 cd08639, DNA_pol_A_Aquificae_like, Phylum Aquificae Pol A is different from Escherichia coli Pol A by three signature sequences. Family A polymerase functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. DNA-dependent DNA polymerases can be classified in six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerase are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I, mitochondrial polymerase delta, and several bacteriphage polymerases including those from odd-numbered phage (T3, T5, and T7). Prokaryotic Pol Is have two functional domains located on the same polypeptide; a 5'-3' polymerase and 5'-3' exonuclease. Pol I uses its 5' nuclease activity to remove the ribonucleotide portion of newly synthesized Okazaki fragments and DNA polymerase activity to fill in the resulting gap. A combination of phylogenomic and signature sequence-based (or phonetic) approaches is used to understand the evolutionary relationships among bacteria. DNA polymerase I is one of the conserved proteins that is used for phylogenetic anaylsis of bacteria. Species of the phylum Aquificae grow in extreme thermophilic environments. The Aquificae are non-spore-forming, Gram-negative rods and strictly thermophilic. Phylum Aquificae Pol A is different from E. coli Pol I by three signature sequences consisting of a 2 amino acids (aa) insert, a 5-6 aa insert and a 6 aa deletion. These signature sequences may provide a molecular marker for the family Aquificaceae and related species
LDLERWKELEKELERERQEAAKELYIEEHPAVRLLLEYRKLNKLISTFGEKLPKHIHPVTGRIHPSFNQI
GAASGRMSCSNPNLQQIPREREFRRCFVAPEGNKLIIADYSQIELRIAAEISGDERMISAYQKGEDLHRL
TASLITGKPIEEITKEERQLAKAVNFGLIYGMSAKGLREYARTNYGVEMSLEEAEKFRESFFFFYKGILR
WHHRLKAKGPIEVRTLLGRRRVFEYFTFTEALNYPIQGTGADILKLALALLVDRLKDLDAKIVLCVHDEI
VLEVPEDEAEEAKKILESSMEEAGKRILKKVPVEVEVSISDSWA
>gnl|CDD|176477 cd08640, DNA_pol_A_plastid_like, DNA polymerase A type from plastids of higher plants possibly involve in DNA replication or in the repair of errors occurring during replication. DNA polymerase A type from plastids of higher plants possibly involve in DNA replication or in the repair of errors occurring during replication. Family A polymerase functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. DNA-dependent DNA polymerases can be classified in six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerase are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I, mitochondrial polymerase delta, and several bacteriphage polymerases including those from odd-numbered phage (T3, T5, and T7). The three-dimensional structure of plastid DNA polymerase has substantial similarity to Pol I. The structure of Pol I resembles in overall morphology a cupped human right hand, with fingers (which bind an incoming nucleotide and interact with the single-stranded template), palm (which harbors the catalytic amino acid residues and also binds an incoming dNTP) and thumb (which binds double-stranded DNA) subdomains
GLPSVDSEALRELAGDPEADILLYEWCYENGVSGGEEGKEACEAIEALKEIKSISTLLSTFIIPLQELLN
DSTGRIHCSLNINTETGRLSSRNPNLQNQPALEKDRYKIRKAFIASPGNTLIVADYSQLELRLLAHMTRC
KSMIEAFNAGGDFHSRTASGMYPHVAEAVANGEVLLEWKSEGKPPAPLLKDKFKSERRKAKVLNFSIAYG
KTAHGLAKDWKVKLKEAERTVDAWYSDRPEVEQWQKKTKKEARERGYTRTLLGRYRYLPDIKSRNRKKRG
HAERAAINTPIQGSAADIAMKAMLRIYRNLRLKRLGWKLLLQIHDEVILEGPEEKADEALKIVKDCMENP
FFGPLDVPLEVDGSVGYNWYE
>gnl|CDD|176478 cd08641, DNA_pol_gammaA, Pol gammaA is a family A polymerase that is responsible for DNA replication and repair in mitochondria. DNA polymerase gamma (Pol gamma), 5'-3' polymerase domain (Pol gammaA). Pol gammaA is a family A polymerase that is responsible for DNA replication and repair in mitochondria. Family A polymerase functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. DNA-dependent DNA polymerases can be classified into six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaeota polymerase II (class D), human polymerase beta (class X), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerases are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I, mitochondrial polymerase gammaA, and several bacteriophage polymerases including those from odd-numbered phage (T3, T5, and T7). The structure of these polymerases resembles in overall morphology a cupped human right hand, with fingers (which bind an incoming nucleotide and interact with the single-stranded template), palm (which harbors the catalytic amino acid residues and also binds an incoming dNTP) and thumb (which binds double-stranded DNA) subdomains. Pol gammaA has also the right hand configuration. Pol gammaA has both polymerase and proofreading exonuclease activities separated by a spacer. Pol gamma holoenzyme is a heterotrimer containing one Pol gammaA subunit and a dimeric Pol gammaB subunit. Pol gamma is important for mitochondria DNA maintenance and mutation of the catalytic subunit of Pol gamma is implicated in more than 30 human diseases
GSAYLPVNSNWERYLNTAEETYQELQQEVKESLMQLAEDACQLDPQAKRALEINKMCSYWRNARDRIMSQ
MVVWDDKSELPRAVSRHPQDDEEPGYGAILPQVVPMGTITRRAVEPTWLTASNAKKNRVGSELKAMVQAP
PGYSFVGADVDSQELWIASVLGDAHFGGIHGATAIGWMTLQGKKSEGTDLHSKTASILGISRDHAKVFNY
GRIYGAGQPFAERLLMQFNPRLTPAEATEKAKQMYAATKGIRIAIQRSTKGKRLFKRPFWSGGSESIMFN
KLEEIAAQSQPRTPVLGACITSALLEPNLVKNEFMTSRINWVVQSSAVDYLHLMLVSMRWLIEKYDIDAR
FCISIHDEVRYLVKEEDKYRAALALQITNLLTRAMFAQKLGINDLPQSVAFFSAVDIDTVLRKEVDMDCV
TPSNP
>gnl|CDD|176479 cd08642, DNA_pol_A_pol_I_A, Polymerase I functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. Family A polymerase (polymerase I) functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. DNA-dependent DNA polymerases can be classified in six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerase are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I, mitochondrial polymerase delta, and several bacteriphage polymerases including those from odd-numbered phage (T3, T5, and T7). Prokaryotic Pol Is have two functional domains located on the same polypeptide; a 5'-3' polymerase and 5'-3' exonuclease. Pol I uses its 5' nuclease activity to remove the ribonucleotide portion of newly synthesized Okazaki fragments and DNA polymerase activity to fill in the resulting gap. A combination of phylogenomic and signature sequence-based (or phonetic) approaches is used to understand the evolutionary relationships among bacteria. DNA polymerase I is one of the conserved proteins that is used to search for protein signatures. The structure of these polymerases resembles in overall morphology a cupped human right hand, with fingers (which bind an incoming nucleotide and interact with the single-stranded template), palm (which harbors the catalytic amino acid residues and also binds an incoming dNTP) and thumb (which binds double-stranded DNA) subdomains
LVNAAIACDDQYKEELLEEAKELTGLDNPNSPAQLKDWLNEQGGEVDSLLKKDVVALLLKTAPGDVKRVL
ELRQELSKTSVKKYEAMERAVCSDGRVRGLLQFYGANRTGRWAGRLVQVQNLPRNYLKDLDLARELVKSG
DFDALELLYGSVPDVLSQLIRTAFIPSEGHRFIVSDFSAIEARVIAWLAGEQWRLDVFATHGKIYEASAS
QMFGVPVEKIGKNSHLRQKGKVAELALGYGGSVGALKAMGALEMGLTEDELPGIVDAWRNANPNIVKLWW
DVDKAAKKAVKERKTVKLGGKLVENIVQAIARDCLAEAMLRLEKAGYDIVMHVHDEVVIEVPEGEGSLEE
VNEIMAQPPPWAPGLPLNADGFESPYYM
>gnl|CDD|176480 cd08643, DNA_pol_A_pol_I_B, Polymerase I functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. Family A polymerase functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. DNA-dependent DNA polymerases can be classified in six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerase are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I, mitochondrial polymerase delta, and several bacteriphage polymerases including those from odd-numbered phage (T3, T5, and T7). Prokaryotic Pol Is have two functional domains located on the same polypeptide; a 5'-3' polymerase and 5'-3' exonuclease. Pol I uses its 5' nuclease activity to remove the ribonucleotide portion of newly synthesized Okazaki fragments and DNA polymerase activity to fill in the resulting gap. A combination of phylogenomic and signature sequence-based (or phonetic) approaches is used to understand the evolutionary relationships among bacteria. DNA polymerase I is one of the conserved proteins that is used to search for protein signatures. The structure of these polymerases resembles in overall morphology a cupped human right hand, with fingers (which bind an incoming nucleotide and interact with the single-stranded template), palm (which harbors the catalytic amino acid residues and also binds an incoming dNTP) and thumb (which binds double-stranded DNA) subdomains
FNQEKAAKLYAQLAGRREDLENELQEVFPPWYVSDGFVPKKRTTNNSVRGYVKGAPYTKIKLVTFNPSSR
KHIAKRLKAKYGWEPQEFTESGEPKVDEDVLSKLDYPEAKLLAEYLLVQKRLGQLADGNNAWLKLVHEDG
RIHGAVNTNGAVTGRATHFSPNMAQVPAVGSPYGKECRELFGVPPGWSLVGADASGLELRCLAHYLARYD
GGAYTRKVLGGDIHWANAQAMGLLSRDGAKTFIYAFLYGAGDEKLGQIVGDDLRTAKNLNAEWPQTKKGT
IKKIADKAKGRVVRANFLKGLPALGKLIKKVKEAAKKRGHLVGLDGRRIRVRSAHAALNTLLQSAGAILM
KKWLVLLDDELTAKGGVWGGDFEYCAWVHDEVQIECRKGIAEEVGKIAVEAAEKAGEHFNFRCPLAGEFD
IGRNWAETH
>gnl|CDD|187713 cd08644, FMT_core_ArnA_N, ArnA, N-terminal formyltransferase domain. ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle
MKAVVFAYHEVGYRCLEALLAAGFEVVAVFTHTDNPGENIWFGSVAQLAREHGIPVFTPDDINHPEWVER
LRALKPDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPD
AGAIVDQEKVPILPDDTAKSLFHKLCVAARRLLARTLPALKAGKARERPQDETQASYFGGRKP
>gnl|CDD|187714 cd08645, FMT_core_GART, Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART). Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities
RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEAL
LELLKEYKVDLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDE
EVDTGPIIAQAAVPVLPGDTPETLAERIHALEHRLYPEAIKLL
>gnl|CDD|187715 cd08646, FMT_core_Met-tRNA-FMT_N, Methionyl-tRNA formyltransferase, N-terminal hydrolase domain. Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme
MRIVFMGTPDFAVPSLEALLKSGHEVVAVVTQPDKPRGRGKKLTPSPVKELALELGLPVLQPEKLKDEEF
LEELKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDE
GLDTGDILAQEEVPIDPDDTAGELLDKLAELGADLLLEVLDDIEAGKLNPVPQDESEATYAPKI
>gnl|CDD|187716 cd08647, FMT_core_FDH_N, 10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain. This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain
MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVV
AKYKALGAELNVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDG
LDTGPILLQKECDVLPNDTVDTLYNRFLYPEGIKAMVEAVRLIAEGKAPRIPQPEEGATYEGI
>gnl|CDD|187717 cd08648, FMT_core_Formyl-FH4-Hydrolase_C, Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formate is the substrate of phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase has been proposed to regulate the balance of FH4 and C1-FH4 in the cell. The enzyme uses methionine and glycine to sense the pools of C1-FH4 and FH4, respectively. This domain belongs to the formyltransferase (FMT) domain superfamily. Members of this family have an N-terminal ACT domain, which is commonly involved in specifically bind an amino acid or other small ligand leading to regulation of the enzyme. The N-terminal of this protein family may be responsible for the binding of the regulators methionine and glycine
KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPLAERFGIPFHHIPVTKDTKAEAEAEQLE
LLEEYGVDLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEEL
DEGPIIEQDVERVSHRDSVEDLVRKGRDIEKQVLARAVKWHLEDRVLVYGNKTVVF
>gnl|CDD|187718 cd08649, FMT_core_NRPS_like, N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin. This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins
SCVIIGGGTLLIQCAEQLLAAGHRIAAVVSTDPAIRAWAAAEGIAVLEPGEALEELLSDEPFDWLFSIVN
LRILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAP
DDTALSLNLKCYEAGIEGFGELIDEL
>gnl|CDD|187719 cd08650, FMT_core_HypX_N, HypX protein, N-terminal hydrolase domain. The family represents the N-terminal hydrolase domain of HypX protein. HypX is involved in the maturation process of active [NiFe] hydrogenase [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions [NiFe] hydrogenases consist of a large and a small subunit. The large subunit contains [NiFe] active site, which is synthesized as a precursor without the [NiFe] active site. This precursor then undergoes a complex post-translational maturation process that requires the presence of a number of accessory proteins. HypX has been shown to be involved in this maturation process and have been proposed to participate in the generation and transport of the CO and CN ligands. However, HypX is not present in all hydrogen-metabolizing bacteria. Furthermore, hypX deletion mutants have a reduced but detectable level of hydrogenase activity. Thus, HypX might not be a determining factor in the matur ation process. Members of this group have an N-terminal formyl transferase domain and a C-terminal enoyl-CoA hydratase/isomerase domain
MKILLLCSAFNSLTQRAFLELRERGHEVSVEYALSDDEMREAVALFAPDLIICPFLKKRIPEEIWSNYPC
LIVHPGIVGDRGPSSLDWAILEGEKEWGVTVLQAVEEMDAGPIWATRNFPLRRAATKSSLYRGEVTDAAV
KAVLEAVENFE
>gnl|CDD|187720 cd08651, FMT_core_like_4, Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme
RIVFIGCVEFSLIALEAILEAGGEVVGVITLDDSSSNNDSDYLDLDSFARKNGIPYYKFTDINDEEIIEW
IKEANPDIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGAD
SGDILSQEPFPIDKDDTANSLYDKIMEAAKQQIDKFLPRL
>gnl|CDD|187721 cd08653, FMT_core_like_3, Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme
RIVLLTGDDPSHLYLANALLDAFGGVGVIVVNSINGPEVVAALRALAPDVVSVYGCGIIKDALLAIPPLG
VLNLHGGILPDYRGVHTGFWALANGDPDNVGVTVHLVDAGIDTGDVLAQARPPLAAGDTLLSLYLRLYRA
GVELMVEAIADL
>gnl|CDD|349943 cd08656, M28_like, M28 Zn-peptidase; uncharacterized subfamily. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions
ADSAYQYVQNQVDFGPRVPNTAAHKACGEYLAGKLEAFGAKVYNQYADLIAYDGTILKARNIIGAYNPES
KKRVLLCAHWDSRPYADNDADPKKHHTPILGANDGASGVGALLEIARQIQQQAPAIGIDIIFFDAEDYGT
PEFYEGKYKSDTWCLGSQYWARNPHVQGYNARYGILLDXVGGKNATFLKEQYSLRTARDIVKKIWKTAKR
LGYGKYFVPEAGGTITDDHLYVNQLARIPTIDIINYDPERPTGFPSYWHTIQDNXENIDKETLKAVGQTV
LEVIYNE
>gnl|CDD|349944 cd08659, M20_ArgE_DapE-like, Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like. Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline
SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVATVGGGDGPVLLLNGHIDTVPPGD
GDKWSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALL
EAGYADRLDALIVGEPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELP
AHPLLGPPTLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDP
PFFTDPDHPLVQALQAAARALGGDPVVRPFTGTTDASYFAKDLGFPVVVYGPGDLALAHQPDEYVSLEDL
LRAAEIYKEII
>gnl|CDD|349945 cd08660, M20_Acy1-like, M20 Peptidase Aminoacylase 1-like family. This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1L2 family contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay
LINIRRDIHEHPELGFEEVETSKKIRRWLEEEQIEILDVPQLKTGVIAEIKGGEDGPVIAIRADIDALPI
QEQTNLPFASKVDGTXHACGHDFHTTSIIGTAXLLNQRRAELKGTVVFIFQPAEEGAAGARKVLEAGVLN
GVSAIFGIHNKPDLPVGTIGVKEGPLXASVDVFEIVIKGKGGHASIPNNSIDPIAAAGQIISGLQSVVSR
NISSLQNAVVSITRVQGGTAWNVIPDQAEXEGTVRAFTKEARQAVPEHXRRVAEGIAAGYGCQAEFKWFP
NGPSEVQNDGTLLNAFSKAAARLGYATVHAEQSPGSEDFALYQEKIPGFFVWXGTNGRTEEWHHPAFRLD
EEALTVGAQIFAELAV
>gnl|CDD|341056 cd08662, M13, Peptidase family M13 includes neprilysin and endothelin-converting enzyme I. The M13 family of metallopeptidases includes neprilysin (neutral endopeptidase, NEP, enkephalinase, CD10, CALLA, EC 3.4.24.11), endothelin-converting enzyme I (ECE-1, EC 3.4.24.71), erythrocyte surface antigen KELL (ECE-3), phosphate-regulating gene on the X chromosome (PHEX), soluble secreted endopeptidase (SEP), and damage-induced neuronal endopeptidase (DINE)/X-converting enzyme (XCE). Proteins in this family fulfill a broad range of physiological roles due to the greater variation in the active site's S2' subsite allowing substrate specificity. NEP is expressed in a variety of tissues including kidney and brain, and is involved in many physiological and pathological processes, including blood pressure and inflammatory response. It degrades a wide array of substrates such as substance P, enkephalins, cholecystokinin, neurotensin and somatostatin. It is an important enzyme in the regulation of amyloid-beta (Abeta) protein that forms amyloid plaques that are associated with Alzeimers disease (AD). ECE-1 catalyzes the final rate-limiting step in the biosynthesis of endothelins via post-translational conversion of the biologically inactive big endothelins. Like NEP, it also hydrolyzes bradykinin, substance P, neurotensin, and Abeta. Endothelin-1 overproduction has been implicated in various diseases including stroke, asthma, hypertension, and cardiac and renal failure. Kell is a homolog of NEP and constitutes a major antigen on human erythrocytes; it preferentially cleaves big endothelin-3 to produce bioactive endothelin-3, but is also known to cleave substance P and neurokinin A. PHEX forms a complex interaction with fibroblast growth factor 23 (FGF23) and matrix extracellular phosphoglycoprotein, causing bone mineralization. A loss-of-function mutation in PHEX disrupts this interaction leading to hypophosphatemic rickets; X-linked hypophosphatemic (XLH) rickets is the most common form of metabolic rickets. ECEL1 is a brain metalloprotease which plays a critical role in the nervous regulation of the respiratory system, while DINE is abundantly expressed in the hypothalamus and its expression responds to nerve injury. A majority of these M13 proteases are prime therapeutic targets for selective inhibition
VDPCDDFYQYACGNWLKNHPIPADKSSWGSFSELQDRNEEQLREILEEAASSAADSSAEQKAKDFYKSCM
DEEAIEKLGLKPLKPLLDKIGGLPSLDDLAAELLLALLRRLGVSLLFGLGVSPDPKNSSRNILYLGQPGL
GLPDRDYYLDEENAEIREAYKKYIAKLLELLGADEEEAEKLAEDVLAFETELAKISLSSEELRDPEKTYN
PLTLAELQKLAPSIDWKAYLKALGPPADDPDKVIVSQPEYLKKLDKLLASTPLRTLKNYLIWRLLDSLAP
YLSKEFRDARFFYGKALSGQKEPEPRWKRCVELVNGALGEALGRLYVEKYFSEEAKADVEEMVENIKEAF
KERLENLDWMDEETKKKALEKLDAMKVKIGYPDKWRDYSALDIYYDDLNVSDSYFENVLRLLRFETKRQL
AKLGKPVDRTEWSMSPQTVNAYYNPSLNEIVFPAGILQPPFFDPDAPDALNYGGIGAVIGHEITHGFDDQ
GRQYDENGNLRNWWTNEDRKEFEERAQCLVDQYSNYEVPPGLHVNGKLTLGENIADNGGLRLAYRAYKKW
LKENGPELPGLEGFTPEQLFFLSFAQVWCSKYRPEALRQLLLTDPHSPGKFRVNGPLSNSPEFAEAFNCP
PGSPMNPEKKCR
>gnl|CDD|176450 cd08663, DAP_dppA_1, Peptidase M55, D-aminopeptidase dipeptide-binding protein family. M55 Peptidase, D-Aminopeptidase dipeptide-binding protein (dppA; DAP dppA; EC 3.4.11.-) domain: Peptide transport systems are found in many bacterial species and generally function to accumulate intact peptides in the cell, where they are hydrolyzed. The dipeptide-binding protein (dppA) of Bacillus subtilis belongs to the dipeptide ABC transport (dpp) operon expressed early during sporulation. It is a binuclear zinc-dependent, D-specific aminopeptidase. The biologically active enzyme is a homodecamer with active sites buried in its channel. These self-compartmentalizing proteases are characterized by a SXDXEG motif. D-Ala-D-Ala and D-Ala-Gly-Gly are the preferred substrates. Bacillus subtilis dppA is thought to function as an adaptation to nutrient deficiency; hydrolysis of its substrate releases D-Ala which can be used subsequently as metabolic fuel. This family also contains a number of uncharacterized putative peptidases
MKIYISADMEGVTGVVSPEQVRPGGREYERARRLMTDEVNAAIEGALEAGATEVLVNDSHGSMRNLLPED
LDPRARLISGSPKPLGMMEGLDEGFDAALFVGYHARAGTPPGVLSHTYSGGAVRDVRLNGREVGETGLNA
AVAGEYGVPVVLVTGDDAACAEARELGPGVETVAVKEAIGRFAARCLPPAEARALIREAAAEAVRRLGKV
KPLTPPGPYTLEIEFANTAQADLAALVPGVERIGGRTVRFTADDMAEAYRAFRAML
>gnl|CDD|176485 cd08664, APC10-HERC2, APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2). This model represents the APC10/DOC1 domain present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including a zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT (Homologous to the E6-AP Carboxyl Terminus) domain. The APC10/DOC1 domain of HERC2 is a homolog of the APC10 subunit and the DOC1 domain present in E3 ubiquitin ligases which mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. As suggested by structural relationships between HERC2 and other proteins such as HERC1, the proposed role for HERC2 in protein trafficking and degradation pathways is consistent with observations that mutations in HERC2 lead to neuromuscular secretory vesicle and sperm acrosome defects, other developmental abnormalities, and juvenile lethality of jdf2 mice. Recent studies have shown that the protein complex, HERC2-RNF8, coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes
GKPGKYHRNDPELNAGEGDLIDDWSRCVRSLTVSSNENQAKRLIDGSGSYWQSSGSQGKHWIRLELHPDV
LIHSLKIIVDPADSSYMPSLVVVSGGDSLNSLKELKTINVNATDTLVTLLQDVKEYYRYIEIAIKQCRNN
GIDCKIHGLNII
>gnl|CDD|176486 cd08665, APC10-CUL7, APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that mediates substrate ubiquitination. This model represents the APC10/DOC1 domain present in CUL7, a subunit of the SCF-ROC1-like E3 Ubiquitin (Ub) ligase complex, which mediates substrate ubiquitination (or ubiquitylation), and is a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling the SCF-ROC1-like E3 Ub ligase complex consisting of the adapter protein Skp1, CUL7, the WD40 repeat-containing F-box Fbw8 (also known as Fbx29), and ROC1 (RING-box protein 1). CUL7 is a large protein with a C-terminal cullin domain that binds ROC1 and additional domains, including an APC10/DOC1 domain. While the Fbw8 protein is responsible for substrate protein recognition, the ROC1 RING domain recruits an Ub-charged E2 Ub-conjugating enzyme for substrate ubiquitination. It remains to be determined how CUL7 binds to the Skp1-Fbw8 heterodimer. The CUL7 E3 Ub ligase has been implicated in the proteasomal degradation of the cellular proteins, cyclin D1, an important regulator of the G1 to S-phase cell cycle progression, and insulin receptor substrate 1, a critical component of the signaling pathways downstream of the insulin and insulin-like growth factor 1 receptor. CUL7 appears to be an important regulator of placental development. Germ line mutations of CUL7 are linked to 3-M syndrome and Yakuts short stature syndrome
DKCWEKVEVSSNPHRANKLTDGNPKTYWESNGSTGSHYINIHMHRGVVIRQLYMLVASEDSSYMPARVVV
LGGDSPSCITTELNAVNVSPTASRVVLLENMTRFWPIIQIRIKRCQQGGIDTRVRGLEILG
>gnl|CDD|176487 cd08666, APC10-HECTD3, APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ubiquitination. This model represents the APC10/DOC1 domain present in HECTD3, a HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein. HECT E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), and are a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. They also regulate the trafficking of many receptors, channels, transporters and viral proteins. HECTD3 (HECT domain-containing protein3) contains a C-terminal HECT domain with the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain, which is responsible for substrate recognition and binding. HECTD3 specifically recognizes the Trio-binding protein, Tara (Trio-associated repeat on actin), implicated in regulating actin cytoskeletal, cell motility and cell growth. Tara also binds to TRF1 and may participate in telomere maintenance and/or mitotic regulation through interacting with TRF1. HECTD3 interacts with and promotes the ubiquitination of Syntaxin 8, an endosomal syntaxin proposed to mediate distinct steps of endosomal protein trafficking. HECTD3-mediated Syntaxin 8 degradation has been suggested to contribute to the pathophysiology of neurodegenerative diseases
GSVKQYVESIEVSSYTDDFNVSCLTDGDPDTYWESDGSQGQHWIRLHMKKGTIIKKLLLTVDATDDNYMP
KRVAVYGGEGDNLKKLNDVSIDETLIGDVCILEDMTTHLPVIEIRIKECKDEGIDVRIRGIKIK
>gnl|CDD|176488 cd08667, APC10-ZZEF1, APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing protein 1 (ZZEF1) and homologs. This model represents the APC10/DOC1-like domain present in the uncharacterized Zinc finger ZZ-type and EF-hand domain-containing protein 1 (ZZEF1) of Mus musculus. Members of this family contain EF-hand, APC10, CUB, and zinc finger ZZ-type domains. ZZEF1-like APC10 domains are homologous to the APC10 subunit/DOC1 domains present in E3 ubiquitin ligases, which mediate substrate ubiquitination (or ubiquitylation), and are components of the ubiquitin-26S proteasome pathway for selective proteolytic degradation
TKCYAYIEVSSNSADIDRMTDGETSTYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTV
SVGRSASSLQEVRDVHIPSNVTGYVTLLENANISYLVVQINIKRCHSDGCDTRIHGLKTIG
>gnl|CDD|176571 cd08674, Cdt1_m, The middle winged helix fold of replication licensing factor Cdt1 binds geminin to inhibit binding of the MCM complex to origins of replication and DNA. Cdt1 is a replication licensing factor in eukaryotes that recruits the Minichromosome Maintenance Complex (MCM2-7) to the origin recognition complex (ORC). The Cdt1 protein is divided into three regions based on sequence comparison and biochemical analyses: the N-terminal region (Cdt1_n) binds DNA in a sequence-, strand-, and conformation-independent manner; the middle winged helix fold (Cdt1_m) binds geminin to inhibit both binding of the MCM complex to origins of replication and DNA; and the C-terminal region (Cdt1_c) is essential for Cdt1 activity and directly interacts with the MCM2-7 helicase. Precise duplication of chromosomal DNA is required for genomic stability during replication. Assembly of replication factors to start DNA replication in eukaryotes must occur only once per cell cycle. To form a pre-replicative complex on replication origins in the G phase, ORC first binds origin DNA and triggers the binding of Cdc6 and Cdt1. These two factors recruit a putative replicative helicase and the MCM2-7. The MCM2-7 complex promotes the unwinding of DNA origins, and the binding of additional factors to initiate the DNA replication in S-phase. Cdt1 is present during G1 and early S phase of the cell cycle and degraded during the late S, G2, and M phases. The winged helix fold structure of Cdt1_m is similar to the structures of Cdt1_c and other archaeal homologues of the eukaryotic replication initiator, without apparent sequence similarity
PAYQRYHSLASSVRPSLKLPEKYEVLAELFRSLDTIVRLLFNRKETCTFDKLKPAVERMTRRRFSEKHLA
QIKHIYPEAYTLRQEKNHDEGSLCKKPDYQLTLEPNLVEGLELGGSPKLSESRLLARRQVFRSRLLDFVK
AHHEEFLISLDPPPPIPDDKLTRWHPKFDLESVPDIEPAELPQPP
>gnl|CDD|176057 cd08675, C2B_RasGAP, C2 domain second repeat of Ras GTPase activating proteins (GAPs). RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology
LSVRVLECRDLALKSNGTCDPFARVTLNYSSKTDTKRTKVKKKTNNPRFDEAFYFELTIGFSYEKKSFKV
EEEDLEKSELRVELWHASMVSGDDFLGEVRIPLQGLQQAGSHQAWYFLQPREAPGTRSSNDGSLGSL
>gnl|CDD|176058 cd08676, C2A_Munc13-like, C2 domain first repeat in Munc13 (mammalian uncoordinated)-like proteins. C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology
YAQQAFGVSPEEHEALLERVREAEPPIFVLKVTVIEAKGLLAKDVNGFSDPYCMLGIVPASRERNSEKSK
KRKSHRKKAVLKDTVPAKSIKVTEVKPQTLNPVWNETFRFEVEDVSNDQLHLDIWDHDDDFLGCVNIPLK
DLPSCGLDSWFKL
>gnl|CDD|176059 cd08677, C2A_Synaptotagmin-13, C2 domain. Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 13, a member of class 6 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmins 8 and 12, does not have any consensus Ca2+ binding sites. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This CD contains the first C2 repeat, C2A, and has a type-I topology
PKLHYSLSYDKQKAELHVNILEAENISVDAGCECYISGCVSVSEGQKEAQTALKKLALHTQWEEELVFPL
PEEESLDGTLTLTLRCCDRFSRHSTLGELRLKLADVSMMLGAAQWVDL
>gnl|CDD|176060 cd08678, C2_C21orf25-like, C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein. The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
LLVKNIKANGLSEAAGSSNPYCVLEMDEPPQKYQSSTQKNTSNPFWDEHFLFELSPNSKELLFEVYDNGK
KSDSKFLGLAIVPFDELRKNPSGRQIFPLQGRPYEGDSVSGSITVEFLFMEPAELP
>gnl|CDD|176061 cd08679, C2_DOCK180_related, C2 domains found in Dedicator Of CytoKinesis 1 (DOCK 180) and related proteins. Dock180 was first identified as an 180kd proto-oncogene product c-Crk-interacting protein involved in actin cytoskeletal changes. It is now known that it has Rac-specific GEF activity, but lacks the conventional Dbl homology (DH) domain. There are 10 additional related proteins that can be divided into four classes based on sequence similarity and domain organization: Dock-A which includes Dock180/Dock1, Dock2, and Dock5; Dock-B which includes Dock3/MOCA (modifier of cell adhesion) and Dock4; Dock-C which includes Dock6/Zir1, Dock7/Zir2, and Dock8/Zir3; and Dock-D, which includes Dock9/Zizimin1, Dock10/Zizimin3, and Dock11/Zizimin2/ACG (activated Cdc42-associated GEF). Most of members of classes Dock-A and Dock-B are the GEFs specific for Rac. Those of Dock-D are Cdc42-specific GEFs while those of Dock-C are the GEFs for both. All Dock180-related proteins have two common homology domains: the C2 domain (AKA Dock homology region (DHR)-1, CED-5, Dock180, MBC-zizimin homology (CZH) 1) and the DHR-2 (AKA CZH2, or Docker). DHR-2 has the catalytic activity for Rac and/or Cdc42, but is structurally unrelated to the DH domain. The C2/DHR-1 domains of Dock180 and Dock4 have been shown to bind phosphatidylinositol-3, 4, 5-triphosphate (PtdIns(3,4,5)P3). The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
LRNDLYVYPQSGELSKAKSKGRNIEITVEVRDDDGDIIEPCISAPGSGSELRSEYTSVVYYHKNPVFNDE
IKIQLPADLTPQHHLLFTFYHVSSKKKQGDKEETPFGYAFLPLMDKDGAFIKDGDHTLPVYKYDKRPDVG
PSGYLSLPSTLANGKSSKDTFKIKTRLCSTILTQDKSL
>gnl|CDD|176062 cd08680, C2_Kibra, C2 domain found in Human protein Kibra. Kibra is thought to be a regulator of the Salvador (Sav)/Warts (Wts)/Hippo (Hpo) (SWH) signaling network, which limits tissue growth by inhibiting cell proliferation and promoting apoptosis. The core of the pathway consists of a MST and LATS family kinase cascade that ultimately phosphorylates and inactivates the YAP/Yorkie (Yki) transcription coactivator. The FERM domain proteins Merlin (Mer) and Expanded (Ex) are part of the upstream regulation controlling pathway mechanism. Kibra colocalizes and associates with Mer and Ex and is thought to transduce an extracellular signal via the SWH network. The apical scaffold machinery that contains Hpo, Wts, and Ex recruits Yki to the apical membrane facilitating its inhibitory phosphorlyation by Wts. Since Kibra associates with Ex and is apically located it is hypothesized that KIBRA is part of the scaffold, helps in the Hpo/Wts complex, and helps recruit Yki for inactivation that promotes SWH pathway activity. Kibra contains two amino-terminal WW domains, an internal C2-like domain, and a carboxy-terminal glutamic acid-rich stretch. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
AQVQIGLRYDSGDSSLVISVEQLRNLSALSIPENSKVYVRVALLPCSSSTSCLFRTKALEDQDKPVFNEV
FRVPISSTKLYQKTLQVDVCSVGPDQQEECLGGAQISLADFESSEEMSTKWYNL
>gnl|CDD|176063 cd08681, C2_fungal_Inn1p-like, C2 domain found in fungal Ingression 1 (Inn1) proteins. Saccharomyces cerevisiae Inn1 associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis. The C2 domain of Inn1, located at the N-terminus, is required for ingression of the plasma membrane. The C-terminus is relatively unstructured and contains eight PXXP motifs that are thought to mediate interaction of Inn1 with other proteins with SH3 domains in the cytokinesis proteins Hof1 (an F-BAR protein) and Cyk3 (whose overexpression can restore primary septum formation in Inn1Delta cells) as well as recruiting Inn1 to the bud-neck by binding to Cyk3. Inn1 and Cyk3 appear to cooperate in activating chitin synthase Chs2 for primary septum formation, which allows coordination of actomyosin ring contraction with ingression of the cleavage furrow. It is thought that the C2 domain of Inn1 helps to preserve the link between the actomyosin ring and the plasma membrane, contributing both to membrane ingression, as well as to stability of the contracting ring. Additionally, Inn1 might induce curvature of the plasma membrane adjacent to the contracting ring, thereby promoting ingression of the membrane. It has been shown that the C2 domain of human synaptotagmin induces curvature in target membranes and thereby contributes to fusion of these membranes with synaptic vesicles. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
GTLVVVVLKARNLPNKRKLDKQDPYCVLRIGGVTKKTKTDFRGGQHPEWDEELRFEITEDKKPILKVAVF
DDDKRKPDLIGDTEVDLSPALKEGEFDDWYELTLKGRYAGEVYLELTF
>gnl|CDD|176064 cd08682, C2_Rab11-FIP_classI, C2 domain found in Rab11-family interacting proteins (FIP) class I. Rab GTPases recruit various effector proteins to organelles and vesicles. Rab11-family interacting proteins (FIPs) are involved in mediating the role of Rab11. FIPs can be divided into three classes: class I FIPs (Rip11a, Rip11b, RCP, and FIP2) which contain a C2 domain after N-terminus of the protein, class II FIPs (FIP3 and FIP4) which contain two EF-hands and a proline rich region, and class III FIPs (FIP1) which exhibits no homology to known protein domains. All FIP proteins contain a highly conserved, 20-amino acid motif at the C-terminus of the protein, known as Rab11/25 binding domain (RBD). Class I FIPs are thought to bind to endocytic membranes via their C2 domain, which interacts directly with phospholipids. Class II FIPs do not have any membrane binding domains leaving much to speculate about the mechanism involving FIP3 and FIP4 interactions with endocytic membranes. The members in this CD are class I FIPs. The exact function of the Rab11 and FIP interaction is unknown, but there is speculation that it involves the role of forming a targeting complex that recruits a group of proteins involved in membrane transport to organelles. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
VQVTVLQARGLLCKGKSGTNDAYVIIQLGKEKYSTSVKEKTTSPVWKEECSFELPGLLSGNGNRATLQLT
VMHRNLLGLDKFLGQVSIPLNDLDEDKGRRRTRWFKLESKPGKDDKERGEIEVDIQ
>gnl|CDD|176065 cd08683, C2_C2cd3, C2 domain found in C2 calcium-dependent domain containing 3 (C2cd3) proteins. C2cd3 is a novel C2 domain-containing protein specific to vertebrates. C2cd3 functions in regulator of cilia formation, Hedgehog signaling, and mouse embryonic development. Mutations in C2cd3 mice resulted in lethality in some cases and exencephaly, a twisted body axis, and pericardial edema in others. The presence of calcium-dependent lipid-binding domains in C2cd3 suggests a potential role in vesicular transport. C2cd3 is also an interesting candidate for ciliopathy because of its orthology to certain cilia-related genetic disease loci on chromosome. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
LSVQIHRASGLQAAARALAEQDPSLQYSATVGVNSYVTIHLSFLPEKELRRTRTVARSFCPEFNHHVEFP
CNLVVQRNSGEAISLAELLESAEIILEVWHRNPKSAGDTIKIETSGDILLGTVKIPLRDLLTKRSGITGW
YPI
>gnl|CDD|176066 cd08684, C2A_Tac2-N, C2 domain first repeat found in Tac2-N (Tandem C2 protein in Nucleus). Tac2-N contains two C2 domains and a short C-terminus including a WHXL motif, which are key in stabilizing transport vesicles to the plasma membrane by binding to a plasma membrane. However unlike the usual carboxyl-terminal-type (C-type) tandem C2 proteins, it lacks a transmembrane domain, a Slp-homology domain, and a Munc13-1-interacting domain. Homology search analysis indicate that no known protein motifs are located in its N-terminus, making Tac2-N a novel class of Ca2+-independent, C-type tandem C2 proteins. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
IWITVLKCKDLSWPSSCGENPTIYIKGILTLPKPVHFKSSAKEGSNDIEFMETFVFAIKLQNLQTVRLVF
KIQTQTPRKRTIGECSLSLRTLSTQETDHWLEI
>gnl|CDD|176067 cd08685, C2_RGS-like, C2 domain of the Regulator Of G-Protein Signaling (RGS) family. This CD contains members of the regulator of G-protein signaling (RGS) family. RGS is a GTPase activating protein which inhibits G-protein mediated signal transduction. The protein is largely cytosolic, but G-protein activation leads to translocation of this protein to the plasma membrane. A nuclear form of this protein has also been described, but its sequence has not been identified. There are multiple alternatively spliced transcript variants in this family with some members having additional domains (ex. PDZ and RGS) downstream of the C2 domain. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
GQLKLSIEGQNRKLTLHVLEAKGLRSTNSGTCNSYVKISLSPDKEVRFRQKTSTVPDSANPLFHETFSFD
VNERDYQKRLLVTVWNKLSKSRDSGLLGCMSFGVKSIVNQKEISGWYYL
>gnl|CDD|176068 cd08686, C2_ABR, C2 domain in the Active BCR (Breakpoint cluster region) Related protein. The ABR protein is similar to the breakpoint cluster region protein. It has homology to guanine nucleotide exchange proteins and GTPase-activating proteins (GAPs). ABR is expressed primarily in the brain, but also includes non-neuronal tissues such as the heart. It has been associated with human diseases such as Miller-Dieker syndrome in which mental retardation and malformations of the heart are present. ABR contains a RhoGEF domain and a PH-like domain upstream of its C2 domain and a RhoGAP domain downstream of this domain. A few members also contain a Bcr-Abl oncoprotein oligomerization domain at the very N-terminal end. Splice variants of ABR have been identified. ABR is found in a wide variety of organisms including chimpanzee, dog, mouse, rat, fruit fly, and mosquito. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
LNVIVHSAQGFKQSANLYCTLEVDSFGYFVKKAKTRVCRDTTEPNWNEEFEIELEGSQTLRILCYEKCYS
KVKLDGEGTDAIMGKGQIQLDPQSLQTKKWQEKVISMNGITVNLSIKF
>gnl|CDD|176069 cd08687, C2_PKN-like, C2 domain in Protein kinase C-like (PKN) proteins. PKN is a lipid-activated serine/threonine kinase. It is a member of the protein kinase C (PKC) superfamily, but lacks a C1 domain. There are at least 3 different isoforms of PKN (PRK1/PKNalpha/PAK1; PKNbeta, and PRK2/PAK2/PKNgamma). The C-terminal region contains the Ser/Thr type protein kinase domain, while the N-terminal region of PKN contains three antiparallel coiled-coil (ACC) finger domains which are relatively rich in charged residues and contain a leucine zipper-like sequence. These domains binds to the small GTPase RhoA. Following these domains is a C2-like domain. Its C-terminal part functions as an auto-inhibitory region. PKNs are not activated by classical PKC activators such as diacylglycerol, phorbol ester or Ca2+, but instead are activated by phospholipids and unsaturated fatty acids. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
LEVRLMGCSEVSAVLKLDNTVVGQTQWKPKSNQAWDQSFTLELERSRELEIAVYWRDWRSLCAVKFLKLE
DERHEVQLDMEPQLCLVAELTFATWVRL
>gnl|CDD|176070 cd08688, C2_KIAA0528-like, C2 domain found in the Human KIAA0528 cDNA clone. The members of this CD are named after the Human KIAA0528 cDNA clone. All members here contain a single C2 repeat. No other information on this protein is currently known. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
LKVRVVAARDLPVMDRSSDLTDAFVEVKFGSTTYKTDVVKKSLNPVWNSEWFRFEVDDEELQDEPLQIRV
MDHDTYSANDAIGKVYIDLNPLLLKDSVSQISGWFPIYDT
>gnl|CDD|176071 cd08689, C2_fungal_Pkc1p, C2 domain found in protein kinase C (Pkc1p) in Saccharomyces cerevisiae. This family is named after the protein kinase C in Saccharomyces cerevisiae, Pkc1p. Protein kinase C is a member of a family of Ser/Thr phosphotransferases that are involved in many cellular signaling pathways. PKC has two antiparallel coiled-coiled regions (ACC finger domain) (AKA PKC homology region 1 (HR1)/ Rho binding domain) upstream of the C2 domain and two C1 domains downstream. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains, like those of PKC, are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
LTITITSARDVDHIASPRFSKRPETYVSIKVEDVERARTKPSRNDRWNEDFEIPVEKNNEEEVIVYDKGG
DQPVPVGLLWLRLSDIAEEIRKKKVGQELGATGWVSASN
>gnl|CDD|176072 cd08690, C2_Freud-1, C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1). Freud-1 is a novel calcium-regulated repressor that negatively regulates basal 5-HT1A receptor expression in neurons. It may also play a role in the altered regulation of 5-HT1A receptors associated with anxiety or major depression. Freud-1 contains two DM-14 basic repeats, a helix-loop-helix DNA binding domain, and a C2 domain. The Freud-1 C2 domain is thought to be calcium insensitive and it lacks several acidic residues that mediate calcium binding of the PKC C2 domain. In addition, it contains a poly-basic insert that is not present in calcium-dependent C2 domains and may function as a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology
DSSIELTIVRCIGIPLPSGWNPKDLDTYVKFEFPYPNEEPQSGKTSTIKDTNSPEYNESFKLNINRKHRS
FQRVFKRHGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPL
TGKQLEEITEKWLVI
>gnl|CDD|176073 cd08691, C2_NEDL1-like, C2 domain present in NEDL1 (NEDD4-like ubiquitin protein ligase-1). NEDL1 (AKA HECW1(HECT, C2 and WW domain containing E3 ubiquitin protein ligase 1)) is a newly identified HECT-type E3 ubiquitin protein ligase highly expressed in favorable neuroblastomas. In vertebrates it is found primarily in neuronal tissues, including the spinal cord. NEDL1 is thought to normally function in the quality control of cellular proteins by eliminating misfolded proteins. This is thought to be accomplished via a mechanism analogous to that of ER-associated degradation by forming tight complexes and aggregating misfolded proteins that have escaped ubiquitin-mediated degradation. NEDL1, is composed of a C2 domain, two WW domains, and a ubiquitin ligase Hect domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
LSFSLSGLQARNLKKGMFFNPDPYVKISIQPGKRHIFPALPHHGQECRTSIVENTINPVWHREQFVFVGL
PTDVLEIEVKDKFAKSRPIIRRFLGKLSIPVQRLLERHAIGDQELSYTLGRRTPTDHVSGQLTFRFE
>gnl|CDD|176074 cd08692, C2B_Tac2-N, C2 domain second repeat found in Tac2-N (Tandem C2 protein in Nucleus). Tac2-N contains two C2 domains and a short C-terminus including a WHXL motif, which are key in stabilizing transport vesicles to the plasma membrane by binding to a plasma membrane. However unlike the usual carboxyl-terminal-type (C-type) tandem C2 proteins, it lacks a transmembrane domain, a Slp-homology domain, and a Munc13-1-interacting domain. Homology search analysis indicate that no known protein motifs are located in its N-terminus, making Tac2-N a novel class of Ca2+-independent, C-type tandem C2 proteins. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
AELQLGTCFQAVNSRIQLQILEAQNLPSSSTPLTLSFFVKVGMFSTGGLLYKKKTRLVKSSNGQVKWGET
MIFPVTQQEHGIQFLIKLYSRSSVRRKHFLGQVWISSDSSSSEAVEQWKDTIANPEKVVTKWHSL
>gnl|CDD|176075 cd08693, C2_PI3K_class_I_beta_delta, C2 domain present in class I beta and delta phosphatidylinositol 3-kinases (PI3Ks). PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. The members here are class I, beta and delta isoforms of PI3Ks and contain both a Ras-binding domain and a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-I topology
KSLWDIEEKFSITLHKISNLNAAERTMKVGVQAGLFHGGESLCKTVKTSEVSGKNDPVWNETLEFDINVC
DLPRMARLCFAIYEVSKKAKGKRSRKNQTKKKKKKDDNPIAWVNTMVFDYKGQLKTGDHTLYMWTYAEDQ
SEDLLNPLGTVESNPNTESATALHISFPEYKPE
>gnl|CDD|176076 cd08694, C2_Dock-A, C2 domains found in Dedicator Of CytoKinesis (Dock) class A proteins. Dock-A is one of 4 classes of Dock family proteins. The members here include: Dock180/Dock1, Dock2, and Dock5. Most of these members have been shown to be GEFs specific for Rac. Dock5 has not been well characterized to date, but most likely also is a GEF specific for Rac. In addition to the C2 domain (AKA Dock homology region (DHR)-1, CED-5, Dock180, MBC-zizimin homology (CZH) 1) and the DHR-2 (AKA CZH2, or Docker), which all Dock180-related proteins have, Dock-A members contain a proline-rich region and a SH3 domain upstream of the C2 domain. DHR-2 has the catalytic activity for Rac and/or Cdc42, but is structurally unrelated to the DH domain. The C2/DHR-1 domains of Dock180 and Dock4 have been shown to bind phosphatidylinositol-3, 4, 5-triphosphate (PtdIns(3,4,5)P3). The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
VRNDLYLTLVQGDFDKGSKTSDKNVEVTVSVCNEDGKIIPGVISLGAGEEPIDEYKSVIYYQVDKPKWFE
TFKVAIPIEDFKSSHLRFTFKHRSSNEAKDKSEKPFALSFVKLMQENGTTLTDGEHDLIVYKVDAKKKLE
DAKAYLSLPSTRAELEARKSSPSGSASNLGLSLSSKDSFQISTLVCSTKLTQNVDL
>gnl|CDD|176077 cd08695, C2_Dock-B, C2 domains found in Dedicator Of CytoKinesis (Dock) class B proteins. Dock-B is one of 4 classes of Dock family proteins. The members here include: Dock3/MOCA (modifier of cell adhesion) and Dock4. Most of these members have been shown to be GEFs specific for Rac, although Dock4 has also been shown to interact indirectly with the Ras family GTPase Rap1, probably through Rap regulatory proteins. In addition to the C2 domain (AKA Dock homology region (DHR)-1, CED-5, Dock180, MBC-zizimin homology (CZH) 1) and the DHR-2 (AKA CZH2, or Docker), which all Dock180-related proteins have, Dock-B members contain a SH3 domain upstream of the C2 domain and a proline-rich region downstream. DHR-2 has the catalytic activity for Rac and/or Cdc42, but is structurally unrelated to the DH domain. The C2/DHR-1 domains of Dock180 and Dock4 have been shown to bind phosphatidylinositol-3, 4, 5-triphosphate (PtdIns(3,4,5)P3). The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
VRNDLYLTLERGEFEKGGKSTAKNIEVTMVVLDADGQVLKDCISLGSGEPPCSEYRSFVLYHNNSPRWNE
TIKLPIPIDKFRGSHLRFEFRHCSTKDKGEKKLFGFSFVPLMREDGTTLPDGSHELYVYKCDENATFLDP
ALYLGLPCSKEDFQGCPNSPSPLFSRSSKESFWIRTLLCSTKLTQNVDL
>gnl|CDD|176078 cd08696, C2_Dock-C, C2 domains found in Dedicator Of CytoKinesis (Dock) class C proteins. Dock-C is one of 4 classes of Dock family proteins. The members here include: Dock6/Zir1, Dock7/Zir2, and Dock8/Zir3. Dock-C members are GEFs for both Rac and Cdc42. In addition to the C2 domain (AKA Dock homology region (DHR)-1, CED-5, Dock180, MBC-zizimin homology (CZH) 1) and the DHR-2 (AKA CZH2, or Docker), which all Dock180-related proteins have, Dock-C members contain a functionally uncharacterized domain upstream of the C2 domain. DHR-2 has the catalytic activity for Rac and/or Cdc42, but is structurally unrelated to the DH domain. The C2/DHR-1 domains of Dock180 and Dock4 have been shown to bind phosphatidylinositol-3, 4, 5-triphosphate (PtdIns(3,4,5)P3). The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
YRNLLYVYPQSLNFSNRLGSARNIAVKVQLMSGEDESQALPVIFKGSSPEEFLTEAYTAVTYHNKSPDFY
DEIKIKLPADLTDNHHLLFTFYHISCQKKQEGGSVETPIGYTWLPLLRNGRLQSGEFNLPVSLEKPPSNY
SPDSPEVKLPGTKWVDNHKGVFSVSVEAVSSVHTQDSYL
>gnl|CDD|176079 cd08697, C2_Dock-D, C2 domains found in Dedicator Of CytoKinesis (Dock) class C proteins. Dock-D is one of 4 classes of Dock family proteins. The members here include: Dock9/Zizimin1, Dock10/Zizimin3, and Dock11/Zizimin2/ACG (activated Cdc42-associated GEF). Dock-D are Cdc42-specific GEFs. In addition to the C2 domain (AKA Dock homology region (DHR)-1, CED-5, Dock180, MBC-zizimin homology (CZH) 1) and the DHR-2 (AKA CZH2, or Docker), which all Dock180-related proteins have, Dock-D members contain a functionally uncharacterized domain and a PH domain upstream of the C2 domain. DHR-2 has the catalytic activity for Rac and/or Cdc42, but is structurally unrelated to the DH domain. The C2/DHR-1 domains of Dock180 and Dock4 have been shown to bind phosphatidylinositol-3, 4, 5-triphosphate (PtdIns(3,4,5)P3). The PH domain broadly binds to phospholipids and is thought to be involved in targeting the plasma membrane. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions
YKNHLYVYPLHLKYDSQKTFAKARNIAVCIEFRDSDEEDAKPLKCIYYGPGGGFTTSAYAAVLHHNQNPE
FYDEIKIELPTQLHEKHHLLFTFYHVSCDINKKGKKKDGVETPVGYAWLPLLKDKGRLNSEEQTPPVANL
LPNYPDGYLSIQPHGPEVKWVDGGKPLFKVSTHLVSTVYTQDQHL
>gnl|CDD|381627 cd08698, TGF_beta_SF, transforming growth factor beta (TGF-beta) like domain found in TGF-beta superfamily. TGF-beta superfamily consists of a large group of cell regulatory proteins, such as TFG-betas, Nodal, Activins/Inhibins, glial cell-line-derived neurotrophic factor (GDNF) family of ligands, bone morphogenetic proteins (BMPs), and growth and differentiation factors (GDFs). They play important roles in developmental and physiological processes in a variety of species, including invertebrates as well as vertebrates, through specific receptor complexes that are composed of type I and type II serine/threonine receptor kinases. The receptor kinases subsequently activate Smad proteins, which then propagate the signals into the nucleus to regulate target gene expression. Proteins from the TGF-beta superfamily are only active as homo- or heterodimer
CCKQPLYVNFKDLGGLNWIIAPSGFTANYCRGSCNSESSATTNHTKLLQWSRTRRHTPREELKPCCVPTS
YEPLSILYYDNNGTVVETLLPNLIVTECGC
>gnl|CDD|187728 cd08700, FMT_C_OzmH_like, C-terminal subdomain of the Formyltransferase-like domain found in OzmH-like proteins. Domain found in OzmH-like proteins with similarity to the C-terminal domain of Formyltransferase. OzmH is one of the proteins involved in the synthesis of Oxazolomycin (OZM), which is a hybrid peptide-polyketide antibiotic that exhibits potent antitumor and antiviral activities. OzmH is a multi-domain protein consisting of a formyl transferase domain, a flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a phosphopantetheine (PP)-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins
AGGVLDFTRPAAELSALVRALDFGGYWNPLCVAKILLADRVLLVGKAEVLAVSSGGAPGTVLAVDADGWT
VATGDGAVRLSGLTDLDGAAVDLAALAQAG
>gnl|CDD|187729 cd08701, FMT_C_HypX, C-terminal subdomain of the Formyltransferase-like domain found in HypX-like proteins. Domain found in HypX-like proteins with similarity to the C-terminal domain of Formyltransferase. HypX is involved in the maturation process of active [NiFe] hydrogenase [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalents under aerobic and anaerobic conditions [NiFe] hydrogenases consist of a large and a small subunit. The large subunit contains the [NiFe] active site but is synthesized as a precursor without the [NiFe] active site. This precursor undergoes a complex post-translational maturation process that requires the presence of a number of accessory proteins. HypX has been shown to be involved in this maturation process and have been proposed to participate in the generation and transport of the CO and CN ligands. However, HypX is not present in all hydrogen-metabolizing bacteria. Furthermore, hypX deletion mutants have a reduced but detectable level of hydrogenase activity. Thus, HypX might not be the determining factor in the maturation process. Members of this group have an N-terminal formyl transferase domain and a C-terminal enoyl-CoA hydratase/isomerase domain
ADRRIDWEKDSAEEILRKIRAADSQPGVLDELFGTEVYLFGAHPEEALPDAGKPGTILAQRDGAVLVATG
DGAVWISHLRRPKAPESIKLPATYVL
>gnl|CDD|187730 cd08702, Arna_FMT_C, C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with 4-amino-4-deoxy-l-arabinose. Domain found in ArnA with similarity to the C-terminal domain of Formyltransferase. ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal domain of ArnA is a dehydrogenase domain that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the N-terminal domain is a formyltransferase domain that catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the C-terminal subdomain of the formyltransferase domain, downstream of the N-terminal subdomain containing the catalytic center. ArnA forms a hexameric structure (a dimer of trimers), in which the dehydrogenase domains are arranged at the center with the transformylase domains on the outside of the complex
EDGLIDWRMSAREIYNLVRAVTKPYPGAFTFVGGQKIKIWKARPVDDAFYNGEPGKVLSVDGDPLIVACG
DGALEILEAELDGGLPLAGEQL
>gnl|CDD|187731 cd08703, FDH_Hydrolase_C, The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase. The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding
KELAKINWDQTAEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKPPGGEVEVEGLERPGIVHKNG
LLITGSDGKMVNVKRLQFEDGKMIPASKYG
>gnl|CDD|187732 cd08704, Met_tRNA_FMT_C, C-terminal domain of Formyltransferase and other enzymes. C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases (for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding
EEGRIDWSKSAEEIHNLIRALNPWPGAYTTLNGKRLKILKAEVLEESGEAAPGTILAVDKKGLLVACGDG
ALEILELQPEGKKRMSA
>gnl|CDD|188660 cd08705, RGS_R7-like, Regulator of G protein signaling (RGS) domain found in the R7 subfamily of proteins. The RGS (Regulator of G-protein Signaling) domain is an essential part of the R7 (Neuronal RGS) protein subfamily of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The R7 subfamily includes RGS6, RGS7, RGS9, and RGS11, all of which, in humans, are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes. In addition, R7 proteins were found to bind many other proteins outside of the G protein signaling pathways including: m-opioid receptor, beta-arrestin, alpha-actinin-2, NMDAR, polycystin, spinophilin, guanylyl cyclase, among others
RVKRWGFSFSELLKDPVGREQFLKFLEKEFSGENLRFWEACQDLKYGPQSQVPEKVQEIYQEFLAPGAPS
WINIDSKTMEITLKNLKDPHRYTFDAAQEHIYMLMKKDSYPRFLRSDIYKE
>gnl|CDD|188661 cd08706, RGS_R12-like, Regulator of G protein signaling (RGS) domain found in the R12 subfamily of proteins. The RGS (Regulator of G-protein Signaling) domain is an essential part of the R12 (Neuronal RGS) protein subfamily of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play a critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of G-protein signaling, controlled by RGS domain, accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP that results in reassociation of the alpha-subunit with the beta-gamma-dimer and thereby inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The R12 RGS subfamily includes RGS10, RGS12 and RGS14 all of which are highly selective for G-alpha-i1 over G-alpha-q
FERLLQDPVGVKYFTEFLKKEFSEENILFWQACEKFKKIPDKKQLVQEAREIYDTFLSSKASSPVNIDSQ
AQLAEEMLEEPHPDMFQKQQLQIFNLMKFDSYSRFLKSPLYQQ
>gnl|CDD|188662 cd08707, RGS_Axin, Regulator of G protein signaling (RGS) domain found in the Axin protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the Axin protein. Axin is a member of the RA/RGS subfamily of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, and skeletal and muscle development. The RGS domain of Axin is specifically interacts with the heterotrimeric G-alpha12 protein, but not with closely related G-alpha13, and provides a unique tool to regulate G-alpha12-mediated signaling processes. The RGS domain of Axin also interacts with the tumor suppressor protein APC (Adenomatous Polyposis Coli) in order to control the cytoplasmic level of the proto-oncogene, beta-catenin
LHSLLDDQDGIELFRTYLEQEGCADLLDFWFACNGFRKMSDSEEKRSKLAKAIYRRYIKDNGIVSRQLKP
ATKSFIKECIKKQQLDPAMFDQAQTEIQTTMEENTYPSFLKSDIYLE
>gnl|CDD|188663 cd08708, RGS_FLBA, Regulator of G protein signaling (RGS) domain found in the FLBA (Fluffy Low BrlA) protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the FLBA (Fluffy Low BrlA) protein. FLBA is a member of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins play a critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of the G-protein signaling controlled by the RGS domain accelerates the GTPase activity of the alpha subunit by hydrolysis of GTP to GDP which results in reassociation of the alpha-subunit with the beta-gamma-dimer and thereby inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes. The RGS domain of the FLBA protein antagonizes G protein signaling to block proliferation and allow development. It is required for control of mycelial proliferation and activation of asexual sporulation in yeast
RLDKILKDPGLRYLFREHLEKEFCEENLSFYLEVKEFLKKMTILSKLLDFKSSQAADEDLDRESLAQAYH
IYNTYLAPGSPCELNIDHNLRNRITTIMTEKIVGEDDSMAESLQGVEALFEEAQNAVFKPLMAGDSVPKF
LKQPEYLG
>gnl|CDD|188664 cd08709, RGS_RGS2, Regulator of G protein signaling (RGS) domain found in the RGS2 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS2 protein. RGS2 is a member of R4/RGS subfamily of RGS family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. The RGS domain controls G-protein signaling by accelerating the GTPase activity of the G- alpha subunit which leads to G protein deactivation and promotes desensitization. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS2 plays important roles in the regulation of blood pressure and the pathogenesis of human hypertension, as well as in bone formation in osteoblasts. Outside of the GPCR pathway RGS2 interacts with calmodulin, beta- COP, tubulin, PKG1-alpha, and TRPV6
FDELLASKYGVAAFRAFLKSEFSEENIEFWLACEDFKKTKSPQKLTSKAKKIYTDFIEKEAPKEINIDFQ
TKTLIAQNIQEATSGCFTAAQKRVYSLMENNSYPRFLESEFYQE
>gnl|CDD|188665 cd08710, RGS_RGS16, Regulator of G protein signaling (RGS) domain found in the RGS16 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS16 protein. RGS16 is a member of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha subunits. The RGS domain controls G-protein signaling by accelerating the GTPase activity of the G-alpha subunit which leads to G protein deactivation and promotes desensitization. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS16 is a member of the R4/RGS subfamily and interacts with neuronal G-alpha0. RGS16 expression is upregulated by IL-17 of the NF-kappaB signaling pathway in autoimmune B cells
FDLLLNSKNGVAAFHAFLKTEFSEENLEFWLACEEFKKIRSATKLASRAHHIFEEFIRSEAPKEVNIDHE
TRELTRTNLQAATTSCFDVAQGKTRTLMEKDSYPRFLKSPAYRD
>gnl|CDD|188666 cd08711, RGS_RGS8, Regulator of G protein signaling (RGS) domain found in the RGS8 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS8 protein. RGS8 is a member of R4/RGS subfamily of RGS family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha subunits. The RGS domain controls G-protein signaling by accelerating the GTPase activity of the G-alpha subunit which leads to G protein deactivation and promotes desensitization. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS8 is involved in G-protein-gated potassium channels regulation and predominantly expressed in the brain. RGS8 also is selectively expressed in the hematopoietic system (NK cells)
STEEATRWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTRSTAKLVSKAHRIFEEFVDV
QAPREVNIDFQTREATRKNLQEPSLTCFDQAQGKVHSLMEKDSYPRFLRSKMYLD
>gnl|CDD|188667 cd08712, RGS_RGS18, Regulator of G protein signaling (RGS) domain found in the RGS18 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS18 protein. RGS18 is a member of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha subunits. The RGS domain controls G-protein signaling by accelerating the GTPase activity of the G-alpha subunit which leads to G protein deactivation and promotes desensitization. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS18 is a member of the R4/RGS subfamily and is expressed predominantly in osteoclasts where it acts as a negative regulator of the acidosis-induced osteoclastogenic OGR1/NFAT signaling pathway. RANKL (receptor activator of nuclear factor B ligand) stimulates osteoclastogenesis by inhibiting expression of RGS18
FDKLLSHKDGLEAFTRFLKTEFSEENIEFWIACEDYKKSKTPQQIHLKAKAIYEKFIQTDAPKEVNLDFH
TKEVTTNSIEQPTLTSFDAAQSRVYQLMEQDSYPRFLKSDIYLD
>gnl|CDD|188668 cd08713, RGS_RGS3, Regulator of G protein signaling (RGS) domain found in the RGS3 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS3 protein. RGS3 is a member of the R4/RGS subfamily of the RGS family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha subunits. The RGS domain controls G-protein signaling by accelerating the GTPase activity of the G-alpha subunit which leads to G protein deactivation and promotes desensitization. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes. RGS3 induces apoptosis when overexpressed and is involved in cell migration through interaction with the Ephrin receptor. RGS3 exits as several splice isoforms and interacts with neuroligin, estrogen receptor-alpha, and 14-3-3 outside of the GPCR pathways
LEKLLLHKYGLAVFRAFLQTEFSEENLEFWLACEEYKKIKSQSKMASRAKKIFAEYIAIQSCKEVNLDSY
TREHTKENLQNPTRGCFDLAQKRIYGLMEKDSYPRFLRSDLYQD
>gnl|CDD|188669 cd08714, RGS_RGS4, Regulator of G protein signaling (RGS) domain found in the RGS4 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS4 protein. RGS4 is a member of the R4/RGS subfamily of the RGS family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha subunits. The RGS domain controls G-protein signaling by accelerating the GTPase activity of the G-alpha subunit which leads to G protein deactivation and promotes desensitization. RGS4 is expressed widely in brain including prefrontal cortex, striatum, locus coeruleus (LC), and hippocampus and has been implicated in regulation of opioid, cholinergic, and serotonergic signaling. Dysfunctions in RGS4 proteins are involved in etiology of Parkinson's disease, addiction, and schizophrenia. RGS4 also is up-regulated in the failing human heart. RGS4 interacts with many binding partners outside of GPCR pathways, including calmodulin, COP, Kir3, PIP, calcium/CaM, PA, ErbB3, and 14-3-3
LENLINHECGLAAFKAFLKSEYSEENIDFWVSCEDYKKTKSPSKLSPKARKIYEEFISVQATKEVNLDSC
TREETSRNMLEPTISCFDEAQKKIFTLMEKDSYRRFLKSRFYLD
>gnl|CDD|188670 cd08715, RGS_RGS1, Regulator of G protein signaling (RGS) domain found in the RGS1 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS1 protein. RGS1 is a member of the R4/RGS subfamily of the RGS family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha subunits. The RGS domain controls G-protein signaling by accelerating the GTPase activity of the G-alpha subunit which leads to G protein deactivation and promotes desensitization. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS 1 is expressed predominantly in hematopoietic compartments, including T and B lymphocytes, and may play a major role in chemokine-mediated homing of lymphocytes to secondary lymphoid organs. In addition, RGS1 interacts with calmodulin and 14-3-3 protein outside of the GPCR pathway
LEKLLASQTGQNVFRSFLKSEFSEENIEFWLACEDYKKTESDLLPCKAEEIYKEFVQSDAAKQINIDFRT
RESTAKKIKAPTPTCFDEAQKVIYILMERDSYPRFLKSDIYLNL
>gnl|CDD|188671 cd08716, RGS_RGS13, Regulator of G protein signaling (RGS) domain found in the RGS13 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS13 protein. RGS13 is member of the R4/RGS subfamily of the RGS family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha subunits. The RGS domain controls G-protein signaling by accelerating the GTPase activity of the G-alpha subunit which leads to G protein deactivation and promotes desensitization. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS13 is predominantly expressed in T and B lymphocytes and in mast cells, and plays a role in adaptive immune responses. RGS13 also found in Rgs13, which is also expressed in dendritic cells and in neuroendocrine cells of the thymus, gastrointestinal, and respiratory tracts. Outside of the GPCR pathway, RGS5 interacts with the PIP3 protein
FENLMATKYGPIIYATYLKTEHSDENIEFWLACETYKKIASQRKRISMARKLFASYIQPQAPREINIDSP
TRKAIIRNIQEPTQSCFDEAQRIVYMHMERDSYPRFLESKFYQK
>gnl|CDD|188672 cd08717, RGS_RGS5, Regulator of G protein signaling (RGS) domain found in the RGS5 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS5 protein. RGS5 is member of the R4/RGS subfamily of the RGS family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha subunits. The RGS domain controls G-protein signaling by accelerating the GTPase activity of the G-alpha subunit which leads to G protein deactivation and promotes desensitization. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Two splice isoforms of RGS5 has been found: RGS5L (long) which is expressed in smooth muscle cells (pericytes) and heart and RGS5S (short) which is highly expressed in the ciliary body of the eye, kidney, brain, spleen, skeletal muscle, and small intestine. Outside of the GPCR pathway, RGS5 interacts with the 14-3-3 protein
LDKLLQNSYGLASFKSFLKSEFSEENIEFWEACEDYKKTKSPLKMATKAKKIYEEFIQTEAPKEVNIDHF
TKDVTMKNLVEPSSSSFDLAQKRIFALMEKDSLPRFVRSEFYQE
>gnl|CDD|188673 cd08718, RGS_RZ-like, Regulator of G protein signaling (RGS) domain found in the RZ protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RZ subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of G-protein signaling is controlled by RGS domains, which accelerate GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, which results in reassociation of the alpha-subunit with the beta-gamma-dimer and inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The RZ subfamily of RGS proteins includes RGS17, RGS19 (former GAIP), RGS20, and its splice variant Ret-RGS
WAQSFDKLMKSPAGRNVFREFLRTEYSEENMLFWLACEELKKEANKHVIEEKARLIYEDYISILSPKEVS
LDSRVREVINRNMLEPSPHTFDDAQLQIYTLMHRDSYPRFLNSAIYKS
>gnl|CDD|188674 cd08719, RGS_SNX13, Regulator of G protein signaling (RGS) domain found in the Sorting Nexin 13 (SNX13) protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the SNX13 (Sorting Nexin 13) protein, a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. The RGS-domain of SNX13 plays a major role through attenuation of Galphas-mediated signaling and regulates endocytic trafficking and degradation of the epidermal growth factor receptor. Snx13-null mice were embryonic lethal around midgestation which supports an essential role for SNX13 in mouse development and regulation of endocytosis dynamics
ILVNNVALSYFIDFMQSVGGQAYLFFWLTVEGYRVSAEQQLSELHLRQRGGEHQRSDVYEMLRAAALNIY
DQYLSEKASPRVPLDDSLVKKLLNRLRNDTPSDLWFDDIQQKVFDIMQEDERFYPAFKKSPAYVK
>gnl|CDD|188675 cd08720, RGS_SNX25, Regulator of G protein signaling (RGS) domain found in the Sorting Nexin 25 (SNX25) protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the SNX25 (Sorting Nexin 25) protein, a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. SNX25 is a member of the Dopamine receptors (DAR) signalplex and regulates the trafficking of D1 and D2 DARs
ILANVFGRKYLSQFLERMDSQALIGFWEAVEELRSANKSEWHQLGAEIFYTFIVEPTAEIKVDKSLRKRI
EQFLLGDKGPEVFYEVQENVVETLEEKYYPSFVVSDQYKQ
>gnl|CDD|188676 cd08721, RGS_AKAP2_2, Regulator of G protein signaling (RGS) domain 2 found in the A-kinase anchoring protein, D-AKAP2. The RGS (Regulator of G-protein Signaling) domain is an essential part of the D-AKAP2 (A-kinase anchoring protein), a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. D-AKAP2 contains two RGS domains which play an important role in spatiotemporal localization of cAMP-dependent PKA (cyclic AMP-dependent protein kinase) that regulates many different signaling pathways by phosphorylation of target proteins. This cd contains the second RGS domain
ILYCESALFYFMEYMEQEGARNLLQFWLAADNFQSQLAAKEGQYDGQQAQNDAMIIYDKYFSLQATEPLG
FDDKTRLEVESNICREGGPLPSCFEAPLLQALTTLEQHYLPGFLSSQLYYK
>gnl|CDD|188677 cd08722, RGS_SNX14, Regulator of G protein signaling (RGS) domain found in the Sorting Nexin14 (SNX14) protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the SNX14 (Sorting Nexin14) protein, a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. SNX14 is believed to regulates membrane trafficking in motor neurons
ILDDQRLLFPFMQFLKEEGAVHLLQFCLTVEDFNRRILNPDLTDEEKQSLHKEAQEIYKTYFLPEAPDRI
HFPPDIVEEIKQILEGGPEKIVKLRTSRPLFEAYEHVYSLLESVFCPLFCHSDEYFI
>gnl|CDD|188678 cd08723, RGS_RGS21, Regulator of G protein signaling (RGS) domain found in the RGS21 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part RGS21 protein, a member of RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, apoptosis, and cell proliferation, as well as modulation of cardiac development. RGS21 is a member of the R4/RGS subfamily and its mRNA was detected only in sensory taste cells that express sweet taste receptors and the taste G-alpha subunit, gustducin, suggesting a potential role in regulating taste transduction
LLANQAGLDAFRTFLKSEFSEENVEFWLACEDFKKTKSSTEIALKAQMIYSEFIQADAPKEINIDFHTRD
LISQNISEPTLKCFDEAQSLIYCLMAKDSFPRFLKSEVYKK
>gnl|CDD|188679 cd08724, RGS_GRK-like, Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase (GRK). The RGS domain is found in G protein-coupled receptor kinases (GRKs). These proteins play a key role in phosphorylation-dependent desensitization/resensitization of GPCRs (G protein-coupled receptors), intracellular trafficking, endocytosis, as well as in the modulation of important intracellular signaling cascades by GPCR. GRKs also modulate cellular response in phosphorylation-independent manner using their ability to interact with multiple signaling proteins involved in many essential cellular pathways. The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. Based on sequence homology the GRK family consists of three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development
ICEQQPIGRLLFRQFCETRPELVPQIEFLDEIKEYEVAEDEERAKKAREIYDKYIMKESLAHSHEFSKDA
VEHVQENLEKEVPKDLFQPYIEEIHDYLRGAPFQKFLESDYFTR
>gnl|CDD|188680 cd08725, RGS_RGS22_4, Regulator of G protein signaling domain RGS_RGS22_4. The RGS (Regulator of G-protein Signaling) domain found in the RGS22 protein, a member of the RA/RGS subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. RGS22 contains at least 3 copies of the RGS domain in vertebrata and exists in multiple splicing variants. RGS22 is predominantly expressed in testis and believed to play an important role in spermatogenesis
LLNPVTSEQFQRFVSLKGEELENDLLFWLEVQKYKDLCHSHSDEHIIQNKITAIISCFIDSSVPPALQID
IPPEIANRILEHRRELGPYIFREAQLTVFRVLFKYWAGFCEFRKNLQPEKILT
>gnl|CDD|188681 cd08726, RGS_RGS22_3, Regulator of G protein signaling domain RGS_RGS22_3. The RGS (Regulator of G-protein Signaling) domain found in the RGS22 protein, a member of the RA/RGS subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. RGS22 contains at least 3 copies of the RGS domain in vertebrata and exists in multiple splicing variants. RGS22 is predominantly expressed in testis and believed to play an important role in spermatogenesis
FQDLLHNRLELEFFRKFLEENSASMDLLCWLDIEQFRRIPHTDNAKRDEKAKEIKNKYLNKKYFFGPNSP
ATKEQQNKVMHAGGGWGKILHDRPPSSVLIEIQKIVRARLEKHWLPLFLATEQFRRRQAQ
>gnl|CDD|188682 cd08727, RGS_RGS22_2, Regulator of G protein signaling domain RGS_RGS22_2. The RGS (Regulator of G-protein Signaling) domain found in the RGS22 protein, a member of the RA/RGS subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. RGS22 contains at least 3 copies of the RGS domain in vertebrata and exists in multiple splicing variants. RGS22 is predominantly expressed in testis and believed to play an important role in spermatogenesis
LENRAGNFFTQFCEKSGNKLWKNAVYFWFDLQEYHQLFYTETFQPFKVCRKAQRLFSTYIVPGARHNIGC
SVRKRKEIIKKLSPPFEDLFDAAEEHILLLLLEPWSKMVKQDEAEY
>gnl|CDD|188683 cd08728, RGS-like_2, Uncharacterized Regulator of G protein Signaling (RGS) domain subfamily, child 2. These uncharacterized RGS-like domains consists largely of hypothetical proteins. The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play an important role in neuronal signal modulation. Some RGS proteins are the principal elements needed for proper vision
LRNHTHLEYFKRFLKSRGSDGPLLFWIAVEKMRVEENEKEQKAKIELIVKRYFHGQDPPGVLLQCEAIII
REIAMMKVVTTSMLLSIQHLVSKSLEERWFKKYQDTFPDCPHEVEPDEEIKVPLKPTKLKAPHVISSQKR
AWEIFISFIRSFIKFRRFMVNREIRQEFEDYLVQEMENY
>gnl|CDD|188684 cd08729, RGS_PX, Regulator of G protein signaling domain. These uncharacterized RGS-like domains are found in proteins that also contain one or more PX domains. The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. As a major G-protein regulator, the RGS domain containing proteins that are involves in many crucial cellular processes. RGS proteins regulate intracellular trafficking and provide vital support for signal transduction. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. Several RGS proteins can fine-tune immune responses, others RGS proteins play important role in neuronal signals modulation. Some RGS proteins are the principal elements needed for proper vision
LRDPSSLSYFMEFMDRRNRSQLVQFWLVVEGFKNPLEDTENDYSLDSSQSRSWIDSDKEDIAMIYETYFS
DPSPSLNVPKASRDPIRLFLNAGVNASPNEQYRKARRAVLMAQRAVYEEMEEEDFPEFKKSELFYK
>gnl|CDD|188685 cd08730, RGS-like_3, Uncharacterized Regulator of G protein Signaling (RGS) domain subfamily, child 3. These uncharacterized RGS-like domains consists largely of hypothetical proteins. The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. As a major G-protein regulator, the RGS domain containing proteins that are involved in many crucial cellular processes. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play an important role in neuronal signal modulation. Some RGS proteins are the principal elements needed for proper vision
ALKRARGMRRFRQFLAGTLGEDYLKFWLDVEMYRRDYKFGEIKRLDFFRSVVTKYLLKNSPYCLPVFKRI
ESNIGLDESAIMEVMSPMTEMPWQLLVYQMEVLSSTDTETTDGSTLEDLKRSYCEYIQQEALFILDDANH
EVSRQTVLIPTQMSARLSNGLTSLD
>gnl|CDD|188686 cd08731, RGS_RGS22_1, Regulator of G protein signaling domain RGS_RGS22_1. The RGS (Regulator of G-protein Signaling) domain found in the RGS22 protein, a member of the RA/RGS subfamily of the RGS protein family, which is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. RGS22 contains at least 3 copies of the RGS domain in vertebrata and exists in multiple splicing variants. RGS22 is predominantly expressed in testis and believed to play an important role in spermatogenesis
ITDREQGLEVFKAFLLNTRGEKLFVFWLDVEPYKAKDKVEAYLQSKRIFAKYQVASTKRELLPPSAEPLR
TRVLNAAAKKLEPKINKNFARIQLDIFRGLESLVLDHMTRTAFPQFLSSYPDYLA
>gnl|CDD|188687 cd08732, RGS-like_4, Uncharacterized Regulator of G protein Signaling (RGS) domain subfamily, child 4. These uncharacterized RGS-like domains consists largely of hypothetical proteins. The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play an important role in neuronal signal modulation. Some RGS proteins are the principal elements needed for proper vision
DLEPQKLFVSTIDDLDDFMEIEESIDDIILDPGIEHGEDDDFDEQVEELRYILDTDQILLKDQWRHIMNT
YIHHDSPLQINLSHTMRKEIVEEDDNPNIHTPDLLLNAYNEVLRLLKENFYPEFKNLPKYRKLKEEESK
>gnl|CDD|188688 cd08734, RGS-like_1, Uncharacterized Regulator of G protein Signaling (RGS) domain subfamily, child 1. These uncharacterized RGS-like domains consists largely of hypothetical proteins. The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. As a major G-protein regulator, the RGS domain containing proteins that are involved in many crucial cellular processes. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play an important role in neuronal signal modulation. Some RGS proteins are the principal elements needed for proper vision
DPNTSPLFGFSAESDFSGENLSFLTLVKEYKRLSNPAEKFTLASKIYKEFISSESPFQINISSAMLRRLD
NDFELLTGAFANVDSGLNTPFNEEISKIEASDLYPAFVK
>gnl|CDD|188689 cd08735, RGS_AKAP2_1, Regulator of G protein signaling (RGS) domain 1 found in the A-kinase anchoring protein, D-AKAP2. The RGS (Regulator of G-protein Signaling) domain is an essential part of the D-AKAP2 (A-kinase anchoring protein), a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. D-AKAP2 contains two RGS domains which play an important role in spatiotemporal localization of cAMP-dependent PKA (cyclic AMP-dependent protein kinase) that regulates many different signaling pathways by phosphorylation of target proteins. This cd contains the first RGS domain
LSKTLEQILHDNSALPYFIQFMETRRAEHLIKFWLEAESFKSAAWSRIRAHSLNTVKHSSLEEPVSPSLD
RKVLESKSTDSLSQRLTDDDDEKSMKSIERDAVSIYTKYISPDAAKPIPITEEIRNDIVAKICGEDGQVD
PNCFVEAQSFVFSAMEQDHFTEFLRSHFFCK
>gnl|CDD|188690 cd08736, RGS_RhoGEF-like, Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange factor (RhoGEF) protein. The RGS domain found in the Rho guanine nucleotide exchange factor (RhoGEF) protein subfamily of the RGS domain containing protein family, which is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RhoGEFs link signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RGS domain of the RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. The RGS-GEFs subfamily includes the leukemia-associated RhoGEF (LARG), p115RhoGEF, and PDZ-RhoGEF. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development
KSRPAHLAVFLHYVLSQFDPSPLLFYLITDLYKQGNPKDMRKWAYEIYSTFLEKNAPLKVKVPESLAAEI
DKRLPNLIDEEDLRRVFQEAQERAMPEIQEQLEDFRQKRTMGLGSLEGEL
>gnl|CDD|188691 cd08737, RGS_RGS6, Regulator of G protein signaling (RGS) domain found in the RGS6 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS6 protein, a member of R7 subfamily of the RGS protein family. RGS is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). Other members of the R7 subfamily (Neuronal RGS) include: RGS7, RGS9, and RGS11, all of which are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes such as vision and motor control. Additionally they have been implicated in many neurological conditions such as anxiety, schizophrenia, and drug dependence. RGS6 exists in multiple splice isoforms with identical RGS domains, but possess complete or incomplete GGL domains and distinct N- and C-terminal domains. RGS6 interacts with SCG10, a neuronal growth-associated protein and therefore regulates neuronal differentiation. Another RGS6-binding protein is DMAP1, a component of the Dnmt1 complex involved in repression of newly replicated genes. Mutations of a critical residue required for interaction of RGS6 protein with G proteins did not affect the ability of RGS6 to interact with both SCG10 and DMAP1. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis
QRVKRWGFSLDEVLKDPVGRDQFLRFLESEFSSENLRFWLAVQDLKKQPLQDVAKRVEEIWQEFLAPGAP
SAINLDSHSYEKTSQNVKDPGRYTFEDAQEHIYKLMKSDSYARFLRSNAYQDLLL
>gnl|CDD|188692 cd08738, RGS_RGS7, Regulator of G protein signaling (RGS) domain found in the RGS7 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS7 protein, a member of R7 subfamily of the RGS protein family. RGS is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Other members of the R7 subfamily (Neuronal RGS) include: RGS6, RGS9, and RGS11, all of which are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes such as vision and motor control. Additionally they have been implicated in many neurological conditions such as anxiety, schizophrenia, and drug dependence. R7 RGS proteins are key modulators of the pharmacological effects of drugs involved in the development of tolerance and addiction. In addition, RGS7 was found to bind a component of the synaptic fusion complex, snapin, and some other proteins outside of G protein signaling pathways
RVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIREVPSRVQEIWQEFLAPGAPS
AINLDSKSYDKTTQNVKDPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE
>gnl|CDD|188693 cd08739, RGS_RGS9, Regulator of G protein signaling (RGS) domain found in the RGS9 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS9 protein, a member of R7 subfamily of the RGS protein family. RGS is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Other members of the R7 subfamily (Neuronal RGS) include: RGS6, RGS7, and RGS11, all of which are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes such as vision and motor control. Additionally they have been implicated in many neurological conditions such as anxiety, schizophrenia, and drug dependence. RGS9 forms constitutive complexes with G-beta-5 subunit and controls such fundamental functions as vision and behavior. RGS9 exists in two splice isoforms: RGS9-1 which regulates phototransduction in rods and cones and RGS9-2 which regulates dopamine and opioid signaling in the basal ganglia. In addition, RGS9 was found to bind many other proteins outside of G protein signaling pathways including: mu-opioid receptor, beta-arrestin, alpha-actinin-2, NMDAR, polycystin, spinophilin, and guanylyl cyclase, among others
RVERWAFNFSELIRDPKGRQSFQLFLKKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGARR
WINIDGKTMDITVKGLKHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIYKE
>gnl|CDD|188694 cd08740, RGS_RGS11, Regulator of G protein signaling (RGS) domain found in the RGS11 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS11 protein, a member of R7 subfamily of the RGS protein family. RGS is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Other members of the R7 subfamily (Neuronal RGS) include: RGS6, RGS7, and RGS9, all of which are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes such as vision and motor control. Additionally they have been implicated in many neurological conditions such as anxiety, schizophrenia, and drug dependence. RGS11 is expressed exclusively in retinal ON-bipolar neurons in which it forms complexes with G-beta-5 and R7AP (RGS7 anchor protein) and plays crucial roles in processing the light responses of retinal neurons
LRVERWGFSFRELLNDPVGRKEFLDFLEKEFSAENLSFWEACEELRYGEQSKIPELVDSVYQQFLAPGAT
RWVNIDSKTMERTLEGLKQPHRYVLDDAQMHIYMLMKKDSYPRFLKSDLYKNLLAE
>gnl|CDD|188695 cd08741, RGS_RGS10, Regulator of G protein signaling (RGS) domain found in the RGS10 protein. RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS10 protein. RGS10 is a member of the RA/RGS subfamily of RGS proteins family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS10 belong to the R12 RGS subfamily, which includes RGS12 and RGS14, all of which are highly selective for G-alpha-i1 over G-alpha-q. RGS10 exists in 2 splice isoforms. RGS10A is specifically expressed in osteoclasts and is a key component in the RANKL signaling mechanism for osteoclast differentiation, whereas RGS10B expressed in brain and in immune tissues and has been implicated in diverse processes including: promoting of dopaminergic neuron survival via regulation of the microglial inflammatory response, modulation of presynaptic and postsynaptic G-protein signalling, as well as a possible role in regulation of gene expression
LENLLEDPEGVKRFREFLKKEFSEENVLFWLACEDFKKMQDKTQMQEKAKEIYMTFLSSKASSQVNVEGQ
SRLNEKILEEPHPLMFQKLQDQIFNLMKYDSYSRFLKSDLFLK
>gnl|CDD|188696 cd08742, RGS_RGS12, Regulator of G protein signaling (RGS) domain found in the RGS12 protein. RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS12 protein. RGS12 is a member of the RA/RGS subfamily of RGS proteins family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS12 belong to the R12 RGS subfamily, which includes RGS10 and RGS14, all of which are highly selective for G-alpha-i1 over G-alpha-q. RGS12 exist in multiple splice variants: RGS12s (short) contains the core RGS/RBD/GoLoco domains, while RGS12L (long) has additional N-terminal PDZ and PTB domains. RGS12 splice variants show distinct expression patterns, suggesting that they have discrete functions during mouse embryogenesis. RGS12 also may play a critical role in coordinating Ras-dependent signals that are required for promoting and maintaining neuronal differentiation
FERLLQDPVGVRYFSEFLRKEFSEENILFWQACEYFNHVPAHDKKELSYRAREIFSKFLCSKATTPVNID
SQAQLADDILNAPHPDMFKEQQLQIFNLMKFDSYTRFLKSPLYQE
>gnl|CDD|188697 cd08743, RGS_RGS14, Regulator of G protein signaling (RGS) domain found in the RGS14 protein. RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS14 protein. RGS14 is a member of the RA/RGS subfamily of RGS proteins family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS14 belong to the R12 RGS subfamily, which includes RGS10 and RGS12, all of which are highly selective for G-alpha-i1 over G-alpha-q. RGS14 binds and regulates the subcellular localization and activities of H-Ras and Raf kinases in cells and thereby integrates G protein and Ras/Raf signaling pathways
EKSVASWAVSFERLLQDPLGVEYFTEFLKKEFSAENVNFWKACERFQQIPASDTQQLAQEARKIYNEFLS
SSSQSPVNIDQQAWIGEDMLATPSPDMFRAQQLQIFNLMKFDSYARFVKSPLYQDCLLA
>gnl|CDD|188698 cd08744, RGS_RGS17, Regulator of G protein signaling (RGS) domain found in the RGS17 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS17 protein, a member of the RZ subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, the RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of the G-protein signaling controlled by the RGS domain, which accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, results in reassociation of the alpha-subunit with the beta-gamma-dimer and inhibition of downstream activity. The RZ subfamily of RGS proteins includes RGS19 (former GAIP), RGS20, and its splice variant Ret-RGS. RGS17 is a relatively non-selective GAP for G-alpha-z and other G-alpha-i/o proteins. RGS17 blocks dopamine receptor-mediated inhibition of cAMP accumulation; it also blocks thyrotropin releasing hormone-stimulated Ca++ mobilization. RGS17, like other members of RZ subfamily, can act either as a GAP or as G-protein effector antogonist
WSQNFDKMMKTPAGRNLFREFLRTEYSEENLLFWLACEDLKKEQNKKVIEEKARLIYEDYISILSPKEVS
LDSRVREVINRNLLDPNPHMYEDAQLQIYTLMHRDSFPRFLNSQIYKS
>gnl|CDD|188699 cd08745, RGS_RGS19, Regulator of G protein signaling (RGS) domain found in the RGS19 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS19 protein (also known as GAIP), a member of the RZ subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of G-protein signaling is controlled by RGS domains, which accelerate GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, resulting in a reassociation of the alpha-subunit with the beta-gamma-dimer and an inhibition of downstream activity. As a major G-protein regulator, the RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The RZ subfamily of RGS proteins includes RGS17, RGS20, and its splice variant Ret-RGS. RGS19 participates in regulation of dopamine receptor D2R and D3R, as well as beta-adrenergic receptors
WAQSFDKLMKSPAGRNVFREFLRTEYSEENMLFWLACEELKAEANKHVIDEKARLIYEDYISILSPKEVS
LDSRVREGINRKMQEPSSHTFDDAQLQIYTLMHRDSYPRFLNSPIYKA
>gnl|CDD|188700 cd08746, RGS_RGS20, Regulator of G protein signaling (RGS) domain found in the RGS20 protein. The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS20 protein (also known as RGSZ1), a member of the RZ subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of G-protein signaling is controlled by the RGS domain, which accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP resulting in reassociation of the alpha-subunit with the beta-gamma-dimer and inhibition of downstream activity. As a major G-protein regulator, the RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The RZ subfamily of RGS proteins include RGS17, RGS19 (former GAIP), and the splice variant of RGS20, Ret-RGS. RGS20 is expressed exclusively in brain, with the highest concentrations in the temporal lobe and the caudate nucleus and may play a role in signaling regulation in these brain regions. RGS20 acts as a GAP of both G-alpha-z and G-alpha-I and controls signaling in the mu opioid receptor pathway
CWCCCCSCSCLTVRNQEDERNRRTSYEFRAEGIPNCEESPKPTLEEVCAWGQSFDKLMLTPAGRNAFREF
LRTEFSEENMLFWMACEELKKEANKSVIEEKARIIYEDYISILSPKEVSLDSRVREVINRNMLEPSQHTF
DDAQLQIYTLMHRDSYPRFMNSAIYKN
>gnl|CDD|188701 cd08747, RGS_GRK2_GRK3, Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 2 (GRK2) and G protein-coupled receptor kinase 3 (GRK3). The RGS domain is an essential part of the GRK2 (G protein-coupled receptor kinases 2) and the GRK3 proteins, which are members of the beta-adrenergic receptor kinases subfamily. GRK2 and GRK3 are ubiquitously expressed and can phosphorylate many different GPCR. The C-terminus of GRK2 and 3 contains a plekstrin homology domain (PH) with binding sites for the membrane phospholipid PIP2 and free G#? subunits. These specific interactions could help to maintain a membrane-bound population of GRK2 prior to the agonist-dependent overt GRK2 translocation. GRK2 and GRK3 are members of the GRK kinase family which includes three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development
KKILLPDPSIRSVMHKYLEKRGEVTFDKIFNQKLGYLLFKDFCENVSEEPVPQLKFYEEIKKYEKLDTEE
ERIKKAREIYDNYIMKELLSCSHPFSKSAVEHVQKHLSKKEVPVDLFEPYIEEICDSLRGDVFQKFLESD
KFTRFCQWKNLELNIQL
>gnl|CDD|188702 cd08748, RGS_GRK1, Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 1 (GRK1). The RGS domain is found in G protein-coupled receptor kinases 1 (GRK1, also refered to as Rhodopsin kinase) which play a key role in phosphorylation of rhodopsin (Rho), a G protein-coupled receptor responsible for visual signal transduction in rod cell. GRK1 is a member of the GRK kinase family which includes three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. A few inactivation mutations in GRK1 have been found in patients with Oguchi disease, a stationary form of night blindness. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development
PPLSPCEDLKEELDLSFESMCVEQPIGKRLFQQFLEATEGYAAAVALWKDIEDYDVAEDGERAKKAQAIR
NRYLESSSKEFCAFLDAKAVARVKEDGNKVGDDLFKPLLRELLAHLEEAAFAPFLDSMYFLRFLQWKW
>gnl|CDD|188703 cd08749, RGS_GRK7, Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 7 (GRK7). The RGS domain is an essential part of the GRK7 (G protein-coupled receptor kinases 7) proteins which together with GRK1 (Rhodopsin kinase) have been implicated in the shutoff of the photoresponse and adaptation to changing light conditions via rod and cone opsin phosphorylation. GRK7 is a member of the GRK kinase family which includes three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. GRK7 is expressed in all vertebrate cones except that of mice and rats, which do not have the gene for GRK7. Lack of either GRK7 or both GRK1 and GRK7 in human leads to a vision defect called Enhanced S Cone syndrome. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development
PKPEQCAELRQSLSKDFESLCEQQPIGKRLFRDFLATVPEYTVAADFLDDVQNWELAEEAAKDKARQNII
ANFCKAGSKNPLSFLSGDVATKCKAATEKDFEEVVGQAKDETKEFLQGKPFTDFQTSPFYDKFLQWKEF
>gnl|CDD|188704 cd08750, RGS_GRK4, Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 4 (GRK4). The RGS domain is an essential part of the GRK4 (G protein-coupled receptor kinase4) proteins, which are membrane-associated serine/threonine protein kinases that phosphorylate G protein-coupled receptors (GPCRs) upon agonist stimulation. This phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events. GRK4 is a member of the GRK kinase family which includes three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. GRK4 plays a key role in regulating dopaminergic-mediated natriuresis and is associated with essential hypertension and/or salt-sensitive hypertension. GRK4 exists in four splice variants involved in hyperphosphorylation, desensitization, and internalization of two dopamine receptors (D1R and D3R). GRK4 also increases the expression of a key receptor of the renin-angiotensin system, the AT1R (angiotensin type 1 receptor). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development
DYSSLCDKQPIGRLLFRQFCDTRPTLKRCIEFLDAVAEYEVAPDEKRSDCGLSILDTYFNNGSAAHLPEI
PQDVVTECRLKLEENPSKELFEECTRVVHEYLSGEPFEAYQESMYFSRFLQWKWLERQPVTK
>gnl|CDD|188705 cd08751, RGS_GRK6, Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 6 (GRK6). The RGS domain is an essential part of the GRK6 (G protein-coupled receptor kinase 6) protein which plays an important role in the regulating of dopamine, opioids, M3 muscarinic, and chemokine receptor signaling. GRK6 is a member of the GRK kinase family which includes three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. The RH domain of GRK6 does not have structural determinants that are required for binding G-alpha subunit, in contrast to GRK2 and many other RGS proteins. GRK6 is an important target for treatment of addiction and Parkinson disease. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development
QFPHISLCEELRQSLERDYHSLCERQPIGRLLFRQFCATRPELSRCVAFLDAVAEYEVTPDEKRKECGQN
LTQKYLSHKSEDYIPEVPRQLVTNCTQRLEQEPCKELFQELTKLIHDYLSVAPFADYLDSIYFNRFLQWK
WLERQ
>gnl|CDD|188706 cd08752, RGS_GRK5, Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 5 (GRK5). The RGS domain is an essential part of the GRK5 (G protein-coupled receptor kinase 5) protein, a membrane-associated serine/threonine protein kinases which phosphorylates G protein-coupled receptors (GPCRs) upon agonist stimulation. This phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events. GRK5 is a member of the GRK kinase family which include three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development
YCSLCDKQPIGRLLFRQFCETRPGLECYIQFLDSVAEYEVTPDEKLGEKGKEIMTKYLTPKSPVFIPQVG
QDLVSQTEEKLLQKPCKELFSACTQSVHDYLRGEPFHEYLDSMYFDRFLQWKW
>gnl|CDD|188707 cd08753, RGS_PDZRhoGEF, Regulator of G protein signaling (RGS) domain found in the PDZ-Rho guanine nucleotide exchange factor (RhoGEF) protein. The RGS domain is an essential part of the PDZ-RhoGEF (PDZ:Postsynaptic density 95, Disk large, Zona occludens-1; RhoGEF: Rho guanine nucleotide exchange factor; alias PRG) protein, a member of RhoGEFs subfamily of the RGS protein family. The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration, and cell cycle progression, as well as gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. RhoGEFs subfamily includes leukemia-associated RhoGEF protein (LARG), p115RhoGEF, PDZ-RhoGEF and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. In contrast to p115RhoGEF and LARG, PDZ-RhoGEF cannot serve as a GTPase-activating protein (GAP), due to the mutation of sites in the RGS domain region that are crucial for GAP activity. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development
LIIGPEEDYDPGYFNNESDIIFQDLEKLKSRPAHLVVFLRYIFSQADPGPLLFYLCSEVYQQTSPKDSRS
LGKDIWNIFLEKNAPLRVKIPEMLQAEIDLRLRNNEDPRGVLCEAQEAVMPEIQEQIQDYRSKRTLGLGS
LYGEN
>gnl|CDD|188708 cd08754, RGS_LARG, Regulator of G protein signaling (RGS) domain found in the leukemia-associated Rho guanine nucleotide exchange factor (RhoGEF) protein (LARG). The RGS domain is an essential part of the leukemia-associated RhoGEF protein (LARG), a member of the RhoGEF (Rho guanine nucleotide exchange factor) subfamily of the RGS protein family. The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration, cell cycle progression of cells, and gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RhoGEF subfamily includes p115RhoGEF, LARG, PDZ-RhoGEF, and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. In addition to being a G-alpha13 effector, the LARG protein also functions as a GTPase-activating protein (GAP) for G-alpha13. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development
GIIGAEDDDFPTESEQINGQCSCFQNIELLKSRPAHLAVFLHHVVSQFDPAALLCYLYADLYKQTNSKET
RRVFLEFNQFFLDRAANLKVPVPDEVSLDLEKRRPELIPEELHRHYIQTMQERVSPEVQRNLEDFRQKRS
MGLTLAEGELTKLDAERFRDRNTIEKERACAEQIVAKIEEVLMTSQTPEEDKSSTIQYVILTYMKHLGVK
VKEPRNLEQKRG
>gnl|CDD|188709 cd08755, RGS_p115RhoGEF, Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange factor (GEF), p115 RhoGEF. The RGS (Regulator of G-protein Signaling) domain is an essential part of the p115RhoGEF protein, a member of the RhoGEF (Rho guanine nucleotide exchange factor) subfamily of the RGS protein family. The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration, cell cycle progression of cells, and gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RhoGEF subfamily includes p115RhoGEF, LARG, PDZ-RhoGEF and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. In addition to being a G-alpha13/12 effector, the p115RhoGEF protein also functions as a GTPase-activating protein (GAP) for G-alpha13. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development
VKSRPAHLMVFLQHVMLQFDPAPLLCYLHADMLKNLNTKETKKHFGDFYNTFLEKGAVLKVSVPSNVAFE
LDRTRPELINEEQQRRYVNEIQFAQSPAILRQLEDFRQKRMMGMTPNERELNDLESHRPTDRIPMEAKEK
AVAESLLEKLVEMNPTIVPDEEKSNAIFGAIAYYMKHLGVKTKAFDNKKSKSG
>gnl|CDD|188710 cd08756, RGS_GEF_like, Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange factor (RhoGEF) protein. The RGS domain found in the Rho guanine nucleotide exchange factor (RhoGEF) protein subfamily of the RGS domain containing protein family, which is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration and cell cycle progression as well as gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RhoGEF subfamily includes the leukemia-associated RhoGEF protein (LARG), p115RhoGEF, PDZ-RhoGEF, and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development
KTHPAHLAVFLNYLLSNSDPSSLFFYLITDLYKSGNIKDMRKWAYEIFSTFLVPNAPLLWPNIDESLIQE
IDKILQNEQDDEEILRRVFLKAREKARDEINDQLADFRQKRTLGLGSIFGPN
>gnl|CDD|188885 cd08757, SAM_PNT_ESE, Sterile alpha motif (SAM)/Pointed domain of ESE-like ETS transcriptional regulators. SAM Pointed domain of ESE-like (Epithelium-Specific ETS) subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. It can act as a major transactivator by providing a potential docking site for co-activators. ETS factors are important for cell differentiation. They can be involved in regulation of gene expression in different types of epithelial cells. They are expressed in salivary gland, intestine, stomach, pancreas, lungs, kidneys, colon, mammary gland, and prostate. Members of this group are proto-oncogenes. Expression profiles of these factors are altered in epithelial cancers, which makes them potential targets for cancer therapy
HPQHWTKNDVLDWLLFVAEQNKIDAEEINFQKFDNIDGQTLCSMSLEEFIERDGVYGNLLYAELRRLLS
>gnl|CDD|260086 cd08759, Type_III_cohesin_like, Cohesin domain, interaction partner of dockerin. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. Two specific calcium-dependent interactions between cohesin and dockerin appear to be essential for cellulosome assembly, type I and type II. This subfamily represents type III cohesins and closely related domains
GTLSLVPSKTSVKAGETFTIDLYGQGLKNVNATGAHIPFDSSKLELVKDEGATAAKTAGMENLSKEKTHD
DDTADVNLAFANRGDKDLLNGDGVLATFTLKAKEDATGDKYDIELAYESISEDLLVGPKKDEEGELPQAP
ATKVLSDFDIGITTGNDGYITDDGTNS
>gnl|CDD|176490 cd08760, Cyt_b561_FRRS1_like, Eukaryotic cytochrome b(561), including the FRRS1 gene product. Cytochrome b(561), as found in eukaryotes, similar to and including the human FRRS1 gene product (ferric-chelate reductase 1), also called SDR-2 (stromal cell-derived receptor 2). This family comprises a variety of domain architectures, many of which contain dopamine beta-monooxygenase (DOMON) domains. The protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments
SKSSYSLDLASGTSSSGGSPFLLPNGSSVGSSDTLIKAHGVLMAIAWGILMPIGALLARYFLLGDPVWFY
LHAGLQLLAVLLAIAGFVLGIVLVQGGGGSLNNAHAILGIIVLALAILQPLLGLLRPHPGSKKRSIWNWA
HRWLGRAALILAIVNIFLGLDLAGAGTPKAWKIAYGVVVAVLALVYLILEI
>gnl|CDD|176491 cd08761, Cyt_b561_CYB561D2_like, Eukaryotic cytochrome b(561), including the CYB561D2 gene product. Cytochrome b(561), as found in eukaryotes, similar to and including the human CYB561D2 gene product. CYB561D2 is a candidate tumor suppressor. The protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments
LVAVVFAAFLLYIARPGTSLFSWHPLLMSLGFLLLMTEALLLLQPTSSLTKLARKTKVRLHWILQLLALL
CILAGLVAIYYNKERNGKPHFTSWHGILGLVTVILIVLQALGGLALLYPPGLRRGESKAKKLKKYHRLSG
YVAYLLGLATLVLGLETRWFSKNVTHVALWYLALAVALALAGV
>gnl|CDD|176492 cd08762, Cyt_b561_CYBASC3, Vertebrate cytochrome b(561), CYBASC3 gene product. Cytochrome b ascorbate-dependent 3, as found in vertebrates, which might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments
CLLLGILGIACVVLVVHWNQMWRGGFAWDGSSKNFNWHPVLMVTGMVVLYGNAALVYRIPLTWGGPKLPW
KLLHAGLLLLAFILTVIGLCAVFNFHNVHHTANLYSLHSWVGICTVALFTCQWVMGFTSFLLPWAPMWLR
ALVKPIHVFFGAMILVLSIASCISGINEKLFFSLKNTTN
>gnl|CDD|176493 cd08763, Cyt_b561_CYB561, Vertebrate cytochrome b(561), CYB561 gene product. Cytochrome b(561), as found in vertebrates, which might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments
WSGPLQFNVHPLCMVLGLVFLCGEALLVYRVFRNETKRSTKILHGLLHIMALVISLVGLVAVFDYHQANG
YPDMYSLHSWCGILTFVLYFLQWLIGFSFFLFPGASFTLRSQYKPLHEFFGRALFLSSVGTSLLGLTEKL
LFN
>gnl|CDD|176494 cd08764, Cyt_b561_CG1275_like, Non-vertebrate eumetazoan cytochrome b(561). Cytochrome b(561), as found in non-vertebrate eumetazoans, similar to the Drosophila melanogaster CG1275 gene product. This protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments
VVLVGIWLGKFRGGFSWTGPGLQFNWHPLLMVLGLIFLYGNSILVYRVFRNTRKKRLKLLHAVLHLLAFI
LAVIGLKAVFDSHNLAKPPIPNMYSLHSWLGLTAVILFSLQWVGGFVSFLFPGLPETLRAAYLPLHVFFG
LFIFVLAVATALLGITEKAFFSLNKYSNLPAEGVLGNFIGIVLVIFGGLVVYLVTEPDYKRIELPEEEEL
LIQN
>gnl|CDD|176495 cd08765, Cyt_b561_CYBRD1, Vertebrate cytochrome b(561), CYBRD1 gene product. Duodenal cytochrome b or ferric-chelate reductase 3, a cytochrome b(561), as found in vertebrates, which might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. This protein is expressed at the brush border of duodenal enterocytes and may play a role in the uptake of dietary Fe(3+), facilitating its transport into the mucosal cells. It may also be involved in the recycling of extracellular ascorbate in erythrocyte membranes, and act as a ferrireductase in epithelial cells of the respiratory system. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments
EGLGWDGGAAEFNWHPVLMVIGFIFIQGIAIIVYRLPWTWKCSKLLMKLIHAGLHILAFILAIISVVAVF
VFHNAKNIPNMYSLHSWVGLAAVILYPLQLVLGISVYLLPVAPVRLRAALMPLHVYSGLFIFGTVIATAL
MGITEKLIFSLKS
>gnl|CDD|176496 cd08766, Cyt_b561_ACYB-1_like, Plant cytochrome b(561), including the carbon monoxide oxygenase ACYB-1. Cytochrome b(561), as found in plants, similar to the Arabidopsis thaliana ACYB-1 gene product, a cytochrome b561 isoform localized to the tonoplast. This protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), and might be capable of trans-membrane electron transport from intracellular ascorbate to extracellular ferric chelates. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments
SDNKGLIFNVHPVLMVIGFIFLAGEAILAYKTVPGSREVQKAVHLTLHLVALVLGIVGIYAAFKFHNEVG
IPNLYSLHSWLGIGTISLFGLQWLFGFVTFWFPGASRNTRAALLPWHVFLGLAIYYLAIATAETGLLEKL
TFLQ
>gnl|CDD|176572 cd08767, Cdt1_c, The C-terminal fold of replication licensing factor Cdt1 is essential for Cdt1 activity and directly interacts with MCM2-7 helicase. Cdt1 is a replication licensing factor in eukaryotes that recruits the Minichromosome Maintenance Complex (MCM2-7) to the Origin Recognition Complex (ORC). The Cdt1 protein is divided into three regions based on sequence comparison and biochemical analyses: the N-terminal region (Cdt1_n) binds DNA in a sequence-, strand-, and conformation-independent manner; the middle winged helix fold (Cdt1_m) binds geminin to inhibit both binding of the MCM complex to origins of replication and DNA; and the C-terminal region (Cdt1_c) is essential for Cdt1 activity and directly interacts with the MCM2-7 helicase. Precise duplication of chromosomal DNA is required for genomic stability during replication. Assembly of replication factors to start DNA replication in eukaryotes must occur only once per cell cycle. To form a pre-replicative complex on replication origins in the G phase, ORC first binds origin DNA and triggers the binding of Cdc6 and Cdt1. These two factors recruit a putative replicative helicase and the MCM2-7. The MCM2-7 complex promotes the unwinding of DNA origins, and the binding of additional factors to initiate the DNA replication in S-phase. Cdt1 is present during G1 and early S phase of the cell cycle and is degraded during the late S, G2, and M phases. The winged helix fold structure of Cdt1_m is similar to the structures of Cdt1_c and archaeal homologues of the eukaryotic replication initiator, without apparent sequence similarity
KEALKGVPKSLLERIRAKEAAKALEKMTRRPEQEKRRRMYARLPELARILRNIFVSEKKTVLPLEELVYK
LQASYPSILSRGEVEEHLRLLAELAPDWISEKSLRKGDYLKIDKKVDLEKVRKRLE
>gnl|CDD|176573 cd08768, Cdc6_C, Winged-helix domain of essential DNA replication protein Cell division control protein (Cdc6), which mediates DNA binding. This model characterizes the winged-helix, C-terminal domain of the Cell division control protein (Cdc6_C). Cdc6 (also known as Cell division cycle 6 or Cdc18) functions as a regulator at the early stages of DNA replication, by helping to recruit and load the Minichromosome Maintenance Complex (MCM) onto DNA and may have additional roles in the control of mitotic entry. Precise duplication of chromosomal DNA is required for genomic stability during replication. Cdc6 has an essential role in DNA replication and irregular expression of Cdc6 may lead to genomic instability. Cdc6 over-expression is observed in many cancerous lesions. DNA replication begins when an origin recognition complex (ORC) binds to a replication origin site on the chromatin. Studies indicate that Cdc6 interacts with ORC through the Orc1 subunit, and that this association increases the specificity of the ORC-origins interaction. Further studies suggest that hydrolysis of Cdc6-bound ATP promotes the association of the replication licensing factor Cdt1 with origins through an interaction with Orc6 and this in turn promotes the loading of MCM2-7 helicase onto chromatin. The MCM2-7 complex promotes the unwinding of DNA origins, and the binding of additional factors to initiate the DNA replication. S-Cdk (S-phase cyclin and cyclin-dependent kinase complex) prevents rereplication by causing the Cdc6 protein to dissociate from ORC and prevents the Cdc6 and MCM proteins from reassembling at any origin. By phosphorylating Cdc6, S-Cdk also triggers Cdc6's ubiquitination. The Cdc6 protein is composed of three domains, an N-terminal AAA+ domain with Walker A and B, and Sensor-1 and -2 motifs. The central region contains a conserved nucleotide binding/ATPase domain and is a member of the ATPase superfamily. The C-terminal domain (Cdc6_C) is a conserved winged-helix domain that possibly mediates protein-protein interactions or direct DNA interactions. Cdc6 is conserved in eukaryotes, and related genes are found in Archaea. The winged helix fold structure of Cdc6_C is similar to the structures of other eukaryotic replication initiators without apparent sequence similarity
PLHQKLVLLALLLLFKRGGEEEATTGEVYEVYEELCEEIGVDPLTQRRISDLLSELEMLGLLETEVSSKG
RRGRTRKISLNVDPDDV
>gnl|CDD|176451 cd08769, DAP_dppA_2, Peptidase M55, D-aminopeptidase dipeptide-binding protein family. M55 Peptidase, D-Aminopeptidase dipeptide-binding protein (dppA; DAP dppA; EC 3.4.11.-) domain: Peptide transport systems are found in many bacterial species and generally function to accumulate intact peptides in the cell, where they are hydrolyzed. The dipeptide-binding protein (dppA) of Bacillus subtilis belongs to the dipeptide ABC transport (dpp) operon expressed early during sporulation. It is a binuclear zinc-dependent, D-specific aminopeptidase. The biologically active enzyme is a homodecamer with active sites buried in its channel. These self-compartmentalizing proteases are characterized by a SXDXEG motif. D-Ala-D-Ala and D-Ala-Gly-Gly are the preferred substrates. Bacillus subtilis dppA is thought to function as an adaptation to nutrient deficiency; hydrolysis of its substrate releases D-Ala which can be used subsequently as metabolic fuel. This family also contains a number of uncharacterized putative peptidases
MKIYISVDIEGLPGVVSWEMVAPGKELYKEARRLMTEELNAVLEELFESGFEEIVVADSHGRMDNIDYEE
LDPRVSLVSGYPRPLSMMTGLDESFDAVLFIGYHAGAGTPKGIMDHTYSGSTIYNIWINGKEMNETLINA
AYAGEFGVPVVLVAGDSELEKEVKEETPWAVFVPTKESLSRYSAKSPSMKKVKEELREAVKEALERLKLG
ELKPLKFSKPIELEVEFRDTLMADVVELLPGVERLDGRTVRYVAESYKDAYKAIEAIVFL
>gnl|CDD|176452 cd08770, DAP_dppA_3, Peptidase M55, D-aminopeptidase dipeptide-binding protein family. M55 Peptidase, D-Aminopeptidase dipeptide-binding protein (dppA; DAP dppA; EC 3.4.11.-) domain: Peptide transport systems are found in many bacterial species and generally function to accumulate intact peptides in the cell, where they are hydrolyzed. The dipeptide-binding protein (dppA) of Bacillus subtilis belongs to the dipeptide ABC transport (dpp) operon expressed early during sporulation. It is a binuclear zinc-dependent, D-specific aminopeptidase. The biologically active enzyme is a homodecamer with active sites buried in its channel. These self-compartmentalizing proteases are characterized by a SXDXEG motif. D-Ala-D-Ala and D-Ala-Gly-Gly are the preferred substrates. Bacillus subtilis dppA is thought to function as an adaptation to nutrient deficiency; hydrolysis of its substrate releases D-Ala which can be used subsequently as metabolic fuel. This family also contains a number of uncharacterized putative peptidases
MKVYISADIEGIAGISSWDETTLGGPDYEEFREQMTKEVVAACEGAIEAGATEIVVKDAHGSGRNILPSK
LPDNVKLIRGWSGHPYCMVEGLDESFDAVMFIGYHSAAGSPGNPLAHTLTGGVSYVKINGEIASEFLINA
YTAAYLGVPVVFVSGDAGLCAEAKELNPNIVTVPVKEGFGGATISIHPGLACKEIRKGVKKALSGLSRDL
IELPEEFTLEVKYKDHKEAYRASFYPGATQVDGYTIRFETADYFDVLRFLLFI
>gnl|CDD|206738 cd08771, DLP_1, Dynamin_like protein family includes dynamins and Mx proteins. The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner
IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHLKSKE
FTDFEELREEIEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMV
KSYISNPRSIILAVVPANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLLLQGKVIPL
KLGYVGVVNRSQKDIDSGKSIEEALEAEEEFFETHPWYKLLPASRVGTPALRKRLSKLLQKHIRESLP
>gnl|CDD|350091 cd08772, GH43_62_32_68_117_130, Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130. Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans
FDPSVVPYNGEYHLFFTIGPKNTRPFLGHARSKDLIHWEEEPPAIVARGGGSYDTSYAFDPEVVYIEGTY
YLTYCSDDLGDILRHGQHIGVAYSKDPKGPWTRKDAPLIEPPNAYSPKNRDPVLFPRKIGKYYLLNVPSD
NGHTRFGKIAIAESPDXLHWINHSFVYNYNEQGKVGEGPSLWKTKGGWYLIYHANTLTGYGYGFGYALGD
LDDPSKVLYRSRPEEEYETVGFKPNVVAPAAFLCDSTGIVAIIGHAA
>gnl|CDD|176798 cd08773, FpgNei_N, N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII) base-excision repair DNA glycosylases. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. These enzymes initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycolsylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. The FpgNei DNA glycosylases represent one of the two structural superfamilies of DNA glycosylases that recognize oxidized bases (the other is the HTH-GPD superfamily exemplified by Escherichia coli Nth). Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. One exception is mouse Nei-like glycosylase 3 (Neil3) which forms a Schiff base intermediate via its N-terminal valine. In addition to this FpgNei_N domain, FpgNei proteins have a helix-two-turn-helix (H2TH) domain and a zinc (or zincless)-finger motif which also contribute residues to the active site. FpgNei DNA glycosylases have a broad substrate specificity. They are bifunctional, in addition to the glycosylase (recognition) activity, they have a lyase (cleaving) activity on the phosphodiester backbone of the DNA at the AP site. This superfamily includes eukaryotic, bacterial, and viral proteins
PELPEVELLRRKLRRALKGKRVTRVEVSDPRRLFTPAAELAAALIGRRVRGAERRGKYLLLELSGGPWLV
IHLGMTGRLRVCPEGEPPPKHDRLVLRLANGSQLRFTDPRKFGRVEL
>gnl|CDD|206755 cd08774, 14-3-3, 14-3-3 domain. 14-3-3 domain is an essential part of 14-3-3 proteins, a ubiquitous class of regulatory, phosphoserine/threonine-binding proteins found in all eukaryotic cells, including yeast, protozoa and mammalian cells. 14-3-3 proteins play important roles in many biological processes that are regulated by phosphorylation, including cell cycle regulation, cell proliferation, protein trafficking, metabolic regulation and apoptosis. More than 300 binding partners of the 14-3-3 domain have been identified in all subcellular compartments and include transcription factors, signaling molecules, tumor suppressors, biosynthetic enzymes, cytoskeletal proteins and apoptosis factors. 14-3-3 binding can alter the conformation, localization, stability, phosphorylation state, activity as well as molecular interactions of a target protein. They function only as dimers, some preferring strictly homodimeric interaction, while others form heterodimers. Binding of the 14-3-3 domain to its target occurs in a phosphospecific manner where it binds to one of two consensus sequences of their target proteins; RSXpSXP (mode-1) and RXXXpSXP (mode-2). In some instances, 14-3-3 domain containing proteins are involved in regulation and signaling of a number of cellular processes in phosphorylation-independent manner. Many organisms express multiple isoforms: there are seven mammalian 14-3-3 family members (beta, gamma, eta, theta, epsilon, sigma, zeta), each encoded by a distinct gene, while plants contain up to 13 isoforms. The flexible C-terminal segment of 14-3-3 isoforms shows the highest sequence variability and may significantly contribute to individual isoform uniqueness by playing an important regulatory role by occupying the ligand binding groove and blocking the binding of inappropriate ligands in a distinct manner. Elevated amounts of 14-3-3 proteins are found in the cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. In protozoa, like Plasmodium or Cryptosporidium parvum 14-3-3 proteins play an important role in key steps of parasite development
EELVYLAKLAEQAERYDDMVKYMKQVAELNGELTKEERNLLSVAYKNVVGSRRASWRILSSIEQKESSKG
NEEKLKLIKEYKEKIEKELKDICNDILDLIDKHLIPSATDPESKVFYLKMKGDYYRYLAEFASGDERKEA
AEKAKKAYQEALEIAKKLLPPTHPIRLGLALNFSVFYYEILNDPEEACKLAKKAFDEAIAELDTLSEESY
KDSTLIMQLLRDNLT
>gnl|CDD|176753 cd08775, DED_Caspase-like_r2, Death effector domain, repeat 2, of initator caspase-like proteins. Death Effector Domain (DED), second repeat, found in initator caspase-like proteins like caspase-8, -10 and c-FLIP. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of DISC. All members contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
SAYRVMLYQVSEELSRSELRSLKFLLQEEISSCKLDDDMNFLDIVIEMENRVLLGPGKVDILKRMLRQLR
RKDLLKQINDY
>gnl|CDD|176754 cd08776, DED_Caspase-like_r1, Death effector domain, repeat 1, of initator caspase-like proteins. Death Effector Domain (DED), first repeat, found in initator caspase-like proteins, like caspase-8 and -10 and c-FLIP. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of DISC. All members contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
TYEVLCEVAEKLGTDEREVLLFLLNVFIPQPTLAQLIGALRALKEEGRLTLPLLAECLYRAGRRDLLRSL
L
>gnl|CDD|260048 cd08777, Death_RIP1, Death Domain of Receptor-Interacting Protein 1. Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal DD, which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
TEKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDYERDGLKEKVHQMLEKWKMKEGSKGATVGKLAKA
LEGCIKSDLLVSLLQV
>gnl|CDD|176756 cd08778, Death_TNFRSF21, Death domain of tumor necrosis factor receptor superfamily member 21. Death domain (DD) found in tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also called death receptor-6, DR6. DR6 is an orphan receptor that is expressed ubiquitously, but shows high expression in lymphoid organs, heart, brain and pancreas. Results from DR6(-/-) mice indicate that DR6 plays an important regulatory role for the generation of adaptive immunity. It may also be involved in tumor cell survival and immune evasion. In neuronal cells, it binds beta-amyloid precursor protein (APP) and activates caspase-dependent cell death. It may contribute to the pathogenesis of Alzheimer's disease. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
HGIDILKLVAAQVGSQWKDIYQFLCNASEREVAAFSNGYTADHERAYAALQHWTIRGPEASLAQLISALR
QHRRNDVVEKIRGL
>gnl|CDD|260049 cd08779, Death_PIDD, Death Domain of p53-induced protein with a death domain. Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTAL
SKSGRSDLAEELRDKL
>gnl|CDD|260050 cd08780, Death_TRADD, Death Domain of Tumor Necrosis Factor Receptor 1-Associated Death Domain protein. Death domain (DD) of TRADD (TNF Receptor 1-Associated Death Domain or TNFRSF1A-associated via death domain) protein. TRADD is a central signaling adaptor for TNF-receptor 1 (TNFR1), mediating activation of Nuclear Factor -kappaB (NF-kB) and c-Jun N-terminal kinase (JNK), as well as caspase-dependent apoptosis. It also carries important immunological roles including germinal center formation, DR3-mediated T-cell stimulation, and TNFalpha-mediated inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
TPADQQHFAKSVGKKWKPVGRSLQKNCRALRDPAIDNLAYEYDREGLYEQAYQLLRRFIQSEGKKATLQR
LVQALEENGLTSLAEDLLGL
>gnl|CDD|260051 cd08781, Death_UNC5-like, Death domain found in Uncoordinated-5 homolog family. Death Domain (DD) found in Uncoordinated-5 (UNC-5) homolog family, which includes Unc5A, B, C and D in vertebrates. UNC5 proteins are receptors for secreted netrins (netrin-1, -3 and -4) that are involved in diverse processes like axonal guidance, neuronal migration, blood vessel patterning, and apoptosis. They are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
LPYSIRQKLCSLLDPPNARGNDWRLLAQKLSVDRYINYFATKPSPTEVILDLWEARNRDDGALNSLAAIL
REMGRHDAATILE
>gnl|CDD|260052 cd08782, Death_DAPK1, Death domain found in death-associated protein kinase 1. Death domain (DD) found in death-associated protein kinase 1 (DAPK1). DAPK1 is composed of several functional domains, including a kinase domain, a CaM regulatory domain, ankyrin repeats, a cytoskeletal-binding domain and a C-terminal DD. It plays important roles in a diverse range of signal transduction pathways including apoptosis, growth factor signalling, and autophagy. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
LTRRKLARLLDPPDPMGRDWCLLAVNLGLTDLVAKLDSTSSPLPSPTDRLLQEWTARPPSTIGALLRKLR
ELGRRDAADFLL
>gnl|CDD|260053 cd08783, Death_MALT1, Death domain similar to that found in Mucosa-associated lymphoid tissue-lymphoma-translocation gene 1. Death domain (DD) similar to that found in Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1). Malt1, together with Bcl10 (B-cell lymphoma 10), are the integral components of the CBM signalosome. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells) and with CARMA1 to form L-CBM (CBM complex in lymphoid immune cells), to mediate activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
INSLQEPVLRRLCELLDQASDKGWRKLAEAVGSDPRFKISSQELEQCSLKVLEPEGSPSRCLLKLMGERG
CTLKDLTDFLQTMGHTEALQLLKPPG
>gnl|CDD|260054 cd08784, Death_DRs, Death Domain of Death Receptors. Death domain (DD) found in death receptor proteins. Death receptors are members of the tumor necrosis factor (TNF) receptor superfamily, characterized by having a cytoplasmic DD. Known members of the family are Fas (CD95/APO-1), TNF-receptor 1 (TNFR1/TNFRSF1A/p55/CD120a), TNF-related apoptosis-inducing ligand receptor 1 (TRAIL-R1 /DR4), and receptor 2 (TRAIL-R2/DR5/APO-2/KILLER), as well as Death Receptor 3 (DR3/APO-3/TRAMP/WSL-1/LARD). They are involved in apoptosis signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
YITTIAGVVPLSQWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDLKKM
NLCTLAEKIQ
>gnl|CDD|260055 cd08785, CARD_CARD9-like, Caspase activation and recruitment domain of CARD9 and related proteins. Caspase activation and recruitment domain (CARD) found in CARD9, CARD14 (CARMA2), CARD10 (CARMA3), CARD11 (CARMA1) and BCL10. BCL10 (B-cell lymphoma 10), together with Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), are integral components of the CBM signalosome. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells), and with CARD11 to form L-CBM (CBM complex in lymphoid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. BCL10/Malt1 also associates with CARD10, which is more widely expressed and is not restricted to hematopoietic cells, to play a role in GPCR-induced NF-kB activation. CARD14 has also been shown to associate with BCL10. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
LWEALERHRHRLSRYINPSRLTPYLRQKKVLSEDDEEEILSKPSLPRNRAGYLLDILKTRGKNGYDAFLE
SLEFYYPELFTKVT
>gnl|CDD|176764 cd08786, CARD_RIP2_CARD3, Caspase activation and recruitment domain of Receptor Interacting Protein 2. Caspase activation and recruitment domain (CARD) of Receptor Interacting Protein 2 (RIP2/RIPK2/RICK/CARDIAK/CARD3). RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP2 harbors a C-terminal CARD domain and functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR)-family, NOD1 and NOD2, which recognizes bacterial peptidoglycans released upon infection. This cascade is implicated in inflammatory immune responses and the clearance of intracellular pathogens. RIP2 associates with NOD1 and NOD2 via CARD-CARD interactions. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
QWIASKREEIVSQMTEACLNQSLDALLSRQLLMREDYELISTKPTRTSKVRQLLDTCDCQGEEFARVVVQ
KLKDNKQMGLQPYPDII
>gnl|CDD|176765 cd08787, CARD_NOD2_1_CARD15, Caspase activation and recruitment domain of NOD2, repeat 1. Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 1. NOD2 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD2, as well as NOD1, the N-terminal effector domain is a CARD. NOD2 contains two N-terminal CARD repeats. Mutations in NOD2 have been associated with Crohns disease and Blau syndrome. Nod2-CARDs have been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
FLAQRSELLEVLCSGGSLEPFESVLDWLLSQEVLSWEDYEGFHVLGQPLSHNARQLLDTVYNKGEWACQK
FLAAAQQALAEEQSAGL
>gnl|CDD|260056 cd08788, CARD_NOD2_2_CARD15, Caspase activation and recruitment domain of NOD2, repeat 2. Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 2. NOD2 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD2, as well as NOD1, the N-terminal effector domain is a CARD. NOD2 contains two N-terminal CARD repeats. Mutations in NOD2 have been associated with Crohns disease and Blau syndrome. Nod2-CARDs have been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
LQTQRPALVRRLRDHVDGALELLLTRGFFSQYDCDEIRLPIFTPSQQARRLLDLVKAKGEGAAKFLLQYV
QQLPEPPSPLN
>gnl|CDD|260057 cd08789, CARD_IPS-1_RIG-I, Caspase activation and recruitment domains (CARDs) found in IPS-1 and RIG-I-like RNA helicases. Caspase activation and recruitment domains (CARDs) found in IPS-1 (Interferon beta promoter stimulator protein 1) and Retinoic acid Inducible Gene I (RIG-I)-like DEAD box helicases. RIG-I-like helicases and IPS-1 play important roles in the induction of interferons in response to viral infection. They are crucial in triggering innate immunity and in developing adaptive immunity against viral pathogens. RIG-I-like helicases, including MDA5 and RIG-I, contain two N-terminal CARD domains and a C-terminal DEAD box RNA helicase domain. They are cytoplasmic RNA helicases that play an important role in host antiviral response by sensing incoming viral RNA. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. MDA5 and RIG-I associate with IPS-1 through a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
TDDEKQLLQCYRATVERSLDVVYVLPYLTDCLPDEDRERIRAAEENRGNSGAAALLLNTLLQLEKEGWFR
GFLDALRATGYTGARELIDNW
>gnl|CDD|260058 cd08790, DED_DEDD, Death Effector Domain of DEDD. Death Effector Domain (DED) found in DEDD. DEDD has been shown to block mitotic progression by inhibiting Cdk1 and to be involved in regulating the insulin signaling cascade. DEDD can bind to itself, to DEDD2, and to the two tandem DED-containing caspases, caspase-8 and -10. In general, DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
GLYSLHRMFDIVGDQLTHRDVRVLSFLFVDVIDEYERGRIRDGRDFLLALEKQGRCDETNFRQVLQLLRI
ITRHDLLPYVTLRKRRAVCPDPVDKYL
>gnl|CDD|176769 cd08791, DED_DEDD2, Death Effector Domain of DEDD2. Death Effector Domain (DED) found in DEDD2. DEDD2 has been shown to bind to itself, DEDD, and to the two tandem DED-containing caspases, caspase-8 and -10. It may play a role in apoptosis. In general, DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways
EDECLSYYGMLSLHRMFEVVGSQLTETCGGELAFLLDETYPGKHPLDRPKSGVELLLELERRGYCDESNL
RPLLQLLRVLTRHDLLPFVSQKRRRTVSPERYKYGY
>gnl|CDD|260059 cd08792, DED_Caspase_8_10_r1, Death effector domain, repeat 1, of initator caspases 8 and 10. Death Effector Domain (DED) found in caspase-8 and caspase-10, repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis, and they play partially redundant roles. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. They contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
FRKLLLDIDEELDSDDLDALKFLCTDVLPRNKLEKVESGLDLFSRLEEQGLLSEEDPFLLAELLYRIGRK
DLLRKLG
>gnl|CDD|260060 cd08793, Death_IRAK4, Death domain of Interleukin-1 Receptor-Associated Kinase 4. Death Domain (DD) of Interleukin-1 Receptor-Associated Kinase 4 (IRAK4). IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. They are involved in signal transduction pathways involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB, and mitogen-activated protein kinases. IRAKs contain an N-terminal DD domain and a C-terminal kinase domain. IRAK4 is an active kinase that is also involved in T-cell receptor signaling pathways, implying that it may function in acquired immunity and not just in innate immunity. It is known as the master IRAK member because its absence strongly impairs TLR- and IL-1-mediated signaling and innate immune defenses, while the absence of other IRAK proteins only shows slight effects. IRAK4-deficient patients have impaired inflammatory responses and recurrent life-threatening infections. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
TYVRKLNYGLLRKLSDFLDPQEGWKKIAVAIMKPSGEPRYSQFHIRRFEALVQQGKSPTCELLFDWGTTN
CTVGDLVDLLIQNEFLAAASLLLPDAVPEE
>gnl|CDD|260061 cd08794, Death_IRAK1, Death domain of Interleukin 1 Receptor Associated Kinase-1. Death Domain (DD) of Interleukin-1 Receptor-Associated Kinase 1 (IRAK1). IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. They are involved in signal transduction pathways involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB (NF-kB), and mitogen-activated protein kinases (MAPKs). IRAKs contain an N-terminal DD domain and a C-terminal kinase domain. IRAK1 is an active kinase and also plays adaptor functions. It binds to the MyD88-IRAK4 complex via its DD, which facilitates its phosphorylation by IRAK4, activating it for further auto-phosphorylation. Hyper-phosphorylated IRAK1 forms a cytosolic complex with TRAF6, leading to the activation of NF-kB and MAPK pathways. IRAK1 is involved in autoimmunity and may be associated with lupus pathogenesis. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
EFLYELPPSVMWRFCLVMDSLSDLDWTRFASEIIKDQTELRLLERSGRRTDWVMWRWENRNGRVGELVDI
LERLQLLRPRDVIL
>gnl|CDD|176773 cd08795, Death_IRAK2, Death domain of Interleukin 1 Receptor Associated Kinase-2. Death Domain (DD) of Interleukin-1 Receptor-Associated Kinase 1 (IRAK1). IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. They are involved in signal transduction pathways involving IL-1 and IL-18 receptors, Toll-like receptors (TLRs), nuclear factor-kappaB (NF-kB), and mitogen-activated protein kinases (MAPKs). IRAKs contain an N-terminal DD domain and a C-terminal kinase domain. IRAK2 is an essential component of several signaling pathways, including NF-kappaB and the IL-1 signaling pathways. It is an inactive kinase that participates in septic shock mediated by TLR4 and TLR9. It plays a redundant role with IRAK1 in early NF-kB and MAPK responses, and remains present at later stages whereas IRAK1 disappears. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
PYVYQLPAWVLDDFCRNMDALSDWDWMRFASYVITDQTQLRKIKSMEWTGVSITRELMWWWGMRLATVQQ
LVDLLQRLELYRAAQIIL
>gnl|CDD|260062 cd08796, Death_IRAK-M, Death domain of Interleukin 1 Receptor Associated Kinase-M. Death Domain (DD) of Interleukin-1 Receptor-Associated Kinase M (IRAK-M). IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. They are involved in signal transduction pathways involving IL-1 and IL-18 receptors, Toll-like receptors(TLRs), nuclear factor-kappaB (NF-kB), and mitogen-activated protein kinases (MAPKs). IRAKs contain an N-terminal DD domain and a C-terminal kinase domain. IRAK-M, also called IRAK-3, is an inactive kinase present only in macrophages in an inducible manner. It is a negative regulator of TLR signaling and it contributes to the attenuation of NF-kB activation. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
TLLFDVPPVLMEKFCALLDSGDDSLGWRGLAERISSSWLEVRHIEKYVAQGKSPTRELLWSWAQKNKTVG
DLLKVLEDMGHYRAIQLFT
>gnl|CDD|260063 cd08797, Death_NFkB1_p105, Death domain of the Nuclear Factor-KappaB1 precursor protein p105. Death Domain (DD) of the Nuclear Factor-KappaB1 (NF-kB1) precursor protein p105. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). NF-kB1 (or p50) is produced from the processing of the precursor protein p105, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the classical (or canonical) NF-kB pathway. In the cytosol, p50 forms an inactive complex with RelA (or p65) and the Inhibitor of NF-kB (IkB). Activation is triggered by the phosphorylation and degradation of IkB, resulting in the active DNA-binding p50-RelA dimer to migrate to the nucleus. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
VKQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEA
IEVIEE
>gnl|CDD|176776 cd08798, Death_NFkB2_p100, Death domain of the Nuclear Factor-KappaB2 precursor protein p100. Death Domain (DD) of the Nuclear Factor-KappaB2 (NF-kB2) precursor protein p100. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). NF-kB2 (or p52) is produced from the processing of the precursor protein p100, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the non-canonical NF-kB pathway. The p100 precursor is cytosolic and interacts with RelB. Upon phosphorylation by IKKalpha, p100 is processed to its 52kDa active, DNA-binding form and the p52/RelB complex is translocated into the nucleus. The non-canonical pathway plays a role in adaptive immunity and lymphorganogenesis. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREG
VRLLRK
>gnl|CDD|260064 cd08799, Death_UNC5C, Death domain found in Uncoordinated-5C. Death Domain (DD) found in Uncoordinated-5C (UNC5C). UNC5C is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a role in axonal guidance, angiogenesis, and apoptosis. UNC5C plays a critical role in the development of spinal accessory motor neurons. Methylation of the UNC5C gene is associated with early stages of colorectal carcinogenesis. UNC5 proteins are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
IPLSIRQKLCGSLDAPQTRGNDWRMLAHKLNLDRYLNYFATKSSPTGVILDLWEAQHFPDGNLSRLAAVL
EEMGRHETVVSLA
>gnl|CDD|260065 cd08800, Death_UNC5A, Death domain found in Uncoordinated-5A. Death Domain (DD) found in Uncoordinated-5A (UNC5A). UNC5A is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a critical role in neuronal development and differentiation, as well as axon-guidance. It also plays a role in regulating apoptosis in non-neuronal cells as a downstream target of p53. UNC5 proteins are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
IPFLIRQKIISSLDPPCPRGADWRTLAQKLNLDSHLSFFASKSSPTAMILNLWEAQHFPNGNLSQLAAVV
AEIGKQDAMLFLVS
>gnl|CDD|176779 cd08801, Death_UNC5D, Death domain found in Uncoordinated-5D. Death Domain (DD) found in Uncoordinated-5D (UNC5D). UNC5D is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a role in axonal guidance, angiogenesis, and apoptosis. UNC5 proteins are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
IPYSIRQRICATFDTPNAKGKDWQMLAQKNSIDRNLSYFATQSSPSAVILSLWEARHQHDGDLDSLACAL
EEIGRTHSKQSTIAETLDRESDFNYSRQ
>gnl|CDD|176780 cd08802, Death_UNC5B, Death domain found in Uncoordinated-5B. Death Domain (DD) found in Uncoordinated-5B (UNC5B). UNC5B is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a role in axonal guidance, angiogenesis, and apoptosis. UNC5B signaling is involved in the netrin-1-induced proliferation and migration of renal proximal tubular cells. It is also required for vascular patterning during embryonic development, and its activation inhibits sprouting angiogenesis. UNC5 proteins are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
IPLSIRQKICNSLDAPNSRGNDWRLLAQKLSMDRYLNYFATKASPTGVILDLWEARHQDDGDLNSLASAL
EEMGKSEMLVVMAT
>gnl|CDD|176781 cd08803, Death_ank3, Death domain of Ankyrin-3. Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-3, also called anykyrin-G (for general or giant), is found in neurons and at least one splice variant has been shown to be essential for propagation of action potentials as a binding partner to neurofascin and voltage-gated sodium channels. It is required for maintaining axo-dendritic polarity, and may be a genetic risk factor associated with bipolar disorder. ANK-3 may also play roles in other cell types. Mutations affecting ANK-3 pathways for Na channel localization are associated with Brugada syndrome, a potentially fatal arrythmia. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSV
LTKINRIDIVTLLE
>gnl|CDD|260066 cd08804, Death_ank2, Death domain of Ankyrin-2. Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-2, also called ankyrin-B (for broadly expressed), is required for proper function of the Na/Ca ion exchanger-1 in cardiomyocytes, and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. Human ANK-2 is associated with "Ankyrin-B syndrome", an atypical arrythmia disorder with risk of sudden cardiac death. It also plays key roles in the brain and striated muscle. Loss of ANK-2 is associated with significant nervous system defects and sarcomere disorganization. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQC
LTKINRMDIVHLME
>gnl|CDD|260067 cd08805, Death_ank1, Death domain of Ankyrin-1. Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-1, also called ankyrin-R (for restricted), is found in brain, muscle, and erythrocytes and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. It plays a critical nonredundant role in erythroid development and is associated with hereditary spherocytosis (HS), a common disorder of the red cell membrane. The small alternatively-spliced variant, sANK-1, found in striated muscle and concentrated in the sarcoplasmic reticulum (SR) binds obscurin and titin, which facilitates the anchoring of the network SR to the contractile apparatus. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPA
LYSIDRLTIVNILE
>gnl|CDD|260068 cd08806, CARD_CARD14_CARMA2, Caspase activation and recruitment domain of CARD14-like proteins. Caspase activation and recruitment domain (CARD) similar to that found in CARD14, also known as BIMP2 or CARMA2 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 2). CARD14 has been identified as a novel member of the MAGUK (membrane-associated guanylate kinase) family that functions as upstream activators of BCL10 (B-cell lymphoma 10) and NF-kB signaling. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
LWELINDNRHRIVLGIRPCRLIPYLRQARVLTQLDEDEILHCPRLTNRSMRTSHMLDLLRTQGRNGAIAL
LESLMIHYPTLYTQVT
>gnl|CDD|260069 cd08807, CARD_CARD10_CARMA3, Caspase activation and recruitment domain of CARD10-like proteins. Caspase activation and recruitment domain (CARD) similar to that found in CARD10, also known as CARMA3 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 3) or BIMP1. The CARMA3-BCL10-MALT1 signalosome plays a role in the GPCR-induced NF-kB activation. CARMA3 is more widely expressed than CARMA1, which is found only in hematopoietic cells. In endothelial and smooth muscle cells, CARMA3-mediated NF-kB activation induces pro-inflammatory signals within the vasculature and is a key factor in atherogenesis. In bronchial epithelial cells, CARMA3-mediated NF-kB signaling is important for the development of allergic airway inflammation. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
LWERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAF
LESLEFYYPEHFTLLT
>gnl|CDD|260070 cd08808, CARD_CARD11_CARMA1, Caspase activation and recruitment domain of CARD11-like proteins. Caspase activation and recruitment domain (CARD) similar to that found in CARD11, also known as caspase recruitment domain-containing membrane-associated guanylate kinase protein 1 (CARMA1). CARMA1, together with BCL10 (B-cell lymphoma 10) and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), form the L-CBM signalosome (CBM complex in lymphoid immune cells) which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. CARMA1 associates with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVF
LESLEFYYPELYKLVT
>gnl|CDD|260071 cd08809, CARD_CARD9, Caspase activation and recruitment domain of CARD9-like proteins. Caspase activation and recruitment domain (CARD) similar to that found in CARD9. CARD9 is a central regulator of innate immunity and is highly expressed in dendritic cells and macrophages. Together with BCL10 (B-cell lymphoma 10) and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), it forms the M-CBM signalosome (the CBM complex in myeloid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. CARD9 associates with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
CWNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAF
LESLELYYPQLYKKIT
>gnl|CDD|260072 cd08810, CARD_BCL10, Caspase activation and recruitment domain of B-cell lymphoma 10. Caspase activation and recruitment domain (CARD) similar to that found in BCL10 (B-cell lymphoma 10). BCL10 and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1) are the integral components of CBM signalosomes. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells) and with CARMA1 to form L-CBM (CBM complex in lymphoid immune cells), to mediate activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. Both CARMA1 and CARD9 associate with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
KKEVLEEQRHYLCDKLIADRHFDYLRSKRILTRDDCEEIQCRTTRKKRVDKLLDILAREGPDGLDALIES
IRRNGTQNFLIEKLT
>gnl|CDD|260073 cd08811, CARD_IPS1, Caspase activation and recruitment domain (CARD) found in IPS-1. Caspase activation and recruitment domain (CARD) found in IPS-1 (Interferon beta promoter stimulator protein 1), also known as CARDIF, VISA or MAVS. IPS-1 is an adaptor protein that plays an important role in interferon induction in response to viral infection. It is crucial in triggering innate immunity and in developing adaptive immunity against viral pathogens. The CARD of IPS-1 associates with the CARDs of two RNA helicases, RIG-I and MDA5, which bind viral DNA in the cytoplasm during the initial stage of intracellular antiviral response, leading to the induction of type I interferons. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
FAEDKEYKYLRRNMGVFCHDIKVSEIIPYLPCLTRSDRDEILAKKDMSGNRDTAWTLLDHLQRRPGWVED
FIKALRNCELGHLADELERVYD
>gnl|CDD|176791 cd08813, DED_Caspase_8_r2, Death Effector Domain, repeat 2, of Caspase-8. Death effector domain (DED) found in caspase-8 (CASP8, FLICE), repeat 2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
VSAYRVLLFQLSENVTRDELKSFKFLLQNELPKSKLDDETTLLDIFIEMEKKGILGEDNLDMLKRICAKI
NKSLLKKIEDYEE
>gnl|CDD|260074 cd08814, DED_Caspase_10_r2, Death Effector Domain, repeat 2, of Caspase-10. Death effector domain (DED) found in Caspase-10, repeat 2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-10 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-8 and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
VSSYRQMLYELSENITSEDLKRIIFLLRDSKPKTEMTSLELLRHLEKQGLLTENNLQILEDICKKVSPDL
LKIIEKYKR
>gnl|CDD|176793 cd08815, Death_TNFRSF25_DR3, Death domain of Tumor Necrosis Factor Receptor superfamily 25. Death Domain (DD) found in Tumor Necrosis Factor (TNF) receptor superfamily 25 (TNFRSF25), also known as TRAMP (TNF receptor-related apoptosis-mediating protein), LARD, APO-3, WSL-1, or DR3 (Death Receptor-3). TNFRSF25 is primarily expressed in T cells, is activated by binding to its ligand TL1A, and plays an important role in T-cell function. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
QLYAVMDAVPARRWKEFVRTLGLREAEIEAVELEIGRFRDQQYEMLKRWRQQQPAGLDAVYAALERMGLA
GCAEDLR
>gnl|CDD|260075 cd08816, CARD_RIG-I_r1, Caspase activation and recruitment domain found in RIG-I, first repeat. Caspase activation and recruitment domain (CARD) found in RIG-I (Retinoic acid Inducible Gene I, also known as Ddx58), first repeat. RIG-I is a cytoplasmic RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. RIG-I contains two N-terminal CARD domains and a C-terminal RNA helicase. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. Although very similar in sequence, RIG-I recognizes different sets of viruses compared to MDA5, a related RNA helicase. RIG-I associates with IPS-1 through a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
TALEKRNLRCYRDYIEKILRPSYVLGFMTTWLEDELVERILSEEEKGVTEAAQLFLDAVLQLEEEGWFQG
FLDALLAAGYTGLCEAIENW
>gnl|CDD|260076 cd08817, CARD_RIG-I_r2, Caspase activation and recruitment domain found in RIG-I, second repeat. Caspase activation and recruitment domain (CARD) found in RIG-I (Retinoic acid Inducible Gene I, also known as Ddx58), second repeat. RIG-I is a cytoplasmic RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. RIG-I contains two N-terminal CARD domains and a C-terminal RNA helicase. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. Although very similar in sequence, RIG-I recognizes different sets of viruses compared to MDA5, a related RNA helicase. RIG-I associates with IPS-1 through a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
LEEHRQLLKRIEPSFTKRIKPRDLIPYLSDCLIDRECEEILQIEEQKGMIAGAEKLVECLLRSDKENWPK
TLKLALEKCGYDAASELWPDE
>gnl|CDD|260077 cd08818, CARD_MDA5_r1, Caspase activation and recruitment domain found in MDA5, first repeat. Caspase activation and recruitment domain (CARD) found in MDA5 (melanoma-differentiation-associated gene 5), first repeat. MDA5, also known as IFIH1, contains two N-terminal CARD domains and a C-terminal RNA helicase domain. MDA5 is a cytoplasmic DEAD box RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. Although very similar in sequence, MDA5 recognizes different sets of viruses compared to RIG-I, a related RNA helicase. MDA5 associates with IPS-1 through a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
DENFLYLISCFRPRLKRLIVVEPVLDYLHFLSPEQKERIRQKARTEGNLAAADLLIDAVEKGPHPPGWFR
EFVDALEQGGCDLAARYVNPSL
>gnl|CDD|260078 cd08819, CARD_MDA5_r2, Caspase activation and recruitment domain found in MDA5, second repeat. Caspase activation and recruitment domain (CARD) found in MDA5 (melanoma-differentiation-associated gene 5), second repeat. MDA5, also known as IFIH1, contains two N-terminal CARD domains and a C-terminal RNA helicase domain. MDA5 is a cytoplasmic DEAD box RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. Although very similar in sequence, MDA5 recognizes different sets of viruses compared to RIG-I, a related RNA helicase. MDA5 associates with IPS-1 through a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
NDQCVRLIQLLQPTLVDMKTTDVCDKCLEKGLLTAEDRERILAATENHGNRSGARELLSRIVRQKEGWFS
KFLQALRETEHNNLAEELTGED
>gnl|CDD|187722 cd08820, FMT_core_like_6, Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme
RIVFLGQKPIGEECLRTLLRLQDRGSFEIIAVLTNTSPADVWEGSEPLYDIGSTERNLHKLLEILENKGV
DILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIF
EKRFPIPSDCTVISLYILAHYAAIALFGEHITD
>gnl|CDD|187723 cd08821, FMT_core_like_1, Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme
NIIIASKKAWNRKNFEALKNKTPGKWTIIETKDDLSLEKLTQFNPEYIFFPHWSWIIPKEIFENFECVVF
HMTDLPYGRGGSPLQNLIVRGHYETKISALKMEKGLDTGPIYLKRDLSLKGTAEEIYERASKISLKMIPE
LVTKKPKPIKQEGEPVTFKRRTPEQSNISNEANLEKIYDFIRMLDADGYPSAFIELGNYRIEFSRASLKN
G
>gnl|CDD|187724 cd08822, FMT_core_like_2, Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme
MKIAIAGQKWFGTAVLEALRARGIALLGVAAPEEGDRLAAAARTAGSRGLPRAGVAVLPADAIPPGTDLI
VAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDW
CHVRPGDTAAELWRRALAPMGVKLLTQVIDALLRGGNLPAQPQDERLATWEP
>gnl|CDD|187725 cd08823, FMT_core_like_5, Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme
IVILCNTSMAAPLLGQLLSEGRLAGIAVPAHNASYFPQIFVFTGIRRLVSKQRVDTANLKEQLAEWLRAL
AADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPI
VLEQFTPIHPDDTYGLLCSRLAMLAVGLLEELYQNLA
>gnl|CDD|193585 cd08824, LOTUS, LOTUS is an uncharacterized small globular domain found in Limkain b1, Oskar and Tudor-containing proteins 5 and 7. LOTUS is an uncharacterized small globular domain found in Limkain b1, Oskar and Tudor-containing proteins 5 and 7. The LOTUS containing proteins are germline-specific and are found in the nuage/polar granules of germ cells. Tudor-containing protein 5 and 7 belong to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 and TDRD7 are components of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. Oskar protein is a critical component of the pole plasm in the Drosophila oocyte, which is required for germ cell formation. Limkain b1 is a novel human autoantigen, localized to a subset of ABCD3 and PXF marked peroxisomes. Limkain b1 may be a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. Limkain b1 contains multiple copies of LOTUS domains and a conserved RNA recognition motif. The exact molecular function of LOTUS domain remains to be characterized. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
LKQLAKQLRSLLQSYPGGLPLSKLPQLYKKKFGKPLDLSEYGFSKLSDLLEALPGVVIVLSQGGERIVSL
>gnl|CDD|259807 cd08825, MVP_shoulder, Shoulder domain of the major vault protein. The major vault protein is the major polypeptide component of a large cellular ribonuclear protein complex found in the cytoplasm of eukaryotic cells. Its shoulder domain appears to be a homolog of the SPFH core domain. Vault proteins may be involved in detoxification processes, and have been associated with the multi-drug resistance (MDR) phenotype in malignancies. Presumably they play a role in transport processes
NQIKALCLLLGPDFMTDIITVETADHARLQLQLAYNWHFDVDDKKPEEAAKLFSVPDFIGDACKAIASRI
RGAVASVTFDDFHKNSARIIRSAVFGDDEKGEVRDELRFPANNLVITNVDIQSVEPVDQRTRDSLQKSVQ
LAIEITTNSQE
>gnl|CDD|259808 cd08826, SPFH_eoslipins_u1, Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized. This subgroup contains PH1511 from the hyperthermophilic archaeon Pyrococcus horikoshi
PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVV
GQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAE
GELQAAEKLAEAAEILAKSPGALQLRYLQTLSEIASEK
>gnl|CDD|259809 cd08827, SPFH_podocin, Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in vertebrates. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Podocin is expressed in the kidney and mutations in the gene have been linked to familial idiopathic nephrotic syndrome. Podocin interacts with the TRP ion channel TRPV-6 and may function as a scaffolding protein in the organization of lipid-protein domains
WFCVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDA
ICYYRIENASVCLSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVE
RAEIKDVNLPPELQHSFAVEAEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLR
SEKPSTVVLPLPF
>gnl|CDD|259810 cd08828, SPFH_SLP-3, Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in vertebrates. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this slipin subgroup remain uncharacterized, except for Caenorhabditis elegans UNC-1. Mutations in the unc-1 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics
KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLL
AQTTLRNVLGTQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATRE
ARAKVVAAEGEMNA
>gnl|CDD|259811 cd08829, SPFH_paraslipin, Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in all three kingdoms of life. The conserved domain common to these families has also been referred to as the Band 7 domain. Individual proteins of the SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This subgroup of the SLPs remains largely uncharacterized. It includes human SLP-2 which is upregulated and involved in the progression and development in several types of cancer, including esophageal squamous cell carcinoma, endometrial adenocarcinoma, breast cancer, and glioma
AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMEL
DETLSSREEINAKLLEALDEATDPWGVKVTRVEIKDITPPE
>gnl|CDD|350059 cd08830, ArfGap_ArfGap1, Arf1 GTPase-activating protein 1. ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) domain is a part of ArfGap1-like proteins that play a crucial role in controlling of membrane trafficking, particularly in the formation of COPI (coat protein complex I)-coated vesicles on Golgi membranes. The ArfGAP1 protein subfamily consists of three members: ArfGAP1 (Gcs1p in yeast), ArfGAP2 and ArfGAP3 (both are homologs of yeast Glo3p). ArfGAP2/3 are closely related, but with little similarity to ArfGAP1, except the catalytic ArfGAP domain. They promote hydrolysis of GTP bound to the small G protein ADP-ribosylation factor 1 (Arf1), which leads to the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. Thus, the GAP catalytic activity plays a key role in the formation of COPI vesicles from Golgi membrane. In contrast to ArfGAP1, which displays membrane curvature-dependent ArfGAP activity, ArfGAP2 and ArfGAP3 activities are dependent on coatomer (the core COPI complex) which required for efficient recruitment of ArfGAP2 and ArfGAP3 to the Golgi membrane. Accordingly, ArfGAP2/3 has been implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Unlike ArfGAP1, which is controlled by membrane curvature through its amphipathic lipid packing sensor (ALPS) motifs, ArfGAP2/3 do not possess ALPS motif
ARAVLRELQKLPGNNRCFDCGAPNPQWASVSYGIFICLECSGVHRGLGVHISFVRSITMDSWSEKQLKKM
ELGGNAKLREFFESYGISPDLPIREKYNSKAAELYREKLAAEAEG
>gnl|CDD|350060 cd08831, ArfGap_ArfGap2_3_like, Arf1 GTPase-activating protein 2/3-like. ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) domain is a part of ArfGap1-like proteins that play a crucial role in controlling of membrane trafficking, particularly in the formation of COPI (coat protein complex I)-coated vesicles on Golgi membranes. The ArfGAP1 protein subfamily consists of three members: ArfGAP1 (Gcs1p in yeast), ArfGAP2 and ArfGAP3 (both are homologs of yeast Glo3p). ArfGAP2/3 are closely related, but with little similarity to ArfGAP1, except the catalytic ArfGAP domain. They promote hydrolysis of GTP bound to the small G protein ADP-ribosylation factor 1 (Arf1), which leads to the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. Thus, the GAP catalytic activity plays a key role in the formation of COPI vesicles from Golgi membrane. In contrast to ArfGAP1, which displays membrane curvature-dependent ArfGAP activity, ArfGAP2 and ArfGAP3 activities are dependent on coatomer (the core COPI complex) which required for efficient recruitment of ArfGAP2 and ArfGAP3 to the Golgi membrane. Accordingly, ArfGAP2/3 has been implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Unlike ArfGAP1, which is controlled by membrane curvature through its amphipathic lipid packing sensor (ALPS) motifs, ArfGAP2/3 do not possess ALPS motif
ERDAIFKKLRSKPENKVCFDCGAKNPTWASVTFGVFLCLDCSGVHRSLGVHISFVRSTNLDSWTPEQLRR
MKVGGNAKAREFFKQHGGLLSGDIKQKYTSRAAQKYKEKLDKLVAK
>gnl|CDD|350061 cd08832, ArfGap_ADAP, ArfGap with dual PH domains. The ADAP subfamily, ArfGAPs with dual pleckstrin homology (PH) domains, includes two members: ADAP1 and ADAP2. Both ADAP1 (also known as centaurin-alpha1, p42(IP4), or PIP3BP) and ADAP2 (centaurin-alpha2) display a GTPase-activating protein (GAP) activity toward Arf6 (ADP-ribosylation factor 6), which is involved in protein trafficking that regulates endocytic recycling, cytoskeleton remodeling, and neuronal differentiation. ADAP2 has high sequence similarity to the ADAP1 and they both contain a ArfGAP domain at the N-terminus, followed by two PH domains. However, ADAP1, unlike ADAP2, contains a putative N-terminal nuclear localization signal. The PH domains of ADAP1bind to the two second messenger molecules phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) and inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) with identical high affinity, whereas those of ADAP2 specifically binds phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) and PI(3,4,5)P3, which are produced by activated phosphatidylinositol 3-kinase. ADAP1 is predominantly expressed in the brain neurons, while ADAP2 is broadly expressed, including the adipocytes, heart, and skeletal muscle but not in the brain. The limited distribution and high expression of ADAP1 in the brain indicates that ADAP1 is important for neuronal functions. ADAP1 has been shown to highly expressed in the neurons and plagues of Alzheimer's disease patients. In other hand, ADAP2 gene deletion has been shown to cause circulatory deficiencies and heart shape defects in zebrafish, indicating that ADAP2 has a vital role in heart development. Taken together, the hemizygous deletion of ADAP2 gene may be contributing to the cardiovascular malformation in patients with neurofibromatosis type 1 (NF1) microdeletions
AERNKKRLLELLKLPGNNTCADCGAPDPEWASYNLGVFICLDCSGIHRSLGTHISKVKSLRLDNWDDSQV
EFMEENGNEKAKAKYEAHVPAFYRRPTPTDPQVLREQWIRAKY
>gnl|CDD|350062 cd08833, ArfGap_GIT, The GIT subfamily of ADP-ribosylation factor GTPase-activating proteins. The GIT (G-protein coupled receptor kinase-interacting protein) subfamily includes GIT1 and GIT2, which have three ANK repeats, a Spa-homology domain (SHD), a coiled-coil domain and a C-terminal paxillin-binding site (PBS). The GIT1/2 proteins are GTPase-activating proteins that function as an inactivator of Arf signaling, and interact with the PIX/Cool family of Rac/Cdc42 guanine nucleotide exchange factors (GEFs). Unlike other ArfGAPs, GIT and PIX (Pak-interacting exchange factor) proteins are tightly associated to form an oligomeric complex that acts as a scaffold and signal integrator that can be recruited for multiple signaling pathways. The GIT/PIX complex functions as a signaling scaffold by binding to specific protein partners. As a result, the complex is transported to specific cellular locations. For instance, the GIT partners paxillin or integrin-alpha4 (to focal adhesions), piccolo and liprin-alpha (to synapses), and the beta-PIX partner Scribble (to epithelial cell-cell contacts and synapses). Moreover, the GIT/PIT complex functions to integrate signals from multiple GTP-binding protein and protein kinase pathways to regulate the actin cytoskeleton and thus cell polarity, adhesion and migration
IRGKSSNARVCADCSAPDPEWASINRGVLICDECCSIHRSLGRHISQVKSLRKDQWPPSLLEMVQTLGNN
GANSIWEHSLLDPSQSGKRKPIPPDPVHPTKEEFIKAKY
>gnl|CDD|350063 cd08834, ArfGap_ASAP, ArfGAP domain of ASAP (Arf GAP, SH3, ANK repeat and PH domains) subfamily of ADP-ribosylation factor GTPase-activating proteins. The ArfGAPs are a family of multidomain proteins with a common catalytic domain that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. ASAP-subfamily GAPs include three members: ASAP1, ASAP2, ASAP3. The ASAP subfamily comprises Arf GAP, SH3, ANK repeat and PH domains. From the N-terminus, each member has a BAR, PH, Arf GAP, ANK repeat, and proline rich domains. Unlike ASAP3, ASAP1 and ASAP2 also have an SH3 domain at the C-terminus. ASAP1 and ASAP2 show strong GTPase-activating protein (GAP) activity toward Arf1 and Arf5 and weak activity toward Arf6. ASAP1 is a target of Src and FAK signaling that regulates focal adhesions, circular dorsal ruffles (CDR), invadopodia, and podosomes. ASAP1 GAP activity is synergistically stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. ASAP2 is believed to function as an ArfGAP that controls ARF-mediated vesicle budding when recruited to Golgi membranes. It also functions as a substrate and downstream target for protein tyrosine kinases Pyk2 and Src, a pathway that may be involved in the regulation of vesicular transport. ASAP3 is a focal adhesion-associated ArfGAP that functions in cell migration and invasion. Similar to ASAP1, the GAP activity of ASAP3 is strongly enhanced by PIP2 via PH domain. Like ASAP1, ASAP3 associates with focal adhesions and circular dorsal ruffles. However, unlike ASAP1, ASAP3 does not localize to invadopodia or podosomes. Both ASAP 1 and 3 have been implicated in oncogenesis, as ASAP1 is highly expressed in metastatic breast cancer and ASAP3 in hepatocellular carcinoma
LTKSIIAEVKRLPGNDVCCDCGSPDPTWLSTNLGILTCIECSGVHRELGVHVSRIQSLTLDNLGTSELLL
ARNLGNEGFNEIMEANLPPGYKPTPNSDMEERKDFIRAKYVEKKFVV
>gnl|CDD|350064 cd08835, ArfGap_ACAP, ArfGAP domain of ACAP (ArfGAP with Coiled-coil, ANK repeat and PH domains) proteins. ArfGAP domain is an essential part of ACAP proteins that play important role in endocytosis, actin remodeling and receptor tyrosine kinase-dependent cell movement. ACAP subfamily of ArfGAPs are composed of coiled coils (BAR, Bin-Amphiphysin-Rvs), PH, ArfGAP and ANK repeats domains. ACAP1 (centaurin beta1) and ACAP2 centaurin beta2) have a GAP (GTPase-activating protein) activity preferentially toward Arf6, which regulates endocytic recycling. Both ACAP1/2 are activated by are activated by the phosphoinositides, PI(4,5)P2 and PI(3,5)P2. ACAP1 binds specifically with recycling cargo proteins such as transferrin receptor (TfR) and cellubrevin. Thus, ACAP1 promotes cargo sorting to enhance TfR recycling from the recycling endosome. In addition, phosphorylation of ACAP by Akt, a serine/threonine protein kinase, regulates the recycling of integrin beta1 to control cell migration. In contrast, ACAP2 does not exhibit a similar interaction with the recycling cargo proteins. It has been shown that ACAP2 functions both as an effector of Ras-related protein Rab35 and as an Arf6-GTPase-activating protein (GAP) during neurite outgrowth of PC12 cells. In addition, ACAP2, together with Rab35, regulates phagocytosis in mammalian macrophages. ACAP3 also positively regulates neurite outgrowth through its GAP activity specific to Arf6 in mouse hippocampal neurons
GSALEQVLSVPGNAQCCDCGSPDPRWASINLGVTLCIECSGIHRSLGVHVSKVRSLTLDSWEPELLKVML
ELGNDVVNRIYEANVPDDGSVKPTPDSSRQEREAWIRAKYVEKKFV
>gnl|CDD|350065 cd08836, ArfGap_AGAP, ArfGAP with GTPase domain, ANK repeat and PH domains. The AGAP subfamily of ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) includes three members: AGAP1-3. In addition to the Arf GAP domain, AGAP proteins contain GTP-binding protein-like, ANK repeat and pleckstrin homology (PH) domains. AGAP1 and AGAP2 have phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-mediated GTPase-activating protein (GAP) activity preferentially toward Arf1, and function in the endocytic system. AGAP1 and AGAP2 independently regulate AP-3 endosomes and AP-1/Rab4 fast recycling endosomes, respectively. AGAP1, via its PH domain, directly interacts with the adapter protein 3 (AP-3), which is a coat protein involved in trafficking in the endosomal-lysosomal system, and regulates AP-3-dependent trafficking. In other hand, AGAP2 specifically binds the clathrin adaptor protein AP-1 and regulates the AP-1/Rab-4 dependent endosomal trafficking. AGAP2 is overexpressed in different human cancers including prostate carcinoma and glioblastoma, and promotes cancer cell invasion. AGAP3 exists as a component of the NMDA receptor complex that regulates Arf6 and Ras/ERK signaling pathways. Moreover, AGAP3 regulates AMPA receptor trafficking through the ArfGAP domain. Together, AGAP3 is believed to involve in linking NMDA receptor activation to AMPA receptor trafficking
AALQAIRNVRGNDHCVDCGAPNPDWASLNLGALMCIECSGIHRNLGTHISRVRSLDLDDWPVELLKVMSA
IGNDLANSVWEGNTQGRTKPTPDSSREEKERWIRAKYE
>gnl|CDD|350066 cd08837, ArfGap_ARAP, ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing proteins. The ARAP subfamily includes three members, ARAP1-3, and belongs to the ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) family of proteins that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. The function of Arfs is dependent on GAPs and guanine nucleotide exchange factors (GEFs), which allow Arfs to cycle between the GDP-bound and GTP-bound forms. In addition to the Arf GAP domain, ARAPs contain the SAM (sterile-alpha motif) domain, 5 pleckstrin homology (PH) domains, the Rho-GAP domain, the Ras-association domain, and ANK repeats. ARAPs show phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3)-dependent GAP activity toward Arf6. ARAPs play important roles in endocytic trafficking, cytoskeleton reorganization in response to growth factors stimulation, and focal adhesion dynamics
YEVAEKIWSNPANRFCADCGAPDPDWASINLCVVICKQCAGEHRSLGSNISKVRSLKMDTKVWTEELVEL
FLKLGNDRANRFWAANLPPSEALHPDADSEQRREFITAKYREGKYR
>gnl|CDD|350067 cd08838, ArfGap_AGFG, ArfGAP domain of the AGFG subfamily (ArfGAP domain and FG repeat-containing proteins). The ArfGAP domain and FG repeat-containing proteins (AFGF) subfamily of Arf GTPase-activating proteins consists of the two structurally-related members: AGFG1 and AGFG2. AGFG1 (alias: HIV-1 Rev binding protein, HRB; Rev interacting protein, RIP; Rev/Rex activating domain-binding protein, RAB) and AGFG2 are involved in the maintenance and spread of immunodeficiency virus type 1 (HIV-1) infection. The ArfGAP domain of AGFG is related to nucleoporins, which is a class of proteins that mediate nucleocytoplasmic transport. AGFG plays a role in the Rev export pathway, which mediates the nucleocytoplasmic transfer of proteins and RNAs, possibly together by the nuclear export receptor CRM1. In humans, the presence of the FG repeat motifs (11 in AGFG1 and 7 in AGFG2) are thought to be required for these proteins to act as HIV-1 Rev cofactors. Hence, AGFG promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm, which is an essential step for HIV-1 replication
EKILRELLKLPENKRCFDCGQRGPTYVNLTFGTFVCTTCSGIHREFNHRVKSISMSTFTPEEVEFLQAGG
NEVARKIWLAKWDPRTDPEPDSGDDQKIREFIRLKYVDKRWYD
>gnl|CDD|350068 cd08839, ArfGap_SMAP, Stromal membrane-associated proteins; a subfamily of the ArfGAP family. The SMAP subfamily of Arf GTPase-activating proteins consists of the two structurally-related members, SMAP1 and SMAP2. Each SMAP member exhibits common and distinct functions in vesicle trafficking. They both bind to clathrin heavy chain molecules and are involved in the trafficking of clathrin-coated vesicles. SMAP1 preferentially exhibits GAP toward Arf6, while SMAP2 prefers Arf1 as a substrate. SMAP1 is involved in Arf6-dependent vesicle trafficking, but not Arf6-mediated actin cytoskeleton reorganization, and regulates clathrin-dependent endocytosis of the transferrin receptors and E-cadherin. SMAP2 regulates Arf1-dependent retrograde transport of TGN38/46 from the early endosome to the trans-Golgi network (TGN). SMAP2 has the Clathrin Assembly Lymphoid Myeloid (CALM)-binding domain, but SMAP1 does not
LAKLLREEDNKYCADCGAKGPRWASWNLGVFICIRCAGIHRNLGVHISKVKSVNLDSWTPEQVQSMQEMG
NARANAYYEANLPDGFRRPQTDSALENFIRDKY
>gnl|CDD|350069 cd08843, ArfGap_ADAP1, ADAP1 GTPase activating protein for Arf, with dual PH domains. The ADAP subfamily, ArfGAPs with dual pleckstrin homology (PH) domains, includes two members: ADAP1 and ADAP2. Both ADAP1 (also known as centaurin-alpha1, p42(IP4), or PIP3BP) and ADAP2 (centaurin-alpha2) display a GTPase-activating protein (GAP) activity toward Arf6 (ADP-ribosylation factor 6), which is involved in protein trafficking that regulates endocytic recycling, cytoskeleton remodeling, and neuronal differentiation. ADAP2 has high sequence similarity to the ADAP1 and they both contain a ArfGAP domain at the N-terminus, followed by two PH domains. However, ADAP1, unlike ADAP2, contains a putative N-terminal nuclear localization signal. The PH domains of ADAP1bind to the two second messenger molecules phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) and inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) with identical high affinity, whereas those of ADAP2 specifically binds phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) and PI(3,4,5)P3, which are produced by activated phosphatidylinositol 3-kinase. ADAP1 is predominantly expressed in the brain neurons, while ADAP2 is broadly expressed, including the adipocytes, heart, and skeletal muscle but not in the brain. The limited distribution and high expression of ADAP1 in the brain indicates that ADAP1 is important for neuronal functions. ADAP1 has been shown to highly expressed in the neurons and plagues of Alzheimer's disease patients. In other hand, ADAP2 gene deletion has been shown to cause circulatory deficiencies and heart shape defects in zebrafish, indicating that ADAP2 has a vital role in heart development. Taken together, the hemizygous deletion of ADAP2 gene may be contributing to the cardiovascular malformation in patients with neurofibromatosis type 1 (NF1) microdeletions
GKERRRAVLELLQRPGNARCADCGAPDPDWASYTLGVFICLSCSGIHRNIPQVSKVKSVRLDAWEEAQVE
FMASHGNDAARARFESKVPSFYYRPTPSDCQLLREQWIRAKY
>gnl|CDD|350070 cd08844, ArfGap_ADAP2, ADAP2 GTPase activating protein for Arf, with dual PH domains. The ADAP subfamily, ArfGAPs with dual pleckstrin homology (PH) domains, includes two members: ADAP1 and ADAP2. Both ADAP1 (also known as centaurin-alpha1, p42(IP4), or PIP3BP) and ADAP2 (centaurin-alpha2) display a GTPase-activating protein (GAP) activity toward Arf6 (ADP-ribosylation factor 6), which is involved in protein trafficking that regulates endocytic recycling, cytoskeleton remodeling, and neuronal differentiation. ADAP2 has high sequence similarity to the ADAP1 and they both contain a ArfGAP domain at the N-terminus, followed by two PH domains. However, ADAP1, unlike ADAP2, contains a putative N-terminal nuclear localization signal. The PH domains of ADAP1bind to the two second messenger molecules phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) and inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) with identical high affinity, whereas those of ADAP2 specifically binds phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) and PI(3,4,5)P3, which are produced by activated phosphatidylinositol 3-kinase. ADAP1 is predominantly expressed in the brain neurons, while ADAP2 is broadly expressed, including the adipocytes, heart, and skeletal muscle but not in the brain. The limited distribution and high expression of ADAP1 in the brain indicates that ADAP1 is important for neuronal functions. ADAP1 has been shown to highly expressed in the neurons and plagues of Alzheimer's disease patients. In other hand, ADAP2 gene deletion has been shown to cause circulatory deficiencies and heart shape defects in zebrafish, indicating that ADAP2 has a vital role in heart development. Taken together, the hemizygous deletion of ADAP2 gene may be contributing to the cardiovascular malformation in patients with neurofibromatosis type 1 (NF1) microdeletions
RDRNKKRLLELLKLPGNSVCADCGAPDPDWASYTLGIFICLNCSGVHRNLPDISRVKSIRLDFWEDELVE
FMKENGNLKAKAKFEAFVPPFYYRPQANDCDVLKEQWIRAKY
>gnl|CDD|350071 cd08846, ArfGap_GIT1, GIT1 GTPase activating protein for Arf. The GIT (G-protein coupled receptor kinase-interacting protein) subfamily includes GIT1 and GIT2, which have three ANK repeats, a Spa-homology domain (SHD), a coiled-coil domain and a C-terminal paxillin-binding site (PBS). The GIT1/2 proteins are GTPase-activating proteins that function as an inactivator of Arf signaling, and interact with the PIX/Cool family of Rac/Cdc42 guanine nucleotide exchange factors (GEFs). Unlike other ArfGAPs, GIT and PIX (Pak-interacting exchange factor) proteins are tightly associated to form an oligomeric complex that acts as a scaffold and signal integrator that can be recruited for multiple signaling pathways. The GIT/PIX complex functions as a signaling scaffold by binding to specific protein partners. As a result, the complex is transported to specific cellular locations. For instance, the GIT partners paxillin or integrin-alpha4 (to focal adhesions), piccolo and liprin-alpha (to synapses), and the beta-PIX partner Scribble (to epithelial cell-cell contacts and synapses). Moreover, the GIT/PIT complex functions to integrate signals from multiple GTP-binding protein and protein kinase pathways to regulate the actin cytoskeleton and thus cell polarity, adhesion and migration
MSRKGPRAEVCADCSAPDPGWASINRGVLICDECCSVHRSLGRHISIVKHLRHSAWPPTLLQMVHTLASN
GANSIWEHSLLDPAQVQSGRRKANPQDKVHPTKSEFIRAKY
>gnl|CDD|350072 cd08847, ArfGap_GIT2, GIT2 GTPase activating protein for Arf. The GIT (G-protein coupled receptor kinase-interacting protein) subfamily includes GIT1 and GIT2, which have three ANK repeats, a Spa-homology domain (SHD), a coiled-coil domain and a C-terminal paxillin-binding site (PBS). The GIT1/2 proteins are GTPase-activating proteins that function as an inactivator of Arf signaling, and interact with the PIX/Cool family of Rac/Cdc42 guanine nucleotide exchange factors (GEFs). Unlike other ArfGAPs, GIT and PIX (Pak-interacting exchange factor) proteins are tightly associated to form an oligomeric complex that acts as a scaffold and signal integrator that can be recruited for multiple signaling pathways. The GIT/PIX complex functions as a signaling scaffold by binding to specific protein partners. As a result, the complex is transported to specific cellular locations. For instance, the GIT partners paxillin or integrin-alpha4 (to focal adhesions), piccolo and liprin-alpha (to synapses), and the beta-PIX partner Scribble (to epithelial cell-cell contacts and synapses). Moreover, the GIT/PIT complex functions to integrate signals from multiple GTP-binding protein and protein kinase pathways to regulate the actin cytoskeleton and thus cell polarity, adhesion and migration
MSKRLRSSEVCADCSTSDPRWASVNRGVLICDECCSVHRSLGRHISQVRHLKHTSWPPTLLQMVQTLYNN
GANSIWEHSLLDPASIMSGKRKANPQDKVHPNKAEFIRAKY
>gnl|CDD|350073 cd08848, ArfGap_ASAP1, ArfGAP domain of ASAP1 (ArfGAP with SH3 domain, ANK repeat and PH domain-containing protein 1). The ArfGAPs are a family of multidomain proteins with a common catalytic domain that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. ASAP-subfamily GAPs include three members: ASAP1, ASAP2, ASAP3. The ASAP subfamily comprises Arf GAP, SH3, ANK repeat and PH domains. From the N-terminus, each member has a BAR, PH, Arf GAP, ANK repeat, and proline rich domains. Unlike ASAP3, ASAP1 and ASAP2 also have an SH3 domain at the C-terminus. ASAP1 and ASAP2 show strong GTPase-activating protein (GAP) activity toward Arf1 and Arf5 and weak activity toward Arf6. ASAP1 is a target of Src and FAK signaling that regulates focal adhesions, circular dorsal ruffles (CDR), invadopodia, and podosomes. ASAP1 GAP activity is synergistically stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. ASAP2 is believed to function as an ArfGAP that controls ARF-mediated vesicle budding when recruited to Golgi membranes. It also functions as a substrate and downstream target for protein tyrosine kinases Pyk2 and Src, a pathway that may be involved in the regulation of vesicular transport. ASAP3 is a focal adhesion-associated ArfGAP that functions in cell migration and invasion. Similar to ASAP1, the GAP activity of ASAP3 is strongly enhanced by PIP2 via PH domain. Like ASAP1, ASAP3 associates with focal adhesions and circular dorsal ruffles. However, unlike ASAP1, ASAP3 does not localize to invadopodia or podosomes. ASAP 1 and 3 have been implicated in oncogenesis, as ASAP1 is highly expressed in metastatic breast cancer and ASAP3 in hepatocellular carcinoma
LTKAIIDDVQRLPGNEVCCDCGSPDPTWLSTNLGILTCIECSGIHREMGVHISRIQSLELDKLGTSELLL
AKNVGNNSFNDIMEGNLPSPSPKPSPSSDMTARKEYITAKYVEHRFSRKTCS
>gnl|CDD|350074 cd08849, ArfGap_ASAP2, ArfGAP domain of ASAP2 (ArfGAP2 with SH3 domain, ANK repeat and PH domain-containing protein 2). The Arf GAPs are a family of multidomain proteins with a common catalytic domain that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. ASAP-subfamily GAPs include three members: ASAP1, ASAP2, ASAP3. The ASAP subfamily comprises Arf GAP, SH3, ANK repeat and PH domains. From the N-terminus, each member has a BAR, PH, Arf GAP, ANK repeat, and proline rich domains. Unlike ASAP3, ASAP1 and ASAP2 also have an SH3 domain at the C-terminus. ASAP1 and ASAP2 show strong GTPase-activating protein (GAP) activity toward Arf1 and Arf5 and weak activity toward Arf6. ASAP1 is a target of Src and FAK signaling that regulates focal adhesions, circular dorsal ruffles (CDR), invadopodia, and podosomes. ASAP1 GAP activity is synergistically stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. ASAP2 is believed to function as an ArfGAP that controls ARF-mediated vesicle budding when recruited to Golgi membranes. It also functions as a substrate and downstream target for protein tyrosine kinases Pyk2 and Src, a pathway that may be involved in the regulation of vesicular transport
LTKEIISEVQRMTGNDVCCDCGAPDPTWLSTNLGILTCIECSGIHRELGVHYSRMQSLTLDVLGTSELLL
AKNIGNAGFNEIMEACLPAEDVVKPNPGSDMNARKDYITAKYIERRYARKKHA
>gnl|CDD|350075 cd08850, ArfGap_ACAP3, ArfGAP domain of ACAP3 (ArfGAP with Coiled-coil, ANK repeat and PH domains 3). ACAP3 belongs to the ACAP subfamily of GAPs (GTPase-activating proteins) for the small GTPase Arf (ADP-ribosylation factor). ACAP subfamily of ArfGAPs are composed of Coiled coli (BAR, Bin-Amphiphysin-Rvs), PH, ArfGAP and ANK repeats domains. It has been shown that ACAP3 positively regulates neurite outgrowth through its GAP activity specific to Arf6 in mouse hippocampal neurons. ACAP1 (centaurin beta1) and ACAP2 centaurin beta2) also have a GAP (GTPase-activating protein) activity preferentially toward Arf6, which regulates endocytic recycling. Both ACAP1/2 are activated by are activated by the phosphoinositides, PI(4,5)P2 and PI(3,5)P2. ACAP1 binds specifically with recycling cargo proteins such as transferrin receptor (TfR) and cellubrevin. Thus, ACAP1 promotes cargo sorting to enhance TfR recycling from the recycling endosome. In addition, phosphorylation of ACAP by Akt, a serine/threonine protein kinase, regulates the recycling of integrin beta1 to control cell migration. In contrast, ACAP2 does not exhibit a similar interaction with the recycling cargo proteins. It has been shown that ACAP2 functions both as an effector of Ras-related protein Rab35 and as an Arf6-GTPase-activating protein (GAP) during neurite outgrowth of PC12 cells. Moreover, ACAP2, together with Rab35, regulates phagocytosis in mammalian macrophages
ESILQRVQSIAGNDQCCDCGQPDPRWASINLGILLCIECSGIHRSLGVHCSKVRSLTLDSWEPELLKLMC
ELGNSTVNQIYEAQCEELGLKKPTASSSRQDKEAWIKAKYVEKKFL
>gnl|CDD|350076 cd08851, ArfGap_ACAP2, ArfGAP domain of ACAP2 (ArfGAP with Coiled-coil, ANK repeat and PH domains 2). ACAP2 belongs to the ACAP subfamily of GAPs (GTPase-activating proteins) for the small GTPase Arf (ADP-ribosylation factor). ACAP subfamily of ArfGAPs are composed of Coiled coli (BAR, Bin-Amphiphysin-Rvs), PH, ArfGAP and ANK repeats domains. ACAP1 (centaurin beta1) and ACAP2 centaurin beta2) have a GAP (GTPase-activating protein) activity preferentially toward Arf6, which regulates endocytic recycling. Both ACAP1/2 are activated by are activated by the phosphoinositides, PI(4,5)P2 and PI(3,5)P2. ACAP1 binds specifically with recycling cargo proteins such as transferrin receptor (TfR) and cellubrevin. Thus, ACAP1 promotes cargo sorting to enhance TfR recycling from the recycling endosome. In addition, phosphorylation of ACAP by Akt, a serine/threonine protein kinase, regulates the recycling of integrin beta1 to control cell migration. In contrast, ACAP2 does not exhibit a similar interaction with the recycling cargo proteins. It has been shown that ACAP2 functions both as an effector of Ras-related protein Rab35 and as an Arf6-GTPase-activating protein (GAP) during neurite outgrowth of PC12 cells. Moreover, ACAP2, together with Rab35, regulates phagocytosis in mammalian macrophages. ACAP3 also positively regulates neurite outgrowth through its GAP activity specific to Arf6 in mouse hippocampal neurons
ESALQRVQCIPGNASCCDCGLADPRWASINLGITLCIECSGIHRSLGVHFSKVRSLTLDTWEPELLKLMC
ELGNDVINRIYEARVEKMGAKKPQPGGQRQEKEAYIRAKYVERKFV
>gnl|CDD|350077 cd08852, ArfGap_ACAP1, ArfGAP domain of ACAP1 (ArfGAP with Coiled-coil, ANK repeat and PH domains 1). ACAP1 belongs to the ACAP subfamily of GAPs (GTPase-activating proteins) for the small GTPase Arf (ADP-ribosylation factor). ACAP subfamily of ArfGAPs are composed of Coiled coli (BAR, Bin-Amphiphysin-Rvs), PH, ArfGAP and ANK repeats domains. ACAP1 (centaurin beta1) and ACAP2 centaurin beta2) have a GAP (GTPase-activating protein) activity preferentially toward Arf6, which regulates endocytic recycling. Both ACAP1/2 are activated by are activated by the phosphoinositides, PI(4,5)P2 and PI(3,5)P2. ACAP1 binds specifically with recycling cargo proteins such as transferrin receptor (TfR) and cellubrevin. Thus, ACAP1 promotes cargo sorting to enhance TfR recycling from the recycling endosome. In addition, phosphorylation of ACAP by Akt, a serine/threonine protein kinase, regulates the recycling of integrin beta1 to control cell migration. In contrast, ACAP2 does not exhibit a similar interaction with the recycling cargo proteins. It has been shown that ACAP2 functions both as an effector of Ras-related protein Rab35 and as an Arf6-GTPase-activating protein (GAP) during neurite outgrowth of PC12 cells. Moreover, ACAP2, together with Rab35, regulates phagocytosis in mammalian macrophages. ACAP3 also positively regulates neurite outgrowth through its GAP activity specific to Arf6 in mouse hippocampal neurons
GHAVAQVQSVDGNAQCCDCREPAPEWASINLGVTLCIQCSGIHRSLGVHFSKVRSLTLDSWEPELVKLMC
ELGNVIINQIYEARIEAMAIKKPGPSSSRQEKEAWIRAKYVEKKFITKLP
>gnl|CDD|350078 cd08853, ArfGap_AGAP2, ArfGAP with GTPase domain, ANK repeat and PH domain 2. The AGAP subfamily of ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) includes three members: AGAP1-3. In addition to the Arf GAP domain, AGAP proteins contain GTP-binding protein-like, ANK repeat and pleckstrin homology (PH) domains. AGAP1 and AGAP2 have phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-mediated GTPase-activating protein (GAP) activity preferentially toward Arf1, and function in the endocytic system. AGAP1 and AGAP2 independently regulate AP-3 endosomes and AP-1/Rab4 fast recycling endosomes, respectively. AGAP1, via its PH domain, directly interacts with the adapter protein 3 (AP-3), which is a coat protein involved in trafficking in the endosomal-lysosomal system, and regulates AP-3-dependent trafficking. In other hand, AGAP2 specifically binds the clathrin adaptor protein AP-1 and regulates the AP-1/Rab-4 dependent endosomal trafficking. AGAP2 is overexpressed in different human cancers including prostate carcinoma and glioblastoma, and promotes cancer cell invasion. AGAP3 exists as a component of the NMDA receptor complex that regulates Arf6 and Ras/ERK signaling pathways. Moreover, AGAP3 regulates AMPA receptor trafficking through the ArfGAP domain. Together, AGAP3 is believed to involve in linking NMDA receptor activation to AMPA receptor trafficking
AMALQSIRNMRGNSHCVDCETQNPKWASLNLGVLMCIECSGIHRNLGTHLSRVRSLDLDDWPVELRKVMS
SIGNELANSIWEGSSQGQTKPSSDSTREEKERWIRAKYE
>gnl|CDD|350079 cd08854, ArfGap_AGAP1, ArfGAP with GTPase domain, ANK repeat and PH domain 1. The AGAP subfamily of ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) includes three members: AGAP1-3. In addition to the Arf GAP domain, AGAP proteins contain GTP-binding protein-like, ANK repeat and pleckstrin homology (PH) domains. AGAP1 and AGAP2 have phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-mediated GTPase-activating protein (GAP) activity preferentially toward Arf1, and function in the endocytic system. AGAP1 and AGAP2 independently regulate AP-3 endosomes and AP-1/Rab4 fast recycling endosomes, respectively. AGAP1, via its PH domain, directly interacts with the adapter protein 3 (AP-3), which is a coat protein involved in trafficking in the endosomal-lysosomal system, and regulates AP-3-dependent trafficking. In other hand, AGAP2 specifically binds the clathrin adaptor protein AP-1 and regulates the AP-1/Rab-4 dependent endosomal trafficking. AGAP2 is overexpressed in different human cancers including prostate carcinoma and glioblastoma, and promotes cancer cell invasion. AGAP3 exists as a component of the NMDA receptor complex that regulates Arf6 and Ras/ERK signaling pathways. Moreover, AGAP3 regulates AMPA receptor trafficking through the ArfGAP domain. Together, AGAP3 is believed to involve in linking NMDA receptor activation to AMPA receptor trafficking
AVAIQAIRNAKGNSLCVDCGAPNPTWASLNLGALICIECSGIHRNLGTHLSRVRSLDLDDWPRELTLVLT
AIGNHMANSIWESCTQGRTKPAPDSSREERESWIRAKYE
>gnl|CDD|350080 cd08855, ArfGap_AGAP3, ArfGAP with GTPase domain, ANK repeat and PH domain 3. The AGAP subfamily of ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) includes three members: AGAP1-3. In addition to the Arf GAP domain, AGAP proteins contain GTP-binding protein-like, ANK repeat and pleckstrin homology (PH) domains. AGAP3 exists as a component of the NMDA receptor complex that regulates Arf6 and Ras/ERK signaling pathways. Moreover, AGAP3 regulates AMPA receptor trafficking through the ArfGAP domain. Together, AGAP3 is believed to involve in linking NMDA receptor activation to AMPA receptor trafficking. AGAP1 and AGAP2 have phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-mediated GTPase-activating protein (GAP) activity preferentially toward Arf1, and function in the endocytic system. AGAP1 and AGAP2 independently regulate AP-3 endosomes and AP-1/Rab4 fast recycling endosomes, respectively. AGAP1, via its PH domain, directly interacts with the adapter protein 3 (AP-3), which is a coat protein involved in trafficking in the endosomal-lysosomal system, and regulates AP-3-dependent trafficking. In other hand, AGAP2 specifically binds the clathrin adaptor protein AP-1 and regulates the AP-1/Rab-4 dependent endosomal trafficking. AGAP2 is overexpressed in different human cancers including prostate carcinoma and glioblastoma, and promotes cancer cell invasion
DALAIQSIRNVRGNSFCIDCDAPNPDWASLNLGALMCIECSGIHRNLGTHLSRVRSLDLDDWPVELSMVM
TAIGNAMANSVWEGALDGYSKPGPDSTREEKERWIRAKYE
>gnl|CDD|350081 cd08856, ArfGap_ARAP2, ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing protein 2. The ARAP subfamily includes three members, ARAP1-3, and belongs to the ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) family of proteins that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. The function of Arfs is dependent on GAPs and guanine nucleotide exchange factors (GEFs), which allow Arfs to cycle between the GDP-bound and GTP-bound forms. In addition to the Arf GAP domain, ARAPs contain the SAM (sterile-alpha motif) domain, 5 pleckstrin homology (PH) domains, the Rho-GAP domain, the Ras-association domain, and ANK repeats. ARAPs show phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3)-dependent GAP activity toward Arf6. ARAPs play important roles in endocytic trafficking, cytoskeleton reorganization in response to growth factors stimulation, and focal adhesion dynamics. ARAP2 localizes to the cell periphery and on focal adhesions composed of paxillin and vinculin, and functions downstream of RhoA to regulate focal adhesion dynamics. ARAP2 is a PI(3,4,5)P3-dependent Arf6 GAP that binds RhoA-GTP, but it lacks the predicted catalytic arginine in the RhoGAP domain and does not have RhoGAP activity. ARAP2 reduces Rac1oGTP levels by reducing Arf6oGTP levels through GAP activity. AGAP2 also binds to and regulates focal adhesion kinase (FAK). Thus, ARAP2 signals through Arf6 and Rac1 to control focal adhesion morphology
ETLSDYEVAEKIWFNESNRSCADCKAPDPDWASINLCVVICKKCAGQHRSLGPKDSKVRSLKMDASIWSN
ELIELFIVVGNKPANLFWAANLFSEEDLHMDSDVEQRTPFITQKYKEGKFR
>gnl|CDD|350082 cd08857, ArfGap_AGFG1, ArfGAP domain of AGFG1 (ArfGAP domain and FG repeat-containing protein 1). The ArfGAP domain and FG repeat-containing proteins (AFGF) subfamily of Arf GTPase-activating proteins consists of the two structurally-related members: AGFG1 and AGFG2. AGFG1 (alias: HIV-1 Rev binding protein, HRB; Rev interacting protein, RIP; Rev/Rex activating domain-binding protein, RAB) and AGFG2 are involved in the maintenance and spread of immunodeficiency virus type 1 (HIV-1) infection. The ArfGAP domain of AGFG1 is related to nucleoporins, which is a class of proteins that mediate nucleocytoplasmic transport. AGFG1 plays a role in the Rev export pathway, which mediates the nucleocytoplasmic transfer of proteins and RNAs, possibly together by the nuclear export receptor CRM1. In humans, the presence of the FG repeat motifs (11 in AGFG1 and 7 in AGFG2) are thought to be required for these proteins to act as HIV-1 Rev cofactors. Hence, AGFG1 promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm, which is an essential step for HIV-1 replication
HLKMLREMTSLPHNRKCFDCDQRGPTYANMTVGSFVCTSCSGILRGLNPPHRVKSISMTTFTQQEIEFLQ
KHGNEVCKQIWLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYV
>gnl|CDD|350083 cd08859, ArfGap_SMAP2, Stromal membrane-associated protein 2; a subfamily of the ArfGAP family. The SMAP subfamily of Arf GTPase-activating proteins consists of the two structurally-related members, SMAP1 and SMAP2. Each SMAP member exhibits common and distinct functions in vesicle trafficking. They both bind to clathrin heavy chain molecules and are involved in the trafficking of clathrin-coated vesicles. SMAP1 preferentially exhibits GAP toward Arf6, while SMAP2 prefers Arf1 as a substrate. SMAP1 is involved in Arf6-dependent vesicle trafficking, but not Arf6-mediated actin cytoskeleton reorganization, and regulates clathrin-dependent endocytosis of the transferrin receptors and E-cadherin. SMAP2 regulates Arf1-dependent retrograde transport of TGN38/46 from the early endosome to the trans-Golgi network (TGN). SMAP2 has the Clathrin Assembly Lymphoid Myeloid (CALM)-binding domain, but SMAP1 does not
LASLLLEEENKFCADCQSKGPRWASWNIGVFICIRCAGIHRNLGVHISRVKSVNLDQWTQEQIQCMQEMG
NGKANRLYEAFLPENFRRPQTDQAVEGFIRDKYEKKK
>gnl|CDD|176869 cd08860, TcmN_ARO-CYC_like, N-terminal aromatase/cyclase domain of the multifunctional protein tetracenomycin (TcmN) and related domains. This family includes the N-terminal aromatase/cyclase (ARO/CYC) domain of Streptomyces glaucescens TcmN, and related domains. It belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. ARO/CYC domains participate in the diversification of aromatic polyketides by promoting polyketide cyclization. They occur in two architectural forms, monodomain and didomain. Monodomain aromatase/cyclases have a single ARO/CYC domain. For some, such as TcmN, this single domain is linked to a second domain of unrelated function. TcmN is a multifunctional cyclase-dehydratase-O-methyl transferase. Its N-terminal ARO/CYC domain participates in polyketide binding and catalysis; it promotes C9-C14 first-ring (and C7-C16 second-ring) cyclizations. Its C-terminal domain has O-methyltransferase activity. Didomain aromatase/cyclases contain two ARO/CYC domains, and they biosynthesize C7-C12 first ring cyclized polyketides. These latter domains belong to a different subfamily in the SRPBCC superfamily
GRTDNSIVIDAPLDLVWDMTNDIATWPDLFSEYAEAEVLEEDGDTVRFRLTMHPDANGTVWSWVSERTLD
PVNRTVRARRVETGPFAYMNIRWEYTEVPEGTRMRWVQDFEMKPGAPVDDAAMTDRLNTNTRAQMARIKK
KIEAAA
>gnl|CDD|176870 cd08861, OtcD1_ARO-CYC_like, N-terminal and C-terminal aromatase/cyclase domains of Streptomyces rimosus OtcD1 and related domains. This family includes the N- and C- terminal aromatase/cyclase (ARO/CYC) domains of Streptomyces rimosus OtcD1 and related domains. It belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. ARO/CYC domains participate in the diversification of aromatic polyketides by promoting polyketide cyclization. They occur in two architectural forms, didomain and monodomain. Didomain aromatase/cyclases (ARO/CYCs), contain two ARO/CYC domains, and are associated with C7-C12 first ring cyclized polyketides. Streptomyces rimosus OtcD1 is a didomain ARO/CYC. The polyketide Oxytetracycline (OTC) is a broad spectrum antibiotic made by Streptomyces rimosus. The gene encoding OtcD1 is part of oxytetracycline (OTC) gene cluster. Disruption of this gene results in the production of novel polyketides having shorter chain lengths (by up to 10 carbons) than OTC. Monodomain ARO/CYCs have a single ARO/CYC domain, and are often associated with C9-C14 first ring cyclizations, these latter domains belong to a different subfamily in the SRPBCC superfamily
VEHSVTVAAPAEDVYDLLADAERWPEFLPTVHVERLELDGGVERLRMWATAFDGSVHTWTSRRVLDPEGR
RIVFRQEEPPPPVASMSGEWRFEPLGGGGTRVTLRHDFTLGIDSPEAVPWIRRALDRNSRAELAALRAAA
ER
>gnl|CDD|176871 cd08862, SRPBCC_Smu440-like, Ligand-binding SRPBCC domain of Streptococcus mutans Smu.440 and related proteins. This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Streptococcus mutans Smu.440 and related proteins. This domain belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Streptococcus mutans is a dental pathogen, and the leading cause of dental caries. In this pathogen, the gene encoding Smu.440 is in the same operon as the gene encoding SMU.441, a member of the MarR protein family of transcriptional regulators involved in multiple antibiotic resistance. It has been suggested that SMU.440 is involved in polyketide-like antibiotic resistance
MKFEATIVIDAPPERVWAVLTDVENWPAWTPSVETVRLEGPPPAVGSSFKMKPPGLVRSTFTVTELRPGH
SFTWTGPAPGISAVHRHEFEAKPDGGVRVTTSESLSGPLAFLFGLFVGKKLRALLPEWLEGLKAAAEQ
>gnl|CDD|176872 cd08863, SRPBCC_DUF1857, DUF1857, an uncharacterized ligand-binding domain of the SRPBCC domain superfamily. Uncharacterized family of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins
NFEHTVPINDPGNIPTLTRAQLWRGLVLRAREPQLFVPGLDRCEVLSESGTVLERELTFGPAKIRETVTL
EPPSRVHFLQADAGGTLTNTIEEPEDGALYLRFVYETTLPEVAEEEAKAYQEIVKQAYKEADIDTVRTIR
E
>gnl|CDD|176873 cd08864, SRPBCC_DUF3074, DUF3074, an uncharacterized ligand-binding domain of the SRPBCC domain superfamily. Uncharacterized family of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins
TWKKDKKLYYSLPKTIGVQTYSKHIAVKGDFWFARVSVHEDLGFTGKKSYQEFREGLRDTHTEYEKEYVH
EIGAYDLEPVEVDGEGDGVVTYLVQLTYKFPFPLSPRVFNELVHIKSDLDPASEFMVVSLPITPPLVESL
YENAVLGRYASVEKISYLPDADGKSNKVEWIMATRSDAGGNIPRWLTKLTIPKAIAKDVPLFLDWIDS
>gnl|CDD|176874 cd08865, SRPBCC_10, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins
VEESIVIERPVEEVFAYLADFENAPEWDPGVVEVEKITDGPVGVGTRYHQVRKFLGRRIELTYEITEYEP
GRRVVFRGSSGPFPYEDTYTFEPVGGGTRVRYTAELEPGGFARLLDPLMAPAFRRRARAALENLKALLEA
>gnl|CDD|176875 cd08866, SRPBCC_11, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins
VVARVRVPAPPETVWAVLTDYDNLAEFIPNLAESRLLERNGNRVVLEQTGKQGILFFKFEARVVLELRER
EEFPRELDFEMVEGDFKRFEGSWRLEPLADGGGTLLTYEVEVKPDFFAPVFLVEFVLRQDLPTNLLAIRA
EAES
>gnl|CDD|176876 cd08867, START_STARD4_5_6-like, Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins. This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4, -5, and -6. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7a-hydroxycholesterol. STARD4 and STARD5 are ubiquitously expressed, with highest levels in liver and kidney. STRAD5 functions in the kidney within the proximal tubule cells where it is associated with the Endoplasmic Reticulum (ER), and may participate in ER-associated cholesterol transport. It binds cholesterol and 25-hydroxycholesterol. Expression of the gene encoding STARD5 is increased by ER stress, and its mRNA and protein levels are elevated in a type I diabetic mouse model of human diabetic nephropathy. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis
MDFKVIAEKLANEALQYINDTDGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVIDVIIPPCG
GLRLKWDKSLKHYEVLEKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRYEDNQWSSSGKSVDIPERP
PTPGFVRGYNHPCGYFCSPLKGSPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLVKGVK
>gnl|CDD|176877 cd08868, START_STARD1_3_like, Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins. This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and STARD3 (also known as metastatic lymph node 64/MLN64). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. This STARD1-like subfamily has a high affinity for cholesterol. STARD1/StAR can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads. STARD3 may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers
SQELEYLKQGAEALARAWSILTDPGWKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLN
VESLPSWNPTVLECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENCYLSSGVSVEHPAMP
PTKNYVRGENGPGCWILRPLPNNPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIATL
>gnl|CDD|176878 cd08869, START_RhoGAP, C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain. This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38), STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP), and STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. Some, including STARD12, -and -13, also have an N-terminal SAM (sterile alpha motif) domain; these have a SAM-RhoGAP-START domain organization. This subfamily is involved in cancer development. A large spectrum of cancers have dysregulated genes encoding these proteins. The precise function of the START domain in this subfamily is unclear
SYLERCVQDLLREARDKSKGWVSVSSSDHVELAFKKVDDGHPLRLWRASTEVEAPPEEVLQRILRERHLW
DDDLLQWKVVETLDEDTEVYQYVTNSMAPHPTRDYVVLRTWRTDLPKGACVLVETSVEHTEPVPLGGVRA
VVLASRYLIEPCGSGKSRVTHICRVDLRGRSPEWYNKVYGHLCARELLRIRDSFRQL
>gnl|CDD|176879 cd08870, START_STARD2_7-like, Lipid-binding START domain of mammalian STARD2, -7, and related proteins. This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD2 (also known as phosphatidylcholine transfer protein/PC-TP), and STARD7 (also known as gestational trophoblastic tumor 1/GTT1). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD2 is a cytosolic phosphatidycholine (PtdCho) transfer protein, which traffics PtdCho, the most common class of phospholipids in eukaryotes, between membranes. It represents a minimal START domain structure. STARD2 plays roles in hepatic cholesterol metabolism, in the development of atherosclerosis, and may also have a mitochondrial function. The gene encoding STARD7 is overexpressed in choriocarcinoma. STARD7 appears to be involved in the intracellular trafficking of PtdCho to mitochondria. STARD7 was shown to be surface active and to interact differentially with phospholipid monolayers. It showed a preference for phosphatidylserine, cholesterol, and phosphatidylglycerol
GHVSEEDLRDLVQELQEGAEGQAWQQVMDKSTPDMSYQAWRRKPKGTGLYEYLVRGVFEDCTPELLRDFY
WDDEYRKKWDETVIEHETLEEDEKSGTEIVRWVKKFPFPLSDREYVIARRLWESDDRSYVCVTKGVPYPS
VPRSGRKRVDDYESSLVIRAVKGDGQGSACEVTYFHNPDGGIPRELAKLAVKRGMPGFLKKLENALRKY
>gnl|CDD|176880 cd08871, START_STARD10-like, Lipid-binding START domain of mammalian STARD10 and related proteins. This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2)
GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDVPAETLYDVLHDP
EYRKTWDSNMIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRK
GFVRAISLLTGYLIRPTGPKGCTLTYVTQNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKYPEWKAKN
NPEFKPWLYPEQ
>gnl|CDD|176881 cd08872, START_STARD11-like, Ceramide-binding START domain of mammalian STARD11 and related domains. This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD11 and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD11 can mediate transfer of the natural ceramide isomers, dihydroceramide and phytoceramide, as well as ceramides having C14, C16, C18, and C20 chains. They can also transfer diacylglycerol, but with a lower efficiency. STARD11 is synthesized from two major transcripts: a larger one encoding Goodpasture antigen-binding protein (GPBP)/ceramide transporter long form (CERTL); and a smaller one encoding GPBPdelta26/CERT, which is deleted for 26 amino acids. Both splicing variants mediate ceramide transfer from the ER to the Golgi, in a non-vesicular manner. It is likely that these two carry out different functions in specific sub-cellular locations. These proteins have roles in brain homeostasis and disease processes. GPBP/CERTL exists in multiple isoforms originating from alternative translation initiation sites and post-translational modifications. Goodpasture syndrome is a human disorder caused by antibodies directed against the a3-chain of collagen type IV. GPBP/CERTL binds and phosphorylates this antigen. The human gene encoding STARD11 is referred to as COL4A3BP referring to its collagen binding function. It is unknown whether the ceramide-transfer function of GPBP/CERTL is related to this collagen interaction. The expression of GPBP/CERTL is elevated in these and other spontaneous autoimmune disorders including cutaneous lupus erythematosus, pemphigoid, and lichen planus. GPBL/CERTL contains an N-terminal pleckstrin homology domain (PH), which targets the protein to the Golgi, a middle region containing two serine-rich domains (SR1, SR2), a FFAT (two phenylalanine amino acids in an acidic tract) motif which is involved in endoplasmic reticulum targeting, and this C-terminal SMART domain. The shorter splicing variant, CERT, lacks the SR2 domain
THRLSPEVDEKVQEQLTYALEDVGADGWQLFAEEGEMKVYRREVEEDGVVLDPLKATHAVKGVTGHEVCH
YFFDPDVRMDWETTLENFHVVETLSQDTLIFHQTHKRVWPAAQRDALFVSHIRKIPALEEPNAHDTWIVC
NFSVDHDSAPLNNKCVRAKLTVAMICQTFVSPPDGNQEITRDNILCKITYVANVNPGGWAPASVLRAVYK
REYPKFLKRFTSYVQEKTKGKPILF
>gnl|CDD|176882 cd08873, START_STARD14_15-like, Lipid-binding START domain of mammalian STARDT14, -15, and related proteins. This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974), STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD14/ACOT11 and STARD15/ACOT12 are type II acetyl-CoA thioesterases; they catalyze the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, STARD14 and STARD15 each have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice. Human STARD15 may have roles in cholesterol metabolism and in beta-oxidation
RRYREAAARKKIRLDRKYILSLQREVPLSVAWDRSNQMYLSYGNVTALKRLAAKSDWTVASSTTSVTLYT
LEQDGVLSFCVELKVQTCASDAFDLLSDPFKRPEWDPHGRSCEEVKRVGEDDGIYHTTMPSLTSEKPNDF
VLLVSRRKPATDGDPYKVAFRSVTLPRVPQTPGYSRTEVACAGFVIRQDCGTCTEVSYYNETNPKLLSYV
TCNLAGLSALYCRTFHCCEQFLVTN
>gnl|CDD|176883 cd08874, START_STARD9-like, C-terminal START domain of mammalian STARD9, and related domains; lipid binding. This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C /PITP /Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy
ESIVMAACSVNLSNLDQCQATAGWSYQCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTR
FLYDTMIKTARIHKTFTEDICLVYLVHETPLCLLKQPRDFCCLQVEAKEGELSVVACQSVYDKSMPEPGR
SLVRGEILPSAWILEPVTVEGNQYTRVIYIAQVALCGPDVPAQLLSSLSKRQPLVIARLALFLEA
>gnl|CDD|176884 cd08875, START_ArGLABRA2_like, C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related proteins. This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of the Arabidopsis homeobox protein GLABRA 2 and related proteins. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Most proteins in this subgroup contain an N-terminal homeobox DNA-binding domain, some contain a leucine zipper. ArGLABRA2 plays a role in the differentiation of hairless epidermal cells of the Arabidopsis root. It acts in a cell-position-dependent manner to suppress root hair formation in those cells
KSGLLELAEEAMDELLKLAQGGEPLWIKSPGMKPEILNPDEYERMFPRHGGSKPGGFTTEASRACGLVMM
NAIKLVEILMDVNKWSELFPGIVSKAKTLQVISTGNGGNRNGTLQLMYAELQVPSPLVPTREFYFLRYCK
QLEDGLWAVVDVSIDGVQTAPPPASFVRCRRLPSGCLIQDMPNGYSKVTWVEHVEVDEKPVHLLYRYLVS
SGLAFGATRWVATLQRQCE
>gnl|CDD|176885 cd08876, START_1, Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family. Functionally uncharacterized subgroup of the START domain family. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease
SLLLSLLLAGAALAPDGDWQLVKDKDGIKVYTRDVEGSPLKEFKAVAEVDASIEAFLALLRDTESYPQWM
PNCKESRVLKRTDDNERSVYTVIDLPWPVKDRDMVLRSTTEQDADDGSVTITLEAAPEALPEQKGYVRIK
TVEGQWTFTPLGNGKTRVTYQAYADPGGSIPGWLANAFAKDAPYNTLENLRKQLK
>gnl|CDD|176886 cd08877, START_2, Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family. Functionally uncharacterized subgroup of the START domain family. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease
IDKIRQEATIMQENLKDLDESDGWTLQKESEGIRVYYKFEPDGSLLSLRMEGEIDGPLFNLLALLNEVEL
YKTWVPFCIRSKKVKQLGRADKVCYLRVDLPWPLSNREAVFRGFGVDRLEENGQIVILLKSIDDDPEFLK
LTDLDIPSTSAKGVRRIIKYYGFVITPISPTKCYLRFVANVDPKMSLVPKSLLNFVARKFAGLLFEKIQK
AAKNV
>gnl|CDD|176887 cd08878, RHO_alpha_C_DMO-like, C-terminal catalytic domain of the oxygenase alpha subunit of dicamba O-demethylase and related aromatic ring hydroxylating dioxygenases. C-terminal catalytic domain of the oxygenase alpha subunit of Stenotrophomonas maltophilia dicamba O-demethylase (DMO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and the C-terminal catalytic domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this subgroup include the alpha subunits of carbazole 1,9a-dioxygenase, phthalate dioxygenase, vanillate O-demethylase, Pseudomonas putida 2-oxoquinoline 8-monooxygenase, and Comamonas testosteroni T-2 p-toluenesulfonate dioxygenase. It also includes the C-terminal domain of the lignin biphenyl-specific O-demethylase (LigX) of the 5,5'-dehydrodivanillic acid O- demethylation system of Sphingomonas paucimobilis SYK-6. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket
WGGGYRHIDCNWLQVVENLMDPSHVSFVHRSSIGRDAADLPSGPPKEVEEVPRGVTYRRWREDEDPPPFG
FEGPVDRWRVIEFLLPNVLLIDPGVAPAGTREQGVRMRVTHWITPIDETTTHYFWFFVRNFAPDEEKKDD
EELTETLRSGLSGAFNEDKEAVEAQQRIIDRDPTREHLGLSDKGIVRFRRLLRRLL
>gnl|CDD|176888 cd08879, RHO_alpha_C_AntDO-like, C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas resinovorans strain CA10 anthranilate 1,2-dioxygenase and related aromatic ring hydroxylating dioxygenases. C-terminal catalytic domain of the oxygenase alpha subunit of anthranilate 1,2-dioxygenase (AntDO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and the C-terminal catalytic domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this subgroup include the alpha subunits of AntDO, aniline dioxygenase, Acinetobacter calcoaceticus benzoate 1,2-dioxygenase, 2-halobenzoate 1,2-dioxygenase from Pseudomonas cepacia 2CBS, 2,4,5-trichlorophenoxyacetic acid oxygenase from Pseudomonas cepacia AC1100, 2,4-dichlorophenoxyacetic acid oxygenase from Bradyrhizobium sp. strain HW13, p-cumate 2,3-dioxygenase, 2-halobenzoate 1,2-dioxygenase form Pseudomonas cepacia 2CBS, and Pseudomonas putida IacC, which may be involved in the catabolism of the plant hormone indole 3-acetic acid. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket
GGTHRYRYRGNWKLQLENGTDGYHPPFVHASYVATTGAAAADATRGGLSSFMTGPQGGGVRDLGNGHSVL
DSRPEIPRLDADRPKPPIAEYRAALVAAHGEERARRILRGRGRNLNIFPNLFIIDISQQIRVIRPIAVDE
TEVTSWALRPKGAPDEVNRRRLRYSEDFFGPSGFATPDDLEAFERCQRGLAARGEEWVDLSRGLGREKAD
EDGVVTGAVTDELPMRNQWRAWKRLMT
>gnl|CDD|176889 cd08880, RHO_alpha_C_ahdA1c-like, C-terminal catalytic domain of the large/alpha subunit (ahdA1c) of a ring-hydroxylating dioxygenase from Sphingomonas sp. strain P2 and related proteins. C-terminal catalytic domain of the large subunit (ahdA1c) of the AhdA3A4A2cA1c salicylate 1-hydroxylase complex from Sphingomonas sp. strain P2, and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). AhdA3A4A2cA1c is one of three known isofunctional salicylate 1-hydroxylase complexes in strain P2, involved in phenanthrene degradation, which catalyze the monooxygenation of salicylate, the metabolite of phenanthene degradation, to produce catechol. This complex prefers salicylate over other substituted salicylates; the other two salicylate 1-hydroxylases have different substrate preferences. RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Other oxygenases belonging to this subgroup include the alpha subunits of anthranilate 1,2-dioxygenase from Burkholderia cepacia DBO1, a polycyclic aromatic hydrocarbon dioxygenase from Cycloclasticus sp. strain A5 (PhnA dioxygenase), salicylate-5-hydroxylase from Ralstonia sp. U2, ortho-halobenzoate 1,2-dioxygenase from Pseudomonas aeruginosa strain JB2, and the terephthalate 1,2-dioxygenase system from Delftia tsuruhatensis strain T7. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket
LGYYRQRIPGNWKLYAENVKDPYHASLLHLFFVTFGLWRADQKSSIIDDEHGRHSVMTSTKSGDDEAAEK
DSEEIRSFRDDFTLLDPSLLDGRAEFDDDITLVIQSIFPSLVVQQIQNTLAVRHIIPKGPDSFELVWTYF
GYEDDDEEMTRLRLRQANLVGPAGFVSMEDGEAIEFVQRGVEGDGGDRSVIEMGGGDVESSDHMVTEAAI
RGFWKYYRKVMG
>gnl|CDD|176890 cd08881, RHO_alpha_C_NDO-like, C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) and related aromatic ring hydroxylating dioxygenases. C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). This domain binds non-heme Fe(II). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents form the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Proteins belonging to this subgroup include the terminal oxygenase alpha subunits of biphenyl dioxygenase, cumene dioxygenase from Pseudomonas fluorescens IP01, ethylbenzene dioxygenase, naphthalene 1,2-dioxygenase, nitrobenzene dioxygenase from Comamonas sp. strain JS765, toluene 2,3-dioxygenase from Pseudomonas putida F1, dioxin dioxygenase of Sphingomonas sp. Strain RW1, and the polycyclic aromatic hydrocarbons (PAHs)degrading ring-hydroxylating dioxygenase from Sphingomonas CHY-1. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket
GLEVVGGPQKWVIKANWKLAAENFAGDGYHTGTTHASALEAGLPPDAADLPPIDLGLQFTAPWHGHGLGF
FLDSPQHGTIFPNLSFLPGYFNTLRVWHPRGPDETEVWTWTLVDKDAPEEVKDRVRRQYTRTFGPAGTFE
QDDGENWEEITRVARGYVARQVPLNYQMGLGVEPEPDPGGPGIVGPGFYSEANQRGFYRRWLELME
>gnl|CDD|176891 cd08882, RHO_alpha_C_MupW-like, C-terminal catalytic domain of Pseudomonas fluorescens MupW and related aromatic ring hydroxylating dioxygenases. C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas fluorescens MupW and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. MupW is part of the mupirocin biosynthetic gene cluster in Pseudomonas fluorescens, and may catalyze the oxidation of the 16-methyl group during biosynthesis of this polyketide antibiotic. Mupirocin is a mixture of pseudomonic acids which targets isoleucyl-tRNA synthase and is a strong inhibitor of Gram positive bacterial and mycoplasmal pathogens. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket
VWHVTKVLPCNWKVAQEAFNESYHVPTTHPQLLPFIGDDNSQYDFYGRHVSRGITPFGVPSPHLADPSDD
EEPLLAQMLEAGDLTDPADYTGRTYEAREAVQARRRLGSERGGVDYSALTDAELTDGIHYTLFPNFTILP
GPDGLLVYRFRPHGDDPEKCIFDIWSLERYPEGAEPPEPPEEHEVFSDAPELGGLGLVLDQDFSNLPAVQ
KGMHSRGFGGLVLANQEESRIRHFHEVLDDYLA
>gnl|CDD|176892 cd08883, RHO_alpha_C_CMO-like, C-terminal catalytic domain of plant choline monooxygenase (CMO) and related aromatic ring hydroxylating dioxygenases. C-terminal catalytic domain of plant choline monooxygenase and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Plant choline monooxygenase catalyzes the first step in a two-step oxidation of choline to the osmoprotectant glycine betaine. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket
HARREYVIECNWKVYVDNYLEGYHVPFAHPGLAAVLDYATYRTELFEYVSLQSAPARAEEGSFFYRLGNA
ALYAWIYPNLMLNRYPPGMDVNVVLPLGPERCKVVFDYFVDDSDGSDEAFIAESIESDRVQKEDIEICES
VQRGLESGAYDPGRFSPKRENGVHHFHRLLAQALN
>gnl|CDD|176893 cd08884, RHO_alpha_C_GbcA-like, C-terminal catalytic domain of GbcA (glycine betaine catabolism A) from Pseudomonas aeruginosa PAO1 and related aromatic ring hydroxylating dioxygenases. C-terminal catalytic domain of GbcA (glycine betaine catabolism A) from Pseudomonas aeruginosa PAO1 and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. GbcA is involved in glycine betaine (GB) catabolism in Pseudomonas aeruginosa; it may remove a methyl group from GB via a dioxygenase mechanism, producing dimethylglycine and formaldehyde. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket
APYDLANLKVAHRISYEVAANWKLVVENYRECYHCAGVHPELARSLSEFDDGGNPDPEAGGADFRGRRGP
LRGGAESFTMDGKAVAPPLPGLTEADDRGALYYTLYPNSFLHLHPDHVVTFRVLPLSPDETLVRCKWLVH
PDAVEGVDYDLDDLVEVWDATNRQDWAICERNQRGVNSPAYRPGPYSPMEGGVLAFDRWYLERMG
>gnl|CDD|176894 cd08885, RHO_alpha_C_1, C-terminal catalytic domain of the oxygenase alpha subunit of an uncharacterized subgroup of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases. C-terminal catalytic domain of the oxygenase alpha subunit of a functionally uncharacterized subgroup of the Rieske-type non-heme iron aromatic ring-hydroxylating oxygenase (RHO) family. RHOs, also known as aromatic ring hydroxylating dioxygenases, utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. This group contains two putative Parvibaculum lavamentivorans (T) DS-1 oxygenases; this organism catabolizes commercial linear alkylbenzenesulfonate surfactant (LAS) and other surfactants, by a pathway involving an undefined 'omega-oxygenation' and beta-oxidation of the LAS side chain. The nature of the LAS-oxygenase is unknown but is likely a multicomponent system. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket
VFREEEVWDTNWKVLAENFMEGYHLPGLHPGTLHPFMPAELSYFRPEDGRGFTRHKGTKHFNETIEPAHP
PNPGLTEEWRRRLVLFAIFPTHLLALTPDYVWWLSLLPEGAGRVRVRWGVLVAPEAADDPEAAEYIAELK
ALLDAINDEDRLVVEGVQRGLGSRFAVPGRLSHLERPIWQFQRYLASRLA
>gnl|CDD|176895 cd08886, RHO_alpha_C_2, C-terminal catalytic domain of the oxygenase alpha subunit of an uncharacterized subgroup of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases. C-terminal catalytic domain of the oxygenase alpha subunit of a functionally uncharacterized subgroup of the Rieske-type non-heme iron aromatic ring-hydroxylating oxygenase (RHO) family. RHOs, also known as aromatic ring hydroxylating dioxygenases, utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket
AARLTSEIKANWKNVVDNYLECYHCHTAHPDFVDSLDMDTYKHTTHGNYSSQMANYGSAENSEYSVKPDA
DFAFYWLWPNTMLNVYPGAGNMGVINIIPVDAETTLQHYDFYFRDEELTDEEKELIEYYRQVLQPEDLEL
VESVQRGLKSRAFGQGRIVVDPSGSGISEHAVHHFHGLVLEA
>gnl|CDD|176896 cd08887, RHO_alpha_C_3, C-terminal catalytic domain of the oxygenase alpha subunit of an uncharacterized subgroup of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases. C-terminal catalytic domain of the oxygenase alpha subunit of a functionally uncharacterized subgroup of the Rieske-type non-heme iron aromatic ring-hydroxylating oxygenase (RHO) family. RHOs, also known as aromatic ring hydroxylating dioxygenases, utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. This group contains a putative Parvibaculum lavamentivorans (T) DS-1 oxygenase; this organism catabolizes commercial linear alkylbenzenesulfonate surfactant (LAS) and other surfactants, by a pathway involving an undefined 'omega-oxygenation' and beta-oxidation of the LAS side chain. The nature of the LAS-oxygenase is unknown but is likely a multicomponent system. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket
FESRRFDVAANWKLALDGFLEGYHFKVLHKNTIAPYFYDNLSVYDAFGPHSRIVFPRKSIESLRDLPEDE
WDLRRHLTVIYTLFPNVSLLVQPDHLEIIQIEPGSPDRTRVTVYLLIPPPPDTEEARAYWDKNWDFLMAV
VLDEDFEVAEEIQRGLASGANDHLTFGRNESALQHFHRWLERALA
>gnl|CDD|176897 cd08888, SRPBCC_PITPNA-B_like, Lipid-binding SRPBCC domain of mammalian PITPNA, -B, and related proteins (Class I PITPs). This subgroup includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of mammalian Class 1 phosphatidylinositol transfer proteins (PITPs), PITPNA/PITPalpha and PITPNB/PITPbeta, Drosophila vibrator, and related proteins. These are single domain proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. In addition, PITPNB transfers sphingomyelin in vitro, with a low affinity. PITPNA is found chiefly in the nucleus and cytoplasm; it is enriched in the brain and predominantly localized in the axons. A reduced expression of PITPNA contributes to the neurodegenerative phenotype of the mouse vibrator mutation. The role of PITPNA in vivo may be to provide PtdIns for localized PI3K-dependent signaling, thereby controlling the polarized extension of axonal processes. PITPNA homozygous null mice die soon after birth from complicated organ failure, including intestinal and hepatic steatosis, hypoglycemia, and spinocerebellar disease. PITPNB is associated with the Golgi and ER, and is highly expressed in the liver. Deletion of the PITPNB gene results in embryonic lethality. The PtdIns and PtdCho exchange activity of PITPNB is required for COPI-mediated retrograde transport from the Golgi to the ER. Drosophila vibrator localizes to the ER, and has an essential role in cytokinesis during mitosis and meiosis
LIKEFRVILPLSVEEYQVGQLYSVAEASKNETGGGEGIEVLVNEPYEKDDGEKGQYTHKIYHLQSKVPGF
VRMLAPEGSLEIHEKAWNAYPYCRTIITNEYMKEDFLIIIETWHKPDLGTQENVHNLDPEEWKEVEVVYI
DIADRSQVDPKDYKADEDPAKFQSEKTGRGPLGPNWKKELVNQKDCPIMCAYKLVTVEFKWWGLQNKVEN
FIQKQERRLFTNFHRQVFCWLDKWHGLTMDDIRRMEDETKKELDEMRE
>gnl|CDD|176898 cd08889, SRPBCC_PITPNM1-2_like, Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs). This subgroup includes an N-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of mammalian Class II phosphatidylinositol transfer protein (PITPs), PITPNM1/PITPalphaI/Nir2 (PYK2 N-terminal domain-interacting receptor2) and PITPNM2/PITPalphaII/Nir3), Drosophila RdgB, and related proteins. These are membrane associated multidomain proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Ablation of the mouse gene encoding PITPNM1 results in early embryonic death. PITPNM1 is localized chiefly to the Golgi apparatus, and under certain conditions translocates to the lipid droplets. Targeting to the latter is dependent on a specific threonine residue within the SRPBCC domain. PITPNM1 plays a part in Golgi-mediated transport. It regulates diacylglycerol (DAG) production at the trans-Golgi network (TGN) via the CDP-choline pathway. Drosophila RdgB, the founding member of the PITP family, is implicated in the visual and olfactory transduction. RdgB is required for maintenance of ultra structure in photoreceptors and for sensory transduction. The mouse PITPNM1 gene rescues the phenotype of Drosophila rdgB mutant flies. In addition to the SRPBCC domain, PITPNM1 and -2 contain a Rho-inhibitory domain (Rid), six hydrophobic stretches, a DDHD calcium binding region, and a C-terminal tyrosine kinase Pyk2-binding / HAD-like phosphohydrolase domain. PITPNM1 has a role in regulating cell morphogenesis through its Rho inhibitory domain (Rid). This SRPBCC_PITPNM1-2_like domain model includes the first 52 residues of the 224 residues Rid (Rho-inhibitory domain)
MLIKEYRIPLPMSVEEYRIAQLYMIQKKSREESKGEGSGVEILENRPYTDGPGGSGQYTHKIYHIGSHIP
GWFRAILPKSALRVEEEAWNAYPYTRTRYTCPFVEKFSLDIETYYFDDAGEQENVFNLSPAELRQRIIDF
IDIVKDPVPGSDYKAEEDPKLYVSEKTGRGPLSDDWIEEYKDPPGKGPIMCAYKLCKVEFRYWGMQTKIE
RFIHDVALRKVMLRAHRQAWCWQDEWYGLTMEDIRKLEEETQLALAQKMA
>gnl|CDD|176899 cd08890, SRPBCC_PITPNC1_like, Lipid-binding SRPBCC domain of mammalian PITPNC1,and related proteins (Class IIB PITPs). This subgroup includes the N-terminal SRPBCC (START/RHO_alpha_C /PITP /Bet_v1/CoxG/CalC) domain of mammalian Class IIB phosphatidylinositol transfer protein (PITP), PITPNC1/RdgBbeta, and related proteins. These are metazoan proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Mammalian PITPNC1 contains an amino-terminal SRPBCC PITP-like domain and a short carboxyl-terminal domain. It is a cytoplasmic protein, and is ubiquitously expressed. It can transfer phosphatidylinositol (PtdIns) in vitro with a similar ability to other PITPs
LLKEYRICMPLTVEEYRIGQLYMISRHSHEQSERGEGVEVVQNEPCEDPEHGNGQFTEKRVYLNSRLPSW
ARAVVPKIFYVTEKAWNYYPYTITEYTCSFLPKFSIHIETKYEDNKGKSENCIFLSEAELSEREVCHLDI
AYDEIPEKYYKEEEDPKYFKSEKTGRGPLKEGWRETHKPIMCSYKLVTVKFEVWGLQTRVEQFVHKVVRD
ILLLGHRQAFAWVDEWYDMTMDDVREYERTIQEKTNEKIG
>gnl|CDD|176900 cd08891, SRPBCC_CalC, Ligand-binding SRPBCC domain of Micromonospora echinospora CalC and related proteins. This subfamily includes Micromonospora echinospora CalC (MeCalC) and related proteins. These proteins belong to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM). Enediyne antibiotics are antitumor agents. Enediynes have an in vitro and in vivo role as DNA damaging agents; they consist of a DNA recognition unit (e.g., aryltetrasaccharide of CLM), an activating component (e.g., methyl trisulfide of CLM), which promotes cycloaromatization, and the enediyne warhead which cycloaromatizes to a reactive diradical species, resulting in oxidative strand cleavage of the targeted DNA sequence. MeCalC confers resistance to CLM by a self sacrificing mechanism: the transient enediyne diradical species abstracts a CalC Gly Calpha-hydrogen, thereby quenching the reactive enediyne moiety, and generating a CalC Gly Calpha radical. This radical then reacts with oxygen, leading to oxidative site-specific proteolysis of CalC. This antibiotic-induced proteolysis of CalC results in inactivation of both CalC and the highly reactive diradical species. CalC has also been shown to inactivate two other enediynes, shishijimicin and namenamicin. The crucial Gly of the MeCalC CLM resistance mechanism is contained in a loop (L1) which is displaced when CLM is bound, this Gly is not conserved in this subgroup
PVRKSVTVPAPPERAFEVFTEGFGAWWPPEYHFVFSPGAEVVFEPRAGGRWYEIGEDGTECEWGTVLAWE
PPSRLVFTWQINADWRPDPDKASEVEVRFEAVGAEGTRVELEHRGFERHGDGWEAAAMRMGYDGGWPLLL
ERYAAAAEK
>gnl|CDD|176901 cd08892, SRPBCC_Aha1, Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related proteins. This subfamily includes the C-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Aha1, and related domains. Proteins in this group belong to the SRPBCC domain superfamily of proteins which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Aha1 is one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Hsp90, Aha1, and other accessory proteins interact in a chaperone cycle driven by ATP binding and hydrolysis. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity. One Aha1 molecule binds per Hsp90 dimer. The N- and C- terminal domains of Aha1 cooperatively bind across the dimer interface of Hsp90. The C-terminal domain of Aha1 binds the N-terminal Hsp90 ATPase domain. Aha1 may regulate the dwell time of Hsp90 with client proteins. Aha1 may act as either a negative or positive regulator of chaperone-dependent activation, depending on the client protein; for example, it acts as a negative regulator in the case of Saccharomyces cerevisiae MAL63 MAL-activator, and acts as a positive regulator in the case of glucocorticoid receptor and v-Src kinase. The mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases
TISLTETFQVPAEELYEALTDEERVQAFTRSPAKVDAKVGGKFSLFGGNITGEFVELVPGKKIVQKWRFK
SWPEGHYSTVTLTFTEKDDETELKLTQTGVPAGEEERTREGWERYYFESIKQTFGY
>gnl|CDD|176902 cd08893, SRPBCC_CalC_Aha1-like_GntR-HTH, Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins; some contain an N-terminal GntR family winged HTH DNA-binding domain. SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. Some proteins in this subgroup contain an N-terminal winged helix-turn-helix DNA-binding domain found in the GntR family of proteins which include bacterial transcriptional regulators and their putative homologs from eukaryota and archaea
KFVYVTYIRATPEKVWQALTDPEFTRQYWGGTTVESDWKVGSAFEYRRGDDGTVDVEGEVLESDPPRRLV
HTWRAVWDPEMAAEPPSRVTFEIEPVGDVVKLTVTHDGFPPGSPTLEGVSGGWPAILSSLKTLLET
>gnl|CDD|176903 cd08894, SRPBCC_CalC_Aha1-like_1, Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins. SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands
EIVTTRVIDAPRDLVFAAWTDPEHLAQWWGPEGFTNTTHEFDLRPGGRWRFVMHGPDGTDYPNRIVFLEI
EPPERIVYDHGSGPPRFRLTVTFEEQGGKTRLTWRQVFPTAAERCEKIKFGAVEGNEQTLDRLAAYLAR
>gnl|CDD|176904 cd08895, SRPBCC_CalC_Aha1-like_2, Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins. SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands
TDRLHRVIAAPPERVYRAFLDPDALAKWLPPDGMTGTVHEFDAREGGGFRMSLTYFDPSVGKTTGNTDVF
GGRFLELVPNERIVYTDVFDDPSLSGEMTMTWTLSPVSGGTDVTIVQSGIPDGIPPEDCELGWQESLANL
AALVEA
>gnl|CDD|176905 cd08896, SRPBCC_CalC_Aha1-like_3, Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins. SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands
DLVLSRTIDAPRELVWRAWTEPELLKQWFCPKPWTTEVAELDLRPGGAFRTVMRGPDGEEFPNPGCFLEV
VPGERLVFTDALTPGWRPAEKPFMTAIITFEDEGGGTRYTARARHWTEADRKQHEEMGFHDGWGTAADQL
AALAES
>gnl|CDD|176906 cd08897, SRPBCC_CalC_Aha1-like_4, Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins. SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands
KITVETTVDAPIEKVWEAWTTPEHITKWNFASDDWHCPSAENDLRVGGKFSYRMEAKDGSMGFDFEGTYT
EVEPHKLIEYTMEDGREVEVEFTEEGDGTKVVETFDAENENPVEMQRQGWQAILDNFKKYVES
>gnl|CDD|176907 cd08898, SRPBCC_CalC_Aha1-like_5, Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins. SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands
DRIERTILIDAPRERVWRALTDPEHFGQWFGVKLGPFVVGEGATGEITYPGYEHGVFPVTVVEVDPPRRF
SFRWHPPAIDPGEDYSAEPSTLVEFTLEPIAGGTLLTVTESGFDALPAERRAEAYRMNEGGWDEQLENLV
AYVEA
>gnl|CDD|176908 cd08899, SRPBCC_CalC_Aha1-like_6, Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins. SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands
LGTVTRLDGGATLRFERLLPAPIEDVWAALTDPERLARWFAPGTGDLRVGGRVEFVMDDEEGPNATGTIL
ACEPPRLLAFTWGEGGGESEVRFELAPEGDGTRLTLTHRLLDERFGAGAVGAGWHLCLDVLEAALEGGPP
APFWDAFAQLEEEYRAY
>gnl|CDD|176909 cd08900, SRPBCC_CalC_Aha1-like_7, Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins. SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands
TFTLERTYPAPPERVFAAWSDPAARARWFVPSPDWTVLEDEFDFRVGGREVSRGGPKGGPEITVEARYHD
IVPDERIVYTYTMHIGGTLLSASLATVEFAPEGGGTRLTLTEQGAFLDGDDDPAGREQGTAALLDNLAAE
LER
>gnl|CDD|176910 cd08901, SRPBCC_CalC_Aha1-like_8, Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins. SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands
VAKTAMLIRRPVAEVFEAFVDPEITTKFWFTGSSGRLEEGKTVTWDWEMYGASVPVNVLEIEPNKRIVIE
WGDPGEPTTVEWTFEELDDGRTFVTITESGFPGTDDEGLKQALGSTEGWTLVLAGLKAYLEHGINL
>gnl|CDD|176911 cd08902, START_STARD4-like, Lipid-binding START domain of mammalian STARD4 and related proteins. This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4 and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7alpha-hydroxycholesterol. STARD4 is ubiquitously expressed, with highest levels in liver and kidney
LDIASKTTKLQNTLIQYHSILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGP
YRLDWDSLMTSMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPN
FVRGFNHPCGWFCVPLKDNPSHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKKALK
>gnl|CDD|176912 cd08903, START_STARD5-like, Lipid-binding START domain of mammalian STARD5 and related proteins. This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD5, and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD5 is ubiquitously expressed, with highest levels in liver and kidney. STARD5 functions in the kidney within the proximal tubule cells where it is associated with the Endoplasmic Reticulum (ER), and may participate in ER-associated cholesterol transport. It binds cholesterol and 25-hydroxycholesterol. Expression of the gene encoding STARD5 is increased by ER stress, and its mRNA and protein levels are elevated in a type I diabetic mouse model of human diabetic nephropathy
MDYAELAESVADKMLLYRRDESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPAAG
GLRVKWDQNVKDFEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCP
PQAGFVRGFNHPCGCFCEPVPGEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKAL
>gnl|CDD|176913 cd08904, START_STARD6-like, Lipid-binding START domain of mammalian STARD6 and related proteins. This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD6 and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis
MDFKKIAQETSQEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEH
RIKWDKSLQVYKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPS
SNYIRGYNHPCGYVCSPLPENPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK
>gnl|CDD|176914 cd08905, START_STARD1-like, Cholesterol-binding START domain of mammalian STARD1 and related proteins. This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD1 has a high affinity for cholesterol. It can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads
EAEMSYIKQGEEALQKSLSILQDQEGWKTEIVAENGDKVLSKVVPDIGKVFRLEVVVDQPLDNLYSELVD
RMEQMGEWNPNVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLM
PEQKGFIRAENGPTCIVLRPLAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQRMASS
>gnl|CDD|176915 cd08906, START_STARD3-like, Cholesterol-binding START domain of mammalian STARD3 and related proteins. This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD3 (also known as metastatic lymph node 64/MLN64) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD3 has a high affinity for cholesterol. It may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers
PQEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVIL
QPEKMVLWNKTVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHK
PPLSKYVRGENGPGGFVVLKSASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIRDL
>gnl|CDD|176916 cd08907, START_STARD8-like, C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain. This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear
QGEGVDLRAYLEDNVQCLLREASERFKGWHSAPGPDNTELACKKVGDGHPLRLWKVSTEVEAPPSVVLQR
VLRERHLWDEDLLHSQVIEALENNTEVYHYVTDSMAPHPRRDFVVLRMWRSDLPRGGCLLVSQSVDHDNP
QLEAGVRAVLLTSQYLIEPCGMGRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVARIRDSFPTL
>gnl|CDD|176917 cd08908, START_STARD12-like, C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain. This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subgroup also have an N-terminal SAM (sterile alpha motif) domain and a RhoGAP domain, and have a SAM-RhoGAP-START domain organization. The precise function of the START domain in this subgroup is unclear
NDEPADYHHFLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVSEGPPLRLWRTTIEVPAAPEEILKR
LLKEQHLWDVDLLDSKVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWRTNLPKGACALLATSVDHDRA
PVAGVRVNVLLSRYLIEPCGSGKSKLTYMCRIDLRGHMPEWYTKSFGHLCAAEVVKIRDSFSNQ
>gnl|CDD|176918 cd08909, START_STARD13-like, C-terminal lipid-binding START domain of mammalian STARD13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain. This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear
EEEGGTYQTYLESLIQNLQKEAKEKFKGWISCSSSDNTELAYKKVGDGNPLRLWKVSVEVEAPPSVVLNR
VLRERHLWDEDFLQWKVVETLDKQTEVYQYVLNCMAPHPSRDFVVLRSWRTDLPKGACSLVSVSVEHEEA
PLLGGVRAVVLDSQYLIEPCGSGKSRLTHICRVDLKGHSPEWYNKGFGHLCAAEAARIRNSFQPL
>gnl|CDD|176919 cd08910, START_STARD2-like, Lipid-binding START domain of mammalian STARD2 and related proteins. This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD2 (also known as phosphatidylcholine transfer protein/PC-TP) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD2 is a cytosolic phosphatidycholine (PtdCho) transfer protein, which traffics PtdCho, the most common class of phospholipids in eukaryotes, between membranes. It represents a minimal START domain structure. STARD2 plays roles in hepatic cholesterol metabolism, in the development of atherosclerosis, and may have a mitochondrial function
AAGTFSEEQFREACAELQQPALDGAAWELLVESSGISIYRLLDEQSGLYEYKVFGVLEDCSPSLLADVYM
DLEYRKQWDQYVKELYEKECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGRKIWVILARSTSLPQL
PEKPGVIRVKQYKQSLAIESDGKKGSKVFMYYFDNPGGMIPSWLINWAAKNGVPNFLKDMQKACQNY
>gnl|CDD|176920 cd08911, START_STARD7-like, Lipid-binding START domain of mammalian STARD7 and related proteins. This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD7 (also known as gestational trophoblastic tumor 1/GTT1). It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. The gene encoding STARD7 is overexpressed in choriocarcinoma. STARD7 appears to be involved in the intracellular trafficking of phosphatidycholine (PtdCho) to mitochondria. STARD7 was shown to be surface active and to interact differentially with phospholipid monolayers, it showed a preference for phosphatidylserine, cholesterol, and phosphatidylglycerol
IVDECRSPNADTSSINNQEPDGWEPFIEKKDMLVWRREHPGTGLYEYKVYGSFDDVTARDFLNVQLDLEY
RKKWDATAVELEVVDEDPETGSEIIYWEMQWPKPFANRDYVYVRRYIIDEENKLIVIVSKAVQHPSYPES
PKKVRVEDYWSYMVIRPHKSFDEPGFEFVLTYFDNPGVNIPSYITSWVAMSGMPDFLERLRNAALKY
>gnl|CDD|176921 cd08913, START_STARD14-like, Lipid-binding START domain of mammalian STARDT14 and related proteins. This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD14/ACOT11 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice
DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQV
RLYTLEEDKFLSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHG
KPQDFVILASRRKPCDNGDPYVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPG
VLPYISTDIAGLSSEFYSTFSACSQFLLDN
>gnl|CDD|176922 cd08914, START_STARD15-like, Lipid-binding START domain of mammalian STARD15 and related proteins. This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114) and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD15/ACOT12 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. Human STARD15/ACOT12 may have roles in cholesterol metabolism and in beta-oxidation
FRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIY
TLEEHDVLSVWVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIVNNDKPKD
LVVLVSRRKPLKDGNTYVVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISASILPY
FAGNLGGWSKSIEETAASCIQFLENA
>gnl|CDD|185746 cd08915, V_Alix_like, Protein-interacting V-domain of mammalian Alix and related domains. This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain
PYDVIESASAYNERQDDYVREHIVEPIEALNKLLNSFLAERNLPASIDDLQKPENLPDSIQHSQEIIEEG
GLDNIEQSFKELSKLRQNVEELLQECEELLEEEAAEDDQLRAKFGTLRWRRPSSDEAAKELYEKVTKLRG
YLEQASNSDNEVLQCYESIDPNLVLLCGGYKELKAFIPSPYPALDPEVSEVVSSLRPLLNEVSELEKERE
RFISELEIKSRNNDILPKLITEYKKNGTTEFEDLFEEHLKKFDKDLTYVEKTKKKQIELIKEIDAANQEF
SQVKNSNDSLDPREEALQDLEASYKKYLELKENLNEGSKFYNDLIEKVNRLLEECEDFVNAR
>gnl|CDD|381257 cd08916, TrHb3_P, Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins); group 3 (P). The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. They are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). TrHb3s include Campylobacter jejuni Ctb, encoded by Cj0465c, which may play a role in moderating O2 flux within C. jejuni
KDIITREDIELLVDTFYAKVRQDPLLGPIFNAVIGVDWPEHLPKMYDFWSSVLLGTGRYKGNPMPKHLAL
PPLTPEHFERWLALFRETLDELFEGEAAEEAKERARRIAESLQMKL
>gnl|CDD|381258 cd08917, TrHb2_O, Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins); group 2 (O). The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). TrHb2s include the dimeric Arabidopsis thaliana TrHb2 AtGLB3. GLB3 is likely to have a function distinct from other plant globins: it exhibits a low O2 affinity, an unusual concentration-independent binding of O2 and CO, and does not respond to any of the treatments that induce plant 3-on-3 globins. Other TrHb2's include Bacillus subtilis trHb (Bs-trHb) which exhibits an extremely high oxygen affinity, and Pseudoalteromonas haloplanktis PhHbO (encoded by the PSHAa0030 gene) which appears to be involved in oxidative and nitrosative stress resistance
YEAIGEETFRKLVRRFYERVAKDPELRALYPEEDLAPAEERLYLFLVQYFGGPPTYSEQRGHPMLRARHF
PFPIDGKAREAWLACMRTAMDDIDLDQEVREEMMAYFEKVANHMVN
>gnl|CDD|381259 cd08919, PBP-like, Phycobiliproteins (PBPs) and related proteins. phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). This family also contains allophycocyanin-like (Apl) proteins, which conserve the residues critical for chromophore interactions, but may not maintain the proper alpha-beta subunit interactions and tertiary structure of PBPs. The genes encoding the Apl proteins cluster with light-responsive regulatory components, so these may have photoresponsive regulatory role(s). Included in this family is the PBP-like domain of the core-membrane linker polypeptide (LCM). The LCM serves both as a terminal energy acceptor and as a linker polypeptide. Its single phycocyanobilin (PCB) chromophore is one of two terminal energy transmitters, and transfers excitations from the hundreds of chromophores of the PBS to the RCs. This family also includes some proteins which have glutathione-S-transferases (GST) domains N-terminal to this PBP-like domain
ALTKLIAEADGGRYLSSSELQALKGYIQSAEARLEAAEKLRENAEEIVKQAVRKLFAENPPLFRPGGXDR
SAKCLRDLDYVLRYIAYAMLAGDPDPLDERLLNWLREIYKALGVPLDAYAAAYKDMKEAASQLLTPEAAK
LVRPYLDYAISAL
>gnl|CDD|271272 cd08920, Ngb, Neuroglobins. The Ngb described in this subfamily is a hexacoordinated heme globin chiefly expressed in neurons of the brain and retina. In the human brain, it is highly expressed in the hypothalamus, amygdala, and in the pontine tegmental nuclei. It affords protection of brain neurons from ischemia and hypoxia. In rats, it plays a role in the neuroprotection of limb ischemic preconditioning (LIP). It plays roles as: a sensor of oxygen levels; a store or reservoir for oxygen; a facilitator for oxygen transport; a regulator of ROS; and a scavenger of nitric oxide. It also functions in the protection against apoptosis and in sleep regulation. This subgroup contains Ngb from mammalian and non-mammalian vertebrates, including fish, amphibians and reptiles; the functionally pentacoordinated acoelomorph Symsagittifera roscoffensis Ngb does not belong to this subgroup
LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFQYNGRQFSSPQDCLSSPEFLDHIRKVML
VIDAAVSHLEDLSSLEEYLTSLGRKHRAVGVKLESFSTVGESLLYMLESSLGPAFTPDTREAWSTLYGAV
VQAMSRGW
>gnl|CDD|381260 cd08922, FHb-globin, Globin domain of flavohemoglobins (flavoHbs). FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses. FlavoHb expression affects Aspergillus nidulans sexual development and mycotoxin production, and Dictyostelium discoideum development. This family also includes some single-domain goblins (SDgbs)
LSEETIAIVKATAPVLAEHGEEITTRFYKRMFAEHPELKNLFNMANQASGRQPKALAAAVLAYAANIDNL
EVLLPAVERIAHKHVSLGVKPEHYPIVGEYLLEAIKEVLGDAATPEVLDAWAEAYGFLADILIEREKQLY
>gnl|CDD|381261 cd08923, class1-2_nsHbs_Lbs, Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related proteins. Class1 nsHbs include the dimeric hexacoordinate Trema tomentosa nsHb and the dimeric hexacoordinate nsHb from monocot barley. Also belonging to this family is ParaHb, a dimeric pentacoordinate Hb from the root nodules of Parasponia andersonii, a non-legume capable of symbiotic nitrogen fixation. ParaHb is unusual in that it has different heme redox potentials for each subunit; it may have evolved from class1 nsHbs. Lbs are pentacoordinate, and facilitate the diffusion of O2 to the respiring Rhizobium bacteroids within root nodules. They may have evolved from class 2 nonsymbiotic hemoglobins (class2 nsHb)
FTEKQEALVKSSWEVLKKNIPQLSLRFFLLILEIAPAAKDMFSFLKDSDEIPENNPKLKAHAMKVFKMTC
ESAIQLRKKGKVVVADTTLKRLGSVHLKKGVADPHFEVVKEALLKTIKEAVGDKWSEEMKCAWGEAYDQL
AAAIKKE
>gnl|CDD|271275 cd08924, Cygb, Cytoglobin and related globins. Cygb is a hexacoordinated heme-containing protein, able to bind O2, NO and carbon monoxide. It has both nitric oxide dioxygenase and lipid peroxidase activities, and potentially participates in the maintenance of normal phenotype by implementing a homeostatic effect, to counteract stress conditions imposed on a cell. Cygb is implicated in multiple human pathologies: it is up-regulated in fibrosis and neurodegenerative disorders, and down-regulated in multiple cancer types, and may have a tumor suppressor role. It is expressed ubiquitously across a broad range of vertebrate organs including liver, heart, brain, lung, retina, and gut. In the human brain, it was detected at high levels in the habenula, hypothalamus, thalamus, hippocampus and pontine tegmental nuclei, detected at a low level in the cerebral cortex, and undetected in the cerebellar cortex
LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPLEMERSSQLRKHARRVMGA
LNTVVENLHDPDKVSSVLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLI
YSHVTAAYKEVGW
>gnl|CDD|381262 cd08925, Hb-beta-like, Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits. Hb is the oxygen transport protein of erythrocytes. It is an allosterically modulated heterotetramer. Hemoglobin A (HbA) is the most common Hb in adult humans, and is formed from two alpha-chains and two beta-chains (alpha2beta2). An equilibrium exists between deoxygenated/unliganded/T(tense state) Hb having low oxygen affinity, and oxygenated /liganded/R(relaxed state) Hb having a high oxygen affinity. Various endogenous heterotropic effectors bind Hb to modulate its oxygen affinity and cooperative behavior, e.g. hydrogen ions, chloride ions, carbon dioxide and 2,3-bisphosphoglycerate. Hb is also an allosterically regulated nitrite reductase; the plasma nitrite anion may be activated by hemoglobin in areas of hypoxia to bring about vasodilation. Other Hb types are: HbA2 (alpha2delta2) which in normal individuals, is naturally expressed at a low level; Hb Portland-1 (zeta2gamma2), Hb Gower-1 (zeta2epsilon2), and Hb Gower-2 (alpha2epsilon2), which are Hbs present during the embryonic period; and fetal hemoglobin (HbF, alpha2gamma2), the primary hemoglobin throughout most of gestation. These Hbs types have differences in O2 affinity and in their interactions with allosteric effectors
EKAAITAVWGKVDVDEVGAEALARLLIVYPWTQRYFSSFGDLSSAAAIAGNPKVAAHGKKVLGALGEAIK
HLDDIKATFADLSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY
>gnl|CDD|271277 cd08926, Mb, Animal Myoglobins. Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein whose expression has long been considered limited to cardiomyocytes and striated skeletal muscle cell, however it has recently been found localized in a wide variety of tissues including smooth muscle cells. As a physiological catalyst, it can modulate reactive oxygen species levels, facilitate oxygen diffusion within the cell, and scavenge or generate NO depending on oxygen tensions within the cell. Through its NO dioxygenase and nitrite reductase activities, Mb regulates mitochondrial function in energy-demanding tissues
ADWDLVLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKGISQDDLKSNEDLKKHGVTVLTALGEI
LKQKGSHEAELKPLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEAN
YKELGFQG
>gnl|CDD|381263 cd08927, Hb-alpha-like, Hemoglobin alpha, zeta, mu, theta, and related Hb subunits. Hb is the oxygen transport protein of erythrocytes. It is an allosterically modulated heterotetramer. Hemoglobin A (HbA) is the most common Hb in adult humans, and is formed from two alpha-chains and two beta-chains (alpha2beta2). An equilibrium exists between deoxygenated/unliganded/T(tense state) Hb having low oxygen affinity, and oxygenated /liganded/R(relaxed state) Hb having a high oxygen affinity. Various endogenous heterotropic effectors bind Hb to modulate its oxygen affinity and cooperative behavior, e.g. hydrogen ions, chloride ions, carbon dioxide and 2,3-bisphosphoglycerate. Hb is also an allosterically regulated nitrite reductase; the plasma nitrite anion may be activated by hemoglobin in areas of hypoxia to bring about vasodilation. Other Hb types are: HbA2 (alpha2delta2) which in normal individuals, is naturally expressed at a low level; Hb Portland-1 (zeta2gamma2), Hb Gower-1 (zeta2epsilon2), and Hb Gower-2 (alpha2epsilon2), which are Hbs present during the embryonic period; and fetal hemoglobin (HbF, alpha2gamma2), the primary hemoglobin throughout most of gestation. These Hbs types have differences in O2 affinity and in their interactions with allosteric effectors
LSAADKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAGSAQVKAHGKKVMDALGDAVK
HLDDLPGALSKLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKYR
>gnl|CDD|187633 cd08928, KR_fFAS_like_SDR_c_like, ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c)-like SDRs. KR domain of FAS, including the fungal-type multidomain FAS alpha chain, and the single domain daunorubicin C-13 ketoreductase. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD(P)-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Single domain daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
VLITGAGDGSIGAEVLQGLLNGGAKVYVTTSRFSRQVTKYYQDIYAACGAAGSVLIVVPFNQGSKQDVEA
LAIGIYDTVNGLGWDLDLYGPFAAIPETGIEIPAIDSKSEVAHRIMLTNLLRPKGLVKIQKQLRGQETRP
AQVILPFSPNHGTFGDDGAYSESKLHLETLFNRWASESWGNDLTVCGAHIGWTRGTLGGEAAPEGLEKGG
VRTFSQAEMAFNLLGLYFPPKVVLCQPLPVSADLNGGL
>gnl|CDD|187634 cd08929, SDR_c4, classical (c) SDR, subgroup 4. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEE
AFGGLDALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAF
KGGAAYNASKFGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFAGSPEGQAWKLAPEDVAQAVLFALEMP
ARALVSRIELRPTRPP
>gnl|CDD|187635 cd08930, SDR_c8, classical (c) SDR, subgroup 8. This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSKESIKEL
IESYLEKFGRIDILINNAYPSPKVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINI
ASIYGVIAPDFRIYENTQMYSPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQPSEFLEKY
TKKCPLKRMLNPEDLRGAIIFLLSDASSYVTGQNLVIDGG
>gnl|CDD|187636 cd08931, SDR_c9, classical (c) SDR, subgroup 9. This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAENVVAGALDVTDRAAWAAALADFA
AATGGRLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIY
GQPDLAVYSATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTPILTKGETGAAPKKGLGRVLPVSDVAK
VVWAAAHGVPKLHYTVG
>gnl|CDD|212493 cd08932, HetN_like_SDR_c, HetN oxidoreductase-like, classical (c) SDR. This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASGGDVEAVPYDARDPEDARALVDALRDR
FGRIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLA
GNAGYSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVGAFPPEEMIQPKDIANLVRMV
IELPENITSVAVL
>gnl|CDD|187638 cd08933, RDH_SDR_c, retinal dehydrogenase-like, classical (c) SDR. These classical SDRs includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the short-chain dehydrogenases/reductase family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
MASGLRYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVPCDVTK
EEDIKTLISVTVERFGRIDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGN
IINLSSLVGSIGQKQAAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTLAT
IKEGELAQLLGRMGTEAESGLAALFLAAEATFCTGIDLLLSGGAELGYGYK
>gnl|CDD|187639 cd08934, CAD_SDR_c, clavulanic acid dehydrogenase (CAD), classical (c) SDR. CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAA
VERTVEALGRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSV
AGRVAVRNSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEAYEERISTIR
KLQAEDIAAAVRYAVTAPHHVTVNEILIRPTDQ
>gnl|CDD|187640 cd08935, mannonate_red_SDR_c, putative D-mannonate oxidoreductase, classical (c) SDR. D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
FSLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLE
RAREEIVAQFGTVDILINGAGGNHPDATTDPEHYEPETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGK
DMLEQKGGSIINISSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLL
INPDGSYTDRSNKILGRTPMGRFGKPEELLGALLFLASEKASSFVTGVVIPVDGGFSAYSG
>gnl|CDD|187641 cd08936, CR_SDR_c, Porcine peroxisomal carbonyl reductase like, classical (c) SDR. This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
GVTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGK
AEDRERLVATAVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGG
SVVIVSSVAAFHPFPGLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDKAVEES
MKETLRIRRLGQPEDCAGIVSFLCSEDASYITGETVVVGGGTPSRL
>gnl|CDD|187642 cd08937, DHB_DH-like_SDR_c, 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR. DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEILAAGDAAHVHTADLETYAGAQGV
VRAAVERFGRVDVLINNVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSS
IATRGIYRIPYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNAAPMSEQEKVWYQRIV
DQTLDSSLMGRYGTIDEQVRAILFLASDEASYITGTVLPVGGGDLG
>gnl|CDD|187643 cd08939, KDSR-like_SDR_c, 3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR. These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANASGQKVSYISADLSDYEEVE
QAFAQAVEKGGPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVS
SQAALVGIYGYSAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEEENKTKPEETKAIEGSS
GPITPEEAARIIVKGLDRGYDDVFTDFIG
>gnl|CDD|187644 cd08940, HBDH_SDR_c, d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs. DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
KGKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAKHGVKVLYHGADLSKPAAIED
MVAYAQRQFGGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIAS
VHGLVASANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEKQISALAQKNGVPQEQAA
RELLLEKQPSKQFVTPEQLGDTAVFLASDAASQITGTAVSVDGGWTAQ
>gnl|CDD|187645 cd08941, 3KS_SDR_c, 3-keto steroid reductase, classical (c) SDRs. 3-keto steroid reductase (in concert with other enzymes) catalyzes NADP-dependent sterol C-4 demethylation, as part of steroid biosynthesis. 3-keto reductase is a classical SDR, with a well conserved canonical active site tetrad and fairly well conserved characteristic NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
RKVVLVTGANSGLGLAICERLLAEDDENPELTLILACRNLQRAEAACRALLASHPDARVVFDYVLVDLSN
MVSVFAAAKELKKRYPRLDYLYLNAGIMPNPGIDWIGAIKEVLTNPLFAVTNPTYKIQAEGLLSQGDKAT
EDGLGEVFQTNVFGHYYLIRELEPLLCRSDGGSQIIWTSSLNASPKYFSLEDIQHLKGPAPYSSSKYLVD
LLSLALNRKFNKLGVYSYVVHPGICTTNLTYGILPPFTWTLALPLFYLLRRLGSPWHTISPYNGAEALVW
LALQKPESQD
>gnl|CDD|187646 cd08942, RhlG_SDR_c, RhlG and related beta-ketoacyl reductases, classical (c) SDRs. Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
LFSVAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYGECIAIPADLSSEEGIE
ALVARVAERSDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATAENPARV
INIGSIAGIVVSGLENYSYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNDPAALEAE
EKSIPLGRWGRPEDMAGLAIMLASRAGAYLTGAVIPVDGG
>gnl|CDD|187647 cd08943, R1PA_ADH_SDR_c, rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs. This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQGGPRALGVQCDVTSEAQVQSAFEQ
AVLEFGGLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIVFNASKNA
VAPGPNAAAYSAAKAAEAHLARCLALEGGEDGIRVNTVNPDAVFRGSKIWEGVWRAARAKAYGLLEEEYR
TRNLLKREVLPEDVAEAVVAMASEDFGKTTGAIVTVDGGN
>gnl|CDD|187648 cd08944, SDR_c12, classical (c) SDR, subgroup 12. These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFER
AVEEFGGLDLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAG
QSGDPGYGAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGALGPGGFHLLIHQ
LQGRLGRPEDVAAAVVFLLSDDASFITGQVLCVDGG
>gnl|CDD|187649 cd08945, PKR_SDR_c, Polyketide ketoreductase, classical (c) SDR. Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
QDSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEAL
VAAAVARYGPIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAGGMLERGTGRIINIA
STGGKQGVVHAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVREHYADIWEVSTEEA
FDRITARVPLGRYVTPEEVAGMVAYLIGDGAAAVTAQALNVCGGLGNY
>gnl|CDD|212494 cd08946, SDR_e, extended (e) SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
ILVTGGAGFIGSHLVRRLLERGHEVVVIDRLDVVVHLAALVGVPASWDNPDEDFETNVVGTLNLLEAARK
AGVKRFVYASSASVYGSPEGLPEEEETPPRPLSPYGVSKLAAEHLLRSYGESYGLPVVILRLANVYGPGQ
RPRLDGVVNDFIRRALEGKPLTVFGGGNQTRDFIHVDDVVRAILHALENPLEGGGVYNIG
>gnl|CDD|187651 cd08947, NmrA_TMR_like_SDR_a, NmrA (a transcriptional regulator), HSCARG (an NADPH sensor), and triphenylmethane reductase (TMR) like proteins, atypical (a) SDRs. Atypical SDRs belonging to this subgroup include NmrA, HSCARG, and TMR, these proteins bind NAD(P) but they lack the usual catalytic residues of the SDRs. Atypical SDRs are distinct from classical SDRs. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. TMR, an NADP-binding protein, lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
IAVTGATGQQGGSVIRHLLAKGASQVRAVVRNVEKAATLADQGVEVRQGDYNQPELLQKAFAGASKLFII
TGPHYDNTLEIKQGKNVADAARRAGVKHIYSTGYAFAEESAIPLAHVKLAVEYAIRTTGIPYTFLRNGLY
TENFVSEGLPAADTGSGAIVLPAGDGPVPSVTRNDLGPAAAQLLKEEGHEGKTINLVSNCRWTPDELAAA
LSRVLGKKVVHQPV
>gnl|CDD|187652 cd08948, 5beta-POR_like_SDR_a, progesterone 5-beta-reductase-like proteins (5beta-POR), atypical (a) SDRs. 5beta-POR catalyzes the reduction of progesterone to 5beta-pregnane-3,20-dione in Digitalis plants. This subgroup of atypical-extended SDRs, shares the structure of an extended SDR, but has a different glycine-rich nucleotide binding motif (GXXGXXG) and lacks the YXXXK active site motif of classical and extended SDRs. Tyr-179 and Lys 147 are present in the active site, but not in the usual SDR configuration. Given these differences, it has been proposed that this subfamily represents a new SDR class. Other atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
VALVVGATGISGWALVEHLLSDPGTWWKVYGLSRRPLPTEDDPRLVEHIGIDLLDPADTVLRAKLPGLED
VTHVFYAAYIERPDEAELVEVNGAMLRNFLDALEPASPNLKHVVLQTGTKHYGVHLGPFKTPRPEEPARE
DPPRLLPPNFYYDQEDLLFEAAKGKGWTWSVLRPDAIIGFAPGNAMNLALTLAVYAAICRELGAPLRFPG
SPAAWNALSDATDARLLARFTIWAATHPEAANEAFNVTNGDVFRWKELWPRLAEYFGLEGAPPEPEAEAG
ADKAPVWEELMADHGLQAAWDELVERHG
>gnl|CDD|187653 cd08950, KR_fFAS_SDR_c_like, ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like SDRs. KR domain of fungal-type fatty acid synthase (FAS), type I. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member, is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the Classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
SGLSFAGKVALVTGAGPGSIGAEVVAGLLAGGATVIVTTSRFSHERTAFFQKLYRKHGAKGSKLWVVPFN
QASKQDVEALVEYIYDEQTKLAWDLDFLFPFAAISENGRLIDIDSKSELAHRLMLTNVLRLLGCVKKQKR
ARGIVTRPTHVVLPLSPNHGTFGGDGLYSESKLALEALFNRWHSESWSDYLSICGAVIGWTRGTGLMGGN
DVLAEAVEKLGVRTFSTEEMAFNLLGLLSPEVVELAQEAPVYADLTGGL
>gnl|CDD|187654 cd08951, DR_C-13_KR_SDR_c_like, daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs. Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
TRSPPPMKRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRK
LADQVNAIGRFDAVIHNAGILSGPNRKTPDTGIPAMVAVNVLAPYVLTALIRRPKRLIYLSSGMHRGGNA
SLDDIDWFNRGENDSPAYSDSKLHVLTLAAAVARRWKDVSSNAVHPGWVPTKMGGAGAPDDLEQGHLTQV
WLAESDDPQALTSGGYFYHRRLQEPHPASEDSRLQEKLVQALEEVTGVKL
>gnl|CDD|187655 cd08952, KR_1_SDR_x, ketoreductase (KR), subgroup 1, complex (x) SDRs. Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
WRRRRRERAAVDSWRYRVTWRPLPDPPAARLTGTWLVVVPAGADDALAAAVARALAAAGAEVVVLEVDAA
DADAAAAAALAAAAAGGPVAGVLSLLALDERPHPDHPAVPAGLAATLALVQALGDAGVDAPLWCVTRGAV
AVGPDDPLPDPAQAAVWGLGRVAALEHPDRWGGLVDLPADLDARALRRLAAVLAGAGGEDQVAVRASGVF
ARRLVRAPAPAPAARPWRPRGTVLVTGGTGALGAHVARWLARRGAEHLVLTSRRGPDAPGAAELVAELTA
LGARVTVAACDVADRDALAALLAALPAGHPLTAVVHAAGVLDDGPLDDLTPERLAEVLRAKVAGARHLDE
LTRDRDLDAFVLFSSIAGVWGSGGQGAYAAANAYLDALAERRRARGLPATSVAWGPWAGGGMAAGAAAER
LRRRGLRPMDPELALAALRRALDHDETAVVVADVDWERFAPAFTAARPSPLLDELPEARA
>gnl|CDD|187656 cd08953, KR_2_SDR_x, ketoreductase (KR), subgroup 2, complex (x) SDRs. Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
FGMGGTNAHVIDLAYTLQVGREAMEERRRLEALASLQPVWAPAALASAFLALAYEAALLGLAAAEAALLD
ALSALDPAAALQLLESLQRLLKAGLLAARASGRALLQVVTGLPGALGLDALDPAGAGLAGLLRTLAQEYP
GLTCRLIDLDAGEASAEALARELAAELAAPGAAEVRYRDGLRYVQTLEPLPLPAGAAASAPLKPGGVYLV
TGGAGGIGRALARALARRYGARLVLLGRSPLPPEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLE
KVRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFVLFSSVSAFFGG
AGQADYAAANAFLDAFAAYLRQRGPQGRVLSINWPAWREGGMAADLGARELLARAGLLPIEPEEGLQALE
QALSSDLPQVLVSPGD
>gnl|CDD|187657 cd08954, KR_1_FAS_SDR_x, beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs. NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
ILENVCNLVLNGNLQSENLYALLKPNGFLLFVEPLKGSTLGDTWWLTDNDIRKQSCLLSQEQWNQLLKST
QEVSIKLSGVKKSFYGSVLCRIQSPTDKSEFLPVEEQTFEYVEILKSLLATASCKPVLLTADGCESSGVI
GAVRYFREEPQLKLIRCLFVSNLNSQKEPIIRNGKVYYERVKKNSNIKNVYKSGSWGDFRHLLLDLSILK
TNYPINLGKSYLITGGSGGLGLEILKWLVKRGAVENIIILSRSGMKWELELLIREWKSQNIKFHFVSVDV
SDVSSLEKAINLILNAPKIGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCWKL
DYFVLFSSVSSIRGSAGQCNYVCANSVLDSLSRYRKSIGLPSIAINWGAIGDVGFVSRNESVDTLLGGQG
LLPQSINSCLGTLDLFLQNPSPNLVLSSFNFA
>gnl|CDD|187658 cd08955, KR_2_FAS_SDR_x, beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x). Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS, an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
ALLGSAPLAGVVHLWSLDAPREEPADAASQELGCASALHLVQALSKAGLRRAPRLWLVTRGAQSVLADGE
PVSPAQAPLWGLGRVIALEHPELRCGLVDLDPEATAAEEAEALLAELLAADAEDQVALRGGARYVARLVR
APARPLRPDATYLITGGLGGLGLLVAEWLVERGARHLVLTGRRAPSAAARQAIAALEEAGAEVVVLAADV
SDRDALAAALAQIRASLPPLRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLPLDFFV
LFSSVASLLGSPGQANYAAANAFLDALAHYRRARGLPALSINWGPWAEVGMAASLARQARLEARGVGAIS
PAAGLQALGQLLRTGSTQVGVAPVDW
>gnl|CDD|187659 cd08956, KR_3_FAS_SDR_x, beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x). Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
ALFRVDWTPVAAPPAAAPPDWALLGLAAAGAAGAAHADLDALAAALAAGAAVPDVVVVPCPAAAGGDLAA
AAHAAAARALALLQAWLADPRLADSRLVVVTRGAVAAGPDEDVPDLAAAAVWGLVRSAQAEHPGRFVLVD
LDDDAASAAALPAALASGEPQLALRDGRLLVPRLARVAPAATLPPVPRPLDPDGTVLITGGTGTLGALLA
RHLVTEHGVRHLLLVSRRGPDAPGAAELVAELAALGAEVTVAACDVADRAALAALLAAVPADHPLTAVVH
AAGVLDDGVLTSLTPERLDAVLRPKVDAAWHLHELTRDLDLAAFVLFSSAAGVLGSPGQANYAAANAFLD
ALAQHRRARGLPATSLAWGLWAQASGMTAHLSDADLARLARGGLRPLSAEEGLALFDAALAADEPVLVPA
RLDLAALRAAAAGALPPLLRGLVRAPRR
>gnl|CDD|187660 cd08957, WbmH_like_SDR_e, Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs. Bordetella bronchiseptica enzymes WbmH and WbmG, and related proteins. This subgroup exhibits the active site tetrad and NAD-binding motif of the extended SDR family. It has been proposed that the active site in Bordetella WbmG and WbmH cannot function as an epimerase, and that it plays a role in O-antigen synthesis pathway from UDP-2,3-diacetamido-2,3-dideoxy-l-galacturonic acid. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
MKVLITGGAGQIGSHLIEHLLERGHQVVVIDNFATGRREHLPDHPNLTVVEGSIADKALVDKLFGDFKPD
AVVHTAAAYKDPDDWYEDTLTNVVGGANVVQAAKKAGVKRLIYFQTALCYGLKPMQQPIRLDHPRAPPGS
SYAISKTAGEYYLELSGVDFVTFRLANVTGPRNVIGPLPTFYQRLKAGKKCFVTDTRRDFVFVKDLARVV
DKALDGIRGHGAYHFSSGEDVSIKELFDAVVEALDLPLRPEVEVVELGPDDVPSILLDPSRTFQDFGWKE
FTPLSETVSAALAWYDKHGVTGEFTHL
>gnl|CDD|187661 cd08958, FR_SDR_e, flavonoid reductase (FR), extended (e) SDRs. This subgroup contains FRs of the extended SDR-type and related proteins. These FRs act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites; they have the characteristic active site triad of the SDRs (though not the upstream active site Asn) and a NADP-binding motif that is very similar to the typical extended SDR motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
VCVTGASGFIGSWLVKRLLQRGYTVRATVRDPGDEKKVAHLLELEGAKERLKLFKADLLDYGSFDAAIDG
CDGVFHVASPVDFDSEDPEEEMIEPAVKGTLNVLEACAKAKSVKRVVFTSSVAAVVWNPNRGEGKVVDES
CWSDLDFCKKTKLWYALSKTLAEKAAWEFAEENGLDLVTVNPSLVVGPFLQPSLNSSSQLILSLLKGNAE
MYQNGSLALVHVDDVADAHILLYEKPSASGRYICSSHVVTRPELAALLAKKYPQYNIPTKFEDDQPGVAR
VKLSSKKLKDLGF
>gnl|CDD|350084 cd08959, ArfGap_ArfGap1_like, ARF1 GTPase-activating protein 1-like. ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) domain is a part of ArfGap1-like proteins that play a crucial role in controlling of membrane trafficking, particularly in the formation of COPI (coat protein complex I)-coated vesicles on Golgi membranes. The ArfGAP1 protein subfamily consists of three members: ArfGAP1 (Gcs1p in yeast), ArfGAP2 and ArfGAP3 (both are homologs of yeast Glo3p). ArfGAP2/3 are closely related, but with little similarity to ArfGAP1, except the catalytic ArfGAP domain. They promote hydrolysis of GTP bound to the small G protein ADP-ribosylation factor 1 (Arf1), which leads to the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. Thus, the GAP catalytic activity plays a key role in the formation of COPI vesicles from Golgi membrane. In contrast to ArfGAP1, which displays membrane curvature-dependent ArfGAP activity, ArfGAP2 and ArfGAP3 activities are dependent on coatomer (the core COPI complex) which required for efficient recruitment of ArfGAP2 and ArfGAP3 to the Golgi membrane. Accordingly, ArfGAP2/3 has been implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Unlike ArfGAP1, which is controlled by membrane curvature through its amphipathic lipid packing sensor (ALPS) motifs, ArfGAP2/3 do not possess ALPS motif
TRAVFKKLRSKPENKVCFDCGAKNPQWASVTYGIFICLDCSGVHRGLGVHISFVRSTTMDKWTEEQLRKM
KVGGNANAREFFKQHGIYDSMDIKEKYNSRAAALYRDKLAALAEG
>gnl|CDD|185752 cd08961, GH64-TLP-SF, glycoside hydrolase family 64 (beta-1,3-glucanases which produce specific pentasaccharide oligomers) and thaumatin-like proteins. This superfamily includes glycoside hydrolases of family 64 (GH64), these are mostly bacterial beta-1,3-glucanases which cleave long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers and are implicated in fungal cell wall degradation. Also included in this superfamily are thaumatin, the sweet-tasting protein from the African berry Thaumatococcus daniellii, and thaumatin-like proteins (TLPs) which are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Like GH64s, some TLPs also hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. Plant TLPs are classified as pathogenesis-related (PR) protein family 5 (PR5), their expression is induced by environmental stresses such as pathogen/pest attack, drought and cold. Several members of the plant TLP family have been reported as food allergens from fruits, and pollen allergens from conifers. Streptomyces matensis laminaripentaose-producing, beta-1,3-glucanase (GH64-LPHase), and TLPs have in common, a core N-terminal barrel domain (domain I) composed of 10 beta-strands, two coming from the C-terminal region of the protein. In TLPs, this core domain is flanked by two shorter domains (domains II and III). Small TLPs, such as Triticum aestivum thaumatin-like xylanase inhibitor, have a deletion in the third domain (domain II). GH64-LPHase has a second C-terminal domain which corresponds positional to, but is much larger than, domain III of TLP. GH64-LPHase and TLPs are described as crescent-fold structures. Critical functional residues, common to GH64-LPHase and TLPs are a Glu and an Asp residue. LPHase has an electronegative, substrate-binding cleft and the afore mentioned conserved Glu and Asp residues are the catalytic residues essential for beta-1,3-glucan cleavage. In TLPs, these residues are two of the four conserved residues which contribute to the strong electronegative character of the cleft which is associated with the antifungal activity of TLPs
LTITNNCGYQVWIYNLGTELSSAPDASGPGLAPGRSTTIQIPKGFSGRIWFRTGCSMDFSGTTGCLTQDP
GVVNPTDPNRDPPFTLAEFTLNDFNSGDFIDSSLVDGFNAPMTVGPRRGDGTCLSTGDAYSYAFDDHEST
FTCGGGRNYSLTF
>gnl|CDD|199206 cd08962, GatD, GatD subunit of archaeal Glu-tRNA amidotransferase. GatD is involved in the alternative synthesis of Gln-tRNA(Gln) in archaea via the transamidation of incorrectly charged Glu-tRNA(Gln). GatD is active as a dimer, and it provides the amino group required for this reaction. GatD is related to bacterial L-asparaginases (amidohydrolases), which catalyze the hydrolysis of asparagine to aspartic acid and ammonia. This CD spans both the L-asparaginase_like domain and an N-terminal supplementary domain
DRVRVKKGDRVYEGILMPRPELSDDDIIVLKLDNGYNIGIDISIEEIELIEKGEKPKPELGEEIEKKPGL
PKVSIISTGGTIASRVDYRTGAVSPAFTAEELLRAIPELLDIANIKAEVLFNILSENMTPEYWVKIAEAV
YKEIKEGADGVVVAHGTDTMHYTASALSFMLETLPVPVVFVGAQRSSDRPSSDAAMNLIAAVLVAASDIA
EVVVVMHGTTSDDYCLLHRGTRVRKMHTSRRDAFQSINDEPLAKVDPPGKIEKLSKDYRKRGDEELELND
KLEEKVALIKFYPGMDPEIIDFYVDKGYKGIVIEGTGLGHVSEDLIPSIKKAIDDGIPVVMTSQCIYGRV
NLNVYSTGRELLKAGVIPGEDMLPETAYVKLMWVLGNTDDLEEVRKLMLTNL
>gnl|CDD|199207 cd08963, L-asparaginase_I, Type I (cytosolic) bacterial L-asparaginase. Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type I L-asparaginases, which are highly specific for asparagine and localized in the cytosol. Type I L-asparaginase acts as a dimer. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. One example of an enzyme with no L-glutaminase activity is the type I L-asparaginase from Wolinella succinogenes
KKILLLYTGGTIASVKTEGGLAPALTAEELLSYLPELLEDCFIEVEQLPNIDSSNMTPEDWLRIARAIAE
NYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGSIRGV
YVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLFYPDLDPNVFLLKLI
PGLLPAILDALLEKYPRGLILEGFGAGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSDLSVYAVGQA
LLEAGVIPGGDMTTEAAVAKLMWLLGQTDDAEEVRQ
>gnl|CDD|199208 cd08964, L-asparaginase_II, Type II (periplasmic) bacterial L-asparaginase. Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type II L-asparaginases, which tend to be highly specific for asparagine and localized to the periplasm. They are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL), but not without severe side effects. Tumor cells appear to have a heightened dependence on exogenous L-aspartate, and depleting their surroundings of L-aspartate may starve cancerous ALL cells. Type II L-asparaginase acts as a tetramer, which is actually a dimer of two tightly bound dimers. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase
PRIAVLATGGTIAGTADSSGAYAAPTLSGEELLAAVPGLADVADVEVEQVSNLPSSDMTPADWLALAARV
NEALADPDVDGVVVTHGTDTLEETAYFLDLTLDSDKPVVLTGAMRPADAPSADGPANLLDAVRVAASPEA
RGRGVLVVFNDEIHAARDVTKTHTTSLDAFASPGFGPLGYVDGGKVRFYRRPARPHTLPSEFDDELPRVD
IVYAYAGADGALLDAAVAAGAKGIVIAGFGAGNVPPALVEALERAVAKGIPVVRSSRVGNGRVLPVYGYG
GGADLAEAGAIFAGDLSPQKARILLMLALAAGLDPEEIQ
>gnl|CDD|176799 cd08965, EcNei-like_N, N-terminal domain of Escherichia coli Nei/endonuclease VIII and related DNA glycosylases. This family contains the N-terminal domain of proteobacteria Nei and related DNA glycosylases. It includes Escherichia coli Nei, and belongs to the FpgNei_N [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. Escherichia coli Nei has been well studied, it is a DNA glycosylase/AP lyase that excises damaged pyrimidines, including 5-hydroxycytosine, 5-hydroxyuracil, and uracil glycol. In addition to this EcNei-like_N domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a canonical zinc-finger motif
PEGPEIRRAADRIEAAIKGRPLEEVWFAFPHLKEYEAQLKGQNVTRVETRGKALLTHFDNGLSIYSHNQL
YGVWRVRKRGNYPKTNRQLRVALHTAKKSALLYSASDIDVLPTEE
>gnl|CDD|176800 cd08966, EcFpg-like_N, N-terminal domain of Escherichia coli Fpg1/MutM and related bacterial DNA glycosylases. This family contains the N-terminal domain of Escherichia coli Fpg1/MutM and related bacterial DNA glycosylases. It belongs to the FpgNei_N [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. Escherichia coli Fpg mainly recognizes and excises damaged purines such as 8-oxo-7,8-dihydroguanine (8-oxoG) and 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG). It is bifunctional, having both a DNA glycosylase (recognition activity) and a AP lyase activity. In addition to this EcFpg-like_N domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zinc-finger motif, which also contribute residues to the active site
PELPEVETVRRGLAPHLVGRRIEDVEVRRPKLRRPPDPEEFAERLVGRRITGVERRGKYLLFELDDGLVL
VIHLGMTGRLLVVPPDEPPEKHDHVIFELDDGRELRFNDPRRFGTLLLVP
>gnl|CDD|176801 cd08967, MeNeil1_N, N-terminal domain of metazoan Nei-like glycosylase 1 (NEIL1). This family contains the N-terminal domain of metazoan NEIL1. It belongs to the FpgNei_N [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. NEIL1 recognizes the oxidized pyrimidines 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG) and 4,6-diamino- 5-formamidopyrimidine (FapyA), thymine glycol (Tg) and 5-hydroxyuracil (5-OHU). However, even though it has weak activity on 8-oxo-7,8-dihydroguanine (8-oxoG), it does show strong preference for the products of its further oxidation: spiroiminodihydantoin and guanidinohydantoin. In addition to this MeNeil1_N domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zincless finger motif. This characteristic "zincless finger" motif, is a structural equivalent of the zinc finger common to other members of the Fpg/Nei family. Neil1 is one of three homologs found in eukaryotes and its lineage extends back as far as early metazoans
MPEGPELHLASLFVNKMCKGLIFTGAVEKSSVSKNPEVPFACKAYTISAESRGKELRLILSPLPAANGKK
ECKSQEEMRIVFRFGMSGSFQFTPVDEIPKHAHLRFYTKEEPKRVLSFVDIRRFGTWQVGG
>gnl|CDD|176802 cd08968, MeNeil2_N, N-terminal domain of metazoan Nei-like glycosylase 2 (NEIL2). This family contains the N-terminal domain of the metazoan protein Neil2. It belongs to the FpgNei_N [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. NEIL2 repairs 5-hydroxyuracil (5-OHU) and other oxidized derivatives of cytosine, but it shows preference for DNA bubble structures. In addition to this MeNeil2_N domain, NEIL2 contains a helix-two turn-helix (H2TH) domain and a characteristic CHCC zinc finger motif. Neil2 is one of three homologs found in eukaryotes
MPEGPSVRKFHHLVSPFVGQRVVKVGGSSKKINPNDLQGLRLQDSQVHGKNLFLHFDLDEEMGPDRDAGR
WLRFHFGLFGSVRANEFSRAKKANKRGDWKDPNPRLVLHFESGGFLVFYNCRMSWC
>gnl|CDD|176803 cd08969, MeNeil3_N, N-terminal domain of metazoan Nei-like glycosylase 3 (NEIL3). This family contains the N-terminal domain of the Metazoan Neil3. It belongs to the FpgNei_N [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. In contrast, mouse NEIL3 (MmuNEIL3) forms a Schiff base intermediate via its N-terminal valine. The latter is a functional DNA glycosylase in vitro and in vivo. MmuNEIL3 prefers lesions in single-stranded DNA and in bubble structures. In duplex DNA, it recognizes the oxidized purines spiroiminodihydantoin (Sp), guanidinohydantoin (Gh), 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG) and 4,6-diamino-5-formamidopyrimidine (FapyA), but not 8-oxo-7,8-dihydroguanine (8-oxoG). Since the expression of the MmuNeil3 glycosylase domain (MmuNeil3delta324) reduces both the high spontaneous mutation frequency and the FapyG level in a Escherichia coli mutant lacking Fpg, Nei and MutY glycosylase activites, NEIL3 may play a role in repairing FapyG in vivo. In addition to this MeNeil3_N domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zinc finger motif, plus a characteristic C-terminal extension that contains additional zinc fingers. Neil3 is one of three homologs found in eukaryotes
MVEGPGCTLNGEKIRARVEKGQRVVHVRGSAPSSPSGAASRNGAGSKDERSHVLDSLTGQVYTGVETLGK
ELFMYFGDKALRIHFGMNGSMRINPLESKDRSGASPVLEVQLTKDLICFFDSTVEIRNAAECQQKIRMME
>gnl|CDD|176804 cd08970, AcNei1_N, N-terminal domain of the actinomycetal Nei1 and related DNA glycosylases. This family contains the N-terminal domain of the actinomycetal Nei1 and related DNA glycosylases. It belongs to the FpgNei_N [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. This family contains mostly actinomycetes and includes Mycobacterium tuberculosis Nei1 (MtuNei1). MtuNei1 recognizes oxidized pyrimidines such as thymine glycol (Tg) and 5,6-dihydrouracil on both double stranded and single stranded DNA, it has a strong preference for the 5R isomer of Tg. In addition to this domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zinc-finger motif
MPEGHVIHRLARDLNAAFAGQPVRVSSPQGRFADGAALLDGRVLADAEAHGKHLFLGFEGDRILHVHLGL
YGKFRFGGDPPPPPRGQVRLRLVGDTHAADLRGPTVCELL
>gnl|CDD|176805 cd08971, AcNei2_N, N-terminal domain of the actinomycetal Nei2 and related DNA glycosylases. This family contains the N-terminal domain of the actinomycetal Nei2 and related DNA glycosylases. It belongs to the FpgNei_N [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. This family contains mostly actinomycetes and includes Mycobacterium tuberculosis Nei2 (MtuNei2). Complementation experiments in repair-deficient Escherichia coli (fpg mutY nei triple and nei nth double mutants), support that MtuNei2 is functionally active in vivo and recognizes both guanine and cytosine oxidation products. In addition to this AcNei2_N domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zinc-finger motif
MPEGDTVHRAARRLRRALAGRVLTRADLRVPRLATADLAGRTVEEVVARGKHLLIRFDGGLTLHTHLRMD
GSWHVYRPGERWRRPAHQARAVLATADWTAVGFRLGVLELVPTR
>gnl|CDD|176806 cd08972, PF_Nei_N, N-terminal domain of the plant and fungal Nei and related proteins. This family contains the N-terminal domain of plant and Fungi Nei and related proteins. It belongs to the FpgNei_N [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. The plant and fungal FpgNei glycosylases prefer the oxidized pyrimidines spiroiminodihydantoin (Sp), guanidinohydantoin (Gh) over 8-oxoguanine in double stranded oligonucleotides and also show weak activity on single stranded DNA. In addition to this domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a characteristic zincless finger motif. They share a common ancestor not shared with other eukaryotic members of the FpgNei family
MPELPEVERARRLLEEHCLGKKITKVDAQDDDKVFGGVTPGAFQKALLGRTITSAHRKGKYFWLTLDGDA
PVPVMHFGMTGAISIKGVKTIYYKMLRPPKEEDQTWPPRFYKFVLTLEDGTELAFTDPRRLGRVRLV
>gnl|CDD|176807 cd08973, BaFpgNei_N_1, Uncharacterized bacterial subgroup of the N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII) base-excision repair DNA glycosylases. This family is an uncharacterized bacterial subgroup of the FpgNei_N domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. This N-terminal proline is conserved in this family. Escherichia coli Fpg prefers 8-oxo-7,8-dihydroguanine (8-oxoG) and oxidized purines and Escherichia coli Nei recognizes oxidized pyrimidines. However, neither Escherichia coli Fpg or Nei belong to this family. In addition to this BaFpgNei_N_1 domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zinc-finger motif
MPELPEVEVYAENLERRLTGKTITRVELASKSLLVTPDPPLEALEGRTVTGVRRHGKRLDFEFDNGLHLV
LHLMLAGWLYWTEAGALLPGKKGPIALRFEDYGGGLDLTEAGTKKRAALHLV
>gnl|CDD|176808 cd08974, BaFpgNei_N_2, Uncharacterized bacterial subgroup of the N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII) base-excision repair DNA glycosylases. This family is an uncharacterized bacterial subgroup of the FpgNei_N domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. This N-terminal proline is conserved in this family. Escherichia coli Fpg prefers 8-oxo-7,8-dihydroguanine (8-oxoG) and oxidized purines, and Escherichia coli Nei recognizes oxidized pyrimidines. However, neither Escherichia coli Fpg or Nei belong to this family. In addition to this BaFpgNei_N_2 domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain. Most also contain a zinc-finger motif
MPEGPSIVILREAAAAFKGQTVIRASGNAKIDKDRLAGQKVLAIRSWGKHFLLEFEDFTVRIHLLLFGSY
RINERKDAPPRLSLGFDNGELNFYTCSV
>gnl|CDD|176809 cd08975, BaFpgNei_N_3, Uncharacterized bacterial subgroup of the N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII) base-excision repair DNA glycosylases. This family is an uncharacterized bacterial subgroup of the FpgNei_N domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. One exception is mouse Nei-like glycosylase 3 (Neil3) which forms a Schiff base intermediate via its N-terminal valine. In this family the N-terminal proline is replaced by an isoleucine or valine. Escherichia coli Fpg prefers 8-oxo-7,8-dihydroguanine (8-oxoG) and oxidized purines and Escherichia coli Nei recognizes oxidized pyrimidines. However, neither Escherichia coli Fpg or Nei belong to this family. In addition to this BaFpgNei_N_3 domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zinc-finger motif
LELPESATLSKQLNETLKGKRITDVFPATSPHKFTWYNGDPNEYDELLVGKRITSAEGFGGFVEIIFEDK
RLLFNDGVNVRYYYGGEKIPKKYQLLIEFDDDSFLVFTVAMYGGIAA
>gnl|CDD|176810 cd08976, BaFpgNei_N_4, Uncharacterized bacterial subgroup of the N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII) base-excision repair DNA glycosylases. This family is an uncharacterized bacterial subgroup of the FpgNei_N domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. This N-terminal proline is conserved in this family. Escherichia coli Fpg prefers 8-oxo-7,8-dihydroguanine (8-oxoG) and oxidized purines and Escherichia coli Nei recognizes oxidized pyrimidines. However, neither Escherichia coli Fpg or Nei belong to this family. In addition to this BaFpgNei_N_4 domain, most enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zinc-finger motif
PELPEVEVQKQYLERTSLHRKIVEVEVGDDKILGEPKATLREVLEGRTFTETHRIGKYLFLKTKEGGWLV
MHFGMTGKLDYYPDDEDPPKHARLLLHFEDGFRLAFECPRKFGRVRL
>gnl|CDD|185760 cd08977, SusD, starch binding outer membrane protein SusD. SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases
DPTDAEAALTGLYAGLRSSGNYYGGTLGLLGDLRADDXVAASNSGDYTEVNTNNNPNDSAFGTSSWNGVY
TNINNANIFLEKIDEASELTEANRNRYKGEAKFIRALAYFYLTRLFGGVPLSTAADQGTETPPRDSQEEV
YTQILADLDEAIALLPEASSAQDFYIYFGDGRAWKKAARALLARVYLYLANYTAADYAEALTAAEKSFKG
GVTLLTNLFGENAANSKEDIFEIYYADSGDNSNPLGSLNNNNGYANFRVSADIIDKLDGYGDPRLSLAPI
PIIRYAEVLLLRAEALARLGNGADAIEYLNAVRRRSGGNAANNTSQASTAEELLEEILDERRLELFGEGH
RWYDLRRTG
>gnl|CDD|350092 cd08978, GH_F, Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 enzymes, is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
ADPSILKDNGRYYIYATTDDTGTGTGIVVWKSKDLVNWKEEGTVLSRGKSKSWGTGNLWAPEVYYFNSGK
WYLYYSAVPNGGGGRIYVATSDSPEGPFTPIVSGKLGDRGSGSIDPTVFVDDDGKLYLYYGDEDDSGDIY
VAELDPDLLTIKGDVTLLIGEVVGSGFRGNYFEGPAVFKRNGYYYLIYSAGGTDGGYAIGYATSDSPLGP
WEKASHNPGLQTSGATGIYGPGHGSIFQDEGDRWYIVYHAR
>gnl|CDD|350093 cd08979, GH_J, Glycosyl hydrolase families 32 and 68, which form the clan GH-J. This glycosyl hydrolase family clan J (according to carbohydrate-active enzymes database (CAZY)) includes family 32 (GH32) and 68 (GH68). GH32 enzymes include invertase (EC 3.2.1.26) and other other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). The GH68 family consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10, also known as beta-D-fructofuranosyl transferase), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9). GH32 and GH68 family enzymes are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) and catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
WDPWPLQNANGYYHLFYLYGPPKNFADNVSIGHAYSKDLENWIDLPKALGANDTISDDQTQEWSGSATFT
SDGKWRAFYTGFSGKHYGVQSQTIAYSKDLASWSSLNINGVPQFPDELPPSSGDNQTFRDPHVVWDKEKG
HWYMVFTAREGANGVLGMYESTDLKHWKKVMKPIASNTVTGEWECPNLVKMNGRWYLFFGSRGSKGITSN
GIHYLYAVGPSGPWRYKPLNKTGLVLSTDLDPDDGTFFYAGKLVPDAKGNNLVLTGWMPNRGFYADSGAD
WQSGFAIPRLLN
>gnl|CDD|350094 cd08980, GH43_LbAraf43-like, Glycosyl hydrolase family 43 proteins such as Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans GbtXyl43B. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities. In addition to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans IT-08 beta-xylosidase / exo-xylanase (GbtXyl43B). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) familiesGH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
ADPYIFKHEDYYYFTATVGANRIYLRKADTLLGLSTAEEVTIWDKPPSGDYSGLIWAPEIHYIDGKWYIY
FAASPENDFGAGHHRMYVLKNLSGDPFEGDWGEPGEIANNDADRQTVKDGLTNTESFSLDCTVFKVNGKL
YFTWAQRDGDPEKFNQCIYIAKMENPWTLKGDPVMLTKPEYDWEKKGDKVNEGPAVVEHNGKVYLAYSAS
AFWDDNYAIGMLTAEAGADLLNPASWTKSPTPVFKSSDENGQYGPGHNSFVKSEDGTEDWIVYHAR
>gnl|CDD|350095 cd08981, GH43_Bt1873-like, Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron BT_1873. This glycosyl hydrolase family 43 (GH43) subfamily includes Bacteroides thetaiotaomicron VPI-5482 endo-arabinase (Bt1873;BT_1873), as well as uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the GH43 enzymes in this family may display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
LEDIRIRDPFILADKKTGTYYLYGTTDKDCWWGKGTGFDVYVSKDLENWEGPYEVFRPPEDFWADRNFWA
PEVHEYNGKYYLFATFKAEGNGRRGTQILVSDSPLGPFVPLSDGPVTPEDWMCLDGTLYVDEDGKPWMVF
CHEWVQVGDGTICAVRLSDDLKEAIGEPVLLFRASEAPWARPIPEFGIGGPGYVTDGPFLYRTKDGKLLM
LWSSFGEGGYAIGVARSESGKITGPWIQEPEPLFSDDGGHGMLFRTFDGQLMLTLHSPNDTPPERPIFIE
VEEEGDGLL
>gnl|CDD|350096 cd08982, GH43-like, Glycosyl hydrolase family 43 protein; uncharacterized. This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
SYREAADPTVVLFKGKYYLFASKSGGYWHSDDLVNWKFIPTNGLPIEDYAPTVVEINGTLYFTASGGPGP
IYRTDDPLGGKWELVAESGPFGFWDPALFVDDDGRLYLYWGCSNKDPIYGVELDPNTGFRPIGEPVPLIS
FDPDKHGWERFGEDNEDPGLAPWIEGAWMTKHNGKYYLQYAAPGTEFKTYADGVYVSDSPLGPFTYAPNN
PFSYKPGGFITGAGHGSTFQDKYGNYWHFGTMVISVNHNFERRIGLFPAGFDKDGELYCNTRFGDYPQYL
PGKKFDPPDSLFTGWMLLSYNKPVTASS
>gnl|CDD|350097 cd08983, GH43_Bt3655-like, Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655. This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
ALNGGNPVLTSTVGTKGVRDPFIIRGPEDGKFYLVATDLWIAGGAQWNGSRGIGVWESTDLVNWSEQRLV
KMVSPPNAGNAWAPEAIYDPETGQYVVYWSSSLYGDGGGGNHRIYYATTKDFKTFSEPKVLFDPGFNVID
TTIVKDGGTYYRFYKDETTGKGIRLATSDSLTGPWTTVTTGGGAGTGGGVEGPTVFKLNDGGKWYLYYDQ
YGGGGYGPFETTDLASGTWTPASEDYSLPGGPRHGTVLPITAAEYDALLAAW
>gnl|CDD|350098 cd08984, GH43-like, Glycosyl hydrolase family 43. This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
LFRDPVYDGAADPVVIWNPATKEWWMFYTQRRATVDGPGVAWVHGTPIGIASSKDGATWTYRGTADGLGP
EPGENTFWAPEVIVDGGTYHMFVTYIPGVPTDWGGPRRIVHYTSPDLWNWKFVGTLDLSSDRVIDACVAR
LPDGTWRMWYKDEADGSTTYAADSPDLYHWTVEGPAIGDRPHEGPNVFRWKGYYWMITDEWRGLAVYRSD
DAENWTRQGGILLEPGTRPDDGVRGRHADVVVSGDRAYIFYFTHPGRDYENEDAVDPYAQRRSSIQVAEL
EVVDGKLVCDR
>gnl|CDD|350099 cd08985, GH43_CtGH43-like, Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
IHAHGGGILQEGDTYYWYGESRKGLDNDNLSHGINCYSSTDLYNWRFEGLVLPASGVEVVRDISPGYVIE
RPKVLYNARTRKYVMWFHLDNPNYGFAAVGVATSDTPTGPFTFVRSFRPDGYPSRDMTLFQDPDGTAYLV
RSTDHNTDIGISRLSDDYLDTTGASSTFKGPKREAPALFKRGGTYYLITSGLTGWNPNPSRLARADSPLG
PWSTWGNLPVGGPGADTTYDSQPAFVFPVEGQGGELFIYMGDRWNPGGGGVGNATYVWLPLLF
>gnl|CDD|350100 cd08986, GH43-like, Glycosyl hydrolase family 43 protein; uncharacterized. This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
WLRDPYITLGPDGYYYLTGTTGGPDWWGVNDGIRLWRSKDLKDWEYLGLVWDLEKDGWWQWEPQWWTPDS
KNKRALWAPEIHYINGTWYITHSMNGGGTGLLKSTTGKPEGPYVDPMGGPLGKGIDPSLFEDDDGTVYLV
WGNGQIARLKKDMSGFAEEPRKIDPSGNREIGHEGAFIFKIGGKYVLFGAAWSTDKMRKGTYDLYYATSD
SIYGPYSERRFAGPHGGHGTPFKDKDGQWWCTAFGNDNVAPIREQPG
>gnl|CDD|350101 cd08987, GH62, Glycosyl hydrolase family 62, characterized arabinofuranosidases. The glycosyl hydrolase family 62 (GH62) includes eukaryotic (mostly fungal) and prokaryotic enzymes which are characterized arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. These enzymes show significantly different substrate preference with rather low specific activity towards natural substrates and differ in catalytic efficiency. They do not act on xylose moieties in xylan that are adorned with an arabinose side chain at both O2 and O3 positions, nor do they display any non-specific arabinofuranosidase activity. The synergistic action in biomass degradation makes GH62 promising candidates for biotechnological improvements of biofuel production and in various biorefinery applications. These enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan
LPSTFRWTSTGPLISPKADWDDIVSVKDPTIVYYNGKYHVFATTADKSGGWQMGYFSFTDWSDAASAPQY
YLDQIGGGYRCAPQVFYFAPHKLWYLIYQNKGGAAYSTNTDITDPNGWSAPQPLFSGTINGGGGGWIDFW
VICDDANCYLFFSDDDGKLYRSETTLANFPNGWSEPVIALQDNRNDLFEAAHVYKVKGTNKYLLLVEAIG
SGGRYFRSWTADSLDGPWTPLADTESNPFAGNANVTFSGAKWTDDISHGELIRSGYDQTLEIDPCNLQFL
YQGVDPNAGGDYGELPYRLGLLTL
>gnl|CDD|350102 cd08988, GH43_ABN, Glycosyl hydrolase family 43. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
HDPSIIKEGGTYYAFGTGTDGFGIPIAKSKDLGNWTIVGEAFATLPSWKGGSPPSADGNLWAPDISQHKG
KYYLYYSVSDNGSNTSAIGLATANNPQGPFKDEGPAKPVVTSDNAGNAIDPDLFQDEDGQNWLLYGSFWG
GIWLQKLDKNGLVVNPPGNGKSIAVLYYVSIEAPYITYAGGYYYLFVSAGSCCDGGNSTYHTRVGRSKKV
TGPYLDKGGLDMLEGGGTLLTKGKNQWVGPGHNSIVTGDNGVDYLVLHAYDANDNSSRKLYILSLFW
>gnl|CDD|350103 cd08989, GH43_XYL-like, Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium beta-D-xylosidase SXA. These are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. It also includes various GH43 family GH43 arabinofuranosidases (EC 3.2.1.55) including Humicola insolens alpha-L-arabinofuranosidase AXHd3, Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB), and the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
NPVLPGFHPDPSVVRVGDDYYMVNSTFQYFPGIPISHSKDLVHWTPIGHALTRPEQLDLTGGPDGGGIWA
PDISYHDGKFYIYYTVVLNVGSWKGRRNYLVTSEDPEGPWSEPVWLDEGGIDPSLFVDDDGKHYMLLNPG
GIRLAELNPDCTKQIGEPKRIWEGTGGRAPEGPHLYKKDGYYYLLTAEGGTGYGHAITIARSKTIYGPYE
PCPYNPILRQQDPQAPLQRCGHGKLVETPDGEWWMVYLCGRPLPGGYCPLGRETALAPVEWT
>gnl|CDD|350104 cd08990, GH43_AXH_like, Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, beta-xylosidase, endo-1,4-beta-xylanase, and alpha-L-arabinofuranosidase. This subgroup includes Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160), Butyrivibrio proteoclasticus alpha-L-arabinofuranosidase (Xsa43E;bpr_I2319), Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and metagenomic beta-xylosidase (EC 3.2.1.37) / alpha-L-arabinofuranosidase (EC 3.2.1.55) CoXyl43. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_AXH-like subgroup includes enzymes that have been characterized with beta-xylosidase, alpha-L-arabinofuranosidase, endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43 shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
ADPAAHVFNGKVYVYASHDEAPANGYFIMDDWHVFSSTDLVNWTDHGEILPPDDVFWWASGNAWAPDAVY
KNGKYYFYFPVGQASDGFGIGVAVSDSPAGPFKDALGKPLIPEGLNGIEGIDPAVFVDDDGRAYLYFGGG
GGYYVAKLKDDMISLAGEPQKIKNGGLKGFFEAPWVFKRNGTYYLSYAGGWAYPAEIAYSTADSPLGPYT
YRGVILDPVGSGTNHGSIVEFKGQWYLFYHTADLSGGGDFRRSVCIDYLHYNADGTIVP
>gnl|CDD|350105 cd08991, GH43_HoAraf43-like, Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580). This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
ADPFVLKHNGTYYLYGTGGDDGRGFKVYVSDDLVNWEYPGGALEEPGLWGTKGFWAPEVFYYNGKFYMYY
SANGGDHGEHIAVAVSDSPLGPFRDKGKLLIPAGGFSIDAHVFIDDDGKWYLYYVRDDLGGEPGNRIYVA
ELEDDLSLIGEPTLVLCPTADERWEYGEGRDWHTTEGPTVLKHNGTYYLTYSANHFRSPDYAVGYATADS
PLGPWTKYEGNPILSRNDGGVNGPGHNSVFKDPDGDLYIVYHTHDSDETVEPRKMRIDRLRFDGDKLSVL
GPT
>gnl|CDD|350106 cd08992, GH117, Glycosyl hydrolase family 117 (GH117). This glycoside hydrolase 117 (GH117) family includes alpha-1,3-L-neoagarooligosaccharide hydrolase (EC 3.2.1.-); alpha-1,3-L-neoagarobiase/neoagarobiose hydrolase (NABH, EC 3.2.1.-). In the agarolytic pathway, in order to metabolize agar, NABH is an essential enzyme because it converts alpha-neoagarobiose (O-3,6-anhydro-alpha-l-galactopyranosyl-(1,3)-d-galactose) into fermentable monosaccharides (d-galactose and 3,6-anhydro-l-galactose). Thus, these enzymes have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate. This family includes Zobellia galactanivorans enzymes, Zg4663 and Zg3615 (also known as ZgAhgA and ZgAhgB, respectively) that have been shown to have similar activity on unsubstituted agarose oligosaccharides while Zg3597 has been shown to be inactive, possibly due to differences in dimerization conformation, active-site structure and function. GH117 shares distant sequence similarity with families GH43 and GH32. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
EWFSEFKYTPVKGLGYEEGVTRRDPSSVIKVNGTYYVWYTKSDEGPPVGFGKANDTLKVFPWDLADIWYA
TSKDGWTWKEQGVAVGRGPKGAYDDRSVFTPEILVHKGKYYLYYQAVKSPYGGIRDKNPIGMAVADSPDG
PWTKLDEPILEPGDEGEWEKAKGDFDSHKVHDPCLIVYNGKFYLYYKGEPMGEGITGGGREIKWGVAIAD
NPEGPYVKSPYNPITNSGHEVCVWPYKGGIAALLTTDGPEKNTIQYAEDGINFEIMSVIKNAPVAAGLFR
PDDFDTDPGEGLRWGLSHVYNASKDWSYLRRFDC
>gnl|CDD|350107 cd08993, GH130, Glycosyl hydrolase family 130. This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), among others that have yet to be characterized. They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor. This family includes Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) and beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2), enzymes that phosphorolyze beta-mannosidic linkages at the non-reducing ends of their substrates, and have substantially diverse substrate specificity that are determined by three loop regions
YPANSVFNAGAVKFNGKYLLLFRVEDLNGRSFLGLAESDDGIHFTVEPEPILTPDEPFEPYEETGVYDPR
ITKIDDTYYITFAADSDHGPRIGLARTKDFKTFERLELISEPDNRNGVLFPEKINGKYARLDRPSDGGHT
SGGDIWISYSPDLIHWGNSRLVMGPRPGPWDNDKIGPGAPPIKTEEGWLLIYHGVRTTCSGFVYRLGAAL
LDLEDPSKVIARSREPILAPEEPYERVGDVPNVVFPCGAIVEEDGEVKIYYGAADTVICLATATIDDLV
>gnl|CDD|350108 cd08994, GH43_62_32_68_117_130-like, Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130. Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans
PVGNGFEDPGYSVWGGSIIKGEDGKYHLFYSRWPKGCGFHGWLTHSEIAHAVSDSPEGPYKFVEVVLPGR
GGGFWDGDTTHNPTIKKFDGKYYLYYIGNTGPGPDPPLWWGHRNNQRIGVAVADSPNGPWKRFDKPILDP
RPRSWDDLITSNPAVLKRPDGSYLLYYKGGKKNPGGNRKHGVAVSDSPEGPYTKLSDPPVYEPGVNGQTE
DPFIWYDKGQYHLIVKDMGGIFTGEGGGGALLRSKDGINWKLAPGLAYSTEVKWTDGTTEKWGRLERPQL
LQDEDGKPTYLFLA
>gnl|CDD|350109 cd08995, GH32_EcAec43-like, Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 (FosGH2). This glycosyl hydrolase family 32 (GH32) subgroup includes Escherichia coli strain BEN2908 putative glycoside hydrolase Aec43 (FosGH2). GH32 enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). GH32 family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize
GDVMPFYDDGKFHLFYLHDPRDPAPHRGGHPWALVTTKDLVHWTEHGEAIPYGGDDDQDLAIGTGSVIKD
DGTYHAFYTGHNPDFGKPKQVIMHATSTDLKTWTKDPEFTFIADPEGYEKNDFRDPFVFWNEEEGEYWML
VAARKNDGPGNRRGCIALYTSKDLKNWTFEGPFYAPGSYNMPECPDLFKMGDWWYLVFSEFSERRKTHYR
ISDSPEGPWRTPADDTFDGRAFYAAKTASDGGRRYLFGWIPTREGNKDSGAWDWGGNLVVHELVQNEDGT
L
>gnl|CDD|350110 cd08996, GH32_FFase, Glycosyl hydrolase family 32, beta-fructosidases. Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
GWMNDPNGLIYYKGRYHLFYQYNPYGPVWGPMHWGHAVSDDLVHWEHLPIALAPPGGYDEDGCFSGSAVV
DDGKPTLFYTGVRDLGDGRQTQCLATSDDDLITWEKYPGNPVIPPPPGGGVTDFRDPFVWKEGGTWYMVV
GGGLEDGGGAVLLYRSDDLRDWEYLGVLLDAASDGDTGEMWECPDFFPLGGKWVLLFSPQGGGNLLGVVY
LIGDFDGETFRFEPESFGLLDYGGDFYAPQTFLDPDGRRILIGWLREWRSPEPEAEAGWAGALSLPRELS
L
>gnl|CDD|350111 cd08997, GH68, Glycosyl hydrolase family 68, includes levansucrase, beta-fructofuranosidase and inulosucrase. Glycosyl hydrolase family 68 (GH68) consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Levansucrase, also known as beta-D-fructofuranosyl transferase, catalyzes the transfer of the sucrose fructosyl moiety to a growing levan chain. Similarly, inulosucrase catalyzes long inulin-type of fructans, and beta-fructofuranosidases create fructooligosaccharides (FOS). However, in the absence of high fructan/sucrose ratio, some GH68 enzymes can also use fructan as donor substrate. GH68 retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Biotechnological applications of these enzymes include use of inulin in inexpensive production of rich fructose syrups as well as use of FOS as health-promoting pre-biotics
VWDSWPLQDADGTVANYNGYRLVFALTAPRNPDPDDRHDDARIRLFYSRDGGWWDLGGKAFPDGLTPGSR
EWSGSAVLDPDGTVTLFYTAAGRRGEAGQTFEQRLFEVTATLSGDGGGVSISGWTDHKEIFEADGEIYQT
VDQGGGAGGDIKAFRDPHYFRDPADGKRYLVFEANTAGSRGQQGCNNLDNGQVLKNSVKKDGASYFNGAI
GLAEANNDDLTKWELLPPLLSANGVNDELERPHIVVHNGKYYLFTSTHGSTFAPDGLSGPTGLYGFVSDS
LRGPYKPLNGSGLVLANPPEAPFQTYSWYVLPDLLVTSFVDTRGLAGGEARARFGGTFAPSFKLRIDGDT
TRVV
>gnl|CDD|350112 cd08998, GH43_Arb43a-like, Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase Arb43A. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
VHDPSIIKDDGGTYYVFSTGAGIQIRTSKDLVNWEFVGTVFPEGPAWAAAEVPGGAGGLWAPDVVYVNGR
YYLYYSASTFGSNRSAIGLATSTTLDDGPWTDQGLVVSSSPGDDYNAIDPNVFVDADGRLWLAYGSFWGG
IKLVELDPATGKLRPGSTGTSIASRPGGPGAIEAPYIIYRGGYYYLFVSYGSCCRGANSTYNIRVGRSTS
ITGPYVDRNGVDMLEGGGTLLLGGHGRWIGPGHNSVFRDGDGDYLVYHYYDGDDGGAPKLQIRPLLWT
>gnl|CDD|350113 cd08999, GH43_ABN-like, Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
NPVIDGDFPDPSVIRVGGTYYAFATNSGGKNVQVATSTDLVTWTLLGGDALPDLPAWAAAGGNTWAPDVV
RRPDGKYVMYYSARLKSSGKHCIGVATSDSPLGPFTPVGEPPLCPLDQGGAIDPSGFVDPDGKRYLVYKV
DGNSIGVPTPIMLQELSADGLTLVGEPVELLLNDGPWDGPLVEAPSLVKRDGTYYLFYSSNCYCSPSYAV
GYATSKSITGPYTKAGEPLLLTGDGGLTGPGGADVVEDDGGDWMVFHAWDGGDDVGGGRAMYTAELTWEG
GWPV
>gnl|CDD|350114 cd09000, GH43_SXA-like, Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA. This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPDSGGIWA
PCLSYADGKFWLVYTDVKSVDGPFKDVHNYLVTAESIEGPWSEPIYLNSSGFDPSLFHDDDGRKYLVNML
WDHRPGHNRFAGIVLQEFDPETKKLVGERKVIFKGTELGLTEGPHLYKRDGYYYLLTAEGGTGYEHAVTV
ARSRNIFGPYEVDPDNPLLTSWDDPENPLQKAGHGSLVETPDGEWYLAHLCGRPLPGRGRCPLGRETAIQ
KVEWTDDGWPRL
>gnl|CDD|350115 cd09001, GH43_FsAxh1-like, Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase. This glycosyl hydrolase family 43 (GH43) includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase; xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. This subfamily includes the characterized Clostridium stercorarium F-9 beta-xylosidase Xyl43B. It also includes Humicola insolens AXHd3 (HiAXHd3), a GH43 arabinofuranosidase (EC 3.2.1.55) that hydrolyzes O3-linked arabinose of doubly substituted xylans, a feature of the polysaccharide that is recalcitrant to degradation. It possesses an additional C-terminal beta-sandwich domain such that the interface between the domains comprises a xylan binding cleft that houses the active site pocket. The HiAXHd3 active site is tuned to hydrolyze arabinofuranosyl or xylosyl linkages, and the topology of the distal regions of the substrate binding surface confers specificity. It also includes Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase (Axh1;Fisuc_1769;FSU_2269), Paenibacillus sp. E18 alpha-L-arabinofuranosidase (Abf43A), Bifidobacterium adolescentis ATCC 15703 double substituted xylan alpha-1,3-L-specific arabinofuranosidase d3 (AXHd3;AXH-d3;BaAXH-d3;BAD_0301;E-AFAM2), and Chrysosporium lucknowense C1 arabinoxylan hydrolase / double substituted xylan alpha-1,3-L-arabinofuranosidase (Abn7;AXHd). A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
TYTNPVLWADYPDPDVIRVGDTYYMVSSTMHFSPGAPILHSKDLVNWEIVGYVVDRLDDGDAYYLEDGKN
AYGKGIWAPSLRYHNGKFYVYFCTNTGGTYVYTADDPAGPWSRPALIGKGYHDPSLLFDDDGKAYLVYGN
GEIRLTELSPDGTGVGGEGRVIIDGTEEGLGAEGSHLYKINGYYYIFNIEWGGGGRTQVVLRSKSLYGPY
EGRVVLDDGSGTGDNGPHQGGLVDTPDGEWWFMLFQDRGAVGRIPVLVPVTWKDGWPVIG
>gnl|CDD|350116 cd09002, GH43_XYL-like, Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
YLNPILAGDYPDPSILRDGDDYYMTHSSFDYYPGLLIWHSRDLVNWEPIGAALTEYIGTVWAPDLIKHDG
RYYIYFPAKGGTNYVITADDIAGPWSEPIDLKVGSGIDPGHVVDEDGKRYLFLSGGRRVRLTDDGLSVAG
PPEKVYDGWRYPDEWDVECFCLEGPKLFRRGGYYYLTTAQGGTAGPPTSHMVVSARSKSPHGPWENSPYN
PLVRTQSREEKWWSKGHGTLVEGPDGKWWMVYHGYENGYRTLGRQTLLEPVEWTADGWFRI
>gnl|CDD|350117 cd09003, GH43_XynD-like, Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized Bacillus subtilis arabinoxylan arabinofuranohydrolase (AXH), Caldicellulosiruptor sp. Tok7B.1 beta-1,4-xylanase (EC 3.2.1.8) / alpha-L-arabinosidase (EC 3.2.1.55) XynA, Caldicellulosiruptor sp. Rt69B.1 xylanase C (EC 3.2.1.8) XynC, and Caldicellulosiruptor saccharolyticus beta-xylosidase (EC 3.2.1.37)/ alpha-L-arabinofuranosidase (EC 3.2.1.55) XynF. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. It belongs to the GH43_AXH-like subgroup which includes enzymes that have been annotated as having beta-xylosidase, alpha-L-arabinofuranosidase and arabinoxylan alpha-L-1,3-arabinofuranohydrolase, xylanase (endo-alpha-L-arabinanase) as well as AXH activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Bacillus subtilis AXH (BsAXH-m2,3) has been shown to cleave arabinose units from O-2- or O-3-mono-substituted xylose residues and superposition of its structure with known structures of the GH43 exo-acting enzymes, beta-xylosidase and alpha-L-arabinanase, each in complex with their substrate, reveals a different orientation of the sugar backbone. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
NPIISHRFGADPTALVYNGRVYVYGTNDDQQYNANGKKKDNSYYNINSLTVISSDDMVNWTDHGEIPVAG
PNGIAKWAGNSWAPSVAYKNINGKDKFYLYFANGGGGIGVLTADSPTGPWTDPLGKPLITRSTPGCAGVV
WLFDPAVFIDDDGQGYLYFGGGVPGGSEANPKTARVIKLGDDMISVDGSAVTIDAPYFFEASGINKINGK
YYYSYCTNFSGRDDPAYPGAGSIAYMTSDNPMGPFTYKGVILKNPGTFFGNGGNNHHSIFEFKGKWYIFY
HARTLAKALGGATKGYRSPHIDELTYNADGTIKEV
>gnl|CDD|350118 cd09004, GH43_bXyl-like, Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675) and (BT3662;BT_3662); includes mostly xylanases. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
ADPDIVVFGGRYYIYPTTDGPPGWSSTSFHVFSSTDLVNWTDHGIILDLANDVWWANKGAWAPAVAERNG
KYYFYFSAGSQIGVAVSDSPTGPFTDLGRPLVTGGDYGGQAIDPMVFVDDDGQAYLYWGNGTAYVARLND
DMVSFDGEVVVSITPPNFREGPFVHKRNGIYYLSWSENDTRDPDYRVRYATSDSPLGPWTYRGVGLLLDS
AGGIKGTGHHSIVQVPGTDEWYIAYHRFAVPGGDGYHREVAIDRLEFDADGTIRPV
>gnl|CDD|350156 cd09005, NP-I, nucleoside phosphorylase-I family. The nucleoside phosphorylase-I family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases such as purine nucleoside phosphorylase (PNP, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases such as AMP nucleosidase (AMN, EC 3.2.2.4) and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Members of this family display different physiologically relevant quaternary structures: hexameric (trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP); homotrimeric (human PNP and Escherichia coli PNPII or XapA); hexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD); or homodimeric such as human and Trypanosoma brucei UP. The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
YAIIPGDPERVDVIDSKLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCALGVDTII
RVGSCGALREDIKVGDLVIADGAIRGDGVTPYYVVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTT
DAFYRETREESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEFLSEAEKKAI
EIALDA
>gnl|CDD|350157 cd09006, PNP_EcPNPI-like, purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas vaginalis PNP. Escherichia coli purine nucleoside phosphorylase (PNP)-I (or DeoD) accepts both 6-oxo and 6-amino purine nucleosides as substrates. Trichomonas vaginalis PNP has broad substrate specificity, having phosphorolytic catalytic activity with adenosine, inosine, and guanosine (with adenosine as the preferred substrate). This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYA
YELFKFYGVKNIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKE
LGIPVHVGNVFSSDVFYDDDPELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEELS
AEERETSFTNMIELALET
>gnl|CDD|350158 cd09007, NP-I_spr0068, uncharacterized subfamily of the nucleoside phosphorylase-I family. This subfamily is composed of uncharacterized members including Streptococcus pneumoniae hypothetical protein spr0068. The nucleoside phosphorylase-I (NP-I) family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases such as purine nucleoside phosphorylase (PNP, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases such as AMP nucleosidase (AMN, EC 3.2.2.4) and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Members of the NP-I family display different physiologically relevant quaternary structures: hexameric (trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP); homotrimeric (human PNP and Escherichia coli PNPII or XapA); hexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD); or homodimeric such as human and Trypanosoma brucei UP. The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
LPEKCVLVFSGDLLEYLLEEYGAEKIGELSSAGHTPLYRLEYDGEEVGVVGPPVGAPAAVLVLEELIALG
AKKFIVVGSCGSLDPDLAVGDIILPTSALRDEGTSYHYLPPSRYIEPDPELLDALEEALEKAGIPYVRGK
TWTTDAPYRETRAKVARRRAEGCLAVEMEAAALFAVAQFRGVELAQLLYVSDSLAGEEWDPRGRDEGKDA
REKALELALEA
>gnl|CDD|350159 cd09008, MTAN, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases. This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs): bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAII
NTGVAGGLDPDLKIGDVVIATKVVYHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAAKELGPKVHT
GLIASGDQFVASSEKKEELRENFPALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDFEEFLEL
AAKNSAEVVLEL
>gnl|CDD|350160 cd09009, PNP-EcPNPII_like, purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA). Human PNP catalyzes the reversible phosphorolysis of the purine nucleosides and deoxynucleosides inosine, guanosine, deoxyinosine, and deoxyguanosine. Patients with PNP deficiency typically present with severe immunodeficiency, neurological dysfunction, and autoimmunity. Escherichia coli PNPII, product of the xapA/pndA gene, catalyzes the phosphorolysis of xanthosine, inosine and guanosine with equal efficiency and has been referred to as xanthosine phosphorylase and inosine-guanosine phosphorylase. E. coli PNPII is also capable of converting nicotinamide to nicotinamide riboside, and may be involved in the NAD+ salvage pathway. It is one of two purine nucleoside phosphorylases found in E. coli, which also contains PNPI, which displays a different substrate specificity and belongs to a different subgroup of the nucleoside phosphorylase-I (NP-I) family than PNPII. NP-I family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
EKIEEAADYIRSRIGFKPKIGIILGSGLGGLADEIEDPVEIPYSDIPGFPVSTVEGHAGRLVFGTLGGKP
VLVMQGRFHYYEGYSMQEVTFPVRVMKALGVKTLILTNAAGGLNPDFKPGDLMLITDHINLTGDNPLIGP
NDDEFGPRFPDMSDAYDPELRELAKEAAKELGIPLHEGVYAGVSGPSYETPAEIRMLRTLGADAVGMSTV
PEVIVARHLGMRVLGLSLITNLAAGDSDEPLSHEEVLEAAKKAAPKLSRLLREII
>gnl|CDD|350161 cd09010, MTAP_SsMTAPII_like_MTIP, 5'-deoxy-5'-methylthioadenosine phosphorylases (MTAP) similar to Sulfolobus solfataricus MTAPII and Pseudomonas aeruginosa PAO1 5'-methylthioinosine phosphorylase (MTIP). MTAP catalyzes the reversible phosphorolysis of 5'-deoxy-5'-methylthioadenosine (MTA) to adenine and 5-methylthio-D-ribose-1-phosphate. This subfamily includes human MTAP which is highly specific for MTA, and Sulfolobus solfataricus MTAPII which accepts adenosine in addition to MTA. Two MTAPs have been isolated from S. solfataricus: SsMTAP1 and SsMTAPII, SsMTAP1 belongs to a different subfamily of the nucleoside phosphorylase-I (NP-I) family. This group also includes Pseudomonas aeruginosa PAO1 MTI phosphorylase (MTIP) which uses 5'-methylthioinosine (MTI) as a preferred substrate, and does not use MTA. NP-I family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
IGIIGGSGLYDLDGLEDVEEVTVETPYGKPSGPVTIGELGGREVAFLPRHGRGHRIPPHRINYRANIWAL
KELGVTRIIAVSAVGSLREEIKPGDLVIPDQFIDFTKGRPSTFFDGGGVVHVDFAEPFCPELRELLIEAA
KELGIPVHDGGTYVCTEGPRFETRAEIRMFRRLGGDVVGMTGVPEAVLARELGICYASIALVTNYAAGLE
DEPVTVEEVLEVLKENAEKVKRLLLAAI
>gnl|CDD|319953 cd09011, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
MKFVNPLLVVKDIEKSKKFYEDVLGQKILLDFGENVVFEGGFALQEKKSWLETIIISDLSIKQQSNNFEL
YFEVDDFDAFFEKLNPHKDIEFIHPILEHPWGQRVFRFYDPDGHIIEIGESM
>gnl|CDD|319954 cd09012, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
MIFINLPVTDLEASTAFYEALGFKKNPQFSDEHASCMVVSDNIFVMLLAHDRFKTFIPEPIAVDAKKSTE
VLLTLSAKSRQEVDAFVDKAVEAGGKADPYVNGGDEGFMYGRSFEDLDGHLWEVVWM
>gnl|CDD|319955 cd09013, BphC-JF8_N_like, N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Bacillus sp. JF8, and similar proteins. 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, a key step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). BphC belongs to the type I extradiol dioxygenase family, which requires a metal ion in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. This subfamily of BphC is represented by the enzyme purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8. The members in this family of BphC enzymes may use either Mn(II) or Fe(II) as cofactors. The enzyme purified from Bacillus sp. JF8 is Mn(II)-dependent, however, the enzyme from Rhodococcus jostii RHAI has Fe(II) bound to it. BphC_JF8 is thermostable and its optimum activity is at 85 degrees C. The enzymes in this family have an internal duplication. This family represents the N-terminal repeat
IFDLAQLAHVELLTPKPEESLWFFTDVLGLEETHREGQSVYLRAWGDWEHHTLKLTESPEAGLGHIAWRA
SSPEALERRVAALEASGVGIGWIDGDLGQGPAYRFQSPDGHPMEIYWEVEK
>gnl|CDD|319956 cd09014, BphC-JF8_C_like, C-terminal, catalytic domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase). 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, a key step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). BphC belongs to the type I extradiol dioxygenase family, which requires a metal ion in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. This subfamily of BphC is represented by the enzyme purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8. The members in this family of BphC enzymes may use either Mn(II) or Fe(II) as cofactors. The enzyme purified from Bacillus sp. JF8 is Mn(II)-dependent, however, the enzyme from Rhodococcus jostii RHAI has Fe(II) bound to it. BphC_JF8 is thermostable and its optimum activity is at 85 degrees C. The enzymes in this family have an internal duplication. This family represents the C-terminal repeat
GIPVRRIDHLNLLASDVTANRQFMSDTLGFRLREQIRDNNGGEAGAWMSVSSLVHDVAVMRDGKGEPGRL
HHLAYWYGTPEDLLRAADIFREHGIQIEAGPGKHGISQAFFLYVYEPGGNRVELFGGAGYLIFDPDWEPV
EWTEEDLDRGIAWGGPTLPDSFFTYGT
>gnl|CDD|212511 cd09015, Ureohydrolase, Ureohydrolase superfamily includes arginase, formiminoglutamase, agmatinase and proclavaminate amidinohydrolase (PAH). This family, also known as arginase-like amidino hydrolase family, includes Mn-dependent enzymes: arginase (Arg, EC 3.5.3.1), formimidoylglutamase (HutG, EC 3.5.3.8), agmatinase (SpeB, EC 3.5.3.11), guanidinobutyrase (Gbh, EC=3.5.3.7), proclavaminate amidinohydrolase (PAH, EC 3.5.3.22) and related proteins. These enzymes catalyze hydrolysis of amide bond. They are involved in control of cellular levels of arginine and ornithine (both involved in protein biosynthesis, and production of creatine, polyamines, proline and nitric acid), in histidine and arginine degradation, and in clavulanic acid biosynthesis
AIIGFPYDAGCEGRPGAKFGPSAIRQALLRLALVFTGLGKTRHHHINIYDAGDIRLEGDELEEAHEKLAS
VVQQVLKRGAFPVVLGGDHSIAIATLRAVARHHPDLGVINLDAHLDVNTPETDGRNSSGTPFRQLLEELQ
QSPKHIVCIGVRGLDPGPALFEYARKLGVKYVTMDEVDKLGLGGVLEQLFHYDDGDNVYLSVDVDGLDPA
DAPGVSTPAAGGLSYREGLPILERAGKTKKVMGADIVEVNPLLDEDGRTARLAVRLCWEL
>gnl|CDD|176656 cd09018, DEDDy_polA_RNaseD_like_exo, DEDDy 3'-5' exonuclease domain of family-A DNA polymerases, RNase D, WRN, and similar proteins. DEDDy exonucleases, part of the DnaQ-like (or DEDD) exonuclease superfamily, catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. They contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDy exonucleases are classified as such because of the presence of a specific YX(3)D pattern at ExoIII. The four conserved acidic residues serve as ligands for the two metal ions required for catalysis. This family of DEDDy exonucleases includes the proofreading domains of family A DNA polymerases, as well as RNases such as RNase D and yeast Rrp6p. The Egalitarian (Egl) and Bacillus-like DNA Polymerase I subfamilies do not possess a completely conserved YX(3)D pattern at the ExoIII motif. In addition, the Bacillus-like DNA polymerase I subfamily has inactive 3'-5' exonuclease domains which do not possess the metal-binding residues necessary for activity
VFAFDTETDSLDNISANLVLIQLAIEPGVAALIPVAHDYLALELLKPLLEDEKALKVGQNLKYDRGILLN
YFIELRGIAFDTMLEAYILNSVAGRWDMDSLVERWLGHKLIKFESIAGKLWFNQPLTEEQGRYAAEDADV
TLQIHLKLWP
>gnl|CDD|185696 cd09019, galactose_mutarotase_like, galactose mutarotase_like. Galactose mutarotase catalyzes the conversion of beta-D-galactose to alpha-D-galactose. Beta-D-galactose is produced by the degradation of lactose, a disaccharide composed of beta-D-glucose and beta-D-galactose. This epimerization reaction is the first step in the four-step Leloir pathway, which converts galactose into metabolically important glucose. This epimerization step is followed by the phosophorylation of alpha-D-galactose by galactokinase, an enzyme which can only act on the alpha anomer. A glutamate and a histidine residue of the galactose mutarotase have been shown to be critical for catalysis, the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. Galactose mutarotase is a member of the aldose-1-epimerase superfamily
LYTLTNGNGLRVSILNYGATIQSLKVPDKNGKLRDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFT
LDGKTYQLEANEGPNHLHGGPKGFDKRVWDVEEVEENSVTFSLVSPDGEEGFPGNLTVTVTYTLTDDNEL
TIEYEATTDKPTPVNLTNHSYFNLAGEGSGDILDHELQINADRYLPVDEELIPTGEILPVAGTPFDFRKP
KPIGRIDLDDEQLKLGGGYDHNFVLDKGGGKLRPAARLTSPESGRKLEVYTTQPGVQFYTGNFLDGTPGG
GGKVYGKRSGFCLETQHFPDAPNHPNFPSIILRPGETYRHTTVYRF
>gnl|CDD|185697 cd09020, D-hex-6-P-epi_like, D-hexose-6-phosphate epimerase-like. D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces cerevisiae belongs to the large superfamily of aldose-1-epimerases. Its active site is very similar to the catalytic site of galactose mutarotase, the best studied member of the superfamily. It also contains the conserved glutamate and histidine residues that have been shown in galactose mutarotase to be critical for catalysis, the glutamate serving as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. In addition Ymr099c contains 2 conserved arginine residues which are involved in phosphate binding, and exhibits hexose-6-phosphate mutarotase activity on glucose-6-P, galactose-6-P and mannose-6-P
AIVLDHPGASAEIALQGAQVLSWKPKGGQDLLWLSPQAPFDGGKAIRGGIPVCWPWFGPHGPNADLPAHG
FARTRLWELLEVSEDEDGVTVSLELDDTDETRAIWPHAFELRLTVTLGFDTLELELTVTNTGDKPFSFTA
ALHTYFRVSDIEQVRVEGLEGATYLDKLTDQREKVQGGAVTFDGEVDRVYLNTPAPLTIDDPAWGRRIRI
EKSGSPSAVVWNPWIEKAARMADFPDDGYRRMVCVEAANVADPVTLAPGESHTLSQTIS
>gnl|CDD|185698 cd09021, Aldose_epim_Ec_YphB, aldose 1-epimerase, similar to Escherichia coli YphB. Proteins similar to Escherichia coli YphB are uncharacterized members of the aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen
RLVLAPELGGSIAALTSRGDPTPLLRPADPDAADALAMACFPLVPFSNRIRGGRFLFAGREVALPPNTAD
EPHPLHGDGWRRPWQVVAASADSAELQLDHEADDPPWAYRAEQRFHLAGDGLSITLSVTNRGDRPMPAGL
GFHPYFPRTPDTRLQADADGVWLEDEDHLPTGLRPHPPDWDFSQPRPLPDRWIDNCFTGWDGAALIWPPE
RGLALTIEADAPFSHLVVYRPPGEDFFCLEPVSHAPDAHHGPGDPGLRVLAPGESLSLSMRIT
>gnl|CDD|185699 cd09022, Aldose_epim_Ec_YihR, Aldose 1-epimerase, similar to Escherichia coli YihR. Proteins similar to Escherichia coli YihR are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen
YRAVVTEVGAGLRSLTVGGRDLVEPYPADEVPPGAAGQVLAPWPNRIADGRYTFDGVEHQLPITEPERGN
AIHGLVRWADWQLVEHTDSSVTLRTRIPPQPGYPFTLELTVTYELDDDGLTVTLTATNVGDEPAPFGVGF
HPYLSAGGAPLDECTLTLPADTWLPVDERLLPTGTEPVAGTPYDFRTGRRLGGTALDTAFTDLTRDADGR
ARARLTGPDGRGVELWADESFPWVQVFTADTLPPPGRRRGLAVEPMTCPPNAFNSGTDLIVLAPGETHTA
SWGI
>gnl|CDD|185700 cd09023, Aldose_epim_Ec_c4013, Aldose 1-epimerase, similar to Escherichia coli c4013. Proteins, similar to Escherichia coli c4013, are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen
SFEVLPDRGMDIGRASYKGIPLGWLSPVGLVVPPYYESEGGGGWRSFFGGLLTTCGLDHIGHPEVDDGEE
YPLHGRISNTPAELVGVEEDEEGDYEIEVSGEVREAALFGENLRLERTIETDLGSNEIRLEDRVTNEGFR
PTPHMLLYHVNFGYPLLDEGARLEIPSKEVTPRDAHAAEGLASWNTYLAPTPGFAEQVYFHEPAADEDGR
APAALVNPRLGLGVEVRFDTDTLPYLTQWKNTGAGAYVLGLEPATNFPNGRAFEREQGELPTLAPGESRS
YRLE
>gnl|CDD|185701 cd09024, Aldose_epim_lacX, Aldose 1-epimerase, similar to Lactococcus lactis lacX. Proteins similar to Lactococcus lactis lacX are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen
ITLENEFLTVTISEHGAELTSIKDKKTGREYLWQGDPAYWGRHAPILFPIVGRLKDDTYTIDGKTYPMPQ
HGFARDMEFEVVEQSDDSVTFELTDNEETLKVYPFDFELRVTYTLEGNTLKVTYEVKNPDDKTMPFSIGG
HPAFNCPLDEGEKFEDYYLEFEPKEELERIPLVGPLGLLGEKKPLLLNEGTLPLTHDLFDDDALIFDNLK
SREVTLKSKKTGHGVTVDFDDFPYLGIWSKPNGAPFVCIEPWYGLADSVGFDGDLEDKEGINKLEPGESF
EASYSITI
>gnl|CDD|185702 cd09025, Aldose_epim_Slr1438, Aldose 1-epimerase, similar to Synechocystis Slr1438. Proteins similar to Synechocystis Slr1438 are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen
YPTYELSDEEAGSRLRVVPERGGLITRWTVQGRELLYLDEERFADPAKSVRGGIPILFPICGNLPDDGYP
LAGQEYTLKQHGFARDLPWEVELLGDGAGLTLTLRDNEATRAVYPFDFELELTYRLAGNTLEIAQRVHNL
GDQPMPFSFGFHPYFAVPDKAKLSLDLPPTRCFDQKTDEEANTPGQFDETEEGVDLLFRPLGPASLTDGA
RGLKITLDHDEPFSNLVVWTDKGKDFVCLEPWTGPRNALNTGERLLLLPPGETEEASVRIQ
>gnl|CDD|193601 cd09027, PET, PET ((Prickle Espinas Testin) domain is involved in protein-protein interactions. PET domain is involved in protein-protein interactions and is usually found in conjunction with LIM domain, which is also a protein-protein interaction domain. The PET containing proteins serve as adaptors or scaffolds to support the assembly of multimeric protein complexes. The PET domain has been found at the N-terminal of four known groups of proteins: prickle, testin, LIMPETin/LIM-9 and overexpressed breast tumor protein (OEBT). Prickle has been implicated in regulation of cell movement through its association with the Dishevelled (Dsh) protein in the planar cell polarity (PCP) pathway. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell contact areas, and at focal adhesion plaques. It interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin, and is involved in cell motility and adhesion events. Knockout mice experiments reveal tumor repressor function of Testin. LIMPETin/LIM-9 contains an N-terminal PET domain and 6 LIM domains at the C-terminal. In Schistosoma mansoni, where LIMPETin was first identified, it is down regulated in sexually mature adult females compared to sexually immature adult females and adult males. Its differential expression indicates that it is a transcription regulator. In C. elegans, LIM-9 may play a role in regulating the assembly and maintenance of the muscle A-band by forming a protein complex with SCPL-1 and UNC-89 and other proteins. OEBT displays a PET domain with two LIM domains, and is predicted to be localized in the nucleus with a possible role in cancer differentiation
EKYAWVPPGLNASLIEQYFECLPKEKVPRLGSEGAKYRRRQLLYQLPAHDLDPRYCDALSEEERAEFEDF
VAARKQEALGVG
>gnl|CDD|350085 cd09028, ArfGap_ArfGap3, Arf1 GTPase-activating protein 3. ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) domain is a part of ArfGap1-like proteins that play a crucial role in controlling of membrane trafficking, particularly in the formation of COPI (coat protein complex I)-coated vesicles on Golgi membranes. The ArfGAP1 protein subfamily consists of three members: ArfGAP1 (Gcs1p in yeast), ArfGAP2 and ArfGAP3 (both are homologs of yeast Glo3p). ArfGAP2/3 are closely related, but with little similarity to ArfGAP1, except the catalytic ArfGAP domain. They promote hydrolysis of GTP bound to the small G protein ADP-ribosylation factor 1 (Arf1), which leads to the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. Thus, the GAP catalytic activity plays a key role in the formation of COPI vesicles from Golgi membrane. In contrast to ArfGAP1, which displays membrane curvature-dependent ArfGAP activity, ArfGAP2 and ArfGAP3 activities are dependent on coatomer (the core COPI complex) which required for efficient recruitment of ArfGAP2 and ArfGAP3 to the Golgi membrane. Accordingly, ArfGAP2/3 has been implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Unlike ArfGAP1, which is controlled by membrane curvature through its amphipathic lipid packing sensor (ALPS) motifs, ArfGAP2/3 do not possess ALPS motif
PSKQDIAAIFKRLRSVPTNKVCFDCGAKNPSWASITYGVFLCIDCSGIHRSLGVHLSFIRSTELDSNWSW
FQLRCMQVGGNANASAFFHQHGCTTNDTNAKYNSRAAQLYREKIKSLATQ
>gnl|CDD|350086 cd09029, ArfGap_ArfGap2, Arf1 GTPase-activating protein 2. ArfGAP (ADP Ribosylation Factor GTPase Activating Protein) domain is a part of ArfGap1-like proteins that play a crucial role in controlling of membrane trafficking, particularly in the formation of COPI (coat protein complex I)-coated vesicles on Golgi membranes. The ArfGAP1 protein subfamily consists of three members: ArfGAP1 (Gcs1p in yeast), ArfGAP2 and ArfGAP3 (both are homologs of yeast Glo3p). ArfGAP2/3 are closely related, but with little similarity to ArfGAP1, except the catalytic ArfGAP domain. They promote hydrolysis of GTP bound to the small G protein ADP-ribosylation factor 1 (Arf1), which leads to the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. Thus, the GAP catalytic activity plays a key role in the formation of COPI vesicles from Golgi membrane. In contrast to ArfGAP1, which displays membrane curvature-dependent ArfGAP activity, ArfGAP2 and ArfGAP3 activities are dependent on coatomer (the core COPI complex) which required for efficient recruitment of ArfGAP2 and ArfGAP3 to the Golgi membrane. Accordingly, ArfGAP2/3 has been implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Unlike ArfGAP1, which is controlled by membrane curvature through its amphipathic lipid packing sensor (ALPS) motifs, ArfGAP2/3 do not possess ALPS motif
PNKTEIQTLFKRLRAIPTNKACFDCGAKNPSWASITYGVFLCIDCSGVHRSLGVHLSFIRSTELDSNWNW
FQLRCMQVGGNANATAFFRQHGCTTNDANAKYNSRAAQMYREKIRQLASA
>gnl|CDD|176923 cd09030, DUF1425, Putative periplasmic lipoprotein. This bacterial family of proteins contains members described as putative lipoproteins, some are also known as YcfL. The function of this family is unknown. Family members have also been annotated as predicted periplasmic lipoproteins (COG5633), and appear to contain an N-terminal membrane lipoprotein lipid attachment side (pfam08139), which is not included in this alignment model
GIAINSQQSVVMDSSLAAGISVIEPRISRTNGLLEAQATLSNTSSKPLTLQYRFYWYDAQGLEVEPEQEP
WQSLTLPGGQTVTLQAVAPNPEAKDFRLYLR
>gnl|CDD|411807 cd09031, KH-I_NOVA_rpt3, third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova). The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one
TVIELEVPENLVGAILGKGGKTLVEIQELTGARIQISKKGEFVPGTRNRKVTITGTPAAVQAAQYLIEQR
I
>gnl|CDD|411808 cd09032, KH-I_N4BP1_like_rpt1, first type I K homology (KH) RNA-binding domain found in the family of NEDD4-binding protein 1 (N4BP1). The N4BP1 family includes N4BP1, NYN domain and retroviral integrase catalytic domain-containing protein (NYNRIN) and KH and NYN domain-containing protein (KHNYN). These proteins are probably of retroviral origin. N4BP1 interacts with and is a substrate of NEDD4 ubiquitin ligase (neural precursor cell expressed, developmentally downregulated 4, E3 ubiquitin protein ligase). It is also an inhibitor of the E3 ubiquitin-protein ligase ITCH, a NEDD4 structurally related E3. N4BP1 acts by interacting with the second WW domain of ITCH, leading to compete with ITCH's substrates and impairing ubiquitination of substrates. NYNRIN, also known as CGIN1/Cousin of GIN1, may contribute to retroviral resistance in mammals by regulating the ubiquitination of viral proteins. KHNYN acts as a novel cofactor for zinc finger antiviral protein (ZAP) to target CpG-containing retroviral RNA for degradation. Members of this family contains two type I K homology (KH) RNA-binding domain. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif
DEFVVPAEKVPLLERSRPRIERLFGVKVSLLEELSKPKDGGKQWVQLEGDEEDVRKAKEYIKALC
>gnl|CDD|411809 cd09033, KH-I_PNPT1, type I K homology (KH) RNA-binding domain found in mitochondrial polyribonucleotide nucleotidyltransferase 1 (PNPT1) and similar proteins. PNPT1, also called 3'-5' RNA exonuclease OLD35, or PNPase old-35, or polynucleotide phosphorylase 1, or PNPase 1, or polynucleotide phosphorylase-like protein, is an RNA-binding protein implicated in numerous RNA metabolic processes. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. It acts as a mitochondrial intermembrane factor with RNA-processing exoribonulease activity. PNPT1 is a component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. It is involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules and required for correct processing and polyadenylation of mitochondrial mRNAs. PNPT1 also plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix
KENGPVTETLEVPPSKRAKFVGPGGYNIKKLQAETGVTITQVDEETFSVFAPNQSAMDEAKEMIEEL
>gnl|CDD|185761 cd09034, BRO1_Alix_like, Protein-interacting Bro1-like domain of mammalian Alix and related domains. This superfamily includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and Rhophilin-2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Brox, Bro1 and Rim20 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 (in the case of Alix, HD-PTP, and Brox) and Snf7 (in the case of yeast Bro1, and Rim20). The single domain protein human Brox, and the isolated Bro1-like domains of Alix, HD-PTP and Rhophilin can bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Alix, HD-PTP, Bro1, and Rim20 also have a V-shaped (V) domain, which in the case of Alix, has been shown to be a dimerization domain and to contain a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in this superfamily. Alix, HD-PTP and Bro1 also have a proline-rich region (PRR); the Alix PRR binds multiple partners. Rhophilin-1, and -2, in addition to this Bro1-like domain, have an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This protein has a C-terminal, catalytically inactive tyrosine phosphatase domain
FIGLPLKKTKEVDVKVPLSKFIPKNYGELEATAVEDLIEKLSKLRNNIVTEQNNDTTCENLLEALKEYLP
YLLGLEKKLPFQKLRDNVEFTWTDSFDTKKESATSLRYELLSILFNLAALASQLANEKLITGSEEDLKQA
IKSLQKAAGYFEYLKEHVLPLPPDELPVDLTEAVLSALSLIMLAQAQECFLLKAEEDKKAKLSLLARLAC
EAAKYYEEALKCLSGVDLETIKNIPKKWLLFLKWKKCIFKALAYYYHGLKLDEANKIGEAIARLQAALEL
LKESERLCKSFLLDVWGNLKKLKEKIEKELEKAERENDFIYFEEVPPEDPLPEIKGALLVKPPPL
>gnl|CDD|176924 cd09071, FAR_C, C-terminal domain of fatty acyl CoA reductases. C-terminal domain of fatty acyl CoA reductases, a family of SDR-like proteins. SDRs or short-chain dehydrogenases/reductases are Rossmann-fold NAD(P)H-binding proteins. Many proteins in this FAR_C family may function as fatty acyl-CoA reductases (FARs), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as the biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. The function of this C-terminal domain is unclear
FLHLLPAYLLDLLLRLLGRKPRLLKLYRKIHKLLDLLEYFTTNEWRFDNDNTRALWERLSEEDRELFNFD
IRSIDWDDYFENYIPGLRKYLL
>gnl|CDD|197307 cd09073, ExoIII_AP-endo, Escherichia coli exonuclease III (ExoIII)-like apurinic/apyrimidinic (AP) endonucleases. The ExoIII family AP endonucleases belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, which is then followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, which have both mutagenic and cytotoxic effects. AP endonucleases can carry out a wide range of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two functional AP endonucleases, for example, APE1/Ref-1 and Ape2 in humans, Apn1 and Apn2 in bakers yeast, Nape and NExo in Neisseria meningitides, and exonuclease III (ExoIII) and endonuclease IV (EndoIV) in Escherichia coli. Usually, one of the two is the dominant AP endonuclease, the other has weak AP endonuclease activity, but exhibits strong 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, and 3'-phosphatase activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes. This family contains the ExoIII family; the EndoIV family belongs to a different superfamily
KIISWNVNGLRARLKKGVLKWLKEEKPDILCLQETKADEDKLPEELQHVEGYHSYWSPARKKGYSGVATL
SKEEPLDVSYGIGGEEFDSEGRVITAEFDDFYLINVYFPNGGRGLERLDYKLRFYEAFLEFLEKLRKRGK
PVVICGDFNVAHEEIDLARPKKNEKNAGFTPEERAWFDKLLSLGYVDTFRHFHPEPGAYTWWSYRGNARE
RNVGWRIDYFLVSEELAEKVKDSGILSKVKGSDHAPVTLEL
>gnl|CDD|197308 cd09074, INPP5c, Catalytic domain of inositol polyphosphate 5-phosphatases. Inositol polyphosphate 5-phosphatases (5-phosphatases) are signal-modifying enzymes, which hydrolyze the 5-phosphate from the inositol ring of specific 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), such as PI(4,5)P2, PI(3,4,5)P3, PI(3,5)P2, I(1,4,5)P3, and I(1,3,4,5)P4. These enzymes are Mg2+-dependent, and belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. In addition to this INPP5c domain, 5-phosphatases often contain additional domains and motifs, such as the SH2 domain, the Sac-1 domain, the proline-rich domain (PRD), CAAX, RhoGAP (RhoGTPase-activating protein), and SKICH [SKIP (skeletal muscle- and kidney-enriched inositol phosphatase) carboxyl homology] domains, that are important for protein-protein interactions and/or for the subcellular localization of these enzymes. 5-phosphatases incorporate into large signaling complexes, and regulate diverse cellular processes including postsynaptic vesicular trafficking, insulin signaling, cell growth and survival, and endocytosis. Loss or gain of function of 5-phosphatases is implicated in certain human diseases. This family also contains a functionally unrelated nitric oxide transport protein, Cimex lectularius (bedbug) nitrophorin, which catalyzes a heme-assisted S-nitrosation of a proximal thiolate; the heme however binds at a site distinct from the active site of the 5-phosphatases
VKIFVVTWNVGGGISPPENLENWLSPKGTEAPDIYAVGVQEVDMSVQGFVGNDDSAKAREWVDNIQEALN
EKENYVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVEGVTVGTGGGGKLGNKGGVAIRFQINDTSFCFVNS
HLAAGQEEVERRNQDYRDILSKLKFYRGDPAIDSIFDHDVVFWFGDLNYRIDSTDDEVRKLISQGDLDDL
LEKDQLKKQKEKGKVFDGFQELPITFPPTYKFDPGTDEYDTSDKKRIPAWCDRILYKSKAGSEIQPLSYT
SVPLYKTSDHKPVRATFRV
>gnl|CDD|197309 cd09075, DNase1-like, Deoxyribonuclease 1 and related proteins. This family includes Deoxyribonuclease 1 (DNase1, EC 3.1.21.1) and related proteins. DNase1, also known as DNase I, is a Ca2+, Mg2+/Mn2+-dependent secretory endonuclease, first isolated from bovine pancreas extracts. It cleaves DNA preferentially at phosphodiester linkages next to a pyrimidine nucleotide, producing 5'-phosphate terminated polynucleotides with a free hydroxyl group on position 3'. It generally produces tetranucleotides. DNase1 substrates include single-stranded DNA, double-stranded DNA, and chromatin. This enzyme may be responsible for apoptotic DNA fragmentation. Other deoxyribonucleases in this subfamily include human DNL1L (human DNase I lysosomal-like, also known as DNASE1L1, Xib and DNase X), human DNASE1L2 (also known as DNAS1L2), and DNASE1L3 (also known as DNAS1L3, nhDNase, LS-DNase, DNase Y, and DNase gamma). DNASE1L3 is also implicated in apoptotic DNA fragmentation. DNase1 is also a cytoskeletal protein which binds actin. A recombinant form of human DNase1 is used as a mucoactive therapy in patients with cystic fibrosis; it hydrolyzes the extracellular DNA in sputum and reduces its viscosity. Mutations in the gene encoding DNase1 have been associated with Systemic Lupus Erythematosus, a multifactorial autoimmune disease. This family also includes a subfamily of mostly uncharacterized proteins, which includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease. The in vivo role of MnuA is as yet undetermined. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds
KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPL
GRNSYKERYLFLFRPNKVSVLDTYQYDDGCKSCGNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAV
AEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAY
DRIVVAGSLLQSSVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTL
>gnl|CDD|197310 cd09076, L1-EN, Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains. This family contains the endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains, including the endonuclease of Xenopus laevis Tx1. These retrotranspons belong to the subtype 2, L1-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. LINE-1/L1 elements (full length and truncated) comprise about 17% of the human genome. This endonuclease nicks the genomic DNA at the consensus target sequence 5'TTTT-AA3' producing a ribose 3'-hydroxyl end as a primer for reverse transcription of associated template RNA. This subgroup also includes the endonuclease of Xenopus laevis Tx1, another member of the L1-clade. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds
IGTLNVRGLRSPGKRAQLLEELKRKKLDILGLQETHWTGEGELKKKREGGTILYSGSDSGKSRGVAILLS
KTAANKLLEYTKVVSGRIIMVRFKIKGKRLTIINVYAPTARDEEEKEEFYDQLQDVLDKVPRHDTLIIGG
DFNAVLGPKDDGRKGLDKRNENGERALSALIEEHDLVDVWRENNPKTREYTWRSPDHGSRSRIDRILVSK
RLRVKVKKTKITPGAGSDHRLVTLKL
>gnl|CDD|197311 cd09077, R1-I-EN, Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat retrotransposons. This family contains the endonuclease (EN) domain of various non-long terminal repeat (non-LTR) retrotransposons, long interspersed nuclear elements (LINEs) which belong to the subtype 2, R1- and I-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. Most non-LTR retrotransposons are inserted throughout the host genome; however, many retrotransposons of the R1 clade exhibit target-specific retrotransposition. This family includes the endonucleases of SART1 and R1bm, from the silkworm Bombyx mori, which belong to the R1-clade. It also includes the endonuclease of snail (Biomphalaria glabrata) Nimbus/Bgl and mosquito Aedes aegypti (MosquI), both which belong to the I-clade. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds
LRILQINLNRCKAAQDLLLQTAREEGADIALIQEPYLVPVNNPNWVTDESGRAAIVVSDRLPRKPIQRLS
LGLGIVAARVGGITVVSCYAPPSESLEEFEEYLENLVRIVRGLSRPVIIGGDFNAWSPAWGSKRTDRRGR
LLEDWIANLGLVLLNDGNSPTFVRPRGTSIIDVTFCSPSLARRISNWRVLEDETLSDHRYIRFTI
>gnl|CDD|197312 cd09078, nSMase, Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine. Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds
LKVLTYNVFLLPPLLYNNGDDGQDERLDLIPKALLQYDVVVLQEVFDARARKRLLNGLKKEYPYQTDVVG
RSPSGWSSKLVDGGVVILSRYPIVEKDQYIFPNGCGADCLAAKGVLYAKINKGGTKVYHVFGTHLQASDG
SCLDRAVRQKQLDELRAFIEEKNIPDNEPVIIAGDFNVDKRSSRDEYDDMLEQLHDYNAPEPITAGETPL
TWDPGTNLLAKYNYPGGGGERLDYILYSNDHLQPSSWSNEVEVPKSPTWSVTNGYTFADLSDHYPVSATF
>gnl|CDD|197313 cd09079, RgfB-like, Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, and related proteins. This family includes Streptococcus agalactiae RgfB (for regulator of fibrinogen binding) and related proteins. The function of RgfB is unknown. It is part of a putative two component signal transduction system designated rgfBDAC (the rgf locus was identified in a screen for mutants of Streptococcus agalactiae with altered binding to fibrinogen). RgfA,-C,and -D do not belong to this superfamily: rgfA encodes a putative response regulator, and rgfC, a putative histidine kinase. All four genes are co-transcribed, and may be involved in regulating expression of bacterial cell surface components. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds
LLTLNTHSWLEENQKEKLERLAKIIAEEDYDVIALQEVNQSIDAPVSQVPIKEDNFALLLYEKLRELGAT
YYWTWILSHIGYDKYDEGLAILSKRPIAEVEDFYVSKSQDYTDYKSRKILGATIEINGQPIDVYSCHLGW
WYDEEEPFAYEWSKLEKALAEAGRPVLLMGDFNNPAGSRGEGYDLISSLGLQDTYDLAEEKDGGVTVEKA
IDGWRGNKEAKRIDYIFVNRKVKVKSSRVIFNGKNPPIVSDHFGVEVEL
>gnl|CDD|197314 cd09080, TDP2, Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains. Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds
LKVLTWNVDFLDDVNLAERMRAILKLLEELDPDVIFLQEVTPPFLAYLLSQPWVRKNYYFSEGPPSPAVD
PYGVLILSKKSLVVRRVPFTSTRMGRNLLAAEINLGSGEPLRLATTHLESLKSHSSERTAQLEEIAKKLK
KPPGAANVILGGDFNLRDKEDDTGGLPNGFVDAWEELGPPGEPGYTWDTQKNPMLRKGEAGPRKRFDRVL
LRGSDLKPKSIELIGTEPIPGDEEGLFPSDHFGLLAEL
>gnl|CDD|197315 cd09081, CdtB, CdtB, the catalytic DNase I-like subunit of cytolethal distending toxin (CDT) protein. CDT is a secreted protein toxin produced by a number of Gram-negative disease-causing bacteria. CDT causes cell cycle arrest and eventual cell death in eukaryotic cells, as a result of chromosomal DNA damage caused by the catalytic, DNase I-like, CdtB subunit. Bacterial CDTs are generally comprised of three subunits, CdtA, -B and -C. CdtB is translocated into the host cell, where it acts as a genotoxin. CdtA and CdtC are needed for cell surface binding and cellular entry, and it is likely that they remain associated with the membrane, when CdtB is internalized. CdtB enters the target nucleus via nuclear translocation signal domain(s). This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds
VATWNLQGASASTESKWNTNVRQMLRGNNADILMIQEAGALPASARRTGRPAISNLDQIFGVGIPVEEYT
WNLGTSSRPENVYIYYYDRDVGANRVNLAIVSRQRADEVFILSPTVATSTSRPILGIRIGNDVFFTIHAL
ANGGNDAPALVNIIDNFFANNRPNATWVIMGDFNRSPDELEPSLRQPPAVTPNINIVSPNEATHPSGNTL
DYAVAGGSNARSRIAASLIGALLRQLSSDHNPVSFTP
>gnl|CDD|197316 cd09082, Deadenylase, C-terminal deadenylase domain of CCR4, nocturnin, and related domains. This family contains the C-terminal catalytic domains of the deadenylases, CCR4 and nocturnin, and related domains. Nocturnin is a poly(A)-specific 3' exonuclease that specifically degrades the 3' poly(A) tail of RNA in a process known as deadenylation. This nuclease activity is manganese dependent. Nocturnin is expressed in the cytoplasm of the Xenopus laevis retinal photoreceptor cells in a rhythmic fashion, and it has been proposed that it participates in posttranscriptional regulation of the circadian clock or its outputs, and that the mRNA target(s) of this deadenylase are circadian clock-related. Saccharomyces cerevisiae CCR4p is a 3'-5' poly(A) RNA and ssDNA exonuclease. It is the catalytic subunit of the yeast mRNA deadenylase (Ccr4p/Pop2p/Not complex). This complex participates in various ways in mRNA metabolism, including transcription initiation and elongation, and mRNA degradation. The deadenylase activities of Ccr4p and nocturnin differ: nocturnin degrades poly(A), Ccr4p degrades both poly(A) and single-stranded DNA, and in contrast to Ccr4p, nocturnin appears to function in a highly processive manner. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds
VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYD
GFFSPKSRAKIMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAV
VLEVHKELFGAGMKPIHAADKQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADP
NSIPLVLCADLNSLPDSGVVEYLSNGGVADNHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAY
ENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQWLVENNITGCPHPHIPSDHFSLLTQLEL
>gnl|CDD|197317 cd09083, EEP-1, Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1. This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds. Their substrates range from nucleic acids to phospholipids and perhaps, proteins
RVMTFNIRYDNPSDGENSWENRKDLVAELIKFYDPDIIGTQEALPHQLADLEELLPEYDWIGVGRDDGKE
KGEFSAIFYRKDRFELLDSGTFWLSETPDVVGSKGWDAALPRICTWARFKDKKTGKEFYVFNTHLDHVGE
EAREESAKLILERIKEIAGDLPVILTGDFNAEPDSEPYKTLTSGGLKDARDTAATTDGGPEGTFHGFKGP
PGGSRIDYIFVSPGVKVLSYEILTDRYDGRYPSDHFPVVADL
>gnl|CDD|197318 cd09084, EEP-2, Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2. This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps, proteins
VMSYNVRSFNRYKWKDDPDKILDFIKKQDPDILCLQEYYGSEGDKDDDLRLLLKGYPYYYVVYKSDSGGT
GLAIFSKYPILNSGSIDFPNTNNNAIFADIRVGGDTIRVYNVHLESFRITPSDKELYKEEKKAKELSRNL
LRKLAEAFKRRAAQADLLAADIAASPYPVIVCGDFNDTPASYVYRTLKKGLTDAFVEAGSGFGYTFNGLF
FPLRIDYILTSKGFKVLRYRVDPGKYSDHYPIVATL
>gnl|CDD|197319 cd09085, Mth212-like_AP-endo, Methanothermobacter thermautotrophicus Mth212-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases. This subfamily includes the thermophilic archaeon Methanothermobacter thermautotrophicus Mth212and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Mth212 is an AP endonuclease, and a DNA uridine endonuclease (U-endo) that nicks double-stranded DNA at the 5'-side of a 2'-d-uridine residue. After incision at the 5'-side of a 2'-d-uridine residue by Mth212, DNA polymerase B takes over the 3'-OH terminus and carries out repair synthesis, generating a 5'-flap structure that is resolved by a 5'-flap endonuclease. Finally, DNA ligase seals the resulting nick. This U-endo activity shares the same catalytic center as its AP-endo activity, and is absent from other AP endonuclease homologues
MKIISWNVNGLRAVHKKGFLDWFKEEKPDILCLQETKAQPEQLPEDLRNIEGYHSYFNSAERKGYSGVAL
YSKIEPDSVREGLGVEEFDNEGRILIADFDDFTLFNIYFPNGQMSEERLDYKLEFYDAFLEYLNELRDSG
KNVIICGDFNTAHKEIDLARPKENEKVSGFLPEERAWMDKFIENGYVDTFRMFNKEPGQYTWWSYRTRAR
ERNVGWRIDYFFVNEEFKPKVKDAGILPDVMGSDHCPVSLEL
>gnl|CDD|197320 cd09086, ExoIII-like_AP-endo, Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases. This subfamily includes Escherichia coli ExoIII, Neisseria meningitides NExo,and related proteins. These are ExoIII family AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiencies. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity. For example, Neisseria meningitides Nape and NExo, and exonuclease III (ExoIII) and endonuclease IV (EndoIV) in Escherichia coli. NExo and ExoIII are found in this subfamily. NExo is the non-dominant AP endonuclease. It exhibits strong 3'-5' exonuclease and 3'-deoxyribose phosphodiesterase activities. Escherichia coli ExoIII is an active AP endonuclease, and in addition, it exhibits double strand (ds)-specific 3'-5' exonuclease, exonucleolytic RNase H, 3'-phosphomonoesterase and 3'-phosphodiesterase activities, all catalyzed by a single active site. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes ExoIII and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily
MKIATWNVNSIRARLEQVLDWLKEEDPDVLCLQETKVEDDQFPADAFEALGYHVAVHGQKAYNGVAILSR
LPLEDVRTGFPGDPDDDQARLIAARVGGVRVINLYVPNGGDIGSPKFAYKLDWLDRLIRYLQKLLKPDDP
LVLVGDFNIAPEDIDVWDPKQLLGKVLFTPEEREALRALLDLGFVDAFRALHPDEKLFTWWDYRAGAFER
NRGLRIDHILASPALADRLKDVGIDREPRGWEKPSDHAPVVAEL
>gnl|CDD|197321 cd09087, Ape1-like_AP-endo, Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases. This subfamily includes human Ape1 (also known as Apex, Hap1, or Ref-1) and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Ape1 and Ape2 in humans. Ape1 is found in this subfamily, it exhibits strong AP-endonuclease activity but shows weak 3'-5' exonuclease and 3'-phosphodiesterase activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes exonuclease III (ExoIII) and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily
LKIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKELKELLKGYHQYWNAAEKKGYSGTA
ILSKKKPLSVTYGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSK
KPVIWCGDLNVAHEEIDLANPKTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNA
RAKNVGWRLDYFLVSERLKDRVVDSFIRSDIMGSDHCPIGLEL
>gnl|CDD|197322 cd09088, Ape2-like_AP-endo, Human Ape2-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases. This subfamily includes human APE2, Saccharomyces cerevisiae Apn2/Eth1, and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity. For examples, Ape1 and Ape2 in humans, and Apn1 and Apn2 in bakers yeast. Ape2 and Apn2/Eth1 are both found in this subfamily, and have the weaker AP endonuclease activity. Ape2 shows strong 3'-5' exonuclease and 3'-phosphodiesterase activities; it can reduce the mutagenic consequences of attack by reactive oxygen species by removing 3'-end adenine opposite from 8-oxoG, in addition to repairing 3'-damaged termini. Apn2/Eth1 exhibits AP endonuclease activity, but has 30-40 fold more active 3'-phosphodiesterase and 3'-5' exonuclease activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes exonuclease III (ExoIII) and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily
RIVTWNVNGIRTRLQYQPWNKENSLKSFLDSLDADIICLQETKLTRDELDEPSAIVEGYDSFFSFSRGRK
GYSGVATYCRDSAATPVAAEEGLTGVLSSPNQKNELSENDDIGCYGEMLEFTDSKELLELDSEGRCVLTD
HGTFVLINVYCPRADPEKEERLEFKLDFYRLLEERVEALLKAGRRVILVGDVNVSHRPIDHCDPDDSEDF
GGESFEDNPSRQWLDQLLGDSGEGGGSPGGLLIDSFRYFHPTRKGAYTCWNTLTGARPTNYGTRIDYILA
DRGLLPWVKAADILPEVEGSDHCPVYADL
>gnl|CDD|197323 cd09089, INPP5c_Synj, Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins. This subfamily contains the INPP5c domains of two human synaptojanins, synaptojanin 1 (Synj1) and synaptojanin 2 (Synj2), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs). They belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj1 occurs as two main isoforms: a brain enriched 145 KDa protein (Synj1-145) and a ubiquitously expressed 170KDa protein (Synj1-170). Synj1-145 participates in clathrin-mediated endocytosis. The primary substrate of the Synj1-145 INPP5c domain is PI(4,5)P2, which it converts to PI4P. Synj1-145 may work with membrane curvature sensors/generators (such as endophilin) to remove PI(4,5)P2 from curved membranes. The recruitment of the INPP5c domain of Synj1-145 to endophilin-induced membranes leads to a fragmentation and condensation of these structures. The PI(4,5)P2 to PI4P conversion may cooperate with dynamin to produce membrane fission. In addition to this INPP5c domain, Synjs contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro. Synj2 can hydrolyze phosphatidylinositol diphosphate (PIP2) to phosphatidylinositol phosphate (PIP). Synj2 occurs as multiple alternative splice variants in various tissues. These variants share the INPP5c domain and the Sac1 domain. Synj2A is recruited to the mitochondria via its interaction with OMP25 (a mitochondrial outer membrane protein). Synj2B is found at nerve terminals in the brain and at the spermatid manchette in testis. Synj2B undergoes further alternative splicing to give 2B1 and 2B2. In clathrin-mediated endocytosis, Synj2 participates in the formation of clathrin-coated pits, and perhaps also in vesicle decoating. Rac1 GTPase regulates the intracellular localization of Synj2 forms, but not Synj1. Synj2 may contribute to the role of Rac1 in cell migration and invasion, and is a potential target for therapeutic intervention in malignant tumors
LRVFVGTWNVNGGKHFRSIAFKHQSMTDWLLDNPKLAGQCSNDSEEDEKPVDIFAIGFEEMVDLNASNIV
SASTTNQKEWGEELQKTISRDHKYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGA
VAIRFLLHSTSLCFVCSHFAAGQSQVKERNEDFAEIARKLSFPMGRTLDSHDYVFWCGDFNYRIDLPNDE
VKELVRNGDWLKLLEFDQLTKQKAAGNVFKGFLEGEINFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWR
RRKWPSDKTEESLVETNDPTWNPGTLLYYGRAELKTSDHRPVVAIIDI
>gnl|CDD|197324 cd09090, INPP5c_ScInp51p-like, Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae Inp51p, Inp52p, and Inp53p, and related proteins. This subfamily contains the INPP5c domain of three Saccharomyces cerevisiae synaptojanin-like inositol polyphosphate 5-phosphatases (INP51, INP52, and INP53), Schizosaccharomyces pombe synaptojanin (SPsynaptojanin), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. In addition to this INPP5c domain, these proteins have an N-terminal catalytic Sac1-like domain (found in other proteins including the phophoinositide phosphatase Sac1p), and a C-terminal proline-rich domain (PRD). The Sac1 domain allows Inp52p and Inp53p to recognize and dephosphorylate a wider range of substrates including PI3P, PI4P, and PI(3,5)P2. The Sac1 domain of Inp51p is non-functional. Disruption of any two of INP51, INP52, and INP53, in S. cerevisiae leads to abnormal vacuolar and plasma membrane morphology. During hyperosmotic stress, Inp52p and Inp53p localize at actin patches, where they may facilitate the hydrolysis of PI(4,5)P2, and consequently promote actin rearrangement to regulate cell growth. SPsynaptojanin is also active against a range of soluble and lipid inositol phosphates, including I(1,4,5)P3, I(1,3,4,5)P4, I(1,4,5,6)P4, PI(4,5)P2, and PIP3. Transformation of S. cerevisiae with a plasmid expressing the SPsynaptojanin 5-phosphatase domain rescues inp51/inp52/inp53 triple-mutant strains
INIFVGTFNVNGKSYKDDLSSWLFPEENDELPDIVVIGLQEVVELTAGQILNSDPSKSSFWEKKIKTTLN
GRGGEKYVLLRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTS
HLAAGLTNYEERNNDYKTIARGLRFSRGRTIKDHDHVIWLGDFNYRISLTNEDVRRFILNGKLDKLLEYD
QLNQQMNAGEVFPGFSEGPITFPPTYKYDKGTDNYDTSEKQRIPAWTDRILYRGENLRQLSYNSAPLRFS
DHRPVYATFEA
>gnl|CDD|197325 cd09091, INPP5c_SHIP, Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol polyphosphate 5-phosphatase-1 and -2, and related proteins. This subfamily contains the INPP5c domain of SHIP1 (SH2 domain containing inositol polyphosphate 5-phosphatase-1, also known as SHIP/INPP5D), and SHIP2 (also known as INPPL1). It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Both SHIP1 and -2 catalyze the dephosphorylation of the PI, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3], to phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2]. SHIP1 also converts inositol-1,3,4,5- polyphosphate [I(1,3,4,5)P4] to inositol-1,3,4-polyphosphate [I(1,3,4)P3]. SHIP1 and SHIP2 have little overlap in their in vivo functions. SHIP1 is a negative regulator of cell growth and plays a major part in mediating the inhibitory signaling in B cells; it is predominantly expressed in hematopoietic cells. SHIP2 is as an inhibitor of the insulin signaling pathway, and is implicated in actin structure remodeling, cell adhesion and cell spreading, receptor endocytosis and degradation, and in the JIP1-mediated JNK pathway. SHIP2 is widely expressed, most prominently in brain, heart and in skeletal muscle. In addition to this INPP5c domain, SHIP1 has an N-terminal SH2 domain, two NPXY motifs, and a C-terminal proline-rich region (PRD), while SHIP2 has an N-terminal SH2 domain, a C-terminal proline-rich domain (PRD), which includes a WW-domain binding motif (PPLP), an NPXY motif, and a sterile alpha motif (SAM) domain. The gene encoding SHIP2 is a candidate gene for conferring a predisposition for type 2 diabetes
ISIFIGTWNMGSAPPPKNITSWFTSKGQGKTRDDVADYIPHDIYVIGTQEDPLGEKEWLDLLRHSLKELT
SLDYKPIAMQTLWNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLT
SGSEKKLRRNQNYLNILRFLSLGDKKLSAFNITHRFTHLFWLGDLNYRLDLPIQEAENIIQKIEQQQFEP
LLRHDQLNLEREEHKVFLRFSEEEITFPPTYRYERGSRDTYAYTKQKATGVKYNLPSWCDRILWKSYPET
HIICQSYGCTDDIVTSDHSPVFGTFEV
>gnl|CDD|197326 cd09092, INPP5A, Type I inositol polyphosphate 5-phosphatase I. Type I inositol polyphosphate 5-phosphatase I (INPP5A) hydrolyzes the 5-phosphate from inositol 1,3,4,5-tetrakisphosphate [I(1,3,4,5)P4] and inositol 1,4,5-trisphosphate [I(1,4,5)P3]. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. As the substrates of INPP5A mobilize intracellular calcium ions, INPP5A is a calcium signal-terminating enzyme. In platelets, phosphorylated pleckstrin binds and activates INPP5A in a 1:1 complex, and accelerates the degradation of the calcium ion-mobilizing I(1,4,5)P3
VDVLLVTANVGSLFEDPENLEKNWLREFLQTVHAHKPSFVALHLQEVGGKNYEASMEHVEKFIRELLSSD
AMKDFDRVRVYVDEDFKSAEHFTALGSLYFIHKSLKNIYQFDFHAKKYKKVTGKEIYSGTLESVPTVEKE
KFPQDFFPECKWSRKGFMRTRWKINNCVFDLVNIHLFHDASNLAACESSPSVYSQNRHRALGYVLERLTD
ERFEKVPFFVFGDFNFRLDTKSVVETLCAKATMQTVRKADSNIVVKLEFREKDNDNKVVLQIEKKKFDYF
NQDVFRDNNGKALLKFDKELEVFKDVLYELDISFPPSYPYSEDPEQGTQYMNTRCPAWCDRILMSHSARE
LKSENEEKSVTYDMIGPNVCMGDHKPVFLTFRI
>gnl|CDD|197327 cd09093, INPP5c_INPP5B, Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol polyphosphate 5-phosphatase I, Oculocerebrorenal syndrome of Lowe 1, and related proteins. This subfamily contains the INPP5c domain of type II inositol polyphosphate 5-phosphatase I (INPP5B), Oculocerebrorenal syndrome of Lowe 1 (OCRL-1), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5B and OCRL1 preferentially hydrolyze the 5-phosphate of phosphatidylinositol (4,5)- bisphosphate [PI(4,5)P2] and phosphatidylinositol (3,4,5)- trisphosphate [PI(3,4,5)P3]. INPP5B can also hydrolyze soluble inositol (1,4,5)-trisphosphate [I(1,4,5)P3] and inositol (1,3,4,5)-tetrakisphosphate [I(1,3,4,5)P4]. INPP5B participates in the endocytic pathway and in the early secretory pathway. In the latter, it may function in retrograde ERGIC (ER-to-Golgi intermediate compartment)-to-ER transport; it binds specific RAB proteins within the secretory pathway. In the endocytic pathway, it binds RAB5 and during endocytosis, may function in a RAB5-controlled cascade for converting PI(3,4,5)P3 to phosphatidylinositol 3-phosphate (PI3P). This cascade may link growth factor signaling and membrane dynamics. Mutation in OCRL1 is implicated in Lowe syndrome, an X-linked recessive multisystem disorder, which includes defects in eye, brain, and kidney function, and in Type 2 Dent's disease, a disorder with only the renal symptoms. OCRL-1 may have a role in membrane trafficking within the endocytic pathway and at the trans-Golgi network, and may participate in actin dynamics or signaling from endomembranes. OCRL1 and INPP5B have overlapping functions: deletion of both 5-phosphatases in mice is embryonic lethal, deletion of OCRL1 alone has no phenotype, and deletion of Inpp5b alone has only a mild phenotype (male sterility). Several of the proteins that interact with OCRL1 also bind INPP5B, for examples, inositol polyphosphate phosphatase interacting protein of 27kDa (IPIP27)A and B (also known as Ses1 and 2), and endocytic signaling adaptor APPL1. OCRL1, but not INPP5B, binds clathrin heavy chain, the plasma membrane AP2 adaptor subunit alpha-adaptin. In addition to this INPP5c domain, most proteins in this subfamily have a C-terminal RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain
FRIFVGTWNVNGQSPDESLRPWLSCDEEPPDIYAIGFQELDLSAEAFLFNDSSREQEWVKAVERGLHPDA
KYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAAH
MEEVERRNQDYKDICARMKFEDPDGPPLSISDHDVVFWLGDLNYRIQELPTEEVKELIEKNDLEELLKYD
QLNIQRRAGKVFEGFTEGEINFIPTYKYDPGTDNWDSSEKCRAPAWCDRILWRGTNIVQLSYRSHMELKT
SDHKPVSALFDI
>gnl|CDD|197328 cd09094, INPP5c_INPP5J-like, Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate 5-phosphatase J and related proteins. INPP5c domain of Inositol polyphosphate-5-phosphatase J (INPP5J), also known as PIB5PA or PIPP, and related proteins. This subfamily belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5J hydrolyzes PI(4,5)P2, I(1,4,5)P3, and I(1,3,4,5)P4 at ruffling membranes. These proteins contain a C-terminal, SKIP carboxyl homology domain (SKICH), which may direct plasma membrane ruffle localization
LRVYVVTWNVATAPPPIDVRSLLGLQSPEVAPDIYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPK
GYVKVSSIRLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAH
MEKWEQRIDDFETILSTQVFNECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQL
NMAKRKEEAFQGFQEGPLNFAPTYKFDLGTDEYDTSGKKRKPAWTDRILWKVNPDASTEEKFLSITQTSY
KSHMEYGISDHKPVTAQFRL
>gnl|CDD|197329 cd09095, INPP5c_INPP5E-like, Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol polyphosphate-5-phosphatase E and related proteins. INPP5c domain of Inositol polyphosphate-5-phosphatase E (also called type IV or 72 kDa 5-phosphatase), rat pharbin, and related proteins. This subfamily belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5E hydrolyzes the 5-phosphate from PI(3,5)P2, PI(4,5)P2 and PI(3,4,5)P3, forming PI3P, PI4P, and PI(3,4)P2, respectively. It is a very potent PI(3,4,5)P3 5-phosphatase. Its intracellular localization is chiefly cytosolic, with pronounced perinuclear/Golgi localization. INPP5E also has an N-terminal proline rich domain (PRD) and a C-terminal CAAX motif. This protein is expressed in a variety of tissues, including the breast, brain, testis, and haemopoietic cells. It is differentially expressed in several cancers, for example, it is up-regulated in cervical cancer and down-regulated in stomach cancer. It is a candidate target for therapeutics of obesity and related disorders, as it is expressed in the hypothalamus, and following insulin stimulation, it undergoes tyrosine phosphorylation, associates with insulin receptor substrate-1, -2, and PI3-kinase, and become active as a 5-phosphatase. INPP5E may play a role, along with other 5-phosphatases SHIP2 and SKIP, in regulating glucose homoeostasis and energy metabolism. Mice deficient in INPPE5 develop a multi-organ disorder associated with structural defects of the primary cilium
PDRNVGIFVATWNMQGQKELPENLDDFLLPTSADFAQDIYVIGVQEGCSDRREWEIRLQETLGPSHVLLH
SASHGVLHLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSGDGKVKE
RVLDYNKIIQALNLPRNVPTNPYKSESGDVTTRFDEVFWFGDFNFRLSGPRHLVDALINQGQEVDVSALL
QHDQLTREMSKGSIFKGFQEAPIHFPPTYKFDIGSDVYDTSSKQRVPSYTDRILYRSRQKGDVCCLKYNS
CPSIKTSDHRPVFALFRV
>gnl|CDD|197330 cd09096, Deadenylase_nocturnin, C-terminal deadenylase domain of nocturnin and related domains. This subfamily contains the C-terminal catalytic domain of the deadenylase, nocturnin, and related domains. Nocturnin is a poly(A)-specific 3' exonuclease that specifically degrades the 3' poly(A) tail of RNA in a process known as deadenylation. This nuclease activity is manganese dependent. Nocturnin is expressed in the cytoplasm of Xenopus laevis retinal photoreceptor cells in a rhythmic fashion, and it has been proposed that it participates in posttranscriptional regulation of the circadian clock or its outputs, and that the mRNA target(s) of this deadenylase are circadian clock-related. In mouse, the nocturnin gene, mNoc, is expressed in a circadian pattern in a range of tissues including retina, spleen, heart, kidney, and liver. It is highly expressed in bone-marrow stromal cells, adipocytes and hepatocytes. In mammals, nocturnin plays a role in regulating mesenchymal stem-cell lineage allocation, perhaps through regulating PPAR-gamma (peroxisome proliferator-activated receptor-gamma) nuclear translocation. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds
RVMQWNILAQALGEGKDGFVRCPCEALKWEERKYLILEEILTYDPDILCLQEVDHYKDTLQPLLSRLGYQ
GTFFPKPDSPCLYIENNNGPDGCALFFRKDRFELVNTEKIRLSAMTLKTNQVAIACTLRCKETGREICLA
VTHLKARTGWERLRSEQGKDLLQNLQSFIEGAKIPLIICGDFNAEPTEPVYKTFSNSSLNLNSAYKLLSA
DGQSEPPYTTWKIRTSGECRHTLDYIFYSKDALSVEQLLDLPTEEQIGPNRLPSFNYPSDHLSLVCDFSL
>gnl|CDD|197331 cd09097, Deadenylase_CCR4, C-terminal deadenylase domain of CCR4 and related domains. This subfamily contains the C-terminal catalytic domain of the deadenylases, Saccharomyces cerevisiae Ccr4p and two vertebrate homologs (CCR4a and CCR4b), and related domains. CCR4 belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. CCR4 is the major deadenylase subunit of the CCR4-NOT transcription complex, which contains two deadenylase subunits and several noncatalytic subunits. The other deadenylase subunit, Caf1 (called Pop2 in yeast), is a DEDD-type protein and does not belong in this superfamily. Saccharomyces cerevisiae CCR4 (or Ccr4p) is a 3'-5' poly(A) RNA and ssDNA exonuclease. It is the catalytic subunit of the yeast mRNA deadenylase (Ccr4p/Pop2p/Not complex). This complex participates in various ways in mRNA metabolism, including transcription initiation and elongation, and mRNA degradation. Ccr4p degrades both poly(A) and single-stranded DNA. There are two vertebrate homologs of Ccr4p, CCR4a (also called CCR4-NOT transcription complex subunit 6 or CNOT6) and CCR4b (also called CNOT6-like or CNOT6L), which independently associate with other components to form distinct CCR4-NOT multisubunit complexes. The nuclease domain of CNOT6 and CNOT6L exhibits Mg2+-dependent deadenylase activity, with specificity for poly (A) RNA as substrate. CCR4a is a component of P-bodies and is necessary for foci formation. CCR4b regulates p27/Kip1 mRNA levels, thereby influencing cell cycle progression. They both contribute to the prevention of cell death by regulating insulin-like growth factor-binding protein 5
VMCYNVLCDKYATRQQYGYCPSWALNWDYRKQNILKEILSYNADILCLQEVETDQYEDFFLPELKQHGYD
GVFKPKSRAKTMSEAERKHVDGCAIFFKTSKFKLVEKHLIEFNQLAMANADAEGSEDMLNRVMTKDNIAL
IVVLEARETSYEGNKGQLLIVANTHIHWDPEFSDVKLVQTMMLLEELEKIAEKFSRYPYEDSADIPLVVC
GDFNSLPDSGVYELLSNGSVSPNHPDFKEDPYGEYLTASGLTHSFKLKSAYANLGELPFTNYTPDFKGVI
DYIFYSADTLSVLGLLGPPDEDWYLNKVVGLPNPHFPSDHIALLAEFRI
>gnl|CDD|197332 cd09098, INPP5c_Synj1, Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1. This subfamily contains the INPP5c domains of human synaptojanin 1 (Synj1) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj1 occurs as two main isoforms: a brain enriched 145 KDa protein (Synj1-145) and a ubiquitously expressed 170KDa protein (Synj1-170). Synj1-145 participates in clathrin-mediated endocytosis. The primary substrate of the Synj1-145 INPP5c domain is PI(4,5)P2, which it converts to PI4P. Synj1-145 may work with membrane curvature sensors/generators (such as endophilin) to remove PI(4,5)P2 from curved membranes. The recruitment of the INPP5c domain of Synj1-145 to endophilin-induced membranes leads to a fragmentation and condensation of these structures. The PI(4,5)P2 to PI4P conversion may cooperate with dynamin to produce membrane fission. In addition to this INPP5c domain, these proteins contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro
IRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKKAGIPEFQDVRSKPVDIFAIGFEEMVELNAGNIVS
ASTTNQKLWAAELQKTISRDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAV
AIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDIPNEEV
KELIRQQNWDSLIAGDQLINQKNAGQVFRGFLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRR
RKWPFDRSAEDLDLLNASFPDNSKEQYTWSPGTLLHYGRAELKTSDHRPVVALIDI
>gnl|CDD|197333 cd09099, INPP5c_Synj2, Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2. This subfamily contains the INPP5c domains of human synaptojanin 2 (Synj2) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj2 can hydrolyze phosphatidylinositol diphosphate (PIP2) to phosphatidylinositol phosphate (PIP). In addition to this INPP5c domain, these proteins contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro. Synj2 occurs as multiple alternative splice variants in various tissues. These variants share the INPP5c domain and the Sac1 domain. Synj2A is recruited to the mitochondria via its interaction with OMP25, a mitochondrial outer membrane protein. Synj2B is found at nerve terminals in the brain and at the spermatid manchette in testis. Synj2B undergoes further alternative splicing to give 2B1 and 2B2. In clathrin-mediated endocytosis, Synj2 participates in the formation of clathrin-coated pits, and perhaps also in vesicle decoating. Rac1 GTPase regulates the intracellular localization of Synj2 forms, but not Synj1. Synj2 may contribute to the role of Rac1 in cell migration and invasion, and is a potential target for therapeutic intervention in malignant tumors
TRVAMGTWNVNGGKQFRSNILGTSELTDWLLDSPKLSGTPDFQDDESNPPDIFAVGFEEMVELSAGNIVN
ASTTNRKMWGEQLQKAISRSHRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAV
AIRFQFYSTSFCFICSHLTAGQNQVKERNEDYKEITQKLSFPMGRNVFSHDYVFWCGDFNYRIDLTYEEV
FYFIKRQDWKKLLEFDQLQLQKSSGKIFKDFHEGTINFGPTYKYDVGSEAYDTSDKCRTPAWTDRVLWWR
KKWPFEKTAGEINLLDSDLDFDTKIRHTWTPGALMYYGRAELQASDHRPVLAIVEV
>gnl|CDD|197334 cd09100, INPP5c_SHIP1-INPP5D, Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol polyphosphate 5-phosphatase-1 and related proteins. This subfamily contains the INPP5c domain of SHIP1 (SH2 domain containing inositol polyphosphate 5-phosphatase-1, also known as SHIP/INPP5D) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. SHIP1's enzymic activity is restricted to phosphatidylinositol 3,4,5-trisphosphate [PI (3,4,5)P3] and inositol-1,3,4,5- polyphosphate [I(1,3,4,5)P4]. It converts these two phosphoinositides to phosphatidylinositol 3,4-bisphosphate [PI (3,4)P2] and inositol-1,3,4-polyphosphate [I(1,3,4)P3], respectively. SHIP1 is a negative regulator of cell growth and plays a major part in mediating the inhibitory signaling in B cells; it is predominantly expressed in hematopoietic cells. In addition to this INPP5c domain, SHIP1 has an N-terminal SH2 domain, two NPXY motifs, and a C-terminal proline-rich region (PRD). SHIP1's phosphorylated NPXY motifs interact with proteins with phosphotyrosine binding (PTB) domains, and facilitate the translocation of SHIP1 to the plasma membrane to hydrolyze PI(3,4,5)P3. SHIP1 generally acts to oppose the activity of phosphatidylinositol 3-kinase (PI3K). It acts as a negative signaling molecule, reducing the levels of PI(3,4,5)P3, thereby removing the latter as a membrane-targeting signal for PH domain-containing effector molecules. SHIP1 may also, in certain contexts, amplify PI3K signals. SHIP1 and SHIP2 have little overlap in their in vivo functions
ITIFIGTWNMGNAPPPKKITSWFQCKGQGKTRDDTADYIPHDIYVIGTQEDPLGEKEWLDTLKHSLREIT
SISFKVIAIQTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLT
SGSEKKLRRNQNYFNILRFLVLGDKKLSPFNITHRFTHLFWLGDLNYRVELPNTEAENIIQKIKQQQYQE
LLPHDQLLIERKESKVFLQFEEEEITFAPTYRFERGTRERYAYTKQKATGMKYNLPSWCDRVLWKSYPLV
HVVCQSYGCTDDITTSDHSPVFATFEV
>gnl|CDD|197335 cd09101, INPP5c_SHIP2-INPPL1, Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol 5-phosphatase-2 and related proteins. This subfamily contains the INPP5c domain of SHIP2 (SH2 domain containing inositol 5-phosphatase-2, also called INPPL1) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. SHIP2 catalyzes the dephosphorylation of the PI, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3], to phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2]. SHIP2 is widely expressed, most prominently in brain, heart and in skeletal muscle. SHIP2 is an inhibitor of the insulin signaling pathway. It is implicated in actin structure remodeling, cell adhesion and cell spreading, receptor endocytosis and degradation, and in the JIP1-mediated JNK pathway. Its interacting partners include filamin/actin, p130Cas, Shc, Vinexin, Interesectin 1, and c-Jun NH2-terminal kinase (JNK)-interacting protein 1 (JIP1). A large variety of extracellular stimuli appear to lead to the tyrosine phosphorylation of SHIP2, including epidermal growth factor (EGF), platelet-derived growth factor (PDGF), insulin, macrophage colony-stimulating factor (M-CSF) and hepatocyte growth factor (HGF). SHIP2 is localized to the cytosol in quiescent cells; following growth factor stimulation and /or cell adhesion, it relocalizes to membrane ruffles. In addition to this INPP5c domain, SHIP2 has an N-terminal SH2 domain, a C-terminal proline-rich domain (PRD), which includes a WW-domain binding motif (PPLP), an NPXY motif and a sterile alpha motif (SAM) domain. The gene encoding SHIP2 is a candidate for conferring a predisposition for type 2 diabetes; it has been suggested that suppression of SHIP2 may be of benefit in the treatment of obesity and thereby prevent type 2 diabetes. SHIP2 and SHIP1 have little overlap in their in vivo functions
ISIFIGTWNMGSVPPPKSLASWLTSRGLGKTLDETTVTIPHDIYVFGTQENSVGDREWVDFLRASLKELT
DIDYQPIALQCLWNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLT
SGNEKTHRRNQNYLDILRSLSLGDKQLNAFDISLRFTHLFWFGDLNYRLDMDIQEILNYITRKEFDPLLA
VDQLNLEREKNKVFLRFREEEISFPPTYRYERGSRDTYMWQKQKTTGMRTNVPSWCDRILWKSYPETHIV
CNSYGCTDDIVTSDHSPVFGTFEV
>gnl|CDD|197201 cd09102, PLDc_CDP-OH_P_transf_II_1, Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members. Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members, which mainly include gram-negative bacterial phosphatidylserine synthases (PSS; CDP-diacylglycerol--serine O-phosphatidyltransferase, EC 2.7.8.8), yeast phosphatidylglycerophosphate synthase (PGP synthase; CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, EC 2.7.8.5), and metazoan PGP synthase 1. All members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterize the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism, involving a substrate-enzyme intermediate, to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involving phosphatidyl group transfer. Phosphatidylserine synthases from gram-positive bacteria and eukaryotes, and prokaryotic phosphatidylglycerophosphate synthases are not members of this subfamily
HIRFLGSPAEFKTQIIELIRNAKRRVYVASLYWGKDEAGQEILDEIYSVKQENPNLDVSVLIDWHRAQRN
LLGSETKSATNADWYCEQRQTSQLHLLPDDGNXFFGVPINTNEVFGVLHVKGYVFDDTVLLSGANLSNVY
FHYRYDRYVKITHGAELADSXVNLINAY
>gnl|CDD|197202 cd09103, PLDc_CDP-OH_P_transf_II_2, Catalytic domain, repeat 2, of CDP-alcohol phosphatidyltransferase class-II family members. Catalytic domain, repeat 2, of CDP-alcohol phosphatidyltransferase class-II family members, which mainly include gram-negative bacterial phosphatidylserine synthases (PSS; CDP-diacylglycerol--serine O-phosphatidyltransferase, EC 2.7.8.8), yeast phosphatidylglycerophosphate synthase (PGP synthase; CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, EC 2.7.8.5), and metazoan PGP synthase 1. All members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterize the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism, involving a substrate-enzyme intermediate, to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involving phosphatidyl group transfer. Phosphatidylserine synthases from gram-positive bacteria and eukaryotes, and prokaryotic phosphatidylglycerophosphate synthases are not members of this subfamily
LSITPLVGLGKRGNILNRTIEQLITSAESKIILCTPYFNLPQALMRDILRLLKRGVKVEIIVGDKTANDF
YIPPEEPFKVIGALPYLYEINLRRFAKRLQKYIDQGQLNVRLWKDGDNSFHLKGIWVDDRYTLLTGNNLN
PRAWRLDLENGLLIHDPQKQLQQQLEKELEQILLHTTRISHYTQ
>gnl|CDD|197203 cd09104, PLDc_vPLD1_2_like_1, Catalytic domain, repeat 1, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins. Catalytic domain, repeat 1, of phospholipase D (PLD, EC 3.1.4.4) found in yeast, plants, and vertebrates, and their bacterial homologs. PLDs are involved in signal transduction, vesicle formation, protein transport, and mitosis by participating in phospholipid metabolism. They hydrolyze the terminal phosphodiester bond of phospholipids resulting in the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Both prokaryotic and eukaryotic PLDs have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. PLDs are active as bi-lobed monomers. Each monomer contains two domains, each of which carries one copy of the HKD motif. Two HKD motifs from two domains form a single active site. PLDs utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
VEPLIDGEEYFDDLAEALDGARHSVYITGWQVSADIILAPLLAGPDRLGDTLRTLAARRGVDVRVLLWDS
PLLVLLGPDDKDLNLGFPTFLRLTTALLVLDLRLRRHTLFSHHQKLVVIDSAEVAFVGGIDLAYGRYDDP
DHALAAP
>gnl|CDD|197204 cd09105, PLDc_vPLD1_2_like_2, Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins. Catalytic domain, repeat 2, of phospholipase D (PLD, EC 3.1.4.4) found in yeast, plants, and vertebrates, and their bacterial homologs. PLDs are involved in signal transduction, vesicle formation, protein transport, and mitosis by participating in phospholipid metabolism. They hydrolyze the terminal phosphodiester bond of phospholipids resulting in the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Both prokaryotic and eukaryotic PLDs have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. PLDs are active as bi-lobed monomers. Each monomer contains two domains, each of which carries one copy of the HKD motif. Two HKD motifs from two domains form a single active site. PLDs utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
FAPSGEFEIADAYLKAIRNARRYIYIEDQYLWSPELLDALAEALKANPGLRVVLVLPALPDAVAFGADDG
LDALALLALLLLADAAPDRVAVFSLATHRRGLLGGPPIYVHSKVVIVDDEWATVGSANLNRRSMTWDTEL
NLAVVD
>gnl|CDD|197205 cd09106, PLDc_vPLD3_4_5_like_1, Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral envelope proteins K4 and p37, and similar proteins. Putative catalytic domain, repeat 1, of vertebrate phospholipases D, PLD3, PLD4, and PLD5 (EC 3.1.4.4), viral envelope proteins (vaccinia virus proteins K4 and p37), and similar proteins. Most family members contain two copies of the HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue), and have been classified into the phospholipase D (PLD) superfamily. Proteins in this subfamily are associated with Golgi membranes, altering their lipid content by the conversion of phospholipids into phosphatidic acid, which is thought to be involved in the regulation of lipid movement. ADP ribosylation factor (ARF), a small guanosine triphosphate binding protein, might be required activity. The vaccinia virus p37 protein, encoded by the F13L gene, is also associated with Golgi membranes and is required for the envelopment and spread of the extracellular enveloped virus (EEV). The vaccinia virus protein K4, encoded by the HindIII K4L gene, remains to be characterized. Sequence analysis indicates that the vaccinia virus proteins K4 and p37 might have evolved from one or more captured eukaryotic genes involved in cellular lipid metabolism. Up to date, no catalytic activity of PLD3 has been shown. Furthermore, due to the lack of functional important histidine and lysine residues in the HKD motif, mammalian PLD5 has been characterized as an inactive PLD. The poxvirus p37 proteins may also lack PLD enzymatic activity, since they contain only one partially conserved HKD motif (N-x-K-x(4)-D)
LVESIPEGLTFLSSSSHLSTFEAWMELISSAKKSIDIASFYWNLRGTDTNPDSSAQEGEDIFNALLEAAK
RGVKIRILQDKPSKDKPDEDDLELAALGGAEVRSLDFTKLIGGGVLHTKFWIVDGKHFYLGSANLDWRSL
TQVKELGVYIYNC
>gnl|CDD|197206 cd09107, PLDc_vPLD3_4_5_like_2, Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral envelope proteins K4 and p37, and similar proteins. Putative catalytic domain, repeat 2, of vertebrate phospholipases D, PLD3, PLD4, and PLD5 (EC 3.1.4.4), viral envelope proteins (vaccinia virus proteins K4 and p37), and similar proteins. Most family members contain two copies of the HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue), and have been classified into the phospholipase D (PLD) superfamily. Proteins in this subfamily are associated with Golgi membranes, altering their lipid content by the conversion of phospholipids into phosphatidic acid, which is thought to be involved in the regulation of lipid movement. ADP ribosylation factor (ARF), a small guanosine triphosphate binding protein, might be required activity. The vaccinia virus p37 protein, encoded by the F13L gene, is also associated with Golgi membranes and is required for the envelopment and spread of the extracellular enveloped virus (EEV). The vaccinia virus protein K4, encoded by the HindIII K4L gene, remains to be characterized. Sequence analysis indicates that the vaccinia virus proteins K4 and p37 might have evolved from one or more captured eukaryotic genes involved in cellular lipid metabolism. Up to date, no catalytic activity of PLD3 has been shown. Furthermore, due to the lack of functional important histidine and lysine residues in the HKD motif, mammalian PLD5 has been characterized as an inactive PLD. The poxvirus p37 proteins may also lack PLD enzymatic activity, since they contain only one partially conserved HKD motif (N-x-K-x(4)-D)
FLSSSPPELCPPGRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADPRKYWPVIDNALRRAAVDRGVKV
RLLVSNWKHTDPSMDAFLKSLQLLKSGVGNGDIEVKIFTVPGDQSTKIPFARVNHAKYMVTDERAYIGTS
NWSGDYFYNTAGVSLVINDPAIVQQLKDVFERDWN
>gnl|CDD|197207 cd09108, PLDc_PMFPLD_like_1, Catalytic domain, repeat 1, of phospholipase D from Streptomyces Sp. Strain PMF and similar proteins. Catalytic domain, repeat 1, of phospholipases D (PLD, EC 3.1.4.4) from Streptomyces Sp. Strain PMF (PMFPLD) and similar proteins, which are generally extracellular and bear N-terminal signal sequences. PMFPLD hydrolyzes the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. It also catalyzes a transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. In contrast to eukaryotic PLDs, PMFPLD has a compact structure, which consists of two catalytic domains, but lacks the regulatory domains. Each catalytic domain contains one copy of the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily. Two HKD motifs from two domains form a single active site. Like other PLD enzymes, PMFPLD may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group. A calcium-dependent PLD from Streptomyce chromofuscus is excluded from this family, since it displays very little sequence homology with other Streptomyces PLDs. Moreover, it does not contain the conserved HKD motif and hydrolyzes the phospholipids via a different mechanism
RDPSDELEGAVWELTDGNRLDCSCGNAFISLLQTPGPWGATACLIDGAGDDELLEKMADNIGSLPNARRI
VGITTLAPFPAFLAAAVAGLKRRVSAHESYGEGITVRILVGNFPRYHLGQVVSAVRDLLTAGLPLDDPAS
GWTLSVANMTYFLPWNHAKLLVVDGEELLTGGYNLWDDHYLDGGNPVHDLSLVVRGPAARSGVRFFDDLW
>gnl|CDD|197208 cd09109, PLDc_PMFPLD_like_2, Catalytic domain, repeat 2, of phospholipase D from Streptomyces Sp. Strain PMF and similar proteins. Catalytic domain, repeat 2, of phospholipases D (PLD, EC 3.1.4.4) from Streptomyces Sp. Strain PMF (PMFPLD) and similar proteins, which are generally extracellular and bear N-terminal signal sequences. PMFPLD hydrolyzes the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. It also catalyzes a transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. In contrast to eukaryotic PLDs, PMFPLD has a compact structure, which consists of two catalytic domains, but lacks the regulatory domains. Each catalytic domain contains one copy of the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily. Two HKD motifs from two domains form a single active site. Like other PLD enzymes, PMFPLD may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group. A calcium-dependent PLD from Streptomyce chromofuscus is excluded from this family, since it displays very little sequence homology with other Streptomyces PLDs. Moreover, it does not contain the conserved HKD motif and hydrolyzes the phospholipids via a different mechanism
VPVIAVGGLGVGINDDDRDYDTVNPEEFALRILIASAKIHIEISQQDLNATCPLPRYDIFTYNFIAVSLA
ASTGVKVRIVVSDPDNRGAVGSGGYVQIKSLTEIADTLSRRLAILTSVGNLSKDPGSDQMARRALCKNLQ
LAPPRSSGAGKWADGAPYALHAKLVIVDGKLFYIGSDNLYPSWLQEFGYIVEDPDAAKQLEDGYLDPLWK
YS
>gnl|CDD|197209 cd09110, PLDc_CLS_1, Catalytic domain, repeat 1, of bacterial cardiolipin synthase and similar proteins. Catalytic domain, repeat 1, of bacterial cardiolipin (CL) synthase and a few homologs found in eukaryotes and archaea. Bacterial CL synthases catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. The monomer of bacterial CL synthase consists of two catalytic domains. Each catalytic domain contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. Two HKD motifs from two domains form a single active site involved in phosphatidyl group transfer. Bacterial CL synthases can be stimulated by phosphate and inhibited by CL, the product of the reaction, and by phosphatidate. Phosphate stimulation may be unique to enzymes with CL synthase activity belonging to the PLD superfamily. Like other PLD enzymes, bacterial CL synthases utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
TDGEEFFPALLEAIRAARHSIHLEYYIFRDDEIGRRFRDALIEKARRGVEVRLLYDGFGSLGLSRRFLRE
LREAGVEVRAFNPLSFPLFLLRLNYRNHRKILVIDGKIAFVGGFNIGDEYLGKDPGFGPWRDTHVRIEGP
AVADLQAAFLEDWY
>gnl|CDD|197210 cd09111, PLDc_ymdC_like_1, Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and similar proteins. Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and similar proteins. In Escherichia coli, there are two genes, f413 (ybhO) and o493 (ymdC), which are homologous to gene cls that encodes the Escherichia coli cardiolipin (CL) synthase. The prototype of this subfamily is an uncharacterized protein ymdC specified by the o493 (ymdC) gene. Although the functional characterization of ymdC and similar proteins remains unknown, members of this subfamily show high sequence homology to bacterial CL synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Moreover, ymdC and its similar proteins contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characteriszes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
LEDGLDALAARLALIRSAERSIDLQYYIWHDDESGRLLLGELLEAADRGVRVRLLLDDLGTSGRDRLLAA
LDAHPNIEVRLFNPFRNRGGRLLEFLTDFSRLNRRMHNKLFIVDGAVAIVGGRNIGDEYFGASPEVNFRD
LDVLAVGPVVRQLSESFDTYWN
>gnl|CDD|197211 cd09112, PLDc_CLS_2, catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins. This CD corresponds to the catalytic domain repeat 2 of bacterial cardiolipin synthase (CL synthase, EC 2.7.8.-) and a few homologs found in eukaryotes and archea. Bacterial CL synthases catalyze reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form cardiolipin (CL) and glycerol. The monomer of bacterial CL synthase consists of two catalytic domains. Each catalytic domain contains one copy of conserved HKD motifs (H-X-K-X(4)-D, X represents any amino acid residue) that are the characteristic of the phospholipase D (PLD) superfamily. Two HKD motifs from two domains together form a single active site involving in phosphatidyl group transfer. Bacterial CL synthases can be stimulated by phosphate and inhibited by CL, the product of the reaction, and by phosphatidate. Phosphate stimulation may be unique to enzymes with CL synthase activity in PLD superfamily. Like other PLD enzymes, bacterial CL synthase utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid stabilizing the leaving group
VSSGPDSDWSSIEQAYLKAINSAKKSIYIQTPYFIPDESLLEALKTAALSGVDVRIMIPGKPDHKLVYWA
SRSYFEELLKAGVKIYEYNKGFLHSKTLIVDDEIASVGTANLDIRSFELNFEVNAVIYDKEVAKKLEEIF
EEDLKDSELLTLEEWRKRSLWKRFKESLARLLSP
>gnl|CDD|197212 cd09113, PLDc_ymdC_like_2, Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and similar proteins. Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and similar proteins. In Escherichia coli, there are two genes, f413 (ybhO) and o493 (ymdC), which are homologous to gene cls that encodes the Escherichia coli cardiolipin (CL) synthase. The prototype of this subfamily is an uncharacterized protein ymdC specified by the o493 (ymdC) gene. Although the functional characterization of ymdC and similar proteins remains unknown, members of this subfamily show high sequence homology to bacterial CL synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Moreover, ymdC and its similar proteins contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characteriszes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
LSDPPEKALKEAGPEPVLAYQLAELLKNAKREVLIVSPYFVPGDEGVALLAELARRGVRVRILTNSLAAT
DVPAVHSGYARYRKRLLKAGVELYELKPDAAKRKRLRGLFGSSRASLHAKSFVIDDRLVFVGSFNLDPRS
AYLNTEMGLVIDSPELAAQLRAAMEEDLAPSAYWVLLLDDGGLVWETEEDGKEKEYDSEPETSFWRRLGA
WLLSLLPI
>gnl|CDD|197213 cd09114, PLDc_PPK1_C1, Catalytic C-terminal domain, first repeat, of prokaryotic polyphosphate kinase 1 and similar proteins. Catalytic C-terminal domain, first repeat (C1 domain), of bacterial polyphosphate kinases 1 (Poly P kinase 1 or PPK1, EC 2.7.4.1) and similar proteins. Inorganic polyphosphate (Poly P) plays an important role in bacterial stress responses and stationary-phase survival. PPK1 is the key enzyme responsible for the synthesis of Poly P in bacteria. It can catalyze the reversible conversion of the terminal-phosphate of ATP to Poly P. Therefore, PPK1 is essential for bacterial motility, quorum sensing, biofilm formation, and the production of virulence factors and may serve as an attractive antimicrobial drug target. Dimerization is crucial for the enzymatic activity of PPK1. Each PPK1 monomer includes four structural domains, the N-terminal (N) domain, the head (H) domain, and two closely related C-terminal (C1 and C2) domains. The N domain provides the upper binding interface for the adenine ring of the ATP. The H domain is involved in dimerization, while both the C1 and C2 domains contain residues crucial for catalytic activity. The intersection of the N, C1, and C2 domains forms a structural tunnel in which the PPK catalytic reactions are carried out. In spite of the lack of sequence homology, the C1 and C2 domains of PPK1 are structurally similar to the two repetitive catalytic domains of phospholipase D (PLD). Moreover, some residues in the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) of the PLD superfamily are spatially conserved in the active site of PPK1. It is possible that the bacterial PPK1 family and the PLD family have a common ancestor and diverged early in evolution. There is a second bacterial-type enzyme, PPK2, which is involved in the synthesis of poly P from GTP or ATP. PPK2 shows no sequence similarity to PPK1 and belongs to different superfamily
NVFPQVKKKDVLLCYPYESFEPVLQLLRQASTDPEVLAIKITIYRLAKKSRIVDYLCAAAENGKEVTVVI
ELRARFDEENNIDWAERLEEAGCRVIYGFEGYKVHAKICLITRRERGEIHRYAHIGTGNYNEKTARLYTD
YSLLTADQEIGEDAAVFFNNMS
>gnl|CDD|197214 cd09115, PLDc_PPK1_C2, Catalytic C-terminal domain, second repeat, of prokaryotic polyphosphate kinase 1 and similar proteins. Catalytic C-terminal domain, second repeat (C2 domain), of bacterial polyphosphate kinases 1 (Poly P kinase 1 or PPK1, EC 2.7.4.1) and similar proteins. Inorganic polyphosphate (Poly P) plays an important role in bacterial stress responses and stationary-phase survival. PPK1 is the key enzyme responsible for the synthesis of Poly P in bacteria. It can catalyze the reversible conversion of the terminal-phosphate of ATP to Poly P. Therefore, PPK1 is essential for bacterial motility, quorum sensing, biofilm formation, and the production of virulence factors and may serve as an attractive antimicrobial drug target. Dimerization is crucial for the enzymatic activity of PPK1. Each PPK1 monomer includes four structural domains, the N-terminal (N) domain, the head (H) domain, and two closely related C-terminal (C1 and C2) domains. The N domain provides the upper binding interface for the adenine ring of the ATP. The H domain is involved in dimerization, while both the C1 and C2 domains contain residues crucial for catalytic activity. The intersection of the N, C1, and C2 domains forms a structural tunnel in which the PPK catalytic reactions are carried out. In spite of the lack of sequence homology, the C1 and C2 domains of PPK1 are structurally similar to the two repetitive catalytic domains of phospholipase D (PLD). Moreover, some residues in the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) of the PLD superfamily are spatially conserved in the active site of PPK1. It is possible that the bacterial PPK1 family and the PLD family have a common ancestor and diverged early in evolution. There is a second bacterial-type enzyme, PPK2, which is involved in the synthesis of poly P from GTP or ATP. PPK2 shows no sequence similarity to PPK1 and belongs to different superfamily
DYLLVAPQNLRRLLYEMIDREIANAQQGLPAGITLKLNSLTDKKLVDRLYKASSAGVPIDLVVRGMCCLI
PGLEGISDNIRVRSIVGRYLEHSRIYIFENGGDEKVYLSSADWMTRNIDYRVEVATPLLDPRLKQRVLDI
IDTLLSDNVKARYIDKEGSYRY
>gnl|CDD|197215 cd09116, PLDc_Nuc_like, Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar proteins. Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6 (PLD6, EC 3.1.4.4), and similar proteins. Nuc is an endonuclease from Salmonella typhimurium and the smallest known member of the PLD superfamily. It cleaves both single- and double-stranded DNA. PLD6 selectively hydrolyzes the terminal phosphodiester bond of phosphatidylcholine (PC), with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLD6 also catalyzes the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Both Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which is essential for catalysis. PLDs utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. This subfamily also includes some uncharacterized hypothetical proteins, which have two HKD motifs in a single polypeptide chain
YFLPRPQDNLERLIVALIANAKSSIDVAMYALTDPEIAEALKRAAKRGVRVRIILDKDSLADNLSITLLA
LLSNLGIPVRTDSGSKLMHHKFIIIDGKIVITGSANWTKSGFHRNDENLLIIDDPKLAASFEEEFNRL
>gnl|CDD|197216 cd09117, PLDc_Bfil_DEXD_like, Catalytic domain of type II restriction endonucleases BfiI and NgoFVII, and uncharacterized proteins with a DEAD domain. Catalytic domain of type II restriction endonucleases BfiI and NgoFVII, uncharacterized type III restriction endonuclease Res subunit, and uncharacterized DNA/RNA helicase superfamily II members. Proteins in this family are found mainly in prokaryotes. They contain one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in a single polypeptide chain, and have been classified as members of the phospholipase D (PLD, EC 3.1.4.4) superfamily. BfiI consists of two discrete domains with distinct functions: an N-terminal catalytic domain with non-specific nuclease activity and dimerization function that is more closely related to Nuc, an EDTA-resistant nuclease from the phospholipase D (PLD) superfamily; and a C-terminal domain that specifically recognizes its target sequences, 5'-ACTGGG-3'. BfiI forms a functionally active homodimer which has two DNA-binding surfaces located at the C-terminal domains but only one active site, located at the dimer interface between the two N-terminal catalytic domains that contain the two HKD motifs from both subunits. BfiI utilizes a single active site to cut both DNA strands, which represents a novel mechanism for the scission of double-stranded DNA. It uses a histidine residue from the HKD motif in one subunit as the nucleophile for the cleavage of the target phosphodiester bond in both of the anti-parallel DNA strands, while the symmetrically-related histidine residue from the HKD motif of the opposite subunit acts as the proton donor/acceptor during both strand-scission events
ESLEELLTRLIERADTIRIAVAFASAGGAIKLLDKFREGKKIRLIVGLDFGGTSPADFALKLLLALGNLN
VRIFDAGPLLHAKLYLFENDDPTRAIVGSANLTQGGLSGNIEAAVVI
>gnl|CDD|197217 cd09118, PLDc_yjhR_C_like, C-terminal domain of Escherichia coli uncharacterized protein yjhR and similar proteins. C-terminal domain of Escherichia coli uncharacterized protein yjhR, encoded by the o338 gene, and similar proteins. Although the biological function of yjhR remains unknown, it shows sequence similarity to the C-terminal portions of superfamily I DNA and RNA helicases, which are ubiquitous enzymes mediating ATP-dependent unwinding of DNA and RNA duplexes, and play essential roles in gene replication and expression. Moreover, The C-termini of yjhR and similar proteins contain one HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The PLDc-like domain of yjhR is similar to bacterial endonucleases, Nuc and BfiI, both of which have only one copy of the HKD motif per chain. They function as homodimers, with a single active site at the dimer interface containing the HKD motifs from both subunits. They utilize a two-step mechanism to cleave phosphodiester bonds. Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit
EHDAFLLKALATVRERIVIVSPWISLDALEADGLLEAIREAVSRGVDVTIYTDPHLNTGDANDTKANLED
AAEALAEAGIRIHEVNGVHSKIVIVDNHLLAVGSFNWLSAVRDGKYARHETSLVYRGEGLEKEINTILDS
LNSR
>gnl|CDD|197218 cd09119, PLDc_FAM83_N, N-terminal phospholipase D-like domain of proteins from the Family with sequence similarity 83. N-terminal phospholipase D (PLD)-like domain of vetebrate proteins from the Family with sequence similarity 83 (FAM83), which is comprised of 8 members, designated FAM83A through FAM83H. Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, the FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are unlikely to carry PLD activity. Members of the FAM83 are mostly uncharacterized proteins. FAM83A, also known as tumor antigen BJ-TSA-9, is a novel tumor-specific gene highly expressed in human lung adenocarcinoma. FAM83D, also known as spindle protein CHICA, is a cell-cycle-regulated spindle component which localizes to the mitotic spindle and is both upregulated and phosphorylated during mitosis. The gene encoding protein FAM83H is the first gene involved in the etiology of amelogenesis imperfecta (AI), that encodes a non-secreted protein due to the absence of a signal peptide. Defects in gene FAM83H cause autosomal dominant hypocalcified amelogenesis imperfecta (ADHCAI). FAM83B, FAM83C, FAM83F, and FAM83G are uncharacterized proteins present across vertebrates while FAM83E is an uncharacterized protein found only in mammals
ESYPEFFYSESARLALEALLEGGPEAYYRVLSTEREADFLSPEEIQYILSAARPYPEKPEAPGAAAGTQL
SLSSELSSGTYFPVNSDVEPPDLDLGWPETDAYRGVTRATVHFQPPKEGAPNIKDLVRRMIQQAQKVIAV
VMDVFTDVDIFCDLLEAANKRGVAVYILLDQGNVKHFLEMCDKLQLSDEHLKNMRVRSVGGKTYCSRSGK
KFKGQMKEKFLLVDGDRVVSGSYSFTWSDAKLHRSMLSVLTGQVVESFDEEFRILYAQS
>gnl|CDD|197219 cd09120, PLDc_DNaseII_1, Catalytic domain, repeat 1, of Deoxyribonuclease II and similar proteins. Catalytic domain, repeat 1, of Deoxyribonuclease II (DNase II, EC 3.1.22.1), an endodeoxyribonuclease with ubiquitous tissue distribution. It is essential for accessory apoptotic DNA fragmentation and DNA clearance during development, as well as in tissue regeneration in higher eukaryotes. Unlike the majority of nucleases, DNase II functions optimally at acidic pH in the absence of divalent metal ion cofactors. It hydrolyzes the phosphodiester backbone of DNA by a single strand cleavage mechanism to generate 3'-phosphate termini. The majority of family members contain an N-terminal signal-peptide leader sequence, which is critical for N-glycosylation and DNase II activity. DNase II is a monomeric nuclease that contains two copies of a variant HKD motif, where the aspartic acid residue is not conserved. The HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. The catalytic center of DNase II is formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. Members of this family are mainly found in metazoans, and vertebrate proteins have been further classified into DNase II alpha and beta (also known as DNase II-like acid DNase, DLAD) subtypes. A few homologs are found in non-metazoan species, but none are found in fungi, plants or prokaryotes, with the sole exception of Burkholderia pseudomallei. Among those homologs, the Caenorhabditis elegans C07B5.5 ORF encoding NUC-1 apoptotic nuclease, the uncharacterized C. elegans crn-6 (cell death related nuclease) gene encoding protein, and the putative gene CG7780 encoding Drosophila DNase II (dDNase II) have similar cleavage activity and specificity to mammalian DNase II enzymes. They may function like an acid DNase implicated in degrading DNA from apoptotic cells engulfed by macrophages. Plancitoxin I, the major lethal factor from the Acanthaster planci venom, is a unique homolog of mammalian DNase II. It has potent hepatotoxicity and the optimum pH for its activity is 7.2, unlike the optimum acidic PH for mammalian DNase II. Some members of this family contain substitutions of conserved residues found in the putative active site, which suggest that these proteins may have diverged from a canonical DNase II activity and may perform other functions
SALSCKDDNGNDVDWFFVYKLPKLKSSGDSGLGYLYADSTNGEWQLSLDNINDNNSALGRTLAQIYDSNK
ENILYVLYNDQPPNGTSSSSRGHAKGVVAFDNTSGFWLVHSVPKFPPLAEKSYSYPSTGTKYGQHFLCVS
L
>gnl|CDD|197220 cd09121, PLDc_DNaseII_2, Catalytic domain, repeat 2, of Deoxyribonuclease II and similar proteins. Catalytic domain, repeat 2, of Deoxyribonuclease II (DNase II, EC 3.1.22.1), an endodeoxyribonuclease with ubiquitous tissue distribution. It is essential for accessory apoptotic DNA fragmentation and DNA clearance during development, as well as in tissue regeneration in higher eukaryotes. Unlike the majority of nucleases, DNase II functions optimally at acidic pH in the absence of divalent metal ion cofactors. It hydrolyzes the phosphodiester backbone of DNA by a single strand cleavage mechanism to generate 3'-phosphate termini. The majority of family members contain an N-terminal signal-peptide leader sequence, which is critical for N-glycosylation and DNase II activity. DNase II is a monomeric nuclease that contains two copies of a variant HKD motif, where the aspartic acid residue is not conserved. The HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. The catalytic center of DNase II is formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. Members of this family are mainly found in metazoans, and vertebrate proteins have been further classified into DNase II alpha and beta (also known as DNase II-like acid DNase, DLAD) subtypes. A few homologs are found in non-metazoan species, but none are found in fungi, plants or prokaryotes, with the sole exception of Burkholderia pseudomallei. Among those homologs, the Caenorhabditis elegans C07B5.5 ORF encoding NUC-1 apoptotic nuclease, the uncharacterized C. elegans crn-6 (cell death related nuclease) gene encoding protein, and the putative gene CG7780 encoding Drosophila DNase II (dDNase II) have similar cleavage activity and specificity to mammalian DNase II enzymes. They may function like an acid DNase implicated in degrading DNA from apoptotic cells engulfed by macrophages. Plancitoxin I, the major lethal factor from the Acanthaster planci venom, is a unique homolog of mammalian DNase II. It has potent hepatotoxicity and the optimum pH for its activity is 7.2, unlike the optimum acidic PH for mammalian DNase II. Some members of this family contain substitutions of conserved residues found in the putative active site, which suggest that these proteins may have diverged from the canonical DNase II activity and may perform other functions
PPWQSSLELKSLGGVSFTSFAKSSKWGKDLYSDLVAPTLKTDLLVETWRGGGGNLPSDCSSKYKVYNVKS
ISLPGDIAFKSTKDHSKWAVSVDSSKPWVCIGDINRQESQFKRGGGTVCFKNKKLWKAFRKSVIDVEPC
>gnl|CDD|197221 cd09122, PLDc_Tdp1_1, Catalytic domain, repeat 1, of Tyrosyl-DNA phosphodiesterase. Catalytic domain, repeat 1, of Tyrosyl-DNA phosphodiesterase (Tdp1, EC 3.1.4.-), which exists in eukaryotes but not in prokaryotes. Tdp1 acts as an important DNA repair enzyme that removes stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of a phosphodiester bond between a tyrosine side chain and a DNA 3'-phosphate. It is a monomeric protein that contains two copies of a variant HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which consists of the highly conserved histidine and lysine residues, but lacks the aspartate residue that is well conserved in other phospholipase D (PLD, EC 3.1.4.4) enzymes. Thus, this family represents a distinct class within the PLD superfamily. Like other PLD enzymes, Tdp1 may utilize a common two-step general acid/base catalytic mechanism, involving a DNA-enzyme intermediate to cleave phosphodiester bonds. A single active site involved in phosphatidyl group transfer would be formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way
LSLKDLLGGDDLESALLSSYMLDIDWLLSQLPLLKIVPVTIVHGEKKEATKRASMIAQLNGLPNWTLVYP
PLPGGYGTHHSKLILLKYPTGLRVVIPTANLTPYDWGEKSQGIWVQDFPLKNKRSASSGNNENPSDFKED
LIRFL
>gnl|CDD|197222 cd09123, PLDc_Tdp1_2, Catalytic domain, repeat 2, of tyrosyl-DNA phosphodiesterase. Catalytic domain, repeat 2, of Tyrosyl-DNA phosphodiesterase (Tdp1, EC 3.1.4.-), which exists in eukaryotes but not in prokaryotes. Tdp1 acts as an important DNA repair enzyme that removes stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of a phosphodiester bond between a tyrosine side chain and a DNA 3'-phosphate. It is a monomeric protein that contains two copies of a variant HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which consists of the highly conserved histidine and lysine residues, but lacks the aspartate residue that is well conserved in other phospholipase D (PLD, EC 3.1.4.4) enzymes. Thus, this family represents a distinct class within the PLD superfamily. Like other PLD enzymes, Tdp1 may utilize a common two-step general acid/base catalytic mechanism, involving a DNA-enzyme intermediate to cleave phosphodiester bonds. A single active site involved in phosphatidyl group transfer would be formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way
LGRLRKLLQNLTLDNKEKEKSKPLVYQFSSIGSLDEKWWLNEFASSLGGVSSRSELPLVKKNSPSLGKPK
LKIIFPTVEEVRTSLEGYNGGGSIPFTIKNYESKEFLKKLFHRWKPRNNARRRQRAMPHIKTYIRYTDDG
KIDKLGWVYLGSHNLSKAAWGALQKNGSQLRIRNYELGVLFP
>gnl|CDD|197223 cd09124, PLDc_like_TrmB_middle, Middle phospholipase D-like domain of the transcriptional regulator TrmB and similar proteins. Middle phospholipase D (PLD)-like domain of the transcriptional regulator TrmB and similar proteins. TrmB acts as a bifunctional sugar-sensing transcriptional regulator which controls two operons encoding maltose/trehalose and maltodextrin ABC transporters of Pyrococcus fruiosus. It functions as a dimer. Full length TrmB includes an N-terminal DNA-binding domain, a C-terminal sugar-binding domain and middle region that has been named as a PLD-like domain. The middle domain displays homology to PLD enzymes, which contain one or two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) per chain. The HKD motif characterizes the PLD superfamily. Due to the lack of key residues related to PLD activity in the PLD-like domain, members of this subfamily are unlikely to carry PLD activity
RVWTIKGEENILAKIREMINSAKEEIYISLPSEELEELLEELEKAAERGVKVVIIIFGDDDLDDLDSPAI
EVRVREGGGRPFLLIVDSKEALIGPSSEEEETYALYTENPALVLLAREYFRHDIYL
>gnl|CDD|197224 cd09126, PLDc_C_DEXD_like, C-terminal putative phospholipase D-like domain of uncharacterized prokaryotic HKD family nucleases fused to DEAD/DEAH box helicases. C-terminal putative phospholipase D (PLD)-like domain of uncharacterized prokaryotic HKD family nucleases fused to a DEAD/DEAH box helicase domain. All members of this subfamily are uncharacterized. In addition to the helicase-like region, members of this family also contain a PLD-like domain in the C-terminal region, which is characterized by a variant HKD (H-x-K-x(4)-D motif, where x represents any amino acid residue) motif. Due to the lack of key residues related to PLD activity in the variant HKD motif, members of this subfamily are most unlikely to carry PLD activity
NSIYDGNNYEEVFRKDLAQAKKSIIISSPYVSQKRITKLINLLKEAQERGVEVTVVTREPKEYKELIEEL
RSAGVKVKLKEEIHEKFAIIDKKIVWYGSINLLGYSNAEDSIIRLKSAEIASELLE
>gnl|CDD|197225 cd09127, PLDc_unchar1_1, Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins. Putative catalytic domain, repeat 1, of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze transphosphatidylation of phospholipids to acceptor alcohols. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
TLFVQPDDGVAPVVDAIASAKRSILLKMYEFTDPALEKALAAAAKRGVRVRVLLEGGPVGGISRAEKLLD
YLNEAGVEVRWTNGTARYRYTHAKYIVVDDERALVLTENFKPSGFTGTRGFGVVTDDPAVVAEIADVFDA
D
>gnl|CDD|197226 cd09128, PLDc_unchar1_2, Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins. Putative catalytic domain, repeat 2, of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze transphosphatidylation of phospholipids to acceptor alcohols. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
SVQLLLSPDNAREALLALIDSAEESLLIQNEEMGDDAPILDALVDAAKRGVDVRVLLPSAWSAEDERQAR
LRALEGAGVPVRLLKDKFLKIHAKGIVVDGKTALVGSENWSANSLDRNREVGLIFDDPEVAAYLQAVFES
DW
>gnl|CDD|197227 cd09129, PLDc_unchar2_1, Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins. Putative catalytic domain, repeat 1, of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze transphosphatidylation of phospholipids to acceptor alcohols. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
IFDEILEIIDEAKDFIVLDMFLFNDYYDKKKGKFPPLSEELTDALIEKKKENPDLPIVVITDPINTFYGS
HDNPHLKKLKEAGIEVVETDLDKLRDSNPLYSGIWRTFIQWFGNSGKGWLPNPFGKEAPKVTLRSYLRLL
NFKANHRKVLVTENTALVTSANPHDASARHSNIAFEVSGPIIGDLLKSEQAVARFS
>gnl|CDD|197228 cd09130, PLDc_unchar2_2, Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins. Putative catalytic domain, repeat 2, of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze transphosphatidylation of phospholipids to acceptor alcohols. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
LTEGKIGEALLKEINSARAGDKIWIGMFYLADRDVIKALIDAANRGVDVRLILDPNKDAFGREKNGIPNR
PVAAELMKKTKGKIQIRWYNTGGEQFHTKLLLIKKKGQAIIIGGSANFTRRNLRDYNLETDLKILAPNDS
PVSKDVDAYFDRLWNNE
>gnl|CDD|197229 cd09131, PLDc_unchar3, Putative catalytic domain of uncharacterized phospholipase D-like proteins. Putative catalytic domain of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. Members of this subfamily contain one copy of HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily
DQEYYPALLDLINNAKRSIYIAMYMFKYYENPGNGVNTLLEALIDAHKRGVDVKVVLEDSIDDDEVTEEN
DNTYRYLKDNGVEVRFDSPSVTTHTKLVVIDGRTVYVGSHNWTYSALDYNHEASVLIESPEVADFAINYF
DSI
>gnl|CDD|197230 cd09132, PLDc_unchar4, Putative catalytic domain of uncharacterized phospholipase D-like proteins. Putative catalytic domain of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. Members of this subfamily contain one copy of HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily
EQVLLELIEGAERSLLIVGYSAYKVSELLQALAAALERGVQVRVVVESSEKAGSVLSLDEDELMWPKLAG
ATLYVWPEKKRPGKRASLHAKVIVADRRRLLVTSANLTGAGMERNIEAGVLV
>gnl|CDD|197231 cd09133, PLDc_unchar5, Putative catalytic domain of uncharacterized hypothetical proteins with one or two copies of the HKD motif. Putative catalytic domain of uncharacterized hypothetical proteins with similarity to phospholipase D (PLD, EC 3.1.4.4). PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze transphosphatidylation of phospholipids to acceptor alcohols. Members of this subfamily contain one or two copies of the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily
EHREKLLRALREAKRRVIIHSPWLGNAVFENLLEALEKAAERGVKIDILWGISSDEEKEKKALSEIAEKL
LADRGLRGGVNVHLRTTGSHAKFLVCDDWFALVGSCNWLSSGGDDFPRGELGVRLRD
>gnl|CDD|197232 cd09134, PLDc_PSS_G_neg_1, Catalytic domain, repeat 1, of phosphatidylserine synthases from gram-negative bacteria. Catalytic domain, repeat 1, of phosphatidylserine synthases (PSSs) from gram-negative bacteria. There are two subclasses of PSS enzymes in bacteria: subclass I of gram-negative bacteria and subclass II of gram-positive bacteria. It is common that PSSs in gram-positive bacteria and yeast are tight membrane-associated enzymes. By contrast, the gram-negative bacterial PSSs, such as Escherichia coli PSS, are commonly bound to the ribosomes. They are peripheral membrane proteins that can interact with the surface of the inner membrane by binding to the lipid substrate (CDP-diacylglycerol) and the lipid product (phosphatidylserine). The prototypical member of this subfamily is Escherichia coli PSS (also called CDP-diacylglycerol-L-serine O-phosphatidyltransferase, EC 2.7.8.8), which catalyzes the exchange reactions between CMP and CDP-diacylglycerol, and between serine and phosphatidylserine. The phosphatidylserine is then decarboxylated by phosphatidylserine decarboxylase to yield phosphatidylethanolamine, the major phospholipid in Escherichia coli. It also catalyzes the hydrolysis of CDP-diacylglycerol to form phosphatidic acid with the release of CMP. PSS may utilize a ping-pong mechanism involving a phosphatidyl-enzyme intermediate, which is distinct from those of gram-positive bacterial phosphatidylserine synthases. Moreover, all members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs constitute an active site for the formation of a covalent substrate-enzyme intermediate
LPKIPQQPEDIDVLYSPKDFRARLLELISNAKKRIYIVALYLEDDEAGREILDALYEAKANNPGLDIKVL
VDWHRAQRGLIGAKKSLGNADWYRKIAQRYGHDVPIYGVPVKTRELFGVLHLKGFIIDDTVLYSGASLNN
VYLHQFDKYRYDRYHLIYNPELADSMVNFIQDY
>gnl|CDD|197233 cd09135, PLDc_PGS1_euk_1, Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases. Catalytic domain, repeat 1, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer
QIRILRTPSEFYNTLLDKIRNAKRRIVLSSLYIGTGPLEQELVDALQEALERNPNLKVSILLDYLRGTRG
EPNSRTASLLLPLLKLFPDRVRVSLYHTPNLRGLLKKLLPERFNEIIGLQHMKLYIFDDDVILSGANLSD
DYFTNRQDRYMLIENCPELADFYHDLIKAV
>gnl|CDD|197234 cd09136, PLDc_PSS_G_neg_2, Catalytic domain, repeat 2, of phosphatidylserine synthases from gram-negative bacteria. Catalytic domain, repeat 2, of phosphatidylserine synthases (PSSs) from gram-negative bacteria. There are two subclasses of PSS enzymes in bacteria: subclass I of gram-negative bacteria and subclass II of gram-positive bacteria. It is common that PSSs in gram-positive bacteria and yeast are tight membrane-associated enzymes. By contrast, the gram-negative bacterial PSSs, such as Escherichia coli PSS, are commonly bound to the ribosomes. They are peripheral membrane proteins that can interact with the surface of the inner membrane by binding to the lipid substrate (CDP-diacylglycerol) and the lipid product (phosphatidylserine). The prototypical member of this subfamily is Escherichia coli PSS (also called CDP-diacylglycerol-L-serine O-phosphatidyltransferase, EC 2.7.8.8), which catalyzes the exchange reactions between CMP and CDP-diacylglycerol, and between serine and phosphatidylserine. The phosphatidylserine is then decarboxylated by phosphatidylserine decarboxylase to yield phosphatidylethanolamine, the major phospholipid in Escherichia coli. It also catalyzes the hydrolysis of CDP-diacylglycerol to form phosphatidic acid with the release of CMP. PSS may utilize a ping-pong mechanism involving a phosphatidyl-enzyme intermediate, which is distinct from those of gram-positive bacterial phosphatidylserine synthases. Moreover, all members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs constitute an active site for the formation of a covalent substrate-enzyme intermediate
LSITPLVGLGKRGNQLNRTIRQLIQSAESELIICTPYFNLPRSLVRDIARLLKRGVKVEIIVGDKTANDF
YIPPEEPFKTIGALPYLYEINLRRFAKRLQKYIDNGQLNVRLWKDGNNSFHLKGIWVDDRYHLLTGNNLN
PRAWRLDLENGLLIHDPQGQLKAQFEKELEQILAHTTRIKHYSQLESIADYPEKVQKLLRRIRRVRADRL
LKRIL
>gnl|CDD|197235 cd09137, PLDc_PGS1_euk_2, Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases. Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer
TWVYPLLQMGPLNISQEEQVTSRLLQLLPRGSSLTLASGYFNLTPEYLNLLLNSSANLDVLTASPEANGF
YGSKGVSGYIPPAYTYIARQFLKRVRKNGKQPRIKLFEYKRPGWTFHAKGLWIYLPGTDLPSLTLIGSSN
YGYRSVHRDLEAQFLIVTNNPKLQQQLKEELENLFEYSKPVTPETF
>gnl|CDD|197236 cd09138, PLDc_vPLD1_2_yPLD_like_1, Catalytic domain, repeat 1, of vertebrate phospholipases, PLD1 and PLD2, yeast PLDs, and similar proteins. Catalytic domain, repeat 1, of vertebrate phospholipases D (PLD1 and PLD2), yeast phospholipase D (PLD SPO14/PLD1), and other similar eukaryotic proteins. These PLD enzymes play a pivotal role in transmembrane signaling and cellular regulation. They hydrolyze the terminal phosphodiester bond of phospholipids resulting in the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. The vertebrate PLD1 and PLD2 are membrane associated phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent enzymes that selectively hydrolyze phosphatidylcholine (PC). Protein cofactors and calcium may be required for their activation. Yeast SPO14/PLD1 is a calcium-independent PLD, which needs PIP2 for its activity. Instead of the regulatory calcium-dependent phospholipid-binding C2 domain in plants, most mammalian and yeast PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at the N-terminus, which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. The PX and PH domains are also present in zeta-type PLD from Arabidopsis, which is more closely related to vertebrate PLDs than to other plant PLD types. In addition, this subfamily also includes some related proteins which have either PX-like or PH domains in their N-termini. Like other members of the PLD superfamily, the monomer of mammalian and yeast PLDs consists of two catalytic domains, each containing one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from the two domains form a single active site. These PLDs utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
AKWYVDGKDYFWAVADAIENAKEEIFITDWWLSPELYLRRPPAGNERWRLDRLLKRKAEEGVKIYILLYK
EVELALTINSKYTKRTLENLHPNIKVLRHPDHLPQGPLLWSHHEKIVVIDQSIAFVGGLDLCYGRWDTHQ
HPLTDD
>gnl|CDD|197237 cd09139, PLDc_pPLD_like_1, Catalytic domain, repeat 1, of plant phospholipase D and similar proteins. Catalytic domain, repeat 1, of plant phospholipase D (PLD, EC 3.1.4.4) and similar proteins. Plant PLDs have broad substrate specificity and can hydrolyze the terminal phosphodiester bond of several common membrane phospholipids such as phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG), and phosphatidylserine (PS), with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Most plant PLDs possess a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and require calcium for activity, which is unique to plant PLDs and is not present in animal or fungal PLDs. Like other PLD enzymes, the monomer of plant PLDs consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDs may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group. This subfamily includes two types of plant PLDs, alpha-type and beta-type PLDs, which are derived from different gene products and distinctly regulated. The zeta-type PLD from Arabidopsis is not included in this subfamily
NGQVYNPRRLWEDMYDAICNAKHLIYIAGWSVNPEISLIRDSEREDPPKYSPTLGELLKRKAEEGVAVLL
LLWDDKTVNGFKNDGVMATHDEETRNFFRNTKVNCLLCPRNGDAGNTYVEQIEVSTAFTHHQKTVIVDAP
APNGERREIVAFVGGIDLCDGRYDNPEHSLFRTLDT
>gnl|CDD|197238 cd09140, PLDc_vPLD1_2_like_bac_1, Catalytic domain, repeat 1, of uncharacterized bacterial proteins with similarity to vertebrate phospholipases, PLD1 and PLD2. Catalytic domain, repeat 1, of uncharacterized bacterial counterparts of vertebrate, yeast and plant phospholipase D (PLD, EC 3.1.4.4). PLDs hydrolyze the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. They also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Instead of the regulatory C2 (calcium-activated lipid binding) domain in plants and the adjacent Phox (PX) and the Pleckstrin homology (PH) N-terminal domains in most mammalian and yeast PLDs, many members in this subfamily contain a SNARE associated C-terminal domain, whose functional role is unclear. Like other PLD enzymes, members in this subfamily contain two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), that may play an important role in the catalysis
AAVLIDAADYFRALREALLRARRSILIVGWDFDSRIRLRRGGDDDGGPERLGDFLNWLAERRPDLDIRIL
KWDFAMLYALERELLPLFLLRWKTHPRIHFRLDGHHPLGASHHQKIVVIDDALAFCGGIDLTVDRWDTRE
HLDDDP
>gnl|CDD|197239 cd09141, PLDc_vPLD1_2_yPLD_like_2, Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, yeast PLDs, and similar proteins. Catalytic domain, repeat 2, of vertebrate phospholipases D (PLD1 and PLD2), yeast phospholipase D (PLD SPO14/PLD1), and other similar eukaryotic proteins. These PLD enzymes play a pivotal role in transmembrane signaling and cellular regulation. They hydrolyze the terminal phosphodiester bond of phospholipids resulting in the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. The vertebrate PLD1 and PLD2 are membrane associated phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent enzymes that selectively hydrolyze phosphatidylcholine (PC). Protein cofactors and calcium may be required for their activation. Yeast SPO14/PLD1 is a calcium-independent PLD, which needs PIP2 for its activity. Instead of the regulatory calcium-dependent phospholipid-binding C2 domain in plants, most mammalian and yeast PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at the N-terminus, which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. The PX and PH domains are also present in zeta-type PLD from Arabidopsis, which is more closely related to vertebrate PLDs than to other plant PLD types. In addition, this subfamily also includes some related proteins which have either PX-like or PH domains in their N-termini. Like other members of the PLD superfamily, the monomer of mammalian and yeast PLDs consists of two catalytic domains, each containing one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from the two domains form a single active site. These PLDs utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
GGIQTEDSIQNAYLDLIENAEHFIYIENQFFISSTGGEDPVKNRIGEALVDRIIRAHKEGEKFRVYIVLP
LLPGFEGDLDDPGGSSIRAIMHWQYQSICRGEHSLLERLKKEEGVDPEQYISFLSLRTHGKLGGRPVTEQ
IYVHSKLMIVDDRIVIIGSANINDRSMLGDRDSEIAVVIEDTE
>gnl|CDD|197240 cd09142, PLDc_pPLD_like_2, Catalytic domain, repeat 2, of plant phospholipase D and similar proteins. Catalytic domain, repeat 2, of plant phospholipase D (PLD, EC 3.1.4.4) and similar proteins. Plant PLDs have broad substrate specificity and can hydrolyze the terminal phosphodiester bond of several common membrane phospholipids such as phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG), and phosphatidylserine (PS), with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Most plant PLDs possess a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and require calcium for activity, which is unique to plant PLDs and is not present in animal or fungal PLDs. Like other PLD enzymes, the monomer of plant PLDs consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDs may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group. This subfamily includes two types of plant PLDs, alpha-type and beta-type PLDs, which are derived from different gene products and distinctly regulated. The zeta-type PLD from Arabidopsis is not included in this subfamily
KGRTIDRSIQDAYVHAIRRAKRFIYIENQYFLGSSFMWSNRDRDIGCANLIPAELALKIAEKIRARERFA
VYIVIPMWPEGIPESESVQEILYWQRLTIEMMYKIIGKAIQATGLFSEHPTDYLNFFCLGNREEVEGGEY
EATETPTQGTDYYRLQKNRRFMIYVHSKMMIVDDEYIIIGSANINQRSMDGCRDSEIAMGAYQPDHLA
>gnl|CDD|197241 cd09143, PLDc_vPLD1_2_like_bac_2, Catalytic domain, repeat 2, of uncharacterized bacterial proteins with similarity to vertebrate phospholipases, PLD1 and PLD2. Catalytic domain, repeat 2, of uncharacterized bacterial counterparts of vertebrate, yeast and plant phospholipase D (PLD, EC 3.1.4.4). PLDs hydrolyze the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. They also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Instead of the regulatory C2 (calcium-activated lipid binding) domain in plants and the adjacent Phox (PX) and the Pleckstrin homology (PH) N-terminal domains in most mammalian and yeast PLDs, many members in this subfamily contain a SNARE associated C-terminal domain, whose functional role is unclear. Like other PLD enzymes, members in this subfamily contain two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), that may play an important role in the catalysis
RGQPEVREIEALYLDAIAAARRFIYIENQYFTSRRIAEALAERLREPDGPEIVIVLPRTSDGWLEQLTMG
VARARLLRRLREADRHGRLRVYYPVTAGGGGRPIYVHSKLMIVDDRLLRVGSANLNNRSMGLDTECDLAI
EA
>gnl|CDD|197242 cd09144, PLDc_vPLD3_1, Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD3. Putative catalytic domain, repeat 1, of phospholipase D3 (PLD3, EC 3.1.4.4). The human protein is also known as Hu-K4 or HUK4 and it was identified as a human homolog of the vaccinia virus protein K4, which is encoded by the HindIII K4L gene. PLD3 is found in many human organs with highest expression levels found in the central nervous system. Due to the presence of two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), PLD3 has been assigned to the PLD superfamily although no catalytic activity has been detected experimentally. PLD3 is a membrane-bound protein that colocalizes with protein disulfide isomerase, an endoplasmic reticulum (ER) protein. Like other homologs of protein K4, PLD3 might alter the lipid content of associated membranes by selectively hydrolyzing phosphatidylcholine (PC) into the corresponding phosphatidic acid, which is thought to be involved in the regulation of lipid movement
VLVESIPEGLVFNSSSTINPSIYQAWLNLISAAQSSLDIASFYWTLTNSDTHTQEPSANQGEQILKKLGQ
LSQSGVYVRIAVDKPADPKPMEDINALSSYGADVRMVDMRKLTTGVLHTKFWVVDKKHFYIGSANMDWRS
LTQVKELGAVVYNCSCLAEDLGKIFEAYWYLG
>gnl|CDD|197243 cd09145, PLDc_vPLD4_1, Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4. Putative catalytic domain, repeat 1, of vertebrate phospholipases D4 (PLD4, EC 3.1.4.4), homologs of the vaccinia virus protein K4 which is encoded by the HindIII K4L gene. Due to the presence of two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), PLD4 has been assigned to PLD superfamily although no catalytic activity has been detected to date. Unlike PLD1 and PLD2, PLD4 does not contain Phox (PX) and Pleckstrin homology (PH) domains but has a putative transmembrane domain. Like other vertebrate homologs of protein K4, PLD4 might be associated with Golgi membranes and alter their lipid content by selectively hydrolyze phosphatidylcholine (PC) into corresponding phosphatidic acid, which is thought to be involved in the regulation of lipid movement
LVESIPEDLTYEGNSTFALPLQKAWTKLLDMAQEQVHVASYYWSLTGEDIGVNDSSSLPGEDILKELAEL
LSRNVSVRAAASIPTLAANSTDLKILRQKGAHVRKVNFGRLTGGVLHSKFWIIDKKHIYVGSANMDWRSL
TQVKELGAVIYNCSSLAKDLHKTFQTYWVL
>gnl|CDD|197244 cd09146, PLDc_vPLD5_1, Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5. Putative catalytic domain, repeat 1, of inactive veterbrate phospholipases D5 (PLD5, EC 3.1.4.4), homologs of the vaccinia virus protein K4 encoded by the HindIII K4L gene. Vertebrate PLD5 has been assigned to the PLD superfamily, since it shows high sequence similarity to other human homologs of protein K4, which contain two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). However, due to the lack of functionally important histidine and lysine residues in the HKD motif, vetebrate PLD5 has been characterized as an inactive PLD
ALVENIPDGINFSEHAPPHLPLSQGWMNLLDMAVKSVEIVSPLWDLNASHPSACQGQRLFERLLGLASRG
VELKIVSGITDSTEVLVLLKKKGAEVHYVNMTALTKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELG
VIVYNCSCLALDLHRVFALYWSL
>gnl|CDD|197245 cd09147, PLDc_vPLD3_2, Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3. Putative catalytic domain, repeat 2, of phospholipase D3 (PLD3, EC 3.1.4.4). The human protein is also known as Hu-K4 or HUK4 and it was identified as a human homolog of the vaccinia virus protein K4, which is encoded by the HindIII K4L gene. PLD3 is found in many human organs with highest expression levels found in the central nervous system. Due to the presence of two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), PLD3 has been assigned to the PLD superfamily although no catalytic activity has been detected experimentally. PLD3 is a membrane-bound protein that colocalizes with protein disulfide isomerase, an endoplasmic reticulum (ER) protein. Like other homologs of protein K4, PLD3 might alter the lipid content of associated membranes by selectively hydrolyzing phosphatidylcholine (PC) into the corresponding phosphatidic acid, which is thought to be involved in the regulation of lipid movement
YLSSSPPPLCASGRTPDLQSILNVIDNARSFVYIAVMNYLPTLEFSHPHRYWPAIDDGLRRATYERGVKV
RLLISCWGHSEPSMFAFLRSLAALRDNTTHSDIQVKIFVVPADEAQKKIPYARVNHNKYMVTDRVAYIGT
SNWSGDYFTNTAGSALVVNQTGRSASGTLQSQLQAVFERDWDSPYS
>gnl|CDD|197246 cd09148, PLDc_vPLD4_2, Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4. Putative catalytic domain, repeat 2, of vertebrate phospholipases D4 (PLD4, EC 3.1.4.4), homologs of the vaccinia virus protein K4 which is encoded by the HindIII K4L gene. Due to the presence of two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), PLD4 has been assigned to PLD superfamily although no catalytic activity has been detected to date. Unlike PLD1 and PLD2, PLD4 does not contain Phox (PX) and Pleckstrin homology (PH) domains but has a putative transmembrane domain. Like other vertebrate homologs of protein K4, PLD4 might be associated with Golgi membranes and alter their lipid content by selectively hydrolyze phosphatidylcholine (PC) into corresponding phosphatidic acid, which is thought to be involved in the regulation of lipid movement
YLSASPPALCPTGRTSDLQAILSVISQAQEFIYISVMEYFPTCRFCHPKRYWSVLDNALRAAAFDRRVLI
RLLISCGRHSDPDMFPFLRSLNALSNPPLSISVHVKLFIVPVGNQTNIPYSRVNHNKFMVTDKAAYIGTS
NWSEDYFLNTAGVGLVILQSPGANEEMLPVQEQLRSLFERDWSSPYA
>gnl|CDD|197247 cd09149, PLDc_vPLD5_2, Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5. Putative catalytic domain, repeat 2, of inactive veterbrate phospholipases D5 (PLD5, EC 3.1.4.4), homologs of the vaccinia virus protein K4 encoded by the HindIII K4L gene. Vertebrate PLD5 has been assigned to the PLD superfamily, since it shows high sequence similarity to other human homologs of protein K4, which contain two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). However, due to the lack of functionally important histidine and lysine residues in the HKD motif, vetebrate PLD5 has been characterized as an inactive PLD
YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRV
RLLISFWRKTDPLTFNFVSSLKSLCTEQANCSLEVKFFDLEEESDCTSPRLNRNKYMVTDGAAYIGNFDW
VGNDFTQNAGVGLVINQADGVEENNATIIEQLRAAFERDWYSNYAKSL
>gnl|CDD|197248 cd09150, PLDc_Ymt_1, Putative catalytic domain, repeat 1, of Yersinia pestis murine toxin-like proteins. Putative catalytic domain, repeat 1, of Yersinia pestis murine toxin (Ymt), a plasmid-encoded phospholipase D (PLD, EC 3.1.4.4), and similar proteins. Ymt is important in order for Yersinia pestis to survive and spread. It is toxic to mice and rats but not to other animals. It is not a conventional secreted exotoxin, but a cytoplasmic protein that is released upon bacterial lysis. Ymt may be active as a dimer. The monomeric Ymt consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Ymt has PLD-like activity and has been classified into the PLD superfamily. It hydrolyzes the terminal phosphodiester bond in several phospholipids, with preference for phosphatidylethanolamine (PE) over phosphatidylcholine (PC) and phosphatidylserine (PS). Like other PLD enzymes, Ymt may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group. In terms of sequence similarity, Ymt is closely related to Streptomyces PLDs
GINYVRLLDTPRVWGLPFGKEIMPQAWERQGEFERAIVEVLQKTRYRCDISSLNSPDPDWRKVILGAIDT
ALSKKMNRTEPTQFRFLFGQTPLVPMNGPTNYTAFKAALIRLIRERGHYWERMPEIWLGRFYRIEEGLLD
SLQKKVLPEDFFPGDDTKMTWNHTKIIAVDGLEALVGGHNLNMDLFRSYPPVHDVSVIVHGPAALGSQLY
LNELW
>gnl|CDD|197249 cd09151, PLDc_Ymt_2, Putative catalytic domain, repeat 2, of Yersinia pestis murine toxin-like proteins. Putative catalytic domain, repeat 2, of Yersinia pestis murine toxin (Ymt), a plasmid-encoded phospholipase D (PLD, EC 3.1.4.4), and similar proteins. Ymt is important in order for Yersinia pestis to survive and spread. It is toxic to mice and rats but not to other animals. It is not a conventional secreted exotoxin, but a cytoplasmic protein that is released upon bacterial lysis. Ymt may be active as a dimer. The monomeric Ymt consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Ymt has PLD-like activity and has been classified into the PLD superfamily. It hydrolyzes the terminal phosphodiester bond in several phospholipids, with preference for phosphatidylethanolamine (PE) over phosphatidylcholine (PC) and phosphatidylserine (PS). Like other PLD enzymes, Ymt may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group. In terms of sequence similarity, Ymt is closely related to Streptomyces PLDs
TRMLSVGKYWRGPTMRTDYQGGSEIMKEQLIKNAKRSIRMSQQDLVSAWKKNWSDHVVCQWVIEALLANK
SLKVEVVVSPLDAAAGAAGDQYSFGSGAVRTFELFKYYLTHDVATDAVLPDPDGARKEALKRIFVAPFFF
TDKVPPGDNIEGDTYKWPNLPKEGYTATLKQPPLSEEPPKHGVIGSAAMSVIKASGYIYPKVPSAPGNHA
KLMIIDDELYVVGSDNLYPGYLSEFDYLIEGPDAVSELLKSYWEPLWKYSGPHA
>gnl|CDD|197250 cd09152, PLDc_EcCLS_like_1, Catalytic domain, repeat 1, of Escherichia coli cardiolipin synthase and similar proteins. Catalytic domain, repeat 1, of Escherichia coli cardiolipin (CL) synthase and similar proteins. Escherichia coli CL synthase (EcCLS), specified by the cls gene, is the prototype of this family. EcCLS is a multi-pass membrane protein that catalyzes reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form cardiolipin (CL) and glycerol. The monomer of EcCLS consists of two catalytic domains. Each catalytic domain contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. Two HKD motifs from two domains form a single active site involved in phosphatidyl group transfer. EcCLS can be stimulated by phosphate and inhibited by CL, the product of the reaction, and by phosphatidate. Phosphate stimulation may be unique to enzymes with CL synthase activity belonging to the PLD superfamily. Like other PLD enzymes, EcCLS utilizes a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
GNRVELLTDYDAVIDRLIADIDAAKHHVHLLFYIWADDGTGDRVAEALERAAKRGVTCRLLLDAVGSRAF
FRSSLWKRLREAGVEVVEALPLRLFRRRLARFDLRNHRKIAVIDGRIAYTGSQNIIDPEFFKKAGGGPWV
DLMVRVEGPVVSQLQAVFASDWY
>gnl|CDD|197251 cd09154, PLDc_SMU_988_like_1, Putative catalytic domain, repeat 1, of Streptococcus mutans uncharacterized protein SMU_988 and similar proteins. Putative catalytic domain, repeat 1, of Streptococcus mutans uncharacterized protein SMU_988 and similar proteins. Although SMU_988 and similar proteins have not been functionally characterized, members in this subfamily show high sequence homology to bacterial cardiolipin (CL) synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
FPLGEDMFEDMLEDLKKAEKFIFMEYFIIEEGYMWDSILEILKEKAKEGVEVRIMYDDFGSITTLPKDYP
KELEKIGIKCRVFNPFKPILSLYMNNRDHRKITVIDGKVAFTGGINLADEYINKIERFGYWKDTGIRLEG
EAVWSLTVMFLEMWN
>gnl|CDD|197252 cd09155, PLDc_PaCLS_like_1, Putative catalytic domain, repeat 1, of Pseudomonas aeruginosa cardiolipin synthase and similar proteins. Putative catalytic domain, repeat 1, of Pseudomonas aeruginosa cardiolipin (CL) synthase (PaCLS) and similar proteins. Although PaCLS and similar proteins have not been functionally characterized, members in this subfamily show high sequence homology to bacterial CL synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Moreover, PaCLS and other members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
IDGEATFAAIFEAIASAEEYILVQFYIIRDDDLGRELKDALIARAQAGVRVYLLYDEIGSHSLSRSYIER
LRKAGVEVSAFNTTRGWGNRFQLNFRNHRKIVVVDGQTAFVGGHNVGDEYLGRDPRLGPWRDTHVKLEGP
AVQQLQLSFAEDWYWA
>gnl|CDD|197253 cd09156, PLDc_CLS_unchar1_1, Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial cardiolipin synthase. Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial cardiolipin (CL) synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
ADGVEAYQALIQLIESAKHSIDVCTFILGDDATGRRVIDALARKAREGVEVRLLLDALGSFFLSRRALKK
LRAAGGKVAFFMPVFRLPFRGRTNLRNHRKIAIADGSTAISGGMNLANEYMGPEPDDGRWVDLSFLIEGP
AVAQYQEVFRSDWA
>gnl|CDD|197254 cd09157, PLDc_CLS_unchar2_1, Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial cardiolipin synthase. Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial cardiolipin (CL) synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
VNGDEAYPAMLEAIDAARHSIALSSYIFDNDGVGREFVDALAEAVARGVDVRVLIDGVGARYSRPSIRRR
LRRAGVPVARFLPPRLPPRLPFINLRNHRKILVVDGRTGFTGGMNIRDGHLVADDPKNPVQDLHFRVEGP
VVAQLQEVFAEDWYF
>gnl|CDD|197255 cd09158, PLDc_EcCLS_like_2, Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase and similar proteins. Catalytic domain, repeat 2, of Escherichia coli cardiolipin (CL) synthase and similar proteins. Escherichia coli CL synthase (EcCLS), specified by the cls gene, is the prototype of this family. EcCLS is a multi-pass membrane protein that catalyzes reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form cardiolipin (CL) and glycerol. The monomer of EcCLS consists of two catalytic domains. Each catalytic domain contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. Two HKD motifs from two domains form a single active site involved in phosphatidyl group transfer. EcCLS can be stimulated by phosphate and inhibited by CL, the product of the reaction, and by phosphatidate. Phosphate stimulation may be unique to enzymes with CL synthase activity belonging to the PLD superfamily. Like other PLD enzymes, EcCLS utilizes a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
VPSGPDYPTENIPQLLLSAIHAARRRVVITTPYFVPDESLLQALCTAALRGVEVTLILPAKNDSFLVGAA
SRSYYEELLEAGVKIYLYRGGLLHAKTVTVDDEVALVGSSNFDIRSFALNFEISLILYDKEFTAQLRAIQ
ERYLARSDPLTLEEWKKRPLWRRLLENLARLLSP
>gnl|CDD|197256 cd09159, PLDc_ybhO_like_2, Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins. Catalytic domain, repeat 2, of Escherichia coli cardiolipin (CL) synthase ybhO and similar proteins. In Escherichia coli, there are two genes, f413 (ybhO) and o493 (ymdC), which are homologous to gene cls that encodes the Escherichia coli CL synthase. The prototype of this subfamily is Escherichia coli CL synthase ybhO specified by the f413 (ybhO) gene. ybhO is a membrane-bound protein that catalyzes the formation of cardiolipin (CL) by transferring phosphatidyl group between two phosphatidylglycerol molecules. It can also catalyze phosphatidyl group transfer to water to form phosphatidate. In contrast to the Escherichia coli CL synthase encoded by the cls gene (EcCLS), ybhO does not hydrolyze CL. Moreover, ybhO lacks an N-terminal segment encoded by Escherichia coli cls, which makes ybhO easy to denature. The monomer of ybhO consists of two catalytic domains. Each catalytic domain contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. Two HKD motifs from two domains form a single active site involved in phosphatidyl group transfer. ybhO can be stimulated by phosphate and inhibited by CL, the product of the reaction, and by phosphatidate. Phosphate stimulation may be unique to enzymes with CL synthase activity belonging to the PLD superfamily
VVSDPRRRRSSIRRAYLVAIAAARRRIWIANAYFVPDRRLRRALIEAARRGVDVRLLLPGKSDDPLTVAA
SRALYGKLLRAGVRIFEYQPSMLHAKTAVIDGDWATVGSSNLDPRSLRLNLEANLVVEDPAFAAQLEELF
EEDLARSREITLEEWRRRPLWQRLLEWLAY
>gnl|CDD|197257 cd09160, PLDc_SMU_988_like_2, Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 and similar proteins. Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 and similar proteins. Although SMU_988 and similar proteins have not been functionally characterized, members in this subfamily show high sequence homology to bacterial cardiolipin (CL) synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
FGDSPLDNEPVGENVYLDLINQAKDYVYITTPYLILDDEMLDALCLAAKRGVDVRIITPHIPDKKYVFLV
TRSNYPELLEAGVKIYEYTPGFIHAKTFVSDDKAAVVGTINLDYRSLYLHFECGVYMYDTPVISDIKEDF
EETLAQSQEITLEECRKRSLVTRLIGAILRLFAPLM
>gnl|CDD|197258 cd09161, PLDc_PaCLS_like_2, Putative catalytic domain, repeat 2, of Pseudomonas aeruginosa cardiolipin synthase and similar proteins. Putative catalytic domain, repeat 2, of Pseudomonas aeruginosa cardiolipin (CL) synthase (PaCLS) and similar proteins. Although PaCLS and similar proteins have not been functionally characterized, members in this subfamily show high sequence homology to bacterial CL synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Moreover, PaCLS and other members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
LPTGPADRIETCSLFFVQAINAAQKRLWIASPYFVPDEGVLAALQLAALRGVDVRILIPERPDHLLVYLA
SFSYLPELIRAGVKVYRYQPGFLHQKVVLVDDELAAVGTANLDNRSFRLNFEITALVADPGFAQEVEAML
EADFAASREVTAAELANRPLWFRLGARVARLFAPIL
>gnl|CDD|197259 cd09162, PLDc_CLS_unchar1_2, Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial cardiolipin synthase. Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial cardiolipin (CL) synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
VPSGPDVPGDPLYEALLSAIFEAEHRIWIVTPYFVPDEVLLRALRLAARRGVDVRLIVPKRSNHRIADLA
RGSYLRDLQEAGAEIYLYQPGMLHAKAVVVDDKLALVGSANLDMRSLFLNYEVAVFFYSPADIKELSDWI
ESLISQCTEGAPPPSALRDIAEGLMRLLAPLL
>gnl|CDD|197260 cd09163, PLDc_CLS_unchar2_2, Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial cardiolipin synthase. Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial cardiolipin (CL) synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer
IPDGPDEDLDKLRWTLLGAISAARHSIRIMTPYFLPDRTLITALQAAALRGVEVDIVLPERNNLPLVDWA
MRANLWELLEHGVRIYLQPPPFDHSKLMVVDGAWALIGSANWDPRSLRLNFELNLEVYDTALAGQLDALF
DSKIAKSREVTLEELDARPLPIRLRDAAARLFSPYL
>gnl|CDD|197261 cd09164, PLDc_EcPPK1_C1_like, Catalytic C-terminal domain, first repeat, of Escherichia coli polyphosphate kinase 1 and similar proteins. Catalytic C-terminal domain, first repeat (C1 domain), of Escherichia coli polyphosphate kinase 1 (Poly P kinase 1 or PPK1, EC 2.7.4.1) and similar proteins. Inorganic polyphosphate (Poly P) plays an important role in bacterial stress responses and stationary-phase survival. PPK1 is the key enzyme responsible for the synthesis of Poly P in bacteria. It can catalyze the reversible conversion of the terminal-phosphate of ATP to Poly P. Therefore, PPK1 is essential for bacterial motility, quorum sensing, biofilm formation, and the production of virulence factors and may serve as an attractive antimicrobial drug target. Dimerization is crucial for the enzymatic activity of PPK1. The prototype of this subfamily is Escherichia coli polyphosphate kinase (EcPPK), which forms a homotetramer in solution, and becomes a homodimer upon the binding of AMPPNP, a non-hydrolysable ATP analogue. Each EcPPK monomer includes four structural domains, the N-terminal (N) domain, the head (H) domain, and two closely related C-terminal (C1 and C2)domains. The N domain provides the upper binding interface for the adenine ring of the ATP. The H domain is involved in dimerization, while both the C1 and C2 domains contain residues crucial for catalytic activity. The intersection of the N, C1, and C2 domains forms a structural tunnel in which the PPK catalytic reactions are carried out. In spite of the lack of sequence homology, the C1 and C2 domains of EcPPK are structurally similar to the two repetitive catalytic domains of phospholipase D (PLD). Moreover, some residues in the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) of the PLD superfamily are spatially conserved in the active site of EcPPK. It is possible that the bacterial PPK1 family and the PLD family have a common ancestor and diverged early in evolution
SLFEAIREKDVLLHFPYQSFDYVIRLLREAAIDPNVTEIKITLYRVAKNSRIINALINAAKNGKKVTVFV
ELKARFDEENNIYWAKRLEEAGVKVIYSVPGLKVHAKLCLITRREGGGTVRYAYIGTGNFNEKTARLYTD
HALLTANKKITAELEKVFDFLE
>gnl|CDD|197262 cd09165, PLDc_PaPPK1_C1_like, Catalytic C-terminal domain, first repeat, of Pseudomonas aeruginosa polyphosphate kinase 1 and similar proteins. Catalytic C-terminal domain, first repeat (C1 domain), of polyphosphate kinase (Poly P kinase 1 or PPK1, EC 2.7.4.1) from Pseudomonas aeruginosa (PaPPK1), Dictyostelium discoideum (DdPPK1), and other similar proteins. Inorganic polyphosphate (Poly P) plays an important role in bacterial stress responses and stationary-phase survival. PaPPK1 is the key enzyme responsible for the synthesis of Poly P in Pseudomonas aeruginosa. It can catalyze the reversible conversion of the terminal-phosphate of ATP to Poly P. PaPPK1 shows high sequence homolog to Escherichia coli polyphosphate kinase (EcPPK), which contains four structural domains per chain: the N-terminal (N) domain, the head (H) domain, and two closely related C-terminal (C1 and C2) domains. The N domain provides the upper binding interface for the adenine ring of the ATP. The H domain is involved in dimerization, while both the C1 and C2 domains contain residues crucial for catalytic activity. The intersection of the N, C1, and C2 domains forms a structural tunnel in which the PPK catalytic reactions are carried out. The polyphosphate kinase from Dictyostelium discoideum (DdPPK1) shares similar structural features with EcPPK1 in the ATP-binding pocket and poly P tunnel, but has a unique N-terminal extension that may be responsible for its enzymatic activity, cellular localization, and physiological functions. In spite of the lack of sequence homology, the C1 and C2 domains of the family members are structurally similar to the two repetitive catalytic domains of phospholipase D (PLD). Moreover, some residues in the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) of the PLD superfamily are spatially conserved in the active site of PPK1. It is possible that the bacterial PPK1 family and the PLD family have a common ancestor and diverged early in evolution. In some bacteria, such as Pseudomonas aeruginosa, a second enzyme, PPK2, which is involved in the alternative pathway of polyphosphate synthesis, has been found. It can catalyze the synthesis of poly P from GTP or ATP, with a preference for Mn2+ over Mg2+. PPK2 shows no sequence similarity to PPK1 and belongs to a different superfamily
DIFSAIRKKDILLHHPYESFDPVVDFLEQAARDPDVLAIKMTLYRTSGNSPIVDALIEAAENGKQVTVLV
ELKARFDEENNIHWARKLEEAGCHVVYGLVGLKTHAKLLLVVRREDGGLRRYVHLGTGNYNPKTARLYTD
LGLFTADPEIGADVANLFNALTGY
>gnl|CDD|197263 cd09166, PLDc_PPK1_C1_unchar, Catalytic C-terminal domain, first repeat, of uncharacterized prokaryotic polyphosphate kinases. Catalytic C-terminal domain, first repeat (C1 domain), of a group of uncharacterized prokaryotic polyphosphate kinases (Poly P kinase 1 or PPK1, EC 2.7.4.1). Inorganic polyphosphate (Poly P) plays an important role in bacterial stress responses and stationary-phase survival. PPK1 is the key enzyme responsible for the synthesis of Poly P in bacteria. It can catalyze the reversible conversion of the terminal-phosphate of ATP to Poly P. Therefore, PPK1 is essential for bacterial motility, quorum sensing, biofilm formation, and the production of virulence factors and may serve as an attractive antimicrobial drug target. Dimerization is crucial for the enzymatic activity of PPK1. Each PPK1 monomer includes four structural domains, the N-terminal (N) domain, the head (H) domain, and two closely related C-terminal (C1 and C2) domains. The N domain provides the upper binding interface for the adenine ring of the ATP. The H domain is involved in dimerization, while both the C1 and C2 domains contain residues crucial for catalytic activity. The intersection of the N, C1, and C2 domains forms a structural tunnel in which the PPK catalytic reactions are carried out. In spite of the lack of sequence homology, the C1 and C2 domains of PPK1 are structurally similar to the two repetitive catalytic domains of phospholipase D (PLD). Moreover, some residues in the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) of the PLD superfamily are spatially conserved in the active site of PPK1. It is possible that the bacterial PPK1 family and the PLD family have a common ancestor and diverged early in evolution
SIFKQVRQKDVLLSYPYESMDPFLNLLKEAAEDPEVISIKITLYRLAKQSRLVEYLIEAAENGKDVTVLM
ELRARFDEENNIEWAERLEEAGCTVIYGFEDYKVHSKICLITRKEDGGITYITQIGTGNYNEKTAKIYTD
LSLLTADQEIGQDAADFFKNLA
>gnl|CDD|197264 cd09167, PLDc_EcPPK1_C2_like, Catalytic C-terminal domain, second repeat, of Escherichia coli polyphosphate kinase 1 and similar proteins. Catalytic C-terminal domain, second repeat (C2 domain), of Escherichia coli polyphosphate kinase 1 (Poly P kinase 1 or PPK1, EC 2.7.4.1) and similar proteins. Inorganic polyphosphate (Poly P) plays an important role in bacterial stress responses and stationary-phase survival. PPK1 is the key enzyme responsible for the synthesis of Poly P in bacteria. It can catalyze the reversible conversion of the terminal-phosphate of ATP to Poly P. Therefore, PPK1 is essential for bacterial motility, quorum sensing, biofilm formation, and the production of virulence factors and may serve as an attractive antimicrobial drug target. Dimerization is crucial for the enzymatic activity of PPK1. The prototype of this subfamily is Escherichia coli polyphosphate kinase (EcPPK), which forms a homotetramer in solution, and becomes a homodimer upon the binding of AMPPNP, a non-hydrolysable ATP analogue. Each EcPPK monomer includes four structural domains, the N-terminal (N) domain, the head (H) domain, and two closely related C-terminal (C1 and C2)domains. The N domain provides the upper binding interface for the adenine ring of the ATP. The H domain is involved in dimerization, while both the C1 and C2 domains contain residues crucial for catalytic activity. The intersection of the N, C1, and C2 domains forms a structural tunnel in which the PPK catalytic reactions are carried out. In spite of the lack of sequence homology, the C1 and C2 domains of EcPPK are structurally similar to the two repetitive catalytic domains of phospholipase D (PLD). Moreover, some residues in the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) of the PLD superfamily are spatially conserved in the active site of EcPPK. It is possible that the bacterial PPK1 family and the PLD family have a common ancestor and diverged early in evolution
FKHLLVSPFNMRNRLLELIDREIKNAKAGKPAGITLKLNNLQDKEMIDKLYEASQAGVKIDLIVRGICSL
IPGIPGISENIRVISIVDRYLEHSRVYIFGNGGNEKVYISSADWMTRNLDRRIEVAFPIYDPDLKQELLD
ILDIQLADNVKARIIDAEQSNEYVK
>gnl|CDD|197265 cd09168, PLDc_PaPPK1_C2_like, Catalytic C-terminal domain, second repeat, of Pseudomonas aeruginosa polyphosphate kinase 1 and similar proteins. Catalytic C-terminal domain, second repeat (C2 domain), of polyphosphate kinase (Poly P kinase 1 or PPK1, EC 2.7.4.1) from Pseudomonas aeruginosa (PaPPK1), Dictyostelium discoideum (DdPPK1), and other similar proteins. Inorganic polyphosphate (Poly P) plays an important role in bacterial stress responses and stationary-phase survival. PaPPK1 is the key enzyme responsible for the synthesis of Poly P in Pseudomonas aeruginosa. It can catalyze the reversible conversion of the terminal-phosphate of ATP to Poly P. PaPPK1 shows high sequence homolog to Escherichia coli polyphosphate kinase (EcPPK), which contains four structural domains per chain: the N-terminal (N) domain, the head (H) domain, and two closely related C-terminal (C1 and C2) domains. The N domain provides the upper binding interface for the adenine ring of the ATP. The H domain is involved in dimerization, while both the C1 and C2 domains contain residues crucial for catalytic activity. The intersection of the N, C1, and C2 domains forms a structural tunnel in which the PPK catalytic reactions are carried out. The polyphosphate kinase from Dictyostelium discoideum (DdPPK1) shares similar structural features with EcPPK1 in the ATP-binding pocket and poly P tunnel, but has a unique N-terminal extension that may be responsible for its enzymatic activity, cellular localization, and physiological functions. In spite of the lack of sequence homology, the C1 and C2 domains of the family members are structurally similar to the two repetitive catalytic domains of phospholipase D (PLD). Moreover, some residues in the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) of the PLD superfamily are spatially conserved in the active site of PPK1. It is possible that the bacterial PPK1 family and the PLD family have a common ancestor and diverged early in evolution. In some bacteria, such as Pseudomonas aeruginosa, a second enzyme, PPK2, which is involved in the alternative pathway of polyphosphate synthesis, has been found. It can catalyze the synthesis of poly P from GTP or ATP, with a preference for Mn2+ over Mg2+. PPK2 shows no sequence similarity to PPK1 and belongs to a different superfamily
YRKLLVAPFTLRRRLLELIEREIEHAKAGKPARIIAKMNSLVDPEIIDALYRASQAGVKIDLIVRGICCL
RPGVPGLSENIRVRSIVGRFLEHSRIFYFHNGGEEEVYLGSADWMPRNLDRRVELLFPVEDPKLKARLIE
ILDLYLADNVKAWELQPDGRYTR
>gnl|CDD|197266 cd09169, PLDc_PPK1_C2_unchar, Catalytic C-terminal domain, second repeat, of uncharacterized prokaryotic polyphosphate kinases. Catalytic C-terminal domain, second repeat (C2 domain), of a group of uncharacterized prokaryotic polyphosphate kinases (Poly P kinase 1 or PPK1, EC 2.7.4.1). Inorganic polyphosphate (Poly P) plays an important role in bacterial stress responses and stationary-phase survival. PPK1 is the key enzyme responsible for the synthesis of Poly P in bacteria. It can catalyze the reversible conversion of the terminal-phosphate of ATP to Poly P. Therefore, PPK1 is essential for bacterial motility, quorum sensing, biofilm formation, and the production of virulence factors and may serve as an attractive antimicrobial drug target. Dimerization is crucial for the enzymatic activity of PPK1. Each PPK1 monomer includes four structural domains, the N-terminal (N) domain, the head (H) domain, and two closely related C-terminal (C1 and C2) domains. The N domain provides the upper binding interface for the adenine ring of the ATP. The H domain is involved in dimerization, while both the C1 and C2 domains contain residues crucial for catalytic activity. The intersection of the N, C1, and C2 domains forms a structural tunnel in which the PPK catalytic reactions are carried out. In spite of the lack of sequence homology, the C1 and C2 domains of PPK1 are structurally similar to the two repetitive catalytic domains of phospholipase D (PLD). Moreover, some residues in the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) of the PLD superfamily are spatially conserved in the active site of PPK1. It is possible that the bacterial PPK1 family and the PLD family have a common ancestor and diverged early in evolution
KHLLVAPTSLKNKILKLIDREIEKAKAGEPGYIFLKMNSLTDKDIIDKLIEASQAGVKIDMIVRGICCLI
PGVPGKTENIRVRSIVGRYLEHSRIYIFGQGEDAKIYISSADFMTRNTERRVEVAVPIYDPAIKARILEI
LDVMLSDNVKARELQPDGEYVK
>gnl|CDD|197267 cd09170, PLDc_Nuc, Catalytic domain of EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar proteins. Catalytic domain of an EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar proteins. Nuc is an endonuclease cleaving both single- and double-stranded DNA. It is the smallest known member of the phospholipase D (PLD, EC 3.1.4.4) superfamily that includes a diverse group of proteins with various catalytic functions. Most members of this superfamily have two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in a single polypeptide chain and both are required for catalytic activity. However, Nuc only has one copy of the HKD motif per subunit but form a functionally active homodimer (it is most likely also active in solution as a multimeric protein), which has a single active site at the dimer interface containing the HKD motifs from both subunits. Due to the lack of a distinct domain for DNA binding, Nuc cuts DNA non-specifically. It utilizes a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit
TVEVYFSPEGGARELILDVIDSARRSIDVAAYSFTSPPIARALIAAKKRGVDVRVVLDKSQAGGKYSALN
YLANAGIPVRIDDNYAIMHNKVMVIDGKTVITGSFNFTASAEKRNAENLLVIRNPPELAQQYLQEWQRRW
AQ
>gnl|CDD|197268 cd09171, PLDc_vPLD6_like, Catalytic domain of vertebrate phospholipase D6 and similar proteins. Catalytic domain of vertebrate phospholipase D6 (PLD6, EC 3.1.4.4), a homolog of the EDTA-resistant nuclease Nuc from Salmonella typhimurium, and similar proteins. PLD6 can selectively hydrolyze the terminal phosphodiester bond of phosphatidylcholine (PC) with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. It also catalyzes the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. PLD6 belongs to the phospholipase D (PLD) superfamily. Its monomer contains a short conserved sequence motif, H-x-K-x(4)-D (where x represents any amino acid residue), termed the HKD motif, which is essential in catalysis. PLD6 is more closely related to the nuclease Nuc than to other vertebrate phospholipases, which have two copies of the HKD motif in a single polypeptide chain. Like Nuc, PLD6 may utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from the HKD motif of one subunit to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit
CLFFPGETSLSKLLRYLLSARKSLDVCVFTITCDDLADAILDLHRRGVRVRIITDDDQMEDKGSDIGKLR
KAGIPVRTDLSSGHMHHKFAVIDGKILITGSFNWTRQAVTGNQENVLITNDPKLVKPFTEEFEKLW
>gnl|CDD|197269 cd09172, PLDc_Nuc_like_unchar1_1, Putative catalytic domain, repeat 1, of uncharacterized hypothetical proteins similar to Nuc, an endonuclease from Salmonella typhimurium. Putative catalytic domain, repeat 1, of uncharacterized hypothetical proteins, which show high sequence homology to the endonuclease from Salmonella typhimurium and vertebrate phospholipase D6. Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which characterizes the PLD superfamily and is essential for catalysis. Nuc and PLD6 utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. However, proteins in this subfamily have two HKD motifs in a single polypeptide chain
AWLSRELREALLAFLDEARSAGSSIRLAIYELDDPEIIDALKAAKDRGVRVRIILDDSSVTGDPTEESAA
ATLSKGPGALVKRRHSSGLMHNKFLVVDRKDGPNRVLTGSTNFTTSGLYGQSNNVLIFRNPAFAAAYLAY
WNTL
>gnl|CDD|197270 cd09173, PLDc_Nuc_like_unchar1_2, Putative catalytic domain, repeat 2, of uncharacterized hypothetical proteins similar to Nuc, an endonuclease from Salmonella typhimurium. Putative catalytic domain, repeat 2, of uncharacterized hypothetical proteins, which show high sequence homology to the endonuclease from Salmonella typhimurium and vertebrate phospholipase D6. Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which characterizes the PLD superfamily and is essential for catalysis. Nuc and PLD6 utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. However, proteins in this subfamily have two HKD motifs in a single polypeptide chain
FSPPPKGNADLALIAELVAKAKSSVLFALFDFSDGALLDALLAAADAGLFVRGLVDKRFGGRYYSAAADM
GGIDPVYPAALAPDEPEKFVGEPLLGVGDKLHHKFMVIDPFGDDPVVITGSHNFSGAANDNNDENLLVIR
DPAIADAYAIEFLRLYDHY
>gnl|CDD|197271 cd09174, PLDc_Nuc_like_unchar2, Putative catalytic domain of uncharacterized hypothetical proteins closely related to Nuc, an endonuclease from Salmonella typhimurium. Putative catalytic domain of uncharacterized hypothetical proteins, which show high sequence homology to the endonuclease from Salmonella typhimurium and vertebrate phospholipase D6. Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which characterizes the PLD superfamily and is essential for catalysis. Nuc and PLD6 utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. However, proteins in this subfamily have two HKD motifs in a single polypeptide chain
TEVLFDDIENRIIEEIKKAKFSIWIAVAWFTNKDIFNALKNKKKEGVNIQIIINDDDINKKDVLILDEDS
FEIYKLPGNGSRYGNLMHNKFCVIDFKTVITGSYNWTKNAEYNFENIIITDDRELAEQFAKEFIKL
>gnl|CDD|197272 cd09175, PLDc_Bfil, Catalytic domain of type IIs restriction endonuclease BfiI and similar proteins. Catalytic domain of a novel type IIs restriction endonuclease BfiI and similar proteins. Type II restriction endonucleases are components of restriction modification (RM) systems that protect bacteria and archaea against invading foreign DNA. They usually function as homodimers or homotetramers that cleave DNA at defined sites of 4 to 8 bp in length, and they require Mg2+, not ATP or GTP, for catalysis. Unlike all other restriction enzymes known to date, BfiI is unique in cleaving DNA at fixed positions downstream of an asymmetric sequence in the absence of Mg2+. BfiI consists of two discrete domains with distinct functions: an N-terminal catalytic domain with non-specific nuclease activity and dimerization function that is more closely related to Nuc, an EDTA-resistant nuclease from the phospholipase D (PLD) superfamily; and a C-terminal domain that specifically recognizes its target sequences, 5'-ACTGGG-3'. BfiI presumably evolved through domain fusion of a DNA recognition domain to the catalytic Nuc-like domain from the PLD superfamily. Most PLD enzymes have two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in a single polypeptide chain and both are required for catalytic activity. However, BfiI contains only one HKD motif per protein chain and forms a functionally active homodimer which has two DNA-binding surfaces located at the C-terminal domains but only one active site, located at the dimer interface between the two N-terminal catalytic domains that contain the two HKD motifs from both subunits. BfiI utilizes a single active site to cut both DNA strands, which represents a novel mechanism for the scission of double-stranded DNA. It uses a histidine residue from the HKD motif in one subunit as the nucleophile for the cleavage of the target phosphodiester bond in both of the anti-parallel DNA strands, while the symmetrically-related histidine residue from the HKD motif of the opposite subunit acts as the proton donor/acceptor during both strand-scission events
EFTLHPNVYATGNSKGLINLLERVWVKEHTSGEGTLYIISGFANYNGGVRFYPVFTEHIHKGGKVVAIFG
GSTSQRLSSKQVVEELLNCGAEVHIVNRKRLLHAKSYGTKTNSGESLVVTSGNFTGPGMSQNVEAAVLLD
SNTTQNMGFSWEDMFNNMLSQ
>gnl|CDD|197273 cd09176, PLDc_unchar6, Putative catalytic domain of uncharacterized hypothetical proteins with one or two copies of the HKD motif. Putative catalytic domain of uncharacterized hypothetical proteins with similarity to phospholipase D (PLD, EC 3.1.4.4). PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze transphosphatidylation of phospholipids to acceptor alcohols. Members of this subfamily contain one or two copies of the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily
RGLGGLIREAAKRLLVISPFIDLGNALKELAEALPAKIRVLISRSEELAALGASDLEGFDLLLALDDAEI
LVLRGLHAKLYIAETGDGTHVIIGSANATEAAAAGNNVEFGVLL
>gnl|CDD|197274 cd09177, PLDc_RE_NgoFVII, Putative catalytic domain of type II restriction enzyme NgoFVII and similar proteins. Putative catalytic domain of type II restriction enzyme NgoFVII (EC 3.1.21.4), which shows high sequence similarity to type IIs restriction endonuclease BfiI. Type II restriction endonucleases are components of restriction modification (RM) systems that protect bacteria and archaea against invading foreign DNA. They usually function as homodimers or homotetramers that cleave DNA at defined sites of 4 to 8 bp in length, and they require Mg2+, not ATP or GTP, for catalysis. The prototype of this subfamily is the NgoFVII restriction endonuclease from Neisseria gonorrhoeae. It plays an essential role in the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. It recognizes the double-stranded sequence GCSGC and cleaves after G-4. Members of this subfamily contain one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) per protein chain and have been classified into the phospholipase D (PLD, EC 3.1.4.4) superfamily
LNKVFTELLKQSDEVEIAVGYVSNDSLQELDKLVEEHNISTIKLTIGMYFIEGMPELQYNTAIRLNDKWQ
EEGIGGVYIVPFFKYHGKLYLFKKDGKPFSAIIGSANLGAIWLTASTRRQYETSVILEDISEPAEIQLHI
EKL
>gnl|CDD|197275 cd09178, PLDc_N_Snf2_like, N-terminal putative catalytic domain of uncharacterized HKD family nucleases fused to putative helicases from the Snf2-like family. N-terminal putative catalytic domain of uncharacterized archaeal and prokaryotic HKD family nucleases fused to putative helicases from the Snf2-like family, which belong to the DNA/RNA helicase superfamily II (SF2). Although Snf2-like family enzymes do not possess helicase activity, they contain a helicase-like region, where seven helicase-related sequence motifs are found, similar to those in DEAD/DEAH box helicases, which represent the biggest family within the SF2 superfamily. In addition to the helicase-like region, members of this family also contain an N-terminal putative catalytic domain with one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), and have been classified as members of the phospholipase D (PLD, EC 3.1.4.4) superfamily
IIDNREGKTLADALKELLKDSDRLDIAVGYFYLSGFRLLKEELENFEKLRILIGIELIKEGKVEIRVYTK
GFLHAKAYLFDGPDNDNGPGTAIVGSSNFTKAGLTGNLELNVEVKDRDDVEELKEWFEELWEDS
>gnl|CDD|197276 cd09179, PLDc_N_DEXD_a, N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. All members of this subfamily are uncharacterized. Other characterized members of the superfamily that have a related domain architecture (containing a DEAD/DEAH box helicase domain), include the DNA/RNA helicase superfamily II (SF2) and Res-subunit of type III restriction endonucleases. In addition to the helicase-like region, members of this subfamily also contain one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in the N-terminal putative catalytic domain. The HKD motif characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily
TEYSSDRDDIVEDFYIPALSEAVSYDRAVGYFSSSSLALAAAGLEIFIKNGGKMRLICSPELSPEDIEAI
KAGYDLREELILRLLLEELEELEDLLERERLKLLAWLIANGRLEIKVAFPKNEGAGIFHEKAGIFTDADG
NKVAFSGSANETASAWKRNYESIDVFRSWDDGDAERVQWKEEEFEALWNN
>gnl|CDD|197277 cd09180, PLDc_N_DEXD_b, N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. All members of this subfamily are uncharacterized. Other characterized members of the superfamily that have a related domain architecture (containing a DEAD/DEAH box helicase domain), include the DNA/RNA helicase superfamily II (SF2) and Res-subunit of type III restriction endonucleases. In addition to the helicase-like region, members of this subfamily also contain one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in the N-terminal putative catalytic domain. The HKD motif characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. A few family members contain additional domains, like a C-terminal peptidase S24-like domain
DKLLSELKNEMETADSVDFIVSFISESGIQLLIPELEELINKGVPIRIITSTYLGITEPKALRELADYDN
VEVKIYNNIKSESFHAKAYLFERETGYSSAIIGSSNLSQSALTTGIEWNVRITTDNNPDLVDQIKHEFEK
LW
>gnl|CDD|197278 cd09181, PLDc_FAM83A_N, N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence similarity 83A. N-terminal phospholipase D (PLD)-like domain of the uncharacterized protein, Family with sequence similarity 83A (FAM83A), also known as tumor antigen BJ-TSA-9. FAM83A or BJ-TSA-9 is a novel tumor-specific gene highly expressed in human lung adenocarcinoma. Due to this specific expression pattern, it may serve as a biomarker for lung cancer, especially in the early detection of micrometastasis for lung adenocarcinoma patients. Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are most unlikely to carry PLD activity
GHRLDLSHNESARLATDALLDGGLDEYHQVLRKEGEVDFLSSVEKQYIMENAREPSYGSDRTLSTSADQV
GSSSPSLQSETYFPVASESSEPVLLHDWSSAEVKPYLKEKSSATVYFQTVKASNMRDLIRRCIRKTTQVL
AIVMDVFTDVEIFCDLLEAANKRNVFVYLLLDHGNLSLFQEMCEKLQINDSHFKNISVRSVEGDTYCAKS
GRKFTGQIREKFIISDWREVLSGSYSFTWLSGQVHRNLLVKFKGSAVELFDEEFRHLYASSKPVPG
>gnl|CDD|197279 cd09182, PLDc_FAM83B_N, N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence similarity 83B. N-terminal phospholipase D (PLD)-like domain of the uncharacterized protein, Family with sequence similarity 83B (FAM83B). Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are most unlikely to carry PLD activity. The N-terminus of FAM83B shows high homology to other FAM83 family members, indicating that FAM83B might have arisen early in vertebrate evolution by duplication of a gene in the FAM83 family
DNYIQPHYKEWYRLAIDALIEGGLEAYQEFLRAERISDFLSEEEILYILENVEKPPQETDESEDKRTDDT
ASSGTYWPAESDVEAPNLDLGWPYVMLEAGGTSIDLLFHPPRANTPTIKEVIRKQIQEARQVIAIAMDVF
TDVDIFKEVVEASTRGVAVYILLDHSHFASFLTMTEKQGIQIQRLRNIRVRTVKGQDYQCKSGAKFHGAM
EQKFLLVDCQKVLYGSYSYMWSFEKIHLSMVQVITGQLVESYDEEFRTLYARSAVP
>gnl|CDD|197280 cd09183, PLDc_FAM83C_N, N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence similarity 83C. N-terminal phospholipase D (PLD)-like domain of the uncharacterized protein, Family with sequence similarity 83C (FAM83C). Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are most unlikely to carry PLD activity. The N-terminus of FAM83C shows high homology to other FAM83 family members, indicating that FAM83C might have arisen early in vertebrate evolution by duplication of a gene in the FAM83 family
SSPLVLNHNETARLATDALLERGEKAYLQVLQEEKELPFLSTLDIDYITNSVAINGKANHAIVSELDGTN
DIDEDSLPSELTSGTYFPMMSDFDPPDLELGWPEIPLATKASPTEAQIFFQRDKANNIKDLIRSLISMAK
TVIAIVMDLFTDVDILCDLMEASNKRRVPVYLLLDEENLGHFLEMCEKLDLNKTSLPNMRIRSVCGDTYC
TKSGKKFTGQVLEKFLLIDCEQVVAGSYSFTWLSSQVHSNLVTHFRGNIVEEFDREFRCLYADS
>gnl|CDD|197281 cd09184, PLDc_FAM83D_N, N-terminal phospholipase D-like domain of the protein, Family with sequence similarity 83D. N-terminal phospholipase D (PLD)-like domain of the protein Family with sequence similarity 83D (FAM83D), also known as spindle protein CHICA. CHICA is a cell-cycle-regulated spindle component, which localizes to the mitotic spindle and is both upregulated and phosphorylated during mitosis. CHICA is required to localize the chromokinesin Kid to the mitotic spindle and serves as a novel interaction partner of Kid, which is required for the generation of polar ejection forces and chromosome congression. Since the N-terminal PLD-like domain of FAM83D shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83D may share a similar three-dimensional fold with PLD enzymes, but is unlikely to carry PLD activity
PPNPPELYNEAHRLALEELVAGGPEAFRGFLKRERLPNFLSEDEVRAILRAAVVPKTISINGDDSELSQS
ASLDCSSVTYFPERSDIEPPVLELGWPAFTTGSYRGVTRVEAHFQPSYGDCIYGCKEAARRQIRSAREVI
ALVMDSFTDLDIFRDLREACRKRRVPVYILLDQSSVSHFLQMCKNLGVHLEQEKLMRVRTITGNTYYTRS
GAKIIGKVHEKFMLIDGIKVATGSYSFTWTDGKLNSSNLLILSGQVVEKFDLEFRILYAQS
>gnl|CDD|197282 cd09186, PLDc_FAM83F_N, N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence similarity 83F. N-terminal phospholipase D (PLD)-like domain of the uncharacterized protein, Family with sequence similarity 83F (FAM83F). Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are most unlikely to carry PLD activity. The N-terminus of FAM83F shows high homology to other FAM83 family members, indicating that FAM83F might have arisen early in vertebrate evolution by duplication of a gene in the FAM83 family
EAKAEFYYSEEQRAALEQLLRNGEGAYRERLKKERLKDFLSSQEIQALRETWQEYDSDSDTCCSRSPHDT
PEDSGVSLAYWPTMSDTEVPPLDLGWTDNGFYRGVSRVSLFTHPPKEENSPHLKEVVRKMIQQAQKLIAV
VMDLFTDLDIFQDIVDAASKRRVPVYIILDENGVKHFLEMCSRLQLSDFHIRNIRVRSVTGSGFYMSFGK
IPGTLCSKFLMVDGEKVATGSYSFTWSSSRMDRNTLLVLTGQVVEFFDNEFRELYAIS
>gnl|CDD|197283 cd09187, PLDc_FAM83G_N, N-terminal phospholipase D-like domain of the uncharacterized protein Family with sequence similarity 83G. N-terminal phospholipase D (PLD)-like domain of the uncharacterized protein, Family with sequence similarity 83G (FAM83G). Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are most unlikely to carry PLD activity. The N-terminus of FAM83G shows high homology to other FAM83 family members, indicating that FAM83G might have arisen early in vertebrate evolution by duplication of a gene in the FAM83 family
ESKAEFFYSEEQRLALEALIARGRDAFYEVLKDENIRDFLSELELKRILQRLEAYDPGSEHQRPEGPGNL
TPGSAEDEQDGAPSLEYWPDRSDRSIPQLDLGWPEAIAYRGVTRATVYMQPPVEGQAHIKEVVRKMIAQA
QKVIAVVMDMFTDVDIFRDLLDAGFKRKVPVYIILDETNVKYFLQMCERAQMHRGHLKNLRVRSCGGTEF
FTRSATKFKGSLGQKFMFVDGDRAICGSYSFTWSASRTDRNLITVLSGQVVETFDRQFQDLYLMS
>gnl|CDD|197284 cd09188, PLDc_FAM83H_N, N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence similarity 83H. N-terminal phospholipase D (PLD)-like domain of the protein, Family with sequence similarity 83H (FAM83H) on chromosome 8q24.3, which localizes in the intracellular environment and is associated with vesicles, can be regulated by kinases, and plays important roles during ameloblast differentiation and enamel matrix calcification. The gene encoding protein FAM83H is the first gene involved in the etiology of amelogenesis imperfecta (AI), that encodes a non-secreted protein due to the absence of a signal peptide. Defects in gene FAM83H cause autosomal dominant hypocalcified amelogenesis imperfecta (ADHCAI). Since the N-terminal PLD-like domain of FAM83H shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83H may share a similar three-dimensional fold with PLD enzymes, but is most unlikely to carry PLD activity
PNYLPPHYKEYYRLAIDALAEDGIEGYERFLAEEGVPDFLCPSEVEHIKSTLQTPQYAGQEPEYLPYGDI
DQDGSSGTYWPMNSDLAAPELDLGWPMQFGFQGTEVTTLVQPPPPDNPSIKEEARRMIRSAQQVIAVVMD
IFTDVDILSELLEAAARRVPVYILLDEMNAQLFLDMAAKCRVNLNYVEFLRVRTVSGPTYFCRTGKSFKG
HVKEKFLLVDCRVVLSGNYSFMWSFEKIHRSIAHIFQGELVASFDEEFRILFAQS
>gnl|CDD|197285 cd09189, PLDc_DNaseII_alpha_1, Catalytic domain, repeat 1, of Deoxyribonuclease II alpha and similar proteins. Catalytic domain, repeat 1, of Deoxyribonuclease II alpha (DNase II alpha, EC 3.1.22.1) and similar proteins. DNase II is a monomeric nuclease that contains two copies of a variant HKD motif, where the aspartic acid residue is not conserved. The HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. The catalytic center of DNase II is formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. Members of this family are mainly found in metazoans, and vertebrate proteins have been further classified into DNase II alpha and beta. DNase II alpha is an acidic endonuclease found in lysosomes, nuclei, and various secretions. It plays a critical role in the degradation of nuclear DNA expelled from erythroid precursor cells, as well as in the degradation of the apoptotic DNA after macrophages engulf them. It cleaves double-stranded DNA to short 3'-phosphoryl oligonucleotides, rather than 3'-hydroxyl groups, and functions optimally at acidic pH in the absence of divalent metal ion cofactors
SAISCYGDQGQAVDWFYVYKLPKEDGMEPQEEGDRYLYLDKSSGGWSNGQGLVNSTTGAVGRTVGQLYSQ
GKNTERAYILYNDQPPTVSLTDSGSSRGHTKGVLLLDKHQGFWLVHSTPHFPPPAKEGQYYWPHSALING
QNFLCVTYPLEQFQTIGKQLQY
>gnl|CDD|197286 cd09190, PLDc_DNaseII_beta_1, Catalytic domain, repeat 1, of Deoxyribonuclease II beta and similar proteins. Catalytic domain, repeat 1, of Deoxyribonuclease II beta (DNase II beta, EC 3.1.22.1), also known as DNase II-like acid DNase (DLAD), and similar proteins. DNase II is a monomeric nuclease that contains two copies of a variant HKD motif, where the aspartic acid residue is not conserved. The HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. The catalytic center of DNase II is formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. Members of this family are mainly found in metazoans, and vertebrate proteins have been further classified into DNase II alpha and beta. DNase II beta, or DLAD, is a novel mammalian divalent cation-independent endonuclease with homology to DNase II alpha. It is highly expressed in the eye lens and in salivary glands and is responsible for the degradation of nuclear DNA during lens cell differentiation. DLAD mainly exists as a cytoplasmic protein and cleaves DNA to produce 3'-phosphoryl/5'-hydroxyl ends. Like DNase II alpha, DLAD is active under acidic conditions with maximum activity at pH 5.2. Aurintricarboxylic acid and Zn2+ are effective inhibitors of DLAD activity. Mice deficient in DLAD develop cataracts as they are unable to degrade DNA during differentiation of the lens cells
AAEISCRNEEGEAVDWFVFYKLPKRKNGGSTGSGLEYLYLDSTTQSWQKSKYLVNTTKSALGQTLQQLYE
AYASKSNNTVYAIYNDAVPKPVNISRKYGHTKGLLLWDRSQGFWLIHSVPHFPPFPEDGYGYPSTGKRNG
QTAICITFSYNQFEEIDSQLLYCNP
>gnl|CDD|197287 cd09191, PLDc_DNaseII_alpha_2, Catalytic domain, repeat 2, of Deoxyribonuclease II alpha and similar proteins. Catalytic domain, repeat 2, of Deoxyribonuclease II alpha (DNase II alpha, EC 3.1.22.1) and similar proteins. DNase II is a monomeric nuclease that contains two copies of a variant HKD motif, where the aspartic acid residue is not conserved. The HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. The catalytic center of DNase II is formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. Members of this family are mainly found in metazoans, and vertebrate proteins have been further classified into DNase II alpha and beta. DNase II alpha is an acidic endonuclease found in lysosomes, nuclei, and various secretions. It plays a critical role in the degradation of nuclear DNA expelled from erythroid precursor cells, as well as in the degradation of the apoptotic DNA after macrophages engulf them. It cleaves double-stranded DNA to short 3'-phosphoryl oligonucleotides, rather than 3'-hydroxyl groups, and functions optimally at acidic pH in the absence of divalent metal ion cofactors
RPWNRSVTLTSAGGTNFISFAKGASFGDDLYSGWVAPALQSDLLVQFWVRSTGVLPSNCSLGWKVLDVTR
INFPKTSSFKSSQDHSKWCVSTKAGWVCVGDMNRNMAEEQRGGGTVCLRDPAVWKAFRTLVVDYEDC
>gnl|CDD|197288 cd09192, PLDc_DNaseII_beta_2, Catalytic domain, repeat 2, of Deoxyribonuclease II beta and similar proteins. Catalytic domain, repeat 2, of Deoxyribonuclease II beta (DNase II beta, EC 3.1.22.1), also known as DNase II-like acid DNase (DLAD), and similar proteins. DNase II is a monomeric nuclease that contains two copies of a variant HKD motif, where the aspartic acid residue is not conserved. The HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. The catalytic center of DNase II is formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. Members of this family are mainly found in metazoans, and vertebrate proteins have been further classified into DNase II alpha and beta. DNase II beta, or DLAD, is a novel mammalian divalent cation-independent endonuclease with homology to DNase II alpha. It is highly expressed in the eye lens and in salivary glands and is responsible for the degradation of nuclear DNA during lens cell differentiation. DLAD mainly exists as a cytoplasmic protein and cleaves DNA to produce 3'-phosphoryl/5'-hydroxyl ends. Like DNase II alpha, DLAD is active under acidic conditions with maximum activity at pH 5.2. Aurintricarboxylic acid and Zn2+ are effective inhibitors of DLAD activity. Mice deficient in DLAD develop cataracts as they are unable to degrade DNA during differentiation of the lens cells
IPERRLAKLQSAQGEKFLHFAKSKYFVDDIFTAWVAQKLKTDLLVETWQHKGQELPSNCSLPYHVYNINR
IGLPGLSTFSSRYDHSKWCVSQKFKDQWTCIGDLNRSPEQAWRSGGFICTQNKHIYKAFRKLVLYYKSC
>gnl|CDD|197289 cd09193, PLDc_mTdp1_1, Catalytic domain, repeat 1, of metazoan tyrosyl-DNA phosphodiesterase. Catalytic domain, repeat 1, of metazoan tyrosyl-DNA phosphodiesterase (Tdp1, EC 3.1.4.-). Human Tdp1 (hTdp1) acts as an important DNA repair enzyme with a preference for single-stranded or blunt-ended duplex oligonucleotides. It can remove stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of a phosphodiester bond between a tyrosine side chain and a DNA 3'-phosphate. It is therefore a potential molecular target for new anti-cancer drugs. hTdp1 has been shown to associate with additional proteins, such as XRCC1, to form a multi-enzyme complex. These additional proteins may be involved in recognizing 3'-phoshotyrosyl DNA in vivo. hTdp1 is a monomeric protein containing two copies of a variant HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which consists of the highly conserved histidine and lysine residues, but lacks the aspartate residue that is well conserved in other phospholipase D (PLD, EC 3.1.4.4) enzymes. Like other PLD enzymes, hTdp1 may utilize a common two-step general acid/base catalytic mechanism, involving a DNA-enzyme intermediate to cleave phosphodiester bonds. A single active site involved in phosphatidyl group transfer would be formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way
PYFRFYTTKVGGIDTHYNPSSLSFKEILDPSLGELVSSLQFNFMFDIPWLVEQYPPELRNKPLTIVHGEK
REPKAELAQAKPYPNVTFCQAKLPIPFGTHHTKMMILLYEDGSLRVVISTANLIEDDWEQKTQGIWISPL
LPRLSEDANSDGESPTGFKADLLEYLSSY
>gnl|CDD|197290 cd09194, PLDc_yTdp1_1, Catalytic domain, repeat 1, of yeast tyrosyl-DNA phosphodiesterase. Catalytic domain, repeat 1, of yeast tyrosyl-DNA phosphodiesterase (yTdp1, EC 3.1.4.-). yTdp1 is involved in the repair of topoisomerase I DNA lesions by hydrolyzing the topoisomerase from the 3'-end of the DNA during double-strand break repair. Unlike human Tdp1 whose substrate-binding pocket can accommodate a fairly large topoisomerase I peptide fragment, yTdp1 has a preference for substrates containing one to four amino acid residues. The monomeric yTdp1 contains two copies of a variant HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which consists of the highly conserved histidine and lysine residues, but lacks the aspartate residue that is well conserved in other phospholipase D (PLD, EC 3.1.4.4) enzymes. Like other PLD enzymes, yTdp1 may utilize a common two-step general acid/base catalytic mechanism, involving a DNA-enzyme intermediate to cleave phosphodiester bonds. A single active site involved in phosphatidyl group transfer would be formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way
SPFKLVKSSAYDEEEEVNVDTITLKDLLGDPDLKETWLFNFQYDLDFLLDQFHPNVNHVKITIVAGSGTI
EPPTRRRIKLNKIYPNVKLIEAYMPPPFGTHHSKMMINFYQDDSCQIVIPSANLTEMDTNLPQQVVWKSP
RLPLKSETVPGSGSRFKRDLLAYLKS
>gnl|CDD|197291 cd09195, PLDc_mTdp1_2, Catalytic domain, repeat 2, of metazoan tyrosyl-DNA phosphodiesterase. Catalytic domain, repeat 2, of metazoan tyrosyl-DNA phosphodiesterase (Tdp1, EC 3.1.4.-). Human Tdp1 (hTdp1) acts as an important DNA repair enzyme with a preference for single-stranded or blunt-ended duplex oligonucleotides. It can remove stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of a phosphodiester bond between a tyrosine side chain and a DNA 3'-phosphate. It is therefore a potential molecular target for new anti-cancer drugs. hTdp1 has been shown to associate with additional proteins, such as XRCC1, to form a multi-enzyme complex. These additional proteins may be involved in recognizing 3'-phoshotyrosyl DNA in vivo. hTdp1 is a monomeric protein containing two copies of a variant HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which consists of the highly conserved histidine and lysine residues, but lacks the aspartate residue that is well conserved in other phospholipase D (PLD, EC 3.1.4.4) enzymes. Like other PLD enzymes, hTdp1 may utilize a common two-step general acid/base catalytic mechanism, involving a DNA-enzyme intermediate to cleave phosphodiester bonds. A single active site involved in phosphatidyl group transfer would be formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way
VFLIGSVPGRHTGSSLDKWGHLRLRKLLKEHASLPPVAESWPVIAQFSSIGSLGPDPQKWLCSEFLESLS
GLGKTSGKSSPPLKLIYPSVENVRNSLEGYPAGGCLPYSKQTAEKQPWLKSYLHKWKADKRGRSRAMPHI
KTYTRISPDLSKIAWFLLTSANLSKAAWGALEKNGTQLMIRSYEAGVLFLP
>gnl|CDD|197292 cd09196, PLDc_yTdp1_2, Catalytic domain, repeat 2, of yeast tyrosyl-DNA phosphodiesterase. Catalytic domain, repeat 2, of yeast tyrosyl-DNA phosphodiesterase (yTdp1, EC 3.1.4.-). yTdp1 is involved in the repair of topoisomerase I DNA lesions by hydrolyzing the topoisomerase from the 3'-end of the DNA during double-strand break repair. Unlike human Tdp1 whose substrate-binding pocket can accommodate a fairly large topoisomerase I peptide fragment, yTdp1 has a preference for substrates containing one to four amino acid residues. The monomeric yTdp1 contains two copies of a variant HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which consists of the highly conserved histidine and lysine residues, but lacks the aspartate residue that is well conserved in other phospholipase D (PLD, EC 3.1.4.4) enzymes. Like other PLD enzymes, yTdp1 may utilize a common two-step general acid/base catalytic mechanism, involving a DNA-enzyme intermediate to cleave phosphodiester bonds. A single active site involved in phosphatidyl group transfer would be formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way
GYGKLYQVLRRNNLLLDNSDGDKHHNYLCQVSSIGYPFSRRKDNPANLFTHLLIPLLFGDWEKPFGELEP
GIELLKSHQKEHNYKPYIVYPTVEEIANSPVGWLSGGWFHFKYTRSDTHKNQYEQLRKNPYLYKWNSSDT
TKGRERVPPHVKFYMCDNTDNWFKTLDWCLFTSANLSKQAWGTPLSYKPRNYELGVLYTS
>gnl|CDD|197293 cd09197, PLDc_pPLDalpha_1, Catalytic domain, repeat 1, of plant alpha-type phospholipase D. Catalytic domain, repeat 1, of plant alpha-type phospholipase D (PLDalpha, EC 3.1.4.4). Plant PLDalpha is a phosphatidylinositol 4,5-bisphosphate (PIP2)-independent PLD that possesses a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and require millimolar calcium for optimal activity. The C2 domain is unique to plant PLDs and is not present in animal or fungal PLDs. Like other PLD enzymes, the monomer of plant PLDalpha consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDalpha may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
GGQKYEPTRCWEDVFDAIMNAKHLIYITGWSVYCEIVLVRDSRRPKPGGDLTLGELLKKKASEGVRVLML
VWDDRTSVEFLKKDGLMATHDEETEAFFQDSDVHCFLCPRNPDDGGSKVQGLQISTMFTHHQKIVVVDSP
MPGSDSGRRRIVSFVGGIDLCDGRYDNPFHSLFRTLDD
>gnl|CDD|197294 cd09198, PLDc_pPLDbeta_1, Catalytic domain, repeat 1, of plant beta-type phospholipase D. Catalytic domain, repeat 1, of plant beta-type phospholipase D (PLDbeta, EC 3.1.4.4). Plant PLDbeta is a phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent PLD that possesses a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and requires nanomolar calcium and cytosolic factors for optimal activity. The C2 domain is unique to plant PLDs and is not present in animal or fungal PLDs. Sequence analysis shows that plant PLDbeta is evolutionarily divergent from alpha-type plant PLD, and plant PLDbeta is more closely related to mammalian and yeast PLDs than to plant PLDalpha. Like other PLD enzymes, the monomer of plant PLDbeta consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDbeta may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
GGKVYEHGKCWEDMCDAIREARRLIYITGWSVYHKVKLIRDKLRPVPPGGELTLGELLKSKSQEGVRVLL
LVWDDKTSHSILGYKTDGVMATHDEETKRFFKHSSVQCVLAPRYAGKKHSWFKQQVVGTLYTHHQKNVIV
DADAGGNRRKITAFIGGLDLCDGRYDTPQHPLFRTLETIH
>gnl|CDD|197295 cd09199, PLDc_pPLDalpha_2, Catalytic domain, repeat 2, of plant alpha-type phospholipase D. Catalytic domain, repeat 2, of plant alpha-type phospholipase D (PLDalpha, EC 3.1.4.4). Plant PLDalpha is a phosphatidylinositol 4,5-bisphosphate (PIP2)-independent PLD that possesses a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and require millimolar calcium for optimal activity. The C2 domain is unique to plant PLDs and is not present in animal or fungal PLDs. Like other PLD enzymes, the monomer of plant PLDalpha consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDalpha may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
KDNIIDRSIQDAYINAIRRAKDFIYIENQYFLGSSYAWSPDGIKPQDIGALHLIPKELSLKIVSKIEAGE
RFRVYVVVPMWPEGIPESGSVQAILDWQKRTMEMMYTDIAQALRAQGIDDEDPRDYLTFFCLANREVKKE
GEYEPAEKPEEDSDYARAQEARRFMIYVHTKMMIVDDEYIIIGSANINQRSMDGARDSEIAMGAYQPHHL
S
>gnl|CDD|197296 cd09200, PLDc_pPLDbeta_2, Catalytic domain, repeat 2, of plant beta-type phospholipase D. Catalytic domain, repeat 2, of plant beta-type phospholipase D (PLDbeta, EC 3.1.4.4). Plant PLDbeta is a phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent PLD that possesses a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and requires nanomolar calcium and cytosolic factors for optimal activity. The C2 domain is unique to plant PLDs and is not present in animal or fungal PLDs. Sequence analysis shows that plant PLDbeta is evolutionarily divergent from alpha-type plant PLD, and plant PLDbeta is more closely related to mammalian and yeast PLDs than to plant PLDalpha. Like other PLD enzymes, the monomer of plant PLDbeta consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDbeta may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
KNVLIDMSIHTAYVKAIRSAQHFIYIENQYFIGSSYNWPAYKDAGADNLIPMEIALKIAEKIRAGERFAV
YIVIPMWPEGVPTGAAVQEILYWQHQTMQMMYETIAKALVDTGLEGAFSPQDYLNFYCLGNREMKDGIEP
SPTNSPRQNSTQGRSQKSRRFMIYVHSKGMIVDDEYVIIGSANINQRSMDGSRDTEIAMGAYQPHHTWAR
K
>gnl|CDD|197297 cd09203, PLDc_N_DEXD_b1, N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. All members of this subfamily are uncharacterized. Other characterized members of the superfamily that have a related domain architecture (containing a DEAD/DEAH box helicase domain), include the DNA/RNA helicase superfamily II (SF2) and Res-subunit of type III restriction endonucleases. In addition to the helicase-like region, members of this subfamily also contain one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in the N-terminal putative catalytic domain. The HKD motif characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily
PSLGSELRKEIASADRIDLLVSFIKWSGLRLLLDALKEFTDRGIPLRVITTTYMGATDAKALEALAELPG
TEVKVSYDTRRTRLHAKAYLFHRNTGFSTAYIGSSNLSKAALTSGLEWNVKVTEVETPAVIDKFRATFES
YWN
>gnl|CDD|197298 cd09204, PLDc_N_DEXD_b2, N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. All members of this subfamily are uncharacterized. Other characterized members of the superfamily that have a related domain architecture (containing a DEAD/DEAH box helicase domain), include the DNA/RNA helicase superfamily II (SF2) and Res-subunit of type III restriction endonucleases. In addition to the helicase-like region, members of this subfamily also contain one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in the N-terminal putative catalytic domain. The HKD motif characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily
SKVLNELRDELKTCKSFTFSVAFITESGLALLKQVLKDLEERGIKGRILTSTYLNFNEPKAFRELLKLPN
IEVRIYDEDEGFHAKGYIFEHEDYYTIIVGSSNLTQSALKSNYEWNLKVSSTENGDLVEQVLEEFERLW
>gnl|CDD|197299 cd09205, PLDc_N_DEXD_b3, N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. All members of this subfamily are uncharacterized. Other characterized members of the superfamily that have a related domain architecture (containing a DEAD/DEAH box helicase domain), include the DNA/RNA helicase superfamily II (SF2) and Res-subunit of type III restriction endonucleases. In addition to the helicase-like region, members of this subfamily also contain one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in the N-terminal putative catalytic domain. The HKD motif characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. A few family members contain additional domains, like a C-terminal peptidase S24-like domain
DPLLPHLKEAIARATEIDIAVSFVMESGVDLLLPALKEALSRGARIRILTGDYLDITQPEALRRLLDLLG
DGIEIRVFESGGRSFHPKAYLFEREDGGGAAFVGSSNLSKSALTDGIEWNLRIDRSADPDAFDEAKEAFE
KLF
>gnl|CDD|187741 cd09208, Lumazine_synthase-II, lumazine synthase (6,7-dimethyl-8-ribityllumazine synthase, LS), catalyzes the penultimate step in the biosynthesis of riboflavin (vitamin B2); type-II. Type-II LS also known as RibH2, catalyzes the penultimate step in the biosynthesis of riboflavin in plants and microorganisms. LS catalyses the formation of 6,7-dimethyl-8-ribityllumazine by the condensation of 5-amino-6-ribitylamino- 2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy- 2-butanone-4-phosphate. Subsequently, the lumazine intermediate dismutates yielding riboflavin and 5-amino-6-ribitylamino- 2,4(1H,3H)-pyrimidinedione, in a reaction catalyzed by riboflavin synthase (RS); RS belongs to a different family of the Lumazine-synthase-like superfamily. Riboflavin is the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) which are essential cofactors for the catalysis of a wide range of redox reactions. These cofactors are also involved in many other processes involving DNA repair, circadian time-keeping, light sensing, and bioluminescence. Riboflavin is biosynthesized in plants, fungi and certain microorganisms; as animals lack the necessary enzymes to produce this vitamin, they acquire it from dietary sources. Type II LSs are distinct from type-I LS not only in protein sequence, but in that they exhibit different quaternary assemblies; type-II LSs form decamers (dimers of pentamers). The pathogen Brucella spp. have both a type-I LS and a type-II LS called RibH1 and RibH2, respectively. RibH1/type-I LS appears to be a functional LS in Brucella spp., whereas RibH2/type-II LS has much lower catalytic activity as LS and may be regulated by a riboswitch that senses FMN, suggesting that the type-II LSs may have evolved into very poor catalysts or, that they may harbor a new, as-yet-unknown function
FRIAFIQARWHADIVDQARKGFEAEMAAKGGASDEVDIFDVPGAFEIPLHAKRLARTGRYAAIVGAALVV
DGGIYRHEFVAQAVIDGLMRVQLETEVPVFSVVLTPHHFHEHKEHHEFFFAHFKKKGVEVAHACLAI
>gnl|CDD|187742 cd09209, Lumazine_synthase-I, lumazine synthase (6,7-dimethyl-8-ribityllumazine synthase, LS), catalyzes the penultimate step in the biosynthesis of riboflavin (vitamin B2); type-I. Type-I LS, also known as RibH1, catalyzes the penultimate step in the biosynthesis of riboflavin in plants and microorganisms. LS catalyse the formation of 6,7-dimethyl-8-ribityllumazine by the condensation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy- 2-butanone-4-phosphate. Subsequently, the lumazine intermediate dismutates to yield riboflavin and 5-amino-6-ribitylamino- 2,4(1H,3H)-pyrimidinedione, in a reaction catalyzed by riboflavin synthase synthase (RS); RS belongs to a different family of the Lumazine-synthase-like superfamily. Riboflavin is the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) which are essential cofactors for the catalysis of a wide range of redox reactions. These cofactors are also involved in many other processes involving DNA repair, circadian time-keeping, light sensing, and bioluminescence. Riboflavin is biosynthesized in plants, fungi and certain microorganisms; as animals lack the necessary enzymes to produce this vitamin, they acquire it from dietary sources. Type II LSs are distinct from type-I LS not only in protein sequence, but in that they exhibit different quaternary assemblies; type-I LSs form pentamers. The pathogen Brucella spp. encode both a Type-I LS and a Type-II LS called RibH1 and RibH2, respectively. RibH1/type-I LS appears to be the functional LS in Brucella spp., whereas RibH2/type-II LS has much lower catalytic activity as LS. The pathogen Brucella spp. have both a type-I LS and a type-II LS called RibH1 and RibH2, respectively. RibH1/type-I LS appears to be a functional LS in Brucella spp., whereas RibH2/type-II LS has much lower catalytic activity as LS
IAIVVSRFNEEITDALLEGALDALKRHGVKEENIDVVRVPGAFEIPLAAKRLARSGKYDAIIALGCVIRG
ETPHFDYVCNEVTRGLMRLSLETGVPVIFGVLTTDNEEQALERAGGKAGNKGAEAALAALEMA
>gnl|CDD|187743 cd09210, Riboflavin_synthase_archaeal, archaeal riboflavin synthase (RS); involved in the biosynthesis pathway of riboflavin (vitamin B2). Archaeal RSs are homopentamers catalyzing the formation of riboflavin from 6,7-dimethyl-8-ribityllumazine in riboflavin biosynthesis. Divalent metal ions, preferably manganese or magnesium, are needed for maximum activity. Riboflavin serves as the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), essential cofactors for several oxidoreductases that are indispensable in most living cells. In the final steps of the riboflavin biosynthetic pathway, lumazine synthase (6,7-dimethyl-8-ribityllumazine synthase, LS) catalyzes the condensation of the 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy- 2-butanone-4-phosphate to release water, inorganic phosphate and 6,7-dimethyl-8-ribityllumazine (DMRL), followed by RS which catalyzes a dismutation of DMRL yielding riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. In the latter reaction, a four-carbon moiety is transferred between two DMRL molecules serving as donor and acceptor, respectively. Both the LS and RS catalyzed reactions are thermodynamically irreversible and can proceed in the absence of a catalyst. Archaeal RSs share sequence similarity with LSs, both appear to have diverged early in the evolution of archaea from a common ancestor
IGIVDTTFARVDMGSVAIDELKKLLPGIKIVRYTVPGIKDLPVAAKKLIEEEGCDIVMALGWVGPTEKDK
VSYHEASLGLILVQLMTNKHIIDVTVHEDEAEDEKELKELADDRAREHAENLVYLLFKPEYLTREAGMGL
RQG
>gnl|CDD|187744 cd09211, Lumazine_synthase_archaeal, lumazine synthase (6,7-dimethyl-8-ribityllumazine synthase, LS); catalyzes the penultimate step in the biosynthesis of riboflavin (vitamin B2). Archaeal LS is an important enzyme in the riboflavin biosynthetic pathway. Riboflavin is the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) which are essential cofactors for the catalysis of a wide range of redox reactions. These cofactors are also involved in many other processes involving DNA repair, circadian time-keeping, light sensing, and bioluminescence. In the final steps of the riboflavin biosynthetic pathway LS catalyzes the condensation of the 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy- 2-butanone-4-phosphate to release water, inorganic phosphate and 6,7-dimethyl-8-ribityllumazine (DMRL), and riboflavin synthase (RS) catalyzes a dismutation of DMRL which yields riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. In the latter reaction, a four-carbon moiety is transferred between two DMRL molecules serving as donor and acceptor, respectively. Both the LS and RS catalyzed reactions are thermodynamically irreversible and can proceed in the absence of a catalyst. LS from Methanococcus jannaschii forms capsids with icosahedral 532 symmetry consisting of 60 subunits. Archaeal LSs share sequence similarity with archaeal RSs, both appear to have diverged early in the evolution of archaea from a common ancestor
LGIVVAEFNYDITYMMEEKALEHAKFLGAEVKYVLRVPGVFDMPLAVKKLLEKDDIDAVVTLGAVIKGET
KHDELIANQAARKILDLSLEYGKPVTLGISGPGMSRLQALERIEYYAKRAVEAAVKMVKRL
>gnl|CDD|198416 cd09212, PUB, PNGase/UBA or UBX (PUB) domain of p97 adaptor proteins. The PUB domain is found in p97 adaptor proteins such as PNGase, UBXD1 (UBX domain-containing protein 1), and RNF31 (RING finger protein 31). It functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The p97, a type II AAA+ ATPase, is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. The PUB domain in UBX-domain protein 1 (UBXD1), which is widely expressed in higher eukaryotes (except for fungi) and which is involved in substrate recruitment to p97, interacts strongly with the C-terminus of p97. Peptide:N-glycanase (PNGase), a deglycosylating enzyme that functions in proteasome-dependent degradation of misfolded glycoproteins which are translocated from the endoplasmic reticulum (ER) to the cytosol during ERAD, associates with the ubiquitin-proteasome system proteins mediated by the N-terminal PUB domain. PNGase is present in all eukaryotic organisms; however, the yeast PNGase ortholog does not contain the PUB domain. The RNF31 protein, also known as HOIP or Zibra, contains an N-terminal PUB domain similar to those in PNGase and UBXD1, suggesting its association with p97
LDALRSNNDLEAFKEALKTLLKILDNILSNPTEEKYRRIRLSNKAFQEKVLPVPGGLELLLALGFVEETE
SGESFLVLPDDADVDLLKDAKAALEE
>gnl|CDD|188873 cd09213, Luminal_IRE1_like, The Luminal domain, a dimerization domain, of Inositol-requiring protein 1-like proteins. The Luminal domain is a dimerization domain present in Inositol-requiring protein 1 (IRE1), eukaryotic translation Initiation Factor 2-Alpha Kinase 3 (EIF2AK3), and similar proteins. IRE1 and EIF2AK3 are serine/threonine protein kinases (STKs) and are type I transmembrane proteins that are localized in the endoplasmic reticulum (ER). They are kinase receptors that are activated through the release of BiP, a chaperone bound to their luminal domains under unstressed conditions. This results in dimerization through their luminal domains, allowing trans-autophosphorylation of their kinase domains and activation. They play roles in the signaling of the unfolded protein response (UPR), which is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), contains an endoribonuclease domain in its cytoplasmic side and acts as an ER stress sensor. It is the oldest and most conserved component of the UPR in eukaryotes. Its activation results in the cleavage of its mRNA substrate, HAC1 in yeast and Xbp1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. EIF2AK3, also called PKR-like Endoplasmic Reticulum Kinase (PERK), phosphorylates the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. It functions as the central regulator of translational control during the UPR pathway. In addition to the eIF-2 alpha subunit, EIF2AK3 also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR
LLLVATLDGTIYAVDASSGEIQWSFDGGGPLYSSYQSSRDGNAESSSTMLIPSLDGDGNLYQHDKGHGSL
QRLPLTIEDLVEASPLVSDTNEDDVVVVGSKRTSVFALDAKTGKIIKTYRADGLPSTGGSDSDGNSTPGP
DELQEEEELLYIGRTDYVLQAIDPRSGKELWNVTYGEYEALTLDADELGTSSSSSPLSASFRISENEPVP
AVYLLGLQGGKSLWEHLFDSPIVSAFDYSSKLTNFEGLIKPIFVFQVHEYASSNSVYIGAHENGQLFALS
SPSKSEDKESAISNILEGENTSPSALEGVSGN
>gnl|CDD|185753 cd09214, GH64-like, glycosyl hydrolase 64 family. This family is represented by the laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis and related bacterial and ascomycete proteins. LPHase is a member of glycoside hydrolase family 64 (GH64), it is an inverting enzyme involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. LPHase is a two-domain crescent fold structure: one domain is composed of 10 beta-strands, eight coming from the N-terminus of the protein and two from the C-terminal region, and the protein has a second inserted domain; this cd includes both domains. This protein has an electronegative, substrate-binding cleft, and conserved Glu and Asp residues involved in the cleavage of the beta-1,3-glucan, laminarin, a plant and fungal cell wall component. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. Also included in this family is GluB, the beta-1,3-glucanase B from Lysobacter enzymogenes Strain N4-7. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain. In the Cellulosimicrobium cellulans, glucan endo-1,3-beta-glucosidase, they are positioned N-terminal of a RICIN, carbohydrate-binding domain, and in the Salinispora tropica CNB-440, coagulation factor 5/8 C-terminal domain (FA58C) protein, they are positioned C-terminal of two FA58C domains which are proposed to function as cell surface-attached, carbohydrate-binding domain. This FA58C-containing protein has an internal peptide deletion (of approx. 44 residues) in the LPHase domain II
IPLTITNNTGGADSQIYVTVLGIDPSTGNWVYVDATGNLVPISVADNDAPGHLTKNGGNYANIFFTLSEA
SNKILPPPLPSGRIYISFGNPLYIKAFQDGGDMPGYAGPDLNNPTDPNNGTLFDFIEFTYNATGLWGNTT
RVDAFGIPLTLRLIGKGGYDKTVGELDQESRAEIFNAFAATVPAEFKSLVQYGAPYRILAPGKGPFKPGG
ANANYFDSYIPSTQEVFGCAGPLAGGNDTQGQIQAQLCAALNRHVALSPAAQWSDASNYYQAAPANYYAQ
FWHAHSINGLAYGFPYDDVNGQSSTLSTTDPTHATITLG
>gnl|CDD|185754 cd09215, Thaumatin-like, the sweet-tasting protein, thaumatin, and thaumatin-like proteins involved in host defense. This family is represented by the sweet-tasting protein thaumatin from the African berry Thaumatococcus daniellii and thaumatin-like proteins (TLPs) involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Plant TLPs are classified as pathogenesis-related (PR) protein family 5 (PR5), their expression is induced by environmental stresses such as pathogen/pest attack, drought and cold. TLPs included in this family are such proteins as zeamatin, found in high concentrations in cereal seeds; osmotin, a salt-induced protein in osmotically stressed plants; and PpAZ44, a propylene-induced TLP in abscission of young fruit. Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). Thaumatin and TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. Most TLPs contain 16 conserved Cys residues. A deletion within the third domain (domain II) of the Triticum aestivum thaumatin-like xylanase inhibitor is observed, thus, only 10 conserved Cys residues are present within this smaller TLP and similar homologs
FTITNRCPYTIWPAIFTQVGKGPYTGGFELNPGETKSFDVSAGWQGRIWARTNCSFNANSGGNACLTGDC
NGGLNCQGTGGPPATLAEFTLSGGGGLDYYDISLVDGYNLPMSITPQPGECPTPICAACPDAYSYAYDDQ
TSTFTCPGGAGYEVVFC
>gnl|CDD|185755 cd09216, GH64-LPHase-like, glycoside hydrolase family 64: laminaripentaose-producing, beta-1,3-glucanase (LPHase)-like. This subfamily is represented by the laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis and related bacterial and ascomycete proteins. LPHase is a member of glycoside hydrolase family 64 (GH64), it is an inverting enzyme involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. LPHase is a two-domain crescent fold structure: one domain is composed of 10 beta-strands, eight coming from the N-terminus of the protein and two from the C-terminal region, and the protein has a second inserted domain; this cd includes both domains. This protein has an electronegative, substrate-binding cleft, and conserved Glu and Asp residues involved in the cleavage of the beta-1,3-glucan, laminarin, a plant and fungal cell wall component. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. Also included in this family is GluB, the beta-1,3-glucanase B from Lysobacter enzymogenes Strain N4-7. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain. In the Cellulosimicrobium cellulans, glucan endo-1,3-beta-glucosidase, they are positioned N-terminal of a RICIN, carbohydrate-binding domain
LPLTITNNSGRNNQIYLYVVGTDLQTGRQGWVDADGAAHPVPPGDNVPDGAADYAIPLPSPGDTTTVLPP
RMSGRIYFSLGSKLRFKVVTNPALVQPAGWNPSDPNFNILHDWVEFTFNDAGLFCNTTQVDMFSAPLAIG
LRGADGRDQTTGTLKPGGRDAVFDALSGQPAWAGLVQRRPDGTVLRVIAPGHGLDAGAFPATYLDGYIDE
VWNKYRTTDLTVTTFSDGGTFTGRVSGDWLRFTGGNVAAFAKPSTRDVLFCDGALAAPNDGVTGPIAATL
GAAFNRTTLLDNPNQPGTDPAAFYRDAVTNHYAKVVHEAMADGKAYGFAFDDVGAFASYVQDGAPTGATV
TLT
>gnl|CDD|185756 cd09217, TLP-P, thaumatin and allergenic/antifungal thaumatin-like proteins: plant homologs. This subfamily is represented by the sweet-tasting protein thaumatin from the African berry Thaumatococcus daniellii, allergenic/antifungal Thaumatin-like proteins (TLPs), and related plant proteins. TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Plant TLPs are classified as pathogenesis-related (PR) protein family 5 (PR5), their expression is induced by environmental stresses such as pathogen/pest attack, drought and cold. TLPs in this subfamily include such proteins as zeamatin, found in high concentrations in cereal seeds, and osmotin, a salt-induced protein in osmotically stressed plants. Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). Thaumatin and TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. IgE-binding epitopes of mountain Cedar (Juniperus ashei) allergen Jun a 3, which interact with pooled IgE from patients suffering allergenic response to this allergen, were mainly located on the helical domain II; the best-conserved IgE-binding epitope predicted for TLPs corresponds to this region. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. Most TLPs contain 16 conserved Cys residues. A deletion within the third domain (domain II) of the Triticum aestivum thaumatin-like xylanase inhibitor is observed, thus, only 10 conserved Cys residues are present within this smaller TLP and similar homologs
FTITNNCGYTVWPAATPVGGGRQLNPGQSWTIDVPAGTAGGRIWGRTGCSFDASGRGSCQTGDCGGVLSC
TGSGKPPATLAEYTLNQSGQDFYDISLVDGFNVPMDFSPTGGGCHAIPCAANCPDAYSYPKDPTTTFTCP
GGTNYRIVFCP
>gnl|CDD|185757 cd09218, TLP-PA, allergenic/antifungal thaumatin-like proteins: plant and animal homologs. This subfamily is represented by the thaumatin-like proteins (TLPs), Cherry Allergen Pru Av 2 TLP, Peach PpAZ44 TLP (a propylene-induced TLP in abscission), the Caenorhabditis elegans thaumatin family member (thn-6), and other plant and animal homologs. TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Due to their inducible expression by environmental stresses such as pathogen/pest attack, drought and cold, plant TLPs are classified as the pathogenesis-related (PR) protein family 5 (PR5). Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. TLPs within this subfamily contain 16 conserved Cys residues
TFTIYNKCPFTVWPGILGNAGHPQLGGGGFELAPGQSRTIDAPSGWSGRFWGRTGCSFDSSGKGSCATGD
CGGGLECNGAGGAPPATLAEFTLGGSGGQDFYDVSLVDGYNLPVSITPQGGSGGCRTAGCVADLNAVCPA
ELQVKNSGGRVVACKSACLAFNTDEYCCRGAYGTPETCKPTTYSRLFKNACPQAYSYAYDDPTSTFTCSS
GANYVITFC
>gnl|CDD|185758 cd09219, TLP-F, thaumatin-like proteins: basidiomycete homologs. This subfamily is represented by Lentinula edodes TLG1, a thaumatin-like protein (TLP), as well as, other basidiomycete homologs. In general, TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. TLG1 TLP is involved in lentinan degradation and fruiting body senescence. TLG1 expressed in Escherichia coli and Aspergillus oryzae exhibited beta-1,3-glucanase activity and demonstrated lentinan degrading activity. TLG1 is proposed to be involved in lentinan and cell wall degradation during senescence following harvest and spore diffusion. TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. TLG1 from Lentinula edodes contains the required acidic amino acids conserved in the appropriate positions to possess an electronegative cleft. TLPs within this subfamily contain 13 conserved Cys residues; the number of total Cys residues in these TLPs varies from 16 in L. edodes TLG1 to 18 in other basidiomycete homologs
FTVKNSCSSTIWPAMFTGGNFIDAVPDQATGWEAAAGGQVEFTVPDNWTAGRIWARTGCDFSDNPGPFSC
LTGGCGGGLTCENSDQPPASLAEFTLIGGKEDNYDISLVDGFNIPLNITNNITCPQPQCQVDLNVLCPAL
LRGPLDQKGVNLGCISPCNRDKNHDDSPSCCTGSHNKPETCPQSGVGNYAYFKDNCPTAYAYAYDEKSHT
ALWTCGDSKSADYTVTFCP
>gnl|CDD|185759 cd09220, GH64-GluB-like, glycoside hydrolase family 64: beta-1,3-glucanase B (GluB)-like. This subfamily is represented by GluB, beta-1,3-glucanase B, from Lysobacter enzymogenes Strain N4-7 and related bacterial and ascomycete proteins. GluB is a member of the glycoside hydrolase family 64 (GH64) involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. GluB possesses the conserved Glu and Asp residues required to cleave substrate beta-1,3-glucans. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Based on the structure of laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis, which belongs to the same family as GluB but to a different subfamily, this cd is a two-domain model. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain
LPLALVNNSGSGTVYAYITGLDLNNNRVVFLRADGSTYYPPSSPSAVPSPLGADCAIPLGAPGSTTTVTI
PILAGGRIWFSVDDKLTFLLNPGGPALVEPSVTNPSDPNYNKNWGFCEFTYNSGQLYANISYVDFVGLPL
GLSLTTTDGGTQTVPGLPADALDTICDALRAQGQRDGAPWDQLVVTNDDGKVLRVLSPNNGMVLNPSLFS
GYWTSYVDQVWDKYANTPLTVNTQAGWGVVTGRVSGDTLTFGGGGSFAKPSTADIFGCNSGPFANNPGDN
AVRGAIVPRLAAAFNRSTLLVNGGQPPGEGASTYYKNPPTNHYSRIVHENNPDGRGYAFPYDDVNPDGGE
DQSGAVNDGNPTLLTVTVG
>gnl|CDD|187745 cd09223, Photo_RC, D1, D2 subunits of photosystem II (PSII); M, L subunits of bacterial photosynthetic reaction center. This protein superfamily contains the D1, D2 subunits of the photosystem II (PS II) and the M, L subunits of the bacterial photosynthetic reaction center (RC). These four proteins are highly homologous and share a common fold. PS II is a multi-subunit protein found in the photosynthetic membranes of plants, algae, and cyanobacteria. It utilizes light-induced electron transfer and water-splitting reactions to produce protons, electrons, and molecular oxygen. The protons generated are instrumental in ATP formation. Bacterial photosynthetic reaction center (RC) complex is found in photosynthetic bacteria, such as purple bacteria and other proteobacteria species. It couples light-induced electron transfer to proton pumping across the membrane by reactions of a quinone molecule (QB) that binds two electrons and two protons at the active site. Protons are translocated from the bacterial cytoplasm to the periplasmic space, generating an electrochemical gradient of protons (the protonmotive force) that can be used to power reactions such as the synthesis of ATP
YVGWFGVLMFFFALLATILIGIAGGLWQIITFHALGAFISWMLRQVEIARKLGMGPHIAVAFSAPIASFF
VLFLIRPIGQGSWSDAFPYGISSHLDWVNNFQYEHNNWHYNPFHMLGVAFVFGGALLCAMHGALVLSVLN
PEGEETEGQEAEEYNTAEHANYFWRDIFGYAIGNRSIHRFGLFLAVVGVWFSAIGIITS
>gnl|CDD|198423 cd09224, CytoC_RC, Cytochrome C subunit of the bacterial photosynthetic reaction center. Photosynthesis in purple bacteria is dependent on light-induced electron transfer in the reaction center (RC), coupled to the uptake of protons from the cytoplasm. The RC contains a cytochrome molecule which re-reduces the oxidized electron donor. The electron transfer reactions of photosynthesis are performed by the following three components: the photosynthetic reaction center (RC), the cytochrome, and the soluble electron carrier protein. Firstly, the RC promotes the light-induced charge separation across the plasma membrane, which results in the oxidation of a pair of light-harvesting complexes, LH1 and LH2, and the reduction of quinone to quinol. The quinol then leaves the RC and moves to the cytochrome complex through the quinone pool of the plasma membrane. Secondly, the cytochrome complex reoxidizes the quinol to quinone, and the released electrons are transferred to soluble electron carriers. Third, the soluble electron carriers transport the electrons to the RC through the periplasmic space. Finally, the photo-oxidized light-harvesting complex is reduced by the soluble electron carriers, and the RC comes back to the initial state. In the course of the oxidation and reduction of the quinones, a transmembrane electrochemical gradient of protons is formed, and its energy is used to produce ATP by the ATP synthase complex
ERPPVETVQTGYRGTGMEQVKNPRALQPPADANQAPAPLPAAPNEGPKAGQVYQNVQVLGDLSSAEFNRL
MVAITEWVSPEEGCNYCHNIENFASDELYTKVVARRMLEMTQDINANWTAHVAGTGVTCYTCHRGNPVPL
EVWFTDPGPSHPPGGAGNDPGQNRASAAVGYTSLPNDPFTPFLLDDEEIRVTGTTALPGVDNRASIKQAE
WTYGLMMHMSDSLGVNCTFCHNSRAFADWDQSTPQRVTAWYGIRMVRDINNNYLEPLTAEFPASRLGPLG
DAPKVNCATCHQGANKPLYG
>gnl|CDD|185717 cd09232, Snurportin-1_C, C-terminal m3G cap-binding domain of nuclear import adaptor snurportin-1. Snurportin-1 (SPN1 or SNUPN) is a nuclear import adaptor for m3G-capped spliceosomal U small nucleoproteins (snRNPs), which are assembled in the cytoplasm. After capping and assembly, the U snRNPs are transported into the nucleus by SPN1 and importin beta; SPN1 is then returned to the cytoplasm by exportin 1 (CRM1), which also transports the non-capped U snRNPs. The U snRNPs are essential elements of the spliceosome, which catalyzes the excision of introns and the ligation of exons to form a mature mRNA. SPN1 contains two domains, an N-terminal importin beta-binding (IBB) domain and a C-terminal m3G cap-binding domain
LYANQLMLSEWMVEVPDDLSEEWLVVPCPVGKRCLVVASKGKTVARSKNGRTLHRFSSALPGGSRKTSNS
GYTILDCIYNEDDRTYYVLDVLCWNGHPLYDCETEFRFFWLRSKLEELPELDEPSEKNPFRFVPLPYFPC
TKESLQSAYSGPLNDDPYELDGLLFYHKESHYTPGSTPLVLWLKDY
>gnl|CDD|187750 cd09233, ACE1-Sec16-like, Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16. COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site
FPGPLIKGKTKKKDVLKWLEEKIAELEENEGYLDLEDKLLLWKLLKLLVRQNGKLVGTDIAEQKALNRFR
NLLLTGNRKEALELALDNGLWAHALLLASSLGKETWAEVVSRFARSESKLNDPLQTLYQLFSGNSPEAIT
ELADNPAEAEWALGNWREHLAIILSNRTSNLDLEALVELGDLLAQRGLVEAAHICYLLAGVPLGPYPSSP
SSCLLGGAVHNKSPRTFATPEAIQLTEIYEYALSLGNPQFGLPHLQPYKLIHAARLAELGLVSEALKYCE
AIASSLKSLTKSPYYDPNLLAQLQDLSERLSGTS
>gnl|CDD|185747 cd09234, V_HD-PTP_like, Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains. This family contains the V-shaped (V) domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23) and related domains. It belongs to the V_Alix_like superfamily which includes the V domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X/ also known as apoptosis-linked gene-2 interacting protein 1, AIP1), and related domains. HD_PTP interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in cell migration and endosomal trafficking. The related Alix V-domain (belonging to a different family in this superfamily) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to the V-domain, HD_PTP also has an N-terminal Bro1-like domain, a proline-rich region (PRR), a catalytically inactive tyrosine phosphatase domain, and a region containing a PEST motif. Bro1-like domains bind components of the ESCRT-III complex, specifically to CHMP4 in the case of HD-PTP. The Bro1-like domain of HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This family also contains Drosophila Myopic, which promotes epidermal growth factor receptor (EGFR) signaling, and Caenorhabditis elegans (enhancer of glp-1) EGO-2 which promotes Notch signaling
PMEAHEASSLYSEEKAKLLREVVSEIEDKDEELDQFLSSLQLDPLNVMDMDGQFELPQDLVERCAALSVR
PDTIKNLVEAMGELSDVYQDVEAMLNEIESLLEEEELQEKEFQEAVGKRGSSIAHVTELKRELKKYKEAH
EKASQSNTELHKAMNLHIANLKLLAGPLDELQKKLPSPSLLDRPEDEAIEKELKRILNKVNEMRKQRRSL
EQQLRDAIHEDDITSKLVTTTGGDMEDLFKEELKKHDQLVNLIEQNLAAQENILKALTEANAKYAPVRKA
LSETKQKRESTISSLIASYEAYEDLLKKSQKGIDFYKKLEGNVSKLLQRIKSVCKVQ
>gnl|CDD|185748 cd09235, V_Alix, Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction modules. This family contains the middle V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X) and related domains. It belongs to the V_Alix_like superfamily which includes the V-domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), is part of the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in membrane remodeling processes, including the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), the abscission reactions of mammalian cell division, and in apoptosis. The Alix V-domain is a dimerization domain, and contains a binding site, partially conserved in the V_Alix_like superfamily, for the retroviral late assembly (L) domain YPXnL motif. In addition to the V-domain, Alix also has an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex, in particular CHMP4. The Bro1-like domain of Alix can also bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Alix also has a C-terminal proline-rich region (PRR) that binds multiple partners including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1), and the apoptotic protein ALG-2
PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGG
IQTIDQLIKELPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTIL
DNAVQADKIVREKYESHREGIELLSKPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVI
ESELKSATFDMKSKFLSALAQDGAINEEAISVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKE
KQSNSGANEREEVLKDLAAAYDAFMELTANLKEGTKFYNDLTEILVKFQNKCSDFVFAR
>gnl|CDD|185749 cd09236, V_AnPalA_UmRIM20_like, Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and related proteins. This family belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Aspergillus nidulas PalA/RIM20 and Ustilago maydis RIM20, like Saccharomyces cerevisiae Rim20, participate in the response to the external pH via the Pal/Rim101 pathway; however, Saccharomyces cerevisiae Rim20 does not belong to this family. This pathway is a signaling cascade resulting in the activation of the transcription factor PacC/Rim101. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. Aspergillus nidulas PalA binds a nonviral YPXnL motif (tandem YPXL/I motifs within PacC). The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_like superfamily also have an N-terminal Bro1-like domain, which has been shown to bind CHMP4/Snf7, a component of the ESCRT-III complex
PFGVHLAISIYDDRKDRLVNESIIDELEELTNRAHSTLRSLNLPGSLQALEKPLGLPPSLLRHAEEIRQE
DGLERIRASLDDVARLAASDRAILEEAMDILDDEASEDESLRRKFGTDRWTRPDSHEANPKLYTQAAEYE
GYLKQAGASDELVRRKLDEWEDLIQILTGDERDLENFVPSSRRPSIPPELERHVRALRVSLEELDRLESR
RRRKVERARTKARADDIRPEILREAARLEREYPATEVAPAHFEDLFDKRLAKYDKDLDAVSEEAQEQEEI
LQQIEVANKAFLQSRKGDPATKERERALQSLDLAYFKYKEIVSNLDEGRKFYNDLAKILSQFRDACKAWV
YER
>gnl|CDD|185750 cd09237, V_ScBro1_like, Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains. This family contains the V-shaped (V) domain of Saccharomyces cerevisiae Bro1, and related domains. It belongs to the V_Alix_like superfamily which also includes the V-domain of Saccharomyces cerevisiae Rim20 (also known as PalA), mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Bro1 interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in endosomal trafficking. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Bro1 also has an N-terminal Bro1-like domain, which binds Snf7, a component of the ESCRT-III complex, and a C-terminal proline-rich region (PRR). The C-terminal portion (V-domain and PRR) of S. cerevisiae Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes. It interacts with a YPxL motif in the Doa4s catalytic domain to stimulate its deubiquitination activity
PLAVHEKESLYSEEKAKLLRAEVERVEVANEEYASFLEYLNLPKLLVDLKERFEGENELMEIVSGLKSSS
VDSQLELLRPQSASWVNEIDSSYNDLDEEMKEIEKMRKKILAKWTQSPSSSLTASLREDLVKLKKSLVEA
SASDEKLFSLVDPVKEDIALLLNGGSLWEELFGFSSSGSPEPSLLDLDDSQNEQTVLKQIKQLEELLEDL
NLIKEERQRVLKDLKQKIHNDDISDILILNSKSKSEIEKQLFPEELEKFKPLQNRLEATIFKQSSLINEL
KIELDKLFKLPGVKEKQSKEKSKQKLRKEFFEKLKKAYNSFKKFSAGLPKGLEFYDDLLKMAKDLAKNVQ
AFVNQR
>gnl|CDD|185751 cd09238, V_Alix_like_1, Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily. This domain family is comprised of uncharacterized plant proteins. It belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), (His-Domain) type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_Rim20_Bro1_like superfamily also have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members of the V_Alix_like superfamily also have a proline-rich region (PRR)
PESSAKALSKYTEMVDELIRTEADRLAAASDEARVALREMELPETLIALDGGASLPGDLGLDEEVEAVQI
SGGLAALEGELPRLRELRRVCTELLAAAQESLEAEATEDSAARTQYGTAWTRPPSATLTKNLWERLNRFR
VNLEQAGDSDESLRRRIEDAMDGMLILDDEPAAAAAPTLRAPMLSTDEDDASIVGTLRSNLEELEALGNE
RAGIEDMMKALKRNDNILAKVMATTGSYDALFKEELKKYDSVREAVSKNISSQDDLLSRLRALNEKFSQI
FDVEGWRAATESHATQIRAAVAKYRELREGMEEGLRFYSGFQEAVRRLKQECEDFVMTR
>gnl|CDD|185762 cd09239, BRO1_HD-PTP_like, Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains. This family contains the N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP) and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. HD-PTP participates in cell migration and endosomal trafficking. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 in the case of HD-PTP. The Bro1-like domain of HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. HD-PTP, and some other members of the BRO1_Alix_like superfamily including Alix, also have a V-shaped (V) domain. In the case of Alix, the V-domain contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the V-domain superfamily. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This family also contains Drosophila Myopic which promotes epidermal growth factor receptor (EGFR) signaling, and Caenorhabditis elegans (enhancer of glp-1) EGO-2 which promotes Notch signaling
EAVPRLPMLWLQLKSSGEFTFQPALKKYILENYGEDPELYSEELKSLEQLRQEAVNPPRDFEGCSVLKRY
YGQLHLLQSRFPMGAGQEAAVPFTWTDIFSGSEVTHEDIKFEEASVLYNIGALHSQLGASDKRDSEEGMK
VACTHFQCAAWAFAYLREHYPQVYGAVDMSSQLLSFNYSLMLAQAQECLLEKSLLDNRKSHITAKVSAQV
VEYYKEALRALENWESNSKIILGKIQKEWRKLVQMKIAYYASIAHLHMGKQSEEQQKMGERVAYYQLAND
KLEEAIKNAKGQPDTVNLQEALSFTMDVIGGKRNSAKKENDFIYHEAVPKLDTLQAVKGANLVKGIPFSP
TDPEVCGPDIF
>gnl|CDD|185763 cd09240, BRO1_Alix, Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains. This family contains the N-terminal, Bro1-like domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), also called apoptosis-linked gene-2 interacting protein 1 (AIP1). It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4, in the case of Alix. The Alix Bro1-like domain can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid and Rab5-specfic GAP (RabGAP5, also known as Rab-GAPLP). In addition to this Bro1-like domain, Alix has a middle V-shaped (V) domain. The Alix V-domain is a dimerization domain, and carries a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the superfamily. Alix also has a C-terminal proline-rich region (PRR) that binds multiple partners including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2
ASFISVPLKKSSEVDLVKPLEKFIKNTYSSGEEQADYKEAIKELNKLRNNAVCRPLDKHESSLELLLRYY
DQLCAIEPKFPFSESQIQVTFTWKDAFDKGSLFGGSKKLALSSLGYEKVCVLFNIAALQSQIAAEQNLDT
DEGLKLAAKLFQQAAGIFNHLKETVLSALQQEPTPDLSPDTLSALSALMLAQAQEVFYLKATRDKMKDAI
IAKLAAQAADYYGDAFKQCQREDVRSLLPKDWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQH
ALELIKTAQSRAGEYVDVKDFAAKISRALTAAKKDNDFIYHDRVPDVKSLPPIGKAALAKPTPVNV
>gnl|CDD|185764 cd09241, BRO1_ScRim20-like, Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and related proteins. This family contains the N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 (also known as PalA) and related proteins. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Saccharomyces cerevisiae Bro1, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Rim20 and Rim23 participate in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: Snf7 in the case of Rim20. RIM20, and some other members of the BRO1_Alix_like superfamily including Alix, also have a V-shaped (V) domain. In the case of Alix, the V-domain is a dimerization domain that also contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the V-domain superfamily. Rim20 localizes to endosomes under alkaline pH conditions. By binding Snf7, it may bring the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and thus aid in the proteolytic activation of the latter. Rim20 and other intermediates in the Rim101 pathway play roles in the pathogenesis of fungal corneal infection during Candida albicans keratitis
NLLSIPFKRTLPVDLKDALRNYISNHYFQTPSSFEDDLAEIDKLRNDAINPEPSVNGLSLLKEYYAQLVV
LSKKFPDDQLEFTWYPTLGYKSSGPVSLSSLKFERANILYNLGALYSQLALSENRYTDEGLKRACSYFQA
SAGCFEYILQHLLPTLSPPPDLDENTLKALESLMLAQAQECFWQKAISDGTKDSLIAKLAAQVSDYYQEA
LKYANKSDLIRSDWINHLKVKKHHFKAAAHYRMALVALEKSKYGEEVARLRVALAACKEALKEARYGNKA
VLEDLQGLKDIVKESLKRAERDNDLIYLQPVPPASELPPIKPASMVKAIVPPELEEGSKLGKPLFKDLLP
YGVHE
>gnl|CDD|185765 cd09242, BRO1_ScBro1_like, Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related proteins. This family contains the N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related proteins. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Saccharomyces cerevisiae Rim20 (also known as PalA), Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Bro1 participates in endosomal trafficking. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: Snf7 in the case of Bro1. Snf7 binds to a conserved hydrophobic patch on the middle of the concave side of the Bro1 domain. RIM20, and some other members of the BRO1_Alix_like superfamily including Alix, also have a V-shaped (V) domain. In the case of Alix, the V-domain contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the superfamily. The Alix V-domain is also a dimerization domain. The C-terminal portion (V-domain and proline rich-region) of Bro1 interacts with Doa4, a protease that deubiquitinates integral membrane proteins sorted into the lumenal vesicles of late-endosomal multivesicular bodies. It interacts with a YPxL motif in the Doa4 catalytic domain to stimulate its deubiquitination activity
LISLPLKDTEEVDWKKPLSSYLKRSYGSSTFYYEEEIAEFDRLRQDANGVLADETGRDLLYKYYGQLELL
ELRFPFNNKELKVDFTWYDAFYKSKKVKQHSLAFEKASVLFNIGALLSQLAAEKYREDEDDLKEAITNLQ
QAAGCFQYINENFLHAPSVDLQQENVKFLVKLMLAQAQEIFLLKLINGDDAQKKASLISKLASATANLYE
SCVEFLKEIQEKGISYGDPKWISLVQCKAHYYKSLAAYYHALALEAAGKYGEAIAYLTQAESILKEANPQ
KLSLKASAGDAAYALNDDFKGQKDTVEEKLKELEKDNDFIYHDIVPSEVTLPSIKPLDAAKPIPIEEQ
>gnl|CDD|185766 cd09243, BRO1_Brox_like, Protein-interacting Bro1-like domain of human Brox1 and related proteins. This family contains the Bro1-like domain of a single-domain protein, human Brox, and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 in the case of Brox. Human Brox can bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. In addition to a Bro1-like domain, Brox also has a C-terminal thioester-linkage site for isoprenoid lipids (CaaX motif). This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily
WFHRNPLKATAPVKFDLKGVATTPAASKLCSDLRTARARLLELLSDPSNDVDTVKTAFNAYLSLLQGFIL
ALDGKTQESKLRYLINFKWTDSLLGNEPSVQQDAIFELASMLFNVALWYTKHASKLAGKEDITEDEAKDV
HKSLRTAAGIFQFVKENYIPKLIEPAEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALA
YETAKLFQKADDSLSSLDPEYSGKWRKYLQLKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNK
AEALCKEYAKTKGPGTTAKPDQHLFFRKLGPLVKRTLEKCERENGFIYHQKVPDEVPQLELKATYGLVSP
EEF
>gnl|CDD|185767 cd09244, BRO1_Rhophilin, Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains. This family contains the Bro1-like domain of RhoA-binding proteins, Rhophilin-1 and -2, and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-1 and -2 bind both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-1 and -2, contain an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. Their PDZ domains have limited homology. Rhophilin-1 and -2 have different activities. The Drosophila knockout of Rhophilin-1 is embryonic lethal, suggesting an essential role in embryonic development. Roles of Rhophilin-2 may include limiting stress fiber formation or increasing the turnover of F-actin in the absence of high levels of RhoA signaling activity. The isolated Bro1-like domain of Rhophilin-1 binds human immunodeficiency virus type 1 (HIV-1) nucleocapsid. This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix _like superfamily
MIPLGLKETKEIDFMEPFKDFILEHYSEDPSLYEDEIADFTDLRQAMRTPSRDEAGIELLFEYYNQLYFV
ERRFFPPDRSLGIYFHWYDSLTGVPSVQRSVAFEKASVLFNIGALYTQIGAKQDRTTEEGIEAAVDAFQR
AAGAFNYLRENFSNAPSMDLSPEMLEALIKLMLAQAQECVFEKLVLPGEDSKDIQACLDLAQEAAQVSDC
YSEVHKLMNQEPVKDYIPYSWISLVEVKSEHYKALAHYYAAMGLLLEERRLLGKAHLKEALLLHEEALRL
HRMCRFLRNVDSLQEVLKEAHDRSLNKYSSLEEEDDFSDALDAPDIQAKTKQQLEIIPPDFTQVKVKDLF
>gnl|CDD|185768 cd09245, BRO1_UmRIM23-like, Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains. This family contains the Bro1-like domain of Ustilago maydis Rim23 (also known as PalC), and related proteins. It belongs to the BRO1_Alix_like superfamily which includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Rim20 and Rim23 participate in the response to the external pH via the Rim101 pathway. Through its Bro1-like domain, Rim23 allows the interaction between the endosomal and plasma membrane complexes. Bro1-like domains are boomerang-shape, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Intermediates in the Rim101 pathway may play roles in the pathogenesis of fungal corneal infection during Candida albicans keratitis. This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily
PYPFELPTTSSISFSDFFNSDSYPSLPLNATTARAVLRAALKAHKRTPPGSQASNLLTVVKALEEYLPYL
LAIDACLSHDELILKSEPTFEWRTTLSSTSGRESPRLPLPGLHYELAFVLLTYAYALSNLARSILAPLGA
YETDRSISDASRKQRDERLKAATKLLCKAAGIFDYLATRVLPQWESNRGGAPPPPDLSPEVLSALSSLAL
AEATLLAVRKLDPYPAAVDKDWMTPGPPLPKVHPSAHLLARLCLAASEHAESARALLSTPGSKRGSGEVS
EELLRYLSDLRRVARALACKFLGIDAGENGKVGEAIGWLRAAKKELEDLKSPSGVASKAKLKKSWKEKRE
DRKVEKGAGVEEELRTLEMLLKKYKKMNDTVSFQPVPPSSELQSSMPSGREAHTAKPYTPPPS
>gnl|CDD|185769 cd09246, BRO1_Alix_like_1, Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like superfamily. This domain family is comprised of uncharacterized proteins. It belongs to the BRO1_Alix_like superfamily which includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20 and Rim23 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP and Bro1 function in endosomal trafficking, with HD-PTP having additional functions in cell migration. Rim20 and Rim23 play roles in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 (in the case of Alix, Brox and HD-PTP) and Snf7 (in the case of yeast Bro1 and Rim20). The Bro1-like domains of Alix, HD-PTP, Brox, and Rhophilin can bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. In addition to this Bro1-like domain, Alix, Bro1, Rim20, HD_PTP, and proteins belonging to this uncharacterized family, also have a V-shaped (V) domain. The Alix V-domain is a dimerization domain, and contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the BRO1_Alix_like superfamily. Many members of this superfamily also have a proline-rich region (PRR), a protein interaction domain
MLSIHRKKTETVDLVSPLRAYISETYSEREAQDAEDDLAELQQLRSEVRTLQEKHAASRELLLRYYRALC
AVESRFPISEESGHARVSFSWYDAFRPHRKATQANVHFEKAAVLFNLGALSSQLGLQQDRTTAEGIKQAC
HAFQAAAGAFAHLRDKVSGKTGGFRTPDLTAECLGMLESLMLAQAQECFYEKAVADGKSPAVCSKLAKQA
RSYYEEALEALDSPPLKGHFDKSWVAHVQLKAAYFRAEALYRAAKDLHEKEDIGEEIARLRAASDALAEA
RKQAKGVNGDELIEAVSELEQVINELLERAEKENDCVYLDRVPAPSDLPPLGAASMVKPAAPPAELDASP
EDM
>gnl|CDD|185770 cd09247, BRO1_Alix_like_2, Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like superfamily. This domain family is comprised of uncharacterized proteins. It belongs to the BRO1_Alix_like superfamily which includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20 and Rim23 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP and Bro1 function in endosomal trafficking, with HD-PTP having additional functions in cell migration. Rim20 and Rim23 play roles in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. These domains bind components of the ESCRT-III complex: CHMP4 (in the case of Alix, Brox and HD-PTP) and Snf7 (in the case of yeast Bro1 and Rim20). The Bro1-like domains of Alix, HD-PTP, Brox, and Rhophilin can bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily
YDFAKPKTKKIVFEKTFQARDSLTLEQLKELSLRRRAIIESINGSPFIALAIAREKAQYLPYLEGYLPAL
ENLVNHRDKVQLNEQLSFRWTSGLGSSKGPKAFQSDSLRFELGMVLFLYGAALRERASEVLPTEDFKEAA
THLRRAAGVFEFLAHDELPRLRGALSADERPPECTPSLALAMSLLCLAEAQAVTARKAEEKGTSPSLLAK
LHYGATQFLEEAKNVLRSLATDLKDLDPRFLRFISSCIALHEARSQLYLARRLKEAGHIGVAVGVLREAL
RNLKKKLPGSDISSPVIFRDERAEVATLLQKYEKENEVIYFEKVPDIDELPLPEGKVIVKPVPYKP
>gnl|CDD|185771 cd09248, BRO1_Rhophilin_1, Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1. This subfamily contains the Bro1-like domain of the RhoA-binding protein, Rhophilin-1. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding protein Rhophilin-2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-1 binds both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-1 contains an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. The Drosophila knockout of the Rhophilin-1 is embryonic lethal, suggesting an essential role in embryonic development. The isolated Bro1-like domain of Rhophilin-1 binds human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Rhophilin-1 lacks the V-shaped (V) domain found in many members of the BRO1_Alix_ like superfamily
MIPLGLKETKELDLPTPLKELISEHFGEDGTSYEAEIRELEDLRQAMRTPSRSEAGLELLMAYYNQLCFL
DARFFPPAKSLGLFFHWYDSLTGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGTRRAIDAFQR
AAGAFSLLRENFSNAPSPDMSTASLSMLEQLMVAQAQECIFEGLLLPLLATPQDFFAQLQLAQEAAQVAA
EYRLVHRTMAQPPVRDYVPFSWTALVHVKAEHFCALAHYHAAMALCDSSPASEGELATQEKAFLQPHTSQ
PEGPSLPQEPEERRKLGKAHLKRAILGQEEALRLHALCRILRKVDLLQAVLTQALRRSLAKYSELDREDD
FFETGEAPDIQPKTHQKPEIRAPSFSQVKVTDIF
>gnl|CDD|185772 cd09249, BRO1_Rhophilin_2, Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2. This subfamily contains the Bro1-like domain of RhoA-binding protein, Rhophilin-2. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding protein Rhophilin-1, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-2, binds both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-2 contains an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. Roles for Rhophilin-2 may include limiting stress fiber formation or increasing the turnover of F-actin in the absence of high levels of RhoA signaling activity. Rhophilin-2 lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily
LIPLGLKETKDVDFSVPLKDFILEHYSEDGSEYEDEIADLMDLRQACRTPSRDEAGVELLMSYFSQLGFL
ENRFFPPTRQMGILFTWYDSFTGVPVSQQNLLLEKASILFNIGALYTQIGTRCNRQTQAGLESAVDAFQR
AAGVLNYLKETFTHTPSYDMSPAMLSVLVKMMLAQAQECLFEKISLPGIRNEFFTLVKMAQEAAKVGEVY
MQVHTAMNQAPVKENIPYSWSSLVQVKAHHYNALAHYFVATLLIDHQLNPSDDEDKQEKALSQLYDHMPE
GLTPLTILKNKQQRRLLGKAHLRRAIMHHEEAIREASLCKKLRNIDVLQEVLSAAHNRSLLKYAQHQKED
DFLDLIDAPDIVSKTEKKVEMIIPQFSKVKVTDLF
>gnl|CDD|271158 cd09250, AP-1_Mu1_Cterm, C-terminal domain of medium Mu1 subunit in clathrin-associated adaptor protein (AP) complex AP-1. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1 subunit, which includes two closely related homologs, mu1A (encoded by ap1m1) and mu1B (encoded by ap1m2). Mu1A is ubiquitously expressed, but mu1B is expressed exclusively in polarized epithelial cells. AP-1 has been implicated in bi-directional transport between the trans-Golgi network (TGN) and endosomes. It plays an essential role in the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). Epithelial cell-specific AP-1 is also involved in sorting to the basolateral surface of polarized epithelial cells. Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). Phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding
TNAVSWRPEGIKYKKNEVFLDVIESVNLLVDLNGQVLRSEIVGAIKMRSYLSGMPELKLGLNDKVLFEAT
GRSSKGKAVELEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLSTQVKPLIWVEPTVERHSRSRVE
IMVKAKTQFKRRSTANNVEIRIPVPPDADSPRFKCSAGSVVYAPEKDALLWKIKSFPGGKEFSMRAEFGL
PSIESEEEQGTEKKAPIQVKFEIPYFTVSGLQVRYLKIIEKSGYQALPWVRYITQSGDYYIR
>gnl|CDD|271159 cd09251, AP-2_Mu2_Cterm, C-terminal domain of medium Mu2 subunit in ubiquitously expressed clathrin-associated adaptor protein (AP) complex AP-2. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, -2, -3, and -4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 2 (AP-2) medium mu2 subunit. Mu2 is ubiquitously expressed in mammals. In higher eukaryotes, AP-2 plays a critical role in clathrin-mediated endocytosis from the plasma membrane in different cells. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-2. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-2 mu2 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding. Since the Y-X-X-Phi binding site is buried in the core structure of AP-2, a phosphorylation induced conformational change is required when the cargo molecules binds to AP-2. In addition, the C-terminal domain of mu2 subunit has been shown to bind other molecules. For instance, it can bind phosphoinositides, in particular PI[4,5]P2, which might be involved in the recognition process of the tyrosine-based signals. It can also interact with synaptotagmins, a family of important modulators of calcium-dependent neurosecretion within the synaptic vesicle (SV) membrane. Since many of the other endocytic adaptors responsible for biogenesis of synaptic vesicles exist, in the absence of AP-2, clathrin-mediated endocytosis can still occur. However, the cells may not survive in the complete absence of clathrin as well as AP-2
YRKNEVFLDVVESVNLLMSPQGQVLRADVDGVIVMKTYLSGMPECKFGLNDKLVLESEGKEKSGSKSGKG
SVELDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRYRVTENINLPFRVIPLVKEVGRTKLEYKVKIKS
NFPPKLLATNVVVRIPVPKNTAKVTINVSKGKAKYDPEENAIVWKIKKFAGMTESTLSAEVELLSTTSKK
KKWSRPPISMDFEVPMFTASGLRVRYLKVFEKSNYKTVKWVRYITRAGSYEIR
>gnl|CDD|271160 cd09252, AP-3_Mu3_Cterm, C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3 subunit, which includes two closely related homologs, mu3A (P47A, encoded by ap3m1) and mu1B (P47B, encoded by ap3m2). Mu3A is ubiquitously expressed, but mu3B is specifically expressed in neurons and neuroendocrine cells. AP-3 is particularly important for targeting integral membrane proteins to lysosomes and lysome-related organelles at trans-Golgi network (TGN) and/or endosomes, such as the yeast vacuole, fly pigment granules and mammalian melanosomes, platelet dense bodies and the secretory lysosomes of cytotoxic T lymphocytes. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding
VPWRRAGVKYTNNEIYFDVVEEIDAIVDKSGKPVSGEVRGEIDCNSRLSGMPDLLLSFNNPRLLDDPSFH
PCVRYSRWESERVLSFIPPDGKFTLMSYRVDLNSLVSLPVYVKPQISFSGSSGRFEITVGSRQNLGKSIE
NVVVEIPLPKGVKSLRLTASHGSFSFDSSTKTLVWNIGKLTPGKTPTLRGSVSLSSGLEAPSESPSISVQ
FKIPGYTPSGLKVDSLDIYNEKYKPFKGVKYITKAGKYQVR
>gnl|CDD|271161 cd09253, AP-4_Mu4_Cterm, C-terminal domain of medium Mu4 subunit in adaptor protein (AP) complex AP-4. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 4 (AP-4) medium mu4 subunit. AP-4 plays a role in signal-mediated trafficking of integral membrane proteins in mammalian cells. Unlike other AP complexes, AP-4 is found only in mammals and plants. It is believed to be part of a nonclathrin coat, since it might function independently of clathrin, a scaffolding protein participating in the formation of coated vesicles. Recruitment of AP-4 to the trans-Golgi network (TGN) membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1) or a related protein. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. One of the most important sorting signals binding to mu subunits of AP complexes are tyrosine-based endocytotic signals, which are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. However, AP-4 does not bind most canonical tyrosine-based signals except for two naturally occurring ones from the lysosomal membrane proteins CD63 and LAMP-2a. It binds YX [FYL][FL]E motif, where X can be any residue, from the cytosolic tails of amyloid precursor protein (APP) family members in a distinct way
LSSRGSQDKRNEIFVDVLERLSVVFNANGQVLNSEIDGSIQMKSYLPGNPELRLALNEDLVIGKRENRAY
YSAVVLDDCNFHESVDLEEFESDRTLSLTPPDGEFTLMNYRISGEFKPPFRVFPSVEETSPYKLELVLKL
RADFPPKSTATNVVVRIPLPKGTTSVSCELGSGASGQSAEYKEKEKLVLWNIKKFPGGTELTLRAKITLS
SPVSSSVRKEIGPISLSFEIPMYNVSGLQVRYLRILERSSSYNPHRWVRYVTQSSSYVCRI
>gnl|CDD|271162 cd09254, AP_delta-COPI_MHD, Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit. COPI complex-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. COPI complex-coated vesicles consist of a small GTPase, ADP-ribosylation factor 1 (ARF1) and a heteroheptameric coatomer composed of two subcomplexes, F-COPI and B-COPI. ARF1 regulates COPI vesicle formation by recruiting the coatomer onto Golgi membranes to initiate its coat function. Coatomer complexes then bind cargo molecules and self-assemble to form spherical cages that yield COPI-coated vesicles. The heterotetrameric F-COPI subcomplex contains beta-, gamma-, delta-, and zeta-COP subunits, where beta- and gamma-COP subunits are related to the large AP subunits, and delta- and zeta-COP subunits are related to the medium and small AP subunits, respectively. Due to the sequence similarity to the AP complexes, the F-COPI subcomplex might play a role in the cargo-binding. The heterotrimeric B-COPI contains alpha-, beta-, and epsilon-COP subunits, which are not related to the adaptins. This subcomplex is thought to participate in the cage-forming and might serve a function similar to that of clathrin. This family corresponds to the mu homology domain of delta-subunit of COPI complex (delta-COP), which is distantly related to the C-terminal domain of mu chains among AP complexes. The delta-COP subunit appears tightly associated with the beta-COP subunit to confer its interaction with ARF1. In addition, both delta- and beta-COP subunits contribute to a common binding site for arginine (R)-based signals, which are sorting motifs conferring transient endoplasmic reticulum (ER) localization to unassembled subunits of multimeric membrane proteins
EGVHITVEEKISATLSRDGGLESLEVKGTLSLRINDEELAHIKLQLANNSDKGFQFKTHPNVDKKLFTSD
SVLGLKDPSKPFPVNDPVGVLKWRLQGSDESLLPLTINCWPSESGGGCDVTIEYELNRDDLELNDVVISI
PLPSGDAPVVNSIDGNYEYDSRKNVLEWKIPVIDASNSSGSLEFSIPADDEDAFFPISVSFTSSKTFCGV
KVVEVVSADDGEPVPFSLETSLVADKY
>gnl|CDD|271163 cd09255, AP-like_stonins_MHD, Mu homology domain (MHD) of adaptor-like proteins (AP-like), stonins. A small family of proteins named stonins has been characterized as clathrin-dependent AP-2 mu2 chain related factors, which may act as cargo-specific sorting adaptors in endocytosis. Stonins include stonin 1 and stonin 2, which are only mammalian homologs of Drosophila stoned B, a presynaptic protein implicated in neurotransmission and synaptic vesicle (SV) recycling. They are conserved from C. elegans to humans, but are not found in prokaryotes or yeasts. This family corresponds to the mu homology domain of stonins, which is distantly related to the C-terminal domain of mu chains among AP complexes. Due to the low degree of sequence conservation of the corresponding binding site, the mu homology domain of stonins is unable to recognize tyrosine-based endocytic sorting signals. To data, little is known about the localization and function of stonin 1. Stonin 2, also known as stoned B, acts as an AP-2-dependent synaptotagmin-specific sorting adaptors for SV endocytosis. Stoned A is not a stonin. It is structurally unrelated to the adaptins and does not appear to have mammalian homologs. It is not included in this family
YRDRGITYREDEITVDVTDEFHGKVTKTGEIKKLGVTVQIHILSFVTGDPECVLGLNDLEVEGREVVRRQ
DIMPSSTDQWIKLHNCEFHSCVDVEEFEQSRSIKFHPLDACRFELMRFRTRYNKKNLPLTLKSVVSVKGA
HVELRADVRMSGYHSRNPLAQVPCENIMIRFPVPESWVPAFRTEKRFREKSLKSKKNKKASGGSTAESLS
EPVIEVSVGSAKYEHAYRAVVWRIDRLPDKNSAADTPHTFSCRLDLASDLEIPSSTYPHAEVEFTMPSTT
ASKTTVRSISVSNKNIPEKWVRYRAHYSYKVEIEV
>gnl|CDD|271164 cd09256, AP_MuD_MHD, Mu-homology domain (MHD) of a adaptor protein (AP) encoded by mu-2 related death-inducing gene, MuD (also known as MUDENG). This family corresponds to the MHD found in a protein encoded by MuD (also known as Adapter-related protein complex 5 subunit mu-1), which is distantly related to the C-terminal domain of the mu2 subunit of AP complexes that participates in clathrin-mediated endocytosis. MuD is evolutionary conserved from mammals to amphibians. It is able to induce cell death by itself and plays an important role in cell death in various tissues
PAWKPVLLKGKQQLSFKIRETVRAAQYDRDDISDVWSVFGEVRCKAELEGLPEVTVSLSVPANSPLQAII
VHPCVQSPESGMLAFSGPYKIRFSPPLGNFVLCRYQSQSVPVPPILGFYQMKGDEKHVKFLIQLKLHESV
KNSFEYCEVHIPFPNRGLIKHVSATPSNGQLEVSKEKRRLVWNIGQKFPKSLEATLSGTVNFGSESNRRA
DPEDPFCVGLNAYVKLFFKISDYTLSGCSIDPKSVQIYPSAKTKIITSREVVSSDYIIWNSLGDAP
>gnl|CDD|271165 cd09257, AP_muniscins_like_MHD, Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins. This family corresponds to the MHD found in muniscins, a novel family of endocytic adaptor proteins. The term, muniscins, has been assigned to name the MHD of proteins with both EFC/F-BAR domain and MHD. These two domains are responsible for the membrane-tubulation activity associated with transmembrane cargo proteins. Members in this family include an endocytic adaptor Syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related uncharacterized proteins. Syp1 is a poorly characterized yeast protein with multiple biological functions. Syp1 contains an N-terminal EFC/F-BAR domain that induces membrane tabulation, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD that can directly binds to the endocytic adaptor/scaffold protein Ede1 or a transmembrane stress sensor cargo protein Mid2. Thus, Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress response. Syp1 shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, the membrane-sculpting F-BAR domain-containing Fer/Cip4 homology domain-only proteins 1 and 2 (FCHo1/2). FCHo1/2 represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They are required for plasma membrane clathrin-coated vesicle (CCV) budding and marked sites of CCV formation. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Another mammalian neuronal-specific protein, neuronal-specific transcript Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 [SGIP1] does not contain EFC/F-BAR domain, but does have a PRD and a C-terminal MHD and has been classified into this family as well. SGIP1 is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15
GVKAALTEELNAEFKGSSLQSVGVEGEVQLAVPSSDAKPKPAPFNLRLNDASSLEKAAPNVAFLNSVPSG
SSPGEFLVNTKAIRASEVGSPILKYSCSSKLRPVPLRVQTVWRCESHQTSVMLQYVSNPSLPGPLQDVTV
IVNVPPGAGENLKSSPGAVWNEEKRRLTWKLPELGVNGEGGELRARFQIDAGQTAEKVPFPVLVRCLSEG
STLSGLGLEVVALEEEWAFIEVKVTRRFGVYHAE
>gnl|CDD|271166 cd09258, AP-1_Mu1A_Cterm, C-terminal domain of medium Mu1A subunit in ubiquitously expressed clathrin-associated adaptor protein (AP) complex AP-1. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1A subunit encoded by ap1m1 gene, which is ubiquitously expressed in all mammalian tissues and cells. AP-1 has been implicated in bidirectional transport between the trans-Golgi network (TGN) and endosomes. It is involved in the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). The ubiquitous AP-1 is recruited to the TGN membrane, as well as to immature secretory granules. Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). Phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1A subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding
VTNAVSWRSEGIKYRKNEVFLDVIESVNLLVSANGNVLRSEIVGSIKMRVYLSGMPELRLGLNDKVLFEN
TGRGKSKSVELEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLNTHVKPLIWIESVIERHSHSRVE
YMIKAKSQFKRRSTANNVEIHIPVPNDADSPKFKTTVGSVKYVPENSEIVWSIKSFPGGKEYLMRAHFGL
PSVESEEKEGRPPISVKFEIPYFTTSGIQVRYLKIIEKSGYQALPWVRYITQNGDYQLRT
>gnl|CDD|271167 cd09259, AP-1_Mu1B_Cterm, C-terminal domain of medium Mu1B subunit in epithelial cell-specific clathrin-associated adaptor protein (AP) complex AP-1. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1B subunit encoded by ap1m2 gene exclusively expressed in polarized epithelial cells. Epithelial cell-specific AP-1 is used to sort proteins to the basolateral plasma membrane, which involves the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). The phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1B subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic reside-binding. Besides, AP-1 mu1B subunit mediates the basolateral recycling of low-density lipoprotein receptor (LDLR) and transferrin receptor (TfR) from the sorting endosomes, where the basolateral sorting signal does not belong to the tyrosine-based signals. Thus, the binding site in mu1B subunit of AP-1 for the signals of LDLR and TfR might be distinct from that for YXXPhi signals
TNAVSWRSEGIKYKKNEVFIDVIESVNVLVNANGSVLSSEIVGCIKLKVFLSGMPELRLGLNDRVLFELT
GRDKNKTVELEDVKFHQCVRLSRFENDRTISFIPPDGDFELMSYRLNTQVKPLIWIESVIEKFSHSRVEI
MVKAKGQFKKQSVANNVEIRVPVPSDADSPKFKTSVGSAKYVPEKNVVVWSIKSFPGGKEYLMRAHFGLP
SVENEELEGKPPITVKFEIPYFTVSGIQVRYMKIIEKSGYQALPWVRYITQSGDYQLR
>gnl|CDD|211371 cd09260, AP-3_Mu3A_Cterm, C-terminal domain of medium Mu3A subunit in ubiquitously expressed adaptor protein (AP) complex AP-3. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3A subunit encoded by ap3m1gene. Mu3A is ubiquitously expressed in all mammalian tissues and cells. It appears to be localized to the trans-Golgi network (TGN) and/or endosomes and participates in trafficking to the vacuole/lysosome in yeast, flies, and mammals. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of ubiquitous AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3A subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding
IPWRRAGVKYTNNEAYFDVVEEIDAIIDKSGSTVFAEIQGVIDACIKLSGMPDLSLSFMNPRLLDDVSFH
PCIRFKRWESERVLSFIPPDGNFRLISYRVSSQNLVAIPVYVKHNISFKENSSCGRFDITIGPKQNMGKT
IEGITVTVHMPKVVLNMNLTPTQGSYTFDPVTKVLAWDVGKITPQKLPSLKGLVNLQSGAPKPEENPSLN
IQFKIQQLAISGLKVNRLDMYGEKYKPFKGVKYITKAGKFQVRT
>gnl|CDD|211372 cd09261, AP-3_Mu3B_Cterm, C-terminal domain of medium Mu3B subunit in neuron-specific adaptor protein (AP) complex AP-3. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3B subunit encoded by ap3m2 gene. Mu3B is specifically expressed in neurons and neuroendocrine cells. Neuron-specific AP-3 appears to be involved in synaptic vesicle biogenesis from endosomes in neurons and plays an important role in synaptic transmission in the central nervous system. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of neuron-specific AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3B subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding
VPWRRTGVKYTNNEAYFDVIEEIDAIIDKSGSTITAEIQGVIDACVKLTGMPDLTLSFMNPRLLDDVSFH
PCVRFKRWESERILSFIPPDGNFRLLSYHVSAQNLVAIPVYVKHNISFREGSSLGRFEITLGPKQTMGKT
VEGVTVTSQMPKGVLNMSLTPSQGTYTFDPVTKLLSWDVGKINPQKLPSLKGSMSLQAGASKPDENPTIN
LQFKIQQLAISGLKVNRLDMYGEKYKPFKGIKYMTKAGKFQVRT
>gnl|CDD|271168 cd09262, AP_stonin-1_MHD, Mu homology domain (MHD) of adaptor-like protein (AP-like), stonin-1 (also called Stoned B-like factor). A small family of proteins named stonins has been characterized as clathrin-dependent AP-2 mu2 chain related factors, which may act as cargo-specific sorting adaptors in endocytosis. Stonins include stonin 1 and stonin 2, which are the only mammalian homologs of Drosophila stoned B, a presynaptic protein implicated in neurotransmission and synaptic vesicle (SV) recycling. They are conserved from C. elegans to humans, but are not found in prokaryotes or yeasts. This family corresponds to the mu homology domain of stonin 1, which is distantly related to the C-terminal domain of mu chains among AP complexes. Due to the low degree of sequence conservation of the corresponding binding site, the mu homology domain of stonin-1 is unable to recognize tyrosine-based endocytic sorting signals. To data, little is known about the localization and function of stonin-1
VSQPKRNYEEQELSLEIVDNFWGKVTKEGKVVESAVITQIYCLCFVNGPGECFLTLNDLELLKRDESYGE
KEAGKKWIEILDCHFHKCVNEQEFEQSRIIKFSPLDACRAELMRFKTAYNGTQLPFSVKATVVVQGAYVE
LQAFLNMASTALSFGVSDSHPLCENVVIRFPVPAQWIKALWTMNLQRQKSLKAKMNRRACLGALRETESR
PVIQVSVGTAKYESAYSAVVWKIDRLPDKNSSLDHPHSLSYKLELGSDQEIPSDWYPFATVQFEVMDTCA
SQTEVKSLGTESDMQPQKHVTQWARYHCQAEFYK
>gnl|CDD|271169 cd09263, AP_stonin-2_MHD, Mu homology domain (MHD) of adaptor-like protein (AP-like), stonin-2. A small family of proteins named stonins has been characterized as clathrin-dependent AP-2 mu2 chain related factors, which may act as cargo-specific sorting adaptors in endocytosis. Stonins include stonin 1 and stonin 2, which are the only mammalian homologs of Drosophila stoned B, a presynaptic protein implicated in neurotransmission and synaptic vesicle (SV) recycling. They are conserved from C. elegans to humans, but are not found in prokaryotes or yeasts. This family corresponds to the mu homology domain of stonin 2, which is distantly related to the C-terminal domain of mu chains among AP complexes. Due to the low degree of sequence conservation of the corresponding binding site, the mu homology domain of stonin-2 is unable to recognize tyrosine-based endocytic sorting signals. It acts as an AP-2-dependent synaptotagmin-specific sorting adaptor for SV endocytosis
LSTVGLNYTEEEITVDVRDEFYGILSKGDSRILQHLVLTRINMLSFLSGLAECRLGLNDILIKGNEIVSR
QDIMPTTTTKWIKLRDCRFHECVDEDEFNNSRAILFNPLDACRFELMRFRTVFAEKTLPFTLRTAASVNG
AEVEVQSWLVMSTGFSSNRDPLTQVPCENVMIRYPVPEEWVKNFRRESVLGEKSLKAKVNKGASFGSTST
SGSEPVMRVTLGTAKYEHAFNSIVWRINRLPDKNSASGHPHCFFCHLELGSDREVPSTFECHVEVEFDMP
TTSASKAAVRSISVEDKTDVRKWVNYSAHYSYQVAVEQ
>gnl|CDD|271170 cd09264, AP_Syp1_MHD, mu-homology domain (MHD) of adaptor protein (AP), Syp1, and related proteins. This family corresponds to the MHD found in a novel endocytic adaptor Syp1 and related proteins. Syp1 is a poorly characterized yeast protein with multiple biological functions. It was originally identified as a suppressor of a yeast profiling deletion and later as a suppressor of arf3delta (Arf3 is the yeast homologue of Arf6, a mammalian regulator of endocytosis). Syp1 can bind to septins and physically link with cell polarity factors. It also directly binds to the endocytic adaptor/scaffold protein Ede1, and plays a role in endocytosis. Further studies show that Syp1 is itself an endocytic adaptor protein contributing to stress responses. Its mu-homology domain at the C-terminus binds to the cargo protein Mid2, a transmembrane stress sensor protein, and mediates Mid2 internalization. In addition, Syp1 contains an EFC/F-BAR domain which can induce membrane tabulation
GLNASIVETVNASFKDGQLTKSSVIGEVALNYNSDPNVTPTSNINVRLNNFQVLEKVLLNPTFVEPVVSP
NEFTVNPSLITSKTLGAFKYQLHLDPSASQCPIIVTPVWKFEEHQASLIIFVKLNPSFRNSESLTLENLV
LSVALDGAVKATSAQSKPQGSFSREKSRITWRLPDPTVLDDSEEKLIARFMTEGLGSEAPGGVEARFEIT
DPDAGSGLTISVFETTENSERSSAESAGEWKEVPTSRKLVSGNYSSH
>gnl|CDD|271171 cd09265, AP_Syp1_like_MHD, Mu-homology domain (MHD) of endocytic adaptor protein (AP), Syp1. This family corresponds to the MHD found in the metazoan counterparts of yeast Syp1, which includes two ubiquitously expressed membrane-sculpting F-BAR domain-containing Fer/Cip4 homology domain-only proteins 1 and 2 (FCH domain only 1 and 2, or FCHo1/FCHo2), neuronal-specific SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related uncharacterized proteins. FCHo1/FCHo2 represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They are required for plasma membrane clathrin-coated vesicle (CCV) budding and marked sites of CCV formation. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Both FCHo1/FCHo2 contain an N-terminal EFC/F-BAR domain that induces membrane tabulation, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD responsible for the binding of eps15 and intersectin. Another mammalian neuronal-specific protein, neuronal-specific transcript Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 [SGIP1] does not contain EFC/F-BAR domain, but does have a PRD and a C-terminal MHD and has been classified into this family as well. SGIP1 is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15
PVAAAFTETVHAYFKGADPSKCIVKITGDMMMSFPAGIIRLLTSNPTPAPLTFRLKNASRLEHVLPNKQL
IFSDPSQSDSETKDFWFNMPALTTYLKRQAEQNPTASYYNVDVLKYQVSPTGPQSTPLQLASYWKCEPSS
TDLRVDYKYNPEAMAIATPLLNVQFSVPVDGGVTNVQSEPPATWNAEQKRLLWKLPDISQNSEGGGVGSL
RARFELSEGPSKPAPLAVQFNSEGTTLSGVDIELVGSGYRLSLIKKRFAAGKYLCD
>gnl|CDD|271172 cd09266, SGIP1_MHD, mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 (also known as endophilin-3-interacting protein, SGIP1) and similar proteins. This family corresponds to the MHD found in mammalian neuronal-specific transcript SGIP1 and similar proteins. Unlike other members in this family, SGIP1 does not contain EFC/F-BAR domain, but does have a proline-rich domain (PRD) and a C-terminal MHD. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis, and is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15
PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQL
LCCDNTQAKGNAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSS
TDLRIDYKYNGDAMTTPVALNNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGS
LLARFQLSEGPSKPAPLAVQFTSEGSTLSGCDIELVGPGYRFSLIKKRFAAGKYLAD
>gnl|CDD|211378 cd09267, FCHo2_MHD, mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 (FCH domain only 2 or FCHo2) and similar proteins. This family corresponds to the MHD found in the ubiquitously expressed mammalian membrane-sculpting FCHo2 and similar proteins. FCHo2 represents a key initial protein that ultimately controls cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. It is required for plasma membrane clathrin-coated vesicle (CCV) budding and marks sites of CCV formation. It binds specifically to the plasma membrane and recruits the scaffold proteins eps15 and intersectin, which subsequently engages the adaptor complex AP2 and clathrin, leading to coated vesicle formation. FCHo2 contains an N-terminal EFC/F-BAR domain, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD. The crescent-shaped EFC/F-BAR domain can form an antiparallel dimer structure that binds PtdIns(4,5)P2-enriched membranes and can polymerize into rings to generate membrane tubules. The MHD is structurally related to the cargo-binding mu2 subunit of adaptor complex 2 (AP-2) and is responsible for the binding of eps15 and intersectin
PVAVALTESVNAYFKGADPTKCIVKITGDMTVSFPSGIIKVFTSNPSPAVLCFRLKNTSRLEQILPNAQL
LYSDPSQSDSNTKDFWMNMQAVTVYLKKSSEQNPAASYYNVDILKYQVSSNGIQSTPLNLATYWKCSAST
TDLRVDYKYNPEAMQPPSPLSNVQVLVPVDGGVTNMQSLPPAIWNAEQMKALWKLSSISEKSENGGSGSL
RAKFELSEGPSKPATLAVQFFSEGSTLSGVDMELVGTGYRLSLNKKRFATGRYMADC
>gnl|CDD|271173 cd09268, FCHo1_MHD, mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 (FCH domain only 1 or FCHo1, also known as KIAA0290) and similar proteins. This family corresponds to the MHD found in ubiquitously expressed mammalian membrane-sculpting FCHo1 and similar proteins. FCHo1 represents a key initial protein that ultimately controls cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. It is required for plasma membrane clathrin-coated vesicle (CCV) budding and marks sites of CCV formation. It binds specifically to the plasma membrane and recruits the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. FCHo1 contains an N-terminal EFC/F-BAR domain, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD. The crescent-shaped EFC/F-BAR domain can form an antiparallel dimer structure that binds PtdIns(4,5)P2-enriched membranes and can polymerize into rings to generate membrane tubules. The MHD is structurally related to the cargo-binding mu2 subunit of adaptor complex 2 (AP-2) and is responsible for the binding of eps15 and intersectin. Unlike other F-BAR domain containing proteins, FCHo1 has neither the Src homology 3 (SH3) domain nor any other known domain for interaction with dynamin and actin cytoskeleton. However, it can periodically accumulate at the budding site of clathrin. FCHo1 may utilize a unique action mode for vesicle formation as compared with other F-BAR proteins
PVAAAFTEYVHAYFRGGALEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSEL
LFSDPSQSDPNTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTS
TDVSLDYRQNPATAPATFLTDVQILLPLDEPFTNLQSQPPAAWNAEERRLHWQLPHESAGNEHDGSGRLC
ASWQPLHAPSRPTSAAAQFTSEGSTLSGVDIELVGSGYRMSLVKKRFATGKYLVC
>gnl|CDD|185703 cd09269, deoxyribose_mutarotase, deoxyribose mutarotase_like. Salmonella enterica serovar Typhi DeoM (earlier named as DeoX) is a mutarotase with high specificity for deoxyribose. It is encoded by one of four genes beonging to the deoK operon. This operon has also been found in Escherichia coli where it is more common in pathogenic than in commensal strains and is associated with pathogenicity. It has been found on a pathogenicity island from a human blood isolate AL863 and confers the ability to use deoxyribose as a carbon source; deoxyribose is not fermented by non-pathogenic E.coli K-12. Proteins in this family are members of the aldose-1-epimerase superfamily. Aldose 1-epimerases, or mutarotases, are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. Site directed mutagenesis of this latter histidine residue renders Salmonella enterica DeoM inactive
HLVVLPFMGQMIWDAEFDGRDLTMKNMFDQPRPATEIVDTYGCFAFHSGLLANGCPGPEDTHPLHGEFPC
APMDEAWLEVGEDASGDYLALTGEYEYVQGFGHHYLAQPSVTLRAGSALFDIGMDVTNLSAQPMPLMYMC
HMNYAYVEGARIVQNLPDEAFVLRRSVPAHVKPTPAWLAYNEALVADPARGDVLDKPDLYDPEIVFFADD
LGKYTGWAHFMMVHPDGDAFYTRFSTAEFPYATRWILYNGDQQVAAFALPATCRPEGYLAAKEAGTLRTL
APGETRRFSVTTG
>gnl|CDD|187751 cd09270, RNase_H2-B, Ribonuclease H2-B is a subunit of the eukaryotic RNase H complex which cleaves RNA-DNA hybrids. Ribonuclease H2B is one of the three proteins of eukaryotic RNase H2 complex that is required for nucleic acid binding and hydrolysis. RNase H is classified into two families, type I (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type II (prokaryotic RNase HII and HIII, and eukaryotic RNase H2/HII). RNase H endonucleolytically hydrolyzes an RNA strand when it is annealed to a complementary DNA strand in the presence of divalent cations, in DNA replication and repair. The enzyme can be found in bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite a lack of evidence for homology from sequence comparisons, type I and type II RNase H share a common fold and similar steric configurations of the four acidic active-site residues, suggesting identical or very similar catalytic mechanisms. Eukaryotic RNase HII is active during replication and is believed to play a role in removal of Okazaki fragment primers and single ribonucleotides in DNA-DNA duplexes. Eukaryotic RNase HII is functional when it forms a complex with RNase H2B and RNase H2C proteins. It is speculated that the two accessory subunits are required for correct folding of the catalytic subunit of RNase HII. Mutations in the three subunits of human RNase HII cause neurological disorder
VFILPKEATDESQLRIVTLPHPRTGKPTRYLFCPDGQLYELTAFKESKAPRSWFIGNGTVLQDGSLYVAT
PFDPLFLLLPILYKADNKFAGKFLTLDDILDDLSSPSSHLLEDLPLPILESSLAKICDVKEEGDDKFYKY
SDEKLLAWLLKKVERLKKKELDIKEAEAARDKKKSNNAEEEKKKKKKKSAKKKKLKKVAAVGMKAISSFF
K
>gnl|CDD|187752 cd09271, RNase_H2-C, Ribonuclease H2-C is a subunit of the eukaryotic RNase H complex which cleaves RNA-DNA hybrids. Ribonuclease H2C is one of the three protein of eukaryotic RNase H2 complex that is required for nucleic acid binding and hydrolysis. RNase H is classified into two families, type I (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type II (prokaryotic RNase HII and HIII, and eukaryotic RNase H2/HII). RNase H endonucleolytically hydrolyzes an RNA strand when it is annealed to a complementary DNA strand in the presence of divalent cations, in DNA replication and repair. The enzyme can be found in bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite a lack of evidence for homology from sequence comparisons, type I and type II RNase H share a common fold and similar steric configurations of the four acidic active-site residues, suggesting identical or very similar catalytic mechanisms. Eukaryotic RNase HII is active during replication and is believed to play a role in removal of Okazaki fragment primers and single ribonucleotides in DNA-DNA duplexes. Eukaryotic RNase HII is functional when it forms a complex with RNase H2B and RNase H2C proteins. It is speculated that the two accessory subunits are required for correct folding of the catalytic subunit of RNase HII. Mutations in the three subunits of human RNase HII cause neurological disorder
HLLPCKIQYDGPANVSEYFKPKTDGDNEEGTLVAYFRGRKLVGKTVSLPEGYSGYVLSKTEKPDSEEKLE
EEEEVRNLEITATFDEVTVWNHD
>gnl|CDD|260004 cd09272, RNase_HI_RT_Ty1, Ty1/Copia family of RNase HI in long-term repeat retroelements. Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms including bacteria, archaea, and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD) are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1, and the vertebrate retroviruses. The Ty1/Copia family is widely distributed among the genomes of plants, fungi, and animals. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription
EGYSDADWAGDPDDRRSTSGYVFFLGGGPISWKSKKQTTVALSSTEAEYIALAEAAKEALWLRRLLEELG
IPLDGPTTIYCDNQSAIALAKNPVFHSRTKHIDIRYHFIREKVEKGEIKVEYVPTEDQLADILTKPLPRP
>gnl|CDD|260005 cd09273, RNase_HI_RT_Bel, Bel/Pao family of RNase HI in long-term repeat retroelements. Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryote. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. Bel/Pao family has been described only in metazoan genomes. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription
TVFTDGSSFKAGYAIVSGTEIVEAQPLPPGTSAQRAELIALIQALELAKGKPVNIYTDSAYAVHALHLLE
TIGIERGFLKSIKNLSLFLQLLEAVQRPKPVAIIHIRAHSKLPGPLAEGNAQADAAAKQAA
>gnl|CDD|260006 cd09274, RNase_HI_RT_Ty3, Ty3/Gypsy family of RNase HI in long-term repeat retroelements. Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. Ty3/Gypsy family widely distributed among the genomes of plants, fungi and animals. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription
ILETDASDYGIGAVLSQEDDDGKERPIAFFSRKLTPAERNYSTTEKELLAIVWALKKFRHYLLGRPFTVY
TDHKALKYLLTQKDLNGRLARWLLLLSEFDFEIEYRPGKENVVADALSRLP
>gnl|CDD|260007 cd09275, RNase_HI_RT_DIRS1, DIRS1 family of RNase HI in long-term repeat retroelements. Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. The structural features of DIRS1-group elements are different from typical LTR elements. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription
VLFTDASLSGWGAYLLNSRAHGPWSADERNKHINLLELKAVLLALQHFAAELKNRKILIRTDNTTAVAYI
NKQGGTSSPPLLALARQILLWCEQRNIWLRASHIPGVLNTEADRLSRLGL
>gnl|CDD|260008 cd09276, Rnase_HI_RT_non_LTR, non-LTR RNase HI domain of reverse transcriptases. Ribonuclease H (RNase H) is classified into two families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). Ribonuclease HI (RNase HI) is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as an adjunct domain to the reverse transcriptase gene in retroviruses, long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. The position of the RNase domain of non-LTR and LTR transposons is at the carboxyl terminal of the reverse transcriptase (RT) domain and their RNase domains group together, indicating a common evolutionary origin. Many non-LTR transposons have lost the RNase domain because their activity is at the nucleus and cellular RNase may suffice; however LTR retrotransposons always encode their own RNase domain because it requires RNase activity in RNA-protein particles in the cytoplasm. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription
VIYTDGSKLEGSVGAGFVIYRGGEVISRSYRLGTHASVFDAELEAILEALELALATARRARKVTIFTDSQ
SALQALRNPRRSSGQVILIRILRLLRLLKAKGVKVRLRWVPGHVGIEGNEAADRLAKEAAS
>gnl|CDD|260009 cd09277, RNase_HI_bacteria_like, Bacterial RNase HI containing a hybrid binding domain (HBD) at the N-terminus. Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, Type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Prokaryotic RNase H varies greatly in domain structures and substrate specificities. Prokaryotes and some single-cell eukaryotes do not require RNase H for viability. Some bacteria distinguished from other bacterial RNase HI in the presence of a hybrid binding domain (HBD) at the N-terminus which is commonly present at the N-termini of eukaryotic RNase HI. It has been reported that this domain is required for dimerization and processivity of RNase HI upon binding to RNA-DNA hybrids
VIAYVDGSYNKETKKYGYGVVIIKNGKEEEFSGSGNDPEYASMRNVAGEIKGAMKAIKYAIENGIKKITI
YYDYEGIEKWATGEWKANKELTKEYKEFMQKYKKKIKIEFVKVKAHSGDKYNELADKLAKKAL
>gnl|CDD|260010 cd09278, RNase_HI_prokaryote_like, RNase HI family found mainly in prokaryotes. Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD), residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Prokaryotic RNase H varies greatly in domain structures and substrate specificities. Prokaryotes and some single-cell eukaryotes do not require RNase H for viability
EIVIYTDGACLGNPGPGGWAAVIRYGDHEKELSGGEPGTTNNRMELTAAIEALEALKEPCPVTIYTDSQY
VINGITKWIKGWKKNGWKTADGKPVKNRDLWQELDALLAGHKVTWEWVKGHAGHPGNERADRLANKAAD
>gnl|CDD|260011 cd09279, RNase_HI_like, RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI. Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Most archaeal genomes contain only type 2 RNase H (RNase HII); however, a few contain RNase HI as well. Although archaeal RNase HI sequences conserve the DEDD active-site motif, they lack other common features important for catalytic function, such as the basic protrusion region. Archaeal RNase HI homologs are more closely related to retroviral RNase HI than bacterial and eukaryotic type I RNase H in enzymatic properties
WTLYFDGASRGNPGPAGAGVVIYSPGGEVLELSERLGFPATNNEAEYEALIAGLELALELGAEKLEIYGD
SQLVVNQLNGEYKVKNERLKPLLEKVLELLAKFELVELKWIPREQNKEADALANQALD
>gnl|CDD|260012 cd09280, RNase_HI_eukaryote_like, Eukaryotic RNase H is essential and is longer and more complex than their prokaryotic counterparts. Ribonuclease H (RNase H) is classified into two families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. RNase H is widely present in various organisms, including bacteria, archaea and eukaryote and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. Eukaryotic RNase H is longer and more complex than in prokaryotes. Almost all eukaryotic RNase HI have highly conserved regions at their N-termini called hybrid binding domain (HBD). It is speculated that the HBD contributes to binding the RNA/DNA hybrid. Prokaryotes and some single-cell eukaryotes do not require RNase H for viability, but RNase H is essential in higher eukaryotes. RNase H knockout mice lack mitochondrial DNA replication and die as embryos
VVYTDGSCLNNGKPGARAGIGVYFGPGDPRNVSEPLPGRKQTNNRAELLAVIHALEQAPEEGIRKLEIRT
DSKYAINCITKWIPKWKKNGWKTSKGKPVKNQDLIKELDKLLRKRGIKVKFEHVKGHSGDPGNEEADRLA
REGAD
>gnl|CDD|187753 cd09281, UPF0066, Escherichia coli YaeB and related proteins. Uncharacterized protein family UPF0066. This domain includes Escherichia coli YeaB, Archeoglobus fulgidus AF0241, and Agrobacterium tumefaciens VirR. Proteins with this domain are probable S-adenosylmethionine-dependent methyltransferases but they have not been functionally characterized and the substrate is unknown
PIGVVRSPFKERFGAPQQGLVGGVESEIEIDPEYAEGLKGLEEFSHIWVLYWFHKADREELRVTVRPPPR
GDNPKVGVFATRSPHRPNPIGLSVVRLLKVEGNRLHVSGLDALDGTPVLDIKPY
>gnl|CDD|185681 cd09286, NMNAT_Eukarya, Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic. Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis. This subfamily consists strictly of eukaryotic members and includes secondary structural elements not found in all NMNATs
VVLLACGSFNPITNMHLRMFELARDHLHETGRYEVVGGIISPVNDAYGKKGLASAKHRVAMCRLAVQSSD
WIRVDDWESLQPEWMRTAKVLRHHREEINNKYGGIEGAAKRVLDGSRREVKIMLLCGADLLESFGIPGLW
KDADLEEILGEFGLVVVERTGSDPENFIASSDILRKYQDNIHLVKDWIPNDISSTKVRRALRRGMSVKYL
LPDPVIEYIEQHQLY
>gnl|CDD|185682 cd09287, GluRS_non_core, catalytic core domain of non-discriminating glutamyl-tRNA synthetase. Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme
KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDPEAYDMIPEDLEWLGVKWD
EVVIASDRIELYYEYARKLIEMGGAYVHPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQ
RYIYEYFGWEYPETIHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFII
EVGVKQTDATISWENLYAINRKLIDPRANR
>gnl|CDD|187746 cd09288, Photosystem-II_D2, D2 subunit of photosystem II (PS II). Photosystem II (PS II), D2 subunit. PS II is a multi-subunit protein found in the photosynthetic membranes of plants, algae, and cyanobacteria. It utilizes light-induced electron transfer and water-splitting reactions to produce protons, electrons, and molecular oxygen. The protons generated are instrumental in ATP formation. Molecular dioxygen is released as a by-product. PS II can be described as containing two parts: the photochemical part and the catalytic part. The photochemical portion promotes the fast, efficient light-induced charge separation and stabilization that occur when light is absorbed by chlorophyll. The catalytic portion, where water is oxidized, involves a cluster of Mn ions close to a redox-active tyrosine residue. The Mn cluster and its ligands form a functional unit called the oxygen-evolving complex (OEC) or the water-oxidizing complex (WOC). The D1 and D2 subunits are a pair of intertwined polypeptides. They contain all the cofactors involved directly in water oxidation and plastoquinone reduction. D1 and D2 are highly homologous and are also similar to the L and M proteins in bacterial photosynthetic reaction centers
LFDLVDDWLRRDRFVFVGWSGLLLFPCAYLALGGWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPAN
SMGHSLLLLWGPEAQGDFTRWCQLGGLWTFVALHGAFGLIGFMLRQFEIARSVGIRPYNAIAFSGPIAVF
VSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLF
EDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSAIGVVGLALNL
RAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHENLVFPEEVLPRGNAL
>gnl|CDD|187747 cd09289, Photosystem-II_D1, D1 subunit of photosystem II (PS II). Photosystem II (PS II), D2 subunit. PS II is a multi-subunit protein found in the photosynthetic membranes of plants, algae, and cyanobacteria. It utilizes light-induced electron transfer and water-splitting reactions to produce protons, electrons, and molecular oxygen. The protons generated are instrumental in ATP formation. Molecular dioxygen is released as a by-product. PS II can be described as containing two parts: the photochemical part and the catalytic part. The photochemical portion promotes the fast, efficient light-induced charge separation and stabilization that occur when light is absorbed by chlorophyll. The catalytic portion, where water is oxidized, involves a cluster of Mn ions close to a redox-active tyrosine residue. The Mn cluster and its ligands form a functional unit called the oxygen-evolving complex (OEC) or the water-oxidizing complex (WOC). The D1 and D2 subunits are a pair of interwined polypeptides. They contain all the cofactors involved directly in water oxidation and plastoquinone reduction. The D1 subunit contains the Mn cluster that constitutes the site of water oxidation. D1 and D2 are highly homologous and are also similar to the L and M proteins in bacterial photosynthetic reaction centers
RRESASLWERFCAWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNN
IISGAVVPTSNAIGLHFYPIWEAASLDEWLYNGGPYQLIVLHFLLGVCCYMGREWELSYRLGMRPWIAVA
YSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHG
SLVTSSLIRETTENESANAGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFT
ALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLA
>gnl|CDD|187748 cd09290, Photo-RC_L, Subunit L of bacterial photosynthetic reaction center. Bacterial photosynthetic reaction center (RC) complex, subunit L. The bacterial photosynthetic reaction center couples light-induced electron transfer with pumping protons across the membrane using reactions involving a quinone molecule (QB) that binds two electrons and two protons at the active site. The reaction center consists of three membrane-bound subunits, designated L, M, and H, plus an additional extracellular cytochrome subunit. The L and M subunits are arranged around an axis of 2-fold rotational symmetry perpendicular to the membrane, forming a scaffold that maintains the cofactors in a precise configuration. The L and M subunits have both sequence and structural similarity, suggesting a common evolutionary origin. The L and M subunits bind noncovalently to the nine cofactors in 2-fold symmetric branches: four bacteriochlorophylls (Bchl), two bacteriopheophytins (Bphe), two ubiquinone molecules (QA and QB), and a non-heme iron. Two Bchls on the periplasmic side of the membrane form the 'special pair' or dimer which is the primary electron donor for the photosynthetic reactions. The electron transfer reaction proceeds from the dimer to an intermediate acceptor (PA), a primary quinone (QA), and a secondary quinone (QB). Protons are translocated from the bacterial cytoplasm to the periplasmic space, generating an electrochemical gradient of protons (the protonmotive force) that can be used to power reactions such as ATP synthesis. The RC complex is found in photosynthetic bacteria, such as purple bacteria and other proteobacteria species
AMLSFEKKYRVRGGTLIGGDLFDFWVGPFYVGFFGVVSIFFIILGVALIIWEAVLGGPTWNIWAISINPP
DLSYGLGAAPLTEGGLWQIITVCATGAFVSWALRQVEISRKLGMGYHVPIAFGVAISAYLTLQVIRPILM
GAWGHGFPYGIMSHLDWVSNFGYQYLNFHYNPAHMIAITFLFTNTLALSMHGSLILSAANPKKGEPVKTP
DHENTFFRDVVGYSIGELGIHRLGLFLALSAALWSALCILISGPFWTDGWPEWWGWWLKLPIW
>gnl|CDD|187749 cd09291, Photo-RC_M, Subunit M of bacterial photosynthetic reaction center. Bacterial photosynthetic reaction center (RC) complex, subunit M. The bacterial photosynthetic reaction center couples light-induced electron transfer with pumping protons across the membrane using reactions involving a quinone molecule (QB) that binds two electrons and two protons at the active site. The reaction center consists of three membrane-bound subunits, designated L, M, and H, plus an additional extracellular cytochrome subunit. The L and M subunits are arranged around an axis of 2-fold rotational symmetry perpendicular to the membrane, forming a scaffold that maintains the cofactors in a precise configuration. The L and M subunits have both sequence and structural similarity, suggesting a common evolutionary origin. The L and M subunits bind noncovalently to the nine cofactors in 2-fold symmetric branches: four bacteriochlorophylls (Bchl), two bacteriopheophytins (Bphe), two ubiquinone molecules (QA and QB), and a non-heme iron. Two Bchls on the periplasmic side of the membrane form the 'special pair' or dimer which is the primary electron donor for the photosynthetic reactions. The electron transfer reaction proceeds from the dimer to an intermediate acceptor (PA), a primary quinone (QA), and a secondary quinone (QB). Protons are translocated from the bacterial cytoplasm to the periplasmic space, generating an electrochemical gradient of protons (the protonmotive force) that can be used to power reactions such as ATP synthesis. The RC complex is found in photosynthetic bacteria, such as purple bacteria and other proteobacteria species
QVRGPADPGDPEPGDDLGRIGKPPFSYWLGKIGDAQIGPIYLGLWGVLSIIFGFIAIFIILFNMLAQVNW
NPVQFLRQFFWLALEPPPPEYGLSIPPLNEGGWWLIAGFFLTLSILLWWIRTYTRAKALGMGTHLAWAFA
AAIFLYLVIGFIRPVLMGSWSEAVPFGIFPHLDWTNAFSIRYGNFYYNPFHMLSIAFLYGSTLLFAMHGA
TILAVSRFGGEREIEQITDRGTATERAQLFWRWTMGFNATMESIHRWAWWFAVLVVITGGIGILLSGTVV
DNWYLWGVKHGIAPPYP
>gnl|CDD|187754 cd09293, AMN1, Antagonist of mitotic exit network protein 1. Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model
KDPLLFILHKLGQITQSNISQLLRILHSGLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGL
IALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRNGHLITDVSLSALGKNCTFLQTVGF
AGCDVTDKGVWELASGCSKSLERLSLNNCRNLTDQSIPAILASNYFPNLSVLEFRGCPLITDFSRIILFK
LWQPRLNKPILVEWCE
>gnl|CDD|187755 cd09294, SmpB, Small protein B (SmpB) is a component of the trans-translation system in prokaryotes for releasing stalled ribosome from damaged messenger RNAs. Small protein B (SmpB) is a component of the trans-translation system in prokaryotes for releasing stalled ribosome from damaged messenger RNAs and targeting incompletely synthesized protein fragments for degradation. Trans-translation system is composed of a ribonucleoprotein complex of tmRNA, a specialized RNA with properties of both tRNA and mRNA, and SmpB. SmpB is highly conserved and present in all bacterial kingdoms and is also found in some chloroplasts and mitochondria. This is suggesting Trans-translation arose early in bacterial evolution and its mechanism is a quality control for protein synthesis in spite of challenges such as transcription errors, mRNA damage, and translation frame shifting. SmpB deletion results in phage development defects phenotype and absence of tagged proteins translated from defective mRNAs
NKKARHDYEIEETFEAGIVLLGTEVKSLRAGKVNLKDSYVRIKNGEAWLLNAHISPYEFANRFNHDPKRP
RKLLLHKKEIDKLIGKVEQKGLTIVPLKLYFKNGKAKVEIALAKGK
>gnl|CDD|200495 cd09295, Sema, The Sema domain, a protein interacting module, of semaphorins and plexins. Both semaphorins and plexins have a Sema domain on their N-termini. Plexins function as receptors for the semaphorins. Evolutionarily, plexins may be the ancestor of semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems, and cancer. Semaphorins can be divided into 7 classes. Vertebrates have members in classes 3-7, whereas classes 1 and 2 are known only in invertebrates. Class 2 and 3 semaphorins are secreted; classes 1 and 4 through 6 are transmembrane proteins; and class 7 is membrane associated via glycosylphosphatidylinositol (GPI) linkage. Plexins are a large family of transmembrane proteins, which are divided into four types (A-D) according to sequence similarity. In vertebrates, type A plexins serve as co-receptors for neuropilins to mediate the signalling of class 3 semaphorins. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B plexins. This family also includes the MET and RON receptor tyrosine kinases. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves to recognize and bind receptors
DDDKILVSFRKDTIYVGAIARIYKVDGGGTRLLLSCISPELNFGFNEDQKAFCPLRRGKWTECINYIKVL
QQKGDLDILAVCGSNAAQPSCGSYRLDVLVELGKVRWPSGRPRCPIDNKHSNMGVNVDSKLYSATDHDFK
DGDRPALSRRSSNVHYLRIVVDSSTGLDEITFVYAFVSGDDDDEVYFFFRQEPVEYLKKGMVYVPRIARV
CKLDVGGCHRLKKKLTSFLKADLNCSRPQSGFAFNLLQDATGDTKNLIQDVKFAIFSSCLNKSVESAVCA
YLFTDINNVFDDPVEAINNRPLYAHQNQRSRLTSIAVDATKQKSVGYQVVFLGLKLGSLGKALAFFFLYK
GHIIEEWKVFKDSSRITNLDLSRPPLYLYVGSESGVLGVPVQ
>gnl|CDD|187756 cd09299, TDT, The Tellurite-resistance/Dicarboxylate Transporter (TDT) family. The Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes members from all three kingdoms, but only three members of the family have been functionally characterized: the TehA protein of E. coli functioning as a tellurite-resistance uptake permease, the Mae1 protein of S. pombe functioning in the uptake of malate and other dicarboxylates, and the sulfite efflux pump (SSU1) of Saccharomyces cerevisiae. In plants, the plasma membrane protein SLAC1 (Slow Anion Channel-Associated 1), which is preferentially expressed in guard cells, encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. SLAC1 is essential in mediating stomatal responses to physiological and stress stimuli. Members of the TDT family exhibit 10 putative transmembrane alpha-helical spanners (TMSs)
WFGIVMGTGILSLALYLLPYQFPGLRIIGKILFILAIVIFILFFALWLLRLIRYPRHVVRESHHNPVEAS
FLAAVPISLFTIIDFLALYGGANTGRLVILIAYVLWWIGLALSLVSAVGVPYLLFTNHVYEIEHISPAWL
LPIVPPMTSAALAGALLPYSPGGAIQLSVIFLGYLFFGIGFFLFIFIGAIIFSRLVINKLPPGQLAPTLM
IVLGPMGQSIFALLLLGKNARLIFFLYASFLQALAVFASIILWGFGLWWLLLALVSILRTLRKKLPFSLG
WWSYVFPLGVYTNGTYALYKLMDLPAFSIFATILLIILVALWILCT
>gnl|CDD|350171 cd09300, DEAD-like_helicase_C, C-terminal helicase domain of the DEAD-like helicases. This hierarchy of DEAD-like helicases is composed of two superfamilies, SF1 and SF2, that share almost identical folds and extensive structural similarity in their catalytic core. Helicases are involved in ATP-dependent RNA or DNA unwinding. Two distinct types of helicases exist, those forming toroidal, predominantly hexameric structures, and those that do not. SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Their conserved helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
NALVAVSVLIAVNXALTGFDAPELNTIIVDKNLRSYRGLNQAFGRANRIYTFGGIVTYR
>gnl|CDD|212512 cd09301, HDAC, Histone deacetylase (HDAC) classes I, II, IV and related proteins. The HDAC/HDAC-like family includes Zn-dependent histone deacetylase classes I, II and IV (class III HDACs, also called sirtuins, are NAD-dependent and structurally unrelated, and therefore not part of this family). Histone deacetylases catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98), as opposed to the acetylation reaction by some histone acetyltransferases (EC 2.3.1.48). Deacetylases of this family are involved in signal transduction through histone and other protein modification, and can repress/activate transcription of a number of different genes. They usually act via the formation of large multiprotein complexes. They are involved in various cellular processes, including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. In mammals, they are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs
RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKPVIFGPNFPVQRHY
FRGARLSTGGVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRERGISRILIID
TDAHHGDGTREAFYDDDRVLHMSFHNYDIYPFGRGKGKGYKINVPLEDGLGDEEYLDAVERVISKVLEEF
EPEVVVLQFGHDTHEGDRLGGFNLSEKGFVKLAEIVKEFARGGPILMVLGGGYNPEAAARIWTAIIKEL
>gnl|CDD|187706 cd09302, Jacalin_like, Jacalin-like lectin domain. Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. Taxonomic distribution is not restricted to plants, the domain is also found in various mammalian proteins, for example
GKPFSDTGGDGARLTEIRVRSGGAVDAIRVVLRDYTDGRHGGNGGPNTSSVFLDPGEYITITSVSSGDNG
GGTRIDAIQFTTNKGRSGTYGTTSGALGTEFTVPVGGEIVGIYGRAGDDVDAFGFILS
>gnl|CDD|187757 cd09317, TDT_Mae1_like, C4-dicarboxylate transporter/malic acid transport protein family includes Mae1. This family contains eukaryotic homologs of C4-dicarboxylate transporter/malic acid transport proteins which are part of the Tellurite-resistance/Dicarboxylate Transporter (TDT) family. This includes the MAE1 gene in Schizosaccharomyces pombe gene that encodes malate permease, Mae1, which functions by proton symport and transports C4-dicarboxylates (malate, fumarate, succinate, oxaloacetate, etc.), but not K-ketoglutarate
WFTCTMSTGGIALLLSGTPFRFPGLRTIGTIVFILNLILFTLITLCLILRFILYPGTFLASLTHPTEGLF
VPTFLLSIATIIIGTQSYGVPSCGPWLVTALRVLFWIYVALSLIVAIGQYLLLFSTHTFPLTTMTPAWIL
PIFPLMLTGTIASVLAASQPPSSAVPMIVAGLTFQGLGFLMSLFIYAVYIGRLMTSGLPAPSQRPGMFIA
VGPPGFTALALIGLANAAPRIFPAHFLGTANAAEILRVVAVVAGLFLWGLAFWFFCIAVVSVLAGLRKRR
FHLGWWAFVFPNVGFVLATIELGKAFDSEGILIVGSVMTILLVIVWLIVF
>gnl|CDD|187758 cd09318, TDT_SSU1, Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes sulfite sensitivity protein (sulfite efflux pump; SSU1). This family contains the sulfite sensitivity protein (sulfite efflux pump; SSU1) and belongs to the tellurite-resistance/dicarboxylate transporter (TDT) family. The SSU1 gene encodes the sulfite pump required for efficient sulfite efflux. Mutations in the SSU1 gene cause sensitivity to sulfite while overexpression confers heightened resistance to sulfite toxicity. In dematophytes and other filamentous fungi, sulfite is excreted as a reducing agent during keratin degradation; thus sulfite transporters in keratinolytic fungi could be a new target for antifungal drugs in dermatology. The number of genes encoding sulfite efflux pumps in fungal genomes varies from species to species
LVRNFTPAWFAVTMGTGIVSILLYNFPYPARWLRIIGYILFGINVLLFILFTVLFIARYVLYPERFRAML
KHPTQSLFLGTIPMGLATIINGIVLLCGPVWGPWAIILAWVLWWIDVALSLATAWGVPFLMFTRQNKHAL
EKMTAVWLLPIVALVVAASSGGLVAPHLPNPNHALLTLVVSYVLWGIGVPLAFIILTIYLLRLALHKLPP
KALIFSSFLPLGPLGQGAFGILLLGKNAKKLFPSTYTLSAAVGQIFYVLGLLIALILWGFGLWWLFLAVA
SILSYIRPGLPFNKGWWGFTFPLGVMALATIELGKELPSKFFRVLGAILSVALILLWIVVA
>gnl|CDD|187759 cd09319, TDT_like_1, The Tellurite-resistance/Dicarboxylate Transporter (TDT) family. The Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes members from all three kingdoms, but only three members of the family have been functionally characterized: the TehA protein of E. coli functioning as a tellurite-resistance uptake permease, the Mae1 protein of S. pombe functioning in the uptake of malate and other dicarboxylates, and the sulfite efflux pump (SSU1) of Saccharomyces cerevisiae. In plants, the plasma membrane protein SLAC1 (Slow Anion Channel-Associated 1), which is preferentially expressed in guard cells, encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. SLAC1 is essential in mediating stomatal responses to physiological and stress stimuli. Members of the TDT family exhibit 10 putative transmembrane alpha-helical spanners (TMSs)
PAYFALVMATGIVSIALHLLGLEVLSRALLVLNLVAYVVLWVLTLARLLFYPRALRADLADPARGPGFFT
AVAGTNVLGSQLVLLGWNAVALVLWAVALVLWLVLTYAVFRALTVRRLKPTERGVNGAWLLAVVATQSLA
VLGALLAPAVPAGREWLLFLALVLWLLGLALYLVVISLIDYRLVFFPFKPEDLAPPYWINMGALAISTLA
GAKLILAASASPFLADLRPFLKGTTLLLWAAATWWIPLLVALGIWRHVVHRIPLRYDPLRWSTVFPLGMY
AAATLALARALGLPWLMAIGRVFLWVALAAWLLVFVG
>gnl|CDD|187760 cd09320, TDT_like_2, The Tellurite-resistance/Dicarboxylate Transporter (TDT) family. The Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes members from all three kingdoms, but only three members of the family have been functionally characterized: the TehA protein of E. coli functioning as a tellurite-resistance uptake permease, the Mae1 protein of S. pombe functioning in the uptake of malate and other dicarboxylates, and the sulfite efflux pump (SSU1) of Saccharomyces cerevisiae. In plants, the plasma membrane protein SLAC1 (Slow Anion Channel-Associated 1), which is preferentially expressed in guard cells, encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. SLAC1 is essential in mediating stomatal responses to physiological and stress stimuli. Members of the TDT family exhibit 10 putative transmembrane alpha-helical spanners (TMSs)
PNWFGSVMGTGIVATLAVILPLGAPGLRTGAEAFWLVAALLLVALTAGFAAHWRRHPAFARARDPVMMPF
WGMVSMGLLAVGAATLTVGPDVIGHDAAVAVDTVLWVIGTVLGLVTAVVIPRRLIRRHRGTPTPVWGLPV
VPPMVSATTGAQLVPHLPAGQPRLTLLLACYACFGLSLLAAAIIFALVYRRLWRGGPLPLAAAPTAWIPL
GVVGQSTAAAQLLAAAAGHVLPPPTAQTLHVFAVLYGVVMLGFGVPLLALAAAVTVRAVRRGMPFSPTWW
AFTFPVGTCVLGAHALAVHTGLAWFDWLAAALLVLLLAHWTVCAART
>gnl|CDD|187761 cd09321, TDT_like_3, The Tellurite-resistance/Dicarboxylate Transporter (TDT) family. The Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes members from all three kingdoms, but only three members of the family have been functionally characterized: the TehA protein of E. coli functioning as a tellurite-resistance uptake permease, the Mae1 protein of S. pombe functioning in the uptake of malate and other dicarboxylates, and the sulfite efflux pump (SSU1) of Saccharomyces cerevisiae. In plants, the plasma membrane protein SLAC1 (Slow Anion Channel-Associated 1), which is preferentially expressed in guard cells, encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. SLAC1 is essential in mediating stomatal responses to physiological and stress stimuli. Members of the TDT family exhibit 10 putative transmembrane a-helical spanners (TMSs)
FAPSWFASVMGTGALAIASYLYSAYFPFLKTLAVFLTYLNFLLFFVLLVPWLLRWILYPKEALADLKHPV
LSNFYPTMPIALLVLATNILIVGQGPLGYSLALTLWILGSILIFIFSFIVSYIMFINEEIPIEHINPAWF
IPPVGLIVIPLAGNFLIPHFPGAWQESILVINLFGFGIGFFLFLFLLAIILHRLILHEPPPPELAPTFWI
NLAPIGAGVVALINLVKALPFAGLENLVDLANIFALILWGFGLWWLILAVLLTLYYLKRGNLPFSLGWWA
FIFPLGAYTIATYLVAKVLNFSFLSGLGIFLYWLLLILWAITLFKTL
>gnl|CDD|187762 cd09322, TDT_TehA_like, The Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes TehA proteins. The Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes members from all three kingdoms, but only three members of the family have been functionally characterized: the TehA protein of E. coli functioning as a tellurite-resistance uptake permease, the Mae1 protein of S. pombe functioning in the uptake of malate and other dicarboxylates, and the sulfite efflux pump (SSU1) of Saccharomyces cerevisiae. In plants, the plasma membrane protein SLAC1 (Slow Anion Channel-Associated 1), which is preferentially expressed in guard cells, encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. SLAC1 is essential in mediating stomatal responses to physiological and stress stimuli. Members of the TDT family exhibit 10 putative transmembrane a-helical spanners (TMSs)
LFPIVLGLLGLGLAWLGALLLLGLPSIVGEILGILALLLWLLLLLKYLLKLLRYPEAVKAELRHPVRASF
FATFSMSLMLLSIYLLPYSPLLARVLWILGAVLHLVFTLYFVSRWIRGGKFLEHVTPSWFIPYVGNIVVP
VTGPALGGPELGWFFFGVGLIFWLVLLPLVLYRLIFHEPLPEPLRPTLAILLAPPSLGLAAYLALFGGPI
DLFALILLGLALFLFLLLLRLLPRLLKLPFSPSWWAFTFPLAALAIALLKMAAYLGSGFLQLLALVLLEL
LTAVILVLY
>gnl|CDD|187763 cd09323, TDT_SLAC1_like, Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes SLAC1 (Slow Anion Channel-Associated 1). SLAC1 (Slow Anion Channel-Associated 1) is a plasma membrane protein, preferentially expressed in guard cells, which encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. It is essential for stomatal closure in response to carbon dioxide, abscisic acid, ozone, light/dark transitions, humidity change, calcium ions, hydrogen peroxide and nitric oxide. In the Arabidopsis genome, SLAC1 is part of a gene family with five members and encodes a membrane protein that has ten putative transmembrane domains flanked by large N- and C-terminal domains. Mutations in SLAC1 impair slow (S-type) anion channel currents that are activated by cytosolic calcium ions and abscisic acid, but do not affect rapid (R-type) anion channel currents or calcium ion channel function
HFPVSLFAIVMGLSGLALAWRKAAELLGLPAAISEALGWLAVAVFVVLAALYALKILRYPEAVKAEFNHP
VRINFFPAISISLLLLSIALLPYSPVLALALWIIGAVLQLALTLYVVSRWISHRQFQIGHANPAWFIPVV
GNLVVPIAGVPLGYAEVSWFFFSVGLFFWLVLFTIVFNRLIFHEPLPAKLLPTLFILIAPPAVGFLAYLK
LTGSLDAFARILYYIALFLFLLLLFQVRRFRKLPFFLSWWAYSFPLAALAIATLRMAELTGSLFLQVLAL
VLLALLTLVVAVLLVRT
>gnl|CDD|187764 cd09324, TDT_TehA, Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes TehA protein. This subfamily includes Tellurite resistance protein TehA that belongs to the C4-dicarboxylate transporter/malic acid transport (TDT) protein family and is a homolog of plant Slow Anion Channel-Associated 1 (SLAC1). The tehA gene encodes an integral membrane protein that has been shown to have efflux activity of quaternary ammonium compounds. TehA protein of Escherichia coli functions as a tellurite-resistance uptake permease
PVGYFGIVLGLAALGLAWRYAAQLWPLPAIVGESLLALASVVWLLLIGAYAYKWLKYREEARAELRHPVQ
CCFISLIPITTMLVGIALYPYSRLLAEVLIVLGIIGQLAFAAWRTGGLWQGGHFPEATTPVLYLPTVAGN
FVSASALAALGYHDLGMLFFGAGMFSWLSLEPVILQRLRTSPPLPPALRPTLGIQLAPAFVGCSAYLSLN
GGEVDLLAKMLWGYGLLQLLFLLRLLPWIAEQGFSMGFWAFSFGLAAMATSGLHLYHGGVLGPLSLLALA
LFNVANGLIALLTLGTLTLGL
>gnl|CDD|187765 cd09325, TDT_C4-dicarb_trans, C4-dicarboxylate transporters of the Tellurite-resistance/Dicarboxylate Transporter (TDT) family. This subfamily contains bacterial C4-dicarboxylate transporters, which is part of the Tellurite-resistance/Dicarboxylate Transporter (TDT) family. It includes Tellurite resistance protein tehA; the tehA gene encodes an integral membrane protein that has been shown to have efflux activity of quaternary ammonium compounds. TehA protein of Escherichia coli functions as a tellurite-resistance uptake permease
KIPIPIAGLALGLASLGNLLELSYGSILRNICGLIALILLILLLLKIILFPKTLKEELKNPVIASVFPTF
PMALMLLSTYLKPFFPALAQLLWLLAIILHIILIIYFTYKRILKFNLEHVFPSWFVVYVGIVVASVTAPA
FGQPLLGQIAFWFGFVAYLILLPLVLYRLVKIKELPDAALPTIAIFAAPASLCLAGYLNSFPEPNPVLVL
FLLILSQLLYFFVLLQLPRLLKLPFYPSFAAFTFPLVISATALKKTSTYLASYGLYLPILKYLALFEILI
ATVIVLYVLIRYL
>gnl|CDD|188712 cd09326, LIM_CRP_like, The LIM domains of Cysteine Rich Protein (CRP) family. The LIM domains of Cysteine Rich Protein (CRP) family: Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to a short glycine-rich repeats (GRRs). The known CRP family members include CRP1, CRP2, and CRP3/MLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription control, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. CRP1, CRP2, and CRP3/MLP are involved in promoting protein assembly along the actin-based cytoskeleton. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CPRCGKSVYAAEEVIAAGKSWHKSCFTCAVCNKRLDSTTLAEHDGEIYCKSCY
>gnl|CDD|188713 cd09327, LIM1_abLIM, The first LIM domain of actin binding LIM (abLIM) proteins. The first LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CYKCGKKCKGEVLRVQDKYFHIKCFTCKVCGCDLAQGGFFVKEGEYYCTDDY
>gnl|CDD|188714 cd09328, LIM2_abLIM, The second LIM domain on actin binding LIM (abLIM) proteins. The second LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
GTKCDSCQDFVEGEVVSALGKTYHPKCFVCSVCRQPFPPGDRVTFNGKECLCQKCS
>gnl|CDD|188715 cd09329, LIM3_abLIM, The third LIM domain of actin binding LIM (abLIM) proteins. The third LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAGCGQEIKNGQALLALDKQWHVWCFKCKECGKVLTGEYMGKDGKPYCERDY
>gnl|CDD|188716 cd09330, LIM4_abLIM, The fourth LIM domain of actin binding LIM (abLIM) proteins. The fourth LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CEACDKFITGKVLEAGGKHYHPTCARCSRCGQMFGEGEEMYLQGSEIWHPDCRQAA
>gnl|CDD|188717 cd09331, LIM1_PINCH, The first LIM domain of protein PINCH. The first LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CERCREGFEPDEKIVNSNGELYHEQCFVCAQCFQPFPDGLFYEFEGRKYCEHDFQVLFA
>gnl|CDD|188718 cd09332, LIM2_PINCH, The second LIM domain of protein PINCH. The second LIM domain of protein PINCH: PINCH plays a pivotal role in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CGKCGEFVIGRVIKAMNNNWHPDCFRCEICNKELADIGFVKNAGRALCHPCN
>gnl|CDD|188719 cd09333, LIM3_PINCH, The third LIM domain of protein PINCH. The third LIM domain of protein PINCH: PINCH plays pivotal roles in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CQKCHAIIEEQHLKFKGDPYHPYHFNCANCGKELTADARELKGELYCLRCH
>gnl|CDD|188720 cd09334, LIM4_PINCH, The fourth LIM domain of protein PINCH. The fourth LIM domain of protein PINCH: PINCH plays a pivotal role in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. The PINCH LIM4 domain recognizes the third SH3 domain of another adaptor protein, Nck2. This step is an important component of integrin signaling event. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assem bly of multimeric protein complexes
PICGACRRPIEGRVVTALGKHWHVEHFVCAKCEKPFLGHRHYEKKGLAYCETHY
>gnl|CDD|188721 cd09335, LIM5_PINCH, The fifth LIM domain of protein PINCH. The fifth LIM domain of protein PINCH: PINCH plays pivotal roles in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CYHCNQVIEGDVVSALNKTWCVDHFSCSFCDTKLTLKSKFYEFDMKPVCKKCYD
>gnl|CDD|259830 cd09336, LIM1_Paxillin_like, The first LIM domain of the paxillin like protein family. The first LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAACNKPIVGQVVTALGKTWHPEHFVCVHCQTELGTSNFFERDGKPYCEKDYH
>gnl|CDD|188723 cd09337, LIM2_Paxillin_like, The second LIM domain of the paxillin like protein family. The second LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAYCNGPILDKCVTALDKTWHPEHFFCAQCGKPFGDEGFHEKDGKPYCREDY
>gnl|CDD|188724 cd09338, LIM3_Paxillin_like, The third LIM domain of the paxillin like protein family. The third LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CGGCNKPILENYISALNTQWHPECFVCRECHKPFINGSFFEHEGLPYCETHYH
>gnl|CDD|188725 cd09339, LIM4_Paxillin_like, The fourth LIM domain of the Paxillin-like protein family. The fourth LIM domain of the Paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAGCGKPITGRCITAMGRKFHPEHFVCAFCLKQLSKGTFKEQDDKPYCHPCF
>gnl|CDD|188726 cd09340, LIM1_Testin_like, The first LIM domain of Testin-like family. The first LIM domain of Testin_like family: This family includes testin, prickle, dyxin and LIMPETin. Structurally, testin and prickle proteins contain three LIM domains at C-terminal; LIMPETin has six LIM domains; and dyxin presents only two LIM domains. However, all members of the family contain a PET protein-protein interaction domain. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell-contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and it is involved in cell motility and adhesion events. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). Dyxin involves in lung and heart development by interaction with GATA6 and blocking GATA6 activated target genes. LIMPETin might be the recombinant product of genes coding testin and four and half LIM proteins and its function is not well understood. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CEKCKEPINPGEVAVFAERAGEDACWHPGCFVCETCNELLVDLIYFYHDGKIYCGRHY
>gnl|CDD|188727 cd09341, LIM2_Testin_like, The second LIM domain of Testin-like family. The second LIM domain of Testin-like family: This family includes testin, prickle, dyxin and LIMPETin. Structurally, testin and prickle proteins contain three LIM domains at C-terminal; LIMPETin has six LIM domains; and dyxin presents only two LIM domains. However, all members of the family contain a PET protein-protein interaction domain. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell-contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and it is involved in cell motility and adhesion events. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). Dyxin involves in lung and heart development by interaction with GATA6 and blocking GATA6 activated target genes. LIMPETin might be the recombinant product of genes coding testin and four and half LIM proteins and its function is not well understood. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
PRCAACDELIFSGEYTQAEGKNWHLKHFCCFQCDEPLGGQRYVLREGKPYCLDCYE
>gnl|CDD|188728 cd09342, LIM3_Testin_like, The third LIM domain of Testin-like family. The third LIM domain of Testin_like family: This family includes testin, prickle, dyxin and LIMPETin. Structurally, testin and prickle proteins contain three LIM domains at C-terminal; LIMPETin has six LIM domains; and dyxin presents only two LIM domains. However, all members of the family contain a PET protein-protein interaction domain. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell-contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and it is involved in cell motility and adhesion events. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). Dyxin involves in lung and heart development by interaction with GATA6 and blocking GATA6 activated target genes. LIMPETin might be the recombinant product of genes coding testin and four and half LIM proteins and its function is not well understood. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CDACGEPIGPDVQRVAHNGQHWHATEECFCCSNCKKSLLGQPFLPKNGQIFCSPKCK
>gnl|CDD|188729 cd09343, LIM1_FHL, The first LIM domain of Four and a half LIM domains protein (FHL). The first LIM domain of Four and a half LIM domains protein (FHL): LIM-only protein family consists of five members, designated FHL1, FHL2, FHL3, FHL5 and LIMPETin. The first four members are composed of four complete LIM domains arranged in tandem and an N-terminal single zinc finger domain with a consensus sequence equivalent to the C-terminal half of a LIM domain. LIMPETin is an exception, containing six LIM domains. FHL1, 2 and 3 are predominantly expressed in muscle tissues, and FHL5 is highly expressed in male germ cells. FHL proteins exert their roles as transcription co-activators or co-repressors through a wide array of interaction partners. For example, FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. FHL3 int eracts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. FHL5 is a tissue-specific coactivator of CREB/CREM family transcription factors. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
FANTCEECKKKIGCDSKDLSYKDRHWHEGCFKCFKCQRSLVDKPFAAKDEDLLCTECYS
>gnl|CDD|188730 cd09344, LIM1_FHL1, The first LIM domain of Four and a half LIM domains protein 1. The first LIM domain of Four and a half LIM domains protein 1 (FHL1): FHL1 is heavily expressed in skeletal and cardiac muscles. It plays important roles in muscle growth, differentiation, and sarcomere assembly by acting as a modulator of transcription factors. Defects in FHL1 gene are responsible for a number of Muscular dystrophy-like muscle disorders. It has been detected that FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAECRKPIGADSKELHHKNRYWHETCFRCAKCYKPLANEPFVAKDNKILCGKCT
>gnl|CDD|188731 cd09345, LIM2_FHL, The second LIM domain of Four and a half LIM domains protein (FHL). The second LIM domain of Four and a half LIM domains protein (FHL): LIM-only protein family consists of five members, designated FHL1, FHL2, FHL3, FHL5 and LIMPETin. The first four members are composed of four complete LIM domains arranged in tandem and an N-terminal single zinc finger domain with a consensus sequence equivalent to the C-terminal half of a LIM domain. LIMPETin is an exception, containing six LIM domains. FHL1, 2 and 3 are predominantly expressed in muscle tissues, and FHL5 is highly expressed in male germ cells. FHL proteins exert their roles as transcription co-activators or co-repressors through a wide array of interaction partners. For example, FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. FHL3 int eracts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. FHL5 is a tissue-specific coactivator of CREB/CREM family transcription factors. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CKACGKAIMPGSKKMEYKGKFWHEKCFTCSECKKPIGTKSFIPKDDKIYCVPCY
>gnl|CDD|188732 cd09346, LIM3_FHL, The third LIM domain of Four and a half LIM domains protein (FHL). The third LIM domain of Four and a half LIM domains protein (FHL): LIM-only protein family consists of five members, designated FHL1, FHL2, FHL3, FHL5 and LIMPETin. The first four members are composed of four complete LIM domains arranged in tandem and an N-terminal single zinc finger domain with a consensus sequence equivalent to the C-terminal half of a LIM domain. LIMPETin is an exception, containing six LIM domains. FHL1, 2 and 3 are predominantly expressed in muscle tissues, and FHL5 is highly expressed in male germ cells. FHL proteins exert their roles as transcription co-activators or co-repressors through a wide array of interaction partners. For example, FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. FHL3 int eracts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. FHL5 is a tissue-specific coactivator of CREB/CREM family transcription factors. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAKCKKAITSGGVTYRDQPWHKECFVCTGCKKQLAGQRFTSRDEYPYCVDCF
>gnl|CDD|188733 cd09347, LIM4_FHL, The fourth LIM domain of Four and a half LIM domains protein (FHL). The fourth LIM domain of Four and a half LIM domains protein (FHL): LIM-only protein family consists of five members, designated FHL1, FHL2, FHL3, FHL5 and LIMPETin. The first four members are composed of four complete LIM domains arranged in tandem and an N-terminal single zinc finger domain with a consensus sequence equivalent to the C-terminal half of a LIM domain. LIMPETin is an exception, containing six LIM domains. FHL1, 2 and 3 are predominantly expressed in muscle tissues, and FHL5 is highly expressed in male germ cells. FHL proteins exert their roles as transcription co-activators or co-repressors through a wide array of interaction partners. For example, FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. FHL3 interacts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. FHL5 is a tissue-specific coactivator of CREB/CREM family transcription factors. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAACTKPITGLGGAKFISFEERQWHSDCFNCGKCSVSLVGQGFLTQRDEILCPECG
>gnl|CDD|188734 cd09348, LIM4_FHL1, The fourth LIM domain of Four and a half LIM domains protein 1 (FHL1). The fourth LIM domain of Four and a half LIM domains protein 1 (FHL1): FHL1 is heavily expressed in skeletal and cardiac muscles. It plays important roles in muscle growth, differentiation, and sarcomere assembly by acting as a modulator of transcription factors. Defects in FHL1 gene are responsible for a number of Muscular dystrophy-like muscle disorders. It has been detected that FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
VAKKCSGCQNPITGFGKGTNVVNYEGSSWHDYCFNCKKCSLNLANKRFVFHNGQIYCSDCAKKL
>gnl|CDD|188735 cd09349, LIM1_Zyxin, The first LIM domain of Zyxin. The first LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cell substratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
LTMKEVEELEMLTQQLMQDMDHPPAAEAATNELCGICGQPLSRTQPAVRALGHLFHVTCFTCHQCEQQLQ
GQQFYSLEGKPYCEECY
>gnl|CDD|188736 cd09350, LIM1_TRIP6, The first LIM domain of Thyroid receptor-interacting protein 6 (TRIP6). The first LIM domain of Thyroid receptor-interacting protein 6 (TRIP6): TRIP6 is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal. TRIP6 protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner. TRIP6 recruits a number of molecules involved in actin assembly, cell motility, survival and transcriptional control. The function of TRIP6 in cell motility is regulated by Src-dependent phosphorylation at a Tyr residue. The phosphorylation activates the coupling to the Crk SH2 domain, which is required for the function of TRIP6 in promoting lysophosphatidic acid (LPA)-induced cell migration. TRIP6 can shuttle to the nucleus to serve as a coactivator of AP-1 and NF-kappaB transcriptional factors. Moreover, TRIP6 can form a ternary complex with the NHERF2 PDZ protein and LPA2 receptor to regulate LPA-induced activation of ERK and AKT, rendering cells resistant to chemotherapy. Recent evidence shows that TRIP6 antagonizes Fas-Induced apoptosis by enhancing the antiapoptotic effect of LPA in cells. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CGRCGENVVGEGTGCTAMDQVFHVDCFTCMTCNGKLRGQPFYAVEKKAYCEPCY
>gnl|CDD|188737 cd09351, LIM1_LPP, The first LIM domain of lipoma preferred partner (LPP). The first LIM domain of lipoma preferred partner (LPP): LPP is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal and proline-rich region at the N-terminal. LPP initially identified as the most frequent translocation partner of HMGA2 (High Mobility Group A2) in a subgroup of benign tumors of adipose tissue (lipomas). It was also shown to be rearranged in a number of other soft tissues, as well as in a case of acute monoblastic leukemia. In addition to its involvement in tumors, LPP was inedited as a smooth muscle restricted LIM protein that plays an important role in SMC migration. LPP is localized at sites of cell adhesion, cell-cell contacts and transiently in the nucleus. In nucleus, it acts as a coactivator for the ETS domain transcription factor PEA3. In addition to PEA3, it interacts with alpha-actinin,vasodilator stimulated phosphoprotein (VASP),Palladin, and Scrib. The LIM domains are the main focal adhesion targeting elements and that the proline- rich region, which harbors binding sites for alpha-actinin and vasodilator- stimulated phosphoprotein (VASP), has a weak targeting capacity. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CVKCGEKVLGEGSGCTAMDQVYHISCFTCHQCQINLQGKPFYALDGKPYCEEDY
>gnl|CDD|188738 cd09352, LIM1_Ajuba_like, The first LIM domain of Ajuba-like proteins. The first LIM domain of Ajuba-like proteins: Ajuba like LIM protein family includes three highly homologous proteins Ajuba, Limd1, and WTIP. Members of the family contain three tandem C-terminal LIM domains and a proline-rich N-terminal region. This family of proteins functions as scaffolds, participating in the assembly of numerous protein complexes. In the cytoplasm, Ajuba binds Grb2 to modulate serum-stimulated ERK activation. Ajuba also recruits the TNF receptor-associated factor 6 (TRAF6) to p62 and activates PKCKappa activity. Ajuba interacts with alpha-catenin and F-actin to contribute to the formation or stabilization of adheren junctions by linking adhesive receptors to the actin cytoskeleton. Although Ajuba is a cytoplasmic protein, it can shuttle into the nucleus. In nucleus, Ajuba functions as a corepressor for the zinc finger-protein Snail. It binds to the SNAG repression domain of Snail through its LIM region. Arginine methyltransferase-5 (Prmt5), a protein in the complex, is recruited to Snai l through an interaction with Ajuba. This ternary complex functions to repress E-cadherin, a Snail target gene. In addition, Ajuba contains functional nuclear-receptor interacting motifs and selectively interacts with retinoic acid receptors (RARs) and rexinoid receptor (RXRs) to negatively regulate retinoic acid signaling. Wtip, the Wt1-interacting protein, was originally identified as an interaction partner of the Wilms tumour protein 1 (WT1). Wtip is involved in kidney and neural crest development. Wtip interacts with the receptor tyrosine kinase Ror2 and inhibits canonical Wnt signaling. LIMD1 was reported to inhibit cell growth and metastases. The inhibition may be mediated through an interaction with the protein barrier-to-autointegration (BAF), a component of SWI/SNF chromatin-remodeling protein; or through the interaction with retinoblastoma protein (pRB), resulting in inhibition of E2F-mediated transcription, and expression of the majority of genes with E2F1- responsive elements. Recently, Limd1 was shown to interact with the p62/sequestosome protein and influence IL-1 and RANKL signaling by facilitating the assembly of a p62/TRAF6/a-PKC multi-protein complex. The Limd1-p62 interaction affects both NF-kappaB and AP-1 activity in epithelial cells and osteoclasts. Moreover, LIMD1 functions as tumor repressor to block lung tumor cell line in vitro and in vivo. Recent studies revealed that LIM proteins Wtip, LIMD1 and Ajuba interact with components of RNA induced silencing complexes (RISC) as well as eIF4E and the mRNA m7GTP cap-protein complex and are required for microRNA-mediated gene silencing. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CVKCGKGVYGASQACQAMGNLYHTNCFTCCSCGRTLRGKAFYNVNGKVYCEEDY
>gnl|CDD|188739 cd09353, LIM2_Zyxin, The second LIM domain of Zyxin. The second LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cellsubstratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors o r scaffolds to support the assembly of multimeric protein
CAVCDQKITDRMLKATGKSYHPQCFTCVVCKCPLEGESFIVDQANQPHCVNDYHRRYAPR
>gnl|CDD|188740 cd09354, LIM2_LPP, The second LIM domain of lipoma preferred partner (LPP). The second LIM domain of lipoma preferred partner (LPP): LPP is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal and proline-rich region at the N-terminal. LPP initially identified as the most frequent translocation partner of HMGA2 (High Mobility Group A2) in a subgroup of benign tumors of adipose tissue (lipomas). It was also shown to be rearranged in a number of other soft tissues, as well as in a case of acute monoblastic leukemia. In addition to its involvement in tumors, LPP was inedited as a smooth muscle restricted LIM protein that plays an important role in SMC migration. LPP is localized at sites of cell adhesion, cell-cell contacts and transiently in the nucleus. In nucleus, it acts as a coactivator for the ETS domain transcription factor PEA3. In addition to PEA3, it interacts with alpha-actinin,vasodilator stimulated phosphoprotein (VASP),Palladin, and Scrib. The LIM domains are the main focal adhesion targeting elements and that the proline- rich region, which harbors binding sites for alpha-actinin and vasodilator- stimulated phosphoprotein (VASP), has a weak targeting capacity. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CSVCSKPILDRILRATGKPYHPQCFTCVVCGKSLDGIPFTVDATNQIHCIEDFHKKFAPR
>gnl|CDD|188741 cd09355, LIM2_Ajuba_like, The second LIM domain of Ajuba-like proteins. The second LIM domain of Ajuba-like proteins: Ajuba like LIM protein family includes three highly homologous proteins Ajuba, Limd1, and WTIP. Members of the family contain three tandem C-terminal LIM domains and a proline-rich N-terminal region. This family of proteins functions as scaffolds, participating in the assembly of numerous protein complexes. In the cytoplasm, Ajuba binds Grb2 to modulate serum-stimulated ERK activation. Ajuba also recruits the TNF receptor-associated factor 6 (TRAF6) to p62 and activates PKCKappa activity. Ajuba interacts with alpha-catenin and F-actin to contribute to the formation or stabilization of adheren junctions by linking adhesive receptors to the actin cytoskeleton. Although Ajuba is a cytoplasmic protein, it can shuttle into the nucleus. In nucleus, Ajuba functions as a corepressor for the zinc finger-protein Snail. It binds to the SNAG repression domain of Snail through its LIM region. Arginine methyltransferase-5 (Prmt5), a protein in the complex, is recruited to Snai l through an interaction with Ajuba. This ternary complex functions to repress E-cadherin, a Snail target gene. In addition, Ajuba contains functional nuclear-receptor interacting motifs and selectively interacts with retinoic acid receptors (RARs) and rexinoid receptor (RXRs) to negatively regulate retinoic acid signaling. Wtip, the Wt1-interacting protein, was originally identified as an interaction partner of the Wilms tumour protein 1 (WT1). Wtip is involved in kidney and neural crest development. Wtip interacts with the receptor tyrosine kinase Ror2 and inhibits canonical Wnt signaling. LIMD1 was reported to inhibit cell growth and metastases. The inhibition may be mediated through an interaction with the protein barrier-to-autointegration (BAF), a component of SWI/SNF chromatin-remodeling protein; or through the interaction with retinoblastoma protein (pRB), resulting in inhibition of E2F-mediated transcription, and expression of the majority of genes with E2F1- responsive elements. Recently, Limd1 was shown to interact with the p62/sequestosome protein and influence IL-1 and RANKL signaling by facilitating the assembly of a p62/TRAF6/a-PKC multi-protein complex. The Limd1-p62 interaction affects both NF-kappaB and AP-1 activity in epithelial cells and osteoclasts. Moreover, LIMD1 functions as tumor repressor to block lung tumor cell line in vitro and in vivo. Recent studies revealed that LIM proteins Wtip, LIMD1 and Ajuba interact with components of RNA induced silencing complexes (RISC) as well as eIF4E and the mRNA m7GTP cap-protein complex and are required for microRNA-mediated gene silencing. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CAVCGHLIMEMILQALGKSYHPGCFRCCVCNECLDGVPFTVDVENNIYCVKDY
>gnl|CDD|188742 cd09356, LIM2_TRIP6, The second LIM domain of Thyroid receptor-interacting protein 6 (TRIP6). The second LIM domain of Thyroid receptor-interacting protein 6 (TRIP6): TRIP6 is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal. TRIP6 protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner. TRIP6 recruits a number of molecules involved in actin assembly, cell motility, survival and transcriptional control. The function of TRIP6 in cell motility is regulated by Src-dependent phosphorylation at a Tyr residue. The phosphorylation activates the coupling to the Crk SH2 domain, which is required for the function of TRIP6 in promoting lysophosphatidic acid (LPA)-induced cell migration. TRIP6 can shuttle to the nucleus to serve as a coactivator of AP-1 and NF-kappaB transcriptional factors. Moreover, TRIP6 can form a ternary complex with the NHERF2 PDZ protein and LPA2 receptor to regulate LPA-induced activation of ERK and AKT, rendering cells resistant to chemotherapy. Recent evidence shows that TRIP6 antagonizes Fas-Induced apoptosis by enhancing the antiapoptotic effect of LPA in cells. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CSVCSKPIMERILRATGKAYHPHCFTCVVCHRSLDGIPFTVDATGQIHCIEDF
>gnl|CDD|188743 cd09357, LIM3_Zyxin_like, The third LIM domain of Zyxin-like family. The third LIM domain of Zyxin like family: This family includes Ajuba, Limd1, WTIP, Zyxin, LPP, and Trip6 LIM proteins. Members of Zyxin family contain three tandem C-terminal LIM domains, and a proline-rich N-terminal region. Zyxin proteins are detected primarily in focal adhesion plaques. They function as scaffolds, participating in the assembly of multiple interactions and signal transduction networks, which regulate cell adhesion, spreading, and motility. They can also shuffle into nucleus. In nucleus, zyxin proteins affect gene transcription by interaction with a variety of nuclear proteins, including several transcription factors, playing regulating roles in cell proliferation, differentiation and apoptosis. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CSVCGEPIMPEPGQDETVRIVALDRSFHVNCYKCEDCGMLLSSEDEGQGCYPLDGHLLCKSCN
>gnl|CDD|188744 cd09358, LIM_Mical_like, The LIM domain of Mical (molecule interacting with CasL) like family. The LIM domain of Mical (molecule interacting with CasL) like family: Known members of this family includes LIM domain containing proteins; Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2) and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth and mobility. Eplin has also found to be tumor suppressor. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs.. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CAVCGKTVYPMERLVADGKLFHKSCFRCSHCNKTLRLGNYASLEGKLYCKPHF
>gnl|CDD|188745 cd09359, LIM_LASP_like, The LIM domain of LIM and SH3 Protein (LASP)-like proteins. The LIM domain of LIM and SH3 Protein (LASP) like proteins: This family contains two types of LIM containing proteins; LASP and N-RAP. LASP family contains two highly homologous members, LASP-1 and LASP-2. LASP contains a LIM motif at its amino terminus, a src homology 3 (SH3) domains at its C-terminal part, and a nebulin-like region in the middle. LASP-1 and -2 are highly conserved in their LIM, nebulin-like, and SH3 domains, but differ significantly at their linker regions. Both proteins are ubiquitously expressed and involved in cytoskeletal architecture, especially in the organization of focal adhesions. LASP-1 and LASP-2, are important during early embryo- and fetogenesis and are highly expressed in the central nervous system of the adult. However, only LASP-1 seems to participate significantly in neuronal differentiation and plays an important functional role in migration and proliferation of certain cancer cells while the role of LASP-2 is more structural. The expression of LASP-1 in breast tumors is increased significantly. N-RAP is a muscle-specific protein concentrated at myotendinous junctions in skeletal muscle and intercalated disks in cardiac muscle. LIM domain is found at the N-terminus of N-RAP and the C-terminal of N-RAP contains a region with multiple of nebulin repeats. N-RAP functions as a scaffolding protein that organizes alpha-actinin and actin into symmetrical I-Z-I structures in developing myofibrils. Nebulin repeat is known as actin binding domain. The N-RAP is hypothesized to form antiparallel dimerization via its LIM domain. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CARCGKIVYPTEKVNCLDKTWHKACFHCEVCKMTLNMNNYKGYQKKPYCNAHY
>gnl|CDD|188746 cd09360, LIM_ALP_like, The LIM domain of ALP (actinin-associated LIM protein) family. This family represents the LIM domain of ALP (actinin-associated LIM protein) family. Four proteins: ALP, CLP36, RIL, and Mystique have been classified into the ALP subfamily of LIM domain proteins. Each member of the subfamily contains an N-terminal PDZ domain and a C-terminal LIM domain. Functionally, these proteins bind to alpha-actinin through their PDZ domains and bind or other signaling molecules through their LIM domains. ALP proteins have been implicated in cardiac and skeletal muscle structure, function and disease, platelet, and epithelial cell motility. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CDKCGNGIVGVVVKARDKNRHPECFVCADCGLNLKNKGYFFIEDELYCETHA
>gnl|CDD|188747 cd09361, LIM1_Enigma_like, The first LIM domain of Enigma-like family. The first LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAHCNQVIRGPFLVALGRSWHPEEFTCSHCHCSLAEIGFVEEKGSLYCELCY
>gnl|CDD|188748 cd09362, LIM2_Enigma_like, The second LIM domain of Enigma-like family. The second LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CARCHKKILGEVMHALKQTWHVSCFVCAACKQPIGNSLFHMEDGEPYCEKDY
>gnl|CDD|188749 cd09363, LIM3_Enigma_like, The third LIM domain of Enigma-like family. The third LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CHGCDFPIEAGDRFLEALGHTWHDTCFVCAVCHVNLEGQTFYSKKDKPLCKNHA
>gnl|CDD|188750 cd09364, LIM1_LIMK, The first LIM domain of LIMK (LIM domain Kinase). The first LIM domain of LIMK (LIM domain Kinase): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerisation. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAGCRGKILDSQYVQALNQDWHCDCFRCSVCSDSLSNWYFEKDGKLYCRKDYW
>gnl|CDD|188751 cd09365, LIM2_LIMK, The second LIM domain of LIMK (LIM domain Kinase). The second LIM domain of LIMK (LIM domain Kinase): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CHGCSQIITGPVMVAGDHKFHPECFSCSSCKAFIGDGDSYALVERSKLYCGVCY
>gnl|CDD|188752 cd09366, LIM1_Isl, The first LIM domain of Isl, a member of LHX protein family. The first LIM domain of Isl: Isl is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Isl1 and Isl2 are the two conserved members of this family. Proteins in this group are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Isl-1 is one of the LHX proteins isolated originally by virtue of its ability to bind DNA sequences from the 5'-flanking region of the rat insulin gene in pancreatic insulin-producing cells. Mice deficient in Isl-1 fail to form the dorsal exocrine pancreas and islet cells fail to differentiate. On the other hand, Isl-1 takes part in the pituitary development by activating the gonadotropin-releasing hormone receptor gene together with LHX3 and steroidogenic factor 1. Mouse Is l2 is expressed in the retinal ganglion cells and the developing spinal cord where it plays a role in motor neuron development. Same as Isl1, Isl2 may also be able to bind to the insulin gene enhancer to promote gene activation. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CVGCGGKIHDQYILRVAPDLEWHAACLKCAECGQYLDETCTCFVRDGKTYCKRDY
>gnl|CDD|188753 cd09367, LIM1_Lhx1_Lhx5, The first LIM domain of Lhx1 (also known as Lim1) and Lhx5. The first LIM domain of Lhx1 (also known as Lim1) and Lhx5. Lhx1 and Lhx5 are closely related members of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx1 is required for regulating the vertebrate head organizer, the nervous system, and female reproductive tract development. During embryogenesis in the mouse, Lhx1 is expressed early in mesodermal tissue, then later during urogenital, kidney, liver, and nervous system development. In the adult, expression is restricted to the kidney and brain. A mouse embryos with Lhx1 gene knockout cannot grow normal anterior head structures, kidneys, and gonads, but with normally developed trunk and tail morphology. In the developing nervous system, Lhx1 is required to direct the trajectories of motor axons in the limb. Lhx1 null female mice lack the oviducts and uterus. Lhx5 protein may play complementary or overlapping roles with Lhx1. The expression of Lhx5 in the anterior portion of the mouse neural tube suggests a role in patterning of the forebrain. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAGCDRPILDKFLLNVLDRAWHAKCVQCCDCKCPLTEKCFSREGKLYCRNDF
>gnl|CDD|188754 cd09368, LIM1_Lhx3_Lhx4, The first LIM domain of Lhx3 and Lhx4 family. The first LIM domain of Lhx3-Lhx4 family: Lhx3 and Lhx4 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. The LHX3 and LHX4 LIM-homeodomain transcription factors play essential roles in pituitary gland and nervous system development. Although LHX3 and LHX4 share marked sequence homology, the genes have different expression patterns. They play overlapping, but distinct functions during the establishment of the specialized cells of the mammalian pituitary gland and the nervous system. Lhx3 proteins have been demonstrated the ability to directly bind to the promoters/enhancers of several pituitary hormone gene promoters to cause increased transcription. Lhx3a and Lhx3b, whose mRNAs have distinct temporal expression profiles during development, are two isoforms of Lhx3. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CGGCQEHILDRFILKVLDRTWHAKCLKCNDCGAQLTDKCFARNGHVYCKDDF
>gnl|CDD|188755 cd09369, LIM1_Lhx2_Lhx9, The first LIM domain of Lhx2 and Lhx9 family. The first LIM domain of Lhx2 and Lhx9 family: Lhx2 and Lhx9 are highly homologous LHX regulatory proteins. They belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Although Lhx2 and Lhx9 are highly homologous, they seems to play regulatory roles in different organs. In animals, Lhx2 plays important roles in eye, cerebral cortex, limb, the olfactory organs, and erythrocyte development. Lhx2 gene knockout mice exhibit impaired patterning of the cortical hem and the telencephalon of the developing brain, and a lack of development in olfactory structures. Lhx9 is expressed in several regions of the developing mouse brain, the spinal cord, the pancreas, in limb mesenchyme, and in the urogenital region. Lhx9 plays critical roles in gonad development. Homozygous mice lacking functional Lhx9 alleles exhibit numerous urogenital defects, such as gonadal agenesis, infertility, and undetectable levels of testosterone and estradiol coupled with high FSH levels. Lhx9 null mice are phenotypically female, even those that are genotypically male. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CAGCGEKIQDRFYLLAVDRQWHASCLKCCECRLPLDSELSCFSRDGNIYCKEDY
>gnl|CDD|188756 cd09370, LIM1_Lmx1a, The first LIM domain of Lmx1a. The first LIM domain of Lmx1a: Lmx1a belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Mouse Lmx1a is expressed in multiple tissues, including the roof plate of the neural tube, the developing brain, the otic vesicles, the notochord, and the pancreas. Human Lmx1a can be found in pancreas, skeletal muscle, adipose tissue, developing brain, mammary glands, and pituitary. The functions of Lmx1a in the developing nervous system were revealed by studies of mutant mouse. In mouse, mutations in Lmx1a result in failure of the roof plate to develop. Lmx1a may act upstream of other roof plate markers such as MafB, Gdf7, Bmp 6, and Bmp7. Further characterization of these mice reveals numerous defects including disorganized cerebellum, hippocampus, and cortex; altered pigmentation; female sterility; skeletal defects; and behavioral abnormalities. Within pancreatic cells, the Lmx1a protein interacts synergistically with the bHLH transcription factor E47 to activate the insulin gene enhancer/promoter. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CEGCNRVIQDRFLLRVNDSLWHERCLQCASCKEPLETTCFYRDKKLYCKEDY
>gnl|CDD|188757 cd09371, LIM1_Lmx1b, The first LIM domain of Lmx1b. The first LIM domain of Lmx1b: Lmx1b belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. In mouse, Lmx1b functions in the developing limbs and eyes, the kidneys, the brain, and in cranial mesenchyme. The disruption of Lmx1b gene results kidney and limb defects. In the brain, Lmx1b is important for generation of mesencephalic dopamine neurons and the differentiation of serotonergic neurons. In the mouse eye, Lmx1b regulates anterior segment (cornea, iris, ciliary body, trabecular meshwork, and lens) development. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CAGCQRPISDRYLLRVNERSWHEECLQCSVCQQPLTTSCYFRDRKLYCKQDYQ
>gnl|CDD|188758 cd09372, LIM2_FBLP-1, The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1). The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1): Fblp-1 contains a proline-rich domain near its N terminus and two LIM domains at its C terminus. FBLP-1 mRNA was detected in a variety of tissues and cells including platelets and endothelial cells. FBLP-1 binds to Filamins. The association between filamin B and FBLP-1 may play an unknown role in cytoskeletal function, cell adhesion, and cell motility. As in other LIM domains, this domain family is 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CAKCQGVITEHIIRALGKGYHPPCFTCVTCGRRIGDESFAVDEQNEVYCLDDY
>gnl|CDD|188759 cd09373, LIM1_AWH, The first LIM domain of Arrowhead (AWH). The first LIM domain of Arrowhead (AWH): Arrowhead belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. During embryogenesis of Drosophila, Arrowhead is expressed in each abdominal segment and in the labial segment. Late in embryonic development, expression of arrowhead is refined to the abdominal histoblasts and salivary gland imaginal ring cells themselves. The Arrowhead gene required for establishment of a subset of imaginal tissues: the abdominal histoblasts and the salivary gland imaginal rings. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CTGCGEPITDRFLLKVSGRSWHVSCLRCCVCQTPLERQPSCFTRDRQIYCKADY
>gnl|CDD|188760 cd09374, LIM2_Isl, The second LIM domain of Isl, a member of LHX protein family. The second LIM domain of Isl: Isl is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Isl1 and Isl2 are the two conserved members of this family. Proteins in this group are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Isl-1 is one of the LHX proteins isolated originally by virtue of its ability to bind DNA sequences from the 5'-flanking region of the rat insulin gene in pancreatic insulin-producing cells. Mice deficient in Isl-1 fail to form the dorsal exocrine pancreas and islet cells fail to differentiate. On the other hand, Isl-1 takes part in the pituitary development by activating the gonadotropin-releasing hormone receptor gene together with LHX3 and steroidogenic factor 1. Mouse Isl2 is expressed in the retinal ganglion cells and the developing spinal cord where it plays a role in motor neuron development. Same as Isl1, Isl2 may also be able to bind to the insulin gene enhancer to promote gene activation. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAKCQQSFSKNDFVMRARTKIYHIECFRCSACSRQLIPGDEFALRDDGLFCKADH
>gnl|CDD|188761 cd09375, LIM2_Lhx1_Lhx5, The second LIM domain of Lhx1 (also known as Lim1) and Lhx5. The second LIM domain of Lhx1 (also known as Lim1) and Lhx5. Lhx1 and Lhx5 are closely related members of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx1 is required for regulating the vertebrate head organizer, the nervous system, and female reproductive tract development. During embryogenesis in the mouse, Lhx1 is expressed early in mesodermal tissue, then later during urogenital, kidney, liver, and nervous system development. In the adult, expression is restricted to the kidney and brain. A mouse embryos with Lhx1 gene knockout cannot grow normal anterior head structures, kidneys, and gonads, but with normally developed trunk and tail morphology. In the developing nervous system, Lhx1 is required to direct the trajectories of motor axons in the limb. Lhx1 null female mice lack the oviducts and uterus. Lhx5 protein may play complementary or overlapping roles with Lhx1. The expression of Lhx5 in the anterior portion of the mouse neural tube suggests a role in patterning of the forebrain. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAGCDQGISPNDLVRRARDKVFHLNCFTCMVCRKQLSTGEELYILDENKFICKEDY
>gnl|CDD|188762 cd09376, LIM2_Lhx3_Lhx4, The second LIM domain of Lhx3-Lhx4 family. The second LIM domain of Lhx3-Lhx4 family: Lhx3 and Lhx4 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. The LHX3 and LHX4 LIM-homeodomain transcription factors play essential roles in pituitary gland and nervous system development. Although LHX3 and LHX4 share marked sequence homology, the genes have different expression patterns. They play overlapping, but distinct functions during the establishment of the specialized cells of the mammalian pituitary gland and the nervous system. Lhx3 proteins have been demonstrated the ability to directly bind to the promoters/enhancers of several pituitary hormone gene promoters to cause increased transcription.Lhx3a and Lhx3b, whose mRNAs have distinct temporal expression profiles during development, are two isoforms of Lhx3. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CAGCDEGIPPTQVVRRAQDNVYHLECFACFMCKRQLETGDEFYLMEDDRLVCKKDY
>gnl|CDD|188763 cd09377, LIM2_Lhx2_Lhx9, The second LIM domain of Lhx2 and Lhx9 family. The second LIM domain of Lhx2 and Lhx9 family: Lhx2 and Lhx9 are highly homologous LHX regulatory proteins. They belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Although Lhx2 and Lhx9 are highly homologous, they seems to play regulatory roles in different organs. In animals, Lhx2 plays important roles in eye, cerebral cortex, limb, the olfactory organs, and erythrocyte development. Lhx2 gene knockout mice exhibit impaired patterning of the cortical hem and the telencephalon of the developing brain, and a lack of development in olfactory structures. Lhx9 is expressed in several regions of the developing mouse brain, the spinal cord, the pancreas, in limb mesenchyme, and in the urogenital region. Lhx9 plays critical roles in gonad development. Homozygous mice lacking functional Lhx9 alleles exhibit numerous urogenital defects, such as gonadal agenesis, infertility, and undetectable levels of testosterone and estradiol coupled with high FSH levels. Lhx9 null mice are phenotypically female, even those that are genotypically male. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
SVKRCARCHLGISASELVMRARDLVFHLNCFTCATCNKPLTKGDHFGMRDGLVYCRLHY
>gnl|CDD|188764 cd09378, LIM2_Lmx1a_Lmx1b, The second LIM domain of Lmx1a and Lmx1b. The second LIM domain of Lmx1a and Lmx1b: Lmx1a and Lmx1b belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. Mouse Lmx1a is expressed in multiple tissues, including the roof plate of the neural tube, the developing brain, the otic vesicles, the notochord, and the pancreas. In mouse, mutations in Lmx1a result in failure of the roof plate to develop. Lmx1a may act upstream of other roof plate markers such as MafB, Gdf7, Bmp6, and Bmp7. Further characterization of these mice reveals numerous defects including disorganized cerebellum, hippocampus, and cortex; altered pigmentation; female sterility, skeletal defects, and behavioral abnormalities. In the mouse, Lmx1b functions in the developing limbs and eyes, the kidneys, the brain, and in cranial mesenchyme. The disruption of Lmx1b gene results kidney and limb defects. In the brain, Lmx1b is important for generation of mesencephalic dopamine neurons and the differentiation of serotonergic neurons. In the mouse eye, Lmx1b regulates anterior segment (cornea, iris, ciliary body, trabecular meshwork, and lens) development. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CSGCLEKIAPSELVMRALENVYHLRCFCCCVCERQLQKGDEFVLKEGQLLCKSDY
>gnl|CDD|188765 cd09379, LIM2_AWH, The second LIM domain of Arrowhead (AWH). The second LIM domain of Arrowhead (AWH): Arrowhead belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. During embryogenesis of Drosophila, Arrowhead is expressed in each abdominal segment and in the labial segment. Late in embryonic development, expression of arrowhead is refined to the abdominal histoblasts and salivary gland imaginal ring cells themselves. The Arrowhead gene required for establishment of a subset of imaginal tissues: the abdominal histoblasts and the salivary gland imaginal rings. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CAKCSRNISASDWVRRARDHVYHLACFACDACKRQLSTGEEFALIEDRVLCKAHY
>gnl|CDD|188766 cd09380, LIM1_Lhx6, The first LIM domain of Lhx6. The first LIM domain of Lhx6. Lhx6 is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. Lhx6 functions in the brain and nervous system. It is expressed at high levels in several regions of the embryonic mouse CNS, including the telencephalon and hypothalamus, and the first branchial arch. Lhx6 is proposed to have a role in patterning of the mandible and maxilla, and in signaling during odontogenesis. In brain sections, knockdown of Lhx6 gene blocks the normal migration of neurons to the cortex. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CSSCGLEILDRYLLKVNNLIWHVRCLECSVCRTSLRQHNSCYIKNKEIFCKMDY
>gnl|CDD|188767 cd09381, LIM1_Lhx7_Lhx8, The first LIM domain of Lhx7 and Lhx8. The first LIM domain of Lhx7 and Lhx8: Lhx7 and Lhx8 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. Studies using mutant mice have revealed roles for Lhx7 and Lhx8 in the development of cholinergic neurons in the telencephalon and in basal forebrain development. Mice lacking alleles of the LIM-homeobox gene Lhx7 or Lhx8 display dramatically reduced number of forebrain cholinergic neurons. In addition, Lhx7 mutation affects male and female mice differently, with females appearing more affected than males. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
VCSSCGLEIVDKYLLKVNDLCWHVRCLSCSVCRTSLGRHTSCYIKDKDIFCKLDYF
>gnl|CDD|188768 cd09382, LIM2_Lhx6, The second LIM domain of Lhx6. The second LIM domain of Lhx6. Lhx6 is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. Lhx6 functions in brain and nervous system. It is expressed at high levels in several regions of the embryonic mouse CNS, including the telencephalon and hypothalamus, and the first branchial arch. Lhx6 is proposed to have a role in patterning of the mandible and maxilla, and in signaling during odontogenesis. In brain sections, knockdown of Lhx6 gene blocks the normal migration of neurons to the cortex. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CARCGRQIYASDWVRRARGNAYHLACFACFSCKRQLSTGEEFGLVEEKVLCRIHY
>gnl|CDD|188769 cd09383, LIM2_Lhx7_Lhx8, The second LIM domain of Lhx7 and Lhx8. The second LIM domain of Lhx7 and Lhx8: Lhx7 and Lhx8 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. Studies using mutant mice have revealed roles for Lhx7 and Lhx8 in the development of cholinergic neurons in the telencephalon and in basal forebrain development. Mice lacking alleles of the LIM-homeobox gene Lhx7 or Lhx8 display dramatically reduced number of forebrain cholinergic neurons. In addition, Lhx7 mutation affects male and female mice differently, with females appearing more affected than males. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CSRCGRHIHSTDWVRRAKGNVYHLACFACFSCKRQLSTGEEFALVEEKVLCRVHY
>gnl|CDD|188770 cd09384, LIM1_LMO2, The first LIM domain of LMO2 (LIM domain only protein 2). The first LIM domain of LMO2 (LIM domain only protein 2): LMO2 is a nuclear protein that plays important roles in transcriptional regulation and development. The two tandem LIM domains of LMO2 support the assembly of a crucial cell-regulatory complex by interacting with both the TAL1-E47 and GATA1 transcription factors to form a DNA-binding complex that is capable of transcriptional activation. LMOs have also been shown to be involved in oncogenesis. LMO1 and LMO2 are activated in T-cell acute lymphoblastic leukemia by distinct chromosomal translocations. LMO2 was also shown to be involved in erythropoiesis and is required for the hematopoiesis in the adult animals. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CGGCQQNIGDRYFLKAIDQYWHEDCLSCDLCGCRLGEVGRRLYYKLGRKLCRRDYL
>gnl|CDD|188771 cd09385, LIM2_LMO2, The second LIM domain of LMO2 (LIM domain only protein 2). The second LIM domain of LMO2 (LIM domain only protein 2): LMO2 is a nuclear protein that plays important roles in transcriptional regulation and development. The two tandem LIM domains of LMO2 support the assembly of a crucial cell-regulatory complex by interacting with both the TAL1-E47 and GATA1 transcription factors to form a DNA-binding complex that is capable of transcriptional activation. LMOs have also been shown to be involved in oncogenesis. LMO1 and LMO2 are activated in T-cell acute lymphoblastic leukemia by distinct chromosomal translocations. LMO2 was also shown to be involved in erythropoiesis and is required for the hematopoiesis in the adult animals. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CASCDKRIRAYEMTMRVKDKVYHLECFKCAACQKHFCVGDRYLLINSDIVCEQDIY
>gnl|CDD|188772 cd09386, LIM1_LMO4, The first LIM domain of LMO4 (LIM domain only protein 4). The first LIM domain of LMO4 (LIM domain only protein 4): LMO4 is a nuclear protein that plays important roles in transcriptional regulation and development. LMO4 is involved in various functions in tumorigenesis and cellular differentiation. LMO4 proteins regulate gene expression by interacting with a wide variety of transcription factors and cofactors to form large transcription complexes. It can interact with Smad proteins, and associate with the promoter of the PAI-1 (plasminogen activator inhibitor-1) gene in a TGFbeta (transforming growth factor beta)-dependent manner. LMO4 can also form a complex with transcription regulator CREB (cAMP response element-binding protein) and interact with CLIM1 and CLIM2. In breast tissue, LMO4 interacts with multiple proteins, including the cofactor CtIP [CtBP (C-terminal binding protein)-interacting protein], the breast and ovarian tumor suppressor BRCA1 (breast-cancer susceptibility gene 1) and the LIM-domain-binding protein LDB1. Functionally, LMO4 is shown to repress BRCA1-mediated transcription activation, thus invoking a potential role for LMO4 as a negative regulator of BRCA1 in sporadic breast cancer. LMO4 also forms complex to both ERa (oestrogen receptor alpha), MTA1 (metastasis tumor antigen 1), and HDACs (histone deacetylases), implying that LMO4 is also a component of the MTA1 corepressor complex. Over-expressed LMO4 represses ERa transactivation functions in an HDAC-dependent manner, and contributes to the process of breast cancer progression by allowing the development of Era-negative phenotypes. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAGCGGKIVDRFLLHALDRYWHNGCLKCSCCQAQLGEIGSSCYTKGGMILCKNDY
>gnl|CDD|188773 cd09387, LIM2_LMO4, The second LIM domain of LMO4 (LIM domain only protein 4). The second LIM domain of LMO4 (LIM domain only protein 4): LMO4 is a nuclear protein that plays important roles in transcriptional regulation and development. LMO4 is involved in various functions in tumorigenesis and cellular differentiation. LMO4 proteins regulate gene expression by interacting with a wide variety of transcription factors and cofactors to form large transcription complexes. It can interact with Smad proteins, and associate with the promoter of the PAI-1 (plasminogen activator inhibitor-1) gene in a TGFbeta (transforming growth factor beta)-dependent manner. LMO4 can also form a complex with transcription regulator CREB (cAMP response element-binding protein) and interact with CLIM1 and CLIM2. In breast tissue, LMO4 interacts with multiple proteins, including the cofactor CtIP [CtBP (C-terminal binding protein)-interacting protein], the breast and ovarian tumor suppressor BRCA1 (breast-cancer susceptibility gene 1) and the LIM-domain-binding protein LDB1. Functionally, LMO4 is shown to repress BRCA1-mediated transcription activation, thus invoking a potential role for LMO4 as a negative regulator of BRCA1 in sporadic breast cancer. LMO4 also forms complex to both ERa (oestrogen receptor alpha), MTA1 (metastasis tumor antigen 1), and HDACs (histone deacetylases), implying that LMO4 is also a component of the MTA1 corepressor complex. Over-expressed LMO4 represses ERa transactivation functions in an HDAC-dependent manner, and contributes to the process of breast cancer progression by allowing the development of Era-negative phenotypes. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CSACGQSIPASELVMRAQGNVYHLKCFTCSTCHNQLVPGDRFHYVNGSLFCEHDR
>gnl|CDD|188774 cd09388, LIM1_LMO1_LMO3, The first LIM domain of LMO1 and LMO3 (LIM domain only protein 1 and 3). The first LIM domain of LMO1 and LMO3 (LIM domain only protein 1 and 3): LMO1 and LMO3 are highly homologous and belong to the LMO protein family. LMO1 and LMO3 are nuclear protein that plays important roles in transcriptional regulation and development. As LIM domains lack intrinsic DNA-binding activity, nuclear LMOs are involved in transcriptional regulation by forming complexes with other transcription factors or cofactors. For example, LMO1 interacts with the the bHLH domain of bHLH transcription factor, TAL1 (T-cell acute leukemia1)/SCL (stem cell leukemia) . LMO1 inhibits the expression of TAL1/SCL target genes. LMO3 facilitates p53 binding to its response elements, which suggests that LMO3 acts as a co-repressor of p53, suppressing p53-dependent transcriptional regulation. In addition, LMO3 interacts with neuronal transcription factor, HEN2, and acts as an oncogene in neuroblastoma. Another binding partner of LMO3 is calcium- and integrin-binding protein CIB, which binds via the second LIM domain (LIM2) of LMO3. One role of the CIB/LMO3 complex is to inhibit cell proliferation. Although LMO1 and LMO3 are highly homologous proteins, they play different roles in the regulation of the pituitary glycoprotein hormone alpha-subunit (alpha GSU) gene. Alpha GSU promoter activity was markedly repressed by LMO1 but activated by LMO3. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAGCNRKIKDRYLLKALDQYWHEDCLKCACCDCRLGEVGSTLYTKANLILCRRDY
>gnl|CDD|188775 cd09389, LIM2_LMO1_LMO3, The second LIM domain of LMO1 and LMO3 (LIM domain only protein 1 and 3). The second LIM domain of LMO1 and LMO3 (LIM domain only protein 1 and 3): LMO1 and LMO3 are highly homologous and belong to the LMO protein family. LMO1 and LMO3 are nuclear protein that plays important roles in transcriptional regulation and development. As LIM domains lack intrinsic DNA-binding activity, nuclear LMOs are involved in transcriptional regulation by forming complexes with other transcription factors or cofactors. For example, LMO1 interacts with the the bHLH domain of bHLH transcription factor, TAL1 (T-cell acute leukemia1)/SCL (stem cell leukemia) . LMO1 inhibits the expression of TAL1/SCL target genes. LMO3 facilitates p53 binding to its response elements, which suggests that LMO3 acts as a co-repressor of p53, suppressing p53-dependent transcriptional regulation. In addition, LMO3 interacts with neuronal transcription factor, HEN2, and acts as an oncogene in neuroblastoma. Another binding partner of LMO3 is calcium- and integrin-binding protein CIB, which binds via the second LIM domain (LIM2) of LMO3. One role of the CIB/LMO3 complex is to inhibit cell proliferation. Although LMO1 and LMO3 are highly homologous proteins, they play different roles in the regulation of the pituitary glycoprotein hormone alpha-subunit (alpha GSU) gene. Alpha GSU promoter activity was markedly repressed by LMO1 but activated by LMO3. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAACSKLIPAFEMVMRAKDNVYHLDCFACQLCNQRFCVGDKFFLKNNMILCQMDY
>gnl|CDD|188776 cd09390, LIM2_dLMO, The second LIM domain of dLMO (Beaderx). The second LIM domain of dLMO (Beaderx): dLMO is a nuclear protein that plays important roles in transcriptional regulation and development. In Drosophila dLMO modulates the activity of LIM-homeodomain protein Apterous (Ap), which regulates the formation of the dorsal-ventral axis of the Drosophila wing. Biochemical analysis shows that dLMO protein influences the activity of Apterous by binding of its cofactor Chip. Further studies shown that dLMO proteins might function in an evolutionarily conserved mechanism involved in patterning the appendages. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAACSKTIPAFEMVMRARTNVYHLECFACQRCNHRFCVGDRFYLCENKILCEYDY
>gnl|CDD|188777 cd09391, LIM1_Lrg1p_like, The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein. The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CAKCGKPITGQFVRALGDVYHLDCFTCHDCGKPVASKFFPVDDPDTSEQVPLCETDY
>gnl|CDD|188778 cd09392, LIM2_Lrg1p_like, The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein. The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CFKCGGALRGSYITALGRKYHVEHFTCSVCPTVFGPNDSYYEHEGKIYCHYHY
>gnl|CDD|188779 cd09393, LIM3_Lrg1p_like, The third LIM domain of Lrg1p, a LIM and RhoGap domain containing protein. The third LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CASCGKSIEDECIKFEDKRWHLKCFTCSRCHREISSELSDAAFNNKDQRILCSNCS
>gnl|CDD|188780 cd09394, LIM1_Rga, The first LIM domain of Rga GTPase-Activating Proteins. The first LIM domain of Rga GTPase-Activating Proteins: The members of this family contain two tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Rga activates GTPases during polarized morphogenesis. In yeast, a known regulating target of Rga is CDC42p, a small GTPase. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CVGCKESITEGHAYELGGDRWHIHCFKCYKCDKKLSCDSNFLVLGDGSLICSDCS
>gnl|CDD|188781 cd09395, LIM2_Rga, The second LIM domain of Rga GTPase-Activating Proteins. The second LIM domain of Rga GTPase-Activating Proteins: The members of this family contain two tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Rga activates GTPases during polarized morphogenesis. In yeast, a known regulating target of Rga is CDC42p, a small GTPase. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CKNCGKKIDDTAILLSSDEAYCSDCFRCRRCSRDITDLKYAKTKRGLFCMSCH
>gnl|CDD|188782 cd09396, LIM_DA1, The Lim domain of DA1. The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain of unknown function. DA1 is predicted as an ubiquitin receptor, which sets final seed and organ size by restricting the period of cell proliferation. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CAGCKSEIGHGRFLSALGAVWHPECFRCHACRKPIAEHEFSVSGNDPYHKSCY
>gnl|CDD|188783 cd09397, LIM1_UF1, LIM domain in proteins of unknown function. The first Lim domain of a LIM domain containing protein: The functions of the proteins are unknown. The members of this family contain two copies of LIM domain. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CRKCGLEIEGKSISSKDGELSGQWHRECFVCTTCGCPFQFSVPCYVLDDKPYCQQHYH
>gnl|CDD|188784 cd09400, LIM_like_1, LIM domain in proteins of unknown function. LIM domain in proteins of unknown function: LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation, and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. The LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid)
RREPCASCGLPVFLAERLLIEGKVYHRTCFKCARCGVQLTPGSFYETEYGSYCCETCPDEE
>gnl|CDD|188785 cd09401, LIM_TLP_like, The LIM domains of thymus LIM protein (TLP). The LIM domain of thymus LIM protein (TLP) like proteins: This family includes the LIM domains of TLP and CRIP (Cysteine-Rich Intestinal Protein). TLP is the distant member of the CRP family of proteins. TLP has two isomers (TLP-A and TLP-B) and sharing approximately 30% with each of the three other CRPs. Like CRP1, CRP2 and CRP3/MLP, TLP has two LIM domains, connected by a flexible linker region. Unlike the CRPs, TLP lacks the nuclear targeting signal (K/R-K/R-Y-G-P-K) and is localized solely in the cytoplasm. TLP is specifically expressed in the thymus in a subset of cortical epithelial cells. TLP has a role in development of normal thymus and in controlling the development and differentiation of thymic epithelial cells. CRIP is a short LIM protein with only one LIM domain. CRIP gene is developmentally regulated and can be induced by glucocorticoid hormones during the first three postnatal weeks. The domain shows close sequence homology to LIM domain of thymus LIM protein. However, unlike the TLP proteins which have two LIM domains, the members of this family have only one LIM domain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CPKCGKPVYFAEKKTSLGRDWHKPCLRCEKCKKTLTPGQHSEHEGKPYCNKCY
>gnl|CDD|188786 cd09402, LIM1_CRP, The first LIM domain of Cysteine Rich Protein (CRP). The first LIM domain of Cysteine Rich Protein (CRP): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to a short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription control, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. It is evident that CRP1, CRP2, and CRP3/MLP are involved in promoting protein assembly along the actin-based cytoskeleton. Although members of the CRP family share common binding partners, they are also capable of recognizing different and specific targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CGACEKTVYHAEEVQCEGRSFHKSCFLCMVCRKNLDSTTVAAHEDEIYCKSCY
>gnl|CDD|188787 cd09403, LIM2_CRP, The second LIM domain of Cysteine Rich Protein (CRP). The second LIM domain of Cysteine Rich Protein (CRP): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to a short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription control, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. It is evident that CRP1, CRP2, and CRP3/MLP are involved in promoting protein assembly along the actin-based cytoskeleton. Although members of the CRP family share common binding partners, they are also capable of recognizing different and specific targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residu es, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CPRCGKSVYAAEKIIGAGKPWHKNCFRCAKCGKSLESTTLADKDGEIYCKGCYA
>gnl|CDD|188788 cd09404, LIM1_MLP84B_like, The LIM domain of Mlp84B and Mlp60A. The LIM domain of Mlp84B and Mlp60A: Mlp84B and Mlp60A belong to the CRP LIM domain protein family. The Mlp84B protein contains five copies of the LIM domains, each followed by a Glycin Rich Region (GRR). However, only the first LIM domain of Mlp84B is in this family. Mlp60A exhibits only one LIM domain linked to a glycin-rich region. Mlp84B and Mlp60A are muscle specific proteins and have been implicated in muscle differentiation. While Mlp84B transcripts are enriched at the terminal ends of muscle fibers, Mlp60A transcripts are found throughout the muscle fibers. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
KCPKCGKSVYAAEERLAGGYKWHKMCFKCGMCNKLLDSTNCAEHEGELYCKQCH
>gnl|CDD|188789 cd09405, LIM1_Paxillin, The first LIM domain of paxillin. The first LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight cons erved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
VCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYH
>gnl|CDD|188790 cd09406, LIM1_Leupaxin, The first LIM domain of Leupaxin. The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
GDCASCQKPIAGQVVTALGQTWHPEHFVCCQCGKELGSRPFFERNGQAYCEEDYH
>gnl|CDD|188791 cd09407, LIM2_Paxillin, The second LIM domain of paxillin. The second LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGPEGFHEKDGKAYCRKDY
>gnl|CDD|188792 cd09408, LIM2_Leupaxin, The second LIM domain of Leupaxin. The second LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAYCAGPILQNVLTAMDQTWHPEHFFCSHCGELFGDEGFLERDGKPYCRRDF
>gnl|CDD|188793 cd09409, LIM3_Paxillin, The third LIM domain of paxillin. The third LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CGGCARAILENYISALNTLWHPECFVCRECFTPFVNGSFFEHDGQPYCEAHYH
>gnl|CDD|188794 cd09410, LIM3_Leupaxin, The third LIM domain of Leupaxin. The third LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CSGCGRPVKENYLSAANGVWHPECFVCSDCLKPFTDGSFFELDGRPLCELHYH
>gnl|CDD|188795 cd09411, LIM4_Paxillin, The fourth LIM domain of Paxillin. The fourth LIM domain of Paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CSGCQKPITGRCITAMGKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCHNCF
>gnl|CDD|188796 cd09412, LIM4_Leupaxin, The fourth LIM domain of Leupaxin. The fourth LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CGSCGLPITGRCISALGRKFHPEHFVCAFCLRPLTQGSFKEQSGKPYCSTCF
>gnl|CDD|188797 cd09413, LIM1_Testin, The first LIM domain of Testin. The first LIM domain of Testin: Testin contains three C-terminal LIM domains and a PET protein-protein interaction domain at the N-terminal. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell-contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and it is involved in cell motility and adhesion events. Knockout mice experiments reveal that tumor repressor function of Testin. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CYCCKQPMKEGDPAVYAERAGYDKLWHPACFVCSTCGELLVDMIYFWKNGKLYCGRHY
>gnl|CDD|188798 cd09414, LIM1_LIMPETin, The first LIM domain of protein LIMPETin. The first LIM domain of protein LIMPETin: LIMPETin contains 6 LIM domains at the C-terminal and an N-terminal PET domain. Four of the six LIM domains are highly homologous to the four and half LIM domain protein family and two of them show sequence similarity to the LIM domains of the Testin family. Thus, LIMPETin may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Its differential expression indicates that it is a transcription regulator. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CGGCSEPLKYGELAVTAPKFGESLLWHPACFRCSTCEELLVDLTYCVHDDQIYCERHY
>gnl|CDD|188799 cd09415, LIM1_Prickle, The first LIM domain of Prickle. The first LIM domain of Prickle: Prickle contains three C-terminal LIM domains and a N-terminal PET domain. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). PCP establishment requires the conserved Frizzled/Dishevelled PCP pathway. Prickle interacts with Dishevelled, thereby modulating Frizzled/Dishevelled activity and PCP signaling. Four forms of prickles have been identified: prickle 1-4. The best characterized is prickle 1 and prickle 2 which are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. Mutations in prickle 1 have been linked to progressive myoclonus epilepsy. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CEQCGEQISGGDIAVFASRAGPGACWHPACFVCSTCKELLVDLIYFYQDGKVYCGRHHA
>gnl|CDD|188800 cd09416, LIM2_Testin, The second LIM domain of Testin. The second LIM domain of Testin: Testin contains three C-terminal LIM domains and a PET protein-protein interaction domain at the N-terminal. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell-contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and it is involved in cell motility and adhesion events. Knockout mice experiments reveal that tumor repressor function of testin. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
PRCAGCDELIFSNEYTQAENQNWHLKHFCCFDCDNILAGEIYVMVNDKPVCKPCYM
>gnl|CDD|188801 cd09417, LIM2_LIMPETin_like, The second LIM domain of protein LIMPETin and related proteins. The second LIM domain of protein LIMPETin: LIMPETin contains 6 LIM domains at the C-terminal and an N-terminal PET domain. Four of the six LIM domains are highly homologous to the four and half LIM domain protein family and two of them show sequence similarity to the LIM domains of the testin family. Thus, LIMPETin may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Its differential expression indicates that it is a transcription regulator. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
DRSVQCDELIFSGEYTKAMNKDWHSGHFCCWQCDESLTGQRYVLRDEHPYCIKCYE
>gnl|CDD|188802 cd09418, LIM2_Prickle, The second LIM domain of Prickle. The second LIM domain of Prickle: Prickle contains three C-terminal LIM domains and a N-terminal PET domain. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). PCP establishment requires the conserved Frizzled/Dishevelled PCP pathway. Prickle interacts with Dishevelled, thereby modulating Frizzled/Dishevelled activity and PCP signaling. Two forms of prickles have been identified; namely prickle 1 and prickle 2. Prickle 1 and prickle 2 are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
PRCSACDEIIFADECTEAEGRHWHMKHFCCFECECQLGGQRYIMREGRPYCCHCFE
>gnl|CDD|188803 cd09419, LIM3_Testin, The third LIM domain of Testin. The third LIM domain of Testin: Testin contains three C-terminal LIM domains and a PET protein-protein interaction domain at the N-terminal. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers at cell-cell-contact areas and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and it is involved in cell motility and adhesion events. Knockout mice experiments reveal that tumor repressor function of Testin. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CQGCHNAIDPEVQRVSYNNFHWHAEPECFLCSCCSKCLIGQKFMPVEGMVFCSVECKKK
>gnl|CDD|188804 cd09420, LIM3_Prickle, The third LIM domain of Prickle. The third LIM domain of Prickle: Prickle contains three C-terminal LIM domains and a N-terminal PET domain. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). PCP establishment requires the conserved Frizzled/Dishevelled PCP pathway. Prickle interacts with Dishevelled, thereby modulating Frizzled/Dishevelled activity and PCP signaling. Two forms of prickles have been identified; namely prickle 1 and prickle 2. Prickle 1 and prickle 2 are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
EYCDTCGEHIGVDQGQMTYDGQHWHATEKCFCCAQCKKSLLGRPFLPKQGQIYCSRACS
>gnl|CDD|188805 cd09421, LIM3_LIMPETin, The third LIM domain of protein LIMPETin. The third LIM domain of protein LIMPETin: LIMPETin contains 6 LIM domains at the C-terminal and an N-terminal PET domain. Four of the six LIM domains are highly homologous to the four and half LIM domain protein family and two of them show sequence similarity to the LIM domains of the testin family. Thus, LIMPETin may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Its differential expression indicates that it is a transcription regulator. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
FANQCEECSKIIGIDSKDLSYKDKHWHEACFLCSKCKISLVDKPFGSKADRIYCGNCYD
>gnl|CDD|188806 cd09422, LIM1_FHL2, The first LIM domain of Four and a half LIM domains protein 2 (FHL2). The first LIM domain of Four and a half LIM domains protein 2 (FHL2): FHL2 is one of the best studied FHL proteins. FHL2 expression is most abundant in the heart, and in brain, liver and lung at lesser extent. FHL2 participates in a wide range of cellular processes, such as transcriptional regulation, signal transduction, and cell survival by binding to various protein partners. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. Although FHL2 is abundantly expressed in heart, the fhl2 null mice are viable and had no detectable abnormal cardiac phenotype. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
YSNTCEECKKPIGCDCKDLSYKDRHWHESCFHCFQCKNSLVDKPFAAKEEHLLCTECYSNEY
>gnl|CDD|188807 cd09423, LIM1_FHL3, The first LIM domain of Four and a half LIM domains protein 3 (FHL3). The first LIM domain of Four and a half LIM domains protein 3 (FHL3): FHL3 is highly expressed in the skeleton and cardiac muscles and possesses the transactivation and repression activities. FHL3 interacts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. Moreover, FHL3 interacts with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor. FHL3 was also proved to possess the auto-activation ability and was confirmed that the second zinc finger motif in fourth LIM domain was responsible for the auto-activation of FHL3. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
FANTCDECKELIGHDSRELYYEDRHYHEHCFRCFRCDRSLADEPFTCQDEELLCNDCYC
>gnl|CDD|188808 cd09424, LIM2_FHL1, The second LIM domain of Four and a half LIM domains protein 1 (FHL1). The second LIM domain of Four and a half LIM domains protein 1 (FHL1): FHL1 is heavily expressed in skeletal and cardiac muscles. It plays important roles in muscle growth, differentiation, and sarcomere assembly by acting as a modulator of transcription factors. Defects in FHL1 gene are responsible for a number of Muscular dystrophy-like muscle disorders. It has been detected that FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CKGCYKDILAGDQNVEYKGNVWHKDCFTCSNCKQPIGTKSFFPKGEDFYCVPCHEKKF
>gnl|CDD|188809 cd09425, LIM4_LIMPETin, The fourth LIM domain of protein LIMPETin. The fourth LIM domain of protein LIMPETin: LIMPETin contains 6 LIM domains at the C-terminal and an N-terminal PET domain. Four of the six LIM domains are highly homologous to the four and half LIM domain protein family and two of them show sequence similarity to the LIM domains of the Testin family. Thus, LIMPETin may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Its differential expression indicates that it is a transcription regulator. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CDGCGEIFRAGMKKMEYKGQQWHEKCFCCCECKQPIGTKSFIPKDDDVYCVPCY
>gnl|CDD|188810 cd09426, LIM2_FHL2, The second LIM domain of Four and a half LIM domains protein 2 (FHL2). The second LIM domain of Four and a half LIM domains protein 2 (FHL2): FHL2 is one of the best studied FHL proteins. FHL2 expression is most abundant in the heart, and in brain, liver and lung to a lesser extent. FHL2 participates in a wide range of cellular processes, such as transcriptional regulation, signal transduction, and cell survival by binding to various protein partners. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. Although FHL2 is abundantly expressed in heart, the fhl2 null mice are viable and had no detectable abnormal cardiac phenotype. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to s upport the assembly of multimeric protein complexes
CSECKKTIMPGTRKMEYKGNSWHETCFICQRCQQPIGTKSFIPKDNQNFCVPCYEKQ
>gnl|CDD|188811 cd09427, LIM2_FHL3, The second LIM domain of Four and a half LIM domains protein 3 (FHL3). The second LIM domain of Four and a half LIM domains protein 3 (FHL3): FHL3 is highly expressed in the skeleton and cardiac muscles and possesses the transactivation and repression activities. FHL3 interacts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. Moreover, FHL3 interacts with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor. FHL3 was also proved to possess the auto-activation ability and was confirmed that the second zinc finger motif in fourth LIM domain was responsible for the auto-activation of FHL3. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
SSKCVACGKTVMPGSRKLEYEGQTWHEHCFICHGCEQPIGSRSFIPDKDEHYCVPCYE
>gnl|CDD|188812 cd09428, LIM2_FHL5, The second LIM domain of Four and a half LIM domains protein 5 (FHL5). The second LIM domain of Four and a half LIM domains protein 5 (FHL5): FHL5 is a tissue-specific coactivator of CREB/CREM family transcription factors, which are highly expressed in male germ cells and is required for post-meiotic gene expression. FHL5 associates with CREM and confers a powerful transcriptional activation function. Activation by CREB has known to occur upon phosphorylation at an essential regulatory site and the subsequent interaction with the ubiquitous coactivator CREB-binding protein (CBP). However, the activation by FHL5 is independent of phosphorylation and CBP association. It represents a new route for transcriptional activation by CREM and CREB. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CFHCKKTIMPGSRKLEFEGNEWHETCFVCQSCQQPIGTKPLITKENKNYCVPCF
>gnl|CDD|188813 cd09429, LIM3_FHL1, The third LIM domain of Four and a half LIM domains protein 1 (FHL1). The third LIM domain of Four and a half LIM domains protein 1 (FHL1): FHL1 is heavily expressed in skeletal and cardiac muscles. It plays important roles in muscle growth, differentiation, and sarcomere assembly by acting as a modulator of transcription factors. Defects in FHL1 gene are responsible for a number of Muscular dystrophy-like muscle disorders. It has been detected that FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CVKCNKPITSGGVTYQDQPWHSECFVCSSCSKKLAGQRFTAVEDQYYCVDCYK
>gnl|CDD|188814 cd09430, LIM5_LIMPETin, The fifth LIM domain of protein LIMPETin. The fifth LIM domain of protein LIMPETin: LIMPETin contains 6 LIM domains at the C-terminal and an N-terminal PET domain. Four of the six LIM domains are highly homologous to the four and half LIM domain protein family and two of them show sequence similarity to the LIM domains of the testin family. Thus, LIMPETin may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Its differential expression indicates that it is a transcription regulator. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CSKCNKIINSGGVTYKNEPWHRECFTCTNCSKSLAGQRFTSRDEKPYCADCF
>gnl|CDD|188815 cd09431, LIM3_Fhl2, The third LIM domain of Four and a half LIM domains protein 2 (FHL2). The third LIM domain of Four and a half LIM domains protein 2 (FHL2): FHL2 is one of the best studied FHL proteins. FHL2 expression is most abundant in the heart, and in brain, liver and lung to a lesser extent. FHL2 participates in a wide range of cellular processes, such as transcriptional regulation, signal transduction, and cell survival by binding to various protein partners. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. Although FHL2 is abundantly expressed in heart, the fhl2 null mice are viable and had no detectable abnormal cardiac phenotype. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to s upport the assembly of multimeric protein complexes
CVQCKKPITTGGVTYRDQPWHKECFVCTGCKKQLSGQRFTSRDDFAYCLNCFCNLYA
>gnl|CDD|188816 cd09432, LIM6_LIMPETin, The sixth LIM domain of protein LIMPETin. The sixth LIM domain of protein LIMPETin: LIMPETin contains 6 LIM domains at the C-terminal and an N-terminal PET domain. Four of the six LIM domains are highly homologous to the four and half LIM domain protein family and two of them show sequence similarity to the LIM domains of the testin family. Thus, LIMPETin may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Its differential expression indicates that it is a transcription regulator. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAACGKPITGIGGTKFISFEDRHWHNDCFNCAGCRTSLVGKGFITDGGRILCPDCA
>gnl|CDD|188817 cd09433, LIM4_FHL2, The fourth LIM domain of Four and a half LIM domains protein 2 (FHL2). The fourth LIM domain of Four and a half LIM domains protein 2 (FHL2): FHL2 is one of the best studied FHL proteins. FHL2 expression is most abundant in the heart, and in brain, liver and lung to a lesser extent. FHL2 participates in a wide range of cellular processes, such as transcriptional regulation, signal transduction, and cell survival by binding to various protein partners. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. Although FHL2 is abundantly expressed in heart, the fhl2 null mice are viable and had no detectable abnormal cardiac phenotype. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to s upport the assembly of multimeric protein complexes
CAGCTNPISGLGGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPECGKD
>gnl|CDD|188818 cd09434, LIM4_FHL3, The fourth LIM domain of Four and a half LIM domains protein 3 (FHL3). The fourth LIM domain of Four and a half LIM domains protein 3 (FHL3): FHL3 is highly expressed in the skeleton and cardiac muscles and possesses the transactivation and repression activities. FHL3 interacts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. Moreover, FHL3 interacts with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor. FHL3 was also proved to possess the auto-activation ability and was confirmed that the second zinc finger motif in fourth LIM domain was responsible for the auto-activation of FHL3. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAACNKPITGFGGGKYVSFEDRQWHQPCFKCSRCSVSLVGAGFFPDGDQILCRDCN
>gnl|CDD|188819 cd09435, LIM3_Zyxin, The third LIM domain of Zyxin. The third LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cellsubstratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CCVCSEPIMPEPGRDETVRVVALEKNFHMKCYKCEDCGRPLSIEADDNGCFPLDGHVLCMKCHTARA
>gnl|CDD|188820 cd09436, LIM3_TRIP6, The third LIM domain of Thyroid receptor-interacting protein 6 (TRIP6). The third LIM domain of Thyroid receptor-interacting protein 6 (TRIP6): TRIP6 is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal. TRIP6 protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner. TRIP6 recruits a number of molecules involved in actin assembly, cell motility, survival and transcriptional control. The function of TRIP6 in cell motility is regulated by Src-dependent phosphorylation at a Tyr residue. The phosphorylation activates the coupling to the Crk SH2 domain, which is required for the function of TRIP6 in promoting lysophosphatidic acid (LPA)-induced cell migration. TRIP6 can shuttle to the nucleus to serve as a coactivator of AP-1 and NF-kappaB transcriptional factors. Moreover, TRIP6 can form a ternary complex with the NHERF2 PDZ protein and LPA2 receptor to regulate LPA-induced activation of ERK and AKT, rendering cells resistant to chemotherapy. Recent evidence shows that TRIP6 antagonizes Fas-Induced apoptosis by enhancing the antiapoptotic effect of LPA in cells. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CSVCKEPIMPAPGQEETVRIVALDRDFHVQCYRCEDCGSLLSEGDNQGCYPLDGHILCKACNSARI
>gnl|CDD|188821 cd09437, LIM3_LPP, The third LIM domain of lipoma preferred partner (LPP). The third LIM domain of lipoma preferred partner (LPP): LPP is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal and proline-rich region at the N-terminal. LPP initially identified as the most frequent translocation partner of HMGA2 (High Mobility Group A2) in a subgroup of benign tumors of adipose tissue (lipomas). It was also shown to be rearranged in a number of other soft tissues, as well as in a case of acute monoblastic leukemia. In addition to its involvement in tumors, LPP was inedited as a smooth muscle restricted LIM protein that plays an important role in SMC migration. LPP is localized at sites of cell adhesion, cell-cell contacts and transiently in the nucleus. In nucleus, it acts as a coactivator for the ETS domain transcription factor PEA3. In addition to PEA3, it interacts with alpha-actinin,vasodilator stimulated phosphoprotein (VASP), Palladin, and Scrib. The LIM domains are the main focal adhesion targeting elements and that the proline- rich region, which harbors binding sites for alpha-actinin and vasodilator- stimulated phosphoprotein (VASP), has a weak targeting capacity. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CCVCKLPIMPEPGQDETVRVVALDRSFHVQCYKCEDCGLLLSSEAEGRGCYPLDDHVLCKSCNAKRVQ
>gnl|CDD|188822 cd09438, LIM3_Ajuba_like, The third LIM domain of Ajuba-like proteins. The third LIM domain of Ajuba-like proteins: Ajuba like LIM protein family includes three highly homologous proteins Ajuba, Limd1, and WTIP. Members of the family contain three tandem C-terminal LIM domains and a proline-rich N-terminal region. This family of proteins functions as scaffolds, participating in the assembly of numerous protein complexes. In the cytoplasm, Ajuba binds Grb2 to modulate serum-stimulated ERK activation. Ajuba also recruits the TNF receptor-associated factor 6 (TRAF6) to p62 and activates PKCKappa activity. Ajuba interacts with alpha-catenin and F-actin to contribute to the formation or stabilization of adheren junctions by linking adhesive receptors to the actin cytoskeleton. Although Ajuba is a cytoplasmic protein, it can shuttle into the nucleus. In nucleus, Ajuba functions as a corepressor for the zinc finger-protein Snail. It binds to the SNAG repression domain of Snail through its LIM region. Arginine methyltransferase-5 (Prmt5), a protein in the complex, is recruited to Snai l through an interaction with Ajuba. This ternary complex functions to repress E-cadherin, a Snail target gene. In addition, Ajuba contains functional nuclear-receptor interacting motifs and selectively interacts with retinoic acid receptors (RARs) and rexinoid receptor (RXRs) to negatively regulate retinoic acid signaling. Wtip, the Wt1-interacting protein, was originally identified as an interaction partner of the Wilms tumour protein 1 (WT1). Wtip is involved in kidney and neural crest development. Wtip interacts with the receptor tyrosine kinase Ror2 and inhibits canonical Wnt signaling. LIMD1 was reported to inhibit cell growth and metastases. The inhibition may be mediated through an interaction with the protein barrier-to-autointegration (BAF), a component of SWI/SNF chromatin-remodeling protein; or through the interaction with retinoblastoma protein (pRB), resulting in inhibition of E2F-mediated transcription, and expression of the majority of genes with E2F1- responsive elements. Recently, Limd1 was shown to interact with the p62/sequestosome protein and influence IL-1 and RANKL signaling by facilitating the assembly of a p62/TRAF6/a-PKC multi-protein complex. The Limd1-p62 interaction affects both NF-kappaB and AP-1 activity in epithelial cells and osteoclasts. Moreover, LIMD1 functions as tumor repressor to block lung tumor cell line in vitro and in vivo. Recent studies revealed that LIM proteins Wtip, LIMD1 and Ajuba interact with components of RNA induced silencing complexes (RISC) as well as eIF4E and the mRNA m7GTP cap-protein complex and are required for microRNA-mediated gene silencing. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CAACGQPILPAEGSEETIRVVSMDKDYHVECYHCEDCGLQLNDEEGHRCYPLDGHLLCHSCH
>gnl|CDD|188823 cd09439, LIM_Mical, The LIM domain of Mical (molecule interacting with CasL). The LIM domain of Mical (molecule interacting with CasL): MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semapho-rin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM domain and calporin homology domain are known for interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein monooxygenase (MO) is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL was characterized to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL was also named junctional Rab13-binding protein (JRAB). As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPHF
>gnl|CDD|188824 cd09440, LIM1_SF3, The first Lim domain of pollen specific protein SF3. The first Lim domain of pollen specific protein SF3: SF3 is a Lim protein that is found exclusively in mature plant pollen grains. It contains two LIM domains. The exact function of SF3 is unknown. It may be a transcription factor required for the expression of late pollen genes. It is possible that SF3 protein is involved in controlling pollen-specific processes such as male gamete maturation, pollen tube formation, or even fertilization. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
TTQKCKACDKTVYLVDQLSADGVVYHKSCFRCSHCKGTLKLSNYSSMEGVLYCKPHFEQLFKE
>gnl|CDD|188825 cd09441, LIM2_SF3, The second Lim domain of pollen specific protein SF3. The second Lim domain of pollen specific protein SF3: SF3 is a Lim protein that is found exclusively in mature plant pollen grains. It contains two LIM domains. The exact function of SF3 is unknown. It may be a transcription factor required for the expression of late pollen genes. It is possible that SF3 protein is involved in controlling pollen-specific processes such as male gamete maturation, pollen tube formation, or even fertilization. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CVACGKTVYPIEKVTVEGTSYHKSCFKCSHGGCTISPSNYAAHEGRLYCKHHHSQLFKEKG
>gnl|CDD|188826 cd09442, LIM_Eplin_like, The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin) like proteins. The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin) like proteins: This family contains Epithelial Protein Lost in Neoplasm in Neoplasm (Eplin), xin actin-binding repeat-containing protein 2 (XIRP2) and a group of protein with unknown function. The members of this family all contain a single LIM domain. Epithelial Protein Lost in Neoplasm is a cytoskeleton-associated tumor suppressor whose expression inversely correlates with cell growth, motility, invasion and cancer mortality. Eplin interacts and stabilizes F-actin filaments and stress fibers, which correlates with its ability to suppress anchorage independent growth. In epithelial cells, Eplin is required for formation of the F-actin adhesion belt by binding to the E-cadherin-catenin complex through alpha-catenin. Eplin is expressed in two isoforms, a longer Eplin-beta and a shorter Eplin-alpha. Eplin-alpha mRNA is detected in various tissues and cell lines, but is absent or down regulated in cancer cells. Xirp2 contains a LIM domain and Xin re peats for binding to and stabilising F-actin. Xirp2 is expressed in muscles and is significantly induced in the heart in response to systemic administration of angiotensin II. Xirp2 is an important effector of the Ang II signaling pathway in the heart. The expression of Xirp2 is activated by myocyte enhancer factor (MEF)2A, whose transcriptional activity is stimulated by angiotersin II. Thus, Xirp2 plays important pathological roles in the angiotensin II induced hypertension. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CTVCQKRVYPMERLIADKQNFHKSCFRCEHCNSKLSLGNYASLHGRIYCKPHF
>gnl|CDD|188827 cd09443, LIM_Ltd-1, The LIM domain of LIM and transglutaminase domains protein (Ltd-1). The LIM domain of LIM and transglutaminase domains protein (Ltd-1): This family includes mouse Ky protein and Caenorhabditis elegans Ltd-1 protein. The members of this family consists a N-terminal Lim domain and a C-terminal transglutaminase domain. The mouse Ky protein has putative function in muscle development. The mouse with ky mutant exhibits combined posterior and lateral curvature of the spine. The Ltd-1 gene in C. elegans is expressed in developing hypodermal cells from the twofold stage embryo through adulthood. These data define the ltd-1 gene as a novel marker for C. elegans epithelial cell development. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CPRCGKTAYPAESVDKDGTFYHKGCFKCRECGTRLSLKTFTFVQGDGEVYCARHV
>gnl|CDD|188828 cd09444, LIM_Mical_like_1, This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins. The LIM domain on proteins of unknown function: This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins. Known members of the Mical-like family includes single LIM domain containing proteins, Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2), and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth, and mobility. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CAACGQHVHLVQRHLVDGKLYHRNCFRCKECSSTLLPGSYKAGPEPGTFVCTHHH
>gnl|CDD|188829 cd09445, LIM_Mical_like_2, This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins. The LIM domain on proteins of unknown function: This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL)-like proteins. Known members of the Mical-like family includes single LIM domain containing proteins, Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2), and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth, and mobility. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CRSCGKPVYKMEEIIAEKHIYHKNCFRCKDCNKQLKVDNYQSHEGNLYCKVHF
>gnl|CDD|188830 cd09446, LIM_N_RAP, The LIM domain of N-RAP. The LIM domain of N-RAP: N-RAP is a muscle-specific protein concentrated at myotendinous junctions in skeletal muscle and intercalated disks in cardiac muscle. LIM domain is found at the N-terminus of N-RAP and the C-terminal of N-RAP contains a region with multiple of nebulin repeats. N-RAP functions as a scaffolding protein that organizes alpha-actinin and actin into symmetrical I-Z-I structures in developing myofibrils. Nebulin repeat is known as actin binding domain. The N-RAP is hypothesized to form antiparallel dimerization via its LIM domain. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CARCGYGVYPAEKINCIDQTWHKACFHCEVCKMMLTVNNFVSHQKKPYCQAHN
>gnl|CDD|188831 cd09447, LIM_LASP, The LIM domain of LIM and SH3 Protein (LASP). The LIM domain of LIM and SH3 Protein (LASP): LASP family contains two highly homologous members, LASP-1 and LASP-2. LASP contains a LIM motif at its amino terminus, a src homology 3 (SH3) domains at its C-terminal part, and a nebulin-like region in the middle. LASP-1 and -2 are highly conserved in their LIM, nebulin-like, and SH3 domains, but differ significantly at their linker regions. Both proteins are ubiquitously expressed and involved in cytoskeletal architecture, especially in the organization of focal adhesions. LASP-1 and LASP-2, are important during early embryo- and fetogenesis and are highly expressed in the central nervous system of the adult. However, only LASP-1 seems to participate significantly in neuronal differentiation and plays an important functional role in migration and proliferation of certain cancer cells while the role of LASP-2 is more structural. The expression of LASP-1 in breast tumors is increased significantly. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CARCGKTVYPTEKLNCLDKIWHKGCFKCEVCGMTLNMKNYKGYNKKPYCNAHY
>gnl|CDD|188832 cd09448, LIM_CLP36, This family represents the LIM domain of CLP36. This family represents the LIM domain of CLP36. CLP36 has also been named as CLIM1, Elfin, or PDLIM1. CLP36 contains a C-terminal LIM domain and an N-terminal PDZ domain. CLP36 is highly expressed in heart and is present in many other tissues including lung, liver, spleen, and blood. CLP36 has been implicated in many processes including hypoxia and regulation of actin stress fibers. CLP36 co-localizes with alpha-actinin-2 at the Z-lines in myocardium. In addition, CLP36 binds to alpha-actinin-1 and alpha-actinin-4, and associates with F-actin filaments and stress fibers. CLP36 might be involved in not only the function of sarcomeres in muscle cells, but also in actin stress fiber-mediated cellular processes, such as cell shape, migration, polarit, and cytokinesis in non-muscle cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CDKCGSGIVGVFVKIRDKPRHPECYVCTDCGTNLKQKGHFFVEDQIYCEKHA
>gnl|CDD|188833 cd09449, LIM_Mystique, The LIM domain of Mystique, a subfamily of ALP LIM domain proteins. The LIM domain of Mystique, a subfamily of ALP LIM domain proteins: Mystique is the most recently identified member of the ALP protein family. It also interacts with alpha-actinin, as other ALP proteins do. Mystique promotes cell attachment and migration and suppresses anchorage-independent growth. The LIM domain of Mystique is required for the suppression function. Moreover, Mystique functions as an ubiquitin E3 ligase acting on STAT proteins to cause their proteosome mediated degradation. As in all LIM domains, this domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CEKCGTSIVTQAVRIQEGRYRHPGCYTCTDCGLNLKMRGHFWAGEKMFCEKHA
>gnl|CDD|188834 cd09450, LIM_ALP, This family represents the LIM domain of ALP, actinin-associated LIM protein. This family represents the LIM domain of ALP, actinin-associated LIM protein. ALP contains an N-terminal PDZ domain, a C-terminal LIM domain and an ALP-subfamily-specific 34-amino-acid motif termed ALP-like motif (AM), which contains a putative consensus protein kinase C (PKC) phosphorylation site and two alpha-helices. ALP proteins are found in heart and in skeletal muscle. ALP may act as a signaling molecule which is regulated by PKC-dependent signaling. ALP plays an essential role in the development of RV (right ventricle) chamber. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CDKCGSGIVGTVVKARDKYRHPECFVCSDCNLNLKQKGYFFVEGQLYCEAHAR
>gnl|CDD|188835 cd09451, LIM_RIL, The LIM domain of RIL. The LIM domain of RIL: RIL contains an N-terminal PDZ domain, a LIM domain, and a short consensus C-terminal region. It is the smallest molecule in the ALP LIM domain containing protein family. RIL was identified in rat fibroblasts and in human lymphocytes. The LIM domain interacts with the AMPA glutamate receptor in dendritic spines. The consensus C-terminus interacts with PTP-BL, a submembranous protein tyrosine phosphatase and the PDZ domain is responsible to interact with alpha-actinin molecules. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CTRCGNGIVGTIVKARDKLYHPECFMCDDCGLNLKQRGYFFIDEQLYCETHAK
>gnl|CDD|188836 cd09452, LIM1_Enigma, The first LIM domain of Enigma. The first LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAQCNKIIRGRYLVALGRSYHPEEFTCSQCKKVLDEGGFFEEKGSIFCPKCY
>gnl|CDD|188837 cd09453, LIM1_ENH, The first LIM domain of the Enigma Homolog (ENH) family. The first LIM domain of the Enigma Homolog (ENH) family: ENH was initially identified in rat brain. Same as enigma, it contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ENH is implicated in signal transduction processes involving protein kinases. It has also been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ENH is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CATCNQVIRGPFLVALGKSWHPEEFNCAHCKSSMAYIGFVEEKGALYCEICY
>gnl|CDD|188838 cd09454, LIM1_ZASP_Cypher, The first LIM domain of ZASP/Cypher family. The first LIM domain of ZASP/Cypher family: ZASP was identified in human heart and skeletal muscle and Cypher is a mice ortholog of ZASP. ZASP/Cyppher contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CGHCNNIIRGPFLVALGRSWHPEEFTCHYCHTSLADVSFVEEQNNVYCENCY
>gnl|CDD|188839 cd09455, LIM1_Enigma_like_1, The first LIM domain of an Enigma subfamily with unknown function. The first LIM domain of an Enigma subfamily with unknown function: The Enigma LIM domain family is comprised of three characterized members: Enigma, ENH and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. They serve as adaptor proteins, where the PDZ domain tethers the protein to the cytoskeleton and the LIM domains, recruit signaling proteins to implement corresponding functions. The members of the Enigma family have been implicated in regulating or organizing cytoskeletal structure, as well as involving multiple signaling pathways. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CESCNQQIRGPFITALGKIWCPDHFICANASCRRPLQDIGFVEEKGQLYCEYCF
>gnl|CDD|188840 cd09456, LIM2_Enigma, The second LIM domain of Enigma. The second LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAKCKKKITGEIMHALKMTWHVHCFTCAACKTPIRNRAFYMEEGAPYCERDY
>gnl|CDD|188841 cd09457, LIM2_ENH, The second LIM domain of the Enigma Homolog (ENH) family. The second LIM domain of the Enigma Homolog (ENH) family: ENH was initially identified in rat brain. Same as enigma, it contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ENH is implicated in signal transduction processes involving protein kinases. It has also been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ENH is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CGRCQRKILGEVINALKQTWHVSCFVCVACHNPIRNNVFHLEDGEPYCETDY
>gnl|CDD|188842 cd09458, LIM3_Enigma, The third LIM domain of Enigma. The third LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CHGCDFKIDAGDRFLEALGFSWHDTCFVCAICQINLEGKTFYSKKDKPLCKSHAF
>gnl|CDD|188843 cd09459, LIM3_ENH, The third LIM domain of the Enigma Homolog (ENH) family. The third LIM domain of the Enigma Homolog (ENH) family: ENH was initially identified in rat brain. Same as enigma, it contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ENH is implicated in signal transduction processes involving protein kinases. It has also been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ENH is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CHGCEFPIEAGDRFLEALGHTWHDTCFVCSVCCESLEGQTFFSKKDKPLCKKHAH
>gnl|CDD|188844 cd09460, LIM3_ZASP_Cypher, The third LIM domain of ZASP/Cypher family. The third LIM domain of ZASP/Cypher family: ZASP was identified in human heart and skeletal muscle and Cypher is a mice ortholog of ZASP. ZASP/Cyppher contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CHGCDFPVEAGDKFIEALGHTWHDTCFICAVCHVNLEGQPFYSKKDKPLCKKHAH
>gnl|CDD|188845 cd09461, LIM3_Enigma_like_1, The third LIM domain of an Enigma subfamily with unknown function. The third LIM domain of an Enigma subfamily with unknown function: The Enigma LIM domain family is comprised of three characterized members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. They serve as adaptor proteins, where the PDZ domain tethers the protein to the cytoskeleton and the LIM domains, recruit signaling proteins to implement corresponding functions. The members of the enigma family have been implicated in regulating or organizing cytoskeletal structure, as well as involving multiple signaling pathways. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CVSCGFPIEAGDRWVEALNNNYHSQCFNCTRCNVNLEGQSFYAKGGRPFCKLHA
>gnl|CDD|188846 cd09462, LIM1_LIMK1, The first LIM domain of LIMK1 (LIM domain Kinase 1). The first LIM domain of LIMK1 (LIM domain Kinase 1): LIMK1 belongs to the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK1 is expressed in all tissues and is localized to focal adhesions in the cell. LIMK1 can form homodimers upon binding of HSP90 and is activated by Rho effector Rho kinase and MAPKAPK2. LIMK1 is important for normal central nervous system development, and its deletion has been implicated in the development of the human genetic disorder Williams syndrome. Moreover, LIMK1 up-regulates the promoter activity of urokinase type plasminogen activator and induces its mRNA and protein expression in breast cancer cells. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
LLCCTWKEERMGEEEGNVLPVCASCGQSIYDGQYLQALNSDWHADCFRCCECGASLSHWYYEKDGRLFCK
KDYW
>gnl|CDD|188847 cd09463, LIM1_LIMK2, The first LIM domain of LIMK2 (LIM domain Kinase 2). The first LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerization. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CTGCGGRIQDSFHYRVVQEAWHNSCFQCSVCQDLLTNWYYEKDGKLYCHKHYW
>gnl|CDD|188848 cd09464, LIM2_LIMK1, The second LIM domain of LIMK1 (LIM domain Kinase 1). The second LIM domain of LIMK1 (LIM domain Kinase 1): LIMK1 belongs to the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK1 is expressed in all tissues and is localized to focal adhesions in the cell. LIMK1 can form homodimers upon binding of HSP90 and is activated by Rho effector Rho kinase and MAPKAPK2. LIMK1 is important for normal central nervous system development, and its deletion has been implicated in the development of the human genetic disorder Williams syndrome. Moreover, LIMK1 up-regulates the promoter activity of urokinase type plasminogen activator and induces its mRNA and protein expression in breast cancer cells. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CHGCSETITTGLVMVAGEQKYHPECFSCLRCGAFIGDGDTYALVEHSKLYCGHCY
>gnl|CDD|188849 cd09465, LIM2_LIMK2, The second LIM domain of LIMK2 (LIM domain Kinase 2). The second LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerisation. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
KFGELCHGCSLLMTGPAMVAGEYKYHPECFACMSCKVIIEDGDTYALVQHTTLYCGKCH
>gnl|CDD|188850 cd09466, LIM1_Lhx3a, The first LIM domain of Lhx3a. The first LIM domain of Lhx3a: Lhx3a is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx3a is one of the two isoforms of Lhx3. The Lhx3 gene is expressed in the ventral spinal cord, the pons, the medulla oblongata, and the pineal gland of the developing nervous system during mouse embryogenesis, and transcripts are found in the emergent pituitary gland. Lhx3 functions in concert with other transcription factors to specify interneuron and motor neuron fates during development. Lhx3 proteins have been demonstrated to directly bind to the promoters of several pituitary hormone gene promoters. The Lhx3 gene encodes two isoforms, LHX3a and LHX3b that differ in their amino-terminal sequences, where Lhx3a has longer N-terminal. They show differential activation of pituitary hormone genes and distinct DNA binding properties. In human, Lhx3a trans-activated the alpha-glycoprotein subunit promoter and genes containing a high-affinity Lhx3 binding site more effectively than the hLhx3b isoform. In addition, hLhx3a induce transcription of the TSHbeta-subunit gene by acting on pituitary POU domain factor, Pit-1, while hLhx3b does not. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
IPKCAGCDHPIFDRFILKVQDKPWHSKCLKCVDCQAQLTDKCFSRGGQVYCKEDFF
>gnl|CDD|188851 cd09467, LIM1_Lhx3b, The first LIM domain of Lhx3b. The first LIM domain of Lhx3b. Lhx3b is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx3b is one of the two isoforms of Lhx3. The Lhx3 gene is expressed in the ventral spinal cord, the pons, the medulla oblongata, and the pineal gland of the developing nervous system during mouse embryogenesis, and transcripts are found in the emergent pituitary gland. Lhx3 functions in concert with other transcription factors to specify interneuron and motor neuron fates during development. Lhx3 proteins have been demonstrated to directly bind to the promoters of several pituitary hormone gene promoters. The Lhx3 gene encodes two isoforms, LHX3a and LHX3b that differ in their amino-terminal sequences, where Lhx3a has longer N-terminal. They show differential activation of pituitary hormone genes and distinct DNA binding properties. In human, Lhx3a trans-activated the alpha-glycoprotein subunit promoter and genes containing a high-affinity Lhx3 binding site more effectively than the hLhx3b isoform. In addition, hLhx3a induce transcription of the TSHbeta-subunit gene by acting on pituitary POU domain factor, Pit-1, while hLhx3b does not. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
IPLCAGCNQHIVDRFILKVLDRHWHSKCLKCSDCQTQLAEKCFSRGDSVYCKDDF
>gnl|CDD|188852 cd09468, LIM1_Lhx4, The first LIM domain of Lhx4. The first LIM domain of Lhx4. Lhx4 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CAGCNQHILDKFILKVLDRHWHSSCLKCADCQMQLAERCFSRAGNVYCKEDF
>gnl|CDD|188853 cd09469, LIM1_Lhx2, The first LIM domain of Lhx2. The first LIM domain of Lhx2: Lhx2 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. In animals, Lhx2 plays important roles in eye, cerebral cortex, limb, the olfactory organs, and erythrocyte development. Lhx2 gene knockout mice exhibit impaired patterning of the cortical hem and the telencephalon of the developing brain, and a lack of development in olfactory structures. The Lhx2 protein has been shown to bind to the mouse M71 olfactory receptor promoter. Similar to other LIM domains, this domain family is 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
PSISSDRAALCAGCGGKISDRYYLLAVDKQWHMRCLKCCECKLNLESELTCFSKDGSIYCKEDY
>gnl|CDD|188854 cd09470, LIM1_Lhx9, The first LIM domain of Lhx9. The first LIM domain of Lhx9: Lhx9 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx9 is highly homologous to Lhx2. It is expressed in several regions of the developing mouse brain, the spinal cord, the pancreas, in limb mesenchyme, and in the urogenital region. Lhx9 plays critical roles in gonad development. Homozygous mice lacking functional Lhx9 alleles exhibit numerous urogenital defects, such as gonadal agenesis, infertility, and undetectable levels of testosterone and estradiol coupled with high FSH levels. Lhx9 null mice have reduced levels of the Sf1 nuclear receptor that is required for gonadogenesis, and recent studies have shown that Lhx9 is able to activate the Sf1/FtzF1 gene. Lhx9 null mice are phenotypically female, even those that are genotypically male. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CAGCGGKISDRYYLLAVDKQWHLRCLKCCECKLALESELTCFAKDGSIYCKEDY
>gnl|CDD|188855 cd09471, LIM2_Isl2, The second LIM domain of Isl2. The second LIM domain of Isl2: Isl is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Isl proteins are found in the nucleus and act as transcription factors or cofactors. Isl1 and Isl2 are the two conserved members of this family. Mouse Isl2 is expressed in the retinal ganglion cells and the developing spinal cord where it plays a role in motor neuron development. Isl2 may be able to bind to the insulin gene enhancer to promote gene activation. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CAQCRLGFSSSDLVMRARDSVYHIECFRCSVCSRQLLPGDEFCLREHELLCRADH
>gnl|CDD|188856 cd09472, LIM2_Lhx3b, The second LIM domain of Lhx3b. The second LIM domain of Lhx3b. Lhx3b is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx3b is one of the two isoforms of Lhx3. The Lhx3 gene is expressed in the ventral spinal cord, the pons, the medulla oblongata, and the pineal gland of the developing nervous system during mouse embryogenesis, and transcripts are found in the emergent pituitary gland. Lhx3 functions in concert with other transcription factors to specify interneuron and motor neuron fates during development. Lhx3 proteins have been demonstrated to directly bind to the promoters of several pituitary hormone gene promoters. The Lhx3 gene encodes two isoforms, LHX3a and LHX3b that differ in their amino-terminal sequences, where Lhx3a has longer N-terminal. They show differential activation of pituitary hormone genes and distinct DNA binding properties. In human, Lhx3a trans-activated the alpha-glycoprotein subunit promoter and genes containing a high-affinity Lhx3 binding site more effectively than the hLhx3b isoform. In addition, hLhx3a induce transcription of the TSHbeta-subunit gene by acting on pituitary POU domain factor, Pit-1, while hLhx3b does not. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
KCAACQQGIPPTQVVRRAQDFVYHLHCFACIVCKRQLATGDEFYLMEDSRLVCKADY
>gnl|CDD|188857 cd09473, LIM2_Lhx4, The second LIM domain of Lhx4. The second LIM domain of Lhx4. Lhx4 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CTACQQGIPPTQVVRKAQDFVYHLHCFACIICSRQLATGDEFYLMEDGRLVCKEDY
>gnl|CDD|188858 cd09474, LIM2_Lhx2, The second LIM domain of Lhx2. The second LIM domain of Lhx2: Lhx2 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. In animals, Lhx2 plays important roles in eye, cerebral cortex, limb, the olfactory organs, and erythrocyte development. Lhx2 gene knockout mice exhibit impaired patterning of the cortical hem and the telencephalon of the developing brain, and a lack of development in olfactory structures. The Lhx2 protein has been shown to bind to the mouse M71 olfactory receptor promoter. Similar to other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
SVQRCARCHLGISASEMVMRARDLVYHLNCFTCTTCNKMLTTGDHFGMKDNLVYCRLHF
>gnl|CDD|188859 cd09475, LIM2_Lhx9, The second LIM domain of Lhx9. The second LIM domain of Lhx9: Lhx9 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx9 is highly homologous to Lhx2. It is expressed in several regions of the developing mouse brain, the spinal cord, the pancreas, in limb mesenchyme, and in the urogenital region. Lhx9 plays critical roles in gonad development. Homozygous mice lacking functional Lhx9 alleles exhibit numerous urogenital defects, such as gonadal agenesis, infertility, and undetectable levels of testosterone and estradiol coupled with high FSH levels. Lhx9 null mice have reduced levels of the Sf1 nuclear receptor that is required for gonadogenesis, and recent studies have shown that Lhx9 is able to activate the Sf1/FtzF1 gene. Lhx9 null mice are phenotypically female, even those that are genotypically male. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
SVQRCARCHLGISASEMVMRARESVYHLSCFTCTTCNKTLTTGDHFGMKDNLVYCRAHF
>gnl|CDD|188860 cd09476, LIM1_TLP, The first LIM domain of thymus LIM protein (TLP). The first LIM domain of thymus LIM protein (TLP): TLP is the distant member of the CRP family of proteins. TLP has two isomers (TLP-A and TLP-B) and sharing approximately 30% with each of the three other CRPs. Like CRP1, CRP2 and CRP3/MLP, TLP has two LIM domains, connected by a flexible linker region. Unlike the CRPs, TLP lacks the nuclear targeting signal (K/R-K/R-Y-G-P-K) and is localized solely in the cytoplasm. TLP is specifically expressed in the thymus in a subset of cortical epithelial cells. TLP has a role in development of normal thymus and in controlling the development and differentiation of thymic epithelial cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CPRCDKTVYFAEKVSSLGKNWHRFCLKCERCSKILSPGGHAEHDGKPYCHKPCY
>gnl|CDD|188861 cd09477, LIM2_TLP, The second LIM domain of thymus LIM protein (TLP). The second LIM domain of thymus LIM protein (TLP): TLP is the distant member of the CRP family of proteins. TLP has two isomers (TLP-A and TLP-B) and sharing approximately 30% with each of the three other CRPs. Like CRP1, CRP2 and CRP3/MLP, TLP has two LIM domains, connected by a flexible linker region. Unlike the CRPs, TLP lacks the nuclear targeting signal (K/R-K/R-Y-G-P-K) and is localized solely in the cytoplasm. TLP is specifically expressed in the thymus in a subset of cortical epithelial cells. TLP has a role in development of normal thymus and in controlling the development and differentiation of thymic epithelial cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CPGCGKPVYFAEKVMSLGRNWHRPCLRCQRCKKTLTAGGHAEHDGSPYCHVPCY
>gnl|CDD|188862 cd09478, LIM_CRIP, The LIM domain of Cysteine-Rich Intestinal Protein (CRIP). The LIM domain of Cysteine-Rich Intestinal Protein (CRIP): CRIP is a short protein with only one LIM domain. CRIP gene is developmentally regulated and can be induced by glucocorticoid hormones during the first three postnatal weeks. The domain shows close sequence homology to LIM domain of thymus LIM protein. However, unlike the TLP proteins which have two LIM domains, the members of this family have only one LIM domain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CPKCDKEVYFAERVTSLGKDWHRPCLKCEKCGKTLTPGSHAEHDGKPYCNHPCY
>gnl|CDD|188863 cd09479, LIM1_CRP1, The first LIM domain of Cysteine Rich Protein 1 (CRP1). The first LIM domain of Cysteine Rich Protein 1 (CRP1): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to a short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP and TLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. CRP1 can associate with the actin cytoskeleton and are capable of interacting with alpha-actinin and zyxin. CRP1 was shown to regulate actin filament bundling by interaction with alpha-actinin and direct binding to actin filaments. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
KKCGVCQKTVYFAEEVQCEGRSFHKSCFLCMVCKKNLDSTTVAVHGEEIYCKSCYG
>gnl|CDD|188864 cd09480, LIM1_CRP2, The first LIM domain of Cysteine Rich Protein 2 (CRP2). The first LIM domain of Cysteine Rich Protein 2 (CRP2): The CRP family members include CRP1, CRP2, CRP3/MLP and TLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. CRP2 specifically binds to protein inhibitor of activated STAT-1 (PIAS1) and a novel human protein designed CRP2BP (for CRP2 binding partner). PIAS1 specifically inhibits the STAT-1 pathway and CRP2BP is homologous to members of the histone acetyltransferase family raising the possibility that CRP2 is a modulator of cytokine-controlled pathways or is functionally active in the transcriptional regulatory network. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
KCGACGRTVYHAEEVQCDGRSFHKCCFLCMVCRKNLDSTTVAIHDQEIYCKSCYG
>gnl|CDD|188865 cd09481, LIM1_CRP3, The first LIM domain of Cysteine Rich Protein 3 (CRP3/MLP). The first LIM domain of Cysteine Rich Protein 3 (CRP3/MLP): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP and TLPCRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network.CRP3 also called Muscle LIM Protein (MLP), which is a striated muscle-specific factor that enhances myogenic differentiation. CRP3/MLP interacts with cytoskeletal protein beta-spectrin. CRP3/MLP also interacts with the basic helix-loop-helix myogenic transcriptio n factors MyoD, myogenin, and MRF4 thereby increasing their affinity for specific DNA regulatory elements. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
KCGACEKTVYHAEEIQCNGRSFHKTCFICMACRKALDSTTVAAHESEIYCKTCY
>gnl|CDD|188866 cd09482, LIM2_CRP3, The second LIM domain of Cysteine Rich Protein 3 (CRP3/MLP). The second LIM domain of Cysteine Rich Protein 3 (CRP3/MLP): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP and TLPCRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network.CRP3 also called Muscle LIM Protein (MLP), which is a striated muscle-specific factor that enhances myogenic differentiation. The second LIM domain of CRP3/MLP interacts with cytoskeletal protein beta-spectrin. CRP3/MLP also interacts with the basic helix-loop-helix myogenic transcription factors MyoD, myogenin, and MRF4 thereby increasing their affinity for specific DNA regulatory elements. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CPRCGKSVYAAEKVMGGGKPWHKTCFRCAICGKSLESTTVTDKDGELYCKVCYA
>gnl|CDD|188867 cd09483, LIM1_Prickle_1, The first LIM domain of Prickle 1. The first LIM domain of Prickle 1. Prickle contains three C-terminal LIM domains and a N-terminal PET domain Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). PCP establishment requires the conserved Frizzled/Dishevelled PCP pathway. Prickle interacts with Dishevelled, thereby modulating Frizzled/Dishevelled activity and PCP signaling. Four forms of prickles have been identified: prickle 1-4. The best characterized is prickle 1 and prickle 2 which are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in mainly expressed in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. In addition, Prickle 1 regulates cell movements during gastrulation and neuronal migration through interaction with the noncanonical Wnt11/Wnt5 pathway in zebrafish. Mutations in prickle 1 have been linked to progressive myoclonus epilepsy. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CEQCGIKINGGEVAVFASRAGPGVCWHPSCFVCFTCNELLVDLIYFYQDGKIHCGRHHA
>gnl|CDD|188868 cd09484, LIM1_Prickle_2, The first LIM domain of Prickle 2. The first LIM domain of Prickle 2: Prickle contains three C-terminal LIM domains and a N-terminal PET domain. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). PCP establishment requires the conserved Frizzled/Dishevelled PCP pathway. Prickle interacts with Dishevelled, thereby modulating Frizzled/Dishevelled activity and PCP signaling. Four forms of prickles have been identified: prickle 1-4. The best characterized is prickle 1 and prickle 2 which are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. Mutations in prickle 1 have been linked to progressive myoclonus epilepsy. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CEQCGGQINGGDIAVFASRAGHGVCWHPQCFVCSVCNELLVDLIYFYQDGKIYCGRHHA
>gnl|CDD|188869 cd09485, LIM_Eplin_alpha_beta, The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin). The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin): Epithelial Protein Lost in Neoplasm is a cytoskeleton-associated tumor suppressor whose expression inversely correlates with cell growth, motility, invasion and cancer mortality. Eplin interacts and stabilizes F-actin filaments and stress fibers, which correlates with its ability to suppress anchorage independent growth. In epithelial cells, Eplin is required for formation of the F-actin adhesion belt by binding to the E-cadherin-catenin complex through alpha-catenin. Eplin is expressed in two isoforms, a longer Eplin-beta and a shorter Eplin-alpha. Eplin-alpha mRNA is detected in various tissues and cell lines, but is absent or down regulated in cancer cells. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CVSCQKTVYPLERLVANQQIYHNSCFRCSYCNTKLSLGTYASLHGNIYCKPHF
>gnl|CDD|188870 cd09486, LIM_Eplin_like_1, a LIM domain subfamily on a group of proteins with unknown function. This model represents a LIM domain subfamily of Eplin-like family. This family shows highest homology to the LIM domains on Eplin and XIRP2 protein families. Epithelial Protein Lost in Neoplasm is a cytoskeleton-associated tumor suppressor whose expression inversely correlates with cell growth, motility, invasion and cancer mortality. Xirp2 is expressed in muscles and is an important effector of the Ang II signaling pathway in the heart. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein
CSSCQKTVYPMERLVADKLVFHNSCFCCKHCNAKLSLGSYAALHGEFYCKPHF
>gnl|CDD|188886 cd09487, SAM_superfamily, SAM (Sterile alpha motif). SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases
DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR
>gnl|CDD|188887 cd09488, SAM_EPH-R, SAM domain of EPH family of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy
AFRSVGEWLESIKMGRYKENFTAAGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL
>gnl|CDD|188888 cd09489, SAM_Smaug-like, SAM (Sterile alpha motif). SAM (sterile alpha motif) domain of Smaug-like subfamily proteins is an RNA binding domain. SAM interacts with stem-loop structures in target mRNAs. Proteins of this subfamily are post-transcriptional regulators involved in mRNA silencing and deadenylation; they can be implicated in transcript stability regulation and vacuolar protein transport as well. SAM_Smaug-like domain-containing proteins are found in metazoa from yeast to human. In animals they are active during early embryogenesis
GIPMWLKSLRLHKYSDAFKGTTWEELLYLTEETLEKKGVLTLGARRKLLKAFGIVKE
>gnl|CDD|188889 cd09490, SAM_Arap1,2,3, SAM domain of Arap1,2,3 (angiotensin receptor-associated protein). SAM (sterile alpha motif) domain of Arap1,2,3 subfamily proteins (angiotensin receptor-associated) is a protein-protein interaction domain. Arap1,2,3 proteins are phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating proteins. They are involved in phosphatidylinositol-3 kinase (PI3K) signaling pathways. In addition to SAM domain, Arap1,2,3 proteins contain ArfGap, PH-like, RhoGAP and UBQ domains. SAM domain of Arap3 protein was shown to interact with SAM domain of Ship2 phosphatidylinositol-trisphosphate phosphatase proteins. Such interaction apparently plays a role in inhibition of PI3K regulated pathways since Ship2 converts PI(3,4,5)P3 into PI(3,4)P2. Proteins of this subfamily participate in regulation of signaling and trafficking associated with a number of different receptors (including EGFR, TRAIL-R1/DR4, TRAIL-R2/DR5) in normal and cancer cells; they are involved in regulation of actin cytoskeleton remodeling, cell spreading and formation of lamellipodia
EADLDIAEWLASIHLEQYLDLFREHGYVTATDCQGINDSRLKQIGISPTGHRRRILKQLPIIT
>gnl|CDD|188890 cd09491, SAM_Ship2, SAM domain of Ship2 lipid phosphatase proteins. SAM (sterile alpha motif) domain of Ship2 subfamily is a protein-protein interaction domain. Ship2 proteins are lipid phosphatases (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2) containing an N-terminal SH2 domain, a central phosphatase domain and a C-terminal SAM domain. Ship2 is involved in a number of PI3K signaling pathways. For example, it plays a role in regulation of the actin cytoskeleton remodeling, in insulin signaling pathways, and in EphA2 receptor endocytosis. SAM domain of Ship2 can interact with SAM domain of other proteins in these pathways, thus participating in signal transduction. In particular, SAM of Ship2 is known to form heterodimers with SAM domain of Eph-A2 receptor tyrosine kinase during receptor endocytosis as well as with SAM domain of PI3K effector protein Arap3 in the actin cytoskeleton signaling network. Since Ship2 plays a role in negatively regulating insulin signaling, it has been suggested that inhibition of its expression or function may contribute in treating type 2 diabetes and obesity-induced insulin resistance
SLSWPKTVSEWLMNLGLQQYEEGLMHNGWDSLEFLSDITEEDLEEAGVTNPAHKRRLLDSLQD
>gnl|CDD|188891 cd09492, SAM_SASH1_repeat2, SAM domain of SASH1 proteins, repeat 2. SAM (sterile alpha motif) repeat 2 of SASH1 proteins is a protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. SASH1 can bind 14-3-3 proteins in response to IGF1/phosphatidylinositol 3-kinase signaling. SASH1 was found upregulated in different tissues including thymus, placenta, lungs and downregulated in some breast tumors, liver metastases and colon cancers if compare to corresponding normal tissues. SASH1 is a potential candidate for a tumor suppressor gene in breast cancers. At the same time, downregulation of SASH1 in colon cancer is associated with metastasis and a poor prognosis
PVSPGHVSSVSDWLVSIGLPMYSPPLLEAGFSTLSRVSSLSETCLREAGITEERHIRKLLSAARLVSAEQ
>gnl|CDD|188892 cd09493, SAM_SASH-like, SAM (Sterile alpha motif), SASH1-like. SAM (sterile alpha motif) domain of SASH1-like proteins is a protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. Proteins of this subfamily are known to be involved in preventing DN thymocytes from premature initiation of programmed cell death and in B cells activation and differentiation. They have been found downregulated in some breast tumors, liver metastases and colon cancers if compare to corresponding normal tissues
KPKTVEELLERINLQEHTSTLLLNGYETLEDFKDLKESHLNELNITDPEHRAKLLTAAEL
>gnl|CDD|188893 cd09494, SAM_liprin-kazrin_repeat1, SAM domain of liprin/kazrin proteins repeat 1. SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization
RVCAWLEDFGLMPMYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE
>gnl|CDD|188894 cd09495, SAM_liprin-kazrin_repeat2, SAM domain of liprin/kazrin proteins repeat 2. SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization
WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH
>gnl|CDD|188895 cd09496, SAM_liprin-kazrin_repeat3, SAM domain of liprin/kazrin proteins repeat 3. SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization
RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN
>gnl|CDD|188896 cd09497, SAM_caskin1,2_repeat1, SAM domain of caskin protein repeat 1. SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression
NPDAEAIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQIPD
>gnl|CDD|188897 cd09498, SAM_caskin1,2_repeat2, SAM domain of caskin protein repeat 2. SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression
WLPDYPPNDLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLKDLQ
K
>gnl|CDD|188898 cd09499, SAM_AIDA1AB-like_repeat1, SAM domain of AIDA1AB-like proteins, repeat 1. SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions
VVQSVGQWLESIGLPQYESKLLLNGFDDVDFLGSGVMEDQDLKEIGITDEQHRQIILQAARSLPKKK
>gnl|CDD|188899 cd09500, SAM_AIDA1AB-like_repeat2, SAM domain of AIDA1AB-like proteins, repeat 2. SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions
DGNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRIWEVELTNVLEINKLGHRKRILASLADR
>gnl|CDD|188900 cd09501, SAM_SARM1-like_repeat1, SAM domain ot SARM1-like proteins, repeat 1. SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver
VPLWSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRFLRELVELKTSA
>gnl|CDD|188901 cd09502, SAM_SARM1-like_repeat2, SAM domain of SARM1-like, repeat 2. SAM (sterile alpha motif) domain repeat 2 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver
DYSSCDTTNLHNWLQSLGPEYSQYTYQMLNAGIDRNSLPSLTEDQLLEDCGITNGIHRLRILNAIKGMEH
>gnl|CDD|188902 cd09503, SAM_tumor-p63,p73, SAM domain of tumor-p63,p73 proteins. SAM (sterile alpha motif) domain of p63, p73 transcriptional factors is a putative protein-protein interaction domain and lipid-binding domain. p63 and p73 are homologs to the tumor suppressor p53. They have a C-terminal SAM domain in their longest spliced alpha forms, while p53 doesn't have it. p63 or p73 knockout mice show significant developmental abnormalities but no increased cancer susceptibility, suggesting that p63 and p73 play a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for p63/p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain
YPTDNSVASWLTKLGCSNYIDNFHQQGLLSIFQLDEFTLEDLAAMKIPEQHRNKIWKGLLEYRQA
>gnl|CDD|188903 cd09504, SAM_STIM-1,2-like, SAM domain of STIM-1,2-like proteins. SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane
EVHNWTVEDTVEWLVNSVELPQYVEAFKENGVDGSALPRLAVNNPSFLTSVLGIKDPIHRQKLSLKAMDV
VLFG
>gnl|CDD|188904 cd09505, SAM_WDSUB1, SAM domain of WDSUB1 proteins. SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding
SLQDWSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEELKMKS
DS
>gnl|CDD|188905 cd09506, SAM_Shank1,2,3, SAM domain of Shank1,2,3 family proteins. SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen
PVHEWTVDDVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKLL
>gnl|CDD|188906 cd09507, SAM_DGK-delta-eta, SAM domain of diacylglycerol kinase delta and eta subunits. SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization
PVTNWTTEEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITKVGHVKRILQAIKDL
>gnl|CDD|188907 cd09508, SAM_HD, SAM domain of HD-phosphohydrolase. SAM (sterile alpha motif) domain of SAM_HD subfamily proteins is a putative protein-protein interaction domain. Proteins of this group, additionally to the SAM domain, contain a HD hydrolase domain. Human SAM-HD1 is a nuclear protein involved in innate immune response and may act as a negative regulator of the cell-intrinsic antiviral response. Mutations in this gene lead to Aicardi-Goutieres syndrome (symptoms include cerebral atrophy, leukoencephalopathy, hepatosplenomegaly, and increased production of alpha-interferon)
DFRSWDPEDVCQFLRGNGFGEPELLEIFRENEITGAHLPDLTESRLEKLGVSSLGERLKLLKCLQKLSQI
>gnl|CDD|188908 cd09509, SAM_Polycomb, SAM domain of Polycomb group. SAM (sterile alpha motif) domain of Polycomb group is a protein-protein interaction domain. The Polycomb group includes transcriptional repressors which are involved in the regulation of some key regulatory genes during development in many organisms. They are best known for silencing Hox (Homeobox) genes. Polycomb proteins work together in large multimeric and chromatin-associated complexes. They organize chromatin of the target genes and maintain repressed states during many cell divisions. Polycomb proteins are classified based on their common function, but not on conserved domains and/or motifs; however many Polycomb proteins (members of PRC1 class complex) contain SAM domains which are more similar to each other inside of the Polycomb group than to SAM domains outside of it. Most information about structure and function of Polycomb SAM domains comes from studies of Ph (Polyhomeotic) and Scm (Sex comb on midleg) proteins. Polycomb SAM domains usually can be found at the C-terminus of the proteins. Some members of this group contain, in addition to the SAM domain, MTB repeats, Zn finger, and/or DUF3588 domains. Polycomb SAM domains can form homo- and/or heterooligomers through ML and EH surfaces. SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Polycomb proteins are known to be highly expressed in some cells years before their cancer pathology; thus they are attractive markers for early cancer therapy
PSKWSVDDVAQFIKSLDGCAEYAEVFREQEIDGQALLLLTEDDLLKGMGLKLGPALKIYNHIVK
>gnl|CDD|188909 cd09510, SAM_aveugle-like, SAM domain of aveugle-like subfamily. SAM (sterile alpha motif) domain of SAM_aveugle-like subfamily is a protein-protein interaction domain. In Drosophila, the aveugle (AVE) protein (also known as HYP (Hyphen)) is involved in normal photoreceptor differentiation, and required for epidermal growth factor receptor (EGFR) signaling between ras and raf genes during eye development and wing vein formation. SAM domain of the HYP(AVE) protein interacts with SAM domain of CNK, the multidomain scaffold protein connector enhancer of kinase suppressor of ras. CNK/HYP(AVE) complex interacts with KSR (kinase suppressor of Ras) protein. This interaction leads to stimulation of Ras-dependent Raf activation. This subfamily also includes vertebrate AVE homologs - Samd10 and Samd12 proteins. Their exact function is unknown, but they may play a role in signal transduction during embryogenesis
KPVYLWSVQDVCKWLKRHCPDYYLLYAELFLQHDITGRALLRLNDNKLERMGITDEDHRQDILREILKLR
LKTEI
>gnl|CDD|188910 cd09511, SAM_CNK1,2,3-suppressor, SAM domain of CNK1,2,3-suppressor subfamily. SAM (sterile alpha motif) domain of CNK (connector enhancer of kinase suppressor of ras (Ksr)) subfamily is a protein-protein interaction domain. CNK proteins are multidomain scaffold proteins containing a few protein-protein interaction domains and are required for connecting Rho and Ras signaling pathways. In Drosophila, the SAM domain of CNK is known to interact with the SAM domain of the aveugle protein, forming a heterodimer. Mutation of the SAM domain in human CNK1 abolishes the ability to cooperate with the Ras effector, supporting the idea that this interaction is necessary for proper Ras signal transduction
VAKWSPKQVTDWLKGLDDCLQQYIYTFEREKVTGEQLLNLSPQDLENLGVTKIGHQELILEAVELLCAL
>gnl|CDD|188911 cd09512, SAM_Neurabin-like, SAM domain of SAM_Neurabin-like subfamily. SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions
SRPVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSSKLKALGITSSSDRSLLKKKLKELKAQ
>gnl|CDD|188912 cd09513, SAM_BAR, SAM domain of BAR subfamily. SAM (sterile alpha motif) domain of BAR (Bifunctional Apoptosis Regulator) subfamily is a protein-protein interaction domain. In addition to the SAM domain, this type of regulator has a RING finger domain. Proteins of this subfamily are involved in the apoptosis signal network. Their overexpression in human neuronal cells significantly protects cells from a broad range of cell death stimuli. SAM domain can interact with Caspase8, Bcl-2 and Bcl-X resulting in suppression of Bax-induced cell death
VSKWTPEEVVLWLEQLGPWASLYRERFLSENVNGRLLLTLTEEELSKPPFNIENSLHRRAILTELERVKT
L
>gnl|CDD|188913 cd09514, SAM_SGMS1, SAM domain of sphingomyelin synthase. SAM (sterile alpha motif) domain of SGMS-1 (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. Sphingomyelin synthase 1 is a transmembrane protein with a SAM domain at the N-terminus and a catalytic domain at the C-terminus. Sphingomyelin synthase 1 is a Golgi-associated enzyme, and depending on the concentration of diacylglycerol and ceramide, can catalyze synthesis phosphocholine or sphingomyelin, respectively. It plays a central role in sphingolipid and glycerophospholipid metabolism
MKEVVQWSPKEVSDWLSEEGMQEYSEALRSFDGQALLNLTEEDFKKTPLSLVSSDSGRQLLEMIETLKIE
HH
>gnl|CDD|188914 cd09515, SAM_SGMS1-like, SAM domain of sphingomyelin synthase related subfamily. SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism
VHEWTCEDVAKWLKKEGFSKYVDLLCNKHRIDGKVLLSLTEEDLRSPPLEIKVLGDIKRLWLAIRKLQRQ
>gnl|CDD|188915 cd09516, SAM_sec23ip-like, SAM domain of sec23ip-like subfamily. SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 interacting protein) subfamily is a potential protein-protein interaction domain. This group of proteins includes Sec23ip and DDHD2 proteins. All of them contain at least two domains: a SAM domain and a predicted metal-binding domain. For mammalian DDHD2 members of this group, phospholipase activity has been demonstrated. Sec23ip proteins of this group interact with Sec23 proteins via an N-terminal proline-rich region. Members of this subfamily are involved in organization of ER/Golgi intermediate compartment
NSVEEQEEPLTLEEDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGIPMGPRKKLLGFLKDQKAK
>gnl|CDD|188916 cd09517, SAM_USH1G_HARP, SAM domain of USH1G_HARP family. SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans
ETSPLERFLTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPLGPRRKLLNAIAKRKQALENP
>gnl|CDD|188917 cd09518, SAM_ANKS6, SAM domain of ANKS6 (or SamCystin) subfamily. SAM (sterile alpha motif) domain of ANKS6 (or SamCystin) subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. They are able to form self-associated complexes and both (SAM and ANK) domains play a role in such interactions. Mutations in Anks6 gene are associated with polycystic kidney disease. They cause formation of renal cysts in rodent models. It was suggested that the ANKS6 protein can interact indirectly (through RNA and protein intermediates) with BICC1, another polycystic kidney disease-associated protein
TITEEDELSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISELNA
>gnl|CDD|188918 cd09519, SAM_ANKS3, SAM domain of ANKS3 subfamily. SAM (sterile alpha motif) domain of ANKS3 subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. SAM is a widespread domain in signaling proteins. In many cases it mediates homo-dimerization/oligomerization
YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS
>gnl|CDD|188919 cd09520, SAM_BICC1, SAM domain of BICC1 (bicaudal) subfamily. SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates
SAKYSDLPELLAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKMLLAISELNKR
>gnl|CDD|188920 cd09521, SAM_ASZ1, SAM domain of ASZ1 subfamily. SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state
SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPGDQKKILDAIKEVH
>gnl|CDD|188921 cd09522, SAM_SLP76, SAM domain of SLP76 subfamily. SAM (sterile alpha motif) domain of SLP76 (SH2 domain-containing leukocyte protein 76), also known as LCP2 (Lymphocyte cytosolic protein), subfamily is a protein-protein interaction domain. Proteins of this group have an N-terminal SAM domain, 3 phosphotyrosine motifs, a proline-rich region and a C-terminal SH2 domain. They are scaffold proteins involved in protein complex formation. The complexes play a role in T-cell receptor mediated signaling pathways such as integrin activation, cytoskeletal organization, MARK activation, and calcium flux. SAM domain deleted SLP76 knockin mice show a number of defects, including partially blocked thymocyte development, impaired positive and negative thymic selection and changes in T-cell receptor mediated signaling
SEVMGWNPHSLADYFKKLNLKGCDKVVKKSNINGQRFLNMTENDIQKFPKLHVPFISKICQEINKNEER
>gnl|CDD|188922 cd09523, SAM_TAL, SAM domain of TAL subfamily. SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) proteins, also known as LRSAM1 (Leucine-rich repeat and sterile alpha motif-containing) proteins, is a putative protein-protein interaction domain. Proteins of this subfamily participate in the regulation of retrovirus budding and receptor endocytosis. They show E3 ubiquitin ligase activity. Human TAL protein interacts with Tsg101 and TAL's C-terminal ring finger domain is essential for the multiple monoubiquitylation of Tsg101
EAGVDPQLVNLLNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQELLL
>gnl|CDD|188923 cd09524, SAM_tankyrase1,2, SAM domain of tankyrase1,2 subfamily. SAM (sterile alpha motif) domain of Tankyrase1,2 subfamily is a protein-protein interaction domain. In addition to the SAM domain, proteins of this group have ankyrin repeats and a ADP- ribosyltransferase (poly-(ADP-ribose) synthase) domain. Tankyrases can polymerize through their SAM domains forming homoligomers and these complexes are disrupted by autoribosylation. Tankyrases apparently act as master scaffolding proteins and thus may interact simultaneously with multiple proteins, in particular with TRF1, NuMA, IRAP and Grb14 (ankyrin repeats are involved in these interactions). Tankyrases participate in a variety of cell signaling pathways as effector molecules. Their functions are different depending on the intracellular location: at telomeres they play a role in the regulation of telomere length via control of telomerase access to telomeres, at centrosomes they promote spindle assembly/disassembly, in Golgi vesicles they participate in the regulation of vesicle trafficking and Golgi dynamics. Tankyrase 1 may be of interest as new potential target for telomerase-directed cancer therapy
VNGTDFSISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLISG
>gnl|CDD|188924 cd09525, SAM_GAREM, SAM domain of GAREM subfamily. SAM (sterile alpha motif) domain of GAREM (Grb2-associated and regulator of Erk/MARK) protein subfamily (also known as FAM59A) is a putative protein-protein interaction domain. SAM domain is a widespread domain in signaling proteins. Proteins of this group have SAM at the C-terminus. Human GAREM protein is known to play a role in regulation of the EGF (Epidermal Growth Factor) receptor and of Gab or insulin preceptor substrate-1 family proteins. Grb2 (Growth factor receptor-bound) protein was identified as a binding partner of human GAREM. Proline-rich motifs and phosphorylation of two conserved tyrosines in GAREM are important for the interaction with the SH3 domains of Grb2 protein; however these motifs and residues do not belong to the SAM domain
LSGLSIEEVSKSLRFIGLSEDVVSFFVTEKIDGNLLVQLTEEILSEDFKLSKLQVKKIMQFINGWRP
>gnl|CDD|188925 cd09526, SAM_Samd3, SAM domain of Samd3 subfamily. SAM (sterile alpha motif) domain of the Samd3 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. Exact function of proteins belonging to this subfamily is unknown
METWSVEQVCNWLVEKNLGELVPRFQEEEVSGAALLALNDRMVQQLVKKIGHQAVLMDLIKKYKQQ
>gnl|CDD|188926 cd09527, SAM_Samd5, SAM domain of Samd5 subfamily. SAM (sterile alpha motif) domain of Samd5 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown
CSNIVYDWLRTLQLEQYAEKFVDNGYDDLEVCKQIGDPDLDAIGVMNPAHRKRILEAVRRLKE
>gnl|CDD|188927 cd09528, SAM_Samd9_Samd9L, SAM domain of Samd9/Samd9L subfamily. SAM (sterile alpha motif) domain of Samd9/Samd9L subfamily is a putative protein-protein interaction domain. SAM is a widespread domain in signaling proteins. Samd9 is a tumor suppressor gene. It is involved in death signaling of malignant glioblastoma. Samd9 suppression blocks cancer cell death induced by HVJ-E or IFN-beta treatment. Deleterious mutations in Samd9 lead to normophosphatemic familial tumoral calcinosis, a cutaneous disorder characterized by cutaneous calcification or ossification
DDWTKEHVKQWLIEDLIDKKYAEILYEEEVTGAVLKELTEEDLVDMGLPHGPALLIIHSFNELN
>gnl|CDD|188928 cd09529, SAM_MLTK, SAM domain of MLTK subfamily. SAM (sterile alpha motif) domain of MLTK subfamily is a protein-protein interaction domain. Besides SAM domain, these proteins have N-terminal protein tyrosine kinase domain and leucine-zipper motif. Proteins of this group act as mitogen-activated protein triple kinase in a number of MAPK cascades. They can be activated by autophosphorylation in response to stress signals. MLTK-alpha is known to phosphorylate histone H3. In mammals, MLTKs participate in the activation of the JNK/SAPK, p38, ERK5 pathways, the transcriptional factor NF-kB, in the regulation of the cell cycle checkpoint, and in the induction of apoptosis in a hepatoma cell line. Some members of this subfamily are proto-oncogenes, thus MLTK-alpha is involved in neoplasmic cell transformation and/or skin cancer development in athymic nude mice. Based on in vivo coprecipitation experiments in mammalian cells, it has been demonstrated that MLTK proteins might form homodimers/oligomers via their SAM domains
AWTEEDVHFWMQQLVRKGGHPSELSQYADLFKENHITGKRLLLLTEEDLRDMGIGSKGHIIHLKSAIEKL
T
>gnl|CDD|188929 cd09530, SAM_Samd14, SAM domain of Samd14 subfamily. SAM (sterile alpha motif) domain of SamD14 (or FAM15A) subfamily is a putative protein-protein interaction domain. SAM is widespread domain in proteins involved in signal transduction and regulation. In many cases SAM mediates homodimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown
LSWDTEDVAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIRELLGIE
>gnl|CDD|188930 cd09531, SAM_CS047, SAM domain of CS047 subfamily. SAM (sterile alpha motif) domain of CS047 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates homodimerization/oligomerization. The exact function of proteins belonging to this group is unknown
TSEWIKFFKDAGIPSGLAAKYAVIFVENRIQKEMLLDLNKEILKEMGITVMGDIIAILKHAKKVH
>gnl|CDD|188931 cd09532, SAM_SLA1_fungal, SAM domain of SLA1 subfamily. SAM (sterile alpha motif) domain of fungal SLA1 proteins is a protein-protein interaction domain. Proteins of this group consist of a few N-terminal SH3 domains followed by SHD1 domain, SAM domain (also known as SHD2) and multiple C-terminal repeats. The yeast SLA1 protein is an endocytic clathrin adaptor. It is associated with a variety of endocytic accessory factors and required for endocytic vesicle formation and for clathrin and actin-dependent cargo recognition. SLA1 binds clathrin through a variant clathrin-binding motif (vCB). The SAM domain negatively regulates this binding by blocking the vCB site. The SAM domains of SLA1 proteins can form oligomers via their mid-loop (ML) and end-helix (EH) regions. Such self-associations apparently are important for SLA1 function. A proposed regulatory model suggests that SAM can be considered a mediator of two aspects of clathrin adaptor function. It plays a role in negative regulation of clathrin binding via an intramolecular interaction with the vCB, and a role in positive regulation of vesicle coat assembly via self-oligomerization
YDWFEFFLNCGVDVSLCQRYASNFERDQMDESVLPDINPSTLRTLGLREGDIIRVMKFLDKK
>gnl|CDD|188932 cd09533, SAM_Ste50-like_fungal, SAM domain of Ste50_like (ubc2) subfamily. SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity
DVADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVYELK
>gnl|CDD|188933 cd09534, SAM_Ste11_fungal, SAM domain of Ste11_fungal subfamily. SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator
WDEEFVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSLR
>gnl|CDD|188934 cd09535, SAM_BOI-like_fungal, SAM domain of BOI-like fungal subfamily. SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation)
RSWSPEQVAEWLLSAGFDDSVCEKFRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEIKSLR
>gnl|CDD|188935 cd09536, SAM_Ste50_fungal, SAM domain of Ste50 fungal subfamily. SAM (sterile alpha motif) domain of Ste50 fungal subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and Ras-associated UBQ superfamily domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response, and contribute to cell wall integrity in vegetative cells. Ste50 of S.cerevisiae acts as an adaptor protein between G protein and MAP triple kinase Ste11. Ste50 proteins are able to form homooligomers, binding each other via their SAM domains, as well as heterodimers and heterogeneous complexes with SAM domain or SAM homodimers of MAPKKK Ste11 protein kinase
EEFNEWSTDEVVKWCISSLGLDDGDPLCDRLRENNITGSLLSELTLEDCKELCDNDLSLAIRLKLLINKL
RDSK
>gnl|CDD|188936 cd09537, SAM_CP2-like, SAM domain of CP2-like transcription factors. SAM (sterile alpha motif) domain of CP2-like transcription factor is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and some also have a C-terminal dimerization domain. CP2-like family of transcriptional factors includes three subgroups: LBP1, TFCP2, and LBP9. Members of this family are involved in transcriptional regulation from early development to terminal differentiation. They play a role in regulation of expression of P450scc (the cholesterol side-chain cleavage enzyme, cytochrome) in placenta, and alpha-globin in erythroid cells. They are required for proper maturation of the dust (epithelial component of tubular organs) of kidney and salivary gland. Human LBP1 is known to be induced by HIV type I infection in lymphocytes; it represses HIV transcription by preventing the binding of TFIID to the virus promoter. Additionally, it has been suggested that UBP1 (LBP1) regulator might be a member of a blood pressure controlling network. LBP1 protein isoforms are able to form dimers apparently via SAM domain since SAM deletion or mutation resulted in a loss of this ability
SPQQTTQWLRKNRFGAYLRTFSNFSGADLLRLTRDDLIQICGLADGIRLFNALHSRAIRPRLTLYVC
>gnl|CDD|188937 cd09538, SAM_DLC1,2-like, SAM domain of DLC1,2-like subfamily. SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted in liver cancer) subfamily is a protein-protein interaction domain located at the N-terminus of the protein. Members of this subfamily do not form dimers/oligomers through their SAM domains. They participate in regulation of cell migration and lipid transfer. SAM domain of human DLC1 protein contains the EF1A1 (eukaryotic elongation factor) binding motif, thus SAM facilitates recruitment of EF1A1 to the membrane periphery and suppresses cell migration. Human Dlc2 gene is known as a tumor suppressor gene. It was found underexpressed in hepatocellular carcinoma
KEACKWLRAAGFPQYAQLYEDSQFPIDISAVKRDHDFLDRDSLQALIRRLNTLNKCASMK
>gnl|CDD|188938 cd09539, SAM_TNK-like, SAM domain of TNK(ACK)-like non-receptor tyrosine-protein kinases. SAM (sterile alpha motif) domain of TNK-like subfamily is a putative protein-protein interaction domain. This subfamily includes TNK1 and TNK2 (also known as ACK1) non-receptor tyrosine-protein kinases. They contain a SAM domain at the N-terminus followed by a catalytic domain and a few other domains. Members of this group are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Deletion of the SAM domain resulted in reduction of Ack1 ability to undergo autophosphorylation and dramatically reduces ubiquitination of Ack1 catalyzed by HECT E3 ubiquitin ligase (Nedd4-1) during EGF-induced Ack1 degradation. It has been suggested that the lysine-rich region in SAM domain might be a major ubiquitination site. Members of this group are also associated with some cancers. Amplification of the Ack1 gene correlates with prostate and lung cancer progression, and Ack1 overexpression increases invasiveness. Oncogenecity of Tnk1 gene apparently depends on cell context; it may play a role in tumor suppression since Tnk1 knockout mice can develop spontaneous tumors
GTDWLYEFLREAQLQQFYSRIRDDLKVTRLSHFKYVKEEDLEKIGMSKPEQRRLREAVKKYK
>gnl|CDD|188939 cd09540, SAM_EPS8-like, SAM domain of EPS8-like subfamily. SAM (sterile alpha motif) domain of EPS8-like subfamily is a putative protein-protein interaction domain. This subfamily includes epidermal growth factor receptor kinase substrate 8 proteins (EPS8) and epidermal growth factor receptor kinase substrate 8-like (EPSL8) 1, 2, 3 proteins with the SAM domain located in the C-terminal effector region. This region is responsible for intracellular protein localization and is involved in small GTPases (such as Rac and Rab5) activation/inhibition. Proteins belonging to this group participate in coordination and integration of multiple signaling pathways; in particular, they play a role in the control of actin dynamics and in receptor endocytosis. They can form complexes with other proteins; for example, in the actin signaling network they interact with SOS1 and E3b1 (Abl1) proteins as well as with CRIB (via SH3 domains) during the actin filament formation, and in the receptor endocytosis their partner is RN-tre protein
PLTYDSSPEEVKAWLQAKGFSKITVRSLGVLTGAQLFSLNKEELKTVCPEEGARVYSQLTVQKSAL
>gnl|CDD|188940 cd09541, SAM_KIF24-like, SAM domain of KIF24-like subfamily. SAM (sterile alpha motif) domain of KIF24 subfamily is a putative protein-protein interaction domain. This subfamily includes proteins related to human kinesin-like protein KIF24. SAM domain is located at the N-terminus followed by kinesin motor domain. Kinesins are proteins involved in a number of different cell processes including microtubule dynamics and axonal transport. Kinesins of this group belong to N-type; they drive microtubule plus end-directed transport. SAM apparently plays the role of adaptor or scaffold domain. In many cases SAM is known as a mediator of dimerization/oligomerization
SVLYEWLEEAGLQHYYPAFAAGGVTSIEALAQLTMQDYASLGVQDMEDKQKLFRLIQTLK
>gnl|CDD|188941 cd09542, SAM_EPH-A1, SAM domain of EPH-A1 subfamily of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell
GIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGF
>gnl|CDD|188942 cd09543, SAM_EPH-A2, SAM domain of EPH-A2 family of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-A2 subfamily of receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A2 receptors and appears to mediate cell-cell initiated signal transduction. For example, SAM domain of EPH-A2 receptors interacts with SAM domain of Ship2 proteins (SH2 containing phosphoinositide 5-phosphotase-2) forming heterodimers; such recruitment of Ship2 by EPH-A2 attenuates the positive signal for receptor endocytosis. Eph-A2 is found overexpressed in many types of human cancer, including breast, prostate, lung and colon cancer. High level of expression could induce cancer progression by a variety of mechanisms and could be used as a novel tag for cancer immunotherapy. EPH-A2 receptors are attractive targets for drag design
EGVPFRTVAEWLESIKMQQYTEHFMAAGYNSIDKVLQMTQEDIKHIGVRLPGHQKRIAYSILGLKEQVST
>gnl|CDD|188943 cd09544, SAM_EPH-A3, SAM domain of EPH-A3 subfamily of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-A3 subfamily of receptor tyrosine kinases is a C-terminal putative protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A3 receptors bind SH2/SH3 containing adaptor protein Nck1 and this adaptor is a key factor in EPH-A3 mediated signaling. However SAM domain is not implemented in this interaction. Activation of EPH-A3 receptors inhibits outgrowth and cell migration. Mutations in SAM domain may play a role in development of hepatocellular carcinoma. Expression of EPH-A3 is associated with lymphocytic leukemia and defines the subset of rhabdomyosarcoma tumors. EPH-A3 receptors are attractive targets for drug design
TFHTTGDWLNGARTAHCKEIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIVSSIKTLET
>gnl|CDD|188944 cd09545, SAM_EPH-A4, SAM domain of EPH-A4 subfamily of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-A4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A4 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of EPH-A4 receptors can form homodimers. EPH-A4 receptors bind ligands such as erphirin A1, A4, A5. They are known to interact with a number of different proteins, including meltrin beta metalloprotease, Cdk5, and EFS2alpha, however SAM domain doesn't participate in these interactions. EPH-A4 receptors are involved in regulation of corticospinal tract formation, in pathway controlling voluntary movements, in formation of motor neurons, and in axon guidance (SAM domain is not required for axon guidance or for EPH-A4 kinase signaling). In Xenopus embryos EPH-A4 induces loss of cell adhesion, ventro-lateral protrusions, and severely expanded posterior structures. Mutations in SAM domain conserved tyrosine (Y928F) enhance the ability of EPH-A4 to induce these phenotypes, thus supporting the idea that the SAM domain may negatively regulate some aspects of EPH-A4 activity. EphA4 gene was found overexpressed in a number of different cancers including human gastric cancer, colorectal cancer, and pancreatic ductal adenocarcinoma. It is likely to be a promising molecular target for the cancer therapy
SAVASVDDWLQAIKMERYKDNFTAAGYTTLEAVVHMNQDDLARIGISAIAHQNKILSSVQGMRSQMQQMQ
G
>gnl|CDD|188945 cd09546, SAM_EPH-A5, SAM domain of EPH-A5 subfamily of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-A5 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A5 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A5 gene is almost exclusively expressed in the nervous system. Murine EPH-A5 receptors participate in axon guidance during embryogenesis and play a role in the adult synaptic plasticity, particularly in neuron-target interactions in multiple neural circuits. Additionally EPH-A5 receptors and its ligand ephrin A5 regulate dopaminergic axon outgrowth and influence the formation of the midbrain dopaminergic pathways. EphA5 gene expression was found decreased in a few different breast cancer cell lines, thus it might be a potential molecular marker for breast cancer carcinogenesis and progression
GAYRSVGEWLEAIKMGRYTEIFMENGYSSMDAVAQVTLEDLRRLGVTLVGHQKKIMNSIQEMRVQL
>gnl|CDD|188946 cd09547, SAM_EPH-A6, SAM domain of EPH-A6 subfamily of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers
PLFVTVSDWLDSIKMGQYKNNFMAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLRL
>gnl|CDD|188947 cd09548, SAM_EPH-A7, SAM domain of EPH-A7 subfamily of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-A7 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A7 receptors and appears to mediate cell-cell initiated signal transduction. EphA7 was found expressed in human embryonic stem (ES) cells, neural tissues, kidney vasculature. EphA7 knockout mice show decrease in cortical progenitor cell death at mid-neurogenesis and significant increase in cortical size. EphA7 may be involved in the pathogenesis and development of different cancers; in particular, EphA7 was found upregulated in glioblastoma and downregulated in colorectal cancer and gastric cancer. Thus, it is a potential molecular marker and/or therapy target for these types of cancers
TPDFTSFCSVGEWLEAIKMERYKDNFTAAGYNSLESVARMTIEDVMSLGITLVGHQKKIMSSIQTMRAQM
>gnl|CDD|188948 cd09549, SAM_EPH-A10, SAM domain of EPH-A10 subfamily of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers
FSTFPSFGSVGEWLEALDLCRYKDNFAAAGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQALRAQV
>gnl|CDD|188949 cd09550, SAM_EPH-A8, SAM domain of EPH-A8 subfamily of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-A8 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A8 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A8 receptors are involved in ligand dependent (ephirin A2, A3, A5) regulation of cell adhesion and migration, and in ligand independent regulation of neurite outgrowth in neuronal cells. They perform signaling in kinase dependent and kinase independent manner. EPH-A8 receptors are known to interact with a number of different proteins including PI 3-kinase and AIDA1-like subfamily SAM repeat domain containing proteins. However other domains (not SAM) of EPH-A8 receptors are involved in these interactions
SCLSVDDWLDSIKMGRYKDHFAAGGYSSLGMVMRMNIEDIRRLGITLMGHQKKILTSIQVMRAQL
>gnl|CDD|188950 cd09551, SAM_EPH-B1, SAM domain of EPH-B1 subfamily of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-B1 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH- B1 receptors. In human vascular endothelial cells it appears to mediate cell-cell initiated signal transduction via the binding of the adaptor protein GRB10 (growth factor) through its SH2 domain to a conserved tyrosine that is phosphorylated. EPH-B1 receptors play a role in neurogenesis, in particular in regulation of proliferation and migration of neural progenitors in the hippocampus and in corneal neovascularization; they are involved in converting the crossed retinal projection to ipsilateral retinal projection. They may be potential targets in angiogenesis-related disorders
PDFTAFTSVEDWLSAIKMSQYRDNFLSSGFTSLQLVAQMTSEDLLRIGVTLAGHQKKILNSIQSMRVQ
>gnl|CDD|188951 cd09552, SAM_EPH-B2, SAM domain of EPH-B2 subfamily of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-B2 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B2 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of this subfamily form homodimers/oligomers (in head-to-head/tail-to-tail orientation); apparently such clustering is necessary for signaling. EPH-B2 receptor is involved in regulation of synaptic function; it is needed for normal vestibular function, proper formation of anterior commissure, control of cell positioning, and ordered migration in the intestinal epithelium. EPH-B2 plays a tumor suppressor role in colorectal cancer. It was found to be downregulated in gastric cancer and thus may be a negative biomarker for it
PDYTSFSTVDEWLDAIKMGQYKESFANAGFTSFDVVSQMTMEDILRVGVTLAGHQKKILNSIQVMRAQMN
Q
>gnl|CDD|188952 cd09553, SAM_EPH-B3, SAM domain of EPH-B3 subfamily of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-B3 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B3 receptor protein kinase performs kinase-dependent and kinase-independent functions. It is known to be involved in thymus morphogenesis, in regulation of cell adhesion and migration. Also EphB3 controls cell positioning and ordered migration in the intestinal epithelium and plays a role in the regulation of adult retinal ganglion cell axon plasticity after optic nerve injury. In some experimental models overexpression of EphB3 enhances cell/cell contacts and suppresses colon tumor growth
PDYTTFTTVGDWLDAIKMGRYKENFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMRLQM
>gnl|CDD|188953 cd09554, SAM_EPH-B4, SAM domain of EPH-B4 subfamily of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-B4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B4 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B4 protein kinase performs kinase-dependent and kinase-independent functions. These receptors play a role in the regular vascular system development during embryogenesis. They were found overexpressed in a variety of cancers, including carcinoma of the head and neck, ovarian cancer, bladder cancer, and downregulated in bone myeloma. Thus, EphB4 is a potential biomarker and a target for drug design
SSCGSVGEWLRAIKMERYEDSFLQAGFTTFQLVSQISTEDLLRMGVTLAGHQKKILSSIQAMGIQNK
>gnl|CDD|188954 cd09555, SAM_EPH-B6, SAM domain of EPH-B6 subfamily of tyrosine kinase receptors. SAM (sterile alpha motif) domain of EPH-B6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B6 receptors and appears to mediate cell-cell initiated signal transduction. Receptors of this type are highly expressed in embryo and adult nervous system, in thymus and also in T-cells. They are involved in regulation of cell adhesion and migration. (EPH-B6 receptor is unusual; it fails to show catalytic activity due to alteration in kinase domain). EPH-B6 may be considered as a biomarker in some types of tumors; EPH-B6 activates MAP kinase signaling in lung adenocarcinoma, suppresses metastasis formation in non-small cell lung cancer, and slows invasiveness in some breast cancer cell lines
LDFPCLDSPQAWLSAIGLECYQDNFSKFGLCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQLLQQHL
>gnl|CDD|188955 cd09556, SAM_VTS1_fungal, SAM domain of VTS1 RNA-binding proteins. SAM (sterile alpha motif) domain of VTS1 subfamily proteins is RNA binding domain located in the C-terminal region. SAM interacts with stem-loop structures of mRNA. Proteins of this subfamily participate in regulation of transcript stability and degradation, and also may be involved in vacuolar protein transport regulation. VTS1 protein of S.cerevisiae induces mRNA degradation via the major deadenylation-dependent mRNA decay pathway; VTS1 recruits CCR4/POP2/NOT deadenylase complex to target mRNA. The recruitment is the initial step resulting in poly(A) tail removal transcripts. Potentially SAM domain may be responsible not only for RNA binding but also for deadenylase binding
TDPKLLKDIPAWLRSLRLHKYTDNLKDLSWKELIELDDEDLEDKGVSALGARRKLLKAFEIVREYKERG
>gnl|CDD|188956 cd09557, SAM_Smaug, SAM domain of Smaug subfamily. SAM (sterile alpha motif) domain of Smaug proteins is an RNA recognition domain. It binds a specific RNA motif known as Smaug recognition element (SRE). Among members of this group are invertebrate Smaug (Smg) proteins and vertebrate Smaug1 and Smaug2 proteins. They are involved in post-transcriptional control during early embryogenesis in animals. In Drosophila, Smaug protein is a translational repressor of mRNA of Nanos (Nos) protein. Gradient of Nanos is required for proper abdominal segmentation. SAM domain interacts specifically with the Nanos mRNA regulatory regions. Moreover, Smaug protein is involved in regulation of specific maternal transcripts degradation in Drosophila early embryo via recruitment of the CCR4/POP2/NOT deadenylase
EEGSGMKDVPAWLKSLRLHKYASLFSQMTYEEMLNLTEEQLEAQGVTKGARHKIALSIQKLKE
>gnl|CDD|188957 cd09558, SAM_ZCCH14, SAM domain of ZCCH14 subfamily. SAM (sterile alpha motif) domain of ZCCH14 (Zinc finger CCHC domain 14) protein subfamily (also known as BDG-29 or KIAA0579) is a putative RNA binding domain. Members of this group are believed to be involved in post-translational regulation during early embryogenesis
QTQEQNGILDWLRKLRLHKYYPVFKQLTMEKFLSLTEEDLNKFESLTMGAKKKLKTQLELEKEKS
>gnl|CDD|188958 cd09559, SAM_SASH1_repeat1, SAM domain of SASH1 proteins, repeat 1. SAM (sterile alpha motif) repeat 1 of SASH1 proteins is a predicted protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. SASH1 can bind 14-3-3 proteins in response to IGF1/phosphatidylinositol 3-kinase signaling. SASH1 was found upregulated in different tissues including thymus, placenta, lungs and downregulated in some breast tumors, liver metastases and colon cancers, relative to corresponding normal tissues. SASH1 is a potential candidate for a tumor suppressor gene in breast cancers. At the same time, downregulation of SASH1 in colon cancer is associated with metastasis and a poor prognosis
PQPKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQEYD
>gnl|CDD|188959 cd09560, SAM_SASH3, SAM domain of SASH3 subfamily. SAM (sterile alpha motif) domain of SAHS3 (also known as SLY) proteins is a predicted protein-protein interaction domain. Members of this subfamily are putative signaling/adaptor proteins. In addition to SAM, they contain SLY and SH3 domains. They appear to mediate signal transduction in lymphoid tissues. Murine SASH3 is involved in preventing DN thymocytes from premature initiation of programmed cell death and in mTOR (mammalian target of rapamycin) activation via signal integration of the Notch receptor and preTCR (T cell receptor) pathways
KRPKPKTLHELLERIGLEEHTSTLLLNGYQTLEDFKELRETHLNELNIMDPQHRAKLLTAAELLLDYD
>gnl|CDD|188960 cd09561, SAM_SAMSN1, SAM domain of SAMSN1 subfamily. SAM (sterile alpha motif) domain of SAMSN1 (also known as HACS1 or NASH1) proteins is a predicted protein-protein interaction domain. Members of this group are putative signaling/adaptor proteins. They appear to mediate signal transduction in lymphoid tissues. Murine HACS1 protein likely plays a role in B cell activation and differentiation. Potential binding partners of HACS1 are SLAM, DEC205 and PIR-B receptors and also some unidentified tyrosine-phosphorylated proteins. Proteins of this group were found preferentially expressed in normal hematopietic tissues and in some malignancies including lymphoma, myeloid leukemia and myeloma
RRPKPKTLQELLERIHLQEYTSTLLLNGYETLEDLKDLKESHLIELNITDPEDRARLLSAAENLLD
>gnl|CDD|188961 cd09562, SAM_liprin-alpha1,2,3,4_repeat1, SAM domain of liprin-alpha1,2,3,4 proteins repeat 1. SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone
FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSL
T
>gnl|CDD|188962 cd09563, SAM_liprin-beta1,2_repeat1, SAM domain of liprin-beta1,2 proteins repeat 1. SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity
FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA
>gnl|CDD|188963 cd09564, SAM_kazrin_repeat1, SAM domain of kazrin proteins repeat 1. SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization
MSRWKADMVLAWLEVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEEYRDPE
>gnl|CDD|188964 cd09565, SAM_liprin-alpha1,2,3,4_repeat2, SAM domain of liprin-alpha1,2,3,4 proteins repeat 2. SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone
MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL
>gnl|CDD|188965 cd09566, SAM_liprin-beta1,2_repeat2, SAM domain of liprin-beta1,2 proteins repeat 2. SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity
KLDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR
>gnl|CDD|188966 cd09567, SAM_kazrin_repeat2, SAM domain of kazrin proteins repeat 2. SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization
QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR
>gnl|CDD|188967 cd09568, SAM_liprin-alpha1,2,3,4_repeat3, SAM domain of liprin-alpha1,2,3,4 proteins repeat 3. SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone
DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNN
LL
>gnl|CDD|188968 cd09569, SAM_liprin-beta1,2_repeat3, SAM domain of liprin-beta proteins repeat 3. SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity
EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQ
LL
>gnl|CDD|188969 cd09570, SAM_kazrin_repeat3, SAM domain of kazrin proteins repeat 3. SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization
DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEA
LV
>gnl|CDD|188970 cd09571, SAM_tumor-p73, SAM domain of tumor-p73 proteins. SAM (sterile alpha motif) domain of p73 proteins is a putative protein-protein interaction and lipid-binding domain. p73 is a homolog to the tumor suppressor p53. p73 has a C-terminal SAM domain in the longest spliced alpha form, while p53 doesn't have it. p73 knockout mouse shows significant developmental abnormalities but no increased cancer susceptibility, suggesting that p73 plays a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for the p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain
YNPDPSLVSFLTGLGCPNCIDYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMAIWRGLQELKQG
>gnl|CDD|188971 cd09572, SAM_tumor-p63, SAM domain of tumor-p63 proteins. SAM (sterile alpha motif) domain of p63 proteins is a putative protein-protein interaction domain. p63 is homolog to the tumor suppressor p53. p63 has a C-terminal SAM domain in the longest spliced alpha form, while p53 doesn't have it. p63 knockout mice show significant developmental abnormalities but no increased cancer susceptibility, suggesting that p63 plays a role in regulation of normal development. No evidence for homooligomerization through SAM domains was found for the p63 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain. Mutations in the SAM domain of p63 are found in AEC syndrome patients
YPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLSSLKIPEQFRHAIWKGILDHRQL
>gnl|CDD|188972 cd09573, SAM_STIM1, SAM domain of STIM1 subfamily proteins. SAM (sterile alpha motif) domain of STIM1 (Stromal interaction molecule) subfamily proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 protein is an activator of store operated channels in plasma membrane
EVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNATMTGTVLKMTDRSHRQKLQLKALDT
VLFG
>gnl|CDD|188973 cd09574, SAM_STIM2, SAM domain of STIM2 subfamily proteins. SAM (sterile alpha motif) domain of STIM2 (Stromal interaction molecule) subfamily proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM2 protein is an inhibitor of store operated channels in plasma membrane
EVHNWTMEDTLQWLKEFVELPQYEKNFRDNNVKGTTLPRIAVNEPSFMISQLKILDRSHRQKLQLKALDV
VLFG
>gnl|CDD|188974 cd09575, SAM_DGK-delta, SAM domain of diacylglycerol kinase delta. SAM (sterile alpha motif) domain of DGK-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK-delta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. In particular DGK-delta is involved in the regulation of clathrin-dependent endocytosis. The SAM domain of DGK-delta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-eta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it inhibits the translocation of the protein to the plasma membrane from the cytoplasm. The SAM domain also can bind Zn at multiple (not conserved) sites driving the formation of highly ordered large sheets of polymers, thus suggesting that Zn may play important role in the function of DCK-delta
PVHLWGTEEVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL
>gnl|CDD|188975 cd09576, SAM_DGK-eta, SAM domain of diacylglycerol kinase eta. SAM (sterile alpha motif) domain of DGK-eta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases. The SAM domain is located at the C-terminus of two out of three isoforms of DGK-eta protein. DGK-eta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DCK-eta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-delta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it is responsible for sustained endosomal localization of the protein and resulted in negative regulation of DCK-eta catalytic activity
PVQKWGTDEVAAWLDLLSLGEYKEIFIRHDIRGSELLHLERRDLKDLGIPKVGHMKRILQGIKEL
>gnl|CDD|188976 cd09577, SAM_Ph1,2,3, SAM domain of Ph (polyhomeotic) proteins of Polycomb group. SAM (sterile alpha motif) domain of Ph (polyhomeotic) proteins of Polycomb group is a protein-protein interaction domain. Ph1,2,3 proteins are members of PRC1 complex. This complex is involved in transcriptional repression of Hox (Homeobox) cluster genes. It is recruited through methylated H3Lys27 and supports the repression state by mediating monoubiquitination of histone H2A. Proteins of the Ph1,2,3 subfamily contribute to anterior-posterior neural tissue specification during embryogenesis. Additionally, the P2 protein of zebrafish is known to be involved in epiboly and tailbud formation. SAM domains of Ph proteins may interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with the SAM domain of Scm (sex comb on midleg) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome
SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE
>gnl|CDD|188977 cd09578, SAM_Scm, SAM domain of Scm proteins of Polycomb group. SAM (sterile alpha motif) domain of Scm (Sex comb on midleg) subfamily of Polycomb group is a protein-protein interaction domain. Proteins of this subfamily are transcriptional repressors associated with PRC1 complex. This group includes invertebrate Scm protein and chordate Scm homolog 1 and Scm-like 1, 2, 3 proteins. Most have a SAM domain, two MBT repeats, and a DUF3588 domain, except Scm-like 4 proteins which do not have MBT repeats. Originally the Scm protein was described in Drosophila as a regulator required for proper spatial expression of homeotic genes. It plays a major role during early embryogenesis. SAM domains of Scm proteins can interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with SAM domains of Ph (polyhomeotic) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Mammalian Scmh1 protein is known be indispensible member of PRC1 complex; it plays a regulatory role for the complex during meiotic prophase of male sperm cells, and is particularly involved in regulation of chromatin modification at the XY chromatin domain of the pachytene spermatocytes
SKDPSTWSVEDVVQFIKEADPQALAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKL
KQ
>gnl|CDD|188978 cd09579, SAM_Samd7,11, SAM domain of Samd7,11 subfamily of Polycomb group. SAM (sterile alpha motif) domain is a protein-protein interaction domain. Phylogenetic analysis suggests that proteins of this subfamily are most closely related to SAM-Ph1,2,3 subfamily of Polycomb group. They are predicted transcriptional repressors in photoreceptor cells and pinealocytes of vertebrates. SAM domain containing protein 11 is also known as Mr-s (major retinal SAM) protein. In mouse, it is predominantly expressed in developing retinal photoreceptors and in adult pineal gland. The SAM domain is involved in homooligomerization of whole proteins (it was shown based on immunoprecipitation assay and mutagenesis), however its repression activity is not due to SAM/SAM interactions but to the C-terminal region
IRKWTVDDVCSFIGSLPGCAEYAQVFREHSIDGETLPLLTEEHLLNTMGLKLGPALKIRSQVAKRLGR
>gnl|CDD|188979 cd09580, SAM_Scm-like-4MBT, SAM domain of Scm-like-4MBT proteins of Polycomb group. SAM (sterile alpha motif) domain of Scm-like-4MBT (Sex comb on midleg like, Malignant Brain Tumor) subfamily proteins of the polycomb group is a putative protein-protein interaction domain. Additionally to the SAM domain, most of the proteins of this subfamily have 4 MBT repeats. In Drosophila SAM-Scm-like-4MBT protein (known as dSfmbt) is a member of Pho repressive complex (PhoRC). Additionally to dSfmbt, the PhoRC complex includes Pho or Pho-like proteins. This complex is responsible for HOX (Homeobox) gene silencing: Pho or Pho-like proteins bind DNA and dSmbt binds methylated histones. dSmbt can interact with mono- and di-methylated histones H3 and H4 (however this activity has been shown for the MBT repeats, while exact function of the SAM domain is unclear). Besides interaction with histones, dSmbt can interact with Scm (a member of PRC complex), but this interaction also seems to be SAM domain independent
PSTWGVKDVSQFLRENDCGAYCECFCRQNIDGKRLLSLTKEQIMTLTGMKVGPSLKIYDLIQQLKCK
>gnl|CDD|188980 cd09581, SAM_Scm-like-4MBT1,2, SAM domain of Scm-like-4MBT1,2 proteins of Polycomb group. SAM (sterile alpha motif) domain of Scm-like-4MBT1,2 (Sex comb on midleg, Malignant Brain Tumor) subfamily proteins (also known as Sfmbt1,2 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain four MBT repeats and DUF5388 domain. The MBT repeats of the human sfmbt1 protein are responsible for association with the nuclear matrix and for selective binding of H3 histone N-terminal tails, while the exact function of the SAM domain is unclear
EEEERLKLDSNPLFWSVDDVVRFIKSTDCAPLAKIFKDQEIDGQALLLLTLPTVQECMELKLGPAIKLCH
HIERVKVAFYEQFAN
>gnl|CDD|188981 cd09582, SAM_Scm-like-3MBT3,4, SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group. SAM (sterile alpha motif) domain of Scm-like-3MBT3,4 (Sex comb on midleg, Malignant brain tumor) subfamily proteins (also known as L3mbtl3,4 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are predicted transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain three MBT repeats and Zn finger domain. Murine L3mbtl3 protein of this subfamily is essential for maturation of myeloid progenitor cells during differentiation. Human L3mbtl4 is a potential tumor suppressor gene in breast cancer, while deregulation of L3MBTL3 is associated with neuroblastoma
VLRWSVDEVAEFVQSLPGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR
>gnl|CDD|188982 cd09583, SAM_Atherin-like, SAM domain of Atherin/Atherin-like subfamily. SAM (sterile alpha motif) domain of SAM_Atherin and Atherin-like subfamily proteins is a putative protein-protein and/or protein-lipid interaction domain. In addition to the C-terminal SAM domain, the majority of proteins belonging to this group also have PHD (or Zn finger) domain. As potential members of the polycomb group, these proteins may be involved in regulation of some key regulatory genes during development. Atherin can be recruited by Ruk/CIN85 kinase-binding proteins via its SH3 domains thus participating in the signal transferring kinase cascades. Also, atherin was found associated with low density lipids (LDL) in atherosclerotic lesions in human. It was suggested that atherin plays an essential role in atherogenesis via immobilization of LDL in the arterial wall. SAM domains of atherins are predicted to form polymers. Inhibition of polymer formation could be a potential antiatherosclerotic therapy
PSNWSVEDVVQYFKTAGFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKLQQQSH
>gnl|CDD|188983 cd09584, SAM_sec23ip, SAM domain of sec23ip. SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) group is a potential protein-protein interaction domain. Sec23ip proteins (also known as p125) contain an N-terminal proline-rich region, a central region containing a SAM domain and a C-terminal region with a predicted metal-binding domain. Sec23ip interacts with Sec23p/Sec24p part of COPII-coated vesicles complex involved in protein transport from the ER to the Golgi apparatus. The proline-rich region plays an essential role in this interaction. Overexpression of Sec23ip leads to disorganization of ER/Golgi intermediate compartment
RLNEEEEDVPSLQSVLEALSLSEYKSTFEKEKIDMESLLMCTVDDLKEMGIPLGPRKKIANFVKEKAAK
>gnl|CDD|188984 cd09585, SAM_DDHD2, SAM domain of DDHD2. SAM (sterile alpha motif) domain of DDHD2 group is a potential protein-protein interaction domain. DDHD2 proteins contain at least two domains:a SAM domain and a predicted metal-binding domain. Phospholipase A1 activity was demonstrated for the mammalian DDHD2 protein. Mutation of the putative catalytic serine resulted in elimination of activity. Unlike SEC23IP, DDHD2 proteins do not have an N-terminal proline-rich region and correspondingly they are not able to interact with Sec23p/Sec24p complex. Overexpression of DDHD2 is the cause of dispersion of ER/Golgi intermediate compartment and dispersion of tethering proteins located in the Golgi region, leading to aggregation in the endoplasmic reticulum
PADKSQGDTPTLEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGIPLGPRKKILNYIRRRFLL
>gnl|CDD|188985 cd09586, SAM_USH1G, SAM domain of USH1G. SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) proteins (also known as SANS) is a putative protein-protein interaction domain. Members of this group have an N-terminal ankyrin repeat region and C-terminal SAM domain. USH1G is expressed in the hair bundles of the inner ear sensory cells. It can form a functional network with USH1B (myosin VIIa), USH1C (harmonin b), USH1F (protocadherin-related 15), and USH1D (cadherin 23). The SAM domain of the USH1G protein is involved in synergetic interactions with the PDZ domain of harmonin. Such interactions contribute to the stability of harmonin. The network is required for the correct cohesion of the hair bundle. Mutations in the ush1g gene lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans
DTSPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDACQRRRQTIERP
>gnl|CDD|188986 cd09587, SAM_HARP, SAM domain of HARP subfamily. SAM (sterile alpha motif) domain of HARP (Harmonin-interacting Ankyrin Repeat-containing) proteins, also known as ANKS4B, is a protein-protein interaction domain. Proteins of this subfamily have an N-terminal ankyrin repeat region and C-terminal SAM. In mouse epithelial tissues, HARP protein interacts with the PDZ domain of harmonin. This scaffolding complex facilitates signal transduction in epithelia. HARP was found co-expressed with harmonin in a number of epithelial cells including pancreatic ductal epithelium, embryonic epithelia of the lung, kidney, salivary glands, and cochlea
DATPLEVFLSSQHLEEFLPIFMREQIDLEALMLCSDEDLQNIQMQLGPRKKILSAVARRKQVLQQPG
>gnl|CDD|188987 cd09588, SAM_LBP1, SAM domain of LBP1 (UBP1) transcription factors. SAM (sterile alpha motif) domain of LBP1 (also known as UBP1) transcription factor is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and some also have a C-terminal dimerization domain. They are involved in transcriptional regulation from early development to terminal differentiation. In particular, they regulate alpha-globin in erythroid cells and P450scc (the cholesterol side-chain cleavage enzyme, cytochrome) in human placenta. Human LBP1 is known to be induced by HIV type I infection in lymphocytes; it represses HIV transcription by preventing the binding of TFIID to the virus promoter. Additionally, it has been suggested that UBP1 (LPB1) regulator might be a member of a blood pressure controlling network. LBP1 protein isoforms are able to form dimers, apparently via SAM domain since SAM deletion or mutation resulted in a loss of this ability
TIQETQQWLLKNRFSSYTRLFSNFSGADLLKLTREDLVQICGAADGIRLYNALKSRSVRPRLTIYVC
>gnl|CDD|188988 cd09589, SAM_TFCP2, SAM domain of TFCP2 transcription factors. SAM (sterile alpha motif) domain of TFCP2 transcription factors is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and a C-terminal dimerization domain. They are involved in transcriptional regulation from early development to terminal differentiation. In particular, they regulate expression of erythroid cell-specific alpha-globin, fibrinogen, and sex-determining gene SRY as well as lens alpha-crystallin. TFCP2 regulators can interact with NF-E4 proteins forming heteromeric stage selector protein complex (SSP). This complex is able to bind stage selector element (SSE) and regulate embryonic globin expression in fetal-erythroid cells
TPQEAQQWLHRNRFSTFSRLFTNFSGADLLKLTREDVIQICGPADGIRLFNALKGRMVRPRLTIYVC
>gnl|CDD|188989 cd09590, SAM_LBP9, SAM domain of LBP9 transcriptional factors. SAM (sterile alpha motif) domain of LBP9 (also known as TFCP2L1 or CRTR-1 (CP2-Related Transcriptional Repressor-1)) transcription factor is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and a C-terminal dimerization domain. They are involved in transcriptional regulation from early development to terminal differentiation. In particular, they are required for proper maturation of the dust (epithelial component of tubular organs) of kidney and salivary gland as well as for regulation of P450scc (the cholesterol side-chain cleavage enzyme, cytochrome) in human placenta
SIQDAQQWLHRNRFSQFCRLFSSFSGADLLKMSRDDFIQICGPADGIRLFNAIKGRNVRPRLTIYVC
>gnl|CDD|188990 cd09591, SAM_DLC1, SAM domain of DLC1 subfamily. SAM (sterile alpha motif) domain of DLC1 (Deleted in liver cancer) protein is a protein-protein interaction domain located at the N-terminus. Proteins of this subfamily do not form dimers/oligomers through their SAM domains. They participate in regulation of cell migration. SAM domain of human DLC1 protein contains the EF1A1 (eukaryotic elongation factor) binding motif, thus SAM facilitates recruitment of EF1A1 to the membrane periphery and suppresses cell migration
KEACDWLRAAGFPQYAQLYEDLLFPIDIELVKREHDFLDRDAIEALCRRLNTLNKCAVMK
>gnl|CDD|188991 cd09592, SAM_DLC2, SAM domain of STARD13-like subfamily. SAM (sterile alpha motif) domain of DLC2 (Deleted in liver cancer) protein is a lipid-binding and putative protein-protein interaction domain located at the N-terminus of the protein. Members of this subfamily do not form dimers/oligomers through their SAM domains. They participate in lipid transfer. Human Dlc2 gene is known as a tumor suppressor gene. It was found underexpressed in hepatocellular carcinoma
EIEAKEACDWLRAAGFPQYAQLYEDSQFPIDIASVKRDHDFLDRDLVEPLCRRLNTLNKCASMK
>gnl|CDD|381677 cd09593, UDG-like, uracil-DNA glycosylases (UDG) and related enzymes. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil may arise from misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C-_A:T mutations; thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other. UDG family 1 is the most efficient uracil-DNA glycosylase (UDG, also known as UNG) and shows a specificity for uracil in DNA. UDG family 2 includes thymine DNA glycosylase which removes uracil and thymine from G:U and G:T mismatches, and mismatch-specific uracil DNA glycosylase (MUG) which in Escherichia coli is highly specific to G:U mismatches, but also repairs G:T mismatches at high enzyme concentration. UDG family 3 includes Human SMUG1 which can remove uracil and its oxidized pyrimidine derivatives from, single-stranded DNA and double-stranded DNA with a preference for single-stranded DNA. Pedobacter heparinus SMUG2, which is UDG family 3 SMUG1-like, displays catalytic activities towards DNA containing uracil or hypoxanthine/xanthine. UDG family 4 includes Thermotoga maritima TTUDGA, a robust UDG which like family 1, acts on double-stranded and single-stranded uracil-containing DNA. UDG family 5 (UDGb) includes Thermus thermophilus HB8 TTUDGB which acts on double-stranded uracil-containing DNA; it is a hypoxanthine DNA glycosylase acting on double-stranded hypoxanthine-containing DNA except for the C/I base pair, as well as a xanthine DNA glycosylase which acts on both double-stranded and single-stranded xanthine-containing DNA. UDG family 6 hypoxanthine-DNA glycosylase lacks any detectable UDG activity; it excises hypoxanthine. Other UDG families include one represented by Bradyrhizobium diazoefficiens Blr0248 which prefers single-stranded DNA and removes uracil, 5-hydroxymethyl-uracil or xanthine from it
VLIVGQNPGPHGARAGGVPPGPSGNRLWRLLAAAGGTPRLFRYGVGLTNTVPRGPPGAAAGSEKKELRFC
GRWLRKLLELLNPRVVVLLGKKAQEAYLAVLTSSKGAPGKGTEVLVLPHPSPRNR
>gnl|CDD|341057 cd09594, GluZincin, Gluzincin Peptidase family (thermolysin-like proteinases, TLPs) which includes peptidases M1, M2, M3, M4, M13, M32 and M36 (fungalysins). The Gluzincin family (thermolysin-like peptidases or TLPs) includes several zinc-dependent metallopeptidases such as M1, M2, M3, M4, M13, M32, M36 peptidases (MEROPS classification), which contain the HEXXH motif as part of their active site. Peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. The M1 family includes aminopeptidase N (APN) and leukotriene A4 hydrolase (LTA4H). APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types. LTA4H is a bifunctional enzyme, possessing an aminopeptidase as well as an epoxide hydrolase activity such that the two activities occupy different, but overlapping sites. The M3_like peptidases include the M2_ACE, M3 or neurolysin-like family (subfamilies M3B_PepF and M3A) and M32_Taq peptidases. The M2 peptidase angiotensin converting enzyme (ACE, EC 3.4.15.1) catalyzes the conversion of decapeptide angiotensin I to the potent vasopressor octapeptide angiotensin II. ACE is a key component of the renin-angiotensin system that regulates blood pressure, thus ACE inhibitors are important for the treatment of hypertension. M3A includes thimet oligopeptidase (TOP; endopeptidase 3.4.24.15), neurolysin (3.4.24.16), and the mitochondrial intermediate peptidase; and M3B includes oligopeptidase F. The M32 family includes eukaryotic enzymes from protozoa Trypanosoma cruzi, a causative agent of Chagas' disease, and from Leishmania major, a parasite that causes leishmaniasis, making these enzymes attractive targets for drug development. The M4 family includes secreted protease thermolysin (EC 3.4.24.27), pseudolysin, aureolysin, and neutral protease as well as bacillolysin (EC 3.4.24.28) that degrade extracellular proteins and peptides for bacterial nutrition, especially prior to sporulation. Thermolysin is widely used as a nonspecific protease to obtain fragments for peptide sequencing as well as in production of the artificial sweetener aspartame. The M13 family includes neprilysin (EC 3.4.24.11) and endothelin-converting enzyme I (ECE-1, EC 3.4.24.71), which fulfill a broad range of physiological roles due to the greater variation in the S2' subsite allowing substrate specificity and are prime therapeutic targets for selective inhibition. The peptidase M36 fungalysin family includes endopeptidases from pathogenic fungi. Fungalysin hydrolyzes extracellular matrix proteins such as elastin and keratin. Aspergillus fumigatus causes the pulmonary disease aspergillosis by invading the lungs of immuno-compromised animals and secreting fungalysin that possibly breaks down proteinaceous structural barriers
TSYAHETYKYYEELLGRTSFRYPVSPIYSLLVYPAYVEVNAYNAMWIPSTNIFYGAGILDTLSGTIDVLA
HELTHAFTGQFSNLMYSWSSGWLNEGISDYFGGLV
>gnl|CDD|341058 cd09595, M1, Peptidase M1 family includes the catalytic domains of aminopeptidase N and leukotriene A4 hydrolase. The model represents the catalytic domains of M1 peptidase family members including aminopeptidase N (APN) and leukotriene A4 hydrolase (LTA4H). All peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile upon activation during catalysis. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types. APN expression is dysregulated in many inflammatory diseases and is enhanced in numerous tumor cells, making it a lead target in the development of anti-cancer and anti-inflammatory drugs. LTA4H is a bifunctional enzyme, possessing an aminopeptidase as well as an epoxide hydrolase activity. The two activities occupy different, but overlapping sites. The activity and physiological relevance of the aminopeptidase in LTA4H is as yet unknown, while the epoxide hydrolase converts leukotriene A4 (LTA4) into leukotriene B4 (LTB4), a potent chemotaxin that is fundamental to the inflammatory response of mammals
YHYDLDLDVDFTTKTLNGTETLTVDASQVGRELVLDLVGLTIHSVSVNGAAVDFGEREHYDGEKLTIPGP
KPPGQTFTVRISFEAKPSKNLLGWLWEQTAGKEKPYLFTQFEATHARRIFPCIDHPAVKATFTVTITTPK
KDLLASNGALVGEETGANGRKTYRFEDTPPIPTYLVAVVVGDLEFKYVTVKSQPRVGLSVYSEPLQVDQA
QYAFDATRAALAWFEDYFGGPYPLPKYDLLAVPDFNSGAMENPGLITFRTTYLLRSKVTDTGARSIENVI
AHELAHQWFGNLVTMRWWNDLWLNEGFAVYYENRIMDATFGTSSRHLDQLSGSSDLNTEQLLEDSSPTST
PVRSPADPDVAYDGVTYAKGALVLRMLEELVGEEAFDKGVQAYFNRHKFKNATTDDFIDALEE
>gnl|CDD|341059 cd09596, M36, Peptidase M36 family, also known as fungalysin family. The M36 peptidase family, also known as fungalysin (elastinolytic metalloproteinase) family, includes endopeptidases from pathogenic fungi. Fungalysin can hydrolyze extracellular matrix proteins such as elastin and keratin, with a preference for cleavage on the amino side of hydrophobic residues with bulky side-chains. This family is similar to the M4 (thermolysin) family due to the presence of the HEXXH motif in the active site residues, as well as its fold prediction. Some of these enzymes also contain a protease-associated (PA) domain insert. The eukaryotic M36 and bacterial M4 families of metalloproteases also share a conserved domain in their propeptides called FTP (fungalysin/thermolysin propeptide). Aspergillus fumigatus causes the pulmonary disease aspergillosis by invading the lungs of immuno-compromised animals; it secretes fungalysin that possibly breaks down proteinaceous structural barriers. A solid lesion known as an aspergilloma can grow in a lung cavity, particularly following recovery from tuberculosis. Fungalysins are also found as multiple copies in the human and animal pathogenic fungi such as Microsporum canis, Trichophyton rubrum and T. mentagrophytes, which cause cutaneous infections
NVIAYEDWSGGNNPPNNPGAPVSPPLVFDYPFDPALSPSPQTNVNAAITNLFYTVNKMHDILYRYGFTEA
AGNFQEDNFGKGGKGGDPVIAEVQDGSGRNNANFATPPDGQPPRMRMYLFTGTTAPYRDGALDNGVIIHE
YTHGLSNRLTGGPANASCLSNGEAGGMGEGWSDFFALWLTQKPGDTTDRTIGTYVTGQPTRGIRRYPYST
DPTTNPLTYSDVNGGSEVHAIGEVWAAMLWEVYWALVDKHGFSDTALTDPGGTGGNVVALQLVIDGLKLQ
PCNPTFLDARDAILQADAARYGGANQCLIWRAFAKRG
>gnl|CDD|341060 cd09597, M4_TLP, Peptidase M4 family including thermolysin, protealysin, aureolysin, and neutral protease. This peptidase M4 family includes several endopeptidases such as thermolysin (EC 3.4.24.27), aureolysin (the extracellular metalloproteinase from Staphylococcus aureus), neutral protease from Bacillus cereus, protealysin, and bacillolysin (EC 3.4.24.28). Typically, the M4 peptidases consist of a presequence (signal sequence), a propeptide sequence, and a peptidase unit. The presequence is cleaved off during export while the propeptide has inhibitory and chaperone functions and facilitates folding. The propeptide remains attached until the peptidase is secreted and can be safely activated. All peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. The active site is found between two sub-domains; the N-terminal domain contains the HEXXH zinc-binding motif while the helical C-terminal domain, which is unique for the family, carries the third zinc ligand. These peptidases are secreted eubacterial endopeptidases from Gram-positive or Gram-negative sources that degrade extracellular proteins and peptides for bacterial nutrition. They are selectively inhibited by Steptomyces metalloproteinase inhibitor (SMPI) as well as by phosphoramidon from Streptomyces tanashiensis. A large number of these enzymes are implicated as key factors in the pathogenesis of various diseases, including gastritis, peptic ulcer, gastric carcinoma, cholera and several types of bacterial infections, and are therefore important drug targets. Some enzymes of the family can function at extremes of temperatures, while some function in organic solvents, thus rendering them novel targets for biotechnological applications. Thermolysin is widely used as a nonspecific protease to obtain fragments for peptide sequencing. It has also been used in production of the artificial sweetener aspartame
RRTYDANNGTTLPGSLVVPVRGEGTAASGDSAAVDAHYNAGKVYDFYKNVFGRNSIDGKGMPLVSSVHYG
DNYDNAFWNGSQMVFGDGDGGTFPFLTSLDVVAHELTHGVTEYTAGLIYSGQSGALNESFSDIFGALVEQ
YANGTADKADWLIGEDIFTKGGGALRSMSNPSTDGGQPDHMSDYYTTYNDNGGVHINSGIPNKAFYLLAT
GGGGNGTVTGIGIEKAGKIWYRALTNYLTPTSTFADARRATLQAAKDLYGANSAEVAAVKKAWDAVGV
>gnl|CDD|341061 cd09598, M4_like, Peptidase M4 family containing mostly uncharacterized proteins. This family of uncharacterized bacterial proteins are homologs of the M4 peptidase family that is also known as the thermolysin-like peptidase (TLP) family. Typically, the M4 peptidases consist of a presequence (signal sequence), a propeptide sequence and a peptidase unit. The presequence is cleaved off during export while the propeptide has inhibitory and chaperone functions and facilitates folding. The propeptide remains attached until the peptidase is secreted and can be safely activated. All peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. TLPs are secreted eubacterial endopeptidases from Gram-positive or Gram-negative sources that degrade extracellular proteins and peptides for bacterial nutrition. They contain the HEXXH motif as part of their active site and belong to the Gluzincins family and are selectively inhibited by Steptomyces metalloproteinase inhibitor (SMPI) as well as by phosphoramidon from Streptomyces tanashiensis. A large number of these enzymes are implicated as key factors in the pathogenesis of various diseases, including gastritis, peptic ulcer, gastric carcinoma, cholera and several types of bacterial infections, and are therefore important drug targets. Some enzymes of the family can function at extremes of temperatures, while some function in organic solvents, thus rendering them novel targets for biotechnological applications
PGPIGARLEVYVVDPFHQQHVYAVARRTLDIFERALGRRIQWAFAQTGPRLEIVPHALREANAYYSRGDK
ALEFGYFRADDGGTVFTCLSHDIVAHETGHAVLDGLRPRFGEPSNPDVGAFHEAFADLVALFSHFHFPSV
VDALLARTRGNLLANNELSRLAEQFGQALGRADALRNAINSFKYSDVLQLSSEVHDRSRVFTGAVFDALA
DDVLSLLIRAIDYCPPVDLTFGDYARALITADQDLVPDLAYRGALEEAFRRRG
>gnl|CDD|341062 cd09599, M1_LTA4H, Peptidase M1 family including Leukotriene A4 hydrolase catalytic domain. This model represents the N-terminal catalytic domain of leukotriene A4 hydrolase (LTA4H; E.C. 3.3.2.6) and the close homolog cold-active aminopeptidase (Colwellia psychrerythraea-type peptidase; ColAP), both members of the aminopeptidase M1 family. LTA4H is a bifunctional enzyme, possessing an aminopeptidase as well as an epoxide hydrolase activity. The two activities occupy different, but overlapping sites. The activity and physiological relevance of the aminopeptidase is poorly understood while the epoxide hydrolase converts leukotriene A4 (LTA4) into leukotriene B4 (LTB4), a potent chemotaxin that is fundamental to the inflammatory response of mammals. It accepts a variety of substrates, including some opioid, di- and tripeptides, as well as chromogenic aminoacyl-p-nitroanilide derivatives. The aminopeptidase activity of LTA4H is possibly involved in the processing of peptides related to inflammation and host defense. Kinetic analysis shows that LTA4H hydrolyzes arginyl tripeptides with high efficiency and specificity, indicating its function as an arginyl aminopeptidase. Thermodynamic characterization using different biophysical methods shows that structurally distinct inhibitors of the LTA4H occupy different regions of the binding site; while some (RB202, ARM1 and SC57461A) bind to the hydrophobic hydrolase side, both bestatin and captopril are located at the hydrophilic peptidase side. LTB4H overexpression is associated with different pathological conditions and diseases such as cystic fibrosis, coronary heart disease, sepsis, shock, connective tissue disease, and chronic obstructive pulmonary disease. It is also overexpressed in certain human cancers, and has been identified as a functionally important target for mediating anticancer properties of resveratrol, a well-known red wine polyphenolic compound with cancer chemopreventive activity
DPSSFSNYDEVRTTHLDLDLTVDFDKKTISGSATLTLEVLQDGADELVLDTRDLDISSVTVNGGKELKFE
LGPRDPVLGSALTITLPSPLAKGDTFKVKIEYSTTPQATALQWLTPEQTAGKKHPYLFTQCQAIHARSLF
PCQDTPSVKSTYSATVTVPKGLTALMSALRTGEKEEAGTGTYTFEQPVPIPSYLIAIAVGDLESREIGPR
SGVWAEPSVVDAAAEEFADTEKFLKAAEKLYGPYVWGRYDLLVLPPSFPYGGMENPCLTFATPTLIAGDR
SLVDVIAHEIAHSWSGNLVTNANWEHFWLNEGFTVYLERRILERLYGEEYRQFEAILGWKDLQESIKEFG
EDPPYTLLVPDLKGVDPDDAFSSVPYEKGFQFLYYLEQLGGREVFDPFLRAYFKKFAFQSIDTEDFKDFL
LEYFAEDKPEILDKIDWDAWLY
>gnl|CDD|341063 cd09600, M1_APN, Peptidase M1 family, including aminopeptidase N catalytic domain. This model represents the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. It includes bacterial-type alanyl aminopeptidases as well as PfA-M1 aminopeptidase (Plasmodium falciparum-type). APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established
DYKPPDFLIDHVDLDFDLDDDETIVTSRLRVRRNPDSGEGAPLVLDGEDLELLSVKIDGKPLSPSDYTLD
EEGLTIKNVPDRFVLEIEVRINPAANTSLEGLYKSGGILCTQCEAEGFRRITYFPDRPDVMSKFTVTIEA
DKEKYPVLLSNGNLIEEGELPNGRHFAVWEDPFPKPSYLFALVAGDLGSVEDTFTTKSGRKVKLRIYVEP
GNEDKCHHAMESLKKAMKWDEERFGLEYDLDLFNIVAVDDFNMGAMENKGLNIFNSKYVLADPETATDAD
YERIESVIAHEYFHNWTGNRVTCRDWFQLSLKEGLTVFRDQEFSADMNSRAVKRIEDVRRLRSAQFPEDA
GPMAHPIRPDSYIEINNFYTVTVYEKGAEVIRMLHTLLGEEGFRKGMDLYFERHDGQAVTCEDFVAAMED
ASGRDLSQFKRWYS
>gnl|CDD|341064 cd09601, M1_APN-Q_like, Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), aminopeptidase Q (APQ), tricorn interacting factor F3, and endoplasmic reticulum aminopeptidase 1 (ERAP1). This M1 peptidase family includes eukaryotic and bacterial members: the catalytic domains of aminopeptidase N (APN), aminopeptidase Q (APQ, laeverin), endoplasmic reticulum aminopeptidase 1 (ERAP1) as well as tricorn interacting factor F3. Aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease, preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is considered a marker of differentiation since it is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. ERAP1, also known as endoplasmic reticulum aminopeptidase associated with antigen processing (ERAAP), adipocyte derived leucine aminopeptidase (A-LAP), or aminopeptidase regulating tumor necrosis factor receptor I (THFRI) shedding (ARTS-1), associates with the closely related ER aminopeptidase ERAP2, for the final trimming of peptides within the ER for presentation by MHC class I molecules. ERAP1 is associated with ankylosing spondylitis (AS), an inflammatory arthritis that predominantly affects the spine. ERAP1 also aids in the shedding of membrane-bound cytokine receptors. The tricorn interacting factor F3, together with factors F1 and F2, degrades the tricorn protease products, producing free amino acids, thus completing the proteasomal degradation pathway. F3 is homologous to F2, but not F1, and shows a strong preference for glutamate in the P1' position. APQ, also known as laeverin, is specifically expressed in human embryo-derived extravillous trophoblasts (EVTs) that invade the uterus during early placentation. It cleaves the N-terminal amino acid of various peptides such as angiotensin III, endokinin C, and kisspeptin-10, all expressed in the placenta in large quantities. APN is a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs are also putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established
LHYDLTLTPDLENFTFSGSVTITLEVLEPTDTIVLHAKDLTITSASLTLKGGSGIIEVTVVTDEETEFLT
ITLDETLPPGENYTLSIEFTGKLNDDLRGFYRSSYTDEDGETRYLAATQFEPTDARRAFPCFDEPAFKAT
FDITITHPKGYTALSNMPPVESTELEDGWKTTTFETTPPMSTYLVAFVVGDFEYIESTTKSGVPVRVYAR
PGKIEQGDFALEVAPKILDFYEDYFGIPYPLPKLDLVAIPDFAAGAMENWGLITYRETALLYDPKTSSAS
DKQRVAEVIAHELAHQWFGNLVTMKWWDDLWLNEGFATYMEYLAVDKLFPEWNMWDQFVVDELQSALELD
SLASSHPIEVPVESPSEISEIFDAISYSKGASVLRMLENFLGEEVFRKGLRKYLKKHAYGNATTDDLWEA
LQEASGESKPLDVKEIMDSWTL
>gnl|CDD|341065 cd09602, M1_APN, Peptidase M1 family including aminopeptidase N catalytic domain. This model represents the catalytic domain of bacterial and eukaryotic aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established
LTREEAEQRAALISVVSYDLDLDLTEGAETFRGTVTIRFTLREPGASLFLDFRGGEVKSVTLNGRPLDPS
AFDGERITLPGLLKAGENTVVVEFTAPYSSDGEGLHRFVDPADGETYLYTLFEPDDARRVFPCFDQPDLK
ATFTLTVTAPADWTVISNGPETSTEEAGGRKRWRFAETPPLSTYLFAFVAGPYHRVEDEHDGIPLGLYCR
ESLAEYERDADEIFEVTKQGLDFYEDYFGIPYPFGKYDQVFVPEFNFGAMENPGAVTFRESYLFREEPTR
AQRLRRANTILHEMAHMWFGDLVTMKWWDDLWLNESFADFMAAKALAEATPFTDAWLTFLLRRKPWAYRA
DQLPTTHPIAQDVPDLEAAGSNFDGITYAKGASVLKQLVALVGEEAFRAGLREYFKKHAYGNATLDDLIA
ALDEASGRDLSAWADAWLRT
>gnl|CDD|341066 cd09603, M1_APN_like, Peptidase M1 family similar to aminopeptidase N catalytic domain. This family contains mostly bacterial and some archaeal M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established
YDVLHYDLDLDYDPATKSLSGTATITFRATQDLDSLQLDLVGLTVSSVTVDGVPAAFFTHDGDKLVITLP
RPLAAGETFTVTVRYSGKPRPAGYPPGDGGGWEEGDDGVWTAGQPEGASTWFPCNDHPDDKATYDITVTV
PAGLTVVSNGRLVSTTTNGGGTTTWHWKMDYPIATYLVTLAVGRYAVVEDGSGGGIPLRYYVPPGDAAKA
KASFARTPEMLDFFEELFGPYPFEKYGQVVVPDLGGGMEHQTATTYGNNFLNGDRGSERLIAHELAHQWF
GDSVTCADWADIWLNEGFATYAEWLWSEHKGGADAYRAYLAGQRQDYLNADPGPGRPPDPDDLFDRDVYQ
KGALVLHMLRNLLGDEAFFAALRAYLARYAHGNVTTEDFIAAAEEVSGRDLTWFFDQWLY
>gnl|CDD|341067 cd09604, M1_APN_like, Peptidase M1 family similar to aminopeptidase N catalytic domain. This family contains bacterial M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established
YDIDVTLDPETHTLTGKETITYTNNSPDTLDELYFHLYPNAFKPGSTMPARDSRIAKLKGDEPGGIDIDS
VKVNGKGLKLEVTLTITRLKLALPLPLKPGESVTVEIDFTVKLPEQGGRFGYDGDEYNLAQWYPKLAVYD
DGGWNTDPYYGRGEFFYSDFGDYDVTITVPKNYVVAATGELQNPEEVLDGTKTWHFKAENVRDFAWAASP
DFVVDAATVDGVTVNVYYLPENAEAAERALEYAKDALEFFSEKFGPYPYPELDVVQGPFGGGGMEYPGLV
FIGSRLYDPKRSLEGVVVHEIAHQWFYGIVGNDERREPWLDEGLATYAESLYLEEKYGKEAADELLGRRY
YRAYARGPGGPINLPLDTFPDGSYYSNAVYSKGALFLEELREELGDEAFDKALREYYRRYKFKHPTPEDF
FRTAEEVSGKDLDWFFRGWL
>gnl|CDD|341068 cd09605, M3A, Peptidase M3A family includes thimet oligopeptidase, dipeptidyl carboxypeptidase and mitochondrial intermediate peptidase. The M3-like family also called neurolysin-like family, is part of the "zincins" metallopeptidases, and includes M3, M2 and M32 families of metallopeptidases. The M3 family is subdivided into two subfamilies: the widespread M3A, represented by this CD, which comprises a number of high-molecular mass endo- and exopeptidases from bacteria, archaea, protozoa, fungi, plants and animals, and the small M3B, whose members are enzymes primarily from bacteria. Well-known mammalian/eukaryotic M3A endopeptidases are the thimet oligopeptidase (TOP; endopeptidase 3.4.24.15), neurolysin (alias endopeptidase 3.4.24.16), and the mitochondrial intermediate peptidase. The first two are intracellular oligopeptidases, which act only on relatively short substrates of less than 20 amino acid residues, while the latter cleaves N-terminal octapeptides from proteins during their import into the mitochondria. The M3A subfamily also contains several bacterial endopeptidases, called oligopeptidases A, as well as a large number of bacterial carboxypeptidases, called dipeptidyl peptidases (Dcp; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). The peptidases in the M3 family contain the HEXXH motif that forms part of the active site in conjunction with a C-terminally-located Glutamic acid (Glu) residue. A single zinc ion is ligated by the side-chains of the two Histidine (His) residues, and the more C-terminal Glu. Most of the peptidases are synthesized without signal peptides or propeptides, and function intracellularly
PERFHELIEQTKRVYDLVGTRACSTPPYENTLLALADLEVTLTRVRDLLDFPQHAHPEPEFREASEEADK
KLSEFDEEMSMNEDLYQRIVKLQEDKKLVSLDPEARRYLELFIKDFERNGLHLDKEKRKRIKDLNKKISD
LCSDFNKNLNPETREKAEKAFLTRCKAENLAILQELLSLRAQLAKLLGYSTHADRVLEGNMAKTPETVAQ
FLDELSQKLKPRGEKEREMILGLKMKECEQDGEIMPWDPPYYMGQVREERYNVDQSLLKPYFPLGVVTEG
LLIIYNELLGISFYAEQDAEVWHEDVRLYTVVDEAEEVLGYFYLDFFPREGKYGHAACFGLQPGCLKEDG
SRQLPVAALVLNFPKPSAGSPSLLTHDEVRTLFHEFGHVMHQLCARTRYAHFSGTNVPTDFVEVPSQMLE
NWAWDVNQFARHSRHYQSGAPLPDELLEKLCESRLVNTGLDMLRQIVLAKLDQILHTKHPLRNDTADELA
ELCEEILGLPATPGTNMPATFGHLAGGYDAQYYGYLWSEVVAMDMFHECFKQEPLNREVGMRYRREILAP
GGSEDPMLMLRGFLQKCPKQSAFLFSR
>gnl|CDD|341069 cd09606, M3B_PepF, Peptidase family M3B, oligopeptidase F (PepF). Peptidase family M3 oligopeptidase F (oligendopeptidase) is mostly bacterial and includes oligoendopeptidase F from Geobacillus stearothermophilus. This enzyme hydrolyzes peptides containing between 7 and 17 amino acids and may cleave proteins at Leu-Gly. The PepF gene is duplicated in Lactococcus lactis on the plasmid that bears it, while a shortened second copy is found in Bacillus subtilis. Most bacterial PepFs are cytoplasmic endopeptidases; however, the Bacillus amyloliquefaciens PepF oligopeptidase is a secreted protein and may facilitate the process of sporulation. Specifically, the yjbG gene encoding the homolog of the PepF1 and PepF2 oligoendopeptidases of Lactococcus lactis has been identified in Bacillus subtilis as an inhibitor of sporulation initiation when over-expressed from a multicopy plasmid
PDWEELEPEFQELLERFINAKSAEELEAWLKEISELRAEVEEMATLAYIRHTIDTDDEFYEAEQDFFDEI
SPLLEELEQELNKKLLASPFRKELEEEFGKQLFRLAENALKLFSEENIPLLQEENKLSSEYQKLIASATI
EFDGEELTLSQLSPYLESPDREVRKEAWEAIAEFFLEHEEELDEIYDELVKLRTQIAKNLGFENYREYGY
KRMGRFDYTPEDVAKFREAVEKHVVPLASKLREEQRKRLGLDKLRPYDEAVDFPGGNPKPFGDADELVEK
AQKMYHELSPETGEFFDFMRENGLLDLESRKGKAPGGYCTYLPEYKAPFIFANFNGTSGDVDVLTHEAGH
AFQAYLSRDLPLPEYRWPTMEAAEIHSMSMELLTWPWMELFFGEDADKYRREHLEGALTFLPYGATVDEF
QHWVYENPEHTPEERKAKWRELEKRYLPWVDYDGLPFLEKGGFWQRQLHIFEVPFYYIDYALAQLGALQF
WKNYQEDPEKAWEDYLKLCSLGGSKSFPELLEAAGLKFPFSEGTLKELVEFVE
>gnl|CDD|341070 cd09607, M3B_PepF, Peptidase family M3B, oligopeptidase F (PepF). Peptidase family M3B Oligopeptidase F (PepF; Pz-peptidase B; EC 3.4.24.-) is mostly bacterial and is similar to oligoendopeptidase F from Lactococcus lactis. This enzyme hydrolyzes peptides containing between 7 and 17 amino acids with fairly broad specificity. The PepF gene is duplicated in L. lactis on the plasmid that bears it, while a shortened second copy is found in Bacillus subtilis. Most bacterial PepFs are cytoplasmic endopeptidases; however, the Bacillus amyloliquefaciens PepF oligopeptidase is a secreted protein and may facilitate the process of sporulation. Specifically, the yjbG gene encoding the homolog of the PepF1 and PepF2 oligoendopeptidases of Lactococcus lactis has been identified in Bacillus subtilis as an inhibitor of sporulation initiation when over-expressed from a multicopy plasmid
WDLDSLYPGFDSPEFQEDLEKLKELIDALRELLEALLKDDENAVEKLEQILKLLEELRALLSQLSAYASC
LLSADTTDEEALKLLSRLALLQAKLSSALVPLDQFLALLSDEDLEALLADSELLEHRFYLEELREEAKHL
LSPEEEELIADLSVDGLHAWGRLYDQLTSTLRVPVEVDGETVTLSQARNLAYDPDREVRKAAYEAELKAW
EKIEDPFAAALNHIKGFRLTLYKLRGYESPLDESLEQNRMSRETLDAMWSAIEENLPLFRRYLKRKAKLL
GHEKLPWYDLFAPLGESSKKYTYEEAKDFIVEAFSSFSPELGDFARRAFEEGWIDAEPRPGKRGGAFCTN
FPLIKESRIFMNFTGSFSDVSTLAHELGHAYHNWVLRDLPPLNQDYPMTLAETASTFAETIVLDAALKQA
ESDEEKLALLEQKLSDAAQFIVDIYSRFLFEKAFYEERKEGELSAEELKELMLEAQKEAYGDGLDEYLHP
YMWASKLHFYSTDLSFYNFPYTFGYLFSLGLYAQYQKEGEAFVEKYDALLRDTGRMTAEELVAKHLGIDL
TSPDFWQSSLDLIEEDIEEF
>gnl|CDD|341071 cd09608, M3B_PepF, Peptidase family M3B, oligopeptidase F (PepF). Peptidase family M3B oligopeptidase F (PepF; Pz-peptidase B; EC 3.4.24.-) is mostly bacterial and includes oligoendopeptidase F from Lactococcus lactis. This enzyme hydrolyzes peptides containing between 7 and 17 amino acids with fairly broad specificity. The PepF gene is duplicated in L. lactis on the plasmid that bears it, while a shortened second copy is found in Bacillus subtilis. Most bacterial PepFs are cytoplasmic endopeptidases; however, the Bacillus amyloliquefaciens PepF oligopeptidase is a secreted protein and may facilitate the process of sporulation. Specifically, the yjbG gene encoding the homolog of the PepF1 and PepF2 oligoendopeptidases of Lactococcus lactis has been identified in Bacillus subtilis as an inhibitor of sporulation initiation when over-expressed from a multicopy plasmid. This PepF family includes Streptococcus agalactiae PepB, a group B streptococcal oligopeptidase which has been shown to degrade a variety of bioactive peptides as well as the synthetic collagen-like substrate N-(3-[2-furyl]acryloyl)-Leu-Gly- Pro-Ala in vitro
KLKELLEELKKYKGKLGDSAETLLEALKLYEELSRLLEKLYVYASLKLDEDTTNSEYQALSQKAESLYTK
FSEATSFIEPEILALDEEKIESFLKEEPELKDYRFYLEDLLRYKPHTLSEEEEKLLAKASEALGAPENIF
SMLTNADLKFPTIKDSDGKKVELTHGNYSKLLESPDREVRKNAFEAYYKTYKKHKNTLAATLYGNVKKDV
FYAKARKYPSALEAALFSDNIPVSVYDNLIETVHKNLPLLHRYYKLRKKVLGLDELHMYDLYVPLVKDKD
KKYSYEEAKELVLEALAPLGEEYLDVLKKAFNERWIDVYENKGKRSGAYSSGSYGVHPYILLNYNGTLDS
VFTLAHELGHSMHSYYSNKNQPYVYADYPIFVAEVASTFNELLLLDYLLKKAKDKEEKLYLLNHYLENFR
GTVFRQTMFAEFELEIHELVEKGEPLTAEKLSEIYYDLNKKYYGPDVVVDDEIAYEWARIPHFYYNFYVY
QYATGFSAATALAERILNGGEGAVEKYLNFLKSGGSDYPLELLKKAGVDMTSPEPYEAALKVFEELLDEL
>gnl|CDD|341072 cd09609, M3B_PepF, Peptidase family M3B, oligopeptidase F (PepF). Peptidase family M3B oligopeptidase F (PepF; Pz-peptidase B; EC 3.4.24.-) is mostly bacterial and is similar to oligoendopeptidase F from Lactococcus lactis. This enzyme hydrolyzes peptides containing between 7 and 17 amino acids with fairly broad specificity. The PepF gene is duplicated in L. lactis on the plasmid that bears it, while a shortened second copy is found in Bacillus subtilis. Most bacterial PepFs are cytoplasmic endopeptidases; however, the Bacillus amyloliquefaciens PepF oligopeptidase is a secreted protein and may facilitate the process of sporulation. Specifically, the yjbG gene encoding the homolog of the PepF1 and PepF2 oligoendopeptidases of Lactococcus lactis has been identified in Bacillus subtilis as an inhibitor of sporulation initiation when over-expressed from a multicopy plasmid
RSEVPEEETWDLTDLFKDEEAFEAALEELEQLVDEFKKKYKGKLTDAEDILNALLDYEEILELLDRISHY
ASLPFSTDGTDPEAQARAGKFDSLLAEVSAALSFFESELLALDEGTLEEVKKEEPEYAPYLRDILRKKPH
TLSPEVEKALAALSPVLDAPYNIYNQAKLADMRFEDFEVDGKEYPNSFVLYENKYEYSPDTEVRRKAFES
FSKTLRKYQNTFAATYLTQVQKEKALAKLRGYDSVFDYLLFDQEVSREMYDRQIDVIMKELAPHMRRYAK
LLKKVYGLDKMTFADLKAPLDPEFSPKITIEEAKDYILDALSVLGEDYLAIIRRAFDERWVDFAQNIGKS
TGGFCASPYGVHPYILMSWTGLMSDVFTLAHELGHAGHFSLAGKNQSILNSEPSLYFVEAPSTMNELLLA
NYLLQQADDDRFKRWALSNMLSNTYYHNFVTHLLEAAYQREVYRLIDKGEPLTADVLNQIKKEVLEEFWG
DAVEIDEGAELTWMRQPHYYMGLYSYTYSAGLTISTQAAQRIEEEGEPAAKRWLEVLKAGGSKSPLELAK
MAGVDITTDKPLRDTIAYVGSLVDEL
>gnl|CDD|341073 cd09610, M3B_PepF, Peptidase family M3B, oligopeptidase F (PepF). Peptidase family M3B oligopeptidase F (PepF; Pz-peptidase B; EC 3.4.24.-) is mostly bacterial and is similar to oligoendopeptidase F from Lactococcus lactis. This enzyme hydrolyzes peptides containing between 7 and 17 amino acids with fairly broad specificity. The PepF gene is duplicated in L. lactis on the plasmid that bears it, while a shortened second copy is found in Bacillus subtilis. Most bacterial PepFs are cytoplasmic endopeptidases; however, the Bacillus amyloliquefaciens PepF oligopeptidase is a secreted protein and may facilitate the process of sporulation. Specifically, the yjbG gene encoding the homolog of the PepF1 and PepF2 oligoendopeptidases of Lactococcus lactis has been identified in Bacillus subtilis as an inhibitor of sporulation initiation when over-expressed from a multicopy plasmid
PEELLEALEEYEELSELLGKPGYYASLLFSTDTTDPEAKALLQKIEERLTEISNKLLFFELELAKLDEEK
QAKLLADPELADYRHYLERLRRFAPHTLSEPEEKILNLKSLTGRSAWVRLFDELLSRLTFVFEIDGKKKT
LSESELLSLLRSPDREVRKAAAKALTEVLKKNADVLTFIYNTILKDKKIEDKLRGYKSPISSRNLSNDVD
DEVVDALLEVVTKNYDLVQRYYKLKAKLLGLKKLRYYDRYAPLPDSKKKYSFEEAKEIVLDAFGSFSPEF
GEIARRFFDEGWIDAPPRKGKRGGAFCASVVPSLHPYVLLNFTGKLRDVMTLAHELGHGIHSYLARKQGI
LNQHTPLTLAETASTFGEMLVFDRLLKKESDPEEKLALLAEKLEDIIATVFRQIAFYRFEQEAHEARREG
GELSKEEISELWLETMKEMFGDSVELTEDYRYWWSYIPHFRHTPFYVYAYAFGELLVLSLYRRYKEEGKS
FVPKYLELLSAGGSKSPEELLKPFGIDISDPDFWQKGLDVIE
>gnl|CDD|187707 cd09611, Jacalin_ZG16_like, Jacalin-like lectin domain of the zymogen granule protein 16 and related proteins. ZG16p is a conserved secreted vertebrate protein with tissue-specific expression profiles, which might play a role in glycoprotein secretion, perhaps as a linker protein that participates in the formation and/or transport of the zymogen granule. Its paralog ZG16b (PAUF) has been associated with roles in gene regulation and cancer. This domain family also contains mammalian proteins labelled as prostatic spermine-binding protein (SBP) and salivary-gland specific secreted proteins
GSGGGKYFSDVGEGGGPITGIRVSVGNNYIKGIQVRYGSNWSDVYGGRGGNEQEIVLEPGESITKVSGSY
KIYLHGLVFTTNKGRYLSFGKLRGRSFNATPPPSNYVLRGISGRYGGLGIKSIGFHWG
>gnl|CDD|187708 cd09612, Jacalin, Jacalin-like plant lectin domain. Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. The family was initially named after an abundant protein found in the jackfruit seed. Jacalin specifically binds to the alpha-O-glycoside of the disaccharide Gal-beta1-3-GalNAc, and has proven useful in the study of O-linked glycoproteins. Jacalin-like lectins in this family may occur in various oligomerization states
GSAWDDGVFPDGLRKITVRSGENGIDSIKFEYDKDGQHVVGPWHGGGGGTPEEIVLDYPDEYITSVSGTY
GPVSGSNVITSLTFKTNKRTYGPFGVESGTPFSLPVEGGKIVGFHGRSGDYLDAIGVYVS
>gnl|CDD|187709 cd09613, Jacalin_metallopeptidase_like, Jacalin-like lectin domain of putative metalloproteases and similar proteins. Members of this family, which appears restricted to fungi, co-occur with protein domains that contain an HExxH motif characteristic of metallopeptidases. They have not been functionally characterized
GELSFDLIAIEKRLLTAVRVYHGYALDGIEFVYGDDASVLFGNRGGSPTDFELQPGEQILGFNVRCGAWI
DAIQILTSLGRTSPFYGNANGGGLHTLIPPRGYTILGVYGSCGQWVDGFGIIIG
>gnl|CDD|187710 cd09614, griffithsin_like, Jacalin-like lectin domain of griffithsin and related proteins. Griffithsin is a lectin isolated from a red alga, which has shown potential as an inhibitor of viral entry, exhibiting antiviral activity against HIV and SARS. The biological functions of griffithsin and griffithsin-like proteins with respect to their source organisms are not known
GFGGSPGSDFDILTVSAIQLRSGSYVDQIITDYQDLNGTQNFHHGGGGGNLSPTLNFSSGEYITEVTGRS
GDRVDQVQFTTNYGGRTLPGGGGGGSAFTWTVPDNQKVIGFAGRSGSYLDQLQVYYLS
>gnl|CDD|187711 cd09615, Jacalin_EEP, Jacalin-like lectin domains of putative endonucleases/exonucleases/phosphatases and related proteins. Members of this taxonomically diverse family co-occur with metal-dependent endonucleases/exonucleases/phosphatases. They have not been functionally characterized
GGPHGTSFNDLDALPGGPKVASVTLRGGSRVDGVSLTLTAGTTLAHGGTGGTASSLTLGSGEYLTSATLC
QGQKNGHTRIFYASFTTSTGRTLAGGTTTSDCVTYTAPEGWQIVGFHGRAGDEVDKLGVIYAPQ
>gnl|CDD|187737 cd09616, Peptidase_C12_UCH_L1_L3, Cysteine peptidase C12 containing ubiquitin carboxyl-terminal hydrolase (UCH) families L1 and L3. This ubiquitin C-terminal hydrolase (UCH) family includes UCH-L1 and UCH-L3, the two members sharing around 53% sequence identity as well as conserved catalytic residues. Both enzymes hydrolyze carboxyl terminal esters and amides of ubiquitin (Ub). UCH-L1, in dimeric form, has additional enzymatic activity as a ubiquitin ligase. It is highly abundant in the brain, constituting up to 2% of total protein, and is expressed exclusively in neurons and testes. Abnormal expression of UCH-L1 has been shown to correlate with several forms of cancer, including several primary lung tumors, lung tumor cell lines, and colorectal cancers. Mutations in the UCH-L1 gene have been linked to susceptibility to and protection from Parkinson's disease (PD); dysfunction of the hydrolase activity can lead to an accumulation of alpha-synuclein, which is linked to Parkinson's disease (PD), while accumulation of neurofibrillary tangles is linked to Alzheimer's disease (AD). UCH-L3 hydrolyzes isopeptide bonds at the C-terminal glycine of either Ub or Nedd8, a ubiquitin-like protein. It can also interact with Lys48-linked Ub dimers to protect them from degradation while inhibiting its hydrolase activity at the same time. Unlike UCH-L1, neither dimerization nor ligase activity have been observed for UCH-L3. It has been shown that levels of Nedd8 and the apoptotic protein p53 and Bax are elevated in UCH-L3 knockout mice upon cryptorchid injury, possibly contributing to profound germ cell loss via apoptosis
WIPLESNPEVMNKFLHKLGVSPGWEFVDVYGLDPELLAFVPRPVLAVLLLFPITKAYEEFRKEEEEEIKE
KGQEVSESVYFMKQTIGNACGTIALIHAVANNEDRINILEGSFLKKFLEEAKGLSPEERAKLLEKSEALE
KAHAAAATEGQTEAPSADEKVNLHFIAFVKKDGHLYELDGRKPGPINHGPTSEETLLKDAAKVCRKFIER
EPDEIRFSAIAL
>gnl|CDD|187738 cd09617, Peptidase_C12_UCH37_BAP1, Cysteine peptidase C12 containing ubiquitin carboxyl-terminal hydrolase (UCH) families UCH37 (UCH-L5) and BAP1. This ubiquitin C-terminal hydrolase (UCH) family includes UCH37 (also known as UCH-L5) and BRCA1-associated protein-1 (BAP1). They contain a UCH catalytic domain as well as an additional C-terminal extension which plays a role in protein-protein interactions. UCH37 is responsible for ubiquitin (Ub) isopeptidase activity in the 19S proteasome regulatory complex; it disassembles Lys48-linked poly-ubiquitin from the distal end of the chain. It is also associated with the human Ino80 chromatin-remodeling complex (hINO80) in the nucleus and can be activated through transient association of hINO80 with hRpn13 that is bound to the 19S regulatory particle or the proteasome. UCH37 possibly plays a role in oncogenesis; it competes with Smad ubiquitination regulatory factor 2 (Smurf2, ubiquitin ligase) in binding concurrently to Smad7 in order to deubiquitinate the activated type I transforming growth factor beta (TGF-beta) receptor, thus rescuing it from proteasomal degradation. BAP1 binds to the wild-type BRCA1 RING finger domain, localized in the nucleus. In addition to the UCH catalytic domain, BAP1 contains a UCH37-like domain (ULD), binding domains for BRCA1 and BARD1, which form a tumor suppressor heterodimeric complex, and a binding domain for HCFC1, which interacts with histone-modifying complexes during cell division. The full-length human BRCA1 is a ubiquitin ligase. However, BAP1 does not appear to function in the deubiquitination of autoubiquitinated BRCA1. BAP1 exhibits tumor suppressor activity in cancer cells, and gene mutations have been reported in a small number of breast and lung cancer samples. In metastasis of uveal melanoma, the most common primary cancer of the eye, inactivating somatic mutations have been identified in the gene encoding BAP1 on chromosome 3p21.1. These mutations include several that cause premature protein termination as well as affect its UCH domain, thus implicating loss of BAP1 and suggesting that the BAP1 pathway may be a valuable therapeutic target
WCEIESDPGVFTELLEEFGVKGVQVEELYSLDADSLEQLPPVYGLIFLFKWQEGEEDEGSVVDDEIPSNI
FFANQVIPNACATQALLSVLLNCSDEVDLGETLSEFKEFTKGFDPEMKGEAIGNSEEIRKVHNSFARPEP
FLLDEKLNKKATKEEDAFHFISYVPIGGRLYELDGLKEGPIDHGPCSEGEDWLEKARPVIQARIARYSEG
EIRFNLMAV
>gnl|CDD|187676 cd09618, CBM9_like_2, DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized subfamily are typically found at the N-terminus of longer proteins that lack additional annotation with domain footprints
SLTAVRISGPPVIDGVLDEAVWQQAPVATDFVQREPNDGGPAPERTEVRVLYDDEALYVAAVCYDPEPDK
IRAQLLRRDDDGENDDRFGVALDTFNDRRNAYQFGVNPAGVQRDALEFDGNNEDFSWDAVWESATKITDD
GWTAEMAIPFSSLRFPKGSVQTWGINFYRNIPRTNERSSWPPIPRN
>gnl|CDD|187677 cd09619, CBM9_like_4, DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other domains
APAIDGTLEAAWYPGSILPLEAKGLIDDTGPSATDLSATFAAMWDDTNLYVLVDVTDDTLRNDLDGKDHW
RGDAVEIFIDPDGNKLATYTANDFQLGFRPNDETGQPEGWNHTTPAPGIRVASTPRYGGYTVEAAIPWST
LGITPAANLLLGFDVAINDDDTGGTRDQQIAWNAKDDQNWSNPSLFG
>gnl|CDD|187678 cd09620, CBM9_like_3, DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily may co-occur with various other domains
IDGKLDEPAWQAAPWVELFVDIGGGPPPKPQTRVRLLYDDEYLYLAFEVEDDDIWATYTERDDPVWEDDV
VEVFIDPDGDGPNYYEFEVNPLGTVLDAFIRRPRDGGGDRDNRQPDSAGLESAVSIDGTLNDSDGDKGWT
VELAIPFAALAKAAGGPPLPGDVWRANFYRCGDPTETPPHYLSWSPTGVPDPHFHEPFGF
>gnl|CDD|187679 cd09621, CBM9_like_5, DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates
PDFRLDDADQVTSLSEKEHLRWKGPEDLSAKVWLGWDADNLYLAARVTDDRHSQPFTGADIWKGDSIQLA
LDLPGQKGGADGFWELGLARTDDGGALVWRWNAPAGFDPAAAAAAIRLETSRDEAKVTVYEAAIPWAELG
LTGPAAGDGFRFNLLVNDNDGGGREGWIEWAPGIGESKDPALFPLVTL
>gnl|CDD|187680 cd09622, CBM9_like_HisKa, DOMON-like type 9 carbohydrate binding module at the N-terminus of bacterial sensor histidine kinases. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this family are located at the N-terminus of bacterial sensor histidine kinases and may constitute or contribute to the ligand-binding moiety
MSLTRQLLAVSLLMLLLPWAGCQFLKELEQALRQQQSQQLQQQGNRLAALAGTDLYAYPLAGAILLDGYA
DDWPGYDSAFQLEGEAGQASSLAFKHRAGKYDRYLYLLFQVSDNTVIYRFNPSLPEDAHDHLLLQTEDPN
GQRQRYLIATSAPGWVNAFRLTRNAGAPEYRIQGHWQETADGYQLELRLPLSLVGSRLGFALTDVDNSNN
RIIGTANPLTLIPLPTLVVPSPELERILAGMSRPGSRLWVLDSHGWVLARQGDIQ
>gnl|CDD|187681 cd09623, DOMON_EBDH, Heme-binding domain of bacterial ethylbenzene dehydrogenase. Ethylbenzene dehydrogenase (EBDH) is a bacterial molybdopterin enzyme. It catalyzes anaerobic hydroxylation of alkylaromatic compounds to secondary alcohols. The DOMON domain in EBDH and related proteins, typically called the gamma subunit, binds a heme; its function in the catalytic mechanism is unclear. It co-occurs with a molybdopterin-binding subunit and an iron-sulfur protein. This family also contains heme-binding domains of dimethylsulfide dehydrogenase, selenate reductases, and chlorate reductase
MKRTLALLAALSLAAAAALTAAGAVLTAKVKEGEIPVDPPLDEIWSKVPLYPLTSVRLGDPLNKDTAVKS
LEVAAAHNGERIAVRLRWADGTKNVQTDGTDVFRDGVAVQFPVKTDTLPYIGMGDEGNPVNIWYWKADAG
STEELVAGGFGSTTELKEQDVKGVAAYKNGKWTVVFSRPLKTDDEGVADLEAGGTIPVAFAVWDGSNGER
DGLKAVSSWYYLRL
>gnl|CDD|187682 cd09624, DOMON_b558_566, DOMON-like heme-binding domain of CbsA. This family, conserved in some lineages of the Crenarchaeota, represents a mono-heme cytochrome b558/566. CbsA is reported to be a subunit in a heterodimeric complex (CbsA-CbsB in Sulfolobus species), and appears to be glycosylated
CPETAYTPVGAIWQPFSGPLPPGWWVVLVSYKTSNQGVASVYTLPNSEQIGYPPGQALVNPITIYGRNKL
NGSIIGAPNPNGTPNITSLNLGTIGILVTSPRPFEDLGYNDTTWDTAFYGYYFNNTTWYYPDRAAIMWYL
GSVPPTSDTMNIGTPHMMPGTSGDGITGGSLAQSAGQAEIWMWNSNPRANNTQDSGYPGATWFNRTSPPP
YFVATGATYENGYWIVEFVRPLSVPGVYGGYMPNLTPGKTYYVAFAVWQGKAGETLFDKSITSSFLTLT
>gnl|CDD|187683 cd09625, DOMON_like_cytochrome, DOMON-like domain of an uncharacterized protein family. This family of uncharacterized bacterial proteins contains a DOMON-like domain and an N-terminal B- or C-type cytochrome domain. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases
ALAVLAAVASGAAGLSTLDNDTLAALKVASAPTLDGKLDDAAWLTAPPVPVKTYQGENVAGGGETTVEVK
AAYDDDEIYFLFRWKDPTRSLDHLPLVKDGDGWKVLGNGFPTGDENTLYEDKLAIMFDDGDVAQGCAGTC
HLGPRPLPGKPASLNGRGRKYTTDGSEFVDLWHWKAVRSGPLGQADDQYVGPPDDPGRRRYAGGRLDDPG
KGGYVNNWDDDSVTPKRLPDDSKTGSAALGADDLNDGSDWYLLWEDVAVYFDDDADWPVGDVLPGRLLRG
FEGSRADVRARAVWKDGGWTLELKRKLDTGSADDVAFKDGGGYYFWVAVFDDSQTRHRWHSVPLRLTL
>gnl|CDD|187684 cd09626, DOMON_glucodextranase_like, DOMON-like domain of various glycoside hydrolases. This DOMON-like domain is found at the C-terminus of various bacterial proteins that play roles in metabolizing carbohydrates, such as glucodextranase (hydrolyzes alpha-1,6-glucosidic linkages of dextran from the non-reducing end), glucan alpha-1,4-glucosidase, pullulanase (degrades pullulan, a polysaccharide built from maltotriose units), arabinogalactan endo-1,4-beta-galactosidase, and others. Consequently, the DOMON-like domains in this family co-occur with catalytic domains from various glycosyl hydrolase families. The precise function of the DOMON domains in these proteins is not clear, they may be involved in interactions with carbohydrates
LLEFTDPAGDDYGPGTYTYPTDPVFKPGAFDLTGFTVYEAGDKYRFRVKLALLTNPWGGPNGFSLQLIDI
YIDTGSPGGTETLPGLNVEFAPDYGWDYAILISGWWSTVPVPEGEESAADLLAAPSVYADPDGNTITVTV
PKKLLGDNLASWRYYVLVGSQDGFGPDGIRPVAPEGGEWVFGGGDPDGVAPNVIDVLAPSGAQQEEMLDP
YDPSVTRLAV
>gnl|CDD|187685 cd09627, DOMON_murB_like, Domon-like domain of UDP-N-acetylenolpyruvoylglucosamine reductase. UDP-N-acetylenolpyruvoylglucosamine reductase (murB) catalyzes an essential step in peptidoglycan biosynthesis, the reduction of UDP-N-acetylglucosamine-enolpyruvate to UDP-N-acetylmuramate. A subset of these FAD-dependent enzymes contains a C-terminal DOMON-like domain. DOMON domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes; initially DOMON domains were suspected to confer protein-protein interactions. The DOMON-like domain in murB may bind a heme
PQTLALQPFTGYPFPPDLEVSAEQLRSLNGQLFLRWGLRGAPAALLIPLPAAPAGGRRDGLWEHTCFELF
LGAPGQPGYWEFNLSPSGHWNAYRFEGYRQRLEGELSAEPPRIGLTRQPDDLRLGLRLDLALLPPFVRGT
LELGLTAVIEDGDGLLSYWALAHPGAQPDFHDRDRFLLT
>gnl|CDD|187686 cd09628, DOMON_SDR_2_like, DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related proteins. Stromal cell-derived receptor 2 (or ferric chelate reductase 1) reduces Fe(3+) to Fe(2+) ahead of iron transport from the endosome to the cytoplasm. This transmembrane protein is a member of the cytochrome b561 family and contains a DOMON domain which may bind to heme or another ligand. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases
PISYSGCGKTKGCFGLPVGCDPSKDCNFLVTYRVDGDSVEFELSGKTVDDGYVAVGFSDDKKMGDDDVVE
CVRDAGGRVEVRHSYNPGTGNTQGSIELESENVSRDGAEYSDGVIYCRFLRNVVPTVQGNRFDLNSGSYL
LFAAGSASSTGSVQYHSIGSVSSSTPVDL
>gnl|CDD|187687 cd09629, DOMON_CIL1_like, DOMON-like domain of Brassica carinata CIL1 and similar proteins. Brassica carinata CIL1 has been described as involved in suppression of axillary meristem development. It contains a single DOMON domain, the function of which is unclear. Members in this diverse family of plant proteins may have a cytochrome b561 domain C-terminal to the DOMON domain, some members from Arabidopsis have been characterized as auxin-responsive or auxin-induced proteins. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases
FAACNDLPTLGASLHWTYNASNSTLDVAFRATPPSSSGWVAWGINPTGTGMVGTQALVAFRNSNGSVLVY
TYNITSYTKLGEPLPLSFDVSDLSAEYSGGEMTIFATLKLPSNLTSVNHVWQVGPAVTGGSPGPHPTSGA
NLASKGTLDLLT
>gnl|CDD|187688 cd09630, CDH_like_cytochrome, Heme-binding cytochrome domain of fungal cellobiose dehydrogenases. Cellobiose dehydrogenase (CellobioseDH or CDH) is an extracellular fungal oxidoreductase that degrades both lignin and cellulose. Specifically, CDHs oxidize cellobiose, cellodextrins, and lactose to corresponding lactones, utilizing a variety of electron acceptors. Class-II CDHs are monomeric hemoflavoenzymes that are comprised of a b-type cytochrome domain linked to a large flavodehydrogenase domain. The cytochrome domain of CDH and related enzymes, which this model describes, folds as a beta sandwich and complexes a heme molecule. It is found at the N-terminus of this family of enzymes, and belongs to the DOMON domain superfamily, a ligand-interacting motif found in all three kingdoms of life
AYTDPLTGITFSRFSDPDGGFTFGIALPENATSTDSGDFYGQLSAPSSVGWVGVGLGGSMTGSLLFVAYP
DGDGNVTLSPRWATGHVEPTVYTGATVTLLPGTGVNNTHMTANFRCQNCLSWNGGSASATSGSQVWIWAL
SPGLPSDPASATASISFHDGFGGFGADL
>gnl|CDD|187689 cd09631, DOMON_DOH, DOMON-like domain of copper-dependent monooxygenases and related proteins. This diverse family characterizes DOMON domains found in dopamine beta-hydroxylase (DBH), monooxygenase X (MOX), and various other proteins, some of which contain DOMON domains exclusively; the family is not restricted to eukaryotes. DBH is a membrane-bound enzyme that converts dopamine to L-norepinephrine, and plays a central role in the metabolism of catecholamine neurotransmitters. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases
SSLDLDGNFSLSWSVDGEGTITFELSARTTGWVGIGFSPDGGMVGADAVVGWVDGGNAYVTDYYLTGRST
PDVDGSQDLTLLSGSENNGVTTLRFSRKLDTCDPTDLSITDGTTTYVIWAYGSEDPFSLLSYHGSKRG
>gnl|CDD|193606 cd09632, PliI_like, Periplasmic lysozyme inhibitor, I-type (PliI) and similar proteins. Aeromonas hydrophila PliI is a dimeric periplasmic protein that enables bacteria to resist permeabilization of the outer membrane by the bactericidal action of lysozyme. PliI may be a direct inhibitor of lysozyme that inserts a conserved loop into the active site of type I (invertebrate) lysozymes
KIGKALLLPSKQVVVLSEGDLEPASIGSYSVRLYKIKDPAYPLGLFISGEVFPRDGGSVTRAEVADLNGD
GRPELFVYTRSAGSGSYGSVDAYSINNGKSLSLITSPAG
>gnl|CDD|193607 cd09633, Deltex_C, Domain found at the C-terminus of deltex-like. The deltex family of proteins is involved in the regulation of Notch signaling, and therefore may play roles in cell-to-cell communications that regulate mechanisms determining cell fate. They have a central RING-type zinc finger domain and contain a C-terminal domain, described here, that is also found in other domain architectures. Deltex-1 (DTX1) contains a RING finger and two WWE domains, indicating that it may be an E3 ubiquitin ligase. Human deltex 3-like, which contains an additional N-terminal domain (presumably with ubiquitin ligase activity) is also described as E3 ubiquitin-protein ligase DTX3L, B-lymphoma- and BAL-associated protein (BBAP), or rhysin-2. DTX3L mediates monoubiquitination of K91 of histone H4 in response to DNA damage
GNQPPGTMTYHVIDTSLPGYEGCGTIVIVYNIPSGIQGPEHPGPGKPYRGTPRIAYLPDNEEGRKVLRLL
KKAFDRRLIFTVGTSVTTGREDVVVWNGIHHKTSLTGGPSGHGYPDPTYLDRVLEELAAKG
>gnl|CDD|187766 cd09634, Cas1_I-II-III, CRISPR/Cas system-associated protein Cas1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas1 is the most universal CRISPR system protein thought to be involved in spacer integration; Cas1 is metal-dependent deoxyribonuclease, also binds RNA; Shown to possess a unique fold consisting of a N-terminal beta-strand domain and a C-terminal alpha-helical domain
RTLYITTPGAYLSRKGNRLVVEKEDEKKKRIPLEDIDSIVIFGNVSISTAALRLLAENGIPVHFLDYYGR
YLGRLYPPEGGRSVLLRRAQYEAYLDPEKRLELAREIVRGKIRNQRRVLKRYARDGKELLLALAELEELL
EKLDKAKSIEELRGIEGNAAKIYFEALFQLLPKEFRFEGRSRRPPKDPVNALLSYGYSLLYSAVLSAIVA
AGLDPYIGFLHEDRPGRPSLALDLMEEFRPIIVDRLVLSLINKGQIKKKDFEKELGGVLLTEEGRKKLIE
ALEERLKETIKHYLGRKVSYRRLIRLQAYKLAKHLRG
>gnl|CDD|187767 cd09636, Cas1_I-II-III, CRISPR/Cas system-associated protein Cas1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas1 is the most universal CRISPR system protein thought to be involved in spacer integration; Cas1 is metal-dependent deoxyribonuclease, also binds RNA; Shown to possess a unique fold consisting of a N-terminal beta-strand domain and a C-terminal alpha-helical domain
LYVLEYGSYLSRKGNTLVVEKEGELKKNIPVANVDCIVIFGGVSISSAAIRELAKRGIDIVFLGGDGNYL
GRLYPPEPGSSVFTRRAQYKAYLNPAKRLKLAREFVEGKLANQAALLRYLTRRREDLKSELAEYIAELLK
ELDNANSIEELMGIEGNAARAYYAALAQLLPDEFGFNGRSRRPPKDPFNALLSYGYSLLYSNVLTAIYIA
GLDPYIGFLHTDRSGRPSLVLDLMEEFRPQIVDRLVFSLINRGIITPEDF
>gnl|CDD|187768 cd09637, Cas4_I-A_I-B_I-C_I-D_II-B, CRISPR/Cas system-associated protein Cas4. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas4 is RecB-like nuclease with three-cysteine C-terminal cluster
ITGSDVLEYAYCPRKLWYMKCLGISERPTESMELGRLIHERAEVALKARFGVREEKEVPLKSKKYGLKGV
IDIVLKEDGELVPVEVKSGRAGSPREAHKLQLVAYAYLLEEMYGKRVARGYIVYLEGGKRLEVEISEELR
KKAEKLLEEIRKLLEGELPPPVKSSPKCKFCPYREICL
>gnl|CDD|187769 cd09638, Cas2_I_II_III, CRISPR/Cas system-associated protein Cas2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas2 is present in majority of CRISPR/Cas systems along with Cas1; RNAse specific to U-rich regions; Possesses an RRM/ferredoxin fold
MLVLVVYDIPEDTERKRRRKLRKLLEKYGLFRVQYSVFEGILEPNLLASLIERLKKIIPDEDSIRIYPLT
EKQKTAIRILGGEAEVNAEP
>gnl|CDD|187770 cd09639, Cas3_I, CRISPR/Cas system-associated protein Cas3. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
LLVIEAPTGYGKTEAALLWALHSLKSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSILSSRIKE
MGDSEEFEHLFPLYIHSNDTLFLDPITVCTIDQVLKSVFGEFGHYEFTLASIANSLLIFDEVHFYDEYTL
ALILAVLEVLKDNDVPILLMSATLPKFLKEYAEKIGYVEENEPLDLKPNERAPFIKIESDKVGEISSLER
LLEFIKKGGSVAIIVNTVDRAQEFYQQLKEKGPEEEIMLIHSRFTEKDRAKKEAELLLEFKKSEKFVIVA
TQVIEASLDISVDVMITELAPIDSLIQRLGRLHRYGEKNGEEVYIITDAPDGKGQKPYPYDLVERTIELL
EEG
>gnl|CDD|187771 cd09640, Cas7_I-C, CRISPR/Cas system-associated RAMP superfamily protein Cas7. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas7 is a RAMP superfamily protein; Subunit of the Cascade complex; also known as CT1132 family
VENRIDFLVTLDVKEANPNGDPLNGNMPRTDAETGYGVVSDVRIKRKVRNYLQDMGKSIFVQTKERIEDK
FRSEKRFSQHFTAKTGDKEIEEKACAKYIDVRAFGAVITYLKKSIGVRGPVQISMAKSLEPVVISSLQIT
RATAGMEAKNQRTMGTKYFVPYGLYVLYGVINANFAKKTGFSEEDLEAFKEALVNGFENDRSSARPEGEM
RYCVVVVFEHSSELGNDISARVFDLLELKQSIESKKRTYKAYEVHVNN
>gnl|CDD|193608 cd09641, Cas3''_I, CRISPR/Cas system-associated protein Cas3''. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; HD-like nuclease, specifically digesting double-stranded oligonucleotides and preferably cleaving at G:C pairs; signature gene for Type I
AKSGPWQPLLEHLLDVAAWDAELAEEFARKLGLELGLSRELLALAGLLHDLGKATPAFQKYLRGGKEALR
EGKRKEVRHSLLGALLLYELLKELGLDEELALLLAYAIAGHHGGLPDVLLLLDEDDESALKERLEELDEE
KLLLELWEEELEELLDELLKELLLLLLPELLSFELYLLLRLLFSLLVDADWLASAEFFFP
>gnl|CDD|187773 cd09642, Cas8c_I-C, CRISPR/Cas system-associated protein Cas8c. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; signature gene for I-C subtype; also known as Csd1 family
MILQALYDYYERKLEQPLLLPIGFETKEIPFFIVLDEDGQFLRLEDTREGEGKKKRPGSTLIPCPEKDRS
GGIAPNLLWDNLSYVLGDFAKFGGGVEERDAALFIEALRELAETKDEGLKAVLDFLDSPEVEDLKAAPAL
ATEIDLPGANLAFRVDGAPGIVHEREAVQAFWARHLAESELGERGICLVSGEEGPIARLHPKIKGVQPDG
AKLVSFNNSAFESYGKEQGANAPVSYEAAFAYVLALNYLLRKESRQKIQIGDATFVFWAEDDSTEEDELF
LSLEEPPDDDLLPDSRAATALDDRAGKRIKKGQPLRLDDTRFYVLGLSANAGRLSVRYWRSLTVEELLEN
LERHFEDLEWEPRPKDDGSPSLFDILEATYGLGKVENVPPDLAGRLLRSILDGGPYPRSLLSAALRRIRA
DVAYREEWYKRLALLKACLNRQNRRGKKKKELTVALDKTNTNRAYLLGRLLAVLEKLQERALPGELNATI
ADRYYGAASSTPAAVFPTLLRLLQHHLSKLGKNGRWINLERLKGEILELLDGEFPVTFNLPLQGRFALGY
YHQRAALFTKKEAE
>gnl|CDD|187774 cd09643, Csn1, CRISPR/Cas system-associated protein Cas9. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Very large protein containing McrA/HNH-nuclease related domain and a RuvC-like nuclease domain; signature gene for type II
EYILGLDIGIASVGWAIVEDDYKVPAKKMIDCGVKIFTGAELFKTGETAALDRRLARGARRRIRRRKHRL
LRLQELFAREGSLTDFDFFSRLEDSFLEYHKNYPTIYHLRKAALENKLKPDELYLALLHIIKHRGHFLIE
GDEDTTADKETGALLSASMIKRYDEHKADLRKLKELIKKEFFKKYKEIFGDETFLRNQRGFYNGSIPRQL
LLEELEAIFRKQREYYPFEKILTFRIPYYIGPLAEGKSEFAWLTRPALSEAFIEKMTGKCTYLPEEKRAP
KHSLLAEKFTVLNELNNLRIIEEQGETKILSKEEKQELLDLLFKKNKLTYKQKRKLLGLKEEEIFKGLRY
EGLKAEKNFNISLKTYHDLRKALGKEFLKDLELNEKILDEIVKILTLYKDREMIEKILELYKDLLNEEQL
KKLLKRHFTGWGRLSLKALRGIRPLMEQGKRYDEAILELGGNHNQKINSDELKFLPIIKKAQVKDEILNP
VVKRALLQARKVVNELVKKYGPPDKIVIEMARENGTNKGTKNRKKRQKKNEDNIKEAASALEQKLKELPL
DIKSKNILKLRLYYQQNGKCMYTGKEIDIDDLFDLSYYEIDHILPQSRSFDDSISNKVLVLASENQEKGD
QTPYEEIVSKMSAFWNKLEAAKLISQRGDSKKDRLLLEKGISDDEKAGFIDRNLNDTRYITRVVANYLKD
RFNFHLKKRKVKVVTLKGQLTSQLRKKWGLYKKREINNYHHAHDAYINAVVTNALVKKFSQLERYKEYKR
FDSEKGNKKTLDENKKFFFANPMNFFKQE
>gnl|CDD|213407 cd09644, Csn2, CRISPR/Cas system-associated protein Csn2. Csn2 is a Nmeni subtype-specific Cas protein, which may function in the adaptation process which mediates the incorporation of foreign nucleic acids into the microbial host genome. Csn 2 may interact directly with double-stranded DNA. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Csn2 has been predicted to be a functional analog of Cas4 based on anti-correlated phyletic patterns; also known as SPy1049 family
MKLVYSDLEKEIEIEENRVNTLVIENPELFRRIILELVSQIEGAEGPFILSDDDKEVSIKKYLEIITDPF
NLDINSKKLLNKLYKRLEKELLEEELYEETQELKSALSSFLEKLGLSLPYELEFEEEIDMQDLLKAFGFK
IEESYDSLLENLIDYLKILSELLKKKIFVFVNLRTFLTEEELEELYEHALYNKIKVLLLENSLDRDLSDY
ENKYIIDKDLCEI
>gnl|CDD|187776 cd09645, Cas5_I-E, CRISPR/Cas system-associated RAMP superfamily protein Cas5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas5 is a RAMP superfamily protein; Subunit of the Cascade complex
LLLRLAGPLQSWGEVSRFGRRDTGDFPTKSALLGLLAAALGIRRDEPERLLALLRFTILSYRDYLADAVF
TVALTEGAEPLLEELAAALRSPVFPLYLGRKSCPPARPLFLGLFEADAPEAALALLPAPALRVRQRR
>gnl|CDD|187777 cd09646, Cas7_I-E, CRISPR/Cas system-associated RAMP superfamily protein Cas7. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas7 is a RAMP superfamily protein; Subunit of the Cascade complex; also known as Cse4/CasC family
TFIQIHLLQSYPASNLNRDDTGAPKTAVYGGSTRTRVSSQSLKRAWRLEAHAPLLGGHGGIRSRRLATEL
AKRLLELGYDEDIAEPDAAKIAYGLKKASGKKSDKLLLLSAPEAAWVARYAAELADEFDAAAAADAVADK
ELDKNFKEDLAAARLPQGGVDIALFGRMLASLPEANVDAAVQVAHAFTVHAVEVEVDFFTAVDDLKKEED
SGSGHMGETEFSSGTFYRYANIDLDQLVENLGGDRELAAQAVEAFTYALAEVVPGAKQNSTAAYNPADLV
LIEARDDQPLSLANAFEKAIKADRGQLLPAVQALNGYLEKLAAVY
>gnl|CDD|187778 cd09647, Csm2_III-A, CRISPR/Cas system-associated protein Csm2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Small alpha-helical protein; signature gene for subtype III-A
LTTTQLRRFYDELRRIEEKIGTEEKKNEDITAELEMLKPKLAYAVGREGVREFEGFVELLEDLLDKIDKI
DNDRNAFERFVKFFEAIVAYHKFYG
>gnl|CDD|187779 cd09648, Cas2_I-E, CRISPR/Cas system-associated protein Cas2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas2 is present in majority of CRISPR/Cas systems along with Cas1; RNAse specific to U-rich regions; Possesses an RRM/ferredoxin fold
MLVVVTENVPPRLRGRLALWLLEPRAGVYVGGVSASVRERIWDYLAQHCPPKGSLVITWSSNTCPGFEFF
TLGENRKEIVEIDGLPLVIRALP
>gnl|CDD|187780 cd09649, Cas5_I-A, CRISPR/Cas system-associated RAMP superfamily protein Cas5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas5 is a RAMP superfamily protein; Subunit of the Cascade complex
IMVLVFLLLHWGFSVRYPEASKVRPSLPLPPPSTLIGALAYGLARGGDGKGETSGEKRKALKGRNELFAV
ATKKAESVLAPYSDILRILVVKLSEEEKELLEKALWLITRLGSKESLVSVEDVEVVEAEKSEKGPVETIY
YFP
>gnl|CDD|187781 cd09650, Cas7_I, CRISPR/Cas system-associated RAMP superfamily protein Cas7. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas7 is a RAMP superfamily protein; Subunit of the Cascade complex; also known as MJ0381 family
TPVNNHSLNGGETEGNISSLKKVRVGDGRVVPYVSGEALKHALRVILVEDLFGFMSAKKGGTVRRTSPVK
VSYAISITPFIGDADFHVRIALANNSSKEVGEGQMPYETEYHSTLYAYSFFLDLDRIGVPESFEEKDFYV
LPDEERKKRVKALLKALPPLLGGNIGANLTDFSPVFVVFSLVVRKSPKF
>gnl|CDD|187782 cd09651, Cas5_I-C, CRISPR/Cas system-associated RAMP superfamily protein Cas5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas5 is a RAMP superfamily protein; Subunit of the Cascade complex; in subtype I-C this protein might be the endoribonuclease that generates crRNAs; also known as DevS family
IRLKVWGDYACFTRPEMKVERVSYDVPTPSAARGILEAIYWKPAIRWVIDEIRVLKPIRTESIRRNEVGS
RARVGGLPLLIEEGRQQRAYTYLRDVAYVIEAHFELNEHAPADDRVEKKHEIFARRARKGQCFHDPYLGT
REFPAYFEPCDFGEGEGAYDNGGERDLGWMLHDFDFPDEELTPRFFRARMKNGVIKVP
>gnl|CDD|410980 cd09652, Cas6, Class 1 CRISPR-associated endoribonuclease Cas6. CRISPR-Cas (clustered regularly interspaced short palindromic repeats and CRISPR-associated proteins) adaptive immune systems defend microbes against foreign nucleic acids via RNA-guided endonucleases. These systems are divided into two classes: class 1 systems utilize multiple Cas proteins and CRISPR RNA (crRNA) to form an effector complex while class 2 systems employ a large, single effector with crRNA to mediate interference. Cas6 family endoribonucleases are typically found within types I and III CRISPR-Cas systems and are metal-independent nucleases that catalyze RNA cleavage via a mechanism involving a 2'-3' cyclic intermediate. They share a common ferredoxin or RNA recognition motif (RRM) fold, and they recognize and excise CRISPR repeat RNAs that vary widely in primary and secondary structures. Cas6 is also found in the rare type IV system that includes rudimentary CRISPR-cas loci lacking the adaptation module
IFKIEVKLIPLDDVILPTPYPKYLHGLIYEGKLSIEPKNLIHERKKYKPFAISHFIMNKRRIFQTNKTIL
GGSKLSFYISSSTQDITDAVLERLLKGPEVRLGYGKFHVTIIKIIKVEVEKLKEEVEKHGNDGFTISFLS
PTAFKSVVLGKAGYVTPPSVGLIIKSLYNKYCRLIGKKPEEVEAFLSDSNALSRIIGYDLQPKRFRIGEL
RYIRGFKGKIRFDGPDEKLKRLALYLLRFGSYSGVGEKKGLGFGMIKL
>gnl|CDD|187784 cd09653, Csa5_I-A, CRISPR/Cas system-associated protein Csa5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Predicted transcriptional regulator of CRISPR/Cas system; contains DNA binding HTH domain; also known as Csa5 family
FFLYSESFTYVDRIGNALSKEAVEFALYEAQRALRSGIETAMIDEKGYRYAEKEGRKILVGYLPTDKEVE
DFLREVREDIEYAKLVAALALAYPSRT
>gnl|CDD|187785 cd09654, Cmr5_III-B, CRISPR/Cas system-associated protein Cmr5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Small alpha-helical protein; signature gene for subtype III-B
EQERAKLAIKVVEEVEKSLDKFREKYRSRVRKLPSMILNNGLIPTLAFYLSKAENCTLNKFVSDETSYTK
YYAHILYWLKERNLKTGVDNALKELMEKDYSEYRIATEEALRYLNWLKRLAEALLKE
>gnl|CDD|187786 cd09655, CasRa_I-A, CRISPR/Cas system-associated transcriptional regulator CasRa. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Predicted transcriptional regulator of CRISPR/Cas system
YIFTVGFDEKFIIRALMEIGIKDVSVVLIVSSIVDGARRAVESLRAIISDLGGFVEGTTKEIELKDPFSI
VRQMVDIIKEEREPRVIINLSGGMRTLNVGALLGAAALKKVVVRVEYESEEEIDFIELDLVPLLAGLSRE
ELKILEVLKAKGEKSVKNIAKKLGKSLSTISRHLRELEKKGLVEQKGTKGKRYSLTKL
>gnl|CDD|187787 cd09656, Cmr3_III-B, CRISPR/Cas system-associated RAMP superfamily protein Cmr3. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; This protein is a subunit of Cmr complex
FFRSSRPFDAGNVSVVSSIFPSPTTIAGAVRTALLEKAGKKLDVIDDLEEPYFPIYGPFVVEKGPGFFPL
PSDINFTEKEEGGLAVDRSLEKTPKPPIEGDDSETTPGYLSESKLSKYLAGNISELHTVDGEEEIFKKEE
RIGIALDRERKVVKEGALYSQRFLRFKDDVGFIVWVEDPEIKDISPGRIVGLGGERRLAKLEVDEDNEDT
FNPEIEPEGKYVKFYLLTPAIFIEGGVLSDLKGLLCEVEIFAVLIDKRKQIVSGWDYVEKKPKPTLEAVP
PGSVYFFKAKEEVPEDNEPLIKLGKFHKIGYGLAIIGE
>gnl|CDD|187788 cd09657, Cmr1_III-B, CRISPR/Cas system-associated RAMP superfamily protein Cmr1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; This protein is a subunit of Cmr complex
VAEIELEIITPIFGGGARGRSEEEVRSTSIKGLLRWWFRALAGGYKGDNLQKLKEAEREIFGSTNRKSRF
RLEVEDNNTLRILLEGNDKKIIAFINNLLIEKKKLLRLDILSNFGGIGARSRRGFGSIEIKS
>gnl|CDD|187789 cd09658, Cas5_I-B, CRISPR/Cas system-associated RAMP superfamily protein Cas5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas5 is a RAMP superfamily protein; Subunit of the Cascade complex
LRVEAFQLFAHFRIPFTIKYLDTYPLPPYSTIIGMLHNILGLRGEYSPFSMSVQGKYESIFEDYQTFIEE
VSYNYKNKSSPSSPVTRQSLYNPRIYIFLAGDERIIEEVYESLLNPKFVPSLGRSEDLVRIGKVRYVEVV
DVKKEKFDTYRSVIKLSGGKYRMPSRRKVDLVPKVGERYVK
>gnl|CDD|187790 cd09659, Cas4_I-A, CRISPR/Cas system-associated protein Cas4. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas4 is RecB-like nuclease with three-cysteine C-terminal cluster
LLRLRRRGAPDPVSEELRGWNWNEPPVKPRYYLGLSLSDIAYGYCPTGRDVYLKRVLGVRGEVNAGLLLG
QAIHEAFAKALEEVKSLNYGAEPPSYLLESVNADVFYRSEVGAELEYTLSLCYSAYLEKARKPFSDSAGF
LSIPVAVEYRVDGSPLGLSDRVRVDALDYINVVVEVKVGSYQEFHALALAGYALAIESDLEIPVDYGLLI
YINVNGGRVEIKARLVYISDDLRTEFLEERDRAIEIVFNGSDPGLAKKCSPTCPFLEHCH
>gnl|CDD|187791 cd09660, Csx1_III-U, CRISPR/Cas system-associated protein Csx1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; Some proteins could have an additional fusion with RecB-family nuclease domain; Core domain appears to have a Rossmann-like fold; loosely associated with CRISPR/Cas systems; also known as MJ1666 family
MKILIAPWGNPKGWQKVKYSINGKKYESNSSLKAIKELLKPDKVIIIVPDSLANNYSSNKEDIELESIKE
KVIEFLKELLTIKNSDVIVLPGVGSFKYIKFEGKPLDYFSYAYYHLLKILEKENINEIYLDITHGINYMT
VLTYEAIRLALGLLALEKEVKLELYNSDPYPKGYSAILHIHEIEEIEIRPSLPQLKNVDGKILNKYKGAQ
KNNFNIFFSSIINATPLVASTFYPDARDVEIYLKIKLERFIRELSYGEPKVERSYVAFKEDYLTILKLYF
HSLLLEILKFIDYKNEVKLEEIKKLAETFFDKIEVTRVIIENEVDKIEKGQNWSEKSELLARIYSEIMER
KISGFDKRNFLAHAGFEYNVVYVKKENKKLYLRYNDSKKEKIEN
>gnl|CDD|187792 cd09661, Cmr6_III-B, CRISPR/Cas system-associated RAMP superfamily protein Cmr6. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; This protein is a subunit of Cmr complex
NKLNENFGKVEKLIKSIREALESKLNNLCVIEFKLKTSSRLLVGLGTPHVYETGLTLDPIYGLPYIPGSA
IKGVLRSYTFEVLAREDYEEKDTVQKEELASKLFGSQEKEGELIFLDAYPIPDENKSIFELDIINPHYQP
YYQEEKPPGDWVNPIPIKFLTVKKGVTFQFVVEFDDLGLNLLDKLEKLLKKALKEFGIGAKTSLGYGRFE
>gnl|CDD|187793 cd09662, Csm5_III-A, CRISPR/Cas system-associated RAMP superfamily protein Csm5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein
VTLEVLTPLHIGNGEEYTPVDYIMHVEGDRIYVIDFEKLYADLLEKKRKDEESGDNNRDYAGSNAELKEV
LEEVKLDPAKYRDYSSKIGIPEPRKASRHKKFIKPLGRPYIPGSSIKGAIRTALLWNYLKKNTDLLTRVP
NHLQKDLRQYGRAFERKELKKNGISNTIPKKIVNDVFRALKVSDSRPLRTSRLIVHRIKLNYNGRPILPF
YREFLDSGTTFSFNVKIDREELKRGLDRENERYLPCLPFNKLIIIKINDASDHTKNEEAETELSDVQKAY
EEFRKLEKEVNNKVGEILHIGWGGGLRSKTIGILLDDEDGKLVALFGKVRKALGLGKKPLTNKLSLRFPK
TKRVINGKPMGWCKL
>gnl|CDD|187794 cd09663, Csm4_III-A, CRISPR/Cas system-associated RAMP superfamily protein Csm4. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein
LVKLKFKSSFHYGIILHSDTIFSAIINAYIKLYGREHVDKLIEKFKDDSPFRISSLLPYIGNTYLVPKPL
HNALSDLNLLEKKKKKLKKISYIPIDELESWLSGEADEKKQLKNITKIKTEGNGDNKGKPHKVLIEEPKV
SIDRIEIKSNLYFVEDIFFKENFGLWFLADYSDESFEKLLEAALKLLEDFGLGGKRTTGYGLFNVEIEDN
PLEEPNGEGYMTLSLFIPDDDELESDTELARYRLVKRRGFNIDGTKPKKQIRYFAEGSIFYLKFQGKVKD
VSLILNGQTSVYPYGFPITLP
>gnl|CDD|187795 cd09664, Cas6_I-E, CRISPR/Cas system-associated RAMP superfamily protein Cas6e. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas6e is an endoribonuclease that generates crRNA; This family is specific for CRISPR/Cas system I-E subtype; Homologous to Cas6 (RAMP superfamily protein); Possesses double RRM/ferredoxin fold; also known as Cse3 family
MYLSKLTLSRADLAAALRSADPYSLHQWLWSLFPDVEAEKRQFLFRDEGGDAKGGKVLVLSARPPLQSAY
AFVIETKPFPPELLQGQFLKFRLRANPTKTILGKRKRLDSKGNAEGKRVPLKTQAEAAAWLERQGQTGGF
RLVEPERLDVQALQQQQFSRKQGDRTITFGSVDFSGMLTVEDRDLFIDSLNQGIGKSRAFGCGLLLIKPL
>gnl|CDD|187796 cd09665, Cas8a1_I-A, CRISPR/Cas system-associated protein Cas8a1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; signature gene for I-A subtype; also known as CXXC_CXXC family
CINCGERHAKKDTIFDTGISLFGGLNGDVPNFFWNGKPKAPLCEICEFIYFFYFRGLTLLLKHGKPPFLF
VNSDTSAISLVSLNLLLNSKLKYKLPENILFELFTEVVLKSEEEKARENLQNIYIIEYDLTNEIRMPKIY
SFNISRRKAEFLKNAKEKDQKNWESIVYRKEHQDKIKKEVDEKILGNSLYFKLLNGSILKYFIKNAKRSK
YYDTNLLPYYLTELNLLYEEFLQKIKEVGDSMSETIKELWRIYNLGKKLAKRLRELEAENKIKSFAYKLL
NALRIRDRLGFMDSLLRLYMFYELEIPYGFVKAISWKETFNLLGYSFLNGLLGR
>gnl|CDD|187797 cd09666, Cas8a2_I-A, CRISPR/Cas system-associated protein Csa8a2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Zn-finger domain containing protein, distant homologs of Cas8 proteins; signature gene for I-A subtype; also known as Csa4 family
VCEFYTPGHNLILDTLIMYGIVESLARSGVVEGEVEPVGERYVIKVDADNCHLESIELALRGLQEALEEV
LSGHEATGRARSSKEGNKILSNTRISAGANINNVNADILPKTLEKIHKNLEGKRLSKKGLVTVPLTLMPL
YGKYMTKSLGVKGGKPIKVCPLCYALAWIGFHYYSPYIKYQKGDETKVVILQPAPAEEVDMIELLLLKDL
ASKIMPYILFHFRISNELALLYHLLYTESLGETELVTESHFEVLSYTLEVSGNNQRVRDFGELDLGVLMD
FIAYLKARDFYSWPKFVDFLARRDPEISLQLTDAILNGDEEAFYTALRELKKSGVRYDPEQVDALAEILA
ER
>gnl|CDD|187798 cd09667, Csb2_I-U, CRISPR/Cas system-associated protein Csb2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Duplicated RAMP domains; also known as GSU0054 family
GALSGAPYRLYVPNNDADAVAGAWSSGPTRVATLRVEKDIRPRHLDADPPLHYLWDFDEEPAHYLEQIGS
IARSITHLGWGVDMAHGNAVILDEEAAHRLDGEGWLPAATRGATQLRVPTNGSLDALMARHEAFLNRLSA
GGFVPVPPLTVFDIIGYRRDIDPPARAIAAFRLLLYDISKSDPLFDAPQKLLKVAGMVRHLAGAAAQRCR
WLPSPIASLVEGHFESRLQTDPQRTSRFAYLPLPSIEFRGDRKAVGAIRRVLVAAPAGCGEEVDWIRRAL
SGRDLAKGAPDKGGLLSLLPASDKMLRRYTKAASTWATVTPVILPGGDDWGPGGGFARSKAEALLRKAVV
DAGFHEGVAENAAEIEWRRVGFWAGADLASRFAVPDHLPAPRYHVRITFAAPVRGPLCIGGGRWYGLG
>gnl|CDD|187799 cd09668, Csx1_III-U, CRISPR/Cas system-associated protein Csx1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; Some proteins could have an additional fusion with RecB-family nuclease domain; Core domain appears to have a Rossmann-like fold; loosely associated with CRISPR/Cas systems; also known as TM1812 family
TFISFLGVGDTDYKRQYKTAVYKFIDGIECPFVLFVLIEKLKPDKVIVVGTRFSMWAKVYEYYASEDYVL
LLIKVAGESRVDNEALSEEDLKLIEKVVDPYLIELIPNSVDGSEQWDLFMSLTNEVDHGDEIYLDITHGF
RFLPVVALAAIEYLRYVKNVKVEGVLYGALDMNSELGHSPIVDLKPMLEISDWVEGLGRFVTYGDSYVLA
KLLE
>gnl|CDD|187800 cd09669, Cse1_I-E, CRISPR/Cas system-associated protein Cse1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; subunit of the Cascade complex; signature gene for I-E subtype; also known as Cse1/CasA/YgcL family
NLLDEPWIPVRFPDGRIEELSLRDLLDERDVVELALPRPDQEGAALRLLLAILQRAFAPKDTEEWEDIWR
EGLADKLRKYLNPWRDRFQLFHPTPPFMQDADLLDEKDGGPVAKLLAELPGANNHKFVFKRGSGESLCLG
CAALALFSLQTNAPSGGGGYGVGLRGGGPLTTLVAGQETGATLWETLWLNLVPQEPWEDDLPSGFDWLPW
ERTSEVAGELIPALSLGPLDAYTWMPRRVRLDDETGESLLVGDGKNYGLNYTGGWPHPLTPYRVPVKKGN
EPKAVKVSPEGLLWRDLDSLLLTRGSQNNREPAAVVDGASELRSALVRLWVFGQGFDNAKARCVYSRHFP
LPGNSEWQKLAAIAVGAAVQILEILRNALKNAVFALAEAAKGDFERAGLSFWNEAEERFYWQWLDGAFPQ
LAGADEALPEWLDALWLLARQLFDEYVAREPYRAIDAWRARAAARKDLYKSLRKLKA
>gnl|CDD|187801 cd09670, Cse2_I-E, CRISPR/Cas system-associated protein Cse2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Small alpha-helical protein; also known as Cse2/CasB/YgcK family; specific gene for I-E subtype
ALYEALERLDGDRGARAALRRGLPPELADLPAGFRFLWQYLTGDNPETERRAYLMVAALIALKDQSRHRE
GISLGRALAELGRSSSDVSERRFLALLAADRPELLRRLRRLVRLLRSKAISVDYAQLARDLLRWNHPSER
VRRRWARDYYRA
>gnl|CDD|187802 cd09671, Csx1_III-U, CRISPR/Cas system-associated protein Csx1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; Some proteins could have an additional fusion with RecB-family nuclease domain; Core domain appears to have a Rossmann-like fold; loosely associated with CRISPR/Cas systems; also known as DxTHG family
ILIAPLGDPRGWVVVKYSFNGKAEESKSSPLAIVEYLKKDKIKIEVIEELSKEDVENNGYDEDKKKLEEE
LKEFSIEPAAFVVGGSYNKIKLEGIASDIYYLYLLYNLLESLEKEKIDEIILDVTHGFNFMPLLAYEAVR
YLLEVKAVNKKVKLEYYNSDPYTKGNVQIPLLDLIEIQEILFISSGVAKLGYYLIKKDYKEIERKLESDS
LPIGEIRSLERRALSIKAIRNGLPLLFYAFDTKKAKIFIPELDELEDKLNKVLNLIRKQFENELAKVNIE
REKKLLSLYLMYLLRDIYSLYKAYFNRFVLKTPKLEKKLEEIRKISEMLFRKEYDKLEQLRNFVAH
>gnl|CDD|187803 cd09672, Cas8a1_I-A, CRISPR/Cas system-associated protein Cas8a1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; signature gene for I-A subtype; also known as TM1802 family
MLENIKNIGKIVRTTSAEDYDEDLMVEEKSGDYLVIIDLNLNSEKINIYRRDFDKQEKVFLYRAKGNNGQ
DFLPTTYKICSAKAGNGSSIVKLFDVLLGGTLKNLLKEVKDKLFKNKEKVRYCLDLSKIGNGEITIKIDG
KFLKEIENLWKIIEEKLGLKKKKIEGTCHLCGERSDITYDSFVYKFYTTDKPGFSSDKGFSKNFSICRDC
YKDVIYGRKFIQENLSTRFGGNDLWIIPGLFFNGKELKESWIRISREFKKSTFNLKFEERIERNIINYLE
FKDGGTVDFLFYEKEKSAEKIKLYIKDVHPSRVSKIRESIKKVENEIFGENWFLEDNFFVIPIFLGNVSK
YFKMLDLYEDIFLEGKIDKDLLLDYFVSKIKVDFFEGFNTKMVANTDMGFIVKLGLLLKLFEKLNLITGG
DSMPKFEDDKDFFEYISKFFDSPEKKALFLLGYLIGELLYEQISGRDLSAKKKNLNKLKGLKISAKDLIG
LLNEVFEKLDQYGGYNEGTFELMKSTSKKLLKAGKWSLSEDEIVYYFVSGMALNT
>gnl|CDD|187804 cd09673, Cas3_Cas2_I-F, CRISPR/Cas system-associated protein Cas3/Cas2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas3/Cas2 fusion; This protein includes both DEAH and HD motifs for helicase and N-terminal domain corresponding to Cas2 RNAse; signature gene for Type I and subtype I-F
MNILLISQCEKRALTETRRILDQFAERTGDRVWQTPITQEGLKTLRKLLRKTARRNTAVACYWIFGMNRS
ELLWIVGDKRRFNHQGAVPTNSTQRDILRALDENEWVSAESISLLAGLAGLLHDIGKASVHFQNKLSPEM
NGPKIADDYRHEWVSLRLFQAFVEGCTDNGWLWRLAWKNLDDGTDKFTLKDRQERDQGIQFSAALPPLAA
VDYWLVTSHHRLPVEEALKNDPLALPHYENHARTLVPSLEQIWNPAVGWVGNGTTPQAWWFPQGGPLQDA
IWKKHQARMAKLALLIPKLKTDQLLYWKFLALHSRLALMLADHHYSAQQYSLQWQELNVALFANTKLKNI
DQDKKAKLQKQPLDEHLIGVGQRALRIARMLPDLSRELPAIQTHKYFCQRSAHPRFRWQNKAFNLAQKLR
QKSPEQGAFGVNMASTGCGKTLANARAMYALRDDKQGARFAIALGLRSLTLQTGHALKTRLNLSDDDLAV
LIGGTAVQTLFDLSKEKIEQVDEDGSESAPIFLAEGQDCNLPDWDGPLDTIELLGRLSLDDKEKTLLAAP
VLVCTIDHLIPATESHRGGHHIAPMLRLMSSDLILDEPDDYEPEDLPALLRLVQLAGLLGSRVLLSSATL
PPALVKTLFRAYEAGRQMYQALYGQPKKPLNICCAWVDEPQVWQADCNQKSEFIQRHQDFLRDRAVQLAK
KPVRRLAELLSLSSLKPRNESTYLALAQSLLEGALRLHQAHAQTDPKSEKKVSVGLIRVANIDPLIRLAQ
FLYALLAEEKFAIHLCCYHAQDPLLLRSYIERRLDQLLTRHKPEQLFQDDEIIDLMQNSPALNHLFIVLA
TPVEEVGRDHDYDWAIADPSSMRSIIQLAGRVNRHRLEKVQQPNIVILQWNYRYLERRDKQRRPVYIRPG
FETYRVSRLSTHDLDQLLELLPYDHISALPRIARLRFLQPGTLFADLEHEQIKDFLNGYFADQGLQLASR
WDRKAAILTANLYRITPFRESNYQEEYMFELAESDEVDKQVFGFLEKATKNLKYRKYGLVWEDVKLEEAA
GKSPWWLASTLQQLKDLAEELNIALEEGCRPFGCVSLPYNRDEVPTWHYHPGLGVF
>gnl|CDD|187805 cd09674, Cas6_I-F, CRISPR/Cas system-associated RAMP superfamily protein Cas6f. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas6f is an endoribonuclease that generates crRNA; This family is specific for CRISPR/Cas system I-F subtype; Possesses RRM fold; also known as Csy4 family
MNHYLDITLLPDAEFSQEVLMNACYKKLHRALADYETGRIGVSFPLYGQETLGRQLRLHGTAEDLDKLHS
RRWLSGLSDYASISEISTVPADTSHVRTVRRKQTKSSAARLRRRLERRQGINDEEARPRAPDKTTQRANL
PYLSLKSASSGQRFRLFIEQGELAPESVTGKFNAYGLSNTATVPWF
>gnl|CDD|187806 cd09675, Csy1_I-F, CRISPR/Cas system-associated protein Csy1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins; Predicted subunit of the Cascade complex; signature gene for I-F subtype; also known as Csy1 family
AKYRPDIWLTDAARRAGQLKLGTHISKGIHSDSRGSNVFFSEQKVDHDYVGSHTLANNALDVVGNAAALD
LVKLLQWEHEGGSLRALLWAGDPRLLRCFADDPELSEQWQTTFQTILTANRNPASHKLAKQLYWPLPPTS
DNRDNYHLLSPLYSSSLTHAFYQRIEAIRFSEENKNARQARRKSVWHQKRYADYLDLAVQKLGGTKPQNI
SQLNSSRKGRSYLLPSLPPVWKNIDKPPIKFSSILESRFFSKSLARRTLDQLKILLLVVKPKENNYDIRN
MRLAALDQIIEQLLSIVAEIQNLPPAGWSKDCDLKRAEQYWLDPKRADLDEVFKAEREKGDWDQEVEKDF
ARWLNKRLQHDRLEFGDVEHHEWRREMLFKIRER
>gnl|CDD|187807 cd09676, Csy2_I-F, CRISPR/Cas system-associated RAMP superfamily protein Csy2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; predicted Cas5 ortholog
LIVLPRIRVQNANAISGPLTYGFPALTAFTGFMHALSRKLGASHGLTLHGVGVACHGQQLHTYGSAQRWD
RVFILTRNPVTKNGKTAAIIEEGRCHLTVSLVIGVSGQDIAVFEASQALPEHLKHALQQQRLAGGTVIEI
LAVTVINFYEAETRALLRRLLPGFALLDRQDLLAEHTQRLQQTNPQATALDAWLDFAALKHIPERAQSND
TVWSWSVKKGRGWLVPIPVGYQAISPLYAPGQVDNARDPHYPFQFVEALYSLGEWVFPHRIVDIDQLLWY
YHDAQNDLYLCR
>gnl|CDD|187808 cd09677, Csy3_I-F, CRISPR/Cas system-associated RAMP superfamily protein Csy3. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; predicted Cas7 ortholog
KLPSVLSFERKLDPSDAIFFAGNWDGKDEVTPLPIREKAVRGTISNRLKKYKYDTQIDDPAKLDAEIQKP
NLQRVDVAALPYDADTLKLSFTLKVLASLAKPSKCNDAEYKQTLLQTVKLYIEEQGFEELARRYAENIAN
GRWLWRNRVGAESIEIRITAWPEDEKAIWPFDAIRFNLRGFAQPSKDLDALAKLIAQGLSGENGFAILEV
TAYVRLGTGQEVYPSQELVLDKSKGKKSKILYAVNQIGSSAALHSQKIGNAIRTIDTWYPDADENDPIAI
EPYGAVTELGKAYRQPKTKKDDFYTLFDNWVLKEQVPPVEQQHFVMAVLIRGGVFGEKG
>gnl|CDD|187809 cd09678, Csb1_I-U, CRISPR/Cas system-associated protein Csb1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; Contains several motifs similar to Cas7 family; also known as GSU0053 family
AALVIREPLMPVEGADGVLFPATFAPTGFPDLGYAIDKGPEGTKVCLVDSVGSQANRIEAVFMDTGNNNA
PAKLLPQIVVNAGNKKVNSLEAGHRAGDAIIRCSELQGELKQAFNFDASRPLVLAGNATALLKIAPTSLL
FGVWDSRDTGQAKLPRAVASTIRAYDVRPLTRGA
>gnl|CDD|187810 cd09679, Cas10_III, CRISPR/Cas system-associated protein Cas10. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Multidomain protein with permuted HD nuclease domain, palm domain and Zn-ribbon; MTH326-like has inactivated polymerase catalytic domain; alr1562 and slr7011 - predicted only on the basis of size, presence of HD domain, and location with RAMPs in one operon; signature gene for type III; also known as Crm2 family
SLVVFTIGPVQEFIATARKTRDLWAGSYLLSYLAWKALEVLVEEFGADVVIFPYLRGNPLFEKKLENKDN
PELEIASLPNRFLAIVPGNEEEAEELKEEIEEETWESILNKVKEYLDIENVEPFLLKSDALERISDRIED
GNEDREEAEELEAARKNVRDFAPVPWIPPAPKIYIYIVSIFNEKELSEKYKEFLLKKRNGLLLDKLGGRA
RKEYRSVCGLLAAAWKLEKETEQYSLFAKDDLEEDLKLLLEAGERLCPLCLIKRLLPERLKEKLVLIDEV
IKRSKRNREEPRLKYENFREELRELLEKEPEIVYLFIKAKKNPGPYYALLMADGDNMGKWLSGEKLPEKR
LITPEYHRAISRALSNFALKAVKIVVEEHRGKLVYAGGDDVLALLPVDKALDCAKKLRKAFSGILNKEIG
EDMGEGPTMSAGIVIAHHKEPLQDALELARRAEKRAKKEGRNRLAVGLLKRSGKD
>gnl|CDD|187811 cd09680, Cas10_III, CRISPR/Cas system-associated protein Cas10. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Multidomain protein with permuted HD nuclease domain, palm domain and Zn-ribbon; signature gene for type III; also known as Csm1 family
LALGALLHDIGKVVQRAGLGFYSKTHSKFGAEFLKEFSKNKDDLGDCISYHHTKELAKALLENHHPLAYI
VYIADNIAASVERREGEEEGEGFDKERPLHSIFNVININEKKKNYKPKKLAYSLKPLNPEIPPSEKIKAS
QSDYKELYEKLKEELKKINFNEESFNSLLSLLEKYLSYVPSSTDTGEVPDISLYDHLKLTAAIALCLYRY
LKENNITDYKLKLFKNSDDFRDEKKFLLISGDLSGIQDFIYTISSKGALKSLRGRSFYLELLTEHIADEI
LEELGLTRANILYNGGGHFYLLLPNTEEAVKKLEEFEEEINEWLLKEFGTDLYLAIAWVEFSGNDFMNDE
GGFAELFRKLSEKLSEKKLKRYSYLELAALNPRDSKEGSKGTRECKVCGREEPIAEDEDEGLCPTCERLY
ELGKELLKDDSFLVTEKEDGGKKLPKFNGYYLLFAYEADEYEELALEDELVRIYSKNKPDTGDLIATKIW
VGDYVPRNGDGKELTFEELAKKSTGIKRLGVLKADVDNLGEIFASGFKEEKRTLSRLATLSRQLSLFFKG
YVNYLAKNGEAGLKPERKRNIYIVYSGGDDLFIVGAWDDIIELALDIREAFARFTGGKLTLSAGIGLFPP
KYPISRMARIAEELEEAAKE
>gnl|CDD|187812 cd09681, Csx3_III-U, CRISPR/Cas system-associated protein Csx3. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Small protein in some cases fused to Csx1 (COG1517) family domains
FTLIEFELERPLVPEDLKQLQPPAGVNTRKGVVLSGRGPIWLYGFLVHFYHPTPFVAVYDPRLGAVVVSS
HSPEVRVGDVIDW
>gnl|CDD|187813 cd09682, Cmr4_III-B, CRISPR/Cas system-associated RAMP superfamily protein Cmr4. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; This protein is a subunit of Cmr complex
YLVLLYALTPLHVGAGQGIGVVDLPIQRERHTGYPIIYGSSLKGALRSYFSAQIVDDKDESKVECVFGGP
KEEAEESAGKVVFSDARLLAYPVRSFDGVFAYVTSGKVLLEEIKLEAILNEAPGVRELWLAIKTEAPVPE
LNELLRLVVVSDSLFRDLVNSALERVPRIRLNQETKTVEEGGLWYEEYIPAGTIFYGLIRVDEDSNKECR
NVDEIFKEFSKIINGKVIQIGGKETVGKGLVR
>gnl|CDD|187814 cd09683, Csm3_III-A, CRISPR/Cas system-associated RAMP superfamily protein Csm3. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein
KSQTKISGILENQTPLRIGYGKSQEPTGPDDPVIKDANGRPIIPGSSFKGALRSLAERYLKRRNLITCSW
NDPDYWVCDPDDNKCTSCNGKENYIEDALETFWNKTCLPCILFGSPWLASRVYILDAVAEEPSDQQRTMV
AIDRDFGTALPGHLYDFEYVEPGSVFNFSIFLENLNEWEIGALLTVLKTLITGGIFIGGKKSRGFGLVKL
TSGEIE
>gnl|CDD|187815 cd09684, Csm3_III-A, CRISPR/Cas system-associated RAMP superfamily protein Csm3. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein
GKIIITGTIEVLTGLHIGGSKEELKIGGTDSPVIRDPLTDLPYIPGSSLKGKIRSLLEKVLGLDYILKDK
NQYECNQGDCEVCRLFGSAPNAGEGIKGPTRLIVRDAFLTEDTKKEAESTDLPYTEIKFENAIDRITSKA
NPRQIERVPAGAKFKFELIYSVYEGDDEEEDFKNILEGLKLLEDDYLGGSGSRGYGKVKFRDIKLITKPG
EYYEG
>gnl|CDD|187816 cd09685, Cas7_I-A, CRISPR/Cas system-associated RAMP superfamily protein Cas7. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas7 is a RAMP superfamily protein; Subunit of the Cascade complex; also known as DevR family
SGRVRVNVEALNGVESAGNYVKHRRAPVVVKTDNGYTVYEVPAISGESLAHWHQVYLVEIAKKLGLPVNE
LCKRGIGLKFGNGDTTKKKGSKPPNDYEAEVIKEDIVEDVHGFLYAEKGPVKRTSLVKFSYMIPVLFIEE
VAGAEAQFHVRHNRVDPDEKGSKKEGTGQMLFNVEYSSALYGFSFVLDLDLIGVPQFLPEKAEGDEEERK
RRIEAALKALIPLLSGFFGAKLARFLPVVKVEELVVAVSEKPFPNPPIHGSYEDYTEKRKSTAK
>gnl|CDD|187817 cd09686, Csx1_III-U, CRISPR/Cas system-associated protein Csx1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; Some proteins could have an additional fusion with RecB-family nuclease domain; Core domain appears to have a Rossmann-like fold; loosely associated with CRISPR/Cas systems; also known as NE0113 family
ILLCVSGMSPQIITETIYALAQESPPVVPEEIHVITTSDGKRDIQQQLLTPDEAGQGVLAKLRHDYFQGP
RPPFDELRIYLIPTGQRKPLADIRTPADNEAAANFIVQTVAPLCAAQDHQLHASIAGGRKTMGFYLGYAL
SLFGREQDRLSHVLVSEPFENIRGFYYPPRKGPILEIRTRDGPPAPADTSEAVVELAELPFVRLRHKLP
>gnl|CDD|187818 cd09687, Cas7_I-C, CRISPR/Cas system-associated RAMP superfamily protein Cas7. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas7 is a RAMP superfamily protein; Subunit of the Cascade complex; also known as Cst2/DevR family
TLTAVSSGNNNYDEGAGNIVSLKKLTRDGEVYPYVSRQAIRYALRDTLKEYGFELSEVVAKEQEDQEAFT
AGNPIKYIDDDLFGYMRTKKSATNKRTSPVRITPAISLEPFQGDVDFGANYDLANRTEANPNPFETEIHS
SLYKYSFLIDLDRVGKFEVGIEEKKCNPRGRLEYRLPKEEKEKRRANNLLKAIRNLSGGAKQARRLEDLS
PKFVVLGVLNGKNPFFLNSLRVEEGKSALKIDVELIVTALEDFSEKIEDLEHIGLLKGKFANELEEIKEL
LADGGVESEVGIFEEIEKAVEE
>gnl|CDD|187819 cd09688, Cas5_I-C, CRISPR/Cas system-associated RAMP superfamily protein Cas5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas5 is a RAMP superfamily protein; Subunit of the Cascade complex; in subtype I-C this protein might be the endoribonuclease that generates crRNAs; also known as DevS family
IALYVEVPIASFRQSRAREYGETYPVPPPSTVYGMLLSLVGEDDRYRHCGVKLAIAVLSEPEKSTVLRTF
RRFKTKNIDDPKNENPEYQEVLSNIDFIVWVISGNEGAQPTLAERIVEALTNPESVDRFGGLSLGESRDL
VNDIRLLPEDYTAESRRWLIQDEDGLLTLPYWVD
>gnl|CDD|187820 cd09689, Cas7_I-C, CRISPR/Cas system-associated RAMP superfamily protein Cas7. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas7 is a RAMP superfamily protein; Subunit of the Cascade complex; also known as Csd2 family
RIDFVVLFDVKNGNPNGDPDAGNMPRIDAETGHGLVTDVSLKRKIRNRVLLMGQDIFVQEKARLNDTIKS
LYKRLDIKLEPKKEGRAKKASVEEFRKWMCANWFDVRAFGAVMATKGNAGQVRGPVQITFARSIDPVVIQ
EHSITRMAVTTEKEAEKQSNRTMGRKHTVDYGLYVAHGFISAQLAEKTGFSDEDLELIKEALVNMFENDR
SAARGSMSVRKVYWFKHSSKLGNAPAAKLFDLLSVSRKDGSGPARSFDDYAVHLNAAYEPKGLEVEEL
>gnl|CDD|187821 cd09690, Cas7_I-B, CRISPR/Cas system-associated RAMP superfamily protein Cas7. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas7 is a RAMP superfamily protein; Subunit of the Cascade complex; also known as Csh2 family
RSEILFLYDAVDANPNGDPLSANRPRIDEQTQQLIVTDVRLKRYVRDQLDDDGHGVLIRTVQEEGEQYDR
LKSVDYDVYDLDDVKEAEQFRFGEYLRKSIDVRLFGAVISVDKDDVYPDHITGPVQFSPGKSMHAVNENE
EQGTSAIATQEGKEQGGFDDDHRIPYALIRFYGVVNENGAKDTGLTEEDVERLDTLCWRGIKNTISRSKV
GQEPRLLCRVEYKEESFHLGELDYDVDVEASKEDEELRDISDLALDIDDLVDRLDGAKAQIERIRVVASD
VLKFTH
>gnl|CDD|187822 cd09691, Cas8b_I-B, CRISPR/Cas system-associated protein Cas8b. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Zn-finger domain containing protein, distant homologs of Cas8 proteins; signature gene for I-B subtype; also known as Csh1 family
SDTTSDPYKFYTTDKPGYSPGLEKKEAYKNYPICEDCYKDVLIARKFIEEKLDFNFGGNNLYIIPGVWAF
DTKKSKIKKIFEFKNTQFNINLREIKGLEEQISEDFTDGEGLRVDFLFYEKEKAAEKIVLYIKDVEPSRI
EKILELEKKVENYNKEIGEIENLNLGLDNIYFLIPLSKDNFFEDREFLNLLDAIFRGGKIDKDTLLTWFV
KKIKNEFFENDSISSLNLIKINKRYLLKAGLQANLDCLLLDKLELISRGDSLLEVKDVKREDLNEYVKKF
FDSPQKRALFLLGALAGELISLQKSKNKSKSLLNKLKGLKINKKTIEGLLNEVREKLTQYGRQNKYKAEL
VESTIKSLLPAGKWKLSEDEIVFYFLSGMSY
>gnl|CDD|187823 cd09692, Cas5_I-B, CRISPR/Cas system-associated RAMP superfamily protein Cas5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas5 is a RAMP superfamily protein; Subunit of the Cascade complex
LVFRVSGPYALFRKPYTNTSKLTYPFPPRTTLLGLIGAVLGYDKDEYYDLFEPVRGRLDLAKPVRKIMQV
LKFLRTKTDKVETKKNEDKKMSKRTIVKLQVLRNPAYRVFIAWDDEKFEELKNKLEALESIFIPYLGKSE
FIANIDYVGKFENTELADDTVILDTVLENTKKELVEPSHYLIDEKVISK
>gnl|CDD|187824 cd09693, Cas5_I, CRISPR/Cas system-associated RAMP superfamily protein Cas5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas5 is a RAMP superfamily protein; Subunit of the Cascade complex
LLLRLEGPLASFGRPSTKEERPTYPVPTPSALLGLLAAALGKERRDDIDELAVLKILAFAVRRNEPGSKL
RDYHTAQGGKRKLEGEDRKKRAGTILSDREYLADAVFVVALSNEGDEYLLEELRKALGQPRFPLYLGRKE
CLVSVPLVEGVVGLGEALKAYEGEEDLGSMLGDEEFEDGLDPLRRRFGRRRVPINGVIDVPE
>gnl|CDD|187825 cd09694, Csm6_III-A, CRISPR/Cas system-associated protein Csm6. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; loosely associated with CRISPR/Cas systems
PDANLEPQDPWLGQKTIGDPEQALAWLVRTDPERISAELNTYLQLAPRSDRLFSGNDAAILYHSDTADGR
ECAQILKLFLERELGARQQVKLVPGLGRDFNYGLSGLSLERMADVLVQLAEGNVGIVTFTGGFKPEAMIL
ALAGSLAGAVPVFYIHEQYNSLVYLPYLQPQVQPRLPRAAL
>gnl|CDD|187826 cd09695, Csx16_III-U, CRISPR/Cas system-associated protein Csx16. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Small protein often seen in proximity to Csx1 (COG1517) family; also known as VVA1548 family
AQLDKFELHLDPSGIFKGDRVIGTLPIKLAAHICRRGARYFRLSLNVPATLRGLELAWEQLLACGAHLEE
FAIGKS
>gnl|CDD|187827 cd09696, Cas3_I, CRISPR/Cas system-associated protein Cas3; Distinct Cas3 family with HD domain fused to C-termus of Helicase domain. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DNA helicase Cas3; This protein includes both DEAH and HD motifs; signature gene for Type I
LKFDEWYQGLHGYSPFPWQLSLAERFVAGQPPESCSTPTGLGKTSIIAAWLLAVEIGAKVPRRLVYVVNR
RTVVDQVTEEAEKIGERLPDVPEVEAALWTRPEKPDPKKDRPLAISTLRGQFADNDEWMLDPHRPAVIVG
TVDMIGSRLLFSGYGCGFKSRPLHAGFLGQDALIVHDEAHLEPAFQELLKQIMNEQQRPPDFLPLRVVEL
TATSRTDGPDRTTLLSAEDYKHPVLKKRLAAKKIVKLVPPSDEKFLSTMVKELNLLMKDSGGAILVFCRT
VKHVRKVFAKLPKEKFELLTGTLRGAERDDLVKKEIFNRFLPQMLSGSRARPQQGTVYLVCTSAGEVGVN
ISADHLVCDLAPFESMQQRFGRVNRFGELQACQIAVVHLDLGKDQDFDVYGKKIDKSTWSTLKKLQQLKG
KNKRAALGVLAIKKRQEAFSPPPRILPLSDILFDHWALTCLRQKLPGRPPVSPWLHGDDEWNPPTVHVAW
REEVPCITGLLTQCPPEDLLEDYPLKPHELLRDMPCRVFEVLRKLGRRSGTPVWVVDDDDSVRVVVLGDL
VDRGKSIRGGCTVLLPPRYGGLDNGMLDATSTSADDVADGWMPDELRHRRCRPWDDLGNQSGMRFRRVGI
DEDPDIPELEEEANEPTVKRLWTWYPAVIVTDTDGSKRSGDEVALSDHLDNVFEVAKNFVAKLGLGDLDK
AVRQAARLHDLGKQRPRFQTMLGNRSYPLAKLAKSGPWAAKIARSMYRHEKGSLIDVANPDGFSMLSEEL
SDLVLHLVATHHGRNRPHFPESEDFDLWRPDADAKAGGSEVPRRTCRLQRKYGRWGLAYLESLVRAADWV
ASK
>gnl|CDD|187828 cd09697, Cas8a1_I-A, CRISPR/Cas system-associated protein Cas8a1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; signature gene for I-A subtype; also known as Csx8 family
FDTALEASDWRYSATIVGLIYYFKELEKKYEIKKITIYEIEDDYLLYNSEDINEENYLDFVEKFYSDTLH
HKKVENILKHKEFTEEIIKSINEKLSANTVMKKVFGKIKFDGTNKDEILDLIDKNRHSLIKETFRRKKDL
YDNYCNTNRLFEDDNSPCRLKGYCFDPGKKGKSTGYNFVSSTFDYFDDKIFDFIPFAFTGSFEAFFINDN
LDIEILKKSNKAIKEKKNEETEGENNSVPLRKTLFNILQEKVDYIKYDVEVILKNRDKEYFETWYLRNES
IKIFKESDIEDYKKLDFRIKITDKYYFNLLDEVFSAILNLSLLDNSIEYLLKDKNSYSYAINELIKINQL
IRNGGKEMDENLKKAKACAKAVVKKFIKELNKLASYKQKLLSSVVFKDHDRICDILLQLSVYSGVYFSFA
YDLIEDFEQNKDLAYTFINAL
>gnl|CDD|187829 cd09698, Cas8a2_I-A, CRISPR/Cas system-associated protein Csa8a2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; signature gene for I-A subtype; also known as Csx9 family
MSWVVMDAGLEPDPEELADALEGALDSLKSRAMINTSKIGRNDRNSFDRVLSAWFGRSAPETYGELFELV
INETIKLLRSGKIDPAKSLSTIKTDKNGTYLGQAYNGEQAILPAIIKQPEYYEFQSEFLKPTTGQKAQIR
MDPLWFSFMALGFFTSFAGFIRGKYYLMTKPGIEVFWPYEVEEIIEDGILPLTDAGASGRISLDTEELYE
MKLAMKLAEEGRKVIEEVYPVTLHVISLEGQVYTELKTLQLNLKELSNYLAEYVKKIENYRVGGVDLLVE
LKEGGATVEKYPLWALVDIAEKELWKGVSGDREMLAYIFVKDLYRAINSGRKELIEDSIFRLFRQGRALL
EGSGRASGEFRKVMRTFMWEEHLEVLL
>gnl|CDD|187830 cd09699, Csm6_III-A, CRISPR/Cas system-associated protein Csm6. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; loosely associated with CRISPR/Cas systems
ITRLAPNTEVEIIIYTNPSVHRFDLFVPVFRNHLVILSAEYPDREIILNTSSGTPQMQSALVAINVFGIP
NTKAVQVSTPARASNKDIESPNAYDLEEMWDANDDNQPGAPNRCFEANSAAFGAALERANLKQLIVSYDY
SAALTIAADSRLFDNVKNLIRGKLHRSRLEHKVAPKFFKITAFTYDDANKKVLEYYLALALLAKREQWAE
FLISAKSAAEFVLRAAIAKHLPELIYLDDGMPRLNREDKLEREPKIRCALKHPPKSFNVEWYLYLKDWLA
ILRQFEPDSQLALEVNGRFESNGVRNTAAHELVSISEDKRITKDGGLLPEQLLKLLARETGIDLTLYNYL
NDENKEQIDM
>gnl|CDD|187831 cd09700, Csx10, CRISPR/Cas system-associated RAMP superfamily protein Csx10. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Duplicated RAMP domains
IELTITALSPLAIGRQKPGGSIGEAYPYIPGSVLRGAAAAMLLRQKGIVAVDAREGDAARLFFDGRTRYF
CYANVLPATASSSKTNPGFRSEFHHGVFDTLIDDFALEVLDAVNEETAQFVGAGRRVEPFCGFYSSNRER
YCSPARRIRLLTRVGINRYRATAVDQILYSYEALNEVTVQPDEKVSGQVFAGWIYVDKDDLAELLSSLLR
HIYRLGGSVSRGYGRVTVAADEPQGFPDIVERVIPFNQVLIDRWQDWVVLLGDTLVPLPAKRTYFSTGLY
SWDILPELWQVALPPMLQVEAEHEDPSLGLERAVSRYDYVGGWNRAWGLPKPVELATAGGSVFVFRTRSP
IDWIQTLAGLEWDGIGERRAEGFGQLEVCWQFHQEF
>gnl|CDD|187832 cd09701, Cas10_III, CRISPR/Cas system-associated protein Cas10. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Multidomain protein with permuted HD nuclease domain, inactivated palm domain and Zn-ribbon; signature gene for type III
MSDLKKLKNNRDEILLAEIGAYLHDWGKCSDEFIKTNSINAQNQRPYHSLNNDKLKTRELKDIKDFIVLE
VNVEKVTIYDFIEKGHTWRNKLKGLKLCRILGSAHGIVGIDKGLVKRGKQSKEYTWISSPFGYEKEKIIL
QKEFDNLLSELIELIKNKLSDFSQENRSNLLKSLKEYFSHALGETRRPINEVTLWDWSYSVASLYKSALA
AILLTGQIPDPQDLKWRILSIRFNGLGLLLKGLKIPDILARKELLEEILDRVKKLLEETYPLGNEVYRDE
NGIYFVVPDLERLLDETLECAVGDEKLIEEEILKTFNEELENEGELVITLSKASRLLTSLAPEREKALEN
ELPPIISPLLFDISPATQADIPNFWENKENKGICPVCGLRPQGPTSKAEEKERCDICDERRTDRAKEWLH
SLEETIWIDEVADKNDRIALIVGRFDLDKWLDGELLNSLINIIPDTNNKTENKYLFTKNPSFARLRRIWR
TTRDFWQDVKEFLDSKFIKAYKNRVIKFNERKKEIKSSLKPNPSYKKIPENTTCDISISGLRLSPVCVFH
GENGIFTTTTSLQIFDKFGITEELIKEALKEKLIKLKSEGEKRWNLINIIKKIDADDIEFEDYYPYIPIL
AEPDSFMFLVPADDALDIIEKIKEKYEREFGKVRDRLPLHLGVVFAKRRTPLYAVLDAGRRMLKREEFKK
QVEEDPWIQEERHDENYLEKTKKLVQVNRRSVPLFWAQSYSTKDKRWLDLWSPLKRGDIKYLHPGTLCFD
YTVVHIKETFDFEFLDIETRRFEICYIEDESDRRRRDLKRPFYLDDIDRITDLWDVLSRLLSNQQIQIIQ
LIEKKREEWKIVEDNGPDIVFEQFVEDTLINANWLDWDRLDDELRDKLEDAGKKGCLADLLELRMEILK
>gnl|CDD|187833 cd09702, Csx1_III-U, CRISPR/Cas system-associated protein Csx1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; Some proteins could have an additional fusion with RecB-family nuclease domain; Core domain appears to have a Rossmann-like fold; loosely associated with CRISPR/Cas systems; also known as TIGR02710 family
HPLAQAIAEKRPDKVVFLGSEMTVEYIKEEAEALGRDPPEYWLCKTIELEDIDGVVKELFALREAQMDIY
DQEILADLTGGTKPMTAGLVLAAILYGKELSVITGFRRRNGRVIPGTERLIEQSDPYQVYGKLEIGRFRR
AFNAGDYETALAILENLLRRVLAENHTFYEAMIKLTRAYLHWDRFEHEEALDYLNSDLVNSLEEAEDVLK
QNKSIVHEIASISLDQQASRNGARKQKYRPLLPDLLANAERRATQGRYDDAAARLYRALELIVQIRLEER
VGYGDEDDDINPAGYPESTRAALALRDGKKSHLALKNAYDLLECEGDDLAQRLFGEDNRLLDLLQIRNHS
ILAHGFRPVTEEQYREFYDKVLELARMI
>gnl|CDD|187834 cd09703, Cas6-I-III, CRISPR/Cas system-associated RAMP superfamily protein Cas6. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas6 is an endoribonuclease that generates crRNAs, predicted subunit of Cascade complex; RAMP superfamily protein; Possesses double RRM/ferredoxin fold; also known as Cse3 family
IDLLFPVRGGTVPADHAYMLFSALSGVLPALHERDSLGIQTLRGVPDGDGVLNLTRRSRLRIRIPVEQVP
LVLPLAGKSLDIGGHRLRLGAPSIRALQPAPSLFARIVTFKHAEEPAAFLAAAQRQLEALGIQARPFIGP
RRRTVRIAGFTVVGFALELHGLSAEDSLRLQEQGLGGRRKMGCGLFLP
>gnl|CDD|187835 cd09704, Csx12, CRISPR/Cas system-associated protein Cas9. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Very large protein containing McrA/HNH-nuclease related domain and a RuvC-like nuclease domain; signature gene for type II
PIAIDLGGKNTGVFSAFYQKGTSLEKLDNKNGKVYELDKDSFTLSQNNRRARRHKRRNIDRNQLVKRLFL
LVWQEQLNLEWDKDTQQAISFLFNRRGYTYIEDDLDEYLKDATEQELLKEILEFKEISSYEFELLADFLA
NYSSSLKTQKFSYTDFQGNLKSLSYYHHDKYELKEFLKRHANIKDEILGTLLTDFEKFDFDKNEEKGGRH
RSQYFEEITNVIDENNHQESYLKNFNLSVKNLVNLVGNLSNLQLKPLRRYFNDKIHAKADHWDEQKFTET
YCRWILGEDHDKKDGAKYSYKDLCNELKQKVGLIDFLLETDPCRTIPPYLDNNNRGPPKCQSLILNPEFL
DNQYPNWRQYLQELKKLFETDLKDLKHSKDQPSNQQMASGQRDYKDDSRILQRILDRVKAIDELLLNEIY
FKLESGKKLDEVLANTQLILKSQHTNGLFEQGTFLCKYYKQRRRARDSGIWIMPEYRNNTGRFDDNNQLL
TYCNHNPPQKRYQLLNLVAGILQNQLLSSVEEWAKFKIWWQQAKVGEIKLASYCKAIEEMRKQYGNTFKI
DIEEAIFENPKDVTADEKALLKLIENIAKASQKIGESLGLNDKQIKKFNNIFSFAQLQTIAFTKRKGFAN
TCAVCTAENAHRSQQIKITEEVEDNNIILSAKAQRLPADPTRPFDGAVKRMATILAYEIADDKWQNIKQV
LSKHQLHIPIILEQNAFEFEESLAKVKGKSLDDRRKKALERAIESPENIFKDKNNRIKEFSKGICPYSGA
NIGAKGEIDHIIPRSHSKKKYGTLFNDEANLIYV
>gnl|CDD|187836 cd09705, Csf1_U, CRISPR/Cas system-associated protein Csf1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Zn-finger domain containing protein; also known as Csf1 family
CGKNIWVGDRYTKFSVGPSFMDVADLAARGGGMVCGHCTALMSKDMLQAYAKSIFSEGGVFPFASNVDVA
RGLLNPPEPPFVALYATRKSQHMAWRAPVNLSRDLMYVRVGDRDLKIRRPVLLSAVQACQTLGSFMGIKP
IAKSLAHPPARLERDLKDPAHGLLRPKGPEKTLAEAPAYPEAYQLLQSLTVGETWALRFLLS
>gnl|CDD|187837 cd09706, Csf2_U, CRISPR/Cas system-associated RAMP superfamily protein Csf2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; Contains several motifs similar to Cas7 family
ISGFIRLTAPLHIAAPGSMRFDGKTVYGGKTVGVPCTGITREVLFNEAGEAKHIPYIAANNIRGRLRRHA
ARIIMEALRLRGQKVSLALYNVLQCGAVTGNPDGKDMTLGEYRQARDDPYFGLFGGGPKMMRSRCLEVED
ALPVHADTTALLPSMAHPHAHRAAPGDHFTEVWGIRRNDDLRRLVNIDQAAEVVQNFEAEFAARQQAILN
EVDREQKGSSKTSGVFLKDLKTNDLKTYSAVEFIIPGTLLYFSILMKDAITDAQAGLLLLALDSLANTEA
LGGYGRNGFGRFTAAILLTSDGDEHQDAFHDGRLNGEDPLTAHTLPAW
>gnl|CDD|187838 cd09707, Csf3_U, CRISPR/Cas system-associated RAMP superfamily protein Csf3. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein
PLEIRFRLATPMVHSDYPFHFDALMAYAVSRDALMNASADPWGDARDLSEDLPLGKEEEGDSWVWKASRL
EVLAFLPYPKRYETAKTLPFTDPSRFIGDDLDRGLWQARGKVNPETFRIDTNRGQQKNYQMYYTTENAQE
LAAWCIGDEEALEFLLSQITHIGKGTRNGHGRISNAEIRDDEEAADRWKKRWLPKDMPGADYAPIMGRLR
QPYW
>gnl|CDD|187839 cd09708, Csf4_U, CRISPR/Cas system-associated DinG family helicase Csf4. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DinG family DNA helicase
EQALFYRNCLTSLRQKRIGMLEASTGVGKTLAMIMAALTMLKERPDQKIAIAVPTLALMGQLWSELERLT
AEGLAGPVQAGFFPGSQEFVSPGALQELLDQSDGPGDKDAVVRLWMGQGGPRKVAPLFNRMRDVTLLIHD
TADIRGYVSYREQWDSLPRCSAMSRAPTKMASMTHDLKALATLNPQDFVTEDEEDKRWVTSLVESREYYA
RKSRILACTHTMLKWGLLPQPDILIVDEAHLFEQNISRVYSNALSLRMLRFHLEVSHRKTGAIGSAVVAA
VSAVSHRLRQVSALGDGQTLCLDAGNKELETLFADLDAALEIKSTPNKKALSVVKDVKKARIILDNAITA
IQGKQSTVYLQFSPDRRFPSLIVGREDLGKVMGGLWKDVTHGAIIVSATLYLPDRFGQMSCDYLKRVLSL
PLSRLDTPSPIVAPWVRNLIPHLHVPNAKARFLLSRPVGKTEQGDANLAGWLENVSLSTAAILRKAQGGT
LVLTTAFSHISAIGQLVELGIPAEIVIQSEKNRLASAEQQFLALYANGIQPVLIAAGGAWTGIDLHDPSV
SPDKDNLLTDLIITCAPFGLNRSLSMLKRIRKTSVRPEIINESLMMLRQGLGRLVRHPDMPINRRIHDLD
PR
>gnl|CDD|187840 cd09709, Csc2_I-D, CRISPR/Cas system-associated protein Csc2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; predicted Cas7 ortholog; also known as Cse1 family
PKGRYVTLLVLRETESEALFRTEGGPENSSLVRAGDEGKTTISPLIMFKRKQSAPERRLGRELLRKYEYD
KHISSNCSLNVNSMCRECPDCALYGFAAGEADGSVKSRVMYDTAFSITPASKSVEERTQNAPGEDGTKTS
FIETRTSSINEPDFIKPGTLFPCVVTLKDVTPAEFLYVVNNIARTARYGANTTRFGRVRNRILGVFLSPY
EGPSNLELTQATYDQTNNSLNSPLGLDSVIDQVNAAVREAIKNLSKEGRIVTFDLLGDEVVDLL
>gnl|CDD|187841 cd09710, Cas3_I-D, CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D
HQVATFEALQSKDADIIFNTAPTGAGKTLAWLTPLLHGENKAIALYPTNALIEDQTEAIKEFVDDANPRH
QVKSLSASDITLWPNDKNVGSSKGEKLYNLLRNDIGTSTPIILLTNPDIFVYLTRFAYIDRGDIAAGFYT
KFSTVIFDEFHLYDAKQLVGLLFYLAYMQLIRFFECRRKFVFLSATPDPALILRLQNAKQAGVKIAPIDG
EAGQFPDNPELEQQLKNTSFRPVLPPVELELIPAPDFKEEWLAELAAEVIERFRQLPGERGAIILDSLDE
VNRLSDLLQQQGLGDDIGRITGFAPKKDRERAMQFDILLGTSTVDVGVDFKRDWLIFSARDAAAFWQRLG
RLG
>gnl|CDD|187842 cd09711, Csc1_I-D, CRISPR/Cas system-associated protein Csc1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; predicted Cas5 ortholog; also known as CasA/Cse1 family
LTLHSPVFFASRESGRLYETEPYIGNTALDYALGYSLGEHPYRYVDATQRPTYNEDLAPINDFGYVTPAK
PVYRNTMLGIWYYQTNNYPAEMVGTLYNYPNFGRAKEIAPGNKFYFYVFSDQGEEKLPVYIRLGKKRSKA
KVTVKEVPVERKSGVYILNHPLNPLDLKNIPNLDFNVVNMPPYPLINNGQFEGDYWQIVENTGGPAGEHY
>gnl|CDD|187843 cd09712, Cas10d_I-D, CRISPR/Cas system-associated protein Cas10d. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain. Fused to N-terminal HD domain; signature gene for I-D subtype; also known as Csc3 family
KGDQSLANHILNGLLTLWNLLQQLEFTVLNVKERRLLIAGFTLHDYHKHCHAQDMPNDEFDLNIQEIIPI
ILELGKRLGLDEFWAPEEYIDFRSCAAEITHGTQHTNLISSNTSNAGYPFTKLDHPLRHLLLLADSAASL
SSPHDAVSSTMKDRLRFLLNGIEKRFVYHHLRETTGVLSNVVHNVVLETVQELDYKPLLFFAQGVIYLAP
QDTEIPETNEIKQIVVQGISQELGKKISASHVGFKRDGKGLKSSEETSFFYAGAGIVRIAPQAISVKVNN
AKSSATDKRTESLELLDAELEKKYEVADLRCDRLAELGGLVQRKEWFELPDPLLEAVEFWVLKDLLLQSV
VIMPEETQVQKNSGGVWYYWYAIAAHYLDRHPGATSVLEEIQEFLQYFGDRLATWAEEEGYESEIQSPTR
QIFEDYLDEYLSIQGWESDHQAFYQELENYNNAKTKKSKQPICSLSSGEFPSEEQMDSVVLFLPQQYSNK
NPLGGSQIKRGISSIWSIEMLLRQIFWSVRSGKFEDGQPIFFYLYPDYVYTPQTVEAISELVNGIASNLG
DVRVRWVNLAMDLTSLESLPSVDIDLNLEVEAGRTAILSYTDDQNLTFLATVYTKTRDKTDTEAWFFPAF
LALLLPYLLGVKVVASESPVPLMRSGQDFRESVHLDGAPHFWVLLGIPDRLRLEDITPALNKLLAIYTLH
LAIRSSPPDANWQDFPKTLQTFRTDPLPVFALLKQGVRNSKRDRPYISEITRYAYFAELFSQGNIVMTDT
LKLTVKRLVELYRRFYRVALSKNPKPHAVLKPFREAVEAILKVGSQWDEEDLVLQVSGRLQKMIDRQEVI
KGDSVAYETRQLQELEAIQIFATYFVDEIFYEMAKGDRAILKRQRNNLADGFAEFTYRLE
>gnl|CDD|187844 cd09713, Cas8c_I-C, CRISPR/Cas system-associated protein Cas8c. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; signature gene for I-C subtype; also known as Csx13_N family
LFQRLLSPCMTPLLRAGLAGLAMTLKSLEKEYPPPAPRLGTLTWELTQDSIQLDWKGQDSKDLDWLFKHS
FQIKEGLISLPGLHPTKMPHPDQIHFHQALTGTFLQHGKFFKSGAGTSVECKVDYIPVLVEYKIAYSYAH
QSFAFAECDGSGWLFEEPIELSGWLYPGAPVRHIAFTHETKWEETAADALALLFAPVACSYYELRSSRGT
YAIVIPELTDLETFARFRRDLTELNYINMFVGGPGDAGLKYLTYMATTGNKKDNSLNGCEVIVIGTVAWN
KQQKVRALVMRIHPTEKVNRIYKLMRGIFPNKIHVK
>gnl|CDD|187845 cd09714, Cas8c'_I-D, CRISPR/Cas system-associated protein Cas8c'. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; signature gene for I-C subtype; also known as Csx13_C family
IAENLAAGRPWYANFAGASKEKGRFKHDRRERDELNKMIENSEIWDGEAEQWFVQSFHEALRRIYAKIAA
DTKERAPETLGDRLKRENERIYSSLARAKTPEQFRAFIADLWARAGRIPELQEHWGALLKLIGKDRWEAA
RDLALVALASYQ
>gnl|CDD|187846 cd09715, Csp2_I-U, CRISPR/Cas system-associated protein Cas8c. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Predicted Cas8 ortholog
HPYIRYAQALLLYENNLSSIERITPKHIKFEIEKGLSSFRIQPQEPFSGKSKVRYSFVKREKGDTKNGVF
LSPNIISKDMHAQNVWTKASKFLEIDKDNEREDLLKKDNVSMSNIPISGEYLTFSEKGDTGRGKPKSSIE
EQTYGLITTLTPLKPCLQVGKDNFCIIPDLPLNQMVDFIALFKKMQITHLSGDLMLGNVVKSKDNKGKDI
YIPKRPKIFRGNFPNSPKSDALGSVALLGAIGEFAKHAEFSTLAQKVLDSLKGSTLYLVTYGNAIPFTYN
HYIIDLAKKGKLRSIVDSLYYSRLYNKEKRVYGDTDYDRFDLFTNRFLQLFNKPAFKDFLSFRAEYPNQI
KLLLQMYFTKMEKIDADVVASAQILGSWLNQVAYFAAKEESRESPGNIFEELRKTKAKFLVELESSIFAA
KSGDALIAQVITRAGRLSGNDAPKEASLFMEKTISGELDLSVAKNLLIAFSRLR
>gnl|CDD|187847 cd09716, Cas5_I, CRISPR/Cas system-associated RAMP superfamily protein Cas5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas5 is a RAMP superfamily protein; Subunit of the Cascade complex
IKLHIEPHAPISMVSELPGSYYKALLYPDKHILCGLFENVLGWHFSRKDREIITKEIKNIRKKTKKGYIP
PTIRSIFIPLLSDFFELDSVRIVSTDSPFFYNDLWKRAFRRKDAGKIHFGGTQNIDYTLVMDKFRFMCEN
ERTLETEEKTDQKEEKFLRENIDRISFFYTTPTNREYLFFEGNYECVIKMDPQLVDLLSKTLPQQNMGYL
GNSEGWVTLY
>gnl|CDD|187848 cd09717, Cas7_I, CRISPR/Cas system-associated RAMP superfamily protein Cas7. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas7 is a RAMP superfamily protein; Subunit of the Cascade complex; also known as Csp1 family
VAPFENHMANGGEKLFGNASSIKRRPDGRVYVSGQMQRHVLFSAIDRLNHLDKAKGTTFVSNGDGITNLI
EIDLRADLGGFMHTNKGDYSDRRIAPLSVTPATALDTSSVGRDLLVRIRFDKSSDAKNQALATREYSEQD
KMNMNFFLDITSVGVSKSFVYKDGLNLGTKYFKHITDDEKKRRVKLFLEATRIMNDYANQARNAVCGEPE
KVLIVFDDRLSRKACRYYTVGEKEQANIIKELDQYQVKYFVGDDASDYSVADAYRDAMNYLDKATLVDFA
EGEEIMTFAEAF
>gnl|CDD|187849 cd09718, Cas1_I-F, CRISPR/Cas system-associated protein Cas1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas1 is the most universal CRISPR system protein thought to be involved in spacer integration; Cas1 is metal-dependent deoxyribonuclease, also binds RNA; Shown to possess a unique fold consisting of a N-terminal beta-strand domain and a C-terminal alpha-helical domain
ILHSKRANIYYLEKCRVLVNGGRVEYVTDEGNESLYWNIPIANTTVLLLGTGTSITQAAMRELAKAGVMV
GFCGGGGTPLFSANEVEVDVEWLSPQSEYRPTEYLQAWMKFWFDDDKRLAAAKAFQLIRIELLSQHWKKS
LDLKEHFYPDENALEALLNRYEQDIDRAENSQTLLAAEARLTKALYKLAANTTGYGDFTRDKRGGGIDPA
NRFLDHGNYLAYGLAATALWVLGIPHGLAVLHGKTRRGGLVFDVADLIKDALVLPQAFICAMAGDSEQEF
RQQCIAILQDSDALDYMIESIKEIAL
>gnl|CDD|187850 cd09719, Cas1_I-E, CRISPR/Cas system-associated protein Cas1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas1 is the most universal CRISPR system protein thought to be involved in spacer integration; Cas1 is metal-dependent deoxyribonuclease, also binds RNA; Shown to possess a unique fold consisting of a N-terminal beta-strand domain and a C-terminal alpha-helical domain
VKDRISFLYLERGRLDVDDGAVVLIDAEGGRVQIPVASLSCLLLGPGTSVTHAAVKLLARHGCLVVWVGE
GGVRFYAAGLGGTRSAARLLRQARLWADPRRRLEVARRMYAMRFGEELPPGLTLEQLRGLEGARVREAYR
LLAEKYGVPWKGRRYDPNDWEAGDPVNRALSAANACLYGICHAAILAAGYSPALGFIHTGKPLSFVYDIA
DLYKAETTIPLAFSLAATNPDNLEREVRHACRDLFRETKLLERIIPDIEELL
>gnl|CDD|187851 cd09720, Cas1_II, CRISPR/Cas system-associated protein Cas1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas1 is the most universal CRISPR system protein thought to be involved in spacer intergration. Cas1 is metal-dependent deoxyribonuclease, also binds RNA; Shown to possess a unique fold consisting of a N-terminal beta-strand domain and a C-terminal alpha-helical domain
WRVVEISNHEKLSLKLNQLVVKKDNGRITLPLEDIDVILIENPQVTISAALLNALAENNIALIFCDEKHL
PVGQLLPFYGHHRSLKRLKLQIKWSDPFKKRLWQKIIKQKILNQAFVLEKLGIFEDAEKLKNLANKVESG
DKTNREAHAAKLYFKTLFGEDFSRDDNGDPINAALNYGYSILRSAVARALVKAGLLPRLGIFHKSEYNPF
NLADDLMEPFRPLVDYLVYELLFESREELFKEIKRKLFSILNEKIIYNGKGMSLNNAIDKYVKSL
>gnl|CDD|187852 cd09721, Cas1_I-C, CRISPR/Cas system-associated protein Cas1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas1 is the most universal CRISPR system protein thought to be involved in spacer integration; Cas1 is metal-dependent deoxyribonuclease, also binds RNA; Shown to possess a unique fold consisting of a N-terminal beta-strand domain and a C-terminal alpha-helical domain
LLNTLYVTTQGTYLHKDGETVVVEVEGEKKARVPLHHLGGIVCFGNVGLSPFLMGRCAEDGISLVFLTEN
GRFLARVEGPVSGNVLLRRAQYRAADDPERSLAIARSIVAGKIRNARQVLLRAARDHGEEDDRAALEAAA
DRLAVALRRLQRADDLDELRGIEGEAARLYFAVFDHLLRQDAPAFRFDGRSRRPPLDPVNALLSFLYTLL
THDCRSALEGVGLDPAVGFLHRDRPGRPSLALDLMEEFRAVLADRLALSLINRGQLTAKDFEVREGGAVL
LTDDARKTVLVAYQERKQEEITHPFLGEKVPLGLLPHVQARLLARHLRGDLDGYPPFL
>gnl|CDD|187853 cd09722, Cas1_I-B, CRISPR/Cas system-associated protein Cas1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas1 is the most universal CRISPR system protein thought to be involved in spacer integration; Cas1 is metal-dependent deoxyribonuclease, also binds RNA; Shown to possess a unique fold consisting of a N-terminal beta-strand domain and a C-terminal alpha-helical domain
TYYIFSDGTLKRKENTLYFENEGEKKYIPVENIDEIYVFGEVSLNSKALSFLSKKGIPIHFFNYYGYYSG
SFYPRESLNSGYLIVKQVEHYLDSEKRLELARSFVEGAAHNMRRVLKYYKDRGDDLDDYLDEIEEQKESA
NSINELMGVEGNIRKTYYSAFDEILKDEFRFEKRTRRPPKNELNALISFGNSLLYTTVLSEIYKTHLNPT
ISYLHEPSERRFSLALDIAEIFKPIIVDRLIFRLVNKKIIKEKHFEKDLNGVLLNEEGRKKFVKEFEEKL
KTTIKHRKLKRKVSYRRLIRLELYKLIKHLLGEEEYKPFK
>gnl|CDD|187854 cd09723, Csx1_III-U, CRISPR/Cas system-associated protein Csx1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; Some proteins could have an additional fusion with RecB-family nuclease domain; Core domain appears to have a Rossmann-like fold; loosely associated with CRISPR/Cas systems; also known as csx13 family
KTLLIATLGTSPMVITEAIDYLKEKGYPISDVILIYTKDPYVLSALRALKDSLLKKFYFAKVHVKLLSFD
DILSDEDILTFMSIAAKEVKKERENYGCERIIVNISGGRKIMTIILALYAQLLFEDEVYHII
>gnl|CDD|187855 cd09724, CsaX_III-U, CRISPR/Cas system-associated protein CsaX. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; No prediction
LEIDDKELRDVLDLASDIAQGFEEDNKKRIEKTKKIEGILRIIPLSGNDKKPFEKALKCFNFPTQDPISE
VLKNFNIDMAKECQKVSAPSFVKPEMYEFGRIPGKPGGQKVEVKVDPRYLILAIAGWVFSRLGEAMVSNG
DRVGVNVFTLTKDMLYSVLVKDSGLIPGFKPETAFILWLADQVVSSKAEIISGARIYAMSDAGGQNPTTI
LGGFSIDFEKLLEKKELIDEDLIAVEALARDALNDDSGKRDFAIRISNLLYEVLGGSKRSEDLMYFANRE
LLMNLTKAKEDCRLNE
>gnl|CDD|187856 cd09725, Cas2_I_II_III, CRISPR/Cas system-associated protein Cas2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas2 is present in majority of CRISPR/Cas systems along with Cas1; RNAse specific to U-rich regions; Possesses an RRM/ferredoxin fold
VIVVYDISDDKRRNKVAKLLKKYLQRVQNSVFEGELTEAQLKKLKAELKKIIDPEEDSVRIYPLRSEKYL
EREILGAEK
>gnl|CDD|187857 cd09726, RAMP_I_III, CRISPR/Cas system-associated RAMP superfamily protein. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily proteins
TLTPLHIGGGRSSGSLDDIVRRDSTGLPYIPGSSLKGALRSALEALGKILEALSEKEKKDDDKCLVEKLF
GSEPDEGDDLAGRLRISDAYLVNIPVRKLRILKRTGVAIDRITGEAADGSPFFLEYVAKGGLFTFELTLD
NGAGKAEDEELLKELLKALLDLLTDLGLGAKRTRGFG
>gnl|CDD|187858 cd09727, Cas6_I-E, CRISPR/Cas system-associated RAMP superfamily protein Cas6e. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas6e is an endoribonuclease that generates crRNA; This family is specific for CRISPR/Cas system I-E subtype; Homologous to Cas6 (RAMP superfamily protein); Possesses double RRM/ferredoxin fold; also known as Cse3 family
MYLSRLRLDPRSRAARRDLRDPYALHRALWSLFPDDPSRAERRFLFRLEPGTDGGPRLLVQSAREPDWTH
LLEQGAGEVQTKPFDPALKAGQRLRFRLRANPTRRLNGKRKDRKRRPDGKRVALLREQEQLAWLQRKGEA
AGFELLEAELQPRDVIVGKSRKKGGRRITLSSVDFEGVLRVTDPDLFREALAQGIGRAKAFGCGLLSLAP
>gnl|CDD|187859 cd09728, Csx1_III-U, CRISPR/Cas system-associated protein Csx1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; Some proteins could have an additional fusion with RecB-family nuclease domain; Core domain appears to have a Rossmann-like fold; loosely associated with CRISPR/Cas systems; also known as DxTHG family
KILLIAPWGNPKNWREVKYSIDGEKVESLASLSVLREALKPDKTVILVPDSLSTNLDNGDENLKEDLKSE
VEELLKNIGQEFINDDDVIVLPSVGTYGNYVFDGDPDDFFSFIYYKLLKRLEKEEPDEILLDITHGINYM
PLLALEAARLALSLYAAANRKNVRLEVYNSDPYVKGEKEPLNIHEIESETIAPVTEISYLKEKFINKYKD
NNKDLKRYFKKALNEGLEKIIKFASALYNGLPLYLLYLKPSIEELREPLEFKLEIIEIIESNKNQEEEIK
VKREVYVDENFPKYLKLYFFLKIYKGIFENSEISLEDLEKLLELFFEREVISKIIKNELSKIKNLAEEIK
GEELIKLILFYNEGDKIDCQVDERNFFAHAGLEYNVTYVKKEGDKIYIKY
>gnl|CDD|187860 cd09729, Cse1_I-E, CRISPR/Cas system-associated protein Cse1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; subunit of the Cascade complex; signature gene for I-E subtype; also known as Cse1/CasA/YgcL family
FNLLDEPWIPVRRADGRRGEISLRELLLRAHEIRDLAGPRPDQQGALLRLLLAILQRAFGPEDEDEWRDL
WENGLPPDALDAYLEKWRDRFDLFGPGPPFMQDADLLTKGEVKPVAKLLAEVPGGNNLKLFVHRGDADAA
LCPAEAARALFTLQAFAPSGGAGHRVGDLRGGGPLTTLVAPLPEGETLWETLWLNLLPQETADLLPHKTD
DDVPPWERPTPVSDKKGAPTLPVGPLDLLTWMSRRIRLLPEDGQLVRGVRGKNYGAGYAGPDHWPHPMTP
YRLSKKEGEPLPLKPQPGRALWRDLDALLLGEDSGGRAGRPAVVDQAAELKGRGLPPREPLRLWVFGYDM
DQAKARCWRWDELTLPLVLLSDEQEDLAAQIREAVDAAEEAARRLRSALKEAWFALGGKDAKGDASAIDE
ESRFWQRLESAFRALLADLEEDDDADEARAAWRKTLRRAALRAFD
>gnl|CDD|187861 cd09730, Cas8a1_I-A, CRISPR/Cas system-associated protein Cas8a1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; signature gene for I-A subtype; also known as TM1802 family
MIESIYEIGKIVLEEESGNENLLEELPENPKEGGNYSHVLKIDFDTEENEINIKGEEEFDKKTFRKYLYK
GQAGNASQDYLPTNKITYLLKTTEPLNKKIKKWFEKSYLLLESKKEILKLKNIKDVLEKNIEKILKDIQD
LKPGENVILTIKIDGKKLLEYDEDYEEFRDKVLKKKVFKDKKAKEKGICSICGKEDEVYGDIDIKFKFYT
TDKPGFASGLDKKNAWKNFPICKECALKLLAGKKYIRNKLSFKFYGLEYYIIPKFIFGDKLLEKELEEIL
EGIKDSSNESKKYKRIEGLEEEILDVLSELKSYLLVNFLFYKKSQAAFKILLHIEDVLPSRFKKIFEALK
KVNSIVKEDNGMNYLLKLTLNQIYYLLPGNKSGSKNEDKYFLELYNSIFSGKPIDYKLLINQFMSKIRKD
FFKKEGEEIRFNVLQAFMLINFLEKLNLLKGGEKMVEKSEELVLDEDIKEFFRKNNEFFNSPQKKALFLL
GVLVGKLLNIQYSKDENKPFLNKLNGLKMDKKKVIRLLNEVSNKLEQYKIYGYNEELYSEMKELIDLEIG
NWKLSKDEISFYFLSGMSL
>gnl|CDD|187862 cd09731, Cse2_I-E, CRISPR/Cas system-associated protein Cse2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Small alpha-helical protein; also known as Cse2/CasB/YgcK family; specific gene for I-E subtype
RGDRAALRRALGPDDVLAVPAFWRLLLSLLPDEATRWERAAYALVALLAAHQKSDRKPGISLGAALARLR
EGSGSDVSERRFRQLLRADTPDELLRRLRRLVRLLKSKGVPVDYGQLARDLLYWNHEDDRVRRRWARDYY
R
>gnl|CDD|187863 cd09732, Csx1_III-U, CRISPR/Cas system-associated protein Csx1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; Some proteins could have an additional fusion with RecB-family nuclease domain; Core domain appears to have a Rossmann-like fold; loosely associated with CRISPR/Cas systems; also known as TM1812 family
KLISFLGTGRYKETTYVFEDREEIKTRFVQEALIEYLKPDEVIVFLTDEAAWSNWEVNQPGLKKHLEKLN
EVLPKLVRIPDGRSEDELWEIFDKITEEVEEGDEVIFDITHGFRSIPFLAFLAALYLKVVKNVTIKGIYY
GAYEAGGTDGRAPVIDLTPLLELLDWIYAVDRFLNTGDAGPLAELLKQLALIKWYLERGLYLQALTLLRE
WLISFLCLEDG
>gnl|CDD|187864 cd09733, Cas6-I-III, CRISPR/Cas system-associated RAMP superfamily protein Cas6. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas6 is an endoribonuclease that generates crRNAs, predicted subunit of Cascade complex; RAMP superfamily protein; Possesses double RRM/ferredoxin fold; also known as AF0072 family
VDLTFPVFGKVLPADHAYPLASALLRLLPWLHEDDGLGIQTLHGPPSGNGDGLLYLSRRSRLRLRVPKEQ
VDLVYPLAGKPLDLGGHALRLGIPKLRLLQPAPVLFARIVVIKGAMEEEAFLQAAQRQLEALGIQAKKML
CGRRRTIKIRRGTVVGRSLMVAGLSPEDSLRLQEEGLGGKRLMGCGLFLPHKS
>gnl|CDD|320705 cd09734, Csb2_I-U, CRISPR/Cas system-associated protein Csb2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Duplicated RAMP domains; also known as GSU0054 family
KYHGRPWGRDVAEPVPEWPPSPWRIFQALVATWALKVDAEDKDVLNWLESLPEPPVFALPPALVANATRH
YVPRAWGRGKKNWHGSATLIFDRPVVLPRESPVIYLWRNVEPDDRSIALLVQIAENLSYFGRVTSWCIAE
VVEEGSVPSVLKELDSYFVWKPHAEEGIVNVRVPNEGSLDELDAKGENGLPLLIRTSILPTQPKNLYPPM
SRLVAYERSLDCFEPSKISHVVDWGERKVNVPRRLLDVNALTPITDIARRAAISTYGKSSKLPSVVSGHG
DDGNILLSNMHVAYLPSPDVEHRDAGKLLGLGLYAPGGYSEFDEIAHQLSLLRMRKLYGYELKNDVNLLL
VGLFGLDPWSETRKWIPLSSSRSWATVTPVILDRYPKVTRAGQWKIQGTPYGVLPDLSGMQIDGPVSQLA
FSIDRAGLPQPSSIEPLPAYEINGTIRQWLTAKRYGVRRGKQSPPPYHVRISWPEEIKGPIIIGAGRYYG
LGLFVP
>gnl|CDD|187866 cd09735, Csy1_I-F, CRISPR/Cas system-associated protein Csy1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins; Predicted subunit of the Cascade complex; signature gene for I-F subtype; also known as Csy1 family
RYEPANWLTDAAKRAGQISLVTHALKFIHPDARGSSLYVVPSSLPQRPEAGSGYLGSANLVHVAIDAVGN
AAALDVYKFLQLEVDGESLLAHLQAGDPSALAALADDTEQLEEWRTGFLAVLTSEGKPTSHKLAKQLYFP
VGDDGYHLLSPLFSSSLAHELYQRIQETRFGEENKEARKARRKNKWHPQGYVDYPNLAVQNFGGTKPQNI
SQLNSERGGKAYLLPSLPPRWKNSIVKPPINLKSIFSVRSEFRYDVRGTLRQLQRFLKGVKKENNLHIRQ
RRDAYLDEIIDELLDYAAELQNLLPAGWSAESECQLKRAEQLWLDPKRAPDDEDFKQEREKGDWPAEVAK
DFARWLNRRLKKDALDLGDVERREWKR
>gnl|CDD|187867 cd09736, Csy2_I-F, CRISPR/Cas system-associated RAMP superfamily protein Csy2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; predicted Cas5 ortholog
LLLPHIRVQNANAISSPLTIGFPSLTAFLGFVHALERKLQTSGIAVELEGVAVVCHDHQLQTYQPSYDRV
FNLTRNPLDKDGGTAAIIEEGRCHLTVSLVIEVSGKDAAGEQEQELIEKLTIILQQMRLAGGSIIPIGPV
EIKSDEKELRKLLRRLLPGFALLDRSDLLAEALQRLQTTNPEATLLDAWLDFAALNHQPLRDEEEAIESA
YSRKKGNGWLVPIPVGYQALSPLYDAGSVSNARDPETPHAFAESLYGLGEWVSPHRLTDLSQLLWRYHYD
QEKGLYLCR
>gnl|CDD|187868 cd09737, Csy3_I-F, CRISPR/Cas system-associated RAMP superfamily protein Csy3. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; predicted Cas7 ortholog
LASVLAFERKLVPSDAVFFAGNWDGRDWVPLEIREKSVRGTISNRLKAAKQSDPAKLDAEIEKANLQTVD
VAALPPDADTLKLRFTLRVLANLGTPSACNDAEYRQKLSQLVNGYKEKQGFKELAKRYAANLANGRFLWR
NRVGAESIQIEVTASDNEKTWEFDALQLSLRGFDQDSEDLDELAKEIAKGLSGENGFVLLDVTAFVRLGA
GQEVYPSQELVLDKGKGEKSKILYQVDVKGEGVAAMHSQKIGNALRTIDTWYPEADELGPIAVEPYGAVT
ERGKAYRQPKDKNDFYTLLDNWVLKDKAPSSEQQHYVMAVLIRGGVFGE
>gnl|CDD|187869 cd09738, Csb1_I-U, CRISPR/Cas system-associated protein Csb1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; Contains several motifs similar to Cas7 family; also known as GSU0053 family
SALVIEADLEPVQGYDRFQPPTFPDLGGAGYNAVALDDGTNMVLVDSVGSQANRIEAELAAWDEAEKGLP
YIRVKVDGATLSSLEEPHRINDAYIRDSELIDNTNFNSTLGNALKSVTNKNAYPLLYYDPNSLLFGVWDS
HRDGRIKLARLVSSFIEAYGVKPVQSGG
>gnl|CDD|187870 cd09739, Cas6_I-F, CRISPR/Cas system-associated RAMP superfamily protein Cas6f. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas6f is an endoribonuclease that generates crRNA; This family is specific for CRISPR/Cas system I-F subtype; Possesses RRM fold; also known as Csy4 family
MDHYIEIRLLPDPEFSLAFLMGKLFAKLHRALVELGSGDIGVSFPKYSLRTLGNKLRLHGDEEALEQLQA
QPWLKGLRDYFHISDVAPVPDDTEYRTVSRVQAKSSPERLRRRRLKRGEETEEEARARDIPDTESRTDLP
FIQLKSLSTGQRFRLFIEQGPLQPEPVSGLFNSYGLSSNATVPWF
>gnl|CDD|187871 cd09740, Csx3_III-U, CRISPR/Cas system-associated protein Csx3. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Small protein in some cases fused to Csx1 (COG1517) family domains
YTLLHIELERPDIDPEDLKELELPPGIDTQRGVVVSGRAPIWLYGFLIHEYHPTPWVAVYDPRLGAVVVA
SHTPEYRPGQVIDV
>gnl|CDD|187872 cd09741, Csx1_III-U, CRISPR/Cas system-associated protein Csx1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; Some proteins could have an additional fusion with RecB-family nuclease domain; Core domain appears to have a Rossmann-like fold; loosely associated with CRISPR/Cas systems; also known as NE0113 family
MKNILLATTGLSPQVVTETLYALLQQGEPPDEVYVITTKDGRVRIALGLLAREFGRYYRGYQRPALKFDE
RHIHVIEDVSGEELDDIRTEEDNEAAADFILRLVRELTQDPGRRLHVSIAGGRKTMGFYLGYAAQLYGRP
QDRLSHVLVTPEFESHRDFFYPPKEPRKLHLPPRNGEVDTSKAEVTLAEIPFVRLRESLPDDLLVGEIPF
SRSVKALQQ
>gnl|CDD|187873 cd09742, Csm6_III-A, CRISPR/Cas system-associated protein Csm6. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; loosely associated with CRISPR/Cas systems; also known as APE2256 family
LSNLGLEDDEKELALRGDDDVERVVEFLKESIEDPRRCSAELNSILSILERGKLGKDDELVLLASDTGAG
RLCAEILKEYLEEKGNGAQVTVTEVLLVTGLGRFFREGLRNLVKALAREVRNYRRSGYKVYINATGGFKA
EIAFAVLLGSLLGAPVYYIHESFSELVELPPLPLSLDPELFEA
>gnl|CDD|187874 cd09743, Csx16_III-U, CRISPR/Cas system-associated protein Csx16. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Small protein often seen in proximity to Csx1 (COG1517) family; also known as VVA1548 family
WFITRHSGAVEWASRQGLDVDRFVIHLDPEQISAGDKVIGTLPVHLAADVCEKGARYFHLSLDIPPELRG
KELTAEQMKACDARLEKYEV
>gnl|CDD|187875 cd09744, Cas8a1_I-A, CRISPR/Cas system-associated protein Cas8a1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; signature gene for I-A subtype; also known as Csx8 family
FDTALEASDWRYSATIVGLIYYFKELEKKYEIKKITIDEIEDDYLLYNSEDINEENYLDFVEKFYEDTLH
HKKVENILKHKEFTEEIIKSINEKLSANTVMKKVFGKIKFDGTNKDEILDLIDKNRHSLIKETFRRKKDL
YDNYCNTNRLFEDDNSPCRLKGYCFDPGKKGKSTGYNFVSSTFDYFDDKIFDFIPFAFTGSFEAFFINDN
LDIEILKKSNKAIKEKKNEETEGNQNSVPLRKTLFNILQEKVDYIKYDVEVILKNRDKEYFETWYLRNES
IKIFKEIEDFSYKDIRFWYKITDKYYFNLLDEVFSAILNLSLLDNSIEYLLKDKNSFSYAINELIKINQL
IRNGGKEMDENLKKAIACAKAVVKKFINSLNKLASYKQKLLSSVVFKDHDRICDILLQLSVYSGVYFSFA
YDLIEDFEQNKDLAYTFINAL
>gnl|CDD|187876 cd09745, Cas8a2_I-A, CRISPR/Cas system-associated protein Csa8a2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; signature gene for I-A subtype; also known as Csx9 family
MSWVVMDAGLEPDPEELADALEGALDSLKSRAMINTSKIGRNDRNSFDRVLSAWFGRSAPETYGELFELV
INETIKLLRSGKIDPAKSLSTIKTDKNGTYLGQAYNGEQAILPAIIKQPEYYEFQSEFLKPTTGQKAQIR
MDPLWFSFMALGFFTSFAGFIRGKYYLMTKPGIEVFWPYEVEEIIEDGILPLTDAGASGRISLDTEELYE
MKLAMKLAEEGRKVIEEVYPVTLHVISLEGQVYTELKTLQLNLKELSNYLAEYVKKIENYRVGGVDLLVE
LKEGGATVEKYPLWALVDIAEKELWKGVSGDREMLAYIFVKDLYRAINSGRKELIEDSIFRLFRQGRALL
EGSGRASGEFRKVMRTFMWEEHLEVLL
>gnl|CDD|187877 cd09746, Csm6_III-A, CRISPR/Cas system-associated protein Csm6. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; loosely associated with CRISPR/Cas systems
NYDVEIIELRYEEIDNPQQFDIFYPVFEKELIILHNAYPDCEILLNLSSGTPQMKSALHLINLTTPFNVK
AVQVSTPARLSNEGINYSNDNYDLEESWKVNEDNKPGTNNRTQEVNSDNLRYLLLREAAISLINAFDYSA
ALAILASVAEFVPEDVIHLLMGAQHRKKLDLREAKKKSHLVNPDIFPVKSDDAAKKLLEYYLLLDLLQNR
EQLADFLRGAKPAAEFVLECFIRKHCPRLIKYCVNKRYLNDHYWLKRDKLAEKDPSLLCYYDLRFPNDSD
FSVSTLLPLIEFLCILGGREPDSQLLLAANYMRSVEGKIRNPAAHNIVAIKEDQFMQLVGLLSASLLKDL
QWMFKITYPQYFNILENDWNYYDRMNKEIISR
>gnl|CDD|187878 cd09747, Csx1_III-U, CRISPR/Cas system-associated protein Csx1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; Some proteins could have an additional fusion with RecB-family nuclease domain; Core domain appears to have a Rossmann-like fold; loosely associated with CRISPR/Cas systems; also known as Cas02710 family
EPLILSIAGHRPERVVFLASDESHPKLPEVREDTGLKAKFEFCLIEDANDVLECYKKARDVLEKWGELRE
EVIVDYTGGTKTMTAGLALAAFLYRVRFSYVGGETDKDLGRVEPGTERLRILENPYAAFGDLERRQAIRL
FNKGDYGSALRILEDLARRVLDQPDYAAYKLLSEGYLAWDSFDHEEAADYLSKVLALLHLLNAEREGLEA
LTAVLRALERILNDLAGALNALKKKYYALLGDLLANAERRAAEGRYDDAAARLYRALELLSQHRLATYGI
DTSNPDFDKALPEGLRSAYRQKRGDSGFIVIKIGLLAGYELLEALGDDVGRRFLGEINELLQALQIRNHS
ILAHGFRPVSEEAYEEFRDVVEELLNRL
>gnl|CDD|187879 cd09748, Cmr3_III-B, CRISPR/Cas system-associated RAMP superfamily protein Cmr3. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; This protein is a subunit of Cmr complex
IEPLDVLFFRDGRPFGPGEGARAQSLFPPSPSTLAGAIRAALGRAAGLDFGDFEACSGENDELGKLALRG
PLLLREDENEPLFPAPLDLLVKRKKEDGLRFLLRLEPRPFSTGTDPEDALEGLLEPDIGDKKKPAPGYLS
WEGLQKYLLGEAPDAREVVEGSELWEPETRIGIALDPETRTVEEGQLYQTEGIRLKEGVGLALGVEGDGP
NELELPEPGLLRLGGEGRLAALEICEAGLPAWPAPSKGAIAAKGRFRLVLLTPALFGRGWLPPWLLATPK
GVEAELVAAAVGKPVPISGWDLANNRPKPTRRAVPAGSVYFLELPNGEDAALLEASDSKLDDEQDRKDGF
GLALIG
>gnl|CDD|187880 cd09749, Cmr5_III-B, CRISPR/Cas system-associated protein Cmr5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Small alpha-helical protein; signature gene for subtype III-B
REQQRAAHAYEKVKAVKGAGKKLKKKYKSLVKKLPALILQNGLGQALAFLLAKGKKNGKNSKLLEHLASW
LRERDKLQDGKGREALLEAIITADLKEYMRATREVLALLVWLRRFAQAV
>gnl|CDD|187881 cd09750, Csa5_I-A, CRISPR/Cas system-associated protein Csa5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Predicted transcriptional regulator of CRISPR/Cas system; contains DNA binding HTH domain; also known as Csa5 family
FFVYSENPTYVDRIGNALSKEAVEKVLYEAQRIFRSGIERGEIRLQTGENGRRYIAEKEGEYIVVGYLPS
DEDVEQFLEDVERDIYYARKVGALAMAYPNR
>gnl|CDD|187882 cd09751, Cas8a2_I-A, CRISPR/Cas system-associated protein Csa8a2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Zn-finger domain containing protein, distant homologs of Cas8 proteins; signature gene for I-A subtype; also known as Csa4 family
VPELYTPGHSPYTDTLIMYGIVRSLARSGVVEGRVEPTGERYVIETEVDNRTLADIEYGLLRALEEELHY
AFLGREPLNGRLRSDKDFSAGASILNPYWDRVPAELEVFTLEKELKRGHKSLKGRGLLTVPLTLMPSAGK
YLHKSRKPKEEKPYRVCKYCYALAWLGFHYYASYIYVKDGRSRVVHITPAPPYEELEDIELLLQKDEAKK
ILGVMGNLVDNVENLLAALLYHLLTGETLEELDTESAFWVVSYGLESDNGQAVRSFRELELSRLMDFLWY
LKARAFYHTIRWPKFLDQLARADGAYLLEILLQLIEAVLNADEDGLYGALRSLKCSGYSGEAWQVDALAE
ILVER
>gnl|CDD|187534 cd09752, Cas5_I-C, CRISPR/Cas system-associated RAMP superfamily protein Cas5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas5 is a RAMP superfamily protein; Subunit of the Cascade complex; in subtype I-C this protein might be the endoribonuclease that generates crRNAs; also known as DevS family
IRLKVWGDYACFTRPEMKVERVSYDVPTPSAARGILEAIYWKPAIRWVIDEIRVLKPIRTESIRRNEVGS
KARVGGLPLLIEEGRQQRAYTYLRDVAYVIEAHFELNEHRPADDRVEKKHEIFARRARKGQCFHDPYLGT
REFPAYFEPCDFGEGEGAYDNGGERDLGWMLHDFDFPDEELTPRFFRARMKNGVIKVP
>gnl|CDD|187883 cd09753, Cas5_I-A, CRISPR/Cas system-associated RAMP superfamily protein Cas5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas5 is a RAMP superfamily protein; Subunit of the Cascade complex
IGVKVFLLLHWGFSVRVPEASKVRPSLPLPPPTTLLGALSYGKFRGGGVKGGTLKEKAIRRFGVFARGKV
YGENVNFEIVVALSEEEKEDLEKALWSITRLGSKESLVSVEDVEVVKVEREKGEVKTAYYFPAVVGGSHG
GGTLQAV
>gnl|CDD|187884 cd09754, Cas8a1_I-A, CRISPR/Cas system-associated protein Cas8a1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; signature gene for I-A subtype; also known as CXXC_CXXC family
DESKKKYNCIFCGRRNSELKKVLSFENPLGGSTGRKKNYFWNGKNGADICPICELIYQFSPLGFT
>gnl|CDD|187885 cd09755, Cas2_I-E, CRISPR/Cas system-associated protein Cas2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas2 is present in majority of CRISPR/Cas systems along with Cas1; RNAse specific to U-rich regions; Possesses an RRM/ferredoxin fold
RAGVYVGNVSARVRERLWEKVTEGIGDGSAVMVWSTNNEQGFSFRTLGDPRREPVDFDGLLL
>gnl|CDD|187886 cd09756, Cas5_I-E, CRISPR/Cas system-associated RAMP superfamily protein Cas5. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas5 is a RAMP superfamily protein; Subunit of the Cascade complex
LLLRLEGPLQSWGEVSRFGRRDTGDFPTKSALLGLLAAALGIRRDEPEELLALLRFTILSYRDYLADAVF
TVALTEGAPPLLEELAAALRSPVFPLYLGRKSCPPARPLFLGLFEAADLLAALAALPWQASRAQR
>gnl|CDD|187887 cd09757, Cas8c_I-C, CRISPR/Cas system-associated protein Cas8c. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Zn-finger domain containing protein, distant homologs of Cas8 proteins; signature gene for I-C subtype; also known as Csd1 family
LQALYEYYERLAAEPDSGLPPLGHSTKKIHFEVVLDEDGNFLDIEDTREGDGKKKALMLIPATEKGRSSG
IAPNPLWDKLSYVLGDFAKGGGKEAAEQHEAFIELLEEWLAETEDPGVKAVLRFLKKWELEEDLIEAIKK
EVEEELKDANVRFRVEGDGELVHEDPAVQQAWARYYAATEGKKGLCLVTGEEAPIARLHPAIKGVQGSGA
KLVSFNDDGFTSYGKEQGENAPVSYEAAFKYHTALNWLLRRQSYQRLQIGDATTVFWAEKSSPAEDPFAA
LFDPPDDTKPDDAATTQAVALLLKKPITGYRADLDDDTRFYVLGLAPNAGRLSVRFWRELTVGEFLERLE
RHFDDLAWEPSYGGAPSPPDIARLLYGTARDGKTENIPPNLAGRLLRSILDGQPYPRSLLSAALRRIRAD
VGMEEWEWERAALIKAALFRGYRIKSNEEEYPMSLDPENTNRGYLLGRLFAVLEKIQERALGGGINATIA
DRYYGAASATPASVFPTLLRLLQPHLAKLRKEKRAVNLERLIGEILDGLNPDDFPRTLSLEEQGEFALGY
YHQRQALFT
>gnl|CDD|213408 cd09758, Csn2, CRISPR/Cas system-associated protein Csn2. Csn2 is a Nmeni subtype-specific Cas protein, which may function in the adaptation process which mediates the incorporation of foreign nucleic acids into the microbial host genome. Csn 2 may interact directly with double-stranded DNA. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA. Csn2 has been predicted to be a functional analog of Cas4 based on anti-correlated phyletic patterns; also known as SPy1049 family
MKINFSLLDEPIEIEKATILVIEDVEVFAQLVKLFYQYDEESELKLFDDKQKSLKSSELMLVTDILGYDI
NSSAILKLIYADLEDQLNEKPEVKSMIEKLTNTITELIGYECLEHELDLEYDEITIQELFKALGIKIETK
SDTIFEKVFEILQVFKYLSKKKLLVFVNVGAYLTKDEIAELLEYISLNNVNVLFLEPRKIEGLPQYILDE
DYFLLYEN
>gnl|CDD|187889 cd09759, Cas6_I-A, CRISPR/Cas system-associated RAMP superfamily protein Cas6. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas6 is an endoribonuclease that generates crRNAs, predicted subunit of Cascade complex; RAMP superfamily protein; Possesses double RRM/ferredoxin fold
MRIEIRLRPENDPFKIPFNHQYYLASAIYNKIASSNPRLAQELHSSKGFKFFTFSRLFIRKRRIRKEGII
RKLGYKASFYFSSPNPEVIESLVEGLLEDPEIRLGNVDFIVEEIKVLPEPEFKDGSTFVTLSPIYVRTKK
EQNGKLKIYDLYPNESKFYENLKKNLVKKYVEFYGSKPEKSNFEMEVLNFKPKRIRIKPDTYHRCSLMVF
RAWGDPELLKFGYDAGFGEKNSMGFGMVKV
>gnl|CDD|187890 cd09760, Cas6_III, CRISPR/Cas system-associated RAMP superfamily protein Cas6. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas6 is an endoribonuclease that generates crRNAs, predicted subunit of Cascade complex
MSFSLQLTRLKARLYFPQYHLPPFLGNKFRGGFGSVLLKAVCSYLKPSCNICKSVDDCLYHALYTRDRQK
RGRSQPVRPIVFIPPFFGRSVSGRGELTLYINVFGDYVKYLPHIIYGLRYLGKMGLNATSKYEIVSISDA
ISGKEVYDGETVFVENLSSIELGKIKPREVEKEIEVDYLTPMEAKTPINLPFLIHIVRRRLILFVNEYGS
GEVPEFYCEAETLESSWEKHELHHRSKRQGLRSFFGVTGRARYSISEIDDNALTLLSIGELIGGGAKASF
GMGFFRIRS
>gnl|CDD|187662 cd09761, A3DFK9-like_SDR_c, Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs. This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAML
EKLGRIDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSE
PDSEAYAASKGGLVALTHALAMSLGPDIRVNCISPGWINTTEQQEFTAAPLTQEDHAQHPAGRVGTPKDI
ANLVLFLCQQDAGFITGETFIVDGGMTKKMIY
>gnl|CDD|187663 cd09762, HSDL2_SDR_c, human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs. This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHPKLPGTIYTAAEEIEAAGGKALPCIVDIRD
EDQVRAAVEKAVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPH
ILNLSPPLNLNPKWFKNHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWPRTAIATAAMNMLGGVDVAA
CCRKPEIMADAAYAILTKPSSEFTGNFLIDEEV
>gnl|CDD|187664 cd09763, DHRS1-like_SDR_c, human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs. This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver, a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs
LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEA
LFERVAREQQGRLDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGK
GLIVIISSTGGLEYLFNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEGSWH
AKERDAFLNGETTEYSGRCVVALAADPDLMELSGRVLITGELAREYGFTDVDGRQ
>gnl|CDD|187733 cd09764, Csb3_I-U, CRISPR/Cas system-associated RAMP superfamily protein Csb3. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; Might be a catalytically active RNA endoribonuclease
TIAGDYTSALTHLALVGLASILEQAHPQRVTRLWWSDAVPARQLTVEEGDAETEAAHIVRLHAQRWAPSS
WLNARNSYGTMKNHATFSPRLGEISGPEGWKRLQKDREHAIDSLRTELDYRYIGALGSPGYWSGWFPEKN
KKEYPDHGASRWEMKTRNRGQEFVGYRLRPLCEEVATWSAEKILDGLIGTTEVDDLIGKEKSLTATGFTV
PSPTDTALALCALTGMSNFPVTHVAHRGLSITAGAWPSNDVAPRLLVLPLSIENITPARLRTVLRSHALA
RVVNYVCHEESGVSDDREVLLAADSREWLREKGVDACCRFPVKKSDNASAPERWLLRGKLI
>gnl|CDD|187734 cd09765, Csx14_I-U, CRISPR/Cas system-associated protein Csx14. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein containing C-terminal alpha-helical domain resembling Cas8a2, also known as GSU0052
SIPVDPTNPGQFFACCGLLELADRLWDGAEGWFDKDGFFWSDRETHVRFTLTTPATLDPVLTVLRFLTQA
EDVALKRYHSLIRDSKKIRTVETKNREKPCLLKAWTALPIFLQAPFVRVPDWHWVDSSGVTNVKTWAGNQ
SVAKIANLMLSALKSVSWDIHSISAHLFRFAHPQSLPFRFDWRRDGVYIPLDVGFSPNDHKKKVRVGRPL
LELLAFVGLQRFRPLRLQANLRYRYGAWFGPLVPTVAARAALGLSNPGFIRAFEFRLLYRTK
>gnl|CDD|187735 cd09766, Csx15_I-U, CRISPR/Cas system-associated protein Csx15. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Small protein loosely associated with CRISPR/Cas systems; some are fused to AAA ATPase domain, also known as TTE2665 family
IPEVIDIPGQIDEQRPLVPQIEKLVDRVGLTPEEWQTIPILVNPPGLAPLAAALLAELHGRLGYFPPVVR
LRPVAGSVPPRYEVAEIINLQALREEARRRR
>gnl|CDD|187705 cd09767, Csx17_I-U, CRISPR/Cas system-associated protein Csx17. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins; Predicted subunit of the Cascade complex
LKALGVFRLVSEQKDPDARGWWSNDMFRITTRLDAADLVKFFLEEYQPTPIIAPWNGGSGFYRGDNEEAL
EAIINTKSSRFRPYRDDIEAMLEASELKKLTEKPKRGDKTEILARLRAELPDEVLEWLDAAVILTDDRRG
YPPLLGTGGNDGRLDFTNNYMQRLIEVLDPKGGADDKAARFLESSLFGEPVPGLSKLKIGQFFPGAAGGP
NSGLGFEAGDTVNPWDDVLMLEGGTLLAAGAVRKREGASDSFLAFPFTVRPSGGGFGSSSFSDEAGARAE
IWLPLWNRPASLGELKQLFSEGRAQLGGRQARNGLDFARAVASLGVDRGITAFQRYAFLKRSGRAKLAVP
LGRFAVRRKPSADLLNELDRWLDRLRFRLRAPRKPPPSALSALRPIEEAIFEFCQHGSPTKFQDLLVALG
QLERQLALSAAKSGRRVTRPLPGLSPDWIEAADDLSPEFRIAAALASIRDGGKKGDRTSLGPAPINRRLR
WKWVEPESQVVWTGGDLARNLAAVLTRRLLDEERKGRPNTPIVGPCAASLTDILRFLAGETDDRRIADLI
WGLSLIDNAARSVLNQSGADEEVANTSLPRAYALLKLLFVPDELLREALEVEIDRSLPRPPVPEVLALLQ
AQRVDRACELATRRLRASGLAP
>gnl|CDD|188874 cd09768, Luminal_EIF2AK3, The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3. The Luminal domain is a dimerization domain present in eukaryotic translation Initiation Factor 2-Alpha Kinase 3 (EIF2AK3), also called PKR-like Endoplasmic Reticulum Kinase (PERK). EIF2AK3 is a serine/threonine protein kinase (STK) and a type I transmembrane protein that is localized in the endoplasmic reticulum (ER). As a EIF2AK, it phosphorylates the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis: General Control Non-derepressible-2 (GCN2), protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PERK. PERK contains a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize through its luminal domain and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR
SLIIVSTLDGKLTALDIENSGKKVWSLDAGSGPLVSSSLSTLELINNGKSVRLIPSLDGSLYQFDGESIE
AIPFTAESLLSSSYKLGDDSVLVGGKEVTSYGINPYTGKLRYICSAEGCKSSDTEENESNDDVLIVRRTT
QTVRAVDPRTGSERWNLSVGQYELSLVGSIECKLGEEDESNSAVSDVEIKVSVPDGKIMAVSKSAPGRLI
WEYKFESPIASAWQLSDGKLRPISLFDDTTSDFTTNTEQSNDEKDNAEARPATEPSLYLGMYNGQLYIQP
SDRIREEADTSSKILSQLNDE
>gnl|CDD|188875 cd09769, Luminal_IRE1, The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, Inositol-requiring protein 1. The Luminal domain is a dimerization domain present in Inositol-requiring protein 1 (IRE1), a serine/threonine protein kinase (STK) and a type I transmembrane protein that is localized in the endoplasmic reticulum (ER). IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is a kinase receptor that also contains an endoribonuclease domain in the cytoplasmic side. It plays roles in the signaling of the unfolded protein response (UPR), which is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1 acts as an ER stress sensor and is the oldest and most conserved component of the UPR in eukaryotes. During ER stress, IRE1 dimerizes through its luminal domain and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and Xbp1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). IRE1alpha is expressed in all cells and tissues while IRE1beta is found only in intestinal epithelial cells
EDLLLVSTVDGGLHAVDRKTGKILWSLKAEDPLVEVPHHSTLSIDGPTFIVEPRDGSLYVLNPGNEGLKK
LPFTIPQLVQSSPCRSSDGILYTGSKQTTWYTVDPRTGEKIQVLGSGGADSNCPESCVDPDDDEQSECSS
SSTIYIGRTEYTVTIYDSKTREPIWNVTYSDYTPNSNDRDLQSQYSKTYDLRYIASSSDGSLVTFDRDTG
RVLWVQNLPSPVVAVFDVLRPEPGLVKLPFPPVALETLQYLEDESPDFSSSEDKLRPTVYIGQTENGGLY
ALSSKELLIGVHELP
>gnl|CDD|197361 cd09803, UBAN, polyubiquitin binding domain of NEMO and related proteins. NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well
GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKE
QLAEQLEYLQRENQELK
>gnl|CDD|197362 cd09804, Dcp1, mRNA decapping enzyme 1 (Dcp1). mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of the decapping complex which catalyzes the removal of the 5' cap structure of mRNA. This decapping reaction is an essential step in mRNA degradation, by exposing the 5' end for exonucleolytic digestion. Dcp1 binds to the N-terminal helical domain of catalytic subunit Dcp2 and enhances its function by promoting Dsp2's closed conformation which is catalytically more active
EARQALNLKVLQRHDPYIVSILDTASHVAVYEFDDDTNEWEKTDVEGTLFVYKRSAEPRYGFIILNRLST
ENLIEPITPELELELQDPYLIYRNANGEIYGIWFYDEEDRERIYKLLERLL
>gnl|CDD|187665 cd09805, type2_17beta_HSD-like_SDR_c, human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs. 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWV
KEHVGEKGLWGLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGG
RVPFPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQAKKLWERLPPEVK
KDYGEDYIDELKNKMLKYCSRASPDLSPVIDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFL
L
>gnl|CDD|187666 cd09806, type1_17beta-HSD-like_SDR_c, human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs. 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
TVVLITGCSSGIGLHLAVRLASDPSKRFKVYATMRDLKKKGRLWEAAGALAGGTLETLQLDVCDSKSVAA
AVERVTERHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVG
GLQGLPFNDVYCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVLDRTADDITTF
HFFYQYLAHSKQVFREAAQNPEEVAEVFLTAIRAPKPPLRYFTNERYL
>gnl|CDD|212495 cd09807, retinol-DH_like_SDR_c, retinol dehydrogenases (retinol-DHs), classical (c) SDRs. Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13, and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVIVRHLDLASLKSIRAF
AAEFLAEEDRLDVLINNAGVMRCPYSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAH
KAGKINFDDLNSEKSYNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRHTGIHHLFL
STLLNPLFWPFVKTPREGAQTSIYLALAEELEGVSGKYFSDCKLKEPAPEAMDEETARRLWEIS
>gnl|CDD|187668 cd09808, DHRS-12_like_SDR_c-like, human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs. Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETESGNQNIFLHIVDMSDPKQVWEF
VEEFKEEGKKLHVLINNAGCMVNKRELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSSGGM
LVQKLNTNNLQSERTAFDGTMVYAQNKRQQVIMTEQWAKKHPEIHFSVMHPGWADTPAVRNSMPDFHARF
KDRLRSEEQGADTVVWLALSSAAAKAPSGRFYQDRKPVSTHLPLA
>gnl|CDD|187669 cd09809, human_WWOX_like_SDR_c-like, human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs. Classical-like SDR domain of human WWOX and related proteins. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWHKARVEAMTLDLASLRSVQRF
AEAFKAKNSPLHVLVCNAAVFALPWTLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSSESH
RFTDLPDSCGNLDFSLLSPPKKKYWSMLAYNRAKLCNILFSNELHRRLSPRGITSNSLHPGNMMYSSIHR
NWWVYTLLFTLARPFTKSMQQGAATTVYCATAPELEGLGGMYFNNCFRCLPSPEAQSEATAQQLWELSER
LIQE
>gnl|CDD|187670 cd09810, LPOR_like_SDR_c_like, light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs. Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
KGTVVITGASSGLGLAAAKALARRGEWHVVMACRDFLKAEQAAQEVGMPKDSYSVLHCDLASLDSVRQFV
DNFRRTGRPLDALVCNAAVYLPTAKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQRSENASPRIVIVG
SITHNPNTLAGNVPPRATLGDLEGLAGGLKGFNSMIDGGEFEGAKAYKDSKVCNMLTTYELHRRLHEETG
ITFNSLYPGCIAETGLFREHYPLFRTLFPPFQKYITKGYVSEEEAGERLAAVIADPSLGVSGVYWSWGKA
SGSFENQSSQESSDDEKARKLWEISEKLVGL
>gnl|CDD|187671 cd09811, 3b-HSD_HSDB1_like_SDR_e, human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs. This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
VCLVTGGGGFLGQHIIRLLLERKEELKEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRAC
QGVSVVIHTAAIVDVFGPPNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFNGVE
DTPYEDTSTPPYASSKLLAENIVLNANGAPLKQGGYLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLF
PRIKGSGVNPLVYVGNVAWAHILAAKALQVPDKAIRGQFYFISDDTPHNSYSDFNYELLKELGLRLKTSW
WYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAVALTNSMFTFSYLKAQRHFGYMPLFSWEESKERT
AKWV
>gnl|CDD|187672 cd09812, 3b-HSD_like_1_SDR_e, 3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs. An uncharacterized subgroup of the 3b-HSD-like extended-SDR family. Proteins in this subgroup have the characteristic active site tetrad and NAD(P)-binding motif of extended-SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
SVLITGGGGYFGFRLGCALAKSGVHVILFDIRRPQQELPEGIKFIQADVRDLSQLEKAVAGVDCVFHIAS
YGMSGREQLNRELIEEINVRGTENIIQVCVRRRVPRLIYTSTFNVIFGGQPIRNGDESLPYLPLDLHVDH
YSRTKSIAEQLVLKANNMPLPNNGGVLRTCALRPAGIYGPGEQRHLPRIVSYIEKGLFMFVYGDPKSLVE
FVHVDNLVQAHILAAEALTTAKGYIASGQAYFISDGRPVNNFEFFRPLVEGLGYSFPSLRLPLSLVYFFA
FLTEMVHFALGPICNFQPLLTRTEVYKTGVTHYFSIEKARAELGYEPQPFDLQDAVEWF
>gnl|CDD|187673 cd09813, 3b-HSD-NSDHL-like_SDR_e, human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs. This subgroup includes human NSDHL and related proteins. These proteins have the characteristic active site tetrad of extended SDRs, and also have a close match to their NAD(P)-binding motif. Human NSDHL is a 3beta-hydroxysteroid dehydrogenase (3 beta-HSD) which functions in the cholesterol biosynthetic pathway. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Mutations in the gene encoding NSDHL cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. This subgroup also includes an unusual bifunctional [3beta-hydroxysteroid dehydrogenase (3b-HSD)/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif
SCLVVGGSGFLGRHLVEQLLRRGNPTVHVFDIRPTFELDPSSSGRVQFHTGDLTDPQDLEKAFNEKGPNV
VFHTASPDHGSNDDLYYKVNVQGTRNVIEACRKCGVKKLVYTSSASVVFNGQDIINGDESLPYPDKHQDA
YNETKALAEKLVLKANDPESGLLTCALRPAGIFGPGDRQLVPGLLKAAKNGKTKFQIGDGNNLFDFTYVE
NVAHAHILAADALLSSSHAETVAGEAFFITNDEPIYFWDFARAIWEGLGYERPPSIKLPRPVALYLASLL
EWTCKVLGKEPTFTPFRVALLCSTRYFNIEKAKKRLGYTPVVTLEEGIERTLQWF
>gnl|CDD|381167 cd09815, TP_methylase, S-AdoMet-dependent tetrapyrrole methylases. This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide
VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAILKDGKRIYDLHDPNVEEEMAELLLEEAR
QGKDVAFLSPGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDLGESFLFVTASDLLENPR
LLVLKALAKERRHLVLFLDGHRFLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKELRAERTERG
KPLTTILVG
>gnl|CDD|188648 cd09816, prostaglandin_endoperoxide_synthase, Animal prostaglandin endoperoxide synthase and related bacterial proteins. Animal prostaglandin endoperoxide synthases, including prostaglandin H2 synthase and a set of similar bacterial proteins which may function as cyclooxygenases. Prostaglandin H2 synthase catalyzes the synthesis of prostaglandin H2 from arachidonic acid. In two reaction steps, arachidonic acid is converted to Prostaglandin G2, a peroxide (cyclooxygenase activity) and subsequently converted to the end product via the enzyme's peroxidase activity. Prostaglandin H2 synthase is the target of aspirin and other non-steroid anti-inflammatory drugs such as ibuprofen, which block the substrate's access to the active site and may acetylate a conserved serine residue. In humans and other mammals, prostaglandin H2 synthase (PGHS), also called cyclooxygenase (COX) is present as at least two isozymes, PGHS-1 (or COX-1) and PGHS-2 (or COX-2), respectively. PGHS-1 is expressed constitutively in most mammalian cells, while the expression of PGHS-2 is induced via inflammation response in endothelial cells, activated macrophages, and others. COX-3 is a splice variant of COX-1
HFLLTHFRWLWNIVNRIPFLRRLINRLVINSRVDLIPSRPTPLSTMHDYTSWESLTDRTYYGRHLPPVPR
DCPTELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLRTDPGDPRRNTSNHGIDLSQIYGLT
EARTHALRLFKDGKLKSQMINGEEYPPYLFEDGGVKMEFPPLVPPLGDELTPEREAKLFAVGHERFNLTP
GLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELA
FNEPWQRQNRIALEFNLLYRWHPLVPDTFNIGGQRYPLSDFLFNNDLVVDHGLGALVDAASRQPAGRIGL
RNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYTSFEELTGDPEVAAELEELYGDVDAVEFYVGL
FAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGFDIVKTATLQDLVCRNVKGGCP
>gnl|CDD|188649 cd09817, linoleate_diol_synthase_like, Linoleate (8R)-dioxygenase and related enzymes. These fungal enzymes, related to animal heme peroxidases, catalyze the oxygenation of linoleate and similar targets. Linoleate (8R)-dioxygenase, also called linoleate:oxygen 7S,8S-oxidoreductase, generates (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate as a product. Other members are 5,8-linoleate dioxygenase (LDS, ppoA) and linoleate 10R-dioxygenase (ppoC), involved in the biosynthesis of oxylipins
SKLRDKLTGGLVDTLWDDLPHPPDSYLGDNYKYRKADGSNNNILNPRLGAAGSPYARSVPPKHDQPGVLP
DPGLIFDTLLARDTGKFHPNGISSMLFYLATIIIHDIFRTDHRDMNINNTSSYLDLSPLYGSNQEEQNKV
RTMKDGKLKPDTFSDKRLLGQPPGVCALLVMFNRFHNYVVEQLAQINEGGRFTPPGDKLDSSAKEEKLDE
DLFQTARLITCGLYINIVLHDYVRAILNLNRTDSTWTLDPRVEIGRSLTGVPRGTGNQVSVEFNLLYRWH
SAISARDEKWTEDLFESLFGGKSPDEVTLKEFMQALGRFEALIPKDPSQRTFGGLKRGPDGRFRDEDLVR
ILKDSIEDPAGAFGARNVPASLKVIEILGILQAREWNVATLNEFRKFFGLKPYETFEDINSDPEVAEALE
LLYGHPDNVELYPGLVAEDAKPPMPPGSGLCPGYTISRAILSDAVALVRGDRFYTVDYNPNNLTNWGYAE
VSPDPDVAFGGVFYKLLLRALPNWFPGNSVYAHYPFTTPEENKEILKKLGRADKYSFDRP
>gnl|CDD|188650 cd09818, PIOX_like, Animal heme oxidases similar to plant pathogen-inducible oxygenases. This is a diverse family of oxygenases related to the animal heme peroxidases, with members from plants, animals, and bacteria. The plant pathogen-inducible oxygenases (PIOX) oxygenate fatty acids into 2R-hydroperoxides. They may be involved in the hypersensitive reaction, rapid and localized cell death induced by infection with pathogens, and the rapidly induced expression of PIOX may be caused by the oxidative burst that occurs in the process of cell death
RTADGSYNDLDNPSMGSVGTRFGRNVPLDATFPEDKDELLTPNPRVISRRLLARTEFKPATSLNLLAAAW
IQFMVHDWFSHGPPTYINTNTHWWDGSQIYGSTEEAQKRLRTFPPDGKLKLDADGLLPVDEHTGLPLTGF
NDNWWVGLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAILAHPTLEI
AMRANWWGLLGERLKRVLGRDGTSELLSGIPGSPPNHHGVPYSLTEEFVAVYRMHPLIPDDIDFRSADDG
ATGEEISLTDLAGGKARELLRKLGFADLLYSFGITHPGALTLHNYPRFLRDLHRPDGRVIDLAAIDILRD
RERGVPRYNEFRRLLHLPPAKSFEDLTGDEEVAAELREVYGGDVEKVDLLVGLLAEPLPPGFGFSDTAFR
IFILMASRRLKSDRFFTNDFRPEVYTPEGMDWVNNNTMKSVLLRHFPELAPALRGVENAFAPWR
>gnl|CDD|188651 cd09819, An_peroxidase_bacterial_1, Uncharacterized bacterial family of heme peroxidases. Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins
GRFGRMFPKLPPPAFDPATLAILAALGAAMGDADPGAPAGDNESGIPAGYTYLGQFIDHDITLDTTSSLA
PRQIDPAELRNFRTPALDLDSVYGGGPDGSPYLYDQATPNDGAKLRVGRESPGGPGGLPGDGARDLPRNG
QGTALIGDPRNDENLIVAQLHLAFLRFHNAVVDALRAHGTPGDELFEEARRLVRWHYQWLVLNDFLPRIC
DPDVVDDVLANGRRFYRFFREGKPFMPVEFSVAAYRFGHSMVRASYDYNRNFPDASLELLFTFTGGGEGD
LGGFSPLPENWIIDWRRFFDIDGSAPPQFARKIDTKLAPPLFDLPNGGVGLAPPMKSLAFRNLLRGYRLG
LPSGQAVARALGIAPLTADELGDGEDGAPAVAGGGLHEATPLWFYILKEAEVRGGGNRLGPVGSRIVAEV
FIGLLEGDPSSYLSLGFNPDWTPTLPSATPGIFTMADLLRFAGVL
>gnl|CDD|188652 cd09820, dual_peroxidase_like, Dual oxidase and related animal heme peroxidases. Animal heme peroxidases of the dual-oxidase like subfamily play vital roles in the innate mucosal immunity of gut epithelia. They provide reactive oxygen species which help control infection
YDGWYNNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGEERPNPRSLSNLLMKGESGLPSTRNRTALLVFF
GQHVVSEILDASRPGCPPEYFNIEIPKGDPVFDPECTGNIELPFQRSRYDKNTGYSPNNPREQLNEVTSW
IDGSSIYGSSKAWSDALRSFSGGRLASGDDGGFPRRNTNRLPLANPPPPSYHGTRGPERLFKLGNPRGNE
NPFLLTFGILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGTNVPPYTGYK
PHVDPGISHEFQAAAFRFGHTLVPPGVYRRNRQCNFREVLTTSGGSPALRLCNTYWNSQEPLLKSDIDEL
LLGMASQIAEREDNIIVEDLRDYLFGPLEFSRRDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDIN
PDLFKKDPELLERLAELYGNDLSKLDLYVGGMLESKGGGPGELFRAIILDQFQRLRDGDRFWFENVKNGL
FTAEEIEEIRNTTLRDVILAVTDIDNTDLQKNVFFWKNGDPCPQPKQLTENMLEPCTPLTVYDYFEGS
>gnl|CDD|188653 cd09821, An_peroxidase_bacterial_2, Uncharacterized bacterial family of heme peroxidases. Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins
PNVAPDAGLSAPYNSWMTFFGQFFDHGLDFIPKGGNGTVLIPLPPDDPLYDLGRGTNGMALDRGTNNAGP
DGILGTADGEGEHTNVTTPFVDQNQTYGSHASHQVFLREYDGDGVATGRLLEGATGGSARTGHAFLDDIA
HNAAPKGGLGSLRDNPTEDPPGPGAPGSYDNELLDAHFVAGDGRVNENIGLTAVHTVFHREHNRLVDQIK
DTLLQSADLAFANEAGGNNLAWDGERLFQAARFANEMQYQHLVFEEFARRIQPGIDGFGSFNGYNPEINP
SISAEFAHAVYRFGHSMLTETVTRIGPDADEGLDNQVGLIDAFLNPVAFLPATLYAEEGAGAILRGMTRQ
VGNEIDEFVTDALRNNLVGLPLDLAALNIARGRDTGLPTLNEARAQLFAATGDTILKAPYESWNDFGARL
KNPESLINFIAAYGTHLTITGATTLAAKRAAAQDLVDGGDGAPADRADFMNAAGAGAGTVKGLDNVDLWV
GGLAEKQVPFGGMLGSTFNFVFEEQMDRLQDGDRFYYLSRTAGLDLLNQLENNTFADMIMRNTGATHLPQ
DIFSVPDYDT
>gnl|CDD|188654 cd09822, peroxinectin_like_bacterial, Uncharacterized family of heme peroxidases, mostly bacterial. Animal heme peroxidases are diverse family of enzymes which are not restricted to animals. Members are also found in metazoans, fungi, and plants, and also in bacteria - like most members of this family of uncharacterized proteins
DRPSPREISNAVADQTESIPNSRGLSDWFWVWGQFLDHDIDLTPDNPREQINAITAYIDGSNVYGSDEER
ADALRSFGGGKLKTSVANAGDLLPFNEAGLPNDNGGVPADDLFLAGDVRANENPGLTALHTLFVREHNRL
ADELARRNPSLSDEEIYQAARAIVIAEIQAITYNEFLPALLGENALPAYSGYDETVNPGISNEFSTAAYR
FGHSMLSSELLRGDEDGTEATSLALRDAFFNPDELEENGIDPLLRGLASQVAQEIDTFIVDDVRNFLFGP
PGAGGFDLAALNIQRGRDHGLPSYNQLREALGLPAVTSFSDITSDPDLAARLASVYGDVDQIDLWVGGLA
EDHVNGGLVGETFSTIIADQFTRLRDGDRFFYENDDLLLDEIADIENTTLADVIRRNTDVDDIQDNVFLV
>gnl|CDD|188655 cd09823, peroxinectin_like, peroxinectin_like animal heme peroxidases. Peroxinectin is an arthropod protein that plays a role in invertebrate immunity mechanisms. Specifically, peroxinectins are secreted as cell-adhesive and opsonic peroxidases. The immunity mechanism appears to involve an interaction between peroxinectin and a transmembrane receptor of the integrin family. Human myeloperoxidase, which is included in this wider family, has also been reported to interact with integrins
REQLNQVTSFLDGSQVYGSSEEEARKLRTFKGGLLKTQRRNGRELLPFSNNPTDDCSLSSAGKPCFLAGD
GRVNEQPGLTSMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELME
KFGLYLLTSGYFNGYDPNVDPSILNEFAAAAFRFGHSLVPGTFERLDENYRPQGSVNLHDLFFNPDRLYE
EGGLDPLLRGLATQPAQKVDRFFTDELTTHFFFRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPR
ATTFDDLLGIMSPETIQKLRRLYKSVDDIDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYE
NGGQPSSFTPAQLNEIRKVSLARIICDN
>gnl|CDD|188656 cd09824, myeloperoxidase_like, Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases. This well conserved family of animal heme peroxidases contains members with somewhat diverse functions. Myeloperoxidases are lysosomal proteins found in azurophilic granules of neutrophils and the lysosomes of monocytes. They are involved in the formation of microbicidal agents upon activation of activated neutrophils (neutrophils undergoing respiratory bursts as a result of phagocytosis), by catalyzing the conversion of hydrogen peroxide to hypochlorous acid. As a heme protein, myeloperoxidase is responsible for the greenish tint of pus, which is rich in neutrophils. Eosinophil peroxidases are haloperoxidases as well, preferring bromide over chloride. Expressed by eosinophil granulocytes, they are involved in attacking multicellular parasites and play roles in various inflammatory diseases such as asthma. The haloperoxidase lactoperoxidase is secreted from mucosal glands and provides antibacterial activity by oxidizing a variety of substrates such as bromide or chloride in the presence of hydrogen peroxide
SCGACTSKRNVREQINALTSFVDASMVYGSEPSLAKXLRNLTNQLGLLAVNQRFTDNGLALLPFENLHND
PCALRNTSANIPCFLAGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQ
IITYRDYLPLILGEDAAARLPPYRGYNESVDPRIANVFTTAFRRGHTTVQPFVFRLDENYQPHPPNPQVP
LHKAFFASWRIIREGGIDPILRGLMATPAKLNNQNQMLVDELRERLFQQTKRMGLDLAALNLQRGRDHGL
PGYNAWRRFCGLSQPQNLAELAAVLNNTVLARKLLDLYGTPDNIDIWIGGVAEPLVPGGRVGPLLACLIS
RQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICDNTGITKVPRDPFQPNSYPRDFV
>gnl|CDD|188657 cd09825, thyroid_peroxidase, Thyroid peroxidase (TPO). TPO is a member of the animal heme peroxidase family, which is expressed in the thyroid and involved in the processing of iodine and iodine compounds. Specifically, TPO oxidizes iodide via hydrogen peroxide to form active iodine, which is then, for example, incorporated into the tyrosine residues of thyroglobulin to yield mono- and di-iodotyrosines
GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQY
IDHDIDFTPQSVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTLFG
NLSLANPREQINGLTSFIDASTVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQPEEVSSCNP
DPNGGERVPCFLAGDGRASEVLTLTASHTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIIT
FRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNVFSTAAFRFGHATIHPTVRRLDENFQEHPVLPNLAL
HDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEELTEKLFVLSNSSTLDLASLNLQRGRDHGLP
GYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPGARTGPLFACLIGK
QMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPGINL
EAWRE
>gnl|CDD|188658 cd09826, peroxidasin_like, Animal heme peroxidase domain of peroxidasin and related proteins. Peroxidasin is a secreted heme peroxidase which is involved in hydrogen peroxide metabolism and peroxidative reactions in the cardiovascular system. The domain co-occurs with extracellular matrix domains and may play a role in the formation of the extracellular matrix
PPDDPRRRGHRCIEFVRSSAVCGSGSTSLLFNSVTPREQINQLTSYIDASNVYGSSDEEALELRDLASDR
GLLRVGIVSEAGKPLLPFERDSPMDCRRDPNESPIPCFLAGDHRANEQLGLTSMHTLWLREHNRIASELL
ELNPHWDGETIYHETRKIVGAQMQHITYSHWLPKILGPVGMEMLGEYRGYNPNVNPSIANEFATAAFRFG
HTLINPILFRLDEDFQPIPEGHLPLHKAFFAPYRLVNEGGIDPLLRGLFATAAKDRVPDQLLNTELTEKL
FEMAHEVALDLAALNIQRGRDHGLPGYNDYRKFCNLSVAETFEDLKNEIKNDDVREKLKRLYGHPGNIDL
FVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWYENPGVFSPAQLTQIKKTSLARVLCDNGDNITR
VQEDVFLVPGNPHGYVSCES
>gnl|CDD|193602 cd09827, PET_Prickle, The PET domain of Prickle. The PET domain of Prickle: Prickle contains an N-terminal PET domain and three C-terminal LIM domains. Prickle has been implicated in regulation of cell movement in the planar cell polarity (PCP) pathway which requires the conserved Frizzled/Dishevelled (Dsh); Prickle interacts with Dishevelled, thereby modulating the activity of Frizzled/Dishevelled and the PCP signaling. Two forms of Prickle have been identified, namely Prickle 1 and Prickle 2. These are differentially expressed; Prickle 1 is found in fetal heart and hematological malignancies, while Prickle 2 is expressed in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. The PET domain is a protein-protein interaction domain, usually found in conjunction with the LIM domain, which is also involved in protein-protein interactions. The PET containing proteins serve as adaptors or scaffolds to support the assembly of multimeric protein complexes
SDDDSGCALEEYAWVPPGLKPEQVHAYFSCLPEDKVPYVNSPGEKYRIKQLLHQLPPHDNEVRYCNSLSE
EEKRELRLFSAQRKREALGRGIVRPLP
>gnl|CDD|193603 cd09828, PET_OEBT, The PET domain of overexpressed breast tumor protein (OEBT). The PET domain of overexpressed breast tumor protein (OEBT): OEBT contains an N-terminal PET domain and two C-terminal LIM domains, and is predicted to be localized in the nucleus. The expression pattern of OEBT in malignant tissues indicates a possible role of OEBT in cancer differentiation. The PET domain is a protein-protein interaction domain and is usually found in conjunction with LIM domain, which is also involved in protein-protein interactions. PET containing proteins serve as adaptors or scaffolds to support the assembly of multimeric protein complexes
MSVQNSGWPHQEDSPCGRTPGPPANSDSDSGHLPGEEYEDPSAQAAPPISLGPCCLDRNQAPNWPGLRTL
LQQLPPQDSDERYCLALAEEERAQLRLFCARRKQEALGQGVARPVP
>gnl|CDD|193604 cd09829, PET_testin, The PET domain of Testin. The PET domain of Testin: Testin contains a PET domain at the N-terminus and three C-terminal LIM domains. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and is involved in cell motility and adhesion events. Knockout mice experiments reveal a tumor repressor function of Testin. The PET domain is a protein-protein interaction domain and is usually found in conjunction with LIM domain, which is also involved in protein-protein interactions. The PET containing proteins serve as adaptors or scaffolds to support the assembly of multimeric protein complexes
VTYEWAPPGVTQELARYYMELLPKEKQPIAGSEGAQYRKKQLQKQLPLHDQDPSLCHELSENEVKQMEQF
VKKYKEEALGVGKVIEPG
>gnl|CDD|193605 cd09830, PET_LIMPETin_LIM-9, The PET domain of protein LIMPETin and LIM-9. The PET domain of protein LIMPETin and LIM-9: Members of this family contain an N-terminal PETdomain and five to six LIM domains at the C-terminus. Four of the six LIM domains are highly homologous to the four-and-half LIM (FHL) domain family while the other two show sequence similarity to LIM domains of the Testin family. Thus, proteins of this family may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Thus, proteins of this family may be the recombinant product of genes coding Testin and FHL proteins. SmLIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult males. Its differential expression indicates that it is a transcription regulator. In C. elegans, LIM-9 binds to UNC-97 and UNC-96, components of sarcomeric muscle M-lines. LIM-9 also forms a complex with SCPL-1 and UNC-89, whose function is to organize sarcomeric A-bands, especially the M-line of muscle. Thus, it might play a role in regulating the assembly and maintenance of muscle A-band. The PET domain is a protein-protein interaction domain and is usually found in conjunction with LIM domain, which is also involved in protein-protein interactions. The PET containing proteins serve as adaptors or scaffolds to support the assembly of multimeric protein complexes
LGYTWVPPGLSSTKIDDYMSSLPNEKVPKLGSPGERYREKQLILQLPKQDLSLAYCKHLEEDEKRSFEDF
VNARNEIALGIGY
>gnl|CDD|341402 cd09831, CBS_pair_ABC_Gly_Pro_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the glycine betaine/L-proline ABC transporter. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
DIARKTQVTVIEKTGDGPRAALQLLREHDREYGYVVDKKRRFLGVVSVDSLRAALKENAQSLEDAFLTDV
ETVPADTSLSDILGLVASAPCPLPVVDEDGRYLGVISKASLLETLD
>gnl|CDD|341403 cd09833, CBS_pair_GGDEF_PAS_repeat1, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 1. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
RIVSTSLLTCSPDTPLADAAARMAERRCSSILIVENGEIVGIWTERDALKLDFSDPDAFRRPISEVMSSP
VLTIPQDTTLGEAAVRFRQEGVRHLLVVDDDGRPVGIVSQTDVVLN
>gnl|CDD|341404 cd09834, CBS_pair_bac, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
KSEVAYLYDDSTLRQALEKMEYHRYTAIPILNRDGKYVGTITEGDLLWYIKNKPNLDLKDAEKISIKDIP
RRRDNKPVNINANMEDLLDLAMNQNFVPVVDDRGVFIGIVTRKDIIKY
>gnl|CDD|341405 cd09836, CBS_pair_arch, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGIDLDTPVEEIMTKNLV
TVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLARELS
>gnl|CDD|341406 cd09837, CBS_pair_chlorobiales, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in chlorobiales. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
DTTYPFFTDDAPAAEVLAFMQAKELSCAPVLHDGRYVAMVTLADLLPARQGTPTAGLKLGELSLEEVGSI
GPHEHLFDLFSRLALFPCSIIPVSDEDGRYIGVVSKKRVLE
>gnl|CDD|341074 cd09839, M1_like_TAF2, TATA binding protein (TBP) associated factor 2. This family includes TATA binding protein (TBP) associated factor 2 (TAF2, TBP-associated factor TAFII150, transcription initiation factor TFIID subunit 2, RNA polymerase II TBP-associated factor subunit B), and has homology to the M1 gluzincin family. TAF2 is part of the TFIID multidomain subunit complex essential for transcription of most protein-encoded genes by RNA polymerase II. TAF2 is known to interact with the initiator element (Inr) found at the transcription start site of many genes, thus possibly playing a key role in promoter binding as well as start-site selection. Image analysis has shown TAF2 to form a complex with TAF1 and TBP, inferring its role in promoter recognition. Peptidases in the M1 family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. TAF2, however, lacks these active site residues
VAHQKVELDVDFANRSIIGYTEITIVPTSPDLRTIRLNCRQCKIKSVTVNGVEAEFTYNDPLQNLDLSDN
TDVNAHHELKRKLAAALAEPDEGNEELVISLPPSVKIELQDPNSASTQATTSSPDTSEDEFTPLTIRIEY
SLKNPRDGLHFVGPDEGGDKRYPHVYTTNSPLPGSARCWFPCVDSLWERCTWELEITVPRTLGDAGRPPL
AGSKEDEDDDDLTEEDKELEMVVVCSGDLVEQVVHPEDPSKKTFSFSLSNPTSAQHIGFAVGPFEIVPLP
EFRESEEDDKLGSSAVEVTGFCLPGRLEELRNTCSFLHKAMDFFEEEYGSYPFSSYKQVFVDDLPEDVSS
FASLSICSSRLLYPPDIIDQAYETRRKLAHALASQWFGINIIPKTWSDTWLVIGIAGYMTGLFLKKLFGN
NEYRFRIKKDADRVCELDIGRPPLAQPGFILPLDPSELEFMALKAPLVLFILDRRLTKTGGSFGLSRVLP
KIFLQAMSGDLSNNALSTSHFLRTCEKVSGNKLESFFDQWV
>gnl|CDD|188871 cd09840, LIM2_CRP2, The second LIM domain of Cysteine Rich Protein 2 (CRP2). The second LIM domain of Cysteine Rich Protein 2 (CRP2): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP and TLPCRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network.CRP3 also called Muscle LIM Protein (MLP), which is a striated muscle-specific factor that enhances myogenic differentiation. The second LIM domain of CRP3/MLP interacts with cytoskeletal protein beta-spectrin. CRP3/MLP also interacts with the basic helix-loop-helix myogenic transcription factors MyoD, myogenin, and MRF4 thereby increasing their affinity for specific DNA regulatory elements. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CSRCGDSVYAAEKIMGAGKPWHKNCFRCAKCGKSLESTTLTEKEGEIYCKGCYA
>gnl|CDD|188872 cd09841, LIM1_Prickle_3, The first LIM domain of Prickle 3. The first LIM domain of Prickle 3/LIM domain only 6 (LM06): Prickle contains three C-terminal LIM domains and a N-terminal PET domain. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). PCP establishment requires the conserved Frizzled/Dishevelled PCP pathway. Prickle interacts with Dishevelled, thereby modulating Frizzled/Dishevelled activity and PCP signaling. Four forms of prickles have been identified: prickle 1-4. The best characterized is prickle 1 and prickle 2 which are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. Mutations in prickle 1 have been linked to progressive myoclonus epilepsy. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes
CQQCGRQICGGDIAVFASRAGLGACWHPQCFQCASCQELLVDLIYFYQDGKIYCGRHHA
>gnl|CDD|197300 cd09842, PLDc_vPLD1_1, Catalytic domain, repeat 1, of vertebrate phospholipase D1. Catalytic domain, repeat 1, of vertebrate phospholipase D1 (PLD1). PLDs play a pivotal role in transmembrane signaling and cellular regulation. They hydrolyze the terminal phosphodiester bond of phospholipids resulting in the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Vertebrate PLD1 is a membrane associated phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent enzyme that selectively hydrolyzes phosphatidylcholine (PC). Protein cofactors and calcium might be required for its activation. Most vertebrate PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at their N-terminus, which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. Like other members of the PLD superfamily, the monomer of vertebrate PLDs consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. These PLDs utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
SKWYVNAKCYFEDVANAMEEAKEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFVMLYK
EVELALGINSEYSKRTLMRLHPNIKVMRHPDHVSSSVYLWAHHEKIVVIDQSVAFVGGIDLAYGRWDDDE
HRLTDVGSVKR
>gnl|CDD|197301 cd09843, PLDc_vPLD2_1, Catalytic domain, repeat 1, of vertebrate phospholipase D2. Catalytic domain, repeat 1, of vertebrate phospholipase D2 (PLD2). PLDs play a pivotal role in transmembrane signaling and cellular regulation. They hydrolyze the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. They also catalyze a transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Vertebrate PLD2 is a membrane associated phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent enzyme that selectively hydrolyzes phosphatidylcholine (PC). Protein cofactors and calcium might be required for its activation. Most vertebrate PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at their N-terminus, which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. Like other members of the PLD superfamily, the monomer of vertebrate PLDs consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. These PLDs utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
TKWFVNGHGYFAAVADALEQAQEEIFITDWWLSPEVFLKRPAHGDDWRLDIILKRKAEQGVRVCVLLFKE
VELALGINSGYSKRKLMLLHPNIKVMRHPDHVASVVVLWAHHEKMVAIDQSVAFLGGLDLAYGRWDDSDY
RLTDL
>gnl|CDD|197302 cd09844, PLDc_vPLD1_2, Catalytic domain, repeat 2, of vertebrate phospholipase D1. Catalytic domain, repeat 2, of vertebrate phospholipase D1 (PLD1). PLDs play a pivotal role in transmembrane signaling and cellular regulation. They hydrolyze the terminal phosphodiester bond of phospholipids resulting in the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Vertebrate PLD1 is a membrane associated phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent enzyme that selectively hydrolyzes phosphatidylcholine (PC). Protein cofactors and calcium might be required for its activation. Most vertebrate PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at their N-terminus, which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. Like other members of the PLD superfamily, the monomer of vertebrate PLDs consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. These PLDs utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
GIKYHEESIHAAYVSVIENSKHYIYIENQFFISCADDKVVFNKIGDAIAQRILKAHRENKRYRVYVVIPL
LPGFEGDISTGGGNALQAIMHFNYRTMCRGEHSIIGQLKAEMGDQWINYISFCGLRTHAELEGNLVTELI
YVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVVVQDTE
>gnl|CDD|197303 cd09845, PLDc_vPLD2_2, Catalytic domain, repeat 2, of vertebrate phospholipase D2. Catalytic domain, repeat 2, of vertebrate phospholipase D2 (PLD2). PLDs play a pivotal role in transmembrane signaling and cellular regulation. They hydrolyze the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. They also catalyze a transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Vertebrate PLD2 is a membrane associated phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent enzyme that selectively hydrolyzes phosphatidylcholine (PC). Protein cofactors and calcium might be required for its activation. Most vertebrate PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at their N-terminus, which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. Like other members of the PLD superfamily, the monomer of vertebrate PLDs consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. These PLDs utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group
SAGTLENSILNAYLHTIENSQHYLYLENQFFISCADGRTVLNKIGDAIVKRILKAHSQGWCFRVFVVIPL
LPGFEGDISTGGGNSIQAILHFTYRTICRGEYSILSRLKEAMGTAWTDYISICGLRTHGELGGSPVTELI
YIHSKVLIADDRTVIIGSANINDRSMLGKRDSELAVLVEDTE
>gnl|CDD|197363 cd09846, DUF1312, N-Utilization Substance G (NusG) N terminal (NGN) insert and Lin0431 are part of DUF1312. Domains of Unknown Function 1312 (DUF1312) are represented in at least 71 bacterial species with no functional annotation. Included in this family are N-Utilization Substance G (NusG) N terminal (NGN) insert and Lin0431, having similar structure and surface features that appear to be conserved across these domain families, suggesting similar function. NusG contains NGN at the N-terminus and Kyrpides Ouzounis and Woese (KOW) repeats at the C-terminus in bacteria and archaea, and this insert (often known as Domain II) is found in several bacteria. Lin0431 is similar to NGN-insert but does ot contain the disulphite bridge
VAVIEVDGKVVRRIDLDGVGKPYTFSIEGEGYTNIIEVEDGRVRVKESDCPDKICVKTGWISKPGQTIVC
LPNRVIIKIEG
>gnl|CDD|349946 cd09848, M28_TfR, M28 Zn-peptidase Transferrin Receptor family. Peptidase M28 family; Transferrin Receptor (TfR) subfamily. TfRs are homodimeric type II transmembrane proteins containing three distinct domains: protease-like, apical or protease-associated (PA), and helical domains. The protease-like domain is a large extracellular portion (ectodomain). In TfR, it contains a binding site for the transferrin molecule and has 28% identity to membrane glutamate carboxypeptidase II (mGCP-II or PSMA). The PA domain is inserted between the first and second strands of the central beta sheet in the protease-like domain. TfR1 is widely expressed, and is a key player in the uptake of iron-loaded transferrin (Tf) into cells. The TfR1 homodimer binds two molecules of Tf and the complex is then internalized. TfR1 may also participate in cell growth and proliferation. TfR2 binds Tf but with a significantly lower affinity than TfR1. It is expressed chiefly in hepatocytes, hematopoietic cells, and duodenal crypt cells; its expression overlaps with that of hereditary hemochromatosis protein (HFE). TfR2 is involved in iron homeostasis; in humans, mutations in TfR2 are associated with a form of hemochromatosis (HFE3). While related in sequence to peptidase M28 glutamate carboxypeptidase II (also called prostate-specific membrane antigen or PSMA), TfR lacks the metal ion coordination centers and protease activity of that group
LKKKLSEKDFEQTLRDLSSISHEAGSSGDENLANYIMNEFKNLKLMKVWTDEHYKIHNIFGVIKGFVEPD
RYVVIGAQRDAWGPGAAKSGVGTALLLELARTFSDMVKNDGFKPRRSIVFASWSAGDFGSVGATEWLEGY
LSSLHLKAFTYISLDGAVLGDDSFKASASPLLYTLIESTMKQVKSPVHSGQSYYETRSSWWASIVEPLGL
DSAAYPFLAFSGIPSVSFHFTEDDEDYPFLGTKEDTKENLDKFTNGELWEVAAAAAEVAGQMALRLVHDH
LLPLD
>gnl|CDD|349947 cd09849, M20_Acy1L2-like, M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family. Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine)
DENKEKIIAIGQTIYDNPELGYKEFKTTETVADFFKNLLNLDVEKNIASTGCRATLNGDKKGPNIAVLGE
LDAISCPEHPDANEATGAAHACGHNIQIAGMLGAAVALFKSGVYEELDGKLTFIATPAEEFIELAYRDQL
KKSGKISYFGGKQELIKRGVFDDIDISLMFHALDLGEDKALINPESNGFIGKKVKFTGKESHAGSAPFSG
INALNAATLAINNVNAQRETFKESDKVRFHPIITKGGDIVNVVPADVRVESYVRARSIDYMKEANSKVNR
ALRASAMAVGAEVEIKELPGYLPILQDRDLDNFLKENLQDLGLIERIIDGGDFTGSFDFGDLSHLMPTLH
PMFGGVEGALHTRDFKIVDPEFAYILPAKALALTVVDLL
>gnl|CDD|197367 cd09850, Ebola-like_HR1-HR2, heptad repeat 1-heptad repeat 2 region of the transmembrane subunit of Filoviridae viruses, Ebola virus and Marburg virus, and related domains. This domain subfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including Ebola virus gp2, Marburg virus gp, and the envelope proteins of various ERVs, including human HERV-R_c7q21.2 (ERV-3). This domain includes an N-terminal heptad repeat, a CKS17-like immunosuppressive region, a CX6C motif that forms an intrasubunit disulfide bond, and a C-terminal heptad repeat. N-terminal to HR1-HR2 region is a fusion peptide (FP), and C-terminal, is a membrane-spanning region (MSR). Viral infection involves the formation of a trimer-of-hairpins structure (three HR1s helices, buttressed by three HR2 helices lying in antiparallel orientation). In this structure, the FP (inserted in the host cell membrane) and MSR (inserted in the viral membrane) are in close proximity. ERVs are likely to originate from ancient germ-line infections by active retroviruses. Some ERVs play specific roles in the host. However, it is unclear whether ERV-3 has a critical biological role: it is expressed in the placenta, but is not fusogenic, has an immunosuppressive domain, but lacks a fusion peptide. Filoviridae, the family of viruses including Ebola and Marburg, may have acquired this domain via horizontal transfer from retroviruses
VLEILANETAQALELLLRQTTEMRTFSYQNRLALDYLLAREGGVCGKFNPDNCCIEIDDWGEVIKNITDK
IDQIAHD
>gnl|CDD|197368 cd09851, HTLV-1-like_HR1-HR2, heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of human T-cell leukemia virus type 1 (HTLV-1), and related domains. This domain subfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane(TM) subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including HTLV-1, HTLV -2, primate Mason-Pfizer monkey virus, Moloney murine leukemia virus, simian T-cell lymphotropic virus, feline leukemia virus (FeLV), bovine leukemia virus, and various human endogenous retroviruses (HERVs), including, HERV-H1_c2q24.3, HERV-H2_3q26, HERV-F(c)1_cXq21.33, HERV-T_19q13.11, Syncytin-1 (HERV-W_c7q21.2/ ERVWE1), Syncytin-2 (HERV-FRD_6p24.1), and related domains. This domain includes an N-terminal heptad repeat, a CKS17-like immunosuppressive region, a CX6C motif that forms an intrasubunit disulfide bond, and a C-terminal heptad repeat. N-terminal to HR1-HR2 region is a fusion peptide (FP), and C-terminal, is a membrane-spanning region (MSR). Viral infection involves the formation of a trimer-of-hairpins structure (three HR1s helices, buttressed by three HR2 helices lying in antiparallel orientation). In this structure, the FP (inserted in the host cell membrane) and MSR (inserted in the viral membrane) are in close proximity. ERVs are likely to originate from ancient germ-line infections by active retroviruses. Some modern ERVs, those that integrated into the host genome post-speciation, have a currently active exogenous counterpart, such as FeLV. Some ERVs play specific roles in the host, including placental development, protection of the host from infection by related pathogenic and exogenous retroviruses, and genome plasticity. Syncytin-1 and Syncytin-2 are expressed in the placenta, and are fusogenic, although they have a different cell specificity for fusion. Syncytin-2, but not Syncytin-1, is immunosuppressive; its immunosuppressive domain may protect the fetus from the mother's immune system. Syncytin-1 may participate in the formation of the placental trophoblast; it is also implicated in cell fusions between cancer and host cells and between cancer cell, and in human osteclast fusion. This subfamily also contains a mouse envelope protein encoded by the Fv-4 env gene, that blocks infection by exogenous MuLV
QSYKSLSHALDADIQRLAQSISKLQKQLTSLAEVVLQNRRGLDLLTLEQGGLCAALQEECCFYANQSGLV
RDSIAKLR
>gnl|CDD|350203 cd09852, PIN_SF, PIN (PilT N terminus) domain: Superfamily. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily, and were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. The PIN domain superfamily includes: the FEN-like PIN domain family such as the PIN domains of Flap endonuclease-1 (FEN1), exonuclease-1 (EXO1), Mkt1, Gap Endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease, 5'-3' exonucleases of DNA polymerase I and bacteriophage T4- and T5-5' nucleases; the VapC-like PIN domain family which includes toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1; the LabA-like PIN domain family which includes the PIN domains of Synechococcus elongatus LabA (low-amplitude and bright); the PRORP-Zc3h12a-like PIN domain family which includes the PIN domains of RNase P (PRORP), ribonuclease Zc3h12a; and Bacillus subtilis YacP/Rae1-like PIN domains. It also includes the Mut7-C PIN domain family, which is not represented here as it is a shortened version of the PIN fold and lacks a core strand and helix (H3 and S3). The Mut7-C PIN domain family includes the C-terminus of Caenorhabditis elegans exonuclease Mut-7
LVDGSNMIYTCREAVRTYRLNFDMAQRQYVAKEGVSPIVVFDASPVQLKVKVTKNDRKQLQFHGVGFAVX
LTPPISDADVGIAALAIAIDRVALATGDGDFLAIVENKGVTVYR
>gnl|CDD|350204 cd09853, PIN_FEN-like, FEN-like PIN domains of structure-specific 5' nucleases (or Flap endonuclease-1-like) involved in DNA replication, repair, and recombination. Structure-specific 5' nucleases are capable of both 5'-3' exonucleolytic activity and cleaving bifurcated or branched DNA, in an endonucleolytic, structure-specific manner. The family includes the PIN (PilT N terminus) domains of Flap endonuclease-1 (FEN1), exonuclease-1 (EXO1), Mkt1, Gap Endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease. Also included are the PIN domains of the 5'-3' exonucleases of DNA polymerase I and single domain protein homologs, as well as, the bacteriophage T4- and T5-5' nucleases, and other homologs. Canonical members of this FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
VIDGMNIAFNFAHPVRNLKEEEGSDFQGYFSAVDDLVKKLKPGIKPILLFDGGKPKAKKGNRDKRRERRA
REEDRKKGQLKEHKEFDKRLIELGPEYLIRLFELLKHFMGIPVMDAPGEAEDEIAYLVKKHKHLGTVHLI
ISTDGDFLLLGTDHPYIPRNLLTVKEETFQEFHL
>gnl|CDD|350205 cd09854, PIN_VapC-like, VapC-like PIN domains of VapC and Smg6 ribonucleases, ribosome assembly factor NOB1, rRNA-processing protein Fcf1, Archaeoglobus fulgidus AF0591 protein, and homologs. PIN (PilT N terminus) domains of such ribonucleases as the toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1, are included in VapC-like this family. Also included are the PIN domains of the Pyrobaculum aerophilum Pea0151 and Archaeoglobus fulgidus AF0591 proteins and other similar archaeal homologs. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
VLDTNVLIALLSSEPESEAAKELLALLLGDSELVIPPLVLAELLRLLARERGARRALEILELLRALEVVE
EEPALAEIALEVLALGLERGLDFGDALILALAKELGGAVLVTNDRDFRRLAKLGLKVIV
>gnl|CDD|350206 cd09856, PIN_FEN1-like, FEN-like PIN domains of Flap endonuclease-1 (FEN1)-like, structure-specific, divalent-metal-ion dependent, 5' nucleases. PIN (PilT N terminus) domain of Flap endonuclease-1 (FEN1)-like nucleases: FEN1, Gap endonuclease 1 (GEN1) and Xeroderma pigmentosum complementation group G (XPG) nuclease. Nucleases in this subfamily are members of the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
GFWKIIGPSKRRISLESLRGKRVAIDASIWIYQFLTAVRGQGGNGVSNSHIRGLFYRIIRLLENGIKPVF
VFDGEPPKLKKRTRRKRKERRQGAEESAKSAVEDELFEEQSKDKKRSGTVTKVMTAECKHLLSLFGIPYV
DAPGEAEAQCAYLEQQGIVDAVLTEDVDTFLFGSPVVYRNLTSEGKKTHVELYDASSILEGLFLPWSTPD
LEGLRKFTREEFDWPFEKLIKVLAP
>gnl|CDD|350207 cd09857, PIN_EXO1, FEN-like PIN domains of Exonuclease-1, a structure-specific, divalent-metal-ion dependent, 5' nuclease and homologs. exonuclease-1 (EXO1) is involved in multiple, eukaryotic DNA metabolic pathways, including DNA replication processes (5' flap DNA endonuclease activity and double stranded DNA 5'-exonuclease activity), DNA repair processes (DNA mismatch repair (MMR) and post-replication repair (PRR)), recombination, and telomere integrity. EXO1 functions in the MMS2 error-free branch of the PRR pathway in the maintenance and repair of stalled replication forks. Studies also suggest that EXO1 plays both structural and catalytic roles during MMR-mediated mutation avoidance. These nucleases are members of the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. EXO1 nucleases also have C-terminal Mlh1- and Msh2-binding domains which allow interaction with MMR and PRR proteins, respectively
MGIQGLLPFLKPIQRPVHISEYAGKTVAVDAYCWLHRGAYSCAEELALGKPTDKYIDYCMKRVNMLLHHG
ITPILVFDGAPLPSKAGTEEERRERREEALEKALELLREGKKSEARECFQRAVDITPEMAHELIKALRKE
NVEYIVAPYEADAQLAYLAKTGYVDAVITEDSDLLAFGCPKVLFKLDKDGNGQEIDRDDLGK
>gnl|CDD|350208 cd09858, PIN_MKT1, FEN-like PIN domains of Mkt1, a global regulator of mRNAs encoding mitochondrial proteins and eukaryotic homologs. The Mkt1 gene product interacts with the Poly(A)-binding protein associated factor, Pbp1, and is present at the 3' end of RNA transcripts during translation. The Mkt1-Pbp1 complex is involved in the post-transcriptional regulation of HO endonuclease expression. Mkt1 and eukaryotic homologs are atypical members of the structure-specific, 5' nuclease family (FEN-like). Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. Although Mkt1 appears to possess both a PIN and H3TH domain, the Mkt1 PIN domain lacks several of the active site residues necessary to bind essential divalent metal ion cofactors (Mg2+/Mn2+) required for nuclease activity in this family. Also, Mkt1 lacks the glycine-rich loop in the H3TH domain which is proposed to facilitate duplex DNA binding
IRSLDSYLTERKLVTTSPLSALKGARLGIDASYYLRKLLDNKPTREPLAALGGLPLALKAHIESDLEQLK
KLNITPVFVFNGLSLKGQDEPSSQSEQAAQKREEAWDLYEKGQADQAVKAFGESGSYRLEDLYRLLQRIL
KERGVEFLVAPYSAWAQLAYLEKHGKQYIDAIYGSTELLLFGVDKVITSIDFEKGTFTWVDKKRLL
>gnl|CDD|350209 cd09859, PIN_53EXO, FEN-like PIN domains of PIN domain of the 5'-3' exonuclease of Thermus aquaticus DNA polymerase I (Taq) and homologs. The 5'-3' exonuclease (53EXO) PIN (PilT N terminus) domain of multi-domain DNA polymerase I and single domain protein homologs are included in this family. Taq contains a polymerase domain for synthesizing a new DNA strand and a 53EXO PIN domain for cleaving RNA primers or damaged DNA strands. Taq's 53EXO PIN domain recognizes and endonucleolytically cleaves a structure-specific DNA substrate that has a bifurcated downstream duplex and an upstream template-primer duplex that overlaps the downstream duplex by 1 bp. The 53EXO PIN domain cleaves the unpaired 5'-arm of the overlap flap DNA substrate. 5'-3' exonucleases are members of the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LIDGSSLLYRAYYALPPLTTSDGEPTNAVYGFTNMLLKLLKEEKPDYIAVAFDAKGPTFRHELYPEYKAN
RPPMPEELIPQIPLIKELLEALGIPVLEVEGYEADDIIGTLAKKAEKEGLEVVIVTGDKDLLQLVDDNVK
VLDPKKGSKTEIYDEEEVKE
>gnl|CDD|350210 cd09860, PIN_T4-like, FEN-like PIN domains of bacteriophage T3, T4 RNase H, T5-5'nuclease, and homologs. PIN (PilT N terminus) domain of bacteriophage T5-5'nuclease (5'-3' exonuclease or T5FEN), bacteriophage T4 RNase H (T4FEN), bacteriophage T3 (T3 phage exodeoxyribonuclease) and other similar 5' nucleases are included in this family. T5-5'nuclease is a 5'-3'exodeoxyribonuclease that also exhibits endonucleolytic activity on flap structures (branched duplex DNA containing a free single-stranded 5'end). T4 RNase H, which removes the RNA primers that initiate lagging strand fragments, has 5'- 3'exonuclease activity on DNA/DNA and RNA/DNA duplexes and has endonuclease activity on flap or forked DNA structures. Bacteriophage T3 is believed to function in the removal of DNA-linked RNA primers and is essential for phage DNA replication and also necessary for host DNA degradation and phage genetic recombination. These nucleases are members of the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. In the T5-5'nuclease, structure-specific endonuclease activity requires binding of a single metal ion in the high-affinity, metal binding site 1, whereas exonuclease activity requires both, the high-affinity, metal binding site 1 and the low-affinity, metal binding site 2 to be occupied by a divalent cofactor. The T5-5'nuclease is reported to be able to bind several metal ions including, Mg2+, Mn2+, Zn2+ and Co2+, as co-factors
LLLIDGNSIGFAAQHSAKLTAGGMEVQARFGFLRSIRSYLKRYKYAKPIVLWDGRASWRKDLFPEYKANR
KKTREEKKAWREAFEAQRPFIEEALEYLGVPQIRAPGAEADDLAGVLVKRLAAFGDKVLLVSGDKDWLQL
VYENVSWFSPITDKEVTL
>gnl|CDD|350211 cd09862, PIN_Rrp44-like, VapC-like PIN domain of yeast exosome subunit Rrp44 endoribonuclease and other eukaryotic homologs. PIN (PilT N terminus) domain of the Saccharomyces cerevisiae exosome subunit Rrp44 (Ribosomal RNA-processing protein 44 or Protein Dis3 homolog) and other similar eukaryotic homologs are included in this family. The eukaryotic exosome is a conserved macromolecular complex responsible for many RNA-processing and RNA-degradation reactions. It is composed of nine core subunits that directly binds Rrp44. The Rrp44 nuclease is the catalytic subunit of the exosome and has endonuclease activity in the PIN domain and an exoribonuclease activity in its RNase II-like region. Rrp44 binding to the exosome is mediated mainly by the PIN domain and by subunits Rrp41-Rrp45, and binding predictions indicate that the PIN domain active site is positioned on the outer surface of the exosome. This subgroup belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. PIN domains within this subgroup contain four of these residues which cluster at the C-terminal end of the beta-sheet and form a negatively charged pocket near the center of the molecule. Recombinant Rrp44 was shown to possess manganese-dependent endonuclease activity in vitro that was abolished by point mutations in these putative metal binding residues of its PIN domain. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
KKTRRGKVVKVVREHYLRDDIPCGSELCPLCPQTNPKLLLLSLLSDAKHYLIPDTNVVLHQIDLLEDPEI
TNVIILQTVLEEVRHRSLPLYNRLRALLKDPRKRFYVFSNEFHRETYVEREPGESPNDRNDRAIRKAAKW
YQNHLAKLGIPVVLLTDDADNREKAEEEGILALTVREY
>gnl|CDD|350212 cd09864, PIN_Fcf1-like, VapC-like PIN domain of rRNA-processing protein, Fcf1 (Utp24, YDR339C), and other eukaryotic homologs. Fcf1/Utp24 (FAF1-copurifying factor 1/U three-associated protein 24) is an essential protein involved in pre-rRNA processing and 40S ribosomal subunit assembly. Component of the small subunit (SSU) processome, Fcf1 is an essential nucleolar protein that is required for processing of the 18S pre-rRNA at sites A0-A2. The Fcf1 protein was reported to interact with Pmc1p (vacuolar Ca2+ ATPase) and Cor1p (core subunit of the ubiquinol-cytochrome c reductase complex). The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. Most members of the Fcf1 PIN domain subfamily have four of these conserved residues and the Fcf1-Utp23 homolog PIN domain subfamily has three. Point mutation studies of the conserved acidic residues in the putative active site of Saccharomyces cerevisiae Fcf1 determined they were essential for pre-rRNA processing at sites A1 and A2, whereas the presence of the Fcf1 protein itself is also required for cleavage at site A0
FKYNTALGPPYHVLLDTNFINFSIQNKLDIVKGMMDCLYAKCIPCITDCVMAELEKLGRKYRVALRIAKD
PRFERLKCDHKGTYADDCIVNRVTQHRCYIVATCDRDLKRRIRKIPGVPIMYIKGHKYSIE
>gnl|CDD|350213 cd09865, PIN_ScUtp23p-like, VapC-like PIN domain of rRNA-processing protein, Utp23 (YOR004W), and other fungal homologs. Saccharomyces cerevisiae Utp23 (U three-associated protein 23), component of the small subunit (SSU) processome, is an essential protein involved in pre-rRNA processing and 40S ribosomal subunit assembly. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily, including S. cerevisiae Utp23, lack several of these key catalytic residues. Mutation of the remaining conserved putative active site residues seen in Utp23 did not interfere with rRNA maturation and cell viability. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
QKRAKAYRKLMHVYQLTFGFREPYQVLVDDDFLLEAAKQKMDLLKRLERVLQGEVKPMITQCCIQALYAL
GPKNQPAIDLAKTFERRRCNHREADLSPEECIKSVVGPTNKNKHRYIVATQDPKLRRKLRSVPGVPLIHI
NRSVMVLEP
>gnl|CDD|350214 cd09866, PIN_Fcf1-Utp23-H, VapC-like PIN domain of rRNA-processing protein Fcf1- and Utp23-like homologs found in eukaryotes except fungi; similar to human rRNA-processing protein UTP23. PIN domain homologs of Fcf1/Utp24 (FAF1-copurifying factor 1/U three-associated protein 24) and Utp23, essential proteins involved in pre-rRNA processing and 40S ribosomal subunit assembly, are included in this subfamily. It includes human UTP24 which hUTP24 plays a crucial role in human rRNA processing and is essential for accurate endonucleolytic cleavage at the 5'-end of 18S rRNA. Fcf1 is a component of the small subunit (SSU) processome and an essential nucleolar protein required for processing of the 18S pre-rRNA at sites A0-A2. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The Fcf1-Utp23 homolog PIN domain subfamily has three of these conserved acidic residues rather than the four seen in the Fcf1 PIN domain subfamily
NFGFREPYQVLVDGTFCQAALKNKVNIKEQLPKYLQAEVKLCTTQCVIKELEKLGPLLYGALLILKQFQV
HKCGHEKKPVSASECLKSMIKKNNPNHYFVATQDPELQEKLRKIPGVPLLYLHNNTITLE
>gnl|CDD|350215 cd09867, PIN_FEN1, FEN-like PIN domains of Flap endonuclease-1, a structure-specific, divalent-metal-ion dependent, 5' nuclease and homologs. Flap endonuclease-1 (FEN1) is involved in multiple DNA metabolic pathways, including DNA replication processes (5' flap DNA endonuclease activity and double stranded DNA 5'-exonuclease activity) and DNA repair processes (long-patch base excision repair) in eukaryotes and archaea. Interaction between FEN1 and PCNA (Proliferating cell nuclear antigen) is an essential prerequisite to FEN1's DNA replication functionality and stimulates FEN1 nuclease activity by 10-50 fold. FEN1 belongs to the FEN1-EXO1-like subfamily of structure-specific, 5' nucleases (FEN-like family). Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. FEN1 has a C-terminal extension containing residues forming the consensus PIP-box - Qxx(M/L/I)xxF(Y/F) which serves to anchor FEN1 to PCNA
VNLSKLIAIKEIELKDLSGKKIAIDASNALYQFLSAIRQPDGTPLTDSKGRVTSHLSGLFYRTINLLENG
IKPVYVFDGKPPELKSGELEKRRERREEAEEKLEEALEEGDLEEARKYAKRTVRVTKEMVEEAKKLLDLM
GIPYVQAPSEGEAQAAYLVKKGDVYAVASQDYDSLLFGAPRLVRNLTISGKRKLKGVYRKVPPEEIELEE
VLEELELKWKEPDEEGLVKFLCEEHDFSEERVEKALERLKK
>gnl|CDD|350216 cd09868, PIN_XPG_RAD2, FEN-like PIN domains of Xeroderma pigmentosum complementation group G (XPG) nuclease, a structure-specific, divalent-metal-ion dependent, 5' nuclease and homologs. The Xeroderma pigmentosum complementation group G (XPG) nuclease plays a central role in nucleotide excision repair (NER) in cleaving DNA bubble structures or loops. XPG is a member of the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
GVKGLWKLLEPTGRPVSLESLEGKVLAVDASIWLHQFVKGMRDNEGNSVPNAHLLGFFRRICKLLFYGIK
PVFVFDGPAPALKRRTLARRRSVTDEMYEEIQELLRLFGIPYIVAPMEAEAQCAFLERLGLVDGVITDDS
DVFLFGAKRVYKNFFNQNKYVEYYDMEDIERELKFSWGKPDLELLREFCLDKFGWPKEKTDELLLPVLK
>gnl|CDD|350217 cd09869, PIN_GEN1, FEN-like PIN domains of Gap Endonuclease 1, a structure-specific, divalent-metal-ion dependent, 5' nuclease and homologs. Gap Endonuclease 1 (GEN1) is a Holliday junction resolvase reported to symmetrically cleave Holliday junctions and allow religation without additional processing. GEN1 is a member of the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
GVKGLWTILDPVKKRKPLSELRGKTLAVDLSIWICEAQTVLALFETVPKPHLRNLFFRTVNLLRLGIKPV
FVLDGDAPELKLQTIKKRNAARFGGAKKKGGSKKRGRSRFSRVLKECEELLELLGVPVVQAPGEAEALCA
LLNAEGLVDGCITNDGDAFLYGARTVYRNFSLNTKDGSVECYDMSDIEKRLSLRWRRPDLDLLQDFLLKK
LDWDEEYAREKLLPLLT
>gnl|CDD|350218 cd09870, PIN_YEN1, FEN-like PIN domains of Saccharomyces cerevisiae endonuclease 1 (YEN1), Chaetomium thermophilum junction-resolving enzyme GEN1, and fungal homologs. Fungal Endonuclease 1 (YEN1 and GEN1, GEN1 is known as YEN1 in Saccharomyces cerevisiae) is a four-way (Holliday) junction resolvase. Members of this subgroup belong to the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
GIPGLWDLLEPAAESRSLAELAVVEEFNKRGGRPLRIGIDASIWLFHAQSSFGGGHIQAGENPELRTLFY
RLARLLSLPIQPVFVFDGPNRPPFKRGKKVGKSTPHWLTKLFKELLDAFGFPWHEAPGEAEAELARLQRL
GVVDAVLTDDSDALVFGATTVLRNFSKKLSDDDVKVYTASAIKDKADLTRTSLRGPREPDLPRLAALCEK
YFSWGTKEILKRFRRLLWP
>gnl|CDD|350219 cd09871, PIN_MtVapC28-VapC30-like, VapC-like PIN domain of Mycobacterium tuberculosis VapC28 and 30 and related proteins. This subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC28 and VapC30 toxins. M. tuberculosis VapC28 and VapC30 both cleave tRNA25Ser-TGA and tRNA28Ser-CGA. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
MVVDTSALVAILLGEPEAERFLAALAAAPRRLISAATLVEAAIVLERRRGPEARSELDELLAELGIEIVP
VDAEQARLAREAYRRFGKGRHPARLNFGDCFAYALAKELGEPLLFKGDDFAHTDIRSA
>gnl|CDD|350220 cd09872, PIN_Sll0205-like, VapC-like PIN domain of Sll0205 protein and homologs. Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of the Synechocystis sp. (strain PCC 6803) Sll0205 protein and other uncharacterized homologs are included in this subfamily. They are similar to the PIN domains of the Mycobacterium tuberculosis VapC and Neisseria gonorrhoeae FitB toxins of the prokaryotic toxin/antitoxin operons, VapBC and FitAB, respectively, which are believed to be involved in growth inhibition by regulating translation. These toxins are nearly always co-expressed with an antitoxin, a cognate protein inhibitor, forming an inert protein complex. Disassociation of the protein complex activates the ribonuclease activity of the toxin by an, as yet undefined mechanism. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTHALLWWLTDPPRLSPKARALIEDPANEVFVSAASLWEIAIKVSLGKLDLPGPLEEWLEELLAANGF
EILPITPEHALAAASLPLHHRDPFDRLLIAQAIVEGLTLVTADRKILAYGVKTIW
>gnl|CDD|350221 cd09873, PIN_Pae0151-like, VapC-like PIN domain of the Pyrobaculum aerophilum Pae0151 and Pae2754 proteins and homologs. Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of the Pyrobaculum aerophilum proteins, Pae0151 and Pae2754, and homologs are included in this subfamily. They are similar to the PIN domains of the Mycobacterium tuberculosis VapC and Neisseria gonorrhoeae FitB toxins of the prokaryotic toxin/antitoxin operons, VapBC and FitAB, respectively, which are believed to be involved in growth inhibition by regulating translation. These toxins are nearly always co-expressed with an antitoxin, a cognate protein inhibitor, forming an inert protein complex. Disassociation of the protein complex activates the ribonuclease activity of the toxin by an, as yet undefined mechanism. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
VVDASVAVKWLLPEEESEAADRLLERLEEELVAPDLWLYEVANVLRKAVRRGRLTEEEAEEALEDLLDLP
IEIDPDPELLEEALELARRHGLTAYDAAYLALAERLGAPLVTADRKLARAAKAAGVKL
>gnl|CDD|350222 cd09874, PIN_MT3492-like, VapC-like PIN domain of the hypothetical protein MT3492 of Mycobacterium tuberculosis CDC1551 and other uncharacterized, annotated PilT protein domain proteins. Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis CDC1551, hypothetical protein MT3492, and similar bacterial and archaeal proteins are included in this subfamily. They are PIN domain homologs of the Mycobacterium tuberculosis VapC and Neisseria gonorrhoeae FitB toxins of the prokaryotic toxin/antitoxin operons, VapBC and FitAB, respectively, which are believed to be involved in growth inhibition by regulating translation. These toxins are nearly always co-expressed with an antitoxin, a cognate protein inhibitor, forming an inert protein complex. Disassociation of the protein complex activates the ribonuclease activity of the toxin by an, as yet undefined mechanism. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LYLDTSALVKLYVREPGSDAVRALLDAASDVLAISDLTRVEFASALARKVREGELSEEQARAALAAFERD
WASLLRVVPVTDSLFRRAAELAERHGLRALDALHLASALRLGALTFVTADKRLAEAARAEGLKV
>gnl|CDD|350223 cd09875, PIN_VapC-FitB-like, VapC-like PIN domain of ribonucleases (toxins), VapC and FitB, of prokaryotic toxin/antitoxin operons, Pyrococcus horikoshii protein PH0500, and other similar bacterial and archaeal homologs. PIN (PilT N terminus) domain-containing proteins of prokaryotic toxin/antitoxin (TA) operons, such as, Mycobacterium tuberculosis VapC of the VapBC (virulence associated proteins) TA operon, and Neisseria gonorrhoeae FitB of the FitAB (fast intracellular trafficking) TA operon, as well as, the archaeal Pyrococcus horikoshii protein PH0500 are included in this family. Toxins of TA operons are believed to be involved in growth inhibition by regulating translation and are nearly always co-expressed with an antitoxin, a cognate protein inhibitor, forming an inert protein complex. Disassociation of the complex activates the ribonuclease activity of the toxin. In N. gonorrhoeae, FitA and FitB form a heterodimer: FitA is the DNA binding subunit and FitB contains a ribonuclease activity that is blocked by the presence of FitA. A tetramer of FitAB heterodimers binds DNA from the fitAB upstream promoter region with high affinity. This results in both sequestration of FitAB and repression of fitAB transcription. It is thought that FitAB release from the DNA and subsequent dissociation both slows N. gonorrhoeae replication and transcytosis by an as yet undefined mechanism. The toxin M. tuberculosis VapC is a structural homolog of N. gonorrhoeae FitB, but their antitoxin partners, VapB and FitA, respectively, differ structurally. The M. tuberculosis VapC-5 is proposed to be both an endoribonuclease and an exoribonuclease that can act on free RNA in a similar manner to the endo and exonuclease Flap endonuclease-1 (FEN1). VapC-like toxins are structural homologs of FEN1-like PIN domains, but lack the extensive arch/clamp region and the H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region, seen in FEN1-like PIN domains. PIN domains within this group typically contain three or four conserved acidic residues that cluster at the C-terminal end of the beta-sheet and form a negatively charged pocket near the center of the molecule. These putative active site residues are thought to bind Mg2+ and/or Mn2+ ions and be essential for single-stranded ribonuclease activity. VapC-like PIN domains are single domain proteins that form dimers and dimerization configures the active sites in a groove along the long-axis of the structure
LLDTSVLIWLLDNDPKSHLRSLADRIERGKVYVSIVSRWELAIGVNINKLRLNYAFADLENLLADLAIPV
LPLTPRIADEYLEACRNLPLRGRHRSPFDRMIAAQALQHGFTVAHRDEDFKAINAVNLEW
>gnl|CDD|350224 cd09876, PIN_Nob1-like, VapC-like PIN domain of eukaryotic ribosome assembly factor Nob1 and archaeal UPF0129 protein Ta0041-like homologs. PIN (PilT N terminus) domain of the Saccharomyces cerevisiae ribosome assembly factor, Nob1 (Nin one binding) protein, the Thermoplasma acidophilum DSM 1728, UPF0129 protein Ta0041, and similar eukaryotic and archaeal homologs are included in this family. The Nob1 PIN domain binds the single-stranded cleavage site D at the 3-prime end of 18S rRNA. Recombinant Nob1 binds as a tetramer to pre-18S rRNA fragments containing cleavage site D and believed to cleave at this site. This subgroup belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_6
LVLDTSAFISGAPLDGLAEKLYTTPEVLEEIRDKKSRLRLELLPGKLKVREPSEESIKAVKEFAKKTGDY
GSLSATDIKVLALALELEAEIVTDDYAIQNVAKHLGIKFKSI
>gnl|CDD|350225 cd09877, PIN_YacL-like, VapC-like PIN domain of Thermus Thermophilus Hb8, uncharacterized Bacillus subtilis YacL, and other bacterial homologs. PIN (PilT N terminus) domain of the conserved membrane protein of unknown function of Thermus Thermophilus Hb8, Bacillus subtilis YacL and other similar homologs are included in this family. This subgroup belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Proteins in this group have a C-terminal TRAM domain whose function is unknown but predicted to be a RNA-binding domain common to tRNA uracil methylation and adenine thiolation enzymes
KVLDTSVLIDGRIADIAKTGFLDGTLVVPRFVLDELQLLADSSDPLKRARGRRGLDVLKKLQKLPGLDVR
IVDTDFPEIKEVDAKLVRLAKELGAKLLTNDFNLNKVAKLQGVKVLNINELANALKP
>gnl|CDD|350226 cd09878, PIN_VapC_VirB11L-ATPase-like, VapC-like PIN domain of an uncharacterized AAA+, VirB11-like ATPase-, KH- and PIN-domain containing protein MJ1533 from Methanocaldococcus jannaschii DSM 2661, and other similar archaeal homologs. PIN (PilT N terminus) domain present N-terminal of AAA+, VirB11-like ATPases. Several members of this subfamily possess an AAA+, VirB11-like ATPase domain, flanked by PIN and KH nucleic acid-binding domains. VirB11-ATPase is a type IV secretory pathway component required for T-pilus biogenesis and virulence. This subgroup belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. PIN domains within this subgroup contain four of these highly conserved residues which cluster at the C-terminal end of the beta-sheet and form a negatively charged pocket near the center of the molecule. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
YVPDTSVIIDGRISKLIEEGELKGGEIIIPEAVVAELEHQANKGREIGFAGLEELKKLRELAKEGGIKLE
FVGERPTLEEIKLAKSGEIDALIRDVAREEGATLVTSDRVQAEVAEAEGIEVIYL
>gnl|CDD|350227 cd09879, PIN_VapC_AF0591-like, VapC-like PIN domain of Archaeoglobus fulgidus AF0591 protein and other similar archaeal homologs. PIN (PilT N terminus) domain of Archaeoglobus fulgidus AF0591 protein and other similar uncharacterized archaeal homologs are included in this family. This subgroup belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. PIN domains within this subgroup contain four of these highly conserved putative metal-binding, active site residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains and included distant subgroups, this subgroup includes some sequences belonging to one of these, PIN_14
VILDTNFLMYPFQFGVDIFEELERLLGKYEIVVPSAVIEELERLAKKGKGKDKRAARLALKLAERCKVVE
SEGEPADDAILELAKELGAIVATNDRELRKRLREKGIPVIYLRQKKRL
>gnl|CDD|350228 cd09880, PIN_Smg5-6-like, VapC-like PIN domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and related proteins. PIN (PilT N terminus) domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and homologs are included in this family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo. Many of the bacterial homologs in this group have an N-terminal PIN domain and a C-terminal PhoH-like ATPase domain
VFDTNILLSHLDVLKLLVESGKWTVVIPLIVITELDGLKKNPDPLGPKARSALRYIEACLKKHSRWLRVQ
TSKGNYLADLTIRSEQLSDASELRRRNNDDRILECALWQQKHFVDREDGDGKVVLVTNDRNLRLKARARG
VEAVTVKELLKS
>gnl|CDD|350229 cd09881, PIN_VapC4-5_FitB-like, VapC-like PIN domain of Mycobacterium tuberculosis VapC4 and VapC5, and Neisseria gonorrhoeae FitB and related proteins. This family includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This family belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTNICIDLLRGRPPSVLERLEELLPEDLAISSITLAELLYGAEKSQRPEKNLAALEAFLSRLEVLPFD
EEAAEIYGEIRAELEKKGKPIGDNDLLIAATALAHGLTLVTNNTKHFERIPGLKVEN
>gnl|CDD|350230 cd09882, PIN_MtVapC3-like_start, VapC-like PIN domain of Mycobacterium tuberculosis VapC3 toxin and related proteins. The VapC3-like nuclease subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of various Mycobacterium tuberculosis VapC toxins including VapC3, VapC11, VapC15, and VapC21. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LVDTSVWIDFFRGRDTPQVERLKELIEEGEDVALTGIILTEVLQGIRDEKEFQRVKEYLLALPILPLTGE
TYIAAARLYRRLRRKGVTVRSTIDCLIAATAIENGLTLLHNDRDFEAIAKHTGLKLYR
>gnl|CDD|350231 cd09883, PIN_VapC_PhoHL-ATPase, VapC-like PIN domain of bacterial Smg6-like proteins with C-terminal PhoH-like ATPase domains. PIN (PilT N terminus) domain of Smg6-like bacterial proteins with C-terminal PhoH-like ATPase domains and other similar homologs are included in this family. Eukaryotic Smg5 and Smg6 nucleases are essential factors in nonsense-mediated mRNA decay (NMD), a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal ion dependent, degradation of single-stranded RNA, in vitro. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. PIN domains within this subgroup contain four highly conserved acidic residues (putative metal-binding, active site residues). Many of the bacterial homologs in this group have an N-terminal PIN domain and a C-terminal PhoH-like ATPase domain and are predicted to be ATPases which are induced by phosphate starvation
KKTYVLDTNVLLHDPNAIFKFEDNDVVIPITVLEELDKLKKRNDELGRNAREAIRNLDELREKGSLAEGV
PLENGGTLRVELNHKDLLPLPELDLDKNDNRILAVALKLKEEGDRPVILVTKDINLRIKADALGIKAEDY
ETDKVS
>gnl|CDD|350232 cd09884, PIN_Smg5-like, VapC-like PIN domain of human nonsense-mediated decay factor Smg5, and other similar eukaryotic homologs. Nonsense-mediated decay (NMD) factors, Smg5 and Smg6 are essential to the post-transcriptional regulatory pathway, NMD, which recognizes and rapidly degrades mRNAs containing premature translation termination codons. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo
PYLVPDTSALCDHLHLIKQLVQSGKFIVIIPLAVIDGLDELKKESAGAREAIRWLEAEFKKGNRYIRAQK
PNEKLPLPLLKRPKKKDRDAWRLYQILDCCKYLAQQQGDGEEDGAGMVTLLTGNDLDEKEAFNKGFSVLG
AAHAAGVEIENILDFYSKWK
>gnl|CDD|350233 cd09885, PIN_Smg6-like, VapC-like PIN domain of human telomerase-binding protein EST1, Smg6, and other similar eukaryotic homologs. Nonsense-mediated decay (NMD) factors, Smg5 and Smg6 are essential to the post-transcriptional regulatory pathway, NMD, which recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN (PilT N terminus) domain elicits degradation of bound mRNAs, as well as, metal ion dependent, degradation of single-stranded RNA, in vitro. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. PIN domains within this subgroup contain four highly conserved acidic residues (putative metal-binding, active site residues) which cluster at the C-terminal end of the beta-sheet and form a negatively charged pocket near the center of the molecule. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo. Eukaryotic Smg6 PIN domains are present at the C-terminal end of the telomerase activating proteins, EST1
IEVRPRYLVPDTNCFIDHLELIEKLVESRKFTVLVPLIVVNELDGLAKGSESDSYADEAHAEEVQAKARK
AVKFLEEQFEARNPYVRALTSKGTLLDTIAFRSEDINDGDGGNNDDLILSCCLNLCKDKAVDFMPASKDQ
PIRLYREVVLLTDDRNLRVKALSRNIPVRDLPSFLKWA
>gnl|CDD|193575 cd09886, NGN_SP, N-Utilization Substance G (NusG) N-terminal domain in the NusG Specialized Paralog (SP). The N-Utilization Substance G (NusG) protein is involved in transcription elongation and termination. NusG is essential in Escherichia coli and is associated with RNA polymerase elongation and Rho-termination in bacteria. Paralogs of eubacterial NusG, NusG SP (Specialized Paralog of NusG), are more diverse and often found as the first ORF in operons encoding secreted proteins and LPS biosynthesis genes. NusG SP family members are operon-specific transcriptional antitermination factors. The NusG N-terminal (NGN) domain is quite similar in all NusG orthologs, but its C-terminal domains and the linker that separate these two domains are different. The domain organization of NusG and its orthologs suggest that the common properties of NusG and its orthologs and paralogs are due to their similar NGN domains
SWYALRTNPGCEQRAEEALEARGVEAFLPMLTEERKRRRKKFDVERPLFPGYVFARLDRSKGQDTSTIRA
CDGVLGVVGFDGRPAPVPEQEMRDLRK
>gnl|CDD|193576 cd09887, NGN_Arch, Archaeal N-Utilization Substance G (NusG) N-terminal (NGN) domain. The N-Utilization Substance G (NusG) protein and its eukaryotic homolog, Spt5, are involved in transcription elongation and termination. Transcription in archaea has a eukaryotic-type transcription apparatus, but contains bacterial-type transcription factors. NusG is one of the few archaeal transcription factors that has orthologs in both bacteria and eukaryotes. Archaeal NusG is similar to bacterial NusG, composed of an NGN domain and a Kyrpides Ouzounis and Woese (KOW) repeat. The eukaryotic ortholog, Spt5, is a large protein composed of an acidic N-terminus, an NGN domain, and multiple KOW motifs at its C-terminus. NusG was originally discovered as a N-dependent antitermination enhancing activity in Escherichia coli and has a variety of functions, such as being involved in RNA polymerase elongation and Rho-termination in bacteria. Archaeal NusG forms a complex with DNA-directed RNA polymerase subunit E (rpoE) that is similar to the Spt5-Spt4 complex in eukaryotes
RIYAVKTTAGQERNVADLLAMRAEKENLDVYSILVPEELKGYVFVEAEDPDRVEELIRGIPHVRGVVPGE
ISLEEIEHFLKP
>gnl|CDD|193577 cd09888, NGN_Euk, Eukaryotic N-Utilization Substance G (NusG) N-terminal (NGN) domain, including plant KTF1 (KOW domain-containing Transcription Factor 1). The N-Utilization Substance G (NusG) protein and its eukaryotic homolog, Spt5, are involved in transcription elongation and termination. NusG contains an NGN domain at its N-terminus and Kyrpides Ouzounis and Woese (KOW) repeats at its C-terminus. Spt5 forms an Spt4-Spt5 complex that is an essential RNA polymerase II elongation factor. NusG was originally discovered as an N-dependent antitermination enhancing activity in Escherichia coli, and has a variety of functions such as its involvement in RNA polymerase elongation and Rho-termination in bacteria. Orthologs of the NusG gene exist in all bacteria, but their functions and requirements are different. Spt5-like is homologous to the Spt5 proteins present in all eukaryotes, which is unique as it encodes a protein with an additional long carboxy-terminal extension that contains WG/GW motifs. Spt5-like, or KTF1 (KOW domain-containing Transcription Factor 1), is a RNA-directed DNA methylation (RdDM) pathway effector in plants
KLWAVKCKPGKEREIVISLMRKFLDLQRTGNPLGIKSVFARDGLKGYIYIEARKEAHVKDAIEGLRGVYL
NTIKLVPIKEMPDVLS
>gnl|CDD|193578 cd09889, NGN_Bact_2, Bacterial N-Utilization Substance G (NusG) N-terminal (NGN) domain, subgroup 2. The N-Utilization Substance G (NusG) protein is involved in transcription elongation and termination. NusG is essential in Escherichia coli and associates with RNA polymerase elongation and Rho-termination. Paralogs of eubacterial NusG, NusG SP (Specialized Paralog of NusG), are more diverse and often found as the first ORF in operons encoding secreted proteins and LPS biosynthesis genes. NusG SP family members are operon-specific transcriptional antitermination factors. The NusG N-terminal domain (NGN) is quite similar in all NusG orthologs, but its C-terminal domain and the linker that separates these two domains are different. The domain organization of NusG and its orthologs suggests that the common properties of NusG and its orthologs and paralogs are due to their similar NGN domains
MWYVVQVRTGREKAVLELLEKLVGPDVLQECFIPQYERKKRSQGVWRERKYTLFPGYVFVVTDDIDELYY
ELKRVPGFTRLLGNDGSFFPLTPEEADFIR
>gnl|CDD|193579 cd09890, NGN_plant, Plant N-Utilization Substance G (NusG) N-terminal (NGN) domain. The N-Utilization Substance G (NusG) protein and its eukaryotic homolog, Spt5, are involved in transcription elongation and termination. NusG contains a NGN domain at its N-terminus and Kyrpides Ouzounis and Woese (KOW) repeats at its C-terminus in bacteria and archaea. The eukaryotic ortholog, Spt5, is a large protein comprising an acidic N-terminus, an NGN domain, and multiple KOW motifs at its C-terminus. Spt5 forms an Spt4-Spt5 complex that is an essential RNA polymerase II elongation factor. The bacterial infected plants contain bacterial DNA, such as NGN sequences, that can be used to clone the DNA of uncultured organisms
QWYMLRVPAGRENQAAEALERALATEFPDREFEVWVPSIPVDRKLKNGSISVKEKPLFPGYVLLRCVLNK
EVYDFIRDNDSVYGFVGSKVGKTGKRQIEIPRPVPVEEIEAIF
>gnl|CDD|193580 cd09891, NGN_Bact_1, Bacterial N-Utilization Substance G (NusG) N-terminal (NGN) domain, subgroup 1. The N-Utilization Substance G (NusG) protein is involved in transcription elongation and termination in bacteria. NusG is essential in Escherichia coli and associates with RNA polymerase elongation and Rho-termination. Homologs of the NusG gene exist in all bacteria. The NusG N-terminal domain (NGN) is similar in all NusG homologs, but its C-terminal domain and the linker that separates these two domains are different. The domain organization of NusG suggests that the common properties of NusG and its homologs are due to their similar NGN domains
KWYVVHTYSGYENKVKENLEKRIESEGLEDYIGEVLVPTEEVVEVKNGKKKVKERKLFPGYVLVEMDMND
DTWHLVRNTPGVTGFVGSGGKPVPLSEEEVERILGQV
>gnl|CDD|193581 cd09892, NGN_SP_RfaH, N-Utilization Substance G (NusG) N-terminal domain in the NusG Specialized Paralog (SP), RfaH. RfaH is an operon-specific virulence regulator, thought to have arisen from an early duplication of N-Utilization Substance G (NusG). Paralogs of eubacterial NusG, NusG SP (Specialized Paralog of NusG), are more diverse and often found as the first ORF in operons encoding secreted proteins and LPS biosynthesis genes. NusG SP family members are operon-specific transcriptional antitermination factors. NusG is essential in Escherichia coli and is associated with RNA polymerase elongation and Rho-termination in bacteria. In contrast, RfaH is a non-essential protein that controls expression of operons containing an ops (operon polarity suppressor) element in their transcribed DNA. RfaH and NusG are different in their response to Rho-dependent terminators and regulatory targets. The NusG N-terminal (NGN) domain is quite similar in all NusG orthologs, but its C-terminal domains and the linker that separate these two domains are different. The domain organization of NusG and its homologs suggest that the common properties of NusG and RfaH are due to their similar NGN domains
AWYLLYTKPRQEERAAENLERQGFEVFLPMIRVEKRRRGKRTVVTEPLFPGYLFVRLDPEVQNWRPIRST
RGVSRLVRFGGEPAPVPDALIEALRA
>gnl|CDD|193582 cd09893, NGN_SP_TaA, N-Utilization Substance G (NusG) N-terminal domain in the NusG Specialized Paralog (SP), TaA. The N-Utilization Substance G (NusG) protein is involved in transcription elongation and termination. NusG is essential in Escherichia coli and is associated with RNA polymerase elongation and Rho-termination in bacteria. Paralogs of eubacterial NusG, NusG SP (Specialized Paralog of NusG), are more diverse and often found as the first ORF in operons encoding secreted proteins and LPS biosynthesis genes. NusG SP family members are operon-specific transcriptional antiterminationn factors. TaA is a NusG SP factor that is required for synthesis of a polyketide antibiotic TA in Myxococcus xanthus. Orthologs of the NusG gene exist in all bacteria, but its functions and requirements are different. The NusG N-terminal (NGN) domain is quite similar in all NusG orthologs, but its C-terminal domains and the linker that separate these two domains are different. The domain organization of NusG and its orthologs suggest that the common properties of NusG and its orthologs and paralogs are due to their similar NGN domains
SWYALYTRSRHEKKVADRLAKKGIESFLPLYEVLSRWKDRKKKIKVPLFPGYLFVRFQLDPERLRILKTP
GVVRIVGNSGGPIPIPDEEIASLRI
>gnl|CDD|193583 cd09894, NGN_SP_AnfA1, N-Utilization Substance G (NusG) N-terminal domain in the NusG Specialized Paralog (SP), AnFA1. Regulation of the afp, antifeeding prophage, gene cluster is mediated by AnFA1, a RfaH-like transcriptional antiterminator. RfaH is an operon-specific virulence regulator, thought to arisen from an early duplication of N-Utilization Substance G (NusG). NusG is essential in Escherichia coli and is associated with RNA polymerase elongation and Rho-termination in bacteria. Paralogs of eubacterial NusG, NusG SP (Specialized Paralog of NusG), are more diverse and often found as the first ORF in operons encoding secreted proteins and LPS biosynthesis genes. NusG SP family members are operon-specific transcriptional antitermination factors. Orthologs of the NusG gene exist in all bacteria, but their functions and requirements are different. The NusG N-terminal domain (NGN) is similar in all NusG orthologs, but its C-terminal domain and the linker that separate these two domains are different. The domain organization of NusG and its orthologs suggests that the common properties of NusG and its orthologs and paralogs are due to their similar NGN domains
KRWYLLRCKSGKIQSVIFSLERLGVEVFCPMIRTRRKRTDCKSYREKIEPLFPGYLFVRFDPEVVHTSKI
TLASGVSGFVRFGGEPCPVPDAVIRALML
>gnl|CDD|193584 cd09895, NGN_SP_UpxY, N-Utilization Substance G (NusG) N-terminal domain in the NusG Specialized Paralog (SP), UpxY. The N-Utilization Substance G (NusG) proteins are involved in transcription elongation and termination. NusG is essential in Escherichia coli and is associated with RNA polymerase elongation and Rho-termination. Paralogs of eubacterial NusG, NusG SP (Specialized Paralog of NusG), are more diverse and often found as the first ORF in operons encoding secreted proteins and LPS (lipopolysaccharide) biosynthesis genes. NusG SP family members are operon-specific transcriptional antitermination factors. UpxY proteins, UpxY proteins, where the x is replaced by the letter designation of the specific polysaccharide (UpaY to UphY), are a family of NusG SP factors that act specifically in transcriptional antitermination of operons from which they are encoded. UpxYs are necessary and specific for transcription regulation of the polysaccharide biosynthesis operon. Orthologs of the NusG gene exist in all bacteria, but their functions and requirements are different. The NusG N-terminal (NGN) domain is similar in all NusG orthologs, but its C-terminal domain and the linker that separate these two domains are different. The domain organization of NusG and its orthologs suggests that the common properties of NusG and its orthologs and paralogs are due to their similar NGN domains
PWYALYTFPRREKKVAEYLEKKGIECFLPMQYEVRQWSGRKKRVEVPLFPNLVFVHITREELDEVLETPG
VVRFVRYRGKEPAIIPDKQMESFRL
>gnl|CDD|188617 cd09897, H3TH_FEN1-XPG-like, H3TH domains of Flap endonuclease-1 (FEN1)-like structure specific 5' nucleases. The 5' nucleases within this family are capable of both 5'-3' exonucleolytic activity and cleaving bifurcated or branched DNA, in an endonucleolytic, structure-specific manner, and are involved in DNA replication, repair, and recombination. This family includes the H3TH (helix-3-turn-helix) domains of Flap Endonuclease-1 (FEN1), Exonuclease-1 (EXO1), Mkt1, Gap Endonuclease 1 (GEN1), Xeroderma pigmentosum complementation group G (XPG) nuclease, and other eukaryotic and archaeal homologs. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Both the H3TH domain and the helical arch/clamp region are involved in DNA binding. Studies suggest that a glycine-rich loop in the H3TH domain contacts the phosphate backbone of the template strand in the downstream DNA duplex. With the except of the Mkt1-like proteins, the nucleases within this family have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors (i. e., Mg2+, Mn2+, Zn2+, or Co2+) required for nuclease activity. The first metal binding site is composed entirely of Asp/Glu residues from the PIN domain, whereas, the second metal binding site is composed generally of two Asp residues from the PIN domain and one Asp residue from the H3TH domain. Together with the helical arch and network of amino acids interacting with metal binding ions, the H3TH region defines a positively charged active-site DNA-binding groove in structure-specific 5' nucleases
EQFIDLCILSGCDYLPGLPGIGPKTALKLIKEYGSLEKVLKALRDDKKDKVPVPYDFPYKKARELFLH
>gnl|CDD|188618 cd09898, H3TH_53EXO, H3TH domain of the 5'-3' exonuclease of Taq DNA polymerase I and homologs. H3TH (helix-3-turn-helix) domains of the 5'-3' exonuclease (53EXO) of mutli-domain DNA polymerase I and single domain protein homologs are included in this family. Taq DNA polymerase I contains a polymerase domain for synthesizing a new DNA strand and a 53EXO domain for cleaving RNA primers or damaged DNA strands. Taq's 53EXO recognizes and endonucleolytically cleaves a structure-specific DNA substrate that has a bifurcated downstream duplex and an upstream template-primer duplex that overlaps the downstream duplex by 1 bp. The 53EXO cleaves the unpaired 5'-arm of the overlap flap DNA substrate. 5'-3' exonucleases are members of the structure-specific, 5' nuclease family that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Both the H3TH domain and the helical arch/clamp region are involved in DNA binding. Studies suggest that a glycine-rich loop in the H3TH domain contacts the phosphate backbone of the template strand in the downstream DNA duplex. The nucleases within this family have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors (i. e., Mg2+ or Mn2+ or Zn2+) required for nuclease activity. The first metal binding site is composed entirely of Asp/Glu residues from the PIN domain, whereas, the second metal binding site is composed generally of two Asp residues from the PIN domain and two Asp residues from the H3TH domain. Together with the helical arch and network of amino acids interacting with metal binding ions, the H3TH region defines a positively charged active-site DNA-binding groove in structure-specific 5' nucleases
PEQIIDYLALVGDSSDNIPGVPGIGPKTAAKLLQEYGSLENILANLDELKGKLREKLEENKEQALLSRKL
ATL
>gnl|CDD|188619 cd09899, H3TH_T4-like, H3TH domain of bacteriophage T3, T4 RNase H, T5-5' nucleases, and homologs. H3TH (helix-3-turn-helix) domains of bacteriophage T5-5'nuclease (5'-3' exonuclease or T5FEN), bacteriophage T4 RNase H (T4FEN), bacteriophage T3 (T3 phage exodeoxyribonuclease) and other similar 5' nucleases are included in this family. The T5-5'nuclease is a 5'-3' exodeoxyribonuclease that also exhibits endonucleolytic activity on flap structures (branched duplex DNA containing a free single-stranded 5'end). T4 RNase H, which removes the RNA primers that initiate lagging strand fragments, has 5'- 3' exonuclease activity on DNA/DNA and RNA/DNA duplexes and has endonuclease activity on flap or forked DNA structures. Bacteriophage T3 is believed to function in the removal of DNA-linked RNA primers and is essential for phage DNA replication and also necessary for host DNA degradation and phage genetic recombination. These nucleases are members of the structure-specific, 5' nuclease family that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. They contain a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Both the H3TH domain and the helical arch/clamp region are involved in DNA binding. Studies suggest that a glycine-rich loop in the H3TH domain contacts the phosphate backbone of the template strand in the downstream DNA duplex. The nucleases within this family have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors required for nuclease activity. The first metal binding site (MBS-1) is composed entirely of Asp/Glu residues from the PIN domain, whereas, the second metal binding site (MBS-2) is composed generally of two Asp residues from the PIN domain and two Asp residues from the H3TH domain. In the T5-5'nuclease, structure-specific endonuclease activity requires binding of a single metal ion in the high-affinity, MBS-1, whereas exonuclease activity requires both, the high-affinity, MBS-1 and the low-affinity, MBS-2 to be occupied by a divalent cofactor. The T5-5'nuclease is reported to be able to bind several metal ions including, Mg2+, Mn2+, Zn2+ and Co2+, as co-factors. Together with the helical arch and network of amino acids interacting with metal binding ions, the H3TH region defines a positively charged active-site DNA-binding groove in structure-specific 5' nucleases
DPEAYLSAKALAGDTKDNIAGVPGIGTGRATKLLEEIGDVADIIDALLTPGKVKNSLALEEAYERFKENL
ILID
>gnl|CDD|188620 cd09900, H3TH_XPG-like, H3TH domains of Flap endonuclease-1 (FEN1)-like structure specific 5' nucleases: FEN1 (archaeal), GEN1, YEN1, and XPG. The 5' nucleases within this family are capable of both 5'-3' exonucleolytic activity and cleaving bifurcated or branched DNA, in an endonucleolytic, structure-specific manner, and are involved in DNA replication, repair, and recombination. This family includes the H3TH (helix-3-turn-helix) domains of archaeal Flap Endonuclease-1 (FEN1), Gap Endonuclease 1 (GEN1), Yeast Endonuclease 1 (YEN1), Xeroderma pigmentosum complementation group G (XPG) nuclease, and other eukaryotic and archaeal homologs. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Both the H3TH domain and the helical arch/clamp region are involved in DNA binding. Studies suggest that a glycine-rich loop in the H3TH domain contacts the phosphate backbone of the template strand in the downstream DNA duplex. With the except of the Mkt1-like proteins, the nucleases within this family have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors (i. e., Mg2+, Mn2+, Zn2+, or Co2+) required for nuclease activity. The first metal binding site is composed entirely of Asp/Glu residues from the PIN domain, whereas, the second metal binding site is composed generally of two Asp residues from the PIN domain and one Asp residue from the H3TH domain. Together with the helical arch and network of amino acids interacting with metal binding ions, the H3TH region defines a positively charged active-site DNA-binding groove in structure-specific 5' nucleases
EQLILLALLLGTDYNPGVPGIGPKTALELLKEFGEDLEKFLESEEILEAYLN
>gnl|CDD|188621 cd09901, H3TH_FEN1-like, H3TH domains of Flap endonuclease-1 (FEN1)-like structure specific 5' nucleases: FEN1 (eukaryotic) and EXO1. The 5' nucleases within this family are capable of both 5'-3' exonucleolytic activity and cleaving bifurcated or branched DNA, in an endonucleolytic, structure-specific manner, and are involved in DNA replication, repair, and recombination. This family includes the H3TH (helix-3-turn-helix) domains of eukaryotic Flap Endonuclease-1 (FEN1), Exonuclease-1 (EXO1), and other eukaryotic homologs. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Both the H3TH domain and the helical arch/clamp region are involved in DNA binding. Studies suggest that a glycine-rich loop in the H3TH domain contacts the phosphate backbone of the template strand in the downstream DNA duplex. The nucleases within this family have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors (i. e., Mg2+, Mn2+, Zn2+, or Co2+) required for nuclease activity. The first metal binding site is composed entirely of Asp/Glu residues from the PIN domain, whereas, the second metal binding site is composed generally of two Asp residues from the PIN domain and one Asp residue from the H3TH domain. Together with the helical arch and network of amino acids interacting with metal binding ions, the H3TH region defines a positively charged active-site DNA-binding groove in structure-specific 5' nucleases
EQFIDLCILSGCDYLPSIPGIGPKTAYKLIKKHKSIEKVLKALRSNKKKKVPVPYEEPFKEARLTFLHQR
VYD
>gnl|CDD|188622 cd09902, H3TH_MKT1, H3TH domain of Mkt1: A global regulator of mRNAs encoding mitochondrial proteins and eukaryotic homologs. The Mkt1 gene product interacts with the Poly(A)-binding protein associated factor, Pbp1, and is present at the 3' end of RNA transcripts during translation. The Mkt1-Pbp1 complex is involved in the post-transcriptional regulation of HO endonuclease expression. Mkt1 and eukaryotic homologs are atypical members of the structure-specific, 5' nuclease family. Conical members of this family possess a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH (helix-3-turn-helix) domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Although Mkt1 appears to possess both a PIN and H3TH domain, the Mkt1 PIN domain lacks several of the active site residues necessary to bind essential divalent metal ion cofactors (Mg2+/Mn2+) required for nuclease activity in this family. Also, Mkt1 lacks the glycine-rich loop in the H3TH domain which is proposed to facilitate duplex DNA binding
EQFLDACLLAGTELCPTFPPLQDSPFPKPQNFRDALDMVKQARSGISVCQQFPDTPSVNDKNYLDQYCKA
KSAVKYHLVLT
>gnl|CDD|188623 cd09903, H3TH_FEN1-Arc, H3TH domain of Flap Endonuclease-1, a structure-specific, divalent-metal-ion dependent, 5' nuclease: Archaeal homologs. Members of this subgroup include the H3TH (helix-3-turn-helix) domains of archaeal Flap endonuclease-1 (FEN1), 5' nucleases. FEN1 is involved in multiple DNA metabolic pathways, including DNA replication processes (5' flap DNA endonuclease activity and double stranded DNA 5'-exonuclease activity) and DNA repair processes (long-patch base excision repair) in eukaryotes and archaea. Interaction between FEN1 and PCNA (Proliferating cell nuclear antigen) is an essential prerequisite to FEN1's DNA replication functionality and stimulates FEN1 nuclease activity by 10-50 fold. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Both the H3TH domain and the helical arch/clamp region are involved in DNA binding. Studies suggest that a glycine-rich loop in the H3TH domain contacts the phosphate backbone of the template strand in the downstream DNA duplex. The nucleases within this subfamily have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors (Mg2+ or Mn2+) required for nuclease activity. The first metal binding site is composed entirely of Asp/Glu residues from the PIN domain, whereas, the second metal binding site is composed generally of two Asp residues from the PIN domain and one Asp residue from the H3TH domain. Together with the helical arch and network of amino acids interacting with metal binding ions, the H3TH region defines a positively charged active-site DNA-binding groove in structure-specific 5' nucleases. Also, FEN1 has a C-terminal extension containing residues forming the consensus PIP-box - Qxx(M/L/I)xxF(Y/F) which serves to anchor FEN1 to PCNA
EQLIDIAILVGTDYNPGGVKGIGPKTALKLVKEYGDLEKVLRSVEDEIVDPEEIREIFLNPPVTD
>gnl|CDD|188624 cd09904, H3TH_XPG, H3TH domain of Xeroderma pigmentosum complementation group G (XPG) nuclease, a structure-specific, divalent-metal-ion dependent, 5' nuclease. The Xeroderma pigmentosum complementation group G (XPG) nuclease plays a central role in nucleotide excision repair (NER) in cleaving DNA bubble structures or loops. XPG is a member of the structure-specific, 5' nuclease family that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Members of this subgroup include the H3TH (helix-3-turn-helix) domains of XPG and other similar eukaryotic 5' nucleases. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Both the H3TH domain and the helical arch/clamp region are involved in DNA binding. Studies suggest that a glycine-rich loop in the H3TH domain contacts the phosphate backbone of the template strand in the downstream DNA duplex. These nucleases have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors (Mg2+ or Mn2+) required for nuclease activity. The first metal binding site is composed entirely of Asp/Glu residues from the PIN domain, whereas, the second metal binding site is composed generally of two Asp residues from the PIN domain and one Asp residue from the H3TH domain. Together with the helical arch and network of amino acids interacting with metal binding ions, the H3TH region defines a positively charged active-site DNA-binding groove in structure-specific 5' nucleases
DKLIRLALLLGSDYTEGVSGIGPVNAMEILSEFPGEEDLEKFKDWWENAQPEKSEDSDNDKQEFKRKHKN
YLKNLILPPGFPSPAVINAYLNPNVDD
>gnl|CDD|188625 cd09905, H3TH_GEN1, H3TH domain of Gap Endonuclease 1, a structure-specific, divalent-metal-ion dependent, 5' nuclease. Gap Endonuclease 1 (GEN1): Holliday junction resolvase reported to symmetrically cleave Holliday junctions and allow religation without additional processing. GEN1 is a member of the structure-specific, 5' nuclease family that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Members of this subgroup include the H3TH (helix-3-turn-helix) domains of GEN1 and other similar eukaryotic 5' nucleases. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Both the H3TH domain and the helical arch/clamp region are involved in DNA binding. Studies suggest that a glycine-rich loop in the H3TH domain contacts the phosphate backbone of the template strand in the downstream DNA duplex. These nucleases have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors (Mg2+ or Mn2+) required for nuclease activity. The first metal binding site is composed entirely of Asp/Glu residues from the PIN domain, whereas, the second metal binding site is composed generally of two Asp residues from the PIN domain and one Asp residue from the H3TH domain. Together with the helical arch and network of amino acids interacting with metal binding ions, the H3TH region defines a positively charged active-site DNA-binding groove in structure-specific 5' nucleases
REKLIALALLCGCDYNPKGVPGVGKERALRLVNIVSSDEVLDRLRNWRATSDPSSPQELKKKDKNHCSNC
GHLGKKQEHIKSGCEDCDKALLDPGFPNEEIIEEFLSR
>gnl|CDD|188626 cd09906, H3TH_YEN1, H3TH domain of Yeast Endonuclease 1, a structure-specific, divalent-metal-ion dependent, 5' nuclease. Yeast Endonuclease 1 (YEN1): Holliday junction resolvase which promotes reciprocal exchange during mitotic recombination to maintain genome integrity in budding yeast. YEN1 is a member of the structure-specific, 5' nuclease family that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Members of this subgroup include the H3TH (helix-3-turn-helix) domains of YEN1 and other similar fungal 5' nucleases. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Both the H3TH domain and the helical arch/clamp region are involved in DNA binding. Studies suggest that a glycine-rich loop in the H3TH domain contacts the phosphate backbone of the template strand in the downstream DNA duplex. These nucleases have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors (Mg2+ or Mn2+) required for nuclease activity. The first metal binding site is composed entirely of Asp/Glu residues from the PIN domain, whereas, the second metal binding site is composed generally of two Asp residues from the PIN domain and one Asp residue from the H3TH domain. Together with the helical arch and network of amino acids interacting with metal binding ions, the H3TH region defines a positively charged active-site DNA-binding groove in structure-specific 5' nucleases
RGGMVLFALLSGGDYDTVGLPGCGKKTALELAKLGFGDSLLEAAEDLSEEELESFLEEWRERLLEELRTN
GRGLFGRNYPALSLSIPEGFPDPDVLLYYTHPVVS
>gnl|CDD|188627 cd09907, H3TH_FEN1-Euk, H3TH domain of Flap Endonuclease-1, a structure-specific, divalent-metal-ion dependent, 5' nuclease: Eukaryotic homologs. Members of this subgroup include the H3TH (helix-3-turn-helix) domains of eukaryotic Flap endonuclease-1 (FEN1), 5' nucleases. FEN1 is involved in multiple DNA metabolic pathways, including DNA replication processes (5' flap DNA endonuclease activity and double stranded DNA 5'-exonuclease activity) and DNA repair processes (long-patch base excision repair) in eukaryotes and archaea. Interaction between FEN1 and PCNA (Proliferating cell nuclear antigen) is an essential prerequisite to FEN1's DNA replication functionality and stimulates FEN1 nuclease activity by 10-50 fold. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Both the H3TH domain and the helical arch/clamp region are involved in DNA binding. Studies suggest that a glycine-rich loop in the H3TH domain contacts the phosphate backbone of the template strand in the downstream DNA duplex. The nucleases within this subfamily have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors (Mg2+ or Mn2+) required for nuclease activity. The first metal binding site is composed entirely of Asp/Glu residues from the PIN domain, whereas, the second metal binding site is composed generally of two Asp residues from the PIN domain and one Asp residue from the H3TH domain. Together with the helical arch and network of amino acids interacting with metal binding ions, the H3TH region defines a positively charged active-site DNA-binding groove in structure-specific 5' nucleases. Also, FEN1 has a C-terminal extension containing residues forming the consensus PIP-box - Qxx(M/L/I)xxF(Y/F) which serves to anchor FEN1 to PCNA
EQFIDLCILLGCDYCESIKGIGPKTALKLIKKHKSIEKILENIDKSKYPVPEDWPYKEARELFLNPEVTD
>gnl|CDD|188628 cd09908, H3TH_EXO1, H3TH domain of Exonuclease-1, a structure-specific, divalent-metal-ion dependent, 5' nuclease. Exonuclease-1 (EXO1) is involved in multiple, eukaryotic DNA metabolic pathways, including DNA replication processes (5' flap DNA endonuclease activity and double stranded DNA 5'-exonuclease activity), DNA repair processes (DNA mismatch repair (MMR) and post-replication repair (PRR), recombination, and telomere integrity. EXO1 functions in the MMS2 error-free branch of the PRR pathway in the maintenance and repair of stalled replication forks. Studies also suggest that EXO1 plays both structural and catalytic roles during MMR-mediated mutation avoidance. Members of this subgroup include the H3TH (helix-3-turn-helix) domains of EXO1 and other similar eukaryotic 5' nucleases. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Both the H3TH domain and the helical arch/clamp region are involved in DNA binding. Studies suggest that a glycine-rich loop in the H3TH domain contacts the phosphate backbone of the template strand in the downstream DNA duplex. These nucleases have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors (Mg2+ or Mn2+) required for nuclease activity. The first metal binding site is composed entirely of Asp/Glu residues from the PIN domain, whereas, the second metal binding site is composed generally of two Asp residues from the PIN domain and one Asp residue from the H3TH domain. Together with the helical arch and network of amino acids interacting with metal binding ions, the H3TH region defines a positively charged active-site DNA-binding groove in structure-specific 5' nucleases. EXO1 nucleases also have C-terminal Mlh1- and Msh2-binding domains which allow interaction with MMR and PRR proteins, respectively
EKFRHMCILSGCDYLPSLPGIGLKKAYKLVRRHRTIEKVIKALRFDGKKEVPPDYEEGFQKALLTFLHQR
VFD
>gnl|CDD|197369 cd09909, HIV-1-like_HR1-HR2, heptad repeat 1-heptad repeat 2 region (ectodomain) of the gp41 subunit of human immunodeficiency virus (HIV-1), and related domains. This domain family spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including human, simian, and feline immunodeficiency viruses (HIV, SIV, and FIV), bovine immunodeficiency-like virus (BIV), equine infectious anaemia virus (EIAV), and Jaagsiekte sheep retrovirus (JSRV), mouse mammary tumour virus (MMTV) and various ERVs including sheep enJSRV-26, and human ERVs (HERVs): HERV-K_c1q23.3 and HERV-K_c12q14.1. This domain belongs to a larger superfamily containing the HR1-HR2 domain of ERVs and infectious retroviruses, including Ebola virus, and Rous sarcoma virus. Proteins in this family lack the canonical CSK17-like immunosuppressive sequence, and the intrasubunit disulfide bond-forming CX6C motif found in linker region between HR1 and HR2 in the Ebola_RSV-like_HR1-HR2 family. N-terminal to the HR1-HR2 region is a fusion peptide (FP), and C-terminal is a membrane-spanning region (MSR). Viral infection involves the formation of a trimer-of-hairpins structure (three HR1 helices, buttressed by three HR2 helices lying in antiparallel orientation). In this structure, the FP (inserted in the host cell membrane) and MSR (inserted in the viral membrane) are in close proximity. ERVs are likely to originate from ancient germ-line infections by active retroviruses. Some modern ERVs, those that integrated into the host genome post-speciation, have a currently active exogenous counterpart, such as JSRV. Some ERVs play specific roles in the host, including placental development, protection of the host from infection by related pathogenic and exogenous retroviruses, and genome plasticity. Included in this subgroup are ERVs from domestic sheep that are related to JSRV, the agent of transmissible lung cancer in sheep, for example enJSRV-26 that retains an intact genome. These endogenous JSRVs protect the sheep against JSRV infection and are required for sheep placental development. HERV-K_c12q14.1 is potentially a complete envelope protein; however, it does not appear to be fusogenic
VQARQLLVTRVQQQQSLIDAIEKLEHLLNLLYWVVKQLGARVQALEFRLKIQCHLNLWGCVTKQPYCHTD
VPWNRSWNHLQGNDNWISLTWQEWENKIDDLEEKILNLLEEAQNQLEKLADGLLSLDP
>gnl|CDD|197364 cd09910, NGN-insert_like, NGN-insert domain found between N-terminal domain (D1) and C-terminal KOW domain (DIII) repeats of some N-Utilization Substance G (NusG) N-terminal (NGN). This family contains a unique insert (domain II, DII) found between the highly conserved N-terminal domain (NGN, domain I, D1) and C-terminal Kyrpides Ouzounis and Woese domain (KOW, domain III, DIII) repeats of some N-Utilization Substance G (NusG) N-terminal (NGN) proteins in bacteria such as Aquifex aeolicus NusG (AaeNusG). NusG was originally discovered as having an N-dependent antitermination enhancing activity in Escherichia coli, and has since been shown to have a variety of functions such as being involved in RNA polymerase elongation and Rho-termination. Orthologs of NusG gene exist in bacteria, but their functions and requirements are diverse. The function of DII is as yet unknown, and belongs to Domains of Unknown Function 1312 (DUF1312)
DYVVIRAGGKVIYELDLSQDRTIEVEGPLGPTTIEIKDGKARVVSSPCPNKYCVRQGWISRAGQWIVCLP
NQVSVEIEGR
>gnl|CDD|197365 cd09911, Lin0431_like, Listerrria innocua Lin0431 is similar to the N-Utilization Substance G (NusG) N terminal (NGN) insert (DII). This family contains domains homologous to Listeria innocua Lin0431, a protein that is similar to the N-Utilization Substance G (NusG) N terminal (NGN) insert (domain II, DII). Lin0431 and Aquifex aeolicus NusG DII (AaeNusG DII) have similar structure and similar basic charged surface distributions that may bind negatively charged nucleic acids and/or another anionic binding partner, suggesting a possible role in transcription/translation regulating functions. Despite these two domains having low sequence similarity, the NusG DII and DUF1312 domain families may have diverged from common evolutionary ancestral proteins, and may have similar biochemical functions
KYAVITVDGKVYKTYPLDEKDETITIKTGGGYNIIEIKDGKVRMIEADCPDQICVKTGAISKPGQTIVCL
PHKLVIEIEGGE
>gnl|CDD|206739 cd09912, DLP_2, Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins. The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner
FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAVITVLRYGLLKGVVLVDTPGLNSTIEHHTEITESF
LPRADAVIFVLSADQPLTESEREFLKEILKWSGKKIFFVLNKIDLLSEEELEEVLEYSREELGVLELGGG
EPRIFPVSAKEALEARLQGDEELLEQSGFEELEEHLEEFL
>gnl|CDD|206740 cd09913, EHD, Eps15 homology domain (EHD), C-terminal domain. Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling
MVLFLGQYSTGKSTFINYLLGQDYPGLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFG
NGFLNKFEGSTLPHPLLESVTIVDTPGILSGEKQRQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDE
FRRVIEQLKGHESKIRIVLNKADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRK
LFLEEEIDLLRDLNSLPRNAALRKLNDLIKR
>gnl|CDD|206741 cd09914, RocCOR, Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family. RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease
EAKLMLVGQGGVGKTSLCKQLIGEKFDGDESSTHGINVQDWKIPAPERKKIRLNVWDFGGQEIYHATHQF
FLTSRSLYLLVFDLRTGDEVSRVPYWLRQIKAFGGVSPVILVGTHIDESCDEDILKKALNKKFPAIINDI
HFVSCKNGKGIAELKKAIAKE
>gnl|CDD|206742 cd09915, Rag, Rag GTPase subfamily of Ras-related GTPases. Rag GTPases (ras-related GTP-binding proteins) constitute a unique subgroup of the Ras superfamily, playing an essential role in regulating amino acid-induced target of rapamycin complex 1 (TORC1) kinase signaling, exocytic cargo sorting at endosomes, and epigenetic control of gene expression. This subfamily consists of RagA and RagB as well as RagC and RagD that are closely related. Saccharomyces cerevisiae encodes single orthologs of metazoan RagA/B and RagC/D, Gtr1 and Gtr2, respectively. Dimer formation is important for their cellular function; these domains form heterodimers, as RagA or RagB dimerizes with RagC or RagD, and similarly, Gtr1 dimerizes with Gtr2. In response to amino acids, the Rag GTPases guide the TORC1 complex to activate the platform containing Rheb proto-oncogene by driving the relocalization of mTORC1 from discrete locations in the cytoplasm to a late endosomal and/or lysosomal compartment that is Rheb-enriched and contains Rab-7
KLLLXGRRRSGKSSIRKVVFHNYSPFDTLRLESTIDVEHSHLSFLGNXTLNLWDCPGQDVFFEPTKDKEH
IFQXVGALIYVIDVQDEYLKAITILAKALKQAYKVNPDANIEVLIHKVDGLSLDKKEELQRDIXQRLSET
LSEFGLEFPNLSFYLTSIWDHSIYEAFSQIVQKLI
>gnl|CDD|197366 cd09916, CpxP_like, CpxP component of the bacterial Cpx-two-component system and related proteins. This family summarizes bacterial proteins related to CpxP, a periplasmic protein that forms part of a two-component system which acts as a global modulator of cell-envelope stress in gram-negative bacteria. CpxP aids in combating extracytoplasmic protein-mediated toxicity, and may also be involved in the response to alkaline pH. Functioning as a dimer, it inhibits activation of the kinase CpxA, but also plays a vital role in the quality control system of P pili. It has been suggested that CpxP directly interacts with CpxA via its concave polar surface. Another member of this family, Spy, is also a periplasmic protein that may be involved in the response to stress. The homology between CpxP and Spy suggests similar functions. A characteristic 5-residue sequence motif LTXXQ is found repeated twice in many members of this family
GLDLTDEQKAQIKAIRQAARAQMKALREQMRAAREELRALLTADTFDEAAVRALAAEMAELQQELAVERA
KARNQIYQVLTPEQRAKLNELFAKRR
>gnl|CDD|438852 cd09917, F-box_SF, F-box domain superfamily. This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures
SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS
>gnl|CDD|198174 cd09918, SH2_Nterm_SPT6_like, N-terminal Src homology 2 (SH2) domain found in Spt6. N-terminal SH2 domain in Spt6. Spt6 is an essential transcription elongation factor and histone chaperone that binds the C-terminal repeat domain (CTD) of RNA polymerase II. Spt6 contains a tandem SH2 domain with a novel structure and CTD-binding mode. The tandem SH2 domain binds to a serine 2-phosphorylated CTD peptide in vitro, whereas its N-terminal SH2 subdomain does not. CTD binding requires a positively charged crevice in the C-terminal SH2 subdomain, which lacks the canonical phospho-binding pocket of SH2 domains. The tandem SH2 domain is apparently required for transcription elongation in vivo as its deletion in cells is lethal in the presence of 6-azauracil. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
RHPLFKNVNYKQAEAYLKSKDVGEVVIRPSSKGVDHLTVTWKVADGVYQHIDIEELNKENPFSLGKELII
GGEEYEDLDEIIARF
>gnl|CDD|198175 cd09919, SH2_STAT_family, Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) family. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated by a receptor. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. The CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
WFFAIMLLTKRHLLKLWQDGLIMGFISKEEAEDLLKKKPPGTFLLRFSDSELGGITIAWVNEDPDGQSQV
IHLQPYTKKDLDIRSLADRIRDLPQLVYLYPDIPKDEAFGKYYSP
>gnl|CDD|198176 cd09920, SH2_Cbl-b_TKB, Src homology 2 (SH2) domain found in the Cbl-b TKB domain. SH2 found in the Cbl-b TKB domain. The Cbl (for Casitas B-lineage lymphoma) family of E3 ubiquitin ligases contains three members Cbl, Cbl-b and Cbl-c. The founding member Cbl was discovered first as the oncogenic protein v-Cbl, a Gag-fusion transforming protein of Cas NS-1 retrovirus, which causes pre- and pro-B lymphomas in mice. The N-terminus of the Cbl proteins is composed of a tyrosine kinase-binding (TKB) domain, also called phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. In addition, Cbl and Cbl-b contain a leucine zipper motif and a proline-rich domain in the C-terminus. The TKB domain consists of a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain. Cbl-b plays a role in early hematopoietic development and is a negative regulator of T-cell receptor, B-cell receptor and high affinity immunoglobulin epsilon receptor signal transduction pathways. It also negatively regulates insulin-like growth factor 1 signaling during muscle atrophy caused by unloading and is involved in EGFR ubiquitination and internalization. Diseases associated with defects in Cbl-b include: multiple sclerosis, autoimmune diseases, including type 1 diabetes, and a craniofacial phenotype. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
RNWQVLAVTHPGYMAFLTYDEVKARLQKFRDKPGSYVFRLSCTRLGQWAIGYVTADGKILQTIPQNKSLC
QALIDGSREGFYLYPDGRLDNPDLSGA
>gnl|CDD|198177 cd09921, SH2_Jak_family, Src homology 2 (SH2) domain in the Janus kinase (Jak) family. The Janus kinases (Jak) are a family of 4 non-receptor tyrosine kinases (Jak1, Jak2, Jak3, Tyk2) which respond to cytokine or growth factor receptor activation. To transduce cytokine signaling, a series of conformational changes occur in the receptor-Jak complex upon extracellular ligand binding. This results in trans-activation of the receptor-associated Jaks followed by phosphorylation of receptor tail tyrosine sites. The Signal Transducers and Activators of Transcription (STAT) are then recruited to the receptor tail, become phosphorylated and translocate to the nucleus to regulate transcription. Jaks have four domains: the pseudokinase domain, the catalytic tyrosine kinase domain, the FERM (band four-point-one, ezrin, radixin, and moesin) domain, and the SH2 (Src Homology-2) domain. The Jak kinases are regulated by several enzymatic and non-enzymatic mechanisms. First, the Jak kinase domain is regulated by phosphorylation of the activation loop which is associated with the catalytically competent kinase conformation and is distinct from the inactive kinase conformation. Second, the pseudokinase domain directly modulates Jak catalytic activity with the FERM domain maintaining an active state. Third, the suppressor of cytokine signaling (SOCS) family and tyrosine phosphatases directly regulate Jak activity. Dysregulation of Jak activity can manifest as either a reduction or an increase in kinase activity resulting in immunodeficiency, inflammatory diseases, hematological defects, autoimmune and myeloproliferative disorders, and susceptibility to infection. Altered Jak regulation occurs by many mechanisms, including: gene translocations, somatic or inherited point mutations, receptor mutations, and alterations in the activity of Jak regulators such as SOCS or phosphatases. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
DVATPSLVELIELRCHGPIGGEFSYRKLKERGNKPGSYILRESETEYDTYYIDVCVKDGSRFQTKTFKIE
KKEGGVFFLDGDSREYPSLRDLLNSLQ
>gnl|CDD|198178 cd09923, SH2_SOCS_family, Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) family. SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
GWYWGGITRYEAEELLAGKPEGTFLVRDSSDSRYLFSVSFRTYGRTLHARIEYSNGRFSFDSSDPSVPRF
PCVVELIEHYV
>gnl|CDD|198179 cd09925, SH2_SHC, Src homology 2 (SH2) domain found in SH2 adaptor protein C (SHC). SHC is involved in a wide variety of pathways including regulating proliferation, angiogenesis, invasion and metastasis, and bone metabolism. An adapter protein, SHC has been implicated in Ras activation following the stimulation of a number of different receptors, including growth factors [insulin, epidermal growth factor (EGF), nerve growth factor, and platelet derived growth factor (PDGF)], cytokines [interleukins 2, 3, and 5], erythropoietin, and granulocyte/macrophage colony-stimulating factor, and antigens [T-cell and B-cell receptors]. SHC has been shown to bind to tyrosine-phosphorylated receptors, and receptor stimulation leads to tyrosine phosphorylation of SHC. Upon phosphorylation, SHC interacts with another adapter protein, Grb2, which binds to the Ras GTP/GDP exchange factor mSOS which leads to Ras activation. SHC is composed of an N-terminal domain that interacts with proteins containing phosphorylated tyrosines, a (glycine/proline)-rich collagen-homology domain that contains the phosphorylated binding site, and a C-terminal SH2 domain. SH2 has been shown to interact with the tyrosine-phosphorylated receptors of EGF and PDGF and with the tyrosine-phosphorylated C chain of the T-cell receptor, providing one of the mechanisms of T-cell-mediated Ras activation. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
AEQLRGEPWYHGKMSRRDAESLLQTDGDFLVRESTTTPGQYVLTGMQNGQPKHLLLVDPEGVVRTKDRVF
ESISHLINYHVTNGLPIISEGSELHLRRPVRRPA
>gnl|CDD|198180 cd09926, SH2_CRK_like, Src homology 2 domain found in cancer-related signaling adaptor protein CRK. SH2 domain in the CRK proteins. CRKI (SH2-SH3) and CRKII (SH2-SH3-SH3) are splicing isoforms of the oncoprotein CRK. CRKs regulate transcription and cytoskeletal reorganization for cell growth and motility by linking tyrosine kinases to small G proteins. The SH2 domain of CRK associates with tyrosine-phosphorylated receptors or components of focal adhesions, such as p130Cas and paxillin. CRK transmits signals to small G proteins through effectors that bind its SH3 domain, such as C3G, the guanine-nucleotide exchange factor (GEF) for Rap1 and R-Ras, and DOCK180, the GEF for Rac6. The binding of p130Cas to the CRK-C3G complex activates Rap1, leading to regulation of cell adhesion, and activates R-Ras, leading to JNK-mediated activation of cell proliferation, whereas the binding of CRK DOCK180 induces Rac1-mediated activation of cellular migration. The activity of the different splicing isoforms varies greatly with CRKI displaying substantial transforming activity, CRKII less so, and phosphorylated CRKII with no biological activity whatsoever. CRKII has a linker region with a phosphorylated Tyr and an additional C-terminal SH3 domain. The phosphorylated Tyr creates a binding site for its SH2 domain which disrupts the association between CRK and its SH2 target proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
FDSSDRSSWYFGPMSRQEAQELLQGQRHGVFLVRDSSTIPGDYVLSVSENSRVSHYIINSLGQPAPNQSR
YRIGDQEFDDLPALLEFYKLHYLDTTTLIEPASRGR
>gnl|CDD|198181 cd09927, SH2_Tensin_like, Src homology 2 domain found in Tensin-like proteins. SH2 domain found in Tensin-like proteins. The Tensins are a family of intracellular proteins that interact with receptor tyrosine kinases (RTKs), integrins, and actin. They are thought act as signaling bridges between the extracellular space and the cytoskeleton. There are four homologues: Tensin1, Tensin2 (TENC1, C1-TEN), Tensin3 and Tensin4 (cten), all of which contain a C-terminal tandem SH2-PTB domain pairing, as well as actin-binding regions that may localize them to focal adhesions. The isoforms of Tensin2 and Tensin3 contain N-terminal C1 domains, which are atypical and not expected to bind to phorbol esters. Tensins 1-3 contain a phosphatase (PTPase) and C2 domain pairing which resembles PTEN (phosphatase and tensin homologue deleted on chromosome 10) protein. PTEN is a lipid phosphatase that dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to yield phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). As PtdIns(3,4,5)P3 is the product of phosphatidylinositol 3-kinase (PI3K) activity, PTEN is therefore a key negative regulator of the PI3K pathway. Because of their PTEN-like domains, the Tensins may also possess phosphoinositide-binding or phosphatase capabilities. However, only Tensin2 and Tensin3 have the potential to be phosphatases since only their PTPase domains contain a cysteine residue that is essential for catalytic activity. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
TSKYWYKPNISRDQAIALLKDKPPGTFLVRDSTTYKGAYGLAVKVATPPPGVNPFEAKGDPESELVRHFL
IEPSPKGVKLKGCPNEPVFGSLSALVYQHSITPLALPCKLRIPDRD
>gnl|CDD|198182 cd09928, SH2_Cterm_SPT6_like, C-terminal Src homology 2 (SH2) domain found in Spt6. Spt6 is an essential transcription elongation factor and histone chaperone that binds the C-terminal repeat domain (CTD) of RNA polymerase II. Spt6 contains a tandem SH2 domain with a novel structure and CTD-binding mode. The tandem SH2 domain binds to a serine 2-phosphorylated CTD peptide in vitro, whereas its N-terminal SH2 subdomain does not. CTD binding requires a positively charged crevice in the C-terminal SH2 subdomain, which lacks the canonical phospho-binding pocket of SH2 domains. The tandem SH2 domain is apparently required for transcription elongation in vivo as its deletion in cells is lethal in the presence of 6-azauracil. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
EMLNHHKYFRGTKEEVEKLLKEEKKANPKRIPYAFCVSKKYPGKFLLSYLPANTRVRHEYVKVTPDGFRF
RGQVFPSVDSLLNWFKEHF
>gnl|CDD|198183 cd09929, SH2_BLNK_SLP-76, Src homology 2 (SH2) domain found in B-cell linker (BLNK) protein and SH2 domain-containing leukocyte protein of 76 kDa (SLP-76). BLNK (also known as SLP-65 or BASH) is an important adaptor protein expressed in B-lineage cells. BLNK consists of a N-terminal sterile alpha motif (SAM) domain and a C-terminal SH2 domain. BLNK is a cytoplasmic protein, but a part of it is bound to the plasma membrane through an N-terminal leucine zipper motif and transiently bound to a cytoplasmic domain of Iga through its C-terminal SH2 domain upon B cell antigen receptor (BCR)-stimulation. A non-ITAM phosphotyrosine in Iga is necessary for the binding with the BLNK SH2 domain and/or for normal BLNK function in signaling and B cell activation. Upon phosphorylation BLNK binds Btk and PLCgamma2 through their SH2 domains and mediates PLCgamma2 activation by Btk. BLNK also binds other signaling molecules such as Vav, Grb2, Syk, and HPK1. BLNK has been shown to be necessary for BCR-mediated Ca2+ mobilization, for the activation of mitogen-activated protein kinases such as ERK, JNK, and p38 in a chicken B cell line DT40, and for activation of transcription factors such as NF-AT and NF-kappaB in human or mouse B cells. BLNK is involved in B cell development, B cell survival, activation, proliferation, and T-independent immune responses. BLNK is structurally homologous to SLP-76. SLP-76 and (linker for activation of T cells) LAT are adaptor/linker proteins in T cell antigen receptor activation and T cell development. BLNK interacts with many downstream signaling proteins that interact directly with both SLP-76 and LAT. New data suggest functional complementation of SLP-76 and LAT in T cell antigen receptor function with BLNK in BCR function. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
SAEEEADLLPKEWYAGNIDRKEAEEALRRSNKDGTFLVRDSSGKDSSQPYTLMVLYNDKVYNIQIRFLEN
TRQYALGTGLRGEETFSSVAEIIEHHQKTPLLLIDGKDNTKDSTCLLYAAG
>gnl|CDD|198184 cd09930, SH2_cSH2_p85_like, C-terminal Src homology 2 (cSH2) domain found in p85. Phosphoinositide 3-kinases (PI3Ks) are essential for cell growth, migration, and survival. p110, the catalytic subunit, is composed of an adaptor-binding domain, a Ras-binding domain, a C2 domain, a helical domain, and a kinase domain. The regulatory unit is called p85 and is composed of an SH3 domain, a RhoGap domain, a N-terminal SH2 (nSH2) domain, a inter SH2 (iSH2) domain, and C-terminal (cSH2) domain. There are 2 inhibitory interactions between p110alpha and p85 of P13K: 1) p85 nSH2 domain with the C2, helical, and kinase domains of p110alpha and 2) p85 iSH2 domain with C2 domain of p110alpha. There are 3 inhibitory interactions between p110beta and p85 of P13K: 1) p85 nSH2 domain with the C2, helical, and kinase domains of p110beta, 2) p85 iSH2 domain with C2 domain of p110alpha, and 3) p85 cSH2 domain with the kinase domain of p110alpha. It is interesting to note that p110beta is oncogenic as a wild type protein while p110alpha lacks this ability. One explanation is the idea that the regulation of p110beta by p85 is unique because of the addition of inhibitory contacts from the cSH2 domain and the loss of contacts in the iSH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
PHHDERTWLVGDINRTQAEELLRGKPDGTFLIRESSTQGCYACSVVCNGEVKHCVIYKTETGYGFAEPYN
LYESLKELVLHYAHNSLEQHNDSLTVTLAYPVLA
>gnl|CDD|198185 cd09931, SH2_C-SH2_SHP_like, C-terminal Src homology 2 (C-SH2) domain found in SH2 domain Phosphatases (SHP) proteins. The SH2 domain phosphatases (SHP-1, SHP-2/Syp, Drosophila corkscrew (csw), and Caenorhabditis elegans Protein Tyrosine Phosphatase (Ptp-2)) are cytoplasmic signaling enzymes. They are both targeted and regulated by interactions of their SH2 domains with phosphotyrosine docking sites. These proteins contain two SH2 domains (N-SH2, C-SH2) followed by a tyrosine phosphatase (PTP) domain, and a C-terminal extension. Shp1 and Shp2 have two tyrosyl phosphorylation sites in their C-tails, which are phosphorylated differentially by receptor and nonreceptor PTKs. Csw retains the proximal tyrosine and Ptp-2 lacks both sites. Shp-binding proteins include receptors, scaffolding adapters, and inhibitory receptors. Some of these bind both Shp1 and Shp2 while others bind only one. Most proteins that bind a Shp SH2 domain contain one or more immuno-receptor tyrosine-based inhibitory motifs (ITIMs): [SIVL]xpYxx[IVL]. Shp1 N-SH2 domain blocks the catalytic domain and keeps the enzyme in the inactive conformation, and is thus believed to regulate the phosphatase activity of SHP-1. Its C-SH2 domain is thought to be involved in searching for phosphotyrosine activators. The SHP2 N-SH2 domain is a conformational switch; it either binds and inhibits the phosphatase, or it binds phosphoproteins and activates the enzyme. The C-SH2 domain contributes binding energy and specificity, but it does not have a direct role in activation. Csw SH2 domain function is essential, but either SH2 domain can fulfill this requirement. The role of the csw SH2 domains during Sevenless receptor tyrosine kinase (SEV) signaling is to bind Daughter of Sevenless rather than activated SEV. Ptp-2 acts in oocytes downstream of sheath/oocyte gap junctions to promote major sperm protein (MSP)-induced MAP Kinase (MPK-1) phosphorylation. Ptp-2 functions in the oocyte cytoplasm, not at the cell surface to inhibit multiple RasGAPs, resulting in sustained Ras activation. It is thought that MSP triggers PTP-2/Ras activation and ROS production to stimulate MPK-1 activity essential for oocyte maturation and that secreted MSP domains and Cu/Zn superoxide dismutases function antagonistically to control ROS and MAPK signaling. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
RWFHGHLSGKEAEKLLLEKGKPGSFLVRESQSKPGDFVLSVRTDDDKVTHIMIRCQGGKYDVGGGEEFDS
LTDLVEHYKKNPMVETSGTVVHLKQPLNA
>gnl|CDD|198186 cd09932, SH2_C-SH2_PLC_gamma_like, C-terminal Src homology 2 (C-SH2) domain in Phospholipase C gamma. Phospholipase C gamma is a signaling molecule that is recruited to the C-terminal tail of the receptor upon autophosphorylation of a highly conserved tyrosine. PLCgamma is composed of a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, 2 catalytic regions of PLC domains that flank 2 tandem SH2 domains (N-SH2, C-SH2), and ending with a SH3 domain and C2 domain. N-SH2 SH2 domain-mediated interactions represent a crucial step in transmembrane signaling by receptor tyrosine kinases. SH2 domains recognize phosphotyrosine (pY) in the context of particular sequence motifs in receptor phosphorylation sites. Both N-SH2 and C-SH2 have a very similar binding affinity to pY. But in growth factor stimulated cells these domains bind to different target proteins. N-SH2 binds to pY containing sites in the C-terminal tails of tyrosine kinases and other receptors. Recently it has been shown that this interaction is mediated by phosphorylation-independent interactions between a secondary binding site found exclusively on the N-SH2 domain and a region of the FGFR1 tyrosine kinase domain. This secondary site on the SH2 cooperates with the canonical pY site to regulate selectivity in mediating a specific cellular process. C-SH2 binds to an intramolecular site on PLCgamma itself which allows it to hydrolyze phosphatidylinositol-4,5-bisphosphate into diacylglycerol and inositol triphosphate. These then activate protein kinase C and release calcium. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
HESKEWFHANLTREQAEEMLMRVPRDGAFLVRPSETDPNSFAISFRAEGKIKHCRIKQEGRLFVIGTSQF
ESLVELVSYYEKHPLYRKIKLRYPVNEELLEKYG
>gnl|CDD|199827 cd09933, SH2_Src_family, Src homology 2 (SH2) domain found in the Src family of non-receptor tyrosine kinases. The Src family kinases are nonreceptor tyrosine kinases that have been implicated in pathways regulating proliferation, angiogenesis, invasion and metastasis, and bone metabolism. It is thought that transforming ability of Src is linked to its ability to activate key signaling molecules in these pathways, rather than through direct activity. As such blocking Src activation has been a target for drug companies. Src family members can be divided into 3 groups based on their expression pattern: 1) Src, Fyn, and Yes; 2) Blk, Fgr, Hck, Lck, and Lyn; and 3) Frk-related kinases Frk/Rak and Iyk/Bsk Of these, cellular c-Src is the best studied and most frequently implicated in oncogenesis. The c-Src contains five distinct regions: a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. Src exists in both active and inactive conformations. Negative regulation occurs through phosphorylation of Tyr, resulting in an intramolecular association between phosphorylated Tyr and the SH2 domain of SRC, which locks the protein in a closed conformation. Further stabilization of the inactive state occurs through interactions between the SH3 domain and a proline-rich stretch of residues within the kinase domain. Conversely, dephosphorylation of Tyr allows SRC to assume an open conformation. Full activity requires additional autophosphorylation of a Tyr residue within the catalytic domain. Loss of the negative-regulatory C-terminal segment has been shown to result in increased activity and transforming potential. Phosphorylation of the C-terminal Tyr residue by C-terminal Src kinase (Csk) and Csk homology kinase results in increased intramolecular interactions and consequent Src inactivation. Specific phosphatases, protein tyrosine phosphatase a (PTPa) and the SH-containing phosphatases SHP1/SHP2, have also been shown to take a part in Src activation. Src is also activated by direct binding of focal adhesion kinase (Fak) and Crk-associated substrate (Cas) to the SH2 domain. SRC activity can also be regulated by numerous receptor tyrosine kinases (RTKs), such as Her2, epidermal growth factor receptor (EGFR), fibroblast growth factor receptor, platelet-derived growth factor receptor (PDGFR), and vascular endothelial growth factor receptor (VEGFR). In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
EAEEWFFGKIKRKDAEKLLLAPGNPRGTFLIRESETTPGAYSLSVRDGDDARGDTVKHYRIRKLDNGGYY
ITTRATFPTLQELVQHYSKDADGLCCRLTVP
>gnl|CDD|198188 cd09934, SH2_Tec_family, Src homology 2 (SH2) domain found in Tec-like proteins. The Tec protein tyrosine kinase is the founding member of a family that includes Btk, Itk, Bmx, and Txk. The members have a PH domain, a zinc-binding motif, a SH3 domain, a SH2 domain, and a protein kinase catalytic domain. Btk is involved in B-cell receptor signaling with mutations in Btk responsible for X-linked agammaglobulinemia (XLA) in humans and X-linked immunodeficiency (xid) in mice. Itk is involved in T-cell receptor signaling. Tec is expressed in both T and B cells, and is thought to function in activated and effector T lymphocytes to induce the expression of genes regulated by NFAT transcription factors. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
LNLEKYEWYVGDMSRQRAESLLKQEDKEGCFVVRNSSTKGLYTVSLFTKVPGSPHVKHYHIKQNARSEFY
LAEKHCFETIPELINYHQHNSGGLATRLKYPVCD
>gnl|CDD|198189 cd09935, SH2_ABL, Src homology 2 (SH2) domain found in Abelson murine lymphosarcoma virus (ABL) proteins. ABL-family proteins are highly conserved tyrosine kinases. Each ABL protein contains an SH3-SH2-TK (Src homology 3-Src homology 2-tyrosine kinase) domain cassette, which confers autoregulated kinase activity and is common among nonreceptor tyrosine kinases. Several types of posttranslational modifications control ABL catalytic activity, subcellular localization, and stability, with consequences for both cytoplasmic and nuclear ABL functions. Binding partners provide additional regulation of ABL catalytic activity, substrate specificity, and downstream signaling. By combining this cassette with actin-binding and -bundling domain, ABL proteins are capable of connecting phosphoregulation with actin-filament reorganization. Vertebrate paralogs, ABL1 and ABL2, have evolved to perform specialized functions. ABL1 includes nuclear localization signals and a DNA binding domain which is used to mediate DNA damage-repair functions, while ABL2 has additional binding capacity for actin and for microtubules to enhance its cytoskeletal remodeling functions. SH2 is involved in several autoinhibitory mechanism that constrain the enzymatic activity of the ABL-family kinases. In one mechanism SH2 and SH3 cradle the kinase domain while a cap sequence stabilizes the inactive conformation resulting in a locked inactive state. Another involves phosphatidylinositol 4,5-bisphosphate (PIP2) which binds the SH2 domain through residues normally required for phosphotyrosine binding in the linker segment between the SH2 and kinase domains. The SH2 domain contributes to ABL catalytic activity and target site specificity. It is thought that the ABL catalytic site and SH2 pocket have coevolved to recognize the same sequences. Recent work now supports a hierarchical processivity model in which the substrate target site most compatible with ABL kinase domain preferences is phosphorylated with greatest efficiency. If this site is compatible with the ABL SH2 domain specificity, it will then reposition and dock in the SH2 pocket. This mechanism also explains how ABL kinases phosphorylates poor targets on the same substrate if they are properly positioned and how relatively poor substrate proteins might be recruited to ABL through a complex with strong substrates that can also dock with the SH2 pocket. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
EKHSWYHGPISRNAAEYLLSSGINGSFLVRESESSPGQYSISLRYDGRVYHYRISEDSDGKVYVTQEHRF
NTLAELVHHHSKNADGLITTLRYP
>gnl|CDD|198190 cd09937, SH2_csk_like, Src homology 2 (SH2) domain found in Carboxyl-Terminal Src Kinase (Csk). Both the C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK) are members of the CSK-family of protein tyrosine kinases. These proteins suppress activity of Src-family kinases (SFK) by selectively phosphorylating the conserved C-terminal tail regulatory tyrosine by a similar mechanism. CHK is also capable of inhibiting SFKs by a non-catalytic mechanism that involves binding of CHK to SFKs to form stable protein complexes. The unphosphorylated form of SFKs is inhibited by CSK and CHK by a two-step mechanism. The first step involves the formation of a complex of SFKs with CSK/CHK with the SFKs in the complex are inactive. The second step, involves the phosphorylation of the C-terminal tail tyrosine of SFKs, which then dissociates and adopt an inactive conformation. The structural basis of how the phosphorylated SFKs dissociate from CSK/CHK to adopt the inactive conformation is not known. The inactive conformation of SFKs is stabilized by two intramolecular inhibitory interactions: (a) the pYT:SH2 interaction in which the phosphorylated C-terminal tail tyrosine (YT) binds to the SH2 domain, and (b) the linker:SH3 interaction of which the SH2-kinase domain linker binds to the SH3 domain. SFKs are activated by multiple mechanisms including binding of the ligands to the SH2 and SH3 domains to displace the two inhibitory intramolecular interactions, autophosphorylation, and dephosphorylation of YT. By selective phosphorylation and the non-catalytic inhibitory mechanism CSK and CHK are able to inhibit the active forms of SFKs. CSK and CHK are regulated by phosphorylation and inter-domain interactions. They both contain SH3, SH2, and kinase domains separated by the SH3-SH2 connector and SH2 kinase linker, intervening segments separating the three domains. They lack a conserved tyrosine phosphorylation site in the kinase domain and the C-terminal tail regulatory tyrosine phosphorylation site. The CSK SH2 domain is crucial for stabilizing the kinase domain in the active conformation. A disulfide bond here regulates CSK kinase activity. The subcellular localization and activity of CSK are regulated by its SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
SLMPWFHGKISREEAERLLQPPEDGLFLVRESTNYPGDYTLCVSFEGKVEHYRVIYRNGKLTIDEEEYFE
NLIQLVEHYTKDADGLCTRLVKPKVKEG
>gnl|CDD|198191 cd09938, SH2_N-SH2_Zap70_Syk_like, N-terminal Src homology 2 (SH2) domain found in Zeta-chain-associated protein kinase 70 (ZAP-70) and Spleen tyrosine kinase (Syk) proteins. ZAP-70 and Syk comprise a family of hematopoietic cell specific protein tyrosine kinases (PTKs) that are required for antigen and antibody receptor function. ZAP-70 is expressed in T and natural killer (NK) cells and Syk is expressed in B cells, mast cells, polymorphonuclear leukocytes, platelets, macrophages, and immature T cells. They are required for the proper development of T and B cells, immune receptors, and activating NK cells. They consist of two N-terminal Src homology 2 (SH2) domains and a C-terminal kinase domain separated from the SH2 domains by a linker or hinge region. Phosphorylation of both tyrosine residues within the Immunoreceptor Tyrosine-based Activation Motifs (ITAM; consensus sequence Yxx[LI]x(7,8)Yxx[LI]) by the Src-family PTKs is required for efficient interaction of ZAP-70 and Syk with the receptor subunits and for receptor function. ZAP-70 forms two phosphotyrosine binding pockets, one of which is shared by both SH2 domains. In Syk the two SH2 domains do not form such a phosphotyrosine-binding site. The SH2 domains here are believed to function independently. In addition, the two SH2 domains of Syk display flexibility in their relative orientation, allowing Syk to accommodate a greater variety of spacing sequences between the ITAM phosphotyrosines and singly phosphorylated non-classical ITAM ligands. This model contains the N-terminus SH2 domains of both Syk and Zap70. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
LPFFYGSITREEAEEYLKLAGMSDGLFLLRQSLRSLGGYVLSVCHGRKFHHYTIERQLNGTYAIAGGKAH
CGPAELCEYHSTDLDGLVCLLRKPCNRPPGVEPK
>gnl|CDD|198192 cd09939, SH2_STAP_family, Src homology 2 domain found in Signal-transducing adaptor protein (STAP) family. STAP1 and STAP2 are signal-transducing adaptor proteins. They are composed of a Pleckstrin homology (PH) and SH2 domains along with several tyrosine phosphorylation sites. STAP-1 is an ortholog of BRDG1 (BCR downstream signaling 1). STAP1 protein functions as a docking protein acting downstream of Tec tyrosine kinase in B cell antigen receptor signaling. The protein is phosphorylated by Tec and participates in a positive feedback loop, increasing Tec activity. STAP1 has been shown to interact with C19orf2, an unconventional prefoldin RPB5 interactor. The STAP2 protein is the substrate of breast tumor kinase, an Src-type non-receptor tyrosine kinase that mediates the interactions linking proteins involved in signal transduction pathways. STAP2 has alternative splicing variants. STAP2 has been shown to interact with tyrosine-protein kinase 6 (PTK6). In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
PACFYTVSRKEATELLERNPSCGNMLLRPGSDSRNYSVTTRQEINIPVIRHYKVMSVGQNYTIELEKPVT
CPNLFSVINYFVKETRGNLRPFIL
>gnl|CDD|198193 cd09940, SH2_Vav_family, Src homology 2 (SH2) domain found in the Vav family. Vav proteins are involved in several processes that require cytoskeletal reorganization, such as the formation of the immunological synapse (IS), phagocytosis, platelet aggregation, spreading, and transformation. Vavs function as guanine nucleotide exchange factors (GEFs) for the Rho/Rac family of GTPases. Vav family members have several conserved motifs/domains including: a leucine-rich region, a leucine-zipper, a calponin homology (CH) domain, an acidic domain, a Dbl-homology (DH) domain, a pleckstrin homology (PH) domain, a cysteine-rich domain, 2 SH3 domains, a proline-rich region, and a SH2 domain. Vavs are the only known Rho GEFs that have both the DH/PH motifs and SH2/SH3 domains in the same protein. The leucine-rich helix-loop-helix (HLH) domain is thought to be involved in protein heterodimerization with other HLH proteins and it may function as a negative regulator by forming inactive heterodimers. The CH domain is usually involved in the association with filamentous actin, but in Vav it controls NFAT stimulation, Ca2+ mobilization, and its transforming activity. Acidic domains are involved in protein-protein interactions and contain regulatory tyrosines. The DH domain is a GDP-GTP exchange factor on Rho/Rac GTPases. The PH domain in involved in interactions with GTP-binding proteins, lipids and/or phosphorylated serine/threonine residues. The SH3 domain is involved in localization of proteins to specific sites within the cell interacting with protein with proline-rich sequences. The SH2 domain mediates a high affinity interaction with tyrosine phosphorylated proteins. There are three Vav mammalian family members: Vav1 which is expressed in the hematopoietic system, Vav2 and Vav3 are more ubiquitously expressed. The members here include insect and amphibian Vavs. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
DLSEFLWFVGEMERDTAENRLENRPDGTYLVRVRPQGETQYALSIKYNGDVKHMKIEQRSDGLYYLSESR
HFKSLVELVNYYERNSLGENFAGLDTTLKWPY
>gnl|CDD|199828 cd09941, SH2_Grb2_like, Src homology 2 domain found in Growth factor receptor-bound protein 2 (Grb2) and similar proteins. The adaptor proteins here include homologs Grb2 in humans, Sex muscle abnormal protein 5 (Sem-5) in Caenorhabditis elegans, and Downstream of receptor kinase (drk) in Drosophila melanogaster. They are composed of one SH2 and two SH3 domains. Grb2/Sem-5/drk regulates the Ras pathway by linking the tyrosine kinases to the Ras guanine nucleotide releasing protein Sos, which converts Ras to the active GTP-bound state. The SH2 domain of Grb2/Sem-5/drk binds class II phosphotyrosyl peptides while its SH3 domain binds to Sos and Sos-derived, proline-rich peptides. Besides it function in Ras signaling, Grb2 is also thought to play a role in apoptosis. Unlike most SH2 structures in which the peptide binds in an extended conformation (such that the +3 peptide residue occupies a hydrophobic pocket in the protein, conferring a modest degree of selectivity), Grb2 forms several hydrogen bonds via main chain atoms with the side chain of +2 Asn. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
KPHPWFHGKISRAEAEEILMNQRPDGAFLIRESESSPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKF
NSLNELVDYHRTTSVSRNQQIFLRD
>gnl|CDD|198195 cd09942, SH2_nSH2_p85_like, N-terminal Src homology 2 (nSH2) domain found in p85. Phosphoinositide 3-kinases (PI3Ks) are essential for cell growth, migration, and survival. p110, the catalytic subunit, is composed of an adaptor-binding domain, a Ras-binding domain, a C2 domain, a helical domain, and a kinase domain. The regulatory unit is called p85 and is composed of an SH3 domain, a RhoGap domain, a N-terminal SH2 (nSH2) domain, an internal SH2 (iSH2) domain, and C-terminal (cSH2) domain. There are 2 inhibitory interactions between p110alpha and p85 of P13K: (1) p85 nSH2 domain with the C2, helical, and kinase domains of p110alpha and (2) p85 iSH2 domain with C2 domain of p110alpha. There are 3 inhibitory interactions between p110beta and p85 of P13K: (1) p85 nSH2 domain with the C2, helical, and kinase domains of p110beta, (2) p85 iSH2 domain with C2 domain of p110alpha, and (3) p85 cSH2 domain with the kinase domain of p110alpha. It is interesting to note that p110beta is oncogenic as a wild type protein while p110alpha lacks this ability. One explanation is the idea that the regulation of p110beta by p85 is unique because of the addition of inhibitory contacts from the cSH2 domain and the loss of contacts in the iSH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
PHSLQEAEWYWGDISREEVNEKMRDTPDGTFLVRDASTMKGDYTLTLRKGGNNKLIKIFHRDGKYGFSDP
LTFNSVVELINYYRNNSLAEYNRKLDVKLLYPVSRFQQDQ
>gnl|CDD|198196 cd09943, SH2_Nck_family, Src homology 2 (SH2) domain found in the Nck family. Nck proteins are adaptors that modulate actin cytoskeleton dynamics by linking proline-rich effector molecules to tyrosine kinases or phosphorylated signaling intermediates. There are two members known in this family: Nck1 (Nckalpha) and Nck2 (Nckbeta and Growth factor receptor-bound protein 4 (Grb4)). They are characterized by having 3 SH3 domains and a C-terminal SH2 domain. Nck1 and Nck2 have overlapping functions as determined by gene knockouts. Both bind receptor tyrosine kinases and other tyrosine-phosphorylated proteins through their SH2 domains. In addition they also bind distinct targets. Neuronal signaling proteins: EphrinB1, EphrinB2, and Disabled-1 (Dab-1) all bind to Nck-2 exclusively. And in the case of PDGFR, Tyr(P)751 binds to Nck1 while Tyr(P)1009 binds to Nck2. Nck1 and Nck2 have a role in the infection process of enteropathogenic Escherichia coli (EPEC). Their SH3 domains are involved in recruiting and activating the N-WASP/Arp2/3 complex inducing actin polymerization resulting in the production of pedestals, dynamic bacteria-presenting protrusions of the plasma membrane. A similar thing occurs in the vaccinia virus where motile plasma membrane projections are formed beneath the virus. Recently it has been shown that the SH2 domains of both Nck1 and Nck2 bind the G-protein coupled receptor kinase-interacting protein 1 (GIT1) in a phosphorylation-dependent manner. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QPWYYGRITRHQAETLLNEHGHEGDFLIRDSESNPGDYSVSLKAPGRNKHFKVQVVDNVYCIGQRKFHTM
DELVEHYKKAPIFTSEQGEKLYL
>gnl|CDD|198197 cd09944, SH2_Grb7_family, Src homology 2 (SH2) domain found in the growth factor receptor bound, subclass 7 (Grb7) proteins. The Grb family binds to the epidermal growth factor receptor (EGFR, erbB1) via their SH2 domains. There are 3 members of the Grb7 family of proteins: Grb7, Grb10, and Grb14. They are composed of an N-terminal Proline-rich domain, a Ras Associating-like (RA) domain, a Pleckstrin Homology (PH) domain, a phosphotyrosine interaction region (PIR, BPS) and a C-terminal SH2 domain. The SH2 domains of Grb7, Grb10 and Grb14 preferentially bind to a different RTK. Grb7 binds strongly to the erbB2 receptor, unlike Grb10 and Grb14 which bind weakly to it. Grb14 binds to Fibroblast Growth Factor Receptor (FGFR). Grb10 has been shown to interact with many different proteins, including the insulin and IGF1 receptors, platelet-derived growth factor (PDGF) receptor-beta, Ret, Kit, Raf1 and MEK1, and Nedd4. Grb7 family proteins are phosphorylated on serine/threonine as well as tyrosine residues. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
IHRSQPWFHGGISRDEAARLIRQQGLVDGVFLVRESQSNPGAFVLSLKHGQKIKHYQIIPIEDEGQWYFT
LDDGVTKFYDLLQLVEFYQLNAGSLPTRLKHYCTRVAL
>gnl|CDD|198198 cd09945, SH2_SHB_SHD_SHE_SHF_like, Src homology 2 domain found in SH2 domain-containing adapter proteins B, D, E, and F (SHB, SHD, SHE, SHF). SHB, SHD, SHE, and SHF are SH2 domain-containing proteins that play various roles throughout the cell. SHB functions in generating signaling compounds in response to tyrosine kinase activation. SHB contains proline-rich motifs, a phosphotyrosine binding (PTB) domain, tyrosine phosphorylation sites, and a SH2 domain. SHB mediates certain aspects of platelet-derived growth factor (PDGF) receptor-, fibroblast growth factor (FGF) receptor-, neural growth factor (NGF) receptor TRKA-, T cell receptor-, interleukin-2 (IL-2) receptor- and focal adhesion kinase- (FAK) signaling. SRC-like FYN-Related Kinase FRK/RAK (also named BSK/IYK or GTK) and SHB regulate apoptosis, proliferation and differentiation. SHB promotes apoptosis and is also required for proper mitogenicity, spreading and tubular morphogenesis in endothelial cells. SHB also plays a role in preventing early cavitation of embryoid bodies and reduces differentiation to cells expressing albumin, amylase, insulin and glucagon. SHB is a multifunctional protein that has difference responses in different cells under various conditions. SHE is expressed in heart, lung, brain, and skeletal muscle, while expression of SHD is restricted to the brain. SHF is mainly expressed in skeletal muscle, brain, liver, prostate, testis, ovary, small intestine, and colon. SHD may be a physiological substrate of c-Abl and may function as an adapter protein in the central nervous system. It is also thought to be involved in apoptotic regulation. SHD contains five YXXP motifs, a substrate sequence preferred by Abl tyrosine kinases, in addition to a poly-proline rich region and a C-terminal SH2 domain. SHE contains two pTry protein binding domains, protein interaction domain (PID) and a SH2 domain, followed by a glycine-proline rich region, all of which are N-terminal to the phosphotyrosine binding (PTB) domain. SHF contains four putative tyrosine phosphorylation sites and an SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QGWYHGAITRIEAESLLRPCKEGSYLVRNSESTKQDYSLSLKSAKGFMHMRIQRNETGQYILGQFSRPFE
TIPEMIRHYCLNKLPVRGAEHMCLLEPV
>gnl|CDD|198199 cd09946, SH2_HSH2_like, Src homology 2 domain found in hematopoietic SH2 (HSH2) protein. HSH2 is thought to function as an adapter protein involved in tyrosine kinase signaling. It may also be involved in regulating cytokine signaling and cytoskeletal reorganization in hematopoietic cells. HSH2 contains several putative protein-binding motifs, SH3-binding proline-rich regions, and phosphotyrosine sites, but lacks enzymatic motifs. HSH2 was found to interact with cytokine-regulated tyrosine kinase c-FES and an activated Cdc42-associated tyrosine kinase ACK1. HSH2 binds c-FES through both its C-terminal region and its N-terminal region including the SH2 domain and binds ACK1 via its N-terminal proline-rich region. Both kinases bound and tyrosine-phosphorylated HSH2 in mammalian cells. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
LAQDGVPEWFHGAISREAAENMLESQPLGSFLIRVSHSHVGYTLSYKAQSSCRHFMVKLLDDGTFMIPGE
KVAHTSLHALVTFHQQKPIEPRRELLTQACRQ
>gnl|CDD|197370 cd09947, Ebola_HIV-1-like_HR1-HR2, heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including Ebola virus and human immunodeficiency virus type 1 (HIV-1). This domain superfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including Ebola virus gp2, Rous sarcoma virus gp37, human immunodeficiency virus type 1 (HIV-1) gp41, and the envelope proteins of various ERVs. In the HR1-HR2 region of Ebola virus and RSV, the linker region between the two repeats includes a CKS17-like immunosuppressive region and a CX6C motif that forms an intra-subunit disulfide bond; MMTV, HIV-1, HERV-K endogenous retroviruses and related sequences lack a canonical CSK17-like sequence, and CX6C motif. N-terminal to the HR1-HR2 region is a fusion peptide (FP), and C-terminal, is a membrane-spanning region (MSR). Viral infection involves the formation of a trimer-of-hairpins structure (three HR1 helices, buttressed by three HR2 helices lying in antiparallel orientation). In this structure, the FP (inserted in the host cell membrane) and MSR (inserted in the viral membrane) are in close proximity. ERVs are likely to originate from ancient germ-line infections by active retroviruses. Some modern ERVs, those that integrated into the host genome post-speciation, have a currently active exogenous counterpart, such as Jaagsiekte sheep retrovirus (JSRV), feline leukemia virus (FeLV), and avian leukemia virus (ALV). Some ERVs play specific roles in the host, including placental development, protection of the host from infection by related pathogenic and exogenous retroviruses, and genome plasticity. Human ERVs (HERVs) belonging to this superfamily include Syncytin-1 (HERV-W_c7q21.2/ ERVWE1), and Syncytin-2 (HERV-FRD_6p24.1) which are expressed in the placenta, and are fusogenic, although they have a different cell specificity for fusion. Syncytin-2, but not Syncytin-1, is immunosuppressive; its immunosuppressive domain may protect the fetus from the mother's immune system. Syncytin-1 may participate in the formation of the placental trophoblast; it is also implicated in cell fusions between cancer and host cells and between cancer cell, and in human osteclast fusion. This superfamily also contains human HERV-R_c7q21.2 (ERV-3), which is also expressed in the placenta, but is not fusogenic, and has an immunosuppressive domain, but lacks a fusion peptide. It is unclear whether ERV-3 has a critical biological role. Included in this superfamily are ERVs from domestic sheep that are related to JSRV, the agent of transmissible lung cancer in sheep; for example, enJSRV-26 that retains an intact genome. These endogenous JSRVs protect the sheep against JSRV infection and are required for sheep placental development
RLQQLLRLTTQAIKNLHTNLTAIAKYLAQNRRGLDWLAARRGGTCVALTEVCCPFLSITNKWWQDWIRKL
DFL
>gnl|CDD|197371 cd09948, Ebola_RSV-like_HR1-HR2, heptad repeat 1-heptad repeat 2 region of the transmembrane subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including Ebola virus and Rous sarcoma virus. This domain family spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of endogenous retroviruses (ERVs) and infectious retroviruses, including Ebola virus gp2, Rous sarcoma virus gp37, and the envelope proteins of various ERVs. This domain includes an N-terminal heptad repeat, a CKS17-like immunosuppressive region, a CX6C motif that forms an intra-subunit disulfide bond, and a C-terminal heptad repeat. N-terminal to HR1-HR2 region is a fusion peptide (FP), while C-terminal, is a membrane-spanning region (MSR). Viral infection involves the formation of a trimer-of-hairpins structure (three HR1s helices, buttressed by three HR2 helices lying in antiparallel orientation). In this structure, the FP (inserted in the host cell membrane) and MSR (inserted in the viral membrane) are in close proximity. ERVs are likely to originate from ancient germ-line infections by active retroviruses. Some modern ERVs, those that integrated into the host genome post-speciation, have a currently active exogenous counterpart, such as Jaagsiekte sheep retrovirus (JSRV), feline leukemia virus (FeLV), and avian leukemia virus (ALV). Some ERVs play specific roles in the host, including placental development, protection of the host from infection by related pathogenic and exogenous retroviruses, and genome plasticity. Human ERVs (HERVs) belonging to this family include Syncytin-1 (HERV-W_c7q21.2/ ERVWE1), and Syncytin-2 (HERV-FRD_6p24.1) which are expressed in the placenta, and are fusogenic, although they have a different cell specificity for fusion. Syncytin-2, but not Syncytin-1, is immunosuppressive. Its immunosuppressive domain may protect the fetus from the mother's immune system. Syncytin-1 may participate in the formation of the placental trophoblast. It is also implicated in cell fusions between cancer and host cells and between cancer cells, and in human osteclast fusion. This family also contains human HERV-R_c7q21.2 (ERV-3), which is also expressed in the placenta, but is not fusogenic, has an immunosuppressive domain, but lacks a fusion peptide. It is unclear whether ERV-3 has a critical biological role
GLEQDANETTQALQLFLRNVTSLRTVVLQNRRALDFLLAREGGTCHIINEDCCCFLNDQSRITDKIDQLI
EQ
>gnl|CDD|197372 cd09949, RSV-like_HR1-HR2, heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of Rous sarcoma virus (RSV), and related domains. This domain subfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including Rous sarcoma virus gp37, Avian leukosis virus subgroup J (ALV-J) envelope protein, and the envelope proteins of various ERVs, including those belonging to the ev/J (or EAV-HP) family of chicken ERVs, such as ev/J 4.1 Rb. ALV-J is a recently emerged avian pathogen, the causative agent of myeloid leukosis in meat-type chicken. ERVs are likely to originate from ancient germ-line infections by active retroviruses. ALV-J may have emerged from a recombination event between an unknown ALV and an EAV-HP ERV. This domain includes an N-terminal heptad repeat, a CKS17-like immunosuppressive region, a CX6C motif that forms an intrasubunit disulfide bond, and a C-terminal heptad repeat. N-terminal to HR1-HR2 region is a fusion peptide (FP), and C-terminal, is a membrane-spanning region (MSR). Viral infection involves the formation of a trimer-of-hairpins structure (three HR1s helices, buttressed by three HR2 helices lying in antiparallel orientation). In this structure, the FP (inserted in the host cell membrane) and MSR (inserted in the viral membrane) are in close proximity
WSVKQANATSLALNDLLEDIGSIRHAVLQNRAAIDFLLLAHGHGCEDFEGLCCFNLSDHSEIIHKILQAM
KE
>gnl|CDD|197373 cd09950, ENVV1-like_HR1-HR2, heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of the human endogenous retrovirus ENVV1, and related domains. This domain subfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of various endogenous retroviruses (ERVs), including chicken FET-1 (Female Expressed Transcript 1) protein, and the envelope proteins of the human ERVs (HERVs): ENVV1 (also known as HERV-V2_c19q13.41) and ENVV2 (also known as HERV-V1_c19q13.41). This domain belongs to a larger superfamily containing the HR1-HR2 domain of endogenous retroviruses (ERVs) and infectious retroviruses, such as Ebola virus, Rous sarcoma virus and human immunodeficiency virus type 1. This domain includes an N-terminal heptad repeat, a CKS17-like immunosuppressive region, a CX6C motif that forms an intra-subunit disulfide bond, and a C-terminal heptad repeat. N-terminal to HR1-HR2 region is a fusion peptide (FP), and C-terminal, is a membrane-spanning region (MSR). Viral infection involves the formation of a trimer-of-hairpins structure (three HR1 helices, buttressed by three HR2 helices lying in antiparallel orientation). In this structure, the FP (inserted in the host cell membrane) and MSR (inserted in the viral membrane) are in close proximity. ERVs are likely to originate from ancient germ-line infections by active retroviruses. Some ERVs play specific roles in the host, including placental development, protection of the host from infection by related pathogenic and exogenous retroviruses, and genome plasticity. FET-1 may have an ovary-determining role. The FET-1 gene is located on the female specific W chromosome in chickens. During the sex-determining period, the FET-1 transcript is up-regulated in the cortex of the left gonad (the only gonad which develops in female chickens); it is also expressed at a lower level, in neural tissue and waste collection ducts. The genes encoding ENVV1 and ENVV2 proteins are located in tandem on chromosome 19q13.41, and show placenta-specific expression in human and baboon
QLDNIANSTRDSISALQAEVSSLSNVVLQNRMALDLLLAEQGGVCAVINQSCCAYVNNSGRIETDIKKIY
DQ
>gnl|CDD|197374 cd09951, HERV-Rb-like_HR1-HR2, heptad repeat 1- heptad repeat 2 region (ectodomain) of the transmembrane subunit of the human endogenous retrovirus HERV-R(b)_c3p24.3 and related domains. This domain subfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of various endogenous retroviruses (ERVs) including the human ERVs (HERVs): HERV-R(b)_c3p24.3 and Syncytin-3 (also known as HERV-P(b)_c14q32.12). This domain belongs to a larger superfamily containing the HR1-HR2 domain of endogenous retroviruses (ERVs) and infectious retroviruses, such as Ebola virus, Rous sarcoma virus (RSV) and human immunodeficiency virus type 1 (HIV-1). This domain includes an N-terminal heptad repeat, a CKS17-like immunosuppressive region, a CX6C motif that forms an intrasubunit disulfide bond, and a C-terminal, is a heptad repeat. In intact retroviruses, N-terminal to HR1-HR2 region is a fusion peptide (FP), and C-terminal, is a membrane-spanning region (MSR). Viral infection involves the formation of a trimer-of-hairpins structure (three HR1s helices, buttressed by three HR2 helices lying in antiparallel orientation). In this structure, the FP (inserted in the host cell membrane) and MSR (inserted in the viral membrane) are in close proximity. ERVs are likely to originate from ancient germ-line infections by active retroviruses. Some ERVs play specific roles in the host, including placental development, protection of the host from infection by related pathogenic and exogenous retroviruses, and genome plasticity. Syncytin-3 is fusogenic, HERV-R(b)_c3p24.3 appears not to have fusogenic activity
YIHYNVQRLLNLTRQAISGMNEQLYATSLMALQNRMALDMLLAEKGGVCSMIKTECCTYIPNNTAPDGSI
SLALEGLCRLS
>gnl|CDD|197375 cd09966, UP_III_II, Uroplakin IIIb, IIIa and II. Uroplakins (UPs) are a family of proteins that associate with each other to form plaques on the apical surface of the urothelium, the pseudo-stratified epithelium lining the urinary tract from renal pelvis to the bladder outlet. UPs are classified into 3 types: UPIa and UPIb, UPII, and UPIIIa and IIIb. UPIs are tetraspanins that have four transmembrane domains separating one large and one small extracellular domain while UPII and UPIIIs are single-pass transmembrane proteins. UPIa and UPIb form specific heterodimers with UPII and UPIII, respectively, which allows them to exit the endoplasmatic rediculum. UPII/UPIa and UPIIIs/UPIb form heterotetramers; six of these tetramers form the 16nm particle, seen in the hexagonal array of the asymmetric unit membrane, which is believed to form a urinary tract barrier. Uroplakins are also believed to play a role during urinary tract morphogenesis
LSYVPQLTASTGAGNPTLSTFTLEQPPCMFDSSSTDDVWLVVALPNATLAFQNVTLSTDISTYLTFTTGN
YYKTLRASFDLPPCRNRRDIVSAYVLRVGNTTTCLSGYCNTPLPGPGPYRVKYLVMNGSGPSAQTEWSTP
IRLNQNKIYSTTWPGARSGGMIVITVILSVLMFLLLVALIA
>gnl|CDD|197376 cd09967, UP_II, Uroplakin II. Uroplakin II, the dimerization partner of uroplakin Ia, is a member of the uroplakin family. Uroplakins (UPs) are a family of proteins that associate with each other to form plaques on the apical surface of the urothelium, the pseudo-stratified epithelium lining the urinary tract from renal pelvis to the bladder outlet. UPs are classified into 3 types: UPIa and UPIb, UPII, and UPIIIa and IIIb. UPIs are tetraspanins that have four transmembrane domains seperating one large and one small extracellular domain while UPII and UPIIIs are single-pass transmembrane proteins. UPIa and UPIb form specific heterodimers with UPII and UPIII, respectively, which allows them to exit the endoplasmatic rediculum. UPII/UPIa and UPIIIs/UPIb form heterotetramers and six of these tetramers form the 16nm particle, seen in the hexagonal array of the asymmetric unit membrane, which is believed to form a urinary tract barrier. Uroplakins are also believed to play a role during urinary tract morphogenesis
LGIILILLAVLGAADFNISSLSGVLTPALTESLLVALPPCHLTGQNVTLELMNRRANDSKVVKSSFVVPP
CRGRRDIVSVVDSGSGFTVTRNSGYQVTNLTPGTKYYISYLVGKGTESSREIPMSTLPRKNMNSIGLGMA
RSGGMVVITVLLSVAMFLLLVGLIF
>gnl|CDD|197377 cd09968, UP_III, Uroplakin III. Uroplakin IIIa and IIIb, the dimerization partners of uroplakin Ib, are a members of the uroplakin family. Uroplakins (UPs) are a family of proteins that associate with each other to form plaques on the apical surface of the urothelium, the pseudo-stratified epithelium lining the urinary tract from renal pelvis to the bladder outlet. UPs are classified into 3 types: UPIa and UPIb, UPII, and UPIIIa and IIIb. UPIs are tetraspanins that have four transmembrane domains seperating one large and one small extracellular domain while UPII and UPIIIs are single-pass transmembrane proteins. UPIa and UPIb form specific heterodimers with UPII and UPIII, respectively, which allows them to exit the endoplasmatic rediculum. UPII/UPIa and UPIIIs/UPIb form heterotetramers and six of these tetramers form the 16nm particle, seen in the hexagonal array of the asymmetric unit membrane, which is believed to form a urinary tract barrier. Uroplakins are also believed to play a role during urinary tract morphogenesis
EAVSYVPQLASTFLEGNPTSTTFTLEQPRCVFDSSASDTDDVWLVVAVSNATNNFNAPQNSTDPISTYSQ
FSGGQYYLTLRASRDLYPCGNPSLNAYVLRVGADGNCTDNGNCNGPLPGPGPYRVKYLVMNGSGVVAQTN
WSDPIRLNQAKSYQTIDTWPGRRSGGMIVITSILSVLLALLLLALLA
>gnl|CDD|197378 cd09969, UP_IIIb, Uroplakin IIIb. Uroplakin IIIb, minor isoform of the dimerization partner of uroplakin Ib, is a members of the uroplakin family. Uroplakins (UPs) are a family of proteins that associate with each other to form plaques on the apical surface of the urothelium, the pseudo-stratified epithelium lining the urinary tract from renal pelvis to the bladder outlet. UPs are classified into 3 types: UPIa and UPIb, UPII, and UPIIIa and IIIb. UPIs are tetraspanins that have four transmembrane domains seperating one large and one small extracellular domain while UPII and UPIIIs are single-pass transmembrane proteins. UPIa and UPIb form specific heterodimers with UPII and UPIII, respectively, which allows them to exit the endoplasmatic rediculum. UPII/UPIa and UPIIIs/UPIb form heterotetramers and six of these tetramers form the 16nm particle, seen in the hexagonal array of the asymmetric unit membrane, which is believed to form a urinary tract barrier. Uroplakins are also believed to play a role during urinary tract morphogenesis
EKISYVPQLTPAPLEGRITSSTFVLEQPRCVFSSSSDGDDIWLVVALSNATQNFNAPVKSSDIPTASSFS
TKGYYLTLRASRALYPCGNPSMGLPVLRVGADTGCTDNNCNGPLPGPGPYRVKFLVMNNRGPVAETNWSD
PITLRTGKSPQTIDTWPGRRSGGMIVITTILSVLLALLLLALLA
>gnl|CDD|197379 cd09970, UP_IIIa, Uroplakin IIIa. Uroplakin IIIa, mayor isoform of the dimerization partner of uroplakin Ib, is a members of the uroplakin family. Uroplakins (UPs) are a family of proteins that associate with each other to form plaques on the apical surface of the urothelium, the pseudo-stratified epithelium lining the urinary tract from renal pelvis to the bladder outlet. UPs are classified into 3 types: UPIa and UPIb, UPII, and UPIIIa and IIIb. UPIs are tetraspanins that have four transmembrane domains seperating one large and one small extracellular domain while UPII and UPIIIs are single-pass transmembrane proteins. UPIa and UPIb form specific heterodimers with UPII and UPIII, respectively, which allows them to exit the endoplasmatic rediculum. UPII/UPIa and UPIIIs/UPIb form heterotetramers and six of these tetramers form the 16nm particle, seen in the hexagonal array of the asymmetric unit membrane, which is believed to form a urinary tract barrier. Uroplakins are also believed to play a role during urinary tract morphogenesis
SAVNLQPQLASVTFATNNPTLTTITLEKPFCMFDSKEALTGTHEVYLYVLVDSAISRNASVQDSTNTPLG
STFLQTEGGRTGPYKAAAFDLPPCSDLPSLDAIGDVSKASQILNAYLVRVGANGTCLWDPNFKGLCNPPL
SAATEYRFKYVLVNMSTGLVEDQTLWSDPIRTNQLTPYSTIDTWPGRRSGGMIVITSILSTLPFFLLVGF
AG
>gnl|CDD|197380 cd09971, SdiA-regulated, SdiA-regulated. This model represents a bacterial family of proteins that may be regulated by SdiA, a member of the LuxR family of transcriptional regulators. The C-terminal domain included in the alignment forms a five-bladed beta-propeller structure. The X-ray structure of Escherichia coli yjiK (C-terminal domain) exhibits binding of calcium ions (Ca++) in what appears to be an evolutionarily conserved site. Sequence analysis suggests a distant relationship to proteins that are characterized as containing NHL-repeats. The latter also form beta-propeller structures, with several examples known to form six-bladed beta-propellers. Several of the six-bladed beta-propellers containing NHL repeats have been characterized functionally, including members with enzymatic functions that are dependent on metal ions. No functional characterization is available for this family of five-bladed propellers, though
YRLAIEGKPIGGILDELSGLTYNPDTDTLFAVTNKPPALVELSKDGDVLRRIPLDGFSDPEGITYLGDGQ
FAIVDERLQALLIVYVDGDTTSLDAADAQSITLGFTEKGNKGFEGIAWDPRNGRLFVVKERNPGRLFEVN
GDGAANLALVVKDRKLLAAADLFLSDLSSLSFDPRTGHLLVLSDESRLLVELDRQGRVVSSLSLTRGFNG
LSKTIPQAEGVAMDPDGTLYIVSEPNLFYRFK
>gnl|CDD|193586 cd09972, LOTUS_TDRD_OSKAR, The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7. The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7: The LOTUS containing proteins are germline-specific and are found in the nuage/polar granules of germ cells. Tudor-containing protein 5 and 7 belong to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 and TDRD7 are components of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. Oskar protein is a critical component of the pole plasm in the Drosophila oocyte, which is required for germ cell formation.The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
LEEVKKVLRSLLISSKGGLTLSELERDYRELEGEPIPYRKLGYSSLEDFLRSIPDVVTVRSSGGEVLVKA
VADEKTAHIASLVAKQK
>gnl|CDD|193587 cd09973, LOTUS_2_TDRD7, The second LOTUS domain on Tudor-containing protein 7 (TDRD7). The second LOTUS domain on Tudor-containing protein 7 (TDRD7): TDRD7 contains three N-terminal LOTUS domains and three Tudor domain repeats at the C-terminus. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD7 together with TDRD1/MTR-1, TDRD5 and TDRD6 forms a ribonucleoprotein complex in the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs) involving in RNA processing for spermatogenesis. TDRD7 is functionally essential for the differentiation of germ cells. The exact molecular function of LOTUS domain on TDRD7 remains to be characterized. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
VQEVQNRIKELLNKYSNGVWLSKLPQLYKEMYKEDLSTEVLKQLESWPHVCTVEKPHSGDPTDLLLYP
>gnl|CDD|193588 cd09974, LOTUS_3_TDRD7, The third LOTUS domain on Tudor-containing protein 7 (TDRD7). The third LOTUS domain on Tudor-containing protein 7 (TDRD7): TDRD7 contains three N-terminal LOTUS domains and three Tudor domain repeats at the C-terminus. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD7 together with TDRD1/MTR-1, TDRD5 and TDRD6 forms a ribonucleoprotein complex in the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs) involving in RNA processing for spermatogenesis. TDRD7 is functionally essential for the differentiation of germ cells. The exact molecular function of LOTUS domain on TDRD7 remains to be characterized. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
SDDLKEKVAQLLVKYSNGLWASALPKLFEDAYKVKFPEHILENLSLLTDICIVDYPSGNPQKAILYS
>gnl|CDD|193589 cd09975, LOTUS_2_TDRD5, The second LOTUS domain on Tudor-containing protein 5 (TDRD5). The second LOTUS domain on Tudor-containing protein 5 (TDRD5): TDRD5 contains three N-terminal LOTUS domains and a C-terminal Tudor domain. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice TDRD5 is a component of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. The exact molecular function of LOTUS domain on TDRD5 remains to be discovered. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
PAHVKSELKDLLSHSPVLLSELEKAYVARFGRSFQYTQYGFFSMLEVLSAASDFIIVKQTRTGSLLLLKK
>gnl|CDD|193590 cd09976, LOTUS_3_TDRD5, The third LOTUS domain on Tudor-containing protein 5 (TDRD5). The third LOTUS domain on Tudor-containing protein 5 (TDRD5): TDRD5 contains three N-terminal LOTUS domains and a C-terminal Tudor domain. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice TDRD5 is a component of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. The exact molecular function of LOTUS domain on TDRD5 remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
SRELREEIRKVVENHPNGLFIALLPTEYKVLFKEELPVKQLGFLSVTELVGSLSDILAIERREKESDWLV
FDAK
>gnl|CDD|193591 cd09977, LOTUS_1_Limkain_b1, The first LOTUS domain on Limkain b1(LKAP). The first LOTUS domain on Limkain b1(LKAP): Limkain b1 is a novel human autoantigen, localized to a subset of ABCD3 and PXF marked peroxisomes. Limkain b1 may be a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. The protein contains multiple copies of LOTUS domains and a conserved RNA recognition motif. The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
LSLLSSETVSILQDAPACCLPLFKFTEIYEKKFGHKLAVSDLYRLTDTVAIREQGGGRLVCL
>gnl|CDD|193592 cd09978, LOTUS_2_Limkain_b1, The second LOTUS domain on Limkain b1(LKAP). The second LOTUS domain on Limkain b1(LKAP): Limkain b1 is a novel human autoantigen, localized to a subset of ABCD3 and PXF marked peroxisomes. Limkain b1 may be a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. The protein contains multiple copies of LOTUS domains and a conserved RNA recognition motif. The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
LKTFAPQVHSLLQTHEGTVPLLSFPDCYAAEFSALEVVQEGQGGVPLEHLITCIPGVNIATAQNGIKVIK
W
>gnl|CDD|193593 cd09979, LOTUS_3_Limkain_b1, The third LOTUS domain on Limkain b1(LKAP). The third LOTUS domain on Limkain b1(LKAP): Limkain b1 is a novel human autoantigen, localized to a subset of ABCD3 and PXF marked peroxisomes. Limkain b1 may be a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. The protein contains multiple copies of LOTUS domains and a conserved RNA recognition motif. The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
LIQFSREVIDLLKSQPSCLLPFSRFIPAYHHHFGKQCRVSDYGYTKLIELLEAVPHVLQILGMGSKRLLT
LS
>gnl|CDD|193594 cd09980, LOTUS_4_Limkain_b1, The fourth LOTUS domain on Limkain b1(LKAP). The fourth LOTUS domain on Limkain b1(LKAP): Limkain b1 is a novel human autoantigen, localized to a subset of ABCD3 and PXF marked peroxisomes. Limkain b1 may be a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. The protein contains multiple copies of LOTUS domains and a conserved RNA recognition motif. The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
VRRFTQDLLRVLKSQASKQVIVKDFGQAYEWCFGRDWDPVDYGLCDLQDLLSEIPDNTIVIEQQDGDKVI
SI
>gnl|CDD|193595 cd09981, LOTUS_5_Limkain_b1, The fifth LOTUS domain on Limkain b1(LKAP). The fifth LOTUS domain on Limkain b1(LKAP): Limkain b1 is a novel human autoantigen, localized to a subset of ABCD3 and PXF marked peroxisomes. Limkain b1 may be a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. The protein contains multiple copies of LOTUS domains and a conserved RNA recognition motif. The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
TKQFSKEVVELLRHQPHFRMPFTKFIPSYHHHFGRQCKLSYYGFTKLLELFEAIPDVVQVLECGEEKYLQ
L
>gnl|CDD|193596 cd09982, LOTUS_6_Limkain_b1, The sixth LOTUS domain on Limkain b1(LKAP). The sixth LOTUS domain on Limkain b1(LKAP): Limkain b1 is a novel human autoantigen, localized to a subset of ABCD3 and PXF marked peroxisomes. Limkain b1 may be a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. The protein contains multiple copies of LOTUS domains and a conserved RNA recognition motif. The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
VKALAAQLVKLLRSQKDSCLMMCDLLTEYSKTFGYTLRLQDYDVSSVPALMQKLCHVVKVVDTESGKQIQ
L
>gnl|CDD|193597 cd09983, LOTUS_7_Limkain_b1, The seventh LOTUS domain on Limkain b1(LKAP). The seventh LOTUS domain on Limkain b1(LKAP): Limkain b1 is a novel human autoantigen, localized to a subset of ABCD3 and PXF marked peroxisomes. Limkain b1 may be a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. The protein contains multiple copies of LOTUS domains and a conserved RNA recognition motif. The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
LRSLTAQLLVLLMSWEGASDLSVEELRQHYESVHGTPLNPCEYGFMSLTELLKSLPYLVEVFTNGGGEEY
VRL
>gnl|CDD|193598 cd09984, LOTUS_8_Limkain_b1, The eighth LOTUS domain on Limkain b1(LKAP). The eighth LOTUS domain on Limkain b1(LKAP): Limkain b1 is a novel human autoantigen, localized to a subset of ABCD3 and PXF marked peroxisomes. Limkain b1 may be a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. The protein contains multiple copies of LOTUS domains and a conserved RNA recognition motif. The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
LYQFAKNVRSLLHTYHYQQIFLHEFSSAYSKYVGETLQPKNYGYNSLEELLGAIPQVVWIKGHGHKRIVV
LKNDMK
>gnl|CDD|193599 cd09985, LOTUS_1_TDRD5, The first LOTUS domain on Tudor-containing protein 5 (TDRD5). The first LOTUS domain on Tudor-containing protein 5 (TDRD5): TDRD5 contains three N-terminal LOTUS domains and a C-terminal Tudor domain. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 is a component of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. The exact molecular function of LOTUS domain on TDRD5 remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
QEQIMERLKKDVRSLLISSKNGLTPEQLEQDYLAMVGSPLPLRSLGFRSTMELVLDMPDVVRVHPQLDGT
VILKAVGDETTKGIEDLVSKQRDSK
>gnl|CDD|193600 cd09986, LOTUS_1_TDRD7, The first LOTUS domain on Tudor-containing protein 7 (TDRD7). The first LOTUS domain on Tudor-containing protein 7 (TDRD7): TDRD7 contains three N-terminal LOTUS domains and three Tudor domain repeats at the C-terminus. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD7 together with TDRD1/MTR-1, TDRD5 and TDRD6 forms a ribonucleoprotein complex in the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs) involving in RNA processing for spermatogenesis. TDRD7 is functionally essential for the differentiation of germ cells. The exact molecular function of LOTUS domain on TDRD7 remains to be characterized. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization
VELVKKMLRAVLQSSKGGVSLPRLQGEYKELTGEQIPFKQLGYHTLDALLRSMPSVVRLERSRSGEVMCF
ASLCNETAHIAKLVARQR
>gnl|CDD|212513 cd09987, Arginase_HDAC, Arginase-like and histone-like hydrolases. Arginase-like/histone-like hydrolase superfamily includes metal-dependent enzymes that belong to Arginase-like amidino hydrolase family and histone/histone-like deacetylase class I, II, IV family, respectively. These enzymes catalyze hydrolysis of amide bond. Arginases are known to be involved in control of cellular levels of arginine and ornithine, in histidine and arginine degradation and in clavulanic acid biosynthesis. Deacetylases play a role in signal transduction through histone and/or other protein modification and can repress/activate transcription of a number of different genes. They participate in different cellular processes including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. Mammalian histone deacetyases are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs
APSAIRKAEAHELLAGVVVAVLKDGKVPVVLGGDHSIANGAIRAVAELHPDLGVIDVDAHHDVRTPEAFG
KGNHHTPRHLLCEPLISDVHIVSIGIRGVSNGEAGGAYARKLGVVYFSMTEVDKLGLGDVFEEIVSYLGD
KGDNVYLSVDVDGLDPSFAPGTGTPGPGGLSYREGLYITERIAKTNLVVGLDIVEVNPLLDETGRTARLA
AALTLEL
>gnl|CDD|212514 cd09988, Formimidoylglutamase, Formimidoylglutamase or HutE. Formimidoylglutamase (N-formimidoyl-L-glutamate formimidoylhydrolase; formiminoglutamase; N-formiminoglutamate hydrolase; N-formimino-L-glutamate formiminohydrolase; HutE; EC 3.5.3.8) is a metalloenzyme that catalyzes hydrolysis of N-formimidoyl-L-glutamate to L-glutamate and formamide. This enzyme is involved in histidine degradation, requiring Mn as a cofactor while glutathione may be required for maximal activity. In Pseudomonas PAO1, mutation studies show that histidine degradation proceeds via a 'four-step' pathway if the 'five-step' route is absent and vice versa; in the four-step pathway, formiminoglutaminase (HutE, EC 3.5.3.8) directly converts formiminoglutamate (FIGLU) to L-glutamate and formamide in a single step. Formiminoglutamase has traditionally also been referred to as HutG; however, formiminoglutamase is structurally and mechanistically unrelated to N-formyl-glutamate deformylase (also called HutG). Phylogenetic analysis has suggested that HutE was acquired by horizontal gene transfer from a Ralstonia-like ancestor
ALLGFPEDEGVRRNKGRVGAAQGPDAIRKALYNLPPGNWGLKIYDLGDIICDGDSLEDTQQALAEVVAEL
LKKGIIPIVIGGGHDLAYGHYRGLDKALEKKIGIINFDAHFDLRPLEEGRHSGTPFRQILEECPNNLFNY
SVLGIQEYYNTQELFDLAKELGVLYFEAERLLGEKILDILEAEPALRDAIYLSIDLDVISSSDAPGVSAP
SPNGLSPEEACAIARYAGKSGKVRSFDIAELNPSLDIDNRTAKLAAYLIEGF
>gnl|CDD|212515 cd09989, Arginase, Arginase family. This family includes arginase, also known as arginase-like amidino hydrolase family, and related proteins. Arginase is a binuclear Mn-dependent metalloenzyme and catalyzes hydrolysis of L-arginine to L-ornithine and urea (Arg, EC 3.5.3.1), the reaction being the fifth and final step in the urea cycle, providing the path for the disposal of nitrogenous compounds. Arginase controls cellular levels of arginine and ornithine which are involved in protein biosynthesis, and in production of creatine, polyamines, proline and nitric acid. In vertebrates, at least two isozymes have been identified: type I (ARG1) cytoplasmic or hepatic liver-type arginase and type II (ARG2) mitochondrial or non-hepatic arginase. Point mutations in human arginase ARG1 gene lead to hyperargininemia with consequent mental disorders, retarded development and early death. Hyperargininemia is associated with a several-fold increase in the activity of the mitochondrial arginase (ARG2), causing persistent ureagenesis in patients. ARG2 overexpression plays a critical role in the pathophysiology of cholesterol mediated endothelial dysfunction. Thus, arginase is a therapeutic target to treat asthma, erectile dysfunction, atherosclerosis and cancer
ISIIGVPFDLGAGKRGVELGPEALREAGLLERLEELGHDVEDLGDLLVPNPEEESPFNGNAKNLDEVLEA
NEKLAEAVAEALEEGRFPLVLGGDHSIAIGTIAGVARAPYPDLGVIWIDAHADINTPETSPSGNIHGMPL
AALLGEGHPELTNIGGVGPKLKPENLVYIGLRDLDPGERELIKKLGIKVFTMDEIDERGIGAVMEEALEY
LKPGTDGIHVSFDVDVLDPSIAPGTGTPVPGGLTYREAHLLLEELAETGRLVSLDIVEVNPLLDKENRTA
ELAVELIASA
>gnl|CDD|212516 cd09990, Agmatinase-like, Agmatinase-like family. Agmatinase subfamily currently includes metalloenzymes such as agmatinase, guanidinobutyrase, guanidopropionase, formimidoylglutamase and proclavaminate amidinohydrolase. Agmatinase (agmatine ureohydrolase; SpeB; EC=3.5.3.11) is the key enzyme in the synthesis of polyamine putrescine; it catalyzes hydrolysis of agmatine to yield putrescine and urea. This enzyme has been found in bacteria, archaea and eukaryotes, requiring divalent Mn and sometimes Zn, Co or Ca for activity. In mammals, the highest level of agmatinase mRNA was found in liver and kidney. However, catabolism of agmatine via agmatinase apparently is a not major path; it is mostly catabolized via diamine oxidase. Agmatinase has been shown to be down-regulated in tumor renal cells. Guanidinobutyrase (Gbh, EC=3.5.3.7) catalyzes hydrolysis of 4-guanidinobutanoate to yield 4-aminobutanoate and urea in arginine degradation pathway. Activity has been shown for purified enzyme from Arthrobacter sp. KUJ 8602. Additionally, guanidinobutyrase is able to hydrolyze D-arginine, 3-guanidinopropionate, 5-guanidinovaleriate and L-arginine with much less affinity, having divalent Zn ions for catalysis. Proclavaminate amidinohydrolase (Pah, EC 3.5.3.22) hydrolyzes amidinoproclavaminate to yield proclavaminate and urea in clavulanic acid biosynthesis. Activity has been shown for purified enzyme from Streptomyces clavuligerus. Clavulanic acid is the effective inhibitor of beta-lactamases. This acid is used in combination with the penicillin amoxicillin to prevent antibiotic's beta-lactam rings from hydrolysis, thus keeping the antibiotics biologically active
VAVLGVPFDGGSTSRPGARFGPRAIREASAGYSTYSPDLGVDDFDDLTVVDYGDVPVDPGDIEKTFDRIR
EAVAEIAEAGAIPIVLGGDHSITYPAVRGLAERHKGKVGVIHFDAHLDTRDTDGGGELSHGTPFRRLLED
GNVDGENIVQIGIRGFWNSPEYVEYAREQGVTVITMRDVRERGLDAVIEEALEIASDGTDAVYVSVDIDV
LDPAFAPGTGTPEPGGLTPRELLDAVRALGAEAGVVGMDIVEVSPPLDPTDITARLAARAVLEFL
>gnl|CDD|212517 cd09991, HDAC_classI, Class I histone deacetylases. Class I histone deacetylases (HDACs) are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. This group includes animal HDAC1, HDAC2, HDAC3, HDAC8, fungal RPD3, HOS1 and HOS2, plant HDA9, protist, archaeal and bacterial (AcuC) deacetylases. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase. In mammals, they are known to be involved in progression of various tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs
FYDPDVGNYYYGQGHPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDN
MKEFKKQLERFNVGEDCPVFDGLYEYCQLYAGGSIAAAVKLNRGQADIAINWAGGLHHAKKSEASGFCYV
NDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKFGEYFFPGTGLRDIGAGKGKYYA
VNVPLKDGIDDESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKSFNI
PLLVLGGGGYTLRNVARCWTYETAVL
>gnl|CDD|212518 cd09992, HDAC_classII, Histone deacetylases and histone-like deacetylases, classII. Class II histone deacetylases are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. This group includes animal HDAC4,5,6,7,8,9,10, fungal HOS3 and HDA1, plant HDA5 and HDA15 as well as other eukaryotes, archaeal and bacterial histone-like deacetylases. Eukaryotic deacetylases mostly use histones (H2, H3, H4) as substrates for deacetylation; however, non-histone substrates are known (for example, tubulin). Substrates for prokaryotic histone-like deacetylases are not known. Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Interaction partners of class II deacetylases include 14-3-3 proteins, MEF2 family of transcriptional factors, CtBP, calmodulin (CaM), SMRT, N-CoR, BCL6, HP1alpha and SUMO. Histone deacetylases play a role in the regulation of cell cycle, cell differentiation and survival. Class II mammalian HDACs are differentially inhibited by structurally diverse compounds with known antitumor activities, thus presenting them as potential drug targets for human diseases resulting from aberrant acetylation
HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGYLDPDTYVSPGS
YEAALLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLKRVLIV
DWDVHHGNGTQDIFYDDPSVLYFSIHQYPFYPGTGAAEETGGGAGEGFTINVPLPPGSGDAEYLAAFEEV
LLPIAREFQPDLVLVSAGFDAHRGDPLGGMNLTPEGYARLTRLLKELADEHCGGRLVFVLEGGYNLEALA
ESVLAVLEALL
>gnl|CDD|212519 cd09993, HDAC_classIV, Histone deacetylase class IV also known as histone deacetylase 11. Class IV histone deacetylases (HDAC11; EC 3.5.1.98) are predicted Zn-dependent enzymes. This class includes animal HDAC11, plant HDA2 and related bacterial deacetylases. Enzymes in this subfamily participate in regulation of a number of different processes through protein modification (deacetylation). They catalyze hydrolysis of N(6)-acetyl-lysine of histones (or other proteins) to yield a deacetylated proteins. Histone deacetylases often act as members of large multi-protein complexes such as mSin3A or SMRT/N-CoR. Human HDAC11 does not associate with them but can interact with HDAC6 in vivo. It has been suggested that HDAC11 and HDAC6 may use non-histone proteins as their substrates and play a role other than to directly modulate chromatin structure. In normal tissues, expression of HDAC11 is limited to kidney, heart, brain, skeletal muscle and testis, suggesting that its function might be tissue-specific. In mammals, HDAC11 proteins are known to be involved in progression of various tumors. HDAC11 plays an essential role in regulating OX40 ligand (OX40L) expression in Hodgkin lymphoma (HL); selective inhibition of HDAC11 expression significantly up-regulates OX40L and induces apoptosis in HL cell lines. Thus, inhibition of HDAC11 could be a therapeutic drug option for antitumor immune response in HL patients
HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSGELSREEIRRIGFPWSPEL
VERTRLAVGGTILAARLALEHGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDLD
VHQGNGTAAIFADDPSVFTFSMHGEKNYPFRKEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLV
FYNAGVDVLAGDRLGRLSLSLEGLRERDRLVLRFARARGIPVAMVLGGGYSRDIARLVARHAQTL
>gnl|CDD|212520 cd09994, HDAC_AcuC_like, Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes. AcuC (Acetoin utilization protein) is a class I deacetylase found only in bacteria and is involved in post-translational control of the acetyl-coenzyme A synthetase (AcsA). Deacetylase AcuC works in coordination with deacetylase SrtN (class III), possibly to maintain AcsA in active (deacetylated) form and let the cell grow under low concentration of acetate. B. subtilis AcuC is a member of operon acuABC; this operon is repressed by the presence of glucose and does not show induction by acetoin; acetoin is a bacterial fermentation product that can be converted to acetate via the butanediol cycle in absence of other carbon sources. Inactivation of AcuC leads to slower growth and lower cell yield under low-acetate conditions in Bacillus subtilis. In general, Class I histone deacetylases (HDACs) are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase
AFIYSEEYLRYSFGPNHPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASR
GQEPEGRGRLGLGTEDNPVFPGMHEAAALVVGGTLLAARLVLEGEARRAFNPAGGLHHAMRGRASGFCVY
NDAAVAIERLRDKGGLRVAYVDIDAHHGDGVQAAFYDDPRVLTISLHESGRYLFPGTGFVDEIGEGEGYG
YAVNIPLPPGTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIREL
ADEYCGGRWLALGGGGYNPDVVARAWALLWAVL
>gnl|CDD|212521 cd09996, HDAC_classII_1, Histone deacetylases and histone-like deacetylases, classII. This subfamily includes bacterial as well as eukaryotic Class II histone deacetylase (HDAC) and related proteins. Deacetylases of class II are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. Included in this family is a bacterial HDAC-like amidohydrolase (Bordetella/Alcaligenes species FB18817, denoted as FB188 HDAH) shown to be most similar in sequence and function to class II HDAC6 domain 3 or b (HDAC6b). FB188 HDAH is able to remove the acetyl moiety from acetylated histones, and can be inhibited by common HDAC inhibitors such as SAHA (suberoylanilide hydroxamic acid) as well as class II-specific but not class I specific inhibitors
TGFVWDERYLWHDTGTGALFLPVGGLLVQPGRHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELL
RVHTPEYIDRVKAASAAGGGEAGGGTPFGPGSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPGHHAE
PDQGMGFCLFNNVAIAARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQDRCFPPDSGAV
EERGEGAGEGYNLNIPLPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLGRMMLTSDGF
RALTRKLRDLADELCGGRLVMVHEGGYSEAYVPFCGLAVLEELSGVRTGIADPLLYYPEAQGGQELQPHQ
RAAIDAAAA
>gnl|CDD|212522 cd09998, HDAC_Hos3, Class II histone deacetylases Hos3 and related proteins. Fungal histone deacetylase Hos3 from Saccharomyces cerevisiae is a Zn-dependent enzyme belonging to HDAC class II. It catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Hos3 deacetylase is homodimer, in vitro it shows specificity to H4, H3 and H2A
QDECYKHRYSRSKTSKSYLSTIVERPERLRASVLGLSAAVHGSKWSAELIEMCDMAEAKLAKGESEIPAH
LPQGDLYLCPESLDAIQGALGAVCEAVDSVFKPESPGTKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGA
AHAYLTHGITRVVILDIDLHHGNGTQDIAWRINAEANKQALESSSYDDFKPAGAPGLRIFYSSLHDINSF
PCEDGDPAKVKDASVSIDGAHGQWIWNVHLQPWTTEEDFWELYYPKYRILFEKAAEFLRLTTAATPFKTL
VFISAGFDASEHEYESMQRHGVNVPTSFYYRFARDAVRFADAHAHGRLISVLEGGYSDRALCSGVLAHLT
GLA
>gnl|CDD|212523 cd09999, Arginase-like_1, Arginase-like amidino hydrolase family. This family includes arginase, also known as arginase-like amidino hydrolase family, as well as arginase-like proteins and are found in bacteria, archaea and eykaryotes, but does not include metazoan arginases. Arginase is a binuclear Mn-dependent metalloenzyme and catalyzes hydrolysis of L-arginine to L-ornithine and urea (Arg, EC 3.5.3.1), the reaction being the fifth and final step in the urea cycle, providing the path for the disposal of nitrogenous compounds. Arginase controls cellular levels of arginine and ornithine which are involved in protein biosynthesis, and in production of creatine, polyamines, proline and nitric acid
LRLVAPQWQGGNPPNPGYVLGAELLAWLLPESADETVEVPVPPDPAPLDPETGIIGRSALLAQLRAAADI
IEAALPDRPVVLGGDCSVSLAPFAYLARKYGDLGLLWIDAHPDFNTPETSPTGYAHGMVLAALLGEGDPE
LTAIVKPPLSPERVVLAGLRDPDDEEEEFIARLGIRVLRPEGLAASAQAVLDWLKEEGLSGVWIHLDLDV
LDPAIFPAVDFPEPGGLSLDELVALLAALAASADLVGLTIAEFDPDLDWDAINLKNLLDALP
>gnl|CDD|212524 cd10000, HDAC8, Histone deacetylase 8 (HDAC8). HDAC8 is a Zn-dependent class I histone deacetylase that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. HDAC8 is found in human cytoskeleton-bound protein fraction and insoluble cell pellets. It plays a crucial role in intramembraneous bone formation; germline deletion of HDAC8 is detrimental to skull bone formation. HDAC8 is possibly associated with the smooth muscle actin cytockeleton and may regulate the contractive capacity of smooth muscle cells. HDAC8 is also involved in the metabolic control of the estrogen receptor related receptor (ERR)-alpha/peroxisome proliferator activated receptor (PPAR) gamma coactivator 1 alpha (PGC1-alpha) transcriptional complex as well as in the development of neuroblastoma and T-cell lymphoma. HDAC8-selective small-molecule inhibitors could be a therapeutic drug option for these diseases
VVYIHSPEYVNLCDRLPKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNE
GDNDEEPSEQQEFGLGYDCPIFEGIYDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFC
YVNDIVLGILKLREKFDRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPGFFPGTGDVSDVGLGKGK
YYTVNVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLG
WKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPDHEFFTSYGPDYELEISPSLRPDLNEDQYIE
KILETIKGNLKNVV
>gnl|CDD|212525 cd10001, HDAC_classII_APAH, Histone deacetylase class IIa. This subfamily includes bacterial acetylpolyamine amidohydrolase (APAH) as well as other Class II histone deacetylase (HDAC) and related proteins. Deacetylases of class II are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. Mycoplana ramosa APAH exhibits broad substrate specificity and catalyzes the deacetylation of polyamines such as putrescine, spermidine, and spermine by cleavage of a non-peptide amide bond
KIVYSEDHLLHHPKTELSRGKLVPHPENPERAEAILDALKRAGLGEVLPPRDFGLEPILAVHDPDYVDFL
ETADTDTPISEGTWEAALAAADTALTAADLVLEGERAAYALCRPPGHHAGRDRAGGFCYFNNAAIAAQYL
RDRAGRVAILDVDVHHGNGTQEIFYERPDVLYVSIHGDPRTFYPFFLGFADETGEGEGEGYNLNLPLPPG
TGDDDYLAALDEALAAIAAFGPDALVVSLGFDTHEGDPLSDFKLTTEDYARIGRRIAALGLPTVFVQEGG
YNVDALGRNAVAFLAGFE
>gnl|CDD|212526 cd10002, HDAC10_HDAC6-dom1, Histone deacetylase 6, domain 1 and histone deacetylase 10. Histone deacetylases 6 and 10 are class IIb Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDACs usually act via association with DNA binding proteins to target specific chromatin regions. HDAC6 is the only histone deacetylase with internal duplication of two catalytic domains which appear to function independently of each other, and also has a C-terminal ubiquitin-binding domain. It is located in the cytoplasm and associates with microtubule motor complex, functioning as the tubulin deacetylase and regulating microtubule-dependent cell motility. HDAC10 has an N-terminal deacetylase domain and a C-terminal pseudo-repeat that shares significant similarity with its catalytic domain. It is located in the nucleus and cytoplasm, and is involved in regulation of melanogenesis. It transcriptionally down-regulates thioredoxin-interacting protein (TXNIP), leading to altered reactive oxygen species (ROS) signaling in human gastric cancer cells. Known interaction partners of HDAC6 are alpha tubulin (substrate) and ubiquitin-like modifier FAT10 (also known as Ubiquitin D or UBD) while interaction partners of HDAC10 are Pax3, KAP1, hsc70 and HDAC3 proteins
CNWDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESLC
SGYDSVYLCPSTYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYA
IEKLGLKRILIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVP
LNQTGLGDADYLAIFHHILLPLALEFQPELVLVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKL
LLVLEGGYLLESLAESVSMTLRGLLGDPLPPLAPPIPIRSVLETILNAIAHLSPRW
>gnl|CDD|212527 cd10003, HDAC6-dom2, Histone deacetylase 6, domain 2. Histone deacetylase 6 is a class IIb Zn-dependent enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDACs usually act via association with DNA binding proteins to target specific chromatin regions. HDAC6 is the only histone deacetylase with internal duplication of two catalytic domains which appear to function independently of each other, and also has a C-terminal ubiquitin-binding domain. It is located in the cytoplasm and associates with microtubule motor complex, functioning as the tubulin deacetylase and regulating microtubule-dependent cell motility. Known interaction partners of HDAC6 are alpha tubulin and ubiquitin-like modifier FAT10 (also known as Ubiquitin D or UBD)
YDQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKM
KPRELNRLGKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFN
NVAIAARYAQKKYGLKRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGK
GEGFNVNIPWNKGGMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHM
LMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPPPVLDLPRPPCSSALKSINNVLQVHQKYWKSLR
>gnl|CDD|212528 cd10004, RPD3-like, reduced potassium dependency-3 (RPD3)-like. Proteins of the Rpd3-like family are class I Zn-dependent Histone deacetylases that catalyze hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). RPD3 is the yeast homolog of class I HDACs. The main function of RPD3-like group members is regulation of a number of different processes through protein (mostly different histones) modification (deacetylation). This group includes fungal RPD3 and acts via the formation of large multiprotein complexes. Members of this group are involved in cell cycle regulation, DNA damage response, embryonic development and cytokine signaling important for immune response. Histone deacetylation by yeast RPD3 represses genes regulated by the Ash1 and Ume6 DNA-binding proteins. In mammals, they are known to be involved in progression of various tumors. Specific inhibitors of mammalian histone deacetylases could be a therapeutic drug option
KKKVAYFYDSDVGNYAYGPGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLS
RVTPDNMEKFQKEQVKYNVGDDCPVFDGLFEFCSISAGGSMEGAARLNRGKCDIAVNWAGGLHHAKKSEA
SGFCYVNDIVLGILELLRYHQRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEYFPGTGELRDIGIG
TGKNYAVNVPLRDGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNF
VKSFNLPMLVLGGGGYTMRNVARTWAFETGLLAGEELDKDLPYNEYYEYYGPDYELNVRPSNMENHNTPE
YLDKITTAVIENLRNTSFAPSVQMQ
>gnl|CDD|212529 cd10005, HDAC3, Histone deacetylase 3 (HDAC3). HDAC3 is a Zn-dependent class I histone deacetylase that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. In order to target specific chromatin regions, HDAC3 can interact with DNA-binding proteins (transcriptional factors) either directly or after forming complexes with a number of other proteins, as observed for the SMPT/N-CoR complex which recruits human HDAC3 to specific chromatin loci and activates deacetylation. Human HDAC3 is also involved in deacetylation of non-histone substrates such as RelA, SPY and p53 factors. This protein can also down-regulate p53 function and subsequently modulate cell growth and apoptosis. This gene is therefore regarded as a potential tumor suppressor gene. HDAC3 plays a role in various physiological processes, including subcellular protein localization, cell cycle progression, cell differentiation, apoptosis and survival. HDAC3 has been found to be overexpressed in some tumors including leukemia, lung carcinoma, colon cancer and maxillary carcinoma. Thus, inhibitors precisely targeting HDAC3 (in some cases together with retinoic acid or hyperthermia) could be a therapeutic drug option
KRVAYFYDPDVGNFHYGPGHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQR
VTPQNIQGFTKSLNQFNVGDDCPVFPGLFDFCSMYTGASLEGATKLNHKICDIAINWSGGLHHAKKFEAS
GFCYVNDIVIAILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAE
SGRYYSVNVPLKDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEF
VKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNELPYNEYFEYFAPDFTLHPDVSTRIENQNSK
QYLDQIRQTVFENLKMLNHAPSVQMQDVPPD
>gnl|CDD|212530 cd10006, HDAC4, Histone deacetylase 4. Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, having N-terminal regulatory domain with two or three conserved serine residues; phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC4 participates in regulation of chondrocyte hypertrophy and skeletogenesis. However, biological substrates for HDAC4 have not been identified; only low lysine deacetylation activity has been demonstrated and active site mutant has enhanced activity toward acetylated lysines. HDAC4 does not bind DNA directly, but through transcription factors MEF2C (myocyte enhancer factor-2C) and MEF2D. Other known interaction partners of the protein are 14-3-3 proteins, SMRT and N-CoR co-repressors, BCL6, HP1, SUMO-1 ubiquitin-like protein, and ANKRA2. It appears to interact in a multiprotein complex with RbAp48 and HDAC3. Furthermore, HDAC4 is required for TGFbeta1-induced myofibroblastic differentiation
KPRFTTGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEA
HTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATG
ELKNGFAVVRPPGHHAEESTPMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVL
YMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVL
VSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELD
PLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGYSLIEAQTCENEEAETVT
>gnl|CDD|212531 cd10007, HDAC5, Histone deacetylase 5. Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, having N-terminal regulatory domain with two or three conserved serine residues; phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC5 is involved in integration of chronic drug (cocaine) addiction and depression with changes in chromatin structure and gene expression; cocaine regulates HDAC5 function to antagonize the rewarding impact of cocaine, possibly by blocking drug-stimulated gene expression that supports drug-induced behavioral change. It is also involved in regulation of angiogenesis and cell cycle as well as immune system development. HDAC5 and HDAC9 have been found to be significantly up-regulated in high-risk medulloblastoma compared with low-risk and may potentially be novel drug targets
HLFTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHH
TLLYGTSPLNRQKLDSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAG
ELKNGFAVIRPPGHHAEESTAMGFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVL
YISLHRYDDGNFFPGSGAPDEVGAGPGVGFNVNIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVL
VSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLGMELT
PLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRGELEEAETVSAMASLSVDTEQ
>gnl|CDD|212532 cd10008, HDAC7, Histone deacetylase 7. Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, having N-terminal regulatory domain with two or three conserved serine residues; phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC7 is involved in regulation of myocyte migration and differentiation. Known interaction partners of class IIa HDAC7 are myocyte enhancer factors - MEF2A, -2C, and -2D, 14-3-3 proteins, SMRT and N-CoR co-repressors, HDAC3, ETA (endothelin receptor). This enzyme is also involved in the development of the immune system as well as brain and heart development. Multiple alternatively spliced transcript variants encoding several isoforms have been found for this gene
FTTGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVL
LYGTNPLSRLKLDNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASREL
KNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYI
SLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVS
AGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGNEVDPL
SEESWKQKPNLNAIRSLEAVIRVHSKYW
>gnl|CDD|212533 cd10009, HDAC9, Histone deacetylase 9. Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, they have N-terminal regulatory domain with two or three conserved serine residues, phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC9 is involved in regulation of gene expression and dendritic growth in developing cortical neurons. It also plays a role in hematopoiesis. Its deregulated expression may be associated with some human cancers. HDAC5 and HDAC9 have been found to be significantly up-regulated in high-risk medulloblastoma compared with low-risk and may potentially be novel drug targets
SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSL
LYGTNPLDGQKLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGEL
KNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYI
SLHRYDEGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVS
AGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACVNALLGNELEPL
AEDILHQSPNMNAVISLQKIIEIQSKYWK
>gnl|CDD|212534 cd10010, HDAC1, Histone deacetylase 1 (HDAC1). Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDAC1 is involved in regulation through association with DNA binding proteins to target specific chromatin regions. In particular, HDAC1 appears to play a major role in pre-implantation embryogenesis in establishing a repressive chromatin state. Its interaction with retinoblastoma tumor-suppressor protein is essential in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2 (MTA2), it deacetylates p53, thereby modulating its effect on cell growth and apoptosis. It participates in DNA-damage response, along with HDAC2; together, they promote DNA non-homologous end-joining. HDAC1 is also involved in tumorogenesis; its overexpression modulates cancer progression. Specific inhibitors of HDAC1 are currently used in cancer therapy
SQGTKKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYI
KFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSAGGSVASAVKLNKQQTDIAVNWAGGLHHAK
KSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRD
IGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAK
CVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSEIPNELPYNDYFEYFGPDFKLHISPSNMTNQ
NTNEYLEKIKQRLFENLRMLP
>gnl|CDD|212535 cd10011, HDAC2, Histone deacetylase 2 (HDAC2). Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDAC2 is involved in regulation through association with DNA binding proteins to target specific chromatin regions. It forms transcriptional repressor complexes by associating with several proteins, including the mammalian zinc-finger transcription factor YY1, thus playing an important role in transcriptional regulation, cell cycle progression and developmental events. Additionally, a few non-histone HDAC2 substrates have been found. HDAC2 plays a role in embryonic development and cytokine signaling important for immune response, and is over-expressed in several solid tumors including oral, prostate, ovarian, endometrial and gastric cancer. It participates in DNA-damage response, along with HDAC1; together, they can promote DNA non-homologous end-joining. HDAC2 is considered an important cancer prognostic marker. Inhibitors specifically targeting HDAC2 could be a therapeutic drug option
KKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLR
SIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEA
SGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAG
KGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEV
VKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPE
YMEKIKQRLFENLRML
>gnl|CDD|193609 cd10013, Cas3''_I, CRISPR/Cas system-associated protein Cas3''. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; HD-like nuclease, specifically digesting double-stranded oligonucleotides and preferably cleaving at G:C pairs; signature gene for Type I
EDHVKGSLEVWEKYLKESYIPIISRRLGVDGELVEELVKKAIILHDIGKAAEYYQNKFDGLSFYGHEVYS
AYYAYKILEEEKDEELRFIIALAVMLHHEAIRMRSLRSEDGEPENFLLPMLELKEELKRVIEKYLGEIIL
NVPPYTRYEVVREVVRLSKRSDKLLKLVYLILLPLVVADNLDASLNRG
>gnl|CDD|199900 cd10014, TFIIA_gamma_C, Gamma subunit of transcription initiation factor IIA, C-terminal domain. Transcription factor II A (TFIIA) is one of the general transcription factors for RNA polymerase II. TFIIA increases the affinity of the TATA-binding protein (TBP) for DNA, in order to assemble the initiation complex. TFIIA also functions as an activator during development and differentiation, and is involved in transcription from TATA-less promoters. TFIIA is composed of more than one subunit in various organisms. Mammalian TFIIA large subunits (TFIIA alpha and beta), and the smaller subunit (TFIIA gamma) form a heterotrimer. TFIIA alpha and beta are encoded by a single TFIIA_alpha_beta gene and post-translationally processed and cleaved. TOA1 and TOA2 are the two subunits of Yeast TFIIA which correspond to Mammalian TFIIA_alpha_beta and TFIIA gamma, respectively. TOA1 and TOA2 form a heterodimeric protein complex. The TFIIA gamma subunit is highly conserved between humans, Drosophila and yeast and it is required for TFIIA function. The C-terminal domain of the gamma (TFIIA_gamma_C) subunit forms a beta-barrel structure together with TFIIA beta
LTFKGHLKTYRFCDNVWTFILNDVEFKESNTEVVTVDKVKIVACDGK
>gnl|CDD|197381 cd10015, BfiI_C_EcoRII_N_B3, DNA binding domains of BfiI, EcoRII and plant B3 proteins. This family contains the N-terminal DNA binding domain of type IIE restriction endonuclease EcoRII-like proteins, the C-terminal DNA binding domain of type IIS restriction endonuclease BfiI-like proteins and plant-specific B3 proteins. Type II restriction endonucleases are components of restriction modification (RM) systems that protect bacteria and archaea against invading foreign DNA. They usually function as homodimers or homotetramers that cleave DNA at defined sites of 4 to 8 bp in length, and they require Mg2+, not ATP or GTP, for catalysis. EcoRII is specific for the 5'-CCWGG sequence (W stands for A or T). EcoRII consists of 2 domains, the C-terminal catalytic/dimerization domain (EcoRII-C), and the N-terminal effector DNA binding domain (EcoRII-N). BfiI is unique in cleaving DNA at fixed positions downstream of an asymmetric sequence in the absence of Mg2+. BfiI consists of two discrete domains with distinct functions: an N-terminal catalytic domain with non-specific nuclease activity and dimerization function that is more closely related to Nuc, an EDTA-resistant nuclease from the phospholipase D (PLD) superfamily; and a C-terminal domain that specifically recognizes its target sequences, 5'-ACTGGG-3'. B3 proteins are a family of plant-specific transcription factors, involved in a great variety of processes, including seed development and auxin response
VVLIKRLSANDTGATGGHQVGLYIPKGIVEKFPPSINHTREANPSIFLTMHDISDCRDWEARAIFYNSNR
NEKRLTRGGRGFVKQNPLNTGDLTLIAFDLDKEYNIRIC
>gnl|CDD|197382 cd10016, EcoRII_N, N-terminal domain of type IIE restriction endonuclease EcoRII and similar proteins. N-terminal domain of type IIE restriction endonuclease EcoRII and similar proteins. Type II restriction endonucleases are components of restriction modification (RM) systems that protect bacteria and archaea against invading foreign DNA. They usually function as homodimers or homotetramers that cleave DNA at defined sites of 4 to 8 bp in length, and they require Mg2+, not ATP or GTP, for catalysis. EcoRII is specific for the 5'-CCWGG sequence (W stands for A or T). EcoRII consists of 2 domains, the C-terminal catalytic/dimerization domain (EcoRII-C), and the N-terminal effector DNA binding domain (EcoRII-N). To be catalytically active, EcoRII has to form a dimer
MSIQVYCKRLSANDTGATGGHQAGIYIPKSAAELLFPSNHPDEKNPNPDLTAKISSHDGPTTESRFIYYN
NGLFGGTRNEYRITRFGKGFPFLDPDNTGALLVLAFQSSDCDLYSVWVCRSDEEEDEFEAEIEVLPGALN
LL
>gnl|CDD|197383 cd10017, B3_DNA, Plant-specific B3-DNA binding domain. The plant-specific B3 DNA binding domain superfamily includes the well-characterized auxin response factor (ARF) and the LAV (Leafy cotyledon2 [LEC2]-Abscisic acid insensitive3 [ABI3]-VAL) families, as well as the RAV (Related to ABI3 and VP1) and REM (REproductive Meristem) families. LEC2 and ABI3 have been shown to be involved in seed development, while other members of the LAV family seem to have a more general role, being expressed in many organs during plant development. Members of the ARF family bind to the auxin response element and depending on presence of an activation or repression domain, they activate or repress transcription. RAV and REM families are less studied B3 protein famillies
PLFFKVLTPSDVSSLGRLVLPKKFAKAHLPPKEGVEVTLEDPDGKKWTVKLKKRKNSGRMVLSGGWKEFV
RANGLKEGDFLVFELDGRNSKFKVRIFR
>gnl|CDD|197384 cd10018, BfiI_C, C-terminal domain of type IIs restriction endonuclease BfiI and similar proteins. C-terminal domain of a novel type IIs restriction endonuclease BfiI and similar proteins. Type II restriction endonucleases are components of restriction modification (RM) systems that protect bacteria and archaea against invading foreign DNA. They usually function as homodimers or homotetramers that cleave DNA at defined sites of 4 to 8 bp in length, and they require Mg2+, not ATP or GTP, for catalysis. Unlike all other restriction enzymes known to date, BfiI is unique in cleaving DNA at fixed positions downstream of an asymmetric sequence in the absence of Mg2+. BfiI consists of two discrete domains with distinct functions: an N-terminal catalytic domain with non-specific nuclease activity and dimerization function that is more closely related to Nuc, an EDTA-resistant nuclease from the phospholipase D (PLD) superfamily; and a C-terminal domain that specifically recognizes its target sequences, 5'-ACTGGG-3'. BfiI presumably evolved through domain fusion of a DNA recognition domain to the catalytic Nuc-like domain from the PLD superfamily. BfiI forms a functionally active homodimer which has two DNA-binding surfaces located at the C-terminal domains but only one active site, located at the dimer interface between the two N-terminal catalytic domains
VTMILTLGHADTARIQAAPGTTAGKGTQYFWLSKDSYDFFPPLTIRNRRGTKATYSCLINMNYIDINYID
TQCRVTFEAENNLDFRLGTGKLRYTGVAKSGDLAAITRVGESDYELRIIKQGTAEYSALDPYAVNFIGNQ
GKRFGYISNEEFGRIIG
>gnl|CDD|206756 cd10019, 14-3-3_sigma, 14-3-3 sigma, an isoform of 14-3-3 protein. 14-3-3 protein sigma isoform, also known as stratifin or human mammary epithelial marker (HME) 1, has been most directly linked to tumor development. In humans, it is expressed by the SFN gene, strictly in stratified squamous epithelial cells in response to DNA damage where it is transcriptionally induced in a p53-dependent manner, subsequently causing cell-cycle arrest at the G2/M checkpoint. Up-regulation and down-regulation of 14-3-3 sigma expression have both been described in tumors. For example, in human breast cancer, 14-3-3 sigma is predominantly down-regulated by CpG methylation, acting as both a tumor suppressor and a prognostic indicator, while in human scirrhous-type gastric carcinoma (SGC), it is up-regulated and may play an important role in SGC carcinogenesis and progression. Loss of 14-3-3 sigma expression sensitizes tumor cells to treatment with conventional cytostatic drugs, making this protein an attractive therapeutic target. 14-3-3 domains are an essential part of 14-3-3 proteins, a ubiquitous class of regulatory, phosphoserine/threonine-binding proteins found in all eukaryotic cells, including yeast, protozoa and mammalian cells
MERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSNEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSN
EEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDK
KRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSE
DSYKDSTLIMQLLRDNLTLWTADNAGEEGGEA
>gnl|CDD|206757 cd10020, 14-3-3_epsilon, 14-3-3 epsilon, an isoform of 14-3-3 protein. 14-3-3 protein epsilon isoform (isoform (also known as tyrosine 3-monooxygenase/ tryptophan 5-monooxygenase activation protein, epsilon polypeptide) is encoded by the YWHAE gene in humans and is involved in cancer cell survival and growth. It interacts with CDC25 phosphatases, RAF1 and IRS1 proteins, suggesting its role in diverse biochemical activities related to signal transduction, such as cell division and regulation of insulin sensitivity. Overexpression of 14-3-3 epsilon in primary hepatocellular carcinoma (HCC) tissues predicts a high risk of extrahepatic metastasis and worse survival, and is a potential therapeutic target. It has also been implicated in the pathogenesis of small cell lung cancer. 14-3-3 epsilon overexpression protects colorectal cancer and endothelial cells from oxidative stress-induced apoptosis, while its suppression by non-steroidal anti-inflammatory drugs induces cancer and endothelial cell death. Cellular levels of 14-3-3 epsilon could possibly serve as an important regulator of cell survival in response to oxidative stress and other death signals. 14-3-3 domains are an essential part of 14-3-3 proteins, a ubiquitous class of regulatory, phosphoserine/threonine-binding proteins found in all eukaryotic cells, including yeast, protozoa and mammalian cells
REDNVYKAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENK
GGEDKLKMIREYRQQVEKELKDICNDILDVLDKHLIPAANSGESKVFYYKMKGDYHRYLAEFATGNDRKE
AAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEES
YKDSTLIMQLLRDNLTLWTS
>gnl|CDD|206758 cd10022, 14-3-3_beta_zeta, 14-3-3 beta and zeta isoforms of 14-3-3 protein. 14-3-3 protein beta and zeta isoform (also known as tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, beta and zeta polypeptide) are encoded by the YWHAB gene and YWHAZ gene in humans. They have been linked to mitogenic signaling and the cell cycle machinery, and to cancer initiation and progression, respectively. The beta isoform has been shown to interact with RAF1 and CDC25 phosphatases and its overexpression is associated with invasion, migration, metastasis and proliferation of tumor cells and its elevated levels are correlated with tumor size, the number of lymph node metastases and a reduced survival rate. It is significantly overexpressed in lung cancer tissues, mutated chronic lymphocytic leukemia (M-CLL), gastric cancer tissues, aflatoxin B1-induced rat hepatocellular carcinoma K1 and K2 cells, as well as renal cell carcinoma cysts, and can potentially be used as a diagnostic and prognostic biomarker in the cancer. Numerous proteins involved in anti-apoptosis and tumor progression were also found to be differentially expressed in gastric cancer cells where 14-3-3 beta is overexpressed. 14-3-3 beta also interacts with human Dapper1 (hDpr1), a key negative regulator of Wnt signaling, via hDpr1 phosphorylation by protein kinase A, thus attenuating the ability of hDpr1 to promote Dishevelled (Dvl) degradation, and subsequently enhancing Wnt signaling. The zeta isoform is ubiquitously expressed and localized to most subcellular regions, including the cytoplasm, plasma membrane, mitochondria, and nucleus. Its overexpression and gene amplification in multiple cancers are correlated with poor prognosis and chemoresistance in cancer patients. 14-3-3 zeta has been identified as a biomarker with high sensitivity and specificity for diagnosis and prognosis in multiple tumor types, including hepatocellular carcinoma, head and neck cancer, indicating a potential clinical application for using 14-3-3 zeta in selecting treatment options and predicting cancer outcome. It also interacts with IRS1 protein, suggesting a role in regulating insulin sensitivity. 14-3-3 domains are an essential part of 14-3-3 proteins, a ubiquitous class of regulatory, phosphoserine/threonine-binding proteins found in all eukaryotic cells, including yeast, protozoa and mammalian cells
DKNELVQKAKLAEQAERYDDMAACMKAVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEG
AEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGI
VEQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESY
KDSTLIMQLLRDNLTLWTS
>gnl|CDD|206759 cd10023, 14-3-3_theta, 14-3-3 theta/tau (theta in mice, tau in human), an isoform of 14-3-3 protein. 14-3-3 tau/theta (tau in humans, theta in mice) isoform (also known as tyrosine 3-monooxygenase/ tryptophan 5-monooxygenase activation protein, theta polypeptide) is encoded by the YWHAQ gene in humans and plays an important role in controlling apoptosis through interactions with ASK1, c-jun NH-terminal kinase, and p38 mitogen-activated protein kinase (MAPK). Its interaction with CDC25c regulates entry into the cell cycle and subsequent interaction with Bad prevents apoptosis. 14-3-3 theta protein expression is induced in patients with amyotrophic lateral sclerosis. 14-3-3 tau is often overexpressed in breast cancer, which is associated with the downregulation of p21, a p53 target gene, and thus leads to tamoxifen resistance in MCF7 breast cancer cells and shorter patient survival. Therefore, 14-3-3 tau may be a potential therapeutic target in breast cancer. Additionally, 14-3-3 theta mediates nucleocytoplasmic shuttling of the coronavirus nucleocapsid protein which causes severe acute respiratory syndrome. 14-3-3 domain is an essential part of 14-3-3 proteins, a ubiquitous class of regulatory, phosphoserine/threonine-binding proteins found in all eukaryotic cells, including yeast, protozoa and mammalian cells
MDKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTD
TSDKKLQLVKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQ
TIENSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDS
YKDSTLIMQLLRDNLTLWTSDSAG
>gnl|CDD|206760 cd10024, 14-3-3_gamma, 14-3-3 gamma, an isoform of 14-3-3 protein. 14-3-3 gamma isoform (also known as tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide) is encoded by the YWHAG gene in humans and is induced by growth factors in human vascular smooth muscle cells. It is also highly expressed in skeletal and heart muscles, suggesting an important role in muscle tissue. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways. 14-3-3 gamma mediates Cdc25A proteolysis to block premature mitotic entry after DNA damage. 14-3-3 gamma mediates the interaction between Chk1 and Cdc25A; this complex has an essential function in Cdc25A phosphorylation and degradation to block premature mitotic entry after DNA damage. Increased expression of 14-3-3 gamma in lung cancer coincides with loss of functional p53, possibly in a cooperative manner promoting genomic instability. Also, during cell cycle, 14-3-3 gamma protects p21, a cyclin-dependent kinase inhibitor, from degradation mediated by the p53 suppressor MDMX, which may account for elevation of p21 levels independent of p53 and in response to DNA damage. Elevated expression of 14-3-3 gamma in human hepatocellular carcinoma predicts extrahepatic metastasis and worse survival, thus making this protein a candidate biomarker and a potential target for novel therapies against the disease
VDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTS
ADGNEKKIEMVRAYREKIEKELETVCQDVLSLLDNFLIKNCSETQYESKVFYLKMKGDYYRYLAEVATGE
KRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTL
NEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGGEGNN
>gnl|CDD|206761 cd10025, 14-3-3_eta, 14-3-3 eta, an isoform of 14-3-3 protein. 14-3-3 eta isoform (also known as tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, eta polypeptide) is expressed mainly in brain, and is involved in hypothalamic-pituitary-adrenocortical (HPA) axis regulation. In humans, it is encoded by the YWHAH gene, and is a positional and functional candidate for schizophrenia as well as bipolar disorder (BP). This gene contains a 7 bp repeat sequence in its 5' Untranslated Region (UTR), and early-onset schizophrenia has been associated with changes in the number of this repeat. 14-3-3 eta and gamma are found in the serum and synovial fluid of patients with joint inflammation. Specifically, 14-3-3 eta, which plays a regulatory role in chondrogenic differentiation, is significantly overexpressed in juvenile rheumatoid arthritis (JRA), a chronic inflammatory disease often associated with growth impairment. Overexpression of Gremlin 1, the bone morphogenetic protein antagonist, may play an oncogenic role in carcinomas of the uterine cervix, lung, ovary, kidney, breast, colon, pancreas, and sarcoma, since it functions by interaction with the 14-3-3 eta domain. Therefore, Gremlin 1 and its binding protein 14-3-3 eta could be appropriate targets for developing diagnostic and therapeutic strategies against human cancers. 14-3-3 domain is an essential part of 14-3-3 proteins, a ubiquitous class of regulatory, phosphoserine/threonine-binding proteins found in all eukaryotic cells, including yeast, protozoa and mammalian cells
DREQLLQRARLAEQAERYDDMASAMKSVTELNEPLSNEDRNLLSVAYKNVVGARRSSWRVISSIEQKTMA
DGNEKKLEKVKAYREKIEKELETVCNDVLALLDKFLIKNCNDFQYESKVFYLKMKGDYYRYLAEVASGEK
KNSVVEASEAAYKEAFEISKEHMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLN
EDSYKDSTLIMQLLRDNLTLWTSDQQDEE
>gnl|CDD|206762 cd10026, 14-3-3_plant, Plant 14-3-3 protein domain. Plant 14-3-3 isoforms, similar to their highly conserved homologs in mammals, bind to phosphorylated target proteins to modulate their function. They have been implicated in a variety of physiological functions; in particular, abiotic and biotic stress responses, primary metabolism, as well as various aspects of plant growth and development. They function through the regulation of a diverse range of proteins including transcription factors, kinases, structural proteins, ion channels as well as pathogen defense-related proteins. The 14-3-3 proteins are affected transcriptionally as well as functionally by the environment of the plant, both intracellular and extracellular, thus playing a key role in the response to environmental stress, pathogens and light conditions. Plant 14-3-3 proteins have been divided into epsilon-like groups and non-epsilon groups based on phylogenetic clustering. They have a varying number of isoforms (for example, Arabidopsis has thirteen known protein isoforms, cotton has six) with variation in their affinity for specific binding partners, suggesting specific roles in specific processes
REENVYMAKLAEQAERYDEMVEFMEKVAKSVDSEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEE
SKGNEEHVNSIREYRSKVENELSKICDGILKLLDAHLIPSAASGESKVFYLKMKGDYHRYLAEFKTGAER
KEAAESTLLAYKAAQDIALTELAPTHPIRLGLALNFSVFYYEILNSPDRACTLAKQAFDEAIAELDTLGE
ESYKDSTLIMQLLRDNLTLWTSDMQDE
>gnl|CDD|381678 cd10027, UDG-F1-like, Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar proteins. Uracil DNA glycosylase family 1 is the most efficient of all uracil-DNA glycosylases (UDGs, also known as UNGs) and shows a specificity for uracil in DNA. UDG catalyzes the removal of uracil from DNA to initiate the DNA base excision repair pathway. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. Uracil mispaired with guanine in DNA is one of the major pro-mutagenic events, causing G:C-_A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other
YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSL
RNIFKELKSDLGIFPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVV
FLLWGNHAQKKKKLIDKKKHLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW
>gnl|CDD|381679 cd10028, UDG-F2_TDG_MUG, Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil DNA glycosylase and similar proteins. Uracil DNA glycosylase family 2 consists of thymine DNA glycosylase (TDG), which removes uracil and thymine from G:U and G:T mismatches in double-stranded DNA. It includes mismatch-specific uracil DNA glycosylase (MUG), the prokaryotic homolog of TDG. Escherichia coli MUG is highly specific to G:U mismatches but also repairs G:T mismatches at high enzyme concentration. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C-_A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other
LPDLLAPGLDVLFCGINPGLRSAAVGHHYAHPGNRFWPLLHESGLTPRLLTPEEDRRLPEYGIGLTNLVK
RPTASAAELSKAELRAGVPRLLAKIARYRPRVVAFVGKGAYRAFFGRLKKKAAYGLQPETGIGGTRVFVL
PSTSGLNAHYSLEDKLEPWRELA
>gnl|CDD|381680 cd10030, UDG-F4_TTUDGA_SPO1dp_like, Uracil DNA glycosylase family 4, includes Thermotoga maritima TTUDGA, Bacillus phage SPO1 DNA polymerase, and similar proteins. Uracil DNA glycosylase family 4 includes Thermotoga maritima TTUDGA, a robust uracil DNA glycosylase that shares narrow substrate specificity and high catalytic efficiency with family 1, acting on double-stranded and single-stranded uracil-containing DNA. Members of this family possess four conserved cysteine residues required to coordinate the [4Fe-4S] iron-sulfur cluster. This family also includes the N-terminal domain of Bacillus phage SPO1 DNA polymerase. Bacteriophage SPO1 is one of a group of large, lytic, tailed bacteriophages of Bacillus subtilis, and contains hydroxymethyluracil (hmUra) in place of thymine in their DNA. It has been speculated that this UDG domain may help discriminate between hmUra containing SPO1 DNA and thymine-containing host DNA. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C-_A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other
CTRCPLSKTRTNVVFGEGNPDAKLMFIGEAPGAEEDRQGRPFVGRAGKLLDKMLAAIGLSREDVYITNVV
KCRPPGNRTPTPEEIAACRPFLDRQIELIKPKVIVTLGRTAAQALLGKDAPISKLRGKWHEYEKGIPVLP
TYHPAALLRNPSLKRLAWEDLKKLK
>gnl|CDD|381681 cd10031, UDG-F5_TTUDGB_like, Uracil DNA glycosylase family 5, includes Thermotoga maritima TTUDGB and similar proteins. Uracil DNA glycosylase family 5 includes Thermus thermophilus HB8 TTUDGB (also called UDGb) which is not only a UDG acting on double-stranded uracil-containing DNA, but also a hypoxanthine DNA glycosylase acting on double-stranded hypoxanthine-containing DNA (except for the C/I base pair), as well as a xanthine DNA glycosylase acting on both, double-stranded and single-stranded xanthine-containing DNA. TTUDGB also excises thymine from G:T mismatched DNA, and removes analogs of uracil from DNA, including 5-hydroxymethyluracil (hmU) and 5-fluorouracil (fU). This subfamily also contains Bradyrhizobium diazoefficiens family 5 homolog Blr5068 (UdgB) which has been found to efficiently excise uracil from ssDNA and dsDNA. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Similar to family 4 UDGs, members of this family possess four conserved cysteine residues required to coordinate the [4Fe-4S] iron-sulfur cluster. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C-_A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other
CRRCPRLVAYREEVAKKKRRFRDPDYWGKPVPGFGDPNARLLIVGLAPAAHGGNRTGRPFTGDRSGDFLY
RALYEAGFANQPTSESRDDGLELKDCYITAAVRCAPPQNKPTPEEIRNCRPFLEEELALLKNLKVILALG
RIAFDAVLRALGLKLKDPKFGHGAVYRLPNGITLVASYHPSRQNTNTGRLTEEMFDEVFRRAKE
>gnl|CDD|381682 cd10032, UDG-F6_HDG, Uracil DNA glycosylase family 6, includes hypoxanthine-DNA glycosylase and similar proteins. Uracil DNA glycosylase family 6 hypoxanthine-DNA glycosylase (HDG) lacks any detectable UDG activity; it excises hypoxanthine, a deamination product of adenine, from double-stranded DNA. Uracil-DNA glycosylase (UDGs) initiates repair of uracils in DNA. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C-_A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other
HGFPPVVDENSRVLILGSFPSVKSLEAQFYYGHPRNRFWRILGALFGEDLKALDYEERKAFLLEHGIALW
DVLASCRRKGSLDSAIRNVEPNDIAGLLAKAPNIKAIIFNGKKAARLFKKYVAPLRGIETLRLPSTSPAN
A
>gnl|CDD|381683 cd10033, UDG_like, uncharacterized family of the uracil-DNA glycosylase superfamily. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil may arise from mis-incorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C-_A:T mutations; thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other. UDG family 1 is the most efficient uracil-DNA glycosylase (UDG, also known as UNG) and shows a specificity for uracil in DNA. UDG family 2 includes thymine DNA glycosylase which removes uracil and thymine from G:U and G:T mismatches, and mismatch-specific uracil DNA glycosylase (MUG) which in Escherichia coli is highly specific to G:U mismatches but also repairs G:T mismatches at high enzyme concentration. UDG family 3 includes Human SMUG1 which can remove uracil and its oxidized pyrimidine derivatives from, single-stranded DNA and double-stranded DNA with a preference for single-stranded DNA. Pedobacter heparinus SMUG2, which is UDG family 3 SMUG1-like, displays catalytic activities towards DNA containing uracil or hypoxanthine/xanthine. UDG family 4 includes Thermotoga maritima TTUDGA, a robust UDG which like family 1, acts on double-stranded and single-stranded uracil-containing DNA. UDG family 5 (UDGb) includes Thermus thermophilus HB8 TTUDGB which acts on double-stranded uracil-containing DNA; it is a hypoxanthine DNA glycosylase acting on double-stranded hypoxanthine-containing DNA except for the C/I base pair, as well as a xanthine DNA glycosylase which acts on both double-stranded and single-stranded xanthine-containing DNA. UDG family 6 hypoxanthine-DNA glycosylase lacks any detectable UDG activity; it excises hypoxanthine. Other UDG families include one represented by Bradyrhizobium diazoefficiens Blr0248 which prefers single-stranded DNA and removes uracil, 5-hydroxymethyl-uracil or xanthine from it
PLGPRPVFQGSPNAKILIIGQAPGRKVHESGIPFNDASGKRLREWLGVSDETFYDPDRFAILPMGFCYPG
KGKGGDLPPRKECAPTWHPRLLELLPNPELTILIGRYAQKYYLPKRRKKLLTLTVKNWREYGPKYFPLPH
PSPRNNRWLKKNPWFEEEVLPELRKRVRAIL
>gnl|CDD|381684 cd10034, UDG_BdiUng_like, Uracil DNA glycosylase family which includes Bradyrhizobium diazoefficiens Blr0248 (BdiUng) and similar proteins. Bradyrhizobium diazoefficiens (previously B. japonicum) Blr0248 uracil-DNA glycosylase (BdiUng) has broad substrate specificity, preferring single-stranded DNA and removing uracil, 5-hydroxymethyl-uracil or xanthine from it. BdiUng is impervious to inhibition by AP DNA, and Ugi protein that specifically inhibits conventional family 1 UDGs. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C-_A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other
FASLCAAYPDEDVYPADDFRVEWGPVFYRGRLDGSARVLVIGQDPAQTEAIARRILVGTAGQRVQGFLAK
LGITRSYVMVNAFLYSVYGQFGGARHLNDPAITAYRNRWLDALLAPGPIEAVVAFGALADKAWRAKATPW
GNRPNVPVFHLPHPTAPESSALGTRKKMLDNWNAALAALRP
>gnl|CDD|381685 cd10035, UDG_like, uncharacterized family of the uracil-DNA glycosylase superfamily. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil may arise from misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C-_A:T mutations; thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other. UDG family 1 is the most efficient uracil-DNA glycosylase (UDG, also known as UNG) and shows a specificity for uracil in DNA. UDG family 2 includes thymine DNA glycosylase which removes uracil and thymine from G:U and G:T mismatches, and mismatch-specific uracil DNA glycosylase (MUG) which in Escherichia coli is highly specific to G:U mismatches, but also repairs G:T mismatches at high enzyme concentration. UDG family 3 includes Human SMUG1 which can remove uracil and its oxidized pyrimidine derivatives from, single-stranded DNA and double-stranded DNA with a preference for single-stranded DNA. Pedobacter heparinus SMUG2, which is UDG family 3 SMUG1-like, displays catalytic activities towards DNA containing uracil or hypoxanthine/xanthine. UDG family 4 includes Thermotoga maritima TTUDGA, a robust UDG which like family 1, acts on double-stranded and single-stranded uracil-containing DNA. UDG family 5 (UDGb) includes Thermus thermophilus HB8 TTUDGB which acts on double-stranded uracil-containing DNA; it is a hypoxanthine DNA glycosylase acting on double-stranded hypoxanthine-containing DNA except for the C/I base pair, as well as a xanthine DNA glycosylase which acts on both double-stranded and single-stranded xanthine-containing DNA. UDG family 6 hypoxanthine-DNA glycosylase lacks any detectable UDG activity; it excises hypoxanthine. Other UDG families include one represented by Bradyrhizobium diazoefficiens Blr0248 which prefers single-stranded DNA and removes uracil, 5-hydroxymethyl-uracil or xanthine from it
VPEADGYRGGRFAGVLFTSERPLPKTAAPLGGELGSGFISRDNDEPTATIVWRALAEAGIDRRDPLLWNA
VPWHPHKPGNPLSNRTPTAAELRAGLPFLRELLELLPNLRVVVAVGRKAQRALARLEPGIPVLAVRHPSP
GGA
>gnl|CDD|197344 cd10036, Reelin_subrepeat_Nt, Additional N-terminal subrepeat of reelin. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. Some family members appear to have an additional subrepeat at the N-terminus as characterized in this model. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1). Genetic deficiency of reelin, or ApoER2 and VLDLR, or Dab1, all exhibit the same phenotypes, including ataxia, cortical layer inversion and abnormal positioning patterns
LRDDFDSYPLLELNNNIWSECCGCNVGEQCGVIMHGNALTFCEPYGPRELITVPLNTTTASVLQFAIGSG
SCRFSYSDPSIIVSYAVNNTSSDWITLEKIRAPSNGSTIIHIIPLPTDAKQDNVSFRFRQEAPNAGEVYE
SCWALDNVLII
>gnl|CDD|197345 cd10037, Reelin_repeat_1_subrepeat_1, N-terminal subrepeat of tandem repeat unit 1 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the N-terminal subrepeat, which directly contacts the C-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
PIPPDLQTPATKFCLRQKSHGGHNRNVWAVDFFHLLPVLPSTVTHFAQFSINLGCGSHQPGNSVSLEFST
NHGRSWSLLHTECLPELCAGPHLPHSTVYSSDNYSGWNRITIPLPNAALTSATRFRWRQTGSVVGSMWAI
DNVYIG
>gnl|CDD|197346 cd10038, Reelin_repeat_2_subrepeat_1, N-terminal subrepeat of tandem repeat unit 2 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the N-terminal subrepeat, which directly contacts the C-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
NSISLDFSNLVEVTQSLGFYLGNVQPYCNHDWTLCFTGDSKHASSARYVETQSMQIGASYMIQFSLVMGC
GQQYTPHMDNQVKLEYSTNHGLTWHLVQEECLPGMPSCQEFTSGSIYHSSEFTEWRRITLPLPQKTWSSA
TRFRWSQSYYTDQDEWALDNIYIGQQCP
>gnl|CDD|197347 cd10039, Reelin_repeat_3_subrepeat_1, N-terminal subrepeat of tandem repeat unit 3 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the N-terminal subrepeat, which directly contacts the C-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
YEKPAFDYPLNQMSVWLMLSNEGMGKNESCSPTPSAMVFGKSDGDRFAVTRDLTLKPGYVLQFKVNIGCT
SEFSSFAPVLLQYSHDAGLTWSLVREGCYPASPGSKGCEGSSRELREPTVYHTGDYEDWTRITIPIPRSL
AASKTRFRWIQESSSLKNAPPFGLDGVYIS
>gnl|CDD|197348 cd10040, Reelin_repeat_4_subrepeat_1, N-terminal subrepeat of tandem repeat unit 4 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the N-terminal subrepeat, which directly contacts the C-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
GFQDKFDGSVDLQANWYRIQGGQVDIDCLSMDTALMFTENIGKPRYAETWDFHVSASTFLQFELSMGCSK
PYSNSHSVQLQYSLNNGRDWHLVTEECVPPAIGCLHYTESSVYSSERFQNWKRITVYLPPATISPRTRFR
WIQPNYAPGADSWAIDNVVLASGCPWMCSG
>gnl|CDD|197349 cd10041, Reelin_repeat_5_subrepeat_1, N-terminal subrepeat of tandem repeat unit 5 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the N-terminal subrepeat, which directly contacts the C-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
LLLDTFDFGPNESNWLFYPGGNTGLYCPYQSKGAPEEDSAMVFVSSELGEHSITTRDLDVNENTIIQFEI
NVGCTTESSSADPVRLEFSRDFGATWHLLLPLCYGSSSISSLCSTELHPSSVYYTGTTQGWRREVILFGK
LHLCGSVRFRWYQGFHPAGSQPVTWAIDNVYIGP
>gnl|CDD|197350 cd10042, Reelin_repeat_6_subrepeat_1, N-terminal subrepeat of tandem repeat unit 6 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the N-terminal subrepeat, which directly contacts the C-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
VLEDDFSTLDSRKWLLHPGGTKMPVCGSTGDALVFIEKASTRYVVTTDIMVNEDSFLQIDFAASCSVTDS
CYAIELEYSVDLGLSWHPLLRDCLPTNVECSSYHLQRILVSDTFNKWTRVTLPLPHYTRSQATRFRWHQP
APFDKQQTWAIDNVYIG
>gnl|CDD|197351 cd10043, Reelin_repeat_7_subrepeat_1, N-terminal subrepeat of tandem repeat unit 7 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the N-terminal subrepeat, which directly contacts the C-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
VLLDTFSSANLPQHERSPEDKTTVNDHWLFHDNCSIERFCDSPDGVMICGSHDDGREVSAVTHDLTPTEG
WILQFKISVGCKSSEKSAQQPVHVQYSTDFGVSWSYVTPQCLPSDPKCGGSVTQPSVFFPSKGWRRVTIP
LPDKLVGRPIRFRFYQKASDMQWALDNFYIG
>gnl|CDD|197352 cd10044, Reelin_repeat_8_subrepeat_1, N-terminal subrepeat of tandem repeat unit 8 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the N-terminal subrepeat, which directly contacts the C-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
PSSLVETFEDEGTSHDENWEFYPNGVRTDEFCGNPSFHLTWPNKKKDKTHNALTTRQLIVQPGYMIQFKI
VVGCGSVSSCGDLHPVMLEYTTDPRSDHWQLVQTECLPSSSNSIDCSPFQYHEASIYSSVNSSVWKRVTI
QLPDHVSSSATQFRWIQKTESTEAPSWAIDDVYIGE
>gnl|CDD|197353 cd10045, Reelin_repeat_1_subrepeat_2, C-terminal subrepeat of tandem repeat unit 1 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the C-terminal subrepeat, which directly contacts the N-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
PGFLSESFNSSRLSSYHNFSSIRGGEVGFGCGVLASGKALVFNGDGRRQLITAPLDSTQSRYLQFTLRLG
SKSVLGTCPPPDRPGEGVLLHYSCDNGITWKLLEHYSYDNYHEPRIVSVELPEDARNFGVQFRWWQPYHS
GQNQDVWALDEISMT
>gnl|CDD|197354 cd10046, Reelin_repeat_2_subrepeat_2, C-terminal subrepeat of tandem repeat unit 2 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the C-terminal subrepeat, which directly contacts the N-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
LPSTVMSDFENQDSLETEWQEVIGGEIVKPEMGCGVISSGSSLYFNKDGLRQLVSWDLDTTWVDFIQFYI
QIGGGSASCNYPDSREEGVLLQYSNNGGISWKLLAEMYFSDFSKPRFVYLELPTAAKTPCTRFRWWQPVF
SGEGYDQWALDDIIIL
>gnl|CDD|197355 cd10047, Reelin_repeat_3_subrepeat_2, C-terminal subrepeat of tandem repeat unit 3 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the C-terminal subrepeat, which directly contacts the N-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
PSEFFDRFEGKLSPLWYKITGGQVGTGCGVIKDGKSLYFNGPGKREARTVPLDTTNIRLVQFYIQIGSKL
NGETCLRPRSRNEGIIVQYSNDNGITWHLLRELDFMSYLEPQVISIELPREAKTPATAFRWWQPQHGKPS
AQWALDDVLIG
>gnl|CDD|197356 cd10048, Reelin_repeat_4_subrepeat_2, C-terminal subrepeat of tandem repeat unit 4 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the C-terminal subrepeat, which directly contacts the N-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
LPSVLKDDFNGNLRPDLWPEVYGAERGNLNGETIKSGTALIFKGEGLRMLVSRDLDCTHTLYIQFSFKFI
TKGTPERSHSVLLQYSINGGITWHLIDEFYFPTTTDVLFVNVPLPYTAQTNATRFRLWQPYNSGKKEEVW
ILDDLVIDGN
>gnl|CDD|197357 cd10049, Reelin_repeat_5_subrepeat_2, C-terminal subrepeat of tandem repeat unit 5 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the C-terminal subrepeat, which directly contacts the N-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
NPDFLKDDFEGQLESDRFLLMSGGKPSRKCGILSSGNNLFFNEDGLRMLVTRDLDLSMARFVQFFMRLGC
GKGVPDPRSQPVLLQYSLNGGLTWSLLQEFLFSNSSNVGRYVALEIPLKARSPSTRLRWWQPSENGHFYS
PWVIDQILIG
>gnl|CDD|197358 cd10050, Reelin_repeat_6_subrepeat_2, C-terminal subrepeat of tandem repeat unit 6 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the C-terminal subrepeat, which directly contacts the N-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
LPTQLKDTFNRAPSSSNWLTVVGGKLSTVCGAVASGTALHFSGGCSRQLVTVDLNLTNAEFVQFYFMYGC
LIPPSNRNQGVLLEYSVNGGITWNLLMEIFYDQYSKPGFVNILLPPEARGVGTRFRWWQPSHDGLDQNDW
AIDNVLIG
>gnl|CDD|197359 cd10051, Reelin_repeat_7_subrepeat_2, C-terminal subrepeat of tandem repeat unit 7 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the C-terminal subrepeat, which directly contacts the N-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
KTFLKERFDSEEISSDQWLSLEGGVTCTDCGVLAEGDALYFGGSGARQAVTQDLDLRGAKFVQYWARIGS
ENNMTLCLRPTCRKEGVLLQYSTDGGISWTLLHELDYQKYISVRYDYITLPENARTNSTRLRWWQPFTIS
NGLVVSGTERAQWALDNILIGG
>gnl|CDD|197360 cd10052, Reelin_repeat_8_subrepeat_2, C-terminal subrepeat of tandem repeat unit 8 of reelin and related proteins. Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the C-terminal subrepeat, which directly contacts the N-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1)
PSYIKDNFESGSVSELKWSLIQGGGIGSGCGQLAPHAHGDSLYFNGCGIRQAVTVELDLTRASKIMFVLQ
IGSRSQTDSCNINLSSPRAVDKAVLLQYSVNNGITWYLIAQHQPKDFMRAQRVSYNLPLEARTKGVVLRW
WQPRHDGTGHDQWALDNVEVV
>gnl|CDD|380782 cd10140, PFM_aerolysin_family, pore-forming module of aerolysin-type beta-barrel pore-forming proteins. Pore-forming proteins (PFPs) are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta pore-forming proteins (beta-PFPs) form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Members of this family includes enterolobin, a cytolytic, inflammatory and insecticidal protein from the Brazilian tree Enterolobium contortisiliquum
PVVVGSQTVTNTSSTTQTQTVTLSETKTVSVTVTVTVPPGKTVKVTVTVTKAKIDVPYTATLKATYSTSG
TGTTGTVSGVFTGVNYANVETT
>gnl|CDD|381074 cd10141, CopZ-like_Fer2_BFD-like, bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of Archaeoglobus fulgidus CopZ, and similar proteins. Archaeoglobus fulgidus CopZ is a fusion of a redox-active domain (containing a mononuclear metal center and an [2Fe-2S] cluster) with a CXXC-containing copper-binding domain. It is a soluble Cu+ chaperone which delivers cytoplasmic Cu+ to the transmembrane metal-binding sites in the Cu+-ATPase CopA; CopA couples the hydrolysis of ATP to the efflux of cytoplasmic Cu+. In addition to CopZ, the BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), and the large subunit of NADH-dependent nitrite reductase. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport
PKPVCYCFGVTEEDIIEAVAETGATTVEEIRATGKAGRCACEVNNPSGRCCLGNVKKA
>gnl|CDD|408998 cd10142, HD_SAS6_N, N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins. Spindle assembly abnormal protein 6 (SAS6) is a central scaffolding component of the centrioles that ensures their 9-fold symmetry. It is required for centrosome biogenesis and duplication, and is required for both mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells. It is also required for the recruitment of microcephaly protein STIL to the procentriole and for STIL-mediated centriole amplification. SAS6 is comprised of an N-terminal globular head domain, a centrally located coiled-coil domain, and a disordered C-terminus. These monomers homodimerize symmetrically, through two dimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. These homodimers can self-assemble into a 9-fold symmetric cartwheel structure comprised of nine SAS6 homodimers associated via their head domains; the dimerized coiled-coil domains being the spokes, the central hub being the head domains. This model corresponds to the N-terminal head domain of SAS6, which is structurally related to other XRCC4-superfamily members, XRCC4, PAXX, XLF and CCDC61
VLYSRELPVEVKSQDREERLEVLRVKIEILSSGSGHKKELRVRLTDETDLFFLYTLELNEEDFQSLKEQQ
GLLVDFSAFPQKLIDLLELCIKEESKEPPKFLLVLVISSDKGRATLEIVETNPFKHLTHLSLKFLPG
>gnl|CDD|381748 cd10144, Peptidase_S74_CIMCD, Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F endosialidase and related proteins. This peptidase S74 family includes C-terminal intramolecular chaperone domain (CIMCD) of Escherichia coli phage K1F endosialidase, Bacillus phage GA-1 neck appendage protein, and Bacteriophage T5 L-shaped tail fibre. This domain acts as a molecular chaperone; during virus particle assembly, the CIMCD of phage tailspike proteins induces the homo-trimerization of phage tailspike proteins by chaperoning the formation of a triple beta-helix. Homo-trimeric phage tailspike proteins are then auto-cleaved by the CIMCD domain. This family also includes the peptidase S74 Intramolecular Chaperone Auto-processing (ICA) domain of mammalian Myrf. The ICA domain drives the homo-oligomerization of Myrf in the endoplasmic reticulum (ER) membrane. The homo-oligomeric Myrf is proteolyzed by the ICA domain, releasing its N-terminal fragments from the ER membrane
SDARLKTEIREIDDAELDAWKKVRFVQYKWKEAVAEKGDDARLHFGVIAQEVIAAFEDAGLDAGKYGILC
YDEWDAVTDEVITMENVGIEAGERYGTRYDELLIFEAAAQRRR
>gnl|CDD|199901 cd10145, TFIIA_gamma_N, Gamma subunit of transcription initiation factor IIA, N-terminal helical domain. Transcription factor II A (TFIIA) is one of the general transcription factors for RNA polymerase II. TFIIA increases the affinity of the TATA-binding protein (TBP) for DNA, in order to assemble the initiation complex. TFIIA also functions as an activator during development and differentiation, and is involved in transcription from TATA-less promoters. TFIIA is composed of more than one subunit in various organisms. Mammalian TFIIA large subunits (TFIIA alpha and beta), and the smaller subunit (TFIIA gamma) form a heterotrimer. TFIIA alpha and beta are encoded by a single TFIIA_alpha_beta gene and post-translationally processed and cleaved. TOA1 and TOA2 are the two subunits of Yeast TFIIA which correspond to Mammalian TFIIA_alpha_beta and TFIIA gamma, respectively. TOA1 and TOA2 form a heterodimeric protein complex. The TFIIA gamma subunit is highly conserved between humans, Drosophila and yeast and it is required for TFIIA function. The N-terminal domain of the gamma subunit forms a 4-helix bundle together with the alpha subunit
YYELYRNTTLGIALQDALDELIQDGQITPQLAMKVLLQFDKSINEALAN
>gnl|CDD|199214 cd10146, LabA_like_C, C-terminal domain of LabA_like proteins. This C-terminal domain is found in a well conserved group of mainly bacterial proteins with no defined function, which contain an N-terminal LabA-like domain. LabA from Synechococcus elongatus PCC 7942, (which does not contain this C-terminal domain) has been shown to play a role in cyanobacterial circadian timing. LabA-like C-terminal domains described here may be related to the LOTUS domain family (which also co-occurs with LabA-like N-terminal domains)
LVELLRKAIEALADDDGWANLGAVGSYLKKKYPDFDPRNYGYSKLSDLIKALDLFEIKKRGNGGQVYVR
>gnl|CDD|199902 cd10147, Wzt_C-like, C-Terminal domain of O-antigenic polysaccharide transporter protein Wzt and related proteins. The Escherichia coli ABC protein Wzt consists of 2 domains, a conventional ABC domain that binds ATP and utilizes its energy to transport molecules across membranes, and a C terminal domain which is responsible for its target molecule specificity. Wzt is part of the ATP-binding-cassette (ABC) transporter complex, responsible for the transport of the O-antigenic polysaccharide (O-PS) portion of lipopolysaccharide (LPS), a major component of the outer membrane of Gram-negative bacteria. This CD includes Wzt proteins from two Escherichia coli serotypes O8 and O9a, WztO8 and WztO9a; these proteins are specific for their cognate polysaccharides (O8 or O9a O-PS)
SESRFGSGGARITDVELLDEDGEPVNTFRSGEPVTLRIEYEVNEDIEDPVVGFTIKDRDGQDVFGTNTLL
LGGVLPSLKAGGEGEVEFTFPLPLNPGEYSLSVALADGDGHHEVLDWIDDALSFEVESSSKSLFVGLVDL
PHEW
>gnl|CDD|197385 cd10148, CsoR-like_DUF156, Transcriptional regulators CsoR (copper-sensitive operon repressor), RcnR, and FrmR, and related domains; this domain superfamily was previously known as DUF156. This superfamily includes various transcriptional regulators that respond to stressors including Cu(I), Ni(I), sulfite, and formaldehyde. It includes CsoR (copper-sensitive operon repressor) from Mycobacterium tuberculosis (MtCsoR), Bacillus subtilis (BsCsoR), Thermus thermophilus (TthCsoR), and Staphylococcus aureus (SaCsoR), Mycobacterium tuberculosis RicR (regulated in copper repressor, MtRicR), Escherichia coli RncR (formally known as YohL, nickel and cobalt-sensitive), Alcaligenes xylosoxidans NreA (nickel-sensitive), E. coli FrmR (formally known as YaiN, formaldehyde sensitive), and Staphylococcus aureus CstR (CsoR-like sulfur transferase repressor, NWMN_0026.5, SaCstR). CsoR is Cu(I)-inducible, and regulates the expression of genes involved in copper homeostasis. For example, TthCsoR binds the promoter region of the copZ-csoR-copA operon, and represses expression of these genes, which encode the copper chaperone CopZ, CsoR, and the copper efflux P-type ATPase CopA, respectively. In the presence of excess Cu(I), TthCsoR binds this ion, and is released from the DNA, allowing expression of the downstream genes. TthCsoR also senses other metal ions such as Cu(II), Zn(II), Ag(I), Cd(II) and Ni(II). CsoRs form a homotetramer (dimer of dimers). In the case of MtCsoR, two Cys residues on opposite subunits within each dimer, along with a His residue, bind the Cu(I) ion. These residues are conserved in the majority of members of this superfamily. Exceptions include the functionally uncharacterized Bacillus subtilis YrkD where there is an Asn instead of His (C-N-C), E.coli RcnR where there is a Thr instead of the second Cys (C-H-T), or TthCsoR and E.coli FrmR where there is a His instead of the second Cys and which have an additional N-terminal His (not found in those family members having C-H-C) that may also be involved in metal binding (H-C-H-H). A conserved Tyr and a Glu residue facilitate allosteric regulation of DNA binding. SaCstR regulates genes predicted to function in sulfur metabolism; it is thought that oxidation of the intersubunit Cys pair to a mixture of disulphide and trisulphide linkages by sulfite, results in a reduced affinity of SaCstR for the operator DNA. SaCstR exists as a mixture of oligomeric states, including dimers, tetramers and octamers. The sequence of SaCstR was not available at the time this hierarchy was curated and therefore was not included. Escherichia coli RncR represses expression of the gene encoding the nickel and cobalt-efflux protein RcnA. The gene encoding Alcaligenes xylosoxidans NreA is part of the nre nickel resistance locus located on the pTOM9 plasmid from thisbacteria. Escherichia coli FrmR regulates the formaldehyde degradation frmRAB operon
KKDLLKRLRRIEGQVRGIQRMIEEDRYCVDILTQLAAVRSALDKVGLLILEDHLKHCVAEAIESGEAEEK
IEELLKLLKK
>gnl|CDD|197397 cd10149, ClassIIa_HDAC_Gln-rich-N, Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, HDAC5 and HDCA9). This superfamily consists of a glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDAC9; it is missing in HDAC7. It is referred to as the glutamine-rich domain, and confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors. This domain is able to repress transcription independently of the HDAC's C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues
DPVLREQQLQQELLALKQQQQIQKQLLIAEFQKQHENLTRQHEAQLQEHIKQQQEMLAIKQQQELLEKQR
KLEQQRQEQELEKQRREQQL
>gnl|CDD|199903 cd10150, CobN_like, CobN subunit of cobaltochelatase, bchH and chlH subunits of magnesium chelatases, and similar proteins. Cobaltochelatase is a complex enzyme that catalyzes the insertion of cobalt into hydrogenobyrinic acid a,c-diamide, resulting in cobyrinic acid, as demonstrated for Pseudomonas denitrificans. This is an essential step in the bacterial synthesis of cobalamine (B12). The insertion of cobalt requires a complex composed of three polypeptides, cobN, cobS, and cobT. Also included in this family are protoporphyrin IX magnesium chelatases involved in the synthesis of chlorophyll and bacteriochlorophyll, specifically the large (chlH or bchH) subunits.They are thought to bind both the protoporphyrin and the magnesium ion. Hydrolysis of ATP by the smaller subunits in the complex may trigger a conformational change that results in the insertion of the ion into the protoporphyrin scaffold. Cryo electron microscopy studies have suggested that a distinct bchH C-terminal domain may bind tightly to the N-terminal domain upon substrate binding, requiring a substantial conformational change of the bchH subunit. It has also been suggested that chlH of higher plants binds abscisic acid via a C-terminal domain and plays a role in abscisic acid signaling, and that the protein spans the chloroplast envelope, with the C-terminus exposed to the cytosol
ANLAELRHEASVDLYVETTLSKADVIILRLLGGFSYWPYGLELLAALARANGIPLIVLPGDDEEDLLSTV
DLENWARLLAYLRYGGPENLRNLLRYLAALYGGGDYEPEPPVPLPEAGIYHPDAGGIFEDDEEYYKEHRY
DPGAPTVGILFYRSYLLAGNTAVVDALIRALEARGLNVIPVFVSSLKDEDAGRELFMLDGKPRVDAIINL
TGFSLGGGPAEEGVELLKKLNVPVLQAIPSYSQTEEWWESPRGLSPLDLAMQVALPELDGRIEPIVIAGK
EEDEDDETTVEKYVPIPERIERLADRAARWARLRRKPNAEKKIAIILYNYPPGKGNIGAAVGLDTPSSLS
LLLIRLKAEGYGVGELPESGEELIELLLEGGANIGFPGELEELVKGGAAALLPLEEYLEWFNELPEALRK
EVEERWGEPPGEIMVYENGYFVIPGLRFGNVFVGPQPPRGWEGDPEKLYHDPDLPPPHQYLAFYLWLRKV
FGADAVIHFGTHGTLEWLPGKEVGLSASCWPDILIGDLPNIYPYIVDNPGEGTQAKRRGYAVIIDHLTPP
LTRAGLYGELAELEELIDEYERLHDYLCELKESLIPDGLHVFPLLLSTSDEIEALLRALNGRYIPPPSGG
DPRGNPDVLPTGRNFYSFDPRAIPTKAAWEVGKKLAEELLERYLQEHGEYPEKVAFVLWGTETMRTGGED
IAQILYLLGVRPVWDAGGRVTGVEIIPLEELGRPRIDVTVRISGLFRDLFPNLIELLDEAVRLVAALDEP
DEMNYVRKHALEDKLLAEGLSEEEARRLATARIFGPAPGAYGAGVNEAVESGAWEDEEDLAEAYLNRMGY
AYGKGVWGEKARELFEARLKGVDAVVHNRDSNEYDLLDNDDYYQYLGGLSAAVRALSGKAPELYIGDTRD
>gnl|CDD|197386 cd10151, TthCsoR-like_DUF156, Thermus thermophilus CsoR, a Cu(I)-sensing transcriptional regulator, and related domains; this domain family was previously known as part of DUF156. This domain family contains various Cu(I)-inducible transcriptional regulators including CsoR (copper-sensitive operon repressor) from Mycobacterium tuberculosis (MtCsoR), and Thermus thermophilus (TthCsoR). CsoR regulates the expression of genes involved in copper homeostasis. For example, TthCsoR binds the promoter region of the copZ-csoR-copA operon, and represses expression of these genes, which encode the copper chaperone CopZ, CsoR, and the copper efflux P-type ATPase CopA, respectively. In the presence of excess Cu(I), TthCsoR binds this ion, and is released from the DNA, allowing expression of the downstream genes. TthCsoR also senses other metal ions such as Cu(II), Zn(II), Ag(I), Cd(II) and Ni(II). MtCsoR regulates an operon that includes CsoR and a putative copper transporter gene, ctpV (cation transporter P-type ATPase). CsoRs form a homotetramer (dimer of dimers). In MtCsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in some but not all members of this family; for example, for TthCsoR, there is a His instead of the second Cys as well as an N-terminal His (not found in those family members having C-H-C) which may also be involved in metal binding (H-C-H-H). A conserved Tyr and a Glu residue facilitate allosteric regulation of DNA binding
AKKEDALRRLKIIEGHLEGIQKMLEEDKYCVDVLRQIKAVQSALEKVSDLILEGHLESCVTTAIERGERE
EVIEELMEAFKY
>gnl|CDD|197387 cd10152, SaCsoR-like_DUF156, Staphylococcus aureus copper-sensitive operon repressor (CsoR), and related domains; this family was previously known as part of DUF156. This domain family includes Staphylococcus aureus CsoR (SaCsoR). SaCsoR is Cu(I)-inducible, and regulates the expression of genes involved in copper homeostasis; it represses a genetically unlinked copA-copZ operon. copA encodes a copper efflux P-type ATPase, and copZ, a copper chaperone. This family belongs to a larger superfamily that contains various transcriptional regulators that respond to different stressors such as Cu(I), Ni(I), sulfite, and formaldehyde, and includes Mycobacterium tuberculosis CsoR (MtCsoR), Bacillus subtilis CsoR, and Thermus thermophilus CsoR. The latter three proteins do not belong to this family. CsoRs form homotetramers (dimer of dimers). In MtCsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in the majority of members of this superfamily, including this family, and a conserved Tyr and a Glu residue that facilitate allosteric regulation of DNA binding for CsoRs are also well conserved
KKNLINRLNRIEGQIRGIKGMIENDVYCDDVLNQIASVKSALDGVSKLLLESHIKSCVVEQIKEGEEEVV
EELLYTINKMIK
>gnl|CDD|197388 cd10153, RcnR-FrmR-like_DUF156, Transcriptional regulators RcnR and FrmR, and related domains; this domain family was previously known as part of DUF156. This domain family includes various transcriptional regulators that respond to different stressors. It includes Escherichia coli RncR (formally known as YohL, nickel and cobalt-sensitive), and E. coli FrmR (formally known as YaiN, formaldehyde sensitive). Escherichia coli RncR represses expression of the gene encoding the nickel and cobalt-efflux protein RcnA; RcnA may act through modulating NikR, to repress the NIkABCDE nickel transporter. In vitro, purified RncR binds to the rncA promoter DNA fragment in the absence of Ni2+ or Co2+, and the affinity of RncR for this promoter is reduced in the presence of excess nickel. Escherichia coli FrmR regulates the formaldehyde degradation frmRAB operon. This family belongs to a larger superfamily that includes CsoRs (copper-sensitive operon repressors). CsoRs form homotetramers (dimer of dimers). In Mycobacterium tuberculosis CsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in the majority of members of this superfamily. In this family, however, not all these residues are conserved; in E.coli RcnR and FrmR there is a His or a Thr instead of the second Cys (C-H-H or C-H-T) respectively. For E. coli FrmR, an N-terminal His residue, not conserved in all members of this family, is also involved in metal binding (H-C-H-H). A conserved Tyr and a Glu residue that facilitate allosteric regulation of DNA binding for CsoRs are poorly conserved in this family
HTPKEKKKLLARVRRIRGQVEALERALEAEADCAAVLQQIAAVRGAVNGLMAEVLESHLREHVADPELSD
AERAQAAEELIEVLRSYL
>gnl|CDD|197389 cd10154, NreA-like_DUF156, Alcaligenes xylosoxidans NreA and related domains; this domain family was previously known as part of DUF156. This domain family includes Alcaligenes xylosoxidans NreA, Psudomonas putida MreA, and related domains. The gene encoding Alcaligenes xylosoxidans NreA is part of the nre nickel resistance locus located on the pTOM9 plasmid from this bacteria; it confers low-level nickel resistance on both Ralstonia and Escherichia coli strains. The Pseudomonas putida MreA gene is found in association with a gene encoding mrdH, a heavy metal efflux transporter of broad specificity. MreA may have a role in cadmium and nickel resistance. This family is part of a larger superfamily that contains various transcriptional regulators that respond to different stressors such as Cu(I), Ni(I), sulfite, and formaldehyde, and includes CsoRs (copper-sensitive operon repressors). CsoRs form homotetramers (dimer of dimers). In Mycobacterium tuberculosis CsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in the majority of members of this superfamily, including members of this family; however, a conserved Tyr and a Glu residue that facilitates allosteric regulation of DNA binding for CsoRs are poorly conserved
HASHPDIIKRLKRAEGHLRSIITMIEEGRPCVDIAQQLHAVEKAITQAKRTLIHDHIDHCLEEAVGDLPR
DERSVLAEFKAITKYL
>gnl|CDD|197390 cd10155, BsYrkD-like_DUF156, Uncharacterized protein YrkD from Bacillus subtilis and related domains; this domain superfamily was previously known as part of DUF156. This domain family contains an uncharacterized protein YrkD from Bacillus subtilis and related proteins. This family is part of a larger superfamily that contains various transcriptional regulators that respond to different stressors such as Cu(I), Ni(I), sulfite, and formaldehyde, and includes CsoRs (copper-sensitive operon repressors). CsoRs form homotetramers (dimer of dimers). In Mycobacterium tuberculosis CsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in the majority of members of this superfamily. In this family, however, not all these residues are conserved, there is an Asn instead of the His (C-N-C); also a conserved Tyr and a Glu residue that facilitates allosteric regulation of DNA binding for CsoRs are very poorly conserved
DKKIKNRLKRAEGQLRGILKMMEEGKECKDVVTQLSAVRSSVDRAIGLIVAENLEECVREEEEDGEDQEE
KIQEAINLLVKS
>gnl|CDD|197391 cd10156, FpFrmR-Cterm-like_DUF156, C-terminal domain of Faecalibacterium prausnitzii A2-165 FrmR, and related domains; this domain family was previously known as part of DUF156. This domain family contains the C-terminal domain of the functionally uncharacterized protein Faecalibacterium prausnitzii A2-165 FrmR, and related domains. This family is part of a larger superfamily that contains various transcriptional regulators that respond to different stressors such as Cu(I), Ni(I), sulfite, and formaldehyde, and includes CsoRs (copper-sensitive operon repressors). CsoRs form homotetramers (dimer of dimers). In Mycobacterium tuberculosis CsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in the majority of members of this superfamily, including this family, and a conserved Tyr and a Glu residue that facilitate allosteric regulation of DNA binding for CsoRs are also conserved
RDEEEKKDLINRLNRIEGQIRGIKKMLEEDRYCGDILVQVAAVESALNSFNKELLQNHIRTCVVEDIRNG
NEEVVDELMDLLQKLM
>gnl|CDD|197392 cd10157, BsCsoR-like_DUF156, Bacillus subtilis copper-sensitive operon repressor (BsCsoR), and related domains; this family was previously known as part of DUF156. This domain family includes Bacillus subtilis CsoR (BsCsoR). CsoRs are Cu(I)-inducible, and regulate the expression of genes involved in copper homeostasis. BsCsoR regulates the copZA operon which encodes the copper chaperone CopZ, and the copper efflux P-type ATPase CopA. This family belongs to a larger superfamily that contains various transcriptional regulators that respond to different stressors such as Cu(I), Ni(I), sulfite, and formaldehyde, and includes Mycobacterium tuberculosis CsoR (MtCsoR), Thermus thermophilus CsoR, and Staphylococcus aureus CsoR. The latter three proteins do not belong to this family. CsoRs regulate the expression of genes involved in copper homeostasis. CsoRs form homotetramers (dimer of dimers). In MtCsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in the majority of members of this superfamily, including this family, and the conserved Tyr and a Glu residue that facilitate allosteric regulation of DNA binding for CsoRs are also well conserved
KENDALLNRLKRIEGQVRGLQKMVEDDRYCIDILVQISAIQAALKQVGLQVLEDHTSHCVADAIKNGDGE
ESIKELMKVIKQFSK
>gnl|CDD|197393 cd10158, CsoR-like_DUF156_1, Uncharacterized family 1; belongs to a superfamily containing the transcriptional regulators CsoR (copper-sensitive operon repressor), RcnR, and FrmR, and related domains; this family was previously known as part of DUF156. Uncharacterized family 1, belonging to a larger superfamily that contains various transcriptional regulators that respond to different stressors such as Cu(I), Ni(I), sulfite, and formaldehyde, and includes CsoRs (copper-sensitive operon repressors). CsoRs form homotetramers (dimer of dimers). In Mycobacterium tuberculosis CsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in the majority of members of this superfamily, including this family; however, a conserved Tyr and a Glu residue that facilitates allosteric regulation of DNA binding for CsoRs are poorly conserved
RKKVINRLARIIGHLRSVKRMVEEDRDCSEVLIQIAAVRSALNNVAKVILKDHLEHCIVEAVEENDEEAI
EELNEAIDKFI
>gnl|CDD|197394 cd10159, CsoR-like_DUF156_2, Uncharacterized family 2; belongs to a superfamily containing transcriptional regulators CsoR (copper-sensitive operon repressor), RcnR, and FrmR, and related domains; this family was previously known as part of DUF156. Uncharacterized family 2, belonging to a larger superfamily that contains various transcriptional regulators that respond to different stressors such as Cu(I), Ni(I), sulfite, and formaldehyde, and includes CsoRs (copper-sensitive operon repressors). CsoRs form homotetramers (dimer of dimers). In Mycobacterium tuberculosis CsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in the majority of members of this superfamily, including this family, and a conserved Tyr and a Glu residue that facilitate allosteric regulation of DNA binding for CsoRs are also conserved
DKKKALRLLKTARGQIDGIIKMIEEDRYCIDISNQILATQALLKKANKEILSAHMKHCVKEAVESEDAEE
KIEEIIELLDKL
>gnl|CDD|197395 cd10160, CsoR-like_DUF156_3, Uncharacterized family 3; belongs to a superfamily containing the transcriptional regulators CsoR (copper-sensitive operon repressor), RcnR, and FrmR, and related domains; this family was previously known as part of DUF156. Uncharacterized family 3, belonging to a larger superfamily that contains various transcriptional regulators that respond to different stressors such as Cu(I), Ni(I), sulfite, and formaldehyde, and includes CsoRs (copper-sensitive operon repressors). CsoRs form homotetramers (dimer of dimers). In Mycobacterium tuberculosis CsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in the majority of members of this superfamily, including this family; however, a conserved Tyr and a Glu residue that facilitate allosteric regulation of DNA binding for CsoRs are not conserved
DSENLHRRLKKIIGQVNAIDRMIDEDVPCEDVLIQINAAKSALHKVGQIVLEGHLNHCVRDGIEHGDADE
TIEDFSKAIEYFSRM
>gnl|CDD|197396 cd10161, CsoR-like_DUF156_4, Uncharacterized family 4; belongs to a superfamily containing the transcriptional regulators CsoR (copper-sensitive operon repressor), RcnR, and FrmR, and related domains; this family was previously known as part of DUF156. Uncharacterized family 4, belonging to a larger superfamily that contains various transcriptional regulators that respond to different stressors such as Cu(I), Ni(I), sulfite, and formaldehyde, and includes CsoRs (copper-sensitive operon repressors). CsoRs form homotetramers (dimer of dimers). In Mycobacterium tuberculosis CsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in the majority of members of this superfamily. In this family, however, only one of these residues is conserved (the first Cys); and a conserved Tyr and a Glu residue that facilitate allosteric regulation of DNA binding for CsoRs are also not conserved
RTGLLNRLARVEGQIRGIQRMIEEGEDCESIAQQMSASRKALDKAYCEMLACFIEQEIQEEGQLNDAVQT
MLSDVTTLLTKY
>gnl|CDD|197398 cd10162, ClassIIa_HDAC4_Gln-rich-N, Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase. This family consists of the glutamine-rich domain of histone deacetylase 4 (HDAC4). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues
EPALREQQLQQELLALKQKQQIQRQLLIAEFQRQHEQLSRQHEAQLHEHIKQQQELLAMKHQQELLEHQR
KLERHRQEQEMEKQQREQKL
>gnl|CDD|197399 cd10163, ClassIIa_HDAC9_Gln-rich-N, Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase. This family consists of the glutamine-rich domain of histone deacetylase 9 (HDAC9). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues
DPTVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHLKLQQELLAMKQQQELLEKEQ
KLEQQRQEQELERHRREQQL
>gnl|CDD|197400 cd10164, ClassIIa_HDAC5_Gln-rich-N, Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase. This family consists of the glutamine-rich domain of histone deacetylase 5 (HDAC5). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues
DPSLREQQLQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKHLKVRAELFSEQQQQEILAAKR
QQELEQQRKREQQRQEELEKQRLEQQL
>gnl|CDD|466810 cd10169, ASKHA_NBD_actin-like, nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs). Actin is ubiquitous in eukaryotes, and the major component of the actin cytoskeleton; monomeric globular protein (G-actin) reversibly polymerizes to form filaments (F-actin). Each actin protomer binds one molecule of ATP and either calcium or magnesium ions. F-actin filaments form with the consequent hydrolysis of ATP. Some actin-related proteins (Arps) have roles in cytoskeletal functions, such as actin polymerization (Arp2/3) and dynein motor activity (Arp1). Both conventional actin and specific Arps have been implicated in chromatin remodeling and/or transcription regulation. The actin/ARP family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains
IVIDNGSGTIKAGFAGEDAPRLIFPWDDMEKIWEHVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEIL
FETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVYEGYVLPHAVRRLDIGGRDLTDYLAKLL
REKGYSFSTSAEREIVRDIKEKLCGLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELS
KLAPSSVKVKVIAPPERKYSAWIGGSILASLSTFQQMWITKEEYEEHG
>gnl|CDD|466811 cd10170, ASKHA_NBD_HSP70, nucleotide-binding domain (NBD) of the HSP70 family. HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains
VGIDFGTTYSGVAYALLGPGEPPLVVLQLPWPGGDGGSSKVPSVLEVVADFLRALLEHAKAELGDRIWEL
EKAPIEVVITVPAGWSDAAREALREAARAAGFGSDSDNVRLVSEPEAAALYALEDKGDLLPLKPGDVVLV
CDAGGGTVDLSLYEVTSGSPLLLEEVAPGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLL
REFEEAKKRFSGGEEDERLVPSLLGGGLPELGLEKGTLLLTEEEIRDLFDPVIDKILELIEEQLEAKSGT
PPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVLRSDDPDTAVARGAAL
>gnl|CDD|466812 cd10206, ASKHA_NBD_Arp8-like, nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily. The Arp8-like family includes Arp8, also called actin-like protein 8, from vertebrates and fungi. Human Arp8 is encoded by the ACTR8 gene and is also known as INO80 complex subunit N. It plays an important role in the functional organization of mitotic chromosomes. Arp8 exhibits low basal ATPase activity, and is unable to polymerize. It is probably a core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication, and probably DNA repair. it is required for the recruitment of INO80 (and probably the INO80 complex) to sites of DNA damage. Arp8 strongly prefers nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex. This subfamily also contains Arabidopsis thaliana Arp9
KTIVIHPGSRNLRIGRASDDLPVVIPHCIARRRKQTGSARPEDVPPAVRNGEDSVESEEEREEALKEVER
ALKSRKKSNGRRRIPNQVSAKQNKPSKPENVPEDLDASSGENWTDTSDYPDFLVGEEALRLPPSEEYNLH
WPIRRGRLNVHSDGGSLTAVLDDLEDIWSHALEEKLEIPRKDLKNYRAVLVIPDLFDRRHVKELVDLLLR
RLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFLWLLRR
SGFPYRECNLNSPLDFLLLERLKETYCTLDQDDIGVQLHEFYVREPGQPTLKYQFKLLPLDEAIVQSILS
CASDELKRKMYSSILLVGGGAKIPGLAEALEDRLLIKIPSLFEAVETVEVLPPPKDMDPSLLAWKGGAVL
ACLDSAQELWITRKEWQRLGVRALRER
>gnl|CDD|466813 cd10207, ASKHA_NBD_Arp10, nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins. Arp10, also known as actin-related protein 11 (Arp11), is a subunit of the cargo-binding portion of the dynein activator, dynactin. It, together with dynactin4 (p62), -5(p25), and -6(p27), forms a heterotetrameric complex located at the pointed end of Arp1. Arp1 forms a mini-filament of uniform size, with proteins bound along its length and at both ends. Human Arp10 is encoded by the ACTR10 gene
VVLDIGSAYTKCGFAGESAPRCIIPSEVKLPGGKKVIRVVDQRSGNEEELYEALKEFLHELYFKHLLVNP
KDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVYEG
VPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNKGQLLSSVDSLLSEEVLEDIKVRACFVTSLERGK
TLQSATEEGSTEEPSPPPPVDYPLDGEKILIVPGSIRESAEELLFEGDNEEKSLPTLILDSLLKCPIDVR
KQLAENIVVIGGTSMLPGFKHRLLEELRALLRKPKYFEELAPKTFRFHTPPSVFKPNYLAWLGGSIFGAL
ESILGRSLSREAYLQTGRIPDWCSL
>gnl|CDD|466814 cd10208, ASKHA_NBD_ScArp9-like, nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and similar proteins. Saccharomyces cerevisiae Arp9, also called actin-like protein 9, chromatin structure-remodeling complex protein ARP9, or SWI/SNF complex component ARP9, is a component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. It is also part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of many genes. Arp9 forms a stable heterodimer with Arp7 protein in both the RSC and SWI/SNF chromatin-remodeling complexes. It has been suggested that this dimer functions as a module with DNA bending proteins, to achieve correct architecture and facilitate complex-complex interactions. Fission yeast SWI/SNF and RSC complexes do not contain Arp7 and Arp8, but instead contain Arp9 and Arp42
NILVIDPGSQTTRAGLGLGELLTPPTIEIPTRVEIIWPIQDGRVVDWDALEALWRHILFSLLSIPRPTNN
SPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAALYAAGATSGIVVDIGHEKTDITPIVDSQV
VPHALVSIPIGGQDCTAHLAQLLKSDEPELKSQAESGEEATLDLAEALKKSPICEVLSDGADLASGTEIT
VGKERFRACEPLFKPSSLRVDLLIAAIAGALVLNASDEPDKRPALWENIIIVGGGSRIRGLKEALLSELQ
QFHLISETSASPQQPRIIRLAKIPDYFPEWKKSGYEEAAFLGASIVAKLVFNDPSSKHYISKVDYNEKGP
AAIHTK
>gnl|CDD|466815 cd10209, ASKHA_NBD_AtARP7-like, nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar proteins. Arabidopsis thaliana ARP7 is an essential nuclear protein, ubiquitously expressed in all cell types. It is needed for normal embryogenesis, plant architecture, and floral organ abscission. It may play a role in regulating various phases of plant development through chromatin-mediated gene regulation
VVIDAGSRLLKAGYAYPDREPSVVEPTRVTPAVEDGEESDTVVEGNTVSPIRRGRIEDWDALEALLRYVF
YTGLGWEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGK
IDIAPVWEGAIQHNAVRRFEIGGRDLTELLAAELGKSNPKVKLDRSIVERLKEAVAWSADDEEAYEKKVL
TCSPETYTLPDGRVISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGT
SSVPGLEARLQKEIRLLSSPSSRPALVKPPEYMPENTLRYSAWIGGAILAKVVFPQNQHVTKADYDETGP
SVVH
>gnl|CDD|466816 cd10210, ASKHA_NBD_Arp6, nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins. Arp6, also called actin-like protein 6, is required for formation and/or maintenance of proper nucleolar structure and function, plays a dual role in the regulation of ribosomal DNA (rDNA) transcription. In the presence of high glucose, Arp6 maintains active rDNA transcription through H2A.Z deposition and under glucose starvation, it is required for the repression of rDNA transcription, and this function may be independent of H2A.Z. Arp6 is also required for telomere silencing in both fission and budding yeast. It is a component of the budding yeast and Arabidopsis SWR1 complex (SWR1C) and the human SWI2/SNF2-related CBP activator protein (SRCAP) chromatin remodeling complexes which catalyze the exchange of the histone H2A with the H2AZ. Drosophila Arp6 colocalizes with HP1 (heterochromatin protein 1) in the pericentric heterochromatin, and vertebrate Arp6 also interacts with HP1. Human Arp6 is encoded by the ACTR6 gene. Arabidopsis thaliana ACTIN RELATED PROTEIN 6/EARLY IN SHORT DAYS 1/SUPPRESSOR OF FRIGIDA 3 (encoded by ARP6/ESD1/SUF3) participates in regulating several leaf and flower development stages. It is needed for Flowering locus C (FLC, the master repressor of flowering) and FLC-like gene expression in the shoot and root apex, and for the activity of the floral repressor pathway
TLVLDNGAYTIKAGFASDDPPRVIPNCIAKPKSERRRLFGDDQLDECKDLSGLFYRRPFERGYLVNWDLQ
RQIWDHLFGKLLLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAYLADSEQ
SSSSSSQCCLVVDSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQLNVMDETYLVNQIK
EDLCFVSTDFYEDLEIAKKKGKENTIRRDYVLPDYTTSKRGYVRDPEEPNRGKLKEDEQVLRLNNERFTV
PELLFHPSDIGIQQAGIAEAIVQSINACPEELQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDV
NVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEHG
>gnl|CDD|466817 cd10211, ASKHA_NBD_Arp5, nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins. Arp5, also called actin-like protein 5, may act as a core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. It is involved in DNA double-strand break repair and UV-damage excision repair. Human Arp5 is encoded by the ACTR5 gene. Arabidopsis thaliana ARP5 (AtARp5) is a ubiquitously expressed nuclear protein involved in DNA repair and required for multicellular development of all organs. AtARp5 may be part of other chromatin remodeling machines in addition to INO80
PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPRDRKKGITVTLVGNDILNDEAVRSHLRSPFDRNVVTNF
DLQEQILDYIFSHLGINSEGSVDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQP
QGDPSDGLVISSGYSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELV
HEHCYVAEDYDEELKKWEDPEYYEENVRKIQLPFGLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPG
LKERLEKELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEYEEKGGEYLKEH
>gnl|CDD|466818 cd10212, ASKHA_NBD_ScArp7-like, nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and similar proteins. Saccharomyces cerevisiae Arp7, also called actin-like protein 7, is a component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. It is also part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of many genes. Arp7 forms a stable heterodimer with Arp9 protein in both the RSC and SWI/SNF chromatin-remodeling complexes. It has been suggested that this dimer functions as a module with DNA bending proteins, to achieve correct architecture and facilitate complex-complex interactions. Fission yeast SWI/SNF and RSC complexes do not contain Arp7 and Arp8, but instead contain Arp9 and Arp42
LNRKCVVIHNGSHRTVAGFSNVELPQCIIPSSYIKRTDEGGEAEFIFGTYNMIDAAAEKRNGDEVYTLVD
SQGLPYNWDALEMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMAILERYYELAFDKLNVPVFQIVIEP
LAIALSMGKSSAFVIDIGASGCNVTPIIDGIVVKNAVVRSKFGGDFLDFQVHERLAPLIKEENDMENMAD
EQKRSTDVWYEASTWIQQFKSTMLQVSEKDLFELERYYKEQADIYAKQQEQLKQMDQQLQYTALTGSPNN
PLVQKKNFLFKPLNKTLTLDLKECYQFAEYLFKPQLISDKFSPEDGLGPLMAKSVKKAPEQVYSLLLTNV
IITGSTSLIEGMEQRIIKELSIRFPQYKLTTFANQVMMDRKIQGWLGALTMANLPSWSLGKWYSKEDYET
LKRD
>gnl|CDD|466819 cd10214, ASKHA_NBD_ACTL7, nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family. The ACTL7-like family includes ACTL7A, ACTL7B and ACTL9 (also known as ACTL7C). In mammalian, ACTL7A is expressed in a wide variety of adult tissues, while the ACTL7B is expressed in spermatids through the elongation phase of spermatid development. ACTL7A, also called actin-like-7-alpha, or T-ACTIN-2 in mouse, may play an important role in formation and fusion of Golgi-derived vesicles during acrosome biogenesis. ACTL7B, also called actin-like-7-beta, acts as a key regulator of spermiogenesis that is required for male fertility. ACTL9 is a testis-specific protein that plays an important role in fusion of proacrosomal vesicles and perinuclear theca formation
KETKAVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPPQESAKTGDNRKETFVGKELANVEPPLKLVNPLR
HGIVVDWDCVQDIWEYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSL
YSYGRTSGLVVESGHGVSYVVPIHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTDDQLHIVEDIK
KKCCYVALDFEEEMGLPPQEYTVDYELPDGHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKC
DANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCPNDNPIVAASPERKYSVWTGGSILASLKSFQQLW
VRRREYEERGPFVIYRKC
>gnl|CDD|466820 cd10216, ASKHA_NBD_Arp1, nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins. Arp1, also called centractin, actin-like protein, alpha-centractin, actin-RPV, or centrosome-associated actin homolog, may be a component of a multi-subunit centrosomal complex involved in microtubule-based vesicle motility. In yeast, actin-related protein is essential for viability and is associated with the centrosome. In vertebrates, Arp1 is a core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding. The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. ARP1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. It is required for proper orientation of the mitotic spindle. Arp1 is the only actin-related protein known to form actin-like filaments. Human Arp1/centractin is encoded by the ACTR1A gene
NQPVVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHG
IVTDWNDMERIWQYVYSKLQLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLY
ASGRTTGVVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIK
EKACYVALNPQKEEKLEEEKTEKAQYTLPDGSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQK
SDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIRISAPPERLYSTWIGGSILASLSTFKK
MWVSKKEYEEDGARILHRKT
>gnl|CDD|466821 cd10220, ASKHA_NBD_Arp2, nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins. Arp2, also called actin-like protein 2, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp2 is encoded by the ACTR2 gene
KVVVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPILRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMEN
GIVRNWDDMEHLWDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLY
AQGLLTGVVVDSGDGVTHIVPVYEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIK
EKLCYVAYDIELEQKLALETTVLVESYTLPDGRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQ
AADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLYLERVLKGDTERLSKFKIRIEDPPRRKHMVFLG
GAVLADIMKDKDEFWITRQEYEEQGVRVLDK
>gnl|CDD|466822 cd10221, ASKHA_NBD_Arp3-like, nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins. Arp3, also called actin-like protein 3, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp3 and Arp3B are encoded by the ACTR3 and ACTR3B genes respectively. Arp3B is also known as actin-related protein Arp4
AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAIKESAKVGDGQRRSKKGIEDLDFYIGDEALANSPTYALKY
PIRHGIVEDWDLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAV
LALAASWTSRKVGERTLTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIP
PEDSLEVAKRIKERYCYVCPDIVKEFAKYDSDPAKYIKQYTGINSVTGKPYTVDVGYERFLAPEIFFNPE
IASSDFTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGSTMFKDFGRRLQRDVKRIVDARLKASEELSGG
KLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGPSICRH
>gnl|CDD|466823 cd10224, ASKHA_NBD_actin, nucleotide-binding domain (NBD) of actin and similar proteins. Actin is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. It is a highly dynamic structural protein network involved in processes such as cell contraction, cell motility, vesicle trafficking, intracellular organization, cytokinesis, endocytosis and apoptosis. Actin is a monomeric globular protein (G-actin) that reversibly polymerizes to form filaments (F-actin). Each actin protomer binds one molecule of ATP and either calcium or magnesium ions. At low salt concentrations, actin exists as a monomer, and as the salt concentration rises F-actin forms, with the consequent hydrolysis of ATP. F-actin assembly is in constant flux with G-actin association occurring at the barbed end (+) and its disassociation at the pointed end (-). Actin monomers that have been released from the pointed end can be reused, if the ADP is exchanged for ATP. F-actin filaments can assemble into higher order structures, for example branched F-actin, and stress fibers. Actin binding proteins regulate actin filament dynamics by a range of functions including actin severing, depolymerizing, capping, stabilizing and de novo actin polymerization. Actins interaction with myosin is the basis of muscular contraction and many aspects of cell motility. In vertebrates there are three main groups of actin isoforms, alpha, beta and gamma. The alpha actins found in muscle tissues are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton and as mediators of internal cell motility. In plants there are many isoforms which are probably involved in a variety of functions such as cytoplasmic streaming, cell shape determination, tip growth, graviperception, cell wall deposition, etc
AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGI
VTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYAS
GRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEK
LCYVALDFEQEMQTAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKC
DVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTMKIKIVAPPERKYSVWIGGSILASLSTFQQM
WISKQEYDESGPSIV
>gnl|CDD|466824 cd10225, ASKHA_NBD_MreB-like, nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins. MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains
DIGIDLGTANTLVYVKGKGIVLNEPSVVAVDKNTGKVLAVGEEAKKMLGRTPGNIVAIRPLRDGVIADFE
ATEAMLRYFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVKEAAEHAGAREVYLIEEPMAAAIGAGLPIE
EPRGSMVVDIGGGTTEIAVISLGGIVTSRSVRVAGDEMDEAIINYVRRKYNLLIGERTAERIKIEIGSAY
PLDEELSMEVRGRDLVTGLPRTIEITSEEVREALEEPVNAIVEAVRSTLERTPPELAADIVDRGIVLTGG
GALLRGLDELLREETGLPVHVADDPLTCVAKGAGKAL
>gnl|CDD|466825 cd10227, ASKHA_NBD_ParM-like, nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family. ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains
IGIDIGNGNTKVVTGGGKEFKFPSAVAEARESSLDDGLLEDDIIVEYNGKRYLVGELALREGGGGRSTGD
DKKKSEDALLLLLAALALLGDDEEVDVNLVVGLPISEYKEEKKELKKKLLKGLHEFTFNGKERRITINDV
KVLPEGAGAYLDYLLDDDELEDGNVLVIDIGGGTTDILTFENGKPIEESSDTLPGGEEALEKYADDILNE
LLKKLGDELDSADKILLTGGGAELLKDYLKEAYFPNIIVLDDPQFANARGLYK
>gnl|CDD|466826 cd10228, ASKHA_NBD_HSP70_HSPA4_like, nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily. This subgroup includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25). They belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins
VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGR
KFDDPFVQKELKHLPYKVVKLPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVIS
VPSYFTDAERRAVLDAAQIAGLNCLRLLNDTTAVALAYGIYKQDLPAEEEKPRNVVFVDMGHSSLQVSVC
AFNKGKLKVLATAADPNLGGRDFDELLVEHFAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSANATE
LPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEI
IKKVFGKEPSTTLNQDEAVARGCALQCA
>gnl|CDD|466827 cd10229, ASKHA_NBD_HSP70_HSPA12, nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins. The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B
VVVAIDFGTTYSGYAYSFITDPGDIHTMYNWWGAPTGVSSPKTPTCLLLNPDGEFHSFGYEAREKYSDLA
EDEEHQWLYFFKFKMMLLSEKELTRDTKVKAVNGKSMPALEVFAEALRYLKDHALKELRDRSGSSLDEDD
IRWVLTVPAIWSDAAKQFMREAAVKAGLISEENSEQLIIALEPEAAALYCQKLLAEGEEKELKPGDKYLV
VDCGGGTVDITVHEVLEDGKLEELLKASGGPWGSTSVDEEFEELLEEIFGDDFMEAFKQKYPSDYLDLLQ
AFERKKRSFKLRLSPELMKSLFDPVVKKIIEHIKELLEKPELKGVDYIFLVGGFAESPYLQKAVKEAFST
KVKIIIPPEPGLAVVKGAVLFG
>gnl|CDD|466828 cd10230, ASKHA_NBD_HSP70_HYOU1, nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins. This subgroup includes human HYOU1 (also known as human hypoxia up-regulated 1, 170 kDa glucose-regulated protein/GRP170; HSP12A; 150 kDa oxygen-regulated protein/ORP150; GRP-170; ORP-150) and Saccharomyces cerevisiae Lhs1p (also known as Cer1p, SsI1). Mammalian HYOU1 has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. It may play a role as a molecular chaperone and participate in protein folding. HYOU1 functions as a nucleotide exchange factor (NEF) for HSPA5 (also known as BiP, Grp78 or HspA5) and may also act as a HSPA5-independent chaperone. S. cerevisiae Lhs1p, does not have a detectable endogenous ATPase activity like canonical HSP70s, but functions as a NEF for Kar2p; it's interaction with Kar2p is stimulated by nucleotide-binding. In addition, Lhs1p has a nucleotide-independent holdase activity that prevents heat-induced aggregation of proteins in vitro. Members in this subgroup belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs)
AVLGIDLGSEFIKVALVKPGVPFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDL
LGYSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLNVLSLINDNTAAAL
NYGIDRRFENNEPQNVLFYDMGASSTSATVVEFSSVKEKDKGKNKTVPQVEVLGVGWDRTLGGLEFDLRL
ADHLADEFNEKHKKDKDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEEL
CADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAF
YAA
>gnl|CDD|466829 cd10231, ASKHA_NBD_HSP70_YegD-like, nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar proteins. The family includes a group of uncharacterized proteins similar to Escherichia coli chaperone protein YegD that belongs to the heat shock protein 70 family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. YegD lacks the SBD. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some family members are not chaperones but instead, function as NEFs for their Hsp70 partners, other family members function as both chaperones and NEFs
IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEEGAESIYFGNDAIDAYLNDPEEGRLIK
SVKSFLGSSLFDETTIFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDAQAES
RLRDAARRAGFRNVEFQYEPIAAALDYEQRLDREELVLVVDFGGGTSDFSVLRLGPNRTDRRADILATSG
VGIGGDDFDRELALKKVMPHLGRGSTYVSGDKGLPVPAWLYADLSNWHAISLLYTKKTLRLLLDLRRDAA
DPEKIERLLSLVEDQLGHRLFRAVEQAKIALSSADEATLSFDFIEISIKVTITRDEFETAIAFPLARILE
ALERTLNDAGVKPSDVDRVFLTGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLAL
>gnl|CDD|466830 cd10232, ASKHA_NBD_HSP70_ScSsz1p-like, nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex subunit Ssz1 and similar proteins. Ssz1, also called DnaK-related protein Ssz1, heat shock protein 70 homolog Ssz1, or pleiotropic drug resistance protein 13 (PDR13), is a component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones Ssb1/Ssb2 that bind to the nascent polypeptide chain. Ssz1 is required for Zuo1 to function efficiently as a J-protein for Ssb1/Ssb2. It is also involved in pleiotropic drug resistance by post-translational activation of transcription factor PDR1. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis
VVIGISFGNSNSSIAIINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDL
LGTTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLEVLQLIPEPAA
AALAYDLRAETSGDTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHFAKE
FKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFA
DLVTDAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPESTIIRAPTQINPDELIARGAALQASLI
>gnl|CDD|466831 cd10233, ASKHA_NBD_HSP70_HSPA1, nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins. This subfamily includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7, also known as HSP70B), and HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10). They are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The subfamily also includes Saccharomyces cerevisiae heat shock protein Ssa1-4, which may play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs)
AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIG
RKFDDPVVQSDMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVIT
VPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKGERNVLIFDLGGGTFDVSLLTIEDG
IFEVKATAGDTHLGGEDFDNRLVNHFVQEFKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEID
SLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFN
GKELNKSINPDEAVAYGAAVQAAIL
>gnl|CDD|466832 cd10234, ASKHA_NBD_HSP70_DnaK-like, nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar proteins. This subfamily includes Escherichia coli chaperone protein DnaK (also known as heat shock 70 kDa protein/HSP70), human mitochondrial heat shock 70 kDa protein HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74), Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively
IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRFM
GRRYKEVEVERKQVPYPVVSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAY
FNDSQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKKKDEKILVYDLGGGTFDVSILEIGDGVFEVLS
TNGDTHLGGDDFDQRIIDYLADEFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADA
SGPKHLEMKLTRAKFEELTEDLVERTIEPVEQALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFFGKE
PNKGVNPDEVVAIGAAIQGGVLA
>gnl|CDD|466833 cd10235, ASKHA_NBD_HSP70_HscC, nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar proteins. Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. Members in this subfamily belong to the heat shock protein 70 (Hsp70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, Hsp70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Two genes in the vicinity of the HscC gene code for potential cochaperones: J-domain containing proteins, DjlB/YbeS and DjlC/YbeV. HscC and its co-chaperone partners may play a role in the SOS DNA damage response. HscC does not appear to require a NEF
IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILVGRAAKERLVTHPDRTAASFKRFMG
TDKQYRLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLKVERL
INEPTAAALAYGLHKREDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLK
KHRLDFTSLSPSELAALRKRAEQAKRQLSSQDSAEIRLTYRGEELEIELTREEFEELCAPLLERLRQPIE
RALRDAGLKPSDIDAVILVGGATRMPLVRQLIARLFGRLPLSSLDPDEAVALGAAIQAALKAR
>gnl|CDD|466834 cd10236, ASKHA_NBD_HSP70_HscA, nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar proteins. Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HscA's partner J-domain protein is HscB; it does not appear to require a NEF and has been shown to be induced by cold-shock. The HscA-HscB chaperone/co-chaperone pair is involved in [Fe-S] cluster assembly
HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITVGEKAKENAITDPENTISSVK
RLMGRSLADVKEELPLLPYRLVGDENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITV
PAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAALAYGLDQKKEGTIAVYDLGGGTFDISILRLSDGVFE
VLATGGDTALGGDDFDHLLADWILKQIGIDARLDPAVQQALLQAARRAKEALSDADSASIEVEVEGKDWE
REITREEFEELIQPLVKRTLEPCRRALKDAGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINP
DEVVALGAAIQADILAG
>gnl|CDD|466835 cd10237, ASKHA_NBD_HSP70_HSPA13, nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins. HSPA13, also called 70-kDa heat shock protein 13, STCH, microsomal stress-70 protein ATPase core, or stress-70 protein chaperone microsome-associated 60 kDa protein, has peptide-independent ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HSPA13 contains an NBD but lacks an SBD. It may function to regulate cell proliferation and survival and modulate the TRAIL-mediated cell death pathway. The HSPA13 gene is a candidate stomach cancer susceptibility gene; a mutation in the NBD coding region of HSPA13 has been identified in stomach cancer cells. The NBD of HSPA13 interacts with the ubiquitin-like proteins Chap1 and Chap2, implicating HSPA13 in regulating cell cycle and cell death events. HSPA13 is induced by the Ca2+ ionophore A23187
SGILALLLAGYLGQQYLPPPKPKIVGIDLGTTYSCVGVYHAVTGEVEVIPDDDGHKSIPSVVAFTPDGGV
LVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEELEEEAKRYPFKVVNDNIGSAFFEVPLNGSTLVVSPED
IGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAANLAGLEVLRVINEPTAAAMAYGLHKK
SDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYLIDRIAKKFGKTLTDKEDI
QRLRQAVEEVKLNLTNHNSASLSLPLQISLPSAFKVKFKEEITRDLFETLNEDLFQRVLEPIRQVLAEVE
LGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGGMWP
>gnl|CDD|466836 cd10238, ASKHA_NBD_HSP70_HSPA14, nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins. HSPA14, also called HSP70-like protein 1 (Hsp70L1), or heat shock protein HSP60, is a component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, HSPA14 binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis
AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLL
GRSFDDPAVQELKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVL
TVPLDFDEDQRNALKEAAEKAGFNVLRVISEPSAAALAYGIGQDDPTENSNVLVYRLGGTSLDVTVLSVN
NGMYRVLATRTDDNLGGDDFTEALAEHLASEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCS
VESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDL
FPSAEVLSSIPPDEVIAIGAAKQAGLL
>gnl|CDD|466837 cd10241, ASKHA_NBD_HSP70_BiP, nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins. This subfamily includes human BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), Sacchaormyces cerevisiae BiP (also known as Grp78p), Arabidopsis thaliana BiP1-3 (also known as luminal-binding protein 1-3) and related proteins. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). BiP may function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. It appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. BiP may also play a role in apoptosis and cell proliferation. Plant BiP may be required for pollen development and pollen tube growth. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs)
GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRL
IGRKFDDKEVQKDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAV
VTVPAYFNDAQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDN
GVFEVLATNGDTHLGGEDFDQRVMDHFIKLFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEI
ESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFF
NGKEPSRGINPDEAVAYGAAVQAGIL
>gnl|CDD|199834 cd10276, BamB_YfgL, Beta-barrel assembly machinery (Bam) complex component B and related proteins. BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization
PPTDLPEPTPEFDPEVLWSKSVGNGGMAGIDLTPVVAGDMVYAADANGQVSAFNATTGKIIWETSLSGKG
FLGGTPAVGNGKIFVGTESGYLYALDAKDGSELWRTEVSDSQLLSPPTYADGKIYVGTGDGRLYYCNAET
GKVVWNRTSTAPELSLRGGAAPVGAYDVVFVGDGNGTVVALNTGTGVDIWEFSVSEPRGRTELPRMIDSS
VTYVVVGGYLYSTSYQGYLVALDFESGQFLWSRKASGGTSTSTDANGRVYVGDGEGSLYCLDASTGDELW
SQTVLLGRVLSSPAIYVGVYIYVTDNAEGYLYCLKDNDGLTVARVEVDYSQYILQGPAVSDGWLYYGTDD
GYLYALTR
>gnl|CDD|199835 cd10277, PQQ_ADH_I, Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase). This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller
LLNDAKETGNWLTYGRGYNGQRYSPLKQINTDNVKNLVPAWSFSFGGKQRGQESQPIVNDGVMYVTTSYN
RVFAIDAKTGKELWKYKHRLPEDIRPCCDVVNRGVALYGDKVYFGTLDAHLVALDAKTGKVVWKKKVADY
KAGYSMTLAPLVVKGKVIVGVSGGEFGVRGFIAALDAETGKEVWRTYTVPGPGEPGSTDTWPGDAWKTGG
GATWLTGTYDPETNLLYWGVGNPAPWNGDLRPGDNLYTSSVLALDPDTGKIKWHYQYTPNDTWDYDGVNE
PVLFDYTKNGKPVKALVHADRNGFFYVLDRTNGKLIWATPFVKKITWASIDLKTGRPIYDEDKVPPKKGK
TVDFCPSFLGGKNWPPMAYSPDTGLFYVPANHWCMDLTGEPVSYKKGAAYLGAGFTIKPPFEDHIGELQA
IDPTTGKKVWEHKTPLPLWGGVLTTAGGLVFTGTPDGYFRAFDAKTGKELWEFQTGSGIIGPPVTWEVDG
KQYVAVLSGWGGAAPLWGGDMAKLLKNVPQGGSLWVFAL
>gnl|CDD|199836 cd10278, PQQ_MDH, Large subunit of methanol dehydrogenase (moxF). Methanol dehydrogenase is a key enzyme in the utilization of C1 compounds as a source of energy and carbon by bacteria. It catalyzes the oxidation of methanol to formaldehyde, transfering two electrons per methanol to cytochrome c(L) as the acceptor. Methanol dehydrogenase belongs to a family of dehydrogenases with pyrroloquinoline quinone (PQQ) as cofactor, which also includes dehydrogenases specific to other alcohols and membrane-bound glucose dehydrogenases. This alignment model for the large subunit contains an 8-bladed beta-propeller; the functional enzyme forms a heterotetramer composed of two large and two small subunits
WVMPGKDYANTRYSPLAQINKDNVKNLKVAWTFSTGVLRGHEGAPLVVGDTMYVVTPFPNNVYALDLNDP
GKILWKYKPKQDPSAVAVACCDVVNRGLAYADGKIFFNQLDGHLVALDAKTGKEVWKVKNGDPKVGETLT
MAPLVVKDKVIVGISGGEFGVRGYVTAYDLKTGKLVWRAYSTGPDKDVLIGPDFNPFNPHDGGKDLGLST
WPGDAWKIGGGTNWGWYSYDPKLNLVYYGTGNPGPWNPTQRPGDNKWSMTIFARDPDTGEAKWAYQMTPH
DEWDYDGVNEMILVDQTVDGKKRKLLVHFDRNGFVYTLDRTTGELLSAEKFDPVNNWKGVDLKTGRPVKD
PEKSTHMDHNVTDICPSAMGGKDQQPSSYSPKTGLFYVPTNHLCMDYEPFEVNYTAGQPYVGATLAMYPG
PGGHMGQFKAWDPVTGKTKWEIKERFPVWSGTLATAGGLVFYGTLDGWFKAVDAKTGKLLWKFKLPSGII
GNPITYKHDGKQYVAVLSGVGGWAGVGVAAGLRDPTAGLGAVGAFKDLPNYTQMGGTLYVFSL
>gnl|CDD|199837 cd10279, PQQ_ADH_II, PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II). This family of monomeric and soluble type II alcohol dehydrogenases utilizes pyrroloquinoline quinone (PQQ) as a cofactor and is related to ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller
GNWLSYGRDYDEQRFSPLTQINRSNVGQLGLAWYFDLDTNRGQEATPLVVDGVMYVSGPWSVVYALDART
GKLLWQYDPEVDRESGRKACCDVVNRGVAVWDGKVFVGTLDGRLIALDAKTGKEVWSVDTIDPRKPYTIT
GAPRVAKGKVVIGNGGAEFGVRGYVSAYDAETGKLVWRFYTVPGNPAKPFEHASLEAAAATWWTGEWWRT
GGGGTVWDSITYDPELDLLYIGTGNGSPWNRKVRSPGGGDNLFLSSIVALDADTGRYKWHYQTTPGDTWD
YTATQPIILADLEIDGKPRKVLMHAPKNGFFYVLDRATGKLLSAEPFVPVNWATGIDLKTGRPIENPEAR
YTKGPKLVFPGPLGAHNWHPMSYNPDTGLVYIPAQEIPAVYEDDPGDFGYNPLGWNTGITPDATPPPAAA
KRALRKATRGRLVAWDPVTQKAAWRVEHPGPWNGGVLATAGNLVFQGTADGELAAYDARTGEKLWSFDTG
SGIVAAPMTYSVDGEQYVAVLAGWGGAGALSGGPPGAAGKVQNPGRLLVFKLGGKAVLP
>gnl|CDD|199838 cd10280, PQQ_mGDH, Membrane-bound PQQ-dependent glucose dehydrogenase. This bacterial subfamily of enzymes belongs to the dehydrogenase family with pyrroloquinoline quinone (PQQ) as cofactor, and is the only subfamily that is bound to the membrane. Glucose dehydrogenase converts D-glucose to D-glucono-1,5-lactone in a reaction that is coupled with the respiratory chain in the periplasmic oxidation of sugars and alcohols in gram-negative bacteria. Ubiquinone functions as the electron acceptor. The alignment model contains an 8-bladed beta-propeller
WPAYGGDPGGTRYSPLDQITPDNVGKLKVAWTYHTGDLPGPDGNEGTFEATPLKVGGTLYLCTPHNRVIA
LDAATGKELWRFDPKAGADAAPGHQTCRGVSYWEDGAAAAACARRIFFGTGDARLIALDARTGKPCPDFG
DNGVVDLREGLGRVKPGFYSSTSPPTVYGDLVIVGSAVADNQAVDAPSGVIRAFDVRTGKLVWAFDTIPP
PGEAGPDTAGAWYTRGGPNVWAGMSADEKLGLVYLPTGSATPDFYGGDRPGDNLFANSLVALDAATGKRR
WHFQTVHHDLWDYDLPAQPTLVDVPRDGKTVPAVAQPTKQGFVFVLDRRTGKPLWPVEERPVPQGDVPGE
RTSPTQPFPTLPPPFARQGLTEDDMWGATPFDQLACRIQFRSLRYEGLFTPPSLDGTLIFPGNDGGANWG
GAAVDPERGILYVNSNRLPFVIQLVPRAPGDPAGVAGGGEGGGGGGGPSPQAGTPYGVGRGRFLSPLGLP
CQAPPWGTLTAIDLNTGKILWQVPLGTVPDLGPKGIPLPIPTGTPNLGGPVVTAGGLVFIAATQDNYLRA
FDKATGKELWEARLPAGGQATPMTYEVDGKQYVVIAAGGHGSLGTKRGDSVIAYAL
>gnl|CDD|197336 cd10281, Nape_like_AP-endo, Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases. This subfamily includes Neisseria meningitides Nape and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Neisseria meningitides Nape and NExo. Nape, found in this subfamily, is the dominant AP endonuclease. It exhibits strong AP endonuclease activity, and also exhibits 3'-5'exonuclease and 3'-deoxyribose phosphodiesterase activities
MRVISVNVNGIRAAAKKGFLEWLAAQDADVVCLQEVRAQEEQLDDDFFEPEGYNAYFFDAEKKGYAGVAI
YSRTQPKAVIYGLGFEEFDDEGRYIEADFDNVSVASLYVPSGSSGDERQEAKMAFLDAFLEHLKELRRKR
REFIVCGDFNIAHTEIDIKNWKANQKNSGFLPEERAWLDQVFGELGYVDAFRELNPDEGQYTWWSNRGQA
RANNVGWRIDYQIATPGLASKVVSAWIYREERFSDHAPLIVDY
>gnl|CDD|197337 cd10282, DNase1, Deoxyribonuclease 1. Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a Ca2+, Mg2+/Mn2+-dependent secretory endonuclease, first isolated from bovine pancreas extracts. It cleaves DNA preferentially at phosphodiester linkages next to a pyrimidine nucleotide, producing 5'-phosphate terminated polynucleotides with a free hydroxyl group on position 3'. It generally produces tetranucleotides. DNase1 substrates include single-stranded DNA, double-stranded DNA, and chromatin. This enzyme may be responsible for apoptotic DNA fragmentation. Other deoxyribonucleases in this subfamily include human DNL1L (human DNase I lysosomal-like, also known as DNASE1L1, Xib, and DNase X), human DNASE1L2 (also known as DNAS1L2), and DNASE1L3 (also known as DNAS1L3, nhDNase, LS-DNase, DNase Y, and DNase gamma) . DNASE1L3 is implicated in apoptotic DNA fragmentation. DNase I is also a cytoskeletal protein which binds actin. A recombinant form of human DNase1 is used as a mucoactive therapy in patients with cystic fibrosis; it hydrolyzes the extracellular DNA in sputum and reduces its viscosity. Mutations in the gene encoding DNase1 have been associated with Systemic Lupus Erythematosus, a multifactorial autoimmune disease. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds
RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERL
GRSSYKEQYAFIYRSDKVSVLESYQYDDGDEGTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAE
IDALYDVYDDVKQRWREDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDR
IVVAGSLLQSAVVPGSAGVFDFDKEFGLTEEEALAVSDHYPVEVEL
>gnl|CDD|197338 cd10283, MnuA_DNase1-like, Mycoplasma pulmonis MnuA nuclease-like. This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds
LRIASWNILNFGNSKGKEKNPAIAEIISAFDLDLIALQEVMDNGGGLDALAKLVNELNKPGGTWKYIVSD
KTGGSSGDKERYAFLYKSSKVRKVGKAVLEKDSNTDGFARPPYAAKFKSGGTGFDFTLVNVHLKSGGSSK
SGQGAKRVAEAQALAEYLKELADEDPDDDVILLGDFNIPADEDAFKALTKAGFKSLLPDSTNLSTSFKGY
ANSYDNIFVSGNLKEKFSNSGVFDFNILVDEAGEEDLDYSKWRKQISDHDPVWVEF
>gnl|CDD|198434 cd10284, growth_hormone_like, Somatotropin/prolactin hormone family. The somatotropin/prolactin hormone family includes growth hormones 1 and 2, prolactin, prolactin 2, and other members that play vital roles in a variety of processes, including growth control. They are long-chain class-I helical cytokines, most of which are secreted by the pituitary gland, and are active as monomers, binding to cellular receptors with EpoR-like ligand binding domains
LFDRAIPHAERVYHLSSEAYAEFEEKYIPGENPPNNVVMSCHTASIPTPSSKEEAQQKSDKELLRISLEL
LQSWSEPLLHLHTVLANSKGTSLALLPKAKQVSEMLKLLEDGVETLSERIKDLPLEFNSVGALWSVDETH
NSLRRMHDYDLLSCFKKDAHKVETYLKILKCRRFEHSC
>gnl|CDD|198435 cd10285, somatotropin_like, Somatotropin or growth hormone (GH), placental lactogen, and related pituitary gland hormones. Growth hormone (GH) or somatotropin is a peptide hormone synthesized by the pituitary gland, which mediates anabolic effects in development. GH is known to activate, via binding to specific cellular receptors, the MAPK/ERK and JAK-STAT signaling pathways. Via the latter, it triggers the secretion of insulin-like growth factor 1 (mostly in the liver). Besides increasing body height, GH has been shown to have a host of other effects
LFSNAVLRAQHLHQLAADIYKDFERSYIPEEQRQSNKNSPAAFCYSESIPAPTGKDETQQKSDLELLRIS
LLLIQSWLKPVQFLSSVFTNQLHFGSSDRIYEKLKDLEEGIQTLIRELEDGSPRGGQLLKQTYSKFDVNL
RSDEALLKNYGLLSCFKKDMHKVETYLRVMKCRRFPESNC
>gnl|CDD|198436 cd10286, somatolactin, Somatolactin (SL) and somatolactin-like proteins. This family of hormones specific to Actinopterygii is expressed in the pars intermedia bordering the neurohypophysis (posterior pituitary). Somatolactin appears to be involved in acid-base regulation, but much of its physiological role remains to be understood
GSPLDCPDQDTGGRCCSISLEKLLDRAIQHAELIYRVSEESCTLFEEMFIPFSVRALLIQEGNACSTKTV
SIPTSKTEIQQISDKWLLHSVLILVQFWIDPLVDLQTSLDRYDNAPSALLNKTKWMSTKLMNLEQGVLVL
IRKMLGEGMLLNNESPADTLDHFVMSDMLESVLRDYTLLSCFKKDAHKVETFLKLLKCRQTDRLNCS
>gnl|CDD|198437 cd10287, prolactin_2, Vertebrate, non-mammalian prolactin 2 (PRL2). A functionally uncharacterized subfamily of the growth-hormone-like helical cytokines, which is found in vertebrata (except for mammals). The protein has been shown to be expressed in the zebrafish eye and brain, but not the pituitary gland, and might play a role in retina development
VADLFDRVIQHSSRMHSLSSELHWELEQYFLPSRNIRRKRKCHTAGILTPNGKENAQKLEREELTEVILR
LLGAWREPLSHFHQSMGHDKDFNSYSPGKAKQMSDMVHELRDGVEKVTEKMQLLGVISNSLGGLSPEDAG
PSAISGHLDAMSDYDLLHCFRRDSNKVQNYLKILKCRIFPESSC
>gnl|CDD|198438 cd10288, prolactin_like, Prolactin (PRL or PRL1), chorionic somatomammotropin, and related pituitary gland hormones. Prolactin is primarily responsible for stimulating milk production and breast development in mammals. Aside from roles in reproduction, various functions have been attributed to prolactin, more than for other pituitary gland hormones combined. These are roles in growth and development, metamorphosis, metabolism of lipids, carbohydrates, and steroids, brain biochemistry and even immunoregulation, among others. Most of these roles are poorly understood, but it has become clear that many prolactin-like hormones are actually produced in the placenta and not the pituitary
LPICPAGNGGCQLSLEDLFDRAVSLSHNIHNLSSEMFNEFDENYAQGRGFVDRALTSCHTSSLTTPENKE
QAQQIKNEDLLKLIISLLRSWNEPLKHLVTELSSMKGAPDTILSKAKEIEEKNKELLEGLKRILSRVQPG
IEENEDYPVWSGLPSLQSSDEDSRLFAFYNLFHCLRRDSHKIDTYLKLLKCRIIHGNDC
>gnl|CDD|198322 cd10289, GST_C_AaRS_like, Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA synthetases and similar domains. Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl-tRNA synthetase (AaRS)-like subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of some eukaryotic AaRSs, as well as similar domains found in proteins involved in protein synthesis including Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2 (AIMP2), AIMP3, and eukaryotic translation Elongation Factor 1 beta (eEF1b). AaRSs comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. AaRSs in this subfamily include GluRS from lower eukaryotes, as well as GluProRS, MetRS, and CysRS from higher eukaryotes. AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex found in higher eukaryotes. The GST_C-like domain is involved in protein-protein interactions, mediating the formation of aaRS complexes such as the MetRS-Arc1p-GluRS ternary complex in lower eukaryotes and the multi-aaRS complex in higher eukaryotes, that act as molecular hubs for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain
EAAQVDQWLDLAGSLLKGKELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYPSGQKLSDKEKKKFP
HVTRWFNHIQNL
>gnl|CDD|198323 cd10290, GST_C_MetRS_N_fungi, Glutathione S-transferase C-terminal-like, alpha helical domain of Saccharomycetales Methionyl-tRNA synthetase. Glutathione S-transferase (GST) C-terminal domain family, Saccharomycetales Methionyl-tRNA synthetase (MetRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of Saccharomycetales MetRS. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. MetRS is a class I aaRS, containing a Rossman fold catalytic core. It recognizes the initiator tRNA as well as the Met-tRNA for protein chain elongation. The GST_C-like domain of MetRS from Saccharomycetales is involved in protein-protein interactions, to mediate the formation of the the MetRS-Arc1p-GluRS ternary complex which is considered an evolutionary intermediate between prokaryotic aaRS and the multi-aaRS complex found in higher eukaryotes. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain
NAILRYVLNDFEGQQSDEYQYALSSLEALLYHKDTLPEHAKELVTKSLENYLVSLEEPLTATRLIIFANA
YALNPAAVNARFAILPAKLEKALET
>gnl|CDD|198324 cd10291, GST_C_YfcG_like, C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins. Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG and related proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG does not contain a redox active cysteine residue and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified
ERYAVLQWLMWQMGGLGPMQGQAHHFKRYAPEKIPYAIKRYTNETKRLYGVLDRRLAKSKYLAGDEYSIA
DIAIWPWVARHEWQGIDLADFPNLKRWFERLAARPAVQKG
>gnl|CDD|198325 cd10292, GST_C_YghU_like, C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and related uncharacterized proteins. Glutathione S-transferase (GST) C-terminal domain family, YghU-like subfamily; composed of the Escherichia coli YghU and related proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YghU is one of nine GST homologs in the genome of Escherichia coli. It is similar to Escherichia coli YfcG in that it has poor GSH transferase activity towards typical substrates. It shows modest reductase activity towards some organic hydroperoxides. Like YfcG, YghU also shows good disulfide bond oxidoreductase activity comparable to the activities of glutaredoxins and thioredoxins. YghU does not contain a redox active cysteine residue, and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YghU reveals two GSH molecules bound in its active site
KRTETLNWLFWQMGSAPYLGGGFGHFYSYAPVKIEYAIDRFTMEAKRQLDVLDRQLATHKYLAGDEYTIA
DMAIWPWYGGLALGSLYDAAEFLDVDEYKHVQRWAKDIAARPAVKRGR
>gnl|CDD|198326 cd10293, GST_C_Ure2p, C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Ure2p subfamily; composed of the Saccharomyces cerevisiae Ure2p and related fungal proteins. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of GSH with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain
EYYQAKQWLFFQASGQGPYWGQAGWFNVFHAEKVPSAIERYTNEIRRVLGVLETALAERYRVWLVGDKFT
IADLAFVPWNNVVDMIFIDPELDIKKEFPHVYKWLKRMLARPAVKKA
>gnl|CDD|198327 cd10294, GST_C_ValRS_N, Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA synthetase. Glutathione S-transferase (GST) C-terminal domain family, Valyl-tRNA synthetase (ValRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of human ValRS and its homologs from other vertebrates such as frog and zebrafish. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. They typically form large stable complexes with other proteins. ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF. The GST_C-like domain of ValRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. ValRSs from prokaryotes and lower eukaryotes, such as fungi and plants, do not appear to contain this GST_C-like domain
ACALVWQWVSFADNELTPAACAAAFPLLGLSGSDKQNQQRSLAELQRVLKVLDCYLKLRTYLVGEAITLA
DIAVACALLLPFKYVLDPARRESLLNVTRWFLTCVNQPEFLAVLGEVSLCEKA
>gnl|CDD|198328 cd10295, GST_C_Sigma, C-terminal, alpha helical domain of Class Sigma Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, Class Sigma; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation, and mediation of allergy and inflammation
ELEQCLVDALVDTLDDFMSCFPWAEKKQDVKEKMFNEALTGPAPHLLKDLDTYLGGREWLVGKSVTWADF
YWDTCSTTLLSFKPDLLKNYPRLVALRDKV
>gnl|CDD|198329 cd10296, GST_C_CLIC4, C-terminal, alpha helical domain of Chloride Intracellular Channel 4. Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 4 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC4, also known as p64H1, is expressed ubiquitously and its localization varies depending on the nature of the cells and tissues, from the plasma membrane to subcellular compartments including the nucleus, mitochondria, ER, and the trans-Golgi network, among others. In response to cellular stress such as DNA damage and senescence, cytoplasmic CLIC4 translocates to the nucleus, where it acts on the TGF-beta pathway. Studies on knockout mice suggest that CLIC4 also plays an important role in angiogenesis, specifically in network formation, capillary sprouting, and lumen formation. CLIC4 has been found to induce apoptosis in several cell types and to retard the growth of grafted tumors in vivo
HPESNTAGMDIFAKFSAYIKNSRPEANEALERGLLKTLQKLDEYLNSPLPDEIDENSMEDIKFSTRKFLD
GNEMTLADCNLLPKLHIVKVVAKKYRNFEIPKEMTGIWRYLSNAYSRDEFTNTCPSDKEIEIAYSDVAKR
L
>gnl|CDD|198330 cd10297, GST_C_CLIC5, C-terminal, alpha helical domain of Chloride Intracellular Channel 5. Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 5 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC5 exists in two alternatively-spliced isoforms, CLIC5A or CLIC5B (also called p64). It is expressed at high levels in hair cell stereocilia and is associated with the actin cytoskeleton and ezrin. A recessive mutation in the CLIC5 gene in mice led to the lack of coordination and deafness, due to a defect in the basal region of the hair bundle causing stereocilia to degrade. CLIC5 is therefore essential for normal inner ear function. CLIC5 is also highly expressed in podocytes where it is colocalized with the ezrin/radixin/moesin (ERM) complex. It is essential for foot process integrity, and for podocyte morphology and function
HRESNTAGIDIFSKFSAYIKNTKQQANAALEKGLTKALKKLDDYLNTPLPEEIDADSTEEEKVSNRKFLD
GDELTLADCNLLPKLHVVKIVAKKYRNFEIPSDMTGVWRYLKNAYARDEFTNTCAADKEIELAYADVAKR
L
>gnl|CDD|198331 cd10298, GST_C_CLIC2, C-terminal, alpha helical domain of Chloride Intracellular Channel 2. Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 2 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC2 contains an intramolecular disulfide bond and exists as a monomer regardless of redox conditions, in contrast to CLIC1 which forms a dimer under oxidizing conditions. It is expressed in most tissues except the brain, and is highly expressed in the lung, spleen, and in cardiac and skeletal muscles. CLIC2 interacts with ryanodine receptors (cardiac RyR2 and skeletal RyR1) and modulates their activity, suggesting that CLIC2 may function in the regulation of calcium release and signaling in cardiac and skeletal muscles
YKESFDVGSDIFAKFSAYIKNSPENNANQEKALLREFKRLDDYLNTPLPEEIDHDSAENITVSKRKFLDG
DRLTLADCNLLPKLHVIKVAAKKYCDFDIPADFTGVWRYLNNAYEREEFSQTCPADIEIEKAYASVAK
>gnl|CDD|198332 cd10299, GST_C_CLIC3, C-terminal, alpha helical domain of Chloride Intracellular Channel 3. Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 3 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC3 is highly expressed in placental tissues, and may play a role in fetal development
YKESNTAGNDVFHKFSAFIKNPVPAQDDALQKKLLRALLKLDSYLLTPLPHELAQNPHLSESQRRFLDGD
ALTLADCNLLPKLHIVKVVCKHYRQFEIPAELKGVTRYLDSASQEKEFKYTCPNSAEILLAYR
>gnl|CDD|198333 cd10300, GST_C_CLIC1, C-terminal, alpha helical domain of Chloride Intracellular Channel 1. Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 1 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Soluble CLIC1 is monomeric and adopts a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. Upon oxidation, the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. The CLIC1 dimer bears no similarity to GST dimers. The redox-controlled structural rearrangement exposes a large hydrophobic surface, which is masked by dimerization in vitro. In vivo, this surface may represent the docking interface of CLIC1 in its membrane-bound state. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity. CLIC1 is widely expressed in many tissues and its subcellular localization is dependent on cell type and cell cycle phase. It acts as a sensor of cell oxidation and appears to have a role in diseases that involve oxidative stress including tumorigenic and neurodegenerative diseases
NPESNTAGLDVFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDENSAEDEGVSQRKFLD
GNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAK
>gnl|CDD|198334 cd10301, GST_C_CLIC6, C-terminal, alpha helical domain of Chloride Intracellular Channel 6. Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 6 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC6 is expressed predominantly in the stomach, pituitary, and brain. It interacts with D2-like dopamine receptors directly and through scaffolding proteins. CLIC6 may be involved in the regulation of secretion, possibly through chloride ion transport regulation
HPESNSAGNDVFAKFSAFIKNPRKDANENLEKNLLKALRKLDNYLNTPLPDEIDAYSTEDITVSDRKFLD
GNELTLADCNLLPKLHIIKVVAKKYRNFEFPTEMTGIWRYLNNAYARDEFTNTCPADQEIEYAYSDVAKR
>gnl|CDD|198335 cd10302, GST_C_GDAP1L1, C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein 1-like 1. Glutathione S-transferase (GST) C-terminal domain family, Ganglioside-induced differentiation-associated protein 1-like 1 (GDAP1L1) subfamily; GDAP1L1 is a paralogue of GDAP1 with about 56% sequence identity and 70% similarity. It's function is unknown. Like GDAP1, it does not exhibit GST activity using standard substrates. GDAP1 was originally identified as a highly expressed gene at the differentiated stage of GD3 synthase-transfected cells. More recently, mutations in GDAP1 have been reported to cause both axonal and demyelinating autosomal-recessive Charcot-Marie-Tooth (CMT) type 4A neuropathy. CMT is characterized by slow and progressive weakness and atrophy of muscles. Sequence analysis of GDAP1 shows similarities and differences with GSTs; it appears to contain both N-terminal thioredoxin-fold and C-terminal alpha helical domains of GSTs, however, it also contains additional C-terminal transmembrane domains unlike GSTs. GDAP1 is mainly expressed in neuronal cells and is localized in the mitochondria through its transmembrane domains
PQLTEPYLSKQKKLMAKILEHDNVNYLKKILGELAMVLDQIEAELEKRKLEYEGQKCELWLCGCIFTLAD
VLLGATLHRLKFLGLSKKYWEDGSRPNLQSFFERVQKRYAF
>gnl|CDD|198336 cd10303, GST_C_GDAP1, C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein 1. Glutathione S-transferase (GST) C-terminal domain family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; GDAP1 was originally identified as a highly expressed gene at the differentiated stage of GD3 synthase-transfected cells. More recently, mutations in GDAP1 have been reported to cause both axonal and demyelinating autosomal-recessive Charcot-Marie-Tooth (CMT) type 4A neuropathy. CMT is characterized by slow and progressive weakness and atrophy of muscles. Sequence analysis of GDAP1 shows similarities and differences with GSTs; it appears to contain both N-terminal thioredoxin-fold and C-terminal alpha helical domains of GSTs, however, it also contains additional C-terminal transmembrane domains unlike GSTs. GDAP1 is mainly expressed in neuronal cells and is localized in the mitochondria through its transmembrane domains. It does not exhibit GST activity using standard substrates
PDLQDAYIAKQKRLKSKLLDHDNIKYLKKILDELEKVLDQVETELQRRNEETPEEGQQPWLCGEFFSLAD
VSLAVTLHRLKFLGLARRNWGNGKRPNLETYYERVLKRKTF
>gnl|CDD|198337 cd10304, GST_C_Arc1p_N_like, Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA synthetase cofactor 1 and similar proteins. Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase cofactor 1 (Arc1p)-like subfamily; Arc1p, also called GU4 nucleic binding protein 1 (G4p1) or p42, is a tRNA-aminoacylation and nuclear-export cofactor. It contains a domain in the N-terminal region with similarity to the C-terminal alpha helical domain of GSTs. This domain mediates the association of the aminoacyl tRNA synthetases (aaRSs), MetRS and GluRS, in yeast to form a stable stoichiometric ternany complex. The GST_C-like domain of Arc1p is a protein-protein interaction domain containing two binding sites which enable it to bind the two aaRSs simultaneously and independently. The MetRS-Arc1p-GluRS complex selectively recruits and aminoacylates its cognate tRNAs without additional cofactors. Arc1p also plays a role in the transport of tRNA from the nucleus to the cytoplasm. It may also control the subcellular distribution of GluRS in the cytoplasm, nucleoplasm, and the mitochondrial matrix
PEQSAEVAQWLSVAKSGPVSKDVQETLGQLNLHLRTRTFLLGTGKPSVADVAVFEAVLPVVKEWSDEVKT
GYAKYRHILRWVDYVQNLLLFIPEADKIEV
>gnl|CDD|198338 cd10305, GST_C_AIMP3, Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 3. Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 3 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP3, also called p18 or eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1), contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It specifically interacts with methionyl-tRNA synthetase (MetRS) and is translocated to the nucleus during DNA synthesis or in response to DNA damage and oncogenic stress. In the nucleus, it interacts with ATM and ATR, which are upstream kinase regulators of p53. It appears to work against DNA damage in cooperation with AIMP2, and similar to AIMP2, AIMP3 is also a haploinsufficient tumor suppressor. AIMP3 transgenic mice have shorter lifespans than wild-type mice and they show characteristics of progeria, suggesting that AIMP3 may also be involved in cellular and organismal aging
AEERAQVDQWLEYRVTQVAPASDKADAKSLLKELNSYLQDRTYLVGHKLTLADVVLYYGLHPIMKDLSPQ
EKEQYLNVSRWFDHVQHLPGIRQHLPLINFT
>gnl|CDD|198339 cd10306, GST_C_GluRS_N, Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase. Glutathione S-transferase (GST) C-terminal domain family, Glutamyl-tRNA synthetase (GluRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluRS from lower eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluRS is involved in protein-protein interactions. This domain mediates the formation of the MetRS-Arc1p-GluRS ternary complex found in lower eukaryotes, which is considered an evolutionary intermediate between prokaryotic aaRS and the multi-aaRS complex found in higher eukaryotes. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain
NGDKEQVAEWIDFATTLLVLKDFKALSQALEELDSHLTLRTFIVGYSLSLADIAVWGALRGNGVAGSLIK
NKVYVNLSRWFSFLESL
>gnl|CDD|198340 cd10307, GST_C_MetRS_N, Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase from higher eukaryotes. Glutathione S-transferase (GST) C-terminal domain family, Methionyl-tRNA synthetase (MetRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of MetRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. MetRS is a class I aaRS, containing a Rossman fold catalytic core. It recognizes the initiator tRNA as well as the Met-tRNA for protein chain elongation. The GST_C-like domain of MetRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain
DDDLSNQWLEWEAWLLQPALSLALALTHVQGKKSEADLNTVLNALVHLDQSLLKKSTPLLGDKLSSADVV
VWSALYPLGTDKSALPENLDNLRRWFQNVSTL
>gnl|CDD|198341 cd10308, GST_C_eEF1b_like, Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation Elongation Factor 1 beta. Glutathione S-transferase (GST) C-terminal domain family, eukaryotic translation Elongation Factor 1 beta (eEF1b) subfamily; eEF1b is a component of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. eEF1b contains a GST_C-like alpha helical domain at the N-terminal region and a C-terminal guanine nucleotide exchange domain. The GST_C-like domain likely functions as a protein-protein interaction domain, similar to the function of the GST_C-like domains of EF1Bgamma and various aminoacyl-tRNA synthetases (aaRSs) from higher eukaryotes
KANLATESKHKLLLGVSLDGSFADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATKFP
HLARWYRHIASF
>gnl|CDD|198342 cd10309, GST_C_GluProRS_N, Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional Glutamyl-Prolyl-tRNA synthetase. Glutathione S-transferase (GST) C-terminal domain family, bifunctional GluRS-Prolyl-tRNA synthetase (GluProRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluProRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluProRS may be involved in protein-protein interactions, mediating the formation of the multi-aaRS complex in higher eukaryotes. The multi-aaRS complex acts as a molecular hub for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain
EQTEVDHWISFSAGRLSCDQDFSSALSYLDKALSLRTYLVGNSLTLADFAVWAALRGNGEWLASKEKYVN
VTRWFKFISSQ
>gnl|CDD|198343 cd10310, GST_C_CysRS_N, Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase from higher eukaryotes. Glutathione S-transferase (GST) C-terminal domain family, Cysteinyl-tRNA synthetase (CysRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of CysRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of CysRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. CysRSs from prokaryotes and lower eukaryotes do not appear to contain this GST_C-like domain
ASSGQAAFDYGFILSISEEAARAEALNEYLSTRSYLQGFGPSQADVEVFRLLSRPPADRLVHVLRWYRHI
EAL
>gnl|CDD|197304 cd10311, PLDc_N_DEXD_c, N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. All members of this subfamily are uncharacterized. Other characterized members of the superfamily that have a related domain architecture (containing a DEAD/DEAH box helicase domain), include the DNA/RNA helicase superfamily II (SF2) and Res-subunit of type III restriction endonucleases. In addition to the helicase-like region, members of this subfamily also contain one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in the N-terminal putative catalytic domain. The HKD motif characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily
NNGTDRVGDDLKKELKKGSKLSIAAASFSIYAFEELKKELEKIDELRFIFTSPTFVKDKVKKEKEFYIPR
LSRERSLLGTEFEIKLRNELQQRAIARECAEWIRKKAEFRSNRSGSVPQGFIVVENKDEVIAYMGSNEFT
TDGLGLTPGNALSLIQ
>gnl|CDD|197339 cd10312, Deadenylase_CCR4b, C-terminal deadenylase domain of CCR4b, also known as CCR4-NOT transcription complex subunit 6-like. This subfamily contains the C-terminal catalytic domain of the deadenylase, CCR4b, also known as CCR4-NOT transcription complex subunit 6-like (CNOT6L). CCR4 belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. CCR4 is the major deadenylase subunit of the CCR4-NOT transcription complex, which contains two deadenylase subunits and several noncatalytic subunits. The other deadenylase subunit, Caf1, is a DEDD-type protein and does not belong in this superfamily. There are two vertebrate CCR4 proteins, CCR4a (also called CCR4-NOT transcription complex subunit 6 or CNOT6) and CCR4b. CCR4b associates with other components, such as CNOT1-3 and Caf1, to form a CCR4-NOT multisubunit complex, which regulates transcription and mRNA degradation. The nuclease domain of CCR4b exhibits Mg2+-dependent deadenylase activity with strict specificity for poly (A) RNA as substrate. CCR4b is mainly localized in the cytoplasm. It regulates cell growth and influences cell cycle progression by regulating p27/Kip1 mRNA levels. It contributes to the prevention of cell death by regulating insulin-like growth factor-binding protein 5
VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYD
GFFSPKSRAKIMSEQERKHVDGCAIFFKTEKFSLVQKHTVEFNQVAMANSEGSEAMLNRVMTKDNIGVAV
VLEVHKELFGAGMKPIHAADKQLLIVANAHMHWDPEYSDVKLIQTMMFVSELKNILEKASSRPGSPTADP
NSIPLVLCADLNSLPDSGVVEYLSNGGVADNHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAY
ENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQWLVENNITGCPHPHIPSDHFSLLTQLEL
>gnl|CDD|197340 cd10313, Deadenylase_CCR4a, C-terminal deadenylase domain of CCR4a, also known as CCR4-NOT transcription complex subunit 6. This subfamily contains the C-terminal catalytic domain of the deadenylase, CCR4a, also known as CCR4-NOT transcription complex subunit 6 (CNOT6). CCR4 belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. CCR4 is the major deadenylase subunit of the CCR4-NOT transcription complex, which contains two deadenylase subunits and several noncatalytic subunits. The other deadenylase subunit, Caf1, is a DEDD-type protein and does not belong in this superfamily. There are two vertebrate CCR4 proteins, CCR4a and CCR4b (also called CNOT6-like or CNOT6L). CCR4a associates with other components, such as CNOT1-3 and Caf1, to form a CCR4-NOT multisubunit complex, which regulates transcription and mRNA degradation. The nuclease domain of CCR4a exhibits Mg2+-dependent deadenylase activity with specificity for poly (A) RNA as substrate. CCR4a is a component of P-bodies and is necessary for foci formation of various P-body components. It also plays a role in cellular responses to DNA damage, by regulating Chk2 activity
VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIMQEILSCNADIISLQEVETEQYYSFFLVELKERGYN
GFFSPKSRARTMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAV
LLELRKELIEMSSGKPHLGMEKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLG
ETGTIPLVLCADLNSLPDSGVVEYLSTGGVETNHKDFKELRYNESLTNFSCNGKNGTTNGRITHGFKLKS
AYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLGILGPLDHHWLVENNISGCPHPLIPSDHFSLFAQLEL
>gnl|CDD|198457 cd10314, FAM20_C, C-terminal putative kinase domain of FAM20 (family with sequence similarity 20) proteins. This family contains the C-terminal domain of FAM20A, -B, -C and related proteins. FAM20A may participate in enamel development and gingival homeostasis, FAM20B in proteoglycan production, and FAM20C in bone development. FAM20B is a xylose kinase that may regulate the number of glycosaminoglycan chains by phosphorylating the xylose residue in the glycosaminoglycan-protein linkage region of proteoglycans. FAM20C, also called Dentin Matrix Protein 4, is abundant in the dentin matrix, and may participate in the differentiation of mesenchymal precursor cells into functional odontoblast-like cells. Mutations in FAM20C are associated with lethal Osteosclerotic Bone Dysplasia (Raine Syndrome), and mutations in FAM20A with Amelogenesis imperfecta (AI) and Gingival Hyperplasia Syndrome. The C-terminal domains of members of this family are putative kinase domains, based on mutagenesis of the C-terminal domain of Drosophila Four-Jointed, a related Golgi kinase. This domain family is also known as DUF1193
FISPANNTCFYGKCYYCKTEEAVCGNPDLLEGSLTAFLPDLSLLKKWRHPWRRTYHKRKKAEWEVDPDYC
DKVKKTPPYDSGRRLLDLIDMAIFDFLIGNMDRHHYETFEKFGNETFLIHLDNGKSFGNPSHDELSILAP
LYQCCLIRKSTWLRLQLLAKGGGSLSDLLRESLSHDPLSPVLTEPHLDALDRRLLIVLATVEDCIEKNG
>gnl|CDD|199215 cd10315, CBM41_pullulanase, Family 41 Carbohydrate-Binding Module from pullulanase-like enzymes. Pullulanases (EC 3.2.1.41) are a group of starch-debranching enzymes, catalyzing the hydrolysis of the alpha-1,6-glucosidic linkages of alpha-glucans, preferentially pullulan. Pullulan is a polysaccharide in which alpha-1,4 linked maltotriosyl units are combined via an alpha-1,6 linkage. These enzymes are of importance in the starch industry, where they are used to hydrolyze amylopectin starch. Pullulanases consist of multiple distinct domains, including a catalytic domain belonging to the glycoside hydrolase (GH) family 13 and carbohydrate-binding modules (CBM), including CBM41
NTVRVHYKRPDGDYDGWGLWLWGDGACPTWWGGAYAFTGDDDYGAYADVPLKEDATKIGFIVRKGTDEKD
GGGDRFIDLLKDGGNEVWIVQGDETVYYSP
>gnl|CDD|199904 cd10316, RGL4_M, Middle domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold. Both the middle domain represented by this model and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11
GRGTVSGRLLLPDGASAAIAVVGLANPGEQGSQFETKGYQYWTEADSDGRFTIPNVRPGTYRLTAYADGI
FGYVAQDTVTVTAGGTTALGDL
>gnl|CDD|199905 cd10317, RGL4_C, C-terminal domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold. Both the middle and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11
WQIGTPDRTAAEFRNGDLLPNYHPSDWRLAPPGDLTYTVGSSDSDFDWYYAQSVNGPWTIRFDLTAVQAT
GGATLRIALAGASAGGRPQVRVNDNGPLLPTAPTGNDSRGIYRGAYRGNYHLYEFDIPASLLVAGTNTIT
LTVVSGSSLSPGVMYDAIRLE
>gnl|CDD|199906 cd10318, RGL11, Rhamnogalacturonan lyase of the polysaccharide lyase family 11. The rhamnogalacturonan lyase of the polysaccharide lyase family 11 (RGL11) cleaves glycoside bonds in polygalacturonan as well as RG (rhamnogalacturonan) type-I through a beta-elimination reaction. Functionally characterized members of this family, YesW and YesX from Bacillus subtilis, cleave glycoside bonds between rhamnose and galacturonic acid residues in the RG-I region of plant cell wall pectin. YesW and YesX work synergistically, with YesW cleaving the glycoside bond of the RG chain endolytically, and YesX converting the resultant oligosaccharides through an exotype reaction. This domain is sometimes found in architectures with non-catalytic carbohydrate-binding modules (CBMs). There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain through a beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11
MEYLDRGLVAVKTGNGVFVSWRLLGTDPDGIGFNVYRDGVKLNSAPITNSTNFLDAKGTASSKYTVRAVV
NGVEQTESESVEVWANPYLEIPLNKPAGGTTPDGETYTYTANDASVGDLDGDGEYEIVLKWDPSNSKDNS
QSGYTGNVYLDAYKLDGTRLWRIDLGKNIRAGAHYTQFMVYDLDGDGKAEVAVKTADGTKDGTGNVIGDA
SADYRNSSGYILSGPEYLTVFDGLTGAALATVPYVPGRGTVSSWGDSYGNRVDRFLAGVAYLDGQRPSLV
MARGYYTRTVLAAYDFRNGKLKQRWTFDSSDSGNEAYAGQGNHNLSVADVDGDGKDEIIYGSATIDHDGT
GLYSTGLGHGDALHVGDFDPSRPGLEVFQVHEDKGGPYGEAFRDAATGEILWGVYGGGDTGRGMAGDIDP
RYPGAEVWSFGGGLYNAKGNKISSDRPPSTNFGIWWDGDLLRELLDGTTIDKWNWENEKSDRLLTASGVT
SNNGTKGTPCLSADILGDWREEVIWRTEDSSELRIYTTTIPTDHRLYTLMHDPQYRTAIAWQNVAYNQPP
HPSF
>gnl|CDD|198439 cd10319, EphR_LBD, Ligand Binding Domain of Ephrin Receptors. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). They are subdivided into 2 groups, A and B type receptors, depending on their ligand ephrin-A or ephrin-B, respectively. In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis
VVLLDTTLATSDLGWLTYPYGHGGWDEESGLDPDGANIRTYVVCNVAMPNQDNWLRTPFIERRGAQRIYV
ELKFTVRDCESFPGNARSCKETFNLYYYESDHDTATKEFPPWNEDPYTKIDTIAADESFKSSNEDTTEKL
NTETRSIGPLTKRGFYLAFQDQGACMSLLSVKVYYKK
>gnl|CDD|199907 cd10320, RGL4_N, N-terminal catalytic domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold; the middle and C-terminal domains are both putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11
FGLTDSGSAVVVDNGLLGLVFSVDGGIVTGILYGGLLENDNGKGDRGYLDLVSIVYGGTEQTPGKLSHIE
SGLGATVSATQSGDYIQISFSRTFETELHYVVRKGEPGIYMYTVATHPAPEPSLGELRTVFRLNPDLFPN
GAISDDRGDPPPGTALEGKEVQDDTFPLPDGEYDSKYYYSGYNRDNKVHGVYGDGVGAWMIMPSREYSSG
GPLKQDLTVHGGPILLNYFNSGHYGGKDLNATEGWRKLFGPYLLYFNSGGAPSTL
>gnl|CDD|199216 cd10321, RNase_Ire1_like, RNase domain (also known as the kinase extension nuclease domain) of Ire1 and RNase L. This RNase domain is found in the multi-functional protein Ire1; Ire1 also contains a type I transmembrane serine/threonine protein kinase (STK) domain, and a Luminal dimerization domain. Ire1 is essential for the endoplasmic reticulum (ER) unfolded protein response (UPR). The UPR is activated when protein misfolding is detected in the ER in order to reduce the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1 acts as an ER stress sensor; IRE1 dimerizes through its N-terminal luminal domain and forms oligomers, promoting trans-autophosphorylation by its cytosolic kinase domain which stimulates its endoribonuclease (RNase) activity and results in the cleavage of its mRNA substrate, Hac1 in yeast and Xbp1 in metazoans, thus promoting a splicing event that enables translation into a transcription factor which activates the UPR. This RNase domain is also found in Ribonuclease L (RNase L), sometimes referred to as the 2-5A-dependent RNase. RNase L is a highly regulated, latent endoribonuclease widely expressed in most mammalian tissues. It is involved in the mediation of the antiviral and pro-apoptotic activities of the interferon-inducible 2-5A system; the interferon (IFN)-inducible 2'-5'-oligoadenylate synthetase (OAS)/RNase L pathway blocks infections by certain types of viruses through cleavage of viral and cellular single-stranded RNA. RNase L has been shown to have an impact on the pathogenesis of prostate cancer; the RNase L gene, RNASEL, has been identified as a strong candidate for the hereditary prostate cancer 1 (HPC1) allele
EKKIQFIDAVLNLLKDSNLPPSTLNKLLNPGSDTVSSSFLSKPWNTLIDKNLMDDLSNFVRRTYNYDQVK
DLIRCIRNTIQHHKEIKNQLPEKNKEILESLKSQDSFFNYFESRFPNLLIFLYYKFK
>gnl|CDD|271357 cd10322, SLC5sbd, Solute carrier 5 family, sodium/glucose transporters and related proteins; solute-binding domain. This family represents the solute-binding domain of SLC5 proteins (also called the sodium/glucose cotransporter family or solute sodium symporter family) that co-transport Na+ with sugars, amino acids, inorganic ions or vitamins. Family members include: the human glucose (SGLT1, 2, 4, 5), chiro-inositol (SGLT5), myo-inositol (SMIT), choline (CHT), iodide (NIS), multivitamin (SMVT), and monocarboxylate (SMCT) cotransporters, as well as Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. Vibrio parahaemolyticus Na(+)/galactose cotransporter (vSGLT) has 13 transmembrane helices (TMs): TM-1, an inverted topology repeat: TMs1-5 and TMs6-10, and TMs 11-12 (TMs numbered to conform to the solute carrier 6 family Aquifex aeolicus LeuT). One member of this family, human SGLT3, has been characterized as a glucose sensor and not a transporter. Members of this family are important in human physiology and disease
IDLIIVVVYLALLLGIGLYASKKVKSSEDFFLAGRSLGPWLLAGTLAATWISAGSFVGVAGLAYTYGLSA
IWYILGAALGALLLALFLAPRLRRLGKTTIPETILERYYSKGLRLLVAIIIIIALIPYLALQLIGGGYIL
STLLGIPYTVAVIIAAVIVILYTVFGGMRAVAWTDVIQGIVMLIGVLVAAIFILSKVGGGGFSALAAALP
ALLLALGPGGGLGWSTILSLILLTGLGVLALPQVFQRILAAKDEKTARRAFLLAGLLLLLIGFLVALIGL
AARALFPDLENPDLALPTLINSLLPPGLAGLVLAGLLAAAMSTADSLLLAASTLFTRDIYKPLINPKASD
KKLLRVSRIAVVVVGVLALLLALLPPSILLLLSLAAGLLAAALFPPLLGGLFWKRATKAGAIAGIIVGLI
VTLVWLLLPLASPLGIDPIIPALLVSLIVFVVVS
>gnl|CDD|271358 cd10323, SLC-NCS1sbd, nucleobase-cation-symport-1 (NCS1) transporters; solute-binding domain. NCS1s are essential components of salvage pathways for nucleobases and related metabolites; their known substrates include allantoin, uracil, thiamine, and nicotinamide riboside. This family includes Microbacterium liquefaciens Mhp1, a transporter that mediates the uptake of indolyl methyl- and benzyl-hydantoins as part of a metabolic salvage pathway for their conversion to amino acids. It also includes various Saccharomyces cerevisiae transporters: Fcy21p (Purine-cytosine permease), vitamin B6 transporter Tpn1, nicotinamide riboside transporter 1 (Nrt1p, also called Thi71p), Dal4p (allantoin permease), Fui1p (uridine permease), and Fur4p (uracil permease). Mhp1 has 12 transmembrane (TM) helices (an inverted topology repeat: TMs1-5 and TMs6-10, and TMs11-12; TMs numbered to conform to the solute carrier 6 family Aquifex aeolicus LeuT). NCS1s belong to a superfamily which also contains the solute carrier 5 family sodium/glucose transporters (SLC5s), and SLC6 neurotransmitter transporters
TMGPLSYLAMWLGDCVSIGTFTLGGSLVGLGLLWQVILAILIGCLIIGIFLVLNGRIGYKYGIPFAVQLR
ASFGIKGSHIPSLLRGVPAIVWFGFQTWLGALALNEISGLLFGFDNIVLCFIIFGLLQIVLSFFGIKAIK
WLENIAAPAIIAALVYMFYLLVNKAGDEIGENLWYKAGTWGLPFLVAIMAFVGNWAALALNAPDYSRELK
PGKRNRNVGLAQFVALVPAFLFMGLIGAMSTAATGIWNPVDVIQGVVSNGFLLVLTLVFIVLAQWSTNIA
ANIVPPAYVFMNLFPRKITYKTGVVIAGILGLCICPWLLVNDLSALTTFLGIYSAFLGPIFGIMIADYYV
LRRRRVNVDDLYDANGQYKYFKGVNWAAIIAMAVGAAAALLLVDLSWFVGLIVAGLLYYPLMKR
>gnl|CDD|271359 cd10324, SLC6sbd, Solute carrier 6 family, neurotransmitter transporters; solute-binding domain. This family represents the solute-binding domain of SLC6 proteins (also called the sodium- and chloride-dependent neurotransmitter transporter family or Na+/Cl--dependent transporter family). These use sodium and chloride electrochemical gradients to catalyze the thermodynamically uphill movement of a variety of substrates, and include neurotransmitter transporters (NTTs). The latter are Na+/Cl--dependent plasma membrane transporters for the monoamine neurotransmitters serotonin (5-hydroxytryptamine), dopamine, and norepinephrine, and the amino acid neurotransmitters GABA and glycine. NTTs are widely expressed in the mammalian brain, and are involved in regulating neurotransmitter signaling and homeostasis, through facilitating the uptake of released neurotransmitters from the extracellular space into neurons and glial cells. NTTs are the target of a range of therapeutic drugs for the treatment of psychiatric diseases, such as major depression, anxiety disorders, attention deficit hyperactivity disorder and epilepsy. In addition, they are the primary targets of cocaine, amphetamines and other psychostimulants. This family also includes Drosophila Blot which is expressed primarily in epithelial tissues of ectodermal origin and in the nervous system of the embryo and larvae, but in addition found in the developing oocyte and the freshly laid egg. A lack or reduction of Blot function during oogenesis results in early arrest of embryonic development. 12 transmembrane helices (TMs) appears to be common for eukaryotic and some prokaryotic and archaeal SLC6s, (a core inverted topology repeat, TM1-5 and TM6-10, plus TMs11-12; TMs numbered to conform to the SLC6 Aquifex aeolicus LeuT), although a majority of bacterial, and some archaeal SLC6s lack TM12, for example the functional Fusobacterium nucleatum tyrosine transporter Tyt1
EQWGSKLEFLLSCIGYAVGLGNIWRFPYLAYENGGGAFLIPYLIMLFLVGIPLFYLELALGQYTSRGPVG
AFWRIAPLFKGVGYAQVLVSFLVAIYYNVIIAWTLYYLFASFINWELFLCLLLAWILVYLCKGVKSIGKG
VKFTGPFPYVLLLFLLIRGVTLPGAGDGILFYLTPDWSKLLDPKVWIAAATQIFFSLGIGFGGLITYASY
NKFKNNIYRDALIVAILNTLTSLLAGFVIFSILGFLAHEPGTPVEDVVASGPGLAFIVYPEAIAQMPGPQ
LWSVLFFLMLFLLGLDSQFAMVEVIVTALADEFPKLRKRRWLVTLGVCVVGFLLGLPYTTPGGIYVLDLF
DYYAAGFSLLVIALLELIAIAWIYGVDRFLEDIEFMLGIRPSIYWRICWKFITPVVLLIILVFSL
>gnl|CDD|271360 cd10325, SLC5sbd_vSGLT, Vibrio parahaemolyticus Na(+)/galactose cotransporter (vSGLT) and related proteins; solute binding domain. vSGLT transports D-galactose, D-glucose, and alpha-D-fucose, with a sugar specificity in the order of D-galactose _D-fucose _D-glucose. It transports one Na+ ion for each sugar molecule, and appears to function as a monomer. vSGLT has 13 transmembrane helices (TMs): TM-1, an inverted topology repeat: TMs1-5 and TMs6-10, and TMs 11-12 (TMs numbered to conform to the solute carrier 6 family Aquifex aeolicus LeuT). This subfamily belongs to the solute carrier 5 (SLC5) transporter family
VIFIVYVILIIGLGLWVSREKKGGEKDATDYFLAGKSLPWWAIGASLIAANISAEQFIGMSGSGFAIGLA
IASYEWMAAITLIIVAKFFLPIFLKNGIYTMPQFLEERYDGRVRTIMAVFWLLLYVFVNLTSVLYLGALA
IETITGIPLTYSIIGLALFAAAYSIYGGLKAVAWTDVIQVVFLVLGGLVTTYIALSLLGGGEGVFAGFTL
LAAEAPEHFHMILDKSNPEDAYKDLPGIAVLLGGLWVANLSYWGFNQYIIQRALAAKSLSEAQKGIVFAA
FLKLLIPFIVVIPGIAAYVLASNLLLPAATGIEKPDQAYPWLLRNLPTGLKGLVFAALTAAIVSSLASML
NSISTIFTMDIYKKYIPKKASEKQLVNVGRLAAVIALIIAALIAPPLLGLDQAFQYIQEYTGFISPGILA
IFLLGLFWKRATSAGALVAAILSIVLSALFKFLLPELPFLDRMGYVFFICVVLIVLVSLLTPKGKDDPKA
IEIDPDMFKTSPSFNLGAVGVLAILAALYVVFW
>gnl|CDD|271361 cd10326, SLC5sbd_NIS-like, Na(+)/iodide (NIS) and Na(+)/multivitamin (SMVT) cotransporters, and related proteins; solute binding domain. NIS (product of the SLC5A5 gene) transports I-, and other anions including ClO4-, SCN-, and Br-. SMVT (product of the SLC5A6 gene) transports biotin, pantothenic acid and lipoate. This subfamily also includes SMCT1 and 2. SMCT1(the product of the SLC5A8 gene) is a high-affinity transporter of various monocarboxylates including lactate and pyruvate, short-chain fatty acids, ketone bodies, nicotinate and its structural analogs, pyroglutamate, benzoate and its derivatives, and iodide. SMCT2 (product of the SLC5A12 gene) is a low-affinity transporter for short-chain fatty acids, lactate, pyruvate, and nicotinate. This subfamily belongs to the solute carrier 5 (SLC5) transporter family
DWAVVVVYFLILLAISYYTSRRNADNDDFFLGNRQSPWYLVAFSMIGTSLSGVTFVSVPGEVGGSGFTYL
QMVLGFLLGYLIIAFVLLPLYYRLNLTSIYEYLEDRFGVSSRKTGAVFFLLSRILGAGIRLYLVALVLQQ
FLFDSLGIPFWLTVLITGLLIWLYTFRGGIKTVVWTDTLQTVFLLVGLVLTIIIISNSLGLGFGEAISAA
GESGYSRIFNFDDDNSRRTFWKQFLGGIFITIAMTGLDQDMMQRNLSCKNLKDAQKNMLTFGVILVPVNL
LFLLLGVLLYTYAQKNGIALPAKDSDQLFPYFALNGLPPGVSGLFVAGIIAAAMSSADSALTALTTSFCV
DILNRFKRKSEKKSERKYVHIAFSLTFVLGILVFGSASNSGSLIDAIFKVAGYTYGPLLGLFAFGLFTKR
AVKDKWVPLVGLLAPVLSYLLVSNSEGFFGYKFGFELLIINGLLTFLGLLLS
>gnl|CDD|212037 cd10327, SLC5sbd_PanF, Na(+)/pantothenate cotransporters: PanF of Escherichia coli and related proteins; solute binding domain. PanF catalyzes the Na+-coupled uptake of extracellular pantothenate for coenzyme A biosynthesis in cells. This subfamily belongs to the solute carrier 5 (SLC5) transporter family
VLLPIIIYLVILLGIGFYARRSKKRRSGDFLEEYFIGGRSMGGFVLAMTLVATYTSASSFIGGPGAAYKI
GLGWVLLAMIQVPTGFLTLGVLGKKFAIIARKINAVTIIDYLRARYNSKALVVLSSLALIVFFIAAMVAQ
FIGGARLLEAVTGLSYVTGLLIFGLTVILYTTIGGFRAVALTDAIQGIVMIIGTVLLLVGVLAAGGGMEA
IMATLAEIDPNLLTPFGPGFLSPPYILSFWVLVGFGVIGLPQTAVRCMGYKDSKSMHRAMIIGTVVVGFL
MLGMHLAGVLGRAVLPDLEVPDKVIPTLALKVLPPWLAGLFLAGPLAAIMSTVDSQLILASSAIVKDLYL
NYKNKEKKTSEKKVKRISLIITIILGLLVFLLAINPPDLIVWLNLFAFGGLEAAFFWPLVLGLYWKRANA
TGALASMVVGLVSYILITYLKIKILGLHPIVPSLLLSLIAFIIVSLATKKPD
>gnl|CDD|271362 cd10328, SLC5sbd_YidK, uncharacterized SLC5 subfamily, Escherichia coli YidK-like; solute binding domain. Uncharacterized subfamily of the solute binding domain of the solute carrier 5 (SLC5) transporter family (also called the sodium/glucose cotransporter family or solute sodium symporter family) that co-transports Na+ with sugars, amino acids, inorganic ions or vitamins. One member of the SLC5 family, human SGLT3, has been characterized as a glucose sensor and not a transporter. This subfamily includes the uncharacterized Escherichia coli YidK protein, and belongs to the solute carrier 5 (SLC5) transporter family
FLLFTALVALISWYKTRGDDLSSSDGYFLAGRSLTGVVIAGSLLLTNLSTEQLVGLNGQAYALGMSVMAW
EVTAAIALIILALVFLPRYLKGGITTIPEFLEERYDETTRRIVSILFLLGYVVILLPIVLYSGALALNSL
FDVSELLGISYFQALWLLVWLIGIIGAIYAIFGGLKAVAVSDTINGVGLLIGGLLIPILGLIALGDGSFL
AGLDTLLTAHPEKLNAIGGADSPVPFSTLFTGMLLVNLFYWCTNQAIIQRALAAKNLKEGQKGVLLAGFF
KLLVPLILVLPGIIAFHLYGDGLENADMAYPTLVADVLPKWLSGFFAAVLFGAILSSFNSALNSAATLFS
LDIYKPIINKNATDKQLVKVGKIFGIVLALISMIIAPFIAYAPEGLFNYLQQFNGFFSIPILAIVLVGFF
TKRVPALAAKIALIFGVILYALLQFVFLVPIHFLHVLAILFVICVAIMLIIG
>gnl|CDD|271363 cd10329, SLC5sbd_SGLT1-like, Na(+)/glucose cotransporter SGLT1 and related proteins; solute binding domain. This subfamily includes the solute-binding domain of SGLT proteins that cotransport Na+ with various solutes. Its members include: the human glucose (SGLT1, -2, -4, -5), chiro-inositol (SGLT5), and myo-inositol (SMIT) cotransporters. It also includes human SGLT3 which has been characterized as a glucose sensor and not a transporter. It belongs to the solute carrier 5 (SLC5) transporter family
IVIIAVYFVAVIAIGLWSSRKKRSTVSGYFLAGRSMGWPVIGASLFASNIGSSHLVGLAGSGAASGIAVG
NYEWNAAFVLLLLGWVFLPFYIRSGVSTMPEFLEKRFGGRSRVYLSVLSLILYVFTKISVDLYAGALVIK
QLLGWDLYLSIIVLLVITAIYTIAGGLKAVIYTDTLQAVILIIGSAILMFLAFNEVGGGWSAYMAAIPSG
TAFHLFRPPDDPDLPWPGLLLGYPILGIWYWCTDQVIVQRVLAAKNLKHARRGALFAGYLKLLPLFLMVL
PGMIARALFPDLVACVVPCGNGVGCSDIAYPTLVTELLPVGLRGLVLAVLLAALMSSLTSIFNSASTLFT
MDIYKRLRPEASEKELVRVGRIATLVVVVISILWAPIIQAQGGSLFNYIQSVLSYLAPPIAAVFLLGIFW
KRTNEQGAFWGLIAGLVLGLVRLILEFAYGEPDTRPAIIGGIHFLYFAFLLFVVSVIVTVIVSLLTPPPP
AEKLAGLTWSTRLTKETSTLERPPWYKNVRILAILLLALTIFLYGYFA
>gnl|CDD|271364 cd10332, SLC6sbd-B0AT-like, System B(0) neutral amino acid transporter AT1, 2 and 3, and related proteins; solute-binding domain. This subgroup includes the solute-binding domain of transmembrane transporters, which transport, i) neutral amino acids: NTT4 (also called XT1), SBAT1 (also called B0AT2, v7-3, NTT7-3), and B0AT1 (also called HND); the human genes encoding these are SLC6A17, SLC6A15, and SLC6A19 respectively, ii) glycine: B0AT3 (also called Xtrp2, XT2), iii) imino acids, such as proline, pipecolate, MeAIB, and sarcosine: SIT1 (also called XTRP3, XT3, IMINO). The human genes encoding B0AT3 and SIT1 are SLC6A18 and SLC6A20 respectively. Transporters in this subgroup may play a role in disorders including major depression, Hartnup disorder, increased susceptibility to myocardial infarction, and iminoglycinuria. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RPAWDNKLQFLLATIGYAVGLGNVWRFPYLCQKNGGGAFLIPYFIMLILEGIPLFFLELAIGQRLRKGSI
GVWNTISPYLGGVGIASVVVSFLVALYYNVIIAWCFFYLFNSFQYPLPWSSCPTNGNGTGYVEECAKSSP
TQYFWYRTTLDISPSIDESGGLNWWMTLCLLLAWIIVYLCMMKGIKSSGKVVYFTATFPYIVLIIFFIRG
LTLKGAGDGLKHMFTPKFEKLLDPQVWLDAATQIFFSLGLGFGSLIAFSSYNPPKNNCQRDAVLVSLINC
FTSIFASIVVFSVLGFKINNVTLTENQTLGLTNCSLEDELDEAVQGTGLAFIVFTEAITKMPGAPFWSVL
FFLMLLTLGLGSMFGTLEGVVTPLFDSKILPKVPKEYLTGLVCLVCFLIGLIFTQRSGNYWVQMFDSYAG
TLPLLIIALFEMIAVSYVYGLDRFEEDIEYMTGKRPGWYWKITWRYVSPLLMLVILVASIIQLITKPPTY
SAWNAELAKTESLPYPNWGLAVIILLILLSILPIPGVALLR
>gnl|CDD|271365 cd10333, LeuT-like_sbd, Aquifex aeolicus LeuT and related proteins; solute binding domain. LeuT is a bacterial amino acid transporter with specificity for the hydrophobic amino acids glycine, alanine, methionine, and leucine. This subgroup belongs to the solute carrier 6 (SLC6) transporter family; LeuT has been used as a structural template for understanding fundamental aspects of SLC6 function. It has an arrangement of 12 transmembrane helices (TMs), which appears to be a common motif for eukaryotic and some prokaryotic and archaeal SLC6s: an inverted topology repeat: TMs1-5 and TMs6-10, and TMs11-12
REHWGSRIGLILAMAGNAVGLGNFLRFPVQAAQNGGGAFMIPYFIAFLLLGIPLMWIEWAMGRYGGKYGH
GTTPMIFLLAWENRFAKILGAIGLAIPLLVNSYYVYIESWTLGYAFKSLTGAYPEPPSILRPTAEFFYSY
IGKPSGLAYIFFLITMALNFFILYRGVSKGIEAFAKIAMPLLYVFAIILLIRVLTLGSPVNPNWTALKGL
NFLWNPDFSKLKNPKVWLAAAGQIFFTLSLGMGIIQNYASYLKKDDDVVLSGLTAASLNEFAEVILGGSI
AIPAAFAFLGVAVAIAKAGGFGLGFIALPNVFSQMPGGQFFGFLWFLLLFFAGITSSIAMYQPLIAFLEE
ELGISRKHAAWVVFAIVFFLGLPVVLEFDLKALDELDFWVGTILLVILGLIEIIVFGWIFGAKKGWEEIN
RGALIKVPRFYKYVMKYITPAFLAVVLVFWTISYIPKGYFKMNLIPTVWIARFVIIGLFLFLAFLVYLAI
KRKYHE
>gnl|CDD|271366 cd10334, SLC6sbd_u1, uncharacterized bacterial and archaeal solute carrier 6 subfamily; solute-binding domain. SLC6 proteins (also called the sodium- and chloride-dependent neurotransmitter transporter family or Na+/Cl--dependent transporter family) include neurotransmitter transporters (NTTs): these are sodium- and chloride-dependent plasma membrane transporters for the monoamine neurotransmitters serotonin (5-hydroxytryptamine), dopamine, and norepinephrine, and the amino acid neurotransmitters GABA and glycine. These NTTs are widely expressed in the mammalian brain, involved in regulating neurotransmitter signaling and homeostasis, and the target of a range of therapeutic drugs for the treatment of psychiatric diseases. Bacterial members of the SLC6 family include the LeuT amino acid transporter
REQWGSRAGFILAAIGSAVGLGNIWRFPYVAYENGGGAFLIPYLIALLTAGIPLLILEYGLGHKYRGSAP
LAFRRLNKKFEWIGWWQVLVAFVIATYYAVIIAWALSYLFFSFTLAWGDDPEAFFFGDFLQLSDSPFDLG
GIVWPILIALVLVWLIIWFILYRGVKKGIEKASKIFMPLLFVLFLILVIRALTLPGAADGLNALFTPDWS
ALLDPKVWIAAYGQIFFSLSLGFGIMITYASYLPKKSDLTNNALITAFANSGFEILAGIGVFSILGFMAQ
AQGVPVSEVVSSGIGLAFVAFPKAINLMPPLGALFGVLFFLSLVFAGLTSLISLVEVVISAVQDKFGLSR
KKAVTIVCLVGFLVSLLFATGAGLYLLDIVDHFINNYGIVLVGLVEVIVVGWVFGAEKLREHLNAVSDFK
VGKWWDFLIKVVTPLVLGYMLILGLIGLLTEPYGGYPVWALLLFGWGIVALILVAALLLS
>gnl|CDD|271367 cd10336, SLC6sbd_Tyt1-Like, solute carrier 6 subfamily, Fusobacterium nucleatum Tyt1-like; solute-binding domain. SLC6 proteins (also called the sodium- and chloride-dependent neurotransmitter transporter family or Na+/Cl--dependent transporter family) include neurotransmitter transporters (NTTs): these are sodium- and chloride-dependent plasma membrane transporters for the monoamine neurotransmitters serotonin (5-hydroxytryptamine), dopamine, and norepinephrine, and the amino acid neurotransmitters GABA and glycine. These NTTs are widely expressed in the mammalian brain, involved in regulating neurotransmitter signaling and homeostasis, and the target of a range of therapeutic drugs for the treatment of psychiatric diseases. Bacterial members of the SLC6 family include the LeuT amino acid transporter. An arrangement of 12 transmembrane (TM) helices appears to be as a common topological motif for eukaryotic and some prokaryotic and archaeal NTTs. However, this subfamily which contains the majority of bacterial members and some archaeal members, appears to contain only 11 TMs; for example the functional Fusobacterium nucleatum tyrosine transporter Tyt1
EQWSSRLGFILAAAGSAVGLGNIWRFPYLAGENGGGAFLLVYLLFVLLIGLPLLIAEFAIGRRTRKNPVG
AFAKLAGGGKKWKLIGWLGVLGGFLILSFYSVVGGWVLKYLFKSLTGLFAGADAAEVGAAFFGFIASPLS
PLLWHLLFLLLTALIVARGVKKGIERANKILMPLLFILLIILAIRSLTLPGAGEGLKFLLKPDFSKLTPE
VVLAALGQAFFSLSLGMGVMITYGSYLSKDENLPKSALIVAVLDTLVALLAGLVIFPAVFAFGLDPAAGP
GLLFITLPAVFAQMPGGRLFGILFFLLLLFAALTSAISLLEVVVAYLIDEFGWSRKKATLIVGIIIFLLG
IPSALSFGVLSDVTIFGKTFFDLLDFLVSNILLPLGGLLIAIFVGWVLGKEALLEELNKGGLGKKLFKIW
LFLLRYVAPVAILIIFLLGL
>gnl|CDD|198200 cd10337, SH2_BCAR3, Src homology 2 (SH2) domain in the Breast Cancer Anti-estrogen Resistance protein 3. BCAR3 is part of a growing family of guanine nucleotide exchange factors is responsible for activation of Ras-family GTPases, including Sos1 and 2, GRF1 and 2, CalDAG-GEF/GRP1-4, C3G, cAMP-GEF/Epac 1 and 2, PDZ-GEFs, MR-GEF, RalGDS family members, RalGPS, RasGEF, Smg GDS, and phospholipase C(epsilon). 12102558 21262352 BCAR3 binds to the carboxy-terminus of BCAR1/p130Cas, a focal adhesion adapter protein. Over expression of BCAR1 (p130Cas) and BCAR3 induces estrogen independent growth in normally estrogen-dependent cell lines. They have been linked to resistance to anti-estrogens in breast cancer, Rac activation, and cell motility, though the BCAR3/p130Cas complex is not required for this activity in BCAR3. Many BCAR3-mediated signaling events in epithelial and mesenchymal cells are independent of p130Cas association. Structurally these proteins contain a single SH2 domain upstream of their RasGEF domain, which is responsible for the ability of BCAR3 to enhance p130Cas over-expression-induced migration. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
EDLRSHAWYHGRIPRQVAESLVQREGDFLVRDSLSSPGDYVLTCRWKGQPLHFKINRVVLRPSEAYTRVQ
YQFEDEQFDSIPALVHFYVGNRRPISQASGAIISRPVNRTVPLRCLEEKDGLEQGSTRMLRSQSVK
>gnl|CDD|198201 cd10338, SH2_SHA, Src homology 2 (SH2) domain found in SH2 adaptor proteins A (SHA) Signal transducers. Signal transducing adaptor proteins are accessory to main proteins in a signal transduction pathway. These proteins lack intrinsic enzymatic activity, but mediate specific protein-protein interactions that drive the formation of protein complexes. Adaptor proteins usually contain several domains within their structure (e.g. SH2 and SH3 domains) which allow specific interactions with several other specific proteins. Not much is known about the SHA protein except that it is predicted to act as a transcription factor. Arabidopsis SHA pulled down a 120-kD tyrosine-phosphorylated protein in vitro. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
INGMWRSASPKWIEGFITKEEAERSLQGQVPGTFILRFPTSRSWPHPDAGSLVVTYVGHDLVIHHRLLSI
DNICDSSERYTDAKPLQDMLLAEPELSRLGRIIRLI
>gnl|CDD|198202 cd10339, SH2_RIN_family, Src homology 2 (SH2) domain found in Ras and Rab interactor (RIN)-family. The RIN (AKA Ras interaction/interference) family is composed of RIN1, RIN2 and RIN3. These proteins have multifunctional domains including SH2 and proline-rich (PR) domains in the N-terminal region, and RIN-family homology (RH), VPS9 and Ras-association (RA) domains in the C-terminal region. RIN proteins function as Rab5-GEFs, and RIN3 specifically functions as a Rab31-GEF. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
LLERLLLTRPVWLQLQLNAAEAAHMLQTEPPGTFLVRKSNTRQCQVLCMRLPEASGPAFVSEHYIKESPG
GVSLEGSELMFPDLFRLIAFYCHSRDILPFT
>gnl|CDD|198203 cd10340, SH2_N-SH2_SHP_like, N-terminal Src homology 2 (N-SH2) domain found in SH2 domain Phosphatases (SHP) proteins. The SH2 domain phosphatases (SHP-1, SHP-2/Syp, Drosophila corkscrew (csw), and Caenorhabditis elegans Protein Tyrosine Phosphatase (Ptp-2)) are cytoplasmic signaling enzymes. They are both targeted and regulated by interactions of their SH2 domains with phosphotyrosine docking sites. These proteins contain two SH2 domains (N-SH2, C-SH2) followed by a tyrosine phosphatase (PTP) domain, and a C-terminal extension. Shp1 and Shp2 have two tyrosyl phosphorylation sites in their C-tails, which are phosphorylated differentially by receptor and nonreceptor PTKs. Csw retains the proximal tyrosine and Ptp-2 lacks both sites. Shp-binding proteins include receptors, scaffolding adapters, and inhibitory receptors. Some of these bind both Shp1 and Shp2 while others bind only one. Most proteins that bind a Shp SH2 domain contain one or more immuno-receptor tyrosine-based inhibitory motifs (ITIMs): [IVL]xpYxx[IVL]. Shp1 N-SH2 domain blocks the catalytic domain and keeps the enzyme in the inactive conformation, and is thus believed to regulate the phosphatase activity of SHP-1. Its C-SH2 domain is thought to be involved in searching for phosphotyrosine activators. The SHP2 N-SH2 domain is a conformational switch; it either binds and inhibits the phosphatase, or it binds phosphoproteins and activates the enzyme. The C-SH2 domain contributes binding energy and specificity, but it does not have a direct role in activation. Csw SH2 domain function is essential, but either SH2 domain can fulfill this requirement. The role of the csw SH2 domains during Sevenless receptor tyrosine kinase (SEV) signaling is to bind Daughter of Sevenless rather than activated SEV. Ptp-2 acts in oocytes downstream of sheath/oocyte gap junctions to promote major sperm protein (MSP)-induced MAP Kinase (MPK-1) phosphorylation. Ptp-2 functions in the oocyte cytoplasm, not at the cell surface to inhibit multiple RasGAPs, resulting in sustained Ras activation. It is thought that MSP triggers PTP-2/Ras activation and ROS production to stimulate MPK-1 activity essential for oocyte maturation and that secreted MSP domains and Cu/Zn superoxide dismutases function antagonistically to control ROS and MAPK signaling. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
RWFHPVISGIEAENLLKTRGVDGSFLARPSKSNPGDFTLSVRRGDEVTHIKIQNTGDYYDLYGGEKFATL
SELVQYYMEQHGQLREKNGDVIELKYPLN
>gnl|CDD|199829 cd10341, SH2_N-SH2_PLC_gamma_like, N-terminal Src homology 2 (N-SH2) domain in Phospholipase C gamma. Phospholipase C gamma is a signaling molecule that is recruited to the C-terminal tail of the receptor upon autophosphorylation of a highly conserved tyrosine. PLCgamma is composed of a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, 2 catalytic regions of PLC domains that flank 2 tandem SH2 domains (N-SH2, C-SH2), and ending with a SH3 domain and C2 domain. N-SH2 SH2 domain-mediated interactions represent a crucial step in transmembrane signaling by receptor tyrosine kinases. SH2 domains recognize phosphotyrosine (pY) in the context of particular sequence motifs in receptor phosphorylation sites. Both N-SH2 and C-SH2 have a very similar binding affinity to pY. But in growth factor stimulated cells these domains bind to different target proteins. N-SH2 binds to pY containing sites in the C-terminal tails of tyrosine kinases and other receptors. Recently it has been shown that this interaction is mediated by phosphorylation-independent interactions between a secondary binding site found exclusively on the N-SH2 domain and a region of the FGFR1 tyrosine kinase domain. This secondary site on the SH2 cooperates with the canonical pY site to regulate selectivity in mediating a specific cellular process. C-SH2 binds to an intramolecular site on PLCgamma itself which allows it to hydrolyze phosphatidylinositol-4,5-bisphosphate into diacylglycerol and inositol triphosphate. These then activate protein kinase C and release calcium. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
HFTEPWFHGKLGDGRDEAEKLLLEYCEGGDGTFLVRESETFVGDYTLSFWRNGKVQHCRIRSRQENGEKK
YYLTDNLVFDSLYELIDYYRQNPLRCAEF
>gnl|CDD|198205 cd10342, SH2_SAP1, Src homology 2 (SH2) domain found in SLAM-associated protein (SAP)1. The X-linked lymphoproliferative syndrome (XLP) gene encodes SAP (also called SH2D1A/DSHP) a protein that consists of a 5 residue N-terminus, a single SH2 domain, and a short 25 residue C-terminal tail. XLP is characterized by an extreme sensitivity to Epstein-Barr virus. Both T and natural killer (NK) cell dysfunctions have been seen in XLP patients. SAP binds the cytoplasmic tail of Signaling lymphocytic activation molecule (SLAM), 2B4, Ly-9, and CD84. SAP is believed to function as a signaling inhibitor, by blocking or regulating binding of other signaling proteins. SAP and the SAP-like protein EAT-2 recognize the sequence motif TIpYXX[VI], which is found in the cytoplasmic domains of a restricted number of T, B, and NK cell surface receptors and are proposed to be natural inhibitors or regulators of the physiological role of a small family of receptors on the surface of these cells. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
DAVAVYHGKISRETGEKLLLATGLDGSYLLRDSESVPGVYCLCVLYHGYIYTYRVSQTETGSWSAETAPG
VHKRYFRKIKNLISAFQKPDQGIVIPLQYPVEK
>gnl|CDD|198206 cd10343, SH2_SHIP, Src homology 2 (SH2) domain found in SH2-containing inositol-5'-phosphatase (SHIP) and SLAM-associated protein (SAP). The SH2-containing inositol-5'-phosphatase, SHIP (also called SHIP1/SHIP1a), is a hematopoietic-restricted phosphatidylinositide phosphatase that translocates to the plasma membrane after extracellular stimulation and hydrolyzes the phosphatidylinositol-3-kinase (PI3K)-generated second messenger PI-3,4,5-P3 (PIP3) to PI-3,4-P2. As a result, SHIP dampens down PIP3 mediated signaling and represses the proliferation, differentiation, survival, activation, and migration of hematopoietic cells. PIP3 recruits lipid-binding pleckstrin homology(PH) domain-containing proteins to the inner wall of the plasma membrane and activates them. PH domain-containing downstream effectors include the survival/proliferation enhancing serine/threonine kinase, Akt (protein kinase B), the tyrosine kinase, Btk, the regulator of protein translation, S6K, and the Rac and cdc42 guanine nucleotide exchange factor, Vav. SHIP is believed to act as a tumor suppressor during leukemogenesis and lymphomagenesis, and may play a role in activating the immune system to combat cancer. SHIP contains an N-terminal SH2 domain, a centrally located phosphatase domain that specifically hydrolyzes the 5'-phosphate from PIP3, PI-4,5-P2 and inositol-1,3,4,5- tetrakisphosphate (IP4), a C2 domain, that is an allosteric activating site when bound by SHIP's enzymatic product, PI-3,4-P2; 2 NPXY motifs that bind proteins with a phosphotyrosine binding (Shc, Dok 1, Dok 2) or an SH2 (p85a, SHIP2) domain; and a proline-rich domain consisting of four PxxP motifs that bind a subset of SH3-containing proteins including Grb2, Src, Lyn, Hck, Abl, PLCg1, and PIAS1. The SH2 domain of SHIP binds to the tyrosine phosphorylated forms of Shc, SHP-2, Doks, Gabs, CD150, platelet-endothelial cell adhesion molecule, Cas, c-Cbl, immunoreceptor tyrosine-based inhibitory motifs (ITIMs), and immunoreceptor tyrosine-based activation motifs (ITAMs). The X-linked lymphoproliferative syndrome (XLP) gene encodes SAP (also called SH2D1A/DSHP) a protein that consists of a 5 residue N-terminus, a single SH2 domain, and a short 25 residue C-terminal tail. XLP is characterized by an extreme sensitivity to Epstein-Barr virus. Both T and natural killer (NK) cell dysfunctions have been seen in XLP patients. SAP binds the cytoplasmic tail of Signaling lymphocytic activation molecule (SLAM), 2B4, Ly-9, and CD84. SAP is believed to function as a signaling inhibitor, by blocking or regulating binding of other signaling proteins. SAP and the SAP-like protein EAT-2 recognize the sequence motif TIpYXX(V/I), which is found in the cytoplasmic domains of a restricted number of T, B, and NK cell surface receptors and are proposed to be natural inhibitors or regulators of the physiological role of a small family of receptors on the surface of these cells. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
MAPPWYHGNITRSKAEELLSKAGKDGSFLVRDSESVSGAYALCVLYQNCVHTYRILPNAEDKLSVQASEG
VPVRFFTTLPELIEFYQKENMGLVTHLLYPVER
>gnl|CDD|198207 cd10344, SH2_SLAP, Src homology 2 domain found in Src-like adaptor proteins. SLAP belongs to the subfamily of adapter proteins that negatively regulate cellular signaling initiated by tyrosine kinases. It has a myristylated N-terminus, SH3 and SH2 domains with high homology to Src family tyrosine kinases, and a unique C-terminal tail, which is important for c-Cbl binding. SLAP negatively regulates platelet-derived growth factor (PDGF)-induced mitogenesis in fibroblasts and regulates F-actin assembly for dorsal ruffles formation. c-Cbl mediated SLAP inhibition towards actin remodeling. Moreover, SLAP enhanced PDGF-induced c-Cbl phosphorylation by SFK. In contrast, SLAP mitogenic inhibition was not mediated by c-Cbl, but it rather involved a competitive mechanism with SFK for PDGF-receptor (PDGFR) association and mitogenic signaling. Accordingly, phosphorylation of the Src mitogenic substrates Stat3 and Shc were reduced by SLAP. Thus, we concluded that SLAP regulates PDGFR signaling by two independent mechanisms: a competitive mechanism for PDGF-induced Src mitogenic signaling and a non-competitive mechanism for dorsal ruffles formation mediated by c-Cbl. SLAP is a hematopoietic adaptor containing Src homology (SH)3 and SH2 motifs and a unique carboxy terminus. Unlike c-Src, SLAP lacks a tyrosine kinase domain. Unlike c-Src, SLAP does not impact resorptive function of mature osteoclasts but induces their early apoptosis. SLAP negatively regulates differentiation of osteoclasts and proliferation of their precursors. Conversely, SLAP decreases osteoclast death by inhibiting activation of caspase 3. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
PSNYVAKVYHGWLFEGLSREKAEELLMLPGNQVGSFLIRESETRRGCYSLSVRHRGSQSRDSVKHYRIFR
LDNGWFYISPRLTFQCLEDMVNHYSESADGLCCV
>gnl|CDD|198208 cd10345, SH2_C-SH2_Zap70_Syk_like, C-terminal Src homology 2 (SH2) domain found in Zeta-chain-associated protein kinase 70 (ZAP-70) and Spleen tyrosine kinase (Syk) proteins. ZAP-70 and Syk comprise a family of hematopoietic cell specific protein tyrosine kinases (PTKs) that are required for antigen and antibody receptor function. ZAP-70 is expressed in T and natural killer (NK) cells and Syk is expressed in B cells, mast cells, polymorphonuclear leukocytes, platelets, macrophages, and immature T cells. They are required for the proper development of T and B cells, immune receptors, and activating NK cells. They consist of two N-terminal Src homology 2 (SH2) domains and a C-terminal kinase domain separated from the SH2 domains by a linker or hinge region. Phosphorylation of both tyrosine residues within the Immunoreceptor Tyrosine-based Activation Motifs (ITAM; consensus sequence Yxx[LI]x(7,8)Yxx[LI]) by the Src-family PTKs is required for efficient interaction of ZAP-70 and Syk with the receptor subunits and for receptor function. ZAP-70 forms two phosphotyrosine binding pockets, one of which is shared by both SH2 domains. In Syk the two SH2 domains do not form such a phosphotyrosine-binding site. The SH2 domains here are believed to function independently. In addition, the two SH2 domains of Syk display flexibility in their relative orientation, allowing Syk to accommodate a greater variety of spacing sequences between the ITAM phosphotyrosines and singly phosphorylated non-classical ITAM ligands. This model contains the C-terminus SH2 domains of both Syk and Zap70. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
PWFHGKISREESEQIVLIGSKTNGKFLIRARDNNGSYALCLLHEGKVLHYRIDKDKTGKLSIPEGKKFDT
LWQLVEHYSYKADGLLRVLTVPCQK
>gnl|CDD|198209 cd10346, SH2_SH2B_family, Src homology 2 (SH2) domain found in SH2B adapter protein family. The SH2B adapter protein family has 3 members: SH2B1 (SH2-B, PSM), SH2B2 (APS), and SH2B3 (Lnk). SH2B family members contain a pleckstrin homology domain, at least one dimerization domain, and a C-terminal SH2 domain which binds to phosphorylated tyrosines in a variety of tyrosine kinases. SH2B1 and SH2B2 function in signaling pathways found downstream of growth hormone receptor and receptor tyrosine kinases, including the insulin, insulin-like growth factor-I (IGF-I), platelet-derived growth factor (PDGF), nerve growth factor, hepatocyte growth factor, and fibroblast growth factor receptors. SH2B2beta, a new isoform of SH2B2, is an endogenous inhibitor of SH2B1 and/or SH2B2 (SH2B2alpha), negatively regulating insulin signaling and/or JAK2-mediated cellular responses. SH2B3 negatively regulates lymphopoiesis and early hematopoiesis. The lnk-deficiency results in enhanced production of B cells, and expansion as well as enhanced function of hematopoietic stem cells (HSCs), demonstrating negative regulatory functions of Sh2b3/Lnk in cytokine signaling. Sh2b3/Lnk also functions in responses controlled by cell adhesion and in crosstalk between integrin- and cytokine-mediated signaling. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
LTAELSEYPWFHGTLSRSDAAQLVLHSGADGHGVFLVRQSETRRGEFVLTFNFQGRAKHLRLTLNEKGQC
RVQHLWFPSIFDMLEHFRQNPIPLESG
>gnl|CDD|198210 cd10347, SH2_Nterm_shark_like, N-terminal Src homology 2 (SH2) domain found in SH2 domains, ANK, and kinase domain (shark) proteins. These non-receptor protein-tyrosine kinases contain two SH2 domains, five ankyrin (ANK)-like repeats, and a potential tyrosine phosphorylation site in the carboxyl-terminal tail which resembles the phosphorylation site in members of the src family. Like, mammalian non-receptor protein-tyrosine kinases, ZAP-70 and syk proteins, they do not have SH3 domains. However, the presence of ANK makes these unique among protein-tyrosine kinases. Both tyrosine kinases and ANK repeats have been shown to transduce developmental signals, and SH2 domains are known to participate intimately in tyrosine kinase signaling. These tyrosine kinases are believed to be involved in epithelial cell polarity. The members of this family include the shark (SH2 domains, ANK, and kinase domain) gene in Drosophila and yellow fever mosquitos, as well as the hydra protein HTK16. Drosophila Shark is proposed to transduce intracellularly the Crumbs, a protein necessary for proper organization of ectodermal epithelia, intercellular signal. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
LRWYHGKISREVAEALLLREGGRDGLFLVRESTSAPGDYVLSLLAQGEVLHYQIRRHGEDAFFSDDGPLI
FHGLDTLIEHY
>gnl|CDD|198211 cd10348, SH2_Cterm_shark_like, C-terminal Src homology 2 (SH2) domain found in SH2 domains, ANK, and kinase domain (shark) proteins. These non-receptor protein-tyrosine kinases contain two SH2 domains, five ankyrin (ANK)-like repeats, and a potential tyrosine phosphorylation site in its carboxyl-terminal tail which resembles the phosphorylation site in members of the src family. Like, mammalian non-receptor protein-tyrosine kinases, ZAP-70 and syk proteins, they do not have SH3 domains. However, the presence of ANK makes these unique among protein-tyrosine kinases. Both tyrosine kinases and ANK repeats have been shown to transduce developmental signals, and SH2 domains are known to participate intimately in tyrosine kinase signaling. These tyrosine kinases are believed to be involved in epithelial cell polarity. The members of this family include the shark (SH2 domains, ANK, and kinase domain) gene in Drosophila and yellow fever mosquitos, as well as the hydra protein HTK16. Drosophila Shark is proposed to transduce intracellularly the Crumbs, a protein necessary for proper organization of ectodermal epithelia, intercellular signal. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QWLHGALDRNEAVEILKQKADADGSFLVRYSRRRPGGYVLTLVYENHVYHFEIQNRDDKWFYIDDGPYFE
SLEHLIEHYTQFADGL
>gnl|CDD|199830 cd10349, SH2_SH2D2A_SH2D7, Src homology 2 domain found in the SH2 domain containing protein 2A and 7 (SH2D2A and SH2D7). SH2D2A and SH7 both contain a single SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
AWFHGFITRREAERLLEPKPQGCYLVRFSESAVTFVLSYRSRTCCRHFLLAQLRDGRHVVLGEDSAHARL
QDLLLHY
>gnl|CDD|198213 cd10350, SH2_SH2D4A, Src homology 2 domain found in the SH2 domain containing protein 4A (SH2D4A). SH2D4A contains a single SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
KSSDTIAPWFHGILTLKKANELLLSTMPGSFLIRVSEKIKGYALSYLSEEGCKHFLIDASADSYSFLGVD
QLQHATLADLVEYHKEEPITSLGKELLLYPCGQ
>gnl|CDD|198214 cd10351, SH2_SH2D4B, Src homology 2 domain found in the SH2 domain containing protein 4B (SH2D4B). SH2D4B contains a single SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
RNTKTIAPWFHGIISREEAEALLMNATEGSFLVRVSEKIWGYTLSYRLQSGFKHFLVDASGDFYSFLGVD
PNRHATLTDLIDFHKEEIITTSGGELLQEPCGQ
>gnl|CDD|198215 cd10352, SH2_a2chimerin_b2chimerin, Src homology 2 (SH2) domain found in alpha2-chimerin and beta2-chimerin proteins. Chimerins are a family of phorbol ester- and diacylglycerol-responsive GTPase-activating proteins. Alpha1-chimerin (formerly known as n-chimerin) and alpha2-chimerin are alternatively spliced products of a single gene, as are beta1- and beta2-chimerin. alpha1- and beta1-chimerin have a relatively short N-terminal region that does not encode any recognizable domains, whereas alpha2- and beta2-chimerin both include a functional SH2 domain that can bind to phosphotyrosine motifs within receptors. All of the isoforms contain a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. Other C1 domain-containing diacylglycerol receptors including: PKC, Munc-13 proteins, phorbol ester binding scaffolding proteins involved in Ca2+-stimulated exocytosis, and RasGRPs, diacylglycerol-activated guanine-nucleotide exchange factors (GEFs) for Ras and Rap1. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
RPRFYGREYHGLISREEAEQLLSGASDGSYLIRESSRDDGYYTLSLRFNGKVKNYKLYYDGKNHYHYVGE
KRFDTIHDLVADGLITLYMET
>gnl|CDD|198216 cd10353, SH2_Nterm_RasGAP, N-terminal Src homology 2 (SH2) domain found in Ras GTPase-activating protein 1 (GAP). RasGAP is part of the GAP1 family of GTPase-activating proteins. The protein is located in the cytoplasm and stimulates the GTPase activity of normal RAS p21, but not its oncogenic counterpart. Acting as a suppressor of RAS function, the protein enhances the weak intrinsic GTPase activity of RAS proteins resulting in RAS inactivation, thereby allowing control of cellular proliferation and differentiation. Mutations leading to changes in the binding sites of either protein are associated with basal cell carcinomas. Alternative splicing results in two isoforms. The shorter isoform which lacks the N-terminal hydrophobic region, has the same activity, and is expressed in placental tissues. In general the longer isoform contains 2 SH2 domains, a SH3 domain, a pleckstrin homology (PH) domain, and a calcium-dependent phospholipid-binding C2 domain. The C-terminus contains the catalytic domain of RasGap which catalyzes the activation of Ras by hydrolyzing GTP-bound active Ras into an inactive GDP-bound form of Ras. This model contains the N-terminal SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
GPEYEEEEVAIPLTAPPTNQWYHGRLDRTIAEERLRQAGKLGSYLIRESDRRPGSFVLSFLSRTGVNHFR
IIAMCGDYYIGGRRFSSLSDLIGYYSHVSCLLK
>gnl|CDD|198217 cd10354, SH2_Cterm_RasGAP, C-terminal Src homology 2 (SH2) domain found in Ras GTPase-activating protein 1 (GAP). RasGAP is part of the GAP1 family of GTPase-activating proteins. The protein is located in the cytoplasm and stimulates the GTPase activity of normal RAS p21, but not its oncogenic counterpart. Acting as a suppressor of RAS function, the protein enhances the weak intrinsic GTPase activity of RAS proteins resulting in RAS inactivation, thereby allowing control of cellular proliferation and differentiation. Mutations leading to changes in the binding sites of either protein are associated with basal cell carcinomas. Alternative splicing results in two isoforms. The shorter isoform which lacks the N-terminal hydrophobic region, has the same activity, and is expressed in placental tissues. In general longer isoform contains 2 SH2 domains, a SH3 domain, a pleckstrin homology (PH) domain, and a calcium-dependent phospholipid-binding C2 domain. The C-terminus contains the catalytic domain of RasGap which catalyzes the activation of Ras by hydrolyzing GTP-bound active Ras into an inactive GDP-bound form of Ras. This model contains the C-terminal SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
IWFHGKISREEAYNMLVKVGGPGSFLVRESDNTPGDYSLSFRVNEGIKHFKIIPTGNNQFMMGGRYFSSL
DDVIDRY
>gnl|CDD|198218 cd10355, SH2_DAPP1_BAM32_like, Src homology 2 domain found in dual adaptor for phosphotyrosine and 3-phosphoinositides (DAPP1)/B lymphocyte adaptor molecule of 32 kDa (Bam32)-like proteins. DAPP1/Bam32 contains a putative myristoylation site at its N-terminus, followed by a SH2 domain, and a pleckstrin homology (PH) domain at its C-terminus. DAPP1 could potentially be recruited to the cell membrane by any of these domains. Its putative myristoylation site could facilitate the interaction of DAPP1 with the lipid bilayer. Its SH2 domain may also interact with phosphotyrosine residues on membrane-associated proteins such as activated tyrosine kinase receptors. And finally its PH domain exhibits a high-affinity interaction with the PtdIns(3,4,5)P(3) PtdIns(3,4)P(2) second messengers produced at the cell membrane following the activation of PI 3-kinases. DAPP1 is thought to interact with both tyrosine phosphorylated proteins and 3-phosphoinositides and therefore may play a role in regulating the location and/or activity of such proteins(s) in response to agonists that elevate PtdIns(3,4,5)P(3) and PtdIns(3,4)P(2). This protein is likely to play an important role in triggering signal transduction pathways that lie downstream from receptor tyrosine kinases and PI 3-kinase. It is likely that DAPP1 functions as an adaptor to recruit other proteins to the plasma membrane in response to extracellular signals. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
ELLQSLGWYHGNLTRHAAEALLLSNGVDGSYLLRNSNEGTGLFSLSVRAKDSVKHFHVEYTGYSFKFGFN
EFSSLQDFVKHFANQPLIGSET
>gnl|CDD|198219 cd10356, SH2_ShkA_ShkC, Src homology 2 (SH2) domain found in SH2 domain-bearing protein kinases A and C (ShkA and ShkC). SH2-bearing genes cloned from Dictyostelium include two transcription factors, STATa and STATc, and a signaling factor, SHK1 (shkA). A database search of the Dictyostelium discoideum genome revealed two additional putative STAT sequences, dd-STATb and dd-STATd, and four additional putative SHK genes, dd-SHK2 (shkB), dd-SHK3 (shkC), dd-SHK4 (shkD), and dd-SHK5 (shkE). This model contains members of shkA and shkC. All of the SHK members are most closely related to the protein kinases found in plants. However these kinases in plants are not conjugated to any SH2 or SH2-like sequences. Alignment data indicates that the SHK SH2 domains carry some features of the STAT SH2 domains in Dictyostelium. When STATc's linker domain was used for a BLAST search, the sequence between the protein kinase domain and the SH2 domain (the linker) of SHK was recovered, suggesting a close relationship among these molecules within this region. SHK's linker domain is predicted to contain an alpha-helix which is indeed homologous to that of STAT. Based on the phylogenetic alignment, SH2 domains can be grouped into two categories, STAT-type and Src-type. SHK family members are in between, but are closer to the STAT-type which indicates a close relationship between SHK and STAT families in their SH2 domains and further supports the notion that SHKs linker-SH2 domain evolved from STAT or STATL (STAT-like Linker-SH2) domain found in plants. In SHK, STAT, and SPT6, the linker-SH2 domains all reside exclusively in the C-terminal regions. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
LDKIRELMECAWFHGDISTSESENRLNGKPEGTFLVRFSTSEPGAYTISKVSKNGGISHQRIHRPGGKFQ
VNNSKYLSVKELIAGEAQALGIDTPCLGSRFLPLIYKMQLSGY
>gnl|CDD|198220 cd10357, SH2_ShkD_ShkE, Src homology 2 (SH2) domain found in SH2 domain-bearing protein kinases D and E (ShkD and ShkE). SH2-bearing genes cloned from Dictyostelium include two transcription factors, STATa and STATc, and a signaling factor, SHK1 (shkA). A database search of the Dictyostelium discoideum genome revealed two additional putative STAT sequences, dd-STATb and dd-STATd, and four additional putative SHK genes, dd-SHK2 (shkB), dd-SHK3 (shkC), dd-SHK4 (shkD), and dd-SHK5 (shkE). This model contains members of shkD and shkE. All of the SHK members are most closely related to the protein kinases found in plants. However these kinases in plants are not conjugated to any SH2 or SH2-like sequences. Alignment data indicates that the SHK SH2 domains carry some features of the STAT SH2 domains in Dictyostelium. When STATc's linker domain was used for a BLAST search, the sequence between the protein kinase domain and the SH2 domain (the linker) of SHK was recovered, suggesting a close relationship among these molecules within this region. SHK's linker domain is predicted to contain an alpha-helix which is indeed homologous to that of STAT. Based on the phylogenetic alignment, SH2 domains can be grouped into two categories, STAT-type and Src-type. SHK family members are in between, but are closer to the STAT-type which indicates a close relationship between SHK and STAT families in their SH2 domains and further supports the notion that SHKs linker-SH2 domain evolved from STAT or STATL (STAT-like Linker-SH2) domain found in plants. In SHK, STAT, and SPT6, the linker-SH2 domains all reside exclusively in the C-terminal regions. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
IMNINILLAKSWFHGDISRDEAEKRLRGRPEGTFLIRLSSTDPKKTPFTISKKKKSKPVHKRISRIDVNN
YTSFKIPGGYAVSVPLD
>gnl|CDD|198221 cd10358, SH2_PTK6_Brk, Src homology 2 domain found in protein-tyrosine kinase-6 (PTK6) which is also known as breast tumor kinase (Brk). Human protein-tyrosine kinase-6 (PTK6, also known as breast tumor kinase (Brk)) is a member of the non-receptor protein-tyrosine kinase family and is expressed in two-thirds of all breast tumors. PTK6 (9). PTK6 contains a SH3 domain, a SH2 domain, and catalytic domains. For the case of the non-receptor protein-tyrosine kinases, the SH2 domain is typically involved in negative regulation of kinase activity by binding to a phosphorylated tyrosine residue near to the C terminus. The C-terminal sequence of PTK6 (PTSpYENPT where pY is phosphotyrosine) is thought to be a self-ligand for the SH2 domain. The structure of the SH2 domain resembles other SH2 domains except for a centrally located four-stranded antiparallel beta-sheet (strands betaA, betaB, betaC, and betaD). There are also differences in the loop length which might be responsible for PTK6 ligand specificity. There are two possible means of regulation of PTK6: autoinhibitory with the phosphorylation of Tyr playing a role in its negative regulation and autophosphorylation at this site, though it has been shown that PTK6 might phosphorylate signal transduction-associated proteins Sam68 and signal transducing adaptor family member 2 (STAP/BKS) in vivo. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
SEPWFFGCISRSEAVRRLQAEGNATGAFLIRVSEKPSADYVLSVRDTQAVRHYKIWRRAGGRLHLNEAVS
FLSLPELVNYHRAQSLSHGLRLAAPCRKHE
>gnl|CDD|198222 cd10359, SH2_SH3BP2, Src homology 2 domain found in c-Abl SH3 domain-binding protein-2 (SH3BP2). The adaptor protein 3BP2/SH3BP2 plays a regulatory role in signaling from immunoreceptors. The protein-tyrosine kinase Syk phosphorylates 3BP2 which results in the activation of Rac1 through the interaction with the SH2 domain of Vav1 and induces the binding to the SH2 domain of the upstream protein-tyrosine kinase Lyn and enhances its kinase activity. 3BP2 has a positive regulatory role in IgE-mediated mast cell activation. In lymphocytes, engagement of T cell or B cell receptors triggers tyrosine phosphorylation of 3BP2. Suppression of the 3BP2 expression by siRNA results in the inhibition of T cell or B cell receptor-mediated activation of NFAT. 3BP2 is required for the proliferation of B cells and B cell receptor signaling. Mutations in the 3BP2 gene are responsible for cherubism resulting in excessive bone resorption in the jaw. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
STFKNTMESREVERLFKATSPKGGPQDGLYCIRNSSTKGGKVLVVWDGGAEKVRNYRIFEKDCKFYLHER
EVFSSLGSLVEHYATHVLPSHTSLTLRVPYG
>gnl|CDD|198223 cd10360, SH2_Srm, Src homology 2 (SH2) domain found in Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristoylation sites (srm). Srm is a nonreceptor protein kinase that has two SH2 domains, a SH3 domain, and a kinase domain with a tyrosine residue for autophosphorylation. However it lacks an N-terminal glycine for myristoylation and a C-terminal tyrosine which suppresses kinase activity when phosphorylated. Srm is most similar to members of the Tec family who other members include: Tec, Btk/Emb, and Itk/Tsk/Emt. However Srm differs in its N-terminal unique domain it being much smaller than in the Tec family and is closer to Src. Srm is thought to be a new family of nonreceptor tyrosine kinases that may be redundant in function. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
PWYFSGISRTQAQQLLLSPPNEPGAFLIRPSESSLGGYSLSVRAQAKVCHYRICMAPSGSLYLQKGRLFP
GLEELLAYY
>gnl|CDD|198224 cd10361, SH2_Fps_family, Src homology 2 (SH2) domain found in feline sarcoma, Fujinami poultry sarcoma, and fes-related (Fes/Fps/Fer) proteins. The Fps family consists of members Fps/Fes and Fer/Flk/Tyk3. They are cytoplasmic protein-tyrosine kinases implicated in signaling downstream from cytokines, growth factors and immune receptors. Fes/Fps/Fer contains three coiled-coil regions, an SH2 (Src-homology-2) and a TK (tyrosine kinase catalytic) domain signature. Members here include: Fps/Fes, Fer, Kin-31, and In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
KDLENEPYYHGLLPREDAEELLKNDGDFLVRKTEPKGGGKRKLVLSVRWDGKIRHFVINRDDGGKYYIEG
KSFKSISELINYYQKTKEPI
>gnl|CDD|198225 cd10362, SH2_Src_Lck, Src homology 2 (SH2) domain in lymphocyte cell kinase (Lck). Lck is a member of the Src non-receptor type tyrosine kinase family of proteins. It is expressed in the brain, T-cells, and NK cells. The unique domain of Lck mediates its interaction with two T-cell surface molecules, CD4 and CD8. It associates with their cytoplasmic tails on CD4 T helper cells and CD8 cytotoxic T cells to assist signaling from the T cell receptor (TCR) complex. When the T cell receptor is engaged by the specific antigen presented by MHC, Lck phosphorylase the intracellular chains of the CD3 and zeta-chains of the TCR complex, allowing ZAP-70 to bind them. Lck then phosphorylates and activates ZAP-70, which in turn phosphorylates Linker of Activated T cells (LAT), a transmembrane protein that serves as a docking site for proteins including: Shc-Grb2-SOS, PI3K, and phospholipase C (PLC). The tyrosine phosphorylation cascade culminates in the intracellular mobilization of a calcium ions and activation of important signaling cascades within the lymphocyte, including the Ras-MEK-ERK pathway, which goes on to activate certain transcription factors such as NFAT, NF-kappaB, and AP-1. These transcription factors regulate the production cytokines such as Interleukin-2 that promote long-term proliferation and differentiation of the activated lymphocytes. The N-terminal tail of Lck is myristoylated and palmitoylated and it tethers the protein to the plasma membrane of the cell. Lck also contains a SH3 domain, a SH2 domain, and a C-terminal tyrosine kinase domain. Lck has 2 phosphorylation sites, the first an autophosphorylation site that is linked to activation of the protein and the second which is phosphorylated by Csk, which inhibits it. Lck is also inhibited by SHP-1 dephosphorylation and by Cbl ubiquitin ligase, which is part of the ubiquitin-mediated pathway. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
EPEPWFFKNLSRNDAERQLLAPGNTHGSFLIRESETTAGSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFY
ISPRITFPGLHELVRHYTNASDGLCTRLSRP
>gnl|CDD|198226 cd10363, SH2_Src_HCK, Src homology 2 (SH2) domain found in HCK. HCK is a member of the Src non-receptor type tyrosine kinase family of proteins and is expressed in hemopoietic cells. HCK is proposed to couple the Fc receptor to the activation of the respiratory burst. It may also play a role in neutrophil migration and in the degranulation of neutrophils. It has two different translational starts that have different subcellular localization. HCK has been shown to interact with BCR gene, ELMO1 Cbl gene, RAS p21 protein activator 1, RASA3, Granulocyte colony-stimulating factor receptor, ADAM15 and RAPGEF1. Like the other members of the Src family the SH2 domain in addition to binding the target, also plays an autoinhibitory role by binding to its C-terminal tail. In general SH2 domains are involved in signal transduction. HCK has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
ETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSYSLSVRDYDPQHGDTVKHYKIRTLDNGGFY
ISPRSTFSTLQELVDHYKKGNDGLCQKLSVPCMS
>gnl|CDD|198227 cd10364, SH2_Src_Lyn, Src homology 2 (SH2) domain found in Lyn. Lyn is a member of the Src non-receptor type tyrosine kinase family of proteins and is expressed in the hematopoietic cells, in neural tissues, liver, and adipose tissue. There are two alternatively spliced forms of Lyn. Lyn plays an inhibitory role in myeloid lineage proliferation. Following engagement of the B cell receptors, Lyn undergoes rapid phosphorylation and activation, triggering a cascade of signaling events mediated by Lyn phosphorylation of tyrosine residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the receptor proteins, and subsequent recruitment and activation of other kinases including Syk, phospholipase C2 (PLC2) and phosphatidyl inositol-3 kinase. These kinases play critical roles in proliferation, Ca2+ mobilization and cell differentiation. Lyn plays an essential role in the transmission of inhibitory signals through phosphorylation of tyrosine residues within the immunoreceptor tyrosine-based inhibitory motifs (ITIM) in regulatory proteins such as CD22, PIR-B and FC RIIb1. Their ITIM phosphorylation subsequently leads to recruitment and activation of phosphatases such as SHIP-1 and SHP-1 which further down modulate signaling pathways, attenuate cell activation and can mediate tolerance. Lyn also plays a role in the insulin signaling pathway. Activated Lyn phosphorylates insulin receptor substrate 1 (IRS1) leading to an increase in translocation of Glut-4 to the cell membrane and increased glucose utilization. It is the primary Src family member involved in signaling downstream of the B cell receptor. Lyn plays an unusual, 2-fold role in B cell receptor signaling; it is essential for initiation of signaling but is also later involved in negative regulation of the signal. Lyn has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
ETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSYSLSVRDYDPQHGDVIKHYKIRSLDNGGYY
ISPRITFPCISDMIKHYQKQSDGLCRRLEKA
>gnl|CDD|198228 cd10365, SH2_Src_Src, Src homology 2 (SH2) domain found in tyrosine kinase sarcoma (Src). Src is a member of the Src non-receptor type tyrosine kinase family of proteins. Src is thought to play a role in the regulation of embryonic development and cell growth. Members here include v-Src and c-Src. v-Src lacks the C-terminal inhibitory phosphorylation site and is therefore constitutively active as opposed to normal cellular src (c-Src) which is only activated under certain circumstances where it is required (e.g. growth factor signaling). v-Src is an oncogene whereas c-Src is a proto-oncogene. c-Src consists of three domains, an N-terminal SH3 domain, a central SH2 domain and a tyrosine kinase domain. The SH2 and SH3 domains work together in the auto-inhibition of the kinase domain. The phosphorylation of an inhibitory tyrosine near the c-terminus of the protein produces a binding site for the SH2 domain which then facilitates binding of the SH3 domain to a polyproline site within the linker between the SH2 domain and the kinase domain. Binding of the SH3 domain inactivates the enzyme. This allows for multiple mechanisms for c-Src activation: dephosphorylation of the C-terminal tyrosine by a protein tyrosine phosphatase, binding of the SH2 domain by a competitive phospho-tyrosine residue, or competitive binding of a polyproline binding site to the SH3 domain. Unlike most other Src members Src lacks cysteine residues in the SH4 domain that undergo palmitylation. Serine and threonine phosphorylation sites have also been identified in the unique domains of Src and are believed to modulate protein-protein interactions or regulate catalytic activity. Alternatively spliced forms of Src, which contain 6- or 11-amino acid insertions in the SH3 domain, are expressed in CNS neurons. c-Src has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFY
ITSRTQFNSLQQLVAYYSKHADGLCHRLTTV
>gnl|CDD|198229 cd10366, SH2_Src_Yes, Src homology 2 (SH2) domain found in Yes. Yes is a member of the Src non-receptor type tyrosine kinase family of proteins. Yes is the cellular homolog of the Yamaguchi sarcoma virus oncogene. In humans it is encoded by the YES1 gene which maps to chromosome 18 and is in close proximity to thymidylate synthase. A corresponding Yes pseudogene has been found on chromosome 22. YES1 has been shown to interact with Janus kinase 2, CTNND1,RPL10, and Occludin. Yes1 has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEVRGDNVKHYKIRKLDNGGYY
ITTRAQFDTLQKLVKHYTEHADGLCHKLTTV
>gnl|CDD|198230 cd10367, SH2_Src_Fgr, Src homology 2 (SH2) domain found in Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog, Fgr. Fgr is a member of the Src non-receptor type tyrosine kinase family of proteins. The protein contains N-terminal sites for myristoylation and palmitoylation, a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine-containing and proline-rich motifs, respectively. Fgr is expressed in B-cells and myeloid cells, localizes to plasma membrane ruffles, and functions as a negative regulator of cell migration and adhesion triggered by the beta-2 integrin signal transduction pathway. Multiple alternatively spliced variants, encoding the same protein, have been identified Fgr has been shown to interact with Wiskott-Aldrich syndrome protein. Fgr has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QAEEWYFGKIGRKDAERQLLSPGNPRGAFLIRESETTKGAYSLSIRDWDQNRGDHVKHYKIRKLDTGGYY
ITTRAQFDTVQELVQHYMEVNDGLCYLLTAP
>gnl|CDD|198231 cd10368, SH2_Src_Fyn, Src homology 2 (SH2) domain found in Fyn. Fyn is a member of the Src non-receptor type tyrosine kinase family of proteins. Fyn is involved in the control of cell growth and is required in the following pathways: T and B cell receptor signaling, integrin-mediated signaling, growth factor and cytokine receptor signaling, platelet activation, ion channel function, cell adhesion, axon guidance, fertilization, entry into mitosis, and differentiation of natural killer cells, oligodendrocytes and keratinocytes. The protein associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the Fyn-binding protein. Alternatively spliced transcript variants encoding distinct isoforms exist. Fyn is primarily localized to the cytoplasmic leaflet of the plasma membrane. Tyrosine phosphorylation of target proteins by Fyn serves to either regulate target protein activity, and/or to generate a binding site on the target protein that recruits other signaling molecules. FYN has been shown to interact with a number of proteins including: BCAR1, Cbl, Janus kinase, nephrin, Sky, tyrosine kinase, Wiskott-Aldrich syndrome protein, and Zap-70. Fyn has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYY
ITTRAQFETLQQLVQHYSETANGLCKVLIVT
>gnl|CDD|199831 cd10369, SH2_Src_Frk, Src homology 2 (SH2) domain found in the Fyn-related kinase (Frk). Frk is a member of the Src non-receptor type tyrosine kinase family of proteins. The Frk subfamily is composed of Frk/Rak and Iyk/Bsk/Gst. It is expressed primarily epithelial cells. Frk is a nuclear protein and may function during G1 and S phase of the cell cycle and suppress growth. Unlike the other Src members it lacks a glycine at position 2 of SH4 which is important for addition of a myristic acid moiety that is involved in targeting Src PTKs to cellular membranes. FRK and SHB exert similar effects when overexpressed in rat phaeochromocytoma (PC12) and beta-cells, where both induce PC12 cell differentiation and beta-cell proliferation. Under conditions that cause beta-cell degeneration these proteins augment beta-cell apoptosis. The FRK-SHB responses involve FAK and insulin receptor substrates (IRS) -1 and -2. Frk has been demonstrated to interact with retinoblastoma protein. Frk regulates PTEN protein stability by phosphorylating PTEN, which in turn prevents PTEN degradation. Frk also plays a role in regulation of embryonal pancreatic beta cell formation. Frk has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. Like the other members of the Src family the SH2 domain in addition to binding the target, also plays an autoinhibitory role by binding to its activation loop. The tryosine involved is at the same site as the tyrosine involved in the autophosphorylation of Src. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QAEPWFFGAIKRADAEKQLLYSENQTGAFLIRESESQKGEFSLSVLDGGVVKHYRIRRLDEGGFFLTRRK
TFSTLNEFVNYYTTTSDGLCVKLGKP
>gnl|CDD|198233 cd10370, SH2_Src_Src42, Src homology 2 (SH2) domain found in the Src oncogene at 42A (Src42). Src42 is a member of the Src non-receptor type tyrosine kinase family of proteins. The integration of receptor tyrosine kinase-induced RAS and Src42 signals by Connector eNhancer of KSR (CNK) as a two-component input is essential for RAF activation in Drosophila. Src42 is present in a wide variety of organisms including: California sea hare, pea aphid, yellow fever mosquito, honey bee, Panamanian leafcutter ant, and sea urchin. Src42 has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. Like the other members of the Src family the SH2 domain in addition to binding the target, also plays an autoinhibitory role by binding to its C-terminal tail. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
EAEPWYFGKIKRIEAEKKLLLPENEHGAFLIRDSESRHNDYSLSVRDGDTVKHYRIRQLDEGGFFIARRT
TFRTLQELVEHYSKDSDGLCVNLRKP
>gnl|CDD|198234 cd10371, SH2_Src_Blk, Src homology 2 (SH2) domain found in B lymphoid kinase (Blk). Blk is a member of the Src non-receptor type tyrosine kinase family of proteins. Blk is expressed in the B-cells. Unlike most other Src members Blk lacks cysteine residues in the SH4 domain that undergo palmitylation. Blk is required for the development of IL-17-producing gamma-delta T cells. Furthermore, Blk is expressed in lymphoid precursors and, in this capacity, plays a role in regulating thymus cellularity during ontogeny. Blk has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
EVEKWFFRTISRKDAERQLLAPMNKAGSFLIRESESNKGAFSLSVKDVTTQGEVVKHYKIRSLDNGGYYI
SPRITFPTLQALVQHYSKKGDGLCQKLTLP
>gnl|CDD|198235 cd10372, SH2_STAT1, Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 1 proteins. STAT1 is a member of the STAT family of transcription factors. STAT1 is involved in upregulating genes due to a signal by interferons. STAT1 forms homodimers or heterodimers with STAT3 that bind to the Interferon-Gamma Activated Sequence (GAS) promoter element in response to IFN-gamma stimulation. STAT1 forms a heterodimer with STAT2 that can bind Interferon Stimulated Response Element (ISRE) promoter element in response to either IFN-alpha or IFN-beta stimulation. Binding in both cases leads to an increased expression of ISG (Interferon Stimulated Genes). STAT1 has been shown to interact with protein kinase R, Src, IRF1, STAT3, MCM5, STAT2, CD117, Fanconi anemia, complementation group C, CREB-binding protein, Interleukin 27 receptor, alpha subunit, PIAS1, BRCA1, Epidermal growth factor receptor, PTK2, Mammalian target of rapamycin, IFNAR2, PRKCD, TRADD, C-jun, Calcitriol receptor, ISGF3G, and GNB2L1. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
WIESILELIKKHLLSLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSREGAITFTWVERSQNGGEP
DFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPEPMELDGP
KGTGYIKTELI
>gnl|CDD|198236 cd10373, SH2_STAT2, Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 2 proteins. STAT2 is a member of the STAT protein family. In response to interferon, STAT2 forms a complex with STAT1 and IFN regulatory factor family protein p48 (ISGF3G), in which this protein acts as a transactivator, but lacks the ability to bind DNA directly. Transcription adaptor P300/CBP (EP300/CREBBP) has been shown to interact specifically with STAT2, which is thought to be involved in the process of blocking IFN-alpha response by adenovirus. STAT2 has been shown to interact with MED14, CREB-binding protein, SMARCA4, STAT1, IFNAR2, IFNAR1, and ISGF3G. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKTISGTFLLRFSETSEGGITCSWVEHQDDDKVLI
YSVQPYTKEVLQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLEEREKYLKHKL
IVVSNRQVDEL
>gnl|CDD|198237 cd10374, SH2_STAT3, Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 3 proteins. STAT3 encoded by this gene is a member of the STAT protein family. STAT3 mediates the expression of a variety of genes in response to cell stimuli, and plays a key role in many cellular processes such as cell growth and apoptosis. The small GTPase Rac1 regulates the activity of STAT3 and PIAS3 inhibits it. Three alternatively spliced transcript variants encoding distinct isoforms have been described. STAT 3 activation is required for self-renewal of embryonic stem cells (ESCs) and is essential for the differentiation of the TH17 helper T cells. Mutations in the STAT3 gene result in Hyperimmunoglobulin E syndrome and human cancers. STAT3 has been shown to interact with Androgen receptor, C-jun, ELP2, EP300, Epidermal growth factor receptor, Glucocorticoid receptor, HIF1A, Janus kinase 1, KHDRBS1, Mammalian target of rapamycin, MyoD, NDUFA13, NFKB1, Nuclear receptor coactivator 1, Promyelocytic leukemia protein, RAC1, RELA, RET proto-oncogene, RPA2, Src, STAT1, and TRIP10. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
MAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTW
VEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQE
HPEADPGSAAPYLKTKFICVTP
>gnl|CDD|198238 cd10375, SH2_STAT4, Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 4proteins. STAT4 mediate signals from the IL-12 receptors. STAT4 is mainly phosphorylated by IL-12-mediated signaling pathway in T cells. STAT4 expression is restricted in myeloid cells, thymus and testis. L-12 is the major cytokine that can activate STAT4, resulting in its tyrosine phosphorylation. The IL-12 receptor has two chains, termed IL-12R 1 and IL-12R 2, and ligand binding results in heterodimer formation and activation of the receptor associated JAK kinases, Jak2 and Tyk2. Phosphorylated STAT4 homo-dimerizes via its SH2 domain, and translocates into nucleus where it can recognize traditional N3 STAT target sequences in IL-12 responsive genes. STAT4 can also be phosphorylated in response to IFN-gamma stimulation through activation of Jak1 and Tyk2 in human. IL-17 can also activate STAT4 in human monocytic leukemia cell lines and IL-2 can induce Jak2 and Stat4 activation in NK cells but not in T cells. T helper 1 (Th1) cells produce IL-2 and IFNgamma, whereas Th2 cells secrete IL-4, IL-5, IL-6 and IL-13. Th1 cells are responsible for cell-mediated/inflammatory immunity and can enhance defenses against infectious agents and cancer, while Th2 cells are essential for humoral immunity and the clearance of parasitic antigens. The most potent factors that can promote Th1 and Th2 differentiation are the cytokines IL-12 and IL-4 respectively Although STAT4 is expressed both in Th1 and Th2 cells, STAT4 can only be phosphorylated by IL-12 which suggests that STAT4 plays an important role in Th1 cell function or development. STAT4 activation leads to Th1 differentiation, including the target genes of STAT4 such as ERM, a transcription factor that belongs to the Ets family of transcription factors. The expression of ERM is specifically induced by IL-12 in wild-type Th1 cells, but not in STAT4-deficient T cells. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
WLEAILDLIKKHILPLWIDGYIMGFVSKEKERLLLKDKMPGTFLLRFSESHLGGITFTWVDQSENGEVRF
HSVEPYNKGRLSALPFADILRDYKVIMAENIPENPLKYLYPDIPKDKAFGKHYSSQPCEVSRPTERGDKG
YVPSVFIP
>gnl|CDD|198239 cd10376, SH2_STAT5, Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5 proteins. STAT5 is a member of the STAT family of transcription factors. Two highly related proteins, STAT5a and STAT5b are encoded by separate genes, but are 90% identical at the amino acid level. Both STAT5a and STAT5b are ubiquitously expressed and functionally interchangeable. Mice lacking either STAT5a or STAT5b have mild defects in prolactin dependent mammary differentiation or sexually dimorphic growth hormone-dependent effects, respectively. Mice lacking both STAT5a and STAT5b exhibit a perinatal lethal phenotype and have multiple defects, including anemia and a virtual absence of B and T lymphocytes. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins
WFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPDRALWN
LMPFTTRDFSIRSLADRLGDLNYLIYVFPDRPKDEVFSKYYTPVLCNPSAVDGYVKPQIKQVVPEFV
>gnl|CDD|198240 cd10377, SH2_STAT6, Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 6 proteins. STAT6 mediate signals from the IL-4 receptor. Unlike the other STAT proteins which bind an IFNgamma Activating Sequence (GAS), STAT6 stands out as having a unique binding site preference. This site consists of a palindromic sequence separated by a 3 bp spacer (TTCNNNG-AA)(N3 site). STAT6 is able to bind the GAS site but only at a low affinity. STAT6 may be an important regulator of mitogenesis when cells respond normally to IL-4. There is speculation that the inappropriate activation of STAT6 is involved in uncontrolled cell growth in an oncogenic state. IFNgamma is a negative regulator of STAT6 dependent transcription of target genes. Bcl-6 is another negative regulator of STAT6 activity. Bcl-6 is a transcriptional repressor normally expressed in germinal center B cells and some T cells. IL-4 signaling via STAT6 initially occurs unopposed, but is then dampened by a negative feedback mechanism through the IL-4/Stat6 dependent induction of SOCS1 expression. The IL-4 dependent aspect of Th2 differentiation requires the activation of STAT6. IL-4 signaling and STAT6 appear to play an important role in the immune response. Recently, it was shown that large scale chromatin remodeling of the IL-4 gene occurs as cells differentiate into Th2 effectors is STAT6 dependent. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
WFDGVLDLTKRCLRSYWSDRLIIGFISKQYVTSLLLNEPDGTFLLRFSDSEIGGITIAHVIRGQDGSPQI
ENIQPFSAKDLSIRSLGDRIRDLAQLKNLYPKKPKDEAFRSHYKPEQMKDGRGYVPATI
>gnl|CDD|198241 cd10378, SH2_Jak1, Src homology 2 (SH2) domain in the Janus kinase 1 (Jak1) proteins. Janus kinase 1 (JAK1), is a member of a class of protein-tyrosine kinases (PTK) characterized by the presence of a second phosphotransferase-related domain immediately N-terminal to the PTK domain. The second phosphotransferase domain bears all the hallmarks of a protein kinase, although its structure differs significantly from that of the PTK and threonine/serine kinase family members. JAK1 is a large, widely expressed membrane-associated phosphoprotein. JAK1 is involved in the interferon-alpha/beta and -gamma signal transduction pathways. The reciprocal interdependence between JAK1 and TYK2 activities in the interferon-alpha pathway, and between JAK1 and JAK2 in the interferon-gamma pathway, may reflect a requirement for these kinases in the correct assembly of interferon receptor complexes. These kinases couple cytokine ligand binding to tyrosine phosphorylation of various known signaling proteins and of a unique family of transcription factors termed the signal transducers and activators of transcription, or STATs. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
DVAPPLIVHNIKNGCHGPICTEYAINKLRQEGNEEGMYVLRWSCTDFNNILMTVTCIELSECESRPVKQY
KNFQIEVKKGGYSLHGSDTFFPSLKELMEHLK
>gnl|CDD|198242 cd10379, SH2_Jak2, Src homology 2 (SH2) domain in the Janus kinase 2 (Jak2) proteins. Jak2 is a protein tyrosine kinase involved in a specific subset of cytokine receptor signaling pathways. It has been found to be constitutively associated with the prolactin receptor and is required for responses to gamma interferon. Mice that do not express an active protein for this gene exhibit embryonic lethality associated with the absence of definitive erythropoiesis. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
EVAPPRLLEAIQSYCHGPISMEFAISKLRKAGNQTGLYILRCSPKDYNKYFLTFAVEREGALEYKHCLIT
KNENGEYNLSGAKKSFGSLKDLLNCYQ
>gnl|CDD|198243 cd10380, SH2_Jak3, Src homology 2 (SH2) domain in the Janus kinase 3 (Jak3) proteins. Jak3 is a member of the Janus kinase (JAK) family of tyrosine kinases involved in cytokine receptor-mediated intracellular signal transduction. It is predominantly expressed in immune cells and transduces a signal in response to its activation via tyrosine phosphorylation by interleukin receptors. Mutations in this gene are associated with autosomal SCID (severe combined immunodeficiency disease). In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
EVAPPRLLEDIENQCHGPITSEFAVNKLKKAGSEPGSFVLRRSPQDFDKFLLTVCVQTTLGLDYKDCLIR
KNEGHFSLAGVSRSFSSLKELLVTYQ
>gnl|CDD|198244 cd10381, SH2_Jak_Tyk2, Src homology 2 (SH2) domain in Tyrosine Kinase 2 (Tyk2), a member of the Janus kinases (JAK). Tyk2 is a member of the tyrosine kinase and, more specifically, the Janus kinases (JAKs) protein families. This protein associates with the cytoplasmic domain of type I and type II cytokine receptors and promulgate cytokine signals by phosphorylating receptor subunits. It is also component of both the type I and type III interferon signaling pathways. As such, it may play a role in anti-viral immunity. A mutation in this gene has been associated with hyperimmunoglobulin E syndrome (HIES) - a primary immunodeficiency characterized by elevated serum immunoglobulin E. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
EVAPPRLVTSIQNGIHGPMMDPFVQAKLKKEWPEEGLYLIRWSTLDLHRLILAVAHRNPAXSNGPGGLRL
RQFRIQQKGSAFVLEGWGREFASVGDLRDALQ
>gnl|CDD|198245 cd10382, SH2_SOCS1, Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins. SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
TRTSAMLDASGFYWGPLSVEEAHAKLKREPVGTFLIRDSRQKNCFFALSVKMASGPVSIRILFKAGKFSL
DGSKESFDCLFKLLEHYVASPKKMLGRP
>gnl|CDD|198246 cd10383, SH2_SOCS2, Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins. SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
MRELSQTGWYWGSMTVNEAKEKLQDAPEGTFLVRDSSHSDYLLTISVKTSAGPTNLRIEYQDGKFRLDSI
ICVKSKLKQFDSVVHLIEYYVQMCKDKRTGPEA
>gnl|CDD|198247 cd10384, SH2_SOCS3, Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins. SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
VNAVRKLQESGFYWSTVSGKEANLLLSAEPAGTFLIRDSSDQRHFFTLSVKTESGTKNLRIQCEGGSFSL
QTDPRSTQPVPRFDCVLKLVHHYMPPSAAPS
>gnl|CDD|198248 cd10385, SH2_SOCS4, Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins. SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
VPDLLQINNNPCYWGVMDKYAAEALLEGKPEGTFLLRDSAQEDYLFSVSFRRYSRSLHARIEQWNHNFSF
DAHDPCVFHSPDITGLLEHYKDPSACMFFEP
>gnl|CDD|198249 cd10386, SH2_SOCS5, Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) family. SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
PCYWGVMDRYEAEALLEGKPEGTFLLRDSAQEDYLFSVSFRRYNRSLHARIEQWNHNFSFDAHDPCVFHS
STVTGLLEHYK
>gnl|CDD|198250 cd10387, SH2_SOCS6, Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins. SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
TEELKKLAKQGWYWGPITRWEAEGKLANVPDGSFLVRDSSDDRYLLSLSFRSHGKTLHTRIEHSNGRFSF
YEQPDVEGHTSIVDLIEHSIRDSENGAFCY
>gnl|CDD|198251 cd10388, SH2_SOCS7, Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins. SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
TASLRELKDCGWYWGPMSWEDAEKVLSNKPDGSFLVRDSSDDRYIFSLSFRSQGSVHHTRIEQYQGTFSL
GSRNKFVDRSQSLVEFIERAVEHSRSGRFLY
>gnl|CDD|198252 cd10389, SH2_SHB, Src homology 2 domain found in SH2 domain-containing adapter protein B (SHB). SHB functions in generating signaling compounds in response to tyrosine kinase activation. SHB contains proline-rich motifs, a phosphotyrosine binding (PTB) domain, tyrosine phosphorylation sites, and a SH2 domain. SHB mediates certain aspects of platelet-derived growth factor (PDGF) receptor-, fibroblast growth factor (FGF) receptor-, neural growth factor (NGF) receptor TRKA-, T cell receptor-, interleukin-2 (IL-2) receptor- and focal adhesion kinase- (FAK) signaling. SRC-like FYN-Related Kinase FRK/RAK (also named BSK/IYK or GTK) and SHB regulate apoptosis, proliferation and differentiation. SHB promotes apoptosis and is also required for proper mitogenicity, spreading and tubular morphogenesis in endothelial cells. SHB also plays a role in preventing early cavitation of embryoid bodies and reduces differentiation to cells expressing albumin, amylase, insulin and glucagon. SHB is a multifunctional protein that has difference responses in different cells under various conditions. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QIWYHGAISRGDAENLLRLCKECSYLVRNSQTSKHDYSLSLKSNQGFMHMKLAKTKEKYVLGQNSPPFDS
VPEVIHYYTTRKLPIKGAEHLSLLYPV
>gnl|CDD|198253 cd10390, SH2_SHD, Src homology 2 domain found in SH2 domain-containing adapter proteins D (SHD). The expression of SHD is restricted to the brain. SHD may be a physiological substrate of c-Abl and may function as an adapter protein in the central nervous system. It is also thought to be involved in apoptotic regulation. SHD contains five YXXP motifs, a substrate sequence preferred by Abl tyrosine kinases, in addition to a poly-proline rich region and a C-terminal SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QPWFHGPLSRADAENLLSLCKEGSYLVRLSETRPQDCSLSLRSSQGFLHLKFARTRENQVVLGQHSGPFP
SVPELVLHYSSRPLPVQGAEHLALLYPV
>gnl|CDD|198254 cd10391, SH2_SHE, Src homology 2 domain found in SH2 domain-containing adapter protein E (SHE). SHE is expressed in heart, lung, brain, and skeletal muscle. SHE contains two pTry protein binding domains, protein interaction domain (PID) and a SH2 domain, followed by a glycine-proline rich region, all of which are N-terminal to the phosphotyrosine binding (PTB) domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QPWYHGSISRAEAESRLQPCKEASYLVRNSESGNSKYSIALKTSQGCVHIIVAQTKDNKYTLNQTSAVFD
SIPEVVHYYSNEKLPFKGAEHMTLLHPV
>gnl|CDD|198255 cd10392, SH2_SHF, Src homology 2 domain found in SH2 domain-containing adapter protein F (SHF). SHF is thought to play a role in PDGF-receptor signaling and regulation of apoptosis. SHF is mainly expressed in skeletal muscle, brain, liver, prostate, testis, ovary, small intestine, and colon. SHF contains four putative tyrosine phosphorylation sites and an SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QVWYHGAISRTDAENLLRLCKEASYLVRNSETSKNDFSLSLKSSQGFMHMKLSRTKEHKYVLGQNSPPFS
SVPEIIHHYASRKLPIKGAEHMSLLYPV
>gnl|CDD|198256 cd10393, SH2_RIN1, Src homology 2 (SH2) domain found in Ras and Rab interactor 1 (RIN1)-like proteins. RIN1, a member of the RIN (AKA Ras interaction/interference) family, have multifunctional domains including SH2 and proline-rich (PR) domains in the N-terminal region, and RIN-family homology (RH), VPS9 and Ras-association (RA) domains in the C-terminal region. RIN proteins function as Rab5-GEFs. Previous studies showed that RIN1 interacts with EGF receptors via its SH2 domain and regulates trafficking and degradation of EGF receptors via its interaction with STAM, indicating a vital role for RIN1 in regulating endosomal trafficking of receptor tyrosine kinases (RTKs). RIN1 was first identified as a Ras-binding protein that suppresses the activated RAS2 allele in S. cerevisiae. RIN1 binds to the activated Ras through its carboxyl-terminal domain and this Ras-binding domain also binds to 14-3-3 proteins as Raf-1 does. The SH2 domain of RIN1 are thought to interact with the phosphotyrosine-containing proteins, but the physiological partners for this domain are unknown. The proline-rich domain in RIN1 is similar to the consensus SH3 binding regions. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
LRERLLLTRPVWLQLRANAAAALHVLRTEPPGTFLVRKSNTRQCQALCVRLPEASGPSFVSSHYIQESPG
GVSLEGSELTFPDLVQLICAYCHTRDILLLP
>gnl|CDD|198257 cd10394, SH2_RIN2, Src homology 2 (SH2) domain found in Ras and Rab interactor 2 (RIN2)-like proteins. RIN2, a member of the RIN (AKA Ras interaction/interference) family, have multifunctional domains including SH2 and proline-rich (PR) domains in the N-terminal region, and RIN-family homology (RH), VPS9 and Ras-association (RA) domains in the C-terminal region. RIN proteins function as Rab5-GEFs. Ras induces activation of Rab5 through RIN2, which is a direct downstream target of Ras and a direct upstream regulator of Rab5. In other words it is the binding of the GTP-bound form of Ras to the RA domain of RIN2 that enhances the GEF activity toward Rab5. It is thought that the RA domain negatively regulates the Rab5 GEF activity. In steady state, RIN2 is likely to form a closed conformation by an intramolecular interaction between the RA domain and the Vps9p-like (Rab5 GEF) domain, negatively regulating the Rab5 GEF activity. In the active state, the binding of Ras to the RA domain may reduce the intramolecular interaction and stabilize an open conformation of RIN2. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
ILDRLLHTHPIWLQLSLSEEEAAEVLQAQPPGIFLVRKSSKMQKKVLSLRLPCEFGAPLKEFAIKESTYT
FSLEGSGISFADLFRLIAFYCISRDVLPFT
>gnl|CDD|198258 cd10395, SH2_RIN3, Src homology 2 (SH2) domain found in Ras and Rab interactor 3 (RIN3)-like proteins. RIN3, a member of the RIN (AKA Ras interaction/interference) family, have multifunctional domains including SH2 and proline-rich (PR) domains in the N-terminal region, and RIN-family homology (RH), VPS9 and Ras-association (RA) domains in the C-terminal region. RIN proteins function as Rab5-GEFs. RIN3 stimulated the formation of GTP-bound Rab31, a Rab5-subfamily GTPase, and formed enlarged vesicles and tubular structures, where it colocalized with Rab31. Transferrin appeared to be transported partly through the RIN3-positive vesicles to early endosomes. RIN3 interacts via its Pro-rich domain with amphiphysin II, which contains SH3 domain and participates in receptor-mediated endocytosis. RIN3, a Rab5 and Rab31 GEF, plays an important role in the transport pathway from plasma membrane to early endosomes. Mutations in the region between the SH2 and RH domain of RIN3 specifically abolished its GEF action on Rab31, but not Rab5. RIN3 was also found to partially translocate the cation-dependent mannose 6-phosphate receptor from the trans-Golgi network to peripheral vesicles and that this is dependent on its Rab31-GEF activity. These data indicate that RIN3 specifically acts as a GEF for Rab31. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
ILEKLIKTCPVWLQLGMNQAEAARILHKEVAGMFLVRRDSNSKQMVLCVHFPSNESSAEVLEYPIKEEKS
ILYLEGSVLVFEDIFKLIAFYCVSRDLLPFT
>gnl|CDD|198259 cd10396, SH2_Tec_Itk, Src homology 2 (SH2) domain found in Tec protein, IL2-inducible T-cell kinase (Itk). A member of the Tec protein tyrosine kinase Itk is expressed thymus, spleen, lymph node, T lymphocytes, NK and mast cells. It plays a role in T-cell proliferation and differentiation, analogous to Tec family kinases Txk. Itk has been shown to interact with Fyn, Wiskott-Aldrich syndrome protein, KHDRBS1, PLCG1, Lymphocyte cytosolic protein 2, Linker of activated T cells, Karyopherin alpha 2, Grb2, and Peptidylprolyl isomerase A. Most of the Tec family members have a PH domain (Txk and the short (type 1) splice variant of Drosophila Btk29A are exceptions), a Tec homology (TH) domain, a SH3 domain, a SH2 domain, and a protein kinase catalytic domain. The TH domain consists of a Zn2+-binding Btk motif and a proline-rich region. The Btk motif is found in Tec kinases, Ras GAP, and IGBP. It is crucial for the function of Tec PH domains and it's lack of presence in Txk is not surprising since it lacks a PH domain. The type 1 splice form of the Drosophila homolog also lacks both the PH domain and the Btk motif. The proline-rich regions are highly conserved for the most part with the exception of Bmx whose residues surrounding the PXXP motif are not conserved (TH-like) and Btk29A which is entirely unique with large numbers of glycine residues (TH-extended). Tec family members all lack a C-terminal tyrosine having an autoinhibitory function in its phosphorylated state. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
NNLDQYEWYNKNINRSKAEKLLRDEGKEGGFMVRDSSQPGLYTVSLYTKAGGEGNPCIRHYHIKETNDSP
KKYYLAEKHVFNSIPELIEYHKHNAAGLVTRLRYPVSS
>gnl|CDD|198260 cd10397, SH2_Tec_Btk, Src homology 2 (SH2) domain found in Tec protein, Bruton's tyrosine kinase (Btk). A member of the Tec protein tyrosine kinase Btk is expressed in bone marrow, spleen, all hematopoietic cells except T lymphocytes and plasma cells where it plays a crucial role in B cell maturation and mast cell activation. Btk has been shown to interact with GNAQ, PLCG2, protein kinase D1, B-cell linker, SH3BP5, caveolin 1, ARID3A, and GTF2I. Most of the Tec family members have a PH domain (Txk and the short (type 1) splice variant of Drosophila Btk29A are exceptions), a Tec homology (TH) domain, a SH3 domain, a SH2 domain, and a protein kinase catalytic domain. Btk is implicated in the primary immunodeficiency disease X-linked agammaglobulinemia (Bruton's agammaglobulinemia). The TH domain consists of a Zn2+-binding Btk motif and a proline-rich region. The Btk motif is found in Tec kinases, Ras GAP, and IGBP. It is crucial for the function of Tec PH domains and it's lack of presence in Txk is not surprising since it lacks a PH domain. The type 1 splice form of the Drosophila homolog also lacks both the PH domain and the Btk motif. The proline-rich regions are highly conserved for the most part with the exception of Bmx whose residues surrounding the PXXP motif are not conserved (TH-like) and Btk29A which is entirely unique with large numbers of glycine residues (TH-extended). Tec family members all lack a C-terminal tyrosine having an autoinhibitory function in its phosphorylated state. Two tyrosine phosphorylation (pY) sites have been identified in Btk: one located in the activation loop of the catalytic domain which regulates the transition between open (active) and closed (inactive) states and the other in its SH3 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
DSLEMYEWYSKNMTRSQAEQLLKQEGKEGGFIVRDSSKAGKYTVSVFAKSAGDPQGVIRHYVVCSTPQSQ
YYLAEKHLFSTIPELINYHQHNAAGLISRLKYPVSS
>gnl|CDD|198261 cd10398, SH2_Tec_Txk, Src homology 2 (SH2) domain found in Tec protein, Txk. A member of the Tec protein tyrosine kinase Txk is expressed in thymus, spleen, lymph node, T lymphocytes, NK cells, mast cell lines, and myeloid cell line. Txk plays a role in TCR signal transduction, T cell development, and selection which is analogous to the function of Itk. Txk has been shown to interact with IFN-gamma. Unlike most of the Tec family members Txk lacks a PH domain. Instead Txk has a unique region containing a palmitoylated cysteine string which has a similar membrane tethering function as the PH domain. Txk also has a zinc-binding motif, a SH3 domain, a SH2 domain, and a protein kinase catalytic domain. The TH domain consists of a Zn2+-binding Btk motif and a proline-rich region. The Btk motif is found in Tec kinases, Ras GAP, and IGBP and crucial to the function of the PH domain. It is not present in Txk which is not surprising since it lacks a PH domain. The type 1 splice form of the Drosophila homolog also lacks both the PH domain and the Btk motif. The proline-rich regions are highly conserved for the most part with the exception of Bmx whose residues surrounding the PXXP motif are not conserved (TH-like) and Btk29A which is entirely unique with large numbers of glycine residues (TH-extended). Tec family members all lack a C-terminal tyrosine having an autoinhibitory function in its phosphorylated state. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
TNLEIYEWYHKNITRNQAERLLRQESKEGAFIVRDSRHLGSYTISVFTRARRSTEASIKHYQIKKNDSGQ
WYVAERHLFQSIPELIQYHQHNAAGLMSRLRYPVGL
>gnl|CDD|198262 cd10399, SH2_Tec_Bmx, Src homology 2 (SH2) domain found in Tec protein, Bmx. A member of the Tec protein tyrosine kinase Bmx is expressed in the endothelium of large arteries, fetal endocardium, adult endocardium of the left ventricle, bone marrow, lung, testis, granulocytes, myeloid cell lines, and prostate cell lines. Bmx is involved in the regulation of Rho and serum response factor (SRF). Bmx has been shown to interact with PAK1, PTK2, PTPN21, and RUFY1. Most of the Tec family members have a PH domain (Txk and the short (type 1) splice variant of Drosophila Btk29A are exceptions), a Tec homology (TH) domain, a SH3 domain, a SH2 domain, and a protein kinase catalytic domain. The TH domain consists of a Zn2+-binding Btk motif and a proline-rich region. The Btk motif is found in Tec kinases, Ras GAP, and IGBP. It is crucial for the function of Tec PH domains. It is not present in Txk and the type 1 splice form of the Drosophila homolog. The proline-rich regions are highly conserved for the most part with the exception of Bmx whose residues surrounding the PXXP motif are not conserved (TH-like) and Btk29A which is entirely unique with large numbers of glycine residues (TH-extended). Tec family members all lack a C-terminal tyrosine having an autoinhibitory function in its phosphorylated state. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
ENLDAYDWFAGNISRSQSEQLLRQKGKEGAFMVRNSSQVGMYTVSLFSKAVNDKKGTVKHYHVHTNAENK
LYLAENYCFDSIPKLIHYHQHNSAGMITRLRHPVST
>gnl|CDD|198263 cd10400, SH2_SAP1a, Src homology 2 (SH2) domain found in SLAM-associated protein (SAP) 1a. The X-linked lymphoproliferative syndrome (XLP) gene encodes SAP (also called SH2D1A/DSHP) a protein that consists of a 5 residue N-terminus, a single SH2 domain, and a short 25 residue C-terminal tail. XLP is characterized by an extreme sensitivity to Epstein-Barr virus. Both T and natural killer (NK) cell dysfunctions have been seen in XLP patients. SAP binds the cytoplasmic tail of Signaling lymphocytic activation molecule (SLAM), 2B4, Ly-9, and CD84. SAP is believed to function as a signaling inhibitor, by blocking or regulating binding of other signaling proteins. SAP and the SAP-like protein EAT-2 recognize the sequence motif TIpYXX[VI], which is found in the cytoplasmic domains of a restricted number of T, B, and NK cell surface receptors and are proposed to be natural inhibitors or regulators of the physiological role of a small family of receptors on the surface of these cells. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
EAVAVYHGKISRETGEKLLLAAGLDGSYLLRDSESVPGVYCLCVLYKGYVYTYRVSQTETGSWSAETAPG
VHKRLFRKVKNLISAFQKPDQGIVTPLQYPVEK
>gnl|CDD|198264 cd10401, SH2_C-SH2_Syk_like, C-terminal Src homology 2 (SH2) domain found in Spleen tyrosine kinase (Syk) proteins. ZAP-70 and Syk comprise a family of hematopoietic cell specific protein tyrosine kinases (PTKs) that are required for antigen and antibody receptor function. ZAP-70 is expressed in T and natural killer (NK) cells and Syk is expressed in B cells, mast cells, polymorphonuclear leukocytes, platelets, macrophages, and immature T cells. They are required for the proper development of T and B cells, immune receptors, and activating NK cells. They consist of two N-terminal Src homology 2 (SH2) domains and a C-terminal kinase domain separated from the SH2 domains by a linker or hinge region. Phosphorylation of both tyrosine residues within the Immunoreceptor Tyrosine-based Activation Motifs (ITAM; consensus sequence Yxx[LI]x(7,8)Yxx[LI]) by the Src-family PTKs is required for efficient interaction of ZAP-70 and Syk with the receptor subunits and for receptor function. ZAP-70 forms two phosphotyrosine binding pockets, one of which is shared by both SH2 domains. In Syk the two SH2 domains do not form such a phosphotyrosine-binding site. The SH2 domains here are believed to function independently. In addition, the two SH2 domains of Syk display flexibility in their relative orientation, allowing Syk to accommodate a greater variety of spacing sequences between the ITAM phosphotyrosines and singly phosphorylated non-classical ITAM ligands. This model contains the C-terminus SH2 domains of Syk. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
EKMPWFHGKISREESEQILLIGSKTNGKFLIRERDNNGSYALCLLHDGKVLHYRIDKDKTGKLSIPDGKK
FDTLWQLVEHYSYKPDGLLRVLTEPCPRI
>gnl|CDD|198265 cd10402, SH2_C-SH2_Zap70, C-terminal Src homology 2 (SH2) domain found in Zeta-chain-associated protein kinase 70 (ZAP-70). ZAP-70 and Syk comprise a family of hematopoietic cell specific protein tyrosine kinases (PTKs) that are required for antigen and antibody receptor function. ZAP-70 is expressed in T and natural killer (NK) cells and Syk is expressed in B cells, mast cells, polymorphonuclear leukocytes, platelets, macrophages, and immature T cells. They are required for the proper development of T and B cells, immune receptors, and activating NK cells. They consist of two N-terminal Src homology 2 (SH2) domains and a C-terminal kinase domain separated from the SH2 domains by a linker or hinge region. Phosphorylation of both tyrosine residues within the Immunoreceptor Tyrosine-based Activation Motifs (ITAM; consensus sequence Yxx[LI]x(7,8)Yxx[LI]) by the Src-family PTKs is required for efficient interaction of ZAP-70 and Syk with the receptor subunits and for receptor function. ZAP-70 forms two phosphotyrosine binding pockets, one of which is shared by both SH2 domains. In Syk the two SH2 domains do not form such a phosphotyrosine-binding site. The SH2 domains here are believed to function independently. In addition, the two SH2 domains of Syk display flexibility in their relative orientation, allowing Syk to accommodate a greater variety of spacing sequences between the ITAM phosphotyrosines and singly phosphorylated non-classical ITAM ligands. This model contains the C-terminus SH2 domains of Zap70. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
LIATTAHERMPWYHGSIARDEAERRLYSGAQPDGKFLLRERKESGTYALSLVYGKTVYHYRIDQDKSGKY
SIPEGTKFDTLWQLVEYLKLKPDGLIFVLRESCPN
>gnl|CDD|198266 cd10403, SH2_STAP1, Src homology 2 domain found in Signal-transducing adaptor protein 1 (STAP1). STAP1 is a signal-transducing adaptor protein. It is composed of a Pleckstrin homology (PH) and SH2 domains along with several tyrosine phosphorylation sites. STAP-1 is an ortholog of BRDG1 (BCR downstream signaling 1). STAP1 protein functions as a docking protein acting downstream of Tec tyrosine kinase in B cell antigen receptor signaling. The protein is phosphorylated by Tec and participates in a positive feedback loop, increasing Tec activity. STAP1 has been shown to interact with C19orf2, an unconventional prefoldin RPB5 interactor. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
PACFYKVSRKEAEELLERNPSCGNMLLRPGSDSSNYSITTRQEINKPRIKHYRVMSRGQGYTIELEKPVT
CPTLHDVINYFVEKTRGNLRPFIM
>gnl|CDD|198267 cd10404, SH2_STAP2, Src homology 2 domain found in Signal-transducing adaptor protein 2 (STAP2). STAP2 is a signal-transducing adaptor protein. It is composed of a Pleckstrin homology (PH) and SH2 domains along with several tyrosine phosphorylation sites. The STAP2 protein is the substrate of breast tumor kinase, an Src-type non-receptor tyrosine kinase that mediates the interactions linking proteins involved in signal transduction pathways. STAP2 has alternative splicing variants. STAP2 has been shown to interact with tyrosine-protein kinase 6 (PTK6). In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
PSCFLKVSRLEAQLLLERYPECGNLLLRPGGDGADGVSVTTRQMLNGTPVVRHYKVKREGPKYVIDVEEP
FSCTSLDAVVNYFVSHTKKALVPFLLD
>gnl|CDD|198268 cd10405, SH2_Vav1, Src homology 2 (SH2) domain found in the Vav1 proteins. Proto-oncogene vav is a member of the Dbl family of guanine nucleotide exchange factors (GEF) for the Rho family of GTP binding proteins. All vavs are activated by tyrosine phosphorylation leading to their activation. There are three Vav mammalian family members: Vav1 which is expressed in the hematopoietic system, and Vav2 and Vav3 are more ubiquitously expressed. Vav1 plays a role in T-cell and B-cell development and activation. It has been identified as the specific binding partner of Nef proteins from HIV-1, resulting in morphological changes, cytoskeletal rearrangements, and the JNK/SAPK signaling cascade, leading to increased levels of viral transcription and replication. Vav1 has been shown to interact with Ku70, PLCG1, Lymphocyte cytosolic protein 2, Janus kinase 2, SIAH2, S100B, Abl gene, ARHGDIB, SHB, PIK3R1, PRKCQ, Grb2, MAPK1, Syk, Linker of activated T cells, Cbl gene and EZH2. Vav proteins are involved in several processes that require cytoskeletal reorganization, such as the formation of the immunological synapse (IS), phagocytosis, platelet aggregation, spreading, and transformation. Vavs function as guanine nucleotide exchange factors (GEFs) for the Rho/Rac family of GTPases. Vav family members have several conserved motifs/domains including: a leucine-rich region, a leucine-zipper, a calponin homology (CH) domain, an acidic domain, a Dbl-homology (DH) domain, a pleckstrin homology (PH) domain, a cysteine-rich domain, 2 SH3 domains, a proline-rich region, and a SH2 domain. Vavs are the only known Rho GEFs that have both the DH/PH motifs and SH2/SH3 domains in the same protein. The leucine-rich helix-loop-helix (HLH) domain is thought to be involved in protein heterodimerization with other HLH proteins and it may function as a negative regulator by forming inactive heterodimers. The CH domain is usually involved in the association with filamentous actin, but in Vav it controls NFAT stimulation, Ca2+ mobilization, and its transforming activity. Acidic domains are involved in protein-protein interactions and contain regulatory tyrosines. The DH domain is a GDP-GTP exchange factor on Rho/Rac GTPases. The PH domain in involved in interactions with GTP-binding proteins, lipids and/or phosphorylated serine/threonine residues. The SH3 domain is involved in localization of proteins to specific sites within the cell interacting with protein with proline-rich sequences. The SH2 domain mediates a high affinity interaction with tyrosine phosphorylated proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
DLSVHLWYAGPMERAGAESILANRSDGTYLVRQRVKDAAEFAISIKYNVEVKHIKIMTAEGLYRITEKKA
FRGLTELVEFYQQNSLKDCFKSLDTTLQFPFKE
>gnl|CDD|198269 cd10406, SH2_Vav2, Src homology 2 (SH2) domain found in the Vav2 proteins. Proto-oncogene vav is a member of the Dbl family of guanine nucleotide exchange factors (GEF) for the Rho family of GTP binding proteins. All vavs are activated by tyrosine phosphorylation leading to their activation. There are three Vav mammalian family members: Vav1 which is expressed in the hematopoietic system, and Vav2 and Vav3 are more ubiquitously expressed. Vav2 is a GEF for RhoA, RhoB and RhoG and may activate Rac1 and Cdc42. Vav2 has been shown to interact with CD19 and Grb2. Alternatively spliced transcript variants encoding different isoforms have been found for Vav2. Vav proteins are involved in several processes that require cytoskeletal reorganization, such as the formation of the immunological synapse (IS), phagocytosis, platelet aggregation, spreading, and transformation. Vavs function as guanine nucleotide exchange factors (GEFs) for the Rho/Rac family of GTPases. Vav family members have several conserved motifs/domains including: a leucine-rich region, a leucine-zipper, a calponin homology (CH) domain, an acidic domain, a Dbl-homology (DH) domain, a pleckstrin homology (PH) domain, a cysteine-rich domain, 2 SH3 domains, a proline-rich region, and a SH2 domain. Vavs are the only known Rho GEFs that have both the DH/PH motifs and SH2/SH3 domains in the same protein. The leucine-rich helix-loop-helix (HLH) domain is thought to be involved in protein heterodimerization with other HLH proteins and it may function as a negative regulator by forming inactive heterodimers. The CH domain is usually involved in the association with filamentous actin, but in Vav it controls NFAT stimulation, Ca2+ mobilization, and its transforming activity. Acidic domains are involved in protein-protein interactions and contain regulatory tyrosines. The DH domain is a GDP-GTP exchange factor on Rho/Rac GTPases. The PH domain in involved in interactions with GTP-binding proteins, lipids and/or phosphorylated serine/threonine residues. The SH3 domain is involved in localization of proteins to specific sites within the cell interacting with protein with proline-rich sequences. The SH2 domain mediates a high affinity interaction with tyrosine phosphorylated proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
DYTAYPWFAGNMERQQTDNLLKSHASGTYLIRERPAEAERFAISIKFNDEVKHIKVVEKDNWIHITEAKK
FESLLELVEYYQCHSLKESFKQLDTTLKYPYKS
>gnl|CDD|198270 cd10407, SH2_Vav3, Src homology 2 (SH2) domain found in the Vav3 proteins. Proto-oncogene vav is a member of the Dbl family of guanine nucleotide exchange factors (GEF) for the Rho family of GTP binding proteins. All vavs are activated by tyrosine phosphorylation leading to their activation. There are three Vav mammalian family members: Vav1 which is expressed in the hematopoietic system, and Vav2 and Vav3 are more ubiquitously expressed. Vav3 preferentially activates RhoA, RhoG and, to a lesser extent, Rac1. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. VAV3 has been shown to interact with Grb2. Vav proteins are involved in several processes that require cytoskeletal reorganization, such as the formation of the immunological synapse (IS), phagocytosis, platelet aggregation, spreading, and transformation. Vavs function as guanine nucleotide exchange factors (GEFs) for the Rho/Rac family of GTPases. Vav family members have several conserved motifs/domains including: a leucine-rich region, a leucine-zipper, a calponin homology (CH) domain, an acidic domain, a Dbl-homology (DH) domain, a pleckstrin homology (PH) domain, a cysteine-rich domain, 2 SH3 domains, a proline-rich region, and a SH2 domain. Vavs are the only known Rho GEFs that have both the DH/PH motifs and SH2/SH3 domains in the same protein. The leucine-rich helix-loop-helix (HLH) domain is thought to be involved in protein heterodimerization with other HLH proteins and it may function as a negative regulator by forming inactive heterodimers. The CH domain is usually involved in the association with filamentous actin, but in Vav it controls NFAT stimulation, Ca2+ mobilization, and its transforming activity. Acidic domains are involved in protein-protein interactions and contain regulatory tyrosines. The DH domain is a GDP-GTP exchange factor on Rho/Rac GTPases. The PH domain in involved in interactions with GTP-binding proteins, lipids and/or phosphorylated serine/threonine residues. The SH3 domain is involved in localization of proteins to specific sites within the cell interacting with protein with proline-rich sequences. The SH2 domain mediates a high affinity interaction with tyrosine phosphorylated proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
DYSCQPWYAGAMERLQAETELINRVNSTYLVRHRTKESGEYAISIKYNNEVKHIKILTRDGFFHIAENRK
FKSLMELVEYYKHHSLKEGFRSLDTTLQFPYKE
>gnl|CDD|198271 cd10408, SH2_Nck1, Src homology 2 (SH2) domain found in Nck. Nck proteins are adaptors that modulate actin cytoskeleton dynamics by linking proline-rich effector molecules to tyrosine kinases or phosphorylated signaling intermediates. There are two members known in this family: Nck1 (Nckalpha) and Nck2 (Nckbeta and Growth factor receptor-bound protein 4 (Grb4)). They are characterized by having 3 SH3 domains and a C-terminal SH2 domain. Nck1 and Nck2 have overlapping functions as determined by gene knockouts. Both bind receptor tyrosine kinases and other tyrosine-phosphorylated proteins through their SH2 domains. In addition they also bind distinct targets. Neuronal signaling proteins: EphrinB1, EphrinB2, and Disabled-1 (Dab-1) all bind to Nck-2 exclusively. And in the case of PDGFR, Tyr(P)751 binds to Nck1 while Tyr(P)1009 binds to Nck2. Nck1 and Nck2 have a role in the infection process of enteropathogenic Escherichia coli (EPEC). Their SH3 domains are involved in recruiting and activating the N-WASP/Arp2/3 complex inducing actin polymerization resulting in the production of pedestals, dynamic bacteria-presenting protrusions of the plasma membrane. A similar thing occurs in the vaccinia virus where motile plasma membrane projections are formed beneath the virus. Recently it has been shown that the SH2 domains of both Nck1 and Nck2 bind the G-protein coupled receptor kinase-interacting protein 1 (GIT1) in a phosphorylation-dependent manner. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
NPWYYGKVTRHQAEMALNERGNEGDFLIRDSESSPNDFSVSLKAQGKNKHFKVQLKECVYCIGQRKFSSM
EELVEHYKKAPIFTSEQGEKLYLIKAL
>gnl|CDD|198272 cd10409, SH2_Nck2, Src homology 2 (SH2) domain found in Nck. Nck proteins are adaptors that modulate actin cytoskeleton dynamics by linking proline-rich effector molecules to tyrosine kinases or phosphorylated signaling intermediates. There are two members known in this family: Nck1 (Nckalpha) and Nck2 (Nckbeta and Growth factor receptor-bound protein 4 (Grb4)). They are characterized by having 3 SH3 domains and a C-terminal SH2 domain. Nck1 and Nck2 have overlapping functions as determined by gene knockouts. Both bind receptor tyrosine kinases and other tyrosine-phosphorylated proteins through their SH2 domains. In addition they also bind distinct targets. Neuronal signaling proteins: EphrinB1, EphrinB2, and Disabled-1 (Dab-1) all bind to Nck-2 exclusively. And in the case of PDGFR, Tyr(P)751 binds to Nck1 while Tyr(P)1009 binds to Nck2. Nck1 and Nck2 have a role in the infection process of enteropathogenic Escherichia coli (EPEC). Their SH3 domains are involved in recruiting and activating the N-WASP/Arp2/3 complex inducing actin polymerization resulting in the production of pedestals, dynamic bacteria-presenting protrusions of the plasma membrane. A similar thing occurs in the vaccinia virus where motile plasma membrane projections are formed beneath the virus. Recently it has been shown that the SH2 domains of both Nck1 and Nck2 bind the G-protein coupled receptor kinase-interacting protein 1 (GIT1) in a phosphorylation-dependent manner. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
KEWYYGNVTRHQAECALNERGVEGDFLIRDSESSPSDFSVSLKAVGKNKHFKVQLVDNVYCIGQRRFNSM
DELVEHYKKAPIFTSEHGEKLYLVKALQ
>gnl|CDD|198273 cd10410, SH2_SH2B1, Src homology 2 (SH2) domain found in SH2B adapter proteins (SH2B1, SH2B2, SH2B3). SH2B1 (SH2-B, PSM), like other members of the SH2B adapter protein family, contains a pleckstrin homology domain, at least one dimerization domain, and a C-terminal SH2 domain which binds to phosphorylated tyrosines in a variety of tyrosine kinases. SH2B1 and SH2B2 function in signaling pathways found downstream of growth hormone receptor and receptor tyrosine kinases, including the insulin, insulin-like growth factor-I (IGF-I), platelet-derived growth factor (PDGF), nerve growth factor, hepatocyte growth factor, and fibroblast growth factor receptors. SH2B2beta, a new isoform of SH2B2, is an endogenous inhibitor of SH2B1 and/or SH2B2 (SH2B2alpha), negatively regulating insulin signaling and/or JAK2-mediated cellular responses. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
GDQPLSGYPWFHGMLSRLKAAQLVLEGGTGSHGVFLVRQSETRRGEYVLTFNFQGKAKHLRLSLNEEGQC
RVQHLWFQSIFDMLEHFRVHPIPLESG
>gnl|CDD|198274 cd10411, SH2_SH2B2, Src homology 2 (SH2) domain found in SH2B adapter proteins (SH2B1, SH2B2, SH2B3). SH2B2 (APS), like other members of the SH2B adapter protein family, contains a pleckstrin homology domain, at least one dimerization domain, and a C-terminal SH2 domain which binds to phosphorylated tyrosines in a variety of tyrosine kinases. SH2B1 and SH2B2 function in signaling pathways found downstream of growth hormone receptor and receptor tyrosine kinases, including the insulin, insulin-like growth factor-I (IGF-I), platelet-derived growth factor (PDGF), nerve growth factor, hepatocyte growth factor, and fibroblast growth factor receptors. SH2B2beta, a new isoform of SH2B2, is an endogenous inhibitor of SH2B1 and/or SH2B2 (SH2B2alpha), negatively regulating insulin signaling and/or JAK2-mediated cellular responses. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
AELELSDYPWFHGTLSRVKAAQLVLAGGPRSHGLFVIRQSETRPGEYVLTFNFQGKAKHLRLSLNGHGQC
HVQHLWFQSVFDMLRHFHTHPIPLESG
>gnl|CDD|198275 cd10412, SH2_SH2B3, Src homology 2 (SH2) domain found in SH2B adapter proteins (SH2B1, SH2B2, SH2B3). SH2B3 (Lnk), like other members of the SH2B adapter protein family, contains a pleckstrin homology domain, at least one dimerization domain, and a C-terminal SH2 domain which binds to phosphorylated tyrosines in a variety of tyrosine kinases. SH2B3 negatively regulates lymphopoiesis and early hematopoiesis. The lnk-deficiency results in enhanced production of B cells, and expansion as well as enhanced function of hematopoietic stem cells (HSCs), demonstrating negative regulatory functions of Sh2b3/Lnk in cytokine signaling. Sh2b3/Lnk also functions in responses controlled by cell adhesion and in crosstalk between integrin- and cytokine-mediated signaling. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
TDHFLSCYPWFHGPISRVKAAQLVQLQGPDAHGVFLVRQSETRRGEYVLTFNFQGRAKHLRLSLTERGQC
RVQHLHFPSVVDMLHHFQRSPIPLECG
>gnl|CDD|198276 cd10413, SH2_Grb7, Src homology 2 (SH2) domain found in the growth factor receptor bound, subclass 7 (Grb7) proteins. The Grb family binds to the epidermal growth factor receptor (EGFR, erbB1) via their SH2 domains. Grb7 is part of the Grb7 family of proteins which also includes Grb10, and Grb14. They are composed of an N-terminal Proline-rich domain, a Ras Associating-like (RA) domain, a Pleckstrin Homology (PH) domain, a phosphotyrosine interaction region (PIR, BPS) and a C-terminal SH2 domain. The SH2 domains of Grb7, Grb10 and Grb14 preferentially bind to a different RTK. Grb7 binds strongly to the erbB2 receptor, unlike Grb10 and Grb14 which bind weakly to it. Grb7 family proteins are phosphorylated on serine/threonine as well as tyrosine residues. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
IHRTQPWFHGRISREESQRLIGQQGLVDGVFLVRESQRNPQGFVLSLCHLQKVKHYLILPSEEEGRLYFS
MDDGQTRFTDLLQLVEFHQLNRGILPCLLRHCCTRVAL
>gnl|CDD|198277 cd10414, SH2_Grb14, Src homology 2 (SH2) domain found in the growth factor receptor bound, subclass 14 (Grb14) proteins. The Grb family binds to the epidermal growth factor receptor (EGFR, erbB1) via their SH2 domains. Grb14 is part of the Grb7 family of proteins which also includes Grb7, and Grb14. They are composed of an N-terminal Proline-rich domain, a Ras Associating-like (RA) domain, a Pleckstrin Homology (PH) domain, a phosphotyrosine interaction region (PIR, BPS) and a C-terminal SH2 domain. The SH2 domains of Grb7, Grb10 and Grb14 preferentially bind to a different RTK. Grb14 binds to Fibroblast Growth Factor Receptor (FGFR) and weakly to the erbB2 receptor. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
IHRSQPWFHHKISRDEAQRLIIQQGLVDGVFLVRDSQSNPRTFVLSMSHGQKIKHFQIIPVEDDGELFHT
LDDGHTRFTDLIQLVEFYQLNKGVLPCKLKHYCARIAL
>gnl|CDD|198278 cd10415, SH2_Grb10, Src homology 2 (SH2) domain found in the growth factor receptor bound, subclass 10 (Grb10) proteins. The Grb family binds to the epidermal growth factor receptor (EGFR, erbB1) via their SH2 domains. Grb10 is part of the Grb7 family of proteins which also includes Grb7, and Grb14. They are composed of an N-terminal Proline-rich domain, a Ras Associating-like (RA) domain, a Pleckstrin Homology (PH) domain, a phosphotyrosine interaction region (PIR, BPS) and a C-terminal SH2 domain. The SH2 domains of Grb7, Grb10 and Grb14 preferentially bind to a different RTK. Grb10 has been shown to interact with many different proteins, including the insulin and IGF1 receptors, platelet-derived growth factor (PDGF) receptor-beta, Ret, Kit, Raf1 and MEK1, and Nedd4. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
IHRTQHWFHGRISREESHRIIKQQGLVDGLFLLRDSQSNPKAFVLTLCHHQKIKNFQILPCEDDGQTFFS
LDDGNTKFSDLIQLVDFYQLNKGVLPCKLKHHCIRVAL
>gnl|CDD|198279 cd10416, SH2_SH2D2A, Src homology 2 domain found in the SH2 domain containing protein 2A (SH2D2A). SH2D2A contains a single SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
LQHGAAPAWFHGFITRREAERLLEPKPQGCYLVRFSESAVTFVLTYRSRTCCRHFLLAQLRDGRHVVLGE
DSAHARLQDLLLHYTAHPLSPYGETLTEPLAR
>gnl|CDD|199832 cd10417, SH2_SH2D7, Src homology 2 domain found in the SH2 domain containing protein 7 (SH2D7). SH2D7 contains a single SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
LQNGALPPWFHGFITRKQTEQLLRDKALGSFLIRLSDRATGYILSYRGSDRCRHFVINQLRNRRYLISGD
TSSHSTLAELVRHYQEVQLEPFGETLTAACPR
>gnl|CDD|198281 cd10418, SH2_Src_Fyn_isoform_a_like, Src homology 2 (SH2) domain found in Fyn isoform a like proteins. Fyn is a member of the Src non-receptor type tyrosine kinase family of proteins. This cd contains the SH2 domain found in Fyn isoform a type proteins. Fyn is involved in the control of cell growth and is required in the following pathways: T and B cell receptor signaling, integrin-mediated signaling, growth factor and cytokine receptor signaling, platelet activation, ion channel function, cell adhesion, axon guidance, fertilization, entry into mitosis, and differentiation of natural killer cells, oligodendrocytes and keratinocytes. The protein associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the Fyn-binding protein. Alternatively spliced transcript variants encoding distinct isoforms exist. Fyn is primarily localized to the cytoplasmic leaflet of the plasma membrane. Tyrosine phosphorylation of target proteins by Fyn serves to either regulate target protein activity, and/or to generate a binding site on the target protein that recruits other signaling molecules. FYN has been shown to interact with a number of proteins including: BCAR1, Cbl, Janus kinase, nephrin, Sky, tyrosine kinase, Wiskott-Aldrich syndrome protein, and Zap-70. Fyn has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYY
ITTRAQFETLQQLVQHYSERAAGLCCRLVVP
>gnl|CDD|198282 cd10419, SH2_Src_Fyn_isoform_b_like, Src homology 2 (SH2) domain found in Fyn isoform b like proteins. Fyn is a member of the Src non-receptor type tyrosine kinase family of proteins. This cd contains the SH2 domain found in Fyn isoform b type proteins. Fyn is involved in the control of cell growth and is required in the following pathways: T and B cell receptor signaling, integrin-mediated signaling, growth factor and cytokine receptor signaling, platelet activation, ion channel function, cell adhesion, axon guidance, fertilization, entry into mitosis, and differentiation of natural killer cells, oligodendrocytes and keratinocytes. The protein associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the Fyn-binding protein. Alternatively spliced transcript variants encoding distinct isoforms exist. Fyn is primarily localized to the cytoplasmic leaflet of the plasma membrane. Tyrosine phosphorylation of target proteins by Fyn serves to either regulate target protein activity, and/or to generate a binding site on the target protein that recruits other signaling molecules. FYN has been shown to interact with a number of proteins including: BCAR1, Cbl, Janus kinase, nephrin, Sky, tyrosine kinase, Wiskott-Aldrich syndrome protein, and Zap-70. Fyn has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
QAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYY
ITTRAQFETLQQLVQHYSEKADGLCFNLTVI
>gnl|CDD|198283 cd10420, SH2_STAT5b, Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5b proteins. STAT5 is a member of the STAT family of transcription factors. Two highly related proteins, STAT5a and STAT5b are encoded by separate genes, but are 90% identical at the amino acid level. Both STAT5a and STAT5b are ubiquitously expressed and functionally interchangeable. Mice lacking either STAT5a or STAT5b have mild defects in prolactin dependent mammary differentiation or sexually dimorphic growth hormone-dependent effects, respectively. Mice lacking both STAT5a and STAT5b exhibit a perinatal lethal phenotype and have multiple defects, including anemia and a virtual absence of B and T lymphocytes. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
WFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSQERMFWN
LMPFTTRDFSIRSLADRLGDLNYLIYVFPDRPKDEVYSKYYTPVPCEPATAKAVDGYVKPQIKQVVPEFV
SASAD
>gnl|CDD|198284 cd10421, SH2_STAT5a, Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5a proteins. STAT5 is a member of the STAT family of transcription factors. Two highly related proteins, STAT5a and STAT5b are encoded by separate genes, but are 90% identical at the amino acid level. Both STAT5a and STAT5b are ubiquitously expressed and functionally interchangeable. Mice lacking either STAT5a or STAT5b have mild defects in prolactin dependent mammary differentiation or sexually dimorphic growth hormone-dependent effects, respectively. Mice lacking both STAT5a and STAT5b exhibit a perinatal lethal phenotype and have multiple defects, including anemia and a virtual absence of B and T lymphocytes. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPDRNLWN
LKPFTTRDFSIRSLADRLGDLNYLIYVFPDRPKDEVFSKYYTPVLAKAVDGYVKPQIKQVVPEFVSASAD
>gnl|CDD|199217 cd10422, RNase_Ire1, RNase domain (also known as the kinase extension nuclease domain) of Ire1. The model represents the C-terminal endoribonuclease domain of the multi-functional protein Ire1; Ire1 in addition contains a type I transmembrane serine/threonine protein kinase (STK) domain, and a Luminal dimerization domain. Ire1 is essential for the endoplasmic reticulum (ER) unfolded protein response (UPR), which acts as an ER stress sensor and is the oldest and most conserved component of the UPR in eukaryotes. During ER stress, IRE1 dimerizes through its N-terminal luminal domain and forms oligomers, promoting trans-autophosphorylation by its cytosolic kinase domain. This leads to a conformational change that stimulates its endoribonuclease (RNase) activity and results in the cleavage of its mRNA substrate, Hac1 in yeast and Xbp1 in metazoans, thus promoting a splicing event that enables translation into a transcription factor which activates the UPR. This RNase domain is homologous to the RNase domain of RNase L, and possesses a novel fold for a nuclease and appears to be rigid irrespective of the activation state of IRE1. Structural analysis and mutational studies have revealed that an early stage 'phosphoryl-transfer' competent conformation of IRE1 favors face-to-face dimerization of the kinase domains which precedes and is distinct from the RNase 'active' back-to-back conformation. Furthermore, in yeast IRE1, the flavonol quercetin activates the RNase and potentiates activation of the protein kinase by ADP, hinting at the possible existence of endogenous cytoplasmic ligands that may function along with stress signals from ER lumen in order to modulate IRE1 activity, thus identifying IRE1 as a target for development of ATP-competitive inhibitors to modulate the UPR with specific relevance for multiple myeloma
EKRLSFLQDVSDRFEKEPRDPPSPLLLALESGADEVVGGDWREKLDKTFIDNLGKYRKYKGSSVRDLLRA
LRNKKHHYRELPPDVQELLGPLPDGFLRYFTSRFPNLLIHVYRAVSDSLKNESTFKKYY
>gnl|CDD|199218 cd10423, RNase_RNase-L, RNase domain (also known as the kinase extension nuclease domain) of RNase L. Ribonuclease L (RNase L), sometimes referred to as the 2-5A-dependent RNase, is a highly regulated, latent endoribonuclease (thus the 'L' in RNase L) and is widely expressed in most mammalian tissues. It is involved in the mediation of the antiviral and pro-apoptotic activities of the interferon-inducible 2-5A system, which blocks infections by certain types of viruses through cleavage of viral and cellular single-stranded RNA. RNase L is unique in that it is composed of three major domains; N-terminus regulatory ankyrin repeat domain (ARD), followed by a linker, a protein kinase (PK)-like domain and a C-terminal ribonuclease (RNase) domain. The RNase domain has homology with IRE1, also containing both a kinase and an endoribonuclease, that functions in the unfolded protein response (UPR). RNase L has been shown to have an impact on the pathogenesis of prostate cancer; the RNase L gene, RNASEL, has been identified as a strong candidate for the hereditary prostate cancer 1 (HPC1) allele. The broad range of biological functions of RNase offers a possibility for RNase L as a therapeutic target
ENRYRTLRNVGNESDIKTRDDKSDILRLLQAGKSECSRSFPNWTSKIDKEVMDIMNKFYEKKKFFYQDTV
GDLLKFIRNLGEHIDEEKNKRMKEIIGDPSEYFQKTFPDLVIYVYKKLR
>gnl|CDD|198344 cd10424, GST_C_9, C-terminal, alpha helical domain of an unknown subfamily 9 of Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 9; composed of uncharacterized proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain
VRELTTELELYLELPARRLYPEAFFGGKVSPEIKEEVRKDLLRGIAALARLARFAPYVAGETFTLADCAA
FVHLPLVALATKKFYGEDFLADLPGAKAYLARL
>gnl|CDD|259896 cd10425, Ephrin-A_Ectodomain, Ectodomain of Ephrin A. Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrin As contain a highly conserved receptor binding ectodomain described by this model. Although ephrin As do not have a cytoplasmic tail (in contrast to ephrin Bs), they are still capable of downstream activation of Src family kinases and phosphoinositide-3-kinases, most likely involving coreceptors such as neurotrophin receptors
DRHAVYWNSSNNRFLRGDYTVQVQINDYLDILCPHYESSDPAGEEMERYILYMVSEEGYETCSHTDKGFK
RWECNRPFAPHGPIKFSEKFQRFTPFSLGFEFRPGHEYYYISKPIHNHRRSCLRLKVFVE
>gnl|CDD|259897 cd10426, Ephrin-B_Ectodomain, Ectodomain of Ephrin B. Ephrin Bs have several conserved tyrosine phosphorylation sites in their cytoplasmic PDZ-like domain, which are important for signal transduction. Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands and the five EphB receptors bind to three transmembrane ephrin-B ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrin Bs contain a highly conserved receptor binding ectodomain described in this model
VLEPIYWNSSNPKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKLYMVDKDQADRCSIKKDPNPL
LTCAKPDQDVRFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGTLEGLENQEGGVCQTRSMKILMKVG
>gnl|CDD|198410 cd10428, LFG_like, Proteins similar to and including lifeguard (LFG), a putative regulator of apoptosis. Lifeguard (LFG) inhibits Fas-mediated apoptosis and interacts with the death receptor FasR/CD95/Apo1. LFG has been shown to interact with Bax and is supposed to be integral to cellular membranes such as the ER. A close homolog, PP1201 or RECS1, appears located in the Golgi compartment and also interacts with the Fas receptor CD95/Apo1. PP1201 is expressed in response to shear stress
PFDDKTIRRAFIRKVYSILTIQLLVTVAVIALFTFHDPVKKFVRKNPWLYYVSYIVFFITYIALACCEGL
RRRFPWNLILLGIFTLAMSYMLGTIASFYDTKAVLIAVGITAVVCLGLTLFAFQTKYDFTSCGGVLFVLS
IVLLIFGIVAIFFYVKWLHIVYASLGALLFSLYLAVDTQLLMGGRKYELSPEEYIFAALNIYVDIVNIFL
YILQLIG
>gnl|CDD|198411 cd10429, GAAP_like, Golgi antiapoptotic protein. GAAP (or transmembrane BAX inhibitor motif containing 4) is a regulator of apoptosis that is related to the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. Human GAAP has been linked to the modulation of intracellular fluxes of Ca(2+), by suppressing influx from the extracellular medium and reducing release from intracellular stores. A viral homolog (vaccinia virus vGAAP) acts similar to its human counterpart in inhibiting apoptosis
GSRYAEADIPDDFKYGTNVASAEPEIRMAFLRKVYSILSVQLLATTAVSALFYLSPSIKTFVQSHPWLFL
ISLIGSLILLIALYWKRHSHPVNLILLSLFTLCEAYTVGLVVSFYDGKIVLQALILTLGVFVGLTAYTFQ
TKRDFSSFGALLFILLWALILLALIFQFFPYSPTFELVYAGLGALLFSGYIVYDTQLIMKRLSPDEYILA
AISLYLDIINLFLSILRILAAMN
>gnl|CDD|198412 cd10430, BI-1, BAX inhibitor (BI)-1. Mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. Their broad tissue distribution and high degree of conservation suggests an important regulatory role. In plants, BI-1 like proteins play a role in pathogen resistance
FNQISPSVQQHLKKVYLTLAVALLAAAVGAYVHMVINIGGLLTGLLSLGLSLWLAFTPSTGKNEPKRLGL
LLGFAFLTGASLGPLLDLVIAINPSIIVTAFLGTAVIFACFSLAALLAKRREYLYLGGLLSSALSILLLV
SLANIFGGSKFLFQAELYLGLLVFCGFVLFDTQMIIEKAENGDRDYIWHALDLFVDFVALFRRLLIILAK
KEK
>gnl|CDD|198413 cd10431, GHITM, Growth-hormone inducible transmembrane protein. GHITM appears to be ubiquitiously expressed in mammalian cells and expression has also been observed in various cancer cell lines. A cytoprotective function has been suggested. It is closely related to the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect
GRALLAGAAAVGLGALCYYGLGLSSEIGAIEKAVIWPQYVRDRIHSTYMYFGGSLGLTALAAVALSRSPA
LMRLMAAGPWLAIGATLAAMIGSGMLVRSYTYPENPGAKHLAWLGHSGVQGAVLAPLCFLGGPLLIRAAL
YTAGIVGGLSTVAACAPSEKFLYMGGPLAIGLGVVFASSLGSMFLPPTTALGAGLYSVSLYGGLVLFGGF
LLYDTQKIIKRAETHPLYGVRKYDPINASMSIYMDTINIFIRLVTILAGGGNRR
>gnl|CDD|198414 cd10432, BI-1-like_bacterial, Bacterial BAX inhibitor (BI)-1/YccA-like proteins. This family is comprised of bacterial relatives of the mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. In plants, BI-1 like proteins play a role in pathogen resistance. A characterized prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes
GLRSFMKKVYGLMAAGLLLTAVGAYVGASTPALLLIAGSPLMWVLLIAELALVFGLSFRINKMSVATALP
LFFAFAALTGLTLSPILLVYTGASIAQAFFTTAATFGGLSLYGYTTKKDLSFLGSFLFMGLIGLIIASLV
NIFLQSSALQFAISAIGVLIFSGLIAYDTQRIKRMYEAGGGESGYKDAIMGALSLYLDFINLFLFLLRLF
G
>gnl|CDD|198415 cd10433, YccA_like, YccA-like proteins. A prokaryotic member of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes
LSTNKVLRNTYMLLSMTLAFSALGAGVSMAGGSPIMGLLLTLVGAYGLLFLIEKTRNSAWGIVLVFAFTG
FMGYTLGPILNMYLALPNGGQIIMTALGGTAAIFFGLSAYALTTKKDFSFLGGFLFVGAIVLLLAAVANI
FLQIPALSLAISAAFVLFSSGFILYDTSRIIHGGETNYIMATVSLYVSIYNLFVSLLNLLGAFSG
>gnl|CDD|198381 cd10434, GIY-YIG_UvrC_Cho, Catalytic GIY-YIG domain of nucleotide excision repair endonucleases UvrC, Cho, and similar proteins. UvrC is essential for nucleotide excision repair (NER). The N-terminal catalytic GIY-YIG domain of UvrC (also known as Uri domain) is responsible for the 3' incision reaction and the C-terminal half of UvrC, consisting of an UvrB-binding domain (UvrBb), EndoV-like nuclease domain and a helix-hairpin-helix (HhH) DNA-binding domain, contains the residues involved in 5' incision. The N- and C-terminal regions are joined by a common Cys-rich domain containing four conserved Cys residues. Besides UvrC, protein Cho (UvrC homolog) serves as a second endonuclease in E. coli NER. Cho contains GIY-YIG motif followed by a Cys-rich region and shares sequence homology with the N-terminal half of UvrC. It is capable of incising the DNA at the 3' side of a lesion in the presence of the UvrA and UvrB proteins during NER. The C-terminal half of Cho is a unique uncharacterized domain, which is distinct from that of UvrC. Moreover, unlike UvrC, Cho does not require the UvrC-binding domain of UvrB for the 3' incision reaction, which might cause the shift in incision position and the difference in incision efficiencies between Cho and UvrC on different damaged substrates. Due to this, the range of NER in E. coli can be broadened by combining action of Cho and UvrC. This family also includes many uncharacterized epsilon proofreading subunits of DNA polymerase III, which have an additional N-terminal ExoIII domain and a 3'-5' exonuclease domain homolog, fused to an UvrC-like region or a Cho-like region. The UvrC-like region includes a GIY-YIG motif, followed by a Cys-rich region, and an UvrB-binding domain (UvrBb), but lacks the EndoV-like nuclease domain and the helix-hairpin-helix (HhH) DNA-binding domain. The Cho-like region consists of a GIY-YIG motif, followed by the Cys-rich region, and the unique uncharacterized domain presenting in the C-terminal half of Cho. Some family members may not carry the Cys-rich region. This family also includes a specific Cho-like protein from G. violaceus, which possesses only UvrBb domain at the C-terminus, but lacks the additional N-terminal ExoIII domain. The oother two remote homologs of UvrC, Bacillus-I and -II, are included in this family as well. Both of them contain a GIY-YIG domain, but no Cys-rich region. Moreover, the whole C-terminal region of Bacillus-I is replaces by an unknown domain, and Bacillus-II possesses another unknown N-terminal extension
LPDSPGVYLFKDADGEVLYVGKAKNLRKRVSSYFTGERHSPKTRRLVEEIRDIEYIVTDSELEALLLEAN
LIKKYKPRYNI
>gnl|CDD|198382 cd10435, GIY-YIG_RE_Eco29kI_like, Catalytic GIY-YIG domain of type II restriction endonucleases R.Eco29kI, R.Cfr42I, and similar proteins. This family corresponds to the catalytic GIY-YIG domain of a group of GGCGCC-specific type II restriction endonucleases R.Eco29kI, R.Cfr42I, and similar proteins. R.Eco29kI is encoded on plasmid pECO29 in the E. coli strain 29K. This enzyme recognizes the palindromic 5'-CCGC/GG-3' target and cuts between Cyt4 and Gua5 on each strand of the restriction site to generate 3'-staggered ends. R.Eco29kI forms a domain-swapped homodimeric catalytically active complex during DNA binding and cleavage. Each subunit contains one GIY-YIG catalytic motif. Restriction endonucleases R.Cfr42I is an isoschizomer of R.Eco29kI. Unlike R.Eco29kI, R.Cfr42I is functional as a homotetramer, binding and cleaving two cognate DNA molecules in a cooperative manner. Members in this family are single-domain proteins sharing sequence similarities with the catalytic domain of GIY-YIG endonucleases, such as homing endonuclease I-TevI. However, they utilize loop insertions and terminal extensions instead of the separate DNA-binding domain to interact with the target site 5'-CCGC/GG-3'. A divalent metal-ion cofactor is required for their catalysis, but not for substrate binding. This family also includes a hypothetical protein from Deinococcus radiodurans that corresponds to MraI, a type II restriction enzyme similar to GIY-YIG family of homing endonucleases. MraI is shown to be an isoschizomer of Eco29kI, Cfr42I recognizing the palindromic nucleotide sequence 5'-CCGC reduced GG-3'. The enzyme shows an absolute requirement of Mg2+, but is active in the absence of added 2-mercaptoethanol. MraI represents the first restriction enzyme from a bacterium whose DNA lacks modified methylated bases
GAGVYALYYTGPHPLYAPLAENNQQGFQTPIYVGKAVPAGARQGEGKKAEQGSALYKRLSEHRKSIAATS
NLDVADFYCRVLVVAPGWIPLAESVLISLFRPAWNSHVDGFGNHGPG
>gnl|CDD|198383 cd10436, GIY-YIG_EndoII_Hpy188I_like, Catalytic GIY-YIG domain of coliphage T4 non-specific endonuclease II, type II restriction endonuclease R.Hpy188I, and similar proteins. This family includes two different GIY-YIG enzymes, coliphage T4 non-specific endonuclease II (EndoII), and type II restriction endonuclease R.Hpy188I. They display high sequence similarity to each other, and both of them contain an extra N-terminal hairpin that lacks counterparts in other GIY-YIG enzymes. EndoII encoded by gene denA catalyzes the initial step in degradation of host DNA, which permits scavenging of host-derived nucleotides for phage DNA synthesis. R.Hpy188I recognizes the unique sequence, 5'-TCNGA-3', and cleaves the DNA between nucleotides N and G in its recognition sequence to generate a single nucleotide 3'-overhang. EndoII binds to two DNA substrates as an X-shaped tetrameric structure composed as a dimer of dimers. In contrast, two subunits of R.Hpy188I form a dimer to embrace one bound DNA. Divalent metal-ion cofactors are required for their catalytic events, but not for the substrates binding
NGVYAFVVDGEIVYIGETQDLRKRFNSYRGGISPRNGQTTNCRINKLILKALKKGKVVELYVKQPEELVI
TLGDPVNTAKGLEDELIEKIKPEWNSQ
>gnl|CDD|198384 cd10437, GIY-YIG_HE_I-TevI_like, N-terminal catalytic domain of GIY-YIG intron endonuclease I-TevI, I-BmoI, I-BanI, I-BthII and similar proteins. I-TevI is a site-specific GIY-YIG homing endonuclease encoded within the group I intron of the thymidylate synthase gene (td) from Escherichia coli phage T4. It functions as an endonuclease that catalyzes the first step in intron homing by generating a double-strand break in the intronless td allele within a sequence designated the homing site. I-TevI recognizes its extensive 37 base pair DNA target in a site-specific, but sequence-tolerant manner. The cleavage site is located at 23 (upper strand) and 25 (lower strand) nucleotides upstream of the intron insertion site. A divalent cation, such as Mg2+, is required for the catalysis. I-TevI also acts as a repressor of its own transcription. It binds an operator that is located upstream of the I-TevI coding sequence and overlaps the T4 late promoter, which drives I-TevI expression from within the td intron. I-TevI binds the homing sites and the operator with the same affinity, but cleaves the homing site more efficiently than the operator. I-TevI consists of an N-terminal catalytic domain, containing the GIY-YIG motif, and a C-terminal DNA-binding domain that binds DNA as a monomer, joined by a flexible linker. The C-terminal domain includes three subdomains: a zinc finger, a minor-groove binding alpha-helix (NUMOD3, nuclease-associated modular domain 3), and a helix-turn-helix domain (HTH). The last two are responsible for DNA-binding. The zinc finger is part of the linker and not required for DNA-binding. It is implicated as a distance sensor to constrain the catalytic domain to cleave the homing site at a fixed position. None of other GIY-YIG endonucleases have been found to have the zinc finger motif. This family also includes a reduced activity isoschizomer of I-TevI, I-BmoI, which is encoded within the group I intron of the thymidylate synthase (TS) gene (thyA) from Bacillus mojavensis. I-BmoI catalyzes the first step in intron homing by generating a double-strand break in the intronless td allele within a sequence designated the homing site in the presence of a divalent cation cofactor, such as Mg2+. In the absence of Mg2+, I-Bmol only nicks one of the strands. Both I-BmoI and I-TevI bind a homologous stretch of TS-encoding DNA as monomers, but use different strategies to distinguish intronless from intron-containing substrates. I-TevI recognizes substrates at the level of DNA-binding. However, I-BmoI binds both intron-containing and intronless TS-encoding substrates, but efficiently cleaves only intronless substrate. Afterwards they cleave their respective intronless substrates in the same positions, and both require a critical G-C base pair adjacent to the top strand site for efficient cleavage. The C-terminal domain of I-BmoI has nuclease-associated modular DNA-binding domains (NUMODs), but lacks the zinc finger, which is different from that of I-TevI. Although the zinc finger implicated as a distance determination in I-TevI is absent, I-BmoI still possesses some cleavage distance discrimination. Besides I-TevI and I-BmoI, this family contains a putative GIY-YIG homing endonuclease, I-BanI, encoded within the self-splicing group I intron of nrdE gene from Bacillus anthracis. It contains two major domains, the N-terminal GIY-YIG domain and the C-terminal DNA-binding domain that consists of a minor-groove DNA binding alpha-helix motif and a helix-turn-helix (HTH) motif. I-BanI generates a double-strand break (DSB) in the intronless nrdE gene. The cleavage site is located at 5 and 7 nucleotides upstream of the intron insertion site, with 2-nucleotide 3' extensions. The recognition site is 35 to 40 base pairs and covers the cleavage site with a bias toward the downstream region including the (intervening sequence) IVS insertion site. Moreover, this family contains another putative GIY-YIG homing endonuclease, I-BthII, encoded within the self-splicing group I intron of nrdF gene from Bacillus thuringiensis ssp. pakistani. It contains a GIY-YIG motif that generates a double-strand break (DSB) in the intronless nrdF gene. The cleavage site is located at 7 and 9 nucleotides upstream of the intron insertion site, leaving 2-nucleotide 3' extensions. The recognition site is 27 to 29 base pairs with the DSB cleavage site at the 5'-end of the top strand, and with the intervening sequence (IVS) insertion site approximately in the middle of the recognition site
SGIYKITNLENGKIYIGSSKNILKRLSQHKRDLKAGKHHNKKLQRDFNKYGEENFEFTILEEGEEIEKLL
ELEQEYIDKYKSEKGYNIEP
>gnl|CDD|198385 cd10438, GIY-YIG_MSH, Catalytic GIY-YIG domain of eukaryotic DNA mismatch repair protein MutS homologs. This family represents a putative GIY-YIG nuclease domain C-terminally fused to the DNA-repair ATPase on a small group of eukaryotic DNA mismatch repair protein mutS homologs (MSH). The MSH proteins in this family do not have the zinc finger domain, but have a predicted mitochondrial localization. They might play roles in the recognition and repair of errors made during the replication of DNA. The prototype of this family is the protein encoded by the chloroplast mutator (CHM) locus from Arabidopsis thaliana. It is suggested that this protein could be involved in the maintenance of mitochondrial genome stability
SCVYILRRGDGEYYVGETDNLSGRLEQHRASLGETLVISGFLYLLVGGKSEARSLESALIQQLQGQGANL
AS
>gnl|CDD|198386 cd10439, GIY-YIG_COG3410, GIY-YIG domain of uncharacterized bacterial protein structurally related to COG3410. This family contains a group of uncharacterized bacterial proteins. Although their function roles have not been recognized, these proteins contain a putative GIY-YIG domain in their N-terminus. Moreover, a conserved domain COG3410 with unknown function has been found in the C-terminus of most family members
NYPVVYILYDKKKKKVYIGETNNILRRLKQHLKDPEKKFLRDLNQVIVIGHELFNKSATLDIENRLINYF
SADEVFKVLN
>gnl|CDD|198387 cd10440, GIY-YIG_COG3680, GIY-YIG domain of uncharacterized proteins from bacteria and their eukaryotic homologs. This family includes a group of functionally uncharacterized proteins from bacteria and their eukaryotic homologs which are present only in metazoa. These proteins might have nuclease activities and possibly be engaged in DNA repair or recombination, since they share sequence homology with the catalytic GIY-YIG domain of bacterial UvrC DNA repair proteins. Distinct from their prokaryotic relatives, the eukaryotic homologs contain an N-terminal extension that includes the region of approximately 3-4 ankyrin repeats, unique motifs mediating protein-protein interactions. Some of eukaryotic homologs do have an additional LEM domain located between ankyrin repeats region and GIY-YIG domain. The LEM domain, found in inner nuclear membrane proteins, may be involved in protein- or DNA-binding. The different domain composition of the eukaryotic homologs suggests that they might participate in interactions with multiple partners and implies important cellular function
YYVYALIDPRTGEVFYVGKGKGNRVFSHVKEALGEYENIKEKLSAKLQRIREILSAGLEVEHYILRHGLD
EVEAFEVEAALIDALGLTLPGLTN
>gnl|CDD|198388 cd10441, GIY-YIG_COG1833, GIY-YIG domain of hypothetical proteins from archaea and their bacterial homologs. This family includes a group of functionally uncharacterized hypothetical proteins from archaea and their bacterial homologs. These proteins contain a putative GIY-YIG domain that shows sequence homology with bacterial UvrC DNA repair proteins. Meanwhile, all of them share a C-terminal extension with semi-conserved Cys and His residues, which suggests that the extended region may be a zinc-binding nucleic acid interaction domain. Although the majority of family members have a standalone GIY-YIG domain composition, some of them do have additional endonulcease III domain or sugar fermentation stimulation protein domain, both of which are N-terminally fused to the GIY-YIG domain. As a result, those proteins could perform some other role by cooperating with different domains, which remains to be determined in the future
KGTYLLVLKLPRSTEIEVGALGEFEFPPGYYVYVGSAFGGGLAARISRHLRRAKKLHWHIDYLLEHAEVE
LAIVIRTGERLECELARALSELPSVPVPGFGASDCRCKSHLF
>gnl|CDD|198389 cd10442, GIY-YIG_PLEs, Catalytic GIY-YIG endonuclease domain of penelope-like elements and similar proteins. This model corresponds to the EN domain of PLEs that contains catalytic module of the GIY-YIG endonucleases of group I bacterial/organellar introns, as well as bacterial UvrC DNA repair proteins. It can cleave DNA with low nucleotide sequence specificity. However, the PLEs EN domain is distinct from other GIY-YIG endonucleases by the presence of a well-conserved CCHH motif (CX(2-7)CX(33-39)HX(3-5)H, X can be any residue). The role of the CCHH motif has not yet been identified. Penelope-like elements (PLEs) represent a novel class of eukaryotic retroelements, which do not belong to either long terminal repeat (LTR) retrotransposons or non-LTR retrotransposons (often called LINEs), but instead form a sister clade to telomerase reverse transcriptases (TERTs), highly specialized non-mobile reverse transcriptases (RTs) which are responsible for the addition of telomeric repeats to the ends of eukaryotic chromosomes. The single open reading frame (ORF) encoded by PLE consists of two principal domains, RT domain and endonuclease (EN) domain, jointed by a linker region of variable length. Both of these two domains are functionally active
VIYLIPCPKCGLVYIGETKRPLRERMKEHRRAIRLSGTKKSAVAKHFNEEGHSIDSDRVRILDKERNDTK
ERLALEAIHIIKNRTLKPKGLN
>gnl|CDD|198390 cd10443, GIY-YIG_HE_Tlr8p_PBC-V_like, GIY-YIG domain of uncharacterized hypothetical protein found in phycodnavirus PBCV-1 DNA virus, T. thermophila Tlr element eoncoding protein Tlr8p, and similar proteins found in bacteria. The family includes a group of diverse uncharacterized hypothetical proteins with a GIY-YIG domain that shows statistically significant similarity to the N-terminal catalytic domains of GIY-YIG family of intron-encoded homing endonuclease I-TevI. Similar to I-TevI, family members from phycodnavirus PBCV-1 DNA virus have nuclease-associated modular DNA-binding domains (NUMODs) and a helix-turn-helix (HTH) domain C-terminally fused to the GIY-YIG domain, which suggests that these PBCV-1 acquired the I-TevI-like homing endonucleases from phages by horizontal gene transfer. This family also includes proteins that appear to connect homing endonucleases with Penelope elements, such as Tetrahymena thermophila Tlr element encoding protein Tlr8p that possess additional N-terminal and central structural regions, followed by a putative superfamily 1 helicase domain and I-TevI-like GIY-YIG domain, but lacks the NUMOD domains and HTH domain. It is suggested that the Tlr8p element could have acquired its GIY-YIG domain w ithin the nucleus of the ciliate cell infected by the Phycodnavirus. Some family members only contain a standalone GIY-YIG domain and their biological functions are unclear
GVIYKITNPINGKVYIGQTTRTLEERLKQHKKAASAGPKKDFYNAIRKYGWDNFTIEILDEGESKEELNE
LEIEYIAEYNSNGPNGYNLT
>gnl|CDD|198391 cd10444, GIY-YIG_SegABCDEFG, N-terminal catalytic GIY-YIG domain of bacteriophage T4 segABCDEFG gene encoding proteins. The prototypes of Seg family are proteins SegA, B, C, D, E, F, and G encoded by five seg genes segA, B, C, D, E, F, and G in the bacteriophage T4 genome, respectively. SegA, B, C, D, E, F, and G are not encoded by introns, but free-standing homologs of the GIY-YIG family of endonucleases encoded by group I introns, which are thought to initiate the homing of their own intron by cleaving the intronless DNA at or near the site of insertion. Both phage T4 intron-encoded and free-standing GIY-YIG endonucleases contribute to the exclusion of T2 markers from the progeny of mixed infections. SegA, encoded by the bacteriophage T4 segA gene, is a double-strand DNA endonulcease with a hierarchy of site specificity. The cleavage site of SegA is located in the uvsX gene of T4. Its cleaving activity requires the presence of Mg2+ and can be stimulated by the presence of ATP or ATPgammaS. Bacteriophage T4 segB gene encoding protein SegB is a site-specific endonuclease that recognizes a 27-bp sequence, cleaves DNA by introdu cing double-strand breaks in the adjacent gene 56 of T2 during mixed infection in the presence of Mg2+, Mn2+, or Ca2+ cations, and produces mostly 3' 2-nt protruding ends at its DNA cleavage site. It functions as a homing endonuclease to ensure spreading of its own gene and the surrounding tRNA genes among T4-related phages. Bacteriophage T4 segE gene encoding SegE is a site-specific endonuclease that preferentially cleaves DNA in a site located at the 5' end of the uvsW gene in the RB30 genome. It is responsible for a non-reciprocal genetic exchange between T-even-related phages. Bacteriophage T4 gene 69 encoding SegF is a site-specific double-strand DNA endonuclease that promotes marker exclusion. It preferentially introduces a double-strand break in the adjacent T2 gene 56 over T4 gene 56 both in vitro and in vivo during mixed infection, which results in the replacement of T2 gene 56 by T4 gene 56 in a process similar to group I intron homing. The cleavage site is located 210- and 212-bp upstream from its insertion site. Bacteriophage T4 segG gene (formerly gene 32.1) encoding SegG (also known as F-TevIV) is a double-strand DNA endonuclease adjacent to gene 32 of phage T4 that promotes marker exclusion. Although it is absent from phage T2, SegG preferentially introduces a double-strand break in T2 gene 32 during mixed infection, which results in replacement of T2 genetic markers by the corresponding T4 markers. The cleavage site is located 332- and 334-bp from its insertion site
FVYRITNLTTGKIYIGKHHSCITNSLWDDYWGSGKILKNLIKKYGGENFSREILKVFPSREEAYEAEALL
ISELNVKSPNCYNIA
>gnl|CDD|198392 cd10445, GIY-YIG_bI1_like, Catalytic GIY-YIG domain of putative intron-encoded endonuclease bI1 and similar proteins. The prototype of this family is a putative intron-encoded mitochondrial DNA endonuclease bI1 found in mitochondrion Ustilago maydis. This protein may arise from proteolytic cleavage of an in-frame translation of COB exon 1 plus intron 1, containing the bI1 open reading frame. It contains an N-terminal truncated non-functional cytochrome b region and a C-terminal intron-encoded endonuclease bI1 region. The bI1 region shows high sequence similarity to endonucleases of group I introns of fungi and phage and might be involved in intron homing. Many uncharacterized bI1 homologs existing in fungi and chlorophyta in this family do not contain the cytochrome b region, but have a standalone bI1-like region, which contains a GIY-YIG domain and a minor-groove binding alpha-helix nuclease-associated modular domain (NUMOD). This family also includes a Yarrowia lipolytica mobile group-II intron COX1-i1, also called intron alpha, encoding protein with reverse transcriptase activity. The group-II intron COX1-i1 may be involv ed both in the generation of the circular multimeric DNA molecules (senDNA alpha) which amplify during the senescence syndrome and in the generation of the site-specific deletion which accumulates in the premature-death syndrome
SGIYIWINKINGKIYVGSSINLYKRLRSYLNPSYLKKNSPILRALLKYGLSNFTLTILEYYNGENKEELL
ELEQYYIDLLKPEYNILK
>gnl|CDD|198393 cd10446, GIY-YIG_unchar_1, GIY-YIG domain of uncharacterized hypothetical protein found in bacteria. The family includes a group of uncharacterized bacterial hypothetical proteins with a GIY-YIG domain that shows statistically significant similarity to the N-terminal catalytic domains of GIY-YIG family of intron-encoded homing endonuclease I-TevI and catalytic GIY-YIG domain of nucleotide excision repair endonuclease UvrC
WKTALSSVKGVYLITDTKTGKQYVGSAYGDEGIWGRWSAYANTGHGGNKELKELVPNKGYIKKNFQFSIL
EILPPTTDDKEIIARESYWKRKLGSREFGLNRN
>gnl|CDD|198394 cd10447, GIY-YIG_unchar_2, GIY-YIG domain of uncharacterized hypothetical protein found in bacteria and archaea. The family includes a group of uncharacterized hypothetical proteins, mainly found in bacteria and a few found in archaea, with a GIY-YIG domain that shows statistically significant similarity to the N-terminal catalytic domains of GIY-YIG family of intron-encoded homing endonuclease I-TevI and catalytic GIY-YIG domain of nucleotide excision repair endonuclease UvrC
GVYFLFGEDDEGGKPTVYIGEAENVLKRLKQHLKDKDFWNRAVVFVSKDNNLTKAHIKYLESRLIQLAKE
AGRYKLDNGN
>gnl|CDD|198395 cd10448, GIY-YIG_unchar_3, GIY-YIG domain of uncharacterized hypothetical protein found in bacteria. The family includes a group of uncharacterized bacterial proteins with a GIY-YIG domain that shows statistically significant similarity to the N-terminal catalytic domains of GIY-YIG family of intron-encoded homing endonuclease I-TevI and catalytic GIY-YIG domain of nucleotide excision repair endonuclease UvrC
YYVYILANKRNGTLYIGVTSDLIRRIYEHKEGLGSGFTSKYNVTRLVYYEEFEDIEEAIAREKQLKKWRR
AWKINLIEKMNPDWKDL
>gnl|CDD|198396 cd10449, GIY-YIG_SLX1_like, Catalytic GIY-YIG domain of yeast structure-specific endonuclease subunit SLX1 and its homologs. Structure-specific endonuclease subunit SLX1 is a highly conserved protein from yeast to human, with an N-terminal GIY-YIG endonuclease domain and a C-terminal PHD-type zinc finger postulated to mediate protein-protein or protein-DNA interaction. SLX1 forms active heterodimeric complexes with its SLX4 partner, which has additional roles in the DNA damage response that are distinct from the function of the heterodimeric SLX1-SLX4 nuclease. In yeast, the SLX1-SLX4 complex functions as a 5' flap endonuclease that maintains ribosomal DNA copy number, where SLX1 and SLX4 are shown to be catalytic and regulatory subunits, respectively. This endonuclease introduces single-strand cuts in duplex DNA on the 3' side of junctions with single-strand DNA. In addition to 5' flap endonuclease activity, human SLX1-SLX4 complex has been identified as a Holliday junction resolvase that promotes symmetrical cleavage of static and migrating Holliday junctions. SLX1 also associates with MUS81, EME1, C20orf94, PLK1, and ERCC1. Some eukaryotic SLX1 homologs lack the zinc finger domain, but possess intrinsically unstructured extensions of unknown function. These unstructured segments might be involved in interactions with other proteins
YVYILYSEKLDRYYIGYTSDLERRLEQHNSGKSKFTSKYRPWELVYSEAFESKSEALKREKYLKSGK
>gnl|CDD|198397 cd10450, GIY-YIG_AtGrxS16_like, GIY-YIG domain found in CAXIP1-like proteins, iron-sulfur cluster assembly proteins, and similar proteins. The family includes CAX-interacting protein-1 (CXIP1)-like proteins and iron-sulfur cluster assembly proteins, both of which contain a GIY-YIG domain that shows statistically significant similarity to the N-terminal catalytic domains of GIY-YIG family of intron-encoded homing endonuclease I-TevI and catalytic GIY-YIG domain of nucleotide excision repair endonuclease UvrC. CAXIP1 is a novel PICOT (protein kinase C-interacting cousin of thioredoxin) domain-containing Arabidopsis protein that activates H+/Ca2+ exchanger CAX1, and its homolog CAX4, but not CAX2 or CAX3. Iron-sulfur cluster assembly proteins in this family also contain a C-terminal NifU-like domain that corresponds to a common region between the NifU protein from nitrogen-fixing bacteria and rhodobacterial species. The biochemical function of NifU is unknown
GVYAVYDKSGTLQYVGYSRNVALSLRTHLARVPELCHSVKVAIFDRPDRAALEAVRDAWIEELGTVPPGN
>gnl|CDD|198398 cd10451, GIY-YIG_LuxR_like, GIY-YIG domain of LuxR and ArsR family transcriptional regulators, and uncharacterized hypothetical proteins found in bacteria. The family includes some bacterial LuxR and ArsR family transcriptional regulators. The a C-terminal conserved domain shows sequence similarity to the N-terminal catalytic GIY-YIG domains of intron-encoded homing endonucleases. Besides, they have an N-terminally fused transcriptional regulators module, comprising the winged helix-turn-helix (wHTH) domain and uncharacterized domain DUF2087. At this point, they are distinct from GIY-YIG homing endonucleases, which typically contain a variety of C-terminally fused nuclease-associated modular DNA-binding domains (NUMODs). Moreover, some key residues relevant to catalysis in GIY-YIG endonucleases are mutanted or absent in this family, which suggests that members in this family might lose the catalytic function that GIY-YIG endonucleases possess. This family also includes many uncharacterized hypothetical proteins that consist of a standalone GIY-YIG like domain
KELKRAYKERKPEMGVYAIRNTATGKVFIGSSPNLKGTLNRLRFQLNTGSHPNKELQADWNEHGAEAFTF
EVLEELEKDEDQTFDYKDELKALLELWLEKL
>gnl|CDD|198399 cd10452, GIY-YIG_RE_Eco29kI_NgoMIII, Catalytic GIY-YIG domain of type II restriction enzyme R.Eco29kI, R.NgoMIII, and similar proteins. This family corresponds to the catalytic GIY-YIG domain of GGCGCC-specific type II restriction endonucleases R.Eco29kI, NgoMIII, and similar proteins. R.Eco29kI is encoded on plasmid pECO29 in the E. coli strain 29K. This enzyme recognizes the palindromic 5'-CCGC/GG-3' target and cuts between Cyt4 and Gua5 on each strand of the restriction site to generate 3'-staggered ends. R.Eco29kI forms a domain-swapped homodimeric catalytically active complex during DNA binding and cleavage. Each subunit contains one GIY-YIG catalytic motif. Restriction endonucleases R.NgoMIII is an isoschizomer of R.Eco29kI. Members in this family are single-domain proteins sharing sequence similarities with the catalytic domain of GIY-YIG endonucleases, such as homing endonuclease I-TevI. However, they utilize loop insertions and terminal extensions instead of the separate DNA-binding domain to interact with the target site 5'-CCGC/GG-3'. A divalent metal-ion cofactor is required for their catalysis, but not for their substrate binding
FDRSKHVYRNDAFLELIKDAIRFFNGTPVHTLPPPERFQGTGVYALYYIGKNPLYKEYADINRLAYNAPI
YVGKAVPKGWRQARTSDNALNQGSELSNRLREHGRSIALTSNLDLSDFMCRFMIFEGAGSDMIGTVEAAL
IRIYKPLWNTVVDGFGNHDPGKGRYAQAKSDWDVLHPGRSWAEKCQGVHAEKKDILEKILQYLS
>gnl|CDD|198400 cd10453, GIY-YIG_RE_Cfr42I, Catalytic GIY-YIG domain of type II restriction enzyme R.Cfr42I and similar proteins. This family corresponds to the catalytic GIY-YIG domain of GGCGCC-specific type II restriction endonucleases R.Cfr42I and similar proteins. R.Cfr42I is encoded on plasmid pET21b(+) in the Citrobacter freundii RFL42 strain. This enzyme recognizes the palindromic 5'-CCGC/GG-3' target and cuts between Cyt4 and Gua5 on each strand of the restriction site to generate 3'-staggered ends. It is an isoschizomer of R.Eco29kI. Unlike R.Eco29kI, R.Cfr42I is functional as a homotetramer, binding and cleaving two cognate DNA molecules in a cooperative manner. Members in this family are single-domain proteins sharing sequence similarities with the catalytic domain of GIY-YIG endonucleases, such as homing endonuclease I-TevI. However, they utilize loop insertions and terminal extensions instead of the separate DNA-binding domain to interact with the target site 5'-CCGC/GG-3'. A divalent metal-ion cofactor is required for their catalysis
PFNPLDKRNLGKSVAEALLEQDIHPLPPLESFEGAGIYALYYTGDFEAYAPLAARNRDGQFEAPIYVGKA
VPAGARKGGFGLNHPPGKVLFNRLREHAESIRAAENLDIEDFYCRFLVVDDIWIPLGESLLIERFQPVWN
AVLDGFGNHDPGKGRY
>gnl|CDD|198401 cd10454, GIY-YIG_COG3680_Meta, GIY-YIG domain of hypothetical proteins from Metazoa. Members of this family are functionally uncharacterized hypothetical proteins from Metazoa. They have bacterial homologs that display sequence homology with the catalytic GIY-YIG domain of bacterial UvrC DNA repair proteins. However, unlike their bacterial relatives, these Metazoan proteins contain an N-terminal extension that includes the region of approximately 3-4 ankyrin repeats, unique motifs mediating protein-protein interactions. Some of them do have an additional LEM domain located between ankyrin repeats region and GIY-YIG domain. The LEM domain, found in inner nuclear membrane proteins, may be involved in protein- or DNA-binding. The different domains composition suggests members in this subfamily might participate in interactions with multiple partners and imply some important cellular functions
SFNYLLLDPRVTRNLPSRARGLTPIETFQTFVSSIFYVGKGKRSRPYAHFYEALKQHNDKDKKKGSRKLR
RILDIWNSGLGVVSLHCFQNVIPVEAYTREAAMIEALGLSNLTN
>gnl|CDD|198402 cd10455, GIY-YIG_SLX1, Catalytic GIY-YIG domain of yeast structure-specific endonuclease subunit SLX1 and its eukaryotic homologs. Structure-specific endonuclease subunit SLX1 is a highly conserved protein from yeast to human, with an N-terminal GIY-YIG endonuclease domain and a C-terminal PHD-type zinc finger postulated to mediate protein-protein or protein-DNA interaction. SLX1 forms active heterodimeric complexes with its SLX4 partner, which has additional roles in the DNA damage response that are distinct from the function of the heterodimeric SLX1-SLX4 nuclease. In yeast, the SLX1-SLX4 complex functions as a 5' flap endonuclease that maintains ribosomal DNA copy number, where SLX1 and SLX4 are shown to be catalytic and regulatory subunits, respectively. This endonuclease introduces single-strand cuts in duplex DNA on the 3' side of junctions with single-strand DNA. In addition to 5' flap endonuclease activity, human SLX1-SLX4 complex has been identified as a Holliday junction resolvase that promotes symmetrical cleavage of static and migrating Holliday junctions. SLX1 also associates with MUS81, EME1, C20orf94, PLK1, and ERCC1. Some eukaryotic SLX1 homologs lack the zinc finger domain, but possess intrinsically unstructured extensions of unknown function. These unstructured segments might be involved in interactions with other proteins
FYGVYLLRSLNPKYKGRTYIGFTVNPPRRLRQHNGELKGGAKKTSRKRPWEMVLIVHGFPSKVAALQFEW
AWQHPS
>gnl|CDD|198403 cd10456, GIY-YIG_UPF0213, The GIY-YIG domain of uncharacterized protein family UPF0213 related to structure-specific endonuclease SLX1. This family contains a group of uncharacterized proteins found mainly in bacteria and several in dsDNA viruses. Although their function roles have not been recognized, these proteins show significant sequence similarities with the N-terminal GIY-YIG endonuclease domain of structure-specific endonuclease subunit SLX1, which binds another structure-specific endonuclease subunit SLX4 to form an active heterodimeric SLX1-SLX4 complex. This complex functions as a 5' flap endonuclease in yeast, and has also been identified as a Holliday junction resolvase in human
WYVYILRCADGSLYTGITTDLERRLAEHNSGKGAKYTRGRRPVKLVYSEEFDDRSEALKREYRIKKLS
>gnl|CDD|198404 cd10457, GIY-YIG_AtGrxS16, GIY-YIG domain found in CAXIP1-like proteins. The family includes CAX-interacting protein-1 (CXIP1)-like proteins which contain a GIY-YIG domain that shows statistically significant similarity to the N-terminal catalytic domains of GIY-YIG family of intron-encoded homing endonuclease I-TevI and catalytic GIY-YIG domain of nucleotide excision repair endonuclease UvrC. CAXIP1 is a novel PICOT (protein kinase C-interacting cousin of thioredoxin) domain-containing Arabidopsis protein that activates H+/Ca2+ exchanger CAX1, and its homolog CAX4, but not CAX2 or CAX3
GVYAVYDKSGTLQYIGLSRKIAASLATHMEELPELCGSVKVLIVDEPSKAELTEAWKSWMEEHIAEAGAV
PPGN
>gnl|CDD|198405 cd10458, GIY-YIG_NifU, GIY-YIG domain found in iron-sulfur cluster assembly proteins. This family includes a group of uncharacterized iron-sulfur cluster assembly proteins that transiently bind the iron-sulfur cluster before transfer to target apoproteins. These iron-sulfur cluster assembly proteins contains a GIY-YIG domain that shows statistically significant similarity to the N-terminal catalytic domains of GIY-YIG family of intron-encoded homing endonuclease I-TevI and catalytic GIY-YIG domain of nucleotide excision repair endonuclease UvrC. They also contain a C-terminal NifU-like domain that corresponds to a common region between the NifU protein from nitrogen-fixing bacteria and rhodobacterial species. The biochemical function of NifU is unknown
GVYAMYDPSDNMQYVGYARNVVLAVKTHLARVGPGRCARVRVAIFANKAMASRANLEREQDRWLGEWGDT
ALPPGN
>gnl|CDD|198417 cd10459, PUB_PNGase, PNGase/UBA or UBX (PUB) domain of the P97 adaptor protein Peptide:N-glycanase (PNGase). This PUB (PNGase/UBA or UBX) domain is found in the p97 adaptor protein PNGase (Peptide:N-glycanase). The PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. Peptide:N-glycanase (PNGase), a deglycosylating enzyme that functions in proteasome-dependent degradation of misfolded glycoproteins which are translocated from the endoplasmic reticulum (ER) to the cytosol during ERAD, associates with the ubiquitin-proteasome system proteins mediated by the N-terminal PUB domain. PNGase is present in all eukaryotic organisms; however, the yeast PNGase ortholog does not contain the PUB domain. The mammalian PNGase binds a considerable number of proteins via its PUB domain; these include ERAD E3 enzyme, the autocrine motility factor receptor (AMFR or gp78), SAKS and Derlin-1
VRLLEENSEDVFLEASEALLTYANNILRNPNDPKYRSIRLDNPVFSTKLLPARGAIECLFEMGFVEDEDR
LFLPRNASLEKLQDLRDLLAAER
>gnl|CDD|198418 cd10460, PUB_UBXD1, PNGase/UBA or UBX (PUB) domain of UBXD1. This PUB domain is found in p97 adaptor protein UBXD1 (UBX domain-containing protein 1, also called UBXD6). It functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. The PUB domain in UBX-domain protein 1 (UBXD1), which is widely expressed in higher eukaryotes, except for fungi, and which is involved in substrate recruitment to p97, interacts strongly with the C-terminus of p97. UBXD1 also interacts with HRD1 and HERP, both components of the ERAD pathway, via p97. It is possibly involved in aggresome formation; aggresomes are perinuclear compartments that contain misfolded proteins colocalized with centrosome markers
CLMIHTLNKDREKVEECVDTLCKYLENIIDHPDEEKYRKIRLSNKVFQEKVLPVEGALEFLEAAGFEEKT
LPEQEDEEDFLVLSEECDIDSLELAKDLLQSL
>gnl|CDD|198419 cd10461, PUB_UBA_plant, PNGase/UBA or UBX (PUB) domain of plant Ubiquitin-associated (UBA) domain containing proteins. The PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. The UBA domain, along with UBL (ubiquitin-like) domain, has been implicated in proteasomal degradation by associating with substrates destined for degradation as well as with subunits of the proteasome, thus regulating protein turnover. This family contains only plant UBA domain-containing proteins
LVDLKKAHKDDPDAVKTAFQTLLTYLGNVAKNPDEEKFRRIRLTNAAFQERVGALRGGIEFLELCGFERD
EGDEALVLPRDKVDMALLNTAGAELNSAINNPFFGVL
>gnl|CDD|198420 cd10462, PUB_UBA, PNGase/UBA or UBX (PUB) domain of Ubiquitin-associated (UBA) domain containing proteins. The PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. The UBA domain, along with UBL (ubiquitin-like) domain, has been implicated in proteasomal degradation by associating with substrates destined for degradation as well as with subunits of the proteasome, thus regulating protein turnover
CNNLKKEYKDTDKQGLMTCLNTLRTYISNAHDHPLEEKYKKIRKENKAFVSKVLIFEGAIEILLACGFED
TGDFLFIINKIPDTFLCSQAIKFIDLILQT
>gnl|CDD|198421 cd10463, PUB_WLM, PNGase/UBA or UBX (PUB) domain of the Wss1p-like metalloprotease (WLM) family. The PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. WLM domains are found mostly in plant proteins, belonging to the Zincin-like superfamily of Zn-dependent peptidases that are linked to the ubiquitin signaling pathway through its fusion with the ubiquitin-binding PUB, ubiquitin-like, and Little Finger domains. More specifically, genetic evidence implicates the WLM family in de-SUMOylation
ALAALRSAVSPAEAVSALQTLFKILGNAIEHPNEDKFRRLRKSNPAFQRRVARFPGAVELLLAAGFAEEG
VSGPDTYLLLRNDPGLLWLAKSSVEE
>gnl|CDD|198422 cd10464, PUB_RNF31, PNGase/UBA or UBX (PUB) domain of the RNF31 (or HOIP) protein. This PUB domain is found in the p97 adaptor protein RNF31 (RING finger protein 31). The PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. The RNF31 protein, also known as HOIP or Zibra, contains an N-terminal PUB domain similar to those in PNGase and UBXD1, suggesting its association with p97. RNF31 functions in a complex with another RING-finger protein (HOIL-IL), displaying E3 ubiquitin-protein ligase activity, and forming linear ubiquitin chain assembly complex (LUBAC) through linkages between the N- and C-termini of ubiquitin. LUBAC has been shown to activate the NF-kappaB pathway
NFARLLRLNQHVNNQFLNKLVTALNILEKYGRNLLSPGRPKFWRSVKFSNPVFRTKVDAVQGGRNVLSLY
GYTESQPDGLSFPDDVEEPDISKVAKVTLDLIVLRHELEML
>gnl|CDD|198456 cd10466, FimH_man-bind, Mannose binding domain of FimH and related proteins. This family, restricted to gammaproteobacteria, includes FimH, a mannose-specific adhesin of uropathogenic Escherichia coli strains. The domain appears to bind specifically to D-mannose and mediates cellular adhesion to mannosylated proteins, a prerequisite to colonization and subsequent invasion of epithelial tissues
FTCRVADTGQIFGSGSANVYVNLSPTVNVGQNLVVDLSQLIQCMNDDPSGTITDYVNLLRGSGFGGPLLN
FSGSLDFYGSTYPFPLQSDTKVIVYSSGTWKPLPLKLYLTPVSAAGGVVIKAGDLIATLTMNKKSTYGGR
ADPFNFTWRFYAKNDVVIPT
>gnl|CDD|198458 cd10467, FAM20_C_like, C-terminal putative kinase domain of FAM20 (family with sequence similarity 20), Drosophila Four-jointed (Fj), and related proteins. Drosophila Fj is a Golgi kinase that phosphorylates Ser or Thr residues within extracellular cadherin domains of a transmembrane receptor Fat and its ligand, Dachsous (Ds). The Fat signaling pathway regulates growth, gene expression, and planar cell polarity (PCP). Defects from mutation in the Drosophila fj gene include loss of the intermediate leg joint, and a PCP defect in the eye. Fjx1, the murine homologue of Fj, has been shown to be involved in both the Fat and Hippo signaling pathways, these two pathways intersect at multiple points. The Hippo pathway is important in organ size control and in cancer. FAM20B is a xylose kinase that may regulate the number of glycosaminoglycan chains by phosphorylating the xylose residue in the glycosaminoglycan-protein linkage region of proteoglycans. This domain has homology to a kinase-active site, mutation of three conserved Asp residues at the Drosophila Fj putative active site abolished its ability to phosphorylate Ft and Ds cadherin domains. FAM20A may participate in enamel development and gingival homeostasis, FAM20B in proteoglycan production, and FAM20C in bone development. FAM20C, also called Dentin Matrix Protein 4, is abundant in the dentin matrix, and may participate in the differentiation of mesenchymal precursor cells into functional odontoblast-like cells. Mutations in FAM20C are associated with lethal Osteosclerotic Bone Dysplasia (Raine Syndrome), and mutations in FAM20A with Amelogenesis imperfecta (AI) and Gingival Hyperplasia Syndrome. This model includes the FAM20_C domain family, previously known as DUF1193; FAM20_C appears to be homologous to the catalytic domain of the phosphoinositide 3-kinase (PI3K)-like family
FFSPANNTCFYGGCGYYCKTEEAACGNPDQIEGSLTSFLPDLLLLLRKKWRHPWQRTYTERKKAEWEVDL
DYCDEVKKLPPYDSGRRLLDLIDMAIFDFLIGNMDRHHYELFELQWNEGFLIHLDNGKGFGRPSHDELSI
LAPLYQCCVIRKSTWERLLLLHRGGGVLSRLLRESLRHDPLLPVLTEPHLQALDRRLDIVLATVEKCIEK
>gnl|CDD|198459 cd10468, Four-jointed-like_C, C-terminal kinase domain of Drosophila Four-jointed (Fj), mouse Fjx1, and related proteins. Drosophila Fj is a Golgi type II transmembrane protein that is partially secreted, and is a kinase that phosphorylates Ser or Thr residues within extracellular cadherin domains of a transmembrane receptor Fat and its ligand, Dachsous (Ds). Mutation of three conserved Asp residues at the Drosophila Fj putative active site abolished its ability to phosphorylate Ft and Ds cadherin domains. The Fat signaling pathway regulates growth, gene expression, and planar cell polarity (PCP). Defects from mutation in Drosophila Fj include loss of the intermediate leg joint, and a PCP defect in the eye. The expression of the Drospophila fj gene is modulated by Notch, Unpaired (JAK/STAT), and Wingless signals. Mouse Fjx1, has been shown to be involved in both the Fat and Hippo signaling pathways; these two pathways intersect at multiple points. The Hippo pathway is important in organ size control and in cancer. The expression of the mouse fjx1 gene is also Notch dependent; fjx1 is expressed in the brain, the peripheral nervous system, in epithelial structures of different organs, and during limb development
EFARQSRVVRLEEGCGRMQNRLATFADGTRACVRYRINTDQIQGEIFSYYLARLLGLRNLPPLALGLVEA
RGAQWVAVQSELRQAQWTERRPVVLTRWLPNLTPAVIPAPFRSEDRRLNPLDVAGGTLQNGLSQAELVEL
AQWSDLIVFDYLTANLDRLVNNLYNLQWNPAVMDRPTHNLARTPHSGLLVFLDNESGLLHGYRLLDKYEK
YHSPLLQSLCVFRKRTAERVRELHRGQDAGARLLDLYRRHEPGVFDELPSLPDKSAQILQERIDQVYKHI
LKCKSK
>gnl|CDD|198460 cd10469, FAM20A_C, C-terminal putative kinase domain of FAM20A. Human FAM20A may play a fundamental role in enamel development and gingival homeostasis as mutations in FAM20A may underlie the pathogenesis of the autosomal recessive Amelogenesis imperfecta (AI) and Gingival Hyperplasia Syndrome. It is expressed in ameloblasts and gingivae. AI refers to a heterogeneous group of disorders of biomineralization caused by a lack of normal enamel formation. Mouse FAM20A is a secreted protein and the gene encoding it is differentially expressed in hematopoietic cells undergoing myeloid differentiation. This protein has also been associated with growth disorder in mice. The C-terminal domain of FAM20A is a putative kinase domain, based on mutagenesis of the C-terminal domain of Drosophila Four-Jointed, a related Golgi kinase. This subfamily belongs to the FAM20_C (also known as DUF1193) domain family
FNSPASNVCFFAKCPYMCKTEYAVCGNPHLLEGSLSAFLPSLNLAPRLSIPNPWIRSYTFAGKEEWEVNP
LYCDTVKEIYPYNSGNRLLNIIDMAIFDFLIGNMDRHHYEMFTKFGDDGFLLHLDNARGFGKHSHDEISI
LSPLSQCCIIKKSTLLRLQLLAQPDYRLSDVMRESLEKDALQPVLTEPHLLALDRRLQKILRTVERCIRA
LGKDKVV
>gnl|CDD|198461 cd10470, FAM20B_C, C-terminal putative kinase domain of FAM20B xylose kinase. Experiments with human FAM20B suggest that it is a xylose kinase that participates in proteoglycan production. It may regulate the number of glycosaminoglycan chains by phosphorylating the xylose residue in the glycosaminoglycan-protein linkage region of proteoglycans. The C-terminal domain of FAM20B is a putative kinase domain, based on mutagenesis of the C-terminal domain of Drosophila Four-Jointed, a related Golgi kinase. This subfamily belongs to the FAM20_C (also known as DUF1193) domain family
FLKVGNNTCFYGVCYYCKEEEPACGEGDIMEGSVTLWLPDVWPLQKHRHPWQRTYKENKLARWETDEDYC
DKVKKKSPYDSGPRLLDLIDTAIFDFLIGNGDRHHYETFQDDPESMLLLLDNAKSFGNPDLDELSILAPL
YQCCIIRKSTWDRLKLLKGGVLTELLEEATKHDPLSPLLTEPHLRAIERRLLIVYATVEQCVDKFG
>gnl|CDD|198462 cd10471, FAM20C_C, C-terminal putative kinase domain of FAM20C (also known as Dentin Matrix Protein 4, DMP4). Mouse DMP4 is abundant in the dentin matrix, and is expressed in high levels in odontoblasts. These latter cells synthesize various nucleators or inhibitors of mineralization. The in vivo role of DMP4 in dentinogenesis is unclear. However, gain- and loss-of-function experiments suggest that it participates in the differentiation of mesenchymal precursor cells into functional odontoblast-like cells. In addition to this domain, DMP4 contains a Greek key calcium-binding domain. Human FAM20C participates in bone development; mutations in FAM20C are associated with lethal Osteosclerotic Bone Dysplasia (Raine Syndrome), an autosomal recessive disorder in which affected individuals die within days or weeks of birth, usually due to thoratic malformation resulting in respiratory failure. The C-terminal domain of FAM20C is a putative kinase domain, based on mutagenesis of the C-terminal domain of Drosophila Four-Jointed, a related Golgi kinase. This subfamily belongs to the FAM20_C (also known as DUF1193) domain family
FISPANNICFYGECSYYCSTEHALCGKPDQIEGSLAAFLPDLSLAKRKTWRNPWRRSYHKRKKAEWEVDP
DYCEEVKQTPPYDSGTRILDIMDMTVFDFLMGNMDRHHYETFEKFGNETFIIHLDNGRGFGKYSHDELSI
LVPLTQCCRIRKSTYLRLQLLAKEEYKLSLLMAESLQRDKLAPILYQPHLEALDRRLRIVLKAVSDCVEK
DG
>gnl|CDD|198440 cd10472, EphR_LBD_B, Ligand Binding Domain of Ephrin type-B receptors. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. They play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphB receptors are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis
ETLMDTRTATAELGWTAHPPSGWEEVSGYDENMNTIRTYQVCNVFESNQNNWLRTKFIRRRGAHRVYVEM
KFTVRDCSSIPNVPGSCKETFNLYYYESDSDIATKTSPFWMENPYVKVDTIAADESFSQVDLGGRVMKVN
TEVRSFGPLSRNGFYLAFQDYGACMSLISVRVFYKK
>gnl|CDD|198441 cd10473, EphR_LBD_A, Ligand Binding Domain of Ephrin type-A Receptors. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis
EVVLLDSKTAQGELGWITYPPNGWEEISEMDEDYTPIRTYQVCNVMEPNQNNWLRTNWIYRGEAQRIYIE
LKFTLRDCNSFPGVLGTCKETFNLYYMESDLDLGRNIRENQFTKIDTIAADESFTQGDLGDRIMKLNTEV
REVGPLTKKGFYLAFQDVGACVALVSVRVYYKK
>gnl|CDD|198442 cd10474, EphR_LBD_B4, Ligand Binding Domain of Ephrin type-B Receptor 4. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB4 plays a role in osteoblast differentiation and has been linked to multiple myeloma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling)
EETLLNTKLETADLKWVTYPQVDGQWEELSGLDEEQHSVRTYEVCDAQRAGGQAHWLRTGWVPRRGAVHV
YATLRFTMLECLSLPRAGRSCKETFTVFYYESDADTATAHTPAWMENPYIKVDTVAAEHLTRKRPGAEAT
GKVNVKTLRLGPLSKAGFYLAFQDQGACMALLSLHLFYKK
>gnl|CDD|198443 cd10475, EphR_LBD_B6, Ligand Binding Domain of Ephrin type-B Receptor 6. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB6, a kinase-defective member of this family, is downregulated in MDA-MB-231-breast cancer cells and myeloid cancers and upregulated in neuroblasoma and glioblastoma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling)
EEVLLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEVCNVAAQGPGQDNWLRTHFIERRGAHRVH
VRLHFSVRDCASLGVPGGTCRETFTLYYRQADEPDEPADKSEWHEGPWTKVDTIAADESFPASLGKGGQG
LQMNVKERSFGPLTQRGFYLAFQDSGACLSLVAVKVFFYK
>gnl|CDD|198444 cd10476, EphR_LBD_B1, Ligand Binding Domain of Ephrin type-B Receptor 1. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. Using EphB1 knockout-mice, EphB1 has been shown to be essential to the development of long-term potentiation (LTP), a cellular model of synaptic plasticity, learning and memory formation. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling)
ETLMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEM
RFTVRDCSSLPNVPGSCKETFNLYYYETDSVIATKKSAFWTEAPYLKVDTIAADESFSQVDFGGRLMKVN
TEVRSFGPLTRNGFYLAFQDYGACMSLLSVRVFFKK
>gnl|CDD|198445 cd10477, EphR_LBD_B2, Ligand Binding Domain of Ephrin type-B Receptor 2. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB2 plays a role in cell positioning in the gastrointestinal tract by being expressed in proliferating progenitor cells. It also has been implicated in colorectal cancer. A loss of EphB2, as well as EphA4, also precedes memory decline in a murine model of Alzheimers disease. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling)
AEETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKYIRRRGAHRIHV
EMKFSVRDCSSIPSVPGSCKETFNLYYYESDFDSATKTFPNWMENPWVKVDTIAADESFSQVDLGGRVMK
INTEVRSFGPVSRNGFYLAFQDYGGCMSLIAVRVFYRK
>gnl|CDD|198446 cd10478, EphR_LBD_B3, Ligand Binding Domain of Ephrin type-B Receptor 3. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB3 plays a role in cell positioning in the gastrointestinal tract by being preferentially expressed in Paneth cells. It also has been implicated in early colorectal cancer and early stage squamous cell lung cancer. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling)
EETLMDTKWVTSELAWTTHPESGWEEVSGYDEAMNPIRTYQVCNVRESNQNNWLRTGFIPRRDVQRVYVE
LKFTVRDCNSIPNIPGSCKETFNLFYYESDSDSASASSPFWMENPYVKVDTIAPDESFSRLDSGRVNTKV
RSFGPLSKAGFYLAFQDLGACMSLISVRAFFKK
>gnl|CDD|198447 cd10479, EphR_LBD_A1, Ligand Binding Domain of Ephrin type-A Receptor 1. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA1 is downregulated in some advanced colorectal and myeloid cancers and upregulated in neuroblasoma and glioblastoma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion
EVTLMDTSTAQGELGWLLDPPEVGWSEVQQMLNGTPLYMYQDCPVQSEGDTDHWLRSNWIYRGEEASRIY
VELQFTVRDCKSFPGGAGPLGCKETFNLYYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKL
NVERCSLGKLTRRGLYLAFHNPGACVALVSVRVFYQR
>gnl|CDD|198448 cd10480, EphR_LBD_A2, Ligand Binding Domain of Ephrin type-A Receptor 2. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA2 negatively regulates cell differentiation and has been shown to be overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion
EVVLLDFAAAGGELGWLTHPYGKGWDLMQNVMNDSPIYMYSVCNVMSGEQDNWLRTNWIYRSEAERIFIE
LKFTVRDCNSFPGGAGSCKETFNLYYAESDVDYGTNFQKRQFRKIDTIAPDEITVSSDFETRNVKLNVEE
RSVGPLTRKGFYLAFQDIGACVALLSVRVYYKKC
>gnl|CDD|198449 cd10481, EphR_LBD_A3, Ligand Binding Domain of Ephrin type-A Receptor 3. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA3 has been implicated in leukemia, lung and other cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion
EVNLLDSKAIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWIPRNSAQKIYVE
LKFTLRDCNSIPLVLGTCKETFNLYYMESDEDQGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEV
REVGPVSKKGFYLAFQDVGACVALVSVRVYFKK
>gnl|CDD|198450 cd10482, EphR_LBD_A4, Ligand Binding Domain of Ephrin type-A Receptor 4. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. A loss of EphA4, as well as EphB2, precedes memory decline in a murine model of Alzheimers disease. EphA4 has been shown to have a negative effect on axon regeneration and functional restoration in corticospinal lesions and is downregulated in some cervical cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling)
EVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWIPREGAQRVYI
EIKFTLRDCNSLPGVMGTCKETFNLYYYESNNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNTE
VRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKK
>gnl|CDD|198451 cd10483, EphR_LBD_A5, Ligand Binding Domain of Ephrin type-A Receptor 5. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA5 is almost exclusively expressed in the nervous system. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling)
EVNLLDSRSVMGDLGWIAYPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGASRIFIE
LKFTLRDCNSLPGGLGTCKETFNVYYFESNDEDGRNIRENQYIKIDTIAADESFTELDLGDRVMKLNTEV
RDVGPLTKKGFYLAFQDLGACIALVSVRVYYKK
>gnl|CDD|198452 cd10484, EphR_LBD_A6, Ligand Binding Domain of Ephrin type-A Receptor 6. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA6, like other Eph receptors and their ephrin ligands, seems to play a role in neural development, underlying learning and memory. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling)
QVVLLDTTMVLGELNWKTYPCNGWDAITEMDEYNRPIHTYQVCNVMEPNQNNWLRTNWISRDAAQKIYVE
MKFTLRDCNSIPWVVGTCKETFNLHYMESDEAHAVKFKPNQYSKIDTIAADESFTQMDLGDRILKLNTEV
REVGPITRKGFYLAFQDIGACIALVSVRVYYKK
>gnl|CDD|198453 cd10485, EphR_LBD_A7, Ligand Binding Domain of Ephrin type-A Receptor 7. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA7 has been implicated in various cancers, including prostate, gastic and colorectal cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling)
AKEVILLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIF
VELKFTLRDCNSLPGVLGTCKETFNLYYYETDYDTGRNIRENQYVKIDTIAADESFTQGDLGERKMKLNT
EVREIGPLSKKGFYLAFQDVGACIALVSVKVYYKKCW
>gnl|CDD|198454 cd10486, EphR_LBD_A8, Ligand Binding Domain of Ephrin type-A Receptor 8. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA8 has been implicated in various cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling)
EVNLLDTSTISGDWGWLTYPSHGWDSINEMDEYFSPIHTYQVCNVMSPNQNNWLRTNWVQRDGARRVYAE
IKFTLRDCNSMPGVLGTCKETFNLYYYESDRDLGTSTWESQFLKIDTIAADESFTNVDLGVRRLKLNTEV
RGVGPLSKRGFYLAFQDIGACIAIVSVRVYYKK
>gnl|CDD|198455 cd10487, EphR_LBD_A10, Ligand Binding Domain of Ephrin type-A Receptor 10. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction results in cell-cell repulsion or adhesion
EVVLLDSKESQAELGWTSLPSNGWEEISGVDEHYKPIRTYQVCNVMEPNQNNWLQTGWISRGRGQRIFIE
LQFTLRDCNSIPGVAGTCKETFNLYYAESDADLGRRLRESRPRKIDTIAADESFTQGDLGERKMKLNTEV
REIGHLSRRGFHLAFQDVGACVALVSVRVYYKQ
>gnl|CDD|199812 cd10488, MH1_R-SMAD, N-terminal Mad Homology 1 (MH1) domain of receptor regulated SMADs. The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. It binds to the major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 domain is found in all receptor regulated SMADs (R-SMADs) including SMAD1, SMAD2, SMAD3, SMAD5 and SMAD9. SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD2 regulates multiple cellular processes, such as cell proliferation, apoptosis and differentiation, while SMAD3 modulates signals of activin and TGF-beta. SMAD4, a common mediator SMAD (co-SMAD) binds R-SMADs, forming an oligomeric complex that binds to DNA and serves as a transcription factor. SMAD5 is involved in bone morphogenetic proteins (BMP) signal modulation, possibly playing a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 (also known as SMAD8) can mediate the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway
PIVKRLLGWKKGEQNGEEEKWAEKAVKSLVKKLKKKGQLEELEKAISTQNVNTRCVTIPRSLDGRLQVSH
RKGLPHVIYCRLWRWPDLQSHHELKPLELCEFAFNMKKEEVCINPYHYKRVET
>gnl|CDD|199813 cd10489, MH1_SMAD_6_7, N-terminal Mad Homology 1 (MH1) domain in SMAD6 and SMAD7. The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 domain is found in SMAD6 and SMAD7, both inhibitory SMADs (I-SMADs) and negative regulators of signaling mediated by TGF-beta superfamily. SMAD6 specifically inhibits bone morphogenetic protein (BMP) type I receptor mediated signaling while SMAD7 enhances muscle differentiation and is often associated with cancer, tissue fibrosis and inflammatory diseases
GAVRRLWAHRTRHSQNPLEERDLRAAFHALLKRLKEKQLELLLQAVESRGGDYLACVLLPRRDPRSMPQD
PHVLCCQLFRWPDLRHSSELKRLPTCESAKDPVYVCCNPYHWSRLCRPE
>gnl|CDD|199814 cd10490, MH1_SMAD_1_5_9, N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8). The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 domain is found in SMAD1, SMAD5 and SMAD9, all closely related receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in bone morphogenetic proteins (BMP) signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway
FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEELEKALSCPGQPSKCVTIPRSLDGRLQVS
HRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVES
>gnl|CDD|199815 cd10491, MH1_SMAD_2_3, N-terminal Mad Homology 1 (MH1) domain in SMAD2 and SMAD3. The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 is found in SMAD2 as well as SMAD3. SMAD2 mediates the signal of the transforming growth factor (TGF)-beta, and thereby regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. It plays a role in the transmission of extracellular signals from ligands of the TGF-beta superfamily growth factors into the cell nucleus. SMAD3 modulates signals of activin and TGF-beta. It binds SMAD4, enabling its transmigration into the nucleus where it forms complexes with other proteins and acts as a transcription factor. Increased SMAD3 activity has been implicated in the pathogenesis of scleroderma
TPPVVKRLLGWKKGENGQEEKWSEKAVKSLVKKLKKTGGLDELEKAITTQNSNTKCITIPRSLDGRLQVS
HRKGLPHVIYCRLWRWPDLQSHHELRAIETCEYAFNLKKDEVCVNPYHYQRVET
>gnl|CDD|199816 cd10492, MH1_SMAD_4, N-terminal Mad Homology 1 (MH1) domain in SMAD4. The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 belongs to SMAD4, a common mediator SMAD (co-SMAD), which belongs to the Dwarfin family of proteins and is involved in many cell functions such as differentiation, apoptosis, gastrulation, embryonic development and cell cycle. SMAD4 binds receptor regulated SMADs (R-SMADs) such as SMAD1 or SMAD2, and forms an oligomeric complex that binds to DNA and serves as a transcription factor. SMAD4 is often mutated in several cancers, such as multiploid colorectal cancer and pancreatic carcinoma, as well as in juvenile polyposis syndrome (JPS)
DACLSIVHSLMCHRQGGESESFAKRAIESLVKKLKDKRDELDSLITAITSNGAHPSKCVTIQRTLDGRLQ
VAGRKGFPHVIYARIWRWPDLHKNELKHVKFCQYAFDLKCDSVCVNPYHYERVVS
>gnl|CDD|199817 cd10493, MH1_SMAD_6, N-terminal Mad Homology 1 (MH1) domain in SMAD6. The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 belongs to SMAD6, an inhibitory SMAD (I-SMAD) or antagonistic SMAD, which acts as a negative regulator of signaling mediated by TGF-beta superfamily ligands, by competing with SMAD4 and preventing the transcription of SMAD4's gene products. SMAD6 specifically inhibits bone morphogenetic protein (BMP) type I receptor mediated signaling
EGKSRQVALEQELKSVTYALLKRLKERSLDVLLEAVESRGGLPSGCVMVPRTELRLGGRRVPPQLLLCRL
FRWPDLQHPAQLKALCHCQSFGAQDGPTVCCNPYHYSRLCGPE
>gnl|CDD|199818 cd10494, MH1_SMAD_7, N-terminal Mad Homology 1 (MH1) domain in SMAD7. The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins. It binds to the major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 belongs to SMAD7, an inhibitory SMAD (I-SMAD) or antagonistic SMAD, which acts as a negative regulator of signaling mediated by TGF-beta superfamily ligands, by blocking TGF-beta type 1 and activin association with the receptor as well as access to SMAD2. SMAD7 enhances muscle differentiation, playing pivotal roles in embryonic development and adult homoeostasis. Altered expression of SMAD7 is often associated with cancer, tissue fibrosis and inflammatory diseases
GCCLAKPPRGGGGGAAEAELKALTHSVLKKLKERQLEGLLQAVESRGGARTPCLLLPARLDARLGQQSYS
LPLLLCKVFRWPDLRHSSEVKRLSCCESYGKINPELVCCNPHHLSRLCELESP
>gnl|CDD|199820 cd10495, MH2_R-SMAD, C-terminal Mad Homology 2 (MH2) domain in receptor regulated SMADs. The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain. Receptor regulated SMADs (R-SMADs) include SMAD1, SMAD2, SMAD3, SMAD5 and SMAD9. SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD2 regulates multiple cellular processes, such as cell proliferation, apoptosis and differentiation, while SMAD3 modulates signals of activin and TGF-beta. SMAD5 is involved in BMP signal modulation, possibly playing a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 (also known as SMAD8) can mediate the differentiation of mesenchymal stem cells into tendon-like cells by inhibiting the osteogenic pathway
WCSISYYELNSRVGEQFKASNPSIIVDGFTDPSNNSDRFCLGLLSNVNRNATIENTRRHIGRGVHLFYVG
GEVYAECLSDSAIFVQSRNCNLRHGFHPATVCKIPPGCSLKIFNNQSFAQLLEQSVNRGFEAVYELTKMC
TIRISFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLT
>gnl|CDD|199821 cd10496, MH2_I-SMAD, C-terminal Mad Homology 2 (MH2) domain in Inhibitory SMADs. The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD6 and SMAD7 are inhibitory SMADs (I-SMADs) that function as negative regulators of signaling mediated by the TGF-beta superfamily. SMAD6 specifically inhibits bone morphogenetic protein (BMP) type I receptor mediated signaling, while SMAD7 enhances muscle differentiation and is often associated with cancer, tissue fibrosis and inflammatory diseases
WCTIAYWELRERVGRLYPVKQPAVNIFDDLPKGDGFCLGALNRQGNASEAVARVRSKIGLGVTLSREPDG
VWIYNRSEYPIFVNSPTLDSPPSRNLLVTKVPPGYSLKVFDYERAALLQRRDDHFSPQGPVDPNSVRISF
VKGWGPNYSRQFITSCPCWLEILLN
>gnl|CDD|199822 cd10497, MH2_SMAD_1_5_9, C-terminal Mad Homology 2 (MH2) domain in SMAD1, SMAD5 and SMAD9. The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD1, SMAD5 and SMAD9 (also known as SMAD8), are receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in BMP signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway
YQEPKYWCSIAYYELNNRVGEAFHASSTSIIVDGFTDPSNNSDRFCLGLLSNVNRNSTIENTRRHIGKGV
HLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVY
ELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS
>gnl|CDD|199823 cd10498, MH2_SMAD_4, C-terminal Mad Homology 2 (MH2) domain in SMAD4. The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain. SMAD4, which belongs to the Dwarfin family of proteins, is involved in many cell functions such as differentiation, apoptosis, gastrulation, embryonic development and the cell cycle. SMAD4 binds receptor regulated SMADs (R-SMADs) such as SMAD1 or SMAD2, and forms an oligomeric complex that binds to DNA and serves as a transcription factor. SMAD4 is often mutated in several cancers, such as multiploid colorectal cancer, cervical cancer and pancreatic carcinoma, as well as in juvenile polyposis syndrome
PEYWCSIAYFELDTQVGETFKVPSSCPTVTVDGYVDPSGGNRFCLGQLSNVHRTEASERARLHIGKGVQL
DCKGEGDVWLRCLSDHSVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAA
AQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHL
HRALQLLDEVLH
>gnl|CDD|199824 cd10499, MH2_SMAD_6, C-terminal Mad Homology 2 (MH2) domain in SMAD6. The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD6, an inhibitory or antagonistic SMAD (I-SMAD), acts as a negative regulator of signaling mediated by the TGF-beta superfamily of ligands, by competing with SMAD4 and preventing the transcription of SMAD4's gene products. SMAD6 specifically inhibits bone morphogenetic protein (BMP) type I receptor mediated signaling. SMAD6 and SMAD7 act as critical mediators for effective TGF-beta I-mediated suppression of Interleukin-1/Toll-like receptor (IL-1R/TLR) signaling through simultaneous binding to Pellino-1, an adaptor protein of interleukin-1 receptor associated kinase 1 (IRAK1), via their MH2 domains
SPDATKRSHWCSVAYWEHRTRVGRLYAVYDQSVSIFYDLPQGSGFCLGQLNLEQRSESVRRTRSKIGYGI
LLSKEPDGVWAYNRSEHPIFVNSPTLDIPGSRTLVVRKVPPGYSIKVFDYERSCLLQHTAEPELADGPYD
PNSVRISFAKGWGPCYSRQFITSCPCWLEILLNN
>gnl|CDD|199825 cd10500, MH2_SMAD_7, C-terminal Mad Homology 2 (MH2) domain in SMAD7. The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD7, an inhibitory or antagonistic SMAD (I-SMAD), acts as a negative regulator of signaling mediated by the TGF-beta superfamily of ligands, by blocking TGF-beta type 1 and activin association with the receptor as well as access to SMAD2. SMAD7 enhances muscle differentiation, playing pivotal roles in embryonic development and adult homoeostasis. SMAD7 and SMAD6 act as critical mediators for effective TGF-beta I-mediated suppression of Interleukin-1/Toll-like receptor (IL-1R/TLR) signaling through simultaneous binding to Pellino-1, an adaptor protein of interleukin-1 receptor associated kinase 1(IRAK1), via their MH2 domains. Altered expression of SMAD7 is often associated with cancer, tissue fibrosis and inflammatory diseases
ERGDQSHWCVVAYWEEKTRVGRLYSVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGYGIQL
TREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGF
TVQISFVKGWGQCYTRQFISSCPCWLEVIFN
>gnl|CDD|259849 cd10506, RNAP_IV_RPD1_N, Largest subunit (NRPD1) of higher plant RNA polymerase IV, N-terminal domain. NRPD1 and NRPE1 are the largest subunits of plant DNA-dependent RNA polymerase IV and V that, together with second largest subunits (NRPD2 and NRPE2), form the active site region of the DNA entry and RNA exit channel. Higher plants have five multi-subunit nuclear RNA polymerases; RNAP I, RNAP II and RNAP III, which are essential for viability, plus the two isoforms of the non-essential polymerase RNAP IV and V, which specialize in small RNA-mediated gene silencing pathways. RNAP IV and/or V might be involved in RNA-directed DNA methylation of endogenous repetitive elements, silencing of transgenes, regulation of flowering-time genes, inducible regulation of adjacent gene pairs, and spreading of mobile silencing signals. The subunit compositions of RNAP IV and V reveal that they evolved from RNAP II
STEIDIEKISVSEIKAPNQVTNPRLGLPNESGQCTTCGAKDNKKCEGHFGVIKLPVTIYHPYFISEVAQI
LNKICPGCKSIKQKKKKPPRETLPPDYWDFIPKDGQQEESCVTKNLPILSLAQVKKILKEIDPKLIAKGL
PRQEGLFLKCLPVPPNCHRVTEFTHGFSTGSRLIFDERTRAYKKLVDFIGTANESAASKKSGLKWMKDLL
LGKRSGHSFRSVVVGDPYLELNEIGIPCEIAERLTVSERVSSWNRERLQEYCDLTLLLKGVIGVRRNGRL
VGVRSHNTLQIGDVIHRPLVDGDVVLVNRPPSIHQHSLIALSVKVLPTNSVVSINPLCCSPFRGDFDGDC
LHGYIPQSLQARAELEELVALPKQLISSQSGQNLLSLTQDSLLAAHLMTERGVFLDKAQMQQLQMLCPSQ
LPPPAIIKSPPSNGPLWTGKQLFQMLLPTDLDYSFPSNLVFISDGELISSSGGSSWLRDSEGNLFSILVK
HGPGKALDFLDSAQGLLCEWLSMRGFSVSLSDLYLSSDSYSRQKMIEEISLGLREAEIACNIKQLLVDSR
KDFLSGSGEENDVSSDVERVIYERQKSAALSQASVSAFKQVFRDIQNLVYKYASKDNSLLAMIKAGSKGS
LLKLVQQSGCLGLQLSLVKLSYRIPRQLSCAAWNSQKSPRVIEKDGSECTESYIPYGVVESSFLDGLNPL
ECFVHSITSRDSSFSSNADLPGTLFRKLMFFMRDIYVAYDGTVR
>gnl|CDD|259792 cd10507, Zn-ribbon_RPA12, C-terminal zinc ribbon domain of RPA12 subunit of RNA polymerase I. The C-terminal zinc ribbon domain (C-ribbon) of subunit A12 (Zn-ribbon_RPA12) in RNA polymerase (Pol) I is involved in intrinsic transcript cleavage. Eukaryote genomes are transcribed by three nuclear RNA polymerases (Pol I, II and III) that share some subunits. RPA12 in Pol I, RPB9 in Pol II, RPC11 in Pol III and TFS in archaea are distantly related to each other and to the TFIIS elongation factor of Pol II. RPA12 has two zinc-binding domains separated by a flexible linker
KGATIEEKCPKCGHDEMTYSTLQLRSADEGQTVFYECPKCGHRFSEN
>gnl|CDD|259793 cd10508, Zn-ribbon_RPB9, C-terminal zinc ribbon domain of RPB9 subunit of RNA polymerase II. The C-terminal zinc ribbon domain (C_ribbon) of subunit B9 (Zn-ribbon_RPB9) in RNA polymerase (Pol) II is involved in intrinsic transcript cleavage. Eukaryote genomes are transcribed by three nuclear RNA polymerases (Pol I, II and III) that share some subunits. RPB9 have strong homology to RPA12 of Pol I and RPC11 of Pol III subunits but its intrinsic cleavage activity is weaker for Pol II. Zn-ribbon_RPB9 is homologous to Pol II elongation factor TFIIS domain III. The very weak cleavage activity of Pol II is stimulated by TFIIS. RPB9 has two zinc-binding domains separated by a flexible linker
QDPTLPRTEDHPCPKCGHNEAVFFQSQSRRAEEGMTLFYVCTNCGHRWT
>gnl|CDD|259794 cd10509, Zn-ribbon_RPC11, C-terminal zinc ribbon domain of RPC11 subunit of RNA polymerase III. The C-terminal zinc ribbon domain (C_ribbon) of subunit C11 (C-ribbon_RPC11) in RNA polymerase (Pol) III is required for intrinsic transcript cleavage. RPC11 is also involved in Pol III termination. Eukaryote genomes are transcribed by three nuclear RNA polymerases (Pol I, II and III) that share some subunits. RPC11 have strong homology to RPB9 of Pol II and RPA12 of Pol I. C-ribbon_RPC11 is homologous to Pol II elongation factor TFIIS domain III. C11 has two zinc-binding domains separated by a flexible linker
NVDKTEATCPKCGHNRAYFMQIQTRSADEPMTTFYKCCKCGHQWRE
>gnl|CDD|259795 cd10511, Zn-ribbon_TFS, C-terminal zinc ribbon domain of archaeal Transcription Factor S (TFS). TFS is an archaeal protein that stimulates the intrinsic cleavage activity of archaeal RNA polymerase. TFS C-terminal domain shows sequence similarity to the homologous C-terminal zinc ribbon domain of subunits A12.2, Rpb9, and C11 in eukaryotic RNA Polymerases (Pol) I, II, and III, respectively and domain III of TFIIS. TFS is not a subunit of archaeal RNA polymerase even though its domains arrangement is similar to A12.2, Rpb9, and C1. TFS is a transcription factor with a similar function to eukaryotic TFIIS. TFS has external cleavage induction activity and improves the fidelity of transcription. TFS has two zinc-binding domains
TLPTTKITCPKCGHDEAYWWMVQTRSADEPPTRFYKCTKCGHTWREY
>gnl|CDD|380915 cd10517, SET_SETDB1, SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and similar proteins. SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes
KPYYYICDISYGKEGVPIPCVNEIDNSSPPYVEYSKERIPGKGVNINLDPDFLVGCDCTDGCRDKSKCAC
QQLTIEATAATPGGQINPSAGYQYRRLMEKLPTGVYECNSRCKCDKRCYNRVVQNGLQVRLQVFKTEKKG
WGIRCLDDIPKGSFVCIYAGQILTEDEANEEGLQYGDEYFAELDYIEVVEKLKEGYESDVEEHCYIIDAK
SEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASRYIRAGTELTWDYNYEVGSVPGKVLYCYCGS
SNCRGRLL
>gnl|CDD|380916 cd10518, SET_SETD1-like, SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), histone-lysine N-methyltransferases (KMT2A/KMT2B/KMT2C/KMT2D) and similar proteins. This family includes SET domain-containing protein 1A (SETD1A), 1B (SETD1B), as well as histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B), 2C (KMT2C), 2D (KMT2D). These proteins are histone-lysine N-methyltransferases (EC 2.1.1.43) that specifically methylate 'Lys-4' of histone H3 (H3K4me)
MSKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGGGGTYM
FRIDEDLVIDATKKGNIARFINHSCDPNCYAKIITVDGEKHIVIFAKRDIAPGEELTYDYKFPIEDEEKI
PCLCGAPNCR
>gnl|CDD|380917 cd10519, SET_EZH, SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar proteins. The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both, EZH1 and EZH2, can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively
KRLLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSSYLFNLNDQFVVDATRKG
NKIRFANHSSNPNCYAKVMMVNGDHRIGIFAKRDIEAGEELFFDYGY
>gnl|CDD|380918 cd10520, PR-SET_PRDM17, PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins. PRDM17 (also termed zinc finger protein 408 (ZNF408)) may be involved in transcriptional regulation
ALRSLPPGLALGPSLAQEERLGVWCVGDALQKGTFLGPLEEELESHDLTEGGSPRQEESGQSGDVLACEQ
SSKWMRFACRARSEEESNVAVVRLSGRLHLRVCKDIEPGSELLLWPEENGA
>gnl|CDD|380919 cd10521, SET_SMYD5, SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 5 (SMYD5) and similar proteins. SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions. It plays an important role in chromosome integrity by regulating heterochromatin and repressing endogenous repetitive DNA elements during differentiation. In zebrafish embryogenesis, it plays pivotal roles in both primitive and definitive hematopoiesis
HVEVRFIDAAKGRGLFATRDFKKGDIIFEEKPLVCAQFLWNELHPLNKLQEAWRNMHYPPETASIMLIAR
MIATVKQAKDKDEWLKLFSQFCSATANEEEHIAHKLLGKQFQGQLELLRQLFTEALYEERLSQWFTPEGF
RSLFALVGTNGQGIGTSSLSVWVHNCDALELPEQEREELDAFIDQLYVDIEKESGEFLNCEGSGLYLLQS
CCNHSCVPNAEITFPENNFTLSLKALRDIQEGEEICISYLDECQRERSRHSRQKILRENYLFICNCPKCE
AQ
>gnl|CDD|380920 cd10522, SET_LegAS4-like, SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and similar proteins. LegAS4 is a type IV secretion system effector of Legionella pneumophila. It contains a SET domain that is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. It also contains an ankyrin repeat domain of unknown function at its C-terminal region
KVDISMIPNLSHNGLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDSVYHYDPLYPFDLNGDILVIDAGKK
GNLTRFINHSDQPNLELIVRTLKGEQHIGFVAIRDIKPGEELFISYGPKYWK
>gnl|CDD|380921 cd10523, SET_SETDB2, SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) and similar proteins. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis
FSFNTYVQLDRNPQDQQQLVDDFDISNGAFVDSCDCTDGCIDILKCACLQLTARAFSKSESSPSKGGRGY
KYKRLQEPIPSGLYECNVSCKCNRMLCQNRVVQHGLQVRLQVFKTEKKGWGVRCLDDIDKGTFVCIYAGR
VLSRARSPTEPLPPKLELPSENEVEVVTSWLILSKKRKLRENVCFLDASKEGNVGRFLNHSCCPNLFVQN
VFVDTHDKNFPWVAFFTNRVVKAGTELTWDYSYDAGTSPEQEIPCLCGVNKCQKKI
>gnl|CDD|380922 cd10524, SET_Suv4-20-like, SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of variegation 4-20 (Suv4-20) and similar proteins. Suv4-20 (also termed Su(var)4-20) is a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-20' of histone H4. It acts as a dominant suppressor of position-effect variegation. The family also includes Suv4-20 homologs, lysine N-methyltransferase 5B (KMT5B) and lysine N-methyltransferase 5C (KMT5C). Both KMT5B (also termed lysine-specific methyltransferase 5B, or suppressor of variegation 4-20 homolog 1, or Su(var)4-20 homolog 1, or Suv4-20h1) and KMT5C (also termed lysine-specific methyltransferase 5C, or suppressor of variegation 4-20 homolog 2, or Su(var)4-20 homolog 2, or Suv4-20h2) are histone methyltransferases that specifically trimethylate 'Lys-20' of histone H4 (H4K20me3). They play central roles in the establishment of constitutive heterochromatin in pericentric heterochromatin regions
DSGFTICPCNRYSLENHYGAKIIATKPIKKGEKIHELCGCIAELSEEEEALLRPGGNDFSVMYSSRKKCS
QLWLGPAAFINHDCRPNCKFVPTGKSTACVKVLRDIEPGEEITVYYGDNYFGENNEECECETCERRGRGA
F
>gnl|CDD|380923 cd10525, SET_SUV39H1, SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homolog 1 (SUV39H1) and similar proteins. SUV39H1 (EC 2.1.1.43; also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A (KMT1A), position-effect variegation 3-9 homolog (SUV39H), or Su(var)3-9 homolog 1) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. It mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions
RDFVYINEYKVGEGVTLNQVAVGCECQDCLSQPVGGCCPGASKHRFAYNEQGQVKVRPGLPIYECNSRCR
CGPDCPNRVVQKGIQYDLCIFRTDNGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATY
LFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDYNM
QVDPVDAESTKMDSNFGLAGLPGSPKKRVRIECKCGVRSCRKYLF
>gnl|CDD|380924 cd10526, SET_SMYD1, SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 (SMYD1) and similar proteins. SMYD1 (EC 2.1.1.43), also termed BOP, is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD1 plays a critical role in cardiomyocyte differentiation, cardiac morphogenesis and myofibril organization, as well as in the regulation of endothelial cells (ECs). It is expressed in vascular endothelial cells, it has beenshown that knockdown of SMYD1 in endothelial cells impairs EC migration and tube formation
EGVEVFTSEGKGRGLKATKEFWAGDVIFAEPPYAAVVFGKAPNENIRLAARILWRIEREGGGLKEGELVS
IEDLQDHLEDFSEEEKKDLREDVHSFLDYWPYQSQQFSMEYISHIFGVINCNGFTLSDQRGLQAVGVGIF
PNLCLVNHDCWPNCTVIFNNGRIELRALGKISEGDELTVSYIDFLNTSEDRKEQLKKQYYFDCTCEHCTK
>gnl|CDD|380925 cd10527, SET_LSMT, SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins. Rubisco LSMT is a non-histone protein methyl transferase responsible for the trimethylation of lysine14 in the large subunit of Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase). The family also includes SET domain-containing proteins, SETD3, SETD4 and SETD6, which belong to methyltransferase class VII that represents classical non-histone SET domain methyltransferases. Members in this family contain a SET domain and a C-terminal RubisCO LSMT substrate-binding (Rubis-subs-bind) domain
GVELAESPDGGRGLFATRDIAAGEVLLSVPRSLLLTVETARESPLGGAALALLELDPELSWDVALALFLL
YERARGPDSFWAPYLDSLPRPFEDTPLFWSEEELDALQGTPLLEAAAAQRRRLREEYEALVEALPEALPA
EPGEAFTLEEFLWALALVLSRAFSLPVPDGGGGLALVPLADMLNHSPDAPNVRYEYDEDEGSFVLVATRD
IAAGEEVFISYGPKSNDELLLYYGFV
>gnl|CDD|380926 cd10528, SET_SETD8, SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins. SETD8 (EC 2.1.1.43; also termed N-lysine methyltransferase KMT5A, H4-K20-HMTase KMT5A, lysine N-methyltransferase 5A, lysine-specific methylase 5A, PR/SET domain-containing protein 07, PR-Set7 or PR/SET07) is a nucleosomal histone-lysine N-methyltransferase that specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). It plays a central role in the silencing of euchromatic genes
KEKKKEIEELILSGKEEGLKVIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREALYAKDPSTG
CYMYYFQYKGKTYCVDATKESGRLGRLINHSKKKPNLKTKLLVIDGVPHLILVAKRDIKPGEELLYDYGD
R
>gnl|CDD|380927 cd10529, SET_SETD5-like, SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins. SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. KMT2E (also termed inactive lysine N-methyltransferase 2E or myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. The family also includes Saccharomyces cerevisiae SET domain-containing proteins, SET3 and SET4, and Schizosaccharomyces pombe SET3. Most of these family members contain a post-SET domain which harbors a zinc-binding site
RKLTSRTVEKVVGKNRKGLVATEDISPGEPILEYKGEVSLRSEFKEDNGFFKRPSPFVFFYDGFEGLPLC
VDARKYGNEARFIRRSCRPNAELRHVVVSNGELRLFIFALKDIRKGTEITIPFDYDY
>gnl|CDD|380928 cd10530, SET_SETD7, SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins. SETD7 (EC 2.1.1.43; also termed histone H3-K4 methyltransferase SETD7, H3-K4-HMTase SETD7, lysine N-methyltransferase 7 (KMT7) or SET7/9) is a histone-lysine N-methyltransferase that specifically monomethylates 'Lys-4' of histone H3. It plays a central role in the transcriptional activation of genes such as collagenase or insulin. Set7/9 also methylates non-histone proteins, including estrogen receptor alpha (ERa), suggesting it has a role in diverse biological processes. ERa methylation by Set7/9 stabilizes ERa and activates its transcriptional activities, which are involved in the carcinogenesis of breast cancer. In a high-throughput screen, treatment of human breast cancer cells (MCF7 cells) with cyproheptadine, a Set7/9 inhibitor, decreased the expression and transcriptional activity of ERa, thereby inhibiting estrogen-dependent cell growth
PDPYESERVYVAESLIPSAGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNGNTISLDEETVIDV
PEPYNSVSKYCASLGHKANHSFTPNCIYDPFVHPRFGPIKCIRTLRAVEAGEELTVAYGY
>gnl|CDD|380929 cd10531, SET_SETD2-like, SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2), ASH1-like protein (ASH1L) and similar proteins. This family includes SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2) and ASH1-like protein (ASH1L), which function as histone-lysine N-methyltransferases. SETD2 specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. NSD2 shows histone H3 'Lys-27' (H3K27me) methyltransferase activity. ASH1L specifically methylates 'Lys-36' of histone H3 (H3K36me). The family also includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins
KLELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDEYEELGKSNFYILSLSDDVVIDATRK
GNLSRFINHSCEPNCETQKWIVNGEYRIGIFALRDIPAGEELTFDYNFVNYNEAKQVCLCGAQNCR
>gnl|CDD|380930 cd10532, SET_SUV39H2, SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homolog 2 (SUV39H2) and similar proteins. SUV39H2 (EC 2.1.1.43; also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B (KMT1B), or Su(var)3-9 homolog 2) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. It mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions
IDFYYINEYKPAPGINLDNEATVGCDCSDCFFGKCCPAEAGVLFAYNEHGQLKIPPGTPIYECNSRCKCG
PDCPNRVVQKGTQYSLCIFRTSNGRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQFYDSKGITYLF
DLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTIKAGEELTFDYQMKG
SGDLSSDSIDNSPAKKRVRTVCKCGAVTCRGYL
>gnl|CDD|380931 cd10533, SET_EHMT2, SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 2 (EHMT2) and similar proteins. EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C (KMT1C), or protein G9a) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin
EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFEC
NQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLF
DLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDR
FWDIKSKYFTCQCGSEKCKHSAEAIALEQ
>gnl|CDD|380932 cd10534, PR-SET_PRDM-like, PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins. PRDM family of proteins is defined based on the conserved N-terminal PR domain, which is closely related to the Su(var)3-9, enhancer of zeste, and trithorax (SET) domains of histone methyltransferases, and is specifically called PR-SET domain. The family consists of 17 members in primates. PRDMs play diverse roles in cell-cycle regulation, differentiation, and meiotic recombination. The family also contains zinc finger protein ZFPM1 and ZFPM2. ZFPM1 (also termed friend of GATA protein 1, FOG-1, friend of GATA 1, zinc finger protein 89A, or zinc finger protein multitype 1) functions as a transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. ZFPM2 (also termed friend of GATA protein 2, FOG-2, friend of GATA 2, zinc finger protein 89B, or zinc finger protein multitype 2) functions as a transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis
LPAGLELVLSSIPEGGLGVFARRTIPAGTRFGPLEGVVNWMRFVRPARNEEEQNLVAYQHGGQIYFRTTR
DIPPGEELLVWYS
>gnl|CDD|380933 cd10535, SET_EHMT1, SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 1 (EHMT1) and similar proteins. EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, or lysine N-methyltransferase 1D (KMT1D)) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin
SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFEC
NHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLF
DLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGER
FWDIKGKLFSCRCGSPKCRHS
>gnl|CDD|380934 cd10536, SET_SMYD4, SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 4 (SMYD4) and similar proteins. SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. In zebrafish, SMYD4 is ubiquitously expressed in early embryos and becomes enriched in the developing heart; mutants show a strong defect in cardiomyocyte proliferation, which lead to a severe cardiac malformation
IPGASSAVSLRYSEEKGRFLVATRDIKAGEVLIVEKPYASVLLPYSSDYRSVYNLVTHTENRSPEDLFQR
ALTAVFLAKCLQLSGYFLLWEASTELNGEEPESILGGLLLRHLQQLQCNAHAITELQTTSSGSQVDTSKQ
VRIATAIYPTLSLLNHSCDPNTIRSFYGNTIVVRATRPIKKGEEITICYGPHFSRMKRSERQRLLKEQYF
FDCSCEAC
>gnl|CDD|380935 cd10537, SET_SETD9, SET domain found in SET domain-containing protein 9 (SETD9) and similar proteins. SETD9 is an uncharacterized protein that belongs to the class V-like SAM-binding methyltransferase superfamily
VLGFTLHRKPSSIPDAGTGVFVEKGRVPPGTVVALYPGTVYLPYEPILFQSIGNPFLFRRYDGIIIDGNP
LALGHYVNHPPKGTPPNVAYQEYDFPEDFPEELRRYIPNVYYSPDQVFNMTRGKRPLRGVVLVATRDIKD
GEELFSNYRT
>gnl|CDD|380936 cd10538, SET_SETDB-like, SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2, and similar proteins. The family includes SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2. SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis. SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. This family also includes the pre-SET domain, which is found in a number of histone methyltransferases (HMTase), N-terminal to the SET domain. Pre-SET domain is a zinc binding motif which contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilizing SET domains. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site
PSFTYIKDNIVGKNVQPFSNIIDSVGCKCKDDCLDSKCACAAESDGIFAYTKNGLLRLNNSPPPIFECNS
KCSCDDDCKNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIYDKSGG
SYLFDLDEFSDSDGDGEELCVDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRIALFATRDILPGE
ELTFDYG
>gnl|CDD|380937 cd10539, SET_ATXR5_6-like, SET domain found in fungal protein lysine methyltransferase SET5 and similar protein. The family includes Arabidopsis thaliana ATXR5 and ATXR6. Both ATXR5 (also termed protein SET DOMAIN GROUP 15, or TRX-related protein 5) and ATXR6 (also termed protein SET DOMAIN GROUP 34, or TRX-related protein 6) function as histone methyltransferase that specifically monomethylates 'Lys-37' of histone H3 (H3K27me1). They are required for chromatin structure and gene silencing
GECPPLLVVFDPREGFTVEADGFIKDLTIIAEYTGDVDYIRNREFDDNDSIMTLLLAGDPSKSLVICPDK
RGNIARFISGINNHTKDGKKKQNCKCVRYSINGEARVLLVATRDIAKGERLYYDYNGYEHEYPTEHFV
>gnl|CDD|380938 cd10540, SET_SpSet7-like, SET domain found in Schizossacharomyces pombe Set7 and similar proteins. Schizosaccharomyces pombe Set7 is a novel histone-lysine N-methyltransferase. The family also includes a viral histone H3 lysine 27 methyltransferase from Paramecium bursaria Chlorella virus 1 (PBCV-1)
RLEVKPSTLKGRGVFATRPIKKGEVIEEAPVIVLPKEEYQHLCKTVLDHYVFSWGDGCLALALGYGSMFN
HSYTPNAEYEIDFENQTIVFYALRDIEAGEELTINYGDDLWD
>gnl|CDD|380939 cd10541, SET_SETDB, SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), SET domain bifurcated 2 (SETDB2), and similar proteins. SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis
KPFYYIPDISYGKFLVGCDCTDGCRDKSKCACHQLTIQATACTPGGQDNPTAGYQYKRLEECLPTGVYEC
NKLCKCDPNMCQNRLVQHGLQVRLQLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADKEGLEMGD
EYFANLDHIEESCYIIDAKLEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASKRIKAGTELTWD
YNYEVGSVEGKELLCCCGSNECRGRL
>gnl|CDD|380940 cd10542, SET_SUV39H, SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homologs, SUV39H1, SUV39H2 and similar proteins. This family includes SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. Also included are Schizosaccharomyces pombe H3K9 methyltransferase Clr4 (SUV39H homolog) and Neurospora crassa DIM-5, both of which also methylate 'Lys-9' of histone H3
PNFQYINDYIPGDGVKIPEDFLVGCECTEDCHNNNPTCCPAESGVKFAYDKQGRLRLPPGTPIYECNSRC
KCGPDCPNRVVQRGRKVPLCIFRTSNGRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANGRT
YLFDLDYNDDDCEYTVDAAYYGNISHFINHSCDPNLAVYAVWINHLDPRLPRIAFFAKRDIKAGEELTFD
YLMTGTGGSSESTIPKPKDVRVPCLCGSKNCRKYL
>gnl|CDD|380941 cd10543, SET_EHMT, SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase EHMT1, EHMT2 and similar proteins. This family includes EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin
PDFLYVTENCETSPLNIDRNITSLQTCSCRDDCSSDNCVCGRLSVRCWYDKEGRLLPDFNKLDPPLIFEC
NRACSCWRNCRNRVVQNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSREDDSYLF
DLDNKDGETYCIDARRYGNISRFINHLCEPNLIPVRVFVEHQDLRFPRIAFFASRDIKAGEELGFDYGEK
FWRIKGKYFTCRCGSPKCKYS
>gnl|CDD|380942 cd10544, SET_SETMAR, SET domain (including pre-SET and post-SET domains) found in SET domain and mariner transposase fusion protein (SETMAR) and similar proteins. SETMAR (also termed metnase) is a DNA-binding protein that is indirectly recruited to sites of DNA damage through protein-protein interactions. It has a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. SETMAR also acts as a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3. It specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining
PDFQYTPENVPGPGADTDPNEITFPGCDCKTSSCEPETCSCLRKYGPNYDDDGCLLDFDGKYSGPVFECN
SMCKCSESCQNRVVQNGLQFKLQVFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRTKSQTKGD
MNYIIVLREHLSSGKVLETFVDPTYIGNIGRFLNHSCEPNLFMVPVRVDSMVPKLALFAARDIVAGEELS
FDYSGEFSNSVESVTLARQDESKSRKPCLCGAENCRGFLPFDES
>gnl|CDD|380943 cd10545, SET_AtSUVH-like, SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar proteins. Arabidopsis thaliana SUVH protein (also termed suppressor of variegation 3-9 homolog protein) is a histone-lysine N-methyltransferase that methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. Some family members contain a post-SET domain which binds a Zn2+ ion. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site
SGFTYTVKLIIPPGVSLPVPSTGCDCKNRCTDGASDCACVKKNGGEIPYNFNGRLIRAKPAIYECGPLCK
CPPSCYNRVTQKGLRYRLEVFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADTRSGNDDYLFDIDN
RQTNRGWDGGQRLDVGMSDGERSSAEDEESSEFTIDAGSFGNVARFINHSCSPNLFVQCVLYDHNDLRLP
RVMLFAADNIPPLQELTYDYGY
>gnl|CDD|240598 cd10546, VKOR, Vitamin K epoxide reductase (VKOR) family. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. This family includes enzymes that are present in vertebrates, Drosophila, plants, bacteria, and archaea. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some plant and bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade. Warfarin, a widely used oral anticoagulant used in medicine as well as rodenticides, inhibits the activity of VKOR, resulting in decreased levels of reduced vitamin K, which is required for the function of several clotting factors. However, anticoagulation effect of warfarin is significantly associated with polymorphism of certain genes, including VKORC1. Interestingly, in rodents, an adaptive trait appears to have evolved convergently by selection on new or standing genetic polymorphisms in VKORC1 as well as by adaptive introgressive hybridization between species, likely brought about by human-mediated dispersal
LILLLLAAIGLLVSLYLTYYELTEGAVAGCDAGPSSSCDLVLTSRWSRIFGVPLSLLGALYYLVVLGLLL
SPPAGARLRWTALAAATFAGLGAAAWLIYLQLFVLGAFCPYCLVAHAAGLALLALT
>gnl|CDD|380415 cd10547, cupin_BacB_C, Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain. This model represents the C-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold
PTRDKITGLPCQFFVGSWFEIMISQIPPGGKMPLHQHRGEQIGIILNGKYDMTVGGEEQELGYGKIYYAP
PNVSHSGYNDSDETATLINIFI
>gnl|CDD|380416 cd10548, cupin_CDO, cysteine dioxygenase, cupin domain. This family contains cysteine dioxygenase (CDO; EC 1.13.11.20), which catalyzes the conversion of cysteine to cysteine sulfinic acid, the first step in the biosynthesis of essential oxidized cysteine metabolites such as sulfate, hypotaurine, and taurine. CDO also plays an important role in the regulation of intracellular cysteine levels in mammals; CDO expression is altered in cancer cells, and abnormal or deficient CDO activity has been linked to Parkinson's disease, Alzheimer's disease, and rheumatoid arthritis. CDO is an iron-dependent thiol dioxygenase that uses molecular oxygen to oxidize the sulfhydryl group of cysteine to generate cysteine sulfinic acid. The CDO active site contains an amino acid-derived cofactor. These enzymes are found in prokaryotes as well as eukaryotes and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization
YTRNLLYRDPDFELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGSLSGEETLEETPGDV
TYINPDGGIHRVENPSDEPAVSLHLYSPPL
>gnl|CDD|319871 cd10549, MtMvhB_like, Uncharacterized polyferredoxin-like protein. This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction
LKYDPEKCIGCGICVKACPTDAIELGPNGAIARGPEIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKE
KEAEIDEEKCIGCGLCVKVCPVDAITLEDELEIVIDKEKCIGCGICAEVCPVNAIKLV
>gnl|CDD|319872 cd10550, DMSOR_beta_like, uncharacterized subfamily of DMSO Reductase beta subunit family. This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system
LVVDPEKCTGCRTCELACSLKHEGVFNPSLSRIRVVRFEPEGLDVPVVCRQCEDAPCVEACPVGAISRDE
ETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLCGGDPACVKVCPTGALEFV
>gnl|CDD|319873 cd10551, PsrB, polysulfide reductase beta (PsrB) subunit. This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane
MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVCPTGAT
YKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPHEFGEVPVRPKGVVEKCTFCYHRLDEGLLPACV
EACPTGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYYI
>gnl|CDD|319874 cd10552, TH_beta_N, N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit. This family includes the beta subunit of pyrogallol-phloroglucinol transhydroxylase (TH), a cytoplasmic molybdenum (Mo) enzyme from anaerobic microorganisms like Pelobacter acidigallici and Desulfitobacterium hafniense which catalyzes the conversion of pyrogallol to phloroglucinol, an important building block of plant polymers. TH belongs to the DMSO reductase (DMSOR) family; it is a heterodimer consisting of a large alpha catalytic subunit and a small beta FeS subunit. The beta subunit has two domains with the N-terminal domain containing three [4Fe-4S] centers and a seven-stranded, mainly antiparallel beta-barrel domain. In the anaerobic bacterium Pelobacter acidigallici, gallic acid, pyrogallol, phloroglucinol, or phloroglucinol carboxylic acid are fermented to three molecules of acetate (plus CO2), and TH is the key enzyme in the fermentation pathway, which converts pyrogallol to phloroglucinol in the absence of O2
LVIDVAKCNGCYNCFLACKDEHVGNDWPGYAAPQPRHGHFWMRILRRERGQYPKVDVAYLPVPCNHCDNA
PCIKAAKDGAVYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGWKEPRCV
QACPTGALRFGKLEDEEMAAKAAEEGLEVLHPELGTKPRVYYKNLP
>gnl|CDD|319875 cd10553, PhsB_like, uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB. This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system
SKYYLYHDSKRCIGCLACEVHCKVKNNLPVGPRLCRIFAVGPKMVGGKPRLKFVYMSCFHCENPWCVKAC
PTGAMQKREKDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLKPACVTGCTTH
ALSFVR
>gnl|CDD|319876 cd10554, HycB_like, HycB, HydN and similar proteins. This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation
FVIADPDKCIGCRTCEVACAAAHSGKGIFEAGTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPV
GAISQEDGVVQVDEERCIGCKLCVLACPFGAIEMAPTTVPGVDWERGPRAVAVKCDLCAGREGGPACVEA
CPTKALTLV
>gnl|CDD|319877 cd10555, EBDH_beta, beta subunit of ethylbenzene-dehydrogenase (EBDH). This subfamily includes ethylbenzene dehydrogenase (EBDH, EC 1.17.99.2), a member of the DMSO reductase family. EBDH oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. It is a heterotrimer, with the alpha subunit containing the catalytic center with a molybdenum held by two molybdopterin-guanine dinucleotides, the beta subunit containing four iron-sulfur clusters (the electron transfer subunit) and the gamma subunit containing a methionine and a lysine as axial heme ligands. During catalysis, electrons produced by substrate oxidation are transferred to a heme in the gamma subunit and then presumably to a separate cytochrome involved in nitrate respiration
SKRQLAMVMDLNKCIGCQTCTVACKTLWTNRNGREYMYWNNVETQPGKGYPKNWEKKGGGFKDKGELKPG
IIPTLEDYGVPWEYNHEEELFEGKGGRVRPSPKGDPTWGPNWDEDQGAGEYPNSYYFYLPRICNHCTNPA
CLAACPRKAIYKREEDGIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIFCYPRIEKGVAPACAR
QCVGRIRFVGYLDDEESPVYKLVKKWKVALPLHPEYGTEPNVFYVPPLSPPKLGDDGEPTDEPRIPLEYL
ESLFGPRVKQALDTLKAEREKKRAGGESELMDILIA
>gnl|CDD|319878 cd10556, SER_beta, Beta subunit of selenate reductase. This subfamily includes beta FeS subunit of selenate reductase (SER), a member of the DMSO reductase family. SER catalyzes the reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor. The enzyme comprises three subunits SerABC, forming a heterotrimer, with the catalytic component (alpha-subunit), iron-sulfur protein (beta-subunit) and monomeric b-type heme-containing gamma subunit. Beta subunit contains coordinating one [3Fe-4S] cluster and three [4Fe-4S] clusters and functions as electron carrier
YPYEESRPDKQFAMVFDTNKCIACQTCTMACKSTWTSGKGQEYMWWNNVETKPYGGYPLGWDVRLLDEEG
GQTWAEGGVYEGKTIFEAAAAGEQVLGYRPEDEDWRYPNIGEDEVNGERTPDTGSSLPPHPIWFFYLPRI
CNHCTYPACLAACPRKAIYKREEDGIVLIDQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRIEE
GDQTQCVSACIGKIRLQGFINTPPDARWADDRDNPIDFLVHIKKVALPLYPQFGTEPNVYYIPPIHVPRE
YLRQMFG
>gnl|CDD|319879 cd10557, NarH_beta-like, beta subunit of nitrate reductase A (NarH) and similar proteins. This subfamily includes nitrate reductase A, a member of the DMSO reductase family. The respiratory nitrate reductase complex (NarGHI) from E. coli is a heterotrimer, with the catalytic subunit (NarG) with a molybdo-bis (molybdopterin guanine dinucleotide) cofactor and an [Fe-S] cluster, the electron transfer subunit (NarH) with four [Fe-S] clusters, and the integral membrane subunit (NarI) with two b-type hemes. Nitrate reductase A often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Electron transfer from formate to nitrate is coupled to proton translocation across the cytoplasmic membrane generating proton motive force by a redox loop mechanism. Demethylmenaquinol (DMKH2) has been shown to be a good substrate for NarGHI in nitrate respiration in E. coli
IRAQISMVMNLDKCIGCHTCSVTCKNVWTNRKGAEYMWWNNVETKPGIGYPKQWEDQEKYRGGWVLKGGK
LKLKRGGKIQKLANIFYNPKLPEIDDYYEPWTYDYENLFTAPEGDDQPVARPKSLITGEPMDIEWGPNWD
DDLAGSPEYAAEDPNLKKLQEEIYLEFENTFMFYLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQD
RCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLEAGQPTVCSETCVGRIRYLGVLLYDADRILEAAA
VVPEKDLVEAQLDIILDPNDPEVIAAAKANGIPDNWIEAAQRSPVYKMVKEWKIALPLHPEYRTLPMVFY
VPPLSPVVAAVEA
>gnl|CDD|319880 cd10558, FDH-N, The beta FeS subunit of formate dehydrogenase-N (FDH-N). This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups
AKLIDVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQNPADLSPETWTLMKFREVEDNGKLEWLIRKDGC
MHCADPGCLKACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVG
LEPACVKTCPTGALHFGTKEDMLALAEKRVAALKERGYTNAGLYDPKGVGGTHVMYVLHHADKPEGYP
>gnl|CDD|319881 cd10559, W-FDH, tungsten-containing formate dehydrogenase, small subunit. This subfamily contains beta subunit of Tungsten-containing formate dehydrogenase (W-FDH), a member of the DMSO reductase family. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons
SFLIDTTRCTACRGCQVACKQWNQLPAEQTKNTGSHQNPPDLSANTYKLVRFNEVRNENGKPDWLFFPDQ
CRHCVTPPCKDAADMVPGAVIQDEATGAVVFTEKTAELDFDDVLSACPYNIPRKNEATGRIVKCDMCIDR
VSNGLQPACVKACPTGAMNFGDRDEMLAMASKRLEELKKRYPKANLYDPDDVRVIWLLAE
>gnl|CDD|319882 cd10560, FDH-O_like, beta subunit of formate dehydrogenase O (FDH-O) and similar proteins. This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N
GFFTDTSICIGCKACEVACKQWNQLPADGYDFSGMSYDNTGDLSASTWRHVKFIERPTEDGPANEGGDLQ
WLFMSDVCKHCTDAGCLEACPTGAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLC
YDRLKDGLEPACAKACPTGSIQFGPLEELRERARARVEQLHEQGVVEAYLYGADPTEGYGGLNAFFLLLD
KPEVYGLPADPLLPT
>gnl|CDD|319883 cd10561, HybA_like, the FeS subunit of hydrogenase 2. This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction
GVLYDTTRCIGCRACEVACKEWNGLPAEDTAFGPGWDNPRDLSAKTYTVIKRYEVETGGKGFVFVKRQCM
HCLDPACVSACPVGALRKTPEGPVTYDEDKCIGCRYCMVACPFNIPKYEWDSANPKIRKCTMCYDRLKEG
KQPACVEACPTGALLFGKREELLAEAKRRIAANPGRYVDHVYGEKEAGGTSVLYLS
>gnl|CDD|319884 cd10562, FDH_b_like, uncharacterized subfamily of beta subunit of formate dehydrogenase. This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons
MLVDTSKCTACRGCQVACKQWNQLPAEKTPFTGSYQNPPDLTPNTWTLIRFYEHEEDNGGIRWLFRKRQC
MHCTDAACVKVCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGM
QPACVKTCPTGALTFGDRDEL
>gnl|CDD|319885 cd10563, CooF_like, CooF, iron-sulfur subunit of carbon monoxide dehydrogenase. This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction
RIFIDEEKCLGCKLCEVACAVAHSKSKDLIKAKLEKERPRPRIRVEESGGRSFPLQCRHCDEPPCVKACM
SGAMHKDPETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDRETPACVEACPTGALVLE
>gnl|CDD|319886 cd10564, NapF_like, NapF, iron-sulfur subunit of periplasmic nitrate reductase. This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system
RPPWAVDEALFLDLCTRCGDCVEACPEGIIVRGDGGFPELDFSRGECTFCGACAEACPEGALDPAREAPW
PLRAEIGDSCLALQGVECRSCQDACPTQAIRFRPRLGGIALPELDADACTGCGACVSVCPVGAITLTPL
>gnl|CDD|349488 cd10566, MDM2_like, p53-binding domain found in E3 ubiquitin-protein ligase MDM2, MDM4, and similar proteins. MDM2 (also termed HDM2) and MDM4 (also termed MDMX or HDMX) are the primary negative regulators of p53 tumor suppressor. They have non-redundant roles in the regulation of p53. MDM2 mainly functions to control p53 stability, while MDM4 controls p53 transcriptional activity. Both MDM2 and MDM4 contain an N-terminal p53-binding domain, a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region, and a C-terminal RING domain. Mdm2 can form homo-oligomers through its RING domain and display E3 ubiquitin ligase activity that catalyzes the attachment of ubiquitin to p53 as an essential step in the regulation of its level in cells. Despite its RING domain and structural similarity with MDM2, MDM4 does not homo-oligomerize and lacks ubiquitin-ligase function, but inhibits the transcriptional activity of p53. In addition, both their RING domains are responsible for the hetero-oligomerization, which is crucial for the suppression of p53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. Moreover, MDM2 and MDM4 can be phosphorylated and destabilized in response to DNA damage stress. In response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through the interaction with ribosomal proteins L5, L11 and L23. However, MDM4 is not bound to ribosomal proteins, suggesting its different response to regulation by small basic proteins such as ribosomal proteins and ARF
PKPELLKLLKSVGAKGEVFTRKEVLHYLKQYISSRKLYDPLDPRIVYCKNDPLGKVFGVQSFTIKDVLGL
LAKNL
>gnl|CDD|349489 cd10567, SWIB-MDM2_like, SWIB/MDM2 domain found in SWIB/MDM2 homologous proteins. This family includes Schizosaccharomyces pombe upstream activation factor subunit spp27, Saccharomyces cerevisiae upstream activation factor subunit UAF30, Chlamydiae DNA topoisomerase/SWIB domain fusion protein, Arabidopsis thaliana zinc finger CCCH domain-containing proteins, AtC3H19 and AtC3H44, and similar proteins. S. pombe spp27, also termed upstream activation factor 27 KDa subunit (p27), or upstream activation factor 30 KDa subunit (p30), or upstream activation factor subunit uaf30, is a component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. S. cerevisiae UAF30, also termed upstream activation factor 30 KDa subunit (p30), is a non-essential component of the UAF. It seems to play a role in silencing transcription by RNA polymerase II. The SWIB domain found in Chlamydiae DNA topoisomerase may play a role in chromatin condensation-decondensation, which is characteristic of the chlamydial developmental cycle and not found in any other types of bacteria. AtC3H19, also termed protein needed for RDR2-independent DNA methylation (NERD), is a plant-specific GW repeat- and PHD finger-containing protein that plays a central role in integrating RNA silencing and chromatin signals in 21 nt small-interfering RNA (siRNA)-dependent DNA methylation on the cytosine pathway, leading to transcriptional gene silencing of specific sequences. This family also includes many uncharacterized proteins containing two copies of SWIB/MDM2 domain
YKLSPELAAFLGVSELSRTEVVKKLWAYIKENNLQDPKNKREILCDEKLKKVFGKDEVVMFEMNKLLSKH
L
>gnl|CDD|349490 cd10568, SWIB_like, SWIB domain found in the 60 kda subunit of the ATP-dependent SWI/SNF chromatin-remodeling complexes and similar proteins. SWIB domain is a conserved region found within proteins in the SWI/SNF family of complexes. SWI/SNF complex proteins display helicase and ATPase activities and are thought to regulate transcription of certain genes by altering the chromatin structure around those genes. The mammalian complexes are made up of 9-12 proteins called BAFs (BRG1-associated factors), among which the BAF60 subunit serves as a key link between the core complexes and specific transcriptional factors. The BAF60 subunit have at least three members: BAF60a, which is ubiquitous, BAF60b and BAF60c, which are expressed in muscle and pancreatic tissues, respectively. The family also includes Saccharomyces cerevisiae transcription regulatory protein SNF12 and remodel the structure of chromatin complex subunit 6 (RSC6), and Schizosaccharomyces pombe SWI/SNF and RSC complexes subunit SSR3. SNF12, also termed 73-kDa subunit of the SWI/SNF transcriptional regulatory complex, or SWI/SNF complex component SWP73, is involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). RSC6 and SSR3 are components of the RSC, which is involved in transcription regulation and nucleosome positioning. RSC6 is essential for mitotic growth and suppresses formamide sensitivity of the RSC8 mutants
LSPALAQLLGIKEGTRPNIIYALWQYIKLNKLQDPEDRRLINCDEALKQLFGVERFKFSELPELLNPHL
>gnl|CDD|269973 cd10569, FERM_C_Talin, FERM domain C-lobe/F3 of Talin. Talin (also called filopodin) plays an important role in initiating actin filament growth in motile cell protrusions. It is responsible for linking the cytoplasmic domains of integrins to the actin-based cytoskeleton, and is involved in vinculin, integrin and actin interactions. At the leading edge of motile cells, talin colocalises with the hyaluronan receptor layilin in transient adhesions, some of which become more stable focal adhesions (FA). During this maturation process, layilin is replaced with integrins, where localized production of PI(4,5)P(2) by type 1 phosphatidyl inositol phosphate kinase type 1gamma (PIPK1gamma) is thought to play a role in FA assembly. Talins are composed of a N-terminal region FERM domain which us made up of 3 subdomains (N, alpha-, and C-lobe; or- A-lobe, B-lobe, and C-lobe; or F1, F2, and F3) connected by short linkers, a talin rod which binds vinculin, and a conserved C-terminal region with actin- and integrin-binding sites. There are 2 additional actin-binding domains, one in the talin rod and the other in the FERM domain. Both the F2 and F3 FERM subdomains contribute to F-actin binding. Subdomain F3 of the FERM domain contains overlapping binding sites for integrin cytoplasmic domains and for the type 1 gamma isoform of PIP-kinase (phosphatidylinositol 4-phosphate 5-kinase). The FERM domain has a cloverleaf tripart structure . F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GVTFFLVKEKMKGKNKLVPRLLGITKESVLRLDEETKEVLKVWPLTTIKRWAASPKSFTLDFGDYSENYY
SVQTTEGEQISQLISGYIDIIL
>gnl|CDD|275393 cd10570, PH-GRAM, Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold
IEKLGVRFCCALRPRKLPLEGTLYLSTYRLIFSSKADGDETKLVIPLVDITDVEKIAGASFLPSGLIITC
KDFRTIKFSFDSEDEAVKVIARVL
>gnl|CDD|269975 cd10571, PH_beta_spectrin, Beta-spectrin pleckstrin homology (PH) domain. Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MEGFLERKHEWESGGKKASNRSWKNVYTVLRGQELSFYKDQKAAKSGITYAAEPPLNLYNAVCEVASDYT
KKKHVFRLKLSDGAEFLFQAKDEEEMNQWVKKISFA
>gnl|CDD|269976 cd10572, PH_RhoGEF3_XPLN, Rho guanine nucleotide exchange factor 3 Pleckstrin homology (PH) domain. RhoGEF3/XPLN, a Rho family GEF, preferentially stimulates guanine nucleotide exchange on RhoA and RhoB, but not RhoC, RhoG, Rac1, or Cdc42 in vitro. It also possesses transforming activity. RhoGEF3/XPLN contains a tandem Dbl homology and PH domain, but lacks homology with other known functional domains or motifs. It is expressed in the brain, skeletal muscle, heart, kidney, platelets, and macrophage and neuronal cell lines. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RLEYLDEKQRDPLIDSSRLLLCHGELKNNRGTKLHVFLFEEVLVLTRPVTRNEQLCYQVYRQPIPVADLV
LEDLPDGEVRLGGSFRGAFSNNERAKNFFRVSFTDRSLGQSHTLQANDEFDKQQWLNCIRQAV
>gnl|CDD|269977 cd10573, PH_DAPP1, Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain. DAPP1 (also known as PHISH/3' phosphoinositide-interacting SH2 domain-containing protein or Bam32) plays a role in B-cell activation and has potential roles in T-cell and mast cell function. DAPP1 promotes B cell receptor (BCR) induced activation of Rho GTPases Rac1 and Cdc42, which feed into mitogen-activated protein kinases (MAPK) activation pathways and affect cytoskeletal rearrangement. DAPP1can also regulate BCR-induced activation of extracellular signal-regulated kinase (ERK), and c-jun NH2-terminal kinase (JNK). DAPP1 contains an N-terminal SH2 domain and a C-terminal pleckstrin homology (PH) domain with a single tyrosine phosphorylation site located centrally. DAPP1 binds strongly to both PtdIns(3,4,5)P3 and PtdIns(3,4)P2. The PH domain is essential for plasma membrane recruitment of PI3K upon cell activation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SLGSKEGYLTKLGGIVKNWKTRWFVLRRNELKYFKTRGDTKPIRVLDLRECSSVQRDYSQGKVNCFCLVF
PERTFYMYANTEEEADEWVKLLKWKL
>gnl|CDD|269978 cd10574, EVH1_SPRED-like, Sprouty-related EVH1 domain-containing-like proteins EVH1 domain. The Spred family has the following domains: an N-terminal EVH1 domain, a unique KBD (c-Kit kinase binding) domain which that is phosphorylated by the stem cell factor receptor c-Kit, and a C-terminal cysteine-rich SPR (Sprouty-related) domain which is involved in membrane localization. There are 3 Spred proteins: Spred1 which interacts with both Ras and Raf through its SPR domain; Spred2 which is the most abundant isoform; and Spred3 which has a non-functional KBD and maintains the inhibitory action on Raf. Legius syndrome is caused by heterozygous mutations in Spred1. Both EVH1 and SPR domains are involved in the inhibition of the MAP kinase pathway by Spred proteins. The specific function of the Spred2 EVH1 domain is unknown and there are no known interacting proteins to date. It is thought that its EVH1 domain will have a fourth distinct peptide binding mechanism within the EVH1 family. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains
CLVRVRAVVMTRDDSSGGWLPLGGGGLSIVSVCKVMPEEGAPRTEYVIHGERIRDKTVVLECTLRKDLVY
NKVMPTFHHWRIGEKKFGLTFQSPADARAFDRGVRRALEDLSR
>gnl|CDD|276901 cd10575, TNFRSF6B, Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor 3 (DcR3). The subfamily TNFRSF6B is also known as decoy receptor 3 (DcR3), M68, or TR6. This protein is a soluble receptor without death domain and cytoplasmic domain, and secreted by cells. It acts as a decoy receptor that competes with death receptors for ligand binding. It is a pleiotropic immunomodulator and biomarker for inflammatory diseases, autoimmune diseases, and cancer. Over-expression of this gene has been noted in several cancers, including pancreatic carcinoma, and gastrointestinal tract tumors. It can neutralize the biological effects of three tumor necrosis factor superfamily (TNFSF) members: TNFSF6 (Fas ligand/FasL/CD95L) and TNFSF14 (LIGHT) which are both involved in apoptosis and inflammation, and TNFSF15 (TNF-like molecule 1A/TL1A), which is a T cell co-stimulator and involved in gut inflammation. DcR3 is a novel inflammatory marker; higher DcR3 levels strongly correlate with inflammation and independently predict cardiovascular and all-cause mortality in chronic kidney disease (CKD) patients on hemodialysis. Increased synovial inflammatory cells infiltration in rheumatoid arthritis and ankylosing spondylitis is also associated with the elevated DcR3 expression. In cartilaginous fish, mRNA expression of DcR3 in the thymus and leydig, which are the representative lymphoid tissues of elasmobranchs, suggests that DcR3 may act as a modulator in the immune system. Interestingly, in banded dogfish (Triakis scyllia), DcR3 mRNA is strongly expressed in the gill, compared with human expression in the normal lung; both are respiratory organs, suggesting potential relevance of DcR3 to respiratory function
PTYQWKDDVTGESLTCDQCPPGTFVAKHCTRDRPTVCGPCPDLHYTQFWNYLEKCRYCNVFCTERQVEKR
QCNATHNRVCECKPGYYMEHGFCLRHSSCPPGEGVIKLGTPYSDTQCEPCPPGFFSASSSSTEPCQPHTN
CTQGGLETNVPGNDYHDTLCTSC
>gnl|CDD|276902 cd10576, TNFRSF1A, Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A), also known as TNFR1. TNFRSF1A (also known as type I TNFR, TNFR1, DR1, TNFRSF1A, CD120a, p55) binds TNF-alpha, through the death domain (DD), and activates NF-kappaB, mediates apoptosis and activates signaling pathways controlling inflammatory, immune, and stress responses. It mediates signal transduction by interacting with antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRAF2 and TRADD that play regulatory roles. The human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS), or periodic fever syndrome, is associated with germline mutations of the extracellular domains of this receptor, possibly due to impaired receptor clearance. TNFRSF1A polymorphisms rs1800693 and rs4149584 are associated with elevated risk of multiple sclerosis. Serum levels of TNFRSF1A are elevated in schizophrenia and bipolar disorder, and high levels are also associated with cognitive impairment and dementia. Patients with idiopathic recurrent acute pericarditis (IRAP), presumed to be an autoimmune process, have also been shown to carry rare mutations (R104Q and D12E) in the TNFRSF1A gene
CPQGKYLHPNNNHCCTKCHKGTYLYNDCPGPGQDTVCRECENGTFTASENYLRKCLSCSRCRKEMGQVEI
SPCTVDQDTVCGCRKNQYQHYWSSLFQCKNCSLCLNGTIRQPCQEKQDTICTCHTGFFLR
>gnl|CDD|276903 cd10577, TNFRSF1B, Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2. TNFRSF1B (also known as TNFR2, type 2 TNFR, TNFBR, TNFR80, TNF-R75, TNF-R-II, p75, CD120b) binds TNF-alpha, but lacks the death domain (DD) that is associated with the cytoplasmic domain of TNFRSF1A (TNFR1). It is inducible and expressed exclusively by oligodendrocytes, astrocytes, T cells, thymocytes, myocytes, endothelial cells, and in human mesenchymal stem cells. TNFRSF1B protects oligodendrocyte progenitor cells (OLGs) against oxidative stress, and induces the up-regulation of cell survival genes. While pro-inflammatory and pathogen-clearing activities of TNF are mediated mainly through activation of TNFRSF1A, a strong activator of NF-kappaB, TNFRSF1B is more responsible for suppression of inflammation. Although the affinities of both receptors for soluble TNF are similar, TNFRSF1B is sometimes more abundantly expressed and thought to associate with TNF, thereby increasing its concentration near TNFRSF1A receptors, and making TNF available to activate TNFRSF1A (a ligand-passing mechanism)
CRNSKEYYDEKAQMCCSKCPPGQHVKHSCTKTSDTVCAPCEESTYTQLWNWVPECLSCSSPCSSDQVETQ
ACTRQQNRICSCKPGWYCVLKLQEGCRQCRPLKKCGPGFGVARPGTASSDVECKPCAPGTFSDTTSSTDT
CRPHRICSSVAIPGNASMDAVCA
>gnl|CDD|276904 cd10578, TNFRSF3, Tumor necrosis factor receptor superfamily member 3 (TNFRSF3), also known as lymphotoxin beta receptor (LTBR). TNFRSF3 (also known as lymphotoxin beta receptor, LTbetaR, CD18, TNFCR, TNFR3, D12S370, TNFR-RP, TNFR2-RP, LT-BETA-R, TNF-R-III) plays a role in signaling during development of lymphoid and other organs, lipid metabolism, immune response, and programmed cell death. Its ligands include lymphotoxin (LT) alpha/beta membrane form (heterotrimer) and tumor necrosis factor ligand superfamily member 14 (also known as LIGHT). TNFRSF3 agonism by these ligands initiates canonical, as well as non-canonical nuclear factor-kappaB (NF-kappaB) signaling, and preferentially results in the translocation of p52-RELB complexes into the nucleus. While these ligands are often expressed by T and B cells, TNFRSF3 is conspicuous absence on T and B lymphocytes and NK cells, suggesting that signaling may be unidirectional for TNFRSF3. Activity of this receptor has also been linked to carcinogenesis; it helps trigger apoptosis and can also lead to release of the interleukin 8 (IL8). Alternatively spliced transcript variants encoding multiple isoforms have been observed
GLAWGPLLLGLCGLLAASQPQLVPPYRTENQTCWDQEKEYYEPRHQVCCSRCPPGTHVSAECSRSQDTVC
ATCPENSYNEHWNHLSICQLCRPCDPVLGFEEVAPCTSDRKTQCRCQPGMFCVHWDNECEHCEPLSDCPP
GTEAELTDEVGEADNNCV
>gnl|CDD|276905 cd10579, TNFRSF6, Tumor necrosis factor receptor superfamily member 6 (TNFRSF6), also known as fas cell surface death receptor (Fas). TNFRSF6 (also known as fas cell surface death receptor (FasR) or Fas, APT1, CD95, FAS1, APO-1, FASTM, ALPS1A) contains a death domain and plays a central role in the physiological regulation of programmed cell death. It has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The receptor interactions with the Fas ligand (FasL), allowing the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10; autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, leading to apoptosis. This receptor has also been shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is involved in transducing the proliferating signals in normal diploid fibroblast and T cells. Of the several alternatively spliced transcript variants, some are candidates for nonsense-mediated mRNA decay (NMD). Isoforms lacking the transmembrane domain may negatively regulate the apoptosis mediated by the full length isoform
RNITKREINCSEGLYRGGQFCCQPCPPGTRKAIDCTTNGGKPDCVPCTEGKEYTDKKHYSDKCRRCKICD
EEHGLEVEKNCTRTQNTKCRCKSNFFCNSSPCEHCDPCTTCEHGIIEECTPTSNTKCKK
>gnl|CDD|276906 cd10580, TNFRSF10, Tumor necrosis factor receptor superfamily member 10 (TNFRSF10), includes TNFRSF10A (DR4), TNFRSF10B (DR5), TNFRSF10C (DcR1) and TNFRSF10D (DcR2). TNFRSF10 family contains TNFRSF10A (also known as DR4, Apo2, TRAIL-R1, CD261), TNFRSF10B (also known as DR5, KILLER, TRICK2A, TRAIL-R2, TRICKB, CD262), TNFRSF10C (also known as DcR1, TRAIL-R3, LIT, TRID, CD263), and TNFRSF10D (also known as DcR2, TRUNDD, TRAIL-R4, CD264). Tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL) binds to all 4 receptors. DR4 (TRAIL-R1) and DR5 (TRAIL-R2) are membrane-bound and contain a death domain in their intracellular portion, which is able to transmit an apoptotic signal, thus often called death receptors. In contrast, DcR1 (TRAIL-R3), which lacks the complete intracellular portion and DcR2 (TRAIL-R4), which has a truncated cytoplasmic death domain, do not transmit an apoptotic signal, thus known as decoy receptors. Apoptosis mediated by DR4 and DR5 requires Fas (TNFRSF6)-associated via death domain (FADD), a death domain containing adaptor protein. Two transcript variants encoding different isoforms and one non-coding transcript have been found for TNFRSF10B/DR5. DcR1 appears to function as an antagonistic receptor that protects cells from TRAIL-induced apoptosis; it has been found to be a p53-regulated DNA damage-inducible gene. The expression of this gene is detected in many normal tissues but not in most cancer cell lines, which may explain the specific sensitivity of cancer cells to the apoptosis-inducing activity of TRAIL. DcR2 has been shown to play an inhibitory role in TRAIL-induced cell apoptosis. The membrane expression of all of these receptors (DR4, DR5, DcR1, and DcR2) is greater in normal endometrium (NE) than in endometrioid adenocarcinoma (EAC). In EAC patients, membrane expression of these receptors are not independent predictors of survival. DcR1 and DcR2 expression is critical in cell growth and apoptosis in cutaneous or uveal melanoma; DcR1 and DcR2 are frequently methylated in both, leading to loss of gene expression and melanomagenesis. On the other hand, DR4 and DR5 methylation is rare in cutaneous melanoma and frequent in uveal melanoma; their expression is wholly independent of the promoter methylation status. DcR1 and DcR2 genes are also reported to be hyper-methylated in prostate cancer. The TRAIL ligand, a potent and specific inducer of apoptosis in cancer cells, has been explored as a therapeutic drug; experimental data has shown that DR4 specific TRAIL variants are more efficacious than wild-type TRAIL in pancreatic cancer
SCGLCPAGTYVSEDSGDCIPCKEGVDYTEHPNGLPSCLPCTVCKSDEEELSPCTTTRNTECQCKPGTFCD
PDSPEVCQKCSTRCPEGMVEVSPCTPWSDLKCV
>gnl|CDD|276907 cd10581, TNFRSF11B, Tumor necrosis factor receptor superfamily member 11B (TNFRSF11B), also known as Osteoprotegerin (OPG). TNFRSF11B (also known as Osteoprotegerin, OPG, TR1, OCIF) is a secreted glycoprotein that regulates bone resorption. It binds to two ligands, RANKL (receptor activator of nuclear factor kappaB ligand, also known as osteoprotegerin ligand, OPGL, TRANCE, TNF-related activation induced cytokine), a critical cytokine for osteoclast differentiation, and TRAIL (TNF-related apoptosis-inducing ligand), involved in immune surveillance. Therefore, acting as a decoy receptor for RANKL and TRAIL, OPG inhibits the regulatory effects of nuclear factor-kappaB on inflammation, skeletal, and vascular systems, and prevents TRAIL-induced apoptosis. Studies in mice counterparts suggest that this protein and its ligand also play a role in lymph-node organogenesis and vascular calcification. Circulating OPG levels have emerged as independent biomarkers of cardiovascular disease (CVD) in patients with acute or chronic heart disease. OPG has also been implicated in various inflammations and linked to diabetes and poor glycemic control. Alternatively spliced transcript variants of this gene have been reported, although their full length nature has not been determined
CCLLVLLDISVKWTFQETFPPKYLHYDPVTSRQLMCDQCPPGTYVKQHCSASRKTVCAPCPDHHYADDWN
SNDECQYCNTVCKELQYVKQECNSTHNRVCECVEGRYLELEFCLKHTECPPGFGVVQPGTPESDTVCERC
PEGFFSN
>gnl|CDD|276908 cd10582, TNFRSF14, Tumor necrosis factor receptor superfamily member 14 (TNFRSF14), also known as herpes virus entry mediator (HVEM). TNFRSF14 (also known as herpes virus entry mediator or HVEM, ATAR, CD270, HVEA, LIGHTR, TR2) regulates T-cell immune responses by activating inflammatory, as well as inhibitory signaling pathways. HVEM acts as a receptor for the canonical TNF-related ligand LIGHT (lymphotoxin-like), which exhibits inducible expression, and competes with herpes simplex virus glycoprotein D for HVEM. It also acts as a ligand for the immunoglobulin superfamily proteins BTLA (B and T lymphocyte attenuator) and CD160, a feature distinguishing HVEM from other immune regulatory molecules, thus, creating a functionally diverse set of intrinsic and bidirectional signaling pathways. HVEM is highly expressed in the gut epithelium. Genome-wide association studies have shown that Hvem is an inflammatory bowel disease (IBD) risk gene, suggesting that HVEM could have a regulatory role influencing the regulation of epithelial barrier, host defense, and the microbiota. Mouse models have revealed that HVEM is involved in colitis pathogenesis, mucosal host defense, and epithelial immunity, thus acting as a mucosal gatekeeper with multiple regulatory functions in the mucosa. HVEM plays a critical role in both tumor progression and resistance to antitumor immune responses, possibly through direct and indirect mechanisms. It is known to be expressed in several human malignancies, including esophageal squamous cell carcinoma, follicular lymphoma and melanoma. HVEM network may therefore be an attractive target for drug intervention
CKEDEYPVGSECCPKCSPGYRVKKACGELTGTVCEPCPPGTYTAHLNGLSKCLQCRVCDPAMGLVTRRNC
SSTENTVCGCIPGHFCSAQDGDHCVECVPHS
>gnl|CDD|276909 cd10583, TNFRSF21, Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor (DR6). TNFRSF21 (also known as death receptor 6 (DR6), CD358, BM-018) is highly expressed in differentiating neurons as well as in the adult brain, and is upregulated in injured neurons. DR6 negatively regulates neurondendrocyte, axondendrocyte, and oligodendrocyte survival, hinders axondendrocyte and oligodendrocyte regeneration and its inhibition has a neuro-protective effect in nerve injury. It activates nuclear factor kappa-B (NFkB) and mitogen-activated protein kinase 8 (MAPK8, also called c-Jun N-terminal kinase 1), and induces cell apoptosis by associating with TNFRSF1A-associated via death domain (TRADD), which is known to mediate signal transduction of tumor necrosis factor receptors. TNFRSF21 plays a role in T-helper cell activation, and may be involved in inflammation and immune regulation. Its possible ligand is alpha-amyloid precursor protein (APP), hence probably involved in the development of Alzheimer's disease; when released, APP binds in an autocrine/paracrine manner to activate a caspase-dependent self-destruction program that removes unnecessary or connectionless axons. Increasing beta-catenin levels in brain endothelium upregulates TNFRSF21 and TNFRSF19, indicating that these death receptors are downstream target genes of Wnt/beta-catenin signaling, which has been shown to be required for blood-brain barrier development. DR6 is up-regulated in numerous solid tumors as well as in tumor vascular cells, including ovarian cancer and may be a clinically useful diagnostic and predictive serum biomarker for some adult sarcoma subtypes
KYRHVDPATGTQLTCDKCPAGTYVSKHCTETSLRECSPCPNGTFTRHENGIEQCHRCRKPCPAPMIEKTP
CTALTDRECTCPPGTFLSNDTCVPHSVCPVGWGVRKKGTETEDVRCKPCPRGTFSDVPSSVLKCKTYTDC
LGLGLVVIKPGTKETDNVC
>gnl|CDD|213020 cd10585, CE4_SF, Catalytic NodB homology domain of the carbohydrate esterase 4 superfamily. The carbohydrate esterase 4 (CE4) superfamily mainly includes chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan, respectively. Members in this superfamily contain a NodB homology domain that adopts a deformed (beta/alpha)8 barrel fold, which encompasses a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad, closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The NodB homology domain of CE4 superfamily is remotely related to the 7-stranded beta/alpha barrel catalytic domain of the superfamily consisting of family 38 glycoside hydrolases (GH38), family 57 heat stable retaining glycoside hydrolases (GH57), lactam utilization protein LamB/YcsF family proteins, and YdjC-family proteins
LVLLTLDDDPAFEGSPAALQRLLDLLEGYGIPATLFVIPGNANPDKLMKSPLNWDLLRELLAYGHEIGLH
GYTHPDLAYGNLSPEEVLEDLLRARRILEEAGGQPPKGFRAPGGNLSETVKALKELGDIQYDSDLAFVLL
VH
>gnl|CDD|198285 cd10718, SH2_CIS, Src homology 2 (SH2) domain found in cytokine-inducible SH2-containing protein (CIS). CIS family members are known to be cytokine-inducible negative regulators of cytokine signaling. The expression of the CIS gene can be induced by IL2, IL3, GM-CSF and EPO in hematopoietic cells. Proteasome-mediated degradation of this protein has been shown to be involved in the inactivation of the erythropoietin receptor. Suppressor of cytokine signalling (SOCS) was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites
LRESGWYWGSITASEAHQALQKAPEGTFLVRDSSHPSYMLTLSVKTTRGPTNVRIEYSDGSFRLDSSSLA
RPRLLSFPDVVSLVQHYV
>gnl|CDD|199908 cd10719, DnaJ_zf, Zinc finger domain of DnaJ and HSP40. Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding
CPTCNGSGAKPGTKPKTCPTCGGSGQVRQVQGTGFGFFQTQTTCPTCGGTGKIIKDPCPKCKGKG
>gnl|CDD|199909 cd10747, DnaJ_C, C-terminal substrate binding domain of DnaJ and HSP40. The C-terminal region of the DnaJ/Hsp40 protein mediates oligomerization and binding to denatured polypeptide substrate. DnaJ/Hsp40 is a widely conserved heat-shock protein. It prevents the aggregation of unfolded substrate and forms a ternary complex with both substrate and DnaK/Hsp70; the N-terminal J-domain of DnaJ/Hsp40 stimulates the ATPase activity of DnaK/Hsp70
ADLRYDLELTLEEAYFGKEKEIKIPRKVTRVREKKTLTVKIPAGVDDGQRLRLRGEGDAGPNGGPPGDLY
VVIRVKPHPVFRRDGNDLYCEVPISLTEALLGGEIEVPTLGGKVKLKIPPGTQPGTVLRLKGKGMPRLRG
GGRGDLYVEVKVEFPKKL
>gnl|CDD|199910 cd10748, anti-TRAP, anti-TRAP (AT) protein specific to Bacilli. In Bacillus subtilis and related bacteria, AT binds to the TRAP protein, (tryptophan-activated trp RNA-binding attenuation protein), effectively disrupting interaction of TRAP with mRNAs. Upon binding of tryptophan, TRAP (which forms a complex of 11 identical subunits) interacts with a specific location in the leader RNA and blocks translation of the tryptophan biosynthetic operon. AT, in turn, recognizes the tryptophan-activated TRAP complex and prevents RNA binding. AT is expressed in response to high levels of uncharged tryptophan tRNA. AT contains a zinc-binding motif that closely resembles the zinc-binding motifs in the zinc-finger region of DnaJ/Hsp40. AT has been shown to form homo-dodecameric assemblies, and can actually do that in two different relative orientations, resulting in two different dodecamers. Recent data suggest that the trimeric form of AT may be the biologically relevant active complex
VIATDDLEVTCPKCERAGEEEGTPCPKCSGKGVILTAQGYTLLHFIKKHLNE
>gnl|CDD|212097 cd10785, GH38-57_N_LamB_YdjC_SF, Catalytic domain of glycoside hydrolase (GH) families 38 and 57, lactam utilization protein LamB/YcsF family proteins, YdjC-family proteins, and similar proteins. The superfamily possesses strong sequence similarities across a wide range of all three kingdoms of life. It mainly includes four families, glycoside hydrolases family 38 (GH38), heat stable retaining glycoside hydrolases family 57 (GH57), lactam utilization protein LamB/YcsF family, and YdjC-family. The GH38 family corresponds to class II alpha-mannosidases (alphaMII, EC 3.2.1.24), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides by employing a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. GH57 is a purely prokaryotic family with the majority of thermostable enzymes from extremophiles (many of them are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57 cleaves alpha-glycosidic bond by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation. Although the exact molecular function of LamB/YcsF family and YdjC-family remains unclear, they show high sequence and structure homology to the members of GH38 and GH57. Their catalytic domains adopt a similar parallel 7-stranded beta/alpha barrel, which is remotely related to catalytic NodB homology domain of the carbohydrate esterase 4 superfamily
FINAHSHNPYVWIQTFEEWYFEATKATYIPLLMHFHRNFEMSFNIAPISYEALFYHDLGENIKLQMKSIQ
KNGQLEIGTHGATHPDESEAQSHPENVYAQITEGITWLEKHMGVTPRHIWLHECFYNQAKQLSQGIPYIL
QKSGFLYLFVQSRSISVKKELALWRQIWYNKKDSGVFTFIVIPLHDEFFGHWWFEGVVFLERL
>gnl|CDD|212098 cd10786, GH38N_AMII_like, N-terminal catalytic domain of class II alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38). Alpha-mannosidases (EC 3.2.1.24) are extensively found in eukaryotes and play important roles in the processing of newly formed N-glycans and in degradation of mature glycoproteins. A deficiency of this enzyme causes the lysosomal storage disease alpha-mannosidosis. Many bacterial and archaeal species also possess putative alpha-mannosidases, but their activity and specificity is largely unknown. Based on different functional characteristics and sequence homology, alpha-mannosidases have been organized into two classes (class I, belonging to glycoside hydrolase family 47, and class II, belonging to glycoside hydrolase family 38). Members of this family corresponds to class II alpha-mannosidases (alphaMII), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst
TVHLVPHSHYDVGWLQTFEQYYQINFKAILDKALRLLDANPEYKFLIEEVILLERYWDVRPDLKAKLKQA
VRSGRLEIAGGGYVMPDTNLPDGESLVRQILLGKRWLKEFLGARPPVMWQADVFGHSPQLPQILAKSGFT
GFAFGRGPYSQKRMQRPSEFLWRGLDGTRILTHWMPNGYSDGPFLCGPDIPGDNSGPNALASLEALVEQW
KKLAELGATNHLLMPSGGDFTIPQADPLQVNQARLVEPWNS
>gnl|CDD|212099 cd10787, LamB_YcsF_like, LamB/YcsF family of lactam utilization protein. The LamB/YbgL family includes the Aspergillus nidulans protein LamB, and its homologs from all three kingdoms of life. The lamb gene locates at the lam locus of Aspergillus nidulans, consisting of two divergently transcribed genes, lamA and lamB, needed for the utilization of lactams such as 2-pyrrolidinone. Both genes are under the control of the positive regulatory gene amdR and are subject to carbon and nitrogen metabolite repression. Although the exact molecular function of LamB is unknown, it might be required for conversion of exogenous 2-pyrrolidinone to endogenous GABA
IDLNCDLGESFGAWKMGDDEALLPLVTSANIACGFHAGDPLVMRRTVRLAKEHGVAIGAHPGYPDLQGFG
RRSMDLSPDELRALVLYQIGALQAFARAAGTRLSHVKPHGALYNMAAKDEELARAVARAVAAVDPDLILL
GLAGSALERAARAAGLRVAFEAFADRAYTDDGTLVPRSEPGAVIHDPEEAAARVLRMVKEGTVTTIDGKT
IPLRADTICVHGDTPGAVALARAIRAAL
>gnl|CDD|212100 cd10788, YdjC_like, YdjC-family proteins. YdjC-family proteins are widely distributed, from human to bacteria. It is represented by an uncharacterised protein YdjC (also known as ChbG), encoded by the chb (N,N'-diacetylchitobiose, also called [GlcNAc]2) or cel operon in Escherichia coli, which encodes enzymes involved in growth on an N,N'-diacetylchitobiose carbon source. This subfamily also includes hopanoid biosynthesis associated proteins HpnK and many uncharacterized YdjC homologs. Although the exact molecular function of the YdjC-family proteins remains unclear, it has been suggested that they play a role in the cleavage of cellobiosephosphate
LILNADDFGLTHAVNEGIIDAHRNGRLTSTSLMVNSPASAEAAALAKRNPRLDLGLHLNLTEGQPLTPPA
KSPSLLDEAGRFKSSPIFRRSFEGKLNAAEVRKEIEAQIDRFKELGRTPDHIDSHHHVHVLPVLLGVLLE
LLREGGILPVRIPGNLEFNGNNRYDKDLLPELERFLKLKIFTHDYSLDLYVDGTIDQGPILRLPDLVKEG
VAELMVHPGLPDDIRALGSDLDREKELEALLSP
>gnl|CDD|212101 cd10789, GH38N_AMII_ER_cytosolic, N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily is represented by Saccharomyces cerevisiae vacuolar alpha-mannosidase Ams1, rat ER/cytosolic alpha-mannosidase Man2C1, and similar proteins. Members in this family share high sequence similarity. None of them have any classical signal sequence or membrane spanning domains, which are typical of sorting or targeting signals. Ams1 functions as a second resident vacuolar hydrolase in S. cerevisiae. It aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing alpha-d-mannose residues. Ams1 utilizes both the cytoplasm to vacuole targeting (Cvt, nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Man2C1is involved in oligosaccharide catabolism in both the ER and cytosol. It can catalyze the cobalt-dependent cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl-enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst
KIYAVGHAHIDLAWLWPVRETRRKAARTFSTVLDLMEEYPDFVFTQSQAQLYEWLEEDYPELFERIKERV
KEGRWEPVGGMWVEPDCNLPSGESLVRQFLYGQRYFREEFGVESRILWLPDSFGFSAALPQILKKSGIDY
FVTQKLSWNDTNKFPYDTFRWRGIDGSEVLAHFIPTGYYNGDLTPEEILEAWRNFRDKDVSDELLLLYGV
GDGGGGPTREMLERLRRLKDLPGLPRVEFSTPEEFFERLEEE
>gnl|CDD|212102 cd10790, GH38N_AMII_1, N-terminal catalytic domain of putative prokaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). This mainly bacterial subfamily corresponds to a group of putative class II alpha-mannosidases, including various proteins assigned as alpha-mannosidases, Streptococcus pyogenes (SpGH38) encoded by ORF spy1604. Escherichia coli MngB encoded by the mngB/ybgG gene, and Thermotoga maritime TMM, and similar proteins. SpGH38 targets alpha-1,3 mannosidic linkages. SpGH38 appears to exist as an elongated dimer and display alpha-1,3 mannosidase activity. It is active on disaccharides and some aryl glycosides. SpGH38 can also effectively deglycosylate human N-glycans in vitro. MngB exhibits alpha-mannosidase activity that catalyzes the conversion of 2-O-(6-phospho-alpha-mannosyl)-D-glycerate to mannose-6-phosphate and glycerate in the pathway which enables use of mannosyl-D-glycerate as a sole carbon source. TMM is a homodimeric enzyme that hydrolyzes p-nitrophenyl-alpha-D-mannopyranoside, alpha -1,2-mannobiose, alpha -1,3-mannobiose, alpha -1,4-mannobiose, and alpha -1,6-mannobiose. The GH38 family contains retaining glycosyl hydrolases that employ a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. Divalent metal ions, such as zinc or cobalt ions, are suggested to be required for the catalytic activities of typical class II alpha-mannosidases. However, TMM requires the cobalt or cadmium for its activity. The cadmium ion dependency is unique to TMM. Moreover, TMM is inhibited by swainsonine but not 1-deoxymannojirimycin, which is in agreement with the features of cytosolic alpha-mannosidase
KVHIISHTHWDREWFATTEQTHKWLINLFERLLELIQKDPEYSFVLDGQTAILEDYLKVFPEREKKLRQA
IKSGKLIIGPYYIQIDWRITSEESIVRNFEIGKKDCDRFGASMKIGWLPDSFGFISQLPQLMRKFGIEAV
FLWRGISPEGSSPKIEFSWQSPDGSRVLGVFLAGGYRNGYELPTTEDIARKRLDHEIAKLEKFSSTKEIL
LLNGYDLDPVPEDPTDALAKANELYPDEEFVESCFEEYLADLVGELPEGSYLSVFPGELSSRE
>gnl|CDD|212103 cd10791, GH38N_AMII_like_1, N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily of mainly uncharacterized eukaryotic proteins shows sequence homology with class II alpha-mannosidases (AlphaAMIIs). AlphaAMIIs possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyze the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. This subfamily belongs to the GH38 family of retaining glycosyl hydrolases, which employ a two-step mechanism involving the formation of a covalent glycosyl enzyme complex; two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst
TVHVVHHSHTDIGYTDLQEKVDRYHVDYIPQALDLAEATKNYPEDARFRWTTESTWLVEEYLKCASPEQR
ERLEQAVRRGRIGWHALPLNITTELMDEELLRRGLYLSKELDRRFGLPIIVAMQTDVPGHTWGLVDVLAD
AGIKYLSIGVNGHSGPYPPRVPGPFYWESPDGRKVLVWYGGHYGGGNLLGGGEDAGDFAHTGDNSGPATP
EELLYLLELERKDYPFDPALVSGSFTDNAPPPVVISEIIDTWNH
>gnl|CDD|212104 cd10792, GH57N_AmyC_like, N-terminal catalytic domain of alpha-amylase (AmyC) and similar proteins. Alpha-amylases (alpha-1,4-glucan-4-glucanohydrolases, EC 3.2.1.1) play essential roles in alpha-glucan metabolism by catalyzing the hydrolysis of polysaccharides such as amylose starch, and beta-limit dextrin. This subfamily is represented by a novel alpha-amylase (AmyC) encoded by hyperthermophilic organism Thermotoga maritime ORF tm1438, and its prokaryotic homologs. AmyC functions as a homotetramer and shows thermostable amylolytic activity. It is strongly inhibited by acarbose. AmyC is composed of a N-terminal catalytic domain, containing a distorted TIM-barrel structure with a characteristic (beta/alpha)7 fold motif, and two additional less conserved domains. There are other two canonical alpha-amylases encoded from T. maritime that lack the sequence similarity to AmyC, and belong to a different superfamily
GYLALVLHAHLPYVRHPEYDRFLEERWLFEAITETYLPLLRMFERLERDGVPFKLTLSLSPTLCSMLADP
LLQERYLRYLDRLIELAEKEVERTRGDPEFHKLARFYLERFEETKEDFEERYGRNLLKAFKYFQEKGKLE
LITCAATHGFLPLYQDYPEAVRAQIETGVRSYRRHFGRKPRGIWLPECGYYPGLDRILAEYGIRYFFVDT
HGILFADPRPRYGVYAPVYTPNGVAAFGRDPESSRQVWSAEEGYPGDPDYREFYRDIGFDLDYEYIKPYI
HPDGIRGITGFKYTRITGKTDDKEPYDPEWAREKAAEHARNFLANREKQLEKLAALMDRPPLVVAPYDAE
LFGHWWFEGPDFLEAVFRKAAEDQDIELITPSEYLKEHPDLQVAEPSFSSWGEGGYGEVWLN
>gnl|CDD|212105 cd10793, GH57N_TLGT_like, N-terminal catalytic domain of 4-alpha-glucanotransferase; glycoside hydrolase family 57 (GH57). 4-alpha-glucanotransferase (TLGT, EC 2.4.1.25) plays a key role in the maltose metabolism. It catalyzes the disproportionation of amylose and the formation of large cyclic alpha-1,4-glucan (cycloamylose) from linear amylose. TLGT functions as a homodimer. Each monomer is composed of two domains, an N-terminal catalytic domain with a (beta/alpha)7 barrel fold and a C-terminal domain with a twisted beta-sandwich fold. Some family members have been designated as alpha-amylases, such as the heat-stable eubacterial amylase from Dictyoglomus thermophilum (DtAmyA) and the extremely thermostable archaeal amylase from Pyrococcus furiosus(PfAmyA). However, both of these proteins are 4-alpha-glucanotransferases. DtAmyA was shown to have transglycosylating activity and PfAmyA exhibits 4-alpha-glucanotransferase activity
NLIFGIHNHQPVGNFDEVFEEAYEKSYKPFLEVLKKYPDFKFSLHFSGWLLEWLEENHPEYLDLLRKLVD
RGQIEILGGGFYEPILASIPSEDRVGQIKKLNRFIEKNFGQRPKGLWLTERVWEPSLVPDLAEAGIEYVV
VDDYHFLSAGLPPEELYGYYLTEDEGHKLKVFPISKKLRYLIPFKPPEETIDYLRSIAREEGGRVAVIFD
DGEKFGLWPGTYEWVYERGWLERFLELLLENSDWIETTHPSEYLEEQKPLGLVYLPTASYEEMGEWSLP
>gnl|CDD|212106 cd10794, GH57N_PfGalA_like, N-terminal catalytic domain of alpha-galactosidase; glycoside hydrolase family 57 (GH57). Alpha-galactosidases (GalA, EC 3.2.1.22) catalyze the hydrolysis of alpha-1,6-linked galactose residues from oligosaccharides and polymeric galactomannans. Based on sequence similarity, the majority of eukaryotic and bacterial GalAs have been classified into glycoside hydrolase family GH27, GH36, and GH4, respectively. This subfamily is represented by a novel type of GalA from Pyrococcus furiosus (PfGalA), which belongs to the GH57 family. PfGalA is an extremely thermo-active and thermostable GalA that functions as a bacterial-like GalA, however, without the capacity to hydrolyze polysaccharides. It specifically catalyzes the hydrolysis of para-nitrophenyl-alpha-galactopyranoside, and to some extent that of melibiose and raffinose. PfGalA has a pH optimum between 5.0-5.5
YFVFHANLQFSSIPEEQRPEVIRRCYWPLLRLHEEGRIPLGIEASGYTLESLHWIDPEWIAKLKELIASG
LIEILGSGYAQAIGPLVPANVNVHNLRLGNRTYEDLLGVRPQTAWVPEQAWSAGLPEIYRDAGYEAVIMD
ADNPFSNHPNWNPKLVYGPQKILGSDGRELPVLWNDSIAFQKFYVHGDLGLDEYLSYLARWLATDQRAIM
LYGNDAEIFDFRPGRYTNTYRYPEAGEWIRISQLLDVLREDLGFEFWLPSKVLYSGEGTYAGLKTTLEQP
VPVKKQAKYNGSRWAVSGRSDAWYN
>gnl|CDD|212107 cd10795, GH57N_MJA1_like, N-terminal catalytic domain of a thermoactive alpha-amylase from Methanococcus jannaschii and similar proteins; glycoside hydrolase family 57 (GH57). The subfamily is represented by a thermostable alpha-amylase (MJA1, EC 3.2.1.1) encoded from the hyperthermophilic archaeon Methanococcus jannaschii locus, M J1611. MJA1 has a broad pH optimum 5.0-8.0. It exhibits extremely thermophilic alpha-amylase activity that catalyzes the hydrolysis of large sugar polymers with alpha-l,6 and alpha-l,4 linkages, and yields products including glucose polymers of 1-7 units. MJ1611 also encodes another alpha-amylase with catalytic features distinct from MJA1, which belongs to glycoside hydrolase family 13 (GH-13), and is not included here. This subfamily also includes many uncharacterized proteins found in bacteria and archaea
NVCLYFEVHQPYRLKRYFFQFDIGLDHRYFDDELNREIFRRVAEKCYLPANRLLLELIEEYGGFKVAFSI
SGTFLEQAEKYAPEVIDSFRELADTGNVEFLAETYYHSLASLFDKDEFREQVKMHRELIKELFGVKPTVF
RNTELIYSDDIAEIAEDMGFKAILTEGADHILGWRSPNYVYKAAGPGLKLLLRNYRLSDDIAFRFSDRSW
DEYPLTADKYASWIAATPGDVVNLFMDYETFGEHQWAESGIFEFLRALPEELLKRGIEFITPSEAAKRHP
PVGELSVPETISWADEERDLSAWLGN
>gnl|CDD|212108 cd10796, GH57N_APU, N-terminal catalytic domain of thermoactive amylopullulanases; glycoside hydrolase family 57 (GH57). Pullulanases (EC 3.2.1.41) are capable of hydrolyzing the alpha-1,6 glucosidic bonds of pullulan, producing maltotriose. Amylopullulanases (APU, E.C 3.2.1.1/41) are type II pullulanases which can also degrade both the alpha-1,6 and alpha-1,4 glucosidic bonds of starch, producing oligosaccharides. This subfamily includes GH57 archaeal thermoactive APUs, which show both pullulanolytic and amylolytic activities. They have an acid pH optimum and the presence of Ca2+ might increase their activity, thermostability, and substrate affinity. Besides GH57 thermoactive APUs, all mesophilic and some thermoactive APUs belong to glycoside hydrolase family 13 with catalytic features distinct from GH57. This subfamily also includes many uncharacterized proteins found in bacteria and archaea
LVFVWHMHQPPYYDPLDGEYHLPWVRLHAIKDYYDMAYLLEAYPNVKVTFNLSPSLLEQLEDYGIIPLYR
ELAEEGQIELSTTPYYHPILPLLIDTNSARENPPLPLPPERFGWPEDAEAQLRKAKEYYKEVFGVTPRGL
WPPEGAVSEELLPLYAELGIKWTATDEAVLFKSLGNVGDKESLYRPYRVEGGGKSIYVFFRDHELSDLIG
FTYSFWPAEDAARDFIHRLKSIREQIYNPGGVVTIALDGENAWEFYPNNGYDFLEALYQALSELQDIGTV
TLSEAIEKHPPERVLTRLPTGSWIGGNFSTWIG
>gnl|CDD|212109 cd10797, GH57N_APU_like_1, N-terminal putative catalytic domain of mainly uncharacterized prokaryotic proteins similar to archaeal thermoactive amylopullulanases; glycoside hydrolase family 57 (GH57). This subfamily of mainly uncharacterized bacterial proteins, shows high sequence homology to GH57 archaeal thermoactive amylopullulanases (APU, E.C 3.2.1.1/41). Thermoactive APUs are type II pullulanases with both pullulanolytic and amylolytic activities. They have an acid pH optimum and the presence of Ca2+ might increase their activity, thermostability, and substrate affinity
YLCIHGHFYQPPRENPWLEEIEVQPSAAPFHDWNERITAECYAPNAAARILDEEGRIVDIVNNYSWISFN
FGPTLLSWLERHAPEVYQRILEADRESVERLGHGNAIAQVYNHIILPLANRRDKETQIRWGIRDFERRFG
RAPEGMWLPETAVDLETLEALADEGIKFTILAPWQAKRVRPIGGGWHDVSGGPIDPTRPYRVRLPSGRSI
TVFFYDGPLSRAVAFGGLLSSGERFAGRLLSAFDDRRGGPQLVHIATDGETYGHHHRFGDMALAYALQKI
APERGAELTNYAAYLEKHPPTWEVEIVENSSWSCAHGVERWRSDCGC
>gnl|CDD|212110 cd10798, GH57N_like_1, Uncharacterized subfamily of glycoside hydrolase family 57 (GH57). This subfamily of uncharacterized bacterial proteins, shows high sequence homology to glycoside hydrolase family 57 (GH57). Glycoside hydrolase family 57(GH57) is a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22)
HALGLHMHQPPINLGLGEEGRAILKYMHGHLLDGDNWNAEQILRCYERPARFVPRLSDQGKVPRVMLDYS
GVLLEQLLDPGIQGRYRDIVDLLKMLECYRYQPNVELLGTGYYHPVFPLTPEQDWEEHLQRWRAIFAEVF
GREALARVRGFWPPEMAFPMHPDVAYEMVPALKKCGYEWVIVDEVHVEPPDGWTLQDRHQPHRLVHANSQ
GGTEIIIVPRDTRDSSNAQVAQMQPYWFAKELSRRAKLSPEIPPLVTTWSDGENGGVMMNNFFPHFFAPL
MEQARGGGTPEPVNVSEYLDRYPPVGPKEEPRFEVEGGSWNVDFISWVGG
>gnl|CDD|212111 cd10800, LamB_YcsF_YbgL_like, Escherichia coli putative lactam utilization protein YbgL and similar proteins. This subfamily of the LamB/YbgL family is represented by the Escherichia coli putative lactam utilization protein YbgL. Although their molecular function of member of this subfamily is unknown, they show high sequence similarity to the Aspergillus nidulans lactam utilization protein LamB, which might be required for conversion of exogenous 2-pyrrolidinone to endogenous GABA
IDLNADLGEGCGNDAALLTLVSSANIACGWHAGDATTMRATVALALENGVAIGAHPGFPDRENFGRTEME
LSPDELYAGLLYQLGALKAIVRAEGGRLAHVKPHGALYNQAAKDAALADAIARAVRDFDPSLKLMGLAGG
HLVRAARELGLQAISEVFADRGYRADGSLVPRSQPGALIEDDEEAIAQVLQMVTEGTVTAVDGSWIPVQA
QTICLHGDGEHALAFARRIRAALESKGIKI
>gnl|CDD|212112 cd10801, LamB_YcsF_like_1, uncharacterized proteins similar to the Aspergillus nidulans lactam utilization protein LamB. This mainly bacterial subfamily of the LamB/YbgL family, contains many well conserved uncharacterized proteins. Although their molecular function remains unknown, those proteins show high sequence similarity to the Aspergillus nidulans lactam utilization protein LamB, which might be required for conversion of exogenous 2-pyrrolidinone to endogenous GABA
IDLNADLGEGVGNDAALMPLISSCNIACGGHAGDEESMRKTVKLAKEYGVKIGAHPSYPDRENFGRVSME
ISPQELKESLREQIELLKEVAAEEGVTLHHIKPHGALYNDAAKDEALAELIIEAIKEVDPSLKLYVPAGS
VLAKAAKAAGLTIIFEAFADRAYNADGSLVSRSQPGAVITDPEEVLNQVLSMVKGGKVTTIEGEKIPIKA
DTLCVHGDTPNALEIARALRAAL
>gnl|CDD|212113 cd10802, YdjC_TTHB029_like, Thermus thermophiles TTHB029 and similar proteins. This subfamily is represented by an YdjC-family protein TTHB029 from Thermus thermophilus HB8; it is similar to Escherichia coli YdjC, a hypothetical protein encoded by the celG gene. TTHB029 functions as a homodimer. Each of monomer consists of (beta/alpha)-barrel fold. The molecular function of TTHB029 is unclear
RLLIIHADDFGMSHSANEAIIELLEEGIVSSASVMVPCPWFPEAAAYAAANPEIDVGLHLTLTSEWDNYR
WGPLTPKEQVPSLVDEEGYFPPDVAELEANADPDEVEKELRAQIERALKAGIRPTHLDSHMGSLYGGPEF
LELYLRLAAEYGLPVRLPRLLAALGRQAALADVGELAYAFGVPVLDDLIGGPFPVTYEEKRASYIQALRK
LPPGLTELIIHPALDTEELKAIEDSAQKRQWDYDLFTDPEL
>gnl|CDD|212114 cd10803, YdjC_EF3048_like, Enterococcus faecalis EF3048 and similar proteins. This subfamily is represented by a putative cellobiose-phosphate cleavage protein EF3048 from Enterococcus faecalis v583. It is similar to Escherichia coli YdjC, a hypothetical protein encoded by the celG gene. EF3048 might function as a homodimer. Each of the monomers consists of a (beta/alpha)-barrel fold that forms an active homodimer. The molecular function of the EF3048 is unclear
KLIVNADDFGLTKGVNYGIIEAHRNGVVTSTTLMVNMPGFEHAVELAKENPGLGVGVHLTLTCGKPLLDD
VPSLVDEDGNFRKQSDYEGEGEIDPEEVYREWKAQIEKFLALGLKPTHLDSHHHVHTHPQVLPVVERLAK
EYGLPVRAGDTAILYLGVKTTDRFSDDFYGEGVSLENLLEILDEAAAGYEVVEIMCHPAYVDQELLEISS
YNLPRLKELEILTSPELK
>gnl|CDD|212115 cd10804, YdjC_HpnK_like, hopanoid biosynthesis associated protein HpnK and similar proteins. The subfamily includes some uncharacterized proteins annotated as hopanoid biosynthesis associated proteins, HpnK. They show high sequence similarity to proteins from the YdjC-family, the latter is represented by an uncharacterised protein YdjC (also known as ChbG) encoded by the chb (N,N'-diacetylchitobiose, also called [GlcNAc]2) or cel operon in Escherichia coli, which encodes enzymes involved in growth on an N,N'-diacetylchitobiose carbon source
RLIVTADDFGLSHEVNEAVEQAHREGILTSASLMVGGPAADDAVARARRLPGLGVGLHLVLVEGRSVLPP
EEIPDLVDAQGRFPSDPVRAGFRYFFSPAARRQLRAEIRAQFEAFRATGLPLDHVDGHKHFHLHPTVFDL
LLELAPEYGIRAVRLPREPLRLNLAADRQWLGRGLGALIFRPLARRLRRRLRRAGLRVNDRVFGLLWSGA
MTEDYLLALLEHLPEGLTEIYFHPAVAPDAELRGRMPGYRHAEELAALLSP
>gnl|CDD|212116 cd10805, YdjC_like_1, uncharacterized YdjC-like family proteins from bacteria. The subfamily contains many hypothetical proteins, and belongs to the YdjC-like family of uncharacterized proteins from bacteria. The YdjC-family is represented by an uncharacterised protein YdjC (also known as ChbG) encoded by the chb (N,N'-diacetylchitobiose, also called [GlcNAc]2) or cel operon in Escherichia coli, which encodes enzymes involved in growth on an N,N'-diacetylchitobiose carbon source. The molecular function of this subfamily is unclear
KLLVRADDLGYSEGVNYGILKAVRNGIVRSTGLMVNMPAAEHALELIKDYPDVCLGLHTNIVLGKPLSDP
ELIPSLVDENGEFKSSKEYRAELAEGEDFVNYEEVYLEIEAQVERFIELVGRKPDYIEGHAVETPNFEKA
IEDVAEKYGIPYNGDYLPKDSKLSGGSADYMNKPFSGEKYDPLEDFFGLLESAKDDEIALLVFHPGYLDD
YLLDHSSLTLPRCKDLEALTSPEVKEWLEENDIELITYRDL
>gnl|CDD|212117 cd10806, YdjC_like_2, uncharacterized YdjC-like family proteins from eukaryotes. This eukaryotic subfamily contains hypothetical and uncharacterized proteins, and belongs to the YdjC-like family of uncharacterized proteins. The YdjC-family is represented by an uncharacterised protein YdjC (also known as ChbG) encoded by the chb (N,N'-diacetylchitobiose, also called [GlcNAc]2) or cel operon in Escherichia coli, which encodes enzymes involved in growth on an N,N'-diacetylchitobiose carbon source. The molecular function of this subfamily is unclear
KLVVNADDFGYCPQRNRGIVECFLAGVVTSVSLLVNGSSAEDAAKLAKRHNIPIGLHLNLTEGRPVSDEL
RGVSSLLGKDGFFLGKMGFREALKQGDIDMSEVRIEIRAQIAWFIELLGRLPTHVDGHQHVHVLPGVREV
FAEVLQEFGIKKTRIPVELGLESCNWIEEARREFYKGVEEDALEAVKIFSSHGIRWTDYFIGLSTMGKNM
TEQRLQSSLITFKKSKPASRSVTCELMVHPGYPSVNGCGGCGEGPDDFSQSPDREHELKVLTSPSLRNFL
>gnl|CDD|212118 cd10807, YdjC_like_3, uncharacterized YdjC-like family proteins from bacteria. This subfamily contains many hypothetical proteins, and belongs to the YdjC-like family of uncharacterized proteins from bacteria. The YdjC-family is represented by an uncharacterised protein YdjC (also known as ChbG) encoded by the chb (N,N'-diacetylchitobiose, also called [GlcNAc]2) or cel operon in Escherichia coli, which encodes enzymes involved in growth on an N,N'-diacetylchitobiose carbon source. The molecular function of this subfamily is unclear
IILCADDFGLSPGVSAAILDLAEAGRLSATSCMVNGPAWPEAAAALRPLRGRADIGLHLNLTEGFPLLAP
GGLLPPLGRLLLRSLLGRLDRAAIRAEIEAQLDAFEEAFGRAPDFVDGHQHVHQLPVIRDALLDLLARRY
PGGRPWLRSTAEPLPAGLPLAGLLKALVLAALGAGALRRLARAGIPTNRGFAGVYDFGPQADYAALLRRW
LAAAGDGPLIMCHPGLPDEELSAADPIAPAREREYAYLASD
>gnl|CDD|212119 cd10808, YdjC, Escherichia coli YdjC-like family of proteins. Uncharacterized subfamily of YdjC-like family of proteins. Included in this subfamily is the uncharacterized Escherichia coli protein YdjC (also known as ChbG), encoded by the chb (N,N'-diacetylchitobiose, also called [GlcNAc]2) or cel operon, which encodes enzymes involved in growth on an N,N'-diacetylchitobiose carbon source. The molecular function of this subfamily is unclear
RLIVNADDFGLHPGVNRAILEAHRAGIVTSTTLMAGGPAFDDAVALARENPGLGVGVHLTLVGGLPVVPP
AEIPSLVDEDGVFLRSYLAFAKRLLTGRIRLSEVERELRAQIERVLDAGIRPTHLDSHQHTHVLPGVLDI
VLDLAARYGIPAVRIPDEPPFFARLAKSGLRRRAGVGLSVLAARARARLRRLGLSTPDGFWGIVAGGALD
EATLRAILDRLPEGVTELMCHPGEDDAALSAPTRWGYHWEEELAALLSP
>gnl|CDD|212120 cd10809, GH38N_AMII_GMII_SfManIII_like, N-terminal catalytic domain of Golgi alpha-mannosidase II, Spodoptera frugiperda Sf9 alpha-mannosidase III, and similar proteins; glycoside hydrolase family 38 (GH38). This subfamily is represented by Golgi alpha-mannosidase II (GMII, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A1), a monomeric, membrane-anchored class II alpha-mannosidase existing in the Golgi apparatus of eukaryotes. GMII plays a key role in the N-glycosylation pathway. It catalyzes the hydrolysis of the terminal both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. GMII is activated by zinc or cobalt ions and is strongly inhibited by swainsonine. Inhibition of GMII provides a route to block cancer-induced changes in cell surface oligosaccharide structures. GMII has a pH optimum of 5.5-6.0, which is intermediate between those of acidic (lysosomal alpha-mannosidase) and neutral (ER/cytosolic alpha-mannosidase) enzymes. GMII is a retaining glycosyl hydrolase of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex; two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. This subfamily also includes human alpha-mannosidase 2x (MX, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A2). MX is enzymatically and functionally very similar to GMII, and is thought to also function in the N-glycosylation pathway. Also found in this subfamily is class II alpha-mannosidase encoded by Spodoptera frugiperda Sf9 cell. This alpha-mannosidase is an integral membrane glycoprotein localized in the Golgi apparatus. It shows high sequence homology with mammalian Golgi alpha-mannosidase II(GMII). It can hydrolyze p-nitrophenyl alpha-D-mannopyranoside (pNP-alpha-Man), and it is inhibited by swainsonine. However, the Sf9 enzyme is stimulated by cobalt and can hydrolyze (Man)5(GlcNAc)2 to (Man)3(GlcNAc)2, but it cannot hydrolyze GlcNAc(Man)5(GlcNAc)2, which is distinct from that of GMII. Thus, this enzyme has been designated as Sf9 alpha-mannosidase III (SfManIII). It probably functions in an alternate N-glycan processing pathway in Sf9 cells
KLKVFVVPHSHNDPGWIKTFEEYYQDQTKHILDNMVDKLSKNPKMKFIWAEISFLERWWDDASPDKKEAV
KKLVKNGQLEIVTGGWVMTDEANSHYFAMIDQLIEGHQWLKENLGVKPKSGWSIDPFGHSPTMPYLLKRA
GFKNMVIQRIHYEVKKYLAQRKALEFMWRQYWDATGSTDILTHMMPFYSYDIPHTCGPDPAVCCQFDFKR
LPGGGESCPWKKPPQPITDDNVAERAELLLDQYRKKSQLYRSNVVLIPLGDDFRYDSDEEWDAQYDNYQK
LFDYINSNPELNVEIQFGTLSDYFNALRKRTGTNTPGFPTLSGDFFTYADRDDDYWSGYY
>gnl|CDD|212121 cd10810, GH38N_AMII_LAM_like, N-terminal catalytic domain of lysosomal alpha-mannosidase and similar proteins; glycoside hydrolase family 38 (GH38). The subfamily is represented by lysosomal alpha-mannosidase (LAM, Man2B1, EC 3.2.1.114), which is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. LAM is expressed in all tissues and in many species. In mammals, the absence of LAM can cause the autosomal recessive disease alpha-mannosidosis. LAM has an acidic pH optimum at 4.0-4.5. It is stimulated by zinc ion and is inhibited by cobalt ion and plant alkaloids, such as swainsonine (SW). LAM catalyzes hydrolysis by a double displacement mechanism in which a glycosyl-enzyme intermediate is formed and hydrolyzed via oxacarbenium ion-like transition states. A carboxylic acid in the active site acts as the catalytic nucleophile in the formation of the covalent intermediate while a second carboxylic acid acts as a general acid catalyst. The same residue is thought to assist in the hydrolysis (deglycosylation) step, this time acting as a general base
LNVHLVPHTHDDVGWLKTVDQYYYGSNNSIQHAGVQYILDSVIEELLKNPDRKFIYVEIAFFSRWWREQS
EDTRQKVKKLVKNGQLEFINGGWCMNDEATTHYEDIIDQMTLGHQFLKDTFGECARPRVGWQIDPFGHSR
TQASLFAQMGFDGLFFGRIDYQDKAQRLKNKEMEFIWRGSPSLGPDADIFTGVLYNHYGPPPGFCFDILC
GDEPIQDDPNLEDYNVDERVDDFVQYAKEQAQHYRTNHIMLTMGSDFQYQNAEMWFKNMDKLIKYVNK
>gnl|CDD|212122 cd10811, GH38N_AMII_Epman_like, N-terminal catalytic domain of mammalian core-specific lysosomal alpha 1,6-mannosidase and similar proteins; glycoside hydrolase family 38 (GH38). The subfamily is represented by a novel human core-specific lysosomal alpha 1,6-mannosidase (Epman, Man2B2) and similar proteins. Although it was previously named as epididymal alpha-mannosidase, Epman has a broadly distributed transcript expression profile. Different from the major broad specificity lysosomal alpha-mannosidases (LAM, MAN2B1), Epman is not associated with genetic alpha-mannosidosis that is caused by the absence of LAM. Furthermore, Epman has unique substrate specificity. It can efficiently cleave only the alpha 1,6-linked mannose residue from (Man)3GlcNAc, but not (Man)3(GlcNAc)2 or other larger high mannose oligosaccharides, in the core of N-linked glycans. In contrast, the major LAM can cleave all of the alpha-linked mannose residues from high mannose oligosaccharides except the core alpha 1,6-linked mannose residue. Moreover, it is suggested that the catalytic activity of Epman is dependent on prior action by di-N-acetyl-chitobiase (chitobiase), which indicates there is a functional cooperation between these two enzymes for the full and efficient catabolism of mammalian lysosomal N-glycan core structures. Epman has an acidic pH optimum. It is strongly stimulated by cobalt or zinc ions and strongly inhibited by furanose analogues swainsonine (SW) and 1,4-dideoxy-1,4-imino-d-mannitol (DIM)
IQAFVIPHSHMDVGWVYTVQESMHAYAANVYTSVVEELMRGKQRRFIAVEQEFFRLWWDGVATDKQKQQV
RQLLSEGRLEFVIGGQVMHDEAVTELDDQILQLTEGHGFLYETFGVRPRFSWHVDPFGASATTPTLFALA
GFNAHLISRIDYDLKAAMQKAKGLQFVWRGSPSLSESQEIFTHVMDQYSYCTPSYIPFSNRSGFYWNGVA
VFPDPPKDGIYPNMSLPVTTQNIHQYAETMVANIKQRAAWFRTPHVLWPWGCDKQFFNASVQFSNMDPLL
DYINQHSSEFGVTVQYATLGDYFQALHNSNLTWEVRGSQDFLPYST
>gnl|CDD|212123 cd10812, GH38N_AMII_ScAms1_like, N-terminal catalytic domain of yeast vacuolar alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38). The family is represented by Saccharomyces cerevisiae alpha-mannosidase (Ams1) and its eukaryotic homologs. Ams1 functions as a second resident vacuolar hydrolase in S. cerevisiae. It aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing alpha-d-mannose residues. Ams1 forms an oligomer in the cytoplasm and retains its oligomeric form during the import process. It utilizes both the Cvt (nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Mutants in either pathway are defective in Ams1 import. Members in this family show high sequence similarity with rat ER/cytosolic alpha-mannosidase Man2C1
NVYGIGNCHIDTAWLWPFSETQQKVARSWSTQCDLMDRYPEYRFVASQAQQFKWLETLYPDLFEKVKEYV
KQGRFHPIGGSWVENDTNMPSGESLARQFLYGQRYFESRFGKRCDTFWLPDTFGYSSQIPQLCRLAGMDY
FFTQKLSWNNINSFPHSTFNWVGIDGTQVLVHMTPVNTYTADASVGDVLRSIKNHKDLENDDTGLLLFGK
GDGGGGPLAEMLEKLRRIRAAANNGAGDLPKVQLGRTVDDFFDDILKR
>gnl|CDD|212124 cd10813, GH38N_AMII_Man2C1, N-terminal catalytic domain of mammalian cytosolic alpha-mannosidase Man2C1 and similar proteins; glycoside hydrolase family 38 (GH38). The subfamily corresponds to cytosolic alpha-mannosidase Man2C1 (also known as ER-mannosidase II or neutral/cytosolic mannosidase), mainly found in various vertebrates, and similar proteins. Man2C1 plays an essential role in the catabolism of cytosolic free oligomannosides derived from dolichol intermediates and the degradation of newly synthesized glycoproteins in ER or cytosol. It can catalyze the cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. Man2C1 is a cobalt-dependent enzyme belonging to alpha-mannosidase class II. It has a neutral pH optimum and is strongly inhitibed by furanose analogs swainsonine (SW) and 1,4-dideoxy-1,4-imino-D-mannitol (DIM), moderately by deoxymannojirimycin (DMM), but not by kifunensine (KIF). DMM and KIF, both pyranose analogs, are normally known to inhibit class I alpha-mannosidase
TIHAMGHCHIDSAWLWPYEETIRKCARSWVTVLRLMEDYPDFTFACSQAQQLEWVKSWYPGLYEEIQERV
KNGRFIPVGGTWVEMDGNLPSGESMVRQFLYGQRFFKEEFGITCKEFWLPDTFGYSAQLPQIMKGCGISR
FLTQKLSWNLVNKFPHHTFFWEGIDGSRVLTHFPPGDSYGMQGKVEEVLKTVANFKDKGRSNHSMMLFGF
GDGGGGPTQNMLERLKRLQDTDGLPRVKLSTPDEFFSAVEKD
>gnl|CDD|212125 cd10814, GH38N_AMII_SpGH38_like, N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, and its prokaryotic homologs; glycoside hydrolase family 38 (GH38). The subfamily is represented by SpGH38 of Streptococcus pyogenes, which has been assigned as a putative alpha-mannosidase, and is encoded by ORF spy1604. SpGH38 appears to exist as an elongated dimer and display alpha-1,3 mannosidase activity. It is active on disaccharides and some aryl glycosides. SpGH38 can also effectively deglycosylate human N-glycans in vitro. A divalent metal ion, such as a zinc ion, is required for its activity. SpGH38 is inhibited by swainsonine. The absence of any secretion signal peptide suggests that SpGH38 may be intracellular
KVHIISHTHWDREWYLPFEEFRMRLIDLIDRLLELLEEDPEFKSFHLDGQTIVLEDYLEVRPEKRERLKK
LIREGKLVIGPWYVLQDEFLTSGEANIRNLLIGKKVAEEFGKSMKIGYFPDTFGHIGQMPQILKGFGIDN
AVFGRGVKPTESQYSEFWWESPDGSRVLGILLANWYSNGNEIPVDEEEAKEFWDKKLADAERYASTDHLL
LMNGCDHQPVQPDLTKAIREANELYPDYEFIHSNFDEYLEALKSELPEDLSTVKGELRSQK
>gnl|CDD|212126 cd10815, GH38N_AMII_EcMngB_like, N-terminal catalytic domain of Escherichia coli alpha-mannosidase MngB and its bacterial homologs; glycoside hydrolase family 38 (GH38). The bacterial subfamily is represented by Escherichia coli alpha-mannosidase MngB, which is encoded by the mngB gene (previously called ybgG). MngB exhibits alpha-mannosidase activity that converts 2-O-(6-phospho-alpha-mannosyl)-D-glycerate to mannose-6-phosphate and glycerate in the pathway which enables use of mannosyl-D-glycerate as a sole carbon source. A divalent metal ion is required for its activity
KVHVVPHTHWDREWYFTTEDSRILLVNHMDEVLDELENNPDFPYYVLDGQSSILDDYLAVRPEDKERIKK
LVKEGRLFIGPWYTQTDELVVSGESIVRNLLYGIKDARKLGGYMKIGYLPDSFGQSAQMPQIYNGFGIDN
AVFWRGVSEDLVKSTEFIWKSLDGSKVLAANIPFGYGIGKYLPEDPDYLKKRLDPILEKLERRATTDNIL
LPNGGDQMPIRKNLPEVIEELNEISPDYEYVISSYEEFFKALEKNKDLLPTIEGELLDPK
>gnl|CDD|212127 cd10816, GH57N_BE_TK1436_like, N-terminal catalytic domain of Gh57 branching enzyme TK 1436 and similar proteins. The subfamily is represented by a novel branching-enzyme TK1436 of hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. Branching enzymes (BEs, EC 2.4.1.18) play a key role in synthesis of alpha-glucans and they generally are classified into glycoside hydrolase family 13 (GH13). However, TK1436 belongs to the GH57 family. It functions as a monomer and possesses BE activity. TK1436 is composed of a distorted N-terminal (beta/alpha)7-barrel domain and a C-terminal five alpha-helical domain, both of which participate in the formation of the active-site cleft
GYFTLVLHAHLPYVRKHGRWPFGEEWLHEAAAETYIPLLRVLERLRDDGVGFRLTLGITPVLMEQLADPY
ILAEFEEYLERKIEAAQEDLARYTQSGESHYEEAARYWHRFFEIALDFFNRLSGDILGAFRKLQDKGYIE
IITSCATHGYLPLLGRDESIRAQIATGVTTYERHFGRKPKGIWLPECAYRPAGYWEYPVAGGFTRPGIEE
FLEESGIRYFFVDTHLIEGGQILSPYGEGNRHLVTDPKSTYQPYWVTPSNVAVFARDPRTGLQVWSAEYG
YPGDGNYREFHKKDPPSGLQYWRITGPKVDLGEKEPYDPDDAAARVEEHARHFVGLLEELLAEHRKGDGP
PGIICAPYDTELFGHWWFEGVQWLEAVLRLLHQNPKVELTTASEYLEQYPPAESIALPEGSWGRGGTHEV
WLN
>gnl|CDD|467263 cd10817, PDZ9_MUPP1-like, PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 9 of MUPP1. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ9 domain is therefore absent from PATJ. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ9 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
HVELPKDQGGLGIAISEEDTENGIVIKSLTEGGPAAKDGRLKVGDQILAVDDESVVGCPYEKAISLLKTA
KGTVKLTVS
>gnl|CDD|467264 cd10820, PDZ_SYNPO2-like, PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNPO2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
CVTLTGGAPWGFRLQGGSEQKKPLQVAKIRKKSKAALAGLCEGDELLSINGKPCADLSHSEAMDLIDSSG
DTLQLLIK
>gnl|CDD|467265 cd10822, PDZ_TAX1BP3-like, PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of TAX1BP3, and related domains. TAX1BP3 (also known as glutaminase-interacting protein 3, tax interaction protein 1, TIP-1, tax-interacting protein 1) may regulate a number of protein-protein interactions by competing for PDZ domain binding sites. TAX1BP3 binds beta-catenin and may act as an inhibitor of the Wnt signaling pathway. It competes with LIN7A (also known as Lin-7A or LIN-7A) for inward rectifier potassium channel 4 (KCNJ4) binding, and thereby promotes KCNJ4 internalization. It may play a role in the Rho signaling pathway, and in the activation of CDC42 by the viral protein HPV16 E6. Binding partners of the TAX1BP3 PDZ domain include beta-catenin, KCNJ4, glutaminase liver isoform (GLS2), rho guanine nucleotide exchange factor 16 (ARHGEF16), rhotekin, and CDK5 regulatory subunit-associated protein 3 (also known as LAPZ). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This TAX1BP3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RIEIHKLRQGENLILGFSIGGGIDQDPSKNPFSYTDKGIYVTRVSEGGPAEKAGLQVGDKILQVNGWDMT
MVTHKQAVKRLTKKKPVLRMLVTR
>gnl|CDD|467635 cd10823, cpPDZ_RseP_YlbL-like_arch, circularly permuted PDZ domains of uncharacterized archaeal proteins related to Escherichia coli Regulator of sigma-E protease (RseP) and Bacillus subtilis YlbL protease. Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of uncharacterized archaeal proteins related to Escherichia coli ResP (also known as Site-2 protease RseP, and YaeL) and Bacillus subtilis YlbL protease. RseP participates in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmaE) protein RseA. YlbL is an S16 protease which participates with another unrelated S41 protease (CtpA) in a dual protease mechanism that promotes DNA damage checkpoint recovery. PDZ domains usually bind in sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP-YlbL archaeal family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus
VEVDRVVEGSPSSKVLPEGMVIESIDGYSVKDLSSYSEALRKFKPGDNIYITTDRGTFKIRLGSNPNNSS
KPYMGIQAI
>gnl|CDD|467636 cd10824, cpPDZ_RseP_YlbL-like, circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP), Bacillus subtilis YlbL protease, and related domains. Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ResP (also known as Site-2 protease RseP, and YaeL), Bacillus subtilis YlbL, and related domains, including archaeal and chloroplast PDZ domains. RseP participates in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmaE) protein RseA. YlbL is an S16 protease which participates with another unrelated S41 protease (CtpA) in a dual protease mechanism that promotes DNA damage checkpoint recovery. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP-YlbL family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus
VVVLSVKPNSPAAKALHAGDLITEIDGQPTKSWQTFIDYIHDKKVGESVKITYKHGNKNEEASLKLTAIP
KEKGTPGIGIRP
>gnl|CDD|467627 cd10827, cpPDZ3_ScNma111-like, circularly permuted third PDZ domain (PDZ3) of Saccharomyces cerevisiae pro-apoptotic serine protease Nma111p and related domains. Third PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the HtrA-type protease Saccharomyces cerevisiae Nma111p (also known as Ynm3p), and related domains. Nma111p is a nuclear serine protease which mediates apoptosis through proteolysis of the apoptotic inhibitor Bir1p. Nma111p is composed of two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This ScNma111-like PDZ3 domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation places both beta-strands A and B on the C-terminus
ARIRGVPEEWIKKMEEESENRLQFISVSRVSAPSLTEEKNPLKTGDIILSVNGKLVKRMRDLDGMYSTQS
LDFKIVRQGKEMDLKIK
>gnl|CDD|467628 cd10828, cpPDZ_Tricorn-protease, circularly permuted PDZ domain of Tricorn protease, and related proteins. permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Tricorn protease, and related domains. The tricorn protease can degrade oligopeptides (which may have been generated by the proteasome) and channel the products to F1, F2 and F3 proteases which, in turn, catalyze the terminal degradation step yielding free amino acids. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. The tricorn family PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus
IGLLGADFKYDESGCYRIARIYKGDSWNENERSPLAAPGVDVRVGDLIVAIDGEPVGAVKNPYSLLVGKA
GTQVVLTVSPKGGGDVRRVTVVP
>gnl|CDD|467266 cd10830, PDZ_MPP1-like, PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1, and related domains. MPP1 (also known as MAGUK p55 subfamily member 1, erythrocyte membrane protein p55, EMP55) is a membrane-associated guanylate kinase (MAGUK)-like protein which forms a complex with protein 4.1 and glycophorin C (GPC) at the cytoplasmic face of the plasma membrane; this complex is essential for cytoskeleton-membrane linkage in erythrocytes and many non-erythroid cells, and participates in the determination of membrane stability and cell shape. MPP1, by interacting with various scaffold proteins and cytoskeletal proteins in the postsynaptic density, also plays an important role in organizing synaptic and non-synaptic structures. MPP1 is also a component of the Crumbs protein complex in the mammalian retina and may link the Usher protein network and the Crumbs protein complex. The MPP1 PDZ domain binding partners include GPC, ABCC4, and CADM1/Necl-2/SynCAM1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RLVQFEKNTEEPMGITLKLNEKQSCIVARILHGGMIHRQGSLHVGDEILEINGKSVTNHSVDQLQKMLKE
TKGMVSLKVIP
>gnl|CDD|467267 cd10831, PDZ_CASK-like, PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CASK, Caenorhabditis elegans Lin-2, and related domains. CASK and Lin-2 are membrane-associated guanylate kinase (MAGUK)-like proteins. CASK (also known as Calcium/calmodulin-dependent protein kinase, CAKI, and Camguk) has a role in synaptic transmembrane protein anchoring and ion channel trafficking. CASK may regulate transmembrane proteins that bind calcium, calmodulin, or nucleotides; it regulates the Drosophila ether a go-go (eag) potassium channel, and also regulates autophosphorylation of CaMKII. CASK binding partners include the transcription factor TBR1, and cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. Lin-2, as a component of the CLin-10-Lin-2-Lin-7 complex, plays a role in controlling the basolateral localization of the EGF receptor Let-23; this complex also associates with the neuron-specific motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules. CASK may also function in targeting or scaffolding of the protein parkin which is selectively truncated by a Parkinson's disease-causing mutation; the C-terminus of parkin functions as a class II PDZ-binding motif that binds CASK. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP6-MPP2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RLVQFQKNTDEPMGITLKMNEDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLRE
ARGSITFKIVP
>gnl|CDD|467268 cd10832, PDZ_MPP6-MPP2-like, PDZ domain of membrane palmitoylated protein 6 (MPP6), MPP2, and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP6, MPP2, and related domains. MPP6 (also known as MAGUK p55 subfamily member, Protein associated with Lin-7, 2 (PALS2), Veli-associated MAGUK 1, and VAM-1) is a membrane-associated guanylate kinase (MAGUK)-like protein. MPP6 is a regulator of Lin-7 expression and localization. MPP6 is also known to bind cell-adhesion protein, nectin-like molecule-2 (Necl-2), and localize to the basolateral plasma membrane in mammalian epithelial cells. MPP2 (also known as MAGUK p55 subfamily member 2) is a postsynaptic protein that links SynCAM1 cell adhesion molecules to core components of the postsynaptic density. Other members of this family include the Drosophila Vari protein, an essential basolateral septate junction protein which interacts with the cell-adhesion protein neurexin IV. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP6-MPP2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RMVGIRKNPGEPLGVTVRLEEGELVIARILHGGMIDRQGLLHVGDIIKEVNGVPVGSPEQLQEMLKNASG
SVTLKILP
>gnl|CDD|467269 cd10833, PDZ1_PDZD7-like, PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the first PDZ domain of the canonical isoform of PDZD7- isoform 1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD7-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
IHTVTVEKSPDGSLGFSVRGGSEHGLGIFVSKVEEGSAAERAGLCVGDKITEVNGVSLENITMSSAVKVL
TGSNRLRMVVRRMG
>gnl|CDD|467270 cd10834, PDZ2_PDZD7-like, PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the second PDZ domain of the canonical isoform of PDZD7- isoform 1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD7-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
RRIVHLYTTSDDYCLGFNIRGGSEYGLGIYVSKVDPGGLAEQNGIKVGDQILAVNGVSFEDITHSKAVEV
LKSQTHLMLTIKEVG
>gnl|CDD|467629 cd10838, cpPDZ_HhoA-like, circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB, and HtrA and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the cyanobacterial Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB and HtrA, and related domains. These three proteases are functionally overlapping, and are involved in a number of key physiological responses, ranging from protection against light and heat stresses to phototaxis. HhoA assembles into trimers, mediated by its protease domain and further into a hexamer by a novel interaction between the PDZ domains of opposing trimers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This HhoA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus
HPYLGIQMTTLTPELAQQNNRNPNSPVRIPEVDGVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADD
VQRIVEQAGVGEELELTVLRGDRRQTLAVKPGDL
>gnl|CDD|467630 cd10839, cpPDZ1_DegP-like, circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine endoprotease DegP and related domains. PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Escherichia coli DegP (also known as heat shock protein DegP and Protease Do) and related domains. DegP belongs to the HtrA family of housekeeping proteases. It acts as a protease, degrading transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and as a molecular chaperone at low temperatures. DegP has two PDZ domains in addition to the protease domain; its PDZ1 domain is responsible for identifying the distinct substrate sequences that affect degradation (degron) of the substrate sequence, and its PDZ2 domain is responsible for combining with other DegP monomers to form a stable oligomer structure. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This DegP family PDZ domain 1 is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus
RGWLGVQIQELTPDLAESFGLKEPKGALVAQVLPDSPAAKAGLKAGDVILSLNGKPITSSADLRNRVATT
KPGTKVELKILRDGKEKTLTV
>gnl|CDD|380680 cd10843, DSRM_DICER, double-stranded RNA binding motif of endoribonuclease Dicer and similar proteins. Dicer (also known as helicase with RNase motif (HERNA), or helicase MOI) is a double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. It cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. Dicer contains a double-stranded RNA binding motif (DSRM) at the C-terminus. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
RSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGRFKGVGRNYRIAKSAAARRALRSLK
>gnl|CDD|380681 cd10844, DSRM_TARBP2_rpt2, second double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and similar proteins. TARBP2 (also known as TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)) participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. TARBP2 contains three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
NPVGALQELVVQKGWRLPEYTVTQESGPAHRKEFTMTCRVERFIEIGSGTSKKLAKRNAAAKMLLRI
>gnl|CDD|380682 cd10845, DSRM_RNAse_III_family, double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins. RNase III (EC 3.1.26.3; also known as ribonuclease 3) digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. It is involved in the processing of rRNA precursors, viral transcripts, some mRNAs, and at least 1 tRNA (metY, a minor form of tRNA-init-Met). It cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs. The cleavage can occur in assembled 30S, 50S, and even 70S subunits and is influenced by the presence of ribosomal proteins. The RNase III family also includes the mitochondrion-specific ribosomal protein mL44 subfamily, which is composed of mitochondrial 54S ribosomal protein L3 (MRPL3) and mitochondrial 39S ribosomal protein L44 (MRPL44). Members of this family contain an RNase III domain and a C-terminal double-stranded RNA binding motif (DSRM). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KDYKTALQEYLQKRGLPLPEYELVEEEGPDHNKTFTVEVKVNGKVIGEGTGRSKKEAEQAAAKAALEKL
>gnl|CDD|211315 cd10909, ChtBD1_GH18_2, Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with family 18 glycosyl hydrolases. This subfamily includes a Toxoplasma gondii ME49 protein annotated as a putative mannosyl-oligosaccharide glucosidase. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements
ERSDGRCGKGFPLLDGYPPVCDPDSEHPCCSNGGYCGSGADHCDCPGCIDF
>gnl|CDD|350234 cd10910, PIN_limkain_b1_N_like, N-terminal LabA-like PIN domain of limkain b1 and similar proteins. Limkain b1 is a human autoantigen, localized to a subset of ABCD3 and PXF marked peroxisomes. Limkain b1 may be a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. Limkain b1 contains multiple copies of LOTUS domains and a conserved RNA recognition motif, this and similar domain architectures are shared by several members of this family, and a function of these architectures in RNA binding or RNA metabolism has been suggested. The function of the N-terminal domain is unknown. This subfamily belongs to LabA-like PIN domain family which includes Synechococcus elongatus PCC 7942 LabA, human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
KTGVFWDIENCPVPDGYDARRVGPNIRRALRKLGYSGPVSITAYGDLSKVPKDVLSELSSSGVSLVHVPH
GGKKAADKKILVDMLLWALDNPPPANIMLISGDVRDFAYALSRLRSRGYNVLLAYP
>gnl|CDD|350235 cd10911, PIN_LabA, PIN domain of Synechococcus elongatus LabA (low-amplitude and bright) and related proteins. This subfamily contains Synechococcus elongatus PCC 7942 LabA which participates in cyanobacterial circadian timing, it is required for negative feedback regulation of the autokinase/autophosphatase KaiC, a central component of the circadian clock system, and appears to be necessary for KaiC-dependent repression of gene expression. This subfamily belongs to the LabA-like domain family which includes the N-terminal domain of limkain b1, a human autoantigen localized to a subset of ABCD3 and PXF marked peroxisomes. Also included in the LabA-like domain family are human ZNF451, uncharacterized Bacillus subtilis YqxD, uncharacterized Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously Pseudomonas putida S16 NicB, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
ERVAVFIDGANLYYAAKKLGWKIDYEKLLKYLVGGRELVRAYYYTAVDDEEDEKQQKFLDALRKIGYEVV
TKPLKEFRDEGGGSVKGNVDVEIAVDMLRLADKYDTAILVSGDGDFAPLVEYLQRKGKRVEVVSFRGSTS
KELRRAADRFIDLD
>gnl|CDD|350236 cd10912, PIN_YacP-like, PIN_domain of Bacillus subtilis YacP/Rae1 and related proteins. Bacillus subtilis YacP, also known as Rae1, is an endoribonuclease involved in ribosome-dependent mRNA decay. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. PIN domains were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
ILLVDGYNVIGAWPELKKLKRESLEEARDKLIEELANYQAYKGYEVIVVFDAYYVKGGLEKEEESGGVEV
VFTKEGETADSYIERLVASLKRRCKRVTVATSDRAEQRTVFGQGALRISARELLKEIERAKEEIRRSKRR
TK
>gnl|CDD|199211 cd10913, Peptidase_C25_N_gingipain, gingipain subgroup of the Peptidase C25 family N-terminal domain. Gingipain, produced by Porphyromonas gingivalis, exemplifies the Peptidase family C25, a unique class of cysteine proteases. P. gingivalis is one of the primary gram-negative pathogens that causes periodontitis, a disease also associated with other diseases such as diabetes and cardiovascular disease. The gingipain subgroup contains extracellular Arg- and Lys-specific proteinases called Arg-gingipain (Rgp) and Lys-gingipain (Kgp); RgpA and RgpB are homologous Arg-specific gingipains encoded by two closely related genes, rgpA and rgpB, while Lys-specific gingipain is encoded by the single kgp gene. Mutant studies have shown that, among the large quantities of proteolytic enzymes produced by P. gingivalis, these three proteases are major virulence factors of this bacterium. All three genes encode an N-terminal pre-pro fragment, followed by the protease domain; however, rgpA and kgp also encode additional C-terminal HA (hemaglutinin/adhesion) subunits which consist of several sequence-related adhesion domains. Although unique, their cysteine protease active site residues (His and Cys) forming the catalytic dyad, are well-conserved, cleaving the C-terminal peptide bond with Arg or Lys residues. Gingipains are evolutionarily related to other highly specific proteases including caspases, clostripain, legumains, and separase. Gingipains function by dysregulating host defense and inflammatory responses, and degrading host proteins, e.g. tissue, cells, matrix, plasma and immunological proteins. It has been suggested that they enhance gingival crevicular fluid (GCF) production through activation of the kallikrein/kinin pathways, thus increasing vascular permeability and causing gingival inflammation, a distinctive feature of periodontitis. RgpA and RgpB are also able to cleave and activate coagulation factors IX and X in order to activate prothrombin to produce thrombin, which in turn increases production of GCF. The gingipains also play a pivotal role in the survival of P. gingivalis in the host by attacking the host defense system through cleavage of several immunological molecules, while at the same time evading the host-immune response by dysregulating the cytokine network
TDLDESRPRMLVIYGNNFTSTIQPFVAWKKQKGYDVEVVSTATIGTTNAAIKAYIQNAYNNPTTAPDYVL
LVGDTDGIPTIPTNGEGGVTDYYYTQLAGNDYYPEVFIGRFSAESAAELTTQVNKTIMYEKNIMPDDSWL
NKALLIAGAEGGGGATHGIGQINYSGISYYNVNHNITDLSYLTPIYKPGAPATQINQAINQGVGFINYTG
HGSETGWGTPHFTTSNINALTNGNKLPFVVSVACVTGNFDNSTCFAEAWMRAGNDGAPGGAVAFIGSTIS
STQTWANPMRGQDEFDDILAEGHPANWKRTMGSALLNGKLYLVQVYGSDQANYYAETWNIFGDPSLMV
>gnl|CDD|199212 cd10914, Peptidase_C25_N_1, uncharacterized subgroup of the Peptidase C25 family N-terminal domain. Domains in this subgroup are uncharacterized members of the Peptidase family C25 N-terminal domain family. Peptidase family C25 is a unique class of cysteine proteases, exemplified by gingipain, which is produced by Porphyromonas gingivalis. P. gingivalis is one of the primary gram-negative pathogens that causes periodontitis, a disease that is also associated with other diseases such as diabetes and cardiovascular disease. Gingipains are a group of extracellular Arg- and Lys-specific proteinases called Arg-gingipain (Rgp) and Lys-gingipain (Kgp); RgpA and RgpB are homologous Arg-specific gingipains encoded by two closely related genes, rgpA and rgpB, while Lys-specific gingipain is encoded by the single kgp gene (also called prtK, prkP). Mutant studies have shown that, among the large quantities of proteolytic enzymes produced by P. gingivalis, these three proteases are major virulence factors of this bacterium. All three genes encode an N-terminal pre-pro fragment, followed by the protease domain; however, rgpA and kgp also encode additional C-terminal HA (hemaglutinin/adhesion) subunits which consist of several sequence-related adhesion domains. Although unique, their cysteine protease active site residues (His and Cys) forming the catalytic dyad are well-conserved, cleaving the C-terminal peptide bond with Arg or Lys residues. Gingipains are evolutionarily related to other highly specific proteases including caspases, clostripain, legumains, and separase. Gingipains function by dysregulating host defense and inflammatory responses, and degrading host proteins, e.g. tissue, cells, matrix, plasma and immunological proteins. They are proposed to enhance gingival crevicular fluid (GCF) production through activation of the kallikrein/kinin pathways, thus increasing vascular permeability and causing gingival inflammation, a distinctive feature of periodontitis. RgpA and RgpB are also able to cleave and activate coagulation factors IX and X in order to activate prothrombin to produce thrombin, which in turn increases production of GCF. The gingipains also play a pivotal role in the survival of P. gingivalis in the host by attacking the host defense system through cleavage of several immunological molecules, while at the same time evading the host-immune response by dysregulating the cytokine network
LPTLQGLRGADYILITHGLLSDALRPLAEQRRNQGWNPLLVDVEQIYDQFSAGIVDPNAIRDFLRYAAST
WPPAPRFVLLVGDGTFDPKDYLGRGLPNLIPPLLAMVDPWLGETASDNRYAQLDGDDPLPDLAIGRLPAT
TVEELERLVAKILAYEASPAAAWRGKALFIADNPDSSGDFPRLSDQIAGLLPSQTTIKRAYYTPIGPAAA
RALAQELLAALNQGAELVHYVGHGGQDQWATTDPDLPTLLDLSDVGSLTNSPALPVLLSMTCLTGAFQHP
SGTSLAEALVLAPDGGAVAVWASSGLGVAHGHDNLLRGLVRGLWSIGGTPLGQAIAAGKLELAAAGGCRD
LLETFNLLGDPALRL
>gnl|CDD|199213 cd10915, Peptidase_C25_N_2, uncharacterized subgroup of the Peptidase C25 family N-terminal domain. Domains in this subgroup are uncharacterized members of the Peptidase family C25 N-terminal domain family. Peptidases family C25 are a unique class of cysteine proteases, exemplified by gingipain, which is produced by Porphyromonas gingivalis. P. gingivalis is one of the primary gram-negative pathogens that causes periodontitis, a disease that is also associated with other diseases such as diabetes and cardiovascular disease. Gingipains are a group of extracellular Arg- and Lys-specific proteinases called Arg-gingipain (Rgp) and Lys-gingipain (Kgp); RgpA and RgpB are homologous Arg-specific gingipains encoded by two closely related genes, rgpA and rgpB, while Lys-specific gingipain is encoded by the single kgp gene. Mutant studies have shown that, among the large quantities of proteolytic enzymes produced by P. gingivalis, these three proteases are major virulence factors of this bacterium. All three genes encode an N-terminal pre-pro fragment, followed by the protease domain; however, rgpA and kgp also encode additional C-terminal HA (hemaglutinin/adhesion) subunits which consist of several sequence-related adhesion domains. Although unique, their cysteine protease active site residues (His and Cys) forming the catalytic dyad are well-conserved, cleaving the C-terminal peptide bond with Arg or Lys residues. Gingipains are evolutionarily related to other highly specific proteases including caspases, clostripain, legumains, and separase. Gingipains function by dysregulating host defense and inflammatory responses, and degrading host proteins, e.g. tissue, cells, matrix, plasma and immunological proteins. They are proposed to enhance gingival crevicular fluid (GCF) production through activation of the kallikrein/kinin pathways, thus increasing vascular permeability and causing gingival inflammation, a distinctive feature of periodontitis. RgpA and RgpB are also able to cleave and activate coagulation factors IX and X in order to activate prothrombin to produce thrombin, which in turn increases production of GCF. The gingipains also play a pivotal role in the survival of P. gingivalis in the host by attacking the host defense system through cleavage of several immunological molecules, while at the same time evading the host-immune response by dysregulating the cytokine network
MPIDVIQETIPDYLIITNNKLIGEFQRLADWRTQKGVPTLVKSVEDIGKEYQGSDLQEKIRNYIIECYHT
WPLLFVLLGGDTNVIPARGYYIAYAYSDAEYPADAYYSDLDGDWNANGNHIYGETGDGMDLDPEVYIGRF
PVEDIEEAKNFINKLLMYEKNPETENVSTAYLMGELLISAYISKDESKDSLNGYLSHYPQITKWYLFDHY
NWTCPYHRDSIAPNWQPETLGLAFDTDTTYHAADELNKEHFLSALSDGGHIVYHMGHSNPTALGASKHES
IYIQDANNLTNGDYPLFMYTQGCYPAAFDERADDCIAEHFLTNPLGGAVAFIGNSRYGWADETYQSNNFA
SQYYRRQFYSDFIHIGTALNQSKNDNDPSAVYTGVMRWEYYELNLFGDPAMMV
>gnl|CDD|213021 cd10916, CE4_PuuE_HpPgdA_like, Catalytic domain of bacterial PuuE allantoinases, Helicobacter pylori peptidoglycan deacetylase (HpPgdA), and similar proteins. This family is a member of the very large and functionally diverse carbohydrate esterase 4 (CE4) superfamily. It contains bacterial PuuE (purine utilization E) allantoinases, a peptidoglycan deacetylase from Helicobacter pylori (HpPgdA), Escherichia coli ArnD, and many uncharacterized homologs from all three kingdoms of life. PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as a homotetramer. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of polysaccharide deacetylase (DCA)-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. However, in contrast with the typical DCAs, PuuE allantoinase and HpPgdA might not exhibit a solvent-accessible polysaccharide binding groove and only recognize a small substrate molecule. ArnD catalyzes the deformylation of 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol
AVSVTVDVEGWAGGAASHGAPMAPAAYSWGRYGLRVGIPRLLDLLDRHGVRATFFVPGRVAERFPDAVRA
IVAAGHEIAAHGYAHEDVLALSREQEREVLLRSLELLEELTGQRPTGWRSPGLTFSPDTLELLAELGYLY
DGDTYDDDLPYYWRDATGGGPILELPYTTVLNDLRFFMGGGGLPRAFYENWKEQFDVLYARGRYLSLTLH
PRVIGRPARAAALDRFLRYVKSHPDVWFATHDEIARH
>gnl|CDD|213022 cd10917, CE4_NodB_like_6s_7s, Catalytic NodB homology domain of rhizobial NodB-like proteins. This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal
KVVALTFDDGPDPEYTPKILDILAEYGVKATFFVVGENVEKHPDLVRRIVAEGHEIGNHTYSHPDLTKLS
PEEIRAEIERTQDAIEEATGVRPRLFRPPYGAYNPEVLAAAAELGLTVVLWSVDSLDWKDPSPDQIVDRV
LAGLKPGSIILLHDGGGTTVEALPRIIDALK
>gnl|CDD|213023 cd10918, CE4_NodB_like_5s_6s, Putative catalytic NodB homology domain of PgaB, IcaB, and similar proteins which consist of a deformed (beta/alpha)8 barrel fold with 5- or 6-strands. This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes bacterial poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB, hemin storage system HmsF protein in gram-negative species, intercellular adhesion proteins IcaB, and many uncharacterized prokaryotic polysaccharide deacetylases. It also includes a putative polysaccharide deacetylase YxkH encoded by the Bacillus subtilis yxkH gene, which is one of six polysaccharide deacetylase gene homologs present in the Bacillus subtilis genome. Sequence comparison shows all family members contain a conserved domain similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, which consists of a deformed (beta/alpha)8 barrel fold with 6 or 7 strands. However, in this family, most proteins have 5 strands and some have 6 strands. Moreover, long insertions are found in many family members, whose function remains unknown
PVVLTFDDGYRDNYTYALPILKKYGLPATFFVITGYIGGGNPWWAPAPPRPPYLTWDQLRELAASGVEIG
SHTHTHPDLTTLSDEELRRELAESKERLEEELGKPVRSFAYPYGRYNPRVIAALKEAGYKAAFTTDPGLN
SPGDDPYALPRINVSGD
>gnl|CDD|200545 cd10919, CE4_CDA_like, Putative catalytic domain of chitin deacetylase-like proteins from insects and similar proteins. Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues. CDAs have been isolated and characterized from various bacterial and fungal species and belong to the larger carbohydrate esterase family 4 (CE4). This family includes many CDA-like proteins, mainly from insects, which contain a putative CDA-like catalytic domain similar to the catalytic NodB homology domain of CE4 esterases. Some family members have an additional chitin binding domain (ChBD), or an additional low-density lipoprotein receptor class A domain (LDLa), or both. Due to the lack of some catalytically relevant residues, several insect CDA-like proteins are devoid of enzymatic activity and may simply bind to chitin and thus influence the mechanical or permeability properties of chitin-containing structures such as the cuticle or the peritrophic membrane. This family also includes many uncharacterized hypothetical proteins from bacteria, exhibiting high sequence similarity to insect CDA-like proteins
PQFVLFTFDDAINELNTDAVIQEIADGTNNNGGCPIPATFFVSTNYTDCSLVKQLWREGHEIATHTVTHV
PDDSNASVDEWEEEIAGQREWLNKTCGIPLEKVVGFRAPYLAYNPNTREVLEENGFLYDSSIPEPYTPSG
TNRLWPYTLDYGIPQDCNLVPGSCSPTERYPGLWEVPLYTLQDGNDTTGDSYYCTPDDGPLNGDSFYALL
KYNFDRHYNGNRAPFGIYLHAAWLSPPYSERRAALEKFLDYALSKPDVWFVTNSQLLDWMQNP
>gnl|CDD|200546 cd10920, CE4_WbmS, Catalytic domain of a putative polysaccharide deacetylase WbmS from Bordetella bronchiseptica and similar proteins. This family is represented by a putative polysaccharide deacetylase encoded by the O-antigen-related gene wbmS in Bordetella bronchiseptica. Although its precise function remains unknown, it has been suggested that WbmS might be involved in the biosynthesis of O-antigen, an important component of the gram-negative bacterial outer membrane, and may also play a role in sugar phosphate transfer. Structural superposition and sequence comparison show that WbmS consists of a conserved domain similar to the 7-stranded barrel catalytic domain of polysaccharide deacetylases (DACs) from the carbohydrate esterase 4 (CE4) superfamily, which removes N-linked acetyl groups from cell wall polysaccharides
EISDIDINFKQSLDAIFITFDIDWASDFVIETCVELFEEANIPATWFATHMSPLLKKIIQNPLFELGIHP
NFNPLLSGDQGGDYQEILDYYLEIVPQAKVFRSHSLYADSRILTELYERGIRYESNICTPLDAGVPLSPF
VHWSGLIRFPYFWEDDIACLYKLDLKFSQASFFEQPGIKVFNFHPIHIYLNTESLERYEDIKDFVSNPDW
LSFSVDRVANKTMFGSTDFLEEL
>gnl|CDD|200547 cd10921, CE4_MJ0505_like, Putative catalytic domain of uncharacterized protein MJ0505 from Methanocaldococcus jannaschii and similar proteins. This family contains an uncharacterized protein MJ0505 from Methanocaldococcus jannaschii and its prokaryotic homologs. Although their biochemical properties remain to be determined, members in this family is composed of a seven-stranded barrel with a detectable sequence similarity to the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups of cell wall polysaccharides and belong to a larger carbohydrate esterase 4 (CE4) superfamily
IPKPIILVHDVSPVYFEDLKEITAIIDKYGCSNSTILFVIPNHANKHPLRKDPDFVNYLHELEKEGYKVE
LHGYDHIYHEFNCNKTTAEEKLEKALEILSALGFDNITLFLPPRYAISEDSLKVILEHNFTVILKDKLIY
PNGTCYRITNREYTWYLGKNRAKIRLNIAKFDYKHTRGKFYLSIHPKAVNYGGGLEFLDEFLNFTK
>gnl|CDD|200548 cd10922, CE4_PelA_like_C, C-terminal Putative NodB-like catalytic domain of PelA-like uncharacterized hypothetical proteins found in bacteria. This family is represented by a protein PelA of unknown function that is encoded by a gene in the pelA-G gene cluster for pellicle production and biofilm formation in Pseudomonas aeruginosa. PelA and most of the family members contain a domain of unknown function, DUF297, in the N-terminus and a C-terminal domain that shows high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
NGRRLFFSHVDGDGFVSKAEVPGSPLAGEVLLREILEKYPLPTTVSVIEGELDPDGYPKLAPQGEKIARE
IFALPQVEVASHTYSHPFNWAPFEGYDPKEYLADYDEIPLRVPGYPFDLHREIVGSTDYINERLAPPGKP
VRVLLWSGDCLPPAAAVALAYEAGLLNMNGGDTRISRTNPSLTAVSPLGRPVGGYLQVYAPLSNENVYTN
LWTGPYYGFRRVIETFRLTDSPRRLKPIDIYYHFYSGEKEASLKALEQVYDWALKQ
>gnl|CDD|200549 cd10923, CE4_COG5298, Putative NodB-like catalytic domain of uncharacterized proteins found in bacteria. This family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily. Some family members contain an additional copper amine oxidase N-terminal domain
KRALVRLEDVSPGGDPEKLKEIADYLYSENIPFHVAVIPVYVDPKTGIDNDITLSDNPELVAALKYLQAR
GGSIILHGYTHQYGGGVSGDGFEFWDAKNDAPLAEDSQAWAEQRVEKGLQILKELGLPPVAFETPHYTAS
PEQYKAIEQYFPTAYERRQYYVDDRSGGQFPPYIVSDQYGTLVIPENLGYVDPNNFTVDVVLENARINRV
VRDGLASFFFHPYLELSYLKQKVDGDGAQVVTFITLSDLQ
>gnl|CDD|200550 cd10924, CE4_COG4878, Putative NodB-like catalytic domain of uncharacterized proteins found in bacteria. The family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
INSKVFYIDDFPSPVPNGDNKDIKREYNMSISEFYYKVWWPDMKKLAERYGIKYTGVMIENYNNKTDPPF
EFFEEKDTDTFIYYGRELLKSGGELGIHGYNHQPLVLPDYTDEELLYVPWPDEEDMVESLKELIKFIKSL
FPNYEIRSYVPPSNILSQEGREALKKAFPTLKTIASTYTGDDEKGPYIQEFGVDPDGIYELPRITSGYYP
DDDLLLTAVSALNNLGVVSHFVHPDDVLDAERSANKGWEELFKSLEKFMKEIKEKYPWLRNLT
>gnl|CDD|200551 cd10925, CE4_u1, Putative catalytic domain of uncharacterized bacterial proteins from the carbohydrate esterase 4 superfamily. This family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
MYIIRLDDATPYMDWSKWDKMEDILDKYGIKPLVGVIPDNQDPKLRIEPADEDFWDKVRGWQDKGWTIAL
HGYNHVYVTRDGGLNPVNSRSEFAGVPLEEQKEKIAAGKAILQKEGIITDIFMAPSHTFDKNTLRALKDE
TFIIISDGIANDPYKRGGFTFIPQQSGRVRKLPFGVVTFCYHPNTMNEDEFDRLERFIKKNRERSFISAA
EKDEKL
>gnl|CDD|200552 cd10926, CE4_u2, Putative catalytic domain of uncharacterized bacterial proteins from the carbohydrate esterase 4 superfamily. This family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
PDGKGGLVLNWHVDSSIAIKSLAQLKKEGVFNKGPFSIHITAGPDTNQPGDGLGFDAPNNPKGRELVKGL
QARGHAIGSHGGWIHNYFGDNINETNQAEFEEYLVLNNDALQAITGKPIREYSAPGGNHPPWVTRWLEQH
GVVAYYYTGNTGSGPTRTYLNGKLVSPKLWAFPVTPFGKYATFEEAKRGHVPEAEVKNWLTSLIDFVAAN
RVIRLIYTHPPGAPLYLNALRALLDYANTLQQEGKFKWYTMSE
>gnl|CDD|200553 cd10927, CE4_u3, Putative catalytic domain of uncharacterized bacterial proteins from the carbohydrate esterase 4 superfamily. This family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
NQPLIILKLDDLKATGGIVHPKWQRVIAFAEQRDIKLSIGIIGNSLETDKPAYFDWIKERAATGGIEFWN
HGYDHKRWGEGGVKLTEFRGTSLEHQKESILKTQTLAKEKLGITFTTFGAPYNSTDANTARVLAEIPDIK
VWLYKPESDVAGKFVLRRINKVNIEYPVHKPNFEKFLEGYFDKSKEPPYIVIQGHPRSWDEERFEEFVKI
VDFLKPEGVKFVTPSEY
>gnl|CDD|200554 cd10928, CE4_u4, Putative catalytic domain of uncharacterized bacterial proteins from the carbohydrate esterase 4 superfamily. This family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
DLWWRDDDAGAPTPALDRLLDLFGRHSVPLALAVIPAWRTDALLKALAGDPLAAVHQHGWAHVNHAPPGK
KKQEFGPSRPLEDVLAELGAGLARLEALFGDRFVPAFVPPWNRLDPGLLPALGGLGYSALSRFGPRKPPP
PPGLPRLDVHVDLHDWKGKRGFRGDEILLSALARRLASRRRWDEPVGILTHHLVHDEAAWEFLDALLAAL
AAHPAARWLDPA
>gnl|CDD|200555 cd10929, CE4_u5, Putative catalytic domain of uncharacterized bacterial proteins from the carbohydrate esterase 4 superfamily. This family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
GSFVISLDFELAWGVRDKRSVPEYEENLLGAREAIPRLLELFDEYNIPATWATVGFLFHFAPSLIDLIAS
TPGQEIGSHTFSHYYCLEEGQTREVFEADLEAAKKAASKYGVDLRSFVFPRNQVNVGYLDVLAEHGIKCY
RGNEPSWLYQEGGTLKLSLLRRAPRLVDPYVNLSGLVNIPASLFLFGFFLRPYSKRLAFLEDLRLRRIKR
GMTYAAKNDGIFHLWWHPHNFGKDTEENLSFLEEILEHLAALREEYGLESLTM
>gnl|CDD|200556 cd10930, CE4_u6, Putative catalytic domain of uncharacterized bacterial proteins from the carbohydrate esterase 4 superfamily. This family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
GYDAAITMRLDCDEDIESARPLWEAYRTLGVPFSLAVHTTNLLKPEHFDILREVLASGGALLSHTATHAP
NWGGSYEKAKAEAETSRQCLESFTGDVVRYAVSPFHQNPPYAMAALEDAGYSGCVGGIIRNDPEFLLARG
GYIAGLPEGFVGHSQQCMLHGDCMLKEGDPLAIFKQAFDCAIAARTLFGYLDHPFSSRYQYGWPSEEERI
KAHEKLIRHIRSRARNPLFLSEEQALDFLR
>gnl|CDD|200557 cd10931, CE4_u7, Putative catalytic domain of uncharacterized bacterial proteins from the carbohydrate esterase 4 superfamily. This family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
FAVCLTHDVDDPYDTFDWLMDLEKKYGVRSTFFFLAGDYSPYDDGNYSYNDPKIRSLIKEIADRGWEIGL
HGSYNSYTDPEKLKKEKERLEKILGRPVTGGRQHYLRFDLPETWRNLADAGFTYDSTMGYADVAGFRAGT
CFPFRFYDLNTERQLPLLEHPLVIMDCTLFGYKYMNPEEALEEIKQLIDEVKKVGGVFTLLWHNSSFSEK
EWPGWKKLYEEILK
>gnl|CDD|200558 cd10932, CE4_u8, Putative catalytic domain of uncharacterized bacterial proteins from the carbohydrate esterase 4 superfamily. This family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
MKLILTLDYELFFGGKSGTVQKCLIEPTQLLLKILDKVGVKLTFFVDVGMLEKLKELSERFPKTEYDYNA
IKNQLRELVAQGHDIQLHLHPHWEDAYYDGGGWVLDTSRYYLLDFSEEEIIEMFRRGKELLEEIARPVDP
DYTIIAFRAGGWCVQPFEKISRALQENGIKIDSSVFPGGRLDNKVHNFDFRSAPSNAQWRFEDDVLTPDP
NGYFLEVPISSYKISPLFKWKLALRRKLNKSKAKSFGDGTAMLAGESQGIRSKPSRKNDFAYLSSQRYIQ
SLLKAFKERKASKSGRKPFVLIGHPKDLSPSSLSALDYFLKSHK
>gnl|CDD|200559 cd10933, CE4_u9, Putative catalytic domain of uncharacterized bacterial proteins from the carbohydrate esterase 4 superfamily. This family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
RVLLTVDTELWPNGANRDDQKFPPAFRRSIYGETDGGEYGLPLILDILNRYGLKGTFFVEPLPALRFGDE
PLEDIVRLIVARGHDVQLHLHPEWLDEARPLLPGGDRNRRHMHDYSLEEQTQLIEEGRDLLKRAGAPDPI
AFRAGGFGANDDTLRALAANGIRIDSSYNYCYLGPGCNISLERTLNGPVKIEGVLEVPVTVFKDGPGRLR
HAQVTALSLDEMRRALLHARDSGLSSFVLLLHSFELLNLKRERRRFRPDRIVVRRF
>gnl|CDD|200560 cd10934, CE4_cadherin_MopE_like_N, N-terminal Putative NodB-like catalytic domain of hypothetical proteins containing C-terminal cadherin or MopE copper binding domains. The family includes several cadherin or MopE copper binding domain containing hypothetical proteins found in bacteria. Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium. They play a role in cell fate, signalling, proliferation, differentiation, and migration. The copper binding domain involves a tryptophan metabolite, kynurenine, in the protein MopE. Members of this family contain an additional conserved domain, which is N-terminally fused to the cadherin domain or the MopE copper binding domain. Although its function remains unclear, the conserved domain exhibits a seven-stranded barrel with a detectable sequence similarity to the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
RDAGIFASRNDMDQSQEIDDVVDENPGIYDALLPILEQWKNDYNFVGSYYVNIGNNPPQGQYTDWSVSLP
YYQAMLALGNEIGTHSYTHPEDTNLLSASQLQFEFQQSTAELEQQLGADLVGAAIPGAPETLAVSQEINK
YVDYLSGGYSGVGAGYPGAFGYLTPGDQGKVYLAPNMSFDFTLIGFLNKTPAEASAIWQDEYAKITNHAG
TPIFVWPWHDYGATNWNDPDNDPPYTPEMFTNFIAKAAADGAEFVTLADLANRINAF
>gnl|CDD|200561 cd10935, CE4_WalW, Putative catalytic domain of lipopolysaccharide biosynthesis protein WalW and its bacterial homologs. This family corresponds to a group of uncharacterized lipopolysaccharide biosynthesis protein WalW found in bacteria. Although their biochemical properties remain to be determined, members of this family is composed of a seven-stranded barrel with detectable sequence similarity to the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
RFVVTVDTEEEFDWSGPFARRGAGVSNVQALPRFQALCERFGVRPTYLVDYPVASDPAAVAILARALDRG
RAEIGAHLHPWVTPPFDELTDPYNSYAGNLPEELERAKLDALTDAIEDRFGVPPTSFRAGRWGLGPRTAR
LLAELGIRVDSSVRPLFDYSGNGGPDYSAAPSDPYWVDLENGGDRPLLELPLTIGFLGPLRSRGRRLLSS
LPLRRARLGGLLARLGLLRRVALSPEGVSLADMLRLADALLARGGPVLTFSLHSSSLLPGGTPYVRTEAD
LEALYDWLEAFLAYL
>gnl|CDD|200562 cd10936, CE4_DAC2, Putative catalytic domain of family 2 polysaccharide deacetylases (DACs) from bacteria. This family contains an uncharacterized protein BH1492 from Bacillus halodurans, an uncharacterized protein ATU2773 from Agrobacterium tumefaciens C58, and other bacterial hypothetical proteins. Although their functions are still unknown, structural superposition and sequence comparison suggest that BH1492 and ATU2773 might be divergently related to the 7-stranded barrel catalytic domain of polysaccharide deacetylases (DACs) from the carbohydrate esterase 4 (CE4) superfamily, which remove N-linked acetyl groups from cell wall polysaccharides. This family is designated as DAC family 2, a divergent DAC family
RLAIVIDDLGYDLATAEALLALPFPVTLAILPYAPHAAELAEAARAAGHEVLLHLPMEPLGYPKNDPPGA
LLTGMSAEEIEKRLEAALARVPGAVGVNNHMGSRFTADREAMRQVLEALKERGLFFVDSRTTPKSVAYRV
AKELGVPTARRDVFLDNEQDEAAIRRQLDKAAKIARKRGSAIAIGHPRPETLAALKEWLPELEARGIELV
PVSAL
>gnl|CDD|200563 cd10938, CE4_HpPgdA_like, Catalytic domain of Helicobacter pylori peptidoglycan deacetylase (HpPgdA) and similar proteins. This family is represented by a peptidoglycan deacetylase (HP0310, HpPgdA) from the gram-negative pathogen Helicobacter pylori. HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. It functions as a homotetramer. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of polysaccharide deacetylase (DCA)-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. In contrast to typical NodB-like DCAs, HpPgdA does not exhibit a solvent-accessible polysaccharide binding groove, suggesting that the enzyme binds a small molecule at the active site
AVALTFDVDAESGWLGSGGGAADRPTDLSRGEYGARVGVPRLLDLLDRYDVKATFFVPGHTAETFPEAVE
AILAAGHEIGHHGYLHENPTGLTPEEERELLERGLELLEKLTGKRPVGYRSPSWEFSPNTLDLLLEHGFL
YDSSLMGDDRPYYYVRRGEETGLVEIPVHWELDDFPYFAFNRSPPGPPGIAPPRDVLDNWKDEFDGAYEE
GGVFTLTLHPQVIGRPSRIAMLERLIEHIKAHGGVWFATGEEIADYWR
>gnl|CDD|200564 cd10939, CE4_ArnD, Catalytic domain of Escherichia coli 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD and other bacterial homologs. This family is represented by Escherichia coli 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD (EC 3.5.1.n3). ArnD plays an important role in the biosynthesis of undecaprenyl phosphate alpha-4-amino-4-deoxy-L-arabinose (alpha-L-Ara4N). It catalyzes the deformylation of 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol. The ArnD-dependent deformylation likely occurs on the inner leaflet of the inner membrane. This family also includes many uncharacterized bacterial polysaccharide deacetylases. All family members show high sequence homology to the catalytic domain of bacterial PuuE (purine utilization E) allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA), and are classified within the larger carbohydrate esterase 4 (CE4) superfamily
KIALKIDVDTYRGTREGVPRLLRILRRHGIKATFFFSVGPDNTGRALWRLFRPGFLKKMLRTNAPSLYGW
RTLLYGTLLPGPIIGRRLADIIRQVAKAGHEVGIHAWDHVKWQDRLDAMSAAEIKREFDKGVALFEKIFG
RPPSTSAAPGWQANDRSLEIKDEFGFRYASDCRGGHPFYPLLAGKPLGTLQIPTTLPTLDELLGRDGATA
DNINDYLLSLLRPDGLNVLTIHAEVEGMKYAPIFEELLKRARARGYRFVPLGELAEELLINTPVGEVVMG
EIPGRSGWLA
>gnl|CDD|200565 cd10940, CE4_PuuE_HpPgdA_like_1, Putative catalytic domain of uncharacterized bacterial polysaccharide deacetylases similar to bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). This family contains many uncharacterized bacterial polysaccharide deacetylases (DCAs) that show high sequence similarity to the catalytic domain of bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as homotetramers. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCA-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. In contrast to typical NodB-like DCAs, PuuE allantoinase and HpPgdA do not exhibit a solvent-accessible polysaccharide binding groove and might only bind a small molecule at the active site
LASVSLDLDNLWSYLKIHGLPGWEARPSYLDIAVPRFLDVLDELGLTITVFVVGRDLARDENAKALRAIA
DAGHEIANHSFAHDPWLHRYSREEIEREIARAEAAILSATGQRPRGFRGPGYSVSADLLEVLAARGYAYD
ASTFPTFLGPLARAYYLGTAKLSGEEKEKRKRLFGGFARGLRPLGAPQWRHGSVKLVELPVTTMPLLRLP
IHGSYLLYLAQFSLTLARLYFRTALRLCKVTGVSPSLLLHPTDFLGAEDDPSMGFFPGMVLPQERKRAFA
TEVLGRLRRHFDVLTMLDHALSLARA
>gnl|CDD|200566 cd10941, CE4_PuuE_HpPgdA_like_2, Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar to bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). This family contains many uncharacterized prokaryotic polysaccharide deacetylases (DCAs) that show high sequence similarity to the catalytic domain of bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as homotetramers. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCA-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. In contrast to typical NodB-like DCAs, PuuE allantoinase and HpPgdA do not exhibit a solvent-accessible polysaccharide binding groove and might only bind a small molecule at the active site
MNILTFDVEDWYHPYAFEGEIDWEDQERRLEEGLDRLLDLLDKHGVKATFFVLGEVAERYPDLIRRIAEA
GHEIASHGYAHERVDRLTPEEFREDLRRSKKILEDITGQKVVGFRAPNFSITPWALDILAEAGYLYDSSV
FPTKRPGYGGPLAPKSEPLPPIRAKGGILEFPVSVTKLPGLRLPLAGGGYFRLLPYRLIKALIKRSLRRG
GPLVLYFHPWEFDPEQPVPGLPLLRRFRTYVGLGKAEEKLERLLEDFK
>gnl|CDD|200567 cd10942, CE4_u11, Putative catalytic domain of uncharacterized bacterial proteins from the carbohydrate esterase 4 superfamily. This family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
AVCITFDNLGEARDVGVGAWPCDTSIGTHPSVTEGLPRILDLLDELGIRCTYFVEGWSALHYPDELEAIL
AHGHEIGLHGWQHEPWAGLSPLEEDDLINRSLSIAERLGLAPVGFRPPGGALGAHTLALLAKHGIRYVSL
AGTGRSLATMPDGLAVLPFAWAAVDGFYYLDSFDGLRGPPQEEVDTPAALAQALRSALDAVVARGGFLTI
VFHPFLSGSPERLAVFEQVLRRIANDSRIWCAPAREVASWAR
>gnl|CDD|200568 cd10943, CE4_NodB, Putative catalytic domain of rhizobial NodB chitooligosaccharide N-deacetylase and its bacterial homologs. This family corresponds to rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-), encoded by nodB gene from the nodulation (nod) gene cluster that is responsible for the biosynthesis of bacterial nodulation signals, termed Nod factors. NodB is involved in de-N-acetylating the nonreducing N-acetylglucosamine residue of chitooligosaccharides to allow for the attachment of the fatty acyl group by the acyltransferase NodA. The monosaccharide N-acetylglucosamine cannot be deacetylated by NodB. NodB is composed of a 6-stranded barrel catalytic domain with detectable sequence similarity to the 7-stranded barrel homology domain of polysaccharide deacetylase (DCA)-like proteins in the larger carbohydrate esterase 4 (CE4) superfamily
RSIYLTFDDGPNPSCTPQVLDVLAEHRVPATFFVIGAYAAEHPELIRRMIAEGHEVGNHTMTHPDLSRCE
PGEVQREISSANKVIRHACPRASVRYFRAPYGAWSEEVLTASNKAGLAPLHWSVDPRDWSRPGIDAIVNA
VLASVRPGAIILLHDGCPPDEAARWTVAGLREQTLMALRYLIPALHARGFAIQ
>gnl|CDD|200569 cd10944, CE4_SmPgdA_like, Catalytic NodB homology domain of Streptococcus mutans polysaccharide deacetylase PgdA, Bacillus subtilis YheN, and similar proteins. This family is represented by a putative polysaccharide deacetylase PgdA from the oral pathogen Streptococcus mutans (SmPgdA) and Bacillus subtilis YheN (BsYheN), which are members of the carbohydrate esterase 4 (CE4) superfamily. SmPgdA is an extracellular metal-dependent polysaccharide deacetylase with a typical CE4 fold, with metal bound to a His-His-Asp triad. It possesses de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. SmPgdA plays a role in tuning cell surface properties and in interactions with (salivary) agglutinin, an essential component of the innate immune system, most likely through deacetylation of an as-yet-unidentified polysaccharide. SmPgdA shows significant homology to the catalytic domains of peptidoglycan deacetylases from Streptococcus pneumoniae (SpPgdA) and Listeria monocytogenes (LmPgdA), both of which are involved in the bacterial defense mechanism against human mucosal lysozyme. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. The biological function of BsYheN is still unknown. This family also includes many uncharacterized polysaccharide deacetylases mainly found in bacteria
KVVYLTFDDGPSKNTPKILDILKKYNVKATFFVIGSNVEKYPELVKRIVKEGHAIGLHSYTHDYKKLYSS
PEAFIKDLNKTQDLIKKITGVKTKLIRFPGGSSNTGLMKALRKALTKRGYKYWDWNVDSGDAKGKPKSAE
QIVQNVIKQVKNKNVIVILMHDTAGKETTVEALPEIIKYLKEQGYEFKT
>gnl|CDD|200570 cd10946, CE4_Mll8295_like, Putative catalytic NodB homology domain of uncharacterized Mll8295 protein encoded from Rhizobium loti and its bacterial homologs. This family is represented by a putative polysaccharide deacetylase Mll8295 encoded from Rhizobium loti. Although its biological function still remains unknown, Mll8295 shows high sequence homology to the catalytic domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), which is an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Both Mll8295 and SpPgdA belong to the carbohydrate esterase 4 (CE4) superfamily. This family also includes many uncharacterized bacterial polysaccharide deacetylases
KTIYLTFDDGPLDGTENILKILKAENVKATVFLVGFHADGGDKAKEALKLYLDNPGIILANHSYTHANNN
YTLFYSNTDKVVEDILKAQSYLNLKYKIARLPGRNGWRVNNRKQTDDNSSNVAAAGQDSLAASGYKIYGW
DVEWQPEDWGGTPVQSVDEMVKKIDHLLNTNNTFTKGKVILLTHDFMFQDGWNLTKLKEFIRLLKKRGYV
FDTIRNY
>gnl|CDD|200571 cd10947, CE4_SpPgdA_BsYjeA_like, Catalytic NodB homology domain of Streptococcus pneumoniae peptidoglycan deacetylase PgdA, Bacillus subtilis BsYjeA protein, and their bacterial homologs. This family is represented by Streptococcus pneumoniae peptidoglycan GlcNAc deacetylase (SpPgdA), a member of the carbohydrate esterase 4 (CE4) superfamily. SpPgdA protects gram-positive bacterial cell wall from host lysozymes by deacetylating peptidoglycan N-acetylglucosamine (GlcNAc) residues. It consists of three separate domains: N-terminal, middle and C-terminal (catalytic) domains. The catalytic NodB homology domain is similar to the deformed (beta/alpha)8 barrel fold adopted by other CE4 esterases, which harbors a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad closely associated with conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The enzyme is able to accept GlcNAc3 as a substrate, with the N-acetyl of the middle sugar being removed by the enzyme. This family also includes Bacillus subtilis BsYjeA protein encoded by the yjeA gene, which is one of the six polysaccharide deacetylase gene homologs (pdaA, pdaB/ybaN, yheN, yjeA, yxkH and ylxY) in the Bacillus subtilis genome. Although homology comparison shows that the BsYjeA protein contains a polysaccharide deacetylase domain, and was predicted to be a membrane-bound xylanase or a membrane-bound chitooligosaccharide deacetylase, more recent research indicates BsYjeA might be a novel non-specific secretory endonuclease which creates random nicks progressively on the two strands of dsDNA, resulting in highly distinguishable intermediates/products very different in chemical and physical compositions over time. In addition, BsYjeA shares several enzymatic properties with the well-understood DNase I endonuclease. Both enzymes are active on ssDNA and dsDNA, both generate random nicks, and both require Mg2+ or Mn2+ for hydrolytic activity
KVVALTFDDGPDPTTTPQVLKTLKKYKAPATFFMLGSNVKTYPELVRRVLDAGHEIGNHSWSHPQLTKLS
VAEAEKQINDTDDAIEKATGNRPTLLRPPYGATNRSIRQIAGLTIALWDVDTRDWSKRNKDKIVTIVMNQ
VQPGSIVLMHDIHRTTADALPRILDYLKDQGYTFVTL
>gnl|CDD|200572 cd10948, CE4_BsPdaA_like, Catalytic NodB homology domain of Bacillus subtilis polysaccharide deacetylase PdaA, and its bacterial homologs. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. This family is represented by Bacillus subtilis pdaA gene encoding polysaccharide deacetylase BsPdaA, which is a member of the carbohydrate esterase 4 (CE4) superfamily. BsPdaA deacetylates peptidoglycan N-acetylmuramic acid (MurNAc) residues to facilitate the formation of muramic delta-lactam, which is required for recognition of germination lytic enzymes. BsPdaA deficiency leads to the absence of muramic delta-lactam residues in the spore cortex. Like other CE4 esterases, BsPdaA consists of a single catalytic NodB homology domain that appears to adopt a deformed (beta/alpha)8 barrel fold with a putative substrate binding groove harboring the majority of the conserved residues. It utilizes a general acid/base catalytic mechanism involving a tetrahedral transition intermediate, where a water molecule functions as the nucleophile tightly associated to the zinc cofactor
TPIGWGFSKSKNHQPPATGKLYNELIKKYNAYYVGNSKEKVIYLTFDEGYENGYTPKILDVLKKNDVKAT
FFVTGHYVKSNPDLIKRMVDEGHIIGNHTVHHPDMTTLSDEKFKKEITGVEEEYKEVTGKEMMKYFRPPR
GEFSERSLKITKDLGYTTVFWSFAYRDWEVDNQPGPEEALKKIMNQLHPGAIYLLHAVSKTNAEALDDII
KDLRKQGYEFKSL
>gnl|CDD|200573 cd10949, CE4_BsPdaB_like, Putative catalytic NodB homology domain of Bacillus subtilis putative polysaccharide deacetylase PdaB, and its bacterial homologs. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. This family is represented by the putative polysaccharide deacetylase PdaB encoded by the pdaB gene on sporulation of Bacillus subtilis. Although its biochemical properties remain to be determined, the PdaB (YbaN) protein is essential for maintaining spores after the late stage of sporulation and is highly conserved in spore-forming bacteria. The glycans of the spore cortex may be candidate PdaB substrates. Based on sequence similarity, the family members are classified as carbohydrate esterase 4 (CE4) superfamily members. However, the classical His-His-Asp zinc-binding motif of CE4 esterases is missing in this family
TDEKVVALTFDISWGEERVEPILDTLKKNGNKKATFFISGPWAERHPELVKRIVADGHEIGSHGYRYKNY
SDYEDEEIKKDLLRAQQAIEKVTGVKPTLLRPPNGDFNKRVLKLAESLGYTVVHWSVNSLDWKNPGVEAI
VDRVMKRVKPGDIVLMHASDSAKQTAEALPIILEGLKNKGYEFVTVSELLAN
>gnl|CDD|200574 cd10950, CE4_BsYlxY_like, Putative catalytic NodB homology domain of uncharacterized protein YlxY from Bacillus subtilis and its bacterial homologs. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. This family is represented by Bacillus subtilis putative polysaccharide deacetylase BsYlxY, encoded by the ylxY gene, which is a member of the carbohydrate esterase 4 (CE4) superfamily. Although its biological function still remains unknown, BsYlxY shows high sequence homology to the catalytic domain of Bacillus subtilis pdaB gene encoding a putative polysaccharide deacetylase (BsPdaB), which is essential for the maintenance of spores after the late stage of sporulation and is highly conserved in spore-forming bacteria. However, disruption of the ylxY gene in B. subtilis did not cause any sporulation defect. Moreover, the Asp residue in the classical His-His-Asp zinc-binding motif of CE4 esterases is mutated to a Val residue in this family. Other catalytically relevant residues of CE4 esterases are also not conserved, which suggest that members of this family may be inactive
GNPEKKMVALLINVAWGEEYLPAMLTILEKHDVKATFFLEGRWAKKNPDLVRKIAKDGHEIGNHGYSHPD
PSQLSYEQNREEIRKTNEIIEEITGEKPKLFAPPYGEFNDAVVKAAAELGMRTILWTVDTIDWKKPSPDV
IVDRVLSKIHPGAIILMHPTESTVEALPEMIRQLKEKGYKIVTVSELL
>gnl|CDD|200575 cd10951, CE4_ClCDA_like, Catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase and similar proteins. This family is represented by the chitin deacetylase (endo-chitin de-N-acetylase, ClCDA, EC 3.5.1.41) from Colletotrichum lindemuthianum (also known as Glomerella lindemuthiana), which is a member of the carbohydrate esterase 4 (CE4) superfamily. ClCDA catalyzes the hydrolysis of N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, converting it to chitosan in fungal cell walls. It consists of a single catalytic domain similar to the deformed (alpha/beta)8 barrel fold adopted by other CE4 esterases, which encompasses a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine), to carry out acid/base catalysis. It possesses a highly conserved substrate-binding groove, with subtle alterations that influence substrate specificity and subsite affinity. Unlike its bacterial homologs, ClCDA contains two intramolecular disulfide bonds that may add stability to this secreted protein. The family also includes many uncharacterized deacetylases and hypothetical proteins mainly from eukaryotes, which show high sequence similarity to ClCDA
ITSCTVPGTVALTFDDGPSTYTPQLLDLLKEAGAKATFFVNGNNFNGCIYDYADVLRRMYNEGHQIASHT
WSHPDLTKLSAAQIRDEMTKLEDALRKILGVKPTYMRPPYGECNDEVLAVLGELGYHVVTWNLDTGDYNN
NSPGSVEESKAKFDQGSLPAAGGSIVLAHDVHQSTVEQLTPYIIDILKKKGYRLVTV
>gnl|CDD|200576 cd10952, CE4_MrCDA_like, Catalytic NodB homology domain of Mucor rouxii chitin deacetylase and similar proteins. This family is represented by the chitin deacetylase (MrCDA, EC 3.5.1.41) encoded from the fungus Mucor rouxii (also known as Amylomyces rouxii). MrCDA is an acidic glycoprotein with a very stringent specificity for beta1-4-linked N-acetylglucosamine homopolymers. It requires at least four residues (chitotetraose) for catalysis, and can achieve extensive deacetylation on chitin polymers. MrCDA shows high sequence similarity to Colletotrichum lindemuthianum chitin deacetylase (endo-chitin de-N-acetylase, ClCDA), which consists of a single catalytic domain similar to the deformed (beta/alpha)8 barrel fold adopted by the carbohydrate esterase 4 (CE4) superfamily, which encompasses a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The family also includes some uncharacterized eukaryotic and bacterial homologs of MrCDA
GTWGLTFDDGPTPATPALLDYLKSHNQKATFFVIGSNVVNNPDILQRALEAGHEIGVHTWSHPAMTTLTN
EQIVAELGWTMQIIKDTIGVTPKYWRPPYGDIDDRVRAIAKQLGLTTVLWNLDTNDWKLTTGPDATATVV
DVFQDIAARANKSGFISLEHDLTNSTVSVAVKSLPQIL
>gnl|CDD|200577 cd10953, CE4_SlAXE_like, Catalytic NodB homology domain of Streptomyces lividans acetylxylan esterase and its bacterial homologs. This family is represented by Streptomyces lividans acetylxylan esterase (SlAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. SlAXE deacetylates O-acetylated xylan, a key component of plant cell walls. It shows no detectable activity on generic esterase substrates including para-nitrophenyl acetate. It is specific for sugar-based substrates and will precipitate acetylxylan as a result of deacetylation. SlAXE also functions as a chitin and chitooligosaccharide de-N-acetylase with equal efficiency to its activity on xylan. SlAXE forms a dimer. Each monomer contains a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases, which encompasses a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine), to carry out acid/base catalysis. SlAXE possess a single metal center with a chemical preference for Co2+
GYVGLTFDDGPNNSNTATLLSALKQNGLRATLFNQGQNAQSNPSLMRAQKNAGMWIGNHSWSHPHMTSWS
YQQMYSELTRTQQAIQNAGGPAPTLFRPPYGESNATLQQAESALGLTEVIWDVDSQDWNGASTAQIVNAA
NRLNNGQVILMHDGYANTNSAIPQIAQNLKNRGLCSGMI
>gnl|CDD|200578 cd10954, CE4_CtAXE_like, Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its bacterial homologs. This family is represented by Clostridium thermocellum acetylxylan esterase (CtAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. CtAXE deacetylates O-acetylated xylan, a key component of plant cell walls. It shows no detectable activity on generic esterase substrates including para-nitrophenyl acetate. It is specific for sugar-based substrates and will precipitate acetylxylan, as a consequence of deacetylation. CtAXE is a monomeric protein containing a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases. However, due to differences in the topography of the substrate-binding groove, the chemistry of the active center, and metal ion coordination, CtAXE has different metal ion preference and lacks activity on N-acetyl substrates. It is significantly activated by Co2+. Moreover, CtAXE displays distinctly different ligand coordination to the metal ion, utilizing an aspartate, a histidine, and four water molecules, as opposed to the conserved His-His-Asp zinc-binding triad of other CE4 esterases
KMVALTFDDGPNAKYTPRLLDVLEKYNVRATFFLVGQNVNGNKEIVKRMVEMGCEIGNHSYTHPDLTKLS
PSEIKKEIEKTNEAIKKITGKRPKLFRPPYGAVNDTVKKAIDLPFILWSVDTEDWKSKNAEKIVSTVLKQ
AKDGDIILMHDIYPSTVEAAETIIPELKKRGYQFVTVSEL
>gnl|CDD|200579 cd10955, CE4_BH0857_like, Putative catalytic NodB homology domain of uncharacterized BH0857 protein from Bacillus halodurans and its bacterial homologs. This family is represented by a putative polysaccharide deacetylase BH0857 from Bacillus halodurans. Although its biological function still remains unknown, BH0857 shows high sequence homology to the catalytic NodB homology domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), which is an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Both BH0857 and SpPgdA belong to the carbohydrate esterase 4 (CE4) superfamily. This family also includes many uncharacterized bacterial polysaccharide deacetylases
KVVALTFDACGGPGGSGYDAALIDFLREHKIPATLFVTGRWIDRNPAEAKELAANPLFEIENHGYRHPPL
SVNGRIKGTLSVEEVRREIEGNQEAIEKATGRKPRYFRFPTAYYDEVAVELVEALGYKVVGWDSVSGDPG
ATLTEEIVDRVLARAKPGSIIIMHMNGPASGTAEGLPAAIPELKAKGYRFVTLSE
>gnl|CDD|200580 cd10956, CE4_BH1302_like, Putative catalytic NodB homology domain of uncharacterized BH1302 protein from Bacillus halodurans and its bacterial homologs. This family is represented by a putative polysaccharide deacetylase BH1302 from Bacillus halodurans. Although its biological function is unknown, BH1302 shows high sequence homology to the catalytic NodB homology domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), which is an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Both BH1302 and SpPgdA belong to the carbohydrate esterase 4 (CE4) superfamily. This family also includes many uncharacterized bacterial polysaccharide deacetylases
ETTEKVIALTFDDGPTPAHTDAILSILDEYDIKATFFLIGREIEENPSEARAIVAAGHEIGNHSYSHRRM
VFKSPSFIADEIEKTDQLIRQAGYTGEIHFRPPYGKKLLGLPYYLAQHNRTTVMWDVEPETFPDKAQDAD
DIAAYVIEQVKPGSIILLHVMYGSRQNSREALPLILDGLRQQGYRFVTVSELLE
>gnl|CDD|200581 cd10958, CE4_NodB_like_2, Catalytic NodB homology domain of uncharacterized chitin deacetylases and hypothetical proteins. This family includes some uncharacterized chitin deacetylases and hypothetical proteins, mainly from eukaryotes. Although their biological function is unknown, members in this family show high sequence homology to the catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase (endo-chitin de-N-acetylase, ClCDA, EC 3.5.1.41), which catalyzes the hydrolysis of N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, converting it to chitosan in fungal cell walls. Like ClCDA, this family is a member the carbohydrate esterase 4 (CE4) superfamily
KVVALTIDDAPSPSTEEILDLLEEHNVRATFFVIGSHAPRREEVLSRIVEEGHELGNHGMHDEPSASLSL
AEFETQLLECERLISRLYPNRGISQKTKWFRPGSGFFTRRMLDTVIRLGYRVVLGSVYPFDPQIPSPWFN
SFFLRRRVSPGSIVILHDRPWTIANTADVLRKLLPELTRRGYDVVTLSNL
>gnl|CDD|200582 cd10959, CE4_NodB_like_3, Catalytic NodB homology domain of uncharacterized bacterial polysaccharide deacetylases. This family includes many uncharacterized bacterial polysaccharide deacetylases. Although their biological function still remains unknown, members in this family show high sequence homology to the catalytic NodB homology domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), which is an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Like SpPgdA, this family is a member of the carbohydrate esterase 4 (CE4) superfamily
KEVALTFDDGPDPEYTPALLDLLARHGAKATFFVVGERAERHPDLIRRIVDEGHEIGNHGYRHRHPWLRS
PWKAIRDLRRAARIIEQLTGRPPRYYRPPWGHLNLATLLAARRLGLKIVLWSVDGGDWRPNATAAEIAAR
LLRRVRPGDIILLHDGGPTPGAPRRTLEALPTLLPGLKERGLEFVTL
>gnl|CDD|200583 cd10960, CE4_NodB_like_1, Catalytic NodB homology domain of uncharacterized bacterial polysaccharide deacetylases. This family includes many uncharacterized bacterial polysaccharide deacetylases. Although their biological function still remains unknown, members in this family show high sequence homology to the catalytic NodB homology domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), which is an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Like SpPgdA, this family is a member of the carbohydrate esterase 4 (CE4) superfamily
KEIAITFDDLPFVGGLPPGESRQEITEKLLAALKKHGIPAYGFVNEGKLENDPDGIELLEAWRDAGHELG
NHTYSHPSLNSVTAEAYIADIEKGEPVLKPLMGKAFWKYFRFPYLAEGDTAEKRDAVRAFLKKHGYRIAP
VTIDFSDWAFNDAYARALAKGDKADLARLRQAYLAHAWDRLDYYEKLSQKVFGRDIPHILLLHANLLNAD
FLPDLLAAFKKRGYTFVSLDEALKDPAY
>gnl|CDD|200584 cd10962, CE4_GT2-like, Catalytic NodB homology domain of uncharacterized bacterial glycosyl transferase, group 2-like family proteins. This family includes many uncharacterized bacterial proteins containing an N-terminal GH18 (glycosyl hydrolase, family 18) domain, a middle NodB-like homology domain, and a C-terminal GT2-like (glycosyl transferase group 2) domain. Although their biological function is unknown, members in this family contain a middle NodB homology domain that is similar to the catalytic domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Like SpPgdA, this family is a member of the carbohydrate esterase 4 (CE4) superfamily. The presence of three domains suggests that members of this family may be multifunctional
KKIALTFDDGPDPEWTPQILDILKEYQIPATFFVIGENAVNNPELVKRIIDEGHEIGNHTFTHPDLDLLS
EKRTRLELNATQRLIEAATGHSTLLFRPPYGADANPTSADEIAPILKAQDRGYLVVGEDIDPKDWAEPGP
DEIADRIIDQVDGAGNIILLHDGGGDRSATVAALPLIIPELKARGYEFVTVSDLLG
>gnl|CDD|200585 cd10963, CE4_RC0012_like, Putative catalytic NodB homology domain of uncharacterized protein RC0012 from Rickettsia conorii and its bacterial homologs. This family contains an uncharacterized protein RC0012 from Rickettsia conorii and its bacterial homologs. Although their biochemical properties remain to be determined, members in this family seems to be composed of a seven-stranded barrel with detectable sequence similarity to the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
KGLFLTVDLCPSSKPFERELFEKLIELFQKATKIPVAISVSGLWIKSHPEDFAWLKNKKRAGALAITWVN
HSYSHPYDPGLPLEENFLLSPGTDLNVEVLETEKLLLENGILPSVFFRFPGLVSDKALMEKLRELGLIPL
GADAWLAKGERPQAGSIILVHGNGNEPEGVKLFLKLLKEGKV
>gnl|CDD|200586 cd10964, CE4_PgaB_5s, N-terminal putative catalytic polysaccharide deacetylase domain of bacterial poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB, and similar proteins. This family is represented by an outer membrane lipoprotein, poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase (PgaB, EC 3.5.1.-), encoded by Escherichia coli pgaB gene from the pgaABCD (formerly ycdSRQP) operon, which affects biofilm development by promoting abiotic surface binding and intercellular adhesion. PgaB catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PGA), a biofilm adhesin polysaccharide that stabilizes biofilms of E. coli and other bacteria. PgaB contains an N-terminal NodB homology domain with a 5-stranded beta/alpha barrel, and a C-terminal carbohydrate binding domain required for PGA N-deacetylation, which may be involved in binding to unmodified poly-beta-1,6-GlcNAc and assisting catalysis by the deacetylase domain. This family also includes several orthologs of PgaB, such as the hemin storage system HmsF protein, encoded by Yersinia pestis hmsF gene from the hmsHFRS operon, which is essential for Y. pestis biofilm formation. Like PgaB, HmsF is an outer membrane protein with an N-terminal NodB homology domain, which is likely involved in the modification of the exopolysaccharide (EPS) component of the biofilm. HmsF also has a conserved but uncharacterized C-terminal domain that is present in other HmsF-like proteins in Gram-negative bacteria. This alignment model corresponds to the N-terminal NodB homology domain
LPAKAVLLTFDDGYQSFYTRVYPLLKAYKYPAVLALVGSWLETPAGKKVDYGGEQLPRDRFLSWEQIREM
QASGLVEIASHSHDLHHGIPANPQGNLLPAATTRQYDPKTGRYETDAEYRQRIRNDLKKSSALIKKHTGR
APRVMVWPYGAYNGTLIEEAAKLGMQLTFTLEDGANNADQSLSSIPRILVENN
>gnl|CDD|200587 cd10965, CE4_IcaB_5s, Putative catalytic polysaccharide deacetylase domain of bacterial intercellular adhesion protein IcaB and similar proteins. The family is represented by the surface-attached protein intercellular adhesion protein IcaB (Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase, EC 3.5.1.-), encoded by Staphylococcus epidermidis icaB gene from the icaABC gene cluster that is involved in the synthesis of polysaccharide intercellular adhesin (PIA), which is located mainly on the cell surface. IcaB is a secreted, cell wall-associated protein that plays a crucial role in exopolysaccharide modification in bacterial biofilm formation. It catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. IcaB shows high homology to the N-terminal NodB homology domain of Escherichia coli PgaB. At this point, they are classified in the same family
PGKYVVITFDDVDQTVYDNAFPILKKLKIPFTQFVITGQVGSTNFGLNLATWSQIKEMVASGLVTFGLHT
NDLHYLVKDKKKLFTPASYSRFAEDYAKSQKCLKEKLGKKTRYFAYPYGEGNKDTQKILKKQGIQYGFTL
RDKVVTNDSDNYRIPRILVTNDSFWKLIKKWI
>gnl|CDD|213024 cd10966, CE4_yadE_5s, Putative catalytic polysaccharide deacetylase domain of uncharacterized protein yadE and similar proteins. This family contains an uncharacterized protein yadE from Escherichia coli and its bacterial homologs. Although its molecular function remains unknown, yadE shows high sequence similarity with the catalytic NodB homology domain of outer membrane lipoprotein PgaB and the surface-attached protein intercellular adhesion protein IcaB. Both PgaB and IcaB are essential in bacterial biofilm formation
PEKSVVITFDDGYKSNYEYAYPILKKYGFKATIFVIGSRIGEKPQDPKILQYLSIEELKEMRDVFEFQSH
TYNMHRGGGTGGHGLLALSEEEILADLKKSEEILGSSKAFAYPYGDYNDNAIEALKEAGVKLAFTTNEGK
VTPGDDPYELPRVRITGGTSLEDF
>gnl|CDD|200589 cd10967, CE4_GLA_like_6s, Putative catalytic NodB homology domain of gellan lyase and similar proteins. This family is represented by the extracellular polysaccharide-degrading enzyme, gellan lyase (gellanase, EC 4.2.2.-), from Bacillus sp. The enzyme acts on gellan exolytically and releases a tetrasaccharide of glucuronyl-glucosyl-rhamnosyl-glucose with unsaturated glucuronic acid at the nonreducing terminus. The family also includes many uncharacterized prokaryotic polysaccharide deacetylases, which show high sequence similarity to Bacillus sp. gellan lyase. Although their biological functions remain unknown, all members of the family contain a conserved domain with a 6-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily
LAVSLTFDDGYAQDLRAAPLLAKYGLKGTFFVNSGLLGRRGYLDLEELRELAAAGHEIGSHTVTHPDLTS
LPPAELRREIAESRAALEEIGGFPVTSFAYPFGSTNPSIVPLLARGFIAARGVGGGGNPPNPSDPPADPA
DCHNADSLALGGPELLLAPDLLDAAKKNGGWLVLWGHSVEGDGTKYSVSWEALEALLAYLAE
>gnl|CDD|213025 cd10968, CE4_Mlr8448_like_5s, Putative catalytic NodB homology domain of Mesorhizobium loti Mlr8448 protein and its bacterial homologs. This family contains Mesorhizobium loti Mlr8448 protein and its bacterial homologs. Although their biochemical properties are yet to be determined, members in this subfamily contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily
RFAVLTFDDGYRDNLEFALPVFERHGVPFTIYVTTGFPDGTGELWWLTLECLDWDELRRLAADPLVTIGA
HTITHPNLARLSDDEARREIAASRARLEAELGREVRHFAYPYGDRTAAGPREADLAREAGFATAVTTRPG
VLFAEHRENLHALPRISLNGR
>gnl|CDD|213026 cd10969, CE4_Ecf1_like_5s, Putative catalytic NodB homology domain of a hypothetical protein Ecf1 from Escherichia coli and similar proteins. This family contains a hypothetical protein Ecf1 from Escherichia coli and its prokaryotic homologs. Although their biochemical properties remain to be determined, members in this family contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily
PETFEEQLKYLKKNGYRTLSLEELLAFLKGGKPLPKKSVLITFDDGYLDNYVYAYPILKKYGLKATIFVV
TGFIDEASGVRPTLFDYWSGDMPEANKIFFLKGRDEVFLSWEELREMEDSGVFDIQSHSHSHTRVEYELE
ESKRLLEENLGKKVDHFCWPWGHYSPESLRIAKELGFKFFFTTKKGVNVPGEDPDRIKRITVKKDGGFWL
KKRLFLFS
>gnl|CDD|213027 cd10970, CE4_DAC_u1_6s, Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide deacetylases which consist of a 6-stranded beta/alpha barrel. This family contains uncharacterized prokaryotic polysaccharide deacetylases. Although their biological functions remain unknown, all members of the family contain a conserved domain with a 6-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily
GKVSLTFDDGYESQYTTAFPILQEYGIPATAAVIPDSIGSSGRLTLDQLRELQDAGWEIASHTLTHTDLT
ELSADEQRAELTESKRWLEDNGFGDGADHFAYPYGRYDDEVLELVREYYDLGRSGGGGPNGRPPLDPYRL
RRVTGEADTTTEEVKTLLDRAAAYNQWLILMFHDVGEEDGDDYSVARFEETLDY
>gnl|CDD|200593 cd10971, CE4_DAC_u2_5s, Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide deacetylases which consist of a 5-stranded beta/alpha barrel. This family contains many uncharacterized prokaryotic polysaccharide deacetylases. Although their biological functions remain unknown, all members of this family are predicted to contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily
AILLTFDDGYKDHYTYVLPELEERGIQGSFFVPAKPVEEHKVLDVNKIHFILFIKRLLQYELPEKLRTEI
LDKLFKKYVDISEEAFAKELYMTKDQIKQLERAGMHIGSHGYDHYWLGRLSPEEQEAEIKKSLKFLSEVG
GGHDRWTFCYPYGSFNEETLEILKENGCRLGFTTEVAIADLDDLEPLELPRYDCNDFP
>gnl|CDD|200594 cd10972, CE4_DAC_u3_5s, Putative catalytic NodB homology domain of uncharacterized bacterial polysaccharide deacetylases which consist of a 5-stranded beta/alpha barrel. This family contains uncharacterized bacterial polysaccharide deacetylases. Although their biological functions remain unknown, all members of the family are predicted to contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily
PAGKTPVVLTFDDGSPGQFRYIEKNGQLVIDPDTAVGILEDFKEEHPDFPPTGTFYVNPGPFGFGQPEYA
EQKLRWLVELGYEIGNHTYTHVNLNKLDAEEIQEELARVNKMIEEAIPGYEVESLALPFGMKPKENRALV
LSGEYEGVSYKHQAVLLVGAEPAPSPYSKDFDPAAIPRIRASGTQGDDWYLYMKKFAANPELRYISDGDP
NTITIP
>gnl|CDD|213028 cd10973, CE4_DAC_u4_5s, Putative catalytic NodB homology domain of uncharacterized bacterial polysaccharide deacetylases which consist of a 5-stranded beta/alpha barrel. This family contains many uncharacterized bacterial polysaccharide deacetylases. Although their biological functions remain unknown, all members of the family are predicted to contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily
KTVVITIDDGYKSVYTNAFPILKKYGYPFTLFVYTEAIGRGYPDYLSWDQIREMAKYGVEIANHSYSHPH
LVRLGEKMQEQWLEWIRQDIEKSQQRFEKELGKKPKLFAYPYGEYNPAIIKLVKEAGFEAAFQQSGGVVS
AGTDLTALPRFPLSGDY
>gnl|CDD|200596 cd10974, CE4_CDA_like_1, Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding peritrophin-A domain (ChBD) and/or a low-density lipoprotein receptor class A domain (LDLa). Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues. CDAs have been isolated and characterized from various bacterial and fungal species and belong to the larger carbohydrate esterase 4 (CE4) superfamily. This family includes many CDA-like proteins mainly from insects, which contain a putative CDA-like catalytic domain similar to the catalytic NodB homology domain of CE4 esterases. In addition to the CDA-like domain, family members contain two additional domains, a chitin-binding peritrophin-A domain (ChBD) and a low-density lipoprotein receptor class A domain (LDLa), or have the ChBD domain but do not have the LDLa domain
PQMITLTFDDAINDNNIELYKKIFNGKRNNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHN
DDENNATYEDWVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAPPSNV
PLWPYTLDYKMPHECHGQNCPTRSFPGVWEMVLNELDVRDDPQGDEPLAMDDSCLNILSGDQVYEWLQHN
FERHYLTNRAPYGLYFHTNWLKTKNELLRALQKFLDEILQLPDVYFVTMTQAIQWMQNP
>gnl|CDD|200597 cd10975, CE4_CDA_like_2, Putative catalytic domain of chitin deacetylase-like proteins. Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues. CDAs have been isolated and characterized from various bacterial and fungal species and belong to the larger carbohydrate esterase 4 (CE4) superfamily. This family includes many midgut-specific CDA-like proteins mainly from insects, such as Tribolium castaneum CDAs (TcCDA6-9). These proteins contain a putative CDA-like catalytic domain similar to the catalytic NodB homology domain of CE4 esterases. In addition to the CDA-like domain, some family members have an additional chitin-binding peritrophin-A domain (ChBD)
PQLVTLTFDDAVNTLNYPYYEKLFGNRKNPNGCPIGATFFVSHEYTDYRLVQELYNDGHEIALHSISHRS
PQDYWRNASVDEWEREFGGQREILAHFANIPAEDIKGFRAPFLQLGGDATFKALKQLGLTYDSSWPTQSF
TNPPLWPYTLDYGSTQDCVIPPCPTDSYPGFWVVPMVDWQDLNGVPCSMLAACPPPGTADEVYDWLLSNF
ERHYNTNRAPFGLYLHASWFEFTPNRLEGFKKFLDELLSLDDVYLVTISQAIEWMRNP
>gnl|CDD|200598 cd10976, CE4_CDA_like_3, Putative catalytic domain of uncharacterized bacterial hypothetical proteins similar to insect chitin deacetylase-like proteins. The family includes many uncharacterized bacterial hypothetical proteins that show high sequence similarity to insect chitin deacetylase-like proteins. Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues
PPQFVVFSFDGAGDNQLWSRSRAVAKQTNARFTYFLSGVYLLTTENRTLYTPPGQKAGRSNIGFAGSRQE
VADRLRQLNAAYREGHEIGSHANGHFDGKGGGGRWSVADWKREFDQFYRFVENAYAINGIEGAPPWPAFA
PNSIKGFRAPCLEGSKGLQPALKKHGFTYDASSVTQGPYWPQKVDGIWNFPLPLVPEGPTSRPVIAMDYN
LFVRHSGGVEAPAKAAEFEARMLATYRNAFDRAYNGNRAPLQLGNHFVKWNGGAYWNALERFAEEVCTKP
EVKCVTYRELVDFLEAQDP
>gnl|CDD|200599 cd10977, CE4_PuuE_SpCDA1, Catalytic domain of bacterial PuuE allantoinases, Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), and similar proteins. Allantoinase (EC 3.5.2.5) can hydrolyze allantoin((2,5-dioxoimidazolidin-4-yl)urea), one of the most important nitrogen carrier for some plants, soil animals, and microorganisms, to allantoate. DAL1 gene from Saccharomyces cerevisiae encodes an allantoinase. However, some organisms possess allantoinase activity but lack DAL1 allantoinase. In those organisms, a defective allantoinase gene, named puuE (purine utilization E), encodes an allantoinase that specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. PuuE allantoinase is related to polysaccharide deacetylase (DCA), one member of the carbohydrate esterase 4 (CE4) superfamily, that removes N-linked or O-linked acetyl groups of cell wall polysaccharides, and lacks sequence similarity with the known DAL1 allantoinase that belongs to the amidohydrolase superfamily. PuuE allantoinase functions as a homotetramer. Its monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCAs. It appears to be metal-independent and acts on a small substrate molecule, which is distinct from the common features of DCAs that are normally metal ion dependent and recognize multimeric substrates. This family also includes a chitin deacetylase 1 (SpCDA1) encoded by the Schizosaccharomyces pombe cda1 gene. Although the general function of chitin deacetylase (CDA) is the synthesis of chitosan from chitin, a polymer of N-acetyl glucosamine, to build up the proper ascospore wall, the actual function of SpCDA1 might involve allantoin hydrolysis. It is likely orthologous to PuuE allantoinase, whereas it is more distantly related to the CDAs found in other fungi, such as Saccharomyces cerevisiae and Mucor rouxii. Those CDAs are similar with rizobial NodB protein and are not included in this family
WPGGARVAVSFVLNYEEGGERSILHGDGASESFLSEIVGAPLPGVRDLSMESLYEYGSRAGVWRILRLFD
RRDVPLTVFAVAMALERNPAVARAMVAAGHEIASHGWRWIDYQGMDEAEEREHIRRAIAIIERLTGERPL
GWYTGRASPNTRRLVVEEGGFLYDSDSYDDDLPYWVDVEGKPHLVVPYTLDTNDMRFATAQGFNTADDFF
TYLKDAFDVLYEEGAEAPKMMSIGLHCRLIGRPGRFAGLERFLEHVKSHDGVWVARREDIARH
>gnl|CDD|200600 cd10978, CE4_Sll1306_like, Putative catalytic domain of Synechocystis sp. Sll1306 protein and other bacterial homologs. The family contains Synechocystis sp. Sll1306 protein and uncharacterized bacterial polysaccharide deacetylases. Although their biological function remains unknown, they show very high sequence homology to the catalytic domain of bacterial PuuE (purine utilization E) allantoinases. PuuE allantoinase specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. It functions as a homotetramer. Its monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of polysaccharide deacetylase-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. PuuE allantoinase appears to be metal-independent and acts on a small substrate molecule, which is distinct from the common feature of polysaccharide deacetylases that are normally metal ion dependent and recognize multimeric substrates
FWPNGARLVISISMQFEAGGQPIKGEGPFPPEDPPKGYPDLPTNTWYQYGYKEGIPRMLDLWDKHGIKVT
SHMVGRAVEKHPDLAKEIVQRGHEAAAHGRDWQNQFSMSREQERAFIQDGVDSIQKVTGQRPVGYNAFWL
RGSPNTLDILQELGFVYHIDDVSRDEPFIIPVNGKDFVVVPYTLRNNDIVRFEGRAYSSDAYLQELKDEF
DQLYEEAAHRRRMMSISLHDRISGTPQRVRVLDEFLTYAKSHPGVTFMRKDDIARFALADK
>gnl|CDD|200601 cd10979, CE4_PuuE_like, Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar to bacterial PuuE allantoinases. The family includes a group of uncharacterized prokaryotic polysaccharide deacetylases (DCAs) that show high sequence similarity to the catalytic domain of bacterial PuuE (purine utilization E) allantoinases. PuuE allantoinase specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. It functions as a homotetramer. Its monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCA-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. PuuE allantoinase appears to be metal-independent and acts on a small substrate molecule, which is distinct from the common feature of DCAs which are normally metal ion dependent and recognize multimeric substrates
YDYSPITDRPPLRWPGGARVAVWVAVNVEHFPLDPPMPPILPAPATPYPDVLNYSWRDYGNRVGIWRLLD
ALDELGIPPTVALNAAVADRYPELIEAIRERGWEFIAHGISNSTLHAGLDEAQEREVIAESLDRIEKATG
QRPRGWLSPGLSETENTPDLLAEAGIEYLCDWVNDDQPYWLRTPAGPLLSLPYTLELNDIPIYLVRGHSA
DEFADRIIDQFDQLYAEGAESGRVMAIALHPYIVGQPHRIRALEEALEYIAAHPDVWFATGGEIADWFLA
Q
>gnl|CDD|200602 cd10980, CE4_SpCDA1, Putative catalytic domain of Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), and similar proteins. This family is represented by Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), encoded by the cda1 gene. The general function of chitin deacetylase (CDA) is the synthesis of chitosan from chitin, a polymer of N-acetyl glucosamine, to build up the proper ascospore wall. The actual function of SpCDA1 might be involved in allantoin hydrolysis. It is likely an ortholog to bacterial PuuE allantoinase, whereas it is more distantly related to the CDAs found in other fungi, such as Saccharomyces cerevisiae and Mucor rouxii. Those CDAs are similar with rizobial NodB protein and are not included in this family
WPNNAKIAVSFVLNYEEGSERSPLNGDEITETFLTELGPGPFPNRGVRDVSIESLYEYGSRCGFWRILRL
FKKHGVKFTCFAVGQALEKNPAVAGAMEEGGHEVASHGWRWIDYSGWPVEEEYENIKKAVQAIKKTTPSG
RAPRGWYYGRASLRSRSLVAQVYKELGLPLLWYSDAYNDDLPYWVPYPGGSKPEDDKGLLIVPYTLDTND
YKNAGYQGFINSDDFYTYLRDAFDVLYEEGLEGAPKMMTIGLHCRITGRPGRFAGLRKFMEYITSKEGVW
VATREEIAQAWSEKFPY
>gnl|CDD|211380 cd10981, ZnPC_S1P1, Zinc dependent phospholipase C/S1-P1 nuclease. This model describes both the bacterial and archeal zinc-dependent phospholipase C, a domain found in the alpha toxin of Clostridium perfringens, as well as S1/P1 nucleases, which predominantly act on single-stranded DNA and RNA
GFGTHHKIARDAVFTLPPELAEFWSDLLKRNIDELLEGAVAPDKRRYDDDGEAQNHVLDVDDYGDSALDK
YGEDTLGYWGGAPWQIQEWYQRLVDAFRRKDWKDIAFAAGVLSHYIGDAHVPLHTTQNYNGQLTGQDGIH
RAWETRIPELYAELYALTDAFGDPFVGKADYIKWPKEYIWDAAKHANALYDTVLSHEKELAGSRKYPYEG
RNDVVRKTYSEALAKAYHGLANGLVEAL
>gnl|CDD|199826 cd10985, MH2_SMAD_2_3, C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3. The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain. SMAD2 and SMAD3 are receptor regulated SMADs (R-SMADs). SMAD2 regulates multiple cellular processes, such as cell proliferation, apoptosis and differentiation, while SMAD3 modulates signals of activin and TGF-beta
VTYCEPAFWCSISYYEMNTRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNPQVELTRRHIGKG
VRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLSQSVNQGFEAV
YQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDRVLTQM
>gnl|CDD|199911 cd11005, M35_like, Peptidase M35 family. Family M35 Zn2+-metallopeptidase domain, also known as the deuterolysin family, contains fungal as well as bacterial metalloendopeptidases that include deuterolysin (EC2.4.24.39), peptidyl-Lys metalloendopeptidase (MEP), penicillolysin, as well as uncharacterized sequences. Typically, members of this family of extracellular peptidases contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand and is found in a GTXDXXYG motif C-terminal to the His zinc ligands. Deuterolysins are highly active towards basic nuclear proteins such as histones and protamines, with a preference for a Lys or Arg residue in the P1' subsite. MEPs specifically cleave peptidyl-lysine bonds (-X-Lys-) in proteins and peptides. Penicillolysin, a thermolabile protease from Penicillium citrinum, strongly hydrolyzes nuclear proteins such as clupeine, salmine and histone. Many members of the M35 peptidases display unusual thermostabilities
ICPNMTNSQLRTAASAALKWSNIAVEYLITDLTDKDRYIYWFGRYDSNTRQTVLDGFSRHLSILKTLPHH
SVTFDCNLDMLGCVPNMEFAYVYPPISIAVYLCTNFWGAPPTGADSQAGTVVHEVTHFVDTFGTGDLGYG
QDAAAALAAADPDKALNNADNHEYFAE
>gnl|CDD|199912 cd11006, M35_peptidyl-Lys_like, Peptidase M35 domain of peptidyl-Lys metalloendopeptidases and related proteins. This family M35 Zn2+-metallopeptidase extracellular domain is mostly found in proteins characterized as peptidyl-Lys metalloendopeptidases (MEP; peptidyllysine metalloproteinase; EC 3.4.24.20), including some well-characterized domains in Aeromonas salmonicida subsp. Achromogenes (AsaP1) and Grifola frondosa (GfMEP). These proteins specifically cleave peptidyl-lysine bonds (-X-Lys- where X may even be Pro) in proteins and peptides. AsaP1 peptidase has been shown to be important in the virulence of A. salmonicida subsp. achromogenes, having a major role in the fish innate immune response. Members of this family contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand and is found in a GTXDXXYG or similar motif C-terminal to the His zinc ligands
GCSMKERSAVLTALAAAKSYVLKAASYVGDTSATTPRYRRWFGSYSAERAATVRANFKSIVDALRSGGIT
FDCSGDGCDAAGYAYVYANVPYTVYLCPAFFQLPTRTGNDSRAGTIVHELSHFRGVAGTDDHCYGQANAQ
ELALTDPEAAVENADSYEYFAED
>gnl|CDD|199913 cd11007, M35_like_1, Peptidase M35-like domain of uncharacterized proteins. This family contains proteins similar to the M35 Zn2+-metallopeptidases, also known as the deuterolysin family, presumably these are bacterial metalloendopeptidases that have yet to be characterized. Typically, members of this family of extracellular peptidases contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand; however, members of this family do not contain the GTXDXXYG motif C-terminal to the His zinc ligands that is typical for the M35 proteases. Deuterolysins are highly active towards basic nuclear proteins such as histones and protamines, with a preference for a Lys or Arg residue in the P1' subsite. MEPs specifically cleave peptidyl-lysine bonds (-X-Lys-) in proteins and peptides. Many members of the M35 peptidases display unusual thermostabilities
ICPNMTNKEFRDMILRLRDEALVLIKKRLKDLARWDASEQARVKRWFGRNDEDTRQKLLAGLKKILAVLN
SLTPENFVRSDSEKDTCGCVPNDGDGEAAFVCGPDTISIHVIFCELGAFFDAASNGLDSQASTIIHELSH
FEDTFGTDDHRYGDQGLDPCAAAFRDNPDKAIENADSIAGYIA
>gnl|CDD|199914 cd11008, M35_deuterolysin_like, Peptidase M35 domain of deuterolysins and related proteins. This family M35 Zn2+-metallopeptidase extracellular domain is found in fungal deutrolysins (acid metalloproteinase, neutral proteinase II), including some well-characterized metallopeptidase domains in Aspergillus oryzae (NpII), Aspergillus fumigatus (MEP20), Penicillium roqueforti (protease II) and Emericella nidulans (PepJ peptidase). The neutral proteinase II from Aspergillus oryzae (NpII) unfolds reversibly upon incubation at higher temperatures, and loss in activity is mainly due to autoproteolysis. MEP20 is encoded by the mepB gene, which appears to be associated with the cytoplasmic degradation of small peptides. PepJ peptidase is a thermostable enzyme released under carbon starvation. Most members of this family contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand and is found in a GTXDXXYG or similar motif C-terminal to the His zinc ligands. The aspzincin motif is poorly conserved in one subgroup, that includes Asp f2, a major allergen from Aspergillus fumigatus. This subgroup in addition lacks the key conserved Tyr residue which acts as a proton donor during catalysis, and no protease activity has been detected to date for Asp f2
SCTGSQLKAIRAALSECAKLAQAAAEAASSGNSALFEEYFKTTDQSTRKIVADRFEAIAEECSSTDGGSL
TYYCDDPYGACSSGVLAYTLPSTNLIVFCPAFFDLPPLSQTVCHAQDQATTLLHELTHAPAVYSPGTDDY
AYGYDACKQLSAEQALRNADSYALFAN
>gnl|CDD|211381 cd11009, Zn_dep_PLPC, Zinc dependent phospholipase C (alpha toxin). This domain conveys a zinc dependent phospholipase C activity (EC 3.1.4.3). It is found in a monomeric phospholipase C of Bacillus cereus as well as in the alpha toxin of Clostridium perfringens and Clostridium bifermentans, which is involved in haemolysis and cell rupture. It is also found in a lecithinase of Listeria monocytogenes, which is involved in breaking the 2-membrane vacuoles that surround the bacterium
KLENKITECSTHKFITYQAIKILGNDGKAEAYQFLKKYLYGLNQGLYWADQDWKSGDQYVNHFYDPDTGK
GLYGFPTALTEFRKYYDLALEYWRKGDYEKAMFYLGRALHYLQDLTVPHHAANATAVALNGHSAYENYVE
DHKDDYKLNTAGIYANKPYLSDSPEEYIKENAKYAKKYYPKIYNEKKGSEEAYDRAAGELLPEAQRTTAG
FLLKFLKE
>gnl|CDD|211382 cd11010, S1-P1_nuclease, S1/P1 nucleases and related enzymes. This family summarizes both S1 and P1 nucleases (EC:3.1.30.1) which cleave RNA and single stranded DNA with no base specificity. S1 nuclease is more active on DNA than RNA. Its reaction products are oligonucleotides or single nucleotides with 5' phosphoryl groups. Although its primary substrate is single-stranded, it may also introduce single-stranded breaks in double-stranded DNA or RNA, or DNA-RNA hybrids. It is used as a reagent in nuclease protection assays and in removing single stranded tails from DNA molecules to create blunt ended molecules and opening hairpin loops generated during synthesis of double stranded cDNA. P1 nuclease cleaves its substrate at every position yielding nucleoside 5' monophosphates, and it does not recognize or act on double-stranded DNA. It is useful at removing single stranded strands hanging off the end of double stranded DNA and at completely cleaving melted DNA for simple DNA composition analysis
WGAEGHRIVAEIAEQYLTPKARKAVDRLLGGLSGESLAEAATWADDIRSDPAYKWTAPWHYVNIPDNPCK
FYDERDCPPGGCVVSAIKNYTARLKDPSLSDAERAEALKFLIHFVGDIHQPLHVGSREDGGGNDGDVGGW
FGRKTNLHSVWDSGLIDKAKGSYTELAAALLAALLAEAIETGLEEADAEGDPADWAQESYELACEIYYPN
LPGDTLELSYAYYYKAKPVVEEQLAKAGYRLAAVLNEIF
>gnl|CDD|259898 cd11012, CuRO_6_ceruloplasmin, The sixth cupredoxin domain of Ceruloplasmin. Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the sixth cupredoxin domain of ceruloplasmin
KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYW
YLMGMGNEIDIHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMET
TYTVL
>gnl|CDD|259899 cd11013, Plantacyanin, Plantacyanin is a subclass of phytocyanins, plant type I copper proteins. Plantacyanins belong to the phytocyanin family of blue copper proteins, a ubiquitous family of plant cupredoxins. Plantacyanin is involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. The exact function of plantacyanin is unknown. However plantacyanin is shown to play a role in reproduction in Arabidopsis. Plantacyanins may also be stress-related proteins and be involved in plant defense responses
ATYVVGDSIGWTFGVVGWPNGKTFRAGDVLVFNYDPSAHNVVVVDEGGYRTCKAPPGAIVYTSGDDKITL
PKGVNYFICSFPGHCTSGMKIAVTA
>gnl|CDD|259900 cd11014, Mavicyanin, Mavicyanin is a subclass of phytocyanins, a plant blue copper protein. Mavicyanin is a glycosylated protein isolated from Cucurbita pepo medullosa (zucchini) peelings. It belongs to the phytocyanin family of blue copper proteins, a ubiquitous family of plant cupredoxins. Mavicyanin is involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. The copper is tetrahedrally coordinated by a cysteine, 2 histidines, and a glutamine residue, like in the case of stellacyanin. The biological roles of mavicyanin have not been elucidated yet
TVYKVGDSDGWTVYDSDYYYKWSSSKTFHVGDSLIFQYNKEFHDVTEVTGEEFESCNSTSPIAVYNTGHD
IIKLTKPGQYYFICGVPGHCDSGQKLQVNVT
>gnl|CDD|259901 cd11015, CuRO_2_FVIII_like, The second cupredoxin domain of coagulation factor VIII and similar proteins. Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 2 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins
NQAFVLLFAVFDEGKSWYSEVGERKSRDKFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGT
APEVHSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV
>gnl|CDD|259902 cd11016, CuRO_4_FVIII_like, The fourth cupredoxin domain of coagulation factor VIII and similar proteins. Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 4 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins
DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWY
VLSVGAQTDFLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTV
STC
>gnl|CDD|259903 cd11017, Phytocyanin_like_1, A subclass of phytocyanins, plant blue or type I copper proteins. Phytocyanins are plant blue or type I copper proteins. They are involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Phytocyanins are classified into four groups: stellacyanin, plantacyanin, uclacyanin and early nodulin groups. Members of this unknown subgroup appear to have lost the T1 copper binding site
TLHTVGGNRIGWNPNINYTDWAKMHGFYSGDWLVFRYQRGRHNVVQVNETGYDNCDASNPISNYSSGGRD
IFQLNETKRYYFICGRGYCYGGMKLAITV
>gnl|CDD|259904 cd11018, CuRO_6_FVIII_like, The sixth cupredoxin domain of coagulation factor VIII and similar proteins. Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 6 of unprocessed Factor VIII or the second cupredoxin domain the light chain of circulating Factor VIII, and similar proteins
VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRW
HLLNMGSDEEIHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSA
LFLV
>gnl|CDD|259905 cd11019, OsENODL1_like, Early nodulin-like protein (OsENODL1) and similar proteins. This family includes early nodulin-like protein (OsENODL1) from Oryza sativa and similar proteins. It belongs to the phytocyanin family of blue copper proteins, a ubiquitous family of plant cupredoxins. Phytocyanin is involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. OsENODL1 expression occurs specifically at the late developmental stage of the seeds. Members of this subgroup appear to have lost the T1 copper binding site
REFKVGGKDGWKVPPSASESYNQWAERNRFQVGDSLVFKYDKGNDSVLEVTKEDYDSCNTSSPIARFNDG
NTKFTLDRSGPFYFISGAPGHCEKGQKLIVVVM
>gnl|CDD|259906 cd11020, CuRO_1_CuNIR, Cupredoxin domain 1 of Copper-containing nitrite reductase. Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center, which serves as the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis
VVEVTLTTVEKVVEIAPGVTYTAWTFNGQVPGPVIRVREGDTVELTLTNPGTNTMPHSIDFHAATGPGGG
EFTTIAPGETKTFSFKALYPGVFMYHCATAPVLMHIANGMYGAIIVEPK
>gnl|CDD|259907 cd11021, CuRO_2_ceruloplasmin, The second cupredoxin domain of Ceruloplasmin. Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the second cupredoxin domain of ceruloplasmin
DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKW
HLFGMGNEVDIHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYE
V
>gnl|CDD|259908 cd11022, CuRO_4_ceruloplasmin, The fourth cupredoxin domain of Ceruloplasmin. Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the fourth cupredoxin domain of ceruloplasmin
DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSW
HLFGLGTETDVHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYT
VSQC
>gnl|CDD|259909 cd11023, CuRO_2_ceruloplasmin_like_2, cupredoxin domain of ceruloplasmin homologs. Uncharacterized subfamily of ceruloplasmin homologous proteins. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. Ceruloplasmin also functions in copper transport, amine oxidase and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first domain of the triplicated units
DQEFIENSSIFLDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEAD
KSRRTDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV
>gnl|CDD|259910 cd11024, CuRO_1_2DMCO_NIR_like, The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase. The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. Three copper ions of type 1 lie close to one another near the surface of the central part of the trimer, and, effectively, a trimeric substrate binding site is formed in their vicinity. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities
VREFTLVAEDAEIEIAPGVVFKAWTYNGTVPGPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAMDGT
GLGPIMPGESFTYEFVAEPAGTHLYHCHVQPLKEHIAMGLYGAFIVDPK
>gnl|CDD|410652 cd11026, CYP2, cytochrome P450 family 2. The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, most diverse CYP families in vertebrates. It includes many subfamilies across vertebrate species but not all subfamilies are found in multiple vertebrate taxonomic classes. The CYP2U and CYP2R genes are present in the vertebrate ancestor and are shared across all vertebrate classes, whereas some subfamilies are lineage-specific, such as CYP2B and CYP2S in mammals. CYP2 enzymes play important roles in drug metabolism. The CYP2 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYGVVFSNGERWKQLRRFSLTT
LRNFGMGKRSIEERIQEEAKFLVEAFRKTKGKPFDPTFLLSNAVSNVICSIVFGSRFDYEDKEFLKLLDL
INENLRLLSSPWGQLYNMFPPLLKHLPGPHQKLFRNVEEIKSFIRELVEEHRETLDPSSPRDFIDCFLLK
MEKEKDNPNSEFHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLE
DRAKMPYTDAVIHEVQRFGDIVPLGVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPG
HFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSSPVGPKDPDLTPRFSGFTNSP
RPYQL
>gnl|CDD|410653 cd11027, CYP17A1-like, cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s. This subfamily contains cytochrome P450 17A1 (CYP17A1 or Cyp17a1), cytochrome P450 21 (CYP21 or Cyp21) and similar proteins. CYP17A1, also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione; it catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. This subfamily also contains CYP21, also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2, catalyzes the 21-hydroxylation of steroids and is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. The CYP17A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDLFSRGGKDIAFGDYSPTWKLHRKLAH
SALRLYASGGPRLEEKIAEEAEKLLKRLASQEGQPFDPKDELFLAVLNVICSITFGKRYKLDDPEFLRLL
DLNDKFFELLGAGSLLDIFPFLKYFPNKALRELKELMKERDEILRKKLEEHKETFDPGNIRDLTDALIKA
KKEAEDEGDEDSGLLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLP
TLSDRKRLPYLEATIAEVLRLSSVVPLALPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEF
RPERFLDENGKLVPKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFSPPEGEPPPELEGIPGLV
LYPLPYKV
>gnl|CDD|410654 cd11028, CYP1, cytochrome P450 family 1. The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three functional human members: CYP1A1, CYP1A2 and CYP1B1, which are regulated by the aryl hydrocarbon receptor (AhR), ligand-activated transcriptional factor that dimerizes with AhR nuclear translocator (ARNT). CYP1 enzymes are involved in the metabolism of endogenous hormones, xenobiotics, and drugs. Included in the CYP1 family is CYP1D1 (cytochrome P450 family 1, subfamily D, polypeptide 1), which is not expressed in humans as its gene is pseudogenized due to five nonsense mutations in the putative coding region, but is functional in in other organisms including cynomolgus monkey. Zebrafish CYP1D1 expression is not regulated by AhR. The CYP1 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFISNGKSMAFSDYGPRWKLHRKLAQN
ALRTFSNARTHNPLEEHVTEEAEELVTELTENNGKPGPFDPRNEIYLSVGNVICAICFGKRYSRDDPEFL
ELVKSNDDFGAFVGAGNPVDVMPWLRYLTRRKLQKFKELLNRLNSFILKKVKEHLDTYDKGHIRDITDAL
IKASEEKPEEEKPEVGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRER
LPRLSDRPNLPYTEAFILETMRHSSFVPFTIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPS
VFRPERFLDDNGLLDKTKVDKFLPFGAGRRRCLGEELARMELFLFFATLLQQCEFSVKPGEKLDLTPIYG
LTMKPKPFKV
>gnl|CDD|410655 cd11029, CYP107-like, cytochrome P450 family 107 and similar cytochrome P450s. This group contains bacterial cytochrome P450s from families 107 (CYP107), 154 (CYP154), 197 (CYP197), and similar proteins. Among the members of this group are: Pseudonocardia autotrophica vitamin D(3) 25-hydroxylase (also known as CYP197A; EC 1.14.15.15) that catalyzes the hydroxylation of vitamin D(3) into 25-hydroxyvitamin D(3) and 1-alpha,25-dihydroxyvitamin D(3), its physiologically active forms; Saccharopolyspora erythraea CYP107A1, also called P450eryF or 6-deoxyerythronolide B hydroxylase (EC 1.14.15.35), that catalyzes the conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB; Bacillus megaterium CYP107DY1 that displays C6-hydroxylation activity towards mevastatin to produce pravastatin; Streptomyces coelicolor CYP154C1 that shows activity towards 12- and 14-membered ring macrolactones in vitro and may be involved in catalyzing the site-specific oxidation of the precursors to macrolide antibiotics, which introduces regiochemical diversity into the macrolide ring system; and Nocardia farcinica CYP154C5 that acts on steroids with regioselectivity and stereoselectivity, converting various pregnans and androstans to yield 16 alpha-hydroxylated steroid products. Bacillus subtilis CYP107H1 is not included in this group. The CYP107-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
PHPEYARLREQGPVHRVRLPGGVPAWLVTRYDDARAALADPRLSKDPRKAWPAFRGRAPGAPPDLPPVLS
DNMLTSDPPDHTRLRRLVAKAFTPRRVEALRPRIEEITDELLDALAARGVVDLVADFAYPLPITVICELL
GVPEEDRDRFRRWSDALVDTDPPPEEAAAALRELVDYLAELVARKRAEPGDDLLSALVAARDEGDRLSEE
ELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLALLRADPELWPAAVEELLRYDGPVALATLRFATED
VEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITRDANGHLAFGHGIHYCLGAPLARLEAEIALGAL
LTRFPDLRLAVPPDELRWRPSFLLRGLRALPVRL
>gnl|CDD|410656 cd11030, CYP105-like, cytochrome P450 family 105 and similar cytochrome P450s. This group predominantly contains bacterial cytochrome P450s, including those belonging to families 105 (CYP105) and 165 (CYP165). Also included in this group are fungal family 55 proteins (CYP55). CYP105s are predominantly found in bacteria belonging to the phylum Actinobacteria and the order Actinomycetales, and are associated with a wide variety of pathways and processes, from steroid biotransformation to production of macrolide metabolites. CYP105A1 catalyzes two sequential hydroxylations of vitamin D3 with differing specificity and cytochrome P450-SOY (also known as CYP105D1) has been shown to be capable of both oxidation and dealkylation reactions. CYP105D6 and CYP105P1, from the filipin biosynthetic pathway, perform highly regio- and stereospecific hydroxylations. Other members of this group include, but are not limited to: CYP165D3 (also called OxyE) from the teicoplanin biosynthetic gene cluster of Actinoplanes teichomyceticus, which is responsible for the phenolic coupling of the aromatic side chains of the first and third peptide residues in the teicoplanin peptide; Micromonospora griseorubida cytochrome P450 MycCI that catalyzes hydroxylation at the C21 methyl group of mycinamicin VIII, the earliest macrolide form in the postpolyketide synthase tailoring pathway; and Fusarium oxysporum CYP55A1 (also called nitric oxide reductase cytochrome P450nor) that catalyzes an unusual reaction, the direct electron transfer from NAD(P)H to bound heme. The CYP105-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
PPAEYAELREEGPVSRVTLPDGRPAWLVTGHDEVRAVLADPRFSSDRTRPGFPALSPEGKAAAALPGSFI
RMDPPEHTRLRRMLAPEFTVRRVRALRPRIQEIVDELLDAMEAAGPPADLVEAFALPVPSLVICELLGVP
YEDREFFQRRSARLLDLSSTAEEAAAAGAELRAYLDELVARKRREPGDDLLSRLVAEHGAPGELTDEELV
GIAVLLLVAGHETTANMIALGTLALLEHPEQLAALRADPSLVPGAVEELLRYLSIVQDGLPRVATEDVEI
GGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITRPARRHLAFGHGVHQCLGQNLARLELEIALPTLFRR
FPGLRLAVPAEELPFRPDSLVYGVHELPVTW
>gnl|CDD|410657 cd11031, Cyp158A-like, cytochrome P450 family 158, subfamily A and similar cytochrome P450s. This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces coelicolor CYP158A1 and CYP158A2, Streptomyces natalensis PimD (also known as CYP107E), Mycobacterium tuberculosis CYP121, and Micromonospora griseorubida MycG (also known as CYP107B). CYP158A1 and CYP158A2 catalyze an unusual oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments; CYP158A2 produces three isomers of biflaviolin and one triflaviolin while CYP158A1 produces only two isomers of biflaviolin. PimD is a cytochrome P450 monooxygenase with native epoxidase activity that is critical in the biosynthesis of the polyene macrolide antibiotic pimaricin. CYP121 is essential for the viability of M. tuberculosis and is a novel drug target for the inhibition of mycobacterial growth. MycG catalyzes both hydroxylation and epoxidation reactions in the biosynthesis of the 16-membered ring macrolide antibiotic mycinamicin II. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
PPPEYAELRREGPVARVRLPYGDEAWLVTRYADVRQVLADPRFSRAAAAPPDAPRLTPEPLLPGSLMSMD
PPEHTRLRRLVAKAFTARRVERLRPRIEEIADELLDAMEAQGPPADLVEALALPLPVAVICELLGVPYED
RERFRAWSDALLSTSALTPEEAEAARQELRGYMAELVAARRAEPGDDLLSALVAARDDDDRLSEEELVTL
AVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRADPELVPAAVEELLRYIPLGAGGGFPRYATEDVELG
GVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDREPNPHLAFGHGPHHCLGAPLARLELQVALGALLRRL
PGLRLAVPEEELRWREGLLTRGPEELPVTW
>gnl|CDD|410658 cd11032, P450_EryK-like, cytochrome P450 EryK and similar cytochrome P450s. This subfamily contains archaeal and bacterial CYPs including Saccharopolyspora erythraea P450 EryK, Saccharolobus solfataricus cytochrome P450 119 (CYP119), Picrophilus torridus CYP231A2, Bacillus subtilis CYP109, Streptomyces himastatinicus HmtT and HmtN, and Bacillus megaterium CYP106A2, among others. EryK, also called erythromycin C-12 hydroxylase, is active during the final steps of erythromycin A (ErA) biosynthesis. CYP106A2 catalyzes the hydroxylation of a variety of 3-oxo-delta(4)-steroids such as progesterone and deoxycorticosterone, mainly in the 15beta-position. It is also capable of hydroxylating a variety of terpenoids. HmtT and HmtN is involved in the post-tailoring of the cyclohexadepsipeptide backbone during the biosynthesis of the himastatin antibiotic. The EryK-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
REESPVYYDEETGAWHVFRYADVKRVLSDPATFSSDLGRLLPGEDDALTEGSLLTMDPPRHRKLRKLVSQ
AFTPRLIADLEPRIAEITDELLDAVDGRGEFDLVEDLAYPLPVIVIAELLGVPAEDRELFKKWSDALVSG
LGDDSFEEEEVEEMAEALRELNAYLLEHLEERRRNPRDDLISRLVEAEVDGERLTDEEIVGFAILLLIAG
HETTTNLLGNAVLCLDEDPEVAARLRADPSLIPGAIEEVLRYRPPVQRTARVTTEDVELGGVTIPAGQLV
IAWLASANRDERQFEDPDTFDIDRNPNPHLSFGHGIHFCLGAPLARLEARIALEALLDRFPRIRVDPDVP
LELIDSPVVFGVRSLPVR
>gnl|CDD|410659 cd11033, CYP142-like, cytochrome P450 family 142 and similar cytochrome P450s. This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces sp. P450sky (also called CYP163B3), Sphingopyxis macrogoltabida P450pyr hydroxylase, Novosphingobium aromaticivorans CYP108D1, Pseudomonas sp. cytochrome P450-Terp (P450terp), and Amycolatopsis balhimycina P450 OxyD, as well as several Mycobacterium proteins CYP124, CYP125, CYP126, and CYP142. P450sky is involved in the hydroxylation of three beta-hydroxylated amino acid precursors required for the biosynthesis of the cyclic depsipeptide skyllamycin. P450pyr hydroxylase is an active and selective catalyst for the regio- and stereo-selective hydroxylation at non-activated carbon atoms with a broad substrate range. P450terp catalyzes the hydroxylation of alpha-terpineol as part of its catabolic assimilation. OxyD is involved in beta-hydroxytyrosine formation during vancomycin biosynthesis. CYP124 is a methyl-branched lipid omega-hydroxylase while CYP142 is a cholesterol 27-oxidase with likely roles in host response modulation and cholesterol metabolism. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
FARLRAEAPVHWHPPPDGGPGFWAVTRHADVVAVSRDPELFSSARGGVLIDLPEEDADPAAGRMLINMDP
PRHTRLRRLVSRAFTPRAVARLEDRIRERARRLVDRALARGECDFVEDVAAELPLQVIADLLGVPEEDRP
KLLEWTNELVGADDPDYAGEAEEELAAALAELFAYFRELAEERRANPGDDLISVLANAEVDGEPLTDEEF
ASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLRADPSLLPTAVEEILRWASPVIHFRRTATRDTEL
GGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITRSPNPHLAFGGGPHFCLGAHLARLELRVLFEELLDR
VPDIELAGEPERLRSNFVNGIKSLPVRF
>gnl|CDD|410660 cd11034, P450cin-like, P450cin and similar cytochrome P450s. This group is composed of Citrobacter braakii cytochrome P450cin (P450cin, also called CYP176A1) and similar proteins. P450cin is a bacterial P450 enzyme that catalyzes the enantiospecific hydroxylation of 1,8-cineole to (1R)-6beta-hydroxycineole; its natural reduction-oxidation partner is cindoxin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
RETCPVGHSDALGGFWVLTRYAEVQAVARDTDTFSSKGVTFPRPELGEFRLMPIETDPPEHKKYRKLLNP
FFTPEAVEAFRPRVRQLTNDLIDAFIERGECDLVTELANPLPARLTLRLLGLPDEDGERLRDWVHAILHD
EDPEEGAAAFAELFGHLRDLIAERRANPRDDLISRLIEGEIDGKPLSDGEVIGFLTLLLLGGTDTTSSAL
SGALLWLAQHPEDRRRLIADPSLIPNAVEEFLRFYSPVAGLARTVTQEVEVGGCRLKPGDRVLLAFASAN
RDEEKFEDPDRIDIDRTPNRHLAFGSGVHRCLGSHLARVEARVALTEVLKRIPDFELDPGATCEFLDSGT
VRGLRTLPVIF
>gnl|CDD|410661 cd11035, P450cam-like, P450cam and similar cytochrome P450s. This family is composed of cytochrome P450s (CYPs) with similarity to Pseudomonas putida P450cam and Cyp101 proteins from Novosphingobium aromaticivorans such as CYP101C1 and CYP101D2. P450cam catalyzes the hydroxylation of camphor in a process that involves two electron transfers from the iron-sulfur protein, putidaredoxin. CYP101D2 is capable of oxidizing camphor while CYP101C1 does not bind camphor but is capable of binding and hydroxylating ionone derivatives such as alpha- and beta-ionone and beta-damascone. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
RDGPPIVYTPRNGGHWIVTRGEDIREVLRDPETFSSRVITVPPPAGEPYPLIPLELDPPEHTRYRRLLNP
LFSPKAVAALEPRIRERAVELIESFAPRGECDFVADFAEPFPTRVFLELMGLPLEDLDRFLEWEDAMLRP
DDAEERAAAAQAVLDYLTPLIAERRANPGDDLISAILNAEIDGRPLTDDELLGLCFLLFLAGLDTVASAL
GFIFRHLARHPEDRRRLREDPELIPAAVEELLRRYPLVNVARIVTRDVEFHGVQLKAGDMVLLPLALANR
DPREFPDPDTVDFDRKPNRHLAFGAGPHRCLGSHLARLELRIALEEWLKRIPDFRLAPGAQPTYHGGSVM
GLESLPLVW
>gnl|CDD|410662 cd11036, AknT-like, AknT-like proteins. This family is composed of proteins similar to Streptomyces biosynthesis proteins including anthracycline biosynthesis proteins DnrQ and AknT, and macrolide antibiotic biosynthesis proteins TylM3 and DesVIII. Streptomyces peucetius DnrQ is involved in the biosynthesis of carminomycin and daunorubicin (daunomycin) while Streptomyces galilaeus AknT functions in the biosynthesis of aclacinomycin A. Streptomyces fradiae TylM3 is involved in the biosynthesis of tylosin derived from the polyketide lactone tylactone, and Streptomyces venezuelae functions in the biosynthesis of methymycin, neomethymycin, narbomycin, and pikromycin. These proteins are required for the glycosylation of specific substrates during the biosynthesis of specific anthracyclines and macrolide antibiotics. Although members of this family belong to the large cytochrome P450 (P450, CYP) superfamily and show significant similarity to cytochrome P450s, they lack heme-binding sites and are not functional cytochromes
ARGPLYRSDLLGLWVTSDAAAADAVLADPALRVRPAAGPVPPAAGLPFGRLVRMTDGPDHSALRPAAAPA
LGGADVRPLAERARARALDAAPPGFDLVADFLRPLPVRVAAALLGLPADDRARFARLFAALAPALDSLLC
ARALLAARALLRAALAELLALTRSAAADALALSAPGDLVANAILLAVQGAEAAAGLVGNAVLALLRRPAQ
WARLRPDPELAAAAVAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFD
LGRPTARSAHFGLGRHACLGAALARAAAAAALRALAARFPGLRAAGPVVRRLNARIPVFP
>gnl|CDD|410663 cd11037, CYP199A2-like, cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s. This family is composed of cytochrome P450s (CYPs) with similarity to Rhodopseudomonas palustris CYP199A2 and CYP199A4. CYP199A2 catalyzes the oxidation of aromatic carboxylic acids including indole-2-carboxylic acid, 2-naphthoic acid and 4-ethylbenzoic acid. CYP199A4 catalyzes the hydroxylation of para-substituted benzoic acids. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
DPYPHYAELRDAGPVVYLEKYDVYALARYDEVRAALRDHETFSSARGVGLNDFLNWRLPGSILASDPPEH
DRLRAVLSRPLSPRALRKLRDRIEEAADELVDELVARGEFDAVTDLAEAFPLRVVPDLVGLPEEGRENLL
PWAAATFNAFGPLNERTRAALPRLKELRDWVAEQCARERLRPGGWGAAIFEAADRGEITEDEAPLLMRDY
LSAGLDTTISAIGNALWLLARHPDQWERLRADPSLAPNAFEEAVRLESPVQTFSRTTTRDTELAGVTIPA
GSRVLVFLGSANRDPRKWDDPDRFDITRNPSGHVGFGHGVHACVGQHLARLEGEALLTALARRVDRIELA
GPPVRALNNTLRGLASLPVRI
>gnl|CDD|410664 cd11038, CYP_AurH-like, cytochrome P450 AurH and similar cytochrome P450s. This group includes Streptomyces thioluteus P450 monooxygenase AurH which is uniquely capable of forming a homochiral tetrahydrofuran ring, a vital component of the polyketide antibiotic aureothin. AurH catalyzes an unprecedented tandem oxygenation process: first, it catalyzes an asymmetric hydroxylation of deoxyaureothin to yield (7R)-7-hydroxydeoxyaureothin as an intermediate; and second, it mediates another C-O bond formation that leads to O-heterocyclization. The AurH-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
TDPAFSWDSPEVAEAREKSWYARTPYGLAVLRYEEVGQLLRDRRLRQGGHRWLAMNGVTEGPFADWWVDF
LLSLEGADHARLRGLVNPAFTPKAVEALRPRFRATANDLIDGFAEGGECEFVEAFAEPYPARVICTLLGL
PEEDWPRVHRWSADLGLAFGLEVKDHLPRIEAAVEELYDYADALIEARRAEPGDDLISTLVAAEQDGDRL
SDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPDQWRALREDPELAPAAVEEVLRWCPTTTWATREAV
EDVEYNGVTIPAGTVVHLCSHAANRDPRVFDADRFDITAKRAPHLGFGGGVHHCLGAFLARAELAEALTV
LARRLPTPAIAGEPTWLPDSGNTGPATLPLRF
>gnl|CDD|410665 cd11039, P450-pinF2-like, P450-pinF2 and similar cytochrome P450s. This family is composed of cytochrome P450s (CYPs) with similarity to Agrobacterium tumefaciens P450-pinF2, whose expression is induced by the presence of wounded plant tissue and by plant phenolic compounds such as acetosyringone. P450-pinF2 may be involved in the detoxification of plant protective agents at the site of wounding. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
DPYPIYARMRSEAPVAYVPSLRETLVTRRDDIRAVEKDIEVFSSSQPAGLMNVLMGHNMMRKDGEAHACE
RRAIFPTFSPKTVKSYWAALFRAVVQRFLDDIEPGGAADLFTELAEPVSARCLKDILGLTETSNAELDRW
SQAMIDGAGNYSGDPEVEARCDEATAGIDAAIDALIPVHRSNPNPSLLSVMLNAGMPMSLEQIRANIKVA
IGGGLNEPRDAIAGTCWGLLSNPEQLAEVMAGDVHWLRAFEEGLRWISPIGMSPRRVAEDFEIRGVTLPA
GDRVFLMFGSANRDEARFENPDRFDVFRPKSPHVSFGAGPHFCAGAWASRQMVGEIALPELFRRLPNLIR
LDPEARIGGWAFRGPINLPVRW
>gnl|CDD|410666 cd11040, CYP7_CYP8-like, cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome P450 family 7, subfamily B, polypeptide 1, cytochrome P450 family 8, subfamily A, polypeptide 1. This family is composed of cytochrome P450s (CYPs) with similarity to the human P450s CYP7A1, CYP7B1, CYP8B1, CYP39A1 and prostacyclin synthase (CYP8A1). CYP7A1, CYP7B1, CYP8B1, and CYP39A1 are involved in the catabolism of cholesterol to bile acids (BAs) in two major pathways. CYP7A1 (cholesterol 7alpha-hydroxylase) and CYP8B1 (sterol 12-alpha-hydroxylase) function in the classic (or neutral) pathway, which leads to two bile acids: cholic acid (CA) and chenodeoxycholic acid (CDCA). CYP7B1 and CYP39A1 are 7-alpha-hydroxylases involved in the alternative (or acidic) pathway, which leads mainly to the formation of CDCA. Prostacyclin synthase (CYP8A1) catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
LLRNGKKYFSGGPIFTIRLGGQKIYVITDPELISAVFRNPKTLSFDPIVIVVVGRVFGSPESAKKKEGEP
GGKGLIRLLHDLHKKALSGGEGLDRLNEAMLENLSKLLDELSLSGGTSTVEVDLYEWLRDVLTRATTEAL
FGPKLPELDPDLVEDFWTFDRGLPKLLLGLPRLLARKAYAARDRLLKALEKYYQAAREERDDGSELIRAR
AKVLREAGLSEEDIARAELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAILDL
TDLLTSCPLLDSTYLETLRLHSSSTSVRLVTEDTVLGGGYLLRKGSLVMIPPRLLHMDPEIWGPDPEEFD
PERFLKKDGDKKGRGLPGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDVEPVGGGDWKVPGMDESP
GLGILPPKRDVR
>gnl|CDD|410667 cd11041, CYP503A1-like, cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s. This family is composed of predominantly fungal cytochrome P450s (CYPs) with similarity to Fusarium fujikuroi Cytochrome P450 503A1 (CYP503A1, also called ent-kaurene oxidase or cytochrome P450-4), Aspergillus nidulans austinol synthesis protein I (ausI), Alternaria alternata tentoxin synthesis protein 1 (TES1), and Acanthamoeba polyphaga mimivirus cytochrome P450 51 (CYP51, also called P450-LIA1 or sterol 14-alpha demethylase). Ent-kaurene oxidase catalyzes three successive oxidations of the 4-methyl group of ent-kaurene to form kaurenoic acid, an intermediate in gibberellin biosynthesis. AusI and TES1 are cytochrome P450 monooxygenases that mediate the biosynthesis of the meroterpenoids, austinol and dehydroaustinol, and the phytotoxin tentoxin, respectively. P450-LIA1 catalyzes the 14-alpha demethylation of obtusifoliol and functions in steroid biosynthesis. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
KEGYEKYKKNGGPFQLPTPDGPLVVLPPKYLDELRNLPESVLSFLEALEEHLAGFGTGGSVVLDSPLHVD
VVRKDLTPNLPKLLPDLQEELRAALDEELGSCTEWTEVNLYDTVLRIVARVSARVFVGPPLCRNEEWLDL
TINYTIDVFAAAAALRLFPPFLRPLVAPFLPEPRRLRRLLRRARPLIIPEIERRRKLKKGPKEDKPNDLL
QWLIEAAKGEGERTPYDLADRQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTK
AALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVTLSDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFD
GFRFYRLREQPGQEKKHQFVSTSPDFLGFGHGRHACPGRFFASNEIKLILAHLLLNYDFKLPEGGERPKN
IWFGEFIMPDPNAKVLVRRRE
>gnl|CDD|410668 cd11042, CYP51-like, cytochrome P450 family 51 and similar cytochrome P450s. This family is composed of cytochrome P450 51 (CYP51 or sterol 14alpha-demethylase) and related cytochrome P450s. CYP51 is the only cytochrome P450 enzyme with a conserved function across animals, fungi, and plants, in the synthesis of essential sterols. In mammals, it is expressed in many different tissues, with highest expression in testis, ovary, adrenal gland, prostate, liver, kidney, and lung. In fungi, CYP51 is a significant drug target for treatment of human protozoan infections. In plants, it functions within a specialized defense-related metabolic pathway. CYP51 is also found in several bacterial species. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
CRKKYGDVFTFNLLGKKVTVLLGPEANEFFFNGKDEDLSAEEVYGFLTPPFGGGVVYYAPFAEQKEQLKF
GLNILRRGKLRGYVPLIVEEVEKYFAKWGESGEVDLFEEMSELTILTASRCLLGKEVRELLDDEFAQLYH
DLDGGFTPIAFFFPPLPLPSFRRRDRARAKLKEIFSEIIQKRRKSPDKDEDDMLQTLMDAKYKDGRPLTD
DEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDDPLTYDVLKEMPLLHACIK
ETLRLHPPIHSLMRKARKPFEVEGGGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSKG
GKFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDSPFPEPDYTTMVVWPKGPARVRYK
>gnl|CDD|410669 cd11043, CYP90-like, plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, cytochrome P450 family 90, subfamily B, polypeptide 1, and cytochrome P450 family 90, subfamily D, polypeptide 2. This family is composed of plant cytochrome P450s including: Arabidopsis thaliana cytochrome P450s 85A1 (CYP85A1 or brassinosteroid-6-oxidase 1), 90A1 (CYP90A1), 88A3 (CYP88A3 or ent-kaurenoic acid oxidase 1), 90B1 (CYP90B1 or Dwarf4 or steroid 22-alpha-hydroxylase), and 90C1 (CYP90C1 or 3-epi-6-deoxocathasterone 23-monooxygenase); Oryza sativa cytochrome P450s 90D2 (CYP90D2 or C6-oxidase), 87A3 (CYP87A3), and 724B1 (CYP724B1 or dwarf protein 11); and Taxus cuspidata cytochrome P450 725A2 (CYP725A2 or taxane 13-alpha-hydroxylase). These enzymes are monooxygenases that catalyze oxidation reactions involved in steroid or hormone biosynthesis. CYP85A1, CYP90D2, and CYP90C1 are involved in brassinosteroids biosynthesis, while CYP88A3 catalyzes three successive oxidations of ent-kaurenoic acid, which is a key step in the synthesis of gibberellins. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
RIKRYGPVFKTSLFGRPTVVSADPEANRFILQNEGKLFVSWYPKSVRKLLGKSSLLTVSGEEHKRLRGLL
LSFLGPEALKDRLLGDIDELVRQHLDSWWRGKSVVVLELAKKMTFELICKLLLGIDPEEVVEELRKEFQA
FLEGLLSFPLNLPGTTFHRALKARKRIRKELKKIIEERRAELEKASPKGDLLDVLLEEKDEDGDSLTDEE
ILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIAKRKEEGEGLTWEDYKSMKYTWQVIN
ETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGVPYTFL
PFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEVVPDEKISRFPLPRPPKGLPIRLSP
>gnl|CDD|410670 cd11044, CYP120A1_CYP26-like, cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate cytochrome P450 family 26 enzymes, and similar cytochrome P450s. This family includes cyanobacterial CYP120A1 and vertebrate cytochrome P450s 26A1 (CYP26A1), 26B1 (CYP26B1), and 26C1 (CYP26C1). These are retinoic acid-metabolizing cytochromes that play key roles in retinoic acid (RA) metabolism. Human and zebrafish CYP26a1, as well as Synechocystis CYP120A1 are characterized as RA hydroxylases. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
GETLEFLRDPEDFIQSRYQKYGPVFKTHLLGRPTVFVIGAEAVRFILSGEGKLVRYGWPRSVRRLLGENS
LSLQDGEEHRRRRKLLAPAFSREALESYVPTIQAIVQSYLRKWLKAGEVALYPELRRLTFDVAARLLLGL
DPEVEAEALSQDFETWTDGLFSLPVPLPFTPFGRAIRARNKLLARLEQAIRERQEEENAEAKDALGLLLE
AKDEDGEPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLEEPLTLESLKK
MPYLDQVIKEVLRLVPPVGGGFRKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPA
RSEDKKKPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWELLPNQDLEPVVVPTPRPKDGLRVRF
>gnl|CDD|410671 cd11045, CYP136-like, putative cytochrome P450 family 136 and similar cytochrome P450s. This group is composed of Mycobacterium tuberculosis putative cytochrome P450 136 (CYP136) and similar proteins. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
EFARQRYRRYGPVSWTGMLGLRVVALLGPDANQLVLRNRDKAFSSKQGWDPVIGPFFHRGLMLLDFDEHR
AHRRIMQQAFTRSALAGYLDRMTPGIERALARWPTGAGFQFYPAIKELTLDLATRVFLGVDLGPEADKVN
KAFIDTVRASTAIIRTPIPGTRWWRGLRGRRYLEEYFRRRIPERRAGGGDDLFSALCRAEDEDGDRFSDD
DIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLALGKGTLDYEDLGQLEVTDWVFKEALR
LVPPVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVHRYAWAP
FGGGAHKCIGLHFAGMEVKAILHQMLRRFRWWSVPGYYPPWWQSPLPAPKDGLPVVL
>gnl|CDD|410672 cd11046, CYP97, cytochrome P450 family/clan 97. CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). Members of the CYP97 clan include Arabidopsis thaliana cytochrome P450s 97A3 (CYP97A3), CYP97B3, and CYP97C1. CYP97A3 is also called protein LUTEIN DEFICIENT 5 (LUT5) and CYP97C1 is also called carotene epsilon-monooxygenase or protein LUTEIN DEFICIENT 1 (LUT1). These cytochromes function as beta- and epsilon-ring carotenoid hydroxylases and are involved in the biosynthesis of xanthophylls. CYP97 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
LDLYKWFLEYGPIYKLAFGPKSFLVISDPAIAKHVLRSNAFSYDKKGLLAEILEPIMGKGLIPADGEIWK
KRRRALVPALHKDYLEMMVRVFGRCSERLMEKLDAAAETGESVDMEEEFSSLTLDIIGLAVFNYDFGSVT
EESPVIKAVYLPLVEAEHRSVWEPPYWDIPAALFIVPRQRKFLRDLKLLNDTLDDLIRKRKEMRQEEDIE
LQQEDYLNEDDPSLLRFLVDMRDEDVDSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAE
VDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLPGGGVKVPAGTDIFISVYNLH
RSPELWEDPEEFDPERFLDPFINPPNEVIDDFAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELD
VGPRHVGMTTGATIHTKNGLK
>gnl|CDD|410673 cd11049, CYP170A1-like, cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s. This subfamily is composed of Streptomyces coelicolor cytochrome P450 170A1 (CYP170A1), Streptomyces avermitilis pentalenene oxygenase, and similar actinobacterial cytochrome P450s. CYP170A1, also called epi-isozizaene 5-monooxygenase (EC 1.14.13.106)/(E)-beta-farnesene synthase (EC 4.2.3.47), catalyzes the two-step allylic oxidation of epi-isozizaene to albaflavenone, which is a sesquiterpenoid antibiotic. Pentalenene oxygenase (EC 1.14.15.32) catalyzes the conversion of pentalenene to pentalen-13-al by stepwise oxidation via pentalen-13-ol, a precursor of the neopentalenolactone antibiotic. The CYP170A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
DPLGFLSSLRAHGDLVRIRLGPRPAYVVTSPELVRQVLVNDRVFDKGGPLFDRARPLLGNGLATCPGEDH
RRQRRLMQPAFHRSRIPAYAEVMREEAEALAGSWRPGRVVDVDAEMHRLTLRVVARTLFSTDLGPEAAAE
LRQALPVVLAGMLRRAVPPKFLERLPTPGNRRFDRALARLRELVDEIIAEYRASGTDRDDLLSLLLAARD
EEGRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLGGRPATFEDLPRLTY
TRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAA
AVPRGAFIPFGAGARKCIGDTFALTELTLALATIASRWRLRPVPGRPVRPRPLATLRPRRLRMRV
>gnl|CDD|410674 cd11051, CYP59-like, cytochrome P450 family 59 and similar cytochrome P450s. This family is composed of Aspergillus nidulans cytochrome P450 59 (CYP59), also called sterigmatocystin biosynthesis P450 monooxygenase stcS, and similar fungal proteins. CYP59 is required for the conversion of versicolorin A to sterigmatocystin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
FYLDLWPFAPPLLVVTDPELAEQITQVTNLPKPPPLRKFLTPLTGGSSLISMEGEEWKRLRKRFNPGFSP
QHLMTLVPTILDEVEIFAAILRELAESGEVFSLEELTTNLTFDVIGRVTLDIDLHAQTGDNSLLTALRLL
LALYRSLLNPFKRLNPLRPLRRWRNGRRLDRYLKPEVRKRFELERAIDQIKTFLFAGHDTTSSTLCWAFY
LLSKHPEVLAKVRAEHDEVFGPDPSAAAELLREGPELLNQLPYTTAVIKETLRLFPPAGTARRGPPGVGL
TDRDGKEYPTDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHELYPPKSAWRPFERGPRNCIGQEL
AMLELKIILAMTVRRFDFEKAYDEWDAKGGYKGLKELFVTGQGTAHPVDGMPC
>gnl|CDD|410675 cd11052, CYP72_clan, Plant cytochrome P450s, clan CYP72. CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). The CYP72 clan is associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. This clan includes: CYP734 enzymes that are involved in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis; CYP714 enzymes that are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels; and CYP72 family enzymes, among others. The CYP72 clan belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
LPHYYHWIKQYGKNFLYWYGTDPRLYVTEPELIKELLSKKEGYFGKSPLQPGLKKLLGRGLVMSNGEKWA
KHRRIANPAFHGEKLKGMVPAMVESVSDMLERWKKQMGEEGEEVDVFEEFKALTADIISRTAFGSSYEEG
KEVFKLLRELQKICAQANRDVGIPGSRFLPTKGNKKIKKLDKEIEDSLLEIIKKREDSLKMGRGDDYGDD
LLGLLLEANQSDDQNKNMTVQEIVDECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKD
KPPSDSLSKLKTVSMVINESLRLYPPAVFLTRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWGEDAN
EFNPERFADGVAKAAKHPMAFLPFGLGPRNCIGQNFATMEAKIVLAMILQRFSFTLSPTYRHAPTVVLTL
RPQYGLQ
>gnl|CDD|410676 cd11053, CYP110-like, cytochrome P450 family 110 and similar cytochrome P450s. This group is composed of mostly uncharacterized proteins, including Nostoc sp. probable cytochrome P450 110 (CYP110) and putative cytochrome P450s 139 (CYP139), 138 (CYP138), and 135B1 (CYP135B1) from Mycobacterium bovis. CYP110 genes, unique to cyanobacteria, are widely distributed in heterocyst-forming cyanobacteria including nitrogen-fixing genera Nostoc and Anabaena. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
VGFLERLRARYGDVFTLRVPGLGPVVVLSDPEAIKQIFTADPDVLHPGEGNSLLEPLLGPNSLLLLDGDR
HRRRRKLLMPAFHGERLRAYGELIAEITEREIDRWPPGQPFDLRELMQEITLEVILRVVFGVDDGERLQE
LRRLLPRLLDLLSSPLASFPALQRDLGPWSPWGRFLRARRRIDALIYAEIAERRAEPDAERDDILSLLLS
ARDEDGQPLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPDPEDIAKLP
YLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRKP
SPYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPRPERPVRRGVTLAPSRGVRMVV
>gnl|CDD|410677 cd11054, CYP24A1-like, cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s. This family is composed of vertebrate cytochrome P450 24A1 (CYP24A1) and similar proteins including several Drosophila proteins such as CYP315A1 (also called protein shadow) and CYP314A1 (also called ecdysone 20-monooxygenase), and vertebrate CYP11 and CYP27 subfamilies. Both CYP314A1 and CYP315A1, which has ecdysteroid C2-hydroxylase activity, are involved in the metabolism of insect hormones. CYP24A1 and CYP27B1 have roles in calcium homeostasis and metabolism, and the regulation of vitamin D. CYP24A1 catabolizes calcitriol (1,25(OH)2D), the physiologically active vitamin D hormone, by catalyzing its hydroxylation, while CYP27B1 is a calcidiol 1-monooxygenase that coverts 25-hydroxyvitamin D3 to calcitriol. The CYP24A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
HKKYGPIVREKLGGRDIVHLFDPDDIEKVFRNEGKYPIRPSLEPLEKYRKKRGKPLGLLNSNGEEWHRLR
SAVQKPLLRPKSVASYLPAINEVADDFVERIRRLRDEDGEEVPDLEDELYKWSLESIGTVLFGKRLGCLD
DNPDSDAQKLIEAVKDIFESSAKLMFGPPLWKYFPTPAWKKFVKAWDTIFDIASKYVDEALEELKKKDEE
DEEEDSLLEYLLSKPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGE
PITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEE
FIPERWLRDDSENKNIHPFASLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHEELKVKTRLILV
PDKPLK
>gnl|CDD|410678 cd11055, CYP3A-like, cytochrome P450 family 3, subfamily A and similar cytochrome P450s. This family includes vertebrate CYP3A subfamily enzymes and CYP5a1, and similar proteins. CYP5A1, also called thromboxane-A synthase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid. CYP3A enzymes are drug-metabolizing enzymes embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. The CYP3A-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
KYGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNRPLFILLDEPFDSSLLFLKGERWKRLRTTLSPT
FSSGKLKLMVPIINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQNNPDDPFLKA
AKKIFRNSIIRLFLLLLLFPLRLFLFLLFPFVFGFKSFSFLEDVVKKIIEQRRKNKSSRRKDLLQLMLDA
QDSDEDVSKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYD
TVSKLKYLDMVINETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPER
FSPENKAKRHPYAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVPCKETEIPLKLVGGATLSPKNG
IY
>gnl|CDD|410679 cd11056, CYP6-like, cytochrome P450 family 6 and similar cytochrome P450s. This family is composed of cytochrome P450s from insects and crustaceans, including the CYP6, CYP9 and CYP310 subfamilies, which are involved in the metabolism of insect hormones and xenobiotic detoxification. The CYP6-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
GGEPFVGIYLFRRPALLVRDPELIKQILVKDFAHFHDRGLYSDEKDDPLSANLFSLDGEKWKELRQKLTP
AFTSGKLKNMFPLMVEVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFGLDANSLNDPENEFRE
MGRRLFEPSRLRGLKFMLLFFFPKLARLLRLKFFPKEVEDFFRKLVRDTIEYREKNNIVRNDFIDLLLEL
KKKGKIEDDKSEKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHGGE
LTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGTDVVIEKGTPVIIPVYALHHDPKYYPEPE
KFDPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKTKIPLKLSPKSF
VLSPKGGIW
>gnl|CDD|410680 cd11057, CYP313-like, cytochrome P450 family 313 and similar cytochrome P450s. This subfamily is composed of insect cytochrome P450s from families 313 (CYP313) and 318 (CYP318), and similar proteins. These proteins may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. Their specific function is yet unknown. They belong to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
GSPFRAWLGPRPFVITSDPEIVQVVLNSPHCLNKSFFYDFFRLGRGLFSAPYPIWKLQRKALNPSFNPKI
LLSFLPIFNEEAQKLVQRLDTYVGGGEFDILPDLSRCTLEMICQTTLGSDVNDESDGNEEYLESYERLFE
LIAKRVLNPWLHPEFIYRLTGDYKEEQKARKILRAFSEKIIEKKLQEVELESNLDSEEDEENGRKPQIFI
DQLLELARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDGQFIT
YEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSNGVVIPKGTTIVIDIFNMHRRKDIWGPDADQF
DPDNFLPERSAQRHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLKTSLRLEDLRFKFNITLKL
ANGHLVT
>gnl|CDD|410681 cd11058, CYP60B-like, cytochrome P450 family 60, subfamily B and similar cytochrome P450s. This family is composed of fungal cytochrome P450s including: Aspergillus nidulans cytochrome P450 60B (CYP60B), also called versicolorin B desaturase, which catalyzes the conversion of versicolorin B to versicolorin A during sterigmatocystin biosynthesis; Fusarium sporotrichioides cytochrome P450 65A1 (CYP65A1), also called isotrichodermin C-15 hydroxylase, which catalyzes the hydroxylation at C-15 of isotricodermin in trichothecene biosynthesis; and Penicillium aethiopicum P450 monooxygenase vrtK, also called viridicatumtoxin synthesis protein K, which catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to produce viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP60B-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
GPVVRIAPNELSFISPEAWKDIYGHRPGGPKFPKKDPRFYPPAPNGPPSISTADDEDHARLRRLLAHAFS
EKALREQEPIIQRYVDLLVSRLRERAGSGTPVDMVKWFNFTTFDIIGDLAFGESFGCLENGEYHPWVALI
FDSIKALTIIQALRRYPWLLRLLRLLIPKSLRKKRKEHFQYTREKVDRRLAKGTDRPDFMSYILRNKDEK
KGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSSEDDITLDSLAQLPYLN
AVIQEALRLYPPVPAGLPRVVPAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRF
EFDNDKKEAFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPESEDWLDQQKVYILWEKPPLMV
>gnl|CDD|410682 cd11059, CYP_fungal, unknown subfamily of fungal cytochrome P450s. This subfamily is composed of uncharacterized fungal cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle
GPVVRLGPNEVSVNDLDAVREIYGGGFGKTKSYWYFTLRGGGGPNLFSTLDPKEHSARRRLLSGVYSKSS
LLRAAMEPIIRERVLPLIDRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLLGDKDSRERELL
RRLLASLAPWLRWLPRYLPLATSRLIIGIYFRAFDEIEEWALDLCARAESSLAESSDSESLTVLLLEKLK
GLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLPGPFRGPPDLEDLDK
LPYLNAVIRETLRLYPPIPGSLPRVVPEGGATIGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWL
DPSGETAREMKRAFWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTSTTTDDDMEQEDAFLAAPKGRRC
LL
>gnl|CDD|410683 cd11060, CYP57A1-like, cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s. This family is composed of fungal cytochrome P450s including: Nectria haematococca cytochrome P450 57A1 (CYP57A1), also called pisatin demethylase, which detoxifies the phytoalexin pisatin; Penicillium aethiopicum P450 monooxygenase gsfF, also called griseofulvin synthesis protein F, which catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A during the biosynthesis of griseofulvin, a spirocyclic fungal natural product used to treat dermatophyte infections; and Penicillium aethiopicum P450 monooxygenase vrtE, also called viridicatumtoxin synthesis protein E, which catalyzes hydroxylation at C5 of the polyketide backbone during the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP57A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
GPVVRIGPNEVSISDPEAIKTIYGTRSPYTKSDWYKAFRPKDPRKDNLFSERDEKRHAALRRKVASGYSM
SSLLSLEPFVDECIDLLVDLLDEKAVSGKEVDLGKWLQYFAFDVIGEITFGKPFGFLEAGTDVDGYIASI
DKLLPYFAVVGQIPWLDRLLLKNPLGPKRKDKTGFGPLMRFALEAVAERLAEDAESAKGRKDMLDSFLEA
GLKDPEKVTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEGKLSSPITFAE
AQKLPYLQAVIKEALRLHPPVGLPLERVVPPGGATICGRFIPGGTIVGVNPWVIHRDKEVFGEDADVFRP
ERWLEADEEQRRMMDRADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELVDPEKEWKTRNYWFVKQ
SDFDV
>gnl|CDD|410684 cd11061, CYP67-like, cytochrome P450 family 67 and similar cytochrome P450s. This subfamily includes Uromyces viciae-fabae cytochrome P450 67 (CYP67), also called planta-induced rust protein 16, Cystobasidium minutum (Rhodotorula minuta) cytochrome P450rm, and other fungal cytochrome P450s. P450rm catalyzes the formation of isobutene and 4-hydroxylation of benzoate. The gene encoding CYP67 is a planta-induced gene that is expressed in haustoria and rust-infected leaves. The CYP67-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
GDVVRIGPNELSINDPDALKDIYGHGSNCLKGPFYDALSPSASLTFTTRDKAEHARRRRVWSHAFSDKAL
RGYEPRILSHVEQLCEQLDDRAGKPVSWPVDMSDWFNYLSFDVMGDLAFGKSFGMLESGKDRYILDLLEK
SMVRLGVLGHAPWLRPLLLDLPLFPGATKARKRFLDFVRAQLKERLKAEEEKRPDIFSYLLEAKDPETGE
GLDLEELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIRLGPKLKSLPYLR
ACIDEALRLSPPVPSGLPRETPPGGLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEE
LVRARSAFIPFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRLAPGEDGEAGEGGFKDAFGRGPGDLR
>gnl|CDD|410685 cd11062, CYP58-like, cytochrome P450 family 58-like fungal cytochrome P450s. This group includes Fusarium sporotrichioides cytochrome P450 58 (CYP58, also known as Tri4 and trichodiene oxygenase), and similar fungal proteins. CYP58 catalyzes the oxygenation of trichodiene during the biosynthesis of trichothecenes, which are sesquiterpenoid toxins that act by inhibiting protein biosynthesis. The CYP58-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
GPIVRINPNELHISDPDFYDEIYAGGSRRRKDPPYFYGAFGAPGSTFSTVDHDLHRLRRKALSPFFSKRS
ILRLEPLIQEKVDKLVSRLREAKGTGEPVNLDDAFRALTADVITEYAFGRSYGYLDEPDFGPEFLDALRA
LAEMIHLLRHFPWLLKLLRSLPESLLKRLNPGLAVFLDFQESIAKQVDEVLRQVSAGDPPSIVTSLFHAL
LNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMPDPDSPPSLAE
LEKLPYLTAVIKEGLRLSYGVPTRLPRVVPDEGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPE
RWLGAAEKGKLDRYLVPFSKGSRSCLGINLAYAELYLALAALFRRFDLELYETTEEDVEIVHDFFLGVPK
PGSKG
>gnl|CDD|410686 cd11063, CYP52, cytochrome P450 family 52. Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases catalyze the first hydroxylation step in the assimilation of alkanes and fatty acids by filamentous fungi. The number of CYP52 proteins depend on the fungal species: for example, Candida tropicalis has seven, Candida maltose has eight, and Yarrowia lipolytica has twelve. The CYP52 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
YGNTFEVNLLGTRVIFTIEPENIKAVLATQFKDFGLGERRRDAFKPLLGDGIFTSDGEEWKHSRALLRPQ
FSRDQISDLELFERHVQNLIKLLPRDGSTVDLQDLFFRLTLDSATEFLFGESVDSLKPGGDSPPAARFAE
AFDYAQKYLAKRLRLGKLLWLLRDKKFREACKVVHRFVDPYVDKALARKEESKDEESSDRYVFLDELAKE
TRDPKELRDQLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRA
VINETLRLYPPVPLNSRVAVRDTTLPRGGGPDGKSPIFVPKGTRVLYSVYAMHRRKDIWGPDAEEFRPER
WEDLKRPGWEYLPFNGGPRICLGQQFALTEASYVLVRLLQTFDRIESRDVRPPEERLTLTLSNANGVKV
>gnl|CDD|410687 cd11064, CYP86A, cytochrome P450 family 86, subfamily A. This subfamily includes several Arabidopsis thaliana cytochrome P450s (CYP86A1, CYP86A2, CYP86A4, among others), Petunia x hybrida CYP86A22, and Vicia sativa CYP94A1 and CYP94A2. They are P450-dependent fatty acid omega-hydroxylases that catalyze the omega-hydroxylation of various fatty acids. CYP86A2 acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18; CYP86A22 prefers substrates with chain lengths of C16 and C18; and CYP94A1 acts on various fatty acids from 10 to 18 carbons. They play roles in the biosynthesis of extracellular lipids, cutin synthesis, and plant defense. The CYP86A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
FTFRGPWPGGPDGIVTADPANVEHILKTNFDNYPKGPEFRDLFFDLLGDGIFNVDGELWKFQRKTASHEF
SSRALREFMESVVREKVEKLLVPLLDHAAESGKVVDLQDVLQRFTFDVICKIAFGVDPGSLSPSLPEVPF
AKAFDDASEAVAKRFIVPPWLWKLKRWLNIGSEKKLREAIRVIDDFVYEVISRRREELNSREEENNVRED
LLSRFLASEEEEGEPVSDKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKLTT
DESRVPTYEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPDGTFVKKGTRIVYSIYAMGRMESIW
GEDALEFKPERWLDEDGGLRPESPYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKVEP
KMSLTLHMKGGL
>gnl|CDD|410688 cd11065, CYP64-like, cytochrome P450 family 64-like fungal cytochrome P450s. This group includes Aspergillus flavus cytochrome P450 64 (CYP64), also called O-methylsterigmatocystin (OMST) oxidoreductase or aflatoxin B synthase or aflatoxin biosynthesis protein Q, and similar fungal cytochrome P450s. CYP64 converts OMST to aflatoxin B1 and converts dihydro-O-methylsterigmatocystin (DHOMST) to aflatoxin B2 in the aflatoxin biosynthesis pathway. The CYP64-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAGELMGWGMRLLLMPYGPRWRLHRRLFH
QLLNPSAVRKYRPLQELESKQLLRDLLESPDDFLDHIRRYAASIILRLAYGYRVPSYDDPLLRDAEEAME
GFSEAGSPGAYLVDFFPFLRYLPSWLGAPWKRKARELRELTRRLYEGPFEAAKERMASGTATPSFVKDLL
EELDKEGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRP
NLPYVNAIVKEVLRWRPVAPLGIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYL
DDPKGTPDPPDPPHFAFGFGRRICPGRHLAENSLFIAIARLLWAFDIKKPKDEGGKEIPDEPEFTDGLVS
HPLPF
>gnl|CDD|410689 cd11066, CYP_PhacA-like, fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase. This group includes Aspergillus nidulans phenylacetate 2-hydroxylase (encoded by the phacA gene) and similar fungal cytochrome P450s. PhacA catalyzes the ortho-hydroxylation of phenylacetate, the first step of A. nidulans phenylacetate catabolism. The PhacA-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
NGPVFQIRLGNKRIVVVNSFASVRDLWIKNSSALNSRPTFYTFHKVVSSTQGFTIGTSPWDESCKRRRKA
AASALNRPAVQSYAPIIDLESKSFIRELLRDSAEGKGDIDPLIYFQRFSLNLSLTLNYGIRLDCVDDDSL
LLEIIEVESAISKFRSTSSNLQDYIPILRYFPKMSKFRERADEYRNRRDKYLKKLLAKLKEEIEDGTDKP
CIVGNILKDKESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPGQEIQEKAYEEILEAYGNDED
AWEDCAAEEKCPYVVALVKETLRYFTVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDP
DEFIPERWLDASGDLIPGPPHFSFGAGSRMCAGSHLANRELYTAICRLILLFRIGPKDEEEPMELDPFEY
NACPTALVAEPKPF
>gnl|CDD|410690 cd11067, CYP152, cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases. The cytochrome P450 152 (CYP152) family enzymes act as peroxygenases, converting fatty acids through oxidative decarboxylation, yielding terminal alkenes, and via alpha- and beta-hydroxylation to yield hydroxy-fatty acids. Included in this family are Bacillus subtilis CYP152A1, also called cytochrome P450BsBeta, that catalyzes the alpha- and beta-hydroxylation of long-chain fatty acids such as myristic acid in the presence of hydrogen peroxide, and Sphingomonas paucimobilis CYP152B1, also called cytochrome P450(SPalpha), that hydroxylates fatty acids with high alpha-regioselectivity. The CYP152 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
DSTLALLREGYRFISNRCRRLGSDAFRTRLMGRPAICLRGPEAARLFYDEDRFTRKGAMPPRVQKTLFGK
GGVQGLDGEAHRHRKAMFMSLMTPERVARLARLFRREWRAALARWEGRDEVVLFDEAQEVLTRAACRWAG
VPLPEEDVERRARDLAAMIDGAGAVGPRHWRARLARRRAERWAAELIEDVRAGRLAPPEGTPLAAIAHHR
DPDGELLPERVAAVELLNLLRPTVAVARFVTFAALALHEHPEWRERLRSGDEDYAEAFVQEVRRFYPFFP
FVGARARRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGWEGDPFDFIPQGGGDHATGH
RCPGEWITIALMKEALRLLARRDYYDVPPQDLSIDLNRMPALPRSGFVIR
>gnl|CDD|410691 cd11068, CYP120A1, cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome P450/NADPH--P450 reductase. Cytochrome P450 102A1, also called cytochrome P450(BM-3) or P450BM-3, is a bifunctional cytochrome P450/NADPH--P450 reductase. These proteins fuse an N-terminal cytochrome p450 with a C-terminal cytochrome p450 reductase (CYPOR). It functions as a fatty acid monooxygenase, catalyzing the hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions, with activity towards fatty acids with a chain length of 9-18 carbons. Its NADPH-dependent reductase activity (via the C-terminal domain) allows electron transfer from NADPH to the heme iron of the N-terminal cytochrome P450. CYP120A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
PVQSLLRLADELGPIFKLTLPGRRVVVVSSHDLIAELCDESRFDKKVSGPLEELRDFAGDGLFTAYTHEP
NWGKAHRILMPAFGPLAMRGYFPMMLDIAEQLVLKWERLGPDEPIDVPDDMTRLTLDTIALCGFGYRFNS
FYRDEPHPFVEAMVRALTEAGRRANRPPILNKLRRRAKRQFREDIALMRDLVDEIIAERRANPDGSPDDL
LNLMLNGKDPETGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPP
PYEQVAKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLGGKYPLKKGDPVLVLLPALHRDPSVWGEDAEE
FRPERFLPEEFRKLPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQRFDFEDDPDYELDIKETLTLKP
DGFRLKARPR
>gnl|CDD|410692 cd11069, CYP_FUM15-like, Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s. Fusarium verticillioides cytochrome P450 monooxygenase FUM15, is also called fumonisin biosynthesis cluster protein 15. The FUM15 gene is part of the gene cluster that mediates the biosynthesis of fumonisins B1, B2, B3, and B4, which are carcinogenic mycotoxins. This FUM15-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
YGGLIRYRGLFGSERLLVTDPKALKHILVTNSYDFEKPPAFRRLLRRILGDGLLAAEGEEHKRQRKILNP
AFSYRHVKELYPIFWSKAEELVDKLEEEIEESGDESISIDVLEWLSRATLDIIGLAGFGYDFDSLENPDN
ELAEAYRRLFEPTLLGSLLFILLLFLPRWLVRILPWKANREIRRAKDVLRRLAREIIREKKAALLEGKDD
SGKDILSILLRANDFADDERLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAAL
PDPPDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEI
WGPDAEEFNPERWLEPDGAASPGGAGSNYALLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELDPDA
EVERPIGIITRPPVDGL
>gnl|CDD|410693 cd11070, CYP56-like, cytochrome P450 family 56-like fungal cytochrome P450s. This group includes Saccharomyces cerevisiae cytochrome P450 56, also called cytochrome P450-DIT2, and similar fungal proteins. CYP56 is involved in spore wall maturation and is thought to catalyze the oxidation of tyrosine residues in the formation of LL-dityrosine-containing precursors of the spore wall. The CYP56-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
KLGAVKILFVSRWNILVTKPEYLTQIFRRRDDFPKPGNQYKIPAFYGPNVISSEGEDWKRYRKIVAPAFN
ERNNALVWEESIRQAQRLIRYLLEEQPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDEEESSLHDT
LNAIKLAIFPPLFLNFPFLDRLPWVLFPSRKRAFKDVDEFLSELLDEVEAELSADSKGKQGTESVVASRL
KRARRSGGLTEKELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYEED
FPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVVITGLGQEIVIPKGTYVGYNAYATHRDPTIWGPDADE
FDPERWGSTSGEIGAATRFTPARGAFIPFSAGPRACLGRKFALVEFVAALAELFRQYEWRVDPEWEEGET
PAGATRDSPAKLRLRFRE
>gnl|CDD|410694 cd11071, CYP74, cytochrome P450 family 74. The cytochrome P450 74 (CYP74) family controls several enzymatic conversions of fatty acid hydroperoxides to bioactive oxylipins in plants, some invertebrates, and bacteria. It includes two dehydrases, namely allene oxide synthase (AOS) and divinyl ether synthase (DES), and two isomerases, hydroperoxide lyase (HPL) and epoxyalcohol synthase (EAS). AOS (EC 4.2.1.92, also called hydroperoxide dehydratase), such as Arabidopsis thaliana CYP74A acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides. DES (EC 4.2.1.121), also called colneleate synthase or CYP74D, catalyzes the selective removal of pro-R hydrogen at C-8 in the biosynthesis of colneleic acid. The linolenate HPL, Arabidopsis thaliana CYP74B2, is required for the synthesis of the green leaf volatiles (GLVs) hexanal and trans-2-hexenal. The fatty acid HPL, Solanum lycopersicum CYP74B, is involved in the biosynthesis of traumatin and C6 aldehydes. The epoxyalcohol synthase Ranunculus japonicus CYP74A88 (also known as RjEAS) specifically converts linoleic acid 9- and 13-hydroperoxides to oxiranyl carbinols 9,10-epoxy-11-hydroxy-12-octadecenoic acid and 11-hydroxy-12,13-epoxy-9-octadecenoic acid, respectively. The CYP74 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
KSRMEKYKSTVFRVNMPPGPPISSDPRVVALLDAKSFPVLFDNSKVEKEDVFGGTYMPSTSFTGGYRVLP
YLDTSEPKHAKLKAFLFELLKSRSSRFIPEFRSALSELFDKWEAELAKKGKASFNDDLEKLAFDFLFRLL
FGADPSETKLGSDGPDALDKWLALQLAPTLSLGLPKILEELLLHTFPLPFFLVKPDYQKLYKFFANAGLE
VLDEAEKLGLSREEAVHNLLFMLGFNAFGGFSALLPSLLARLGLAGEELHARLAEEIRSALGSEGGLTLA
ALEKMPLLKSVVYETLRLHPPVPLQYGRARKDFVIESHDASYKIKKGELLVGYQPLATRDPKVFDNPDEF
VPDRFMGEEGKLLKHLIWSNGPETEEPTPDNKQCPGKDLVVLLARLFVAELFLRYDTFTIEPGWTGKKLS
VTVT
>gnl|CDD|410695 cd11072, CYP71-like, cytochrome P450 family 71 and similar cytochrome P450s. The group includes plant cytochrome P450 family 71 (CYP71) proteins, as well as some CYPs designated as belonging to a different family including CYP99A1, CYP83B1, and CYP84A1, among others. Characterized CYP71 enzymes include: parsnip (Pastinaca sativa) CYP71AJ4, also called angelicin synthase, that converts (+)-columbianetin to angelicin, an angular furanocumarin; periwinkle (Catharanthus roseus) CYP71D351, also called tabersonine 16-hydroxylase 2, that is involved in the foliar biosynthesis of vindoline; sorghum CYP71E1, also called 4-hydroxyphenylacetaldehyde oxime monooxygenase, that catalyzes the conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile; as well as maize CYP71C1, CYP71C2, and CYP71C4, which are monooxygenases catalyzing the oxidation of 3-hydroxyindolin-2-one, indolin-2-one, and indole, respectively. CYPs within a single CYP71 subfamily, such as the C subfamily, usually metabolize similar/related compounds. The CYP71-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
KYGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILSYGGKDIAFAPYGEYWRQMRKIC
VLELLSAKRVQSFRSIREEEVSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQDKFK
ELVKEALELLGGFSVGDYFPSLGWIDLLTGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLL
DLRLQKEGDLEFPLTRDNIKAIILDMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVT
EEDLEKLKYLKAVIKETLRLHPPAPLLLPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFR
PERFLDSSIDFKGQDFELIPFGAGRRICPGITFGLANVELALANLLYHFDWKLPDGMKPEDLDMEEAFGL
TVHRKNPL
>gnl|CDD|410696 cd11073, CYP76-like, cytochrome P450 family 76 and similar cytochrome P450s. Characterized members of the plant cytochrome P450 family 76 (CYP76 or Cyp76) include: Catharanthus roseus CYP76B6, a multifunctional enzyme catalyzing two sequential oxidation steps leading to the formation of 8-oxogeraniol from geraniol; the Brassicaceae-specific CYP76C subfamily of enzymes that are involved in the metabolism of monoterpenols and phenylurea herbicides; and two P450s from Lamiaceae, CYP76AH and CYP76AK, that are involved in the oxidation of abietane diterpenes. CYP76AH produces ferruginol and 11-hydroxyferruginol, while CYP76AK catalyzes oxidations at the C20 position. Also included in this group is Berberis stolonifera Cyp80, also called berbamunine synthase or (S)-N-methylcoclaurine oxidase [C-O phenol-coupling], that catalyzes the phenol oxidation of N-methylcoclaurine to form the bisbenzylisoquinoline alkaloid berbamunine. The CYP76-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRK
ICTTELFSPKRLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDSES
GSEFKELVREIMELAGKPNVADFFPFLKFLDLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKD
DDLLLLLDLELDSESELTRNHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDK
IVEESDISKLPYLQAVVKETLRLHPPAPLLLPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPL
EFKPERFLGSEIDFKGRDFELIPFGSGRRICPGLPLAERMVHLVLASLLHSFDWKLPDGMKPEDLDMEEK
FGLTLQKAVPLKAIP
>gnl|CDD|410697 cd11074, CYP73, cytochrome P450 family 73. Cytochrome P450 family 73 (CYP73 pr Cyp73), also called trans-cinnamate 4-monooxygenase (EC 1.14.14.91) or cinnamic acid 4-hydroxylase, catalyzes the regiospecific 4-hydroxylation of cinnamic acid to form precursors of lignin and many other phenolic compounds. It controls the general phenylpropanoid pathway, and controls carbon flux to pigments essential for pollination or UV protection. CYP73 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
KKFGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGEHWRKMRRI
MTVPFFTNKVVQQYRYGWEEEAARVVEDVKKNPEAATEGIVIRRRLQLMMYNNMYRIMFDRRFESEDDPL
FVKLKALNGERSRLAQSFEYNYGDFIPILRPFLRGYLKICKEVKERRLQLFKDYFVDERKKLGSTKSTKN
EGLKCAIDHILDAQKKGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGP
GVQITEPDLHKLPYLQAVVKETLRLRMAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKK
PEEFRPERFLEEESKVEANGNDFRYLPFGVGRRSCPGIILALPILGITIGRLVQNFELLPPPGQSKIDTS
EKGGQFSLHILKHS
>gnl|CDD|410698 cd11075, CYP77_89, cytochrome P450 families 77 and 89, and similar cytochrome P450s. This group includes cytochrome P450 families 73 (CYP77) and 89 (CYP89), which are sister families that share a common ancestor. CYP89, present only in angiosperms, is younger than CYP77, which is already found in lycopods; thus, CYP89 may have evolved from CYP77 after duplication and divergence. Also included in this group is ent-kaurene oxidase, called CYP701A3 in Arabidopsis thaliana and CYP701B1 in Physcomitrella patens, that catalyzes the oxidation of ent-kaurene to form ent-kaurenoic acid. CYP701A3 is sensitive to inhibitor uniconazole-P while CYP701B1 is not. This CYP77/89 group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPLRVLFSSNKHMVNSSPYGPLWRTLRRN
LVSEVLSPSRLKQFRPARRRALDNLVERLREEAKENPGPVNVRDHFRHALFSLLLYMCFGERLDEETVRE
LERVQRELLLSFTDFDVRDFFPALTWLLNRRRWKKVLELRRRQEEVLLPLIRARRKRRASGEADKDYTDF
LLLDLLDLKEEGGERKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEA
VVTEEDLPKMPYLKAVVLETLRRHPPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPE
EFKPERFLAGGEAADIDTGSKEIKMMPFGAGRRICPGLGLATLHLELFVARLVQEFEWKLVEGEEVDFSE
KQEFTVVMKNPLR
>gnl|CDD|410699 cd11076, CYP78, cytochrome P450 family 78. Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins include: CYP78A5, which is expressed in leaf, flora and embryo, and has been reported to stimulate plant organ growth in Arabidopsis thaliana and to regulate plant architecture, ripening time, and fruit mass in tomato; Glycine max CYP78A10 that functions in regulating seed size/weight and pod number; and Physcomitrella patens CYP78A27 or CYP78A28, which together, are essential in bud formation. The CYP78 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
RAKRLMAFSLGETRVVITSHPETAREILNSPAFADRPVKESAYELMFNRAIGFAPYGEYWRNLRRIASNH
LFSPRRIAASEPQRQAIAAQMVKAIAKEMERSGEVAVRKHLQRASLNNIMGSVFGRRYDFEAGNEEAEEL
GEMVREGYELLGAFNWSDHLPWLRWLDLQGIRRRCSALVPRVNTFVGKIIEEHRAKRSNRARDDEDDVDV
LLSLQGEEKLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDV
AKLPYLQAVVKETLRLHPPGPLLSWARLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPER
FVAAEGGADVSVLGSDLRLAPFGAGRRVCPGKALGLATVHLWVAQLLHEFEWLPDDAKPVDLSEVLKLSC
EMKNPL
>gnl|CDD|410700 cd11078, CYP130-like, cytochrome P450 family 130-like and similar cytochrome P450s. This subfamily includes Mycobacterium tuberculosis cytochrome P450 130 (CYP130), Rhodococcus erythropolis CYP116, and similar bacterial proteins. CYP130 catalyzes the N-demethylation of dextromethorphan, and has also shown a natural propensity to bind primary arylamines. CYP116 is involved in the degradation of thiocarbamate herbicides. The CYP130-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
YPFYARLRDEEPVFFSEPLGYWVVSRYEDVKAVLRDPQTFSSAGGLTPESPLWPEAGFAPTPSLVNEDPP
RHTRLRRLVSRAFTPRRIAALEPRIRELAAELLDRLAEDGRADFVADFAAPLPALVIAELLGVPEEDMER
FRRWADAFALVTWGRPSEEEQVEAAAAVGELWAYFADLVAERRREPRDDLISDLLAAADGDGERLTDEEL
VAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRADPSLIPNAVEETLRYDSPVQGLRRTATRDVEI
GGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDRPNARKHLTFGHGIHFCLGAALARMEARIALEELLR
RLPGMRVPGQEVVYSPSLSFRGPESLPVEW
>gnl|CDD|410701 cd11079, Cyp_unk, unknown subfamily of mostly bacterial cytochrome P450s. This subfamily is composed of uncharacterized cytochrome P450s, predominantly from bacteria. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle
CPVAHSDDGFWVVLRHADVKAAAEDPETFSSAVSARLSVPNGMDPPEHTAYRAAIDRYFTPERLARFEPV
CRRVAARLVAELPAGGGGDVVGQFAQPFAVRVQTAFLGWPAALERPLAEWVNKNHAATRSGDRAATAEVA
EEFDGIIRDLLADRRAAPRDADDDVTARLLRERVDGRPLTDEEIVSILRNWTVGELGTIAACVGVLVHYL
ARHPELQARLRANPALLPAAIDEILRLDDPFVANRRITTRDVELGGRTIPAGSRVTLNWASANRDERVFG
DPDEFDPDRHAADNLVYGRGIHVCPGAPLARLELRILLEELLAQTEAITLAAGGPPERATYPVGGYASVP
>gnl|CDD|410702 cd11080, CYP134A1, cytochrome P450 family 134, subfamily A, polypeptide 1. Cytochrome P450 134A1 (CYP134A1, EC 1.14.15.13), also called pulcherriminic acid synthase or cyclo-L-leucyl-L-leucyl dipeptide oxidase or cytochrome P450 CYPX, catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms the red pigment pulcherrimin via a non-enzymatic spontaneous reaction with Fe(3+). It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
DPVHYEESIDSYFVSRYEDVRRILKDPDGFTTKSLAERAEPVMRGPVLAQMTGKEHAAKRAIVVRAFRGD
ALDHLLPLIKENAEELIAPFLERGRVDLVNDFGKPFAVNVTMDMLGLDKRDHEKIHEWHSSVAAFITSLS
QDPEARAHGLRCAEQLSQYLLPVIEERRVNPGSDLISILCTAEYEGEALSDEDIKALILNVLLAATEPAD
KTLALMIYHLLNNPEQLAAVRADRSLVPRAIAETLRYHPPVQLIPRQASQDVVVSGMEIKKGTTVFCLIG
AANRDPAAFEDPDTFNIHREDLGIRSAFSGAADHLAFGSGRHFCVGAALAKREIEIVANQVLDALPNIRL
EPGFEYAESGLYTRGPVSLL
>gnl|CDD|410703 cd11082, CYP61_CYP710, C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 710. C-22 sterol desaturase (EC 1.14.19.41), also called sterol 22-desaturase, is required for the formation of the C-22 double bond in the sterol side chain of delta22-unsaturated sterols, which are present specifically in fungi and plants. This enzyme is also called cytochrome P450 61 (CYP61) in fungi and cytochrome P450 710 (CYP710) in plants. The CYP61/CYP710 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop
GLSSNVLVGKFIVFVTDAELSRKIFSNNRPDAFHLCLHPNAKKILGEDNLIFMFGEEHKELRKSLLPLFT
RKALGLYLPIQERVIRKHLAKWLENSKSGDKPIEMRPLIRDLNLETSQTVFVGPYLDDEARRFRIDYNYF
NVGFLALPVDFPGTALWKAIQARKRIVKTLEKCAAKSKKRMAAGEEPTCLLDFWTHEILEEIKEAEEEGE
PPPPHSSDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEPPLTLDLLEEM
KYTRQVVKEVLRYRPPAPMVPHIAKKDFPLTEDYTVPKGTIVIPSIYDSCFQGFPEPDKFDPDRFSPERQ
EDRKYKKNFLVFGAGPHQCVGQEYAINHLMLFLALFSTLVDWKRHRTPGSDEIIYFPTIYPKDGC
>gnl|CDD|410704 cd11083, CYP_unk, unknown subfamily of cytochrome P450s. This subfamily is composed of uncharacterized cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle
GSAYRFRLGRQPVLVISDPELIREVLRRRPDEFRRISSLESVFREMGINGVFSAEGDAWRRQRRLVMPAF
SPKHLRYFFPTLRQITERLRERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGYDLNTLERGGDPLQEHL
ERVFPMLNRRVNAPFPYWRYLRLPADRALDRALVEVRALVLDIIAAARARLAANPALAEAPETLLAMMLA
EDDPDARLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPLLEALD
RLPYLEAVARETLRLKPVAPLLFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLD
GARAAEPHDPSSLLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFDIELPEPAPAVGEEFAFTMSPEGLRV
R
>gnl|CDD|199893 cd11234, E_set_GDE_N, N-terminal Early set domain associated with the catalytic domain of Glycogen debranching enzyme. E or "early" set domains are associated with the catalytic domain of the glycogen debranching enzyme at the N-terminal end. Glycogen debranching enzymes have both 4-alpha-glucanotransferase and amylo-1,6-glucosidase activities. As a transferase, it transfers a segment of a 1,4-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or another 1,4-alpha-D-glucan. As a glucosidase, it catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. The N-terminal domain of the glycogen debranching enzyme may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase
GATIVGGGVNFSVAVPEGKSCELLLYRKGEKEPYAEIPFPEEYRIGDVRSMAVFGLDEEEYEYNYDIDGK
IVLDPYAKALSGREVWGDKDEGAKHQVRGRV
>gnl|CDD|200496 cd11235, Sema_semaphorin, The Sema domain, a protein interacting module, of semaphorins. Semaphorins are regulator molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. They can be divided into 7 classes. Vertebrates have members in classes 3-7, whereas classes 1 and 2 are known only in invertebrates. Class 2 and 3 semaphorins are secreted proteins; classes 1 and 4 through 6 are transmembrane proteins; and class 7 is membrane associated via glycosylphosphatidylinositol (GPI) linkage. The semaphorins exert their function through their receptors, the neuropilin and plexin families. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
LKYHTKLLHEDRSTLYVGARDRVYLVDLDSLYTEQKVAWPSSPDDVDTCYLKGKSKDDCRNFIKVLEKNS
DDSLLVCGTNAFNPSCRNYNVETFELVGKEESGRGKCPYDPDHNSTALFADGELYSGTSADFLGTDPVIY
RTLGHNPPLRTEYHDSKWLNEPQFVGAFDIGDYVYFFFREIAVEYINCGKAVYSRVARVCKNDQGGSRSL
EKKWTTFLKARLNCSVPGEFPFYFNELQDVFDLPSPSNKEKIFYAVFTTPYNSIPGSAVCAYSLSDIEAV
FNGPFKEQHSSNSAWLPVPDERVPEPRPGTCVDDSSPLPDDTLNFIKSHPLMDEAVTPILNRPLFIKTDV
NYRFTKIAVDRVQAKLGQTYDVLFVGTDRGIILKVVSLPEQGLQASNILEEMPVGPPPEPIQTMQLSRKR
RSLYVGSETGVLQVPLA
>gnl|CDD|200497 cd11236, Sema_plexin_like, The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine kinases. Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestor of semaphorins. Ligand binding activates signal transduction pathways controlling axon guidance in the nervous system and other developmental processes including cell migration and morphogenesis, immune function, and tumor progression. Plexins are divided into four types (A-D) according to sequence similarity. In vertebrates, type A Plexins serve as the co-receptors for neuropilins to mediate the signalling of class 3 semaphorins except Sema3E, which signals through Plexin D1. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B. Plexin C1 serves as the receptor of Sema7A and plays regulation roles in both immune and nervous systems. This family also includes the Met and RON receptor tyrosine kinases. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module
PFNHLAVDNSTGRVYVGAVNRLYQLDSSLLLEAEVSTGPVLDSPLCLPPGCCSCDHPRSPTDNYNKILLI
DYSSGRLITCGSLYQGVCQLRNLSNISVVVERSSTPVAANDPNASTVGFVGPGPYNNENVLYVGATYTNN
GYRDYRPAVSSRSLPPDDDFNAGSLTGGSAISIDDEYRDRYSIKYVYGFSSGGFSYFVTVQRKSVDDESP
YISRLVRVCQSDSNYYSYTEVPLQCTGGDGTNYNLLQAAYVGKAGSDLARSLGISTDDDVLFGVFSKSKG
PSAEPSSKSALCVFSMKDIEAAFNDNCPLGGGVPITTSAVLSDSLLTSVAVTTTRNHTVAFLGTSDGQLK
KVVLESSSSATQYETLLVDSGSPILPDMVFDPDGEHLYVMTPKKVTKVPVE
>gnl|CDD|200498 cd11237, Sema_1A, The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A). Sema1A is a transmembrane protein. It has been shown to mediate the defasciculation of motor axon bundles at specific choice points. Sema1A binds to its receptor plexin A (PlexA), which in turn triggers downstream signaling events involving the receptor tyrosine kinase Otk, the evolutionarily conserved flavoprotein monooxygenase molecule interacting with CasL (MICAL), and the A kinase anchoring protein Nervy, leading to repulsive growth-cone response. Sema1A has also been shown to be involved in synaptic formation. It is a member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
ETHSDHFKLLDQDGNSLLVGARNAVYNISLSDLTENQRIEWPSSDAHREMCLLKGKSEDDCQNYIRVLAK
KSAGRLLVCGTNAYKPLCREYTVKDGGYRVEREFDGQGLCPYDPKHNSTAVYADGQLYSATVADFSGADP
LIYREPLRTERYDLKQLNAPNFVSSFAYGDYVYFFFRETAVEYINCGKAIYSRVARVCKNDKGGPHPFRD
RWTSFLKARLNCSVPGEYPFYFNEIQSTSDIVEGGYGGKSAKLIYGVFTTPVNSISGSAVCAFSLQDILE
VFDGSFKEQQDINSNWLPVPSNKVPEPRPGQCVNDSRTLPDVTVNFIKSHPLMDEAVPSFFGRPILVRTS
LQYRFTQIAVDPQVKALDGKYYDVLFIGTDDGKVLKAVNIASADTVDKVSPVVIEETQVFPRGVPIRNLL
IVRGKDDGRLVVVSDDEIVSIPLHRC
>gnl|CDD|200499 cd11238, Sema_2A, The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A). Sema2A, a secreted semaphorin, signals through its receptor plexin B (PlexB) to regulate central and peripheral axon pathfinding. In the Drosophila embryo, Sema2A secreted by oenocytes interacts with PlexB to guide sensory axons. Sema2A is a member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
LYYRTLLLDEKRNALYVGAMDRVFRLNLYNINDTGNNCARDELTLSPSDVSECVSKGKDEEYECRNHVRV
IQPMGDGQTLYVCSTNAMNPKDRVLDANLLHLPEYVPGPGNGIGKCPYDPDDNSTAVWVEWGNPGDLPAL
YSGTRTEFTKANTVIYRPPLYNNTKGRHESFMRTLKYDSKWLDEPNFVGSFDIGDYVYFFFRETAVEYIN
CGKVVYSRVARVCKKDTGGKNVLRQNWTTFLKARLNCSISGEFPFYFNEIQSVYKVPGRDDTLFYATFTT
SENGFTGSAVCVFTLSDINAAFDTGKFKEQASSSSAWLPVLSSEVPEPRPGTCVNDSATLSDTVLHFART
HPLMDDAVSHGPPLLYLRDVVFTHLVVDKLRIDDQEYVVFYAGSNDGKVYKIVHWKDAGESKSNLLDVFE
LTPGEPIRAMELLPGEFLYVASDHRVSQIDLA
>gnl|CDD|200500 cd11239, Sema_3, The Sema domain, a protein interacting module, of class 3 semaphorins. Class 3 semaphorins (Sema3s) are secreted regulator molecules involved in the development of the nervous system, vasculogenesis, angiogenesis,and tumorigenesis. There are 7 distinct subfamilies named Sema3A to 3G. Sema3s function as repellent signals during axon guidance by repelling neurons away from the source of Sema3s. However, Sema3s that are secreted by tumor cells play an inhibitory role in tumor growth and angiogenesis (specifically Sema3B and Sema3F). Sema3s functions by forming complexes with neuropilins and A-type plexins, where neuropilins serve as the ligand binding moiety and the plexins function as signal transduction component. Sema3s primarily inhibit the cell motility and migration of tumor and endothelial cells by inducing collapse of the actin cytoskeleton via neuropilins and plexins. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
FLGSMNSLDYRSLLLDEDRDRLYVGGKDHILSLSLDNINQDPKKIYWPASPERIEECKMAGKDPNTECAN
FVRVLQPYNRTHLYACGTGAFHPICAFINVGRRLEDPIFKLDDSSLESGRGKCPFDPNQPFASVLIDGEL
YSGTAIDFMGRDAAIFRSLGHRHYIRTEQYDSRWLNEPKFVGAYLIPDSDNPDDDKVYFFFREKAVEAEG
SGKAIYSRVGRICKNDVGGQRSLVNKWSTFLKARLVCSVPGPDGIDTYFDELEDVFLLPTRDPKNPLIYG
VFTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPNYQWVEYQGKVPYPRPGTCPSKTYGPLYKSTKDF
PDDVISFARSHPLMYNPVYPLHGRPLLIRTNVPYRLTQIAVDRVEAEDGQYDVLFIGTDSGTVLKVVSLP
KENWEMEEVILEELQVFKHPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC
>gnl|CDD|200501 cd11240, Sema_4, The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4). Class 4 semaphorins (Sema4s) are transmembrane regulator molecules involved in the development of the nervous system, immune response, cytoskeletal organization, angiogenesis, and cell-cell interactions. There are 7 distinct subfamilies in class 4 semaphorins, named 4A to 4G. Several class 4 subfamilies play important roles in the immune system and are called "immune semaphorins". Sema4A plays critical roles in T cell-DC interactions in the immune response. Sema4D/CD100, expressed by lymphocytes, promotes the aggregation and survival of B lymphocytes and inhibits cytokine-induced migration of immune cells in vitro. It is required for normal activation of B and T lymphocytes. Sema4B negatively regulates basophil functions through T cell-basophil contacts and significantly inhibits IL-4 and IL-6 production from basophils in response to various stimuli, including IL-3 and papain. Sema4s not only influence the activation state of cells but also modulate their migration and survival. The effects of Sema4s on nonlymphoid cells are mediated by plexin D1 and plexin Bs. The Sema4G and Sema4C genes are expressed in the developing cerebellar cortex and are involved in neural tube closure and development of cerebellar granules cells through receptor plexin B2. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
FSQEGIQNYSTLLLSEDEGTLYVGAREALFALNVSDISTELKDKIKWEASEDKKKECANKGKDNQTDCFN
FIRILQFYNSTHLYVCGTFAFSPRCTYINLSDFSLSSIKFEDGKGRCPFDPAQRYTAIMVDGELYSATVN
NFLGSEPVISRNHSEGNVLKTENTLRWLNEPAFVGSAHIRESIDSPDGDDDKIYFFFTETAVEYDFYEKV
TVSRVARVCKGDLGGQRTLQKKWTTFLKAQLVCSQPDSGLPFNVLRDVFVLSPDSWDATIFYGVFTSQWN
VSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSRYTGPVPDPRPGACITNSARSQGITSSLNLPDNVLT
FVKDHPLMDEQVHPINRPLLVKSGVNYTRIAVHRVQALDGQTYTVLFLGTEDGFLHKAVSLDGGMHIIEE
IQLFDQPQPVKNLLLSSSKGVLYVGSSSGVVQVPLS
>gnl|CDD|200502 cd11241, Sema_5, The Sema domain, a protein interacting module, of semaphorin 5 (Sema5). Class 5 semaphorins are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. There are three subfamilies in class 5 semaphorins, namely 5A, 5B and 5C. Sema5A and Sema5B function as guidance cues for optic and corticofugal nerve development, respectively. Sema5A-induced cell migration requires Met signaling. Sema5C is an early development gene and may play a role in odor-guided behavior. Sema5A is also implicated in cancer. In a screening model for metastasis, the Drosophila Sema5A ortholog, Dsema-5C, has been found to be required in tumorigenicity and metastasis. Sema5A is highly expressed in human pancreatic cancer cells and is associated with tumor growth, invasion and metastasis. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
FEIEYVSDFSRLVLDPTHDQLIVGARNYLFRLRLQSLSLLQAVPWNSDEDTKRQCQSKGKSVEECQNYVR
VLLVVGKNLFTCGTYAFSPVCTIRKLSNLTQILDTISGVARCPYSPAHNSTALISASGELYAGTVYDFSG
RDPAIYRSLGGKPPLRTAQYNSKWLNEPNFVGSYEIGNHTYFFFRENAVEHQDCGKTVYSRIARVCKNDI
GGRFLLEDTWTTFMKARLNCSLPGEFPFYYNEIQGTFYLPETDLIYAVFTTNVNGIAGSAICAFNLSAIN
QAFNGPFKYQENNGSAWLPTPNPHPNFQCTTSIDRGQPANTTERDLQDAQKYQLMAEVVQPVTKIPLVTM
DDVRFSKLAVDVVQGRGTQLVHIFYVGTDYGTILKMYQPHRSQKSCTLEEIKILPAMKGEPITSLQFLKS
EKSLFVGLETGVLRIPLN
>gnl|CDD|200503 cd11242, Sema_6, The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6). Class 6 semaphorins (Sema6s) are membrane associated semaphorins. There are 6 subfamilies named 6A to 6D. Sema6s bind to plexin As in a neuropilin independent fashion. Sema6-plexin A signaling plays important roles in lamina-specific axon projections. Interactions between plexin A2, plexin A4, and Sema6A control lamina-restricted projection of hippocampal mossy fibers. Interactions between Sema6C, Sema6D and plexin A1 shape the stereotypic trajectories of sensory axons in the spinal cord. In addition to axon targeting, Sema6D-plexin A1 interactions influence a wide range of other biological processes. During cardiac development, Sema6D attracts or repels endothelial cells in the cardiac tube depending on the expression patterns of specific coreceptors in addition to plexin A1. Furthermore, Sema6D binds a receptor complex comprising of plexin A1, Trem2 (triggering receptor expressed on myeloid cells 2), and DAP12 on dendritic cells and osteoclasts to mediate T-cell-DC interactions and to control bone development, respectively. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
DNTTARHRLDFQRMLRINRTLYIAARDHVYTVDLDASHTEEIVPSKKLTWRSRQADVENCRMKGKHKDEC
HNFIKVLVPRNDETLFVCGTNAFNPVCRNYRIDTLEQDGEEISGMARCPFDAKQANVALFADGKLYSATV
TDFLASDAVIYRSLGDSPTLRTVKYDSKWLKEPHFVHAVEYGDYVYFFFREIAVEYNTLGKVVFSRVARV
CKNDMGGSPRVLEKQWTSFLKARLNCSVPGDSHFYFDVLQAVTDVIRINGRPVVLGVFTTQYNSIPGSAV
CAFDMDDIEKVFEGRFKEQKSPDSAWTPVPEDRVPKPRPGCCAGSGSAEKYKTSNDFPDDTLNFIKTHPL
MDEAVPSIINRPWFTRTMVRYRLTQIAVDNAAGPYQNYTVVFLGSEAGTVLKFLARIGPSGSNGSVFLEE
IDVYNPAKCSYDGEEDRRIIGLELDRASHALFVAFSGCVIRVPLS
>gnl|CDD|200504 cd11243, Sema_7A, The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108). Sema7A plays regulatory roles in both immune and nervous systems. Unlike other semaphorins, which act as repulsive guidance cues, Sema7A enhances central and peripheral axon growth and is required for proper axon tract formation during embryonic development. Sema7A also plays a critical role in the negative regulation of T cell activation and function. Sema7A is a membrane-anchored member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
KESYPVFFHEAGSSSVYVGGQGALYLLDFTGSAVIVKKIPDEKTEKDCKKRATLDDCENYITLIKKLDYR
LLVCGTNAGSPKCWFLVNQTLVTLSADRGVAPFLPDENSLVLIEGNNVYSTISGKKGNIPRFRRYGGKKE
LYTSDTVMQKPQFVKATLLPEDEQYQDKIYYFFREDNEDKGPEAEPNISRVARLCKEDQGGTSSLSTSKW
STFLKARLVCGDPATPMNFNRLQDVFLLPKEEWREAVVYGVFSNTWGSSAVCSYSLGDIDKVFRTSSLKG
YSGSLPNPRPGTCVPPEQTHPSETFSFADEHPELDDRIEPDEPRKLPVFQNKDHYQKVVVDEVRASDGVS
YDVLYLATDKGKIHKVVESKGQTHNIMEIQPFKEQEPIQSMILDAERSHLYVGTKAEVTRLPLD
>gnl|CDD|200505 cd11244, Sema_plexin_A, The Sema domain, a protein interacting module, of Plexin A. Plexins serve as receptors of semaphorins and may be the ancestor of semaphorins. Members of the Plexin A subfamily are receptors for Sema1s, Sema3s, and Sema6s, and they mediate diverse biological functions including axon guidance, cardiovascular development, and immune function. Guanylyl cyclase Gyc76C and Off-track kinase (OTK), a putative receptor tyrosine kinase, modulate Sema1a-Plexin A mediated axon repulsion. Sema3s do not interact directly with plexin A receptors, but instead bind Neuropilin-1 or Neuropilin-2 toactivate neuropilin-plexin A holoreceptor complexes. In contrast to Sema3s, Sema6s do not require neuropilins for plexin A binding. In the complex, plexin As serve as signal-transducing subunits. An increasing number of molecules that interact with the intracellular region of Plexin A have been identified; among them are IgCAMs (in axon guidance events) and Trem2-DAP12 (in immune responses). The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module
FVTFRGEPRDWSFNHLTVHRRTGEVYVGAINRVYKLSSNLTVLVTHETGPVEDNPKCYPPPIVQTCNEPL
TTTNNVNKLLLIDYSENRLIACGSLYQGVCKLLRLEDLFKLGEPHHKKEHYLSGVNESGTMFGVIVSYSN
GDDKLFIGTAVDGKSEYFPTLSSRKLTADEESDGMFAYVYHDEFVSSQIKIPSDTLSIIPDFDIYYVYGF
SSGNFVYFLTLQPETQLTPGDSTGEQFYTSKIVRLCKDDTKFYSYVEFPIGCTRDGVEYRLLQAAYLSKP
GKALAQALGISEDEDVLFTIFSKGQKNRMKPPDESALCLFTLKQINLRIKERLQSCYRGEGKLSLPWLLN
KDLPCINAPLQIDDNFCGLDMNQPLGGSDMVEGIPLFTDDRDRMTSVAAYVYKGHSVVFVGTKSGKLKKI
RVDGPPHNALQYETVQVVEGSPILRDMAFSPDHQYLYIMSERQVTRVPVE
>gnl|CDD|200506 cd11245, Sema_plexin_B, The Sema domain, a protein interacting module, of Plexin B. Plexins, which contain semaphorin domains, function as receptors of semaphorins and may be the ancestors of semaphorins. There are three members of the Plexin B subfamily, namely B1, B2 and B3. Plexins B1, B2 and B3 are receptors for Sema4D, Sema4C and Sema4G, and Sema5A, respectively. The activation of plexin B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. By signaling the effect of Sema4C and Sema4G, the plexin B2 receptor is critically involved in neural tube closure and cerebellar granule cell development. Plexin B3, the receptor of Sema5A, is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin B3 has been linked to verbal performance and white matter volume in human brain. Small GTPases play important roles in plexin B signaling. Plexin B1 activates Rho through Rho-specific guanine nucleotide exchange factors, leading to neurite retraction. Plexin B1 possesses an intrinsic GTPase-activating protein activity for R-Ras and induces growth cone collapse through R-Ras inactivation. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module
IINHLAQDPQTGRLYLGAVNGLFQLSPNLQLESRADTGPKKDSPQCLPPITAAECPQAKETDNFNKLLLV
NSANGTLVVCGSLFQGVCELRNLNSVNKPLYRPETPGDKQYVAANEPSVSTVGLISYFKDGLSLLFVGRG
YTSSLSGGIPPITTRLLQEHGEMDAFSNEVEAKLVVGSASRYHHDFVYAFADNGYIYFLFSRRPGTADST
KRTYISRLCENDHHYYSYVELPLNCTVNQENTYNLVQAAYLAKPGKVLNGKVLFGVFSADEASTAAPDGR
SALCMYPLSSVDARFERTRESCYTGEGLEDDKPETAYIEYNVKSICKTLPDKNVKAYPCGAEHTPSPLAS
RYPLAAKPILTRNDMLTAVAVAVENGHTIAFLGDSGGQLHKVYLDPNHTDFYSTIPGDQDSAVNKDLLFD
STLNHLYVMTGKKISKVPVQ
>gnl|CDD|200507 cd11246, Sema_plexin_C1, The Sema domain, a protein interacting module, of Plexin C1. Plexins serve as semaphorin receptors. Plexin C1 has been identified as the receptor of semaphorin 7A, which plays regulation roles in both the immune and nervous systems. Unlike other semaphorins which act as repulsive guidance cues, Sema7A enhances central and peripheral axon growth and is required for proper axon tract formation during embryonic development. Plexin C1 is a potential tumor suppressor for melanoma progression. The expression of Plexin C1 is diminished or absent in human melanoma cell lines. Cofilin, an actin-binding protein involved in cell migration, is a downstream target of Sema7A-Plexin C1 signaling. Cofilin is not phosphorylated when Plexin C1 expression is silenced. Thus, melanoma invasion and metastasis may be promoted through the loss of Plexin C1 inhibitory signaling on cofilin activation. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module
SAIGAIAASLADSSFVASGSCLDQLDYSLELALARLYRDQAGNCTEPVSLAPPARPRPGSQFSRLLLPYL
REGAGGLSGLLLTGWTFPGDRGACEVRPLGNLPGASQRNGTEVVSCHPQGSTAGVVYRANRSGGWYLAVA
ATYVLPEDETASRCNPSASDLDTAIALKATEGRSLATQELGRLKLLGSLHFVDAFLWNGSLYFPYYPYNY
TSGAATGEPSMARVAHSLEVLFQGQAGLDCLHGHPRGRRLLLSSSLVRALDVGAGVFSAGEGQERRAPCT
TALCLFRMEEIQARANGESGDFPERVQVPIAPSNNLTTLIHSDLVSVYGTVVLNRTVLFLGTGDGQLLKV
ILGENMTSNCPEVLYEIKEETPVFYKLVPDPVNNIYIYLTSGNKVRRIPVA
>gnl|CDD|200508 cd11247, Sema_plexin_D1, The Sema domain, a protein interacting module, of Plexin D1. Plexins are known as semaphorin receptors and Plexin D1 has been identified as the receptor of Sema3E. It binds to Sema3E directly with high affinity. Sema3E is implicated in axonal path finding and inhibition of developmental and post-ischemic angiogenesis. Plexin D1 is broadly expressed on tumor vessels and tumor cells in a number of different types of human tumors. Plexin D1-Sema3E interaction inhibits tumor growth but promotes invasiveness and metastasis. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module
VQRKFRSPTRTNNFALDGGRGRLYLAAVNRLYQLSGLVLALEAEAAVGPVLDSPLCHAPQLPQATCEHPR
TLTDNYNKILQPDPEQGVLVVCGSIYQGLCQLRRLYNISAVAVRFPVDGDTVFPSMLNVAANHPNASTVG
LVLWPRGGGGGLRLLVGATYTGYGSGFFPRNRSLEDHRFENTPEIAIRALNTRGDLAKLFTFDINPSDDN
IFKIKQGAKARHKLSFVRAFLQHFLQPYAYLAMNGEANAAGKESQPPSLLARICLPGRAPPPPGEAKKLT
ESYIQLGLRCEGAYTRLVSVFPARVEEEQLFAVFERAGGAPAALCAFRFAEVEEPIRAARTACFVSPAAG
VVTVLDSVVQGTGPACERKLNIQLQPEQLDCGAAHLQHPLAILQPLKATPVFRAPGLTSVAVASVNNYTV
VFLGTVSGRLLKINLDESMQVVSRRSVTVAYGEPVHHVMQFDPSDSTYLYLMTSHQMTRVKVA
>gnl|CDD|200509 cd11248, Sema_MET_like, The Sema domain, a protein interacting module, of MET and RON receptor tyrosine kinases. This family includes MET and RON receptor tyrosine kinases. MET is encoded by the c-met protooncogene. MET is the receptor for hepatocyte growth factor/scatter factor (HGF/SF). HGF/SF and MET regulates multiple cellular events and are essential for the development of several tissues and organs, including the placenta, liver, and several groups of skeletal muscles. RON receptor tyrosine kinase is a Macrophage-stimulating protein (MSP) receptor. Upon binding of MSP, RON is activated via autophosphorylation within its kinase catalytic domain, resulting in a variety of effects including proliferation, tubular morphogenesis, angiogenesis, cellular motility and invasiveness. By interacting with downstream signaling molecules, it regulates macrophage migration, phagocytosis, and nitric oxide production. MET and RON receptors have been implicated in cancer development and migration. They are composed of alpha-beta heterodimers. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a Sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic tyrosine kinase domain. The Sema domain is necessary for receptor dimerization and activation
LPFFTADTPIQNIVLNEGSTEVYVAAQNVIYALNPDLQKVWEYKTGPVGSPDCQTCQDCSSGADPGVPKD
TDNMVLVLETYYDDYLYSCGSTQNGVCYRHVLEDGADIQSEVHCLFSKKNNSPSYCPDCVASPLGTKVTN
VESGRTIYFFVANSVNSSLAGSFPPHSISVRRLKEDGFGFLSDQSYLDVLPSLRDSYPIKYVYSFHSGPF
VYFLTVQRESLTKPSSAFHTRLVRLCSSDSEIWRYREMPLECIFTPKRRRRSTEEDVVYNVLQAAHVSKV
GADLADELGASEGDDILFGVFARSKPDSGEPMPNSALCAFPIKYVNDAIEKGVEKCCTSGLEHFSGSLCH
FQPCPTCPGESSSCEATCKEYRTEVTKPYQRVDLFNGQMSNVLLTSILVTTIGNHTVAHLGTSDGRVLQV
VLSRSGPIPHVNFSLDSQPVSREVAVLSSNGSLLFVTGDKITKVPLI
>gnl|CDD|200510 cd11249, Sema_3A, The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A). Sema3A has been reported to inhibit the growth of certain experimental tumors and to regulate endothelial cell migration and apoptosis in vitro, as well as arteriogenesis in the muscle, skin vessel permeability, and tumor angiogenesis in vivo. The function of Sema3A is mediated through receptors neuropilin-1 (NP1) and plexins, although little is known about the requirement of specific plexins in its receptor complex. It is known however that Plexin-A4 is the receptor for Sema3A in the Toll-like receptor- and sepsis-induced cytokine storm during immune response. Sema3A is a member of the Class 3 semaphorin family of secreted proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
KNNVPRLKLSYKEMLESNNLITFNGLANSSSYHTFLLDEERGRLYVGAKDHIFSFNLVNIKDFQKIVWPV
SPSRRDECKWAGKDILKECANFIKVLKAYNQTHLYACGTGAFHPVCTYIEVGHHPEDNIFRLEDSHFENG
RGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPES
DNPEDDKIYFFFRENAIDGEHTGKATHARIGQLCKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHF
DELQDVFLMNSKDPKNPIVYAVFTTSSNIFKGSAVCMYSMTDIRRVFLGPYAHRDGPNYQWVPFQGRVPY
PRPGTCPSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIIIKTDVDYQFTQIVVDRVEAEDGQ
YDVMFIGTDMGTVLKVVSIPKETWHDLEEVLLEEMTVFREPTAISAMELSTKQQQLYIGSAIGVSQLPLH
RCD
>gnl|CDD|200511 cd11250, Sema_3B, The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B). Sema3B is coexpressed with semaphorin 3F and both proteins are candidate tumor suppressors. Both Sema3B and Sema3F show high levels of expression in normal tissues and low-grade tumors but are down-regulated in highly metastatic tumors in the lung, melanoma cells, bladder carcinoma cells and prostate carcinoma. They are upregulated by estrogen and inhibit cell motility and invasiveness through decreased FAK phosphorylation and inhibition of MMP-2 and MMP-9 expression. Two receptor families, the neuropilins (NP) and plexins, have been implicated in mediating the actions of semaphorins 3B and 3F. Sema3B is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
TFDLERSCCYDALLLDEERGRLFVGAKNYLASLSLDNISKQEKKIYWPAPVEWREECNWAGKDINTDCMN
YVKILHHYNRTHLYACGTGAFHPTCAFVEVGQRMEDHVFRLDPSRVEDGKGKSPYDPRHTAASVLVGDEL
YSGVATDLMGRDFTIFRSLGQRPSLRTEQHDSRWLNEPKFVKVFWIPESENPDDDKIYFFFRETAVEAAG
LGKQSYSRIGQICRNDMGGQRSLVNKWTTFLKARLVCSVPGNEGGDTHFDELRDVFLLQTRDKRNPLIYA
VFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSYQGKVPYPRPGMCPSKTFGSFESTKDFP
DDVIQFARNHPLMFNPVLPLGGRPLFLRTGIPYTFTQIAVDRVAAADGHYDVMFIGTDVGSVLKVISVPK
GSWPSNEELLLEELHVFKDSSPITSMQISSKRQQLYVGSRSGVSQLPLHRC
>gnl|CDD|200512 cd11251, Sema_3C, The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C). Sema3C is a secreted semaphorin expressed in and adjacent to cardiac neural crest cells, and causes impaired migration of neural crest cells to the developing cardiac outflow tract, resulting in the interruption of the aortic arch and persistent truncus arteriosus. It has been proposed that Sema3C acts as a guidance molecule, regulating migration of neural crest cells that express semaphorin receptors such as plexin A2. Sema3C may also participate in tumor progression. The cleavage of Sema3C induced by ADAMTS1 promotes the migration of breast cancer cells. Sema3C is a member of the class 3 semaphorin family of secreted proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
YSLSERPLDYRILFMDEDQDRIYVGSKDHILSLNINNISQDALSIFWPASASKVEECKMAGKDPTHGCGN
FVRVIQPYNRTHLYVCGSGAFSPVCVYVNRGRRSEEQVFHIDSKAESGKGRCSFNPNVNTVSVMINEELF
SGMYIDFMGTDAAIFRSLTKRNAVRTDQHNSKWLSEPIFVDAHLIPDGTDPNDAKLYFFLKERLTDNSGS
TKQIHSMIARVCPNDTGGQRSLVNKWTTFLKARLVCSVMDEDGTETHFDELEDVFLLETDNPRTTLVYGI
FTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLIAYQGRIPYPRPGTCPGGAFTPNMQSTKEFP
DDVVTFIRNHPLMFNPIYPIGRRPLLVRTGTDYKYTKIAVDRVNAADGRYHVLFLGTDKGTVQKVVVLPT
NGSLSGELILEELEVFKNHAPITNMKISSKKQQLYVSSEEGISQVSLHRC
>gnl|CDD|200513 cd11252, Sema_3D, The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D). Sema3D is a secreted semaphorin expressed during the development of the nervous system. In zebrafish, Sema3D is expressed in the ventral tectum. It guides retinal axons along the dorsoventral axis of the tectum and guides the laterality of retinal ganglion cell (RGC) projections. Both Sema3D knockdown or its ubiquitous overexpression induced aberrant ipsilateral projections. Proper balance of Sema3D is needed at the midline for the progression of RGC axons from the chiasm midline into the contralateral optic tract. Sema3D is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
FLGSSEGLDFQTLLLDEERGRLLLGAKDHIYLLDLVDLNKNPKKIYWPAAKERVELCKLAGKDANTECAN
FIRVLHPYNRTHVYVCGTGAFHPTCGYIELGTHKEDRIFLLDTQNLESGRLKCPFDPQQPFASVMTDEYL
YAGTASDFLGKDTTFTRSLGPTPDHHYIRTDISEHYWLNGAKFIGTFPIPDTYNPDDDKIYFFFREASQD
GSTSDKSVLSRVGRVCKNDVGGQRSLINKWTTFLKARLVCSIPGPDGADTHFDELQDIFLLPTRDERNPV
VYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPDHRWVQYEGRIPYPRPGTCPSKTYDPLIKST
KDFPDEVISFIKRHPLMYKSVYPLTGGPVFTRINVDYRLTQIVVDHVAAEDGQYDVMFLGTDIGTVLKVV
SITKEKWTMEEVVLEELQIFKHPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC
>gnl|CDD|200514 cd11253, Sema_3E, The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E). Sema3E is a secreted molecule implicated in axonal path finding and inhibition of developmental and postischemic angiogenesis. It is also highly expressed in metastatic cancer cells. Sema3E signaling, through its high affinity functional receptor Plexin D1, drives cancer cell invasiveness and metastatic spreading. Sema3E is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
FHSPFGFLDLHTMLLDEYQERLFVGGRDLLYSLSLERISANYKEIHWPSTQLQVEDCIMKGRDKPECANY
IRVLHHYNRTHLLACGTGAFDPVCAFIRVGRGSEDHLFQLESDKFERGRGRCPFDPNSSFISTLIGGELF
VGLYSDYWGRDAAIFRTMNHLAHIRTEHDDERLLKEPKFVGSYMIPDNEDPDDNKVYFFFTEKALEAEGG
NHAIYTRVGRVCANDQGGQRMLVNKWSTFLKTRLICSVPGPNGIDTHFDELEDVFLLRTRDNKNPEIFGL
FSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYHWSVYEGKVPYPRPGSCASKVNGGHYGTTKDYP
DEALRFARSHPLMYQAVKPVHKRPILVKTDGKYNLKQIAVDRVEAEDGQYDVLFIGTDNGIVLKVITIYN
QETETMEEVILEELQVFKVPVPIISMEISSKRQQLYIGSESGVAQIRFHQC
>gnl|CDD|200515 cd11254, Sema_3F, The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F). Sema3F is coexpressed with semaphorin3B. Both Sema3B and Sema3F proteins are candidate tumor suppressors that are down-regulated in highly metastatic tumors. Two receptor families, the neuropilins and plexins, have been implicated in mediating the actions of semaphorins 3B and 3F. Sema3F is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
FSFLLNTSDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWPASPQRIEECILSGKGSNGECGN
FIRLIQPWNRTHLYVCGTGAYNPVCAYINRGRRAEDYMFRLEPDKLESGKGKCPYDPKQDSVSALINGEL
YAGVYIDFMGTDAAIFRTMGKQPAMRTDQYNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREKSLEAPQ
SPAVLSRIGRVCLNDDGGHCCLVNKWSTFLKARLVCSVPGADGIETHFDELRDVFIQPTQDTKNPVIYAV
FSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPYTGKIPYPRPGTCPGGTFTPSMKSTKDYP
DEVINFMRTHPLMYNAVYPVHRRPLVVRTNVNYRFTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPK
DDLETEELTLEEVEVFKVPAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC
>gnl|CDD|200516 cd11255, Sema_3G, The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G). Semaphorin 3G is identified as a primarily endothelial cell- expressed class 3 semaphorin that controls endothelial and smooth muscle cell functions in autocrine and paracrine manners, respectively. It is mainly expressed in the lung and kidney, and a little in the brain. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
FLGLHGDLHLSAVYLDEYRDRLFLGGKDVLYSLRLDQTHPDAKEIHWPPLPGQREECIRKGKDPETECAN
FVRVLQPFNRTHLLACGTGAFQPVCALINVGHRGEHVFSLDPTTVESGRGRCPHEPKRPFASTFTGGELY
TGLTADFLGRDSVIFRGFGTRSPLRTETDQRLLHEPRFVAAHLIPDNADRDNDKVYFFFTERATETAEDD
DGAIHSRVGRLCANDAGGQRVLVNKWSTFIKARLVCSVPGPHGIQTHFDQLEDVFLLRTKDGKSPEIYAL
FSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWGPYEGKVPYPRPGVCPSKITAQPGRAFRSTK
DYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLPYRLTQIVVDRVEAEDGYYDVMFIGTDSGSVLKVIV
LQKGNSAAGEEVTLEELQVFKVPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC
>gnl|CDD|200517 cd11256, Sema_4A, The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A). Sema4A is expressed in immune cells and is thus termed an "immune semaphorin". It plays critical roles in T cell-DC interactions in the immune response. It has been reported to enhance activation and differentiation of T cells in vitro and generation of antigen-specific T cells in vivo. The function of Sema4A in the immune response implicates its role in infectious and noninfectious diseases. Sema4A exerts its function through three receptors, namely Plexin B, Plexin D1, and Tim-2. Sema4A belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. TThe Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
RFRQENVHNYDQLLLSPDETTLYVGARDNILALGIRTPGPIRLKHQIPWPANDSKISECAFKKKSNETEC
FNFIRVLVPVNGTHLYTCGTYAFSPACTYIELDHFSLPPPNGTIITMDGKGQSPFDPQHNYTAILVDGEL
YTGTMNNFRGNEPIIFRNLGTKVSLKTDGFLRWLNADAVFVASFNPQGDSKVYFFFEETAREFDFFEKLT
VARVARVCKNDVGGEKLLQKKWTTFLKAQLTCSQQGHFPFNVIHHVALLNQPDPNNSVFYAVFTSQWQLG
GRRSSAVCAYKLNDIEKVFNGKYKELNKESSRWTRYMGPVSDPRPGSCSGGKSSDKALNFMKDHFLMDEV
VLPGAGRPLLVKSNVQYTRIAVDSVQGVSGHNYTVMFLGTDKGFLHKAVLMGGSESHIIEEIELLTPPEP
VENLLLAANEGVVYIGYSAGVWRVPLA
>gnl|CDD|200518 cd11257, Sema_4B, The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B). Sema4B, expressed in T and B cells, is an immune semaphorin. It functions as a negative regulatory of basophils through T cell-basophil contacts and it significantly inhibits IL-4 and IL-6 production from basophils in response to various stimuli, including IL-3 and papain. In addition, T cell-derived Sema4B suppresses basophil-mediated Th2 skewing and humoral memory responses. Sema4B may be also involved in lung cancer cell mobility by inducing the degradation of CLCP1 (CUB, LCCL-homology, coagulation factor V/VIII homology domains protein). Sema4B is characterized by a PDZ-binding motif at the carboxy-terminus, which mediates interaction with the post-synaptic density protein PSD-95/SAP90, which is thought to play a central role during synaptogenesis and in the structure and function of post-synaptic specializations of excitatory synapses. Sema4B belongs to class 4 transmembrane semaphorin family proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
RFEAEGVSNYTALLLSKDGNMLYVGARETLFALSSNDISPTGEQQELTWSADEEKKQECSFKGKDPQRDC
QNYIKILLRLNSTHLFTCGTYAFSPICTYIVMTNFSLERDEKGEPLLEDGKGRCPFDPEYKSTAIMVDGE
LYTGTVSNFQGNDPIIYRSLGSGTPLKTENSLNWLQDPAFVGSAYIQESLPKLVGDDDKIYFFFSETGKE
FDFFENTIVSRIARVCKGDEGGERVLQKRWTTFLKAQLLCSLPDDGFPFNVLQDVFVLTPSPEDWKDTLF
YGVFTSQWHKGTAGSSAVCVFTMDQVQRAFNGLYKEVNRETQQWYTYTHPVPEPRPGACITNSARERKIN
SSLHMPDRVLNFVKDHFLMDGQVRSQPLLLQPQVRYTQIAVHRVKGLHKTYDVLFLGTDDGRLHKAVSVG
PMVHIIEELQIFSEGQPVQNLLLDTHKGLLYASSHSGVVQVPVA
>gnl|CDD|200519 cd11258, Sema_4C, The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C). Sema4C acts as a Plexin B2 ligand to regulate the development of cerebellar granule cells and to modulate ureteric branching in the developing kidney. The binding of Sema4C to Plexin B2 results the phosphorylation of downstream regulator ErbB-2 and the plexin protein itself. The cytoplasmic region of Sema4C binds a neurite-outgrowth-related protein SFAP75, suggesting that Sema4C may also play a role in neural function. Sema4C belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
VRRFSQVGVSNYTTLTLAEHRGLLYVGAREAIFALSLSNIELQPPISWEAPAEKKTECAQKGKSNQTECF
NYIRFLQPYNQSHLYTCGTYAFQPKCAYINMLTFTLDRAEFEDGKGKCPYDPAKGHTGLIVDGELYSATL
NNFLGTEPVILRNLGQHYSMKTEYLAFWLNEPHFVGSAFVPESVGSFTGDDDKIYFFFSERAVEYDCDSE
QVVARVARVCKGDLGGARTLQKKWTTFLKARLLCSIPEWQLYFNQLKAVFTLEGASWRNTTFFAVFQARW
GDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRYTDPVPSPRPGSCINNWHRDHGYTSSLELPDNTL
NFVKKHPLMEDRVKPRLGRPLLVPCNSNFTHVVWTRVLGLDGETYSVLFIGTLDGWLIKAVSLGSWVHMI
EELQVFDQEPPESLVVSQSSKKLLFAGSRSELLQLPWA
>gnl|CDD|200520 cd11259, Sema_4D, The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100). Sema4D/CD100 is expressed in immune cells and plays critical roles in immune response; it is thus termed an "immune semaphorin". It is expressed by lymphocytes and promotes the aggregation and survival of B lymphocytes and inhibits cytokine-induced migration of immune cells in vitro. Sema4D/CD100 knock-out mice demonstrate that Sema4D is required for normal activation of B and T lymphocytes. Sema4D increases B-cell and DC function using either Plexin B1 or CD72 as receptors. The function of Sema4D in immune response implicates its role in infectious and noninfectious diseases. Sema4D belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
TWEHKEVQLVHFHEPDVSNYSTLLLSEDKDVLYVGAREAVFALNALNISEKQHELYWKVSEDKRTKCAVK
GKSKQTECRNYIRVLQPLNDTFLYVCGTNAFQPTCDYLNLTSFRLLGKNEDGKGRCPFDPAQSYTSVMVD
GELYSGTSYNFLGSEPIISRNSSQSPLRTEYAIPWLNEPSFVFADVIRADPDSPDGEDDKIYFFFTEVSV
EYEFVGKLLIPRIARVCKGDQGGLRTLQKKWTSFLKARLICSIPDKNLVFNVVNDVFILKSPTLKEPVIY
GVFTPQLNNVGLSAVCAYNLSTVEEVFSKGKYMQSATVEQSHTKWVRYNGEVPKPRPGACINNEARAANY
TSSLNLPDKTLQFVKDHPLMDDSVTPIGNRPRLIKKDVNYTQIVVDRVQALDGTIYDVMFISTDRGALHK
AISLENEVHIIEETQLFPDFEPVQTLLLSSKKGRRFLYAGSNSGVVQSPLA
>gnl|CDD|200521 cd11260, Sema_4E, The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E). Sema4E is expressed in the epithelial cells that line the pharyngeal arches in zebrafish. It may act as a guidance molecule to restrict the branchiomotor axons to the mesenchymal cells. Gain-of-function and loss-of-function studies demonstrate that Sema4E is essential for the guidance of facial axons from the hindbrain into their pharyngeal arch targets and is sufficient for guidance of gill motor axons. Sema4E guides facial motor axons by a repulsive action. Sema4E belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
FKEQGIWNYSTMLLREDLGLLVLGAREAVFALDLNDISVKRAKVLWEVTEEKQKDCTNKGKHADIDCHNY
IRILHKMNDSRMYVCGTNAFSPTCDYISYDDGQLTLEGKQEDGKGKCPFDPFQRYSSVMVDQDLYSATSM
NFLGSEPVIMRSSPITIRTEFKSSWLNEPNFIYMAAVPESEDSPEGDDDKIYLFFSETAVEYDFYNKLVV
SRVARVCKGDLGGQRTLQKKWTSFLKARLDCSVPEPSLPYVIQDVFHVCHQDWRKCVFYAVFTSQSDSSQ
SSAVCAYNVTDISNVFSRGKFKTPVAVETSFVKWVMYSGELPVPRPGACINNAARTSGIKKSLNLPDKTL
QFVKDKPLMDQAVHPITGKPLLVKRGALFTRIVVDMVTAADGQSYPVMFIGTANGYVLKAVNYDGEMHII
EEVQLFEPEEPIDILRLSQNQLYAGSASGVVQMPVS
>gnl|CDD|200522 cd11261, Sema_4F, The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F). Sema4F plays role in heterotypic cell-cell contacts and controls cell proliferation and suppresses tumorigenesis. In neurofibromatosis type 1 (NF1) patients, reduced Sema4F level disrupts Schwann cell/axonal interactions. Experiments using a yeast two-hybrid system show that the extreme C-terminus of Sema4F interacts with the PDZ domains of post-synaptic density protein SAP90/PSD-95, indicating possible functional involvement of Semas4F at glutamatergic synapses. Recent work also suggests a role for Sema4F in the injury response of intramedullary axotomized motoneuron. Sema4F belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulator molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
SALTRFSAPHTYNYSVLLVDPASHTLYVGARDAIFALTLPFSGERPRRIDWMVPEAHRQNCRKKGKKEAE
CHNFIRILAIANASHLLTCGTFAFDPKCGVIDVSSFQQVERLESGRGKCPFEPAQRSAAIMAGGVLYAAT
VKNFLGTEPIISRAVGRAEEWIRTETLPSWLNAPAFVAAVFLSPAEWGDEDGDDEIYFFFTETAREYDSY
ERIKVPRVARVCAGDLGGRKTLQQRWTTFLKADLLCPGPEHGRASSILQDVTTLRPLPGAGTPIFYGIFS
SQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCNRGLPVMDSDVPQPRPGECITNNMKLLGFGSSLSLP
DRVLTFVRDHPLMDRPVFPADGHPLLVTTDTAYLRVAAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQ
LSVLEDLALFPEPQPVENLQLHHNWLLVGSDTEVTQINTS
>gnl|CDD|200523 cd11262, Sema_4G, The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G). The Sema4G and Sema4C genes are expressed in the developing cerebellar cortex. Sema4G and Sema4C proteins specifically bind to Plexin B2 expressed in the cerebellar granule cells. Sema4G and Sema4C are involved in neural tube closure and cerebellar granule cell development through Plexin B2.Sema4G belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
RRFRGPAQNYSTLLLEDESGRLYVGARGAIFSLNASDISDSSALTIDWEASPEQKHQCLKKGKNNQTECF
NHVRFLQRFNSTHLYTCGTHAFRPLCAYIDAERFTLSSQFEEGKEKCPYDPAKGYTGLIVDGQLYTASQY
EFRSFPDIRRNSPQPTLRTEEAPTRWLNDADFVGSVLVRESMNSSVGDDDKIYFFFTERSQEETAYFSQS
RVARVARVCKGDRGGKKTLQRKWTSFLKARLVCYIPEYEFLFNVLRSVFVLWGSTPQDTVFYGIFGLEWK
NVKASAICRYSLSDIQTAFEGPYMEYQDSSSKWSRYTGKVPEPRPGSCITDEHRSQGINSSQDLPDNVLD
FVRRHPLMAEQVLPVEGRPLLFKRNVIYTKIAVQTVRGLDGRVYDVLFLGTDEGWLHKAVVIGSAVHIIE
ELQVFREPQPVENLVISKKQNSLYVGARSGVVQVPLS
>gnl|CDD|200524 cd11263, Sema_5A, The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A). Originally, mouse Sema5A was identified as a protein that induces inhibitory responses during optic nerve development. Recent studies show that Sema5A controls innate immunity in mice. It also has been identified as a candidate gene for causing idiopathic autism in humans. Plexin B3 functions as a binding partner and receptor for Sema5A. Furthermore, Sema5A is also implicated in cancer. The role of the Drosophila Sema5A ortholog, Dsema-5C, in tumorigenicity and metastasis has been reported. Sema5A is highly expressed in human pancreatic cancer cells and is associated with tumor growth, invasion and metastasis. Sema5A belongs to class 5 semaphorin family of proteins, which are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
FRAENAVDFSQLTFDPGQKELIVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIR
VLLVGGDRLFTCGTNAFTPICTNRTLNNLTEIHDQISGMARCPYSPQHNSTALLTSSGELYAATAMDFPG
RDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIG
GRFLLEDTWTTFMKARLNCSRPGEIPFYYNELQSTFFLPELDLIYGIFTTNVNSIAASAVCVFNLSAISQ
AFNGPFKYQENSRSAWLPYPNPNPNFQCGTMDQGLYVNLTERNLQDAQKFILMHEVVQPVTPVPYFMEDN
SRFSHVAVDVVQGKDMLFHIIYLATDYGTIKKVLAPLNQSSSSCLLEEIELFPKRQREPIRSLQILHSQS
VLFVGLQEHVIKIPLK
>gnl|CDD|200525 cd11264, Sema_5B, The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B). Sema5B is expressed in regions of the basal telencephalon in rat. Sema5B is an inhibitory cue for corticofugal axons and acts as a source of repulsion for the appropriate guidance of cortical axons away from structures such as the ventricular zone as they navigate toward and within subcortical regions. In addition to its role as a guidance cue, Sema5B regulates the development and maintenance of synapse size and number in hippocampal neurons. In addition, the sema domain of Sema5B can be cleaved of the whole protein and exerts its function in regulation of synapse morphology. Sema5B belongs to the class 5 semaphorin family of proteins, which are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKTEEECQNYVR
VLIVYGKKVFTCGTNAFSPVCTSRQVGNLSKVIERINGVARCPYDPRHNSTAVITSRGELYAATVIDFSG
RDPAIYRSLGSVPPLRTAQYNSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIG
GRFLLEDTWTTFMKARLNCSRPGEIPFYYNELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQ
AFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNENLTERSLQDAQRLFLMNDVVQPVTVDPLVTQD
SVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEMQILPPGQREPIRSLQILHSD
RSLFVGLNNGVLKIPLE
>gnl|CDD|200526 cd11265, Sema_5C, The Sema domain, a protein interacting module, of semaphorin 5C (sema5C). In Drosophila, Sema5C was identified as an early development gene, which is expressed in stage 2 embryos with a striped pattern emerging at later stages. Sema5c may play a role in odor-guided behavior and in tumorigenesis. Sema5C belongs to class 5 semaphorin family of proteins, which are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
FSDPEVTSYSQMLFDVARNQVIVGARDNLYRLSLDGLELLERASWPAAESKVALCQNKGQSEEDCHNYVK
VLLSYGKQLFACGTNAFSPRCSWREMENLTSVTEWDSGVAKCPYSPHANITALLSSSGQLFVGSPTDFSG
SDSAIYRTLGTSNKSFLRTKQYNSKWLNEPQFVGSFETGNFVYFLFRESAVEYMNCGKVIYSRIARVCKN
DVGGGTMLLKDNWTTFLKARLNCSLPGEYPFYFDEIQGMTYLPDEGILYATFTTPENSIAGSAVCAFNLS
SINAAFDGPFKHQESSGAAWERVNVNHRDHFNQCSSSSSSHLLESSRYQLMDEAVQPITLEPLHHAKLER
FSHIAVDVIPTKIHQSVHVLYVATTGGLIKKISVLPRTQETCLVEIWQPLPTPDSPIKTMQYLKVTDSLY
VGTELALMRIPAQ
>gnl|CDD|200527 cd11266, Sema_6A, The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A). In the cerebellum, Sema6A-plexin A2 signaling modulates granule cell migration by controlling centrosome positioning. Besides plexin A2, plexin A4 is also found to be a receptor of Sema6A. Interactions between plexin A2, plexin A4, and Sema6A control lamina-restricted projection of hippocampal mossy fibers. It is required for the clustering of boundary cap cells at the PNS/CNS interface and thus, prevents motoneurons from streaming out of the ventral spinal cord. At the dorsal root entry site, it organizes the segregation of dorsal roots. Sema6A may also be involved in axonal pathfinding processes in the periinfarct and homotopic contralateral cortex. Sema6A is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
RNTTQRHRLDIQMIMIMNRTLYIAARDHIYTVDIDTSHTEEIYFSKKLTWKSRQADVDTCRMKGKHKDEC
HNFIKVLLKRNDDTLFVCGTNAFNPSCRNYKMDTLEFFGDEFSGMARCPYDAKHANVALFADGKLYSATV
TDFLAIDAVIYRSLGDSPTLRTVKHDSKWLKEPYFVQAVDYGDYIYFFFREIAVEYNSMGKVVFPRVAQV
CKNDMGGSQRVLEKQWTSFLKARLNCSVPGDSHFYFNILQAVTDVIHINGRDVVLATFSTPYNSIPGSAV
CAYDMLDIASVFTGRFKEQKSPDSTWTPVPDERVPKPRPGCCAGSSSLEKYATSNEFPDDTLNFIKTHPL
MDEAVPSIINRPWFLRTMVRYRLTKIAVDNAAGPYQNHTVVFLGSEKGIILKFLARTGNSGFLNDSLFLE
EMNVYNSEKCSYDGVEDKRIMGMQLDKASSALYVAFSTCVIKVPLG
>gnl|CDD|200528 cd11267, Sema_6B, The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B). Sema6B functions as repellents for axon growth; this repulsive activity is mediated by its receptor Plexin A4. Sema6B is expressed in CA3, and repels mossy fibers in a Plexin A4 dependent manner. In human, it was shown that peroxisome proliferator-activated receptors (PPARs) and 9-cis-retinoic acid receptor (RXR) regulate human semaphorin 6B (Sema6B) gene expression. Sema6B is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
TAERGRDRLNIQRVLRVNRTLYIGDRDNLYRVELDPTAGTEMRYHKKLTWRSNKNDINVCRMKGKHEGEC
RNFIKVLLLRDYGTLFVCGTNAFNPVCANYSIDTLEPVGDNISGMARCPYDPKHANVALFADGMLFTATV
TDFLAIDAVIYRSLGDSPALRTVKHDSKWFKEPYFVHAVEWGSHVYFFFREIAMEFNYLEKVVVSRVARV
CKNDMGGSQRVLEKQWTSFLKARLNCSVPGDSHFYFNVLQAVSDILNLGGRPVVLAVFSTPTNSIPGSAV
CAFDMTQVAAVFEGRFREQKSPESIWTPVPEELVPRPRPGCCAAPGMRYNSSSTLPDEVLNFVKTHPLMD
EAVPSLGHAPWIVRTMTRYQLTHMVVDTEAGPHGNHTVVFLGSTRGTVLKFLIIPNASSSEISNQSVFLE
ELETYNPERCGWDSPQAQKLLSLELDKGSGGLLLAFPSCVVRVPVA
>gnl|CDD|200529 cd11268, Sema_6C, The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called semaphorin Y). Sema6C is highly expressed in adult brain and skeletal muscle and it shows growth cone collapsing activity. It may play a role in the maintenance and remodelling of neuronal connections. In adult skeletal muscle, this role includes prevention of motor neuron sprouting and uncontrolled motor neuron growth. The expression of Sema6C in adult skeletal muscle is down-regulated following denervation. Sema6C is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
DAVAAELGLDFQRFLTLNRTLLVAARDHVFSFDLQAEEEGEGLVPNKYLTWRSQDVENCAVRGKLTDECY
NYIRVLVPWDSQTLLACGTNSFSPVCRSYGITSLQQEGEELSGQARCPFDATQSNVAIFAEGSLYSATAA
DFQASDAVVYRSLGPQPPLRSAKYDSKWLREPHFVQALEHGDHVYFFFREVSVEDARLGRVQFSRVARVC
KRDMGGSPRALDRHWTSFLKLRLNCSVPGDSTFYFDVLQALTGPVNLHGRSALFGVFTTQTNSIPGSAVC
AFYLDEIERGFEGKFKEQRSLDGAWTPVSEDRVPSPRPGSCAGVGGAALFSSSRDLPDDVLTFIKAHPLL
DPAVPPVTHQPLLTLTSRALLTQVAVDGMAGPHSNITVMFLGSNDGTVLKVLPPGGRSGGPEPILLEEID
AYSPARCSGKRTAQTARRIIGLELDTEGHRLFVAFSGCIVYLPLS
>gnl|CDD|200530 cd11269, Sema_6D, The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D). Sema6D is expressed predominantly in the nervous system during embryogenesis and it uses Plexin-A1 as a receptor. It displays repellent activity for dorsal root ganglion axons. Sema6D also acts as a regulator of late phase primary immune responses. In addition, Sema6D is overexpressed in gastric carcinoma, indicating that it may have an important role in the occurrence and development of the cancer. Sema6D is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
SGNESQHRLDFQLMLKIRDTLYIAGRDQVYTVNLNEVPKTEVTPSRKLTWRSRQQDRENCAMKGKHKDEC
HNFIKVFVPRNDEMVFVCGTNAFNPMCRYYRLSTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATV
ADFLASDAVIYRSMGDGSALRTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARI
CKNDMGGSQRVLEKHWTSFLKARLNCSVPGDSFFYFDVLQSITDIIEINGIPTVVGVFTTQLNSIPGSAV
CAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPGCCAKHGLAEAYKTSIDFPDETLSFIKSHPL
MDSAVPSIIEEPWFTKTRVRYRLTAIAVDHAAGPHQNYTVIFVGSEAGVVLKILAKTSPFSLNDSVLLEE
IEAYNHAKCSAENEEDRRVISLQLDRDHHALFVAFSSCVVRIPLS
>gnl|CDD|200531 cd11270, Sema_6E, The Sema domain, a protein interacting module, semaphorin 6E (sema6E). Sema6E is expressed predominantly in the nervous system during embryogenesis. It binds Plexin A1 and might utilize it as a receptor to repel axons of specific types during development. Sema6E acts as a repellent to dorsal root ganglion axons as well as sympathetic axons. Sema6E is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module
DNDTARLGLDFQRMLRINHMVYIAARDHVFAINLSASLERIVPQQKLTWKTKDVEKCTVRGKNSDECYNY
IKVLVPRNDETLFACGTNAFNPTCRNYKMSSLEQDGEEVIGQARCPFESRQSNVGLFAGGDFYSATMTDF
LASDAVIYRSLGESSPVLRTVKYDSKWLREPHFLHAIEYGNYVYFFLSEIAVEYTTLGKVVFSRVARVCK
NDNGGSPRVLERYWTSFLKARLNCSVPGDSFFYFDVLQSLTNVMQINHRPAVLGVFTTQANSITGSAVCA
FYMDDIEKVFNGKFKEQRNSESAWTPVPDEAVPKPRPGSCAGDGPAAGYKSSTNFPDETLTFIKSYPLMD
EAVPSVNNRPCFTRTTSRFKLTQIAVDTAAGPYKNYTVVFLGSENGHVLKVLASMHPNSSYSTQVLEDID
VYNPNKCNVRGEDRRILGLELDKDHHALFVAFTGCVIRVPLS
>gnl|CDD|200532 cd11271, Sema_plexin_A1, The Sema domain, a protein interacting module, of Plexin A1. Plexin A1 is found in both the nervous and immune systems. Its external Sema domain is also shared by semaphorin proteins. In the nervous system, Plexin A1 mediates Sema3A axon guidance function by interacting with the Sema3A coreceptor neuropilin, resulting in actin depolarization and cell repulsion. In the immune system, Plexin A1 mediates Sema6D signaling by binding to the Sema6D-Trem2-DAP12 complex on immune cells and osteoclasts to promote Rac activation and DAP12 phosphorylation. In gene profiling experiments, Plexin A1 was identified as a CIITA (class II transactivator) regulated gene in primary dendritic cells (DCs). The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module
QPPFRTFTASDWSLTHLVVHNKTGEVYVGAVNRIYKLSNNLTLLRTHVTGPVEDNEKCYPPPSVQSCPHG
LGTTNNVNKLLLVDYAANRLIACGSASQGICQFLRLDDLFKLGEPHHRKEHYLSSVNESGTMSGVIIEVG
NGQNKLFVGTPIDGKSEYFPTLSSRKLMANEENAEMFGFVYQDEFVSSQLKIPSDTLSKFPTFDIYYVYS
FSSEQFVYYLTLQLDTQLTSPDSTGEQFFTSKIVRLCVDDPKFYSYVEFPIGCEQDGVEYRLIQDAYLSK
PGKALAKQLGISEREDILFTVFSQGQKNRVKPPKESVLCLFTLKKIKDKIKERIQSCYRGEGKLSLPWLL
NKELGCINSPLQIDDNFCGQDFNQPLGGTVTIEGTPLFVDKEDGMTSVAAYDYRGRTVVFAGTRSGRIKK
ILVDLSAPSSRPALQYENVVAHEGSPILRDLVLSPDRQYIYAMTEKQVTRVPVE
>gnl|CDD|200533 cd11272, Sema_plexin_A2, The Sema domain, a protein interacting module, of Plexin A2. Plexin A2 serves as a receptor for class 6 semaphorins. Interactions between Plexin A2, A4 and semaphorins 6A and 6B control the lamina-restricted projection of hippocampal mossy fibers. Sema6B also repels the growth of mossy fibers in a Plexin A4 dependent manner. Plexin A2 does not suppress Sema6B function. In addition, studies have shown that Plexin A2 may be related to anxiety and other psychiatric disorders. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module
FNTFHSENRDWTFNHLTVHQSTGAVYVGAINRVYKLSGNLTILVAHKTGPEEDNKSCYPPLIVQPCSEVL
TLTNNVNKLLIIDYSENRLLACGSLYQGVCKLLRLDDLFILVEPSHKKEHYLSSVNKTGTMYGVIVRSEG
EDGKLFIGTAVDGKQDYFPTLSSRKLPRDPESSAMLDYELHSDFVSSLIKIPSDTLALVSHFDIFYIYGF
ASGNFVYFLTVQPETPEGVSINSAGDLFYTSRIVRLCKDDPKFHSYVSLPFGCVRGGVEYRLLQAAYLSK
PGEVLARSLNITAQEDVLFAIFSKGQKQYHHPPDDSALCAFPIRAINAQIKERLQSCYQGEGNLELNWLL
GKDVQCTKAPVPIDDNFCGLDINQPLGGSTPVEGVTLYTSSRDRLTSVASYVYNGYSVVFVGTKSGKLKK
IRADGPPHGGVQYEMVSVFKDGSPILRDMAFSIDHKYLYVMSERQVSRVPVESCEQYTTCGECLSSGDPH
CGWCALHNMCSRRDKCQRAWEPFRF
>gnl|CDD|200534 cd11273, Sema_plexin_A3, The Sema domain, a protein interacting module, of Plexin A3. Plexin-A3 forms a receptor complex with neuropilin-2 and transduces signals for class 3 semaphorins in the nervous system. Both plexins A3 and A4 are essential for normal sympathetic neuron development. They function cooperatively to regulate the migration of sympathetic neurons, and differentially to guide sympathetic axons. Both plexins A3 and A4 are not required for guiding neural crest precursors prior to reaching the sympathetic anlagen. Plexin A3 is a major driving force for intraspinal motor growth cone guidance. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module
RPFRAFVVTDTTLTHLAVHRVTGEVFVGAVNRVYKLSANLTELRAHVTGPVEDNARCYPPPSVRVCAHRL
APVDNVNKLLLVDYAGNRLVACGSIWQGVCQFLRLEDLFKLGEPHHRKEHYLSGAQEPDSMAGVIVEQGK
GPSKLFVGTAIDGKSEYFPTLSSRKLISDEDSADMFSLVYQDEFVSSQIKIPSDTLSLYPAFDIYYVYGF
VSASFVYFLTLQLDTQQTLLDTAGEKFFTSKIVRMCANDTEFYSYVEFPLGCSKDGVEYRLVQAAHLAKP
GLLLAQALGVPEDEDVLFTIFSQGQKNRASPPRETILCLFTLSNINAHIRERIQSCYRGEGTLSLPWLLN
KELPCINTPMQINGNFCGLVLNQPLGGLHVIEGLPLLADSTDGMASVAAYTYRQHSVVFIGTRSGSLKKV
RVDGFQDAHLYETVPVVDGSPILRDMVFSPDHRYIYLLSEKQVSQLPVE
>gnl|CDD|200535 cd11274, Sema_plexin_A4, The Sema domain, a protein interacting module, of Plexin A4. Plexin A4 forms a receptor complex with neuropilins (NRPs) and transduces signals for class 3 semaphorins in the nervous system. It regulates facial nerve development by functioning as a receptor for Sema3A/NRP1. Both plexins A3 and A4 are essential for normal sympathetic development. They function both cooperatively, to regulate the migration of sympathetic neurons, and differentially, to guide sympathetic axons. Plexin A4 is also expressed in lymphoid tissues and functions in the immune system. It negatively regulates T lymphocyte responses. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module
FITFTGDQTEWTFNHLVVDERTGHIYLGAVNRIYKLSSDLKVLVTHQTGPDEDNPKCYPPRIVQTCNEPL
TLTNNINKMLLIDYKENRLIACGSLYQGICKLLRLDDLFKLGEPFHKKEHYLSGVNESGSVFGVIVSYSN
LDDKLFIATAVDGKPEYFPTISSRKLTKNSEADGMFAYVFHDEFVASMIKIPSDTFTIIPDFDIYYIYGF
SSGNFVYFLTLQPEMISPPGSTTKEQVYTSKLVRLCKEDTAFNSYVEVPIGCEKNGVEYRLLQAAYLSKA
GAILARSLGVGPDDDILFTVFSKGQKRKMKSLDESALCIFVLKEINDRIKDRLQSCYRGEGTLDLAWLKV
KDIPCSSALLTIDDNFCGLDMNAPLGVSEMVRGLPVFTEDRDRMTSVIAYVYKNHSLAFVGTKSGKLKKI
RVDGTTKNALQYETVQVVDTGPILRDMAFSKDHEQLYIMSEKQLTRVPVESCG
>gnl|CDD|200536 cd11275, Sema_plexin_B1, The Sema domain, a protein interacting module, of Plexin B1. Plexin B1 serves as the Semaphorin 4D receptor and functions as a regulator of developing neurons and a tumor suppressor protein for melanoma. The Sema4D-plexin B signaling complex regulates dendritic and axonal complexity. The activation of Plexin B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. As a tumor suppressor, plexin B1 abrogates activation of the oncogenic receptor, c-Met, by its ligand, hepatocyte growth factor (HGF), in melanoma. Furthermore, plexin B1 suppresses integrin-dependent migration and activation of pp125FAK and inhibits Rho activity. Plexin B1 is highly expressed in endothelial cells and its activation by Sema4D elicits a potent proangiogenic response. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module
FSPNGTKFLHLSMDPESGTLYLGATNFLFQLTPDLLLENMVQTGPVLDSKDCLPPVSKLECPQAQHTNNH
NKLLLVNPVQKELIVCGSVHQGICEKRRLGSIDHVLFRPERPGDTQYVAANDPNVTTVGLVAYSKDGVPL
LFVGRGYTSRGVGGGIPPITTRNLRAHGDDATDSHSIFSYEETAKLAVGRLSEYNHHFIKAFTYGSSVYF
LFYRRDLKSQSREYKTYISRICLDDSHYYSYVELPLLCQSKANTYSLLQAAYVTQPGERLAQGQLDTDGE
VLFAAFSAWQASSGKLSEESALCAYPMDEVDRLTNWTRDVCYTRDGKAEDGTEVAYIEYDVSSNCVQLPA
DTLDAYPCGSDHTPSPMASRVPLEATPLLEWTEIRLTAVAVNVEDGHTIAFLGDSRGRLHKVYLGAGGDA
HTYSSQSIQQNSAVSGDLLFDQLQEHLYVMTQSTVLKVPIA
>gnl|CDD|200537 cd11276, Sema_plexin_B2, The Sema domain, a protein interacting module, of Plexin B2. Plexin B2 serves as the receptor of Sema4C and Sema4G. By signaling the effect of Sema4C and Sema4G, the plexin B2 receptor plays important roles in neural tube closure and cerebellar granule cell development. Mice lacking Plexin B2 demonstrated defects in closure of the neural tube and disorganization of the embryonic brain. In developing kidney, Sema4C-Plexin B2 signaling modulates ureteric branching. Plexin B2 is expressed both in the pretubular aggregates and the ureteric epithelium in the developing kidney. Deletion of Plexin B2 results in renal hypoplasia and occasional double ureters. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module
FFQSATELNHLVVDPQTGRVYLGAVNALYQLDADLQLESRVETGPKKDNKKCTPPIEENQCTEAKMTDNY
NKLLLLDSANKTLVVCGSLFKGICSLRNLSNISEVIYYSDTSGEKSFVASNDEGVSTVGLISSLKPGNDR
VFFVGKGNGSNDNGKIISTRLLQNYDDREVFENYIDAATVKSAYVSRYTQQFRYAFEDNNYVYFLFNQQL
GHPDKNRTLIARLCENDHHYYSYTEMDLNCRDGANAYNKCQAAYVSTPGKELAQNYGNSILSDKVLFAVF
SRDEKDSGESALCMFPLKSINAKMEANREACYTGTIDDRDVFYKPFHSQKDIICGSHQQKNSKSFPCGSE
HLPYPLGSRDELALTAPVLQRGGLNLTAVTVAVENGHTVAFLGTSDGRILKVHLSPDPEEYNSILIEKNK
PVNKDLVLDKTLEHLYIMTEDKVFRLPVQ
>gnl|CDD|200538 cd11277, Sema_plexin_B3, The Sema domain, a protein interacting module, of Plexin B3. Plexin B3 is the receptor of semaphorin 5A. It is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin B3 has been linked to verbal performance and white matter volume in human brain. Furthermore, Sema5A and plexin B3 have been implicated in the progression of various types of cancer. They play an important role in the invasion and metastasis of gastric carcinoma. The stimulation of plexin B3 by Sema5A binding in human glioma cells results in the inhibition of cell migration and invasion. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module
FSAPNATFNHLALDPGSGTLYVGAVNRLYQLSPDLQLLGEAVTGPVLDSPDCLPFRDPADCPQARLTDNA
NKLLLVSERAGELVACGQVRQGVCEKRRLGNVAQVLYQAEDPGDGQFVAANDPGVATVGLVVEAPGRDLL
LVGRGLTGKLSAGIPPLTIRQLAGAQAFSSEGLGKLVVGDFSDYNNSYVGAFAHNGYVYFLFRRRGARAQ
AEYRTYVARVCLGDTNLYSYVEVPLVCQGGYNLAQAAYLAPGQGTLFVVFAAGQGSTPTPTDQTALCAYP
LVELDSAMERARRLCYTAGGGGPNGKEEATIEYGVTSRCVNLPKDSPESYPCGDEHTPSPIASRQPLEAE
PLLTLTPPLTAVAALQEDGHTIAFLGDTQGQLHKVFLNGSAGQVYSSQPVGPPGSAVNPDLLLDATGSHL
YVLTARQVTKVPVA
>gnl|CDD|200539 cd11278, Sema_MET, The Sema domain, a protein interacting module, of MET (also called hepatocyte growth factor receptor, HGFR). MET is encoded by the c-met protooncogene. MET is a receptor tyrosine kinase that binds its ligand, hepatocyte growth factor/scatter factor (HGF/SF). HGF/SF and MET are essential for the development of several tissues and organs, including the placenta, liver, and several groups of skeletal muscles. It also plays a major role in the abnormal migration of cancer cells as a result of overexpression or MET mutations. MET is composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a Sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic tyrosine kinase domain. The cytoplasmic C-terminal region acts as a docking site for multiple protein substrates, including Grb2, Gab1, STAT3, Shc, SHIP-1 and Src. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. The Sema domain of Met is necessary for receptor dimerization and activation
QCKEAAKKSEMNLNMKYQLPNFTAETPIQNVILHKHHIYVGAVNKIYVLNEDLQKVSEYKTGPVLEHPDC
FPCQDCSDKANLSNGVWKDNVNMALFVETYYDDQLISCGSVNRGTCQRHVFPHDHPADIQSEVHCIYSPQ
IEEEPDQCPDCVVSTLGSKVLVTVKDRFVNFFVGNTINSSYFPDHPLHSISVRRLKETQDGFEFLTDQSY
IDVLPEFRDSYPIKYVHAFESNNFVYFLTVQRESLDSQTFHTRIIRFCSIDSELRSYMEMPLECIFTEKR
RKRSTKKEVFNILQAAYVSKPGAQLAREMGASLNDDILFGVFAQSKPDSAEPMNRSAVCAVSIKTINEFF
NKIVDKQNVKCLQHFYGKNHEHCFNRTFLRNASYCEARRDEYRVEVTTALQRVDLFMGQFSNVLLTSISV
FTKGDLTIANLGTSEGRFMQVVVSRSGPSTPHVNFLLDSHPVSPEVIVEHTLNQNGYTLVITGKKITKIP
LN
>gnl|CDD|200540 cd11279, Sema_RON, The Sema domain, a protein interacting module, of RON Receptor Tyrosine Kinase. RON receptor tyrosine kinase is a Macrophage-stimulating protein (MSP) receptor. Upon binding of MSP, RON is activated via autophosphorylation within its kinase catalytic domain, resulting in a wide range of effects, including proliferation, tubular morphogenesis, angiogenesis, cellular motility and invasiveness. By interacting with downstream signaling molecules, it regulates macrophage migration, phagocytosis, and nitric oxide production. RON has been implicated in cancers of the breast, colon, pancreas and ovaries because both splice variants and receptor overexpression have been identified in these tumors. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as ligand recognition and binding model. RON is composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a Sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic tyrosine kinase domain. The Sema domain of RON may be necessary for receptor dimerization and activation
WQCPRIPYALTRNFSVKYVVPSFSAGSPIQNIVSYEDASAVFVATRNHLHVLNPELKLLQNLVTGPTGSP
GCQICALCPPGPPGPSPEDTDNKVLVLDPEEPWLYSCGSSLHGRCFLHELESRGSAVHIASTACLFSANA
NKPSDCPDCVASPLGTRVTVVEQSHTSYFYVASTLNSSVAASYSPRSVSIRRLKSDQDGFAPGFHSLTVL
PKYLDSYPIHYVHSFTSGDFVYFLTVQPESPDSSAYHTRLVRLSAKEPELRDYRELVLDCRFEPKRRRRR
RPAEREVPYNVLQAAHAAPVGSKLAVELGISEGQEVLFGVFAESQPGSPVPQKNSAVCAFPISLLNEAID
EGMEKCCSSSNSDRLFRGLDFFQPQSYCPHPPNLSAAVSNTSCWNFPTLVSTSSFRVDLFNGHLSGVLLT
SIYVTVLDNVTVAHLGTSDGRILQVVLQRSLNYLLYVSNFSLGDGQPVQRDVSRLGDSLLFASGNQVFKV
NIT
>gnl|CDD|200436 cd11280, gelsolin_like, Tandemly repeated domains found in gelsolin, severin, villin, and related proteins. Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins
PPRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEERKGKP
EIVRIRQGQEPREFWSLF
>gnl|CDD|200437 cd11281, ADF_drebrin_like, ADF homology domain of drebrin and actin-binding protein 1 (abp1). Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Many of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. Abp1 and drebrin (developmentally regulated brain protein) are multidomain proteins with an N-terminal ADF homology domain and one or more C-terminal SH3 domains. They have been shown to interact with polymeric F-actin, but not with monomeric G-actin, and do not appear to promote the disassembly of actin filaments. Drebrin rather stabilizes actin filaments by inducing changes in the helical twist and may promote or interfere with the interactions of other proteins with actin filaments
IDLSTNSPEILAAYEDVVDGKSSTDWALFTYEGKSNDLKVADTGDGGLEELVEEFSDGKVQYGFARVKDP
NSGLPKFVLINWCGEGVPDARKGSFASHVAAVANFLKGAHVQINARSEDDLDEDAILKKVSKASGA
>gnl|CDD|200438 cd11282, ADF_coactosin_like, Coactosin-like members of the ADF homology domain family. Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Many of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. The function of coactosins is not well understood. They appear to interfere with the capping of actin filaments in Dictyostelium, and may not be able to bind monomeric globular actin. A role for coactosins as chaperones stabilizing 5-lipoxygenase (5LO) has been suggested; 5LO plays a crucial role in leukotriene synthesis
EIREAYNDVRSDVSDTNWVLLGYESSNTLVLRGSGSGGIDELKAQLPDDEVLFGYVRITLGDGESKRSKF
VFITWIGENVSVLRRAKVSVHKGDVKEVLSPFHVELTASSKDEL
>gnl|CDD|200439 cd11283, ADF_GMF-beta_like, ADF-homology domain of glia maturation factor beta and related proteins. Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Most of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. The glia maturation factor (GMF), however, does not bind actin but interacts with the Arp2/3 complex (which contains actin-related proteins, amongst others) and suppresses Arp2/3 activity, inducing the dissociation of branched daughter filaments from their mother filaments. This family includes both mammalian GMF isoforms, GMF-beta and GMF-gamma. GMF-beta regulates cellular growth, fission, differentiation and apoptosis. GMF-gamma is important in myeloid cell development and is an important regulator for cell migration and polarity in neutrophils
DISDEVKEALKKFRFRKSKANAALILKIDKEKQEIVVDEELEDISIEELAEELPEHSPRFVLYSYKMKHD
DGRISYPLVLIYWSPQGCSPELQMLYAGAKELLVKEAEVTKVFEIRDGEELT
>gnl|CDD|200440 cd11284, ADF_Twf-C_like, C-terminal ADF domain of twinfilin and related proteins. Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Twinfilin contains two ADF domains, and inhibits the assembly of actin filaments by strongly interacting with monomeric ADP-actin (ADP-G-actin) in a 1:1 stochiometry (with it's C-terminal ADF domain, Twf-C) and inhibiting the actin monomer's nucleotide exchange. Mammalian twinfilin may also cap the barbed ends of F-actin filaments and prevent further assembly (or disassembly), in a process which requires both ADF domains. The N-terminal ADF domain (Twf-N) binds G-actin with a lower affinity than Twf-C; Twf-C can also bind F-actin. During capping, Twf-N may interact with the terminal actin subunit, and Twf-C may bind between two adjacent subunits at the side of the filament
PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIELVSSSSISIPDDLSSLIPSDHPRYHFYRYPHT
YLSSVVFIYSCPSGSKVKERMLYASSKSGLLNHAEDEGKIEIDKKIEIGDPDELTESFLSDE
>gnl|CDD|200441 cd11285, ADF_Twf-N_like, N-terminal ADF domain of twinfilin and related proteins. Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Twinfilin contains two ADF domains, and inhibits the assembly of actin filaments by strongly interacting with monomeric ADP-actin (ADP-G-actin) in a 1:1 stochiometry (with it's C-terminal ADF domain, Twf-C) and inhibiting the actin monomer's nucleotide exchange. Mammalian twinfilin may also cap the barbed ends of F-actin filaments and prevent further assembly (or disassembly), in a process which requires both ADF domains. The N-terminal ADF domain (Twf-N) binds G-actin with a lower affinity than Twf-C; Twf-C can also bind F-actin. During capping, Twf-N may interact with the terminal actin subunit, and Twf-C may bind between two adjacent subunits at the side of the filament
QSGITASEELLDAFKSAKSSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYR
LDSKSAGYEWVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA
>gnl|CDD|200442 cd11286, ADF_cofilin_like, Cofilin, Destrin, and related actin depolymerizing factors. Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. These proteins enhance the turnover rate of actin, and interact with actin monomers (G-actin) as well as actin filaments (F-actin), typically with a preference for ADP-G-actin subunits. The basic function of cofilin is to promote disassembly of aged actin filaments. Vertebrates have three isoforms of cofilin: cofilin-1 (Cfl1, non-muscle cofilin), cofilin-2 (muscle cofilin), and ADF (destrin). When bound to actin monomers, cofilins inhibit their spontaneous exchange of nucleotides. The cooperative binding to (aged) ADP-F-actin induces a local change in the actin filament structure and further promotes aging
SGVKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYE
TKDGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL
>gnl|CDD|200443 cd11287, Sec23_C, C-terminal Actin depolymerization factor-homology domain of Sec23. The C-terminal domain of the Sec23 subunit of the coat protein complex II (COPII) is distantly related to gelsolin-like repeats and the actin depolymerizing domains found in cofilin and similar proteins. Sec23 forms a tight complex with Sec24. The cytoplasmic Sec23/24 complex is recruited together with Sar1-GTP and Sec13/31 to induce coat polymerization and membrane deformation in the forming of COPII-coated endoplasmic reticulum vesicles. The function of the Sec23 C-terminal domain is unclear
EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYE
NFKDLLEAPVDDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN
>gnl|CDD|200444 cd11288, gelsolin_S5_like, Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins. Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins
SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKAS
LQEVAEGSEPDEFWEALGGKSE
>gnl|CDD|200445 cd11289, gelsolin_S2_like, Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins. Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins
KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGR
AKVIVLDEGDTNESPEFWKVLG
>gnl|CDD|200446 cd11290, gelsolin_S1_like, Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins. Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin_like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins
FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAA
AIKAVELDDYLGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG
>gnl|CDD|200447 cd11291, gelsolin_S6_like, Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins. Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins
KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPL
GRSKPRTPIYLVKQGNEPPTFTGYFHAWD
>gnl|CDD|200448 cd11292, gelsolin_S3_like, Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins. Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins
AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLR
KKKRPPYTQVTRVTEGGESALFKSKFAN
>gnl|CDD|200449 cd11293, gelsolin_S4_like, Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins. Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins
MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAAL
LTVELDEELKGRAVQVRVVQGKEPPHFLALF
>gnl|CDD|199894 cd11294, E_set_Esterase_like_N, N-terminal Early set domain associated with the catalytic domain of putative esterases. E or "early" set domains are associated with the catalytic domain of esterase at the N-terminal end. Esterases catalyze the hydrolysis of organic esters to release an alcohol or thiol and acid. The term esterase can be applied to enzymes that hydrolyze carboxylate, phosphate and sulphate esters, but is more often restricted to the first class of substrate. The N-terminal domain of esterase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others
GTVTFRLFAPKAKKVEVTGDFLPGPGPVAMTKDDDGVWSVTTGPLAPEIYSYSFNVDGVKVLDPSNPYVK
RDVSTVSSVFEVP
>gnl|CDD|199917 cd11295, Mago_nashi, Mago nashi proteins, integral members of the exon junction complex. Members of this family, which was originally identified in Drosophila and called mago nashi, are integral members of the exon junction complex (EJC). The EJC is a multiprotein complex that is deposited on spliced mRNAs after intron removal at a conserved position upstream of the exon-exon junction, and transported to the cytoplasm where it has been shown to influence translation, surveillance, and localization of the spliced mRNA. It consists of four core proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP and is supposed to be a binding platform for more peripherally and transiently associated factors along mRNA travel. Mago and Y14 form a stable heterodimer that stabilizes the complex by inhibiting eIF4AIII's ATPase activity. In humans, but not Drosophila, EJC is involved in nonsense-mediated mRNA decay (NMD) via binding to Upf3b, a central NMD effector. EJC is stripped off the mRNA during the first round of translation and then the complex components are transported back into the nucleus and recycled. The Mago-Y14 heterodimer has been shown to interact with the cytoplasmic protein PYM, an EJC disassembly factor, and specifically binds to the karyopherin nuclear receptor importin 13
DFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDTMIRKEAYVSPAVLEELKRIIEDSEILKED
DAKWPEPDRVGRQELEIVMGDEHISFTTSKIGSLVDVQQSKDPEGLRVFYYLVQDLKCLVFSLIGLHFKI
KPI
>gnl|CDD|211383 cd11296, O-FucT_like, GDP-fucose protein O-fucosyltransferase and related proteins. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes
YLLPIPDGGGFNNQRNEFLNALLLAILLGRTLVLPLCLACPIRLVGKHLRFSPEIRKLADRFVRKLLGLP
GGPYLAVHLRRGDFEVECCHLAKWMGEYLEECLLSAEEIAEKIKELMAERKLKVVYVATDEADREELREE
LRKAGIRVVTKDDLLEDAELLELEKLDNYLLSLVDQEICSRADVFIGTGFSTFSSNVALLRRWRGK
>gnl|CDD|350237 cd11297, PIN_LabA-like_N_1, uncharacterized subfamily of N-terminal LabA-like PIN domains. This N-terminal LabA-like PIN domain is found in a well conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. LabA from Synechococcus elongatus PCC 7942, (which does not contain this C-terminal domain), has been shown to play a role in cyanobacterial circadian timing. The LabA-like C-terminal domains characteristic of this subfamily may be related to the LOTUS domain family (which also co-occurs with LabA-like N-terminal domains). The function of the N-terminal domain is unknown. The LabA-like PIN domain family also includes the N-terminal domain of limkain b1, a human autoantigen localized to a subset of ABCD3 and PXF marked peroxisomes. Other members are the LabA-like PIN domains of human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
IAVLIDAENISASYADAILEELAKYGRVVVRRAYGDWSSPRLKGWKDELLEHGIEPIQQFSYTKGKNAAD
IALVIDAMDLLYTGRIDTFVIVSSDSDFTPLAQRLRELGKTVIGIGE
>gnl|CDD|211384 cd11298, O-FucT-2, GDP-fucose protein O-fucosyltransferase 2. O-FucT-2 adds O-fucose to thrombospondin type 1 repeats (TSRs), and appears conserved in bilateria. The O-fucosylation of TSRs appears to play a role in regulating secretion of metalloproteases of the ADAMTS superfamily. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes
YLLYDVNPGEGFNLRRDVYIRVANLVKSLNKRGKEQDWVLVLPPWGRLYHWKSRDIKQSRLPWSLFFDLE
SLNRYIPVIEYEEFLKETGPVSIDILYYLQHYAEGWEKGKWEDKLEERSCIIEPVYSKDCDGKYRGWFWG
YCEVTARKFSCLSFQGSASYLAPSLLENKFLRSIMIDRAEVLLHDHYGILDYWNARRSMRFAKHLRDIAN
EFRKEYLNSTDESDKTVRPEWWRMKKKKGSALGGPYLAVHLRRGDFVYGRKKDVPSLKGAAKQILNLMKK
LKLKKVFIATDAKKEELEELKKLLKKLKVVRYEPTLEELEKLKDGGVAIIDQWICAHARYFIGTKESTFS
FRIQEEREILGFPPDTTFNRLCGD
>gnl|CDD|211385 cd11299, O-FucT_plant, GDP-fucose protein O-fucosyltransferase, plant specific subfamily. Some members of this plant-specific family of O-fucosyltransferases have been annotated as auxin-independent growth promotors. The function of the protein seems unclear. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes
YLLVSANGGLNQQRSQICDAVAVARLLNATLVLPELDKNSVWGDSSKFGDIYDVDHFIKSLKDDVRVVKK
LPEELASKKPEITVKRVPSRSSPSYYLEEVLPLLKKHGVIRLAPFDSRLANDLLPPEIQRLRCRVNFHAL
RFVPEIEELGDKLVDRLREAGGPFLALHLRFEKDMLAFSGCGKCPLTPEEVGLLLRALGFPRSTRIYLAA
GEIYGGERRLDPLRSIFPNLYTKETLATAEELAPFSGHSSRLAALDYIVCLESDVFVPTYGGNFAKAVAG
HRRYLGHRKT
>gnl|CDD|211386 cd11300, Fut8_like, Alpha 1-6-fucosyltransferase. Alpha 1,6-fucosyltransferase (Fut8) transfers a fucose moiety from GDP-fucose to the reducing terminal N-acetylglucosamine of the core structure of Asn-linked oligosaccharides, in a process termed core fucosylation. Core fucosylation is essential for the function of growth factor receptors. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes
DGDSEWRRKELKKLSKLVQKRIHKLQNPKDCSKAKKLVCNLNKGCGFGCQLHHVVYCLIVAYGTNRTLIL
DSKGWRYSPGGWEKVFLPLSETCTDRSGDNTAVWWWEPTNSDVQVVKLPIIDSLHSRPPFLPLAVPEDLA
ERLERLHGDPRVWWIGQLLKYLMRPQPWLQDEIDEAKKELGFKHPIVGVHIRRTDKLGTEAAFHSLEEYM
EHVEEWYDKYELRGPSEKVKRRVYLATDDPSVFDEAKNKYPNYFFIGDPGISKSASLSTRYSDSSLKGII
IDIHLLSECDYLVCTFSSQVCRLAYELMQTRHPDASDRFHSLDDIYYY
>gnl|CDD|211387 cd11301, Fut1_Fut2_like, Alpha-1,2-fucosyltransferase. Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer of alpha-L-fucose to the terminal beta-D-galactose residue of glycoconjugates via an alpha-1,2-linkage, generating carbohydrate structures that exhibit H-antigenicity for blood-group carbohydrates. These structures also act as ligands for morphogenesis, the adhesion of microbes, and metastasizing cancer cells. Fut1 is responsible for producing the H antigen on red blood cells. Fut2 is expressed in epithelia of secretory tissues, and individuals termed "secretors" have at least one functional copy of the gene; they secrete H antigen which is further processed into A and/or B antigens depending on the ABO genotype. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes
MKIVSLLAGGLGNQLFQYAFLRALAKKLGRRKLFLDTSGYFERNLLKLLEFFNISLPILSRKEILLLKNL
RLLNEDPVLKKLLRENYRHYLGRYYQFWKYFYSIKGEIRQEFKFFEDLEEENNKILKKLKEELKNTNSVS
VHIRRGDYLTNGNAKGYHGICDLEYYKKAIEYIKEKVKNPVFFVFSDDIEWVKENLALTSKENVYFVDGN
NSSYEDLYLMSLCKHVIISNSTFSWWGAYLNKNPDKIVIIAPNPWFVKKKLFPPD
>gnl|CDD|211388 cd11302, O-FucT-1, GDP-fucose protein O-fucosyltransferase 1. The protein O-fucosyltransferase 1 (Ofut1 or O-FucT-1) adds O-fucose to EGF (epidermal growth factor-like) repeats. The O-fucsosylation of the Notch receptor signaling protein is dependent on this enzyme, which requires GDP-fucose as a substrate. O-fucose residues added to the target of O-FucT-1 may be further elongated by other glycosyltransferases. On top of O-fucosylation, O-FucT-1 may have other functions such as the regulation of the Notch receptor exit from the ER. Six highly conserved cysteines are present in O-FucT-1, which is a soluble ER protein, as well as a DXD-like motif (ERD), conserved in mammals, Drosophila, and C. elegans. Both features are characteristic of several glycosyltransferase families. The membrane-bound pre-protein is released by proteolysis and, as for most glycosyltransferases, is strongly activated by manganese. O-FucT-1 is similar to family 1 glycosyltransferases (GT1)
DPNGYILYCPCMGRFGNQADHFLGSLAFAKALNRTLVLPPWIEYRHGPPPSVQIPFDDYFKVEPLQEYHR
VITMEDFMEELAPTIWPPGKRKGYCYSPRASPDSKDCPMKEGNPFGPFWDHFGVDFDGSELYGPLSYDTF
YPDVREAWNERFPPSEHPVLAFTGAPASFPVLPENRPLHKYLEWSDEIVKEADEFINENLPRPFVGIHLR
NGIDWKNACEHVKGTSRNLMASPQCLGYGNERGTLTKEMCLPSKEEILKQVKRAVKKIKAKSVFIATDND
HMIEELKKALKSLKVKVVHLDPDEPQIDLAILGKADHFIGNCVSSFSAFVKRERDVAGLPSSFFGFN
>gnl|CDD|206636 cd11303, Dystroglycan_repeat, Cadherin-like repeat domain of alpha dystroglycan. Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. Cadherin-like dystroglycan repeats are present in the extracellular alpha-dystroglycan subunit, which binds to the alpha-2-laminin G-domain in the basement membrane as part of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with other etxtracellular matrix components as well, such as perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand
SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDTYQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYI
SVTAEDKGSAGSQASDVFSIDVHPEPHPE
>gnl|CDD|206637 cd11304, Cadherin_repeat, Cadherin tandem repeat domain. Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers
SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTL
TVTATDGGGPPLSSTATVTITVLDVNDN
>gnl|CDD|206765 cd11305, alpha_DG_C, C-terminal domain of alpha dystroglycan. Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. This C-terminal domain of the alpha-subunit appears to contact neighboring cadherin-like repeats of alpha dystroglycan, and may also be involved in interactions with other components of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with extracellular matrix components such as laminin, perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand
VCPNGEPVTVLTVILDADLSKLTPKQRVHLLNKLAKFLGLPLDAFKLLPVSNNGLFDMSALMAGPGNVKK
ANEAGTLLSWQVGCGGDLNHLPLVSQLEEQAKDGTLAEVLGLPVIGWHVANKKP
>gnl|CDD|199915 cd11306, M35_peptidyl-Lys, Peptidase M35 domain of peptidyl-Lys metalloendopeptidases. This family M35 Zn2+-metallopeptidase extracellular domain is mostly found in proteins characterized as peptidyl-Lys metalloendopeptidases (MEP; peptidyllysine metalloproteinase; EC 3.4.24.20), including some well-characterized domains in Aeromonas salmonicida subsp. Achromogenes (AsaP1) and Grifola frondosa (GfMEP). These proteins specifically cleave peptidyl-lysine bonds (-X-Lys- where X may even be Pro) in proteins and peptides. AsaP1 peptidase has been shown to be important in the virulence of A. salmonicida subsp. achromogenes, having a major role in the fish innate immune response. Members of this family contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand and is found in a GTXDXXYG or similar motif C-terminal to the His zinc ligands
GCSSTQQSQLNAAVTAASTYAANALSYLNAHTSGTTRYTTWFGTYTSSRYSTVLSHFSNIKSALDNKPYT
FDCSCTESGTYAYVYPSQPYTVYLCGAFWQAPTTGTDSKAGTLIHELSHFTVVAGTDDHVYGQSGAKSLA
RSNPAQAINNADNHEYFAEN
>gnl|CDD|199916 cd11307, M35_Asp_f2_like, Peptidase M35 domain of Asp f2, a major allergen from Aspergillus fumigatus, and related proteins; non catalytic. In this domain subgroup the unique zinc-binding motif (the aspzincin motif, characteristic of the M35 deuterolysin family, and defined as the "HEXXH + D" motif: two His ligands and Asp as third ligand), is poorly conserved and may not bind Zinc. Members of this subgroup also lack a key conserved Tyr residue which acts as a proton donor during metallopeptidase catalysis. These include Asp f2, a major allergen from Aspergillus fumigatus, which reacts with serum from patients with ABPA (allergic bronchopulmonary aspergillosis), and pH-regulated antigen 1 (PRA1) from Candida albicans, which has a role in fungal morphogenesis and perhaps in the host-parasite interaction during candidal infection. No protease activity has been detected for Asp f2 to date. This subgroup also includes Saccharomyces cerevisiae Zps1p. The expression of the Zsp1 gene is increased in response to zinc deficiency; it is a target of the Zap1p transcription factor
SCNATQRRQLSSALDETVELAAHAKDHLLRYGNSSEFYRKYFGNGPTAEVIGWYDNLIEGDKAGVLFRCD
DPDGNCAANPYWAGHWRGENATAETVICDLSYTSRKPLSQICSEGYTVAVGKPNTYWGIDLLHRYFHVPA
IGEGYIGHYAEEYEEVLELAKNNSTFAVRNSDSLQYYAA
>gnl|CDD|200604 cd11308, Peptidase_M14NE-CP-C_like, Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain. This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families
GIKGFVTDATGNPIANATISVEGINHDVTTAKDGDYWRLLLPGTYNVTASAPGYQPVTKTVTVPNNFSAT
VVNFTL
>gnl|CDD|206763 cd11309, 14-3-3_fungi, Fungal 14-3-3 protein domain. This family containing fungal 14-3-3 domains includes the yeasts Saccharomyces cerevisiae (BMH1 and BMH2) and Schizosaccharomyces pombe (rad24 and rad25) isoforms. They possess distinctively variant C-terminal segments that differentiate them from the mammalian isoforms; the C-terminus is longer and BMH1/2 isoforms contain polyglutamine (polyQ) sequences of unknown function. The C-terminal segments of yeast 14-3-3 isoforms may thus behave in a different manner compared to the higher eukaryote isoforms. Yeast 14-3-3 proteins bind to numerous proteins involved in a variety of yeast cellular processes making them excellent model organisms for elucidating the function of the 14-3-3 protein family. BMH1 and BMH2 are positive regulators of rapamycin-sensitive signaling via TOR kinases while they play an inhibitory role in Rtg3p-dependent transcription involved in retrograde signaling. 14-3-3 domains are an essential part of 14-3-3 proteins, a ubiquitous class of regulatory, phosphoserine/threonine-binding proteins found in all eukaryotic cells, including yeast, protozoa and mammalian cells
REDSVYLAKLAEQAERYEEMVENMKKVASSDQELTVEERNLLSVAYKNVIGARRASWRIVSSIEQKEESK
GNESQVALIKEYRSKIESELTKICDDILSVLDKHLIPSATTGESKVFYYKMKGDYHRYLAEFAVGDKRKE
AADSSLEAYKAASDIAVTELPPTHPIRLGLALNFSVFYYEILNSPDSACHLAKQAFDDAIAELDTLSEES
YKDSTLIMQLLRDNLTLWTSD
>gnl|CDD|206764 cd11310, 14-3-3_1, 14-3-3 protein domain. This 14-3-3 domain family includes proteins in Caenorhabditis elegans, the silkworm (Bombyx mori) as well as barley (Hordeum vulgare). In C. elegans, 14-3-3 proteins are SIR-2.1 binding partners which induce transcriptional activation of DAF-16 during stress and are required for the life-span extension conferred by extra copies of sir-2.1. In B. mori, the 14-3-3 proteins are expressed widely in larval and adult tissues, including the brain, fat body, Malpighian tube, silk gland, midgut, testis, ovary, antenna, and pheromone gland, and interact with the N-terminal fragment of Hsp60, suggesting that 14-3-3 (a molecular adaptor) and Hsp60 (a molecular chaperone) work together to achieve a wide range of cellular functions in B. mori. In barley aleurone cells, 14-3-3 proteins and members of the ABF transcription factor family have a regulatory function in the gibberellic acid (GA) pathway since the balance of GA and abscisic acid (ABA) is a determining factor during transition of embryogenesis and seed germination. 14-3-3 is an essential part of 14-3-3 proteins, a ubiquitous class of regulatory, phosphoserine/threonine-binding proteins found in all eukaryotic cells, including yeast, protozoa and mammalian cells
DKEELVQRAKLAEQAERYDDMAAAMKKVTETGVELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEG
SERKQQMAKEYREKVEKELREICYDVLGLLDKFLIPKASNPESKVFYLKMKGDYYRYLAEVATGDTRNSV
VEDSQKAYQEAFDISKAKMQPTHPIRLGLALNFSVFYYEILNSPDKACQLAKQAFDDAIAELDTLNEDSY
KDSTLIMQLLRDNLTLWTSD
>gnl|CDD|200452 cd11313, AmyAc_arch_bac_AmyA, Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes firmicutes, bacteroidetes, and proteobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
WLRDAVIYEVNVRQFTPEGTFKAVTKDLPRLKDLGVDILWLMPIHPIGEKNRKGSLGSPYAVKDYRAVNP
EYGTLEDFKALVDEAHDRGMKVILDWVANHTAWDHPLVEEHPEWYLRDSDGNITNKVFDWTDVADLDYSN
PELRDYMIDAMKYWVREFDVDGFRCDVAWGVPLDFWKEARAELRAVKPDVFMLAEAEPRDDDELYSAFDM
TYDWDLHHTLNDVAKGKASASDLLDALNAQEAGYPKNAVKMRFLENHDENRWAGTVGEGDALRAAAALSF
TLPGMPLIYNGQEYGLDKRPSFFEKDPIDWTKNHDLTDLYQKLIALKKENPALRGG
>gnl|CDD|200453 cd11314, AmyAc_arch_bac_plant_AmyA, Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
VMLQGFYWDSPKDGTWWNHLESKAPELAAAGFTAIWLPPPSKSVSGSSMGYDPGDLYDLNSRYGSEAELR
SLIAALHAKGIKVIADIVINHRSGPDTGEDFGGAPDLDHTNPEVQNDLKAWLNWLKNDIGFDGWRFDFVK
GYAPSYVKEYNEATSPSFSVGEYWDGLSYENQDAHRQRLVDWIDATGGGSAAFDFTTKYILQEAVNNNEY
WRLRDGQGKPPGLIGWWPQKAVTFVDNHDTGSTQGHWPFPTDNVLQGYAYILTHPGTPCVFWDHYYDWGL
KDEIKALIAARKRAGIGSTSKV
>gnl|CDD|200454 cd11315, AmyAc_bac1_AmyA, Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
DGVILHAFDWSFNTIKENLPEIAAAGYTAIQTSPPQKSKEGGNEGGNWWYRYQPTDYRIGNNQLGTEDDF
KALCAAAHKYGIKIIVDVVFNHMANEGSAIEDLWYPSADIELFSPEDFHGNGGISNWNDRWQVTQGRLGG
LPDLNTENPAVQQQQKAYLKALVALGVDGFRFDAAKHIELPDEPSKASDFWTNILNNLDKDGLFIYGEVL
QDGGSRDSDYASYLSLGGVTASAYGFPLRGALKNAFLFGGSLDPASYGQALPSDRAVTWVESHDTYNNDG
FESTGLDDEDERLAWAYLAARDGGTPLFFSRPNGSGGTNPQIGDRGDDAWKSPDVVAVNKFHNAMHGQPE
YL
>gnl|CDD|200455 cd11316, AmyAc_bac2_AmyA, Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Chloroflexi, Dictyoglomi, and Fusobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
GVFYEIFVRSFYDSDGDGIGDLNGLTEKLDYLNDLGVNGIWLMPIFPSPSYHGYDVTDYYAIEPDYGTME
DFERLIAEAHKRGIKVIIDLVINHTSSEHPWFQEAASSPDSPYRDYYIWADDDPGGWSSWGGNVWHKAGD
GGYYYGAFWSGMPDLNLDNPAVREEIKKIAKFWLDKGVDGFRLDAAKHIYENGEGQADQEENIEFWKEFR
DYVKSVKPDAYLVGEVWDDPSTIAPYYASGLDSAFNFDLAEAIIDSVKNGGSGAGLAKALLRVYELYAKY
NPDYIDAPFLSNHDQDRVASQLGGDEAKAKLAAALLLTLPGNPFIYYGEEIGMLGSKPDENIRTPMSWDA
DSGAGFTTWIPPRPNTNATTASVEAQEADPDSLLNHYKRLIALRNEYPALARG
>gnl|CDD|200456 cd11317, AmyAc_bac_euk_AmyA, Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRD
MVNRCNAAGVRVYVDAVINHMAGDANEVRNCELVGLADLNTESDYVRDKIADYLNDLISLGVAGFRIDAA
KHMWPEDLAAILARLKDLNGGPLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFRYARGLSNAFRGKIK
LLLLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGGDMLTYKDGRRYKLANAFMLAWPYGTPRVMSSYYF
SDSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV
>gnl|CDD|200457 cd11318, AmyAc_bac_fung_AmyA, Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes bacterial and fungal proteins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
NGTMMQYFEWYLPADGQHWKRLAEDAPELAELGITAVWLPPAYKGASGTEDVGYDVYDLYDLGEFDQKGT
VRTKYGTKEELLEAIKALHENGIQVYADAVLNHKAGADETETVKAVEVDPNDRNKEISEPYEIEAWTKFT
FPGRGGKYSDFKWNWQHFSGVDYDQKTKKKGIFKINFEGKGWDEDVDDENGNYDYLMGADIDYSNPEVRE
ELKRWGKWYINTTGLDGFRLDAVKHISASFIKDWIDHLRRETGKDLFAVGEYWSGDLEALEDYLDATDGK
MSLFDVPLHYNFHEASKSGGNYDLRKIFDGTLVQSRPDKAVTFVDNHDTQPGQSLESWVEPWFKPLAYAL
ILLRKDGYPCVFYGDYYGIPGEDPIPPKKELLDKLLKARKL
>gnl|CDD|200458 cd11319, AmyAc_euk_AmyA, Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
ASADEWRSRSIYQVLTDRFARTDGSSTAPCDTADRTYCGGTWKGIINKLDYIQGMGFDAIWISPIVKNIE
GNTAYGEAYHGYWAQDLYSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHMASAGPGSDVDYSSFVPF
NDSSYYHPYCWITDYNNQTSVEDCWLGDDVVALPDLNTENPFVVSTLNDWIKNLVSNYSIDGLRIDTAKH
VRKDFWPGFVEAAGVFAIGEVFDGDPNYVCPYQNYLDGVLNYPLYYPLVDAFQSTKGSMSALVDTINSVQ
SSCKDPTLLGTFLENHDNPRFLSYTSDQALAKNALAFTLLSDGIPIIYYGQEQGFNGGNDPYNREALWLS
GYDTSSPLYKFIKTLNAIRKAAISQ
>gnl|CDD|200459 cd11320, AmyAc_AmyMalt_CGTase_like, Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
DFETDVIYQILTDRFYDGDTSNNPPGSPGLYDPTHSNLKKYWGGDWQGIIDKLPYLKDLGVTAIWISPPV
ENINSPIEGGGNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPADYAEDGAL
YDNGTLVGDYPNDDNGWFHHNGGIDDWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGI
RVDAVKHMPPGWQKSFADAIYSKKPVFTFGEWFLGSPDPGYEDYVKFANNSGMSLLDFPLNQAIRDVFAG
FTATMYDLDAMLQQTSSDYNYENDLVTFIDNHDMPRFLTLNNNDKRLHQALAFLLTSRGIPVIYYGTEQY
LHGGTQVGGDPYNRPMMPSFDTTTTAYKLIKKLADLRKS
>gnl|CDD|200460 cd11321, AmyAc_bac_euk_BE, Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
PEEPYQFKHPRPPKPRALRIYEAHVGMSSEEPKVASYREFTDNVLPRIKKLGYNAIQLMAIMEHAYYASF
GYQVTNFFAASSRFGTPEDLKYLIDTAHGMGIAVLLDVVHSHASKNVLDGLNMFDGTDGCYFHEGERGNH
PLWDSRLFNYGKWEVLRFLLSNLRWWLEEYRFDGFRFDGVTSMLYHHHGLGTGFSGDYGEYFGLNVDEDA
LVYLMLANDLLHELYPNAITIAEDVSGMPGLCRPVSEGGIGFDYRLAMAIPDKWIKLLKEKKDEDWNMGN
IVHTLTNRRYGEKTIAYAESHDQALVGDKTLAFWLMDKEMYTNMSVLSPLTPVIDRGIALHKMIRLITHA
LGGEGYLNFMGNEFGHPEWLDFPREGNNWSYHYARRQWNLVDDDLLRYKFLNNFDR
>gnl|CDD|200461 cd11322, AmyAc_Glg_BE, Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1,4-alpha-glucan branching enzyme). The glycogen branching enzyme catalyzes the third step of glycogen biosynthesis by the cleavage of an alpha-(1,4)-glucosidic linkage and the formation a new alpha-(1,6)-branch by subsequent transfer of cleaved oligosaccharide. They are part of a group called branching enzymes which catalyze the formation of alpha-1,6 branch points in either glycogen or starch. This group includes proteins from bacteria, eukaryotes, and archaea. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
LRPNTASIVYDLSGYKWTDKKWMKKRKRKNKKNKPMNIYEVHLGSWKRKEDGRFLSYRELADELIPYVKE
MGYTHVELMPVMEHPFDGSWGYQVTGYFAPTSRYGTPDDFKYFVDACHQAGIGVILDWVPGHFPKDDHGL
ARFDGTPLYEYPDPRKGEHPDWGTLNFDYGRNEVRSFLISNALYWLEEYHIDGLRVDAVSSMLYLDYDRG
PGEWIPNIYGGNENLEAIEFLKELNTVIHKRHPGVLTIAEESTAWPGVTAPVEEGGLGFDYKWNMGWMND
TLDYFKTDPIYRKYHHNKLTFSMMYAYSENFILPLSHDEVVHGKKSLLDKMPGDYWQKFANLRLLYGYMM
AHPGKKLLFMGNEFGQFREWNEDRELDWFLLEYPLHRGFQRFVKDLNKLYRE
>gnl|CDD|200462 cd11323, AmyAc_AGS, Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine diphosphoglucose-1,3-alpha-glucan glucosyltransferase and 1,3-alpha-D-glucan synthase). Alpha 1,3-glucan synthase (AGS, EC 2.4.1.183) is an enzyme that catalyzes the reversible chemical reaction of UDP-glucose and [alpha-D-glucosyl-(1-3)]n to form UDP and [alpha-D-glucosyl-(1-3)]n+1. AGS is a component of fungal cell walls. The cell wall of filamentous fungi is composed of 10-15% chitin and 10-35% alpha-1,3-glucan. AGS is triggered in fungi as a response to cell wall stress and elongates the glucan chains in cell wall synthesis. This group includes proteins from Ascomycetes and Basidomycetes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
LLLLLLLLSSLVLALPYDEELVDYNLNQNKSATDPLDYSGEWPGHEYTPSPDNWRFPFYTIFLDRFVNGD
PTNDDANGTVFEQDIYETQLRHGGDIVGLVDSLDYLQGMGIKGIYIAGTPFINMPWGADGYSPLDFTLLD
HHFGTIADWRAAIDEIHRRGMYVVLDNTVATMGDLIGFEGYLNTSAPFSLKEYKAEWKTPRRYVDFNFTN
TYNETCEYPRFWDEDGTPVTADVTETLTGCYDSDFDQYGDVEAFGVHPDWQRQLSKFASVQDRLREWRPS
VAQKLKHFSCLTIQMLDIDGFRIDKATQVTVDFLGEWSAAVRECARKVGKDNFFIPGEITGGNTFGSIYI
GRGRQPNQRPNNLTEALNTTSSDSQYFLREEGQNALDAAAFHYSVYRALTRFLGMDGNLEAGYDVPVNFV
EAWNQMLVTNDFLNANTGKFDPRHMYGVSNQDVFRWPAIENGTERQLLGLFITTLLMPGIPLLYYGEEQA
FYVLDNTADNYLYGRQPMTSAPAWQLHGCYKLGSSQYYNFPLEKALTGCHDDWNSLDHRDPSHPVRNILK
HMNELREQY
>gnl|CDD|200463 cd11324, AmyAc_Amylosucrase, Alpha amylase catalytic domain found in Amylosucrase. Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
DADIFLLRLARHFPDLFELLYTLYGDRADFDEHLERLLASLAKAYAARPADLKALDLAREADPDWFQSPD
MVGYALYVDLFAGDLKGLAEKIPYLKELGVTYLHLMPLLKPPEGDNDGGYAVSDYREVDPRLGTMEDLRA
LAAELRERGISLVLDFVLNHTADEHEWAQKARAGDPEYQDYYYMFPDRTLPDAYERTLPEVFPDTAPGNF
TWDEEMGKWVWTTFNPFQWDLNYANPAVFNEMLDEMLFLANQGVDVLRLDAVAFIWKRLGTNCQNLPEAH
TILQALRACLRIVAPAVVFKAEAIVAPDEVVKYFGTGEHPECELAYNNSLMALLWSALATRDTRLLRRAL
RRRPALPPGATWVNYVRCHDDIGWGFDDEDAAALGIDPFAHRRFLNDFYTGRFPGSFARGEPFQENPVTG
DARISGTAASLAGLEKALEEGDAAAIDLAIRRILLLHGVILSFGGIPLIYMGDELGLLNDYSYLDDPAKA
DDSRWVHRPKMDWERAARRHDPGTVEGRIFQGLRRLIAVRRQLPAL
>gnl|CDD|200464 cd11325, AmyAc_GTHase, Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase). Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase
DPASRFQPEGVHGPSVVVDPSAFWWTDAGWRGPPLEELVIYELHVGTFTPEGTFDAAIERLDYLADLGVT
AIELMPVAEFPGERNWGYDGVLPFAPESSYGGPDDLKRLVDAAHRRGLAVILDVVYNHFGPDGNYLWQFA
GPYFTDDYSTPWGDAINFDGPGDEVRQFFIDNALYWLREYHVDGLRLDAVHAIRDDSGWHFLQELAREVR
AAAAGRPAHLIAEDDRNDPRLVRPPELGGAGFDAQWNDDFHHALHVALTGEREGYYADFGPAEDLARALA
EGFVYQGQYSPFRGRRHGRPSADLPPTRFVVFLQNHDQVGNRAAGERLSSLAAPARLRLAAALLLLSPGI
PMLFMGEEFGEDTPFLFFTDHDDPELAEAVREGRRREFAAGWDRDLIPDPQAPETFTRSKLDWAERGIHA
AHLALYRRLLALRRWD
>gnl|CDD|200465 cd11326, AmyAc_Glg_debranch, Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
FDWEGDARPRIPWEDTVIYEMHVRGFTKLHPDVPEELRGTYAGLAEPAKIPYLKELGVTAVELLPVHAFD
DEEHLVERGLTNYWGYNTLNFFAPDPRYASDDAPGGPVDEFKAMVKALHKAGIEVILDVVYNHTAEGGEL
GPTLSFRGLDNASYYRLDPDGPYYLNYTGCGNTLNTNHPVVLRLILDSLRYWVTEMHVDGFRFDLASVLG
RDPDGFPDPNPPLLEAIAQDPVLSGVKLIAEPWDIGGGGYQVGNFPPGWAEWNDRYRDDVRRFWRGDGGL
VGDFATRLAGSSDLFGHDGRSPSASVNFITAHDGFTLADLVSYNEKHNEANGENNRDGHNDNLSWNCGVE
GPTDDPEILALRRRQMRNLLATLLLSQGTPMLLAGDEFGRTQQGNNNAYCQDNEISWLDWDLLEADSDLF
RFVRRLIALRKAH
>gnl|CDD|200466 cd11327, AmyAc_Glg_debranch_2, Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities, 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. The catalytic triad (DED), which is highly conserved in other debranching enzymes, is not present in this group. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
SGYFQVDPVLTINGKPLPLDGITIQTVLSKCLGPFDEWEERLRVAKELGYNMIHFTPLQELGESNSPYSI
ADQLELNPDFFPDGKKKTFEDVEELVKKLEKEWGLLSITDVVLNHTANNSPWLLEHPEAGYNLENSPHLR
PAYELDRALLEFSNDLAEGKYPERGVPSENEEDLNAIMEILKEEVLPPLKLWEFYVLDVEKAVEQFKEAL
KSGKPKLPKKGSDVSLADILKKEELLIIQDPLYERFGATVDMEKAAEIFNSHRGDEERIEECLERFRKAL
DELNVPLYREYDEDLNAAVNNIIGRIRYERLDENGPKLGEITKKHPLVERYFTRLFADESSAKSDKKKLV
LANNGWVMGADPLKDFASPDSKVYLRRELIVWGDCVKLRYGSKPEDSPFLWKHMKEYTQLTAKIFHGFRI
DNCHSTPLHVAEYLLDAARKVNPDLYVVAELFTGSEEMDNIFVNRLGINSLIREAMQA
>gnl|CDD|200467 cd11328, AmyAc_maltase, Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related proteins. Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1-_4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. In most cases, maltase is equivalent to alpha-glucosidase, but the term "maltase" emphasizes the disaccharide nature of the substrate from which glucose is cleaved, and the term "alpha-glucosidase" emphasizes the bond, whether the substrate is a disaccharide or polysaccharide. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
DKDWWENAVFYQIYPRSFKDSDGDGIGDLKGITEKLDYFKDIGIDAIWLSPIFKSPMVDFGYDISDFTDI
DPIFGTMEDFEELIAEAKKLGLKVILDFVPNHSSDEHEWFQKSVKRDEPYKDYYVWHDGKNNDNGTRVPP
NNWLSVFGGSAWTWNEERQQYYLHQFAVKQPDLNYRNPKVVEEMKNVLRFWLDKGVDGFRIDAVPHLFED
EDFLDEPYSDEPGADPDDYDYLDHIYTKDQPETYDLVYEWREVLDEYAKENNGDTRVMMTEAYSSLDNTM
KYYGNETTYGAHFPFNFELITNLNKNSNATDFKDLIDKWLDNMPEGQTANWVLGNHDNPRVASRFGEERV
DGMNMLSMLLPGVAVTYYGEEIGMEDTTISWEDTVDPPACNAGPENYEAYSRDPARTPFQWDDSKNAGFS
TANKTWLPVNPNYKTLNLEAQKKDPRSHYNIYKKLAQLRKSPTFLRGDLE
>gnl|CDD|200468 cd11329, AmyAc_maltase-like, Alpha amylase catalytic domain family found in maltase. Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1-_4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. The catalytic triad (DED) which is highly conserved in the other maltase group is not present in this subfamily. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
IGGSKQAFSGMGKEELMKYANDPFWVRLRWLLFVLFWLLWVAMLLGAVAIIVLAPKCAAPVPLKWWQKGP
LVELDTESFFKEEHVEAISKLGAKGVIYELPADETYLNNSYGVESDLKELVKTAKQKDIKVILDLTPNHS
SKQHPLFKDSVLKEPPYRSAFVWADGKGHTPPNNWLSVTGGSAWKWVEDRQYYLHQFGPDQPDLNLNNPA
VVDELKDVLKHWLDLGVRGFRLANAKYLLEDPNLKDEEISSNTKGVTPNDYGFYTHIKTTNLPELGELLR
EWRSVVKNYTDGGGLSVAEDIIRPDVYQVNGTLDLLIDLPLYGNFLAKLSKAITANALHKILASISTVSA
TTSWPQWNLRYRDTKVVASDALTLFTSLLPGTPVVPLDSELYANVSKPTISTLEKFRATPSIQHGSFNAY
LLNNDTVFAYTRIKSGNPGYLVALNLSENPTVVDFSSDDGIPEEVTVVLTSENYVVN
>gnl|CDD|200469 cd11330, AmyAc_OligoGlu, Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
PWWRGAVIYQIYPRSFLDSNGDGIGDLPGITEKLDYIASLGVDAIWLSPFFKSPMKDFGYDVSDYCAVDP
LFGTLDDFDRLVARAHALGLKVMIDQVLSHTSDQHPWFEESRQSRDNPKADWYVWADPKPDGSPPNNWLS
VFGGSAWQWDPRRGQYYLHNFLPSQPDLNFHNPEVQDALLDVARFWLDRGVDGFRLDAVNFYMHDPALRD
NPPRPPDEREDGVAPTNPYGMQLHIHDKSQPENLAFLERLRALLDEYPGRFLVGEVSDDDPLEVMAEYTS
GGDRLHMAYSFDLLGRPFSAAVVRDALEAFEAEAPDGWPCWAFSNHDVPRAVSRWAGGADDPALARLLLA
LLLSLRGSVCLYQGEELGLPEAELPFEELQDPYGITFWPEFKGRDGCRTPMPWQADAPHAGFSTAKPWLP
VPPEHLALAVDVQEKDPGSVLNFYRRFLAWRKAQPALRTGTITFLDAPEPLL
>gnl|CDD|200470 cd11331, AmyAc_OligoGlu_like, Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
LWWQTGVIYQIYPRSFQDSNGDGVGDLRGIISRLDYLSDLGVDAVWLSPIYPSPMADFGYDVSDYCGIDP
LFGTLEDFDRLVAEAHARGLKVILDFVPNHTSDQHPWFLESRSSRDNPKRDWYIWRDPAPDGGPPNNWRS
EFGGSAWTWDERTGQYYLHAFLPEQPDLNWRNPEVRAAMHDVLRFWLDRGVDGFRVDVLWLLIKDPQFRD
NPPNPDWRGGMPPHERLLHIYTADQPETHEIVREMRRVVDEFGDRVLIGEIYLPLDRLVAYYGAGRDGLH
LPFNFHLISLPWDAAALARAIEEYEAALPAGAWPNWVLGNHDQPRIASRVGPAQARVAAMLLLTLRGTPT
LYYGDELGMEDVPIPPERVQDPAELNQPGGGLGRDPERTPMPWDASPNAGFSAADPWLPLSPDARQRNVA
TQEADPGSMLSLYRRLLALRRAHPALSAGS
>gnl|CDD|200471 cd11332, AmyAc_OligoGlu_TS, Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), trehalose synthase (also called maltose alpha-D-glucosyltransferase), and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Trehalose synthase (EC 5.4.99.16) catalyzes the isomerization of maltose to produce trehalulose. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
PWWRDAVVYQVYPRSFADANGDGIGDLAGIRARLPYLAALGVDAIWLSPFYPSPMADGGYDVADYRDVDP
LFGTLADFDALVAAAHELGLRVIVDIVPNHTSDQHPWFQAALAAGPGSPERARYIFRDGRGPDGELPPNN
WQSVFGGPAWTRVTEPDGTDGQWYLHLFAPEQPDLNWDNPEVRAEFEDVLRFWLDRGVDGFRIDVAHGLA
KDPGLPDAPGGGLPVGERPGSHPYWDRDEVHDIYREWRAVLDEYDPPRVLVAEAWVPDPERLARYLRPDE
LHQAFNFDFLKAPWDAAALRRAIDRSLAAAAAVGAPPTWVLSNHDVVRHVSRYGLPTPGPDPSGIDGTDE
PPDLALGLRRARAAALLMLALPGSAYLYQGEELGLPEVEDLPDALRQDPIWERSGGTERGRDGCRVPLPW
SGDAPPFGFSPGGAEPWLPQPAWWARYAVDAQEADPGSTLSLYRRALRLRRELPAGGGGLV
>gnl|CDD|200472 cd11333, AmyAc_SI_OligoGlu_DGase, Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
KEAVVYQIYPRSFKDSNGDGIGDLPGIISKLDYLKDLGVDAIWLSPIYPSPQVDNGYDISDYRAIDPEFG
TMEDFDELIKEAHKRGIKIIMDLVVNHTSDEHPWFQESRSSRDNPYRDYYIWRDGKDGKPPNNWRSFFGG
SAWEYDPETGQYYLHLFAKEQPDLNWENPEVRQEIYDMMRFWLDKGVDGFRLDVINLISKDPDFPDAPPG
DGDGLSGHKYYANGPGVHEYLQELNREVFSKYDIMTVGEAPGVDPEEALKYVGPDRGELSMVFNFEHLDL
DYGPGGKWKPKPWDLEELKKILSKWQKALQGDGWNALFLENHDQPRSVSRFGNDGEYRVESAKMLATLLL
TLRGTPFIYQGEEIGMTNSRDNARTPMQWDDSPNAGFSTGKPWLPVNPNYKEINVEAQLADPDSVLNFYK
KLIALRKE
>gnl|CDD|200473 cd11334, AmyAc_TreS, Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
WYKNAVIYQLDVRTFMDSNGDGIGDFRGLTEKLDYLQWLGVTAIWLLPFYPSPLRDDGYDIADYYGVDPR
LGTLGDFVEFLREAHERGIRVIIDLVVNHTSDQHPWFQAARRDPDSPYRDYYVWSDTPPKYKDARIIFPD
VEKSNWTWDEVAGAYYWHRFYSHQPDLNFDNPAVREEILRIMDFWLDLGVDGFRLDAVPYLIEREGTNCE
NLPETHDFLKRLRAFVDRRYPDAILLAEANQWPEEVREYFGDGDELHMAFNFPLNPRLFLALAREDAFPI
IDALRQTPPIPEGCQWANFLRNHDELTLEMLTDEERDYVYAAFAPDPRMRIYNRGIRRRLAPMLGGDRRR
IELAYSLLFSLPGTPVIYYGDEIGMGDNLYLPDRDGVRTPMQWSADRNGGFSTADPQKLYLPVIDDGPYG
YERVNVEAQRRDPSSLLNWVRRLIALR
>gnl|CDD|200474 cd11335, AmyAc_MTase_N, Alpha amylase catalytic domain found in maltosyltransferase. Maltosyltransferase (MTase), a maltodextrin glycosyltransferase, acts on starch and maltooligosaccharides. It catalyzes the transfer of maltosyl units from alpha-1,4-linked glucans or maltooligosaccharides to other alpha-1,4-linked glucans, maltooligosaccharides or glucose. MTase is a homodimer. The catalytic core domain has the (beta/alpha) 8 barrel fold with the active-site cleft formed at the C-terminal end of the barrel. Substrate binding experiments have led to the location of two distinct maltose-binding sites: one lies in the active-site cleft and the other is located in a pocket adjacent to the active-site cleft. It is a member of the alpha-amylase family, but unlike typical alpha-amylases, MTase does not require calcium for activity and lacks two histidine residues which are predicted to be critical for binding the glucose residue adjacent to the scissile bond in the substrates. The common reaction chemistry of the alpha-amylase family of enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
GEIFVNPYEFYLETINKILKDPKGAVKYYKLSKLKGASKGDWIKSSSVYSLFVRTTTAWDHDGDGALEPE
NLYGFRETGTFLKMIALLPYLKRMGINTIYLLPITKISKKFKKGELGSPYAVKNFFEIDPLLHDPLLGDL
SVEEEFKAFVEACHMLGIRVVLDFIPRTAARDSDLILEHPEWFYWIKVDELNNYHPPKVPGLGFVLPSQE
TLPLIYESEDVKEHLKLFRWSPNKIDPEKWRNFFKENPKPEGDFLGEIEKEFGCTTAPAFSDWINDPQPP
WTDVTYLRLYLDHPFEAKKFLDANQPPYILFDVIKASLFPGKEPNMELWEYLSGIIPYYQKEFGIDGARI
DMGHALPEELKKMIVEKARKIDPDFAFIAEELDMENSPAAKEEGYNAIIGSSWYVEPRVWERKLHNFLYK
LGVLALPFFAAGETHDTPRVASREGGRKLSKFLTVLNAFLPNGIPFINSGQEIFEVQPMNLGLDFDPEDR
YVLPPEDLPYGKLAFFDWYALHYNNGLEPLPALLEKLLKIRKRYLDAI
>gnl|CDD|200475 cd11336, AmyAc_MTSase, Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase). Maltooligosyl trehalose synthase (MTSase) domain. MTSase and maltooligosyl trehalose trehalohydrolase (MTHase) work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
ATYRLQLHKGFTFADAAALVPYLADLGISHLYASPILTARPGSTHGYDVVDHTRINPELGGEEGLRRLAA
ALRAHGMGLILDIVPNHMAVSGAENPWWWDVLENGPDSPYAGFFDIDWEPPKELRGKVLLPVLGDPYGEV
LEAGELKLVFDGGGFVLRYYDHRFPLAPLLERQHYRLAHWRVADDEINYRRFFDVNDLAGLRVEDPEVFD
ATHALILRLVREGLVDGLRIDHPDGLADPAGYLRRLREALGGPAYIVVEKILAPGEELPADWPVDGTTGY
DFLNEVNGLFVDPAGEAALTRLYRRFTGDPGDFAELVREAKRLVLDTSLAGELNRLARLLGRIAEADRRT
RDFTLNALRRALAELLAAFPVYRTYLEFAMRFQQLTGPVMAKGVEDTAFYRYNRLLSLNEVGGDPGRFGL
SVAAFHAANAERAARWPHTMTATSTHDTKRGEDVRARLAVLSELPEEWAEAVRRWRRLNAPLRTGPAPDP
NDEYLLYQTLVGAWPLDGDALADFAERLAAYMLKALREAKLHTSWTDPDEAYEEAVAAFVDALLDPPPSR
AFLADFAAFVRRIAPAGALNSLAQTLLKLTSPGVPDVYQGTELWDLSLVDPDNRRPVDYAARARLLAELD
AGEAALLANWRDGRIKLALTARLLRLRREH
>gnl|CDD|200476 cd11337, AmyAc_CMD_like, Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is mainly bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
IFYHIYPLGFCGAPIRNDFDGPPEHRLLKLEDWLPHLKELGCNALYLGPVFESDSHGYDTRDYYRIDRRL
GTNEDFKALVAALHERGIRVVLDGVFNHVGRDFFWEGHYDLVKLNLDNPAVVDYLFDVVRFWIEEFDIDG
LRLDAAYCLDPDFWRELRPFCRELKPDFWLMGEVIHGDYNRWVNDSMLDSVTNYELYKGLWSSHNDHNFF
EIAHSLNRLFRHNGLYRGFHLYTFVDNHDVTRIASILGDKAHLPLAYALLFTMPGIPSIYYGSEWGIEGV
KEEGSDADLRPLPLRPAELSPLGNELTRLIQALIALRRRSPALCYGSY
>gnl|CDD|200477 cd11338, AmyAc_CMD, Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
DAVFYQIFPDRFANGDPSNDPKGGEYNYFGWPDLPDYPPPWGGEPTRRDFYGGDLQGIIEKLDYLKDLGV
NAIYLNPIFEAPSNHKYDTADYFKIDPHLGTEEDFKELVEEAHKRGIRVILDGVFNHTGDDSPYFQDVLK
YGESSAYQDWFSIYYFWPYFTDEPPNYESWWGVPSLPKLNTENPEVREYLDSVARYWLKEGDIDGWRLDV
ADEVPHEFWREFRKAVKAVNPDAYIIGEVWEDARPWLQGDQFDSVMNYPFRDAVLDFLAGEEIDAEEFAN
RLNSLRANYPKQVLYAMMNLLDSHDTPRILTLLGGDKARLKLALALQFTLPGAPCIYYGDEIGLEGGKDP
DNRRPMPWDEEKWDQDLLEFYKKLIALRKEHPALRTGGF
>gnl|CDD|200478 cd11339, AmyAc_bac_CMD_like_2, Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
REETIYFVMTDRFYDGDPSNDNGGGDGDPRSNPTDNGPYHGGDFKGLIDKLDYIKDLGFTAIWITPVVKN
RSVQAGSAGYHGYWGYDFYRIDPHLGTDADLQDLIDAAHARGIKVILDIVVNHTGDLNTENPEVVDYLID
AYKWWIDTGVDGFRIDTVKHVPREFWQEFAPAIRQAAGKPDFFMFGEVYDGDPSYIAPYTTTAGGDSVLD
FPLYGAIRDAFAGGGSGDLLQDLFLSDDLYNDATELVTFLDNHDMGRFLSSLKDGSADGTARLALALALL
FTSRGIPCIYYGTEQGFTGGGDPDNGRRNMFASTGDLTSADDNFDTDHPLYQYIARLNRIRRAY
>gnl|CDD|200479 cd11340, AmyAc_bac_CMD_like_3, Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
SSSDVIYLIMPDRFANGDPSNDSVPGMLEKADRSNPNGRHGGDIQGIIDHLDYLQDLGVTAIWLTPLLEN
DMPSYSYHGYAATDFYRIDPRFGSNEDYKELVSKAHARGMKLIMDMVPNHCGSEHWWMKDLPTKDWINQT
PEYTQTNHRRTALQDPYASQADRKLFLDGWFVPTMPDLNQRNPLVARYLIQNSIWWIEYAGLDGIRVDTY
PYSDKDFMSEWTKAIMEEYPNFNIVGEEWSGNPAIVAYWQKGKKNPDGYDSHLPSVMDFPLQDALRDALN
EEEGWDTGLNRLYETLANDFLYPDPNNLVIFLDNHDTSRFYSQVGEDLDKFKLALALLLTTRGIPQLYYG
TEILMKGTKKKDDGAIRRDFPGGWAGDKVNAFTAAGRTPEQNEAFDFVRKLLNWRKN
>gnl|CDD|200480 cd11341, AmyAc_Pullulanase_LD-like, Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of limit dextrins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
TDAIIYELHVRDFSIDPNSGVKNKRGKFLGFTEEGTTTPTGVSTGLDYLKELGVTHVQLLPVFDFASVDE
DKSRPEDNYNWGYDPVNYNVPEGSYSTDPYDPYARIKEFKEMVQALHKNGIRVIMDVVYNHTYDSENSPF
EKIVPGYYYRYNADGGFSNGSGCGNDTASERPMVRKYIIDSLKYWAKEYKIDGFRFDLMGLHDVETMNEI
REALDKIDPNILLYGEGWDFGTSPLPREEKATQKNAAKMPGIGFFNDRFRDAIKGSVFDDGDGGFVSGNL
GLEDAIKKGIAGNIADFKFDAGFALDPSQSINYVECHDNLTLWDKLQLSNPNESEEERVRRQKLALAIVL
LSQGIPFLHAGQEFLRTKSGDHNSYNSPDEINRIDWSRKENYKDVVDYYKGLIALR
>gnl|CDD|200481 cd11343, AmyAc_Sucrose_phosphorylase-like, Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
ENDVQLITYGDSLGREGEKPLKTLNKFLDEHLKGAIGGVHILPFFPYSSDDGFSVIDYTEVDPRLGDWDD
IEALAEDYDLMFDLVINHISSQSPWFQDFLAGGDPSKDYFIEADPEEDLSKVVRPRTSPLLTEFETAGGT
KHVWTTFSEDQIDLNFRNPEVLLEFLDILLFYAANGARIIRLDAVGYLWKELGTSCFHLPETHEIIKLLR
ALLDALAPGVELLTETNVPHKENISYFGNGDEAHMVYNFALPPLVLHALLSGDATALKHWLKSLPRPSDG
TTYFNFLASHDGIGVRPVEGLLPDEEIDALVETIEERGGLVSYRTAADGNLDPYEINITYYDALGGDDED
EDLQVDRFLAARAIQLFLPGIPAVYYHSLLAGENDLEGVERTGVNRDINRHKYDLEELEEELADPDSLRR
PVVKRLKRLIRFRNEQPAFHPNASQ
>gnl|CDD|200482 cd11344, AmyAc_GlgE_like, Alpha amylase catalytic domain found in GlgE-like proteins. GlgE is a (1,4)-a-D-glucan:phosphate a-D-maltosyltransferase, involved in a-glucan biosynthesis in bacteria. It is also an anti-tuberculosis drug target. GlgE isoform I from Streptomyces coelicolor has the same catalytic and very similar kinetic properties to GlgE from Mycobacterium tuberculosis. GlgE from Streptomyces coelicolor forms a homodimer with each subunit comprising five domains (A, B, C, N, and S) and 2 inserts. Domain A is a catalytic alpha-amylase-type domain that along with domain N, which has a beta-sandwich fold and forms the core of the dimer interface, binds cyclodextrins. Domain A, B, and the 2 inserts define a well conserved donor pocket that binds maltose. Cyclodextrins competitively inhibit the binding of maltooligosaccharides to the S. coelicolor enzyme, indicating that the hydrophobic patch overlaps with the acceptor binding site. This is not the case in M. tuberculosis GlgE because cyclodextrins do not inhibit this enzyme, despite acceptor length specificity being conserved. Domain C is hypothesized to help stabilize domain A and could be involved in substrate binding. Domain S is a helix bundle that is inserted within the N domain and it plays a role in the dimer interface and interacts directly with domain B. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
FSAWYEFFPRSAGADPGRHGTFRDAEARLPRIAAMGFDVLYLPPIHPIGRTNRKGKNNALVAGPGDPGSP
WAIGSEEGGHDAIHPELGTLEDFDRLVAEARELGIEVALDIALQCSPDHPYVKEHPEWFRHRPDGSIQYA
ENPPKKYQDIYPLDFETEDWKGLWQELKRVFLFWIEHGVRIFRVDNPHTKPFPFWEWLIAEVKRDHPDVI
FLSEAFTRPKMMYRLAKLGFTQSYTYFTWRNTKQELTEYLTELTQTEVREYFRPNFWPNTPDILPEYLQF
GGRPAFIIRAVLAATLSSSYGIYGGAYELCENPPRPGKEEYLDSEKYEIKVWDWNAPGNIKPLITRLNRI
RRENP
>gnl|CDD|200483 cd11345, AmyAc_SLC3A2, Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins. 4F2 cell-surface antigen heavy chain (hc) is a protein that in humans is encoded by the SLC3A2 gene. 4F2hc is a multifunctional type II membrane glycoprotein involved in amino acid transport and cell fusion, adhesion, and transformation. It is related to bacterial alpha-glycosidases, but lacks alpha-glycosidase activity. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
APRCKPIPEMNWWNEGPLYQIGDLQAFSEAGGLKGVEGKLDYLSQLKVKGLVLGPIHVVQADQPGELNLT
EIDPDLGTLEDFTSLLTAAHKKGISVVLDLTPNYRGESSWAFSDAENVAEKVKEALEFWLNQGVDGIQVS
DLENVASSASSEWSNLTAIVQKNTDGKKRVLIGVTSSSSLSEISLLLNTSGVDLLLSGALLSASNRPSFG
TLVTQLLSTTGQRSLAWGIGARQGGHLASLVPAALVRLYQLLLFTLPGTPVFNYGDEIGLQDAQGKSPKM
LRPNNEPEIAEEVNANMTAKAQKEDRGSLRSFFRSLSDLRGKERSL
>gnl|CDD|200484 cd11346, AmyAc_plant_IsoA, Alpha amylase catalytic domain family found in plant isoamylases. Two types of debranching enzymes exist in plants: isoamylase-type (EC 3.2.1.68) and a pullulanase-type (EC 3.2.1.41, also known as limit-dextrinase). These efficiently hydrolyze alpha-(1,6)-linkages in amylopectin and pullulan. This group does not contain the conserved catalytic triad present in other alpha-amylase-like proteins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
PLEQLVVYELDVATFTSHRSAQLPPQHAGTFLGVLEKVDHLKSLGVNTVLLQPIFAFARVKGPYYPPSFF
SAPDPYGAGDSSLSASAELRAMVKGLHSNGIEVLLEVVLTHTAEGTDESPESESLRGIDAASYYILGKSG
VLENSGVPGAAVLNCNHPVTQSLILDSLRHWATEFGVDGFCFINAEGLVRGPHGEVLSRPPLLEAIAFDP
VLANTKLIADPSDPLLLPRKAGKFPHWGRWGERNTRYGRDVRQFFRGEPGVLSDFATRLCGSADLFLRSL
LVTLFLSLGIPVINMGDEYGHSSFGSVSSLSSSPRWWALLKSAFGKATTSFISALSALRRRRADLFQ
>gnl|CDD|200485 cd11347, AmyAc_1, Alpha amylase catalytic domain found in an uncharacterized protein family. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
PLLYEINTRVWLYELSRKYGRPVTLADIPDEEFDRLAALGFDYVWLMGVWQRGPYGRAIARSNPGLRAEY
REVLPDLTPDDIIGSPYAITDYTVNPDLGGEDDLAALRERLAARGLKLMLDFVPNHVALDHPWVEEHPEY
FIRGTDEDLARDPANYTYYGGNILAHGRDPYFPPWTDTAQLNYANPATRAAMIETLLKIASQCDGVRCDM
AMLLLNDVFERTWGSRLYGPPSEEFWPEAISAVKARHPDFIFIAEVYWDLEWELQQLGFDYTYDKRLYDR
LRHGDAEVVRYHLSADLDYQSHLVRFIENHDEPRAAAKFGPERHRAAALITLTLPGMRLFHQGQLEGRRK
KLPVHLGRRPEEPVDPDLQAFYRRLLAILRRPVFRGGQWEL
>gnl|CDD|200486 cd11348, AmyAc_2, Alpha amylase catalytic domain found in an uncharacterized protein family. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The catalytic triad (DED) is not present here. The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
VFYEIYPQSFYDSNGDGIGDLQGIISKLDYIKSLGCNAIWLNPCFDSPFKDAGYDVRDYYKVAPRYGTNE
DLVRLFDEAHKRGIHVLLDLVPGHTSDEHPWFKESKKAENNEYSDRYIWTDSIWSGGPGLPFVGGEAERN
GNYIVNFFSCQPALNYGFAHPPTEPWQQPVDAPGPQATREAMKDIMRFWLDKGADGFRVDMADSLVKNDP
GNKETIKLWQEIRAWLDEEYPEAVLVSEWGNPEQSLKAGFDMDFLLHFGGNGYNSLFRNLNTDGGHRRDN
CYFDASGKGDIKPFVDEYLPQYEATKGKGYISLPTCNHDTPRLNARLTEEELKLAFAFLLTMPGVPFIYY
GDEIGMRYIEGLPSKEGGYNRTGSRTPMQWDSGKNAGFSTAPAERLYLPVDPAPDRPTVAAQEDDPNSLL
NFVRDLIAL
>gnl|CDD|200487 cd11349, AmyAc_3, Alpha amylase catalytic domain found in an uncharacterized protein family. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
IIIYQLLPRLFGNKNTTNIPNGTIEENGVGKFNDFDDTALKEIKSLGFTHVWYTGVIRHATQTDYSAYGI
PPDDPDIVKGRAGSPYAIKDYYDVDPDLATDPTNRMEEFEALVERTHAAGLKVIIDFVPNHVARQYHSDA
KPEGVKDFGANDDTSKAFDPSNNFYYLPGEPFVLPFSLNGSPATDGPYHESPAKATGNDCFSAAPSINDW
YETVKLNYGVDYDGGGSFHFDPIPDTWIKMLDILLFWAAKGVDGFRCDMAEMVPVEFWHWAIPEIKARYP
ELIFIAEIYNPGLYRDYLDEGGFDYLYDKVGLYDTLRAVICGGGSASEITVWWQESDDIADHMLYFLENH
DEQRIASPFFAGNAEKALPAMVVSATLSTGPFMLYFGQEVGERGMDAEGFSGDDGRTTIFDYWSVPALQR
WLNGGRFDGGQLTAEEKALRDFYQRLLHLSNDNKAI
>gnl|CDD|200488 cd11350, AmyAc_4, Alpha amylase catalytic domain found in an uncharacterized protein family. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
YVWQHDDFELPAKEDLVIYELLVRDFTERGDFKGVIDKLDYLQDLGVNAIELMPVQEFPGNDSWGYNPRH
YFALDKAYGTPEDLKRLVDECHQRGIAVILDVVYNHAEGQSPLARLYWDYWYNPPPADPPWFNVWGPHFY
YVGYDFNHESPPTRDFVDDVNRYWLEEYHIDGFRFDLTKGFTQKPTGGGAWGGYDAARIDFLKRYADEAK
AVDKDFYVIAEHLPDNPEETELATYGMSLWGNSNYSFSQAAMGYQGGSLLLDYSGDPYQNGGWSPKNAVN
YMESHDEERLMYKLGAYGNGNSYLGINLETALKRLKLAAAFLFTAPGPPMIWQGGEFGYDYSIPEDGRGT
TLPKPIRWDYLYDPERKRLYELYRKLIKLRREHPALRTDN
>gnl|CDD|200489 cd11352, AmyAc_5, Alpha amylase catalytic domain found in an uncharacterized protein family. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
VLYFLLVDRFSDGKERPRPLFDGNDPAVATWEDNFGWESQGQRFQGGTLKGVRSKLGYLKRLGVTALWLS
PVFKQRPELETYHGYGIQNFLDVDPRFGTREDLRDLVDAAHARGIYVILDIILNHSGDVFSYDDDRPYSS
SPGYYRGFPNYPPGGWFIGGDQDALPEWRPDDAIWPAELQNLEYYTRKGRIRNWDGYPEYKEGDFFSLKD
FRTGSGSIPSAALDILARVYQYWIAYADIDGFRIDTVKHMEPGAARYFCNAIKEFAQSIGKDNFFLFGEI
TGGREAAAYEDLDVTGLDAALDIPEIPFKLENVAKGLAPPAEYFQLFENSKLVGMGSHRWYGKFHVTFLD
DHDQVGRFYKKRRAADAAGDAQLAAALALNLFTLGIPCIYYGTEQGLDGSGDSDRYVREAMFGGDFGAFR
SRGRHFFNEEHPIYRRIAALSEL
>gnl|CDD|200490 cd11353, AmyAc_euk_bac_CMD_like, Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is mainly bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
EAVFYHIYPLGFCGAPKENDFDGETEHRILKLEDWIPHLKKLGINAIYFGPVFESDSHGYDTRDYYKIDR
RLGTNEDFKAVCKKLHENGIKVVLDGVFNHVGRDFFAFKDVQENRENSPYKDWFKGVNFDGNSPYNDGFS
YEGWEGHYELVKLNLHNPEVVDYLFDAVRFWIEEFDIDGLRLDVADCLDFDFLRELRDFCKSLKPDFWLM
GEVIHGDYNRWANDEMLDSVTNYECYKGLYSSHNDHNYFEIAHSLNRQFGLEGIYRGKHLYNFVDNHDVN
RIASILKNKEHLPPIYALLFTMPGIPSIYYGSEWGIEGVKGNGSDAALRPALDEPELSGENNELTDLIAK
LARIRRASPALCYGSY
>gnl|CDD|200491 cd11354, AmyAc_bac_CMD_like, Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
HAIWWHVYPLGFVGAPIRPREPEAAVEHRLDRLEPWLDYAVELGCNGLLLGPVFESASHGYDTLDHYRID
PRLGDDEDFDALIAAAHERGLRVLLDGVFNHVGRSHPAVAQALEDGPGSEEDRWHGHAGGGTPAVFEGHE
DLVELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDAAYAVPPEFWARVLPRVRERHPDAWILGEVIHGDYA
GIVAASGMDSVTQYELWKAIWSSIKDRNFFELDWALGRHNEFLDSFVPQTFVGNHDVTRIASQVGDDGAA
LAAAVLFTVPGIPSIYYGDEQGFTGVKEERAGGDDAVRPAFPASPAELAPLGEWIYRLHQDLIGLRRRHP
WLHRART
>gnl|CDD|200492 cd11355, AmyAc_Sucrose_phosphorylase, Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
KNKVQLITYADRLGGNLKDLNTVLDTYFKGVFGGVHILPFFPSSDDRGFDPIDYTEVDPRFGTWDDIEAL
GEDYELMADLMVNHISAQSPYFQDFLAKGDASEYADLFLTYKDFWFPGGPTEEDLDKIYRRRPGAPFTTI
TFADGSTEKVWTTFTEEQIDIDVRSDVGKEYLESILEFLAANGVKLIRLDAFGYAIKKAGTSCFFVEPET
WEFLDELAQIAKPLGIEVLPEIHSHYSIQIKIAEKGDWVYDFALPPLVLHTLYSGDSRRLKHWLEICPRN
QFTVLDTHDGIGVVDVGPGLLPDEEIDALVETIHERGANVSRKYTGAAASNLDLYQVNCTYYSALGRDDD
AYLLARAIQFFAPGIPQVYYVGLLAGENDMELLERTKVGRDINRHYYTLEEIEEALERPVVKRLLRLIRF
RNEHPAFDGDFSV
>gnl|CDD|200493 cd11356, AmyAc_Sucrose_phosphorylase-like_1, Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
WDEKDVVLITYGDSIREEGEKPLQTLHKFLKEHLKDTISGVHILPFFPYSSDDGFSVIDYRQVNPELGDW
EDIEALAKDFRLMFDLVINHVSSSSPWFQQFLAGEPPYKDYFIEADPDTDLSQVVRPRTSPLLTPFETAD
GTKHVWTTFSPDQVDLNFRNPEVLLEFLDILLFYLERGARIIRLDAVAFLWKEPGTTCIHLPQTHEIVKL
LRALLDAVAPGVVLITETNVPHKENISYFGNGDEAHMVYNFALPPLLLHAFLTGDATKLSAWAKSLPPPS
DGTTYFNFLASHDGIGLRPAEGILPEEEIDALVETVEERGGLVSYRRNPDGSQSPYELNITYFDALSGTG
EGSDELQVERFLASQAIMLSLEGVPAIYIHSLLGSRNDYEGVEETGQNRSINREKLDLEELEAELADPDS
LRSKVFKGLKHLLEIRKKQPAFHPNATQFVLDLGPSVF
>gnl|CDD|206766 cd11358, RNase_PH, RNase PH-like 3'-5' exoribonucleases. RNase PH-like 3'-5' exoribonucleases are enzymes that catalyze the 3' to 5' processing and decay of RNA substrates. Evolutionarily related members can be fond in prokaryotes, archaea, and eukaryotes. Bacterial ribonuclease PH contains a single copy of this domain, and removes nucleotide residues following the -CCA terminus of tRNA. Polyribonucleotide nucleotidyltransferase (PNPase) contains two tandem copies of the domain and is involved in mRNA degradation in a 3'-5' direction. Archaeal exosomes contain two individually encoded RNase PH-like 3'-5' exoribonucleases and are required for 3' processing of the 5.8S rRNA. The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits, but it is not a phosphorolytic enzyme per se; it directly associates with Rrp44 and Rrp6, which are hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. All members of the RNase PH-like family form ring structures by oligomerization of six domains or subunits, except for a total of 3 subunits with tandem repeats in the case of PNPase, with a central channel through which the RNA substrate must pass to gain access to the phosphorolytic active sites
FRPVEIETGVLNQADGSALVKLGNTKVICAVTGPIVEPDKLERPDKGTLYVNVEISPGAVGERRQGPPGD
EEMEISRLLERTIEASVILDKSTRKPSWVLYVDIQVLSRDGGLLDACWNAAIAALKDAGIPRVFVDERSP
PLLLMKDLIVAVSVGGISDGVLLLDPTGEEEELADSTLTVAVDKSGKLCLLSKVGGGSLDTEEIKECLEL
AKKRSLHL
>gnl|CDD|200494 cd11359, AmyAc_SLC3A1, Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins. SLC3A1, also called Neutral and basic amino acid transport protein rBAT or NBAT, plays a role in amino acid and cystine absorption. Mutations in the gene encoding SLC3A1 causes cystinuria, an autosomal recessive disorder characterized by the failure of proximal tubules to reabsorb filtered cystine and dibasic amino acids. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase
PWWQTSVIYQIYPRSFKDSNGDGNGDLKGIREKLDYLKYLGVKTVWLSPIYKSPMKDFGYDVSDFTDIDP
MFGTMEDFERLLAAMHDRGMKLIMDFVPNHTSDKHEWFQLSRNSTNPYTDYYIWADCTADGPGTPPNNWV
SVFGNSAWEYDEKRNQCYLHQFLKEQPDLNFRNPDVQQEMDDVLRFWLDKGVDGFRVDAVKHLLEATHLR
DEPQVNPTQPPETQYNYSELYHDYTTNQEGVHDIIRDWRQTMDKYSSEPGRYRFMITEVYDDIDTTMRYY
GTSFKQEADFPFNFYLLDLGANLSGNSINELVESWMSNMPEGKWPNWVLGNHDNSRIASRLGPQYVRAMN
MLLLTLPGTPTTYYGEEIGMEDVDISVDKEKDPYTFESRDPERTPMQWNNSNNAGFSDANKTWLPVNSDY
KTVNVEVQKTDPTSMLNLYRELLLLRSSELALHRGW
>gnl|CDD|206767 cd11362, RNase_PH_bact, Ribonuclease PH. Ribonuclease PH (RNase PH)-like 3'-5' exoribonucleases are enzymes that catalyze the 3' to 5' processing and decay of RNA substrates. Structurally all members of this family form hexameric rings (trimers of dimers). Bacterial RNase PH forms a homohexameric ring, and removes nucleotide residues following the -CCA terminus of tRNA
QLRPISITRGFNKHAEGSVLIEFGDTKVLCTASVEEKVPPFLRGKGKGWVTAEYSMLPRSTHERTQREAS
KGKQSGRTQEIQRLIGRSLRAAVDLEALGERTITIDCDVLQADGGTRTASITGAYVALADAVDKLVEKGV
LEENPLKHFVAAVSVGIVDGEPLLDLDYEEDSAADVDMNVVMTGSGRFVEVQGTGEEAPFSRDELNELLD
LAEKGIQELIELQKEAL
>gnl|CDD|206768 cd11363, RNase_PH_PNPase_1, Polyribonucleotide nucleotidyltransferase, repeat 1. Polyribonucleotide nucleotidyltransferase (PNPase) is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally, all members of this family form hexameric rings. In the case of PNPase the complex is a trimer, since each monomer contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction and in quality control of ribosomal RNA precursors. It is part of the RNA degradosome complex and binds to the scaffolding domain of the endoribonuclease RNase E
KVFEVLVGGRTLTFETGKLAKQADGSVVVQYGDTVVLVTAVSSKKPKEGIDFFPLTVDYREKLYAAGKIP
GGFFKREGRPSEKEILTSRLIDRPIRPLFPKGFRNEVQVIATVLSVDGVNDPDVLAINGASAALSLSDIP
FNGPVGAVRVGRIDGEFVVNPTREELEESDLDLVVAGTKDAVLMVEAGAKEVSEEDMLEAIKFGHEAIQQ
LIAAQEELAAEVGKEKREY
>gnl|CDD|206769 cd11364, RNase_PH_PNPase_2, Polyribonucleotide nucleotidyltransferase, repeat 2. Polyribonucleotide nucleotidyltransferase (PNPase) is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally, all members of this family form hexameric rings. In the case of PNPase the complex is a trimer, since each monomer contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction and in quality control of ribosomal RNA precursors, with the second repeat containing the active site. PNPase is part of the RNA degradosome complex and binds to the scaffolding domain of the endoribonuclease RNase E
EIRPISCEVGLLPRTHGSALFTRGETQVLCTVTLGTLEDAQKIDSLGGEKSKRFMLHYNFPPYSVGETGR
VGGPGRREIGHGALAERALLPVLPSPEDFPYTIRVVSEVLESNGSSSMASVCGGSLALMDAGVPIKAPVA
GIAMGLITEGIDDYRVLTDILGLEDHLGDMDFKVAGTRDGITALQMDIKIPGITLEIMREALQQAKEGRL
HILDIMEKAISEP
>gnl|CDD|206770 cd11365, RNase_PH_archRRP42, RRP42 subunit of archaeal exosome. The RRP42 subunit of the archaeal exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of dimers). In archaea, the ring is formed by three Rrp41:Rrp42 dimers. The central chamber within the ring contains three phosphorolytic active sites located in an Rrp41 pocket at the interface between Rrp42 and Rrp41. The ring is capped by three copies of Rrp4 and/or Csl4 which contain putative RNA interaction domains. The archaeal exosome degrades single-stranded RNA (ssRNA) in the 3'-5' direction, but also can catalyze the reverse reaction of adding nucleoside diphosphates to the 3'-end of RNA which has been shown to lead to the formation of poly-A-rich tails on RNA. It is required for 3' processing of the 5.8S rRNA
PKIKRDYILSLLEKGKRIDGRGLDEYRDIEIETGVIPKAEGSALVKLGNTQVLAGVKLEVGEPFPDTPNE
GVLIVNAELLPLASPTFEPGPPDENAIELARVVDRGIRESKAIDLEKLVIEPGKKVWVVFIDIYVLDYDG
NLFDASALAAVAALLNTKVPEYEVDENEVIEVLGEELPLPVNTLPVSVTVAKIGGYIVVDPTLEEELVMD
ARITITIDEDGNIVALQKGGGGSFTEDEIDKAIDIALEKAAELREK
>gnl|CDD|206771 cd11366, RNase_PH_archRRP41, RRP41 subunit of archaeal exosome. The RRP41 subunit of the archaeal exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of dimers). In archaea, the ring is formed by three Rrp41:Rrp42 dimers. The central chamber within the ring contains three phosphorolytic active sites located in an Rrp41 pocket at the interface between Rrp42 and Rrp41. The ring is capped by three copies of Rrp4 and/or Csl4 which contain putative RNA interaction domains. The archaeal exosome degrades single-stranded RNA (ssRNA) in the 3'-5' direction, but also can catalyze the reverse reaction of adding nucleoside diphosphates to the 3'-end of RNA which has been shown to lead to the formation of poly-A-rich tails on RNA
ELRPIKIEVGVLKNADGSAYVEWGNNKIIAAVYGPREVHPRHLQLPDRAVIRVRYNMAPFSVDERKRPGP
DRREIEISKVIKEALEPAIILEEFPRTAIDVFVEVLQADAGTRVAGLNAASLALADAGIPMRDLVAACAA
GKVDGKIVLDLNKEEDNYGEADMPIAMMPNLGEITLLQLDGDLTPDEFKQAIELAKKGCKRIYELQKEAL
KRKY
>gnl|CDD|206772 cd11367, RNase_PH_RRP42, RRP42 subunit of eukaryotic exosome. The RRP42 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts
KLSEAEKSYIIHGVEQNIRNDGRSRLDYRPIELETGVLSNTNGSARVRLGNTDVLVGVKAEVGSPDPETP
NKGRLEFFVDCSPNASPEFEGRGGEELATELSSALERALKSGSAIDLSKLCIVPGKQCWVLYVDVLVLES
GGNLLDAISIAVKAALFNTRIPKVEVSEDDEGTKEIELSDDPYDVKRLDVSNVPLIVTLSKIGNRHIVDA
TAEEEACSSARLLVAVNAKGRICGVQKSGGGSLEPESIIEMIETAKEVGKKLNAALDKALKE
>gnl|CDD|206773 cd11368, RNase_PH_RRP45, RRP45 subunit of eukaryotic exosome. The RRP45 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts
LSNNEREFILKALKEGLRLDGRGLDEFRPIKITFGLEYGCVEVSLGKTRVLAQVSCEIVEPKPDRPNEGI
LFINVELSPMASPAFEPGRPSEEEVELSRLLERALRDSRAVDTESLCIIAGEKVWSIRVDVHVLNHDGNL
IDAASLAAIAALMHFRRPDVTVDGEEVTVHSPEEREPVPLSIHHIPICVTFAFFDDGEIVVVDPTLLEEA
VADGSLTVALNKHREICALSKSGGAPLSPSQILRCVKIAAAKAKELTEL
>gnl|CDD|206774 cd11369, RNase_PH_RRP43, RRP43 subunit of eukaryotic exosome. The RRP43 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts
KKLHPLEYYRRFLAENVRPDGRELDEFRPTSVNVGSISTADGSALVKLGNTTVLCGIKAEVATPAADTPD
EGYLVPNVDLPPLCSSKFRPGPPSEEAQVLSSFLADILLNSNVLDLEQLCIVPGKLAWVLYCDVYCLDYD
GNLLDAALLALVAALKNLRLPAVTIDEETELVVVNPEERRPLNLKNLPVSTTFAVFDDKHLLADPTAEEE
LLASGLVTVVVDENGELCSVHKPGGSPLSQAQLQECIELAKKRAKELQKLI
>gnl|CDD|206775 cd11370, RNase_PH_RRP41, RRP41 subunit of eukaryotic exosome. The RRP41 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts
GLRLDGRRPNELRRIRCRIGVFSSADGSAYLEQGNTKVLAAVYGPHEPRNRSQALHDRAVVNCEYSMATF
STGERKRRGKGDRRSTELSLAIRQTFEAVILTHLYPRSQIDIYVQVLQADGGLLAACINAATLALIDAGI
PMKDYVCACSAGYLDSTPLLDLNYLEESGDLPDLTVAVLPKSDKVVLLQMESRLHLDRLEKVLELAIEGC
KVIREIMDEVVREHTK
>gnl|CDD|206776 cd11371, RNase_PH_MTR3, MTR3 subunit of eukaryotic exosome. The MTR3 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts
IRPIFLKTGVVSQAKGSAYVELGNTKVICSVYGPRPIPGRTEFSDRGRLNCEVKFAPFATPGRRRHGQDS
EERELSSLLHQALEPAVRLEKYPKSQIDVFVTVLESDGSVLAAAITAASLALADAGIEMYDLVTACSAAL
IGDELLLDPTREEEEASSGGVMLAYMPSLNQVTQLWQSGEMDVDQLEEALDLCIDGCNRIHPVVRQALLE
>gnl|CDD|206777 cd11372, RNase_PH_RRP46, RRP46 subunit of eukaryotic exosome. The RRP46 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts
LRPLSCELGLLSRADGSARFSQGDTSVLAAVYGPIEVKLRKELPDRATLEVIVRPKSGLPGVKEKLLELL
LRSTLEPIILLHLHPRTLISVVLQVLQDDGSLLACAINAACLALLDAGVPMKGLFAAVTCAITEDGEIIL
DPTAEEEKEAKAVATFAFDSGEEKNLVLSESEGSFTEEELFACLELAQAASAAIFDFYR
>gnl|CDD|200603 cd11374, CE4_u10, Putative catalytic domain of uncharacterized bacterial proteins from the carbohydrate esterase 4 superfamily. The family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups of cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily
SRRLLVSVHDVSPATLATVERLLEALDARGVRPVSLLVIPNYHGKWLEADPEFVAWLRDRVAAGDELVLH
GFDHRADRRGGGSHRGHLRLLTRGEAEFAALGEHEARARLTAALRWFKALGLPPKGFVPPAWLMSAGTLA
ALPALGFRYLADRHGVYDLVTGRRILSPGVGFSARSWWRRAVSRAVNRLLRRRLRSGGLVRIAIHPRDLR
HPRLRDDLRELLREAL
>gnl|CDD|213029 cd11375, Peptidase_M54, Peptidase family M54, also called archaemetzincins or archaelysins. Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events
KIYLVPIGSVDPDLLDELKERLSAFFGLPVEVLPSIPVPPLEAYNPSRGQYLADDILDALLKLKPPDADC
VLGVTDVDLYEPGLNFVFGLADGGSGVAVVSTARLRPEFYGLPPDEGLFLERLLKEAVHELGHLFGLDHC
PYYACVMNFSNSLEETDRKPPYLCPVCLRKLQR
>gnl|CDD|271138 cd11376, Imelysin-like, imelysin also called Peptidase M75. This family includes insulin-cleaving membrane protease (imelysin, ICMP), imelysin-like protein (IPPA from Psychrobacter arcticus), iron-regulated protein A (IrpA) and iron-transporter EfeO-like alginate-binding protein (Algp7). Imelysin is a membrane protein with the active site outside the cell envelope. It is also called the peptidase M75 since the HxxE sequence motif characteristic of the M14 peptidase is completely conserved. However, the overall structure and the GxHxxE motif region differ from the known HxxE metallopeptidases, suggesting that imelysin-like proteins may not be peptidases. Imelysin's cleavage of the oxidized insulin B chain shows a preference for aromatic hydrophobic amino acids at P1'. Imelysin was first identified in Pseudomonas aeruginosa and has also been shown to cleave fibrinogen. The tertiary structure shows a fold consisting of two domains, each consisting of a bundle of four helices that are similar to each other, implying an ancient gene duplication and fusion event. In addition to an imelysin-like domain, Algp7 typically contains an N-terminal cupredoxin (CUP) domain and has a deep cleft between the 4-helix bundles sufficiently large to accommodate macromolecules such as alginate polysaccharide
VYPASDYKIYVLPNYKDLVKQTDALTDAVKKGDLAAARDAWAVTRVPYEQAEPFAFGPALFSDLDASIDG
FHRLEYALFAQDSLDAGQCAYLKPVSDKLLSDLKDLEKRWQDLTFKLLVITAESDQGLEKVVNGAASLSE
EVAATKISGPLGLSGAKGHLEDRYSHNSLADFQANIAGIKKAYDGFRPLAILGKNNDPTLDDKVDANLAT
TTAALAAYRTDDGGFEYAKADEADRNELYGAVNTLAEDLSSQR
>gnl|CDD|206778 cd11377, Pro-peptidase_S53, Activation domain of S53 peptidases. Members of this family are found in various subtilase propeptides, such as pro-kumamolysin and tripeptidyl peptidase I, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase
GWVDVGRADPSTPITLTIALKQRNLAELEQLLLEVSDPGSPNYGKFLSPEEVAALFAPSPADVAAVTAWL
ESHGFTITSVAANRDWIVFTGTVAQVEKAFGTSLHVYSHKGSGGTYIRTPGNYSVPASLADHVDFVLGL
>gnl|CDD|211390 cd11378, DUF296, Domain of unknown function found in archaea, bacteria, and plants. This domain is found in proteins that contain AT-hook motifs, which suggests a role in DNA-binding for the proteins as a whole. Three conserved histidine residues appear to form a zinc-binding site, and the domain has been observed to form homotrimers. It co-occurs with a thioredoxin-like domain in uncharacterized cyanobacterial proteins
RPFVLRLEPGEDLVESLEAFAREEGIKAAVLSGIGAVSNATLRYPDPEPKEYETVTFEGRLEILSLSGNI
SPDDGKPSGHLHVSLADSDGRVIGGHLLGALVAGTVEVVIGEL
>gnl|CDD|211391 cd11379, DUF4425, Uncharacterized protein conserved in Bacteroidetes. This family appears to form homodimers, the 3D structure has been determined by both NMR and X-ray crystallography
TGIHKIVIEQSGDTDSFEVSVVFGAANTGGPAKLYDENGEYLGDSYSVSKMAVAKVSCQTGGDAFFMTCA
GSVTSTSEGSGKKLKITVIAYIDGKEVNRLEKEYITKGEILIENFSVST
>gnl|CDD|211392 cd11380, Ribosomal_S8e_like, Eukaryotic/archaeal ribosomal protein S8e and similar proteins. This family contains the eukaryotic/archaeal ribosomal protein S8, a component of the small ribosomal subunits, as well as the NSA2 gene product
PQGKHKRKATGGKFKVVRKKRKYELGRKPANTKLGGERFTRKVRVRGGNIKPRALRLDKANVSHPELGKT
KKLKILGVKKNPSNNEYVRRGVITKGTIIETDVSPLGLVTEEGKVVWGGYAQVTSRPGQDGCVNAVLL
>gnl|CDD|211393 cd11381, NSA2, pre-ribosomal protein NSA2 (Nop seven-associated 2). NSA2 appears to be a protein required for the maturation of 27S pre-rRNA in yeast; it has been characterized in mammalian cells as a nucleolar protein that might play a role in the regulation of the cell cycle and in cell proliferation
NEYIELHRKRHGRRLDHEERKRKKEAREPHKRSKKAQKLRGLKAKLYNKKRYKEKIQMKKTIKMHEERNV
KQKVDDKVPEGAVPAYLLDREGQSRAKVLSNMIKQKRKEKAGKWSVPLPKVRGISEDEMFKVVKTGKRKK
KSWKRMVTKVTFVGEGFTRKPPKYERFIRPMGLRFKKAHVTHPELKATFCLPIIGVKKNPQSPLYTQLGV
ITKGTIIEVNVSELGLVTQGGKVVWGKYAQVTNNPENDGCINAVLLV
>gnl|CDD|211394 cd11382, Ribosomal_S8e, Eukaryotic/archaeal ribosomal protein S8e (RPS8). The eukaryotic/archaeal ribosomal protein S8 is a component of the small (40S in eukaryotes, 30S in archaea) ribosomal subunits and interacts tightly with 18S rRNA (16S rRNA in archaea, presumably)
RQGRHKRKKTGGKRRPYRKKRKYELGRPPANTKLGERRVKTVRVRGGNTKVRALRLDTGNVSWPSEGKTK
KVKILDVVYNPANNELVRRNTLTKGAIIETDRGLARVTSRPGQDGVVNGVLL
>gnl|CDD|206743 cd11383, YfjP, YfjP GTPase. The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain
GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYR
RLLPEADLVLWLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVDPVLAVSARTGWGLDELAEALITAL
>gnl|CDD|206744 cd11384, RagA_like, Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and B. RagA and RagB are closely related Rag GTPases (ras-related GTP-binding protein A and B) that constitute a unique subgroup of the Ras superfamily, and are functional homologs of Saccharomyces cerevisiae Gtr1. These domains function by forming heterodimers with RagC or RagD, and similarly, Gtr1 dimerizes with Gtr2, through the carboxy-terminal segments. They play an essential role in regulating amino acid-induced target of rapamycin complex 1 (TORC1) kinase signaling, exocytic cargo sorting at endosomes, and epigenetic control of gene expression. In response to amino acids, the Rag GTPases guide the TORC1 complex to activate the platform containing Rheb proto-oncogene by driving the relocalization of mTORC1 from discrete locations in the cytoplasm to a late endosomal and/or lysosomal compartment that is Rheb-enriched and contains Rab-7
KVLLMGKSGSGKTSMRSIIFANYLARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDAFMENYFTSQR
DHIFRNVEVLIYVFDVESRELEKDLTYFRSCLEALRQNSPDAKVFVLIHKMDLVQEDEREAVFERKEKEL
RRLSEPLEVTCFPTSIWDETLYKAWSSIVYSLIPNIQVLESNLKKFADICEADEVVLFERATFLVISHSS
RKEASALDPHRFEKISNIIKQFKLSCSKLQASFQSMEVRNSNFSAFIDEFTSNTYIMVVMSDPSIESAAI
LMNIRN
>gnl|CDD|206745 cd11385, RagC_like, Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins C and D. RagC and RagD are closely related Rag GTPases (ras-related GTP-binding protein C and D) that constitute a unique subgroup of the Ras superfamily, and are functional homologs of Saccharomyces cerevisiae Gtr2. These domains form heterodimers with RagA or RagB, and similarly, Gtr2 dimerizes with Gtr1 in order to function. They play an essential role in regulating amino acid-induced target of rapamycin complex 1 (TORC1) kinase signaling, exocytic cargo sorting at endosomes, and epigenetic control of gene expression. In response to amino acids, the Rag GTPases guide the TORC1 complex to activate the platform containing Rheb proto-oncogene by driving the relocalization of mTORC1 from discrete locations in the cytoplasm to a late endosomal and/or lysosomal compartment that is Rheb-enriched and contains Rab-7
RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKITKDDISNSSFVNFQIWDFPGQLDPFDPTLDPEM
IFSGCGALVFVIDAQDDYDEAIARLVETVTKAYKVNPNINFEVFIHKVDGLSEDHKIETQRDIQQRVTDE
LADAGLEDVQISFYLTSIYDHSIFEAFSKVVQKLI
>gnl|CDD|206779 cd11386, MCP_signal, Methyl-accepting chemotaxis protein (MCP), signaling domain. Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW
EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIV
EVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAM
EETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA
>gnl|CDD|381393 cd11387, bHLHzip_USF_MITF, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in USF/MITF family. The USF (upstream stimulatory factor)/MITF (microphthalmia-associated transcription factor) family includes two bHLHzip transcription factor subfamilies. USFs are ubiquitously expressed and key regulators of a wide number of gene regulation networks, including the stress and immune responses, cell cycle and proliferation, lipid and glucid metabolism. USFs recruit chromatin remodeling enzymes and interact with co-activators and the members of the transcription pre-initiation complex. USFs interact with high affinity to E-box regulatory elements. The MITF (also known as microphthalmia-TFE, or MiT) subfamily comprises four genes in mammals (MITF, TFE3, TFEB, and TFEC); each gene has different functions. MITF is involved in neural crest melanocytes development as well as the pigmented retinal epithelium. TFEB is required for vascularization of the mouse placenta. TFE3 is involved in B cell function. TFEC regulates gene expression in macrophages. The MITF subfamily proteins can form homodimers or heterodimers with each other but not with other bHLH or bHLHzip proteins
SHNAVERRRRDNINEKIQELGSLVPPSRLETKDLKPNKGSILSKAVEYIRELQNQNQE
>gnl|CDD|381394 cd11388, bHLH_ScINO2_like, basic helix-loop-helix (bHLH) domain found in Saccharomyces cerevisiae protein INO2 and similar proteins. INO2 is a positive regulatory factor required for depression of the co-regulated phospholipid biosynthetic enzymes in Saccharomyces cerevisiae. It is also involved in the expression of ITR1
PVKKWKHVEAEKKRRNQIKKGFEDLINLINYPRNNNEKRISKSELLNKAVDDIRGLLKANEQLQEEIN
>gnl|CDD|381395 cd11389, bHLH-O_HERP_like, basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES)-related repressor protein (HERP)-like family. The HERP-like family includes bHLH-O transcriptional regulators that are related to the Drosophila hairy and Enhancer-of-split proteins. They contain a basic helix-loop-helix (bHLH) domain with an invariant glycine residue in its basic region, an orange domain in the central region and YXXW sequence motif at its C-terminal region. HERP proteins (HEY1, HEY2 and HEYL) act as downstream effectors of Notch signaling. They are involved in cardiovascular development and have roles in somitogenesis, myogenesis and gliogenesis. Hairy and enhancer of split-related protein HELT is a transcriptional repressor expressed in the developing central nervous system. It binds preferentially to the canonical E box sequence 5'-CACGCG-3' and regulates neuronal differentiation and/or identity. Differentially expressed in chondrocytes proteins, DEC1 and DEC2, are widely expressed in both embryonic and adult tissues and have been implicated in apoptosis, cell proliferation, and circadian rhythms, as well as malignancy in various cancers. Drosophila melanogaster protein clockwork orange (Cwo) is also included in this family. It is involved in the regulation of Drosophila circadian rhythms. It functions as both an activator and a repressor of clock gene expression
HKVIEKRRRDRINESLAELRRLVPEARKSKGSGKLEKAEILEMTLQHLKALQSST
>gnl|CDD|381396 cd11390, bHLH_TS, tissue specific basic helix-loop-helix (bHLH-TS) domain family. Tissue specific bHLH domain family includes transcription regulators whose expression are restricted to certain tissues. They are involved in cell-fate determination and process in neurogenesis, cardiogenesis, myogenesis, and hematopoiesis and include proteins from myogenic regulatory factor (MRF) family, twist-related protein (TWIST) family, scleraxis-like family, heart- and neural crest derivatives-expressed protein (HAND) family, helix-loop-helix protein (HEN) family, musculin-like family, germline alpha (FIGLA) family, T-cell acute lymphocytic leukemia protein/ lymphoblastic leukemia-derived sequence (TAL/LYL) family, ovary, uterus and testis protein (OUT) family, mesoderm posterior protein (Mesp) family, muscle, intestine and stomach expression 1 (MIST-1) family, protein atonal homologs (ATOH) family, neurogenin (NGN) family, neurogenic differentiation factor (NeuroD) family, achaete-scute complex-like (ASCL) family, Fer3-like protein (FERD3L)-like family, and Oligodendrocyte lineage genes (OLIG) family of transcription factors
RNAANARERRRMHDLNDAFEALRKVLPTVPPDKKLSKIETLRLAINYIAALSDLL
>gnl|CDD|381397 cd11391, bHLH_PAS, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain family. bHLH-PAS domain has been found in a large group of bHLH transcription regulators that are involved in gene expression responding to environmental change and controlling aspects of neural development, including proteins from aryl hydrocarbon receptor nuclear translocator (ARNT) family, hypoxia-inducible factor (HIF) family, aryl hydrocarbon receptor (AhR) family, neuronal PAS domain-containing protein (NPAS) family, Circadian locomotor output cycles protein kaput (CLOCK)-like family, and single-minded (SIM) family. bHLH-PAS transcriptional regulatory factors have a bHLH DNA-binding domain followed by two PAS domains and a C-terminal activation or repression domain. bHLH-PAS family members can be divided into class I and class II based on their dimerization partner. bHLH-PAS class I factors include AhR, HIF and SIM. The best characterized bHLH-PAS Class II protein is the ubiquitous ARNT. Some members of bHLH-PAS family act as transcriptional coactivators (such as NCoA) that lack the ability to dimerize and bind DNA
REKSREAAKKRRDKENAEISELASLLPLPPAVGSKLDKLSVLRLAVAYLRLKKFL
>gnl|CDD|381398 cd11392, bHLH_ScPHO4_like, basic helix-loop-helix (bHLH) domain found in Saccharomyces cerevisiae phosphate system positive regulatory protein PHO4 and similar proteins. PHO4 is a transcriptional activator that regulates the expression of repressible phosphatase under phosphate starvation conditions in Saccharomyces cerevisiae. The PHO4 protein has four functional domains with the bHLH domain at its carboxyl-terminal region. It regulates transcription by binding to promoter of the genes as a homodimer
SKRTAHKVAERGRRDRLNAALKELASLMPAEFVEGKMGADGSASDSNDKEKAAASAAGSKAATVEMAIDY
IKHLQKEVEE
>gnl|CDD|381399 cd11393, bHLH_AtbHLH_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana genes coding transcription factors and similar proteins. bHLH proteins are the second largest class of plant transcription factors that regulate transcription of genes that are involve in many essential physiological and developmental process. bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. The Arabidopsis bHLH proteins that have been characterized so far have roles in regulation of fruit dehiscence, cell development (carpel, anther and epidermal), phytochrome signaling, flavonoid biosynthesis, hormone signaling and stress responses
HSIAERKRREKINERIRALRSLVPNGGKTDKASILDEAIEYIKFLQEQVKVLS
>gnl|CDD|381400 cd11394, bHLHzip_SREBP, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein (SREBP) family. The SREBP family includes SREBP1 and SREBP2, which are bHLHzip transcriptional activator of genes encoding proteins essential for cholesterol biosynthesis/uptake and fatty acid biosynthesis. SREBP1 and SREBP2 are principally found in the liver and in adipocytes and made up of an N-terminal transcription factor portion (composed of an activation domain, a bHLHzip domain, and a nuclear localization signal), a hydrophobic region containing two membrane spanning regions, and a C-terminal regulatory segment. They recognize a symmetric sterol regulatory element (TCACNCCAC) instead of E-box
PPKVEKRSAHNAIEKRYRSSINDRIIELKDLVVGPDAKMNKSAVLRKAIDYIRYLQKVNQKLKQENMALK
KAL
>gnl|CDD|381401 cd11395, bHLHzip_SREBP_like, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein (SREBP) family and similar proteins. The SREBP family includes SREBP1 and SREBP2, which are bHLHzip transcriptional activator of genes encoding proteins essential for cholesterol biosynthesis/uptake and fatty acid biosynthesis. SREBP1 and SREBP2 are principally found in the liver and in adipocytes and made up of an N-terminal transcription factor portion (composed of an activation domain, a bHLHzip domain, and a nuclear localization signal), a hydrophobic region containing two membrane spanning regions, and a C-terminal regulatory segment. They recognize a symmetric sterol regulatory element (TCACNCCAC) instead of E-box. The family also includes Saccharomyces cerevisiae transcription factor HMS1 (also termed high-copy MEP suppressor protein 1) and serine-rich protein TYE7. HMS1 is a putative bHLHzip transcription factor involved in exit from mitosis and pseudohyphal differentiation. TYE7, also termed basic-helix-loop-helix protein SGC1, is a putative bHLHzip transcription activator required for Ty1-mediated glycolytic gene expression. TYE7 N-terminal is extremely rich in serine residues. It binds DNA on E-box motifs, 5'-CANNTG-3'. TYE7 is not essential for growth
PRKRLPHNAIEKRYRSNLNTKIERLRDAIPSLRSPEGKSDDGGLGGLAPTTKLSKATILTKAIEYIRHLE
QENERLEEENEELRQQV
>gnl|CDD|381402 cd11396, bHLHzip_USF, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in upstream stimulatory factors, USF1, USF2 and similar proteins. Upstream stimulatory factor 1 and 2 (USF-1 and USF-2) are members of bHLHzip transcription factor family. USFs are ubiquitously expressed and key regulators of a wide number of gene regulation networks, including the stress and immune responses, cell cycle and proliferation, lipid and glucid metabolism. USFs recruit chromatin remodeling enzymes and interact with co-activators and the members of the transcription pre-initiation complex. USFs interact with high affinity to E-box regulatory elements
THNEVERRRRDKINNWIVKLAKIVPDCEKDNSKQGQSKGGILSKACDYIQELRSQNER
>gnl|CDD|381403 cd11397, bHLHzip_MITF_like, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the microphthalmia-associated transcription factor family (MITF) family. The MITF (also known as microphthalmia-TFE, or MiT) family is a small family that contain a basic helix loop helix domain associated with a leucine zipper (bHLHZip). The MITF family comprises four genes in mammals (MITF, TFE3, TFEB, and TFEC); each gene has different functions. MITF is involved in neural crest melanocytes development as well as the pigmented retinal epithelium. TFEB is required for vascularization of the mouse placenta. TFE3 is involved in B cell function. TFEC regulates gene expression in macrophages. The MITF family can form homodimers or heterodimers with each other but not with other bHLH or bHLHzip proteins
KDRQKKDNHNMIERRRRFNINDRIKELGTLLPKSNDPDMRWNKGTILKASVDYIRKLQKEQERLRQLEE
>gnl|CDD|381404 cd11398, bHLHzip_scCBP1, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae centromere-binding protein 1 (CBP-1) and similar proteins. CBP-1, also termed centromere promoter factor 1 (CPF1), or centromere-binding factor 1 (CBF1), is a bHLHzip protein that is required for chromosome stability and methionine prototrophy. It binds as a homodimer to the centromere DNA elements I (CDEI, GTCACATG) region of the centromere that is required for optimal centromere function
EEWHRQRRDNHKEVERRRRENINEGINELAALVPGNAREKNKGAILARAVEYIQELQETEAKNIEKWTLE
KLLTDQAIAELAALNEKLR
>gnl|CDD|381405 cd11399, bHLHzip_scHMS1_like, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae transcription factor HMS1 and similar proteins. HMS1, also termed high-copy MEP suppressor protein 1, is a putative bHLHzip transcription factor involved in exit from mitosis and pseudohyphal differentiation
PSKKTAHNMIEKRYRSNINDRIAELRDSVPALREAYKSARGEDEDEEDLGGLTPATKLNKATILSKATEY
IRHLEKKNKRLSRENASLRERLAAHE
>gnl|CDD|381406 cd11400, bHLHzip_Myc, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family. The Myc family is a member of the bHLHzip family of transcription factors that play important roles in the control of normal cell proliferation, growth, survival and differentiation. All Myc isoforms contain two independently functioning polypeptide chain regions: N-terminal transactivating residues and a C-terminal bHLHzip segment. The bHLHzip family of bHLH transcription factors are characterized by a highly conserved N-terminal basic region that may bind DNA at a consensus hexanucleotide sequence known as the E-box (CANNTG) followed by HLH and leucine zipper motifs that may interact with other proteins to form homo- and heterodimers. Myc heterodimerizes with Max enabling specific binding to E-box DNA sequences in the promoters of target genes. The Myc proto-oncoprotein family includes at least five different functional members: c-, N-, L-, S- and B-Myc (which is lacking the bHLH domain)
KRRLHNVLERQRRNDLKNSFEKLRDLVPELADNEKASKVVILKKATEYIKQLQQEEKKLEKEKDKLKARN
EQLRKKLERL
>gnl|CDD|381407 cd11401, bHLHzip_Mad, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Mad family. Members of the Mad family (Mad1, Mxi, Mad3, and Mad4) bear the bHLHzip domain (also known as basic-helix-loop-helix-leucine-zipper or bHLH-LZ domain), which mediates heterodimerization to Max and the sequence-specific DNA binding ability to E-box DNA. Mad family proteins can repress transcription at the E-box through their interaction with co-repressors. Mad family proteins antagonize Myc function in transactivation and transformation and they are growth/tumor suppressors. The developmental phenotypes of the individual Mad family member knockout mice are relatively mild- all these mice have been shown to be viable and normal
RSTHNELEKNRRAHLRLCLERLKELVPLGPDATRHTTLSLLTKAKAYIKNLEDKEKRQRQQKEQLRREQR
ELKRRL
>gnl|CDD|381408 cd11402, bHLHzip_Mnt, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-binding protein Mnt and similar proteins. Mnt, also termed Class D basic helix-loop-helix protein 3 (bHLHd3), or Myc antagonist MNT, or protein ROX, is a bHLHZip transcriptional repressor that binds DNA as a heterodimer with MAX. It binds to the canonical E box sequence 5'-CACGTG-3' and, with higher affinity, to 5'-CACGCG-3'. Mnt has an important role as an antagonist and regulator of Myc activities and it is a potential tumor suppressor. Mnt is ubiquitously expressed. Mnt-deficient mice shown to exhibit early postnatal lethality
GTREVHNKLEKNRRAHLKECFETLKRQIPNLDDKKTSNLNILRSALRYIQILKRKEKEYEHEMERLAREK
IALQQRL
>gnl|CDD|381409 cd11403, bHLH_scINO4_like, basic Helix-Loop-Helix (bHLH) domain found in Saccharomyces cerevisiae INO4 and similar proteins. INO4 is a bHLH transcriptional activator of phospholipid synthetic genes (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.). It is required for de-repression of phospholipid biosynthetic gene expression in response to inositol deprivation in yeast. INO4 dimerizes with INO2 and binds to an UAS DNA element to control expression of the genes whose expression is inositol-responsive
QKKENHISSEHKRREAIREGFDRLCAIVPALSSSQSRSEAVVYVKTVEYLKELYERRAKLRSQLRSKGVE
I
>gnl|CDD|381410 cd11404, bHLHzip_Mlx_like, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family. Mlx, also termed Class D basic helix-loop-helix protein 13 (bHLHd13), or Max-like bHLHZip protein, or protein BigMax, or transcription factor-like protein 4, is a Max-like bHLHZip transcription regulator that interacts with the Max network of transcription factors. It forms a sequence-specific DNA-binding protein complex with some member of Mad family (Mad1 and Mad4) and Mondo family but not the Myc family and bind the E-box DNA to control transcription. The family also includes Saccharomyces cerevisiae INO4, which is a bHLH transcriptional activator of phospholipid synthetic genes (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.). It is required for de-repression of phospholipid biosynthetic gene expression in response to inositol deprivation in yeast
QRRLNHVRSEKKRRELIKKGYDELCALVPGLDPQKRTKADILQKAADWIQELKEENEKLEEQLDELKEAA
>gnl|CDD|381411 cd11405, bHLHzip_MLXIP_like, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), MLX-interacting protein-like (MLXIPL) and similar proteins. The family includes MLXIP and MLXIPL. MLXIP, also termed Class E basic helix-loop-helix protein 36 (bHLHe36), or transcriptional activator MondoA, is a bHLHZip transcriptional activator that binds DNA as a heterodimer with Mlx. It binds to the canonical E box sequence 5'-CACGTG-3' and plays a role in transcriptional activation of glycolytic target genes. MLXIP is most highly expressed in skeletal muscle and functions as an indirect glucose sensor, by sensing glucose 6-phosphate and shuttling between the nucleus and the cytoplasm. MLXIPL, also termed carbohydrate-responsive element-binding protein (ChREBP), or Class D basic helix-loop-helix protein 14 (bHLHd14), or MLX interactor, or WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), is a bHLHZip transcriptional factor integral to the regulation of glycolysis and lipogenesis in the liver. It forms heterodimers with the bHLHZip protein Mlx to bind the DNA sequence 5'-CACGTG-3'
EQRRLSHISAEQKRRFNIKSGFDTLQSLIPSLGQNPNQKVSKAAMLQKAAEYIKSLKRERQQMQEEAEQL
RQEI
>gnl|CDD|381412 cd11406, bHLHzip_Max, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max and similar proteins. Max, also termed Class D basic helix-loop-helix protein 4 (bHLHd4), or Myc-associated factor X, is a bHLHZip transcription regulator that forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a transcriptional repressor. Max homodimer bind DNA but is transcriptionally inactive. Targeted deletion of max results in early embryonic lethality in mice
KRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILKKATEYIQYMRRKNHTHQQDIDDLKRQN
>gnl|CDD|381413 cd11407, bHLH-O_HERP, basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES)-related repressor protein (HERP) family. HERP (also called Hey/Hesr/HRT/CHF/gridlock) proteins corresponds to a family of bHLH-O transcriptional repressors that are related to the Drosophila hairy and Enhancer-of-split proteins and act as downstream effectors of Notch signaling. They contain a basic helix-loop-helix (bHLH) domain with an invariant glycine residue in its basic region, an orange domain in the central region and YXXW sequence motif at its C-terminal region. HERP proteins are involved in cardiovascular development and have roles in somitogenesis, myogenesis and gliogenesis
RKKRRGIIEKRRRDRINNSLAELRRLVPTAFEKQGSAKLEKAEILQMTVDHLKMLHSKG
>gnl|CDD|381414 cd11408, bHLH-O_HELT, basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split-related protein HELT and similar proteins. HELT, also termed HES/HEY-like transcription factor, is a bHLH-O transcriptional repressor expressed in the developing central nervous system. It binds preferentially to the canonical E box sequence 5'-CACGCG-3' and regulates neuronal differentiation and/or identity. HELT could homodimerize and heterodimerize with other bHLH-O protein such as HES-5 or HEY-2 and bound to E box to repress gene transcription
SHKVIEKRRRDRINRCLNELGKTVPMALAKQTSGKLEKAEILEMTVQYLRALHSAD
>gnl|CDD|381415 cd11409, bHLH-O_DEC, basic helix-loop-helix-orange (bHLH-O) domain found in differentially expressed in chondrocytes protein (DEC) family. The DEC family includes two bHLH-O transcriptional repressors, DEC1 and DEC2, which are widely expressed in both embryonic and adult tissues and have been implicated in apoptosis, cell proliferation, and circadian rhythms, as well as malignancy in various cancers. They mediate the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. They are induced by CLOCK:BMAL1 heterodimer via the CACGTG E-box in the promoter
KETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHLKALTALTEQQQQKII
ALQNG
>gnl|CDD|381416 cd11410, bHLH_O_HES, basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES) family. The HES family includes bHLH-O transcriptional regulators that are related to the Drosophila hairy and Enhancer-of-split (HES) proteins. They contain a basic helix-loop-helix (bHLH) domain with an invariant proline residue in its basic region, an orange domain in the central region and a conserved tetrapeptide motif, WRPW, at its C-terminal region. HES family proteins form heterodimers or homodimers via their HLH domain and bind DNA to repress gene transcription that play an essential role in development of both compartment and boundary cells of the central nervous system
MEKKRRARINKSLEQLKTLVLEALNKDNTRYSKLEKADILEMTVKYLKQLQRSK
>gnl|CDD|381417 cd11411, bHLH_TS_MRF, basic helix-loop-helix (bHLH) domain found in myogenic regulatory factor (MRF) family. MRFs are a family of muscle-specific bHLH transcription proteins (MyoD, Myf5, Mrf4 and MyoG) that plays an essential role in regulating skeletal muscle development and growth. MRFs are capable of binding to E-box motifs as a heterodimer with E-proteins to regulate transcription expression
DRRKAATMRERRRLKKVNEAFEALKRCTSANPNQRLPKVEILRNAIEYIESLQDLL
>gnl|CDD|381418 cd11412, bHLH_TS_TWIST1, basic helix-loop-helix (bHLH) domain found in twist-related protein 1 (TWIST1) and similar proteins. TWIST1, also termed Class A basic helix-loop-helix protein 38 (bHLHa38), or H-twist, is a bHLH transcriptional regulator that inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. It also represses expression of proinflammatory cytokines such as TNFA and IL1B. In addition, TWIST1 is involved in cancer development and progression
GSPQSFEELQTQRVMANVRERQRTQSLNEAFAALRKIIPTLPSDKLSKIQTLKLAARYIDFLYQVLQSDE
LDSKMAS
>gnl|CDD|381419 cd11413, bHLH_TS_TAL_LYL, basic helix-loop-helix (bHLH) domain found in T-cell acute lymphocytic leukemia protein/ lymphoblastic leukemia-derived sequence (TAL/LYL) family. The TAL/LYL family includes a group of bHLH transcription factors (TAL1, TAL2 and LYL1) implicated in T cell acute leukaemia. They act as mediators of T cell leukaemogenesis. TAL-1, also termed Class A basic helix-loop-helix protein 17 (bHLHa17), or stem cell protein (SCL), or T-cell leukemia/lymphoma protein 5, is a hematopoietic-specific bHLH transcription factor that functions in embryonic and adult hematopoiesis in vertebrates. It is also required for embryonic vascular remodeling. It acts as a regulator of erythroid differentiation and binds to regulatory regions of a large cohort of erythroid genes as part of a complex with GATA-1, LMO2 and Ldb1. TAL-2, also termed Class A basic helix-loop-helix protein 19 (bHLHa19), is a bHLH transcription factor essential for the normal brain development. Lyl-1, also termed Class A basic helix-loop-helix protein 18 (bHLHa18), or lymphoblastic leukemia-derived sequence 1, is a proto-oncogenic bHLH transcription factor that plays an important role in hematopoietic stem cell function and is required for the late stages of postnatal angiogenesis to limit the formation of new blood vessels, notably by regulating the activity of the small GTPase Rap1. LYL-1 deficiency induces a stress erythropoiesis
RRIFTNTRERWRQQNVNGAFAELRKLIPTHPPDKKLSKNEILRLAMKYIKFLEKILEDQE
>gnl|CDD|381420 cd11414, bHLH_TS_HEN, basic helix-loop-helix (bHLH) domain found in helix-loop-helix protein (HEN) family. The HEN family includes two neuron-specific bHLH transcription factors, HEN-1 (also known as Nhlh1 or bHLHa35 or NSCL-1) and HEN-2 (also known as Nhlh2 or bHLHa34 or NSCL-2). They may serve as DNA-binding protein that is involved in the control of cell-type determination, possibly within the developing nervous system
KYRNAHATRERIRVEAFNSAFAQLRKLLPTLPPDKKLSKIEILRLAICYISYLNHVL
>gnl|CDD|381421 cd11415, bHLH_TS_FERD3L_NATO3, basic helix-loop-helix (bHLH) domain found in Fer3-like protein (FERD3L) and similar proteins. FERD3L, also termed basic helix-loop-helix protein N-twist, or Class A basic helix-loop-helix protein 31 (bHLHa31), or nephew of atonal 3 (NATO3), or Neuronal twist (NTWIST), is a bHLH transcription factor expressed in the developing central nervous system (CNS). It regulates floor plate (FP) cells development. FP is a critical organizing center located at the ventral-most midline of the neural tube. FERD3L binds to the E-box and functions as inhibitor of transcription
RKRVITYAQRQAANIRERRRMFNLNEAFDKLRKKVPTFAYEKRLSRIETLRLAIVYISFMTDLL
>gnl|CDD|381422 cd11416, bHLH_TS_ceHLH13_like, basic helix-loop-helix (bHLH) domain found in Caenorhabditis elegans Helix-loop-helix protein 13 (HLH13) and similar proteins. Caenorhabditis elegans HLH13, also termed Fer3-like protein, or nephew of atonal 3, is a bHLH transcription factor that plays a role in the negative regulation of exit from L1 arrest and dauer diapause dependent on IIS signaling (insulin and insulin-like growth factor (IGF) signaling)
PYKVQRHAANIRERKRMLSINSAFEELRCHVPTFPYEKRLSKIDTLRLAIAYIALLRDILRSG
>gnl|CDD|381423 cd11417, bHLH_TS_PTF1A, basic helix-loop-helix (bHLH) domain found in pancreas transcription factor 1 subunit alpha (PTF1A) and similar proteins. PTF1A, also termed Class A basic helix-loop-helix protein 29 (bHLHa29), or pancreas-specific transcription factor 1a, or bHLH transcription factor p48, or p48 DNA-binding subunit of transcription factor PTF1 (PTF1-p48), is a bHLH transcription factor implicated in the cell fate determination in various organs. It binds to the E-box consensus sequence 5'-CANNTG-3' and plays a role in early and late pancreas development and differentiation
QRQAANLRERRRMQSINDAFEGLRSHIPTLPYEKRLSKVDTLRLAIGYINFLSELV
>gnl|CDD|381424 cd11418, bHLH_TS_ASCL, basic helix-loop-helix (bHLH) domain found in achaete-scute complex-like (ASCL) family. The achaete-scute complex-like (ASCL, also known as achaete-scute complex homolog or ASH) family of bHLH transcription factors, ASCL1-5, have been implicated in cell fate specification and differentiation. They are critical for proper development of the nervous system. The deregulation of ASCL plays a key role in psychiatric and neurological disorders. ASCL-1, also termed Class A basic helix-loop-helix protein 46 (bHLHa46), or achaete-scute homolog 1 (ASH-1), or mammalian achaete-scute homolog 1 (Mash1), is a neural-specific bHLH transcription factor that is expressed in subsets of neural progenitors in both the central and peripheral nervous system. It plays a key role in neuronal differentiation and specification in the nervous system. ASCL-2, also termed achaete-scute homolog 2 (ASH-2), or Class A basic helix-loop-helix protein 45 (bHLHa45), or mammalian achaete-scute homolog 2 (Mash2), is a bHLH transcription factor that is involved in Schwann cell differentiation and control of proliferation in adult peripheral nerves. ASCL-3, also termed Class A basic helix-loop-helix protein 42 (bHLHa42), or bHLH transcriptional regulator Sgn-1, or achaete-scute homolog 3 (ASH-3), is a bHLH transcription factor specifically localized in the duct cells of the salivary glands. It may act as transcriptional repressor that inhibits myogenesis. The family also includes Drosophila melanogaster achaete-scute complex (AS-C) proteins, which consists of lethal of scute (also known as achaete-scute complex protein T3 or AST3), scute (also known as achaete-scute complex protein T4 or AST4), achaete (also known as achaete-scute complex protein T5 or AST5), and asense (also known as achaete-scute complex protein T8 or AST8). They are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system, as well as in sex determination and dosage compensation
RVARRNERERRRVQAVNDAFDRLRQHVPYLKRRKKLSKVKTLRRAIEYIRHLQKLL
>gnl|CDD|381425 cd11419, bHLHzip_TFAP4, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor AP-4 (TFAP4) and similar proteins. TFAP4, also termed activating enhancer-binding protein 4, or Class C basic helix-loop-helix protein 41 (bHLHc41), is a bHLHzip transcription factor that activates both viral and cellular genes involved in the regulation of cellular proliferation, stemness, and epithelial-mesenchymal transition by binding to the symmetrical DNA sequence 5'-CAGCTG-3'
RRIRREIANSNERRRMQSINAGFQSLRTLLPHCDGEKLSKAAILQQTAEYIFSLEQEKTRL
>gnl|CDD|381426 cd11420, bHLH_E-protein, basic helix-loop-helix (bHLH) domain found in E proteins family. The E proteins family corresponds to class I bHLH proteins, which are widely expressed within the immune system and on which the majority of this chapter will be focused. Members in this family include E2A (also referred to as TCF-3), E47, TCF-12 (also referred to as HEB), and TCF-4 (also referred to as E2-2) in vertebrates, as well as the E protein ortholog, Daughterless (Da), from Drosophila melanogaster. E-proteins are expressed broadly and in certain complexes they are restricted to specific cell types. E-proteins homodimerize and heterodimerize with the tissue specific bHLH factors to bind DNA and regulate transcription and differentiation of cells during development. The activity of the E-proteins is regulated by two main mechanisms: first, the relative concentrations of E-proteins, tissue specific bHLH factors, and the Id proteins, and second, covalent modification
ERIRVRDINEAFKELGRMCQLHLKSDKPQTKLLILHQAVSVITSLEQ
>gnl|CDD|381427 cd11421, bHLH_TS_ATOH8, basic helix-loop-helix (bHLH) domain found in protein atonal homolog 8 (ATOH8) and similar proteins. ATOH8, also termed Class A basic helix-loop-helix protein 21 (bHLHa21), or helix-loop-helix protein hATH-6 (hATH6), is a bHLH shear-stress-responsive transcription factor expressed in activated satellite cells and proliferating myoblasts of human skeletal muscle tissue. It regulates endothelial cell proliferation, migration and tube-like structures formation. ATOH8 binds a palindromic (canonical) core consensus DNA sequence 5'-CANNTG- 3' known as an E-box element, possibly as a heterodimer with other bHLH proteins
YKNMTRQRRIEANARERTRVHTISAAFEALRKAVPSYSYNQKLSKLAILRIACSYILALARLADLDYS
>gnl|CDD|381428 cd11422, bHLH_TS_FIGLA, basic helix-loop-helix (bHLH) domain found in factor in the germline alpha (FIGLA) and similar proteins. FIGLA, also termed FIGalpha, or Class C basic helix-loop-helix protein 8 (bHLHc8), or folliculogenesis-specific basic helix-loop-helix protein, or transcription factor FIGa, is a germ-cell-specific bHLH transcription factor expressed abundantly in female and less so in male germ cells. It is essential for primordial follicle formation and expression of many genes required for folliculogenesis, fertilization and early embryonic survival. FIGLA knockout mice cannot form primordial follicles and lose oocytes rapidly after birth, whereas male gonads are unaffected
RRVANARERERVRNLNSGFSKLRRIVPLIPRDRKPSKVDTLKGATEYIRLLQRILE
>gnl|CDD|381429 cd11423, bHLH_TS_musculin_like, basic helix-loop-helix (bHLH) domain found in musculin, transcription factor 21 (TCF-21) and similar proteins. The family includes two bHLH transcription factors, musculin and transcription factor 21 (TCF-21). Musculin, also termed activated B-cell factor 1 (ABF-1), or Class A basic helix-loop-helix protein 22 (bHLHa22), is a bHLH transcription factor expressed in activated B lymphocytes. It acts as a transcription repressor capable of inhibiting the transactivation capability of TCF3/E47. Musculin may play a role in regulating antigen-dependent B-cell differentiation. The mouse homolog, musculin, is suggested to be a repressor of myogenesis that is expressed in developing muscle and in the spleen. TCF-21, also termed capsulin, or Class A basic helix-loop-helix protein 23 (bHLHa23), or epicardin, or podocyte-expressed 1 (Pod-1), is a bHLH transcription factor expressed specifically in mesodermally-derived cells that surround the epithelium of the developing gastrointestinal, genitourinary and respiratory systems during mouse embryogenesis. It may play a role in the specification or differentiation of one or more subsets of epicardial cell types
QRNAANARERARMRVLSKAFSRLKTTLPWVPPDTKLSKLDTLRLAASYIAHLRQIL
>gnl|CDD|381430 cd11424, bHLH_TS_OUT, basic helix-loop-helix (bHLH) domain found in ovary, uterus and testis protein (OUT) family. The OUT family includes transcription factor 23 (TCF-23), transcription factor 24 (TCF-24) and similar proteins. TCF-23, also termed Class A basic helix-loop-helix protein 24 (bHLHa24), is a bHLH transcription factor that is essential for progesterone-dependent decidualization. The mouse homolog is also called ovary, uterus and testis protein (OUT), which is expressed predominantly in the reproductive organs such as the uterus, ovary and testis. It shows an Id-like inhibitory activity and functions as a negative regulator of bHLH factors through the formation of a functionally inactive heterodimeric complex. OUT inhibits the formation of TCF3 and MYOD1 homodimers and heterodimers, but lacks DNA binding activity. OUT is involved in the regulation or modulation of smooth muscle contraction of the uterus during pregnancy and particularly around the time of delivery. It also plays a role in the inhibition of myogenesis. Unlike typical bHLH factors, OUT proteins do not bind E-box (CANNTG) or N-box DNA sequences and inhibit DNA binding of homo- and heterodimers consisting of E12 and MyoD in gel mobility shift assays. TCF-24 is an uncharacterized bHLH transcription factor that shows high sequence similarity with TCF-23
AAGNAARERSRVRTLRTAFQSLQRALPAVPPDTKLSKLDVLLLASRYIAHLTRKL
>gnl|CDD|381431 cd11425, bHLH_TS_Mesp_like, basic helix-loop-helix (bHLH) domain found in mesoderm posterior protein (Mesp) family. Mesp, a bHLH tissue specific transcription factor, acts as a key regulator of the cardiovascular transcriptional network by inducing directly and/or indirectly the expression of the majority of key cardiovascular transcription factors. The Mesp family includes two bHLH transcription factors, Mesp1 and Mesp2. Mesp1, also termed Class C basic helix-loop-helix protein 5 (bHLHc5), promotes cardiovascular differentiation during embryonic development and embryonic stem cell differentiation. Mesp2, also termed Class C basic helix-loop-helix protein 6 (bHLHc6), plays an important role in somitogenesis. The family also includes mesogenin-1 (Msgn1) and similar proteins. Msgn1, also termed paraxial mesoderm-specific mesogenin1, or pMesogenin1 (pMsgn1), is a bHLH transcription factor required for maturation and segmentation of paraxial mesoderm. It may regulate the expression of T-box transcription factors essential for mesoderm formation and differentiation
QRQLANERERLRMRTLADALGELRQHLPPSVAPKGKRLSKIQTLKYAIRYIGYLGNVLQ
>gnl|CDD|381432 cd11426, bHLH_TS_MIST1_like, basic helix-loop-helix (bHLH) domain found in muscle, intestine and stomach expression 1 (MIST-1) family. MIST-1, also termed Class A basic helix-loop-helix protein 15 (bHLHa15), or Class B basic helix-loop-helix protein 8 (bHLHb8), is a bHLH transcription factor expressed in pancreatic acinar cells and other serous exocrine cells. It is essential for cytoskeletal organization and secretory activity. It also functions as a potent endoplasmic reticulum (ER) stress-inducible transcriptional regulator. MIST-1 is capable of binding to E-box (CANNTG) motifs as a homodimer or a heterodimer with E-proteins (E12 and E47) to regulate transcription. The family also includes Drosophila melanogaster protein dimmed and similar proteins. Dimmed, also termed DIMM, is a bHLH transcription factor that regulates neurosecretory (NS) cell function and neuroendocrine cell fate in Drosophila
RRLESNERERLRMHQLNDAFQALREVIPHVRSERKLSKIETLTLAKNYIKSLTNMI
>gnl|CDD|381433 cd11427, bHLH_TS_NeuroD, basic helix-loop-helix (bHLH) domain found in neurogenic differentiation factor (NeuroD) family. The NeuroD family includes NeuroD1, NeuroD2, NeuroD4 and NeuroD6. NeuroD1, also termed Class A basic helix-loop-helix protein 3 (bHLHa3), is a neuronal bHLH transcription factor involved in the development and maintenance of the endocrine pancreas and neuronal elements. It acts as an essential regulator of glutamatergic neuronal differentiation. Loss of NeuroD1 causes ataxia, cerebellar hypoplasia, sensorineural deafness, and severe retinal dystrophy in mice. NeuroD2, also termed Class A basic helix-loop-helix protein 1 (bHLHa1), or NeuroD-related factor (NDRF), is a neuronal calcium-dependent bHLH transcription factor that induces neuronal differentiation and promotes neuronal survival. It plays a central role in thalamocortical synaptic maturation. NeuroD2 mediates calcium-dependent transcription activation by binding to E box-containing promoter. NeuroD4, also termed Class A basic helix-loop-helix protein 4 (bHLHa4), or protein atonal homolog 3 (ATH-3), or Atoh3, or Math-3, is a bHLH transcriptional activator that mediates neuronal differentiation. NeuroD6, also termed Class A basic helix-loop-helix protein 2 (bHLHa2), or protein atonal homolog 2 (ATH-2), or Atoh2, or Math2, or Nex1, is a neurogenic bHLH transcription factor involved in neuronal development, differentiation, and survival in Alzheimer's disease (AD) brains of both cohorts. It plays an integrative role in coordinating increase in mitochondrial mass with cytoskeletal remodeling, suggesting that it may act as a co-regulator of neuronal differentiation and energy metabolism
RVKANARERNRMHGLNDALDNLRKVVPCYSKTQKLSKIETLRLARNYIWALSEIL
>gnl|CDD|381434 cd11428, bHLH_TS_NGN, basic helix-loop-helix (bHLH) domain found in neurogenin (NGN) family. The NGN family includes three neural-specific bHLH transcription factors, NGN1-3, which may function at neuroblast selection genes during the development of several neuronal lineages. NGN-1, also termed Class A basic helix-loop-helix protein 6 (bHLHa6), or neurogenic basic-helix-loop-helix protein, or neurogenic differentiation factor 3 (NeuroD3), is a neural-specific bHLH transcription factor involved in the initiation of neuronal differentiation. NGN-2, also termed Class A basic helix-loop-helix protein 8 (bHLHa8), or protein atonal homolog 4 (ATOH4), is a neural-specific bHLH transcription factor required for sensory neurogenesis. NGN-3, also termed Class A basic helix-loop-helix protein 7 (bHLHa7), or protein atonal homolog 5 (ATOH5), is a neural-specific bHLH transcription factor expressed in the developing central nervous system and the embryonic pancreas. It is involved in neurogenesis and plays an important role in spermatogenesis
RRLKANDRERNRMHNLNDALDALREVLPSFPDETKLTKIETLRFAHNYIWALSETLK
>gnl|CDD|381435 cd11429, bHLH_TS_OLIG, basic helix-loop-helix (bHLH) domain found in Oligodendrocyte lineage genes (OLIG) family of transcription factors. The OLIG family includes three bHLH transcription factors, Oligo1-3, which are expressed in both the developing and mature central nervous system. Oligo1 and Oligo2 are expressed in a nervous tissue-specific manner, but Oligo3 is found mainly in non-neural tissues. Oligo (also known as Olig) have key roles in the specification of motor neurons, dorsal interneurons, and oligodendrocytes. Oligo1, also termed Class B basic helix-loop-helix protein 6 (bHLHb6), or Class E basic helix-loop-helix protein 21 (bHLHe21), promotes formation and maturation of oligodendrocytes, especially within the brain. Oligo2, also termed Class B basic helix-loop-helix protein 1 (bHLHb1), or Class E basic helix-loop-helix protein 19 (bHLHe19), or protein kinase C-binding protein 2, or protein kinase C-binding protein RACK17, is required for oligodendrocyte and motor neuron specification in the spinal cord, as well as for the development of somatic motor neurons in the hindbrain. It cooperates with OLIG1 to establish the MN progenitors (pMN) domain of the embryonic neural tube. Oligo3, also termed Class B basic helix-loop-helix protein 7 (bHLHb7), or Class E basic helix-loop-helix protein 20 (bHLHe20), is expressed in the ventricular zone of the dorsal alar plate of the hindbrain and involved in regulating the development of dorsal and ventral spinal cord. It may determine the distinct specification program of class A neurons in the dorsal part of the spinal cord and suppress specification of class B neurons. This family also includes two OLIG-related bHLH transcription factors, bHLHe22 and bHLHe23. bHLHe22, also termed Class B basic helix-loop-helix protein 5 (bHLHb5), or trinucleotide repeat-containing gene 20 protein, is a neural-specific transcriptional repressor that is expressed in both excitatory (unipolar brush cells) and inhibitory neurons (cartwheel cells) of the dorsal cochlear nucleus (DCN) during development. It is important for the proper development and/or survival of a number of neural cell types. bHLHe23, also termed Class B basic helix-loop-helix protein 4 (bHLHb4), is expressed in rod bipolar cells and is required for rod bipolar cell maturation. bHLHe23 have roles in spinal interneuron differentiation by mechanisms linked to the Notch signaling pathway. It modulates the expression of genes required for the differentiation and/or maintenance of pancreatic and neuronal cell types
RLKINSRERKRMHDLNSALDGLRSVMPYAQGPSVRKLSKIATLLLARNYILMLTQALEELR
>gnl|CDD|381436 cd11430, bHLH_TS_ATOH1_like, basic helix-loop-helix (bHLH) domain found in protein atonal homologs ATOH1, ATOH7 and similar proteins. The family includes ATOH1 and ATOH7. ATOH1, also termed Class A basic helix-loop-helix protein 14 (bHLHa14), or helix-loop-helix protein hATH-1 (hATH1), or Math1, or Cath1, is a proneural bHLH transcription factor that is essential for inner ear hair cell differentiation. It dimerizes with E47 and activates E-box (CANNTG) dependent transcription. ATOH1 is a mammalian homolog of the Drosophila melanogaster gene atonal and mouse atonal homolog 1 (Math1). ATOH7, also termed Class A basic helix-loop-helix protein 13 (bHLHa13), or helix-loop-helix protein hATH-5 (hATH5), or Math5, is a bHLH transcription factor involved in the differentiation of retinal ganglion cells. The family also includes protein Amos (also termed absent MD neurons and olfactory sensilla protein, or reduced olfactory organs protein, or rough eye protein). It is a bHLH transcription factor that promotes multiple dendritic neuron formation in the Drosophila peripheral nervous system
RRLAANARERRRMNGLNRAFDQLRSVVPSIGNDKKLSKYETLQMAQIYIETLSELL
>gnl|CDD|381437 cd11431, bHLH_TS_taxi_Dei, basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster protein taxi and similar proteins. Protein taxi, also termed protein delilah (Dei), is a bHLH transcription factor that is involved in regulation of cell adhesion and attachment that is expressed in specialized cells that provide anchoring sites to either muscles (tendon cells), or proprioceptors (chordotonal attachment cells) during embryonic development. It probably plays an important role in the differentiation of epidermal cells into the tendon cells that form the attachment sites for all muscles
RRKTANARERDRMREINDAFEALRRAVPEYPVAGKDGKLTKITTLRLAMNYIKALTDLL
>gnl|CDD|381438 cd11432, bHLH-PAS_NPAS1_3_like, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing proteins, NPAS1, NPAS3 and similar proteins. The family includes neuronal PAS domain proteins NPAS1 and NPAS3, both of which are master regulators of neuropsychiatric function. NPAS1, also termed neuronal PAS1, or Basic-helix-loop-helix-PAS protein MOP5, or Class E basic helix-loop-helix protein 11 (bHLHe11), or member of PAS protein 5, or PAS domain-containing protein 5 (PASD5), is a bHLH-PAS transcriptional repressor expressed in the central nervous system and involved in neuronal differentiation. It is active during late embryogenesis and postnatal development. NPAS3, also termed neuronal PAS3, or Basic-helix-loop-helix-PAS protein MOP6, or Class E basic helix-loop-helix protein 12 (bHLHe12), or member of PAS protein 6, or PAS domain-containing protein 6 (PASD6), is a bHLH-PAS brain-enriched transcription factor that is involved in central nervous system development and neurogenesis. It is a replicated genetic risk factor for psychiatric disorders. Human chromosomal rearrangements that affect NPAS3 normal expression are associated with schizophrenia and mental retardation
KEKSRNAARSRRGKENYEFYELAKLLPLPAAISSQLDKASIVRLTISYLKLRDFM
>gnl|CDD|381439 cd11433, bHLH-PAS_HIF, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor (HIF) family. The HIF family contains bHLH-PAS transcription regulators involved in oxygen homeostasis, including HIF1a, HIF2a, and HIF3a. They have been implicated in development, postnatal physiology as well as disease pathogenesis. HIF1a, also termed HIF-1-alpha, or HIF1-alpha, or ARNT-interacting protein, or Basic-helix-loop-helix-PAS protein MOP1, or Class E basic helix-loop-helix protein 78 (bHLHe78), or Member of PAS protein 1, or PAS domain-containing protein 8 (PASD8), functions as a master transcriptional regulator of the adaptive response to hypoxia. HIF2a, also termed HIF-2-alpha, or HIF2-alpha, or endothelial PAS domain-containing protein 1 (EPAS-1), or Basic-helix-loop-helix-PAS protein MOP2, or Class E basic helix-loop-helix protein 73 (bHLHe73), or Member of PAS protein 2, or PAS domain-containing protein 2 (PASD2), or HIF-1-alpha-like factor (HLF), is a bHLH-PAS transcription factor involved in the induction of oxygen regulated genes. HIF3a, also termed HIF-3-alpha, or HIF3-alpha, or endothelial PAS domain-containing protein 1 (EPAS-1), or Basic-helix-loop-helix-PAS protein MOP7, or Class E basic helix-loop-helix protein 17 (bHLHe17), or Member of PAS protein 7, or PAS domain-containing protein 7 (PASD7), or HIF3-alpha-1, or inhibitory PAS domain protein (IPAS), is a bHLH-PAS transcriptional regulator in adaptive response to low oxygen tension. It plays a role in the regulation of hypoxia-inducible gene expression
RKEKSRDAARCRRGKESEIFYELAHQLPLPHSVSSQLDKASIMRLTISYLKLRKLLSA
>gnl|CDD|381440 cd11434, bHLH-PAS_SIM, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in single-minded (SIM) family. The SIM family includes Drosophila melanogaster protein SIM and its homologs from vertebrates, single-minded homolog 1 (SIM1) and single-minded homolog 2 (SIM2). SIM is a nuclear bHLH-PAS transcription factor that functions as a master developmental regulator controlling midline development of the ventral nerve cord in Drosophila. SIM1, also termed Class E basic helix-loop-helix protein 14 (bHLHe14), is a bHLH-PAS transcription factor that may have pleiotropic effects during embryogenesis and in the adult. SIM2, also termed Class E basic helix-loop-helix protein 15 (bHLHe15), is a bHLH-PAS transcription factor that may be a master gene of central nervous system (CNS) development in cooperation with ARNT. It may have pleiotropic effects in the tissues expressed during development
MKEKSKNAARTRREKENAEFYELAKLLPLPSAITSQLDKASIIRLTTSYLKMRAVFPEGLG
>gnl|CDD|381441 cd11435, bHLH-PAS_AhRR, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor repressor (AhRR) and similar proteins. AhRR, also termed AhR repressor, or Class E basic helix-loop-helix protein 77 (bHLHe77), is a member of bHLH-PAS transcription factors that acts as a negative regulator of AhR (or Dioxin Receptor), playing key roles in development and environmental sensing. AhR is activated by Dioxin to control the expression of certain genes to influence biological processes such as apoptosis, proliferation, cell growth and differentiation. To form active DNA binding complexes, AhR dimerizes with a bHLH-PAS factor ARNT (Aryl hydrocarbon Nuclear Receptor Translocator). AhRR functions by competing with AhR for its partner ARNT. AhRR-ARNT complexes are transcriptionally inactive
GSEKSNPSKRHRDRLNAELDHLASLLPFPPDIISKLDKLSVLRLSVSYLRVKSFFQAIQE
>gnl|CDD|381442 cd11436, bHLH-PAS_AhR, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor (AhR) and similar proteins. AhR, also termed Ah receptor, or Dioxin receptor (DR), or Class E basic helix-loop-helix protein 76 (bHLHe76), is the only member of bHLH-PAS transcription regulators that bind and be activated by small chemical ligands. It is activated by Dioxin to control the expression of certain genes to influence biological processes such as apoptosis, proliferation, cell growth and differentiation. To form active DNA binding complexes AhR dimerize with a bHLH-PAS factor ARNT (Aryl hydrocarbon Nuclear Receptor Translocator)
AEGVKSNPSKRHRDRLNTELDRLASLLPFPQDVISKLDKLSVLRLSVSYLRAKSFFDVALK
>gnl|CDD|381443 cd11437, bHLH-PAS_ARNT_like, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator (ARNT) family. The ARNT family of bHLH-PAS transcription regulators includes ARNT, ARNT-like proteins (ARNTL and ARNTL2), and Drosophila melanogaster protein cycle. They act as the heterodimeric partner for bHLH-PAS proteins such as aryl hydrocarbon receptor (AhR), hypoxia-inducible factor (HIF), and single-minded (SIM). These bHLH-PAS transcription complexes are involved in transcriptional responses to xenobiotic, hypoxia, and developmental pathways. Heterodimerization of bHLH-PAS proteins with ARNT is mediated by contacts between both the bHLH and the tandem PAS domains. ARNT use bHLH and/or PAS domains to interact with several transcriptional coactivators. It is required for activity of the aryl hydrocarbon (dioxin) receptor. ARNTL, also termed Basic-helix-loop-helix-PAS protein MOP3, or brain and muscle ARNT-like 1 (BMAL1), or Class E basic helix-loop-helix protein 5 (bHLHe5), or member of PAS protein 3, or PAS domain-containing protein 3 (PASD3), or bHLH-PAS protein JAP3, is a member of the bHLH-PAS transcription factor family that forms heterodimers with another bHLH-PAS protein, CLOCK (circadian locomotor output cycle kaput), which regulates circadian rhythm. ARNTL-CLOCK heterodimer complex activates transcription from E-box (CANNTG) elements found in the promoter of circadian responsive genes. ARNTL is highly homologous to ARNT. ARNTL2, also termed Basic-helix-loop-helix-PAS protein MOP9, or brain and muscle ARNT-like 2 (BMAL2), or CYCLE-like factor (CLIF), or Class E basic helix-loop-helix protein 6 (bHLHe6), or member of PAS protein 9, or PAS domain-containing protein 9 (PASD9), is a neuronal bHLH-PAS transcriptional factor, regulating cell cycle progression and preventing cell death, whose sustained expression might ensure brain neuron survival. It also plays important roles in tumor angiogenesis. Protein cycle, also termed brain and muscle ARNT-like 1 (BMAL1), or MOP3, is a putative bHLH-PAS transcription factor involved in the generation of biological rhythms in Drosophila. It activates cycling transcription of Period (PER) and Timeless (TIM) by binding to the E-box (5'-CACGTG-3') present in their promoters
SRSNHSEIEKRRRDKMNAYIQELSALVPACNAMSRKLDKLTVLRMAVQHLKSLRGTGS
>gnl|CDD|381444 cd11438, bHLH-PAS_ARNTL_PASD3, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator-like protein 1 (ARNTL) and similar proteins. ARNTL, also termed Basic-helix-loop-helix-PAS protein MOP3, or brain and muscle ARNT-like 1 (BMAL1), or Class E basic helix-loop-helix protein 5 (bHLHe5), or member of PAS protein 3, or PAS domain-containing protein 3 (PASD3), or bHLH-PAS protein JAP3, is a member of the bHLH-PAS transcription factor family that forms heterodimers with another bHLH-PAS protein, CLOCK (circadian locomotor output cycle kaput), which regulates circadian rhythm. ARNTL-CLOCK heterodimer complex activates transcription from E-box (CANNTG) elements found in the promoter of circadian responsive genes. ARNTL is highly homologous to ARNT
QGRIKNAREAHSQIEKRRRDKMNSFIDELASLVPTCNAMSRKLDKLTVLRMAVQHMKTLRGATN
>gnl|CDD|381445 cd11439, bHLH-PAS_SRC, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in steroid receptor coactivator (SRC) family. The SRC family of coactivators includes SRC-1 (NcoA-1/p160), SRC-2(TIF2/GRIP1/NcoA-2) and SRC-3(NcoA-3/pCIP/RAC3/ACTR/pCIP/AIB1/TRAM1), which are critical mediators of steroid receptor action. They contain bHLH-PAS domain at the N-terminal that is followed by receptor interacting domain and C-terminal transcriptional activation domain. SRC coactivators interact with nuclear receptors in a ligand-dependent manner and enhance transcriptional activation by the receptor via histone acetylation/methylation
NKCLNEKRRREQENKYIEELAELISASISDMDSLSVKPDKCAILQETVKQIRQIKEQE
>gnl|CDD|381446 cd11440, bHLH-O_Cwo_like, basic helix-loop-helix-orange (bHLH-O) domain found in Drosophila melanogaster protein clockwork orange (Cwo) and similar proteins. Cwo is a bHLH-O transcriptional regulator involved in the regulation of Drosophila circadian rhythms. It functions as both an activator and a repressor of clock gene expression
RDPMSHRIIEKRRRDRMNNCLADLSRLIPPTYLKKGRGRIEKTEIIEMAIKHIKHLQQHA
>gnl|CDD|381447 cd11441, bHLH-PAS_CLOCK_like, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output cycles protein kaput (CLOCK) and similar proteins. The family includes CLOCK, neuronal PAS domain-containing protein 2 (NPAS2) and non-mammalian circadian clock protein PASD1. CLOCK, also termed Class E basic helix-loop-helix protein 8 (bHLHe8), is a transcriptional activator which forms a core component of the circadian clock. NPAS2, also termed neuronal PAS2, or basic-helix-loop-helix-PAS protein MOP4, or Class E basic helix-loop-helix protein 9 (bHLHe9), or member of PAS protein 4, or PAS domain-containing protein 4, is a transcriptional activator which forms a core component of the circadian clock. PASD1 is evolutionarily related to Circadian locomotor output cycles protein kaput (CLOCK)and functions as a suppressor of the biological clock that drives the daily circadian rhythms of cells throughout the body
RKSRNLSEKKRRDQFNVLINELASMLPGRGRKMDKSTVLKKTIAFLRKHKELTA
>gnl|CDD|381448 cd11442, bHLH_AtPRE_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana paclobutrazol resistance (PRE) family. The PRE family includes several bHLH transcription factors from Arabidopsis thaliana, such as PRE1-6. PRE1 (also termed AtbHLH136, or protein banquo 1), PRE2 (also termed AtbHLH134, or protein banquo 2, or EN 52), PRE4 (also termed AtbHLH161, or protein banquo 3), and PRE5 (also termed AtbHLH164) are atypical and probable non DNA-binding bHLH transcription factors that integrate multiple signaling pathways to regulate cell elongation and plant development. PRE3 (also termed AtbHLH135, or protein activation-tagged BRI1 suppressor 1, or ATBS1, or protein target of MOOPTEROS 7, or EN 67) is an atypical and probable non DNA-binding bHLH transcription factor required for MONOPTEROS-dependent root initiation in embryo. It promotes the correct definition of the hypophysis cell division plane. PRE5 (also termed AtbHLH163, or protein KIDARI) is an atypical and probable non DNA-binding bHLH transcription factor that regulates light-mediated responses in day light conditions by binding and inhibiting the activity of the bHLH transcription factor HFR1, a critical regulator of light signaling and shade avoidance
RSSSSRISDDQKNDLYSRLRALLPSIATSDKVSKATVLEEACNYIRNLHREVDDLSERLSRLLTS
>gnl|CDD|381449 cd11443, bHLH_AtAMS_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein aborted microspores (AMS) and similar proteins. The family includes several bHLH transcription factors from Arabidopsis thaliana, such as AMS, ICE1 and SCREAM2. AMS, also termed AtbHLH21, or EN 48, plays a crucial role in tapetum development and it is required for male fertility and pollen differentiation. ICE1, also termed inducer of CBF expression 1, or AtbHLH116, or EN 45, or SCREAM, acts as a transcriptional activator that regulates the cold-induced transcription of CBF/DREB1 genes. It binds specifically to the MYC recognition sites (5'-CANNTG-3') found in the CBF3/DREB1A promoter. SCREAM2, also termed AtbHLH33, or EN 44, mediates stomatal differentiation in the epidermis probably by controlling successive roles of SPCH, MUTE, and FAMA
SKNLMAERRRRKKLNDRLYMLRSVVPKITKMDRASILGDAIDYVKELLQEINELQDELEGLPESESGETL
SQ
>gnl|CDD|381450 cd11444, bHLH_AtIBH1_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana ILI1-BINDING BHLH 1 (IBH1) and similar proteins. The family includes several bHLH transcription factors from Arabidopsis thaliana, such as IBH1, UPBEAT1, PAR1 and PAR2. IBH1, also termed bHLH zeta, or AtbHLH158, is an atypical and probable non DNA-binding bHLH transcription factor that acts as transcriptional repressor that negatively regulates cell and organ elongation in response to gibberellin (GA) and brassinosteroid (BR) signaling. IBH1 forms heterodimer with BHLH49, thus inhibiting DNA binding of BHLH49, which is a transcriptional activator that regulates the expression of a subset of genes involved in cell expansion by binding to the G-box motif. UPBEAT1, also termed AtbHLH151, or EN 146, is a bHLH transcription factor that modulates the balance between cellular proliferation and differentiation in root growth. It does not act through cytokinin and auxin signaling, but by repressing peroxidase expression in the elongation zone. PAR1 (also termed AtbHLH165, or protein helix-loop-helix 1, or protein phytochrome rapidly regulated 1) and PAR2 (also termed AtbHLH166, or protein helix-loop-helix 2, or protein phytochrome rapidly regulated 2) are two atypical bHLH transcription factors that act as negative regulators of a variety of shade avoidance syndrome (SAS) responses, including seedling elongation and photosynthetic pigment accumulation. They act as direct transcriptional repressor of two auxin-responsive genes, SAUR15 and SAUR68. They may function in integrating shade and hormone transcriptional networks in response to light and auxin changes
IRERRRRGEEAIERRLRALRRLVPGGRESMEVEELLQETADYIMFLEMQVKVMKSLV
>gnl|CDD|381451 cd11445, bHLH_AtPIF_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana phytochrome interacting factors (PIFs) and similar proteins. The family includes several bHLH transcription factors from Arabidopsis thaliana, such as PIFs, ALC, PIL1, SPATULA, and UNE10. PIFs (PIF1, PIF3, PIF4, PIF5, PIF6 and PIF7) have been shown to control light-regulated gene expression. They directly bind to the photoactivated phytochromes and are degraded in response to light signals. ALC, also termed AtbHLH73, or protein ALCATRAZ, or EN 98, is required for the dehiscence of fruit, especially for the separation of the valve cells from the replum. It promotes the differentiation of a strip of labile non-lignified cells sandwiched between layers of lignified cells. PIL1, also termed AtbHLH124, or protein phytochrome interacting factor 3-like 1, or EN 110, is involved in responses to transient and long-term shade. It is required for the light-mediated inhibition of hypocotyl elongation and necessary for rapid light-induced expression of the photomorphogenesis- and circadian-related gene APRR9. PIL1 seems to play a role in multiple PHYB responses, such as flowering transition and petiole elongation. SPATULA, also termed AtbHLH24, or EN 99, plays a role in floral organogenesis. It promotes the growth of carpel margins and of pollen tract tissues derived from them. UNE10, also termed AtbHLH16, or protein UNFERTILIZED EMBRYO SAC 10, or EN 99, is required during the fertilization of ovules by pollen
RAAEVHNLSERRRRDRINEKMKALQELIPNCNKTDKASMLDEAIEYLKSLQLQVQMMSMGNGMP
>gnl|CDD|381452 cd11446, bHLH_AtILR3_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine resistant 3 (ILR3) and similar proteins. ILR3, also termed AtbHLH105, or EN 133, is a bHLH transcription factor that plays a role in resistance to amide-linked indole-3-acetic acid (IAA) conjugates such as IAA-Leu and IAA-Phe. It may regulate gene expression in response to metal homeostasis changes
KACREKLRRDKLNERFMELSNVLEPGRPPKTDKATILGDAIRMLKQLRGEVQKLKEENSSLQEESKELKA
EKNELR
>gnl|CDD|381453 cd11447, bHLH-O_HEYL, basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with YRPW motif-like protein (HEYL) and similar proteins. HEYL, also termed Class B basic helix-loop-helix protein 33 (bHLHb33), or hairy-related transcription factor 3 (HRT-3), is a bHLH-O transcriptional repressor that is strongly expressed in the presomitic mesoderm, the somites, the peripheral nervous system and smooth muscle of all arteries and is a downstream effector of the Notch and transforming growth factor-beta pathways. It promotes neuronal differentiation by activating proneural genes and inhibiting other hairy and enhancer of split (HES) and hairy/enhancer-of-split related with YRPW motif protein (HEY) proteins. HEYL also functions as a tumor suppressor involved in the progression of human cancers
TTSSQIQARKKRRGIIEKRRRDRINSSLSELRRLVPTAFEKQGSSKLEKAEILQMTVDHLKMLHATGGAG
KFDA
>gnl|CDD|381454 cd11448, bHLH_AtFAMA_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein FAMA and similar proteins. The family includes several bHLH transcription factors from Arabidopsis thaliana, such as FAMA, MUTE and SPEECHLESS, which work together to regulate the sequential cell fate specification during stomatal development and differentiation. FAMA, also termed AtbHLH97, or EN 14, is a transcription activator required to promote differentiation and morphogenesis of stomatal guard cells and to halt proliferative divisions in their immediate precursors. It mediates the formation of stomata. MUTE, also termed AtbHLH45, or EN 20, is required for the differentiation of stomatal guard cells, by promoting successive asymmetric cell divisions and the formation of guard mother cells. It promotes the conversion of the leaf epidermis into stomata. SPEECHLESS, also termed AtbHLH98, or EN 19, is required for the initiation and the formation of stomata, by promoting the first asymmetric cell divisions. FAMA, MUTE and SPEECHLESS form heterodimers with SCREAM/ICE1 and SCRM2 to regulate transcription of genes during stomatal development
MTHIAVERNRRKQMNEHLNVLRSLMPGSYIQRGDQASIVGGAIEFVKELEQLLQSLEAQKRRRTLNESSV
PSST
>gnl|CDD|381455 cd11449, bHLH_AtAIB_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein ABA-INDUCIBLE bHLH-TYPE (AIB) and similar proteins. The family includes several bHLH transcription factors from Arabidopsis thaliana, such as AIB and MYC proteins (MYC2, MYC3 and MYC4). AIB, also termed AtbHLH17, or EN 35, is a transcription activator that regulates positively abscisic acid (ABA) response. MYC2, also termed protein jasmonate insensitive 1, or R-homologous Arabidopsis protein 1 (RAP-1), or AtbHLH6, or EN 38, or Z-box binding factor 1 protein, is a transcriptional activator involved in abscisic acid (ABA), jasmonic acid (JA), and light signaling pathways. MYC3, also termed protein altered tryptophan regulation 2, or AtbHLH5, or transcription factor ATR2, or EN 36, is a transcription factor involved in tryptophan, jasmonic acid (JA) and other stress-responsive gene regulation. MYC4, also termed AtbHLH4, or EN 37, is a transcription factor involved in jasmonic acid (JA) gene regulation. MYC2, together with MYC3 and MYC4, controls additively subsets of JA-dependent responses
NGREEPLNHVEAERQRREKLNQRFYALRAVVPNVSKMDKASLLGDAISYINELKSKVQDMETEKKEMKRQ
ESEKKTEA
>gnl|CDD|381456 cd11450, bHLH_AtFIT_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana Fe-deficiency induced transcription factor 1 (FIT) and similar proteins. The family includes bHLH transcription factors from Arabidopsis thaliana, such as FIT and DYT1. FIT, also termed FER-like iron deficiency-induced transcription factor, or FER-like regulator of iron uptake, or AtbHLH29, or EN 43, is a bHLH transcription factor that is required for the iron deficiency response in plant. It regulates FRO2 at the level of mRNA accumulation and IRT1 at the level of protein accumulation. DYT1, also termed AtbHLH22, or protein dysfunctional tapetum 1, or EN 49, is a bHLH transcription factor involved in the control of tapetum development. It is required for male fertility and pollen differentiation, especially during callose deposition
SSPASKNLVSERNRRQKLNQRLFALRSVVPNITKMDKASIIKDAISYIQELQYQEKKLEAEIRELESRPP
STLSFQ
>gnl|CDD|381457 cd11451, bHLH_AtTT8_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein transparent testa 8 (TT8) and similar proteins. The family includes several bHLH transcription factors from Arabidopsis thaliana, such as TT8, EGL1, and GL3. TT8, also termed AtbHLH42, or EN 32, is involved in the control of flavonoid pigmentation and plays a key role in regulating leucoanthocyanidin reductase (BANYULS) and dihydroflavonol-4-reductase (DFR). EGL1, also termed AtbHLH2, or EN 30, or AtMYC146, or protein enhancer of GLABRA 3, is involved in epidermal cell fate specification and regulates negatively stomata formation but promotes trichome formation. GL3, also termed AtbHLH1, or AtMYC6, or protein shapeshifter, or EN 31, is involved in epidermal cell fate specification. It regulates negatively stomata formation, but, in association with TTG1 and MYB0/GL1, promotes trichome formation, branching and endoreplication
DEDGSHAMAERRRREKLNERFITLRSMVPFVTKMDKVSILGDAIEYLKQLQRRVEELESRRKSSDTETRP
TMERK
>gnl|CDD|381458 cd11452, bHLH_AtNAI1_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein NAI1 and similar proteins. NAI1, also termed AtbHLH20, or EN 27, is a bHLH transcription activator that regulates the expression of at least NAI2, PYK10 and PBP1. It is required for and mediates the formation of endoplasmic reticulum bodies (ER bodies). It plays a role in the symbiotic interactions with the endophytes of the Sebacinaceae fungus family, such as Piriformospora indica and Sebacina
SLAQDHILAERKRREKLSQRFIALSALVPGLKKMDKASVLGDAIKHIKQLQERVKELEEEKKEKRLMSVV
IVKKS
>gnl|CDD|381459 cd11453, bHLH_AtBIM_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana BES1-interacting Myc-like proteins (BIMs) and similar proteins. The family includes Arabidopsis thaliana BIM1 and its homologs (BIM2 and BIM3), which are bHLH transcription factors that interact with BES1 to regulate transcription of Brassinosteroid (BR)-induced gene. BR regulates many growth and developmental processes such as cell elongation, vascular development, senescence stress responses, and photomorphogenesis. BIM1 heterodimerize with BES1 and bind to E-box sequences present in many BR-induced promoters to regulated BR-induced genes
STPRSKHSATEQRRRSKINERLQALRDLIPHSDQKRDKASFLLEVIEYIQALQEKVAKLEEQVQGWGGEP
AKLTPWA
>gnl|CDD|381460 cd11454, bHLH_AtIND_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein INDEHISCENT (IND) and similar proteins. The family includes several bHLH transcription factors from Arabidopsis thaliana, such as IND, HEC proteins (HEC1, HEC2 and HEC3) and UNE12. IND, also termed AtbHLH40, or EN 120, is a bHLH transcription regulator required for seed dispersal. It is involved in the differentiation of all three cell types required for fruit dehiscence. HEC1 (also termed AtbHLH88, or protein HECATE 1, or EN 118), HEC2 (also termed AtbHLH37, or protein HECATE 2, or EN 117) and HEC3 (also termed AtbHLH43, or protein HECATE 3, or EN 119) are required for the female reproductive tract development and fertility. Both IND and HEC proteins have been implicated in regulation of auxin signaling. They heterodimerize with SPATULA (SPT) bHLH transcription factor to regulate reproductive tract development in plant. UNE12, also termed AtbHLH59, or protein UNFERTILIZED EMBRYO SAC 12, or EN 93, is required for ovule fertilization
STDPQSVAARHRRERISERIRILQRLVPGGTKMDTASMLDEAIHYVKFLQLQVKLLQSDDLWM
>gnl|CDD|381461 cd11455, bHLH_AtAIG1_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein AIG1 and similar proteins. AIG1, also termed AtbHLH32, or EN 54, or protein target of MOOPTEROS 5, is a transcription factor required for MONOPTEROS-dependent root initiation in embryo
EDKALAASKSHSEAERRRRERINSHLATLRTLLPNLSKTDKASLLAEVVQHVKELKRQAAEITTPPDVPT
EDEEDTVGVE
>gnl|CDD|381462 cd11456, bHLHzip_N-Myc_like, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in N-Myc and similar proteins. N-Myc, also termed Class E basic helix-loop-helix protein 37 (bHLHe37), is a bHLHZip proto-oncogene protein that positively regulates the transcription of MYCNOS in neuroblastoma cells. It is also essential during embryonic development. N-Myc has a critical role in regulating the switch between proliferation and differentiation of progenitor cells. It binds DNA as a heterodimer with MAX. The family also includes S-Myc, encoded by rat or mouse intronless myc gene, which has apoptosis-inducing activity
EDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEQKLLLEKEKL
QARQQQLLKKIEQARTC
>gnl|CDD|381463 cd11457, bHLHzip_L-Myc, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in L-Myc and similar proteins. L-Myc, also termed Class E basic helix-loop-helix protein 38 (bHLHe38), or protein L-Myc-1, or V-myc myelocytomatosis viral oncogene homolog, is a bHLHZip oncoprotein belonging to the Myc oncogene protein family. It binds DNA as a heterodimer with MAX. L-Myc is co-expressed with another Myc family member and has weaker transformation/transactivation activities. L-Myc knockout mouse did not exhibit any phenotypic abnormalities
DTEDVAKRKNHNFLERKRRNDLRSRFLALRDEVPGLASCSKTPKVVILSKATEYLRGLVSAERRMAAEKR
QLKSRQQQLLRRIAQLKGR
>gnl|CDD|381464 cd11458, bHLHzip_c-Myc, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in c-Myc and similar proteins. c-Myc, also termed Myc proto-oncogene protein, or Class E basic helix-loop-helix protein 39 (bHLHe39), or transcription factor p64, a bHLHZip proto-oncogene protein that functions as a transcription factor, which binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. It activates the transcription of growth-related genes
EENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYILSMQADEQRLISEKEQL
RRRREQLKHRLEQL
>gnl|CDD|381465 cd11459, bHLH-O_HES1_4, basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split HES-1, HES-4 and similar proteins. The family includes two bHLH-O transcriptional repressors, HES-1 and HES-4. HES-1, also termed Class B basic helix-loop-helix protein 39 (bHLHb39), or hairy homolog, or hairy-like protein (HL), plays an essential role in development of both compartment and boundary cells of the central nervous system. It regulates the maintenance of neural stem/progenitor cells by inhibiting proneural gene expression via Notch signaling. HES-4, also termed Class B basic helix-loop-helix protein 42 (bHLHb42), or bHLH factor Hes4, antagonizes the function of Twist-1 to regulate lineage commitment of bone marrow stromal/stem cells (BMSC). Epigenetic dysregulation of HES-4 is associated with striatal degeneration in postmortem Huntington brains. Both HES-1 and HES-4 are mammalian counterparts of the Hairy and Enhancer of split proteins that play a critical role in many physiological processes including cellular differentiation, cell cycle arrest, apoptosis and self-renewal ability
EHRKSSKPIMEKRRRARINESLSQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRQQ
>gnl|CDD|381466 cd11460, bHLH-O_HES6, basic helix-loop-helix-orange (bHLH-O) domain found in transcription factor HES-6 and similar proteins. HES-6, also termed Class B basic helix-loop-helix protein 41 (bHLHb41), or hairy and enhancer of split 6, or C-HAIRY1, is a bHLH-O transcription factor that is expressed in developing muscle and involved in angiogenesis, myogenesis, neural differentiation and neurogenesis. HES-6 antagonizes Notch signaling but is not regulated by Notch signaling. It is a transcription co-factor associated with stem cell characteristics in neural tissue. It may act as an inhibitor of Hes-1 during neuronal development and forms a heterodimer with HES-1 to prevent its association with transcriptional co-repressors. The overexpression of HES-6 has been reported in metastatic cancers of different origins. HES-6 is one mammalian counterpart of the Hairy and Enhancer of split proteins that play a critical role in many physiological processes including cellular differentiation, cell cycle arrest, apoptosis and self-renewal ability
GDRKARKPLVEKKRRARINESLQELRLILADAELQSKMENAEVLELTVKRVQGILRNR
>gnl|CDD|381467 cd11461, bHLH-O_HES5, basic helix-loop-helix-orange (bHLH-O) domain found in transcription factor HES-5 and similar proteins. HES-5, also termed Class B basic helix-loop-helix protein 38 (bHLHb38), or hairy and enhancer of split 5, is a bHLH-O transcription factor that is involved in cell differentiation and proliferation in a variety of tissues. HES-5 is an essential effector for Notch signaling. It acts as a transducer of Notch signals in brain vascular development. It also acts as a key mediator of Wnt-3a-induced neuronal differentiation and plays a crucial role in normal inner ear hair cell development. HES-5 is one mammalian counterpart of the Hairy and Enhancer of split proteins that play a critical role in many physiological processes including cellular differentiation, cell cycle arrest, apoptosis and self-renewal ability
KLRKPVVEKTRRDRINSSIEQLKTLLEKEFQRHQPNSKLEKADILEMTVSFLKQSAKLS
>gnl|CDD|381468 cd11462, bHLH-O_HES7, basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split 7 (HES-7) and similar proteins. HES-7, also termed Class B basic helix-loop-helix protein 37 (bHLHb37), or bHLH factor Hes7, is a bHLH-O transcriptional repressor that is expressed in an oscillatory manner and acts as a key regulator of the pace of the segmentation clock. It is regulated by the Notch and Fgf/Mapk pathways. HES-7 is one mammalian counterpart of the Hairy and Enhancer of split proteins that play a critical role in many physiological processes including cellular differentiation, cell cycle arrest, apoptosis and self-renewal ability
RKLLKPLVEKRRRDRINRSLEELRVLLLQNTQDEKLKNPKVEKAEILELTVQFLRNSSLSA
>gnl|CDD|381469 cd11463, bHLH-O_HES2, basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split 2 (HES-2) and similar proteins. HES-2, also termed Class B basic helix-loop-helix protein 40 (bHLHb40), is a bHLH-O transcriptional repressor of genes that require a bHLH protein for their transcription. It acts as a negative regulator through interaction with both E-box and N-box sequences. HES-2 is one mammalian counterpart of the Hairy and Enhancer of split proteins that play a critical role in many physiological processes including cellular differentiation, cell cycle arrest, apoptosis and self-renewal ability
ASELRKTLKPLMEKRRRARINESLNQLKTLILPLVGKDSSRYSKLEKADILEMTVRFLQDLPASS
>gnl|CDD|381470 cd11464, bHLH_TS_TWIST, basic helix-loop-helix (bHLH) domain found in twist-related protein (TWIST) family. The TWIST family includes TWIST1 and TWIST2, which are highly homologous bHLH transcription factors that promote epithelial-mesenchymal transition (EMT) during development and tumor metastasis. They are involved in the negative regulation of cellular determination and in the differentiation of several lineages, including myogenesis, osteogenesis, and neurogenesis. TWIST factors express in broad partially-overlapping patterns during embryo development and dimerize with a broad sets of dimer partners that form numerous unique transcriptional complexes to regulate embryonic development
QRVLANVRERQRTQSLNEAFTSLRKIIPTLPSDKLSKIQTLKLAARYIDFLYQVLRSDE
>gnl|CDD|381471 cd11465, bHLH_TS_scleraxis_like, basic helix-loop-helix (bHLH) domain found in scleraxis, transcription factor 15 (TCF-15) and similar proteins. The family includes scleraxis and transcription factor 15 (TCF-15). Scleraxis, also termed SCX, or Class A basic helix-loop-helix protein 41 (bHLHa41), or Class A basic helix-loop-helix protein 48 (bHLHa48), is a bHLH transcription factor that is expressed in sclerotome limb bud cranial and body wall mesenchyme, pericardium and heart valves, ligaments and tendons. It is required for tendon formation ligaments, connective tissue, the diaphragm, and testis development. Scleraxis plays a central role in promoting fibroblast proliferation and matrix synthesis during the embryonic development of tendons. TCF-15, also termed Class A basic helix-loop-helix protein 40 (bHLHa40), or paraxis, or protein bHLH-EC2, is a bHLH transcription factor expressed in caudal lateral and paraxial mesoderm dermomyotome and sclerotome fore limb buds during embryo development. It may function as an early transcriptional regulator involved in the patterning of the mesoderm and in lineage determination of cell types derived from the mesoderm
RQAANARERDRTHSVNSAFTALRTLIPTEPADRKLSKIETLRLASSYISHLATVL
>gnl|CDD|381472 cd11466, bHLH_TS_HAND, basic helix-loop-helix (bHLH) domain found in heart- and neural crest derivatives-expressed protein (HAND) family. The HAND family includes two bHLH transcription factors, HAND1 and HAND2. HAND1, also termed Class A basic helix-loop-helix protein 27 (bHLHa27), or extraembryonic tissues, heart, autonomic nervous system and neural crest derivatives-expressed protein 1 (eHAND), plays an essential role in both trophoblast-giant cells differentiation and in cardiac morphogenesis. HAND2, also termed Class A basic helix-loop-helix protein 26 (bHLHa26), or deciduum, heart, autonomic nervous system and neural crest derivatives-expressed protein 2 (dHAND), is essential for cardiac morphogenesis, particularly for the formation of the right ventricle and of the aortic arch arteries
RRGSANKKERRRTQSINSAFADLRECIPNVPADTKLSKIKTLRLATSYIAYLMDVL
>gnl|CDD|381473 cd11467, bHLH_E-protein_Da_like, basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster protein daughterless (Da) and similar proteins. Da is a nuclear bHLH transcription factor that is a sole E protein ortholog essential for both neurogenesis and sex determination in Drosophila. Da is expressed in a broad range of tissues and is involved in diverse developmental processes such as oogenesis, sex determination and neurogenesis depending on its bHLH-binding partners. Da and achaete-scute complex (AS-C) form heterodimers that act as transcriptional activators of neural cell fates and are involved in sex determination
ERRQANNARERIRIRDINEALKELGRMCMTHLKSDKPQTKLGILNMAVEVIMTLEQQVRERNLNPKAACL
>gnl|CDD|381474 cd11468, bHLH_TS_bHLHe22_like, basic helix-loop-helix (bHLH) domain found in Class E basic helix-loop-helix protein bHLHe22, bHLHe23 and similar proteins. The family includes two OLIG-related bHLH transcription factors, bHLHe22 and bHLHe23. bHLHe22, also termed Class B basic helix-loop-helix protein 5 (bHLHb5), or trinucleotide repeat-containing gene 20 protein, is a neural-specific transcriptional repressor that is expressed in both excitatory (unipolar brush cells) and inhibitory neurons (cartwheel cells) of the dorsal cochlear nucleus (DCN) during development. It is important for the proper development and/or survival of a number of neural cell types. bHLHe23, also termed Class B basic helix-loop-helix protein 4 (bHLHb4), is expressed in rod bipolar cells and is required for rod bipolar cell maturation. bHLHe23 have roles in spinal interneuron differentiation by mechanisms linked to the Notch signaling pathway. It modulates the expression of genes required for the differentiation and/or maintenance of pancreatic and neuronal cell types
RLSINARERRRMHDLNDALDDLRAVIPYAHSPSVRKLSKIATLLLAKNYILMQARAIEELRR
>gnl|CDD|381475 cd11469, bHLH-PAS_ARNTL2_PASD9, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator-like protein 2 (ARNTL2) and similar proteins. ARNTL2, also termed Basic-helix-loop-helix-PAS protein MOP9, or brain and muscle ARNT-like 2 (BMAL2), or CYCLE-like factor (CLIF), or Class E basic helix-loop-helix protein 6 (bHLHe6), or member of PAS protein 9, or PAS domain-containing protein 9 (PASD9), is a neuronal bHLH-PAS transcriptional factor, regulating cell cycle progression and preventing cell death, whose sustained expression might ensure brain neuron survival. It also plays important roles in tumor angiogenesis. ARNT-2 heterodimerize with other bHLH-PAS proteins such as aryl hydrocarbon receptor (AhR), hypoxia-inducible factor (HIF), and single-minded (SIM)
FREAHSQTEKRRRDKMNNLIEELSAMIPQCNPMARKLDKLTVLRMAVQHLKSLKGSTSSF
>gnl|CDD|381476 cd11470, bHLH_TS_TCF15_paraxis, basic helix-loop-helix (bHLH) domain found in transcription factor 15 (TCF-15) and similar proteins. TCF-15, also termed Class A basic helix-loop-helix protein 40 (bHLHa40), or paraxis, or protein bHLH-EC2, is a bHLH transcription factor expressed in caudal lateral and paraxial mesoderm dermomyotome and sclerotome fore limb buds during embryo development. It may function as an early transcriptional regulator involved in the patterning of the mesoderm and in lineage determination of cell types derived from the mesoderm
GPVVVVKQRQAANARERDRTQSVNTAFTALRTLIPTEPVDRKLSKIETLRLASSYIAHLANVLLLG
>gnl|CDD|381477 cd11471, bHLH_TS_HAND2, basic helix-loop-helix (bHLH) domain found in heart- and neural crest derivatives-expressed protein 2 (HAND2) and similar proteins. HAND2, also termed Class A basic helix-loop-helix protein 26 (bHLHa26), or deciduum, heart, autonomic nervous system and neural crest derivatives-expressed protein 2 (dHAND), is a bHLH transcription factor that is essential for cardiac morphogenesis, particularly for the formation of the right ventricle and of the aortic arch arteries
RRGTANRKERRRTQSINSAFAELRECIPNVPADTKLSKIKTLRLATSYIAYLMDLLAKDDQN
>gnl|CDD|211395 cd11473, W2, C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon. This domain is found at the C-terminus of several translation initiation factors, including the epsilon chain of eIF2b, where it has been found to catalyze the conversion of eIF2.GDP to its active eIF2.GTP form. The structure of the domain resembles that of a set of concatenated HEAT repeats
EKNKKLRDSLLKELEEDKSSDVESVKAAKSKLDLDPISLEEVVKVLLTAVVNAVESADSISLTQKEQLVL
VLKKYGPVLRELLKLIKKDQLYLLLKIEKLCLQLKLSELISLLEKILDLLYDADVLSEEAILSWF
>gnl|CDD|271368 cd11474, SLC5sbd_CHT, Na(+)- and Cl(-)-dependent choline cotransporter CHT and related proteins; solute-binding domain. Na+/choline co-transport by CHT is Cl- dependent. Human CHT (also called CHT1) is encoded by the SLC5A7 gene, and is expressed in the central nervous system. hCHT1-mediated choline uptake may be the rate-limiting step in acetylcholine synthesis, and essential for cholinergic transmission. Changes in this choline uptake in cortical neurons may contribute to Alzheimer's dementia. This subfamily belongs to the solute carrier 5 (SLC5) transporter family
LIGVILYYLLILGIGLWASRRVKSSEDFLLAGRSLPLPVGVFTLFATWFGGETILGAAETFYEEGLGGVA
QDPFGYALCLILGGLFFAKPMRRMGLLTLGDFFRQRYGRRVEVLLSIPAVLSYLGWVAAQLVALGLVLSV
ILGLPVETGILISAAIVLAYTLFGGMWSVAYTDVVQLIVIFVGLLVLVPFVLTNPGGVDIASAAAAGKLR
FFPWLGTKSDWLIWIDAWLTLGLGSIPQQDVFQRVLSAKSEKTAQRLSLLAGVGYLLFAIPPLLIGLAAA
SIDPSLTQYGLEEDAQLILPLLLQYLTPLWVQVLFLGALLSAVMSTADSALLAPSSVFSENIYKPPFRPK
ASDRELLWVMRISVVVFGAIATLMALTVESIYGLVELASDLVLVGLFVPLLAGLYWKRANTYGALAAIIV
GLVLRLLGGELLLGLPADIPPQLQGFPFSTLAMVIGSLLPLAVS
>gnl|CDD|271369 cd11475, SLC5sbd_PutP, Na(+)/proline cotransporter PutP and related proteins; solute binding domain. Escherichia coli PutP catalyzes the Na+-coupled uptake of proline with a stoichiometry of 1:1. The putP gene is part of the put operon; this operon in addition encodes a proline dehydrogenase, allowing the use of proline as a source of nitrogen and/or carbon. This subfamily also includes the Bacillus subtilis Na+/proline cotransporter (OpuE) which has an osmoprotective instead of catabolic role. Expression of the opuE gene is under osmotic control and different sigma factors contribute to its regulation; it is also a putative CcpA-activated gene. This subfamily belongs to the solute carrier 5 (SLC5) transporter family
LITFIVYLLLMLGIGIYSYRKTKTLEDYFLGGRSLGPWVTALSAGASDMSGWLLLGLPGAAYASGLSAIW
IAIGLILGAYLNWLFVAKRLRRYTEKNDSITLPDYLENRFRDKSKLLRILSALIILIFFTIYAAAQLVAG
GKLFESLFGIDYSTGLLIGAVVVVAYTFLGGFLAVSWTDFFQGLLMLLALVLVPIVALAALGGLSGLVAA
LAAIDPGLLSPFGGDLGAGGLLAIISLLAWGLGYFGQPHILVRFMAIRSPKEIKKARRIAMVWMILFLLG
AVLVGLLGRALFPDGLLGDPETVFPVLAQELFPPWLAGILLAAILAAIMSTADSQLLVCSSALTEDLYKA
FLRKEASDKELVWVSRLAVLVIALIALLIALNPPSSVFSLVSFAWAGLGAAFGPLLLLSLYWKRTTRQGA
LAGMIAGAVTVVVWKLLGLGIFGLYEIVPGFLASLLAIVVVSLL
>gnl|CDD|271370 cd11476, SLC5sbd_DUR3, Na(+)/urea-polyamine cotransporter DUR3, and related proteins; solute-binding domain. Dur3 is the yeast plasma membrane urea transporter. Saccharomyces cerevisiae DUR3 also transports polyamine. The polyamine uptake of S. cerevisiae DUR3 is activated upon its phosphorylation by polyamine transport protein kinase 2 (PTK2). S. cerevisiae DUR3 also appears to play a role in regulating the cellular boron concentration. This subfamily belongs to the solute carrier 5 (SLC5) transporter family
YGVVIGLGALFALLMVFITRLLKRYRGKNQSSEEFMTAGRSVGTGLTAAAIVSSWTWAATLLQSATVAYQ
YGVSGPFWYASGATLQILLFAPLAIRIKRLAPNAHTLLEIVRARYGTAAHLVFLVFALFTNVIVLAMLLL
GGSAVVNALTGMPIVAASFLIPLGVLLYTLFGGLRATFLTDYIHTVIILIILLVFAFAVYTSSDIGSPSK
VYDLLQEAAPDLPVEGNQGSYLTFKSKAGLIFGIINIVGNFGTVFLDQGYWQRAIAARPSAAVKGYFLGG
LAWFAIPFLLATTLGLAALALGLNPTFEEVSAGLVLPYVAAALLGKGGAAAVLVLLFMAVTSTASAELIA
VSSIVTYDIYRTYINPNATGKQLLRVSRIAVIGFGLFMGGLAVGLNYIGISLGWLLLFMGILIGSAVFPV
ALGLYWRRQTGTAAVVSPIAGLVAGLAVWLVTAKSYYGEVNVDTTGGNYPMLAGNLVALFSPAIVSVLLS
LIF
>gnl|CDD|271371 cd11477, SLC5sbd_u1, Uncharacterized bacterial solute carrier 5 subfamily; putative solute-binding domain. SLC5 (also called the sodium/glucose cotransporter family or solute sodium symporter family) is a family of proteins that co-transports Na+ with sugars, amino acids, inorganic ions or vitamins. Prokaryotic members of this family include Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. One member of the SLC5 family, human SGLT3, has been characterized as a glucose sensor and not a transporter. This subfamily belongs to the solute carrier 5 (SLC5) transporter family
LDWLVIALYFLLMLGIGLWFSKRASKSTSDFFLGGRKLPWWLAGISMAATTFSADTFVAVAGIAYTYGIA
GNWIWWLWAVAGLIGAFVFARRWRRLRVLTDGEFPEERYGGRYGAPLRQFYAVYFALLSNVDILAWVFLA
AIKVSAVFGPWDPWLTILILGLITLIYTVIGGLWAVVVTDVVQFVIAMAASIAVAVLALNAVGGPGGLFA
QLPEGHLDLFGSGLGASGFYITFFFILFFGWYPLSYSGGGWYLAQRYLSAKSEKAAKAAAWLFAALYLVR
PWPWMLPALAALVLYPDLDDPEADFELAYPMMIKEYLPAGLLGLVLAGLLAATMSTVSTHLNWGAAYLVN
DIYKRFIKPNASEKHLLKVGRLATVLFGLLSIVVALASDSIGGAFWIVLALGAGLGGPLILPWLWWRFNA
WTEIWAMIASIIVGLVVSVLLKVFGLPEDFLFSFLVPVLLSLVVWLAVTLLTPPTDEETLVAFYKKVRPW
GFW
>gnl|CDD|271372 cd11478, SLC5sbd_u2, Uncharacterized bacterial solute carrier 5 subfamily; putative solute-binding domain. SLC5 (also called the sodium/glucose cotransporter family or solute sodium symporter family) is a family of proteins that co-transports Na+ with sugars, amino acids, inorganic ions or vitamins. Prokaryotic members of this family include Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. One member of the SLC5 family, human SGLT3, has been characterized as a glucose sensor and not a transporter. This subfamily belongs to the solute carrier 5 (SLC5) transporter family
VDYLIVAVYFVFVLGIGFYLKRKVKTSEDFFLSGRSLPAWITGLAFISANLGALEIVGMSANGAQYGIAT
VHFYWIGAIPAMVFLGIVMMPFYYGSKVRSVPEYLKLRFNKSTRLLNAVSFAVMTILMSGINLYALALVL
NVLLGWPLWLSIILSAAIVLAYTTLGGLTSAIYNEVLQFFLIVAGLIPLVIIGLIKVGGWDGLSEKIDAN
GPPGWNGLSWGPQGSQSTNPMGVNLGLVFGLGFVLSFGYWTTNFLEVQRAMAAKDLSAARRTPLIAAFPK
MFIPFLVILPGLIALVLVPELGASGGLDYNQALPYLMAKYLPPGLLGLGITALLAAFMSGMAGNVSAFNT
VFTYDIYQTYIVKDAPDKHYLKVGRIATVVGVLISIGTAYIASSFNNIMDYLQLLFSFFNAPLFATFLLG
MFWKRATPWGGFWGLLAGTASAIVLYGLYELGLIVYHSDMAPNFYGAWWAFVVCFVVTVLVSLLTKPKPE
KELAGL
>gnl|CDD|271373 cd11479, SLC5sbd_u3, Uncharacterized bacterial solute carrier 5 subfamily; putative solute-binding domain. SLC5 (also called the sodium/glucose cotransporter family or solute sodium symporter family) is a family of proteins that co-transports Na+ with sugars, amino acids, inorganic ions or vitamins. Prokaryotic members of this family include Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. One member of the SLC5 family, human SGLT3, has been characterized as a glucose sensor and not a transporter. This subfamily belongs to the solute carrier 5 (SLC5) transporter family
LDYGVIALYFAAMIAIGWWGMRRAKTSEDYLVAGRRLGPGLYLGTMAAVVLGGASTIGGVGLGYQYGISG
MWLVVAIGLGILALSLLLAKRIARLKVYTVSEVLELRYGPSARVISALVMLAYTLMVAVTSTIAIGTVFS
VLFGLPRTLSILVGGGIVVLYSVLGGMWSITLTDIIQFVIKTIGIFLLLLPLALSKAGGLSGLQEKLPAS
YFDLTSIGWDTIVTYFLLYFFGILIGQDIWQRVFTARSEKVARWGGVAAGLYCVLYGVAGALIGMAAAVL
LPDLANPQNAFATMAQEVLPVGLRGLVLAAALAAMMSTASGALLASSTVLTNDVLPRLRRKNESERSEVR
LSRLFTLLLGVVVIVIAVLVNDVVAALTIAYAILVGGLLVPILGGLFWKRATGAGALASMVAGSVVVLAG
MAVDGLLANTPIYYGLAVSLVAFVAVSLLTRPTP
>gnl|CDD|271374 cd11480, SLC5sbd_u4, Uncharacterized bacterial solute carrier 5 subfamily; putative solute-binding domain. SLC5 (also called the sodium/glucose cotransporter family or solute sodium symporter family) is a family of proteins that co-transports Na+ with sugars, amino acids, inorganic ions or vitamins. Prokaryotic members of this family include Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. One member of the SLC5 family, human SGLT3, has been characterized as a glucose sensor and not a transporter. This subfamily belongs to the solute carrier 5 (SLC5) transporter family
IGLFFVFVTITLYITIWAARRTRSTSDFYVAGRGVPPVQNGLAIAGDYMSAASFLGIAGLIALSGYDGLA
YAIGWTGGYVLLLLLVAEPLRNFGKYTVPDFLGARLGSRPVRLVAAVSTLVISFFYLVAQMVGAGLLLSL
LLGIPYEVGVVVVGALMIVYVVLGGMRATTWVQIIQYVLLLGAFLVPAILVLARFGGNPLGAGPGLLGLA
AAAASGAGEAYLAPGLLLTDPLDVISLTLALMLGTAGLPHVLMRFYTVPDARAARKSVVWALGFIGLFYL
LAPALGFGARALVGPDVIGAPIAGELDGGGDMAVLLLPEIAGLGDLLLALVAAGAFAAILATVAGLLLAA
ASALAHDLYAGVIRPGASERREVRVARIAAVVVGVIAILLALLFPPQNVAFLVALAFAIAASAFFPVLVL
GIFWRRFTTRGAIAGMLVGLLVSLVLIVLSPAVSGAPPGHDFAGFPLTNPGLVSVPLGFLVAIVVSLL
>gnl|CDD|271375 cd11482, SLC-NCS1sbd_NRT1-like, nucleobase-cation-symport-1 (NCS1) transporter NRT1-like; solute-binding domain. This fungal NCS1 subfamily includes various Saccharomyces cerevisiae transporters: nicotinamide riboside transporter 1 (Nrt1p, also called Thi71p), Dal4p (allantoin permease), Fui1p (uridine permease), Fur4p (uracil permease), and Thi7p (thiamine transporter). NCS1s are essential components of salvage pathways for nucleobases and related metabolites. NCS1s belong to a superfamily which also contains the solute carrier 5 family sodium/glucose transporters, and solute carrier 6 family neurotransmitter transporters
WSNRDLDPVPPERRTWGWWSFFAYWISDSFNISTWQTGSSLLALGLSWWQAIGAVIIGNILIAIFVVLNG
RPGAKYHIGFPVASRASFGIYGSYFPVIIRVVLAIVWFGVQAWTGGQCVTVMLRAIFPSFLNIPNTLPAS
AGITTAQLIGFFLFWLIQLPFLFIPPEKLRHLFTVKAVIVPIAALGLLIWALAKAGGAGPLVSQPSSLSG
SALGWAWLSGINSIIGGFSTLIVNQPDFTRYAKKPPDAVWGQLISIPLSGTLVPLLGILTTSASKVLYGE
AYWNPLDLLDAWLDHDYSAGARAAAFFAALGFALAQLGTNISANSISAGNDLTGLFPKYINIRRGAIICA
ILGWAIVPWKLLNSASSFLTFLSSYSVFLAPIAGIMIADYYIVRRGKLKLPDLYTASPHGIYWYTKGVNW
RAFVAWLVGVAPNLPGLANSVNPPVSVPGGAVRLYYLGYLLGFLISFVVYYVLCLIFPPK
>gnl|CDD|271376 cd11483, SLC-NCS1sbd_Mhp1-like, nucleobase-cation-symport-1 (NCS1) transporter Mhp1-like; solute-binding domain. This NCS1 subfamily includes Microbacterium liquefaciens Mhp1, and various uncharacterized NCS1s. Mhp1 mediates the uptake of indolyl methyl- and benzyl-hydantoins as part of a metabolic salvage pathway for their conversion to amino acids. Mhp1 has 12 transmembrane (TM) helices (an inverted topology repeat: TMs1-5 and TMs6-10, and TMs11-12; TMs numbered to conform to the Solute carrier 6 (SLC6) family Aquifex aeolicus LeuT). NCS1s are essential components of salvage pathways for nucleobases and related metabolites; their other known substrates include allantoin, uracil, thiamine, and nicotinamide riboside. NCS1s belong to a superfamily which also contains the solute carrier 5 family sodium/glucose transporters (SLC5s), and SLC6 neurotransmitter transporters
ESRSLRNPELLPTRYAERSMSLFDYAILWAGMTINVVAFSLGAQYYNGGDGLSPWTVIVVILIGYGIVTI
LTFLTGDIGTKYGVPFAVYARAPFGYKGSLIAGLLRAIPSLYWFGFQTWVGALALNEIMRILFGFSNLTL
MIIIFAAIQVVNTMYGLKAMAKFDWIAIPVLAIMFVAIVYLMLDKYNVSLPEIMSTGGEGGYSFAFAIMG
IAGGWITMALNGSDLVRQIKRDPNYENEGFFKRNKRAIIGQWLGLMPVGIIFMLIGMASGILTGEWDLNI
VITELFGGSIPVLILFFIFILFAQWSTNTAANLLPPAYVLLNIFPKLKFKMSVIISGVIGLLMMPWKFQG
VGFLVTFQNLISSMLGPIIGIMLADYFLIRKCKLNVHDLYRAGGQYQYTNGFNWSAVAALVVAFAVSLLT
PDYAFFTGLIASLVLYIVLMKWFTLKKYLQS
>gnl|CDD|271377 cd11484, SLC-NCS1sbd_CobB-like, nucleobase-cation-symport-1 (NCS1) transporter CobB-like; solute-binding domain. This NCS1 subfamily includes Escherichia coli CodB (cytosine permease), and the Saccharomyces cerevisiae transporters: Fcy21p (Purine-cytosine permease), and vitamin B6 transporter Tpn1. NCS1s are essential components of salvage pathways for nucleobases and related metabolites; their known substrates include allantoin, uracil, thiamine, and nicotinamide riboside. NCS1s belong to a superfamily which also contains the solute carrier 5 family sodium/glucose transporters (SLC5s), and solute carrier 6 family neurotransmitter transporters (SLC6s)
VPEERRKSFLSMFSVWLGANFFLASMVTGALLGVGLSLSQAILAVLLGNLIGGAYMALLGYIGARTGLPQ
MLLSRASFGEKGSYLPSLLLGITQIGWFGVGTAMFAIALSKLLGINGSLWLLILIAGVLMTLTAIFGYKA
LHKLEKIAVPLIIALFVYSVVLALRDYGVGGLAALTATGPLSFLVAVSLVAGSFISGATYTADYSRYAKS
SKKAFWATFLGFFVGNSLMMILGALLAAATGTADISEVMIAQGLGIPAILVLVLNIWTTNDNNLYSSGLS
LSNITKIFRRKVLTLVAGIVGTLLAALGIYNHFLNFLLLLGYALPPWGGVMLADYFVVRRGRYDIDALAD
PQYGGVNWAALIAWAVGVAVGIPFPYGLLGGGGIAPINGLLVAAVVYYILRKILSK
>gnl|CDD|271378 cd11485, SLC-NCS1sbd_YbbW-like, uncharacterized nucleobase-cation-symport-1 (NCS1) transporter subfamily, YbbW-like; solute-binding domain. NCS1s are essential components of salvage pathways for nucleobases and related metabolites; their known substrates include allantoin, uracil, thiamine, and nicotinamide riboside. This subfamily includes the putative allantoin transporter Escherichia coli YbbW (also known as GlxB2). NCS1s belong to a superfamily which also contains the solute carrier 5 family sodium/glucose transporters (SLC5s), and solute carrier 6 family neurotransmitter transporters (SLC6s)
DSRLYNEDLAPVPPEQRTWTTWNYAALWIGMVHNIPTYMLASGLIALGMSWWQALLTVVLGNLIVLIPMV
LNGHAGTKYGIPFPVLARASFGVRGANIPALLRAIVACGWFGIQTWIGGQAIYAILGVLIWPGWLGIGFG
QLFCFLLFPWALNVWIIYKGMESIRKLEAWAAPLLILLSLALLIWAISKAGGFGPILSQPSAFGPKGGNF
WKVFFPALTAMIGFWATLALNIPDFTRFAKSQRAQVLGQAIGLPITMALFAFVGVAVTSATVVIFGEAIW
DPVDLLSRFDNPAVVIIALLAIILATLSTNVAANLVSPAYDFANLFPKKISFRRGGLITAVLGLLIMPWK
LLENADGYIFTWLGGYGALLGPIAGIMIADYWLVRRTRLDLDDLYRRGGRYWYSNGWNWRALIALAVGVL
PALPGFLIPALKWLYDYAWFVGFAVAGLLYLLLMKR
>gnl|CDD|271379 cd11486, SLC5sbd_SGLT1, Na(+)/glucose cotransporter SGLT1;solute binding domain. Human SGLT1 (hSGLT1) is a high-affinity/low-capacity glucose transporter, which can also transport galactose. In the transport mechanism, two Na+ ions first bind to the extracellular side of the transporter and induce a conformational change in the glucose binding site. This results in an increased affinity for glucose. A second conformational change in the transporter follows, bringing the Na+ and glucose binding sites to the inner surface of the membrane. Glucose is then released, followed by the Na+ ions. In the process, hSGLT1 is also able to transport water and urea and may be a major pathway for transport of these across the intestinal brush-border membrane. hSGLT1 is encoded by the SLC5A1 gene and expressed mostly in the intestine, but also in the trachea, kidney, heart, brain, testis, and prostate. The WHO/UNICEF oral rehydration solution (ORS) for the treatment of secretory diarrhea contains salt and glucose. The glucose, along with sodium ions, is transported by hSGLT1 and water is either co-transported along with these or follows by osmosis. Mutations in SGLT1 are associated with intestinal glucose galactose malabsorption (GGM). Up-regulation of intestinal SGLT1 may protect against enteric infections. SGLT1 is expressed in colorectal, head and neck, and prostate tumors. Epidermal growth factor receptor (EGFR) functions in cell survival by stabilizing SGLT1, and thereby maintaining intracellular glucose levels. SGLT1 is predicted to have 14 membrane-spanning regions. This subgroup belongs to the solute carrier 5 (SLC5)transporter family
ADISVIVIYFVVVLAVGVWAMVSTNRGTVGGFFLAGRSMVWWPIGASLFASNIGSGHFVGIAGTGAAAGI
AIGGFEWNALVVVVVLGWLFVPIYIKAGVVTMPEYLRKRFGGQRIQVYLSVLSLCLYIFTKISADIFSGA
IFINLALGLNLYLAIVILLAITALYTITGGLAAVIYTDTLQTIIMVVGSFILMGFAFNEVGGYDAFMEKY
MTAIPSVIGTGNSTSQEKCYTPRADSFHIFRDPITGDLPWPGLLFGLSILTLWYWCTDQVIVQRCLSAKN
MSHVKAGCILCGYLKLLPMFIMVMPGMISRILYTDEIACVVPDECKAVCGTEVGCTNIAYPKLVVELMPN
GLRGLMLSVMLASLMSSLTSIFNSASTLFTMDIYTKVRKKASEKELMIAGRLFMLVLIGISIAWVPIVQS
AQSGQLFDYIQSITSYLGPPIAAVFLLAIFCKRVNEPGAFWGLCVGLLVGLARMITEFAYGTGSCVNPSN
CPTIICGVHYLYFAIILFGISCILILSISLMTKPIPDVHLYRLCWSLRNSKEERIDLDADDETEDQDSNS
MIETDEMREEPGCCKKAYNWFCGLDQGNAPKLTKEEEAALKMKLTDTSEKPLWRNVVNANGIILLTVAVF
CHAFFA
>gnl|CDD|212056 cd11487, SLC5sbd_SGLT2, Na(+)/glucose cotransporter SGLT2 and related proteins; solute-binding domain. Human SGLT2 (hSGLT2) is a high-capacity, low-affinity glucose transporter, that plays an important role in renal glucose reabsorption. It is encoded by the SLC5A2 gene and expressed almost exclusively in renal proximal tubule cells. Mutations in hSGLT2 cause Familial Renal Glucosuria (FRG), a rare autosomal defect in glucose transport. hSGLT2 is a major drug target for regulating blood glucose levels in diabetes. hSGLT2 is predicted to have 14 membrane-spanning regions. This subgroup belongs to the solute carrier 5 (SLC5) transporter family
ADISVIAAYFLLVIGVGLWSMCRTNRGTVGGYFLAGRSMVWWPVGASLFASNIGSGHFVGLAGTGAASGI
AVAGFEWNALFVVLLLGWLFVPVYLTAGVITMPQYLKKRFGGQRIRLYLSVLSLFLYIFTKISVDMFSGA
VFIQQALGWNIYASVIALLGITMIYTVTGGLAALMYTDTVQTFVIIGGACVLMGYAFHEVGGYSALFEKY
LKAVPSLTVSEDPAVGNISSSCYRPRPDSYHLLRDPVTGDLPWPALILGLTIVSSWYWCSDQVIVQRCLA
ARSLTHVKAGCILCGYLKLLPMFLMVMPGMISRVLYPDEVACVEPSVCLRVCGTEVGCSNIAYPKLVVKL
MPNGLRGLMLAVMLAALMSSLASIFNSSSTLFTMDIWTRLRPQAGDKELLLVGRVWVVCIVAVSVAWIPV
VQAAQGGQLFDYIQSVSSYLAPPIAAVFFLALFVKRVNEPGAFWGLIGGLLMGLCRMVPEFSFGSGSCVA
PSSCPAIICGVHYLYFAILLFFCSGLLVLIVSLCTPPIPRKHLHRLVFSLRHSKEEREDLLPDISEDPKW
ARVVNLNALIMMAVAVFLWGFYA
>gnl|CDD|271380 cd11488, SLC5sbd_SGLT4, Na(+)/glucose cotransporter SGLT4 and related proteins; solute-binding domain. Human SGLT4 (hSGLT4) has been reported to be a low-affinity glucose transporter with unusual sugar selectivity: it transports D-mannose but not galactose or 3-O-methyl-D-glucoside. It is encoded by the SLC5A9 gene and is expressed in intestine, kidney, liver, brain, lung, trachea, uterus, and pancreas. hSLGT4 is predicted to contain 14 membrane-spanning regions. This subgroup belongs to the solute carrier 5 (SLC5)transporter family
DIAVVVVYFVFVLAVGIWSSIRASRGTVGGYFLAGRSMTWWPIGASLMSSNVGSGLFIGLAGTGAAGGLA
VGGFEWNAAWVLIALGWIFVPVYIAAGVVTMPEYLKKRFGGQRIRIYMSVLSLILYIFTKISTDIFSGAL
FIQVSLGWNLYLSTVILLAVTALYTIAGGLTAVIYTDALQTVIMVIGAFVLMFIAFDKVGWYPGLEQQYE
KAIPALTVPNTTCHLPRSDAFHIFRDPVTGDIPWPGLIFGLTVLATWVWCTDQVIVQRSLSAKNLSHAKG
GSVLGGYLKILPMFFVVMPGMISRALFPDEVGCVDPDECQKICGAKVGCSNIAYPKLVVELMPVGLRGLM
IAVIMAALMSSLTSIFNSSSTLFTMDVWQRIRRRASEQELMVVGRVFILLLVVISILWIPIIQTANSGQL
FDYIQAVTSYLSPPITAVFILAIFWKRVNEPGAFWGLMVGLVVGLVRMIMEFVYGAPSCGETDLRPSVLK
DVHYLYFAIILLGLTAIVIVAVSLCTAPIPEKHLVRLTWWTRNSPEERVELWWKRLGMWFCGLSQTPEQD
LSEEERQALEKKLTSIEEDPLWRTVCNINALILLAINVFLWGYFA
>gnl|CDD|212058 cd11489, SLC5sbd_SGLT5, Na(+)/glucose cotransporter SGLT5 and related proteins; solute-binding domain. Human SGLT5 is a glucose transporter, which also transports galactose. It is encoded by the SLC5A10 gene, and is exclusively expressed in the renal cortex. This subgroup belongs to the solute carrier 5 (SLC5) transporter family
SVADIIVIGVYFALNVAVGIWSSCRVSRNTVSGYFLAGRDMAWWPIGASLFASSEGSGLFIGLAGTGAAG
GIAVAGFEWNATYALLALAWVFVPVYISSGIVTMPEYLQRRFGGERIRMYLSVLSLLLSVFTKISTDLYS
GALFVQVCLGWNLYLSTVLMLVVTALYTIAGGLAAVIYTDALQTLIMVIGAVILTIKAFNQIGGYSNLEE
AYLQAVPSKIIPNTTCHLPRADAMHLFRDPVTGDLPWTGMTFGLTIMATWYWCTDQVIVQRSLSARSLSH
AKGGSILASYLKMLPMGLIIMPGMISRALFPDDVACVDPEECLRVCGAEVGCSNIAYPKLVMELMPSGLR
GLMIAVMMAALMSSLTSIFNSSSTLFTMDIWRRLRPGASERELLLVGRLVTVILVGVSVVWIPILQSSNS
GQLYIYIQSVTSYLAPPVTAVFVLAVFWRRANEQGAFWGLMAGLVVGLTRMVLEFAHPAPRCGVPDTRPS
VLRSMHYLHFAVALCALSGAVVVAGSLLTPPPQSVQIRNLTWWTLAQDTPLGIKLGDGQTLSRRTDGCES
VRFASGTPPPIIHSTTEHPFWARVCGVNAILLMCVNIFFYAYFA
>gnl|CDD|271381 cd11490, SLC5sbd_SGLT6, Na(+)/chiro-inositol cotransporter SGLT6 and related proteins; solute-binding domain. Human SGLT6 (also called KST1, SMIT2) is a chiro-inositol transporter, which also transports myo-inositol. It is encoded by the SLC5A11 gene. Xenopus Na1-glucose cotransporter type 1 (SGLT-1)-like protein is predicted to contain 14 membrane-spanning regions. This subgroup belongs to the solute carrier 5 (SLC5) transporter family
DIVVLVLYFLFVLAVGLWSMWKTKRSTVKGYFLAGKDMTWWPVGASLFASNVGSGHFIGLAGSGAAAGIG
VVAYEWNGLFMVLVLAWLFLPIYIASRVTTMPEYLKKRFGGKRIQIFLAVLYLFIYIFTKISVDMYAGAV
FIQQALQWDLYLAVVGLLGITALYTVAGGLAAVIYTDALQTIIMVIGALILMGYSFAEVGGFEALLEKYF
QAIPSIRSPNSTCGIPREDAFHIFRDPVTSDLPWPGVLLGMSIPSLWYWCTDQVIVQRSLAAKNLSHAKG
GSLLAAYLKVLPLFMMVIPGMISRILFPDQVACADPEVCKEICGNPSGCSDIAYPKLVMELLPTGLRGLM
MAVMLAALMSSLTSIFNSASTIFTMDLWRHIRPRASEWELMIVGRVFVLVLVVVSILWIPLVQASQGGQL
FIYIQSISSYLQPPVAVVFIAGCFWKRTNEKGAFWGLMVGLAVGLTRMVLDFIYVTPQCDQPDTRPDIVK
YVHYLYFSMILTILTLVVVVCVSLATEPPSKEMISRLTWFTRFDAVVESEELKKAILWLCGMEKQTEKSS
SSPAPPEAAMVSLEEEPLMKHVLNANLIICVSVAVFLWAYFA
>gnl|CDD|271382 cd11491, SLC5sbd_SMIT, Na(+)/myo-inositol cotransporter SMIT and related proteins; solute-binding domain. Human SMIT is a high-affinity myo-inositol transporter, and is expressed in brain, heart, kidney, and lung. Inhibition of myo-inositol uptake, through down-regulation of SMIT, may be a common mechanism of action of mood stabilizers, including lithium, carbamazepine, and valproate. SMIT is encoded by the SLC5A3 gene, which is a candidate gene for pathogenesis of nervous system dysfunction in Down syndrome (DS). The SNP, 21q22 near SLC5A3-MRPS6-KCNE2, has been associated with coronary heart disease, cardiovascular disease, and myocardial infarction. SMIT may also be involved in the pathogeneisis of congenital cataract. SMIT also plays roles in osteogenesis, bone formation, and bone mineral density determination. This subgroup belongs to the solute carrier 5 (SLC5) transporter family
DIAVVALYFILVMCIGIYAMWKSNRSTVSGYFLAGRSMTWLPVGASLFASNIGSEHFIGLAGSGAAAGFA
VGAFEFNALILLQLLGWVFIPVYIRSGVYTLPEYLSKRFGGHRIQVYLAALSLILYIFTKISVNLYSGAL
FIQEALGWNLYVSIILLLGLTALLTVTGGLAAVIYTDTLQAFLMIIGALTLMIISMMEIGGFEGVKSRYM
LASPNVTSILLTYNLSNTNSCCVHPKKDAFKLLRDPTDEDVPWPGFILGQTPASIWYWCADQVIVQRVLA
AKSLSHAQGATLMAGFIKLLPLFIIVIPGMISRILFPDDIACINPEHCMQVCGSRAGCSNIAYPRLVMKI
MPSGLRGLMMAVMIAALMSDLTSIFNSASTLFTLDVYKLIRKKASSRELMIVGRIFVAVMVVISIAWIPV
IQEMQGGQLYLYIQEVAAYLTPPVASLYLLAIFWKRTTEQGAFYGGMAGFVLGAVRLILAFAYRAPECGQ
PDNRPGIIKDIHYMYFATALFWITGLITVIVSLLTPPPTKENIRTTTFWTKKSLKFIDWFCGFKSKSLSK
RSLRDLMEHDEEAVCIQSLEQTPQVKLILNIGLFAVCILGIFMFIYFSV
>gnl|CDD|271383 cd11492, SLC5sbd_NIS-SMVT, Na(+)/iodide (NIS) and Na(+)/multivitamin (SMVT) cotransporters, and related proteins; solute binding domain. NIS (encoded by the SLC5A5 gene) transports I-, and other anions including ClO4-, SCN-, and Br-. SMVT (encoded by the SLC5A6 gene) transports biotin, pantothenic acid and lipoate. This subfamily also includes SMCT1 and -2. SMCT1(encoded by the SLC5A8 gene) is a high-affinity transporter of various monocarboxylates including lactate and pyruvate, short-chain fatty acids, ketone bodies, nicotinate and its structural analogs, pyroglutamate, benzoate and its derivatives, and iodide. SMCT2 (encoded by the SLC5A12 gene) is a low-affinity transporter for short-chain fatty acids, lactate, pyruvate, and nicotinate. This subgroup belongs to the solute carrier 5 (SLC5) transporter family
VDYVVFVAMLLISAAIGIYFGFFGGKQKTTEEYLLGGRNMSVFPVALSLIASFISGITLLGTPAEIYYYG
TQYWLIVIAYVLVGPITAYIFLPVFYNLQLTSVYEYLELRFNRRVRLLASFLFILQMLLYLPIVIYAPAL
ALSQVTGINLHIIILVVGIVCIFYTTLGGLKAVVWTDVFQVVVMFGGVLAVIILGTIDVGGFSEVWEIAE
EGGRLEFFNFDPDPTVRHTFWSLVIGGTFTWLSLYGVNQTQVQRYLSLPSLKSAKKALWLNIVGLILILS
LCCFTGLVIYAKYHDCDPLTAGLIKKPDQLLPYFVMDVLGHLPGLPGLFVAGIFSAALSTLSSGLNSLAA
VILEDFIKPFFKKKLSERQATNIMKLLVVVFGLLCIGLAFLVEKLGGVLQLSLSIFGITGGPLLGIFTLG
MFFPWANSKGALVGLLVGLIFMLWIGIGGQIAIAPGPLSFPPLPTSTEGCNYTNTTTITTSTTTTTTEDE
SEPFPLYRISYLWYSLIGFLITVVVGLIVSLL
>gnl|CDD|271384 cd11493, SLC5sbd_NIS-like_u1, uncharacterized subgroup of the Na(+)/iodide (NIS) cotransporter subfamily; putative solute-binding domain. Proteins belonging to the same subfamily as this uncharacterized subgroup include i) NIS, which transports I-, and other anions including ClO4-, SCN-, and Br-, ii) SMVT, which transports biotin, pantothenic acid and lipoate, and iii) the Na(+)/monocarboxylate cotransporters SMCT1 and 2. SMCT1 is a high-affinity transporter while SMCT2 is a low-affinity transporter. This subgroup belongs to the solute carrier 5 (SLC5) transporter family
DLAVIVLYLLGLPLLGLWLSGRQKSTADYFLGGRSMPWWAVCLSVVATETSTLTFLSIPGLAYGGDLTFL
QLALGYILGRIIVAFVLLPRYFRGEVVSAYELLGQRFGGGMQKTASVTFLVTRLLADGVRLFAAAIPVSM
ILGADGVALSYIASILIISVVTLLYTYFGGIRAVVWTDVIQLVVYIGGAVAALAYLLGALPADWLQIAAA
AGKFHLFDLSDLILGLTSPYTFWAAIIGGALLSMASHGTDQLMVQRLLACRNLRDAQKALIGSGVVVFPQ
FALFLLIGLLLYVYYGGASLAALGLGSPDEVFPYFIVHELPAGLRGLLIAGILAAAMSTLSSALNSLASS
TVQDLYQPWKRRRLSDEKLLRASRLLTLVWAVVLVGIALLFQYTDQPVVELGLSIASFTYGGLLGVFLLG
LLTRRASQRDAIAAFIVGFLVMLLLIFGVKFLGLLFALAFPWYVPIGTLVTFLVGLLLS
>gnl|CDD|271385 cd11494, SLC5sbd_NIS-like_u2, uncharacterized subgroup of the Na(+)/iodide (NIS) cotransporter subfamily; putative solute-binding domain. Proteins belonging to the same subfamily as this uncharacterized subgroup include i) NIS, which transports I-, and other anions including ClO4-, SCN-, and Br-, ii) SMVT, which transports biotin, pantothenic acid and lipoate, and iii) the Na(+)/monocarboxylate cotransporters, SMCT1 and 2. SMCT1 is a high-affinity transporter while SMCT2 is a low-affinity transporter. This subgroup belongs to the solute carrier 5 (SLC5) transporter family
LDWIVLVGYLLGILVYGVYKGRGQKNQEDYFLGGRSMPWWPIGLSIMATQASAITFLSAPGQAYSDGMRF
VQYYFGLPLAMIFLCITFVPVFYKLKVYTAYEYLERRFGLKTRLLTSILFLISRGLATGVTIYAPAIILS
TILGWSLWLTILLIGGITIIYTVLGGIKAVIWTDVIQMVIIWAGLFIAFGLLLKLLPVGFVDALLVAGKS
GRLNALDFSFDLSDTYTFWSGLIGGFFLYLSYFGTDQSQVQRYLTAKSIKEARKSLLLNGFLKFPMQFFI
LLIGVLVFVFYQFNPFPVSFNPAEDETKDTNYIFLRFVLNYLPPGVIGLLIAAIFAAAMSSIDSALNSLA
TVTVIDIYRRFFKKDASDEHYLKVSRLLTVFWGLLAIVFALFAGLAGSLIEAVNKLGSLFYGPILGVFLL
AFFTKKANGKGVFAGAILGVIVVIVLWLFPDVSWLWWNVIGCVVVIGVALLLS
>gnl|CDD|271386 cd11495, SLC5sbd_NIS-like_u3, uncharacterized subgroup of the Na(+)/iodide (NIS) cotransporter subfamily; putative solute-binding domain. Proteins belonging to the same subfamily as this uncharacterized subgroup include i) NIS, which transports I-, and other anions including ClO4-, SCN-, and Br-, ii) SMVT, which transports biotin, pantothenic acid and lipoate, and iii) the Na(+)/monocarboxylate cotransporters SMCT1 and 2. SMCT1 is a high-affinity transporter while SMCT2 is a low-affinity transporter. This subgroup belongs to the solute carrier 5 (SLC5) transporter family
FGWLDYLVLVIYLLAMLGIGLYFSKKQKSTDDYFKGGGRIPWWAAGLSIFATTLSSITFLAIPGKAYATD
WNYFVGSLSIIIAAPLAAYFFVPFFRRLNVTSAYEYLEKRFGPWARVYGSLLFILFQLGRMGIVLYLPAL
ALSAVTGINPYIIIILMGVLCIIYTVLGGIEAVIWTDVIQGVVLLGGALLCLIILLFSIPGGFGEVFDIA
IANGKFSLGDFSFSLTESTIWVIFIGGIFNNLQSYTSDQDVVQRYLTTKSIKEAKKSLWTNALLALPVAL
LFFGIGTALYVFYQQHPELLPAGINGDAVFPYFIVTQLPVGVAGLIIAAIFAAAMSTISSSLNSVATCIT
TDFYKRLSPDPSDKQYLKVARLITLLVGLLGTLVALYLANAGVKSLLDAFNTLTGLFGGGLAGLFLLGIF
TKRANAKGALVGIIVSIIVIFWISLLYTPIHFFLYSVIGTLVCFVVGYVVSLL
>gnl|CDD|271387 cd11496, SLC6sbd-TauT-like, Na(+)- and Cl(-)-dependent taurine transporter TauT, and related proteins; solute-binding domain. This subgroup represents the solute-binding domain of TauT-like Na(+)- and Cl(-)-dependent transporters. Family members include: human TauT which transports taurine, human GAT1, GAT2, and GAT3, and BGT1, which transport gamma-aminobutyric acid (GABA), and human CT1 which transports creatine. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RGKWSNKIDFLLSVAGYAIGLGNVWRFPYLCYKNGGGAFLIPYFIFLVLCGIPIFFLETSLGQYTSQGGI
TAWKICPLFKGIGYASAVIVFWLNIYYIVILAWALFYLFNSFTSPLPWTTCDNWWNTECCVEFYSNNNLS
NSRENASNNTNATSPVEEFWERRVLGISDGIDEIGSIRWELVLCLLLAWVIVYFCIWKGVKSTGKVVYFT
ATFPYVMLIILLIRGVTLPGASDGIKFYLKPDLTKLLDPQVWIDAGTQIFFSYGIGLGSLTALGSYNKFN
NNCYKDSIILCFLNSGTSFFAGFAIFSILGFMAQEQGVPISEVAESGPGLAFIAYPRAVSLLPLPQLWAV
LFFIMLLLLGLDSQFVGVEGFVTAIVDLYPRVLRRRYRREIFVAIVCLVSFLIGLPMVTEGGIYVFQLFD
YYAASGICLLWLAFFECIAISWVYGADRFYDNIKDMIGYRPGPWWKYCWLFGTPAICLGIFIFSLVKYTP
LTYGNTYVYPWWAEAIGWFLALSSMLCIPLYAIYELLRTPGTFKERLRKLTTP
>gnl|CDD|271388 cd11497, SLC6sbd_SERT-like, Na(+)- and Cl(-)-dependent monoamine transporters, SERT, NET, DAT1 and related proteins; solute binding domain. This subgroup represents the solute-binding domain of transmembrane transporters that transport monoamine neurotransmitters from synaptic spaces into presynaptic neurons. Members include: NET which transports norepinephrine, SERT which transports serotonin, and DAT1 which transports dopamine. These transporters may play a role in diseases including depression, anxiety disorders, attention-deficit hyperactivity disorder, and in the control of human behavior and emotional states. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RETWGKKIDFLLSVIGFAVDLGNVWRFPYLCYKNGGGAFLIPYLIMLIFGGLPLFYMELALGQFNRSGCI
TVWKKICPLFKGVGYAICIIAFYVAFYYNVIIAWALYYLFSSFTSELPWTSCNNPWNTPNCTDVSNRNNS
SSINGTGLTSPAEEYFERKVLELQKSEGIDDLGPIKWQLALCLFAVFIIVYFSLWKGVKSSGKVVWVTAT
MPYVVLSILLIRGLTLPGASDGIKYYLTPDFSKLKDPEVWIDAATQIFFSLGPGFGVLLALSSYNKFHNN
CYRDALVTSSINCATSFFSGFVIFSVLGYMAHKQNVPIEDVATEGPGLVFIVYPEAIATLPGSTFWAIIF
FLMLITLGLDSTFGGLEAVITGLCDEFPFLSRRRELFVLGLVIICFLLALPTVTYGGIYVVTLLDRYAAG
ISILFIVFFEAVAVSWFYGVDRFSDDIEEMLGFRPGLYWRVCWKFISPIFLLFIVIFSLVSYEPLQYQDY
VYPPWANVVGWVIACSSIVLIPIYAIYKLISTPGTFRQRIAYCITPE
>gnl|CDD|212067 cd11498, SLC6sbd_GlyT1, Na(+)- and Cl(-)-dependent glycine transporter GlyT1; solute-binding domain. GlyT1 is a membrane-bound transporter that re-uptakes glycine from the synaptic cleft. Human GlyT1 is encoded by the SLC6A9 gene. GlyT1 is expressed in brain, pancreas, uterus, stomach, spleen, liver, and retina. GlyT1 may play a role in schizophrenia. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
NGAVPGEATKRDENLKRGNWGNQIEFVLTSVGYAVGLGNVWRFPYLCYRNGGGAFMFPYFIMLVFCGIPL
FFMELSFGQFASQGCLGVWRVSPMFKGVGYGMMVVSTYIGIYYNVVICIAFYYFFMSMTRVLPWTYCNNP
WNTPDCAGVLSTNRSNATFANMSAVVSNLTELLNRTLKRTSPSEEYWRRYVLNISDDIGNFGEVRLPLLG
CLGVSWLVVFLCLIRGVKSSGKVVYFTATFPYVVLTILFIRGITLEGAISGIMYYLTPQWDKILDAKVWG
DAASQIFYSLGCAWGGLITMASYNKFHNNCYRDSIIISITNCATSVYAGFVIFSILGFMANHLGVDVSEV
ADHGPGLAFVAYPEALTLLPISPLWSLLFFFMLILLGLGTQFCLLETLVTAVVDEIGNDWIIRNKTYVTL
GVAIIGFLLGIPLTTQAGIYWLLLMDNYAASFSLVIISCIMCIAIMYIYGHRNYFKDIEMMLGFPPPLFF
QICWRFVSPAIIFFILIFTVIQYRPITYNDYVYPGWAIVIGFLMALSSVICIPIYAIFKICMSEGDTFLE
RLKNAVKPSKDWGPALQEHRTGRYA
>gnl|CDD|271389 cd11499, SLC6sbd_GlyT2, Na(+)- and Cl(-)-dependent glycine transporter GlyT2; solute-binding domain. GlyT2 (also called NET1) is a membrane-bound transporter that re-uptakes glycine from the synaptic cleft. Human GlyT2 is encoded by the SLC6A5 gene. GlyT2 is expressed in brain and spinal cord. GlyT2 may play a role in pain, and in spasticity. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RGNWSNKLDFILSMVGYAVGLGNVWRFPYLAFQNGGGAFLIPYLIMLALAGLPIFLLEVSLGQFASQGPV
SVWKAIPALQGCGIAMLIISVLIAIYYNIIMCYTLFYLFASLVEVLPWASCNNPWNTPECKDKDMLLLDS
CIISDRPIIQIKNSTFCMTAYPNVTMVNFTSVDNKTFVSGSEEYFKYNVLKISAGIEYPGEIRWPLAACL
FLAWLIVYASLAKGIKTSGKVVYFTATFPYVVLVILLIRGVTLPGAGSGIWYFITPKWEKLNDATVWKDA
ATQIFFSLSAAWGGLITLSSYNKFHNNCYRDTLIVTCTNSATSIFAGFVIFSVIGFMAHELKVPIESVAD
QGPGIAFVVYPEALTRLPLSPFWAIIFFLMLLTLGLDTMFATIETIVTSVSDEFPKYLRTHKPQFTLVCC
LSFFIMGFPMITQGGIYMLQLVDTYAASYSLVIIAIFELVGISYIYGLQRFCEDIEMMIGFQPNKFWKVC
WAFVTPTILTFILAFSFYQWEPMTYGSYTYPNWSMVLGWLMLACSVIWIPIMFVIKMHLAPGSFIERLKL
VCSPQPDWGPFLAKHRGERYKNMIDPLGTSSLGLKLP
>gnl|CDD|271390 cd11500, SLC6sbd_PROT, Na(+)- and Cl(-)-dependent L-proline transporter PROT; solute-binding domain. PROT is a high-affinity L-proline transporter that transports L-proline, and may have a role in excitatory neurotransmission. Human PROT is encoded by the SLC6A7 gene, a potential susceptible gene for asthma. PROT is expressed in the brain. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RGQWGGKLEFLLSCIGYCVGLGNVWRFPYLCYRNGGGAFLIPYFIMLAFCGIPLFFMELSLGQYGSLGPL
TVWKCCPIFKGIGYGMLLVSGLVCIYYNVIIAWTLFYLFASFTSVLPWEHCGNWWNTESCLEHRGNGALT
VNLTRTVSPSEEYWNRRVLGIQGSSGIGDPGEVRWELALCLLLAWVIVFFCLFKGVKSSGKVVYFTATFP
YIILIVLLVRGVTLEGALKGIQFYLTPDFHRLASSQVWYDAASQIFYSLGIGFGGLLTMASYNKFNNNIY
RDTLIITLGNCITSVFAGFAIFSVLGHMAHELGVPVKDVADAGPGLAFVAYPEALTLLPVSPFWSILFFF
MLLTLGLDSQFAMLETIVTAVTDEFPYLLRKYKTWFLGLICVGMYLLGLLLVTDGGMYWLTLMDWYSASF
GLMVLALFMCLAISWVYGIQRFCRDIKMMIGFEPNLYFKACWMFISPALLLFILVYSIVKYQPSEYGSYR
YPPWAELLGILMGLLSCLMIPIGAIVAILREEGSLWERLKQACRPAMDWGP
>gnl|CDD|271391 cd11501, SLC6sbd_ATB0, Na(+)- and Cl(-)-dependent beta-alanine transporter ATB0+; solute-binding domain. ATB0+ (also known as the beta-alanine carrier) is a transmembrane transporter with a broad substrate specificity; it can transport non-alpha-amino acids such as beta-alanine with low affinity, and can transport dipolar and cationic amino acids such as leucine and lysine, with a higher affinity. It may have a role in the absorption of essential nutrients and drugs in the distal regions of the human gastrointestinal tract. Human ATB0+ is encoded by the SLC6A14 gene. ATB0+ is expressed in the lung, trachea, salivary gland, mammary gland, stomach, and pituitary gland. ATB0+ may play a role in obesity, and its upregulation may have a pathogenic role in colorectal cancer. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RGNWSKKSDYLLSMIGYAVGLGNVWRFPYLTYKNGGGAFLIPYTIMLALAGLPLFFMECSLGQFASLGPI
SVWRILPLFQGVGITMVLISTFVAIYYNVIIAYSLYYLFASFQSELPWSDCFSWADENCSKTPIVTHCNV
STANNGIHENKSWVDINNLTCINGSIIYQPGQLPSEQYWNKVALQRSSGMDETGVIVWYLALCLLLSWII
VGAALFKGIKSSGKVVYFTALFPYVVLLILLVRGATLEGASDGIEYYIGAQSNITKLMEAEVWKDAATQI
FYSLSVAWGGLVALSSYNKFHNNCYSDAIVVCVTNCLTSVFAGFAIFSVLGHMAHVSGRPVSEVVDSGFD
LAFIAYPEALSKLPISPLWSILFFFMLLTLGLDSQFASIETITTTIQDAYPKVMKKMRIPITLGVCVILF
LLGLVCVTQAGIYWVNLIDHFCAGWGILFAAVLELVGIIWIYGGNRFIEDIEMMIGAKSWIFWLWWRACW
FFITPVLLIAILIWSLVTFHSPTYGSVPYPDWGTALGWCMIIFCLIWIPIVAVIKIIKAKGNLFQRIKSC
CRPTSNWGPYLECHRGERYKHMVDPKKEKDHEIPTVSGSTKP
>gnl|CDD|271392 cd11502, SLC6sbd_NTT5, Neurotransmitter transporter 5; solute-binding domain. Human NTT5 is encoded by the SLC6A16 gene. NTT5 is expressed in testis, pancreas, and prostate; its expression is predominantly intracellular, indicative of a vesicular location. Its substrates are unknown. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RPLWSKKTEYILAQVGFSVGLSSIWRFPYLWHHNGGGSFLLIYILMLFLVGIPLLFLEMAVGQRLRQGSI
GVWKILSPWLGGVGYSSFLVCFIVGLYNNVLNSWSLFYLSQSFQFPLPWEKCPLVKNSSDFDPECARTTP
SQYFWYRQTLKASDRIEDGGVLVLSLTLSLFLAWCLLCVFMINGLKSTGKMLYVLVLLPYIILLCFLIRT
LFLEGAKFGLKHLLVAKVSALYSLSVWRQAGGQVLYSLGLGFGTIISFSSYMPRSNNCLKDAFLVALVNL
VTSLLTTPFIFAVLGFWATPASIYLSWLNNLPQHIKSQVLSKVPECSIQKQKEKIMEGPGFAFLAFSEAI
SLFPGSSFWSILFFLMLLILGLSTMLGIMQGIITPLQDTFSFFRKHPKLLTVGVCLLMFLCSLIFTRPSG
SYYVSLLDDYWVPMPIIFIVICENLAVAWAYGAKRFLADLMILLGHPISPIFTWLWCYLTPVVLLVLFTI
TLIQLYVKPITYLAWDSSTSHEVTRPYPSWALGLVIFLSVIVLLP
>gnl|CDD|271393 cd11503, SLC5sbd_NIS, Na(+)/iodide cotransporter NIS and related proteins; solute-binding domain. NIS (product of the SLC5A5 gene) transports I-, and other anions including ClO4-, SCN-, and Br-. NIS is expressed in the thyroid, colon, ovary, and in human breast cancers. It mediates the active transport and the concentration of iodide from the blood into thyroid follicular cells, a fundamental step in thyroid hormone biosynthesis, and is the basis of radioiodine therapy for thyroid cancer. Mutation in the SLC5A5 gene can result in a form of thyroid hormone dysgenesis. Human NIS exists mainly as a dimer stabilized by a disulfide bridge. This subgroup belongs to the solute carrier 5 (SLC5) transporter family
WDYGVFAAMLLVSTGIGLFVGLARGGQRSADDFFTGGRGLSAVPVGLSLSASFMSAVQVLGVPSEAYRYG
LKFLWMCLGQLLNSLMTAVLFMPVFYRLGITSTYQYLEMRFSRAVRLCGTLQFIVATMLYTGIVIYAPAL
ILNQVTGLDIWASLFSTGIICTFYTTVGGMKAVIWTDVFQVVVMLSGFWAVLIRGVILVGGPRRVLEIAQ
NHSRINFMDFDPDPRRRYTFWTFVVGGTLVWLSMYGVNQAQVQRYVACRTEKQAKLALLVNQVGLCLIVS
SAATCGIVMFVYYSNCDPLLIGRISAPDQYMPYLVLDIFEDLPGVPGLFLACAYSGTLSTASTSINAMAA
VTVEDLIKPRLPTIAPRKLVFISKGLSLIYGSACITVAALSSLLGGGVLQGSFTVMGVISGPLLGAFALG
MFLPACNTPGVFSGLAVGLALSLWVAVGATIYPPSEQTMGVLPTSAAQCLTTNVTLNTTGSVNASSVPPS
SGMDNIRPALADYFYALSYLYYGAVGTLTTYICGALISDLTGPTK
>gnl|CDD|271394 cd11504, SLC5sbd_SMVT, Na(+)/multivitamin cotransporter SMVT and related proteins; solute-binding domain. This multivitamin transporter SMVT (product of the SLC5A6 gene) transports biotin, pantothenic acid and lipoate, and is essential for mediating biotin uptake into mammalian cells. SMVT is expressed in the placenta, intestine, heart, brain, lung, liver, kidney and pancreas. Biotin may regulate its own cellular uptake through participation in holocarboxylase synthetase-dependent chromatin remodeling events at SMVT promoter loci. The cis regulatory elements, Kruppel-like factor 4 and activator protein-2, regulate the activity of the human SMVT promoter in the intestine. Glycosylation of the hSMVT is important for its transport function. This subgroup belongs to the solute carrier 5 (SLC5) transporter family
FHVADYVVFSLLLVISAGIGLYYACTGGKQKTTREFLMADRKMGCLPVALSLLATFQSAVAILGGPSESY
TFGTQYWFLGCSYFLGLLIPAHVFIPVFYRLELTSAYEYLELRFNKTVRICGTVTFIFQMVIYMGVVLYA
PALALNAVTGFNLWISVLAMGVVCTFYTALGGLKAVIWTDVFQTVVMFAGQLAVIIVGSIEAGGIARVWR
VAAESDRIDGFNLSPDPTIRHTFWTLVVGGVFNMLALYGVNQAQVQRYLSSRTEKQAKRSCYLVFPGQQL
SLCIGCLCGLVMFARYHECDPLKNGIVARSDQLVPYFVMDVLDGLPGLPGLFIACLFSGALSTISSAFNS
LATVTMEDLIVPKFPDMTEERATLLSKGLAVGYGLLCLLMAYLASTMGQVLQAANSIFGMIGGPLLGLFC
LGMFFPCANSAGAVVGLLAGLFMAFWIGIGSKVFPPYSPTKSTPINDCIFPNVTMANATTPTTPFATPTD
EPPPGLAELYSLSYMWYSAHNSTTVVVVGLLVSLLTG
>gnl|CDD|271395 cd11505, SLC5sbd_SMCT, Na(+)/monocarboxylate cotransporters SMCT1 and 2 and related proteins; solute-binding domain. SMCT1 is a high-affinity transporter of various monocarboxylates including lactate and pyruvate, short-chain fatty acids, ketone bodies, nicotinate and its structural analogs, pyroglutamate, benzoate and its derivatives, and iodide. Human SMCT1 (hSMCT1, also called AIT) is encoded by the tumor suppressor gene SLC5A8. SMCT1 is expressed in the colon, small intestine, kidney, thyroid gland, retina, and brain. SMCT1 may contribute to the intestinal/colonic and oral absorption of monocarboxylate drugs. It also mediates iodide transport from thyrocyte into the colloid lumen in thyroid gland and, through transporting L-lactate and ketone bodies, helps maintain the energy status and the function of neurons. SMCT2 is a low-affinity transporter for short-chain fatty acids, lactate, pyruvate, and nicotinate. hSMCT2 is encoded by the SLC5A12 gene. SMCT2 is expressed in the kidney, small intestine, skeletal muscle, and retina. In the kidney, SMCT2 may initiate lactate absorption in the early parts of the tubule, SMCT1 in the latter parts of the tubule. In the retina, SMCT1 and SMCT2 may play a differential role in monocarboxylate transport in a cell type-specific manner. This subgroup belongs to the solute carrier 5 (SLC5) transporter family
IGNFAVWDYVVFAAMLFISAGIGIYYAFAGGGQATSKDFLMGGRQMTAVPVALSLTASFMSAVTVLGTPS
EVYRFGASFLIFAFAYLFVVLISSEVFLPVFYRLGITSTYEYLELRFNKPVRLAGTVLFIVQTILYTGIV
IYAPALALNQVTGFDLWGAVVATGVVCTFYCTLGGLKAVVWTDVFQVGIMVAGFLSVIIQAVVHQGGIHN
ILNDSYNGSRLNFWDFDPNPLRRHTFWTITVGGTFTWTGIYGVNQSQVQRYISCKTRFQAKLSLYFNLLG
LWAILVCAVFSGLAMYSHYKDCDPWTAKIVSAPDQLMPYLVLDILADYPGLPGLFVACAYSGTLSTVSSS
INALAAVTVEDLIKPYFRSLSEKLSSWISKGLSLLYGAMCIGMAVAASLMGGLLQAALSIFGMVGGPLLG
LFSLGILFPFVNSKGALGGLLTGFAISLWVGIGAQIYPPPPSKTLPLPLSTDGCNKTNVEANGPPTTEMP
FTTSVFQIYLSSRPGLADTWYSLSYLYFSTVGTLVCILVGVIVSLITG
>gnl|CDD|212075 cd11506, SLC6sbd_GAT1, Na(+)- and Cl(-)-dependent GABA transporter 1; solute-binding domain. GAT1 transports gamma-aminobutyric acid (GABA). GABA is the main inhibitory neurotransmitter within the mammalian CNS. Human GAT1 is encoded by the SLC6A1 gene. GAT1 is expressed in brain and peripheral nervous system. The antiepileptic drug, Tiagabine, inhibits GAT1. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
ATNGTKVADGQISTEVSEAPIANDKPKTLVVKVQKKKTDLPDRDTWKGKFDFLMSCVGYAIGLGNVWRFP
YLCGKNGGGAFLIPYFLTLIFAGVPLFLLECSLGQYTSIGGLGVWKLAPMFKGVGLAAAVLSFWLNIYYI
VIIAWAIYYLYNSFTTTLPWKSCDNPWNTDRCFSNYSMANTTNMTSAVVEFWERNMHQMTDGLEKPGQIR
WPLAITLAIAWVLVYFCIWKGVGWTGKVVYFSATYPYIMLFILFFRGVTLPGAKEGILFYITPNFSKLSD
SEVWLDAATQIFFSYGLGLGSLIALGSYNPFHNNVYRDSIIVCCINSCTSMFAGFVIFSIVGFMAHVTKR
PIADVAASGPGLAFLAYPEAVTQLPISPLWAVLFFSMLLMLGIDSQFCTVEGFITALVDEFPRLLRNRRE
IFIAVVCIVSYLIGLSNITQGGIYVFKLFDYYSASGMSLLFLVFFECVSISWFYGVNRFYDNIEEMVGYR
PCIWWKLCWSFFTPIIVAGVFLFSAVQMTPLTMGNYVFPKWGQGVGWFMALSSMVLIPGYMAYMFLTLKG
SLKQRLQVMIQPTEDIVTPENGPEQQQQSNSANKEAYI
>gnl|CDD|271396 cd11507, SLC6sbd_GAT2, Na(+)- and Cl(-)-dependent GABA transporter 2; solute-binding domain. This family includes human GAT2 (hGAT2) which transports gamma-aminobutyric acid (GABA). GABA is the main inhibitory neurotransmitter within the mammalian CNS. hGAT2 is encoded by the SLC6A13 gene, and is similar to mouse GAT-3, and rat GAT2. hGAT2 is expressed in brain, kidney, lung, and testis. hGAT2 is a potential drug target for treatment of epilepsy. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RGQWNNKVEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYLIFLFTCGIPVFFLETALGQYTSQGGV
TAWRKICPLFEGIGYASQVIVMLLNCYYIIVLAWALFYLFSSFTIDLPWGSCGHEWNTENCMEFQKANST
LNVTSENATSPVIEFWERRVLKISDGIQHLGSLRWELALCLLLAWIICYFCIWKGVKSTGKVVYFTATFP
YLMLVVLLIRGVSLPGALQGIQFYLYPDLSRLQDPQVWMDAGTQIFFSYAICLGCLTALGSYNKYHNNCY
RDCIALCFLNSGTSFVAGFAIFSILGFMAEEQGVPISEVAESGPGLAFIAYPRAVVMLPFSPLWACFFFF
MVVLLGLDSQFVCVESLVTALVDMYPTIFRKKNRRELLILAVSIVSFLVGLIMLTEGGMYVFQLFDYYAA
SGMCLLFVAIFETLCVAWVYGADRFYDNIEDMIGYRPWAIIKYCWLFITPAVCMATFLFSLIKYTPLTYN
KKYVYPWWGDALGWLLALSSMVCIPLWVGYKLSTIKGSLRERFRQLTCPDEDLP
>gnl|CDD|212077 cd11508, SLC6sbd_GAT3, Na(+)- and Cl(-)-dependent GABA transporter 3; solute-binding domain. This family includes human GAT3 (hGAT3) a high-affinity transporter of gamma-aminobutyric acid (GABA). GABA is the main inhibitory neurotransmitter within the mammalian CNS. hGAT3 is encoded by the SLC6A11 gene, and is similar to mouse GAT4, and rat GAT3/GATB. GAT3 is expressed primarily in the glia of the brain, and is a potential drug target for antiepileptic drugs. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
ERGHWNNKVEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFLIPYVVFFICCGIPVFFLETALGQFTSEGG
ITCWRKVCPLFEGIGYATQVIEAHLNVYYIIILAWAIFYLFNCFTTELPWATCGHEWNTENCVEFQKLNS
SNCSHVSLQNATSPVMEFWERRVLAISDGIEHIGNLRWELALCLLAAWTICYFCIWKGTKSTGKVVYVTA
TFPYIMLLILLIRGVTLPGASEGIKFYLYPDLSRLSDPQVWVDAGTQIFFSYAICLGCLTALGSYNNYNN
NCYRDCIMLCCLNSGTSFVAGFAIFSVLGFMAYEQGVPIAEVAESGPGLAFIAYPKAVTMMPLSPLWATL
FFMMLIFLGLDSQFVCVESLVTAVVDMYPKVFRRGYRRELLILALSIVSYFLGLVMLTEGGMYIFQLFDS
YAASGMCLLFVAIFECICIGWVYGSNRFYDNIEDMIGYRPLSLIKWCWMVITPGICAGIFIFFLVKYKPL
KYNNVYTYPDWGYGIGWLMALSSMICIPLWICIKMWKTEGTFPEKLQKLTTP
>gnl|CDD|271397 cd11509, SLC6sbd_CT1, Na(+)- and Cl(-)-dependent creatine transporter 1; solute-binding domain. CT1 (also called CRTR, CRT) transports creatine. Human CT1 is encoded by the SLC6A8 gene. CT1 is ubiquitously expressed, with highest levels found in skeletal muscle and kidney. Creatine is absorbed from food or synthesized from arginine and plays an important role in energy metabolism. Deficiency in human CT1 leads to X-linked cerebral creatine transporter deficiency. In males, this disorder is characterized by language and speech delays, autistic-like behavior, seizures in about 50% of cases, and can also involve midfacial hypoplasia, and short stature. In females, it is characterized by mild cognitive impairment with behavior and learning problems. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RETWTRQMDFIMSCVGFAVGLGNVWRFPYLCYKNGGGVFLIPYLLIAFVGGIPIFFLEIALGQFMKAGGI
NAWNIAPLFKGLGYASMVIVFFCNTYYIMVLAWGFYYLVKSFTNTLPWATCGNPWNTPNCTEIFRHADCN
NGASSAGSLANLTCDELANRRSPVIEFWERKVLRLSGGLEEPGALNWELTLCLLATWVLVYFCVWKGVKS
TGKVVYFTATFPYVVLVVLLVRGVTLPGALDGIIYYLKPDWSKLGEAQVWIDAGTQIFFSYAIGLGALTA
LGSYNRFHNNCYKDAFILALINSGTSFFAGFVVFSILGFMASEQGVDISKVAESGPGLAFIAYPKAVTLM
PVAPLWAALFFFMLLLLGLDSQFVGVEGFITGILDLLPAKYYFRYQREVVVALCCLLCFLIDLSMVTEGG
MYVFQLFDYYSASGTTLLWQAFWECVVVAWVYGADRFMDDIARMIGYRPLPWMKWCWSVITPLVCMGIFL
FHVVNYKPLTYNKTYVYPWWGEAIGWCLALSSMLCIPLTVLYKLLRAKGSLKERWQKLTTPVWGLHHLEY
RAPDADVRGLPTLLPVSEEEKVVIFESVM
>gnl|CDD|271398 cd11510, SLC6sbd_TauT, Na(+)- and Cl(-)-dependent taurine transporter; solute-binding domain. TauT is a Na(+)- and Cl(-)-dependent, high-affinity, low-capacity transporter of taurine and beta-alanine. Human TauT is encoded by the SLC6A6 gene. TauT is expressed in brain, retina, liver, kidney, heart, spleen, and pancreas. It may play a part in the supply of taurine to the intestinal epithelium and in the between-meal-capture of taurine. It may also participate in re-absorbing taurine that has been deconjugated from bile acids in the distal lumen. Functional TauT protects kidney cells from nephrotoxicity caused by the chemotherapeutic agent cisplatin; cisplatin down-regulates TauT in a p53-dependent manner. In mice, TauT has been shown to be important for the maintenance of skeletal muscle function and total exercise capacity. TauT-/- mice develop additional clinically important diseases, some of which are characterized by apoptosis, including vision loss, olfactory dysfunction, and chronic liver disease. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
REKWASKIDFLLSVAGGFVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGGGLPVFFLEVALGQYTSEGGI
TCWEKLCPIFTGIGYASIVIVSLLNIYYIVILAWALYYLFQSFQSELPWAHCNQKWNTPCCVEDTLRKNK
TLWASINATNFTSPVTEFWERNVLSLSAGIEHVGTIKWDLALCLLLVWVVCFFCIWKGVKSTGKVVYFTA
TFPFLMLIVLLIRGVTLPGAAEGIKFYLYPDITRLGDPQVWIDAGTQIFFSYAICLGAMTSLGSYNKYKY
NCYRDCLLLGCLNSGTSFVSGFAIFSVLGFMAQEQGVDIADVAESGPGLAFIAYPKAVTMMPLPTFWAIL
FFIMLLLLGLDSQFVEVEGQITSLVDLYPSFLRKGYRREIFIAIVCFISYLLGLTMVTEGGMYVFQLFDY
YAASGVCLLWVAFFECIAVAWVYGGDNMYDAIEDMIGYRPGPWMKYSWIVITPVLCVGCFIFSLVKYEPL
TYNKVYVYPEWAIGLGWVLALSSMICIPMVAVIRIIQTDGPLIERIKALTTP
>gnl|CDD|212080 cd11511, SLC6sbd_BGT1, Na(+)- and Cl(-)-dependent betaine/GABA transporter-1, and related proteins; solute-binding domain. BGT1 is a relatively low-affinity transporter of gamma-aminobutyric acid (GABA), and can also transport betaine. GABA is the main inhibitory neurotransmitter within the mammalian CNS. Human BGT1 is encoded by the SLC6A12 gene, and is similar to mouse GAT2. Mouse GAT2 plays a role in transporting GABA across the blood-brain barrier. In addition to being expressed in cells of the central nervous system, BGT1 is expressed in peripheral tissues, including kidney, liver, and heart. An association has been shown between the SLC6A12 gene and the occurrence of aspirin-intolerant asthma, and BGT1 is a drug target for antiepileptic drugs. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
ERGQWRNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFLIPYLIFLFTCGIPLFFLETALGQYTSQGG
VTAWRKICPIFEGIGYASQVIESYLNVYYIIILSWALFYLFSSFTSVLPWATCNNPWNSDLCVDFLNHSG
ADNRTPPENATSPVMEFWEKRVLGLTDGIHKLGTVRWELALCLLLAWIICYFCIWKGVKSTGKVVYFTAT
FPYLMLVILLVRGVTLPGAAEGIIFYLKPDLSRLADPQVWMDAGTQILFSYAICQGCLTALGSYNKYTNN
CYRDCIMLCFLNSATSFVAGFAIFSVLGFMAREQGVPISEVAESGPGLAFIAYPTAVTMMPVSQLWSCLF
FLMLIFLGLDSQFVCVESMVTASIDMFPGVFRKKGRRELLILAIAVICYLLGLLLVTEGGMYIFQLFDYY
AASGTCLLFLAIFEVICIGWVYGANRFYDNIEDMIGYRPWPLIKICWLVFTPGLCLAVFLFSLIKYTPLK
YNNSYVYPPWGYVLGWLMALSSMVCIPLYAIFILLKTKGSLKQRLMQLISP
>gnl|CDD|212081 cd11512, SLC6sbd_NET, Na(+)- and Cl(-)-dependent norepinephrine transporter NET; solute-binding domain. NET (also called NAT1, NET1), is a transmembrane transporter that transports the neurotransmitter norepinephrine from synaptic spaces into presynaptic neurons. Human NET is encoded by the SLC6A2 gene. NET is expressed in brain, peripheral nervous system, adrenal gland, and placenta. NET may play a role in diseases or disorders including depression, orthostatic intolerance, anorexia nervosa, cardiovascular diseases, alcoholism, and attention-deficit hyperactivity disorder. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RETWGKKIDFLLSVVGFAVDLANVWRFPYLCYKNGGGAFLIPYTLFLIIAGMPLFYMELALGQYNREGAA
TVWKICPCFKGVGYAVILIALYVGFYYNVIIAWSLYYLFSSFTSELPWTTCGNVWNSPNCTDPKLLNASV
LGNGTKYSKYKLTPAAEFYERGVLHLHESAGIHDLGLPRWQLTLCLFVVVIVLFFSLWKGVKTSGKVVWI
TATLPYVVLFVLLIHGVTLPGAFNGINAYLHIDFKRLKEATVWIDAATQIFYSLGAGFGVLIAFASYNKF
DNNCYRDALLTSTINCVTSFISGFAIFSILGYMAHEHKVKIEDVATEGAGLVFILYPEAISTLSGSTFWA
VVFFIMLLTLGIDSSMGGMEAVITGLADDFSILKKHRKLFTFGVAFITFLLALFCITNGGIYVLTLLDTF
AAGTSILFAVLMEAIGVSWFYGVDRFSDDIQQMMGFRPGLYWRLCWKFVSPAFLLFVVIVSIINFKPLTY
DDYNFPPWANRTGWGIALSSMLLVPIYVIYKFFTVPGTFEERLAYCITPENEHYLVAQGDIRQFKLQHWL
>gnl|CDD|271399 cd11513, SLC6sbd_SERT, Na(+)- and Cl(-)-dependent serotonin transporter SERT; solute-binding domain. SERT (also called 5-HTT), is a transmembrane transporter that transports the neurotransmitter serotonin from synaptic spaces into presynaptic neurons. The antiport of a K+ ion is believed to follow the transport of serotonin and promote the reorientation of SERT for another transport cycle. Human SERT is encoded by the SLC6A4 gene. SERT is expressed in brain, peripheral nervous system, placenta, epithelium, and platelets. SERT may play a role in diseases or disorders including anxiety, depression, autism, gastrointestinal disorders, premature ejaculation, and obesity. It may also have a role in social cognition. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RETWGKKMDFLLSVIGYAVDLGNVWRFPYICYQNGGGAFLIPYTIMAIFGGIPLFYMELALGQYHRNGCI
SIWRKICPIFKGIGYAICIIALYVASYYNTIIAWALYYLYSSFTDELPWTSCNNSWNTGNCTNYFAKDNI
TWTLHSTSPAEEFYTRHVLQVHRSKGLGDLGGISWQLTLCLFLIFTIVYFSIWKGVKTSGKVVWVTATFP
YIVLFILLVRGATLPGAWRGVVFYLKPNWQKLLETGVWVDAAAQIFFSLGPGFGVLLALASYNKFNNNCY
QDALVTSVVNCLTSFVSGFVIFTVLGYMAEMRNEDVSEVAKDAGPSLLFITYAEAIANMPASTFFAIIFF
LMLITLGLDSTFAGLEGVITAVLDEFPHVWSKRREKFVLGLVIVCFLGSLATLTFGGAYVVKLLEEYATG
PAVLTVVLLEAVAVSWFYGITQFCNDVKEMLGFSPGWFWRVCWVAISPLFLLFIICSFLMNPPQLRLFDY
NYPYWSIVVGYCIGTSSIICIPIYMAYRLIITPGTLKERIIKSITPE
>gnl|CDD|212083 cd11514, SLC6sbd_DAT1, Na(+)- and Cl(-)-dependent dopamine transporter 1; solute-binding domain. DAT1 (also called DAT), is a plasma membrane transport protein that functions at the dopaminergic synapses to transport dopamine from the extracellular space back into the presynaptic nerve terminal. Human DAT1 is encoded by the SLC6A3 gene, and is expressed in the brain. DAT1 may play a role in diseases or disorders related to dopaminergic neurons, including attention-deficit hyperactivity disorder (ADHD), Tourette syndrome, Parkinson's disease, alcoholism, drug abuse, schizophrenia, extraversion, and risky behavior. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RETWGKKIDFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLVPYLFFMVIAGMPLFYMELALGQFNREGAA
GVWKICPIFKGVGFTVILISLYVGFFYNVIIAWALFYLFSSFTGELPWIHCNNSWNSPNCSDAHPGDSSG
DSSGLNDTYKTTPAAEYFERGVLHLHESHGIHDLGPPRWQLTSCLVVVIVLLYFSLWKGVKTSGKVVWIT
ATMPYVVLTALLLRGVTLPGAIDGIKAYLSVDFLRLCEASVWIDAATQICFSLGVGFGVLIAFSSYNKFT
NNCYRDAIITTSINSLTSFFSGFVVFSFLGYMAQKHNVPIGDVAKDGPGLIFIIYPEAIATLPLSSVWAV
IFFIMLLTLGIDSAMGGMESVITGLIDEFKFLHRHRELFTLFIVLSTFLISLFCVTNGGIYVFTLLDHFA
AGTSILFGVLIEAIGIAWFYGVGRFSDDIEEMIGQRPGLYWRLCWKFVSPCFLLFVVVVSIVTFRPPKYG
SYIFPDWANMVGWCLAISSMAMVPLYAIYKFCSLPGSFREKLAYAITPEKEHELVDRGEVRQFTL
>gnl|CDD|271400 cd11515, SLC6sbd_NTT4-like, Na(+)-dependent neurotransmitter transporter 4, and related proteins; solute-binding domain. This subgroup includes the solute-binding domain of NTT4 (also called XT1) and SBAT1 (also called B0AT2, v7-3, NTT7-3); both these proteins can transport neutral amino acids. Human SBAT1 is encoded by the SLC6A15 gene, a susceptibility gene for major depression. SBAT1 is expressed in brain, and may have a role in transporting neurotransmitter precursors into neurons. Human NTT4 is encoded by the SLC6A17 gene. NTT4 is specifically expressed in the nervous system, in synaptic vesicles of glutamatergic and GABAergic neurons, and may play an important role in synaptic transmission. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RPAWNSKLQYILAQVGFSVGLGNVWRFPYLCQKNGGGAYLLPYLILLIVIGIPLFFLELSVGQRIRRGSI
GVWNYISPRLGGIGFASCVVCLFVALYYNVIIGWSLFYFSQSFQQPLPWDQCPLVKNASHTFVEPECEKS
SATTYYWYREALNISDSISESGGLNWKMTICLLAAWVIVCLAMIKGIQSSGKIMYFSSLFPYVVLICFLI
RALLLNGSVDGIRHMFTPKLEIMLEPKVWREAATQVFFALGLGFGGVIAFSSYNKRDNNCHFDAVLVSFI
NFFTSVLATLVVFAVLGFKIQKVKEEEFPALHLNPCLIEDELNKAVQGTGLAFIAFTEAMTHFPASPFWS
VMFFLMLVNLGLGSMFGTIEGITTPIVDTFKVRKEILTVICCLLAFCIGLIFVQRSGNYFVTMFDDYSAT
LPLLIVVILENIAVAFVYGIDKFMEDLKDMLGFRPYRYYYYMWKYISPLMLLSLLIASIVNMGLSPPGYN
AWIEDKASERFLSYPTWGMVLCISLIVVAILPIPVVFILR
>gnl|CDD|212085 cd11516, SLC6sbd_B0AT1, Na(+)-dependent neutral amino acids transporter, B0AT1; solute-binding domain. B0AT1 (also called HND) transports neutral amino acids. Human B0AT1 is encoded by the SLC6A19 gene. B0AT1 is expressed primarily in the kidney and intestine; it requires collectrin for expression in the kidney, and angiotensin-converting enzyme 2 for expression in the intestine. Interaction with these two proteins implicates B0AT1 in more complex processes such as glomerular structure, exocytosis, and blood pressure control. The autosomal recessive disorder, Hartnup disorder, is caused by mutations in B0AT1. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RPKWDNKAQYMLTCVGFCVGLGNVWRFPYLCQSHGGGAFMIPFLILLVFEGIPLLHLEFAIGQRLRKGSV
GVWSTIHPTLKGVGIASMCVSFLVSLYYNTIIAWVMWYFFNSFQEPLPWSQCPLNENRTGYIPECAKSSP
VDYFWYRETLNTSTSIDDSGGIQWWMVLCLACAWGVLYVCTIRGIETTGKAVYVTSTLPYLVLTIFLIRG
LTLKGSVNGIKFLFTPDINELANPVTWLDAGAQVFYSFSLAFGGLISFSSYNSVHNNCEKDAVIISVING
FTSIYAATVIYSIIGFRATERFDDCFDGNILTLINAFDLPEGNITQDNYQDMQQSLNSTDPDIISSLSLQ
TCDLNNFLSEGVEGTGLAFIVFTEAITKMPLSPLWSVLFFIMLFCLGLSSMFGNMEGVLVPLQDLKVIPK
SWPKEIITGLICLVSFLIGLIFVLGSGNYWLALFDSFAGSIPLLIIAFCEMFSVVYVYGIDRFNKDIEFM
IGHKPNIFWQATWRVISPLIMLVIFLFYFVVKVSQELFYSAWDPEYEEFPKSQKISYPTWIYVIIVILAG
VPSLAIPGYAIYKAIRNCCQK
>gnl|CDD|212086 cd11517, SLC6sbd_B0AT3, glycine transporter, B0AT3; solute-binding domain. B0AT3 (also called Xtrp2, XT2) transports glycine. Human B0AT3 is encoded by the SLC6A18 gene. B0AT3 is expressed in the kidney. Mutations in the SLC6A18 gene may contribute to the autosomal recessive disorder iminoglycinuria and its related disorder hyperglycinuria. SLC6A18 or its neighboring genes are associated with increased susceptibility to myocardial infarction. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
ERPKWDNKAQYLLSCIGFAVGLGNIWRFPYLCQTYGGGAFLIPYFIALVFEGIPLFHLELAIGQRLRKGS
IGVWTTISPYLGGVGLGCVTVSFLVSLYYNTILAWVLWYFLNSFQHPLPWSSCPLDLNRTGFVEECQGST
AVSYFWYRQTLNITPDINDSGSIQWWLLLCLAACWAIVYLCVIRGIETTGKVIYFTALFPYLVLTIFLIR
GLTLPGATEGLIYLFTPNMHILQNPRVWLDAATQIFFSLSLAFGGHIAFASYNPPRNDCEKDAVTIALVN
SMTSLYASIPVFSVLGFKATNDYEHCLDRNILSLINEFDFPEQSISRDNYPSVLMHLNATWPERVAQLPL
KACLLEDFLDKSASGPGLAFIVFTEAVLHMPGAQVWAVLFFGMLFTLGLSSMFGNVEGVITPLLDVGVLP
RWVPKEALTGLVCLVCFLSALCFTLQSGNYWLEIFDSFAASLNLLVIAFFEVVGVVYVYGIKRFCDDIEW
MTGRRPSLYWRLTWRVVSPLLLLTIFVAYIILLFQKPPSYKAWNPKYELFPSREEKLYPGWVQAICVLLS
LLPVLWVPVVALAQLL
>gnl|CDD|271401 cd11518, SLC6sbd_SIT1, Na(+)- and Cl(-)-dependent imino acid transporter SIT1; solute-binding domain. SIT1 (also called XTRP3, XT3, IMINO) transports imino acids, such as proline, pipecolate, MeAIB, and sarcosine. It has weak affinity for neutral amino acids such as phenylalanine. Human SIT1 is encoded by the SLC6A20 gene. SIT1 is expressed in brain, kidney, small intestine, thymus, spleen, ovary, and lung. SLC6A20 is a candidate gene for the rare disorder iminoglycinuria. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
EKTRPLWDNPLQFVFACISYAVGLGNVWRFPYLCQMYGGGGFLIPYLIMLILEGMPLLYLELAVGQLMRQ
GSIGAWKSISPYLGGVGVASVVVSFFLSMYYNVINAWAFWYLFHSFQDPLPWSNCPLNSNHTAYNEECEK
ASPTQYFWYRKTLNISPSILENGGIQWELAVCLILAWLVVYLCILRGTESTGKVVYVTALIPYLVLLIYL
IRGLTLHGAANGLAYMFTPKLEQLANPKTWINAATQIFFSLGLGFGSLIAFASYNEPSNNCERHAIIVSL
INSGTSIFASIVTFSIYGFKATFNYENCMKKVILLLTNTFDLEEGSVTTENLGDMKNYLASAFPQEYSSI
VPQIKNCSLEKELDTAVQGTGLAFIVYTEAIKNMEVSQLWSVLYFLMLLMLGIGSMLGNTAAILTPLTDS
KFISSHLPKEAISGLLCFTNCIIGLVFTMEAGNYWFDIFNDYAATLSLLLIVLVETIAVCYVYGLRRFEN
DLEAMTGHKLSWYWKIMWAFVSPLLIVSLFIFYLTDYIMTGTLQYQAWDATLGQLVTKDYPPYALAVIGL
LVAASTCCIPLVAIVN
>gnl|CDD|271402 cd11519, SLC5sbd_SMCT1, Na(+)/monocarboxylate cotransporter SMCT1 and related proteins; solute-binding domain. SMCT1 is a high-affinity transporter of various monocarboxylates including lactate and pyruvate, short-chain fatty acids, ketone bodies, nicotinate and its structural analogs, pyroglutamate, benzoate and its derivatives, and iodide. Human SMCT1 (hSMCT1, also called AIT) is encoded by the tumor suppressor gene SLC5A8. Its expression is under the control of the C/EBP transcription factor. Its tumor-suppressive role is related to uptake of butyrate, propionate, and pyruvate, these latter are inhibitors of histone deacetylases. SMCT1 is expressed in the colon, small intestine, kidney, thyroid gland, retina, and brain. SMCT1 may contribute to the intestinal/colonic and oral absorption of monocarboxylate drugs. SMCT1 also mediates iodide transport from thyrocyte into the colloid lumen in thyroid gland and through transporting l-lactate and ketone bodies helps maintain the energy status and the function of neurons. In the kidney its expression is limited to the S3 segment of the proximal convoluted tubule (in contrast to the low-affinity monocarboxylate transporter SMCT2, belonging to a different family, which is expressed along the entire length of the tubule). In the retina, SMCT1 and SMCT2 may play a differential role in monocarboxylate transport in a cell type-specific manner, SMCT1 is expressed predominantly in retinal neurons and in retinal pigmented epithelial (RPE) cells. This subgroup belongs to the solute carrier 5 (SLC5) transporter family
IGTFSVWDYVVFAGMLLISAGIGIYYAFAGGGQQTSKDFLMGGRQMTAVPVALSLTASFMSAVTVLGTPA
EVYRFGAIFSIFAFTYAIVVVISAEVFLPVFYRLGITSTYEYLELRFNKCVRLIGTSLFIVQTALYTGIV
IYAPALALNQVTGFDLWGAVVATGVVCTFYCTLGGLKAVIWTDVFQVGIMVAGFVSVIIRAVVLQGGIGT
ILNDSYYGGRLNFWDFDPNPLQRHTFWTIVIGGTFTWTSIYGVNQSQVQRYISCKTRFQAKMSLYVNLVG
LWAILSCAVLSGLAMYSIYKDCDPWTAKDVSAPDQLMPYLVLDILADYPGLPGLFVACAYSGTLSTVSSS
INALAAVTVEDLIKPYFRSLSERQLSWISMGMSVFYGALCIGMAGLASLMGALLQAALSIFGMVGGPLLG
LFALGILFPFANSIGALVGLMSGFAISLWVGIGAQIYPPLPEKTLPLPLSLEGCNSTYNETNWTTTPEMP
FTSVFTTQPSSRPPLADNWYSLSYLYFSTVGTLVTMLVGLLVSLITGGCKQN
>gnl|CDD|212089 cd11520, SLC5sbd_SMCT2, Na(+)/monocarboxylate cotransporter SMCT2 and related proteins; solute-binding domain. SMCT2 is a low-affinity transporter for short-chain fatty acids, lactate, pyruvate, and nicotinate. Human SMCT2 (hSMCT2) is encoded by the SLC5A12 gene. SMCT2 is expressed in the kidney, small intestine, skeletal muscle, and retina. In the kidney, it is expressed in the apical membrane of the proximal convoluted tubule, along the entire length of the tubule (in contrast to the high-affinity monocarboxylate transporter SMCT1, belonging to a different family, which is limited to the S3 segment of the tubule). SMCT2 may initiate lactate absorption in the early parts of the tubule. In the retina, SMCT1 and SMCT2 may play a differential role in monocarboxylate transport in a cell type-specific manner, SMCT2 is expressed exclusively in Muller cells. Nicotine transport by hSMCT2 is inhibited by several non-steroidal anti-inflammatory drugs. This subgroup belongs to the solute carrier 5 (SLC5) transporter family
VKNFVAWDYVVFAGLFLVSSGIGVFFAIKERKKATSKEFLVGGRQMSCGPVALSLTASFMSAVTVLGTPA
EVYRFGASFVLFFIAYTFVIIFTSELFLPVFYRSGITSTYEYLELRFNKPVRYAATLIYIVQTILYTGVV
VYAPALALNQVTGFDLWGSVFATGIVCTFYCTLGGLKAVVWTDAFQMVVMVVGFLTVLIQGSIHNGGFTN
VWETAYNGSRLNIFDFDVDPLRRHTFWTITVGGTFTWLGIYGVNQSTIQRCISCKTEKHAKLALYLNLLG
LWIILVCAVFSGLIMYSHYKDCDPWTSGFISAPDQLMPYFVMEIFSTMPGLPGLFVACAFSGTLSTVAAS
INALATVTFEDFVKSCFPHLSEKLSTWISKGLCILFGVMCTSMAVAASLMGGVVQAALSIHGMCGGPMLG
LFTLGIVFPFVNWKGALGGLLTGITLSFWVGIGAFIYPAPSSKTLPLELSTAGCILANSTATPTPATPIL
TSDRPLLADTWYSLSYLYYSAVGCLGCIAAGLLISFLTG
>gnl|CDD|271403 cd11521, SLC6sbd_NTT4, Na(+)-dependent neurotransmitter transporter 4; solute-binding domain. NTT4 (also called XT1) transports the neutral amino acids, proline, glycine, leucine, and alanine, and may play an important role in synaptic transmission. Human NTT4 is encoded by the SLC6A17 gene. NTT4 is specifically expressed in the nervous system, in synaptic vesicles of glutamatergic and GABAergic neurons. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RPAWNSKLQYILAQIGYSVGLGNVWRFPYLCQKNGGGAYLVPYLVLLIIIGIPLFFLELAVGQRIRRGSI
GVWNYICPRLGGIGYASCLVCFFVGLYYNVIIGWSIFYFFKSFQYPLPWSECPVVRNGSVAVVEAECEKS
SATTYFWYREALDISNSISESGGLNWKMTLCLLVAWSLVGMAMIKGIQSSGKVMYFSSLFPYVVLVCFLV
RGLLLRGAVDGILHMFTPKLDKMLDPQVWREAATQVFFALGLGFGGVIAFSSYNKQDNNCHFDAALVSFI
NFFTSVLATLVVFAVLGFKANIMNEKCVVENAEKILGYLNTNVLSHDLIPPHVNFSHLTTKDYNEMYRVI
MTVKEDHFKELGLDACLLEDELDKSVQGTGLAFIAFTEAMTHFPASPFWSVMFFLMLINLGLGSMIGTMS
GITTPIIDTFKVRKEVFTVGCCIFAFLVGLIFVQRSGNYFVTMFDDYSATLPLTVVVILENIAVAWIYGT
KKFMQELTEMLGFRPYQFYFYTWKYVSPICMAVLMTASIIQLGVSPPGYSAWIREEAAEKFLFYPTWAMA
LLITLIILASLPLPVVFILRQFHLVSDGS
>gnl|CDD|212091 cd11522, SLC6sbd_SBAT1, Sodium-coupled branched-chain amino-acid transporter 1; solute-binding domain. SBAT1 (also called B0AT2, v7-3, NTT7-3) is a high-affinity Na(+)-dependent transporter for large neutral amino acids, including leucine, isoleucine, valine, proline and methionine. Human SBAT1 is encoded by the SLC6A15 gene, a susceptibility gene for major depression. SBAT1 is expressed in brain, and may have a role in transporting neurotransmitter precursors into neurons. This subgroup belongs to the solute carrier 6 (SLC6) transporter family
RPAWNSKLQYILAQVGFSVGLGNVWRFPYLCQKNGGGAYLVPYLILLLVIGIPLFFLELSVGQRIRRGSI
GVWNYISPKLGGIGFASCIVCFFVALYYNVIIGWSLFYFSQSFQQPLPWDQCPLVKNASHTFVEPECEKS
SATTYYWYREALNISSSISESGGLNWKMTICLLAAWVMVCLAMIKGIQSSGKIMYFSSLFPYVVLICFLI
RALLLNGSVDGIRHMFTPKLEIMLEPKVWREAATQVFFALGLGFGGVIAFSSYNKRDNNCHFDAVLVSFI
NFFTSVLATLVVFAVLGFKANVINEKCIIQNSEKIIKLLKMGNLSQDIIPHHINFSSITAEDYNLVYDII
QKVKEEEFPALGLKSCQIEDELNKAVQGTGLAFIAFTEAMTHFPASPFWSVMFFLMLVNLGLGSMFGTIE
GIITPIVDTFKVRKEILTVICCLLAFCIGLIFVQRSGNYFVTMFDDYSATLPLLIVVILENIAVSFVYGI
DKFMEDLKDMLGFTPNRYYYYMWKYISPLVLLSLLVASVVQMGLSPPGYNAWIEDKATEEFLSYPTWGLV
VCISLVVLAILPVPVVFIIR
>gnl|CDD|212133 cd11523, NTP-PPase, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily. This superfamily contains enzymes that hydrolyze the alpha-beta phosphodiester bond of all canonical NTPs into monophosphate derivatives and pyrophosphate (PPi). Divalent ions, such as Mg2+ ion(s), are essential to activate a proposed water nucleophile and stabilize the charged intermediates to facilitate catalysis. These enzymes share a conserved divalent ion-binding motif EXX[E/D] in their active sites. They also share a highly conserved four-helix bundle, where one face forms the active site, while the other participates in oligomer assembly. The four-helix bundle consists of two central antiparallel alpha-helices that can be contained within a single protomer or form upon dimerization. The superfamily members include dimeric dUTP pyrophosphatases (dUTPases; EC 3.6.1.23), the nonspecific NTP-PPase MazG proteins, HisE-encoded phosphoribosyl ATP pyrophosphohydolase (PRA-PH), fungal histidine biosynthesis trifunctional proteins, and several uncharacterized protein families
QERIKEFRRERGWDKEEGPETRALKLAEEVGELAEAIRKEEGYGRSSAEDKENLAEELADVLWNLLILAN
KL
>gnl|CDD|211400 cd11524, SYLF, The SYLF domain (also called DUF500), a novel lipid-binding module. The SYLF domain is named after SH3YL1, Ysc84p/Lsb4p, Lsb3p, and plant FYVE, which are proteins that contain it. It is also called DUF500 and is highly conserved from bacteria to mammals. Some members, such as SH3YL1, Ysc84p, and Lsb3p, which represent the best characterized members of the family, also contain an SH3 domain, while family members from plants and stramenopiles also contain a FYVE zinc finger domain. Other members only contain a stand-alone SYLF domain. The SYLF domain of SH3YL1 binds phosphoinositides with high affinity, while the N-terminal SYLF domains of both Ysc84p and Lsb3p have been shown to bind and bundle actin filaments, as well as bind liposomes with high affinity
ELVDDAARVLKEFTSDPDKGIPPSLLQNAKGIAIFPSVVKAGFIVGGAGGSGVVLARDPDGTWSAPAFIS
LTGGSFGLQIGVQSTDLVLVFMTDRALDAFLSGKFTLGADASAAAGPVGRGAEAGTDTALGAEIYSYSRS
KGLFAGVSLEGSVISVDDDANRAYYGRPVSPEDILLGKVAPPPEAQPLREALAK
>gnl|CDD|211401 cd11525, SYLF_SH3YL1_like, The SYLF domain (also called DUF500), a novel lipid-binding module, of SH3 domain containing Ysc84-like 1 (SH3YL1) and similar proteins. This subfamily is composed of yeast Ysc84 (also called LAS17-binding protein 4, Lsb4p) and Lsb3p proteins, vertebrate SH3YL1 (SH3 domain containing Ysc84-like 1), and similar proteins. They contain an N-terminal SYLF domain (also called DUF500) and a C-terminal SH3 domain. SH3YL1 localizes to the plasma membrane and is required for dorsal ruffle formation. Ysc84p localizes to actin patches and plays an important role in actin polymerization during endocytosis. A study of the yeast SH3 domain interactome predicts that Lsb3p and Lsb4p may function as molecular hubs for the assembly of endocytic complexes. The SYLF domain of SH3YL1 binds phosphoinositides with high affinity, while the N-terminal SYLF domains of both Ysc84p and Lsb3p have been shown to bind and bundle actin filaments, as well as bind liposomes with high affinity
SECKKAAKILREFTEPSNRNGPDKLIPPHVLAKAKGLAIISVIKAGFLVSARAGSGLVVARLPDGTWSAP
SAIGIAGLGGGFEIGVEVTDFVIVLNSKSAVRAFSQGGSLTLGGNVSVAAGPLGRNAEAAGSASGLAAIF
SYSKTRGLFAGVSLEGSVLIERKDANRKFYGKDISAKDLLSGEVPPPPEADPLYRILDS
>gnl|CDD|211402 cd11526, SYLF_FYVE, The SYLF domain (also called DUF500), a novel lipid-binding module, of FYVE zinc finger domain containing proteins. This subfamily is composed of uncharacterized proteins from plants and stramenopiles containing a FYVE zinc finger domain followed by a SYLF domain (also called DUF500). The SYLF domain of the related protein, SH3YL1, binds phosphoinositides with high affinity, while the N-terminal SYLF domains of both Ysc84p and Lsb3p have been shown to bind and bundle actin filaments, as well as bind liposomes with high affinity
GEIRKAANTLQNFFKGGNLEPDQSIPHALLRGAKGLAFLTVAKAGFIVSGKVGTGLVVARLPDGSWSAPS
AIGTAGLGWGAQVGGELTDFVIVLRTRSAVKAFCGRGQVSLGAELSVAVGPLGRAAEADLRAGDGGVAAC
YSYSHSKGLFAGVSLEGSVVATRKDVNHKFYGRPVTPTEILLGSVPQPPAAEPLYDALDEL
>gnl|CDD|212134 cd11527, NTP-PPase_dUTPase, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in dimeric 2-Deoxyuridine 5'-triphosphate nucleotidohydrolase and similar proteins. dUTPase (dUTP pyrophosphatase; EC 3.6.1.23) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate. It acts to ensure chromosomal integrity by reducing the effective ratio of dUTP/dTTP. Members in this family are dimeric dUTPases, such as those from Leishmania major, Trypanosoma cruzi, and Campylobacter jejuni, which differ from the monomeric and trimeric forms and adopt an all-alpha topology. A central four-helix bundle, consisting of two alpha-helices from the rigid domain and two helices from the mobile domain and connecting loops, form the active site in dimeric dUTPase-like proteins, requiring the presence of metal ion cofactors to hydrolyze both dUTP and dUDP
LFELQKELDDKINKKWNLNNKKKLLKNKALALIVELAELANETESFKYWKKNKPNDKEKILEELVDILHF
LLSIALELYIEKNKLNHKRQDNGY
>gnl|CDD|212135 cd11528, NTP-PPase_MazG_Nterm, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs. MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the N-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer; each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active site and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity; however, this domain does not exhibit an NTPase activity despite containing structural features such as the EEXX(E/D) motif and key basic catalytic residues responsible for nucleotide pyrophosphohydrolysis activity. It is suggested that the N-terminal domain of EcMazG might have a house-cleaning function by hydrolyzing noncanonical NTPs whose incorporation into the nascent DNA leads to increased mutagenesis and DNA damage
ERLVEIVARLRGPGGCPWDREQTHESLRPYLLEEAYELVEAIEEGDPDNLREELGDVLLQVLFHAQIAEE
EGAFDLDDVIDGLTEKLIRRHPHVFGDEKAETAEEVLRNWEKIK
>gnl|CDD|212136 cd11529, NTP-PPase_MazG_Cterm, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs'. MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the C-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer. Each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active sites and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity, along with structural features such as EEXX(E/D) motifs and key basic catalytic residues. It has been shown that the C-terminus NTPase activity is responsible for regulation of bacterial cell survival under nutritional stress
PALMRAQKLQKRAAKVGFDWPDAEGVLDKVEEELAELKEALASGDKEEIEEELGDLLFSLVNLARFLGVD
PEEALRRANRKFERRFRYMEELAAEQGKDLEDLSLEELDALWEEAK
>gnl|CDD|212137 cd11530, NTP-PPase_DR2231_like, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Deinococcus radiodurans DR2231 protein and its bacterial homologs. This family includes a MazG-like NTP-PPase from Deinococcus radiodurans (DR2231), a putative NTP-PPase YP_001813558.1 from Exiguobacterium sibiricum and their bacterial homologs. DR2231 shows significant structural resemblance to MazG proteins, but is functionally related to the dimeric dUTPases. It can hydrolyze dUTP into dUMP. DR2231-like proteins contain a well conserved divalent ion binding motif, EXXEX(12-28)EXXD, which is the identity signature for the all-alpha-helical NTP-PPase superfamily. Unlike normal dimeric dUTPase-like proteins with a central four-helix bundle forming the active site, YP_001813558.1 displays a very unusual interlaced segment-swapped dimer. It potentially prefers to hydrolyze dCTPs or its derivatives. YP_001813558.1-like proteins contain a variant divalent ion binding motif, EXXEX(12-28)AXXD
LADVREFHRAFGLPVAEQPTLSDEDLALRQALLAEELAELAEALKKGDMVELADALADLLYVAYGTAVEH
GIDLDAAFAEVHRSNMSK
>gnl|CDD|212138 cd11531, NTP-PPase_BsYpjD, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative pyrophosphatase YpjD from Bacillus subtilis and its bacterial homologs. This family includes a putative pyrophosphatase Ypjd from Bacillus subtilis (BsYpjD) and its homologs. Although its biological role has not been described in detail, BsYpjD shows significant sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, BsYpjD contains a single MazG-like domain
KELQQEVDEWISQFEEGYFSPLSNLARLTEEVGELAREINHRYGEKPKPGEDEGELEEELADILFVLTCL
ANQLGIDLEEAFKRTMEKKETRD
>gnl|CDD|212139 cd11532, NTP-PPase_COG4997, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from archaea and bacteria. The family includes some uncharacterized hypothetical proteins from archaea and bacteria. Although their biological roles remain unclear, the family members show significant sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, the family contains a single MazG-like domain
YNKLVRDRIPEIIRASGKTCVTRILSDEEYLEALKKKLVEEAAEYAEAKTEDSLEELADLLEVIYAIAEA
HGISLEELEKVREKKREERGGFEKR
>gnl|CDD|212140 cd11533, NTP-PPase_Af0060_like, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in uncharacterized protein from Archaeoglobus fulgidus (Af0060) and its bacterial homologs. This family includes an uncharacterized protein from Archaeoglobus fulgidus (Af0060) and its homologs from bacteria. Although its biological role remains unclear, Af0060 shows high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D]
LLAKLKALLDLEGAKRPTETLELRVLKLGEEVGELAEAILGARGQNPRGKSHTWDDVREELLDVAQVALL
ALEKL
>gnl|CDD|212141 cd11534, NTP-PPase_HisIE_like, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Escherichia coli phosphoribosyl-ATP pyrophosphohydrolase (HisIE or PRATP-PH) and its homologs. This family includes Escherichia coli phosphoribosyl-ATP pyrophosphohydrolase, HisIE, and its homologs from all three kingdoms of life. E. coli HisIE is encoded by the hisIE gene, which is formed by hisE gene fused to hisl. HisIE is a bifunctional enzyme responsible for the second and third steps of the histidine-biosynthesis pathway. Its N-terminal and C-terminal domains have phosphoribosyl-AMP cyclohydrolase (HisI) and phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH) activity, respectively. This family corresponds to the C-terminal domain of HisIE and includes many hisE gene encoding proteins, all of which show significant sequence similarity to Mycobacterium tuberculosis phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH). These proteins may be responsible for only the second step in the histidine-biosynthetic pathway, irreversibly hydrolyzing phosphoribosyl-ATP (PRATP) to phosphoribosyl-AMP (PRAMP) and pyrophosphate
LEELEAVIEDRKEAPPEGSYTAKLLEKGLDKILKKVGEEAVEVIIAAKNGDKEELVYEAADLLYHLLVLL
AYRGISLEDVLEEL
>gnl|CDD|212142 cd11535, NTP-PPase_SsMazG, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Sulfolobus solfataricus (Ss) and its homologs from archaea and bacteria. This family includes a MazG-like protein from Sulfolobus solfataricus (SsMazG) and its homologs from archaea and bacteria. Although its biological roles remain still unclear, SsMazG shows significant sequence similarity to the NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, SsMazG contains a single MazG-like domain. It is predicted that SsMazG might participate in house-cleaning by preventing incorporation of the oxidation product 2-oxo-(d)ATP (iso-dGTP), a mutagenic derivative of ATP, into DNA
LQKLIRENYGERDFNKRGVEKTFLWLVEEVGELAKALRKNDGENIEEELADVFAWLLSLANLLGIDLEEA
FKKKYP
>gnl|CDD|212143 cd11536, NTP-PPase_iMazG, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in integron-associated MazG (iMazG) proteins. This family corresponds to the iMazG proteins representing a new subfamily of MazG NTP-PPases. iMazG is likely to act as a house-cleaning enzyme capable of removing aberrant dNTPs, preventing the incorporation of damaging non-canonical nucleotides into host-cell DNA. It can convert dNTP to dNMP and pyrophosphate by cleaving between the alpha- and beta-phosphates of its dNTP substrates, with a marked preference for dCTP and dATP. Unlike typical tandem-domain MazG proteins, iMazG contains a single MazG-like domain and functions as a tetramer (a dimer of dimers) with a typical four-helical bundle. The divalent ions, such as Mg2+, are required for its pyrophosphatase activity
LKELQYYIKQVDKGPEGDQGLFLKLIEEVGELAEVIRKGKSGQPTGDNLKGSLAEELADVFYYTIAIANI
NGIDLEKIIELKDELNSIKY
>gnl|CDD|212144 cd11537, NTP-PPase_RS21-C6_like, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse RS21-C6 protein and its homologs. RS21-C6 proteins, highly expressed in all vertebrate genomes and green plants, act as house-cleaning enzymes, removing 5-methyl dCTP (m5dCTP) in order to prevent gene silencing. They show significant sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, RS21-C6 contains a single MazG-like domain and functions as a tetramer (a dimer of dimers) with a typical four-helical bundle. Divalent ions, such as Mg2+, are required for its pyrophosphatase activity. This family also includes a pyrophosphatase from Archaeoglobus fulgidus (Af1178). Although its biological role remains unclear, Af1178 shows significant sequence similarity to the mouse RS21-C6 protein
RQALREFRDERDWDQFHTPKNLAMALSIEAGELLEIFQWKSEEESELVWDPEKREHVGEELADVLIYLLR
LADKLGIDLAEAVLEKLEKN
>gnl|CDD|212145 cd11538, NTP-PPase_u1, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria. This family corresponds to a group of uncharacterized hypothetical proteins from bacteria, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D]
LAELSERVEAVSDIYAARFGIDRDDDWYLLKLQEEVGELTQAYLRLTGRGRRKGRSEDELRQDLEDELAD
VLGMLLLFARRFGIDLEAAIERKWLRW
>gnl|CDD|212146 cd11539, NTP-PPase_u2, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea. The family corresponds to a group of uncharacterized hypothetical proteins from bacteria and archaea, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D]
RREIYRKAIETYGKDAQKDVAIEEMAELIQALSKYKRGKGNRENLIEEIADVEIMLEQLKIIFGIEDDEL
EKAKDKKLERLKERL
>gnl|CDD|212147 cd11540, NTP-PPase_u3, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea. This family corresponds to a group of uncharacterized hypothetical proteins from bacteria and archaea, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D]
ELIEKVKEWAEDRNLDEGADPRKQLLKLVEEVGELSEAIAKNKQEEIKDSIGDVLVVLIILCAQLGLSLE
ECLEIA
>gnl|CDD|212148 cd11541, NTP-PPase_u4, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea. This family corresponds to a group of uncharacterized hypothetical proteins from bacteria, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D]
EYQKAALRTDNDPLTEDERLLNALLGLFGEVGEVADAIKKHIRDGHAPLDKEALAEELGDVLWYLAALAN
VLGISLEEIAEANIAKLRSRY
>gnl|CDD|212149 cd11542, NTP-PPase_u5, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea. This family corresponds to a group of uncharacterized hypothetical proteins from bacteria, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D]
INELVDEAHENAVAHGWWDDPRTGNNNFGELLMLIHSEVSEALEGLRKGLMDDKLPHRPMIEVELADAVI
RIFDTAGGLGIDLEGAIAEKMAYNKNRPD
>gnl|CDD|212150 cd11543, NTP-PPase_u6, Nucleoside Triphosphate Pyrophosphohydrolase EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea. This family corresponds to a group of uncharacterized hypothetical proteins from bacteria, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain
ERALAIRALYHQLERKNHGREWTVEEDALGFLGDVGDVGRLVMAQQGRWPIDGVDAELEHKLAECLWWVL
VLADRLDVDILETFLTR
>gnl|CDD|212151 cd11544, NTP-PPase_DR2231, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Deinococcus radiodurans DR2231 protein and its bacterial homologs. This family corresponds to the DR2231 protein, a MazG-like NTP-PPase from Deinococcus radiodurans, and its bacterial homologs. All family members contain a well-conserved divalent ion binding motif, EXXEX(12-28)EXXD, which is the identity signature for all-alpha-helical NTP-PPase superfamily. DR2231 shows significant structural resemblance to MazG proteins, but is functionally related to the dimeric dUTPases. It might be an evolutionary precursor of dimeric dUTPases with very high specificity in hydrolyzing dUTP into dUMP, but an inability to hydrolyze dTTP, a typical feature of dUTPases. Moreover, unlike the dUPase monomer containing a single active site, the DR2231 protein dimer holds two putative active sites
NAARVREFHRAIGADLPETPTLPPPALLRLRQTLLAEEAAEVRAAIDHGDLVPLAHELADLLYVTYGTAL
QYGIDLDAVFAEVHRANLTKASGPRRADGKQLKPEGWRPADVAGVL
>gnl|CDD|212152 cd11545, NTP-PPase_YP_001813558, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Exiguobacterium sibiricum YP_001813558.1 protein and its bacterial homologs. This family contains a putative NTP_PPase (YP_001813558.1) from Exiguobacterium sibiricum and its bacterial homologs. Unlike normal dimeric dUTPase-like proteins with a central four-helix bundle forming the active site, YP_001813558.1 displays a very unusual interlaced segment-swapped dimer that might be important for it to adapt to an extremely cold environment. Moreover, structural analysis and comparisons indicate that YP_001813558.1 potentially prefers to hydrolyze dCTPs or its derivatives
PYEQVKEFHEKFGHPVSEQPTALPEERAVARAGWMLEELVEFLYASQADALIDLIYFAYGSFVEMGVEPD
PLFEIVHKANMGKLFPDGKPRYDPEDGKILKPEGWEAPEPPEPAE
>gnl|CDD|212153 cd11546, NTP-PPase_His4, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in His4-like fungal histidine biosynthesis trifunctional proteins and their homologs. This family includes fungal histidine biosynthesis trifunctional proteins and their homologs from eukaryotes and bacteria. Some family members contain three domains responsible for phosphoribosyl-AMP cyclohydrolase (PRAMP-CH), phosphoribosyl-ATP pyrophosphohydrolase (PRATP-PH), and histidinol dehydrogenase (Histidinol-DH) activity, respectively. Some others do not have Histidinol-DH domain, but have an additional N-terminal TIM phosphate binding domain. This family corresponds to the domain for PRATP-PH activity, which shows significant sequence similarity to Mycobacterium tuberculosis PRATP-PH that catalyzes the second step in the histidine-biosynthetic pathway, irreversibly hydrolyzing phosphoribosyl-ATP (PRATP) to phosphoribosyl-AMP (PRAMP) and pyrophosphate
GLDALEATLTQRKQNAPPGSYTARLFNDEKLLRAKIMEEAEELCEAKTKDEVAWEAADLLYFALVRCVAA
GVSLDDVERELDRR
>gnl|CDD|212154 cd11547, NTP-PPase_HisE, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Mycobacterium tuberculosis phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH) and its bacterial homologs. This family includes M. tuberculosis phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH) and its bacterial homologs. M. tuberculosis HisE is encoded by the hisE gene, which is a separate gene presenting in many bacteria and archaea but is fused to hisI in other bacteria, fungi and plants. HisE is responsible for the second step in the histidine-biosynthetic pathway. It can irreversibly hydrolyze phosphoribosyl-ATP (PRATP) to phosphoribosyl-AMP (PRAMP) and pyrophosphate. HisE dimerizes into a four alpha-helix bundle, forming two inferred PRATP active sites on the outer faces. M. tuberculosis HisE has been found to be essential for growth in vitro, thus making it a potential drug target for tuberculosis
KTFEELFAELCDRAADRPEGSGTVELLDKGVHAIGKKLVEEAAEVWMAAEFESDDAAAEEISQLLYHLQV
MMIAKGLTLEDVYAKL
>gnl|CDD|211389 cd11548, NodZ_like, Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ. Bradyrhizobium NodZ is an alpha 1,6-fucosyltransferase involved in the biosynthesis of the nodulation factor, a lipo-chitooligosaccharide formed by three-to-six beta-1,4-linked N-acetyl-d-glucosamine (GlcNAc) residues and a fatty acid acyl group attached to the nitrogen atom at the non-reducing end. NodZ transfers L-fucose from the GDP-beta-L-fucose donor to the reducing residue of the chitin oligosaccharide backbone, before the attachment of a fatty acid group. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes
FLIFKGRGGLGNRMLALASALELARLTGRTLVIDWRDYEYAPRDENAFPLLFDPIEDRSIDGLPDRDPRR
GTQNIKGYPQQWIRPTSDLSHRVPAQIFRECDELTVLDVKGRKAVQAGYLPKLPRDADKLGRDRGIIKCY
LYRLFTPKQEVRAAVRKLYAKLFGRPTIGVHIRTTDHKDSLFIKLSPLHRVVDALRKKVALHKDATIFLA
TDSAEVKDELKRLFPDVVVTPKEFPPHGERSASDGLEGAEDALIDMYLLARCDHLIGSRFSTFSRMASIL
GDFPKTF
>gnl|CDD|211403 cd11549, Serine_rich_CAS, Serine rich Four helix bundle domain of CAS (Crk-Associated Substrate) scaffolding proteins; a protein interaction module. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes including migration, chemotaxis, apoptosis, differentiation, and progenitor cell function. They mediate the signaling of integrins at focal adhesions where they localize, and thus, regulate cell invasion and survival. Over-expression of these proteins is implicated in poor prognosis, increased metastasis, and resistance to chemotherapeutics in many cancers such as breast, lung, melanoma, and glioblastoma. CAS proteins have also been linked to the pathogenesis of inflammatory disorders, Alzheimer's, Parkinson's, and developmental defects. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. Vertebrates contain four CAS proteins: BCAR1 (or p130Cas), NEDD9 (or HEF1), EFS (or SIN), and CASS4 (or HEPL). CAS proteins associate with the 14-3-3 family; this interaction is regulated by integrin-mediated cell adhesion. The serine rich four helix bundle domain of BCAR1 has been shown to bind 14-3-3 in a phosphorylation-dependent manner. This domain is structurally similar to other helical bundles found in cell adhesion components such as alpha-catenin, vinculin, and FAK, and may bind other proteins in addition to the 14-3-3 family
LDLDAAMEKLVRLQQEVSSSVSNLLSFVSSNWRSRENLEPNIDEIKTAVDRLRTSLHEFLEFARGALANA
ANASDKNLQLKLRRQLQPLEDSHQILSQTSQALDDCNWSLEALVDNSPSNKPDDLDRFVMCARTLPDDAK
QLASFIHGNASLLFKRAPT
>gnl|CDD|211404 cd11550, Serine_rich_NEDD9, Serine rich Four helix bundle domain of CAS (Crk-Associated Substrate) scaffolding protein, Neural precursor cell Expressed, Developmentally Down-regulated 9; a protein interaction module. NEDD9 is also called human enhancer of filamentation 1 (HEF1) or CAS-L (Crk-associated substrate in lymphocyte). It was first described as a gene predominantly expressed in early embryonic brain, and was also isolated from a screen of human proteins that regulate filamentous budding in yeast, and as a tyrosine phosphorylated protein in lymphocytes. It promotes metastasis in different solid tumors. NEDD9 localizes in focal adhesions and associates with FAK and Abl kinase. It also interacts with SMAD3 and the proteasomal machinery which allows its rapid turnover; these interactions are not shared by other CAS proteins. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. CAS proteins associate with the 14-3-3 family; this interaction is regulated by integrin-mediated cell adhesion. The serine rich four helix bundle domain of BCAR1, another CAS protein, has been shown to bind 14-3-3 in a phosphorylation-dependent manner. This domain is structurally similar to other helical bundles found in cell adhesion components such as alpha-catenin, vinculin, and FAK, and may bind other proteins in addition to the 14-3-3 family
RLALDPDTAIERLYRLQQAVESSVSNLMALVSPDWRTYSFMERHINEIRTAVDRVELSLGEYLQFGKGAA
ANATALSENGLHNKMRRELQRLEDSHQILLQTYQDLNSCNWSLNILAANGHHNKCDDLDRFVMVAKTVPD
DAKQLTTTIGSNAELLFRRAPG
>gnl|CDD|211405 cd11551, Serine_rich_CASS4, Serine rich Four helix bundle domain of CAS (Crk-Associated Substrate) scaffolding protein family member 4; a protein interaction module. CASS4, also called HEPL (HEF1-EFS-p130Cas-like), localizes to focal adhesions and plays a role in regulating FAK activity, focal adhesion integrity, and cell spreading. It is most abundant in blood cells and lung tissue, and is also found in high levels in leukemia and ovarian cell lines. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. CAS proteins associate with the 14-3-3 family; this interaction is regulated by integrin-mediated cell adhesion. The serine rich four helix bundle domain of BCAR1, another CAS protein, has been shown to bind 14-3-3 in a phosphorylation-dependent manner. This domain is structurally similar to other helical bundles found in cell adhesion components such as alpha-catenin, vinculin, and FAK, and may bind other proteins in addition to the 14-3-3 family
LDLEEAIETLTELQHAVSSSVASLMLFVSSKWRLREHLEANLDQIHRASDHITDSLDEFLDFARDVRGNA
SRLTDSNLQTRIKKQLQILEDSFQILQETAEALDNCNWSLEVLVDDKPSQMPDDLERFVMVARTIPEDIK
RFVSIIIANGKLLFRKNEK
>gnl|CDD|211406 cd11552, Serine_rich_BCAR1, Serine rich Four helix bundle domain of CAS (Crk-Associated Substrate) scaffolding protein, Breast Cancer Anti-estrogen Resistance 1; a protein interaction module. BCAR1, also called p130cas or CASS1, is the founding member of the CAS family of scaffolding proteins and was originally identified through its ability to associate with Crk. The name BCAR1 was designated because the human gene was identified in a screen for genes that promote resistance to tamoxifen. It is widely expressed and its deletion is lethal in mice. It plays a role in regulating cell motility, survival, proliferation, transformation, cancer progression, and bacterial pathogenesis. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. CAS proteins associate with the 14-3-3 family; this interaction is regulated by integrin-mediated cell adhesion. The serine rich four helix bundle domain of BCAR1 has been shown to bind 14-3-3 in a phosphorylation-dependent manner. This domain is structurally similar to other helical bundles found in cell adhesion components such as alpha-catenin, vinculin, and FAK, and may bind other proteins in addition to the 14-3-3 family
LDLEAAMETLARLQQGVSSSVSHLMSFIGGNWRSPEHMEANVQDIHAAVEGVHGAVRELLEFARGAVSNA
AQASDRTLHAKLSRQLQKMEEVYQTLVRHSQALDACRWSPAALAAPGPTLDDLDRLVMYSRGVPDDAKQL
ASFLHGNASLLFRRTKA
>gnl|CDD|212092 cd11554, SLC6sbd_u2, uncharacterized eukaryotic solute carrier 6 subfamily; solute-binding domain. SLC6 proteins (also called the sodium- and chloride-dependent neurotransmitter transporter family or Na+/Cl--dependent transporter family) include neurotransmitter transporters (NTTs): these are sodium- and chloride-dependent plasma membrane transporters for the monoamine neurotransmitters serotonin (5-hydroxytryptamine), dopamine, and norepinephrine, and the amino acid neurotransmitters GABA and glycine. These NTTs are widely expressed in the mammalian brain, and are involved in regulating neurotransmitter signaling and homeostasis, and are the target of a range of therapeutic drugs for the treatment of psychiatric diseases. Bacterial members of the SLC6 family include the LeuT amino acid transporter
DQWGSRTAFVLAAMGGAVGLGNLLRFPSVVYNNGGLQFFIPYLLALVLLAIPILILELALGQAYRGGCVK
AFNLINRRAKGVGAAVVFGGFVVCTYYVPILAWIMVYFRHSFTVGWLAFTWFVVWLCVFRGVGSTGRVVY
ITMGLPIVLIIILLGRGASLPNAGDGIRLYFATWRGDKLASGEIWQAAAGQVFFSTGVGFGYMTAYASYN
SKFSNAVQDALIIAGSNSLFEIIAGFAVFGIVGYLGMTPGVEGEALGGFVLGFVTYPEAIAQMPGSNFFA
VLFFLTLFLLGISSAFALLEAVVTLICDSGWGRKVKRWWIATVVCFVSFLLSLPYCTRFGYYLLDAVDAW
ISNVALVFVVWAECVAATTVYRFEDVVDQVGLPAFAYYNVGYAGGQTLGAVVAHSV
>gnl|CDD|271404 cd11555, SLC-NCS1sbd_u1, uncharacterized nucleobase-cation-symport-1 (NCS1) transporter subfamily; solute-binding domain. NCS1s are essential components of salvage pathways for nucleobases and related metabolites; their known substrates include allantoin, uracil, thiamine, and nicotinamide riboside. NCS1s belong to a superfamily which also contains the solute carrier 5 family sodium/glucose transporters (SLC5s), and solute carrier 6 family neurotransmitter transporters (SLC6s)
DPRLYNEDLAPTKARGRTWGWYSIFAFWMSDVHSLGGYTFAASLFALGLNGWQVFLALILGILIVYLLCN
LVGKPSQKTGVPFPVMARASFGVFGANIPALIRGVIAIFWYGIQTYLASTAVALLLLKLFPGLASLTQHS
FLGLSTLGWISFLILWALQLLVFWRGMEAIRKFIDWAGPAVYVVMIALAIWILSRAGGNISFTLGTVFLT
GGEMVAAFLAAVALVVAYFSGPMLNFGDFSRYAKSEKAVRRGNFWGLPVNFLLFSLITVVTTAGTLPVFG
EAITDPVEIVARIDNLLATVLAALTFLIATVGINIVANFVSPAYDLSNLAPKKISFRRGGLIAAVLAVVI
TPWNLYNSPVVIHYFLDGLGAFLGPLFGILIVDYYLVRKGRVDVPDLYSDSPKGAYWYRNGWNPKAVAAL
VPAAAISVLTVLVPALAALAGFSWFIGAALGGVLYYLLARR
>gnl|CDD|271405 cd11556, SLC6sbd_SERT-like_u1, uncharacterized subgroup of the SERT-like Na(+)- and Cl(-)-dependent monoamine transporter subfamily; solute binding domain. SERT-like Na(+)- and Cl(-)-dependent monoamine transporters, transport monoamine neurotransmitters from synaptic spaces into presynaptic neurons. Members include: the norepinephrine transporter NET, the serotonin transporter SERT, and the dopamine transporter DAT1. These latter may play a role in diseases or disorders including depression, anxiety disorders, and attention-deficit hyperactivity disorder, and in the control of human behavior and emotional states. They belongs to the solute carrier 6 (SLC6) transporter family. Members of this subgroup are uncharacterized
RETWSKKVDFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLIPYGIMLVVGGIPLFYMELALGQYNRKGAI
TSWGRLCPLFKGIGYAVVLIAFYVDFFYNVIIAWSLYYFFASFTFNLPWTSCNNSWNTPNCREFHWSEDG
TVPCRSANQSFSAENQSAQSENFTSAASEYFERGVLELNRSEGVHDLGNIRWDIALCLFAVYLICYFSLW
KGIHTSGKVVWFTALFPYVVLFILLIRGVTLPGSFNGIQYYLTPNFEALKKAEVWVDAATQVFFSLGPGF
GVLLAYASYNKFHNNVYKDALLTSFINCATSFLSGFVIFSVLGYMAHRSGVPIEDVATEGPGLVFVVYPE
ALSTMPGSTFWSLIFFMMLMTLGLDSSFGGSEAIITALSDEFPIIKRHRELFVGCLFSFYFVIGLASCTQ
GGFYFFHLLDRYAAGYSILIAVLFEAIAVSWIYGTDRFCQDIKEMLGFPPGIYWKVCWKFIAPIFLLFII
TYGLIGYQPLTYDDYVYPTWANALGWCIAGSSISMIPIVAIYKLLSTPGTLRQRFKILTTPP
>gnl|CDD|211407 cd11557, ST7, Suppression of tumorigenicity 7. ST7 is a metazoan protein that behaves as a tumor suppressor in human cancer cells. It appears to localize to the cytoplasm and plasma membrane, and may mediate tumor suppression by regulating genes that are involved in oncogenic pathways and/or maintain cellular structure. It has been suggested that the suppression of tumorigenicity is associated with a function in mediating the remodeling of the extracellular matrix. However, somatic mutations of ST7 have not been observed as being commonly associated with molecular pathogenesis in various human neoplasias
FLNTLTPKFYVALTGTSSLISGLILIFEWWYFRKYGTSFIEQVSLSHLSPLLGGVDLSNGGSNSSDQSVP
ECKVWRNPLNLFRGAEYNRYTWVTGREPLTYYDMNLSAQDHQTFFTCDADAGRPADEIMQKAWRERNPQA
RIKAAHEALELNPECATALILLAEEEAQTILEAEKLLKQALKAAEANYRKSQQLQHQDPQHEAVHRRDTN
VLVYIKRRLAMCARKLGRLKEAVKMMRDLMKEFPLLSVLNIHENLIEALLELQAYADVQAVLAKYDDISL
PKSATICYTAALLKARAVADKFSPEVASRRGLSTAEMNAVEAIHRAVEFNPHVPKYLLEMKSLILPPEHI
LKRGDSEAIAYAFFHLQHWKRVEGALNLLHCTWEGTFRMIPYPLEKGHLFYPYPSCTESADRELLPSFHE
VSVYPKKELPFFILFTAGLCSFTALLALLTHQFPEPMG
>gnl|CDD|211396 cd11558, W2_eIF2B_epsilon, C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon. eIF2B is a heteropentameric complex which functions as a guanine nucleotide exchange factor in the recycling of eIF-2 during the initiation of translation in eukaryotes. The epsilon and gamma subunits are sequence similar and both are essential in yeast. Epsilon appears to be the catalytically active subunit, with gamma enhancing its activity. The C-terminal domain of the eIF2B epsilon subunit contains bipartite motifs rich in acidic and aromatic residues, which are responsible for the interaction with eIF2. The structure of the domain resembles that of a set of concatenated HEAT repeats
DDESDFHSEVVESLERALEENHSVDNAILEINSLRMAYNVTDHDVRRAVVKALLELILEVSSTSTAELLE
ALKKLLSKWGPLLENYVKSQDDQVELLLALEEFCLESEEGGPLFAKLLHALYDLDILEEEAILEWWEEPD
AGADEEMKKVRELVKKFIEWLEEAEEESD
>gnl|CDD|211397 cd11559, W2_eIF4G1_like, C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar proteins. eIF4G1 is a component of the multi-subunit eukaryotic translation initiation factor 4F, which facilitates recruitment of the mRNA to the ribosome, a rate-limiting step during translation initiation. This C-terminal domain, whose structure resembles that of a set of concatenated HEAT repeats, has been associated with binding to/recruiting the kinase Mnk1, which phosphorylates eIF4E
LPLLRVQAELLKLLQEDPNPDELYKWIKENVSPELYASPGFVRALMTAVLKYAIEEKSLPEKEKALLEKY
APLLQKYLDDDEQLQLQALYALQALVHTLEFPKGLLLRFFDALYDEDVIEEEAFLKWKEDVDPA
>gnl|CDD|211398 cd11560, W2_eIF5C_like, C-terminal W2 domain of the eukaryotic translation initiation factor 5C and similar proteins. eIF5C appears to be essential for the initiation of protein translation; its actual function, and specifically that of the C-terminal W2 domain, are not well understood. The Drosophila ortholog, kra (krasavietz) or exba (extra bases), may be involved in translational inhibition in neural development. The structure of this C-terminal domain resembles that of a set of concatenated HEAT repeats
EFFPPNKRTEEHFAEHFKEEGLDELVEFYRKQASQEIKKELQQELKEMIAEEEPVKEIIAAVKEQMKKSS
LPEHEVVGLLWTALMDAVEWSKKEDQIAEQALRHLKKYAPLLAAFCTTARAELALLNKIQEYCYENMKFM
KVFQKIVKLLYKADVLSEDAILKWYKKGHSPKGKQVFLKQMEPFVEWLQEAEEE
>gnl|CDD|211399 cd11561, W2_eIF5, C-terminal W2 domain of eukaryotic translation initiation factor 5. eIF5 functions as a GTPase acceleration protein (GAP), as well as a GDP dissociation inhibitor (GDI) during translational initiation in eukaryotes. The structure of this C-terminal domain resembles that of a set of concatenated HEAT repeats
EEEEDERVDELGEFLKKNKDESGLSELKEILKEAERLDVVKDKAVLVLAEVLFDENIVKEIKKRKALLLK
LVTDEKAQKALLGGIERFCGKHSPELLKKVPLILKALYDNDILEEEVILKWYEKVSKKYVSKEKSKKVRK
AAEPFVEWLEEAEEEEE
>gnl|CDD|211408 cd11564, FAT-like_CAS_C, C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated Substrate) scaffolding proteins; a protein interaction module. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes including migration, chemotaxis, apoptosis, differentiation, and progenitor cell function. They mediate the signaling of integrins at focal adhesions where they localize, and thus, regulate cell invasion and survival. Over-expression of these proteins is implicated in poor prognosis, increased metastasis, and resistance to chemotherapeutics in many cancers such as breast, lung, melanoma, and glioblastoma. CAS proteins have also been linked to the pathogenesis of inflammatory disorders, Alzheimer's, Parkinson's, and developmental defects. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. Vertebrates contain four CAS proteins: BCAR1 (or p130Cas), NEDD9 (or HEF1), EFS (or SIN), and CASS4 (or HEPL). The FAT-like C-terminal domain of CAS proteins binds to the C-terminal domain of NSPs (novel SH2-containing proteins) to form multidomain signaling modules that mediate cell migration and invasion
DRQLLLFYSEQCESHFGALQKAIDAFLSSVESNQPPKVFVAHSKFVILSAHKLVFIGDTLCRNVQSADVR
NKVLRCSNQLCEALKTVVLATKKAALQYPSVAAVQEMVDRVVELSHHAQQFKTSLG
>gnl|CDD|467842 cd11565, RWD_Spc24, RWD domain of the Spc24 component of the nuclear division cycle 80 (NDC80) kinetochore complex. The kinetochore protein Spc24 acts as a component of the essential kinetochore-associated NDC80 complex, which is involved in chromosome segregation and spindle checkpoint activity. Spc24 is required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules. The model corresponds to the Spc24 RWD domain, which provides an interaction platform to mediate kinetochore assembly
TVLKLKLYRSLGIELEEDEDGEYDKALIRNKNKGDVHVVNLDDKYSDYFYSNYLWDLL
>gnl|CDD|211318 cd11566, eIF1_SUI1, Eukaryotic initiation factor 1. eIF1/SUI1 (eukaryotic initiation factor 1) plays an important role in accurate initiator codon recognition during translation initiation. eIF1 interacts with 18S rRNA in the 40S ribosomal subunit during eukaryotic translation initiation. Point mutations in the yeast eIF1 implicate the protein in maintaining accurate start-site selection but its mechanism of action is unknown
GYIHIRIQQRNGRKTLTTVQGLPEEFDLKKILKAFKKEFACNGTVVEDPEYGEVIQLQGDQRKNIKEFLL
EEGIAKKDNIKVHG
>gnl|CDD|211319 cd11567, YciH_like, Homologs of eIF1/SUI1 including Escherichia coli YciH. Members of the eIF1/SUI1 (eukaryotic initiation factor 1) family are found in eukaryotes, archaea, and some bacteria; eukaryotic members are understood to play an important role in accurate initiator codon recognition during translation initiation. The function of non-eukaryotic family members is unclear. Escherichia coli YciH is a non-essential protein and was reported to be able to perform some of the functions of IF3 in prokaryotic initiation
QKVRVRLEKRGRGGKTVTVIEGLPLSEEDLKELAKELKKKCGCGGTVKDGEIELQGDHREKIKELLEKKG
FKVKKI
>gnl|CDD|211409 cd11568, FAT-like_CASS4_C, C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated Substrate) scaffolding protein family member 4; a protein interaction module. CASS4, also called HEPL (HEF1-EFS-p130Cas-like), localizes to focal adhesions and plays a role in regulating FAK activity, focal adhesion integrity, and cell spreading. It is most abundant in blood cells and lung tissue, and is also found in high levels in leukemia and ovarian cell lines. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain, which binds to the C-terminal domain of NSPs (novel SH2-containing proteins) to form multidomain signaling modules that mediate cell migration and invasion
QPARKCPLSEHCRLYFGALQKAISVFHSSLSSNQPPEVFISHSKLIIMVGQKLVDTLCQEAKEREARNEI
LAGSSQLCALLKNLALATKNAALQYPSPAALRELQDIADELAKHTQQFRAMLE
>gnl|CDD|211410 cd11569, FAT-like_BCAR1_C, C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated Substrate) scaffolding protein, Breast Cancer Anti-estrogen Resistance 1; a protein interaction module. BCAR1, also called p130cas or CASS1, is the founding member of the CAS family of scaffolding proteins and was originally identified through its ability to associate with Crk. The name BCAR1 was designated because the human gene was identified in a screen for genes that promote resistance to tamoxifen. It is widely expressed and its deletion is lethal in mice. It plays a role in regulating cell motility, survival, proliferation, transformation, cancer progression, and bacterial pathogenesis. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain, which binds to the C-terminal domain of NSPs (novel SH2-containing proteins) to form multidomain signaling modules that mediate cell migration and invasion
ALGPSDRQLLLFYQEQCEANVTTLTNAIDAFFTSISSNQPPKIFVAHSKFVILSAHKLVFIGDTLSRQAK
AADVRSKVTHYSNLLCEKLKEIVLSTKTAALQYPSPAAAKDMVERVKELGGSTQQFRMVLGQL
>gnl|CDD|211411 cd11570, FAT-like_NEDD9_C, C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated Substrate) scaffolding protein, Neural precursor cell Expressed, Developmentally Down-regulated 9; a protein interaction module. NEDD9 is also called human enhancer of filamentation 1 (HEF1) or CAS-L (Crk-associated substrate in lymphocyte). It was first described as a gene predominantly expressed in early embryonic brain, and was also isolated from a screen of human proteins that regulate filamentous budding in yeast, and as a tyrosine phosphorylated protein in lymphocytes. It promotes metastasis in different solid tumors. NEDD9 localizes in focal adhesions and associates with FAK and Abl kinase. It also interacts with SMAD3 and the proteasomal machinery which allows its rapid turnover; these interactions are not shared by other CAS proteins. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain, which binds to the C-terminal domain of NSPs (novel SH2-containing proteins) to form multidomain signaling modules that mediate cell migration and invasion
DRQLLGFYADQCETHFISLLNAIDAFFSCVSSGQPPRIFVAHSKFVILSAHKLVFIGDTLTRQVTVQDIR
NRVMNSSNQLCELLKTIVMATKMAALHYPSTAALQEMVDRVTDLSHLAQLFKLSLSQM
>gnl|CDD|211412 cd11571, FAT-like_EFS_C, C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated Substrate) scaffolding protein, Embryonal Fyn-associated Substrate; a protein interaction module. EFS is also called HEFS, CASS3 (CAS scaffolding protein family member 3) or SIN (Src-interacting protein). It was identified based on interactions with the Src kinases, Fyn and Yes. It plays a role in thymocyte development and acts as a negative regulator of T cell proliferation. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain, which binds to the C-terminal domain of NSPs (novel SH2-containing proteins) to form multidomain signaling modules that mediate cell migration and invasion
EDSQLLHFYAGQCQSHYSTLLAAVAALLSSTQANQPPRVFVPHGKRLIVAAHKLVFVGDTLGRLASSAPL
RARVATAGGALCQALKAVVLATKGAALGYPSPPAAQEMAQCVADLSGQALQFTTLLQSLA
>gnl|CDD|211413 cd11572, RlmI_M_like, Middle domain of the SAM-dependent methyltransferase RlmI and related proteins. This middle or central domain is typically found between an N-terminal PUA domain and a C-terminal SAM-dependent methyltransferase domain, such as in the Escherichia coli ribosomal RNA large subunit methyltransferase RlmI (YccW). It may be involved in binding to the RNA substrate
AFFKRRIEKALALRKRLLLDDTNAYRLVHGEGDGLPGLIVDRYGDVLVVQILSAGMERLKELIVEALKEL
LGPKGIYERSDAAVRELEGLPEEVGVLYG
>gnl|CDD|211414 cd11573, GH99_GH71_like, Glycoside hydrolase families 71, 99, and related domains. This superfamily of glycoside hydrolases contains families GH71 and GH99 (following the CAZY nomenclature), as well as other members with undefined function and specificity
VFAGYQPWTPEVMRKHIRWAQEAGIDGFAVDWYPEADTSPLAETTAILNKALDAAEEENFTIFFMLDPAS
LREAGELDVVLERITRLINEYRNPSSYYKVGGKPLVFIWGPGLAYTASEWEALKAQLRAGCPYMIGLWTP
WRVPNRDMITDMFDGASPWTPWRGTNPEEAYGHGVKNWRPDQEWMGANGKGYIPTVSPGFSDINRRPGDP
GDIILRRDGQRLHSMLEAALKAGPAMIQIASWNDWGEGTYIEPCEEYGPRDRKFVTYEGRPPDAYLKRTP
RALG
>gnl|CDD|211415 cd11574, GH99, Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase. This family of glycoside hydrolases 99 (following the CAZY nomenclature) includes endo-alpha-1,2-mannosidase (EC 3.2.1.130), which is an important membrane-associated eukaryotic enzyme involved in the maturation of N-linked glycans. Specifically, it cleaves mannoside linkages internal to N-linked glycan chains by hydrolyzing an alpha-1,2-mannosidic bond between a glucose-substituted mannose and the remainder of the chain. The biological function and significance of the soluble bacterial orthologs, which may have obtained the genes via horizontal transfer, is not clear
VHIFYYAWYGNPEFDGKYGHWNHKILPHWDIAKKYPQGRHDPPDDIGSNFYPKLGPYSSSDPSVIDDHMK
QIREAGIGVVVVSWYGPGSSDDNGKPSDDTIPLLLDIAHEYGLKVAFHIEPYEGRTAASLREDIKYILDK
YGSHPAFYKYKKGRGLPVFYIYDSYLTPPSDWAKLLSPNGKLTIRNTAYDAIFIGLLVESDHKSDILEAG
FDGFYTYFAANGFTYGSTPKNWKQLSKFARERGLLFIPSVGPGYDDTRVRPWNASNTRSRENGKYYEKMW
KAALKVDPDIISITSFNEWHEGTQIEPAVPKKGGEFTYLDYSPNDPDFYLELTRKWVE
>gnl|CDD|211416 cd11575, GH99_GH71_like_3, Uncharacterized glycoside hydrolase family 99-like domain. This family of putative glycoside hydrolases resembles glycosyl hydrolase families 71 and 99 (following the CAZY nomenclature) and may share a similar catalytic site and mechanism
VRKTNSKKVYAHYMPWFETRPDDGKWGWHWTMANFDPDHIDASGKRQIASHYYPLIGPYSSGDPDVIEYQ
LLLMKLAGIDGVIVDWYGTGHFSDYALLKENTEALIKKLFEVGLNFADCYEDQTIEQKVNAGKLSDKVAA
AKQDLQYLADNYFTSPSYLKVDGRPLLLLFGPQFLKSEEEWTVIFSALKPKPVFLTLWGETNEVGANLAD
GEFAWVPARLRVSTARLEGLDYLDNFYTNFADWPIAIGSAYPGFDDFYCEGGGGGSYWYIPRNNGETFLR
TLDLALASGLDIIQIATWNDYGEGTMIEPTVEFGYRDLETTQQFARQKKGVSYSEADLTLPLELYQLRKE
AAFLEAIQRQLDQAALAIVSGQVAKA
>gnl|CDD|211417 cd11576, GH99_GH71_like_2, Uncharacterized glycoside hydrolase family 99-like domain. This family of putative glycoside hydrolases resembles glycosyl hydrolase families 71 and 99 (following the CAZY nomenclature) and may share a similar catalytic site and mechanism. The domain may co-occur with other domains involved in the binding/processing of glycans
STLKGKVMVGYQGWFRAPGDGSPNNGWSHWGGGGSFPPGNCTIDLWPDVSEYPKDELFTTGFKLPDGSPA
KLFSSYDPSTVDLHFKWMQEYGIDGVFLQRFVGSLRDPAFKAHRDKVLANVRAAAEKYGRVFAIMYDLSG
LNAGTVLSVIKNDWTNLVDKYKILDSPAYLHHNGKPVVAIWGFGFNDRPGTPADALDLINWFKNDGCYVI
GGVPTGWRTLNGDSRPDPELVYKSADMISPWTVGRYNDISGADNFYTNVIKPDKAWCNANGIDYQPVVFP
GFSWHNLKGGSPLNQIPRLGGDFLWRQAYNAKKAGAKMIYVAMFDEYDEGTAIFKVAEDPPVPPNGQYFL
TLDADGDGLPSDFYLRLTGQAAKMLRGE
>gnl|CDD|211418 cd11577, GH71, Glycoside hydrolase family 71. This family of glycoside hydrolases 71 (following the CAZY nomenclature) function as alpha-1,3-glucanases (mutanases, EC 3.2.1.59). They appear to have an endo-hydrolytic mode of enzymatic activity and bacterial members are investigated as candidates for the development of dental caries treatments.The member from fission yeast, endo-alpha-1,3-glucanase Agn1p, plays a vital role in daughter cell separation, while Agn2p has been associated with endolysis of the ascus wall
AASAKAVFAHFMVGNTPNYTQDDWEKDIRLAQAAGIDGFALNIGSDDSQTPTQLALAYQAAEATGFKLFL
SFDMSGGWSASDVAEVIALIATYAAHPAYYNGKPFVSTFEGEGDNAADWADIKAQLLGTNIFFVPDWSSL
GGPSALNSGLDVADGLFSWDAWPPGGNNDMSTDTDAAYLAALGGKPYMAPVSPWFYTHLPGYGKNWYWRG
DDLWRDRWEQIIALQPDFVEIITWNDYGESHYIGPLRGKANSVGDASANYVDGFPHDGWRDLLPYYIAAY
KTG
>gnl|CDD|211419 cd11578, GH99_GH71_like_1, Uncharacterized glycoside hydrolase family 99-like domain. This family of putative glycoside hydrolases resembles glycosyl hydrolase families 71 and 99 (following the CAZY nomenclature) and may share a similar catalytic site and mechanism
VGAYYYNWTSSGLDWNKKYPEEPLLGEYDALDPAVIEQHIDWADQAGIDFFIVSWWGPDNDNVVLVAFYF
LRKAGDVKMVINYNTAHLLETNEATLLDGAKLQTFINDFKYLADLYFDPDNYYKIDGRPVVFIYPANLSS
NFSIDYKTVFAALRQAVLERGVELYLIGDIPTGWTPPVRYKKAIGAMDAVTAYTWYTNVYDRSKEFLAFY
SFVDLNWRNWTESLGKWNVDFIPCISPGFNDTVDNLFQSYKLERNPSSFKKMCNVALRNDGACNIVLITS
FNEWNEGTNIEPSEEAYGFGYLETLLDELRKQF
>gnl|CDD|211420 cd11579, Glyco_tran_WbsX, Glycosyl hydrolase family 99-like domain of WbsX-like glycosyltransferases. Members of this domain family are found in proteins within O-antigen biosynthesis clusters in Gram negative bacteria, where they may function as glycosyl hydrolases and typically co-occur with glycosyltransferase domains. They bear resemblance to GH71 and the GH99 family of alpha-1,2-mannosidases and may share a similar cataltyic site and mechanism. The O-antigens are essential lipopolysaccharides in gram-negative bacteria's outer membrane and have been linked to pathogenicity
MKVIAFYLPQFHPIPENDEWWGKGFTEWTNVKKAKPLFEGHYQPRVPLDLGYYDLRDPEVREKQAELAKE
YGIDGFCYYHYWFGGKRLLEKPLEELLLSGEPDFPFCLCWANENWTRRWDGRDKEELLEQQYYGEEDWKE
HFRYLLPYFKDPRYIKIDGKPVFLIYRPELIPDPKETLELWRELAREAGLPGLYLVAVASFGIEDPRDLG
FDAAVEFPPHYVVASELSKSRKLLKLKKGFGGNVYDYDDLVKYILNRPDPDYPYYPGVFPGWDNTPRRGK
RGTIFVNSTPELFKKWLRKAIERAKARPEDERLVFINAWNEWAEGAYLEPDLKYGYGYLEALKEALE
>gnl|CDD|211421 cd11580, eIF2D_N_like, N-terminal domain of eIF2D, malignant T cell-amplified sequence 1 and related proteins. This N-terminal domain of various proteins co-occurs with a PUA domain. Members of this family are: (1) MCTS-1 (malignant T cell-amplified sequence 1) or MCT-1 (multiple copies T cell malignancies), which may play roles in the regulation of the cell cycle, (2) the eukayotic translation initiation factor 2D, and (3) an uncharacterized archaeal family
EKLKNKTQLSKKDVKKLREQLIEQFPLLEEILDEIFPKKAPVKVQKFDTHYEIYTVDGEPVFFELDEGEV
FP
>gnl|CDD|212547 cd11581, GINS_A, Alpha-helical domain of GINS complex proteins; Sld5, Psf1, Psf2 and Psf3. The GINS complex is involved in both initiation and elongation stages of eukaryotic chromosome replication, with GINS being the component that most likely serves as the replicative helicase that unwinds duplex DNA ahead of the moving replication fork. In eukaryotes, GINS is a tetrameric arrangement of four subunits Sld5, Psf1, Psf2 and Psf3. The GINS complex has been found in eukaryotes and archaea, but not in bacteria. The four subunits of the complex are homologous and consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3
VEKLAEAIHNERKSENLLPPPPDFMEEVKELLHRLSKRQRSETQEILEHRLKILELSYIRDLLKTYLNSR
LDKIRDLSPEFLPSNLTEEEIGYFQTYWKEVAE
>gnl|CDD|211424 cd11582, Axin_TNKS_binding, Tankyrase binding N-terminal segment of axin. This N-terminal region of axin mediates interactions with the ankyrin-repeat clusters 2 and 3 of tankyrase, which controls the turnover of axin via poly-ADP-ribosylation. Axin functions as a negative regulator of the WNT signaling pathway
DPGSSFREDAPRPPVPGEEGELTPSDPRSSSHSYSNKSDSLKPEPSAATPRRIEAPLGFEPEGSASPTP
>gnl|CDD|211425 cd11583, Orc6_mid, Middle domain of the origin recognition complex subunit 6. Orc6 is a subunit of the origin recognition complex in eukaryotes, and it may be involved in binding to DNA. This model describes the central or middle domain of Orc6, whose structure resembles that of TFIIB, a DNA-binding transcription factor. Orc6 appears to form distinct complexes with DNA, and a putative DNA-binding site has been identified
SRLSVRDLAVQFGCKEAIEEAEKLLNRYKLPFLASEQRRVADFSLPQFTAAAFYLACKKLKVKVDKSKLL
EVSGVDPSIFDRLCASMEKLCKDI
>gnl|CDD|211426 cd11585, SATB1_N, N-terminal domain of SATB1 and similar proteins. SATB1, the special AT-rich sequence-binding protein 1, is involved in organizing chromosomal loci into distinct loops, creating a "loopscape" that has a direct bearing on gene expression. This N-terminal domain, which may be involved in various interactions with chromatin proteins, resembles a ubiquitin domain and has been shown to form tetramers, a function critical to SATB1-DNA interactions. The related Drosophila homeobox gene defective proventriculus (dve) plays a key role in the functional specification during endoderm development
LPVHCVVETVDSLHESVWRRRPRVETDSYVIIPKDTLFNQLVETALLRLGYSHSSAASAKGLIQIKNWKP
LPFDQITDNPDATVGDMLGELTHVATLRIQ
>gnl|CDD|212155 cd11586, VbhA_like, VbhA antitoxin and related proteins. VbhA is the antitoxin to VbhT. The VbhT toxin of the mammalian pathogen Bartonella schoenbuchensis is responsible for the disruptive adenylation of host proteins. VbhT also induces FIC-domain-mediated growth arrest in bacteria; it is inhibited by this antitoxin which binds to block the ATP binding site of the VbhT FIC domain
EEEQAERREAVASAIASNRLEGLEPSPEALAIAERYIRGEITLEEAVAEIRARY
>gnl|CDD|212536 cd11587, Arginase-like, Arginase types I and II and arginase-like family. This family includes arginase, also known as arginase-like amidino hydrolase family, and related proteins, found in bacteria, archaea and eykaryotes. Arginase is a binuclear Mn-dependent metalloenzyme and catalyzes hydrolysis of L-arginine to L-ornithine and urea (Arg, EC 3.5.3.1), the reaction being the fifth and final step in the urea cycle, providing the path for the disposal of nitrogenous compounds. Arginase controls cellular levels of arginine and ornithine which are involved in protein biosynthesis, and in production of creatine, polyamines, proline and nitric acid. In vertebrates, at least two isozymes have been identified: type I cytoplasmic or hepatic liver-type arginase and type II mitochondrial or non-hepatic arginase. Point mutations in human arginase gene lead to hyperargininemia with consequent mental disorders, retarded development and early death. Arginase is a therapeutic target to treat asthma, erectile dysfunction, atherosclerosis and cancer
SIIGAPFSLGQPRGGVEHGPGALRKAGLLEKLKELEYNYEDLGDLPFGDYENDSEFQIVRNPKSVGKASE
QLAGEVAEVVKNGRFSLVLGGDHSLAIGSISGHAQVYPDLGVIWIDAHGDINTPETSPSGNLHGMPLAFL
LGEGKGKLPDVGFSWVTPLISPENVVYIGLRDVDPGEKYIIKTLGIKYYTMFEVDKLGIGKVMEETLSYL
LGRKKRPIHLSFDVDGLDPVFAPATGTPVVGGLSYREGLLIMEELAETGLLSGMDLVEVNPSLDKTPEEV
TKTANTAVALTLAL
>gnl|CDD|212537 cd11589, Agmatinase_like_1, Agmatinase and related proteins. This family includes known and predicted bacterial agmatinase (agmatine ureohydrolase; AUH; SpeB; EC=3.5.3.11), a binuclear manganese metalloenzyme, belonging to the ureohydrolase superfamily. It is a key enzyme in the synthesis of polyamine putrescine; it catalyzes hydrolysis of agmatine to yield urea and putrescine, the precursor for biosynthesis of higher polyamines, spermidine, and spermine. Agmatinase from Deinococcus radiodurans shows approximately 33% of sequence identity to human mitochondrial agmatinase. An analysis of the evolutionary relationship among ureohydrolase superfamily enzymes indicates the pathway involving arginine decarboxylase and agmatinase evolved earlier than the arginase pathway of polyamine
VAVLGVPYDMGYPFRSGARFAPRAIREASTRFARGIGGYDDDDGGLLFLGDGVRIVDCGDVDIDPTDPAG
NFANIEEAVRKILARGAVPVVLGGDHSVTIPVLRALDEHGPIHVVQIDAHLDWRDEVNGVRYGNSSPMRR
ASEMPHVGRITQIGIRGLGSARPEDFDDARAYGSVIITAREVHRIGIEAVLDQIPDGENYYITIDIDGLD
PSIAPGVGSPSPGGLTYDQVRDLLHGLAKKGRVVGFDLVEVAPAYDPSGITSILAARLLLNFIG
>gnl|CDD|212538 cd11592, Agmatinase_PAH, Agmatinase-like family includes proclavaminic acid amidinohydrolase. This agmatinase subfamily contains bacterial and fungal/metazoan enzymes, including proclavaminic acid amidinohydrolase (PAH, EC 3.5.3.22) and Pseudomonas aeruginosa guanidinobutyrase (GbuA) and guanidinopropionase (GpuA). PAH hydrolyzes amidinoproclavaminate to yield proclavaminate and urea in clavulanic acid biosynthesis. Clavulanic acid is an effective inhibitor of beta-lactamases and is used in combination with amoxicillin to prevent the beta-lactam rings of the antibiotic from hydrolysis and, thus keeping the antibiotic biologically active. GbuA hydrolyzes 4-guanidinobutyrate (4-GB) into 4-aminobutyrate and urea while GpuA hydrolyzes 3-guanidinopropionate (3-GP) into beta-alanine and urea. Mutation studies show that significant variations in two active site loops in these two enzymes may be important for substrate specificity. This subfamily belongs to the ureohydrolase superfamily, which includes arginase, agmatinase, proclavaminate amidinohydrolase, and formiminoglutamase
GIATFMRLPYVRDLEGADVAVVGVPFDTGVSYRPGARFGPRAIRQASRLLRPYNPATGVDPFDWLKVVDC
GDVPVTPGDIEDALEQIEEAYRAILAAGPRPLTLGGDHSITLPILRALAKKHGPVALVHFDAHLDTWDPY
FGEKYNHGTPFRRAVEEGLLDPKRSIQIGIRGSLYSPDDLEDDRDLGFRVITADEVDDIGLDAIIEKIRE
RVGDGPVYLSFDIDVLDPAFAPGTGTPEIGGLTSREALEILRGLAGLNIVGADVVEVSPPYDHAEITALA
AANLAFELL
>gnl|CDD|212539 cd11593, Agmatinase-like_2, Agmatinase and related proteins. This family includes known and predicted bacterial and archaeal agmatinase (agmatine ureohydrolase; AUH; SpeB; EC=3.5.3.11), a binuclear manganese metalloenzyme that belongs to the ureohydrolase superfamily. It is a key enzyme in the synthesis of polyamine putrescine; it catalyzes hydrolysis of agmatine to yield urea and putrescine, the precursor for biosynthesis of higher polyamines, spermidine, and spermine. As compared to E. coli where two paths to putrescine exist, via decarboxylation of an amino acid, ornithine or arginine, a single path is found in Bacillus subtilis, where polyamine synthesis starts with agmatine; the speE and speB encode spermidine synthase and agmatinase, respectively. The level of agmatinase synthesis is very low, allowing strict control on the synthesis of putrescine and therefore, of all polyamines, consistent with polyamine levels in the cell. This subfamily belongs to the ureohydrolase superfamily, which includes arginase, agmatinase, proclavaminate amidinohydrolase, and formiminoglutamase
FVILGVPYDGTVSYRPGTRFGPAAIREASYQLELYSPYLDRDLEDIPFYDLGDLTLPPGDPEKVLERIEE
AVKELLDDGKFPIVLGGEHSITLGAVRALAEKYPDLGVLHFDAHADLRDEYEGSKYSHACVMRRILELGG
VKRLVQVGIRSGSKEEFEFAKEKGVRIYTFDDFDLGRWLDELIKVLPEKPVYISIDIDVLDPAFAPGTGT
PEPGGLSWRELLDLLRALAESKNIVGFDVVELSPDYDGGVTAFLAAKLVYELI
>gnl|CDD|212540 cd11598, HDAC_Hos2, Class I histone deacetylases including ScHos2 and SpPhd1. This subfamily includes Class I histone deacetylase (HDAC) Hos2 from Saccharomyces cerevisiae as well as a histone deacetylase Phd1 from Schizosaccharomyces pombe. Hos2 binds to the coding regions of genes during gene activation, specifically it deacetylates the lysines in H3 and H4 histone tails. It is preferentially associated with genes of high activity genome-wide and is shown to be necessary for efficient transcription. Thus, Hos2 is directly required for gene activation in contrast to other class I histone deacetylases. Protein encoded by phd1 is inhibited by trichostatin A (TSA), a specific inhibitor of histone deacetylase, and is involved in the meiotic cell cycle in S. pombe. Class 1 HDACs are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98)
VSYHFNSRVEDYHFGRTHPMKPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLSKVS
PENANQLRFDKAEPFNIGDDCPVFDGMYDYCQLYAGASLDAARKLCSGQSDIAINWSGGLHHAKKSEASG
FCYVNDIVLAILNLLRYFPRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYNGEFFPGTGDLDDNGGTP
GKHFALNVPLEDGIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDRLGQFNLNIKAHGACVKFV
KSFGIPMLVVGGGGYTPRNVARAWCYETAVA
>gnl|CDD|212541 cd11599, HDAC_classII_2, Histone deacetylases and histone-like deacetylases, classII. This subfamily includes eukaryotic as well as bacterial Class II histone deacetylase (HDAC) and related proteins. Deacetylases of class II are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. In D. discoideum, where four homologs (HdaA, HdaB, HdaC, HdaD) have been identified, HDAC activity is important for regulating the timing of gene expression during development. Also, inhibition of HDAC activity by trichostatin A is shown to cause hyperacetylation of the histone and a delay in cell aggregation and differentiation
HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYVDRLEAAAPEEGLVQLDPDTAMSPG
SLEAALRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLERVAI
VDFDVHHGNGTEDIFRDDPRVLFCSSHQHPLYPGTGAPDETGHGNIVNVPLPAGTGGAEFREAVEDRWLP
ALDAFKPDLILISAGFDAHRDDPLAQLNLTEEDYAWITEQLMDVADRYCDGRIVSVLEGGYDLSALARSV
AAHVRALM
>gnl|CDD|212542 cd11600, HDAC_Clr3, Class II Histone deacetylase Clr3 and similar proteins. Clr3 is a class II Histone deacetylase Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Clr3 is the homolog of the class-II HDAC HdaI in S. cerevisiae, and is essential for silencing in heterochromatin regions, such as centromeric regions, ribosomal DNA, the mating-type region and telomeric loci. Clr3 has also been implicated in the regulation of stress-related genes; the histone acetyltransferase, Gcn5, in S. cerevisiae, preferentially acetylates global histone H3K14 while Clr3 preferentially deacetylates H3K14ac, and therefore, interplay between Gcn5 and Clr3 is crucial for the regulation of many stress-response genes
DPHPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEIFE
RDSLYVNNDTAFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQT
EYPDKIKKILILDWDIHHGNGTQRAFYDDPNVLYISLHRFENGGFYPGTPYGDYESVGEGAGLGFNVNIP
WPQGGMGDADYIYAFQRIVMPIAYEFDPDLVIISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGKL
VVALEGGYNLDAISDSALAVAKVLLGEAPPKLP
>gnl|CDD|409282 cd11601, Nip7_N-like, N-terminal domain of Nip7 and similar proteins. This domain of various proteins is often found N-terminal to a PUA (PseudoUridine synthase and Archaeosine transglycosylase) RNA binding domain. The family contains Nip7, a protein that was shown to be required for efficient biogenesis of the 60S ribosome subunit in Saccharomyces cerevisiae. Recently, it was demonstrated that human Nip7 is essential in the accurate processing of pre-rRNA. Also included are KD93, a human homolog of Nip7, as well as an archaeal homolog and bacterial RsmB/RsmF family ribosomal methyltransferases
RQXTKEEEKLWTEFSNKYHYEATGRFLVFNDHVYEVPEELAKSLDGIKVVPYSLGTHLGDFKKDNKFEPS
YALALA
>gnl|CDD|211427 cd11602, Ndc10, Ndc10 component of the yeast centromere-binding factor 3. Ndc10 is a multidomain protein conserved in Saccharomycotina that interacts with kinetochore components. This model characterizes the majority of the protein; some family members may have an additional C-terminal domain that is homologous to transcriptional activators (GCR1_C). Ndc10 is part of the centromere-binding factor 3 (CBF3) complex in budding yeast. The CBF3 complex contains four essential proteins, Ndc10, Cep3, Ctf13, and Skp1. CBF3/Ndc10 is essential for the recruitment of the centromeric nucleosome and formation of the kinetochore. The Kinetochore is the large, multiprotein assembly that serves to connect condensed sister chromatids to the mitotic spindle. Ndc10 forms a dimer and it has non-sequence-specific DNA binding activity via the DNA backbone. Ndc10 also plays an important role in the coordination of cell division. It has been noted that the protein bears resemblance to the tyrosine recombinases (type IB topoisomerase/lambda-integrase)
KIQKLLDSLSPRTAHQYKSYYTKYIEWCRQKGLLPGSENDEEPYRKLPLSAQLVHWFLIDTYITNDPNEE
SVAFKIKTLKKIISSLKFLSKLCDIHNNDDEDPLDEKYLESIIKLHSFWYSLLKNNNQSNTTPPLLKVSI
NLWNPHTTNLSEKYFKTCLEKLRFLVDFHFRNYTNLSYEQRSKIKLSDLKGHKDDNNSSLGLYRSNVTSQ
NGHQPLVLVPQDCPFICPITTLAAYLYLRFYGIKKVYKGDGFPDLSQWEDLPIIRGKSLLDYPREETLGN
YYSTIFRYCHLPYKRREYFQDSQLQYPDWSDEEYNTFFEAYPSESDSAFPYNIPLDYIRIMNLRLSPEAQ
DFIDLMEVLRNVLVSNLPWIYRFFPDHDIFKDPILQNPEFQSYFNDVIGLENQSNGMDQLPFR
>gnl|CDD|211428 cd11603, ThermoDBP, Thermoproteales single-stranded DNA-binding (SSB) domain. ThermoDBP is a SSB protein of the Thermoproteales. SSB proteins are essential for the genome maintenance of all known cellular organisms. Many SSBs contain an OB fold domain, albeit with low sequence conservation and OB fold-containing SSB proteins have been detected in all three domains of life. However, one group of Crenarchaea, the Thermoproteales, lack SSB encoding genes. The Thermoproteales SSB protein, ThermoDBP, lacks the OB fold and binds specifically to ssDNA with low sequence specificity. Its three-dimensional structure resembles that of the Hut operon positive regulatory protein HutP
ERGEVRSELVTEAGKKILKIKWNTGKTSAGRLFGRYGRGGRPDFFRLLFGAVAGSLRSQFGPDKGEELFN
NIRNSQEFKKSLNEVFDSIKRWFFNEAVPKYNLERGDVFMISTELELDIETGELKWNKEKTQVIYWVRSD
R
>gnl|CDD|211429 cd11604, RTT106_N, histone chaperone RTT106, regulator of Ty1 transposition protein 106; N-terminal homodimerization domain. This cd includes the N-terminal homodimerization domain of Saccharomyces cerevisiae Rtt106, a histone chaperone. In addition to this domain, Rtt106 contains two C-terminal pleckstrin-homology (PH) domains. The acetylation of lysine 56 in histone H3 (H3K56ac) is implicated in regulating nucleosome disassembly during gene transcription, and nucleosome assembly during DNA replication and repair. Rtt106 has been shown to aid in the efficient deposition of newly synthesized H3K56ac onto replicating DNA. The interaction of Rtt106 with (H3-H4)2, most likely in the form of a (H3-H4)2 tetramer, is important for gene silencing and for the DNA damage response. Data supports a combinatorial interaction: this N-terminal domain homodimerizes and intercalates between the two H3-H4 components of the (H3-H4)2 tetramer, independent of acetylation, and the two double PH domains bind the K56-containing region of H3. Acetylation of K56 increases the affinity of the interaction. Rtt106 also interacts with both the SWI/SNF and RSC chromatin remodeling complexes and is involved in their cell-cycle dependent recruitment to histone gene pairs regulated by the HIR co-repressor complex (HTA1-HTB1, HHT1-HHF1, and HHT2-HHF2). Saccharomyces cerevisiae Rtt106 also plays a role in a role in regulating Ty1 transposition
DDFLDKLPEELRNKVLTIVRKDPSSLEIFEELYNYALESNDEEKKRKISKTGSS
>gnl|CDD|467641 cd11605, RWD_DRWD_ELF-like, RWD, DRWD, and ELF domain family. The family includes the RWD, double-RWD (DRWD), and ELF domains. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. The RWD domain (named after three major RWD-containing proteins: RING finger, WD-repeat-containing proteins and DEXD-like helicases) mediates protein-protein interactions in a variety of pathways in eukaryotes. The DRWD domain is responsible for substrate binding. It is involved in interactions with other kinetochore proteins. The ELF (N-terminal E2-like fold) domain is found in all Fanconi anemia group L protein (FANCL) homologs. It is required to promote efficient DNA damage-induced FANCD2 (Fanconi anemia group D2 protein) monoubiquitination in vertebrate cells
ALESIYGDELEVLSDDSPLRFSIRLSPEEEEDDPPLELEFTLPPGYPPEEPPLITLRSPKLSSAERLSLL
KLELEEAAEENLGEPMLFDLVEAL
>gnl|CDD|212156 cd11606, COE_DBD, Colier/Olf/Early B-cell factor (EBF) DNA Binding Domain. COE_DBD is the amino-terminal DNA binding domain of the COE protein family. The COE transcription factor is a regulator of development in several organs and tissues that contain the DBD domain as well as IPT/TIG (immunoglobulin-like, Plexins, transcription factors/transcription factor immunoglobulin) and basic helix-loop-helix (bHLH) domains. COE has four members in mammals (COE1-4) with high sequence similarity at the amino-terminal region. COE_DBD requires a zinc ion to bind DNA and contains a zinc finger motif (H-X(3)-C-X(2)-C-X(5)-C) termed the zinc knuckle. COE is homo- or heterodimerized through the bHLH domain to bind DNA. COE1-4 each has a variant due to alternative splicing. However, this alternative splicing does not occur at the DBD domain
GVTDPSAAQTSVGLARAHFEKQPPSNLRKSNFFHFVLALYDRQGQPIEVERTAFVDFVEKEREQGGEKTN
NGIHYRLQLLYSNGIRTEQDLYVRLIDSSTKQAIPYEGQDKNPEMCRVLLTHEIMCSRCCEKKSCGNRNE
TPSDPVIIDRFFLKFFLKCNQNCLKNAGNPRDMRRFQVVLSTTVNVDGHVLAVSDNMFVHNNSKHGRRAR
RL
>gnl|CDD|211320 cd11607, DENR_C, C-terminal domain of DENR and related proteins. DENR (density regulated protein), together with MCT-1 (multiple copies T cell malignancies), has been shown to have similar function as eIF2D translation initiation factor (also known as ligatin), which is involved in the recruitment and delivery of aminoacyl-tRNAs to the P-site of the eukaryotic ribosome in a GTP-independent manner
SKVTIKRISRNKRKFVTTVTGLETFGIDLKKAAKLFAKKFACGASVTKGAEGKDEIVIQGDVTDDIVDLI
LEKWPEIDEDNIEILG
>gnl|CDD|211321 cd11608, eIF2D_C, C-terminal domain of eIF2D and related proteins. eIF2D translation initiation factor (also known as ligatin) is involved in the recruitment and delivery of aminoacyl-tRNAs to the P-site of the eukaryotic ribosome in a GTP-independent manner
PIDITTERRQGNKKVTLISGLESFGIDPEEFAKELQKKCAASTSVSPLPGKKKGVEVQVQGNQVKFVAKL
LTEKYGVPKKYIDGL
>gnl|CDD|211422 cd11609, MCT1_N, N-terminal domain of multiple copies T cell malignancies 1 and related proteins. This N-terminal domain of MCT-1 (multiple copies T cell malignancies 1), also known as MCTS-1 (malignant T cell-amplified sequence 1), co-occurs with a PUA domain. MCT-1, together with DENR (density regulated protein), has been shown to have similar function as eIF2D translation initiation factor (also known as ligatin), which is involved in the recruitment and delivery of aminoacyl-tRNAs to the P-site of the eukaryotic ribosome in a GTP-independent manner
KFFEKEDVSGQTQLKSSVQRGIRAKLLEQYPLLEPYIDEILPKKEPLVLVKCHDHIELLVVNGEPLFFQH
RDGPYIP
>gnl|CDD|211423 cd11610, eIF2D_N, N-terminal domain of eIF2D and related proteins. This N-terminal domain of eIF2D co-occurs with a PUA domain. eIF2D translation initiation factor (also known as ligatin) is involved in the recruitment and delivery of aminoacyl-tRNAs to the P-site of the eukaryotic ribosome in a GTP-independent manner
FRVKSNTALKGSDRKKLRARVLKAFPLLTEEDLDELVPNKEELSVVKLVTHGERVTVYSVDGVPLFFELS
DGNLYP
>gnl|CDD|212157 cd11611, SAF, Domains similar to fish antifreeze type III protein. SAF domains are found in a wide variety of proteins with quite different functions. They are components of enzymes, such as D-altronate-dehydratases or sialic acid synthetases, of antifreeze proteins conserved in fish (where they bind to nascent ice crystals), and may act as periplasmic chaperones in bacterial flagella basal body P-ring formation
VVVAKRNIAVGDVIKEDDVRLEKRNVFYGEPFFDVSEVVGKTSRRYLAEGTVLTAD
>gnl|CDD|212158 cd11613, SAF_AH_GD, Domains similar to fish antifreeze type III protein. Altronate dehydratase (EC 4.2.1.7) converts D-altronate into 2-dehydro-3-deoxy-D-gluconate and is part of a bacterial pathway for the degradation of D-galacturonate. D-galactarate dehydratase (EC 4.2.1.42) eliminates water from D-galactarate to yield 5-dehydro-4-deoxy-D-glucarate, initializing the degradation of D-galactarate. The function of the SAF domain in these enzymes is not clear. It may participate in dimerization
KAIKLHPKDNVAVALRDLKAGEVVEVDGEGVTLLEDIPAGHKIALRDIAAGEPVIKYGEPIGKATRDIAA
GEHVHTHNVK
>gnl|CDD|212159 cd11614, SAF_CpaB_FlgA_like, SAF domains of the flagella basal body P-ring formation protein FlgA and the flp pilus assembly CpaB. FlgA is a putative periplasmic chaperone that assists in the formation of the flagellar P ring; CpaB is a protein invoved in the assembly of the flp pili, which are bacterial virulence factors mediating non-specific adherence to surfaces; these proteins appear to contain a single SAF domain. This intermediate family also contains the SAF domains of sialic acid synthetases and type III antifreeze proteins, which also share the same extensive core structure
PVVVAARDLPAGTVITADDLTLVEVPLSLLPPGALTDPDDVVGRVARRPLRAGEPITASML
>gnl|CDD|212160 cd11615, SAF_NeuB_like, C-terminal SAF domain of sialic acid synthetase. Sialic acid synthetase (N-acetylneuraminate synthase or N-acetylneuraminate-9-phosphate synthase) catalyzes the condensation of phosphoenolpyruvate with N-acetylmannosamine (ManNAc, in bacteria) or N-acetylmannosamine-6-phosphate (ManNAc-6P, in mammals), to yield N-acetylneuramic acid (NeuNAc) or N-acetylneuramic acid-9-phosphate (NeuNAc-9P), respectively. The N-terminal NeuB domain, a TIM-barrel-like structure, contains the catalytic site, the function of the SAF domain is not as clear. It may participate in domain-swapped dimerization and play a role in binding the substrate, in either domain-swapped dimers or by directly interacting with the N-terminal domain. Also included in the family are PEP-sugar pyruvyltransferases known as spore coat polysaccharide biosynthesis proteins (SpsE)
RRSLVAARDIKAGEVLTEENLRVKRPGGGLSPKYLDEVLGKKAKRDIKAGEPLTWDDL
>gnl|CDD|212161 cd11616, SAF_DH_OX_like, SAF domain of putative dehydrogenases or oxidoreductases. C-terminal SAF domain of an uncharacterized family of putative dehydrogenases or oxidoreductases, which are otherwise members of the NAD(P)-dependent Rossmann-fold superfamily
VVAVAKRDLKAGEVLDGIGGYTVYGGLEPAADARAENALPIGLATGARLKRDVKKGELITYDDVELDEGS
LAVRLRREQD
>gnl|CDD|212162 cd11617, Antifreeze_III, Type III antifreeze protein, may be specific to the Zoarcoidei. Antifreeze protein III inhibits the growth of ice crystals and protects fish from cold damage in sub-freezing temperatures
ASVVATQLIPINTALTLVMMKAKVVTPMGIPAEEIPRLVGMQVNRAVPLGTTLMPDMVKGYA
>gnl|CDD|211316 cd11618, ChtBD1_1, Hevein or type 1 chitin binding domain; filamentous ascomycete subfamily. Hevein or type 1 chitin binding domain (ChtBD1), a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements
TCGGDNGYTCAGSGFGNCCSAYGWCGNTSDHCGVGCQPGFGKCG
>gnl|CDD|212009 cd11619, HR1_CIP4-like, Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Cdc42-Interacting Protein 4 and similar proteins. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. It functions downstream of Cdc42 in PDGF-dependent actin reorganization and cell migration, and also regulates the activity of PDGFRbeta. It uses Src as a substrate in regulating the invasiveness of breast tumor cells. CIP4 may also play a role in the pathogenesis of Huntington's disease. Members of this subfamily typically contain an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain, central HR1 domain, and a C-terminal SH3 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; the HR1 domain of CIP4 binds Cdc42 and TC10. Translocation of CIP4 is facilitated by its binding to TC10 at the plasma membrane
PEQRRKKLQQKIDELEKEIEKETKSRDGLMKMKGVYEQNPQLGDPASVEGQLAEYAKKLDKLREELQKYQ
GYLAEAE
>gnl|CDD|212010 cd11620, HR1_PKC-like_2_fungi, Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of fungal Protein Kinase C-like proteins. This subfamily is composed of fungal PKC-like proteins including Pkc1p from Saccharomyces cerevisiae, and Pck1p and Pck2p from Schizosaccharomyces pombe. The yeast PKC-like proteins play a critical role in regulating cell wall biosynthesis and maintaining cell wall integrity. They contain two HR1 domains, C2 and C1 domains, and a kinase domain. This model characterizes the second HR1 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family. The HR1 domains of Pck1p and Pck2p interact with GTP-bound Rho1p and Rho2p
PLTGAKIQRMLQQLEFKLQVEKQYKEGIEKMARLYQAEGDKRSIADAENKRVESEQKIQLLKKALKRYQD
LH
>gnl|CDD|212011 cd11621, HR1_PKC-like_1_fungi, First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of fungal Protein Kinase C-like proteins. This subfamily is composed of fungal PKC-like proteins including Pkc1p from Saccharomyces cerevisiae, and Pck1p and Pck2p from Schizosaccharomyces pombe. The yeast PKC-like proteins play a critical role in regulating cell wall biosynthesis and maintaining cell wall integrity. They contain two HR1 domains, C2 and C1 domains, and a kinase domain. This model characterizes the first HR1 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family. The HR1 domains of Pck1p and Pck2p interact with GTP-bound Rho1p and Rho2p
DSIEEAIQDVYKKIERERSLIQGAKAMKKSTKNPEVIQRLNSNIRESRSNIDYLEERLNKLTLRKAGVSS
GQ
>gnl|CDD|212012 cd11622, HR1_PKN_1, First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N. PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the first HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family
QQKLEELKEQIRREIRKELKIKEGAENLRKATTDKKSLAHVESILKKSNRKLEDLHQELQELEAHI
>gnl|CDD|212013 cd11623, HR1_PKN_2, Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N. PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the second HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family
ENAQNSRLAGLEKQLNIELKVKQGAENMIQMYSNGKSKDRKLLAEAQQMLEDSKAKIEFLRMQILRAKQQ
A
>gnl|CDD|212014 cd11624, HR1_Rhophilin, Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rhophilin. Rhophilins are scaffolding proteins that function as effectors of the Rho family of small GTPases. Vertebrates harbor two proteins, Rhophilin-1 and Rhophilin-2, whose exact functions are yet to be determined. Rhophilin-1 has been implicated in sperm motility. Rhophilin-2 regulates the organization of the actin cytoskeleton. Rhophilins contain N-terminal HR1, central Bro1-like, and C-terminal PDZ domains; all are protein-interacting domains. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; both Rhophilin-1 and Rhophilin-2 bind RhoA, and Rhophilin-2 has also been shown to bind RhoB
QSGRSQLQHKRAALNQKIHKQMKLRAGAENLFKATKNTKVKETVRLELSFVNSQLQLLKEELEGINSSLE
VYQNVS
>gnl|CDD|212015 cd11625, HR1_PKN_3, Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N. PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the third HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family
GPLLLPLELRIEELRHHLRVETAVVEGAKNVIKLLQNAKKDDKKALQEAQKSLSESSQKLDLLRLSLERR
LAEL
>gnl|CDD|212016 cd11626, HR1_ROCK, Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It is a serine/threonine protein kinase that is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. ROCKs are the best-described effectors of RhoA. There are two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. ROCK contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family
ALLQHRQQEYQRKADMEAEKRRNVENDVAALKDQLEDLKKQKQESQKAEEKARQLQKQLEEANRLL
>gnl|CDD|212017 cd11627, HR1_Ste20-like, Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Schizosaccharomyces pombe Ste20-like proteins. This group is composed of predominantly uncharacterized fungal proteins, which contain two known domains: HR1 at the N-terminal region and REM (Ras exchanger motif) at the C-terminal region. One member protein from Schizosaccharomyces pombe is named Ste16 while its gene is called ste20 (a target of rapamycin complex 2 subunit). It is a subunit in the protein kinase TOR complexes in fission yeast. The REM domain is usually found in nucleotide exchange factors for Ras-like small GTPases. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family
LVSEQRLEELRGKLEIETKIKDGAENLLQVLDSKNAKEKKDQRARVESELNSSNRKIAQLTSQLEEEIQR
N
>gnl|CDD|212018 cd11628, HR1_CIP4_FNBP1L, Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of vertebrate Cdc42-Interacting Protein 4 and FormiN Binding Protein 1-Like. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. FNBP1L, also called Toca-1 (Transducer of Cdc42-dependent actin assembly 1), forms a complex with neural WASP; the complex induces the formation of filopodia and endocytic vesicles. FNBP1L is required for Cdc42-induced actin assembly and is essential for autophagy of intracellular pathogens. CIP4 may also play a role in phagocytosis. It functions downstream of Cdc42 in PDGF-dependent actin reorganization and cell migration, and also regulates the activity of PDGFRbeta. It uses Src as a substrate in regulating the invasiveness of breast tumor cells. CIP4 may also play a role in the pathogenesis of Huntington's disease. CIP4 and FNBP1L contain an N-terminal F-BAR domain, a central HR1 domain, and a C-terminal SH3 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; the HR1 domain of CIP4 binds Cdc42 and TC10. Translocation of CIP4 is facilitated by its binding to TC10 at the plasma membrane
PPEQRRKRLQQKIDELSRELQKEMDQSEALMKMKDVYEKNPQMGDPASLQPQIAETASNIDRLRGELHKY
EAWLAEAEGRV
>gnl|CDD|212019 cd11629, HR1_FBP17, Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Formin Binding Protein 17. FBP17, also called FormiN Binding Protein 1 (FNBP1), is involved in dynamin-mediated endocytosis. It is recruited to clathrin-coated pits late in the endocytosis process and may play a role in the invagination and scission steps. FBP17 binds in vivo to tankyrase, a protein involved in telomere maintenance and mitogen activated protein kinase (MAPK) signaling. It also binds to the Fas ligand and may be implicated in the inflammatory response. FBP17 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain, central HR1 domain, and a C-terminal SH3 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; the HR1 domain of the related protein, CIP4, binds Cdc42 and TC10. Translocation of CIP4 is facilitated by its binding to TC10 at the plasma membrane
PEQRRKKLQQKVDELNKDIQKEMDQRDALTKMKDVYIKNPQMGDPASVDHRLEEITQNIEKLRVEVQKFE
GWLAEVE
>gnl|CDD|212020 cd11630, HR1_PKN1_2, Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N1. PKN1, also called PKNalpha or Protein-kinase C-related kinase 1 (PRK1), is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, and by fatty acids such as arachidonic and linoleic acids. It is expressed ubiquitously and is the most abundant PKN isoform in neurons. PKN1 is implicated in a variety of functions including cytoskeletal reorganization, cardiac cell survival, cell adhesion, and glucose transport, among others. PKN1 contains three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the second HR1 domain of PKN1. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN1 binds the GTPases RhoA, RhoB, and RhoC, and can also interact weakly with Rac
GRSAANQSRIAGLEKQLNIELKVKQGAENMIQTYANGSTKDRKLLQTAQQMLQDSKTKIDIIRMQIRKAM
QADELENQ
>gnl|CDD|212021 cd11631, HR1_PKN2_2, Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N2. PKN2, also called PKNgamma or Protein-kinase C-related kinase 2 (PRK2), is a serine/threonine protein kinase and an effector of the small GTPase Rho/Rac. It regulates G2/M cell cycle progression and the exit from cytokinesis. It also phosphorylates hepatitis C virus (HCV) RNA polymerase and thus, plays a role in HCV RNA replication. PKN2 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN2 contains a proline-rich region in between its C2 and kinase domains and has been shown to associate with SH3 domain containing proteins like NCK and Grb4. This model characterizes the second HR1 domain of PKN2. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN2 specifically binds to RhoA GTPase in a GTP-dependent manner. The HR1 domains of PKN2, together with its C2 domain, also facilitate the recruitment of PKN2 to primordial junctions at nascent cell-cell contacts, where it promotes junctional maturation
STRMSTNNNRLMALKKQLDIELKVKQGAENMIQMYSNGSSKDRKLLATAQQMLQDSKTKIEVIRMQILQA
VQTN
>gnl|CDD|212022 cd11632, HR1_PKN3_2, Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N3. PKN3, also called PKNbeta, is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, preferentially by RhoC. Both PKN1 and RhoC show limited and barely detectable expression in normal tissues, but are both upregulated in cancer cells, particularly in late-stage malignancies. PKN3 has been implicated to play a role in the metastatic growth and invasiveness of cancer cells, downstream of the oncogenic phosphoinositide 3-kinase signaling network. PKN3 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN3 contains two proline-rich regions between its C2 and kinase domains, and has been shown to associate with SH3 domain containing proteins like GRAFs, GAP for RhoA, and Cdc42Hs. This model characterizes the second HR1 domain of PKN3. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN3 binds Rho family GTPases, preferentially RhoC
EWATDPRARRLEALKRQLHVELKVKQGAENMIQTYSSGTSKERKLLATAQQMLQDSRTKIELLRMQIVKL
EQSG
>gnl|CDD|212023 cd11633, HR1_Rhophilin-1, Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rhophilin-1. Rhophilin-1 is a scaffolding protein that functions as an effector of the Rho family of small GTPases. It has been implicated in sperm motility. Rhophilin-1 contains an N-terminal HR1, a central Bro1-like, and a C-terminal PDZ domain; all are protein-interacting domains. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; Rhophilin-1 binds RhoA was isolated initially as a RhoA-binding protein
GCDPLAATQRSKLQSRRARINQQINKEMRMRAGAENLFKATSNKKVRETVALELSFVNSNLQLLKEELAE
LNSSVEIYQSDSEAI
>gnl|CDD|212024 cd11634, HR1_Rhophilin-2, Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rhophilin-2. Rhophilin-2 is a scaffolding protein that functions as an effector of the Rho family of small GTPases. It plays a role in regulating the organization of the actin cytoskeleton. Rhophilin-2 contains an N-terminal HR1, a central Bro1-like, and a C-terminal PDZ domain; all are protein-interacting domains. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; Rhophilin-2 has been shown to bind both RhoA and RhoB
PLAQTGRSKLQNQRAVLNQQILKAMRMRAGAENLLKATTNNKVREQVLLELSFVNSDLQLLKEELEGLNI
SVEVYQNTEEAS
>gnl|CDD|212025 cd11635, HR1_PKN2_3, Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N2. PKN2, also called PKNgamma or Protein-kinase C-related kinase 2 (PRK2), is a serine/threonine protein kinase and an effector of the small GTPase Rho/Rac. It regulates G2/M cell cycle progression and the exit from cytokinesis. It also phosphorylates hepatitis C virus (HCV) RNA polymerase and thus, plays a role in HCV RNA replication. PKN2 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN2 contains a proline-rich region in between its C2 and kinase domains and has been shown to associate with SH3 domain containing proteins like NCK and Grb4. This model characterizes the third HR1 domain of PKN2. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN2 specifically binds to RhoA GTPase in a GTP-dependent manner. The HR1 domains of PKN2, together with its C2 domain, also facilitate the recruitment of PKN2 to primordial junctions at nascent cell-cell contacts, where it promotes junctional maturation
KPVISPLELRMEELRHHFRIESAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQR
LNEL
>gnl|CDD|212026 cd11636, HR1_PKN1_3, Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N1. PKN1, also called PKNalpha or Protein-kinase C-related kinase 1 (PRK1), is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, and by fatty acids such as arachidonic and linoleic acids. It is expressed ubiquitously and is the most abundant PKN isoform in neurons. PKN1 is implicated in a variety of functions including cytoskeletal reorganization, cardiac cell survival, cell adhesion, and glucose transport, among others. PKN1 contains three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the third HR1 domain of PKN1. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN1 binds the GTPases RhoA, RhoB, and RhoC, and can also interact weakly with Rac
KPDLCAVELRIEELRHHFRVEHAVAEGAKNVLRLLGAGKAQDRKAISEAQSKLSESSQKLDLLRVSLEQR
LVEL
>gnl|CDD|212027 cd11637, HR1_PKN3_3, Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N3. PKN3, also called PKNbeta, is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, preferentially by RhoC. Both PKN1 and RhoC show limited and barely detectable expression in normal tissues, but are both upregulated in cancer cells, particularly in late-stage malignancies. PKN3 has been implicated to play a role in the metastatic growth and invasiveness of cancer cells, downstream of the oncogenic phosphoinositide 3-kinase signaling network. PKN3 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN3 contains two proline-rich regions between its C2 and kinase domains, and has been shown to associate with SH3 domain containing proteins like GRAFs, GAP for RhoA, and Cdc42Hs. This model characterizes the third HR1 domain of PKN3. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN3 binds Rho family GTPases, preferentially RhoC
GRPMSAPELRVEELRHHLRIEAAVAEGAKNVVKLLGGRRFQDRKILAEAQARLQESSQKIDLLRLSLERC
LAAL
>gnl|CDD|212028 cd11638, HR1_ROCK2, Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 2. ROCK2 is a serine/threonine protein kinase and was the first identified target of activated RhoA. It plays a role in stress fiber and focal adhesion formation, and is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK2 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. ROCK2 is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family
KALLQHKNTEYQRKAEHEADRKRNLENEVNSLKDQLEDLKKKNQNSQISNEKNIQLQRQLDEANALL
>gnl|CDD|212029 cd11639, HR1_ROCK1, Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 1. ROCK1 is a serine/threonine kinase and is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK1 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. It is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family
MMLQHRINEYQRKAEQESEKRRNVENEVSTLKDQLEDLKKISQNSQITNEKINQLQKQLEEANDLL
>gnl|CDD|212163 cd11640, HutP, Histidine Utilizing Protein, the hut operon positive regulatory protein. The HutP protein family regulates the expression of 'hut' structural genes in Bacillus and other bacteria. It forms an anti-termination complex, which recognizes three UAG triplet units, separated by four non-conserved nucleotides on the RNA terminator region. In an L-histidine and Mg2+ dependent manner, HutP binds to the nascent hut mRNA leader transcript, and the ensuing anti-termination complex inhibits formation of a stem-loop terminator, clearing the way for transcription of the hut structural genes
SIDVGRAALLLAMTETREEEDELKKKLLEKGIKVVATDVGGKFSESIPKIIESAVVAAKRTGVIEESHVE
EHALIHATREALSQLMAKVAIGLNVGGKIAIVRGGEWLAVAIYGEIGLHHLLNHERIGLGHRHL
>gnl|CDD|381168 cd11641, Precorrin-4_C11-MT, Precorrin-4 C11-methyltransferase (CbiF/CobM). Precorrin-4 C11-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. In the aerobic pathway, CobM catalyzes the methylation of precorrin-4 at C-11 to yield precorrin-5. In the anaerobic pathway, CibF catalyzes the methylation of cobalt-precorrin-4 to cobalt-precorrin-5. Both CibF and CobM, which are homologous, are included in this model. There are about 30 enzymes involved in vitamin B12 synthetic pathway. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared in both pathways and several of these enzymes are pathway-specific
VGAGPGDPELITVKGARLLEEADVVIYAGSLVPPELLAYAKPGAEIVDSAGMTLEEIIEVMREAAREGKD
VVRLHTGDPSLYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRLEGRTPVP
EGESLRELAKHGATLAIFLSAALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEA
GITRTALILVGPALG
>gnl|CDD|381169 cd11642, SUMT, Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SUMT). SUMT is an enzyme of the cobalamin and siroheme biosynthetic pathway. It catalyzes the first of three steps leading to the formation of siroheme from uroporphyrinogen III; it transfers two methyl groups from S-adenosyl-L-methionine to the C-2 and C-7 atoms of uroporphyrinogen III to yield precorrin-2 via the intermediate formation of precorrin-1. Precorrin-2 is also a precursor for the biosynthesis of vitamin B12, coenzyme F430, siroheme and heme d1. This family includes proteins in which the SUMT domain is fused to other functional domains, such as to a uroporphyrinogen-III synthase domain to form bifunctional uroporphyrinogen-III methylase/uroporphyrinogen-III synthase, or to a dual function dehydrogenase-chelatase domain, as in the case of the multifunctional S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase/dehydrogenase/ferrochelatase CysG, which catalyzes all three steps that transform uroporphyrinogen III into siroheme
VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELA
REGKRVVRLKGGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHE
ADGKLPDDDAALARPGGTLVIYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEK
AAEAGIRSPALIVVGEVV
>gnl|CDD|381170 cd11643, Precorrin-6A-synthase, Precorrin-6A synthase (also named CobF). Precorrin-6A synthase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. This model represents CobF, the precorrin-6A synthase, an enzyme specific to the aerobic pathway. After precorrin-4 is methylated at C-11 by CobM to produce precorrin-5, CobF catalyzes the removal of the extruded acyl group in the subsequent step, and the addition of a methyl group at C-1. The product of this reaction is precorrin-6A, which gets reduced by an NADH-dependent reductase to yield precorrin-6B. This family includes enzymes in GC-rich Gram-positive bacteria, alpha proteobacteria and Pseudomonas-related species
LIGIGPGDPDHLTLQAIEALNRVDVFFVLDKGEEKSDLAALRREICERHLGDRPYRVVEFPDPERDRSPA
DYRAAVADWHDARAALWEDAIAEELPEGGTGAFLVWGDPSLYDSTLRILDRLRAGRVALEVEVIPGISSV
QALAARHRIPLNRIGEPVHITTGRRLAEGGPAGVDNVVVMLDGGCAFRRLAGPDLEIYWGAYLGTPDEIL
ISGPLADVADEIAALRAEARARHGWIMDTYLLRR
>gnl|CDD|381171 cd11644, Precorrin-6Y-MT, Precorrin-6Y methyltransferase (also named CbiE). CbiE (precorrin-6Y methyltransferase, also known as cobalt-precorrin-7 C(5)-methyltransferase, also known as cobalt-precorrin-6Y C(5)-methyltransferase) catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8. It participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. CbiE functions in the anaerobic pathway, it is a subunit of precorrin-6Y C5,15-methyltransferase, a bifunctional enzyme: cobalt-precorrin-7 C(5)-methyltransferase (CbiE)/cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (CbiT), that catalyzes two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. CbiE and CbiT can be found fused (CbiET, also called CobL), or on separate protein chains (CbiE and CbiT). In the aerobic pathway, a single enzyme called CobL catalyzes the methylations at C-5 and C-15, and the decarboxylation of the C-12 acetate side chain of precorrin-6B
IGIGPGGPEYLTPEAREAIEEADVVIGAKRLLELFPDLGAEKIPLPSEDIAELLEEIAEAGKRVVVLASG
DPGFYGIGKTLLRRLGGEEVEVIPGISSVQLAAARLGLPWEDARLVSLHGRDLENLRRALRRGRKVFVLT
DGKNTPAEIARLLLERGLGDSRVTVGENLGYPDERITEGTAEELAEEEFSDLNVVLIE
>gnl|CDD|381172 cd11645, Precorrin_2_C20_MT, Precorrin-2 C20-methyltransferase, also named CobI or CbiL. Precorrin-2 C20-methyltransferase (also known as S-adenosyl-L-methionine--precorrin-2 methyltransferase) participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. Precorrin-2 C20-methyltransferase catalyzes methylation at the C-20 position of a cyclic tetrapyrrole ring of precorrin-2 using S-adenosylmethionine as a methyl group source to produce precorrin-3A. In the anaerobic pathway, cobalt is inserted into precorrin-2 by CbiK to generate cobalt-precorrin-2, which is the substrate for CbiL, a C20 methyltransferase. In Clostridium difficile, CbiK and CbiL are fused into a bifunctional enzyme. In the aerobic pathway, the precorrin-2 C20-methyltransferase is named CobI. This family includes CbiL and CobI precorrin-2 C20-methyltransferases, both as stand-alone enzymes and when CbiL forms part of a bifunctional enzyme
VGVGPGDPELLTLKAVRILKEADVIFVPVSKGGEGSAALIIAAALLIPDKEIIPLEFPMTKDREELEEAW
DEAAEEIAEELKEGKDVAFLTLGDPSLYSTFSYLLERLRAPGVEVEIIPGITSFSAAAARLGIPLAEGDE
SLAILPATYDEEELEKALENFDTVVLMKVGRNLEEIKELLEELGLLDKAVYVERCGMEGERIYTDLEELK
EEKLPYFSLIIVK
>gnl|CDD|381173 cd11646, Precorrin_3B_C17_MT, Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH). Precorrin-3B C(17)-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. This model includes CobJ of the aerobic pathway and CbiH of the anaerobic pathway, both as stand-alone enzymes and when CobJ or CbiH form part of bifunctional enzymes, such as in Mycobacterium tuberculosis CobIJ where CobJ fuses with a precorrin-2 C(20)-methyltransferase domain, or Bacillus megaterium CbiH60, where CbiH is fused to a nitrite and sulfite reductase-like domain. In the aerobic pathway, once CobG has generated precorrin-3b, CobJ catalyzes the methylation of precorrin-3b at C-17 to form precorrin-4 (the extruded methylated C-20 fragment is left attached as an acyl group at C-1). In the corresponding anaerobic pathway, CbiH carries out this ring contraction, using cobalt-precorrin-3b as a substrate to generate a tetramethylated delta-lactone
LYVVGIGPGSADLMTPRAREALEEADVIVGYKTYLDLIEDLLPGKEVISSGMGEEVERAREALELALEGK
RVALVSSGDPGIYGMAGLVLELLDERWDDIEVEVVPGITAALAAAALLGAPLGHDFAVISLSDLLTPWEV
IEKRLRAAAEADFVIALYNPRSKKRPWQLEKALEILLEHRPPDTPVGIVRNAGREGEEVTITTLGELDPE
DVDMFTTVIIGNSQTYIIGGKMITPRGY
>gnl|CDD|381174 cd11647, DHP5_DphB, diphthine methyl ester synthase and diphthine synthase. Eukaryotic diphthine methyl ester synthase (DHP5) and archaeal diphthamide synthase (DphB) participate in the second step of the biosynthetic pathway of diphthamide. The eukaryotic enzyme catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester; the archaeal enzyme, catalyzes only 3 methylations, producing diphthine. Diphtheria toxin ADP-ribosylates diphthamide leading to inhibition of protein synthesis in the eukaryotic host cells
MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKLEELEKLIGKKIILLDREDLEEESEEIL
EEAKKKDVALLVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTSGLQLYKFGRTVTIPFPEE
NYKPESPYDVIKENLKRGLHTLLLLDIKVEEGRFMTINEAIEILLEIEEKRKEGVITEDTLVVGLARLGS
DDQKIVAGTLKELLKEDFGPPPHSLIIPGKL
>gnl|CDD|381175 cd11648, RsmI, Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-)-methyltransferase. RsmI is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress
YLVATPIGNLEDITLRALEVLKEVDLIACEDTRHTRKLLNHYGIKKPLISYHEHNEKKRAEKIIELLKEG
KSVALVSDAGTPGISDPGYRLVRAAIEAGIEVVPIPGPSAVITALSASGLPTDRFTFLGFLPRKKGKRKK
LLEELAEEPRTLIFYESPHRILKTLEDLAEVGGDREVVVARELTKLHEEVIRGTLSELLEELEENKPKGE
FVLVVE
>gnl|CDD|381176 cd11649, RsmI_like, uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small subunit methyltransferase I (RsmI). RsmI, also known as rRNA (cytidine-2'-O-)-methyltransferase, is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress
LYLIPTPLGEESPDEVLPPEVLEIIRSLDHFIVENEKTARRFLKKLGPPKPIDELTFFELNKHTREEDLE
ELLKPLLEGKDIGLISEAGCPGVADPGAELVALAHRLGIKVVPLVGPSSILLALMASGLNGQNFAFHGYL
PIDKEERKKKLKELEKRSRKEGQTQIFIETPYRNNALLEDLLKTLQPDTRLCVACDLTGPSEFIKTKTIA
EWKKKKPDLHKRPAIFLLG
>gnl|CDD|212164 cd11650, AT4G37440_like, Uncharacterized protein domain conserved in plants. This domain contains an extensive protein sequence fragment that appears conserved in a number of plant proteins, including the gene product of Arabidopsis thaliana locus AT4G37440, which has been identified in transcriptional profiling as expressed at different levels in white cabbage cultivars
SGAEDVEVDIVGETTVRDNASEGDEDGDATESSSSFGDSDSASEDDSGGDADTEVDSPFFGGGGLGDTFD
SGPLKVRKKKLTAHWRRFIRPLMWRCKWLELRMKELQSQALKYDRELALIEQEKELQLEGTKAEGENSKS
APFSGERHERKVMKRRKRKRVEETVDVSLYMSKHPLFSYYENKKSKGGVERLIDDLPNDLTTADRVNRKD
PLDLKSSDLEDNDLSLEEILLKIEVLQSRVHKLKNRLSKVMSK
>gnl|CDD|212165 cd11651, YPK1_N_like, Fungal protein kinase domain similar to the N-terminus of YPK1. This fungal domain family includes the N-terminal region of the Saccharomyces cerevisiae AGC kinases YPK1 and YPK2, which were found to be essential for the proliferation of yeast. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity
PPGLLTVKLHEARGLSLPSPYAEPYVVLQALASSFVSSSSVELESGNTASKNRPSVQRSPSTSGPRPLPY
AVLEFDKNEVLIDALGGTVTNPVWNYEATFDVSRPSELTISVYLRNPDALGLGGERDDLNGLVNDMSPSI
QVPEYLSDQWIDLQGGTGEIRVQIDYKPTKNKPL
>gnl|CDD|212166 cd11652, SSH-N, N-terminal domain conserved in slingshot (SSH) phosphatases. This domain or region conserved in Bilateria is found N-terminal to the DEK_C-like and catalytic domains of slingshot phosphatases. Slingshot is a cofilin-specific phosphatase. Dephosphorylation reactivates cofilin, which in turn depolymerizes actin and is thus required for actin filament reorganization. Slingshot is a member of the dual-specificity protein phosphatase family. This N-terminal SSH region may be involved in P-cofilin binding (the model C-terminus plus the DEK_C-like domain, which are characterized as the "B" domain in some of the literature), and may be required for the F-actin mediated activation of slingshot (the N-terminal region of this model, sometimes referred to as the "A" domain)
LVTVQRSPTPSGNSNPDGSDDEEEGDEEQRRKRLQRSESFFAVKGAALILPQGDRTNRPREIASHKHAGE
LQQHLQAMFNLLRPEDTIKLAVRLESVRSNRTRYLVVVSTLGRQDTEESILLGVDFPPKESSCTIGLVLP
IWSDTQVHLDGDGGFSVTSDGKTHIFKPVSVQAMWSALQVLHKACEVAREANYFPGGLALTWVSYYQSRI
SSDQSCLNEWEAMDDLESHRPDS
>gnl|CDD|212167 cd11653, rap1_RCT, C-terminal domain of RAP1 recruits proteins to telomeres. The RAP1 (repressor activator protein 1) C-terminal domain (RCT) mediates interactions with other proteins such as TRF2 (human), Rif1, Rif2, Sir3, Sir4 (Saccharomyces cerevisiae), and Taz1 (Schizosaccharomyces pombe) at telomeres and other loci. RAP1, identified in budding yeast as repressor/activator protein 1, is a well-conserved telomere binding protein, also found in fission yeast and mammals. In Saccharomyces cerevisiae, RAP1 directly binds DNA and is involved in transcriptional activation, gene silencing, as well as binding at numerous sites at each telemore, where it functions in telomere length regulation, telomeric position effect gene silencing and telomere end protection. Human RAP1 apparently does not bind telomeric DNA directly, but binds telomere repeat binding factor 2 (TRF2) via the RCT. RAP1 might act by suppressing nonhomologous end-joining. Yeast RAP1 has two myb-type DNA binding modules, and an RCT domain that recruits Sir proteins 3 and 4 (Sir3, Sir4) for gene silencing, and Rif1 and Rif2 for telomere length maintenance. Schizosaccharomyces pombe RAP1 (spRap1), like human RAP1, lacks direct DNA-binding activity and is localized to telomeres via Taz1, an ortholog of TRF1 and TRF2. The S. pompe RCT resembles the first 3-helix bundle of the yeast and human RCT forms, but is not included in this larger model
SSSYEPEQAEKLVQDLDDEIGIRLVTVTQALLKASGCLSMDPRLALNVLRYLVGIPPDMPGIWTREDDEC
LQSDDPRTIERLIKKHGAENVARRWEFLEM
>gnl|CDD|212553 cd11654, TRF2_RBM, RAP1 binding motif of telomere repeat binding factor. TRF2 (Telomere repeat binding factor 2) functions as part of the 6-component shelterin complex. TRF2 binds DNA and recruits RAP1 (via binding to the RAP1 protein c-terminus (RCT)) and TIN2 in the protection of telomeres from DNA repair machinery. Metazoan shelterin consists of 3 DNA-binding proteins (TRF2, TRF1 and POT1) and 3 recruited proteins that bind to one or more of these DNA-binding proteins (RAP1, TIN2, TPP1). Human TRF1 and TRF2 bind double-stranded DNA. hTRF2 consists of a basic N-terminus, a TRF homology domain, the RAP1 binding motif (RBM) described by this model, the TIN2 binding motif (TBM), and a myb-like DNA binding domain
QPVSTPTTIGISTLKAAFKSLSQAEDSDAAFAKLDQKDLVRP
>gnl|CDD|212554 cd11655, rap1_myb-like, DNA-binding modules of yeast Rap1 and related proteins. Yeast Rap1 DNA-binding activity is mediated by a pair of DNA-binding modules comprised of 2 3-helix bundles with an N-terminal arm, closely matching the structure of homeodomain and myb-type proteins. Human Rap1 has a single myb-like module, and may not bind DNA directly. Rap1, identified in budding yeast as repressor-activator protein 1, is a conserved telomere binding protein, also identified in fission yeast and mammals. In Saccharomyces cerevisiae, Rap1 directly binds DNA and is involved in transcriptional activation, gene silencing, as well as binding at numerous binding sites at each telomere, where it functions in telomere length regulation, telomeric position effect gene silencing and telomere end protection. Human Rap1 apparently does not bind telomeric DNA directly, but binds telomere repeat binding factor 2 (TRF2) via the Rap C-terminal domain (RCT). Rap1 may act by suppressing non-homologous end-joining. Yeast Rap1 has 2 myb-type DNA binding modules, a BRCT domain, and a RCT domain that recruits Sir3 and Sir4 proteins for gene silencing and Rif1 and Rif2 for telomere length maintenance. Human Rap1 has a similar domain architecture but has a single myb-like domain
RTKFTAEDDYILCKYVAKYGRRGRGRLGNSFYKELAEEHPRHTWQSWRDRYRKFLSK
>gnl|CDD|212555 cd11656, FBX4_GTPase_like, C-terminal GTPase-like domain of F-Box Only Protein 4. F-box proteins are involved in substrate recognition as part of SCF (Skp1-Cul1-Rbx1-F-box protein) ubiquitin ligase complexes. Fbx4 (or Fbxo4) binds to the telomere repeat binding factor 1 (TRF1), whose activity at telomeres is regulated in part by selective ubiquitination and degradation. This ubiquitination of TRF1 is mediated by Fbx4, which binds to the TRFH domain of TRF1, via the C-terminal domain characterized by this model, a module resembling a small GTPase domain that lacks the GTP-binding site. When bound to telomeres, TIN2 acts to protect TRF1 from SCF-Fbx4 mediated ubiquitination. Tankyrase-mediated ADP-ribosylation releases TRF1 from telomeres, rendering them susceptible to ubiquitination and degradation, which in turn promotes telomere elongation. Fbx4 has also been reported to target cyclin D1 for degradation by the proteasome, a mechanism ensuring the fidelity of DNA replication. More recently, these findings have been disputed
GAVTSFLQSLIIQNEPRFAMFGPGLEELDTSLVTSLMSSEELLPVAGLPQRQIDGIGSGVSFQLNNQHKF
NILTLYSTTRAERDRAREEDTSAVNKMFSRENEGDDQQGSRYSVIPQVQKVCEVVDGFIYVANAEAHKRH
ERQDEFAQIMAMTDPAFGSTGRPLLVLSCISQADPKRIPCVYMAHELHLNLLPRPWLVQDTEAETLAGLL
DGIAWILEESESK
>gnl|CDD|240667 cd11657, TIN2_N, N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres. TIN2 is one of the six proteins of shelterin complex, which acts to protect telomeres from DNA damage repair machinery. TIN2 binds directly to TRF1 and TRF2 and stabilizes TRF2 complex-telomere binding by tethering it to the TRF1 complex. TIN2 binding to TRF2 is primarily via the TRF binding motif (TBM) region and the N-terminus, while the far C-terminal region has lower affinity. The TIN2 TBM, but not the N-terminal region, is involved in TIN2 binding to TRF1. Truncation of the TIN2 N-terminus in mouse results in telomere elongation, suggesting a negative regulatory function of this region. Three shelterin components (TRF1, TRF2, POT1) bind DNA and 3 components (TIN2, RAP1, TPP1) are recruited by these DNA binding factors. TRF1 activity at telomeres is regulated in part by selective ubiquitination and degradation. Ubiquitination of TRF1 is mediated by Fbx4, which binds TRF1 in the TRFH domain, via a small GTPase module. When bound to telomeres, TIN2 acts to protect TRF1 from SCF-Fbx4 mediated ubiquitination. F-box proteins act in substrate recognition as part of Skp1-Cul1-Rbx1-F- box (SCF) protein complexes. Tankyrase-mediated ADP-ribosylation releases TRF1 from telomeres, rendering them susceptible to ubiquitination and degradation, promoting telomere elongation. TIN2 also binds PIP1, which recruits POT1 to telomeres
VPPLRLVSAAMWQVVQRRDVKHYGKVEEFVSLVTETVPELLTFRQRAKLILGLRARVILELCRNEKAADL
AALNPHLPRLLPPYPNKCQREDALMEEPQLNFLQLVQSLLKDPEEREHFFQEVFPVEYGEEFDQALEKLL
WEFLSRLEKLLPVPDLKQTVSWLSTSPSVLEECLDSVSDPDDLKSLLQ
>gnl|CDD|212556 cd11658, SANT_DMAP1_like, SANT/myb-like domain of Human Dna Methyltransferase 1 Associated Protein 1-like. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins
WTKEETDYLFDLVKRFDLRWNVILDRYPFQKGRSVEDLKEKYYHLC
>gnl|CDD|212557 cd11659, SANT_CDC5_II, SANT/myb-like DNA-binding domain of Cell Division Cycle 5-Like Protein repeat II. In humans, cell division cycle 5-like protein (CDC5) functions in pre-mRNA splicing in cell cycle control. The DNA-binding, myb-like domain of CDC5 is a member of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of DNA-binding Myb domains and is found in a diverse set of proteins
PSIKKTEWTREEDEKLLHLAKLLPTQWRTIAPIVGRTAQQCLERYNKLLDEAQ
>gnl|CDD|212558 cd11660, SANT_TRF, Telomere repeat binding factor-like DNA-binding domains of the SANT/myb-like family. Human telomere repeat binding factors, TRF1 and TRF2, function as part of the 6 component shelterin complex. TRF2 binds DNA and recruits RAP1 (via binding to the RAP1 protein c-terminal (RCT)) and TIN2 in the protection of telomeres from DNA repair machinery. Metazoan shelterin consists of 3 DNA binding proteins (TRF2, TRF1, and POT1) and 3 recruited proteins that bind to one or more of these DNA-binding proteins (RAP1, TIN2, TPP1). Schizosaccharomyces pombe TAZ1 is an orthlog and binds RAP1. Human TRF1 and TRF2 bind double-stranded DNA. hTRF2 consists of a basic N-terminus, a TRF homology domain, the RAP1 binding motif (RBM), the TIN2 binding motif (TBM) and a myb-like DNA binding domain, SANT, named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. Tandem copies of the domain bind telomeric DNA tandem repeats as part of the capping complex. The single myb-like domain of TRF-type proteins is similar to the tandem myb_like domains found in yeast RAP1
RKWTDEEDEALVEGVEKYGVGNWAKILKDYFFVNNRTSVDLKDKWRNLKK
>gnl|CDD|212559 cd11661, SANT_MTA3_like, Myb-Like Dna-Binding Domain of MTA3 and related proteins. Members in this SANT/myb family include domains found in mouse metastasis-associated protein 3 (MTA3) proteins and arginine-glutamic dipeptide (RERE) repeats proteins. SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domains are a diverse set of proteins that share a common 3 alpha-helix bundle. MTA3 has been shown to interact with nucleosome remodeling and deacetylase (NuRD) proteins CHD4 and HDAC1, and the core cohesin complex protein RAD21 in the ovary, and regulate G2/M progression in proliferating granulosa cells. RERE belongs to the atrophin family and has been identified as a nuclear receptor corepressor; altered expression levels of RERE are associated with cancer in humans while mutations of Rere in mice cause failure in closing the anterior neural tube and fusion of the telencephalic and optic vesicles during embryogenesis
EWSESEAKLFEEGLRKYGKDFHDIRQDFLPWKSVGELVEFYYMWKK
>gnl|CDD|212560 cd11662, apollo_TRF2_binding, TRF2-binding region of apollo and similar proteins. Apollo protein, a DNA repair nuclease, is recruited to telomeres by TRF2 where it is associated with the principle components of the shelterin complex. Apollo is a member of the metallo-beta-lactamase family that is required for telomere integrity during S phase; its 5' exonuclease activity is regulated by binding to TRF2. Apollo and TRF2 also suppress damage to engineered interstitial telomere repeat tracts at the chromosome ends. TRF2, which binds preferentially to positively supercoiled DNA substrates, together with Apollo, negatively regulates the amount of DNA topoisomerases (TOP1, TOP2-alpha, and TOP2-beta) at telomeres since they also act in the same pathway of telomere protection. The shelterin complex protein identified in mammals is principally comprised of 6 factors that act to protect telomeres from DNA damage repair machinery. 3 components (TRF1, TRF2, POT1) bind DNA and 3 components are recruited by these factors (TIN2, RAP1, TPP1)
EPRGLALKYLLTPLNFFQSGFSSRRFDQQVEKYH
>gnl|CDD|212128 cd11663, GH119_BcIgtZ-like, putative catalytic domain of glycoside hydrolase family 119 (GH119). The prokaryotic subgroup is represented by IgtZ, an alpha-amylase from a Bacillus circulans strain. The GH119 family is related to GH57, a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). GH57s cleave alpha-glycosidic bonds by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation
SGAPMPHDDLVSYYSHHAKTGAYLTWPWSVAQTLRTNHPQAQMHVTMSGAVVNNVNDLSTLGNVSGYSNT
NWGAPWKNAYNTLKTPAGNRTLDLIHFTGHHSMGPLVGNDYMLKDLIYQNATLAQPYFLGSDFQSSKGFF
PTELGFSERIIPVLEKLGIQWSVIGNNHFSRTLRDYPLLNDPGSDTMVSPPNRADLQNVSTVGSWVSQPM
FNEQQVVRNKYPFASTPHWVRYVDPATGAESRVVGVPVAQAESWEEGYQGQVTADALKPFEGLVPQKQFF
VIAHDGDNSSGRAGSEETWRNAGNVTYADSGVKGMGIDEYLRTNTPAASDVVHVQDGSWIDTRDSSSDPQ
WHHWKLPFGIWKG
>gnl|CDD|212129 cd11664, LamB_YcsF_like_2, uncharacterized proteins similar to the Aspergillus nidulans lactam utilization protein LamB. This bacterial subfamily of the LamB/YbgL family, contains many well conserved uncharacterized proteins. Although their molecular function is unknown, those proteins show high sequence similarity to the Aspergillus nidulans lactam utilization protein LamB, which might be required for conversion of exogenous 2-pyrrolidinone to endogenous GABA
VDLNSDMGEGFGPWTIGDGVDEEIMPLISSANIATGFHAGDPNIMDRTVQLAAEHGVGIGAHPGYRDLVG
FGRRHIAATPEELVNDILYQLGALREFARRHGVSLQHVKPHGALYMHAAKDRDLSELLVSTLQKVAPDLP
LYCMQGSETWRVARELGHPVVREFYADRDYDRSGSIVFTRRARALDPEAVADKVLRACKEGKVRTVEGED
IDIDFDSVCFHSDTPGALSLAAATRAAL
>gnl|CDD|212130 cd11665, LamB_like, Aspergillus nidulans lactam utilization protein LamB and similar proteins. This eukaryotic and bacterial subfamily of the LamB/YbgL family, includes Aspergillus nidulans protein LamB. The lamb gene locates at the lam locus of Aspergillus nidulans, consisting of two divergently transcribed genes, lamA and lamB, needed for the utilization of lactams such as 2-pyrrolidinone. Both genes are under the control of the positive regulatory gene amdR and are subject to carbon and nitrogen metabolite repression. Although the exact molecular function of lamb encoding protein LamB is unknown, it might be required for conversion of exogenous 2-pyrrolidinone to endogenous GABA
VTINCDMGESFGNWKMGDDEELMPHIDVANIACGFHAGDPVVMRKTVRLAKKHGVKVGAHPSLPDLQGFG
RREMALDPEELAACVLYQIGALKGFLDAEGVPLNHIKPHGALYGMAARDEEVARAVADAAKVFGVPVFGL
PGTLHEKVAKELGIPFIPEFYADLDYDPDGKLVITREHKAIDPEEIAERVRRALTDGSVTSVGGKPVGFG
FGVAPFSICIHSDTPNALENAAAVRKAV
>gnl|CDD|212131 cd11666, GH38N_Man2A1, N-terminal catalytic domain of Golgi alpha-mannosidase II and similar proteins; glycoside hydrolase family 38 (GH38). This subfamily is represented by Golgi alpha-mannosidase II (GMII, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A1), a monomeric, membrane-anchored class II alpha-mannosidase existing in the Golgi apparatus of eukaryotes. GMII plays a key role in the N-glycosylation pathway. It catalyzes the hydrolysis of the terminal of both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. GMII is activated by zinc or cobalt ions and is strongly inhibited by swainsonine. Inhibition of GMII provides a route to block cancer-induced changes in cell surface oligosaccharide structures. GMII has a pH optimum of 5.5-6.0, which is intermediate between those of acidic (lysosomal alpha-mannosidase) and neutral (ER/cytosolic alpha-mannosidase) enzymes. GMII is a retaining glycosyl hydrolase of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex; two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst
PLQVFVVPHSHNDPGWLKTFDDYFRDQTQHILNNMVLKLKEDSRRKFIWSEISYFAKWWDIIDGQKKDAV
KRLIENGQLEIVTGGWVMPDEATAHYFALIDQLIEGHQWLERNLGVKPKSGWAVDPFGHSPTMAYLLKRA
GLSNMLIQRVHYSVKKHFSLQKTLEFFWRQNWDLGSSTDILCHMMPFYSYDVPHTCGPDPKICCQFDFKR
LPGGRISCPWRVPPEAIHPGNVQSRAQMLLDQYRKKSKLFRTKVLLAPLGDDFRYTEYTEWDQQFENYQK
LFDYMNSHPELHVKAQFGTLSDYFDALRKSTGMDPVGGQSAFPVLSGDFFTYADRDDHYWSGYF
>gnl|CDD|212132 cd11667, GH38N_Man2A2, N-terminal catalytic domain of Golgi alpha-mannosidase IIx, and similar proteins; glycoside hydrolase family 38 (GH38). This subfamily is represented by human alpha-mannosidase 2x (MX, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A2). MX is enzymatically and functionally very similar to GMII (found in another subfamily), and as an isoenzyme of GMII. It is thought to also function in the N-glycosylation pathway. MX specifically hydrolyzes the same oligosaccharide substrate as does MII. It specifically removes two mannosyl residues from GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine)
PLQVFVVPHSHNDPGWIKTFDKYYYDQTQHILNSMVVKLQEDPRRRFIWSEISFFSKWWDNINAQKRAAV
RRLVGNGQLEMATGGWVMPDEANSHYFAMIDQLIEGHQWLEKNIGVTPRSGWAVDPFGHSSTMPYILRRS
NLTSMLIQRVHYAIKKHFAATQSLEFMWRQTWDPDSSTDIFCHMMPFYSYDVPHTCGPDPKICCQFDFKR
LPGGRINCPWKVPPRAITEANVAERAQLLLDQYRKKSKLYRSKVLLVPLGDDFRYDKPQEWDAQFLNYQR
LFDFLNSHPELHVQAQFGTLSDYFDALYKRTGVVPGMRPPGFPVVSGDFFSYADREDHYWTGYY
>gnl|CDD|212168 cd11669, TTHB210-like, Hypothetical protein TTHB210, a sigma(E)-regulated gene product found in Thermus thermophilus, and similar proteins. TTHB210 is an uncharacterized protein found in Thermus thermophilus, and is controlled by the sigma(E) /anti-sigma(E) regulatory system. It is one of the five proteins of the extracytoplasmic function (ECF) sigma factor sigma(E)-regulated gene products whose physiological function have not been determined. Its crystallographic structure reveals a novel homodecamer although it is a dimer in solution
QAVAGALVALPEFKPSGLGELVARPSLPVRPFVSGDPLGAPVSLGFMFPEKALLGLEGPTAFLDLPLPAK
APTPFDHVDLDWNPHGHPPVGIYDVPHFDFHFYMVSVEEVMKIDP
>gnl|CDD|212561 cd11670, Sp_RAP1_RCT, C-terminal domain of S. pombe RAP1 protein. The Schizosaccharomyces pombe RAP1 (repressor activator protein 1) protein C-terminal (RCT) domain structurally resembles the first 3-helix bundle found in yeast and human RAP1 RCT. S. pombe RAP1 (spRap1), like human RAP1, lacks direct DNA-binding activity and is localized to telomeres via Taz1, an ortholog of TRF1 and TRF2. The RAP1 RCT domain interacts with RAP1 binding motif (RBM) of TAZ1. RAP1, identified in budding yeast as repressor/activator protein 1 is a well-conserved telomere binding protein, found in budding yeast, fission yeast and mammals. In Saccharomyces cerevisiae, RAP1 directly binds DNA and is involved in transcriptional activation and mating type information gene silencing, as well as binding at numerous sites at each telomere, where it functions in telomere length regulation, telomeric position effect gene silencing and telomere end protection. Human RAP1 does not bind telomeric DNA directly, but binds telomere repeat binding factor 2 (TRF2) via the RAP C-terminal domain (RCT). Yeast RAP1 has 2 myb-type DNA binding modules, a BRCT domain, and a RCT domain that recruits Sir3 and Sir4 for gene silencing and Rif1 and Rif2 for telomere length maintenance. S. pombe RAP1 has a BRCT domain, 2 myb like domains, and the RCT
SVEHRESDEAITNILRYTDSTSQQFLEAMESTGGRVTTPRIRIAPLLSKSTS
>gnl|CDD|212562 cd11671, TAZ1_RBM, RAP1 binding motif of Schizosaccharomyces pombe TAZ1. S. pombe TAZ1 recruits the spRAP1 protein to telomeres. The TAZ1 RAP1-binding motif (RBM) binds the RAP1 C-terminal domain (RCT), which structurally resembles the first 3-helix bundle found in yeast and human RAP1 RCT. TAZ1, an ortholog of TRF1 and TRF2, has a TRF homology (TRFH) domain, the RBM domain, a dimerization domain, and a myb-like C-terminus. RAP1, identified in budding yeast as repressor/activator protein 1, is a well-conserved telomere binding protein and is also found in fission yeast and mammals. In Saccharomyces cerevisiae, RAP1 directly binds DNA and is involved in transcriptional activation and mating type information gene silencing, as well as in binding to numerous binding sites at each telomere, where it functions in telomere length regulation, telomeric position effect gene silencing, and telomere end protection. Like S. pombe RAP1, human RAP1 does not bind telomeric DNA directly, but binds telomere repeat binding factor 2 (TRF2) through the RAP C-terminal domain (RCT)
ERTDLSTPGMLYDSDSSKPVFLNQQSLNRLMTRVQRRRAQVVSGSTAQS
>gnl|CDD|277250 cd11672, ADDz, ATRX, Dnmt3 and Dnmt3l PHD-like zinc finger domain (ADDz). The ADDz zinc finger domain is present in the chromatin-associated proteins cytosine-5-methyltransferase 3 (Dnmt3) and ATRX, a SNF2 type transcription factor protein. The Dnmt3 family includes two active DNA methyltransferases, Dnmt3a and -3b, and one regulatory factor Dnmt3l. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The ADDz domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif
IEDICIACGSLVVIYRHPLFQGGICKNCKKYFLSDDISYDDDGYQSYCRICCEGGNLLCCGNNFCHRCFC
KECVDRLVGPGELSTMDENNQWYCYICHP
>gnl|CDD|212563 cd11673, hemoglobin_linker_C, Globular domain of extracellular hemoglobin linker. This family of hemoglobin linker chains is restricted to annelid worms, and participates in the formation of the large erythrocruorin respiratory complex. Via its N-terminal coiled-coil segment (not included in this model), the molecule forms trimers, which are part of a scaffold organizing the overall complex architecture; the latter encompasses 36 linkers and 144 hemoglobins in total. This C-terminal globular domain is involved in trimerization, and also interacts with globins and other C-terminal globular linker domains of neighboring trimers. The structure resembles that of nitrophorins and lipocalins
TAAGSSFSGDLEWDHCTKRRPKHMDIHITSVKRYSFFPSRPKVKATVVIESTKDGDEQTSSLQVKGFYSF
GSRRLILLPPDGLDGLGFVCDFDGGDNDRCKGHIVREASGDVCATFILTR
>gnl|CDD|212564 cd11674, lambda-1, inner capsid protein lambda-1 or VP3. The reovirus inner capsid protein lambda-1 displays nucleoside triphosphate phosphohydrolase (NTPase), RNA-5'-triphosphatase (RTPase), and RNA helicase activity and may play a role in the transcription of the virus genome, the unwinding or reannealing of double-stranded RNA during RNA synthesis. The RTPase activity constitutes the first step in the capping of RNA, resulting in a 5'-diphosphorylated RNA plus-strand. lambda1 is an Orthoreovirus core protein, VP3 is the homologous core protein in Aquareoviruses
AADAAQKQSSIVSSQSGENGKNDIVPSSSVDNDGGIKTQPTSDSIAAVANATKPAAVISPPQSKKATPIN
PSSYVCNVCMAEFSSMDQLAEHQRTTHSIGASSLLTSPAINQAIESFLTSWDDARATSKSVLSVSLVDYL
MSTVAEGPLLITEDSGLCTSFMLVPIVPSATVQKEVIGYTWFMSSYNITTPLPQGAVNRIVCHTNWASKL
DHSRGLEVRLPPPTHSNVHAYRTVLSTGYTPSGQFNPNTLRANVLLMLLQFVLSNLHINKSTAFTLDLTA
ASTGRLIRKFLRRDKLLAVAYPSRVVLPNASKNALFLNTCIADRIGRYDRAQTFSGAVSAWADTYETCDA
LTLYIREMYLLRLRSMHLDPAQIAQAVSRCAQNLLTITAPTAPSPTILCPWRASSEERQLLQVMHLLNVG
NNASAALPIISAAATLLSRVSPLRINPTLLSNAISTIVESTTNTISPAAAILRLLRPMGNDFSAFRRCCA
SWLYNGLVTTYLSEDSFPDSGGSVTSIPTLWDMFICLLALPMTTDPNAPVKAFMVVANLLAGPENIAMDD
PGMTQQTPAAAFNHPTLWPPCFIDPQTIDRRQCPLLYAWATMIHANWPQPSQITYGAPDILGSANLFTPP
NVLLLPWQNQPLPRLTVTPTYDNEMSNWINTVIDFFIRIVNSGRVTATWNDATRRSMTGAMTAFRIVKSM
TPAYIAELLPTELAVLAPVLPVQPFQVPFARLDRNDIITNVNVSRQDPNQRADPALDMSMTQQTIGVPIP
VDARAIVVALLSGQYDTPLIPNVHYAKALAPLFSSDGLFTRNQRAVIASEAYVCARSCIAQCADMGFPVD
RPLDWLRQINLGANEAAEIAKAINDAFKTAFDLDGDLILGPFLEGDPRAAQLSVAYLQYNGDVVREHPEP
GPSMIHEATQMVERTFRHEYNLFGIARGDIILGQTATNSNFNPLAPPASPVFVRGDPGVHVFGRRGTAVF
GMNGLEPMVEDAGGNPRPLDGDWVMPLDLLQVNVAVFRTHLWPRIRSGRTRVRVELGAYPYTLQYYNPRE
QMDGFPLLEQWLSKISPTGIPPVPFLMPIPQDHNVITGRRVHYIWATENNDGSLFSTNAASPATAFGPDV
SIPLERWPALVDPAYRPGTNQLPARIDLYNSLRRYNFEYPPLTAMV
>gnl|CDD|212565 cd11675, SCAB1_middle, middle domain of the stomatal closure-related actin binding protein1. SCAB1 is a dimeric actin crosslinker conserved in plants. The three-dimensional structure of this domain resembles that of fibronectin type III repeat units and immunoglobulins. It is situated between a coiled-coil dimerization domain and a C-terminal pleckstrin homology-like module. SCAB1 appears to be required for normal actin dynamics in guard cells stomatal movement. The function of the middle domain is not clear
LYELDGEERLGSCLRIVPRDDDSPDLSKCSIQWHRIASDGSKKELISGATKPQYAPEPFDVGRLLQADIV
LPGQKESLSTTGPID
>gnl|CDD|212487 cd11676, Gemin6, Gemin 6. Gemins 6, together with the survival motor neuron (SMN) protein, other Gemins, and Unr-interacting protein (UNRIP) form the SMN complex, which plays an important role in the Sm core assembly reaction, by binding directly to the Sm proteins, as well as UsnRNAs. Gemin 6 forms a heterodimer with Gemin 7, which serve as a surrogate for the SmB-SmD3 dimer during the formation of the heptameric Sm ring
PLEWKSYVGKEVKVTASDGKTYTGWVYTVDPVSASVVLVQFLEDEKDKVKVVMGHAVKSVEVV
>gnl|CDD|212488 cd11677, Gemin7, Gemin 7. Gemins 7, together with the survival motor neuron (SMN) protein, other Gemins, and Unr-interacting protein (UNRIP) form the SMN complex, which plays an important role in the Sm core assembly reaction, by binding directly to the Sm proteins, as well as UsnRNAs. Gemin 7 forms a heterodimer with Gemin 6, which serve as a surrogate for the SmB-SmD3 dimer during the formation of the heptameric Sm ring
LEQEARAFLRERFLRSLLALAGKPVEFTMHENTTVTATFKACDIDVENFQVSNLKTPLGIQPEALLRTSD
IISITFD
>gnl|CDD|212489 cd11678, archaeal_LSm, archaeal Like-Sm protein. The archaeal Sm-like (LSm): The Sm proteins are conserved in all three domains of life and are always associated with U-rich RNA sequences. They function to mediate RNA-RNA interactions and RNA biogenesis. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. Eukaryotic Sm proteins form part of specific small nuclear ribonucleoproteins (snRNPs) that are involved in the processing of pre-mRNAs to mature mRNAs, and are a major component of the eukaryotic spliceosome. Most snRNPs consist of seven Sm proteins (B/B', D1, D2, D3, E, F and G) arranged in a ring on a uridine-rich sequence (Sm site), plus a small nuclear RNA (snRNA) (either U1, U2, U5 or U4/6). Since archaebacteria do not have any splicing apparatus, their Sm proteins may play a more general role. Archaeal LSm proteins are likely to represent the ancestral Sm domain. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. Sm-like proteins exist in archaea as well as prokaryotes that form heptameric and hexameric ring structures similar to those found in eukaryotes
PNKKVKSLVGSRIRVEMKGDENQLQGRLVAVDDYMNLHLTDTMECVGEEKVRSLGTVVLRGNNILLIQP
>gnl|CDD|212490 cd11679, archaeal_Sm_like, archaeal Sm-related protein. Archaeal Sm-related proteins: The Sm proteins are conserved in all three domains of life and are always associated with U-rich RNA sequences. They function to mediate RNA-RNA interactions and RNA biogenesis. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. Eukaryotic Sm proteins form part of specific small nuclear ribonucleoproteins (snRNPs) that are involved in the processing of pre-mRNAs to mature mRNAs, and are a major component of the eukaryotic spliceosome. Most snRNPs consist of seven Sm proteins (B/B', D1, D2, D3, E, F and G) arranged in a ring on a uridine-rich sequence (Sm site), plus a small nuclear RNA (snRNA) (either U1, U2, U5 or U4/6). Since archaebacteria do not have any splicing apparatus, their Sm proteins may play a more general role. Archaeal Lsm proteins are likely to represent the ancestral Sm domain
FAAELNSLLDKEVIVTLSNGKTYTGQLVGFDPSSLNIVLTNAKDSSGNKFPKVIINGNRISEILV
>gnl|CDD|212543 cd11680, HDAC_Hos1, Class I histone deacetylases Hos1 and related proteins. Saccharomyces cerevisiae Hos1 is responsible for Smc3 deacetylation. Smc3 is an important player during the establishment of sister chromatid cohesion. Hos1 belongs to the class I histone deacetylases (HDACs). HDACs are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. Other class I HDACs are animal HDAC1, HDAC2, HDAC3, HDAC8, fungal RPD3 and HOS2, plant HDA9, protist, archaeal and bacterial (AcuC) deacetylases. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase
ILSVSEELTKIADLLPSNKGRSSLVHSLIRAYGLLQHFDEIIEPERATRKDLTKYHDKDYVDFLLKKYGL
EDDCPVFPFLSMYVQLVAGSSLALAKHLITQVERDIAINWYGGRHHAQKSRASGFCYVNDIVLAILRLRR
ARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPGFFPGTGSLKNSSDKGMLNIPLKRGLSDKTL
LRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGDPHKEWNLTIRGYGSVIELLLKEFKDKPTLLLGGGGYNH
TEAARAWTYLTSMV
>gnl|CDD|212544 cd11681, HDAC_classIIa, Histone deacetylases, class IIa. Class IIa histone deacetylases are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) to yield deacetylated histones. This subclass includes animal HDAC4, HDAC5, HDAC7, and HDCA9. Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, they have N-terminal regulatory domain with two or three conserved serine residues, phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC9 is involved in regulation of gene expression and dendritic growth in developing cortical neurons. It also plays a role in hematopoiesis. HDAC7 is involved in regulation of myocyte migration and differentiation. HDAC5 is involved in integration of chronic drug (cocaine) addiction and depression with changes in chromatin structure and gene expression. HDAC4 participates in regulation of chondrocyte hypertrophy and skeletogenesis
FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTL
LYGTNPLSRLKLDPTKLAGLPQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELK
NGFAVVRPPGHHAEPSQAMGFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYIS
LHRYDDGNFFPGTGAPTEVGSGAGEGFNVNIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSA
GFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVLALEGGYDLTAICDASEACVRALLGDELDPLS
EEELERRPNPNAVTSLEKVIAIQSPYW
>gnl|CDD|212545 cd11682, HDAC6-dom1, Histone deacetylase 6, domain 1. Histone deacetylases 6 are class IIb Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDACs usually act via association with DNA binding proteins to target specific chromatin regions. HDAC6 is the only histone deacetylase with internal duplication of two catalytic domains which appear to function independently of each other, and also has a C-terminal ubiquitin-binding domain. It is located in the cytoplasm and associates with microtubule motor complex, functioning as the tubulin deacetylase and regulating microtubule-dependent cell motility. Known interaction partners of HDAC6 are alpha tubulin (substrate) and ubiquitin-like modifier FAT10 (also known as Ubiquitin D or UBD)
CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLA
DTYDSVYLHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYA
QQKHGVQRVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVP
WNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKL
ILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGAPCRSALASVSCTISALEPFW
>gnl|CDD|212546 cd11683, HDAC10, Histone deacetylase 10. Histone deacetylases 10 are class IIb Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDACs usually act via association with DNA binding proteins to target specific chromatin regions. HDAC10 has an N-terminal deacetylase domain and a C-terminal pseudo-repeat that shares significant similarity with its catalytic domain. It is located in the nucleus and cytoplasm, and is involved in regulation of melanogenesis. It transcriptionally down-regulates thioredoxin-interacting protein (TXNIP), leading to altered reactive oxygen species (ROS) signaling in human gastric cancer cells. Known interaction partners of HDAC10 are Pax3, KAP1, hsc70 and HDAC3 proteins
WDDPECEIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAIS
GKYDAVYFHPNTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYA
KKKYGLHRILIVDWDVHHGQGIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLP
WNKVGMGNADYLAAFFHVLLPLAFEFDPELVLVSAGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKL
CAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQSALESIQNVRAAQAPYW
>gnl|CDD|212566 cd11684, DHR2_DOCK, Dock Homology Region 2, a GEF domain, of Dedicator of Cytokinesis proteins. DOCK proteins comprise a family of atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate the small GTPases Rac and Cdc42 by exchanging bound GDP for free GTP. They are also called the CZH (CED-5, Dock180, and MBC-zizimin homology) family, after the first family members identified. Dock180 was first isolated as a binding partner for the adaptor protein Crk. The Caenorhabditis elegans protein, Ced-5, is essential for cell migration and phagocytosis, while the Drosophila ortholog, Myoblast city (MBC), is necessary for myoblast fusion and dorsal closure. DOCKs are divided into four classes (A-D) based on sequence similarity and domain architecture: class A includes Dock1 (or Dock180), 2 and 5; class B includes Dock3 and 4; class C includes Dock6, 7, and 8; and class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1, and DHR-2 (also called CZH2 or Docker). This alignment model represents the DHR-2 domain of DOCK proteins, which contains the catalytic GEF activity for Rac and/or Cdc42
ELYIRYLHKLADLHEERGNYVEAALCLLLHADLYAWDLKALVPALAESLSFPEQTSFERKEALYKKAIDL
FDKGKAWEFAIALYKELIPQYENNFDYAKLSEVHRKIAKLYEKIAEKDRLFPTYFRVGFYGKGFPESLRG
KEFIYRGPEFERLGDFCERLKSLYPGAEIIQSSEEPDDEILDSEGQYIQITSVEPYFDDEDLVSRAAPGV
RQFYRNNNINTFVYERPFTKGGKKSQNEITDQWKERTILTTEESFPTILRRSEVVSIEEIELSPIENAIE
DIEKKTEELRSLINKYRSGDSPNVNPLQMLLQGTVDAAVNGGPVAYAEAFLSEEYLSNYPEAEKVKKLKE
AFEEFLEILKRGLALHAKLCPPEMAPLHEELEEGFEKLFKEL
>gnl|CDD|467408 cd11685, UEV_TSG101-like, ubiquitin E2 variant (UEV) domain of TSG101 and related proteins. This subfamily includes the UEV domain of eukaryotic tumor susceptibility gene 101 protein (TSG101, also known as ESCRT-I complex subunit TSG101, vacuolar protein-sorting protein 23, or Vps23) which functions in endocytic trafficking. TSG101 is a component of the ESCRT (endosomal sorting complex required for transport)-I complex, one of four complexes (ESCRT 0, -I, -II, -III) in the vacuolar protein sorting pathway. TSG101 also facilitates HIV-1 virus budding from infected cells, perhaps by linking the p6 domain of the viral structural Gag protein to the vacuolar protein sorting machinery. The UEV domain of TSG101 binds to an essential tetrapeptide motif within the p6 domain of the structural Gag protein and also to ubiquitin. UEVs are homologous to E2 ubiquitin ligases but lack the conserved cysteine residue required for catalytic activity
DRVREDLLNLLQKYPSLKPKTDTFTFNDGSSKLLLCLTGTIPITYRGSTYNIPITIWLPETYPYSPPIVY
VVPTPSMMIIKPHPHVDPNGRVYLPYLSEWNPPSSNLVDLVQELSAVFSEEPPVYS
>gnl|CDD|467409 cd11686, UBCc_UFC1, Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-fold modifier-conjugating enzyme 1 (UFC1) and related proteins. UFC1, also known as Ufm1-conjugating enzyme 1, participates in a ubiquitin-like (UBL) post translation modification enzymatic cascade known as UFMylation, that allows modification by a UBL-type modifier named ubiquitin-fold modifier (UFM1). UBLs are covalently attached to the target proteins or phospholipids through reaction cascades in a manner similar to the ubiquitination pathway. The UFMylation cascade consists of the ubiquitin-like modifier-activating enzyme (UBA5, an E1-like enzyme), UFM1-conjugating enzyme 1 (UFC1, an E2-like enzyme), and the UFM1-specific ligase (UFL1, an E3-like enzyme). UFM1 is synthesized in a precursor form which is then cleaved at the C-terminus to expose a Gly residue. The mature UFM1 is then activated by UBA5, then transferred to UFC1, and finally UFM1 is covalently conjugated with the target protein via UFL1
KKTVAKIPLLTTRAGPRDGDLWIQRLKEEYQALIKYVENNKEADNDWFRIESNKEGTRWFGKCWYIHNLL
KYEFDLEFDIPVTYPTTPPEIALPELDGKTAKMYRGGKICLTVHFKPLWARNVPKFGIAHALALGLGPWL
AAEIPDLVEKG
>gnl|CDD|212582 cd11687, PpPFK_gamma, Pichia pastoris 6-phosphofructokinase, gamma subunit. Pichia pastoris 6-phosphofructokinase (PpPfk) is the most complex and probably largest (1 MDa) eukaryotic Pfk. It forms a dodecamer of four alpha-beta-gamma trimers. The gamma unit is unique, in contrast to other eukaryotic ATP-dependent 6-phosphofructokinases, and participates in oligomerization of the alpha and beta chains. It is not essential for enzymatic activity, but it modulates the allosteric behavior of the enzyme
SIIRDLEKENVGPEFGEFLNTLQTDLNSEKPLIEQVKSQLETHFNLAHETQEFSRKNDNAPVDKLLTNYY
NNYEVNVLEFVLQMGFSKDLSIPLNVWFVLDMISQLSTSKQDLPLDYYLVLNNSQTGKYSDFVRYLIYEA
VGAEIHCFEQGSMPEQYRSSRWEDKVKGPALANRGPIRGNVGAGDRKITFHLLCKKTARMILVGDDRETD
FEMSDRSFVTLLLDYYQRVGTTKKIDLLLLTNNFDTNMNNKLQQLKILESLNMLKSNCYVLDYQITADQV
TANFNSYVEGIPAFRRHEIANFLKKRKTPKNADELIFKYVGRWNICYQKKFHQGNISIHQISGYLD
>gnl|CDD|212583 cd11688, THUMP, THUMP domain, predicted to bind RNA. The THUMP domain is named after THioUridine synthases, RNA Methyltransferases and Pseudo-uridine synthases. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets
VFATTGKGLEEILAAELYELLEVRGFDAEIQVVPHGRVHFKTDTDEAVYQLVMWSRLISRIMPPLGECKA
DLEDLYETALEINEPEMGNEGAKFAVRARRRNKTILNSQEIAMKVGDAIVDAFNPEVDLDNPDIVVNVEV
HKEIASIA
>gnl|CDD|212588 cd11689, SidM_DrrA_GEF, guanine nucleotide-exchange factor domain of Legionella SidM/DrrA. Effector protein DrrA of Legionella pneumophila, an intracellular pathogen, is a potent guanine nucleotide-exchange factor (GEF) specific for the host Rab1 GTPase. It competes with endogenous exchange factors to recruit and activate Rab1 on plasma membrane-derived organelle, therefore effectively hijacking the host's vesicle trafficking to avoid phagosome-lysosome fusion
RVTRIENLENAKKLWDNANSXLEKGNISGYLKAANELHKFXKEKNLKEDDLRPELSDKTISPKGYAILQS
LWGAASDYSRAAATLTESTVEPGLVSAVNKXSAFFXDCKLSPNERATPDPDFKVGKSKILVGIXQFIKDV
ADPTSKIWXHNTKALXNHKIAAIQKLERSNNVNDETLESVLSSKGEN
>gnl|CDD|212589 cd11690, Tsi2_like, Tse2 immunity protein Tsi2 and similar proteins. Tsi2 is an essential protein in Pseudomonas aeruginosa, providing protection from the activity of Tse2, most likely by directly interacting with Tse2. Tse2 is a toxin transported via the type VI secretion system and is targeted towards other bacteria in the environment
NLKPQTLMVAIQCVAAEIRELDAQLQEDDPQNAAELEQLLVGFDLAADDLKNAYEQALGQYSGLPPYDRL
IE
>gnl|CDD|212590 cd11691, HRI1_like, Tandem repeat domain of HRI1 and related proteins. Saccharomyces cerevisiae Hri1p (Hrr25-interacting protein 1, YLR301w) is a non-essential gene product named for its interaction with the yeast protein kinase Hrr25p. It has also been characterized as an interaction partner for Sec72p, but does not seem to be required for protein translocation into the ER. It may be a cytosolic protein. Hri1p contains a tandem repeat of a structural unit that forms a beta-barrel with structural similarity to nitrobindin. The two repeats are sequence dissimilar, and the second (c-terminal) repeat is missing several strands, forming an incomplete barrel
SVVLERVSIRPKEETSGLVVTSPGRWFQGIRILKQPYPSPGEWAIRGTEDSVSGGWKHLIDSGEELDPPP
TAGGFFKLLVGGDVLETGEMEEYGEVWRVLE
>gnl|CDD|212591 cd11692, HRI1_N_like, N-terminal domain of HRI1 and related proteins. Saccharomyces cerevisiae Hri1p (Hrr25-interacting protein 1, YLR301w) is a non-essential gene product named for its interaction with the yeast protein kinase Hrr25p. It has also been characterized as an interaction partner for Sec72p, but does not seem to be required for protein translocation into the ER. It may be a cytosolic protein. Hri1p contains a tandem repeat of a structural unit that forms a beta-barrel with structural similarity to nitrobindin. This N-terminal repeat is involved in homodimerization and may contain a ligand binding site
MSLSKRISIRWGPSEPNEPTSTLVLTSPDGHFVDLRIFKPPYPTDEPSSPFEWAFAGTSISSKVVFSKEG
VSHQDFTHWIDSRVYNPPEADGDIGTFYPLWDSGDRLETGRMVNPETGRVEEYEELWRPLDPTR
>gnl|CDD|212592 cd11693, HRI1_C_like, C-terminal domain of HRI1 and related proteins. Saccharomyces cerevisiae Hri1p (Hrr25-interacting protein 1, YLR301w) is a non-essential gene product named for its interaction with the yeast protein kinase Hrr25p. It has also been characterized as an interaction partner for Sec72p, but does not seem to be required for protein translocation into the ER. It may be a cytosolic protein. Hri1p contains a tandem repeat of a structural unit that forms a beta-barrel with structural similarity to nitrobindin. This C-terminal repeat is missing several strands and forms an incomplete barrel
GRSIVLELEDDKENYEGLVVRVGRWIQGILRDKQNQKGISVIRWEWDSEGGWKRLIEYGEDEDPFPSLEE
NLKVGDTVKVSGGLKWEVVE
>gnl|CDD|212567 cd11694, DHR2_DOCK_D, Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis proteins. DOCK proteins are atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate small GTPases by exchanging bound GDP for free GTP. They are divided into four classes (A-D) based on sequence similarity and domain architecture; class D, also called the Zizimin subfamily, includes Dock9, 10 and 11. Class D Docks are specific GEFs for Cdc42. Dock9 plays important roles in spine formation and dendritic growth. Dock10 and Dock11 are preferentially expressed in lymphocytes. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of class D DOCKs, which contains the catalytic GEF activity for Cdc42. Class D DOCKs also contain a Pleckstrin homology (PH) domain at the N-terminus
ELRKTWLESMARIHEKNGNFSEAAMCYIHIAALVAEYLKRKDLLLELLEACVEGLWKAERYELLGELYKL
IIPIYEKRRDFEQLADCYRTLHRAYEKVVEVMESGKRLLGTYYRVAFYGQAFFEEEDGKEYIYKEPKVTS
LSEISERLLKLYGDKFGSENVKLIQDSGKVNPKDLDPKYAYIQVTHVTPYFDEKELEDRKTEFERNHNIR
RFVFETPFTLSGKARGAVEEQWKRRTILTTSHSFPYVKKRIPVVQREIIELSPIEVAIDEMQSKVKELEE
LISTEPVDMKKLQLRLQGSVSVQVNAGPLAYARAFLEPTTVKNYPDDQVEDLKDVFRDFIKACGQALELN
ERLIKEDQREYHEVLKENYRKMVKEL
>gnl|CDD|212568 cd11695, DHR2_DOCK_C, Dock Homology Region 2, a GEF domain, of Class C Dedicator of Cytokinesis proteins. DOCK proteins are atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate small GTPases by exchanging bound GDP for free GTP. They are divided into four classes (A-D) based on sequence similarity and domain architecture; class C, also called the Zizimin-related (Zir) subfamily, includes Dock6, 7 and 8. Class C DOCKs have been shown to have GEF activity for both Rac and Cdc42. Dock6 regulates neurite outgrowth. Dock7 plays a critical roles in the early stages of axon formation, neuronal polarity, and myelination. Dock8 regulates T and B cell numbers and functions, and plays essential roles in humoral immune responses and the proper formation of B cell immunological synapses. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Class C Docks, which contains the catalytic GEF activity for Rac and Cdc42
SPDLRLTWLQNMAEKHYERKNFAEAAQCLVHAAALGLVGLLEQAAESFSKAGMYEAVNEVYKLLIPILEA
NRDYKKLAEIHGKLQDAFTKIEKQQGGKRMFGTYFRVGFYGSKFGDLDGKEFIYKEPAITKLPEISHRLE
TFYGERFGEERVEVIKDSNPVDTSKLDPDKAYIQITYVEPYFDEYELKERTTYFERNYNLRRFMYATPFT
PDGKAHGELAEQYKRKTILTTENSFPYVKTRLQVVNREEIVLTPIEVAIEDVQKKTRELAAATTQEPPDP
KMLQMVLQGSIGTTVNQGPLEVANVFLSDIPLDPKELDRHQNKLRLCFKEFSKKCYDALEKNKELIGPDQ
KEYQKELERNYENFKEKL
>gnl|CDD|212569 cd11696, DHR2_DOCK_B, Dock Homology Region 2, a GEF domain, of Class B Dedicator of Cytokinesis proteins. DOCK proteins are atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate small GTPases by exchanging bound GDP for free GTP. They are divided into four classes (A-D) based on sequence similarity and domain architecture; class B includes Dock3 and 4. Dock3 is a specific GEF for Rac and it regulates N-cadherin dependent cell-cell adhesion, cell polarity, and neuronal morphology. It promotes axonal growth by stimulating actin polymerization and microtubule assembly. Dock4 activates the Ras family GTPase Rap1, probably indirectly through interaction with Rap regulatory proteins. It plays a role in regulating dendritic growth and branching in hippocampal neurons, where it is highly expressed. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of class B DOCKs, which contains the catalytic GEF activity for Rac and/or Cdc42. Class B DOCKs also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus
EMYLRYIYKLHDLHLQAENYTEAAFTLLLYAELLSWSSDPLPADLHHPSQPEWQRKEALYLKILQYFDRG
KCWEKGIPLCRELAELYESLYDYAKLSHILRMEASFYDNILTQLRPEPEYFRVGFYGKGFPLFLRNKQFV
YRGLDYERIGAFTQRLQSEFPQAHILTKNTPPDDAILQADGQYIQICNVKPVPERRPVLQMVGVPDKVRS
FYRVNDVRKFQYDRPIHKGPIDKDNEFKSLWIERTTLVTEHSLPGILRWFEVVSREVEEIPPVENACETV
ENKNQELRSLISQYQADPTRNINPFSMRLQGVIDAAVNGGIAKYQEAFFTPEFILSHPEDAEHIARLREL
ILEQVQILEAGLALHGKLAPPEVRPLHKRLVERFTQMKQSL
>gnl|CDD|212570 cd11697, DHR2_DOCK_A, Dock Homology Region 2, a GEF domain, of Class A Dedicator of Cytokinesis proteins. DOCK proteins are atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate small GTPases by exchanging bound GDP for free GTP. They are divided into four classes (A-D) based on sequence similarity and domain architecture; class A includes Dock1, 2 and 5. Class A DOCKs are specific GEFs for Rac. Dock1 interacts with the scaffold protein Elmo and the resulting complex functions upstream of Rac in many biological events including phagocytosis of apoptotic cells, cell migration and invasion. Dock2 plays an important role in lymphocyte migration and activation, T-cell differentiation, neutrophil chemotaxis, and type I interferon induction. Dock5 functions upstream of Rac1 to regulate osteoclast function. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of class A DOCKs, which contains the catalytic GEF activity for Rac and/or Cdc42. Class A DOCKs also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus
EMYIRYLYKLCDLHLECDNYTEAAYTLQLHAELLKWSDEPLPTLLRSRRYPEAQTHRQLKEALYYDIIDY
FDKGKMWECAISLCKELAEQYENETFDYLQLSELLKRMATFYDNIMKTLRPEPEYFRVGYYGQGFPSFLR
NKVFIYRGKEYERLSDFSARLLNQFPNAELMNTLTPPGDEIKESPGQYLQINKVDPVMDERPRFKGKPVS
DQILNYYKVNEVQRFTFSRPFRRGTKDPDNEFANMWLERTTLTTAYKLPGILRWFEVVSTSTVEISPLEN
AIETMEDTNKKIRDLILQHQSDPTLPINPLSMLLNGIVDAAVMGGIANYEKAFFTEEYLDEHPEDQELIE
RLKDLIAEQIPLLEAGLKIHKQKAPESLRPLHERMEECFAKMKEHVEEKY
>gnl|CDD|212571 cd11698, DHR2_DOCK9, Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis 9. Dock9, also called Zizimin1, is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates the small GTPase Cdc42 by exchanging bound GDP for free GTP. It plays important roles in spine formation and dendritic growth. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock9, which contains the catalytic GEF activity for Cdc42. Class D DOCKs also contain a Pleckstrin homology (PH) domain at the N-terminus
ELRKTWLDSMARIHVKNGDLSEAAMCYVHVAALVAEYLTRKGMFRQGCTAFRVITPNIDEEASMMEDVGM
QDVHFNEDVLMELLEQCADGLWKAERYELIADIYKLIIPIYEKRRDFERLAHLYDTLHRAYSKVTEVMHS
GKRLLGTYFRVAFFGQGFFEDEDGKEYIYKEPKLTPLSEISQRLLKLYSDKFGSENVKMIQDSGKVNPKD
LDSKYAYIQVTHVTPYFDEKELQERKTDFERSHNIRRFMFEMPFTQSGKRQGGVEEQCKRRTILTAIHCF
PYVKKRIPVMYQHHTDLNPIEVAIDEMSKKVAELRQLCSSAEVDMIKLQLKLQGSVSVQVNAGPLAYARA
FLDDTNTKRYPDNKVKLLKEVFRQFVEACGQALAVNERLIKEDQLEYQEEMKANYREMAKELSEI
>gnl|CDD|212572 cd11699, DHR2_DOCK10, Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis 10. Dock10, also called Zizimin3, is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates the small GTPase Cdc42 by exchanging bound GDP for free GTP. Dock10 is preferentially expressed in lymphocytes and may play a role in interleukin-4 induced activation of B cells. It may also play a role in the invasion of tumor cells. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock10, which contains the catalytic GEF activity for Cdc42. Class D DOCKs also contain a Pleckstrin homology (PH) domain at the N-terminus
PELRRTWLESMAKIHARNGDLSEAAMCYIHIAALIAEYLKRKGYWKMEKICTSSMLPEDSQVYDSNLLLT
TSTGGSMFSMGWPAFLSITPNIKEEGAMKEDSGMQDTPYNENTLVEQLELCVDYLWKSERYELIADVNKP
VIAVFEKQRDFKRLSELYYDIHRSYLKVAEVVNSEKRLFGRYYRVAFYGQGFFEEEEGKEYIYKEPKLTG
LSEISQRLLKLYADKFGADNVKIIQDSNKVNPKELDPKFAYIQVTYVTPYFDEKEQEDRKTDFEMHHNIN
RFVFETPFTLSGKKHGGVEEQCKRRTILTTSHSFPYVKKRIQVVSQTSTELNPIEVAIDEMSKKVSELNQ
LCTMEEVDMIRLQLKLQGSVSVKVNAGPMAYARAFLEETNAKKYPDNQVKLLKEIFRQFAEACGQALDVN
ERLIKEDQLEYQEEMRSHYRDMLSEL
>gnl|CDD|212573 cd11700, DHR2_DOCK11, Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis 11. Dock11, also called Zizimin2 or activated Cdc42-associated GEF (ACG), is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates the small GTPase Cdc42 by exchanging bound GDP for free GTP. Dock11 is predominantly expressed in lymphocytes and is found in high levels in germinal center B lymphocytes after T cell dependent antigen immunization. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock11, which contains the catalytic GEF activity for Cdc42. Class D DOCKs also contain a Pleckstrin homology (PH) domain at the N-terminus
PELRKTWLDSMAKIHVKNGDFSEAAMCYVHVAALVAEFLHRKKLFPSGCAAFKKITPNIDEEGAMKEDIG
MMDVHYSEEVLVELLEQCVDGLWKAERYELISEISKLIIPIYEKRREFEKLTQLYRTLHGAYAKILEVMH
TGKRLLGTFFRVAFYGQGFFEEEDGKEYIYKEPKLTGLSEISHRLLKLYGEKFGSENVKIIQDSNKVNQK
DLDPKYAHIQVTYVKPYFDDKEMAERKTEFERNHNIQRFVFETPYTLSGKKQGGVEEQCKRRTILTTANS
FPYVKKRIPVNGEKQTNLKPIDVATDEIKDKTAELQKLCSNQDVDMIQLQLKLQGCVSVQVNAGPLAYAR
AFLDDSQASKYPNKKVKELKEMFRKFIQACSIALELNERLIKEDQVEYHEGLKSNFRDMVKEL
>gnl|CDD|212574 cd11701, DHR2_DOCK8, Dock Homology Region 2, a GEF domain, of Class C Dedicator of Cytokinesis 8. Dock8, also called Zizimin-related 3 (Zir3), is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates the small GTPases Rac1 and Cdc42 by exchanging bound GDP for free GTP. Dock8 is highly expressed in the immune system and it regulates T and B cell numbers and functions. It plays essential roles in humoral immune responses and the proper formation of B cell immunological synapses. Dock8 deficiency is a primary immune deficiency that results in extreme susceptibility to cutaneous viral infections, elevated IgE levels, and eosinophilia. It was originally described as an autosomal recessive form of hyper IgE syndrome (AR-HIES). DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class C includes Dock6, 7 and 8. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock8, which contains the catalytic GEF activity for Rac and/or Cdc42
TSPDLRLTWLQNMAEKHTKRKCFTEAAMCLVHAAALVAEYLSMLEDHSYLPVGSVSFQNISSNVLEESAV
SDDILSPDEDGVCSGRYFTENGLVGLLEQAAELFSTGGLYETVNEVYKIVIPILEAHRDFRKLASTHDKL
QKAFDNIINKGHKRMFGTYFRVGFYGSKFGDLDEQEFIYKEPAITKLPEISHRLEGFYGQCFGDDVVEVI
KDSTPVDKSKLDPNKAYIQITFVEPYFDDYEMKDRVTYFEKNFNLRRFMYTTPFTLDGRPRGELSEQYKR
KTILTTMHAFPYIKTRINVIQKEEFDLTPIEVAIEDMQKKTRELAEATHQEPPDAKMLQMVLQGSVGATV
NQGPLEVAQVFLAEIPADPKLYRHHNKLRLCFKEFIMRCGEAVEKNKRLITADQREYQQELKKNYNKLRE
NL
>gnl|CDD|212575 cd11702, DHR2_DOCK6, Dock Homology Region 2, a GEF domain, of Class C Dedicator of Cytokinesis 6. Dock6, also called Zizimin-related 1 (Zir1), is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates the small GTPases Rac and Cdc42 by exchanging bound GDP for free GTP. It is widely expressed and shows highest expression in the dorsal root ganglion and the brain. It regulates neurite outgrowth. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class C includes Dock6, 7 and 8. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock6, which contains the catalytic GEF activity for Rac and/or Cdc42
SPDLRLTWLQNMAGKHSERGNHAEAAHCLVHSAALVAEYLSMLEDCRHLPVGCVSFQNISSNVLEESAVS
DDILSPDEEGICSGKYFTELGLVGLLEQAAASFNMGGLYEAVNEVYKILIPIHEANRDYKKLAVVHGKLQ
EAFNKITNQSSGWERMFGTYFRVGFYGCKFGDLDEQEFVYKEPSITKLAEISHRLEEFYTERFGDEVVEI
IKDSNPVDKSKLDPNKAYIQITYVEPFFDTYELKDRVTYFDKNYNLRTFLFCTPFTLDGRAHGELHEQYK
RKTILTTSHAFPYIKTRINVLHREEIVLIPVEVAIEDMQKKTQELAFATHQDPADAKMLQMVLQGCVGTT
VNQGPLEVAQVFLSEIPEDPKLFRHHNKLRLCFKDFTKRCEDALRKNKALIGPDQKEYHRELERNYQRLR
EAL
>gnl|CDD|212576 cd11703, DHR2_DOCK7, Dock Homology Region 2, a GEF domain, of Class C Dedicator of Cytokinesis 7. Dock7, also called Zizimin-related 2 (Zir2), is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates the small GTPases Rac1 and Cdc42 by exchanging bound GDP for free GTP. It plays a critical role in the initial specification of axon formation in hippocampal neurons. It affects neuronal polarity by regulating microtubule dynamics. Dock7 also plays a role in controlling myelination by Schwann cells. It may also play important roles in the function and distribution of dermal and follicular melanocytes. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class C includes Dock6, 7 and 8. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock7, which contains the catalytic GEF activity for Rac and/or Cdc42
DLVFNLHMILSDTVKMKEHQEDPEMLIDLMYRIAKGYQTSPDLRLTWLQNMAGKHSERSNHAEAAQCLVH
SAALVAEYLSMLEDRKYLPVGCVTFQNISSNVLEESAVSDDVVSPDEEGICSGKYFTEAGLVGLLEQAAA
SFSMAGMYEAVNEVYKVLIPIHEANRDAKKLATIHGKLQEAFSKIVHQDGKRMFGTYFRVGFYGTKFGDL
DEQEFVYKEPAITKLAEISHRLEGFYGERFGEDVVEVIKDSNPVDKCKLDPNKAFIQITYVEPYFDTYEM
KDRITYFDKNYNLRRFMYCTPFTLDGRAHGELHEQFKRKTILTTSHAFPYIKTRINVIHKEEIILTPIEV
AIEDMQKKTQELAFATHQDPADPKMLQMVLQGSVGTTVNQGPLEVAQVFLSEIPSDPKLFRHHNKLRLCF
KDFTKRCEDALRKNKSLIGPDQKEYQRELERNYHRLKEALQPLINRKIPQLYK
>gnl|CDD|212577 cd11704, DHR2_DOCK3, Dock Homology Region 2, a GEF domain, of Class B Dedicator of Cytokinesis 3. Dock3, also called modifier of cell adhesion (MOCA), is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates small GTPases by exchanging bound GDP for free GTP. Dock3 is a specific GEF for Rac. It regulates N-cadherin dependent cell-cell adhesion, cell polarity, and neuronal morphology. It promotes axonal growth by stimulating actin polymerization and microtubule assembly. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class B includes Dock3 and 4. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock3, which contains the catalytic GEF activity for Rac and/or Cdc42. Class B DOCKs also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus
EMYIRYIHKLCDMHLQAENYTEAAFTLLLYCELLQWEDRPLREFLHYPSQSEWQRKEGLCRKIIHYFNKG
KSWEFGIPLCRELAFQYESLYDYQSLSWIRKMEAAYYDNIMEQQRLEPEFFRVGFYGRKFPFFLRNKEYV
CRGHDYERLEAFQQRMLSEFPQAIAMQHPNHPDDGILQCDAQYLQIYAVTPIPDNMDVLQMDRVPDRIKS
FYRVNNVRKFRYDRPFHKGPKDKENEFKSLWIERTTLTLTHSLPGISRWFEVERRELVEVSPLENAIQVV
ENKNQELRTLISQYQHKQLHGNINLLSMCLNGVIDAAVNGGIARYQEAFFDKDYISKHPGDAEKITQLKE
LMQEQVHVLGVGLAVHEKFVHPEMRPLHKKLIDQFQMMRSSL
>gnl|CDD|212578 cd11705, DHR2_DOCK4, Dock Homology Region 2, a GEF domain, of Class B Dedicator of Cytokinesis 4. Dock4 is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates small GTPases by exchanging bound GDP for free GTP. It plays a role in regulating dendritic growth and branching in hippocampal neurons, where it is highly expressed. It may also regulate spine morphology and synapse formation. Dock4 activates the Ras family GTPase Rap1, probably indirectly through interaction with Rap regulatory proteins. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class B includes Dock3 and 4. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock4, which contains the catalytic GEF activity for Rac and/or Cdc42. Class B DOCKs also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus
EMYIRYIHKLYDLHLKAQNFTEAAYTLLLYDELLEWSDRPLREFLSYPMQTEWQRKEYLHLTIIQNFDRG
KCWENGIILCRKLAEQYESYYDYRNLSKMRMMEASLYDKIMDQQRLEPEFFRVGFYGKKFPFFLRNKEFV
CRGHDYERLEAFQQRMLNEFPHAIAMQHANQPDETIFQAEAQYLQIYAVTPIPESQEVLQRDGVPDNIKS
FYKVNHIWRFRYDRPFHKGTKDKENEFKSLWVERTTLTLVQSLPGISRWFEVEKREVVEMSPLENAIEVL
ENKNQQLRTLISQCQTRQMQNINPLTMCLNGVIDAAVNGGVSRYQEAFFVKEYILNHPEDGDKITRLREL
MLEQAQILEFGLAVHEKFVPQDMRPLHKKLVDQFFVMKSSL
>gnl|CDD|212579 cd11706, DHR2_DOCK2, Dock Homology Region 2, a GEF domain, of Class A Dedicator of Cytokinesis 2. Dock2 is a hematopoietic cell-specific, class A DOCK and is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates small GTPases by exchanging bound GDP for free GTP. It plays an important role in lymphocyte migration and activation, T-cell differentiation, neutrophil chemotaxis, and type I interferon induction. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class A includes Dock1, 2 and 5. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock2, which contains the catalytic GEF activity for Rac and/or Cdc42. Class A DOCKs, like Dock2, are specific GEFs for Rac and they contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus
RMSCTVNLLNFYKDINREAMYIRYLYKLRDLHLDCENYTEAAYTLLLHTRLLKWSDEQCASQVMQTGQQH
PQTQRQLKETLYETIIGYFDKGKMWEEAISLCKELAEQYEMEIFDYELLSQNLIQQAKFYESIMKILRPK
PDYFAVGYYGQGFPSFLRNKVFIYRGKEYERREDFQMQLMSQFPNAEKLNTTSAPGDDIKNSPGQYIQCF
TVQPVLEEHPRLKNKPVPDQIINFYKSNYVQRFHYSRPVRKGPVDPENEFASMWIERTTFVTAYKLPGIL
RWFEVTHMSQTTISPLENAIETMSTTNEKILMMINQYQSDESLPINPLSMLLNGIVDPAVMGGFAKYEKA
FFTEEYVRDHPEDQDKLTRLKDLIAWQIPLLGAGIKIHGKRVTDDLRPFHERMEECFKQLKMKVEKEYGV
R
>gnl|CDD|212580 cd11707, DHR2_DOCK1, Dock Homology Region 2, a GEF domain, of Class A Dedicator of Cytokinesis 1. Dock1, also called Dock180, is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates small GTPases by exchanging bound GDP for free GTP. Dock1 interacts with the scaffold protein Elmo and the resulting complex functions upstream of Rac in many biological events including phagocytosis of apoptotic cells, cell migration and invasion. In the nervous system, it mediates attractive responses to netrin-1 and thus, plays a role in axon outgrowth and pathfinding. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class A includes Dock1, 2 and 5. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock1, which contains the catalytic GEF activity for Rac and/or Cdc42. Class A DOCKs, like Dock1, are specific GEFs for Rac and they contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus
EMYIRYLYKLCDLHKECDNYTEAAYTLLLHAKLLKWSEEACAAHLTQRDGYQATTQGQLKDQLYQEIIHY
FDKGKMWEEAIALGKELAEQYENEMFDYEQLSELLKKQAQFYENIVKVIRPKPDYFAVGYYGQGFPTFLR
NKMFIYRGKEYERREDFEARLLTQFPNAEKMKTTSPPGDDIKNSSGQYIQCFTVKPLLELPPKFQNKPVS
EQIVSFYRVNEVQRFQYSRPVRKGEKDPDNEFANMWIERTTYVTAYKLPGILRWFEVKSVFMVEISPLEN
AIETMQLTNEKINNMVQQHLNDPNLPINPLSMLLNGIVDPAVMGGFANYEKAFFTEKYMQEHPEDHEKIE
KLKDLIAWQIPFLAEGIRIHGEKVTEALRPFHERMEACFRQLKEKVEKQY
>gnl|CDD|212581 cd11708, DHR2_DOCK5, Dock Homology Region 2, a GEF domain, of Class A Dedicator of Cytokinesis 5. Dock5 is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates small GTPases by exchanging bound GDP for free GTP. It functions upstream of Rac1 to regulate osteoclast function. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class A includes Dock1, 2 and 5. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock5, which contains the catalytic GEF activity for Rac and/or Cdc42. Class A DOCKs, like Dock5, are specific GEFs for Rac and they contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus
DIYIRYLYKLRDLHLDCENYTEAAYTLLLHAELLQWSEKPCVPHLLQRDSYYVYTQQELKERLYQEIISF
FDKGKMWEKAIELSKELADMYENQVFDYEGLGNLLKKQAQFYENIMKAMRPQPEYFAVGYYGQGFPSFLR
NKIFIYRGKEYERLEDFSLKLLTQFPNAEKMTSTSPPGDEIKSSTKQYVQCFTVKPVMNLPSHYKDKPVP
EQILNYYRANEVQQFQYSRPFRKGEKDPDNEFATMWIERTTFTTAYRFPGILKWFEVKQISTEEISPLEN
AIETMELTNEKISNLVQQHAWDRSLPVHPLSMLLNGIVDPAVMGGFSNYEKAFFTEKYLQEHPEDQEKIE
LLKQLIALQMPLLAEGIRIHGEKLTEQLKPLHERLVSCFKDLRAKVEKLY
>gnl|CDD|293931 cd11709, SPRY, SPRY domain. SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome
GKWYWEVRVDSGNGGLIQVGWATKSFSLDGEGGVGDDEESWGYDGSRLRKGHGGSSGPGGRPWKSGDVVG
CLLDLDEGTLSFSLNGKDLGVAFTNLFLKGGGLYPAVSLGSGQGVTIN
>gnl|CDD|212548 cd11710, GINS_A_psf1, Alpha-helical domain of GINS complex protein Psf1. Psf1 is a component of the GINS tetrameric protein complex. Psf1 is mainly expressed in highly proliferative tissues, such as blastocysts, adult bone marrow, and testis, in which the stem cell system is active. Loss of Psf1 causes embryonic lethality. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3
GDKANKLVKELKRSENDTLPPYNEDLVRQVLEEIRDLYEENQALLEEAQEEEEDPGLIPGLLVRHLSILR
NKRCLLAYLYERLDRIRELRWENGSVLPEDIKENLSPAEKEYFKQYSKLLAEYMSSLGD
>gnl|CDD|212549 cd11711, GINS_A_Sld5, Alpha-helical domain of GINS complex protein Sld5. Sld5 is a component of GINS tetrameric protein complex, and within the complex Sld5 interacts with Psf1 via its N-terminal A-domain, and with Psf2 through a combination of the A and B domains. Sld5 in Drosophila is required for normal cell cycle progression and the maintenance of genomic integrity. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3
DLELLKRAWVNEKFAPELLPYQEELVERVLEQIEQQEENLEELKASEKDDLRLSLHEMELERIRFLLRSY
LRTRLQKIEKYALHILSEEELPSRLSPEELEFAKRYAELLENHLKSSVL
>gnl|CDD|212550 cd11712, GINS_A_psf2, Alpha-helical domain of GINS complex protein Psf2 (partner of Sld5 2). Psf2 is a component of GINS tetrameric protein complex and has been found to play important roles in normal eye development in Xenopus laevis. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3
RNKCRIVPPDWLTVEYLKEILEEEKKSETFSPLPFHYLEIAKLLLEVASDDIPDADEIRSLVEDIRDVRQ
AKLRSGLEKLLGSGEVHAKLDNLTAMEINEIRPFLSGALDKLRKLRASA
>gnl|CDD|212551 cd11713, GINS_A_psf3, Alpha-helical domain of GINS complex protein Psf3 (partner of Sld5 3). Psf3 is a component of GINS, a tetrameric protein complex. Psf3 expression is up regulated in malignant colon cancer and it might be involved in cancer cell proliferation. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3
FVSVELPKIYSEKVRNALKADPTSVDLHKLSPYFYELGLKLLSLFPEDEELAEVLLETFKERFREIMDHA
QNASNEDNSEFLRKLDELERKLFRAGQESLKDFKKWLKG
>gnl|CDD|212552 cd11714, GINS_A_archaea, Alpha-helical domain of archaeal GINS complex proteins. The GINS complex is involved in replication of archaeal and eukayotic genomes. The archaeal DNA replication system is a simplified version of that of the eukaryotes. Like its eukaryotic counterpart, the archaeal GINS complex is tetrameric, but instead of four different subunits (Sld5, Psf1, Psf2 and Psf3) it consists of two different proteins named Gins51 and Gins23. All GINS subunits are homologs and they can be classified into two groups. One group (the eukayotic Sld5 and Psf1, as well as the archaeal Gins51) has the alpha-helical (A) domain at the N-terminus and the beta-strand domain (B) at the C-terminus (this arrangement is called ABtype). The arrangement of the A and B domains is reversed in the second group (eukaryotic Psf2 and Psf3 and archaeal Gins23, also referred to as BAtype). The overall fold of each archaeal subunit and the overall tetrameric assembly of GINS are similar, but the relative locations of the C-terminal small domains are different with respect to the alpha helical domain characterized by this model, resulting in different subunit contacts in the archaeal GINS complex.Some archaea may have a homotetrameric GINS complex (4 copies of an AB-type module)
IEELRKILFKERKSASLQKLPEDFYERAKEYIKELEEEARKSPEAQELLDELEKAKSTLRELFRLRLRKI
VKLALLSAEDREELENLTPEEKELYDSLKEIIEEW
>gnl|CDD|212584 cd11715, THUMP_AdoMetMT, THUMP domain associated with S-adenosylmethionine-dependent methyltransferases. Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets
FFATCPPGLEELLAAELKALGAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLY
ELAKAIDWEDYLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREKGKRPSVDLDNPDVRIRVHLS
KDRATLSLDLSG
>gnl|CDD|212585 cd11716, THUMP_ThiI, THUMP domain of thiamine biosynthesis protein ThiI. ThiI is an enzyme responsible for the formation of the modified base S(4)U (4-thiouridine) found at position 8 in some prokaryotic tRNAs. This modification acts as a signal for UV exposure, triggering a response that provides protection against its damaging effects. ThiI consists of an N-terminal THUMP domain, followed by an NFLD domain, and a C-terminal PP-loop pyrophosphatase domain. The N-terminal THUMP domain has been implicated in the recognition of the acceptor-stem region. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets
KILVRYGEIALKGKNRKRFEKRLVKNIRRALKDLPDVKVEREWGRIYVELNGEDLEEVIERLKKVFGIVS
FSPAVEVEKDLEDIKEAALELLKEELKKGKTFKVRAKRADKSFPFTSMEINREVGAALLENTPDLKVDLK
NPDVTIRVEIREDGAYVYTERIPGPG
>gnl|CDD|212586 cd11717, THUMP_THUMPD1_like, THUMP domain-containing protein 1-like. This family contains THUMP domain-only proteins including THUMP domain-containing protein 1 and Saccharomyces cerevisiae Tan1. Tan1 is non essential and has been shown to be required for the formation of the modified nucleoside N(4)-acetylcytidine (ac(4)C) in tRNA. To date, there is no functional information available about THUMPD1. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets
GILVTCNRGKERKAIRELYNLLQSVETGVKNVVFIKTRPPVDPVELVEKIFEDAASTKKKRTRFIQRLIP
IDVTCKASLEEIEKLAKELLKKHFPTAEPPKTFAVECKSRNNNKLSRDEVIKAVAELVPEIHKVDLKNPD
KVILVEVIKNVCGISVVK
>gnl|CDD|212587 cd11718, THUMP_SPOUT, THUMP domain associated with SPOUT RNA Methylases. Members of this archaeal protein family are characterized by containing an N-terminal THUMP domain and a C-terminal SPOUT RNA methyltransferase domain. No functional information is available The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets
ILVKTQLGMERIAASYIKEIDPDAKVEPAPMGFLGLVLVESDEDKKDELALRVPEVERVIPVDAEVKADL
DEIVRVAEEIAKHISEGETFAVRTTRRGKHDFTSIDVNVVLGAAVKELTGAEVDLNNPDKVVYVEIIGDR
AYISI
>gnl|CDD|212593 cd11719, FANC, Fanconi anemia ID complex proteins FANCI and FANCD2. The Fanconi anemia ID complex consists of two subunits, Fanconi anemia I and Fanconi anemia D2 (FANCI-FANCD2) and plays a central role in the repair of DNA interstrand cross-links (ICLs). The complex is activated via DNA damage-induced phosphorylation by ATR (ataxia telangiectasia and Rad3-related) and monoubiquitination by the FA core complex ubiquitin ligase, and it binds to DNA at the ICL site, recognizing branched DNA structures. Defects in the complex cause Fanconi anemia, a cancer predisposition syndrome
RAVGTLLRAVLKGSPCSEEDGALRRYKIYSCCIQLVESGDLQQDVASEIIGLLMLEVHHFPGPLLVDLAS
DFVGAVREDRLVNGKSLELLPIILTALATKKEVLACGKGDLNGEEYKRQLIDTLCSVRWPQRYMIQLTSV
FKDVCLTPEEMNLVVAKVLTMFSKLNLQEIPPLVYQLLVLSSKGSRRSVLDGIIAFFRELDKQHREEQSS
DELSELITAPADELYHVEGTVILHIVFAIKLDCELGRELLKHLKAGQQGDPSKCLCPFSIALLLSLTRIQ
RFEEQVFDLLKTSVVKSFKDLQLLQGSKFLQTLVPQRTCVSTMILEVVRNSVHSWDHVTQGLIEFGFILM
DSYGPKKILDGKAVEIGTSLSKMTNQHACKLGANILLETFKIHEMIRQEILEQVLNRVVTRTSSPINHFL
DLFSDIIMYAPLILQNCSKVTETFDYLTFLPLQTVQGLLKAVQPLLKISMSMRDSLILVLRKAMFASQLD
ARKSAVAGFLLLLKNFKVLGSLPSSQCTQSIGVTQVRVDVHSRYSAVANETFCLEIIDSLKRSLGQQADI
RLMLYDGFYDVLRRNSQLASSIMQTLFSQLKQFYEPEPDLLPPLKLGACVLTQGSQIFLQEPLDHLLSCI
QHCLAWYACLIMGVCEVLMEYNFSISNFSKSKFEEILSLFTCYKKFSDIIFQNLCDITRVLLWRYTSIPT
SVEESGKKEKGKSISLLCLEGLQKTFSVVLQFYQPKVQQFLQALDVMGTEEEEAGVTVTQRASFQIRQFQ
RSLLNLLSSEEDDFNSKEALLLIAVLSTLSRLLEPTSPQFVQMLSWTSKICKEYSQEDASFCKSLMNLFF
SLHVLYKSPVTLLRDLSQDIHGQLGDIDQDVEIEKTDHFAVVNLRTAAPTVCLLVLSQAEKVMQLGTLVT
FFHELVQTALPSGSCVDTLLKGLSKIYSTLTAFVKYYLQVCQSSRGIPNTVEKLVKLSGSHLTPVCY
>gnl|CDD|212594 cd11720, FANCI, Fanconi anemia I protein. The Fanconi anemia ID complex consists of two subunits, Fanconi anemia I and Fanconi anemia D2 (FANCI-FANCD2) and plays a central role in the repair of DNA interstrand cross-links (ICLs). The complex is activated via DNA damage-induced phosphorylation by ATR (ataxia telangiectasia and Rad3-related) and monoubiquitination by the FA core complex ubiquitin ligase, and it binds to DNA at the ICL site, recognizing branched DNA structures. Defects in the complex cause Fanconi anemia, a cancer predisposition syndrome. The phosphorylation of FANCI may function as a molecular switch to turn on the FA pathway
EDTIKLLRAILLGLSCSPDSASKRLKVVKSVINLLNSAELSTKVAFDIISRLLLELPKLPGEQLVELVEL
CVDGIRNGDNSNGSWKDLLPTILSALSEEKEILYEGGELTGAEYKSQIINSICSSKWQPNILTSLTSMFR
DLSLSKEELNFVVEKLCRALKELDLQELPPLVYQLLVLCSKGDKLLVLEGLQKYFDKLYYKRLLSDANSS
STEDDEIETSSPKEVREAEGTVLLHINFAAKQDHELGKEFLKLLKSVQRVPEKALTPFSLSVLLSMSRIN
RFEEQVFDFLKTAIVRSFKEKELQQNSAWLRELLLPQVKDVEKILLRVVKNSVSGRDHVTPGLVNLGFIL
LESYGPKASLESGSKTPAPKAWQLGIKILLKIFKKHEIARSEILEQLKNRIVTLPSPVSQYIDCLSYLVQ
SAPLLMLEHVSKITELLDYLTFIPGSSAMRLLKAIQPLLKISRSLRDSLILVLRKALFSRETETRQMAVT
GFLLLLKNLKLLSSLGSSQSSSASSSTQASIDVHSQYSSSESNESLCLEILGLLRRCLTQQAEVRLMLYE
GLYRVVLRNPELAPHVLDLLLPHFKSFFEEDEDVLLPLKLESCVTTQGDDIVLQEPLGHLIFCIQHCLLL
SKQNNSGRPDAAAALLEESLMLESICKRMIKVELEDFELDKSADFSVNSSVGQKKLLNALLLLGIYEVLI
EYIFNIWNKVSKNACKEILGLFKLYESLLDLVSKLLTLLFDTSVQYATEDQTSLLRSNREFMRYILSVCL
QKLQSLKNTPDYDGGQHSKRIFQNLCDITKVLYLRKISKLTELKKDFGKQIALLALECFLEILNVVLQLY
PSKLEDFLSVIDVEDGGGEKSTIDEQLHFQIRHFIRSLMKLLSTEEEEDFVSKEVVILIEILSVLSDKLP
PNSTQAKQMLTWLLKICKENELEDSSVAKAVLTLLLSLHVRTQEYLELLDEVAQELCAVLGDIDEDEETE
SHKLKIINETTAESVLTLLLASLDKVLDDVDWLIKRLKAELNVDQLPGEDSEQSQGNLKSIERSICEQLY
HIATVLTELVNTAIPPGSCADALLKLLIKLYKTLSNLTKHFIARSTKNPVFPSAKFEKLVELAGKQLTPN
IYNFITYVEENQSEQDSKKKKKKAKSKVQRNKILRETKLIPKLIYAIEQFEKFLIQLSKKTKVNLMRYMK
LSTTRDFRIKDS
>gnl|CDD|212595 cd11721, FANCD2, Fanconi anemia D2 protein. The Fanconi anemia ID complex consists of two subunits, Fanconi anemia I and Fanconi anemia D2 (FANCI-FANCD2) and plays a central role in the repair of DNA interstrand cross-links (ICLs). The complex is activated via DNA damage-induced phosphorylation by ATR (ataxia telangiectasia and Rad3-related) and monoubiquitination by the FA core complex ubiquitin ligase, and it binds to DNA at the ICL site, recognizing branched DNA structures. Defects in the complex cause Fanconi anemia, a cancer predisposition syndrome. The phosphorylation of FANCD2 is required for DNA damage-induced intra-S phase checkpoint and for cellular resistance to DNA crosslinking agents
PENVDEFLSGLEDFLADRDRLRKALLPCNLLTTESSSASSVPQDSLIRLLLQVDPLQPKVIELLLEKLPE
FLDEDASVPSEDNLPRLILNQFKWLDHIVDSEDLTEKLLELLSVAPSELQKEIITSLPEIIGDSQHEDVA
EELCKLLQENSELTVPILDALSNLNLSPELLSEIREKVLSCLKTVPLEDLPVLVKFLLQSITATEALEII
SKLRKNLDFSPLSDPSSSGSSDKSKASANSCQSLILEAIKSALRFSKLLAEAWIKVISSIDAPQDHKVID
LILLLILYSTNEDKRKSIESLLKKKIKSGFIRTSLLDLAFTGHSQVLKDYFKSLLSLADNLLRSAEPVVR
EFGSHLYKLLFKHFDRYYQQEVVGALITHIGSGNSSEVDAALDVLRELAEKNPDELLPYATFIKGILDYL
DSLNLKQIRQLFDILCHLAFSERPLSEGSSIQDDLHIIVRKQLSNSSPKYKRMGIIGAVTLVKHLASANS
SDDAVERSSSNGSSLPDERLKQAANLLELVLSSCKNSPEALALFYDELANIISQASNLDPKFLEWLGETI
TEDFQESFVVDLDETSSAILASLFRLLRLLERSQQGGSLDEIDALLGCPLVLPDFEVDEKFDSLSTEQRS
VVLDCLFYAINWFREVINAFATQKDASTKKKVLKRLRNLIELEGRLSKLLAHCYFRELDLEVFSLLKSGL
VTDTSLELSEEEGVHLGPKELRFLLEDLNRKLEHVLTSPKKKRMPLLKPLKKGQGFSSLSQKSPKEVLKA
LVPLLPHLCKHLEKIHNYLQNLLLSNAGQLDAPGPFVQENQYAKSCYGLLLQCLRLLFAWPGFSSQSNRV
LLKSALRAIASRLKESTGKDLPLKELVSSLFKYLKSFEPSVPSLSTAVSLVQLLQALMEKSPDRPQLREK
LADLARNFLCRQWPDLSGESEKGQKYNDLIDTLLRIYLEHSDDPLKKLEEIAGEALPELLEKKKDKDALE
TFPTLSKSTFPIFFRVLMEALIESVKKILSSAADTGGGEMERLLLWQSAVRVFKALVNLVKTFDKRPVLA
ICLKYGRLFLKLFLKLGMPLLEKLFKNHKEEVQELLKTLQQSTRYLHHICCHSKIHKDTALTNHVPALKK
SLETLVYRVKAMLVANNCSEAFWMGNLKNKDLQGEEILSQR
>gnl|CDD|212596 cd11722, SOAR, STIM1 Orai1-activating region. STIM1 (stromal interaction module 1) is a metazoan transmembrane protein located in the endoplasmic reticulum (ER) membrane, which functions as a sensor for ER calcium ion levels and activates store-operated Ca2+ influx channels (SOCs), such as the Orai1 Ca2+ channel located in the plasma membrane. STIM1 has an N-terminal Ca-binding EF-hand domain, which is located in the ER lumen. Responding to the release of Ca2+ from the ER, STIM1 was found to aggregate near the plasma membrane and contact Orai1. This model describes a region near the C-terminus of STIM1, which has been shown to mediate the interaction with Orai1 and has been labeled SOAR (STIM1 Orai1-activating region). STIM1 has also been linked to sensing oxidative and temperature-variation stress and may play a rather general role in mediating calcium signaling in response to stress. Dimerization of STIM1 via the SOAR domain appears required for the activation of the Orai1 calcium channel. A model for STIM1 activation has been proposed, in which an inhibitory helix N-terminal to the SOAR domain prevents STIM1 clustering or aggregation, and in which conformational changes triggered by depletion of the calcium stores allow the clustering and activation of Orai1
LQQLLQLTYELEMQYYNKKKQDAEKQLQEAKEACEKLRKKRSSVFGSFRLAHSSSLDDVDNRILSAKQAL
EEVTRELQERQHRWSQIESLCG
>gnl|CDD|381177 cd11723, YabN_N_like, N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains. This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known
ITIVGLGPGDPDLLTLGALEALKSADKVYLRTARHPVVEELKEEGIEFESFDDLYEEAEDFEEVYEAIAE
RLLEAAEHGDVVYAVPGHPLVAERTVQLLLERAEEGIEVEIIPGVSFLDAALAALGIDPIEGLQILDALD
LDAEDLDPRLPLLITQVYNRLVASDVKLTLMEVYPDEHEVTVVRAAGLGDEKVEEVPLYELDRQEDIDHL
TSLYVPPL
>gnl|CDD|381178 cd11724, TP_methylase, uncharacterized family of the tetrapyrrole methylase superfamily. Members of this superfamily use S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and Ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide
KLYLVGVGPGDPDLITLRALKAIKKADVVFAPPDLRKRFAEYLAGKEVLDDPHGLFTYYGKKCSPLEEAE
KECEELEKQRAEIVQKIREALAQGKNVALLDSGDPTIYGPWIWYLEEFADLNPEVIPGVSSFNAANAALK
RSLTGGGDSRSVILTAPFALKENEDLLEDLAATGDTLVIFMMRLDLDELVEKLKKHYPPDTPVAIVYHAG
YSEKEKVIRGTLDDILEKLGGEKEPFLGLIYVG
>gnl|CDD|277251 cd11725, ADDz_Dnmt3, ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3). Dnmt3 is a de novo DNA methyltransferase family that includes two active enzymes Dnmt3a and -3b and one regulatory factor Dnmt3l. The ADDz domain of Dnmt3 is located in the C-terminal region of Dnmt3, which is an active catalytic domain in Dnmt3a and -b, but lacks some residues for enzymatic activity in Dnmt3l. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The ADDz_Dnmt3 domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif
IEDICLACGSLEVSETSDHPFFEGGLCKNCKERFLECIFLFDDDGYQMYCTICGGGGEVVLCDNPDCTRV
YCTECLDLLLGPGAVAKILESDPWFCFLCSPESNSLLG
>gnl|CDD|277252 cd11726, ADDz_ATRX, ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked). ADDz_ATRX is a PHD-like zinc finger domain of ATRX, which belongs to the SNF2 family of chromatin remodeling proteins. ATRX is a large chromatin-associated nuclear protein with two domains, ADDz_ATRX at the N-terminus, followed by a C-terminal ATPase/helicase domain. The ADDz_ATRX domain recognizes a specific methylated histone, and this interaction is required for heterochromatin localization of the ATRX protein. Missense mutations in either of the two ATRX domains lead to the X-linked alpha-thalassemia and mental retardation syndrome; however the mutations in the ADDz_ATRX domain produce a more severe disease phenotype that may also relate to disturbing unknown functions or interaction sites of this domain. The ADDz domain is also present in chromatin-associated proteins cytosine-5-methyltransferase 3 (Dnmt3); it is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif
RRVRCTACGEQLNHFSKEVHRHPVLKVLICKSCLKFYNSGEFSKDEDGSDEYCRWCGQGGDLICCDFCPN
VFCKKCIKRNLGRAELSRIEESDKWKCFVCDP
>gnl|CDD|277253 cd11727, ADDz_Dnmt3l, ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 like (Dnmt3l). Dnmt3l is a regulator of DNA methylation, which acts by recognizing unmethylated histone H3 tails and interacting with Dnmt3a to stimulate its de novo DNA methylation activity. The ADDz_Dnmt3l domain is located in the C-terminal region of Dnmt3l that otherwise lacks some residues required for DNA methyltransferase activity. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. Dnmt3l is also associating with HDAC1 and acts as a transcriptional repressor. The ADDz_Dnmt3l domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif
RSIEEICICCGSLQIHTQHPLFHGGICAPCTEKFLEAFFLYDEDGYQAYCTICCSGETLLMCDDPDCTRC
YCFECVDSLVGPGTSEKVKATNNWVCFLCLPSSRSGLLQRKRKWRSQLKAFYD
>gnl|CDD|277254 cd11728, ADDz_Dnmt3b, ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b). ADDz_Dnmt3b is an active catalytic domain of Dnmt3b. Dnmt3b is a member of the Dnmt3 family and is a de novo DNA methyltransferases that has an N-terminal variable region followed by a conserved PWWP region and the cysteine-rich ADDz domain. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The methyltransferase activity of Dnmt3a is not only responsible for the establishment of DNA methylation pattern, but is also essential for the inheritance of these patterns during mitosis. Dnmt3b is ubiquitously expressed in most adult tissues. The ADDz_Dnmt3 domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif. A knockout of Dnmt3b has been shown to be lethal in the mouse model
IEDFCLSCGRSNPATFHPLFEGGLCITCKDRFLELFYMYDDDGYQSYCTVCCEGRELLLCGNASCCRCFC
VDCLEVLVGPGTAAKAKEQDPWSCYMCLPQRCYGVLKRRTDWSVRLQEFF
>gnl|CDD|277255 cd11729, ADDz_Dnmt3a, ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a). Dnmt3a is a member of the Dnmt3 family and is a protein with de novo DNA methyltransferase activity. Dnmt3 family members are Dnmt3a, Dnmt3b, and Dnmt3l the non-enzymatic regulatory factor. Dnmt3a is recruited by Dnmt3l to unmethylated histone H3 and methylates the target. Dnmt3a has a variable region at the N-terminus, followed by a conserved PWWP region and the cysteine-rich ADDz domain. ADDz_Dnmt3a is an active catalytic domain of Dnmt3a. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The methyltransferase activity of Dnmt3a is not only responsible for the establishment of DNA methylation pattern, but is also essential for the inheritance of these patterns during mitosis. The ADDz_Dnmt3 domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif. A knockout of Dnmt3a has been shown to be lethal in the mouse model
CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCR
CFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD
>gnl|CDD|212496 cd11730, Tthb094_like_SDR_c, Tthb094 and related proteins, classical (c) SDRs. Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALARPADVAAELEVWALAQELGPLDLL
VYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFLGAYPELVMLPGLSAYAAAK
AALEAYVEVARKEVRGLRLTLVRPPAVDTGLWAPPGRLPKGALSPEDVAAAILEAHQGEPQGELDL
>gnl|CDD|212497 cd11731, Lin1944_like_SDR_c, Lin1944 and related proteins, classical (c) SDRs. Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction
IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDYQVDITDEASIKALFEKVGHFDAIVSTAGDAEFAPL
AELTDADFQRGLNSKLLGQINLVRHGLPYLNDGGSITLTSGILAQRPIPGGAAAATVNGALEGFVRAAAI
ELPRGIRINAVSPGVVEESLEAYGDFFPGFEPVPAEDVAKAYVRSVEGAFTGQVLHVD
>gnl|CDD|466838 cd11732, ASKHA_NBD_HSP70_HSP105-110-like, nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family. The 105/110 kDa heat shock proteins family includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25), Saccharomyces cerevisiae Sse1p, Sse2p and a sea urchin sperm receptor. They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs)
VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGL
KFDDPEVQKEIKLLPFKLVELEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVIS
VPGYYTDAQRRALLDAAEIAGLNCLRLINETTAAALDYGIYKSDLLESEEKPRIVAFVDMGHSSTQVSIA
AFTKGKLKVLSTAFDRNLGGRDFDRALVEHFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEA
PLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAI
AEVFGKDLSTTLNADEAVARGCALQAA
>gnl|CDD|466839 cd11733, ASKHA_NBD_HSP70_HSPA9, nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and similar proteins. This subgroup includes human mitochondrial HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74). It acts as a chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. It interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. HSPA9 regulates erythropoiesis via stabilization of ISC assembly. It may play a role in the control of cell proliferation and cellular aging. Members in this subgroup belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs)
GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPENTLYATKR
LIGRRFDDPEVQKDIKMVPYKIVKASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVIT
VPAYFNDSQRQATKDAGQIAGLNVLRIINEPTAAALAYGLDKKDDKIIAVYDLGGGTFDISILEIQKGVF
EVKATNGDTFLGGEDFDNALLNYLVAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFI
TADASGPKHLNMKLTRAKFESLVGDLIKRTVEPCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEI
FGKAPSKGVNPDEAVAMGAAIQGGVLA
>gnl|CDD|466840 cd11734, ASKHA_NBD_HSP70_Ssc1_3, nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein Ssc1p and Ssc3p and similar proteins. This subgroup includes Saccharomyces cerevisiae Stress-Seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and sc3p (also called extracellular mutant protein 10/Ecm10). Ssc1p is an essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. It constitutes the ATP-driven core of the motor and binds the precursor preprotein. It is required for the import of the processed frataxin homolog YFH1 into the mitochondrion. Ssc1p also acts as a non-catalytic component of endonuclease SceI (endo.SceI), which cleaves specifically at multiple sites on mitochondrial DNA and produces double-stranded breaks. Ssc1p confers broader sequence specificity, greater stability, and higher activity on the catalytic subunit. Ssc3p plays a role in facilitating the assembly of some protein complexes inside the mitochondria. It may initiate the events that lead to refolding of imported precursors in the matrix space
GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLVGVPAKRQAVVNPENTLFATKR
LIGRKFDDAEVQRDIKEVPYKIVKHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVT
VPAYFNDSQRQATKDAGQIAGLNVLRVINEPTAAALAYGLDKSGDKVIAVYDLGGGTFDISILEIQKGVF
EVKSTNGDTHLGGEDFDIALVRHIVSEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFI
TADASGPKHINMKLTRAQFESLVKPLVDRTVEPCKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSI
FGREPSKGVNPDEAVAIGAAIQGGVLSG
>gnl|CDD|466841 cd11735, ASKHA_NBD_HSP70_HSPA12A, nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A
VVVAIDFGTTSSGYAYSFTKEPECIHVMRRWEGGDPGVSNQKTPTTILLTPERKFHSFGYAARDFYHDLD
PNESKQWLYFEKFKMKLHTTGNLTMETDLTAANGKKVKALEIFAYALQFFKEQALKELSDQAGSEFDNSD
VRWVITVPAIWKQPAKQFMRQAAYKAGLASPENPEQLIIALEPEAASIYCRKLRLHQMDRYVVVDCGGGT
VDLTVHQIRLPEGHLKELYKASGGPYGSLGVDYEFEKLLCKIFGEDFIDQFKIKRPAAWVDLMIAFESRK
RAAAPDRTNPLNITLPFSFIDYYKKFRGHSVEHALRKSNVDFVKWSSQGMLRMSPDAMNALFKPTIDHII
QHLTDLFQKPEVSGVKFLFLVGGFAESPLLQQAVQNAFGDQCRVIIPHDVGLTILKGAVLFGL
>gnl|CDD|466842 cd11736, ASKHA_NBD_HSP70_HSPA12B, nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B
VVVAIDFGTTSSGYAFSFSSDPEAIHMMRKWEGGDPGVANQKTPTSLLLTPDGAFHSFGYTARDYYHDLD
PEEARDWLYFEKFKMKIHSTSDLTMETELEAVNGKKVQALEVFAHALRFFKEHALQELKDQSPSLPEKDA
VRWVLTVPAIWKQPAKQFMREAAYLAGLVSPENPEQLLIALEPEAASIYCRKLDRYIVADCGGGTVDLTV
HQIEQPQGTLKELYKASGGPYGAVGVDLAFEKLLCQIFGEDFIATFKAKRPAAWVDLTIAFEARKRTAAL
RMSSEAMNELFQPTISQIIQHIDDLMKKPEVKGIKFLFLVGGFAESPMLQRAVQAAFGNICRVIIPQDVG
LTILKGAVLFG
>gnl|CDD|466843 cd11737, ASKHA_NBD_HSP70_HSPA4, nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins. HSPA4, also called HSP70RY, HS24/P52, hsp70 RY, and HSPH2, or heat shock 70-related protein APG-2, responds to acidic pH stress, is involved in the radioadaptive response, is required for normal spermatogenesis and is overexpressed in hepatocellular carcinoma. It participates in a pathway along with NBS1 (Nijmegen breakage syndrome 1, also known as p85 or nibrin), heat shock transcription factor 4b (HDF4b), and HSPA14 (belonging to a different HSP70 subfamily) that induces tumor migration, invasion, and transformation. HSPA4 expression in sperm was increased in men with oligozoospermia, especially in those with varicocele. HSPA4 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins
SVVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFH
GRAFSDPFVQAEKPSLAYELVQLPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCV
VSVPCFYTDAERRSVMDATQIAGLNCLRLMNETTAVALAYGIYKQDLPAPEEKPRNVVFVDMGHSAYQVS
VCAFNKGKLKVLATAFDPTLGGRKFDEVLVNHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANA
SDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVK
ERISKFFGKEVSTTLNADEAVARGCALQCAI
>gnl|CDD|466844 cd11738, ASKHA_NBD_HSP70_HSPA4L, nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins. HSPA4L, also called heat shock 70-related protein APG-1, heat-shock protein family A member 4-like protein, HSPA4-like protein, osmotic stress protein 94, or HSPH3, possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. It is expressed ubiquitously and predominantly in the testis. It is required for normal spermatogenesis and plays a role in osmotolerance. HSPA4L belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins
SVVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFH
GRAFDDPFVQAEKIKLPYELQKMPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCV
ISVPSFFTDAERRSVMDAAQIAGLNCLRLMNETTAVALAYGIYKQDLPALEEKPRNVVFVDMGHSAYQVS
ICAFNKGKLKVLATTFDPYLGGRNFDEVLVDYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSANA
SDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLKAVMEQAKLQREDIYSIEIVGGATRIPAVK
ERIAKFFGKDISTTLNADEAVARGCALQCAILS
>gnl|CDD|466845 cd11739, ASKHA_NBD_HSP70_HSPH1, nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar proteins. HSPH1, also called heat shock protein 105 kDa, antigen NY-CO-25, heat shock 110 kDa protein, acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release. It prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. It inhibits HSPA8/HSC70 ATPase and chaperone activities. HSPH1 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins
SVVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFH
GRAFNDPFVQKEKENLSYDLVPLKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCV
ISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNYGIYKQDLPAPDEKPRIVVFVDMGHSAFQVS
ACAFNKGKLKVLGTAFDPYLGGRNFDEKLVEHFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSNS
TDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLYSLMEQTQLKVEDISAVEIVGGATRIPAVK
ERIAKFFGKDVSTTLNADEAVARGCALQCA
>gnl|CDD|213038 cd11740, YajQ_like, Proteins similar to Escherichia coli YajQ. In Pseudomonas syringae, YajQ functions as a host protein involved in the temporal control of bacteriophage Phi6 gene transcription. It has been shown to bind to the phage's major structural core protein P1, most likely activating transcription by acting indirectly on the RNA polymerase. YajQ may remain bound to the phage particles throughout the infection period. Earlier, YajQ was characterized as a putative nucleic acid-binding protein based on the similarity of its (ferredoxin-like) three-dimensional topology with that of RNP-like RNA-binding domains
PSFDIVSEVDMQEVDNAVDQANKEISTRFDFKGSKASIELNEETITLTADSDFKLKQVLDILRSKLIKRG
IDLKALDYGKPEPASGGTVRQEVKLKQGIDQELAKKIVKLIKDSKLKVQAQIQGDQVRVTGKKRDDLQAV
IALLKGADLGQPLQFTNFR
>gnl|CDD|240666 cd11741, TIN2_TBM, TRF-binding motif region of TRF-Interacting Nuclear factor 2. The C-terminal region of TIN2 contains the TRF-binding motif (TBM), while the TIN2 N-terminal region acts in the modulation of TRF1 activity via the inhibition of tankyrase 1. TIN2 binding to TRF2 is primarily via the TRF binding motif (TBM) and the N-terminus, while the far C-terminal region interacts with lower affinity. The TIN2 TBM, but not the N-terminal region, is involved in TIN2 binding to TRF1. Truncation of the TIN2 N-terminus in mouse results in telomere elongation, suggesting a a negative regulatory function of this region. TIN2 is a shelterin complex protein identified in mammals, one of 6 factors that act to protect telomeres from DNA damage repair machinery. Three shelterin components (TRF1, TRF2, POT1) bind DNA and 3 components (TIN2, RAP1, TPP1) are recruited by these DNA binding factors. TIN2 binds directly to TRF1 and TRF2 and stabilizes TRF2 complex-telomere binding by tethering it to the TRF1 complex. TRF1 activity at telomeres is regulated in part by selective ubiquitination and degradation. Ubiquitination of TRF1 is mediated by Fbx4, which binds TRF1 in the TRFH domain, via a small GTPase module. When bound to telomeres, TIN2 acts to protect TRF1 from SCF-Fbx4 mediated ubiquitination. F-box proteins act in substrate recognition as part of SCF complexes (SCF: Skp1-Cul1-Rbx1-F- box protein). Tankyrase-mediated ADP-ribosylation releases TRF1 from telomeres, rendering them susceptible to ubiquitination and degradation, promoting telomere elongation. TIN2 also binds TPP1, which recruits POT1 to telomeres
PPSSLTGRGFGLAPLSKRKSQSRWPSAPRSHKERPTTMLPPRRSTKLPTQKPSRSPASREEHGNNDAAAS
MGTRSSSTPKAKSPDPQDPLGRRSQERPPCSSAASNSF
>gnl|CDD|213039 cd11743, Cthe_2751_like, Uncharacterized protein domain similar to Clostridium thermocellum 2751. Cthe_2751 has been found to form homodimers. Based on structural similarity to other families, a role in processing nucleic acids was suggested, though interactions with DNA could not be demonstrated
LIPKDKFDTDAVKKLKQLGYEEVKPILPELLEWLQDMNWPVAGEIAPLLARFGEELVPEIKEVLRSNDDI
WKYWILLLLVPELPKELIEELKPELERLASNPTEDEDEEEVDELAKEILEKL
>gnl|CDD|213354 cd11744, MIT_CorA-like, metal ion transporter CorA-like divalent cation transporter superfamily. This superfamily of essential membrane proteins is involved in transporting divalent cations (uptake or efflux) across membranes. They are found in most bacteria and archaea, and in some eukaryotes. It is a functionally diverse group which includes the Mg2+ transporters of Escherichia coli and Salmonella typhimurium CorAs (which can also transport Co2+, and Ni2+), the CorA Co2+ transporter from the hyperthermophilic Thermotoga maritima, and the Zn2+ transporter Salmonella typhimurium ZntB, which mediates the efflux of Zn2+ (and Cd2+). It includes five Saccharomyces cerevisiae members: i) two plasma membrane proteins, the Mg2+ transporter Alr1p/Swc3p and the putative Mg2+ transporter, Alr2p, ii) two mitochondrial inner membrane Mg2+ transporters: Mfm1p/Lpe10p, and Mrs2p, and iii) and the vacuole membrane protein Mnr2p, a putative Mg2+ transporter. It also includes a family of Arabidopsis thaliana members (AtMGTs), some of which are localized to distinct tissues, and not all of which can transport Mg2+. Thermotoga maritima CorA and Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, Mrs2p, and Alr1p. Natural variants such as GVN and GIN, as in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport
WIHCERLHDDDIRRVLEDNLHVPRALEDILLAESRPSFHPLDDNFMIILRGFNMDENASPEDMLSVRILY
FQGALISTREIPSRAFMEIRQRLREHSKGPKSAASLLNQLIEGLNGKIDLYLETIEETLNELDVNDEEGH
YDESTYNHIALQKALISIRRFIRPQQYALRDLIRSESELVTSRPHQYRFAHNNITRINETIEFYLGEVAL
LQDEIKHNRDEKTNKNSKLFTLVATIFLPTTFLAGLYGMNFEGMPGVESSMAFTWFCIALIVAFGLEWLL
FKRKGF
>gnl|CDD|213372 cd11745, Yos9_DD, C-terminal dimerization domain (DD) of Saccharomyces cerevisiae Yos9 and related proteins. Yos9 participates in the ER-associated protein degradation pathway that targets misfolded proteins for proteolysis. Yos9 is a component of the reductase degradation (HRD) ubiquitin-ligase complex, specifically part of the luminal submodule of the ligase. Yos9 scans proteins for specific oligosaccharide modifications, which are critical determinants of degradation signal. It has been shown to be involved in the degradation of glycosylated proteins and various nonglycosylated proteins. Yos9 functions as a homodimer where this domain is responsible for the self-association; it has an alphabeta-roll domain architecture, and is found at the C-terminus of the protein. The N-terminal portion of Yos9 which includes an MRH domain is required for binding to Hrd3p, another component of the HRD complex. The DD domain does not appear to be directly binding Hrd3p
YDPTFLGHGFYLLAPKNNSNNDRAKLMYTGNLNSDEEWDEVEEELYKKFGNAFSRMLGLGLLLLPDGLPL
QPGDSFTWIADVVDMTGNFLTRLRFNISSNDIAEIVIDKSLEFPEIGNFEYYER
>gnl|CDD|213062 cd11746, GH94N_like, N-terminal domain of glycoside hydrolase family 94 and related domains. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. This GH64N domain also occurs in tandem repeat arrangements (not at the N-terminus) in cyclic beta 1-2 glucan synthetase and related proteins, and as a standalone domain in distantly related proteins of unknown function
FYFYLSDDGDKWSLGWQPVRREAEHYEVRLGYVTFENEYNGIEAETTIFVPPDDPGEIQRVKLTNTGDRP
RELTLFPYFEWCLPDALFQGTSYDPEGGAVNCTTYYSYNIGARPAFYATSFKPDDFDGDGGRTLANPLAV
VAGQLSNTVGRVEDPIAALAIRFALEPGESKRYTFALGI
>gnl|CDD|213063 cd11747, GH94N_like_1, Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase and many other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain. This GH64N domain also occurs as a standalone domain in distantly related proteins of unknown function, as represented by this model, which also includes N-terminal GH94N-like domains of bacterial rhamnosidases and as found at the C-terminus of polygalacturonases
FALYLPGMGGNLRLGISKGSESKWLDDADSIETRYRPGRMLYTIRDALLGGGSLRLTVLALADTEGFILE
VSGKNLPEGIKLLWAFGGASGKKFSRDGSFYLKPEYCKDNVFQVEGNSFTLYYGESMSSTSKLKTLSGIF
PVGSEIRLSDAHKQDTPLELLSSKKTDAPVLAGKVPLKKGQPLYFCIYRQNAGADYAYYMLPDL
>gnl|CDD|213064 cd11748, GH94N_NdvB_like, Glycoside hydrolase family 94 N-terminal-like domain of NdvB-like proteins. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel)]. The GH64N domain, as represented by this model, is found at the N-terminus of largely uncharacterized proteins, some members from Xanthomonas campestris and related organisms are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants
LFTESGERYELTSPTAMPQAAGFLWNRKMMIQMNCRGYATAQFMQPEPAKYAHAPNLEAKTFMQPEQPYY
AHHPGRFFYVKDEDTGELFSAPYEPVRRPPDSFAFSVGKNDIRWVVEQDGLEVELTLSLPVDDPAELWEV
KVRNLSDRARKLSLYPYFPVGYMSWMNQSARYDEGLNAIVASSVTPYQKVEDYFKNKDLKDKTFLLADRK
PDSWEARQEAFEGEGGLHNPSALQAPTLANGDARYETPAAVMQYRLTLDPGETEQYRFVFGPAKDEAEIA
QLRARYLGAEGFER
>gnl|CDD|213065 cd11749, GH94N_LBP_like, N-terminal-like domain of Paenibacillus sp. YM-1 Laminaribiose Phosphorylase and similar proteins. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes bacterial laminaribiose phosphorylase. This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Bacterial laminaribiose phosphorylase phosphorolyzes laminaribiose into alpha-glucose 1-phosphate and glucose, but does not phosphorolyze other glucobioses; it slightly phosphorolyzed laminaritriose and higher laminarioligosaccharides. The GH64N domain, as represented by this model, is also found at the N-terminus of GH94 members with uncharacterized specificities
FWCYIEGKGAWSATGNSAEQEAQKFTDDKDESELEAGFMWHKVTRTSKELGLKAEITSFVPVDDDNVELM
KVTITNTGDEPLKFTPTAAIPLYGRSADNLRDHRHVTSLLHRIETTEYGVLVNPTLSFDERGHQPNHTTY
GVFGRTGDGEAPVGFYPTVEDFIGEGGSFEWPEAVVENKIPGVKAGTKVDGYEAVGALRFEEVTLKPGES
KSYVVLMGISEDEEEIEEI
>gnl|CDD|213066 cd11750, GH94N_like_3, Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. The GH64N domain, as represented by this model, is found at the N-terminus of GH94 members with uncharacterized specificities
YGYFDDANKEYVITTPKTPIKWINYVGTLDFGGFVDHTGGSLVCKGDPALNRITKYIAQLPSSDFKGSTI
YIRVKDGDNYKIFSPFYVPTLDKYDKYECHVGLGYSRIIAEAYGIRTEITIFVPEGDQVLLQDIKVTNIR
DKPVEVDVIPVVEYTHFDALKQLTNADWVPQTMTSKAHQEENGHTVLEQYAFMKRDYAVNYFTSNRPVSS
FEGDRRSFLGQNEYGTWANPLSLQNDELSNYECLRGDNIGALMHHLGWLAPGETKRVITQLGQEESLKAA
QP
>gnl|CDD|213067 cd11751, GH94N_like_4, Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. The GH64N domain, as represented by this model, is found near the N-terminus of GH94 members and related proteins with uncharacterized specificities
QDLIKDNWGKYFYIRDDDTGEVWSATYKPLKTEPEDYECVHGIGYSEFTSEYNGIRSSLTVFVPKDDPVE
IWSLTLRNTSDRERRLSVFSYFEWELGGFPDEHREFHKLFIETSFDRELNGIYARKYLWGFPDEKGRHNN
RNWPYVAFHAASEPVVSYDGDKESFIGMYGSEENPDAVAMGGLSNSVGRFEDAIGVLQHEVTLEPGEEKT
IHFTLGAAESGEE
>gnl|CDD|213068 cd11752, GH94N_CDP_like, N-terminal domain of cellodextrin phosphorylase (CDP) and similar proteins. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellodextrin phosphorylase (EC:2.4.1.49), also known as 1,4-beta-D-oligo-D-glucan:phosphate alpha-D-glucosyltransferase or CepB. This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Cellodextrin phosphorylase catalyzes the reversible and phosphate dependent removal of a single alpha-D-glucose-1-phosphate unit from a (1,4-beta-D-glucosyl) oligomer
RQFYLVEDGKQIFYSADALDSNIESATCRHSQNHTEIEYKTKCGLEILRTIFLVPQYEGLPIATEVQRIE
IKNKTDKTRNLKIVYTGMFGTAAPHALMEDVLYSNVIMQSQLLKDDEGSLIGITPDYYPESFSRDIRFHT
MIVRNGDARKFPKEFCTHYNEFVGSGSLEKPEGVRKLSNRLNRKGPGFFALGSPITLEPGKTVTIDNFTG
LSSN
>gnl|CDD|213069 cd11753, GH94N_ChvB_NdvB_2_like, Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This second of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants
MQRRFHADPRIQAAELLLQERIPREVPIITPRLEELSRPAKKEEEAPEPVRRFTTPDTALPEVHLLSNGR
YSVMLTASGSGYSRWNDLAVTRWREDATRDNWGSFIYLRDVDSGKVWSATYQPTRDPPDEYEVVFSEDRA
EFRRRDGGIETTTEVVVSPEDDAEIRRVTLTNLSRRPRELEVTSYAEVVLAPPAADEAHPAFSKLFVQTE
FLPEQGALLATRRPRSPDEPPPWAAHFVAVEGEAVGPLQYETDRARFIGRGRSLANPAAMDDGAPLSGTV
GAVLDPIFSLRRRVRLPPGETARVTFVTGVADSREEALELADKYRDPSAVERAFEL
>gnl|CDD|213070 cd11754, GH94N_CBP_like, N-terminal domain of cellobiose phosphorylase (CBP) and similar proteins. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20) or cellobiose:phosphate alpha-D-glucosyltransferase, or CepA. This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Cellobiose phosphorylase participates in the degradation of cellulose, it catalyzes the phosphate dependent hydrolysis of cellobiose into alpha-D-glucose-1-phosphate and D-glucose, a reversible reaction
MKYGHFDDENREYVITTPDTPLPWINYLGSEDFFSLISNTAGGYSFYKDARLRRLTRYRYNNVPLDNGGR
YFYIKDGGTVWNPGWKPVKTPLDSYECRHGLGYTRITGEKNGIEAEVLYFVPLGENAEIWRLTLTNTSDS
PKKLKLFSFVEFCLWNALDDMTNFQRNLSTGEVEVEGSVIYHKTEYRERRNHYAFFAVNAPIDGFDTDRD
AFLGLYNGFDEPQAVLEGKSTNSVAHGWSPIGSHHVELTLAPGESKELIFVLGYVENPDDEKWESPGVIN
KKPAKELIERFATPEAVDAAFAE
>gnl|CDD|213071 cd11755, GH94N_ChBP_like, N-terminal domain of chitobiose phosphorylase (ChBP) and similar proteins. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes chitobiose phosphorylase (EC:2.4.1.-). This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Chitobiose phosphorylase catalyzes the reversible phosphate dependent hydrolysis of chitobiose [(GlcNAc)2] into alpha-GlcNAc-1-phosphate and GlcNAc. In some organisms, ChBP may be involved in the production of GlcNac-6-phosphate in intracellular pathways
MKYGYFDDENREYVITRPDTPTPWTNYLGSGEYGAIISNNAGGYSFYKSPANGRITRFRFNSVPMDRPGR
YVYLRDNESGDYWSASWQPVGKPLDEYKYECRHGTGYTTIESEYKGIAAETTYFVPLDQDYEIWDVKITN
TSSRKRKLSVFSYAEFSFHWNAEQDQQNLQYSLYISRTSYKDGIIEYDNYYNLDDDPNGDERYRFFTSAG
AEVDGFDGSRDRFIGPYRSESNPIAVERGKCSNSLATGGNHCGALQSDITLAPGEEKEIIFILGVGNREE
GRAIRAKYSDPEAVDAEFEA
>gnl|CDD|213072 cd11756, GH94N_ChvB_NdvB_1_like, First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This first of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants
DLQFFNGYGGFSPDGREYVIVLGPGKRTPAPWINVIANPGFGFLVSESGSGYTWAENSRENRLTPWSNDP
VSDPPGEALYLRDEETGEVWSPTPLPIRGGGPYRVRHGFGYSRFEHRSHGIEQELTVFVPRDDPVKISRL
RLRNTSGRPRRLSVTYYAEWVLGVNREKTAPHIVTEYDEETGALLARNPYNEDFGGRVAFLAVSGGPRSF
TGDRREFIGRNGSLANPAALKRGRLSGRTGAGLDPCAALQVDLELAPGEEKEIVFLLGEADDAEEARALI
RRYR
>gnl|CDD|212691 cd11757, SH3_SH3BP4, Src Homology 3 domain of SH3 domain-binding protein 4. SH3 domain-binding protein 4 (SH3BP4) is also called transferrin receptor trafficking protein (TTP). SH3BP4 is an endocytic accessory protein that interacts with endocytic proteins including clathrin and dynamin, and regulates the internalization of the transferrin receptor (TfR). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EVVAIKDYCPTNFTTLKFSKGDHLYVLDTSGGEWWYAHNTTEMGYIPSSYVQ
>gnl|CDD|212692 cd11758, SH3_CRK_N, N-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins. CRK adaptor proteins consists of SH2 and SH3 domains, which bind tyrosine-phosphorylated peptides and proline-rich motifs, respectively. They function downstream of protein tyrosine kinases in many signaling pathways started by various extracellular signals, including growth and differentiation factors. Cellular CRK (c-CRK) contains a single SH2 domain, followed by N-terminal and C-terminal SH3 domains. It is involved in the regulation of many cellular processes including cell growth, motility, adhesion, and apoptosis. CRK has been implicated in the malignancy of various human cancers. The N-terminal SH3 domain of CRK binds a number of target proteins including DOCK180, C3G, SOS, and cABL. The CRK family includes two alternatively spliced protein forms, CRKI and CRKII, that are expressed by the CRK gene, and the CRK-like (CRKL) protein, which is expressed by a distinct gene (CRKL). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EYVRALFDFPGNDDEDLPFKKGEILTVIRKPEEQWWNARNSEGKTGMIPVPYVEK
>gnl|CDD|212693 cd11759, SH3_CRK_C, C-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins. CRK adaptor proteins consists of SH2 and SH3 domains, which bind tyrosine-phosphorylated peptides and proline-rich motifs, respectively. They function downstream of protein tyrosine kinases in many signaling pathways started by various extracellular signals, including growth and differentiation factors. Cellular CRK (c-CRK) contains a single SH2 domain, followed by N-terminal and C-terminal SH3 domains. It is involved in the regulation of many cellular processes including cell growth, motility, adhesion, and apoptosis. CRK has been implicated in the malignancy of various human cancers. The C-terminal SH3 domain of CRK has not been shown to bind any target protein; it acts as a negative regulator of CRK function by stabilizing a structure that inhibits the access by target proteins to the N-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components, and mediating the formation of multiprotein complex assemblies
PAYARVIQKRVPNAYDKTALALEVGDLVKVTKINVSGQWEGELNGKVGHFPFTHVEL
>gnl|CDD|212694 cd11760, SH3_MIA_like, Src Homology 3 domain of Melanoma Inhibitory Activity protein and similar proteins. MIA is a single domain protein that adopts a SH3 domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. MIA is secreted from malignant melanoma cells and it plays an important role in melanoma development and invasion. MIA is expressed by chondrocytes in normal tissues and may be important in the cartilage cell phenotype. Unlike classical SH3 domains, MIA does not bind proline-rich ligands. MIA is a member of the recently identified family that also includes MIA-like (MIAL), MIA2, and MIA3 (also called TANGO); the biological functions of this family are not yet fully understood
LCADAECSNPISRARALEDYHGPDCRFLNFKKGDTIYVYSKLAGERQDLWAGSVGGDAGLFGYFPKNLVQ
ELKVYE
>gnl|CDD|212695 cd11761, SH3_FCHSD_1, First Src Homology 3 domain of FCH and double SH3 domains proteins. This group is composed of FCH and double SH3 domains protein 1 (FCHSD1) and FCHSD2. These proteins have a common domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. They have only been characterized in silico and their functions remain unknown. This group also includes the insect protein, nervous wreck, which acts as a regulator of synaptic growth signaling. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
PVTCKVLYSYEAQRPDELTITEGEELEVIEDGDGDGWVKARNKSGEVGYVPENYLQF
>gnl|CDD|212696 cd11762, SH3_FCHSD_2, Second Src Homology 3 domain of FCH and double SH3 domains proteins. This group is composed of FCH and double SH3 domains protein 1 (FCHSD1) and FCHSD2. These proteins have a common domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. They have only been characterized in silico and their functions remain unknown. This group also includes the insect protein, nervous wreck, which acts as a regulator of synaptic growth signaling. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LVRALYDYEAQSDEELSFPEGAIIRILRKDDNGVDDGWWEGEFNGRVGVFPSLVVEE
>gnl|CDD|212697 cd11763, SH3_SNX9_like, Src Homology 3 domain of Sorting Nexin 9 and similar proteins. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. This subfamily consists of SH3 domain containing SNXs including SNX9, SNX18, SNX33, and similar proteins. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KVRALYDFDSQPSGELSLRAGEVLTITRQDVGDGWLEGRNSRGEVGLFPSSYVEI
>gnl|CDD|212698 cd11764, SH3_Eps8, Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins. This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YVRVLYDFTARNSKELSVLKGEYLEVLDDSRQWWKVRNSRGQVGYVPHNILEPY
>gnl|CDD|212699 cd11765, SH3_Nck_1, First Src Homology 3 domain of Nck adaptor proteins. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The first SH3 domain of Nck proteins preferentially binds the PxxDY sequence, which is present in the CD3e cytoplasmic tail. This binding inhibits phosphorylation by Src kinases, resulting in the downregulation of TCR surface expression. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YVVAKYDYTAQGDQELSIKKNEKLTLLDDSKHWWKVQNSSNQTGYVPSNYV
>gnl|CDD|212700 cd11766, SH3_Nck_2, Second Src Homology 3 domain of Nck adaptor proteins. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
PAVVKFNYEAQREDELSLRKGDRVLVLEKSSDGWWRGECNGQVGWFPSNYVTE
>gnl|CDD|212701 cd11767, SH3_Nck_3, Third Src Homology 3 domain of Nck adaptor proteins. This group contains the third SH3 domain of Nck, the first SH3 domain of Caenorhabditis elegans Ced-2 (Cell death abnormality protein 2), and similar domains. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. Ced-2 is a cell corpse engulfment protein that interacts with Ced-5 in a pathway that regulates the activation of Ced-10, a Rac small GTPase
VVVALYPFTGENDEELSFEKGERLEIIEKPEDDPDWWKARNALGTTGLVPRNYVEV
>gnl|CDD|212702 cd11768, SH3_Tec_like, Src Homology 3 domain of Tec-like Protein Tyrosine Kinases. The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
IVVALYDFQPIEPGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPSNYVTE
>gnl|CDD|212703 cd11769, SH3_CSK, Src Homology 3 domain of C-terminal Src kinase. CSK is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, CSK is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. CSK catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. It is expressed in a wide variety of tissues and plays a role, as a regulator of Src, in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. In addition, CSK also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GTECIAKYNFNGASEEDLPFKKGDILTIVAVTKDPNWYKAKNKDGREGMIPANYVQK
>gnl|CDD|212704 cd11770, SH3_Nephrocystin, Src Homology 3 domain of Nephrocystin (or Nephrocystin-1). Nephrocystin contains an SH3 domain involved in signaling pathways that regulate cell adhesion and cytoskeletal organization. It is a protein that in humans is associated with juvenile nephronophthisis, an inherited kidney disease characterized by renal fibrosis that lead to chronic renal failure in children. It is localized in cell-cell junctions in renal duct cells, and is known to interact with Ack1, an activated Cdc42-associated kinase. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LYEALSDFQAEQEGDLSFKKGEVLRIISKRADGWWLAENSKGNRGLVPKTYLKV
>gnl|CDD|212705 cd11771, SH3_Pex13p_fungal, Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p. Pex13p, located in the peroxisomal membrane, contains two transmembrane regions and a C-terminal SH3 domain. It binds to the peroxisomal targeting type I (PTS1) receptor Pex5p and the docking factor Pex14p through its SH3 domain. It is essential for both PTS1 and PTS2 protein import pathways into the peroxisomal matrix. Pex13p binds Pex14p, which contains a PxxP motif, in a classical fashion to the proline-rich ligand binding site of its SH3 domain. It binds the WxxxF/Y motif of Pex5p in a novel site that does not compete with Pex14p binding. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FCRALYDFTPENPEMELSLKKGDIVAVLSKTDPLGRDSEWWKGRTRDGRIGWFPSNYVEV
>gnl|CDD|212706 cd11772, SH3_OSTF1, Src Homology 3 domain of metazoan osteoclast stimulating factor 1. OSTF1, also named OSF or SH3P2, is a signaling protein containing SH3 and ankyrin-repeat domains. It acts through a Src-related pathway to enhance the formation of osteoclasts and bone resorption. It also acts as a negative regulator of cell motility. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VFRALYDYEAQHPDELSFEEGDLLYISDKSDPNWWKATCGGKTGLIPSNYVEE
>gnl|CDD|212707 cd11773, SH3_Sla1p_1, First Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p. Sla1p facilitates endocytosis by playing a role as an adaptor protein in coupling components of the actin cytoskeleton to the endocytic machinery. It interacts with Abp1p, Las17p and Pan1p, which are activator proteins of actin-related protein 2/3 (Arp2/3). Sla1p contains multiple domains including three SH3 domains, a SAM (sterile alpha motif) domain, and a Sla1 homology domain 1 (SHD1), which binds to the NPFXD motif that is found in many integral membrane proteins such as the Golgi-localized Arf-binding protein Lsb5p and the P4-ATPases, Drs2p and Dnf1p. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VYKALYDYEPQTEDELTIQEDDILYLLEKSDDDWWKVKLKVNSSDDDEPVGLVPATY
>gnl|CDD|212708 cd11774, SH3_Sla1p_2, Second Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p. Sla1p facilitates endocytosis by playing a role as an adaptor protein in coupling components of the actin cytoskeleton to the endocytic machinery. It interacts with Abp1p, Las17p and Pan1p, which are activator proteins of actin-related protein 2/3 (Arp2/3). Sla1p contains multiple domains including three SH3 domains, a SAM (sterile alpha motif) domain, and a Sla1 homology domain 1 (SHD1), which binds to the NPFXD motif that is found in many integral membrane proteins such as the Golgi-localized Arf-binding protein Lsb5p and the P4-ATPases, Drs2p and Dnf1p. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QAKALYDYDKQTEEELSFNEGDTLDVYDDSDSDWILVGFNGTQFGFVPANYI
>gnl|CDD|212709 cd11775, SH3_Sla1p_3, Third Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p. Sla1p facilitates endocytosis by playing a role as an adaptor protein in coupling components of the actin cytoskeleton to the endocytic machinery. It interacts with Abp1p, Las17p and Pan1p, which are activator proteins of actin-related protein 2/3 (Arp2/3). Sla1p contains multiple domains including three SH3 domains, a SAM (sterile alpha motif) domain, and a Sla1 homology domain 1 (SHD1), which binds to the NPFXD motif that is found in many integral membrane proteins such as the Golgi-localized Arf-binding protein Lsb5p and the P4-ATPases, Drs2p and Dnf1p. The third SH3 domain of Sla1p can bind ubiquitin while retaining the ability to bind proline-rich ligands; monoubiquitination of target proteins signals internalization and sorting through the endocytic pathway. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KRGKVLYDFDAQSDDELTVKEGDVVYILDDKKSKDWWMVENVSTGKEGVVPASYIEI
>gnl|CDD|212710 cd11776, SH3_PI3K_p85, Src Homology 3 domain of the p85 regulatory subunit of Class IA Phosphatidylinositol 3-kinases. Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VQYRALYDYEKERDEDIILKTGDVLVVENPELLALGVPDGKETVPKPEGWLEGKNERTGERGDFPGTYVE
FY
>gnl|CDD|212711 cd11777, SH3_CIP4_Bzz1_like, Src Homology 3 domain of Cdc42-Interacting Protein 4, Bzz1 and similar domains. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4) and similar proteins such as Formin Binding Protein 17 (FBP17) and FormiN Binding Protein 1-Like (FNBP1L), as well as yeast Bzz1 (or Bzz1p). CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Bzz1 is also a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Members of this subfamily contain an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain as well as at least one C-terminal SH3 domain. Bzz1 contains a second SH3 domain at the C-terminus. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
ECKALYAFVGSSEGTISMTEGEKLSLVEEDKGDGWTRVRRDTGEEGYVPTSYIRI
>gnl|CDD|212712 cd11778, SH3_Bzz1_2, Second Src Homology 3 domain of Bzz1 and similar domains. Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the second C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YVEALYDYEAQGDDEISIRVGDRIAVIRGDDGSGWTYGEINGVKGLFPTSY
>gnl|CDD|212713 cd11779, SH3_Irsp53_BAIAP2L, Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2 (BAIAP2)-Like proteins, and similar proteins. Proteins in this family include IRSp53, BAIAP2L1, BAIAP2L2, and similar proteins. They all contain an Inverse-Bin/Amphiphysin/Rvs (I-BAR) or IMD domain in addition to the SH3 domain. IRSp53, also known as BAIAP2, is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. BAIAP2L1, also called IRTKS (Insulin Receptor Tyrosine Kinase Substrate), serves as a substrate for the insulin receptor and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. IRSp53 and IRTKS also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. The SH3 domains of IRSp53 and IRTKS have been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
PRVKALYPHAAGGETQLSFEEGDVITLLGPEPRDGWHYGENERSGRRGWFPIAYTEP
>gnl|CDD|212714 cd11780, SH3_Sorbs_3, Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains. This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the third SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RYRALYSYTPQNEDELELREGDIVYVMEKCDDGWFVGTSERTGLFGTFPGNYVAR
>gnl|CDD|212715 cd11781, SH3_Sorbs_1, First Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains. This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the first SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KARALYPFKAQSAKELSLKKGDIIYIRRQIDKNWYEGEHNGRVGIFPASYVEI
>gnl|CDD|212716 cd11782, SH3_Sorbs_2, Second Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains. This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the second SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EARAKYNFNADTGVELSFRKGDVITLTRRVDENWYEGRIGGRQGIFPVSYVQV
>gnl|CDD|212717 cd11783, SH3_SH3RF_3, Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains. SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
IYVALYPYKPQKPDELELRKGEMYTVTEKCQDGWFKGTSLRTGQSGVFPGNYVQP
>gnl|CDD|212718 cd11784, SH3_SH3RF2_3, Third Src Homology 3 domain of SH3 domain containing ring finger 2. SH3RF2 is also called POSHER (POSH-eliminating RING protein) or HEPP1 (heart protein phosphatase 1-binding protein). It acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal RING finger domain and three SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
MCVALHSYSAHRPEELELQKGEGVRVLGKFQEGWLRGLSLVTGRVGIFPSNYVSP
>gnl|CDD|212719 cd11785, SH3_SH3RF_C, C-terminal (Fourth) Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains. SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the fourth SH3 domain, located at the C-terminus of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RYRVIVPYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRTGKTGLFPGSFVES
>gnl|CDD|212720 cd11786, SH3_SH3RF_1, First Src Homology 3 domain of SH3 domain containing ring finger proteins. This model represents the first SH3 domain of SH3RF1 (or POSH), SH3RF2 (or POSHER), SH3RF3 (POSH2), and similar domains. Members of this family are scaffold proteins that function as E3 ubiquitin-protein ligases. They all contain an N-terminal RING finger domain and multiple SH3 domains; SH3RF1 and SH3RF3 have four SH3 domains while SH3RF2 has three. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3RF2 acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
CAKALYNYEGKEPGDLSFKKGDIILLRKRIDENWYHGECNGKQGFFPASYVQV
>gnl|CDD|212721 cd11787, SH3_SH3RF_2, Second Src Homology 3 domain of SH3 domain containing ring finger proteins. This model represents the second SH3 domain of SH3RF1 (or POSH), SH3RF2 (or POSHER), SH3RF3 (POSH2), and similar domains. Members of this family are scaffold proteins that function as E3 ubiquitin-protein ligases. They all contain an N-terminal RING finger domain and multiple SH3 domains; SH3RF1 and SH3RF3 have four SH3 domains while SH3RF2 has three. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3RF2 acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QCKALYDFEMKDEDEKDCLTFKKGDVITVIRRVDENWAEGRLGDKIGIFPISF
>gnl|CDD|212722 cd11788, SH3_RasGAP, Src Homology 3 domain of Ras GTPase-Activating Protein 1. RasGAP, also called Ras p21 protein activator, RASA1, or p120RasGAP, is part of the GAP1 family of GTPase-activating proteins. It is a 120kD cytosolic protein containing an SH3 domain flanked by two SH2 domains at the N-terminal end, a pleckstrin homology (PH) domain, a calcium dependent phospholipid binding domain (CaLB/C2), and a C-terminal catalytic GAP domain. It stimulates the GTPase activity of normal RAS p21. It acts as a positive effector of Ras in tumor cells. It also functions as a regulator downstream of tyrosine receptors such as those of PDGF, EGF, ephrin, and insulin, among others. The SH3 domain of RasGAP is unable to bind proline-rich sequences but have been shown to interact with protein partners such as the G3BP protein, Aurora kinases, and the Calpain small subunit 1. The RasGAP SH3 domain is necessary for the downstream signaling of Ras and it also influences Rho-mediated cytoskeletal reorganization. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RRRVRAILPYNKVPDTDELSFQKGDIFVVHNELEDGWLWVTSLRTGESGLVFRDLVEEL
>gnl|CDD|212723 cd11789, SH3_Nebulin_family_C, C-terminal Src Homology 3 domain of the Nebulin family of proteins. Nebulin family proteins contain multiple nebulin repeats, and may contain an N-terminal LIM domain and/or a C-terminal SH3 domain. They have molecular weights ranging from 34 to 900 kD, depending on the number of nebulin repeats, and they all bind actin. They are involved in the regulation of actin filament architecture and function as stabilizers and scaffolds for cytoskeletal structures with which they associate, such as long actin filaments or focal adhesions. Nebulin family proteins that contain a C-terminal SH3 domain include the giant filamentous protein nebulin, nebulette, Lasp1, and Lasp2. Lasp2, also called LIM-nebulette, is an alternatively spliced variant of nebulette. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RYRAMYDYAAADDDEVSFQEGDVIINVEIIDDGWMEGTVQRTGQSGMLPANYVEL
>gnl|CDD|212724 cd11790, SH3_Amphiphysin, Src Homology 3 domain of Amphiphysin and related domains. Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin, and synaptojanin. They function in synaptic vesicle endocytosis. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. Mutations in Bin1 are associated with autosomal recessive centronuclear myopathy. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VLYKVRATHDYTAEDTDELTFEKGDVILVIPFDDPEEQDEGWLMGVKESTGCRGVFPENFTERI
>gnl|CDD|212725 cd11791, SH3_UBASH3, Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing proteins, also called TULA (T cell Ubiquitin LigAnd) family of proteins. UBASH3 or TULA proteins are also referred to as Suppressor of T cell receptor Signaling (STS) proteins. They contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. In some vertebrates, there are two TULA family proteins, called UBASH3A (also called TULA or STS-2) and UBASH3B (also called TULA-2 or STS-1), which show partly overlapping as well as distinct functions. UBASH3B is widely expressed while UBASH3A is only found in lymphoid cells. UBASH3A facilitates apoptosis induced in T cells through its interaction with the apoptosis-inducing factor AIF. UBASH3B is an active phosphatase while UBASH3A is not. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VLRVLYPYTPQEEDELELVPGDYIYVSPEELDSSSDGWVEGTSWLTGCSGLLPENYTEK
>gnl|CDD|212726 cd11792, SH3_Fut8, Src homology 3 domain of Alpha1,6-fucosyltransferase (Fut8). Fut8 catalyzes the alpha1,6-linkage of a fucose residue from a donor substrate to N-linked oligosaccharides on glycoproteins in a process called core fucosylation, which is crucial for growth factor receptor-mediated biological functions. Fut8-deficient mice show severe growth retardation, early death, and a pulmonary emphysema-like phenotype. Fut8 is also implicated to play roles in aging and cancer metastasis. It contains an N-terminal coiled-coil domain, a catalytic domain, and a C-terminal SH3 domain. The SH3 domain of Fut8 is located in the lumen and its role in glycosyl transfer is unclear. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
NQVAIYPHKPRNHDEIELRVGDIIGVAGNHWDGYSKGRNRRTGKTGLYPSYKVKD
>gnl|CDD|212727 cd11793, SH3_ephexin1_like, Src homology 3 domain of ephexin-1-like SH3 domain containing Rho guanine nucleotide exchange factors. Members of this family contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and C-terminal SH3 domains. They include the Rho guanine nucleotide exchange factors ARHGEF5, ARHGEF16, ARHGEF19, ARHGEF26, ARHGEF27 (also called ephexin-1), and similar proteins, and are also called ephexins because they interact directly with ephrin A receptors. GEFs interact with Rho GTPases via their DH domains to catalyze nucleotide exchange by stabilizing the nucleotide-free GTPase intermediate. They play important roles in neuronal development. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QVQCVHAYTAQQPDELTLEEGDVVNVLRKMPDGWYEGERLRDGERGWFPSSYTEE
>gnl|CDD|212728 cd11794, SH3_DNMBP_N1, First N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba. DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin and key regulatory proteins of the actin cytoskeleton. It plays an important role in regulating cell junction configuration. The four N-terminal SH3 domains of DNMBP binds the GTPase dynamin, which plays an important role in the fission of endocytic vesicles. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VVRAIFDFCPSVSEELPLFAGDVIEVLKVVDEFWLLGTKEGVTGQFPSSFV
>gnl|CDD|212729 cd11795, SH3_DNMBP_N2, Second N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba. DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin and key regulatory proteins of the actin cytoskeleton. It plays an important role in regulating cell junction configuration. The four N-terminal SH3 domains of DNMBP binds the GTPase dynamin, which plays an important role in the fission of endocytic vesicles. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LVVCIEAFTSQEPGHLNLQRGDLVELTGTTDSGWLQGRSCWGSSGFFPSSCVQE
>gnl|CDD|212730 cd11796, SH3_DNMBP_N3, Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba. DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin and key regulatory proteins of the actin cytoskeleton. It plays an important role in regulating cell junction configuration. The four N-terminal SH3 domains of DNMBP binds the GTPase dynamin, which plays an important role in the fission of endocytic vesicles. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QARVLQDLSAQLDEELDLREGDVVTITGILDKGWFRGELNGRRGIFPEGFV
>gnl|CDD|212731 cd11797, SH3_DNMBP_N4, Fourth N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba. DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin and key regulatory proteins of the actin cytoskeleton. It plays an important role in regulating cell junction configuration. The four N-terminal SH3 domains of DNMBP bind the GTPase dynamin, which plays an important role in the fission of endocytic vesicles. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YGVALYRFQALEPNELDFEVGDRIRIIATLEDGWLEGELKGRRGIFPHRF
>gnl|CDD|212732 cd11798, SH3_DNMBP_C1, First C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba. DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. The C-terminal SH3 domains of DNMBP bind to N-WASP and Ena/VASP proteins, which are key regulatory proteins of the actin cytoskeleton. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LFQADRNFNAAQDLDVSLQEGDLVGVIKQQDPMGSQNRWLIDNGVTKGFVYSSFLKP
>gnl|CDD|212733 cd11799, SH3_ARHGEF37_C1, First C-terminal Src homology 3 domain of Rho guanine nucleotide exchange factor 37. ARHGEF37 contains a RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. Its specific function is unknown. Its domain architecture is similar to the C-terminal half of DNMBP or Tuba, a cdc42-specific GEF that provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics, and plays an important role in regulating cell junction configuration. GEFs activate small GTPases by exchanging bound GDP for free GTP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
IYQVMSNVSGTRDLDLTLTRGEIVAVLQEADTKGNTGRWLVDAGGKRGYVPASK
>gnl|CDD|212734 cd11800, SH3_DNMBP_C2_like, Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and similar domains. DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. The C-terminal SH3 domains of DNMBP bind to N-WASP and Ena/VASP proteins, which are key regulatory proteins of the actin cytoskeleton. Also included in this subfamily is the second C-terminal SH3 domain of Rho guanine nucleotide exchange factor 37 (ARHGEF37), whose function is still unknown. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YYYALYTFEARSPGELSVTEGQVVTVLEKHDLKGNPEWWLVEDRGKQGYVPSNYLAK
>gnl|CDD|212735 cd11801, SH3_JIP1_like, Src homology 3 domain of JNK-interacting proteins 1 and 2, and similar domains. JNK-interacting proteins (JIPs) function as scaffolding proteins for c-Jun N-terminal kinase (JNK) signaling pathways. They bind to components of Mitogen-activated protein kinase (MAPK) pathways such as JNK, MKK, and several MAP3Ks such as MLK and DLK. There are four JIPs (JIP1-4); all contain a JNK binding domain. JIP1 and JIP2 also contain SH3 and Phosphotyrosine-binding (PTB) domains. Both are highly expressed in the brain and pancreatic beta-cells. JIP1 functions as an adaptor linking motor to cargo during axonal transport and also is involved in regulating insulin secretion. JIP2 form complexes with fibroblast growth factor homologous factors (FHFs), which facilitates activation of the p38delta MAPK. The SH3 domain of JIP1 homodimerizes at the interface usually involved in proline-rich ligand recognition, despite the lack of this motif in the domain itself. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
THRALHKFIPRHEDEIELDIGDPVYVEQEADDLWCEGTNLRTGQRGIFPAAYVVE
>gnl|CDD|212736 cd11802, SH3_Endophilin_B, Src homology 3 domain of Endophilin-B. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They are classified into two types, A and B. Vertebrates contain two endophilin-B isoforms. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KARVLYDYDAEDSTELSLLADEVITVYELPGMDEDYMMGERGSQRGKVPVAY
>gnl|CDD|212737 cd11803, SH3_Endophilin_A, Src homology 3 domain of Endophilin-A. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms (A1, A2, and A3). Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
PCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMVNGQSGFFPVNYVEVL
>gnl|CDD|212738 cd11804, SH3_GRB2_like_N, N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins. This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The N-terminal SH3 domain of GRB2 binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EAVAKHDFKATAEDELSFKKGSILKVLNMEDDPNWYKAELDGKEGLIPKNYI
>gnl|CDD|212739 cd11805, SH3_GRB2_like_C, C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins. This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The C-terminal SH3 domains (SH3c) of GRB2 and GRAP2 have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RVQALYDFNPQEPGELEFRRGDIITVLDSSDPDWWKGELRGRVGIFPANYVQP
>gnl|CDD|212740 cd11806, SH3_PRMT2, Src homology 3 domain of Protein arginine N-methyltransferase 2. PRMT2, also called HRMT1L1, belongs to the arginine methyltransferase protein family. It functions as a coactivator to both estrogen receptor alpha (ER-alpha) and androgen receptor (AR), presumably through arginine methylation. The ER-alpha transcription factor is involved in cell proliferation, differentiation, morphogenesis, and apoptosis, and is also implicated in the development and progression of breast cancer. PRMT2 and its variants are upregulated in breast cancer cells and may be involved in modulating the ER-alpha signaling pathway during formation of breast cancer. PRMT2 also plays a role in regulating the function of E2F transcription factors, which are critical cell cycle regulators, by binding to the retinoblastoma gene product (RB). It contains an N-terminal SH3 domain and an AdoMet binding domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EYVAIADFVATDDSQLSFESGDKLLVLRKPSVDWWWAEHNGCCGYIPASHLHQ
>gnl|CDD|212741 cd11807, SH3_ASPP, Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP). The ASPP family of proteins bind to important regulators of apoptosis (p53, Bcl-2, and RelA) and cell growth (APCL, PP1). They share similarity at their C-termini, where they harbor a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain. Vertebrates contain three members of the family: ASPP1, ASPP2, and iASPP. ASPP1 and ASPP2 activate the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73), while iASPP is an oncoprotein that specifically inhibits p53-induced apoptosis. The expression of ASPP proteins is altered in tumors; ASPP1 and ASPP2 are downregulated whereas iASPP is upregulated is some cancer types. ASPP proteins also bind and regulate protein phosphatase 1 (PP1), and this binding is competitive with p53 binding. The SH3 domain and the ANK repeats of ASPP contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GVVYALFDYEAENGDELSFREGDELTVLRKGDDDETEWWWARLNDKEGYVPRNLLGL
>gnl|CDD|212742 cd11808, SH3_Alpha_Spectrin, Src homology 3 domain of Alpha Spectrin. Spectrin is a major structural component of the red blood cell membrane skeleton and is important in erythropoiesis and membrane biogenesis. It is a flexible, rope-like molecule composed of two subunits, alpha and beta, which consist of many spectrin-type repeats. Alpha and beta spectrin associate to form heterodimers and tetramers; spectrin tetramer formation is critical for red cell shape and deformability. Defects in alpha spectrin have been associated with inherited hemolytic anemias including hereditary spherocytosis (HSp), hereditary elliptocytosis (HE), and hereditary pyropoikilocytosis (HPP). Alpha spectrin contains a middle SH3 domain and a C-terminal EF-hand binding motif in addition to multiple spectrin repeats. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
CVVALYDYQEKSPREVSMKKGDILTLLNSSNKDWWKVEVNDRQGFVPAAYVKK
>gnl|CDD|212743 cd11809, SH3_srGAP, Src homology 3 domain of Slit-Robo GTPase Activating Proteins. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs (srGAP1-3), all of which are expressed during embryonic and early development in the nervous system but with different localization and timing. A fourth member has also been reported (srGAP4, also called ARHGAP4). srGAPs contain an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EATAQFDYTGRSERELSFKKGDSLTLYRQVSDDWWRGQLNGQDGLVPHKYITL
>gnl|CDD|212744 cd11810, SH3_RUSC1_like, Src homology 3 domain of RUN and SH3 domain-containing proteins 1 and 2. RUSC1 and RUSC2, that were originally characterized in silico. They are adaptor proteins consisting of RUN, leucine zipper, and SH3 domains. RUSC1, also called NESCA (New molecule containing SH3 at the carboxy-terminus), is highly expressed in the brain and is translocated to the nuclear membrane from the cytoplasm upon stimulation with neurotrophin. It plays a role in facilitating neurotrophin-dependent neurite outgrowth. It also interacts with NEMO (or IKKgamma) and may function in NEMO-mediated activation of NF-kB. RUSC2, also called Iporin, is expressed ubiquitously with highest amounts in the brain and testis. It interacts with the small GTPase Rab1 and the Golgi matrix protein GM130, and may function in linking GTPases to certain intracellular signaling pathways. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VVRALCHHVATDSGQLSFRKGDILRVIARVDDDWLLCTRGSTKGLVPLSY
>gnl|CDD|212745 cd11811, SH3_CHK, Src Homology 3 domain of CSK homologous kinase. CHK is also referred to as megakaryocyte-associated tyrosine kinase (Matk). It inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. To inhibit Src kinases that are anchored to the plasma membrane, CHK is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. CHK also plays a role in neural differentiation in a manner independent of Src by enhancing MAPK activation via Ras-mediated signaling. It is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GTQCVTKKDHTKPKPGELAFHKGDIVTIVETCERKGWYRARHNTSGEEGLVAAGALRER
>gnl|CDD|212746 cd11812, SH3_AHI-1, Src Homology 3 domain of Abelson helper integration site-1 (AHI-1). AHI-1, also called Jouberin, is expressed in high levels in the brain, gonad tissues, and skeletal muscle. It is an adaptor protein that interacts with the small GTPase Rab8a and regulates it distribution and function, affecting cilium formation and vesicle transport. Mutations in the AHI-1 gene can cause Joubert syndrome, a disorder characterized by brainstem malformations, cerebellar aplasia/hypoplasia, and retinal dystrophy. AHI-1 variation is also associated with susceptibility to schizophrenia and type 2 diabetes mellitus progression. AHI-1 contains WD40 and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TVVALYDYTANRSDELTIHRGDIIRVLYKDNDNWWFGSLVNGQQGYFPANYV
>gnl|CDD|212747 cd11813, SH3_SGSM3, Src Homology 3 domain of Small G protein Signaling Modulator 3. SGSM3 is also called Merlin-associated protein (MAP), RUN and SH3 domain-containing protein (RUSC3), RUN and TBC1 domain-containing protein 3 (RUTBC3), Rab GTPase-activating protein 5 (RabGAP5), or Rab GAP-like protein (RabGAPLP). It is expressed ubiquitously and functions as a regulator of small G protein RAP- and RAB-mediated neuronal signaling. It is involved in modulating NGF-mediated neurite outgrowth and differentiation. It also interacts with the tumor suppressor merlin and may play a role in the merlin-associated suppression of cell growth. SGSM3 contains TBC, SH3, and RUN domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RAKALLDFERHDDDELGFRKNDIITIISQKDEHCWVGELNGLRGWFPAKFVEL
>gnl|CDD|212748 cd11814, SH3_Eve1_1, First Src homology 3 domain of ADAM-binding protein Eve-1. Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
HGIAKEDCVSRNPGELSCKRGDVLVMLQQKDNNYLECQKGGETGKVPPSH
>gnl|CDD|212749 cd11815, SH3_Eve1_2, Second Src homology 3 domain of ADAM-binding protein Eve-1. Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
HAVVLHDFPAEHSDDLSLNSGEIVYLLEKIDTEWYRGKCKNTTGIFPANHVK
>gnl|CDD|212750 cd11816, SH3_Eve1_3, Third Src homology 3 domain of ADAM-binding protein Eve-1. Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RCVARFDFEGEQEDELSFSEGDVITLKEYVGEEWAKGELNGKIGIFPLNFV
>gnl|CDD|212751 cd11817, SH3_Eve1_4, Fourth Src homology 3 domain of ADAM-binding protein Eve-1. Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
WAVALYDFTGETEEDLSFQRGDRILVTEHLDAEWSRGRLNGREGIFPRAF
>gnl|CDD|212752 cd11818, SH3_Eve1_5, Fifth Src homology 3 domain of ADAM-binding protein Eve-1. Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KARALYDFTGENEDELSFKAGDIITELESIDEEWMSGELRGKSGIFPKNF
>gnl|CDD|212753 cd11819, SH3_Cortactin_like, Src homology 3 domain of Cortactin and related proteins. This subfamily includes cortactin, Abp1 (actin-binding protein 1), hematopoietic lineage cell-specific protein 1 (HS1), and similar proteins. These proteins are involved in regulating actin dynamics through direct or indirect interaction with the Arp2/3 complex, which is required to initiate actin polymerization. They all contain at least one C-terminal SH3 domain. Cortactin and HS1 bind Arp2/3 and actin through an N-terminal region that contains an acidic domain and several copies of a repeat domain found in cortactin and HS1. Abp1 binds actin via an N-terminal actin-depolymerizing factor (ADF) homology domain. Yeast Abp1 binds Arp2/3 directly through two acidic domains. Mammalian Abp1 does not directly interact with Arp2/3; instead, it regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. The C-terminal region of these proteins acts as an adaptor or scaffold that can connect membrane trafficking and signaling proteins that bind the SH3 domain within the actin network. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RAKALYDYQAAEDNEISFVEGDIITQIEQIDEGWWLGVNAKGQKGLFPANYVEL
>gnl|CDD|212754 cd11820, SH3_STAM, Src homology 3 domain of Signal Transducing Adaptor Molecules. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. There are two vertebrate STAMs, STAM1 and STAM2, which may be functionally redundant; vertebrate STAMs contain ITAM motifs. They are part of the endosomal sorting complex required for transport (ESCRT-0). STAM2 deficiency in mice did not cause any obvious abnormality, while STAM1 deficiency resulted in growth retardation. Loss of both STAM1 and STAM2 in mice proved lethal, indicating that STAMs are important for embryonic development. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RKVRALYDFEAAEDNELTFKAGEIITVLDDSDPNWWKGSNHRGEGLFPANFVTA
>gnl|CDD|212755 cd11821, SH3_ASAP, Src homology 3 domain of ArfGAP with SH3 domain, ankyrin repeat and PH domain containing proteins. ASAPs are Arf GTPase activating proteins (GAPs) and they function in regulating cell growth, migration, and invasion. They contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. Vertebrates contain at least three members, ASAP1, ASAP2, and ASAP3, but some ASAP3 proteins do not seem to harbor a C-terminal SH3 domain. ASAP1 and ASAP2 show GTPase activating protein (GAP) activity towards Arf1 and Arf5. They do not show GAP activity towards Arf6, but are able to mediate Arf6 signaling by binding stably to GTP-Arf6. ASAP3 is an Arf6-specific GAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RVRALYDCQADNDDELTFSEGEIIVVTGEEDDEWWEGHIEGDPSRRGVFPVSF
>gnl|CDD|212756 cd11822, SH3_SASH_like, Src homology 3 domain of SAM And SH3 Domain Containing Proteins. This subfamily, also called the SLY family, is composed of SAM And SH3 Domain Containing Protein 1 (SASH1), SASH2, SASH3, and similar proteins. These are adaptor proteins containing a central conserved region with a bipartite nuclear localization signal (NLS) as wells as SAM (sterile alpha motif) and SH3 domains. SASH1 is a potential tumor suppressor in breast and colon cancer. It is widely expressed in normal tissues (except lymphocytes and dendritic cells) and is localized in the nucleus and the cytoplasm. SASH1 interacts with the oncoprotein cortactin and is important in cell migration and adhesion. SASH2 (also called SAMSN-1, SLY2, HACS1 or NASH1) and SASH3 (also called SLY/SLY1) are expressed mainly in hematopoietic cells, although SASH2 is also found in endothelial cells as well as myeloid leukemias and myeloma. SASH2 was found to be differentially expressed in malignant haematopoietic cells and in colorectal tumors, and is a potential tumor suppressor in lung cancer. SASH3 is essential in the full activation of adaptive immunity and is involved in the signaling of T cell receptors. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RAKVHTDFTPSPYDTDSLKLKKGDIIDIINKPPMGIWTGMLNNKVGNFKFIY
>gnl|CDD|212757 cd11823, SH3_Nostrin, Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer. Nostrin is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). It facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of Nostrin may be correlated to preeclampsia. Nostrin contains an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RCKALYSYTANREDELSLQPGDIIEVHEKQDDGWWLGELNGKKGIFPATYVEE
>gnl|CDD|212758 cd11824, SH3_PSTPIP1, Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1. PSTPIP1, also called CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KYSVLYDYTAQEDDELSISKGDVVAVIEKGEDGWWTVERNGQKGLVPGTYLEK
>gnl|CDD|212759 cd11825, SH3_PLCgamma, Src homology 3 domain of Phospholipase C (PLC) gamma. PLC catalyzes the hydrolysis of phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5)P2] to produce Ins(1,4,5)P3 and diacylglycerol (DAG) in response to various receptors. Ins(1,4,5)P3 initiates the calcium signaling cascade while DAG functions as an activator of PKC. PLCgamma catalyzes this reaction in tyrosine kinase-dependent signaling pathways. It is activated and recruited to its substrate at the membrane. Vertebrates contain two forms of PLCgamma, PLCgamma1, which is widely expressed, and PLCgamma2, which is primarily found in haematopoietic cells. PLCgamma contains a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, two catalytic regions of PLC domains that flank two tandem SH2 domains, followed by a SH3 domain and C2 domain. The SH3 domain of PLCgamma1 directly interacts with dynamin-1 and can serve as a guanine nucleotide exchange factor (GEF). It also interacts with Cbl, inhibiting its phosphorylation and activity. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TVKALYDYRAQRPDELSFCKHAIITNVEKEDGGWWRGDYGGKKQKWFPANYVEE
>gnl|CDD|212760 cd11826, SH3_Abi, Src homology 3 domain of Abl Interactor proteins. Abl interactor (Abi) proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. They localize to sites of actin polymerization in epithelial adherens junction and immune synapses, as well as to the leading edge of lamellipodia. Vertebrates contain two Abi proteins, Abi1 and Abi2. Abi1 displays a wide expression pattern while Abi2 is highly expressed in the eye and brain. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KVVALYDYTADKDDELSFQEGDIIYVTKKNDDGWYEGVLNGVTGLFPGNYVE
>gnl|CDD|212761 cd11827, SH3_MyoIe_If_like, Src homology 3 domain of Myosins Ie, If, and similar proteins. Myosins Ie (MyoIe) and If (MyoIf) are nonmuscle, unconventional, long tailed, class I myosins containing an N-terminal motor domain and a myosin tail with TH1, TH2, and SH3 domains. MyoIe interacts with the endocytic proteins, dynamin and synaptojanin-1, through its SH3 domain; it may play a role in clathrin-dependent endocytosis. In the kidney, MyoIe is critical for podocyte function and normal glomerular filtration. Mutations in MyoIe is associated with focal segmental glomerulosclerosis, a disease characterized by massive proteinuria and progression to end-stage kidney disease. MyoIf is predominantly expressed in the immune system; it plays a role in immune cell motility and innate immunity. Mutations in MyoIf may be associated with the loss of hearing. The MyoIf gene has also been found to be fused to the MLL (Mixed lineage leukemia) gene in infant acute myeloid leukemias (AML). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QCKALYAYDAQDTDELSFNEGDIIEILKEDPSGWWTGRLRGKEGLFPGNYVEK
>gnl|CDD|212762 cd11828, SH3_ARHGEF9_like, Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors. Members of this family contain a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. They include the Rho guanine nucleotide exchange factors ARHGEF9, ASEF (also called ARHGEF4), ASEF2, and similar proteins. GEFs activate small GTPases by exchanging bound GDP for free GTP. ARHGEF9 specifically activates Cdc42, while both ASEF and ASEF2 can activate Rac1 and Cdc42. ARHGEF9 is highly expressed in the brain and it interacts with gephyrin, a postsynaptic protein associated with GABA and glycine receptors. ASEF plays a role in angiogenesis and cell migration. ASEF2 is important in cell migration and adhesion dynamics. ASEF exists in an autoinhibited form and is activated upon binding of the tumor suppressor APC (adenomatous polyposis coli), leading to the activation of Rac1 or Cdc42. In its autoinhibited form, the SH3 domain of ASEF forms an extensive interface with the DH and PH domains, blocking the Rac binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LAEALWDHVTMDPEELGFKAGDVIEVLDMSDKDWWWGSIRDEEGWFPASFVRL
>gnl|CDD|212763 cd11829, SH3_GAS7, Src homology 3 domain of Growth Arrest Specific protein 7. GAS7 is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LCRTLYAFTGEQHQQGLSFEAGELIRVLQAPDGGWWEGEKDGLRGWFPASYV
>gnl|CDD|212764 cd11830, SH3_VAV_2, C-terminal (or second) Src homology 3 domain of VAV proteins. VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and scaffold proteins and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TAKARYDFCARDMRELSLKEGDVVKIYNKKGQQGWWRGEINGRIGWFPSTYVEE
>gnl|CDD|212765 cd11831, SH3_VAV_1, First Src homology 3 domain of VAV proteins. VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and scaffold proteins and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KMVVMQNYHGNPPPPGAGGPVLTLQTGDVVELLKGDAESPWWEGRNVATREVGYFPSSSVKP
>gnl|CDD|212766 cd11832, SH3_Shank, Src homology 3 domain of SH3 and multiple ankyrin repeat domains (Shank) proteins. Shank proteins carry scaffolding functions through multiple sites of protein-protein interaction in its domain architecture, including ankyrin (ANK) repeats, a long proline rich region, as well as SH3, PDZ, and SAM domains. They bind a variety of membrane and cytosolic proteins, and exist in alternatively spliced isoforms. They are highly enriched in postsynaptic density (PSD) where they interact with the cytoskeleton and with postsynaptic membrane receptors including NMDA and glutamate receptors. They are crucial in the construction and organization of the PSD and dendritic spines of excitatory synapses. There are three members of this family (Shank1, Shank2, Shank3) which show distinct and cell-type specific patterns of expression. Shank1 is brain-specific; Shank2 is found in neurons, glia, endocrine cells, liver, and kidney; Shank3 is widely expressed. The SH3 domain of Shank binds GRIP, a scaffold protein that binds AMPA receptors and Eph receptors/ligands. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YFIAVKSYSPQEEGEISLHKGDRVKVLSIGEGGFWEGSVRGRTGWFPSDC
>gnl|CDD|212767 cd11833, SH3_Stac_1, First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) proteins. Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. This model represents the first C-terminal SH3 domain of Stac1 and Stac3, and the single C-terminal SH3 domain of Stac2. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TYVALYKFKPQENEDLEMRPGDKITLLDDSNEDWWKGKIEDRVGFFPANFVQR
>gnl|CDD|212768 cd11834, SH3_Stac_2, Second C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing proteins 1 and 3. This model represents the second C-terminal SH3 domain of Stac1 and Stac3. Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VHRVTRSFVGNKEIGQITLKKDQIVVQKGEEQNGYIKVYTGRKVGLFPLDF
>gnl|CDD|212769 cd11835, SH3_ARHGAP32_33, Src homology 3 domain of Rho GTPase-activating proteins 32 and 33, and similar proteins. Members of this family contain N-terminal PX and Src Homology 3 (SH3) domains, a central Rho GAP domain, and C-terminal extensions. RhoGAPs (or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP32 is also called RICS, PX-RICS, p250GAP, or p200RhoGAP. It is a Rho GTPase-activating protein for Cdc42 and Rac1, and is implicated in the regulation of postsynaptic signaling and neurite outgrowth. PX-RICS, a variant of RICS that contain PX and SH3 domains, is the main isoform expressed during neural development. It is involved in neural functions including axon and dendrite extension, postnatal remodeling, and fine-tuning of neural circuits during early brain development. ARHGAP33, also called sorting nexin 26 or TCGAP (Tc10/CDC42 GTPase-activating protein), is widely expressed in the brain where it is involved in regulating the outgrowth of axons and dendrites and is regulated by the protein tyrosine kinase Fyn. It is translocated to the plasma membrane in adipocytes in response to insulin and may be involved in the regulation of insulin-stimulated glucose transport. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
AAHVIKRYTAQAPDELSLEVGDIVSVIDMPPPEESTWWRGKKGFQVGFFPSECV
>gnl|CDD|212770 cd11836, SH3_Intersectin_1, First Src homology 3 domain (or SH3A) of Intersectin. Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KYRALYAFEARNPDEISFQPGDIIQVDESQVAEPGWLAGELKGKTGWFPANYVEK
>gnl|CDD|212771 cd11837, SH3_Intersectin_2, Second Src homology 3 domain (or SH3B) of Intersectin. Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The second SH3 domain (or SH3B) of ITSN1 has been shown to bind WNK and CdGAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TATALYPWRAKKENHLSFAKGDIITVLEQQEMWWFGELEGGEEGWFPKSYVKE
>gnl|CDD|212772 cd11838, SH3_Intersectin_3, Third Src homology 3 domain (or SH3C) of Intersectin. Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The third SH3 domain (or SH3C) of ITSN1 has been shown to bind many proteins including dynamin1/2, CIN85, c-Cbl, SHIP2, Reps1, synaptojanin-1, and WNK, among others. The SH3C of ITSN2 has been shown to bind the K15 protein of Kaposi's sarcoma-associated herpesvirus. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EYIALYPYESNEPGDLTFNAGDVILVTKKDGEWWTGTIGDRTGIFPSNYVRP
>gnl|CDD|212773 cd11839, SH3_Intersectin_4, Fourth Src homology 3 domain (or SH3D) of Intersectin. Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The fourth SH3 domain (or SH3D) of ITSN1 has been shown to bind SHIP2, Numb, CdGAP, and N-WASP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
IAQVIAPFTATAENQLSLAVGQLVLVRKKSPSGWWEGELQARGKKRQIGWFPANYVKL
>gnl|CDD|212774 cd11840, SH3_Intersectin_5, Fifth Src homology 3 domain (or SH3E) of Intersectin. Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QVIALFPYTAQNEDELSFQKGDIINVLSKDDPDWWRGELNGQTGLFPSNYVEP
>gnl|CDD|212775 cd11841, SH3_SH3YL1_like, Src homology 3 domain of SH3 domain containing Ysc84-like 1 (SH3YL1) protein. SH3YL1 localizes to the plasma membrane and is required for dorsal ruffle formation. It binds phosphoinositides (PIs) with high affinity through its N-terminal SYLF domain (also called DUF500). In addition, SH3YL1 contains a C-terminal SH3 domain which has been reported to bind to N-WASP, dynamin 2, and SHIP2 (a PI 5-phosphatase). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EVTALYSFEGQQPCDLSFQAGDRITVLTRTDSQFDWWEGRLRGRVGIFPANYVS
>gnl|CDD|212776 cd11842, SH3_Ysc84p_like, Src homology 3 domain of Ysc84p and similar fungal proteins. This family is composed of the Saccharomyces cerevisiae proteins, Ysc84p (also called LAS17-binding protein 4, Lsb4p) and Lsb3p, and similar fungal proteins. They contain an N-terminal SYLF domain (also called DUF500) and a C-terminal SH3 domain. Ysc84p localizes to actin patches and plays an important in actin polymerization during endocytosis. The N-terminal domain of both Ysc84p and Lsb3p can bind and bundle actin filaments. A study of the yeast SH3 domain interactome predicts that the SH3 domains of Lsb3p and Lsb4p may function as molecular hubs for the assembly of endocytic complexes. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KAVALYDFAGEQPGDLAFQKGDIITILKKSDSQNDWWTGRIGGREGIFPANYVEL
>gnl|CDD|212777 cd11843, SH3_PACSIN, Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins. PACSINs, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
PVRALYDYEGQESDELSFKAGDILTKLEEEDEQGWCKGRLDGRVGLYPANYVE
>gnl|CDD|212778 cd11844, SH3_CAS, Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding proteins. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes including migration, chemotaxis, apoptosis, differentiation, and progenitor cell function. They mediate the signaling of integrins at focal adhesions where they localize, and thus, regulate cell invasion and survival. Over-expression of these proteins is implicated in poor prognosis, increased metastasis, and resistance to chemotherapeutics in many cancers such as breast, lung, melanoma, and glioblastoma. CAS proteins have also been linked to the pathogenesis of inflammatory disorders, Alzheimer's, Parkinson's, and developmental defects. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. Vertebrates contain four CAS proteins: BCAR1 (or p130Cas), NEDD9 (or HEF1), EFS (or SIN), and CASS4 (or HEPL). The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LARALYDNVAESPDELAFRRGDILTVLEQNTAGLEGWWLCSLRGRQGIAPGNRLKL
>gnl|CDD|212779 cd11845, SH3_Src_like, Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
IYVALYDYEARTDDDLSFKKGDRLQILDDSDGDWWLARHLSTGKEGYIPSNY
>gnl|CDD|212780 cd11846, SH3_Srms, Src homology 3 domain of Srms Protein Tyrosine Kinase. Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristoylation sites (Srms) is a cytoplasmic (or non-receptor) PTK with limited homology to Src kinases. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Srms lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LFTALYDFTARSTHELSVEQGDKLCVIEEEGDYIFARKLTGNPESGLVPASYVAQ
>gnl|CDD|212781 cd11847, SH3_Brk, Src homology 3 domain of Brk (Breast tumor kinase) Protein Tyrosine Kinase (PTK), also called PTK6. Brk is a cytoplasmic (or non-receptor) PTK with limited homology to Src kinases. It has been found to be overexpressed in a majority of breast tumors. It plays roles in normal cell differentiation, proliferation, survival, migration, and cell cycle progression. Brk substrates include RNA-binding proteins (SLM-1/2, Sam68), transcription factors (STAT3/5), and signaling molecules (Akt, paxillin, IRS-4). Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation site. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
IYKALWDFKARGDEELSFQAGDQFRIAERSGDWWTALKLDRAGGVVAQGFVPNNYLAR
>gnl|CDD|212782 cd11848, SH3_SLAP-like, Src homology 3 domain of Src-Like Adaptor Proteins. SLAPs are adaptor proteins with limited similarity to Src family tyrosine kinases. They contain an N-terminal SH3 domain followed by an SH2 domain, and a unique C-terminal sequence. They function in regulating the signaling, ubiquitination, and trafficking of T-cell receptor (TCR) and B-cell receptor (BCR) components. Vertebrates contain two SLAPs, named SLAP (or SLA1) and SLAP2 (or SLA2). SLAP has been shown to interact with the EphA receptor, EpoR, Lck, PDGFR, Syk, CD79a, among others, while SLAP2 interacts with CSF1R. Both SLAPs interact with c-Cbl, LAT, CD247, and Zap70. SLAP modulates TCR surface expression levels as well as surface and total BCR levels. As an adaptor to c-Cbl, SLAP increases the ubiquitination, intracellular retention, and targeted degradation of the BCR complex components. SLAP2 plays a role in c-Cbl-dependent regulation of CSF1R, a tyrosine kinase important for myeloid cell growth and differentiation. The SH3 domain of SLAP forms a complex with v-Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TLVALGDYPSGGPAELSLRLGEPLTIVSDEGDWWKVLSEVTGRESYIPSVHVAKV
>gnl|CDD|212783 cd11849, SH3_SPIN90, Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90). SPIN90 is also called NCK interacting protein with SH3 domain (NCKIPSD), Dia-interacting protein (DIP), 54 kDa vimentin-interacting protein (VIP54), or WASP-interacting SH3-domain protein (WISH). It is an F-actin binding protein that regulates actin polymerization and endocytosis. It associates with the Arp2/3 complex near actin filaments and determines filament localization at the leading edge of lamellipodia. SPIN90 is expressed in the early stages of neuronal differentiation and plays a role in regulating growth cone dynamics and neurite outgrowth. It also interacts with IRSp53 and regulates cell motility by playing a role in the formation of membrane protrusions. SPIN90 contains an N-terminal SH3 domain, a proline-rich domain, and a C-terminal VCA (verprolin-homology and cofilin-like acidic) domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
MYRALYDFKSAEPNTLSFSEGETFLLLERSNAHWWLVTNHSGETGYVPANYVK
>gnl|CDD|212784 cd11850, SH3_Abl, Src homology 3 domain of the Protein Tyrosine Kinase, Abelson kinase. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LFVALYDFVASGENQLSIKKGEQLRVLGYNKNGEWCEAESKSTGGQGWVPSNYITP
>gnl|CDD|212785 cd11851, SH3_RIM-BP, Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins. RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LMVALYDYNPETMSPNDDPEEELSFHAGDVVRVYGPMDEDGFYYGELEGGRKGLVPSNFVQE
>gnl|CDD|212786 cd11852, SH3_Kalirin_1, First Src homology 3 domain of the RhoGEF kinase, Kalirin. Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
ELTVVIEDFEATSSQELTVSKGQTVEVLERPSSRPDWCLVRTLEQDNSPPQEGLVPSSILCI
>gnl|CDD|212787 cd11853, SH3_Kalirin_2, Second Src homology 3 domain of the RhoGEF kinase, Kalirin. Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TMPVIQDYYALKEDEICVSQGEVVQILAANQQNMFLVYRPATDQSPAAEGWIPGSVLGH
>gnl|CDD|212788 cd11854, SH3_Fus1p, Src homology 3 domain of yeast cell fusion protein Fus1p. Fus1p is required at the cell surface for cell fusion during the mating response in yeast. It requires Bch1p and Bud7p, which are Chs5p-Arf1p binding proteins, for localization to the plasma membrane. It acts as a scaffold protein to assemble a cell surface complex which is involved in septum degradation and inhibition of the NOG pathway to promote cell fusion. The SH3 domain of Fus1p interacts with Bin1p, a formin that controls the assembly of actin cables in response to Cdc42 signaling. It has been shown to bind the motif, R(S/T)(S/T)SL, instead of PxxP motifs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LMTVISTFEPSLDDELLIKVGETVRVLAEYDDGWCLVERADGLNGDRGMVPGECLQ
>gnl|CDD|212789 cd11855, SH3_Sho1p, Src homology 3 domain of High osmolarity signaling protein Sho1p. Sho1p (or Sho1), also called SSU81 (Suppressor of SUA8-1 mutation), is a yeast membrane protein that regulates adaptation to high salt conditions by activating the HOG (high-osmolarity glycerol) pathway. High salt concentrations lead to the localization to the membrane of the MAPKK Pbs2, which is then activated by the MAPKK Ste11 and in turn, activates the MAPK Hog1. Pbs2 is localized to the membrane though the interaction of its PxxP motif with the SH3 domain of Sho1p. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RARALYPYDASPDDPNELSFEKGEILEVSDTSGKWWQARKSNGETGICPSNYLQL
>gnl|CDD|212790 cd11856, SH3_p47phox_like, Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains. This family is composed of the tandem SH3 domains of p47phox subunit of NADPH oxidase and Nox Organizing protein 1 (NoxO1), the four SH3 domains of Tks4 (Tyr kinase substrate with four SH3 domains), the five SH3 domains of Tks5, the SH3 domain of obscurin, Myosin-I, and similar domains. Most members of this group also contain Phox homology (PX) domains, except for obscurin and Myosin-I. p47phox and NoxO1 are regulators of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) and nonphagocytic NADPH oxidase Nox1, respectively. They play roles in the activation of their respective NADPH oxidase, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Obscurin is a giant muscle protein that plays important roles in the organization and assembly of the myofibril and the sarcoplasmic reticulum. Type I myosins (Myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
SYVAIADYEAQGDDEISLQEGEVVEVLEKNDSGWWYVRKGDKEGWVPASYLEP
>gnl|CDD|212791 cd11857, SH3_DBS, Src homology 3 domain of DBL's Big Sister (DBS), a guanine nucleotide exchange factor. DBS, also called MCF2L (MCF2-transforming sequence-like protein) or OST, is a Rho GTPase guanine nucleotide exchange factor (RhoGEF), facilitating the exchange of GDP and GTP. It was originally isolated from a cDNA screen for sequences that cause malignant growth. It plays roles in regulating clathrin-mediated endocytosis and cell migration through its activation of Rac1 and Cdc42. Depending on cell type, DBS can also activate RhoA and RhoG. DBS contains a Sec14-like domain, spectrin-like repeats, a RhoGEF [or Dbl homology (DH)] domain, a Pleckstrin homology (PH) domain, and an SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KYTVVADYEKGGPDDLTVKSGDLVQLIHEGDEGQWLVKNLSTRKEGWVPAANLQP
>gnl|CDD|212792 cd11858, SH3_Myosin-I_fungi, Src homology 3 domain of Type I fungal Myosins. Type I myosins (myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Saccharomyces cerevisiae has two myosins-I, Myo3 and Myo5, which are involved in endocytosis and the polarization of the actin cytoskeleton. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TYKALYDFAGSVANELSLKKDDIVYIVQKEDNGWWLAKKLDESKEGWVPAAYLEE
>gnl|CDD|212793 cd11859, SH3_ZO, Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins. ZO proteins are scaffolding proteins that associate with each other and with other proteins of the tight junction, zonula adherens, and gap junctions. They play roles in regulating cytoskeletal dynamics at these cell junctions. They are considered members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. Vertebrates contain three ZO proteins (ZO-1, ZO-2, and ZO-3) with redundant and non-redundant roles. They contain three PDZ domains, followed by SH3 and GuK domains; in addition, ZO-1 and ZO-2 contains a proline-rich (PR) actin binding domain at the C-terminus while ZO-3 contains this PR domain between the second and third PDZ domains. The C-terminal regions of the three ZO proteins are unique. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YIRTHFDYEKPAKGELSFKKGEVFHVVDTLYQGTVGSWQAVRVGRNHQELERGVIPNKSRAE
>gnl|CDD|212794 cd11860, SH3_DLG5, Src homology 3 domain of Disks Large homolog 5. DLG5 is a multifunctional scaffold protein that is located at sites of cell-cell contact and is involved in the maintenance of cell shape and polarity. Mutations in the DLG5 gene are associated with Crohn's disease (CD) and inflammatory bowel disease (IBD). DLG5 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG5 contains 4 PDZ domains as well as an N-terminal domain of unknown function. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YVRALFDRSAENEDELSFKKDDILYVDNTMFNGVFGQWRAWLVDEEGRKRKCGIIPSKYKVEE
>gnl|CDD|212795 cd11861, SH3_DLG-like, Src Homology 3 domain of Disks large homolog proteins. The DLG-like proteins are scaffolding proteins that cluster at synapses and are also called PSD (postsynaptic density)-95 proteins or SAPs (synapse-associated proteins). They play important roles in synaptic development and plasticity, cell polarity, migration and proliferation. They are members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG-like proteins contain three PDZ domains and varying N-terminal regions. All DLG proteins exist as alternatively-spliced isoforms. Vertebrates contain four DLG proteins from different genes, called DLG1-4. DLG4 and DLG2 are found predominantly at postsynaptic sites and they mediate surface ion channel and receptor clustering. DLG3 is found axons and some presynaptic terminals. DLG1 interacts with AMPA-type glutamate receptors and is critical in their maturation and delivery to synapses. The SH3 domain of DLG4 binds and clusters the kainate subgroup of glutamate receptors via two proline-rich sequences in their C-terminal tail. It also binds AKAP79/150 (A-kinase anchoring protein). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YVRALFDYDPSRDSGLPSQGLSFKFGDILHVTNASDDEWWQARRVTPNGEEEEVGVIPSKR
>gnl|CDD|212796 cd11862, SH3_MPP, Src Homology 3 domain of Membrane Protein, Palmitoylated (or MAGUK p55 subfamily member) proteins. The MPP/p55 subfamily of MAGUK (membrane-associated guanylate kinase) proteins includes at least eight vertebrate members (MPP1-7 and CASK), four Drosophila proteins (Stardust, Varicose, CASK and Skiff), and other similar proteins; they all contain one each of the core of three domains characteristic of MAGUK proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, most members except for MPP1 contain N-terminal L27 domains and some also contain a Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. CASK has an additional calmodulin-dependent kinase (CaMK)-like domain at the N-terminus. Members of this subfamily are scaffolding proteins that play important roles in regulating and establishing cell polarity, cell adhesion, and synaptic targeting and transmission, among others. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FVRALFDYDPEEDPLIPCKEAGLSFKKGDILQIVNQDDPNWWQARKVGDPNGRAGLIPSQD
>gnl|CDD|212797 cd11863, SH3_CACNB, Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta. Voltage-dependent calcium channels (Ca(V)s) are multi-protein complexes that regulate the entry of calcium into cells. They impact muscle contraction, neuronal migration, hormone and neurotransmitter release, and the activation of calcium-dependent signaling pathways. They are composed of four subunits: alpha1, alpha2delta, beta, and gamma. The beta subunit is a soluble and intracellular protein that interacts with the transmembrane alpha1 subunit. It facilitates the trafficking and proper localization of the alpha1 subunit to the cellular plasma membrane. Vertebrates contain four different beta subunits from distinct genes (beta1-4); each exists as multiple splice variants. All are expressed in the brain while other tissues show more specific expression patterns. The beta subunits show similarity to MAGUK (membrane-associated guanylate kinase) proteins in that they contain SH3 and inactive guanylate kinase (GuK) domains; however, they do not appear to contain a PDZ domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FAVRTNVGYDGSLDDDSPVPGYAVSFEAKDFLHIKEKYNNDWWIGRLVKEGCDIGFIPSPAK
>gnl|CDD|212798 cd11864, SH3_PEX13_eumet, Src Homology 3 domain of eumetazoan Peroxisomal biogenesis factor 13. PEX13 is a peroxin and is required for protein import into the peroxisomal matrix and membrane. It is an integral membrane protein that is essential for the localization of PEX14 and the import of proteins containing the peroxisome matrix targeting signals, PTS1 and PTS2. Mutations of the PEX13 gene in humans lead to a wide range of peroxisome biogenesis disorders (PBDs), the most severe of which is known as Zellweger syndrome (ZS), a severe multisystem disorder characterized by hypotonia, psychomotor retardation, and neuronal migration defects. PEX13 contains two transmembrane regions and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VARAEYDFVAESEDELSFRAGDKLRLAPKELQPRVRGWLLATVDGQKIGLVPANYVKI
>gnl|CDD|212799 cd11865, SH3_Nbp2-like, Src Homology 3 domain of Saccharomyces cerevisiae Nap1-binding protein 2 and similar fungal proteins. This subfamily includes Saccharomyces cerevisiae Nbp2 (Nucleosome assembly protein 1 (Nap1)-binding protein 2), Schizosaccharomyces pombe Skb5, and similar proteins. Nbp2 interacts with Nap1, which is essential for maintaining proper nucleosome structures in transcription and replication. It is also the binding partner of the yeast type II protein phosphatase Ptc1p and serves as a scaffolding protein that brings seven kinases in close contact to Ptc1p. Nbp2 plays a role many cell processes including organelle inheritance, mating hormone response, cell wall stress, mitotic cell growth at elevated temperatures, and high osmolarity. Skb5 interacts with the p21-activated kinase (PAK) homolog Shk1, which is critical for fission yeast cell viability. Skb5 activates Shk1 and plays a role in regulating cell morphology and growth under hypertonic conditions. Nbp2 and Skb5 contain an SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RAVALYDFEPEHDNELGFAEGQILFILYKHGQGWLIAEDESGGKTGLVPEEFVSY
>gnl|CDD|212800 cd11866, SH3_SKAP1-like, Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1 and similar proteins. This subfamily is composed of SKAP1, SKAP2, and similar proteins. SKAP1 and SKAP2 are immune cell-specific adaptor proteins that play roles in T- and B-cell adhesion, respectively, and are thus important in the migration of T- and B-cells to sites of inflammation and for movement during T-cell conjugation with antigen-presenting cells. Both SKAP1 and SKAP2 bind to ADAP (adhesion and degranulation-promoting adaptor protein), among many other binding partners. They contain a pleckstrin homology (PH) domain, a C-terminal SH3 domain, and several tyrosine phosphorylation sites. The SH3 domain of SKAP1 is necessary for its ability to regulate T-cell conjugation with antigen-presenting cells and the formation of LFA-1 clusters. SKAP1 binds primarily to a proline-rich region of ADAP through its SH3 domain; its degradation is regulated by ADAP. A secondary interaction occurs via the ADAP SH3 domain and the RKxxYxxY motif in SKAP1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
WYMGLWDCSGNEPDELSFKRGDLIYIISKEYDSFGWWVGELNGKVGLVPKDYL
>gnl|CDD|212801 cd11867, hSH3_ADAP, Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein. ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides
EKEEKEFRKKFKYNGEIKVLYSTTVLQTLTIKKFGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYV
LRSNLEP
>gnl|CDD|212802 cd11869, SH3_p40phox, Src Homology 3 domain of the p40phox subunit of NADPH oxidase. p40phox, also called Neutrophil cytosol factor 4 (NCF-4), is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. It contains an N-terminal PX domain, a central SH3 domain, and a C-terminal PB1 domain that interacts with p67phox. The SH3 domain of p40phox binds to canonical polyproline and noncanonical motifs at the C-terminus of p47phox. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RAEALFDFTGNSKLELNFKAGDVIFLLSRVNKDWLEGTVRGATGIFPLSFVKII
>gnl|CDD|212803 cd11870, SH3_p67phox-like_C, C-terminal Src Homology 3 domain of the p67phox subunit of NADPH oxidase and similar proteins. This subfamily is composed of p67phox, NADPH oxidase activator 1 (Noxa1), and similar proteins. p67phox, also called Neutrophil cytosol factor 2 (NCF-2), and Noxa1 are homologs and are the cytosolic subunits of the phagocytic (Nox2) and nonphagocytic (Nox1) NADPH oxidase complexes, respectively. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p67phox and Noxa1 play regulatory roles. p67phox contains N-terminal TPR, first SH3 (or N-terminal or central SH3), PB1, and C-terminal SH3 domains. Noxa1 has a similar domain architecture except it is lacking the N-terminal SH3 domain. The TPR domain of both binds activated GTP-bound Rac, while the C-terminal SH3 domain of p67phox and Noxa1 binds the polyproline motif found at the C-terminus of p47phox and Noxo1, respectively. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QVVALHRYEAQGPEDLGFREGDTIDVLSEVNEAWLEGHSDGRVGIFPKCFVVP
>gnl|CDD|212804 cd11871, SH3_p67phox_N, N-terminal (or first) Src Homology 3 domain of the p67phox subunit of NADPH oxidase. p67phox, also called Neutrophil cytosol factor 2 (NCF-2), is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p67phox plays a regulatory role and contains N-terminal TPR, first SH3 (or N-terminal or central SH3), PB1, and C-terminal SH3 domains. It binds, via its C-terminal SH3 domain, to a proline-rich region of p47phox and upon activation, this complex assembles with flavocytochrome b558, the Nox2-p22phox heterodimer. Concurrently, RacGTP translocates to the membrane and interacts with the TPR domain of p67phox, which leads to the activation of NADPH oxidase. The PB1 domain of p67phox binds to its partner PB1 domain in p40phox, and this facilitates the assembly of p47phox-p67phox at the membrane. The N-terminal SH3 domain increases the affinity of p67phox for the oxidase complex. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
PHRVLYEFVPETKEELQVLPGNIVFVLKKGTDNWATVVFNGKKGLVPCNFLEPV
>gnl|CDD|212805 cd11872, SH3_DOCK_AB, Src Homology 3 domain of Class A and B Dedicator of Cytokinesis proteins. DOCK proteins are atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. They are divided into four classes (A-D) based on sequence similarity and domain architecture: class A includes Dock1, 2 and 5; class B includes Dock3 and 4; class C includes Dock6, 7, and 8; and class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate while DHR-2 contains the catalytic activity for Rac and/or Cdc42. This subfamily includes only Class A and B DOCKs, which also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus. Class A/B DOCKs are mostly specific GEFs for Rac, except Dock4 which activates the Ras family GTPase Rap1, probably indirectly through interaction with Rap regulatory proteins. The SH3 domain of class A/B DOCKs have been shown to bind Elmo, a scaffold protein that promotes GEF activity of DOCKs by releasing DHR-2 autoinhibition by the intramolecular SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YGVAIYNFQGDGEHQLSLQVGDTVQILEECEGWYRGFSLRNKSLKGIFPKSYVHIK
>gnl|CDD|212806 cd11873, SH3_CD2AP-like_1, First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins. This subfamily is composed of the first SH3 domain (SH3A) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3A of both proteins bind to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic domain of the cell adhesion protein CD2. CIN85 SH3A binds to internal proline-rich motifs within the proline-rich region; this intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. CIN85 SH3A has also been shown to bind ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EVIVEFDYDAEEPDELTLKVGDIITNVKKMEEGWWEGTLNGKRGMFPDNFVKV
>gnl|CDD|212807 cd11874, SH3_CD2AP-like_2, Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins. This subfamily is composed of the second SH3 domain (SH3B) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3B of both proteins have been shown to bind to Cbl. In the case of CD2AP, its SH3B binds to Cbl at a site distinct from the c-Cbl/SH3A binding site. The CIN85 SH3B also binds ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RCKVLFSYTPQNEDELELKVGDTIEVLGEVEEGWWEGKLNGKVGVFPSNFVKE
>gnl|CDD|212808 cd11875, SH3_CD2AP-like_3, Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins. This subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KARVLFDYEAENEDELTLREGDIVTILSKDCEDKGWWKGELNGKRGVFPDNFVEP
>gnl|CDD|212809 cd11876, SH3_MLK, Src Homology 3 domain of Mixed Lineage Kinases. MLKs are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LWTALFDYDARGEDELTLRRGQPVEVLSKDAAVSGDEGWWTGKIGDKVGIFPSNYVAP
>gnl|CDD|212810 cd11877, SH3_PIX, Src Homology 3 domain of Pak Interactive eXchange factors. PIX proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac 1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX subfamily, alpha-PIX and beta-PIX. Alpha-PIX, also called ARHGEF6, is localized in dendritic spines where it regulates spine morphogenesis. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX play roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LVRAKFNFEGTNEDELSFDKGDIITVTQVVEGGWWEGTLNGKTGWFPSNYVKE
>gnl|CDD|212811 cd11878, SH3_Bem1p_1, First Src Homology 3 domain of Bud emergence protein 1 and similar domains. Members of this subfamily bear similarity to Saccharomyces cerevisiae Bem1p, containing two Src Homology 3 (SH3) domains at the N-terminus, a central PX domain, and a C-terminal PB1 domain. Bem1p is a scaffolding protein that is critical for proper Cdc42p activation during bud formation in yeast. During budding and mating, Bem1p migrates to the plasma membrane where it can serve as an adaptor for Cdc42p and some other proteins. Bem1p also functions as an effector of the G1 cyclin Cln3p and the cyclin-dependent kinase Cdc28p in promoting vacuolar fusion. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
VIRALYDYRAQTPGELSFSKGDFFHVIGEEDQGEWYEATNPVTGKRGLVPKSYF
>gnl|CDD|212812 cd11879, SH3_Bem1p_2, Second Src Homology 3 domain of Bud emergence protein 1 and similar domains. Members of this subfamily bear similarity to Saccharomyces cerevisiae Bem1p, containing two Src Homology 3 (SH3) domains at the N-terminus, a central PX domain, and a C-terminal PB1 domain. Bem1p is a scaffolding protein that is critical for proper Cdc42p activation during bud formation in yeast. During budding and mating, Bem1p migrates to the plasma membrane where it can serve as an adaptor for Cdc42p and some other proteins. Bem1p also functions as an effector of the G1 cyclin Cln3p and the cyclin-dependent kinase Cdc28p in promoting vacuolar fusion. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
FGIVLYDFKAERPDELDAKAGDAIIICAHSNYEWFVAKPIGRLGGPGLIPVSFVEI
>gnl|CDD|212813 cd11880, SH3_Caskin, Src Homology 3 domain of CASK interacting protein. Caskin proteins are multidomain adaptor proteins that contain six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. There are two Caskin proteins called Caskin1 and Caskin2. Caskin1 binds to the multidomain scaffolding protein CASK through the CaM domain in competition with Munc-interacting protein 1 (Mint1). CASK participates in one of two evolutionarily conserved tripartite complexes containing either Mint1 and Velis or Caskin1 and Velis. Caskin1 may play a role in infantile myoclonic epilepsy. There is not much known about Caskin2; despite sharing a domain architecture with Caskin1, Caskin2 does not bind CASK. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
LQVRATKDYWNNHDLTALNVRAGDIITVLEQHPDGRWKGHIHDNQTGNDRVGYFPPSLVEV
>gnl|CDD|212814 cd11881, SH3_MYO7A, Src Homology 3 domain of Myosin VIIa and similar proteins. Myo7A is an uncoventional myosin that is involved in organelle transport. It is required for sensory function in both Drosophila and mammals. Mutations in the Myo7A gene cause both syndromic deaf-blindness [Usher syndrome I (USH1)] and nonsyndromic (DFNB2 and DFNA11) deafness in humans. It contains an N-terminal motor domain, light chain-binding IQ motifs, a coiled-coil region for heavy chain dimerization, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
SKYVVALQDYPNPSDGSSFLSFAKGDLIILDQDTGEQVMNSGWCNGRNDRTGQRGDFPADCVYV
>gnl|CDD|212815 cd11882, SH3_GRAF-like, Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar proteins. This subfamily is composed of Rho GTPase activating proteins (GAPs) with similarity to GRAF. Members contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. Although vertebrates harbor four Rho GAPs in the GRAF subfamily including GRAF, GRAF2, GRAF3, and Oligophrenin-1 (OPHN1), only three are included in this model. OPHN1 contains the BAR, PH and GAP domains, but not the C-terminal SH3 domain. GRAF and GRAF2 show GAP activity towards RhoA and Cdc42. GRAF influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase. GRAF2 regulates caspase-activated p21-activated protein kinase-2. The SH3 domain of GRAF and GRAF2 binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
RARALYACKAEDESELSFEPGQIITNVQPSDEPGWLEGTLNGRTGLIPENYVEF
>gnl|CDD|212816 cd11883, SH3_Sdc25, Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors. This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
VVVALYDFTPKSKNQLSFKAGDIIYVLNKDPSGWWDGVIISSSGKVKRGWFPSNY
>gnl|CDD|212817 cd11884, SH3_MYO15, Src Homology 3 domain of Myosin XV. This subfamily is composed of proteins with similarity to Myosin XVa. Myosin XVa is an unconventional myosin that is critical for the normal growth of mechanosensory stereocilia of inner ear hair cells. Mutations in the myosin XVa gene are associated with nonsyndromic hearing loss. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
YVVAVRAYITRDQTLLSFHKGDVIKLLPKEGPLDPGWLFGTLDGRSGAFPKEYVQP
>gnl|CDD|212818 cd11885, SH3_SH3TC, Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins and similar domains. This subfamily is composed of vertebrate SH3TC proteins and hypothetical fungal proteins containing BAR and SH3 domains. Mammals contain two SH3TC proteins, SH3TC1 and SH3TC2. The function of SH3TC1 is unknown. SH3TC2 is localized in Schwann cells in the peripheral nervous system, where it interacts with Rab11 and plays a role in peripheral nerve myelination. Mutations in SH3TC2 are associated with Charcot-Marie-Tooth disease type 4C, a severe hereditary peripheral neuropathy with symptoms that include progressive scoliosis, delayed age of walking, muscular atrophy, distal weakness, and reduced nerve conduction velocity. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF
>gnl|CDD|212819 cd11886, SH3_BOI, Src Homology 3 domain of fungal BOI-like proteins. This subfamily includes the Saccharomyces cerevisiae proteins BOI1 and BOI2, and similar proteins. They contain an N-terminal SH3 domain, a Sterile alpha motif (SAM), and a Pleckstrin homology (PH) domain at the C-terminus. BOI1 and BOI2 interact with the SH3 domain of Bem1p, a protein involved in bud formation. They promote polarized cell growth and participates in the NoCut signaling pathway, which is involved in the control of cytokinesis. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
LLIVIHDFNARSEDELTLKPGDKIELIEDDEEFGDGWYLGRNLRTGETGLFPVVF
>gnl|CDD|212820 cd11887, SH3_Bbc1, Src Homology 3 domain of Bbc1 and similar domains. This subfamily is composed of Saccharomyces cerevisiae Bbc1p, also called Mti1p (Myosin tail region-interacting protein), and similar proteins. Bbc1p interacts with and regulates type I myosins in yeast, Myo3p and Myo5p, which are involved in actin cytoskeletal reorganization. It also binds and inhibits Las17, a WASp family protein that functions as an activator of the Arp2/3 complex. Bbc1p contains an N-terminal SH3 domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
PFKVKALYPYESDHEDDLNFDVGQLITVTEEEDADWYFGEYVDSNGNTKEGIFPKNFVEV
>gnl|CDD|212821 cd11888, SH3_ARHGAP9_like, Src Homology 3 domain of Rho GTPase-activating protein 9 and similar proteins. This subfamily is composed of Rho GTPase-activating proteins including mammalian ARHGAP9, and vertebrate ARHGAPs 12 and 27. RhoGAPs (or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP9 functions as a GAP for Rac and Cdc42, but not for RhoA. It negatively regulates cell migration and adhesion. It also acts as a docking protein for the MAP kinases Erk2 and p38alpha, and may facilitate cross-talk between the Rho GTPase and MAPK pathways to control actin remodeling. ARHGAP27, also called CAMGAP1, shows GAP activity towards Rac1 and Cdc42. It binds the adaptor protein CIN85 and may play a role in clathrin-mediated endocytosis. ARHGAP12 has been shown to display GAP activity towards Rac1. It plays a role in regulating HFG-driven cell growth and invasiveness. ARHGAPs in this subfamily contain SH3, WW, Pleckstin homology (PH), and RhoGAP domains. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
YVVVLYPFEYTGKDGRKVSIKEGERFLLLKKSNDDWWQVRRPGDSKPFYVPAQY
>gnl|CDD|212822 cd11889, SH3_Cyk3p-like, Src Homology 3 domain of Cytokinesis protein 3 and similar proteins. Cytokinesis protein 3 (Cyk3 or Cyk3p) is a component of the actomyosin ring independent cytokinesis pathway in yeast. It interacts with Inn1 and facilitates its recruitment to the bud neck, thereby promoting cytokinesis. Cyk3p contains an N-terminal SH3 domain and a C-terminal transglutaminase-like domain. The Cyk3p SH3 domain binds to the C-terminal proline-rich region of Inn1. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
KVKAVYSWAGETEGDLGFLEGDLIEVLSIGDGSWWSGKLRRNGAEGIFPSNFV
>gnl|CDD|212823 cd11890, MIA, Melanoma Inhibitory Activity protein. MIA is a single domain protein that adopts a Src Homology 3 (SH3) domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. MIA is secreted from malignant melanoma cells and it plays an important role in melanoma development and invasion. MIA is expressed by chondrocytes in normal tissues and may be important in the cartilage cell phenotype. Unlike classical SH3 domains, MIA does not bind proline-rich ligands. It binds peptide ligands with sequence similarity to type III human fibronectin repeats
KKLCADQECSHPISIAVALQDYMAPDCRFIPIQRGQVVYVFSKLKGRGRLFWGGSVQGDYYGEQAARLGY
FPSSIVQEDQYLKPGKVEVKTDKWDFYC
>gnl|CDD|212824 cd11891, MIAL, Melanoma Inhibitory Activity-Like protein. MIAL is specifically expressed in the cochlea and the vestibule of the inner ear and may contribute to inner ear dysfunction in humans. MIAL is a member of the recently identified family that also includes MIA, MIA2, and MIA3 (also called TANGO); MIA is the most studied member of the family. MIA is a single domain protein that adopts a Src Homology 3 (SH3) domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. MIA is secreted from malignant melanoma cells and it plays an important role in melanoma development and invasion. MIA is expressed by chondrocytes in normal tissues and may be important in the cartilage cell phenotype. Unlike classical SH3 domains, MIA does not bind proline-rich ligands
LCADEECVYAISLARAEDDYNAPDCRFINIKKGQLIYVYSKLVKENGAGEFWSGSVYSERYVDQMGIVGY
FPSNLVKEQTVYK
>gnl|CDD|212825 cd11892, SH3_MIA2, Src Homology 3 domain of Melanoma Inhibitory Activity 2 protein. MIA2 is expressed specifically in hepatocytes and its expression is controlled by hepatocyte nuclear factor 1 binding sites in the MIA2 promoter. It inhibits the growth and invasion of hepatocellular carcinomas (HCC) and may act as a tumor suppressor. A mutation in MIA2 in mice resulted in reduced cholesterol and triglycerides. Since MIA2 localizes to ER exit sites, it may function as an ER-to-Golgi trafficking protein that regulates lipid metabolism. MIA2 contains an N-terminal SH3-like domain, similar to MIA. It is a member of the recently identified family that also includes MIA, MIAL, and MIA3 (also called TANGO). MIA is a single domain protein that adopts a SH3 domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. Unlike classical SH3 domains, MIA does not bind proline-rich ligands
KCGDPECERLMSRVQAIRDYRGPDCRYLSFKKGDEIIVYYKLSGKREDLWAGSTGKEFGYFPKDAVKVEE
VYI
>gnl|CDD|212826 cd11893, SH3_MIA3, Src Homology 3 domain of Melanoma Inhibitory Activity 3 protein. MIA3, also called TANGO or TANGO1, acts as a tumor suppressor of malignant melanoma. It is downregulated or lost in melanoma cells lines. Unlike other MIA family members, MIA3 is widely expressed except in hematopoietic cells. MIA3 is an ER resident transmembrane protein that is required for the loading of collagen VII into transport vesicles. SNPs in the MIA3 gene have been associated with coronary arterial disease and myocardial infarction. MIA3 contains an N-terminal SH3-like domain, similar to MIA. It is a member of the recently identified family that also includes MIA, MIAL, and MIA2. MIA is a single domain protein that adopts a SH3 domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. Unlike classical SH3 domains, MIA does not bind proline-rich ligands
RCADEECSMLLCRGKAVKDFTGPDCRFLSFKKGETIYVYYKLSGRRTDLWAGSVGFDFGYFPKDLLDVNH
LYT
>gnl|CDD|212827 cd11894, SH3_FCHSD2_2, Second Src Homology 3 domain of FCH and double SH3 domains protein 2. FCHSD2 has a domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. It has only been characterized in silico and its function is unknown. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FVKALYDYEGQTDDELSFPEGAIIRILNKENQDDDGFWEGEFNGRIGVFPSVLVEE
>gnl|CDD|212828 cd11895, SH3_FCHSD1_2, Second Src Homology 3 domain of FCH and double SH3 domains protein 1. FCHSD1 has a domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. It has only been characterized in silico and its function is unknown. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LARALYSYTGQSPEELSFPEGALIRLLPRAQDGVDDGFWRGEFGGRVGVFPSLLVEEL
>gnl|CDD|212829 cd11896, SH3_SNX33, Src Homology 3 domain of Sorting Nexin 33. SNX33 interacts with Wiskott-Aldrich syndrome protein (WASP) and plays a role in the maintenance of cell shape and cell cycle progression. It modulates the shedding and endocytosis of cellular prion protein (PrP(c)) and amyloid precursor protein (APP). SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX33 also contains BAR and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KARALYSFQSENKEEINIQENEELVIFSENSLDGWLQGQNSRGETGLFPASYVEI
>gnl|CDD|212830 cd11897, SH3_SNX18, Src Homology 3 domain of Sorting nexin 18. SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. It binds FIP5 and is required for apical lumen formation. It may also play a role in axonal elongation. SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX18 also contains BAR and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RARALYDFRSENPGEISLREHEVLSLCSEQDIEGWLEGVNSRGDRGLFPASYVEV
>gnl|CDD|212831 cd11898, SH3_SNX9, Src Homology 3 domain of Sorting nexin 9. Sorting nexin 9 (SNX9), also known as SH3PX1, is a cytosolic protein that interacts with proteins associated with clathrin-coated pits such as Cdc-42-associated tyrosine kinase 2 (ACK2). It binds class I polyproline sequences found in dynamin 1/2 and the WASP/N-WASP actin regulators. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis. Its array of interacting partners suggests that SNX9 functions at the interface between endocytosis and actin cytoskeletal organization. SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX9 also contains BAR and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KARVLYDFAAEPGNNELTVKEGEIITVTNPNVGGGWIEAKNSQGERGLVPTDYVEIV
>gnl|CDD|212832 cd11899, SH3_Nck2_1, First Src Homology 3 domain of Nck2 adaptor protein. Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling. It binds neuronal signaling proteins such as ephrinB and Disabled-1 (Dab-1) exclusively. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2, which show partly overlapping functions but also bind distinct targets. The first SH3 domain of Nck2 binds the PxxDY sequence in the CD3e cytoplasmic tail; this binding inhibits phosphorylation by Src kinases, resulting in the downregulation of TCR surface expression. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TEEVIVIAKWDYTAQQDQELDIKKNERLWLLDDSKTWWRVRNAANRTGYVPSNYVERK
>gnl|CDD|212833 cd11900, SH3_Nck1_1, First Src Homology 3 domain of Nck1 adaptor protein. Nck1 (also called Nckalpha) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling. It binds and activates RasGAP, resulting in the downregulation of Ras. It is also involved in the signaling of endothilin-mediated inhibition of cell migration. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2, which show partly overlapping functions but also bind distinct targets. The first SH3 domain of Nck1 binds the PxxDY sequence in the CD3e cytoplasmic tail; this binding inhibits phosphorylation by Src kinases, resulting in the downregulation of TCR surface expression. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EEVVVVAKFDYVAQQDQELDIKKNERLWLLDDSKSWWRVRNAMNKTGFVPSNYVERKNS
>gnl|CDD|212834 cd11901, SH3_Nck1_2, Second Src Homology 3 domain of Nck1 adaptor protein. Nck1 (also called Nckalpha) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling. It binds and activates RasGAP, resulting in the downregulation of Ras. It is also involved in the signaling of endothilin-mediated inhibition of cell migration. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2, which show partly overlapping functions but also bind distinct targets. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
NLPAYVKFNYTAEREDELSLVKGTKVIVMEKCSDGWWRGSYNGQVGWFPSNYVTE
>gnl|CDD|212835 cd11902, SH3_Nck2_2, Second Src Homology 3 domain of Nck2 adaptor protein. Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling. It binds neuronal signaling proteins such as ephrinB and Disabled-1 (Dab-1) exclusively. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2, which show partly overlapping functions but also bind distinct targets. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
IPAFVKFAYVAEREDELSLVKGSRVTVMEKCSDGWWRGSYNGQIGWFPSNYVVEE
>gnl|CDD|212836 cd11903, SH3_Nck2_3, Third Src Homology 3 domain of Nck2 adaptor protein. Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling. It binds neuronal signaling proteins such as ephrinB and Disabled-1 (Dab-1) exclusively. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2, which show partly overlapping functions but also bind distinct targets. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
HVVQTLYPFSSVTEEELNFEKGETMEVIEKPENDPEWWKCKNSRGQVGLVPKNYVVVLS
>gnl|CDD|212837 cd11904, SH3_Nck1_3, Third Src Homology 3 domain of Nck1 adaptor protein. Nck1 (also called Nckalpha) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling. It binds and activates RasGAP, resulting in the downregulation of Ras. It is also involved in the signaling of endothilin-mediated inhibition of cell migration. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2, which show partly overlapping functions but also bind distinct targets. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
HVVQALYPFSSSNDEELNFEKGEVMDVIEKPENDPEWWKCRKANGQVGLVPKNYVTV
>gnl|CDD|212838 cd11905, SH3_Tec, Src Homology 3 domain of Tec (Tyrosine kinase expressed in hepatocellular carcinoma). Tec is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. It is more widely-expressed than other Tec subfamily kinases. Tec is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Tec is a key component of T-cell receptor (TCR) signaling, and is important in TCR-stimulated proliferation, IL-2 production and phospholipase C-gamma1 activation. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EIVVAMYDFQPTEPHDLRLETGEEYVILEKNDVHWWKARDKYGKEGYIPSNYVTGK
>gnl|CDD|212839 cd11906, SH3_BTK, Src Homology 3 domain of Bruton's tyrosine kinase. BTK is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor (BCR), leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KKVVALYDYTPMNAQDLQLRKGEEYVILEESNLPWWRARDKNGREGYIPSNYVTE
>gnl|CDD|212840 cd11907, SH3_TXK, Src Homology 3 domain of TXK, also called Resting lymphocyte kinase (Rlk). TXK is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal cysteine-rich region. Rlk is expressed in T-cells and mast cell lines, and is a key component of T-cell receptor (TCR) signaling. It is important in TCR-stimulated proliferation, IL-2 production and phospholipase C-gamma1 activation. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
IQVKALYDFLPREPSNLALKRAEEYLILEQYDPHWWKARDRYGNEGLIPSNYVTE
>gnl|CDD|212841 cd11908, SH3_ITK, Src Homology 3 domain of Interleukin-2-inducible T-cell Kinase. ITK (also known as Tsk or Emt) is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. ITK is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, ITK plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, ITK is crucial for the development of T-helper(Th)2 effector responses. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TLVIALYDYQTNDPQELALRYNEEYHLLDSSEIHWWRVQDKNGHEGYVPSSYLVEK
>gnl|CDD|212842 cd11909, SH3_PI3K_p85beta, Src Homology 3 domain of the p85beta regulatory subunit of Class IA Phosphatidylinositol 3-kinases. Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. In addition to regulating the p110 subunit, p85beta binds CD28 and may be involved in the activation and differentiation of antigen-stimulated T cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FQYRALYPYRKEREEDIDLLPGDVLTVSRAALQALGVKEGGEQCPQSIGWILGLNERTKQRGDFPGTYVE
FLGP
>gnl|CDD|212843 cd11910, SH3_PI3K_p85alpha, Src Homology 3 domain of the p85alpha regulatory subunit of Class IA Phosphatidylinositol 3-kinases. Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. In addition to regulating the p110 subunit, p85alpha interacts with activated FGFR3. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GYQYRALYDYKKEREEDIDLHLGDILTVNKGSLLALGFSEGQEARPEEIGWLNGYNETTGERGDFPGTYV
EYIGR
>gnl|CDD|212844 cd11911, SH3_CIP4-like, Src Homology 3 domain of Cdc42-Interacting Protein 4. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. It functions downstream of Cdc42 in PDGF-dependent actin reorganization and cell migration, and also regulates the activity of PDGFRbeta. It uses Src as a substrate in regulating the invasiveness of breast tumor cells. CIP4 may also play a role in the pathogenesis of Huntington's disease. Members of this subfamily typically contain an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain, a central Cdc42-binding HR1 domain, and a C-terminal SH3 domain. The SH3 domain of CIP4 associates with Gapex-5, a Rab31 GEF. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TCTALYDFDGTSEGTLSMEEGEILLVLEEDGGDGWTRVRKNNGDEGYVPTSYIEV
>gnl|CDD|212845 cd11912, SH3_Bzz1_1, First Src Homology 3 domain of Bzz1 and similar domains. Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the first C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TAKVLYDYTASGDDEVSISEGEEVTVLEPDDGSGWTKVRNGSGEEGLVPTSYIEI
>gnl|CDD|212846 cd11913, SH3_BAIAP2L1, Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1, also called Insulin Receptor Tyrosine Kinase Substrate (IRTKS). BAIAP2L1 or IRTKS is widely expressed, serves as a substrate for the insulin receptor, and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. BAIAP2L1 expression leads to the formation of short actin bundles, distinct from filopodia-like protrusions induced by the expression of the related protein IRSp53. IRTKS mediates the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. It contains an N-terminal IMD or Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The SH3 domain of IRTKS has been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QKVKTIFPHTAGNNKTLLSFAQGDVITLLIPEEKDGWLYGEHDTTKARGWFPSSYTRP
>gnl|CDD|212847 cd11914, SH3_BAIAP2L2, Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2. BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. It contains an N-terminal IMD or Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The related proteins, BAIAP2L1 and IRSp53, function as regulators of membrane dynamics and the actin cytoskeleton. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RRVRAIVSHPAGSNPTLLRFNRGDIITVLVPEARNGWLYGKLEGSSRQGWFPEAYVKAL
>gnl|CDD|212848 cd11915, SH3_Irsp53, Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53. IRSp53 is also known as BAIAP2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2). It is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. One variant (T-form) is expressed exclusively in human breast cancer cells. The gene encoding IRSp53 is a putative susceptibility gene for Gilles de la Tourette syndrome. IRSp53 can also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. It contains an N-terminal IMD, a CRIB (Cdc42 and Rac interactive binding motif), an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The SH3 domain of IRSp53 has been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TRVQAIFSHAAGDNSTLLSFKEGDYITLLVPEARDGWHYGECEKTKMRGWFPFSYTRVL
>gnl|CDD|212849 cd11916, SH3_Sorbs1_3, Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ponsin. Sorbs1 is also called ponsin, SH3P12, or CAP (c-Cbl associated protein). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It binds Cbl and plays a major role in regulating the insulin signaling pathway by enhancing insulin-induced phosphorylation of Cbl. Sorbs1, like vinexin, localizes at cell-ECM and cell-cell adhesion sites where it binds vinculin, paxillin, and afadin. It may function in the control of cell motility. Other interaction partners of Sorbs1 include c-Abl, Sos, flotillin, Grb4, ataxin-7, filamin C, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
AYSYQALYSYAPQNDDELELRDGDIVDVMEKCDDGWFVGTSRRTKQFGTFPGNYVKLLY
>gnl|CDD|212850 cd11917, SH3_Sorbs2_3, Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called Arg-binding protein 2 (ArgBP2). Sorbs2 or ArgBP2 is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It regulates actin-dependent processes including cell adhesion, morphology, and migration. It is expressed in many tissues and is abundant in the heart. Like vinexin, it is found in focal adhesion where it interacts with vinculin and afadin. It also localizes in epithelial cell stress fibers and in cardiac muscle cell Z-discs. Sorbs2 has been implicated to play roles in the signaling of c-Arg, Akt, and Pyk2. Other interaction partners of Sorbs2 include c-Abl, flotillin, spectrin, dynamin 1/2, synaptojanin, PTP-PEST, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QGGGEPFQALYNYMPRNEDELELREGDVIDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL
>gnl|CDD|212851 cd11918, SH3_Vinexin_3, Third (or C-terminal) Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3). Vinexin is also called Sorbs3, SH3P3, and SH3-containing adapter molecule 1 (SCAM-1). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. Vinexin was first identified as a vinculin binding protein; it is co-localized with vinculin at cell-ECM and cell-cell adhesion sites. There are several splice variants of vinexin: alpha, which contains the SoHo and three SH3 domains and displays tissue-specific expression; and beta, which contains only the three SH3 domains and is widely expressed. Vinexin alpha stimulates the accumulation of F-actin at focal contact sites. Vinexin also promotes keratinocyte migration and wound healing. The SH3 domains of vinexin have been reported to bind a number of ligands including vinculin, WAVE2, DLG5, Abl, and Cbl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RTPYKAVYQYRPQNEDELELREGDRVDVMQQCDDGWFVGVSRRTQKFGTFPGNYVAPV
>gnl|CDD|212852 cd11919, SH3_Sorbs1_1, First Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ponsin. Sorbs1 is also called ponsin, SH3P12, or CAP (c-Cbl associated protein). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It binds Cbl and plays a major role in regulating the insulin signaling pathway by enhancing insulin-induced phosphorylation of Cbl. Sorbs1, like vinexin, localizes at cell-ECM and cell-cell adhesion sites where it binds vinculin, paxillin, and afadin. It may function in the control of cell motility. Other interaction partners of Sorbs1 include c-Abl, Sos, flotillin, Grb4, ataxin-7, filamin C, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RPARAKFDFKAQTLKELPLQKGDIVYIYKQIDQNWYEGEHHGRVGIFPRSYIELL
>gnl|CDD|212853 cd11920, SH3_Sorbs2_1, First Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called Arg-binding protein 2 (ArgBP2). Sorbs2 or ArgBP2 is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It regulates actin-dependent processes including cell adhesion, morphology, and migration. It is expressed in many tissues and is abundant in the heart. Like vinexin, it is found in focal adhesion where it interacts with vinculin and afadin. It also localizes in epithelial cell stress fibers and in cardiac muscle cell Z-discs. Sorbs2 has been implicated to play roles in the signaling of c-Arg, Akt, and Pyk2. Other interaction partners of Sorbs2 include c-Abl, flotillin, spectrin, dynamin 1/2, synaptojanin, PTP-PEST, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LPARAVYDFKAQTSKELSFKKGDTVYILRKIDQNWYEGEHHGRVGIFPISYVEKL
>gnl|CDD|212854 cd11921, SH3_Vinexin_1, First Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3). Vinexin is also called Sorbs3, SH3P3, and SH3-containing adapter molecule 1 (SCAM-1). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. Vinexin was first identified as a vinculin binding protein; it is co-localized with vinculin at cell-ECM and cell-cell adhesion sites. There are several splice variants of vinexin: alpha, which contains the SoHo and three SH3 domains and displays tissue-specific expression; and beta, which contains only the three SH3 domains and is widely expressed. Vinexin alpha stimulates the accumulation of F-actin at focal contact sites. Vinexin also promotes keratinocyte migration and wound healing. The SH3 domains of vinexin have been reported to bind a number of ligands including vinculin, WAVE2, DLG5, Abl, and Cbl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KAARLKFDFQAQSPKELTLQKGDIVYIHKEVDKNWLEGEHHGRVGIFPANYVEVL
>gnl|CDD|212855 cd11922, SH3_Sorbs1_2, Second Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ponsin. Sorbs1 is also called ponsin, SH3P12, or CAP (c-Cbl associated protein). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It binds Cbl and plays a major role in regulating the insulin signaling pathway by enhancing insulin-induced phosphorylation of Cbl. Sorbs1, like vinexin, localizes at cell-ECM and cell-cell adhesion sites where it binds vinculin, paxillin, and afadin. It may function in the control of cell motility. Other interaction partners of Sorbs1 include c-Abl, Sos, flotillin, Grb4, ataxin-7, filamin C, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GEAIAKFNFNGDTQVEMSFRKGERITLLRQVDENWYEGRIPGTSRQGIFPITYVDVIK
>gnl|CDD|212856 cd11923, SH3_Sorbs2_2, Second Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called Arg-binding protein 2 (ArgBP2). Sorbs2 or ArgBP2 is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It regulates actin-dependent processes including cell adhesion, morphology, and migration. It is expressed in many tissues and is abundant in the heart. Like vinexin, it is found in focal adhesion where it interacts with vinculin and afadin. It also localizes in epithelial cell stress fibers and in cardiac muscle cell Z-discs. Sorbs2 has been implicated to play roles in the signaling of c-Arg, Akt, and Pyk2. Other interaction partners of Sorbs2 include c-Abl, flotillin, spectrin, dynamin 1/2, synaptojanin, PTP-PEST, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GEAVAKYNFNADTNVELSLRKGDRVVLLKQVDQNWYEGKIPGTNRQGIFPVSYVEVI
>gnl|CDD|212857 cd11924, SH3_Vinexin_2, Second Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3). Vinexin is also called Sorbs3, SH3P3, and SH3-containing adapter molecule 1 (SCAM-1). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. Vinexin was first identified as a vinculin binding protein; it is co-localized with vinculin at cell-ECM and cell-cell adhesion sites. There are several splice variants of vinexin: alpha, which contains the SoHo and three SH3 domains and displays tissue-specific expression; and beta, which contains only the three SH3 domains and is widely expressed. Vinexin alpha stimulates the accumulation of F-actin at focal contact sites. Vinexin also promotes keratinocyte migration and wound healing. The SH3 domains of vinexin have been reported to bind a number of ligands including vinculin, WAVE2, DLG5, Abl, and Cbl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GEAVAQYTFKGDLEVELSFRKGEHICLIRKVNENWYEGRITGTGRQGIFPASYVQV
>gnl|CDD|212858 cd11925, SH3_SH3RF3_3, Third Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ligase. SH3RF3 is also called POSH2 (Plenty of SH3s 2) or SH3MD4 (SH3 multiple domains protein 4). It is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2). It may play a role in regulating JNK mediated apoptosis in certain conditions. It also interacts with GTP-loaded Rac1. SH3RF3 is highly homologous to SH3RF1; it also contains an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF3. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
NIYLALYAYKPQKNDELELRKGEMYRVIEKCQDGWFKGTSLRTGVSGVFPGNYVTPV
>gnl|CDD|212859 cd11926, SH3_SH3RF1_3, Third Src Homology 3 domain of SH3 domain containing ring finger 1, an E3 ubiquitin-protein ligase. SH3RF1 is also called POSH (Plenty of SH3s) or SH3MD2 (SH3 multiple domains protein 2). It is a scaffold protein that acts as an E3 ubiquitin-protein ligase. It plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF1 also enhances the ubiquitination of ROMK1 potassium channel resulting in its increased endocytosis. It contains an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWFKGTSMHTSKIGVFPGNYVAP
>gnl|CDD|212860 cd11927, SH3_SH3RF1_1, First Src Homology 3 domain of SH3 domain containing ring finger protein 1, an E3 ubiquitin-protein ligase. SH3RF1 is also called POSH (Plenty of SH3s) or SH3MD2 (SH3 multiple domains protein 2). It is a scaffold protein that acts as an E3 ubiquitin-protein ligase. It plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF1 also enhances the ubiquitination of ROMK1 potassium channel resulting in its increased endocytosis. It contains an N-terminal RING finger domain and four SH3 domains. This model represents the first SH3 domain, located at the N-terminal half, of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
PCAKALYNYEGKEPGDLKFSKGDIIILRRQVDENWYHGEVNGIHGFFPTNFVQI
>gnl|CDD|212861 cd11928, SH3_SH3RF3_1, First Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ligase. SH3RF3 is also called POSH2 (Plenty of SH3s 2) or SH3MD4 (SH3 multiple domains protein 4). It is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2). It may play a role in regulating JNK mediated apoptosis in certain conditions. It also interacts with GTP-loaded Rac1. SH3RF3 is highly homologous to SH3RF1; it also contains an N-terminal RING finger domain and four SH3 domains. This model represents the first SH3 domain, located at the N-terminal half, of SH3RF3. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
PCGKALYSYEGKEPGDLKFNKGDIIILRRKVDENWYHGELNGCHGFLPASYIQC
>gnl|CDD|212862 cd11929, SH3_SH3RF2_1, First Src Homology 3 domain of SH3 domain containing ring finger 2. SH3RF2 is also called POSHER (POSH-eliminating RING protein) or HEPP1 (heart protein phosphatase 1-binding protein). It acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal RING finger domain and three SH3 domains. This model represents the first SH3 domain, located at the N-terminal half, of SH3RF2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
PRAKALCNYRGHNPGDLKFNKGDVILLRRQLDENWYLGEINGVSGIFPASSVEV
>gnl|CDD|212863 cd11930, SH3_SH3RF1_2, Second Src Homology 3 domain of SH3 domain containing ring finger protein 1, an E3 ubiquitin-protein ligase. SH3RF1 is also called POSH (Plenty of SH3s) or SH3MD2 (SH3 multiple domains protein 2). It is a scaffold protein that acts as an E3 ubiquitin-protein ligase. It plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF1 also enhances the ubiquitination of ROMK1 potassium channel resulting in its increased endocytosis. It contains an N-terminal RING finger domain and four SH3 domains. This model represents the second SH3 domain, located C-terminal of the first SH3 domain at the N-terminal half, of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QCKALYDFEVKDKEADKDCLPFAKDDILTVIRRVDENWAEGMLGDKIGIFPISYV
>gnl|CDD|212864 cd11931, SH3_SH3RF3_2, Second Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ligase. SH3RF3 is also called POSH2 (Plenty of SH3s 2) or SH3MD4 (SH3 multiple domains protein 4). It is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2). It may play a role in regulating JNK mediated apoptosis in certain conditions. It also interacts with GTP-loaded Rac1. SH3RF3 is highly homologous to SH3RF1; it also contains an N-terminal RING finger domain and four SH3 domains. This model represents the second SH3 domain, located C-terminal of the first SH3 domain at the N-terminal half, of SH3RF3. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QGKALYDFEIKDKDQDKDCLTFTKDEILTVIRRVDENWAEGMLGDKIGIFPILYV
>gnl|CDD|212865 cd11932, SH3_SH3RF2_2, Second Src Homology 3 domain of SH3 domain containing ring finger 2. SH3RF2 is also called POSHER (POSH-eliminating RING protein) or HEPP1 (heart protein phosphatase 1-binding protein). It acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal RING finger domain and three SH3 domains. This model represents the second SH3 domain, located C-terminal of the first SH3 domain at the N-terminal half, of SH3RF2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LCRALYNFDLKEKNREESKDCLKFQKDDIITVISRVDENWAEGKLGDQVGIFPILFV
>gnl|CDD|212866 cd11933, SH3_Nebulin_C, C-terminal Src Homology 3 domain of Nebulin. Nebulin is a giant filamentous protein (600-900 kD) that is expressed abundantly in skeletal muscle. It binds to actin thin filaments and regulates its assembly and function. Nebulin was thought to be part of a molecular ruler complex that is critical in determining the lengths of actin thin filaments in skeletal muscle since its length, which varies due to alternative splicing, correlates with the length of thin filaments in various muscle types. Recent studies indicate that nebulin regulates thin filament length by stabilizing the filaments and preventing depolymerization. Mutations in nebulin can cause nemaline myopathy, characterized by muscle weakness which can be severe and can lead to neonatal lethality. Nebulin contains an N-terminal LIM domain, many nebulin repeats/super repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GKSFRAMYDYRAADDDEVSFKDGDTIVNVQTIDEGWMYGTVQRTGKTGMLPANYVEAI
>gnl|CDD|212867 cd11934, SH3_Lasp1_C, C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1. Lasp1 is a cytoplasmic protein that binds focal adhesion proteins and is involved in cell signaling, migration, and proliferation. It is overexpressed in several cancer cells including breast, ovarian, bladder, and liver. In cancer cells, it can be found in the nucleus; its degree of nuclear localization correlates with tumor size and poor prognosis. Lasp1 is a 36kD protein containing an N-terminal LIM domain, two nebulin repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GGKRYRAVYDYNAADEDEVSFQDGDTIVNVQQIDDGWMYGTVERTGDTGMLPANYVEAI
>gnl|CDD|212868 cd11935, SH3_Nebulette_C, C-terminal Src Homology 3 domain of Nebulette and LIM-nebulette (or Lasp2). Nebulette is a cardiac-specific protein that localizes to the Z-disc. It interacts with tropomyosin and is important in stabilizing actin thin filaments in cardiac muscles. Polymorphisms in the nebulette gene are associated with dilated cardiomyopathy, with some mutations resulting in severe heart failure. Nebulette is a 107kD protein that contains an N-terminal acidic region, multiple nebulin repeats, and a C-terminal SH3 domain. LIM-nebulette, also called Lasp2 (LIM and SH3 domain protein 2), is an alternatively spliced variant of nebulette. Although it shares a gene with nebulette, Lasp2 is not transcribed from a muscle-specific promoter, giving rise to its multiple tissue expression pattern with highest amounts in the brain. It can crosslink actin filaments and it affects cell spreading. Lasp2 is a 34kD protein containing an N-terminal LIM domain, three nebulin repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RTYRAMYDYSAQDEDEVSFRDGDYIVNVQPIDEGWMYGTVQRTGRTGMLPANYIEFVN
>gnl|CDD|212869 cd11936, SH3_UBASH3B, Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein B. UBASH3B, also called Suppressor of T cell receptor Signaling (STS)-1 or T cell Ubiquitin LigAnd (TULA)-2 is an active phosphatase that is expressed ubiquitously. The phosphatase activity of UBASH3B is essential for its roles in the suppression of TCR signaling and the regulation of EGFR. It also interacts with Syk and functions as a negative regulator of platelet glycoprotein VI signaling. TULA proteins contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
HETLQVIYPYTPQNDDELELVPGDYIFMSPMEQTSTSEGWIYGTSLTTGCSGLLPENYITKA
>gnl|CDD|212870 cd11937, SH3_UBASH3A, Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein A. UBASH3A is also called Cbl-Interacting Protein 4 (CLIP4), T cell Ubiquitin LigAnd (TULA), or T cell receptor Signaling (STS)-2. It is only found in lymphoid cells and exhibits weak phosphatase activity. UBASH3A facilitates T cell-induced apoptosis through interaction with the apoptosis-inducing factor AIF. It is involved in regulating the level of phosphorylation of the zeta-associated protein (ZAP)-70 tyrosine kinase. TULA proteins contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QTLRALFQYKPQNIDELMLSPGDYIFVDPTQQSEASEGWVIGISHRTGCRGFLPENYTER
>gnl|CDD|212871 cd11938, SH3_ARHGEF16_26, Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF16 and ARHGEF26. ARHGEF16, also called ephexin-4, acts as a GEF for RhoG, activating it by exchanging bound GDP for free GTP. RhoG is a small GTPase that is a crucial regulator of Rac in migrating cells. ARHGEF16 interacts directly with the ephrin receptor EphA2 and mediates cell migration and invasion in breast cancer cells by activating RhoG. ARHGEF26, also called SGEF (SH3 domain-containing guanine exchange factor), also activates RhoG. It is highly expressed in liver and may play a role in regulating membrane dynamics. ARHGEF16 and ARHGEF26 contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and SH3 domains. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QVEIIKAYTAKQPDELSLQQADVVLVLQTESDGWYYGERLRDGERGWFPSSCAKE
>gnl|CDD|212872 cd11939, SH3_ephexin1, Src homology 3 domain of the Rho guanine nucleotide exchange factor, ephexin-1 (also called NGEF or ARHGEF27). Ephexin-1, also called NGEF (neuronal GEF) or ARHGEF27, activates RhoA, Tac1, and Cdc42 by exchanging bound GDP for free GTP. It is expressed mainly in the brain in a region associated with movement control. It regulates the stability of postsynaptic acetylcholine receptor (AChR) clusters and thus, plays a critical role in the maturation and neurotransmission of neuromuscular junctions. Ephexin-1 directly interacts with the ephrin receptor EphA4 and their coexpression enhances the ability of ephexin-1 to activate RhoA. It is required for normal axon growth and EphA-induced growth cone collapse. Ephexin-1 contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and SH3 domains. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QVQCVHPYVSQEPDELSLELADVLNILDKTDDGWIFGERLHDQERGWFPSSVVEE
>gnl|CDD|212873 cd11940, SH3_ARHGEF5_19, Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF5 and ARHGEF19. ARHGEF5, also called ephexin-3 or TIM (Transforming immortalized mammary oncogene), is a potent activator of RhoA and it plays roles in regulating cell shape, adhesion, and migration. It binds to the SH3 domain of Src and is involved in regulating Src-induced podosome formation. ARHGEF19, also called ephexin-2 or WGEF (weak-similarity GEF), is highly expressed in the intestine, liver, heart and kidney. It activates RhoA, Cdc42, and Rac 1, and has been shown to activate RhoA in the Wnt-PCP (planar cell polarity) pathway. It is involved in the regulation of cell polarity and cytoskeletal reorganization. ARHGEF5 and ARHGEF19 contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and SH3 domains. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QVQCIRSYKAQENDELTLEKADIIMVRQQSSDGWLEGVRLSDGERGWFPQSHVEE
>gnl|CDD|212874 cd11941, SH3_ARHGEF37_C2, Second C-terminal Src homology 3 domain of Rho guanine nucleotide exchange factor 37. ARHGEF37 contains a RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. Its specific function is unknown. Its domain architecture is similar to the C-terminal half of DNMBP or Tuba, a cdc42-specific GEF that provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics, and plays an important role in regulating cell junction configuration. GEFs activate small GTPases by exchanging bound GDP for free GTP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QVVAAYPFTARSKHEVSLQAGQPVTVLEPHDKKGSPEWSLVEVNGQRGYVPSSYLAR
>gnl|CDD|212875 cd11942, SH3_JIP2, Src homology 3 domain of JNK-interacting protein 2. JNK-interacting protein 2 (JIP2) is also called Mitogen-activated protein kinase 8-interacting protein 2 (MAPK8IP2) or Islet-brain-2 (IB2). It is widely expressed in the brain, where it forms complexes with fibroblast growth factor homologous factors (FHFs), which facilitates activation of the p38delta MAPK. JIP2 is enriched in postsynaptic densities and may play a role in motor and cognitive function. In addition to a JNK binding domain, JIP2 also contains SH3 and Phosphotyrosine-binding (PTB) domains. The SH3 domain of the related protein JIP1 homodimerizes at the interface usually involved in proline-rich ligand recognition, despite the lack of this motif in the domain itself. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
THRAVFRFIPRHEDELELDVDDPLLVEAEEDDYWYRGYNMRTGERGIFPAFYAHE
>gnl|CDD|212876 cd11943, SH3_JIP1, Src homology 3 domain of JNK-interacting protein 1. JNK-interacting protein 1 (JIP1) is also called Islet-brain 1 (IB1) or Mitogen-activated protein kinase 8-interacting protein 1 (MAPK8IP1). It is highly expressed in neurons, where it functions as an adaptor linking motor to cargo during axonal transport. It also affects microtubule dynamics in neurons. JIP1 is also found in pancreatic beta-cells, where it is involved in regulating insulin secretion. In addition to a JNK binding domain, JIP1 also contains SH3 and Phosphotyrosine-binding (PTB) domains. Its SH3 domain homodimerizes at the interface usually involved in proline-rich ligand recognition, despite the lack of this motif in the domain itself. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
THRAVFRFVPRHPDELELEVDDPLLVEVQAEDYWYEAYNMRTGARGIFPAYYAIE
>gnl|CDD|212877 cd11944, SH3_Endophilin_B2, Src homology 3 domain of Endophilin-B2. Endophilin-B2, also called SH3GLB2 (SH3-domain GRB2-like endophilin B2), is a cytoplasmic protein that interacts with the apoptosis inducer Bax. It is overexpressed in prostate cancer metastasis and has been identified as a cancer antigen with potential utility in immunotherapy. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. Endophilin-B2 forms homo- and heterodimers (with endophilin-B1) through its BAR domain. The related protein endophilin-B1 interacts with amphiphysin 1 and dynamin 1 through its SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KARVLYDYEAADSSELALLADELITVYSLPGMDPDWLIGERGNQKGKVPVTYLEL
>gnl|CDD|212878 cd11945, SH3_Endophilin_B1, Src homology 3 domain of Endophilin-B1. Endophilin-B1, also called Bax-interacting factor 1 (Bif-1) or SH3GLB1 (SH3-domain GRB2-like endophilin B1), is localized mainly to the Golgi apparatus. It is involved in the regulation of many biological events including autophagy, tumorigenesis, nerve growth factor (NGF) trafficking, neurite outgrowth, mitochondrial outer membrane dynamics, and cell death. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. Endophilin-B1 forms homo- and heterodimers (with endophilin-B2) through its BAR domain. It interacts with amphiphysin 1 and dynamin 1 through its SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
SGSRKARVLYDYDAANSTELSLLADEVITVYSVPGMDSDWLMGERGNQKGKVPITYLELLN
>gnl|CDD|212879 cd11946, SH3_GRB2_N, N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2. GRB2 is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. It is ubiquitously expressed in all tissues throughout development and is important in cell cycle progression, motility, morphogenesis, and angiogenesis. In lymphocytes, GRB2 is associated with antigen receptor signaling components. GRB2 contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. Its N-terminal SH3 domain binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
MEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMK
>gnl|CDD|212880 cd11947, SH3_GRAP2_N, N-terminal Src homology 3 domain of GRB2-related adaptor protein 2. GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also have roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EARGKFDFTASGEDELSFKKGDVLKILSSDDIWFKAELNGEEGYVPKNFVDI
>gnl|CDD|212881 cd11948, SH3_GRAP_N, N-terminal Src homology 3 domain of GRB2-related adaptor protein. GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EAVALYSFQATESDELPFQKGDILKILNMEDDQNWYKAELQGREGYIPKNYIKV
>gnl|CDD|212882 cd11949, SH3_GRB2_C, C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2. GRB2 is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. It is ubiquitously expressed in all tissues throughout development and is important in cell cycle progression, motility, morphogenesis, and angiogenesis. In lymphocytes, GRB2 is associated with antigen receptor signaling components. GRB2 contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRB2 binds to Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, as well as to the proline-rich C-terminus of FGRF2. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YVQALFDFDPQEDGELGFRRGDFIEVMDNSDPNWWKGACHGQTGMFPRNYVTP
>gnl|CDD|212883 cd11950, SH3_GRAP2_C, C-terminal Src homology 3 domain of GRB2-related adaptor protein 2. GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also has roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRAP2 binds to different motifs found in substrate peptides including the typical PxxP motif in hematopoietic progenitor kinase 1 (HPK1), the RxxK motif in SLP-76 and HPK1, and the RxxxxK motif in phosphatase-like protein HD-PTP. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QVRALYDFEALEDDELGFNSGDVIEVLDSSNPSWWKGRLHGKLGLFPANYVAP
>gnl|CDD|212884 cd11951, SH3_GRAP_C, C-terminal Src homology 3 domain of GRB2-related adaptor protein. GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domains (SH3c) of the related proteins, GRB2 and GRAP2, have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FVQAQYDFSAEDPSQLSFRRGDIIEVLDCPDPNWWRGRISGRVGFFPRNYVHP
>gnl|CDD|212885 cd11952, SH3_iASPP, Src Homology 3 (SH3) domain of Inhibitor of ASPP protein (iASPP). iASPP, also called RelA-associated inhibitor (RAI), is an oncoprotein that inhibits the apoptotic transactivation potential of p53. It is upregulated in human breast cancers expressing wild-type p53, in acute leukemias regardless of the p53 mutation status, as well as in ovarian cancer where it is associated with poor patient outcome and chemoresistance. iASPP is also a binding partner and negative regulator of p65RelA, which promotes cell proliferation and inhibits apoptosis; p65RelA has the opposite effect on cell growth compared to the p53 family. It contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of iASPP contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GVVYALWDYSAEFPDELSFKEGDMVTVLRKDGEGTDWWWASLCGREGYVPRNYFGL
>gnl|CDD|212886 cd11953, SH3_ASPP2, Src Homology 3 (SH3) domain of Apoptosis Stimulating of p53 protein 2. ASPP2 is the full length form of the previously-identified tumor supressor, p53-binding protein 2 (p53BP2). ASPP2 activates the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73). It plays a central role in regulating apoptosis and cell growth; ASPP2-deficient mice show postnatal death. Downregulated expression of ASPP2 is frequently found in breast tumors, lung cancer, and diffuse large B-cell lymphoma where it is correlated with a poor clinical outcome. ASPP2 contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of ASPP2 contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GVVYALWDYEGESDDELSFKEGDCMTILRREDEDETEWWWARLNDKEGYVPRNLLGL
>gnl|CDD|212887 cd11954, SH3_ASPP1, Src Homology 3 domain of Apoptosis Stimulating of p53 protein 1. ASPP1, like ASPP2, activates the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73). In addition, it functions in the cytoplasm to regulate the nuclear localization of the transcriptional cofactors YAP and TAZ by inihibiting their phosphorylation; YAP and TAZ are important regulators of cell expansion, differentiation, migration, and invasion. ASPP1 is downregulated in breast tumors expressing wild-type p53. It contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of ASPP1 contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GMVYALWDYEAQNADELSFQEGDAITILRRKDDSETEWWWARLNDKEGYVPKNLLGL
>gnl|CDD|212888 cd11955, SH3_srGAP1-3, Src homology 3 domain of Slit-Robo GTPase Activating Proteins 1, 2, and 3. srGAP1, also called Rho GTPase-Activating Protein 13 (ARHGAP13), is a Cdc42- and RhoA-specific GAP and is expressed later in the development of central nervous system tissues. srGAP2 is expressed in zones of neuronal differentiation. It plays a role in the regeneration of neurons and axons. srGAP3, also called MEGAP (MEntal disorder associated GTPase-Activating Protein), is a Rho GAP with activity towards Rac1 and Cdc42. It impacts cell migration by regulating actin and microtubule cytoskeletal dynamics. The association between srGAP3 haploinsufficiency and mental retardation is under debate. srGAPs are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. srGAPs contain an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EAIAKFDYVGRSARELSFKKGASLLLYHRASDDWWEGRHNGIDGLVPHQYIVV
>gnl|CDD|212889 cd11956, SH3_srGAP4, Src homology 3 domain of Slit-Robo GTPase Activating Protein 4. srGAP4, also called ARHGAP4, is highly expressed in hematopoietic cells and may play a role in lymphocyte differentiation. It is able to stimulate the GTPase activity of Rac1, Cdc42, and RhoA. In the nervous system, srGAP4 has been detected in differentiating neurites and may be involved in axon and dendritic growth. srGAPs are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. srGAPs contain an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EVEAVACFDYTGRTAQELSFKRGDVLLLHSKASSDWWRGEHNGMRGLIPHKYISV
>gnl|CDD|212890 cd11957, SH3_RUSC2, Src homology 3 domain of RUN and SH3 domain-containing protein 2. RUSC2, also called Iporin or Interacting protein of Rab1, is expressed ubiquitously with highest amounts in the brain and testis. It interacts with the small GTPase Rab1 and the Golgi matrix protein GM130, and may function in linking GTPases to certain intracellular signaling pathways. RUSC proteins are adaptor proteins consisting of RUN, leucine zipper, and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EVKALCHHIATEPGQLSFNKGDILQVLSRADGDWLRCSLGPDSGLVPIAYVT
>gnl|CDD|212891 cd11958, SH3_RUSC1, Src homology 3 domain of RUN and SH3 domain-containing protein 1. RUSC1, also called NESCA (New molecule containing SH3 at the carboxy-terminus), is highly expressed in the brain and is translocated to the nuclear membrane from the cytoplasm upon stimulation with neurotrophin. It plays a role in facilitating neurotrophin-dependent neurite outgrowth. It also interacts with NEMO (or IKKgamma) and may function in NEMO-mediated activation of NF-kB. RUSC proteins are adaptor proteins consisting of RUN, leucine zipper, and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
AVRALCDHAGSESQLSFRKGEELQVLGTVDEDWIRCRRGDREGLVPVGYTS
>gnl|CDD|212892 cd11959, SH3_Cortactin, Src homology 3 domain of Cortactin. Cortactin was originally identified as a substrate of Src kinase. It is an actin regulatory protein that binds to the Arp2/3 complex and stabilizes branched actin filaments. It is involved in cellular processes that affect cell motility, adhesion, migration, endocytosis, and invasion. It is expressed ubiquitously except in hematopoietic cells, where the homolog hematopoietic lineage cell-specific 1 (HS1) is expressed instead. Cortactin contains an N-terminal acidic domain, several copies of a repeat domain found in cortactin and HS1, a proline-rich region, and a C-terminal SH3 domain. The N-terminal region interacts with the Arp2/3 complex and F-actin, and is crucial in regulating branched actin assembly. Cortactin also serves as a scaffold and provides a bridge to the actin cytoskeleton for membrane trafficking and signaling proteins that bind to its SH3 domain. Binding partners for the SH3 domain of cortactin include dynamin2, N-WASp, MIM, FGD1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TAVALYDYQAADDDEISFDPDDIITNIEMIDEGWWRGVCRGKYGLFPANYVEL
>gnl|CDD|212893 cd11960, SH3_Abp1_eu, Src homology 3 domain of eumetazoan Actin-binding protein 1. Abp1, also called drebrin-like protein, is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a helical domain, and a C-terminal SH3 domain. Mammalian Abp1, unlike yeast Abp1, does not contain an acidic domain that interacts with the Arp2/3 complex. It regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. Abp1 deficiency causes abnormal organ structure and function of the spleen, heart, and lung of mice. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RARALYDYQAADDTEISFDPGDIITDIEQIDEGWWRGTGPDGTYGLFPANYVEL
>gnl|CDD|212894 cd11961, SH3_Abp1_fungi_C2, Second C-terminal Src homology 3 domain of Fungal Actin-binding protein 1. Abp1 is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a central proline-rich region, and a C-terminal SH3 domain (many yeast Abp1 proteins contain two C-terminal SH3 domains). Yeast Abp1 also contains two acidic domains that bind directly to the Arp2/3 complex, which is required to initiate actin polymerization. The SH3 domain of yeast Abp1 binds and localizes the kinases, Ark1p and Prk1p, which facilitate actin patch disassembly following vesicle internalization. It also mediates the localization to the actin patch of the synaptojanin-like protein, Sjl2p, which plays a key role in endocytosis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
WAKALYDYDAAEDNELSFFENDKIINIEFVDDDWWLGECHGSRGLFPSNYVEL
>gnl|CDD|212895 cd11962, SH3_Abp1_fungi_C1, First C-terminal Src homology 3 domain of Fungal Actin-binding protein 1. Abp1 is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a central proline-rich region, and a C-terminal SH3 domain (many yeast Abp1 proteins contain two C-terminal SH3 domains). Yeast Abp1 also contains two acidic domains that bind directly to the Arp2/3 complex, which is required to initiate actin polymerization. The SH3 domain of yeast Abp1 binds and localizes the kinases, Ark1p and Prk1p, which facilitate actin patch disassembly following vesicle internalization. It also mediates the localization to the actin patch of the synaptojanin-like protein, Sjl2p, which plays a key role in endocytosis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RAVVLYDYEKDEDNEIELVEGEIVTNIEMVDEDWWMGTNSKGESGLFPSNYVEL
>gnl|CDD|212896 cd11963, SH3_STAM2, Src homology 3 domain of Signal Transducing Adaptor Molecule 2. STAM2, also called EAST (Epidermal growth factor receptor-associated protein with SH3 and TAM domain) or Hbp (Hrs binding protein), is part of the endosomal sorting complex required for transport (ESCRT-0). It plays a role in sorting mono-ubiquinated endosomal cargo for trafficking to the lysosome for degradation. It is also involved in the regulation of exocytosis. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
ARKVRALYDFEAVEDNELTFKHGEIIIVLDDSDANWWKGENHRGVGLFPSNFVTTDL
>gnl|CDD|212897 cd11964, SH3_STAM1, Src homology 3 domain of Signal Transducing Adaptor Molecule 1. STAM1 is part of the endosomal sorting complex required for transport (ESCRT-0) and is involved in sorting ubiquitinated cargo proteins from the endosome. It may also be involved in the regulation of IL2 and GM-CSF mediated signaling, and has been implicated in neural cell survival. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RKVRAIYDFEAAEDNELTFKAGDIITILDDSDPNWWKGETPQGTGLFPSNFVTAD
>gnl|CDD|212898 cd11965, SH3_ASAP1, Src homology 3 domain of ArfGAP with SH3 domain, ankyrin repeat and PH domain containing protein 1. ASAP1 is also called DDEF1 (Development and Differentiation Enhancing Factor 1), AMAP1, centaurin beta-4, or PAG2. an Arf GTPase activating protein (GAP) with activity towards Arf1 and Arf5 but not Arf6. However, it has been shown to bind GTP-Arf6 stably without GAP activity. It has been implicated in cell growth, migration, and survival, as well as in tumor invasion and malignancy. It binds paxillin and cortactin, two components of invadopodia which are essential for tumor invasiveness. It also binds focal adhesion kinase (FAK) and the SH2/SH3 adaptor CrkL. ASAP1 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RVKTIYDCQADNDDELTFVEGEVIIVTGEEDQEWWIGHIEGQPERKGVFPVSFVHIL
>gnl|CDD|212899 cd11966, SH3_ASAP2, Src homology 3 domain of ArfGAP with SH3 domain, ankyrin repeat and PH domain containing protein 2. ASAP2 is also called DDEF2 (Development and Differentiation Enhancing Factor 2), AMAP2, centaurin beta-3, or PAG3. It mediates the functions of Arf GTPases vial dual mechanisms: it exhibits GTPase activating protein (GAP) activity towards class I (Arf1) and II (Arf5) Arfs; and it binds class III Arfs (GTP-Arf6) stably without GAP activity. It binds paxillin and is implicated in Fcgamma receptor-mediated phagocytosis in macrophages and in cell migration. ASAP2 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RVKALYNCVADNPDELTFSEGEIIIVDGEEDKEWWIGHIDGEPTRRGAFPVSFVHF
>gnl|CDD|212900 cd11967, SH3_SASH1, Src homology 3 domain of SAM And SH3 Domain Containing Protein 1. SASH1 is a potential tumor suppressor in breast and colon cancer. Its decreased expression is associated with aggressive tumor growth, metastasis, and poor prognosis. It is widely expressed in normal tissues (except lymphocytes and dendritic cells) and is localized in the nucleus and the cytoplasm. SASH1 interacts with the oncoprotein cortactin and is important in cell migration and adhesion. It is a member of the SLY family of proteins, which are adaptor proteins containing a central conserved region with a bipartite nuclear localization signal (NLS) as well as SAM (sterile alpha motif) and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GRARVHTDFTPSPYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYVDVL
>gnl|CDD|212901 cd11968, SH3_SASH3, Src homology 3 domain of Sam And SH3 Domain Containing Protein 3. SASH3, also called SLY/SLY1 (SH3-domain containing protein expressed in lymphocytes), is expressed exclusively in lymhocytes and is essential in the full activation of adaptive immunity. It is involved in the signaling of T cell receptors. It was the first described member of the SLY family of proteins, which are adaptor proteins containing a central conserved region with a bipartite nuclear localization signal (NLS) as well as SAM (sterile alpha motif) and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GRARVHTDFIPSPYDGDSLKLQKGDIIQIIEKPPVGTWTGLLNNKVGTFKFIYVDV
>gnl|CDD|212902 cd11969, SH3_PLCgamma2, Src homology 3 domain of Phospholipase C (PLC) gamma 2. PLCgamma2 is primarily expressed in haematopoietic cells, specifically in B cells. It is activated by tyrosine phosphorylation by B cell receptor (BCR) kinases and is recruited to the plasma membrane where its substrate is located. It is required in pre-BCR signaling and in the maturation of B cells. PLCs catalyze the hydrolysis of phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5)P2] to produce Ins(1,4,5)P3 and diacylglycerol (DAG). Ins(1,4,5)P3 initiates the calcium signaling cascade while DAG functions as an activator of PKC. PLCgamma contains a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, two catalytic regions of PLC domains that flank two tandem SH2 domains, followed by a SH3 domain and C2 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TVKALYDYRAKRSDELSFCKGALIHNVSKETGGWWKGDYGGKVQHYFPSNYVEDV
>gnl|CDD|212903 cd11970, SH3_PLCgamma1, Src homology 3 domain of Phospholipase C (PLC) gamma 1. PLCgamma1 is widely expressed and is essential in growth and development. It is activated by the TrkA receptor tyrosine kinase and functions as a key regulator of cell differentiation. It is also the predominant PLCgamma in T cells and is required for T cell and NK cell function. PLCs catalyze the hydrolysis of phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5)P2] to produce Ins(1,4,5)P3 and diacylglycerol (DAG). Ins(1,4,5)P3 initiates the calcium signaling cascade while DAG functions as an activator of PKC. PLCgamma contains a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, two catalytic regions of PLC domains that flank two tandem SH2 domains, followed by a SH3 domain and C2 domain. The SH3 domain of PLCgamma1 directly interacts with dynamin-1 and can serve as a guanine nucleotide exchange factor (GEF). It also interacts with Cbl, inhibiting its phosphorylation and activity. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TFKCAVKALFDYKAQREDELTFTKNAIIQNVEKQEGGWWRGDYGGKKQLWFPSNYVEEIS
>gnl|CDD|212904 cd11971, SH3_Abi1, Src homology 3 domain of Abl Interactor 1. Abi1, also called e3B1, is a central regulator of actin cytoskeletal reorganization through interactions with many protein complexes. It is part of WAVE, a nucleation-promoting factor complex, that links Rac 1 activation to actin polymerization causing lamellipodia protrusion at the plasma membrane. Abi1 interact with formins to promote protrusions at the leading edge of motile cells. It also is a target of alpha4 integrin, regulating membrane protrusions at sites of integrin engagement. Abi proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KVVAIYDYSKDKDDELSFMEGAIIYVIKKNDDGWYEGVCNGVTGLFPGNYVESIMHYAD
>gnl|CDD|212905 cd11972, SH3_Abi2, Src homology 3 domain of Abl Interactor 2. Abi2 is highly expressed in the brain and eye. It regulates actin cytoskeletal reorganization at adherens junctions and dendritic spines, which is important in cell morphogenesis, migration, and cognitive function. Mice deficient with Abi2 show defects in orientation and migration of lens fibers, neuronal migration, dendritic spine morphology, as well as deficits in learning and memory. Abi proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YLEKVVAIYDYTKDKEDELSFQEGAIIYVIKKNDDGWYEGVMNGVTGLFPGNYVESIMHYS
>gnl|CDD|212906 cd11973, SH3_ASEF, Src homology 3 domain of APC-Stimulated guanine nucleotide Exchange Factor. ASEF, also called ARHGEF4, exists in an autoinhibited form and is activated upon binding of the tumor suppressor APC (adenomatous polyposis coli). GEFs activate small GTPases by exchanging bound GDP for free GTP. ASEF can activate Rac1 or Cdc42. Truncated ASEF, which is found in colorectal cancers, is constitutively active and has been shown to promote angiogenesis and cancer cell migration. ASEF contains a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. In its autoinhibited form, the SH3 domain of ASEF forms an extensive interface with the DH and PH domains, blocking the Rac binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GGGEQLAINELISDGSVVCAEALWDHVTMDDQELGFKAGDVIEVMDATNKEWWWGRVLDSEGWFPASFVR
LRV
>gnl|CDD|212907 cd11974, SH3_ASEF2, Src homology 3 domain of APC-Stimulated guanine nucleotide Exchange Factor 2. ASEF2, also called Spermatogenesis-associated protein 13 (SPATA13), is a GEF that localizes with actin at the leading edge of cells and is important in cell migration and adhesion dynamics. GEFs activate small GTPases by exchanging bound GDP for free GTP. ASEF2 can activate both Rac 1 and Cdc42, but only Rac1 activation is necessary for increased cell migration and adhesion turnover. Together with APC (adenomatous polyposis coli) and Neurabin2, a scaffold protein that binds F-actin, it is involved in regulating HGF-induced cell migration. ASEF2 contains a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VYAEALWDHVTMDDQELAFKAGDVIRVLEASNKDWWWGRNEDREAWFPASFVRL
>gnl|CDD|212908 cd11975, SH3_ARHGEF9, Src homology 3 domain of the Rho guanine nucleotide exchange factor ARHGEF9. ARHGEF9, also called PEM2 or collybistin, selectively activates Cdc42 by exchanging bound GDP for free GTP. It is highly expressed in the brain and it interacts with gephyrin, a postsynaptic protein associated with GABA and glycine receptors. Mutations in the ARHGEF9 gene cause X-linked mental retardation with associated features like seizures, hyper-anxiety, aggressive behavior, and sensory hyperarousal. ARHGEF9 contains a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GGSIVSAEAVWDHVTMANRELAFKAGDVIKVLDASNKDWWWGQIDDEEGWFPASFVRLWVNQ
>gnl|CDD|212909 cd11976, SH3_VAV1_2, C-terminal (or second) Src homology 3 domain of VAV1 protein. VAV1 is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The C-terminal SH3 domain of Vav1 interacts with a wide variety of proteins including cytoskeletal regulators (zyxin), RNA-binding proteins (Sam68), transcriptional regulators, viral proteins, and dynamin 2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TAKARYDFCARDRSELSLKEGDIIKILNKKGQQGWWRGEIYGRVGWFPANYVEE
>gnl|CDD|212910 cd11977, SH3_VAV2_2, C-terminal (or second) Src homology 3 domain of VAV2 protein. VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others. It has been reported to associate with Nek3. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GTAVARYNFAARDMRELSLREGDVVRIYSRIGGDQGWWKGETNGRIGWFPSTYVEEEG
>gnl|CDD|212911 cd11978, SH3_VAV3_2, C-terminal (or second) Src homology 3 domain of VAV3 protein. VAV3 is ubiquitously expressed and functions as a phosphorylation-dependent guanine nucleotide exchange factor (GEF) for RhoA, RhoG, and Rac1. It has been implicated to function in the hematopoietic, bone, cerebellar, and cardiovascular systems. VAV3 is essential in axon guidance in neurons that control blood pressure and respiration. It is overexpressed in prostate cancer cells and it plays a role in regulating androgen receptor transcriptional activity. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GIAIARYDFCARDMRELSLLKGDVVKIYTKMSTNGWWRGEVNGRVGWFPSTYVEED
>gnl|CDD|212912 cd11979, SH3_VAV1_1, First Src homology 3 domain of VAV1 protein. VAV1 is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The first SH3 domain of Vav1 has been shown to bind the adaptor protein Grb2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KMEVFQEYYGIPPPPGAFGPFLRLNPGDIVELTKAEAEQNWWEGRNTSTNEIGWFPCNRVKPY
>gnl|CDD|212913 cd11980, SH3_VAV2_1, First Src homology 3 domain of VAV2 protein. VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others. It has been reported to associate with Nek3. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KMVAVQNYHGNPAPPGKPVLTFQTGDVIELLRGDPDSPWWEGRLLQTKKSGYFPSSSVKP
>gnl|CDD|212914 cd11981, SH3_VAV3_1, First Src homology 3 domain of VAV3 protein. VAV3 is ubiquitously expressed and functions as a phosphorylation-dependent guanine nucleotide exchange factor (GEF) for RhoA, RhoG, and Rac1. It has been implicated to function in the hematopoietic, bone, cerebellar, and cardiovascular systems. VAV3 is essential in axon guidance in neurons that control blood pressure and respiration. It is overexpressed in prostate cancer cells and it plays a role in regulating androgen receptor transcriptional activity. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KMQVIRNYSGVPKPQLHGGPPLNAQIGDTIEVLYADPHSLFWQGRNLTTGELGFFPSDAVKP
>gnl|CDD|212915 cd11982, SH3_Shank1, Src homology 3 domain of SH3 and multiple ankyrin repeat domains protein 1. Shank1, also called SSTRIP (Somatostatin receptor-interacting protein), is a brain-specific protein that plays a role in the construction of postsynaptic density (PSD) and the maturation of dendritic spines. Mice deficient in Shank1 show altered PSD composition, thinner PSDs, smaller dendritic spines, and weaker basal synaptic transmission, although synaptic plasticity is normal. They show increased anxiety and impaired fear memory, but also show better spatial learning. Shank proteins carry scaffolding functions through multiple sites of protein-protein interaction in its domain architecture, including ankyrin (ANK) repeats, a long proline rich region, as well as SH3, PDZ, and SAM domains. The SH3 domain of Shank binds GRIP, a scaffold protein that binds AMPA receptors and Eph receptors/ligands. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RTFMAVKPYQSQAEGEISLSKGEKIKVLSVGEGGFWEGQVKGRVGWFPSDCV
>gnl|CDD|212916 cd11983, SH3_Shank2, Src homology 3 domain of SH3 and multiple ankyrin repeat domains protein 2. Shank2, also called ProSAP1 (Proline-rich synapse-associated protein 1) or CortBP1 (Cortactin-binding protein 1), is found in neurons, glia, endocrine cells, liver, and kidney. It plays a role in regulating dendritic spine volume and branching and postsynaptic clustering. Mutations in the Shank2 gene are associated with autism spectrum disorder and mental retardation. Shank proteins carry scaffolding functions through multiple sites of protein-protein interaction in its domain architecture, including ankyrin (ANK) repeats, a long proline rich region, as well as SH3, PDZ, and SAM domains. The SH3 domain of Shank binds GRIP, a scaffold protein that binds AMPA receptors and Eph receptors/ligands. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RHFVVVKSYQPQVEGEIPLHKGDRVKVLSIGEGGFWEGSARGHVGWFPAECV
>gnl|CDD|212917 cd11984, SH3_Shank3, Src homology 3 domain of SH3 and multiple ankyrin repeat domains protein 3. Shank3, also called ProSAP2 (Proline-rich synapse-associated protein 2), is widely expressed. It plays a role in the formation of dendritic spines and synapses. Haploinsufficiency of the Shank3 gene causes the 22q13 deletion/Phelan-McDermid syndrome, and variants of Shank3 have been implicated in autism spectrum disorder, schizophrenia, and intellectual disability. Shank proteins carry scaffolding functions through multiple sites of protein-protein interaction in its domain architecture, including ankyrin (ANK) repeats, a long proline rich region, as well as SH3, PDZ, and SAM domains. The SH3 domain of Shank binds GRIP, a scaffold protein that binds AMPA receptors and Eph receptors/ligands. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RTFIAVKAYSPQGEGEIQLNRGERVKVLSIGEGGFWEGTVKGRTGWFPADCV
>gnl|CDD|212918 cd11985, SH3_Stac2_C, C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing protein 2 (Stac2). Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac2 contains a single SH3 domain at the C-terminus unlike Stac1 and Stac3, which contain two C-terminal SH3 domains. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
SYVALYKFLPQENNDLPLQPGDRVMVVDDSNEDWWKGKSGDRVGFFPANFVQR
>gnl|CDD|212919 cd11986, SH3_Stac3_1, First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing protein 3 (Stac3). Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YFVALYRFKALEKDDLDFHPGERITVIDDSNEEWWRGKIGEKTGYFPMNFIIR
>gnl|CDD|212920 cd11987, SH3_Intersectin1_1, First Src homology 3 domain (or SH3A) of Intersectin-1. Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YYRALYPFEARSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEK
>gnl|CDD|212921 cd11988, SH3_Intersectin2_1, First Src homology 3 domain (or SH3A) of Intersectin-2. Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The first SH3 domain (or SH3A) of ITSN2 is expected to bind many protein partners, similar to ITSN1 which has been shown to bind Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LVNYRALYPFEARNHDEMSFNAGDIIQVDEKTVGEPGWLYGSFQGNFGWFPCNYVEK
>gnl|CDD|212922 cd11989, SH3_Intersectin1_2, Second Src homology 3 domain (or SH3B) of Intersectin-1. Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The second SH3 domain (or SH3B) of ITSN1 has been shown to bind WNK and CdGAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QAQALYPWRAKKDNHLNFNKNDVITVLEQQDMWWFGEVQGQKGWFPKSYVKL
>gnl|CDD|212923 cd11990, SH3_Intersectin2_2, Second Src homology 3 domain (or SH3B) of Intersectin-2. Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The second SH3 domain (or SH3B) of ITSN2 is expected to bind protein partners, similar to ITSN1 which has been shown to bind WNK and CdGAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KAQALCSWTAKKDNHLNFSKNDIITVLEQQENWWFGEVHGGRGWFPKSYVKL
>gnl|CDD|212924 cd11991, SH3_Intersectin1_3, Third Src homology 3 domain (or SH3C) of Intersectin-1. Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The third SH3 domain (or SH3C) of ITSN1 has been shown to bind many proteins including dynamin1/2, CIN85, c-Cbl, SHIP2, Reps1, synaptojanin-1, and WNK, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EYVAMYTYESNEQGDLTFQQGDVILVTKKDGDWWTGTVGDKTGVFPSNYVRP
>gnl|CDD|212925 cd11992, SH3_Intersectin2_3, Third Src homology 3 domain (or SH3C) of Intersectin-2. Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The third SH3 domain (SH3C) of ITSN2 has been shown to bind the K15 protein of Kaposi's sarcoma-associated herpesvirus. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EYIALYPYSSSEPGDLTFNEGEEILVTQKDGEWWTGSIEDRTGIFPSNYVRP
>gnl|CDD|212926 cd11993, SH3_Intersectin1_4, Fourth Src homology 3 domain (or SH3D) of Intersectin-1. Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The fourth SH3 domain (or SH3D) of ITSN1 has been shown to bind SHIP2, Numb, CdGAP, and N-WASP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KKPEIAQVIASYTATGPEQLTLAPGQLILIRKKNPGGWWEGELQARGKKRQIGWFPANYVKLLSP
>gnl|CDD|212927 cd11994, SH3_Intersectin2_4, Fourth Src homology 3 domain (or SH3D) of Intersectin-2. Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The fourth SH3 domain (or SH3D) of ITSN2 is expected to bind protein partners, similar to ITSN1 which has been shown to bind SHIP2, Numb, CdGAP, and N-WASP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
IAQVTTAYVASGVEQLSLSPGQLILILKKNSSGWWLGELQARGKKRQKGWFPASHVKLL
>gnl|CDD|212928 cd11995, SH3_Intersectin1_5, Fifth Src homology 3 domain (or SH3E) of Intersectin-1. Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
CQVIGMYDYTAQNDDELAFSKGQIINVLNKEDPDWWKGELNGQVGLFPSNYVKL
>gnl|CDD|212929 cd11996, SH3_Intersectin2_5, Fifth Src homology 3 domain (or SH3E) of Intersectin-2. Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The fifth SH3 domain (or SH3E) of ITSN2 is expected to bind protein partners, similar to ITSN1 which has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
CQVIAMYDYTANNEDELSFSKGQLINVLNKDDPDWWQGEINGVTGLFPSNYVKM
>gnl|CDD|212930 cd11997, SH3_PACSIN3, Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3). PACSIN 3 or Syndapin III (Synaptic dynamin-associated protein III) is expressed ubiquitously and regulates glucose uptake in adipocytes through its role in GLUT1 trafficking. It also modulates the subcellular localization and stimulus-specific function of the cation channel TRPV4. PACSINs act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GVRVRALYDYTGQEADELSFKAGEELLKIGEEDEQGWCKGRLLSGRIGLYPANYVE
>gnl|CDD|212931 cd11998, SH3_PACSIN1-2, Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) and PACSIN 2. PACSIN 1 or Syndapin I (Synaptic dynamin-associated protein I) is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. PACSIN 2 or Syndapin II is expressed ubiquitously and is involved in the regulation of tubulin polymerization. It associates with Golgi membranes and forms a complex with dynamin II which is crucial in promoting vesicle formation from the trans-Golgi network. PACSINs act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VRVRALYDYDGQEQDELSFKAGDELTKLEDEDEQGWCKGRLDSGQVGLYPANYVEP
>gnl|CDD|212932 cd11999, SH3_PACSIN_like, Src homology 3 domain of an unknown subfamily of proteins with similarity to Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins. PACSINs, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GVRVRAVYDYTGQEPDELSFKAGEELLKVEDEDEQGWCKGVTDGGAVGLYPANYVE
>gnl|CDD|212933 cd12000, SH3_CASS4, Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member 4. CASS4, also called HEPL (HEF1-EFS-p130Cas-like), localizes to focal adhesions and plays a role in regulating FAK activity, focal adhesion integrity, and cell spreading. It is most abundant in blood cells and lung tissue, and is also found in high levels in leukemia and ovarian cell lines. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LLARALYDNKADCSDELAFRRGDILTVLEQNVPGSEGWWKCLLHGRQGLAPANRLQL
>gnl|CDD|212934 cd12001, SH3_BCAR1, Src homology 3 domain of the CAS (Crk-Associated Substrate) scaffolding protein family member, Breast Cancer Anti-estrogen Resistance 1. BCAR1, also called p130cas or CASS1, is the founding member of the CAS family of scaffolding proteins and was originally identified through its ability to associate with Crk. The name BCAR1 was designated because the human gene was identified in a screen for genes that promote resistance to tamoxifen. It is widely expressed and its deletion is lethal in mice. It plays a role in regulating cell motility, survival, proliferation, transformation, cancer progression, and bacterial pathogenesis. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LNVLAKALYDNVAESPDELSFRKGDIMTVLERDTQGLDGWWLCSLHGRQGIVPGNRLKILVGMYDKKQ
>gnl|CDD|212935 cd12002, SH3_NEDD9, Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, Neural precursor cell Expressed, Developmentally Down-regulated 9. NEDD9 is also called human enhancer of filamentation 1 (HEF1) or CAS-L (Crk-associated substrate in lymphocyte). It was first described as a gene predominantly expressed in early embryonic brain, and was also isolated from a screen of human proteins that regulate filamentous budding in yeast, and as a tyrosine phosphorylated protein in lymphocytes. It promotes metastasis in different solid tumors. NEDD9 localizes in focal adhesions and associates with FAK and Abl kinase. It also interacts with SMAD3 and the proteasomal machinery which allows its rapid turnover; these interactions are not shared by other CAS proteins. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
MARALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWLCSLHGRQGIAPGNRLKLL
>gnl|CDD|212936 cd12003, SH3_EFS, Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, Embryonal Fyn-associated Substrate. EFS is also called HEFS, CASS3 (Cas scaffolding protein family member 3) or SIN (Src-interacting protein). It was identified based on interactions with the Src kinases, Fyn and Yes. It plays a role in thymocyte development and acts as a negative regulator of T cell proliferation. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QLAKALYDNAAESPEELSFRRGDVLMVLKREHGSLPGWWLCSLHGQQGIAPANRLRLLPTAP
>gnl|CDD|212937 cd12004, SH3_Lyn, Src homology 3 domain of Lyn Protein Tyrosine Kinase. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
IVVALYPYDGIHEDDLSFKKGEKLKVIEEHGEWWKARSLTTKKEGFIPSNYVAKVN
>gnl|CDD|212938 cd12005, SH3_Lck, Src homology 3 domain of Lck Protein Tyrosine Kinase. Lck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LVVALYSYEPSHDGDLGFEKGEKLRILEQSGEWWKAQSLTTGQEGFIPFNFVAK
>gnl|CDD|212939 cd12006, SH3_Fyn_Yrk, Src homology 3 domain of Fyn and Yrk Protein Tyrosine Kinases. Fyn and Yrk (Yes-related kinase) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAP
>gnl|CDD|212940 cd12007, SH3_Yes, Src homology 3 domain of Yes Protein Tyrosine Kinase. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPAD
>gnl|CDD|212941 cd12008, SH3_Src, Src homology 3 domain of Src Protein Tyrosine Kinase. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK and is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPS
>gnl|CDD|212942 cd12009, SH3_Blk, Src homology 3 domain of Blk Protein Tyrosine Kinase. Blk is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. It is expressed specifically in B-cells and is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
CVIAQYDFVPSNERDLQLKKGEKLQVLKSDGEWWLAKSLTTGKEGYIPSNYVAR
>gnl|CDD|212943 cd12010, SH3_SLAP, Src homology 3 domain of Src-Like Adaptor Protein. SLAP (or SLA1) modulates TCR surface expression levels as well as surface and total BCR levels. As an adaptor to c-Cbl, SLAP increases the ubiquitination, intracellular retention, and targeted degradation of the BCR complex components. SLAP has been shown to interact with the EphA receptor, EpoR, Lck, PDGFR, Syk, CD79a, c-Cbl, LAT, CD247, and Zap70, among others. SLAPs are adaptor proteins with limited similarity to Src family tyrosine kinases. They contain an N-terminal SH3 domain followed by an SH2 domain, and a unique C-terminal sequence. The SH3 domain of SLAP forms a complex with v-Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FLAVLADYPSPDISEPIFHMGEKLRVLSDEGGWWKVRSLQTGRENYIPGKCVAKV
>gnl|CDD|212944 cd12011, SH3_SLAP2, Src homology 3 domain of Src-Like Adaptor Protein 2. SLAP2 plays a role in c-Cbl-dependent regulation of CSF1R, a tyrosine kinase important for myeloid cell growth and differentiation. It has been shown to interact with CSF1R, c-Cbl, LAT, CD247, and Zap70. SLAPs are adaptor proteins with limited similarity to Src family tyrosine kinases. They contain an N-terminal SH3 domain followed by an SH2 domain, and a unique C-terminal sequence. They function in regulating the signaling, ubiquitination, and trafficking of T-cell receptor (TCR) and B-cell receptor (BCR) components. The SH3 domain of SLAP forms a complex with v-Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VAVALCNFPSGGPTELSIRMGEQLTILSEDGDWWKVSSAVTGRECYIPSNYVAKV
>gnl|CDD|212945 cd12012, SH3_RIM-BP_2, Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins. RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LFVALFDYDPLTMSPNPDAAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE
>gnl|CDD|212946 cd12013, SH3_RIM-BP_3, Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins. RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RMVALFDYDPRESSPNVDAEVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE
>gnl|CDD|212947 cd12014, SH3_RIM-BP_1, First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins. RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VFVARYSYNPLRDSPNENPEAELPLNAGDYVYVYGDMDEDGFYEGELLDGRRGLVPSNFVER
>gnl|CDD|212948 cd12015, SH3_Tks_1, First Src homology 3 domain of Tyrosine kinase substrate (Tks) proteins. Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Vertebrates contain two Tks proteins, Tks4 (Tyr kinase substrate with four SH3 domains) and Tks5 (Tyr kinase substrate with five SH3 domains), which display partially overlapping but non-redundant functions. Both associate with the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. Tks5 interacts with N-WASP and Nck, while Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. Tks proteins contain an N-terminal Phox homology (PX) domain and four or five SH3 domains. This model characterizes the first SH3 domain of Tks proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QYVVVADYKKQQPNEISLRAGDVVDVIEKNENGWWFVSLEDEQGWVPATYLEP
>gnl|CDD|212949 cd12016, SH3_Tks_2, Second Src homology 3 domain of Tyrosine kinase substrate (Tks) proteins. Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Vertebrates contain two Tks proteins, Tks4 (Tyr kinase substrate with four SH3 domains) and Tks5 (Tyr kinase substrate with five SH3 domains), which display partially overlapping but non-redundant functions. Both associate with the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. Tks5 interacts with N-WASP and Nck, while Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. Tks proteins contain an N-terminal Phox homology (PX) domain and four or five SH3 domains. This model characterizes the second SH3 domain of Tks proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EKYITTQAYKAENEDEIGFETGVVVEVIQKNLDGWWKIRYQGKEGWAPATYLKK
>gnl|CDD|212950 cd12017, SH3_Tks_3, Third Src homology 3 domain of Tyrosine kinase substrate (Tks) proteins. Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Vertebrates contain two Tks proteins, Tks4 (Tyr kinase substrate with four SH3 domains) and Tks5 (Tyr kinase substrate with five SH3 domains), which display partially overlapping but non-redundant functions. Both associate with the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. Tks5 interacts with N-WASP and Nck, while Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. Tks proteins contain an N-terminal Phox homology (PX) domain and four or five SH3 domains. This model characterizes the third SH3 domain of Tks proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EYFTIGEFQATIQDGISFQKGQKVEVIDKNPSGWWYVKIDGKEGWAPSSYIEK
>gnl|CDD|212951 cd12018, SH3_Tks4_4, Fourth (C-terminal) Src homology 3 domain of Tyrosine kinase substrate with four SH3 domains. Tks4, also called SH3 and PX domain-containing protein 2B (SH3PXD2B) or HOFI, is a Src substrate and scaffolding protein that plays an important role in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. It is required in the formation of functional podosomes, EGF-induced membrane ruffling, and lamellipodia generation. It plays an important role in cellular attachment and cell spreading. Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. It contains an N-terminal Phox homology (PX) domain and four SH3 domains. This model characterizes the fourth (C-terminal) SH3 domain of Tks4. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LYVAVADFEGDEDTSSFKEGTVFEVREKNSSGWWFCKVLSGGPVWEGWIPSNYLRK
>gnl|CDD|212952 cd12019, SH3_Tks5_4, Fourth Src homology 3 domain of Tyrosine kinase substrate with five SH3 domains. Tks5, also called SH3 and PX domain-containing protein 2A (SH3PXD2A) or Five SH (FISH), is a scaffolding protein and Src substrate that is localized in podosomes, which are electron-dense structures found in Src-transformed fibroblasts, osteoclasts, macrophages, and some invasive cancer cells. It binds and regulates some members of the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. It is required for podosome formation, degradation of the extracellular matrix, and cancer cell invasion. Tks5 contains an N-terminal Phox homology (PX) domain and five SH3 domains. This model characterizes the fourth SH3 domain of Tks5. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
SYMTTSAYQKVQDSEISFPAGVEVEVLEKQESGWWYVRFGELEGWAPSHYLEL
>gnl|CDD|212953 cd12020, SH3_Tks5_5, Fifth (C-terminal) Src homology 3 domain of Tyrosine kinase substrate with five SH3 domains. Tks5, also called SH3 and PX domain-containing protein 2A (SH3PXD2A) or Five SH (FISH), is a scaffolding protein and Src substrate that is localized in podosomes, which are electron-dense structures found in Src-transformed fibroblasts, osteoclasts, macrophages, and some invasive cancer cells. It binds and regulates some members of the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. It is required for podosome formation, degradation of the extracellular matrix, and cancer cell invasion. Tks5 contains an N-terminal Phox homology (PX) domain and five SH3 domains. This model characterizes the fifth (C-terminal) SH3 domain of Tks5. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VYVSIADYEGDEETAGFQEGVSMEVLEKNPNGWWYCQILDGVKPFKGWVPSNYLEKK
>gnl|CDD|212954 cd12021, SH3_p47phox_1, First or N-terminal Src homology 3 domain of the p47phox subunit of NADPH oxidase, also called Neutrophil Cytosolic Factor 1. p47phox, or NCF1, is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox), which plays a key role in the ability of phagocytes to defend against bacterial infections. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p47phox is required for activation of NADH oxidase and plays a role in translocation. It contains an N-terminal Phox homology (PX) domain, tandem SH3 domains (N-SH3 and C-SH3), a polybasic/autoinhibitory region, and a C-terminal proline-rich region (PRR). This model characterizes the first SH3 domain (or N-SH3) of p47phox. In its inactive state, the tandem SH3 domains interact intramolecularly with the autoinhibitory region; upon activation, the tandem SH3 domains are exposed through a conformational change, resulting in their binding to the PRR of p22phox and the activation of NADPH oxidase. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TYRAIADYEKSSKSEMALKTGDVVEVVEKSENGWWFCQLKAKRGWVPASYLEP
>gnl|CDD|212955 cd12022, SH3_p47phox_2, Second or C-terminal Src homology 3 domain of the p47phox subunit of NADPH oxidase, also called Neutrophil Cytosolic Factor 1. p47phox, or NCF1, is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox), which plays a key role in the ability of phagocytes to defend against bacterial infections. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p47phox is required for activation of NADH oxidase and plays a role in translocation. It contains an N-terminal Phox homology (PX) domain, tandem SH3 domains (N-SH3 and C-SH3), a polybasic/autoinhibitory region, and a C-terminal proline-rich region (PRR). This model characterizes the second SH3 domain (or C-SH3) of p47phox. In its inactive state, the tandem SH3 domains interact intramolecularly with the autoinhibitory region; upon activation, the tandem SH3 domains are exposed through a conformational change, resulting in their binding to the PRR of p22phox and the activation of NADPH oxidase. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LYITIKAYTAVEEDELTLLEGEAIEVIHKLLDGWWVVRKGEVTGYFPSMYLQK
>gnl|CDD|212956 cd12023, SH3_NoxO1_1, First or N-terminal Src homology 3 domain of Nox Organizing protein 1. Nox Organizing protein 1 (NoxO1) is a critical regulator of enzyme kinetics of the nonphagocytic NADPH oxidase Nox1, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Nox1 is expressed in colon, stomach, uterus, prostate, and vascular smooth muscle cells. NoxO1 is involved in targeting activator subunits (such as NoxA1) to Nox1. It is co-localized with Nox1 in the membranes of resting cells and directs the subcellular localization of Nox1. NoxO1 contains an N-terminal Phox homology (PX) domain, tandem SH3 domains (N-SH3 and C-SH3), and a C-terminal proline-rich region (PRR). This model characterizes the first SH3 domain (or N-SH3) of NoxO1. The tandem SH3 domains of NoxO1 interact with the PRR of p22phox, which also complexes with Nox1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
SYRCLAPFETKDTKNKPFKAAAQESLDVLLKDPTGWWLVENEDRQIAWFPAPYLEE
>gnl|CDD|212957 cd12024, SH3_NoxO1_2, Second or C-terminal Src homology 3 domain of NADPH oxidase (Nox) Organizing protein 1. Nox Organizing protein 1 (NoxO1) is a critical regulator of enzyme kinetics of the nonphagocytic NADPH oxidase Nox1, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Nox1 is expressed in colon, stomach, uterus, prostate, and vascular smooth muscle cells. NoxO1 is involved in targeting activator subunits (such as NoxA1) to Nox1. It is co-localized with Nox1 in the membranes of resting cells and directs the subcellular localization of Nox1. NoxO1 contains an N-terminal Phox homology (PX) domain, tandem SH3 domains (N-SH3 and C-SH3), and a C-terminal proline-rich region (PRR). This model characterizes the second SH3 domain (or C-SH3) of NoxO1. The tandem SH3 domains of NoxO1 interact with the PRR of p22phox, which also complexes with Nox1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LYYATRAYEAQKEDELSVPAGVVVEVLQKSDNGWWLIRYNGRAGYVPSMYLQP
>gnl|CDD|212958 cd12025, SH3_Obscurin_like, Src homology 3 domain of Obscurin and similar proteins. Obscurin is a giant muscle protein that is concentrated at the peripheries of Z-disks and M-lines. It binds small ankyrin I, a component of the sarcoplasmic reticulum (SR) membrane. It is associated with the contractile apparatus through binding with titin and sarcomeric myosin. It plays important roles in the organization and assembly of the myofibril and the SR. Obscurin has been observed as alternatively-spliced isoforms. The major isoform in sleletal muscle, approximately 800 kDa in size, is composed of many adhesion modules and signaling domains. It harbors 49 Ig and 2 FNIII repeats at the N-terminues, a complex middle region with additional Ig domains, an IQ motif, and a conserved SH3 domain near RhoGEF and PH domains, and a non-modular C-terminus with phosphorylation motifs. The obscurin gene also encodes two kinase domains, which are not part of the 800 kDa form of the protein, but is part of smaller spliced products that present in heart muscle. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FDVYIVTADYTPDGADTEAIPLEEGQYVEVLDSAHPLKWLVRTKPTKSSPPRQGWVSPAYLEK
>gnl|CDD|212959 cd12026, SH3_ZO-1, Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1. ZO-1 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-1 plays an essential role in embryonic development. It regulates the assembly and dynamics of the cortical cytoskeleton at cell-cell junctions. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-1 is the largest of the three ZO proteins and contains an actin-binding region and domains of unknown function designated alpha and ZU5. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
DSFYIRTHFEYEKESPYGLSFNKGEVFRVVDTLYNGKLGSWLAIRIGKNHKEVERGIIPNKNRAE
>gnl|CDD|212960 cd12027, SH3_ZO-2, Src homology 3 domain of the Tight junction protein, Zonula occludens protein 2. ZO-2 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-2 plays an essential role in embryonic development. It is critical for the blood-testis barrier integrity and male fertility. It also regulates the expression of cyclin D1 and cell proliferation. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-2 contains an actin-binding region and a domain of unknown function designated beta. The SH3 domain of the related protein ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GDSFFIRTHFEYEKELPQSLAFTRGEIFRVVDTLYDGKLGNWLAVRIGNELEKGLIPNKSRAE
>gnl|CDD|212961 cd12028, SH3_ZO-3, Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3. ZO-3 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-3 is critical for epidermal barrier function. It regulates cyclin D1-dependent cell proliferation. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-3 is the smallest of the three ZO proteins. The SH3 domain of the related protein ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
DSFYIRTHFDYEPDPPSGLSFTRGEVFHVLDTMHRGKLGSWLAVRMGRDLREMEKGIIPNQSRAE
>gnl|CDD|212962 cd12029, SH3_DLG3, Src Homology 3 domain of Disks Large homolog 3. DLG3, also called synapse-associated protein 102 (SAP102), is a scaffolding protein that clusters at synapses and plays an important role in synaptic development and plasticity. Mutations in DLG3 cause midgestational embryonic lethality in mice and may be associated with nonsyndromic X-linked mental retardation in humans. It interacts with the NEDD4 (neural precursor cell-expressed developmentally downregulated 4) family of ubiquitin ligases and promotes apical tight junction formation. DLG3 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG3 contains three PDZ domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RSLYVRALFDYDRTRDSCLPSQGLSFSYGDILHVINASDDEWWQARLVTPHGESEQIGVIPSKKRVE
>gnl|CDD|212963 cd12030, SH3_DLG4, Src Homology 3 domain of Disks Large homolog 4. DLG4, also called postsynaptic density-95 (PSD95) or synapse-associated protein 90 (SAP90), is a scaffolding protein that clusters at synapses and plays an important role in synaptic development and plasticity. It is responsible for the membrane clustering and retention of many transporters and receptors such as potassium channels and PMCA4b, a P-type ion transport ATPase, among others. DLG4 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG4 contains three PDZ domains. The SH3 domain of DLG4 binds and clusters the kainate subgroup of glutamate receptors via two proline-rich sequences in their C-terminal tail. It also binds AKAP79/150 (A-kinase anchoring protein). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GFYIRALFDYDKTKDCGFLSQALSFRFGDVLHVIDAGDEEWWQARRVHSDSETEEIGFIPSKRRVE
>gnl|CDD|212964 cd12031, SH3_DLG1, Src Homology 3 domain of Disks Large homolog 1. DLG1, also called synapse-associated protein 97 (SAP97), is a scaffolding protein that clusters at synapses and plays an important role in synaptic development and plasticity. DLG1 plays roles in regulating cell polarity, proliferation, migration, and cycle progression. It interacts with AMPA-type glutamate receptors and is critical in their maturation and delivery to synapses. It also interacts with PKCalpha and promotes wound healing. DLG1 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG1 contains three PDZ domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVVNASDDEWWQARQVTADGESEEIGVIPSKRRVE
>gnl|CDD|212965 cd12032, SH3_DLG2, Src Homology 3 domain of Disks Large homolog 2. DLG2, also called postsynaptic density-93 (PSD93) or Channel-associated protein of synapse-110 (chapsyn 110), is a scaffolding protein that clusters at synapses and plays an important role in synaptic development and plasticity. The DLG2 delta isoform binds inwardly rectifying potassium Kir2 channels, which determine resting membrane potential in neurons. It regulates the spatial and temporal distribution of Kir2 channels within neuronal membranes. DLG2 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG2 contains three PDZ domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
NQKRSLYVRAMFDYEKSKDSGLPSQGLSFRYGDILHVINASDDEWWQARRVTPDGDSEEMGVIPSKRRVE
RKER
>gnl|CDD|212966 cd12033, SH3_MPP7, Src Homology 3 domain of Membrane Protein, Palmitoylated 7 (or MAGUK p55 subfamily member 7). MPP7 is a scaffolding protein that binds to DLG1 and promotes tight junction formation and epithelial cell polarity. Mutations in the MPP7 gene may be associated with the pathogenesis of diabetes and extreme bone mineral density. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FIKALFDYNPNEDKAIPCKEAGLSFKKGDILQIMSQDDATWWQAKHEGDANPRAGLIPSKH
>gnl|CDD|212967 cd12034, SH3_MPP4, Src Homology 3 domain of Membrane Protein, Palmitoylated 4 (or MAGUK p55 subfamily member 4). MPP4, also called Disks Large homolog 6 (DLG6) or Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 5 protein (ALS2CR5), is a retina-specific scaffolding protein that plays a role in organizing presynaptic protein complexes in the photoreceptor synapse, where it localizes to the plasma membrane. It is required in the proper localization of calcium ATPases and for maintenance of calcium homeostasis. MPP4 is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YVRAMVDYWPQQDPSIPCADAGLPFRKGDILQIVDQNDSLWWQARKLSDLAACAGLIPSNH
>gnl|CDD|212968 cd12035, SH3_MPP1-like, Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1)-like proteins. This subfamily includes MPP1, CASK (Calcium/calmodulin-dependent Serine protein Kinase), Caenorhabditis elegans lin-2, and similar proteins. MPP1 and CASK are scaffolding proteins from the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). In addition, they also have the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. CASK and lin-2 also contain an N-terminal calmodulin-dependent kinase (CaMK)-like domain and two L27 domains. MPP1 is ubiquitously-expressed and plays roles in regulating neutrophil polarity, cell shape, hair cell development, and neural development and patterning of the retina. CASK is highly expressed in the mammalian nervous system and plays roles in synaptic protein targeting, neural development, and gene expression regulation. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YVRAQFDYDPSKDDLIPCQQAGIAFKTGDILQIISKDDHNWWQARKPGASKEPAGLIPSPEL
>gnl|CDD|212969 cd12036, SH3_MPP5, Src Homology 3 domain of Membrane Protein, Palmitoylated 5 (or MAGUK p55 subfamily member 5). MPP5, also called PALS1 (Protein associated with Lin7) or Nagie oko protein in zebrafish or Stardust in Drosophila, is a scaffolding protein which associates with Crumbs homolog 1 (CRB1), CRB2, or CRB3 through its PDZ domain and with PALS1-associated tight junction protein (PATJ) or multi-PDZ domain protein 1 (MUPP1) through its L27 domain. The resulting tri-protein complexes are core proteins of the Crumb complex, which localizes at tight junctions or subapical regions, and is involved in the maintenance of apical-basal polarity in epithelial cells and the morphogenesis and function of photoreceptor cells. MPP5 is critical for the proper stratification of the retina and is also expressed in T lymphocytes where it is important for TCR-mediated activation of NFkB. Drosophila Stardust exists in several isoforms, some of which show opposing functions in photoreceptor cells, which suggests that the relative ratio of different Crumbs complexes regulates photoreceptor homeostasis. MPP5 contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
HVRAHFDYDPEDDPYIPCRELGLSFQKGDILHVISQEDPNWWQAYREGEEDNQSLAGLIPSKS
>gnl|CDD|212970 cd12037, SH3_MPP2, Src Homology 3 domain of Membrane Protein, Palmitoylated 2 (or MAGUK p55 subfamily member 2). MPP2 is a scaffolding protein that interacts with the non-receptor tyrosine kinase c-Src in epithelial cells to negatively regulate its activity and morphological function. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FVKCHFDYDPSSDSLIPCKEAGLKFRAGDLLQIVNQEDPNWWQACHVEGGSAGLIPSQL
>gnl|CDD|212971 cd12038, SH3_MPP6, Src Homology 3 domain of Membrane Protein, Palmitoylated 6 (or MAGUK p55 subfamily member 6). MPP6, also called Veli-associated MAGUK 1 (VAM-1) or PALS2, is a scaffolding protein that binds to Veli-1, a homolog of Caenorhabditis Lin-7. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FVKCHFDYNPYNDNLIPCKEAGLKFSKGEILQIVNREDPNWWQASHVKEGGSAGLIPSQFL
>gnl|CDD|212972 cd12039, SH3_MPP3, Src Homology 3 domain of Membrane Protein, Palmitoylated 3 (or MAGUK p55 subfamily member 3). MPP3 is a scaffolding protein that colocalizes with MPP5 and CRB1 at the subdpical region adjacent to adherens junctions and may function in photoreceptor polarity. It interacts with some nectins and regulates their trafficking and processing. Nectins are cell-cell adhesion proteins involved in the establishment apical-basal polarity at cell adhesion sites. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FMRALFDYNPYEDRAIPCQEAGLPFKRRDILEVVSQDDPTWWQAKRVGDTNLRAGLIPSKQF
>gnl|CDD|212973 cd12040, SH3_CACNB2, Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta2. The beta2 subunit of voltage-dependent calcium channels (Ca(V)s) is one of four beta subunits present in vertebrates. It is expressed in the heart and is present in specific neuronal cells including cerebellar Purkinje cells, hippocampal pyramidal neurons, and photoreceptors. Knockout of the beta2 gene in mice results in embryonic lethality, demonstrating its importance in development. Ca(V)s are multi-protein complexes that regulate the entry of calcium into cells. They impact muscle contraction, neuronal migration, hormone and neurotransmitter release, and the activation of calcium-dependent signaling pathways. They are composed of four subunits: alpha1, alpha2delta, beta, and gamma. The beta subunit is a soluble and intracellular protein that interacts with the transmembrane alpha1 subunit. It facilitates the trafficking and proper localization of the alpha1 subunit to the cellular plasma membrane. Vertebrates contain four different beta subunits from distinct genes (beta1-4); each exists as multiple splice variants. All are expressed in the brain while other tissues show more specific expression patterns. The beta subunits show similarity to MAGUK (membrane-associated guanylate kinase) proteins in that they contain SH3 and inactive guanylate kinase (GuK) domains; however, they do not appear to contain a PDZ domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
TKPVAFAVRTNVGYSAAHEDDVPVPGMAISFEAKDFLHVKEKFNNDWWIGRLVKEGCEIGFIPSPVKLE
>gnl|CDD|212974 cd12041, SH3_CACNB1, Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta-1. The beta1 subunit of voltage-dependent calcium channels (Ca(V)s) is one of four beta subunits present in vertebrates. It is the only beta subunit, as the beta1a variant, expressed in skeletal muscle; the beta1b variant is also widely expressed in other tissues including the heart and brain. Knockout of the beta1 gene in mice results in embryonic lethality, demonstrating its importance in development. Ca(V)s are multi-protein complexes that regulate the entry of calcium into cells. They impact muscle contraction, neuronal migration, hormone and neurotransmitter release, and the activation of calcium-dependent signaling pathways. They are composed of four subunits: alpha1, alpha2delta, beta, and gamma. The beta subunit is a soluble and intracellular protein that interacts with the transmembrane alpha1 subunit. It facilitates the trafficking and proper localization of the alpha1 subunit to the cellular plasma membrane. Vertebrates contain four different beta subunits from distinct genes (beta1-4); each exists as multiple splice variants. All are expressed in the brain while other tissues show more specific expression patterns. The beta subunits show similarity to MAGUK (membrane-associated guanylate kinase) proteins in that they contain SH3 and inactive guanylate kinase (GuK) domains; however, they do not appear to contain a PDZ domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KPVAFAVRTNVGYNPSPGDDVPVQGMAISFEPKDFLHIKEKYNNDWWIGRLVKEGCEVGFIPSPVKLE
>gnl|CDD|212975 cd12042, SH3_CACNB3, Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta3. The beta3 subunit of voltage-dependent calcium channels (Ca(V)s) is one of four beta subunits present in vertebrates. It is the main beta subunit present in smooth muscles and is strongly expressed in the brain; it is predominant in the olfactory bulb, cortex, and hippocampus. It may play a role in regulating the NMDAR (N-methyl-d-aspartate receptor) activity in the hippocampus and thus, activity-dependent synaptic plasticity and cognitive behaviors. Ca(V)s are multi-protein complexes that regulate the entry of calcium into cells. They impact muscle contraction, neuronal migration, hormone and neurotransmitter release, and the activation of calcium-dependent signaling pathways. They are composed of four subunits: alpha1, alpha2delta, beta, and gamma. The beta subunit is a soluble and intracellular protein that interacts with the transmembrane alpha1 subunit. It facilitates the trafficking and proper localization of the alpha1 subunit to the cellular plasma membrane. Vertebrates contain four different beta subunits from distinct genes (beta1-4); each exists as multiple splice variants. All are expressed in the brain while other tissues show more specific expression patterns. The beta subunits show similarity to MAGUK (membrane-associated guanylate kinase) proteins in that they contain SH3 and inactive guanylate kinase (GuK) domains; however, they do not appear to contain a PDZ domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KPVAFAVRTNVSYCGALDEECPVQGAAINFEAKDFLHIKEKYSNDWWIGRLVKEGGDIAFIPSPQRLE
>gnl|CDD|212976 cd12043, SH3_CACNB4, Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta4. The beta4 subunit of voltage-dependent calcium channels (Ca(V)s) is one of four beta subunits present in vertebrates. It is the only beta subunit expressed in the cochlea and is highly expressed in the brain, predominantly in the cerebellum. Ca(V)s are multi-protein complexes that regulate the entry of calcium into cells. They impact muscle contraction, neuronal migration, hormone and neurotransmitter release, and the activation of calcium-dependent signaling pathways. They are composed of four subunits: alpha1, alpha2delta, beta, and gamma. The beta subunit is a soluble and intracellular protein that interacts with the transmembrane alpha1 subunit. It facilitates the trafficking and proper localization of the alpha1 subunit to the cellular plasma membrane. Vertebrates contain four different beta subunits from distinct genes (beta1-4); each exists as multiple splice variants. All are expressed in the brain while other tissues show more specific expression patterns. The beta subunits show similarity to MAGUK (membrane-associated guanylate kinase) proteins in that they contain SH3 and inactive guanylate kinase (GuK) domains; however, they do not appear to contain a PDZ domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KPVAFAVRTNVSYCGALDEDVPVPGTAISFDAKDFLHIKEKYNNDWWIGRLVKEGCEIGFIPSPLRLE
>gnl|CDD|212977 cd12044, SH3_SKAP1, Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1. SKAP1, also called SKAP55 (Src kinase-associated protein of 55kDa), is an immune cell-specific adaptor protein that plays an important role in T-cell adhesion, migration, and integrin clustering. It is expressed exclusively in T-lymphocytes, mast cells, and macrophages. Binding partners include ADAP (adhesion and degranulation-promoting adaptor protein), Fyn, Riam, RapL, and RasGRP. It contains a pleckstrin homology (PH) domain, a C-terminal SH3 domain, and several tyrosine phosphorylation sites. The SH3 domain of SKAP1 is necessary for its ability to regulate T-cell conjugation with antigen-presenting cells and the formation of LFA-1 clusters. SKAP1 binds primarily to a proline-rich region of ADAP through its SH3 domain; its degradation is regulated by ADAP. A secondary interaction occurs via the ADAP SH3 domain and the RKxxYxxY motif in SKAP1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YYQGLWDCFGDNPDELSFQRGDLIYILSKEYNMYGWWVGELNGIVGIVPKDYL
>gnl|CDD|212978 cd12045, SH3_SKAP2, Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 2. SKAP2, also called SKAP55-Related (SKAP55R) or SKAP55 homolog (SKAP-HOM or SKAP55-HOM), is an immune cell-specific adaptor protein that plays an important role in adhesion and migration of B-cells and macrophages. Binding partners include ADAP (adhesion and degranulation-promoting adaptor protein), YopH, SHPS1, and HPK1. SKAP2 has also been identified as a substrate for lymphoid-specific tyrosine phosphatase (Lyp), which has been implicated in a wide variety of autoimmune diseases. It contains a pleckstrin homology (PH) domain, a C-terminal SH3 domain, and several tyrosine phosphorylation sites. Like SKAP1, SKAP2 is expected to bind primarily to a proline-rich region of ADAP through its SH3 domain; its degradation may be regulated by ADAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FYQGLWDCTGDQPDELSFKRGDTIYILSKEYNRFGWWVGEMKGTIGLVPKAYI
>gnl|CDD|212979 cd12046, SH3_p67phox_C, C-terminal (or second) Src Homology 3 domain of the p67phox subunit of NADPH oxidase. p67phox, also called Neutrophil cytosol factor 2 (NCF-2), is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p67phox plays a regulatory role and contains N-terminal TPR, first SH3 (or N-terminal or central SH3), PB1, and C-terminal SH3 domains. It binds, via its C-terminal SH3 domain, to a proline-rich region of p47phox and upon activation, this complex assembles with flavocytochrome b558, the Nox2-p22phox heterodimer. Concurrently, RacGTP translocates to the membrane and interacts with the TPR domain of p67phox, which leads to the activation of NADPH oxidase. The PB1 domain of p67phox binds to its partner PB1 domain in p40phox, and this facilitates the assembly of p47phox-p67phox at the membrane. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QVVALFSYEASQPEDLEFQKGDVILVLSKVNEDWLEGQCKGKIGIFPSAFVED
>gnl|CDD|212980 cd12047, SH3_Noxa1_C, C-terminal Src Homology 3 domain of NADPH oxidase activator 1. Noxa1 is a homolog of p67phox and is a cytosolic subunit of the nonphagocytic NADPH oxidase complex Nox1, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Noxa1 is co-expressed with Nox1 in colon, stomach, uterus, prostate, and vascular smooth muscle cells, consistent with its regulatory role. It does not interact with p40phox, unlike p67phox, making Nox1 activity independent of p40phox, unlike Nox2. Noxa1 contains TPR, PB1, and C-terminal SH3 domains, but lacks the central SH3 domain that is present in p67phox. The TPR domain binds activated GTP-bound Rac. The C-terminal SH3 domain binds the polyproline motif found at the C-terminus of Noxo1, a homolog of p47phox. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RMVAQHDYSAQGPEDLEFSQGDTIDILSEVNQEWLEGHCDGRIGIFPKCFAVR
>gnl|CDD|212981 cd12048, SH3_DOCK3_B, Src Homology 3 domain of Class B Dedicator of Cytokinesis 3. Dock3, also called modifier of cell adhesion (MOCA), and presenilin binding protein (PBP), is a class B DOCK and is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. It regulates N-cadherin dependent cell-cell adhesion, cell polarity, and neuronal morphology. It promotes axonal growth by stimulating actin polymerization and microtubule assembly. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate while DHR-2 contains the catalytic activity for Rac and/or Cdc42. Class B DOCKs also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus; Dock3 is a specific GEFs for Rac. The SH3 domain of Dock3 binds to DHR-2 in an autoinhibitory manner; binding of the scaffold protein Elmo to the SH3 domain of Dock3 exposes the DHR-2 domain and promotes GEF activity. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YGVVICSFRGSVPQGLVLELGETVQILEKCEGWYRGVSIKKPNVKGIFPANYIHLK
>gnl|CDD|212982 cd12049, SH3_DOCK4_B, Src Homology 3 domain of Class B Dedicator of Cytokinesis 4. Dock4 is a class B DOCK and is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. It plays a role in regulating dendritic growth and branching in hippocampal neurons, where it is highly expressed. It may also regulate spine morphology and synapse formation. Dock4 activates the Ras family GTPase Rap1, probably indirectly through interaction with Rap regulatory proteins. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate while DHR-2 contains the catalytic activity for Rac and/or Cdc42. Class B DOCKs also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus. The SH3 domain of Dock4 binds to DHR-2 in an autoinhibitory manner; binding of the scaffold protein Elmo to the SH3 domain of Dock4 exposes the DHR-2 domain and promotes GEF activity. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YGVVVASFRGTVQHGLTLEIGDTVQILEKCEGWYRGFALKNPNVKGIFPQLYLHLK
>gnl|CDD|212983 cd12050, SH3_DOCK2_A, Src Homology 3 domain of Class A Dedicator of Cytokinesis protein 2. Dock2 is a hematopoietic cell-specific, class A DOCK and is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. It plays an important role in lymphocyte migration and activation, T-cell differentiation, neutrophil chemotaxis, and type I interferon induction. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate while DHR-2 contains the catalytic activity for Rac and/or Cdc42. Class A DOCKs also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus; they are specific GEFs for Rac. The SH3 domain of Dock2 binds to DHR-2 in an autoinhibitory manner; binding of the scaffold protein Elmo to the SH3 domain of Dock2 exposes the DHR-2 domain and promotes GEF activity. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YGVAIYNFKGSGVPQLSLQIGDVVHIQETCEDWYKGYLVRHKDLQGIFPKSFIHIK
>gnl|CDD|212984 cd12051, SH3_DOCK1_5_A, Src Homology 3 domain of Class A Dedicator of Cytokinesis proteins 1 and 5. Dock1, also called Dock180, and Dock5 are class A DOCKs and are atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. Dock1 interacts with the scaffold protein Elmo and the resulting complex functions upstream of Rac in many biological events including phagocytosis of apoptotic cells, cell migration and invasion. Dock5 functions upstream of Rac1 to regulate osteoclast function. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate while DHR-2 contains the catalytic activity for Rac and/or Cdc42. Class A DOCKs also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus; they are specific GEFs for Rac. The SH3 domain of Dock1 binds to DHR-2 in an autoinhibitory manner; binding of Elmo to the SH3 domain of Dock1 exposes the DHR-2 domain and promotes GEF activity. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YGVAIYNYDARGPDELSLQIGDTVHILETYEGWYRGYTLRKKSKKGIFPASYIHLK
>gnl|CDD|212985 cd12052, SH3_CIN85_1, First Src Homology 3 domain (SH3A) of Cbl-interacting protein of 85 kDa. CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the first SH3 domain (SH3A) of CIN85; SH3A binds to internal proline-rich motifs within the proline-rich region. This intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. SH3A has also been shown to bind ubiquitin and to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic end of the cell adhesion protein CD2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EAIVEFDYKAQHEDELTITVGDIITKIKKDDGGWWEGEIKGRRGLFPDNFVRE
>gnl|CDD|212986 cd12053, SH3_CD2AP_1, First Src Homology 3 domain (SH3A) of CD2-associated protein. CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the first SH3 domain (SH3A) of CD2AP. SH3A binds to the PXXXPR motif present in c-Cbl and the cytoplasmic domain of cell adhesion protein CD2. Its interaction with CD2 anchors CD2 at sites of cell contact. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EYIVEYDYDAVHEDELTIRVGEIIRNVKKLEEEGWLEGELNGRRGMFPDNFVKEIK
>gnl|CDD|212987 cd12054, SH3_CD2AP_2, Second Src Homology 3 domain (SH3B) of CD2-associated protein. CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the second SH3 domain (SH3B) of CD2AP. SH3B binds to c-Cbl in a site (TPSSRPLR is the core binding motif) distinct from the c-Cbl/SH3A binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RQCKVLFEYVPQNEDELELKVGDIIDINEEVEEGWWSGTLNGKSGLFPSNFVKEL
>gnl|CDD|212988 cd12055, SH3_CIN85_2, Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa. CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the second SH3 domain (SH3B) of CIN85. SH3B has been shown to bind Cbl proline-rich peptides and ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
RCQVAFSYLPQNEDELELKVGDIIEVVGEVEEGWWEGVLNGKTGMFPSNFIKE
>gnl|CDD|212989 cd12056, SH3_CD2AP_3, Third Src Homology 3 domain (SH3C) of CD2-associated protein. CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the third SH3 domain (SH3C) of CD2AP. SH3C has been shown to bind ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
KEYCKALFHYEGTNEDELDFKEGEIILIISKDTGEPGWWKGELNGKEGVFPDNFVSQ
>gnl|CDD|212990 cd12057, SH3_CIN85_3, Third Src Homology 3 domain (SH3C) of Cbl-interacting protein of 85 kDa. CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the third SH3 domain (SH3C) of CIN85. SH3C has been shown to bind ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YCKVLFPYEAQNEDELTIKEGDIVTLISKDCIDAGWWEGELNGRRGVFPDNFVKLL
>gnl|CDD|212991 cd12058, SH3_MLK4, Src Homology 3 domain of Mixed Lineage Kinase 4. MLK4 is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. MLK4 contains an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
LWTALYDYEASGEDELSLRRGDVVEVLSQDAAVSGDDGWWAGKIRHRLGIFPANYVTR
>gnl|CDD|212992 cd12059, SH3_MLK1-3, Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3. MLKs 1, 2, and 3 are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Little is known about the specific function of MLK1, also called MAP3K9. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. MLK2, also called MAP3K10, is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK3, also called MAP3K11, is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. It also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and thus, impacts inflammation and immunity. MLKs contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VWTAVFDYEASAEDELTLRRGDRVEVLSKDSAVSGDEGWWTGKINDRVGIFPSNYVTS
>gnl|CDD|212993 cd12060, SH3_alphaPIX, Src Homology 3 domain of alpha-Pak Interactive eXchange factor. Alpha-PIX, also called Rho guanine nucleotide exchange factor 6 (ARHGEF6) or Cool (Cloned out of Library)-2, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac 1, and is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QLVVKARFNFKQTNEDELSVCKGDIIYVTRVEEGGWWEGTLNGKTGWFPSNYVREIKS
>gnl|CDD|212994 cd12061, SH3_betaPIX, Src Homology 3 domain of beta-Pak Interactive eXchange factor. Beta-PIX, also called Rho guanine nucleotide exchange factor 7 (ARHGEF7) or Cool (Cloned out of Library)-1, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac 1, and plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VVRAKFNFQQTNEDELSFSKGDVIHVTRVEEGGWWEGTHNGRTGWFPSNYVREI
>gnl|CDD|212995 cd12062, SH3_Caskin1, Src Homology 3 domain of CASK interacting protein 1. Caskin1 is a multidomain adaptor protein that contains six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. It is expressed at high levels in the brain and is localized in presynaptic regions. It binds to the multidomain scaffolding protein CASK through the CaMK domain in competition with Munc-interacting protein 1 (Mint1). CASK participates in one of two evolutionarily conserved tripartite complexes containing either Mint1 and Velis or Caskin1 and Velis. Caskin1 may play a role in infantile myoclonic epilepsy. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
LQVRALKDYCNNYDLTSLNIKAGDVITVLEQHPDGRWKGCIHDNRTGNDRVGYFPSSLVEAI
>gnl|CDD|212996 cd12063, SH3_Caskin2, Src Homology 3 domain of CASK interacting protein 2. Caskin2 is a multidomain adaptor protein that contains six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. It shares a domain architecture with Caskin1, but does not bind CASK. The function of Caskin2 is still unknown. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHDSQRGTDRVGYFPPSIVEVI
>gnl|CDD|212997 cd12064, SH3_GRAF, Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase. GRAF, also called Rho GTPase activating protein 26 (ARHGAP26), Oligophrenin-1-like (OPHN1L) or GRAF1, is a GAP with activity towards RhoA and Cdc42 and is only weakly active towards Rac1. It influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase (FAK), which is a critical component of integrin signaling. It is essential for the major clathrin-independent endocytic pathway mediated by pleiomorphic membranes. GRAF contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. The SH3 domain of GRAF binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
RKAKALYACKAEHDSELSFTAGTVFDNVHPSQEPGWLEGTLNGKTGLIPENYVEFL
>gnl|CDD|212998 cd12065, SH3_GRAF2, Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase 2. GRAF2, also called Rho GTPase activating protein 10 (ARHGAP10) or PS-GAP, is a GAP with activity towards Cdc42 and RhoA. It regulates caspase-activated p21-activated protein kinase-2 (PAK-2p34). GRAF2 interacts with PAK-2p34, leading to its stabilization and decrease of cell death. It is highly expressed in skeletal muscle, and is involved in alpha-catenin recruitment at cell-cell junctions. GRAF2 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. The SH3 domain of GRAF binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
KAKAVYPCEAEHSSELSFEVGAIFEDVTLSREPGWLEGTLNGKRGLIPENYVEI
>gnl|CDD|212999 cd12066, SH3_GRAF3, Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase 3. GRAF3 is also called Rho GTPase activating protein 42 (ARHGAP42) or ARHGAP10-like. Though its function has not been characterized, it may be a GAP with activity towards RhoA and Cdc42, based on its similarity to GRAF and GRAF2. It contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. The SH3 domain of GRAF and GRAF2 binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
QAKAMYSCKAEHSHELSFPQGAIFSNVYPSVEPGWLKATYEGKTGLVPENYVVFL
>gnl|CDD|213000 cd12067, SH3_MYO15A, Src Homology 3 domain of Myosin XVa. Myosin XVa is an unconventional myosin that is critical for the normal growth of mechanosensory stereocilia of inner ear hair cells. Mutations in the myosin XVa gene are associated with nonsyndromic hearing loss. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
YVVAVRNYLPEDPALLSFHKGDIIHLQPLEGPKVGQYYGCVVRKKVMYLEELKRGTPDFGWKFGAIHGRS
GVFPAELVQP
>gnl|CDD|213001 cd12068, SH3_MYO15B, Src Homology 3 domain of Myosin XVb. Myosin XVb, also called KIAA1783, was named based on its similarity with myosin XVa. It is a transcribed and unprocessed pseudogene whose predicted amino acid sequence contains mutated or deleted amino acid residues that are normally conserved and important for myosin function. The related myosin XVa is important for normal growth of mechanosensory stereocilia of inner ear hair cells. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
YVVALRSYITDDKSLLSFHRGDLIKLLPMAGLEPGWQFGSTGGRSGLFPADIVQP
>gnl|CDD|213002 cd12069, SH3_ARHGAP27, Src Homology 3 domain of Rho GTPase-activating protein 27. Rho GTPase-activating proteins (RhoGAPs or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP27, also called CAMGAP1, shows GAP activity towards Rac1 and Cdc42. It binds the adaptor protein CIN85 and may play a role in clathrin-mediated endocytosis. It contains SH3, WW, Pleckstin homology (PH), and RhoGAP domains. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
LVLVEHAFEYTGKDGRLVSIKPNERYILLRRTNEHWWHVRRDKGTRPFYIPAKYVKE
>gnl|CDD|213003 cd12070, SH3_ARHGAP12, Src Homology 3 domain of Rho GTPase-activating protein 12. Rho GTPase-activating proteins (RhoGAPs or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP12 has been shown to display GAP activity towards Rac1. It plays a role in regulating hepatocyte growth factor (HGF)-driven cell growth and invasiveness. It contains SH3, WW, Pleckstin homology (PH), and RhoGAP domains. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
TYIEVEYDYDYEAKDRKIVIKQGERYILVKKTNDDWWQVKKDENSKPFYVPAQYVKEVTR
>gnl|CDD|213004 cd12071, SH3_FBP17, Src Homology 3 domain of Formin Binding Protein 17. Formin Binding Protein 17 (FBP17), also called FormiN Binding Protein 1 (FNBP1), is involved in dynamin-mediated endocytosis. It is recruited to clathrin-coated pits late in the endocytosis process and may play a role in the invagination and scission steps. FBP17 binds in vivo to tankyrase, a protein involved in telomere maintenance and mitogen activated protein kinase (MAPK) signaling. It contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain, a Cdc42-binding HR1 domain, and a C-terminal SH3 domain. The SH3 domain of the related protein, CIP4, associates with Gapex-5, a Rab31 GEF. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GTCKALYPFEGQNEGTISVAEGEMLYVIEEDKGDGWTRIRRNEDEEGYVPTSYIEVY
>gnl|CDD|213005 cd12072, SH3_FNBP1L, Src Homology 3 domain of Formin Binding Protein 1-Like. FormiN Binding Protein 1-Like (FNBP1L), also known as Toca-1 (Transducer of Cdc42-dependent actin assembly), forms a complex with neural Wiskott-Aldrich syndrome protein (N-WASP). The FNBP1L/N-WASP complex induces the formation of filopodia and endocytic vesicles. FNBP1L is required for Cdc42-induced actin assembly and is essential for autophagy of intracellular pathogens. It contains an N-terminal F-BAR domain, a central Cdc42-binding HR1 domain, and a C-terminal SH3 domain. The SH3 domain of the related protein, CIP4, associates with Gapex-5, a Rab31 GEF. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
GHCKALYPFDGSNEGTLAMKEGEVLYIIEEDKGDGWTRARKQNGEEGYVPTSYIEIT
>gnl|CDD|213006 cd12073, SH3_HS1, Src homology 3 domain of Hematopoietic lineage cell-specific protein 1. HS1, also called HCLS1 (hematopoietic cell-specific Lyn substrate 1), is a cortactin homolog expressed specifically in hematopoietic cells. It is an actin regulatory protein that binds the Arp2/3 complex and stabilizes branched actin filaments. It is required for cell spreading and signaling in lymphocytes. It regulates cytoskeletal remodeling that controls lymphocyte trafficking, and it also affects tissue invasion and infiltration of leukemic B cells. Like cortactin, HS1 contains an N-terminal acidic domain, several copies of a repeat domain found in cortactin and HS1, a proline-rich region, and a C-terminal SH3 domain. The N-terminal region binds the Arp2/3 complex and F-actin, while the C-terminal region acts as an adaptor or scaffold that can connect varied proteins that bind the SH3 domain within the actin network. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
ICAVALYDYQGEGDDEISFDPQETITDIEMVDEGWWKGTCHGHRGLFPANYVELL
>gnl|CDD|213007 cd12074, SH3_Tks5_1, First Src homology 3 domain of Tyrosine kinase substrate with five SH3 domains. Tks5, also called SH3 and PX domain-containing protein 2A (SH3PXD2A) or Five SH (FISH), is a scaffolding protein and Src substrate that is localized in podosomes, which are electron-dense structures found in Src-transformed fibroblasts, osteoclasts, macrophages, and some invasive cancer cells. It binds and regulates some members of the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. It is required for podosome formation, degradation of the extracellular matrix, and cancer cell invasion. Tks5 contains an N-terminal Phox homology (PX) domain and five SH3 domains. This model characterizes the first SH3 domain of Tks5. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
QYVVVSNYEKQENSEISLQAGEVVDVIEKNESGWWFVSTAEEQGWVPATYLES
>gnl|CDD|213008 cd12075, SH3_Tks4_1, First Src homology 3 domain of Tyrosine kinase substrate with four SH3 domains. Tks4, also called SH3 and PX domain-containing protein 2B (SH3PXD2B) or HOFI, is a Src substrate and scaffolding protein that plays an important role in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. It is required in the formation of functional podosomes, EGF-induced membrane ruffling, and lamellipodia generation. It plays an important role in cellular attachment and cell spreading. Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. It contains an N-terminal Phox homology (PX) domain and four SH3 domains. This model characterizes the first SH3 domain of Tks4. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
DQYVVVANYQKQESSEISLYVGQVVDIIEKNESGWWFVSTADEQGWVPATCLEAQ
>gnl|CDD|213009 cd12076, SH3_Tks4_2, Second Src homology 3 domain of Tyrosine kinase substrate with four SH3 domains. Tks4, also called SH3 and PX domain-containing protein 2B (SH3PXD2B) or HOFI, is a Src substrate and scaffolding protein that plays an important role in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. It is required in the formation of functional podosomes, EGF-induced membrane ruffling, and lamellipodia generation. It plays an important role in cellular attachment and cell spreading. Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. It contains an N-terminal Phox homology (PX) domain and four SH3 domains. This model characterizes the second SH3 domain of Tks4. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EKYTVIYPYTARDQDEINLEKGAVVEVIQKNLEGWWKIRYQGKEGWAPASYLKK
>gnl|CDD|213010 cd12077, SH3_Tks5_2, Second Src homology 3 domain of Tyrosine kinase substrate with five SH3 domains. Tks5, also called SH3 and PX domain-containing protein 2A (SH3PXD2A) or Five SH (FISH), is a scaffolding protein and Src substrate that is localized in podosomes, which are electron-dense structures found in Src-transformed fibroblasts, osteoclasts, macrophages, and some invasive cancer cells. It binds and regulates some members of the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. It is required for podosome formation, degradation of the extracellular matrix, and cancer cell invasion. Tks5 contains an N-terminal Phox homology (PX) domain and five SH3 domains. This model characterizes the second SH3 domain of Tks5. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EKYVTVQPYTSQGKDEIGFEKGVTVEVIQKNLEGWWYIRYLGKEGWAPASYLKK
>gnl|CDD|213011 cd12078, SH3_Tks4_3, Third Src homology 3 domain of Tyrosine kinase substrate with four SH3 domains. Tks4, also called SH3 and PX domain-containing protein 2B (SH3PXD2B) or HOFI, is a Src substrate and scaffolding protein that plays an important role in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. It is required in the formation of functional podosomes, EGF-induced membrane ruffling, and lamellipodia generation. It plays an important role in cellular attachment and cell spreading. Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. It contains an N-terminal Phox homology (PX) domain and four SH3 domains. This model characterizes the third SH3 domain of Tks4. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
EYYTIADFQTTIPDGISFQAGLKVEVIEKNLSGWWYIQIEDKEGWAPATFIDK
>gnl|CDD|213012 cd12079, SH3_Tks5_3, Third Src homology 3 domain of Tyrosine kinase substrate with five SH3 domains. Tks5, also called SH3 and PX domain-containing protein 2A (SH3PXD2A) or Five SH (FISH), is a scaffolding protein and Src substrate that is localized in podosomes, which are electron-dense structures found in Src-transformed fibroblasts, osteoclasts, macrophages, and some invasive cancer cells. It binds and regulates some members of the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. It is required for podosome formation, degradation of the extracellular matrix, and cancer cell invasion. Tks5 contains an N-terminal Phox homology (PX) domain and five SH3 domains. This model characterizes the third SH3 domain of Tks5. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VEYYTIAEFQSCISDGISFRGGQKAEVIEKNSGGWWYVQIGEKEGWAPSSYIDK
>gnl|CDD|213013 cd12080, SH3_MPP1, Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1). MPP1, also called 55 kDa erythrocyte membrane protein (p55), is a ubiquitously-expressed scaffolding protein that plays roles in regulating neutrophil polarity, cell shape, hair cell development, and neural development and patterning of the retina. It was originally identified as an erythrocyte protein that stabilizes the actin cytoskeleton to the plasma membrane by forming a complex with 4.1R protein and glycophorin C. MPP1 is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains the three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YMRAQFDYDPKKDNLIPCKEAGLKFQTGDIIQIINKDDSNWWQGRVEGSGEESAGLIPSPEL
>gnl|CDD|213014 cd12081, SH3_CASK, Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase. CASK is a scaffolding protein that is highly expressed in the mammalian nervous system and plays roles in synaptic protein targeting, neural development, and gene expression regulation. CASK interacts with many different binding partners including parkin, neurexin, syndecans, calcium channel proteins, caskin, among others, to perform specific functions in different subcellular locations. Disruption of the CASK gene in mice results in neonatal lethality while mutations in the human gene have been associated with X-linked mental retardation. Drosophila CASK is associated with both pre- and postsynaptic membranes and is crucial in synaptic transmission and vesicle cycling. CASK contains an N-terminal calmodulin-dependent kinase (CaMK)-like domain, two L27 domains, followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YVRAQFEYDPLKDDLIPCKQAGIRFRVGDILQIISKDDHNWWQAKLENSKNGTAGLIPSPEL
>gnl|CDD|240527 cd12082, MATE_like, Multidrug and toxic compound extrusion family and similar proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. MATE has also been identified as a large multigene family in plants, where the proteins are linked to disease resistance. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
AAPLLLSMLLQTLYNLVDTFFLGRLLGDALAAVGLAFPLIALLIALGVGLSVGTSALISQAIGAGDEEKA
RRVLVQSIVLAILLGLLLAALLLFFSPLILSLLGAEEEVIELAATYLTILILGLPITFLGAVLSGILQGE
GDTRTAMIISVLSNLLNILLDPLLIFGLGPPELGIAGAALATVISYVIGALLLLIYLRKGKKILKFKLSL
LKPDLELLRRLLRIGLPSAIQNSLLSLGLLIIVAIVAAFGGAAALAAYTVAFRIASLAFMPALGLAQAAL
PVVGQNLGAGNFDRARRITWVALLIGLLIGAVLGLLILLFPEPILSLFTNDPEFLELAVSYLRILAIYYL
FVGIGYVLQAGFQAAGRTLKSLIVSLLSYWVVRLPLAYVLAYLGLGLYGIWLALVISLILAALVLLLFFR
>gnl|CDD|213373 cd12083, DD_cGKI, Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I. Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing their targeting to different subcellular compartments and intracellular substrates
SGLLEEKTEELRKKDERIRELEQELQEKDEEIQELRSQLDKFQSVLPP
>gnl|CDD|438517 cd12084, DD_RII_PKA-like, dimerization/docking (D/D) domain of the type II Regulatory subunit of cAMP-dependent protein kinase and similar domains. cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence (IS), and two c-AMP binding domains. RI and RII subunits are distinguished by their IS; RII subunits contain a phosphorylation site and are both substrates and inhibitors while RI subunits are pseudo-substrates. RI subunits require ATP and Mg ions to form a stable holoenzyme while RII subunits do not. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis
VPEGLRELLEDFTREVLREQPEDVYEFAADYFEKLL
>gnl|CDD|213374 cd12085, DD_cGKI-alpha, Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I alpha. Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing for their targeting to different subcellular compartments and intracellular substrates. cGKI-alpha specifically binds to myosin light chain phosphatase targeting subunit (MYPT1) and the regulator of G-protein signaling-2 (RGS-2). cGKI-alpha activates the phosphatase activity of MYPT1, resulting in vasorelaxation. It increases the activity of RGS-2 toward G proteins, with implications in the downstream signaling for vasoconstrictive agents
SGSVEELQKLLQAKEERIRELEQLLQQRDEEIQELRSQLDKFQSVFPF
>gnl|CDD|213375 cd12086, DD_cGKI-beta, Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I beta. Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing for their targeting to different subcellular compartments and intracellular substrates. cGKI-beta binds specifically to inositol triphosphate receptor-associated PKG substrate (IRAG) and the transcriptional regulator TFII-I. Phosphorylation of IRAG by cGKI-beta contributes to smooth muscle relaxation while phosphorylation of TFII-I modulates its co-activator functions for serum response factor and Smad transcription factors
LRDLQRALQEKTEELRKRDELIKELEQELDEKDALIQHLQNELDKYRSVVRP
>gnl|CDD|213052 cd12087, TM_EGFR-like, Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. They are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of EGFR family RTKs have been associated with increased breast cancer risk
RTSKTTSIAAGVVGGLLVLVILGLIVFLFRRRRHIKRK
>gnl|CDD|277187 cd12088, helicase_insert_domain, helicase_insert_domain. helicase_insert_domain; This helical domain can be found inserted in a subset of SF2-type DEAD-box related helicases, like archaeal Hef helicase, MDA5-like helicases and FancM-like helicases. The exact function of this domain is unknown, but seems to play a role in interaction with nucleotides and/or the stabilization of the nucleotide complex
KMILSQLLRDTESLLKLLYTAHLRKLNDALELLEDAGIWDALKYIKMFFTEVREGIFDELERKLTLRFDE
KLQKLIALSRDP
>gnl|CDD|277188 cd12089, Hef_ID, insert domain of Archaeal Hef helicase/nuclease. Archaeal Hef helicase/nuclease, originally identified in the hyperthermophilic archaeon Pyrococcus furiosus, contains an N-terminal SF2 helicase domain and a C-terminal XPF/Mus81-type nuclease domain. Hef has been shown to process flap- or fork-DNA structures, and that both helicase and nuclease domain independently recognize branched DNA, with a strong preference for the forked DNA. The SF2 helicase domain is comprised of 3 structural domains, the 2 generally conserved helicase domains and a helical domain inserted between the two domains. This domain which is not present in all SF2 helicases, has been shown to play an important role in branched structure processing
KEIRKLLKEALDDRLKELKELGVIVSSENVSKKDLLELQKRIQAQIASSGDPSLYRAISILAEALKLDHA
IELLETQGVEALLKYLERLEEEAGSGSKAAKRLLEDPRFRKAVELLKEA
>gnl|CDD|277189 cd12090, MDA5_ID, Insert domain of MDA5. MDA5 (melanoma-differentiation-associated gene 5, also known as IFIH1), as well as RIG-I (Retinoic acid Inducible Gene I, also known as DDX58) and LPG2 (also known as DHX58), contain two N-terminal CARD domains and a C-terminal SF2 helicase domain. They are cytoplasmic DEAD box RNA helicases acting as key innate immune pattern-recognition receptor (PRRs) that play an important role in host antiviral response by sensing incoming viral RNA. Their SF2 helicase domain is comprised of 3 structural domains, the 2 generally conserved helicase domains and a helical domain inserted between the two domains. The inserted domain is involved in conformational changes upon ligand binding
DPFGDIIKKLMTDIEELLKMTPPDIQPREFGTQKYEQWVVTLEKKAAKLGNRALRTCAEHLRKYNDALLI
NDTARMKDALQYLKEFYTNLKEAKFDETERFLTDLFEENLEELKKLARDP
>gnl|CDD|277190 cd12091, FANCM_ID, Insert domain of FANCM and related proteins. FANCM and related proteins, like Mph1 and Fml1, are DNA junction-specific helicases/translocases that bind to and process perturbed replication forks and intermediates of homologous recombination. FANCM contains an N-terminal superfamily 2 helicase (SF2) domain, although FANCM, in contrast to other members of this family, does not exhibit DNA helicase activity. The SF2 helicase domain is comprised of 3 structural domains, the 2 generally conserved helicase domains and a helical domain inserted between the two domains. FANCM is a component of the Fanconi anaemia (FA) core complex. FA is a rare genetic disease in humans that is associated with progressive bone marrow failure, a variety of developmental abnormalities, and a high incidence of cancer. A key role of this complex is to monoubiquitination of FANCD2 and FANCI during S-phase and in response to DNA damage. The role of FANCM during this process seems to be the recruitment of the complex to chromatin
TEIRDLLAKVLEPFLKRLNQAGILPNRDPAKLSPFRLLQARDKFRANPPGNNEGQKGSIEGDFALLISLA
HAMELLLEHGIRPFYDYLKEIKDETKAKGSKSKKELAKNPNFKALM
>gnl|CDD|213053 cd12092, TM_ErbB4, Transmembrane domain of ErbB4, a Protein Tyrosine Kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. ErbB4 (HER4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. It is activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind ErbB4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1, ErbB1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with ErbB4. Upon ligand binding, ErbB4 forms homo- or heterodimers with other ErbB proteins. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of ErbB4 have been associated with increased breast cancer risk. ErbB4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, ErbB4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/ErbB4 signaling may contribute to schizophrenia
DCLGIHDRTPLIAAGVIGGLFIIVIIALTFAVYIRRKSIKKKRA
>gnl|CDD|213054 cd12093, TM_ErbB1, Transmembrane domain of Epidermal Growth Factor Receptor or ErbB1, a Protein Tyrosine Kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. It is activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for ErbB1 include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, ErbB1 can form homo- or heterodimers with other EGFR/ErbB subfamily members. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of ErbB1 have been associated with increased breast cancer risk. The ErbB1 signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. A number of monoclonal antibodies and small molecule inhibitors have been developed that target ErbB1, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder
EGCPDNGSKIPSIAAGVVGGLLCLVVVSLGIGLFVRRRHIVRKR
>gnl|CDD|213055 cd12094, TM_ErbB2, Transmembrane domain of ErbB2, a Protein Tyrosine Kinase. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. ErbB2 (HER2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. It is activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. ErbB2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the ErbB2-ErbB3 heterodimer being the most potent pair in mitogenic signaling. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of ErbB2 have been associated with increased breast cancer risk. ErbB2 plays an important role in cell development, proliferation, survival and motility. Overexpression of ErbB2 results in its activation and downstream signaling, even in the absence of ligand. ErbB2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. ErbB2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. ErbB2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer
GCPAEQRASPLTSIIAGVVGILLVVVLLVVFGILIKRRRQKIRK
>gnl|CDD|213056 cd12095, TM_ErbB3, Transmembrane domain of ErbB3, a Protein Tyrosine Kinase. ErbB3 (HER3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. ErbB receptors are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. ErbB3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. ErbB3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The ErbB2-ErbB3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of ErbB receptors have been associated with increased breast cancer risk. ErbB3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells
GRTPTVIAVAVIAGLFVLFSCFLLTLLYWRGLKIRRKRA
>gnl|CDD|438518 cd12097, DD_RI_PKA, dimerization/docking (D/D) domain of the Type I Regulatory subunit of cAMP-dependent protein kinase. cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. RI subunits are pseudo-substrates as they do not contain a phosphorylation site in their inhibitory site unlike RII subunits. RIalpha function is required for normal development as its deletion is embryonically lethal. RIbeta is expressed highly in the brain and is associated with hippocampal function. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis
LKECEAYIQKHNIQQLLKDCIVQLCVDRPDNPVAFLREYFEKLEKESTR
>gnl|CDD|438519 cd12098, DD_R_ScPKA-like, dimerization/docking (D/D) domain found in Saccharomyces cerevisiae cAMP-dependent protein kinase regulatory subunit and similar domains. cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. The R subunit of fungal PKA is encoded by a single gene, which is called by various names in different organisms (for example: Yarrowia lipolytica RKA1, Saccharomyces cerevisiae Bcy1, and Schizosaccharomyces pombe Cgs1). Although most characterized PKA holoenzymes are tetramers, Y. lipolytica PKA has been reported to be a dimer of RKA1 and the catalytic subunit TPK1. RKA1 is essential and promotes hyphal growth. Cgs1 is essential for sexual differentiation of S. pombe; mutants with defective Cgs1 are partially sterile. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. The D/D domain of metazoan R subunits dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs). The D/D domain of fungal R subunits may also serve as a dimerization domain, in the case of heterotetrameric PKAs. Fungal PKA plays a major role in controlling cell growth and metabolism in response to nutrients and stress conditions
LPSEYPDELNELNREVLRAQPDDILQFCANYFNRKLEEQRAFLRS
>gnl|CDD|438520 cd12099, DD_RII_PKA, dimerization/docking (D/D) domain of the Type II Regulatory subunit of cAMP-dependent protein kinase. cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. RII subunits contain a phosphorylation site in their inhibitory site and are both substrates and inhibitors. RIIalpha plays a role in the association and dissociation of PKA with the centrosome during interphase and mitosis, respectively. RIIbeta plays an important role in adipocytes and neuronal tissues. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis
VPPGLTELLQDFTVAVLREQPTDLVDFAAEYFTRLRE
>gnl|CDD|438521 cd12100, DD_CABYR_SP17, dimerization/docking (D/D) domain of the sperm fibrous sheath proteins, Calcium-Binding tYrosine-phosphorylation Regulated protein and Sperm Protein 17. CABYR and SP17 are naturally located in the human sperm fibrous sheath (FS). CABYR was originally isolated from spermatoza and was thought to be testis-specific, but has recently been observed in lung and brain tumors. It is a polymorphic calcium binding protein that is phosphorylated during capacitation. SP17 plays an important role in the interaction of sperm with the zona pellucida during fertilization. It also promotes cell-cell adhesion. SP17 is found in various human tumors of unrelated histological origin including metastatic squamous cell carcinoma, multiple myeloma, ovarian cancer, and primary nervous system tumors, among others. Both CABYR and SP17 contain an N-terminal dimerization/docking (D/D) domain with similarity to the D/D domain of the R subunit of cAMP-dependent protein kinase (PKA). The D/D domain of the R subunit dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. The D/D domain of CABYR and SP17 have been shown to bind to AKAP3, a protein that is also associated to the FS of mammalian spermatozoa
RLRLPYGLKSLLEGLSREVLREQPEDIPEFAADYFEELLKFR
>gnl|CDD|438522 cd12101, DD_RIalpha_PKA, dimerization/docking (D/D) domain of the Type I alpha Regulatory subunit of cAMP-dependent protein kinase. cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. RI subunits are pseudo-substrates as they do not contain a phosphorylation site in their inhibitory site unlike RII subunits. RIalpha is the key regulatory subunit responsible for maintaining cAMP control of the catalytic subunit. RIalpha function is required for normal development as its deletion is embryonically lethal due to failed cardiac morphogenesis. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis
SLRECELYVQKHNIQQLLKDCIVQLCTARPERPMAFLREYFERLEKEEAK
>gnl|CDD|438523 cd12102, DD_RIbeta_PKA, dimerization/docking (D/D) domain of the Type I beta Regulatory subunit of cAMP-dependent protein kinase. cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. RI subunits are pseudo-substrates as they do not contain a phosphorylation site in their inhibitory site unlike RII subunits. RIbeta is expressed highly in the brain and is associated with hippocampal function. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis
EDESLKGCELYVQKHNIQQILKECIVNLCIAKPDRPMKFLREHFEKLEKEECKQ
>gnl|CDD|438524 cd12103, DD_RIIalpha_PKA, dimerization/docking (D/D) domain of the Type II alpha Regulatory subunit of cAMP-dependent protein kinase. cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. RII subunits contain a phosphorylation site in their inhibitory site and are both substrates and inhibitors. RIIalpha plays a role in the association and dissociation of PKA with the centrosome during interphase and mitosis, respectively. It is also involved in endosome-to-Golgi and Golgi-to-ER transport. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis
IQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREAR
>gnl|CDD|438525 cd12104, DD_RIIbeta_PKA, dimerization/docking (D/D) domain of the Type II beta Regulatory subunit of cAMP-dependent protein kinase. cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. RII subunits contain a phosphorylation site in their inhibitory site and are both substrates and inhibitors. RIIbeta plays an important role in adipocytes and neuronal tissues. Mice deficient with RIIbeta have small fat cells, and are resistant to obesity, diet-induced diabetes, and alcohol-induced motor defects. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis
IEIPEGLTELLQGFTVEVLRNQPGDLLEFALQYFTRLKQAQSK
>gnl|CDD|213031 cd12105, HmuY, Bacterial proteins similar to Porphyromonas gingivalis HmuY. HmuY is a hemophore that scavenges heme from infected hosts and delivers it to the outer membrane receptor HmuR. Related but uncharacterized proteins do not appear to share the specific heme-binding site
KTTTISKTSSTNWVYFSLDTGKVVNVEPEEPTDWDIAFHRYDIRTNGGVSGTGKGGAADLKATDLDSAAV
APADAEFVVDTSSDKVYVVKTADGNYAKLQFTSYYNDAGESGYPTFRYKLL
>gnl|CDD|213061 cd12106, PARMER_03128_N, N-terminal domain of PARMER_03128. PARMER_03128 is an uncharacterized protein from Parabacteroides merdae. This model characterizes its N-terminal domain plus that of related proteins from Bacteroidetes. Structurally, they resemble domains found in streptococcal surface proteins such as SpaP
DPESALKNDLIKKTLGPAIVGDRIEFAYAMGTLEGKLKSAQAEASIAGAAGTGFERNSWYTNRSSGVDVP
VQTGSDAVTNGAVSTATFMDKADTKAATLRYYYVIPEEARGKTVSFTFSAKSSTGQTVSYKMPPYKI
>gnl|CDD|213982 cd12107, Hemerythrin, Hemerythrin. Hemerythrin (Hr) is a non-heme diiron oxygen transport protein found in four marine invertebrate phyla including priapulida, brachiopoda, sipunculida, and annelida, as well as in protozoa. Myohemerythrin (Mhr), a hemerythrin homolog, is found in the muscle tissue of sipunculids as well as in polycheate and oligocheate annelids. In addition to oxygen transport, Mhr proteins are involved in cadmium fixation and host anti-bacterial defense. Hr and Mhr proteins have the same "four alpha helix bundle" motif and active site structure. Hr forms oligomers, the octameric form being most prevalent, while Mhr is monomeric
PEIDEQHKELFELINRLYEAIAAGDGKEELAELLDELIDYTREHFATEEALMEEIGYPDLEEHKAEHRRF
LEKLEELKARLEAGDLELAEELLDFLKDWLVNHILGEDKKLAR
>gnl|CDD|213983 cd12108, Hr-like, Hemerythrin-like domain. Hemerythrin (Hr) like domains have the same four alpha helix bundle and a similar, but slightly different active site structure than hemerythrin. They are non-heme diiron binding proteins mainly found in bacteria and eukaryotes. Like Hr, they may be involved in oxygen transport or like human FBXL5 (F-box and leucine-rich repeat protein 5), a member of this group, play a role in cellular iron homeostasis
DLLKLEHRAIRRELGRLARLAGALAAGGPDDARALAERFRFLATELHHHHTAEEELLFPALRERVPLAAV
LDALEAEHAEIDELLARLEALLPALLAGDAEDAEELAAALEALRTALREHLDEEEEELFP
>gnl|CDD|213984 cd12109, Hr_FBXL5, Hemerythrin-like domain of FBXL5-like proteins. Human FBXL5 (F-box and leucine-rich repeat protein 5) protein plays a role in cellular iron homeostasis. It is part of an E3 ubiquitin ligase complex that targets the iron regulatory protein IRP2 for proteasomal degradation. The FBXL5's stability is regulated by iron concentration, with its iron- and oxygen-binding hemerythrin domain acting as a ligand-dependent regulatory switch
RVDVYGFIHKALRALLFDLLQKLGRTDFSDPQDLAALLESLRRLLQEFKAHEQHENEFIHPLLEKRLPGL
SAAVANEHSDHDLSIMLLLELLGALRTAPEAERPAAGRQLYRALAAFVADNLPHMHEEETVFQPLLWEYF
SDEELKAIKKAVIASHPP
>gnl|CDD|213994 cd12110, PHP_HisPPase_Hisj_like, Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like. Bacillus subtilis YtvP HisJ has strong histidinol phosphate phosphatase (HisPPase) activity. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce histidinol. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel
VDYHTHTPRCDHASGTLEEYVEAAIELGFTEIGFSEHAPLPFEFDDYPESRMAEEELEDYVEEIRRLKEK
YADQIEIKLGLEVDYFPGYEEELRELLYGYPLDYVIGSVHFLGGWGFDFPEDGIAEYFEGDIDELYERYF
DLVEKAIESGLFDIIGHPDLIKKFGKNDEPDEDYEELIERILRAIAEAGVALEINTAGLRKPVGEPYPSP
EFLELAKELGIPVTLGSDAHSPEDVGQGYDEALA
>gnl|CDD|213995 cd12111, PHP_HisPPase_Thermotoga_like, Polymerase and Histidinol Phosphatase domain of Thermotoga like. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. Thermotoga PHP is an uncharacterized protein. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to give histidinol. The HisPPase can be classified into two types: the bifunctional HisPPase found in proteobacteria that belongs to the DDDD superfamily and the monofunctional Bacillus subtilis type that is a member of the PHP family. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel
WLLCDFHIHTTYSDGALSLSEVVDLYGQHGFDVIAITDHVVDRASLIGKFPQGTHPGVTEANFEDYMEAL
KVEAKRAWEKYEMIVIPGVELTNNTDSYHILGIDVKEYIDPCLSVEEIIAEIHKQGGIAVAAHPHRKNLD
GEHNSLYLWNNRERYKHLFDAWEIANRDDLFNVVGLKKLPYIANSDFHKPKHLYSWKTLLKCEKNIEAIK
EAIRKNESVAITLFRG
>gnl|CDD|213996 cd12112, PHP_HisPPase_Chlorobi_like, Polymerase and Histidinol Phosphatase domain of Chlorobi like. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. Chlorobi PHP is uncharacterized protein. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce histidinol. The HisPPase can be classified into two types: the bifunctional Hisppase found in proteobacteria that belongs to the DDDD superfamily and the monofunctional Bacillus subtilis type that is a member of the PHP family. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel
EIQVPDIPGYKTLKCDFHTHTVFSDGHVWPEIRVREAWREGLDAIAITEHIEYRPHKEDIPHPDRNRSYK
IAKEAAESKGLLIIPGAEITREKPPGHLNALFLTDANALLVPDPLDAIRAAKKQGAFVFWNHPGWPDQSP
DGIALPPFHEKLIEEGLIHGIEVMNGTEYYPEAIQWALEYNLTVMGTSDIHGLIDWTYDLKGGHRPRTLV
FAFERSLEALKEALFAGRTTAVYFD
>gnl|CDD|213997 cd12113, PHP_PolIIIA_DnaE3, Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III DnaE3. PolIIIAs that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that is responsible for the replication of the DNA duplex. The alpha subunit of DNA polymerase III core enzyme catalyzes the reaction for polymerizing both DNA strands. The PolIIIA PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination, and like other PHP structures, the PolIIIA PHP exhibits a distorted (beta/alpha) 7 barrel and coordinates up to 3 metals. Initially, it was proposed that PHP region might be involved in pyrophosphate hydrolysis, but such an activity has not been found. It has been shown that the PHP of PolIIIA has a trinuclear metal complex and is capable of proofreading activity. Bacterial genome replication and DNA repair mechanisms is related to the GC content of its genomes. There is a correlation between GC content variations and the dimeric combinations of PolIIIA subunits. Eubacteria can be grouped into different GC variable groups: the full-spectrum or dnaE1 group, the high-GC or dnaE2-dnaE1 group, and the low GC or polC-dnaE3 group
DFVHLHVHTEYSLLDGAIRIKDLVKRAKELGMPALAITDHGNMFGAIEFYKAAKKAGIKPIIGCEVYVAP
GSRFDKKDKKGDKRYYHLVLLAKNEEGYRNLMKLVSLAYLEGFYYKPRIDKELLAKYSEGLIALSACLAG
EIPQLLLNGDEEEAREAALEYRDIFGKDNFYLELQDHGLPEQKKVNEGLIELAKELGIPLVATNDVHYLN
KEDAEAHDVLLCIQTGKTLDDPNRMRFDTDEFYLKSPEEMRELFPDVPEALENTLEIAERCNVELDFGKL
HLP
>gnl|CDD|341279 cd12114, A_NRPS_TlmIV_like, The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety
PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDID
QPAARREAILADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGT
PKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWA
ELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATE
ASIWSIYHPIDEVPPDWRSIPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAAR
FVTHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGG
KRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL
>gnl|CDD|341280 cd12115, A_NRPS_Sfm_like, The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS
LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVL
KAGAAYVPLDPAYPPERLRFILEDAQARLVLTDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAA
FSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPAAAEVTLINTVPSAAAELLRHDA
LPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQAY
VLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGR
ADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLP
AYMVPSRFVRLDALPLTPNGKIDRSAL
>gnl|CDD|341281 cd12116, A_NRPS_Ta1_like, The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity
PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPD
YPADRLRYILEDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGR
PKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALA
RLIEAHSITVMQATPATWRMLLDAGWQGRAGLTALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIWST
AARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGP
GSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAY
VVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL
>gnl|CDD|341282 cd12117, A_NRPS_Srf_like, The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C). The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain
ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKA
GAAYVPLDPELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAY
VMYTSGSTGRPKGVAVTHRGVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKG
TLLDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVN
GYGPTENTTFTTSHVVTELDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRP
ALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVV
VVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL
>gnl|CDD|341283 cd12118, ttLC_FACS_AEE21_like, Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis. This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized
YVPLTPLSFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYEL
HFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREFEYEDLLAEGDPDFEWIPPADEWDPIALNY
TSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLRKVDA
KAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHVYGL
TETYGPATVCAWKPEWDELPTEERARLKARQGVRYVGLEEVDVLDPETMKPVPRDGKTIGEIVFRGNIVM
KGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAV
VARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGELPKTSTGKIQKFVLRD
>gnl|CDD|341284 cd12119, ttLC_FACS_AlkK_like, Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles. This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins
LLEHAARLHGDREIVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAV
PGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVG
VLAYEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSESDVVL
PVVPMFHVNAWGLPYAAAMVGAKLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLS
SLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVARPPSEHSNLSEDEQLALRAKQGRPVPG
VELRIVDDDGRELPWDGKAVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRS
KDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAK
WWLPDDVVFVDEIPKTSTGKIDKKALRE
>gnl|CDD|213376 cd12120, AMPKA_C_like, C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha subunit and similar domains. This family is composed of AMPKs, microtubule-associated protein/microtubule affinity regulating kinases (MARKs), yeast Kcc4p-like proteins, plant calcineurin B-Like (CBL)-interacting protein kinases (CIPKs), and similar proteins. They are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. AMPKs act as sensors for the energy status of the cell and are activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. MARKs phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Kcc4p and related proteins are septin-associated proteins that are involved in septin organization and in the yeast morphogenesis checkpoint coordinating the cell cycle with bud formation. CIPKs interact with the calcineurin B-like (CBL) calcium sensors to form a signaling network that decode specific calcium signals triggered by a variety of environmental stimuli including salinity, drought, cold, light, and mechanical perturbation, among others. All members of this family contain an N-terminal catalytic kinase domain and a C-terminal regulatory domain which is also called kinase associated domain 1 (KA1) in some cases. The C-terminal regulatory domain serves as a protein interaction domain in AMPKs and CIPKs. In MARKs and Kcc4p-like proteins, this domain binds phospholipids and may be involved in membrane localization
RKKWELEIHSRIDPSEIYEGIHKVLEGWGKNLVFRITNFIITGKLVNDHILFLRSTLFEIEVYEVGPGLF
MVDFKKKTGSTKTFTKLATKIQIKL
>gnl|CDD|213377 cd12121, MARK_C_like, C-terminal kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinases, and similar domains. Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. In yeast, MARK/Par-1 homologs are called Kin1/2 kinases. Kin1 is a membrane-associated kinase that is involved in regulating cytokinesis and the cell surface. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain
RSLRGPFSVATTSTKSPEEIMNEIKRVLRSNGIDYEEVGGYLLECKHGDSSGGEFVIFEIEICKLPRLGL
NGIRFKRISGDSWQYKRLCKKILNEL
>gnl|CDD|213378 cd12122, AMPKA_C, C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha catalytic subunit. AMPK, a serine/threonine protein kinase (STK), catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It acts as a sensor for the energy status of the cell and is activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. AMPK is a heterotrimer of three subunits: alpha, beta, and gamma. Co-expression of the three subunits is required for kinase activity; in the absence of one, the other two subunits get degraded. The AMPK alpha subunit is the catalytic subunit and it contains an N-terminal kinase domain and a C-terminal regulatory domain (RD). Vertebrates contain two isoforms of the alpha subunit, alpha1 and alpha2, which are encoded by different genes, PRKAA1 and PRKAA2, respectively. The C-terminal RD of the AMPK alpha subunit is involved in AMPK heterotrimer formation. It mainly interacts with the C-terminal region of the beta subunit to form a tight alpha-beta complex that is associated with the gamma subunit. The AMPK alpha subunit RD also contains an auto-inhibitory region that interacts with the kinase domain; this inhibition is negated by the interaction with the AMPK gamma subunit. AMPK is conserved throughout evolution; the AMPK alpha subunit homologs in yeast and plants are called Snf1 and SnRK1 (Snf1 related kinase), respectively
ERRWHLGIRSQSHPHEIMLEVYRALKALGFEWKKISPYHIKCRWKNPVVGKPGGSSGESSSADGPGAARQ
PTVVKMELQLYKVDDNKYLLDFQSLDYEEERTGPGESAEDAEPQVGSTFLFFDLCAKLITEL
>gnl|CDD|381264 cd12124, Pgbs, Protoglobins (Pgbs). Pgbs are single-domain globins of yet unknown biological function. Included in this subfamily are Pgbs from the strictly anaerobic methanogen Methanosarcina acetivorans (MaPgb) and from the obligate aerobic hyperthermophile Aeropyrum pernix (ApPgb). MaPgb is a dimeric globin which in addition to the 3-on-3 helical sandwich contains an N-terminal extension. This extension, along with other Pgb-specific loops buries the heme within the protein; two orthogonal apolar tunnels grant access of small ligand molecules to the heme. Like other globins, MaPgb can bind O2, CO and NO reversibly in vitro, however it has as unusually low O2 dissociation rate, along with a large structural distortion of the heme moiety. CO binding to and dissociation from the heme occurs through biphasic kinetics. ApPgb also contains heme, and can bind O2, CO and NO. This subfamily belongs to a family which includes the globin-coupled-sensors (GCSs) and single-domain sensor globins. It has been demonstrated that Pgbs and other single-domain globins can function as sensors, when coupled to an appropriate regulator domain
IPGYTYGTESVPTSPVSLEDLELLKATVLFTEEDEEYLRMAGEVLAPQVEEILDVWYGFVGSHPHLLYYF
SGPDGQPNEEYLAAVRKRFGQWILDTCNRPYDQAWLDYQYEIGLRHHRAKKNQTDGVDSVPFIPLRYLIA
FIYPITATIRPFLAKKGHSPEEVEKMHQAWFKAVTLQVTLWSYPY
>gnl|CDD|381265 cd12125, APC_alpha, Allophycocyanin alpha subunit of the phycobilisome core. Phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC)
SIVSQIILNADDELRYPSPGELEAIQDFFNTGEQRIRIAKTLAENEKKIVEQASKQLWQRCPDTPSPGGN
AYGEKKTALCLRDQGWYLRLITYGILAGDVEPLEEIGLIGVREMYNSLGVPLPNMVEAMRCLKEAALALL
SPEDAAEAAPYFDYIIQAM
>gnl|CDD|271281 cd12126, APC_beta, Allophycocyanin beta subunit of the phycobilisome core. Phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC)
MQDAITSVINRYDVTGKYLDRNAIDKLKAYFDTGELRVQAAKVINANAAEIIKEASAKLFEEYPELLRPG
GNAYTTRRYAACLRDMDYYLRYATYAILAGDTSILDERVLNGLKDTYNSLGVPIGPTVRAIQLMKEVVKE
LVGTAIDAGKFVDEPFDYMIRGL
>gnl|CDD|381266 cd12127, PE-PC-PEC_beta, Beta subunits of phycocyanin, phycoerythrin and phycoerythrocyanin; phycobilisome rod components. phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). This family also includes the beta subunits of Cryptophyte phycobiliproteins which represent another type of biliprotein antenna with different structure and organization. The beta subunits of cryptophyte PBPs share a high degree of sequence identity with both the alpha and beta subunits of the cyanobacterial and red algal PBPs, however the alpha cryptophyte subunits are shorter, and unrelated. There is only one type of PBP present in a single species, either phycocyanin or phycoerythrin, but not allophycocyanin. Structurally, phycoerythrin in cryptophytes is an alpha1alpha2betabeta dimer and not a trimer as in the PBS
MLDAFSRVVVQADAKGEYLSNAQLDALKKFIAEGNKRLDAVNRITSNASCIVADAVRAMICENPQLINPG
GXCYTNRRMAACLRDGEIILRYVSYALLAGDSSVLDDRCLNGLKETYQALGVPGSSVARAIEKMKEAAVA
IANDTNGGRSGTKGDCSDLASEAASYFDRAIAAV
>gnl|CDD|381267 cd12128, PBP_PBS-LCM, Phycobiliprotein-like domain of the phycobilisome core-membrane linker polypeptide. phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae, they consist of a central core and radiating rods and function to harvest and channel light energy toward the photosynthetic reaction centers (RCs) within the membrane. They are comprised of phycobiliproteins or chromophorylated proteins (PBPs) maintained together by linker polypeptides. LCM is a chromophore-bearing PBS linker protein; it facilitates PBS assembly and functionally connects the PBS to the chlorophyll-containing core-complexes in the photosynthetic membrane. In addition to being a linker polypeptide that stabilizes the PBS architecture, the LCM also serves as a terminal energy acceptor. The single phycocyanobilin (PCB) chromophore of LCM are one of two terminal energy transmitters that transfer excitations from the hundreds of chromophores of the PBS to the RCs within the membrane
LNAETIVSRAANRIFVGGSPMAYLEKPEELPEDPGAAVTMAEDRDKQAESSTNIFVEVRGNGLSFAGFSS
GPIPPGFRPINVARYGPSNMKKSLRDLDWFLRYVTYAIVAGDPSILVVNTRGLREIIENACSTAATIVAL
QEMRAASLSLFRNDPEAQEIVRQYFDVLISEF
>gnl|CDD|271284 cd12129, PE-PC-PEC_alpha, Alpha subunits of phycoerythrin, phycocyanin and phycoerythrocyanin; phycobilisome rod components. phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC)
KTPITEAIAAADAAGRFLSNTELQAVQGRFQRAAARLEAARALANNHEAVVKEAADAVYQKFPYTTNMQG
PQYASTPEGKAKCYRDIDHYLRLINYCLVVGGTGPLDEYGIAGLREVNSALNLSPSWYIAALEFTRDNHG
LTGQAAVEANTYIDYAINALS
>gnl|CDD|381268 cd12130, Apl, Allophycocyanin-like globins. phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). This subfamily contains allophycocyanin-like proteins (Apls), which have conserved the residues critical for chromophore interactions, but may not maintain the proper alpha-beta subunit interactions and tertiary structure of phycobiliproteins. Indeed AplA isolated from Fremyella diplosiphon was not detected in phycobilisomes. As the genes encoding Apls cluster with light-responsive regulatory components, Apls may have photoresponsive regulatory role(s)
LRALLQAADDERRYLTDEELQAICQLSGVDAAPARQLRDQAHELVDQARATLLAQFPGITEPGGALYPPE
RAEACWRDCWHFLRCITYGIAGGQTDFTSPEGLGAMRLLYQELQVPLPAMLLALEGLKTLSLKRFSGEEA
ALLAPYFDHLIEQL
>gnl|CDD|381269 cd12131, HGbI-like, Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins. HGbI is a single-domain heme-containing protein isolated from Methylacidiphilum infernorum, an aerobic acidophilic and thermophilic methanotroph. M. infernorum grows optimally at pH 2.0 and 60C and its home is New Zealand's Hell's Gate geothermal park. The physiological role of HGbI has yet to be determined. It has an extremely strong resistance to auto-oxidation, and has fast oxygen-binding/slow release characteristics. Its CO on-rate is comparable to the O2 on-rate, and it is able to bind acetate with high affinity in the ferric state. The coordination of the heme iron changes in the ferrous form from pentacoordinate at low pH to predominantly hexacoordinate at high pH; in the ferric form, it is predominantly hexacoordinate at all pH
QIELVQQSFAKVEPIADEAAALFYERLFELDPELKPLFKGTDMEEQGRKLMAMLVLVVKGLDDLEALLPA
LQDLGRRHVKYGVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGILAGTMIE
>gnl|CDD|271287 cd12137, GbX, Globin_X (GbX). Zebrafish globin X (GbX) is expressed at low levels in neurons of the central nervous system, and appears to be associated with the sensory system. GbX is likely to be attached to the cell membrane via S-palmitoylation and N-myristoylation. It's unlikely to have a true respiratory function as it is membrane-associated. It has been suggested that it may protect the lipids in the cell membrane from oxidation or act as a redox-sensing or signaling protein. Zebrafish GbX is hexacoordinate, and displays cooperative O2 binding
LTERQKQLIESSWSILQEDIAKVGVIMFVRLFETHPDCKDAFFPFRDVDLEDLRHSKELRAHGLRVLSFV
EKSLARLHQPDKLEELLHELGRKHYRYNAKVKYVDLVGQQFIFAIEPVLKEQWTPELEEAWKTLFRYLTY
VMKEG
>gnl|CDD|213015 cd12139, SH3_Bin1, Src Homology 3 domain of Bridging integrator 1 (Bin1), also called Amphiphysin-2. Bin1 isoforms are localized in many different tissues and may function in intracellular vesicle trafficking. It plays a role in the organization and maintenance of the T-tubule network in skeletal muscle. Mutations in Bin1 are associated with autosomal recessive centronuclear myopathy. Bin1 contains an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR) and a C-terminal SH3 domain. The SH3 domain of Bin1 forms transient complexes with actin, myosin filaments, and CDK5, to facilitate sarcomere organization and myofiber maturation. It also binds dynamin and prevents its self-assembly. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FLFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKKLEKCRGVFPENFTE
RV
>gnl|CDD|213016 cd12140, SH3_Amphiphysin_I, Src Homology 3 domain of Amphiphysin I. Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin, and synaptojanin. They function in synaptic vesicle endocytosis. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
FLYKVETLHDFEAANSDELELKRGDIVLVVPSETAADQDAGWLTGVKESDWLQYRDASAYKGLFPENFTR
RL
>gnl|CDD|213017 cd12141, SH3_DNMBP_C2, Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and similar domains. DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. The C-terminal SH3 domains of DNMBP bind to N-WASP and Ena/VASP proteins, which are key regulatory proteins of the actin cytoskeleton. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
VYYAVYTFKARSPNELSVSANQRVRILEFSDLTGNKEWWLAEANGQKGYVPSNYIRK
>gnl|CDD|213018 cd12142, SH3_D21-like, Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins. N-terminal SH3 domain of the uncharacterized protein SH3 domain-containing protein 21, and similar uncharacterized domains, it belongs to the CD2AP-like_3 subfamily of proteins. The CD2AP-like_3 subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies
YCRVLFDYNPVAPDELALKKGDVIEVISKETEDEGWWEGELNGRRGFFPDNFVMP
>gnl|CDD|213019 cd12143, SH3_ARHGAP9, Src Homology 3 domain of Rho GTPase-activating protein 9 and similar proteins. Rho GTPase-activating proteins (RhoGAPs or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP9 functions as a GAP for Rac and Cdc42, but not for RhoA. It negatively regulates cell migration and adhesion. It also acts as a docking protein for the MAP kinases Erk2 and p38alpha, and may facilitate cross-talk between the Rho GTPase and MAPK pathways to control actin remodeling. It contains SH3, WW, Pleckstin homology (PH), and RhoGAP domains. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies
QLCALYAYQYTGADGRQVSIAEGERFLLLRKTNSDWWQVRRLEAPSTSRPLFVPATY
>gnl|CDD|213387 cd12144, SDH_N_domain, Saccharopine dehydrogenase N-terminal domain. SDH N-terminal domain is named due to its appearance at the N-terminal of SDH in eukaryotes, but can be found C-terminal of the SDH-like domain in other enzymes, such as the bifunctional lysine ketoglutarate reductase/saccharopine dehydrogenase enzyme. SDH catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SHD is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of a related structure
REVELEGHLIDSGLLNKVLDLIEDAGGDFEILECDVGKSKDDPSYARLEVSADDEEHLDRILDELTSLGA
VLVDSADAELEPAPKDGVLPDGFYSTTNHPTQVRLDGEWIVVEN
>gnl|CDD|213388 cd12145, Rev1_C, C-terminal domain of the Y-family polymerase Rev1. Rev1 is a eukaryotic translesion synthesis (TLS) polymerase; TLS is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Rev1 has both structural and enzymatic roles. Structurally, it is believed to interact with other nonclassical polymerases and replication machinery to act as a scaffold. The C-terminal domain modeled here is essential for TLS and has been shown to mediate interactions with the Rev7 subunit of the B-family TLS polymerase Pol zeta (Rev3/Rev7), as well as with the RIRs (Rev1-interacting regions) of polymerases kappa, iota, and eta. Rev1 is known to actively promote the introduction of mutations, potentially making it a significant target for cancer treatment
PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWE
EAYDRIIDVVQNRVKQTYGSPLKI
>gnl|CDD|213389 cd12146, STING_C, C-terminal domain of STING. STING (stimulator of interferon genes, also known as MITA, ERIS, MPYS and TMEM173) is a master regulator that mediates cytokine production in response to microbial invasion by directly sensing bacterial secondary messengers such as the cyclic dinucleotide bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) and leading to the activation of IFN regulatory factor 3 (IRF3) through TANK-binding kinase 1 (TBK1) stimulation. STING is also a signaling adaptor in the IFN response to cytosolic DNA. This detection of foreign materials is the first step to a successful immune responses. STING is localized in the ER and comprised of an predicted N-terminal transmembrane region and a C-terminal c-di-GMP binding domain
VAHGLAWSYYIGYLKLILPELEERIRQYEDKNNVTLEVKKLFILIPLSCYVPPSLKDADENIEFAENLEE
LIIDRAGVKDRVYKNSVYKIRPNGDKRPYYCAMEYATPLNTLFDMSQDSEAAFSREERLEQAKLFYRTLR
DILEDSPECQGLYELIYYEDFDEDDSVDLSQVILQHLRQQE
>gnl|CDD|213390 cd12147, Cep3_C, C-terminal domain of the Cep3, a subunit of the yeast centromere-binding factor 3. Cep3, together with Skp1, Ctf13, and Ndc10, forms the yeast centromere-binding factor 3 (CBF3) which initiates kinetochore assembly by binding to the CDEIII locus of centromeric DNA. Cep3 is comprised of two domains, the N-terminal DNA-binding module, a Zn2Cys6-cluster, C-terminal domain, which dimerizes and is believed to be involved in the recruitment of the Skp1-Ctf1 heterodimer
KEYLPDLLLFWQSYEYWVMDIGLFKTQNLDTTRKDVDLDEDLKECEFWMNLLNKEQSFKLLDYSMENLGP
LYFGCLSDISELYLQLERYWDRREDKNETTVKSSVDEYYWDALLWSIFTMAVYYMPVEKLAKIFDIDPVH
EYLPSSKEGEWEEQLQLNLFEGFLRTTLTQLKKADFMANPDIRLIQIYLILSNTSFPQSEPSLADSLLTQ
CIHVAKLFHIDDFKPLINDSPALRLTKLTCEKIWYRLCTCDYLQSGPNKPISFHTEISSLLQHAAYLEDL
PNTDVYQSEDNFEVLYWKIISLDRDLDQYLNKSSKPPLKTLDAIQRELDIFQRKVSSLEEQASFNSKFEK
FLLLFLLNSVSWKLHKMYFIYYDTSDSLSKSIHYTKVIIALLVKNFKEKLEFFNKHPIVLRILSRIASFY
SFYNIFDESAEVEQLVLDLNELLANLPDIFGPKLNNLLYLLDRLTKLKLIWEKVQVVDSGNSFQHPVFKI
LQNDIKFIKRSNNKLPSLIKGTGSLIPLKDELEGEEDETGTESEEFLLIVSEFESEYPIDII
>gnl|CDD|213391 cd12148, fungal_TF_MHR, fungal transcription factor regulatory middle homology region. This domain is present in the large family of fungal zinc cluster transcription factors that contain an N-terminal GAL4-like C6 zinc binuclear cluster DNA-binding domain. Examples of members of this large fungal group are the following Saccharomyces cerevisiae transcription factors, GAL4, STB5, DAL81, CAT8, RDR1, HAL9, PUT3, PPR1, ASG1, RSF2, PIP2, as well as the C-terminal domain of the Cep3, a subunit of the yeast centromere-binding factor 3. It has been suggested that this region plays a regulatory role
PPREVADRLLDLYFENVHPLFPILHRPTFLRDLESLYSDPSSLSPASLALLLAVLALAALSLPDSELRGE
SRRSLAERYYEAARQLLDLALFLPPSLETLQALLLLALYLLGTGDPSSAWLLLGLAIRLAQSLGLHRDPS
SLPGLSPFERELRRRLWWSLYILDRLLSLSLGRPPSISDEDIDVPLPSNEDDELSPSSSPPPPPSEEPTS
LSFFIALIRLARILGRILRLLYSPRASSPEDSLETILELDAELEEWRASLPPELRLDSSSLESPSLLPQR
LLLHLLYHLLLILLHRPFLLRSLSSLSPSSSSAESRRACLEAAREILELLRLLLSSSLLLLLWWFLLYYL
FSAALVLLLALLLRPSSSELEEARSLLERALELLERLSERWPRLARRALRLLERLLARAR
>gnl|CDD|213392 cd12149, Flavi_E_C, Immunoglobulin-like domain III (C-terminal domain) of Flavivirus envelope glycoprotein E. The C-terminal domain (domain III) of Flavivirus glycoprotein E appears to be involved in low-affinity interactions with negatively charged glycoaminoglycans on the host cell surface. Domain III may also play a role in interactions with alpha-v-beta-3 integrins in West Nile virus, Japanese encephalitis virus, and Dengue virus. The interface between domain I and domain III appears to be destabilized by the low-pH environment of the endosome, and domain III may play a vital role in the conformational changes of envelope glycoprotein E that follow the clathrin-mediated endocytosis of viral particles and are a prerequisite to membrane fusion
KFSWKKEPADTGHGTVVMEVKYSGTDAPCRIPVRVVDSGSGGENVGRLITVNPIITNANSKVFIEVEPPF
GDSYIVVGVGDTRLKHQWFQK
>gnl|CDD|213393 cd12150, talin-RS, rod-segment of the talin C-terminal domain. The talin rod-segment characterize by this model interacts with its N-terminal FERM domain to mask its integrin-binding site and interferes with interactions between the FERM domain and the cellular membrane. Talin is a large and ubiquitous cytoskeletal protein concentrated at focal adhesion sites. It is involved in linking integrins to the actin cytoskeleton
KAPGQRECDQAIETLNNCIRELDQASLAAISQGLAPRRDNSLQGFQEQMLHSVSEILDKIEPLRSAAKGE
AEQLGHAVTQMAQYFEPLVQAAIGAASKTVNSQQQMALLDQTKTVAESALQLVYAAKEAGGNPKAVHAHP
AVDEAAQMLKEAIEDLTQTLEEAASEAGVVSG
>gnl|CDD|213394 cd12151, F1-ATPase_gamma, mitochondrial ATP synthase gamma subunit. The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinisic membrane domain of F-ATPases is composed of alpha, beta, gamma, delta, and epsilon (not present in bacteria) subunits with a stoichiometry of 3:3:1:1:1. Alpha and beta subunit form the globular catalytic moiety, a hexameric ring of alternating subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton translocating domain
ASLKEIKRRIKSVKNTQKITKAMKMVAAAKLRKAQRALEAARPYAEKLEEVLQRLLSSLDDEDPPLLEKR
EVKKVLLIVITSDRGLCGGFNSNIIKAAEELIKEADGKEVKLIVVGKKGRDYLKRRGYNIALPFSDIGDD
PTYFEAASIIEELILDFLNGEIDEVYIIYNKFKSAISQEPVVEQLLPLDKEEEEEESEGSRSDYIFEPDP
EEVLDALLPFYLASLLYRALLESLASEQAARMTAMDNATDNAGELIDKLTLEYNRARQAAITQELIEIVS
GA
>gnl|CDD|213395 cd12152, F1-ATPase_delta, mitochondrial ATP synthase delta subunit. The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinisic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. Alpha and beta subunit form the globular catalytic moiety, a hexameric ring of alternating subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton translocating domain. In bacteria, which is lacking a eukaryotic epsilon subunit homolog, this subunit is called the epsilon subunit
LKLEIVTPERVFFSGEVESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVTP
NRVTILADEAERPEDIDVERAEEALERAEERLAQAKDEREKARAEAALERALA
>gnl|CDD|213396 cd12153, F1-ATPase_epsilon, eukaryotic mitochondrial ATP synthase epsilon subunit. The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes, and in chloroplast thylakoid membranes. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits (only found in eukaryotes, lacking in bacteria) with a stoichiometry of 3:3:1:1:1. Alpha and beta subunit form the globular catalytic moiety, a hexameric ring of alternating subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton translocating domain.The epsilon subunit is thought to be involved in the regulation of ATP synthase, since a null mutation increased oligomycin sensitivity and decreased inhibition by inhibitor protein IF1
YWRAAGLSYLRYSNICARALRRALKEPFRAKALKREETELKQTKW
>gnl|CDD|240631 cd12154, FDH_GDH_like, Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases. The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases
IAGPKEIKNEEFRVGLSPSVVATLVEAGHEVRVETGAGIGAGFADQAYVQAGAIVVTLAKALWSLDVVLK
VKEPLTNAEYALIQKLGDRLLFTYTIGADHRDLTEALARAGLTAIAVEGVELPLLTSNSIGAGELSVQFI
ARFLEVQQPGRLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNVEEL
EEALAEADVIVTTTLLPGKRAGILVPEELVEQMKPGSVIVNVAVGAVGCVQALHTQLLEEGHGVVHYGDV
NMPGPGCAMGVPWDATLRLAANTLPALVKL
>gnl|CDD|240632 cd12155, PGDH_1, Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family. Phosphoglycerate Dehydrogenase (PGDH) catalyzes the NAD-dependent conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first step in serine biosynthesis. Over-expression of PGDH has been implicated as supporting proliferation of certain breast cancers, while PGDH deficiency is linked to defects in mammalian central nervous system development. PGDH is a member of the 2-hydroxyacid dehydrogenase family, enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
KKLLTLDYGDEKEEQIEDLGYDVDVVFEDELSDEEDLEDIEILYGYNPDFDELDLAKMKNLKWIQLYSAG
VDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGLKKAYKNQKEKKWKMDSSLLELYGKTILF
LGTGSIGQEIAKRLKAFGMKVIGVNTSGRDVEYFDKCYPLEELDEVLKEADIVVNVLPLTEETHHLFDEA
FFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPLPKDSPLWDLDNVLITPHISGVSE
HFNERLFDIFYENLKSFLEDGELLKNVVDLNKGY
>gnl|CDD|240633 cd12156, HPPR, Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase. Hydroxy(phenyl)pyruvate reductase (HPPR) catalyzes the NADP-dependent reduction of hydroxyphenylpyruvates, hydroxypyruvate, or pyruvate to its respective lactate. HPPR acts as a dimer and is related to D-isomer-specific 2-hydroxyacid dehydrogenases, a superfamily that includes groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
PDVLQLGPLPPELLAELEARFTVHRLWEAADPAALLAEHGGRIRAVVTNGETGLSAALIAALPALELIAS
FGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRFVRAGRWPKGAFPLTRKVS
GKRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRPKPDVPYRYYASLLELAAESDVLVVACPGGPATRHLV
NAEVLEALGPDGVLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEPNVPAALLDLDNVVLTPHIASA
TVETRRAMGDLVLANLEAFFA
>gnl|CDD|240634 cd12157, PTDH, Thermostable Phosphite Dehydrogenase. Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain
KPKVVITHKVHPEVLELLKPHCEVISNQTDEPLSREELLRRCKDADGLMAFMPDRIDADFLDACPRLKII
ACALKGYDNFDVEACTARGIWVTIVPDLLTEPTAELTIGLLIGLGRHILAGDRFVRSGKFGGWRPKFYGT
GLDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHPLDQAEEQALNLRRVELDELLESSDFLVLALPLT
PDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAADVFEMEDWARPDRPRSIPQEL
LDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG
>gnl|CDD|240635 cd12158, ErythrP_dh, D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains. D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence
KILADENIPYAEELFSPLGEVTYLPGREITAEDLKDADVLLVRSVTKVNEALLEGSKVKFVGTATIGTDH
IDTDYLKERGIGFANAPGCNANSVAEYVLSALLVLAQRQGFSLKGKTVGIVGVGNVGSRLARRLEALGMN
VLLCDPPRAEAEGDPGFVSLEELLAEADIITLHVPLTRDGEHPTYHLLDEDFLAALKPGQILINASRGAV
IDNQALLALLQRGKDLRVVLDVWENEPEIDLELLDKVDIATPHIAGYSLEGKARGTEMIYEALCQFLGLK
ARKSLSDLLPAPALPSITLDGSLDEALLARLVRAVYDIRRDDARLRKTLALPAGFDALRKNYP
>gnl|CDD|240636 cd12159, 2-Hacid_dh_2, Putative D-isomer specific 2-hydroxyacid dehydrogenases. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
IAVGPSPWPETVAAVEAGGGERVELDEDADALVWTGSAREPERLPASPGVRWVQLPFAGVEAFVEAGVIT
DPGRRWTNAAGAYAETVAEHALALLLAGLRQLPARARATTWDPAEEDDLVTLLRGSTVAIVGAGGIGRAL
IPLLAPFGAKVIAVNRSGRPVEGADETVPADRLDEVWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAW
LVNVARGPLVDTDALVDALRSGEIAGAALDVTDPEPLPDGHPLWSLPNALITPHVANTPEVIRPLLAERV
AENVRAFAAGEPLLGVVDPEAGY
>gnl|CDD|240637 cd12160, 2-Hacid_dh_3, Putative D-isomer specific 2-hydroxyacid dehydrogenases. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
MKILLPTSLPLDPELPPGVTAVPYDVAAPVPAEHHDAEVLVVWGNSSDNLADAARRLTRLRWVQALAAGP
DAVLAAGFAPEVAVTSGRGLHDGTVAEHTLALILAAVRRLDEMREAQREHRWAGELGGLQPLRPAGRLTT
LLGARVLIWGFGSIGQRLAPLLTALGARVTGVARSAGERAGFPVVAEDELPELLPETDVLVMILPATPST
AHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALESGRLGGAALDVTATEPLPASSPLWDAPNLILTP
HAAGGRPQGAEELIAENLRAFLAGGPLRNV
>gnl|CDD|240638 cd12161, GDH_like_1, Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family. This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, aka Hydroxypyruvate Reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
KIVLLEPLGVSEEKIEELAAPLEEQGHEFVYYDTKTTDTAELIERSKDADIVMIANMPLPGEVIEACKNL
KMISVAFTGVDHVDLEACKERGITVSNAAGYSTEAVAELTIGLAIDLLRNIVPCDAAVRAGGTKAGLIGR
ELAGKTVGIVGTGAIGLRVARLFKAFGCKVLAYSRSEKEEAKALGIEYVSLDELLAESDIVSLHLPLNDE
TKGLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDMEPPLPADYPLLHAPNTIL
TPHVAFATEEAMEKRAEIVFDNIEAWLAGKPQNVV
>gnl|CDD|240639 cd12162, 2-Hacid_dh_4, Putative D-isomer specific 2-hydroxyacid dehydrogenases. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
MKIVFLDGYTLNPGDLSWDPLEFLGELTVYDRTSPEEVVERIKDADIVITNKVVLDAEVLAQLPNLKLIG
VLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLALARLVAYHNDVVKAGEWQKSPDFCFWDY
PIIELAGKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPPLREGYVSLDELLAQSDVISLHCPLTPE
TRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEPPRADNPLLKAAPNLII
TPHIAWASREARQRLMDILVDNIKAFL
>gnl|CDD|240640 cd12163, 2-Hacid_dh_5, Putative D-isomer specific 2-hydroxyacid dehydrogenases. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
WLAKLRKRFPGLEIRWVESAPPDGPPEDVPAEVWEGVTILCTFHPHPDAEDVPNLRLVQLFSAGADHWLG
HPLYKDPEVPLCTASGIHGPQIAEWVIGTWLVLSHHFLQYIELQKEQTWGRRQEAYSVEDSVGKRVGILG
YGSIGRQTARLAQALGMEVYAYTRSPRPTPESRKDDGYIVPGTGDPDGSIPSAWFSGTDKASLHEFLRQD
LDLLVVSLPLTPATKHLLGAEEFEILAKRKTFVSNIARGSLVDTDALVAALESGQIRGAALDVTDPEPLP
ADHPLWSAPNVIITPHVSWQTQEYFDRALDVLEENLERLRKGEPLINLVDRERG
>gnl|CDD|240641 cd12164, GDH_like_2, Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family. This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
MTILFASPPDRAAAWRAALAAALPDIEVVVWPDPADPADVDYALVWKPPPGLLARLPNLKAIFSLGAGVD
HLLADPDLPDVPIVRLVDPGLAQGMAEYVLAAVLRLHRDMDRYAAQQRRGVWKPLPQRPAAERRVGVLGL
GELGAAVARRLAALGFPVSGWSRSPKDIEGVTCFHGEEGLDAFLAQTDILVCLLPLTPETRGILNAELLA
RLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLPADHPLWRHPRVTVTPHIAAITDPDS
AAAQVAENIRRLEAGEPLPNLVDRAR
>gnl|CDD|240642 cd12165, 2-Hacid_dh_6, Putative D-isomer specific 2-hydroxyacid dehydrogenases. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
MKVLVNFKAELREEFEAALEGLYAEVPELPDEAAEEALEDADVLVGGRLTKEEALAALKRLKLIQVPSAG
VDHLPLERLPEGVVVANNHGNSPAVAEHALALILALAKRIVEYDNDLRRGIWHGRAGEEPESKELRGKTV
GILGYGHIGREIARLLKAFGMRVIGVSRSPKEDEGADFVGTLSDLDEALEQADVVVVALPLTKQTRGLIG
AAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVWWRYPSRGDPVAPSRYPFHELPNVIMS
PHNAGWTEETFRRRIDEAAENIRRYLRGEPLLNL
>gnl|CDD|240643 cd12166, 2-Hacid_dh_7, Putative D-isomer specific 2-hydroxyacid dehydrogenases. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
TVLVPDPELVAALGPLPPGVEVVVWDGEGPPPDAAADVEFVVPPYMAAPPVLEALRALPRLRVVQTLSAG
YDGVLPLLPEGVTLCNARGVHDASTAELAVALILASLRGLPRFVRAQARGRWEPRRTPSLADRRVLIVGY
GSIGRAIERRLAPFEVRVTRVARTARPGEQVHGIDELPALLPEADVVVLIVPLTDETRGLVDAEFLARMP
DGALLVNVARGPVVDTDALVAELASGRLRAALDVTDPEPLPPGHPLWSAPGVLITPHVGGATPAFLPRAY
ALVRRQLRRYAAGEPLENVV
>gnl|CDD|240644 cd12167, 2-Hacid_dh_8, Putative D-isomer specific 2-hydroxyacid dehydrogenases. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
RILLAMDPERRDLFFGPAALARLAALAEVLPPTPDADFAAEELRALLAGVEVLVTGWGTPPLDAELLARA
PRLRAVVHAAGSVRGLVTDAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRDWGWP
TRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELVSLDELLARSDVVSL
HAPLTPETRGMIDARLLALMRDGATFINTARGALVDEAALLAELRSGRLRAALDVTDPEPLPPDSPLRTL
PNVLLTPHIAGSTGDERRRLGDYALDELERFLAGEPLLHEVTPERLARMA
>gnl|CDD|240645 cd12168, Mand_dh_like, D-Mandelate Dehydrogenase-like dehydrogenases. D-Mandelate dehydrogenase (D-ManDH), identified as an enzyme that interconverts benzoylformate and D-mandelate, is a D-2-hydroxyacid dehydrogenase family member that catalyzes the conversion of c3-branched 2-ketoacids. D-ManDH exhibits broad substrate specificities for 2-ketoacids with large hydrophobic side chains, particularly those with C3-branched side chains. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Glycerate dehydrogenase catalyzes the reaction (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain
KPKVLLLGDPIHAHDEWKELSSIAEVIYPTSGTREEFIEALKEGKYGDFVAIYRTFGSAGETGPFDEELI
SPLPPSLKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKW
RGFLDLTLAHDPRGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSRLPEELEKALATYYVSLDELLAQS
DVVSLNCPLTAATRHLINKKEFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEPEVNP
GLLKMPNVTLLPHMGTLTVETQEKMEELVLENIEAFLETGK
>gnl|CDD|240646 cd12169, PGDH_like_1, Putative D-3-Phosphoglycerate Dehydrogenases. Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric
RIAILDDYQDVARTLADWSKLDDRAEVTVFNDHLLDEDALAERLAPFDAIVLMRERTPFPAALLERLPNL
KLLVTTGMRNASIDLAAAKERGIVVCGTGGGPTATAELTWALILALARNLPEEDAALRAGGWQTTLGTGL
AGKTLGIVGLGRIGARVARIGQAFGMRVIAWSSNLTAERAAAAGVEAAVSKEELFATSDVVSLHLVLSDR
TRGLVGAEDLALMKPTALLVNTSRGPLVDEGALLAALRAGRIAGAALDVFDVEPLPADHPLRGLPNVLLT
PHIGYVTEEAYEGFYGQAVENIAAWLAG
>gnl|CDD|240647 cd12170, 2-Hacid_dh_9, Putative D-isomer specific 2-hydroxyacid dehydrogenases. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
FKKIVAIDPTGLNEEAEEELKKYAEEVVFYDDIPESDEEIIERIGDADCVLVSYTTQIDEEVLEACPNIK
YIGMCCSLYSEESANVDIAAARENGITVTGIRDYGDEGVVEYVISELIRLLHGFGGKQWKEEPRELTGLK
VGIIGLGTTGQMIADALSFFGADVYYYSRTRKPDAEAKGIRYLPLNELLKTVDVICTCLPKNVILLGEEE
FELLGDGKILFNTSLGPSFEVEALKKWLKASGYNIFDCDTAGALGDEELLRYPNVICTNKSAGWTRQAFE
RLSQKVLANLEEYL
>gnl|CDD|240648 cd12171, 2-Hacid_dh_10, Putative D-isomer specific 2-hydroxyacid dehydrogenases. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
MKELETAPIDWPDEPFEDLQEVILVVEKSGPEAVEPEEELLEALKDADILITHFAPVTKKVIEAAPKLKL
IGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLAETRNIARAHAALKDGEWRKDYYNYDG
YGPELRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPYVDPEKIEADGVKKVSLEELLKRSDVVSLHAR
LTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPEEPLPADHPLLKLDN
VTLTPHIAGATRDVAERSPEIIAEELKRYL
>gnl|CDD|240649 cd12172, PGDH_like_2, Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains. Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric
KVLVTPRSFSKYSEEAKELLEAAGFEVVLNPLGRPLTEEELIELLKDADGVIAGLDPITEEVLAAAPRLK
VISRYGVGYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLMLALARQIPQADREVRAGGWDRPVGTEL
YGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDEEFAKEHGVEFVSLEELLKESDFISLHLPLTPET
RHLINAAELALMKPGAILINTARGGLVDEEALYEALKSGRIAGAALDVFEEEPPPADSPLLELPNVILTP
HIGASTKEAVLRMGTMAAQNVIDVLA
>gnl|CDD|240650 cd12173, PGDH_4, Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains. Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence
KVLVTDPIDEEGLELLREAGIEVDVAPGLSEEELLAIIADADALIVRSATKVTAEVIEAAPRLKVIGRAG
VGVDNIDVEAATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKWDRKKFMGVELRGKT
LGIVGLGRIGREVARRARAFGMKVLAYDPYISAERAAAGGVELVSLDELLAEADFISLHTPLTPETRGLI
NAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEPPPADSPLLGLPNVILTPHLGA
STEEAQERVAVDAAEQVLAVLAGE
>gnl|CDD|240651 cd12174, PGDH_like_3, Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains. Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric
MKILTANKISKKGLERFKKDKYEVKEDALEDPDALIVRSDKLHDMDFAPSLKAIARAGAGVNNIDVDAAS
KRGIVVFNTPGANANAVAELVIAMMLALSRNIIQAIKWVTNGDGDDISKGVEKGKKQFVGTELRGKTLGV
IGLGNIGRLVANAALALGMKVIGYDPYLSVEAAWKLSVEVQRVTSLEELLATADYITLHVPLTDETRGLI
NAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDFPEPALLGHLPNVIATPHLGASTEEAE
ENCAVMAARQIMDFLETGNITNSVN
>gnl|CDD|240652 cd12175, 2-Hacid_dh_11, Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
KVLFLGPEFPDAEELLRALLPPAPGVEVVTAAELDEEAALLADADVLVPGMRKVIDAELLAAAPRLRLIQ
QPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAGRWGRPEGRPSREL
SGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFRDPEAEEKDLGVRYVELDELLAESDVVSLHVPLTPE
TRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPLPPDDPLLRLDNVILT
PHIAGVTDESYQRMAAIVAENIARLLRGEPP
>gnl|CDD|240653 cd12176, PGDH_3, Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains. Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence
IKILLLENIHPSADELFRAGGIEVERLKGALDEDELIEALKDVHLLGIRSKTQLTEEVLEAAPKLLAIGC
FCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARRLPDRNAAAHRGIWNKSATGSHEVRG
KTLGIIGYGHIGSQLSVLAEALGMRVIFYDIAEKLPLGNARQVSSLEELLAEADFVTLHVPATPSTKNMI
GAEEIAQMKKGAILINASRGTVVDIDALAEALRSGHLAGAAVDVFPEEPASNGEPFSSPLQGLPNVILTP
HIGGSTEEAQENIGLEVAGKLVKY
>gnl|CDD|240654 cd12177, 2-Hacid_dh_12, Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
KIAIVNSSSFGQYFPEHIQRLKKIGYVDRFEVPPDISGKALAEKLKGYDIIIASVTPNFDKEFFEYNDGL
KLIARHGIGYDNVDLKAATEHGVIVTRVPGAVERDAVAEHAVALILTVLRKINQASEAVKEGKWTERANF
VGHELSGKTVGIIGYGNIGSRVAEILKEGFNAKVLAYDPYVSEEVIKKKGAKPVSLEELLAESDIISLHA
PLTEETYHMINEKAFSKMKKGVILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIKADHPLLHYE
NVVITPHIGAYTYESLYGMGEKVVDDIEDFLAGKEPKGILN
>gnl|CDD|240655 cd12178, 2-Hacid_dh_13, Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
AKVLVTGWIPKEALEELEENFEVTYYDGLGLISKEELLERIADYDALITPLSTPVDKEIIDAAKNLKIIA
NYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARRIAEGDRLMRRGGFLGWAPLFFLGH
ELAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHRLSEETEKELGATYVDLDELLKESDFVSLHAPYT
PETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEPEVSPELKKLDNVIL
TPHIGNATVEARDAMAKEAADNIISFLEGKRPKNIVN
>gnl|CDD|240656 cd12179, 2-Hacid_dh_14, Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
KILIIDKNHPSLTELLEALGFEVDYDPTISREEILAIIPQYDGLIIRSRFPIDKEFIEKATNLKFIARAG
AGLENIDLEYAKEKGIELFNAPEGNRDAVGEHALGMLLALFNKLNRADQEVRNGIWDREGNRGVELMGKT
VGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNFGDAYAEQVSLETLFKEADILSLHIPLTPETRGMVNKE
FISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLDVLEYEKASFESIFNQPEAFEYLIKSPKVIL
TPHIAGWTFESYEKIAEVLVDKIKAL
>gnl|CDD|240657 cd12180, 2-Hacid_dh_15, Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric
LVIASQLDAPLNAVIRRHLGGVEVIEVPPGPAWDLPADADVLLARPTNGRGAAPAVPPPGWPGRLRWVQL
VSSGIDYYPDWLFEGPVVTCARGVAAEAIAEFVLAAILAAAKRLPEIWVKGAEQWRREPLGSLAGSTLGI
VGFGAIGQALARRALALGMRVLALRRSGRPSDVPGVEAAADLAELFARSDHLVLAAPLTPETRHLINADV
LAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPEPLPEGHPLYTHPRVRLSPHTSAIAPD
GRRNLADRFLENLARYRAGQPLHDLVDP
>gnl|CDD|240658 cd12181, ceo_syn, N(5)-(carboxyethyl)ornithine synthase. N(5)-(carboxyethyl)ornithine synthase (ceo_syn) catalyzes the NADP-dependent conversion of N5-(L-1-carboxyethyl)-L-ornithine to L-ornithine + pyruvate. Ornithine plays a key role in the urea cycle, which in mammals is used in arginine biosynthesis, and is a precursor in polyamine synthesis. ceo_syn is related to the NAD-dependent L-alanine dehydrogenases. Like formate dehydrogenase and related enzymes, ceo_syn is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. These ceo_syn proteins have a partially conserved NAD-binding motif and active site residues that are characteristic of related enzymes such as Saccharopine Dehydrogenase
KTGGFGISNKENEKRVPLLPADLERIPLREQLYFEEGYGERLGISDEEYAALGAGIVSREEILAKCDVIC
DPKPGDADYLEILEGQILWGWVHCVQDKEITQLAIDKKLTLIAWEDMFEWSKIGRHVFYKNNELAGYAAV
LHALQLYGITPYRQTKVAVLGFGNTARGAIRALKLGGADVTVYTRRTEALFKEELSEYDIIVNCILQDTD
RPDHIIYEEDLKRLKPGALIIDVSCDEGMGIEFAKPTTFDDPIYKVDGIDYYAVDHTPSLFYRSASRSIS
KALAPYLDTVIEGRE
>gnl|CDD|240659 cd12183, LDH_like_2, D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains. D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2-domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain
MKIAVFSTKPYDREFFEAANEGYGHELTYFEERLTEETASLAKGFDAVCVFVNDDLDAPVLEKLAELGVK
LIALRCAGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGNFSLDGLLGF
DLHGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPELAKLGVEYVDLDELLAESDIISLHCPLTPE
THHLINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLFFEDHSDEIIQDDV
LARLLSFPNVLITGHQAFFTKEALTNIAETTLENLDDFEAGKPLKNEV
>gnl|CDD|240660 cd12184, HGDH_like, (R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic domains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. HGDH is a member of the D-2-hydroxyacid NAD(+)-dependent dehydrogenase family; these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain
MKIICYGVRPVEKPIFEKLNKKFGYDLTLVEEYLNDENVHLAKGHDAVIVRGNCFADKENLEIYKEYGIK
YVFTRTVGFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHTAYTASRTANKNFKVDPFMFS
KEIRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYPSDAAKDVVTFVSLDELLKKSDIISLHVPYIKG
KNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVLNNEKEIFFKDFDGDKIEDP
VVEKLLDLYPRVLLTPHIGSYTDEALSNMIETSYENLKEYLETGDCKNKI
>gnl|CDD|240661 cd12185, HGDH_LDH_like, Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, NAD-binding and catalytic domains. This group contains various putative dehydrogenases related to D-lactate dehydrogenase (LDH), (R)-2-hydroxyglutarate dehydrogenase (HGDH), and related enzymes, members of the 2-hydroxyacid dehydrogenases family. LDH catalyzes the interconversion of pyruvate and lactate, and HGDH catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. Despite often low sequence identity within this 2-hydroxyacid dehydrogenase family, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain
MKIFAYGVRPDELEYFEKFAKEYNVEVTLTKEPLTLENAHLAEGYDGISILGKSKISAELLEKLKEAGVK
YISTRSIGYDHIDLDAAKELGIKVSNVTYSPNSVADYTVMLMLMALRKYKQIMKRAEVNDYSLGGLQGRE
LRNLTVGVIGTGRIGQAVIKNLSGFGCKILAYDPYPNEEVKKYAEYVDLDTLYKESDIITLHTPLTEETY
HLINKESIAKMKDGVIIINTARGELIDTEALIEGLESGKIGGAALDVIEGEDGIYYNDRKGDILSNRELA
ILRSFPNVILTPHMAFYTDQAVSDMVENSIESLVAFEKGGEN
>gnl|CDD|240662 cd12186, LDH, D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding and catalytic domains. D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenases family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain
MKILMYNVRDDEKPYIEEWAKEHPVEVDTTTELLTPETVDLAKGYDGVVVQQTLPYDEEVYEKLAEYGIK
QIALRSAGVDMIDLDLAKENGLKITNVPAYSPRAIAEFAVTQALNLLRNTPEIDRRVAKGDFRWAPGLIG
REIRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPYPNPELEKFLLYYDSLEDLLKQADIISLHVPLTK
ENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAALDTYENETGYFNKDWSGKEIEDE
VLKELIAMPNVLITPHIAFYTDTAVKNMVEISLDDALEIIEGGTSENEV
>gnl|CDD|240663 cd12187, LDH_like_1, D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains. D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain
KIVFFETEEWEQEYFQELLPGHKVVFTSQELLDDNVEEFKDAEVISVFVYSRLDAEVLEKLPRLKLIATR
STGFDHIDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGLRGFELAGK
TLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEELAERLGFRYVSLEELLQESDIISLHVPYTPQTHHL
INRENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDVLEQEEVLREEAELFREDVSPEDLKK
LLADHALLRKPNVIITPHVAYNTKEALERILDTTVENIKAFAAGQPQNV
>gnl|CDD|240664 cd12188, SDH, Saccharopine Dehydrogenase NAD-binding and catalytic domains. Saccharopine Dehydrogenase (SDH) catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SHD is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of related structure
THLWLRAETKPLERRTALTPTTAKKLLDAGFKVTVERSPQRIFPDEEYEAVGCELVPAGSWVNAPKDAII
LGLKELPEDTFPLPHRHIYFAHAYKGQAGWKDVLSRFARGGGTLLDLEYLVDDDGRRVAAFGYWAGFAGA
ALGLLAWAHQQLGPVTLPPVSPYPNEEALVADVKKALATGGRKPRALVIGALGRCGSGAVDLLEAAGIEV
TKWDMAETKAGGPFPEILDHDIFVNCIYLSKPIPPFLTPEMLQAPGRRLRVIGDVSCDPTNPYNPIPIYD
VATTFDKPTLRVPTGGPPLDVIAIDHLPSLLPRESSEDFSNDLLPSLLELAERDTAGVWARAKKLFDTKV
A
>gnl|CDD|240665 cd12189, LKR_SDH_like, bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme. Bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases. Along with formate dehydrogenase and similar enzymes, SDH consists paired domains resembling Rossmann folds in which the NAD-binding domain is inserted within the linear sequence of the catalytic domain. In this bifunctional enzyme, the LKR domain is N-terminal of the SDH domain. These proteins have a close match to the active site motif of SDHs, and an NAD-binding site motif that is a partial match to that found in SDH and other FDH-related proteins
VIGIRREDKNIWERRAPLTPSHVRELVKKPGVKVLVQPSNRRAFPDQEYEAAGAIIQEDLSDADLILGVK
EPPIDKLLPDKTYAFFSHTIKAQPYNMPLLDAILEKNIRLIDYELIVDESGKRLVAFGWFAGVAGMIDIL
HGLGLRLLALGYSTPFLHIGRAYNYPSLEEAKQAVRDAGYEIALGGLPKSLGPLVFVFTGSGNVSQGAQE
IFEELPHEYVEPSDLPELAKSGADRNKVYGCVVTPEDYLERKDGGPFDRADYYANPELYESVFHEKIAPY
LSVLINGIYWDPRFPRLLTNEQLQALLRPPAGPHRLLAIADISCDIGGSIEFLTKATTIDSPFYVYDPDT
DKIHDSVSGDGILVMSVDNLPAELPREASEHFGDALLPYVPDLAKSDASKPLEESELPPVLRRATIASNG
KLTPKYEYIQELR
>gnl|CDD|213397 cd12190, Bacova_04320_like, Uncharacterized proteins similar to Bacteroides ovatus 4320. This model characterized a family of proteins conserved in Bacteroidetes, similar to B. ovatus ATCC 8483 reading frame 04320. Structurally, the protein resembles members of the SRPBCC domain superfamily (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC)
KYLAGAVPEVNGKVVFTKVIEVPGLSKDEIYDRAKKWLTENFKSENSRVIQVNDKEGTIAAKGEEWLVFS
SSFLSLDRTKIKYTIIIKCKDGKYRLTLTRISYDYEVSRQKEKYPAEEWITDKYALNKKKTKLKKLSGKF
RRKTIDRKNEIFDSLKKAL
>gnl|CDD|213398 cd12191, gal11_coact, gall11 coactivator domain. Gall11/MED15 acts in the general regulation of GAL structural genes and is required for full expression for several genes in this pathway, including GALs 1,7, and 10 in Saccharomyces cerevisiae. GAL11 function is dependent on GCN4 functionality and binds GCN4 in a degenerate manner with multiple orientations found at the GCN4-Gal11 interface
PQQQQQPQQQQQQQMPQNPQLVNMMDNMPIPPQLLAKIPNLPPEVKTWRQLKAWLQQNNIPPQAMEQIKE
VQQTHFQLLMQRRQQQQQQQ
>gnl|CDD|213399 cd12192, GCN4_cent, GCN4 central activation domain-like acidic activation domain. GCN4 was identified in Saccharomyces cerevisiae from mutations in a deficiency in activation with the general amino acid control pathway. GCN4 encodes a trans-activator of amino acid biosynthetic genes containing 2 acidic activation domains and a C-terminal bZIP domain, comprised of a basic alpha-helical DNA-binding region and a coiled-coil dimerization region
SADSTPMFDELDFIEDGGKVNSKDDWVSLFDDDIPATAED
>gnl|CDD|269833 cd12193, bZIP_GCN4, Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and dimerization domain. GCN4 was identified in Saccharomyces cerevisiae from mutations in a deficiency in activation with the general amino acid control pathway. GCN4 encodes a trans-activator of amino acid biosynthetic genes containing 2 acidic activation domains and a C-terminal bZIP domain. In amino acid-deprived cells, GCN4 is up-regulated leading to transcriptional activation of genes encoding amino acid biosynthetic enzymes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
DPVAAKRARNTLAARRSRARKLEEMEELEKRVEELEAENEELKTRAEVLEAEAR
>gnl|CDD|213379 cd12194, Kcc4p_like_C, C-terminal kinase associated domain 1 (KA1), a phospholipid binding domain, of Kcc4p and similar proteins. This subfamily is composed of three Saccharomyces cerevisiae proteins, Kcc4p, Gin4p, and Hsl1p, as well as similar serine/threonine protein kinases (STKs). They catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. Kcc4p, Gin4p, and Hsl1p are septin-associated proteins that are involved in septin organization and in the yeast morphogenesis checkpoint coordinating the cell cycle with bud formation. They negatively regulate the Wee1-related kinase Swe1, which phosphorylates the cyclin-dependent kinase Cdc28, and is involved in regulating the entry of cells into mitosis. Kcc4p, Gin4p, and Hsl1p localize in the bud neck in a septin-dependent manner and display distinct but partially overlapping functions. They contain an N-terminal catalytic kinase domain and a C-terminal KA1 domain. The KA1 domain of Kcc4p, Gin4p, and Hsl1p binds acidic phospholipids including phosphatidylserine (PtdSer) and is required for bud neck localization
RNSSFFRKFSGGSSTKKAPSDSDTQLKASILSQQLFNALVKLLQGWSKYGLKNLKSDSSSYTITGKLSSD
NSLSLKSTKFEIKILPEEDQGSEVVFTKKSGSSKTFDKLVDEIEKVLEKEGV
>gnl|CDD|213380 cd12195, CIPK_C, C-terminal regulatory domain of Calcineurin B-Like (CBL)-interacting protein kinases. CIPKs are serine/threonine protein kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They comprise a unique family in higher plants of proteins that interact with the calcineurin B-like (CBL) calcium sensors to form a signaling network that decode specific calcium signals triggered by a variety of environmental stimuli including salinity, drought, cold, light, and mechanical perturbation, among others. The specificity of the response relies on differences in expression and localization of both CBLs and CIPKs, as well as on the interaction specificity of CBL-CIPK combinations. There are 25, 30, and 43 CIPK genes identified in the Arabidopsis thaliana, Oryza sativa, and Zea mays genomes, respectively. The founding member of the CIPK family is Arabidopsis thaliana CIPK24, also called SOS2 (Salt Overlay Sensitive 2). CIPKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory domain that contains the FISL (also called NAF for Asn-Ala-Phe) and PPI-binding motifs, which are involved in the interaction with CBLs and PP2C-type protein phosphatases, respectively. Studies using SOS2, SOS3, and ABI2 phosphatase show that the binding of CBL and PP2C-type protein phosphatase to CIPK is mutually exclusive. The binding of CBL to CIPK is inhibitory to kinase activity
NAFDLISLSSGLDLSGLFEEEDEVKRETRFTSRKPAEEIIEKLEEAAKKLGFRVRKKKEGGVKLEGQKGG
RKGRLAVSVEVFEVTPSLVVVEVKKSAGDTLEYHKFWKDLLRPLLK
>gnl|CDD|213381 cd12196, MARK1-3_C, C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinases 1-3. Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. MARK1/2, through their activation by death-associated protein kinase (DAPK), modulates polarized neurite outgrowth. MARK1, also called Par-1c, is also involved in axon-dendrite specification, and SNPs on the MARK1 gene is associated with autism spectrum disorders. MARK2, also called Par-1b, is implicated in many physiological processes including fertility, immune system homeostasis, learning and memory, growth, and metabolism. MARK3, also called Par-1a, is implicated in gluconeogenesis and adiposity; mice deficient with MARK3 display reduced adiposity, resistance to hepatic steatosis, and defective gluconeogensis. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain
KPRSLRFTWSMKTTSSMDPNDMMREIRKVLDANNCDYEQRERFLLFCVHGDGRTDSLVQWEMEVCKLPRL
SLNGVRFKRISGTSIAFKNIASKIANEL
>gnl|CDD|213382 cd12197, MARK4_C, C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinase 4. Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. MARK4 has two splicing isoforms: MARK4S, predominantly expressed in the brain; and MARK4L, expressed in all tissues. Unlike MARK1-3 that show cytoplasmic localization, MARK4 colocalizes with the centrosome and with microtubules. Decreased MARK4 expression in the brain may be involved in the pathogenesis of Prion diseases and may be correlated to PrP(Sc) deposits. MARK4 is also a component of the ectoplasmic specialization, a testis-specific adherens junction. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain
RLLRGGWDVRLRSSRPPAEVVLALREATAGCGCRVRQAGPFLLACLHGAAGSPEPLVAFEAEVCQLPRGE
LNGVRFKRLWGTPLAFRTIASKISKELEL
>gnl|CDD|213383 cd12198, MELK_C, C-terminal kinase associated domain 1 (KA1) of Maternal embryonic leucine zipper kinase. MELK, also called protein kinase 38 (PK38) or pEg3 kinase, is a cell cycle-regulated serine/threonine protein kinase (STK) that catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It is phosphorylated and maximally active during mitosis and is involved in regulating cell cycle progression, division, proliferation, tumor growth, and mRNA splicing. MELK shows a broad substrate specificity, including the zinc finger-like protein ZPR9, the transcription and splicing factor NIPP1, and the protein-tyrosine phosphatase Cdc25B, among others. MELK contains an N-terminal catalytic domain followed by a ubiquitin-associated (UBA) domain, a TP dipeptide-rich region, and a C-terminal KA1 domain. The KA1 domain of MELK, together with its TP dipeptide-rich region, functions as an autoinhibitory domain. The KA1 domain of the related microtubule affinity-regulating kinases (MARKs) has been shown to bind anionic phospholipids and may be involved in membrane localization
RKVKALYNVSTTSSKDPEQVLNELKRVLAKKGIDCKQKGYTLRCKTKDDFGKVKLTFELEVCRLPGLDEV
VGIRRKRLKGDAWVYKKVCEDILRMA
>gnl|CDD|213384 cd12199, AMPKA1_C, C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha 1 catalytic subunit. AMPK, a serine/threonine protein kinase (STK), catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It acts as a sensor for the energy status of the cell and is activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. AMPK is a heterotrimer of three subunits: alpha, beta, and gamma. Co-expression of the three subunits is required for kinase activity; in the absence of one, the other two subunits get degraded. The AMPK alpha subunit is the catalytic subunit and it contains an N-terminal kinase domain and a C-terminal regulatory domain (RD). Vertebrates contain two isoforms of the alpha subunit, alpha1 and alpha2, which are encoded by different genes, PRKAA1 and PRKAA2, respectively, and show varying expression patterns. AMPKalpha1 is the predominant isoform expressed in bone; it plays a role in bone remodeling in response to hormonal regulation. It is selectively regulated by nucleoside diphosphate kinase (NDPK)-A in an AMP-independent manner. AMPKalpha1 impacts the regulation of fat metabolism through its in vivo target, acetyl coenzyme A carboxylase (ACC). It also mediates the vasoprotective effects of estrogen through phosphorylation of another in vivo substrate, RhoA. The C-terminal RD of the AMPK alpha 1 subunit is involved in AMPK heterotrimer formation. It mainly interacts with the C-terminal region of the beta subunit to form a tight alpha-beta complex that is associated with the gamma subunit. The AMPK alpha subunit RD also contains an auto-inhibitory region that interacts with the kinase domain; this inhibition is negated by the interaction with the AMPK gamma subunit
RAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTFSKMSLQLYQVDSRTYLLD
FRSIDDEITSHTIEFFEMCANLIKIL
>gnl|CDD|213385 cd12200, AMPKA2_C, C-terminal regulatory domain of 5'-AMP-activated serine/threonine kinase, subunit alpha. AMPK, a serine/threonine protein kinase (STK), catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It acts as a sensor for the energy status of the cell and is activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. AMPK is a heterotrimer of three subunits: alpha, beta, and gamma. Co-expression of the three subunits is required for kinase activity; in the absence of one, the other two subunits get degraded. The AMPK alpha subunit is the catalytic subunit and it contains an N-terminal kinase domain and a C-terminal regulatory domain (RD). Vertebrates contain two isoforms of the alpha subunit, alpha1 and alpha2, which are encoded by different genes, PRKAA1 and PRKAA2, respectively, and show varying expression patterns. AMPKalpha2 shows cytoplasmic and nuclear localization, whereas AMPKalpha1 is localized only in the cytoplasm. The C-terminal RD of the AMPK alpha 1 subunit is involved in AMPK heterotrimer formation. It mainly interacts with the C-terminal region of the beta subunit to form a tight alpha-beta complex that is associated with the gamma subunit. The AMPK alpha subunit RD also contains an auto-inhibitory region that interacts with the kinase domain; this inhibition is negated by the interaction with the AMPK gamma subunit
LAVKKAKWHLGIRSQSKPYDIMAEVYRAMKQLDFEWKVVNPYHLRVRRKNPVTGNYVKMSLQLYQVDNRS
YLLDFKSIDDEPRLGSHTMDFFEMCASLITTL
>gnl|CDD|213386 cd12201, MARK2_C, C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinase 2. Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. MARK2, also called Par-1b or ELKL motif kinase 1 (EMK-1), is implicated in many physiological processes including fertility, immune system homeostasis, learning and memory, growth, and metabolism. It also regulates axon formation and has been implicated in neurodegeneration. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain
KPRSLRFTWSMKTTSSMEPNEMMKEIRKVLDANNCQYELQEKYMLLCMHGTPGHDDFVQWEMEVCKLPRL
SLNGVRFKRISGTSIAFKNIASKIANELK
>gnl|CDD|213401 cd12202, CASP8AP2, Caspase 8-associated protein 2 myb-like domain. This domain is the SANT/myb-like domain of Caspase 8-associated protein 2 (CASP8AP2) / GON-4 like proteins. CASP8AP2 (aka Flice-Associated Huge Protein (FLASH)) is implicated in numerous gene regulatory roles including roles in embryogenesis, oncogenesis, down-regulation of replication-dependent histone genes, regulation of Caspase 8 activity at the death-inducing signaling complex (DISC), and as a useful marker in leukemia prognosis. Gon-4 is critical in Caenorhabditis elegans gonadogenesis. Danio rerio GON4 is a regulator of gene expression in hematopoietic development, possibly by repressing expression. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins
NNVIKSKGEKVVLWTRDADRVILTACQEKGASPKTFAALASKLGKKTPQEVSERFRQLMKLFHKSC
>gnl|CDD|213402 cd12203, GT1, GT1, myb-like, SANT family. GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins
KRWPREETLSLIRLRREMESRFQETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK
>gnl|CDD|213176 cd12204, CBD_like, Cellulose-binding domain, chitinase and related proteins. This group contains proteins related to the cellulose-binding domain of Erwinia chrysanthemi endoglucanase Z (EGZ) and Serratia marcescens chitinase B (ChiB). Gram negative plant parasite Erwinia chrysanthemi produces a variety of depolymerizing enzymes to metabolize pectin and cellulose on the host plant. Cellulase EGZ has a modular structure, with N-terminal catalytic domain linked to a C-terminal cellulose-binding domain (CBD). CBD mediates the secretion activity of EGZ. Chitinases allow certain bacteria to utilize chitin as a energy source. Typically, non-plant chitinases are of the glycosidase family 18
AGANAYPNWPQGTHAAGGDLVSYNGAVYQAKWWTQSAPGSDSSWTLVC
>gnl|CDD|213344 cd12205, RasGAP_plexin, Ras-GTPase Activating Domain of plexins. Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Ligand binding activates signal transduction pathways controlling axon guidance in the nervous system and other developmental processes, including cell migration and morphogenesis, immune function, and tumor progression. Plexins are divided into four types (A-D) according to sequence similarity. In vertebrates, type A Plexins serve as the co-receptors for neuropilins to mediate the signaling of class 3 semaphorins except Sema3E, which signals through Plexin D1. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B. Plexin C1 serves as the receptor of Sema7A and plays regulation roles in both immune and nervous systems. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Other proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator
GIPFLDFREYIIRVLFPGVNDHPVLLSKFVHGSRRPDLEDALSQFEQLLCNKQFLLTFIRTLESQPKFSS
RDKCNVASLLMVALQGKMEYATEILFDLLTDLIEKSVSKKHPKLMLRRTESVVEKLLTNWLSLCLYDYLK
ETAGEPLFLLYKALKQQIEKGPVDAIKLIPEIFLTRLLSTKGTLQKFVDDLFESILSVPQRSLPPAIKYL
FDFLDEQARKHGISDPDVLHAWKTNSLPLRFWVNIIKNPDFVFDVNKTPTVDSCLSVIAQTFMDACSTSE
HKLGKDSPSNKLLFAKDIPRYREMVANFYRDISNLPPVSDEEMNSYLAELSESHSGEFNTNVALSELYIY
AVKYGDQLLEALEDDREARVQQLADKLSQVAR
>gnl|CDD|213345 cd12206, RasGAP_IQGAP_related, Ras-GTPase Activating Domain of proteins related to IQGAPs. RasGAP: Ras-GTPase Activating Domain. RasGAP functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a myriad of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGap domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator
SEFIEKNVYVTLPIFQKPTNGKMDSREEFLFIKFILELLKSDIENSNSNQDFLANSDNFWILLLVTFNNL
RERSELKSIFGPLLVQYLENQEIDFESDPSVIYKSLHGRPPLSSEEAIEDDRVSDKFVENLTNLREAVEM
VAEIIFKNVDKIPVEIRYLCTKAYIAFADKFPDESEEDILRAISKILIKSYVAPILVNPENYGFVDNEED
NLNEKARVLLQILSMVFFLKNFDGYLKPLNQYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMSTTR
PCLEILLDKVIEIIQILKENLDEFTPDDQLVQLLEKIVDLSSSSNDKRSGRVTLELNPSAYQFLVNDDKE
RKLYDQVKR
>gnl|CDD|213346 cd12207, RasGAP_IQGAP3, Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3. This family represents the IQ motif containing GTPase activating protein 3 (IQGAP3), which associates with Ras GTP-binding proteins. A primary function of IQGAP proteins is to modulate cytoskeletal architecture. There are three known IQGAP family members: IQGAP1, IQGAP2 and IQGAP3. Human IQGAP1 and IQGAP2 share 62% identity. IQGAPs are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP is an essential regulator of cytoskeletal function. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity, the protein actually lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite of their similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3, only present in mammals, regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton
ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHIL
GPVVQDVLQDKGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVT
DKFLSAITSSVDKIPYGMRYVAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCS
AGGALQPEQRRMLGSVAKVLQHAAANKHFQGDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVD
EYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSDPLHELLEDLGEVPTVQSLIGESWADLGDDP
>gnl|CDD|411994 cd12208, DIP1984-like, DIP1984 family protein and similar proteins. DIP1984 is an uncharacterized protein from Corynebacterium diphtheriae. Some members of this family may have been misnamed as septicolysin
MKLAEALKLRADLQKRIAQLKNRILNNAKVQEGDTPAEDPNELLKELEELLTELEELIIRINRTNSQTKF
EDGKTLTEALAERDVLKLRITILRDLADAASEKQDRYSRSEIKFVSTVDVKELQKKADKLAKELRELDTK
IQEANWTTDL
>gnl|CDD|213404 cd12211, Bc2l-C_N, N-Terminal Domain Of Bc2l-C Lectin. Lectin BC2L-C of Burkholderia cenocepacia is one of several lectins produced by this pathogen. BC2L-C has been shown to bind fucosylated human histo-blood group epitopes H-type 1, Lewis B, and Lewis Y. The C-terminal domain resembles BC2L-A, a calcium dependent mannose-binding protein. The N-terminal domain trimerizes and binds alpha-MeSeFuc in pockets between the monomeric units. The N-terminal domain has a similar structure to tumor necrosis factor (TNF)
LLSASIVSAPVVTSETYVDIPGLYLDVAKAGIRDGKLQVILNVPTPYATGNNFPGIYFAIATNQGVVADG
CFTYSSKVPESTGRMPFTLVATIDVGSGVTFVKGQWKSVRGSAMHIDSYASLSAIGGTAAP
>gnl|CDD|276936 cd12212, Fis1, Mitochondrial Fission Protein Fis1, cytosolic domain. Fis1, along with Dnm1 and Mdv1, is an essential protein in mediating mitochondrial fission. Dnm1 and Fis1 are highly conserved, with a common mechanism in disparate species. In mutants of these proteins, mitochondrial fission is impaired, resulting in networks of undivided mitochondria. The Fis1 N-terminus is cytosolic and tethered to the mitochondrial outer membrane via a C-terminal transmembrane domain. Fis1 appears to act via the recruitment of division complexes to the mitochondrial outer membrane, via interactions with Mdv1 or Caf4. Fis1 has tandem Tetratricopeptide repeat (TPR) motifs which are known to mediate protein-protein interactions
PLSPEELAVLEEQYNSELARGSVSPQTQFNYAWALVKSKNPEDIRRGIELLEELYRDGPERRRECLYYLA
LGHYKLGEYSEARRYVDALLEIEPDNRQALALKELIEDKITKEGL
>gnl|CDD|213406 cd12213, ABD, Alpha-Mannosidase Binding Domain of Atg19/34. These proteins are related to the Alpha-mannosidase (Ams1) Binding Domain of Atg19/Atg34, a key component in the targeting pathway that directs alpha-mannosidase and aminopeptidase I to the vacuole, either through cytoplasm-to-vacuole trafficking or via autophagy in starvation conditions. Autophagy in a eukaryotic mechanism in which cytoplasm is enclosed in double-membraned autophagosomes which fuse with a vacuole for transport into the lumen. In Saccharomyces cerevisiae, alpha-mannosidase is selectively directed to the vacuole via the direct interaction with Atg19 (and paralog Atg34) in the Cvt pathway. Ams1 binding domains (ABD) Atg19/34 have a immunoglobulin fold with eight beta-strands. The ABD is responsible for Ams1 recognition, but its deletion does not affect the fusion of Atg19 with prApe1, and the transport of prApe1 to the vacuole. The Atg19 N-terminal region is a distinct coiled-coil domain
AGSLLVEVNQRDNDLTFRLYNRGDSALPGNLKLVFQYQADDTANPVTVSIYMGPHELQPNGSKKLLNFPY
FGSIILLEGPCKIDLVNQDGEVIYTGKNSSSPKSEFSLKPPN
>gnl|CDD|213177 cd12214, ChiA1_BD, chitin-binding domain of Chi A1-like proteins. This group contains proteins related to the chitin binding domain of chitinase A1 (ChiA1) of Bacillus circulans WL-12. Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal and catalytic domain, and 2 fibronectin type III-like domains. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiAi chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ))
EWAAGTTYKAGDIVTYNGKLYRCLQAHTSLAGWEPPAVPALWQPA
>gnl|CDD|213178 cd12215, ChiC_BD, Chitin-binding domain of chitinase C. Chitin-binding domain of chitinase C (ChiC) of Streptomyces griseus and related proteins. Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. ChiC contains the characteristic chitin-binding aromatic residues
PAWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTSWGVWKL
>gnl|CDD|213409 cd12216, Csn2_like, CRISPR/Cas system-associated protein Csn2. Csn2 is a Nmeni subtype-specific Cas protein, which may function in the adaptation process which mediates the incorporation of foreign nucleic acids into the microbial host genome. Csn 2 may interact directly with double-stranded DNA. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA. Csn2 has been predicted to be a functional analog of Cas4 based on anti-correlated phyletic patterns; also known as SPy1049 family
LFYISHKEVLINNEKITILVGENSEVYYEILQILSNYYEESTILSSDYDEKEISIYHYLLIDDSFGDDIN
DSKKLGKIYSALSKSITDPQENKGHLEKLVEQITLIIEAELIDINLPFEVSYDLDLELLLKAKNISPESG
EWVNIFDKIEEILEVLVELNEKRLLILTNVDQYLTTDELRELCELIKYINLTLILIEFREGYGNIDYILS
DFVIIDN
>gnl|CDD|213410 cd12217, Stu0660_Csn2, Stu0660-like CRISPR/Cas system-associated protein Csn2. Csn2 is a Nmeni subtype-specific Cas protein, which may function in the adaptation process which mediates the incorporation of foreign nucleic acids into the microbial host genome. Csn 2 may interact directly with double-stranded DNA. This family of Csn2 proteins includes Stu0660, the proteins are larger than other (canonical) Csn2 proteins as they have an additional alpha-helical C-terminal domain. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA. Csn2 has been predicted to be a functional analog of Cas4 based on anti-correlated phyletic patterns; also known as SPy1049 family
MKLTITHPYKKNIELNFGQFTQIVGQNVQLKYYIWQILSWYFGGKKYSEEDLSLFNQNEPEIFLDNEKLK
RKSFSIISISSITDIIEQMKYKKGTLLFDYLKKLLDNFDITEQLENINDELDKISLLVNDHLNLQLENIE
YHFESSVLTDQLILKNFLPVFYYNNRNISLEFVSNEEKLLELLNLLERLLSNSTKKILLVLKNLDDFLSY
SSYVEIFEQLKELTKKYPNLYFIIFPSLEGYLYITEEDLEKINIVSDEYEQLPDFEFLYERIEKNYPSND
IPSNEEFLDSLEKIIPYLGSKDQSNQSLSKEDLVLLKILNSLYQYEISVEYKILNQLEENFLK
>gnl|CDD|213411 cd12218, Csn2, CRISPR/Cas system-associated protein Csn2. Csn2 is a Nmeni subtype-specific Cas protein, which may function in the adaptation process which mediates the incorporation of foreign nucleic acids into the microbial host genome. Csn 2 may interact directly with double-stranded DNA. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA. Csn2 has been predicted to be a functional analog of Cas4 based on anti-correlated phyletic patterns; also known as SPy1049 family
KLTYYPHKPIEINPGKITVLSTANPSVYTDLIQGFQNLNDKVKFSDDNYEELDISKAIDWIGDVMLFDLN
KLYLKKIIKKIIENLTDEQRNQITDLNRQLNSVIQDSLFMFDLPLEVDYDFDLKKLLKYCKIHFDTSVWT
NPYDIIETVIKIHAELDLKKLLVLTNVAHYLTVEQINELVQLVKSTELKLLLIEFSEMNRKEFFENCDYY
YIDEDFVDW
>gnl|CDD|340518 cd12219, Ubl_TBK1_like, ubiquitin-like (Ubl) domain found in non-canonical Inhibitor of kappa B kinases IKKepsilon and TBK1, and similar proteins. IKKepsilon and TBK1 (TRAF family member-associated NF-kappaB activator-binding kinase 1) are non-canonical members of IKK family. They have been characterized as activators of nuclear factor-kappaB (NF-kappaB), but they are not essential for NF-kappaB activation. They play critical roles in antiviral response via phosphorylation and activation of transcription factors IRF3, IRF7, STAT1 and STAT3. They are also involved in the survival, tumorigenesis and development of various cancers. Both IKKepsilon and TBK1 contain an N-terminal protein kinase domain followed a ubiquitin-like (Ubl) domain. The Ubl domain acts as a protein-protein interaction domain, and has been implicated in regulating kinase activity, which modulates interactions in the interferon pathway
KKVIHVFSVSTCELLKIYLDPTETLAEFQELIAEQTEIPAKNQLLLFEGQLLEEEVTLPVSDYPKTTEEN
PIILFNK
>gnl|CDD|240617 cd12220, Pesticin_RB, Pesticin Translocation And Receptor Binding Domain. Pesticin (Pst) is a anti-bacterial toxin produced by Yersinia pestis that acts through uptake by the target related bacteria and the hydrolysis of peptidoglycan in the periplasm. Pst contains an N-terminal translocation domain, an intermediate receptor binding domain, and a phage-lysozyme like C-terminal activity domain. The N-terminal domain is further divided into the TonB box (which binds TonB), the T (translocation domain) and the R (receptor binding domain). Bacteriocins such as pesticin are produced by gram-negative bacteria to attack related bacteria stains. Pst is transported to the periplasm via FyuA, an outer-membrane receptor of Y. pestis and E. coli, where it hydrolyzes peptidoglycan via the cleavage of N-acetylmuramic acid and C4 of N-acetylglucosamine. Disruption of the peptidoglycan layer renders the bacteria vulnerable to lysis via osmotic pressure
MSDTMVVNGSGGVPAFLFSGSTLSSYRPNFEANSITIALPHYVDLPGRSNFKLMYIMGFPIDTEMEKDSE
YSNKIRQESKISKTEGTVSYEQKITVETGQEKDGVKVYRVMVLEGTIAESIEHLDKKENEDILNNNRNRI
VLADNTVINFDNISQLKEFLRRSVNI
>gnl|CDD|240616 cd12221, Cin1, Cellophane induced protein repeats of fungus Venturia inaequalis. Cin1 (cellulose induced protein 1) repeat protein of Venturia inaequalis, the fungus responsible for scab disease of apple, encodes 8 cysteine-rich repeats and is greatly upregulated within the plant and on cellophane membranes. The crystal structure reveals a pair of disulfide bridges in each repeat. The repeats have been described as adopting a beads-on-a-string organization. Cin1 function is undetermined, however the alpha-helical structure may be involved in protein-protein or protein-carbohydrate interactions in the extracellular matrix
PPQYGYDGKPLDASFCRKAGSKENECRKDVLACDKKYDDQGRETACSKAIREKYKPFYVAPPPYGYDGKP
LDASFCRLFGAREAECRKDVLACDKKYDNEGRETKCSKAIREKY
>gnl|CDD|240615 cd12222, Caa3-IV, Caa3-Type Cytochrome Oxidase subunit 4 interacts with cyt c subunits I/III. Cytochrome c oxidase, a haem copper oxidase superfamily member, is the final step in the electron-transport chain, linking O2 reduction to transmembrane pumping in mitochondria and aerobic prokaryotes. Cytochrome c oxidase (aka Complex IV) catalyzes the reduction of O2 to 2H2O, and acts downstream of Complexes I-III: NADH-Q oxidoreductase, succinate-Q reductase, and Q-cytochrome c oxidoreductase. In Thermus thermophilus caa3-oxidase is comprised of subunit (SU) I/III, a fusion of classical SU I and SUIII, and IIc as well SU IV, which is composed of 2 connected transmembrane helices that interface with SU I/III
MLYVALFTIGALLVTLVFYLALNPRSLATESETVDLRFIGFALLLIILAAGTVAAMLILGKLG
>gnl|CDD|409670 cd12223, RRM_SR140, RNA recognition motif (RRM) found in U2-associated protein SR140 and similar proteins. This subgroup corresponds to the RRM of SR140 (also termed U2 snRNP-associated SURP motif-containing protein orU2SURP, or 140 kDa Ser/Arg-rich domain protein) which is a putative splicing factor mainly found in higher eukaryotes. Although it is initially identified as one of the 17S U2 snRNP-associated proteins, the molecular and physiological function of SR140 remains unclear. SR140 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a SWAP/SURP domain that is found in a number of pre-mRNA splicing factors in the middle region, and a C-terminal arginine/serine-rich domain (RS domain)
TTNLYVGNLPPSVTEEVLLREFGRFGPLASVKIMWPRTEEERRRNRNCGFVAFMSRADAERAMRELNGKD
VMGYELKLGWGKAV
>gnl|CDD|409671 cd12224, RRM_RBM22, RNA recognition motif (RRM) found in Pre-mRNA-splicing factor RBM22 and similar proteins. This subgroup corresponds to the RRM of RBM22 (also known as RNA-binding motif protein 22, or Zinc finger CCCH domain-containing protein 16), a newly discovered RNA-binding motif protein which belongs to the SLT11 gene family. SLT11 gene encoding protein (Slt11p) is a splicing factor in yeast, which is required for spliceosome assembly. Slt11p has two distinct biochemical properties: RNA-annealing and RNA-binding activities. RBM22 is the homolog of SLT11 in vertebrate. It has been reported to be involved in pre-splicesome assembly and to interact with the Ca2+-signaling protein ALG-2. It also plays an important role in embryogenesis. RBM22 contains a conserved RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a zinc finger of the unusual type C-x8-C-x5-C-x3-H, and a C-terminus that is unusually rich in the amino acids Gly and Pro, including sequences of tetraprolines
ITTLYVGGLGDKITEKDLRDHFYQFGEIRSITVVARQQCAFVQFTTRQAAERAAERTFNKLIIKGRRLKV
KWGR
>gnl|CDD|409672 cd12225, RRM1_2_CID8_like, RNA recognition motif 1 and 2 (RRM1, RRM2) found in Arabidopsis thaliana CTC-interacting domain protein CID8, CID9, CID10, CID11, CID12, CID 13 and similar proteins. This subgroup corresponds to the RRM domains found in A. thaliana CID8, CID9, CID10, CID11, CID12, CID 13 and mainly their plant homologs. These highly related RNA-binding proteins contain an N-terminal PAM2 domain (PABP-interacting motif 2), two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a basic region that resembles a bipartite nuclear localization signal. The biological role of this family remains unclear
RTIHVGGIDGSLSEDELADYFSNCGEVTQVRLCGDRVHTRFAWVEFATDASALSALNLDGTTLGGHPLRV
SPSKTA
>gnl|CDD|409673 cd12226, RRM_NOL8, RNA recognition motif (RRM) found in nucleolar protein 8 (NOL8) and similar proteins. This model corresponds to the RRM of NOL8 (also termed Nop132) encoded by a novel NOL8 gene that is up-regulated in the majority of diffuse-type, but not intestinal-type, gastric cancers. Thus, NOL8 may be a good molecular target for treatment of diffuse-type gastric cancer. Also, NOL8 is a phosphorylated protein that contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), suggesting NOL8 is likely to function as a novel RNA-binding protein. It may be involved in regulation of gene expression at the post-transcriptional level or in ribosome biogenesis in cancer cells
RLFVGGLSPSITEDDLERRFSRFGTVSDVEIIRKKDAPDRGFAYIDLRTSEAALQKCLSTLNGVKWKGSR
LKIQLAK
>gnl|CDD|409674 cd12227, RRM_SCAF4_SCAF8, RNA recognition motif (RRM) found in SR-related and CTD-associated factor 4 (SCAF4), SR-related and CTD-associated factor 8 (SCAF8) and similar proteins. This subfamily corresponds to the RRM in a new class of SCAFs (SR-like CTD-associated factors), including SCAF4, SCAF8 and similar proteins. The biological role of SCAF4 remains unclear, but it shows high sequence similarity to SCAF8 (also termed CDC5L complex-associated protein 7, or RNA-binding motif protein 16, or CTD-binding SR-like protein RA8). SCAF8 is a nuclear matrix protein that interacts specifically with a highly serine-phosphorylated form of the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II (pol II). The pol II CTD plays a role in coupling transcription and pre-mRNA processing. In addition, SCAF8 co-localizes primarily with transcription sites that are enriched in nuclear matrix fraction, which is known to contain proteins involved in pre-mRNA processing. Thus, SCAF8 may play a direct role in coupling with both, transcription and pre-mRNA processing, processes. SCAF8 and SCAF4 both contain a conserved N-terminal CTD-interacting domain (CID), an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain), and serine/arginine-rich motifs
CSTTLWVGHLSKKVTQEELKNLFEEYGEIQSIDMIPPRGCAYVCMKTRQDAHRALQKLKNHKLRGKSIKI
AWAPNKG
>gnl|CDD|409675 cd12228, RRM_ENOX, RNA recognition motif (RRM) found in the cell surface Ecto-NOX disulfide-thiol exchanger (ECTO-NOX or ENOX) proteins. This subgroup corresponds to the conserved RNA recognition motif (RRM) in ECTO-NOX proteins (also termed ENOX), comprising a family of plant and animal NAD(P)H oxidases exhibiting both, oxidative and protein disulfide isomerase-like, activities. They are growth-related and drive cell enlargement, and may play roles in aging and neurodegenerative diseases. ENOX proteins function as terminal oxidases of plasma membrane electron transport (PMET) through catalyzing electron transport from plasma membrane quinones to extracellular oxygen, forming water as a product. They are also hydroquinone oxidases that oxidize externally supplied NADH, hence NOX. ENOX proteins harbor a di-copper center that lack flavin. ENOX proteins display protein disulfide interchange activity that is also possessed by protein disulfide isomerase. In contrast to the classic protein disulfide isomerases, ENOX proteins lack the double CXXC motif. This family includes two ENOX proteins, ENOX1 and ENOX2. ENOX1, also termed candidate growth-related and time keeping constitutive hydroquinone [NADH] oxidase (cCNOX), or cell proliferation-inducing gene 38 protein, or Constitutive Ecto-NOX (cNOX), is the constitutively expressed cell surface NADH (ubiquinone) oxidase that is ubiquitous and refractory to drugs. ENOX2, also termed APK1 antigen, or cytosolic ovarian carcinoma antigen 1, or tumor-associated hydroquinone oxidase (tNOX), is a cancer-specific variant of ENOX1 and plays a key role in cell proliferation and tumor progression. In contrast to ENOX1, ENOX2 is drug-responsive and harbors a drug binding site to which the cancer-specific S-peptide tagged pan-ENOX2 recombinant (scFv) is directed. Moreover, ENOX2 is specifically inhibited by a variety of quinone site inhibitors that have anticancer activity and is unique to the surface of cancer cells. ENOX proteins contain many functional motifs
ERPPGCKTVFVGGLPENATEEIIREVFEQCGEIIAIRMSKKNFCHIRFAEEFAVDKAIYLSGYRVRLGSS
TDPKNTGRLHVDFA
>gnl|CDD|409676 cd12229, RRM_G3BP, RNA recognition motif (RRM) found in ras GTPase-activating protein-binding protein G3BP1, G3BP2 and similar proteins. This subfamily corresponds to the RRM domain in the G3BP family of RNA-binding and SH3 domain-binding proteins. G3BP acts at the level of RNA metabolism in response to cell signaling, possibly as RNA transcript stabilizing factors or an RNase. Members include G3BP1, G3BP2 and similar proteins. These proteins associate directly with the SH3 domain of GTPase-activating protein (GAP), which functions as an inhibitor of Ras. They all contain an N-terminal nuclear transfer factor 2 (NTF2)-like domain, an acidic domain, a domain containing PXXP motif(s), an RNA recognition motif (RRM), and an Arg-Gly-rich region (RGG-rich region, or arginine methylation motif)
PDNHQLFVGNLPHDITEDELKEFFSRFGNVLELRINSKGGGGRLPNFGFVVFDDPEAVQKILANKPIMFR
GEHRLNVEEKK
>gnl|CDD|409677 cd12230, RRM1_U2AF65, RNA recognition motif 1 (RRM1) found in U2 large nuclear ribonucleoprotein auxiliary factor U2AF 65 kDa subunit (U2AF65) and similar proteins. The subfamily corresponds to the RRM1 of U2AF65 and dU2AF50. U2AF65, also termed U2AF2, is the large subunit of U2 small nuclear ribonucleoprotein (snRNP) auxiliary factor (U2AF), which has been implicated in the recruitment of U2 snRNP to pre-mRNAs and is a highly conserved heterodimer composed of large and small subunits. U2AF65 specifically recognizes the intron polypyrimidine tract upstream of the 3' splice site and promotes binding of U2 snRNP to the pre-mRNA branchpoint. U2AF65 also plays an important role in the nuclear export of mRNA. It facilitates the formation of a messenger ribonucleoprotein export complex, containing both the NXF1 receptor and the RNA substrate. Moreover, U2AF65 interacts directly and specifically with expanded CAG RNA, and serves as an adaptor to link expanded CAG RNA to NXF1 for RNA export. U2AF65 contains an N-terminal RS domain rich in arginine and serine, followed by a proline-rich segment and three C-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The N-terminal RS domain stabilizes the interaction of U2 snRNP with the branch point (BP) by contacting the branch region, and further promotes base pair interactions between U2 snRNA and the BP. The proline-rich segment mediates protein-protein interactions with the RRM domain of the small U2AF subunit (U2AF35 or U2AF1). The RRM1 and RRM2 are sufficient for specific RNA binding, while RRM3 is responsible for protein-protein interactions. The family also includes Splicing factor U2AF 50 kDa subunit (dU2AF50), the Drosophila ortholog of U2AF65. dU2AF50 functions as an essential pre-mRNA splicing factor in flies. It associates with intronless mRNAs and plays a significant and unexpected role in the nuclear export of a large number of intronless mRNAs
ARRLYVGNIPPGITEEELMDFFNQAMRAAGLTQAPGNPVLAVQINPDKNFAFVEFRSVEETTAALALDGI
IFKGQPLKIRRP
>gnl|CDD|409678 cd12231, RRM2_U2AF65, RNA recognition motif 2 (RRM2) found in U2 large nuclear ribonucleoprotein auxiliary factor U2AF 65 kDa subunit (U2AF65) and similar proteins. This subfamily corresponds to the RRM2 of U2AF65 and dU2AF50. U2AF65, also termed U2AF2, is the large subunit of U2 small nuclear ribonucleoprotein (snRNP) auxiliary factor (U2AF), which has been implicated in the recruitment of U2 snRNP to pre-mRNAs and is a highly conserved heterodimer composed of large and small subunits. U2AF65 specifically recognizes the intron polypyrimidine tract upstream of the 3' splice site and promotes binding of U2 snRNP to the pre-mRNA branchpoint. U2AF65 also plays an important role in the nuclear export of mRNA. It facilitates the formation of a messenger ribonucleoprotein export complex, containing both the NXF1 receptor and the RNA substrate. Moreover, U2AF65 interacts directly and specifically with expanded CAG RNA, and serves as an adaptor to link expanded CAG RNA to NXF1 for RNA export. U2AF65 contains an N-terminal RS domain rich in arginine and serine, followed by a proline-rich segment and three C-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The N-terminal RS domain stabilizes the interaction of U2 snRNP with the branch point (BP) by contacting the branch region, and further promotes base pair interactions between U2 snRNA and the BP. The proline-rich segment mediates protein-protein interactions with the RRM domain of the small U2AF subunit (U2AF35 or U2AF1). The RRM1 and RRM2 are sufficient for specific RNA binding, while RRM3 is responsible for protein-protein interactions. The family also includes Splicing factor U2AF 50 kDa subunit (dU2AF50), the Drosophila ortholog of U2AF65. dU2AF50 functions as an essential pre-mRNA splicing factor in flies. It associates with intronless mRNAs and plays a significant and unexpected role in the nuclear export of a large number of intronless mRNAs
NKLFIGGLPNYLNEDQVKELLQSFGKLKAFNLVKDSATGLSKGYAFCEYVDDNVTDQAIAGLNGMQLGDK
KLLVQRA
>gnl|CDD|409679 cd12232, RRM3_U2AF65, RNA recognition motif 3 (RRM3) found in U2 large nuclear ribonucleoprotein auxiliary factor U2AF 65 kDa subunit (U2AF65) and similar proteins. This subfamily corresponds to the RRM3 of U2AF65 and dU2AF50. U2AF65, also termed U2AF2, is the large subunit of U2 small nuclear ribonucleoprotein (snRNP) auxiliary factor (U2AF), which has been implicated in the recruitment of U2 snRNP to pre-mRNAs and is a highly conserved heterodimer composed of large and small subunits. U2AF65 specifically recognizes the intron polypyrimidine tract upstream of the 3' splice site and promotes binding of U2 snRNP to the pre-mRNA branchpoint. U2AF65 also plays an important role in the nuclear export of mRNA. It facilitates the formation of a messenger ribonucleoprotein export complex, containing both the NXF1 receptor and the RNA substrate. Moreover, U2AF65 interacts directly and specifically with expanded CAG RNA, and serves as an adaptor to link expanded CAG RNA to NXF1 for RNA export. U2AF65 contains an N-terminal RS domain rich in arginine and serine, followed by a proline-rich segment and three C-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The N-terminal RS domain stabilizes the interaction of U2 snRNP with the branch point (BP) by contacting the branch region, and further promotes base pair interactions between U2 snRNA and the BP. The proline-rich segment mediates protein-protein interactions with the RRM domain of the small U2AF subunit (U2AF35 or U2AF1). The RRM1 and RRM2 are sufficient for specific RNA binding, while RRM3 is responsible for protein-protein interactions. The family also includes Splicing factor U2AF 50 kDa subunit (dU2AF50), the Drosophila ortholog of U2AF65. dU2AF50 functions as an essential pre-mRNA splicing factor in flies. It associates with intronless mRNAs and plays a significant and unexpected role in the nuclear export of a large number of intronless mRNAs
SRVLCLLNMVTPEELEDDEEYEEILEDVKEECSKYGKVLSVVIPRPEAEGVDVPGVGKVFVEFEDVEDAQ
KAQKALAGRKFDGRTVVAS
>gnl|CDD|240679 cd12233, RRM_Srp1p_AtRSp31_like, RNA recognition motif (RRM) found in fission yeast pre-mRNA-splicing factor Srp1p, Arabidopsis thaliana arginine/serine-rich-splicing factor RSp31 and similar proteins. This subfamily corresponds to the RRM of Srp1p and RRM2 of plant SR splicing factors. Srp1p is encoded by gene srp1 from fission yeast Schizosaccharomyces pombe. It plays a role in the pre-mRNA splicing process, but is not essential for growth. Srp1p is closely related to the SR protein family found in Metazoa. It contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a glycine hinge and a RS domain in the middle, and a C-terminal domain. The family also includes a novel group of arginine/serine (RS) or serine/arginine (SR) splicing factors existing in plants, such as A. thaliana RSp31, RSp35, RSp41 and similar proteins. Like vertebrate RS splicing factors, these proteins function as plant splicing factors and play crucial roles in constitutive and alternative splicing in plants. They all contain two RRMs at their N-terminus and an RS domain at their C-terminus
TLFVVGFDPGTTREEDIEKLFEPFGPLVRCDIRKTFAFVEFEDSEDATKALEALHGSRIDGSVLTVEFVK
>gnl|CDD|409680 cd12234, RRM1_AtRSp31_like, RNA recognition motif (RRM) found in Arabidopsis thaliana arginine/serine-rich-splicing factor RSp31 and similar proteins from plants. This subfamily corresponds to the RRM1in a family that represents a novel group of arginine/serine (RS) or serine/arginine (SR) splicing factors existing in plants, such as A. thaliana RSp31, RSp35, RSp41 and similar proteins. Like vertebrate RS splicing factors, these proteins function as plant splicing factors and play crucial roles in constitutive and alternative splicing in plants. They all contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), at their N-terminus, and an RS domain at their C-terminus
KPVFCGNFEYDARQSEIERLFGKYGRVDRVDMKSGYAFVYMEDERDAEDAIRGLDNFEFGRQRRRLRVEW
TK
>gnl|CDD|409681 cd12235, RRM_PPIL4, RNA recognition motif (RRM) found in peptidyl-prolyl cis-trans isomerase-like 4 (PPIase) and similar proteins. This subfamily corresponds to the RRM of PPIase, also termed cyclophilin-like protein PPIL4, or rotamase PPIL4, a novel nuclear RNA-binding protein encoded by cyclophilin-like PPIL4 gene. The precise role of PPIase remains unclear. PPIase contains a conserved N-terminal peptidyl-prolyl cistrans isomerase (PPIase) motif, a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a lysine rich domain, and a pair of bipartite nuclear targeting sequences (NLS) at the C-terminus
PPENVLFVCKLNPVTTDEDLEIIFSRFGKIKSCEVIRDKKTGDSLQYAFIEFETKESCEEAYFKMDNVLI
DDRRIHVDFSQSV
>gnl|CDD|409682 cd12236, RRM_snRNP70, RNA recognition motif (RRM) found in U1 small nuclear ribonucleoprotein 70 kDa (U1-70K) and similar proteins. This subfamily corresponds to the RRM of U1-70K, also termed snRNP70, a key component of the U1 snRNP complex, which is one of the key factors facilitating the splicing of pre-mRNA via interaction at the 5' splice site, and is involved in regulation of polyadenylation of some viral and cellular genes, enhancing or inhibiting efficient poly(A) site usage. U1-70K plays an essential role in targeting the U1 snRNP to the 5' splice site through protein-protein interactions with regulatory RNA-binding splicing factors, such as the RS protein ASF/SF2. Moreover, U1-70K protein can specifically bind to stem-loop I of the U1 small nuclear RNA (U1 snRNA) contained in the U1 snRNP complex. It also mediates the binding of U1C, another U1-specific protein, to the U1 snRNP complex. U1-70K contains a conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by an adjacent glycine-rich region at the N-terminal half, and two serine/arginine-rich (SR) domains at the C-terminal half. The RRM is responsible for the binding of stem-loop I of U1 snRNA molecule. Additionally, the most prominent immunodominant region that can be recognized by auto-antibodies from autoimmune patients may be located within the RRM. The SR domains are involved in protein-protein interaction with SR proteins that mediate 5' splice site recognition. For instance, the first SR domain is necessary and sufficient for ASF/SF2 Binding. The family also includes Drosophila U1-70K that is an essential splicing factor required for viability in flies, but its SR domain is dispensable. The yeast U1-70k doesn't contain easily recognizable SR domains and shows low sequence similarity in the RRM region with other U1-70k proteins and therefore not included in this family. The RRM domain is dispensable for yeast U1-70K function
FKTLFVARLSYDTTESKLRREFEKYGPIKRVRLVRDKKTGKSRGYAFIEFEHERDMKAAYKHADGKKIDG
RRVLVDVERGRTVKGWKPRRL
>gnl|CDD|409683 cd12237, RRM_snRNP35, RNA recognition motif (RRM) found in U11/U12 small nuclear ribonucleoprotein 35 kDa protein (U11/U12-35K) and similar proteins. This subfamily corresponds to the RRM of U11/U12-35K, also termed protein HM-1, or U1 snRNP-binding protein homolog, and is one of the components of the U11/U12 snRNP, which is a subunit of the minor (U12-dependent) spliceosome required for splicing U12-type nuclear pre-mRNA introns. U11/U12-35K is highly conserved among bilateria and plants, but lacks in some organisms, such as Saccharomyces cerevisiae and Caenorhabditis elegans. Moreover, U11/U12-35K shows significant sequence homology to U1 snRNP-specific 70 kDa protein (U1-70K or snRNP70). It contains a conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by an adjacent glycine-rich region, and Arg-Asp and Arg-Glu dipeptide repeats rich domain, making U11/U12-35K a possible functional analog of U1-70K. It may facilitate 5' splice site recognition in the minor spliceosome and play a role in exon bridging, interacting with components of the major spliceosome bound to the pyrimidine tract of an upstream U2-type intron. The family corresponds to the RRM of U11/U12-35K that may directly contact the U11 or U12 snRNA through the RRM domain
GDPRLTLFVGRLSLQTTEEKLKEVFSRYGDIRRLRLVRDIVTGFSKRYAFIEYKEERDALHAYRDAKKLV
IDQYEIFVDFECERTLPGWIPRRL
>gnl|CDD|409684 cd12238, RRM1_RBM40_like, RNA recognition motif 1 (RRM1) found in RNA-binding protein 40 (RBM40) and similar proteins. This subfamily corresponds to the RRM1 of RBM40, also known as RNA-binding region-containing protein 3 (RNPC3) or U11/U12 small nuclear ribonucleoprotein 65 kDa protein (U11/U12-65K protein), It serves as a bridging factor between the U11 and U12 snRNPs. It contains two repeats of RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), connected by a linker that includes a proline-rich region. It binds to the U11-associated 59K protein via its RRM1 and employs the RRM2 to bind hairpin III of the U12 small nuclear RNA (snRNA). The proline-rich region might be involved in protein-protein interactions
TLLVRHLPPELSEDDKEDLLKHFGATSVRVMKRRGKLKHTAFATFDNEQAASKALSRLHQLKILGKRLVV
EYA
>gnl|CDD|409685 cd12239, RRM2_RBM40_like, RNA recognition motif 2 (RRM2) found in RNA-binding protein 40 (RBM40) and similar proteins. This subfamily corresponds to the RRM2 of RBM40 and the RRM of RBM41. RBM40, also known as RNA-binding region-containing protein 3 (RNPC3) or U11/U12 small nuclear ribonucleoprotein 65 kDa protein (U11/U12-65K protein). It serves as a bridging factor between the U11 and U12 snRNPs. It contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), connected by a linker that includes a proline-rich region. It binds to the U11-associated 59K protein via its RRM1 and employs the RRM2 to bind hairpin III of the U12 small nuclear RNA (snRNA). The proline-rich region might be involved in protein-protein interactions. RBM41 contains only one RRM. Its biological function remains unclear
SNRLYVKNLSKRVSEKDLKYIFGRFVDSSSEEKNMFDIRLMTEGRMKGQAFITFPSEELAEKALNLTNGY
VLHGKPMVVQFA
>gnl|CDD|409686 cd12240, RRM_NCBP2, RNA recognition motif (RRM) found in nuclear cap-binding protein subunit 2 (CBP20) and similar proteins. This subfamily corresponds to the RRM of CBP20, also termed nuclear cap-binding protein subunit 2 (NCBP2), or cell proliferation-inducing gene 55 protein, or NCBP-interacting protein 1 (NIP1). CBP20 is the small subunit of the nuclear cap binding complex (CBC), which is a conserved eukaryotic heterodimeric protein complex binding to 5'-capped polymerase II transcripts and plays a central role in the maturation of pre-mRNA and uracil-rich small nuclear RNA (U snRNA). CBP20 is most likely responsible for the binding of capped RNA. It contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and interacts with the second and third domains of CBP80, the large subunit of CBC
LYVGNLSFYTTEEQIYELFSKCGDIKRIIMGLDKFKKTPCGFCFVEYYSREDAENAVKYLNGTKLDDRII
RVDWDAGF
>gnl|CDD|409687 cd12241, RRM_SF3B14, RNA recognition motif (RRM) found in pre-mRNA branch site protein p14 (SF3B14) and similar proteins. This subfamily corresponds to the RRM of SF3B14 (also termed p14), a 14 kDa protein subunit of SF3B which is a multiprotein complex that is an integral part of the U2 small nuclear ribonucleoprotein (snRNP) and the U11/U12 di-snRNP. SF3B is essential for the accurate excision of introns from pre-messenger RNA and has been involved in the recognition of the pre-mRNA's branch site within the major and minor spliceosomes. SF3B14 associates directly with another SF3B subunit called SF3B155. It is also present in both U2- and U12-dependent spliceosomes and may contribute to branch site positioning in both the major and minor spliceosome. Moreover, SF3B14 interacts directly with the pre-mRNA branch adenosine early in spliceosome assembly and within the fully assembled spliceosome. SF3B14 contains one well conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
VNRILYVRNLPYKISSEELYDLFGKYGAIRQIRIGNTKETRGTAFVVYEDIFDAKNACDHLSGFNVCNRY
LVVLYYQ
>gnl|CDD|409688 cd12242, RRM_SLIRP, RNA recognition motif (RRM) found in SRA stem-loop-interacting RNA-binding protein (SLIRP) and similar proteins. This subfamily corresponds to the RRM of SLIRP, a widely expressed small steroid receptor RNA activator (SRA) binding protein, which binds to STR7, a functional substructure of SRA. SLIRP is localized predominantly to the mitochondria and plays a key role in modulating several nuclear receptor (NR) pathways. It functions as a co-repressor to repress SRA-mediated nuclear receptor coactivation. It modulates SHARP- and SKIP-mediated co-regulation of NR activity. SLIRP contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), which is required for SLIRP's corepression activities
KLFVSNLPWTTGSSELKEYFSQFGKVKRCNLPFDKETGFHKGFGFVSFENEDGLRNALQKQKHIFEGNKV
SVQ
>gnl|CDD|409689 cd12243, RRM1_MSSP, RNA recognition motif 1 (RRM1) found in the c-myc gene single-strand binding proteins (MSSP) family. This subfamily corresponds to the RRM1 of c-myc gene single-strand binding proteins (MSSP) family, including single-stranded DNA-binding protein MSSP-1 (also termed RBMS1 or SCR2) and MSSP-2 (also termed RBMS2 or SCR3). All MSSP family members contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), both of which are responsible for the specific DNA binding activity. Both, MSSP-1 and -2, have been identified as protein factors binding to a putative DNA replication origin/transcriptional enhancer sequence present upstream from the human c-myc gene in both single- and double-stranded forms. Thus, they have been implied in regulating DNA replication, transcription, apoptosis induction, and cell-cycle movement, via the interaction with c-MYC, the product of protooncogene c-myc. Moreover, the family includes a new member termed RNA-binding motif, single-stranded-interacting protein 3 (RBMS3), which is not a transcriptional regulator. RBMS3 binds with high affinity to A/U-rich stretches of RNA, and to A/T-rich DNA sequences, and functions as a regulator of cytoplasmic activity. In addition, a putative meiosis-specific RNA-binding protein termed sporulation-specific protein 5 (SPO5, or meiotic RNA-binding protein 1, or meiotically up-regulated gene 12 protein), encoded by Schizosaccharomyces pombe Spo5/Mug12 gene, is also included in this family. SPO5 is a novel meiosis I regulator that may function in the vicinity of the Mei2 dot
TNVYIRGLPPNTTDEDLLLLCQSFGKIISTKAIIDKQTNKCKGYGFVDFDSPEAALKAIEGLNGRGVQAS
F
>gnl|CDD|409690 cd12244, RRM2_MSSP, RNA recognition motif 2 (RRM2) found in the c-myc gene single-strand binding proteins (MSSP) family. This subfamily corresponds to the RRM2 of c-myc gene single-strand binding proteins (MSSP) family, including single-stranded DNA-binding protein MSSP-1 (also termed RBMS1 or SCR2) and MSSP-2 (also termed RBMS2 or SCR3). All MSSP family members contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), both of which are responsible for the specific DNA binding activity. Both, MSSP-1 and -2, have been identified as protein factors binding to a putative DNA replication origin/transcriptional enhancer sequence present upstream from the human c-myc gene in both single- and double-stranded forms. Thus they have been implied in regulating DNA replication, transcription, apoptosis induction, and cell-cycle movement, via the interaction with C-MYC, the product of protooncogene c-myc. Moreover, they family includes a new member termed RNA-binding motif, single-stranded-interacting protein 3 (RBMS3), which is not a transcriptional regulator. RBMS3 binds with high affinity to A/U-rich stretches of RNA, and to A/T-rich DNA sequences, and functions as a regulator of cytoplasmic activity. In addition, a putative meiosis-specific RNA-binding protein termed sporulation-specific protein 5 (SPO5, or meiotic RNA-binding protein 1, or meiotically up-regulated gene 12 protein), encoded by Schizosaccharomyces pombe Spo5/Mug12 gene, is also included in this family. SPO5 is a novel meiosis I regulator that may function in the vicinity of the Mei2 dot
TNLYISNLPLDMDEQDLENMLKPFGQVISTRILRDSKGQSRGVGFARMESREKCEDVISKFNGKVLKTPS
ASGEPLLVKFAD
>gnl|CDD|409691 cd12245, RRM_scw1_like, RNA recognition motif (RRM) found in yeast cell wall integrity protein scw1 and similar proteins. This subfamily corresponds to the RRM of the family including yeast cell wall integrity protein scw1, yeast Whi3 protein, yeast Whi4 protein and similar proteins. The strong cell wall protein 1, scw1, is a nonessential cytoplasmic RNA-binding protein that regulates septation and cell-wall structure in fission yeast. It may function as an inhibitor of septum formation, such that its loss of function allows weak SIN signaling to promote septum formation. It's RRM domain shows high homology to two budding yeast proteins, Whi3 and Whi4. Whi3 is a dose-dependent modulator of cell size and has been implicated in cell cycle control in the yeast Saccharomyces cerevisiae. It functions as a negative regulator of ceroid-lipofuscinosis, neuronal 3 (Cln3), a G1 cyclin that promotes transcription of many genes to trigger the G1/S transition in budding yeast. It specifically binds the CLN3 mRNA and localizes it into discrete cytoplasmic loci that may locally restrict Cln3 synthesis to modulate cell cycle progression. Moreover, Whi3 plays a key role in cell fate determination in budding yeast. The RRM domain is essential for Whi3 function. Whi4 is a partially redundant homolog of Whi3, also containing one RRM. Some uncharacterized family members of this subfamily contain two RRMs; their RRM1 shows high sequence homology to the RRM of RNA-binding protein with multiple splicing (RBP-MS)-like proteins
PCNTLFVANLGPNVSEQELRQLFSRQPGFRRLRMHNKGGGPVCFVEFEDVPFATQALNHLQGAILSSSDR
GGIRIEYAK
>gnl|CDD|409692 cd12246, RRM1_U1A_like, RNA recognition motif 1 (RRM1) found in the U1A/U2B"/SNF protein family. This subfamily corresponds to the RRM1 of U1A/U2B"/SNF protein family which contains Drosophila sex determination protein SNF and its two mammalian counterparts, U1 small nuclear ribonucleoprotein A (U1 snRNP A or U1-A or U1A) and U2 small nuclear ribonucleoprotein B" (U2 snRNP B" or U2B"), all of which consist of two RNA recognition motifs (RRMs), connected by a variable, flexible linker. SNF is an RNA-binding protein found in the U1 and U2 snRNPs of Drosophila where it is essential in sex determination and possesses a novel dual RNA binding specificity. SNF binds with high affinity to both Drosophila U1 snRNA stem-loop II (SLII) and U2 snRNA stem-loop IV (SLIV). It can also bind to poly(U) RNA tracts flanking the alternatively spliced Sex-lethal (Sxl) exon, as does Drosophila Sex-lethal protein (SXL). U1A is an RNA-binding protein associated with the U1 snRNP, a small RNA-protein complex involved in pre-mRNA splicing. U1A binds with high affinity and specificity to stem-loop II (SLII) of U1 snRNA. It is predominantly a nuclear protein that shuttles between the nucleus and the cytoplasm independently of interactions with U1 snRNA. Moreover, U1A may be involved in RNA 3'-end processing, specifically cleavage, splicing and polyadenylation, through interacting with a large number of non-snRNP proteins. U2B", initially identified to bind to stem-loop IV (SLIV) at the 3' end of U2 snRNA, is a unique protein that comprises of the U2 snRNP. Additional research indicates U2B" binds to U1 snRNA stem-loop II (SLII) as well and shows no preference for SLIV or SLII on the basis of binding affinity. Moreover, U2B" does not require an auxiliary protein for binding to RNA, and its nuclear transport is independent of U2 snRNA binding
TLYINNLNEKIKKDELKRSLYALFSQFGPVLDIVASKSLKMRGQAFVVFKDVESATNALRALQGFPFYGK
PMRIQYAK
>gnl|CDD|409693 cd12247, RRM2_U1A_like, RNA recognition motif 2 (RRM2) found in the U1A/U2B"/SNF protein family. This subfamily corresponds to the RRM2 of U1A/U2B"/SNF protein family, containing Drosophila sex determination protein SNF and its two mammalian counterparts, U1 small nuclear ribonucleoprotein A (U1 snRNP A or U1-A or U1A) and U2 small nuclear ribonucleoprotein B" (U2 snRNP B" or U2B"), all of which consist of two RNA recognition motifs (RRMs) connected by a variable, flexible linker. SNF is an RNA-binding protein found in the U1 and U2 snRNPs of Drosophila where it is essential in sex determination and possesses a novel dual RNA binding specificity. SNF binds with high affinity to both Drosophila U1 snRNA stem-loop II (SLII) and U2 snRNA stem-loop IV (SLIV). It can also bind to poly(U) RNA tracts flanking the alternatively spliced Sex-lethal (Sxl) exon, as does Drosophila Sex-lethal protein (SXL). U1A is an RNA-binding protein associated with the U1 snRNP, a small RNA-protein complex involved in pre-mRNA splicing. U1A binds with high affinity and specificity to stem-loop II (SLII) of U1 snRNA. It is predominantly a nuclear protein that shuttles between the nucleus and the cytoplasm independently of interactions with U1 snRNA. Moreover, U1A may be involved in RNA 3'-end processing, specifically cleavage, splicing and polyadenylation, through interacting with a large number of non-snRNP proteins. U2B", initially identified to bind to stem-loop IV (SLIV) at the 3' end of U2 snRNA, is a unique protein that comprises of the U2 snRNP. Additional research indicates U2B" binds to U1 snRNA stem-loop II (SLII) as well and shows no preference for SLIV or SLII on the basis of binding affinity. U2B" does not require an auxiliary protein for binding to RNA and its nuclear transport is independent on U2 snRNA binding
PNKILFLQNLPEETTKEMLEMLFNQFPGFKEVRLVPRRGIAFVEFETEEQATVALQALQGFKITPGHAMK
IS
>gnl|CDD|409694 cd12248, RRM_RBM44, RNA recognition motif (RRM) found in RNA-binding protein 44 (RBM44) and similar proteins. This subgroup corresponds to the RRM of RBM44, a novel germ cell intercellular bridge protein that is localized in the cytoplasm and intercellular bridges from pachytene to secondary spermatocyte stages. RBM44 interacts with itself and testis-expressed gene 14 (TEX14). Unlike TEX14, RBM44 does not function in the formation of stable intercellular bridges. It carries an RNA recognition motif (RRM) that could potentially bind a multitude of RNA sequences in the cytoplasm and help to shuttle them through the intercellular bridge, facilitating their dispersion into the interconnected neighboring cells
CVYVHVGNLAPSVSEEDLLMHFEKYHVSKISIQKLSMNYRYASLTFDDASDAQAAVKEMNGKDISGRKVK
VRYVKES
>gnl|CDD|409695 cd12249, RRM1_hnRNPR_like, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein R (hnRNP R) and similar proteins. This subfamily corresponds to the RRM1 in hnRNP R, hnRNP Q, APOBEC-1 complementation factor (ACF), and dead end protein homolog 1 (DND1). hnRNP R is a ubiquitously expressed nuclear RNA-binding protein that specifically binds mRNAs with a preference for poly(U) stretches. It has been implicated in mRNA processing and mRNA transport, and also acts as a regulator to modify binding to ribosomes and RNA translation. hnRNP Q is also a ubiquitously expressed nuclear RNA-binding protein. It has been identified as a component of the spliceosome complex, as well as a component of the apobec-1 editosome, and has been implicated in the regulation of specific mRNA transport. ACF is an RNA-binding subunit of a core complex that interacts with apoB mRNA to facilitate C to U RNA editing. It may also act as an apoB mRNA recognition factor and chaperone, and play a key role in cell growth and differentiation. DND1 is essential for maintaining viable germ cells in vertebrates. It interacts with the 3'-untranslated region (3'-UTR) of multiple messenger RNAs (mRNAs) and prevents micro-RNA (miRNA) mediated repression of mRNA. This family also includes two functionally unknown RNA-binding proteins, RBM46 and RBM47. All members in this family, except for DND1, contain three conserved RNA recognition motifs (RRMs); DND1 harbors only two RRMs
GCEVFVGKIPRDVFEDELVPLFEKCGKIYELRLMMDFSGLNRGYAFVTYTNKEAAQRAVKTLNNYEIRPG
KLLGVCIS
>gnl|CDD|409696 cd12250, RRM2_hnRNPR_like, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein R (hnRNP R) and similar proteins. This subfamily corresponds to the RRM2 in hnRNP R, hnRNP Q, APOBEC-1 complementation factor (ACF), and dead end protein homolog 1 (DND1). hnRNP R is a ubiquitously expressed nuclear RNA-binding protein that specifically bind mRNAs with a preference for poly(U) stretches. It has been implicated in mRNA processing and mRNA transport, and also acts as a regulator to modify binding to ribosomes and RNA translation. hnRNP Q is also a ubiquitously expressed nuclear RNA-binding protein. It has been identified as a component of the spliceosome complex, as well as a component of the apobec-1 editosome, and has been implicated in the regulation of specific mRNA transport. ACF is an RNA-binding subunit of a core complex that interacts with apoB mRNA to facilitate C to U RNA editing. It may also act as an apoB mRNA recognition factor and chaperone and play a key role in cell growth and differentiation. DND1 is essential for maintaining viable germ cells in vertebrates. It interacts with the 3'-untranslated region (3'-UTR) of multiple messenger RNAs (mRNAs) and prevents micro-RNA (miRNA) mediated repression of mRNA. This family also includes two functionally unknown RNA-binding proteins, RBM46 and RBM47. All members in this family, except for DND1, contain three conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains); DND1 harbors only two RRMs
NNRLFVGGIPKTKTKEEILEEFSKVTEGVVDVIVYPSPDDKKKNRGFAFLEYESHKAAAIARRKLTPGRI
LLWGHDVAVDWA
>gnl|CDD|409697 cd12251, RRM3_hnRNPR_like, RNA recognition motif 3 (RRM3) found in heterogeneous nuclear ribonucleoprotein R (hnRNP R) and similar proteins. This subfamily corresponds to the RRM3 in hnRNP R, hnRNP Q, and APOBEC-1 complementation factor (ACF). hnRNP R is a ubiquitously expressed nuclear RNA-binding protein that specifically bind mRNAs with a preference for poly(U) stretches and has been implicated in mRNA processing and mRNA transport, and also acts as a regulator to modify binding to ribosomes and RNA translation. hnRNP Q is also a ubiquitously expressed nuclear RNA-binding protein. It has been identified as a component of the spliceosome complex, as well as a component of the apobec-1 editosome, and has been implicated in the regulation of specific mRNA transport. ACF is an RNA-binding subunit of a core complex that interacts with apoB mRNA to facilitate C to U RNA editing. It may also act as an apoB mRNA recognition factor and chaperone and play a key role in cell growth and differentiation. This family also includes two functionally unknown RNA-binding proteins, RBM46 and RBM47. All members contain three conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
VKVLYVRNLMLSTTEEKLRELFSEYGKVERVKKIKDYAFVHFEERDDAVKAMEEMNGKELEGSEIEVSLA
KP
>gnl|CDD|409698 cd12252, RRM_DbpA, RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases. This subfamily corresponds to the C-terminal RRM homology domain of dbpA proteins implicated in ribosome biogenesis. They bind with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92), which is part of the ribosomal A-site. The majority of dbpA proteins contain two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding. Several members of this family lack specificity for 23S rRNA. These proteins can generally be distinguished by a basic region that extends beyond the C-terminal domain
RLFINVGRKDGIDPRDLLGAICRAGGISRDDIGAIRIFDNFSFVEVPEAEAERVIEALNGKKIKGKKLRV
E
>gnl|CDD|240699 cd12253, RRM_PIN4_like, RNA recognition motif (RRM) found in yeast RNA-binding protein PIN4, fission yeast RNA-binding post-transcriptional regulators cip1, cip2 and similar proteins. This subfamily corresponds to the RRM in PIN4, also termed psi inducibility protein 4 or modifier of damage tolerance Mdt1, a novel phosphothreonine (pThr)-containing protein that specifically interacts with the pThr-binding site of the Rad53 FHA1 domain. It is encoded by gene MDT1 (YBL051C) from yeast Saccharomyces cerevisiae. PIN4 is involved in normal G2/M cell cycle progression in the absence of DNA damage and functions as a novel target of checkpoint-dependent cell cycle arrest pathways. It contains an N-terminal RRM, a nuclear localization signal, a coiled coil, and a total of 15 SQ/TQ motifs. cip1 (Csx1-interacting protein 1) and cip2 (Csx1-interacting protein 2) are novel cytoplasmic RRM-containing proteins that counteract Csx1 function during oxidative stress. They are not essential for viability in fission yeast Schizosaccharomyces pombe. Both cip1 and cip2 contain one RRM. Like PIN4, Cip2 also possesses an R3H motif that may function in sequence-specific binding to single-stranded nucleic acids
PTAIVIKNIPFSLRKEQLLDIIEDLGIPLPYAFNYHFDNGVFRGLAFANFRSPEEAQTVVEALNGYEISG
RRLRVEYKR
>gnl|CDD|409699 cd12254, RRM_hnRNPH_ESRPs_RBM12_like, RNA recognition motif (RRM) found in heterogeneous nuclear ribonucleoprotein (hnRNP) H protein family, epithelial splicing regulatory proteins (ESRPs), Drosophila RNA-binding protein Fusilli, RNA-binding protein 12 (RBM12) and similar proteins. The family includes RRM domains in the hnRNP H protein family, G-rich sequence factor 1 (GRSF-1), ESRPs (also termed RBM35), Drosophila Fusilli, RBM12 (also termed SWAN), RBM12B, RBM19 (also termed RBD-1) and similar proteins. The hnRNP H protein family includes hnRNP H (also termed mcs94-1), hnRNP H2 (also termed FTP-3 or hnRNP H'), hnRNP F and hnRNP H3 (also termed hnRNP 2H9), which represent a group of nuclear RNA binding proteins that are involved in pre-mRNA processing. GRSF-1 is a cytoplasmic poly(A)+ mRNA binding protein which interacts with RNA in a G-rich element-dependent manner. It may function in RNA packaging, stabilization of RNA secondary structure, or other macromolecular interactions. ESRP1 (also termed RBM35A) and ESRP2 (also termed RBM35B) are epithelial-specific RNA binding proteins that promote splicing of the epithelial variant of fibroblast growth factor receptor 2 (FGFR2), ENAH (also termed hMena), CD44 and CTNND1 (also termed p120-Catenin) transcripts. Fusilli shows high sequence homology to ESRPs. It can regulate endogenous FGFR2 splicing and functions as a splicing factor. The biological roles of both, RBM12 and RBM12B, remain unclear. RBM19 is a nucleolar protein conserved in eukaryotes. It is involved in ribosome biogenesis by processing rRNA. In addition, it is essential for preimplantation development. Members in this family contain 2~6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
VVRLRGLPFSATEEDIRDFFSGLDIPPDGIHIVYDDDGRPTGEAYVEFASEEDAQRALRRHKGKMGGRYI
EVF
>gnl|CDD|409700 cd12255, RRM1_LKAP, RNA recognition motif 1 (RRM1) found in Limkain-b1 (LKAP) and similar proteins. This subfamily corresponds to the RRM1 of LKAP, a novel peroxisomal autoantigen that co-localizes with a subset of cytoplasmic microbodies marked by ABCD3 (ATP-binding cassette subfamily D member 3, known previously as PMP-70) and/or PXF (peroxisomal farnesylated protein, known previously as PEX19). It associates with LIM kinase 2 (LIMK2) and may serve as a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. LKAP contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). However, whether those RRMs are bona fide RNA binding sites remains unclear. Moreover, there is no evidence of LAKP localization in the nucleus. Therefore, if the RRMs are functional, their interaction with RNA species would be restricted to the cytoplasm and peroxisomes
CHTLLYVYNLPTNRDVKSIRNRLRQLSDNCGGKVLSVSGGSAILRFANQESAERAQKRMEGEDVFGNKIS
VSF
>gnl|CDD|409701 cd12256, RRM2_LKAP, RNA recognition motif 2 (RRM2) found in Limkain-b1 (LKAP) and similar proteins. This subfamily corresponds to the RRM2 of LKAP, a novel peroxisomal autoantigen that co-localizes with a subset of cytoplasmic microbodies marked by ABCD3 (ATP-binding cassette subfamily D member 3, known previously as PMP-70) and/or PXF (peroxisomal farnesylated protein, known previously as PEX19). It associates with LIM kinase 2 (LIMK2) and may serve as a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. LKAP contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). However, whether those RRMs are bona fide RNA binding sites remains unclear. Moreover, there is no evidence of LAKP localization in the nucleus. Therefore, if the RRMs are functional, their interaction with RNA species would be restricted to the cytoplasm and peroxisomes
FSNGVDLQVSNLDYRMSRKELQQMLHNQFKRHGKVKSVELSPQTDGSLKASVRVPSLQDAQYAVSQLHRY
KIGSKRIQVSLATGSSNKS
>gnl|CDD|409702 cd12257, RRM1_RBM26_like, RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding protein 26 (RBM26) and similar proteins. This subfamily corresponds to the RRM1 of RBM26, and the RRM of RBM27. RBM26, also known as cutaneous T-cell lymphoma (CTCL) tumor antigen se70-2, represents a cutaneous lymphoma (CL)-associated antigen. It contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The RRMs may play some functional roles in RNA-binding or protein-protein interactions. RBM27 contains only one RRM; its biological function remains unclear
KTTLEVRNIPPELNNITKLREHFSKFGTIVNIQVNYNPESALVQFSTSEEANKAYRSPEAVFNNRFIKVF
WH
>gnl|CDD|409703 cd12258, RRM2_RBM26_like, RNA recognition motif 2 (RRM2) found in vertebrate RNA-binding protein 26 (RBM26) and similar proteins. This subfamily corresponds to the RRM2 of RBM26, also known as cutaneous T-cell lymphoma (CTCL) tumor antigen se70-2, which represents a cutaneous lymphoma (CL)-associated antigen. RBM26 contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The RRMs may play some functional roles in RNA-binding or protein-protein interactions
VDRRPRQLEVTGFTESDKDDLLPHFAQFGEVEDVQVDEEGLHLIITFKTRKEAEIAAVHGARFKGQSLQL
AW
>gnl|CDD|409704 cd12259, RRM_SRSF11_SREK1, RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 11 (SRSF11), splicing regulatory glutamine/lysine-rich protein 1 (SREK1) and similar proteins. This subfamily corresponds to the RRM domain of SRSF11 (SRp54 or p54), SREK1 (SFRS12 or SRrp86) and similar proteins, a group of proteins containing regions rich in serine-arginine dipeptides (SR protein family). These are involved in bridge-complex formation and splicing by mediating protein-protein interactions across either introns or exons. SR proteins have been identified as crucial regulators of alternative splicing. Different SR proteins display different substrate specificity, have distinct functions in alternative splicing of different pre-mRNAs, and can even negatively regulate splicing. All SR family members are characterized by the presence of one or two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and the C-terminal regions rich in serine and arginine dipeptides (SR domains). The RRM domain is responsible for RNA binding and specificity in both alternative and constitutive splicing. In contrast, SR domains are thought to be protein-protein interaction domains that are often interchangeable
VVQVTNVSPQATEEQMRTLFGFIGKIEELRLYPSEDDLAPVLSKVCFVKYEDPEDVAVALHLTNTVFIDR
ALIVIP
>gnl|CDD|409705 cd12260, RRM2_SREK1, RNA recognition motif 2 (RRM2) found in splicing regulatory glutamine/lysine-rich protein 1 (SREK1) and similar proteins. This subfamily corresponds to the RRM2 of SREK1, also termed serine/arginine-rich-splicing regulatory protein 86-kDa (SRrp86), or splicing factor arginine/serine-rich 12 (SFRS12), or splicing regulatory protein 508 amino acid (SRrp508). SREK1 belongs to a family of proteins containing regions rich in serine-arginine dipeptides (SR proteins family), which is involved in bridge-complex formation and splicing by mediating protein-protein interactions across either introns or exons. It is a unique SR family member and it may play a crucial role in determining tissue specific patterns of alternative splicing. SREK1 can alter splice site selection by both positively and negatively modulating the activity of other SR proteins. For instance, SREK1 can activate SRp20 and repress SC35 in a dose-dependent manner both in vitro and in vivo. In addition, SREK1 contains two (some contain only one) RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and two serine-arginine (SR)-rich domains (SR domains) separated by an unusual glutamic acid-lysine (EK) rich region. The RRM and SR domains are highly conserved among other members of the SR superfamily. However, the EK domain is unique to SREK1. It plays a modulatory role controlling SR domain function by involvement in the inhibition of both constitutive and alternative splicing and in the selection of splice-site
EEIRRTVYVGNLDPSTTADQLLEFFSQAGEVKYVRMAGDETQPTRYAFVEFAEQTSVINALKLNGKMFGG
RPLKVNHSNNAIVKP
>gnl|CDD|240707 cd12261, RRM1_3_MRN1, RNA recognition motif 1 (RRM1) and 3 (RRM3) found in RNA-binding protein MRN1 and similar proteins. This subfamily corresponds to the RRM1 and RRM3 of MRN1, also termed multicopy suppressor of RSC-NHP6 synthetic lethality protein 1, or post-transcriptional regulator of 69 kDa, which is an RNA-binding protein found in yeast. Although its specific biological role remains unclear, MRN1 might be involved in translational regulation. Members in this family contain four copies of conserved RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
RTVYLGNLPEDTTIRDILSAIRGGPLESIKLLPTKNSATVSFLDEAAAEAFYAYARNNGFYINGKRIKVG
WGK
>gnl|CDD|409706 cd12262, RRM2_4_MRN1, RNA recognition motif 2 (RRM2) and 4 (RRM4) found in RNA-binding protein MRN1 and similar proteins. This subgroup corresponds to the RRM2 and RRM4 of MRN1, also termed multicopy suppressor of RSC-NHP6 synthetic lethality protein 1, or post-transcriptional regulator of 69 kDa, and is an RNA-binding protein found in yeast. Although its specific biological role remains unclear, MRN1 might be involved in translational regulation. Members in this family contain four copies of conserved RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
GASRNVYVGNLDDSLTEEEIRGILEKYGEIESIKILKEKNCAFVNYLNIANAIKAVQELPIKNPKFKKVR
INYGKDRC
>gnl|CDD|409707 cd12263, RRM_ABT1_like, RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar proteins. This subfamily corresponds to the RRM of novel nuclear proteins termed ABT1 and its homologous counterpart, pre-rRNA-processing protein ESF2 (eighteen S factor 2), from yeast. ABT1 associates with the TATA-binding protein (TBP) and enhances basal transcription activity of class II promoters. Meanwhile, ABT1 could be a transcription cofactor that can bind to DNA in a sequence-independent manner. The yeast ABT1 homolog, ESF2, is a component of 90S preribosomes and 5' ETS-based RNPs. It is previously identified as a putative partner of the TATA-element binding protein. However, it is primarily localized to the nucleolus and physically associates with pre-rRNA processing factors. ESF2 may play a role in ribosome biogenesis. It is required for normal pre-rRNA processing, as well as for SSU processome assembly and function. Both ABT1 and ESF2 contain an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
GIVYLSRIPPGMNPAKLRQLLSQYGEVGRIYLQPEDPSKRKKRKKKGGNKKKKFTEGWVEFEDKKVAKRV
AESLNNTPIGGKKRSRFRDDLWNIKYLP
>gnl|CDD|409708 cd12264, RRM_AKAP17A, RNA recognition motif (RRM) found in A-kinase anchor protein 17A (AKAP-17A) and similar proteins. This subfamily corresponds to the RRM domain of AKAP-17A, also termed 721P, or splicing factor, arginine/serine-rich 17A (SFRS17A). It was originally reported as the pseudoautosomal or X inactivation escape gene 7 (XE7) and as B-lymphocyte antigen precursor. It has been suggested that AKAP-17A is an alternative splicing factor and an SR-related splicing protein that interacts with the classical SR protein ASF/SF2 and the SR-related factor ZNF265. Additional studies have indicated that AKAP-17A is a dual-specific protein kinase A anchoring protein (AKAP) that can bind both type I and type II protein kinase A (PKA) with high affinity and co-localizes with the catalytic subunit of PKA in nuclear speckles as well as the splicing factor SC35 in splicing factor compartments. It is involved in regulation of pre-mRNA splicing possibly by docking a pool of PKA in splicing factor compartments. AKAP-17A contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
GERPDTIHLEGLPCKWFAVPRSSDKPSENVLRKVFEKFGKIRNVDIPMLDPYRKEMDGNGFDTFSFGGHL
HFEAYVQYEEYDGFVKAMDALRGMKLMYKGEDGKALAANIKVDFDKTKHLSE
>gnl|CDD|409709 cd12265, RRM_SLT11, RNA recognition motif (RRM) found in pre-mRNA-splicing factor SLT11 and similar proteins. This subfamily corresponds to the RRM of SLT11, also known as extracellular mutant protein 2, or synthetic lethality with U2 protein 11, and is a splicing factor required for spliceosome assembly in yeast. It contains a conserved RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain). SLT11 can facilitate the cooperative formation of U2/U6 helix II in association with stem II in the yeast spliceosome by utilizing its RNA-annealing and -binding activities
SIKSFFLFGIDDDLPEWKISDYFEQFGKLKSLVVSHRAKCGFVRFETRELAEAFAAAISENGLNAGLSRG
GLLVIEGRPLRVAWGK
>gnl|CDD|409710 cd12266, RRM_like_XS, RNA recognition motif (RRM)-like XS domain found in plants. This XS (named after rice gene X and SGS3) domain is a single-stranded RNA-binding domain (RBD) and possesses a unique version of a RNA recognition motif (RRM) fold. It is conserved in a family of plant proteins including gene X and SGS3. Although its function is still unknown, the plant SGS3 proteins are thought to be involved in post-transcriptional gene silencing (PTGS) pathways. In addition, they contain a conserved aspartate residue that may be functionally important
IVWPWMGIVVNTPTTKDDNRKMEGGSNKELLERLIKFGPTRVKPLWNPQGHTGTAIVKFNSDWNGFRNAL
RFEKAFEVDGHGKKDWRNKKGGRKSKLYGWLARADDY
>gnl|CDD|409711 cd12267, RRM_YRA1_MLO3, RNA recognition motif (RRM) found in yeast RNA annealing protein YRA1 (Yra1p), yeast mRNA export protein mlo3 and similar proteins. This subfamily corresponds to the RRM of Yra1p and mlo3. Yra1p is an essential nuclear RNA-binding protein encoded by Saccharomyces cerevisiae YRA1 gene. It belongs to the evolutionarily conserved REF (RNA and export factor binding proteins) family of hnRNP-like proteins. Yra1p possesses potent RNA annealing activity and interacts with a number of proteins involved in nuclear transport and RNA processing. It binds to the mRNA export factor Mex67p/TAP and couples transcription to export in yeast. Yra1p is associated with Pse1p and Kap123p, two members of the beta-importin family, further mediating transport of Yra1p into the nucleus. In addition, the co-transcriptional loading of Yra1p is required for autoregulation. Yra1p consists of two highly conserved N- and C-terminal boxes and a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). This subfamily includes RNA-annealing protein mlo3, also termed mRNA export protein mlo3, which has been identified in fission yeast as a protein that causes defects in chromosome segregation when overexpressed. It shows high sequence similarity with Yra1p
SKVIVSNLPKDVTEAQIREYFVSQIGPIKRVLLSYNEGGKSTGIANITFKRAGDATKAYDKFNGRLDDGN
RKMKVEVV
>gnl|CDD|240714 cd12268, RRM_Vip1, RNA recognition motif (RRM) found in fission yeast protein Vip1 and similar proteins. This subfamily corresponds to Vip1, an RNA-binding protein encoded by gene vip1 from fission yeast Schizosaccharomyces pombe. Its biological role remains unclear. Vip1 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
VYVSNISPKTTEKQISDFFSFCGKISNLDLTNDGESQTATITFEKPSAAKTALLLDNALLGGKVIQVT
>gnl|CDD|409712 cd12269, RRM_Vip1_like, RNA recognition motif (RRM) found in a group of uncharacterized plant proteins similar to fission yeast Vip1. This subfamily corresponds to the Vip1-like, uncharacterized proteins found in plants. Although their biological roles remain unclear, these proteins show high sequence similarity to the fission yeast Vip1. Like Vip1 protein, members in this family contain an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
VEVTNVSPLATERDLHEFFSFSGDIEHIEIQREGEQSRIAFVTFKDPYALETAVLLSGATIVDQRVTIT
>gnl|CDD|409713 cd12270, RRM_MTHFSD, RNA recognition motif (RRM) found in vertebrate methenyltetrahydrofolate synthetase domain-containing proteins. This subfamily corresponds to methenyltetrahydrofolate synthetase domain (MTHFSD), a putative RNA-binding protein found in various vertebrate species. It contains an N-terminal 5-formyltetrahydrofolate cyclo-ligase domain and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The biological role of MTHFSD remains unclear
TVYVGNIPRSVRVSDLKSALRERGINPLRITWQGARGKAFLHYSDMADADSAVSSLQGLRIGGNTLTVEL
AK
>gnl|CDD|409714 cd12271, RRM1_PHIP1, RNA recognition motif 1 (RRM1) found in Arabidopsis thaliana phragmoplastin interacting protein 1 (PHIP1) and similar proteins. This subfamily corresponds to the RRM1 of PHIP1. A. thaliana PHIP1 and its homologs represent a novel class of plant-specific RNA-binding proteins that may play a unique role in the polarized mRNA transport to the vicinity of the cell plate. The family members consist of multiple functional domains, including a lysine-rich domain (KRD domain) that contains three nuclear localization motifs (KKKR/NK), two RNA recognition motifs (RRMs), and three CCHC-type zinc fingers. PHIP1 is a peripheral membrane protein and is localized at the cell plate during cytokinesis in plants. In addition to phragmoplastin, PHIP1 interacts with two Arabidopsis small GTP-binding proteins, Rop1 and Ran2. However, PHIP1 interacted only with the GTP-bound form of Rop1 but not the GDP-bound form. It also binds specifically to Ran2 mRNA
VYVGGIPYYSTEAEIRSYFSSCGEVRSVDLMRFPDSGNFRGIAFITFKTEEAAKRALALDGEMLGNRFLK
VE
>gnl|CDD|409715 cd12272, RRM2_PHIP1, RNA recognition motif 2 (RRM2) found in Arabidopsis thaliana phragmoplastin interacting protein 1 (PHIP1) and similar proteins. The CD corresponds to the RRM2 of PHIP1. A. thaliana PHIP1 and its homologs represent a novel class of plant-specific RNA-binding proteins that may play a unique role in the polarized mRNA transport to the vicinity of the cell plate. The family members consist of multiple functional domains, including a lysine-rich domain (KRD domain) that contains three nuclear localization motifs (KKKR/NK), two RNA recognition motifs (RRMs), and three CCHC-type zinc fingers. PHIP1 is a peripheral membrane protein and is localized at the cell plate during cytokinesis in plants. In addition to phragmoplastin, PHIP1 interacts with two Arabidopsis small GTP-binding proteins, Rop1 and Ran2. However, PHIP1 interacted only with the GTP-bound form of Rop1 but not the GDP-bound form. It also binds specifically to Ran2 mRNA
TVYIGNLAWDIDEDDLRELFAECCEITNVRLHTDKETGEFKGYGHVEFADEESLDAALKLAGTKLCGRPI
RVD
>gnl|CDD|409716 cd12273, RRM1_NEFsp, RNA recognition motif 1 (RRM1) found in vertebrate putative RNA exonuclease NEF-sp. This subfamily corresponds to the RRM1 of NEF-sp., including uncharacterized putative RNA exonuclease NEF-sp found in vertebrates. Although its cellular functions remains unclear, NEF-sp contains an exonuclease domain and two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), suggesting it may possess both exonuclease and RNA-binding activities
TVYAGPFEKSFCLKSVKRLFRSCGPVQSLTVVTETYQPYVCVQYEVLEAAQLAVETLDGALVDGHCIKVQ
R
>gnl|CDD|409717 cd12274, RRM2_NEFsp, RNA recognition motif 2 (RRM2) found in vertebrate putative RNA exonuclease NEF-sp. This subfamily corresponds to the RRM2 of NEF-sp., including uncharacterized putative RNA exonuclease NEF-sp found in vertebrates. Although its cellular functions remains unclear, NEF-sp contains an exonuclease domain and two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), suggesting it may possess both exonuclease and RNA-binding activities
IYVSGFKKSLTEEDLQERFSQLSDLEAVFLPKDLQSGKHKKYCFLKFRSSQSAQAALDIITGEWKLKGRR
A
>gnl|CDD|240721 cd12275, RRM1_MEI2_EAR1_like, RNA recognition motif 1 (RRM1) found in Mei2-like proteins and terminal EAR1-like proteins. This subfamily corresponds to the RRM1 of Mei2-like proteins from plant and fungi, terminal EAR1-like proteins from plant, and other eukaryotic homologs. Mei2-like proteins represent an ancient eukaryotic RNA-binding protein family whose corresponding Mei2-like genes appear to have arisen early in eukaryote evolution, been lost from some lineages such as Saccharomyces cerevisiae and metazoans, and diversified in the plant lineage. The plant Mei2-like genes may function in cell fate specification during development, rather than as stimulators of meiosis. In the fission yeast Schizosaccharomyces pombe, the Mei2 protein is an essential component of the switch from mitotic to meiotic growth. S. pombe Mei2 stimulates meiosis in the nucleus upon binding a specific non-coding RNA. The terminal EAR1-like protein 1 and 2 (TEL1 and TEL2) are mainly found in land plants. They may play a role in the regulation of leaf initiation. All members in this family are putative RNA-binding proteins carrying three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). In addition to the RRMs, the terminal EAR1-like proteins also contain TEL characteristic motifs that allow sequence and putative functional discrimination between them and Mei2-like proteins
SRSLFVINVPRDVTESTLRRLFEVYGDVRGVQTERISEGIVTVHFYDIRDAKRAVRELCGRHMQQQALGG
S
>gnl|CDD|409718 cd12276, RRM2_MEI2_EAR1_like, RNA recognition motif 2 (RRM2) found in Mei2-like proteins and terminal EAR1-like proteins. This subfamily corresponds to the RRM2 of Mei2-like proteins from plant and fungi, terminal EAR1-like proteins from plant, and other eukaryotic homologs. Mei2-like proteins represent an ancient eukaryotic RNA-binding proteins family whose corresponding Mei2-like genes appear to have arisen early in eukaryote evolution, been lost from some lineages such as Saccharomyces cerevisiae and metazoans, and diversified in the plant lineage. The plant Mei2-like genes may function in cell fate specification during development, rather than as stimulators of meiosis. In the fission yeast Schizosaccharomyces pombe, the Mei2 protein is an essential component of the switch from mitotic to meiotic growth. S. pombe Mei2 stimulates meiosis in the nucleus upon binding a specific non-coding RNA. The terminal EAR1-like protein 1 and 2 (TEL1 and TEL2) are mainly found in land plants. They may play a role in the regulation of leaf initiation. All members in this family are putative RNA-binding proteins carrying three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). In addition to the RRMs, the terminal EAR1-like proteins also contain TEL characteristic motifs that allow sequence and putative functional discrimination between them and Mei2-like proteins
QGTLLVFNLDAPVSNDELKSLFSKFGEIKEIRPTPDKPSQKFVEFYDVRDAEAALDGLNGRELLGGKLKV
A
>gnl|CDD|409719 cd12277, RRM3_MEI2_EAR1_like, RNA recognition motif 3 (RRM3) found in Mei2-like proteins and terminal EAR1-like proteins. This subfamily corresponds to the RRM3 of Mei2-like proteins from plant and fungi, terminal EAR1-like proteins from plant, and other eukaryotic homologs. Mei2-like proteins represent an ancient eukaryotic RNA-binding proteins family whose corresponding Mei2-like genes appear to have arisen early in eukaryote evolution, been lost from some lineages such as Saccharomyces cerevisiae and metazoans, and diversified in the plant lineage. The plant Mei2-like genes may function in cell fate specification during development, rather than as stimulators of meiosis. In the fission yeast Schizosaccharomyces pombe, the Mei2 protein is an essential component of the switch from mitotic to meiotic growth. S. pombe Mei2 stimulates meiosis in the nucleus upon binding a specific non-coding RNA. The terminal EAR1-like protein 1 and 2 (TEL1 and TEL2) are mainly found in land plants. They may play a role in the regulation of leaf initiation. All members in this family are putative RNA-binding proteins carrying three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). In addition to the RRMs, the terminal EAR1-like proteins also contain TEL characteristic motifs that allow sequence and putative functional discrimination between them and Mei2-like proteins
VMLRNIPNKYTQEMLLQEIDEHGKGGAYDFFYLPLDFKTKCNVGYAFINFINPEAAERFYKAFNGKKWKN
FPSKKVCDISYARLQG
>gnl|CDD|409720 cd12278, RRM_eIF3B, RNA recognition motif (RRM) found in eukaryotic translation initiation factor 3 subunit B (eIF-3B) and similar proteins. This subfamily corresponds to the RRM domain in eukaryotic translation initiation factor 3 (eIF-3), a large multisubunit complex that plays a central role in the initiation of translation by binding to the 40 S ribosomal subunit and promoting the binding of methionyl-tRNAi and mRNA. eIF-3B, also termed eIF-3 subunit 9, or Prt1 homolog, eIF-3-eta, eIF-3 p110, or eIF-3 p116, is the major scaffolding subunit of eIF-3. It interacts with eIF-3 subunits A, G, I, and J. eIF-3B contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), which is involved in the interaction with eIF-3J. The interaction between eIF-3B and eIF-3J is crucial for the eIF-3 recruitment to the 40 S ribosomal subunit. eIF-3B also binds directly to domain III of the internal ribosome-entry site (IRES) element of hepatitis-C virus (HCV) RNA through its N-terminal RRM, which may play a critical role in both cap-dependent and cap-independent translation. Additional research has shown that eIF-3B may function as an oncogene in glioma cells and can be served as a potential therapeutic target for anti-glioma therapy. This family also includes the yeast homolog of eIF-3 subunit B (eIF-3B, also termed PRT1 or eIF-3 p90) that interacts with the yeast homologs of eIF-3 subunits A(TIF32), G(TIF35), I(TIF34), J(HCR1), and E(Pci8). In yeast, eIF-3B (PRT1) contains an N-terminal RRM that is directly involved in the interaction with eIF-3A (TIF32) and eIF-3J (HCR1). In contrast to its human homolog, yeast eIF-3B (PRT1) may have potential to bind its total RNA through its RRM domain
DSVVVVDGLPVVGEEKLEKLKKVLTKIFSKFGSGKIVGIYMPVDETGKTKGFAFVEYATPEEAKKAVKAL
NGYKLDKKHTFAVN
>gnl|CDD|409721 cd12279, RRM_TUT1, RNA recognition motif (RRM) found in speckle targeted PIP5K1A-regulated poly(A) polymerase (Star-PAP) and similar proteins. This subfamily corresponds to the RRM of Star-PAP, also termed RNA-binding motif protein 21 (RBM21), which is a ubiquitously expressed U6 snRNA-specific terminal uridylyltransferase (U6-TUTase) essential for cell proliferation. Although it belongs to the well-characterized poly(A) polymerase protein superfamily, Star-PAP is highly divergent from both, the poly(A) polymerase (PAP) and the terminal uridylyl transferase (TUTase), identified within the editing complexes of trypanosomes. Star-PAP predominantly localizes at nuclear speckles and catalyzes RNA-modifying nucleotidyl transferase reactions. It functions in mRNA biosynthesis and may be regulated by phosphoinositides. It binds to glutathione S-transferase (GST)-PIPKIalpha. Star-PAP preferentially uses ATP as a nucleotide substrate and possesses PAP activity that is stimulated by PtdIns4,5P2. It contains an N-terminal C2H2-type zinc finger motif followed by an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a split PAP domain linked by a proline-rich region, a PAP catalytic and core domain, a PAP-associated domain, an RS repeat, and a nuclear localization signal (NLS)
EERSVFVSGFKRGTSELELSDYFQAFGPVASVVMDKDKGVYAIVEMDSTETVEKVLSQPQHCLNGQRLRV
KPRE
>gnl|CDD|409722 cd12280, RRM_FET, RNA recognition motif (RRM) found in the FET family of RNA-binding proteins. This subfamily corresponds to the RRM of FET (previously TET) (FUS/TLS, EWS, TAF15) family of RNA-binding proteins. This ubiquitously expressed family of similarly structured proteins predominantly localizing to the nuclear, includes FUS (also known as TLS or Pigpen or hnRNP P2), EWS (also known as EWSR1), TAF15 (also known as hTAFII68 or TAF2N or RPB56), and Drosophila Cabeza (also known as SARFH). The corresponding coding genes of these proteins are involved in deleterious genomic rearrangements with transcription factor genes in a variety of human sarcomas and acute leukemias. All FET proteins interact with each other and are therefore likely to be part of the very same protein complexes, which suggests a general bridging role for FET proteins coupling RNA transcription, processing, transport, and DNA repair. The FET proteins contain multiple copies of a degenerate hexapeptide repeat motif at the N-terminus. The C-terminal region consists of a conserved nuclear import and retention signal (C-NLS), a putative zinc-finger domain, and a conserved RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), which is flanked by 3 arginine-glycine-glycine (RGG) boxes. FUS and EWS might have similar sequence specificity; both bind preferentially to GGUG-containing RNAs. FUS has also been shown to bind strongly to human telomeric RNA and to small low-copy-number RNAs tethered to the promoter of cyclin D1. To date, nothing is known about the RNA binding specificity of TAF15
IFVSGLPPDVTIDELADLFGQIGIIKRYKDTWPPKIKIYTDKETGKPKGEATLTYEDPSAAKAAIEWFNG
KEFRGNKIKVSL
>gnl|CDD|409723 cd12281, RRM1_TatSF1_like, RNA recognition motif 1 (RRM1) found in HIV Tat-specific factor 1 (Tat-SF1) and similar proteins. This subfamily corresponds to the RRM1 of Tat-SF1 and CUS2. Tat-SF1 is the cofactor for stimulation of transcriptional elongation by human immunodeficiency virus-type 1 (HIV-1) Tat. It is a substrate of an associated cellular kinase. Tat-SF1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a highly acidic carboxyl-terminal half. The family also includes CUS2, a yeast homolog of human Tat-SF1. CUS2 interacts with U2 RNA in splicing extracts and functions as a splicing factor that aids assembly of the splicing-competent U2 snRNP in vivo. CUS2 also associates with PRP11 that is a subunit of the conserved splicing factor SF3a. Like Tat-SF1, CUS2 contains two RRMs as well
NTNVYVSGLPLDITVEEFVELFSKCGIIMEDPETGEPKIKLYRDENGNLKGDALCCYLKEESVELALQLL
DGTEIGRGYKIHVERAKFELKG
>gnl|CDD|409724 cd12282, RRM2_TatSF1_like, RNA recognition motif 2 (RRM2) found in HIV Tat-specific factor 1 (Tat-SF1) and similar proteins. This subfamily corresponds to the RRM2 of Tat-SF1 and CUS2. Tat-SF1 is the cofactor for stimulation of transcriptional elongation by human immunodeficiency virus-type 1 (HIV-1) Tat. It is a substrate of an associated cellular kinase. Tat-SF1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a highly acidic carboxyl-terminal half. The family also includes CUS2, a yeast homolog of human Tat-SF1. CUS2 interacts with U2 RNA in splicing extracts and functions as a splicing factor that aids assembly of the splicing-competent U2 snRNP in vivo. CUS2 also associates with PRP11 that is a subunit of the conserved splicing factor SF3a. Like Tat-SF1, CUS2 contains two RRMs as well
EKVVILKNMFHPKEFEEDPELINEIKEDLREECEKFGQVKKVVVFDRHPDGVASVKFKEPEEADKCIQAL
NGRWFAGRKLEAETWDGKTDY
>gnl|CDD|409725 cd12283, RRM1_RBM39_like, RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding protein 39 (RBM39) and similar proteins. This subfamily corresponds to the RRM1 of RNA-binding protein 39 (RBM39), RNA-binding protein 23 (RBM23) and similar proteins. RBM39 (also termed HCC1) is a nuclear autoantigen that contains an N-terminal arginine/serine rich (RS) motif and three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). An octapeptide sequence called the RS-ERK motif is repeated six times in the RS region of RBM39. Although the cellular function of RBM23 remains unclear, it shows high sequence homology to RBM39 and contains two RRMs. It may possibly function as a pre-mRNA splicing factor
TVFVMQLSLKARERDLYEFFSKAGKVRDVRLIMDRNSRRSKGVAYVEFYDVESVPLALALTGQRLLGQPI
MVQ
>gnl|CDD|409726 cd12284, RRM2_RBM23_RBM39, RNA recognition motif 2 (RRM2) found in vertebrate RNA-binding protein RBM23, RBM39 and similar proteins. This subfamily corresponds to the RRM2 of RBM39 (also termed HCC1), a nuclear autoantigen that contains an N-terminal arginine/serine rich (RS) motif and three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). An octapeptide sequence called the RS-ERK motif is repeated six times in the RS region of RBM39. Although the cellular function of RBM23 remains unclear, it shows high sequence homology to RBM39 and contains two RRMs. It may possibly function as a pre-mRNA splicing factor
LYVGSLHFNITEDMLRGIFEPFGKIEFVQLQKDPETGRSKGYGFIQFRDAEDAKKALEQLNGFELAGRPM
KVGHVTER
>gnl|CDD|409727 cd12285, RRM3_RBM39_like, RNA recognition motif 3 (RRM3) found in vertebrate RNA-binding protein 39 (RBM39) and similar proteins. This subfamily corresponds to the RRM3 of RBM39, also termed hepatocellular carcinoma protein 1, or RNA-binding region-containing protein 2, or splicing factor HCC1, ia nuclear autoantigen that contains an N-terminal arginine/serine rich (RS) motif and three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). An octapeptide sequence called the RS-ERK motif is repeated six times in the RS region of RBM39. Based on the specific domain composition, RBM39 has been classified into a family of non-snRNP (small nuclear ribonucleoprotein) splicing factors that are usually not complexed to snRNAs
SRCVILKNMFDPAEETEDNWDDEIKEDVIEECSKYGPVLHIYVDKNSPQGNVYVKFKTIEAAQKCVQAMN
GRWFDGRQITAAYVP
>gnl|CDD|409728 cd12286, RRM_Man1, RNA recognition motif (RRM) found in inner nuclear membrane protein Man1 (Man1) and similar proteins. This subfamily corresponds to the RRM of Man1, also termed LEM domain-containing protein 3 (LEMD3), an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. It is part of a protein complex essential for chromatin organization and cell division. It also functions as an important negative regulator for the transforming growth factor (TGF) beta/activin/Nodal signaling pathway by directly interacting with chromatin-associated proteins and transcriptional regulators, including the R-Smads, Smad1, Smad2, and Smad3. Moreover, Man1 is a unique type of left-right (LR) signaling regulator that acts on the inner nuclear membrane. Man1 plays a crucial role in angiogenesis. The vascular remodeling can be regulated at the inner nuclear membrane through the interaction between Man1 and Smads. Man1 contains an N-terminal LEM domain, two putative transmembrane domains, a MAN1-Src1p C-terminal (MSC) domain, and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The LEM domain interacts with the DNA and chromatin-binding protein Barrier-to-Autointegration Factor, and is also necessary for efficient localization of MAN1 in the inner nuclear membrane. Research has indicated that C-terminal nucleoplasmic region of Man1 exhibits a DNA binding winged helix domain and is responsible for both DNA- and Smad-binding
CLKIRNMFDPEMEIGEDWHVRIQEAILEKCSDNGGIVHIAVDKNSREGCVYIKCASPEDAGKAFKALHGC
WFDGRLVTVKYLRLERYHSRFP
>gnl|CDD|409729 cd12287, RRM_U2AF35_like, RNA recognition motif (RRM) found in U2 small nuclear ribonucleoprotein auxiliary factor U2AF 35 kDa subunit (U2AF35) and similar proteins. This subfamily corresponds to the RRM in U2 small nuclear ribonucleoprotein (snRNP) auxiliary factor (U2AF) which has been implicated in the recruitment of U2 snRNP to pre-mRNAs. It is a highly conserved heterodimer composed of large and small subunits; this family includes the small subunit of U2AF (U2AF35 or U2AF1) and U2AF 35 kDa subunit B (U2AF35B or C3H60). U2AF35 directly binds to the 3' splice site of the conserved AG dinucleotide and performs multiple functions in the splicing process in a substrate-specific manner. It promotes U2 snRNP binding to the branch-point sequences of introns through association with the large subunit of U2AF (U2AF65 or U2AF2). Although the biological role of U2AF35B remains unclear, it shows high sequence homolgy to U2AF35, which contains two N-terminal zinc fingers, a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal arginine/serine (SR) -rich segment interrupted by glycines. In contrast to U2AF35, U2AF35B has a plant-specific conserved C-terminal region containing SERE motif(s), which may have an important function specific to higher plants
TLLLKNMYPNPDNFISSLDDGSLTLSEEEIQEHFDEFYEDVFLELSRFGEIEDLVVCSNLNDHLLGNVYV
KFESEEDAEAALQALNGRYYAGRPLYPELSP
>gnl|CDD|409730 cd12288, RRM_La_like_plant, RNA recognition motif (RRM) found in plant proteins related to the La autoantigen. This subfamily corresponds to the RRM of plant La-like proteins related to the La autoantigen. A variety of La-related proteins (LARPs or La ribonucleoproteins), with differing domain architecture, appear to function as RNA-binding proteins in eukaryotic cellular processes. Members in this family contain an LAM domain followed by an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
RTVVVENLPEDHSIQNLREIFGTVGSVKNVRVCDPGRVGSGEKAKKPDTFVSNKLHALVEYETVEAAEKA
VTELNNEGNWRNGLRVRLLL
>gnl|CDD|409731 cd12289, RRM_LARP6, RNA recognition motif (RRM) found in La-related protein 6 (LARP6) and similar proteins. This subfamily corresponds to the RRM of LARP6, also termed Acheron (Achn), a novel member of the lupus antigen (La) family. It is expressed predominantly in neurons and muscle in vertebrates. LARP6 functions as a key regulatory protein that may play a role in mediating a variety of developmental and homeostatic processes in animals, including myogenesis, neurogenesis and possibly metastasis. LARP6 binds to Ca2+/calmodulin-dependent serine protein kinase (CASK), and forms a complex with inhibitor of differentiation transcription factors. It is structurally related to the La autoantigen and contains a La motif (LAM), nuclear localization and export (NLS and NES) signals, and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
RTVVAYNLPLNPKSIEHVSKLFSPCGEISLIRILRPGRTIPPDVKRHSNRHSQLGTKECAIVEFEEVEAA
RKAHELLGAEDDGKGGIKVVLLG
>gnl|CDD|409732 cd12290, RRM1_LARP7, RNA recognition motif 1 (RRM1) found in La-related protein 7 (LARP7) and similar proteins. This subfamily corresponds to the RRM1 of LARP7, also termed La ribonucleoprotein domain family member 7, or P-TEFb-interaction protein for 7SK stability (PIP7S), an oligopyrimidine-binding protein that binds to the highly conserved 3'-terminal U-rich stretch (3' -UUU-OH) of 7SK RNA. LARP7 is a stable component of the 7SK small nuclear ribonucleoprotein (7SK snRNP). It intimately associates with all the nuclear 7SK and is required for 7SK stability. LARP7 also acts as a negative transcriptional regulator of cellular and viral polymerase II genes, acting by means of the 7SK snRNP system. It plays an essential role in the inhibition of positive transcription elongation factor b (P-TEFb)-dependent transcription, which has been linked to the global control of cell growth and tumorigenesis. LARP7 contains a La motif (LAM) and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), at the N-terminal region, which mediates binding to the U-rich 3' terminus of 7SK RNA. LARP7 also carries another putative RRM domain at its C-terminus
TVYVELLPKNATHEWIEAVFSKYGEVVYVSIPRYKSTGDPKGFAFIEFETSESAQKAVKHFNSPPEARRK
PGPFPKTVA
>gnl|CDD|409733 cd12291, RRM1_La, RNA recognition motif 1 in La autoantigen (La or LARP3) and similar proteins. This subfamily corresponds to the RRM1 of La autoantigen, also termed Lupus La protein, or La ribonucleoprotein, or Sjoegren syndrome type B antigen (SS-B), a highly abundant nuclear phosphoprotein and well conserved in eukaryotes. It specifically binds the 3'-terminal UUU-OH motif of nascent RNA polymerase III transcripts and protects them from exonucleolytic degradation by 3' exonucleases. In addition, La can directly facilitate the translation and/or metabolism of many UUU-3' OH-lacking cellular and viral mRNAs, through binding internal RNA sequences within the untranslated regions of target mRNAs. La contains an N-terminal La motif (LAM), followed by two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). It also possesses a short basic motif (SBM) and a nuclear localization signal (NLS) at the C-terminus
TVYVKGFPLDATLDDIQEFFEKKGKVENVRMRRDLDSKEFKGSVFVEFKTEEEAKKFLEKEKLKYKGKEL
TIM
>gnl|CDD|409734 cd12292, RRM2_La_like, RNA recognition motif 2 in La autoantigen (La or SS-B or LARP3), La-related protein 7 (LARP7 or PIP7S) and similar proteins. This subfamily corresponds to the RRM2 of La and LARP7. La is a highly abundant nuclear phosphoprotein and well conserved in eukaryotes. It specifically binds the 3'-terminal UUU-OH motif of nascent RNA polymerase III transcripts and protects them from exonucleolytic degradation by 3' exonucleases. In addition, La can directly facilitate the translation and/or metabolism of many UUU-3' OH-lacking cellular and viral mRNAs, through binding internal RNA sequences within the untranslated regions of target mRNAs. LARP7 is an oligopyrimidine-binding protein that binds to the highly conserved 3'-terminal U-rich stretch (3' -UUU-OH) of 7SK RNA. It is a stable component of the 7SK small nuclear ribonucleoprotein (7SK snRNP), intimately associates with all the nuclear 7SK and is required for 7SK stability. LARP7 also acts as a negative transcriptional regulator of cellular and viral polymerase II genes, acting by means of the 7SK snRNP system. LARP7 plays an essential role in the inhibition of positive transcription elongation factor b (P-TEFb)-dependent transcription, which has been linked to the global control of cell growth and tumorigenesis. Both La and LARP7 contain an N-terminal La motif (LAM), followed by two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
GLILKITGIGPSVSRDDLKELFKQFGEVEYVDFTPGDDEGHVRFKTSEAAQKARDAYTGKLELNGKEWKL
EILE
>gnl|CDD|410983 cd12293, dRRM_Rrp7p, deviant RNA recognition motif (dRRM) in yeast ribosomal RNA-processing protein 7 (Rrp7p) and similar proteins. Rrp7p is encoded by YCL031C gene from Saccharomyces cerevisiae. It is an essential yeast protein involved in pre-rRNA processing and ribosome assembly, and is speculated to be required for correct assembly of rpS27 into the pre-ribosomal particle. Rrp7p contains a deviant RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a RRP7 domain. The classic RRM fold has a topology of beta1-alpha1-beta2-beta3-alpha2-beta4 with juxtaposed N- and C-termini. By contrast, the N-terminal region of Rrp7 displays a cyclic permutation of RRM topology: the strand equivalent to RRM beta4 is shuffled to the N-terminus of the strand equivalent to RRM beta1. Moreover, Rrp7 has an extra strand beta1, which, together with other four beta-strands, forms an antiparallel five-stranded beta-sheet
AEINGFLVLPVTVPSPSASPEKTTHYLYIRKHASKNPAETLPASRTLFLVNLPVDSTERHLRKLFGLGGG
RIESVLHSSGSTAHVVFVDKASLDLAMKAIKKLVK
>gnl|CDD|409735 cd12294, RRM_Rrp7A, RNA recognition motif in ribosomal RNA-processing protein 7 homolog A (Rrp7A) and similar proteins. This subfamily corresponds to the RRM of Rrp7A, also termed gastric cancer antigen Zg14, a homolog of yeast ribosomal RNA-processing protein 7 (Rrp7p), and mainly found in Metazoa. Rrp7p is an essential yeast protein involved in pre-rRNA processing and ribosome assembly, and is speculated to be required for correct assembly of rpS27 into the pre-ribosomal particle. In contrast, the cellular function of Rrp7A remains unclear currently. Rrp7A harbors an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal Rrp7 domain
RTLFVLNVPPYCTEESLKRLFSRCGKVESVELQEKPGPAEKIDSKTSKFFNPQPIKGFKVAYVVFKKPSS
LKAALKLKSTKPFVLSTESHPVKTGLEKWIKEY
>gnl|CDD|409736 cd12295, RRM_YRA2, RNA recognition motif in yeast RNA annealing protein YRA2 (Yra2p) and similar proteins. This subfamily corresponds to the RRM of Yra2p, a nonessential nuclear RNA-binding protein encoded by Saccharomyces cerevisiae YRA2 gene. It may share some overlapping functions with Yra1p, and is able to complement an YRA1 deletion when overexpressed in yeast. Yra2p belongs to the evolutionarily conserved REF (RNA and export factor binding proteins) family of hnRNP-like proteins. It is a major component of endogenous Yra1p complexes. It interacts with Yra1p and functions as a negative regulator of Yra1p. Yra2p consists of two highly conserved N- and C-terminal boxes and a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
KRLRITNIPLDVSDYTIEDMIKEFGEPEYINFYDHKDSRSAIFEFEDPEILEKAVEKYNGKELHGAKIEV
EIFE
>gnl|CDD|409737 cd12296, RRM1_Prp24, RNA recognition motif 1 in fungal pre-messenger RNA splicing protein 24 (Prp24) and similar proteins. This subfamily corresponds to the RRM1 of Prp24, also termed U4/U6 snRNA-associated-splicing factor PRP24 (U4/U6 snRNP), an RNA-binding protein with four well conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). It facilitates U6 RNA base-pairing with U4 RNA during spliceosome assembly. Prp24 specifically binds free U6 RNA primarily with RRMs 1 and 2 and facilitates pairing of U6 RNA bases with U4 RNA bases. Additionally, it may also be involved in dissociation of the U4/U6 complex during spliceosome activation
LTVLVKNLPKSITENKIRQFFKDCGEIREVKILESGNGLVAVIEFETEDEALAALTKDHKRIGGNEISVS
R
>gnl|CDD|409738 cd12297, RRM2_Prp24, RNA recognition motif 2 in fungal pre-messenger RNA splicing protein 24 (Prp24) and similar proteins. This subfamily corresponds to the RRM2 of Prp24, also termed U4/U6 snRNA-associated-splicing factor PRP24 (U4/U6 snRNP), an RNA-binding protein with four well conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). It facilitates U6 RNA base-pairing with U4 RNA during spliceosome assembly. Prp24 specifically binds free U6 RNA primarily with RRMs 1 and 2 and facilitates pairing of U6 RNA bases with U4 RNA bases. Additionally, it may also be involved in dissociation of the U4/U6 complex during spliceosome activation
CTLWVTNFPPSYDERSIRDLFGDYGVILSVRLPSLRYNTSRRFCYIDFTSPESARAAVELLNGLLEEGYT
LVVKISDP
>gnl|CDD|409739 cd12298, RRM3_Prp24, RNA recognition motif 3 in fungal pre-messenger RNA splicing protein 24 (Prp24) and similar proteins. This subfamily corresponds to the RRM3 of Prp24, also termed U4/U6 snRNA-associated-splicing factor PRP24 (U4/U6 snRNP), an RNA-binding protein with four well conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). It facilitates U6 RNA base-pairing with U4 RNA during spliceosome assembly. Prp24 specifically binds free U6 RNA primarily with RRMs 1 and 2 and facilitates pairing of U6 RNA bases with U4 RNA bases. Additionally, it may also be involved in dissociation of the U4/U6 complex during spliceosome activation
REIRVRNLDFELDEEALRGIFEKFGEIESINIPKKQKNRKGRHNNGFAFVTFEDADSAESALQLNGTLLD
NRKISVSL
>gnl|CDD|409740 cd12299, RRM4_Prp24, RNA recognition motif 4 in fungal pre-messenger RNA splicing protein 24 (Prp24) and similar proteins. This subfamily corresponds to the RRM4 of Prp24, also termed U4/U6 snRNA-associated-splicing factor PRP24 (U4/U6 snRNP), an RNA-binding protein with four well conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). It facilitates U6 RNA base-pairing with U4 RNA during spliceosome assembly. Prp24 specifically binds free U6 RNA primarily with RRMs 1 and 2 and facilitates pairing of U6 RNA bases with U4 RNA bases. Additionally, it may also be involved in dissociation of the U4/U6 complex during spliceosome activation
RTIGLFNLSDTVNEEQIRAFFEKIGPDIRKILLVPDHEGALVEFEDESDAGKASLSLDGSQFQGKTIRCG
S
>gnl|CDD|409741 cd12300, RRM1_PAR14, RNA recognition motif 1 in vertebrate poly [ADP-ribose] polymerase 14 (PARP-14). This subfamily corresponds to the RRM1 of PARP-14, also termed aggressive lymphoma protein 2, a member of the B aggressive lymphoma (BAL) family of macrodomain-containing PARPs. It is expressed in B lymphocytes and interacts with the IL-4-induced transcription factor Stat6. It plays a fundamental role in the regulation of IL-4-induced B-cell protection against apoptosis after irradiation or growth factor withdrawal. It mediates IL-4 effects on the levels of gene products that regulate cell survival, proliferation, and lymphomagenesis. PARP-14 acts as a transcriptional switch for Stat6-dependent gene activation. In the presence of IL-4, PARP-14 activates transcription by facilitating the binding of Stat6 to the promoter and release of HDACs from the promoter with an IL-4 signal. In contrast, in the absence of a signal, PARP-14 acts as a transcriptional repressor by recruiting HDACs. Moreover, the absence of PARP-14 protects against Myc-induced developmental block and lymphoma. Thus, PARP-14 may play an important role in Myc-induced oncogenesis. Research indicates that PARP-14 is also a binding partner with phosphoglucose isomerase (PGI)/ autocrine motility factor (AMF). It can inhibit PGI/AMF ubiquitination, thus contributing to its stabilization and secretion. PARP-14 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), three tandem macro domains, and C-terminal region with sequence homology to PARP catalytic domain
PFPLLVEGDWDPSPPKKLKNKLEKYFQSKKRSGGGECTVETEGPSPQTARVSFVNEEVRERVLEKKEHEI
LQGEGTVRLTVK
>gnl|CDD|409742 cd12301, RRM1_2_PAR10_like, RNA recognition motif 1 and 2 in poly [ADP-ribose] polymerase PARP-10, RNA recognition motif 2 in PARP-14, RNA recognition motif in N-myc-interactor (Nmi), interferon-induced 35 kDa protein (IFP 35), RNA-binding protein 43 (RBM43) and similar proteins. This subfamily corresponds to the RRM1 and RRM2 of PARP-10, RRM2 of PARP-14, RRM of N-myc-interactor (Nmi), interferon-induced 35 kDa protein (IFP 35) and RNA-binding protein 43 (RBM43). PARP-10 is a novel oncoprotein c-Myc-interacting protein with poly(ADP-ribose) polymerase activity. It is localized to the nuclear and cytoplasmic compartments. In addition to PARP activity, PARP-10 is also involved in the control of cell proliferation by inhibiting c-Myc- and E1A-mediated cotransformation of primary cells. PARP-10 may also play a role in nuclear processes including the regulation of chromatin, gene transcription, and nuclear/cytoplasmic transport. PARP-10 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two overlapping C-terminal domains composed of a glycine-rich region and a region with homology to catalytic domains of PARP enzymes (PARP domain). In addition, PARP-10 contains two ubiquitin-interacting motifs (UIM). PARP-14, also termed aggressive lymphoma protein 2, is a member of the B aggressive lymphoma (BAL) family of macrodomain-containing PARPs. Like PARP-10, PARP-14 also includes two RRMs at the N-terminus. Nmi, also termed N-myc and STAT interactor, is an interferon inducible protein that interacts with c-Myc, N-Myc, Max and c-Fos, and other transcription factors containing bHLH-ZIP, bHLH or ZIP domains. Besides binding Myc proteins, Nmi also associates with all the Stat family of transcription factors except Stat2. In response to cytokine (e.g. IL-2 and IFN-gamma) stimulation, Nmi can enhance Stat-mediated transcriptional activity through recruiting the Stat1 and Stat5 transcriptional coactivators, CREB-binding protein (CBP) and p300. IFP 35 is an interferon-induced leucine zipper protein that can specifically form homodimers. Distinct from known bZIP proteins, IFP 35 lacks a basic domain critical for DNA binding. In addition, IFP 35 may negatively regulate other bZIP transcription factors by protein-protein interaction. For instance, it can form heterodimers with B-ATF, a member of the AP1 transcription factor family. Both Nmi and IFP35 harbor one RRM. RBM43 is a putative RNA-binding protein containing one RRM, but its biological function remains unclear
RSVLVTGLPEAEALDDKLELYFENSRSGGGDVEDVEYLGEKGSAVVTFKDHKVAQRVLAQKKHPLNGMQL
SVRP
>gnl|CDD|409743 cd12302, RRM_scSet1p_like, RNA recognition motif in budding yeast Saccharomyces cerevisiae SET domain-containing protein 1 (scSet1p) and similar proteins. This subfamily corresponds to the RRM of scSet1p, also termed H3 lysine-4 specific histone-lysine N-methyltransferase, or COMPASS component SET1, or lysine N-methyltransferase 2, which is encoded by SET1 from the yeast S. cerevisiae. It is a nuclear protein that may play a role in both silencing and activating transcription. scSet1p is closely related to the SET domain proteins of multicellular organisms, which are implicated in diverse aspects of cell morphology, growth control, and chromatin-mediated transcriptional silencing. scSet1p contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a conserved SET domain that may play a role in DNA repair and telomere function
PPVEIVVWGLNPSTSETIIKNYFKSFGEIAEFRNVMDPDTAVPLGIYTIKFKGSPSKPSEAAKAALKAVR
KMHDKCRISGNKFKVELNDNRKLNKIKSKLIKQNRKKSQA
>gnl|CDD|409744 cd12303, RRM_spSet1p_like, RNA recognition motif in fission yeast Schizosaccharomyces pombe SET domain-containing protein 1 (spSet1p) and similar proteins. This subfamily corresponds to the RRM of spSet1p, also termed H3 lysine-4 specific histone-lysine N-methyltransferase, or COMPASS component SET1, or lysine N-methyltransferase 2, or Set1 complex component, is encoded by SET1 from the fission yeast S. pombe. It is essential for the H3 lysine-4 methylation. in vivo, and plays an important role in telomere maintenance and DNA repair in an ATM kinase Rad3-dependent pathway. spSet1p is the homology counterpart of Saccharomyces cerevisiae Set1p (scSet1p). However, it is more closely related to Set1 found in mammalian. Moreover, unlike scSet1p, spSet1p is not required for heterochromatin assembly in fission yeast. spSet1p contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a conserved SET domain that may play a role in DNA repair and telomere function
IVITGLSPLTTSNQILLHFRPHGEIEASDLKLDPRTGQSIGICWVRFAGPYLRLSNAAESAKRAVSGQNG
YRIGGATIRVFLDRDG
>gnl|CDD|409745 cd12304, RRM_Set1, RNA recognition motif in the Set1-like family of histone-lysine N-methyltransferases. This subfamily corresponds to the RRM of the Set1-like family of histone-lysine N-methyltransferases which includes Set1A and Set1B that are ubiquitously expressed vertebrates histone methyltransferases exhibiting high homology to yeast Set1. Set1A and Set1B proteins exhibit a largely non-overlapping subnuclear distribution in euchromatic nuclear speckles, strongly suggesting that they bind to a unique set of target genes and thus make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. With the exception of the catalytic component, the subunit composition of the Set1A and Set1B histone methyltransferase complexes are identical. Each complex contains six human homologs of the yeast Set1/COMPASS complex, including Set1A or Set1B, Ash2 (homologous to yeast Bre2), CXXC finger protein 1 (CFP1; homologous to yeast Spp1), Rbbp5 (homologous to yeast Swd1), Wdr5 (homologous to yeast Swd3), and Wdr82 (homologous to yeast Swd2). The genomic targeting of these complexes is determined by the identity of the catalytic subunit present in each histone methyltransferase complex. Thus, the Set1A and Set1B complexes may exhibit both overlapping and non-redundant properties. Both Set1A and Set1B contain an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), an N- SET domain, and a C-terminal catalytic SET domain followed by a post-SET domain. In contrast to Set1B, Set1A additionally contains an HCF-1 binding motif that interacts with HCF-1 in vivo
PPREVTFANLNDNINEGFLKDMCKKYGEVEEVKIYFHPKTGKHLGLARVVFDTTKGAKDCVEKLNQTSVM
GNIIHVFLDPKGRIIARLYEDIV
>gnl|CDD|409746 cd12305, RRM_NELFE, RNA recognition motif in negative elongation factor E (NELF-E) and similar proteins. This subfamily corresponds to the RRM of NELF-E, also termed RNA-binding protein RD. NELF-E is the RNA-binding subunit of cellular negative transcription elongation factor NELF (negative elongation factor) involved in transcriptional regulation of HIV-1 by binding to the stem of the viral transactivation-response element (TAR) RNA which is synthesized by cellular RNA polymerase II at the viral long terminal repeat. NELF is a heterotetrameric protein consisting of NELF A, B, C or the splice variant D, and E. NELF-E contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). It plays a role in the control of HIV transcription by binding to TAR RNA. In addition, NELF-E is associated with the NELF-B subunit, probably via a leucine zipper motif
PRKGNTVYVSGYGITEDVLKKAFSPFGNIINISMEIEKNCAFVTFEKMESADQAIAELNGTTVEGVQLKV
SIARR
>gnl|CDD|409747 cd12306, RRM_II_PABPs, RNA recognition motif in type II polyadenylate-binding proteins. This subfamily corresponds to the RRM of type II polyadenylate-binding proteins (PABPs), including polyadenylate-binding protein 2 (PABP-2 or PABPN1), embryonic polyadenylate-binding protein 2 (ePABP-2 or PABPN1L) and similar proteins. PABPs are highly conserved proteins that bind to the poly(A) tail present at the 3' ends of most eukaryotic mRNAs. They have been implicated in the regulation of poly(A) tail length during the polyadenylation reaction, translation initiation, mRNA stabilization by influencing the rate of deadenylation and inhibition of mRNA decapping. ePABP-2 is predominantly located in the cytoplasm and PABP-2 is located in the nucleus. In contrast to the type I PABPs containing four copies of RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), the type II PABPs contains a single highly-conserved RRM. This subfamily also includes Saccharomyces cerevisiae RBP29 (SGN1, YIR001C) gene encoding cytoplasmic mRNA-binding protein Rbp29 that binds preferentially to poly(A). Although not essential for cell viability, Rbp29 plays a role in modulating the expression of cytoplasmic mRNA. Like other type II PABPs, Rbp29 contains one RRM only
SIYVGNVDYGTTPEELQAHFKSCGTINRVTILCDKFTGQPKGFAYIEFVDKSSVENALLLNESEFRGRQI
KVT
>gnl|CDD|409748 cd12307, RRM_NIFK_like, RNA recognition motif in nucleolar protein interacting with the FHA domain of pKI-67 (NIFK) and similar proteins. This subgroup corresponds to the RRM of NIFK and Nop15p. NIFK, also termed MKI67 FHA domain-interacting nucleolar phosphoprotein, or nucleolar phosphoprotein Nopp34, is a putative RNA-binding protein interacting with the forkhead associated (FHA) domain of pKi-67 antigen in a mitosis-specific and phosphorylation-dependent manner. It is nucleolar in interphase but associates with condensed mitotic chromosomes. This family also includes Saccharomyces cerevisiae YNL110C gene encoding ribosome biogenesis protein 15 (Nop15p), also termed nucleolar protein 15. Both, NIFK and Nop15p, contain an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
VVYIGHLPHGFYEPELRKYFSQFGTVTRLRLSRSKKTGKSKGYAFVEFEDPEVAKIVAETMNNYLLFERL
LKCK
>gnl|CDD|409749 cd12308, RRM1_Spen, RNA recognition motif 1 (RRM1) found in the Spen (split end) protein family. This subfamily corresponds to the RRM1 domain in the Spen (split end) family which includes RNA binding motif protein 15 (RBM15), putative RNA binding motif protein 15B (RBM15B), and similar proteins found in Metazoa. RBM15, also termed one-twenty two protein 1 (OTT1), conserved in eukaryotes, is a novel mRNA export factor and component of the NXF1 pathway. It binds to NXF1 and serves as receptor for the RNA export element RTE. It also possesses mRNA export activity and can facilitate the access of DEAD-box protein DBP5 to mRNA at the nuclear pore complex (NPC). RNA-binding protein 15B (RBM15B), also known as one twenty-two 3 (OTT3), is a paralog of RBM15 and therefore has post-transcriptional regulatory activity. It is a nuclear protein sharing with RBM15 the association with the splicing factor compartment and the nuclear envelope as well as the binding to mRNA export factors NXF1 and Aly/REF. Members in this family belong- to the Spen (split end) protein family, which share a domain architecture comprising of three N-terminal RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain
YKTLCVSNLPAKLSDEEIEDVLYHEFKKFGDVSVRLQHDGDERVAYVNFRHPEDAREAKHAKLRLVLFDR
PLNVEPVY
>gnl|CDD|240755 cd12309, RRM2_Spen, RNA recognition motif 2 (RRM2) found in the Spen (split end) protein family. This subfamily corresponds to the RRM2 domain in the Spen (split end) protein family which includes RNA binding motif protein 15 (RBM15), putative RNA binding motif protein 15B (RBM15B), and similar proteins found in Metazoa. RBM15, also termed one-twenty two protein 1 (OTT1), conserved in eukaryotes, is a novel mRNA export factor and component of the NXF1 pathway. It binds to NXF1 and serves as receptor for the RNA export element RTE. It also possess mRNA export activity and can facilitate the access of DEAD-box protein DBP5 to mRNA at the nuclear pore complex (NPC). RNA-binding protein 15B (RBM15B), also termed one twenty-two 3 (OTT3), is a paralog of RBM15 and therefore has post-transcriptional regulatory activity. It is a nuclear protein sharing with RBM15 the association with the splicing factor compartment and the nuclear envelope as well as the binding to mRNA export factors NXF1 and Aly/REF. Members in this family belong to the Spen (split end) protein family, which share a domain architecture comprising of three N-terminal RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain
ATRTLFVGNLEITITEEELRRAFERYGVVEDVDIKRPPRGQGNAYAFVKFLNLDMAHRAKVAMSGQYIGR
NQIKIGYGK
>gnl|CDD|409750 cd12310, RRM3_Spen, RNA recognition motif 3 (RRM3) found in the Spen (split end) protein family. This subfamily corresponds to the RRM3 domain in the Spen (split end) protein family which includes RNA binding motif protein 15 (RBM15), putative RNA binding motif protein 15B (RBM15B) and similar proteins found in Metazoa. RBM15, also termed one-twenty two protein 1 (OTT1), conserved in eukaryotes, is a novel mRNA export factor and is a novel component of the NXF1 pathway. It binds to NXF1 and serves as receptor for the RNA export element RTE. It also possess mRNA export activity and can facilitate the access of DEAD-box protein DBP5 to mRNA at the nuclear pore complex (NPC). RNA-binding protein 15B (RBM15B), also termed one twenty-two 3 (OTT3), is a paralog of RBM15 and therefore has post-transcriptional regulatory activity. It is a nuclear protein sharing with RBM15 the association with the splicing factor compartment and the nuclear envelope as well as the binding to mRNA export factors NXF1 and Aly/REF. Members in this family belong to the Spen (split end) protein family, which shares a domain architecture comprising of three N-terminal RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain
LWVGGLGPWTSLAELEREFDRFGAIRKIDYRKGDDYAYILYESLDAAQAAVRALRGFPLGGPDRRLRVDF
AD
>gnl|CDD|409751 cd12311, RRM_SRSF2_SRSF8, RNA recognition motif (RRM) found in serine/arginine-rich splicing factor SRSF2, SRSF8 and similar proteins. This subfamily corresponds to the RRM of SRSF2 and SRSF8. SRSF2, also termed protein PR264, or splicing component, 35 kDa (splicing factor SC35 or SC-35), is a prototypical SR protein that plays important roles in the alternative splicing of pre-mRNA. It is also involved in transcription elongation by directly or indirectly mediating the recruitment of elongation factors to the C-terminal domain of polymerase II. SRSF2 is exclusively localized in the nucleus and is restricted to nuclear processes. It contains a single N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C-terminal RS domain rich in serine-arginine dipeptides. The RRM is responsible for the specific recognition of 5'-SSNG-3' (S=C/G) RNA. In the regulation of alternative splicing events, it specifically binds to cis-regulatory elements on the pre-mRNA. The RS domain modulates SRSF2 activity through phosphorylation, directly contacts RNA, and promotes protein-protein interactions with the spliceosome. SRSF8, also termed SRP46 or SFRS2B, is a novel mammalian SR splicing factor encoded by a PR264/SC35 functional retropseudogene. SRSF8 is localized in the nucleus and does not display the same activity as PR264/SC35. It functions as an essential splicing factor in complementing a HeLa cell S100 extract deficient in SR proteins. Like SRSF2, SRSF8 contains a single N-terminal RRM and a C-terminal RS domain
LKVDNLTYRTTPDDLRRVFEKYGEVGDVYIPRDRYTRESRGFAFVRFYDKRDAEDAIDAMDGAELDGREL
RVQ
>gnl|CDD|240758 cd12312, RRM_SRSF10_SRSF12, RNA recognition motif (RRM) found in serine/arginine-rich splicing factor SRSF10, SRSF12 and similar proteins. This subfamily corresponds to the RRM of SRSF10 and SRSF12. SRSF10, also termed 40 kDa SR-repressor protein (SRrp40), or FUS-interacting serine-arginine-rich protein 1 (FUSIP1), or splicing factor SRp38, or splicing factor, arginine/serine-rich 13A (SFRS13A), or TLS-associated protein with Ser-Arg repeats (TASR). It is a serine-arginine (SR) protein that acts as a potent and general splicing repressor when dephosphorylated. It mediates global inhibition of splicing both in M phase of the cell cycle and in response to heat shock. SRSF10 emerges as a modulator of cholesterol homeostasis through the regulation of low-density lipoprotein receptor (LDLR) splicing efficiency. It also regulates cardiac-specific alternative splicing of triadin pre-mRNA and is required for proper Ca2+ handling during embryonic heart development. In contrast, the phosphorylated SRSF10 functions as a sequence-specific splicing activator in the presence of a nuclear cofactor. It activates distal alternative 5' splice site of adenovirus E1A pre-mRNA in vivo. Moreover, SRSF10 strengthens pre-mRNA recognition by U1 and U2 snRNPs. SRSF10 localizes to the nuclear speckles and can shuttle between nucleus and cytoplasm. SRSF12, also termed 35 kDa SR repressor protein (SRrp35), or splicing factor, arginine/serine-rich 13B (SFRS13B), or splicing factor, arginine/serine-rich 19 (SFRS19), is a serine/arginine (SR) protein-like alternative splicing regulator that antagonizes authentic SR proteins in the modulation of alternative 5' splice site choice. For instance, it activates distal alternative 5' splice site of the adenovirus E1A pre-mRNA in vivo. Both, SRSF10 and SRSF12, contain a single N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C-terminal RS domain rich in serine-arginine dipeptides
TSLFVRNVADDTRPDDLRREFGRYGPIVDVYIPLDFYTRRPRGFAYIQFEDVRDAEDALYYLDRTRFLGR
EIEIQFAQGDRKTP
>gnl|CDD|409752 cd12313, RRM1_RRM2_RBM5_like, RNA recognition motif 1 (RRM1) and 2 (RRM2) found in RNA-binding protein 5 (RBM5) and similar proteins. This subfamily includes the RRM1 and RRM2 of RNA-binding protein 5 (RBM5 or LUCA15 or H37) and RNA-binding protein 10 (RBM10 or S1-1), and the RRM2 of RNA-binding protein 6 (RBM6 or NY-LU-12 or g16 or DEF-3). These RBMs share high sequence homology and may play an important role in regulating apoptosis. RBM5 is a known modulator of apoptosis. It may also act as a tumor suppressor or an RNA splicing factor. RBM6 has been predicted to be a nuclear factor based on its nuclear localization signal. Both, RBM6 and RBM5, specifically bind poly(G) RNA. RBM10 is a paralog of RBM5. It may play an important role in mRNA generation, processing and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. All family members contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, and a G-patch/D111 domain
PTNVLILRGLDVLTTEEDILSALQAHADLPIKDVRLIRDKLTGTSRGFAFVEFSSLEDATQVMDALQNLL
PPFKIDGRVVSVSYA
>gnl|CDD|409753 cd12314, RRM1_RBM6, RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding protein 6 (RBM6). This subfamily corresponds to the RRM1 of RBM6, also termed lung cancer antigen NY-LU-12, or protein G16, or RNA-binding protein DEF-3, which has been predicted to be a nuclear factor based on its nuclear localization signal. It shows high sequence similarity to RNA-binding protein 5 (RBM5 or LUCA15 or NY-REN-9). Both, RBM6 and RBM5, specifically bind poly(G) RNA. They contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, a nuclear localization signal, and a G-patch/D111 domain. In contrast to RBM5, RBM6 has two additional unique domains: the decamer repeat occurring more than 20 times, and the POZ (poxvirus and zinc finger) domain. The POZ domain may be involved in protein-protein interactions and inhibit binding of target sequences by zinc fingers
NLIRLIGVPETATKEQILNAFRVPDGMPVKNLKLKNYVPGYDYDYVCVEFSLLEDAIGCMEANQGTLKIG
TKEVTLEY
>gnl|CDD|409754 cd12315, RRM1_RBM19_MRD1, RNA recognition motif 1 (RRM1) found in RNA-binding protein 19 (RBM19), yeast multiple RNA-binding domain-containing protein 1 (MRD1) and similar proteins. This subfamily corresponds to the RRM1 of RBM19 and MRD1. RBM19, also termed RNA-binding domain-1 (RBD-1), is a nucleolar protein conserved in eukaryotes. It is involved in ribosome biogenesis by processing rRNA and is essential for preimplantation development. It has a unique domain organization containing 6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). MRD1 is encoded by a novel yeast gene MRD1 (multiple RNA-binding domain). It is well-conserved in yeast and its homologs exist in all eukaryotes. MRD1 is present in the nucleolus and the nucleoplasm. It interacts with the 35 S precursor rRNA (pre-rRNA) and U3 small nucleolar RNAs (snoRNAs). It is essential for the initial processing at the A0-A2 cleavage sites in the 35 S pre-rRNA. MRD1 contains 5 conserved RRMs, which may play an important structural role in organizing specific rRNA processing events
SRLIVKNLPLSLDEDQFRRLFSQKCKDIGLTITDCKLLTKSGGVSRRFGFVGFKDEEDAQKAKEFFNGTY
FRTSKVTVEFS
>gnl|CDD|409755 cd12316, RRM3_RBM19_RRM2_MRD1, RNA recognition motif 3 (RRM3) found in RNA-binding protein 19 (RBM19) and RNA recognition motif 2 found in multiple RNA-binding domain-containing protein 1 (MRD1). This subfamily corresponds to the RRM3 of RBM19 and RRM2 of MRD1. RBM19, also termed RNA-binding domain-1 (RBD-1), is a nucleolar protein conserved in eukaryotes involved in ribosome biogenesis by processing rRNA and is essential for preimplantation development. It has a unique domain organization containing 6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). MRD1 is encoded by a novel yeast gene MRD1 (multiple RNA-binding domain). It is well conserved in yeast and its homologs exist in all eukaryotes. MRD1 is present in the nucleolus and the nucleoplasm. It interacts with the 35 S precursor rRNA (pre-rRNA) and U3 small nucleolar RNAs (snoRNAs). It is essential for the initial processing at the A0-A2 cleavage sites in the 35 S pre-rRNA. MRD1 contains 5 conserved RRMs, which may play an important structural role in organizing specific rRNA processing events
RLFVRNLPFTATEDELRELFEAFGKISEVHIPLDKQTKRSKGFAFVLFVIPEDAVKAYQELDGSIFQGRL
LHVL
>gnl|CDD|409756 cd12317, RRM4_RBM19_RRM3_MRD1, RNA recognition motif 4 (RRM4) found in RNA-binding protein 19 (RBM19) and RNA recognition motif 3 (RRM3) found in multiple RNA-binding domain-containing protein 1 (MRD1). This subfamily corresponds to the RRM4 of RBM19 and the RRM3 of MRD1. RBM19, also termed RNA-binding domain-1 (RBD-1), is a nucleolar protein conserved in eukaryotes involved in ribosome biogenesis by processing rRNA and is essential for preimplantation development. It has a unique domain organization containing 6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). MRD1 is encoded by a novel yeast gene MRD1 (multiple RNA-binding domain). It is well conserved in yeast and its homologues exist in all eukaryotes. MRD1 is present in the nucleolus and the nucleoplasm. It interacts with the 35 S precursor rRNA (pre-rRNA) and U3 small nucleolar RNAs (snoRNAs). MRD1 is essential for the initial processing at the A0-A2 cleavage sites in the 35 S pre-rRNA. MRD1 contains 5 conserved RRMs, which may play an important structural role in organizing specific rRNA processing events
TVILVKNLPFGATEEELRELFEKFGTLGRLLLPPSRTIALVEFLEPQDARRAFKKLAYKRFKHVPLYLEW
AP
>gnl|CDD|409757 cd12318, RRM5_RBM19_like, RNA recognition motif 5 (RRM5) found in RNA-binding protein 19 (RBM19 or RBD-1) and similar proteins. This subfamily corresponds to the RRM5 of RBM19 and RRM4 of MRD1. RBM19, also termed RNA-binding domain-1 (RBD-1), is a nucleolar protein conserved in eukaryotes involved in ribosome biogenesis by processing rRNA and is essential for preimplantation development. It has a unique domain organization containing 6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
TTLFVKNLNFKTTEEALKKHFEKCGPIRSVTIAKKKDPKGPLLSMGYGFVEFKSPEAAQKALKQLQGTVL
DGHALELKIS
>gnl|CDD|409758 cd12319, RRM4_MRD1, RNA recognition motif 4 (RRM4) found in yeast multiple RNA-binding domain-containing protein 1 (MRD1) and similar proteins. This subfamily corresponds to the RRM4 of MRD1which is encoded by a novel yeast gene MRD1 (multiple RNA-binding domain). It is well-conserved in yeast and its homologs exist in all eukaryotes. MRD1 is present in the nucleolus and the nucleoplasm. It interacts with the 35 S precursor rRNA (pre-rRNA) and U3 small nucleolar RNAs (snoRNAs). MRD1 is essential for the initial processing at the A0-A2 cleavage sites in the 35 S pre-rRNA. It contains 5 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which may play an important structural role in organizing specific rRNA processing events
ATLFVKNLNFSTTNQHLTDVFKHLDGFVFARVKTKPDPKRPGKTLSMGFGFVGFKTKEQAQAALKAMDGF
VLDGHKLEVKFSHR
>gnl|CDD|409759 cd12320, RRM6_RBM19_RRM5_MRD1, RNA recognition motif 6 (RRM6) found in RNA-binding protein 19 (RBM19 or RBD-1) and RNA recognition motif 5 (RRM5) found in multiple RNA-binding domain-containing protein 1 (MRD1). This subfamily corresponds to the RRM6 of RBM19 and RRM5 of MRD1. RBM19, also termed RNA-binding domain-1 (RBD-1), is a nucleolar protein conserved in eukaryotes. It is involved in ribosome biogenesis by processing rRNA and is essential for preimplantation development. It has a unique domain organization containing 6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). MRD1 is encoded by a novel yeast gene MRD1 (multiple RNA-binding domain). It is well-conserved in yeast and its homologs exist in all eukaryotes. MRD1 is present in the nucleolus and the nucleoplasm. It interacts with the 35 S precursor rRNA (pre-rRNA) and U3 small nucleolar RNAs (snoRNAs). It is essential for the initial processing at the A0-A2 cleavage sites in the 35 S pre-rRNA. MRD1 contains 5 conserved RRMs, which may play an important structural role in organizing specific rRNA processing events
TKLIVKNVPFEATRKEIRELFSPFGQLKSVRLPKKFDGSHRGFAFVEFVTKQEAQNAMEALKSTHLYGRH
LVLEYA
>gnl|CDD|409760 cd12321, RRM1_TDP43, RNA recognition motif 1 (RRM1) found in TAR DNA-binding protein 43 (TDP-43) and similar proteins. This subfamily corresponds to the RRM1 of TDP-43 (also termed TARDBP), a ubiquitously expressed pathogenic protein whose normal function and abnormal aggregation are directly linked to the genetic disease cystic fibrosis, and two neurodegenerative disorders: frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). TDP-43 binds both DNA and RNA, and has been implicated in transcriptional repression, pre-mRNA splicing and translational regulation. TDP-43 is a dimeric protein with two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal glycine-rich domain. The RRMs are responsible for DNA and RNA binding; they bind to TAR DNA and RNA sequences with UG-repeats. The glycine-rich domain can interact with the hnRNP family proteins to form the hnRNP-rich complex involved in splicing inhibition. It is also essential for the cystic fibrosis transmembrane conductance regulator (CFTR) exon 9-skipping activity
DLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDPKTGRSKGFGFVRFASYETQVKVLSQRHMIDGRWCD
VKLP
>gnl|CDD|409761 cd12322, RRM2_TDP43, RNA recognition motif 2 (RRM2) found in TAR DNA-binding protein 43 (TDP-43) and similar proteins. This subfamily corresponds to the RRM2 of TDP-43 (also termed TARDBP), a ubiquitously expressed pathogenic protein whose normal function and abnormal aggregation are directly linked to the genetic disease cystic fibrosis, and two neurodegenerative disorders: frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). TDP-43 binds both DNA and RNA, and has been implicated in transcriptional repression, pre-mRNA splicing and translational regulation. TDP-43 is a dimeric protein with two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal glycine-rich domain. The RRMs are responsible for DNA and RNA binding; they bind to TAR DNA and RNA sequences with UG-repeats. The glycine-rich domain can interact with the hnRNP family proteins to form the hnRNP-rich complex involved in splicing inhibition. It is also essential for the cystic fibrosis transmembrane conductance regulator (CFTR) exon 9-skipping activity
RKVFVGRCTEDMTEDDLRQYFSQFGEVTDVFIPKPFRAFAFVTFADDEVAQSLCGEDHIIKGVSVHISNA
E
>gnl|CDD|240769 cd12323, RRM2_MSI, RNA recognition motif 2 (RRM2) found in RNA-binding protein Musashi homologs Musashi-1, Musashi-2 and similar proteins. This subfamily corresponds to the RRM2.in Musashi-1 (also termed Msi1), a neural RNA-binding protein putatively expressed in central nervous system (CNS) stem cells and neural progenitor cells, and associated with asymmetric divisions in neural progenitor cells. It is evolutionarily conserved from invertebrates to vertebrates. Musashi-1 is a homolog of Drosophila Musashi and Xenopus laevis nervous system-specific RNP protein-1 (Nrp-1). It has been implicated in the maintenance of the stem-cell state, differentiation, and tumorigenesis. It translationally regulates the expression of a mammalian numb gene by binding to the 3'-untranslated region of mRNA of Numb, encoding a membrane-associated inhibitor of Notch signaling, and further influences neural development. Moreover, Musashi-1 represses translation by interacting with the poly(A)-binding protein and competes for binding of the eukaryotic initiation factor-4G (eIF-4G). Musashi-2 (also termed Msi2) has been identified as a regulator of the hematopoietic stem cell (HSC) compartment and of leukemic stem cells after transplantation of cells with loss and gain of function of the gene. It influences proliferation and differentiation of HSCs and myeloid progenitors, and further modulates normal hematopoiesis and promotes aggressive myeloid leukemia. Both, Musashi-1 and Musashi-2, contain two conserved N-terminal tandem RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), along with other domains of unknown function
KIFVGGLSANTTEDDVKKYFSQFGKVEDAMLMFDKQTNRHRGFGFVTFESEDVVDKVCEIHFHEINNKMV
ECKK
>gnl|CDD|409762 cd12324, RRM_RBM8, RNA recognition motif (RRM) found in RNA-binding protein RBM8A, RBM8B nd similar proteins. This subfamily corresponds to the RRM of RBM8, also termed binder of OVCA1-1 (BOV-1), or RNA-binding protein Y14, which is one of the components of the exon-exon junction complex (EJC). It has two isoforms, RBM8A and RBM8B, both of which are identical except that RBM8B is 16 amino acids shorter at its N-terminus. RBM8, together with other EJC components (such as Magoh, Aly/REF, RNPS1, Srm160, and Upf3), plays critical roles in postsplicing processing, including nuclear export and cytoplasmic localization of the mRNA, and the nonsense-mediated mRNA decay (NMD) surveillance process. RBM8 binds to mRNA 20-24 nucleotides upstream of a spliced exon-exon junction. It is also involved in spliced mRNA nuclear export, and the process of nonsense-mediated decay of mRNAs with premature stop codons. RBM8 forms a specific heterodimer complex with the EJC protein Magoh which then associates with Aly/REF, RNPS1, DEK, and SRm160 on the spliced mRNA, and inhibits ATP turnover by eIF4AIII, thereby trapping the EJC core onto RNA. RBM8 contains an N-terminal putative bipartite nuclear localization signal, one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), in the central region, and a C-terminal serine-arginine rich region (SR domain) and glycine-arginine rich region (RG domain)
QRSVEGWIIFVTGVHEEAQEEDIHDKFAEFGEIKNLHLNLDRRTGFVKGYALVEYETKKEAQAAIEGLNG
KELLGQTISVDWAFVKGP
>gnl|CDD|409763 cd12325, RRM1_hnRNPA_hnRNPD_like, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein hnRNP A and hnRNP D subfamilies and similar proteins. This subfamily corresponds to the RRM1 in the hnRNP A subfamily which includes hnRNP A0, hnRNP A1, hnRNP A2/B1, hnRNP A3 and similar proteins. hnRNP A0 is a low abundance hnRNP protein that has been implicated in mRNA stability in mammalian cells. hnRNP A1 is an abundant eukaryotic nuclear RNA-binding protein that may modulate splice site selection in pre-mRNA splicing. hnRNP A2/B1 is an RNA trafficking response element-binding protein that interacts with the hnRNP A2 response element (A2RE). hnRNP A3 is also a RNA trafficking response element-binding protein that participates in the trafficking of A2RE-containing RNA. The hnRNP A subfamily is characterized by two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a long glycine-rich region at the C-terminus. The hnRNP D subfamily includes hnRNP D0, hnRNP A/B, hnRNP DL and similar proteins. hnRNP D0 is a UUAG-specific nuclear RNA binding protein that may be involved in pre-mRNA splicing and telomere elongation. hnRNP A/B is an RNA unwinding protein with a high affinity for G- followed by U-rich regions. hnRNP A/B has also been identified as an APOBEC1-binding protein that interacts with apolipoprotein B (apoB) mRNA transcripts around the editing site and thus, plays an important role in apoB mRNA editing. hnRNP DL (or hnRNP D-like) is a dual functional protein that possesses DNA- and RNA-binding properties. It has been implicated in mRNA biogenesis at the transcriptional and post-transcriptional levels. All members in this subfamily contain two putative RRMs and a glycine- and tyrosine-rich C-terminus. The family also contains DAZAP1 (Deleted in azoospermia-associated protein 1), RNA-binding protein Musashi homolog Musashi-1, Musashi-2 and similar proteins. They all harbor two RRMs
LFVGGLSWETTEESLREYFSKYGEVVDCVVMKDPATGRSRGFGFVTFKDPSSVDAVLAARPHTLDGRTID
PK
>gnl|CDD|409764 cd12326, RRM1_hnRNPA0, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein A0 (hnRNP A0) and similar proteins. This subfamily corresponds to the RRM1 of hnRNP A0 which is a low abundance hnRNP protein that has been implicated in mRNA stability in mammalian cells. It has been identified as the substrate for MAPKAP-K2 and may be involved in the lipopolysaccharide (LPS)-induced post-transcriptional regulation of tumor necrosis factor-alpha (TNF-alpha), cyclooxygenase 2 (COX-2) and macrophage inflammatory protein 2 (MIP-2). hnRNP A0 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a long glycine-rich region at the C-terminus
QLCKLFIGGLNVQTTEEGLRAHFEAYGQLTDCVVVVNPQTKRSRCFGFVTYSSAEEADAAMAAAPHVVDG
NNVELKRAV
>gnl|CDD|409765 cd12327, RRM2_DAZAP1, RNA recognition motif 2 (RRM2) found in Deleted in azoospermia-associated protein 1 (DAZAP1) and similar proteins. This subfamily corresponds to the RRM2 of DAZAP1 or DAZ-associated protein 1, also termed proline-rich RNA binding protein (Prrp), a multi-functional ubiquitous RNA-binding protein expressed most abundantly in the testis and essential for normal cell growth, development, and spermatogenesis. DAZAP1 is a shuttling protein whose acetylated is predominantly nuclear and the nonacetylated form is in cytoplasm. DAZAP1 also functions as a translational regulator that activates translation in an mRNA-specific manner. DAZAP1 was initially identified as a binding partner of Deleted in Azoospermia (DAZ). It also interacts with numerous hnRNPs, including hnRNP U, hnRNP U like-1, hnRNPA1, hnRNPA/B, and hnRNP D, suggesting DAZAP1 might associate and cooperate with hnRNP particles to regulate adenylate-uridylate-rich elements (AU-rich element or ARE)-containing mRNAs. DAZAP1 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal proline-rich domain
KSKKVFVGGIPHNCGETELRDYFKRYGVVTEVVMMYDAEKQRSRGFGFITFEDEQSVDQAVNMHFHDIMG
KKVEVKRAEP
>gnl|CDD|409766 cd12328, RRM2_hnRNPA_like, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein A subfamily. This subfamily corresponds to the RRM2 of hnRNP A0, hnRNP A1, hnRNP A2/B1, hnRNP A3 and similar proteins. hnRNP A0 is a low abundance hnRNP protein that has been implicated in mRNA stability in mammalian cells. It has been identified as the substrate for MAPKAP-K2 and may be involved in the lipopolysaccharide (LPS)-induced post-transcriptional regulation of tumor necrosis factor-alpha (TNF-alpha), cyclooxygenase 2 (COX-2) and macrophage inflammatory protein 2 (MIP-2). hnRNP A1 is an abundant eukaryotic nuclear RNA-binding protein that may modulate splice site selection in pre-mRNA splicing. hnRNP A2/B1 is an RNA trafficking response element-binding protein that interacts with the hnRNP A2 response element (A2RE). Many mRNAs, such as myelin basic protein (MBP), myelin-associated oligodendrocytic basic protein (MOBP), carboxyanhydrase II (CAII), microtubule-associated protein tau, and amyloid precursor protein (APP) are trafficked by hnRNP A2/B1. hnRNP A3 is also a RNA trafficking response element-binding protein that participates in the trafficking of A2RE-containing RNA. The hnRNP A subfamily is characterized by two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a long glycine-rich region at the C-terminus
KLFVGGLKEDVEEEDLREYFSQFGKVESVEIVTDKETGKKRGFAFVTFDDHDSVDKIVLQKYHTINGHRC
EVK
>gnl|CDD|240775 cd12329, RRM2_hnRNPD_like, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein hnRNP D0, hnRNP A/B, hnRNP DL and similar proteins. This subfamily corresponds to the RRM2 of hnRNP D0, hnRNP A/B, hnRNP DL and similar proteins. hnRNP D0, a UUAG-specific nuclear RNA binding protein that may be involved in pre-mRNA splicing and telomere elongation. hnRNP A/B is an RNA unwinding protein with a high affinity for G- followed by U-rich regions. It has also been identified as an APOBEC1-binding protein that interacts with apolipoprotein B (apoB) mRNA transcripts around the editing site and thus plays an important role in apoB mRNA editing. hnRNP DL (or hnRNP D-like) is a dual functional protein that possesses DNA- and RNA-binding properties. It has been implicated in mRNA biogenesis at the transcriptional and post-transcriptional levels. All memembers in this family contain two putative RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a glycine- and tyrosine-rich C-terminus
KIFVGGLSPETTEEKIREYFGKFGNIVEIELPMDKKTNKRRGFCFITFDSEEPVKKILETQFHVIGGKKV
EVKKA
>gnl|CDD|409767 cd12330, RRM2_Hrp1p, RNA recognition motif 2 (RRM2) found in yeast nuclear polyadenylated RNA-binding protein 4 (Hrp1p or Nab4p) and similar proteins. This subfamily corresponds to the RRM1 of Hrp1p and similar proteins. Hrp1p or Nab4p, also termed cleavage factor IB (CFIB), is a sequence-specific trans-acting factor that is essential for mRNA 3'-end formation in yeast Saccharomyces cerevisiae. It can be UV cross-linked to RNA and specifically recognizes the (UA)6 RNA element required for both, the cleavage and poly(A) addition steps. Moreover, Hrp1p can shuttle between the nucleus and the cytoplasm, and play an additional role in the export of mRNAs to the cytoplasm. Hrp1p also interacts with Rna15p and Rna14p, two components of CF1A. In addition, Hrp1p functions as a factor directly involved in modulating the activity of the nonsense-mediated mRNA decay (NMD) pathway; it binds specifically to a downstream sequence element (DSE)-containing RNA and interacts with Upf1p, a component of the surveillance complex, further triggering the NMD pathway. Hrp1p contains two central RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and an arginine-glycine-rich region harboring repeats of the sequence RGGF/Y
KIFVGGLAPDVTEEEFKEYFEQFGTVVDAVVMLDHDTGRSRGFGFVTFDSESAVEKVLSKGFHELGGKKV
EVKRATPK
>gnl|CDD|409768 cd12331, RRM_NRD1_SEB1_like, RNA recognition motif (RRM) found in Saccharomyces cerevisiae protein Nrd1, Schizosaccharomyces pombe Rpb7-binding protein seb1 and similar proteins. This subfamily corresponds to the RRM of Nrd1 and Seb1. Nrd1 is a novel heterogeneous nuclear ribonucleoprotein (hnRNP)-like RNA-binding protein encoded by gene NRD1 (for nuclear pre-mRNA down-regulation) from yeast S. cerevisiae. It is implicated in 3' end formation of small nucleolar and small nuclear RNAs transcribed by polymerase II, and plays a critical role in pre-mRNA metabolism. Nrd1 contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a short arginine-, serine-, and glutamate-rich segment similar to the regions rich in RE and RS dipeptides (RE/RS domains) in many metazoan splicing factors, and a proline- and glutamine-rich C-terminal domain (P+Q domain) similar to domains found in several yeast hnRNPs. Disruption of NRD1 gene is lethal to yeast cells. Its N-terminal domain is sufficient for viability, which may facilitate interactions with RNA polymerase II where Nrd1 may function as an auxiliary factor. By contrast, the RRM, RE/RS domains, and P+Q domain are dispensable. Seb1 is an RNA-binding protein encoded by gene seb1 (for seven binding) from fission yeast S. pombe. It is essential for cell viability and bound directly to Rpb7 subunit of RNA polymerase II. Seb1 is involved in processing of polymerase II transcripts. It also contains one RRM motif and a region rich in arginine-serine dipeptides (RS domain)
VYSRTLFIGGVTLNMKEWDLRSVFKRFGEVQSVILNNSRRHAFVKMYSRHEAENALQAMEKVPDGDLPLR
TRWGVGFGP
>gnl|CDD|409769 cd12332, RRM1_p54nrb_like, RNA recognition motif 1 (RRM1) found in the p54nrb/PSF/PSP1 family. This subfamily corresponds to the RRM1 of the p54nrb/PSF/PSP1 family, including 54 kDa nuclear RNA- and DNA-binding protein (p54nrb or NonO or NMT55), polypyrimidine tract-binding protein (PTB)-associated-splicing factor (PSF or POMp100), paraspeckle protein 1 (PSP1 or PSPC1), which are ubiquitously expressed and are conserved in vertebrates. p54nrb is a multi-functional protein involved in numerous nuclear processes including transcriptional regulation, splicing, DNA unwinding, nuclear retention of hyperedited double-stranded RNA, viral RNA processing, control of cell proliferation, and circadian rhythm maintenance. PSF is also a multi-functional protein that binds RNA, single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and many factors, and mediates diverse activities in the cell. PSP1 is a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm. The cellular function of PSP1 remains unknown currently. This subfamily also includes some p54nrb/PSF/PSP1 homologs from invertebrate species, such as the Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA) and Chironomus tentans hrp65 gene encoding protein Hrp65. D. melanogaster NONA is involved in eye development and behavior, and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans Hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore. All family members contain a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction module. PSF has an additional large N-terminal domain that differentiates it from other family members
RCRLFVGNLPNDITEEEFKELFQKYGEVSEVFLNKGKGFGFIRLDTRANAEAAKAELDGTPRKGRQLRVR
F
>gnl|CDD|409770 cd12333, RRM2_p54nrb_like, RNA recognition motif 2 (RRM2) found in the p54nrb/PSF/PSP1 family. This subfamily corresponds to the RRM2 of the p54nrb/PSF/PSP1 family, including 54 kDa nuclear RNA- and DNA-binding protein (p54nrb or NonO or NMT55), polypyrimidine tract-binding protein (PTB)-associated-splicing factor (PSF or POMp100), paraspeckle protein 1 (PSP1 or PSPC1), which are ubiquitously expressed and are conserved in vertebrates. p54nrb is a multi-functional protein involved in numerous nuclear processes including transcriptional regulation, splicing, DNA unwinding, nuclear retention of hyperedited double-stranded RNA, viral RNA processing, control of cell proliferation, and circadian rhythm maintenance. PSF is also a multi-functional protein that binds RNA, single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and many factors, and mediates diverse activities in the cell. PSP1 is a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm. The cellular function of PSP1 remains unknown currently. The family also includes some p54nrb/PSF/PSP1 homologs from invertebrate species, such as the Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA) and Chironomus tentans hrp65 gene encoding protein Hrp65. D. melanogaster NONA is involved in eye development and behavior and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans Hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore. All family members contains a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction module. PSF has an additional large N-terminal domain that differentiates it from other family members
ALRVKNLSPYVSNELLEQAFSQFGDVERAVVIVDDRGRSTGEGIVEFSRKPGAQAALKRCSEGCFLLTAS
PRPVIVEPLE
>gnl|CDD|409771 cd12334, RRM1_SF3B4, RNA recognition motif 1 (RRM1) found in splicing factor 3B subunit 4 (SF3B4) and similar proteins. This subfamily corresponds to the RRM1 of SF3B4, also termed pre-mRNA-splicing factor SF3b 49 kDa (SF3b50), or spliceosome-associated protein 49 (SAP 49). SF3B4 a component of the multiprotein complex splicing factor 3b (SF3B), an integral part of the U2 small nuclear ribonucleoprotein (snRNP) and the U11/U12 di-snRNP. SF3B is essential for the accurate excision of introns from pre-messenger RNA, and is involved in the recognition of the pre-mRNA's branch site within the major and minor spliceosomes. SF3B4 functions to tether U2 snRNP with pre-mRNA at the branch site during spliceosome assembly. It is an evolutionarily highly conserved protein with orthologs across diverse species. SF3B4 contains two closely adjacent N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). It binds directly to pre-mRNA and also interacts directly and highly specifically with another SF3B subunit called SAP 145
VYVGNLDEKVTEELLWELFIQAGPVVNVHMPKDRVTQQHQGYGFVEFLSEEDADYAIKIMNMIKLYGKPI
RVNK
>gnl|CDD|409772 cd12335, RRM2_SF3B4, RNA recognition motif 2 (RRM2) found in splicing factor 3B subunit 4 (SF3B4) and similar proteins. This subfamily corresponds to the RRM2 of SF3B4, also termed pre-mRNA-splicing factor SF3b 49 kDa (SF3b50), or spliceosome-associated protein 49 (SAP 49). SF3B4 is a component of the multiprotein complex splicing factor 3b (SF3B), an integral part of the U2 small nuclear ribonucleoprotein (snRNP) and the U11/U12 di-snRNP. SF3B is essential for the accurate excision of introns from pre-messenger RNA, and is involved in the recognition of the pre-mRNA's branch site within the major and minor spliceosomes. SF3B4 functions to tether U2 snRNP with pre-mRNA at the branch site during spliceosome assembly. It is an evolutionarily highly conserved protein with orthologs across diverse species. SF3B4 contains two closely adjacent N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). It binds directly to pre-mRNA and also interacts directly and highly specifically with another SF3B subunit called SAP 145
GANLFIGNLDPEVDEKLLYDTFSAFGVILQTPKIMRDPDTGNSKGFGFVSFDSFEASDAAIEAMNGQYLC
NRPITVSYAFKKD
>gnl|CDD|409773 cd12336, RRM_RBM7_like, RNA recognition motif (RRM) found in RNA-binding protein 7 (RBM7) and similar proteins. This subfamily corresponds to the RRM of RBM7, RBM11 and their eukaryotic homologous. RBM7 is an ubiquitously expressed pre-mRNA splicing factor that enhances messenger RNA (mRNA) splicing in a cell-specific manner or in a certain developmental process, such as spermatogenesis. It interacts with splicing factors SAP145 (the spliceosomal splicing factor 3b subunit 2) and SRp20, and may play a more specific role in meiosis entry and progression. Together with additional testis-specific RNA-binding proteins, RBM7 may regulate the splicing of specific pre-mRNA species that are important in the meiotic cell cycle. RBM11 is a novel tissue-specific splicing regulator that is selectively expressed in brain, cerebellum and testis, and to a lower extent in kidney. It is localized in the nucleoplasm and enriched in SRSF2-containing splicing speckles. It may play a role in the modulation of alternative splicing during neuron and germ cell differentiation. Both, RBM7 and RBM11, contain an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a region lacking known homology at the C-terminus. The RRM is responsible for RNA binding, whereas the C-terminal region permits nuclear localization and homodimerization
DRTLFVGNLDPRVTEEILYELFLQAGPLEGVKIPKDPNGKPKNFAFVTFKHEVSVPYAIQLLNGIRLFGR
EIRIK
>gnl|CDD|409774 cd12337, RRM1_SRSF4_like, RNA recognition motif 1 (RRM1) found in serine/arginine-rich splicing factor 4 (SRSF4) and similar proteins. This subfamily corresponds to the RRM1 in three serine/arginine (SR) proteins: serine/arginine-rich splicing factor 4 (SRSF4 or SRp75 or SFRS4), serine/arginine-rich splicing factor 5 (SRSF5 or SRp40 or SFRS5 or HRS), serine/arginine-rich splicing factor 6 (SRSF6 or SRp55). SRSF4 plays an important role in both, constitutive and alternative, splicing of many pre-mRNAs. It can shuttle between the nucleus and cytoplasm. SRSF5 regulates both alternative splicing and basal splicing. It is the only SR protein efficiently selected from nuclear extracts (NE) by the splicing enhancer (ESE) and essential for enhancer activation. SRSF6 preferentially interacts with a number of purine-rich splicing enhancers (ESEs) to activate splicing of the ESE-containing exon. It is the only protein from HeLa nuclear extract or purified SR proteins that specifically binds B element RNA after UV irradiation. SRSF6 may also recognize different types of RNA sites. Members in this family contain two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a C-terminal RS domains rich in serine-arginine dipeptides
RVYIGRLPYRARERDVERFFRGYGRIRDINLKNGFGFVEFEDPRDADDAVYELNGKELCGERVIVEHARG
>gnl|CDD|409775 cd12338, RRM1_SRSF1_like, RNA recognition motif 1 (RRM1) found in serine/arginine-rich splicing factor 1 (SRSF1) and similar proteins. This subgroup corresponds to the RRM1 in three serine/arginine (SR) proteins: serine/arginine-rich splicing factor 1 (SRSF1 or ASF-1), serine/arginine-rich splicing factor 9 (SRSF9 or SRp30C), and plant pre-mRNA-splicing factor SF2 (SR1). SRSF1 is a shuttling SR protein involved in constitutive and alternative splicing, nonsense-mediated mRNA decay (NMD), mRNA export and translation. It also functions as a splicing-factor oncoprotein that regulates apoptosis and proliferation to promote mammary epithelial cell transformation. SRSF9 has been implicated in the activity of many elements that control splice site selection, the alternative splicing of the glucocorticoid receptor beta in neutrophils and in the gonadotropin-releasing hormone pre-mRNA. It can also interact with other proteins implicated in alternative splicing, including YB-1, rSLM-1, rSLM-2, E4-ORF4, Nop30, and p32. Both, SRSF1 and SRSF9, contain two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal RS domains rich in serine-arginine dipeptides. In contrast, SF2 contains two N-terminal RRMs and a C-terminal PSK domain rich in proline, serine and lysine residues
RIYVGNLPGDIRERDIEDLFYKYGPILAIDLKNRRRGPPFAFVEFEDPRDAEDAIRGRDGYDFDGYRLRV
EF
>gnl|CDD|409776 cd12339, RRM2_SRSF1_4_like, RNA recognition motif 2 (RRM2) found in serine/arginine-rich splicing factor SRSF1, SRSF4 and similar proteins. This subfamily corresponds to the RRM2 of several serine/arginine (SR) proteins that have been classified into two subgroups. The first subgroup consists of serine/arginine-rich splicing factor 4 (SRSF4 or SRp75 or SFRS4), serine/arginine-rich splicing factor 5 (SRSF5 or SRp40 or SFRS5 or HRS) and serine/arginine-rich splicing factor 6 (SRSF6 or SRp55). The second subgroup is composed of serine/arginine-rich splicing factor 1 (SRSF1 or ASF-1), serine/arginine-rich splicing factor 9 (SRSF9 or SRp30C) and plant pre-mRNA-splicing factor SF2 (SR1). These SR proteins are mainly involved in regulating constitutive and alternative pre-mRNA splicing. They also have been implicated in transcription, genomic stability, mRNA export and translation. All SR proteins in this family, except SRSF5, undergo nucleocytoplasmic shuttling, suggesting their widespread roles in gene expression. These SR proteins share a common domain architecture comprising two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a C-terminal RS domains rich in serine-arginine dipeptides. Both domains can directly contact with RNA. The RRMs appear to determine the binding specificity and the SR domain also mediates protein-protein interactions. In addition, this subfamily includes the yeast nucleolar protein 3 (Npl3p), also termed mitochondrial targeting suppressor 1 protein, or nuclear polyadenylated RNA-binding protein 1. It is a major yeast RNA-binding protein that competes with 3'-end processing factors, such as Rna15, for binding to the nascent RNA, protecting the transcript from premature termination and coordinating transcription termination and the packaging of the fully processed transcript for export. It specifically recognizes a class of G/U-rich RNAs. Npl3p is a multi-domain protein with two RRMs, separated by a short linker and a C-terminal domain rich in glycine, arginine and serine residues
FRVVVSNLPERASWQDLKDFMRKAGEVTYADVHRDREGEGVVEFTSEEDMKRAIEKLDGTEFNGRRIRVE
>gnl|CDD|409777 cd12340, RBD_RRM1_NPL3, RNA recognition motif 1 (RRM1) found in yeast nucleolar protein 3 (Npl3p) and similar proteins. This subfamily corresponds to the RRM1 of Npl3p, also termed mitochondrial targeting suppressor 1 protein, or nuclear polyadenylated RNA-binding protein 1. Npl3p is a major yeast RNA-binding protein that competes with 3'-end processing factors, such as Rna15, for binding to the nascent RNA, protecting the transcript from premature termination and coordinating transcription termination and the packaging of the fully processed transcript for export. It specifically recognizes a class of G/U-rich RNAs. Npl3p is a multi-domain protein containing two central RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), separated by a short linker and a C-terminal domain rich in glycine, arginine and serine residues
RLFVRPFPPDTSESAIREIFSPYGPVKEVKMLSDSNFAFVEFEELEDAIRAKDSVHGRVLNNEPLYVTY
>gnl|CDD|409778 cd12341, RRM_hnRNPC_like, RNA recognition motif (RRM) found in heterogeneous nuclear ribonucleoprotein C (hnRNP C)-related proteins. This subfamily corresponds to the RRM in the hnRNP C-related protein family, including hnRNP C proteins, Raly, and Raly-like protein (RALYL). hnRNP C proteins, C1 and C2, are produced by a single coding sequence. They are the major constituents of the heterogeneous nuclear RNA (hnRNA) ribonucleoprotein (hnRNP) complex in vertebrates. They bind hnRNA tightly, suggesting a central role in the formation of the ubiquitous hnRNP complex; they are involved in the packaging of the hnRNA in the nucleus and in processing of pre-mRNA such as splicing and 3'-end formation. Raly, also termed autoantigen p542, is an RNA-binding protein that may play a critical role in embryonic development. The biological role of RALYL remains unclear. It shows high sequence homology with hnRNP C proteins and Raly. Members of this family are characterized by an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal auxiliary domain. The Raly proteins contain a glycine/serine-rich stretch within the C-terminal regions, which is absent in the hnRNP C proteins. Thus, the Raly proteins represent a newly identified class of evolutionarily conserved autoepitopes
SRIFVGNLPTDQMTKEDLEEIFSKYGKILGISLHKGYGFVQFDNEEDARAAVAGENGRTIKGQRLDIN
>gnl|CDD|240788 cd12342, RRM_Nab3p, RNA recognition motif (RRM) found in yeast nuclear polyadenylated RNA-binding protein 3 (Nab3p) and similar proteins. This subfamily corresponds to the RRM of Nab3p, an acidic nuclear polyadenylated RNA-binding protein encoded by Saccharomyces cerevisiae NAB3 gene that is essential for cell viability. Nab3p is predominantly localized within the nucleoplasm and essential for growth in yeast. It may play an important role in packaging pre-mRNAs into ribonucleoprotein structures amenable to efficient nuclear RNA processing. Nab3p contains an N-terminal aspartic/glutamic acid-rich region, a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal region rich in glutamine and proline residues
RLFIGNLPTKRVSKEDLFRIFSPYGHLMQIVIKNAFGFVQFDSPQSCRNAIECEQGEMNRGKKLHLEVSK
S
>gnl|CDD|409779 cd12343, RRM1_2_CoAA_like, RNA recognition motif 1 (RRM1) and 2 (RRM2) found in RRM-containing coactivator activator/modulator (CoAA) and similar proteins. This subfamily corresponds to the RRM in CoAA (also known as RBM14 or PSP2) and RNA-binding protein 4 (RBM4). CoAA is a heterogeneous nuclear ribonucleoprotein (hnRNP)-like protein identified as a nuclear receptor coactivator. It mediates transcriptional coactivation and RNA splicing effects in a promoter-preferential manner, and is enhanced by thyroid hormone receptor-binding protein (TRBP). CoAA contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a TRBP-interacting domain. RBM4 is a ubiquitously expressed splicing factor with two isoforms, RBM4A (also known as Lark homolog) and RBM4B (also known as RBM30), which are very similar in structure and sequence. RBM4 may also function as a translational regulator of stress-associated mRNAs as well as play a role in micro-RNA-mediated gene regulation. RBM4 contains two N-terminal RRMs, a CCHC-type zinc finger, and three alanine-rich regions within their C-terminal regions. This family also includes Drosophila RNA-binding protein lark (Dlark), a homolog of human RBM4. It plays an important role in embryonic development and in the circadian regulation of adult eclosion. Dlark shares high sequence similarity with RBM4 at the N-terminal region. However, Dlark has three proline-rich segments instead of three alanine-rich segments within the C-terminal region
KIFVGNLPDAATSEELRALFEKYGKVTECDIVKNYAFVHMEKEEDAEDAIKALNGYEFMGSRINVE
>gnl|CDD|409780 cd12344, RRM1_SECp43_like, RNA recognition motif 1 (RRM1) found in tRNA selenocysteine-associated protein 1 (SECp43) and similar proteins. This subfamily corresponds to the RRM1 in tRNA selenocysteine-associated protein 1 (SECp43), yeast negative growth regulatory protein NGR1 (RBP1), yeast protein NAM8, and similar proteins. SECp43 is an RNA-binding protein associated specifically with eukaryotic selenocysteine tRNA [tRNA(Sec)]. It may play an adaptor role in the mechanism of selenocysteine insertion. SECp43 is located primarily in the nucleus and contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal polar/acidic region. Yeast proteins, NGR1 and NAM8, show high sequence similarity with SECp43. NGR1 is a putative glucose-repressible protein that binds both RNA and single-stranded DNA (ssDNA). It may function in regulating cell growth in early log phase, possibly through its participation in RNA metabolism. NGR1 contains three RRMs, two of which are followed by a glutamine-rich stretch that may be involved in transcriptional activity. In addition, NGR1 has an asparagine-rich region near the C-terminus which also harbors a methionine-rich region. NAM8 is a putative RNA-binding protein that acts as a suppressor of mitochondrial splicing deficiencies when overexpressed in yeast. It may be a non-essential component of the mitochondrial splicing machinery. NAM8 also contains three RRMs
TLWMGDLEPWMDEAYISSCFAKTGEEVVSVKIIRNKQTGKSAGYCFVEFATQEAAEQALEHLNGKPIPNT
QQRFRLNWASFS
>gnl|CDD|409781 cd12345, RRM2_SECp43_like, RNA recognition motif 2 (RRM2) found in tRNA selenocysteine-associated protein 1 (SECp43) and similar proteins. This subfamily corresponds to the RRM2 in tRNA selenocysteine-associated protein 1 (SECp43), yeast negative growth regulatory protein NGR1 (RBP1), yeast protein NAM8, and similar proteins. SECp43 is an RNA-binding protein associated specifically with eukaryotic selenocysteine tRNA [tRNA(Sec)]. It may play an adaptor role in the mechanism of selenocysteine insertion. SECp43 is located primarily in the nucleus and contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal polar/acidic region. Yeast proteins, NGR1 and NAM8, show high sequence similarity with SECp43. NGR1 is a putative glucose-repressible protein that binds both RNA and single-stranded DNA (ssDNA). It may function in regulating cell growth in early log phase, possibly through its participation in RNA metabolism. NGR1 contains three RRMs, two of which are followed by a glutamine-rich stretch that may be involved in transcriptional activity. In addition, NGR1 has an asparagine-rich region near the C-terminus which also harbors a methionine-rich region. NAM8 is a putative RNA-binding protein that acts as a suppressor of mitochondrial splicing deficiencies when overexpressed in yeast. It may be a non-essential component of the mitochondrial splicing machinery. NAM8 also contains three RRMs
EHSLFVGDLAPDVTDYQLYETFSARYPSVRGAKVVMDPVTGRSKGYGFVRFGDESEQDRALTEMQGVYLG
SRPIRVSPAT
>gnl|CDD|409782 cd12346, RRM3_NGR1_NAM8_like, RNA recognition motif 3 (RRM3) found in yeast negative growth regulatory protein NGR1 (RBP1), yeast protein NAM8 and similar proteins. This subfamily corresponds to the RRM3 of NGR1 and NAM8. NGR1, also termed RNA-binding protein RBP1, is a putative glucose-repressible protein that binds both RNA and single-stranded DNA (ssDNA) in yeast. It may function in regulating cell growth in early log phase, possibly through its participation in RNA metabolism. NGR1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a glutamine-rich stretch that may be involved in transcriptional activity. In addition, NGR1 has an asparagine-rich region near the carboxyl terminus which also harbors a methionine-rich region. The family also includes protein NAM8, which is a putative RNA-binding protein that acts as a suppressor of mitochondrial splicing deficiencies when overexpressed in yeast. It may be a non-essential component of the mitochondrial splicing machinery. Like NGR1, NAM8 contains two RRMs
NTTVFVGGLDPNVTEEDLRVLFGPFGEIVYVKIPPGKGCGFVQFVNRASAEAAIQKLQGTPIGGSRIRLS
WG
>gnl|CDD|409783 cd12347, RRM_PPIE, RNA recognition motif (RRM) found in cyclophilin-33 (Cyp33) and similar proteins. This subfamily corresponds to the RRM of Cyp33, also termed peptidyl-prolyl cis-trans isomerase E (PPIase E), or cyclophilin E, or rotamase E. Cyp33 is a nuclear RNA-binding cyclophilin with an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal PPIase domain. Cyp33 possesses RNA-binding activity and preferentially binds to polyribonucleotide polyA and polyU, but hardly to polyG and polyC. It binds specifically to mRNA, which can stimulate its PPIase activity. Moreover, Cyp33 interacts with the third plant homeodomain (PHD3) zinc finger cassette of the mixed lineage leukemia (MLL) proto-oncoprotein and a poly-A RNA sequence through its RRM domain. It further mediates downregulation of the expression of MLL target genes HOXC8, HOXA9, CDKN1B, and C-MYC, in a proline isomerase-dependent manner. Cyp33 also possesses a PPIase activity that catalyzes cis-trans isomerization of the peptide bond preceding a proline, which has been implicated in the stimulation of folding and conformational changes in folded and unfolded proteins. The PPIase activity can be inhibited by the immunosuppressive drug cyclosporin A
LYVGGLAEEVDEKVLHAAFIPFGDIVDIQIPLDYETEKHRGFAFVEFEEAEDAAAAIDNMNESELFGRTI
RVNLA
>gnl|CDD|409784 cd12348, RRM1_SHARP, RNA recognition motif 1 (RRM1) found in SMART/HDAC1-associated repressor protein (SHARP) and similar proteins. This subfamily corresponds to the RRM1 of SHARP, also termed Msx2-interacting protein (MINT), or SPEN homolog, an estrogen-inducible transcriptional repressor that interacts directly with the nuclear receptor corepressor SMRT, histone deacetylases (HDACs) and components of the NuRD complex. SHARP recruits HDAC activity and binds to the steroid receptor RNA coactivator SRA through four conserved N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), further suppressing SRA-potentiated steroid receptor transcription activity. Thus, SHARP has the capacity to modulate both liganded and nonliganded nuclear receptors. SHARP also has been identified as a component of transcriptional repression complexes in Notch/RBP-Jkappa signaling pathways. In addition to the N-terminal RRMs, SHARP possesses a C-terminal SPOC domain (Spen paralog and ortholog C-terminal domain), which is highly conserved among Spen proteins
HLWVGNLPENVREEKIIEHFKRFGRVESVKILPKRGSEGGVAAFVDFVDIKSAQKAHSAVNKMGGRDLRT
DYNEP
>gnl|CDD|409785 cd12349, RRM2_SHARP, RNA recognition motif 2 (RRM2) found in SMART/HDAC1-associated repressor protein (SHARP) and similar proteins. This subfamily corresponds to the RRM2 of SHARP, also termed Msx2-interacting protein (MINT), or SPEN homolog, an estrogen-inducible transcriptional repressor that interacts directly with the nuclear receptor corepressor SMRT, histone deacetylases (HDACs) and components of the NuRD complex. SHARP recruits HDAC activity and binds to the steroid receptor RNA coactivator SRA through four conserved N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), further suppressing SRA-potentiated steroid receptor transcription activity. Thus, SHARP has the capacity to modulate both liganded and nonliganded nuclear receptors. SHARP also has been identified as a component of transcriptional repression complexes in Notch/RBP-Jkappa signaling pathways. In addition to the N-terminal RRMs, SHARP possesses a C-terminal SPOC domain (Spen paralog and ortholog C-terminal domain), which is highly conserved among Spen proteins
GIKVRNLPVRSSDTSLKDGLFHEFKKHGKVTSVKVHGQGEERYAIVFFRRPEDAEKALEVSKGKLFFGMQ
IEVT
>gnl|CDD|409786 cd12350, RRM3_SHARP, RNA recognition motif 3 (RRM3) found in SMART/HDAC1-associated repressor protein (SHARP) and similar proteins. This subfamily corresponds to the RRM3 of SHARP, also termed Msx2-interacting protein (MINT), or SPEN homolog, an estrogen-inducible transcriptional repressor that interacts directly with the nuclear receptor corepressor SMRT, histone deacetylases (HDACs) and components of the NuRD complex. SHARP recruits HDAC activity and binds to the steroid receptor RNA coactivator SRA through four conserved N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), further suppressing SRA-potentiated steroid receptor transcription activity. Thus, SHARP has the capacity to modulate both liganded and nonliganded nuclear receptors. SHARP also has been identified as a component of transcriptional repression complexes in Notch/RBP-Jkappa signaling pathways. In addition to the N-terminal RRMs, SHARP possesses a C-terminal SPOC domain (Spen paralog and ortholog C-terminal domain), which is highly conserved among Spen proteins
ATRTLFIGNLEKTTTYGDLRNIFERFGEIIDIDIKKQNGNPQYAFLQYCDIASVVKAIKKMDGEYLGNNR
LKLG
>gnl|CDD|409787 cd12351, RRM4_SHARP, RNA recognition motif 4 (RRM4) found in SMART/HDAC1-associated repressor protein (SHARP) and similar proteins. This subfamily corresponds to the RRM of SHARP, also termed Msx2-interacting protein (MINT), or SPEN homolog, is an estrogen-inducible transcriptional repressor that interacts directly with the nuclear receptor corepressor SMRT, histone deacetylases (HDACs) and components of the NuRD complex. SHARP recruits HDAC activity and binds to the steroid receptor RNA coactivator SRA through four conserved N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), further suppressing SRA-potentiated steroid receptor transcription activity. Thus, SHARP has the capacity to modulate both liganded and nonliganded nuclear receptors. SHARP also has been identified as a component of transcriptional repression complexes in Notch/RBP-Jkappa signaling pathways. In addition to the N-terminal RRMs, SHARP possesses a C-terminal SPOC domain (Spen paralog and ortholog C-terminal domain), which is highly conserved among Spen proteins
FGKSMPTNCVWLDGLSENVTEQYLTRHFCRYGPVVKVVIDRQKGMALVLYDEVECAQAAVKETKGRKIGG
RKIQVDF
>gnl|CDD|409788 cd12352, RRM1_TIA1_like, RNA recognition motif 1 (RRM1) found in granule-associated RNA binding proteins p40-TIA-1 and TIAR. This subfamily corresponds to the RRM1 of nucleolysin TIA-1 isoform p40 (p40-TIA-1 or TIA-1) and nucleolysin TIA-1-related protein (TIAR), both of which are granule-associated RNA binding proteins involved in inducing apoptosis in cytotoxic lymphocyte (CTL) target cells. TIA-1 and TIAR share high sequence similarity. They are expressed in a wide variety of cell types. TIA-1 can be phosphorylated by a serine/threonine kinase that is activated during Fas-mediated apoptosis.TIAR is mainly localized in the nucleus of hematopoietic and nonhematopoietic cells. It is translocated from the nucleus to the cytoplasm in response to exogenous triggers of apoptosis. Both, TIA-1 and TIAR, bind specifically to poly(A) but not to poly(C) homopolymers. They are composed of three N-terminal highly homologous RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a glutamine-rich C-terminal auxiliary domain containing a lysosome-targeting motif. TIA-1 and TIAR interact with RNAs containing short stretches of uridylates and their RRM2 can mediate the specific binding to uridylate-rich RNAs. The C-terminal auxiliary domain may be responsible for interacting with other proteins. In addition, TIA-1 and TIAR share a potential serine protease-cleavage site (Phe-Val-Arg) localized at the junction between their RNA binding domains and their C-terminal auxiliary domains
LYVGNLDRQVTEDLILQLFSQIGPCKSCKMITEHGGNDPYCFVEFYEHNHAAAALQAMNGRKILGKEVKV
NWA
>gnl|CDD|409789 cd12353, RRM2_TIA1_like, RNA recognition motif 2 (RRM2) found in granule-associated RNA binding proteins p40-TIA-1 and TIAR. This subfamily corresponds to the RRM2 of nucleolysin TIA-1 isoform p40 (p40-TIA-1 or TIA-1) and nucleolysin TIA-1-related protein (TIAR), both of which are granule-associated RNA binding proteins involved in inducing apoptosis in cytotoxic lymphocyte (CTL) target cells. TIA-1 and TIAR share high sequence similarity. They are expressed in a wide variety of cell types. TIA-1 can be phosphorylated by a serine/threonine kinase that is activated during Fas-mediated apoptosis. TIAR is mainly localized in the nucleus of hematopoietic and nonhematopoietic cells. It is translocated from the nucleus to the cytoplasm in response to exogenous triggers of apoptosis. Both, TIA-1 and TIAR, bind specifically to poly(A) but not to poly(C) homopolymers. They are composed of three N-terminal highly homologous RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a glutamine-rich C-terminal auxiliary domain containing a lysosome-targeting motif. TIA-1 and TIAR interact with RNAs containing short stretches of uridylates and their RRM2 can mediate the specific binding to uridylate-rich RNAs. The C-terminal auxiliary domain may be responsible for interacting with other proteins. In addition, TIA-1 and TIAR share a potential serine protease-cleavage site (Phe-Val-Arg) localized at the junction between their RNA binding domains and their C-terminal auxiliary domains
HIFVGDLSPEIETEDLKEAFAPFGEISDARVVKDTQTGKSKGYGFVSFVKKEDAENAIQGMNGQWLGGRN
IRTNW
>gnl|CDD|409790 cd12354, RRM3_TIA1_like, RNA recognition motif 2 (RRM2) found in granule-associated RNA binding proteins (p40-TIA-1 and TIAR), and yeast nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1. This subfamily corresponds to the RRM3 of TIA-1, TIAR, and PUB1. Nucleolysin TIA-1 isoform p40 (p40-TIA-1 or TIA-1) and nucleolysin TIA-1-related protein (TIAR) are granule-associated RNA binding proteins involved in inducing apoptosis in cytotoxic lymphocyte (CTL) target cells. They share high sequence similarity and are expressed in a wide variety of cell types. TIA-1 can be phosphorylated by a serine/threonine kinase that is activated during Fas-mediated apoptosis.TIAR is mainly localized in the nucleus of hematopoietic and nonhematopoietic cells. It is translocated from the nucleus to the cytoplasm in response to exogenous triggers of apoptosis. Both TIA-1 and TIAR bind specifically to poly(A) but not to poly(C) homopolymers. They are composed of three N-terminal highly homologous RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a glutamine-rich C-terminal auxiliary domain containing a lysosome-targeting motif. TIA-1 and TIAR interact with RNAs containing short stretches of uridylates and their RRM2 can mediate the specific binding to uridylate-rich RNAs. The C-terminal auxiliary domain may be responsible for interacting with other proteins. In addition, TIA-1 and TIAR share a potential serine protease-cleavage site (Phe-Val-Arg) localized at the junction between their RNA binding domains and their C-terminal auxiliary domains. This subfamily also includes a yeast nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1, termed ARS consensus-binding protein ACBP-60, or poly uridylate-binding protein, or poly(U)-binding protein, which has been identified as both a heterogeneous nuclear RNA-binding protein (hnRNP) and a cytoplasmic mRNA-binding protein (mRNP). It may be stably bound to a translationally inactive subpopulation of mRNAs within the cytoplasm. PUB1 is distributed in both, the nucleus and the cytoplasm, and binds to poly(A)+ RNA (mRNA or pre-mRNA). Although it is one of the major cellular proteins cross-linked by UV light to polyadenylated RNAs in vivo, PUB1 is nonessential for cell growth in yeast. PUB1 also binds to T-rich single stranded DNA (ssDNA); however, there is no strong evidence implicating PUB1 in the mechanism of DNA replication. PUB1 contains three RRMs, and a GAR motif (glycine and arginine rich stretch) that is located between RRM2 and RRM3
TTVYVGNITKGLTEALLQQTFSPFGQILEVRVFPDKGYAFIRFDSHEAATHAIVSVNGTIINGQAVKCSW
G
>gnl|CDD|409791 cd12355, RRM_RBM18, RNA recognition motif (RRM) found in eukaryotic RNA-binding protein 18 and similar proteins. This subfamily corresponds to the RRM of RBM18, a putative RNA-binding protein containing a well-conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The biological role of RBM18 remains unclear
RLWIGNLDPRLTEYHLLKLLSKYGKIKKFDFLFHKTGPLKGQPRGYCFVTFETKEEAEKAIECLNGKLAL
GKKLVVRWAH
>gnl|CDD|409792 cd12356, RRM_PPARGC1B, RNA recognition motif (RRM) found in peroxisome proliferator-activated receptor gamma coactivator 1-beta (PGC-1-beta) and similar proteins. This subfamily corresponds to the RRM of PGC-1beta, also termed PPAR-gamma coactivator 1-beta, or PPARGC-1-beta, or PGC-1-related estrogen receptor alpha coactivator, which is one of the members of PGC-1 transcriptional coactivators family, including PGC-1alpha and PGC-1-related coactivator (PRC). PGC-1beta plays a nonredundant role in controlling mitochondrial oxidative energy metabolism and affects both, insulin sensitivity and mitochondrial biogenesis, and functions in a number of oxidative tissues. It is involved in maintaining baseline mitochondrial function and cardiac contractile function following pressure overload hypertrophy by preserving glucose metabolism and preventing oxidative stress. PGC-1beta induces hypertriglyceridemia in response to dietary fats through activating hepatic lipogenesis and lipoprotein secretion. It can stimulate apolipoprotein C3 (APOC3) expression, further mediating hypolipidemic effect of nicotinic acid. PGC-1beta also drives nuclear respiratory factor 1 (NRF-1) target gene expression and NRF-1 and estrogen related receptor alpha (ERRalpha)-dependent mitochondrial biogenesis. The modulation of the expression of PGC-1beta can trigger ERRalpha-induced adipogenesis. PGC-1beta is also a potent regulator inducing angiogenesis in skeletal muscle. The transcriptional activity of PGC-1beta can be increased through binding to host cell factor (HCF), a cellular protein involved in herpes simplex virus (HSV) infection and cell cycle regulation. PGC-1beta is a multi-domain protein containing an N-terminal activation domain, an LXXLL coactivator signature, a tetrapeptide motif (DHDY) responsible for HCF binding, two glutamic/aspartic acid-rich acidic domains, and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). In contrast to PGC-1alpha, PGC-1beta lacks most of the arginine/serine (SR)-rich domain that is responsible for the regulation of RNA processing
EKAIGEGRVVYIRNLSSSMSSNELKRRFEVFGEITECCVLSRSNRGEKYGFITYRDSEHAALSLQKGASL
RKRNEPSFQLSYGGLRHFFWTRYTDLD
>gnl|CDD|409793 cd12357, RRM_PPARGC1A_like, RNA recognition motif (RRM) found in the peroxisome proliferator-activated receptor gamma coactivator 1A (PGC-1alpha) family of regulated coactivators. This subfamily corresponds to the RRM of PGC-1alpha, PGC-1beta, and PGC-1-related coactivator (PRC), which serve as mediators between environmental or endogenous signals and the transcriptional machinery governing mitochondrial biogenesis. They play an important integrative role in the control of respiratory gene expression through interacting with a number of transcription factors, such as NRF-1, NRF-2, ERR, CREB and YY1. All family members are multi-domain proteins containing the N-terminal activation domain, an LXXLL coactivator signature, a tetrapeptide motif (DHDY) responsible for HCF binding, and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). In contrast to PGC-1alpha and PRC, PGC-1beta possesses two glutamic/aspartic acid-rich acidic domains, but lacks most of the arginine/serine (SR)-rich domain that is responsible for the regulation of RNA processing
ERRVVYVGKLEQDTTRSELRRRFEVFGEIEECTVHFRERGDKYGFVTYRYSEDAFLALENGHDLRKRNEP
MFDLSFGGRRAFCKSSYADLD
>gnl|CDD|240804 cd12358, RRM1_VICKZ, RNA recognition motif 1 (RRM1) found in the VICKZ family proteins. Thid subfamily corresponds to the RRM1 of IGF2BPs (or IMPs) found in the VICKZ family that have been implicated in the post-transcriptional regulation of several different RNAs and in subcytoplasmic localization of mRNAs during embryogenesis. IGF2BPs are composed of two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and four hnRNP K homology (KH) domains
LYIGNLSSDVNESDLRQLFEEHKIPVSSVLVKKGGYAFVDCPDQSWADKAIEKLNGKILQGKVIEVEHSV
PKK
>gnl|CDD|409794 cd12359, RRM2_VICKZ, RNA recognition motif 2 (RRM2) found in the VICKZ family proteins. This subfamily corresponds to the RRM2 of IGF-II mRNA-binding proteins (IGF2BPs or IMPs) in the VICKZ family that have been implicated in the post-transcriptional regulation of several different RNAs and in subcytoplasmic localization of mRNAs during embryogenesis. IGF2BPs are composed of two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and four hnRNP K homology (KH) domains
RKIQIRNIPPHARWEDLDSLLSTYGTVENCEQVNTKSETATVNVTYESPEQAQQAVNKLNGYQYEGSALK
VSYIPD
>gnl|CDD|409795 cd12360, RRM_cwf2, RNA recognition motif (RRM) found in yeast pre-mRNA-splicing factor Cwc2 and similar proteins. This subfamily corresponds to the RRM of yeast protein Cwc2, also termed Complexed with CEF1 protein 2, or PRP19-associated complex protein 40 (Ntc40), or synthetic lethal with CLF1 protein 3, one of the components of the Prp19-associated complex [nineteen complex (NTC)] that can bind to RNA. NTC is composed of the scaffold protein Prp19 and a number of associated splicing factors, and plays a crucial role in intron removal during premature mRNA splicing in eukaryotes. Cwc2 functions as an RNA-binding protein that can bind both small nuclear RNAs (snRNAs) and pre-mRNA in vitro. It interacts directly with the U6 snRNA to link the NTC to the spliceosome during pre-mRNA splicing. In the N-terminal half, Cwc2 contains a CCCH-type zinc finger (ZnF domain), a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and an intervening loop, also termed RNA-binding loop or RB loop, between ZnF and RRM, all of which are necessary and sufficient for RNA binding. The ZnF is also responsible for mediating protein-protein interaction. The C-terminal flexible region of Cwc2 interacts with the WD40 domain of Prp19
NRTLYVGGIKAASNKLAQIEEILRRHFGEWGEIERIRVLPSKGIAFVRYKNRANAEFAKEAMADQSLDGG
EVLNVRWAN
>gnl|CDD|409796 cd12361, RRM1_2_CELF1-6_like, RNA recognition motif 1 (RRM1) and 2 (RRM2) found in CELF/Bruno-like family of RNA binding proteins and plant flowering time control protein FCA. This subfamily corresponds to the RRM1 and RRM2 domains of the CUGBP1 and ETR-3-like factors (CELF) as well as plant flowering time control protein FCA. CELF, also termed BRUNOL (Bruno-like) proteins, is a family of structurally related RNA-binding proteins involved in regulation of pre-mRNA splicing in the nucleus, and control of mRNA translation and deadenylation in the cytoplasm. The family contains six members: CELF-1 (also known as BRUNOL-2, CUG-BP1, NAPOR, EDEN-BP), CELF-2 (also known as BRUNOL-3, ETR-3, CUG-BP2, NAPOR-2), CELF-3 (also known as BRUNOL-1, TNRC4, ETR-1, CAGH4, ER DA4), CELF-4 (BRUNOL-4), CELF-5 (BRUNOL-5) and CELF-6 (BRUNOL-6). They all contain three highly conserved RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C-terminus of the protein. The low sequence conservation of the linker region is highly suggestive of a large variety in the co-factors that associate with the various CELF family members. Based on both, sequence similarity and function, the CELF family can be divided into two subfamilies, the first containing CELFs 1 and 2, and the second containing CELFs 3, 4, 5, and 6. The different CELF proteins may act through different sites on at least some substrates. Furthermore, CELF proteins may interact with each other in varying combinations to influence alternative splicing in different contexts. This subfamily also includes plant flowering time control protein FCA that functions in the posttranscriptional regulation of transcripts involved in the flowering process. FCA contains two RRMs, and a WW protein interaction domain
KLFVGMIPKTASEEDVRPLFEQFGNIEEVQILRDKQTGQSKGCAFVTFSTREEALRAIEALHNKKTMPGC
SSPLQVK
>gnl|CDD|409797 cd12362, RRM3_CELF1-6, RNA recognition motif 3 (RRM3) found in CELF/Bruno-like family of RNA binding proteins CELF1, CELF2, CELF3, CELF4, CELF5, CELF6 and similar proteins. This subgroup corresponds to the RRM3 of the CUGBP1 and ETR-3-like factors (CELF) or BRUNOL (Bruno-like) proteins, a family of structurally related RNA-binding proteins involved in the regulation of pre-mRNA splicing in the nucleus and in the control of mRNA translation and deadenylation in the cytoplasm. The family contains six members: CELF-1 (also termed BRUNOL-2, or CUG-BP1, or NAPOR, or EDEN-BP), CELF-2 (also termed BRUNOL-3, or ETR-3, or CUG-BP2, or NAPOR-2), CELF-3 (also termed BRUNOL-1, or TNRC4, or ETR-1, or CAGH4, or ER DA4), CELF-4 (also termed BRUNOL-4), CELF-5 (also termed BRUNOL-5), CELF-6 (also termed BRUNOL-6). They all contain three highly conserved RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C-terminus of the protein. The low sequence conservation of the linker region is highly suggestive of a large variety in the co-factors that associate with the various CELF family members. Based on both sequence similarity and function, the CELF family can be divided into two subfamilies, the first containing CELFs 1 and 2, and the second containing CELFs 3, 4, 5, and 6. The different CELF proteins may act through different sites on at least some substrates. Furthermore, CELF proteins may interact with each other in varying combinations to influence alternative splicing in different contexts
LFVYHLPNEFTDQDLYQLFAPFGNVVSAKVFVDKNTGRSKGFGFVSYDNPLSAQAAIKAMNGFQVGGKRL
KVQ
>gnl|CDD|409798 cd12363, RRM_TRA2, RNA recognition motif (RRM) found in transformer-2 protein homolog TRA2-alpha, TRA2-beta and similar proteins. This subfamily corresponds to the RRM of two mammalian homologs of Drosophila transformer-2 (Tra2), TRA2-alpha, TRA2-beta (also termed SFRS10), and similar proteins found in eukaryotes. TRA2-alpha is a 40-kDa serine/arginine-rich (SR) protein that specifically binds to gonadotropin-releasing hormone (GnRH) exonic splicing enhancer on exon 4 (ESE4) and is necessary for enhanced GnRH pre-mRNA splicing. It strongly stimulates GnRH intron A excision in a dose-dependent manner. In addition, TRA2-alpha can interact with either 9G8 or SRp30c, which may also be crucial for ESE-dependent GnRH pre-mRNA splicing. TRA2-beta is a serine/arginine-rich (SR) protein that controls the pre-mRNA alternative splicing of the calcitonin/calcitonin gene-related peptide (CGRP), the survival motor neuron 1 (SMN1) protein and the tau protein. Both, TRA2-alpha and TRA2-beta, contains a well conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), flanked by the N- and C-terminal arginine/serine (RS)-rich regions
SRCLGVFGLSLYTTERDLREVFSRYGPIEKVQVVYDQQTGRSRGFGFVYFESVEDAKEAKERLNGQEIDG
RRIRVDYSIT
>gnl|CDD|409799 cd12364, RRM_RDM1, RNA recognition motif (RRM) found in RAD52 motif-containing protein 1 (RDM1) and similar proteins. This subfamily corresponds to the RRM of RDM1, also termed RAD52 homolog B, a novel factor involved in the cellular response to the anti-cancer drug cisplatin in vertebrates. RDM1 contains a small RD motif that shares with the recombination and repair protein RAD52, and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The RD motif is responsible for the acidic pH-dependent DNA-binding properties of RDM1. It interacts with ss- and dsDNA, and may act as a DNA-damage recognition factor by recognizing the distortions of the double helix caused by cisplatin-DNA adducts in vitro. In addition, due to the presence of RRM, RDM1 can bind to RNA as well as DNA
KTLFVWNISPKLTEEEIYESLCKAFSAFGLLYSVRVFPNAAVATPGFYAFVKFYSARDASRAQKALNGKW
LFQGSPLKVRF
>gnl|CDD|409800 cd12365, RRM_RNPS1, RNA recognition motif (RRM) found in RNA-binding protein with serine-rich domain 1 (RNPS1) and similar proteins. This subfamily corresponds to the RRM of RNPS1 and its eukaryotic homologs. RNPS1, also termed RNA-binding protein prevalent during the S phase, or SR-related protein LDC2, was originally characterized as a general pre-mRNA splicing activator, which activates both constitutive and alternative splicing of pre-mRNA in vitro.It has been identified as a protein component of the splicing-dependent mRNP complex, or exon-exon junction complex (EJC), and is directly involved in mRNA surveillance. Furthermore, RNPS1 is a splicing regulator whose activator function is controlled in part by CK2 (casein kinase II) protein kinase phosphorylation. It can also function as a squamous-cell carcinoma antigen recognized by T cells-3 (SART3)-binding protein, and is involved in the regulation of mRNA splicing. RNPS1 contains an N-terminal serine-rich (S) domain, a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and the C-terminal arginine/serine/proline-rich (RS/P) domain
LHVGKLTRNVTKDHLKEIFSVYGTVKNVDLPIDREPNLPRGYAYVEFESPEDAEKAIKHMDGGQIDGQEV
TVE
>gnl|CDD|409801 cd12366, RRM1_RBM45, RNA recognition motif 1 (RRM1) found in RNA-binding protein 45 (RBM45) and similar proteins. This subfamily corresponds to the RRM1 of RBM45, also termed developmentally-regulated RNA-binding protein 1 (DRB1), a new member of RNA recognition motif (RRM)-type neural RNA-binding proteins, which expresses under spatiotemporal control. It is encoded by gene drb1 that is expressed in neurons, not in glial cells. RBM45 predominantly localizes in cytoplasm of cultured cells and specifically binds to poly(C) RNA. It could play an important role during neurogenesis. RBM45 carries four RRMs, also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
PPNSRLFVVCSKSVTEDDLREAFSPFGEIQDIWVVKDKQTKESKGIAYVKFAKSSQAARAMEEMHGKCLG
DDTKPIKVLIA
>gnl|CDD|409802 cd12367, RRM2_RBM45, RNA recognition motif 2 (RRM2) found in RNA-binding protein 45 (RBM45) and similar proteins. This subfamily corresponds to the RRM2 of RBM45, also termed developmentally-regulated RNA-binding protein 1 (DRB1), a new member of RNA recognition motif (RRM)-type neural RNA-binding proteins, which expresses under spatiotemporal control. It is encoded by gene drb1 that is expressed in neurons, not in glial cells. RBM45 predominantly localizes in cytoplasm of cultured cells and specifically binds to poly(C) RNA. It could play an important role during neurogenesis. RBM45 carries four RRMs, also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
LTRLFVVIPKSYTEEDLREKFKEFGDIEYCSIVKDKNTGESKGFGYVKFLKPSQAALAIENCDRSFKAVL
AEPK
>gnl|CDD|409803 cd12368, RRM3_RBM45, RNA recognition motif 3 (RRM3) found in RNA-binding protein 45 (RBM45) and similar proteins. This subfamily corresponds to the RRM3 of RBM45, also termed developmentally-regulated RNA-binding protein 1 (DRB1), a new member of RNA recognition motif (RRM)-type neural RNA-binding proteins, which expresses under spatiotemporal control. It is encoded by gene drb1 that is expressed in neurons, not in glial cells. RBM45 predominantly localizes in cytoplasm of cultured cells and specifically binds to poly(C) RNA. It could play an important role during neurogenesis. RBM45 carries four RRMs, also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
QRLFVVVRKSVTQEQLHRLFDLIPGLEYCDLKRDPYTGKSKGFAYVTYNNPASAIYAKEKLNGFEYPPGN
RLKVK
>gnl|CDD|409804 cd12369, RRM4_RBM45, RNA recognition motif 4 (RRM4) found in RNA-binding protein 45 (RBM45) and similar proteins. This subfamily corresponds to the RRM4 of RBM45, also termed developmentally-regulated RNA-binding protein 1 (DRB1), a new member of RNA recognition motif (RRM)-type neural RNA-binding proteins, which expresses under spatiotemporal control. It is encoded by gene drb1 that is expressed in neurons, not in glial cells. RBM45 predominantly localizes in cytoplasm of cultured cells and specifically binds to poly(C) RNA. It could play an important role during neurogenesis. RBM45 carries four RRMs, also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
RLFIVCNPSPPPLDILEDVFCRFGNLIDVYLVPGKNVGYAKYADRESAEEAITTLHGKEVNGVKLKVM
>gnl|CDD|409805 cd12370, RRM1_PUF60, RNA recognition motif 1 (RRM1) found in (U)-binding-splicing factor PUF60 and similar proteins. This subfamily corresponds to the RRM1 of PUF60, also termed FUSE-binding protein-interacting repressor (FBP-interacting repressor or FIR), or Ro-binding protein 1 (RoBP1), or Siah-binding protein 1 (Siah-BP1). PUF60 is an essential splicing factor that functions as a poly-U RNA-binding protein required to reconstitute splicing in depleted nuclear extracts. Its function is enhanced through interaction with U2 auxiliary factor U2AF65. PUF60 also controls human c-myc gene expression by binding and inhibiting the transcription factor far upstream sequence element (FUSE)-binding-protein (FBP), an activator of c-myc promoters. PUF60 contains two central RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors another RRM and binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) in several nuclear proteins. Research indicates that PUF60 binds FUSE as a dimer, and only the first two RRM domains participate in the single-stranded DNA recognition
CRVYVGSIYFELGEDTIRQAFAPFGPIKSIDMSWDPVTMKHKGFAFVEYEVPEAAQLALEQMNGVMLGGR
NIKVGR
>gnl|CDD|409806 cd12371, RRM2_PUF60, RNA recognition motif 2 (RRM2) found in (U)-binding-splicing factor PUF60 and similar proteins. This subfamily corresponds to the RRM2 of PUF60, also termed FUSE-binding protein-interacting repressor (FBP-interacting repressor or FIR), or Ro-binding protein 1 (RoBP1), or Siah-binding protein 1 (Siah-BP1). PUF60 is an essential splicing factor that functions as a poly-U RNA-binding protein required to reconstitute splicing in depleted nuclear extracts. Its function is enhanced through interaction with U2 auxiliary factor U2AF65. PUF60 also controls human c-myc gene expression by binding and inhibiting the transcription factor far upstream sequence element (FUSE)-binding-protein (FBP), an activator of c-myc promoters. PUF60 contains two central RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors another RRM and binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) in several nuclear proteins. Research indicates that PUF60 binds FUSE as a dimer, and only the first two RRM domains participate in the single-stranded DNA recognition
NRIYVASVHPDLSEDDIKSVFEAFGKIKSCSLAPDPETGKHKGYGFIEYENPQSAQDAIASMNLFDLGGQ
YLRVGRA
>gnl|CDD|409807 cd12372, RRM_CFIm68_CFIm59, RNA recognition motif (RRM) found in pre-mRNA cleavage factor Im 68 kDa subunit (CFIm68 or CPSF6), pre-mRNA cleavage factor Im 59 kDa subunit (CFIm59 or CPSF7), and similar proteins. This subfamily corresponds to the RRM of cleavage factor Im (CFIm) subunits. Cleavage factor Im (CFIm) is a highly conserved component of the eukaryotic mRNA 3' processing machinery that functions in UGUA-mediated poly(A) site recognition, the regulation of alternative poly(A) site selection, mRNA export, and mRNA splicing. It is a complex composed of a small 25 kDa (CFIm25) subunit and a larger 59/68/72 kDa subunit. Two separate genes, CPSF6 and CPSF7, code for two isoforms of the large subunit, CFIm68 and CFIm59. Structurally related CFIm68 and CFIm59, also termed cleavage and polyadenylation specificity factor subunit 6 (CPSF7), or cleavage and polyadenylation specificity factor 59 kDa subunit (CPSF59), are functionally redundant. Both contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a central proline-rich region, and a C-terminal RS-like domain. Their N-terminal RRM mediates the interaction with CFIm25, and also serves to enhance RNA binding and facilitate RNA looping
LYVGNLQWWTTDEDLEGACASFGVVDVKEIKFFEHKANGKSKGYAYVEFASPAAAAAVKEKLEKREFNGR
PCVVTP
>gnl|CDD|409808 cd12373, RRM_SRSF3_like, RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 3 (SRSF3) and similar proteins. This subfamily corresponds to the RRM of two serine/arginine (SR) proteins, serine/arginine-rich splicing factor 3 (SRSF3) and serine/arginine-rich splicing factor 7 (SRSF7). SRSF3, also termed pre-mRNA-splicing factor SRp20, modulates alternative splicing by interacting with RNA cis-elements in a concentration- and cell differentiation-dependent manner. It is also involved in termination of transcription, alternative RNA polyadenylation, RNA export, and protein translation. SRSF3 is critical for cell proliferation, and tumor induction and maintenance. It can shuttle between the nucleus and cytoplasm. SRSF7, also termed splicing factor 9G8, plays a crucial role in both constitutive splicing and alternative splicing of many pre-mRNAs. Its localization and functions are tightly regulated by phosphorylation. SRSF7 is predominantly present in the nuclear and can shuttle between nucleus and cytoplasm. It cooperates with the export protein, Tap/NXF1, helps mRNA export to the cytoplasm, and enhances the expression of unspliced mRNA. Moreover, SRSF7 inhibits tau E10 inclusion through directly interacting with the proximal downstream intron of E10, a clustering region for frontotemporal dementia with Parkinsonism (FTDP) mutations. Both SRSF3 and SRSF7 contain a single N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal RS domain rich in serine-arginine dipeptides. The RRM domain is involved in RNA binding, and the RS domain has been implicated in protein shuttling and protein-protein interactions
KVYVGNLGPRVTKRELEDAFEKYGPLRNVWVARNPPGFAFVEFEDPRDAEDAVRALDGRRICGSRVRVEL
SRG
>gnl|CDD|409809 cd12374, RRM_UHM_SPF45_PUF60, RNA recognition motif (RRM) found in UHM domain of 45 kDa-splicing factor (SPF45) and similar proteins. This subfamily corresponds to the RRM found in UHM domain of 45 kDa-splicing factor (SPF45 or RBM17), poly(U)-binding-splicing factor PUF60 (FIR or Hfp or RoBP1 or Siah-BP1), and similar proteins. SPF45 is an RNA-binding protein consisting of an unstructured N-terminal region, followed by a G-patch motif and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain) and an Arg-Xaa-Phe sequence motif. SPF45 regulates alternative splicing of the apoptosis regulatory gene FAS (also known as CD95). It induces exon 6 skipping in FAS pre-mRNA through the UHM domain that binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) present in the 3' splice site-recognizing factors U2AF65, SF1 and SF3b155. PUF60 is an essential splicing factor that functions as a poly-U RNA-binding protein required to reconstitute splicing in depleted nuclear extracts. Its function is enhanced through interaction with U2 auxiliary factor U2AF65. PUF60 also controls human c-myc gene expression by binding and inhibiting the transcription factor far upstream sequence element (FUSE)-binding-protein (FBP), an activator of c-myc promoters. PUF60 contains two central RRMs and a C-terminal UHM domain
TKILVLRNMVGPGEIDEDLKDEIKEECSKYGKVLNVIIHEVASSEADDAVRVFVEFEDADEAIKAFRALN
GRFFGGRKVKARFYD
>gnl|CDD|409810 cd12375, RRM1_Hu_like, RNA recognition motif 1 (RRM1) found in the Hu proteins family, Drosophila sex-lethal (SXL), and similar proteins. This subfamily corresponds to the RRM1 of Hu proteins and SXL. The Hu proteins family represents a group of RNA-binding proteins involved in diverse biological processes. Since the Hu proteins share high homology with the Drosophila embryonic lethal abnormal vision (ELAV) protein, the Hu family is sometimes referred to as the ELAV family. Drosophila ELAV is exclusively expressed in neurons and is required for the correct differentiation and survival of neurons in flies. The neuronal members of the Hu family include Hu-antigen B (HuB or ELAV-2 or Hel-N1), Hu-antigen C (HuC or ELAV-3 or PLE21), and Hu-antigen D (HuD or ELAV-4), which play important roles in neuronal differentiation, plasticity and memory. HuB is also expressed in gonads. Hu-antigen R (HuR or ELAV-1 or HuA) is ubiquitously expressed Hu family member. It has a variety of biological functions mostly related to the regulation of cellular response to DNA damage and other types of stress. Hu proteins perform their cytoplasmic and nuclear molecular functions by coordinately regulating functionally related mRNAs. In the cytoplasm, Hu proteins recognize and bind to AU-rich RNA elements (AREs) in the 3' untranslated regions (UTRs) of certain target mRNAs, such as GAP-43, vascular epithelial growth factor (VEGF), the glucose transporter GLUT1, eotaxin and c-fos, and stabilize those ARE-containing mRNAs. They also bind and regulate the translation of some target mRNAs, such as neurofilament M, GLUT1, and p27. In the nucleus, Hu proteins function as regulators of polyadenylation and alternative splicing. Each Hu protein contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an ARE. RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions. This family also includes the sex-lethal protein (SXL) from Drosophila melanogaster. SXL governs sexual differentiation and X chromosome dosage compensation in flies. It induces female-specific alternative splicing of the transformer (tra) pre-mRNA by binding to the tra uridine-rich polypyrimidine tract at the non-sex-specific 3' splice site during the sex-determination process. SXL binds to its own pre-mRNA and promotes female-specific alternative splicing. It contains an N-terminal Gly/Asn-rich domain that may be responsible for the protein-protein interaction, and tandem RRMs that show high preference to bind single-stranded, uridine-rich target RNA transcripts
NLIVNYLPQSMTQEELRSLFGAIGPIESCKLVRDKITGQSLGYGFVNYRDPNDARKAINTLNGLDLENKR
LKVSYA
>gnl|CDD|240822 cd12376, RRM2_Hu_like, RNA recognition motif 2 (RRM2) found in the Hu proteins family, Drosophila sex-lethal (SXL), and similar proteins. This subfamily corresponds to the RRM2 of Hu proteins and SXL. The Hu proteins family represents a group of RNA-binding proteins involved in diverse biological processes. Since the Hu proteins share high homology with the Drosophila embryonic lethal abnormal vision (ELAV) protein, the Hu family is sometimes referred to as the ELAV family. Drosophila ELAV is exclusively expressed in neurons and is required for the correct differentiation and survival of neurons in flies. The neuronal members of the Hu family include Hu-antigen B (HuB or ELAV-2 or Hel-N1), Hu-antigen C (HuC or ELAV-3 or PLE21), and Hu-antigen D (HuD or ELAV-4), which play important roles in neuronal differentiation, plasticity and memory. HuB is also expressed in gonads. Hu-antigen R (HuR or ELAV-1 or HuA) is the ubiquitously expressed Hu family member. It has a variety of biological functions mostly related to the regulation of cellular response to DNA damage and other types of stress. Hu proteins perform their cytoplasmic and nuclear molecular functions by coordinately regulating functionally related mRNAs. In the cytoplasm, Hu proteins recognize and bind to AU-rich RNA elements (AREs) in the 3' untranslated regions (UTRs) of certain target mRNAs, such as GAP-43, vascular epithelial growth factor (VEGF), the glucose transporter GLUT1, eotaxin and c-fos, and stabilize those ARE-containing mRNAs. They also bind and regulate the translation of some target mRNAs, such as neurofilament M, GLUT1, and p27. In the nucleus, Hu proteins function as regulators of polyadenylation and alternative splicing. Each Hu protein contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an ARE. RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions. Also included in this subfamily is the sex-lethal protein (SXL) from Drosophila melanogaster. SXL governs sexual differentiation and X chromosome dosage compensation in flies. It induces female-specific alternative splicing of the transformer (tra) pre-mRNA by binding to the tra uridine-rich polypyrimidine tract at the non-sex-specific 3' splice site during the sex-determination process. SXL binds also to its own pre-mRNA and promotes female-specific alternative splicing. SXL contains an N-terminal Gly/Asn-rich domain that may be responsible for the protein-protein interaction, and tandem RRMs that show high preference to bind single-stranded, uridine-rich target RNA transcripts
ANLYVSGLPKTMTQKELEQLFSQYGRIITSRILRDQLTGVSRGVGFIRFDKRIEAEEAIKGLNGQKPEGA
SEPITVKFA
>gnl|CDD|409811 cd12377, RRM3_Hu, RNA recognition motif 3 (RRM3) found in the Hu proteins family. This subfamily corresponds to the RRM3 of the Hu proteins family which represent a group of RNA-binding proteins involved in diverse biological processes. Since the Hu proteins share high homology with the Drosophila embryonic lethal abnormal vision (ELAV) protein, the Hu family is sometimes referred to as the ELAV family. Drosophila ELAV is exclusively expressed in neurons and is required for the correct differentiation and survival of neurons in flies. The neuronal members of the Hu family include Hu-antigen B (HuB or ELAV-2 or Hel-N1), Hu-antigen C (HuC or ELAV-3 or PLE21), and Hu-antigen D (HuD or ELAV-4), which play important roles in neuronal differentiation, plasticity and memory. HuB is also expressed in gonads. Hu-antigen R (HuR or ELAV-1 or HuA) is the ubiquitously expressed Hu family member. It has a variety of biological functions mostly related to the regulation of cellular response to DNA damage and other types of stress. Hu proteins perform their cytoplasmic and nuclear molecular functions by coordinately regulating functionally related mRNAs. In the cytoplasm, Hu proteins recognize and bind to AU-rich RNA elements (AREs) in the 3' untranslated regions (UTRs) of certain target mRNAs, such as GAP-43, vascular epithelial growth factor (VEGF), the glucose transporter GLUT1, eotaxin and c-fos, and stabilize those ARE-containing mRNAs. They also bind and regulate the translation of some target mRNAs, such as neurofilament M, GLUT1, and p27. In the nucleus, Hu proteins function as regulators of polyadenylation and alternative splicing. Each Hu protein contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an ARE. RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
CIFVYNLAPDADESLLWQLFGPFGAVQNVKIIRDFTTNKCKGYGFVTMTNYDEAAVAIASLNGYRLGGRV
LQVSFK
>gnl|CDD|409812 cd12378, RRM1_I_PABPs, RNA recognition motif 1 (RRM1) found in type I polyadenylate-binding proteins. This subfamily corresponds to the RRM1 of type I poly(A)-binding proteins (PABPs), highly conserved proteins that bind to the poly(A) tail present at the 3' ends of most eukaryotic mRNAs. They have been implicated in the regulation of poly(A) tail length during the polyadenylation reaction, translation initiation, mRNA stabilization by influencing the rate of deadenylation and inhibition of mRNA decapping. The family represents type I polyadenylate-binding proteins (PABPs), including polyadenylate-binding protein 1 (PABP-1 or PABPC1), polyadenylate-binding protein 3 (PABP-3 or PABPC3), polyadenylate-binding protein 4 (PABP-4 or APP-1 or iPABP), polyadenylate-binding protein 5 (PABP-5 or PABPC5), polyadenylate-binding protein 1-like (PABP-1-like or PABPC1L), polyadenylate-binding protein 1-like 2 (PABPC1L2 or RBM32), polyadenylate-binding protein 4-like (PABP-4-like or PABPC4L), yeast polyadenylate-binding protein, cytoplasmic and nuclear (PABP or ACBP-67), and similar proteins. PABP-1 is a ubiquitously expressed multifunctional protein that may play a role in 3' end formation of mRNA, translation initiation, mRNA stabilization, protection of poly(A) from nuclease activity, mRNA deadenylation, inhibition of mRNA decapping, and mRNP maturation. Although PABP-1 is thought to be a cytoplasmic protein, it is also found in the nucleus. PABP-1 may be involved in nucleocytoplasmic trafficking and utilization of mRNP particles. PABP-1 contains four copies of RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), a less well conserved linker region, and a proline-rich C-terminal conserved domain (CTD). PABP-3 is a testis-specific poly(A)-binding protein specifically expressed in round spermatids. It is mainly found in mammalian and may play an important role in the testis-specific regulation of mRNA homeostasis. PABP-3 shows significant sequence similarity to PABP-1. However, it binds to poly(A) with a lower affinity than PABP-1. Moreover, PABP-1 possesses an A-rich sequence in its 5'-UTR and allows binding of PABP and blockage of translation of its own mRNA. In contrast, PABP-3 lacks the A-rich sequence in its 5'-UTR. PABP-4 is an inducible poly(A)-binding protein (iPABP) that is primarily localized to the cytoplasm. It shows significant sequence similarity to PABP-1 as well. The RNA binding properties of PABP-1 and PABP-4 appear to be identical. PABP-5 is encoded by PABPC5 gene within the X-specific subinterval, and expressed in fetal brain and in a range of adult tissues in mammals, such as ovary and testis. It may play an important role in germ cell development. Moreover, unlike other PABPs, PABP-5 contains only four RRMs, but lacks both the linker region and the CTD. PABP-1-like and PABP-1-like 2 are the orthologs of PABP-1. PABP-4-like is the ortholog of PABP-5. Their cellular functions remain unclear. The family also includes yeast PABP, a conserved poly(A) binding protein containing poly(A) tails that can be attached to the 3'-ends of mRNAs. The yeast PABP and its homologs may play important roles in the initiation of translation and in mRNA decay. Like vertebrate PABP-1, the yeast PABP contains four RRMs, a linker region, and a proline-rich CTD as well. The first two RRMs are mainly responsible for specific binding to poly(A). The proline-rich region may be involved in protein-protein interactions
SLYVGDLHPDVTEAMLYEKFSPAGPVLSIRVCRDAVTRRSLGYAYVNFQQPADAERALDTLNFDVIKGKP
IRIMWSQRDP
>gnl|CDD|409813 cd12379, RRM2_I_PABPs, RNA recognition motif 2 (RRM2) found found in type I polyadenylate-binding proteins. This subfamily corresponds to the RRM2 of type I poly(A)-binding proteins (PABPs), highly conserved proteins that bind to the poly(A) tail present at the 3' ends of most eukaryotic mRNAs. They have been implicated in the regulation of poly(A) tail length during the polyadenylation reaction, translation initiation, mRNA stabilization by influencing the rate of deadenylation and inhibition of mRNA decapping. The family represents type I polyadenylate-binding proteins (PABPs), including polyadenylate-binding protein 1 (PABP-1 or PABPC1), polyadenylate-binding protein 3 (PABP-3 or PABPC3), polyadenylate-binding protein 4 (PABP-4 or APP-1 or iPABP), polyadenylate-binding protein 5 (PABP-5 or PABPC5), polyadenylate-binding protein 1-like (PABP-1-like or PABPC1L), polyadenylate-binding protein 1-like 2 (PABPC1L2 or RBM32), polyadenylate-binding protein 4-like (PABP-4-like or PABPC4L), yeast polyadenylate-binding protein, cytoplasmic and nuclear (PABP or ACBP-67), and similar proteins. PABP-1 is a ubiquitously expressed multifunctional protein that may play a role in 3' end formation of mRNA, translation initiation, mRNA stabilization, protection of poly(A) from nuclease activity, mRNA deadenylation, inhibition of mRNA decapping, and mRNP maturation. Although PABP-1 is thought to be a cytoplasmic protein, it is also found in the nucleus. PABP-1 may be involved in nucleocytoplasmic trafficking and utilization of mRNP particles. PABP-1 contains four copies of RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), a less well conserved linker region, and a proline-rich C-terminal conserved domain (CTD). PABP-3 is a testis-specific poly(A)-binding protein specifically expressed in round spermatids. It is mainly found in mammalian and may play an important role in the testis-specific regulation of mRNA homeostasis. PABP-3 shows significant sequence similarity to PABP-1. However, it binds to poly(A) with a lower affinity than PABP-1. Moreover, PABP-1 possesses an A-rich sequence in its 5'-UTR and allows binding of PABP and blockage of translation of its own mRNA. In contrast, PABP-3 lacks the A-rich sequence in its 5'-UTR. PABP-4 is an inducible poly(A)-binding protein (iPABP) that is primarily localized to the cytoplasm. It shows significant sequence similarity to PABP-1 as well. The RNA binding properties of PABP-1 and PABP-4 appear to be identical. PABP-5 is encoded by PABPC5 gene within the X-specific subinterval, and expressed in fetal brain and in a range of adult tissues in mammalian, such as ovary and testis. It may play an important role in germ cell development. Unlike other PABPs, PABP-5 contains only four RRMs, but lacks both the linker region and the CTD. PABP-1-like and PABP-1-like 2 are the orthologs of PABP-1. PABP-4-like is the ortholog of PABP-5. Their cellular functions remain unclear. The family also includes the yeast PABP, a conserved poly(A) binding protein containing poly(A) tails that can be attached to the 3'-ends of mRNAs. The yeast PABP and its homologs may play important roles in the initiation of translation and in mRNA decay. Like vertebrate PABP-1, the yeast PABP contains four RRMs, a linker region, and a proline-rich CTD as well. The first two RRMs are mainly responsible for specific binding to poly(A). The proline-rich region may be involved in protein-protein interactions
GVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVATDENGGSKGYGFVHFETEEAAERAIEKVNGMLLNG
KKVFVGR
>gnl|CDD|409814 cd12380, RRM3_I_PABPs, RNA recognition motif 3 (RRM3) found found in type I polyadenylate-binding proteins. This subfamily corresponds to the RRM3 of type I poly(A)-binding proteins (PABPs), highly conserved proteins that bind to the poly(A) tail present at the 3' ends of most eukaryotic mRNAs. They have been implicated in the regulation of poly(A) tail length during the polyadenylation reaction, translation initiation, mRNA stabilization by influencing the rate of deadenylation and inhibition of mRNA decapping. The family represents type I polyadenylate-binding proteins (PABPs), including polyadenylate-binding protein 1 (PABP-1 or PABPC1), polyadenylate-binding protein 3 (PABP-3 or PABPC3), polyadenylate-binding protein 4 (PABP-4 or APP-1 or iPABP), polyadenylate-binding protein 5 (PABP-5 or PABPC5), polyadenylate-binding protein 1-like (PABP-1-like or PABPC1L), polyadenylate-binding protein 1-like 2 (PABPC1L2 or RBM32), polyadenylate-binding protein 4-like (PABP-4-like or PABPC4L), yeast polyadenylate-binding protein, cytoplasmic and nuclear (PABP or ACBP-67), and similar proteins. PABP-1 is an ubiquitously expressed multifunctional protein that may play a role in 3' end formation of mRNA, translation initiation, mRNA stabilization, protection of poly(A) from nuclease activity, mRNA deadenylation, inhibition of mRNA decapping, and mRNP maturation. Although PABP-1 is thought to be a cytoplasmic protein, it is also found in the nucleus. PABP-1 may be involved in nucleocytoplasmic trafficking and utilization of mRNP particles. PABP-1 contains four copies of RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), a less well conserved linker region, and a proline-rich C-terminal conserved domain (CTD). PABP-3 is a testis-specific poly(A)-binding protein specifically expressed in round spermatids. It is mainly found in mammalian and may play an important role in the testis-specific regulation of mRNA homeostasis. PABP-3 shows significant sequence similarity to PABP-1. However, it binds to poly(A) with a lower affinity than PABP-1. PABP-1 possesses an A-rich sequence in its 5'-UTR and allows binding of PABP and blockage of translation of its own mRNA. In contrast, PABP-3 lacks the A-rich sequence in its 5'-UTR. PABP-4 is an inducible poly(A)-binding protein (iPABP) that is primarily localized to the cytoplasm. It shows significant sequence similarity to PABP-1 as well. The RNA binding properties of PABP-1 and PABP-4 appear to be identical. PABP-5 is encoded by PABPC5 gene within the X-specific subinterval, and expressed in fetal brain and in a range of adult tissues in mammalian, such as ovary and testis. It may play an important role in germ cell development. Moreover, unlike other PABPs, PABP-5 contains only four RRMs, but lacks both the linker region and the CTD. PABP-1-like and PABP-1-like 2 are the orthologs of PABP-1. PABP-4-like is the ortholog of PABP-5. Their cellular functions remain unclear. The family also includes the yeast PABP, a conserved poly(A) binding protein containing poly(A) tails that can be attached to the 3'-ends of mRNAs. The yeast PABP and its homologs may play important roles in the initiation of translation and in mRNA decay. Like vertebrate PABP-1, the yeast PABP contains four RRMs, a linker region, and a proline-rich CTD as well. The first two RRMs are mainly responsible for specific binding to poly(A). The proline-rich region may be involved in protein-protein interactions
FTNVYVKNFGEDVDDDELKELFEKYGKITSAKVMKDDSGKSKGFGFVNFENHEAAQKAVEELNGKELNGK
KLYVGRAQKK
>gnl|CDD|409815 cd12381, RRM4_I_PABPs, RNA recognition motif 4 (RRM4) found in type I polyadenylate-binding proteins. This subfamily corresponds to the RRM4 of type I poly(A)-binding proteins (PABPs), highly conserved proteins that bind to the poly(A) tail present at the 3' ends of most eukaryotic mRNAs. They have been implicated in theThe CD corresponds to the RRM. regulation of poly(A) tail length during the polyadenylation reaction, translation initiation, mRNA stabilization by influencing the rate of deadenylation and inhibition of mRNA decapping. The family represents type I polyadenylate-binding proteins (PABPs), including polyadenylate-binding protein 1 (PABP-1 or PABPC1), polyadenylate-binding protein 3 (PABP-3 or PABPC3), polyadenylate-binding protein 4 (PABP-4 or APP-1 or iPABP), polyadenylate-binding protein 5 (PABP-5 or PABPC5), polyadenylate-binding protein 1-like (PABP-1-like or PABPC1L), polyadenylate-binding protein 1-like 2 (PABPC1L2 or RBM32), polyadenylate-binding protein 4-like (PABP-4-like or PABPC4L), yeast polyadenylate-binding protein, cytoplasmic and nuclear (PABP or ACBP-67), and similar proteins. PABP-1 is an ubiquitously expressed multifunctional protein that may play a role in 3' end formation of mRNA, translation initiation, mRNA stabilization, protection of poly(A) from nuclease activity, mRNA deadenylation, inhibition of mRNA decapping, and mRNP maturation. Although PABP-1 is thought to be a cytoplasmic protein, it is also found in the nucleus. PABP-1 may be involved in nucleocytoplasmic trafficking and utilization of mRNP particles. PABP-1 contains four copies of RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), a less well conserved linker region, and a proline-rich C-terminal conserved domain (CTD). PABP-3 is a testis-specific poly(A)-binding protein specifically expressed in round spermatids. It is mainly found in mammalian and may play an important role in the testis-specific regulation of mRNA homeostasis. PABP-3 shows significant sequence similarity to PABP-1. However, it binds to poly(A) with a lower affinity than PABP-1. Moreover, PABP-1 possesses an A-rich sequence in its 5'-UTR and allows binding of PABP and blockage of translation of its own mRNA. In contrast, PABP-3 lacks the A-rich sequence in its 5'-UTR. PABP-4 is an inducible poly(A)-binding protein (iPABP) that is primarily localized to the cytoplasm. It shows significant sequence similarity to PABP-1 as well. The RNA binding properties of PABP-1 and PABP-4 appear to be identical. PABP-5 is encoded by PABPC5 gene within the X-specific subinterval, and expressed in fetal brain and in a range of adult tissues in mammalian, such as ovary and testis. It may play an important role in germ cell development. Moreover, unlike other PABPs, PABP-5 contains only four RRMs, but lacks both the linker region and the CTD. PABP-1-like and PABP-1-like 2 are the orthologs of PABP-1. PABP-4-like is the ortholog of PABP-5. Their cellular functions remain unclear. The family also includes the yeast PABP, a conserved poly(A) binding protein containing poly(A) tails that can be attached to the 3'-ends of mRNAs. The yeast PABP and its homologs may play important roles in the initiation of translation and in mRNA decay. Like vertebrate PABP-1, the yeast PABP contains four RRMs, a linker region, and a proline-rich CTD as well. The first two RRMs are mainly responsible for specific binding to poly(A). The proline-rich region may be involved in protein-protein interactions
GVNLYVKNLDDTIDDEKLREEFSPFGTITSAKVMTDEGGRSKGFGFVCFSSPEEATKAVTEMNGRIIGGK
PLYVALAQR
>gnl|CDD|409816 cd12382, RRM_RBMX_like, RNA recognition motif (RRM) found in heterogeneous nuclear ribonucleoprotein G (hnRNP G), Y chromosome RNA recognition motif 1 (hRBMY), testis-specific heterogeneous nuclear ribonucleoprotein G-T (hnRNP G-T) and similar proteins. This subfamily corresponds to the RRM domain of hnRNP G, also termed glycoprotein p43 or RBMX, an RNA-binding motif protein located on the X chromosome. It is expressed ubiquitously and has been implicated in the splicing control of several pre-mRNAs. Moreover, hnRNP G may function as a regulator of transcription for SREBP-1c and GnRH1. Research has shown that hnRNP G may also act as a tumor-suppressor since it upregulates the Txnip gene and promotes the fidelity of DNA end-joining activity. In addition, hnRNP G appears to play a critical role in proper neural development of zebrafish and frog embryos. The family also includes several paralogs of hnRNP G, such as hRBMY and hnRNP G-T (also termed RNA-binding motif protein, X-linked-like-2). Both, hRBMY and hnRNP G-T, are exclusively expressed in testis and critical for male fertility. Like hnRNP G, hRBMY and hnRNP G-T interact with factors implicated in the regulation of pre-mRNA splicing, such as hTra2-beta1 and T-STAR. Although members in this family share a high conserved N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), they appear to recognize different RNA targets. For instance, hRBMY interacts specifically with a stem-loop structure in which the loop is formed by the sequence CA/UCAA. In contrast, hnRNP G associates with single stranded RNA sequences containing a CCA/C motif. In addition to the RRM, hnRNP G contains a nascent transcripts targeting domain (NTD) in the middle region and a novel auxiliary RNA-binding domain (RBD) in its C-terminal region. The C-terminal RBD exhibits distinct RNA binding specificity, and would play a critical role in the regulation of alternative splicing by hnRNP G
PGKLFIGGLNTETNEKALEAVFGKYGRIVEVLLMKDRETNKSRGFAFVTFESPADAKDAARDMNGKELDG
KAIKVEQATK
>gnl|CDD|409817 cd12383, RRM_RBM42, RNA recognition motif (RRM) found in RNA-binding protein 42 (RBM42) and similar proteins. This subfamily corresponds to the RRM of RBM42 which has been identified as a heterogeneous nuclear ribonucleoprotein K (hnRNP K)-binding protein. It also directly binds the 3' untranslated region of p21 mRNA that is one of the target mRNAs for hnRNP K. Both, hnRNP K and RBM42, are components of stress granules (SGs). Under nonstress conditions, RBM42 predominantly localizes within the nucleus and co-localizes with hnRNP K. Under stress conditions, hnRNP K and RBM42 form cytoplasmic foci where the SG marker TIAR localizes, and may play a role in the maintenance of cellular ATP level by protecting their target mRNAs. RBM42 contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
EWPPNDFRIFCGDLGNEVTDEVLARAFSKYPSFQKAKVIRDKRTGKSKGYGFVSFKDPNDYLKALREMNG
KYVGNRPIKLRKS
>gnl|CDD|409818 cd12384, RRM_RBM24_RBM38_like, RNA recognition motif (RRM) found in eukaryotic RNA-binding protein RBM24, RBM38 and similar proteins. This subfamily corresponds to the RRM of RBM24 and RBM38 from vertebrate, SUPpressor family member SUP-12 from Caenorhabditis elegans and similar proteins. Both, RBM24 and RBM38, are preferentially expressed in cardiac and skeletal muscle tissues. They regulate myogenic differentiation by controlling the cell cycle in a p21-dependent or -independent manner. RBM24, also termed RNA-binding region-containing protein 6, interacts with the 3'-untranslated region (UTR) of myogenin mRNA and regulates its stability in C2C12 cells. RBM38, also termed CLL-associated antigen KW-5, or HSRNASEB, or RNA-binding region-containing protein 1(RNPC1), or ssDNA-binding protein SEB4, is a direct target of the p53 family. It is required for maintaining the stability of the basal and stress-induced p21 mRNA by binding to their 3'-UTRs. It also binds the AU-/U-rich elements in p63 3'-UTR and regulates p63 mRNA stability and activity. SUP-12 is a novel tissue-specific splicing factor that controls muscle-specific splicing of the ADF/cofilin pre-mRNA in C. elegans. All family members contain a conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
TKIFVGGLPYHTTDDSLREYFEQFGEIEEAVVITDRQTGKSRGYGFVTMADREAAERACKDPNPIIDGRK
ANVNLA
>gnl|CDD|409819 cd12385, RRM1_hnRNPM_like, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein M (hnRNP M) and similar proteins. This subfamily corresponds to the RRM1 of heterogeneous nuclear ribonucleoprotein M (hnRNP M), myelin expression factor 2 (MEF-2 or MyEF-2 or MST156) and similar proteins. hnRNP M is pre-mRNA binding protein that may play an important role in the pre-mRNA processing. It also preferentially binds to poly(G) and poly(U) RNA homopolymers. Moreover, hnRNP M is able to interact with early spliceosomes, further influencing splicing patterns of specific pre-mRNAs. hnRNP M functions as the receptor of carcinoembryonic antigen (CEA) that contains the penta-peptide sequence PELPK signaling motif. In addition, hnRNP M and another splicing factor Nova-1 work together as dopamine D2 receptor (D2R) pre-mRNA-binding proteins. They regulate alternative splicing of D2R pre-mRNA in an antagonistic manner. hnRNP M contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and an unusual hexapeptide-repeat region rich in methionine and arginine residues (MR repeat motif). MEF-2 is a sequence-specific single-stranded DNA (ssDNA) binding protein that binds specifically to ssDNA derived from the proximal (MB1) element of the myelin basic protein (MBP) promoter and represses transcription of the MBP gene. MEF-2 shows high sequence homology with hnRNP M. It also contains three RRMs, which may be responsible for its ssDNA binding activity
RVFISNIPYDYKWQDLKDLFREKVGEVTYVELFKDENGKSRGCGIVEFKDLESVQKALETMNRYELKGRK
LVVKED
>gnl|CDD|409820 cd12386, RRM2_hnRNPM_like, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein M (hnRNP M) and similar proteins. This subfamily corresponds to the RRM2 of heterogeneous nuclear ribonucleoprotein M (hnRNP M), myelin expression factor 2 (MEF-2 or MyEF-2 or MST156) and similar proteins. hnRNP M is pre-mRNA binding protein that may play an important role in the pre-mRNA processing. It also preferentially binds to poly(G) and poly(U) RNA homopolymers. hnRNP M is able to interact with early spliceosomes, further influencing splicing patterns of specific pre-mRNAs. It functions as the receptor of carcinoembryonic antigen (CEA) that contains the penta-peptide sequence PELPK signaling motif. In addition, hnRNP M and another splicing factor Nova-1 work together as dopamine D2 receptor (D2R) pre-mRNA-binding proteins. They regulate alternative splicing of D2R pre-mRNA in an antagonistic manner. hnRNP M contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and an unusual hexapeptide-repeat region rich in methionine and arginine residues (MR repeat motif). MEF-2 is a sequence-specific single-stranded DNA (ssDNA) binding protein that binds specifically to ssDNA derived from the proximal (MB1) element of the myelin basic protein (MBP) promoter and represses transcription of the MBP gene. MEF-2 shows high sequence homology with hnRNP M. It also contains three RRMs, which may be responsible for its ssDNA binding activity
IFVANLDYKVGWKKLKEVFKLAGKVVRADIREDKDGKSRGMGVVQFEHPIEAVQAISMFNGQMLFDRPMR
VKMD
>gnl|CDD|409821 cd12387, RRM3_hnRNPM_like, RNA recognition motif 3 (RRM3) found in heterogeneous nuclear ribonucleoprotein M (hnRNP M) and similar proteins. This subfamily corresponds to the RRM3 of heterogeneous nuclear ribonucleoprotein M (hnRNP M), myelin expression factor 2 (MEF-2 or MyEF-2 or MST156) and similar proteins. hnRNP M is pre-mRNA binding protein that may play an important role in the pre-mRNA processing. It also preferentially binds to poly(G) and poly(U) RNA homopolymers. hnRNP M is able to interact with early spliceosomes, further influencing splicing patterns of specific pre-mRNAs. hnRNP M functions as the receptor of carcinoembryonic antigen (CEA) that contains the penta-peptide sequence PELPK signaling motif. In addition, hnRNP M and another splicing factor Nova-1 work together as dopamine D2 receptor (D2R) pre-mRNA-binding proteins. They regulate alternative splicing of D2R pre-mRNA in an antagonistic manner. hnRNP M contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and an unusual hexapeptide-repeat region rich in methionine and arginine residues (MR repeat motif). MEF-2 is a sequence-specific single-stranded DNA (ssDNA) binding protein that binds specifically to ssDNA derived from the proximal (MB1) element of the myelin basic protein (MBP) promoter and represses transcription of the MBP gene. MEF-2 shows high sequence homology with hnRNP M. It also contains three RRMs, which may be responsible for its ssDNA binding activity
IFVRNLPFDYTWQKLKDKFKDCGHVTFASIKMENGKSKGCGTVRFDSPEDAENACRMMNGSKQSGREIDV
R
>gnl|CDD|409822 cd12388, RRM1_RAVER, RNA recognition motif 1 (RRM1) found in ribonucleoprotein PTB-binding raver-1, raver-2 and similar proteins. This subfamily corresponds to the RRM1 of raver-1 and raver-2. Raver-1 is a ubiquitously expressed heterogeneous nuclear ribonucleoprotein (hnRNP) that serves as a co-repressor of the nucleoplasmic splicing repressor polypyrimidine tract-binding protein (PTB)-directed splicing of select mRNAs. It shuttles between the cytoplasm and the nucleus and can accumulate in the perinucleolar compartment, a dynamic nuclear substructure that harbors PTB. Raver-1 also modulates focal adhesion assembly by binding to the cytoskeletal proteins, including alpha-actinin, vinculin, and metavinculin (an alternatively spliced isoform of vinculin) at adhesion complexes, particularly in differentiated muscle tissue. Raver-2 is a novel member of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. It shows high sequence homology to raver-1. Raver-2 exerts a spatio-temporal expression pattern during embryogenesis and is mainly limited to differentiated neurons and glia cells. Although it displays nucleo-cytoplasmic shuttling in heterokaryons, raver2 localizes to the nucleus in glia cells and neurons. Raver-2 can interact with PTB and may participate in PTB-mediated RNA-processing. However, there is no evidence indicating that raver-2 can bind to cytoplasmic proteins. Both, raver-1 and raver-2, contain three N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two putative nuclear localization signals (NLS) at the N- and C-termini, a central leucine-rich region, and a C-terminal region harboring two [SG][IL]LGxxP motifs. They binds to RNA through the RRMs. In addition, the two [SG][IL]LGxxP motifs serve as the PTB-binding motifs in raver1. However, raver-2 interacts with PTB through the SLLGEPP motif only
RILVRNLPNDITAQEVHDLLADYGLKYCHVDKAKGTAFVTLLNGEQAGTAILKFHQSSYRDRQLSVQLQP
>gnl|CDD|409823 cd12389, RRM2_RAVER, RNA recognition motif 2 (RRM2) found in ribonucleoprotein PTB-binding raver-1, raver-2 and similar proteins. This subfamily corresponds to the RRM2 of raver-1 and raver-2. Raver-1 is a ubiquitously expressed heterogeneous nuclear ribonucleoprotein (hnRNP) that serves as a co-repressor of the nucleoplasmic splicing repressor polypyrimidine tract-binding protein (PTB)-directed splicing of select mRNAs. It shuttles between the cytoplasm and the nucleus and can accumulate in the perinucleolar compartment, a dynamic nuclear substructure that harbors PTB. Raver-1 also modulates focal adhesion assembly by binding to the cytoskeletal proteins, including alpha-actinin, vinculin, and metavinculin (an alternatively spliced isoform of vinculin) at adhesion complexes, particularly in differentiated muscle tissue. Raver-2 is a novel member of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. It shows high sequence homology to raver-1. Raver-2 exerts a spatio-temporal expression pattern during embryogenesis and is mainly limited to differentiated neurons and glia cells. Although it displays nucleo-cytoplasmic shuttling in heterokaryons, raver2 localizes to the nucleus in glia cells and neurons. Raver-2 can interact with PTB and may participate in PTB-mediated RNA-processing. However, there is no evidence indicating that raver-2 can bind to cytoplasmic proteins. Both, raver-1 and raver-2, contain three N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two putative nuclear localization signals (NLS) at the N- and C-termini, a central leucine-rich region, and a C-terminal region harboring two [SG][IL]LGxxP motifs. They binds to RNA through the RRMs. In addition, the two [SG][IL]LGxxP motifs serve as the PTB-binding motifs in raver1. However, raver-2 interacts with PTB through the SLLGEPP motif only
LLCVTNLPLSFTEEQFEELVRPYGNVERCFLVYSEVTGESKGYGFVEYTSKESAIRAKNQLHGRQIGGRA
LQVDWLD
>gnl|CDD|409824 cd12390, RRM3_RAVER, RNA recognition motif 3 (RRM3) found in ribonucleoprotein PTB-binding raver-1, raver-2 and similar proteins. This subfamily corresponds to the RRM3 of raver-1 and raver-2. Raver-1 is a ubiquitously expressed heterogeneous nuclear ribonucleoprotein (hnRNP) that serves as a co-repressor of the nucleoplasmic splicing repressor polypyrimidine tract-binding protein (PTB)-directed splicing of select mRNAs. It shuttles between the cytoplasm and the nucleus and can accumulate in the perinucleolar compartment, a dynamic nuclear substructure that harbors PTB. Raver-1 also modulates focal adhesion assembly by binding to the cytoskeletal proteins, including alpha-actinin, vinculin, and metavinculin (an alternatively spliced isoform of vinculin) at adhesion complexes, particularly in differentiated muscle tissue. Raver-2 is a novel member of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. It shows high sequence homology to raver-1. Raver-2 exerts a spatio-temporal expression pattern during embryogenesis and is mainly limited to differentiated neurons and glia cells. Although it displays nucleo-cytoplasmic shuttling in heterokaryons, raver2 localizes to the nucleus in glia cells and neurons. Raver-2 can interact with PTB and may participate in PTB-mediated RNA-processing. However, there is no evidence indicating that raver-2 can bind to cytoplasmic proteins. Both, raver-1 and raver-2, contain three N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two putative nuclear localization signals (NLS) at the N- and C-termini, a central leucine-rich region, and a C-terminal region harboring two [SG][IL]LGxxP motifs. They binds to RNA through the RRMs. In addition, the two [SG][IL]LGxxP motifs serve as the PTB-binding motifs in raver1. However, raver-2 interacts with PTB through the SLLGEPP motif only
HSKCLFVDRLPKDFRDGSELRKLFSQVGKPTFCQLAMGNGVPRGFAFVEFASAEDAEEAQQLLNGHDLQG
SPIRVSFGNPGRPGASLLRRL
>gnl|CDD|409825 cd12391, RRM1_SART3, RNA recognition motif 1 (RRM1) found in squamous cell carcinoma antigen recognized by T-cells 3 (SART3) and similar proteins. This subfamily corresponds to the RRM1 of SART3, also termed Tat-interacting protein of 110 kDa (Tip110), an RNA-binding protein expressed in the nucleus of the majority of proliferating cells, including normal cells and malignant cells, but not in normal tissues except for the testes and fetal liver. It is involved in the regulation of mRNA splicing probably via its complex formation with RNA-binding protein with a serine-rich domain (RNPS1), a pre-mRNA-splicing factor. SART3 has also been identified as a nuclear Tat-interacting protein that regulates Tat transactivation activity through direct interaction and functions as an important cellular factor for HIV-1 gene expression and viral replication. In addition, SART3 is required for U6 snRNP targeting to Cajal bodies. It binds specifically and directly to the U6 snRNA, interacts transiently with the U6 and U4/U6 snRNPs, and promotes the reassembly of U4/U6 snRNPs after splicing in vitro. SART3 contains an N-terminal half-a-tetratricopeptide repeat (HAT)-rich domain, a nuclearlocalization signal (NLS) domain, and two C-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
TVFVSNLDYSVPEDKIREIFSGCGEITDVRLVKNYKGKSKGYCYVEFKDEESAQKALKLDRQPVEGRPMF
VS
>gnl|CDD|409826 cd12392, RRM2_SART3, RNA recognition motif 2 (RRM2) found in squamous cell carcinoma antigen recognized by T-cells 3 (SART3) and similar proteins. This subfamily corresponds to the RRM2 of SART3, also termed Tat-interacting protein of 110 kDa (Tip110), is an RNA-binding protein expressed in the nucleus of the majority of proliferating cells, including normal cells and malignant cells, but not in normal tissues except for the testes and fetal liver. It is involved in the regulation of mRNA splicing probably via its complex formation with RNA-binding protein with a serine-rich domain (RNPS1), a pre-mRNA-splicing factor. SART3 has also been identified as a nuclear Tat-interacting protein that regulates Tat transactivation activity through direct interaction and functions as an important cellular factor for HIV-1 gene expression and viral replication. In addition, SART3 is required for U6 snRNP targeting to Cajal bodies. It binds specifically and directly to the U6 snRNA, interacts transiently with the U6 and U4/U6 snRNPs, and promotes the reassembly of U4/U6 snRNPs after splicing in vitro. SART3 contains an N-terminal half-a-tetratricopeptide repeat (HAT)-rich domain, a nuclearlocalization signal (NLS) domain, and two C-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
EKNKLFVKGLPFSCTKEELEELFKQHGTVKDVRLVTYRNGKPKGLAYVEYENEADASQAVLKTDGTEIKD
HTISVAISNPP
>gnl|CDD|409827 cd12393, RRM_ZCRB1, RNA recognition motif (RRM) found in Zinc finger CCHC-type and RNA-binding motif-containing protein 1 (ZCRB1) and similar proteins. This subfamily corresponds to the RRM of ZCRB1, also termed MADP-1, or U11/U12 small nuclear ribonucleoprotein 31 kDa protein (U11/U12 snRNP 31 or U11/U12-31K), a novel multi-functional nuclear factor, which may be involved in morphine dependence, cold/heat stress, and hepatocarcinoma. It is located in the nucleoplasm, but outside the nucleolus. ZCRB1 is one of the components of U11/U12 snRNPs that bind to U12-type pre-mRNAs and form a di-snRNP complex, simultaneously recognizing the 5' splice site and branchpoint sequence. ZCRB1 is characterized by an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a CCHC-type Zinc finger motif. In addition, it contains core nucleocapsid motifs, and Lys- and Glu-rich domains
KSTVYVSNLPFSLTNNDLHQIFSKYGKVVKVTILKDKETRKSKGVAFVLFLDRESAHNAVRAMNNKELFG
RTLKCS
>gnl|CDD|409828 cd12394, RRM1_RBM34, RNA recognition motif 1 (RRM1) found in RNA-binding protein 34 (RBM34) and similar proteins. This subfamily corresponds to the RRM1 of RBM34, a putative RNA-binding protein containing two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). Although the function of RBM34 remains unclear currently, its RRM domains may participate in mRNA processing. RBM34 may act as an mRNA processing-related protein
RTVFVGNLPVTVKKKALKKLFKEFGKIESVRFRSVAVANPKLPKKVAVIKKKFHPKRDSMNAYVVFKEEE
SAQKALKLNGTEFEGHHIRVD
>gnl|CDD|409829 cd12395, RRM2_RBM34, RNA recognition motif 2 (RRM2) found in RNA-binding protein 34 (RBM34) and similar proteins. This subfamily corresponds to the RRM2 of RBM34, a putative RNA-binding protein containing two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). Although the function of RBM34 remains unclear currently, its RRM domains may participate in mRNA processing. RBM34 may act as an mRNA processing-related protein
SVFVGNLPFDIEEEELRKHFEDCGDVEAVRIVRDRETGIGKGFGYVLFKDKDSVDLALKLNGSKLRGRKL
RVK
>gnl|CDD|409830 cd12396, RRM1_Nop13p_fungi, RNA recognition motif 1 (RRM1) found in yeast nucleolar protein 13 (Nop13p) and similar proteins. This subfamily corresponds to the RRM1 of Nop13p encoded by YNL175c from Saccharomyces cerevisiae. It shares high sequence similarity with nucleolar protein 12 (Nop12p). Both, Nop12p and Nop13p, are not essential for growth. However, unlike Nop12p that is localized to the nucleolus, Nop13p localizes primarily to the nucleolus but is also present in the nucleoplasm to a lesser extent. Nop13p contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
VWIGNLSFTTTKEDLRQFFVDKSGDRITEEQITRIHMPTSKAKPKGKPQNKGFAYVDFSSLEATKAAIAL
SEKILNGRNLLIKDA
>gnl|CDD|409831 cd12397, RRM2_Nop13p_fungi, RNA recognition motif 2 (RRM2) found in yeast nucleolar protein 13 (Nop13p) and similar proteins. This subfamily corresponds to the RRM2 of Nop13p encoded by YNL175c from Saccharomyces cerevisiae. It shares high sequence similarity with nucleolar protein 12 (Nop12p). Both Nop12p and Nop13p are not essential for growth. However, unlike Nop12p that is localized to the nucleolus, Nop13p localizes primarily to the nucleolus but is also present in the nucleoplasm to a lesser extent. Nop13p contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
LFVGNLSFETTEEDLRKHFAPAGKIRKVRMATFEDSGKCKGFAFVDFKEIESATNAVKGPINHSLNGRDL
RVEYGE
>gnl|CDD|409832 cd12398, RRM_CSTF2_RNA15_like, RNA recognition motif (RRM) found in cleavage stimulation factor subunit 2 (CSTF2), yeast ortholog mRNA 3'-end-processing protein RNA15 and similar proteins. This subfamily corresponds to the RRM domain of CSTF2, its tau variant and eukaryotic homologs. CSTF2, also termed cleavage stimulation factor 64 kDa subunit (CstF64), is the vertebrate conterpart of yeast mRNA 3'-end-processing protein RNA15. It is expressed in all somatic tissues and is one of three cleavage stimulatory factor (CstF) subunits required for polyadenylation. CstF64 contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a CstF77-binding domain, a repeated MEARA helical region and a conserved C-terminal domain reported to bind the transcription factor PC-4. During polyadenylation, CstF interacts with the pre-mRNA through the RRM of CstF64 at U- or GU-rich sequences within 10 to 30 nucleotides downstream of the cleavage site. CSTF2T, also termed tauCstF64, is a paralog of the X-linked cleavage stimulation factor CstF64 protein that supports polyadenylation in most somatic cells. It is expressed during meiosis and subsequent haploid differentiation in a more limited set of tissues and cell types, largely in meiotic and postmeiotic male germ cells, and to a lesser extent in brain. The loss of CSTF2T will cause male infertility, as it is necessary for spermatogenesis and fertilization. Moreover, CSTF2T is required for expression of genes involved in morphological differentiation of spermatids, as well as for genes having products that function during interaction of motile spermatozoa with eggs. It promotes germ cell-specific patterns of polyadenylation by using its RRM to bind to different sequence elements downstream of polyadenylation sites than does CstF64. The family also includes yeast ortholog mRNA 3'-end-processing protein RNA15 and similar proteins. RNA15 is a core subunit of cleavage factor IA (CFIA), an essential transcriptional 3'-end processing factor from Saccharomyces cerevisiae. RNA recognition by CFIA is mediated by an N-terminal RRM, which is contained in the RNA15 subunit of the complex. The RRM of RNA15 has a strong preference for GU-rich RNAs, mediated by a binding pocket that is entirely conserved in both yeast and vertebrate RNA15 orthologs
RSVFVGNIPYDATEEQLKEIFSEVGPVVSFRLVTDRETGKPKGYGFCEFRDAETALSAVRNLNGYELNGR
PLRVDFA
>gnl|CDD|409833 cd12399, RRM_HP0827_like, RNA recognition motif (RRM) found in Helicobacter pylori HP0827 protein and similar proteins. This subfamily corresponds to the RRM of H. pylori HP0827, a putative ssDNA-binding protein 12rnp2 precursor, containing one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The ssDNA binding may be important in activation of HP0827
LYVGNLPYSASEEQLKSLFGQFGAVFDVKLPMDRETKRPRGFGFVELQEEESAEKAIAKLDGTDFMGRTI
RVNEA
>gnl|CDD|409834 cd12400, RRM_Nop6, RNA recognition motif (RRM) found in Saccharomyces cerevisiae nucleolar protein 6 (Nop6) and similar proteins. This subfamily corresponds to the RRM of Nop6, also known as Ydl213c, a component of 90S pre-ribosomal particles in yeast S. cerevisiae. It is enriched in the nucleolus and is required for 40S ribosomal subunit biogenesis. Nop6 is a non-essential putative RNA-binding protein with two N-terminal putative nuclear localisation sequences (NLS-1 and NLS-2) and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). It binds to the pre-rRNA early during transcription and plays an essential role in pre-rRNA processing
YILFVGNLPYDTTAEDLKEHFKKAGEPPSVRLLTDKKTGKSKGCAFVEFDNQKALQKALKLHHTSLGGRK
INVE
>gnl|CDD|409835 cd12401, RRM_eIF4H, RNA recognition motif (RRM) found in eukaryotic translation initiation factor 4H (eIF-4H) and similar proteins. This subfamily corresponds to the RRM of eIF-4H, also termed Williams-Beuren syndrome chromosomal region 1 protein, which, together with elf-4B/eIF-4G, serves as the accessory protein of RNA helicase eIF-4A. eIF-4H contains a well conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). It stimulates protein synthesis by enhancing the helicase activity of eIF-4A in the initiation step of mRNA translation
PTEPPFTAYVGNLPFNTVQGDLDAIFKDLKVRSVRLVRDRETDKFKGFCYVEFEDLESLKEALEYDGALF
EDRPLRVDIAEGRK
>gnl|CDD|409836 cd12402, RRM_eIF4B, RNA recognition motif (RRM) found in eukaryotic translation initiation factor 4B (eIF-4B) and similar proteins. This subfamily corresponds to the RRM of eIF-4B, a multi-domain RNA-binding protein that has been primarily implicated in promoting the binding of 40S ribosomal subunits to mRNA during translation initiation. It contains two RNA-binding domains; the N-terminal well-conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), binds the 18S rRNA of the 40S ribosomal subunit and the C-terminal basic domain (BD), including two arginine-rich motifs (ARMs), binds mRNA during initiation, and is primarily responsible for the stimulation of the helicase activity of eIF-4A. eIF-4B also contains a DRYG domain (a region rich in Asp, Arg, Tyr, and Gly amino acids) in the middle, which is responsible for both, self-association of eIF-4B and binding to the p170 subunit of eIF3. Additional research indicates that eIF-4B can interact with the poly(A) binding protein (PABP) in mammalian cells, which can stimulate both, the eIF-4B-mediated activation of the helicase activity of eIF-4A and binding of poly(A) by PABP. eIF-4B has also been shown to interact specifically with the internal ribosome entry sites (IRES) of several picornaviruses which facilitate cap-independent translation initiation
PPYTAYLGNLPYDVTEDDIEDFFRGLNISSVRLPRENGPGRLRGFGYVEFEDRESLIQALSLNEESLKNR
RIRVDVAGQAQ
>gnl|CDD|409837 cd12403, RRM1_NCL, RNA recognition motif 1 (RRM1) found in vertebrate nucleolin. This subfamily corresponds to the RRM1 of ubiquitously expressed protein nucleolin, also termed protein C23. Nucleolin is a multifunctional major nucleolar phosphoprotein that has been implicated in various metabolic processes, such as ribosome biogenesis, cytokinesis, nucleogenesis, cell proliferation and growth, cytoplasmic-nucleolar transport of ribosomal components, transcriptional repression, replication, signal transduction, inducing chromatin decondensation, etc. Nucleolin exhibits intrinsic self-cleaving, DNA helicase, RNA helicase and DNA-dependent ATPase activities. It can be phosphorylated by many protein kinases, such as the major mitotic kinase Cdc2, casein kinase 2 (CK2), and protein kinase C-zeta. Nucleolin shares similar domain architecture with gar2 from Schizosaccharomyces pombe and NSR1 from Saccharomyces cerevisiae. The highly phosphorylated N-terminal domain of nucleolin is made up of highly acidic regions separated from each other by basic sequences, and contains multiple phosphorylation sites. The central domain of nucleolin contains four closely adjacent N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which suggests that nucleolin is potentially able to interact with multiple RNA targets. The C-terminal RGG (or GAR) domain of nucleolin is rich in glycine, arginine and phenylalanine residues, and contains high levels of NG,NG-dimethylarginines. RRM1, together with RRM2, binds specifically to RNA stem-loops containing the sequence (U/G)CCCG(A/G) in the loop
FSLFVGNLNSNKSFEELKTAISEFFAKKDLAVVDVRIGSSKKFGYVDFESAEDLEKALELNGKKVLGNEI
KLEKA
>gnl|CDD|409838 cd12404, RRM2_NCL, RNA recognition motif 2 (RRM2) found in vertebrate nucleolin. This subfamily corresponds to the RRM2 of ubiquitously expressed protein nucleolin, also termed protein C23, a multifunctional major nucleolar phosphoprotein that has been implicated in various metabolic processes, such as ribosome biogenesis, cytokinesis, nucleogenesis, cell proliferation and growth, cytoplasmic-nucleolar transport of ribosomal components, transcriptional repression, replication, signal transduction, inducing chromatin decondensation, etc. Nucleolin exhibits intrinsic self-cleaving, DNA helicase, RNA helicase and DNA-dependent ATPase activities. It can be phosphorylated by many protein kinases, such as the major mitotic kinase Cdc2, casein kinase 2 (CK2), and protein kinase C-zeta. Nucleolin shares similar domain architecture with gar2 from Schizosaccharomyces pombe and NSR1 from Saccharomyces cerevisiae. The highly phosphorylated N-terminal domain of nucleolin is made up of highly acidic regions separated from each other by basic sequences, and contains multiple phosphorylation sites. The central domain of nucleolin contains four closely adjacent N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which suggests that nucleolin is potentially able to interact with multiple RNA targets. The C-terminal RGG (or GAR) domain of nucleolin is rich in glycine, arginine and phenylalanine residues, and contains high levels of NG,NG-dimethylarginines.RRM2, together with RRM1, binds specifically to RNA stem-loops containing the sequence (U/G)CCCG(A/G) in the loop
RDARTLFVKNLPYSTTQDELKEVFEDAVDIRIPMGRDGRSKGIAYIEFKSEAEAEKALEEKQGTEVDGRS
IVVDYTG
>gnl|CDD|409839 cd12405, RRM3_NCL, RNA recognition motif 3 (RRM3) found in vertebrate nucleolin. This subfamily corresponds to the RRM3 of ubiquitously expressed protein nucleolin, also termed protein C23, is a multifunctional major nucleolar phosphoprotein that has been implicated in various metabolic processes, such as ribosome biogenesis, cytokinesis, nucleogenesis, cell proliferation and growth, cytoplasmic-nucleolar transport of ribosomal components, transcriptional repression, replication, signal transduction, inducing chromatin decondensation, etc. Nucleolin exhibits intrinsic self-cleaving, DNA helicase, RNA helicase and DNA-dependent ATPase activities. It can be phosphorylated by many protein kinases, such as the major mitotic kinase Cdc2, casein kinase 2 (CK2), and protein kinase C-zeta. Nucleolin shares similar domain architecture with gar2 from Schizosaccharomyces pombe and NSR1 from Saccharomyces cerevisiae. The highly phosphorylated N-terminal domain of nucleolin is made up of highly acidic regions separated from each other by basic sequences, and contains multiple phosphorylation sites. The central domain of nucleolin contains four closely adjacent N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which suggests that nucleolin is potentially able to interact with multiple RNA targets. The C-terminal RGG (or GAR) domain of nucleolin is rich in glycine, arginine and phenylalanine residues, and contains high levels of NG,NG-dimethylarginines
SKTLVVNNLSYSATEESLQSVFEKATSIRIPQNNGRPKGYAFVEFESVEDAKEALESCNNTEIEGRSIRL
EF
>gnl|CDD|409840 cd12406, RRM4_NCL, RNA recognition motif 4 (RRM4) found in vertebrate nucleolin. This subfamily corresponds to the RRM4 of ubiquitously expressed protein nucleolin, also termed protein C23, is a multifunctional major nucleolar phosphoprotein that has been implicated in various metabolic processes, such as ribosome biogenesis, cytokinesis, nucleogenesis, cell proliferation and growth, cytoplasmic-nucleolar transport of ribosomal components, transcriptional repression, replication, signal transduction, inducing chromatin decondensation, etc. Nucleolin exhibits intrinsic self-cleaving, DNA helicase, RNA helicase and DNA-dependent ATPase activities. It can be phosphorylated by many protein kinases, such as the major mitotic kinase Cdc2, casein kinase 2 (CK2), and protein kinase C-zeta. Nucleolin shares similar domain architecture with gar2 from Schizosaccharomyces pombe and NSR1 from Saccharomyces cerevisiae. The highly phosphorylated N-terminal domain of nucleolin is made up of highly acidic regions separated from each other by basic sequences, and contains multiple phosphorylation sites. The central domain of nucleolin contains four closely adjacent N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which suggests that nucleolin is potentially able to interact with multiple RNA targets. The C-terminal RGG (or GAR) domain of nucleolin is rich in glycine, arginine and phenylalanine residues, and contains high levels of NG,NG-dimethylarginines
KTLFVKGLSEDTTEETLKEAFEGAISARIATDRDTGSSKGFGFVDFSSEEDAKAAKEAMEDGEIDGNKVT
LDFAKPKG
>gnl|CDD|409841 cd12407, RRM_FOX1_like, RNA recognition motif (RRM) found in vertebrate RNA binding protein fox-1 homologs and similar proteins. This subfamily corresponds to the RRM of several tissue-specific alternative splicing isoforms of vertebrate RNA binding protein Fox-1 homologs, which show high sequence similarity to the Caenorhabditis elegans feminizing locus on X (Fox-1) gene encoding Fox-1 protein. RNA binding protein Fox-1 homolog 1 (RBFOX1), also termed ataxin-2-binding protein 1 (A2BP1), or Fox-1 homolog A, or hexaribonucleotide-binding protein 1 (HRNBP1), is predominantly expressed in neurons, skeletal muscle and heart. It regulates alternative splicing of tissue-specific exons by binding to UGCAUG elements. Moreover, RBFOX1 binds to the C-terminus of ataxin-2 and forms an ataxin-2/A2BP1 complex involved in RNA processing. RNA binding protein fox-1 homolog 2 (RBFOX2), also termed Fox-1 homolog B, or hexaribonucleotide-binding protein 2 (HRNBP2), or RNA-binding motif protein 9 (RBM9), or repressor of tamoxifen transcriptional activity, is expressed in ovary, whole embryo, and human embryonic cell lines in addition to neurons and muscle. RBFOX2 activates splicing of neuron-specific exons through binding to downstream UGCAUG elements. RBFOX2 also functions as a repressor of tamoxifen activation of the estrogen receptor. RNA binding protein Fox-1 homolog 3 (RBFOX3 or NeuN or HRNBP3), also termed Fox-1 homolog C, is a nuclear RNA-binding protein that regulates alternative splicing of the RBFOX2 pre-mRNA, producing a message encoding a dominant negative form of the RBFOX2 protein. Its message is detected exclusively in post-mitotic regions of embryonic brain. Like RBFOX1, both RBFOX2 and RBFOX3 bind to the hexanucleotide UGCAUG elements and modulate brain and muscle-specific splicing of exon EIIIB of fibronectin, exon N1 of c-src, and calcitonin/CGRP. Members in this family also harbor one RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
KRLHVSNIPFRFRDPDLRQMFGQFGTILDVEIIFNERGSKGFGFVTFANSADADRAREKLNGTVVEGRKI
EVNNAT
>gnl|CDD|409842 cd12408, RRM_eIF3G_like, RNA recognition motif (RRM) found in eukaryotic translation initiation factor 3 subunit G (eIF-3G) and similar proteins. This subfamily corresponds to the RRM of eIF-3G and similar proteins. eIF-3G, also termed eIF-3 subunit 4, or eIF-3-delta, or eIF3-p42, or eIF3-p44, is the RNA-binding subunit of eIF3, a large multisubunit complex that plays a central role in the initiation of translation by binding to the 40 S ribosomal subunit and promoting the binding of methionyl-tRNAi and mRNA. eIF-3G binds 18 S rRNA and beta-globin mRNA, and therefore appears to be a nonspecific RNA-binding protein. eIF-3G is one of the cytosolic targets and interacts with mature apoptosis-inducing factor (AIF). eIF-3G contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). This family also includes yeast eIF3-p33, a homolog of vertebrate eIF-3G, plays an important role in the initiation phase of protein synthesis in yeast. It binds both, mRNA and rRNA, fragments due to an RRM near its C-terminus
TIRVTNLSEDATEEDLRELFRPFGPISRVYLAKDKETGQSKGFAFVTFETREDAERAIEKLNGFGYDNLI
LSVEWA
>gnl|CDD|409843 cd12409, RRM1_RRT5, RNA recognition motif 1 (RRM1) found in yeast regulator of rDNA transcription protein 5 (RRT5) and similar proteins. This subfamily corresponds to the RRM1 of the lineage specific family containing a group of uncharacterized yeast regulators of rDNA transcription protein 5 (RRT5), which may play roles in the modulation of rDNA transcription. RRT5 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
RVYISNLSYSTTEEELEELLKDYKPVSVLIPSYTVRGFRSRKHRPLGIAYAEFSSVEEAEKVVKDLNGKV
FKGRKLFVKLHVPY
>gnl|CDD|409844 cd12410, RRM2_RRT5, RNA recognition motif 2 (RRM2) found in yeast regulator of rDNA transcription protein 5 (RRT5) and similar proteins. This subfamily corresponds to the RRM2 of the lineage specific family containing a group of uncharacterized yeast regulators of rDNA transcription protein 5 (RRT5), which may play roles in the modulation of rDNA transcription. RRT5 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
SKDTVYIGNLPGNTTDNDLREFFKDYNPQEIWIFRTKKSRRNPMYLHRHFTAALVTLPDEERLDEAIESL
KSKKLNGKKISLKPAYISKIEEV
>gnl|CDD|409845 cd12411, RRM_ist3_like, RNA recognition motif (RRM) found in ist3 family. This subfamily corresponds to the RRM of the ist3 family that includes fungal U2 small nuclear ribonucleoprotein (snRNP) component increased sodium tolerance protein 3 (ist3), X-linked 2 RNA-binding motif proteins (RBMX2) found in Metazoa and plants, and similar proteins. Gene IST3 encoding ist3, also termed U2 snRNP protein SNU17 (Snu17p), is a novel yeast Saccharomyces cerevisiae protein required for the first catalytic step of splicing and for progression of spliceosome assembly. It binds specifically to the U2 snRNP and is an intrinsic component of prespliceosomes and spliceosomes. Yeast ist3 contains an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). In the yeast pre-mRNA retention and splicing complex, the atypical RRM of ist3 functions as a scaffold that organizes the other two constituents, Bud13p (bud site selection 13) and Pml1p (pre-mRNA leakage 1). Fission yeast Schizosaccharomyces pombe gene cwf29 encoding ist3, also termed cell cycle control protein cwf29, is an RNA-binding protein complexed with cdc5 protein 29. It also contains one RRM. The biological function of RBMX2 remains unclear. It shows high sequence similarity to yeast ist3 protein and harbors one RRM as well
SWHDEYKDSAYIYIGGLPYELTEGDILCVFSQYGEIVDINLVRDKKTGKSKGFAFLAYEDQRSTILAVDN
LNGIKLLGRTIRVDHVENY
>gnl|CDD|409846 cd12412, RRM_DAZL_BOULE, RNA recognition motif (RRM) found in AZoospermia (DAZ) autosomal homologs, DAZL (DAZ-like) and BOULE. This subfamily corresponds to the RRM domain of two Deleted in AZoospermia (DAZ) autosomal homologs, DAZL (DAZ-like) and BOULE. BOULE is the founder member of the family and DAZL arose from BOULE in an ancestor of vertebrates. The DAZ gene subsequently originated from a duplication transposition of the DAZL gene. Invertebrates contain a single DAZ homolog, BOULE, while vertebrates, other than catarrhine primates, possess both BOULE and DAZL genes. The catarrhine primates possess BOULE, DAZL, and DAZ genes. The family members encode closely related RNA-binding proteins that are required for fertility in numerous organisms. These proteins contain an RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a varying number of copies of a DAZ motif, believed to mediate protein-protein interactions. DAZL and BOULE contain a single copy of the DAZ motif, while DAZ proteins can contain 8-24 copies of this repeat. Although their specific biochemical functions remain to be investigated, DAZL proteins may interact with poly(A)-binding proteins (PABPs), and act as translational activators of specific mRNAs during gametogenesis
IPNRIFVGGIDWDTTEEELREFFSKFGKVKDVKIIKDRAGVSKGYGFVTFETQEDAEKIQKWGANLVFKG
KKLNVGPAIRK
>gnl|CDD|409847 cd12413, RRM1_RBM28_like, RNA recognition motif 1 (RRM1) found in RNA-binding protein 28 (RBM28) and similar proteins. This subfamily corresponds to the RRM1 of RBM28 and Nop4p. RBM28 is a specific nucleolar component of the spliceosomal small nuclear ribonucleoproteins (snRNPs), possibly coordinating their transition through the nucleolus. It specifically associates with U1, U2, U4, U5, and U6 small nuclear RNAs (snRNAs), and may play a role in the maturation of both small nuclear and ribosomal RNAs. RBM28 has four RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and an extremely acidic region between RRM2 and RRM3. The family also includes nucleolar protein 4 (Nop4p or Nop77p) encoded by YPL043W from Saccharomyces cerevisiae. It is an essential nucleolar protein involved in processing and maturation of 27S pre-rRNA and biogenesis of 60S ribosomal subunits. Nop4p also contains four RRMs
TLFVRNLPYDTTDEQLEELFSDVGPVKRCFVVKDKGKDKCRGFGYVTFALAEDAQRALEEVKGKKFGGRK
IKVELAKKK
>gnl|CDD|409848 cd12414, RRM2_RBM28_like, RNA recognition motif 2 (RRM2) found in RNA-binding protein 28 (RBM28) and similar proteins. This subfamily corresponds to the RRM2 of RBM28 and Nop4p. RBM28 is a specific nucleolar component of the spliceosomal small nuclear ribonucleoproteins (snRNPs), possibly coordinating their transition through the nucleolus. It specifically associates with U1, U2, U4, U5, and U6 small nuclear RNAs (snRNAs), and may play a role in the maturation of both small nuclear and ribosomal RNAs. RBM28 has four RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and an extremely acidic region between RRM2 and RRM3. The family also includes nucleolar protein 4 (Nop4p or Nop77p) encoded by YPL043W from Saccharomyces cerevisiae. It is an essential nucleolar protein involved in processing and maturation of 27S pre-rRNA and biogenesis of 60S ribosomal subunits. Nop4p also contains four RRMs
RLIVRNLPFKCTEDDLKKLFSKFGKVLEVTIPKKPDGKLRGFAFVQFTNVADAAKAIKGMNGKKIKGRPV
AVDWAV
>gnl|CDD|409849 cd12415, RRM3_RBM28_like, RNA recognition motif 3 (RRM3) found in RNA-binding protein 28 (RBM28) and similar proteins. This subfamily corresponds to the RRM3 of RBM28 and Nop4p. RBM28 is a specific nucleolar component of the spliceosomal small nuclear ribonucleoproteins (snRNPs), possibly coordinating their transition through the nucleolus. It specifically associates with U1, U2, U4, U5, and U6 small nuclear RNAs (snRNAs), and may play a role in the maturation of both small nuclear and ribosomal RNAs. RBM28 has four RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and an extremely acidic region between RRM2 and RRM3. The family also includes nucleolar protein 4 (Nop4p or Nop77p) encoded by YPL043W from Saccharomyces cerevisiae. It is an essential nucleolar protein involved in processing and maturation of 27S pre-rRNA and biogenesis of 60S ribosomal subunits. Nop4p also contains four RRMs
KTVFIRNLSFDTTEEDLKEFFSKFGEVKYARIVLDKDTGHSKGTAFVQFKTKESADKCIEAANDESEDGG
LVLDGRKLIVSLA
>gnl|CDD|409850 cd12416, RRM4_RBM28_like, RNA recognition motif 4 (RRM4) found in RNA-binding protein 28 (RBM28) and similar proteins. This subfamily corresponds to the RRM4 of RBM28 and Nop4p. RBM28 is a specific nucleolar component of the spliceosomal small nuclear ribonucleoproteins (snRNPs), possibly coordinating their transition through the nucleolus. It specifically associates with U1, U2, U4, U5, and U6 small nuclear RNAs (snRNAs), and may play a role in the maturation of both small nuclear and ribosomal RNAs. RBM28 has four RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and an extremely acidic region between RRM2 and RRM3. The family also includes nucleolar protein 4 (Nop4p or Nop77p) encoded by YPL043W from Saccharomyces cerevisiae. It is an essential nucleolar protein involved in processing and maturation of 27S pre-rRNA and biogenesis of 60S ribosomal subunits. Nop4p also contains four RRMs
TRLCVRNLPKSVDDKKLKKLFLKAVKERAKKKGVKIKEVKVMRDKKRLNSDGKGRSKGYGFVEFTEHEHA
LKALRALNNNPEIFGPDKRPIVEFALEN
>gnl|CDD|409851 cd12417, RRM_SAFB_like, RNA recognition motif (RRM) found in the scaffold attachment factor (SAFB) family. This subfamily corresponds to the RRM domain of the SAFB family, including scaffold attachment factor B1 (SAFB1), scaffold attachment factor B2 (SAFB2), SAFB-like transcriptional modulator (SLTM), and similar proteins, which are ubiquitously expressed. SAFB1, SAFB2 and SLTM have been implicated in many diverse cellular processes including cell growth and transformation, stress response, and apoptosis. They share high sequence similarities and all contain a scaffold attachment factor-box (SAF-box, also known as SAP domain) DNA-binding motif, an RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a region rich in glutamine and arginine residues. SAFB1 is a nuclear protein with a distribution similar to that of SLTM, but unlike that of SAFB2, which is also found in the cytoplasm. To a large extent, SAFB1 and SLTM might share similar functions, such as the inhibition of an oestrogen reporter gene. The additional cytoplasmic localization of SAFB2 implies that it could play additional roles in the cytoplasmic compartment which are distinct from the nuclear functions shared with SAFB1 and SLTM
NLWISGLSDTTKAADLKKIFSKYGKVVSAKVVTSARTPGSRCYGYVTMASVEEADLCIKSLNKTELHGRV
ITVE
>gnl|CDD|409852 cd12418, RRM_Aly_REF_like, RNA recognition motif (RRM) found in the Aly/REF family. This subfamily corresponds to the RRM of Aly/REF family which includes THO complex subunit 4 (THOC4, also termed Aly/REF), S6K1 Aly/REF-like target (SKAR, also termed PDIP3 or PDIP46) and similar proteins. THOC4 is an mRNA transporter protein with a well conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). It is involved in RNA transportation from the nucleus, and was initially identified as a transcription coactivator of LEF-1 and AML-1 for the TCRalpha enhancer function. In addition, THOC4 specifically binds to rhesus (RH) promoter in erythroid, and might be a novel transcription cofactor for erythroid-specific genes. SKAR shows high sequence homology with THOC4 and possesses one RRM as well. SKAR is widely expressed and localizes to the nucleus. It may be a critical player in the function of S6K1 in cell and organism growth control by binding the activated, hyperphosphorylated form of S6K1 but not S6K2. Furthermore, SKAR functions as a protein partner of the p50 subunit of DNA polymerase delta. In addition, SKAR may have particular importance in pancreatic beta cell size determination and insulin secretion
TRVRVSNLHPDVTEEDLRELFGRVGPVKSVKINYDRSGRSTGTAYVVFERPEDAEKAIKQFDGVLLDGQP
MKVEL
>gnl|CDD|409853 cd12419, RRM_Ssp2_like, RNA recognition motif (RRM) found in yeast sporulation-specific protein 2 (Ssp2) and similar protein. This subfamily corresponds to the RRM of the lineage specific yeast sporulation-specific protein 2 (Ssp2) and similar proteins. Ssp2 is encoded by a sporulation-specific gene necessary for outer spore wall assembly in the yeast Saccharomyces cerevisiae. It localizes to the spore wall and may play an important role after meiosis II and during spore wall formation. Ssp2 contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
VLPSDFDVQELSDDFTVFGEIVDISPISSEKGHLSVSIFFRDIRSAMRAKETLHDKGSSLHNKYIIRTWS
IWYGKDIPPTDQPCL
>gnl|CDD|409854 cd12420, RRM_RBPMS_like, RNA recognition motif (RRM) found in RNA-binding protein with multiple splicing (RBP-MS)-like proteins. This subfamily corresponds to the RRM of RNA-binding proteins with multiple splicing (RBP-MS)-like proteins, including protein products of RBPMS genes (RBP-MS and its paralogue RBP-MS2), the Drosophila couch potato (cpo), and Caenorhabditis elegans Mec-8 genes. RBP-MS may be involved in regulation of mRNA translation and localization during Xenopus laevis development. It has also been shown to physically interact with Smad2, Smad3 and Smad4, and stimulates Smad-mediated transactivation. Cpo may play an important role in regulating normal function of the nervous system, whereas mutations in Mec-8 affect mechanosensory and chemosensory neuronal function. All members contain a well conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). Some uncharacterized family members contain two RRMs; this subfamily includes their RRM1. Their RRM2 shows high sequence homology to the RRM of yeast proteins scw1, Whi3, and Whi4
RTLFVSGLPLDVKERELYNLFRPLPGYEASQLKFTGKNTQPVGFVTFESRAAAEAAKDALQGMRFDPDTP
QVLRLE
>gnl|CDD|409855 cd12421, RRM1_PTBP1_hnRNPL_like, RNA recognition motif (RRM) found in polypyrimidine tract-binding protein 1 (PTB or hnRNP I), heterogeneous nuclear ribonucleoprotein L (hnRNP-L), and similar proteins. This subfamily corresponds to the RRM1 of the majority of family members that include polypyrimidine tract-binding protein 1 (PTB or hnRNP I), polypyrimidine tract-binding protein 2 (PTBP2 or nPTB), regulator of differentiation 1 (Rod1), heterogeneous nuclear ribonucleoprotein L (hnRNP-L), heterogeneous nuclear ribonucleoprotein L-like (hnRNP-LL), polypyrimidine tract-binding protein homolog 3 (PTBPH3), polypyrimidine tract-binding protein homolog 1 and 2 (PTBPH1 and PTBPH2), and similar proteins. PTB is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. PTBP2 is highly homologous to PTB and is perhaps specific to the vertebrates. Unlike PTB, PTBP2 is enriched in the brain and in some neural cell lines. It binds more stably to the downstream control sequence (DCS) RNA than PTB does but is a weaker repressor of splicing in vitro. PTBP2 also greatly enhances the binding of two other proteins, heterogeneous nuclear ribonucleoprotein (hnRNP) H and KH-type splicing-regulatory protein (KSRP), to the DCS RNA. The binding properties of PTBP2 and its reduced inhibitory activity on splicing imply roles in controlling the assembly of other splicing-regulatory proteins. Rod1 is a mammalian polypyrimidine tract binding protein (PTB) homolog of a regulator of differentiation in the fission yeast Schizosaccharomyces pombe, where the nrd1 gene encodes an RNA binding protein negatively regulates the onset of differentiation. ROD1 is predominantly expressed in hematopoietic cells or organs. It might play a role controlling differentiation in mammals. hnRNP-L is a higher eukaryotic specific subunit of human KMT3a (also known as HYPB or hSet2) complex required for histone H3 Lys-36 trimethylation activity. It plays both, nuclear and cytoplasmic, roles in mRNA export of intronless genes, IRES-mediated translation, mRNA stability, and splicing. hnRNP-LL protein plays a critical and unique role in the signal-induced regulation of CD45 and acts as a global regulator of alternative splicing in activated T cells. The family also includes polypyrimidine tract binding protein homolog 3 (PTBPH3) found in plant. Although its biological roles remain unclear, PTBPH3 shows significant sequence similarity to other family members, all of which contain four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain). Although their biological roles remain unclear, both PTBPH1 and PTBPH2 show significant sequence similarity to PTB. However, in contrast to PTB, they have three RRMs. In addition, this family also includes RNA-binding motif protein 20 (RBM20) that is an alternative splicing regulator associated with dilated cardiomyopathy (DCM) and contains only one RRM
VVHIRNLPPDATEADLVALGLPFGKVTNVLLLKGKNQALVEMEDVESASSMVNYYTTVPPLIRGRPVYVQ
YSNH
>gnl|CDD|409856 cd12422, RRM2_PTBP1_hnRNPL_like, RNA recognition motif (RRM) found in polypyrimidine tract-binding protein 1 (PTB or hnRNP I), heterogeneous nuclear ribonucleoprotein L (hnRNP-L), and similar proteins. This subfamily corresponds to the RRM2 of polypyrimidine tract-binding protein 1 (PTB or hnRNP I), polypyrimidine tract-binding protein 2 (PTBP2 or nPTB), regulator of differentiation 1 (Rod1), heterogeneous nuclear ribonucleoprotein L (hnRNP-L), heterogeneous nuclear ribonucleoprotein L-like (hnRNP-LL), polypyrimidine tract-binding protein homolog 3 (PTBPH3), polypyrimidine tract-binding protein homolog 1 and 2 (PTBPH1 and PTBPH2), and similar proteins, and RRM3 of PTBPH1 and PTBPH2. PTB is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. PTBP2 is highly homologous to PTB and is perhaps specific to the vertebrates. Unlike PTB, PTBP2 is enriched in the brain and in some neural cell lines. It binds more stably to the downstream control sequence (DCS) RNA than PTB does but is a weaker repressor of splicing in vitro. PTBP2 also greatly enhances the binding of two other proteins, heterogeneous nuclear ribonucleoprotein (hnRNP) H and KH-type splicing-regulatory protein (KSRP), to the DCS RNA. The binding properties of PTBP2 and its reduced inhibitory activity on splicing imply roles in controlling the assembly of other splicing-regulatory proteins. Rod1 is a mammalian polypyrimidine tract binding protein (PTB) homolog of a regulator of differentiation in the fission yeast Schizosaccharomyces pombe, where the nrd1 gene encodes an RNA binding protein negatively regulates the onset of differentiation. ROD1 is predominantly expressed in hematopoietic cells or organs. It might play a role controlling differentiation in mammals. hnRNP-L is a higher eukaryotic specific subunit of human KMT3a (also known as HYPB or hSet2) complex required for histone H3 Lys-36 trimethylation activity. It plays both, nuclear and cytoplasmic, roles in mRNA export of intronless genes, IRES-mediated translation, mRNA stability, and splicing. hnRNP-LL protein plays a critical and unique role in the signal-induced regulation of CD45 and acts as a global regulator of alternative splicing in activated T cells. This family also includes polypyrimidine tract binding protein homolog 3 (PTBPH3) found in plant. Although its biological roles remain unclear, PTBPH3 shows significant sequence similarity to other family members, all of which contain four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain). Although their biological roles remain unclear, both PTBPH1 and PTBPH2 show significant sequence similarity to PTB. However, in contrast to PTB, they have three RRMs
VLLVTVTNLLYPVTVDVLHQVFSPYGAVEKIVIFEKGTGVQALVQFDSVESAEAAKKALNGRNIYDGCCT
LDIQFSRLKELTVKY
>gnl|CDD|409857 cd12423, RRM3_PTBP1_like, RNA recognition motif 3 (RRM3) found in polypyrimidine tract-binding protein 1 (PTB or hnRNP I) and similar proteins. This subfamily corresponds to the RRM3 of polypyrimidine tract-binding protein 1 (PTB or hnRNP I), polypyrimidine tract-binding protein 2 (PTBP2 or nPTB), regulator of differentiation 1 (Rod1), and similar proteins found in Metazoa. PTB is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. PTBP2 is highly homologous to PTB and is perhaps specific to the vertebrates. Unlike PTB, PTBP2 is enriched in the brain and in some neural cell lines. It binds more stably to the downstream control sequence (DCS) RNA than PTB does but is a weaker repressor of splicing in vitro. PTBP2 also greatly enhances the binding of two other proteins, heterogeneous nuclear ribonucleoprotein (hnRNP) H and KH-type splicing-regulatory protein (KSRP), to the DCS RNA. The binding properties of PTBP2 and its reduced inhibitory activity on splicing imply roles in controlling the assembly of other splicing-regulatory proteins. PTBP2 also contains four RRMs. ROD1 coding protein Rod1 is a mammalian PTB homolog of a regulator of differentiation in the fission yeast Schizosaccharomyces pombe, where the nrd1 gene encodes an RNA binding protein negatively regulates the onset of differentiation. ROD1 is predominantly expressed in hematopoietic cells or organs. It may play a role controlling differentiation in mammals. All members in this family contain four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
VLLVSNLNEEMVTPDALFTLFGVYGDVLRVKILFNKKDTALIQMADPQQAQTALQHLNGIKLFGKPIRVT
LSKH
>gnl|CDD|409858 cd12424, RRM3_hnRNPL_like, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein L (hnRNP-L) and similar proteins. This subfamily corresponds to the RRM3 of heterogeneous nuclear ribonucleoprotein L (hnRNP-L), heterogeneous nuclear ribonucleoprotein L-like (hnRNP-LL), and similar proteins. hnRNP-L is a higher eukaryotic specific subunit of human KMT3a (also known as HYPB or hSet2) complex required for histone H3 Lys-36 trimethylation activity. It plays both, nuclear and cytoplasmic, roles in mRNA export of intronless genes, IRES-mediated translation, mRNA stability, and splicing. hnRNP-LL plays a critical and unique role in the signal-induced regulation of CD45 and acts as a global regulator of alternative splicing in activated T cells. It is closely related in domain structure and sequence to hnRNP-L, which contains three RNA-recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The family also includes polypyrimidine tract binding protein homolog 3 (PTBPH3) found in plant. Although its biological roles remain unclear, PTBPH3 shows significant sequence similarity to polypyrimidine tract binding protein (PTB) that is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. Like PTB, PTBPH3 contains four RRMs
VLMVYGLDPDKMNCDRLFNLLCLYGNVLKIKFLKSKPGTAMVQMGDPVAADRAIQNLNNVVLFGQKLQLT
YSKQ
>gnl|CDD|409859 cd12425, RRM4_PTBP1_like, RNA recognition motif 4 (RRM4) found in polypyrimidine tract-binding protein 1 (PTB or hnRNP I) and similar proteins. This subfamily corresponds to the RRM4 of polypyrimidine tract-binding protein 1 (PTB or hnRNP I), polypyrimidine tract-binding protein 2 (PTBP2 or nPTB), regulator of differentiation 1 (Rod1), and similar proteins found in Metazoa. PTB is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. PTBP2 is highly homologous to PTB and is perhaps specific to the vertebrates. Unlike PTB, PTBP2 is enriched in the brain and in some neural cell lines. It binds more stably to the downstream control sequence (DCS) RNA than PTB does but is a weaker repressor of splicing in vitro. PTBP2 also greatly enhances the binding of two other proteins, heterogeneous nuclear ribonucleoprotein (hnRNP) H and KH-type splicing-regulatory protein (KSRP), to the DCS RNA. The binding properties of PTBP2 and its reduced inhibitory activity on splicing imply roles in controlling the assembly of other splicing-regulatory proteins. PTBP2 also contains four RRMs. ROD1 coding protein Rod1 is a mammalian PTB homolog of a regulator of differentiation in the fission yeast Schizosaccharomyces pombe, where the nrd1 gene encodes an RNA binding protein negatively regulates the onset of differentiation. ROD1 is predominantly expressed in hematopoietic cells or organs. It may play a role controlling differentiation in mammals. All members in this family contain four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
TLHLSNIPPSVTEEDLKDLFTSTGGTVKAFKFFQKDRKMALIQMGSVEEAIEALIALHNYQLSENSHLRV
SFSKST
>gnl|CDD|409860 cd12426, RRM4_PTBPH3, RNA recognition motif 4 (RRM4) found in plant polypyrimidine tract-binding protein homolog 3 (PTBPH3). This subfamily corresponds to the RRM4 of PTBPH3. Although its biological roles remain unclear, PTBPH3 shows significant sequence similarity to polypyrimidine tract binding protein (PTB) that is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. Like PTB, PTBPH3 contains four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
RYCCSPTKMIHVSSLPQDVTEEDVLNHLQEHGAIVNTKVFESNGKKQALVLFENEEQATEALVCKHASSL
GGSTIRISF
>gnl|CDD|409861 cd12427, RRM4_hnRNPL_like, RNA recognition motif 4 (RRM4) found in heterogeneous nuclear ribonucleoprotein L (hnRNP-L) and similar proteins. This subfamily corresponds to the RRM4 of heterogeneous nuclear ribonucleoprotein L (hnRNP-L), heterogeneous nuclear ribonucleoprotein L-like (hnRNP-LL), and similar proteins. hnRNP-L is a higher eukaryotic specific subunit of human KMT3a (also known as HYPB or hSet2) complex required for histone H3 Lys-36 trimethylation activity. It plays both, nuclear and cytoplasmic, roles in mRNA export of intronless genes, IRES-mediated translation, mRNA stability, and splicing. hnRNP-LL plays a critical and unique role in the signal-induced regulation of CD45 and acts as a global regulator of alternative splicing in activated T cells. It is closely related in domain structure and sequence to hnRNP-L, which contains three RNA-recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
PSKVLHFFNAPPEITEETLKELFIEAGAPPPVKVKVFPSKSERSSSGLLEFESVEDALEALALCNHTPIK
NPNGKAPYTLKLCF
>gnl|CDD|409862 cd12428, RRM_PARN, RNA recognition motif (RRM) found in poly(A)-specific ribonuclease PARN and similar proteins. The subfamily corresponds to the RRM of PARN, also termed deadenylating nuclease, or deadenylation nuclease, or polyadenylate-specific ribonuclease, a processive poly(A)-specific 3'-exoribonuclease involved in the decay of eukaryotic mRNAs. It specifically binds both, the poly(A) tail at the 3' end and the 7-methylguanosine (m7G) cap located at the 5' end of eukaryotic mRNAs, and catalyzes the 3'- to 5'-end deadenylation of single-stranded mRNA with a free 3' hydroxyl group both in the nucleus and in the cytoplasm. PARN belongs to the DEDD superfamily of exonucleases. It contains a nuclease domain, an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and an R3H domain. PARN exists as a homodimer. The nuclease domain is involved in the dimerization. RRM and R3H domains are essential for the RNA-binding
RDHVFHLTFPKEWKTSDLYQLFSPFGGIQVSWIDDTSAFVALSDPEQVNIALKTITYHPSYRIRSY
>gnl|CDD|409863 cd12429, RRM_DNAJC17, RNA recognition motif (RRM) found in the DnaJ homolog subfamily C member 17. The CD corresponds to the RRM of some eukaryotic DnaJ homolog subfamily C member 17 and similar proteins. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Members in this family contains an N-terminal DnaJ domain or J-domain, which mediates the interaction with Hsp70. They also contains a RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), at the C-terminus, which may play an essential role in RNA binding
PRLKVKWKSKKGNGGYSEEELRKIFSKYGPVSDVVISSKKKGSAIVEFATVVAADAAVENEVGLPDNPLL
VSWL
>gnl|CDD|409864 cd12430, RRM_LARP4_5_like, RNA recognition motif (RRM) found in La-related protein 4 (LARP4), La-related protein 5 (LARP5 or LARP4B) and similar proteins. This subfamily corresponds to the RRM of LARP4 and LARP5. LARP4 is a cytoplasmic factor that can bind poly(A) RNA and interact with poly(A) binding protein (PABP). It may play a role in promoting translation by stabilizing mRNA. LARP5 is a cytosolic protein that co-sediments with polysomes and accumulates upon stress induction in cellular stress granules. It can interact with the cytosolic poly(A) binding protein 1 (PABPC1) and the receptor for activated C Kinase (RACK1), a component of the 40S ribosomal subunit. LARP5 may function as a stimulatory factor of translation through bridging mRNA factors of the 3' end with initiating ribosomes. Both, LARP4 and LARP5, are structurally related to the La autoantigen. Like other La-related proteins (LARPs) family members, LARP4 and LARP5 contain a La motif (LAM) and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
CIVILREIPESTPEEEVEALFSGQNCPKFTSCEFAINDSWYVTFESEEDAQEAYKYLREEVKTFNGKPIM
ARIKAE
>gnl|CDD|409865 cd12431, RRM_ALKBH8, RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and similar proteins. This subfamily corresponds to the RRM of ALKBH8, also termed alpha-ketoglutarate-dependent dioxygenase ABH8, or S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8, expressed in various types of human cancers. It is essential in urothelial carcinoma cell survival mediated by NOX-1-dependent ROS signals. ALKBH8 has also been identified as a tRNA methyltransferase that catalyzes methylation of tRNA to yield 5-methylcarboxymethyl uridine (mcm5U) at the wobble position of the anticodon loop. Thus, ALKBH8 plays a crucial role in the DNA damage survival pathway through a distinct mechanism involving the regulation of tRNA modification. ALKBH8 localizes to the cytoplasm. It contains the characteristic AlkB domain that is composed of a tRNA methyltransferase motif, a motif homologous to the bacterial AlkB DNA/RNA repair enzyme, and a dioxygenase catalytic core domain encompassing cofactor-binding sites for iron and 2-oxoglutarate. In addition, unlike other AlkB homologs, ALKBH8 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal S-adenosylmethionine (SAM)-dependent methyltransferase (MT) domain
TQHLVVANGGLGNGVSREQLLEVFEKYGTVEDIVMLPGKPYSFVSFKSVEEAAKAYNALNGKELELPQQN
VPLYLSFVEK
>gnl|CDD|409866 cd12432, RRM_ACINU, RNA recognition motif (RRM) found in apoptotic chromatin condensation inducer in the nucleus (acinus) and similar proteins. This subfamily corresponds to the RRM of Acinus, a caspase-3-activated nuclear factor that induces apoptotic chromatin condensation after cleavage by caspase-3 without inducing DNA fragmentation. It is essential for apoptotic chromatin condensation and may also participate in nuclear structural changes occurring in normal cells. Acinus contains a P-loop motif and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), which indicates Acinus might have ATPase and DNA/RNA-binding activity
SRILHIDNLVRPFTLGQLKELLSETGTGVIEGFWMDKIKSHCYVTYSSEEEAVATREALHGVVWPSSNGK
RLKVEFVTEEELEELIEGEE
>gnl|CDD|409867 cd12433, RRM_Yme2p_like, RNA recognition motif (RRM) found in yeast mitochondrial escape protein 2 (Yme2p) and similar proteins. This subfamily corresponds to the RRM of Yme2p, also termed protein RNA12, an inner mitochondrial membrane protein that plays a critical role in mitochondrial DNA transactions. It may serve as a mediator of nucleoid structure and number in mitochondria of the yeast Saccharomyces cerevisiae. Yme2p contains an exonuclease domain, an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal domain
RYPSRTIRVEFEGPELSQEELYSLFRPYGRINDITPPPPDSLPRYATVTFRRIRGAIAAKNCLHGYVVNE
GGTRLRIQYEPKLRAH
>gnl|CDD|409868 cd12434, RRM_RCAN_like, RNA recognition motif (RRM) found in regulators of calcineurin (RCANs) and similar proteins. This subfamily corresponds to the RRM of RCANs, a novel family of calcineurin regulators that are key factors contributing to Down syndrome in humans. They can stimulate and inhibit the Ca2+/calmodulin-dependent phosphatase calcineurin (also termed PP2B or PP3C) signaling in vivo through direct interactions with its catalytic subunit. Overexpressed RCANs may bind and inhibit calcineurin. In contrast, low levels of phosphorylated RCANs may stimulate the calcineurin signaling. RCANs are characterized by harboring a central short, unique serine-proline motif containing FLIISPPxSPP box, which is strongly conserved from yeast to human but is absent in bacteria. They consist of an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a highly conserved SP repeat domain containing the phosphorylation site by GSK-3, a well-known PxIxIT motif responsible for docking many substrates to calcineurin, and an unrecognized C-terminal TxxP motif of unknown function
LIVTNVPSEVFDNAELKEAFESLFRTYGEIATFVYLKSFRRARVIFSSPEEAALARIELHGTVFLGSELR
VYFGQ
>gnl|CDD|409869 cd12435, RRM_GW182_like, RNA recognition motif (RRM) found in the GW182 family proteins. This subfamily corresponds to the RRM of the GW182 family which includes three paralogs of TNRC6 (GW182-related) proteins comprising GW182/TNGW1, TNRC6B (containing three isoforms) and TNRC6C in mammal, a single Drosophila ortholog (dGW182, also called Gawky) and two Caenorhabditis elegans orthologs AIN-1 and AIN-2, which contain multiple miRNA-binding sites and have important functions in miRNA-mediated translational repression, as well as mRNA degradation in Metazoa. The GW182 family proteins directly interact with Argonaute (Ago) proteins, and thus function as downstream effectors in the miRNA pathway, responsible for inhibition of translation and acceleration of mRNA decay. Members in this family are characterized by an abnormally high content of glycine/tryptophan (G/W) repeats, one or more glutamine (Q)-rich motifs, and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The only exception is the worm protein that does not contain a recognizable RRM domain. The GW182 family proteins are recruited to miRNA targets through an interaction between their N-terminal domain and an Argonaute protein. Then they promote translational repression and/or degradation of miRNA targets through their C-terminal silencing domain
SNWLVLRNLTPQIDGSTLRTLCMQHGPLLTFHLNLNHGNALIRYSSREEAAKAQKALNMCVLGNTTILAD
F
>gnl|CDD|409870 cd12436, RRM1_2_MATR3_like, RNA recognition motif 1 (RRM1) and 2 (RRM2) found in the matrin 3 family of nuclear proteins. This subfamily corresponds to the RRM of the matrin 3 family of nuclear proteins consisting of Matrin 3 (MATR3), nuclear protein 220 (NP220) and similar proteins. MATR3 is a highly conserved inner nuclear matrix protein that has been implicated in various biological processes. NP220 is a large nucleoplasmic DNA-binding protein that binds to cytidine-rich sequences, such as CCCCC (G/C), in double-stranded DNA (dsDNA). Both, Matrin 3 and NP220, contain two RNA recognition motif (RRM), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a Cys2-His2 zinc finger-like motif at the C-terminal region
RVLYLTGLPVSKYSEEDVLKLAEPFGKVNNVLLIRSKREAFIEMETAEDAQAMLSYCKTKPITIKGKKVK
VSVSQK
>gnl|CDD|409871 cd12437, RRM_BRAP2_like, RNA recognition motif (RRM) found in BRCA1-associated protein (BRAP2) and similar proteins. This subfamily corresponds to the RRM domain of BRAP2, also termed impedes mitogenic signal propagation (IMP), or ring finger protein 52, or renal carcinoma antigen NY-REN-63, a novel cytoplasmic protein interacting with the two functional nuclear localisation signal (NLS) motifs of BRCA1, a nuclear protein linked to breast cancer. It also binds to the SV40 large T antigen NLS motif and the bipartite NLS motif found in mitosin. BRAP2 may serve as a cytoplasmic retention protein and play a role in the regulation of nuclear protein transport. The family also includes RING finger protein ETP1 and its homologs found in fungi. ETP1, also termed BRAP2 homolog, or ethanol tolerance protein 1, is the yeast homolog of BRCA1-associated protein (BRAP2) found in vertebrates. It may be involved in ethanol and salt-induced transcriptional activation of the NHA1 promoter and heat shock protein genes (HSP12 and HSP26), and participate in ethanol-induced turnover of the low-affinity hexose transporter Hxt3p. Members in this family contain an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C3HC4-type ring finger domain and a UBP-type zinc finger
LCILAVPSYMTVADFCQFVGPFIEHISHMRILRDDGPGNRYMVLLRFDSQESADSFYQDFNGKPFSSLEP
EVCHVLFVKSVE
>gnl|CDD|409872 cd12438, RRM_CNOT4, RNA recognition motif (RRM) found in Eukaryotic CCR4-NOT transcription complex subunit 4 (NOT4) and similar proteins. This subfamily corresponds to the RRM of NOT4, also termed CCR4-associated factor 4, or E3 ubiquitin-protein ligase CNOT4, or potential transcriptional repressor NOT4Hp, a component of the CCR4-NOT complex, a global negative regulator of RNA polymerase II transcription. NOT4 functions as an ubiquitin-protein ligase (E3). It contains an N-terminal C4C4 type RING finger motif, followed by a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The RING fingers may interact with a subset of ubiquitin-conjugating enzymes (E2s), including UbcH5B, and mediate protein-protein interactions. T
RVVQKNLVYVVGLPPRLADEEVLKRPEYFGQYGKIKKIVINRSTSYAGSQGPSASAYVTYSRKEDALRAI
QAVDGFVLDGRTLKASFGTTKYCSSFLR
>gnl|CDD|409873 cd12439, RRM_TRMT2A, RNA recognition motif (RRM) found in tRNA (uracil-5-)-methyltransferase homolog A (TRMT2A) and similar proteins. This subfamily corresponds to the RRM of TRMT2A, also known as HpaII tiny fragments locus 9c protein (HTF9C), a novel cell cycle regulated protein. It is an independent biologic factor expressed in tumors associated with clinical outcome in HER2 expressing breast cancer. The function of TRMT2A remains unclear although by sequence homology it has a RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), related to RNA methyltransferases
FTSEIFKIEIKNLPKYIGFGQLKKFLQKLGLKPHKIKLIGRQTFAFVTFRNEEDRDKALKVLNGHKWKGK
VLSAKLAKP
>gnl|CDD|409874 cd12440, RRM_SYNJ, RNA recognition motif (RRM) found in synaptojanin-1, synaptojanin-2 and similar proteins. This subfamily corresponds to the RRM of two active phosphatidylinositol phosphate phosphatases, synaptojanin-1 and synaptojanin-2. They have different interaction partners and are likely to have different biological functions. Synaptojanin-1 was originally identified as one of the major Grb2-binding proteins that may participate in synaptic vesicle endocytosis. It also acts as a Src homology 3 (SH3) domain-binding brain-specific inositol 5-phosphatase with a putative role in clathrin-mediated endocytosis. Synaptojanin-2 is a ubiquitously expressed homolog of synaptojanin-1. It is a novel Rac1 effector regulating the early step of clathrin-mediated endocytosis. Synaptojanin-2 directly and specifically interacts with Rac1 in a GTP-dependent manner. It mediates the inhibitory effect of Rac1 on endocytosis and plays an important role in the Rac1-mediated control of cell growth. Both, synaptojanin-1 and synaptojanin-2, have two tissue-specific alternative splicing isoforms, a shorter isoform expressed in brain and a longer isoform in peripheral tissues. Synaptojanin-1 contains an N-terminal domain homologous to the cytoplasmic portion of the yeast protein Sac1p, a central inositol 5-phosphatase domain followed by a putative RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal proline-rich region mediating the binding of synaptojanin-1 to various SH3 domain-containing proteins including amphiphysin, SH3p4, SH3p8, SH3p13, and Grb2. Synaptojanin-2 shows high sequence homology to the N-terminal Sac1p homology domain, the central inositol 5-phosphatase domain, the putative RNA recognition motif (RRM) of synaptojanin-1, but differs in the proline-rich region
DATVVVSLDSKSEEWNEFEDALIGELLRVLASYGDVVLVRFAHEGMLVTFRDGRSALAALALNGKQILGR
TLKIRLK
>gnl|CDD|409875 cd12441, RRM_Nup53_like, RNA recognition motif (RRM) found in nucleoporin Nup53 and similar proteins. This subfamily corresponds to the RRM domain of nucleoporin Nup53, also termed mitotic phosphoprotein 44 (MP-44), or nuclear pore complex protein Nup53, required for normal cell growth and nuclear morphology in vertebrate. It tightly associates with the nuclear envelope membrane and the nuclear lamina where it interacts with lamin B. It may also interact with a group of nucleoporins including Nup93, Nup155, and Nup205 and play a role in the association of the mitotic checkpoint protein Mad1 with the nuclear pore complex (NPC). The family also includes Saccharomyces cerevisiae Nup53p, an ortholog of vertebrate nucleoporin Nup53. A unique property of yeast Nup53p is that it contains an additional Kap121p-binding domain and interacts specifically with the karyopherin Kap121p, which is involved in the assembly of Nup53p into NPCs. Both, vertebrate Nup35 and yeast Nup53p, contain an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a C-terminal amphipathic alpha-helix and several FG repeats. This family corresponds to the RRM domain which lacks the conserved residues that typically bind RNA in canonical RRM domains
DTWVTVFGFPPSNASLVLREFSKCGDIVEHEYPPGGNWIHIRYENRLQAERALSKNGRVLNGNVMIGVKP
CTD
>gnl|CDD|409876 cd12442, RRM_RBM48, RNA recognition motif (RRM) found in RNA-binding protein 48 (RBM48) and similar proteins. This subfamily corresponds to the RRM of RBM48, a putative RNA-binding protein of unknown function. It contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
VKVYTVNQESRYLLVQGVPALGVEEELLKLFSLYGTIEEYRILDEYPCEEFTEVYLIKFERIQSARFAKR
KLDDHSFFGGILHVCYAPEYETVEDTREKL
>gnl|CDD|409877 cd12443, RRM_MCM3A_like, RNA recognition motif (RRM) found in 80 kDa MCM3-associated protein (Map80) and similar proteins. This subfamily corresponds to the RRM of Map80, also termed germinal center-associated nuclear protein (GANP), involved in the nuclear localization pathway of MCM3, a protein necessary for the initiation of DNA replication and also involves in controls that ensure DNA replication is initiated once per cell cycle. Map80 contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
TAIVCKNIPEELNDKEILRRHFSKFGKVARVFCNPRKNLAIVHFKDHESAALAKKKGKLLSKGGKPIEIF
WSSKK
>gnl|CDD|409878 cd12444, RRM1_CPEBs, RNA recognition motif 1 (RRM1) found in cytoplasmic polyadenylation element-binding protein CPEB-1, CPEB-2, CPEB-3, CPEB-4 and similar protiens. This subfamily corresponds to the RRM1 of the CPEB family of proteins that bind to defined groups of mRNAs and act as either translational repressors or activators to regulate their translation. CPEB proteins are well conserved in both, vertebrates and invertebrates. Based on sequence similarity, RNA-binding specificity, and functional regulation of translation, the CPEB proteins have been classified into two subfamilies. The first subfamily includes CPEB-1 and related proteins. CPEB-1 is an RNA-binding protein that interacts with the cytoplasmic polyadenylation element (CPE), a short U-rich motif in the 3' untranslated regions (UTRs) of certain mRNAs. It functions as a translational regulator that plays a major role in the control of maternal CPE-containing mRNA in oocytes, as well as of subsynaptic CPE-containing mRNA in neurons. Once phosphorylated and recruiting the polyadenylation complex, CPEB-1 may function as a translational activator stimulating polyadenylation and translation. Otherwise, it may function as a translational inhibitor when dephosphorylated and bind to a protein such as maskin or neuroguidin, which blocks translation initiation through interfering with the assembly of eIF-4E and eIF-4G. Although CPEB-1 is mainly located in cytoplasm, it can shuttle between nucleus and cytoplasm. The second subfamily includes CPEB-2, CPEB-3, CPEB-4, and related protiens. Due to high sequence similarity, members in this subfamily may share similar expression patterns and functions. CPEB-2 is an RNA-binding protein that is abundantly expressed in testis and localized in cytoplasm in transfected HeLa cells. It preferentially binds to poly(U) RNA oligomers and may regulate the translation of stored mRNAs during spermiogenesis. CPEB-2 impedes target RNA translation at elongation; it directly interacts with the elongation factor, eEF2, to reduce eEF2/ribosome-activated GTP hydrolysis in vitro and inhibit peptide elongation of CPEB2-bound RNA in vivo. CPEB-3 is a sequence-specific translational regulatory protein that regulates translation in a polyadenylation-independent manner. It functions as a translational repressor that governs the synthesis of the AMPA receptor GluR2 through binding GluR2 mRNA. It also represses translation of a reporter RNA in transfected neurons and stimulates translation in response to NMDA. CPEB-4 is an RNA-binding protein that mediates meiotic mRNA cytoplasmic polyadenylation and translation. It is essential for neuron survival and present on the endoplasmic reticulum (ER). It is accumulated in the nucleus upon ischemia or the depletion of ER calcium. CPEB-4 is overexpressed in a large variety of tumors and is associated with many mRNAs in cancer cells. All CPEB proteins are nucleus-cytoplasm shuttling proteins. They contain an N-terminal unstructured region, followed by two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a Zn-finger motif. CPEB-2, -3, and -4 have conserved nuclear export signals that are not present in CPEB-1
RKVFLGGVPWDITEAELTASFRRFGSLSVDWPGKDESKSYFPPKGYVYLLFESEKSVQALLQACTHDDDK
LYEYYFKVSSRTMKDKEVQVIPWVL
>gnl|CDD|409879 cd12445, RRM2_CPEBs, RNA recognition motif 2 (RRM2) found in cytoplasmic polyadenylation element-binding protein CPEB-1, CPEB-2, CPEB-3, CPEB-4 and similar protiens. This subfamily corresponds to the RRM2 of CPEB family of proteins that bind to defined groups of mRNAs and act as either translational repressors or activators to regulate their translation. CPEB proteins are well conserved in both, vertebrates and invertebrates. Based on sequence similarity, RNA-binding specificity, and functional regulation of translation, the CPEB proteins has been classified into two subfamilies. The first subfamily includes CPEB-1 and related proteins. CPEB-1 is an RNA-binding protein that interacts with the cytoplasmic polyadenylation element (CPE), a short U-rich motif in the 3' untranslated regions (UTRs) of certain mRNAs. It functions as a translational regulator that plays a major role in the control of maternal CPE-containing mRNA in oocytes, as well as of subsynaptic CPE-containing mRNA in neurons. Once phosphorylated and recruiting the polyadenylation complex, CPEB-1 may function as a translational activator stimulating polyadenylation and translation. Otherwise, it may function as a translational inhibitor when dephosphorylated and bound to a protein such as maskin or neuroguidin, which blocks translation initiation through interfering with the assembly of eIF-4E and eIF-4G. Although CPEB-1 is mainly located in cytoplasm, it can shuttle between nucleus and cytoplasm. The second subfamily includes CPEB-2, CPEB-3, CPEB-4, and related protiens. Due to the high sequence similarity, members in this subfamily may share similar expression patterns and functions. CPEB-2 is an RNA-binding protein that is abundantly expressed in testis and localized in cytoplasm in transfected HeLa cells. It preferentially binds to poly(U) RNA oligomers and may regulate the translation of stored mRNAs during spermiogenesis. Moreover, CPEB-2 impedes target RNA translation at elongation. It directly interacts with the elongation factor, eEF2, to reduce eEF2/ribosome-activated GTP hydrolysis in vitro and inhibit peptide elongation of CPEB2-bound RNA in vivo. CPEB-3 is a sequence-specific translational regulatory protein that regulates translation in a polyadenylation-independent manner. It functions as a translational repressor that governs the synthesis of the AMPA receptor GluR2 through binding GluR2 mRNA. It also represses translation of a reporter RNA in transfected neurons and stimulates translation in response to NMDA. CPEB-4 is an RNA-binding protein that mediates meiotic mRNA cytoplasmic polyadenylation and translation. It is essential for neuron survival and present on the endoplasmic reticulum (ER). It is accumulated in the nucleus upon ischemia or the depletion of ER calcium. CPEB-4 is overexpressed in a large variety of tumors and is associated with many mRNAs in cancer cells. All CPEB proteins are nucleus-cytoplasm shuttling proteins. They contain an N-terminal unstructured region, followed by two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a Zn-finger motif. CPEB-2, -3, and -4 have conserved nuclear export signals that are not present in CPEB-1
RTVFVGGLPLPLTAAELAAILERLYGGVCYVEIDTDEFYLYPTGCARVTFNNEQSYIKAVSEVFVELPFG
TINKRVRIRPY
>gnl|CDD|409880 cd12446, RRM_RBM25, RNA recognition motif (RRM) found in eukaryotic RNA-binding protein 25 and similar proteins. This subfamily corresponds to the RRM of RBM25, also termed Arg/Glu/Asp-rich protein of 120 kDa (RED120), or protein S164, or RNA-binding region-containing protein 7, an evolutionary-conserved splicing coactivator SRm160 (SR-related nuclear matrix protein of 160 kDa, )-interacting protein. RBM25 belongs to a family of RNA-binding proteins containing a well conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), at the N-terminus, a RE/RD-rich (ER) central region, and a C-terminal proline-tryptophan-isoleucine (PWI) motif. It localizes to the nuclear speckles and associates with multiple splicing components, including splicing cofactors SRm160/300, U snRNAs, assembled splicing complexes, and spliced mRNAs. It may play an important role in pre-mRNA processing by coupling splicing with mRNA 3'-end formation. Additional research indicates that RBM25 is one of the RNA-binding regulators that direct the alternative splicing of apoptotic factors. It can activate proapoptotic Bcl-xS 5'ss by binding to the exonic splicing enhancer, CGGGCA, and stabilize the pre-mRNA-U1 snRNP through interaction with hLuc7A, a U1 snRNP-associated factor
TTVFVGNIPDDVSDDFIRQLLEKCGKVLSWKRVQDPSGKLKAFGFCEFEDPEGALRALRLLNGLELGGKK
LLVKVDAKTKKFL
>gnl|CDD|409881 cd12447, RRM1_gar2, RNA recognition motif 1 (RRM1) found in yeast protein gar2 and similar proteins. This subfamily corresponds to the RRM1 of yeast protein gar2, a novel nucleolar protein required for 18S rRNA and 40S ribosomal subunit accumulation. It shares similar domain architecture with nucleolin from vertebrates and NSR1 from Saccharomyces cerevisiae. The highly phosphorylated N-terminal domain of gar2 is made up of highly acidic regions separated from each other by basic sequences, and contains multiple phosphorylation sites. The central domain of gar2 contains two closely adjacent N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The C-terminal RGG (or GAR) domain of gar2 is rich in glycine, arginine and phenylalanine residues
TLFVGGLSWNVDDPWLKKEFEKYGGVISARVITDRGSGRSKGYGYVDFATPEAAQKALAAMSGKEIDGRQ
INVDFS
>gnl|CDD|409882 cd12448, RRM2_gar2, RNA recognition motif 2 (RRM2) found in yeast protein gar2 and similar proteins. This subfamily corresponds to the RRM2 of yeast protein gar2, a novel nucleolar protein required for 18S rRNA and 40S ribosomal subunit accumulation. It shares similar domain architecture with nucleolin from vertebrates and NSR1 from Saccharomyces cerevisiae. The highly phosphorylated N-terminal domain of gar2 is made up of highly acidic regions separated from each other by basic sequences, and contains multiple phosphorylation sites. The central domain of gar2 contains two closely adjacent N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The C-terminal RGG (or GAR) domain of gar2 is rich in glycine, arginine and phenylalanine residues
LFVGNLPFSATQDALYEAFSQHGSIVSVRLPTDRETGQPKGFGYVDFSTIDSAEAAIDALGGEYIDGRPI
RLD
>gnl|CDD|409883 cd12449, RRM_CIRBP_RBM3, RNA recognition motif (RRM) found in cold inducible RNA binding protein (CIRBP), RNA binding motif protein 3 (RBM3) and similar proteins. This subfamily corresponds to the RRM domain of two structurally related heterogenous nuclear ribonucleoproteins, CIRBP (also termed CIRP or A18 hnRNP) and RBM3 (also termed RNPL), both of which belong to a highly conserved cold shock proteins family. The cold shock proteins can be induced after exposure to a moderate cold-shock and other cellular stresses such as UV radiation and hypoxia. CIRBP and RBM3 may function in posttranscriptional regulation of gene expression by binding to different transcripts, thus allowing the cell to response rapidly to environmental signals. However, the kinetics and degree of cold induction are different between CIRBP and RBM3. Tissue distribution of their expression is different. CIRBP and RBM3 may be differentially regulated under physiological and stress conditions and may play distinct roles in cold responses of cells. CIRBP, also termed glycine-rich RNA-binding protein CIRP, is localized in the nucleus and mediates the cold-induced suppression of cell cycle progression. CIRBP also binds DNA and possibly serves as a chaperone that assists in the folding/unfolding, assembly/disassembly and transport of various proteins. RBM3 may enhance global protein synthesis and the formation of active polysomes while reducing the levels of ribonucleoprotein complexes containing microRNAs. RBM3 may also serve to prevent the loss of muscle mass by its ability to decrease cell death. Furthermore, RBM3 may be essential for cell proliferation and mitosis. Both, CIRBP and RBM3, contain an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), that is involved in RNA binding, and C-terminal glycine-rich domain (RGG motif) that probably enhances RNA-binding via protein-protein and/or protein-RNA interactions. Like CIRBP, RBM3 can also bind to both RNA and DNA via its RRM domain
GKLFVGGLSFDTNEQSLEEVFSKYGQISEVVVVKDRETQRSRGFGFVTFENPDDAKDAMMAMNGKSLDGR
QIRVDQAGKS
>gnl|CDD|409884 cd12450, RRM1_NUCLs, RNA recognition motif 1 (RRM1) found in nucleolin-like proteins mainly from plants. This subfamily corresponds to the RRM1 of a group of plant nucleolin-like proteins, including nucleolin 1 (also termed protein nucleolin like 1) and nucleolin 2 (also termed protein nucleolin like 2, or protein parallel like 1). They play roles in the regulation of ribosome synthesis and in the growth and development of plants. Like yeast nucleolin, nucleolin-like proteins possess two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
TLFVGNLSWSATQDDLENFFSDCGEVVDVRIAMDRDDGRSKGFGHVEFASAESAQKALEKSGQDLGGREI
RLDLANER
>gnl|CDD|409885 cd12451, RRM2_NUCLs, RNA recognition motif 2 (RRM2) found in nucleolin-like proteins mainly from plants. This subfamily corresponds to the RRM2 of a group of plant nucleolin-like proteins, including nucleolin 1 (also termed protein nucleolin like 1) and nucleolin 2 (also termed protein nucleolin like 2, or protein parallel like 1). They play roles in the regulation of ribosome synthesis and in the growth and development of plants. Like yeast nucleolin, nucleolin-like proteins possess two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
TIFVKGFDASLGEDTIRDELREHFGECGEVTNVRIPTDRETGELKGFAYIEFSTKEAKEKALELNGSDIA
GGNLVVDEA
>gnl|CDD|409886 cd12452, RRM_ARP_like, RNA recognition motif (RRM) found in yeast asparagine-rich protein (ARP) and similar proteins. This subfamily corresponds to the RRM of ARP, also termed NRP1, encoded by Saccharomyces cerevisiae YDL167C. Although its exact biological function remains unclear, ARP contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), two Ran-binding protein zinc fingers (zf-RanBP), and an asparagine-rich region. It may possess RNA-binding and zinc ion binding activities. Additional research had indicated that ARP may function as a factor involved in the stress response
KILYMNGLPHDTTQSELESWFTQHGVRPVAFWTLKTPEQIKPSGSGFAVFQSHEEAAESLALNGRALGDR
AIEVQPSSSRVLE
>gnl|CDD|409887 cd12453, RRM1_RIM4_like, RNA recognition motif 1 (RRM1) found in yeast meiotic activator RIM4 and similar proteins. This subfamily corresponds to the RRM1 of RIM4, also termed regulator of IME2 protein 4, a putative RNA binding protein that is expressed at elevated levels early in meiosis. It functions as a meiotic activator required for both the IME1- and IME2-dependent pathways of meiotic gene expression, as well as early events of meiosis, such as meiotic division and recombination, in Saccharomyces cerevisiae. RIM4 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The family also includes a putative RNA-binding protein termed multicopy suppressor of sporulation protein Msa1. It is a putative RNA-binding protein encoded by a novel gene, msa1, from the fission yeast Schizosaccharomyces pombe. Msa1 may be involved in the inhibition of sexual differentiation by controlling the expression of Ste11-regulated genes, possibly through the pheromone-signaling pathway. Like RIM4, Msa1 also contains two RRMs, both of which are essential for the function of Msa1
PSACLFVASLSSARSDEELCAAVTNHFSKWGELLNVKVLKDWSNRPYAFVQYTNTEDAKNALVNGHNTLL
DGRHLRVEKAKVNRTL
>gnl|CDD|409888 cd12454, RRM2_RIM4_like, RNA recognition motif 2 (RRM2) found in yeast meiotic activator RIM4 and similar proteins. This subfamily corresponds to the RRM2 of RIM4, also termed regulator of IME2 protein 4, a putative RNA binding protein that is expressed at elevated levels early in meiosis. It functions as a meiotic activator required for both the IME1- and IME2-dependent pathways of meiotic gene expression, as well as early events of meiosis, such as meiotic division and recombination, in Saccharomyces cerevisiae. RIM4 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The family also includes a putative RNA-binding protein termed multicopy suppressor of sporulation protein Msa1. It is a putative RNA-binding protein encoded by a novel gene, msa1, from the fission yeast Schizosaccharomyces pombe. Msa1 may be involved in the inhibition of sexual differentiation by controlling the expression of Ste11-regulated genes, possibly through the pheromone-signaling pathway. Like RIM4, Msa1 also contains two RRMs, both of which are essential for the function of Msa1
IDKLSIFVGQLDPKTTDSELFRRFSKYGKIVDCKLIKRPEPVNAFAFLRFESEEAAEAAVEEENHSEFLN
KQIRVQKREL
>gnl|CDD|409889 cd12455, RRM_like_Smg4_UPF3, RNA recognition motif (RRM)-like Smg4_UPF3 domain in yeast up-frameshift suppressor 3 (Upf3p), Caenorhabditis elegans SMG-4, their human orthologs Upf3A and Upf3B, and similar proteins. This subfamily corresponds to the RRM-like Smg4_UPF3 domain found in yeast up-frameshift suppressor 3 (Upf3p), Caenorhabditis elegans SMG-4, their human orthologs Upf3A and Upf3B, and similar proteins. Upf3p, also termed nonsense-mediated mRNA decay protein 3, or Sua6p, a surveillance factor encoded by UPF3 gene from Saccharomyces cerevisiae. It is required for nonsense-mediated mRNA decay (NMD) in yeast. Upf3p is primarily cytoplasmic but accumulates inside the nucleus. Its nuclear import is mediated by the Srp1p (importin-alpha)/beta heterodimer while its nuclear export is mediated by a leucine-rich nuclear export sequence (NES-A), but not the Crm1p exportin. C. elegans SMG-4 is a nuclear shuttling protein that shuttles between the cytoplasm and nucleus through nuclear import and export signals similar to that of the yeast Upf3p. It is regulated by phosphorylation. Human orthologs of yeast Upf3p and C. elegans SMG-4 include Upf3A and Upf3B, which derive from two genes, UPF3A and X-linked UPF3B, respectively. Both, Upf3A (Up-frameshift suppressor 3 homolog A, also termed regulator of nonsense transcripts 3A, or nonsense mRNA reducing factor 3A) and Upf3B (Up-frameshift suppressor 3 homolog B on chromosome X, also termed regulator of nonsense transcripts 3B, or nonsense mRNA reducing factor 3B), are nucleocytoplasmic shuttling proteins. They associate selectively with spliced beta-globin mRNA in vivo, and tethering of any human Upf protein to the 3'UTR of beta-globin mRNA prevents NMD. The function of the Upf proteins in identifying and targeting nonsense mRNAs for rapid decay is conserved among eukaryotes. Besides, all Upf proteins in this family contain a conserved Smg4_UPF3 domain with some similarity to an RNA recognition motif (RRM), indicating that they may be RNA binding proteins
KVVIRRLPPSLTEEEFLEQIAPLIKPTVDWFYFVGGKSSLDFKPPTYSRAYINFKNPEDLIEFRRKFDGY
VFVDSKGNEYPAIVEFAP
>gnl|CDD|240902 cd12456, RRM_p65, RNA recognition motif (RRM) found in the holoenzyme La family protein p65. This subfamily corresponds to the RRM of a lineage specific family containing the essential La family protein p65 found in Tetrahymena thermophila. It is a telomerase holoenzyme protein necessary for telomerase RNA (TER) accumulation in vivo. p65, together with TER and telomerase reverse transcriptase (TERT), comprise a ternary catalytic core complex of Tetrahymena telomerase, which is a ribonucleoprotein complex essential for maintenance of telomere DNA at linear chromosome ends. p65 harbors a cryptic, atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), which displays high structural homology to the RRM in genuine La and LARP7 proteins
NCLIKIINIPQGTLKAEVVLAVRHLGYEFYCDYIDGQAMIRFQNSDEQRLAIQKLLNHNNNKLQIEIRGQ
ICDVIS
>gnl|CDD|409890 cd12457, RRM_XMAS2, RNA recognition motif (RRM) found in X-linked male sterile 2 (Xmas-2) and similar proteins. This subfamily corresponds to the RRM in Xmas-2, the Drosophila homolog of yeast Sac3p protein, together with E(y)2, the Drosophila homologue of yeast Sus1p protein, forming an endogenous complex that is required in the regulation of mRNA transport and also involved in the efficient transcription regulation of the heat-shock protein 70 (hsp70) loci. All family members are found in insects and contain an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a PCI domain
KSITCTDVPEELLDKTAAKEYFRKFGKIKKITLRPKRRTCTVEYTNKEEAERALLNGGEYNGHMFDVEWT
K
>gnl|CDD|409891 cd12458, RRM_AtC3H46_like, RNA recognition motif (RRM) found in Arabidopsis thaliana zinc finger CCCH domain-containing protein 46 (AtC3H46) and similar proteins. This subfamily corresponds to the RRM domain in AtC3H46, a putative RNA-binding protein that contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a CCCH class of zinc finger, typically C-X8-C-X5-C-X3-H. It may possess ribonuclease activity
IYLTFPAESSFTEEDVSTYFSSFGPVQDVRIPYQQKRMFGFVTFANAETVKTILAEGNPHFICDSRVLVK
>gnl|CDD|409892 cd12459, RRM1_CID8_like, RNA recognition motif 1 (RRM1) found in Arabidopsis thaliana CTC-interacting domain protein CID8, CID9, CID10, CID11, CID12, CID 13 and similar proteins. This subgroup corresponds to the RRM1 domains found in A. thaliana CID8, CID9, CID10, CID11, CID12, CID 13 and mainly their plant homologs. These highly related RNA-binding proteins contain an N-terminal PAM2 domain (PABP-interacting motif 2), two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a basic region that resembles a bipartite nuclear localization signal. The biological role of this family remains unclear
IRRTVYVSDIDQQVTEEQLAALFSNCGQVVDCRICGDPNSVLRFAFIEFTDEEGARAALSLSGTMLGFYP
VRVLPSKTAI
>gnl|CDD|409893 cd12460, RRM2_CID8_like, RNA recognition motif 2 (RRM2) found in Arabidopsis thaliana CTC-interacting domain protein CID8, CID9, CID10, CID11, CID12, CID 13 and similar proteins. This subgroup corresponds to the RRM2 domains found in A. thaliana CID8, CID9, CID10, CID11, CID12, CID 13 and mainly their plant homologs. These highly related RNA-binding proteins contain an N-terminal PAM2 domain (PABP-interacting motif 2), two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a basic region that resembles a bipartite nuclear localization signal. The biological role of this family remains unclear
EMCARTIYCTNIDKKVTQDDVKAFFESLCGEVHRLRLLGDYVHSTRIAFVEFVMAESAIAALNCSGALLG
SLPIRVSPSKTP
>gnl|CDD|409894 cd12461, RRM_SCAF4, RNA recognition motif (RRM) found in SR-related and CTD-associated factor 4 (SCAF4) and similar proteins. The CD corresponds to the RRM of SCAF4 (also termed splicing factor, arginine/serine-rich 15 or SFR15, or CTD-binding SR-like protein RA4) that belongs to a new class of SCAFs (SR-like CTD-associated factors). Although its biological function remains unclear, SCAF4 shows high sequence similarity to SCAF8 that interacts specifically with a highly serine-phosphorylated form of the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II (pol II) and may play a direct role in coupling with both, transcription and pre-mRNA processing, processes. SCAF4 and SCAF8 both contain a conserved N-terminal CTD-interacting domain (CID), an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and serine/arginine-rich motifs
SVCSTTLWVGQLDKRTTQQDVASLLEEFGQIESINMIPPRGCAYIVMVHRQDAYRALQKLSRGNYKVNQK
SIKIAWALNKG
>gnl|CDD|409895 cd12462, RRM_SCAF8, RNA recognition motif (RRM) found in SR-related and CTD-associated factor 8 (SCAF8) and similar proteins. This subgroup corresponds to the RRM of SCAF8 (also termed CDC5L complex-associated protein 7, or RNA-binding motif protein 16, or CTD-binding SR-like protein RA8), a nuclear matrix protein that interacts specifically with a highly serine-phosphorylated form of the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II (pol II). The pol II CTD plays a role in coupling transcription and pre-mRNA processing. SCAF8 co-localizes primarily with transcription sites that are enriched in nuclear matrix fraction, which is known to contain proteins involved in pre-mRNA processing. Thus, SCAF8 may play a direct role in coupling with both, transcription and pre-mRNA processing, processes. SCAF8, together with SCAF4, represents a new class of SCAFs (SR-like CTD-associated factors). They contain a conserved N-terminal CTD-interacting domain (CID), an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and serine/arginine-rich motifs
CSTTLWVGQVDKKATQQDLTNLFEEFGQIESINMIPPRGCAYVCMVHRQDAYRALQKLSTGSFKIGSKII
KIAWALNKG
>gnl|CDD|409896 cd12463, RRM_G3BP1, RNA recognition motif (RRM) found in ras GTPase-activating protein-binding protein 1 (G3BP1) and similar proteins. This subgroup corresponds to the RRM of G3BP1, also termed ATP-dependent DNA helicase VIII (DH VIII), or GAP SH3 domain-binding protein 1, which has been identified as a phosphorylation-dependent endoribonuclease that interacts with the SH3 domain of RasGAP, a multi-functional protein controlling Ras activity. The acidic RasGAP binding domain of G3BP1 harbors an arsenite-regulated phosphorylation site and dominantly inhibits stress granule (SG) formation. G3BP1 also contains an N-terminal nuclear transfer factor 2 (NTF2)-like domain, an RNA recognition motif (RRM domain), and an Arg-Gly-rich region (RGG-rich region, or arginine methylation motif). The RRM domain and RGG-rich region are canonically associated with RNA binding. G3BP1 co-immunoprecipitates with mRNAs. It binds to and cleaves the 3'-untranslated region (3'-UTR) of the c-myc mRNA in a phosphorylation-dependent manner. Thus, G3BP1 may play a role in coupling extra-cellular stimuli to mRNA stability. It has been shown that G3BP1 is a novel Dishevelled-associated protein that is methylated upon Wnt3a stimulation and that arginine methylation of G3BP1 regulates both Ctnnb1 mRNA and canonical Wnt/beta-catenin signaling. Furthermore, G3BP1 can be associated with the 3'-UTR of beta-F1 mRNA in cytoplasmic RNA-granules, demonstrating that G3BP1 may specifically repress the translation of the transcript
PDSHQLFVGNLPHDVDKSELKEFFQGYGNVVELRINSGGKLPNFGFVVFDDPEPVQKILSNRPIKFRGEV
RLNVEEKKTR
>gnl|CDD|409897 cd12464, RRM_G3BP2, RNA recognition motif (RRM) found in ras GTPase-activating protein-binding protein 2 (G3BP2) and similar proteins. This subgroup corresponds to the RRM of G3BP2, also termed GAP SH3 domain-binding protein 2, a cytoplasmic protein that interacts with both IkappaBalpha and IkappaBalpha/NF-kappaB complexes, indicating that G3BP2 may play a role in the control of nucleocytoplasmic distribution of IkappaBalpha and cytoplasmic anchoring of the IkappaBalpha/NF-kappaB complex. G3BP2 contains an N-terminal nuclear transfer factor 2 (NTF2)-like domain, an acidic domain, a domain containing five PXXP motifs, an RNA recognition motif (RRM domain), and an Arg-Gly-rich region (RGG-rich region, or arginine methylation motif). It binds to the SH3 domain of RasGAP, a multi-functional protein controlling Ras activity, through its N-terminal NTF2-like domain. The acidic domain is sufficient for the interaction of G3BP2 with the IkappaBalpha cytoplasmic retention sequence. Furthermore, G3BP2 might influence stability or translational efficiency of particular mRNAs by binding to RNA-containing structures within the cytoplasm through its RNA-binding domain
RYPDSHQLFVGNLPHDIDENELKEFFMSFGNVVELRINTKGVGGKLPNFGFVVFDDSDPVQRILNAKPIM
FRGEVRLNVEEKK
>gnl|CDD|409898 cd12465, RRM_UHMK1, RNA recognition motif (RRM) found in U2AF homology motif kinase 1 (UHMK1) and similar proteins. This subgroup corresponds to the RRM of UHMK1. UHMK1, also termed kinase interacting with stathmin (KIS) or P-CIP2, is a serine/threonine protein kinase functionally related to RNA metabolism and neurite outgrowth. It contains an N-terminal kinase domain and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), with high homology to the corresponding motif of the mammalian U2 small nuclear ribonucleoprotein auxiliary factor U2AF 65 kDa subunit (U2AF65 or U2AF2). UHMK1 targets two key regulators of cell proliferation and migration, the cyclin-dependent kinase (CDK) inhibitor p27Kip1 and the microtubule-destabilizing protein stathmin. It plays a critical role during vascular wound repair by preventing excessive vascular smooth muscle cell (VSMC) migration into the vascular lesion. Moreover, UHMK1 may control cell migration and neurite outgrowth by interacting with and phosphorylating the splicing factor SF1, thereby probably contributing to the control of protein expression. Furthermore, UHMK1 may be functionally related to microtubule dynamics and axon development. It localizes to RNA granules, interacts with three proteins found in RNA granules (KIF3A, NonO, and eEF1A), and further enhances the local translation. UHMK1 is highly expressed in regions of the brain implicated in schizophrenia and may play a role in susceptibility to schizophrenia
LPTPVLRLLNVIDDSYLQSEEEYEDIVEDVREECQKYGPVVSLLIPKENPGKGQVFVEYANAGDSKAAQK
MLTGRMFDGKFVVATFYP
>gnl|CDD|409899 cd12466, RRM2_AtRSp31_like, RNA recognition motif 2 (RRM2) found in Arabidopsis thaliana arginine/serine-rich-splicing factor RSp31 and similar proteins from plants. This subgroup corresponds to the RRM2 in a family that represents a novel group of arginine/serine (RS) or serine/arginine (SR) splicing factors existing in plants, such as A. thaliana RSp31, RSp35, RSp41 and similar proteins. Like vertebrate RS splicing factors, these proteins function as plant splicing factors and play crucial roles in constitutive and alternative splicing in plants. They all contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), at their N-terminus, and an RS domain at their C-terminus
TLFVINFDPIRTKERDLERHFEPYGKVVNVRIRRNFAFVQYETQEDATKALDATQSSKIMDRVISVEYAL
>gnl|CDD|240913 cd12467, RRM_Srp1p_like, RNA recognition motif 1 (RRM1) found in fission yeast pre-mRNA-splicing factor Srp1p and similar proteins. This subgroup corresponds to the RRM domain in Srp1p encoded by gene srp1 from fission yeast Schizosaccharomyces pombe. It plays a role in the pre-mRNA splicing process, but not essential for growth. Srp1p is closely related to the SR protein family found in metazoa. It contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a glycine hinge and a RS domain in the middle, and a C-terminal domain. Some family members also contain another RRM domain
TLYVTGFGAETRARDLAYEFERYGRLVRCDIPPPRTFQSRPFAFVEYESHRDAEDAYEEMHGRRFPDTGD
TLHVQWAK
>gnl|CDD|409900 cd12470, RRM1_MSSP1, RNA recognition motif 1 (RRM1) found in vertebrate single-stranded DNA-binding protein MSSP-1. This subgroup corresponds to the RRM1 of MSSP-1, also termed RNA-binding motif, single-stranded-interacting protein 1 (RBMS1), or suppressor of CDC2 with RNA-binding motif 2 (SCR2), a double- and single-stranded DNA binding protein that belongs to the c-myc single-strand binding proteins (MSSP) family. It specifically recognizes the sequence CT(A/T)(A/T)T, and stimulates DNA replication in the system using SV40 DNA. MSSP-1 is identical with Scr2, a human protein which complements the defect of cdc2 kinase in Schizosaccharomyces pombe. MSSP-1 has been implied in regulating DNA replication, transcription, apoptosis induction, and cell-cycle movement, via the interaction with C-MYC, the product of protooncogene c-myc. MSSP-1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), both of which are responsible for the specific DNA binding activity as well as induction of apoptosis
GWDQLSKTNLYIRGLPPNTTDQDLVKLCQPYGKIVSTKAILDKTTNKCKGYGFVDFDSPAAAQKAVSALK
ASGVQAQMAKQQEQDP
>gnl|CDD|409901 cd12471, RRM1_MSSP2, RNA recognition motif 1 (RRM1) found in vertebrate single-stranded DNA-binding protein MSSP-2. This subgroup corresponds to the RRM1 of MSSP-2, also termed RNA-binding motif, single-stranded-interacting protein 2 (RBMS2), or suppressor of CDC2 with RNA-binding motif 3 (SCR3), a double- and single-stranded DNA binding protein that belongs to the c-myc single-strand binding proteins (MSSP) family. It specifically recognizes the sequence T(C/A)TT, and stimulates DNA replication in the system using SV40 DNA. MSSP-2 is identical with Scr3, a human protein which complements the defect of cdc2 kinase in Schizosaccharomyces pombe. MSSP-2 has been implied in regulating DNA replication, transcription, apoptosis induction, and cell-cycle movement, via the interaction with C-MYC, the product of protooncogene c-myc. MSSP-2 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), both of which are responsible for the specific DNA binding activity as well as induction of apoptosis
DQLSKTNLYIRGLHPGTTDQDLVKLCQPYGKIVSTKAILDKTTNKCKGYGFVDFDSPSAAQKAVTALKAS
GVQAQMAKQQEQDP
>gnl|CDD|409902 cd12472, RRM1_RBMS3, RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding motif, single-stranded-interacting protein 3 (RBMS3). This subgroup corresponds to the RRM1 of RBMS3, a new member of the c-myc gene single-strand binding proteins (MSSP) family of DNA regulators. Unlike other MSSP proteins, RBMS3 is not a transcriptional regulator. It binds with high affinity to A/U-rich stretches of RNA, and to A/T-rich DNA sequences, and functions as a regulator of cytoplasmic activity. RBMS3 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and its C-terminal region is acidic and enriched in prolines, glutamines and threonines
QLSKTNLYIRGLPPGTTDQDLIKLCQPYGKIVSTKAILDKNTNQCKGYGFVDFDSPAAAQKAVASLKASG
VQAQMAKQQE
>gnl|CDD|409903 cd12473, RRM2_MSSP1, RNA recognition motif 2 (RRM2) found in vertebrate single-stranded DNA-binding protein MSSP-1. This subgroup corresponds to the RRM2 of MSSP-1, also termed RNA-binding motif, single-stranded-interacting protein 1 (RBMS1), or suppressor of CDC2 with RNA-binding motif 2 (SCR2). MSSP-1 is a double- and single-stranded DNA binding protein that belongs to the c-myc single-strand binding proteins (MSSP) family. It specifically recognizes the sequence CT(A/T)(A/T)T, and stimulates DNA replication in the system using SV40 DNA. MSSP-1 is identical with Scr2, a human protein which complements the defect of cdc2 kinase in Schizosaccharomyces pombe. MSSP-1 has been implied in regulating DNA replication, transcription, apoptosis induction, and cell-cycle movement, via the interaction with c-MYC, the product of protooncogene c-myc. MSSP-1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), both of which are responsible for the specific DNA binding activity as well as induction of apoptosis
TNLYISNLPLSMDEQELENMLKPFGQVISTRILRDSSGTSRGVGFARMESTEKCEAVISHFNGKFIKTPP
GVSAPAEPLLCKFAD
>gnl|CDD|409904 cd12474, RRM2_MSSP2, RNA recognition motif 2 (RRM2) found in vertebrate single-stranded DNA-binding protein MSSP-2. This subgroup corresponds to the RRM2 of MSSP-2, also termed RNA-binding motif, single-stranded-interacting protein 2 (RBMS2), or suppressor of CDC2 with RNA-binding motif 3 (SCR3). MSSP-2 is a double- and single-stranded DNA binding protein that belongs to the c-myc single-strand binding proteins (MSSP) family. It specifically recognizes the sequence T(C/A)TT, and stimulates DNA replication in the system using SV40 DNA. MSSP-2 is identical with Scr3, a human protein which complements the defect of cdc2 kinase in Schizosaccharomyces pombe. MSSP-2 has been implied in regulating DNA replication, transcription, apoptosis induction, and cell-cycle movement, via the interaction with C-MYC, the product of protooncogene c-myc. MSSP-2 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), both of which are responsible for the specific DNA binding activity as well as induction of apoptosis
TNLYISNLPLSMDEQELESMLKPFGQVISTRILRDANGTSRGVGFARMESTEKCEAIITHFNGKYIKTPP
GVPAPTEPLLCKFADG
>gnl|CDD|240919 cd12475, RRM2_RBMS3, RNA recognition motif 2 (RRM2) found in vertebrate RNA-binding motif, single-stranded-interacting protein 3 (RBMS3). This subgroup corresponds to the RRM2 of RBMS3, a new member of the c-myc gene single-strand binding proteins (MSSP) family of DNA regulators. Unlike other MSSP proteins, RBMS3 is not a transcriptional regulator. It binds with high affinity to A/U-rich stretches of RNA, and to A/T-rich DNA sequences, and functions as a regulator of cytoplasmic activity. RBMS3 contain two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and its C-terminal region is acidic and enriched in prolines, glutamines and threonines
PTNLYISNLPISMDEQELENMLKPFGHVISTRILRDANGVSRGVGFARMESTEKCEVVIQHFNGKYLKTP
PGVPAPTEPLLCKFADGG
>gnl|CDD|409905 cd12476, RRM1_SNF, RNA recognition motif 1 (RRM1) found in Drosophila melanogaster sex determination protein SNF and similar proteins. This subgroup corresponds to the RRM1 of SNF (Sans fille), also termed U1 small nuclear ribonucleoprotein A (U1 snRNP A or U1-A or U1A), an RNA-binding protein found in the U1 and U2 snRNPs of Drosophila. It is essential in Drosophila sex determination and possesses a novel dual RNA binding specificity. SNF binds with high affinity to both Drosophila U1 snRNA stem-loop II (SLII) and U2 snRNA stem-loop IV (SLIV). It can also bind to poly(U) RNA tracts flanking the alternatively spliced Sex-lethal (Sxl) exon, as does Drosophila Sex-lethal protein (SXL). SNF contains two RNA recognition motifs (RRMs); it can self-associate through RRM1, and each RRM can recognize poly(U) RNA binding independently
MDIRPNQTIYINNLNEKVKKEELKKSLYAIFSQFGQILDIVALKTLKMRGQAFVIFKDISSATNALRSMQ
GFPFYDKPMRIAYSK
>gnl|CDD|409906 cd12477, RRM1_U1A, RNA recognition motif 1 (RRM1) found in vertebrate U1 small nuclear ribonucleoprotein A (U1A). This subgroup corresponds to the RRM1 of U1A (also termed U1 snRNP A or U1-A), an RNA-binding protein associated with the U1 snRNP, a small RNA-protein complex involved in pre-mRNA splicing. U1A binds with high affinity and specificity to stem-loop II (SLII) of U1 snRNA. It is predominantly a nuclear protein and it also shuttles between the nucleus and the cytoplasm independently of interactions with U1 snRNA. U1A may be involved in RNA 3'-end processing, specifically cleavage, splicing and polyadenylation, through interacting with a large number of non-snRNP proteins, including polypyrimidine tract binding protein (PTB), polypyrimidine-tract binding protein-associated factor (PSF), and non-POU-domain-containing, octamer-binding (NONO), DEAD (Asp-Glu-Ala-Asp) box polypeptide 5 (DDX5). It also binds to a flavivirus NS5 protein and plays an important role in virus replication. U1A contains two RNA recognition motifs (RRMs); the N-terminal RRM (RRM1) binds tightly and specifically to the U1 snRNA SLII and its own 3'-UTR, while in contrast, the C-terminal RRM (RRM2) does not appear to associate with any RNA and may be free to bind other proteins. U1A also contains a proline-rich region, and a nuclear localization signal (NLS) in the central domain that is responsible for its nuclear import
RPNHTIYINNLNEKIKKDELKKSLHAIFSRFGQILDILVSRSLKMRGQAFVIFKEVSSATNALRSMQGFP
FYDKPMRIQYAKTDSDIIA
>gnl|CDD|409907 cd12478, RRM1_U2B, RNA recognition motif 1 in U2 small nuclear ribonucleoprotein B" (U2B") and similar proteins. This subgroup corresponds to the RRM1 of U2B" (also termed U2 snRNP B") a unique protein that comprises the U2 snRNP. It was initially identified as binding to stem-loop IV (SLIV) at the 3' end of U2 snRNA. Additional research indicates U2B" binds to U1 snRNA stem-loop II (SLII) as well and shows no preference for SLIV or SLII on the basis of binding affinity. U2B" does not require an auxiliary protein for binding to RNA. In addition, the nuclear transport of U2B" is independent of U2 snRNA binding. U2B" contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). It also contains a nuclear localization signal (NLS) in the central domain. However, nuclear import of U2B'' does not depend on this NLS. The N-terminal RRM is sufficient to direct U2B" to the nucleus
NHTIYINNINDKIKKEELKRSLYALFSQFGHVVDIVALKTMKMRGQAFVIFKELSSATNALRQLQGFPFY
GKPMRIQYAKTDSDIVSKMRG
>gnl|CDD|240923 cd12479, RRM2_SNF, RNA recognition motif 2 (RRM2) found in Drosophila melanogaster sex determination protein SNF and similar proteins. This subgroup corresponds to the RRM2 of SNF (Sans fille), also termed U1 small nuclear ribonucleoprotein A (U1 snRNP A or U1-A or U1A), an RNA-binding protein found in the U1 and U2 snRNPs of Drosophila. It is essential in Drosophila sex determination and possesses a novel dual RNA binding specificity. SNF binds with high affinity to both Drosophila U1 snRNA stem-loop II (SLII) and U2 snRNA stem-loop IV (SLIV). It can also bind to poly(U) RNA tracts flanking the alternatively spliced Sex-lethal (Sxl) exon, as does Drosophila Sex-lethal protein (SXL). SNF contains two RNA recognition motifs (RRMs); it can self-associate through RRM1, and each RRM can recognize poly(U) RNA binding independently
EQPPNQILFLTNLPEETNEMMLSMLFNQFPGFKEVRLVPGRHDIAFVEFENEVQSAAAKEALQGFKITPT
HAMKITFAKK
>gnl|CDD|409908 cd12480, RRM2_U1A, RNA recognition motif 2 (RRM2) found in vertebrate U1 small nuclear ribonucleoprotein A (U1 snRNP A or U1-A or U1A). This subgroup corresponds to the RRM2 of U1A (also termed U1 snRNP A or U1-A), an RNA-binding protein associated with the U1 snRNP, a small RNA-protein complex involved in pre-mRNA splicing. U1A binds with high affinity and specificity to stem-loop II (SLII) of U1 snRNA. It is predominantly a nuclear protein that shuttles between the nucleus and the cytoplasm independently of interactions with U1 snRNA. U1A may be involved in RNA 3'-end processing, specifically cleavage, splicing and polyadenylation, through interacting with a large number of non-snRNP proteins, including polypyrimidine tract binding protein (PTB), polypyrimidine-tract binding protein-associated factor (PSF), and non-POU-domain-containing, octamer-binding (NONO), DEAD (Asp-Glu-Ala-Asp) box polypeptide 5 (DDX5). U1A also binds to a flavivirus NS5 protein and plays an important role in virus replication. It contains two RNA recognition motifs (RRMs); the N-terminal RRM (RRM1) binds tightly and specifically to the U1 snRNA SLII and its own 3'-UTR, while in contrast, the C-terminal RRM (RRM2) does not appear to associate with any RNA and it may be free for binding other proteins. U1A also contains a proline-rich region, and a nuclear localization signal (NLS) in the central domain that is responsible for its nuclear import
PPQPVSENPPNHILFLTNLPEETNELMLSMLFNQFPGFKEVRLVPGRHDIAFVEFDNEVQAGAAREALQG
FKITQSNAMKISFAKK
>gnl|CDD|240925 cd12481, RRM2_U2B, RNA recognition motif 2 (RRM2) found in vertebrate U2 small nuclear ribonucleoprotein B" (U2B"). This subgroup corresponds to the RRM1 of U2B" (also termed U2 snRNP B"), a unique protein that comprises the U2 snRNP. It was initially identified to bind to stem-loop IV (SLIV) at the 3' end of U2 snRNA. Additional research indicates U2B" binds to U1 snRNA stem-loop II (SLII) as well and shows no preference for SLIV or SLII on the basis of binding affinity. U2B" does not require an auxiliary protein for binding to RNA and its nuclear transport is independent of U2 snRNA binding. U2B" contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). It also contains a nuclear localization signal (NLS) in the central domain. However, nuclear import of U2B'' does not depend on this NLS. The N-terminal RRM is sufficient to direct U2B" to the nucleus
DNPPNYILFLNNLPEETNEMMLSMLFNQFPGFKEVRLVPGRHDIAFVEFENEGQAGAARDALQGFRITPS
HAMKITYAKK
>gnl|CDD|409909 cd12482, RRM1_hnRNPR, RNA recognition motif 1 (RRM1) found in vertebrate heterogeneous nuclear ribonucleoprotein R (hnRNP R). This subgroup corresponds to the RRM1 of hnRNP R, which is a ubiquitously expressed nuclear RNA-binding protein that specifically binds mRNAs with a preference for poly(U) stretches. Upon binding of RNA, hnRNP R forms oligomers, most probably dimers. hnRNP R has been implicated in mRNA processing and mRNA transport, and also acts as a regulator to modify binding to ribosomes and RNA translation. It is predominantly located in axons of motor neurons and to a much lower degree in sensory axons. In axons of motor neurons, it also functions as a cytosolic protein and interacts with wild type of survival motor neuron (SMN) proteins directly, further providing a molecular link between SMN and the spliceosome. Moreover, hnRNP R plays an important role in neural differentiation and development, and in retinal development and light-elicited cellular activities. hnRNP R contains an acidic auxiliary N-terminal region, followed by two well defined and one degenerated RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal RGG motif; it binds RNA through its RRM domains
GTEVFVGKIPRDLYEDELVPLFEKAGPIWDLRLMMDPLSGQNRGYAFITFCNKEAAQEAVKLCDNYEIRP
GKHLGVCIS
>gnl|CDD|409910 cd12483, RRM1_hnRNPQ, RNA recognition motif 1 (RRM1) found in vertebrate heterogeneous nuclear ribonucleoprotein Q (hnRNP Q). This subgroup corresponds to the RRM1 of hnRNP Q, also termed glycine- and tyrosine-rich RNA-binding protein (GRY-RBP), or NS1-associated protein 1 (NASP1), or synaptotagmin-binding, cytoplasmic RNA-interacting protein (SYNCRIP). It is a ubiquitously expressed nuclear RNA-binding protein identified as a component of the spliceosome complex, as well as a component of the apobec-1 editosome. As an alternatively spliced version of NSAP, it acts as an interaction partner of a multifunctional protein required for viral replication, and is implicated in the regulation of specific mRNA transport. hnRNP Q has also been identified as SYNCRIP, a dual functional protein participating in both viral RNA replication and translation. As a synaptotagmin-binding protein, hnRNP Q plays a putative role in organelle-based mRNA transport along the cytoskeleton. Moreover, hnRNP Q has been found in protein complexes involved in translationally coupled mRNA turnover and mRNA splicing. It functions as a wild-type survival motor neuron (SMN)-binding protein that may participate in pre-mRNA splicing and modulate mRNA transport along microtubuli. hnRNP Q contains an acidic auxiliary N-terminal region, followed by two well-defined and one degenerated RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal RGG motif; hnRNP Q binds RNA through its RRM domains
QPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLCNNH
EIRPGKHIGVCISV
>gnl|CDD|409911 cd12484, RRM1_RBM46, RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding protein 46 (RBM46). This subgroup corresponds to the RRM1 of RBM46, also termed cancer/testis antigen 68 (CT68), a putative RNA-binding protein that shows high sequence homology with heterogeneous nuclear ribonucleoprotein R (hnRNP R) and heterogeneous nuclear ribonucleoprotein Q (hnRNP Q). Its biological function remains unclear. Like hnRNP R and hnRNP Q, RBM46 contains two well-defined and one degenerated RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
GCEVFVGKIPRDMYEDELVPVFERAGKIYEFRLMMEFSGENRGYAFVMYTTKEEAQLAIKMLNNYEIRPG
KFIGVCVS
>gnl|CDD|240929 cd12485, RRM1_RBM47, RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding protein 47 (RBM47). This subgroup corresponds to the RRM1 of RBM47, a putative RNA-binding protein that shows high sequence homology with heterogeneous nuclear ribonucleoprotein R (hnRNP R) and heterogeneous nuclear ribonucleoprotein Q (hnRNP Q). Its biological function remains unclear. Like hnRNP R and hnRNP Q, RBM47 contains two well-defined and one degenerated RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
GCEVFVGKIPRDVYEDELVPVFESVGRIYEMRLMMDFDGKNRGYAFVMYTQKHEAKRAVRELNNYEIRPG
RLLGVCCS
>gnl|CDD|409912 cd12486, RRM1_ACF, RNA recognition motif 1 (RRM1) found in vertebrate APOBEC-1 complementation factor (ACF). This subgroup corresponds to the RRM1 of ACF, also termed APOBEC-1-stimulating protein, an RNA-binding subunit of a core complex that interacts with apoB mRNA to facilitate C to U RNA editing. It may also act as an apoB mRNA recognition factor and chaperone, and play a key role in cell growth and differentiation. ACF shuttles between the cytoplasm and nucleus. It contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which display high affinity for an 11 nucleotide AU-rich mooring sequence 3' of the edited cytidine in apoB mRNA. All three RRMs may be required for complementation of editing activity in living cells. RRM2/3 are implicated in ACF interaction with APOBEC-1
GCEIFIGKLPRDLFEDELVPLCEKIGKIYEMRMMMDFNGNNRGYAFVTFSNKQEARNAIKQLNNYEIRNG
RLLGVCAS
>gnl|CDD|409913 cd12487, RRM1_DND1, RNA recognition motif 1 (RRM1) found in vertebrate dead end protein homolog 1 (DND1). This subgroup corresponds to the RRM1 of DND1, also termed RNA-binding motif, single-stranded-interacting protein 4, an RNA-binding protein that is essential for maintaining viable germ cells in vertebrates. It interacts with the 3'-untranslated region (3'-UTR) of multiple messenger RNAs (mRNAs) and prevents micro-RNA (miRNA) mediated repression of mRNA. For instance, DND1 binds cell cycle inhibitor, P27 (p27Kip1, CDKN1B), and cell cycle regulator and tumor suppressor, LATS2 (large tumor suppressor, homolog 2 of Drosophila). It helps maintain their protein expression through blocking the inhibitory function of microRNAs (miRNA) from these transcripts. DND1 may also impose another level of translational regulation to modulate expression of critical factors in embryonic stem (ES) cells. DND1 interacts specifically with apolipoprotein B editing complex 3 (APOBEC3), a multi-functional protein inhibiting retroviral replication. The DND1-APOBEC3 interaction may play a role in maintaining viability of germ cells and for preventing germ cell tumor development. DND1 contains two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
GSEVFIGKIPQDVYEDKLIPLFQSVGQLYEFRLMMTFSGLNRGFAYAKYASRRSAQAAITTLNGYELQKG
CPITVCRS
>gnl|CDD|240932 cd12488, RRM2_hnRNPR, RNA recognition motif 2 (RRM2) found in vertebrate heterogeneous nuclear ribonucleoprotein R (hnRNP R). This subgroup corresponds to the RRM2 of hnRNP R, a ubiquitously expressed nuclear RNA-binding protein that specifically bind mRNAs with a preference for poly(U) stretches. Upon binding of RNA, hnRNP R forms oligomers, most probably dimers. hnRNP R has been implicated in mRNA processing and mRNA transport, and also acts as a regulator to modify binding to ribosomes and RNA translation. hnRNP R is predominantly located in axons of motor neurons and to a much lower degree in sensory axons. In axons of motor neurons, it also functions as a cytosolic protein and interacts with wild type of survival motor neuron (SMN) proteins directly, further providing a molecular link between SMN and the spliceosome. Moreover, hnRNP R plays an important role in neural differentiation and development, as well as in retinal development and light-elicited cellular activities. It contains an acidic auxiliary N-terminal region, followed by two well-defined and one degenerated RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal RGG motif. hnRNP R binds RNA through its RRM domains
ANNRLFVGSIPKNKTKENILEEFSKVTEGLVDVILYHQPDDKKKNRGFCFLEYEDHKSAAQARRRLMSGK
VKVWGNVVTVEWADP
>gnl|CDD|240933 cd12489, RRM2_hnRNPQ, RNA recognition motif 2 (RRM2) found in vertebrate heterogeneous nuclear ribonucleoprotein Q (hnRNP Q). This subgroup corresponds to the RRM3 of hnRNP Q, also termed glycine- and tyrosine-rich RNA-binding protein (GRY-RBP), or NS1-associated protein 1 (NASP1), or synaptotagmin-binding, cytoplasmic RNA-interacting protein (SYNCRIP). It is a ubiquitously expressed nuclear RNA-binding protein identified as a component of the spliceosome complex, as well as a component of the apobec-1 editosome. As an alternatively spliced version of NSAP, it acts as an interaction partner of a multifunctional protein required for viral replication, and is implicated in the regulation of specific mRNA transport. hnRNP Q has also been identified as SYNCRIP that is a dual functional protein participating in both viral RNA replication and translation. As a synaptotagmin-binding protein, hnRNP Q plays a putative role in organelle-based mRNA transport along the cytoskeleton. Moreover, hnRNP Q has been found in protein complexes involved in translationally coupled mRNA turnover and mRNA splicing. It functions as a wild-type survival motor neuron (SMN)-binding protein that may participate in pre-mRNA splicing and modulate mRNA transport along microtubuli. hnRNP Q contains an acidic auxiliary N-terminal region, followed by two well-defined and one degenerated RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal RGG motif; hnRNP Q binds RNA through its RRM domains
ANNRLFVGSIPKSKTKEQIVEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGK
VKVWGNVVTVEWADP
>gnl|CDD|409914 cd12490, RRM2_ACF, RNA recognition motif 2 (RRM2) found in vertebrate APOBEC-1 complementation factor (ACF). This subgroup corresponds to the RRM2 of ACF, also termed APOBEC-1-stimulating protein, an RNA-binding subunit of a core complex that interacts with apoB mRNA to facilitate C to U RNA editing. It may also act as an apoB mRNA recognition factor and chaperone and play a key role in cell growth and differentiation. ACF shuttles between the cytoplasm and nucleus. ACF contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which display high affinity for an 11 nucleotide AU-rich mooring sequence 3' of the edited cytidine in apoB mRNA. All three RRMs may be required for complementation of editing activity in living cells. RRM2/3 are implicated in ACF interaction with APOBEC-1
VDNCRLFVGGIPKTKKREEILAEMKKVTDGVVDVIVYPSAADKTKNRGFAFVEYESHRAAAMARRKLLPG
RIQLWGHPIAVDWAEPEVE
>gnl|CDD|409915 cd12491, RRM2_RBM47, RNA recognition motif 2 (RRM2) found in vertebrate RNA-binding protein 47 (RBM47). This subgroup corresponds to the RRM2 of RBM47, a putative RNA-binding protein that shows high sequence homology with heterogeneous nuclear ribonucleoprotein R (hnRNP R) and heterogeneous nuclear ribonucleoprotein Q (hnRNP Q). Its biological function remains unclear. Like hnRNP R and hnRNP Q, RBM47 contains two well-defined and one degenerated RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
VDNCRLFIGGIPKMKKREEILEEISKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPG
RIQLWGHQIAVDWAEPEIDVDEDVM
>gnl|CDD|240936 cd12492, RRM2_RBM46, RNA recognition motif 2 (RRM2) found in vertebrate RNA-binding protein 46 (RBM46). This subgroup corresponds to the RRM2 of RBM46, also termed cancer/testis antigen 68 (CT68). It is a putative RNA-binding protein that shows high sequence homology with heterogeneous nuclear ribonucleoprotein R (hnRNP R) and heterogeneous nuclear ribonucleoprotein Q (hnRNP Q). Its biological function remains unclear. Like hnRNP R and hnRNP Q, RBM46 contains two well-defined and one degenerated RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
DNCRLFIGAIPKEKKKEEILEEMKKVTEGVVDVIVYPSATDKTKNRGFAFVEYESHRAAAMARRKLIPGT
FQLWGHTIQVDWADP
>gnl|CDD|409916 cd12493, RRM2_DND1, RNA recognition motif 2 (RRM2) found in vertebrate dead end protein homolog 1 (DND1). This subgroup corresponds to the RRM2 of DND1, also termed RNA-binding motif, single-stranded-interacting protein 4. It is an RNA-binding protein that is essential for maintaining viable germ cells in vertebrates. It interacts with the 3'-untranslated region (3'-UTR) of multiple messenger RNAs (mRNAs) and prevents micro-RNA (miRNA) mediated repression of mRNA. For instance, DND1 binds cell cycle inhibitor, P27 (p27Kip1, CDKN1B), and cell cycle regulator and tumor suppressor, LATS2 (large tumor suppressor, homolog 2 of Drosophila). It helps maintain their protein expression through blocking the inhibitory function of microRNAs (miRNA) from these transcripts. DND1 may also impose another level of translational regulation to modulate expression of critical factors in embryonic stem (ES) cells. Moreover, DND1 interacts specifically with apolipoprotein B editing complex 3 (APOBEC3), a multi-functional protein inhibiting retroviral replication. The DND1-APOBEC3 interaction may play a role in maintaining viability of germ cells and for preventing germ cell tumor development. DND1 contains two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
EKCELSVDGLPVSMDESKLLMVLQMLTDGVESVLLHPSPPKGKEVLAVVKYSSHRAAAMAKKALVEGSRN
LCGEQVTVRWLKP
>gnl|CDD|409917 cd12494, RRM3_hnRNPR, RNA recognition motif 3 (RRM3) found in vertebrate heterogeneous nuclear ribonucleoprotein R (hnRNP R). This subgroup corresponds to the RRM3 of hnRNP R. a ubiquitously expressed nuclear RNA-binding protein that specifically bind mRNAs with a preference for poly(U) stretches. Upon binding of RNA, hnRNP R forms oligomers, most probably dimers. hnRNP R has been implicated in mRNA processing and mRNA transport, and also acts as a regulator to modify binding to ribosomes and RNA translation. hnRNP R is predominantly located in axons of motor neurons and to a much lower degree in sensory axons. In axons of motor neurons, it also functions as a cytosolic protein and interacts with wild type of survival motor neuron (SMN) proteins directly, further providing a molecular link between SMN and the spliceosome. Moreover, hnRNP R plays an important role in neural differentiation and development, as well as in retinal development and light-elicited cellular activities. hnRNP R contains an acidic auxiliary N-terminal region, followed by two well-defined and one degenerated RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal RGG motif; hnRNP R binds RNA through its RRM domains
VKVLFVRNLATTVTEEILEKTFSQFGKLERVKKLKDYAFVHFEDRDAAVKAMDEMNGKEVEGEEIEIVLA
KP
>gnl|CDD|409918 cd12495, RRM3_hnRNPQ, RNA recognition motif 3 (RRM3) found in vertebrate heterogeneous nuclear ribonucleoprotein Q (hnRNP Q). This subgroup corresponds to the RRM3 of hnRNP Q, also termed glycine- and tyrosine-rich RNA-binding protein (GRY-RBP), or NS1-associated protein 1 (NASP1), or synaptotagmin-binding, cytoplasmic RNA-interacting protein (SYNCRIP). It is a ubiquitously expressed nuclear RNA-binding protein identified as a component of the spliceosome complex, as well as a component of the apobec-1 editosome. As an alternatively spliced version of NSAP, it acts as an interaction partner of a multifunctional protein required for viral replication, and is implicated in the regulation of specific mRNA transport. hnRNP Q has also been identified as SYNCRIP that is a dual functional protein participating in both viral RNA replication and translation. As a synaptotagmin-binding protein, hnRNP Q plays a putative role in organelle-based mRNA transport along the cytoskeleton. Moreover, hnRNP Q has been found in protein complexes involved in translationally coupled mRNA turnover and mRNA splicing. It functions as a wild-type survival motor neuron (SMN)-binding protein that may participate in pre-mRNA splicing and modulate mRNA transport along microtubuli. hnRNP Q contains an acidic auxiliary N-terminal region, followed by two well defined and one degenerated RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal RGG motif; hnRNP Q binds RNA through its RRM domains
VKVLFVRNLANTVTEEILEKAFSQFGKLERVKKLKDYAFIHFDERDGAVKAMDEMNGKDLEGENIEIVFA
KP
>gnl|CDD|409919 cd12496, RRM3_RBM46, RNA recognition motif 3 (RRM3) found in vertebrate RNA-binding protein 46 (RBM46). This subgroup corresponds to the RRM3 of RBM46, also termed cancer/testis antigen 68 (CT68), is a putative RNA-binding protein that shows high sequence homology with heterogeneous nuclear ribonucleoprotein R (hnRNP R) and heterogeneous nuclear ribonucleoprotein Q (hnRNP Q). Its biological function remains unclear. Like hnRNP R and hnRNP Q, RBM46 contains two well defined and one degenerated RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
VKVLYVRNLMISTTEETIKAEFNKFKPGVVERVKKLRDYAFVHFFNREDAVAAMSVMNGKCIDGASIEVT
LAKP
>gnl|CDD|409920 cd12497, RRM3_RBM47, RNA recognition motif 3 (RRM3) found in vertebrate RNA-binding protein 47 (RBM47). This subgroup corresponds to the RRM3 of RBM47, a putative RNA-binding protein that shows high sequence homology with heterogeneous nuclear ribonucleoprotein R (hnRNP R) and heterogeneous nuclear ribonucleoprotein Q (hnRNP Q). Its biological function remains unclear. Like hnRNP R and hnRNP Q, RBM47 contains two well defined and one degenerated RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
VKILYVRNLMIETTEDTIKKIFGQFNPGCVERVKKIRDYAFVHFASRDDAVVAMNNLNGTELEGSCIEVT
LAKP
>gnl|CDD|409921 cd12498, RRM3_ACF, RNA recognition motif 3 (RRM3) found in vertebrate APOBEC-1 complementation factor (ACF). This subgroup corresponds to the RRM3 of ACF, also termed APOBEC-1-stimulating protein, an RNA-binding subunit of a core complex that interacts with apoB mRNA to facilitate C to U RNA editing. It may also act as an apoB mRNA recognition factor and chaperone and play a key role in cell growth and differentiation. ACF shuttles between the cytoplasm and nucleus. ACF contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which display high affinity for an 11 nucleotide AU-rich mooring sequence 3' of the edited cytidine in apoB mRNA. All three RRMs may be required for complementation of editing activity in living cells. RRM2/3 are implicated in ACF interaction with APOBEC-1
DEDTMSSVKILYVRNLMLSTTEETIEKEFSNIKPGAVERVKKIRDYAFVHFYNREDAVNAMNALNGKVID
GSPIEVTLAKPVD
>gnl|CDD|409922 cd12499, RRM_EcCsdA_like, RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and similar proteins. This subgroup corresponds to the C-terminal RRM homology domain of E. coli CsdA, also termed ATP-dependent RNA helicase deaD, or translation factor W2, a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. CsdA may be involved in translation initiation, gene regulation after cold-shock, mRNA decay and biogenesis of the large or small ribosomal subunit. It contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding
RYRIEVGRKDGVKPGNIVGAIANEAGIDSRFIGRIKIFDDHSTVELPKGMPKDVLQHLKKVRVCGQPLNI
KLL
>gnl|CDD|409923 cd12500, RRM_BsYxiN_like, RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and similar proteins. This subgroup corresponds to the C-terminal RRM homology domain of YxiN. B. subtilis YxiN is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions in an ATP-dependent manner. YxiN contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding
KLYFNGGKKKKIRAVDIVGAISNIDGVTGDDIGIITVQDNCSYVDILNGKGDHVLKVMKNTTIKGKQVKV
NKA
>gnl|CDD|409924 cd12501, RRM_EcDbpA_like, RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins. This subgroup corresponds to the C-terminal RRM homology domain of dbpA. E. coli dbpA is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity for RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions. As a non-processive ATP-dependent helicase, DbpA destabilizes and unwinds short <9bp (base pairs) RNA duplexes as well as long duplex RNA stretches. It disrupts RNA helices exclusively in a 3'- 5' direction and requires a single-stranded loading site 3' of the substrate helix. dbpA contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain binds specifically to hairpin 92
TIQIDGGKKQKLRPGDILGALTGDNGIDGEDIGKINITDFVSYVAVKRSVAKDALKKLREGKIKGRKFRV
RLL
>gnl|CDD|409925 cd12502, RRM2_RMB19, RNA recognition motif 2 (RRM2) found in RNA-binding protein 19 (RBM19) and similar proteins. This subfamily corresponds to the RRM2 of RBM19, also termed RNA-binding domain-1 (RBD-1), a nucleolar protein conserved in eukaryotes. It is involved in ribosome biogenesis by processing rRNA and is also essential for preimplantation development. RBM19 has a unique domain organization containing 6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
FTVKLRGAPFNVKEKQIREFFSPLKPVAIRIVKNAHGNKTGYVFVDFKSEEDVEKALKRNKDYMGGRYIE
VF
>gnl|CDD|409926 cd12503, RRM1_hnRNPH_GRSF1_like, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein (hnRNP) H protein family, G-rich sequence factor 1 (GRSF-1) and similar proteins. This subfamily corresponds to the RRM1 of hnRNP H proteins and GRSF-1. The hnRNP H protein family includes hnRNP H (also termed mcs94-1), hnRNP H2 (also termed FTP-3 or hnRNP H'), hnRNP F and hnRNP H3 (also termed hnRNP 2H9), which represent a group of nuclear RNA binding proteins that are involved in pre-mRNA processing. These proteins have similar RNA binding affinities and specifically recognize the sequence GGGA. They can either stimulate or repress splicing upon binding to a GGG motif. hnRNP H binds to the RNA substrate in the presence or absence of these proteins, whereas hnRNP F binds to the nuclear mRNA only in the presence of cap-binding proteins. hnRNP H and hnRNP H2 are almost identical; both have been found to bind nuclear-matrix proteins. hnRNP H activates exon inclusion by binding G-rich intronic elements downstream of the 5' splice site in the transcripts of c-src, human immunodeficiency virus type 1 (HIV-1), Bcl-X, GRIN1, and myelin. It silences exons when bound to exonic elements in the transcripts of beta-tropomyosin, HIV-1, and alpha-tropomyosin. hnRNP H2 has been implicated in pre-mRNA 3' end formation. hnRNP H3 may be involved in splicing arrest induced by heat shock. Most family members contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), except for hnRNP H3, in which the RRM1 is absent. RRM1 and RRM2 are responsible for the binding to the RNA at DGGGD motifs, and play an important role in efficiently silencing the exon. Members in this family can regulate the alternative splicing of fibroblast growth factor receptor 2 (FGFR2) transcripts, and function as silencers of FGFR2 exon IIIc through an interaction with the exonic GGG motifs. The lack of RRM1 could account for the reduced silencing activity within hnRNP H3. Members in this family have an extensive glycine-rich region near the C-terminus, which may allow them to homo- or heterodimerize. They also include a cytoplasmic poly(A)+ mRNA binding protein, GRSF-1, which interacts with RNA in a G-rich element-dependent manner. They may function in RNA packaging, stabilization of RNA secondary structure, or other macromolecular interactions. GRSF-1 contains three potential RRMs responsible for the RNA binding, and two auxiliary domains (an acidic alpha-helical domain and an N-terminal alanine-rich region) that may play a role in protein-protein interactions and provide binding specificity
VVRARGLPWSATAEDVLNFFTDCRIKGGENGIHFTYTREGRPSGEAFIELESEEDVEKALEKHNEHMGHR
YIEVFRS
>gnl|CDD|409927 cd12504, RRM2_hnRNPH_CRSF1_like, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein (hnRNP) H protein family. This subfamily corresponds to the RRM2 of hnRNP H protein family which includes hnRNP H (also termed mcs94-1), hnRNP H2 (also termed FTP-3 or hnRNP H'), hnRNP F and hnRNP H3 (also termed hnRNP 2H9). They represent a group of nuclear RNA binding proteins that are involved in pre-mRNA processing, having similar RNA binding affinities and specifically recognizing the sequence GGGA. They can either stimulate or repress splicing upon binding to a GGG motif. hnRNP H binds to the RNA substrate in the presence or absence of these proteins, whereas hnRNP F binds to the nuclear mRNA only in the presence of cap-binding proteins. Furthermore, hnRNP H and hnRNP H2 are almost identical; both have been found to bind nuclear-matrix proteins. hnRNP H activates exon inclusion by binding G-rich intronic elements downstream of the 5' splice site in the transcripts of c-src, human immunodeficiency virus type 1 (HIV-1), Bcl-X, GRIN1, and myelin. It silences exons when bound to exonic elements in the transcripts of beta-tropomyosin, HIV-1, and alpha-tropomyosin. hnRNP H2 has been implicated in pre-mRNA 3' end formation. hnRNP H3 may be involved in the splicing arrest induced by heat shock. Most family members contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), except for hnRNP H3, in which the RRM1 is absent. RRM1 and RRM2 are responsible for the binding to the RNA at DGGGD motifs, and they play an important role in efficiently silencing the exon. Members in this family can regulate the alternative splicing of the fibroblast growth factor receptor 2 (FGFR2) transcripts, and function as silencers of FGFR2 exon IIIc through an interaction with the exonic GGG motifs. The lack of RRM1 could account for the reduced silencing activity within hnRNP H3. In addition, the family members have an extensive glycine-rich region near the C-terminus, which may allow them to homo- or heterodimerize. The family also includes a cytoplasmic poly(A)+ mRNA binding protein, GRSF-1, which interacts with RNA in a G-rich element-dependent manner. It may function in RNA packaging, stabilization of RNA secondary structure, or other macromolecular interactions. GRSF-1 also contains three potential RRMs responsible for the RNA binding, and two auxiliary domains (an acidic alpha-helical domain and an N-terminal alanine-rich region) that may play a role in protein-protein interactions and provide binding specificity
GVVRLRGLPYGCTKEEIAQFFSGLEIVPNGITLPMDRRGRSTGEAFVQFASQEIAEQALGKHKEKIGHRY
IEIFRSS
>gnl|CDD|409928 cd12505, RRM2_GRSF1, RNA recognition motif 2 (RRM2) found in G-rich sequence factor 1 (GRSF-1) and similar proteins. This subfamily corresponds to the RRM2 of GRSF-1, a cytoplasmic poly(A)+ mRNA binding protein which interacts with RNA in a G-rich element-dependent manner. It may function in RNA packaging, stabilization of RNA secondary structure, or other macromolecular interactions. GRSF-1 contains three potential RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which are responsible for the RNA binding. In addition, GRSF-1 has two auxiliary domains, an acidic alpha-helical domain and an N-terminal alanine-rich region, that may play a role in protein-protein interactions and provide binding specificity
DGVVRLRGLPYSCTEADIAHFFSGLDIVDITFVMDLRGGRKTGEAFVQFASPEMAAQALLKHKEEIGNRY
IEIFPSR
>gnl|CDD|409929 cd12506, RRM3_hnRNPH_CRSF1_like, RNA recognition motif 3 (RRM3) found in heterogeneous nuclear ribonucleoprotein hnRNP H protein family, G-rich sequence factor 1 (GRSF-1) and similar proteins. This subfamily corresponds to the RRM3 of hnRNP H proteins and GRSF-1. The hnRNP H protein family includes hnRNP H (also termed mcs94-1), hnRNP H2 (also termed FTP-3 or hnRNP H'), hnRNP F and hnRNP H3 (also termed hnRNP 2H9), which represent a group of nuclear RNA binding proteins that are involved in pre-mRNA processing. These proteins have similar RNA binding affinities and specifically recognize the sequence GGGA. They can either stimulate or repress splicing upon binding to a GGG motif. hnRNP H binds to the RNA substrate in the presence or absence of these proteins, whereas hnRNP F binds to the nuclear mRNA only in the presence of cap-binding proteins. hnRNP H and hnRNP H2 are almost identical; both have been found to bind nuclear-matrix proteins. hnRNP H activates exon inclusion by binding G-rich intronic elements downstream of the 5' splice site in the transcripts of c-src, human immunodeficiency virus type 1 (HIV-1), Bcl-X, GRIN1, and myelin. It silences exons when bound to exonic elements in the transcripts of beta-tropomyosin, HIV-1, and alpha-tropomyosin. hnRNP H2 has been implicated in pre-mRNA 3' end formation. hnRNP H3 may be involved in the splicing arrest induced by heat shock. Most family members contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), except for hnRNP H3, in which the RRM1 is absent. RRM1 and RRM2 are responsible for the binding to the RNA at DGGGD motifs, and they play an important role in efficiently silencing the exon. For instance, members in this family can regulate the alternative splicing of the fibroblast growth factor receptor 2 (FGFR2) transcripts, and function as silencers of FGFR2 exon IIIc through an interaction with the exonic GGG motifs. The lack of RRM1 could account for the reduced silencing activity within hnRNP H3. In addition, the family members have an extensive glycine-rich region near the C-terminus, which may allow them to homo- or heterodimerize. The family also includes a cytoplasmic poly(A)+ mRNA binding protein, GRSF-1, which interacts with RNA in a G-rich element-dependent manner. It may function in RNA packaging, stabilization of RNA secondary structure, or other macromolecular interactions. GRSF-1 also contains three potential RRMs responsible for the RNA binding, and two auxiliary domains (an acidic alpha-helical domain and an N-terminal alanine-rich region) that may play a role in protein-protein interactions and provide binding specificity
HTVHMRGLPYRATENDIFEFFSPLNPVNVRIRYNKDGRATGEADVEFATHEDAVAAMSKDRENMGHRYIE
LFLNS
>gnl|CDD|240951 cd12507, RRM1_ESRPs_Fusilli, RNA recognition motif 1 (RRM1) found in epithelial splicing regulatory protein ESRP1, ESRP2, Drosophila RNA-binding protein Fusilli and similar proteins. This subfamily corresponds to the RRM1 of ESRPs and Fusilli. ESRP1 (also termed RBM35A) and ESRP2 (also termed RBM35B). These are epithelial-specific RNA binding proteins that promote splicing of the epithelial variant of the fibroblast growth factor receptor 2 (FGFR2), ENAH (also termed hMena), CD44 and CTNND1 (also termed p120-Catenin) transcripts. They are highly conserved paralogs and specifically bind to GU-rich binding site. ESRP1 and ESRP2 contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The family also includes Drosophila fusilli (fus) gene encoding RNA-binding protein Fusilli. Loss of fusilli activity causes lethality during embryogenesis in flies. Drosophila Fusilli can regulate endogenous fibroblast growth factor receptor 2 (FGFR2) splicing and functions as a splicing factor. It shows high sequence homology to ESRPs and contains three RRMs as well. It also has an N-terminal domain with unknown function and a C-terminal domain particularly rich in alanine, glutamine, and serine
VVRARGLPWQSSDQDIAQFFRGLNIAKGGVALCLSAQGRRNGEALIRFVDQEHRDLALQRHKHHMGTRYI
EVYKA
>gnl|CDD|409930 cd12508, RRM2_ESRPs_Fusilli, RNA recognition motif 2 (RRM2) found in epithelial splicing regulatory protein ESRP1, ESRP2, Drosophila RNA-binding protein Fusilli and similar proteins. This subfamily corresponds to the RRM2 of ESRPs and Fusilli. ESRP1 (also termed RBM35A) and ESRP2 (also termed RBM35B) are epithelial-specific RNA binding proteins that promote splicing of the epithelial variant of the fibroblast growth factor receptor 2 (FGFR2), ENAH (also termed hMena), CD44 and CTNND1 (also termed p120-Catenin) transcripts. They are highly conserved paralogs and specifically bind to GU-rich binding site. ESRP1 and ESRP2 contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The family also includes Drosophila fusilli (fus) gene encoding RNA-binding protein Fusilli.Loss of fusilli activity causes lethality during embryogenesis in flies. Drosophila Fusilli can regulate endogenous FGFR2 splicing and functions as a splicing factor. It shows high sequence homology to ESRPs and contains three RRMs as well. It also has an N-terminal domain with unknown function and a C-terminal domain particularly rich in alanine, glutamine, and serine
QVIVRMRGLPFSATAADILAFFGGECPVTGGKDGILFVTYPDGRPTGDAFVLFATEEDAQQALGKHKELL
GKRYIELFRS
>gnl|CDD|409931 cd12509, RRM3_ESRPs_Fusilli, RNA recognition motif 3 (RRM3) found in epithelial splicing regulatory protein ESRP1, ESRP2, Drosophila RNA-binding protein Fusilli and similar proteins. This subfamily corresponds to the RRM3 of ESRPs and Fusilli. ESRP1 (also termed RBM35A) and ESRP2 (also termed RBM35B) are epithelial-specific RNA binding proteins that promote splicing of the epithelial variant of the fibroblast growth factor receptor 2 (FGFR2), ENAH (also termed hMena), CD44 and CTNND1 (also termed p120-Catenin) transcripts. They are highly conserved paralogs and specifically bind to GU-rich binding site. ESRP1 and ESRP2 contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The family also includes Drosophila fusilli (fus) gene encoding RNA-binding protein Fusilli. Loss of fusilli activity causes lethality during embryogenesis in flies. Drosophila Fusilli can regulate endogenous FGFR2 splicing and functions as a splicing factor. Fusilli shows high sequence homology to ESRPs and contains three RRMs as well. It also has an N-terminal domain with unknown function and a C-terminal domain particularly rich in alanine, glutamine, and serine
RDCIRLRGLPYSATVEDILNFLGEFAKHIAPQGVHMVINAQGRPSGDAFIQMLSAEFARLAAQKRHKHHM
GERYIEVFQCS
>gnl|CDD|409932 cd12510, RRM1_RBM12_like, RNA recognition motif 1 (RRM1) found in RNA-binding protein RBM12, RBM12B and similar proteins. This subfamily corresponds to the RRM1 of RBM12 and RBM12B. RBM12, also termed SH3/WW domain anchor protein in the nucleus (SWAN), is ubiquitously expressed. It contains five distinct RNA binding motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two proline-rich regions, and several putative transmembrane domains. RBM12B show high sequence semilarity with RBM12. It contains five distinct RRMs as well. The biological roles of both RBM12 and RBM12B remain unclear
SVVIRLQGLPWEAGSLDIRRFFSGLTIPDGGVHIIGGEKGEAFIIFATDEDARLAMMRDGQTIKGSKVKL
FLSS
>gnl|CDD|409933 cd12511, RRM2_RBM12_like, RNA recognition motif 2 (RRM2) found in RNA-binding protein RBM12, RBM12B and similar proteins. This subfamily corresponds to the RRM2 of RBM12 and RBM12B. RBM12, also termed SH3/WW domain anchor protein in the nucleus (SWAN), is ubiquitously expressed. It contains five distinct RNA binding motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two proline-rich regions, and several putative transmembrane domains. RBM12B shows high sequence semilarity with RBM12. It contains five distinct RRMs as well. The biological roles of both RBM12 and RBM12B remain unclear
YLSLHGMPYSAMENDVRDFFHGLRVDGVHLLKDHVGRNNGNALVKFASPQDASEGLKCHRMLMGQRFVEV
SPA
>gnl|CDD|409934 cd12512, RRM3_RBM12, RNA recognition motif 3 (RRM3) found in RNA-binding protein 12 (RBM12) and similar proteins. This subfamily corresponds to the RRM3 of RBM12. RBM12, also termed SH3/WW domain anchor protein in the nucleus (SWAN), is ubiquitously expressed. It contains five distinct RNA binding motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two proline-rich regions, and several putative transmembrane domains. The biological role of RBM12 remains unclear
RSRSPHEKGFCVYLKGLPYEAENKHVIEFFKKLDIVEDSIYIAYGPNGRATGEGFVEFRNEIDYKAALCR
HKQYMGNRFIQVHPITKKAMLEKIDMIRKRL
>gnl|CDD|409935 cd12513, RRM3_RBM12B, RNA recognition motif 3 (RRM3) found in RNA-binding protein 12B (RBM12B) and similar proteins. This subgroup corresponds to the RRM3 of RBM12B which contains five distinct RNA binding motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). Its biological role remains unclear
FCVHLKNLSYSVDKRDIRNFFRDLDISDDQIKFLHDKYGKRTREAFVMFKNEKDYQTALSLHKGCLGNRT
VYIYPISRKAM
>gnl|CDD|409936 cd12514, RRM4_RBM12_like, RNA recognition motif 4 (RRM4) found in RNA-binding protein RBM12, RBM12B and similar proteins. This subfamily corresponds to the RRM4 of RBM12 and RBM12B. RBM12, also termed SH3/WW domain anchor protein in the nucleus (SWAN), is ubiquitously expressed. It contains five distinct RNA binding motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two proline-rich regions, and several putative transmembrane domains. RBM12B show high sequence semilarity with RBM12. It contains five distinct RRMs as well. The biological roles of both RBM12 and RBM12B remain unclear
FIRITNLPYDATPVDIQRFFEDHGVRPEDVHLLRNKKGRGNGEALVTFKSEGDAREVLKLNGKKLGKREA
VVE
>gnl|CDD|409937 cd12515, RRM5_RBM12_like, RNA recognition motif 5 (RRM5) found in RNA-binding protein RBM12, RBM12B and similar proteins. This subfamily corresponds to the RRM5 of RBM12 and RBM12B. RBM12, also termed SH3/WW domain anchor protein in the nucleus (SWAN), is ubiquitously expressed. It contains five distinct RNA binding motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two proline-rich regions, and several putative transmembrane domains. RBM12B show high sequence semilarity with RBM12. It contains five distinct RRMs as well. The biological roles of both RBM12 and RBM12B remain unclear
CVVKMRNLPFKATIEDILDFFYGYRVIPDSVSIRYNDDGQPTGDARVAFPSPREARRAVRELNNRPLGGR
KVKLF
>gnl|CDD|409938 cd12516, RRM1_RBM26, RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding protein 26 (RBM26). This subgroup corresponds to the RRM1 of RBM26, also known as cutaneous T-cell lymphoma (CTCL) tumor antigen se70-2, which represents a cutaneous lymphoma (CL)-associated antigen. It contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The RRMs may play some functional roles in RNA-binding or protein-protein interactions
NTKLELRKVPPELNNISKLNEHFSKFGTIVNLQVAYQGDPEGALIQFATHEEAKRAISSTEAVLNNRFIK
VYWHRE
>gnl|CDD|409939 cd12517, RRM_RBM27, RNA recognition motif (RRM) found in vertebrate RNA-binding protein 27 (RBM27). This subgroup corresponds to the RRM of RBM27 which contains a single RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain). Although the specific function of the RRM in RBM27 remains unclear, it shows high sequence similarity with RRM1of RBM26, which functions as a cutaneous lymphoma (CL)-associated antigen
NTKLEVRKIPQELNNITQLNEHFSKFGTIVNIQVAFGGDPEAALIQYTTNEEARRAISSTEAVLNNRFIR
VLWHRE
>gnl|CDD|409940 cd12518, RRM_SRSF11, RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 11 (SRSF11) and similar proteins. This subgroup corresponds to the RRM of SRSF11, also termed arginine-rich 54 kDa nuclear protein (SRp54 or p54), which belongs to a family of proteins containing regions rich in serine-arginine dipeptides (SR proteins family). It is involved in bridge-complex formation and splicing by mediating protein-protein interactions across either introns or exons. SRSF11 has been identified as a tau exon 10 splicing repressor. It interacts with a purine-rich element in exon 10, and suppresses exon 10 inclusion by antagonizing Tra2beta, an SR-domain-containing protein that enhances exon 10 inclusion. SRSF11 is a unique SR family member and may regulate the alternative splicing in a tissue- and substrate-dependent manner. It can directly interact with the U2 auxiliary factor 65-kDa subunit (U2AF65), a protein associated with the 3' splice site. In addition, unlike the typical SR proteins, SRSF11 associates with other SR proteins but not with the U1 small nuclear ribonucleoprotein U1-70K or the U2 auxiliary factor 35-kDa subunit (U2AF35). SREK1 has unique properties in regulating alternative splicing of different pre-mRNAs; it promotes the use of the distal 5' splice site in E1A pre-mRNA alternative splicing. It also inhibits cryptic splice site selection on the beta-globin pre-mRNA containing competing 5' splice sites. SREK1 contains an RNA recognition motif (RRM), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and one serine-arginine (SR)-rich domains (SR domains)
VIQVTNVSPSASSEQMRTLFGFLGKIDELRLFPPDDSPLPVTSRVCFVKFHEPDSAVVAQHLTNTVFVDR
ALIVVPYAEG
>gnl|CDD|409941 cd12519, RRM1_SREK1, RNA recognition motif 1 (RRM1) found in splicing regulatory glutamine/lysine-rich protein 1 (SREK1) and similar proteins. This subgroup corresponds to the RRM1 of SREK1, also termed serine/arginine-rich-splicing regulatory protein 86-kDa (SRrp86), or splicing factor arginine/serine-rich 12 (SFRS12), or splicing regulatory protein 508 amino acid (SRrp508). SREK1 belongs to a family of proteins containing regions rich in serine-arginine dipeptides (SR proteins family), and is involved in bridge-complex formation and splicing by mediating protein-protein interactions across either introns or exons. It is a unique SR family member and may play a crucial role in determining tissue specific patterns of alternative splicing. SREK1 can alter splice site selection by both positively and negatively modulating the activity of other SR proteins. For instance, SREK1 can activate SRp20 and repress SC35 in a dose-dependent manner both in vitro and in vivo. In addition, SREK1 generally contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and two serine-arginine (SR)-rich domains (SR domains) separated by an unusual glutamic acid-lysine (EK) rich region. The RRM and SR domains are highly conserved among other members of the SR superfamily. However, the EK domain is unique to SREK1; plays a modulatory role controlling SR domain function by involvement in the inhibition of both constitutive and alternative splicing and in the selection of splice-site
VIQVTNLSAAVTSDQMRTLFSFLGDIEELRLYPPDNAPLAFSSKVCYVKYREPSSVGVAQHLTNTVFIDR
ALIVVPCAEG
>gnl|CDD|240964 cd12520, RRM1_MRN1, RNA recognition motif 1 (RRM1) found in RNA-binding protein MRN1 and similar proteins. This subgroup corresponds to the RRM1 of MRN1, also termed multicopy suppressor of RSC-NHP6 synthetic lethality protein 1, or post-transcriptional regulator of 69 kDa,which is a RNA-binding protein found in yeast. Although its specific biological role remains unclear, MRN1 might be involved in translational regulation. Members in this family contain four copies of conserved RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
SRTVYLGNLPPNTTVKELLSHVRSGPIENVRILPEKNCAFISFLDPSAATAFHSDAILKRLSIKGVELKI
GWGK
>gnl|CDD|240965 cd12521, RRM3_MRN1, RNA recognition motif 3 (RRM3) found in RNA-binding protein MRN1 and similar proteins. This subgroup corresponds to the RRM3 of MRN1, also termed multicopy suppressor of RSC-NHP6 synthetic lethality protein 1, or post-transcriptional regulator of 69 kDa, which is a RNA-binding protein found in yeast. Although its specific biological role remains unclear, MRN1 might be involved in translational regulation. Members in this family contain four copies of conserved RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
NRTVYLGNIHPDTKIEEICNAVRGGLLQSIRYIPEKHICFVTFIDPTAAAQFYAMSSIQGLTLHNRRLKV
GWGK
>gnl|CDD|409942 cd12522, RRM4_MRN1, RNA recognition motif 4 (RRM4) found in RNA-binding protein MRN1 and similar proteins. This subgroup corresponds to the RRM4 of MRN1, also termed multicopy suppressor of RSC-NHP6 synthetic lethality protein 1, or post-transcriptional regulator of 69 kDa, which is a RNA-binding protein found in yeast. Although its specific biological role remains unclear, MRN1 might be involved in translational regulation. Members in this family contain four copies of conserved RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
GASRNVYIGNIDDVRVLTEERLRHDFSQYGEIEQVNFLREKNCAFVNFTNIANAIKAIDKIKSKPYYKDL
KINFGKDRCGN
>gnl|CDD|409943 cd12523, RRM2_MRN1, RNA recognition motif 2 (RRM2) found in RNA-binding protein MRN1 and similar proteins. This subgroup corresponds to the RRM2 of MRN1, also termed multicopy suppressor of RSC-NHP6 synthetic lethality protein 1, or post-transcriptional regulator of 69 kDa, which is a RNA-binding protein found in yeast. Although its specific biological role remains unclear, MRN1 might be involved in translational regulation. Members in this family contain four copies of conserved RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
GASRNVYLGNLPESITEEELREDLEKFGPIDQIKIVKEKNIAFVHFLSIANAIKVVTTLPLNPKWAKRRI
YYGKDRCA
>gnl|CDD|409944 cd12524, RRM1_MEI2_like, RNA recognition motif 1 (RRM1) found in plant Mei2-like proteins. This subgroup corresponds to the RRM1 of Mei2-like proteins that represent an ancient eukaryotic RNA-binding proteins family. Their corresponding Mei2-like genes appear to have arisen early in eukaryote evolution, been lost from some lineages such as Saccharomyces cerevisiae and metazoans, and diversified in the plant lineage. The plant Mei2-like genes may function in cell fate specification during development, rather than as stimulators of meiosis. Members in this family contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The C-terminal RRM (RRM3) is unique to Mei2-like proteins and it is highly conserved between plants and fungi. Up to date, the intracellular localization, RNA target(s), cellular interactions and phosphorylation states of Mei2-like proteins in plants remain unclear
SRTLFVRNINSSVEDEELRALFEQFGEIRTLYTACKHRGFIMVSYYDIRAAQSAKRALQGTELGGRKLDI
HFSIPKD
>gnl|CDD|409945 cd12525, RRM1_MEI2_fungi, RNA recognition motif 1 (RRM1) found in fungal Mei2-like proteins. This subgroup corresponds to the RRM1 of fungal Mei2-like proteins. The Mei2 protein is an essential component of the switch from mitotic to meiotic growth in the fission yeast Schizosaccharomyces pombe. It is an RNA-binding protein that contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). In the nucleus, S. pombe Mei2 stimulates meiosis upon binding a specific non-coding RNA through its C-terminal RRM motif
DVGSVPTRYLKVTGVPKDVSTSNLKEIFEKMGDVKGIFVKKLLSKGIVIVSFHDLRQAIKAYKDLQSKWR
FINDRYLTAQFCVNNSLIKMI
>gnl|CDD|409946 cd12526, RRM1_EAR1_like, RNA recognition motif 1 (RRM1) found in terminal EAR1-like proteins. This subgroup corresponds to the RRM1 of terminal EAR1-like proteins, including terminal EAR1-like protein 1 and 2 (TEL1 and TEL2) found in land plants. They may play a role in the regulation of leaf initiation. The terminal EAR1-like proteins are putative RNA-binding proteins carrying three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and TEL characteristic motifs that allow sequence and putative functional discrimination between the terminal EAR1-like proteins and Mei2-like proteins
TRSVLLSPVPPHVPETDLRRDLEAFGEVRAVQMERFREGVVTVHFYDLRHAERAFAEIRTRHYFQQLRYG
Q
>gnl|CDD|409947 cd12527, RRM2_EAR1_like, RNA recognition motif 2 (RRM2) found in terminal EAR1-like proteins. This subgroup corresponds to the RRM2 of terminal EAR1-like proteins, including terminal EAR1-like protein 1 and 2 (TEL1 and TEL2) found in land plants. They may play a role in the regulation of leaf initiation. The terminal EAR1-like proteins are putative RNA-binding proteins carrying three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and TEL characteristic motifs that allow sequence and putative functional discrimination between the terminal EAR1-like proteins and Mei2-like proteins
QGSLVILNLLPAVSSFTLREIFQVYGDVKDVRETPLKPSQRFVEFFDVRDAARALHEMNGKEIFGKRLVI
E
>gnl|CDD|240972 cd12528, RRM2_MEI2_fungi, RNA recognition motif 2 (RRM2) found in fungal Mei2-like proteins. This subgroup corresponds to the RRM2 of fungal Mei2-like proteins.The Mei2 protein is an essential component of the switch from mitotic to meiotic growth in the fission yeast Schizosaccharomyces pombe. It is an RNA-binding protein that contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). In the nucleus, S. pombe Mei2 stimulates meiosis upon binding a specific non-coding RNA through its C-terminal RRM motif
SDNEGQILISVQGDSHNSDLVKNSLQNLLSTFGDLKAFKSLPSQQDNVKEFICEFFDTRDADNAVDELNG
RVVDNCKLEAT
>gnl|CDD|409948 cd12529, RRM2_MEI2_like, RNA recognition motif 2 (RRM2) found in plant Mei2-like proteins. This subgroup corresponds to the RRM2 of Mei2-like proteins that represent an ancient eukaryotic RNA-binding proteins family. Their corresponding Mei2-like genes appear to have arisen early in eukaryote evolution, been lost from some lineages such as Saccharomyces cerevisiae and metazoans, and diversified in the plant lineage. The plant Mei2-like genes may function in cell fate specification during development, rather than as stimulators of meiosis. Members in this family contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The C-terminal RRM (RRM3) is unique to Mei2-like proteins and is highly conserved between plants and fungi. To date, the intracellular localization, RNA target(s), cellular interactions and phosphorylation states of Mei2-like proteins in plants remain unclear
QGTLVVFNLDPSISNDDLHQIFGAYGEIKEIRETPNKRHHKFIEFYDVRSAEAALKALNKSEIAGKRIKL
E
>gnl|CDD|240974 cd12530, RRM3_EAR1_like, RNA recognition motif 3 (RRM3) found in terminal EAR1-like proteins. This subgroup corresponds to the RRM3 of terminal EAR1-like proteins, including terminal EAR1-like protein 1 and 2 (TEL1 and TEL2) found in land plants. They may play a role in the regulation of leaf initiation. The terminal EAR1-like proteins are putative RNA-binding proteins carrying three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and TEL characteristic motifs that allow sequence and putative functional discrimination between the terminal EAR1-like proteins and Mei2-like proteins
RTTLMIKNIPNKYSQKLLLDMLDTHCIQCNQHIEDSSQPVSSYDFVYLPIDFKNKCNLGYAFVNFTSPEA
TWRFYKAFHNQQWEEFNSRKICQITYARVQG
>gnl|CDD|240975 cd12531, RRM3_MEI2_like, RNA recognition motif 3 (RRM3) found in plant Mei2-like proteins. This subgroup corresponds to the RRM3 of Mei2-like proteins, representing an ancient eukaryotic RNA-binding proteins family. Their corresponding Mei2-like genes appear to have arisen early in eukaryote evolution, been lost from some lineages such as Saccharomyces cerevisiae and metazoans, and diversified in the plant lineage. The plant Mei2-like genes may function in cell fate specification during development, rather than as stimulators of meiosis. Members in this family contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The C-terminal RRM (RRM3) is unique to Mei2-like proteins and is highly conserved between plants and fungi. To date, the intracellular localization, RNA target(s), cellular interactions and phosphorylation states of Mei2-like proteins in plants remain unclear
LMIKNIPNKYTQKMLLAAIDEKHRGTYDFFYLPIDFKNKCNVGYAFINMISPELIVPFYKAFNGKKWEKF
NSEKVCSLAYARIQGK
>gnl|CDD|409949 cd12532, RRM3_MEI2_fungi, RNA recognition motif 3 (RRM3) found in fungal Mei2-like proteins. This subgroup corresponds to the RRM3 of fungal Mei2-like proteins. The Mei2 protein is an essential component of the switch from mitotic to meiotic growth in the fission yeast Schizosaccharomyces pombe. It is an RNA-binding protein that contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). In the nucleus, S. pombe Mei2 stimulates meiosis upon binding a specific non-coding RNA through its C-terminal RRM motif
RTTCMIKNIPNKFTQQMLKEYLDETNKGTYDFVYLRIDFKNNCNVGYAFINFTEPESIVTFYKARQGKKW
NKFNSEKICDISYANIQGKD
>gnl|CDD|409950 cd12533, RRM_EWS, RNA recognition motif (RRM) found in vertebrate Ewing Sarcoma Protein (EWS). This subgroup corresponds to the RRM of EWS, also termed Ewing sarcoma breakpoint region 1 protein, a member of the FET (previously TET) (FUS/TLS, EWS, TAF15) family of RNA- and DNA-binding proteins whose expression is altered in cancer. It is a multifunctional protein and may play roles in transcription and RNA processing. EWS is involved in transcriptional regulation by interacting with the preinitiation complex TFIID and the RNA polymerase II (RNAPII) complexes. It is also associated with splicing factors, such as the U1 snRNP protein U1C, suggesting its implication in pre-mRNA splicing. Additionally, EWS has been shown to regulate DNA damage-induced alternative splicing (AS). Like other members in the FET family, EWS contains an N-terminal Ser, Gly, Gln and Tyr-rich region composed of multiple copies of a degenerate hexapeptide repeat motif. The C-terminal region consists of a conserved nuclear import and retention signal (C-NLS), a C2/C2 zinc-finger motif, a conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and at least 1 arginine-glycine-glycine (RGG)-repeat region. EWS specifically binds to poly G and poly U RNA. It also binds to the proximal-element DNA of the macrophage-specific promoter of the CSF-1 receptor gene
STIYVQGLNENVTLEELADFFKHCGVVKINKRTGQPMINIYTDKETGKPKGDATVSYEDPPAAKAAVEWF
DGKDFQGNKLKVSM
>gnl|CDD|240978 cd12534, RRM_SARFH, RNA recognition motif (RRM) found in Drosophila melanogaster RNA-binding protein cabeza and similar proteins. This subgroup corresponds to the RRM in cabeza, also termed P19, or sarcoma-associated RNA-binding fly homolog (SARFH). It is a putative homolog of human RNA-binding proteins FUS (also termed TLS or Pigpen or hnRNP P2), EWS (also termed EWSR1), TAF15 (also termed hTAFII68 or TAF2N or RPB56), and belongs to the of the FET (previously TET) (FUS/TLS, EWS, TAF15) family of RNA- and DNA-binding proteins whose expression is altered in cancer. It is a nuclear RNA binding protein that may play an important role in the regulation of RNA metabolism during fly development. Cabeza contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
VFVSNLPPNTTEQDLAEHFGSIGIIKIDKKTGKPKIWLYKDKDTGEPKGEATVTYDDPHAASAAIEWFNN
KDFMGNTIKVSLA
>gnl|CDD|409951 cd12535, RRM_FUS_TAF15, RNA recognition motif (RRM) found in vertebrate fused in Ewing's sarcoma protein (FUS), TATA-binding protein-associated factor 15 (TAF15) and similar proteins. This subgroup corresponds to the RRM of FUS and TAF15. FUS (TLS or Pigpen or hnRNP P2), also termed 75 kDa DNA-pairing protein (POMp75), or oncoprotein TLS (Translocated in liposarcoma), is a member of the FET (previously TET) (FUS/TLS, EWS, TAF15) family of RNA- and DNA-binding proteins whose expression is altered in cancer. It is a multi-functional protein and has been implicated in pre-mRNA splicing, chromosome stability, cell spreading, and transcription. FUS was originally identified in human myxoid and round cell liposarcomas as an oncogenic fusion with the stress-induced DNA-binding transcription factor CHOP (CCAAT enhancer-binding homologous protein) and later as hnRNP P2, a component of hnRNP H complex assembled on pre-mRNA. It can form ternary complexes with hnRNP A1 and hnRNP C1/C2. Additional research indicates that FUS binds preferentially to GGUG-containing RNAs. In the presence of Mg2+, it can bind both single- and double-stranded DNA (ssDNA/dsDNA) and promote ATP-independent annealing of complementary ssDNA and D-loop formation in superhelical dsDNA. FUS has been shown to be recruited by single stranded noncoding RNAs to the regulatory regions of target genes such as cyclin D1, where it represses transcription by disrupting complex formation. TAF15 (TAFII68), also termed TATA-binding protein-associated factor 2N (TAF2N), or RNA-binding protein 56 (RBP56), originally identified as a TAF in the general transcription initiation TFIID complex, is a novel RNA/ssDNA-binding protein with homology to the proto-oncoproteins FUS and EWS (also termed EWSR1), belonging to the FET family as well. TAF15 likely functions in RNA polymerase II (RNAP II) transcription by interacting with TFIID and subunits of RNAP II itself. TAF15 is also associated with U1 snRNA, chromatin and RNA, in a complex distinct from the Sm-containing U1 snRNP that functions in splicing. Like other members in the FET family, both FUS and TAF15 contain an N-terminal Ser, Gly, Gln and Tyr-rich region composed of multiple copies of a degenerate hexapeptide repeat motif. The C-terminal region consists of a conserved nuclear import and retention signal (C-NLS), a C2/C2 zinc-finger motif, a conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and at least 1 arginine-glycine-glycine (RGG)-repeat region
DNNTIFVQGLGEDVTIDSVADYFKQIGIIKTNKKTGKPMINLYTDKETGKLKGEATVSFDDPPSAKAAID
WFDGKEFSGNPIKVSF
>gnl|CDD|409952 cd12536, RRM1_RBM39, RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding protein 39 (RBM39). This subgroup corresponds to the RRM1 of RBM39, also termed hepatocellular carcinoma protein 1, or RNA-binding region-containing protein 2, or splicing factor HCC1, a nuclear autoantigen that contains an N-terminal arginine/serine rich (RS) motif and three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). An octapeptide sequence called the RS-ERK motif is repeated six times in the RS region of RBM39. Based on the specific domain composition, RBM39 has been classified into a family of non-snRNP (small nuclear ribonucleoprotein) splicing factors that are usually not complexed to snRNAs
ARTVFCMQLAARIRPRDLEEFFSTVGKVRDVRMISDRNSRRSKGIAYVEFVDVSSVPLAIGLTGQRVLGV
PIIVQASQAEKNR
>gnl|CDD|409953 cd12537, RRM1_RBM23, RNA recognition motif 1 (RRM1) found in vertebrate probable RNA-binding protein 23 (RBM23). This subgroup corresponds to the RRM1 of RBM23, also termed RNA-binding region-containing protein 4, or splicing factor SF2, which may function as a pre-mRNA splicing factor. It shows high sequence homology to RNA-binding protein 39 (RBM39 or HCC1), a nuclear autoantigen that contains an N-terminal arginine/serine rich (RS) motif and three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). In contrast to RBM39, RBM23 contains only two RRMs
ARTVFCMQLAARIRPRDLEDFFSAVGKVRDVRIISDRNSRRSKGIAYVEFCEIQSVPLAIGLTGQRLLGV
PIIVQASQAEKNRLA
>gnl|CDD|409954 cd12538, RRM_U2AF35, RNA recognition motif (RRM) found in U2 small nuclear ribonucleoprotein auxiliary factor U2AF 35 kDa subunit (U2AF35). This subgroup corresponds to the RRM of U2AF35, also termed U2AF1, which is one of the small subunits of U2 small nuclear ribonucleoprotein (snRNP) auxiliary factor (U2AF). It has been implicated in the recruitment of U2 snRNP to pre-mRNAs and is a highly conserved heterodimer composed of large and small subunits. U2AF35 directly binds to the 3' splice site of the conserved AG dinucleotide and performs multiple functions in the splicing process in a substrate-specific manner. It promotes U2 snRNP binding to the branch-point sequences of introns through association with the large subunit of U2AF, U2AF65 (also termed U2AF2). U2AF35 contains two N-terminal zinc fingers, a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal arginine/serine (SR)-rich segment interrupted by glycines. U2AF35 binds both U2AF65 and the pre-mRNA through its RRM domain
SQTILLQNLYQNPQNTPQSADGLKVKVSDVELQEHFDEFYEDVFVELEEKYGEIEEMNVCDNLGDHLVGN
VYVKFRREEDAEKAVNDLNNRWFNGQPIYAELSP
>gnl|CDD|409955 cd12539, RRM_U2AF35B, RNA recognition motif (RRM) found in splicing factor U2AF 35 kDa subunit B (U2AF35B). This subgroup corresponds to the RRM of U2AF35B, also termed zinc finger CCCH domain-containing protein 60 (C3H60), which is one of the small subunits of U2 small nuclear ribonucleoprotein (snRNP) auxiliary factor (U2AF). It has been implicated in the recruitment of U2 snRNP to pre-mRNAs and is a highly conserved heterodimer composed of large and small subunits. Members in this family are mainly found in plant. They show high sequence homology to vertebrates U2AF35 that directly binds to the 3' splice site of the conserved AG dinucleotide and performs multiple functions in the splicing process in a substrate-specific manner. U2AF35B contains two N-terminal zinc fingers, a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal arginine/serine (SR)-rich domain. In contrast to U2AF35, U2AF35B has a plant-specific conserved C-terminal region containing SERE motif(s), which may have an important function specific to higher plants
PTILLSNMYQNPIMNAPLGAAQGIPLDPRELQEHFEDFYEDVFEELSKFGEVEALNVCDNLGDHMVGNVY
VKFRDEEHAAAALKALQGRFYAGRPIIVEFSP
>gnl|CDD|409956 cd12540, RRM_U2AFBPL, RNA recognition motif (RRM) found in U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1 (U2AFBPL) and similar proteins. This subgroup corresponds to the RRM of U2AFBPL, a human homolog of the imprinted mouse gene U2afbp-rs, which encodes a U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1 (U2AFBPL), also termed CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 1 (U2AF1RS1), or U2 small nuclear RNA auxiliary factor 1-like 1 (U2AF1L1). Although the biological role of U2AFBPL remains unclear, it shows high sequence homology to splicing factor U2AF 35 kDa subunit (U2AF35 or U2AF1) that directly binds to the 3' splice site of the conserved AG dinucleotide and performs multiple functions in the splicing process in a substrate-specific manner. Like U2AF35, U2AFBPL contains two N-terminal zinc fingers, a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal arginine/serine (SR)-rich domain
TLLIPNMFNTFGLEQCKRDDYDTDAGLEYSEEDLYSDFLEFYEDVLPEFKKFGKVVQFKVCCNSEPHLRG
NVYVQYQSEEEALKAFTSFNGRWYAGKQLQCEFSP
>gnl|CDD|409957 cd12541, RRM2_La, RNA recognition motif 2 in La autoantigen (La or LARP3) and similar proteins. This subgroup corresponds to the RRM2 of La autoantigen, also termed Lupus La protein, or La ribonucleoprotein, or Sjoegren syndrome type B antigen (SS-B), a highly abundant nuclear phosphoprotein and well conserved in eukaryotes. It specifically binds the 3'-terminal UUU-OH motif of nascent RNA polymerase III transcripts and protects them from exonucleolytic degradation by 3' exonucleases. In addition, La can directly facilitate the translation and/or metabolism of many UUU-3' OH-lacking cellular and viral mRNAs, through binding internal RNA sequences within the untranslated regions of target mRNAs. La contains an N-terminal La motif (LAM), followed by two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). In addition, it possesses a short basic motif (SBM) and a nuclear localization signal (NLS) at the C-terminus
GCILHFSGVGEQTSREDLKEAFEKHGEVAWIDFARGQTEGYVRFKEEDAAKEALEKAKEAKNGLKIRGKE
VTVKLLE
>gnl|CDD|409958 cd12542, RRM2_LARP7, RNA recognition motif 2 in La-related protein 7 (LARP7) and similar proteins. This subgroup corresponds to the RRM2 of LARP7, also termed La ribonucleoprotein domain family member 7, or P-TEFb-interaction protein for 7SK stability (PIP7S), an oligopyrimidine-binding protein that binds to the highly conserved 3'-terminal U-rich stretch (3' -UUU-OH) of 7SK RNA. LARP7 is a stable component of the 7SK small nuclear ribonucleoprotein (7SK snRNP). It intimately associates with all the nuclear 7SK and is required for 7SK stability. LARP7 also acts as a negative transcriptional regulator of cellular and viral polymerase II genes, acting by means of the 7SK snRNP system. LARP7 plays an essential role in the inhibition of positive transcription elongation factor b (P-TEFb)-dependent transcription, which has been linked to the global control of cell growth and tumorigenesis. LARP7 contains a La motif (LAM) and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), at the N-terminal region, which mediates binding to the U-rich 3' terminus of 7SK RNA. LARP7 also carries another putative RRM domain at its C-terminus
GVIVKIILTEPLPGRKQFKDELKPLSDVAYVDILEGDTEAYVRFKTPEAAQKVVEQKKKHNWKLEILSGD
EEQRYWQK
>gnl|CDD|409959 cd12543, RRM2_PAR14, RNA recognition motif 2 in vertebrate poly [ADP-ribose] polymerase 14 (PARP-14). This subgroup corresponds to the RRM2 of PARP-14, also termed aggressive lymphoma protein 2, a member of the B aggressive lymphoma (BAL) family of macrodomain-containing PARPs. It is expressed in B lymphocytes and interacts with the IL-4-induced transcription factor Stat6. It plays a fundamental role in the regulation of IL-4-induced B-cell protection against apoptosis after irradiation or growth factor withdrawal. It mediates IL-4 effects on the levels of gene products that regulate cell survival, proliferation, and lymphomagenesis. PARP-14 acts as a transcriptional switch for Stat6-dependent gene activation. In the presence of IL-4, PARP-14 activates transcription by facilitating the binding of Stat6 to the promoter and release of HDACs from the promoter with an IL-4 signal. In contrast, in the absence of a signal, PARP-14 acts as a transcriptional repressor by recruiting HDACs. Absence of PARP-14 protects against Myc-induced developmental block and lymphoma. Thus, PARP-14 may play an important role in Myc-induced oncogenesis. Additional research indicates that PARP-14 is also a binding partner with phosphoglucose isomerase (PGI)/ autocrine motility factor (AMF). It can inhibit PGI/AMF ubiquitination, thus contributing to its stabilization and secretion. PARP-14 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), three tandem macro domains, and C-terminal region with sequence homology to PARP catalytic domain
TCKIRAENLPPNTNSDYLMLYFENPYNGGIEVDGVTVDPEEESAIITFADPKDVQKIIALKHQFNKMPFS
VLPYY
>gnl|CDD|409960 cd12544, RRM_NMI, RNA recognition motif in N-myc-interactor (Nmi) and similar proteins. This subgroup corresponds to the RRM.in Nmi, also termed N-myc and STAT interactor, an interferon inducible protein that interacts with c-Myc, N-Myc, Max and c-Fos, and other transcription factors containing bHLH-ZIP, bHLH or ZIP domains. In addition to binding Myc proteins, Nmi also associates with all the Stat family of transcription factors except Stat2. In response to cytokines (e.g. IL-2 and IFN-gamma) stimulation, Nmi can enhance Stat-mediated transcriptional activity through recruiting the Stat1 and Stat5 transcriptional coactivators, CREB-binding protein (CBP) and p300. Nmi contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
KKINVSNIPDPLPDERMRDKLELSFSKPSRGGGEVEDVHYDRESGTAVITFLESGVAERIAKKKHYPFVA
SCGEHRVTVSP
>gnl|CDD|409961 cd12545, RRM_IN35, RNA recognition motif in interferon-induced 35 kDa protein (IFP 35) and similar proteins. This subgroup corresponds to the RRM in IFP 35, an interferon-induced leucine zipper protein that can specifically form homodimers. Distinct from known bZIP proteins, IFP 35 lacks a basic domain critical for DNA binding. IFP 35 may negatively regulate other bZIP transcription factors by protein-protein interaction. For instance, it can form heterodimers with B-ATF, a member of the AP1 transcription factor family. IFP 35 contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
RRILVSNLPIEEPEERILDKLEIFFGKTRNGGGEVDEREFLDDCGSVVLTFVEDGVAKRLTDKGQFEVPF
GKRKYKVKV
>gnl|CDD|409962 cd12546, RRM_RBM43, RNA recognition motif in vertebrate RNA-binding protein 43 (RBM43). This subgroup corresponds to the RRM of RBM43, a putative RNA-binding protein containing one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). Although its biological function remains unclear, RBM43 shows high sequence homology to poly [ADP-ribose] polymerase 10 (PARP-10), which is a novel oncoprotein c-Myc-interacting protein with poly(ADP-ribose) polymerase activity
RTIVVSGLPDDLFEGALKDKLEIHFQRRKNGGGDVETVTYPTNTKGVAYVTFEEEEVAQNVLEKEQVLED
KVLEVKL
>gnl|CDD|409963 cd12547, RRM1_2_PAR10, RNA recognition motif 1 and 2 in poly [ADP-ribose] polymerase 10 (PARP-10) and similar proteins. This subgroup corresponds to the RRM1 and RRM2 of PARP-10, a novel oncoprotein c-Myc-interacting protein with poly(ADP-ribose) polymerase activity. It is localized to the nuclear and cytoplasmic compartments. In addition to the PARP activity, PARP-10 is also involved in the control of cell proliferation by inhibiting c-Myc- and E1A-mediated cotransformation of primary cells. PARP-10 may play a role in nuclear processes including the regulation of chromatin, gene transcription, and nuclear/cytoplasmic transport. It contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two overlapping C-terminal domains composed of a glycine-rich region and a region with homology to catalytic domains of PARP enzymes (PARP domain). In addition, PARP-10 contains two ubiquitin-interacting motifs (UIM)
GTLEVSGFSPDTSDELLELYFENKRRSGGGEVESIQRRGDKAFITFEDPSVAERVLARAEHVLNGATLTV
KP
>gnl|CDD|409964 cd12548, RRM_Set1A, RNA recognition motif in vertebrate histone-lysine N-methyltransferase Setd1A (Set1A). This subgroup corresponds to the RRM of Setd1A, also termed SET domain-containing protein 1A (Set1A), or lysine N-methyltransferase 2F, or Set1/Ash2 histone methyltransferase complex subunit Set1, a ubiquitously expressed vertebrates histone methyltransferase that exhibits high homology to yeast Set1. Set1A is localized to euchromatic nuclear speckles and associates with a complex containing six human homologs of the yeast Set1/COMPASS complex, including CXXC finger protein 1 (CFP1; homologous to yeast Spp1), Rbbp5 (homologous to yeast Swd1), Ash2 (homologous to yeast Bre2), Wdr5 (homologous to yeast Swd3), and Wdr82 (homologous to yeast Swd2). Set1A contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), an N- SET domain, and a C-terminal catalytic SET domain followed by a post-SET domain. In contrast to Set1B, Set1A additionally contains an HCF-1 binding motif that interacts with HCF-1 in vivo
PLKEVTFARLNDNVREPFLADMCRKFGEVEEVEILLHPKTRKHLGLAKVLFTSTRGAKDTVKHLHNTSVM
GNIIHAQLDIKGQQRMKYYDLIVSG
>gnl|CDD|409965 cd12549, RRM_Set1B, RNA recognition motif in vertebrate histone-lysine N-methyltransferase Setd1B (Set1B). This subgroup corresponds to the RRM of Setd1B, also termed SET domain-containing protein 1B (Set1B), or lysine N-methyltransferase 2G, a ubiquitously expressed vertebrates histone methyltransferase that exhibits high homology to yeast Set1. Set1B is localized to euchromatic nuclear speckles and associates with a complex containing six human homologs of the yeast Set1/COMPASS complex, including CXXC finger protein 1 (CFP1; homologous to yeast Spp1), Rbbp5 (homologous to yeast Swd1), Ash2 (homologous to yeast Bre2), Wdr5 (homologous to yeast Swd3), and Wdr82 (homologous to yeast Swd2). Set1B complex is a histone methyltransferase that produces trimethylated histone H3 at Lys4. Set1B contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), an N- SET domain, and a C-terminal catalytic SET domain followed by a post-SET domain
PPKQVTFAKLNDNIRENFLRDMCKKYGEVEEVEILYNPKNKKHLGIAKVVFATVKGAKDAVQHLHNTSVM
GNIIHVELDTKGETRMRFYELLV
>gnl|CDD|409966 cd12550, RRM_II_PABPN1, RNA recognition motif in type II polyadenylate-binding protein 2 (PABP-2) and similar proteins. This subgroup corresponds to the RRM of PABP-2, also termed poly(A)-binding protein 2, or nuclear poly(A)-binding protein 1 (PABPN1), or poly(A)-binding protein II (PABII), which is a ubiquitously expressed type II nuclear poly(A)-binding protein that directs the elongation of mRNA poly(A) tails during pre-mRNA processing. Although PABP-2 binds poly(A) with high affinity and specificity as type I poly(A)-binding proteins, it contains only one highly conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), which is responsible for the poly(A) binding. In addition, PABP-2 possesses an acidic N-terminal domain that is essential for the stimulation of PAP, and an arginine-rich C-terminal domain
SVYVGNVDYGATAEELEAHFHGCGSVNRVTILCDKFSGHPKGFAYIEFADKESVRTALALDESLFRGRQI
KVMPKR
>gnl|CDD|409967 cd12551, RRM_II_PABPN1L, RNA recognition motif in vertebrate type II embryonic polyadenylate-binding protein 2 (ePABP-2). This subgroup corresponds to the RRM of ePABP-2, also termed embryonic poly(A)-binding protein 2, or poly(A)-binding protein nuclear-like 1 (PABPN1L). ePABP-2 is a novel embryonic-specific cytoplasmic type II poly(A)-binding protein that is expressed during the early stages of vertebrate development and in adult ovarian tissue. It may play an important role in the poly(A) metabolism of stored mRNAs during early vertebrate development. ePABP-2 shows significant sequence similarity to the ubiquitously expressed nuclear polyadenylate-binding protein 2 (PABP-2 or PABPN1). Like PABP-2, ePABP-2 contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), which is responsible for the poly(A) binding. In addition, it possesses an acidic N-terminal domain predicted to form a coiled-coil and an arginine-rich C-terminal domain
SVYVGNVDYGSTADELEAHFNGCGPINRVTILCDKFSGHPKGYAYIEFATRSSVQAAVALDESSFRGRVI
KVLPKRT
>gnl|CDD|409968 cd12552, RRM_Nop15p, RNA recognition motif in yeast ribosome biogenesis protein 15 (Nop15p) and similar proteins. This subgroup corresponds to the RRM of Nop15p, also termed nucleolar protein 15, which is encoded by YNL110C from Saccharomyces cerevisiae, and localizes to the nucleoplasm and nucleolus. Nop15p has been identified as a component of a pre-60S particle. It interacts with RNA components of the early pre-60S particles. Furthermore, Nop15p binds directly to a pre-rRNA transcript in vitro and is required for pre-rRNA processing. It functions as a ribosome synthesis factor required for the 5' to 3' exonuclease digestion that generates the 5' end of the major, short form of the 5.8S rRNA as well as for processing of 27SB to 7S pre-rRNA. Nop15p also play a specific role in cell cycle progression. Nop15p contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
IIYVSHLPHGFHEKELKKYFAQFGDLKNVRLARSKKTGNSKHYGFLEFVNPEDAMIAQKSMNNYLLMGKL
LQVRVLP
>gnl|CDD|409969 cd12553, RRM1_RBM15, RNA recognition motif 1 (RRM1) found in vertebrate RNA binding motif protein 15 (RBM15). This subgroup corresponds to the RRM1 of RBM15, also termed one-twenty two protein 1 (OTT1), conserved in eukaryotes, a novel mRNA export factor and component of the NXF1 pathway. It binds to NXF1 and serves as receptor for the RNA export element RTE. It also possesses mRNA export activity and can facilitate the access of DEAD-box protein DBP5 to mRNA at the nuclear pore complex (NPC). RBM15 belongs to the Spen (split end) protein family, which contains three N-terminal RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain. This family also includes a RBM15-MKL1 (OTT-MAL) fusion protein that RBM15 is N-terminally fused to megakaryoblastic leukemia 1 protein (MKL1) at the C-terminus in a translocation involving chromosome 1 and 22, resulting in acute megakaryoblastic leukemia. The fusion protein could interact with the mRNA export machinery. Although it maintains the specific transactivator function of MKL1, the fusion protein cannot activate RTE-mediated mRNA expression and has lost the post-transcriptional activator function of RBM15. However, it has transdominant suppressor function contributing to its oncogenic properties
YKTLKISELGSQLSDEAVEDGLFHEFKKFGDVSVKISRLGDERVAFVNFRRPEDARAAKHARGRLVLYDR
PLKIEAVY
>gnl|CDD|409970 cd12554, RRM1_RBM15B, RNA recognition motif 1 (RRM1) found in putative RNA binding motif protein 15B (RBM15B) from vertebrate. This subfamily corresponds to the RRM1 of RBM15B, also termed one twenty-two 3 (OTT3), a paralog of RNA binding motif protein 15 (RBM15), also known as One-twenty two protein 1 (OTT1). Like RBM15, RBM15B has post-transcriptional regulatory activity. It is a nuclear protein sharing with RBM15 the association with the splicing factor compartment and the nuclear envelope as well as the binding to mRNA export factors NXF1 and Aly/REF. RBM15B belongs to the Spen (split end) protein family, which shares a domain architecture comprising of three N-terminal RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain
EYKTLLVSNLGSQLPDELLEDGLFHEFKKFGEVSVKLSHTPELGRVAYVNFRHPEDAKEARHAKGRLVLY
DRPLKVEPVY
>gnl|CDD|409971 cd12555, RRM2_RBM15, RNA recognition motif 2 (RRM2) found in vertebrate RNA binding motif protein 15 (RBM15). This subgroup corresponds to the RRM2 of RBM15, also termed one-twenty two protein 1 (OTT1), conserved in eukaryotes, a novel mRNA export factor and component of the NXF1 pathway. It binds to NXF1 and serves as receptor for the RNA export element RTE. It also possesses mRNA export activity and can facilitate the access of DEAD-box protein DBP5 to mRNA at the nuclear pore complex (NPC). RBM15 belongs to the Spen (split end) protein family, which contain three N-terminal RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain. This family also includes a RBM15-MKL1 (OTT-MAL) fusion protein that RBM15 is N-terminally fused to megakaryoblastic leukemia 1 protein (MKL1) at the C-terminus in a translocation involving chromosome 1 and 22, resulting in acute megakaryoblastic leukemia. The fusion protein could interact with the mRNA export machinery. Although it maintains the specific transactivator function of MKL1, the fusion protein cannot activate RTE-mediated mRNA expression and has lost the post-transcriptional activator function of RBM15. However, it has transdominant suppressor function contributing to its oncogenic properties
EDDQRANRTLFLGNLDITVTENDLRRAFDRFGVITEVDIKRPGRGQTSTYGFLKFENLDMAHRAKLAMSG
KVIGRNPIKIGYGKATP
>gnl|CDD|409972 cd12556, RRM2_RBM15B, RNA recognition motif 2 (RRM2) found in putative RNA binding motif protein 15B (RBM15B) from vertebrate. This subgroup corresponds to the RRM2 of RBM15B, also termed one twenty-two 3 (OTT3), a paralog of RNA binding motif protein 15 (RBM15), also known as One-twenty two protein 1 (OTT1). Like RBM15, RBM15B has post-transcriptional regulatory activity. It is a nuclear protein sharing with RBM15 the association with the splicing factor compartment and the nuclear envelope as well as the binding to mRNA export factors NXF1 and Aly/REF. RBM15B belongs to the Spen (split end) protein family, which shares a domain architecture comprising of three N-terminal RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain
PEDDQRATRNLFIGNLDHNVSEVELRRAFEKYGIIEEVVIKRPARGQGGAYAFLKFQNLDMAHRAKVAMS
GRVIGRNPIKIGYGK
>gnl|CDD|409973 cd12557, RRM3_RBM15, RNA recognition motif 3 (RRM3) found in vertebrate RNA binding motif protein 15 (RBM15). This subgroup corresponds to the RRM3 of RBM15, also termed one-twenty two protein 1 (OTT1), conserved in eukaryotes, a novel mRNA export factor component of the NXF1 pathway. It binds to NXF1 and serves as receptor for the RNA export element RTE. It also possesses mRNA export activity and can facilitate the access of DEAD-box protein DBP5 to mRNA at the nuclear pore complex (NPC). RBM15 belongs to the Spen (split end) protein family, which contains three N-terminal RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal SPOC (Spen paralogue and ortholog C-terminal) domain. This family also includes a RBM15-MKL1 (OTT-MAL) fusion protein that RBM15 is N-terminally fused to megakaryoblastic leukemia 1 protein (MKL1) at the C-terminus in a translocation involving chromosome 1 and 22, resulting in acute megakaryoblastic leukemia. The fusion protein could interact with the mRNA export machinery. Although it maintains the specific transactivator function of MKL1, the fusion protein cannot activate RTE-mediated mRNA expression and has lost the post-transcriptional activator function of RBM15. However, it has transdominant suppressor function contributing to its oncogenic properties
RLWVGGLGPWVPLAALAREFDRFGTIRTIDYRKGDSWAYIQYESLDAAQAACTHMRGFPLGGPDRRLRVD
FAD
>gnl|CDD|409974 cd12558, RRM3_RBM15B, RNA recognition motif 3 (RRM3) found in putative RNA-binding protein 15B (RBM15B) from vertebrate. This subgroup corresponds to the RRM3 of RBM15B, also termed one twenty-two 3 (OTT3), a paralog of RNA binding motif protein 15 (RBM15), also known as One-twenty two protein 1 (OTT1). Like RBM15, RBM15B has post-transcriptional regulatory activity. It is a nuclear protein sharing with RBM15 the association with the splicing factor compartment and the nuclear envelope as well as the binding to mRNA export factors NXF1 and Aly/REF. RBM15B belongs to the Spen (split end) protein family, which shares a domain architecture comprising of three N-terminal RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain
PTTRLWVGGLGPNTSLAALAREFDRFGSIRTIDYVKGDSFAYIQYESLDAAQAACAQMRGFPLGGPDRRL
RVDFAK
>gnl|CDD|409975 cd12559, RRM_SRSF10, RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 10 (SRSF10) and similar proteins. This subgroup corresponds to the RRM of SRSF10, also termed 40 kDa SR-repressor protein (SRrp40), or FUS-interacting serine-arginine-rich protein 1 (FUSIP1), or splicing factor SRp38, or splicing factor, arginine/serine-rich 13A (SFRS13A), or TLS-associated protein with Ser-Arg repeats (TASR). SRSF10 is a serine-arginine (SR) protein that acts as a potent and general splicing repressor when dephosphorylated. It mediates global inhibition of splicing both in M phase of the cell cycle and in response to heat shock. SRSF10 emerges as a modulator of cholesterol homeostasis through the regulation of low-density lipoprotein receptor (LDLR) splicing efficiency. It also regulates cardiac-specific alternative splicing of triadin pre-mRNA and is required for proper Ca2+ handling during embryonic heart development. In contrast, the phosphorylated SRSF10 functions as a sequence-specific splicing activator in the presence of a nuclear cofactor. It activates distal alternative 5' splice site of adenovirus E1A pre-mRNA in vivo. Moreover, SRSF10 strengthens pre-mRNA recognition by U1 and U2 snRNPs. SRSF10 localizes to the nuclear speckles and can shuttle between nucleus and cytoplasm. It contains a single N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C-terminal RS domain rich in serine-arginine dipeptides
LRPPNTSLFVRNVADDTRSEDLRREFGRYGPIVDVYVPLDFYTRRPRGFAYVQFEDVRDAEDALHNLDRK
WICGRQIEIQFAQGDRKTPNQMKAK
>gnl|CDD|409976 cd12560, RRM_SRSF12, RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 12 (SRSF12) and similar proteins. This subgroup corresponds to the RRM of SRSF12, also termed 35 kDa SR repressor protein (SRrp35), or splicing factor, arginine/serine-rich 13B (SFRS13B), or splicing factor, arginine/serine-rich 19 (SFRS19). SRSF12 is a serine/arginine (SR) protein-like alternative splicing regulator that antagonizes authentic SR proteins in the modulation of alternative 5' splice site choice. For instance, it activates distal alternative 5' splice site of the adenovirus E1A pre-mRNA in vivo. SRSF12 contains a single N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C-terminal RS domain rich in serine-arginine dipeptides
TSLFVRNVADATRPEDLRREFGRYGPIVDVYIPLDFYNRRPRGFAYIQFEDVRDAEDALYNLNRKWVCGR
QIEIQFAQGDRKTP
>gnl|CDD|409977 cd12561, RRM1_RBM5_like, RNA recognition motif 1 (RRM1) found in RNA-binding protein 5 (RBM5) and similar proteins. This subgroup corresponds to the RRM1 of RNA-binding protein 5 (RBM5 or LUCA15 or H37), RNA-binding protein 10 (RBM10 or S1-1) and similar proteins. RBM5 is a known modulator of apoptosis. It may also act as a tumor suppressor or an RNA splicing factor; it specifically binds poly(G) RNA. RBM10, a paralog of RBM5, may play an important role in mRNA generation, processing and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. Both, RBM5 and RBM10, contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, and a G-patch/D111 domain
PNNTIMLRGLPLSVTEEDIRNALVSHGVQPKDVRLMRRKTTGASRGFAFVEFMSLEEATRWMEANQGKLQ
LQGYKITLHYS
>gnl|CDD|409978 cd12562, RRM2_RBM5_like, RNA recognition motif 2 (RRM2) found in RNA-binding protein 5 (RBM5) and similar proteins. This subgroup corresponds to the RRM2 of RNA-binding protein 5 (RBM5 or LUCA15 or H37), RNA-binding protein 10 (RBM10 or S1-1) and similar proteins. RBM5 is a known modulator of apoptosis. It may also act as a tumor suppressor or an RNA splicing factor; it specifically binds poly(G) RNA. RBM10, a paralog of RBM5, may play an important role in mRNA generation, processing and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. Both, RBM5 and RBM10, contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, and a G-patch/D111 domain
ANDTIILRNINPHTTVDSILGALAPYAVLSSSNVRLIKDKQTQLNRGFAFVQLSSPIEASQLLQILQSLH
PPLTIDGKTINVDFAK
>gnl|CDD|409979 cd12563, RRM2_RBM6, RNA recognition motif 2 (RRM2) found in vertebrate RNA-binding protein 6 (RBM6). This subgroup corresponds to the RRM2 of RBM6, also termed lung cancer antigen NY-LU-12, or protein G16, or RNA-binding protein DEF-3, which has been predicted to be a nuclear factor based on its nuclear localization signal. It shows high sequence similarity to RNA-binding protein 5 (RBM5 or LUCA15 or NY-REN-9). Both, RBM6 and RBM5, specifically bind poly(G) RNA. They contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, a nuclear localization signal, and a G-patch/D111 domain. In contrast to RBM5, RBM6 has two additional unique domains: the decamer repeat occurring more than 20 times, and the POZ (poxvirus and zinc finger) domain. The POZ domain may be involved in protein-protein interactions and inhibit binding of target sequences by zinc fingers
DSKTIMLKRIYRSTPPEVIVEVLEPYVRLTTANVRIIKNKTGPMGHTYGFIDLDSHAEALRLVKLLQNLD
PPLYIDGRRVYVNVATG
>gnl|CDD|409980 cd12564, RRM1_RBM19, RNA recognition motif 1 (RRM1) found in RNA-binding protein 19 (RBM19) and similar proteins. This subgroup corresponds to the RRM1 of RBM19, also termed RNA-binding domain-1 (RBD-1), a nucleolar protein conserved in eukaryotes. It is involved in ribosome biogenesis by processing rRNA. In addition, it is essential for preimplantation development. RBM19 has a unique domain organization containing 6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
SRLIVKNLPSSITEDRLRKLFSAFGTITDVQLKYTKDGKFRRFGFVGFKSEEEAQKALKHFNNSFIDTSR
ITVEEC
>gnl|CDD|409981 cd12565, RRM1_MRD1, RNA recognition motif 1 (RRM1) found in yeast multiple RNA-binding domain-containing protein 1 (MRD1) and similar proteins. This subgroup corresponds to the RRM1 of MRD1 which is encoded by a novel yeast gene MRD1 (multiple RNA-binding domain). It is well-conserved in yeast and its homologs exist in all eukaryotes. MRD1 is present in the nucleolus and the nucleoplasm. It interacts with the 35 S precursor rRNA (pre-rRNA) and U3 small nucleolar RNAs (snoRNAs). MRD1 is essential for the initial processing at the A0-A2 cleavage sites in the 35 S pre-rRNA. It contains 5 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which may play an important structural role in organizing specific rRNA processing events
SRIIVKNLPKYVTEKRLKEHFSKKGEITDVKVMRTKDGKSRRFGFIGFKSEEEAQKAVKYFNKTFIDTSK
ISVEFA
>gnl|CDD|409982 cd12566, RRM2_MRD1, RNA recognition motif 2 (RRM2) found in yeast multiple RNA-binding domain-containing protein 1 (MRD1) and similar proteins. This subgroup corresponds to the RRM2 of MRD1 which is encoded by a novel yeast gene MRD1 (multiple RNA-binding domain). It is well-conserved in yeast and its homologs exist in all eukaryotes. MRD1 is present in the nucleolus and the nucleoplasm. It interacts with the 35 S precursor rRNA (pre-rRNA) and U3 small nucleolar RNAs (snoRNAs). It is essential for the initial processing at the A0-A2 cleavage sites in the 35 S pre-rRNA. MRD1 contains 5 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which may play an important structural role in organizing specific rRNA processing events
ETGRLFLRNLPYSTKEDDLQKLFSKFGEVSEVHVPIDKKTKKSKGFAYVLFLDPEDAVQAYNELDGKVFQ
GRLIHILPG
>gnl|CDD|409983 cd12567, RRM3_RBM19, RNA recognition motif 3 (RRM3) found in RNA-binding protein 19 (RBM19) and similar proteins. This subgroup corresponds to the RRM3 of RBM19, also termed RNA-binding domain-1 (RBD-1), which is a nucleolar protein conserved in eukaryotes. It is involved in ribosome biogenesis by processing rRNA. In addition, it is essential for preimplantation development. RBM19 has a unique domain organization containing 6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
ESGRLFVRNLPYTCTEEDLEKLFSKYGPLSEVHFPIDSLTKKPKGFAFVTYMIPEHAVKAYAELDGTVFQ
GRLLHLLPS
>gnl|CDD|241012 cd12568, RRM3_MRD1, RNA recognition motif 3 (RRM3) found in yeast multiple RNA-binding domain-containing protein 1 (MRD1) and similar proteins. This subgroup corresponds to the RRM3 of MRD1 which is encoded by a novel yeast gene MRD1 (multiple RNA-binding domain). It is well-conserved in yeast and its homologs exist in all eukaryotes. MRD1 is present in the nucleolus and the nucleoplasm. It interacts with the 35 S precursor rRNA (pre-rRNA) and U3 small nucleolar RNAs (snoRNAs). MRD1 is essential for the initial processing at the A0-A2 cleavage sites in the 35 S pre-rRNA. It contains 5 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which may play an important structural role in organizing specific rRNA processing events
TTILVKNFPYGTTAEELRDLFEPHGKLTRVLMPPAGTIAIVEFANPQQARLAFKALAYRRFKDSILYLEK
GP
>gnl|CDD|409984 cd12569, RRM4_RBM19, RNA recognition motif 4 (RRM4) found in RNA-binding protein 19 (RBM19) and similar proteins. This subgroup corresponds to the RRM4 of RBM19, also termed RNA-binding domain-1 (RBD-1), which is a nucleolar protein conserved in eukaryotes. It is involved in ribosome biogenesis by processing rRNA. In addition, it is essential for preimplantation development. RBM19 has a unique domain organization containing 6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
TVILVKNLPAGTEVAELEELFSKFGSLGRVVLPPAGVTAIVEFLEPTEAKRAFTKLAYSKFQHVPLYLEW
AP
>gnl|CDD|241014 cd12570, RRM5_MRD1, RNA recognition motif 5 (RRM5) found in yeast multiple RNA-binding domain-containing protein 1 (MRD1) and similar proteins. This subgroup corresponds to the RRM5 of MRD1 which is encoded by a novel yeast gene MRD1 (multiple RNA-binding domain). It is well-conserved in yeast and its homologs exist in all eukaryotes. MRD1 is present in the nucleolus and the nucleoplasm. It interacts with the 35 S precursor rRNA (pre-rRNA) and U3 small nucleolar RNAs (snoRNAs). MRD1 is essential for the initial processing at the A0-A2 cleavage sites in the 35 S pre-rRNA. It contains 5 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which may play an important structural role in organizing specific rRNA processing events
TKILVKNLPFEATKKDVRTLFSSYGQLKSVRVPKKFDQSARGFAFVEFSTAKEALNAMNALKDTHLLGRR
LVLQYA
>gnl|CDD|409985 cd12571, RRM6_RBM19, RNA recognition motif 6 (RRM6) found in RNA-binding protein 19 (RBM19) and similar proteins. This subgroup corresponds to the RRM6 of RBM19, also termed RNA-binding domain-1 (RBD-1), which is a nucleolar protein conserved in eukaryotes. It is involved in ribosome biogenesis by processing rRNA. In addition, it is essential for preimplantation development. RBM19 has a unique domain organization containing 6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
SKILVRNIPFQATVKEVRELFSTFGELKTVRLPKKMGGTGQHRGFGFVDFITKQDAKRAFDALCHSTHLY
GRRLVLEWA
>gnl|CDD|409986 cd12572, RRM2_MSI1, RNA recognition motif 2 (RRM2) found in RNA-binding protein Musashi homolog 1 (Musashi-1) and similar proteins. This subgroup corresponds to the RRM2 of Musashi-1. The mammalian MSI1 gene encoding Musashi-1 (also termed Msi1) is a neural RNA-binding protein putatively expressed in central nervous system (CNS) stem cells and neural progenitor cells, and associated with asymmetric divisions in neural progenitor cells. Musashi-1 is evolutionarily conserved from invertebrates to vertebrates. It is a homolog of Drosophila Musashi and Xenopus laevis nervous system-specific RNP protein-1 (Nrp-1) and has been implicated in the maintenance of the stem-cell state, differentiation, and tumorigenesis. It translationally regulates the expression of a mammalian numb gene by binding to the 3'-untranslated region of mRNA of Numb, encoding a membrane-associated inhibitor of Notch signaling, and further influences neural development. It represses translation by interacting with the poly(A)-binding protein and competes for binding of the eukaryotic initiation factor-4G (eIF-4G). Musashi-1 contains two conserved N-terminal tandem RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), along with other domains of unknown function
KIFVGGLSVNTTVEDVKQYFEQFGKVDDAMLMFDKTTNRHRGFGFVTFESEDIVEKVCEIHFHEINNKMV
ECKK
>gnl|CDD|409987 cd12573, RRM2_MSI2, RNA recognition motif 2 (RRM2) found in RNA-binding protein Musashi homolog 2 (Musashi-2) and similar proteins. This subgroup corresponds to the RRM2 of Musashi-2 (also termed Msi2) which has been identified as a regulator of the hematopoietic stem cell (HSC) compartment and of leukemic stem cells after transplantation of cells with loss and gain of function of the gene. It influences proliferation and differentiation of HSCs and myeloid progenitors, and further modulates normal hematopoiesis and promotes aggressive myeloid leukemia. Musashi-2 contains two conserved N-terminal tandem RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), along with other domains of unknown function
KKIFVGGLSANTVVEDVKQYFEQFGKVEDAMLMFDKTTNRHRGFGFVTFENEDVVEKVCEIHFHEINNKM
VECKKA
>gnl|CDD|409988 cd12574, RRM1_DAZAP1, RNA recognition motif 1 (RRM1) found in Deleted in azoospermia-associated protein 1 (DAZAP1) and similar proteins. This subfamily corresponds to the RRM1 of DAZAP1 or DAZ-associated protein 1, also termed proline-rich RNA binding protein (Prrp), a multi-functional ubiquitous RNA-binding protein expressed most abundantly in the testis and essential for normal cell growth, development, and spermatogenesis. DAZAP1 is a shuttling protein whose acetylated form is predominantly nuclear and the nonacetylated form is in cytoplasm. It also functions as a translational regulator that activates translation in an mRNA-specific manner. DAZAP1 was initially identified as a binding partner of Deleted in Azoospermia (DAZ). It also interacts with numerous hnRNPs, including hnRNP U, hnRNP U like-1, hnRNPA1, hnRNPA/B, and hnRNP D, suggesting DAZAP1 might associate and cooperate with hnRNP particles to regulate adenylate-uridylate-rich elements (AU-rich element or ARE)-containing mRNAs. DAZAP1 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal proline-rich domain
KLFVGGLDWSTTQETLRSYFSQYGEVVDCVIMKDKTTNQSRGFGFVKFKDPNCVGTVLASRPHNLDGRNI
DPKPCTPRGMQP
>gnl|CDD|409989 cd12575, RRM1_hnRNPD_like, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein hnRNP D0, hnRNP A/B, hnRNP DL and similar proteins. This subfamily corresponds to the RRM1 in hnRNP D0, hnRNP A/B, hnRNP DL and similar proteins. hnRNP D0 is a UUAG-specific nuclear RNA binding protein that may be involved in pre-mRNA splicing and telomere elongation. hnRNP A/B is an RNA unwinding protein with a high affinity for G- followed by U-rich regions. hnRNP A/B has also been identified as an APOBEC1-binding protein that interacts with apolipoprotein B (apoB) mRNA transcripts around the editing site and thus plays an important role in apoB mRNA editing. hnRNP DL (or hnRNP D-like) is a dual functional protein that possesses DNA- and RNA-binding properties. It has been implicated in mRNA biogenesis at the transcriptional and post-transcriptional levels. All members in this family contain two putative RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a glycine- and tyrosine-rich C-terminus
MFIGGLSWDTSKKDLKDYFSKFGEVVDCTIKLDPVTGRSRGFGFVLFKDAESVDKVLDQKEHKLDGKVID
PK
>gnl|CDD|409990 cd12576, RRM1_MSI, RNA recognition motif 1 (RRM1) found in RNA-binding protein Musashi homolog Musashi-1, Musashi-2 and similar proteins. This subfamily corresponds to the RRM1 in Musashi-1 and Musashi-2. Musashi-1 (also termed Msi1) is a neural RNA-binding protein putatively expressed in central nervous system (CNS) stem cells and neural progenitor cells, and associated with asymmetric divisions in neural progenitor cells. It is evolutionarily conserved from invertebrates to vertebrates. Musashi-1 is a homolog of Drosophila Musashi and Xenopus laevis nervous system-specific RNP protein-1 (Nrp-1). It has been implicated in the maintenance of the stem-cell state, differentiation, and tumorigenesis. It translationally regulates the expression of a mammalian numb gene by binding to the 3'-untranslated region of mRNA of Numb, encoding a membrane-associated inhibitor of Notch signaling, and further influences neural development. Moreover, Musashi-1 represses translation by interacting with the poly(A)-binding protein and competes for binding of the eukaryotic initiation factor-4G (eIF-4G). Musashi-2 (also termed Msi2) has been identified as a regulator of the hematopoietic stem cell (HSC) compartment and of leukemic stem cells after transplantation of cells with loss and gain of function of the gene. It influences proliferation and differentiation of HSCs and myeloid progenitors, and further modulates normal hematopoiesis and promotes aggressive myeloid leukemia. Both, Musashi-1 and Musashi-2, contain two conserved N-terminal tandem RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), along with other domains of unknown function
KMFIGGLSWQTTPEGLREYFSKFGEITECMVMRDPTTKRSRGFGFVTFSDPASVDKVLAQGPHELDGKKI
DPKVAF
>gnl|CDD|409991 cd12577, RRM1_Hrp1p, RNA recognition motif 1 (RRM1) found in yeast nuclear polyadenylated RNA-binding protein 4 (Hrp1p or Nab4p) and similar proteins. This subfamily corresponds to the RRM1 of Hrp1p and similar proteins. Hrp1p or Nab4p, also termed cleavage factor IB (CFIB), is a sequence-specific trans-acting factor that is essential for mRNA 3'-end formation in yeast Saccharomyces cerevisiae. It can be UV cross-linked to RNA and specifically recognizes the (UA)6 RNA element required for both, the cleavage and poly(A) addition, steps. Moreover, Hrp1p can shuttle between the nucleus and the cytoplasm, and play an additional role in the export of mRNAs to the cytoplasm. Hrp1p also interacts with Rna15p and Rna14p, two components of CF1A. In addition, Hrp1p functions as a factor directly involved in modulating the activity of the nonsense-mediated mRNA decay (NMD) pathway. It binds specifically to a downstream sequence element (DSE)-containing RNA and interacts with Upf1p, a component of the surveillance complex, further triggering the NMD pathway. Hrp1p contains two central RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and an arginine-glycine-rich region harboring repeats of the sequence RGGF/Y
MFIGGLNWDTTEEGLRDYFSQFGTVVDCTIMKDSATGRSRGFGFLTFEDPSSVNEVMKKEHVLDGKIIDP
KRAIPR
>gnl|CDD|409992 cd12578, RRM1_hnRNPA_like, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein A subfamily. This subfamily corresponds to the RRM1 in hnRNP A0, hnRNP A1, hnRNP A2/B1, hnRNP A3 and similar proteins. hnRNP A0 is a low abundance hnRNP protein that has been implicated in mRNA stability in mammalian cells. It has been identified as the substrate for MAPKAP-K2 and may be involved in the lipopolysaccharide (LPS)-induced post-transcriptional regulation of tumor necrosis factor-alpha (TNF-alpha), cyclooxygenase 2 (COX-2) and macrophage inflammatory protein 2 (MIP-2). hnRNP A1 is an abundant eukaryotic nuclear RNA-binding protein that may modulate splice site selection in pre-mRNA splicing. hnRNP A2/B1 is an RNA trafficking response element-binding protein that interacts with the hnRNP A2 response element (A2RE). Many mRNAs, such as myelin basic protein (MBP), myelin-associated oligodendrocytic basic protein (MOBP), carboxyanhydrase II (CAII), microtubule-associated protein tau, and amyloid precursor protein (APP) are trafficked by hnRNP A2/B1. hnRNP A3 is also a RNA trafficking response element-binding protein that participates in the trafficking of A2RE-containing RNA. The hnRNP A subfamily is characterized by two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a long glycine-rich region at the C-terminus
KLFIGGLSYETTDDSLRNHFEQWGEITDVVVMKDPATKRSRGFGFVTYSSASEVDAAMNARPHKVDGRVV
EPKRAVPR
>gnl|CDD|409993 cd12579, RRM2_hnRNPA0, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein A0 (hnRNP A0) and similar proteins. This subgroup corresponds to the RRM2 of hnRNP A0, a low abundance hnRNP protein that has been implicated in mRNA stability in mammalian cells. It has been identified as the substrate for MAPKAP-K2 and may be involved in the lipopolysaccharide (LPS)-induced post-transcriptional regulation of tumor necrosis factor-alpha (TNF-alpha), cyclooxygenase 2 (COX-2) and macrophage inflammatory protein 2 (MIP-2). hnRNP A0 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a long glycine-rich region at the C-terminus
KLFVGGLKGDVGEGDLVEHFSQFGTVEKVEVIADKDTGKKRGFGFVYFEDHDSADKAAVVKFHSINGHRV
EVKKAVPKEE
>gnl|CDD|409994 cd12580, RRM2_hnRNPA1, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) and similar proteins. This subgroup corresponds to the RRM2 of hnRNP A1, also termed helix-destabilizing protein, or single-strand RNA-binding protein, or hnRNP core protein A1, an abundant eukaryotic nuclear RNA-binding protein that may modulate splice site selection in pre-mRNA splicing. hnRNP A1 has been characterized as a splicing silencer, often acting in opposition to an activating hnRNP H. It silences exons when bound to exonic elements in the alternatively spliced transcripts of c-src, HIV, GRIN1, and beta-tropomyosin. hnRNP A1 can shuttle between the nucleus and the cytoplasm. Thus, it may be involved in transport of cellular RNAs, including the packaging of pre-mRNA into hnRNP particles and transport of poly A+ mRNA from the nucleus to the cytoplasm. The cytoplasmic hnRNP A1 has high affinity with AU-rich elements, whereas the nuclear hnRNP A1 has high affinity with a polypyrimidine stretch bordered by AG at the 3' ends of introns. hnRNP A1 is also involved in the replication of an RNA virus, such as mouse hepatitis virus (MHV), through an interaction with the transcription-regulatory region of viral RNA. Moreover, hnRNP A1, together with the scaffold protein septin 6, serves as host proteins to form a complex with NS5b and viral RNA, and further play important roles in the replication of Hepatitis C virus (HCV). hnRNP A1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a long glycine-rich region at the C-terminus. The RRMs of hnRNP A1 play an important role in silencing the exon and the glycine-rich domain is responsible for protein-protein interactions
KKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHN
CEVRKAL
>gnl|CDD|409995 cd12581, RRM2_hnRNPA2B1, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP A2/B1) and similar proteins. This subgroup corresponds to the RRM2 of hnRNP A2/B1, an RNA trafficking response element-binding protein that interacts with the hnRNP A2 response element (A2RE). Many mRNAs, such as myelin basic protein (MBP), myelin-associated oligodendrocytic basic protein (MOBP), carboxyanhydrase II (CAII), microtubule-associated protein tau, and amyloid precursor protein (APP) are trafficked by hnRNP A2/B1. hnRNP A2/B1 also functions as a splicing factor that regulates alternative splicing of the tumor suppressors, such as BIN1, WWOX, the antiapoptotic proteins c-FLIP and caspase-9B, the insulin receptor (IR), and the RON proto-oncogene among others. Overexpression of hnRNP A2/B1 has been described in many cancers. It functions as a nuclear matrix protein involving in RNA synthesis and the regulation of cellular migration through alternatively splicing pre-mRNA. It may play a role in tumor cell differentiation. hnRNP A2/B1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a long glycine-rich region at the C-terminus
KKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHN
AEVRKALSRQ
>gnl|CDD|409996 cd12582, RRM2_hnRNPA3, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein A3 (hnRNP A3) and similar proteins. This subgroup corresponds to the RRM2 of hnRNP A3, a novel RNA trafficking response element-binding protein that interacts with the hnRNP A2 response element (A2RE) independently of hnRNP A2 and participates in the trafficking of A2RE-containing RNA. hnRNP A3 can shuttle between the nucleus and the cytoplasm. It contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a long glycine-rich region at the C-terminus
KKIFVGGIKEDTEEYHLRDYFEKYGKIETIEVMEDRQSGKKRGFAFVTFDDHDTVDKIVVQKYHTINGHN
CEVKKALSKQ
>gnl|CDD|241027 cd12583, RRM2_hnRNPD, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) and similar proteins. This subgroup corresponds to the RRM2 of hnRNP D0, also termed AU-rich element RNA-binding protein 1, a UUAG-specific nuclear RNA binding protein that may be involved in pre-mRNA splicing and telomere elongation. hnRNP D0 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), in the middle and an RGG box rich in glycine and arginine residues in the C-terminal part. Each of RRMs can bind solely to the UUAG sequence specifically
KIFVGGLSPDTPEEKIREYFGAFGEVESIELPMDNKTNKRRGFCFITFKEEEPVKKIMEKKYHNVGLSKC
EIKVA
>gnl|CDD|409997 cd12584, RRM2_hnRNPAB, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein A/B (hnRNP A/B) and similar proteins. This subgroup corresponds to the RRM2 of hnRNP A/B, also termed APOBEC1-binding protein 1 (ABBP-1), an RNA unwinding protein with a high affinity for G- followed by U-rich regions. hnRNP A/B has also been identified as an APOBEC1-binding protein that interacts with apolipoprotein B (apoB) mRNA transcripts around the editing site and thus plays an important role in apoB mRNA editing. hnRNP A/B contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a long C-terminal glycine-rich domain that contains a potential ATP/GTP binding loop
KDPVKKIFVGGLNPETTEEKIREYFGEFGEIEAIELPMDPKTNKRRGFVFITFKEEDPVKKILEKKFHNV
SGSKCEIKIA
>gnl|CDD|409998 cd12585, RRM2_hnRPDL, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein D-like (hnRNP DL) and similar proteins. This subgroup corresponds to the RRM2 of hnRNP DL (or hnRNP D-like), also termed AU-rich element RNA-binding factor, or JKT41-binding protein (protein laAUF1 or JKTBP), is a dual functional protein that possesses DNA- and RNA-binding properties. It has been implicated in mRNA biogenesis at the transcriptional and post-transcriptional levels. hnRNP DL binds single-stranded DNA (ssDNA) or double-stranded DNA (dsDNA) in a non-sequencespecific manner, and interacts with poly(G) and poly(A) tenaciously. It contains two putative two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a glycine- and tyrosine-rich C-terminus
KVFVGGLSPDTSEEQIKEYFGAFGEIENIELPMDTKTNERRGFCFITYTDEEPVQKLLESRYHQIGSGKC
EIKVA
>gnl|CDD|409999 cd12586, RRM1_PSP1, RNA recognition motif 1 (RRM1) found in vertebrate paraspeckle protein 1 (PSP1). This subgroup corresponds to the RRM1 of PSPC1, also termed paraspeckle component 1 (PSPC1), a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm. It is ubiquitously expressed and highly conserved in vertebrates. Its cellular function remains unknown currently, however, PSPC1 forms a novel heterodimer with the nuclear protein p54nrb, also known as non-POU domain-containing octamer-binding protein (NonO), which localizes to paraspeckles in an RNA-dependent manner. PSPC1 contains two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), at the N-terminus
RCRLFVGNLPTDITEEDFKRLFERYGEPSEVFINRDRGFGFIRLESRTLAEIAKAELDGTILKSRPLRIR
F
>gnl|CDD|410000 cd12587, RRM1_PSF, RNA recognition motif 1 (RRM1) found in vertebrate polypyrimidine tract-binding protein (PTB)-associated-splicing factor (PSF). This subgroup corresponds to the RRM1 of PSF, also termed proline- and glutamine-rich splicing factor, or 100 kDa DNA-pairing protein (POMp100), or 100 kDa subunit of DNA-binding p52/p100 complex, a multifunctional protein that mediates diverse activities in the cell. It is ubiquitously expressed and highly conserved in vertebrates. PSF binds not only RNA but also both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) and facilitates the renaturation of complementary ssDNAs. Besides, it promotes the formation of D-loops in superhelical duplex DNA, and is involved in cell proliferation. PSF can also interact with multiple factors. It is an RNA-binding component of spliceosomes and binds to insulin-like growth factor response element (IGFRE). PSF functions as a transcriptional repressor interacting with Sin3A and mediating silencing through the recruitment of histone deacetylases (HDACs) to the DNA binding domain (DBD) of nuclear hormone receptors. Additionally, PSF is an essential pre-mRNA splicing factor and is dissociated from PTB and binds to U1-70K and serine-arginine (SR) proteins during apoptosis. PSF forms a heterodimer with the nuclear protein p54nrb, also known as non-POU domain-containing octamer-binding protein (NonO). The PSF/p54nrb complex displays a variety of functions, such as DNA recombination and RNA synthesis, processing, and transport. PSF contains two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which are responsible for interactions with RNA and for the localization of the protein in speckles. It also contains an N-terminal region rich in proline, glycine, and glutamine residues, which may play a role in interactions recruiting other molecules
RCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVR
F
>gnl|CDD|410001 cd12588, RRM1_p54nrb, RNA recognition motif 1 (RRM1) found in vertebrate 54 kDa nuclear RNA- and DNA-binding protein (p54nrb). This subgroup corresponds to the RRM1 of p54nrb, also termed non-POU domain-containing octamer-binding protein (NonO), or 55 kDa nuclear protein (NMT55), or DNA-binding p52/p100 complex 52 kDa subunit. p54nrb is a multifunctional protein involved in numerous nuclear processes including transcriptional regulation, splicing, DNA unwinding, nuclear retention of hyperedited double-stranded RNA, viral RNA processing, control of cell proliferation, and circadian rhythm maintenance. It is ubiquitously expressed and highly conserved in vertebrates. p54nrb binds both, single- and double-stranded RNA and DNA, and also possesses inherent carbonic anhydrase activity. It forms a heterodimer with paraspeckle component 1 (PSPC1 or PSP1), localizing to paraspeckles in an RNA-dependent manneras well as with polypyrimidine tract-binding protein-associated-splicing factor (PSF). p54nrb contains two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), at the N-terminus
RSRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRVR
F
>gnl|CDD|410002 cd12589, RRM2_PSP1, RNA recognition motif 2 (RRM2) found in vertebrate paraspeckle protein 1 (PSP1 or PSPC1). This subgroup corresponds to the RRM2 of PSPC1, also termed paraspeckle component 1 (PSPC1), a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm. It is ubiquitously expressed and highly conserved in vertebrates. Although its cellular function remains unknown currently, PSPC1 forms a novel heterodimer with the nuclear protein p54nrb, also known as non-POU domain-containing octamer-binding protein (NonO), which localizes to paraspeckles in an RNA-dependent manner. PSPC1 contains two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), at the N-terminus
ALTVKNLSPVVSNELLEQAFSQFGPVERAVVIVDDRGRPTGKGFVEFAAKPPARKALERCSDGAFLLTTT
PRPVIVEPME
>gnl|CDD|410003 cd12590, RRM2_PSF, RNA recognition motif 2 (RRM2) found in vertebrate polypyrimidine tract-binding protein (PTB)-associated-splicing factor (PSF). This subgroup corresponds to the RRM2 of PSF, also termed proline- and glutamine-rich splicing factor, or 100 kDa DNA-pairing protein (POMp100), or 100 kDa subunit of DNA-binding p52/p100 complex, a multifunctional protein that mediates diverse activities in the cell. It is ubiquitously expressed and highly conserved in vertebrates. PSF binds not only RNA but also both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) and facilitates the renaturation of complementary ssDNAs. It promotes the formation of D-loops in superhelical duplex DNA, and is involved in cell proliferation. PSF can also interact with multiple factors. It is an RNA-binding component of spliceosomes and binds to insulin-like growth factor response element (IGFRE). Moreover, PSF functions as a transcriptional repressor interacting with Sin3A and mediating silencing through the recruitment of histone deacetylases (HDACs) to the DNA binding domain (DBD) of nuclear hormone receptors. PSF is an essential pre-mRNA splicing factor and is dissociated from PTB and binds to U1-70K and serine-arginine (SR) proteins during apoptosis. PSF forms a heterodimer with the nuclear protein p54nrb, also known as non-POU domain-containing octamer-binding protein (NonO). The PSF/p54nrb complex displays a variety of functions, such as DNA recombination and RNA synthesis, processing, and transport. PSF contains two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which are responsible for interactions with RNA and for the localization of the protein in speckles. It also contains an N-terminal region rich in proline, glycine, and glutamine residues, which may play a role in interactions recruiting other molecules
ALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTT
PRPVIVEPLE
>gnl|CDD|410004 cd12591, RRM2_p54nrb, RNA recognition motif 2 (RRM2) found in vertebrate 54 kDa nuclear RNA- and DNA-binding protein (p54nrb). This subgroup corresponds to the RRM2 of p54nrb, also termed non-POU domain-containing octamer-binding protein (NonO), or 55 kDa nuclear protein (NMT55), or DNA-binding p52/p100 complex 52 kDa subunit. p54nrb is a multifunctional protein involved in numerous nuclear processes including transcriptional regulation, splicing, DNA unwinding, nuclear retention of hyperedited double-stranded RNA, viral RNA processing, control of cell proliferation, and circadian rhythm maintenance. It is ubiquitously expressed and highly conserved in vertebrates. It binds both, single- and double-stranded RNA and DNA, and also possesses inherent carbonic anhydrase activity. p54nrb forms a heterodimer with paraspeckle component 1 (PSPC1 or PSP1), localizing to paraspeckles in an RNA-dependent manner. It also forms a heterodimer with polypyrimidine tract-binding protein-associated-splicing factor (PSF). p54nrb contains two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), at the N-terminus
ALTVKNLPQFVSNELLEEAFSVFGQVERAVVIVDDRGRPTGKGIVEFSGKPAARKALDRCSDGAFLLTAF
PRPVTVEPMD
>gnl|CDD|410005 cd12592, RRM_RBM7, RNA recognition motif (RRM) found in vertebrate RNA-binding protein 7 (RBM7). This subfamily corresponds to the RRM of RBM7, a ubiquitously expressed pre-mRNA splicing factor that enhances messenger RNA (mRNA) splicing in a cell-specific manner or in a certain developmental process, such as spermatogenesis. RBM7 interacts with splicing factors SAP145 (the spliceosomal splicing factor 3b subunit 2) and SRp20. It may play a more specific role in meiosis entry and progression. Together with additional testis-specific RNA-binding proteins, RBM7 may regulate the splicing of specific pre-mRNA species that are important in the meiotic cell cycle. RBM7 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a region lacking known homology at the C-terminus
DRTLFVGNLDTKVTEELLFELFLQAGPVIKVKIPKDKDGKPKQFAFVNFKHEVSVPYAMNLLNGIKLYGR
PLKIQ
>gnl|CDD|410006 cd12593, RRM_RBM11, RNA recognition motif (RRM) found in vertebrate RNA-binding protein 11 (RBM11). This subfamily corresponds to the RRM or RBM11, a novel tissue-specific splicing regulator that is selectively expressed in brain, cerebellum and testis, and to a lower extent in kidney. RBM11 is localized in the nucleoplasm and enriched in SRSF2-containing splicing speckles. It may play a role in the modulation of alternative splicing during neuron and germ cell differentiation. RBM11 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a region lacking known homology at the C-terminus. The RRM of RBM11 is responsible for RNA binding, whereas the C-terminal region permits nuclear localization and homodimerization
DRTVFVGNLHSNVNEEILYELFLQAGPLTKVTIAKDKEGKPKSFGFVCFKHAESVPYAIALLNGIRLYGR
PIKLQ
>gnl|CDD|410007 cd12594, RRM1_SRSF4, RNA recognition motif 1 (RRM1) found in vertebrate serine/arginine-rich splicing factor 4 (SRSF4). This subgroup corresponds to the RRM1 of SRSF4, also termed pre-mRNA-splicing factor SRp75, or SRP001LB, or splicing factor, arginine/serine-rich 4 (SFRS4). SRSF4 is a splicing regulatory serine/arginine (SR) protein that plays an important role in both constitutive splicing and alternative splicing of many pre-mRNAs. For instance, it interacts with heterogeneous nuclear ribonucleoproteins, hnRNP G and hnRNP E2, and further regulates the 5' splice site of tau exon 10, whose misregulation causes frontotemporal dementia. SFSF4 also induces production of HIV-1 vpr mRNA through the inhibition of the 5'-splice site of exon 3. In addition, it activates splicing of the cardiac troponin T (cTNT) alternative exon by direct interactions with the cTNT exon 5 enhancer RNA. SRSF4 can shuttle between the nucleus and cytoplasm. It contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a glycine-rich region, an internal region homologous to the RRM, and a very long, highly phosphorylated C-terminal SR domains rich in serine-arginine dipeptides
MPRVYIGRLSYQARERDVERFFKGYGKILEVDLKNGYGFVEFDDLRDADDAVYELNGKDLCGERVIVEHA
RGPRRDGSYGSGRSGYG
>gnl|CDD|410008 cd12595, RRM1_SRSF5, RNA recognition motif 1 (RRM1) found in vertebrate serine/arginine-rich splicing factor 5 (SRSF5). This subgroup corresponds to the RRM1 of SRSF5, also termed delayed-early protein HRS, or pre-mRNA-splicing factor SRp40, or splicing factor, arginine/serine-rich 5 (SFRS5). SFSF5 is an essential splicing regulatory serine/arginine (SR) protein that regulates both alternative splicing and basal splicing. It is the only SR protein efficiently selected from nuclear extracts (NE) by the splicing enhancer (ESE) and it is necessary for enhancer activation. SRSF5 also functions as a factor required for insulin-regulated splice site selection for protein kinase C (PKC) betaII mRNA. It is involved in the regulation of PKCbetaII exon inclusion by insulin via its increased phosphorylation by a phosphatidylinositol 3-kinase (PI 3-kinase) signaling pathway. Moreover, SRSF5 can regulate alternative splicing in exon 9 of glucocorticoid receptor pre-mRNA in a dose-dependent manner. SRSF5 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a C-terminal RS domains rich in serine-arginine dipeptides. The specific RNA binding by SRSF5 requires the phosphorylation of its SR domain
RVFIGRLNPAAREKDVERFFKGYGRIRDIDLKRGFGFVEFEDPRDADDAVYELDGKELCNERVTIEHARV
>gnl|CDD|410009 cd12596, RRM1_SRSF6, RNA recognition motif 1 (RRM1) found in vertebrate serine/arginine-rich splicing factor 6 (SRSF6). This subfamily corresponds to the RRM1 of SRSF6, also termed pre-mRNA-splicing factor SRp55, which is an essential splicing regulatory serine/arginine (SR) protein that preferentially interacts with a number of purine-rich splicing enhancers (ESEs) to activate splicing of the ESE-containing exon. It is the only protein from HeLa nuclear extract or purified SR proteins that specifically binds B element RNA after UV irradiation. SRSF6 may also recognize different types of RNA sites. For instance, it does not bind to the purine-rich sequence in the calcitonin-specific ESE, but binds to a region adjacent to the purine tract. Moreover, cellular levels of SRSF6 may control tissue-specific alternative splicing of the calcitonin/ calcitonin gene-related peptide (CGRP) pre-mRNA. SRSF6 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a C-terminal SR domains rich in serine-arginine dipeptides
MPRVYIGRLSYHVREKDIQRFFSGYGKLLEVDLKNGYGFVEFEDSRDADDAVYELNGKELCGERVIVEHA
RG
>gnl|CDD|410010 cd12597, RRM1_SRSF1, RNA recognition motif 1 (RRM1) found in serine/arginine-rich splicing factor 1 (SRSF1) and similar proteins. This subgroup corresponds to the RRM1 of SRSF1, also termed alternative-splicing factor 1 (ASF-1), or pre-mRNA-splicing factor SF2, P33 subunit. SRSF1 is a splicing regulatory serine/arginine (SR) protein involved in constitutive and alternative splicing, nonsense-mediated mRNA decay (NMD), mRNA export and translation. It also functions as a splicing-factor oncoprotein that regulates apoptosis and proliferation to promote mammary epithelial cell transformation. SRSF1 is a shuttling SR protein and contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), separated by a long glycine-rich spacer, and a C-terminal RS domains rich in serine-arginine dipeptides
GNNDCRIYVGNLPPDIRTKDIEDVFYKYGAIRDIDLKNRRGGPPFAFVEFEDPRDAEDAVYGRDGYDYDG
YRLRVEFPR
>gnl|CDD|241042 cd12598, RRM1_SRSF9, RNA recognition motif 1 (RRM1) found in vertebrate serine/arginine-rich splicing factor 9 (SRSF9). This subgroup corresponds to the RRM1 of SRSF9, also termed pre-mRNA-splicing factor SRp30C. SRSF9 is an essential splicing regulatory serine/arginine (SR) protein that has been implicated in the activity of many elements that control splice site selection, the alternative splicing of the glucocorticoid receptor beta in neutrophils and in the gonadotropin-releasing hormone pre-mRNA. SRSF9 can also interact with other proteins implicated in alternative splicing, including YB-1, rSLM-1, rSLM-2, E4-ORF4, Nop30, and p32. SRSF9 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by an unusually short C-terminal RS domains rich in serine-arginine dipeptides
RIYVGNLPSDVREKDLEDLFYKYGRIRDIELKNRRGLVPFAFVRFEDPRDAEDAVFGRNGYDFGQCRLRV
EF
>gnl|CDD|410011 cd12599, RRM1_SF2_plant_like, RNA recognition motif 1 (RRM1) found in plant pre-mRNA-splicing factor SF2 and similar proteins. This subgroup corresponds to the RRM1 of SF2, also termed SR1 protein, a plant serine/arginine (SR)-rich phosphoprotein similar to the mammalian splicing factor SF2/ASF. It promotes splice site switching in mammalian nuclear extracts. SF2 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a C-terminal domain rich in proline, serine and lysine residues (PSK domain), a composition reminiscent of histones. This PSK domain harbors a putative phosphorylation site for the mitotic kinase cyclin/p34cdc2
RVYVGNLPMDIREREVEDLFSKYGPVVSIDLKIPPRPPAYAFVEFEDARDAEDAIRGRDGYDFDGHRLRV
EL
>gnl|CDD|410012 cd12600, RRM2_SRSF4_like, RNA recognition motif 2 (RRM2) found in serine/arginine-rich splicing factor 4 (SRSF4) and similar proteins. This subfamily corresponds to the RRM2 of three serine/arginine (SR) proteins: serine/arginine-rich splicing factor 4 (SRSF4 or SRp75 or SFRS4), serine/arginine-rich splicing factor 5 (SRSF5 or SRp40 or SFRS5 or HRS), serine/arginine-rich splicing factor 6 (SRSF6 or SRp55). SRSF4 plays an important role in both, constitutive and alternative, splicing of many pre-mRNAs. It can shuttle between the nucleus and cytoplasm. SRSF5 regulates both alternative splicing and basal splicing. It is the only SR protein efficiently selected from nuclear extracts (NE) by the splicing enhancer (ESE) and is essential for enhancer activation. SRSF6 preferentially interacts with a number of purine-rich splicing enhancers (ESEs) to activate splicing of the ESE-containing exon. It is the only protein from HeLa nuclear extract or purified SR proteins that specifically binds B element RNA after UV irradiation. SRSF6 may also recognize different types of RNA sites. Members in this family contain two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a C-terminal RS domains rich in serine-arginine dipeptides
YRLIVENLSSRVSWQDLKDYMRQAGEVTYADAHKQRKNEGVVEFASYSDMKNAIEKLDGTELNGRKIRLV
ED
>gnl|CDD|410013 cd12601, RRM2_SRSF1_like, RNA recognition motif 2 (RRM2) found in serine/arginine-rich splicing factor SRSF1, SRSF9 and similar proteins. This subfamily corresponds to the RRM2 of serine/arginine-rich splicing factor SRSF1, SRSF9 and similar proteins. SRSF1, also termed ASF-1, is a shuttling SR protein involved in constitutive and alternative splicing, nonsense-mediated mRNA decay (NMD), mRNA export and translation. It also functions as a splicing-factor oncoprotein that regulates apoptosis and proliferation to promote mammary epithelial cell transformation. SRSF9, also termed SRp30C, has been implicated in the activity of many elements that control splice site selection, the alternative splicing of the glucocorticoid receptor beta in neutrophils and in the gonadotropin-releasing hormone pre-mRNA. SRSF9 can also interact with other proteins implicated in alternative splicing, including YB-1, rSLM-1, rSLM-2, E4-ORF4, Nop30, and p32. Both, SRSF1 and SRSF9, contain two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal RS domains rich in serine-arginine dipeptides
YRVIVSGLPPTGSWQDLKDHMREAGDVCYADVYRDGTGVVEFLRYEDMKYAVRKLDDSKFRSHEGETSYI
RVKE
>gnl|CDD|410014 cd12602, RRM2_SF2_plant_like, RNA recognition motif 2 (RRM2) found in plant pre-mRNA-splicing factor SF2 and similar proteins. This subfamily corresponds to the RRM2 of SF2, also termed SR1 protein, a plant serine/arginine (SR)-rich phosphoprotein similar to the mammalian splicing factor SF2/ASF. It promotes splice site switching in mammalian nuclear extracts. SF2 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a C-terminal domain rich in proline, serine and lysine residues (PSK domain), a composition reminiscent of histones. This PSK domain harbors a putative phosphorylation site for the mitotic kinase cyclin/p34cdc2
FRVLVTGLPSSASWQDLKDHMRRAGEVCFSQVFRDGRGTTGVVDYTTYDDMKYAIRKLDDTEFRNAFSRG
YVRVRE
>gnl|CDD|410015 cd12603, RRM_hnRNPC, RNA recognition motif (RRM) found in vertebrate heterogeneous nuclear ribonucleoprotein C1/C2 (hnRNP C1/C2). This subgroup corresponds to the RRM of heterogeneous nuclear ribonucleoprotein C (hnRNP) proteins C1 and C2, produced by a single coding sequence. They are the major constituents of the heterogeneous nuclear RNA (hnRNA) ribonucleoprotein (hnRNP) complex in vertebrates. They bind hnRNA tightly, suggesting a central role in the formation of the ubiquitous hnRNP complex. They are involved in the packaging of hnRNA in the nucleus and in processing of pre-mRNA such as splicing and 3'-end formation. hnRNP C proteins contain two distinct domains, an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal auxiliary domain that includes the variable region, the basic region and the KSG box rich in repeated Lys-Ser-Gly sequences, the leucine zipper, and the acidic region. The RRM is capable of binding poly(U). The KSG box may bind to RNA. The leucine zipper may be involved in dimer formation. The acidic and hydrophilic C-teminus harbors a putative nucleoside triphosphate (NTP)-binding fold and a protein kinase phosphorylation site
DPRSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQV
LDINLAAEPKVNRS
>gnl|CDD|410016 cd12604, RRM_RALY, RNA recognition motif (RRM) found in vertebrate RNA-binding protein Raly. This subgroup corresponds to the RRM of Raly, also termed autoantigen p542, or heterogeneous nuclear ribonucleoprotein C-like 2, or hnRNP core protein C-like 2, or hnRNP associated with lethal yellow protein homolog, an RNA-binding protein that may play a critical role in embryonic development. It is encoded by Raly, a ubiquitously expressed gene of unknown function. Raly shows a high degree of identity with the 5' sequences of p542 gene encoding autoantigen, which can cross-react with EBNA-1 of the Epstein Barr virus. Raly contains two distinct domains, an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal auxiliary domain that includes a unique glycine/serine-rich stretch
NSRVFIGNLNTAVVKKSDVETIFSKYGRVVGCSVHKGYAFVQYTNERHARAAVIGENGRVLAGQTLDINM
AGEPKP
>gnl|CDD|410017 cd12605, RRM_RALYL, RNA recognition motif (RRM) found in vertebrate RNA-binding Raly-like protein (RALYL). This subgroup corresponds to the RRM of RALYL, also termed heterogeneous nuclear ribonucleoprotein C-like 3, or hnRNP core protein C-like 3, a putative RNA-binding protein that shows high sequence homology with Raly, an RNA-binding protein playing a critical role in embryonic development. The biological role of RALYL remains unclear. Like Raly, RALYL contains two distinct domains, an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal auxiliary domain
NSRVFIGNLNTAIVKKADIEAIFAKYGKIVGCSVHKGYAFVQYMSERHARAAVAGENARIIAGQPLDIN
>gnl|CDD|410018 cd12606, RRM1_RBM4, RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding protein 4 (RBM4). This subgroup corresponds to the RRM1 of RBM4, a ubiquitously expressed splicing factor that has two isoforms, RBM4A (also known as Lark homolog) and RBM4B (also known as RBM30), which are very similar in structure and sequence. RBM4 may function as a translational regulator of stress-associated mRNAs and also plays a role in micro-RNA-mediated gene regulation. RBM4 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), a CCHC-type zinc finger, and three alanine-rich regions within their C-terminal regions. The C-terminal region may be crucial for nuclear localization and protein-protein interaction. The RRMs, in combination with the C-terminal region, are responsible for the splicing function of RBM4
VKLFIGNLPREATEEEIRSLFEQYGKVTECDIIKNYGFVHMEDKSAADEAIRNLHHYKLHGVAINVE
>gnl|CDD|410019 cd12607, RRM2_RBM4, RNA recognition motif 2 (RRM2) found in vertebrate RNA-binding protein 4 (RBM4). This subgroup corresponds to the RRM2 of RBM4, a ubiquitously expressed splicing factor that has two isoforms, RBM4A (also known as Lark homolog) and RBM4B (also known as RBM30), which are very similar in structure and sequence. RBM4 may function as a translational regulator of stress-associated mRNAs and also plays a role in micro-RNA-mediated gene regulation. RBM4 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), a CCHC-type zinc finger, and three alanine-rich regions within their C-terminal regions. The C-terminal region may be crucial for nuclear localization and protein-protein interaction. The RRMs, in combination with the C-terminal region, are responsible for the splicing function of RBM4
TKLHVGNISSSCTNQELRAKFEEYGPVIECDIVKDYAFVHMERAEDAMEAIRGLDNTEFQGKRMHVQ
>gnl|CDD|410020 cd12608, RRM1_CoAA, RNA recognition motif 1 (RRM1) found in vertebrate RRM-containing coactivator activator/modulator (CoAA). This subgroup corresponds to the RRM1 of CoAA, also termed RNA-binding protein 14 (RBM14), or paraspeckle protein 2 (PSP2), or synaptotagmin-interacting protein (SYT-interacting protein), a heterogeneous nuclear ribonucleoprotein (hnRNP)-like protein identified as a nuclear receptor coactivator. It mediates transcriptional coactivation and RNA splicing effects in a promoter-preferential manner and is enhanced by thyroid hormone receptor-binding protein (TRBP). CoAA contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a TRBP-interacting domain. It stimulates transcription through its interactions with coactivators, such as TRBP and CREB-binding protein CBP/p300, via the TRBP-interacting domain and interaction with an RNA-containing complex, such as DNA-dependent protein kinase-poly(ADP-ribose) polymerase complexes, via the RRMs
MKIFVGNVDEDTSQEELSALFEPYGAVLSCAVMKQFAFVHMRGEAAADRAIRELNGRELHGRALVVEES
>gnl|CDD|410021 cd12609, RRM2_CoAA, RNA recognition motif 2 (RRM2) found in vertebrate RRM-containing coactivator activator/modulator (CoAA). This subgroup corresponds to the RRM2 of CoAA, also termed RNA-binding protein 14 (RBM14), or paraspeckle protein 2 (PSP2), or synaptotagmin-interacting protein (SYT-interacting protein), a heterogeneous nuclear ribonucleoprotein (hnRNP)-like protein identified as a nuclear receptor coactivator. It mediates transcriptional coactivation and RNA splicing effects in a promoter-preferential manner and is enhanced by thyroid hormone receptor-binding protein (TRBP). CoAA contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a TRBP-interacting domain. It stimulates transcription through its interactions with coactivators, such as TRBP and CREB-binding protein CBP/p300, via the TRBP-interacting domain and interaction with an RNA-containing complex, such as DNA-dependent protein kinase-poly(ADP-ribose) polymerase complexes, via the RRMs
WKIFVGNVSATCTSDELRGLFEEFGRVVECDKVKDYAFVHMEREEEALAAIEALNGKEVKGRRINVEL
>gnl|CDD|410022 cd12610, RRM1_SECp43, RNA recognition motif 1 (RRM1) found in tRNA selenocysteine-associated protein 1 (SECp43). This subgroup corresponds to the RRM1 of SECp43, an RNA-binding protein associated specifically with eukaryotic selenocysteine tRNA [tRNA(Sec)]. It may play an adaptor role in the mechanism of selenocysteine insertion. SECp43 is located primarily in the nucleus and contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal polar/acidic region
SLWMGDLEPYMDENFIKRAFATMGETVLSVKIIRNRVTGGPAGYCFVEFADEATAERCLHKLNGKPIPGS
NPPKRFKLNHATYG
>gnl|CDD|410023 cd12611, RRM1_NGR1_NAM8_like, RNA recognition motif 1 (RRM1) found in yeast negative growth regulatory protein NGR1, yeast protein NAM8 and similar proteins. This subgroup corresponds to the RRM1 of NGR1 and NAM8. NGR1, also termed RNA-binding protein RBP1, is a putative glucose-repressible protein that binds both, RNA and single-stranded DNA (ssDNA), in yeast. It may function in regulating cell growth in early log phase, possibly through its participation in RNA metabolism. NGR1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two of which are followed by a glutamine-rich stretch that may be involved in transcriptional activity. In addition, NGR1 has an asparagine-rich region near the carboxyl terminus which also harbors a methionine-rich region. The subgroup also includes NAM8, a putative RNA-binding protein that acts as a suppressor of mitochondrial splicing deficiencies when overexpressed in yeast. It may be a non-essential component of the mitochondrial splicing machinery. Like NGR1, NAM8 contains two RRMs
TLWMGDLEPWMDENFIKQIWASLGLKPVNVKVIRSKSGGLNGNAGYCFVEFPSPHAAQNALSLNGTPIPG
SESRTFKLNWASGG
>gnl|CDD|410024 cd12612, RRM2_SECp43, RNA recognition motif 2 (RRM2) found in tRNA selenocysteine-associated protein 1 (SECp43). This subgroup corresponds to the RRM2 of SECp43, an RNA-binding protein associated specifically with eukaryotic selenocysteine tRNA [tRNA(Sec)]. It may play an adaptor role in the mechanism of selenocysteine insertion. SECp43 is located primarily in the nucleus and contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal polar/acidic region
EFSLFVGDLTPEVDDGMLYEFFLKRYPSCKGAKVVLDQLGNSRGYGFVRFSDENEQKRALTECQGASGLG
GKPIRLSVAIPK
>gnl|CDD|410025 cd12613, RRM2_NGR1_NAM8_like, RNA recognition motif 2 (RRM2) found in yeast negative growth regulatory protein NGR1, yeast protein NAM8 and similar proteins. This subgroup corresponds to the RRM2 of NGR1 and NAM8. NGR1, also termed RNA-binding protein RBP1, is a putative glucose-repressible protein that binds both, RNA and single-stranded DNA (ssDNA), in yeast. It may function in regulating cell growth in early log phase, possibly through its participation in RNA metabolism. NGR1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a glutamine-rich stretch that may be involved in transcriptional activity. In addition, NGR1 has an asparagine-rich region near the carboxyl terminus which also harbors a methionine-rich region. The family also includes protein NAM8, which is a putative RNA-binding protein that acts as a suppressor of mitochondrial splicing deficiencies when overexpressed in yeast. It may be a non-essential component of the mitochondrial splicing machinery. Like NGR1, NAM8 contains two RRMs
EYSIFVGDLSPTTNESDLVSLFQSRFPSCKSAKIMTDPVTGVSRGYGFVRFSDENDQQRALIEMQGKYCQ
GRPLRISYAT
>gnl|CDD|410026 cd12614, RRM1_PUB1, RNA recognition motif 1 (RRM1) found in yeast nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1 and similar proteins. This subgroup corresponds to the RRM1 of yeast protein PUB1, also termed ARS consensus-binding protein ACBP-60, or poly uridylate-binding protein, or poly(U)-binding protein. PUB1 has been identified as both, a heterogeneous nuclear RNA-binding protein (hnRNP) and a cytoplasmic mRNA-binding protein (mRNP), which may be stably bound to a translationally inactive subpopulation of mRNAs within the cytoplasm. It is distributed in both, the nucleus and the cytoplasm, and binds to poly(A)+ RNA (mRNA or pre-mRNA). Although it is one of the major cellular proteins cross-linked by UV light to polyadenylated RNAs in vivo, PUB1 is nonessential for cell growth in yeast. PUB1 also binds to T-rich single stranded DNA (ssDNA); however, there is no strong evidence implicating PUB1 in the mechanism of DNA replication. PUB1 contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a GAR motif (glycine and arginine rich stretch) that is located between RRM2 and RRM3
LYVGNLDPRVTEDLLQEIFAVTGPVENCKIIPDKNSKGVNYGFVEYYDRRSAEIAIQTLNGRQIFGQEIK
VNWA
>gnl|CDD|410027 cd12615, RRM1_TIA1, RNA recognition motif 1 (RRM1) found in nucleolysin TIA-1 isoform p40 (p40-TIA-1) and similar proteins. This subgroup corresponds to the RRM1 of TIA-1, the 40-kDa isoform of T-cell-restricted intracellular antigen-1 (TIA-1) and a cytotoxic granule-associated RNA-binding protein mainly found in the granules of cytotoxic lymphocytes. TIA-1 can be phosphorylated by a serine/threonine kinase that is activated during Fas-mediated apoptosis, and functions as the granule component responsible for inducing apoptosis in cytolytic lymphocyte (CTL) targets. It is composed of three N-terminal highly homologous RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a glutamine-rich C-terminal auxiliary domain containing a lysosome-targeting motif. TIA-1 interacts with RNAs containing short stretches of uridylates and its RRM2 can mediate the specific binding to uridylate-rich RNAs
TLYVGNLSRDVTEALILQLFSQIGPCKNCKMIMDTAGNDPYCFVEFHEHRHAAAALAAMNGRKIMGKEVK
VNWA
>gnl|CDD|410028 cd12616, RRM1_TIAR, RNA recognition motif 1 (RRM1) found in nucleolysin TIAR and similar proteins. This subgroup corresponds to the RRM1 of nucleolysin TIAR, also termed TIA-1-related protein, and a cytotoxic granule-associated RNA-binding protein that shows high sequence similarity with 40-kDa isoform of T-cell-restricted intracellular antigen-1 (p40-TIA-1). TIAR is mainly localized in the nucleus of hematopoietic and nonhematopoietic cells. It is translocated from the nucleus to the cytoplasm in response to exogenous triggers of apoptosis. TIAR possesses nucleolytic activity against cytolytic lymphocyte (CTL) target cells. It can trigger DNA fragmentation in permeabilized thymocytes, and thus may function as an effector responsible for inducing apoptosis. TIAR is composed of three N-terminal highly homologous RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a glutamine-rich C-terminal auxiliary domain containing a lysosome-targeting motif. It interacts with RNAs containing short stretches of uridylates and its RRM2 can mediate the specific binding to uridylate-rich RNAs
TLYVGNLSRDVTEVLILQLFSQIGPCKSCKMITEHTSNDPYCFVEFYEHRDAAAALAAMNGRKILGKEVK
VNWATTPSSQK
>gnl|CDD|410029 cd12617, RRM2_TIAR, RNA recognition motif 2 (RRM2) found in nucleolysin TIAR and similar proteins. This subgroup corresponds to the RRM2 of nucleolysin TIAR, also termed TIA-1-related protein, a cytotoxic granule-associated RNA-binding protein that shows high sequence similarity with 40-kDa isoform of T-cell-restricted intracellular antigen-1 (p40-TIA-1). TIAR is mainly localized in the nucleus of hematopoietic and nonhematopoietic cells. It is translocated from the nucleus to the cytoplasm in response to exogenous triggers of apoptosis. TIAR possesses nucleolytic activity against cytolytic lymphocyte (CTL) target cells. It can trigger DNA fragmentation in permeabilized thymocytes, and thus may function as an effector responsible for inducing apoptosis. TIAR is composed of three N-terminal, highly homologous RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a glutamine-rich C-terminal auxiliary domain containing a lysosome-targeting motif. It interacts with RNAs containing short stretches of uridylates and its RRM2 can mediate the specific binding to uridylate-rich RNAs
HFHVFVGDLSPEITTEDIKSAFAPFGKISDARVVKDMATGKSKGYGFVSFYNKLDAENAIVHMGGQWLGG
RQIRTNWATR
>gnl|CDD|410030 cd12618, RRM2_TIA1, RNA recognition motif 2 (RRM2) found in nucleolysin TIA-1 isoform p40 (p40-TIA-1) and similar proteins. This subgroup corresponds to the RRM2 of p40-TIA-1, the 40-kDa isoform of T-cell-restricted intracellular antigen-1 (TIA-1), and a cytotoxic granule-associated RNA-binding protein mainly found in the granules of cytotoxic lymphocytes. TIA-1 can be phosphorylated by a serine/threonine kinase that is activated during Fas-mediated apoptosis, and function as the granule component responsible for inducing apoptosis in cytolytic lymphocyte (CTL) targets. It is composed of three N-terminal highly homologous RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a glutamine-rich C-terminal auxiliary domain containing a lysosome-targeting motif. TIA-1 interacts with RNAs containing short stretches of uridylates and its RRM2 can mediate the specific binding to uridylate-rich RNAs
NHFHVFVGDLSPEITTEDIKAAFAPFGRISDARVVKDMATGKSKGYGFVSFFNKWDAENAIQQMGGQWLG
GRQIRTNW
>gnl|CDD|410031 cd12619, RRM2_PUB1, RNA recognition motif 2 (RRM2) found in yeast nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1 and similar proteins. This subgroup corresponds to the RRM2 of yeast protein PUB1, also termed ARS consensus-binding protein ACBP-60, or poly uridylate-binding protein, or poly(U)-binding protein. PUB1 has been identified as both, a heterogeneous nuclear RNA-binding protein (hnRNP) and a cytoplasmic mRNA-binding protein (mRNP), which may be stably bound to a translationally inactive subpopulation of mRNAs within the cytoplasm. It is distributed in both, the nucleus and the cytoplasm, and binds to poly(A)+ RNA (mRNA or pre-mRNA). Although it is one of the major cellular proteins cross-linked by UV light to polyadenylated RNAs in vivo, PUB1 is nonessential for cell growth in yeast. PUB1 also binds to T-rich single stranded DNA (ssDNA). However, there is no strong evidence implicating PUB1 in the mechanism of DNA replication. PUB1 contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a GAR motif (glycine and arginine rich stretch) that is located between RRM2 and RRM3
HFNIFVGDLSPEVTDAALFNAFSDFPSCSDARVMWDQKTGRSRGYGFVSFRSQQDAQNAINSMNGKWLGS
RPIRCNWATK
>gnl|CDD|241064 cd12620, RRM3_TIAR, RNA recognition motif 3 (RRM3) found in nucleolysin TIAR and similar proteins. This subgroup corresponds to the RRM3 of nucleolysin TIAR, also termed TIA-1-related protein, a cytotoxic granule-associated RNA-binding protein that shows high sequence similarity with 40-kDa isoform of T-cell-restricted intracellular antigen-1 (p40-TIA-1). TIAR is mainly localized in the nucleus of hematopoietic and nonhematopoietic cells. It is translocated from the nucleus to the cytoplasm in response to exogenous triggers of apoptosis. TIAR possesses nucleolytic activity against cytolytic lymphocyte (CTL) target cells. It can trigger DNA fragmentation in permeabilized thymocytes, and thus may function as an effector responsible for inducing apoptosis. TIAR is composed of three N-terminal highly homologous RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a glutamine-rich C-terminal auxiliary domain containing a lysosome-targeting motif. It interacts with RNAs containing short stretches of uridylates and its RRM2 can mediate the specific binding to uridylate-rich RNAs
CTVYCGGIASGLTEQLMRQTFSPFGQIMEIRVFPEKGYSFVRFSTHESAAHAIVSVNGTTIEGHVVKCYW
GKE
>gnl|CDD|410032 cd12621, RRM3_TIA1, RNA recognition motif 3 (RRM3) found in nucleolysin TIA-1 isoform p40 (p40-TIA-1) and similar proteins. This subgroup corresponds to the RRM3 of p40-TIA-1, the 40-kDa isoform of T-cell-restricted intracellular antigen-1 (TIA-1) and a cytotoxic granule-associated RNA-binding protein mainly found in the granules of cytotoxic lymphocytes. TIA-1 can be phosphorylated by a serine/threonine kinase that is activated during Fas-mediated apoptosis, and function as the granule component responsible for inducing apoptosis in cytolytic lymphocyte (CTL) targets. It is composed of three N-terminal highly homologous RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a glutamine-rich C-terminal auxiliary domain containing a lysosome-targeting motif. TIA-1 interacts with RNAs containing short stretches of uridylates and its RRM2 can mediate the specific binding to uridylate-rich RNAs
CTVYCGGVTSGLTEQLMRQTFSPFGQIMEIRVFPDKGYSFVRFNSHESAAHAIVSVNGTTIEGHVVKCYW
GK
>gnl|CDD|410033 cd12622, RRM3_PUB1, RNA recognition motif 3 (RRM3) found in yeast nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1 and similar proteins. This subfamily corresponds to the RRM3 of yeast protein PUB1, also termed ARS consensus-binding protein ACBP-60, or poly uridylate-binding protein, or poly(U)-binding protein. PUB1 has been identified as both, a heterogeneous nuclear RNA-binding protein (hnRNP) and a cytoplasmic mRNA-binding protein (mRNP), which may be stably bound to a translationally inactive subpopulation of mRNAs within the cytoplasm. PUB1 is distributed in both, the nucleus and the cytoplasm, and binds to poly(A)+ RNA (mRNA or pre-mRNA). Although it is one of the major cellular proteins cross-linked by UV light to polyadenylated RNAs in vivo, PUB1 is nonessential for cell growth in yeast. PUB1 also binds to T-rich single stranded DNA (ssDNA); however, there is no strong evidence implicating PUB1 in the mechanism of DNA replication. PUB1 contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a GAR motif (glycine and arginine rich stretch) that is located between RRM2 and RRM3
TTVYVGNLPPEVTQADLIPLFQNFGVIEEVRVQRDKGFGFVKYDTHEEAALAIQQLNGQPFLGRPIKCSW
GKKR
>gnl|CDD|410034 cd12623, RRM_PPARGC1A, RNA recognition motif (RRM) found in peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1alpha, or PPARGC-1-alpha) and similar proteins. This subgroup corresponds to the RRM of PGC-1alpha, also termed PPARGC-1-alpha, or ligand effect modulator 6, a member of a family of transcription coactivators that plays a central role in the regulation of cellular energy metabolism. As an inducible transcription coactivator, PGC-1alpha can interact with a broad range of transcription factors involved in a wide variety of biological responses, such as adaptive thermogenesis, skeletal muscle fiber type switching, glucose/fatty acid metabolism, and heart development. PGC-1alpha stimulates mitochondrial biogenesis and promotes oxidative metabolism. It participates in the regulation of both carbohydrate and lipid metabolism and plays a role in disorders such as obesity, diabetes, and cardiomyopathy. PGC-1alpha is a multi-domain protein containing an N-terminal activation domain region, a central region involved in the interaction with at least a nuclear receptor, and a C-terminal domain region. The N-terminal domain region consists of three leucine-rich motifs (L1, NR box 2 and 3), among which the two last are required for interaction with nuclear receptors, potential nuclear localization signals (NLS), and a proline-rich region overlapping a putative repression domain. The C-terminus of PGC-1alpha is composed of two arginine/serine-rich regions (SR domains), a putative dimerization domain, and an RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain). PGC-1alpha could interact favorably with single-stranded RNA
ERRVIYVGKIRPDITRTELKRRFEVFGEIEECTVNLRDDGDSYGFITYRYTCDAFAALENGYTLRRSNEP
DFELCFGGRKQFCKSNYADLD
>gnl|CDD|410035 cd12624, RRM_PRC, RNA recognition motif (RRM) found in peroxisome proliferator-activated receptor gamma coactivator-related protein 1 (PRC) and similar proteins. This subgroup corresponds to the RRM of PRC, also termed PGC-1-related coactivator, one of the members of PGC-1 transcriptional coactivators family, including peroxisome proliferator-activated receptor gamma coactivators PGC-1alpha and PGC-1beta. Unlike PGC-1alpha and PGC-1beta, PRC is ubiquitous and more abundantly expressed in proliferating cells than in growth-arrested cells. PRC has been implicated in the regulation of several metabolic pathways, mitochondrial biogenesis, and cell growth. It functions as a growth-regulated transcriptional cofactor activating many nuclear genes specifying mitochondrial respiratory function. PRC directly interacts with nuclear transcriptional factors implicated in respiratory chain expression including nuclear respiratory factors 1 and 2 (NRF-1 and NRF-2), CREB (cAMP-response element-binding protein), and estrogen-related receptor alpha (ERRalpha). It interacts indirectly with the NRF-2beta subunit through host cell factor (HCF), a cellular protein involved in herpes simplex virus (HSV) infection and cell cycle regulation. Furthermore, like PGC-1alpha and PGC-1beta, PRC can transactivate a number of NRF-dependent nuclear genes required for mitochondrial respiratory function, including those encoding cytochrome c, 5-aminolevulinate synthase, Tfam, and TFB1M, and TFB2M. Further research indicates that PRC may also act as a sensor of metabolic stress that orchestrates a redox-sensitive program of inflammatory gene expression. PRC is a multi-domain protein containing an N-terminal activation domain, an LXXLL coactivator signature, a central proline-rich region, a tetrapeptide motif (DHDY) responsible for HCF binding, a C-terminal arginine/serine-rich (SR) domain, and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
ERRVVYIGKIRGRMTRSELKDRFSVFGEIEECTIHFREEGDNYGFVTYRYTEDAFAAIENGHKLRRPDEL
PFDLCFGGRRQFCKSSYADLD
>gnl|CDD|241069 cd12625, RRM1_IGF2BP1, RNA recognition motif 1 (RRM1) found in vertebrate insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1). This subgroup corresponds to the RRM1 of IGF2BP1 (IGF2 mRNA-binding protein 1 or IMP-1), also termed coding region determinant-binding protein (CRD-BP), or VICKZ family member 1, or zipcode-binding protein 1 (ZBP-1). IGF2BP1 is a multi-functional regulator of RNA metabolism that has been implicated in the control of aspects of localization, stability, and translation for many mRNAs. It is predominantly located in cytoplasm and was initially identified as a trans-acting factor that interacts with the zipcode in the 3'- untranslated region (UTR) of the beta-actin mRNA, which is important for its localization and translational regulation. It inhibits IGF-II mRNA translation through binding to the 5'-UTR of the transcript. IGF2BP1 also acts as human immunodeficiency virus type 1 (HIV-1) Gag-binding factor that interacts with HIV-1 Gag protein and blocks the formation of infectious HIV-1 particles. IGF2BP1 promotes mRNA stabilization; it functions as a coding region determinant (CRD)-binding protein that binds to the coding region of betaTrCP1 mRNA and prevents miR-183-mediated degradation of betaTrCP1 mRNA. It also promotes c-myc mRNA stability by associating with the CRD and stabilizes CD44 mRNA via interaction with the 3'-UTR of the transcript. In addition, IGF2BP1 specifically interacts with both Hepatitis C virus (HCV) 5'-UTR and 3'-UTR, further recruiting eIF3 and enhancing HCV internal ribosome entry site (IRES)-mediated translation initiation via the 3'-UTR. IGF2BP1 contains four hnRNP K-homology (KH) domains, two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a RGG RNA-binding domain. It also contains two putative nuclear export signals (NESs) and a putative nuclear localization signal (NLS)
MNKLYIGNLNESVTPADLEKVFEDHKISYSGQFLVKSGYAFVDCPDEQWAMKAIETFSGKVELHGKRLEI
EHSVPKK
>gnl|CDD|241070 cd12626, RRM1_IGF2BP2, RNA recognition motif 1 (RRM1) found in vertebrate insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2). This subgroup corresponds to the RRM1 of IGF2BP2 (IGF2 mRNA-binding protein 2 or IMP-2), also termed hepatocellular carcinoma autoantigen p62, or VICKZ family member 2, which is a ubiquitously expressed RNA-binding protein involved in the stimulation of insulin action. It is predominantly nuclear. SNPs in IGF2BP2 gene are implicated in susceptibility to type 2 diabetes. IGF2BP2 plays an important role in cellular motility; it regulates the expression of PINCH-2, an important mediator of cell adhesion and motility, and MURF-3, a microtubule-stabilizing protein, through direct binding to their mRNAs. IGF2BP2 may be involved in the regulation of mRNA stability through the interaction with the AU-rich element-binding factor AUF1. IGF2BP2 binds initially to nascent beta-actin transcripts and facilitates the subsequent binding of the shuttling IGF2BP1. IGF2BP2 contains four hnRNP K-homology (KH) domains, two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a RGG RNA-binding domain
MNKLYIGNLSPAVTAEDLRQLFGDRKLPLTGQVLLKSGYAFVDYPDQNWAIRAIETLSGKVELHGKVMEV
DYSVPKK
>gnl|CDD|410036 cd12627, RRM1_IGF2BP3, RNA recognition motif 1 (RRM1) found in vertebrate insulin-like growth factor 2 mRNA-binding protein 3 (IGF2BP3). This subgroup corresponds to the RRM1 of IGF2BP3 (IGF2 mRNA-binding protein 3 or IMP-3), also termed KH domain-containing protein overexpressed in cancer (KOC), or VICKZ family member 3, an RNA-binding protein that plays an important role in the differentiation process during early embryogenesis. It is known to bind to and repress the translation of IGF2 leader 3 mRNA. IGF2BP3 also acts as a Glioblastoma-specific proproliferative and proinvasive marker acting through IGF2 resulting in the activation of oncogenic phosphatidylinositol 3-kinase/mitogen-activated protein kinase (PI3K/MAPK) pathways. IGF2BP3 contains four hnRNP K-homology (KH) domains, two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a RGG RNA-binding domain
MNKLYIGNLSENASPLDLESIFKDWKIPFSGPFLVKTGYAFVDCPDESWAMKAIDTLSGKVELHGKVIEV
EHSVPKR
>gnl|CDD|410037 cd12628, RRM2_IGF2BP1, RNA recognition motif 2 (RRM2) found in vertebrate insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1). This subgroup corresponds to the RRM2 of IGF2BP1 (IGF2 mRNA-binding protein 1 or IMP-1), also termed coding region determinant-binding protein (CRD-BP), or VICKZ family member 1, or zipcode-binding protein 1 (ZBP-1). IGF2BP1 is a multi-functional regulator of RNA metabolism that has been implicated in the control of aspects of localization, stability, and translation for many mRNAs. It is predominantly located in cytoplasm and was initially identified as a trans-acting factor that interacts with the zipcode in the 3'- untranslated region (UTR) of the beta-actin mRNA, which is important for its localization and translational regulation. It inhibits IGF-II mRNA translation through binding to the 5'-UTR of the transcript. IGF2BP1 also acts as human immunodeficiency virus type 1 (HIV-1) Gag-binding factor that interacts with HIV-1 Gag protein and blocks the formation of infectious HIV-1 particles. It promotes mRNA stabilization and functions as a coding region determinant (CRD)-binding protein that binds to the coding region of betaTrCP1 mRNA and prevents miR-183-mediated degradation of betaTrCP1 mRNA. It also promotes c-myc mRNA stability by associating with the CRD. It stabilizes CD44 mRNA via interaction with the 3'-UTR of the transcript. In addition, IGF2BP1 specifically interacts with both Hepatitis C virus (HCV) 5'-UTR and 3'-UTR, further recruiting eIF3 and enhancing HCV internal ribosome entry site (IRES)-mediated translation initiation via the 3'-UTR. IGF2BP1 contains four hnRNP K-homology (KH) domains, two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a RGG RNA-binding domain. It also contains two putative nuclear export signals (NESs) and a putative nuclear localization signal (NLS)
RKIQIRNIPPQLRWEVLDGLLAQYGTVENCEQVNTDSETAVVNVTYGNREQTRQAIMKLNGHQLENHVLK
VSYIPD
>gnl|CDD|410038 cd12629, RRM2_IGF2BP2, RNA recognition motif 2 (RRM2) found in vertebrate insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2). This subgroup corresponds to the RRM2 of IGF2BP2 (IGF2 mRNA-binding protein 2 or IMP-2), also termed hepatocellular carcinoma autoantigen p62, or VICKZ family member 2, a ubiquitously expressed RNA-binding protein involved in the stimulation of insulin action. It is predominantly nuclear. SNPs in IGF2BP2 gene are implicated in susceptibility to type 2 diabetes. IGF2BP2 plays an important role in cellular motility; it regulates the expression of PINCH-2, an important mediator of cell adhesion and motility, and MURF-3, a microtubule-stabilizing protein, through direct binding to their mRNAs. IGF2BP2 may be involved in the regulation of mRNA stability through the interaction with the AU-rich element-binding factor AUF1. In addition, IGF2BP2 binds initially to nascent beta-actin transcripts and facilitates the subsequent binding of the shuttling IGF2BP1. IGF2BP2 contains four hnRNP K-homology (KH) domains, two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a RGG RNA-binding domain
RKIQIRNIPPHLQWEVLDGLLAQYGTVENVEQVNTDTETAVVNVTYATKEEAKVAVEKLSGHQFENYSFK
ISYIPD
>gnl|CDD|410039 cd12630, RRM2_IGF2BP3, RNA recognition motif 2 (RRM2) found in vertebrate insulin-like growth factor 2 mRNA-binding protein 3 (IGF2BP3). This subgroup corresponds to the RRM2 of IGF2BP3 (IGF2 mRNA-binding protein 3 or IMP-3), also termed KH domain-containing protein overexpressed in cancer (KOC), or VICKZ family member 3, an RNA-binding protein that plays an important role in the differentiation process during early embryogenesis. It is known to bind to and repress the translation of IGF2 leader 3 mRNA. IGF2BP3 also acts as a Glioblastoma-specific proproliferative and proinvasive marker acting through IGF2 resulting in the activation of oncogenic phosphatidylinositol 3-kinase/mitogen-activated protein kinase (PI3K/MAPK) pathways. IGF2BP3 contains four hnRNP K-homology (KH) domains, two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a RGG RNA-binding domain
RKLQIRNIPPHLQWEVLDSLLAQYGTVENCEQVNTDTETAVVNVTYSTKDQARQAIEKLNGFQLENYSLK
VTYIPD
>gnl|CDD|410040 cd12631, RRM1_CELF1_2_Bruno, RNA recognition motif 1 (RRM1) found in CUGBP Elav-like family member CELF-1, CELF-2, Drosophila melanogaster Bruno protein and similar proteins. This subgroup corresponds to the RRM1 of CELF-1, CELF-2 and Bruno protein. CELF-1 (also termed BRUNOL-2, or CUG-BP1, or EDEN-BP) and CELF-2 (also termed BRUNOL-3, or ETR-3, or CUG-BP2, or NAPOR) belong to the CUGBP1 and ETR-3-like factors (CELF) or BRUNOL (Bruno-like) family of RNA-binding proteins that have been implicated in regulation of pre-mRNA splicing, and control of mRNA translation and deadenylation. CELF-1 is strongly expressed in all adult and fetal tissues tested. The human CELF-1 is a nuclear and cytoplasmic RNA-binding protein that regulates multiple aspects of nuclear and cytoplasmic mRNA processing, with implications for onset of type 1 myotonic dystrophy (DM1), a neuromuscular disease associated with an unstable CUG triplet expansion in the 3'-UTR (3'-untranslated region) of the DMPK (myotonic dystrophy protein kinase) gene; it preferentially targets UGU-rich mRNA elements. It has been shown to bind to a Bruno response element, a cis-element involved in translational control of oskar mRNA in Drosophila, and share sequence similarity to Bruno, the Drosophila protein that mediates this process. The Xenopus homolog embryo deadenylation element-binding protein (EDEN-BP) mediates sequence-specific deadenylation of Eg5 mRNA. It binds specifically to the EDEN motif in the 3'-untranslated regions of maternal mRNAs and targets these mRNAs for deadenylation and translational repression. CELF-1 contain three highly conserved RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C-terminus of the protein. The two N-terminal RRMs of EDEN-BP are necessary for the interaction with EDEN as well as a part of the linker region (between RRM2 and RRM3). Oligomerization of EDEN-BP is required for specific mRNA deadenylation and binding. CELF-2 is expressed in all tissues at some level, but highest in brain, heart, and thymus. It has been implicated in the regulation of nuclear and cytoplasmic RNA processing events, including alternative splicing, RNA editing, stability and translation. CELF-2 shares high sequence identity with CELF-1, but shows different binding specificity; it binds preferentially to sequences with UG repeats and UGUU motifs. It has been shown to bind to a Bruno response element, a cis-element involved in translational control of oskar mRNA in Drosophila, and share sequence similarity to Bruno, the Drosophila protein that mediates this process. It also binds to the 3'-UTR of cyclooxygenase-2 messages, affecting both translation and mRNA stability, and binds to apoB mRNA, regulating its C to U editing. CELF-2 also contains three highly conserved RRMs. It binds to RNA via the first two RRMs, which are also important for localization in the cytoplasm. The splicing activation or repression activity of CELF-2 on some specific substrates is mediated by RRM1/RRM2. Both, RRM1 and RRM2 of CELF-2, can activate cardiac troponin T (cTNT) exon 5 inclusion. In addition, CELF-2 possesses a typical arginine and lysine-rich nuclear localization signal (NLS) in the C-terminus, within RRM3. This subgroup also includes Drosophila melanogaster Bruno protein, which plays a central role in regulation of Oskar (Osk) expression in flies. It mediates repression by binding to regulatory Bruno response elements (BREs) in the Osk mRNA 3' UTR. The full-length Bruno protein contains three RRMs, two located in the N-terminal half of the protein and the third near the C-terminus, separated by a linker region
AIKMFVGQIPRSWSEKELRELFEQYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNIKT
LPGMHHPIQMKPAD
>gnl|CDD|410041 cd12632, RRM1_CELF3_4_5_6, RNA recognition motif 1 (RRM1) found in CUGBP Elav-like family member CELF-3, CELF-4, CELF-5, CELF-6 and similar proteins. This subfamily corresponds to the RRM1 of CELF-3, CELF-4, CELF-5, CELF-6, all of which belong to the CUGBP1 and ETR-3-like factors (CELF) or BRUNOL (Bruno-like) family of RNA-binding proteins that display dual nuclear and cytoplasmic localizations and have been implicated in the regulation of pre-mRNA splicing and in the control of mRNA translation and deadenylation. CELF-3, expressed in brain and testis only, is also known as bruno-like protein 1 (BRUNOL-1), or CAG repeat protein 4, or CUG-BP- and ETR-3-like factor 3, or embryonic lethal abnormal vision (ELAV)-type RNA-binding protein 1 (ETR-1), or expanded repeat domain protein CAG/CTG 4, or trinucleotide repeat-containing gene 4 protein (TNRC4). It plays an important role in the pathogenesis of tauopathies. CELF-3 contains three highly conserved RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C-terminus of the protein.The effect of CELF-3 on tau splicing is mediated mainly by the RNA-binding activity of RRM2. The divergent linker region might mediate the interaction of CELF-3 with other proteins regulating its activity or involved in target recognition. CELF-4, highly expressed throughout the brain and in glandular tissues, moderately expressed in heart, skeletal muscle, and liver, is also known as bruno-like protein 4 (BRUNOL-4), or CUG-BP- and ETR-3-like factor 4. Like CELF-3, CELF-4 also contain three highly conserved RRMs. The splicing activation or repression activity of CELF-4 on some specific substrates is mediated by its RRM1/RRM2. On the other hand, both RRM1 and RRM2 of CELF-4 can activate cardiac troponin T (cTNT) exon 5 inclusion. CELF-5, expressed in brain, is also known as bruno-like protein 5 (BRUNOL-5), or CUG-BP- and ETR-3-like factor 5. Although its biological role remains unclear, CELF-5 shares same domain architecture with CELF-3. CELF-6, strongly expressed in kidney, brain, and testis, is also known as bruno-like protein 6 (BRUNOL-6), or CUG-BP- and ETR-3-like factor 6. It activates exon inclusion of a cardiac troponin T minigene in transient transfection assays in an muscle-specific splicing enhancer (MSE)-dependent manner and can activate inclusion via multiple copies of a single element, MSE2. CELF-6 also promotes skipping of exon 11 of insulin receptor, a known target of CELF activity that is expressed in kidney. In additiona to three highly conserved RRMs, CELF-6 also possesses numerous potential phosphorylation sites, a potential nuclear localization signal (NLS) at the C terminus, and an alanine-rich region within the divergent linker region
KDHDAIKLFIGQIPRNLEEKDLRPLFEQFGKIYELTVLKDKYTGMHKGCAFLTYCARESALKAQSALHEQ
KTLPGMNRPIQVKPADS
>gnl|CDD|241077 cd12633, RRM1_FCA, RNA recognition motif 1 (RRM1) found in plant flowering time control protein FCA and similar proteins. This subgroup corresponds to the RRM1 of FCA, a gene controlling flowering time in Arabidopsis, encoding a flowering time control protein that functions in the posttranscriptional regulation of transcripts involved in the flowering process. FCA contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNP (ribonucleoprotein domains), and a WW protein interaction domain
KLFVGSVPRTITEQEVRPMFEEHGNVLEVAIIKDKRTGHQQGCCFVKYSTRDEADRAIRALHNQRTLPGG
ASPVQVRYAD
>gnl|CDD|410042 cd12634, RRM2_CELF1_2, RNA recognition motif 2 (RRM2) found in CUGBP Elav-like family member CELF-1, CELF-2 and similar proteins. This subgroup corresponds to the RRM2 of CELF-1 (also termed BRUNOL-2, or CUG-BP1, or EDEN-BP), CELF-2 (also termed BRUNOL-3, or ETR-3, or CUG-BP2, or NAPOR), both of which belong to the CUGBP1 and ETR-3-like factors (CELF) or BRUNOL (Bruno-like) family of RNA-binding proteins that have been implicated in the regulation of pre-mRNA splicing and in the control of mRNA translation and deadenylation. CELF-1 is strongly expressed in all adult and fetal tissues tested. Human CELF-1 is a nuclear and cytoplasmic RNA-binding protein that regulates multiple aspects of nuclear and cytoplasmic mRNA processing, with implications for onset of type 1 myotonic dystrophy (DM1), a neuromuscular disease associated with an unstable CUG triplet expansion in the 3'-UTR (3'-untranslated region) of the DMPK (myotonic dystrophy protein kinase) gene; it preferentially targets UGU-rich mRNA elements. It has been shown to bind to a Bruno response element, a cis-element involved in translational control of oskar mRNA in Drosophila, and share sequence similarity to Bruno, the Drosophila protein that mediates this process. The Xenopus homolog embryo deadenylation element-binding protein (EDEN-BP) mediates sequence-specific deadenylation of Eg5 mRNA. It binds specifically to the EDEN motif in the 3'-untranslated regions of maternal mRNAs and targets these mRNAs for deadenylation and translational repression. CELF-1 contains three highly conserved RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C-terminus of the protein. The two N-terminal RRMs of EDEN-BP are necessary for the interaction with EDEN as well as a part of the linker region (between RRM2 and RRM3). Oligomerization of EDEN-BP is required for specific mRNA deadenylation and binding. CELF-2 is expressed in all tissues at some level, but highest in brain, heart, and thymus. It has been implicated in the regulation of nuclear and cytoplasmic RNA processing events, including alternative splicing, RNA editing, stability and translation. CELF-2 shares high sequence identity with CELF-1, but shows different binding specificity; it preferentially binds to sequences with UG repeats and UGUU motifs. It has been shown to bind to a Bruno response element, a cis-element involved in translational control of oskar mRNA in Drosophila, and share sequence similarity to Bruno, the Drosophila protein that mediates this process. It also binds to the 3'-UTR of cyclooxygenase-2 messages, affecting both translation and mRNA stability, and binds to apoB mRNA, regulating its C to U editing. CELF-2 also contains three highly conserved RRMs. It binds to RNA via the first two RRMs, which are also important for localization in the cytoplasm. The splicing activation or repression activity of CELF-2 on some specific substrates is mediated by RRM1/RRM2. Both, RRM1 and RRM2 of CELF-2, can activate cardiac troponin T (cTNT) exon 5 inclusion. In addition, CELF-2 possesses a typical arginine and lysine-rich nuclear localization signal (NLS) in the C-terminus, within RRM3
DRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFSTRAMAQNAIKAMHQSQTMEG
CSSPIVVKFAD
>gnl|CDD|410043 cd12635, RRM2_CELF3_4_5_6, RNA recognition motif 2 (RRM2) found in CUGBP Elav-like family member CELF-3, CELF-4, CELF-5, CELF-6 and similar proteins. This subgroup corresponds to the RRM2 of CELF-3, CELF-4, CELF-5, and CELF-6, all of which belong to the CUGBP1 and ETR-3-like factors (CELF) or BRUNOL (Bruno-like) family of RNA-binding proteins that display dual nuclear and cytoplasmic localizations and have been implicated in the regulation of pre-mRNA splicing and in the control of mRNA translation and deadenylation. CELF-3, expressed in brain and testis only, is also known as bruno-like protein 1 (BRUNOL-1), or CAG repeat protein 4, or CUG-BP- and ETR-3-like factor 3, or embryonic lethal abnormal vision (ELAV)-type RNA-binding protein 1 (ETR-1), or expanded repeat domain protein CAG/CTG 4, or trinucleotide repeat-containing gene 4 protein (TNRC4). It plays an important role in the pathogenesis of tauopathies. CELF-3 contains three highly conserved RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C-terminus of the protein. The effect of CELF-3 on tau splicing is mediated mainly by the RNA-binding activity of RRM2. The divergent linker region might mediate the interaction of CELF-3 with other proteins regulating its activity or involved in target recognition. CELF-4, being highly expressed throughout the brain and in glandular tissues, moderately expressed in heart, skeletal muscle, and liver, is also known as bruno-like protein 4 (BRUNOL-4), or CUG-BP- and ETR-3-like factor 4. Like CELF-3, CELF-4 also contain three highly conserved RRMs. The splicing activation or repression activity of CELF-4 on some specific substrates is mediated by its RRM1/RRM2. On the other hand, both RRM1 and RRM2 of CELF-4 can activate cardiac troponin T (cTNT) exon 5 inclusion. CELF-5, expressed in brain, is also known as bruno-like protein 5 (BRUNOL-5), or CUG-BP- and ETR-3-like factor 5. Although its biological role remains unclear, CELF-5 shares same domain architecture with CELF-3. CELF-6, being strongly expressed in kidney, brain, and testis, is also known as bruno-like protein 6 (BRUNOL-6), or CUG-BP- and ETR-3-like factor 6. It activates exon inclusion of a cardiac troponin T minigene in transient transfection assays in a muscle-specific splicing enhancer (MSE)-dependent manner and can activate inclusion via multiple copies of a single element, MSE2. CELF-6 also promotes skipping of exon 11 of insulin receptor, a known target of CELF activity that is expressed in kidney. In addition to three highly conserved RRMs, CELF-6 also possesses numerous potential phosphorylation sites, a potential nuclear localization signal (NLS) at the C terminus, and an alanine-rich region within the divergent linker region
DRKLFVGMLGKQQSEDDVRRLFEPFGSIEECTILRGPDGNSKGCAFVKFSSHAEAQAAINALHGSQTMPG
ASSSLVVKFAD
>gnl|CDD|410044 cd12636, RRM2_Bruno_like, RNA recognition motif 2 (RRM2) found in Drosophila melanogaster Bruno protein and similar proteins. This subgroup corresponds to the RRM2 of Bruno, a Drosophila RNA recognition motif (RRM)-containing protein that plays a central role in regulation of Oskar (Osk) expression. It mediates repression by binding to regulatory Bruno response elements (BREs) in the Osk mRNA 3' UTR. The full-length Bruno protein contains three RRMs, two located in the N-terminal half of the protein and the third near the C-terminus, separated by a linker region
ERKLFVGMLSKKCNESDVRIMFSPYGSIEECTVLRDQNGKSRGCAFVTFTSRQCAVNAIKAMHHSQTMEG
CSSPLVVKFAD
>gnl|CDD|410045 cd12637, RRM2_FCA, RNA recognition motif 2 (RRM2) found in plant flowering time control protein FCA and similar proteins. This subgroup corresponds to the RRM2 of FCA, a gene controlling flowering time in Arabidopsis, which encodes a flowering time control protein that functions in the posttranscriptional regulation of transcripts involved in the flowering process. The flowering time control protein FCA contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNP (ribonucleoprotein domains), and a WW protein interaction domain
KLFVGSLPKTATEQEVRDLFEAYGEVEEVYLMKDPVTQQGTGCAFVKFAYKEEALAAIRSLNGTVTFDGC
SRPVEVRFAES
>gnl|CDD|241082 cd12638, RRM3_CELF1_2, RNA recognition motif 3 (RRM3) found in CUGBP Elav-like family member CELF-1, CELF-2 and similar proteins. This subgroup corresponds to the RRM3 of CELF-1 (also termed BRUNOL-2, or CUG-BP1, or EDEN-BP) and CELF-2 (also termed BRUNOL-3, or ETR-3, or CUG-BP2, or NAPOR), both of which belong to the CUGBP1 and ETR-3-like factors (CELF) or BRUNOL (Bruno-like) family of RNA-binding proteins that have been implicated in the regulation of pre-mRNA splicing and in the control of mRNA translation and deadenylation. CELF-1 is strongly expressed in all adult and fetal tissues tested. Human CELF-1 is a nuclear and cytoplasmic RNA-binding protein that regulates multiple aspects of nuclear and cytoplasmic mRNA processing, with implications for onset of type 1 myotonic dystrophy (DM1), a neuromuscular disease associated with an unstable CUG triplet expansion in the 3'-UTR (3'-untranslated region) of the DMPK (myotonic dystrophy protein kinase) gene; it preferentially targets UGU-rich mRNA elements. It has been shown to bind to a Bruno response element, a cis-element involved in translational control of oskar mRNA in Drosophila, and share sequence similarity to Bruno, the Drosophila protein that mediates this process. The Xenopus homolog embryo deadenylation element-binding protein (EDEN-BP) mediates sequence-specific deadenylation of Eg5 mRNA. It specifically binds to the EDEN motif in the 3'-untranslated regions of maternal mRNAs and targets these mRNAs for deadenylation and translational repression. CELF-1 contain three highly conserved RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C-terminus of the protein. The two N-terminal RRMs of EDEN-BP are necessary for the interaction with EDEN as well as a part of the linker region (between RRM2 and RRM3). Oligomerization of EDEN-BP is required for specific mRNA deadenylation and binding. CELF-2 is expressed in all tissues at some level, but highest in brain, heart, and thymus. It has been implicated in the regulation of nuclear and cytoplasmic RNA processing events, including alternative splicing, RNA editing, stability and translation. CELF-2 shares high sequence identity with CELF-1, but shows different binding specificity; it binds preferentially to sequences with UG repeats and UGUU motifs. It has been shown to bind to a Bruno response element, a cis-element involved in translational control of oskar mRNA in Drosophila, and share sequence similarity to Bruno, the Drosophila protein that mediates this process. It also binds to the 3'-UTR of cyclooxygenase-2 messages, affecting both translation and mRNA stability, and binds to apoB mRNA, regulating its C to U editing. CELF-2 also contain three highly conserved RRMs. It binds to RNA via the first two RRMs, which are important for localization in the cytoplasm. The splicing activation or repression activity of CELF-2 on some specific substrates is mediated by RRM1/RRM2. Both, RRM1 and RRM2 of CELF-2, can activate cardiac troponin T (cTNT) exon 5 inclusion. In addition, CELF-2 possesses a typical arginine and lysine-rich nuclear localization signal (NLS) in the C-terminus, within RRM3
QKEGPEGANLFIYHLPQEFGDQDILQMFMPFGNVVSAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQAMN
GFQIGMKRLKVQLKRSKNDSKP
>gnl|CDD|241083 cd12639, RRM3_CELF3_4_5_6, RNA recognition motif 2 (RRM2) found in CUGBP Elav-like family member CELF-3, CELF-4, CELF-5, CELF-6 and similar proteins. This subgroup corresponds to the RRM3 of CELF-3, CELF-4, CELF-5, and CELF-6, all of which belong to the CUGBP1 and ETR-3-like factors (CELF) or BRUNOL (Bruno-like) family of RNA-binding proteins that display dual nuclear and cytoplasmic localizations and have been implicated in the regulation of pre-mRNA splicing and in the control of mRNA translation and deadenylation. CELF-3, expressed in brain and testis only, is also known as bruno-like protein 1 (BRUNOL-1), or CAG repeat protein 4, or CUG-BP- and ETR-3-like factor 3, or embryonic lethal abnormal vision (ELAV)-type RNA-binding protein 1 (ETR-1), or expanded repeat domain protein CAG/CTG 4, or trinucleotide repeat-containing gene 4 protein (TNRC4). It plays an important role in the pathogenesis of tauopathies. CELF-3 contains three highly conserved RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C-terminus of the protein.The effect of CELF-3 on tau splicing is mediated mainly by the RNA-binding activity of RRM2. The divergent linker region might mediate the interaction of CELF-3 with other proteins regulating its activity or involved in target recognition. CELF-4, highly expressed throughout the brain and in glandular tissues, moderately expressed in heart, skeletal muscle, and liver, is also known as bruno-like protein 4 (BRUNOL-4), or CUG-BP- and ETR-3-like factor 4. Like CELF-3, CELF-4 also contains three highly conserved RRMs. The splicing activation or repression activity of CELF-4 on some specific substrates is mediated by its RRM1/RRM2. Both, RRM1 and RRM2 of CELF-4, can activate cardiac troponin T (cTNT) exon 5 inclusion. CELF-5, expressed in brain, is also known as bruno-like protein 5 (BRUNOL-5), or CUG-BP- and ETR-3-like factor 5. Although its biological role remains unclear, CELF-5 shares same domain architecture with CELF-3. CELF-6, strongly expressed in kidney, brain, and testis, is also known as bruno-like protein 6 (BRUNOL-6), or CUG-BP- and ETR-3-like factor 6. It activates exon inclusion of a cardiac troponin T minigene in transient transfection assays in an muscle-specific splicing enhancer (MSE)-dependent manner and can activate inclusion via multiple copies of a single element, MSE2. CELF-6 also promotes skipping of exon 11 of insulin receptor, a known target of CELF activity that is expressed in kidney. In addition to three highly conserved RRMs, CELF-6 also possesses numerous potential phosphorylation sites, a potential nuclear localization signal (NLS) at the C terminus, and an alanine-rich region within the divergent linker region
GPEGCNLFIYHLPQEFGDAELMQMFLPFGNVISAKVFVDRATNQSKCFGFVSFDNPASAQAAIQAMNGFQ
IGMKRLKVQ
>gnl|CDD|241084 cd12640, RRM3_Bruno_like, RNA recognition motif 3 (RRM3) found in Drosophila melanogaster Bruno protein and similar proteins. This subgroup corresponds to the RRM3 of Bruno protein, a Drosophila RNA recognition motif (RRM)-containing protein that plays a central role in regulation of Oskar (Osk) expression. It mediates repression by binding to regulatory Bruno response elements (BREs) in the Osk mRNA 3' UTR. The full-length Bruno protein contains three RRMs, two located in the N-terminal half of the protein and the third near the C-terminus, separated by a linker region
GPEGCNLFIYHLPQEFTDTDLAQTFLPFGNVISAKVFIDKQTNLSKCFGFVSYDNPDSAQAAIQAMNGFQ
IGTKRLKVQ
>gnl|CDD|410046 cd12641, RRM_TRA2B, RNA recognition motif (RRM) found in Transformer-2 protein homolog beta (TRA-2 beta) and similar proteins. This subgroup corresponds to the RRM of TRA2-beta or TRA-2-beta, also termed splicing factor, arginine/serine-rich 10 (SFRS10), or transformer-2 protein homolog B, a mammalian homolog of Drosophila transformer-2 (Tra2). TRA2-beta is a serine/arginine-rich (SR) protein that controls the pre-mRNA alternative splicing of the calcitonin/calcitonin gene-related peptide (CGRP), the survival motor neuron 1 (SMN1) protein and the tau protein. It contains a well conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), flanked by the N- and C-terminal arginine/serine (RS)-rich regions. TRA2-beta specifically binds to two types of RNA sequences, the CAA and (GAA)2 sequences, through the RRMs in different RNA binding modes
RANPDPNCCLGVFGLSLYTTERDLREVFSKYGPIADVSIVYDQQSRRSRGFAFVYFENVDDAKEAKERAN
GMELDGRRIRVDFSITK
>gnl|CDD|410047 cd12642, RRM_TRA2A, RNA recognition motif (RRM) found in transformer-2 protein homolog alpha (TRA-2 alpha) and similar proteins. This subgroup corresponds to the RRM of TRA2-alpha or TRA-2-alpha, also termed transformer-2 protein homolog A, a mammalian homolog of Drosophila transformer-2 (Tra2). TRA2-alpha is a 40-kDa serine/arginine-rich (SR) protein (SRp40) that specifically binds to gonadotropin-releasing hormone (GnRH) exonic splicing enhancer on exon 4 (ESE4) and is necessary for enhanced GnRH pre-mRNA splicing. It strongly stimulates GnRH intron A excision in a dose-dependent manner. In addition, TRA2-alpha can interact with either 9G8 or SRp30c, which may also be crucial for ESE-dependent GnRH pre-mRNA splicing. TRA2-alpha contains a well conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), flanked by the N- and C-terminal arginine/serine (RS)-rich regions
PDPNTCLGVFGLSLYTTERDLREVFSRYGPLAGVNVVYDQRTGRSRGFAFVYFERIDDSKEAMERANGME
LDGRRIRVDYSITK
>gnl|CDD|410048 cd12643, RRM_CFIm68, RNA recognition motif (RRM) found in pre-mRNA cleavage factor Im 68 kDa subunit (CFIm68 or CPSF6) and similar proteins. This subgroup corresponds to the RRM of CFIm68. Cleavage factor Im (CFIm) is a highly conserved component of the eukaryotic mRNA 3' processing machinery that functions in UGUA-mediated poly(A) site recognition, the regulation of alternative poly(A) site selection, mRNA export, and mRNA splicing. It is a complex composed of a small 25 kDa (CFIm25) subunit and a larger 59/68/72 kDa subunit. Two separate genes, CPSF6 and CPSF7, code for two isoforms of the large subunit, CFIm68 and CFIm59. The family includes CFIm68, also termed cleavage and polyadenylation specificity factor subunit 6 (CPSF6), or cleavage and polyadenylation specificity factor 68 kDa subunit (CPSF68), or protein HPBRII-4/7. CFIm68 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a central proline-rich region, and a C-terminal RS-like domain. The N-terminal RRM of CFIm68 mediates the interaction with CFIm25. It also serves to enhance RNA binding and facilitate RNA looping
ALYVGNLTWWTTDEDLTEALHSIGVNDLLEIKFFENRANGQSKGFALIVVGSEASSRKLMDKLPKKELHG
QNPVVTP
>gnl|CDD|410049 cd12644, RRM_CFIm59, RNA recognition motif (RRM) found in pre-mRNA cleavage factor Im 59 kDa subunit (CFIm59 or CPSF7) and similar proteins. This subgroup corresponds to the RRM of CFIm59. Cleavage factor Im (CFIm) is a highly conserved component of the eukaryotic mRNA 3' processing machinery that functions in UGUA-mediated poly(A) site recognition, the regulation of alternative poly(A) site selection, mRNA export, and mRNA splicing. It is a complex composed of a small 25 kDa (CFIm25) subunit and a larger 59/68/72 kDa subunit. The two separate genes, CPSF6 and CPSF7, code for two isoforms of the large subunit, CFIm68 and CFIm59. The family includes CFIm59, also termed cleavage and polyadenylation specificity factor subunit 6 (CPSF7), or cleavage and polyadenylation specificity factor 59 kDa subunit (CPSF59). CFIm59 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a central proline-rich region, and a C-terminal RS-like domain. The N-terminal RRM of CFIm59 mediates the interaction with CFIm25. It also serves to enhance RNA binding and facilitate RNA looping
RAAVYVGNFSWWTTDQDLINLIRSLGVKDVVELKFAENRANGQSKGYAEVVVASENSVHLLLELLPGKKL
NGEKVDVRLATRQNLSQFEA
>gnl|CDD|241089 cd12645, RRM_SRSF3, RNA recognition motif (RRM) found in vertebrate serine/arginine-rich splicing factor 3 (SRSF3). This subgroup corresponds to the RRM of SRSF3, also termed pre-mRNA-splicing factor SRp20, a splicing regulatory serine/arginine (SR) protein that modulates alternative splicing by interacting with RNA cis-elements in a concentration- and cell differentiation-dependent manner. It is also involved in termination of transcription, alternative RNA polyadenylation, RNA export, and protein translation. SRSF3 is critical for cell proliferation and tumor induction and maintenance. SRSF3 can shuttle between the nucleus and cytoplasm. It contains a single N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal RS domain rich in serine-arginine dipeptides. The RRM domain is involved in RNA binding, and the RS domain has been implicated in protein shuttling and protein-protein interactions
CPLDCKVYVGNLGNNGNKTELERAFGYYGPLRSVWVARNPPGFAFVEFEDPRDAADAVRELDGRTLCGCR
VRVELSNGEKR
>gnl|CDD|410050 cd12646, RRM_SRSF7, RNA recognition motif (RRM) found in vertebrate serine/arginine-rich splicing factor 7 (SRSF7). This subgroup corresponds to the RRM of SRSF7, also termed splicing factor 9G8, is a splicing regulatory serine/arginine (SR) protein that plays a crucial role in both constitutive splicing and alternative splicing of many pre-mRNAs. Its localization and functions are tightly regulated by phosphorylation. SRSF7 is predominantly present in the nuclear and can shuttle between nucleus and cytoplasm. It cooperates with the export protein, Tap/NXF1, helps mRNA export to the cytoplasm, and enhances the expression of unspliced mRNA. SRSF7 inhibits tau E10 inclusion through directly interacting with the proximal downstream intron of E10, a clustering region for frontotemporal dementia with Parkinsonism (FTDP) mutations. SRSF7 contains a single N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a CCHC-type zinc knuckle motif in its median region, and a C-terminal RS domain rich in serine-arginine dipeptides. The RRM domain is involved in RNA binding, and the RS domain has been implicated in protein shuttling and protein-protein interactions
KVYVGNLGTGAGKGELERAFSYYGPLRTVWIARNPPGFAFVEFEDPRDAEDAVRGLDGKVICGSRVRVEL
STGMPRR
>gnl|CDD|410051 cd12647, RRM_UHM_SPF45, RNA recognition motif (RRM) found in UHM domain of 45 kDa-splicing factor (SPF45) and similar proteins. This subgroup corresponds to the RRM of SPF45, also termed RNA-binding motif protein 17 (RBM17), an RNA-binding protein consisting of an unstructured N-terminal region, followed by a G-patch motif and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain) and an Arg-Xaa-Phe sequence motif. SPF45 regulates alternative splicing of the apoptosis regulatory gene FAS (also known as CD95). It induces exon 6 skipping in FAS pre-mRNA through the UHM domain that binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) present in the 3' splice site-recognizing factors U2AF65, SF1 and SF3b155
PSKVVLLRNMVGPGEVDEDLEPEVKEECEKYGKVTKVVIFEIPGAPDDEAVRIFVEFERVESAIKAVVDL
NGRFFGGRTVKASFYDLDRFRRLDL
>gnl|CDD|410052 cd12648, RRM3_UHM_PUF60, RNA recognition motif 3 (RRM3) found in UHM domain of poly(U)-binding-splicing factor PUF60 and similar proteins. This subgroup corresponds to the RRM3 of PUF60, also termed FUSE-binding protein-interacting repressor (FBP-interacting repressor or FIR), or Ro-binding protein 1 (RoBP1), or Siah-binding protein 1 (Siah-BP1), an essential splicing factor that functions as a poly-U RNA-binding protein required to reconstitute splicing in depleted nuclear extracts. Its function is enhanced through interaction with U2 auxiliary factor U2AF65. PUF60 also controls human c-myc gene expression by binding and inhibiting the transcription factor far upstream sequence element (FUSE)-binding-protein (FBP), an activator of c-myc promoters. PUF60 contains two central RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors another RRM and binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) in several nuclear proteins. The research indicates that PUF60 binds FUSE as a dimer, and only the first two RRM domains participate in the single-stranded DNA recognition
SRVMVLRNMVGPEDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGEEEDAEIIVKIFVEFSMPSEAEKAIQ
ALNGRWFGGRKVVAELYDQTRFDNSDLS
>gnl|CDD|241093 cd12649, RRM1_SXL, RNA recognition motif 1 (RRM1) found in Drosophila sex-lethal (SXL) and similar proteins. This subfamily corresponds to the RRM1 of SXL which governs sexual differentiation and X chromosome dosage compensation in Drosophila melanogaster. It induces female-specific alternative splicing of the transformer (tra) pre-mRNA by binding to the tra uridine-rich polypyrimidine tract at the non-sex-specific 3' splice site during the sex-determination process. SXL binds also to its own pre-mRNA and promotes female-specific alternative splicing. SXL contains an N-terminal Gly/Asn-rich domain that may be responsible for the protein-protein interaction, and tandem RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), that show high preference to bind single-stranded, uridine-rich target RNA transcripts
TNLIVNYLPQDLTDREFRALFRAIGPVNTCKIVRDKKTGYSYGFGFVDFTSEEDAQRAIKTLNGLQLQNK
RLKVAYARPGG
>gnl|CDD|410053 cd12650, RRM1_Hu, RNA recognition motif 1 (RRM1) found in the Hu proteins family. This subfamily corresponds to the RRM1 of the Hu proteins family which represents a group of RNA-binding proteins involved in diverse biological processes. Since the Hu proteins share high homology with the Drosophila embryonic lethal abnormal vision (ELAV) protein, the Hu family is sometimes referred to as the ELAV family. Drosophila ELAV is exclusively expressed in neurons and is required for the correct differentiation and survival of neurons in flies. The neuronal members of the Hu family include Hu-antigen B (HuB or ELAV-2 or Hel-N1), Hu-antigen C (HuC or ELAV-3 or PLE21), and Hu-antigen D (HuD or ELAV-4), which play important roles in neuronal differentiation, plasticity and memory. HuB is also expressed in gonads. Hu-antigen R (HuR or ELAV-1 or HuA) is the ubiquitously expressed Hu family member. It has a variety of biological functions mostly related to the regulation of cellular response to DNA damage and other types of stress. HuR has an anti-apoptotic function during early cell stress response. It binds to mRNAs and enhances the expression of several anti-apoptotic proteins, such as p21waf1, p53, and prothymosin alpha. HuR also has pro-apoptotic function by promoting apoptosis when cell death is unavoidable. Furthermore, HuR may be important in muscle differentiation, adipogenesis, suppression of inflammatory response and modulation of gene expression in response to chronic ethanol exposure and amino acid starvation. Hu proteins perform their cytoplasmic and nuclear molecular functions by coordinately regulating functionally related mRNAs. In the cytoplasm, Hu proteins recognize and bind to AU-rich RNA elements (AREs) in the 3' untranslated regions (UTRs) of certain target mRNAs, such as GAP-43, vascular epithelial growth factor (VEGF), the glucose transporter GLUT1, eotaxin and c-fos, and stabilize those ARE-containing mRNAs. They also bind and regulate the translation of some target mRNAs, such as neurofilament M, GLUT1, and p27. In the nucleus, Hu proteins function as regulators of polyadenylation and alternative splicing. Each Hu protein contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an ARE. RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
TNLIVNYLPQNMTQDEIRSLFSSIGEIESCKLIRDKVTGQSLGYGFVNYVDPSDAEKAINTLNGLRLQNK
TIKVSYA
>gnl|CDD|410054 cd12651, RRM2_SXL, RNA recognition motif 2 (RRM2) found in Drosophila sex-lethal (SXL) and similar proteins. This subfamily corresponds to the RRM2 of the sex-lethal protein (SXL) which governs sexual differentiation and X chromosome dosage compensation in Drosophila melanogaster. It induces female-specific alternative splicing of the transformer (tra) pre-mRNA by binding to the tra uridine-rich polypyrimidine tract at the non-sex-specific 3' splice site during the sex-determination process. SXL binds also to its own pre-mRNA and promotes female-specific alternative splicing. SXL contains an N-terminal Gly/Asn-rich domain that may be responsible for the protein-protein interaction, and tandem RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), that show high preference to bind single-stranded, uridine-rich target RNA transcripts
KDTNLYVTNLPRTITEDELDTIFGAYGNIVQKNLLRDKLTGRPRGVAFVRYDKREEAQAAISALNGTIPE
GGTQPLSVRLA
>gnl|CDD|410055 cd12652, RRM2_Hu, RNA recognition motif 2 (RRM2) found in the Hu proteins family. This subfamily corresponds to the RRM2 of Hu proteins family which represents a group of RNA-binding proteins involved in diverse biological processes. Since the Hu proteins share high homology with the Drosophila embryonic lethal abnormal vision (ELAV) protein, the Hu family is sometimes referred to as the ELAV family. Drosophila ELAV is exclusively expressed in neurons and is required for the correct differentiation and survival of neurons in flies. The neuronal members of the Hu family include Hu-antigen B (HuB or ELAV-2 or Hel-N1), Hu-antigen C (HuC or ELAV-3 or PLE21), and Hu-antigen D (HuD or ELAV-4), which play important roles in neuronal differentiation, plasticity and memory. HuB is also expressed in gonads. Hu-antigen R (HuR or ELAV-1 or HuA) is the ubiquitously expressed Hu family member. It has a variety of biological functions mostly related to the regulation of cellular response to DNA damage and other types of stress. Moreover, HuR has an anti-apoptotic function during early cell stress response. It binds to mRNAs and enhances the expression of several anti-apoptotic proteins, such as p21waf1, p53, and prothymosin alpha. HuR also has pro-apoptotic function by promoting apoptosis when cell death is unavoidable. Furthermore, HuR may be important in muscle differentiation, adipogenesis, suppression of inflammatory response and modulation of gene expression in response to chronic ethanol exposure and amino acid starvation. Hu proteins perform their cytoplasmic and nuclear molecular functions by coordinately regulating functionally related mRNAs. In the cytoplasm, Hu proteins recognize and bind to AU-rich RNA elements (AREs) in the 3' untranslated regions (UTRs) of certain target mRNAs, such as GAP-43, vascular epithelial growth factor (VEGF), the glucose transporter GLUT1, eotaxin and c-fos, and stabilize those ARE-containing mRNAs. They also bind and regulate the translation of some target mRNAs, such as neurofilament M, GLUT1, and p27. In the nucleus, Hu proteins function as regulators of polyadenylation and alternative splicing. Each Hu protein contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an ARE. RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
ANLYVSGLPKTMTQKELEQLFSQFGRIITSRILCDNVTGLSRGVGFIRFDKRVEAERAIKALNGTIPPGA
TEPITVKFA
>gnl|CDD|410056 cd12653, RRM3_HuR, RNA recognition motif 3 (RRM3) found in vertebrate Hu-antigen R (HuR). This subgroup corresponds to the RRM3 of HuR, also termed ELAV-like protein 1 (ELAV-1), the ubiquitously expressed Hu family member. It has a variety of biological functions mostly related to the regulation of cellular response to DNA damage and other types of stress. HuR has an anti-apoptotic function during early cell stress response. It binds to mRNAs and enhances the expression of several anti-apoptotic proteins, such as p21waf1, p53, and prothymosin alpha. HuR also has pro-apoptotic function by promoting apoptosis when cell death is unavoidable. Furthermore, HuR may be important in muscle differentiation, adipogenesis, suppression of inflammatory response and modulation of gene expression in response to chronic ethanol exposure and amino acid starvation. Like other Hu proteins, HuR contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an AU-rich RNA element (ARE). RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
SGWCIFIYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAMAIASLNGYRLG
DKILQVSFKTNKSHK
>gnl|CDD|241098 cd12654, RRM3_HuB, RNA recognition motif 3 (RRM3) found in vertebrate Hu-antigen B (HuB). This subgroup corresponds to the RRM3 of HuB, also termed ELAV-like protein 2 (ELAV-2), or ELAV-like neuronal protein 1, or nervous system-specific RNA-binding protein Hel-N1 (Hel-N1), one of the neuronal members of the Hu family. The neuronal Hu proteins play important roles in neuronal differentiation, plasticity and memory. HuB is also expressed in gonads. It is up-regulated during neuronal differentiation of embryonic carcinoma P19 cells. Like other Hu proteins, HuB contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an AU-rich RNA element (ARE). RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
GTGWCIFVYNLAPDADESILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYDEAAMAIASLNGYRL
GDRVLQVSFKTNKTHK
>gnl|CDD|410057 cd12655, RRM3_HuC, RNA recognition motif 3 (RRM3) found in vertebrate Hu-antigen C (HuC). This subgroup corresponds to the RRM3 of HuC, also termed ELAV-like protein 3 (ELAV-3), or paraneoplastic cerebellar degeneration-associated antigen, or paraneoplastic limbic encephalitis antigen 21 (PLE21), one of the neuronal members of the Hu family. The neuronal Hu proteins play important roles in neuronal differentiation, plasticity and memory. Like other Hu proteins, HuC contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an AU-rich RNA element (ARE). The AU-rich element binding of HuC can be inhibited by flavonoids. RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
GWCIFVYNLSPEADESVLWQLFGPFGAVTNVKVIRDFTTNKCKGFGFVTMTNYDEAAMAIASLNGYRLGD
RVLQVSFKTSKQHKA
>gnl|CDD|241100 cd12656, RRM3_HuD, RNA recognition motif 3 (RRM3) found in vertebrate Hu-antigen D (HuD). This subgroup corresponds to the RRM3 of HuD, also termed ELAV-like protein 4 (ELAV-4), or paraneoplastic encephalomyelitis antigen HuD, one of the neuronal members of the Hu family. The neuronal Hu proteins play important roles in neuronal differentiation, plasticity and memory. HuD has been implicated in various aspects of neuronal function, such as the commitment and differentiation of neuronal precursors as well as synaptic remodeling in mature neurons. HuD also functions as an important regulator of mRNA expression in neurons by interacting with AU-rich RNA element (ARE) and stabilizing multiple transcripts. Moreover, HuD regulates the nuclear processing/stability of N-myc pre-mRNA in neuroblastoma cells. And it also regulates the neurite elongation and morphological differentiation. HuD specifically bound poly(A) RNA. Like other Hu proteins, HuD contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an ARE. RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
GTGWCIFVYNLSPDSDESVLWQLFGPFGAVNNVKVIRDFNTNKCKGFGFVTMTNYDEAAMAIASLNGYRL
GDRVLQVSFKTNKTHK
>gnl|CDD|410058 cd12657, RRM1_hnRNPM, RNA recognition motif 1 (RRM1) found in vertebrate heterogeneous nuclear ribonucleoprotein M (hnRNP M). This subgroup corresponds to the RRM1 of hnRNP M, a pre-mRNA binding protein that may play an important role in the pre-mRNA processing. It also preferentially binds to poly(G) and poly(U) RNA homopolymers. Moreover, hnRNP M is able to interact with early spliceosomes, further influencing splicing patterns of specific pre-mRNAs. hnRNP M functions as the receptor of carcinoembryonic antigen (CEA) that contains the penta-peptide sequence PELPK signaling motif. In addition, hnRNP M and another splicing factor Nova-1 work together as dopamine D2 receptor (D2R) pre-mRNA-binding proteins. They regulate alternative splicing of D2R pre-mRNA in an antagonistic manner. hnRNP M contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and an unusual hexapeptide-repeat region rich in methionine and arginine residues (MR repeat motif)
RVFISNIPFDVKWQTLKDLVKEKVGEVTYVELLMDAEGKSRGCAVVEFKTEESMKKAVEVLNKHSFNGRP
LKVKED
>gnl|CDD|410059 cd12658, RRM1_MYEF2, RNA recognition motif 1 (RRM1) found in vertebrate myelin expression factor 2 (MEF-2). This subgroup corresponds to the RRM1 of MEF-2, also termed MyEF-2 or MST156, a sequence-specific single-stranded DNA (ssDNA) binding protein that binds specifically to ssDNA derived from the proximal (MB1) element of the myelin basic protein (MBP) promoter and represses transcription of the MBP gene. MEF-2 contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which may be responsible for its ssDNA binding activity
RVFISNIPYDMKWQAIKDLMREKVGEVTYVELFKDAEGKSRGCGVVEFKDEEFVKKALEVMNKYDLSGRP
LNIKED
>gnl|CDD|410060 cd12659, RRM2_hnRNPM, RNA recognition motif 2 (RRM2) found in vertebrate heterogeneous nuclear ribonucleoprotein M (hnRNP M). This subgroup corresponds to the RRM2 of hnRNP M, a pre-mRNA binding protein that may play an important role in the pre-mRNA processing. It also preferentially binds to poly(G) and poly(U) RNA homopolymers. hnRNP M is able to interact with early spliceosomes, further influencing splicing patterns of specific pre-mRNAs. It functions as the receptor of carcinoembryonic antigen (CEA) that contains the penta-peptide sequence PELPK signaling motif. In addition, hnRNP M and another splicing factor Nova-1 work together as dopamine D2 receptor (D2R) pre-mRNA-binding proteins. They regulate alternative splicing of D2R pre-mRNA in an antagonistic manner. hnRNP M contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and an unusual hexapeptide-repeat region rich in methionine and arginine residues (MR repeat motif)
STVFVANLDYKVGWKKLKEVFSMAGVVVRADILEDKDGKSRGIGTVTFEQPIEAVQAISMFNGQLLFDRP
MHVKMD
>gnl|CDD|410061 cd12660, RRM2_MYEF2, RNA recognition motif 2 (RRM2) found in vertebrate myelin expression factor 2 (MEF-2). This subgroup corresponds to the RRM2 of MEF-2, also termed MyEF-2 or MST156, a sequence-specific single-stranded DNA (ssDNA) binding protein that binds specifically to ssDNA derived from the proximal (MB1) element of the myelin basic protein (MBP) promoter and represses transcription of the MBP gene. MEF-2 contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which may be responsible for its ssDNA binding activity
TTIFVANLDFKVGWKKLKEVFSMAGTVKRADIKEDKDGKSRGMGTVTFEQAIEAVQAISMFNGQFLFDRP
MHVKMD
>gnl|CDD|410062 cd12661, RRM3_hnRNPM, RNA recognition motif 3 (RRM3) found in vertebrate heterogeneous nuclear ribonucleoprotein M (hnRNP M). This subgroup corresponds to the RRM3 of hnRNP M, a pre-mRNA binding protein that may play an important role in the pre-mRNA processing. It also preferentially binds to poly(G) and poly(U) RNA homopolymers. Moreover, hnRNP M is able to interact with early spliceosomes, further influencing splicing patterns of specific pre-mRNAs. hnRNP M functions as the receptor of carcinoembryonic antigen (CEA) that contains the penta-peptide sequence PELPK signaling motif. In addition, hnRNP M and another splicing factor Nova-1 work together as dopamine D2 receptor (D2R) pre-mRNA-binding proteins. They regulate alternative splicing of D2R pre-mRNA in an antagonistic manner. hnRNP M contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and an unusual hexapeptide-repeat region rich in methionine and arginine residues (MR repeat motif)
QIFVRNLPFDFTWKMLKDKFNECGHVLYADIKMENGKSKGCGVVRFESPEVAERACRMMNGIKLNGREID
VRIDRNA
>gnl|CDD|410063 cd12662, RRM3_MYEF2, RNA recognition motif 3 (RRM3) found in vertebrate myelin expression factor 2 (MEF-2). This subgroup corresponds to the RRM3 of MEF-2, also termed MyEF-2 or MST156, a sequence-specific single-stranded DNA (ssDNA) binding protein that binds specifically to ssDNA derived from the proximal (MB1) element of the myelin basic protein (MBP) promoter and represses transcription of the MBP gene. MEF-2 contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which may be responsible for its ssDNA binding activity
QIFVRNLPFDLTWQKLKEKFSQCGHVMFAEIKMENGKSKGCGTVRFDSPESAEKACRLMNGIKISGREID
VRLDRNA
>gnl|CDD|410064 cd12663, RRM1_RAVER1, RNA recognition motif 1 (RRM1) found in vertebrate ribonucleoprotein PTB-binding 1 (raver-1). This subgroup corresponds to the RRM1 of raver-1, a ubiquitously expressed heterogeneous nuclear ribonucleoprotein (hnRNP) that serves as a co-repressor of the nucleoplasmic splicing repressor polypyrimidine tract-binding protein (PTB)-directed splicing of select mRNAs. It shuttles between the cytoplasm and the nucleus and can accumulate in the perinucleolar compartment, a dynamic nuclear substructure that harbors PTB. Raver-1 also modulates focal adhesion assembly by binding to the cytoskeletal proteins, including alpha-actinin, vinculin, and metavinculin (an alternatively spliced isoform of vinculin) at adhesion complexes, particularly in differentiated muscle tissue. Raver-1 contains three N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two putative nuclear localization signals (NLS) at the N- and C-termini, a central leucine-rich region, and a C-terminal region harboring two PTB-binding [SG][IL]LGxxP motifs. Raver1 binds to PTB through the PTB-binding motifs at its C-terminal half, and binds to other partners, such as RNA having the sequence UCAUGCAGUCUG, through its N-terminal RRMs. Interestingly, the 12-nucleotide RNA having the sequence UCAUGCAGUCUG with micromolar affinity is found in vinculin mRNA. Additional research indicates that the RRM1 of raver-1 directs its interaction with the tail domain of activated vinculin. Then the raver1/vinculin tail (Vt) complex binds to vinculin mRNA, which is permissive for vinculin binding to F-actin
RKILIRGLPGDVTNQEVHDLLSDYELKYCFVDKYKGTAFVTLLNGEQAEAAINAFHQSRLRERELSVQLQ
P
>gnl|CDD|410065 cd12664, RRM1_RAVER2, RNA recognition motif 1 (RRM1) found in vertebrate ribonucleoprotein PTB-binding 2 (raver-2). This subgroup corresponds to the RRM1 of raver-2, a novel member of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. It is present in vertebrates and shows high sequence homology to raver-1, a ubiquitously expressed co-repressor of the nucleoplasmic splicing repressor polypyrimidine tract-binding protein (PTB)-directed splicing of select mRNAs. In contrast, raver-2 exerts a distinct spatio-temporal expression pattern during embryogenesis and is mainly limited to differentiated neurons and glia cells. Although it displays nucleo-cytoplasmic shuttling in heterokaryons, raver2 localizes to the nucleus in glia cells and neurons. Raver-2 can interact with PTB and may participate in PTB-mediated RNA-processing. However, there is no evidence indicating that raver-2 can bind to cytoplasmic proteins. Raver-2 contains three N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two putative nuclear localization signals (NLS) at the N- and C-termini, a central leucine-rich region, and a C-terminal region harboring two [SG][IL]LGxxP motifs. Raver-2 binds to PTB through the SLLGEPP motif only, and binds to RNA through its RRMs
KILIKNLPQDSTSQEVHDLLKDYELKYCYVDRNKRTAFVTLLNGEQAQDAIRTFHQHSLRGRDISVQLQP
>gnl|CDD|410066 cd12665, RRM2_RAVER1, RNA recognition motif 2 (RRM2) found found in vertebrate ribonucleoprotein PTB-binding 1 (raver-1). This subgroup corresponds to the RRM2 of raver-1, a ubiquitously expressed heterogeneous nuclear ribonucleoprotein (hnRNP) that serves as a co-repressor of the nucleoplasmic splicing repressor polypyrimidine tract-binding protein (PTB)-directed splicing of select mRNAs. It shuttles between the cytoplasm and the nucleus and can accumulate in the perinucleolar compartment, a dynamic nuclear substructure that harbors PTB. Raver-1 also modulates focal adhesion assembly by binding to the cytoskeletal proteins, including alpha-actinin, vinculin, and metavinculin (an alternatively spliced isoform of vinculin) at adhesion complexes, particularly in differentiated muscle tissue. Raver-1 contains three N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two putative nuclear localization signals (NLS) at the N- and C-termini, a central leucine-rich region, and a C-terminal region harboring two PTB-binding [SG][IL]LGxxP motifs. Raver1 binds to PTB through the PTB-binding motifs at its C-terminal half, and binds to other partners, such as RNA having the sequence UCAUGCAGUCUG, through its N-terminal RRMs. Interestingly, the 12-nucleotide RNA having the sequence UCAUGCAGUCUG with micromolar affinity is found in vinculin mRNA. Additional research indicates that the RRM1 of raver-1 directs its interaction with the tail domain of activated vinculin. Then the raver1/vinculin tail (Vt) complex binds to vinculin mRNA, which is permissive for vinculin binding to F-actin
LLCIANLPPSYTQQQFEELVRPFGNLERCFLVYSETTGHSKGYGFVEYMKKDSAARAKSDLLGKQLGTRT
LYVHWTD
>gnl|CDD|410067 cd12666, RRM2_RAVER2, RNA recognition motif 2 (RRM2) found in vertebrate ribonucleoprotein PTB-binding 2 (raver-2). This subgroup corresponds to the RRM2 of raver-2, a novel member of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. It is present in vertebrates and shows high sequence homology to raver-1, a ubiquitously expressed co-repressor of the nucleoplasmic splicing repressor polypyrimidine tract-binding protein (PTB)-directed splicing of select mRNAs. In contrast, raver-2 exerts a distinct spatio-temporal expression pattern during embryogenesis and is mainly limited to differentiated neurons and glia cells. Although it displays nucleo-cytoplasmic shuttling in heterokaryons, raver2 localizes to the nucleus in glia cells and neurons. Raver-2 can interact with PTB and may participate in PTB-mediated RNA-processing. However, there is no evidence indicating that raver-2 can bind to cytoplasmic proteins. Raver-2 contains three N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two putative nuclear localization signals (NLS) at the N- and C-termini, a central leucine-rich region, and a C-terminal region harboring two [SG][IL]LGxxP motifs. Raver-2 binds to PTB through the SLLGEPP motif only, and binds to RNA through its RRMs
LLCITNLPISFTLQEFEELVRAYGNIERCFLVYSEVTGHSKGYGFVEYMKKDSAAKARLELLGKQLGESS
LFAQWMD
>gnl|CDD|410068 cd12667, RRM3_RAVER1, RNA recognition motif 3 (RRM3) found in vertebrate ribonucleoprotein PTB-binding 1 (raver-1). This subgroup corresponds to the RRM3 of raver-1, a ubiquitously expressed heterogeneous nuclear ribonucleoprotein (hnRNP) that serves as a co-repressor of the nucleoplasmic splicing repressor polypyrimidine tract-binding protein (PTB)-directed splicing of select mRNAs. It shuttles between the cytoplasm and the nucleus and can accumulate in the perinucleolar compartment, a dynamic nuclear substructure that harbors PTB. Raver-1 also modulates focal adhesion assembly by binding to the cytoskeletal proteins, including alpha-actinin, vinculin, and metavinculin (an alternatively spliced isoform of vinculin) at adhesion complexes, particularly in differentiated muscle tissue. Raver-1 contains three N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two putative nuclear localization signals (NLS) at the N- and C-termini, a central leucine-rich region, and a C-terminal region harboring two PTB-binding [SG][IL]LGxxP motifs. Raver1 binds to PTB through the PTB-binding motifs at its C-terminal half, and binds to other partners, such as RNA having the sequence UCAUGCAGUCUG, through its N-terminal RRMs. Interestingly, the 12-nucleotide RNA having the sequence UCAUGCAGUCUG with micromolar affinity is found in vinculin mRNA. Additional research indicates that the RRM1 of raver-1 directs its interaction with the tail domain of activated vinculin. Then the raver1/vinculin tail (Vt) complex binds to vinculin mRNA, which is permissive for vinculin binding to F-actin
HSRCLCVDRLPPGFNDLDDLRRALSAVHAPTFCQLAYGQDGQLKGFAVLEYETAEMAEMVQQQADGLSLG
GSHIRVSFCAPGPPGRSMLAAL
>gnl|CDD|410069 cd12668, RRM3_RAVER2, RNA recognition motif 3 (RRM3) found found in vertebrate ribonucleoprotein PTB-binding 2 (raver-2). This subgroup corresponds to the RRM3 of raver-2, a novel member of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. It is present in vertebrates and shows high sequence homology to raver-1, a ubiquitously expressed co-repressor of the nucleoplasmic splicing repressor polypyrimidine tract-binding protein (PTB)-directed splicing of select mRNAs. In contrast, raver-2 exerts a distinct spatio-temporal expression pattern during embryogenesis and is mainly limited to differentiated neurons and glia cells. Although it displays nucleo-cytoplasmic shuttling in heterokaryons, raver2 localizes to the nucleus in glia cells and neurons. Raver-2 can interact with PTB and may participate in PTB-mediated RNA-processing. However, there is no evidence indicating that raver-2 can bind to cytoplasmic proteins. Raver-2 contains three N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two putative nuclear localization signals (NLS) at the N- and C-termini, a central leucine-rich region, and a C-terminal region harboring two [SG][IL]LGxxP motifs. Raver-2 binds to PTB through the SLLGEPP motif only, and binds to RNA through its RRMs
HSKCLCVDKLPKDYSDSEELTQLFSRPYKPVFCQLAQDEGSCIGGFAVVEYETAEQAEEVQRAMDGMTIG
GSRVQVSFCAPGSPGRSTLAALIAAQGM
>gnl|CDD|410070 cd12669, RRM1_Nop12p_like, RNA recognition motif 1 (RRM1) found in yeast nucleolar protein 12 (Nop12p) and similar proteins. This subgroup corresponds to the RRM1 of Nop12p which is encoded by YOL041C from Saccharomyces cerevisiae. It is a novel nucleolar protein required for pre-25S rRNA processing and normal rates of cell growth at low temperatures. Nop12p shares high sequence similarity with nucleolar protein 13 (Nop13p). Both, Nop12p and Nop13p, are not essential for growth. However, unlike Nop13p that localizes primarily to the nucleolus but also present in the nucleoplasm to a lesser extent, Nop12p is localized to the nucleolus. Nop12p contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
RTIFVGNLPAEVVTSKSVYKNFKKLFNQFGKIQSIRFRSISFSDALPRKVAFIQKKFHSSRDTVNAYIVF
KEQSSAKSALSLNGTVFMDRHLRVDSVAHP
>gnl|CDD|410071 cd12670, RRM2_Nop12p_like, RNA recognition motif 2 (RRM2) found in yeast nucleolar protein 12 (Nop12p) and similar proteins. This subgroup corresponds to the RRM2 of Nop12p, which is encoded by YOL041C from Saccharomyces cerevisiae. It is a novel nucleolar protein required for pre-25S rRNA processing and normal rates of cell growth at low temperatures. Nop12p shares high sequence similarity with nucleolar protein 13 (Nop13p). Both, Nop12p and Nop13p, are not essential for growth. However, unlike Nop13p that localizes primarily to the nucleolus but is also present in the nucleoplasm to a lesser extent, Nop12p is localized to the nucleolus. Nop12p contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
CVFVGNLAFEAEEEGLWRYFGKCGAIESVRIVRDPKTNVGKGFAYVQFKDENAVEKALLLNEKPTMKGRK
LRVSRAK
>gnl|CDD|410072 cd12671, RRM_CSTF2_CSTF2T, RNA recognition motif (RRM) found in cleavage stimulation factor subunit 2 (CSTF2), cleavage stimulation factor subunit 2 tau variant (CSTF2T) and similar proteins. This subgroup corresponds to the RRM domain of CSTF2, its tau variant and eukaryotic homologs. CSTF2, also termed cleavage stimulation factor 64 kDa subunit (CstF64), is the vertebrate conterpart of yeast mRNA 3'-end-processing protein RNA15. It is expressed in all somatic tissues and is one of three cleavage stimulatory factor (CstF) subunits required for polyadenylation. CstF64 contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a CstF77-binding domain, a repeated MEARA helical region and a conserved C-terminal domain reported to bind the transcription factor PC-4. During polyadenylation, CstF interacts with the pre-mRNA through the RRM of CstF64 at U- or GU-rich sequences within 10 to 30 nucleotides downstream of the cleavage site. CSTF2T, also termed tauCstF64, is a paralog of the X-linked cleavage stimulation factor CstF64 protein that supports polyadenylation in most somatic cells. It is expressed during meiosis and subsequent haploid differentiation in a more limited set of tissues and cell types, largely in meiotic and postmeiotic male germ cells, and to a lesser extent in brain. The loss of CSTF2T will cause male infertility, as it is necessary for spermatogenesis and fertilization. Moreover, CSTF2T is required for expression of genes involved in morphological differentiation of spermatids, as well as for genes having products that function during interaction of motile spermatozoa with eggs. It promotes germ cell-specific patterns of polyadenylation by using its RRM to bind to different sequence elements downstream of polyadenylation sites than does CstF64
ASDRSLRSVFVGNIPYEATEEQLKDIFSEVGPVVSFRLVYDRETGKPKGYGFCEYQDQETALSAMRNLNG
YELNGRALRVDNAAS
>gnl|CDD|410073 cd12672, RRM_DAZL, RNA recognition motif (RRM) found in vertebrate deleted in azoospermia-like (DAZL) proteins. This subgroup corresponds to the RRM of DAZL, also termed SPGY-like-autosomal, encoded by the autosomal homolog of DAZ gene, DAZL. It is ancestral to the deleted in azoospermia (DAZ) protein. DAZL is germ-cell-specific RNA-binding protein that contains a RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a DAZ motif, a protein-protein interaction domain. Although their specific biochemical functions remain to be investigated, DAZL proteins may interact with poly(A)-binding proteins (PABPs), and act as translational activators of specific mRNAs during gametogenesis
GKIMPNTVFVGGIDIRMDENEIRSFFARYGSVKEVKIITDRTGVSKGYGFVSFYDDVDIQKIVESQINFH
GKKLKLGPAIRK
>gnl|CDD|410074 cd12673, RRM_BOULE, RNA recognition motif (RRM) found in protein BOULE. This subgroup corresponds to the RRM of BOULE, the founder member of the human DAZ gene family. Invertebrates contain a single BOULE, while vertebrates, other than catarrhine primates, possess both BOULE and DAZL genes. The catarrhine primates possess BOULE, DAZL, and DAZ genes. BOULE encodes an RNA-binding protein containing an RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a single copy of the DAZ motif. Although its specific biochemical functions remains to be investigated, BOULE protein may interact with poly(A)-binding proteins (PABPs), and act as translational activators of specific mRNAs during gametogenesis
IPNRIFVGGIDFKTNENDLRKFFAQYGSVKEVKIVNDRAGVSKGYGFITFETQEDAQKILQEAEKLNYKD
KKLNIGPAIRK
>gnl|CDD|410075 cd12674, RRM1_Nop4p, RNA recognition motif 1 (RRM1) found in yeast nucleolar protein 4 (Nop4p) and similar proteins. This subgroup corresponds to the RRM1 of Nop4p (also known as Nop77p), encoded by YPL043W from Saccharomyces cerevisiae. It is an essential nucleolar protein involved in processing and maturation of 27S pre-rRNA and biogenesis of 60S ribosomal subunits. Nop4p has four RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
TTLFVRNLPFDVTLESLTDFFSDIGPVKHAVVVTDPETKKSRGYGFVSFSTHDDAEEALAKLKNRKLSGH
ILKLDFAKPR
>gnl|CDD|410076 cd12675, RRM2_Nop4p, RNA recognition motif 2 (RRM2) found in yeast nucleolar protein 4 (Nop4p) and similar proteins. This subgroup corresponds to the RRM2 of Nop4p (also known as Nop77p), encoded by YPL043W from Saccharomyces cerevisiae. It is an essential nucleolar protein involved in processing and maturation of 27S pre-rRNA and biogenesis of 60S ribosomal subunits. Nop4p has four RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
PKLIIRNLPWSIKKPVHLKKLFGRYGKVVEATIPRKKGGKLSGFAFVTMKGRKNAEEALESVNGLEIDGR
PVAVDWAVSKNTW
>gnl|CDD|410077 cd12676, RRM3_Nop4p, RNA recognition motif 3 (RRM3) found in yeast nucleolar protein 4 (Nop4p) and similar proteins. This subgroup corresponds to the RRM3 of Nop4p (also known as Nop77p), encoded by YPL043W from Saccharomyces cerevisiae. It is an essential nucleolar protein involved in processing and maturation of 27S pre-rRNA and biogenesis of 60S ribosomal subunits. Nop4p has four RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
GRTLFVRNLPFDATEDELYSHFSQFGPLKYARVVKDPATGRSKGTAFVKFKNKEDADNCLSAAPEAQSTS
LLEKYSLEQDITDDVSAKFTLDGRVLQVTPAVSREEA
>gnl|CDD|410078 cd12677, RRM4_Nop4p, RNA recognition motif 4 (RRM4) found in yeast nucleolar protein 4 (Nop4p) and similar proteins. This subgroup corresponds to the RRM4 of Nop4p (also known as Nop77p), encoded by YPL043W from Saccharomyces cerevisiae. It is an essential nucleolar protein involved in processing and maturation of 27S pre-rRNA and biogenesis of 60S ribosomal subunits. Nop4p has four RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
HLSLTRLSIRNIPRHVTDKDLKALARKAIVGFATEVKEGLRAPLTKEELARDGDEMDEAEQKKKKKKSGV
VRQAKIIFEKAGGGAGRSRGYGFIEYYTHRDALMGLRWLNGHAVTSKKIEEEYKEEMKDEIENDPGKDRK
KRLIVEFAIENIQVVKRR
>gnl|CDD|410079 cd12678, RRM_SLTM, RNA recognition motif (RRM) found in Scaffold attachment factor (SAF)-like transcription modulator (SLTM) and similar proteins. This subgroup corresponds to the RRM domain of SLTM, also termed modulator of estrogen-induced transcription, which shares high sequence similarity with scaffold attachment factor B1 (SAFB1). It contains a scaffold attachment factor-box (SAF-box, also known as SAP domain) DNA-binding motif, an RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a region rich in glutamine and arginine residues. To a large extent, SLTM co-localizes with SAFB1 in the nucleus, which suggests that they share similar functions, such as the inhibition of an oestrogen reporter gene. However, rather than mediating a specific inhibitory effect on oestrogen action, SLTM is shown to exert a generalized inhibitory effect on gene expression associated with induction of apoptosis in a wide range of cell lines
NLWVSGLSSNTKAADLKNLFGKYGKVLSAKVVTNARSPGAKCYGIVTMSSSTEVARCISHLHRTELHGQQ
ISVE
>gnl|CDD|410080 cd12679, RRM_SAFB1_SAFB2, RNA recognition motif (RRM) found in scaffold attachment factor B1 (SAFB1), scaffold attachment factor B2 (SAFB2), and similar proteins. This subgroup corresponds to RRM of SAFB1, also termed scaffold attachment factor B (SAF-B), heat-shock protein 27 estrogen response element ERE and TATA-box-binding protein (HET), or heterogeneous nuclear ribonucleoprotein hnRNP A1- associated protein (HAP), a large multi-domain protein with well-described functions in transcriptional repression, RNA splicing and metabolism, and a proposed role in chromatin organization. Based on the numerous functions, SAFB1 has been implicated in many diverse cellular processes including cell growth and transformation, stress response, and apoptosis. SAFB1 specifically binds to AT-rich scaffold or matrix attachment region DNA elements (S/MAR DNA) by using its N-terminal scaffold attachment factor-box (SAF-box, also known as SAP domain), a homeodomain-like DNA binding motif. The central region of SAFB1 is composed of an RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a nuclear localization signal (NLS). The C-terminus of SAFB1 contains Glu/Arg- and Gly-rich regions that might be involved in protein-protein interaction. Additional studies indicate that the C-terminal region contains a potent and transferable transcriptional repression domain. Another family member is SAFB2, a homolog of SAFB1. Both SAFB1 and SAFB2 are ubiquitously coexpressed and share very high sequence similarity, suggesting that they might function in a similar manner. However, unlike SAFB1, exclusively existing in the nucleus, SAFB2 is also present in the cytoplasm. The additional cytoplasmic localization of SAFB2 implies that it could play additional roles in the cytoplasmic compartment which are distinct from the nuclear functions shared with SAFB1
GRNLWVSGLSSTTRATDLKNLFSKYGKVVGAKVVTNARSPGARCYGFVTMSTSEEATKCISHLHRTELHG
RMISVE
>gnl|CDD|410081 cd12680, RRM_THOC4, RNA recognition motif (RRM) found in THO complex subunit 4 (THOC4) and similar proteins. This subgroup corresponds to the RRM of THOC4, also termed transcriptional coactivator Aly/REF, or ally of AML-1 and LEF-1, or bZIP-enhancing factor BEF, an mRNA transporter protein with a well conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). It is involved in RNA transportation from the nucleus. THOC4 was initially identified as a transcription coactivator of LEF-1 and AML-1 for the TCRalpha enhancer function. In addition, THOC4 specifically binds to rhesus (RH) promoter in erythroid. It might be a novel transcription cofactor for erythroid-specific genes
TKLLVSNLDFGVSDADIKELFAEFGTLKKAAVHYDRSGRSLGTAEVVFERRADALKAMKQYNGVPLDGRP
MKIQL
>gnl|CDD|410082 cd12681, RRM_SKAR, RNA recognition motif (RRM) found in S6K1 Aly/REF-like target (SKAR) and similar proteins. This subgroup corresponds to the RRM of SKAR, also termed polymerase delta-interacting protein 3 (PDIP3), 46 kDa DNA polymerase delta interaction protein (PDIP46), belonging to the Aly/REF family of RNA binding proteins that have been implicated in coupling transcription with pre-mRNA splicing and nucleo-cytoplasmic mRNA transport. SKAR is widely expressed and localizes to the nucleus. It may be a critical player in the function of S6K1 in cell and organism growth control by binding the activated, hyperphosphorylated form of S6K1 but not S6K2. Furthermore, SKAR functions as a protein partner of the p50 subunit of DNA polymerase delta. In addition, SKAR may have particular importance in pancreatic beta cell size determination and insulin secretion. SKAR contains a well conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
TRLTVSNLHPSVTEDDIVELFSVIGALKRARLVRPGVAEVVYVRREDAITAIKKYNNRELDGQPMKCKL
>gnl|CDD|410083 cd12682, RRM_RBPMS, RNA recognition motif (RRM) found in vertebrate RNA-binding protein with multiple splicing (RBP-MS). This subfamily corresponds to the RRM of RBP-MS, also termed heart and RRM expressed sequence (hermes), an RNA-binding proteins found in various vertebrate species. It contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). RBP-MS physically interacts with Smad2, Smad3 and Smad4 and plays a role in regulation of Smad-mediated transcriptional activity. In addition, RBP-MS may be involved in regulation of mRNA translation and localization during Xenopus laevis development
VRTLFVSGLPLDIKPRELYLLFRPFKGYEGSLIKLTSKQPVGFVSFDSRSEAEAAKNALNGIRFDPEIPQ
TLRLEF
>gnl|CDD|410084 cd12683, RRM_RBPMS2, RNA recognition motif (RRM) found in vertebrate RNA-binding protein with multiple splicing 2 (RBP-MS2). This subfamily corresponds to the RRM of RBP-MS2, encoded by RBPMS2 gene, a paralog of RNA-binding protein with multiple splicing (RBP-MS). The biological function of RBP-MS2 remains unclear. Like RBP-MS, RBP-MS2 contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
VRTLFVSGLPVDIKPRELYLLFRPFKGYEGSLIKLTSKQPVGFVTFDSRAGAEAAKNALNGIRFDPENPQ
TLRLEF
>gnl|CDD|410085 cd12684, RRM_cpo, RNA recognition motif (RRM) found in Drosophila couch potato (cpo) coding RNA-binding protein and similar proteins. This subfamily corresponds to the RRM of Cpo, an RNA-binding protein encoded by Drosophila couch potato (cpo) gene. Cpo contains a well conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). It may control the processing of RNA molecules required for the proper functioning of the peripheral nervous system (PNS)
VRTLFVSGLPMDAKPRELYLLFRAYKGYEGSLLKVTSKNGKTTSPVGFVTFLSRQAAEAAKQDLQGVRFD
PDLPQTLRLEFAK
>gnl|CDD|410086 cd12685, RRM_RBM20, RNA recognition motif (RRM) found in vertebrate RNA-binding protein 20 (RBM20). This subfamily corresponds to the RRM of RBM20, an alternative splicing regulator associated with dilated cardiomyopathy (DCM). It contains only one copy of RNA-recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
RVVHICNLPEGSCTENDVINLGLPFGKVTNYILMRSTNQAFLEMAYTEAAQAMVQYYQEKPAMINEEKLL
IRMSKR
>gnl|CDD|410087 cd12686, RRM1_PTBPH1_PTBPH2, RNA recognition motif 1 (RRM1) found in plant polypyrimidine tract-binding protein homolog 1 and 2 (PTBPH1 and PTBPH2). This subfamily corresponds to the RRM1 of PTBPH1 and PTBPH2. Although their biological roles remain unclear, PTBPH1 and PTBPH2 show significant sequence similarity to polypyrimidine tract binding protein (PTB) that is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. Both, PTBPH1 and PTBPH2, contain three RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
PSKVLHLRNLPWECTEEELIELCKPFGTVVNTKCNVGANKNQAFVEFADLNQAISMVSYYASSSEPAQVR
GKTVYLQYSNR
>gnl|CDD|410088 cd12687, RRM1_PTBPH3, RNA recognition motif 1 (RRM1) found in plant polypyrimidine tract-binding protein homolog 3 (PTBPH3). This subfamily corresponds to the RRM1 of PTBPH3. Although its biological roles remain unclear, PTBPH3 shows significant sequence similarity to polypyrimidine tract binding protein (PTB) that is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. Like PTB, PTBPH3 contains four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
KVLHVRNVGHEISENDLLQLAQPFGVVTKLVMLRAKNQALLQMQDVSAAISALQFYTSVQPSIRGRNVYI
QFSSH
>gnl|CDD|410089 cd12688, RRM1_PTBP1_like, RNA recognition motif 1 (RRM1) found in polypyrimidine tract-binding protein 1 (PTB or hnRNP I) and similar proteins. This subfamily corresponds to the RRM1 of polypyrimidine tract-binding protein 1 (PTB or hnRNP I), polypyrimidine tract-binding protein 2 (PTBP2 or nPTB), regulator of differentiation 1 (Rod1), and similar proteins found in Metazoa. PTB is an important negative regulator of alternative splicing in mammalian cells and functions at several aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. PTBP2 is highly homologous to PTB and is perhaps specific to the vertebrates. Unlike PTB, PTBP2 is enriched in the brain and in some neural cell lines. It binds more stably to the downstream control sequence (DCS) RNA than PTB does but is a weaker repressor of splicing in vitro. PTBP2 also greatly enhances the binding of two other proteins, heterogeneous nuclear ribonucleoprotein (hnRNP) H and KH-type splicing-regulatory protein (KSRP), to the DCS RNA. The binding properties of PTBP2 and its reduced inhibitory activity on splicing imply roles in controlling the assembly of other splicing-regulatory proteins. PTBP2 also contains four RRMs. ROD1 coding protein Rod1 is a mammalian PTB homolog of a regulator of differentiation in the fission yeast Schizosaccharomyces pombe, where the nrd1 gene encodes an RNA binding protein and negatively regulates the onset of differentiation. ROD1 is predominantly expressed in hematopoietic cells or organs. It may play a role controlling differentiation in mammals. All members in this family contain four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
RVLHIRKLPCDVTEAEVISLGLPFGKVTNLLMLKGKNQAFLEMATEEAAVTMVNYYTPVTPHLRSQPIYI
QYSNHKELKTD
>gnl|CDD|410090 cd12689, RRM1_hnRNPL_like, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein L (hnRNP-L) and similar proteins. This subfamily corresponds to the RRM1 of heterogeneous nuclear ribonucleoprotein L (hnRNP-L), heterogeneous nuclear ribonucleoprotein L-like (hnRNP-LL), and similar proteins. hnRNP-L is a higher eukaryotic specific subunit of human KMT3a (also known as HYPB or hSet2) complex required for histone H3 Lys-36 trimethylation activity. It plays both, nuclear and cytoplasmic, roles in mRNA export of intronless genes, IRES-mediated translation, mRNA stability, and splicing. hnRNP-LL plays a critical and unique role in the signal-induced regulation of CD45 and acts as a global regulator of alternative splicing in activated T cells. It is closely related in domain structure and sequence to hnRNP-L, which contains three RNA-recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
PSPVVHVRGLSEHVTEADLVEALQNFGPISYVTMMPKKRQALVEFEDIEGAKACVNYAQQNPIYVGGRPA
YFNYSTSQKI
>gnl|CDD|410091 cd12690, RRM3_PTBPH1_PTBPH2, RNA recognition motif 3 (RRM3) found in plant polypyrimidine tract-binding protein homolog 1 and 2 (PTBPH1 and PTBPH2). This subfamily corresponds to the RRM3 of PTBPH1 and PTBPH2. Although their biological roles remain unclear, PTBPH1 and PTBPH2 show significant sequence similarity to polypyrimidine tract binding protein (PTB) that is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. Both, PTBPH1 and PTBPH2, contain three RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
SNVLLASIENMQYAVTLDVLHTVFSAFGFVQKIAIFEKNGGFQALIQYPDVPTAVVAKEALEGHCIYDGG
YCKLHLSYSRHTDLNVKVNNDRSRDYT
>gnl|CDD|241135 cd12691, RRM2_PTBPH1_PTBPH2, RNA recognition motif 2 (RRM2) found in plant polypyrimidine tract-binding protein homolog 1 and 2 (PTBPH1 and PTBPH2). This subfamily corresponds to the RRM2 of PTBPH1 and PTBPH2. Although their biological roles remain unclear, PTBPH1 and PTBPH2 show significant sequence similarity to polypyrimidine tract binding protein (PTB) that is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. Both, PTBPH1 and PTBPH2, contain three RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
GNVLLVTIEGVEAGDVSIDVLHLVFSAFGFVHKIATFEKTAGFQALVQFTDAETASAARSALDGRSIPRY
LLPEHVGPCSLRISYSAHTDLNVKF
>gnl|CDD|410092 cd12692, RRM2_PTBPH3, RNA recognition motif 2 (RRM2) found in plant polypyrimidine tract-binding protein homolog 3 (PTBPH3). This subfamily corresponds to the RRM2 of PTBPH3. Although its biological roles remain unclear, PTBPH3 shows significant sequence similarity to polypyrimidine tract binding protein (PTB) that is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. Like PTB, PTBPH3 contains four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
PNRILLVTIHHPLYPITVDVLHQVFSPHGFVEKIVTFQKSAGLQALIQYQSQQSAVQARSALQGRNIYDG
CCQLDIQFSNLQELQVNY
>gnl|CDD|410093 cd12693, RRM2_PTBP1_like, RNA recognition motif 2 (RRM2) found in polypyrimidine tract-binding protein 1 (PTB or hnRNP I) and similar proteins. This subfamily corresponds to the RRM2 of polypyrimidine tract-binding protein 1 (PTB or hnRNP I), polypyrimidine tract-binding protein 2 (PTBP2 or nPTB), regulator of differentiation 1 (Rod1), and similar proteins found in Metazoa. PTB is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. PTBP2 is highly homologous to PTB and is perhaps specific to the vertebrates. Unlike PTB, PTBP2 is enriched in the brain and in some neural cell lines. It binds more stably to the downstream control sequence (DCS) RNA than PTB does but is a weaker repressor of splicing in vitro. PTBP2 also greatly enhances the binding of two other proteins, heterogeneous nuclear ribonucleoprotein (hnRNP) H and KH-type splicing-regulatory protein (KSRP), to the DCS RNA. The binding properties of PTBP2 and its reduced inhibitory activity on splicing imply roles in controlling the assembly of other splicing-regulatory proteins. PTBP2 also contains four RRMs. ROD1 coding protein Rod1 is a mammalian PTB homolog of a regulator of differentiation in the fission yeast Schizosaccharomyces pombe, where the nrd1 gene encodes an RNA binding protein negatively regulates the onset of differentiation. ROD1 is predominantly expressed in hematopoietic cells or organs. It may play a role controlling differentiation in mammals. All members in this family contain four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
NPVLRVIVENLFYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALIQFADAVSAQAAKLSLDGQNIYNGC
CTLRIDFSKLTSLNVKYNNDKSRDYT
>gnl|CDD|410094 cd12694, RRM2_hnRNPL_like, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein L (hnRNP-L) and similar proteins. This subfamily corresponds to the RRM2 of heterogeneous nuclear ribonucleoprotein L (hnRNP-L), heterogeneous nuclear ribonucleoprotein L-like (hnRNP-LL), and similar proteins. hnRNP-L is a higher eukaryotic specific subunit of human KMT3a (also known as HYPB or hSet2) complex required for histone H3 Lys-36 trimethylation activity. It plays both nuclear and cytoplasmic roles in mRNA export of intronless genes, IRES-mediated translation, mRNA stability, and splicing. hnRNP-LL plays a critical and unique role in the signal-induced regulation of CD45 and acts as a global regulator of alternative splicing in activated T cells. It is closely related in domain structure and sequence to hnRNP-L, which contains three RNA-recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
NHVLLFTILNPLYPITVDVIHTICSPYGKVLRIVIFRKNGVQAMVEFDSVESAQRAKAALNGADIYSGCC
TLKIEYAKPTRLNVYK
>gnl|CDD|410095 cd12695, RRM3_PTBP1, RNA recognition motif 3 (RRM3) found in vertebrate polypyrimidine tract-binding protein 1 (PTB). This subgroup corresponds to the RRM3 of PTB, also known as 58 kDa RNA-binding protein PPTB-1 or heterogeneous nuclear ribonucleoprotein I (hnRNP I), an important negative regulator of alternative splicing in mammalian cells. PTB also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. PTB contains four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain). RRM1 and RRM2 are independent from each other and separated by flexible linkers. By contrast, there is an unusual and conserved interdomain interaction between RRM3 and RRM4. It is widely held that only RRMs 3 and 4 are involved in RNA binding and RRM2 mediates PTB homodimer formation. However, new evidence show that the RRMs 1 and 2 also contribute substantially to RNA binding. Moreover, PTB may not always dimerize to repress splicing. It is a monomer in solution
VLLVSNLNPERVTPQCLFILFGVYGDVQRVKILFNKKENALVQMADGNQAQLAMSHLNGQKLHGKPIRIT
LSKHQTVQLPREGQEDQGLTKDY
>gnl|CDD|410096 cd12696, RRM3_PTBP2, RNA recognition motif 3 (RRM3) found in vertebrate polypyrimidine tract-binding protein 2 (PTBP2). This subgroup corresponds to the RRM3 of PTBP2, also known as neural polypyrimidine tract-binding protein or neurally-enriched homolog of PTB (nPTB), highly homologous to polypyrimidine tract binding protein (PTB) and perhaps specific to the vertebrates. Unlike PTB, PTBP2 is enriched in the brain and in some neural cell lines. It binds more stably to the downstream control sequence (DCS) RNA than PTB does but is a weaker repressor of splicing in vitro. PTBP2 also greatly enhances the binding of two other proteins, heterogeneous nuclear ribonucleoprotein (hnRNP) H and KH-type splicing-regulatory protein (KSRP), to the DCS RNA. The binding properties of PTBP2 and its reduced inhibitory activity on splicing imply roles in controlling the assembly of other splicing-regulatory proteins. PTBP2 contains four RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
GRVGMPGVSAGGNTVLLVSNLNEEMVTPQSLFTLFGVYGDVQRVKILYNKKDSALIQMADGNQSQLAMSH
LNGQKMYGKIIRVTLSKHQTVQLPREGLDDQGLTKDF
>gnl|CDD|410097 cd12697, RRM3_ROD1, RNA recognition motif 3 (RRM3) found in vertebrate regulator of differentiation 1 (Rod1). This subgroup corresponds to the RRM3 of ROD1 coding protein Rod1, a mammalian polypyrimidine tract binding protein (PTB) homolog of a regulator of differentiation in the fission yeast Schizosaccharomyces pombe, where the nrd1 gene encodes an RNA binding protein negatively regulates the onset of differentiation. ROD1 is predominantly expressed in hematopoietic cells or organs. It might play a role controlling differentiation in mammals. Rod1 contains four repeats of RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain) and does have RNA binding activities
SVLLVSNLNPDAITPHGLFILFGVYGDVLRVKIMFNKKENALVQMADATQAQIAMSHLNGQRLYGKVLRA
TLSKHQ
>gnl|CDD|410098 cd12698, RRM3_PTBPH3, RNA recognition motif 3 (RRM3) found in plant polypyrimidine tract-binding protein homolog 3 (PTBPH3). This subgroup corresponds to the RRM3 of PTBPH3. Although its biological roles remain unclear, PTBPH3 shows significant sequence similarity to polypyrimidine tract binding protein (PTB) that is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. Like PTB, PTBPH3 contains four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
TPVLLVSNLNPEKVDVDKLFNLFSLYGNIVRIKILRNKPDHALIQMSDPFQAELAVNYLKGAMLFGKSLE
VNFSKH
>gnl|CDD|410099 cd12699, RRM3_hnRNPL, RNA recognition motif 3 (RRM3) found in vertebrate heterogeneous nuclear ribonucleoprotein L (hnRNP-L). This subgroup corresponds to the RRM3 of hnRNP-L, a higher eukaryotic specific subunit of human KMT3a (also known as HYPB or hSet2) complex required for histone H3 Lys-36 trimethylation activity. It plays both, nuclear and cytoplasmic, roles in mRNA export of intronless genes, IRES-mediated translation, mRNA stability, and splicing. hnRNP-L shows significant sequence homology with polypyrimidine tract-binding protein (PTB or hnRNP I). Both, hnRNP-L and PTB, are localized in the nucleus but excluded from the nucleolus. hnRNP-L is an RNA-binding protein with three RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
DSPVLMVYGLDQSKMNCDRVFNVFCLYGNVEKVKFMKSKPGAAMVEMADGYAVDRAITHLNNNFMFGQKL
NVCVSKQ
>gnl|CDD|410100 cd12700, RRM3_hnRPLL, RNA recognition motif 3 (RRM3) found in vertebrate heterogeneous nuclear ribonucleoprotein L-like (hnRNP-LL). The subgroup corresponds to the RRM3 of hnRNP-LL which plays a critical and unique role in the signal-induced regulation of CD45 and acts as a global regulator of alternative splicing in activated T cells. It is closely related in domain structure and sequence to heterogeneous nuclear ribonucleoprotein L (hnRNP-L), which is an abundant nuclear, multifunctional RNA-binding protein with three RNA-recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
VAMVSGLHQLKMNCSRVFNLFCLYGNIEKVKFMKTIPGTALVEMGDEYAVERAVTHLNNVKLFGKRLNVC
VSKQ
>gnl|CDD|410101 cd12701, RRM4_PTBP1, RNA recognition motif 4 (RRM4) found in vertebrate polypyrimidine tract-binding protein 1 (PTB). This subgroup corresponds to the RRM4 of PTB, also known as 58 kDa RNA-binding protein PPTB-1 or heterogeneous nuclear ribonucleoprotein I (hnRNP I), an important negative regulator of alternative splicing in mammalian cells. PTB also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. PTB contains four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain). RRM1 and RRM2 are independent from each other and separated by flexible linkers. By contrast, there is an unusual and conserved interdomain interaction between RRM3 and RRM4. It is widely held that only RRMs 3 and 4 are involved in RNA binding and RRM2 mediates PTB homodimer formation. However, new evidence shows that the RRMs 1 and 2 also contribute substantially to RNA binding. Moreover, PTB may not always dimerize to repress splicing. It is a monomer in solution
TLHLSNIPPSVSEEDLKMLFSSNGGMVKGFKFFQKDRKMALIQMGSVEEAIQALIDLHNHDLGENHHLRV
SFSKST
>gnl|CDD|241146 cd12702, RRM4_PTBP2, RNA recognition motif 4 (RRM4) found in vertebrate polypyrimidine tract-binding protein 2 (PTBP2). This subgroup corresponds to the RRM4 of PTBP2, also known as neural polypyrimidine tract-binding protein or neurally-enriched homolog of PTB (nPTB), highly homologous to polypyrimidine tract binding protein (PTB) and perhaps specific to the vertebrates. Unlike PTB, PTBP2 is enriched in the brain and in some neural cell lines. It binds more stably to the downstream control sequence (DCS) RNA than PTB does but is a weaker repressor of splicing in vitro. PTBP2 also greatly enhances the binding of two other proteins, heterogeneous nuclear ribonucleoprotein (hnRNP) H and KH-type splicing-regulatory protein (KSRP), to the DCS RNA. The binding properties of PTBP2 and its reduced inhibitory activity on splicing imply roles in controlling the assembly of other splicing-regulatory proteins. PTBP2 contains four RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
PPSATLHLSNIPPSVAEEDLRTLFANTGGTVKAFKFFQDHKMALLQMSTVEEAIQALIDLHNYNLGENHH
LRVSFSKSTI
>gnl|CDD|410102 cd12703, RRM4_ROD1, RNA recognition motif 4 (RRM4) found in vertebrate regulator of differentiation 1 (Rod1). This subgroup corresponds to the RRM4 of ROD1 coding protein Rod1, a mammalian polypyrimidine tract binding protein (PTB) homolog of a regulator of differentiation in the fission yeast Schizosaccharomyces pombe, where the nrd1 gene encodes an RNA binding protein that negatively regulates the onset of differentiation. ROD1 is predominantly expressed in hematopoietic cells or organs. It might play a role controlling differentiation in mammals. Rod1 contains four repeats of RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain) and does have RNA binding activities
PGSKNFQNIFPPSATLHLSNIPPSVTDDDLKRLFASTGCSVKAFKFFQKDRKMALIQLGSVEEAIQALIE
LHNHDLGENHHLRVSFSKSTI
>gnl|CDD|410103 cd12704, RRM4_hnRNPL, RNA recognition motif 4 (RRM4) found in vertebrate heterogeneous nuclear ribonucleoprotein L (hnRNP-L). This subgroup corresponds to the RRM4 of hnRNP-L, a higher eukaryotic specific subunit of human KMT3a (also known as HYPB or hSet2) complex required for histone H3 Lys-36 trimethylation activity. It plays both, nuclear and cytoplasmic, roles in mRNA export of intronless genes, IRES-mediated translation, mRNA stability, and splicing. hnRNP-L shows significant sequence homology with polypyrimidine tract-binding protein (PTB or hnRNP I). Both hnRNP-L and PTB are localized in the nucleus but excluded from the nucleolus. hnRNP-L is an RNA-binding protein with three RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
PSNVLHFFNAPPEVTEENFFEICDELGVKRPTSVKVFSGKSERSSSGLLEWDSKSDALETLGLLNHYQMK
NPNGPYPYTLKLCF
>gnl|CDD|410104 cd12705, RRM4_hnRPLL, RNA recognition motif 4 (RRM4) found in vertebrate heterogeneous nuclear ribonucleoprotein L-like (hnRNP-LL). The subgroup corresponds to the RRM4 of hnRNP-LL which plays a critical and unique role in the signal-induced regulation of CD45 and acts as a global regulator of alternative splicing in activated T cells. It is closely related in domain structure and sequence to heterogeneous nuclear ribonucleoprotein L (hnRNP-L), which is an abundant nuclear, multifunctional RNA-binding protein with three RNA-recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
PSCVLHYYNVPLCVTEETFQKLCEDHEVPTFIKYKVFDAKPSSKTLSGLLEWESKTEAVEALTVLNHYQI
RVPNGSNPYTLKLCF
>gnl|CDD|410105 cd12706, RRM_LARP5, RNA recognition motif (RRM) found in vertebrate La-related protein 5 (LARP5 or LARP4B). This subgroup corresponds to the RRM of LARP5, a cytosolic protein that co-sediments with polysomes and accumulates upon stress induction in cellular stress granules. It can interact with the cytosolic poly(A) binding protein 1 (PABPC1) and the receptor for activated C Kinase (RACK1), a component of the 40S ribosomal subunit. LARP5 may function as a stimulatory factor of translation through bridging mRNA factors of the 3' end with initiating ribosomes. Like other La-related proteins (LARPs) family members, LARP5 contains a La motif (LAM) and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
CIVILREVPESTPIEEVEALFKGDNLPKFINCEFAYNDNWFITFESEADAQQAYKYLREEVKTFQGKPIK
ARIKAKA
>gnl|CDD|410106 cd12707, RRM_LARP4, RNA recognition motif (RRM) found in vertebrate La-related protein 4 (LARP4). This subgroup corresponds to the RRM of LARP4, a cytoplasmic factor that can bind poly(A) RNA and interact with poly(A) binding protein (PABP). It may play a role in promoting translation by stabilizing mRNA. LARP4 is structurally related to the La autoantigen. Like other La-related proteins (LARPs) family members, LARP4 contains a La motif (LAM) and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
CIIILREIPETTPVEEVKALFKNENCPKVISCEFAHNNNWYITFQSDTDAQQAFKYLREEVKTFQGKPIM
ARIKAIN
>gnl|CDD|410107 cd12708, RRM_RCAN1, RNA recognition motif (RRM) found in vertebrate regulator of calcineurin 1 (RCAN1). This subgroup corresponds to the RRM of RCAN1, also termed calcipressin-1, or Adapt78, or Down syndrome critical region protein 1, or myocyte-enriched calcineurin-interacting protein 1 (MCIP1), encoded by the Down syndrome critical region 1 (DSCR1) gene that is abundantly expressed in human brain, heart and muscles. Overexpressed RCAN1 functions as an inhibitor of the Ca2+/calmodulin-dependent phosphatase calcineurin (also termed PP2B or PP3C), and is associated with Alzheimer's disease (AD) and Down syndrome (DS). RCAN1 can be phosphorylated by several kinases such as big MAP kinase 1 (BMK1), glycogen synthase kinase-3 (GSK-3), NF-kappaB inducing kinase (NIK), and protein kinase A (PKA). The phosphorylation of RCAN1 can positively or negatively regulate calcineurin-mediated gene transcription, and also affect its protein stability in the ubiquitin-proteasome pathway. RCAN1 consists of an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a highly conserved SP repeat domain containing the phosphorylation site by GSK-3, a well-known PxIxIT motif responsible for docking many substrates to calcineurin, and an unrecognized C-terminal TxxP motif of unknown function
SSLVACVADTDVFTDSETRAKFESLFRAYDKDATFQFFKSFKRVRINFSNPISAAEARIRLHKTEFNGKE
IKLYFAQTLHIGSPHLAPPNPDK
>gnl|CDD|410108 cd12709, RRM_RCAN2, RNA recognition motif (RRM) found in vertebrate regulator of calcineurin 2 (RCAN2). This subgroup corresponds to the RRM of RCAN2, also termed calcipressin-2, or Down syndrome candidate region 1-like 1 (DSCR1L1), or myocyte-enriched calcineurin-interacting protein 2 (MCIP2), or thyroid hormone-responsive protein ZAKI-4, encoded by a novel thyroid hormone-responsive gene ZAKI-4 that is abundantly expressed in human brain, heart and muscles. RCAN2 binds to the catalytic subunit of Ca2+/calmodulin-dependent phosphatase calcineurin (also termed PP2B or PP3C), calcineurin A, and inhibits its phosphatase activity through its C-terminal region. RCAN2 consists of an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a highly conserved SP repeat domain containing the phosphorylation site by GSK-3, a well-known PxIxIT motif responsible for docking many substrates to calcineurin, and an unrecognized C-terminal TxxP motif of unknown function
STLFACNVDQEVFTSQESKEKFEALFLAYDDCVTFQLFKSFRRVRINFSNPKAAARARIELHETQFRGKK
LKLYFAQ
>gnl|CDD|410109 cd12710, RRM_RCAN3, RNA recognition motif (RRM) found in vertebrate regulator of calcineurin 3 (RCAN3). This subgroup corresponds to the RRM of RCAN3, also termed calcipressin-3, or Down syndrome candidate region 1-like protein 2 (DSCR1L2), or myocyte-enriched calcineurin-interacting protein 3 (MCIP3), encoded by a ubiquitously expressed DSCR1L2 gene. Overexpressed RCAN3 binds and inhibits the Ca2+/calmodulin-dependent phosphatase calcineurin (also termed PP2B or PP3C), and further down-regulates nuclear factor of activated T cells (NFAT)-dependent cytokine gene expression in activated human Jurkat T cells. Moreover, RCAN3 interacts with cardiac troponin I (TNNI3), a heart-specific inhibitory subunit of the troponin complex, and may play a role in cardiac contraction. RCAN3 consists of an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a highly conserved SP repeat domain containing the phosphorylation site by GSK-3, a well-known PxIxIT motif responsible for docking many substrates to calcineurin, and an unrecognized C-terminal TxxP motif of unknown function
TALFACSVHEAVFEDQEQRERFEALFRIYDNQVTFQLFKSFRRVRINFSNPEAAARARIELHESDFNGKK
LKLYFAQ
>gnl|CDD|410110 cd12711, RRM_TNRC6A, RNA recognition motif (RRM) found in vertebrate GW182 autoantigen. This subgroup corresponds to the RRM of the GW182 autoantigen, also termed trinucleotide repeat-containing gene 6A protein (TNRC6A), or CAG repeat protein 26, or EMSY interactor protein, or protein GW1, or glycine-tryptophan protein of 182 kDa, a phosphorylated cytoplasmic autoantigen involved in stabilizing and/or regulating translation and/or storing several different mRNAs. GW182 is characterized by multiple glycine/tryptophan (G/W) repeats and is a critical component of GW bodies (GWBs, also called mammalian processing bodies, or P bodies). The mRNAs associated with GW182 are presumed to reside within GWBs. GW182 has been shown to bind multiple Ago-miRNA complexes, and thus plays a key role in miRNA-mediated translational repression and mRNA degradation. In the absence of Ago2, GW182 may induce translational silencing effect. GW182 is composed of an N-terminal G/W-rich region containing an Ago hook responsible for Ago protein-binding; a ubiquitin-associated (UBA) domain and a glutamine (Q)-rich region in the middle region; a middle G/W-rich region, a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal G/W-rich region, at the C-terminus. A bipartite C-terminal region including the middle and C-terminal G/W-rich regions is referred to as silencing domain that triggers silencing of bound transcripts by inhibiting protein expression and promoting mRNA decay via deadenylation
SSGRITNWLVLKNLTPQIDGSTLRTLCMQHGPLITFHLNLPHGNALVRYSSKEEAVKAQKSLHMCVLGNT
TILAEFASEEEISRFFAQGQSL
>gnl|CDD|410111 cd12712, RRM_TNRC6B, RNA recognition motif (RRM) found in vertebrate trinucleotide repeat-containing gene 6B protein (TNRC6B). This subgroup corresponds to the RRM of TNRC6B, one of three GW182 paralogs in mammalian genomes. It is involved in miRNA-mediated mRNA degradation. TNRC6B is composed of an N-terminal glycine/tryptophan (G/W)-rich region; a ubiquitin-associated (UBA) domain and a glutamine (Q)-rich region in the middle region; a middle G/W-rich region, a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal G/W-rich region, at the C-terminus. TNRC6B directly interacts with Argonaute (Ago) proteins through its N-terminal glycine/tryptophan (G/W)-rich region that is called Ago protein-binding domain. TNRC6B is enriched in P-bodies and its Q-rich domain is responsible for P-body localization. A bipartite C-terminal region including the middle and C-terminal G/W-rich regions is referred as silencing domain that triggers silencing of bound transcripts by inhibiting protein expression and promoting mRNA decay via deadenylation. The C-terminal half of TNRC6B comprising an RRM domain exerts a strong translation inhibition potential, which does not require either association with Agos or localization to P-bodies
SYWLVLHNLTPQIDGSTLRTICMQHGPLLTFHLNLTQGTALIRYSTKQEAAKAQTALHMCVLGNTTILAE
FATEEEVSRYFAQ
>gnl|CDD|410112 cd12713, RRM_TNRC6C, RNA recognition motif (RRM) found in vertebrate trinucleotide repeat-containing gene 6C protein (TNRC6C). This subgroup corresponds to the RRM of TNRC6C, one of three GW182 paralogs in mammalian genomes. It is enriched in P-bodies and important for efficient miRNA-mediated repression. TNRC6C is composed of an N-terminal glycine/tryptophan (G/W)-rich region containing an Ago hook responsible for Ago protein-binding; a ubiquitin-associated (UBA) domain and a glutamine (Q)-rich region in the middle region; a middle G/W-rich region, a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal G/W-rich region, at the C-terminus. A bipartite C-terminal region including the middle and C-terminal G/W-rich regions is referred as silencing domain that triggers silencing of bound transcripts by inhibiting protein expression and promoting mRNA decay via deadenylation. The C-terminal half containing the RRM domain functions as a key effector domain mediating protein synthesis repression by TNRC6C
SSGRTSSWLVLRNLTPQIDGSTLRTLCLQHGPLITFHLNLTQGNAVVRYSSKEEAAKAQKSLHMCVLGNT
TILAEFASEEEVNRFLAQ
>gnl|CDD|410113 cd12714, RRM1_MATR3, RNA recognition motif 1 (RRM1) found in vertebrate matrin-3. This subgroup corresponds to the RRM1 of Matrin 3 (MATR3 or P130), a highly conserved inner nuclear matrix protein with a bipartite nuclear localization signal (NLS), two zinc finger domains predicted to bind DNA, and two RNA recognition motifs (RRM), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), that are known to interact with RNA. MATR3 has been implicated in various biological processes. It is involved in RNA processing by interacting with other nuclear proteins to anchor hyperedited RNAs to the nuclear matrix. It plays a role in mRNA stabilization through maintaining the stability of certain mRNA species. Besides, it modulates the activity of proximal promoters by binding to highly repetitive sequences of matrix/scaffold attachment region (MAR/SAR). The phosphorylation of MATR3 is assumed to cause neuronal death. It is phosphorylated by the protein kinase ATM, which activates the cellular response to double strand breaks in the DNA. Its phosphorylation by protein kinase A (PKA) is responsible for the activation of the N-methyl-d-aspartic acid (NMDA) receptor. Furthermore, MATR3 has been identified as both a Ca2+-dependent CaM-binding protein and a downstream substrate of caspases. Additional research indicates that matrin 3 also binds Rev/Rev responsive element (RRE)-containing viral RNA and functions as a cofactor that mediates the post-transcriptional regulation of HIV-1
RVVHIMDFQRGKNLRYQLLQLAEPFGIITNHLILNKINEAFIEMATTEEAQAAVDYYMTTPALVFGKPVR
VHLSQK
>gnl|CDD|410114 cd12715, RRM2_MATR3, RNA recognition motif 2 (RRM2) found in vertebrate matrin-3. This subgroup corresponds to the RRM2 of Matrin 3 (MATR3 or P130), a highly conserved inner nuclear matrix protein with a bipartite nuclear localization signal (NLS), two zinc finger domains predicted to bind DNA, and two RNA recognition motifs (RRM), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), that are known to interact with RNA. MATR3 has been implicated in various biological processes. It is involved in RNA processing by interacting with other nuclear proteins to anchor hyperedited RNAs to the nuclear matrix. It plays a role in mRNA stabilization through maintaining the stability of certain mRNA species. Besides, it modulates the activity of proximal promoters by binding to highly repetitive sequences of matrix/scaffold attachment region (MAR/SAR). The phosphorylation of MATR3 is assumed to cause neuronal death. It is phosphorylated by the protein kinase ATM, which activates the cellular response to double strand breaks in the DNA. Its phosphorylation by protein kinase A (PKA) is responsible for the activation of the N-methyl-d-aspartic acid (NMDA) receptor. Furthermore, MATR3 has been identified as both a Ca2+-dependent CaM-binding protein and a downstream substrate of caspases. Additional research indicates that matrin 3 also binds Rev/Rev responsive element (RRE)-containing viral RNA and functions as a cofactor that mediates the post-transcriptional regulation of HIV-1
RVIHLSNLPHSGYSDAAVLKLAEPYGKVKNYILMRMKNQAFLEMESREDAMAMVDHCKKKPLWFQGRCVK
VDLSQKYKTL
>gnl|CDD|410115 cd12716, RRM1_2_NP220, RNA recognition motif 1 (RRM1) and 2 (RRM2) found in vertebrate nuclear protein 220 (NP220). This subgroup corresponds to RRM1 and RRM2 of NP220, also termed zinc finger protein 638 (ZN638), or cutaneous T-cell lymphoma-associated antigen se33-1, or zinc finger matrin-like protein, a large nucleoplasmic DNA-binding protein that binds to cytidine-rich sequences, such as CCCCC (G/C), in double-stranded DNA (dsDNA). NP220 contains multiple domains, including MH1, MH2, and MH3, domains homologous to the acidic nuclear protein matrin 3; RS, an arginine/serine-rich domain commonly found in pre-mRNA splicing factors; PstI-HindIII, a domain essential for DNA binding; acidic repeat, a domain with nine repeats of the sequence LVTVDEVIEEEDL; and a Cys2-His2 zinc finger-like motif that is also present in matrin 3. It may be involved in packaging, transferring, or processing transcripts. This subgroup corresponds to the domain of MH2 that contains two tandem RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
CVVLISNLPEKGYTVEEISNLAKPFGGVNDILILSSHKKAYLEMNFKEAVDSMVKYYETFPVLVGGKRLK
ISMAEK
>gnl|CDD|410116 cd12717, RRM_ETP1, RNA recognition motif (RRM) found in yeast RING finger protein ETP1 and similar proteins. This subgroup corresponds to the RRM of ETP1, also termed BRAP2 homolog, or ethanol tolerance protein 1, the yeast homolog of BRCA1-associated protein (BRAP2) found in vertebrates. It may be involved in ethanol and salt-induced transcriptional activation of the NHA1 promoter and heat shock protein genes (HSP12 and HSP26), and participate in ethanol-induced turnover of the low-affinity hexose transporter Hxt3p. ETP1 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C3HC4-type ring finger domain and a UBP-type zinc finger
TLAILAVPSYMTPSDLLGFVGGATLEQVSHFRLIRTSRPNRYMVLLKFRDAKSAKEFQKEFNGKKFNSID
PETCHVVFIKEII
>gnl|CDD|410117 cd12718, RRM_BRAP2, RNA recognition motif (RRM) found in BRCA1-associated protein (BRAP2). This subgroup corresponds to the RRM of BRAP2, also termed impedes mitogenic signal propagation (IMP), or ring finger protein 52, or renal carcinoma antigen NY-REN-63, a novel cytoplasmic protein interacting with the two functional nuclear localisation signal (NLS) motifs of BRCA1, a nuclear protein linked to breast cancer. It also binds to the SV40 large T antigen NLS motif and the bipartite NLS motif found in mitosin. BRAP2 may serve as a cytoplasmic retention protein and play a role in the regulation of nuclear protein transport. It contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C3HC4-type ring finger domain and a UBP-type zinc finger
SEMLCMLAVPATLTCHDLLNFLAPVLPSIEHIKIIRDSTPNQYMVLIKFRSQEDADEFYKTFNGQQFNSL
EEDVCHLVYVSRVE
>gnl|CDD|410118 cd12719, RRM_SYNJ1, RNA recognition motif (RRM) found in synaptojanin-1 and similar proteins. This subgroup corresponds to the RRM of synaptojanin-1, also termed synaptojanin, or synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1, originally identified as one of the major Grb2-binding proteins that may participate in synaptic vesicle endocytosis. It also acts as a Src homology 3 (SH3) domain-binding brain-specific inositol 5-phosphatase with a putative role in clathrin-mediated endocytosis. Synaptojanin-1 contains an N-terminal domain homologous to the cytoplasmic portion of the yeast protein Sac1p, a central inositol 5-phosphatase domain followed by a putative RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal proline-rich region mediating the binding of synaptojanin-1 to various SH3 domain-containing proteins including amphiphysin, SH3p4, SH3p8, SH3p13, and Grb2. Synaptojanin-1 has two tissue-specific alternative splicing isoforms, synaptojanin-145 expressed in brain and synaptojanin-170 expressed in peripheral tissues. Synaptojanin-145 is very abundant in nerve terminals and may play an essential role in the clathrin-mediated endocytosis of synaptic vesicles. In contrast to synaptojanin-145, synaptojanin-170 contains three unique asparagine-proline-phenylalanine (NPF) motifs in the C-terminal region and may functions as a potential binding partner for Eps15, a clathrin coat-associated protein acting as a major substrate for the tyrosine kinase activity of the epidermal growth factor receptor
DGTVVVSVLSSSPEPNYFDDNLIDALLQQFSSFGEVILIRFVEDKMWVTFLEGSSALAALSLNGTEVLGR
TIIISLK
>gnl|CDD|410119 cd12720, RRM_SYNJ2, RNA recognition motif (RRM) found in synaptojanin-2 and similar proteins. This subgroup corresponds to the RRM of synaptojanin-2, also termed synaptic inositol-1,4,5-trisphosphate 5-phosphatase 2, an ubiquitously expressed central regulatory enzyme in the phosphoinositide-signaling cascade. As a novel Rac1 effector regulating the early step of clathrin-mediated endocytosis, synaptojanin-2 acts as a polyphosphoinositide phosphatase directly and specifically interacting with Rac1 in a GTP-dependent manner. It mediates the inhibitory effect of Rac1 on endocytosis and plays an important role in the Rac1-mediated control of cell growth. Synaptojanin-2 shows high sequence homology to the N-terminal Sac1p homology domain, the central inositol 5-phosphatase domain, the putative RNA recognition motif (RRM) of synaptojanin-1, but differs in the proline-rich region
DATVVVNLLSPTLEEKNDFPEDLSTELVQCFQSYGTVILVRFNRGQMLVTFEDSRSALRVLDLDGIKVNG
RAVKIKPK
>gnl|CDD|410120 cd12721, RRM_Nup53p_fungi, RNA recognition motif (RRM) found in yeast nucleoporin Nup53p and similar proteins. This subgroup corresponds to the RRM of Saccharomyces cerevisiae Nup53p, the ortholog of vertebrate nucleoporin Nup53. A unique property of yeast Nup53p is that it contains an additional Kap121p-binding domain and interacts specifically with the karyopherin Kap121p, which is involved in the assembly of Nup53p into NPCs. Like vertebrate Nup35, yeast Nup53p contains an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a C-terminal amphipathic alpha-helix and several FG repeats. The RRM domain lacks the conserved residues that typically bind RNA in canonical RRM domains
GTAVIVFGFPETITSQVIEHFSGFGEILEDFSVPRSGKALQKYPIPTGSNWLKLTYAEPSSALRALRENG
EILNGQCMIGCIWYDD
>gnl|CDD|410121 cd12722, RRM_Nup53, RNA recognition motif (RRM) found in nucleoporin Nup53. This subgroup corresponds to the RRM of nucleoporin Nup53, also termed mitotic phosphoprotein 44 (MP-44), or nuclear pore complex protein Nup53, required for normal cell growth and nuclear morphology in vertebrate. It tightly associates with the nuclear envelope membrane and the nuclear lamina where it interacts with lamin B. It may also interact with a group of nucleoporins including Nup93, Nup155, and Nup205 and play a role in the association of the mitotic checkpoint protein Mad1 with the nuclear pore complex (NPC). Nup35 contains an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a C-terminal amphipathic alpha-helix and several FG repeats. This RRM lacks the conserved residues that typically bind RNA in canonical RRM domains
DDTWVTVFGFPPAAASYILQQFSQYGNILKHVMSNNGNWMHIQYQSKLQAKKALSKNGKIFGENIMIGVK
PCID
>gnl|CDD|410122 cd12723, RRM1_CPEB1, RNA recognition motif 1 (RRM1) found in cytoplasmic polyadenylation element-binding protein 1 (CPEB-1) and similar proteins. This subgroup corresponds to the RRM2 of CPEB-1 (also termed CPE-BP1 or CEBP), an RNA-binding protein that interacts with the cytoplasmic polyadenylation element (CPE), a short U-rich motif in the 3' untranslated regions (UTRs) of certain mRNAs. It functions as a translational regulator that plays a major role in the control of maternal CPE-containing mRNA in oocytes, as well as of subsynaptic CPE-containing mRNA in neurons. Once phosphorylated and recruiting the polyadenylation complex, CPEB-1 may function as a translational activator stimulating polyadenylation and translation. Otherwise, it may function as a translational inhibitor when dephosphorylated and bound to a protein such as maskin or neuroguidin, which blocks translation initiation through interfering with the assembly of eIF-4E and eIF-4G. Although CPEB-1 is mainly located in cytoplasm, it can shuttle between nucleus and cytoplasm. CPEB-1 contains an N-terminal unstructured region, two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a Zn-finger motif. Both of the RRMs and the Zn finger are required for CPEB-1 to bind CPE. The N-terminal regulatory region may be responsible for CPEB-1 interacting with other proteins
YSCKVFLGGVPWDITEAGLQNAFKPFGSLSVEWPGKDGKHPRGHPPKGYVYLIFESEKSVKALLQACTHD
FLGGGEYYFKISSRRMRSKEVQVIPWVLSDS
>gnl|CDD|410123 cd12724, RRM1_CPEB2_like, RNA recognition motif 1 (RRM1) found in cytoplasmic polyadenylation element-binding protein CPEB-2, CPEB-3, CPEB-4 and similar protiens. This subgroup corresponds to the RRM1 of the paralog proteins CPEB-2, CPEB-3 and CPEB-4, all well-conserved in both, vertebrates and invertebrates. Due to the high sequence similarity, members in this family may share similar expression patterns and functions. CPEB-2 is an RNA-binding protein that is abundantly expressed in testis and localized in cytoplasm in transfected HeLa cells. It preferentially binds to poly(U) RNA oligomers and may regulate the translation of stored mRNAs during spermiogenesis. Moreover, CPEB-2 impedes target RNA translation at elongation; it directly interacts with the elongation factor, eEF2, to reduce eEF2/ribosome-activated GTP hydrolysis in vitro and inhibit peptide elongation of CPEB2-bound RNA in vivo. CPEB-3 is a sequence-specific translational regulatory protein that regulates translation in a polyadenylation-independent manner. It functions as a translational repressor that governs the synthesis of the AMPA receptor GluR2 through binding GluR2 mRNA. It also represses translation of a reporter RNA in transfected neurons and stimulates translation in response to NMDA. CPEB-4 is an RNA-binding protein that mediates meiotic mRNA cytoplasmic polyadenylation and translation. It is essential for neuron survival and present on the endoplasmic reticulum (ER). It is accumulated in the nucleus upon ischemia or the depletion of ER calcium. CPEB-4 is overexpressed in a large variety of tumors and is associated with many mRNAs in cancer cells. All family members contain an N-terminal unstructured region, two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a Zn-finger motif. In addition, they do have conserved nuclear export signals that are not present in CPEB-1
RKVFVGGLPPDIDEDEITASFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQDERSVQALIDACIEEDDK
LYLCVSSPTIKDKPVQIRPWNL
>gnl|CDD|410124 cd12725, RRM2_CPEB1, RNA recognition motif 2 (RRM2) found in cytoplasmic polyadenylation element-binding protein 1 (CPEB-1) and similar proteins. This subgroup corresponds to the RRM2 of CPEB-1 (also termed CPE-BP1 or CEBP), an RNA-binding protein that interacts with the cytoplasmic polyadenylation element (CPE), a short U-rich motif in the 3' untranslated regions (UTRs) of certain mRNAs. It functions as a translational regulator that plays a major role in the control of maternal CPE-containing mRNA in oocytes, as well as of subsynaptic CPE-containing mRNA in neurons. Once phosphorylated and recruiting the polyadenylation complex, CPEB-1 may function as a translational activator stimulating polyadenylation and translation. Otherwise, it may function as a translational inhibitor when dephosphorylated and bound to a protein such as maskin or neuroguidin, which blocks translation initiation through interfering with the assembly of eIF-4E and eIF-4G. Although CPEB-1 is mainly located in cytoplasm, it can shuttle between nucleus and cytoplasm. CPEB-1 contains an N-terminal unstructured region, two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a Zn-finger motif. Both of the RRMs and the Zn finger are required for CPEB-1 to bind CPE. The N-terminal regulatory region may be responsible for CPEB-1 interacting with other proteins
DPSKTVFVGALHGMLNAEGLANIMNDLFGGVVYAGIDTDKHKYPIGSGRVTFNNQRSYMKAVNAAFVEIK
TPKFTKKVQIDPYL
>gnl|CDD|410125 cd12726, RRM2_CPEB2_like, RNA recognition motif 2 (RRM2) found in cytoplasmic polyadenylation element-binding protein CPEB-2, CPEB-3, CPEB-4 and similar protiens. This subgroup corresponds to the RRM2 of the paralog proteins CPEB-2, CPEB-3 and CPEB-4, all well conserved in both, vertebrates and invertebrates. Due to the high sequence similarity, members in this family may share similar expression patterns and functions. CPEB-2 is an RNA-binding protein that is abundantly expressed in testis and localized in cytoplasm in transfected HeLa cells. It preferentially binds to poly(U) RNA oligomers and may regulate the translation of stored mRNAs during spermiogenesis. Moreover, CPEB-2 impedes target RNA translation at elongation; it directly interacts with the elongation factor, eEF2, to reduce eEF2/ribosome-activated GTP hydrolysis in vitro and inhibit peptide elongation of CPEB2-bound RNA in vivo. CPEB-3 is a sequence-specific translational regulatory protein that regulates translation in a polyadenylation-independent manner. It functions as a translational repressor that governs the synthesis of the AMPA receptor GluR2 through binding GluR2 mRNA. It also represses translation of a reporter RNA in transfected neurons and stimulates translation in response to NMDA. CPEB-4 is an RNA-binding protein that mediates meiotic mRNA cytoplasmic polyadenylation and translation. It is essential for neuron survival and present on the endoplasmic reticulum (ER). It is accumulated in the nucleus upon ischemia or the depletion of ER calcium. CPEB-4 is overexpressed in a large variety of tumors and is associated with many mRNAs in cancer cells. All family members contain an N-terminal unstructured region, two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a Zn-finger motif. In addition, they do have conserved nuclear export signals that are not present in CPEB-1
KTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHG
DIDKRVEVKPY
>gnl|CDD|410126 cd12727, RRM_like_Smg4_UPF3A, RNA recognition motif (RRM)-like Smg4_UPF3 domain in up-frameshift suppressor 3 homolog A (Upf3A). This subgroup corresponds to the RRM-like Smg4_UPF3 domain in Upf3A, also termed regulator of nonsense transcripts 3A, or nonsense mRNA reducing factor 3A, a human ortholog of yeast Upf3p and Caenorhabditis elegans SMG-4. It derives from gene UPF3A and is required for nonsense-mediated mRNA decay (NMD) in human. Upf3A is a nucleocytoplasmic shuttling protein that associates selectively with spliced beta-globin mRNA in vivo. Like other Upf3 proteins, Upf3A contains nuclear import and export signals, and a conserved Smg4_UPF3 domain with some similarity to an RNA recognition motif (RRM), indicating that it may be an RNA binding protein
TLSKVVIRRLPPNLTKEQLEEQLRPLPAHDYFEFFAADQSLYPHLFSRAYINFKNPEDILLFRDRFDGYV
FIDNKGQEYPAVVEFAP
>gnl|CDD|410127 cd12728, RRM_like_Smg4_UPF3B, RNA recognition motif (RRM)-like Smg4_UPF3 domain in up-frameshift suppressor 3 homolog B on chromosome X (Upf3B). This subgroup corresponds to the RRM-like Smg4_UPF3 domain in Upf3B, also termed regulator of nonsense transcripts 3B, or nonsense mRNA reducing factor 3B, a human ortholog of yeast Upf3p and Caenorhabditis elegans SMG-4. It derives from X-linked gene UPF3B and is required for nonsense-mediated mRNA decay (NMD) in human. Upf3B is a nucleocytoplasmic shuttling protein that associates selectively with spliced beta-globin mRNA in vivo. Like other Upf3 proteins, Upf3B contains nuclear import and export signals, and a conserved Smg4_UPF3 domain with some similarity to an RNA recognition motif (RRM), indicating that it may be an RNA binding protein
LSKVVIRRLPPSLTKEQLEEHLQPLPEHDYFEFFSNDSSLYPHMFSRAYINFKNQEDIVLFRDRFDGYVF
IDNRGQEYPAIVEFAPFQK
>gnl|CDD|410128 cd12729, RRM1_hnRNPH_hnRNPH2_hnRNPF, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2, hnRNP F and similar proteins. This subgroup corresponds to the RRM1 of hnRNP H (also termed mcs94-1), hnRNP H2 (also termed FTP-3 or hnRNP H') and hnRNP F. These represent a group of nuclear RNA binding proteins that play important roles in the regulation of alternative splicing decisions. hnRNP H and hnRNP F are two closely related proteins, both of which bind to the RNA sequence DGGGD. They are present in a complex with the tissue-specific splicing factor Fox2, and regulate the alternative splicing of the fibroblast growth factor receptor 2 (FGFR2) transcripts. The presence of Fox 2 can allows hnRNP H and hnRNP F to better compete with the SR protein ASF/SF2 for binding to FGFR2 exon IIIc. Thus, hnRNP H and hnRNP F can function as potent silencers of FGFR2 exon IIIc inclusion through an interaction with the exonic GGG motifs. Furthermore, hnRNP H and hnRNP H2 are almost identical. Both of them have been found to bind nuclear-matrix proteins. hnRNP H activates exon inclusion by binding G-rich intronic elements downstream of the 5' splice site in the transcripts of c-src, human immunodeficiency virus type 1 (HIV-1), Bcl-X, GRIN1, and myelin. It silences exons when bound to exonic elements in the transcripts of beta-tropomyosin, HIV-1, and alpha-tropomyosin. hnRNP H2 has been implicated in pre-mRNA 3' end formation. Members in this family contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 are responsible for the binding to the RNA at DGGGD motifs, and they play an important role in efficiently silencing the exon. In addition, the family members have an extensive glycine-rich region near the C-terminus, which may allow them to homo- or heterodimerize
GFVVKVRGLPWSCSADEVQNFFSDCKIANGASGIHFIYTREGRPSGEAFVELESEEDVKLALKKDRETMG
HRYVEVFKS
>gnl|CDD|410129 cd12730, RRM1_GRSF1, RNA recognition motif 1 (RRM1) found in G-rich sequence factor 1 (GRSF-1) and similar proteins. This subgroup corresponds to the RRM1 of GRSF-1, a cytoplasmic poly(A)+ mRNA binding protein which interacts with RNA in a G-rich element-dependent manner. It may function in RNA packaging, stabilization of RNA secondary structure, or other macromolecular interactions. GRSF-1 contains three potential RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which are responsible for the RNA binding. In addition, GRSF-1 has two auxiliary domains, an acidic alpha-helical domain and an N-terminal alanine-rich region, that may play a role in protein-protein interactions and provide binding specificity
VFIVRARGLPWSCTAEDVLSFFSDCRIRNGEDGIHFLLNRDGKRRGDALIELESEEDVQKALEQHRKYMG
QRYVEVFEI
>gnl|CDD|410130 cd12731, RRM2_hnRNPH_hnRNPH2_hnRNPF, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2, hnRNP F and similar proteins. This subgroup corresponds to the RRM2 of hnRNP H (also termed mcs94-1), hnRNP H2 (also termed FTP-3 or hnRNP H') and hnRNP F. These represent a group of nuclear RNA binding proteins that play important roles in the regulation of alternative splicing decisions. hnRNP H and hnRNP F are two closely related proteins, both of which bind to the RNA sequence DGGGD. They are present in a complex with the tissue-specific splicing factor Fox2, and regulate the alternative splicing of the fibroblast growth factor receptor 2 (FGFR2) transcripts. The presence of Fox 2 can allows hnRNP H and hnRNP F to better compete with the SR protein ASF/SF2 for binding to FGFR2 exon IIIc. Thus, hnRNP H and hnRNP F can function as potent silencers of FGFR2 exon IIIc inclusion through an interaction with the exonic GGG motifs. Furthermore, hnRNP H and hnRNP H2 are almost identical; both have been found to bind nuclear-matrix proteins. hnRNP H activates exon inclusion by binding G-rich intronic elements downstream of the 5' splice site in the transcripts of c-src, human immunodeficiency virus type 1 (HIV-1), Bcl-X, GRIN1, and myelin. It silences exons when bound to exonic elements in the transcripts of beta-tropomyosin, HIV-1, and alpha-tropomyosin. hnRNP H2 has been implicated in pre-mRNA 3' end formation. Members in this family contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 are responsible for the binding to the RNA at DGGGD motifs, and they play an important role in efficiently silencing the exon. In addition, the family members have an extensive glycine-rich region near the C-terminus, which may allow them to homo- or heterodimerize
NSPDTANDGFVRLRGLPFGCSKEEIVQFFSGLEIVPNGITLPVDFQGRSTGEAFVQFASQEIAEKALKKH
KERIGHRYIEIFKSSRAEVR
>gnl|CDD|410131 cd12732, RRM2_hnRNPH3, RNA recognition motif 2 (RRM2) found in heterogeneous nuclear ribonucleoprotein H3 (hnRNP H3) and similar proteins. This subgroup corresponds to the RRM2 of hnRNP H3 (also termed hnRNP 2H9), a nuclear RNA binding protein that belongs to the hnRNP H protein family that also includes hnRNP H (also termed mcs94-1), hnRNP H2 (also termed FTP-3 or hnRNP H') and hnRNP F. This family is involved in mRNA processing and exhibit extensive sequence homology. Currently, little is known about the functions of hnRNP H3 except for its role in the splicing arrest induced by heat shock. In addition, the typical hnRNP H proteins contain contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), except for hnRNP H3, in which the RRM1 is absent. RRM1 and RRM2 are responsible for the binding to the RNA at DGGGD motifs, and play an important role in efficiently silencing the exon. Members in this family can regulate the alternative splicing of the fibroblast growth factor receptor 2 (FGFR2) transcripts, and function as silencers of FGFR2 exon IIIc through an interaction with the exonic GGG motifs. The lack of RRM1 could account for the reduced silencing activity within hnRNP H3. In addition, like other hnRNP H protein family members, hnRNP H3 has an extensive glycine-rich region near the C-terminus, which may allow it to homo- or heterodimerize
MDWVLKHNGPTDTENSSDGTVRLRGLPFGCSKEEIVQFFSGLEIVPNGITLTMDYQGRSTGEAFVQFASK
EIAENALGKHKERIGHRYIEIFKSSR
>gnl|CDD|410132 cd12733, RRM3_GRSF1, RNA recognition motif 3 (RRM3) found in G-rich sequence factor 1 (GRSF-1) and similar proteins. This subgroup corresponds to the RRM3 of G-rich sequence factor 1 (GRSF-1), a cytoplasmic poly(A)+ mRNA binding protein which interacts with RNA in a G-rich element-dependent manner. It may function in RNA packaging, stabilization of RNA secondary structure, or other macromolecular interactions. GRSF-1 contains three potential RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which are responsible for the RNA binding. In addition, GRSF-1 has two auxiliary domains, an acidic alpha-helical domain and an N-terminal alanine-rich region, that may play a role in protein-protein interactions and provide binding specificity
HFVHMRGLPFQANGQDIINFFAPLKPVRITMEYGPDGKATGEADVHFASHEDAVAAMAKDRSHMQHRYIE
LFLNS
>gnl|CDD|410133 cd12734, RRM3_hnRNPH_hnRNPH2_hnRNPF, RNA recognition motif 3 (RRM3) found in heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2, hnRNP F and similar proteins. This subgroup corresponds to the RRM3 of hnRNP H (also termed mcs94-1), hnRNP H2 (also termed FTP-3 or hnRNP H') and hnRNP F, which represent a group of nuclear RNA binding proteins that play important roles in the regulation of alternative splicing decisions. hnRNP H and hnRNP F are two closely related proteins, both of which bind to the RNA sequence DGGGD. They are present in a complex with the tissue-specific splicing factor Fox2, and regulate the alternative splicing of the fibroblast growth factor receptor 2 (FGFR2) transcripts. The presence of Fox 2 can allows hnRNP H and hnRNP F to better compete with the SR protein ASF/SF2 for binding to FGFR2 exon IIIc. Thus, hnRNP H and hnRNP F can function as potent silencers of FGFR2 exon IIIc inclusion through an interaction with the exonic GGG motifs. Furthermore, hnRNP H and hnRNP H2 are almost identical; bothe have been found to bind nuclear-matrix proteins. hnRNP H activates exon inclusion by binding G-rich intronic elements downstream of the 5' splice site in the transcripts of c-src, human immunodeficiency virus type 1 (HIV-1), Bcl-X, GRIN1, and myelin. It silences exons when bound to exonic elements in the transcripts of beta-tropomyosin, HIV-1, and alpha-tropomyosin. hnRNP H2 has been implicated in pre-mRNA 3' end formation. Members in this family contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 are responsible for the binding to the RNA at DGGGD motifs, and they play an important role in efficiently silencing the exon. In addition, the family members have an extensive glycine-rich region near the C-terminus, which may allow them to homo- or heterodimerize
HCVHMRGLPYRATENDIYNFFSPLNPVRVHIEIGPDGRVTGEADVEFATHEDAVAAMSKDKANMQHRYVE
LFLNST
>gnl|CDD|241179 cd12735, RRM3_hnRNPH3, RNA recognition motif 3 (RRM3) found in heterogeneous nuclear ribonucleoprotein H3 (hnRNP H3) and similar proteins. This subgroup corresponds to the RRM3 of hnRNP H3 (also termed hnRNP 2H9), a nuclear RNA binding protein that belongs to the hnRNP H protein family that also includes hnRNP H (also termed mcs94-1), hnRNP H2 (also termed FTP-3 or hnRNP H'), and hnRNP F. This family is involved in mRNA processing and exhibit extensive sequence homology. Currently, little is known about the functions of hnRNP H3 except for its role in the splicing arrest induced by heat shock. In addition, the typical hnRNP H proteins contain contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), except for hnRNP H3, in which the RRM1 is absent. RRM1 and RRM2 are responsible for the binding to the RNA at DGGGD motifs, and they play an important role in efficiently silencing the exon. Members in this family can regulate the alternative splicing of the fibroblast growth factor receptor 2 (FGFR2) transcripts, and function as silencers of FGFR2 exon IIIc through an interaction with the exonic GGG motifs. The lack of RRM1 could account for the reduced silencing activity within hnRNP H3. In addition, like other hnRNP H protein family members, hnRNP H3 has an extensive glycine-rich region near the C-terminus, which may allow it to homo- or heterodimerize
HFVHMRGLPFRATESDIANFFSPLNPIRVHIDIGADGRATGEADVEFATHEDAVAAMSKDKNHMQHRYIE
LFLNS
>gnl|CDD|410134 cd12736, RRM1_ESRP1, RNA recognition motif 1 (RRM1) found in epithelial splicing regulatory protein 1 (ESRP1) and similar proteins. This subgroup corresponds to the RRM1 of ESRP1, also termed RNA-binding motif protein 35A (RBM35A), which has been identified as an epithelial cell type-specific regulator of fibroblast growth factor receptor 2 (FGFR2) splicing. It is required for expression of epithelial FGFR2-IIIb and the regulation of CD44, CTNND1 (p120-Catenin) and ENAH (hMena) splicing. It enhances epithelial-specific exons of CD44 and ENAH, silences mesenchymal exons of CTNND1, or both within FGFR2. Additional research indicated that ESRP1 functions as a tumor suppressor in colon cancer cells. It may be involved in posttranscriptional regulation of various genes by exerting a differential effect on protein translation via 5' untranslated regions (UTRs) of mRNAs. ESRP1 contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
SKMEIIDDNTVIRARGLPWQSSDQDIARFFKGLNIAKGGAALCLNAQGRRNGEALVRFVNEEHRDLALQR
HKHHMGNRYIEVYKATGEDFLKI
>gnl|CDD|410135 cd12737, RRM1_ESRP2, RNA recognition motif 1 (RRM1) found in epithelial splicing regulatory protein 2 (ESRP2) and similar proteins. This subgroup corresponds to the RRM1 of ESRP2, also termed RNA-binding motif protein 35B (RBM35B), which has been identified as an epithelial cell type-specific regulator of fibroblast growth factor receptor 2 (FGFR2) splicing. It is required for expression of epithelial FGFR2-IIIb and the regulation of CD44, CTNND1 (also termed p120-Catenin) and ENAH (also termed hMena) splicing. It enhances epithelial-specific exons of CD44 and ENAH, silences mesenchymal exons of CTNND1, or both within FGFR2. ESRP2 contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
VIRARGLPWQSSDQDIARFFKGLNIAKGGVALCLNAQGRRNGEALVRFVNSEQRDLALERHKHHMGSRYI
EVYKATGEEF
>gnl|CDD|241182 cd12738, RRM1_Fusilli, RNA recognition motif 1 (RRM1) found in Drosophila RNA-binding protein Fusilli and similar proteins. This subgroup corresponds to the RRM1 of RNA-binding protein Fusilli which is encoded by Drosophila fusilli (fus) gene. Loss of Fusilli activity causes lethality during embryogenesis in flies. Drosophila Fusilli can regulate endogenous fibroblast growth factor receptor 2 (FGFR2) splicing and functions as a splicing factor. Fusilli contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), an N-terminal domain with unknown function and a C-terminal domain particularly rich in alanine, glutamine, and serine
VVRARGLPWQSSDQDIAKFFRGLNIAKGGVALCLNPQGRRNGEALVRFTCTEHRDLALKRHKHHIGQRYI
EVYKATGEDF
>gnl|CDD|410136 cd12739, RRM2_ESRP1, RNA recognition motif 2 (RRM2) found in epithelial splicing regulatory protein 1 (ESRP1) and similar proteins. This subgroup corresponds to the RRM2 of ESRP1, also termed RNA-binding motif protein 35A (RBM35A), which has been identified as an epithelial cell type-specific regulator of fibroblast growth factor receptor 2 (FGFR2) splicing. It is required for expression of epithelial FGFR2-IIIb and the regulation of CD44, CTNND1 (also termed p120-Catenin) and ENAH (also termed hMena) splicing. It enhances epithelial-specific exons of CD44 and ENAH, silences mesenchymal exons of CTNND1, or both within FGFR2. Additional research indicated that ESRP1 functions as a tumor suppressor in colon cancer cells. It may be involved in posttranscriptional regulation of various genes by exerting a differential effect on protein translation via 5' untranslated regions (UTRs) of mRNAs. ESRP1 contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
GGTSNEVAQFLSKENQVIVRMRGLPFTATAEEVLAFFGQHCPVTGGKEGILFVTYPDSRPTGDAFVLFAC
EEYAQNALKKHKDLLGKRYIELFRSTAAEVQQVLNRYSSAP
>gnl|CDD|241184 cd12740, RRM2_ESRP2, RNA recognition motif 2 (RRM2) found in epithelial splicing regulatory protein 2 (ESRP2) and similar proteins. This subgroup corresponds to the RRM2 of ESRP2, also termed RNA-binding motif protein 35B (RBM35B), which has been identified as an epithelial cell type-specific regulator of fibroblast growth factor receptor 2 (FGFR2) splicing. It is required for expression of epithelial FGFR2-IIIb and the regulation of CD44, CTNND1 (also termed p120-Catenin) and ENAH (also termed hMena) splicing. It enhances epithelial-specific exons of CD44 and ENAH, silences mesenchymal exons of CTNND1, or both within FGFR2. ESRP2 contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
GGTSNEVAQFLSKENQVIIRMRGLPFTATPEDVLGFLGPECPVTGGTEGLLFVKYPDGRPTGDAFVLFAC
EEYAQNALKKHKGILGKRYIELFRSTAAEVQQVLNRY
>gnl|CDD|410137 cd12741, RRM2_Fusilli, RNA recognition motif 2 (RRM2) found in Drosophila RNA-binding protein Fusilli and similar proteins. This subgroup corresponds to the RRM2 of RNA-binding protein Fusilli which is encoded by Drosophila fusilli (fus) gene. Loss of Fusilli activity causes lethality during embryogenesis in flies. Drosophila Fusilli can regulate endogenous fibroblast growth factor receptor 2 (FGFR2) splicing and functions as a splicing factor. Fusilli contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), an N-terminal domain with unknown function and a C-terminal domain particularly rich in alanine, glutamine, and serine
AGGESNEAQNFLSKGGQVIIRMRGLPYDCTPKQVVEFFCTGDKIPHVLDGAEGVLFVKKPDGRATGDAFV
LFETEEVAEKALEKHRQHIGSRYIELFRS
>gnl|CDD|410138 cd12742, RRM3_ESRP1_ESRP2, RNA recognition motif 3 (RRM3) found in epithelial splicing regulatory protein ESRP1, ESRP2 and similar proteins. This subgroup corresponds to the RRM3 of ESRP1 (also termed RBM35A) and ESRP2 (also termed RBM35B). These are epithelial-specific RNA binding proteins that promote splicing of the epithelial variant of the fibroblast growth factor receptor 2 (FGFR2), ENAH (also termed hMena), CD44 and CTNND1 (also termed p120-Catenin) transcripts. They are highly conserved paralogs and specifically bind to GU-rich binding site. ESRP1 and ESRP2 contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains)
RDCIRLRGLPYAATIEDILEFLGEFAADIRPHGVHMVLNHQGRPSGDAFIQMKSADRAFLAAQKCHKKTM
KDRYVEVFQCS
>gnl|CDD|241187 cd12743, RRM3_Fusilli, RNA recognition motif 3 (RRM3) found in Drosophila RNA-binding protein Fusilli and similar proteins. This subgroup corresponds to the RRM3 of RNA-binding protein Fusilli which is encoded by Drosophila fusilli (fus) gene. Loss of Fusilli activity causes lethality during embryogenesis in flies. Drosophila Fusilli can regulate endogenous fibroblast growth factor receptor 2 (FGFR2) splicing and functions as a splicing factor. Fusilli contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), an N-terminal domain with unknown function and a C-terminal domain particularly rich in alanine, glutamine, and serine
KDCIRLRGLPYEAQVEHILEFLGDFAKMIVFQGVHMVYNAQGQPSGEAFIQMDSEQSASACAQQRHNRYM
VFGKKQRYIEVFQCS
>gnl|CDD|410139 cd12744, RRM1_RBM12B, RNA recognition motif 1 (RRM1) found in RNA-binding protein 12B (RBM12B) and similar proteins. This subgroup corresponds to the RRM1 of RBM12B which contains five distinct RNA binding motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). Its biological role remains unclear
AVVIRLQGLPVVAGSTDIRHFFTGLTIPDGGVHIIGGELGEAFIIFATDEDARRAMSRSGGFIKGSRVEL
FLSSKAEMQ
>gnl|CDD|241189 cd12745, RRM1_RBM12, RNA recognition motif 1 (RRM1) found in RNA-binding protein 12 (RBM12) and similar proteins. This subgrup corresponds to the RRM1 of RBM12, also termed SH3/WW domain anchor protein in the nucleus (SWAN), is ubiquitously expressed. It contains five distinct RNA binding motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two proline-rich regions, and several putative transmembrane domains. The biological role of RBM12 remains unclear
MAVVIRLQGLPIVAGTMDIRHFFSGLTIPDGGVHIVGGELGEAFIVFATDEDARLGMMRTGGTIKGSKVS
LLLSSKTEMQNMIELSRRRFET
>gnl|CDD|410140 cd12746, RRM2_RBM12B, RNA recognition motif 2 (RRM2) found in RNA-binding protein 12B (RBM12B) and similar proteins. This subgroup corresponds to the RRM2 of RBM12B which contains five distinct RNA binding motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). Its biological role remains unclear
DDVYLFLRGMPYSATEDDVRNFFSGLKVDGVIFLKHPNGRNNGNGLVKFATKEDASEGLKRHRQYMGSRF
IEVTRTTEEQWIEAGG
>gnl|CDD|410141 cd12747, RRM2_RBM12, RNA recognition motif 2 (RRM2) found in RNA-binding protein 12 (RBM12) and similar proteins. This subgroup corresponds to the RRM2 of RBM12, also termed SH3/WW domain anchor protein in the nucleus (SWAN), which is ubiquitously expressed. It contains five distinct RNA binding motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two proline-rich regions, and several putative transmembrane domains. The biological role of RBM12 remains unclear
DLYVHLHGMPFSATEADVRDFFHGLRIDAIHMLKDHLGRNNGNALVKFYSPQDTFEALKRNRMMMGQRYI
EVSPA
>gnl|CDD|410142 cd12748, RRM4_RBM12B, RNA recognition motif 4 (RRM4) found in RNA-binding protein 12B (RBM12B) and similar proteins. This subgroup corresponds to the RRM4 of RBM12B which contains five distinct RNA binding motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). Its biological role remains unclear
LCIYVRNLPFDVTKVEVQDFFEGFALAEDDIILLYDDKGVGLGEALVKFKSEEEAMKAERLNGQRFLGTE
VLLRLI
>gnl|CDD|410143 cd12749, RRM4_RBM12, RNA recognition motif 4 (RRM4) found in RNA-binding protein 12 (RBM12) and similar proteins. This subgroup corresponds to the RRM4 of RBM12, also termed SH3/WW domain anchor protein in the nucleus (SWAN), which is ubiquitously expressed. It contains five distinct RNA binding motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two proline-rich regions, and several putative transmembrane domains. The biological role of RBM12 remains unclear
CAHISNIPYNITKKDVLQFLEGIGLDENSVQVLVDNNGQGLGQALVQFKSEDDARKAERLHRKKLNGRDA
FLHLVTLEEMKEIEKNPP
>gnl|CDD|410144 cd12750, RRM5_RBM12B, RNA recognition motif 5 (RRM5) found in RNA-binding protein 12B (RBM12B) and similar proteins. This subgroup corresponds to the RRM5 of RBM12B which contains five distinct RNA binding motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). Its biological role remains unclear
VAVKLFNLPFKATVNEILDFFYGYRVIPDSVSIQYNEQGLPTGDAIIAMETYEEAMAAVQDLNDRPIGPR
KVKLSLL
>gnl|CDD|410145 cd12751, RRM5_RBM12, RNA recognition motif 5 (RRM5) found in RNA-binding protein 12 (RBM12) and similar proteins. This subgroup corresponds to the RRM5 of RBM12, also termed SH3/WW domain anchor protein in the nucleus (SWAN), which is ubiquitously expressed. It contains five distinct RNA binding motifs (RBMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two proline-rich regions, and several putative transmembrane domains. The biological role of RBM12 remains unclear
PTVIKVQNMPFTVSVDEILDFFYGYQVIPGSVCLKYNEKGMPTGEAMVAFESRDEAMAAVVDLNDRPIGS
RKVKLV
>gnl|CDD|410146 cd12752, RRM1_RBM5, RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding protein 5 (RBM5). This subgroup corresponds to the RRM1 of RBM5, also termed protein G15, or putative tumor suppressor LUCA15, or renal carcinoma antigen NY-REN-9, a known modulator of apoptosis. It may also act as a tumor suppressor or an RNA splicing factor. RBM5 shows high sequence similarity to RNA-binding protein 6 (RBM6 or NY-LU-12 or g16 or DEF-3). Both, RBM5 and RBM6, specifically bind poly(G) RNA. They contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, a nuclear localization signal, and a G-patch/D111 domain
DEKESKTIMLRGLPINITENDIRELIESFEGPQPADVRLMKRKTGVSRGFAFVEFYHLQDATSWMEANQK
KLVIQGKTIAMHYSNPR
>gnl|CDD|410147 cd12753, RRM1_RBM10, RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding protein 10 (RBM10). This subgroup corresponds to the RRM1 of RBM10, also termed G patch domain-containing protein 9, or RNA-binding protein S1-1 (S1-1), a paralog of putative tumor suppressor RNA-binding protein 5 (RBM5 or LUCA15 or H37). It may play an important role in mRNA generation, processing and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. RBM10 is structurally related to RBM5 and RNA-binding protein 6 (RBM6 or NY-LU-12 or g16 or DEF-3). It contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, and a G-patch/D111 domain
SNIIMLRMLPQSATENDIRGQLQAHGVQPREVRLMRNKSSGQSRGFAFVEFNHLQDATRWMEANQHSLTI
LGQKVSMHYSDPKP
>gnl|CDD|410148 cd12754, RRM2_RBM10, RNA recognition motif 2 (RRM2) found in vertebrate RNA-binding protein 10 (RBM10). This subgroup corresponds to the RRM2 of RBM10, also termed G patch domain-containing protein 9, or RNA-binding protein S1-1 (S1-1), a paralog of putative tumor suppressor RNA-binding protein 5 (RBM5 or LUCA15 or H37). It may play an important role in mRNA generation, processing and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. RBM10 is structurally related to RBM5 and RNA-binding protein 6 (RBM6 or NY-LU-12 or g16 or DEF-3). It contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, and a G-patch/D111 domain
ANDTIILRNLNPHSTMDSILSALAPYAVLSSSNVRVIKDKQTQLNRGFAFIQLSTIVEAAQLLQILQALH
PPLTIDGKTINVEFAKG
>gnl|CDD|410149 cd12755, RRM2_RBM5, RNA recognition motif 2 (RRM2) found in vertebrate RNA-binding protein 5 (RBM5). This subgroup corresponds to the RRM2 of RBM5, also termed protein G15, or putative tumor suppressor LUCA15, or renal carcinoma antigen NY-REN-9, a known modulator of apoptosis. It may also act as a tumor suppressor or an RNA splicing factor. RBM5 shows high sequence similarity to RNA-binding protein 6 (RBM6 or NY-LU-12 or g16 or DEF-3). Both, RBM5 and RBM6, specifically bind poly(G) RNA. They contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, a nuclear localization signal, and a G-patch/D111 domain
YSDTIILRNIAPHTVVDSIMTALSPYASLAVNNIRLIKDKQTQQNRGFAFVQLSSALEASQLLQILQSLH
PPLKIDGKTIGVDFAK
>gnl|CDD|410150 cd12756, RRM1_hnRNPD, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) and similar proteins. This subgroup corresponds to the RRM1 of hnRNP D0, also termed AU-rich element RNA-binding protein 1, which is a UUAG-specific nuclear RNA binding protein that may be involved in pre-mRNA splicing and telomere elongation. hnRNP D0 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), in the middle and an RGG box rich in glycine and arginine residues in the C-terminal part. Each of RRMs can bind solely to the UUAG sequence specifically
MFIGGLSWDTTKKDLKDYFSKFGEVVDCTLKLDPITGRSRGFGFVLFKESESVDKVMDQKEHKLNGKVID
PKRA
>gnl|CDD|410151 cd12757, RRM1_hnRNPAB, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein A/B (hnRNP A/B) and similar proteins. This subgroup corresponds to the RRM1 of hnRNP A/B, also termed APOBEC1-binding protein 1 (ABBP-1), which is an RNA unwinding protein with a high affinity for G- followed by U-rich regions. hnRNP A/B has also been identified as an APOBEC1-binding protein that interacts with apolipoprotein B (apoB) mRNA transcripts around the editing site and thus plays an important role in apoB mRNA editing. hnRNP A/B contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a long C-terminal glycine-rich domain that contains a potential ATP/GTP binding loop
EEDAGKMFVGGLSWDTSKKDLKDYFTKFGEVVDCTIKMDPNTGRSRGFGFILFKDAASVDKVLEQKEHRL
DGRVIDPKKA
>gnl|CDD|410152 cd12758, RRM1_hnRPDL, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein D-like (hnRNP D-like or hnRNP DL) and similar proteins. This subgroup corresponds to the RRM1 of hnRNP DL (or hnRNP D-like), also termed AU-rich element RNA-binding factor, or JKT41-binding protein (protein laAUF1 or JKTBP), which is a dual functional protein that possesses DNA- and RNA-binding properties. It has been implicated in mRNA biogenesis at the transcriptional and post-transcriptional levels. hnRNP DL binds single-stranded DNA (ssDNA) or double-stranded DNA (dsDNA) in a non-sequencespecific manner, and interacts with poly(G) and poly(A) tenaciously. It contains two putative two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a glycine- and tyrosine-rich C-terminus
KMFIGGLSWDTSKKDLTEYLSRFGEVVDCTIKTDPVTGRSRGFGFVLFKDAASVDKVLELKEHKLDGKLI
DPKRAK
>gnl|CDD|241203 cd12759, RRM1_MSI1, RNA recognition motif 1 (RRM1) found in RNA-binding protein Musashi homolog 1 (Musashi-1) and similar proteins. This subgroup corresponds to the RRM1 of Musashi-1. The mammalian MSI1 gene encoding Musashi-1 (also termed Msi1) is a neural RNA-binding protein putatively expressed in central nervous system (CNS) stem cells and neural progenitor cells and associated with asymmetric divisions in neural progenitor cells. Musashi-1 is evolutionarily conserved from invertebrates to vertebrates. It is a homolog of Drosophila Musashi and Xenopus laevis nervous system-specific RNP protein-1 (Nrp-1). Musashi-1 has been implicated in the maintenance of the stem-cell state, differentiation, and tumorigenesis. It translationally regulates the expression of a mammalian numb gene by binding to the 3'-untranslated region of mRNA of Numb, encoding a membrane-associated inhibitor of Notch signaling, and further influences neural development. Moreover, it represses translation by interacting with the poly(A)-binding protein and competes for binding of the eukaryotic initiation factor-4G (eIF-4G). Musashi-1 contains two conserved N-terminal tandem RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), along with other domains of unknown function
CKMFIGGLSWQTTQEGLREYFGQFGEVKECLVMRDPLTKRSRGFGFVTFMDQAGVDKVLAQSRHELDSKT
IDPKVAF
>gnl|CDD|410153 cd12760, RRM1_MSI2, RNA recognition motif 1 (RRM1) found in RNA-binding protein Musashi homolog 2 (Musashi-2) and similar proteins. This subgroup corresponds to the RRM2 of Musashi-2 (also termed Msi2) which has been identified as a regulator of the hematopoietic stem cell (HSC) compartment and of leukemic stem cells after transplantation of cells with loss and gain of function of the gene. It influences proliferation and differentiation of HSCs and myeloid progenitors, and further modulates normal hematopoiesis and promotes aggressive myeloid leukemia. Musashi-2 contains two conserved N-terminal tandem RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), along with other domains of unknown function
QHDPGKMFIGGLSWQTSPDSLRDYFSKFGEIRECMVMRDPTTKRSRGFGFVTFADPASVDKVLAQPHHEL
DSKTIDPKVAFPRRAQPKMVTRT
>gnl|CDD|410154 cd12761, RRM1_hnRNPA1, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) and similar proteins. This subgroup corresponds to the RRM1 of hnRNP A1, also termed helix-destabilizing protein, or single-strand RNA-binding protein, or hnRNP core protein A1, and is an abundant eukaryotic nuclear RNA-binding protein that may modulate splice site selection in pre-mRNA splicing. hnRNP A1 has been characterized as a splicing silencer, often acting in opposition to an activating hnRNP H. It silences exons when bound to exonic elements in the alternatively spliced transcripts of c-src, HIV, GRIN1, and beta-tropomyosin. hnRNP A1 can shuttle between the nucleus and the cytoplasm. Thus, it may be involved in transport of cellular RNAs, including the packaging of pre-mRNA into hnRNP particles and transport of poly A+ mRNA from the nucleus to the cytoplasm. The cytoplasmic hnRNP A1 has high affinity with AU-rich elements, whereas the nuclear hnRNP A1 has high affinity with a polypyrimidine stretch bordered by AG at the 3' ends of introns. hnRNP A1 is also involved in the replication of an RNA virus, such as mouse hepatitis virus (MHV), through an interaction with the transcription-regulatory region of viral RNA. hnRNP A1, together with the scaffold protein septin 6, serves as host protein to form a complex with NS5b and viral RNA, and further plays important roles in the replication of Hepatitis C virus (HCV). hnRNP A1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a long glycine-rich region at the C-terminus. The RRMs of hnRNP A1 play an important role in silencing the exon and the glycine-rich domain is responsible for protein-protein interactions
QLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDG
RVVEPKRAVSR
>gnl|CDD|410155 cd12762, RRM1_hnRNPA2B1, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP A2/B1) and similar proteins. This subgroup corresponds to the RRM1 of hnRNP A2/B1 which is an RNA trafficking response element-binding protein that interacts with the hnRNP A2 response element (A2RE). Many mRNAs, such as myelin basic protein (MBP), myelin-associated oligodendrocytic basic protein (MOBP), carboxyanhydrase II (CAII), microtubule-associated protein tau, and amyloid precursor protein (APP) are trafficked by hnRNP A2/B1. hnRNP A2/B1 also functions as a splicing factor that regulates alternative splicing of the tumor suppressors, such as BIN1, WWOX, the antiapoptotic proteins c-FLIP and caspase-9B, the insulin receptor (IR), and the RON proto-oncogene among others. Moreover, the overexpression of hnRNP A2/B1 has been described in many cancers. It functions as a nuclear matrix protein involving in RNA synthesis and the regulation of cellular migration through alternatively splicing pre-mRNA. It may play a role in tumor cell differentiation. hnRNP A2/B1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a long glycine-rich region at the C-terminus
QFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDG
RVVEPKRAVAR
>gnl|CDD|410156 cd12763, RRM1_hnRNPA3, RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein A3 (hnRNP A3) and similar proteins. This subgroup corresponds to the RRM1 of hnRNP A3 which is a novel RNA trafficking response element-binding protein that interacts with the hnRNP A2 response element (A2RE) independently of hnRNP A2 and participates in the trafficking of A2RE-containing RNA. hnRNP A3 can shuttle between the nucleus and the cytoplasm. It contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a long glycine-rich region at the C-terminus
QLRKLFIGGLSFETTDDSLREHFEQWGTLTDCVVMRDPQTKRSRGFGFVTYSCVEEVDAAMSARPHKVDG
RVVEPKRAVSR
>gnl|CDD|410157 cd12764, RRM2_SRSF4, RNA recognition motif 2 (RRM2) found in vertebrate serine/arginine-rich splicing factor 4 (SRSF4). This subgroup corresponds to the RRM2 of SRSF4, also termed pre-mRNA-splicing factor SRp75, or SRP001LB, or splicing factor, arginine/serine-rich 4 (SFRS4), a splicing regulatory serine/arginine (SR) protein that plays an important role in both constitutive splicing and alternative splicing of many pre-mRNAs. For instance, it interacts with heterogeneous nuclear ribonucleoproteins, hnRNP G and hnRNP E2, and further regulates the 5' splice site of tau exon 10, whose misregulation causes frontotemporal dementia. SFRS4 also induces production of HIV-1 vpr mRNA through the inhibition of the 5'-splice site of exon 3. In addition, SRSF4 activates splicing of the cardiac troponin T (cTNT) alternative exon by direct interactions with the cTNT exon 5 enhancer RNA. SRSF4 can shuttle between the nucleus and cytoplasm. It contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a glycine-rich region, an internal region homologous to the RRM, and a very long, highly phosphorylated C-terminal RS domains rich in serine-arginine dipeptides
GRDKYGPPTRTEYRLIVENLSSRCSWQDLKDYMRQAGEVTYADAHKGRKNEGVIEFVSYSDMKRALEKLD
GTEVNGRKIRLVEDKPGSRRRRSYSRS
>gnl|CDD|410158 cd12765, RRM2_SRSF5, RNA recognition motif 2 (RRM2) found in vertebrate serine/arginine-rich splicing factor 5 (SRSF5). This subgroup corresponds to the RRM2 of SRSF5, also termed delayed-early protein HRS, or pre-mRNA-splicing factor SRp40, or splicing factor, arginine/serine-rich 5 (SFRS5), is an essential splicing regulatory serine/arginine (SR) protein that regulates both alternative splicing and basal splicing. It is the only SR protein efficiently selected from nuclear extracts (NE) by the splicing enhancer (ESE) and it is necessary for enhancer activation. SRSF5 also functions as a factor required for insulin-regulated splice site selection for protein kinase C (PKC) betaII mRNA. It is involved in the regulation of PKCbetaII exon inclusion by insulin via its increased phosphorylation by a phosphatidylinositol 3-kinase (PI 3-kinase) signaling pathway. Moreover, SRSF5 can regulate alternative splicing in exon 9 of glucocorticoid receptor pre-mRNA in a dose-dependent manner. SRSF5 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a C-terminal RS domains rich in serine-arginine dipeptides. The specific RNA binding by SRSF5 requires the phosphorylation of its SR domain
RNAPPMRTENRLIVENLSSRVSWQDLKDFMRQAGEVTFADAHRPKLNEGVVEFASYSDLKNAIEKLSGKE
INGRKIKLIEG
>gnl|CDD|410159 cd12766, RRM2_SRSF6, RNA recognition motif 2 (RRM2) found found in vertebrate serine/arginine-rich splicing factor 6 (SRSF6). This subgroup corresponds to the RRM2 of SRSF6, also termed pre-mRNA-splicing factor SRp55, an essential splicing regulatory serine/arginine (SR) protein that preferentially interacts with a number of purine-rich splicing enhancers (ESEs) to activate splicing of the ESE-containing exon. It is the only protein from HeLa nuclear extract or purified SR proteins that specifically binds B element RNA after UV irradiation. SRSF6 may also recognize different types of RNA sites. For instance, it does not bind to the purine-rich sequence in the calcitonin-specific ESE, but binds to a region adjacent to the purine tract. Moreover, cellular levels of SRSF6 may control tissue-specific alternative splicing of the calcitonin/ calcitonin gene-related peptide (CGRP) pre-mRNA. SRSF6 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a C-terminal RS domains rich in serine-arginine dipeptides
YRLIVENLSSRCSWQDLKDFMRQAGEVTYADAHKERTNEGVIEFRSYSDMKRALEKLDGTEINGRKIRLV
EDK
>gnl|CDD|410160 cd12767, RRM2_SRSF1, RNA recognition motif 2 (RRM2) found in serine/arginine-rich splicing factor 1 (SRSF1) and similar proteins. This subgroup corresponds to the RRM2 of SRSF1, also termed alternative-splicing factor 1 (ASF-1), or pre-mRNA-splicing factor SF2, P33 subunit, a splicing regulatory serine/arginine (SR) protein involved in constitutive and alternative splicing, nonsense-mediated mRNA decay (NMD), mRNA export and translation. It also functions as a splicing-factor oncoprotein that regulates apoptosis and proliferation to promote mammary epithelial cell transformation. SRSF1 is a shuttling SR protein and contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), separated by a long glycine-rich spacer, and a C-terminal SR domains rich in serine-arginine dipeptides
GPPSRRSEYRVVVSGLPPSGSWQDLKDHMREAGDVCYADVFRDGTGVVEFVRKEDMTYAVRKLDNTKFRS
HEGETAYIRVKVDG
>gnl|CDD|410161 cd12768, RRM2_SRSF9, RNA recognition motif 2 (RRM2) found in vertebrate serine/arginine-rich splicing factor 9 (SRSF9). This subgroup corresponds to the RRM2 of SRSF9, also termed pre-mRNA-splicing factor SRp30C, an essential splicing regulatory serine/arginine (SR) protein that has been implicated in the activity of many elements that control splice site selection, the alternative splicing of the glucocorticoid receptor beta in neutrophils and in the gonadotropin-releasing hormone pre-mRNA. SRSF9 can also interact with other proteins implicated in alternative splicing, including YB-1, rSLM-1, rSLM-2, E4-ORF4, Nop30, and p32. SRSF9 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by an unusually short C-terminal RS domains rich in serine-arginine dipeptides
GPPSRRSEFRVLVSGLPPSGSWQDLKDHMREAGDVCYADVQKDGMGIVEFLRKEDMEYALRKLDDTKFRS
HEGETSYIRVSPER
>gnl|CDD|410162 cd12769, RRM1_HuR, RNA recognition motif 1 (RRM1) found in vertebrate Hu-antigen R (HuR). This subgroup corresponds to the RRM1 of HuR, also termed ELAV-like protein 1 (ELAV-1), a ubiquitously expressed Hu family member. It has a variety of biological functions mostly related to the regulation of cellular response to DNA damage and other types of stress. HuR has an anti-apoptotic function during early cell stress response; it binds to mRNAs and enhances the expression of several anti-apoptotic proteins, such as p21waf1, p53, and prothymosin alpha. Meanwhile, HuR also has pro-apoptotic function by promoting apoptosis when cell death is unavoidable. Furthermore, HuR may be important in muscle differentiation, adipogenesis, suppression of inflammatory response and modulation of gene expression in response to chronic ethanol exposure and amino acid starvation. Like other Hu proteins, HuR contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an AU-rich RNA element (ARE). RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
GRTNLIVNYLPQNMTQDELRSLFSSIGEVESAKLIRDKVAGHSLGYGFVNYVTAKDAERAINTLNGLRLQ
SKTIKVSYARPS
>gnl|CDD|410163 cd12770, RRM1_HuD, RNA recognition motif 1 (RRM1) found in vertebrate Hu-antigen D (HuD). This subgroup corresponds to the RRM1 of HuD, also termed ELAV-like protein 4 (ELAV-4), or paraneoplastic encephalomyelitis antigen HuD, one of the neuronal members of the Hu family. The neuronal Hu proteins play important roles in neuronal differentiation, plasticity and memory. HuD has been implicated in various aspects of neuronal function, such as the commitment and differentiation of neuronal precursors as well as synaptic remodeling in mature neurons. HuD also functions as an important regulator of mRNA expression in neurons by interacting with AU-rich RNA element (ARE) and stabilizing multiple transcripts. Moreover, HuD regulates the nuclear processing/stability of N-myc pre-mRNA in neuroblastoma cells, as well as the neurite elongation and morphological differentiation. HuD specifically binds poly(A) RNA. Like other Hu proteins, HuD contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an ARE. RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
KTNLIVNYLPQNMTQEEFRSLFGSIGEIESCKLVRDKITGQSLGYGFVNYIDPKDAEKAINTLNGLRLQT
KTIKVSYARPS
>gnl|CDD|410164 cd12771, RRM1_HuB, RNA recognition motif 1 (RRM1) found in vertebrate Hu-antigen B (HuB). This subgroup corresponds to the RRM1 of HuB, also termed ELAV-like protein 2 (ELAV-2), or ELAV-like neuronal protein 1, or nervous system-specific RNA-binding protein Hel-N1 (Hel-N1), one of the neuronal members of the Hu family. The neuronal Hu proteins play important roles in neuronal differentiation, plasticity and memory. HuB is also expressed in gonads and is up-regulated during neuronal differentiation of embryonic carcinoma P19 cells. Like other Hu proteins, HuB contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an AU-rich RNA element (ARE). RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
EDSKTNLIVNYLPQNMTQEELKSLFGSIGEIESCKLVRDKITGQSLGYGFVNYIEPKDAEKAINTLNGLR
LQTKTIKVSYARP
>gnl|CDD|410165 cd12772, RRM1_HuC, RNA recognition motif 1 (RRM1) found in vertebrate Hu-antigen C (HuC). This subgroup corresponds to the RRM1 of HuC, also termed ELAV-like protein 3 (ELAV-3), or paraneoplastic cerebellar degeneration-associated antigen, or paraneoplastic limbic encephalitis antigen 21 (PLE21), one of the neuronal members of the Hu family. The neuronal Hu proteins play important roles in neuronal differentiation, plasticity and memory. Like other Hu proteins, HuC contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an AU-rich RNA element (ARE). The AU-rich element binding of HuC can be inhibited by flavonoids. RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
DDSKTNLIVNYLPQNMTQEEFKSLFGSIGDIESCKLVRDKITGQSLGYGFVNYVDPNDADKAINTLNGLK
LQTKTIKVSYARPSS
>gnl|CDD|410166 cd12773, RRM2_HuR, RNA recognition motif 2 (RRM2) found in vertebrate Hu-antigen R (HuR). This subgroup corresponds to the RRM2 of HuR, also termed ELAV-like protein 1 (ELAV-1), the ubiquitously expressed Hu family member. It has a variety of biological functions mostly related to the regulation of cellular response to DNA damage and other types of stress. HuR has an anti-apoptotic function during early cell stress response. It binds to mRNAs and enhances the expression of several anti-apoptotic proteins, such as p21waf1, p53, and prothymosin alpha. HuR also has pro-apoptotic function by promoting apoptosis when cell death is unavoidable. Furthermore, HuR may be important in muscle differentiation, adipogenesis, suppression of inflammatory response and modulation of gene expression in response to chronic ethanol exposure and amino acid starvation. Like other Hu proteins, HuR contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an AU-rich RNA element (ARE). RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
ANLYISGLPRTMTQKDVEDMFSRFGRIINSRVLVDQATGLSRGVAFIRFDKRSEAEEAITNFNGHKPPGS
SEPITVKFAANPNQ
>gnl|CDD|410167 cd12774, RRM2_HuD, RNA recognition motif 2 (RRM2) found in vertebrate Hu-antigen D (HuD). This subgroup corresponds to the RRM2 of HuD, also termed ELAV-like protein 4 (ELAV-4), or paraneoplastic encephalomyelitis antigen HuD, one of the neuronal members of the Hu family. The neuronal Hu proteins play important roles in neuronal differentiation, plasticity and memory. HuD has been implicated in various aspects of neuronal function, such as the commitment and differentiation of neuronal precursors as well as synaptic remodeling in mature neurons. HuD also functions as an important regulator of mRNA expression in neurons by interacting with AU-rich RNA element (ARE) and stabilizing multiple transcripts. Moreover, HuD regulates the nuclear processing/stability of N-myc pre-mRNA in neuroblastoma cells and also regulates the neurite elongation and morphological differentiation. HuD specifically binds poly(A) RNA. Like other Hu proteins, HuD contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an ARE. RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
ASIRDANLYVSGLPKTMTQKELEQLFSQYGRIITSRILVDQVTGVSRGVGFIRFDKRIEAEEAIKGLNGQ
KPSGATEPITVKFA
>gnl|CDD|410168 cd12775, RRM2_HuB, RNA recognition motif 2 (RRM2) found in vertebrate Hu-antigen B (HuB). This subgroup corresponds to the RRM2 of HuB, also termed ELAV-like protein 2 (ELAV-2), or ELAV-like neuronal protein 1, or nervous system-specific RNA-binding protein Hel-N1 (Hel-N1), one of the neuronal members of the Hu family. The neuronal Hu proteins play important roles in neuronal differentiation, plasticity and memory. HuB is also expressed in gonads. It is up-regulated during neuronal differentiation of embryonic carcinoma P19 cells. Like other Hu proteins, HuB contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an AU-rich RNA element (ARE). RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
ASIRDANLYVSGLPKTMTQKELEQLFSQYGRIITSRILVDQVTGVSRGVGFIRFDKRIEAEEAIKGLNGQ
KPPGATEPITVKFA
>gnl|CDD|241220 cd12776, RRM2_HuC, RNA recognition motif 2 (RRM2) found in vertebrate Hu-antigen C (HuC). This subgroup corresponds to the RRM2 of HuC, also termed ELAV-like protein 3 (ELAV-3), or paraneoplastic cerebellar degeneration-associated antigen, or paraneoplastic limbic encephalitis antigen 21 (PLE21), one of the neuronal members of the Hu family. The neuronal Hu proteins play important roles in neuronal differentiation, plasticity and memory. Like other Hu proteins, HuC contains three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 may cooperate in binding to an AU-rich RNA element (ARE). The AU-rich element binding of HuC can be inhibited by flavonoids. RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions
DANLYVSGLPKTMSQKEMEQLFSQYGRIITSRILVDQVTGVSRGVGFIRFDKRIEAEEAIKGLNGQKPLG
AAEPITVKFAN
>gnl|CDD|410169 cd12777, RRM1_PTBP1, RNA recognition motif 1 (RRM1) found in vertebrate polypyrimidine tract-binding protein 1 (PTB). This subgroup corresponds to the RRM1 of PTB, also known as 58 kDa RNA-binding protein PPTB-1 or heterogeneous nuclear ribonucleoprotein I (hnRNP I), an important negative regulator of alternative splicing in mammalian cells. PTB also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. PTB contains four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain). RRM1 and RRM2 are independent from each other and separated by flexible linkers. By contrast, there is an unusual and conserved interdomain interaction between RRM3 and RRM4. It is widely held that only RRMs 3 and 4 are involved in RNA binding and RRM2 mediates PTB homodimer formation. However, new evidence shows that the RRMs 1 and 2 also contribute substantially to RNA binding. Moreover, PTB may not always dimerize to repress splicing. It is a monomer in solution
RVIHVRKLPNDVTEAEVISLGLPFGKVTNLLMLKGKNQAFIEMNTEEAANTMVNYYTSVTPVLRGQPIYI
QFSNHKELKTD
>gnl|CDD|410170 cd12778, RRM1_PTBP2, RNA recognition motif 1 (RRM1) found in vertebrate polypyrimidine tract-binding protein 2 (PTBP2). This subgroup corresponds to the RRM1 of PTBP2, also known as neural polypyrimidine tract-binding protein or neurally-enriched homolog of PTB (nPTB), highly homologous to polypyrimidine tract binding protein (PTB) and perhaps specific to the vertebrates. Unlike PTB, PTBP2 is enriched in the brain and in some neural cell lines. It binds more stably to the downstream control sequence (DCS) RNA than PTB does but is a weaker repressor of splicing in vitro. PTBP2 also greatly enhances the binding of two other proteins, heterogeneous nuclear ribonucleoprotein (hnRNP) H and KH-type splicing-regulatory protein (KSRP), to the DCS RNA. The binding properties of PTBP2 and its reduced inhibitory activity on splicing imply roles in controlling the assembly of other splicing-regulatory proteins. PTBP2 contains four RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
SRVLHIRKLPGEVTETEVIALGLPFGKVTNILMLKGKNQAFLELATEEAAITMVNYYTAVTPHLRNQPIY
IQYSNHKELKTD
>gnl|CDD|410171 cd12779, RRM1_ROD1, RNA recognition motif 1 (RRM1) found in vertebrate regulator of differentiation 1 (Rod1). This subgroup corresponds to the RRM1 of ROD1 coding protein Rod1, a mammalian polypyrimidine tract binding protein (PTB) homolog of a regulator of differentiation in the fission yeast Schizosaccharomyces pombe, where the nrd1 gene encodes an RNA binding protein that negatively regulates the onset of differentiation. ROD1 is predominantly expressed in hematopoietic cells or organs. It might play a role controlling differentiation in mammals. Rod1 contains four repeats of RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain) and does have RNA binding activities
PCSPSRVLHIRKIPNDVTEAEVISLGLPFGKVTNLLMLKGKNQAFLEMASEEAAVTMVNYYTTVTPHLRN
QPVYIQYSNHRELKTDNLPN
>gnl|CDD|410172 cd12780, RRM1_hnRNPL, RNA recognition motif 1 (RRM1) found in vertebrate heterogeneous nuclear ribonucleoprotein L (hnRNP-L). This subgroup corresponds to the RRM1 of hnRNP-L, a higher eukaryotic specific subunit of human KMT3a (also known as HYPB or hSet2) complex required for histone H3 Lys-36 trimethylation activity. It plays both, nuclear and cytoplasmic, roles in mRNA export of intronless genes, IRES-mediated translation, mRNA stability, and splicing. hnRNP-L shows significant sequence homology to polypyrimidine tract-binding protein (PTB or hnRNP I). Both, hnRNP-L and PTB, are localized in the nucleus but excluded from the nucleolus. hnRNP-L is an RNA-binding protein with three RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
PSPVVHIRGLIDGVVEADLVEALQEFGTISYVVVMPKKRQALVEFEDILGACNAVNYAADNQIYIAGHPA
FVNYSTSQKI
>gnl|CDD|410173 cd12781, RRM1_hnRPLL, RNA recognition motif 1 (RRM1) found in vertebrate heterogeneous nuclear ribonucleoprotein L-like (hnRNP-LL). This subgroup corresponds to the RRM1 of hnRNP-LL, which plays a critical and unique role in the signal-induced regulation of CD45 and acts as a global regulator of alternative splicing in activated T cells. It is closely related in domain structure and sequence to heterogeneous nuclear ribonucleoprotein L (hnRNP-L), which is an abundant nuclear, multifunctional RNA-binding protein with three RNA-recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
SVSPVVHVRGLCESVVEADLVEALEKFGTICYVMMMPFKRQALVEFENVESAKKCVTFAADEPVYIAGQQ
AFFNYSTSKRITRP
>gnl|CDD|410174 cd12782, RRM2_PTBP1, RNA recognition motif 2 (RRM2) found in vertebrate polypyrimidine tract-binding protein 1 (PTB). This subgroup corresponds to the RRM2 of PTB, also known as 58 kDa RNA-binding protein PPTB-1 or heterogeneous nuclear ribonucleoprotein I (hnRNP I), an important negative regulator of alternative splicing in mammalian cells. PTB also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. PTB contains four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain). RRM1 and RRM2 are independent from each other and separated by flexible linkers. By contrast, there is an unusual and conserved interdomain interaction between RRM3 and RRM4. It is widely held that only RRMs 3 and 4 are involved in RNA binding and RRM2 mediates PTB homodimer formation. However, new evidence shows that the RRMs 1 and 2 also contribute substantially to RNA binding. Moreover, PTB may not always dimerize to repress splicing. It is a monomer in solution
MAGQSPVLRIIVENLFYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVSAQHAKLSLDGQNI
YNACCTLRIDFSKLTSLNVKYNNDKSRDYTRPDLPSGD
>gnl|CDD|410175 cd12783, RRM2_PTBP2, RNA recognition motif 2 (RRM2) found in vertebrate polypyrimidine tract-binding protein 2 (PTBP2). This subgroup corresponds to the RRM2 of PTBP2, also known as neural polypyrimidine tract-binding protein or neurally-enriched homolog of PTB (nPTB), highly homologous to polypyrimidine tract binding protein (PTB) and perhaps specific to the vertebrates. Unlike PTB, PTBP2 is enriched in the brain and in some neural cell lines. It binds more stably to the downstream control sequence (DCS) RNA than PTB does but is a weaker repressor of splicing in vitro. PTBP2 also greatly enhances the binding of two other proteins, heterogeneous nuclear ribonucleoprotein (hnRNP) H and KH-type splicing-regulatory protein (KSRP), to the DCS RNA. The binding properties of PTBP2 and its reduced inhibitory activity on splicing imply roles in controlling the assembly of other splicing-regulatory proteins. PTBP2 contains four RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
SPVLRIIIDNMYYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALLQYGDPVNAQQAKLALDGQNIYNAC
CTLRIDFSKLVNLNVKYNNDKSRDYTRPDLPSGDGQP
>gnl|CDD|410176 cd12784, RRM2_ROD1, RNA recognition motif 2 (RRM2) found in vertebrate regulator of differentiation 1 (Rod1). This subgroup corresponds to the RRM2 of ROD1 coding protein Rod1, a mammalian polypyrimidine tract binding protein (PTB) homolog of a regulator of differentiation in the fission yeast Schizosaccharomyces pombe, where the nrd1 gene encodes an RNA binding protein and negatively regulates the onset of differentiation. ROD1 is predominantly expressed in hematopoietic cells or organs. It might play a role controlling differentiation in mammals. Rod1 contains four repeats of RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain) and does have RNA binding activities
GQSPVLRIIVENLFYPVTLEVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPMNAHHAKVALDGQNIYN
ACCTLRIEFSKLTSLNVKYNNDKSRDFTRLDLPSGDGQ
>gnl|CDD|410177 cd12785, RRM2_hnRNPL, RNA recognition motif 2 (RRM2) found in vertebrate heterogeneous nuclear ribonucleoprotein L (hnRNP-L). This subgroup corresponds to the RRM2 of hnRNP-L, a higher eukaryotic specific subunit of human KMT3a (also known as HYPB or hSet2) complex required for histone H3 Lys-36 trimethylation activity. It plays both, nuclear and cytoplasmic, roles in mRNA export of intronless genes, IRES-mediated translation, mRNA stability, and splicing. hnRNP-L shows significant sequence homology to polypyrimidine tract-binding protein (PTB or hnRNP I). Both hnRNP-L and PTB are localized in the nucleus but excluded from the nucleolus. hnRNP-L is an RNA-binding protein with three RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
RSVNNVLLFTILNPIYSITTDVLYTICNPCGPVQRIVIFRKNGVQAMVEFDSVQSAQRAKASLNGADIYS
GCCTLKIEYAKPTRLNVFKNDQDTWDYTNP
>gnl|CDD|241230 cd12786, RRM2_hnRPLL, RNA recognition motif 2 (RRM2) found in vertebrate heterogeneous nuclear ribonucleoprotein L-like (hnRNP-LL). The subgroup corresponds to the RRM2 of hnRNP-LL which plays a critical and unique role in the signal-induced regulation of CD45 and acts as a global regulator of alternative splicing in activated T cells. It is closely related in domain structure and sequence to heterogeneous nuclear ribonucleoprotein L (hnRNP-L), which is an abundant nuclear, multifunctional RNA-binding protein with three RNA-recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain)
GNKVLLLSIQNPLYPITVDVLYTVCNPVGKVQRIVIFKRNGIQAMVEFESVECAQKAKAALNGADIYAGC
CTLKIEYARPTRLNVIRNDNDSWDYT
>gnl|CDD|213347 cd12787, RasGAP_plexin_B, Ras-GTPase Activating Domain of type B plexins. Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Plexins are divided into four types (A-D) according to sequence similarity.There are three members of the Plexin-B subfamily, namely B1, B2 and B3. Plexins-B1, B2 and B3 are receptors for Sema4D, Sema4C and Sema4G, and Sema5A, respectively. The activation of plexin-B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. By signaling the effect of Sema4C and Sema4G, the plexin-B2 receptor is critically involved in neural tube closure and cerebellar granule cell development. Plexin-B3, the receptor of Sema5A, is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin-B3 has been linked to verbal performance and white matter volume in human brain. Small GTPases play important roles in plexin-B signaling. Plexin-B1 activates Rho through Rho-specific guanine nucleotide exchange factors, leading to neurite retraction. Plexin-B1 possesses an intrinsic GTPase-activating protein activity for R-Ras and induces growth cone collapse through R-Ras inactivation. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator
GIPFLDYKTYAERVFFPGHKDGPLDVMIKLDIPEPRRPTVEQGLYQLSNLLNSKLFLINFIHTLENQREF
SARDRVYVASLLTVALHGKLEYYTDIMRTLLLDLLAQYVVKNPKLMLRRTETVVEKLLTNWMSICLYQFL
RDSAGEPLYMLFRAIKHQVDKGPVDAVTGKRAKAIPEIYLTRLLSMKGTLQKFVDDFFQSILSPGRPVPP
AVKYFFDLLDEQAEKHGIQDEDTIHIWKTNSLPLRFWVNILKNPQFIFDVHVSDNVDASLSVIAQTFMDA
CTRTEHKLGRDSPSNKLLYAREIPRYKKMVERYYADIRQMVPASDQEMNSHLAELSRNYTDSLNTLVALH
ELYQYIQKYYDQIINALEEDPAAQKMQLAFRLQQIAAAVEN
>gnl|CDD|213348 cd12788, RasGAP_plexin_D1, Ras-GTPase Activating Domain of plexin-D1. Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Plexins are divided into four types (A-D) according to sequence similarity. Plexin-D1 has been identified as the receptor of Sema3E. It binds to Sema3E directly with high affinity. Sema3E is implicated in axonal path finding and inhibition of developmental and postischemic angiogenesis. Plexin-D1 is broadly expressed on tumor vessels and tumor cells in a number of different types of human tumors. The Plexin-D1 and Sema3E interaction inhibits tumor growth but promotes invasiveness and metastasis. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator
QGIPFLEYKHFVTRTFFPKCSSLYEERYVLPSQENNSQGPRQVPETHPLLQEWKIPESCRPNMEEGITLF
STLLNNKHFLVTFVHALEQQKDFAVRDRCNLASLLTIALHGKLEYYTSIMKDLLVDLIDASASKNPKLML
RRTESVVEKMLTNWMSICMYSYLRETVGEPFFLLLCAIKQQINKGSIDAIKKVLPEIYLTRLLSTKGTLQ
KFLDDLFQAILSIPEDRPPLAVKYFFDFLEEQAEKRGITDPDTLHIWKTNSLPLRFWVNILKNPQFVFDI
DKTDHMDACLSVIAQAFIDACSISDLQLGKDSPTNKLLYAKEIPEYRKIVQRYYQQIQEMPPLSEQEMNA
HLAEESRKYRNEFNTNVAMAEIYKYAKRYRAQIVSALESNPTARRTQLQHKFEQVIALMEDNIYECSSE
>gnl|CDD|213349 cd12789, RasGAP_plexin_C1, Ras-GTPase Activating Domain of plexin-C1. Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Plexins are divided into four types (A-D) according to sequence similarity. Plexin-C1 has been identified as the receptor of semaphorin 7A, which plays regulatory roles in both the immune and nervous systems. Unlike other semaphorins which act as repulsive guidance cues, Sema7A enhances central and peripheral axon growth and is required for proper axon tract formation during embryonic development. Plexin-C1 is a potential tumor suppressor for melanoma progression. The expression of Plexin-C1 is diminished or absent in human melanoma cell lines. Cofilin, an actin-binding protein involved in cell migration, is a downstream target of Sema7A and Plexin-C1 signaling. Melanoma invasion and metastasis may be promoted through the loss of Plexin-C1 inhibitory signaling on cofilin activation. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator
FGTVPFLDYKHFALRTFFPESGGFTHIFTRDDPHDRDQTDKDESLTALDKLICNKSFLVTLIHTLEKQKN
FSVKDRCLFASFLTIALQTKLVYLTEILEVLTKDLMDQSSNAQPKLLLRRTESVVEKLLTNWMSVCLSGF
LRETVGEPFYLLVTTLNQKINKGPVDVIKFKVKEMYLTKLLSTKVAIHSVVEKLFRSIWSLPNNKAPVAI
KYFFDFLDAQAENKKITDPDVLHIWKTNSLPLRFWVNILKNPQFVFDIKKTPHLDGCLSVIAQAFMDSFS
LSEQHLGKEAPTNKLLYAKDIPQYKEEVKSYYKAIRDLPPLSSSELEEFLTQESKKHENEFNEEVALMEI
YKYIVKYFDEILNKLERERGLEEVQKQLLHVKALFDEKKKCKW
>gnl|CDD|213350 cd12790, RasGAP_plexin_A, Ras-GTPase Activating Domain of type A plexins. Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. They are divided into four types (A-D) according to sequence similarity. In vertebrates, there are four type A plexins (A1-A4) that serve as the co-receptors for neuropilins to mediate the signaling of class 3 semaphorins except Sema3E, which signals through Plexin-D1. Plexins serve as direct receptors for several other members of the semaphorin family: class 1 and class 6 semaphorins signal through type A plexins, which mediate diverse biological functions including axon guidance, cardiovascular development, and immune function. Guanylyl cyclase Gyc76C and Off-track kinase (OTK), a putative receptor tyrosine kinase, modulate Sema1a and Plexin-A mediated axon repulsion. In their complex with Sema6s, type A plexins serve as signal-transducing subunits. An increasing number of molecules that interact with the intracellular region of Plexin-A have been identified; among them are IgCAMs (in axon guidance events) and Trem2-DAP12 (in immune responses). Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator
GIPFLDYRTYAMRVLFPGIEDHPVLRELEVERDRQENVEKGLRLFGQLLMNKTFLLTFIRTLESQRSFSM
RDRGNVASLIMVVLQSKMEYATDILKQLLADLIEKNLESKNHPKLLLRRTESVAEKMLTNWFTFLLYKFL
KECAGEPLFMLFCAIKQQMEKGPIDAIKMVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAI
KYMFDFLDEQADQHGITDPEVVHTWKSNCLPLRFWVNLIKNPQFVFDIHKSSITDACLSVVAQTFMDSCS
TSEHRLGKDSPSNKLLYAKDIPNYKSWVERYYADIAKMPAISDQDMNAYLAEQSRLHLNEFNTLSALNEL
YSYVTKYKEEILTALEEDEFARKQRLAYKLEQVIN
>gnl|CDD|213351 cd12791, RasGAP_plexin_B3, Ras-GTPase Activating Domain of plexin-B3. Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Plexins are divided into four types (A-D) according to sequence similarity. Plexin-B3 is the receptor of semaphorin 5A. It is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin-B3 has been linked to verbal performance and white matter volume in human brain. Furthermore, Sema5A and plexin-B3 have been implicated in the progression of various types of cancer. They play an important role in the invasion and metastasis of gastric carcinoma. The protein and mRNA expression of Sema5A and its receptor plexin-B3 increased gradually in non-neoplastic mucosa, primary gastric carcinoma, and lymph node metastasis, and their expression is correlated. The stimulation of plexin-B3 by Sema5A binding in human glioma cells results in the inhibition of cell migration and invasion. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator
GIPFLDYRTYAERVFFPGHGGCPLQPSLEGDGEEGRRATVEQGLTQLSNLLNSKLFLLTLIHTLEEQPSF
SQRDRCHVASLLSLALHGKLEYLTDIMKTLLGDLAAHYVHKNPKLMLRRTETMVEKLLTNWMSICLYAFL
REVAGEPLYMLFRAIKYQVDKGPVDAVTGKRERAKAIPEIYLTRLLSMKGTLQKFVDDTFQAILSVNRPV
PIAVKYLFDFLDELAEKHGIEDPETLHIWKTNSLLLRFWVNTLKNPQFIFDVRVSDNVDAILAVIAQTFI
DSCTISEHKVGRDSPVNKLLYAREIPRYKQMVEKYYADIRQSSPASYQEMNSALTELSGNYTSAPHCLVA
LQELYNHIHRYYDQIISALEEDPVGQKMQLACRLQQIAALVENKVTD
>gnl|CDD|213352 cd12792, RasGAP_plexin_B2, Ras-GTPase Activating Domain of plexin-B2. Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Plexins are divided into four types (A-D) according to sequence similarity. Plexin-B2 serves as the receptor of Sema4C and Sema4G. By signaling the effect of Sema4C and Sema4G, the plexin-B2 receptor is critically involved in neural tube closure and cerebellar granule cell development. Mice lacking Plexin-B2 demonstrated defects in closure of the neural tube and disorganization of the embryonic brain. In developing kidney, Sema4C and Plexin-B2 signaling modulates ureteric branching. Plexin-B2 is expressed both in the pretubular aggregates and the ureteric epithelium in the developing kidney. Deletion of Plexin-B2 results in renal hypoplasia and occasional double ureters. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator
RIPFLDYKTYTDRVFFLPSKDGANDVMITGKLDIPEARRATVEQALNQFSNLLNSKTFLINFIHTLENQR
DFNARAKVYFASLLTVALHGKLEYYTDIMRTLLLELMEQYVHSKNPKLMLRRSETVVERMLSNWMSICLY
QYLKDTAGEPLYKLFKAIKHQVEKGPVDAVQKKKERTKAITEIYLTRLLSVKGTLQQFVDNFFRSVLCSG
AVVPPAVKYFFDFLDEQAEKHDIVDEETIHIWKTNSLPLRFWVNILKNPHFIFDVHVTEVVDASLSVIAQ
TFMDACTKTEHKLSRDSPSNKLLYAKEISTYKKMVDDYYKGIRQMVPVSDQDMNTHLAEISRAHTDKLNT
QVALHQLYQYASKYYDEIINSLEEDPAAQSKQLTLRLQQIAAALENKVTD
>gnl|CDD|213353 cd12793, RasGAP_plexin_B1, Ras-GTPase Activating Domain of plexin-B1. Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Plexins are divided into four types (A-D) according to sequence similarity. Plexin-B1 serves as the Semaphorin 4D receptor and functions as a regulator of developing neurons and a tumor suppressor protein for melanoma. The Sema4D and plexin-B1 signaling complex regulates dendritic and axonal complexity. The activation of Plexin-B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. As a tumor suppressor, plexin-B1 abrogates activation of the oncogenic receptor, c-Met, by its ligand, hepatocyte growth factor (HGF), in melanoma. Furthermore, plexin-B1 suppresses integrin-dependent migration and activation of pp125FAK and inhibits Rho activity. Plexin-B1 is highly expressed in endothelial cells and its activation by Sema4D elicits a potent proangiogenic response. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator
GIPFLDYRMYAERIFFPGHRESPLRRDLDVPECRRQTVEQGLVQLSNLLNSKLFLTKFIHTLESQRTFSP
RDRAYVASLLTVALHGKLEYFTDILKTLLNDLVEQYVAKNPKLMLRRTETVVEKLLTNWMSICLYTFLRD
SAGESLYMLFRAIKHQVDKGPVDAVTGKERAKAIPEIYLTRLLSMKGTLQKFVDDLFTVILSTSRPVPLA
VKYFFDLLDEQALQHGISDPETIHIWKTNSLPLRFWINIIKNPQFIFDVQTSDNVDAVLSVIAQTFMDSC
TIADHKLGRDSPINKLLYARDIPRYKQMVERYYADIRQTVSASDQEMNSALAELSRNYSGELNYLVALHE
LYKYINKYYDQIITALEEDSTAQKMQLGYRLQQIAAAVENKVTD
>gnl|CDD|240614 cd12794, Hsm3_like, Hsm3 is a yeast Proteasome chaperone of the 19S regulatory particle and related proteins. This group contains proteins related to the Hsm3 protein (Yeast Proteasome Interacting Protein) of Saccharomyces cerevisiae. S. cerevisiae Hsm3 is a chaperone of regulatory particles involved in proteasome assembly. The 26S Proteasome is a large, 2.5 MDa complex comprised of at least 33 subunits, and relies on chaperones to facilitate correct assembly. The proteasome contains a cylindrical 20S core particle and 1-2 19S regulatory particles, comprised of AAA-ATPase and non-ATPase subunits. The proteasome acts in ubiquitin-dependent proteolysis. The 19S RP targets and opens the the ubiquitin-tagged substrate and releases ubiquitin. Hsm3 acts as a 19S chaperone, binding to the C-terminal domain of Rpt1 (the 6 ATPase subunits of the 19 S regulatory particle(s). Hsm3 has a C-shape composed of 11 HEAT repeats. Mutations in the Hsm3-Rpt interface disrupt formation of the 26 S Proteasome complex
IQNLLDHLNTALETDPLPPVINKLIDKCSLNLKTITSLPVDLKQLLPAIKSILLDNESYEILDYDLLLEL
LDKILSLLSFDDILEVFSLEDLISALQSGNEPLVILACKVIAKSYPKGLFANTLIIDILLKLYFDEDTDI
SVVNAIEKLLSSLSSDELIRRRLLENNLPLLLSVRKSFNPISFSRLLDLLTILLPYISRSEFPDDLFIFT
TEEIFKSLEKDILLFILLVQYYTKLLDLIDITPDSKDWALRYILPILPYFGKIFKDREEYPDVKSFALSY
LFKLFAKLSYLDDESLFKTLDEDYLKISLENEYIIDFLSFINPQYLVKYHQDLIEDYLHVKPSYLPILRN
LIASEECFNLIKPNITSEKILALPYLEQMVLLEKLSQYEYSVKYLINNLPKVMSNLLDNGNGNITEPETV
ELRLEVLENLLNFDVEDLNVWYEPLLDEYALIVNG
>gnl|CDD|240613 cd12795, FILIA_N_like, FILIA-N KH-like domain. This group contains the N-terminal atypical KH domain of FILIA and related domains. FILIA is expressed in oocytes and embryo, and contains an atypical KH domain at the N-terminus with an N-terminal extension that interacts with RNA. RNA-binding may mediate RNA transcript regulation in oogenesis and embryogenesis. FILIA-N differs from typical KH domains by forming a stable dimer in solution and crystal structure
QLREKVPMSMEVLGLVKRPWWFRPEDLKDPLVLYVEAWLLEKIFGPDGALIPGIEWESQTLLQVEAWDSS
GLAEITVFGRPRARRRVKRMLLNLAAWHREHRARGREKLEELEE
>gnl|CDD|240609 cd12796, LbR_Ice_bind, Ice-binding protein, left-handed beta-roll. The ice-binding protein of the grass Lolium perenne (LpIBP) discourages the recrystallization of ice. Ice-binding proteins produced by organisms to prevent the growing of ice are termed to anti-freeze proteins. LpIBP consists of an unusual left-handed beta roll. Ice-binding is mediated by a flat beta-sheet on one side of the helix
NNSLSSFKNRVLSGSENNVIAGGQNLVVSGSNNLVSGGNHNVLSGNNNTVSGNNHVVTGSNNVVTGNGNT
VSGSNNVVSGSNNTVSGGNNTVSGSNNTVSGSNHIVSGNNKVVT
>gnl|CDD|410984 cd12797, M23_peptidase, M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins. This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity
HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTV
GNTGRSTGPHLHFEI
>gnl|CDD|213998 cd12798, Alt_A1, Alternaria alternata allergen Alt a 1. Alt a 1 defines a new homologous protein family with unknown function exclusively found in fungi. The unique structure of Alt a 1 contains intramolecular disulfide bonds that are conserved among the Alt a 1 homologs. Residues reported to be IgE antibody-binding epitopes are exposed through dimerization via a conserved disulfide bond and hydrophobic and polar interactions. Further mechanistic structure/function studies will give insight into immunologic studies directed toward new forms of immunotherapy for Alternaria species-sensitive allergic patients
ACAAPAPQAATSDETIDISDFSGRKPEDGYIDSVSFNINGTNDTLNLTCSAQADGTFDSKIYSCGESFGD
SAYSFELVKGKEADYGLRLYHSVGPDIGLYGTADIPTYCHAGGNGPGDFICTQVADAYITLV
>gnl|CDD|340366 cd12799, pesticin_lyz-like, lysozyme-like C-terminal domain of pesticin and related proteins. Pesticin (Pst) is an anti-bacterial toxin produced by Yersinia pestis that acts through uptake by the target related bacteria and the hydrolysis of peptidoglycan in the periplasm. Pst contains an N-terminal translocation domain, an intermediate receptor binding domain, and a phage-lysozyme like C-terminal activity domain. Bacteriocins such as pesticin are produced by gram-negative bacteria to attack related bacterial stains. Pst is transported to the periplasm via FyuA, an outer-membrane receptor of Y. pestis and E. coli, where it hydrolyzes peptidoglycan via the cleavage of N-acetylmuramic acid and C4 of N-acetylglucosamine. Disruption of the peptidoglycan layer renders the bacteria vulnerable to lysis via osmotic pressure. The pesticin C-terminal domain resembles the lysozyme-like family, which includes soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, and chitosanases. All the members are involved in the hydrolysis of beta-1,4- linked polysaccharides
DHDIFSSNGFSGFSHWPGNPSSGVTIGSGYDLGQRSKQDLLNDGVPQYIADRLDGYYALRGKEAYDKVRT
APLTISDKEAHLLSNIYIDKFSHKAEGLFNDANRTERIGLRFSDLPPRTRTALVSLGYQ
>gnl|CDD|213999 cd12800, Sol_i_2, Sol i 2, a major allergen from fire ant venom. Sol i 2, one of four known potent allergens from the venom of red imported fire ant, is a powerful trigger of anaphylaxis. It causes production of IgE antibody in many individuals stung by fire ants. The closest structure homolog of Sol I 2 is the sequence-unrelated odorant binding protein and pheromone binding protein LUSH of the fruit fly Drosophila, suggesting a possible similar biological function
DIKELKILRKDIAKCARTLPKCVNQPDDPLARVDVWHCAMSKRGVFDNPDPAVIKKKYIKMCEKIITDPA
DVENCKKVISRCVDKETQRPKSNRQKAINILGCILRAGVLETTVLARK
>gnl|CDD|214000 cd12801, HopAB_KID, Kinase-interacting domains of the HopAB family of Type III Effector proteins. HopAB family members are type III effector proteins that are secreted by the plant pathogen Pseudomonas syringae into the host plant to inhibit its immune system and facilitate the spread of the pathogen. AvrPtoB, also called HopAB3, is the best studied member of the family. It suppresses host basal defenses by interfering with PAMP (pathogen-associated molecular signature)-triggered immunity (PTI) through binding and inhibiting BAK1, a kinase which serves to activate defense signaling. It also recognizes the kinase Pto to activate effector-triggered immunity (ETI). AvrPtoB contains an N-terminal region that contains two kinase-interacting domains (KID) and a C-terminal E3 ligase domain. The first KID recognizes the PTI-associated kinase Bti9 as well as Pto, and is referred to as the Pto-binding domain (PID). The second KID interacts with BAK1 and FLS2, which are leucine-rich repeat-containing receptor-like kinases, and is called the BAK1-interacting domain (BID). This family also contains a unique member, HopPmaL, which is shorter and lacks the C-terminal E3 ligase domain
AVPRANRILQQLVQAGADLERLRTALRNYMMGDAPIPSDIRRALRQVGIFPNIPMEGISLVSHPALNLRE
ALRRALS
>gnl|CDD|214001 cd12802, HopAB_PID, Pto-interacting domain of the HopAB family of Type III Effector proteins. HopAB family members are type III effector proteins that are secreted by the plant pathogen Pseudomonas syringae into the host plant to inhibit its immune system and facilitate the spread of the pathogen. AvrPtoB, also called HopAB3, is the best studied member of the family. It suppresses host basal defenses by interfering with PAMP (pathogen-associated molecular signature)-triggered immunity (PTI) through binding and inhibiting BAK1, a kinase which serves to activate defense signaling. It also recognizes the kinase Pto to activate effector-triggered immunity (ETI). AvrPtoB contains an N-terminal region that contains two kinase-interacting domains (KID) and a C-terminal E3 ligase domain. The first KID recognizes the PTI-associated kinase Bti9 as well as Pto, and is referred to as the Pto-binding domain (PID). The second KID interacts with BAK1 and FLS2, which are leucine-rich repeat-containing receptor-like kinases, and is called the BAK1-interacting domain (BID). This family also contains a unique member, HopPmaL, which is shorter and lacks the C-terminal E3 ligase domain
GAVPHANRIVQQLVEAGADLANIRTMLRNAMNGDAVALSRVEQNILRQHFPNMLMCGISRDSELAIALRE
ALRRAVRQQ
>gnl|CDD|214002 cd12803, HopAB_BID, BAK1-interacting domain of the HopAB family of Type III Effector proteins. HopAB family members are type III effector proteins that are secreted by the plant pathogen Pseudomonas syringae into the host plant to inhibit its immune system and facilitate the spread of the pathogen. AvrPtoB, also called HopAB3, is the best studied member of the family. It suppresses host basal defenses by interfering with PAMP (pathogen-associated molecular signature)-triggered immunity (PTI) through binding and inhibiting BAK1, a kinase which serves to activate defense signaling. It also recognizes the kinase Pto to activate effector-triggered immunity (ETI). AvrPtoB contains an N-terminal region that contains two kinase-interacting domains (KID) and a C-terminal E3 ligase domain. The first KID recognizes the PTI-associated kinase Bti9 as well as Pto, and is referred to as the Pto-binding domain (PID). The second KID interacts with BAK1 and FLS2, which are leucine-rich repeat-containing receptor-like kinases, and is called the BAK1-interacting domain (BID). This family also contains a unique member, HopPmaL, which is shorter and lacks the C-terminal E3 ligase domain
MRNRGNNEANAALRGLAQQGVDMERLRAALERYIMQLRPLPLDIRRALESVGINPRIDEEESLVDHPLLN
LNVALNRRLG
>gnl|CDD|214003 cd12804, AKAP10_AKB, PKA-binding (AKB) domain of A Kinase Anchor Protein 10. AKAPs coordinate the specificity of PKA signaling by facilitating the localization of the kinase to subcellular sites through their binding to regulatory (R) subunits of PKA. AKAP-10, also called PRKA10 or Dual-specific AKAP 2 (D-AKAP2), is a multisubunit protein containing two regulator of G protein signaling (RGS)-like domains and a PKA-binding (AKB) domain. The AKB domain of AKAP10 can bind to the dimerization/docking (D/D) domains of both RI and RII regulatory subunits of PKA. This model also includes a C-terminal PDZ-binding motif that binds to PDZK1 and NHERF-1, allowing AKAP10 to link indirectly to membrane proteins. Mutations in AKAP10 can alter its binding to R subunits, which may alter the targeting of PKA; some AKAP10 mutations are associated with abnormalities including hypertension, increased risk of severe arrhythmias during kidney transplantation, and familial breast cancer
AFKKWVQPEPDEAKEEMAWKIAKMIVNDVEDQAQEEMAWQVAEMI
>gnl|CDD|214004 cd12805, Allergen_V_VI, Group V, VI major allergens from grass, including Phlp 5, Phlp 6, Pha a 5 and Lol p 5. This family contains major allergens from various grass pollen, including Phl p 5 and Phl p 6 (timothy grass), Lol p 5 (rye grass) and Pha a 5 (canary grass). They induce allergic rhinitis and bronchial asthma in millions of allergic patients worldwide. These group V and group VI grass-pollen allergens belong to a new class of protease-resistant four-helix-bundle domains, which also have internal helix-turn-helix homology pointing to a special type of four-helix bundle topology, defined as twinned two-helix bundle. IgE binding experiments with recombinant Phl p 6 fragments indicated that the N terminus of the allergen is required for IgE recognition. Immunotherapy treatment for these allergies generally involves administration of grass pollen extracts which induce an initial rise in specific immunoglobulin E (sIgE) production followed by a progressive decline during the treatment
KLIEKINAAFKQAYAAAAAAAPADKYKVFEAAFKKAITAASAAAKVAKKLDAAYKAAYDAAAAATPEAKY
DAFVAALSEALRIAA
>gnl|CDD|214005 cd12806, Esterase_713_like, Novel bacterial esterase that cleaves esters on halogenated cyclic compounds. This family contains proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown. This enzyme is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized
LSGQGSFFVGGRDVTSSGLSLSPKYDAHGTVTVDQMYVRYQIPVRAKRYPLLLIHGCGLTGMTWETTPDG
RMGWDNYFLRKGYSVYVVDQPGRGRSGWDTQFPVQGQAELWQQMVPDWLGAMPTPNPTVAALSKLADKLD
PTVLLTHSQSGIFGFQTAAMRPKGIKAIVAVEPGGCPKPEDVKPLTSIPVLVVYGDHIEEFPRWAVRLKA
CVAFADALNAAGGDVQVVSLPALGIKGNSHMMMMDKNNLQVADLILDWIGR
>gnl|CDD|214006 cd12807, Esterase_713, Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds. This family contains proteins similar to a novel bacterial esterase (esterase 713) with the alpha/beta hydrolase fold that cleaves esters on halogenated cyclic compounds. This Alcaligenes esterase, however, does not contain the GXSXXG pentapeptide around the active site serine residue as seen in other esterase families. This enzyme is active as a dimer though its natural substrate is unknown. It has two distinct disulfide bridges; one formed between adjacent cysteines appears to facilitate the correct formation of the oxyanion cleft in the catalytic site. Esterase 713 also resembles human pancreatic lipase in its location of the acidic residue of the catalytic triad. It is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized
PLTLADQGSFFVGGRPVFSDFPSSSPSGYSAPGTITVNQMYVQYQIPQKGKKKYPIVLVHGCCLTGKTWE
TTPDGRMGWDEYFVRKGHPVYVVDQVGRGRSGFDPTIINAVKLGLAPPSALPAIFRAGDEFAWTNFRFGP
TYGVPFPDTQFPVEAVAEFYKQVVPDLNATLPTPNPTPNALAALADKLGGAVLLGHSQSGPFPLEAALLR
PAGVKGIVSVEPGCCPAPTADQIKTLAKIPILVVFGDHLDAASGPTWQQRLQACQAFVDRINAAGGDAKL
LHLPDLGIRGNSHMMMQDKNNLQIADLILDWIDKN
>gnl|CDD|214007 cd12808, Esterase_713_like-1, Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds. This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown
LREMGSFFVGGRPVTLSGLPVKEVVFAPGGAPRRVDPNGTYVVGQMYVQYFLPARPRGPLPLLLWHGGGM
TGATWETTPDGRPGWLHYFLRAGHDVYVVDAVERGRAGWAMYPEIYKGAPIFRTKEEAWELFRIGPAYGY
ADQPRRAFPGQQFPLAAFDAFAKQFVPRWLGTDALTLAAYDALLDRVGPCIVVAHSQGGGFAFEAARARP
DLVRAVVALEPSGAPDPAEAAPLADVPHLLVWGDYIDADPRWPRYRATVDAYAAALRAAGGRVDVLDLPA
MGIRGNSHMLMMDRNSDQIAGLVQDWLAR
>gnl|CDD|214008 cd12809, Esterase_713_like-2, Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds. This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown
IHTRGYFYVGGRYVKQGGGTVTVGQMYVEKLTPARVTRPYPIVLIHGGGQTGTNWLNTPDGRPGWASYFL
EKGYEVYIVDQPGRGRSPWNPEVGGPLAASTAETVEQRFTAPERYNLWPQAKLHTQWPGTGRRGDPIFDQ
FYASQVPLLTNLAEQEALVRAAGCALLDIIGPAILITHSQGGPFGWLAADARPDLVKAIVAIEPSGPPFN
LAKVPVLVVTAEASYHAPYDHCTVAFLRQAGVKVDHLRLADHGIRGNGHMMFLEKNSDEIAGVVLGWISK
>gnl|CDD|214009 cd12810, Esterase_713_like-3, Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds. This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown
PLVIAEQGSFAAGGTVVTSPGTFDPSLPPSPAGQTLHGDHAYVFYQIPVNARKLPLVFLHGAGQSGKTWE
TTPDGREGFQTIFLRKGYPVYLVDQPRRGRAGRSTVAGTITPTPDDQTWFDQFRIGAWPNGFPGVQFPKD
PEALDQFFRQMTPNTGPFDAEVIADAVAALFDRIGPSILVTHSQGGGPGWLTAMKNDNVKAIVAYEPGGG
PFPPGEEPPPPPPSAFGPLGPVGVPLEDFLKLTKIPIVIYFGDNIPDGPSDIPGLDFWRVRLAMARLFAE
AINKHGGDATVVHLPDIGIKGNTHFPFSDLNNVEIADLLEKWLKEKGL
>gnl|CDD|411995 cd12811, MALA, Mala s 1 allergenic protein and similar proteins. This family includes the yeast Malassezia sympodialis allergen Mala s 1 which is localized in the cell wall and exposed on the cell surface. It can elicit specific IgE and T-cell activity in patients with atopic eczema (AE), a chronic inflammatory disease. Mala s 1 does not show any significant sequence homology to characterized proteins. However, its structure is a beta-propeller which is a novel fold among allergens
PGVFTVNAKNLYPENADFDAKRCLFYQSNLYKGTVAVYDPYDKSHFNVTIPGVSSDGDQHMSGLSVDPRR
DRLFAVAKDGAAFDFGGQDISGPNSLHAYDLPSSKPLWSVNLTAVTGGRPGGFQDSAQDSDGNSYVVGAL
PPAIAKVSPDGKTVTPWFLEAPNGSTRPGYTGIAYIPEDNVLLASGGEPGQLTRFDLSSATPTPIPVKIS
GENFGGLDDGEKLPLLYSNGTVLVGAKAPGVYVFRSSDGWKSAEVLGTVRNEFGSNGLTTVTVQIGDRIY
GVGAYFGDGAPLAGNRTEFPLYDI
>gnl|CDD|214010 cd12812, BPSL1549, Burkholderia Lethal Factor 1. BPSL1549, also suggested to be called Burkholderia lethal factor 1, is a protein of unknown function from Burkholderia pseudomallei, a causative agent of melioidosis (also called Whitmore's disease). This protein shows similarity to Escherichia coli cytotoxic necrotizing factor 1 which has been found to act as a potent cytotoxin against eukaryotic cells and is lethal when administered to mice. BPSL1549 expression levels correlate with suppression or promotion of pathogenic conditions. BPSL1549 inhibits helicase activity of translation initiation factor eIF4A. As yet, there is no vaccine and the organism is multidrug resistant
LEAQIRQAMKTGSTLTIEFDQALNQKSPGTLNVFLHPANGGVRIDLDSGNQGEPAKILWLPWKQGELQTL
QPGSISTVDMLFFTYYLSGCKVFAGDGGPVWHIDAPVEANQFWRRMSSDEWMEDWEVGTDRQVAYLHRAG
QSDSLWNLSAYLEGAAPSTYGRDNLGQAVVGGIVTGRQQMSLYQYATTSSGSSAWSPLTYTLQ
>gnl|CDD|240610 cd12813, LbR-like, Left-handed beta-roll, including virulence factors and various other proteins. This family contains a variety of protein domains with a left-handed beta-roll structure including cell surface adhesion proteins, bacterial virulence factors, and ice-binding proteins, and other activities. UspA1 Head And Neck Domain and YadA of Yersinia are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric beta-rolls of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region. The collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. The ice-binding protein of the grass Lolium perenne (LpIBP) discourages the recrystallization of ice. Ice-binding proteins produced by organisms to prevent the growing of ice are termed to anti-freeze proteins. LpIBP consists of an unusual left-handed beta roll. Ice-binding is mediated by a flat beta-sheet on one side of the helix. These domains form a left handed beta roll made up of a series of short repeated elements
GNTASGGNATVVGGSGNVATGTDSTVIGGDNNSASGSNSTAVGGANTATGSNAVASGTNAIVTDDNAVAS
GNNNLASGSNSTALGGHSTVTGSNSAALG
>gnl|CDD|240611 cd12819, LbR_vir_like, Cell adhesion-like domain, left-handed beta-roll. This group contains proteins of unknown function related to characterized cell surface adhesion proteins with a left-handed beta-roll, like the UspA1 Head And Neck Domain and YadA of Yersinia. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region. The collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements
SNNASGNYATVSGGYRNTATGEYSTVSGGGSNTASGDSSSVAGGSNNTAGGTSSSVSGGNSNTASGDGSS
VAGGTGNTASGENSVVSGGSTNTASGDYSSIAGGRYNTAVG
>gnl|CDD|240612 cd12820, LbR_YadA-like, YadA-like, left-handed beta-roll. This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region
NSTAIGYNNKASGENSTAFGYNNKASGDNSSAFGYGNKASGENSSAFGYNNKASGENSTAFGYGNKASGE
NSSAFGSNNTASGNNSSAFGYNNTASGENSTAFGNNSKASGENSTALGNGNKASGN
>gnl|CDD|213355 cd12821, EcCorA_ZntB-like, Escherichia coli CorA-Salmonella typhimurium ZntB_like family. A family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of this family are found in all three kingdoms of life. It is a functionally diverse family, including the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs (which can also transport Co2+, and Ni2+), and the Zn2+ transporter Salmonella typhimurium ZntB which mediates the efflux of Zn2+ (and Cd2+). It also includes two Saccharomyces cerevisiae members: the inner membrane Mg2+ transporters Mfm1p/Lpe10p, and Mrs2p, and a family of Arabidopsis thaliana members (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport
WYDIDEPDDEIRRLLEELESSHLPNDLRDILLGVSFPRFEEVSGSGIYIQLRKPQKDADTASFHFLITRD
RLITVRLDELPALDELRQDLRSGQMKSAKSAAELLFVLLGAIIKALLTGIDQFEEKLEELEWDLLEGNNA
IKLDRILELRRELLRLTNLIEPQQEVLMALQEAFAELLFSEDEEELRRTLDRIERLLQLIEEYEQELDTL
QDIEEVVSSHRGNEIMKTLTVVTTVFLPLTLIGGLWGMNFKNMPELEWKYGYLFVLGLIILSTAGLYLYL
RRKGW
>gnl|CDD|213356 cd12822, TmCorA-like, Thermotoga maritima CorA-like family. This family belongs to the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of the Thermotoga maritima CorA_like family are found in all three kingdoms of life. It is a functionally diverse family, in addition to the CorA Co2+ transporter from the hyperthermophilic Thermotoga maritima, it includes three Saccharomyces cerevisiae members: two plasma membrane proteins, the Mg2+ transporter Alr1p/Swc3p and the putative Mg2+ transporter, Alr2p, and the vacuole membrane protein Mnr2p, a putative Mg2+ transporter. Thermotoga maritima CorA forms funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport by Alr1p. Natural variants in this signature sequence may be associated with the transport of different divalent cations. The functional diversity of the MIT superfamily may also be due to minor structural differences regulating gating, substrate selection, and transport
WIDLEGPTEEELQLLAEEFGFHPLAIEDALNERQRPKIEEYDDYLFLVLRALRYDEEELELETSELSIFL
GKNFLVTVHEGPLRLIDEVIERLLSDPKLLPKGPDFLLYAILDAIVDSYFPILDELEDRLDELEDEILEE
PRREVLRELFALRRELLRLRRILSPQREVLNRLLRRENELISEELRPYFRDVYDHLERLAELLDSYRDLL
SSLLDAYLSLQSNRTNEVMKVLTIITTIFLPLTFITGIYGMNFEYMPELHWPYGYFIVLGIMLLIAGGLL
WWFRRKKWL
>gnl|CDD|213357 cd12823, Mrs2_Mfm1p-like, Saccharomyces cerevisiae inner mitochondrial membrane Mg2+ transporters Mfm1p and Mrs2p-like family. A eukaryotic subfamily belonging to the Escherichia coli CorA-Salmonella typhimurium ZntB_like family (EcCorA_ZntB-like) family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This functionally diverse subfamily includes the inner mitochondrial membrane Mg2+ transporters Saccharomyces cerevisiae Mfm1p/Lpe10p, Mrs2p, and human MRS2/ MRS2L. It also includes a family of Arabidopsis thaliana proteins (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of two EcCorA_ZntB-like family transporters: Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, as in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport
WTVIDSTGNATVVELDKSELLRELGLQPRDLRLLDPTLTSYPPSILVRENAILVNLEHIRAIITADEVLL
FDPDGSSSALVSAFLEELQRRLASSNGSESESGGEDSLPFEFRALEAALEEVCSHLEAELKRLEPEALPL
LDELTDKISTSNLERLLPLKRRLVELETRVQKVRDALEELLDDDEDMADMYLTDKAAGPERLESSRKEDD
HEEVEMLLEAYLQQVDELLNKLEELREYIDDTEELINLILDSRRNQLMRLELKLSIGTLSLAVGTLVAGL
FGMNLPSGLEESPYAFWIVTGGSVVGSILIFIVVLRYLRRKRL
>gnl|CDD|213358 cd12824, ZntB-like, Salmonella typhimurium Zn2+ transporter ZntB-like subfamily. A bacterial subfamily belonging to the Escherichia coli CorA-Salmonella typhimurium ZntB_like family (EcCorA_ZntB-like) family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This subfamily includes the Zn2+ transporter Salmonella typhimurium ZntB which mediates the efflux of Zn2+ (and Cd2+). Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, which occur in proteins belonging to this subfamily, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport
GNTWYHCDRADPAIRSWLEDNTHLPEATVDHLLAPVRFPHFEPVDDGFLLSLRGIRMDEAASPSDMADLR
ILIGQGAAVTVRSGPSRAVDELRRALRDHSSLKSLADLLAQMISGMTKRLELVIFDLTETLDEVEDNLLD
GGTAPPPYALIALQRRLFRIRRQIRPQQQALRPLITDPAELLVTSDRETLRRASNNVTRYLETLDFCRTR
VALLQDEIKAQRDEKTTRSSLLLTVVATVFLPLTFITGLLGMNVGGIPDVESPMGFWWVTGLSILVALLA
WLLLRRLGHD
>gnl|CDD|213359 cd12825, EcCorA-like, Escherichia coli Mg2+ transporter CorA_like subfamily. A bacterial subfamily of the Escherichia coli CorA-Salmonella typhimurium ZntB_like(EcCorA_ZntB-like) family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This subfamily includes the Mg2+ transporters Escherichia coli, Salmonella typhimurium, and Helicobacter pylori CorAs (which can also transport Co2+, and Ni2+). Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport
WIDLINPTEEELATLSSEYGFILPPREHLEDIEISSRYWEDDSQLFITLSFPNQTKEDTIEEEPVTFIIK
GNILFTIRYRDLPAFDIFPKRAFSQRKFFNSGEELFLFLFEVIVDYLADILENISKKIKQLSREILEEKQ
FSEEDLDALTKLNENNITLRESLIEKQRIITLLLKSPRENSDTKEKLKIELRDLSSLLDHTTFNFDKLDD
LKNNILGKIELEQNKIIKIFTVVTVCFLPPTLIASIYGMNFKNMPELKWSYGYPFALILMILSTILPLLY
FKRKGWL
>gnl|CDD|213360 cd12826, EcCorA_ZntB-like_u1, uncharacterized bacterial subfamily of the Escherichia coli CorA-Salmonella typhimurium ZntB family. A uncharacterized subfamily of the Escherichia coli CorA-Salmonella typhimurium ZntB (EcCorA-ZntB_like) family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. The EcCorA-ZntB_like family includes the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs, which can also transport Co2+, and Ni2+. Structures of the intracellular domain of EcCorA-ZntB_like family members, Vibrio parahaemolyticus and Salmonella typhimurium ZntB, form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA. Natural variants such as GVN and GIN, as in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport
VGILTLEEFRELKELFGLKKELLESLESIRFCKAEVFEDCLGGTFGIPDKLDVLGKRDRFGFYITKNRLV
FIDDDGFVLKLLERIQEKKSWKGPSLERFLYDFLEYLIKDDLEYLEKYEEKLEELEEEILDGKLKNFNER
ILKIRKELLRLNSYYEQLMDIGEELEENENDLFDEEELRLFRLFSDRVERLHDNVQMLREYSLQIRELYQ
SQIDIRQNRIMKILTVVTTIFLPLTLITGWYGMNFTNMPELHWKYGYPVVIILSILIVVIEIIYFKKKKW
L
>gnl|CDD|213361 cd12827, EcCorA_ZntB-like_u2, uncharacterized bacterial subfamily of the Escherichia coli CorA-Salmonella typhimurium ZntB family. A uncharacterized subfamily of the Escherichia coli CorA-Salmonella typhimurium ZntB (EcCorA-ZntB_like) family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes.The EcCorA-ZntB-like family includes the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs, which can also transport Co2+, and Ni2+. Structures of the intracellular domain of EcCorA-ZntB-like family members, Vibrio parahaemolyticus and Salmonella typhimurium ZntB, form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport
WINVVNPTEEEIEQLAEKYGIPEDFLTYALDEEERSRIEYDDDTDYLLIILDVPVEEEEDDDEYETIPLG
IILTKDRLITICNHETDLLDDFLEGRVKNFDTSSKTRFLLQILYRIATSYLKYLRQINKERDELEQELRK
STKNKELFQLLDLEKSLVYFSTSLKSNEIVLEKLKRSRSLKLDEEDKELLEDVIIENKQAIEMAEIYSDI
LSGLMDAFASVISNNLNNVMKFLTSITIVLTIPTIITGFYGMNVPLPFADSPYAFWIILLISLLLSVIVA
LILRRKKYF
>gnl|CDD|213362 cd12828, TmCorA-like_1, Thermotoga maritima CorA_like subfamily. This subfamily belongs to the Thermotoga maritima CorA (TmCorA)-family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of this subfamily are found in all three kingdoms of life. It is functionally diverse subfamily, in addition to the CorA Co2+ transporter from the hyperthermophilic Thermotoga maritima, it includes Methanosarcina mazei CorA which may be involved in transport of copper and/or other divalent metal ions. Thermotoga maritima CorA forms funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport by a related protein, Saccharomyces cerevisiae Alr1p. Natural variants in this signature sequence may be associated with the transport of different divalent cations. The functional diversity of the MIT superfamily may also be due to minor structural differences regulating gating, substrate selection, and transport
GVTWINVDGLHDIELIEKLGERFGLHPLVLEDILNTGQRPKVEEYDDYLFIVLKMLYYDEDTGELESEQV
SLILGKNYVISFQERPGDVFDPVRERLRNGKGRIRKKGADYLAYALLDAIVDNYFPVLEKLGDRIEDLEE
ELLENPTPETLERIHKLKRELLFLRRSIWPLREVINRLLRGESPLISEETRPYLRDVYDHTIQVIDTIET
YRDMLSGLLDLYLSSVSNRMNEVMKVLTIISTIFIPLTFIAGIYGMNFEYMPELEWKYGYPAVLGVMLLI
ALGMLLYFKRKKWL
>gnl|CDD|213363 cd12829, Alr1p-like, Saccharomyces cerevisiae Alr1p-like subfamily. This eukaryotic subfamily belongs to the Thermotoga maritima CorA (TmCorA)-family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This subfamily includes three Saccharomyces cerevisiae members: two plasma membrane proteins, the Mg2+ transporter Alr1p/Swc3p and the putative Mg2+ transporter, Alr2p, and the vacuole membrane protein Mnr2p, a putative Mg2+ transporter. Thermotoga maritima CorA forms funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport by Alr1p. Natural variants in this signature sequence may be associated with the transport of different divalent cations. The functional diversity of the MIT superfamily may also be due to minor structural differences regulating gating, substrate selection, and transport
WLDVQSPTDDDMRAIGKLFPIHPLTLEDILSQDTREKVELFPNYYFISFRAIESDSELDENVLEPVNVYI
VVFREGILTFHFKPLDHIERVRKRIRLLSDSHLLSSDWVLYALLDSIVDSFFPLVDSIEKEVDSIDELVL
LISSSDQSDLLRRIGDLRRRVTSLLRLLFAKSDVLKQLLKRLMKKTFVSPDSEVAIYLGDVQDHILTLLQ
KLNHYEDLLSRSHSNYLAQLSLEMSQESNGTDKAMLRLTVIATIFLPLQLITGLFGMNVKVPGQDIESLY
WFFGIVIVAIMVLVAIVVVFLVRRW
>gnl|CDD|213364 cd12830, MtCorA-like, Mycobacterium tuberculosis CorA-like subfamily. This bacterial subfamily belongs to the Thermotoga maritima CorA (TmCorA)-like family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This subfamily includes the Mg2+ transporter Mycobacterium tuberculosis CorA (which also transports Co2+). Thermotoga maritima CorA forms funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport by a related protein, Saccharomyces cerevisiae Alr1p. Natural variants in this signature sequence may be associated with the transport of different divalent cations. The functional diversity of the MIT superfamily may also be due to minor structural differences regulating gating, substrate selection, and transport
GFVWVGLHEPDAEELAAVAEEFGLHELAVEDAVHAHQRPKLERYGDSLFLVLRTARYVDHTEEVETGETH
VFVGPDFVVTVRHGAAGPLARVRARLEADPELLALGPDAVLYAILDFIVDGYLPVAEELEDDVDELEEEV
FSPDRRDDIERIYRLKREVLEFRRAVDPLVEVLRRLARGHEPLIPKELRPYFRDVADHLLRVADRVDSLR
ELLSSALQANLALVSVQQNEDMRKISAWAAILAVPTAIAGIYGMNFDHMPELHWTYGYPLVLGLMVAVCL
GLYRRFRRNGWL
>gnl|CDD|213365 cd12831, TmCorA-like_u2, Uncharacterized bacterial subfamily of the Thermotoga maritima CorA-like family. This subfamily belongs to the Thermotoga maritima CorA (TmCorA)-like family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of the TmCorA-like family are found in all three kingdoms of life. It is a functionally diverse family which includes the CorA Co2+ transporter from the hyperthermophilic Thermotoga maritima, and three Saccharomyces cerevisiae proteins: two located in the plasma membrane: the Mg2+ transporter Alr1p/Swc3p and the putative Mg2+ transporter, Alr2p, and the vacuole membrane protein Mnr2p, a putative Mg2+ transporter. Thermotoga maritima CorA forms funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport by a related protein, Saccharomyces cerevisiae Alr1p. Natural variants in this signature sequence may be associated with the transport of different divalent cations. The functional diversity of the MIT superfamily may also be due to minor structural differences regulating gating, substrate selection, and transport
KWYWVDFNNPTEEEIKLLTSFFHFHPLAIEDCLHLLQRPKLDYYDDYQFLVLHAIDQEDLEAEEVNLFVG
ENYIVTFHKEPIREINEVWEKLKEKKDKKLGTLYIAYMIIDKIVDDYFPIVYEIEDRLNEIEDNNVDSSN
KKLMDEVFDIRSDLLKLRRTILPMRDLLYRILNSERLEGDKEQRAYFQDIYDHLLKLSEMLESNREMTAD
IRDNYESYNSNRMNSIMMTLTIISTIFMPLTFIAGIYGMNFEYMPELKWHYGYFVVLGIMLLIAIGMILW
FKKKGWF
>gnl|CDD|213366 cd12832, TmCorA-like_u3, Uncharacterized subfamily of the Thermotoga maritima CorA-like family. This subfamily belongs to the Thermotoga maritima CorA (TmCorA)-like family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of the TmCorA-like family are found in all three kingdoms of life. It is a functionally diverse family which includes the CorA Co2+ transporter from the hyperthermophilic Thermotoga maritima, and three Saccharomyces cerevisiae proteins: two located in the plasma membrane: the Mg2+ transporter Alr1p/Swc3p and the putative Mg2+ transporter, Alr2p, and the vacuole membrane protein Mnr2p, a putative Mg2+ transporter. Thermotoga maritima CorA forms funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport by a related protein, Saccharomyces cerevisiae Alr1p. Natural variants in this signature sequence may be associated with the transport of different divalent cations. The functional diversity of the MIT superfamily may also be due to minor structural differences regulating gating, substrate selection, and transport
WIDVVAPTEEDLEDLARRYNLHETSLKDCLDPDHLPKYEEVDGVTFIILRVYTDKKRENADTIQELTTKI
AIFVVDKFVITIHRTDLEFIANLKEKWLSGMHKCESPTELLLRIVKDALKTYEAPLEKLSEELDKYEEEV
FLKKRKGSLLKRLYHLKRKASVIKRVLNLTQDVIDKIDTPLKSDPYTQDLRDLLIKLLSLYDELHENATN
LLSLYISLSSQRTNEVMRVLTIFSVFFLPLTFIAGVYGMNFKYMPELHWKYGYPATLLVMIVIVVGIYFW
FKRKGWL
>gnl|CDD|213367 cd12833, ZntB-like_1, Salmonella typhimurium Zn2+ transporter ZntB-like subgroup. A bacterial subgroup belonging to the Escherichia coli CorA-Salmonella typhimurium ZntB_like family (EcCorA_ZntB-like) of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This subgroup includes the Zn2+ transporter Salmonella typhimurium ZntB which mediates the efflux of Zn2+ (and Cd2+). Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, which occur in proteins belonging to this subfamily, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport
GFLWLHLDYSDPEAQDWLEQSSGLPELVIDALLAEETRPRATRLGDGLLLNLRGVNLNPGADPEDMVSIR
LWITPGRIISTRRRRLLAVDDIREALEAGKGPKSPGDFLAALAERLTDRMEDVIDELEDRLDELEERVLE
EEDEELRGELAELRRQAIALRRYLAPQRDALERLAREDLPWLSDDDRLRLREAADRLTRYIEDLDAIRER
AAVLQEELTNRRAEQMNRRMYVLSIVAAIFLPLGFLTGLLGINVGGIPGAENPWAFWIFCGLLVVLAVGL
LLLFRRKKWL
>gnl|CDD|213368 cd12834, ZntB_u1, Uncharacterized bacterial subgroup of the Salmonella typhimurium Zn2+ transporter ZntB-like subfamily. The MIT superfamily of essential membrane proteins is involved in transporting divalent cations (uptake or efflux) across membranes. The ZntB-like subfamily includes the Zn2+ transporter Salmonella typhimurium ZntB which mediates the efflux of Zn2+ (and Cd2+). Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN which occur in proteins belonging to this subfamily, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport
GFLWLHFNLADARARQWIAAHPALPEAARALLLSGDTSTRLEVDDDALYGVLNDLERDFAEASTDVGTLR
FAVTPRLLITARRQPLRSVDRLRQAVERGLRFRSPADLLEHLLREQADTLSRIVRELTDELDRIEDRLLS
GRLRRERRELGALRRRLVRLHRLLAPEPAALFRLLRRPPDWLPDADLETLRRLTERLDALDRDLVALQER
ARLLQEEIAARLAEQTNRSLYILSVVTALLLPPTLVTGLFGMNTGGLPLAEGPHGFWIAVALALLAAGLA
YLLLRRLGLL
>gnl|CDD|213369 cd12835, EcCorA-like_1, Escherichia coli Mg2+ transporter CorA_like subgroup. A bacterial subgroup of the Escherichia coli CorA-Salmonella typhimurium ZntB_like (EcCorA_ZntB-like) family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This subgroup includes the Mg2+ transporters Escherichia coli CorA and Salmonella typhimurium CorA (which can also transport Co2+, and Ni2+). Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport
WIDLIAPDDEEREWLEQLLGQELPDLEDLEEIEASARFYVDEDGLHIHSLFLQDSEGRARNVTVAFTLRD
DRLITLREEELPVFRLLRLRARRGPGEVSDPKDLLLDLFEQKVEYLADIIEDIYRDLERVSREVLEENDE
DLEEALGRLARQEDLNGKIRLCLMDTQRALSFLLRTRRLSDEQLEDAREILRDIESLLPHTQFLFDKINF
LMDAAMGFINIEQNKIIKIFSVAAVVFLPPTLIASIYGMNFDFMPELDWKFGYPMAIGLMILSAIAPYLY
FKRKGWL
>gnl|CDD|213370 cd12836, HpCorA-like, Mg2+ transporter Helicobacter pylori CorA-like subgroup. A bacterial subgroup of the Escherichia coli CorA-Salmonella typhimurium ZntB_like (EcCorA_ZntB-like) family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This subgroup includes the Mg2+ transporter Helicobacter pylori CorAs (which can also transport Co2+, and Ni2+); CorA plays an important role in the viability of this pathogen. Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB (members of the EcCorA_ZntB-like family) form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport
VLWIDLINPTEEEIKTVEQYFNIEFPTKQESEEIESSSRYWEDEDSITINSNFLVPDDDGYHNEPVSFIL
KDNILFTIRYGELRTFSETSKKLRANPKKFQTGYDIFSSILEIRIDYDADLLENISKEISKLRKKLFADE
DLDEELLEKISRLQELNMTIRENLIDKQRVLSSLLKSEKFPEDLKENLRIMIKDINSLIEHTTFNFERLD
YLQNTFLGLINIEQNKIIKIFTVATVIFMPPTLIASIYGMNFKFMPELDWKYGYPFALLLMVISSILPLL
YFKKKKWL
>gnl|CDD|213371 cd12837, EcCorA-like_u1, uncharacterized subgroup of the Escherichia coli Mg2+ transporter CorA_like subfamily. A uncharacterized subgroup of the Escherichia coli CorA-Salmonella typhimurium ZntB_like family (EcCorA_ZntB-like) family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. The EcCorA_ZntB-like family includes the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs, which can also transport Co2+, and Ni2+. Structures of the intracellular domain of EcCorA_ZntB-like family members, Vibrio parahaemolyticus and Salmonella typhimurium ZntB, form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport
VWIDLLNPTPEEEAAVEALLGIAIPTREEMSEIEASSRLYREGGALYMTAPLLSRADTDDPELSPVTFVL
TPERLVTVRYADPRAFDTFAARAARQPSGCASGEDVLLGLLEAIVDRLADVLERVGADLDRLSRRIFRSS
AKRRRRASRDLRSVLRRIGRAGDLLSKIRESLLSLGRLLSFLSANAADWLSKELRARLKTLQRDVASLSE
HATFLSNKIQFLLDATLGLINIEQNNIIKIFSVASVVFLPPTLIASIYGMNFKHMPELDWPFGYPLALGL
MVLSAVLPLLWFKRRGWL
>gnl|CDD|214011 cd12838, Killer_toxin_alpha, Alpha subunit of killer toxin from halotolerant yeast. This family contains the alpha subunit of killer toxins that are secreted by several strains of yeasts and fungi. These toxins are proteinous substances that kill sensitive strains. The halotolerant yeast Pichia farinosa KK1 strain produces the SMK toxin, with maximum killer activity under acidic pH and high salt concentration. This toxin is composed of alpha and beta subunits that interact tightly with each other under acidic conditions but easily dissociated and lose activity under neutral conditions. It shares topology to that of the fungal killer toxin, KP4, which contains a rare structural motif, suggesting that these toxins may be evolutionally and/or functionally related
SLRWRMQKSTTIAAIAGCSGAATFGGLAGGIVGCIAAGILAILQGFEVNWHNGGGGDRSNPV
>gnl|CDD|214012 cd12839, Killer_toxin_beta, Beta subunit of killer toxin from halotolerant yeast. This family contains the beta subunit of killer toxins that are secreted by several strains of yeasts and fungi. These toxins are proteinous substances that kill sensitive strains. The halotolerant yeast Pichia farinosa KK1 strain produces the SMK toxin, with maximum killer activity under acidic pH and high salt concentration. This toxin is composed of alpha and beta subunits that interact tightly with each other under acidic conditions but easily dissociated and loose activity under neutral conditions. It shares topology to that of the fungal killer toxin, KP4, which contains a rare structural motif, suggesting that these toxins may be evolutionally and/or functionally related
TTIWGVGADEAIDKGTPSKNDLQNMSADLAKNGFKGHQGVACSTVKDGNKDVYMIKFSLAGGSNDPGGSP
CSDD
>gnl|CDD|214013 cd12840, CarS, Antirepressor CarS. CarS, an antirepressor present in Cystobacterineae, recognizes repressors to turn on the photo-inducible promoter P(B). In the dark, access to the P(B) promoter is blocked by the repressor CarA. Blue light causes expression of CarS, leading the way to the CarA-CarS interaction which dismantles the CarA-operator complex, resulting in the derepression of the P(B) promoter. A parallel pathway for regulating P(B) involves the interaction of CarS with the repressor CarH, which shares the domain architecture of CarA. CarH and CarA contain an N-terminal, MerR-type winged-helix DNA-binding domain that recognizes CarS. CarS adopts an SH3-like fold with loop length variations and acts as an operator DNA mimic
SLIICHDVDGAPVRIGAKVKVVPHSEDGTISQRFLGRTGVVVGLVFDDPATQYPDDPLIQVLVEGLGEDL
FFPEELELAP
>gnl|CDD|214014 cd12841, TM_EphA1, Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase. Ephrin receptors (EphRs) comprise the largest subfamily of receptor PTKs, and are classified into two classes (EphA and EphB), corresponding to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphA1 has been associated with late-onset Alzheimer's disease and certain cancers such as colorectal and gastric carcinomas. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a single-span transmembrane (TM) domain, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The TM domain mediates dimerization
SPPVSRGLTGGEIVAIIFGLLLGVALLLGILVFRSRRA
>gnl|CDD|410985 cd12842, IGCP_Hfx_cass2, integron gene cassette protein (IGCP) Hfx_cass2 and similar proteins. This family contains the unique integron gene cassette protein Hfx_cass2 and similar proteins that have yet to be characterized. The structure of Hfx_cass2 depicts a homodimer incorporating a compact all-alpha fold of six helical segments with a core central bundle of helices. It has a surface cleft reminiscent of an enzyme active site. This family may allow an assessment of the impact of the integron/gene cassette system on the emergence of new phenotypes, such as drug resistance or virulence
AEYLRDGCQWLSRELTRLEQLNRPLSIDEFYSWSEQERFIATLFEKYGSYIIGLHYLDPSSDLCEKELLS
YIENAFGRHSNVITSETYGVVDNAYLLAINVLFAISREAD
>gnl|CDD|240608 cd12843, Bvu_2165_C_like, The C-terminal domain of uncharacterized bacterial proteins. This family contains the C-terminal domain of uncharacterized hypothetical proteins from bacteria, including Bacteroides vulgatus Bvu_2165. The structure of Bvu_2165 is dimeric, with an extensive binding interface
ITSVTDLATGSKNGSLTAGGPVRIKGSNLKIDGDDPSVGIFLVNSDGTETKVTPDSIVRNKPSRLIFLLP
ADLADGEYTLEVRTQYSGGSTLLKTPRTGTFPITL
>gnl|CDD|240607 cd12869, MqsR, Motility quorum-sensing regulator (MqsR). This family includes domains similar to the motility quorum-sensing regulator MqsR, a toxin that is highly upregulated in persisters (dormant cells found in biofilms that are a source of antibiotic resistance). MqsR pairs with its antitoxin MqsA, forming a unique family of toxin:antitoxin (TA) systems. MqsR has been found to be structurally homologous to the bacterial ribonuclease (RelE) toxins; however, its sequence is not similar to any other known toxins and therefore its molecular function is as yet unknown
EKRTPHYDLSKIKALIRTGKTVRITRTALRGAAALGLDEDDIVAVVLSLSRSDFYKSMTTYADHRIWQDV
YHAPYPGGELYIKFTVDENDVVVISFKE
>gnl|CDD|240606 cd12870, MqsA, antitoxin MqsA for MqsR toxin. This family includes domains similar to the antitoxin MqsA that binds motility quorum-sensing regulator MqsR, a toxin that is highly upregulated in persisters (dormant cells found in biofilms that are a source of antibiotic resistance), thus forming a unique toxin:antitoxin (TA) pair. MqsA neutralizes MsqR toxicity. It binds its own promoter as well as those of genes important for E. coli physiology, such as mcbR and spy. It also binds zinc and has been shown to coordinate DNA via its C-terminal domain. This family also includes the B. subtilis YokU protein, which is functionally uncharacterized
KCPICGGGELVGGTTTWTLPRGGRLIVIKNVPALVCENCGEEYLDEETSEEIEDILLAVKKKVLAE
>gnl|CDD|214015 cd12871, Bacuni_01323_like, Uncharacterized protein conserved in Bacteroidetes. A well-conserved family of 16-stranded beta barrels resembling outer membrane porins. The interior of the barrels is mostly occupied by an insert with partially helical structure
VVNETKKFTGGLPKSTSEYTFEYDADGRLTSITTTQEGEAEEITYTTTITYEPNVITVTDDGGKTVSTYT
LNEKGYVTSCTETEYGKGQLRTYTFTYNADGQLTKIVESIGTEYSTITITWNNGDIVSISTKSNTEENES
KITYTSDKVYNPIVNKGCLMLFGLTLGYDLSDLFYAYYAGLLGKATKHLPESIIPKGNEETTTYTYTFDK
NGYPTSIIVTYSGDDKTNTLE
>gnl|CDD|293932 cd12872, SPRY_Ash2, SPRY domain in Ash2. This SPRY domain is found at the C-terminus of Ash2 (absent, small, or homeotic discs 2) -like proteins, core components of all mixed-lineage leukemia (MLL) family histone methyltransferases. Ash2 is a member of the trithorax group of transcriptional regulators of the Hox genes. Recent studies show that the SPRY domain of Ash2 mediates the interaction with RbBP5 and has an important role in regulating the methyltransferase activity of MLL complexes. In yeast, Ash2 is involved in histone methylation and is required for the earliest stages of embryogenesis
LKLSEDRLTVTGEKGYRMARANHGVREGKWYFEVKILEGGGTETGHVRVGWSRREASLQAPVGYDKYSYA
IRDKDGSKFHQSRGKPYGEPGFKEGDVIGFLITLPKIEFFKNGKSQGVAFEDIYGTGGYYPAVSLYKGAT
VTINFGPDFK
>gnl|CDD|293933 cd12873, SPRY_DDX1, SPRY domain associated with DEAD box gene DDX1. This SPRY domain is associated with the DEAD box gene, DDX1, an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. It is suggested that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element (RRE). DDX1 RNA is overexpressed in breast cancer, data showing a strong and independent association between poor prognosis and deregulation of the DEAD box protein DDX1, thus potentially serving as an effective prognostic biomarker for early recurrence in primary breast cancer. DDX1 also interacts with RelA and enhances nuclear factor kappaB-mediated transcription. DEAD-box proteins are associated with all levels of RNA metabolism and function, and have been implicated in translation initiation, transcription, RNA splicing, ribosome assembly, RNA transport, and RNA decay
MNPYDRDAALAISPDGLLCQSREEKGWQGCRATKGVKGKGKYYYEVTVTDEGLCRVGWSTEDASLDLGTD
KFGFGYGGTGKKSHGRQFDDYGEPFGLGDVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRNSALFPAV
CLKNAEVEFNFGDKP
>gnl|CDD|293934 cd12874, SPRY_PRY, PRY/SPRY domain, also known as B30.2. This domain contains residues in the N-terminus that form a distinct PRY domain structure such that the B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Among the TRIM proteins, also known as the N-terminal RING finger/B-box/coiled coil (RBCC) family, only Classes I and II contain the B30.2 domain that has evolved under positive selection. Class I TRIM proteins include multiple members involved in antiviral immunity at various levels of interferon signaling cascade. Among the 75 human TRIMs, roughly half enhance immune response, which they do at multiple levels in signaling pathways. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site
LTFDPDTAHLNLILSDDLRSVRVGDISQHPPEPPPRFFECWQVLGSQSFSSGRHYWEVDVQDDSSWYVGV
TYKSLPRKGKMSNLGRNNGSWCLEWRENEFSAWHNNPETRLPVTPPRRLGVFLDCDGGSLSFYGVTDGVQ
LLYTFKAKFTEPLYPAFWLGEGSTLSIC
>gnl|CDD|293935 cd12875, SPRY_SOCS_Fbox, SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins. This family consists of the SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) as well as F-box protein 45 (Fbxo45), a novel synaptic E3 and ubiquitin ligase. The SPSB protein is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. SPSB1, SPSB2, and SPSB4 interact with prostate apoptosis response protein 4 (Par-4) and are negative regulators that recruit the ECS E3 ubiquitin ligase complex to polyubiquitinate inducible nitric-oxide synthase (iNOS), resulting in its proteasomal degradation. Fbxo45 is related to this family; it is located N-terminal to the SPRY domain, and known to induce the degradation of a synaptic vesicle-priming factor, Munc13-1, via the SPRY domain, thus playing an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse. Suppressor of cytokine signaling (SOCS) proteins negatively regulate signaling from JAK-associated cytokine receptor complexes, and play key roles in the regulation of immune homeostasis
HGWNPADCSKNIYIKEDGLTFHRRPVAQSTDAIRGKKGYTRGLHAWEVKWISRPRGSHAVVGVATKDAPL
QCDGYVTLLGSNSESWGWDLGDNKLYHNGKKVIGSYPAKSENYQVPDRILVILDMEDGTLAFEANGEYLG
VAFRGLPGKLLYPAVSAVYGNCEIRLIYL
>gnl|CDD|293936 cd12876, SPRY_SOCS3, SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family. The SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. All four SPSB proteins interact with c-Met, the hepatocyte growth factor receptor, but SOCS3 regulates cellular response to a variety of cytokines such as leukemia inhibitory factor (LIF) and interleukin 6. SOCS3, along with SOCS1, are expressed by immune cells and cells of the central nervous system (CNS) and have the potential to impact immune processes within the CNS. In non-small cell lung cancer (NSCLC), SOCS3 is silenced and proline-rich tyrosine kinase 2 (Pyk2) is over-expressed; it has been suggested that SOCS3 could be an effective way to prevent the progression of NSCLC due to its role in regulating Pyk2 expression
EWTWDERDKSPAVQLSDNNREVYFHPDYSCGTAAVRGTKPLTNGQHYWEIKMSSPVYGTDMMVGVGTKKA
DLHAYRYEFCSLLGEDEESWGLSYKGLLWHDGQSRPYTSPFGNQGTIIGVHLDMWRGTLTFYKNGKPLGV
AFTGLNGVKPLYPMVSSTAAKSEMKLINSRSFPVSLQDRCCAALR
>gnl|CDD|240457 cd12877, SPRY1_RyR, SPRY domain 1 (SPRY1) of ryanodine receptor (RyR). This SPRY domain is the first of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this first SPRY domain of the RyRs
SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQFTHQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYS
YGFDGLHLWTGGRSRRVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSF
SAGVSCRFLLG
>gnl|CDD|240458 cd12878, SPRY2_RyR, SPRY domain 2 (SPRY2) of ryanodine receptor (RyR). This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1
RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQ
WQPGDVVGCMLDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG
>gnl|CDD|293937 cd12879, SPRY3_RyR, SPRY domain 3 (SPRY3) of ryanodine receptor (RyR). This SPRY domain (SPRY3) is the third of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this third SPRY domain of the RyRs
DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIK
RQNCYMVCAGELLAEVGQDSSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRP
TSKEVLQFELG
>gnl|CDD|293938 cd12880, SPRYD7, SPRY domain-containing protein 7. This family contains SPRY domain-containing protein 7 (also known as SPRY domain-containing protein 7 or CLL deletion region gene 6 protein homolog or CLLD6 or chronic lymphocytic leukemia deletion region gene 6 protein homolog). In humans, CLLD6 is highly expressed in heart, skeletal muscle, and testis as well as cancer cell lines. It also has cross-species conservation, suggesting that it is likely to carry out important cellular processes
MGPDVVIVKNGRRICGTGAALANAPIVQDKAYFEVKIQSTGVWGVGLATRKTDLNRVPLGNDAESWVLRS
DGTIWHNGEVIHKLKQLVEEGDVIGVTYDHVELNFYLNGKPLDCPITGIKGTVYPVVYVDDGAILDVQFS
NFYHPPPSGFEEIMFEQSLL
>gnl|CDD|293939 cd12881, SPRY_HERC1, SPRY domain in HERC1. This SPRY domain is found in the HERC1, a large protein related to chromosome condensation regulator RCC1. It is widely expressed in many tissues, playing an important role in intracellular membrane trafficking in the cytoplasm as well as Golgi apparatus. HERC1 also interacts with tuberous sclerosis 2 (TSC2, tuberin), which suppresses cell growth, and results in the destabilization of TSC2. However, the biological function of HERC1 has yet to be defined
EASFDPEKSTNCVVVENGGTLVHSSGGRGYGLAATWIGISSGCYQWKFYLVKENRGNEGTCVGVSRKPVT
DFNYRTSSDMWLYRAYNGNLYHNGEQLLRLSSKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDAT
ELYPCVMFYSSGPGEKVKITDM
>gnl|CDD|293940 cd12882, SPRY_RNF123, SPRY domain at N-terminus of ring finger protein 123. This SPRY domain is found at the N-terminus of RING finger protein 123 domain (also known as E3 ubiquitin-protein ligase RNF123). The ring finger domain motif is present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RNF123 displays E3 ubiquitin ligase activity toward the cyclin-dependent kinase inhibitor p27 (Kip1)
SIRANACVYKGKWMYEVTLGTKGIMQIGWATISCRFTQEEGVGDTRDSYAYDGNRVRKWNVSTQKYGEPW
VAGDVIGCCIDLDKGTISFYRNGRSLGVAFDNVRRGPGLAYFPAVSLSFGERLELNFG
>gnl|CDD|293941 cd12883, SPRY_RING, SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain. This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development
GVWYYEVTVLTSGVMQIGWATKDSKFLNHEGYGIGDDEYSCAYDGCRQLIWYNAKSKPHTHPRWKPGDVL
GCLLDLNKKQMIFSLNGNRLPPERQVFTSAKSGFFAAASFMSFQQCEFNFG
>gnl|CDD|293942 cd12884, SPRY_hnRNP, SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1 (also known as HNRPUL1) which is a major constituent of nuclear matrix or scaffold and binds directly to DNA sequences through the N-terminal acidic region named serum amyloid P (SAP). Its function is specifically modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signaling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. When associated with bromodomain-containing protein 7 (BRD7), it activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation
VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPH
VVRVGWSVDSSSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESEPVEISFSKNGKD
LGVAFKISKEELGGKALFPHVLTKNCAVEVNFGQKEE
>gnl|CDD|293943 cd12885, SPRY_RanBP_like, SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3. This family includes SPRY domains found in Ran binding proteins (RBP or RanBPM) 9 and 10, SSH4 (suppressor of SHR3 null mutation protein 4), SPRY domain-containing protein 3 (SPRYD3) as well as HECT, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). RanBP9 and RanBP10 act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. SPRYD3 is highly expressed in most tissues in humans, possibly involved in important cellular processes. HECT E3 mediates the direct transfer of ubiquitin from E2 to substrate
GSVRADHPIPPKVPVFYFEVTILDLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGEGE
NYGPPFGTGDVVGCGINFKTGEVFFTKNGELLGTAFENVVKGRLYPTVGLGSPGVKVRVNFG
>gnl|CDD|293944 cd12886, SPRY_like, SPRY domain-like in bacteria. This family contains SPRY-like domains that are found only in bacterial and are mostly uncharacterized. SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 eukaryotic protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L)
GKWYWEVTVVSSAASTYAGIGVANAAATGNNGLNGIELSSIGYSLGVYSGNKLSNGSSVATYGAGFTAGD
VIGVALDLDAGKIWFYKNGVWQGGGDPAPGTNPAFAGTAMYPAVTGGSSTGGSFTANFG
>gnl|CDD|293945 cd12887, SPRY_NHR_like, SPRY domain in neuralized homology repeat. This family contains the neuralized homology repeat 1 (NHR1) domain similar to the SPRY domain (known to mediate specific protein-protein interactions) at the C-terminus of a conserved region within eukaryotic neuralized and neuralized-like proteins. In Drosophila, the neuralized protein (Neur) belongs to a group of ubiquitin ligases and is required in a subset of Notch pathway-mediated cell fate decisions during development of the nervous system. Neur binds to the Notch receptor ligand Delta through its first NHR1 domain and mediates its ubiquitination for endocytosis. Multiple copies of this region are found in some members of the family
RFHENHGKNIRLSNDGRTATRVKASFNNGVVFSSRPLRPGELFEVRIDKLVDRWSGSLEIGVTTLNPETL
DLPPSATDLKSGTWILSGSSVFKNGNKIRENYGPDLDRLRVGDRVGVMRTSDGTLHFYVNGEDQGVAASN
VPQPVYAVVDLYGQCEQVSIV
>gnl|CDD|293946 cd12888, SPRY_PRY_TRIM7_like, PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, TRIM15, TRIM26, TRIM39, TRIM41. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several tripartite motif-containing (TRIM) proteins, including TRIM7 (also referred to as glycogenin-interacting protein, RING finger protein 90 or RNF90), TRIM10, TRIM15, TRIM26, TRIM39 and TRIM41. TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM10 (also known as hematopoietic RING finger 1 (HERF1) or TRIM10/HERF1) plays a key role in definitive erythroid development; downregulation of the Spi-1/PU.1 oncogene induces the expression of TRIM10/HERF1, a key factor required for terminal erythroid cell differentiation and survival. Antiviral activity of TRIM15 is dependent on the ability of its B-box to interact with the MLV Gag precursor protein; downregulation of TRIM15, along with TRIM11, enhances virus release suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. Tripartite motif-containing 26 (TRIM26) function is as yet unknown; however, since it is localized in the human histocompatibility complex (MHC) class I region, TRIM26 may play a role in immune response although studies show no association between TRIM26 polymorphisms and the risk of aspirin-exacerbated respiratory disease. TRIM39 is a MOAP-1 (Modulator of Apoptosis)-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process. TRIM41 (also known as RING finger-interacting protein with C kinase or RINCK) functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C
NVTLDPDTAHPRLVLSEDRKSVRWGDTRQDLPDNPERFDTWPCVLGCEGFTSGRHYWEVEVGDGGGWAVG
VARESVRRKGEISFSPEEGIWAVGQWGGQYWALTSPETPLPLSEVPRRIRVYLDYEGGQVAFFDADNEAP
IFTFPPASFAGERIFPWFWVGKGSQLKLC
>gnl|CDD|293947 cd12889, SPRY_PRY_TRIM67_9, PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM9 proteins. TRIM9 protein is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. It has been shown that TRIM9 is localized to the neurons in the normal human brain and its immunoreactivity in affected brain areas in Parkinson's disease and dementia with Lewy bodies is severely decreased, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis
CLQTAEVAWFTFDPSTSHPDIILSNDNMTVTCNSYEDRVVLGSVGFSRGVHYWEVTIDRYDGHPDPAFGV
ARIDVNKDKMLGKDDKGWSMYIDNNRSWFLHNNEHSNRTEGGITVGSVVGVLLDLDRHTLSFYVNDEPQG
PIAFRNLPGVFYPAVSLNRNVQVTLHTGLEPP
>gnl|CDD|293948 cd12890, SPRY_PRY_TRIM16, PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM16 and TRIM-like proteins. TRIM16 (also known as estrogen-responsive B box protein or EBBP) does not possess a RING domain like the other TRIM proteins, but contains two B-box domains and can heterodimerize with other TRIM proteins such as TRIM24, Promyelocytic leukemia (PML) protein and Midline-1 (MID1 or TRIM18). It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. It has been shown that loss of TRIM16 expression plays an important role in the development of cutaneous squamous cell carcinoma (SCC) and is a determinant of retinoid sensitivity. TRIM16 also has E3 ubiquitin ligase activity
RDDFLKYAYPLTFDPDTAHRYLRLTEDNRKVTNTTPWEHPYPDHPERFEHWRQVLSQQSLYLGRYYFEVE
ISGEGTYVGLTYKSIDRKGSESNSCISGNNFSWCLQWNGKEFSAWHSDVETPLKKGPFTRLGIYLDYPGG
TLSFYGVEDDGMTLLHKFQCKFTEPLYPAFWLSKKENAVRIV
>gnl|CDD|293949 cd12891, SPRY_PRY_C-I_2, PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, TRIM16-like, TRIM25-like, TRIM47-like, TRIM65 and RNF135, and stonustoxin. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM14, TRIM16 and TRIM25, TRIM47 as well as RING finger protein RNF135 and stonustoxin, a secreted poisonous protein of the stonefish Synanceja horrida. TRIM16 (also known as estrogen-responsive B box protein or EBBP) has E3 ubiquitin ligase activity. It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function. TRIM47, also known as GOA (Gene overexpressed in astrocytoma protein) or RNF100 (RING finger protein 100), is highly expressed in kidney tubular cells, but low expressed in most tissue. It is overexpressed in astrocytoma tumor cells and plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. RNF135 ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Stonustoxin (STNX) is a hypotensive and lethal protein factor that also possesses other biological activities such as species-specific hemolysis (due to its ability to form pores in the cell membrane) and platelet aggregation, edema-induction, and endothelium-dependent vasorelaxation (mediated by the nitric oxide pathway and activation of potassium channels). The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site
LTLDPNTAHNNLALSGDLKTVTCSSENQHYPDSPERFTHSQVLSTQSFSSGRHYWEVEVSESGGWSVGVA
YPSIERKGDESRIGRNDKSWCLEWQDKSFSAWHNNEETPLPSVSSRRLGVYLDYEAGRLSFYELSDPIRH
LHTFTATFTEPLHPAFWVLEGGWIRIK
>gnl|CDD|240472 cd12892, SPRY_PRY_TRIM18, PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is at the C-terminus of the overall domain architecture of MID1 (also known as FXY, RNF59, TRIM18) gene represented by a RING finger domain (RING), two B-box motifs (BBOX), coiled-coil C-terminal to Bbox domain (BBC) and fibronectin type 3 domain (FN3). Mutations in the human MID1 gene result in X-linked Opitz G/BBB syndrome (OS), a disorder affecting development of midline structures, causing craniofacial, urogenital, gastrointestinal and cardiovascular abnormalities. A unique MID1 gene mutation located in a variable loop in the SPRY domain alters conformation of the binding pocket and may affect the binding affinity to the PRY/SPRY domain
PFKLDPKSAHRKLKVSHDNLTVERDETSSKKSHTPERFTSQGSYGVAGNVFIDSGRHYWEVVISGSTWYA
IGIAYKSAPKHEWIGKNSASWVLCRCNNNWVVRHNSKEIPIEPSPHLRRVGILLDYDNGSLSFYDALNSI
HLYTFDIAFAQPVCPTFTVWNKCLTILTGLPIPDHLD
>gnl|CDD|293950 cd12893, SPRY_PRY_TRIM35, PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35). This PRY/SPRY domain is found at the C-terminus of the overall domain architecture of tripartite motif 35, TRIM35 (also known as hemopoietic lineage switch protein), which includes a RING finger domain (RING) and a B-box motif (BBOX). TRIM35 may play a role as a tumor suppressor and is implicated in the cell death mechanism
PVTLDPNTAHPWLSLSEDLTSVRYSSEKQQLPDNPERFDPYPCVLGSEGFTSGKHSWDVEVGDNTSWMLG
VAKESVQRKGKFTLSPESGFWTIGFSEGKYSARTSPEPRTPLRVKQKPQRIRVQLDWDRGKVSFSDPDTN
THIHTFTHTFTERVFPYFYTGCKSEPLRILP
>gnl|CDD|293951 cd12894, SPRY_PRY_TRIM36, PRY/SPRY domain in tripartite motif-containing protein 36 (TRIM36). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM36, a Class I TRIM protein. TRIM36 (also known as Haprin or RNF98) has a ubiquitin ligase activity and interacts with centromere protein-H, one of the kinetochore proteins. It has been shown that TRIM36 is potentially associated with chromosome segregation and that an excess of TRIM36 may cause chromosomal instability. In Xenopus laevis, TRIM36 is expressed during early embryogenesis and plays an important role in the arrangement of somites during their formation
FLFDDKCGYNSERLLLNARRDSVESRAGFSLLLGAERIQVGCYTSLDYIIGDTGITKGKHFWAFRVEPYS
YLVKVGVASDSKLQEWFHNPRDISSPRYDQDSGHDSGSEDTSFDSSQPFTLVTIGMKKLFIPKSSASSGD
AENRVLPLPTRIGICLDYDKGKVGFYDADSMKCLYERQVDCSGTMYPAFALMGSGAIHLEEPIT
>gnl|CDD|293952 cd12895, SPRY_PRY_TRIM46, PRY/SPRY domain in tripartite motif-containing protein 46 (TRIM46). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM46 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). The SPRY/PRY combination is a possible component of immune defense. This protein family has not yet been characterized
NFFLDSRWGLHRDRLAISKDQRAVRSVPGLPLLQAADRLLTSCHLSVDLVVGDVAITQGRSYWACSVDPG
SYLVKVGVGLESKLQEWFQLPQDVVSPRYDPDSGHDSGAEDATVESPPFAFLTMGMGKIYLPSSVSSGHG
LTGRDGPPAGCTVPLPPRLGICLDYEKGRVSFYDAVSFRPLWECPVDCSGPVCPAFCFIGGGALQLQEL
>gnl|CDD|293953 cd12896, SPRY_PRY_TRIM65, PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM65 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). The SPRY/PRY combination is a possible component of immune defense. This protein family has not been characterized
LRAELWKDYRNLTFDPRTANKYLELSRQNRRAKHGRSAARGVPASPGSFELWQVQCTQSFQHGHHYWEVE
VSSHSVTLGVTYPGLPRHKQGGHKDNIGRNPCSWGLQIQEDSLQAWHNGRAQKLQGVSYRLLGVDLDLEA
GTLTFYGLEPGTQRLHTFHAIFTQPLYPVFWLLEGRTLTLCH
>gnl|CDD|293954 cd12897, SPRY_PRY_TRIM50_72, PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several TRIM proteins, including TRIM72 and TRIM50. TRIM72 (also known as MG53) has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. It is expressed specifically in skeletal muscle and heart, and tethered to the plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23
RKMFRALMPALESLTFDPATAHPLLVVSSGGTVVECGLQKQRRASQPERFDKSTCVVASQGFSEGEHYWE
VVVGDKPRWALGVIKGTASRKGKLHASPSHGVWLIGLKEGKVYEAHGEPKEPRPLRVAGRPHRIGVYLSF
EDGVLSFFDASDPDDLRTLYTFQERFQGKLYPFFDVCWHDKGKNSQPLVLP
>gnl|CDD|293955 cd12898, SPRY_PRY_TRIM76, PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called cardiomyopathy-associated protein 5. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM76, a Class I TRIM protein. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5 or myospryn or SPRYD2) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It has been suggested that TRIM76 is involved in two distinct processes, protein kinase A signaling and vesicular trafficking. It has also been implicated in Duchenne muscular dystrophy and cardiac disease; gene polymorphism of TRIM76 is associated with left ventricular wall thickness in patients with hypertension while its interactions with M-band titin and calpain 3 link it to tibial and limb-girdle muscular dystrophies
GTRFLLLRETAHPALHISSDRGTVIYFHERRRKMSSLTECPSVLGEELPSCGQYYWETTVTRCPAYRLGI
CSSSASQAGALGEGSTSWCLHCVPTSEPCRYTLLHSGIVSDVFVTERPARVGTLLDYNNGRLIFINAESG
QLLGIFRHRFAQPCHPAFALEKPGKLELHMG
>gnl|CDD|293956 cd12899, SPRY_PRY_TRIM76_like, PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like. This domain is similar to the distinct PRY/SPRY subdomain found at the C-terminus of TRIM76, a Class I TRIM protein. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5 or myospryn or SPRYD2) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It has been suggested that TRIM76 is involved in two distinct processes, protein kinase A signaling and vesicular trafficking
YFHLNEDTAHPLLSISEDGFTVVYGEEELPARDLSFSDNSFTRCVAVMGSLIPVRGKHYWEVEVDEQTEY
RVGVAFEDTQRNGYLGANNTSWCMRHIITPSRHKYEFLHNGWTPDIRITVPPKKIGILLDYDSGRLSFFN
VDLAQHLYTFSCQFQHFVHPCFSLEKPGALKVHNGI
>gnl|CDD|293957 cd12900, SPRY_PRY_TRIM21, PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD Ribonucleoprotein Autoantigen (Ro52). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM21, which is also known as Sjogren Syndrome Antigen A (SSA), SSA1, 52kD Ribonucleoprotein Autoantigen (Ro52, Ro/SSA, SS-A/Ro) or RING finger protein 81 (RNF81). TRIM21 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. As an E3 ligase, TRIM21 mediates target specificity in ubiquitination; it regulates type 1 interferon and proinflammatory cytokines via ubiquitination of interferon regulatory factors (IRFs). It is up-regulated at the site of autoimmune inflammation, such as cutaneous lupus lesions, indicating a central role in the tissue destructive inflammatory process. It interacts with auto-antigens in patients with Sjogren syndrome and systemic lupus erythematosus, a chronic systemic autoimmune disease characterized by the presence of autoantibodies against the protein component of the human intracellular ribonucleoprotein-RNA complexes and more specifically TRIM21, Ro60/TROVE2 and La/SSB proteins. It binds the Fc part of IgG molecules via its PRY-SPRY domain with unexpectedly high affinity
HMVHITLDPDTANPWLILSKDRRQVRLGDTHQNVPENEERFDNYPMVLGAQRFNSGKHYWEVDVTGKEAW
DLGVCRDSVRRKGQFLLSPENGFWTIWLWNKKYEAGTSPQTTLHLQVPPCQVGIFLDYEAGVVSFYNITD
HGSLIYTFSECAFTGPLRPFFNPGFNDSGGNAAPLTLCPL
>gnl|CDD|293958 cd12901, SPRY_PRY_FSD1, Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus. This domain is part of the fibronectin type III and SPRY domain containing 1 (FSD1) and FSD1-like (FSD1L) proteins. These are centrosome-associated proteins that are characterized by an N-terminal coiled-coil region downstream of B-box (BBC) domain, a central fibronectin type III (FN3) domain, and C-terminal repeats in PRY/SPRY domain. The FSD1 protein associates with a subset of microtubules and may be involved in the stability and organization of microtubules during cytokinesis
FKLDASSSHQNLKVEDLSVEWDATGGKVLQKIKGRENDGRSRTASPRNSSARCQSPKRMPSARGGRDRFT
AESYTVLGDTLIDGGQHYWEVRAQKDSKAFSVGVAYRSLGKFDQLGKTNASWCLHVNNWLQNSFAAKHNN
KAKTLDVPVPDRIGVYCDFDEGQLSFYNARTKQLLHTFKMKFTQPVLPAFMVWCGGLSVSTGLQVPS
>gnl|CDD|293959 cd12902, SPRY_PRY_RNF135, PRY/SPRY domain in RING finger protein RNF135. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of the RING finger protein RNF135 (also known as Riplet/RNF135), which ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Normally, RIG-I is activated by TRIM25 in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. However, RNF135, consisting of an N-terminal RING finger domain, C-terminal SPRY and PRY motifs and showing sequence similarity to TRIM25, acts as an alternative factor that promotes RIG-I activation independent of TRIM25
PTFDLRSLSCSLEVSEDSRKVTVSHGPQAYAWSPDRFSISQVLCSQAFSSGQHYWEVDTRQCSHWAVGVA
SWEMSRDQMLGRTMDSWCIEWKGTGQLSAWHMNKETVLGSDKPRVVGIWLDLEEGKLAFYSVANQERLLH
ECEVSASSPLHPAFWLYGLEPGNSLIIK
>gnl|CDD|293960 cd12903, SPRY_PRY_SPRYD4, PRY/SPRY domain containing protein 4 (SPRYD4). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain and is encoded by the SPRYD4 gene. SPRYD4 (SPRY containing domain 4) is ubiquitously expressed in many human tissues, most strongly in kidney, bladder, brain, thymus and stomach. Subcellular localization demonstrates that SPRYD4 protein is localized in the nucleus when overexpressed in COS-7 green monkey cell. It has remained uncharacterized thus far
FKLDERTAHSSLDLFKKDTGVIYRMLGVDPTKVPQNPERFRDWAVVLGDTPVTSGRHYWEVTVKRSQEFR
IGVADVDMSRDECIGTNESSWVFAYAQRKWYAMVANETVPVPLVGKPDRVGLLLDYEAGKLSLVDVEKNS
VVHTMSAEFRGPVVPAFALWDGELLTHSG
>gnl|CDD|293961 cd12904, SPRY_BSPRY, SPRY domain in Ro-Ret family. This domain, named BSPRY, has been identified in the Ro-Ret family, since the protein is composed of a B-box, an alpha-helical coiled coil and a SPRY domain. The gene for BSPRY resides on human chromosome 9 and is specifically expressed in testis. The function of BSPRY is not known, but several related proteins of the RING-Box-coiled-coil (RBCC) family have been implicated in cell transformation
LRFDERTVSPLLSLSEDRRTLTFSPKKARQSPPDDPERFDHWPNALASLSFSSGTHAWVVDVGKSCAYKV
GVCYGSLERKGSGNEARLGYNAFSWVFSRYDGEFSFSHNGQHVPLELLKCPARVGVLLDWPSQELLFYDP
DSCTVLHSHREAFAAPLLPVFAVADQSISIV
>gnl|CDD|293962 cd12905, SPRY_PRY_A33L, zinc-binding protein A33-like. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM69 and TRIM proteins NF7 and bloodthirsty (bty). TRIM69 is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. TRIM protein NF7, which also contains a chromodomain (CHD) at the N-terminus and an RFP (Ret finger protein)-like domain at the C-terminus, is required for its association with transcriptional units of RNA polymerase II which is mediated by a trimeric B box. In Xenopus oocyte, xNF7 has been identified as a nuclear microtubule-associated protein (MAP) whose microtubule-bundling activity, but not E3-ligase activity, contributes to microtubule organization and spindle integrity. Bloodthirsty (bty) is a novel gene identified in zebrafish and has been shown to likely play a role in in regulation of the terminal steps of erythropoiesis
PGPAPLTFDPETAHPSLILSRDLTAVTESDEMQPYPRSPKRFLQCVNVLASQGFQSGRHYWEVWVGSKTK
WDLGVASESVDRQARVKLCPENGYWTLRLRNGDEYWAGTQPWTRLRVTSRPQRIGVFLDCEERKVSFYNA
DDMSLLYSFHQGPRGKVFPFFSTCFSDDGQNAEPMRLL
>gnl|CDD|293963 cd12906, SPRY_SOCS1-2-4, SPRY domain in the suppressor of cytokine signaling 1, 2, 4 families (SOCS1, SOCS2, SOCS4). The SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. All four SPSB proteins interact with c-Met, the hepatocyte growth factor receptor, but only SPSB1, SPSB2, and SPSB4 interact with prostate apoptosis response protein 4 (Par-4). They are negative regulators that recruit the ECS E3 ubiquitin ligase complex to polyubiquitinate inducible nitric-oxide synthase (iNOS), resulting in its proteasomal degradation, thus contributing to protection against the cytotoxic effect of iNOS in activated macrophages. It has been shown that SPSB1 and SPSB4 induce the degradation of iNOS more strongly than SPSB2. The Drosophila melanogaster SPSB1 homolog, GUSTAVUS, interacts with the DEAD box RNA helicase Vasa. Suppressor of cytokine signaling (SOCS) proteins negatively regulate signaling from JAK-associated cytokine receptor complexes, and play key roles in the regulation of immune homeostasis
HAWNPDDRSLNIFVKEDDPLTFHRHPVAQSTDCIRGKVGYSRGLHVWEITWPTRQRGTHAVVGVATKDAP
LHCVGYTSLVGSNEESWGWDIGRNKLYHDSKNQPGWTYPAFLEPDENFVVPDKFLVVLDMDEGTLSFVVD
GQYLGVAFRGLKGKKLYPIVSAVWGHCEVTMKYI
>gnl|CDD|293964 cd12907, SPRY_Fbox, SPRY domain in the F-box family Fbxo45. Fbxo45 is a novel synaptic E3 and ubiquitin ligase, related to the suppressor of cytokine signaling (SOCS) proteins and located N-terminal to a SPRY (SPla and the ryanodine receptor) domain. Fbxo45 induces the degradation of a synaptic vesicle-priming factor, Munc13-1, via the SPRY domain, thus playing an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse. F-box motifs are found in proteins that function as the substrate recognition component of SCF E3 complexes
HAWNPNDCSRNIYIKPNGFTLHRNPVAQSTDGARGKIGFSSGRHAWEVWWEGPLGTVAVVGIATKHAPLQ
CQGYVALLGSDDQSWGWNLVDNHLLHNGDSQGNYPQCNNAPKYQVGERIRVILDCEDNTLAFERGYEFLG
VAFRGLPPTKLYPAVSAVYGNTEVSMVYLGPPLDG
>gnl|CDD|293965 cd12908, SPRYD3, SPRY domain-containing protein 3. This family contains SPRY domain-containing protein 3 (SPRYD3). In humans, it is highly expressed in most tissues, including brain, kidney, heart, intestine, skeletal muscle, and testis. It also has cross-species conservation, suggesting that it is likely to carry out important cellular processes
WERLNDVRVNGDVLEYHGRGIGDVGLAQARRPLSPDNHYFEVEIVDPGVRCYIAIGLAPQDYPLDRHPGW
NPGSVAYHADDGKLFKGSGVGDQFGPRCTKGDRMGCGIRFPRDYDTDSEDQGDEEEGRTVQVFFTRNGKE
VGRTEVPLPPGGFYPAVGMHSEGEKVRVDLH
>gnl|CDD|293966 cd12909, SPRY_RanBP9_10, SPRY domain in Ran binding proteins 9 and 10. This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells
YKGPGKTDKDAAAVRANHPIPPQCGIYYFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDD
GHSFCSSGTGKPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKKGNLYPTVGLRTPGEHVEA
NFGQ
>gnl|CDD|293967 cd12910, SPRY_SSH4_like, SPRY domain in SSH4 and similar proteins. This family includes SPRY domain in SSH4 (suppressor of SHR3 null mutation protein 4) and similar proteins. SSH4 is a component of the endosome-vacuole trafficking pathway that regulates nutrient transport and may be involved in processes determining whether plasma membrane proteins are degraded or routed to the plasma membrane. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. In yeast, SSH4 and the homologous protein EAR1 (endosomal adapter of RSP5) recruit Rsp5p, an essential ubiquitin ligase of the Nedd4 family, and assist it in its function at multivesicular bodies by directing the ubiquitylation of specific cargoes
LQEPGVGAWEFVPNIERTCIVRNKTELSFLDDTILSSLPLYSVQTNLPLPTGRPKTIYFEVKIFELPRAD
DTSVAIGFATKPYPPFRLPGWHRGSLAVHSDDGHRYINDPFGGKDFTPPFREGDTIGIGYRFSSGTIFFT
RNGKRLGGWDLGEELDAEDDGVTGLEGFHDLYAAIGVFGGECEVHVNPGQWG
>gnl|CDD|350336 cd12911, HK_sensor, Sensor domains of Histidine Kinase receptors. Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution
YFDEVLSKLRTFNPDLGYAFMLSNDGRLLSHWTKKDWIGDKALYDFGEELEKYQRAIKNGIDGHTLPTAS
PTTGVTVILFYRPVEKEGTFDGVVVVVVPK
>gnl|CDD|350337 cd12912, PDC2_MCP_like, second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains. Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses
ELSEIISSIKIGETGYAFLVDKDGTIIAHPDKELVGKKISDDEAAEEELAKKMLAGKSGSVEYTFNGEKK
YVAYAPIPGTGWSLVVVVPESE
>gnl|CDD|350338 cd12913, PDC1_MCP_like, first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains. Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses
FLEEAESIAEQLASTLESLVSSGSLDRELLENLLKQVLESNPDILGVYVAFEPNAFSDETGRFAPYWYRD
DGGIIDLDEPPDYDYRTRDWYKLAKETGKPVWTEPYIDEVGTGVLMITISVPIYDNGKFIGVVGVDISL
>gnl|CDD|350339 cd12914, PDC1_DGC_like, first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains. Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses
LDEADLLLRSLADDLEARGAASADPAALQALLRRLLARLPEVRSIFVVDADGRVVASSGPGPAPGLDVSD
RDYFQAARAGGGGLFISEPVISRVTGKPVIPLSRPIRDADGRFAGVVVASIDL
>gnl|CDD|350340 cd12915, PDC2_DGC_like, second PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains. Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses
YFSRLYRSLDLGPGGAVALLRRDGTVLARYPDDEGAVGRSLADPLFRALLAAAPSGTFRAVSPLDGVERL
YAYRRLPGYPLVVVVGLSEDDVLAPW
>gnl|CDD|240599 cd12916, VKOR_1, Vitamin K epoxide reductase family in bacteria and plants. This family includes vitamin K epoxide reductase (VKOR) present in bacteria and plant. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some plant and bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade
SRRLIAGLALIGLLETAYLTYVKLTGSSAVCPGGGGCDTVLNSPYATLLGIPLSLFGFLAYLAILVLAVL
PLLLKSEKLERWTWLLLFGLATAGVVFSAYLTYLLAFVIGAFCPYCLTSAVLSTLLFLLTILG
>gnl|CDD|240600 cd12917, VKOR_euk, Vitamin K epoxide reductase family in eukaryotes, excluding plants. This family includes vitamin K epoxide reductase (VKOR) present in bacteria and plant. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. Warfarin, a widely used oral anticoagulant used in medicine as well as rodenticides, inhibits the activity of VKOR, resulting in decreased levels of reduced vitamin K, which is required for the function of several clotting factors. However, anticoagulation effect of warfarin is significantly associated with polymorphism of certain genes, including VKORC1. Interestingly, in rodents, an adaptive trait appears to have evolved convergently by selection on new or standing genetic polymorphisms in VKORC1 as well as by adaptive introgressive hybridization between species, likely brought about by human-mediated dispersal
LLRLALCLAGLLLSLYALYVELKKERDPDYRALCDISESISCSKVFSSRYGRGFGLLGLILGKDSILNQP
NSVFGIIFYILQLLLGLTNSAVAALLLLTLSILSVVGSLYLAYILYFVLKDFCIVCVSTYVVNFLLLILN
>gnl|CDD|240601 cd12918, VKOR_arc, Vitamin K epoxide reductase family in archaea and some bacteria. This family includes vitamin K epoxide reductase (VKOR) mostly present in archaea and some bacteria. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade
LLGLALSLVGLLASAYLTYEHYLKRPPLACTISGVINCEKVLSSPYSRILGVPLAVLGLAWFAVLLVLSL
LAALRVRLLLGALLYWSILGIAFVPYLVYLELFLIGAICLYCTVAHVIILALFIII
>gnl|CDD|240602 cd12919, VKOR_2, Vitamin K epoxide reductase family in bacteria. This family includes vitamin K epoxide reductase (VKOR) present only in bacteria. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade
GWSYNPSSWPQRLPIIALAFVGLFISRYLAAYQLGYIDSVWDPFFGNGTERVLTSSVSKAFPVPDAGLGA
LAYTLEILTGFMGGRARWRTMPWMVLLFGVLVIPLGLVSILLIIIQPILVGAWCTLCLISAAIMLLMIPL
AVDEVLAMLQFLKRVRRRGQSLWKAFWKG
>gnl|CDD|240603 cd12920, VKOR_3, Vitamin K epoxide reductase family in bacteria. This family includes vitamin K epoxide reductase (VKOR) present in proteobacteria and spirochetes. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade
AIALVLALIGLAFSGLLTYHHYGILTDGVGSSFCAINEVVNCDKVAQSPYSAIGGVPIALWGLLAYGFLA
ALFLLALISREDSERAAGLLFLVLLVGLVADLVLGLISVTAIGALCILCAGTYIVSAALLFGAW
>gnl|CDD|240604 cd12921, VKOR_4, Vitamin K epoxide reductase (VKOR) family in bacteria. This family includes vitamin K epoxide reductase (VKOR) present only in bacteria. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade. This family also has a cysteine peptidase domain present at the N-terminus of the VKOR domain
LLLLLLSLIGLLISILLLLKELGKSNKILKKFCSIGKKVDCNAVLKSKGAKIGGISLSELGLLYFFGLLL
LLLLSPLNSSLLFLLSLLLLLALPAELYSIYYQKFVIKKWCPLCLSIQAILWLLFLLL
>gnl|CDD|240605 cd12922, VKOR_5, Vitamin K epoxide reductase family in bacteria. This family includes vitamin K epoxide reductase (VKOR) mostly present in actinobacteria. VKOR (also named VKORC1) is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. All homologs of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle. In some bacterial homologs, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases which may function as redox partners in initiating the reduction cascade
WLLLVAGLIGLVASFVLTVEKIQLLEDPDYVLSCDINPVVSCGSVMQSWQASLFGFPNPLIGLAAFAVVI
TVGVALLAGARLPRWFWVGLQAGLAAGLVFVHWLIYQSLFVIGALCPYCMVVWAVTIPLFWYV
>gnl|CDD|214016 cd12923, iSH2_PI3K_IA_R, Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits
DDVEKLAKKLKEINKEYLDKSREYDELYEKYNKLSQEIQLKRQALEAFEEAVKMFEEQLRTQEKFQKEAQ
PHEKQRLMENNELLKSRLKELEESKEQLEEDLRKQVAYNRELEREMNSLKPELMQLRKQKDQYLRWLKRK
GVSQEEINQLLK
>gnl|CDD|214017 cd12924, iSH2_PIK3R1, Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 1, PIK3R1, also called p85alpha. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In addition, p85alpha, also called PIK3R1, contains N-terminal SH3 and GAP domains. p85alpha carry functions independent of its PI3K regulatory role. It can independently stimulate signaling pathways involved in cytoskeletal rearrangements. Insulin-sensitive tissues express splice variants of the PIK3R1 gene, p50alpha and p55alpha, which may play important roles in insulin signaling during lipid and glucose metabolism. Mice deficient with PIK3R1 die perinatally, indicating its importance in development
DNIEAVGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNETIKIFEEQCQTQERYSKEYI
EKFKREGNEKEIQRIMHNYEKLKSRISEIVDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQ
YLMWLTQKGVRQKKLNEWLGN
>gnl|CDD|214018 cd12925, iSH2_PIK3R3, Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 3, PIK3R3, also called p55gamma. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p55gamma, also called PIK3R3 or p55PIK, also contains a unique N-terminal 24-amino acid residue (N24) that interacts with cell cycle modulators to promote cell cycle progression
DNIDAVGRKLQEYHSQYQEKSKEYDRLYEEYTKTSQEIQMKRTAIEAFNETIKIFEEQCHTQERYSKEYI
ERFRREGNEKEIERIMMNYEKLKSRLGEIHDSKMRLEQDLKTQALDNREIDKKMNSIKPDLIQLRKIRDQ
YLVWLNHKGVRQKRINDWLGI
>gnl|CDD|214019 cd12926, iSH2_PIK3R2, Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta. PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects
DSVEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKCSKEYL
ERFRREGNEKEMQRILLNSERLKSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKPDLMQLRKIRDQ
YLVWLTQKGARQKKINEWLGI
>gnl|CDD|240571 cd12927, MMP_TTHA0227_like, Minimal MMP-like domain found in Thermus thermophilus TTHA0227, Acidothermus cellulolyticus ACEL2062 and similar proteins. The family includes hypothetical proteins from bacteria that contain a minimal metalloprotease (MMP)-like domain consisting of 3-stranded mixed 2-beta sheets.These proteins may belong to a superfamily of bacterial zinc metallo-peptidases, which is characterized by a conserved HExxHxxGxxD (x could be any amino acid) motif. However, some family members carry a shorter HExxHxxG motif or HExxH motif. Some others do not have such a motif, but still share very high sequence similarity
AEEFDDLVEEALDRLPERFPDELDNVGIAVEDVPPEDPLGWEDDPVLLGLYEGAPLTGGLPDRIVLYRRP
IERRARDEEELRELVRETVVHELAHHL
>gnl|CDD|240592 cd12929, GUCT, RNA-binding GUCT domain found in the RNA helicase II/Gu protein family. This family includes vertebrate RNA helicase II/Gualpha (RH-II/Gualpha) and RNA helicase II/Gubeta (RH-II/Gubeta), both of which consist of a DEAD box helicase domain (DEAD), a helicase conserved C-terminal domain, and a Gu C-terminal (GUCT) domain. They localize to nucleoli, suggesting roles in ribosomal RNA production, but RH-II/Gubeta also localizes to nuclear speckles containing the splicing factor SC35, suggesting its possible involvement in pre-mRNA splicing. In contrast to RH-II/Gualpha, RH-II/Gubeta has RNA-unwinding activity, but no RNA-folding activity. The family also contains plant DEAD-box ATP-dependent RNA helicase 7 (RH7 or PRH75), Thermus thermophilus heat resistant RNA-dependent ATPase (Hera) and similar proteins. RH7 is a new nucleus-localized member of the DEAD-box protein family from higher plants. It displays a weak ATPase activity which is barely stimulated by RNA ligands. RH7 contains an N-terminal KDES domain rich in lysine, glutamic acid, aspartic acid, and serine residues, seven highly conserved helicase motifs in the central region, a GUCT domain, and a C-terminal GYR domain harboring a large number of glycine residues interrupted by either arginines or tyrosines. Thermus thermophilus Hera is a DEAD box helicase that binds fragments of 23S rRNA and RNase P RNA via its C-terminal domain. It contains a helicase core that harbors two RecA-like domains termed RecA_N and RecA_C, a dimerization domain (DD), and a C-terminal RNA-binding domain (RBD) that reveals a compact, RRM-like fold and shows sequence similarity with the typical GUCT domain found in the RNA helicase II/Gu protein family
GWVTYKLEGPRLIQSLSRLVALLKRQLLSNVSEVGKVAELEGNGGFYFDVRPEARERLQAEPEVAGLRLE
VA
>gnl|CDD|410577 cd12930, GAT_SF, GAT domain found in eukaryotic GGAs, metazoan Tom1-like proteins, metazoan STAMs, fungal Vps27, and similar proteins. The GAT (GGA and Tom1) domain superfamily includes the canonical GAT domain found in ADP-ribosylation factor (Arf)-binding proteins (GGAs) from eukaryotes, myb protein 1 (Tom1)-like proteins from metazoa, and LAS seventeen-binding protein 5 (Lsb5p)-like proteins from fungi. The canonical GAT domain is a monomeric three-helix bundle that binds ubiquitin. GGAs, also called Golgi-localized gamma-ear-containing Arf-binding proteins, belong to a family of ubiquitously expressed, monomeric, motif-binding cargo/clathrin adaptor proteins that regulate clathrin-mediated trafficking of cargo proteins from the trans-Golgi network (TGN) to endosomes. GGAs play important roles in ubiquitin-dependent sorting of cargo proteins both in biosynthetic and endocytic pathways. Tom1 and its related proteins, Tom1L1 and Tom1L2, form a protein family sharing an N-terminal VHS-domain followed by a GAT domain. Tom1 family proteins bind to ubiquitin, ubiquitinated proteins, and Toll-interacting protein (Tollip) through its GAT domain. They do not associate with either Arf GTPases through its GAT domain nor with acidic cluster-dileucine sequences through its VHS domain. The GAT domain superfamily also includes the non-canonical GAT domain found in several components of the ESCRT-0 complex, including signal transducing adapter molecules (STAMs) and hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs) from metazoa, as well as vacuolar protein sorting-associated protein 27 (Vps27) and class E vacuolar protein-sorting machinery protein Hse1 from fungi. Hrs, together with STAM, forms a Hrs/STAM core complex. Vps27, together with Hse1, forms a Vps27/Hse1 core complex. Those complexes consist of two intertwined GAT domains, each consisting of two helices from one subunit, and one from the other subunit. The intertwined GAT heterodimer acts as a scaffold for binding of ubiquitinated cargo proteins and coordinating ubiquitination and deubiquitination reactions that regulate sorting
EEVKDNVRXFSELLEKXKSRPLEILDDELLQELAQRCFASKARLNYLLNDKADDQKYNTLLEXNDNLSEV
XNIYDRL
>gnl|CDD|240579 cd12931, eNOPS_SF, NOPS domain, including C-terminal helical extension region, in the p54nrb/PSF/PSP1 family. All members in this family contain a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRM1 and RRM2), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain with a long helical C-terminal extension. The NOPS domain specifically binds to RRM2 domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies. PSF has an additional large N-terminal domain that differentiates it from other family members. The p54nrb/PSF/PSP1 family includes 54 kDa nuclear RNA- and DNA-binding protein (p54nrb), polypyrimidine tract-binding protein (PTB)-associated-splicing factor (PSF) and paraspeckle protein 1 (PSP1), which are ubiquitously expressed and are well conserved in vertebrates. p54nrb, also termed NONO or NMT55, is a multi-functional protein involved in numerous nuclear processes including transcriptional regulation, splicing, DNA unwinding, nuclear retention of hyperedited double-stranded RNA, viral RNA processing, control of cell proliferation, and circadian rhythm maintenance. PSF, also termed POMp100, is also a multi-functional protein that binds RNA, single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and many factors, and mediates diverse activities in the cell. PSP1, also termed PSPC1, is a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm. The cellular function of PSP1 remains unknown currently. The family also includes some p54nrb/PSF/PSP1 homologs from invertebrate species. For instance, the Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA) and Chironomus tentans hrp65 gene encoding protein Hrp65. D. melanogaster NONA is involved in eye development and behavior and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans Hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore
PRPVVVEPLEQRDEEDGLPERNVKKNAGYQKEREVGPRFAPPGSFEYEFGQRWKALYELEKQQREQLEKE
LKEAREKLEAEMEAARYEHQ
>gnl|CDD|240576 cd12932, RRP7_like, RRP7 domain ribosomal RNA-processing protein 7 (Rrp7p), ribosomal RNA-processing protein 7 homolog A (Rrp7A), and similar proteins. This CD corresponds to the RRP7 domain of Rrp7p and Rrp7A. Rrp7p is encoded by YCL031C gene from Saccharomyces cerevisiae. It is an essential yeast protein involved in pre-rRNA processing and ribosome assembly, and is speculated to be required for correct assembly of rpS27 into the pre-ribosomal particle. Rrp7A, also termed gastric cancer antigen Zg14, is the Rrp7p homolog mainly found in Metazoans. The cellular function of Rrp7A remains unclear currently. Both Rrp7p and Rrp7A harbor an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal RRP7 domain
GLKKWVAEYKRSRPDPAELQSEVDEYMEEFDKREEEEKEEAKEARNEPDEDGFVTVTRGGRKGKTAREEA
VEAKAKEKEKKKKKKKELEDFYRFQIREKKKEELAELRKKFEEDKKRI
>gnl|CDD|240597 cd12933, eIF3G, eIF3G domain found in eukaryotic translation initiation factor 3 subunit G (eIF-3G) and similar proteins. eIF-3G, also termed eIF-3 subunit 4, or eIF-3-delta, or eIF3-p42, or eIF3-p44, is the RNA-binding subunit of eIF3. eIF3 is a large multi-subunit complex that plays a central role in the initiation of translation by binding to the 40 S ribosomal subunit and promoting the binding of methionyl-tRNAi and mRNA. eIF-3G binds 18 S rRNA and beta-globin mRNA, and therefore appears to be a nonspecific RNA-binding protein. Besides, eIF-3G is one of the cytosolic targets; it interacts with mature apoptosis-inducing factor (AIF). This family also includes yeast eIF3-p33, a homolog of vertebrate eIF-3G; it plays an important role in the initiation phase of protein synthesis in yeast. It binds both mRNA and rRNA fragments due to an RNA recognition motif near its C-terminus
DGTKTVIEYRINDDGKKVKITRTYKEEKVKRKVSKAVAERKKWKKFGDEKGDPPGPNPATTIVGEEVFLQ
LIRNKEELEEEEEEAKKKKKKGKKLVVCRICKGDHWTTKCPYKD
>gnl|CDD|240585 cd12934, LEM, LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner nuclear membrane protein Man1 and similar proteins. The family corresponds to a group of inner nuclear membrane proteins containing LEM domain. Emerin occurs in four phosphorylated forms and plays a role in cell cycle-dependent events. It is absent from the inner nuclear membrane in most patients with X-linked muscular dystrophy. Emerin interacts with A-type and B-type lamins. Man1, also termed LEM domain-containing protein 3 (LEMD3) is an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. LAP2, also termed thymopoietin (TP), or thymopoietin-related peptide (TPRP), is composed of isoform alpha and isoforms beta/gamma and may be involved in chromatin organization and post-mitotic reassembly. Some LAP2 isoforms are inner nuclear membrane proteins that can bind to nuclear lamins and chromatin, while others are non-membrane nuclear polypeptides. This family also contains LEM domain-containing protein LEMP-1 and LEM2. LEMP-1, also termed cancer/testis antigen 50 (CT50), is encoded by LEMD1, a novel testis-specific gene expressed in colorectal cancers. LEMP-1 may function as a cancer-testis antigen for immunotherapy of colorectal carcinoma (CRC). LEM2, also termed LEMD2, is a novel Man1-related ubiquitously expressed inner nuclear membrane protein required for normal nuclear envelope morphology. Association with lamin A is required for its proper nuclear envelope localization while its binding to lamin C plays an important role in the organization of lamin A/C complexes. Some uncharacterized LEM domain-containing proteins are also included in this family. Unlike other family members, these harbor an ankyrin repeat region that may mediate protein-protein interactions
LSDDELRRELKELGEPPGPITDTTRKVYLKKLAKLLK
>gnl|CDD|240596 cd12935, LEM_like, LEM-like domain of lamina-associated polypeptide 2 (LAP2) and similar proteins. LAP2, also termed thymopoietin (TP), or thymopoietin-related peptide (TPRP), is composed of isoform alpha and isoforms beta/gamma and may be involved in chromatin organization and postmitotic reassembly. Some of the LAP2 isoforms are inner nuclear membrane proteins that can bind to nuclear lamins and chromatin, while others are nonmembrane nuclear polypeptides. All LAP2 isoforms contain an N-terminal lamina-associated polypeptide-Emerin-MAN1 (LEM)-domain that is connected to a highly divergent LEM-like domain by an unstructured linker. Both LEM and LEM-like domains share the same structural fold, mainly composed of two large parallel alpha helices. However, their biochemical nature of the solvent-accessible residues is completely different, which indicates the two domains may target different protein surfaces. The LEM domain is responsible for the interaction with the nonspecific DNA binding protein barrier-to-autointegration factor (BAF), and the LEM-like domain is involved in chromosome binding. The family also includes the yeast helix-extension-helix domain-containing proteins, Heh1p (formerly called Src1p) and Heh2p, and their uncharacterized homologs found mainly in fungi and several in bacteria. Heh1p and Heh2p are inner nuclear membrane proteins that might interact with nuclear pore complexes (NPCs). Heh1p is involved in mitosis. It functions at the interface between subtelomeric gene expression and transcription export (TREX)-dependent messenger RNA export through NPCs. The function of Heh2p remains ill-defined. Both Heh1p and Heh2p contain a LEM-like domain (also termed HeH domain), but lack a LEM domain
PSSLTVAELRSILTEHGVEYPSNAKKAELVKLFNKH
>gnl|CDD|240593 cd12936, GUCT_RHII_Gualpha_beta, RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA helicase II/Gubeta (RH-II/Gubeta) and similar proteins. This subfamily corresponds to the Gu C-terminal (GUCT) domain of RH-II/Gualpha and RH-II/Gubeta, two paralogues found in vertebrates. RH-II/Gualpha, also termed nucleolar RNA helicase 2, or DEAD box protein 21, or nucleolar RNA helicase Gu, is a bifunctional enzyme that displays independent RNA-unwinding and RNA-folding activities. It unwinds double-stranded RNA in the 5' to 3' direction in the presence of Mg2+ through the domains in its N-terminal region. In contrast, it folds single-stranded RNA in an ATP-dependent manner and its C-terminal region is responsible for the Mg2+ independent RNA-foldase activity. RH-II/Gualpha consists of a DEAD box helicase domain (DEAD), a helicase conserved C-terminal domain (helicase_C), and a GUCT followed by three FRGQR repeats and one PRGQR sequence. The DEAD and helicase_C domains may play critical roles in the RNA-helicase activity of RH-II/Gualpha. The function of GUCT domain remains unclear. The C-terminal region responsible for the RNA-foldase activity does not overlap with the GUCT domain. RH-II/Gubeta, also termed ATP-dependent RNA helicase DDX50, or DEAD box protein 50, or nucleolar protein Gu2, shows significant sequence homology with RH-II/Gualpha. It contains a DEAD domain, a helicase_C domain, and a GUCT domain followed by an arginine-serine-rich sequence but not (F/P)RGQR repeats in RH-II/Gualpha. Both RH-II/Gualpha and RH-II/Gubeta localize to nucleoli, suggesting roles in ribosomal RNA production, but RH-II/Gubeta also localizes to nuclear speckles containing the splicing factor SC35, suggesting its possible involvement in pre-mRNA splicing. In contrast to RH-II/Gualpha, RH-II/Gubeta has RNA-unwinding activity, but no RNA-folding activity
HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVP
TAEVESIQAEWHDSRRWQLSVAT
>gnl|CDD|240594 cd12937, GUCT_RH7_like, RNA-binding GUCT domain found in plant DEAD-box ATP-dependent RNA helicase 7 (RH7) and similar proteins. This subfamily corresponds to the Gu C-terminal (GUCT) domain of RH7 and similar proteins. RH7, also termed plant RNA helicase 75 (PRH75), is a new nucleus-localized member of the DEAD-box protein family from higher plants. It displays a weak ATPase activity which is barely stimulated by RNA ligands. RH7 contains an N-terminal KDES domain rich in lysine, glutamic acid, aspartic acid, and serine residues, seven highly conserved helicase motifs in the central region, a GUCT domain, and a C-terminal GYR domain harboring a large number of glycine residues interrupted by either arginines or tyrosines. RH7 is RNA specific and harbors two possible RNA-binding motifs, the helicase motif VI (HRIGRTGR) and the C-terminal glycine-rich GYR domain
RSLLTSHEGYTTLLLKSNTPIRSPGYVWNALRRYLPEDIVESIKGMTLTADGKGAVFDVPSELIEEFLSA
WVDKRGVTLEVATELP
>gnl|CDD|240595 cd12938, GUCT_Hera, RNA-binding GUCT-like domain found in Thermus thermophilus heat resistant RNA-dependent ATPase (Hera) and similar proteins. This subfamily corresponds to the Gu C-terminal (GUCT)-like domain of Hera and similar proteins. Thermus thermophilus Hera is a DEAD box helicase that binds fragments of 23S rRNA and RNase P RNA via its C-terminal domain. It contains a helicase core that harbors two RecA-like domains termed RecA_N and RecA_C, a dimerization domain (DD), and a C-terminal RNA-binding domain (RBD) that reveals a compact, RRM-like fold and shows sequence similarity with GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA helicase II/Gubeta (RH-II/Gubeta) and plant DEAD-box ATP-dependent RNA helicase 7 (RH7 or PRH75)
PRSLLTGEEGWTTLQLTGSRLLPPGSVRRAVGLLSRAAADGVGKIRILADAGGAVFDLPEEIAKELLAKS
DLDG
>gnl|CDD|240586 cd12939, LEM_emerin, LEM (Lap2/Emerin/Man1) domain found in emerin. This CD corresponds to the LEM domain that is critical for binding to lamin A/C and is also involved in interaction with the DNA binding protein barrier-to-autointegration factor (BAF). Emerin is an inner nuclear membrane protein that occurs in four differently phosphorylated forms and plays a role in cell cycle-dependent events. It is absent from the inner nuclear membrane in most patients with X-linked muscular dystrophy. Emerin interacts with A-type and B-type lamins. It contains an N-terminal LEM domain followed by a poly-serine segment, a region rich in hydrophobic amino acids comprising the nuclear localization signal (NLS) followed by another poly-serine segment, and a C-terminal transmembrane region
YKDLSDDELIKVLRKYGIKHGPVVGSTRKLYEKKLREAERESK
>gnl|CDD|240587 cd12940, LEM_LAP2_LEMD1, LEM (Lap2/Emerin/Man1) domain found in lamina-associated polypeptide 2 (LAP2), LEM domain-containing protein 1 (LEMP-1) and similar proteins. This CD corresponds to the LEM domain of LAP2, LEMP-1 and similar proteins. LAP2, also termed thymopoietin (TP), or thymopoietin-related peptide (TPRP), is composed of isoform alpha and isoforms beta/gamma and may be involved in chromatin organization and post-mitotic reassembly. Some of LAP2 isoforms are inner nuclear membrane proteins that can bind to nuclear lamins and chromatin, while others are non-membrane nuclear polypeptides. All LAP2 isoforms contain an N-terminal LEM domain that is connected to a highly divergent LEM-like domain by an unstructured linker. Although LEM and LEM-like domains share the same structural fold composed of two large parallel alpha helices, the biochemical nature of the solvent-accessible residues is completely different, indicating that the two domains may target different protein surfaces. The LEM domain interacts with the nonspecific DNA binding protein barrier-to-autointegration factor (BAF) while the LEM-like domain is involved in chromosome binding. LEMP-1, also termed cancer/testis antigen 50 (CT50), is encoded by LEMD1, a novel testis-specific gene expressed in colorectal cancers. It may function as a cancer-testis antigen for immunotherapy of colorectal carcinoma (CRC). LEMP-1 contains an N-terminal LEM domain
DVTELSDEELKAQLLKYGVKPGPITASTRKLYEKKLQKLLDQ
>gnl|CDD|240588 cd12941, LEM_LEMD2, LEM (Lap2/Emerin/Man1) domain found in LEM domain-containing protein 2 (LEM2). This CD corresponds to the LEM domain that is responsible for the interaction with chromatin protein barrier-to-autointegration factor (BAF). LEM2, also termed LEMD2, is a novel Man1-related ubiquitously expressed inner nuclear membrane protein required for normal nuclear envelope morphology. Association with lamin A is required for its proper nuclear envelope localization. It also binds to lamin C and plays an important role in the organization of lamin A/C complexes. LEM2 contains an N-terminal LEM domain, two putative transmembrane domains and a MAN1-Src1p C-terminal (MSC) domain, but lacks the Man1-specific C-terminal RNA recognition motif (RRM)
LTDAELRRELLALGFRPGPITETTRKVYIKKLSCLRAE
>gnl|CDD|240589 cd12942, LEM_Man1, LEM (Lap2/Emerin/Man1) domain found in inner nuclear membrane protein Man1. This CD corresponds to the LEM domain of Man1 and similar proteins. Man1, also termed LEM domain-containing protein 3 (LEMD3), is an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. It is part of a protein complex essential for chromatin organization and cell division. It also functions as an important negative regulator for the transforming growth factor beta (TGF-beta) /activin/Nodal signaling pathway and bone morphogenetic protein (BMP) signaling pathway by directly interacting with chromatin-associated proteins and transcriptional regulators, including the R-Smads, Smad1, Smad2, and Smad3. Man1 is a unique type of left/right (LR) signaling regulator that acts on the inner nuclear membrane. Furthermore, Man1 plays a crucial role in angiogenesis. The vascular remodeling can be regulated at the inner nuclear membrane through interactions between Man1 and Smads. Man1 contains an N-terminal LEM domain, two putative transmembrane domains, a Man1-Src1p C-terminal (MSC) domain, and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The LEM domain interacts with DNA and chromatin-binding protein Barrier-to-Autointegration Factor, and is also necessary for efficient localization of Man1 in the inner nuclear membrane. It has been shown that the C-terminal nucleoplasmic region of Man1 exhibits a DNA binding winged helix domain and is responsible for both, DNA- and Smad-binding
AAAQLTDEELFSELKRLGFSPGPVTESTRPVYLKKLKKLREEER
>gnl|CDD|240590 cd12943, LEM_ANKL1, LEM (Lap2/Emerin/Man1) domain found in ankyrin repeat and LEM domain-containing protein 1 (ANKL1). The family includes ANKL1, also termed ankyrin repeat domain-containing protein 41 (ANKRD41), or LEM-domain containing protein 3 (LEM3), and similar proteins. Although their biological roles remain unclear, the family members contain an N-terminal ankyrin repeat region, LEM domain and C-terminal GIY-YIG nuclease domain. The ankyrin repeats are unique motifs mediating protein-protein interactions. The LEM domain, mainly found in inner nuclear membrane proteins, may be involved in protein- or DNA-binding
LSDLDLLRGLRALGESPGPITPFTRRVYLRRLEELQRA
>gnl|CDD|240591 cd12944, LEM_ANKL2, LEM (Lap2/Emerin/Man1) domain found in ankyrin repeat and LEM domain-containing protein 2 (ANKL2). The family includes ANKL2 and similar proteins. Although their biological roles remain unclear, the family members share an N-terminal LEM domain and an ankyrin repeat region. The LEM domain, mainly found in inner nuclear membrane proteins, may be involved in protein- or DNA-binding. The ankyrin repeats are unique motifs mediating protein-protein interactions
RLKKLSPDELREELRKAGLKCGPITSTTRFLFEKKLAQALLEQ
>gnl|CDD|240580 cd12945, NOPS_NONA_like, NOPS domain, including C-terminal coiled-coil region, in p54nrb/PSF/PSP1 homologs from invertebrate species. The family contains a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain. This model corresponds to the NOPS domain, with a long helical C-terminal extension, found in Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA), Chironomus tentans hrp65 gene encoding protein Hrp65 and similar proteins. D. melanogaster NONA is involved in eye development and behavior, and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore. The NOPS domain specifically binds to the second RNA recognition motif (RRM2) domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies
LRPCVVEPMEEIDDEDGLPEKSLNKKNPEFNKERSIGPRFAEPNSFEHEYGTRWKQLHELYKQKEEALKR
ELKMEEEKLEAQMEYARYEHETELLREQLR
>gnl|CDD|240581 cd12946, NOPS_p54nrb_PSF_PSPC1, NOPS domain, including C-terminal coiled-coil region, in p54nrb/PSF/PSPC1 family proteins. The family contains a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain. This model corresponds to the NOPS domain, with a long helical C-terminal extension, found in the p54nrb/PSF/PSPC1 proteins. The NOPS domain specifically binds to the second RNA recognition motif (RRM2) domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies. Members in the family include 54 kDa nuclear RNA- and DNA-binding protein (p54nrb), polypyrimidine tract-binding protein (PTB)-associated-splicing factor (PSF) and paraspeckle protein component 1 (PSPC1 or PSP1), which are ubiquitously expressed and are conserved in vertebrates. p54nrb, also termed NONO or NMT55, is a multi-functional protein involved in numerous nuclear processes including transcriptional regulation, splicing, DNA unwinding, nuclear retention of hyperedited double-stranded RNA, viral RNA processing, control of cell proliferation, and circadian rhythm maintenance. PSF, also termed POMp100, is a multi-functional protein that binds RNA, single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and many factors, and mediates diverse activities in the cell. PSPC1 is a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm. The cellular function of PSPC1 remains unknown currently. PSF has an additional large N-terminal domain that differentiates it from other family members
PRPVIVEPMEQLDDEDGLPEKLAQKNQQYHKEREQPPRFAQPGTFEYEYAQRWKALDEMEKQQREQVDRN
IKEAKEKLESEMEAARHEHQAML
>gnl|CDD|240582 cd12947, NOPS_p54nrb, NOPS domain, including C-terminal coiled-coil region, in 54 kDa nuclear RNA- and DNA-binding protein (p54nrb) and similar proteins. The family contains a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain. This model corresponds to the NOPS domain, with a long helical C-terminal extension, found in p54nrb, also termed non-POU domain-containing octamer-binding protein (NONO), or 55 kDa nuclear protein (NMT55), or DNA-binding p52/p100 complex 52 kDa subunit. It is a multi-functional protein involved in numerous nuclear processes including transcriptional regulation, splicing, DNA unwinding, nuclear retention of hyperedited double-stranded RNA, viral RNA processing, control of cell proliferation, and circadian rhythm maintenance. p54nrb is ubiquitously expressed and highly conserved in vertebrates. It binds both single- and double-stranded RNA and DNA, and also possesses inherent carbonic anhydrase activity. p54nrb forms a heterodimer with paraspeckle component 1 (PSPC1 or PSP1), localizing to paraspeckles in an RNA-dependent manner. It also forms a heterodimer with polypyrimidine tract-binding protein-associated-splicing factor (PSF). The NOPS domain specifically binds to the second RNA recognition motif (RRM2) domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for paraspeckle localization to subnuclear bodies
PRPVTVEPMDQLDDEEGLPEKLVIKNQQYHKEREQPPRFAQPGSFEYEYAMRWKALIEMEKQQQEQVDRN
IKEAREKLEMEMEAARHEHQVMLM
>gnl|CDD|240583 cd12948, NOPS_PSF, NOPS domain, including C-terminal coiled-coil region, in polypyrimidine tract-binding protein (PTB)-associated-splicing factor (PSF) and similar proteins. This model contains the NOPS (NONA and PSP1) domain PSF (also termed proline- and glutamine-rich splicing factor, or 100 kDa DNA-pairing protein (POMp100), or 100 kDa subunit of DNA-binding p52/p100 complex), with a long helical C-terminal extension. PSF is a multifunctional protein that mediates diverse activities in the cell. It is ubiquitously expressed and highly conserved in vertebrates. PSF binds not only RNA but also single-stranded DNA (ssDNA) as well as double-stranded DNA (dsDNA) and facilitates the renaturation of complementary ssDNAs. Additionally, it promotes the formation of D-loops in superhelical duplex DNA, and is involved in cell proliferation. PSF can also interact with multiple factors. It is an RNA-binding component of spliceosomes and binds to insulin-like growth factor response element (IGFRE). Moreover, PSF functions as a transcriptional repressor interacting with Sin3A and mediating silencing through the recruitment of histone deacetylases (HDACs) to the DNA binding domain (DBD) of nuclear hormone receptors. As an RNA-binding component of spliceosomes, PSF binds to the insulin-like growth factor response element (IGFRE), and acts as an independent negative regulator of the transcriptional activity of the porcine P-450 cholesterol side-chain cleavage enzyme gene (P450scc) IGFRE. PSF is an essential pre-mRNA splicing factor and is dissociated from PTB and binds to U1-70K and serine-arginine (SR) proteins during apoptosis. In addition, PSF forms a heterodimer with the nuclear protein p54nrb, also known as non-POU domain-containing octamer-binding protein (NONO). The PSF/p54nrb complex displays a variety of functions, such as DNA recombination and RNA synthesis, processing, and transport. PSF contains two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), which are responsible for interactions with RNA and for the localization of the protein in speckles. It also contains an N-terminal region rich in proline, glycine, and glutamine residues, which may play a role in interactions recruiting other molecules. The NOPS domain specifically binds to the second RNA recognition motif (RRM2) domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies
PRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQPGTFEYEYSQRWKSLDEMEKQQREQVEKN
MKEAKEKLESEMEDAYHEHQANLLRQD
>gnl|CDD|240584 cd12949, NOPS_PSPC1, NOPS domain, including C-terminal coiled-coil region, in paraspeckle protein component 1 (PSPC1) and similar proteins. The family contains a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain. This model corresponds to the NOPS domain, with a long helical C-terminal extension, of paraspeckle component 1 (PSPC1, also termed PSP1), a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm. It is ubiquitously expressed and highly conserved in vertebrates. Although its cellular function remains unknown currently, PSPC1 forms a novel heterodimer with the nuclear protein p54nrb, also known as non-POU domain-containing octamer-binding protein (NONO), which localizes to paraspeckles in an RNA-dependent manner. The NOPS domain specifically binds to the second RNA recognition motif (RRM2) domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies
PRPVIVEPMEQFDDEDGLPEKLMQKTQQYHKEREQPPRFAQPGTFEFEYASRWKALDEMEKQQREQVDRN
IREAKEKLEAEMEAARHEHQLMLM
>gnl|CDD|240577 cd12950, RRP7_Rrp7p, RRP7 domain ribosomal RNA-processing protein 7 (Rrp7p) and similar proteins. This CD corresponds to the RRP7 domain of Rrp7p. Rrp7p is encoded by YCL031C gene from Saccharomyces cerevisiae. It is an essential yeast protein involved in pre-rRNA processing and ribosome assembly. Rrp7p contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal RRP7 domain
GLARYRAHYRRLRPPLEALQESVDSFMALFEAREEERKRERKRLRNEPDEDGFVTVVRGGRKGPAAGEEA
GKAAEEEKKEKEKKKKKKKELEDFYRFQLREKKKEEQADLLKKFEEDKERVEKMKEKR
>gnl|CDD|240578 cd12951, RRP7_Rrp7A, RRP7 domain ribosomal RNA-processing protein 7 homolog A (Rrp7A) and similar proteins. The family corresponds to the RRP7 domain of Rrp7A, also termed gastric cancer antigen Zg14, and similar proteins which are yeast ribosomal RNA-processing protein 7 (Rrp7p) homologs mainly found in Metazoans. The cellular function of Rrp7A remains unclear currently. Rrp7A harbors an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal RRP7 domain
GLKKWVEEYNASIPDPAELQSEIDEYMEEYDKEEEEEKEEKEKEAEPDEDGWVTVTKKGRRPKTARKESV
AAKAAEKEKKKKKKKELKNFYRFQIRESKRNELAELRKKFEEDKKRIALLKAARKFKPY
>gnl|CDD|240572 cd12952, MMP_ACEL2062, Minimal MMP-like domain found in Acidothermus cellulolyticus hypothetical protein ACEL2062 and similar protein. The subfamily includes an uncharacterized protein from Acidothermus cellulolyticus (ACEL2062) and its homologs from bacteria. Although its biological role remains unclear, ACEL2062 contains a minimal metalloprotease (MMP)-like domain consisting of 3-stranded mixed 2-beta sheets and a HExxHxxGxxD/S (x could be any amino acid) motif. It may belong to a superfamily of bacterial zinc metallo-peptidases, which is characterized by a conserved HExxHxxGxxD motif
SLEEFEALVEEALDSLPEEFRAALDNVVILVEDFPDDETLEALGIPDPPELLGLYEGVPLTERSVSDSGV
LPDRITLFRRPLLRYCRTREELREEVRHTVLHEIGHHFGLSDDDLHE
>gnl|CDD|240573 cd12953, MMP_TTHA0227, Minimal MMP-like domain found in Thermus thermophilus hypothetical protein TTHA0227 and similar proteins. The subfamily includes an uncharacterized protein from Thermus thermophilus (TTHA0227) and its homologs from bacteria. Although its biological role remains unclear, TTHA0227 contains a minimal metalloprotease (MMP)-like domain consisting of 3-stranded mixed 2-beta sheets and a HExxH (x could be any amino acid) motif. It may belong to a superfamily of bacterial zinc metallo-peptidases, which is characterized by a conserved HExxHxxGxxD motif
DIDEFEELLEEIADEIPEAFFRELNGGIILLPEAKYHPESPNGDLYILGEYVRDILGRQIVIYYGSFAAV
YGDESREDWKEELRETLLHELRHHLESLAGVDDLVDEDAEEL
>gnl|CDD|240574 cd12954, MMP_TTHA0227_like_1, Minimal MMP-like domain found in a group of hypothetical proteins from alphaproteobacteria and actinobacteria. The subfamily includes some uncharacterized bacterial proteins which show high sequence similarity with Thermus thermophilus hypothetical protein TTHA0227. However, they do not contain the conserved HExxH (x could be any amino acid) motif. They may not have any zinc metallo-peptidase activity
TRAERFDDLVAEAVARLAARWPDELAGVEFAVEDVPPSDPAPWEDEPVPLARAFPAGRGTPARIVLYRRP
IERRASSEAELRALVHDVVVEQVAELLGV
>gnl|CDD|214020 cd12955, SKA2, Spindle and kinetochore-associated protein 2. SKA2, also called FAM33A, is a component of the SKA complex, which is formed by the association of three subunits (SKA1, SKA2, annd SKA3). The SKA complex is essential for accurate cell division. It functions with the Ndc80 network to establish stable kinetochore-microtubule interactions, which are crucial for the highly orchestrated chromosome movements during mitosis. The biological unit is a W-shaped homodimer of the three-subunit complex. SKA2 has also been identified as a glucocorticoid receptor-interacting protein and may be involved in regulating cancer cell proliferation
VDKLEAMFQKAESDLDYIQRRLESEFKENSPESAGEKNPVELLERLSAIKSRYSTLCAQAEEIKKAQKES
VSSIRAQLHKAMQLLQELQQTTDTELSPLTEEEKEAAAQLGSHVSA
>gnl|CDD|240562 cd12956, CBM_SusE-F_like, carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins. This group includes five starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins contain an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. CBM-Fa (the CBM unique to SusF), does not bind insoluble starch; CBM-Fb and CBM-Fc both do, deletion of one or the other results in a decrease in the overall affinity of SusF for starch. Both CBM-Eb and CBM-Ec are needed for SusE to bind tightly to starch. CBM-Ec has an additional starch-binding loop that may mediate interactions with partially unwound single helical forms of starch or small starch-breakdown products. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum
TWGIVGSATPNGWDGPPDKPFTYDATDGTFVSYATLAGDGEIKFRPNNDWGENYGDDGDDGTFLSSGGDN
IAVSAGGTYKITLNLNNNTYTIE
>gnl|CDD|240570 cd12957, SKA3_N, Spindle and kinetochore-associated protein 3, N-terminal domain. SKA3, also called RAMA1 or C13orf3, is a component of the SKA complex, which is formed by the association of three subunits (SKA1, SKA2, and SKA3). The SKA complex is essential for accurate cell division. It functions with the Ndc80 network to establish stable kinetochore-microtubule interactions, which are crucial for the highly orchestrated chromosome movements during mitosis. The biological unit is a W-shaped homodimer of the three-subunit complex. SKA3 contributes to SAC (spindle-assembly checkpoint) signaling through its interaction with Bub3. This model represents the N-terminal domain of SKA3, which is involved in interactions with SKA1 and SKA2 to form the SKA complex. The C-terminal portion of SKA3 is involved in creating a microtubule-binding surface
VSRNFFSKLRSLALTLEKETSQLERALSGEETEFEEESPMRVLHDLHSDVRTLKGDANNQLDKARSESQE
LYDFIKACKVLMQRNAEDIDKIREHFQKYG
>gnl|CDD|214021 cd12958, SKA1_N, Spindle and kinetochore-associated protein 1, N-terminal domain. SKA1 is a component of the SKA complex, which is formed by the association of three subunits (SKA1, SKA2, annd SKA3). The SKA complex is essential for accurate cell division. It functions with the Ndc80 network to establish stable kinetochore-microtubule interactions, which are crucial for the highly orchestrated chromosome movements during mitosis. The biological unit is a W-shaped homodimer of the three-subunit complex. This model represents the N-terminal domain of SKA1, which is involved in interactions with SKA2 and SKA3 to form the SKA complex. The C-terminal portion of SKA1 is involved in creating a microtubule-binding surface
SSDLEELCSHINSKISNIKKTLELRNIGQEPSLKTVLKKIGQELIALNELLNELEKEVQKQEELLKSLKE
LQESFEKDLQDAQHLKDNV
>gnl|CDD|214022 cd12959, MMACHC-like, Methylmalonic aciduria and homocystinuria type C protein and similar proteins. MMACHC, also called CblC, is involved in the intracellular processing of vitamin B12 by catalyzing two reactions: the reductive decyanation of cyanocobalamin in the presence of a flavoprotein oxidoreductase and the dealkylation of alkylcobalamins through the nucleophilic displacement of the alkyl group by glutathione. Mutations in MMACHC cause combined methylmalonic acidemia/aciduria and homocystinuria (CblC type), the most common inherited disorder of cobalamin metabolism. The structure of MMACHC reveals it to be the most divergent member of the NADPH-dependent flavin reductase family that can use FMN or FAD to catalyze reductive decyanation; it is also the first enzyme with glutathione transferase (GST) activity that is unrelated to the GST superfamily in structure and sequence
ELIQKLREQLAPNGGFECHPFKVGWYNEVVPPAFKLPYPDDTLAFLVLSTPSMFEKAFLPFLQSDLALED
LKDPLDQCVADTLSAAVEGLPPHEIEIIHDFEMHPNRRPKVLVQTAGHVSGAAYYYQRKDVHNDWWGKKK
IYGVCLHPKYGGWFAFRGVIIFPDVLPPDLPEPEPVDCLTTEEDRIALLELFNYHWRDWRYRDVGPPVER
YSEEQKEYFSTPPRDR
>gnl|CDD|240575 cd12960, Spider_toxin, Spider neurotoxins including agatoxin, purotoxin and ctenitoxin. This domain family contains spider toxins that include the omega-Aga-IVB, a P-type calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta, as well as purotoxin-1 (PT1), a spider peptide venom of the Central Asian spider Geolycosa sp., which specifically exerts inhibitory action on P2X3 purinoreceptors at nanomolar concentrations. These spider toxins, which are ion channel blockers, share a common structural motif composed of a triple-stranded antiparallel beta-sheet, stabilized by internal disulfide bonds known as cystine knots
SCAELYGKCDKGPTPCCEGRPCKCNLWGTNCKCKKK
>gnl|CDD|240569 cd12961, CBM58_SusG, Carbohydrate-binding module 58 from Bacteroides thetaiotaomicron SusG and similar CBMs. This group includes the starch-specific CBM (carbohydrate-binding module) of SusG, a cell surface lipoprotein within the Sus (Starch-utilization system) system of the Human gut symbiont Bacteroides thetaiotaomicron. It represents the CBM58 class of CBMs in the carbohydrate active enzymes (CAZy) database. SusG is an alpha-amylase, and is essential for growth on high molecular weight starch. SusG-CBM58 binds maltooligosaccharide distal to, and on the opposite side of, the amylase catalytic site; it is one of two starch-binding sites in SusG, the other being adjacent to the active site. SusG-CBM58 is required for efficient degradation of insoluble starch by the purified enzyme. Its starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. It may play a role in product exchange with other Sus components
LKFTLDWSNAPSPTVTVTTGTKADADNPDTGTDNAKYLYFGEGICKKFYDKGNNIYELTVDFESTWGFLI
RTSNASFWPAGTKYGASSSSEKLALGKDFTLTNAGNPANI
>gnl|CDD|240568 cd12962, X25_BaPul_like, X25 domain of Bacillus acidopullulyticus pullulanase and similar proteins. Pullulanase (EC 3.2.1.41) cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. BaPul is used industrially in the production of high fructose corn syrup, high maltose content syrups and low calorie and ''light'' beers. Pullulanases, in addition to the catalytic domain, include several carbohydrate-binding domains (CBMs) as well as domains of unknown function (termed ''X'' modules). X25 was identified in Bacillus acidopullulyticus pullulanase, and splits another domain of unknown function (X45). X25 is present in multiple copy in some pullulanases. It has been suggested that X25 and X45 are CBMs which target mixed alpha-1,6/alpha-1,4 linked D-glucan polysaccharides
SVTLVGSFQSELGCAGDWDPDCLATQLTDDGNDGVYTFTTTLPAGDYEYKVALNGSWDENYGAGGAPDGA
NIPLTLPAGAEVTFTYDPATHEVTD
>gnl|CDD|240567 cd12963, X45_BaPul_like, X45 domain of Bacillus acidopullulyticus pullulanase and similar proteins. Pullulanase (EC 3.2.1.41) cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. BaPul is used industrially in the production of high fructose corn syrup, high maltose content syrups and low calorie and ''light'' beers. Pullulanases, in addition to the catalytic domain, include several carbohydrate-binding domains (CBMs) as well as domains of unknown function (termed ''X'' modules). X45 was identified in Bacillus acidopullulyticus pullulanase, it is interupted by another domain of unknown function (X25). It has been suggested that X25 and X45 are CBMs which target mixed alpha-1,6/alpha-1,4 linked D-glucan polysaccharides
PKVSNAYLDNEKTVLAKLTNPMTLSDGSSGFTVTDKTTGEQIPVTAATNANSASSSEQTDLVQLTLASAP
DVSHTIQVGAAGYEAVNLI
>gnl|CDD|240563 cd12964, CBM-Fa, carbohydrate-binding module Fa from Bacteroides thetaiotaomicron SusE, and similar CBMs. CBM-Fa is the first of three starch-specific CBM (carbohydrate-binding modules) of SusF, a cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. The precise mechanistic role of SusF in starch metabolism is unclear. SusF has an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by three tandem starch-binding CBMs: CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus. These CBMs have no enzymatic activity. Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These three CBMs show differences in their affinity for various different starch oligosaccharides, and they contribute differently to binding insoluble starch. CBM-Fa does not bind insoluble starch, and can bind smaller maltooligosaccharides. Proteins in this subgroup are present in the species of the Gram-negative Bacteroidetes phylum
AYYLVGDINGWDANNPIKFNHSGKDVYDDPVFTETLTTTASDQYFKIIPASNIDAANDWDEALGASAVDG
DDSAEGFLAWTGSFGVGAGKIAGAGKYKITLNMMDYTYTV
>gnl|CDD|240564 cd12965, CBM-Eb_CBM-Fb, carbohydrate-binding modules Eb and Fb from SusE and SusF, respectively, and similar CBMs. Included in this subgroup are CBM-Eb and CBM-Fb, starch-specific carbohydrate-binding modules of SusE and SusF, cell surface lipoproteins within the Sus (Starch-utilization system)system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins have an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they contribute differently to binding insoluble starch. CBM-Fb and CBM-Fc both bind insoluble starch, deletion of one or the other results in a decrease in the overall affinity of SusF for starch. Both CBM-Eb and CBM-Ec are needed for SusE to bind tightly to starch. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum
ELYMTGSFFGNWNWDGWKEMTPVNGGDGEFWSIVYFDAGAGFKFNTSKAWDGDFGGFDATIAGEAGAGVS
DGGNIVVANAGWYLVYVTADVYKYTVIF
>gnl|CDD|240565 cd12966, CBM-Ec_CBM-Fc, carbohydrate-binding modules Ec and Fc from SusE and SusF, respectively, and similar CBMs. Included in this subgroup are CBM-Ec and CBM-Fc, starch-specific carbohydrate-binding modules of SusE and SusF, cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins have an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they contribute differently to binding insoluble starch. CBM-Fb and CBM-Fc both bind insoluble starch, deletion of one or the other results in a decrease in the overall affinity of SusF for starch. Both CBM-Eb and CBM-Ec are needed for SusE to bind tightly to starch. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum
PEVYLIGNTVGGGWDENDENLFTVPATADGEFVSPAFAAGGEVRMCVKVPGFDWWRSEFTVFDGKIFYRG
NGGGDQYRVTVKAGQKVYLNFTTGTGSI
>gnl|CDD|240566 cd12967, CBM_SusE-F_like_u1, Uncharacterized subgroup of the CBM-SusE-F_like superfamily. The CBM SusE-F_like superfamily includes starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins have an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum
YLYVPGNYQGWNPATAPALYSPNGDGKYEGYVYLPGNFEFKFTTAPNWDGDYGGDGGGGGLLDGGGGNIK
APEAGYYKVTVDLNDLTYSLT
>gnl|CDD|240556 cd13112, POLO_box, Polo-box domain (PBD), a C-terminal tandemly repeated region of polo-like kinases. The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides
PTLKVWYFTKYGIGQLLSTGSVEILFNDGTKLILSPDGSSLKYYDPDGQLTRYYLSELPSELRSKLEYLN
TFVTHV
>gnl|CDD|381706 cd13113, Wnt, Wnt domain found in the WNT signaling gene family, also called Wingless-type mouse mammary tumor virus (MMTV) integration site family. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about the structure of Wnt proteins, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. Wnt signaling mediated by Wnt proteins orchestrates and influences a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
LMESIAEGAQLALKECQRQFANRRWNCSTFNEPLLFGKILKRGTRETAFVHAITSAGVTHAITRACSRGK
LKNCGCDRTRQGPEGQGDWTWGGCSDNIKFGIKFSRKFLDAREKKKGSDARSLMNLHNNEAGRKAVKKTM
KKKCKCHGVSGSCTTKTCWRQLPSFREIGDYLKEKYDNAVKVKLNNNGSGLRLVPKRSRFRSPTETDLVY
LEESPDYCEPNPTLGSLGTAGRECNPTSPGPDSCELLCCGRGYRTETEIVTEKCNCKFVWCCEVKCETCR
RTVERYTC
>gnl|CDD|240557 cd13114, POLO_box_Plk4_1, First (cryptic) polo-box domain (PBD) of polo-like kinase 4 (Plk4/Sak). The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides
LRSRVPPLNTSRLRPIRQKTKNAVVSILEDGEVCLEFLKGKGREERVVEVLRISSDGQKIVIYQPNGGKG
VPLEPPPLPPPGADATYSYESLPEKYWKKYQYAARFVQLVKS
>gnl|CDD|240558 cd13115, POLO_box_Plk4_2, Second (cryptic) polo-box domain (PBD) of polo-like kinase 4 (Plk4/Sak). The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides
KTPKVTLYTDKAKCMLMENGPPADFEACFYDGAKVHKTSGGIKIIDKSGKSYTLKESDLSSLSPELRKLL
DHFNECRQHCLRLESALSSLESSSGSNSCFPVIIGRRP
>gnl|CDD|240559 cd13116, POLO_box_Plk4_3, C-terminal (third) polo-box domain (PBD) of polo-like kinase 4 (Plk4/Sak). The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides
SSNVLKKVFVPGVGWASQLSSGEIWVQYNDGSQLTVSPNRSSTITYTSSDGTVTRYNQSDSLPEHVREKL
SHLPMVIKLLV
>gnl|CDD|240560 cd13117, POLO_box_2, Second polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5. The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides
PFVKKWLRTKSAIVFRLSNGTVQVNFFDHTKIILSPLGKLVTYIDKKRESRTYPLSELLKSGCSSELAKR
LKYAKEILKEL
>gnl|CDD|240561 cd13118, POLO_box_1, First polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5. The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides
PPVWVSKWVDYSNKYGLGYQLSDGSVGVLFNDSTKMVLSPDGKHVQYIERNGEESELTRSDDSYPPDLAK
KVTLLKYFRNYMEEHLSKGGD
>gnl|CDD|240524 cd13119, BF2867_like, Tandemly repeated domain found in Bacteroides fragilis Nctc 9343 BF2867 and related proteins. Two structurally similar domains with low sequence similarity form a protein that may have a role in cell adhesion. This family also includes BF1858 and overlaps with DUF3988
IRIVLTIYAGEIKDGVIFLLXSGTIGLKVSQDEPEFTVNGEAGATKNALETYSYAYTVATGGSGGVSSTA
STPLYPQGLGEFYLSILYPYKAGNNEDTYAADXTGGNLTSGHAYT
>gnl|CDD|240525 cd13120, BF2867_like_N, N-terminal domain found in Bacteroides fragilis Nctc 9343 BF2867 and related proteins. Two structurally similar domains with low sequence similarity in a tandem repeat arrangement form a protein that may have a role in cell adhesion. This family overlaps with DUF3988
LAAALLLAACSQDEEIESPPGEGGIIISVATTTTTTTTRATTTTFETGDAIGVFAYGDGGAAGTTYTDNV
KYTTTSGGGTWTPSDTTIYWPGGEKVTFYAYYPYQAGATTATDSTTAPTTTDQSTQDNATQSDLLYATGA
TATTSGNGTVSLTFKH
>gnl|CDD|240526 cd13121, BF2867_like_C, C-terminal domain found in Bacteroides fragilisNctc 9343 BF2867 and related proteins. Two structurally similar domains with low sequence similarity in a tandem repeat arrangement form a protein that may have a role in cell adhesion. This family overlaps with DUF3988
SKLVFTIKAGDDGVTLTDVKGTVTLSGLKTTGTFNLATGTVTATTGTTTITTTLADTTTTAAGGTTYEAI
LLPQTLAGATLTLTVTLDDGKTYTYTLPDPNTTLEAGKSYTYTLTLKKTGLTVSGVTIEDWTTGGEGD
>gnl|CDD|240555 cd13122, MSL2_CXC, DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins. The CXC domain of Drosophila melanogaster MSL2 forms a Zn(3)Cys(9) cluster and is involved in recruiting members of the dosage compensation complex (DCC) to sites on the X chromosome
PPEKKGCRCGTATQSPGVLTCRGQRCPCYSNGKSCLDCKCRGCKNPHKAD
>gnl|CDD|240528 cd13123, MATE_MurJ_like, MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins. Escherichia coli MurJ (MviN) has been identified as essential for murein biosynthesis. It has been suggested that MurJ functions as the peptidoglycan lipid II flippase which is involved in translocation of lipid-anchored peptidoglycan precursors across the cytoplasmic membrane, though results obtained in Bacillus subtilis seem to indicate that its MurJ homologs are not essential for growth. Some MviN family members (e.g. in Mycobacterium tuberculosis) possess an extended C-terminal region that contains an intracellular pseudo-kinase domain and an extracellular domain resembling carbohydrate-binding proteins. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR)
AIGTLLSRILGFVRDVLIAAAFGAGPLADAFFVAFRIPNLLRRLFAEGALSAAFVPVFSEYLEKEGEEEA
RRFASRVLTLLLLVLLLLTLLGILFAPLLVKLLAPGFSGDKFELAVALTRIMFPYLLFISLSALLGGILN
AHGRFFAPALAPVLLNLVIIAGLLLLAPLFDLGIYALAWGVLLGGVLQLLVQLPALRRLGFRFRPRLDFR
DPGVRRVLKLMLPALLGVSVSQINLLVDTILASFLPEGSISALYYADRLYQLPLGIFGVAIATALLPRLS
RLAAAGDLDEFRRTLSRGLRLVLFLLLPAAVGLIVLAEPIVRLLFERGAFTAEDTLMTASALAAYALGLP
AFALVKLLSRAFYALKDTKTPVKIAVIAVAVNILLNLLLIKPLGHVGLALATSLSAWVNALLLLVLLRRR
>gnl|CDD|240529 cd13124, MATE_SpoVB_like, Stage V sporulation protein B, also known as Stage III sporulation protein F, and related proteins. The integral membrane protein SpoVB has been implicated in the biosynthesis of the peptidoglycan component of the spore cortex in Bacillus subtilis. This model represents a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR)
LILTIAGLISKILGAIYRIPLQNIIGDEGMGLYQMAYPIYGIFLTLATAGIPVAISKLVAEYNALGDYKG
ARRIFRVSLILLLILGLVFFLLLFFGAPFLAQLLLGDPRLAPVIRALAPAILIVPLLSVLRGYFQGLQNM
TPTAVSQVIEQIVRVIVILVLAYLLLPVGGGLYYAAAGATFGAVIGALAGLLVLLYYYRKKRRELKRLLR
KSPRSKISTKEILKELLSYAIPITLSSLILPLLQLIDSFTVPRRLQAAGLSESEATALYGILTGRAQPLV
QLPTVIATALSTSLVPAISEAYAKGDKKELRRRINQALRLTLLIGLPAAVGLAVLAEPINTLLFGDSEGG
LILQILAPSILFLSLQQVTAAILQGLGKVKIPVINLLIGLLVKIVLNYVLIPIFGIYGAAIATVIGFLVA
ALLNLRALKKLLGF
>gnl|CDD|240530 cd13125, MATE_like_10, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. This family might function as a translocase for lipopolysaccharides, such as O-antigen. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
KVSSLSGISTLIKILAGLIINKVVAVYLGPSGVALLGQLQNFVTILQTIAGGGINNGVVKYTAEYKDDEE
KLARVWSTAFRITLILSILGGLLLLLFSKPLSSLLFGDIDYSWVFILLGLALPLFALNNLLLAILNGLKE
IKRYALINIISSLIGLLVSVLLVYFYGLKGALLALVLNQSLIFLVTLIYSRKQPWFKLKYLWGRLDKDII
KKLLKFSLMALVSALSLPLSQIIVRNILIRQLGWEAAGYWQAVWKISDVYLGFITTALSTYYLPRLSAIK
DNKELKREVNKQLKVILPLVAIGALLIYLLRDLIIQILFSEEFLPARELFLWQLIGDFFKIASWLLGYIL
LAKGMTKLFIITEILFALLFVLLSLLFIPLFGLEGAGIAYAINYILYLILMYFIFRKLL
>gnl|CDD|240531 cd13126, MATE_like_11, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. This family might function as a translocase for lipopolysaccharides, such as O-antigen. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
ALWTLADQALSSLTNFALGVLVARSLGPEAFGAFSLAFTVFGVAVGVSRALVTAPLGIRYSAVDAAAFRR
AVRKATGTALAVGLALGLVTALVGALLGGTVGSPLVALGVVLPGLLLQDAWRGAFFAQGRPGRAAANDLV
WAVAQLAGAMLIVALVSGVAAALLAWGASAVVAALLGRAQAGLWPRPRGALAWLREHRDLTGYLLAEFVL
GQGAAQNSDLLLGALGSLAAVGALRGAQTLLGPLTILAAGLVTAAVPELARRKDMSPRRRRRAALVLSGV
VAAAALVWGLALLLLPDLIGEALLGDVWAGAQALLLPLILAQAGAALAVGPAAYLLALGRAKGTLRVNLV
GAPQLLGLGLTGALLGGAVGAAWGLALALLLGLPVWWLLLRRALRE
>gnl|CDD|240532 cd13127, MATE_tuaB_like, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. This family might function as a translocase for lipopolysaccharides and participate in the biosynthesis of cell wall components such as teichuronic acid. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
AVSGAFWSAISQVVVQLLQFVVTIILARLLTPEDFGLVAMATVFIAFAQLFSDLGLSSALIQRKDLTEED
LSTVFWLNLLLGLLLYLLLFLLAPLIAAFYNEPELIPLLRVLSLSFLLSGLGSVPRALLQRELRFKKLAI
IELISTLVSGVVAIVLALLGFGVWALVAQQLVGALVSTVLLWILSRWRPRLSFSLASLKELLSFGSKLLG
SNLLNYFSRNLDNLIIGKFLGAAALGYYSRAYRLALLPVQNITGPITRVLFPALSRLQDDPERLRRAYLK
ALRLLALITFPLMVGLALLAEPLVLLLLGEKWLPAVPILQILALAGLFQPLSSLNGSLLLALGRTDLLLK
LGLIKAVLTVLALLIGIPYGIIGVAIAYVIASLLSFPLNLYLAGRLIGISLLELLR
>gnl|CDD|240533 cd13128, MATE_Wzx_like, Wzx, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins. Escherichia coli Wzx and related proteins from other gram-negative bacteria are thought to act as flippases, assisting in the membrane translocation of lipopolysaccharides including those containing O-antigens. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR)
LAKNSGWLFVGNIISKLLGFLVRVYLARYLGPEGFGILSLALAFVGLFSIFADLGLPTALVREIARYRKE
KIREIISTSLVLKLILGILALLLLFLFAFLIAFYDPELVLLLYILALSLPFSALNSLFRGIFQGFEKMKY
IVIARIIESVLSLILALILVLLGGGLIGFALAYLIASVLSAILLLYIYRKKILLPKFFSFDLKLAKELLR
FSIPLALSGIFSLIYTRIDTIMLGYFLGDAAVGIYNAAYRIAELLLFIPSAISTALFPRISELYKNDKDE
LKKLLKKSFKYLFLISLPIAIGLFLFAEPIITLLFGEEYLPAALVLQILAWGFLFIFLNGIFGSILQAIG
KQKLTLKILLIGALLNVILNLLLIPKYGIIGAAIATLISEFIIFILLLYLLK
>gnl|CDD|240534 cd13129, MATE_epsE_like, Multidrug and toxic compound extrusion family and similar proteins. This model represents a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins, including Ralstonia solanaceraum GMI1000 epsE, which may be involved in exporting exopolysaccharide EPS I, a virulence factor. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR)
SFASGSFWSLGGLVASRGAVFLTNIMVARSLGKHVFGEFGVIQVTIGLLGTFAGFGLGLAATKVIAETKD
VDPERAGRIIGLSILLAVVTGALAATVLFLSATWIAIATLNAPHLAELLRIAAIILILTAFTGAQTGFLS
GFEAFRAIARVNIWAGLLLLPLMWIGVYIRGLVGAVVILLASAAGNVASNSLILRRECQNQRGPVRTGLT
WQELRVLFKFSLPSVLSGSMGSPVHWIALAILVNQPNGYAELGLFNAANQWRQFITFLPATLGNVALPFL
AENFGNNEGMFRQTFRSALLFGLGLSLPLGCVFILASQIFAWLYGKEYGSAAASMRSLAVAAILVGLSVL
LGQIIASSGKIWRGFALNMVWSVIYVAAAYLLLRLYGAPGLALAMSAAYCVLIIFQTLTLQ
>gnl|CDD|240535 cd13130, MATE_rft1, Rft1-like subfamily of the multidrug and toxic compound extrusion family (MATE). This eukaryotic family may function as a transporter, shuttling phospholipids, lipopolysaccharides or oligosaccharides from cytoplasmic to the lumenal side of the endoplasmic reticulum. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. MATE has also been identified as a large multigene family in plants, where the proteins are linked to disease resistance
SSSRGFKYLIAAQLFSRIITFVFNQLLLRFLTPRYFGYSIQFELFQTTVLFLSREGFRRACLRINSSGAG
ITTESNKSGELQAKVLKIAWAIVPGGIISTILGCLVVLWASESLSYSPPYAKAILIYGFACILELLSEPL
YILSQNLLKFRLRAIVETAATLVRCLTTFILIVLGTGKEPKVLVFALGQLAYGVCLFFGYWYYFLQCFVS
KKSSLFPLRNSNLMFFDKPTLRMCGLFTIQSFFKHLLTEGDKIVLVWFDTPYNQGVYALVDNYGSLVVRI
VFLPFEESSYTTFARLASEKNPKALKKLGNSLTEALKLYSYVGLVAIAFGPSYSYSLLRLLYGERWSDGE
APDALGVYCLYIPFLALNGTSEAFLHSVATEEQLQRQNVWLLVFSVIYLILNVLLIRWFSLGAVGLILAN
ILNMLLRIGYSLVFIKHYFKG
>gnl|CDD|240536 cd13131, MATE_NorM_like, Subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins similar to Vibrio cholerae NorM. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. This subfamily includes Vibrio cholerae NorM and functions most likely as a multidrug efflux pump, removing xenobiotics from the interior of the cell. The pump utilizes a cation gradient across the membrane to facilitate the export process. NorM appears to bind monovalent cations in an outward-facing conformation and may subsequently cycle through an inward-facing and outward-facing conformation to capture and release its substrate
ELRALLRLALPILIAQLAQMAMGFVDTVMAGRLGADDLAAVALGSSLWFPVFTFGMGLLLAVTPLVAQAH
GAGDRRRIRRAVRQGLWLALLLSLPLMLLLWLAPPILPLMGQEPEVAAIARGYLLALAWGIPPALLFQVL
RSFLDALGRTRPAMVITLLALVLNIPLNYVLIFGKFGLPALGGAGAGLATAIVYWLMFLALAFYIRRHKR
FRRYRLFARFWRPDWARLKELLRLGLPIGLTIFFEVSLFAAVALLMGRLGTTVLAAHQIALNFASLLFMV
PLGISMAATVRVGFALGAGDPADARRAGLVGLGLGVGFAALTALLLLLFPEQIAGLYTNDPAVIALAASL
LVFAALFQLFDGIQVVAAGALRGYKDTRVPFLLALISYWGIGLPLGYLLAFTTGLGAFGVWIGLIIGLAL
AAILLLWRFRRLQRR
>gnl|CDD|240537 cd13132, MATE_eukaryotic, Eukaryotic members of the multidrug and toxic compound extrusion (MATE) family. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. MATE has also been identified as a large multigene family in plants, where the proteins are linked to disease resistance. A number of family members are involved in the synthesis of peptidoglycan components in bacteria. This subfamily, which is restricted to eukaryotes, contains vertebrate solute transporters responsible for secretion of cationic drugs across the brush border membranes, yeast proteins located in the vacuole membrane, and plant proteins involved in disease resistance and iron homeostatis under osmotic stress
EAKKLLRLAAPLVLTSLLQYSLSVVSVVFVGHLGKLELAAASLASSFANVTGFSILLGLASALDTLCGQA
FGAKNYKLVGVYLQRALVILLLCCVPISLLWLNTEPILLLLGQDPEIARLAGEYLRWLIPGLFAYALFEP
LKRYLQAQGIVLPLVYISLVALLLNILLNYLLVFVLGLGFIGAALATSISYWLIVVLLLLYIFFSKGHKA
TWGGFSREAFRGWGPFLKLAIPSALMLCLEWWAFEILVLLAGLLPGTVALAAQSICLTTTSLLYMIPLGI
SIAASVRVGNELGAGNPKRAKLAAIVALILSLVIGVVVAILLLVLRDVWAYLFTSDEEVIALVADLLPIL
ALFQIFDGLQAVLSGVLRGCGRQKLGAYVNLVAYYLIGLPVGLLLAFVLGLGLKGLWIGLIAGLILQAVI
LLLIILRTDWDKEAEK
>gnl|CDD|240538 cd13133, MATE_like_7, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
PGGYREILKIALPLVLSMLSQTVMGFTDRAFLGRLSEVALAASGPAGVLYFAILMLFFGLSSGVQVFVAQ
YNGAGRYSRIGRVLWQGLYFSLLLAPLLALLSALAAPLLFLLLGHSPEVQALEVEYFRIRILGAPFSLLG
AALRAFFSGIGRTRVVMVANLVMVVVNIVLDYALIFGKLGFPAMGIAGAAIATVIAEAVSLLFFLLLLFR
RKNRRRFGLRRAWRFDRELLRRILRLGLPSGLQFFLDVGAFTVFFLLIGRLGTTELAATNIVFSINSLAF
LPMIGLGIAVSSLVGQALGAGRPDLAMRVTRRGLKLALAYMLLLGILFLLFPELLLSIFTPGADFALIAE
LAVPLLRFVAAYILFDALALVFAGALRGAGDTRFVMLAELIVAWLYLLPPAYLLVVLGAGLAGAWTVETV
YVIVLALIFLLRFRSGKW
>gnl|CDD|240539 cd13134, MATE_like_8, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
FKLSLFALAWPIFIELLLQMLLGTIDTFMLSRYSDNAVAAVGVANQILFLLILIFSFISTGTSILIAQYL
GAKDKKKARQIAGVALLFNLLLGLVFSLLLLFFGAELLRLMGLPPELLALGSTYLRIVGGSLFLQALSLT
LSAILRSHGRTKIPMYVSLIMNILNIVGNYLLIFGWFGLPKLGVAGVAISTVISRAVGLVLLFILLFRKL
KIRFRLKDLRPFPKKLLKKILKIGLPSAGEELSYNLSQTVITAFIARLGTAALAARTYASNISMFVFLFS
LAIGQATQIIVGHLVGAGDFDEAYKRVLKSLKIGLLVSLAVALLLALFREPILGLFTDDPEIIALGKTLL
LISILLEPGRAFNIVLIGSLRAAGDARFPVLIGIISMWGISVPLAYLLGIVLGLGLLGVWIAFAADEWVR
GIIMLWRWRSGKWIKKAL
>gnl|CDD|240540 cd13135, MATE_like_9, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
KKINHIAIPLILQNLVSQLQMLVDRAFLGRISIRYYSAVGNVTTPFNTITGFLGSISIGFTILGSQSVGA
KDIKRINDYAISSIVYNSIIGVILFLLWLFGARIIFVLFGVDGQILGYSINYVRIFSIYLLLLGILFTFS
SILQGIGETKPIMYGGIIKNLLNVILDYVLIFGNFGFPRLGIIGAAIATTIANVLNLIILVYLCRKIKKL
TFKLSNTKVLKANIRPYKFTIKLGLPLGGEEFLWNIGNLAVIRILNRIGELALGIYTLVFGIENIVLMPM
YGYSSAALTLVGESIGKKDLKEALRIGNICLGLGLLIYIAAAIVFLAFPYKILSLFTNDPELINYSIPYL
IFIIIILFFKSINIVYGFAIRAIGDTKWMLYTQIIGTIIVVSVALLLIFVFKLGLAGVYITLFIDEIIRA
IINFLKYRK
>gnl|CDD|240541 cd13136, MATE_DinF_like, DinF and similar proteins, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins. Escherichia coli DinF is a membrane protein that has been found to protect cells against oxidative stress and bile salts. The expression of DinF is regulated as part of the SOS system. It may act by detoxifying oxidizing molecules that have the potential to damage DNA. Some member of this family have been reported to enhance the virulence of plant pathogenic bacteria by enhancing their ability to grow in the presence of toxic compounds. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR)
LHREILALALPAILSNITVPLLGLVDTAVVGHLGSAAYLGAVALGTTIFNTLFWLFGFLRMGTTGLVAQA
LGAGDREEAIALLVRALLLALAIGLLLILLQSPLLALALLLLGASAAVAALARQYLRIRILGAPAVLLNY
VATGWFRGLQDTRTPLILQIVGNVVNIVLDPLFVFGLGWGVAGAALATVIAQYLGALLGLWLLRRRVRLL
GKSLSRRLPSKAALKRLFKLNRDIFIRTLALLAAFLFFTALAARLGDVILAANQILLQFWLLSSYFLDGF
AYAAEALVGRALGAGDRKAARRVARRLLQWGLGLGVLLALLFFLGGEPIIRLFTDDPAVLALAATYLPWL
ALLPPIGALAFVLDGIFIGATDTRYLRNSMLVSLAVFLPLLFLLVPLWGNHGLWLALILFMLLRGLTLAL
RLPR
>gnl|CDD|240542 cd13137, MATE_NorM_like, Subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins similar to Thermotoga marina NorM. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
RRIWSLAWPVILENLLQTLVGLVDVFMVGRLGAEAIAAVGLATQVLWLLLVLNMALGTGTVALVSQSYGA
GDYERARRALGQSLLLALLLSLPLALLGLLFAEPLLRLLGADPEVIALALTYLRIVLLGIPFFFLSLVGN
AALRGAGDTKTPMYIMIIVNVLNIVLDYVLIFGLWGFPGLGVAGAALATVISRVVGALLLLFLLLRGRLP
IKISFKGFRLDRKIIKKLLRIGLPAGLEQLLRSLGFLVLLAIVASYGTAALAAYQIGLRIESLAFMPGFG
FSMAASTLVGQNLGAGDPDEARRYGKRALRLGVLFMGLLGLLLFIFAPPLASLFTPDPEVIELGVLYLRI
VALSQPFLAISFVLSGALRGAGDTRPPLIINLISMWLVRLPLAYLLGFVLGLGLTGIWLAMFVDTIVRAI
LLLYRFRKGKWK
>gnl|CDD|240543 cd13138, MATE_yoeA_like, Subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins similar to Bacillus subtilis yoeA. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
ILKTLLLFALPLLLSNLLQQLYNLVDLLIVGQFLGVAALAAVSNGSPIIFLLTAIGMGLSMGGTILISQY
IGAKDEEKAKKAVGTLLVLFLILGIVLTILGLLFAPPILRLMNTPAEILELAVSYLRICFLGIPFIFGYN
AYSAILRGLGDSKTPLYFVIIACVLNIILDLLFIAVFHMGVAGAALATVIAQAISVLLALYYLRKKKLPF
KLSLKDFRFDKEILKEILKIGLPSALQQSLVSISFLIINSIVNSYGVVASAAYGIANKINSFAFLPPSAI
GQAVSTFVAQNIGAGKIERAKKGLRTGIIISLIIGLIIILLVFFFAPQLLGLFTSDPEVIEIGAEYLRIY
SIDYILFGILFVFNGLFRGLGKTKFPMIISILRLWLVRIPLAYLLSRLTGLGLFGIWLAMPISNILSAII
CIIYYRKGRWK
>gnl|CDD|240544 cd13139, MATE_like_14, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
SGKEQDFTSGSLNRAIFLLAIPMVLEMVMESLFAVVDLYFVSRLGALAIATVGLTESVLTIVYSIAIGLS
MAATALVARRIGEKDPEGAGFAAVQAILLGVALSLILSILGYFFAEDILSLMGASPAVIAEGYGYTRIMF
GGNGFIMLLFLINGIFRGAGDAAIAMRSLWLANGLNIILDPLFIFGLGPIPAMGVTGAAIATTIGRSIGV
LYQLYHLFKGKGRIQIRRRHLKLDWAIIKKIIKIAVGGILQFLIASSSWIFLVRIIAEFGSTALAGYTIA
IRIIMFALLPAWGLSNAAATLVGQNLGAGQPDRAEKSVWRAGKYNMVFLGIVSLVFFLFAEPLVSFFTTD
PEVIAIAVEALRIISLGYIFYGYGMVLSQAFNGAGDTKTPTLINLVGFWLFQIPLAYLLARHLNLGPKGV
FIAIPIAETVLAIAAIILFRRGKWKTVK
>gnl|CDD|240545 cd13140, MATE_like_1, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. MATE has also been identified as a large multigene family in plants, where the proteins are linked to disease resistance. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
GPILKTLLRLALPIMGTSFIQMAYNLTDMFWVGRLGSDAVAAVGTAGFFVWLAYALALLSKIGAQVKVSQ
SIGAKDEKEARKYARNALQLNLLLGILYGLLLLLFAKPLIGFFNLGDAEVISLAITYLRIVALGLIFSFL
NPVFTGIFNALGDSKTPFIINAIGLVLNIILDPLLIFGFGPFPALGVAGAALATVLAQAIVFLLFLYALK
KKKGLFLKIRILKRPDRKYIKEILKLGLPVALQSILFALISMILARIIASFGPVAIAAQKVGSQIESISW
MTAEGFSTALAAFVGQNYGAGKYDRIRKGYKTALKIASAIGLFATLLLFFFGEPLFSLFIPDPETIAIGV
DYLRILGFSQLFMCLEITTTGAFNGLGRTKPPAIISIVFNGLRIPLALLLSPTGLGLNGIWWAISISSIL
KGIILTIWFLLYKKK
>gnl|CDD|240546 cd13141, MATE_like_13, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
MKDLTQGSIPKHIISMALPIAIGMIIQTLYFLVDLYFVGQLGDAALAGVSLAGNVMFFVMALTQVLNVGT
AALVSHAVGRKDQGEANAVFNQSLLLAAVLGLVVLVLGYLFGRLYLETLAADAATVEAATTYLYWFIPSL
ALQFILTVLGAALRGTGIVKPFMVIQILAVLLNIILAPILITGWGTGRALGVAGAGLASSISVAIAVVLL
LYYFLRLEKYLRLDLALWRPDLPTWKRLLKIGLPSGGEFLLTFVYMAVIYWALRPFGAAAQAGFGIGSRI
MQSLFLPAMAIAFAAPAIAGQNFGAGNYDRVRETFRITAILTTALMLVLTLLCQLVPELLVTPFSDDAAV
IAVAATFLRYVSWNFVAAGLVFTCSGMFQALGNTWPSLLSSASRLLTFALPVIWLSAQPDFRIEQIWYLS
VATTILQAALSLLLLRRELKKRL
>gnl|CDD|240547 cd13142, MATE_like_12, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
RENILEGSILRTLLKLAWPIIVSNLLQVAYNLADTFWLGRLGADAVAAPSISWPLIFLFISLGGGLTVAG
TALVAQYTGAGDYDKANKVAGQTFSFVIILSLILAVLGYILSRPLLLLLIGAPEEVYPLALAYLRIIFLG
LPFMFIFFVFNSLLRGIGDTKTPMKIMFGSVLLNVILDPLLIFGIGPFPGLGVAGAALATVISRGIAAVI
GLYLLFKGRVGLKISLRDLKPDWEWLKKIFRIGLPSSIEQSARALGFTVMTALVAGFGTVVVAAYGIGNR
IISLVFLPAFGLARATSTMVGQNLGAGQIDRAEEIVKKAALLIFLILVIGGVLAFLFAEPIVRVFINDPE
VIKEGADFLRIVAPSFPFFGLFQVINGAFRGSGHTLTAMIISILRLWVIRIPLAYLLAYVLGLGVTGIWI
AMAISNIVAALIALAWFKRGTWKK
>gnl|CDD|240548 cd13143, MATE_MepA_like, Subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins similar to Streptococcus aureus MepA. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. This subfamily includes Streptococcus aureus MepA and Vibrio vulnificus VmrA and functions most likely as a multidrug efflux pump
PIGKLFLKFALPAIIGMLVNGLYNIVDGIFVGHGVGALALAAVNLVFPIIMLLMALGLMIGVGGASLISR
RLGAGDREKANRIFSTALLLSLILGLLLTILGLLFLDPLLRLLGASGELLPYAVDYLRIILLGAPFTILS
SVLNNLLRAEGKPKLAMLGMLIGAVLNIILDPLFIFVLGLGIAGAALATVIAQLISLLLLLLYFFRGKSL
LKLSLLRFKLSLKIIKEILALGFPSFLMQLSSSVVTIVLNLTLLGYGGDIGVAAFGIVTRILTFLFLPLI
GLSQGLQPIIGYNYGAGNYDRVKQALKLALIVALIYGLVLFLILLLFPEQIVSLFTDDPELIALAARILR
IFLLAFPLAGINIVLSGYFQAIGKAKRAALLSLLRQGLFLIPLLLILPRLFGLDGIWLAFPLAEILTLLL
ALILLK
>gnl|CDD|240549 cd13144, MATE_like_4, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
MGSGPVLRLLLTMSIPAMISMLFQALYNIVDSIFVARLGENALTAVSLAFPIQNLMIAVAVGTGVGVNAL
LSRSLGEKDQKEANKAANNGLLLALLSYLLFLLLGLFGVKPFFRLFTDDPEILEYGYAYLSWCVIFSFGM
FFQILCEKVLQSTGNTITPMIAQLIGAIINIILDPILIFGLFGFPAMGIAGAAIATVIGQILAMFLAFFF
LLRKNKDVQPDLRLFRPSLRIIKEIYAVGLPSIIMQAISSVMVFGLNKILAGFGPTAVAVFGIYFKLQSF
VFMPVFGLNNGLIPIVAYNYGAGNKDRIREAIKYAILIAVVIMLAGGLLFQLFPDQLLGLFNASEEMLAI
GVPALRIISLSFLFAALSIILSGLFQALGRGVYSLIISVARQLVVLLPLAWLLAKMFGLNGVWWSFPIAE
IVSFLLSLLFLKRL
>gnl|CDD|240550 cd13145, MATE_like_5, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
DLTKGPIPKLIRKLAIPASVGFFFNTMFNVVDTFFAGKISTEALAALSLSFPIFFIIIAIGVGIGTGTTA
LIGNALGAGDRRKARRYAAQGLSFGIILAILLTVIGLFAAPPLFRLLGAEGDYLDLALEYMDVIFAGSIF
FLLNFGLNGILNAQGDTKSYRNFLIIGFFLNIILDPLFIFGGGGIPAMGVSGIALATIISQFIGMFYLLY
KVRKSGIISGCRLRDFIPRLDVYKEILKQGFPASLNMMTIGLGIFVITYFVGQFGDEAVAAYGIALRIEQ
ILLLPTIGLNTAVLSIAGQNFGAKKYDRVRETYKKALKYGFVIMVVATVFLLFFAEPLMSLFTNDPAVIA
IGAGYLRIDALIFYAYVVLFISVSVLQGLKRPIFALWIGLYRQLVGPALVFWLLVNVLGLGVTGIWWGIF
TIVWSAAIIALLYTRRVLKK
>gnl|CDD|240551 cd13146, MATE_like_6, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
MFSGPISPLLIRLALPILIGQLFQLLYNITDTIWISMIDPSDPALVGGIGLVFPLGMIFLALGNGIQVGV
SSLLARAIGAQRAKELDQAADSGLALALLAATVIVVLGYIFAEPLLQLLGAKGLLLEYALEYFYYSLPGV
PFIMLIGVLMGVLQGEGRTKYMMMAMLIGTVVNIVLDPILIFVFDMGVKGAALATVLAQAISLLYLLYVF
LIGKSNVTIHIKLSNISSSVIVEILRVGLPQMLLQLISSISFLIYNRIIIDIDPVAMTAFTLVGRLDQFI
LIPIFAISSALLTIAGQNWGRGNYDRMLQILMTAVILGIVVVLVLVLGYVLVAPWLFSLFTTVPEVVAYA
VLQVRTMALALPFVAISILVTEFFQAIGKAWPSLLLTLIRHVFLSVPVVYLLAYVFGKGITGVYFGIVSA
NFFTALLAMFWGL
>gnl|CDD|240552 cd13147, MATE_MJ0709_like, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins, similar to Methanocaldococcus jannaschii MJ0709. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
ELLLGDPKKAIIKLSIPMIIAMLLQTLYNLVDAIWVAGLGADALAAIGFVFPLFMIIIGLGNGLGAGASS
AISRRIGAKDKEGADNAAVHSILLGLIISIILTIVLLPFLEPILVLMGAGEVLDLAVDYGRIIFLGSIFL
IFNNVAYGILRGEGDTKRAMYAMVAGSILNIILDPIFIYTLGLGIAGAAWATVISMLISSLVLLYWFFVK
KDTYVSLSLKNFKFDKKIVKDILKVGIPASLEQLIMSVLMIILNLILVIVAGTDGVAVYTAGWRIVSFAI
IPLIGIATAVTSVTGAAYGARNYEKLKTAYNYSIKLGLIIELIIAILIFIFAPQIAYLFTYSEESAHLAP
EIVAFLRIMCLFLPFVPFGMMSSSMFQGIGKGLTSLIITILRELIFQVLFAYLFAIVLGLGLFGVWWGIV
LGNAIGSIVGYLWARLYIKRL
>gnl|CDD|240553 cd13148, MATE_like_3, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
RTRALLTAPILPTLLRLALPNILALLVQTLVGLAETYFVGQLGTDALAGVALVFPLLMLTQMMSNGAMGG
GVSSAIARALGAGDRERAEALVWHALVIALAGGLVFSLLFLLFGPALYRLLGGRGEALDAALAYSNVLFS
GAILIWLVNLLAAALRGTGNMRVPALVTLVGAVVQIPLSPGLILGWGPLPRLGVAGAAVAAVLYYALAAL
VLLRYLASGRSRLRLRLRALRLERRLFRDILRVGLLAALSPLQTNLTVLLLTGLVGRFGTAALAGYGIGS
RLEFLLIPLVFGLGAAMTAMVGMNIGAGQIARARRIAWTGALMAAVLAGAIGLVLALFPELWLGLFTHDP
AVLAAGASYLRIVGPFYGFFGLGLALYFASQGAGRMLWPVLAGTLRLLIAAGGGWIAVALFGAGLAGLFA
AAAAAMVAYGLVTAAAVKLGA
>gnl|CDD|240554 cd13149, MATE_like_2, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria
KLTEGSIPRHLIKLTLPMIFGILAMLIFNLTDTFFVGKLGTKELAAISFTFPVVLFLNSLTIGLGIGASA
VISRAIGAGDRNKAKRLATDSLILSLLLSVIVSLLGLFTIPPLFSLLGASGEILPLIVEYMAIWYLGLVF
LVLPMVGNAIIRATGDTKRPSLVMLGAALVNVILDPILIFGFGPIPGMGIAGAAIATVISRALGLGAALY
FLHYHHRLIDFSEPSLKALFRSWKDILSIGIPAALSNILTPLSAAFITALVATYGPAAVAAFGVATRIES
FAFIIVMALSSALGPFVGQNWGAGQYERVQEGLKISLKFSLIYGAILGIVLALFAGWLASLFSAEPEVIE
LITLYLLIVPIGYGGLGILIITSASFNALGKPLYSLGLNLIRVFLLYIPLAYVGSHLLGFAGVFIGALAG
NLIAGILAYFIAKK
>gnl|CDD|240523 cd13150, DAXX_histone_binding, Histone binding domain of the death-domain associated protein (DAXX). DAXX is a nuclear protein that modulates transcription of various genes and is involved in cell death and/or the suppression of growth. DAXX is also a histone chaperone conserved in Metazoa that acts specifically on histone H3.3. This alignment models a functional domain of DAXX that interacts with the histone H3.3-H4 dimer, and in doing so competes with DNA binding and interactions between the histone chaperone ASF1/CIA and the H3-H4 dimer
KRRKQIRRLEKLLKKLSKEIRKLEEKEVDLLDDEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVE
KKIHFSGTRYPEVNRKIEKFVNRNKTFPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQK
RRQNDLWENFGSHLTDDEKDPALEDPELKRKLEENRKIGDKRLNEVIEKYVNKQDDLE
>gnl|CDD|240522 cd13151, DAXX_helical_bundle, Helical bundle domain of the death-domain associated protein (DAXX). DAXX is a nuclear protein that modulates transcription of various genes and is involved in cell death and/or the suppression of growth. DAXX is also a histone chaperone conserved in Metazoa that acts specifically on histone H3.3. This alignment models the N-terminal helical bundle domain of DAXX, which was shown to interact with the tumor suppressor Ras-association domain family 1C (RASSF1C)
GVNKLENEKLFEEFLDKCLSDSAEHPEVVTFLRNRYSRATPEFLKSVEFKNILSRCLARIAARPAKLYVY
INELCTVLKAHTPKKKLN
>gnl|CDD|240516 cd13152, KOW_GPKOW_A, KOW motif of the "G-patch domain and KOW motifs-containing protein" (GPKOW) repeat A. GPKOW contains one G-patch domain and two KOW motifs. GPKOW is a nuclear protein that regulated by catalytic (C) subunit of Protein Kinase A (PKA) and bind RNA in vivo. PKA may be involved in regulating multiple steps in post-transcriptional processing of pre-mRNAs. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. GPKOW is also known as T54 protein or MOS2 homolog
GAYVKILSGKHKGLYGKVEGFDEDNSRVIVKLAIGGETVSVSEFAVKLVTKKEYKKY
>gnl|CDD|240517 cd13153, KOW_GPKOW_B, KOW motif of the "G-patch domain and KOW motifs-containing protein" (GPKOW) repeat B. GPKOW contains one G-patch domain and two KOW motifs. GPKOW is a nuclear protein that regulated by catalytic (C) subunit of Protein Kinase A (PKA) and bind RNA in vivo. PKA may be involved in regulating multiple steps in post-transcriptional processing of pre-mRNAs. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. GPKOW is also known as the T54 protein or MOS2 homolog
GAYVMVVRGKHRGQVGKLLERDKKKETAVVQLLDDFSVVTLSYDDICEYTG
>gnl|CDD|240518 cd13154, KOW_Mtr4, KOW_Mtr4 is an inserted domain in Mtr4 globular domain. Mtr4 is a conserved helicase with a core DExH region that cooperates with the eukaryotic nuclear exosome in RNA processing and degradation. KOW_Mtr4 motif might be involved in presenting RNA substrates to the helicase core. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. KOW motif is located at the extended insertion of Mtr4 protein
FLQPGRLVKVKVGDDDFGWGVVVNFQKRPNKKNGSENSPPQESYVVDVLLNCSSGSSINNGSPSGIRPPG
PGEKGEMEVVPVLLSLIQAISSIRLYLPKDLRSADARQSVGKSLQEVKRRFPDGLPLLD
>gnl|CDD|240519 cd13155, KOW_KIN17, KOW_Kin17 is a RNA-binding motif. KOW domain of the KIN17protein contributes to the RNA-binding properties of the whole protein. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. KIN17 is conserved from yeast to human that ubiquitously expressed at low levels in mammals tissue and have functions in DNA replication, DNA repair and cell cycle control
IGGRVLVVNGAYRGCEATLESIDEDKFSATVRLDSGPLKGRVVEGVPYEDISKL
>gnl|CDD|240520 cd13156, KOW_RPL6, KOW motif of Ribosomal Protein L6. RPL6 contains KOW motif that has an extra ribosomal role as an oncogenic. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4
KPRKLRSSITPGTVLILLAGRFRGKRVVFLKQLDSGLLLVTGPFKINGVPLRRVNQRYVIATSTKVDISG
VKVPKLNDAYFKRKKKKKKKKKEGEFFEEKKKKYVVSEERKEDQKAVDAALLAAIKKVPLLKGYLKSRFS
LRNGDYPHKMKF
>gnl|CDD|269979 cd13157, PTB_tensin-related, Tensin-related Phosphotyrosine-binding (PTB) domain. Tensin plays critical roles in renal function, muscle regeneration, and cell migration. It binds to actin filaments and interacts with the cytoplasmic tails of beta-integrin via its PTB domain, allowing tensin to link actin filaments to integrin receptors. Tensin functions as a platform for assembly and disassembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules, and also by providing interaction sites for other proteins. In addition to its PTB domain, it contains a C-terminal SH2 domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains
TVSRNAQYIGSFPVSGLDVADRADSVRKQLESLKESGSRGRPVILSVSLSGIKICSEDGKVVLMAHALRR
VSYSTCRPAHAQFAFVARNPGGPTNRQYCHVFVTRSPREAQELNLLLCRAFQLAYLKQH
>gnl|CDD|269980 cd13158, PTB_APPL, Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called DCC-interacting protein (DIP)-13alpha) Phosphotyrosine-binding (PTB) domain. APPL interacts with oncoprotein serine/threonine kinase AKT2, tumor suppressor protein DCC (deleted in colorectal cancer), Rab5, GIPC (GAIP-interacting protein, C terminus), human follicle-stimulating hormone receptor (FSHR), and the adiponectin receptors AdipoR1 and AdipoR2. There are two isoforms of human APPL: APPL1 and APPL2, which share about 50% sequence identity. APPL has a BAR and a PH domain near its N terminus, and the two domains are thought to function as a unit (BAR-PH domain). C-terminal to this is a PTB domain. Lipid binding assays show that the BAR, PH, and PTB domains can bind phospholipids. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains
SSEDEDSLLQQLFIVRFLGSMEVKSDRTSEVIYEAMRQVLAARAIHNIFRMTESHLLVTSDCLRLIDPQT
QVTRARFPLADVVQFAAHQENKRLFGFVVRTPEGDGEEPSFSCYVFESNTEGEKICDAIALAKQI
>gnl|CDD|269981 cd13159, PTB_LDLRAP-mammal-like, Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins Phosphotyrosine-binding (PTB) PH-like fold. The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd contains mammals, insects, and sponges
DGVTFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSI
YRISYCTADANHDKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN
>gnl|CDD|269982 cd13160, PTB_LDLRAP_insect-like, Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins Phosphotyrosine-binding (PTB) PH-like fold. The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd contains insects, ticks, sea urchins, and nematodes
PVFTVKYLGRMPARGLWGIKHTRKPLVDALKNLPKGKTLPKTKLEVSSDGVKLEELRGGFGSSKTVFFPI
HTISYGVQDLVHTRVFSMIVVGEQDSSNHPFECHAFVCDSRADARNLTYWLAKAF
>gnl|CDD|269983 cd13161, PTB_TK_HMTK, Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold. TK kinases catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. TK kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases. In HMTK the conserved His-Arg-Asp sequence within the catalytic loop is replaced by a His-Met sequence. TM/HMTK have are 2-3 N-terminal PTB domains. PTB domains in TKs are thought to function analogously to the membrane targeting (PH, myristoylation) and pTyr binding (SH2) domains of Src subgroup kinases. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
LGVFEAKYLGSVPVKEPKGNDVVMAAVKRLKDLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISF
VTVDPKDKKLFAFISHDPRLGRITCHVFRCKRGAQEICDTIAEAFKAAAE
>gnl|CDD|269984 cd13162, PTB_RGS12, Regulator of G-protein signaling 12 Phosphotyrosine-binding (PTB) PH-like fold. RGS12 functions as a GTPase-activating protein and a transcriptional repressor. It is thought to play a role in tumorigenesis. RGS12 specifically interacts with guanine nucleotide-binding protein G(i), alpha-1 subunit and guanine nucleotide-binding protein G(k) subunit alpha. RGS proteins are multi-functional, GTPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways. Upon activation by GPCRs, heterotrimeric G proteins exchange GDP for GTP, are released from the receptor, and dissociate into free, active GTP-bound alpha subunit and beta-gamma dimer, both of which activate downstream effectors. The response is terminated upon GTP hydrolysis by the alpha subunit, which can then bind the beta-gamma dimer and the receptor. RGS proteins markedly reduce the lifespan of GTP-bound alpha subunits by stabilizing the G protein transition state. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
VRMIVGYLGSIELPSTSSNESDSLQAIRGCVRRLRAEQKIHSLVLMKVMHDSVQLCDDRGGVLATYPAEK
LAFSGVCPDDRRFFGLVTMQSTDDQSEAQESEGSLRTSCHVFMVDPELFEHKIHQGIARRF
>gnl|CDD|269985 cd13163, PTB_ICAP1, Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold. ICAP1 (also called Integrin cytoplasmic domain-associated protein 1) binds specifically to the beta1 integrin subunit cytoplasmic domain and the cerebral cavernous malformation (CCM) protein CCM1. It regulates beta1 integrin-dependent cell migration by affecting the pattern of focal adhesion formation. ICAP1 recruits CCM1 to the cell membrane and activates CCM1 by changing its conformation. Since CCM1 plays role in cardiovascular development, it is hypothesized ICAP1 is involved in vascular differentiation. ICAP-1 has an N-terminal domain that rich in serine and threonine and a C-terminal PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
AEFRVKYVGVIENLEGLSHSLEGPLDLINAIDVAQQDGKLPFVAIEEEVILGLSKYGIKVTELNQPVVLK
RHPLYSIIRMVCYDDGLGGKSLLAVKTGDPGEEVYSLLAYQCNSQEQAIEICKTLSTAF
>gnl|CDD|241318 cd13164, PTB_DOK4_DOK5_DOK6, Downstream of tyrosine kinase 4, 5, and 6 proteins phosphotyrosine-binding domain (PTBi). The Dok family adapters are phosphorylated by different protein tyrosine kinases. Dok proteins are involved in processes such as modulation of cell differentiation and proliferation, as well as in control of the cell spreading and migration The Dok protein contains an N-terminal pleckstrin homology (PH) domain followed by a central phosphotyrosine binding (PTB) domain, which has a PH-like fold, and a proline- and tyrosine-rich C-terminal tail. The PH domain binds to acidic phospholids and localizes proteins to the plasma membrane, while the PTB domain mediates protein-protein interactions by binding to phosphotyrosine-containing motifs. The C-terminal part of Dok contains multiple tyrosine phosphorylation sites that serve as potential docking sites for Src homology 2-containing proteins such as ras GTPase-activating protein and Nck, leading to inhibition of ras signaling pathway activation and the c-Jun N-terminal kinase (JNK) and c-Jun activation, respectively. There are 7 mammalian Dok members: Dok-1 to Dok-7. Dok-1 and Dok-2 act as negative regulators of the Ras-Erk pathway downstream of many immunoreceptor-mediated signaling systems, and it is believed that recruitment of p120 rasGAP by Dok-1 and Dok-2 is critical to their negative regulation. Dok-3 is a negative regulator of the activation of JNK and mobilization of Ca2+ in B-cell receptor-mediated signaling, interacting with SHIP-1 and Grb2. Dok-4- 6 play roles in protein tyrosine kinase(PTK)-mediated signaling in neural cells and Dok-7 is the key cytoplasmic activator of MuSK (Muscle-Specific Protein Tyrosine Kinase). PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the IRS-like subgroup
REQNERFNVFLLPSPNLDVYGECLLQITHENIYLWDIHNPRVKLVSWPLCSLRRYGRDSTWFTFEAGRMC
DTGEGLFTFQTREGEQIYQRVHSATLAIAEQHK
>gnl|CDD|269986 cd13165, PTB_DOK7, Downstream of tyrosine kinase 7 phosphotyrosine-binding domain (PTBi). The Dok family adapters are phosphorylated by different protein tyrosine kinases. Dok proteins are involved in processes such as modulation of cell differentiation and proliferation, as well as in control of the cell spreading and migration The Dok protein contains an N-terminal pleckstrin homology (PH) domain followed by a central phosphotyrosine binding (PTB) domain, which has a PH-like fold, and a proline- and tyrosine-rich C-terminal tail. The PH domain is binds to acidic phospholids and localizes proteins to the plasma membrane, while the PTB domain mediates protein-protein interactions by binding to phosphotyrosine-containing motifs. The C-terminal part of Dok contains multiple tyrosine phosphorylation sites that serve as potential docking sites for Src homology 2-containing proteins such as ras GTPase-activating protein and Nck, leading to inhibition of ras signaling pathway activation and the c-Jun N-terminal kinase (JNK) and c-Jun activation, respectively. There are 7 mammalian Dok members: Dok-1 to Dok-7. Dok-1 and Dok-2 act as negative regulators of the Ras-Erk pathway downstream of many immunoreceptor-mediated signaling systems, and it is believed that recruitment of p120 rasGAP by Dok-1 and Dok-2 is critical to their negative regulation. Dok-3 is a negative regulator of the activation of JNK and mobilization of Ca2+ in B-cell receptor-mediated signaling, interacting with SHIP-1 and Grb2. Dok-4- 6 play roles in protein tyrosine kinase(PTK)-mediated signaling in neural cells and Dok-7 is the key cytoplasmic activator of MuSK (Muscle-Specific Protein Tyrosine Kinase). PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the IRS-like subgroup
LGEVHRFPVVVAPGTKLESGPATLHFCNDILVLARDVPPAVLGQWKLSDLRRYGAVPGGFIFEGGTRCGK
WAGVFFLSTEEGEQISFLFDCIVRGISPTKG
>gnl|CDD|269987 cd13166, PTB_CCM2, Cerebral cavernous malformation 2 FERM domain C-lobe. CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM) along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signalling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours. CCM2 possesses an N-terminal PTB domain and a C-terminal Karet domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
SVPLYPPDYRVDPDVLLNDYIEKEVKYLGQLTSVPGSLDPSSRTELLQLLDTARRLGQLPLQLTPEQDAI
LSLSAYNVKLLWRDGEDLILRVPTHDIAAVSYVRDDSLHLVVLKTASEPGISPSQSLSAESSPTSGSLSE
SGPVPVEYCNLVVLACENKAAAEELCSLLCQVFQIVYTESTIDFLDRAIFDGA
>gnl|CDD|269988 cd13167, PTB_P-CLI1, PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like fold. P-CLI1 (also called Phosphotyrosine interaction domain-containing protein 1) increases proliferation of preadipocytes without affecting adipocytic differentiation. It forms a complex with PID1/PCLI1, LRP1 and CUBNI. It is found in subcutaneous fat, heart, skeletal muscle, brain, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocyte. P-CLI1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains
TGYKVTYLGKVSTTGTQFLSGCTESPVIELWKKHTLAREDIFPSNALLEIRPFQVRLHHLDLRGEATVHM
DTFQVARIAYCTADHNISPNIFAWVYREINDDLSFQMDCHAVECESKLEAKKLAHAMMEAFKKTFHSMR
>gnl|CDD|269989 cd13168, PTB_LOC417372, uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold. The function of LOC417372 and its related proteins are unknown to date. Members here contain a N-terminal RUN domain, followed by a PDZ domain, and a C-terminal PTB domain. The RUN domain is involved in Ras-like GTPase signaling. The PDZ domain (also called DHR/Dlg homologous region or GLGF after its conserved sequence motif) binds C-terminal polypeptides, internal (non-C-terminal) polypeptides, and lipids. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup
ALYKALYLGQVEVGEDGGVEQIESAAIIVVLESDLTPKEVLLELGEIGVTVWDKSTSEVLFKHSFPEISS
CGRRVDDPNYFAYIAGDTPCSLAKHFVCYVFEAADEEEAETILQGIAQGFKRTHW
>gnl|CDD|269990 cd13169, RanBD_NUP50_plant, Ran-binding protein 2, repeat 1. RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP#importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The first RanBD2 is present in this hierarchy
TGEENEKAVFSGDGALFEFIDGGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKM
GGKGVTFACVNSAADAKDKLSTFALKFKDPQVVEEFRAAVEAHKDSA
>gnl|CDD|269991 cd13170, RanBD_NUP50, Nucleoporin 50 Ran-binding domain. NUP50 acts as a cofactor for the importin-alpha:importin-beta heterodimer, which allows for transportation of many nuclear-targeted proteins through nuclear pore complexes. It is thought to function primarily at the terminal stages of nuclear protein import to coordinate import complex disassembly and importin recycling. NUP50 is composed of a N-terminal NUP50 domain which binds the C-terminus of importin-beta, a central domain which binds importin-beta, and a C-terminal RanBD which binds importin-beta through Ran-GTP. NUP50:importin-alpha then binds cargo and can stimulate nuclear import. The N-terminal domain of NUP50 is also able to displace nuclear localization signals from importin-alpha. NUP50 interacts with cyclin-dependent kinase inhibitor 1B which binds to cyclin E-CDK2 or cyclin D-CDK4 complexes and prevents its activation, thereby controling the cell cycle progression at G1. Fungal Nup2 transiently associates with nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity
AGEEEEDTVFEVRAKLFKKKDDGEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSV
AGKNNVFVGCVPNPGKPVTYLLRVKTAEDADELAKALEEEK
>gnl|CDD|269992 cd13171, RanBD1_RanBP2_insect-like, Ran-binding protein 2, Ran binding domain repeat 1. RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 1 is present in this hierarchy
TGEENEEVLFCARAKLFRYVDKEWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPM
KKEDKAYIWAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAKKE
>gnl|CDD|269993 cd13172, RanBD2_RanBP2_insect-like, Ran-binding protein 2, Ran binding domain repeat 2. RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 2 is present in this hierarchy
TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNKEDNNKVRLLMRREQVLKVCCNQRLTKDMEF
KYLTNNPKALTWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKAQ
>gnl|CDD|269994 cd13173, RanBD3_RanBP2_insect-like, Ran-binding protein 2, Ran binding domain repeat 3. RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 3 is present in this hierarchy
TGEEDEEVLYSHRAKLFRFVDKEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRKK
DEKSWMWAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAKNE
>gnl|CDD|269995 cd13174, RanBD4_RanBP2_insect-like, Ran-binding protein 2, Ran binding domain repeat 4. RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 4 is present in this hierarchy
TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLR
PMNTSDKSFTWGGMNYAEDAEPEVETLAVRFKNEEIASQFKNVVDQCQ
>gnl|CDD|269996 cd13175, RanBD5_RanBP2_insect-like, Ran-binding protein 2, Ran binding domain repeat 5. RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 5 is present in this hierarchy
FDDDEELFMFEKRITLEMLIGNGNKWLDLGQGNLRIVYDDEIYGARIVLSDDDTDTIIANTIIAVQTSLR
VEGKEAIWSAIDYSQEPLLRRRFRAEFSSDDAAQEFSVVFNEGK
>gnl|CDD|269997 cd13176, RanBD_RanBP2-like, Ran-binding protein 2, Ran binding domains. RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 1 and 3 are present in this hierarchy
TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLK
PNAGSDRSWVWTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ
>gnl|CDD|269998 cd13177, RanBD2_RanBP2-like, Ran-binding protein 2, Ran binding domain repeat 2. RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 2 is present in this hierarchy
TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLK
PLAGSDRAWMWMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ
>gnl|CDD|269999 cd13178, RanBD4_RanBP2-like, Ran-binding protein 2, Ran binding domain repeat 4. RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 4 is present in this hierarchy
SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQ
PLSASNNTLVWTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ
>gnl|CDD|270000 cd13179, RanBD_RanBP1, Ran-binding domain. RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not activate GTPase activity of Ran, but does markedly increase GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). In both mammalian cells and in yeast, RanBP1 acts as a negative regulator of Regulator of chromosome condensation 1 (RCC1) by inhibiting RCC1-stimulated guanine nucleotide release from Ran. In addition to Ran, RanBP1 has been shown to interact with Exportin-1 and Importin subunit beta-1 which docks the NPC at the cytoplasmic side of the nuclear pore complex. RabBP1 contains a single RanBD. The RanBD is present in RanBD1, RanBD2, RanBD3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBD2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity
DAQFEPIVKLPEVEVKTGEEDEEVLFKMRAKLYRFDTENDPPEWKERGTGDVKLLKHKETKKIRLLMRRD
KTLKICANHYITPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQK
>gnl|CDD|270001 cd13180, RanBD_RanBP3, Ran-binding protein 3 Ran-binding domain. RanBP3, a Ran-interacting nuclear protein, unlike the related proteins RanBP1 and RanBP2, which promote disassembly of the export complex in the cytosol, acts as a CRM1 cofactor, enhancing nuclear export signal (NES) export by stabilizing the export complex in the nucleus. CRM1/Exportin1 is responsible for exporting many proteins and ribonucleoproteins from the nucleus to the cytosol. RanBP3 also alters the cargo selectivity of CRM1, promoting recognition of the NES of HIV-1 Rev and of other cargos while deterring recognition of the import adaptor protein Snurportin1. RanBP3 contains a N-terminal nuclear localization signal (NLS), 2 FxFG motifs, and a single RanBD. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity
TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKSDGSGQSRIVMRTQGSLRVILNTKIWPGMT
VEKVSEKSLRITAMDDEGQVKVFLLQASPEDAKQLYNAIQDRI
>gnl|CDD|270002 cd13181, RanBD_NUP2, Nucleoporin 2 Ran-binding domain. Yeast protein Nup2 transiently associates with Nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity
TGEENEEVLYTKRAKLMLFDPSNTESPYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVK
YEKMGNGSLVRVPTINSDGKIETYVIKVKTAADGEELLKALNDAK
>gnl|CDD|270003 cd13182, EVH1-like_Dcp1, Decapping enzyme EVH1-like domain. Dcp1 is a small protein containing an EVH1 domain. The Dcp1-Dcp2 complex plays a critical step in mRNA degradation with the removal of the 50 cap structure. Dcp1 stimulates the activity of Dcp2 by promoting and/or stabilizing the closed complex. The interface of Dcp1 and Dcp2 is not fully conserved and in higher eukaryotes it requires an additional factor. The proline-rich sequence (PRS)-binding sites in Dcp1p indicates that it belongs to a novel class of EVH1 domains. Dcp1 has 2 prominent sites,one required for the function of the Dcp1p-Dcp2p complex, and the other, the PRS-binding site of EVH1 domains, a binding site for decapping regulatory proteins. It also has a conserved hydrophobic patch is shown to be critical for decapping. The EVH1 domains are part of the PH domain superamily
LNLAVLQRYDPYIEEILDTASHVVLYKFDDDSNEWEKTDVEGTLFVYKRSAAPRYGFIVLNRLSPENFVE
DITPELEVELQDPFLIYRNEDGEIYGIWFYDEDDRERIYKLLEKLL
>gnl|CDD|270004 cd13183, FERM_C_FRMPD1_FRMPD3_FRMPD4, FERM domain C-lobe of FERM and PDZ domain containing proteins 1, 3, and 4 (FRMPD1, 3, 4). The function of FRMPD1, FRMPD3, and FRMPD4 is unknown at present. These proteins contain an N-terminal PDZ (post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) domain and a C-terminal FERM domain. PDZ (also known as DHR (Dlg homologous region) or GLGF (glycine-leucine-glycine-phenylalanine) domains) help anchor transmembrane proteins to the cytoskeleton and hold together signaling complexes. PDZ domains bind to a short region of the C-terminus of other specific proteins. The FERM domain is composed of three subdomains: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3), which form a clover leaf fold. The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GGRSFQATLMLQDRESEVTLLVGPRYGISHVINHKLNLLALLAEFSHISRIELLRESDKVSRVELHIHDV
KPITLLMESPDAKDLACLIAGYYRLLVDPRRSIFS
>gnl|CDD|270005 cd13184, FERM_C_4_1_family, FERM domain C-lobe of Protein 4.1 family. The protein 4.1 family includes four well-defined members: erythroid protein 4.1 (4.1R), the best known and characterized member, 4.1G (general), 4.1N (neuronal), and 4.1 B (brain). The less well understood 4.1O/FRMD3 is not a true member of this family and is not included in this hierarchy. Besides three highly conserved domains, FERM, SAB (spectrin and actin binding domain) and CTD (C-terminal domain), the proteins from this family contain several unique domains: U1, U2 and U3. FERM domains like other members of the FERM domain superfamily have a cloverleaf architecture with three distinct lobes: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The brain is a particularly rich source of protein 4.1 isoforms. The various 4.1R, 4.1G, 4.1N, and 4.1B mRNAs are all expressed in distinct patterns within the brain. It is likely that 4.1 proteins play important functional roles in the brain including motor coordination and spatial learning, postmitotic differentiation, and synaptic architecture and function. In addition they are found in nonerythroid, nonneuronal cells where they may play a general structural role in nuclear architecture and/or may interact with splicing factors. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
YGVDLHPAKDSEGVDIMLGVCSSGLLVYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQYETTIGF
KLPNHRAAKRLWKVCVEHHTFFRL
>gnl|CDD|270006 cd13185, FERM_C_FRMD1_FRMD6, FERM domain C-lobe of FERM domain containing 1 and 6 proteins. FRMD6 (also called willin and hEx/human expanded) is localized throughout the cytoplasm or along the plasma membrane. The Drosophilla protein Ex is a regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and is tumor suppression by restricting proliferation and promoting apoptosis. Surprisingly, hEx is thought to function independently of the Hippo pathway. Instead it is hypothesized that hEx inhibits progression through the S phase of the cell cycle by upregulating p21(Cip1) and downregulating Cyclin A. It is also implicated in the progression of Alzheimer disease. Not much is known about FRMD1 to date. Both FRMD1 and FRMD6 contains a single FERM domain which has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe is a member of the PH superfamily. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
EDLNAHLYRLRKSKKETPGSVLLGITAKGIQIYQESDGEQQLLRTFPWSNIGKLSFDRKKFEIRPEGSLR
KLTYYTSSDEKSKYLLALCRETHQFSMAIQPRLSEIR
>gnl|CDD|270007 cd13186, FERM_C_NBL4_NBL5, FERM domain C-lobe of Novel band 4.1-like protein 4 and 5 (NBL4 and 5). NBL4 (also called Erythrocyte protein band 4.1-like 4; Epb4 1l4) plays a role the beta-catenin/Tcf signaling pathway and is thought to be involved in establishing the cell polarity or proliferation. NBL4 may be also involved in adhesion, in cell motility and/or in cell-to-cell communication. No role for NBL5 has been proposed to date. Both NBL4 and NBL5 contain a N-terminal FERM domain which has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe is a member of the PH superfamily. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GVDLHPVKGEDGNEYFLGLTPTGILVFENKTKIGLFFWPRITKLDFKGKKLKLVVKEKDDQEQEHTFVFR
LPNKKACKHLWKCAVEHHAFFR
>gnl|CDD|270008 cd13187, FERM_C_PTPH13, FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13). There are many functions of PTPN13 (also called PTPL1, PTP-BAS, hPTP1E, FAP1, or PTPL1). Mice lacking PTPN13 activity have abnormal regulation of signal transducer and activator of transcription signaling in their T cells, mild impairment of motor nerve repair, and a significant reduction in the growth of retinal glia cultures. It also plays a role in adipocyte differentiation. PTPN13 contains a kinase non-catalytic C-lobe domain (KIND), a FERM domain with two potential phosphatidylinositol 4,5-biphosphate [PtdIns(4,5)P2]-binding motifs, 5 PDZ domains, and a carboxy-terminal catalytic domain. There is an nteraction between the FERM domain of PTPL1 and PtdIns(4,5)P2 which is thought to regulate the membrane localization of PTPN13. PDZ are protein/protein interaction domains so there is the potential for numerous partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated PTPL1 substrates. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GVHFHRVYREKKSSTLSLWLGICSRGIIIYEEKNGARTPVLRFPWRETQKISFDKKKFTIESRGGSGIKH
TFYTDSYKKSQYLLQLCSAQHKFHIQMRSRQST
>gnl|CDD|270009 cd13188, FERM_C_PTPN14_PTPN21, FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and 21). This CD contains PTP members: pez/PTPN14 and PTPN21. A number of mutations in Pez have been shown to be associated with breast and colorectal cancer. The PTPN protein family belong to larger family of PTPs. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. The members are composed of a N-terminal FERM domain and a C-terminal PTP catalytic domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFED
AETAKYVWKLCVLQHKFYRQN
>gnl|CDD|270010 cd13189, FERM_C_PTPN4_PTPN3_like, FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and PTPN3). PTPN4 (also called PTPMEG, protein tyrosine phosphatase, megakaryocyte) is a cytoplasmic protein-tyrosine phosphatase (PTP) thought to play a role in cerebellar function. PTPMEG-knockout mice have impaired memory formation and cerebellar long-term depression. PTPN3/PTPH1 is a membrane-associated PTP that is implicated in regulating tyrosine phosphorylation of growth factor receptors, p97 VCP (valosin-containing protein, or Cdc48 in Saccharomyces cerevisiae), and HBV (Hepatitis B Virus) gene expression; it is mutated in a subset of colon cancers. PTPMEG and PTPN3/PTPH1 contains a N-terminal FERM domain, a middle PDZ domain, and a C-terminal phosphatase domain. PTP1/Tyrosine-protein phosphatase 1 from nematodes and a FERM_C repeat 1 from Tetraodon nigroviridis are also included in this cd. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILG
FNMLSYRACKNLWKSCVEHHTFFRL
>gnl|CDD|270011 cd13190, FERM_C_FAK1, FERM domain C-lobe of Focal Adhesion Kinase 1 and 2. FAK1 (also called FRNK/Focal adhesion kinase-related nonkinase; p125FAK/pp125FAK;PTK2/Protein-tyrosine kinase 2 protein tyrosine kinase 2 (PTK2) is a non-receptor tyrosine kinase that localizes to focal adhesions in adherent cells. It has been implicated in diverse cellular roles including cell locomotion, mitogen response and cell survival. The N-terminal region of FAK1 contains a FERM domain, a linker, a kinase domain, and a C-terminal FRNK (FAK-related-non-kinase) domain. Three subdomains of FERM: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3), form a cloverleaf fold, similar to those of known FERM structures despite the low sequence conservation. The C-lobe/F3 within the FERM domain is part of the PH domain family. The phosphoinositide-binding site found in ERM family proteins is not present in the FERM domain of FAK1. The adjacent Src SH3 and SH2 binding sites in the linker of FAK1 associates with the F3 and F1 lobes and are thought to be involved in regulation. The FERM domain of FAK1 can inhibit enzymatic activity and repress FAK signaling. In an inactive state of FAK1, the FERM domain is thought to interact with the catalytic domain of FAK1 to repress its activity. Upon activation this interaction is disrupted and its kinase activity restored. The FRNK domain is thought to function as a negative regulator of kinase activity. The C-lobe/F3 is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
DQEIFKCALGSGWSIPVDLVIGPEVGISYLTDKGSAPTHLADFEQIQSIQTSKSEDKDGKALLQLKIAGA
SEPLSITCSSLATAESLADLIDGYCRLVNQTDSSLIIRPEK
>gnl|CDD|270012 cd13191, FERM_C_FRMD4A_FRMD4B, FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B). FRMD4A is part of the Par-3/FRMD4A/cytohesin-1 complex that activates Arf6, a central player in actin cytoskeleton dynamics and membrane trafficking, during junctional remodeling and epithelial polarization. The Par-3/Par-6/aPKC/Cdc42 complex regulates the conversion of primordial adherens junctions (AJs) into belt-like AJs and the formation of linear actin cables. When primordial AJs are formed, Par-3 recruits scaffolding protein FRMD4A which connects Par-3 and the Arf6 guanine-nucleotide exchange factor (GEF), cytohesin-1. FRMD4B (also called GRP1-binding protein, GRSP1) is a novel member of GRP1 signaling complexes that are recruited to plasma membrane ruffles in response to insulin receptor signaling. The GRSP1/FRMD4B protein contains a FERM protein domain as well as two coiled coil domains and may function as a scaffolding protein. GRP1 and GRSP1 interact through the coiled coil domains in the two proteins. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GVHYYEVKDKNGIPWWLGVSYKGIGQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDPRRNSHRSRR
TFQSSSVSVHVWYGQTPALCKTIWSMAIAQHQFYLDRKQSKKK
>gnl|CDD|270013 cd13192, FERM_C_FRMD3_FRMD5, FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5). FRMD3 (also called Band 4.1-like protein 4O/4.1O though it is not a true member of that family) is a novel putative tumor suppressor gene that is implicated in the origin and progression of lung cancer. In humans there are 5 isoforms that are produced by alternative splicing. Less is known about FRMD5, though there are 2 isoforms of the human protein are produced by alternative splicing. Both FRMD3 and FRMD5 contain a N-terminal FERM domain, followed by a FERM adjacent (FA) domain, and 4.1 protein C-terminal domain (CTD). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVHHFRWNDITKFNYEGKMFILHV
MQKEEKKHTLGFKCPTPAACKHLWKCAVEQQAFYT
>gnl|CDD|270014 cd13193, FERM_C_FARP1-like, FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins. Members here include FARP1 (also called Chondrocyte-derived ezrin-like protein; PH domain-containing family C member 2), FARP2 (also called FIR/FERM domain including RhoGEF; FGD1-related Cdc42-GEF/FRG), and FRMD7(FERM domain containing 7). FARP1 and FARP2 are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases. FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons. These members are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains. Other members in this family do not contain the DH domains such as the Human FERM domain containing protein 7 and Caenorhabditis elegans CFRM3, both of which have unknown functions. They contain an N-terminal FERM domain, a PH domain, followed by a FA (FERM adjacent) domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
ETARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKINTFSWAKIRKLSFKRKRFLIKLHPEAYG
SYKDTVEFSFESRNECKSFWKKCIEHHAFFRCSEVPKPPSPKLRLFSRGSSF
>gnl|CDD|270015 cd13194, FERM_C_ERM, FERM domain C-lobe/F3 of the ERM family. The ERM family includes ezrin, radixin, moesin and merlin. They are composed of a N-terminal FERM (ERM) domain (also called N-ERMAD (N-terminal ERM association domain)), a coiled coil region (CRR), and a C-terminal domain CERMAD (C-terminal ERM association domain) which has an F-actin-binding site (ABD). Two actin-binding sites have been identified in the middle and N-terminal domains. Merlin is structurally similar to the ERM proteins, but instead of an actin-binding domain (ABD), it contains a C-terminal domain (CTD), just like the proteins from the 4.1 family. Activated ezrin, radixin and moesin are thought to be involved in the linking of actin filaments to CD43, CD44, ICAM1-3 cell adhesion molecules, various membrane channels and receptors, such as the Na+/H+ exchanger-3 (NHE3), cystic fibrosis transmembrane conductance regulator (CFTR), and the beta2-adrenergic receptor. The ERM proteins exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain of ERM is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVF
YSPRLRINKRILDLCMGNHELYMRRRK
>gnl|CDD|270016 cd13195, FERM_C_MYLIP_IDOL, FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein (MYLIP; also called inducible degrader of the LDL receptor, IDOL). MYLIP/IDOL is a regulator of the LDL receptor (LDLR) pathway via the nuclear receptor liver X receptor (LXR). In response to cellular cholesterol loading, the activation of LXR leads to the induction of MYLIP expression. MYLIP stimulates ubiquitination of the LDLR on its cytoplasmic tail, directing its degradation. The LXR-MYLIP-LDLR pathway provides a complementary pathway to sterol regulatory element-binding proteins for the feedback inhibition of cholesterol uptake. MYLIP has an N-terminal FERM domain and in some cases a C-terminal RING domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
YGVEFFEVRNIEGQKLLIGVGPHGITICNDDFEVIERIPYTAIQMATSSGRVFTLTYLSDDGSVKVLEFK
LPSTRAASGLYRAITEKHAFYRCETVRSAVTDQFSRDLKGT
>gnl|CDD|275394 cd13196, FERM_C_JAK, FERM domain C-lobe of Janus kinase (JAK). JAK (also called Just Another Kinase) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. The JAK family in mammals consists of 4 members: JAK1, JAK2, JAK3 and TYK2. JAKs are composed of seven JAK homology (JH) domains (JH1-JH7) . The C-terminal JH1 domain is the main catalytic domain, followed by JH2, which is often referred to as a pseudokinase domain, followed by JH3-JH4 which is homologous to the SH2 domain, and lastly JH5-JH7 which is a FERM domain. Named after Janus, the two-faced Roman god of doorways, JAKs possess two near-identical phosphate-transferring domains; one which displays the kinase activity (JH1), while the other negatively regulates the kinase activity of the first (JH2). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
LSEKYKATMLEGGSKEASEIPVEVLVSGDEGIKWLRTPNTESDWQTLCDIPELCHISIKQESGTVEISRK
DGKPLELEFSSHAEALSFVSLVDGYYRLTCDWTHYLCKD
>gnl|CDD|270018 cd13197, FERM_C_CCM1, FERM domain C-lobe of Cerebral cavernous malformation 1. CCM1 (also called KRIT-1/Krev interaction trapped 1;ankyrin repeat-containing protein Krit1; CAM), a Rap1-binding protein, is expressed in endothelial cells where it is present in cell-cell junctions and associated with junctional proteins. Together with CCM2/MGC4607 and CCM3/PDCD10, KRIT1 constitutes a set of proteins, mutations of which are found in cerebral cavernous malformations which are characterized by cerebral hemorrhages and vascular malformations in the central nervous system. KRIT-1 possesses four ankyrin repeats, a FERM domain, and multiple NPXY sequences, one of which is essential for integrin cytoplasmic domain-associated protein-1alpha (ICAP1alpha) binding and all of which mediate binding of CCM2. KRIT-1 localization is mediated by its FERM domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENK
MSFVVHTKQAGLIVKLLMKLSGQRKPNDRN
>gnl|CDD|270019 cd13198, FERM_C1_MyoVII, FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7). MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
LLFSRFFEATKFSGPSLPKSEVIIAVNWTGIYFVDEQEQVLLELSFPEITGVSSSRGKRDGGQSFTLTTI
QGEEFVFQSPNAEDIAELVNYFLEGLRKR
>gnl|CDD|270020 cd13199, FERM_C2_MyoVII, FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7). MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GSAFFEVKQTTDPSLPEILLIAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLVRGSKL
LCETSLGYKMDDLLTSYISLLLSNMK
>gnl|CDD|270021 cd13200, FERM_C_KCBP, FERM domain C-lobe of Kinesin-like calmodulin binding protein. KCBPs (also called KIPK/Kinesin-like Calmodulin-Binding Protein-Interacting Protein Kinase), a member of the Kinesin-14 family, is a C-terminal microtubule motor with three unique domains including a myosin tail homology region 4 (MyTH4), a talin-like domain, and a calmodulin-binding domain (CBD). Binding of the Ca2+-activated calmodulin to KCBP causes the motor to dissociate from microtubules. The microtubule binding of KCBP is controlled by the calcium binding protein KIC containing a single EF-hand motif. KCBPs are unique to land plants and green algae. The MyTH4 and talin-like domains are not found in other kinesins, while the CBD domain is also only found in Strongylocentrotus purpuratus kinesin-C (SpKinC). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
NSIFFSVRRIEDPIGLLPGKIILGINKRGVHFFRPVPKEYLHSAELRDIMQFGSSNTAVFFKMRVAGVLH
IFQFETKQGEEICVALQTHINDVMMKRYSKARAAANGAA
>gnl|CDD|270022 cd13201, FERM_C_MyoXV, FERM domain C-lobe of Myosin XV (MyoXV/Myo15). MyoXV, a MyTH-FERM myosin, are actin-based motor proteins essential for a variety of biological processes in actin cytoskeleton function. Specifically MyoXV functions in the actin organization in hair cells of the organ of Corti. Mutations in Human MyoXVa causes non-syndromic deafness, DFNB3 and the mouse shaker-2 mutation. MyoXV consists of a N-terminal motor/head region, a neck made of 1-3 IQ motifs, and a tail that consists of either a myosin tail homology 4 (MyTH4) domains, followed by an SH3 domain, and a MyTH-FERM domains as in rat Myo15 or two MyTH-FERM domains separated by a SH3 domain as in human Myo15A. The MyTH-FERM domains are thought to mediate dimerization and binding to other proteins or cargo. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GSNFFYVQRVSDPRLPGPCLLALNREGLHFLDPKTHETLLRIPLKEVQSTRKLRPLEDGTPFLDIKYGNL
MQQRTIRLETDQAHEISRLIAQYIEEASENR
>gnl|CDD|270023 cd13202, FERM_C_MyoX, FERM domain C-lobe of Myosin X (MyoX, Myo10). MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The MyoX FERM domain binds to the NPXY motif of several beta-integrins, a key family of cell surface receptors that are involved in cell adhesion and migration. In addition the FERM domain binds to the cytoplasmic domains of the netrin receptors DCC (deleted in colorectal cancer) and neogenin. The FERM domain also forms a supramodule with its MyTH4 domain which binds to the negatively charged E-hook region in the tails of alpha- and beta-tubulin forming a proposed motorized link between actin filaments and microtubules. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GCTLFEVECKEGGFPKELWLGVSAEGVSLYKRGESKPLESFPYEHILSFGAPQANTYKIVVDGDRPMLFE
TTQVVEIAKLMKAYINEIVK
>gnl|CDD|270024 cd13203, FERM_C1_myosin_like, FERM domain C-lobe, repeat 1, of Myosin-like proteins. These myosin-like proteins are unidentified though they are sequence similar to myosin 1/myo1, myosin 7/myoVII, and myosin 10/myoX. These myosin-like proteins contain an N-terminal motor/head region and a C-terminal tail consisting of two myosin tail homology 4 (MyTH4) and twos FERM domains. In myoX the FERM domain forms a supramodule with its MyTH4 domain which binds to the negatively charged E-hook region in the tails of alpha- and beta-tubulin forming a proposed motorized link between actin filaments and microtubules and a similar thing might happen in these myosins. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The first FERM_N repeat is present in this hierarchy. The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GTTLFDVTYKGYWSYPNNLILGVHCDGFKFVNPDTKEILAEYRYSDLESILVNPSDDVLTLNLSKSVPDE
HKCFMFETPQKEEIASLIASYSPPLRN
>gnl|CDD|270025 cd13204, FERM_C2_myosin_like, FERM domain C-lobe, repeat 2, of Myosin-like proteins. These myosin-like proteins are unidentified though they are sequence similar to myosin 1/myo1, myosin 7/myoVII, and myosin 10/myoX. These myosin-like proteins contain an N-terminal motor/head region and a C-terminal tail consisting of two myosin tail homology 4 (MyTH4) and twos FERM domains. In myoX the FERM domain forms a supramodule with its MyTH4 domain which binds to the negatively charged E-hook region in the tails of alpha- and beta-tubulin forming a proposed motorized link between actin filaments and microtubules and a similar thing might happen in these myosins. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The second FERM_N repeat is present in this hierarchy. The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GSTVFDVTQSYTSNLPKTLWLAIDQSGVHLLERRTKEPLCSYDYSSIVSYSPSLNSLMIVTGSLTKGSKF
IFNTNQAFQIANLIRDYTHVLQD
>gnl|CDD|270026 cd13205, FERM_C_fermitin, FERM domain C-lobe of the Fermitin family. Fermitin functions as a mediator of integrin inside-out signalling. The recruitment of Fermitin proteins and Talin to the membrane mediates the terminal event of integrin signalling, via interaction with integrin beta subunits. Fermatin has FERM domain interrupted with a pleckstrin homology (PH) domain. Fermitin family homologs (Fermt1, 2, and 3, also known as Kindlins) are each encoded by a different gene. In mammalian studies, Fermt1 is generally expressed in epithelial cells, Fermt2 is expressed inmuscle tissues, and Fermt3 is expressed in hematopoietic lineages. Specifically Fermt2 is expressed in smooth and striated muscle tissues in mice and in the somites (a trunk muscle precursor) and neural crest in Xenopus embryos. As such it has been proposed that Fermt2 plays a role in cardiomyocyte and neural crest differentiation. Expression of mammalian Fermt3 is associated with hematopoietic lineages: the anterior ventral blood islands, vitelline veins, and early myeloid cells. In Xenopus embryos this expression, also include the notochord and cement gland. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). This cd is not included in the C-lobe hierarchy based on its position in the tree. One thing to note is that unlike the other members of the C-lobe hierarchy it contains 2 FERM M domains which might also reflect a difference in its evolutionary history. The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
EFGITYFIVRFRGSKKEELLGVAYNRLIRMDLHTGDPIKTWRYSTMKAWNVNWEIREVIIQFEDENIAFA
CLSADCKIVHEFIGGYIFLSM
>gnl|CDD|241360 cd13206, FERM_C-lobe_PLEKHH1_PLEKHH2, FERM domain C-lobe of Pleckstrin homology domain-containing family H. PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GAKLFAAKPKTPSSLENTVVWLAVNEDGISILDYNTMRLVVTYPYSSVMTFGGCQDDFMLVVNSIKDKKK
PTEKLLFAMAKPKILEITLLIASYINAFHQ
>gnl|CDD|275395 cd13207, FERM-like_C_SNX, Atypical FERM-like domain C-lobe of Sorting nexin family. Sorting nexins function in regulating recycling from endosomes to the cell surface. SNX17, SNX27, and SNX31 contain a N-terminal PX domain, a FERM-like domain, and a unique C-terminal region. All three proteins are able to bind the Ras GTPase through their FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GYLIFDHCSCDSPEGHVITVISIGNFELSACTELPDSQTQGQLFNQVRAFCWDVTQRWDLLDTDGPQRTD
EEGLELCFEYARGEKKPQWVKIFTPQANYMSECLERMFCELMVKKE
>gnl|CDD|275396 cd13208, PH-GRAM_MTMR5_MTMR13, Myotubularian (MTM) related 5 and 13 proteins (MTMR5 and MTMR13) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR5 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It lacks several amino acids in the dsPTPase catalytic pocket which renders it catalytically inactive as a phosphatase. MTMR5 is the most well-studied inactive member of this family and has been implicated in cellular growth control and oncogenic transformation. MTMR13 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Leu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR13 has high sequence similarity to MTMR5 and has recently been shown to be a second gene mutated in type 4B Charcot-Marie-Tooth syndrome. Both MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date. Although the majority of the sequences are MTMR 5 and 13, this cd also contains MTM5 nematode sequences
EELVMEGLRVYLLPDGREEGTGGNGGPNLLPAEGALFLTNYRVIFKGTPCDPLACEQTVVRSFPIASLTK
EKKIAVQKLAHLDQKLQEGLQLRSATFQLIKVAFDEEVSSEKIEKFRKQL
>gnl|CDD|275397 cd13209, PH-GRAM_MTMR3_MTMR4, Myotubularian (MTM) related 3 and 4 proteins (MTMR3 and MTMR4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR3 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR3 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The protein can self-associate and also form heteromers with MTMR4. MTMR4, a member of the myotubularin dual specificity protein phosphatase gene family. MTMR4 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The protein form heteromers with MTMR3. Both MTMR3 and MTMR4 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal lipid-binding FYVE domain which binds phosphotidylinositol-3-phosphate. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
LVKEDENLQVPFPELHGEGTEYVGRAEDAVIAISNYRLHIKFKESVINVPLQLIESVECRDMFQLHITCK
DCKVIRCQFSTFEQCQEWLKRLNR
>gnl|CDD|270030 cd13210, PH-GRAM_MTMR6-like, Myotubularian (MTM) related (MTMR) 7 and 8 proteins Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR6, MTMR7, and MRMR8 are all member of the myotubularin dual specificity protein phosphatase gene family. They bind to phosphoinositide lipids through its PH-GRAM domain. These proteins also interact with each other as well as MTMR9. They contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The lipid-binding FYVE domain has been shown to bind phosphotidylinositol-3-phosphate. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
IRTPKVENVRLLDRFSSRKPAVGTLYLTATHLIFVEPSGKKETWILHSHIASVEKLPLTTAGCPLVIRCK
NFQVITFVIPRERDCHDVYTSLLRLSRP
>gnl|CDD|275398 cd13211, PH-GRAM_MTMR9, Myotubularian (MTM) related 9 protein (MTMR9) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR9 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR9 contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, a SET interaction domain, and a C-terminal coiled-coil region. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
MEFAELIKTPKVDNVVLHRPPRPAVEGTLCITGHHLILSSRQDNAEELWLLHSNIDSVEKKFVGKSSGGT
LTLKCKDFRIIQLDIPDMEECLNIASSIE
>gnl|CDD|275399 cd13212, PH-GRAM_MTMR10-like, Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR10, MTMR11, and MTMR12 are catalytically inactive phosphatases that play a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. They contains a Glu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. They contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, a SET interaction domain, and a C-terminal coiled-coil domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold
LPGEQVLAEAPGVRKGLQEDSSQPELSGTLICTNFKITFQPDDWQWLDNTQQKNPLNGEYDFALVCIGQI
EAVSDLKRVQLLRPGSLLKFIPEELIIHCKDFRVLRFGFEATGGEEPKAFQVTIA
>gnl|CDD|275400 cd13213, PH-GRAM_MTMR14, Myotubularian (MTM) related 14 protein (MTMR14) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR14 is a member of the myotubularin protein phosphatase gene family. MTMR14 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. MTMR14 plays a role in the regulation of autophagy and mutations in MTMR14 result in autosomal dominant centronuclear myopathy. MTMR14 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain (SID), a coiled-coil region, and a C-terminal PDZ domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain (SID), and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
RFVVPVILYKGKHICRSATLSGAPELYGRSGLDYLFSGGSGDASSISDIPSEDEETRNGDWQLFDKVRGH
DIKLLKYLSVTYICDLMVENKKVKFGMNVTSSEKVDKEQRYADFTL
>gnl|CDD|275401 cd13214, PH-GRAM_WBP2, WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. WBP2 plays a number of roles including: acting as a tyrosine kinase substrate, activation of estrogen receptor alpha (ERalpha)/progesterone receptor (PR) transcription, and playing a role in breast cancer. WBP2 contain a N-terminal PH-GRAM domain and a C-terminal WWbp domain. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The WWbp domain is characterized by several short PY and PT-like motifs of the PPPPY form and binds to WW domains. WW domains contain two highly conserved tryptophans that are spaced 20-23 residues apart. They bind proline-rich peptide motifs [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs
VESVKGKGAPPFFKGSKKGTIYLTNQRLIFVSSKPTDNFQSFSMPLLNIRDVKFEQPVFGANYLKGKVKP
VPGGGWPGEAEFKLTFKDGGAIEFGQAFLRLAE
>gnl|CDD|275402 cd13215, PH-GRAM1_AGT26, Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 1. ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LYITSKHLCFFAYLPKRSGAVIKSGYLSKRSKRTLRYTRYWFVLKGDTLSWYNSSTDLYFPAGTIDLRYA
TSIELSKSNGEATTSFKIVTNSRTYKFKADSETSADEWVKALKKQI
>gnl|CDD|275403 cd13216, PH-GRAM2_AGT26, Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 2. ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
TEKLIASYYCYLIRVLPVYGKLYVSNNYLCFRSLLPGVSTKMILPLRDIENVEKEKGFRFGYSGLVIVIK
GHEELFFEFSSKSSRDDCERLLL
>gnl|CDD|275404 cd13217, PH-GRAM1_TCB1D8_TCB1D9_family, TCB1D8 and TCB1D9 family Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 1. TBC1D8, TBC1D8B, TBC1D9 and TBC1D9B may act as a GTPase-activating proteins for Rab family protein(s). They all contain an N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the first repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold
EEKLVTYYSCSYWKGRVPRQGWLYLSINHLCFYSFLLGSESKLIIRWTEVSDLERTSNTILTDTIKVNTR
SKEHPFSMFLNISETFKLMEQLAQIPDRP
>gnl|CDD|275405 cd13218, PH-GRAM2_TCB1D8_TCB1D9_family, TCB1D8 and TCB1D9 family Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 2. TBC1D8, TBC1D8B, TBC1D9 and TBC1D9B may act as a GTPase-activating proteins for Rab family protein(s). They all contain an N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the second repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold
EEKLKEVHDCFLWTPFSHFHTHGKMFISENYICFASKEGNLCSVIIPLREVLAIEKTNDSSVLPKPVIIS
IKGKMAFRFSELKDRDELVAKLRLKL
>gnl|CDD|270039 cd13219, PH-GRAM_C2-GRAM, C2 and GRAM domain-containing protein Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. C2GRAM contains two N-terminal C2 domains followed by a single PH-GRAM domain. Since it contains both of these domains it is assumed that this gene cross-links both calcium and phosphoinositide signaling pathways. In general he C2 domain is involved in binding phospholipids in a calcium dependent manner or calcium independent manner. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold
EEFLINDFSCALKRKFLYQGRMFLSARHIGFHSNVFGKKTKFVFLWEDIEEIQESPHSLINPAIVITLRK
GRGLDAGQGVPPIDPDGRLKYKFASFVNRNHAFRTLMRLWK
>gnl|CDD|275406 cd13220, PH-GRAM_GRAMDC, GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. The GRAMDC proteins are membrane proteins. Nothing is known about its function. Members include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, GRAMDC4, and GRAMDC-like proteins. All of the members, except for GRAMDC4 are included in this hierarchy. Each contains a single PH-GRAM domain at their N-terminus. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold
EDERLIDDFSCALQRDILLQGRLYISENHLCFYSNIFGWETKLVIPFKDITSIEKKKTALIFPNAIEITT
KGEKYFFTSFLSRDSAYKLLTRVW
>gnl|CDD|270041 cd13221, PH-GRAM_GRAMDC4, GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. GRAMDC4 is a membrane protein. Nothing is known about its function. Paralogs include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, and GRAMDC-like proteins. It contains a single PH-GRAM domain at its N-terminus. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold
LPVWENGWRCCLINRDKMPTDYIRNGRLYLTENYLCFESSSSSSKKNVVIPLTDITRIEKAKPYSFLPGS
GMSIEVSVSSADKPLFFGAMFRRDEFFDIIALGA
>gnl|CDD|270042 cd13222, PH-GRAM_GEM, GLABRA 2 expression modulator (GEM) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. GEM interacts with CDT1, a pre-replication complex component that is involved in DNA replication, and with TTG1 (Transparent Testa GLABRA 1), a transcriptional regulator of epidermal cell fate. GEM controls the level of histone H3K9 methylation at the promoters of the GLABRA 2 and CAPRICE (CPC) genes, which are essential for epidermis patterning. GEM also regulates cell division in different root cell types. GEM regulates proliferation-differentiation decisions by integrating DNA replication, cell division and transcriptional controls. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold
EEKLLKTFACYLSTSTGPVAGVLYISTKKIAFCSDRPLSFTSPSGQTSWSYYKVVIPLEQLKSVNPSTNV
EKPAEKYIQIVTVDGHEFWFMGFVNYDKAFKNLQEALRN
>gnl|CDD|275407 cd13223, PH-GRAM_MTM-like, Myotubularian 1 and related proteins Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase. MTM1, MTMR1, and MTMR2 are members of the myotubularin protein phosphatase gene family. They contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. In addition MTMR1 (Myotubularian related 1 protein) and MTMR2 (Myotubularian related 2 protein) contain a C-terminal PDZ domain. Mutations in MTMR2 are a cause of Charcot-Marie-Tooth disease type 4B, an autosomal recessive demyelinating neuropathy. The protein can self-associate and form heteromers with MTMR5 and MTMR12. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
LKEKDVTYLCPFRGPVRGTLYITNYRLYFKSRDREPNFVLDVPLGVISRVEKVGGATSRGENSYGLEIHC
KDMRNLRFAHKQENHSRRKLYETLQKYAFP
>gnl|CDD|270044 cd13224, PH_Net1, Neuroepithelial cell transforming 1 Pleckstrin homology (PH) domain. Net1 (also called ArhGEF8) is part of the family of Rho guanine nucleotide exchange factors. Members of this family activate Rho proteins by catalyzing the exchange of GDP for GTP. The protein encoded by this gene interacts with RhoA within the cell nucleus and may play a role in repairing DNA damage after ionizing radiation. Net1 binds to caspase activation and recruitment domain (CARD)- and membrane-associated guanylate kinase-like domain-containing (CARMA) proteins and regulates nuclear factor kB activation. Net1 contains a RhoGEF domain N-terminal to a single PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KLEYLDDKQRDPRIENSKALLCHGELRNKSGHKLYVFLFQDILVLTRPVTRNERQSFQVYRQPIPVQELV
LEDLQDGDVRMGGSFRGAFSNSEKAKNIFRVRFLDPSPGQSHTLQANDVFHKQQWLNCIRTAISP
>gnl|CDD|270045 cd13225, PH-like_bacteria, Pleckstrin homology (PH)-like domains in bacteria (PHb). Pleckstrin homology (PH) domains were first identified in eukaryotic proteins. Recently PH-like domains have been identified in bacteria as well. These PHb form dome-shaped oligomeric rings with a conserved hydrophilic surface at the intersection of the beta-strands of adjacent protomers that likely mediates protein-protein interactions. It is now thought that the PH domain superfamily is more widespread than previous thought and appears to have existed before prokaryotes and eukaryotes diverged. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
DGEKIEAAFKLIRDTFVFTNKRLILVDKQGITGKKVEYLSIPYSSITHFSIETAGTFDLDAELKIWISGQ
DGPIEKEFKKGVDIYEVQKVLAEHV
>gnl|CDD|275408 cd13226, PH-GRAM-like_Eap45, Pleckstrin homology-like domain or GLUE (GRAM-like ubiquitin-binding in Eap45) domain of Eap45. ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. Human/yeast ESCRT-I consists of Tsg101/Vps23, Vps28/Vps28, and a Vps37 homolog/Vps37. Human/yeast ESCRT-II is composed of EAP20/Vps25, EAP30/Vps22, and EAP45/Vps36. Yeast ESCRT-III consists Vps2, Vps20, Vps24, and Snf7 subunits. In contrast, there are three Human paralogs of Snf7 (hSnf7-1/CHMP4A, hSnf7-2/CHMP4B, and hSnf7-3/CHMP4C) and two paralogs of Vps2 (CHMP2A and CHMP2B). Yeast ESCRT-I links directly to ESCRT-II, through a tight interaction of Vps28 (ESCRT-I) with the yeast-specific zinc-finger insertion within the GLUE domain of Vps36. The Vps36 subunit (ESCRT-II) binds ubiquitin using one of its two NZF zinc fingers in its N-terminal region. Human Vps36, EAP45, also binds ubiquitin despite having no NZF domain. Instead, mammalian ESCRT-II interacts with Ub through the Eap45 GLUE domain directly. While yeast Vps36 GLUE shows a preference for the singly phosphorylated PI(3)P, while Eap45 GLUE preferentially binds the triply phosphorylated phosphatidylinositol PI(3,4,5)P3. Structurally, Eap45 GLUE only has a PH-like fold since it lacks the secondary structure element corresponding to the 4 strand, unlike that of yeast Vps36 GLUE. ESCRT-II also interacts with ESCRT-III via a EAP20(Vps25)/CHMP6(Vps20) interaction. The interactions of ESCRT-II GLUE domain with membranes, ESCRT-I, and ubiquitin are critical for ubiquitinated cargo progression from early to late endosomes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MDRFMWCDGLLFPNETLVIQQRGVRIYDGDEKTKFDSGELVLTSHRLIWRDQKQIERCLSLPLSLIVFIE
EEESGGFGKSAKIVVHLHPAPPNKEPGPKQSSPYNYIKLSFKEGGQSEFYRALSEELTR
>gnl|CDD|275409 cd13227, PH-GRAM-like_Vps36, Pleckstrin homology-like domain or GLUE (GRAM-like ubiquitin-binding in Eap45) domain of Vps36. ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. Yeast/human ESCRT-I consists of Vps23/Tsg101, Vps28/Vps28, and Vps37/Vps37 homolog. Yeast/human ESCRT-II is composed of Vps25/EAP20, Vps22/EAP30, and Vps36/EAP45. Yeast ESCRT-III consists Vps2, Vps20, Vps24, and Snf7 subunits. In contrast, there are three human paralogs of Snf7 (hSnf7-1/CHMP4A, hSnf7-2/CHMP4B, and hSnf7-3/CHMP4C) and two paralogs of Vps2 (CHMP2A and CHMP2B). Yeast ESCRT-I links directly to ESCRT-II, through a tight interaction of Vps28 (ESCRT-I) with the yeast-specific zinc-finger insertion within the GLUE domain of Vps36. The Vps36 subunit (ESCRT-II) binds ubiquitin using one of its two NZF zinc fingers in its N-terminal region. Human Vps36, EAP45, also binds ubiquitin despite having no NZF domain. Instead, mammalian ESCRT-II interacts with Ub through the Eap45 GLUE domain itself. The yeast Vps36 GLUE has a complete PH domain, wherease Eap45 GLUE only has a PH-like fold since it lacks the secondary structure element corresponding to the 4 strand. ESCRT-II also interacts with ESCRT-III via a Vps25(EAP20)/Vps20(CHMP6) interaction. Structure 2CAY is missing this insertion that contains 2 NZF zinc fingers. It is a split PH domain, with a noncanonical lipid binding pocket that binds PI(3)P. The interactions of ESCRT-II GLUE domain with membranes, ESCRT-I, and ubiquitin are critical for ubiquitinated cargo progression from early to late endosomes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
WHYVETTRSGQPILRENEKDIYVDDNVGLYHGKSKILNRQNGRIYLTSQRIIYVDDDDPKKNSVALELDD
IKSVEYSSGFLKRSPKIILFLKDESQEGLKKSKNKKIKIAVVTTWVCPI
>gnl|CDD|270048 cd13228, PHear_NECAP, NECAP (adaptin-ear-binding coat-associated protein) Plextrin Homology (PH) fold with ear-like function (PHear) domain. NECAPs are alpha-ear-binding proteins that enrich on clathrin-coated vesicles (CCVs). NECAP 1 is expressed in brain and non-neuronal tissues and cells while NECAP 2 is ubiquitously expressed. The PH-like domain of NECAPs is a protein-binding interface that mimics the FxDxF motif binding properties of the alpha-ear and is called PHear (PH fold with ear-like function) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SVLLVKPEVYVYRIPPRASAAGYRAADWGLEKPIWTGRLRVVAKGEECEIRLEDPNTGELFAQCPVDVDP
GTAVEPVLDSSRYFVLRVEDGAGRHAFIGIGFRERSDAFDFNVALQDHFK
>gnl|CDD|270049 cd13229, PH_TFIIH, Transcription Factor II H (TFIIH) Pleckstrin homology (PH) domain. The transcription factor II H (TFIIH) is one of the general transcription factors (GTFs) known to be a target of the transactivation domain (TAD) of p53. Human TFIIH and its homologous yeast counterpart (factor b) are composed of ten subunits that can be divided into two groups, the core TFIIH (XPB/Ssl2, p62/Tfb1, p52/Tfb2, p44/Ssl1, p34/Tfb4, and TTDA/Tfb5 in human/yeast) and the CAK complex (cdk7/Kin28, cyclin H/Ccl1, and MAT1/Tfb3). These two complexes are linked by the XPD/Rad3 subunit. The helicase activities of XPB and XPD are essential to the formation of the open complex during transcription initiation and the kinase activity of cdk7 phosphorylates the C-terminal domain (CTD) of the RNA Pol II largest subunit, enabling RNA Pol II to progress from the initiation phase to the elongation phase of transcription. The PH domain of p62/Tfb1 has been shown to interact with herpes simplex virus protein 16 (VP16) TAD and the binding of p53 TAD is mediated by the TAD2 subdomain. TFIIE recruits TFIIH to complete the preinitiation complex (PIC) formation and regulates enzymatic activities of TFIIH. The PH domain of the human TFIIH p62 subunit binds to the C-terminal acidic (AC) domain of the human TFIIEalpha subunit. This interaction could be a switch to replace p53 with TFIIE on TFIIH in transcription. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LLSGAAVYKKKDGTLYLSESRLGWKPSGGDSPPISLPYSDIKNQQISPEGSAKVQLKLVLKDGGSFTFHF
TNPSGARKDRDAVKDLLQQLLAR
>gnl|CDD|270050 cd13230, PH1_SSRP1-like, Structure Specific Recognition protein 1 (SSRP1) Pleckstrin homology (PH) domain, repeat 1. SSRP1 is a component of FACT (facilitator of chromatin transcription), an essential chromatin reorganizing factor. In yeast FACT (yFACT) is composed of three proteins: Spt16/Cdc68, Pob3, and Nhp6. In metazoans the Pob3 and Nhp6 orthologs are fused to form SSRP1/T160 in human and mouse, respectively. The middle domain of the Pob3 subunit (Pob3-M) has an unusual double pleckstrin homology (PH) architecture. yFACT interacts in a physiologically important way with the central single-strand DNA binding factor RPA to promote a step in DNA Replication. Coordinated function by yFACT and RPA is important during nucleosome deposition. These results support the model that the FACT family has an essential role in constructing nucleosomes during DNA replication, and suggest that RPA contributes to this process. Members of this cd are composed of the first PH-like repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VTGDAIVTFEDILCLTPRGRYDIEMYPSFLRLHGKTYDYKIQYKSISRLFLLPKPDDRHVFFVISLDPPI
RQGQTRYPFLVMQFDKDEEVELELNLTEEELEEKYKGKLEKEMSGPLYEVVSRVFKGLTGKKITVPG
>gnl|CDD|270051 cd13231, PH2_SSRP1-like, Structure Specific Recognition protein 1 (SSRP1) Pleckstrin homology (PH) domain, repeat 2. SSRP1 is a component of FACT (facilitator of chromatin transcription), an essential chromatin reorganizing factor. In yeast FACT (yFACT) is composed of three proteins: Spt16/Cdc68, Pob3, and Nhp6. In metazoans the Pob3 and Nhp6 orthologs are fused to form SSRP1/T160 in human and mouse, respectively.The middle domain of the Pob3 subunit (Pob3-M) has an unusual double pleckstrin homology (PH) architecture. yFACT interacts in a physiologically important way with the central single-strand DNA binding factor RPA to promote a step in DNA Replication. Coordinated function by yFACT and RPA is important during nucleosome deposition. These results support the model that the FACT family has an essential role in constructing nucleosomes during DNA replication, and suggest that RPA contributes to this process. Members of this cd are composed of the second PH-like repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
FQSSNGQPAIKCSLKANEGLLYPLEKSFLFVHKPPILIRFDEISSVEFSRVGGGSTSSRTFDLEVELKGG
TEHTFSSIDREEYGPLEDFLKSKKLKIKNE
>gnl|CDD|270052 cd13232, Ig-PH_SCAB1, Stomatal Closure Related Actin-Binding Protein 1 Pleckstrin homology-like domain. SCAB1 is an actin-binding protein that interacts with actin filaments and regulates stomatal movement. SCAB1 is composed of an actin-binding domain, two coiled-coil (CC) domains, and a fused immunoglobulin (Ig) and PH (Ig-PH) domain. SCAB1 homologs are widely present, often in multiple copies (three in Arabidopsis), in plants including eudicots, monocots, ferns and mosses, but are not found in algae and non-plant species. The C-terminal PH domain binds weakly with inositol phosphates via an atypical basic surface patch. SCAB1 forms a dimeric structure via its coiled-coil domains. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
AAGLGNYVEALMKKGDIEFNVVVTQMNGEDVEKKSLHMFHIGKLRIKLRKGRTTKAKEEYSSTMQLCGAR
GGGNAAARALYWQANKGLSYMLAFESERERNAAIMLARRFASDCNVVLA
>gnl|CDD|270053 cd13233, PH_ARHGAP9-like, Beta-spectrin pleckstrin homology (PH) domain. ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with RhoGAP domain. The ARHGAP members here all have a PH domain upstream of their C-terminal RhoGAP domain. Some have additional N-terminal SH3 and WW domains. The members here include: ARHGAP9, ARHGAP12, ARHGAP15, and ARHGAP27. ARHGAP27 and ARHGAP12 shared the common-domain structure, consisting of SH3, WW, PH, and RhoGAP domains. The PH domain of ArhGAP9 employs a non-canonical phosphoinositide binding mechanism, a variation of the spectrin- Ins(4,5)P2-binding mode, that gives rise to a unique PI binding profile, namely a preference for both PI(4,5)P2 and the PI 3-kinase products PI(3,4,5)P3 and PI(3,4)P2. This lipid binding mechanism is also employed by the PH domain of Tiam1 and Slm1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
EKQGLLNKTKIAENGKKLRKNWSTSWVVLTSSHLLFYKDAKSAAKSGNPYSKPESSVDLRGASIEWAKEK
SSRKNVFQISTVTGTEFLLQSDNDTEIREWFDAIKAVIQR
>gnl|CDD|270054 cd13234, PHsplit_PLC_gamma, Phospholipase C-gamma Split pleckstrin homology (PH) domain. PLC-gamma (PLCgamma) is activated by receptor and non-receptor tyrosine kinases due to the presence of its SH2 and SH3 domains. There are two main isoforms of PLC-gamma expressed in human specimens, PLC-gamma1 and PLC-gamma2. PLC-gamma consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves internal to which is a PH domain split by two SH2 domains and a single SH3 domain, and a C-terminal C2 domain. The split PH domain is present in this hierarchy. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SIKNGILYLEDPINHEWYPHFFVLTSNKIYYSEETENSPLGSLLRGILDVPSCHVVKRPEGKNSRPFVFI
LSPKSLSDPPLDVAADSQEELQDWVQKIREVAQTA
>gnl|CDD|270055 cd13235, PH2_FARP1-like, FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin Homology (PH) domain, repeat 2. Members here include FARP1 (also called Chondrocyte-derived ezrin-like protein; PH domain-containing family C member 2), FARP2 (also called FIR/FERM domain including RhoGEF; FGD1-related Cdc42-GEF/FRG), and FARP6 (also called Zinc finger FYVE domain-containing protein 24). They are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases. Little is known about FARP1 and FARP6, though FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons. FARP1 and FARP2 are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains. FARP6 is composed of Dbl-homology (DH), and two C-terminal PH domains separated by a FYVE domain. This hierarchy contains the second PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VENQMSGYLLRKFKNSNGWQKLWVVFTNFCLFFYKSHQDEFPLASLPLLGYSVGLPSEADNIDKDYVFKL
QFKSHVYFFRAESEYTFERWMEVIRSAT
>gnl|CDD|270056 cd13236, PH2_FGD1-4, FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins pleckstrin homology (PH) domain, C-terminus. In general, FGDs have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain. Not much is known about FGD2. FGD1 is the best characterized member of the group with mutations here leading to the X-linked disorder known as faciogenital dysplasia (FGDY). Both FGD1 and FGD3 are targeted by the ubiquitin ligase SCF(FWD1/beta-TrCP) upon phosphorylation of two serine residues in its DSGIDS motif and subsequently degraded by the proteasome. However, FGD1 and FGD3 induced significantly different morphological changes in HeLa Tet-Off cells and while FGD1 induced long finger-like protrusions, FGD3 induced broad sheet-like protrusions when the level of GTP-bound Cdc42 was significantly increased by the inducible expression of FGD3. They also reciprocally regulated cell motility in inducibly expressed in HeLa Tet-Off cells, FGD1 stimulated cell migration while FGD3 inhibited it. FGD1 and FGD3 therefore play different roles to regulate cellular functions, even though their intracellular levels are tightly controlled by the same destruction pathway through SCF(FWD1/beta-TrCP). FGD4 is one of the genes associated with Charcot-Marie-Tooth neuropathy type 4 (CMT4), a group of progressive motor and sensory axonal and demyelinating neuropathies that are distinguished from other forms of CMT by autosomal recessive inheritance. Those affected have distal muscle weakness and atrophy associated with sensory loss and, frequently, pes cavus foot deformity. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
ASAVPENSLLCGFLQYSEKGKTWQKVWCVIPRTEPLVLYLYGAPQDVRAQRTIPLPGCEVTVPPPEERLD
GRHVFKLSQSKQSHYFSAESEELQQRWLEALSRAA
>gnl|CDD|270057 cd13237, PH2_FGD5_FGD6, FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6 pleckstrin homology (PH) domain, C-terminus. FGD5 regulates promotes angiogenesis of vascular endothelial growth factor (VEGF) in vascular endothelial cells, including network formation, permeability, directional movement, and proliferation. The specific function of FGD6 is unknown. In general, FGDs have a RhoGEF (DH) domain, followed by a PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activate the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the PH domain is involved in intracellular targeting of the DH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MSGYLQRRKKSKKSWKRLWFVLKDKVLYTYKASEDVVALESVPLLGFTVVTIDESFEEDESLVFQLLHKG
QLPIIFRADDAETAQRWIEAL
>gnl|CDD|270058 cd13238, PH2_FGD4_insect-like, FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 4 pleckstrin homology (PH) domain, C-terminus, in insect and related arthropods. In general, FGDs have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain. FGD4 is one of the genes associated with Charcot-Marie-Tooth neuropathy type 4 (CMT4), a group of progressive motor and sensory axonal and demyelinating neuropathies that are distinguished from other forms of CMT by autosomal recessive inheritance. Those affected have distal muscle weakness and atrophy associated with sensory loss and, frequently, pes cavus foot deformity. This cd contains insects, crustaceans, and chelicerates. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LSGYLKLKTNGRKTWSRRWFALQPDFVLYSYKSQEDKLPLTATPVPGFLVTLLEKGSAVDPLNDPKRPRT
FKMFHVKKSYYFQANDGDEQKKWVLTL
>gnl|CDD|270059 cd13239, PH_Obscurin, Obscurin pleckstrin homology (PH) domain. Obscurin (also called Obscurin-RhoGEF; Obscurin-myosin light chain kinase/Obscurin-MLCK) is a giant muscle protein that is concentrated at the peripheries of Z-disks and M-lines. It binds small ankyrin I, a component of the sarcoplasmic reticulum (SR) membrane. It is associated with the contractile apparatus through binding with titin and sarcomeric myosin. It plays important roles in the organization and assembly of the myofibril and the SR. Obscurin has been observed as alternatively-spliced isoforms. The major isoform in sleletal muscle, approximately 800 kDa in size, is composed of many adhesion modules and signaling domains. It harbors 49 Ig and 2 FNIII repeats at the N-terminues, a complex middle region with additional Ig domains, an IQ motif, and a conserved SH3 domain near RhoGEF and PH domains, and a non-modular C-terminus with phosphorylation motifs. The obscurin gene also encodes two kinase domains, which are not part of the 800 kDa form of the protein, but is part of smaller spliced products that present in heart muscle. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LIENYPAPLQALGEPIRQGHFTVWEEAPEVKTSSRGHHRHVFLFKNCVVICKPKRDSRTDTVTYVFKNKM
KLSDIDVKDTVEGDDRSFGLWHEHRGSVRKYTLQARSAIIKSSWLKDLRDLQQRL
>gnl|CDD|270060 cd13240, PH1_Kalirin_Trio_like, Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1. RhoGEFs, Kalirin and Trio, the mammalian homologs of Drosophila Trio and Caenorhabditis elegans UNC-73 regulate a novel step in secretory granule maturation. Their signaling modulates the extent to which regulated cargo enter and remain in the regulated secretory pathway. This allows for fine tuning of peptides released by a single secretory cell type with impaired signaling leading to pathological states. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Kalirin and Trio are encoded by separate genes in mammals and by a single one in invertebrates. Kalirin and Trio share the same complex multidomain structure and display several splice variants. The longest Kalirin and Trio proteins have a Sec14 domain, a stretch of spectrin repeats, a RhoGEF(DH)/PH cassette (also called GEF1), an SH3 domain, a second RhoGEF(DH)/PH cassette (also called GEF2), a second SH3 domain, Ig/FNIII domains, and a kinase domain. The first RhoGEF(DH)/PH cassette catalyzes exchange on Rac1 and RhoG while the second RhoGEF(DH)/PH cassette is specific for RhoA. Kalirin and Trio are closely related to p63RhoGEF and have PH domains of similar function. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinases, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, cytoskeletal associated molecules, and in lipid associated enzymes
LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSE
IGVTEHIEGDPCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI
>gnl|CDD|270061 cd13241, PH2_Kalirin_Trio_p63RhoGEF, p63RhoGEF pleckstrin homology (PH) domain, repeat 2. The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VGRLQGFDGKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSEILGKKTQFSNPGYIYKNH
IKVNKMSLEENVDGDPLRFALKSRDPNNPSETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY
>gnl|CDD|270062 cd13242, PH_puratrophin-1, Puratrophin-1 pleckstrin homology (PH) domain. Puratrophin-1 (also called Purkinje cell atrophy-associated protein 1 or PLEKHG4/Pleckstrin homology domain-containing family G member 4) contains a spectrin repeat, a RhoGEF (DH) domain, and a PH domain. It is thought to function in intracellular signaling and cytoskeleton dynamics at the Golgi. Puratrophin-1 is expressed in kidney, Leydig cells in the testis, epithelial cells in the prostate gland and Langerhans islet in the pancreas. A single nucleotide substitution in the puratrophin-1 gene were once thought to result in autosomal dominant cerebellar ataxia (ADCA), but now it has been demonstrated that this ataxia is a result of defects in the BEAN gene. Puratrophin contains a domain architecture similar to that of Dbl family members Dbs and Trio. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a RhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RFQLRHGNDLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQGRKKCLRHVFLFEDLILFSKPKKTPGGKDVY
IYKHSIKTSDIGLTENVGDSGLKFEIWFRRRKARDTYILQATSPEIKQAWTSDIAKLLWKQAIRNR
>gnl|CDD|270063 cd13243, PH_PLEKHG1_G2_G3, Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) domain. PLEKHG1 (also called ARHGEF41), PLEKHG2 (also called ARHGEF42 or CLG/common-site lymphoma/leukemia guanine nucleotide exchange factor2), and PLEKHG3 (also called ARHGEF43) have RhoGEF DH/double-homology domains in tandem with a PH domain which is involved in phospholipid binding. They function as a guanine nucleotide exchange factor (GEF) and are involved in the regulation of Rho protein signal transduction. Mutations in PLEKHG1 have been associated panic disorder (PD), an anxiety disorder characterized by panic attacks and anticipatory anxiety. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RSVVEEALDTMTQVAWHINDMKRKHEHAVRVQEIQSLLDGWEGPELTTYGDLVLEGTFRMAGAKNERLLF
LFDKMLLITKKREDGILQYKTHIMCSNLMLSESIPKEPLSFQVLPFDNPKLQYTLQAKNQEQKRLWTQEI
KRLILEN
>gnl|CDD|270064 cd13244, PH_PLEKHG5_G6, Pleckstrin homology domain-containing family G member 5 and 6 pleckstrin homology (PH) domain. PLEKHG5 has a RhoGEF DH/double-homology domain in tandem with a PH domain which is involved in phospholipid binding. PLEKHG5 activates the nuclear factor kappa B (NFKB1) signaling pathway. Mutations in PLEKHG5 are associated with autosomal recessive distal spinal muscular atrophy. PLEKHG6 (also called MyoGEF) has no known function to date. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RRLLLEGDLRLKEGKGSKVDVHCFLFTDMLLICKPVKRKKDRLKVIRPPYLVDKLVVQELKDPGGFLLVY
LNEFHTAVAAYTFQTSSQEDTRRWLDAIRK
>gnl|CDD|270065 cd13245, PH_PLEKHG7, Pleckstrin homology domain-containing family G member 7 pleckstrin homology (PH) domain. PLEKHG7 has a RhoGEF DH/double-homology domain in tandem with a PH domain which is involved in phospholipid binding. PLEKHG7 is proposed to functions as a guanine nucleotide exchange factor (GEF) and is involved in the regulation of Rho protein signal transduction. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
QLLHEGPLTLIESGKTLDVYLFLFDDMLLITKMKKNLKKKKSSDSENSMPSLELTPLIKEGGSYTVYKQP
IPLDRLCLHDVDPNEATANGLKHAFVLVHLNRYQQVIGVYTLQASSENTKQTWMSKLR
>gnl|CDD|270066 cd13246, PH_Scd1, Shape and Conjugation Deficiency 1 Pleckstrin homology (PH) domain. Fission yeast Scd1 is an exchange factor for Cdc42 and an effector of Ras1, the homolog of the human H-Ras. Scd2/Bem1 mediates Cdc42 activation by binding to Scd1/Cdc24 and to Cdc42. Ras1 regulates Scd1/Cdc24/Ral1, which is a putative guanine nucleotide exchange factor for Cdc42, a member of the Rho family of Ras-like proteins. Cdc42 then activates the Shk1/Orb2 protein kinase. Scd1 interacts with Klp5 and Klp6 kinesins to mediate cytokinesis. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
QRRAENQQVVDDLKARVEDWKGHSLDSFGELLLHDTFTVRKDDSEREYHVYLFERILLCCKEEKKKKKKK
GSKSKSSSSSKKKKGKGPLQLKGRIYIRNITDVTSSSKPGEYSLQITWKGDDELESFILKFRNEEQLKQW
ESTINRLI
>gnl|CDD|270067 cd13247, BAR-PH_APPL, Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif Bin1/amphiphysin/Rvs167 (BAR)-Pleckstrin homology (PH) domain. APPL (also called DCC-interacting protein (DIP)-13alpha) interacts with oncoprotein serine/threonine kinase AKT2, tumor suppressor protein DCC (deleted in colorectal cancer), Rab5, GIPC (GAIP-interacting protein, C terminus), human follicle-stimulating hormone receptor (FSHR), and the adiponectin receptors AdipoR1 and AdipoR2. There are two isoforms of human APPL: APPL1 and APPL2, which share about 50% sequence identity. APPL has a BAR and a PH domain near its N terminus, and the two domains are thought to function as a unit (BAR-PH domain). C-terminal to this is a PTB domain. Lipid binding assays show that the BAR, PH, and PTB domains can bind phospholipids. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
EELSSSADYFYEGDPDETQAAPNRNLTQKAGYLFIRSKTGLVTNKWDRTYFFTQGGNLMSQPRDEVAGSL
VLDLDNCSVQAADCEDRRNVFQITSPDGKKAIVLQAESKKDYEEWIATINNISQQ
>gnl|CDD|270068 cd13248, PH_PEPP1_2_3, Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain. PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RDPNAPVVMSGWLHKQGGSGLKNWRKRWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDEISRK
FAFKAEHANMRTYYFAADTAEEMEQWMNAMSLAA
>gnl|CDD|270069 cd13249, PH_rhotekin2, Anillin Pleckstrin homology (PH) domain. Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
QEMMSGYLSQQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSKGRA
SSLSIINPYSGEEVTHVLSADSREELQKWMEALWQHFYDMS
>gnl|CDD|270070 cd13250, PH_ACAP, ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain. ACAP (also called centaurin beta) functions both as a Rab35 effector and as an Arf6-GTPase-activating protein (GAP) by which it controls actin remodeling and membrane trafficking. ACAP contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain, a phospholipid-binding domain, a PH domain, a GAP domain, and four ankyrin repeats. The AZAPs constitute a family of Arf GAPs that are characterized by an NH2-terminal pleckstrin homology (PH) domain and a central Arf GAP domain followed by two or more ankyrin repeats. On the basis of sequence and domain organization, the AZAP family is further subdivided into four subfamilies: 1) the ACAPs contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain (a phospholipid-binding domain that is thought to sense membrane curvature), a single PH domain followed by the GAP domain, and four ankyrin repeats; 2) the ASAPs also contain an NH2-terminal BAR domain, the tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 domain; 3) the AGAPs contain an NH2-terminal GTPase-like domain (GLD), a split PH domain, and the GAP domain followed by four ankyrin repeats; and 4) the ARAPs contain both an Arf GAP domain and a Rho GAP domain, as well as an NH2-terminal sterile-a motif (SAM), a proline-rich region, a GTPase-binding domain, and five PH domains. PMID 18003747 and 19055940 Centaurin can bind to phosphatidlyinositol (3,4,5)P3. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KEGYLFKRSSNAFKTWKRRWFSLQNGQLYYQKRDKKDEPTVMVEDLRLCTVKPTEDSDRRFCFEVISPTK
SYMLQAESEEDRQAWIQAIQSAIASALN
>gnl|CDD|270071 cd13251, PH_ASAP, ArfGAP with SH3 domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain. ASAPs (ASAP1, ASAP2, and ASAP3) function as an Arf-specific GAPs, participates in rhodopsin trafficking, is associated with tumor cell metastasis, modulates phagocytosis, promotes cell proliferation, facilitates vesicle budding, Golgi exocytosis, and regulates vesicle coat assembly via a Bin/Amphiphysin/Rvs domain. ASAPs contain an NH2-terminal BAR domain, a tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 (SH3) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
QQQGNKSHGTEKSGYLLKKSEGKIRKVWQKRRCSIKDGFLTISHADENKPPAKLNLLTCQVKLVPEDKKC
FDLISHNRTYHFQAEDENDANAWMSVLKNSKEQALNKA
>gnl|CDD|270072 cd13252, PH1_ADAP, ArfGAP with dual PH domains Pleckstrin homology (PH) domain, repeat 1. ADAP (also called centaurin alpha) is a phophatidlyinositide binding protein consisting of an N-terminal ArfGAP domain and two PH domains. In response to growth factor activation, PI3K phosphorylates phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 3,4,5-trisphosphate. Centaurin alpha 1 is recruited to the plasma membrane following growth factor stimulation by specific binding of its PH domain to phosphatidylinositol 3,4,5-trisphosphate. Centaurin alpha 2 is constitutively bound to the plasma membrane since it binds phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate with equal affinity. This cd contains the first PH domain repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
GSKEGFLWKRGKDNNQFKQRKFVLSEREGTLKYFVKEDAKEPKAVISIEELNATFQPEKIGHPNGLQITY
LKDGSTRNIFVYHEDGKEIVDWYNAIRAARLHYLQVAFP
>gnl|CDD|270073 cd13253, PH1_ARAP, ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 1. ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the first PH domain in ARAP. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
IKSGYLDKQGGQGNNKGFQKRWVVFDGLSLRYFDSEKDAYSKRIIPLSAISTVRAVGDNKFELVTTNRTF
VFRAESDDERNLWCSTLQAAISEY
>gnl|CDD|270074 cd13254, PH2_ARAP, ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 2. ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the second PH domain in ARAP. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
PRKPNPDKCGYLELRGYKAKVYAALMGDEVWLYKNEQDFRLGIGITVIEMNGANVKDVDRRSFDLTTPYR
SFSFTAESEHEKQEWIEAVQ
>gnl|CDD|270075 cd13255, PH_TAAP2-like, Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain. The binding of TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP2 contains two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. The members here are most sequence similar to TAPP2 proteins, but may not be actual TAPP2 proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MISEAVLKAGYLEKKGERRKTWKKRWFVLRPTKLAYYKNDKEYRLLRLIDLTDIHTCTEVQLKKHDNTFG
IVTPARTFYVQADSKAEMESWISAINLARQALRATITPNT
>gnl|CDD|270076 cd13256, PH3_ARAP, ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 3. ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the third PH domain in ARAP. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SVFHSGFLYKSPSAAKPTLERRAREEFSRRWCVLEDGFLSYYESERSPEPNGEIDVSEIVCLAVSPPDTH
PGDGFPFTFELYLESERLYLFGLETAEALHEWVKAIAKAF
>gnl|CDD|270077 cd13257, PH4_ARAP, ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 4. ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the fourth PH domain in ARAP. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
FERLGRLFYKDGLALDRAREGWFALDKSSLHACLQMQEVEERMHLRKLQELSIQGDVQLDVLVLVERRRT
LYIQGERKLDFTGWHTAIQKA
>gnl|CDD|270078 cd13258, PH_PLEKHJ1, Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain. PLEKHJ1 (also called GNRPX2/Guanine nucleotide-releasing protein x). It contains a single PH domain. Very little information is known about PLEKHJ1. PLEKHJ1 has been shown to interact with IKBKG (inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma) and KRT33B (keratin 33B). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MRFNEKELAALSSQPAEKEGKIAERQMGGPKKSEVFKERWFKLKGNLLFYFRTNEFGDCSEPIGAIVLEN
CRVQMEEITEKPFAFSIVFNDEPEKKYIFSCRSEEQCEQWIEALRQASYEYLR
>gnl|CDD|270079 cd13259, PH5_ARAP, ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 5. ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the five PH domain in ARAP. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
EAILLYLASKVGSTKHGMLKFREEPSKLLSGNKFQDRYFILNDECLLLYKDVKSSKPEKEWPLKSLKVYL
GIKKKLKPPTSWGFTVLLEKQQWYLCCDSQMEQREWMATILSAQHDGDIWP
>gnl|CDD|270080 cd13260, PH_RASA1, RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain. RASA1 (also called RasGap1 or p120) is a member of the RasGAP family of GTPase-activating proteins. RASA1 contains N-terminal SH2-SH3-SH2 domains, followed by two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Splice variants lack the N-terminal domains. It is a cytosolic vertebrate protein that acts as a suppressor of RAS via its C-terminal GAP domain function, enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. Additionally, it is involved in mitogenic signal transmission towards downstream interacting partners through its N-terminal SH2-SH3-SH2 domains. RASA1 interacts with a number of proteins including: G3BP1, SOCS3, ANXA6, Huntingtin, KHDRBS1, Src, EPHB3, EPH receptor B2, Insulin-like growth factor 1 receptor, PTK2B, DOK1, PDGFRB, HCK, Caveolin 2, DNAJA3, HRAS, GNB2L1 and NCK1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KGIDKKGYLLKKGGKNKKWKNLYFVLEGKEQHLYFFDNEKRTKPKGLIDLSYCSLYPVHDSLFGRPNCFQ
IVVRALNESTITYLCADTAELAQEWMRALRAFC
>gnl|CDD|270081 cd13261, PH_RasGRF1_2, Ras-specific guanine nucleotide-releasing factors 1 and 2 Pleckstrin homology (PH) domain. RasGRF1 (also called GRF1; CDC25Mm/Ras-specific nucleotide exchange factor CDC25; GNRP/Guanine nucleotide-releasing protein) and RasGRF2 (also called GRF2; Ras guanine nucleotide exchange factor 2) are a family of guanine nucleotide exchange factors (GEFs). They both promote the exchange of Ras-bound GDP by GTP, thereby regulating the RAS signaling pathway. RasGRF1 and RasGRF2 form homooligomers and heterooligomers. GRF1 has 3 isoforms and GRF2 has 2 isoforms. The longest isoforms of RasGRF1 and RasGRF2 contain the following domains: a Rho-GEF domain sandwiched between 2 PH domains, IQ domains, a REM (Ras exchanger motif) domain, and a Ras-GEF domainwhich gives them the capacity to activate both Ras and Rac GTPases in response to signals from a variety of neurotransmitter receptors. Their IQ domains allow them to act as calcium sensors to mediate the actions of NMDA-type and calcium-permeable AMPA-type glutamate receptors. GRF1 also mediates the action of dopamine receptors that signal through cAMP. GRF1 and GRF2 play strikingly different roles in regulating MAP kinase family members, neuronal synaptic plasticity, specific forms of learning and memory, and behavioral responses to psychoactive drugs. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
ARKDGTKRGYLSKKTSDSGKWHERWFALYQNLLFYFENESSSRPSGLYLLEGCYCERLPTPKGALKGKDH
LEKQHYFTISFRHENQRQYELRAETESDCDEWVEAIKQASFNKLLLQKEELEQKYLHLLQIVESEK
>gnl|CDD|270082 cd13262, PH_RasSynGAP-like, Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain. The RasSynGAP family is composed of members: DAB2IP, nGAP, and SynGAP. Neuronal growth-associated proteins (nGAPs) are growth cone markers found in multiple types of neurons. There are many nGAPs including Cap1 (Adenylate cyclase-associated protein 1), Capzb (Capping protein (actin filament) muscle Z-line, beta), Clptm1 (Cleft lip and palate associated transmembrane protein 1), Cotl1 (Coactosin-like 1), Crmp1 (Collapsin response mediator protein 1), Cyfip1 (Cytoplasmic FMR1 interacting protein 1), Fabp7 (Fatty acid binding protein 7, brain), Farp2 (FERM, RhoGEF and pleckstrin domain protein 2), Gap43 (Growth associated protein 43), Gnao1 (Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O), Gnai2 (Guanine nucleotide binding protein (G protein), alpha inhibiting 2), Pacs1 (Phosphofurin acidic cluster sorting protein 1), Rtn1 (Reticulon 1), Sept2 (Septin 2), Snap25 (Synaptosomal-associated protein 25), Strap (Serine/threonine kinase receptor associated protein), Stx7 (Syntaxin 7), and Tmod2 (Tropomodulin 2). SynGAP, a neuronal Ras-GAP, has been shown display both Ras-GAP activity and Ras-related protein (Rap)-GAP activity. Saccharomyces cerevisiae Bud2 and GAP1 members CAPRI (Ca2+-promoted Ras inactivator) and RASAL (Ras-GTPase-activating-like protein) also possess this dual activity. Human DOC-2/DAB2-interacting protein (DAB2IP) is encoded by a tumor suppressor gene and a newly recognized member of the Ras-GTPase-activating family. DAB2IP is a critical component of many signal transduction pathways mediated by Ras and tumor necrosis factors including apoptosis pathways, and it is involved in the formation of many types of tumors. DAB2IP participates in regulation of gene expression and pluripotency of cells. It has been reported that DAB2IP was expressed in different tumor tissues. Little information is available concerning the expression levels of DAB2IP in normal tissues and cells, however, and no studies of its expression patterns during the development of human embryos have been reported. DAB2IP was expressed primarily in cell cytoplasm throughout the fetal development. The expression levels varied among tissues and different gestational ages. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
ASGFFSRRLKGPLKRTKSVTKLERKSSKRLPRTRLARAPAGPRLRGSRSHESLLSSSSAALDLSADEDVV
IRPLHSSILGRKHCFQVTTSEGTRCFSCRSAAERDRWIEDLRRAAQPNKDNCRRT
>gnl|CDD|270083 cd13263, PH_RhoGap25-like, Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain. RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
ERPIKSGWLKKQGSIVKNWQQRWFVLRGDQLYYYKDEDDTKPQGTIPLPGNKVKEVPFNPEEPGKFLFEI
IPGGGGDRMTSNHDSYLLMANSQAEMEEWVKVIRRVIGSPFGGG
>gnl|CDD|270084 cd13264, PH_ITSN, Intersectin Pleckstrin homology (PH) domain. ITSNs, an adaptor protein family, play a role in endo- and exocytosis, actin cytoskeleton rearrangement and signal transduction. There are two human ITSN genes: ITSN1 and ITSN2. They share significant sequence identity and a similar domain structure having both short and long isoforms produced by alternative splicing. The short isoform (ITSN-S) consists of two Eps15 homology domains (EH1 and EH2), a coiled-coil region (CCR) and five Src homology 3 domains (SH3A-E). The EH domains bind to Asn-Pro-Phe motifs and are implicated in endocytosis and vesicle transport. The SH3 domains bind to proline-rich sequences and are commonly found in proteins implicated in cell signalling pathways, cytoskeletal organization and membrane traffic. The long isoform (ITSN-L) contains three additional C-terminal domains, a Dbl homology domain (DH), a Pleckstrin homology domain (PH) and a C2 domain. The tandem DH-PH domains are present in all Dbl family of GEFs. ITSN acts specifically on Cdc42 through its DH domain with no portion of the PH domain making contact with Cdc42. This is in contrast to Dbs which requires the PH domain for full catalytic activity. The ITSN PH domain binds phosphoinositides. C2 domains are usually involved in Ca2+-dependent and Ca2+-independent phospholipid binding. There are more than 30 proteins that interact with ITSNs. ITSN-S is present in mammals, frogs, flies and nematodes, while ITSN-L is present only in vertebrates. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
QLIFNSVTNCLGPRKFLHSGKLYKAKSNKELYGFLFNDFLLLTQPIKPLGSSGNDFVFDNKANIQYKMYK
TPIFLNEVLVKLPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASELYIETEKK
>gnl|CDD|270085 cd13265, PH_evt, Evectin Pleckstrin homology (PH) domain. There are 2 members of the evectin family (also called pleckstrin homology domain containing, family B): evt-1 (also called PLEKHB1) and evt-2 (also called PLEKHB2). evt-1 is specific to the nervous system, where it is expressed in photoreceptors and myelinating glia. evt-2 is widely expressed in both neural and nonneural tissues. Evectins possess a single N-terminal PH domain and a C-terminal hydrophobic region. evt-1 is thought to function as a mediator of post-Golgi trafficking in cells that produce large membrane-rich organelles. It is a candidate gene for the inherited human retinopathy autosomal dominant familial exudative vitreoretinopathy and a susceptibility gene for multiple sclerosis. evt-2 is essential for retrograde endosomal membrane transport from the plasma membrane (PM) to the Golgi. Two membrane trafficking pathways pass through recycling endosomes: a recycling pathway and a retrograde pathway that links the PM to the Golgi/ER. Its PH domain that is unique in that it specifically recognizes phosphatidylserine (PS), but not polyphosphoinositides. PS is an anionic phospholipid class in eukaryotic biomembranes, is highly enriched in the PM, and plays key roles in various physiological processes such as the coagulation cascade, recruitment and activation of signaling molecules, and clearance of apoptotic cells. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MALVKSGWLLRQSTILKRWKKNWFVLYGDGNLVYYEDETRREVEGRINMPRECRNIRVGLECRDVQPPEG
RSRDCLLQIVLRDGSTLFLCAESADDALAWKLALQDAR
>gnl|CDD|270086 cd13266, PH_Skap_family, Src kinase-associated phosphoprotein family Pleckstrin homology (PH) domain. Skap adaptor proteins couple receptors to cytoskeletal rearrangements. Src kinase-associated phosphoprotein of 55 kDa (Skap55)/Src kinase-associated phosphoprotein 1 (Skap1), Skap2, and Skap-homology (Skap-hom) have an N-terminal coiled-coil conformation, a central PH domain and a C-terminal SH3 domain. Their PH domains bind 3'-phosphoinositides as well as directly affecting targets such as in Skap55 where it directly affecting integrin regulation by ADAP and NF-kappaB activation or in Skap-hom where the dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch that controls ruffle formation. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VIKAGYLEKRRKDHSFFGSEWQKRWCAISKNVFYYYGSDKDKQQKGEFAINGYDVRMNPTLRKDGKKDCC
FELVCPDKRTYQFTAASPEDAEDWVDQISFILQDLS
>gnl|CDD|270087 cd13267, PH_DOCK-D, Dedicator of cytokinesis-D subfamily Pleckstrin homology (PH) domain. DOCK-D subfamily (also called Zizimin subfamily) consists of Dock9/Zizimin1, Dock10/Zizimin3, and Dock11/Zizimin2. DOCK-D has a N-terminal DUF3398 domain, a PH-like domain, a Dock Homology Region 1, DHR1 (also called CZH1), a C2 domain, and a C-terminal DHR2 domain (also called CZH2). Zizimin1 is enriched in the brain, lung, and kidney; zizimin2 is found in B and T lymphocytes, and zizimin3 is enriched in brain, lung, spleen and thymus. Zizimin1 functions in autoinhibition and membrane targeting. Zizimin2 is an immune-related and age-regulated guanine nucleotide exchange factor, which facilitates filopodial formation through activation of Cdc42, which results in activation of cell migration. No function has been determined for Zizimin3 to date. The N-terminal half of zizimin1 binds to the GEF domain through three distinct areas, including CZH1, to inhibit the interaction with Cdc42. In addition its PH domain binds phosphoinositides and mediates zizimin1 membrane targeting. DOCK is a family of proteins involved in intracellular signalling networks. They act as guanine nucleotide exchange factors for small G proteins of the Rho family, such as Rac and Cdc42. There are 4 subfamilies of DOCK family proteins based on their sequence homology: A-D. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SGESGITKEGYLYKGPENSSDSFISLAMKSFKRRFFHLKQLVDGSYILEFYKDEKKKEAKGTIFLDSCTG
VVQNSKRRKFCFELRMQDKKSYVLAAESEAEMDEWISKLNKILQSSKEQSIQKKRS
>gnl|CDD|270088 cd13268, PH_Brdg1, BCR downstream signaling 1 Pleckstrin homology (PH) domain. Brdg1 is thought to function as a docking protein acting downstream of Tec, a protein tyrosine kinases (PTK), in B-cell antigen receptor (BCR) signaling. BRDG1 contains a proline-rich (PR) motif which is thought to bind SH3 or WW domains, a PH domain, and multiple tyrosine residues which are potential target sites for SH2 domains. Since PH domains bind phospholipids it is thought to be involved in the tethering of Tec and BRDG1 to the cell membrane.Tec and Pyk2, but not Btk, Bmx, Lyn, Syk, or c-Abl, induces phosphorylation of BRDG1 on tyrosine residues. Efficient phosphorylation requires both the PH and SH2 domains of BRDG1 and the kinase domain of Tec. The overexpression of BRDG1 increases theBCR-mediated activation of cAMP-response element binding protein (CREB). Phosphorylated BRDG1 is hypothesized to recruit CREB either directly or through its recruitment of downstream effectors which then recruit CREB. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RQERPKIQLPPCYYEGFLEKKRPKDREYRKLWTELCGTTLFFYNDKKDTQYVEKLDLSALESLTDEISRG
RNLDAARFTLVLKDEEVKFKAENLESREEWKGFILTVTELSVPTSLTLLPGQIHMLK
>gnl|CDD|241423 cd13269, PH_alsin, Alsin Pleckstrin homology (PH) domain. The ALS2 gene encodes alsin, a GEF, that has dual specificity for Rac1 and Rab5 GTPases. Alsin mutations in the form of truncated proteins are responsible for motor function disorders including juvenile-onset amyotrophic lateral sclerosis, familial juvenile primary lateral sclerosis, and infantile-onset ascending hereditary spastic paralysis. The alsin protein is widely expressed in the developing CNS including neurons of the cerebral cortex, brain stem, spinal cord, and cerebellum. Alsin contains a regulator of chromosome condensation 1 (RCC1) domain, a Rho guanine nucleotide exchanging factor (RhoGEF) domain, a PH domain, a Membrane Occupation and Recognition Nexus (MORN), a vacuolar protein sorting 9 (Vps9) domain, and a Dbl homology (DH) domain. Alsin interacts with Rab5 through its Vps9 domain and through this interaction modulates early endosome fusion and trafficking. The GEF activity of alsin towards Rab5 is regulated by Rac1 function. The GEF activity of alsin for Rac1 occurs via its DH domain and this interaction plays a role in promoting spinal motor neuron survival via multiple Rac-dependent signaling pathways. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
DSLRSPDRRLIRESSTRPLTLQNAGRFSSHWFILFNDALVHAQFSTHHIFPLATLWVEPIPDEDSGQNAL
KITTPEESFTLVASTPQEKAEWLRAINQAIDQALNG
>gnl|CDD|270089 cd13270, PH1_TAPP1_2, Tandem PH-domain-containing proteins 1 and 2 Pleckstrin homology (PH) domain, N-terminal repeat. The binding of TAPP1 (also called PLEKHA1/pleckstrin homology domain containing, family A (phosphoinositide binding specific) member 1) and TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP1 and TAPP2 contain two sequential PH domains in which the C-terminal PH domain binds PtdIns(3,4)P2. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MPYVDRQNRTCGFLDIEENENSGKFLRRYFILDTAANLLLYYMDNPQNLPVGAAPVGSLNLTYISKVSDA
TKQRPKAEFCFVINALSRRYFLQANDQQDLVEWVEALNNASKITVPKG
>gnl|CDD|270090 cd13271, PH2_TAPP1_2, Tandem PH-domain-containing proteins 1 and 2 Pleckstrin homology (PH) domain, C-terminal repeat. The binding of TAPP1 (also called PLEKHA1/pleckstrin homology domain containing, family A (phosphoinositide binding specific) member 1) and TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP1 and TAPP2 contain two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RQRAGRNVIKSGYCVKQGAVRKNWKRRFFILDDNTISYYKSETDKEPLRTIPLREVLKVHECLVKSLLMR
DNLFEIITTSRTFYIQADSPEEMHSWIKAISGAIVARRGPSRSS
>gnl|CDD|270091 cd13272, PH_INPP4A_INPP4B, Type I inositol 3,4-bisphosphate 4-phosphatase and Type II inositol 3,4-bisphosphate 4-phosphatase Pleckstrin homology (PH) domain. INPP4A (also called Inositol polyphosphate 4-phosphatase type I) and INPP4B (also called Inositol polyphosphate 4-phosphatase type II) both catalyze the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate and inositol 1,3,4-trisphosphate. They differ in that INPP4A additionally catalyzes the hydrolysis of the 4-position phosphate of inositol 3,4-bisphosphate, while INPP4B catalyzes the hydrolysis of the 4-position phosphate of inositol 1,4-bisphosphate. They both have a single PH domain followed by a C2 domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MRFNKQELATLASQPSTKFDKEGLLIITERQEGFFRRSEGSLERWCRLRGNLLFYLKSKDPWSEPAGVIV
LEQCRPRIQNDERDSGGYPFDLVFEDGLCQRLATRTEAERLSWVQAIELASYEVIRAQLKALREQIERAR
GHTH
>gnl|CDD|270092 cd13273, PH_SWAP-70, Switch-associated protein-70 Pleckstrin homology (PH) domain. SWAP-70 (also called Differentially expressed in FDCP 6/DEF-6 or IRF4-binding protein) functions in cellular signal transduction pathways (in conjunction with Rac), regulates cell motility through actin rearrangement, and contributes to the transformation and invasion activity of mouse embryo fibroblasts. Metazoan SWAP-70 is found in B lymphocytes, mast cells, and in a variety of organs. Metazoan SWAP-70 contains an N-terminal EF-hand motif, a centrally located PH domain, and a C-terminal coiled-coil domain. The PH domain of Metazoan SWAP-70 contains a phosphoinositide-binding site and a nuclear localization signal (NLS), which localize SWAP-70 to the plasma membrane and nucleus, respectively. The NLS is a sequence of four Lys residues located at the N-terminus of the C-terminal a-helix; this is a unique characteristic of the Metazoan SWAP-70 PH domain. The SWAP-70 PH domain binds PtdIns(3,4,5)P3 and PtdIns(4,5)P2 embedded in lipid bilayer vesicles. There are additional plant SWAP70 proteins, but these are not included in this hierarchy. Rice SWAP70 (OsSWAP70) exhibits GEF activity toward the its Rho GTPase, OsRac1, and regulates chitin-induced production of reactive oxygen species and defense gene expression in rice. Arabidopsis SWAP70 (AtSWAP70) plays a role in both PAMP- and effector-triggered immunity. Plant SWAP70 contains both DH and PH domains, but their arrangement is the reverse of that in typical DH-PH-type Rho GEFs, wherein the DH domain is flanked by a C-terminal PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
YDELILDVIKKGYLWKKGHLLPTWTERWFVLKPNSLSYYKSEDLKEKKGEIALDSNCCVESLPDREGKKC
RFLVKTPDKTYELSASDHKTRQEWIAAIQTAIRLSQEGKS
>gnl|CDD|270093 cd13274, PH_DGK_type2, Type 2 Diacylglycerol kinase Pleckstrin homology (PH) domain. DGK (also called DAGK) catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA) utilizing ATP as a source of the phosphate. In non-stimulated cells, DGK activity is low and DAG is used for glycerophospholipid biosynthesis. Upon receptor activation of the phosphoinositide pathway, DGK activity increases which drives the conversion of DAG to PA. DGK acts as a switch by terminating the signalling of one lipid while simultaneously activating signalling by another. There are 9 mammalian DGK isoforms all with conserved catalytic domains and two cysteine rich domains. These are further classified into 5 groups according to the presence of additional functional domains and substrate specificity: Type 1 - DGK-alpha, DGK-beta, DGK-gamma - contain EF-hand motifs and a recoverin homology domain; Type 2 - DGK-delta, DGK-eta, and DGK-kappa- contain a pleckstrin homology domain, two cysteine-rich zinc finger-like structures, and a separated catalytic region; Type 3 - DGK-epsilon - has specificity for arachidonate-containing DAG; Type 4 - DGK-zeta, DGK-iota- contain a MARCKS homology domain, ankyrin repeats, a C-terminal nuclear localization signal, and a PDZ-binding motif; Type 5 - DGK-theta - contains a third cysteine-rich domain, a pleckstrin homology domain and a proline rich region. The type 2 DGKs are present as part of this Metazoan DGK hierarchy. They have a N-terminal PH domain, two cysteine rich domains, followed by bipartite catalytic domains, and a C-terminal SAM domain. Their catalytic domains and perhaps other DGK catalytic domains may function as two independent units in a coordinated fashion. They may also require other motifs for maximal activity because several DGK catalytic domains have very little DAG kinase activity when expressed as isolated subunits. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
IKEGPLLKQTSSFQRWKRRYFKLKGRKLYYAKDSKSLIFEEIDLSDASVAECSTKNVNNSFTVITPFRKL
ILCAESRKEMEEWISALKTVQQREFYE
>gnl|CDD|270094 cd13275, PH_M-RIP, Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain. M-RIP is proposed to play a role in myosin phosphatase regulation by RhoA. M-RIP contains 2 PH domains followed by a Rho binding domain (Rho-BD), and a C-terminal myosin binding subunit (MBS) binding domain (MBS-BD). The amino terminus of M-RIP with its adjacent PH domains and polyproline motifs mediates binding to both actin and Galpha. M-RIP brings RhoA and MBS into close proximity where M-RIP can target RhoA to the myosin phosphatase complex to regulate the myosin phosphorylation state. M-RIP does this via its C-terminal coiled-coil domain which interacts with the MBS leucine zipper domain of myosin phosphatase, while its Rho-BD, directly binds RhoA in a nucleotide-independent manner. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KKGWLMKQGSRQGEWSKHWFVLRGAALKYYRDPSAEEAGELDGVIDLSSCTEVTELPVSRNYGFQVKTWD
GKVYVLSAMTSGIRTNWIQALRKAAGLPSPPALP
>gnl|CDD|270095 cd13276, PH_AtPH1, Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain. AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KAGWLEKQGEFIKTWRRRWFVLKQGKLFWFKEPDVTPYSKPRGVIDLSKCLTVKSAEDATNKENAFELST
PEETFYFIADNEKEKEEWIGAIGRAIVKHSRSVTDD
>gnl|CDD|270096 cd13277, PH_Bem3, Bud emergence protein 3 (Bem3) Pleckstrin homology (PH) domain. Bud emergence in Saccharomyces cerevisiae involves cell cycle-regulated reorganizations of cortical cytoskeletal elements and requires the action of the Rho-type GTPase Cdc42. Bem3 contains a RhoGAP domain and a PH domain. Though Bem3 and Bem2 both contain a RhoGAP, but only Bem3 is able to stimulate the hydrolysis of GTP on Cdc42. Bem3 is thought to be the GAP for Cdc42. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
GDSVKEGYLLKRRKKTLGSTGGWKLRYGVLDGNILELYESRGGQLLESIKLRNAQIERQPNLPDDKYGTR
HGFLINEHKKSGLSSTTKYYLCAETDKERDEWVSALSEYID
>gnl|CDD|241432 cd13278, PH_Bud4, Bud4 Pleckstrin homology (PH) domain. Bud4 is an anillin-like yeast protein involved in the formation and the disassembly of the double ring structure formed by the septins during cytokinesis. Bud4 acts with Bud3 and and in parallel with septin phosphorylation by the p21-activated kinase Cla4 and the septin-dependent kinase Gin4. Bud4 is regulated by the cyclin-dependent protein kinase Cdk1, the master regulator of cell cycle progression. Bud4 contains an anillin-like domain followed by a PH domain. In addition there are two consensus Cdk phosphorylation sites: one at the N-terminus and one right before the C-terminal PH domain. Anillins also have C-terminal PH domains. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KSLESAQEILKKYEEQQKITKEGYLLQEGGDCEYWRRRFFKLQGTKLVAYHEVTRKPRATINLLKVVDVV
DDDDARERTSSFKRNFTDLVLFEECFRLVFANGEVIDFYADSKEEKADWYSKLKEVVELNRFHQPWVKK
>gnl|CDD|270097 cd13279, PH_Cla4_Ste20, Pleckstrin homology (PH) domain. Budding yeast contain two main p21-activated kinases (PAKs), Cla4 and Ste20. The yeast Ste20 protein kinase is involved in pheromone response, though the function of Ste20 mammalian homologs is unknown. Cla4 is involved in budding and cytokinesis and interacts with Cdc42, a GTPase required for polarized cell growth as is Pak. Cla4 and Ste20 kinases share a function in localizing cell growth with respect to the septin ring. They both contain a PH domain, a Cdc42/Rac interactive binding (CRIB) domain, and a C-terminal Protein Kinase catalytic (PKc) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VVKSGWVSVKEDGLLSFRWSKRYLVLREQSLDFYKNESSSSASLSIPLKDISNVSRTDLKPYCFEIVRKS
STKSIYISVKSDDELYDWMDDI
>gnl|CDD|270098 cd13280, PH_SIP3, Snf1p-interacting protein 3 Pleckstrin homology (PH) domain. SIP3 interacts with SNF1 protein kinase and activates transcription when anchored to DNA. It may function in the SNF1 pathway. SIP3 contain an N-terminal Bin/Amphiphysin/Rvs (BAR) domain followed by a PH domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
EKSGWLYMKTSVGKPNRTIWVRRWCFVKNGVFGMLSLSPSKTYVEETDKFGVLLCSVRYAPEEDRRFCFE
VKIFKDISIILQAETLKELKSWLTVFENAKRYALQ
>gnl|CDD|270099 cd13281, PH_PLEKHD1, Pleckstrin homology (PH) domain containing, family D (with coiled-coil domains) member 1 PH domain. Human PLEKHD1 (also called UPF0639, pleckstrin homology domain containing, family D (with M protein repeats) member 1) is a single transcript and contains a single PH domain. PLEKHD1 is conserved in human, chimpanzee, dog, cow, mouse, chicken, zebrafish, and Caenorhabditis elegans. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
GNSDDLDITTKVQLHGILWKKPFGHQSAKWSKRFFIIKEGFLLYYSESEKKDFEKTRHFNIHPKGVIPLG
GCSIEAVEDPGKPYAISISHSDFKGNIILAADSEFEQEKWLDMLRESGKITWKNAQLGETMIEELEAQG
>gnl|CDD|241436 cd13282, PH1_PLEKHH1_PLEKHH2, Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1. PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KAGYLTKLGGKVKTWKRRWFVLKNGELFYYKSPNDVIRKPQGQIALDGSCEIARAEGAQTFEIVTEKRTY
YLTADSENDLDEWIRVIQNVLRRQAS
>gnl|CDD|270100 cd13283, PH_GPBP, Goodpasture antigen binding protein Pleckstrin homology (PH) domain. The GPBP (also called Collagen type IV alpha-3-binding protein/hCERT; START domain-containing protein 11/StARD11; StAR-related lipid transfer protein 11) is a kinase that phosphorylates an N-terminal region of the alpha 3 chain of type IV collagen, which is commonly known as the goodpasture antigen. Its splice variant the ceramide transporter (CERT) mediates the cytosolic transport of ceramide. There have been additional splice variants identified, but all of them function as ceramide transport proteins. GPBP and CERT both contain an N-terminal PH domain, followed by a serine rich domain, and a C-terminal START domain. However, GPBP has an additional serine rich domain just upstream of its START domain. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LRGVLSKWTNYIHGWQDRYFVLKDGTLSYYKSESEKEYGCRGSISLSKAVIKPHEFDECRFDVSVNDSVW
YLRAESPEERQRWIDALESHKAASGYGSSS
>gnl|CDD|270101 cd13284, PH_OSBP_ORP4, Human Oxysterol binding protein and OSBP-related protein 4 Pleckstrin homology (PH) domain. Human OSBP is proposed to function is sterol-dependent regulation of ERK dephosphorylation and sphingomyelin synthesis as well as modulation of insulin signaling and hepatic lipogenesis. It contains a N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. OSBPs and Osh1p PH domains specifically localize to the Golgi apparatus in a PtdIns4P-dependent manner. ORP4 is proposed to function in Vimentin-dependent sterol transport and/or signaling. Human ORP4 has 2 forms, a long (ORP4L) and a short (ORP4S). ORP4L contains a N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP4S is truncated and contains only an OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MKGWLLKWTNYIKGYQRRWFVLSNGLLSYYRNQAEMAHTCRGTINLAGAEIHTEDSCNFVISNGGTQTFH
LKASSEVERQRWVTALELAKAKAIRLLES
>gnl|CDD|270102 cd13285, PH_ORP1, Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain. Human ORP1 has 2 forms, a long (ORP1L) and a short (ORP1S). ORP1L contains 3 N-terminal ankyrin repeats, followed by a PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains only an OSBP-related domain. ORP1L is proposed to function in motility and distribution of late endosomes, autophagy, and macrophage lipid metabolism. ORP1S is proposed to function in vesicle transport from Golgi. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCF
FTIRCFDDTVHRFKVPPKNNPVVTRKKWLEALEEHSAYSTHYCTQEQLSDDEDED
>gnl|CDD|270103 cd13286, PH_OPR5_ORP8, Human Oxysterol binding protein related proteins 5 and 8 Pleckstrin homology (PH) domain. Human ORP5 is proposed to function in efficient nonvesicular transfer of low-density lipoproteins-derived cholesterol (LDL-C) from late endosomes/lysosomes to the endoplasmic reticulum (ER). Human ORP8 is proposed to modulate lipid homeostasis and sterol regulatory element binding proteins (SREBP) activity. Both ORP5 and ORP8 contain a N-terminal PH domain, a C-terminal OSBP-related domain, followed by a transmembrane domain that localizes ORP5 to the ER. Unlike all the other human OSBP/ORPs they lack a FFAT motif (two phenylalanines in an acidic tract). Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
TLKDPSVVVLSDWLKIRGTLKSWTKLWCVLKPGVLLLYKSPKHGQWVGTVLLNACEVIERPSKKDGFCFK
LYHPLDQSIWATRGPKGESVGAITQPLPSSHLIFRAPTESDGRCWMDALELSLKCSSLLK
>gnl|CDD|270104 cd13287, PH_ORP3_ORP6_ORP7, Human Oxysterol binding protein related proteins 3, 6, and 7 Pleckstrin homology (PH) domain. Human ORP3 is proposed to function in regulating the cell-matrix and cell-cell adhesion. A proposed specific function for Human ORP6 was not found at present. Human ORP7is proposed to function in negatively regulating the Golgi soluble NSF attachment protein receptor (SNARE) of 28kDa (GS28) protein stability via sequestration of Golgi-associated ATPase enhancer of 16 kDa (GATE-16). ORP3 has 2 isoforms: the longer ORP3(1) and the shorter ORP3(2). ORP3(1), ORP6, and ORP7 all contain a N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. The shorter ORP3(2) is missing the C-terminal portion of its OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RSDDWEIMEGLKGGQTSVQEPGKQEGYLLKKRKWPLKGWHKRFFVLEKGILKYAKSPLDIAKGKLHGSID
VGLSVMSIKKKARRIDLDTEEFIYHLKVKSQDLFDSWVAKLRAHRLYRQNEIA
>gnl|CDD|270105 cd13288, PH_Ses, Sesquipedalian family Pleckstrin homology (PH) domain. The sesquipedalian family has 2 mammalian members: Ses1 and Ses2, which are also callled 7 kDa inositol polyphosphate phosphatase-interacting protein 1 and 2. They play a role in endocytic trafficking and are required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Members of this family form homodimers and heterodimers. Sesquipedalian interacts with inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein, a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network and INPP5B. Sesquipedalian contains a single PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
YATCNSPVDKEGYLWKKGERNTSYQKRWFVLKGNLLFYFEKKGDREPLGVIVLEGCTVELAEDAEPYAFA
IRFDGPGARSYVLAAENQEDMESWMKALSRASYDYLRLTVEELEKQLEEL
>gnl|CDD|241443 cd13289, PH_Osh3p_yeast, Yeast oxysterol binding protein homolog 3 Pleckstrin homology (PH) domain. Yeast Osh3p is proposed to function in sterol transport and regulation of nuclear fusion during mating and of pseudohyphal growth as well as sphingolipid metabolism. Osh3 contains a N-GOLD (Golgi dynamics) domain, a PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. GOLD domains are thought to mediate protein-protein interactions, but their role in ORPs are unknown. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
YLEGWLLKKRRKKMQGFARRYFVLNFKYGTLSYYFNPNSPVRGQIPLRLASISASPRRRTIHIDSGSEVW
HLKALNDEDFQAWMKALRKF
>gnl|CDD|241444 cd13290, PH_ORP9, Human Oxysterol binding protein related protein 9 Pleckstrin homology (PH) domain. Human ORP9 is proposed to function in regulation of Akt phosphorylation. ORP9 has 2 forms, a long (ORP9L) and a short (ORP9S). ORP9L contains an N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains a FFAT motif and an OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MEGPLSKWTNVMKGWQYRWFVLDDNAGLLSYYTSKEKMMRGSRRGCVRLKGAVVGIDDEDDSTFTITVDQ
KTFHFQARDAEERERWIRALEDTILRHSQQYQ
>gnl|CDD|270106 cd13291, PH_ORP10_ORP11, Human Oxysterol binding protein (OSBP) related proteins 10 and 11 (ORP10 and ORP11) Pleckstrin homology (PH) domain. Human ORP10 is involvedt in intracellular transport or organelle positioning and is proposed to function as a regulator of cellular lipid metabolism. Human ORP11 localizes at the Golgi-late endosome interface and is thought to form a dimer with ORP9 functioning as an intracellular lipid sensor or transporter. Both ORP10 and ORP11 contain a N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LEGQLLKYTNVVKGWQNRWFVLDPDTGILEYFLSEESKNQKPRGSLSLAGAVISPSDEDSHTFTVNAANG
EMYKLRAADAKERQEWVNRLRAVAEHHTEAIAKSNSS
>gnl|CDD|241446 cd13292, PH_Osh1p_Osh2p_yeast, Yeast oxysterol binding protein homologs 1 and 2 Pleckstrin homology (PH) domain. Yeast Osh1p is proposed to function in postsynthetic sterol regulation, piecemeal microautophagy of the nucleus, and cell polarity establishment. Yeast Osh2p is proposed to function in sterol metabolism and cell polarity establishment. Both Osh1p and Osh2p contain 3 N-terminal ankyrin repeats, a PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. OSBP andOsh1p PH domains specifically localize to the Golgi apparatus in a PtdIns4P-dependent manner. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
PPTMKGYLKKWTNYAKGYKTRWFVLEDGVLSYYRHQDDEGSACRGSINMKNARLVSDPSEKLRFEVSSKT
SGSPKWYLKANHPVEAARWIQALQKAIEWAKDE
>gnl|CDD|241447 cd13293, PH_CpORP2-like, Cryptosporidium-like Oxysterol binding protein related protein 2 Pleckstrin homology (PH) domain. There are 2 types of ORPs found in Cryptosporidium: CpORP1 and CpORP2. Cryptosporium differs from other apicomplexans like Plasmodium, Toxoplasma, and Eimeria which possess only a single long-type ORP consisting of an N-terminal PH domain followed by a C-terminal ligand binding (LB) domain. CpORP2 is like this, but CpORP1 differs and has a truncated N-terminus resulting in only having a LB domain present. The exact functions of these proteins are largely unknown though CpORP1 is thought to be involved in lipid transport across the parasitophorous vacuole membrane. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MEGYLKKWTNIFNSWKPRYFILYPGILCYSKQKGGPKKGTIHLKICDIRLVPDDPLRIIINTGTNQLHLR
ASSVEEKLKWYNALKYAQ
>gnl|CDD|241448 cd13294, PH_ORP_plant, Plant Oxysterol binding protein related protein Pleckstrin homology (PH) domain. Plant ORPs contain a N-terminal PH domain and a C-terminal OSBP-related domain. Not much is known about its specific function in plants to date. Members here include: Arabidopsis, spruce, and petunia. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VAGILYKWVNYGKGWRSRWFVLQDGVLSYYKVHGPDKVKPSGEVHLKVSSIRESRSDDKKFYIFTGTKTL
HLRAESREDRAAWLEALQAAKDMFPRMSLN
>gnl|CDD|270107 cd13295, PH_EFA6, Exchange Factor for ARF6 Pleckstrin homology (PH) domain. EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
DPNAVEYKKGYLMRKCCADPDGKKTPFGKRGWKMFYATLKGLVLYLHKDEYGCKKALRYESLRNAISVHH
SLATKATDYTKKPHVFRLRTADWREYLFQASDTKEMQSWIEAINLVAAAFSAPPLP
>gnl|CDD|270108 cd13296, PH2_MyoX, Myosin X Pleckstrin homology (PH) domain, repeat 2. MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the second PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KSGWLTKKGGGSSTLSRRNWKSRWFVLRDTVLKYYENDQEGEKLLGTIDIRSAKEIVDNDPKENRLSITT
EERTYHLVAESPEDASQWVNVLTRVISATDLEL
>gnl|CDD|270109 cd13297, PH3_MyoX-like, Myosin X-like Pleckstrin homology (PH) domain, repeat 3. MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the third MyoX PH repeat. PLEKHH3/Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) member 3 is also part of this CD and like MyoX contains a FERM domain, a MyTH4 domain, and a single PH domain. Not much is known about the function of PLEKHH3. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RPKGDLDEGGQDVIERGWLYKEGGKGGARGNLTKKKRWFVLTGNSLDYYKSSEKNSLKLGTLVLNSLCSV
VPPDEKMAKETGYWTFTVHGRKHSFRLYTKLQEEAMRWVNAIQDVIDSKPPIETPT
>gnl|CDD|270110 cd13298, PH1_PH_fungal, Fungal proteins Pleckstrin homology (PH) domain, repeat 1. The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
FEFDRVLKSGYLLKRSRKTKNWKKRWVVLRPCQLSYYKDEKEYKLRRVINLSELLAVAPLKDKKRKNVFG
IYTPSKNLHFRATSEKDANEWVEALREEFRLDDEEE
>gnl|CDD|270111 cd13299, PH2_PH_fungal, Fungal proteins Pleckstrin homology (PH) domain, repeat 2. The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the second PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
DDPERVIEQGYLQVLKKKGVNQWKKYWLVLRNRSLSFYKDQSEYSPVKIIPIDDIIDVVELDPLSKSKKW
CLQIITPEKRIRFCADDEESLIKWLGALKSLL
>gnl|CDD|270112 cd13300, PH1_TECPR1, Tectonin beta-propeller repeat-containing protein 1 Pleckstrin homology (PH) domain, repeat 1. TECPR1 is a tethering factor involved in autophagy. It promotes the autophagosome fusion with lysosomes by associating with both the ATG5-ATG12 conjugate and phosphatidylinositol-3-phosphate (PtdIns3P) present at the surface of autophagosomes. TECPR1 is also involved in selective autophagy against bacterial pathogens, by being required for phagophore/preautophagosomal structure biogenesis and maturation. It contains 2 DysFN (Dysferlin domains of unknown function, N-terminal), 2 Hyd_WA domains that is a probably beta-propeller, a PH-like domain, a TECPR domain, and a DysFC (C-terminal). The PH domain mediates the binding to phosphatidylinositol-3-phosphate (PtdIns3P). Binding to the ATG5-ATG12 conjugate exposes the PH domain, allowing the association with PtdIns3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPV
NNGGEKPSFAIYTPKRTKQRWPIRLAANTEQELEDWLSLLSMSCCEVRGIQG
>gnl|CDD|270113 cd13301, PH1_Pleckstrin_2, Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1. Pleckstrin is a protein found in platelets. This name is derived from platelet and leukocyte C kinase substrate and the KSTR string of amino acids. Pleckstrin 2 contains two PH domains and a DEP (dishvelled, egl-10, and pleckstrin) domain. Unlike pleckstrin 1, pleckstrin 2 does not contain obvious sites of PKC phosphorylation. Pleckstrin 2 plays a role in actin rearrangement, large lamellipodia and peripheral ruffle formation, and may help orchestrate cytoskeletal arrangement. The PH domains of pleckstrin 2 are thought to contribute to lamellipodia formation. This cd contains the first PH domain repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
PGIIKEGYLVKKGHVVNNWKARWFVLKEDGLEYYKKKTDSSPKGMIPLKGCTITSPCLEYGKRPLVFKLT
TAKGQEHFFQACSREERDAWAKDITKAITCLEGGKRFA
>gnl|CDD|270114 cd13302, PH2_Pleckstrin_2, Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 2. Pleckstrin is a protein found in platelets. This name is derived from platelet and leukocyte C kinase substrate and the KSTR string of amino acids. Pleckstrin 2 contains two PH domains and a DEP (dishvelled, egl-10, and pleckstrin) domain. Unlike pleckstrin 1, pleckstrin 2 does not contain obvious sites of PKC phosphorylation. Pleckstrin 2 plays a role in actin rearrangement, large lamellipodia and peripheral ruffle formation, and may help orchestrate cytoskeletal arrangement. The PH domains of pleckstrin 2 are thought to contribute to lamellipodia formation. This cd contains the second PH domain repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
EEFRGIIVKQGCLLKQGHRRKNWKVRKFVLRDDPAYLHYYDPAKGEDPLGAIHLRGCVVTAVEDNSNPRK
GSVEGNLFEIITADEVHYYLQAATPAERTEWIKAIQMAS
>gnl|CDD|241457 cd13303, PH1-like_Rtt106, Pleckstrin homology-like domain, repeat 1, of Histone chaperone RTT106 (regulator of Ty1 transposition protein 106). Rtt106 is a histone chaperone. The binding of Rtt106 to H3K56-acetylated (H3-H4)2 tetramers contributes to nucleosome assembly in terms of DNA replication, gene silencing and maintenance of genomic stability. Rtt106 contains an N-terminal homodimerization domain and two C-terminal pleckstrin-homology (PH) domains (PH1 and PH2). The N-terminal domain homodimerizes homodimerizes and interacts with H3-H4 independently of acetylation while the double PH domain binds the K56-containing region of H3. Rtt106 also interacts with both the SWI/SNF and RSC chromatin remodeling complexes and is involved in their cell-cycle dependent recruitment to histone gene pairs regulated by the HIR co-repressor complex (HTA1-HTB1, HHT1-HHF1, and HHT2-HHF2). This model contains the first PH-like domain repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VDESNVIFKLKDVSVLSPLRKKLNLVLHLSSVDGKPMLSLLKDNVIELSITNLKTNVKMATFLPVPEKPN
LVYLFINYKKSNDDKYTDPVLITLNKEATLKQFKESGLLDQEVSDFSKCIEYMRKQAILTGFRISDPFS
>gnl|CDD|241458 cd13304, PH2-like_Rtt106, Pleckstrin homology-like domain, repeat 2, of Histone chaperone RTT106 (regulator of Ty1 transposition protein 106). Rtt106 is a histone chaperone. Rtt106 contains an N-terminal homodimerization domain and two C-terminal pleckstrin-homology (PH) domains (PH1 and PH2). The binding of Rtt106 to H3K56-acetylated (H3-H4)2 tetramers contributes to nucleosome assembly in terms of DNA replication, gene silencing and maintenance of genomic stability. The N-terminal domain homodimerizes homodimerizes and interacts with H3-H4 independently of acetylation while the double PH domain binds the K56-containing region of H3. Rtt106 also interacts with both the SWI/SNF and RSC chromatin remodeling complexes and is involved in their cell-cycle dependent recruitment to histone gene pairs regulated by the HIR co-repressor complex (HTA1-HTB1, HHT1-HHF1, and HHT2-HHF2). This model contains the second PH-like domain repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VNKLFHVEAHKGAKEGVLLFLQDYIIFGFKKPILLFDISQIESISYSNITRLTFNLNLTVKNAKKEEETL
EFSMIDQAFFQVIDDFIKR
>gnl|CDD|270115 cd13305, PH_SHARPIN, SHANK-associated RH domain interacting protein Pleckstrin homology (PH) domain. SHARPIN has a variety of roles including: a role as a scaffolding partner of anchoring/scaffold proteins Shank1, a role in carcinogenesis through the interaction with FYN binding protein (FYB), which binds to oncogene FYN, a role in apoptosis by interacting with AIFM1, a mitochondrial regulator of cell death, CAPN13, and NSD1, as well as a role in immune disease and inflammation. SHARPIN has at its N-terminus a PH domain, followed by a E3 ubiquitin ligase domain, and a C-terminal RanBP-type and C3HC4-type zinc finger containing 1 domain (RBCK1, also known as HOIP which functions as a protein kinase C (PKC) binding protein as well as a transcriptional activator. SHARPIN's PH domain functions as a dimerization module, rather than a ligand recognition domain. Instead it acts as a dimerization module extending the functional applications of this superfold. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
AVEEAVVHSEVRPLGPGSPPAPDGLLRLQLSADPARPGRFRLALQGAGDSGPPGEGLEWPLKSVSYEVKT
PTCHELQPPKPPPDALSFHFQDEQEAQRWATVVERALREAQRGT
>gnl|CDD|270116 cd13306, PH1_AFAP, Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 1. There are 3 members of the AFAP family of adaptor proteins: AFAP1, AFAP1L1, and AFAP1L2/XB130. AFAP1 is a cSrc binding partner and actin cross-linking protein. AFAP1L1 is thought to play a similar role to AFAP1 in terms of being an actin cross-linking protein, but it preferentially binds to cortactin and not cSrc, thereby playing a role in invadosome formation. AFAP1L2 is a cSrc binding protein, but does not bind to actin filaments. AFAP1L2 acts as an intermediary between the RET/PTC kinase and PI-3kinase pathway in the thyroid. The AFAPs share a similar structure of a SH3 binding motif, 3 SH2 binding motifs, 2 PH domains, a coiled-coil region corresponding to the AFAP1 leucine zipper, and an actin binding domain. The amino terminal PH1 domain of AFAP1 has been known to function in intra-molecular regulation of AFAP1. In addition, the PH1 domain is a binding partner for PKCa and phospholipids. This cd is the first PH domain of AFAP. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SEEASMELVKDARICAFLLRKKRFGQWAKQLCVIKDNRLLCYKSSKDQQPQLELPLLGCSVIYVPKDGRR
KKHELKFTPPGAEALVLAVQSKEQAEQWLKVIREVSS
>gnl|CDD|270117 cd13307, PH2_AFAP, Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 2. There are 3 members of the AFAP family of adaptor proteins: AFAP1, AFAP1L1, and AFAP1L2/XB130. AFAP1 is a cSrc binding partner and actin cross-linking protein. AFAP1L1 is thought to play a similar role to AFAP1 in terms of being an actin cross-linking protein, but it preferentially binds to cortactin and not cSrc, thereby playing a role in invadosome formation. AFAP1L2 is a cSrc binding protein, but does not bind to actin filaments. AFAP1L2 acts as an intermediary between the RET/PTC kinase and PI-3kinase pathway in the thyroid. The AFAPs share a similar structure of a SH3 binding motif, 3 SH2 binding motifs, 2 PH domains, a coiled-coil region corresponding to the AFAP1 leucine zipper, and an actin binding domain. This cd is the second PH domain of AFAP. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
GVPTCGYLNVLVNQQWRSRWCCVKDGQLHFYQDRNKTKSPQQSLPLHGCEVVPGPDPKHPYSFRILRNGE
EVAALEASSSEDMGRWLGVLLAETGSATDPE
>gnl|CDD|270118 cd13308, PH_3BP2, SH3 domain-binding protein 2 Pleckstrin homology (PH) domain. SH3BP2 (the gene that encodes the adaptor protein 3BP2), HD, ITU, IT10C3, and ADD1 are located near the Huntington's Disease Gene on Human Chromosome 4pl6.3. SH3BP2 lies in a region that is often missing in individuals with Wolf-Hirschhorn syndrome (WHS). Gain of function mutations in SH3BP2 causes enhanced B-cell antigen receptor (BCR)-mediated activation of nuclear factor of activated T cells (NFAT), resulting in a rare, genetic disorder called cherubism. This results in an increase in the signaling complex formation with Syk, phospholipase C-gamma2 (PLC-gamma2), and Vav1. It was recently discovered that Tankyrase regulates 3BP2 stability through ADP-ribosylation and ubiquitylation by the E3-ubiquitin ligase. Cherubism mutations uncouple 3BP2 from Tankyrase-mediated protein destruction, which results in its stabilization and subsequent hyperactivation of the Src, Syk, and Vav signaling pathways. SH3BP2 is also a potential negative regulator of the abl oncogene. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
QLLTLPRDVIHSGTLTKKGGSQKTLQNWQLRYVIIHQGCVYYYKNDQSAKPKGVFSLNGYNRRAAEERTS
KLKFVFKIIHLSPDHRTWYFAAKSEDEMSEWMEYIRREIDHYC
>gnl|CDD|270119 cd13309, PH_SKIP, SifA and kinesin-interacting protein Pleckstrin homology (PH) domain. SKIP (also called PLEKHM2/Pleckstrin homology domain-containing family M member 2) is a soluble cytosolic protein that contains a RUN domain and a PH domain separated by a unstructured linker region. SKIP is a target of the Salmonella effector protein SifA and the SifA-SKIP complex regulates kinesin-1 on the bacterial vacuole. The PH domain of SKIP binds to the N-terminal region of SifA while the N-terminus of SKIP is proposed to bind the TPR domain of the kinesin light chain. The opposite side of the SKIP PH domain is proposed to bind phosphoinositides. TSifA, SKIP, SseJ, and RhoA family GTPases are also thought to promote host membrane tubulation. Recently, it was shown that the lysosomal GTPase Arl8 binds to the kinesin-1 linker SKIP and that both are required for the normal intracellular distribution of lysosomes. Interestingly, two kinesin light chain binding motifs (WD) in SKIP have now been identified to match a consensus sequence for a kinesin light chain binding site found in several proteins including calsyntenin-1/alcadein, caytaxin, and vaccinia virus A36. SKIP has also been shown to interact with Rab1A. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
TKEGMLMYKTGTSYLGGETWKPGYFLLKNGVLYQYPDRSDRLPLLSISLGGEQCGGCRRINNTERPHTFE
LILTDRSSLELAAPDEYEASEWLQSLCQSASGG
>gnl|CDD|270120 cd13310, PH_RalGPS1_2, Ral GEF with PH domain and SH3 binding motif 1 and 2 Pleckstrin homology (PH) domain. RalGPS1 (also called Ral GEF with PH domain and SH3 binding motif 1;RALGEF2/ Ral guanine nucleotide exchange factor 2; RalA exchange factor RalGPS1; Ral guanine nucleotide exchange factor RalGPS1A2; ras-specific guanine nucleotide-releasing factor RalGPS1) and RalGPS2 (also called Ral GEF with PH domain and SH3 binding motif 2; Ral-A exchange factor RalGPS2; ras-specific guanine nucleotide-releasing factor RalGPS22). They activate small GTPase Ral proteins such as RalA and RalB by stimulating the exchange of Ral bound GDP to GTP, thereby regulating various downstream cellular processes. Structurally they contain an N-terminal Cdc25-like catalytic domain, followed by a PXXP motif and a C-terminal PH domain. The Cdc25-like catalytic domain interacts with Ral and its PH domain ensures the correct membrane localization. Its PXXP motif is thought to interact with the SH3 domain of Grb2. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
TMQGCLRRKTVLKEGRKPTVSSWQRYWVQLWGTSLVYYAPKSLKGTERSDFKSEPCKIVSISGWMVVLGD
DPEHPDSFQLTDPEKGNVYKFRAGSRSNALLWLKHLKDACKGNRPP
>gnl|CDD|270121 cd13311, PH_Slm1, Slm1 Pleckstrin homology (PH) domain. Slm1 is a component of the target of rapamycin complex 2 (TORC2) signaling pathway. It plays a role in the regulation of actin organization and is a target of sphingolipid signaling during the heat shock response. Slm1 contains a single PH domain that binds PtdIns(4,5)P2, PtdIns(4)P, and dihydrosphingosine 1-phosphate (DHS-1P). Slm1 possesses two binding sites for anionic lipids. The non-canonical binding site of the PH domain of Slm1 is used for ligand binding, and it is proposed that beta-spectrin, Tiam1 and ArhGAP9 also have this type of phosphoinositide binding site. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
TKPLISGILERKSKFLKSYSKGYYVLTPAGYLHEFKSSDRKKDPAPEMSLYLPECKIGAPSNKGSKSHKF
ILKGKDVGSGKFHRGHEWVFKAESHEEMMAWWEDIKELTK
>gnl|CDD|270122 cd13312, PH_USP37_like, Pleckstrin homology-like domain of Ubiquitin carboxyl-terminal hydrolase 37. Members here include USP37, USP29, and USP26. All of these contain a single PH-like domain. USP37 (also called ubiquitin carboxyl-terminal hydrolase 37, ubiquitin thiolesterase 37, deubiquitinating enzyme 37, and tmp_locus_50) is a deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), resulting in promoting S phase entry. USP37 mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex and 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2). USP29 (also called ubiquitin carboxyl-terminal hydrolase 29, ubiquitin thiolesterase 29, deubiquitinating enzyme 29, and HOM-TES-84/86) plays a role in apoptosis and oxidative stress. In response to oxidative stress, JTV1 dissociates from the ARS complex, translocates to the nucleus, associates with far upstream element binding protein (FBP) and co-activates the transcription of USP29 which binds to, cleaves poly-ubiquitin chains from, and stabilizes p53 leading to apoptosis. The X-linked deubiquitination enzyme USP26 (also called ubiquitin carboxyl-terminal hydrolase 26, ubiquitin thiolesterase 26, and deubiquitinating enzyme 26) is a regulator of androgen receptor (AR) signaling. It binds to AR using three nuclear receptor interaction motifs (LXXLL, FXXLF and FXXFF) and modulates AR ubiquitination. Polymorphism of Usp26 correlates with idiopathic male infertility. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LKIHGFVQIWSKKTGMTKWKEAFIEIVEGKKKVKLVVYFKTGGKPKTFQLSNNIKSVVLRSYGGNQNHLH
LTLKNNSFLFIDKLSSTDAEQLKEFLDKVHQKK
>gnl|CDD|270123 cd13313, PH_NF1, Neurofibromin-1 Pleckstrin homology-like domain. Neurofibromin (NF1) contains a N-terminal RasGAP domain, followed by a Sec14-like domain, and a PH domain. Surprisingly, in neurofibromin the PH domain alone is not sufficient for phospholipid binding and instead requires the presence of the Sec-14 domain. The Sec-14 domain has been shown to bind 1-(3-sn-phosphatidyl)-sn-glycerol (PtdGro), (3-sn-phosphatidyl)-ethanolamine (PtdEtn) and -choline (PtdCho) and to a minor extent to (3-sn-phosphatidyl)-l-serine (PtdSer) and 1-(3-sn-phosphatidyl)-d-myo-inositol (PtdIns). Neurofibromatosis type 1 (also known as von Recklinghausen neurofibromatosis or NF1) is a genetic disorder caused by alterations in the tumor suppressor gene NF1. Hallmark symptoms include neural crest derived tumors, pigmentation anomalies, bone deformations, and learning disabilities. Mutations of the tumour suppressor gene NF1 are responsible for disease pathogenesis, with 90% of the alterations being nonsense codons. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
AATLALEEDLKVFNNALKLSHKDTKVAIKVGPTAIQVTSAEKTKVLGHSVLLNDVYYASEIEEVCLVDDN
QFTLTIANEGGPLSFMHNDCEAIVQAIIHIRTRWELSQPD
>gnl|CDD|270124 cd13314, PH_Rpn13, Pleckstrin homology-like domain of Regulatory Particle Non-ATPase 13. Targeted protein degradation is performed to a great extent by the ubiquitin-proteasome pathway, in which substrate proteins are marked by covalently attached ubiquitin chains that mediate recognition by the proteasome. Rpn13(also called ADRM1/ARM1) is one of the two major ubiquitin receptors of the proteasome, the other being S5a/Rpn10 which is not essential for ubiquitin-mediated protein degradation in budding yeast2. S5a has two ubiquitin interacting motifs (UIMs) that bind simultaneously to ubiquitin moieties to increase affinity while Rpn13 binds ubiquitin with a single, high affinity surface within its N-terminal PH domain. Rpn13 also binds and activates deubiquitinating enzyme Uch37, one of the proteasome's three deubiquitinating enzymes. Recently it was discovered that the ubiquitin-binding domain (BD) and Uch37 BD of human (h) Rpn13 pack against each other when it is not incorporated into the proteasome reducing hRpn13's affinity for ubiquitin. However when hRpn13 binds to hRpn2/S1 this abrogates its interdomain interactions, thus activating hRpn13 for ubiquitin binding. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VEFKAGKMTLKGTTVTPDPRKGLVYLQQGDDGLIHFCWKDRTSGAVEDDLIIFPDDAEFEKVPQCTTGRV
YVLKFKSSSQKHFFWMQEPSTDKDEEICKKVNELL
>gnl|CDD|270125 cd13315, PH_Sec3, Sec 3 Pleckstrin homology-like domain. The Sec3 subunit of the exocyst, a complex involved in polarized exocytosis, bind phospholipids and GTPase Cdc42 and therefore functions as a coincidence detector at the plasma membrane. Unlike most PH domains, Sec3 contains an additional alpha-helix at its N-terminus and two beta-strands at its C-terminus that mediate dimerization through domain swapping. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
YEDIRQRIISSLFSKRDADGALDESYITHVKIIEDSHYPSSRKLGNKKPRYLILSVKKSGRVRLHKSKEN
SNGSFSIGKTWDLDELRAIEVDPPTGFILTLGKTYYWQTESPKERTVFLASLVTSYRKYTGGKVPLLVGF
D
>gnl|CDD|270126 cd13316, PH_Boi, Boi family Pleckstrin homology domain. Yeast Boi proteins Boi1 and Boi2 are functionally redundant and important for cell growth with Boi mutants displaying defects in bud formation and in the maintenance of cell polarity.They appear to be linked to Rho-type GTPase, Cdc42 and Rho3. Boi1 and Boi2 display two-hybrid interactions with the GTP-bound ("active") form of Cdc42, while Rho3 can suppress of the lethality caused by deletion of Boi1 and Boi2. These findings suggest that Boi1 and Boi2 are targets of Cdc42 that promote cell growth in a manner that is regulated by Rho3. Boi proteins contain a N-terminal SH3 domain, followed by a SAM (sterile alpha motif) domain, a proline-rich region, which mediates binding to the second SH3 domain of Bem1, and C-terminal PH domain. The PH domain is essential for its function in cell growth and is important for localization to the bud, while the SH3 domain is needed for localization to the neck. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
DHSGWMKKRGERYGTWKTRYFVLKGTRLYYLKSENDDKEKGLIDLTGHRVVPDDSNSPFRGSYGFKLVPP
AVPKVHYFAVDEKEELREWMKALMKAT
>gnl|CDD|270127 cd13317, PH_PLEKHO1_PLEKHO2, Pleckstrin homology domain-containing family O Pleckstrin homology domain. The PLEKHO family members are PLEKHO1 (also called CKIP-1/Casein kinase 2-interacting protein 1/CK2-interacting protein 1) and PLEKHO2 (PLEKHQ1/PH domain-containing family Q member 1). They both contain a single PH domain. PLEKHO1 acts as a scaffold protein that functions in plasma membrane recruitment, transcriptional activity modulation, and posttranscriptional modification regulation. As an adaptor protein it is involved in signaling pathways, apoptosis, differentiation, cytoskeleton, and bone formation. Not much is know about PLEKHO2. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
GAPQPEKAGWIKKSSGGLLGIWKDRYVVLKGTQLLVYEKEEKVFDLEDYELCEYLRCSKSRASKKNKSRF
TLIRSKQPGNKAPDLKFQAVSPEEKESWINAL
>gnl|CDD|270128 cd13318, PH_IQSEC, IQ motif and SEC7 domain-containing protein family Pleckstrin homology domain. The IQSEC (also called BRAG/Brefeldin A-resistant Arf-gunanine nucleotide exchange factor) family are a subset of Arf GEFs that have been shown to activate Arf6, which acts in the endocytic pathway to control the trafficking of a subset of cargo proteins including integrins and have key roles in the function and organization of distinct excitatory and inhibitory synapses in the retina. The family consists of 3 members: IQSEC1 (also called BRAG2/GEP100), IQSEC2 (also called BRAG1), and IQSEC3 (also called SynArfGEF, BRAG3, or KIAA1110). IQSEC1 interacts with clathrin and modulates cell adhesion by regulating integrin surface expression and in addition to Arf6, it also activates the class II Arfs, Arf4 and Arf5. Mutations in IQSEC2 cause non-syndromic X-linked intellectual disability as well as reduced activation of Arf substrates (Arf1, Arf6). IQSEC3 regulates Arf6 at inhibitory synapses and associates with the dystrophin-associated glycoprotein complex and S-SCAM. These members contains a IQ domain that may bind calmodulin, a PH domain that is thought to mediate membrane localization by binding of phosphoinositides, and a SEC7 domain that can promote GEF activity on ARF. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
PHRRLVCYCRLYEVPDPNKREKPGLHQREVFLFNDLLVVTKIFSKKKSSVTYSFRQSFSLLGMQVLLFET
SHYPFGIRLTSPLDNKVLITFNARNESDRKKFVEDLRESILEVNEMESLRIEEELEKQ
>gnl|CDD|270129 cd13319, PH_RARhoGAP, RA and RhoGAP domain-containing protein Pleckstrin homology PH domain. RARhoGAP (also called Rho GTPase-activating protein 20 and ARHGAP20) is thought to function in rearrangements of the cytoskeleton and cell signaling events that occur during spermatogenesis. RARhoGAP was also shown to be activated by Rap1 and to induce inactivation of Rho, resulting in the neurite outgrowth. Recent findings show that ARHGAP20, even although it is located in the middle of the MDR on 11q22-23, is expressed at higher levels in chronic lymphocytic leukemia patients with 11q22-23 and/or 13q14 deletions and its expression pattern suggests a functional link between cases with 11q22-23 and 13q14 deletions. The mechanism needs to be further studied. RARhoGAP contains a PH domain, a Ras-associating domain, a Rho-GAP domain, and ANXL repeats. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RTFLLEGPVQLTRGLQTQERHLFLFSDVLVVAKPKSKNSFKLKHKIRLSELWLASCVDEVCEGSKSADKS
FVLGWPTTNFVATFSSQEEKDLWLSFL
>gnl|CDD|270130 cd13320, PH_OCRL-like, oculocerebrorenal syndrome of Lowe family Pleckstrin homology-like domain. The OCRL family has two members: OCRL1 (also called INPP5F, LOCR, NPHL2, or phosphatidylinositol polyphosphate 5-phosphatase) and OCRL2 (also called IPNNB5, inositol polyphosphate-5-phosphatase, phosphoinositide 5-phosphatase, 5PTase, or type II inositol-1,4,5-trisphosphate 5-phosphatase). The OCRL proteins hydrolyze phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events. They interact with APPL1, FAM109A and FAM109B and several Rab GTPases which might both target them to the specific membranes and as well as stimulating the phosphatase activity. All OCRL family members contain a PH domain and a Rho-GAP domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
CVAAVQGVLCKGGSREPRLLSLAQRRGQYALIIQSHEREASLQDIIPINSHFRCVQEAEETLLIDIASNS
GCKIRLQGDETLERLFEIPDEEHCLTFLSEVLAAQ
>gnl|CDD|241475 cd13321, PH_PLEKHM1, Pleckstrin homology domain-containing family M member 1 Pleckstrin homology (PH) domain. PLEKHM1 is thought to function in vesicular transport in osteoclasts. Mutations in the PLEKHM1 gene are associated with osteopetrosis OPTB6. PLEKHM1 contains an N-terminal RUN domain (RPIP8/RaP2 interacting protein 8, UNC-14 and NESCA/new molecule containing SH3 at the carboxyl-terminus), followed by a PH domain, and either a C1 domain or a DUF4206 domain at its C-terminus. The RUN domain is thought to be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
QASPAPSQGPLSEPSQVQKPFSVVHRRQMGLSNPFRGLLKLGTLERRGAMGIWKEFYCELSPLEFRLYLS
AEERVCVENCSLLRCESVGPAHSDGRFELVFPGKKLALRAPSRDEAEDWLDRIREALQKVRP
>gnl|CDD|270131 cd13322, PH_PHLPP-like, PH domain leucine-rich repeat protein phosphatase family Pleckstrin homology-like domain. The PHLPP family has members PHLPP1 (also called hSCOP/Suprachiasmatic nucleus circadian oscillatory protein; PLEKHE1/Pleckstrin homology domain-containing family E member 1) and PHLPP2 (PHLPP-like/PHLPPL). The PHLPP family of novel Ser/Thr phosphatases serve as important regulators of cell survival and apoptosis. PHLPP isozymes catalyze the dephosphorylation of a conserved regulatory motif, the hydrophobic motif, on the AGC kinases Akt, PKC, and S6 kinase, as well as an inhibitory site on the kinase Mst1, to inhibit cellular proliferation and induce apoptosis and negatively regulates ERK1/2 activation. Reductions in their expression have been detected in several cancers and linked to cancer progression. PHLPP1 and PHLPP2 both contain an N-terminal PH domain, followed by 21 LRR (leucine-rich) repeats, and a C-terminal PP2C-like domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
ERILLSGIYNVRKGKTQLHKWAERQVILCGTCLIVSSVKDSQTGKMHILPLVGGKVEEVKRRQHCLAFSS
AGPQAQTYYVSFDTLAEYQRWHRQA
>gnl|CDD|270132 cd13323, PH_PLEKHN1, Pleckstrin homology domain containing family N member 1Pleckstrin homology-like domain. Not much is known about PLEKHN1. It is found in a wide range of animals including humans, green anole, frog, and zebrafish. It contains a single PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RESLGSITCVSKVKLQHLPFQEQHDRLLVLYPSSLIILSEESDGLCFKGELPLNAIQVNFEENEKKIRSF
LIEGRLINTIRVSCLSYEDYQDWILCLKTAQVRNGDSSLPGSSSFYGSTQP
>gnl|CDD|270133 cd13324, PH_Gab-like, Grb2-associated binding protein family Pleckstrin homology (PH) domain. Gab proteins are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. There are 3 families: Gab1, Gab2, and Gab3. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VVYEGWLTKSPPEKKIWRAAWRRRWFVLRSGRLSGGQDVLEYYTDDHCKKLKGIIDLDQCEQVDAGLTFE
KKKFKNQFIFDIRTPKRTYYLVAETEEEMNKWVRCICQVCGF
>gnl|CDD|270134 cd13325, PH_unc89, unc89 pleckstrin homology (PH) domain. unc89 is a myofibrillar protein. unc89-B the largest isoform is composed of 53 immunoglobulin (Ig) domains, 2 Fn3 domains, a triplet of SH3, DH and PH domains at its N-terminus, and 2 protein kinase domains (PK1 and PK2) at its C-terminus. unc-89 mutants display disorganization of muscle A-bands, and usually lack M-lines. The COOH-terminal region of obscurin, the human homolog of unc89, interacts via two specific Ig-like domains with the NH(2)-terminal Z-disk region of titin, a protein that connects the Z line to the M line in the sarcomere and contributes to the contraction of striated muscle. obscurin is also thought to be involved in Ca2+/calmodulin via its IQ domains, as well as G protein-coupled signal transduction in the sarcomere via its RhoGEF/DH domain. The DH-PH region of OBSCN and unc89, the C. elegans homolog, has exchange activity for RhoA and Rho-1 respectively, but not for the small GTPases homologous to Cdc42 or Rac. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
GNIHKLGRLLRHDWFTVTDGEGKAKERYLFLFKSRILITKVRRISEDRSVFILKDIIRLPEVNVKQHPDD
ERTFELQPKLPAFGILPIDFKAHKDEIKDYWLNEIEEYANDYVA
>gnl|CDD|270135 cd13326, PH_CNK_insect-like, Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain. CNK family members function as protein scaffolds, regulating the activity and the subcellular localization of RAS activated RAF. There is a single CNK protein present in Drosophila and Caenorhabditis elegans in contrast to mammals which have 3 CNK proteins (CNK1, CNK2, and CNK3). All of the CNK members contain a sterile a motif (SAM), a conserved region in CNK (CRIC) domain, and a PSD-95/DLG-1/ZO-1 (PDZ) domain, and a PH domain. A CNK2 splice variant CNK2A also has a PDZ domain-binding motif at its C terminus and Drosophila CNK (D-CNK) also has a domain known as the Raf-interacting region (RIR) that mediates binding of the Drosophila Raf kinase. This cd contains CNKs from insects, spiders, mollusks, and nematodes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
YQGWLYQRRRKGKGGGKWAKRWFVLKGSNLYGFRSQESTKADCVIFLPGFTVSPAPEVKSRKYAFKVYHT
GTVFYFAAESQEDMKKWLDLL
>gnl|CDD|270136 cd13327, PH_PLEKHM3_2, Pleckstrin homology domain-containing family M member 3 Pleckstrin homology domain 2. PLEKHM3 (also called differentiation associated protein/DAPR)(also called differentiation associated protein/DAPR) exists as three alternatively spliced isoforms that participate in metal ion binding. It contains 2 PH domains and 1 phorbol-ester/DAG-type zinc finger domain. PLEKHM3 is found in Humans, canines, bovine, mouse, rat, chicken and zebrafish. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KSGTLYRLTVQNNWKAFTFVLSRSYLMAFQPGCLDEDPLLSYNVDVCLAVQMDMLDGCDSCFQVIFPQDV
LRLRAETRQRAQEWMEAL
>gnl|CDD|275410 cd13328, PH1_FDG_family, FYVE, RhoGEF and PH domain containing/faciogenital dysplasia family proteins, N-terminal Pleckstrin homology (PH) domain. In general, FGDs have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain. Mutations in the FGD1 gene are responsible for the X-linked disorder known as faciogenital dysplasia (FGDY). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KEGQILKLSAKNGTPQPRYLFLFNDMLLYCVPKLSLVGQKFSVRNRLDVAGMKVREPVNENYPHTFKISG
KERSLELQASSAEEKDEWIQAI
>gnl|CDD|275411 cd13329, PH_RhoGEF, Rho guanine nucleotide exchange factor Pleckstrin homology domain. RhoGEFs belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. The members here all contain Dbl homology (DH)-PH domains. In addition some members contain N-terminal C1 (Protein kinase C conserved region 1) domains, PDZ (also called DHR/Dlg homologous regions) domains, ANK (ankyrin) domains, and RGS (Regulator of G-protein signalling) domains or C-terminal ATP-synthase B subunit. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. RhoGEF2/Rho guanine nucleotide exchange factor 2, p114RhoGEF/p114 Rho guanine nucleotide exchange factor, p115RhoGEF, p190RhoGEF, PRG/PDZ Rho guanine nucleotide exchange factor, RhoGEF 11, RhoGEF 12, RhoGEF 18, AKAP13/A-kinase anchoring protein 13, and LARG/Leukemia-associated Rho guanine nucleotide exchange factor are included in this CD. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LIHEGPLTWKVARGKLIEVHVLLLEDLLVLLQKQDDKYLLKLHLTGSFDSKDTKSPVIKLSTLLVREVAT
DKKAFFLISTSKNGPQMYELVANSSSERKTWIKHISDAV
>gnl|CDD|241484 cd13330, PH_CARM1, Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain. CARM1 (also known as protein arginine methyltransferase 4/PRMT4) is a protein arginine methyltransferase recruited by several transcription factors. It methylates a variety of proteins and plays a role in gene expression. The N-terminal domain of CARM1 contains a N-terminal PH domain, a catalytic core module composed of two parts (a Rossmann fold topology (RF) and a beta-barrel), and a C-terminal domain. The N-terminal and the C-terminal end of CARM1 catalytic module contain molecular switches that may explain how CARM1 regulates its biological activities by protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSVLVLSTNEDVCVFKCSVNRETECSRVGKQSFLITL
GCNSVLLQFATPSEFSSFYNALKNCRGQTNEKSVFSQ
>gnl|CDD|270139 cd13331, PH_Avo1, Avo1 Pleckstrin homology (PH) domain. Target of rapamycin (TOR) is a highly conserved serine/threonine protein kinase and a central controller of the growth, metabolism and ageing of eukaryotic cells. TOR assembles into two protein complexes termed TOR complex 1 (TORC1) and TOR complex 2 (TORC2) which function as central nodes in a complex network of signal transduction pathways that are involved in normal physiological as well as pathogenic events. TORC1 mediates the rapamycin-sensitive signalling branch, which positively regulates anabolic processes and negatively regulates catabolic processes. TORC2 signalling is rapamycinin insensitive and is involved in the spatial aspects of cell growth by controlling the actin cytoskeleton and cell polarity. In Saccharomyces cerevisiae, TORC2 is involved in the regulation of ceramide metabolism. In S. cerevisiae, TORC1 consists of the proteins Kog1, Lst8, Tco89 and either Tor1 or Tor2, while TORC2 consists of the proteins Avo1, Avo2, Avo3, Bit61, Lst8 and Tor2. The C-terminal domain of the Saccharomyces cerevisiae TORC2 component Avo1 is required for plasma-membrane localization of TORC2 and is essential for yeast viability. The C-termini of Avo1 and Sin1, its Human ortholog, both have the pleckstrin homology (PH) domain fold. Comparison with known PH-domain structures suggests a putative binding site for phosphoinositides. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
YKSFKVSMIHRLRFTTDVQLGISGDKVEIDPVTNQKHSTKFWIKQKPISIDSSLLCACDLSEEKSPSHAH
FKITYLSNHDYKHLYFESDAATVNEIVLKVNYILESRA
>gnl|CDD|275412 cd13332, FERM_C_JAK1, FERM domain C-lobe of Janus kinase 1. JAK1 is a tyrosine kinase protein essential in signaling type I and type II cytokines. It interacts with the gamma chain of type I cytokine receptors to elicit signals from the IL-2 receptor family, the IL-4 receptor family, the gp130 receptor family, ciliary neurotrophic factor receptor (CNTF-R), neurotrophin-1 receptor (NNT-1R) and Leptin-R). It also is involved in transducing a signal by type I (IFN-alpha/beta) and type II (IFN-gamma) interferons, and members of the IL-10 family via type II cytokine receptors. JAK (also called Just Another Kinase) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. The JAK family in mammals consists of 4 members: JAK1, JAK2, JAK3 and TYK2. JAKs are composed of seven JAK homology (JH) domains (JH1-JH7) . The C-terminal JH1 domain is the main catalytic domain, followed by JH2, which is often referred to as a pseudokinase domain, followed by JH3-JH4 which is homologous to the SH2 domain, and lastly JH5-JH7 which is a FERM domain. Named after Janus, the two-faced Roman god of doorways, JAKs possess two near-identical phosphate-transferring domains; one which displays the kinase activity (JH1), while the other negatively regulates the kinase activity of the first (JH2). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GAEIFETSSLLISSESELNNFNMGDGGNYGYYEVSVTGNTGISWRRKPATTAVEKKKKGKSKKNKLKGKK
DEDKKKAREGWNNFSYFPEITHIVIKESTVTINRQDNKKMELKLSSRDEALSFAALVDGYFRLTADAHHY
LCTD
>gnl|CDD|270141 cd13333, FERM_C_JAK2, FERM domain C-lobe of Janus kinase (JAK) 2. JAK2 has been implicated in signaling by members of the type II cytokine receptor family, the GM-CSF receptor family, the gp130 receptor family, and the single chain receptors. JAK2 orthologs have been identified in all mammals. Mutations in JAK2 have been implicated in polycythemia vera, essential thrombocythemia, myelofibrosis as well as other myeloproliferative disorders. JAK2 gene fusions with the PCM1 and TEL(ETV6) (TEL-JAK2) genes have been found in leukemia patients. Researcher are targetting JAK2 inhibitors in the treatment of patients with prostate cancer. JAK2 has been shown to interact with a variety of proteins including growth hormone receptor, STAT5A, STAT5B, interleukin 5 receptor alpha subunit, interleukin 12 receptor, SOCS3, PTPN6,PTPN11, Grb2, VAV1, and YES1. JAK (also called Just Another Kinase) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. The JAK family in mammals consists of 4 members: JAK1, JAK2, JAK3 and TYK2. JAKs are composed of seven JAK homology (JH) domains (JH1-JH7) . The C-terminal JH1 domain is the main catalytic domain, followed by JH2, which is often referred to as a pseudokinase domain, followed by JH3-JH4 which is homologous to the SH2 domain, and lastly JH5-JH7 which is a FERM domain. Named after Janus, the two-faced Roman god of doorways, JAKs possess two near-identical phosphate-transferring domains; one which displays the kinase activity (JH1), while the other negatively regulates the kinase activity of the first (JH2). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
YSERFEVKEPSEGQVTIVVTGNGGIQWSRGKHKETEAEQDLQTYCDFPEVIDISIKQANKEGSSESRVVT
INKQDGKNLELEFSSLSEALSFVSLIDGYYRLTTDAHHYLCKE
>gnl|CDD|275413 cd13334, FERM_C_JAK3, FERM domain C-lobe of Janus kinase (JAK) 3. JAK3 functions in signal transduction and interacts with members of the STAT (signal transduction and activators of transcription) family. It is required for signaling of the type I receptors that use the common gamma chain: IL-2, IL-4, IL-7, IL-9, IL-15 and IL-21. Cytokine binding induces the association of separate cytokine receptor subunits and the activation of the receptor-associated JAKs. In the absence of cytokine, JAKs lack protein tyrosine kinase activity. Once activated, the JAKs create docking sites for the STAT transcription factors by phosphorylation of specific tyrosine residues on the cytokine receptor subunits. Unlike the ubiquitous expression of JAK1, JAK2 and Tyk2, JAK3 is predominantly expressed in hematopoietic cells, such as NK cells, T cells and B cells. Mutations of JAK3 result in severe combined immunodeficiency (SCID). In addition to its well-known roles in T cells and NK cells, JAK3 has recently been found to inhibits IL-8-mediated chemotaxis. JAK3 interacts with CD247, TIAF1, and IL2RG. JAK (also called Just Another Kinase) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. The JAK family in mammals consists of 4 members: JAK1, JAK2, JAK3 and TYK2. JAKs are composed of seven JAK homology (JH) domains (JH1-JH7) . The C-terminal JH1 domain is the main catalytic domain, followed by JH2, which is often referred to as a pseudokinase domain, followed by JH3-JH4 which is homologous to the SH2 domain, and lastly JH5-JH7 which is a FERM domain. Named after Janus, the two-faced Roman god of doorways, JAKs possess two near-identical phosphate-transferring domains; one which displays the kinase activity (JH1), while the other negatively regulates the kinase activity of the first (JH2). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GSETFQVHGPGSKEADILLRVSGDGGISWSCVDSELWQTFCDFPEIIDISIKQACRDGGPVEGRIVTLTR
QDNRVLEAEFPTLREALSFVSLVDGYFRLTTDSHHYFCKE
>gnl|CDD|275414 cd13335, FERM_C_TYK2, FERM domain C-lobe of Non-receptor tyrosine-protein kinase TYK2. Tyk2 functions primarily in IL-12 and type I-IFN signaling as well as transduction of IL-23, IL-10, and IL-6 signals. A mutation in the Tyk2 gene has been associated with hyperimmunoglobulin E syndrome (HIES), a primary immunodeficiency characterized by elevated serum immunoglobulin E. Tyk2 has been shown to interact with FYN, PTPN6, IFNAR1, Ku80 and GNB2L1. JAK (also called Just Another Kinase) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. The JAK family in mammals consists of 4 members: JAK1, JAK2, JAK3 and TYK2. JAKs are composed of seven JAK homology (JH) domains (JH1-JH7) . The C-terminal JH1 domain is the main catalytic domain, followed by JH2, which is often referred to as a pseudokinase domain, followed by JH3-JH4 which is homologous to the SH2 domain, and lastly JH5-JH7 which is a FERM domain. Named after Janus, the two-faced Roman god of doorways, JAKs possess two near-identical phosphate-transferring domains; one which displays the kinase activity (JH1), while the other negatively regulates the kinase activity of the first (JH2). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
FGTETFPVLHLDLRADGEKSGSYLNGGHTEGNPPEETINPPTHEVMVSGTDGIQWRKVSAERSQSDSYSR
HYFMKVMRQKSQKSEQPALNEEPKWVIFCDFQEITHIVIQGINVCISRQDNKCMEISLPSSIQALSFVSL
LDGYFRLTADSNHYLCHE
>gnl|CDD|275415 cd13336, FERM-like_C_SNX31, Atypical FERM-like domain C-lobe of Sorting nexin 31. SNX31 functions in regulating recycling from endosomes to the cell surface. SNX31 contains a N-terminal PX domain, a FERM-like domain, and a unique C-terminal region. It bind Ras GTPase through its FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
GYLQLDPCACDYPECGSEANVWVGNNEISCCIHLPGGQTEHLRFNIRRVICWQVTFLGPKKQEVMSPLHQ
HLELRFEYQQGSSWKWIVIRTKQAFLLSSCLKKMISEYPVHRS
>gnl|CDD|270145 cd13337, FERM-like_C_SNX17, Atypical FERM-like domain C-lobe of Sorting nexin 17. SNX17 is a beta1-integrin-tail-binding protein that interacts with the free kindlin-binding site in endosomes to stabilize beta1 integrins, resulting in their recycling to the cell surface where they can be reused. SNX17 contains a N-terminal PX domain, a FERM-like domain, and a unique C-terminal region. SNX17 binds Ras GTPase through its FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
YGYIQFEPCICDYPKPGTRVLVSIGNRELNFRLKDEEGKVKEGSFRVTRMRCWRITASHIEEDSKKDEKK
LELSFEYLMSKDKLQWITIRSDQAILMSLCLQSMVDELLRKKN
>gnl|CDD|270146 cd13338, FERM-like_C_SNX27, Atypical FERM-like domain C-lobe of Sorting nexin 27. SNX27 is localized to early endosomes and known to regulate the intracellular trafficking of ion channels and receptors. SNX27 contain a N-terminal PDZ domain, a PX domain, and a FERM-like domain. SNX27 regulates trafficking of a PAK interacting exchange factor-G protein-coupled receptor kinase interacting protein complex via its PDZ domain interaction. Sorting nexin 27 interacts with multidrug resistance-associated protein 4 (MRP4). SNX27 binds Ras GTPase through its FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites
NEVVFPHCACDSRKEGHVIPSVSMKAFKLHACTEDGELENQEIEFEWDEIQRWETDEEGMAFCFEYSRPG
KKPRWVKVFTPYYEYMHECFERVQEERKWRKE
>gnl|CDD|275416 cd13339, PH-GRAM_MTMR13, Myotubularian (MTM) related 13 protein Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR13 (also called SBF2/SET binding factor 2) is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Leu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR13 has high sequence similarity to MTMR5 and has recently been shown to be a second gene mutated in type 4B Charcot-Marie-Tooth syndrome. Both MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
EEFVCEGLRVLLDPDGREEATGGLLGGPHILPAEGALFLTTYRIIFKGTPHDQLVGEQTVIRSFPIASIT
KEKKITIQNQLQQNMQEGLQITSASFQLIKVAFDEEVSPEVVEIFKKQL
>gnl|CDD|275417 cd13340, PH-GRAM_MTMR5, Myotubularian (MTM) related 5 protein (MTMR5) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR5 (also called SBF1/SET binding factor 1) is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It lacks several amino acids in the dsPTPase catalytic pocket which renders it catalytically inactive as a phosphatase. MTMR5 is the most well-studied inactive member of this family and has been implicated in cellular growth control and oncogenic transformation. MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
EECVMDGLRVYLLPDGREEASGGSLGGPPLLPAEGAIFLTTYRVIFKGTPTDPLVGEQVVVRSFPVASLT
KEKRISVQAQMDQFLQEGLQLRSCTFQLLKIAFDEEVASDSAEVFRKHL
>gnl|CDD|270149 cd13341, PH-GRAM_MTMR3, Myotubularian (MTM) related 3 protein (MTMR3) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR3 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR3 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The protein can self-associate and also form heteromers with MTMR4. Both MTMR3 and MTMR4 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal lipid-binding FYVE domain which binds phosphotidylinositol-3-phosphate. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
LIREDENLQVPFQELHGESTEFVGRAEDAIIALSNYRLHIKFKESVVNVPLQLIESVECRDIFQLHLTCK
DCKVIRCQFSTFEQCQEWLKRLNN
>gnl|CDD|270150 cd13342, PH-GRAM_MTMR4, Myotubularian (MTM) related 4 protein (MTMR4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR4 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR4 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The protein form heteromers with MTMR3. Both MTMR3 and MTMR4 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal lipid-binding FYVE domain which binds phosphotidylinositol-3-phosphate. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
LVKEEESLQVPFPVLQGEGVEYLGHANDAVIAISNYRLHIKFKDSVINVPLRMMESVESRDMFQLHIICK
DSKVVRCHFSTFKQCQEWLKRLNRATARPAKPEDLFAFAYHAWC
>gnl|CDD|270151 cd13343, PH-GRAM_MTMR6, Myotubularian (MTM) related (MTMR) 6 protein Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR6 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR6 binds to phosphoinositide lipids through its PH-GRAM domain. It acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4+ T-cells possibly by decreasing intracellular levels of phosphatidylinositol-3 phosphatase and negatively regulates proliferation of reactivated CD4+ T-cells MTMR6 interacts with MTMR7, MTMR8 and MTMR9. MTMR6 contains a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
MEHIRTTKVEQVKLLDRFSTSNKSLTGTLYLTATHLLFIDNSQQETWILHHHIAPVEKLSLTTSGCPLVI
QCKNFRVVHFVVPRERDCHDIYNSLLQLSRP
>gnl|CDD|270152 cd13344, PH-GRAM_MTMR7, Myotubularian (MTM) related 7 protein (MTMR7) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR7 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR6 binds to phosphoinositide lipids through its PH-GRAM domain and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate. MTMR7 interacts with MTMR6, MTMR8 and MTMR9. MTMR7 contains a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
MEHIRMPKVENVRLVDRISSKKAALGTLYLTATHVIFVENSSDTRKETWILHSQISSIEKQATTATGCPL
LIRCKNFQVIQLIIPQERDCHDVYISLIRLARP
>gnl|CDD|270153 cd13345, PH-GRAM_MTMR8, Myotubularian (MTM) related 8 protein (MTMR8) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR8 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR8 binds to phosphoinositide lipids through its PH-GRAM domain. MTMR8 can self associate and interacts with MTMR6, MTMR7 and MTMR9. MTMR8 contains a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
MEHITTPKVENVKLLDRYTNKKPANGTLYLTATHLIYVEASGAARKETWILHHHIATVEKLPLTSLGCPL
LIRCKNFRVAHFVLDSERDCHEVYISLLKLSQP
>gnl|CDD|270154 cd13346, PH-GRAM_MTMR10, Myotubularian (MTM) related 10 protein (MTMR10) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR10 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Glu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR10 contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, and a SET interaction domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
TDDKINSEPKIKKLEPVLLPGEIVVNEVNFVRKCIATDTSQYDLWGKLICTNFKISFITDDPMPLQKFHY
KNLLLGEHDVPLTCIEQIVTVNDTKRKQKVLGPNQKLKFNPTELIIYCKDFRIVRFRFDEAGPESAKKVC
LAIAHYSQPTDLQLLFAFEYVGKKYHNSAGKVNGIDP
>gnl|CDD|275418 cd13348, PH-GRAM_MTMR12, Myotubularian (MTM) related 12 protein (MTMR12) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR12 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Glu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR12 contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, a SET interaction domain, and a C-terminal a coiled-coil domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
TEEEIKLEKEPQEKEVNPHLLPGEVVLCEANTVLKYTQDDGSQRGVYGRLVCTNFRIAFLGDDAPQDDNS
KQFKNKIYGENDITLQCVDQIYGVYDEKKKLITGGLVKNKYPEKLIIHCKDLRVFQFCLRYTKEEEVKRI
VSGIIHHTQEPKLLKRLFLFSYARAAPNNTVTKREAIM
>gnl|CDD|270156 cd13349, PH-GRAM1_TBC1D8, TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 1. TBC1D8 may act as a GTPase-activating protein for Rab family protein(s). TBC1D8 contains an N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the first repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold
AEKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLLIPWVDVQKLERTSNVFMTDTIRVTTQ
NKERDFSMFLNIDEVFRIMEQLADVTLRR
>gnl|CDD|275419 cd13350, PH-GRAM1_TBC1D8B, TBC1 domain family member 8B (TBC1D8B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 1. TBC1D8B may act as a GTPase-activating protein for Rab family protein(s). TBC1D8B contains an N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the first repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold
QEKLVTYYSCSYWRGRVPCQGWLYLSTNFLSFYSFLLGSEIKLIISWDEISKLEKTSNVILTESIHVCSR
GEDHYFSMFLHINETFLLMEQLANYAVRR
>gnl|CDD|275420 cd13351, PH-GRAM1_TCB1D9_TCB1D9B, TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 1. TBC1D9 and TCB1D9B may act as a GTPase-activating proteins for Rab family protein(s). TBC1D9 and TCB1D9B contain two N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the first repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold
EEKLVNYYSCSYWKGRVPRQGWLYLSVNHLCFYSFLLGKEAKLVIRWTDVTQLEKNNSLLLPDSIKVVTR
DKEHYFSMFLNISETFKLMEQLANLAMRQ
>gnl|CDD|270159 cd13352, PH-GRAM2_TBC1D8B, TBC1 domain family member 8B (TBC1D8B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 2. TBC1D8B may act as a GTPase-activating protein for Rab family protein(s). TBC1D8B contains an N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the second repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold
EETLKEVHECFLWVPFSHFNTHGKMCISENYICFASQDGSLCSVIIPLREVLSIDKTDDSSRAVTISTKG
KRAFRFTEVKDFEQLVAKLRLKC
>gnl|CDD|270160 cd13353, PH-GRAM2_TBC1D8, TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 2. TBC1D8 may act as a GTPase-activating protein for Rab family protein(s). TBC1D8 contains two N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the second repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold
KEKLHEVVDCSLWTPFSRCHTAGRMYTSDSYICFASKEDGSCNVILPLREVVSIEKMEDTSLLPNPIIVS
IRSKMAFQFIELKDRDSLVESLLARL
>gnl|CDD|270161 cd13354, PH-GRAM2_TCB1D9_TCB1D9B, TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 2. TBC1D9 and TCB1D9B may act as a GTPase-activating proteins for Rab family protein(s). TBC1D9 and TCB1D9B contain two N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the second repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold
DEKLDGSTDCTLWTPYNKRHVWGTLYLSQNYICFTSKVRDLVSLVIPLREVTSVEKADSSSVSLPNGILI
TTKSKMTFLFAQIKDRDFLVHKISDFL
>gnl|CDD|270162 cd13355, PH-GRAM_MTM1, Myotubularian 1 protein (MTM1) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTM1 is a member of the myotubularin protein phosphatase gene family. It is required for muscle cell differentiation and mutations in this gene have been identified as being responsible for X-linked myotubular myopathy, a severe congenital muscle disorder characterized by defective muscle cell development. Since its initial discovery, there have been an additional 14 myotubularin-related proteins identified. MTM1 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The protein can self-associate and form heteromers with MTMR12. MTM1 contains a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. All MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE and PH domains C-terminal to the coiled-coil region
VTDKDVIYICPFNGPVKGRVYITNYRLYFKSTESEPPVTLDVPLGVISRIEKMGGASSRGENSYGLDITC
KDMRNLRFALKQEGHSRRDIFEILTKYAFP
>gnl|CDD|270163 cd13356, PH-GRAM_MTMR2_mammal-like, Myotubularian related 2 protein (MTMR2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR2 is a member of the myotubularin protein phosphatase gene family. MTMR2 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. Mutations in MTMR2 are a cause of Charcot-Marie-Tooth disease type 4B, an autosomal recessive demyelinating neuropathy. The protein can self-associate and form heteromers with MTMR5 and MTMR12. MTMR2 contains a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal PDZ domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date.Members in this cd include mammals, chickens, anoles, human body lice, and aphids
MEEPPLLPGENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVINRVEKIGGAS
SRGENSYGLETVCKDIRNLRFAHKPEGRTRRSIFENLMKYAFPVS
>gnl|CDD|270164 cd13357, PH-GRAM_MTMR2_insect-like, Myotubularian related 2 protein (MTMR2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR2 is a member of the myotubularin protein phosphatase gene family. MTMR2 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. Mutations in MTMR2 are a cause of Charcot-Marie-Tooth disease type 4B, an autosomal recessive demyelinating neuropathy. The protein can self-associate and form heteromers with MTMR5 and MTMR12. MTMR2 contains a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal PDZ domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date. Members in this cd include Drosophila, sea urchins, mosquitos, bees, ticks, and anemones
AIAKDVTYLCPFRGPVRGTLTITNYKLYFKSLDREPPFTVEVPLGVIYRVEKVGGATSRGENSYGLEIFC
KDMRNLRFAHKQENHSRRLVFEKLQAYAFP
>gnl|CDD|270165 cd13358, PH-GRAM_MTMR1, Myotubularian related 1 protein (MTMR1) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR1 is a member of the myotubularin protein phosphatase gene family. MTMR1 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. MTMR1 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal PDZ domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date
KAIVKDVMYICPFMGAVSGTLTVTDFKMYFKNVERDPPFILDVPLGVISRVEKIGVQSHGDNSCGIEIVC
KDMRNLRLAYKQEEQSKLEIFENLNKHAFP
>gnl|CDD|270166 cd13359, PH_ELMO1_CED-12, Engulfment and cell motility protein 1 pleckstrin homology (PH) domain. DOCK2 (Dedicator of cytokinesis 2), a hematopoietic cell-specific, atypical GEF, controls lymphocyte migration through Rac activation. A DOCK2-ELMO1 complex s necessary for DOCK2-mediated Rac signaling. DOCK2 contains a SH3 domain at its N-terminus, followed by a lipid binding DHR1 domain, and a Rac-binding DHR2 domain at its C-terminus. ELMO1, a mammalian homolog of C. elegans CED-12, contains the N-terminal RhoG-binding region, the ELMO domain, the PH domain, and the C-terminal sequence with three PxxP motifs. The C-terminal region of ELMO1, including the Pro-rich sequence, binds the SH3-containing region of DOCK2 forming a intermolecular five-helix bundle along with the PH domain of ELMO1. Autoinhibition of ELMO1 and DOCK2 is accomplished by the interactions of the EID and EAD domains and SH3 and DHR2 domains, respectively. The interaction of DOCK2 and ELMO1 mutually relieve their autoinhibition and results in the activation of Rac1. The PH domain of ELMO1 does not bind phosphoinositides due to the absence of key binding residues. It more closely resembles the FERM domain rather than other PH domains. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
ELIKQQRLNFLVEGTLFPKYNARGRKDKFWYCRLSPNHKVLHYGDCEESAQPAPLEELPEKLPVADIKAL
VTGKDCPHMKELKKNKSVASLAFSILYDSDESLDFVAPNETVFDIWTDGLNALLGK
>gnl|CDD|241514 cd13360, PH_PLC_fungal, Fungal Phospholipase C (PLC) pleckstrin homology (PH) domain. Fungal PLC have mostly been characterized in the yeast Saccharomyces cerevisiae via deletion studies which resulted in a pleiotropic phenotype, with defects in growth, carbon source utilization, and sensitivity to osmotic stress and high temperature. Unlike Saccharomyces several other fungi including Neurospora crassa, Cryphonectria parasitica, and Magnaporthe oryzae (Mo) have several PLC proteins, some of which lack a PH domain, with varied functions. MoPLC1-mediated regulation of Ca2+ level is important for conidiogenesis and appressorium formation while both MoPLC2 and MoPLC3 are required for asexual reproduction, cell wall integrity, appressorium development, and pathogenicity. The fungal PLCs in this hierarchy contain an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves, and a C-terminal C2 domain. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LRQGTPLLKVTKKKKKRILFKLDPESGKITWDSKKPSKSLYIDDIKEIRTGEDARNYREEFGISEEFEDR
WITIIYFVPKKNKLKTLHLIADTEEDFKLWTTTLEGLVKLRRELMESL
>gnl|CDD|270167 cd13361, PH_PLC_beta, Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain. PLC-beta (PLCbeta) is regulated by heterotrimeric G protein-coupled receptors through their C2 domain and long C-terminal extension which forms an autoinhibitory helix. There are four isoforms: PLC-beta1-4. The PH domain of PLC-beta2 and PLC-beta3 plays a dual role, much like PLC-delta1, by binding to the plasma membrane, as well as the interaction site for the catalytic activator. However, PLC-beta binds to the lipid surface independent of PIP2. PLC-beta1 seems to play unspecified roles in cellular proliferation and differentiation. PLC-beta consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves, a C2 domain and a C-terminal PDZ. Members of the Rho GTPase family (e.g., Rac1, Rac2, Rac3, and cdc42) have been implicated in their activation by binding to an alternate site on the N-terminal PH domain. A basic amino acid region within the enzyme's long C-terminal tail appears to function as a Nuclear Localization Signal for import into the nucleus. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.the plasma membrane, but only a few (less than 10%) display strong specificity in binding inositol phosphates. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinases, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, cytoskeletal associated molecules, and in lipid associated enzymes
LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREVNV
GGSDEDLEDRTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP
>gnl|CDD|270168 cd13362, PH_PLC_gamma, Phospholipase C-gamma (PLC-gamma) pleckstrin homology (PH) domain. PLC-gamma (PLCgamma) is activated by receptor and non-receptor tyrosine kinases due to the presence of its SH2 and SH3 domains. There are two main isoforms of PLC-gamma expressed in human specimens, PLC-gamma1 and PLC-gamma2. PLC-gamma consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves internal to which is a PH domain split by two SH2 domains and a single SH3 domain, and a C-terminal C2 domain. Only the first PH domain is present in this hierarchy. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LERGTVMTKFYQKKRPERRTFQVKLETRQVVWSRGGGKRAEGAVDIREIKEIRPGKNSKDFERWPDEAKK
LDPSCCFVILYGTEFRLKTLSVAATSEEECDMWIKGLRYLVEDTLSASYPL
>gnl|CDD|270169 cd13363, PH_PLC_delta, Phospholipase C-delta (PLC-delta) pleckstrin homology (PH) domain. The PLC-delta (PLCdelta) consists of three family members, delta 1, 2, and 3. PLC-delta1 is the most well studied. PLC-delta is activated by high calcium levels generated by other PLC family members, and functions as a calcium amplifier within the cell. PLC-delta consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves, and a C-terminal C2 domain. The PH domain binds PIP2 and promotes activation of the catalytic core as well as tethering the enzyme to the plasma membrane. The C2 domain has been shown to mediate calcium-dependent phospholipid binding as well. The PH and C2 domains operate in concert as a "tether and fix" apparatus necessary for processive catalysis by the enzyme. Its leucine-rich nuclear export signal (NES) in its EF hand motif, as well as a Nuclear localization signal within its linker region allow PLC-delta 1 to actively translocate into and out of the nucleus. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LLQGSPLLKVRSRSWKKERFYKLQEDCKTVWHESKKTRSNSKQTFSIEDIESVREGHQSEGLRKYAEAFP
EDRCFSIVFKGRRKNLDLIAPSEEEAQRWVRGLEKLIARLTNMSQRE
>gnl|CDD|270170 cd13364, PH_PLC_eta, Phospholipase C-eta (PLC-eta) pleckstrin homology (PH) domain. PLC-eta (PLCeta) consists of two enzymes, PLCeta1 and PLCeta2. They hydrolyze phosphatidylinositol 4,5-bisphosphate, are more sensitive to Ca2+ than other PLC isozymes, and involved in PKC activation in the brain and neuroendocrine systems. PLC-eta consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves by a variable linker, a C2 domain, and a C-terminal PDZ domain. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.involved in targeting proteins to the plasma membrane, but only a few (less than 10%) display strong specificity in binding inositol phosphates. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinases, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, cytoskeletal associated molecules, and in lipid associated enzymes
MQEGSELVKVRSNSRQYRRFFYLDEDKSSIRWKPSKKKSEKAKIPISSIREVREGKTTDIFRSCDISGDF
PEECCFSIIYGEEYETLDLVASSPDEANIWITGLRYLMS
>gnl|CDD|270171 cd13365, PH_PLC_plant-like, Plant-like Phospholipase C (PLC) pleckstrin homology (PH) domain. PLC-gamma (PLCgamma) was the second class of PLC discovered. PLC-gamma consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves internal to which is a PH domain split by two SH2 domains and a single SH3 domain, and a C-terminal C2 domain. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). This cd contains PLC members from fungi and plants. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RDVIEAITQLKIGSYLLKYGRRGKPHFRYFWLSPDELTLYWSSPKKGSEKRVRLSSVSRIIPGQRTVVFK
RPPPPGLEEHSFSIIYADGERSLDLTCKDRQEFDTWFTGLRYLLS
>gnl|CDD|270172 cd13366, PH_ABR, Active breakpoint cluster region-related protein pleckstrin homology (PH) domain. The ABR protein contains multiple domains including a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. It is related to a slightly larger protein, BCR, which is structurally similar, but has an additional N-terminal kinase domain. ABR has GAP activity for both Rac and Cdc42. It promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them. It is highly enriched in the brain and found to a lesser extent in heart, lung and muscle. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
FLSSINEDIDPRRTAVTTPKGETRQLVKDGFLVEVSEGSRKLRHVFLFTDLLLCAKLKKTAVGKHQQYDC
KWYIPLADLVFPSPEESESLPQVHTLPDHEIEEMKMKISAIKSEIQKEKKNKKGQSRAIERLKKKMFENE
SWLLLNSPTIPFRIHNKNGKSYLFLLSSDYERSEWREAIQKLQKK
>gnl|CDD|270173 cd13367, PH_BCR_vertebrate, Breakpoint Cluster Region-related pleckstrin homology (PH) domain. The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. This hierarchy is composed of vertebrate BCRs. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
FLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCAKLKKQIGGKSQQYDC
KWYIPLADLSFQTVDESEAVPNIPLIPDEEIDALKVKISQIKSDIQREKRANKGGKVLERLRKKLSEQES
LLLLMSPSMAFRVHNRNGKSYTFLISSDYERAEWRENIREQQKKCFKSFSLTSL
>gnl|CDD|270174 cd13368, PH_BCR_arthropod, Breakpoint Cluster Region-related pleckstrin homology (PH) domain. The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. This hierarchy is composed of arthropod BCRs. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
FLNEFNNIQTKSMFPHQDRALRRLVKNSFIVELADGHRKLRHLFLFNDVIACAKYKSSGRTRITFELKWF
IPLNDVTILEEEAPAPKESSPPNIEQLKSNACQVRDQLADRSRASTSGSDKIRKKLADLEAQLVLASPNL
VFRIGNKNNKTYTFFLSSEFERTQWIEAILTLQQTCPLPG
>gnl|CDD|270175 cd13369, PH_RASAL1, Ras-GTPase-activating-like protein pleckstrin homology (PH) domain. RASAL1 is a member of the GAP1 family of GTPase-activating proteins, along with GAP1(m), GAP1(IP4BP) and CAPRI. RASAL1 contains two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. RASAL1 contains two fully conserved C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Its catalytic GAP domain has dual RasGAP and RapGAP activities, while its C2 domains bind phospholipids in the presence of Ca2+. Both CAPRI and RASAL1 are calcium-activated RasGAPs that inactivate Ras at the plasma membrane. Thereby enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS and allowing control of cellular proliferation and differentiation. CAPRI and RASAL1 differ in that CAPRI is an amplitude sensor while RASAL1 senses calcium oscillations. This difference between them resides not in their C2 domains, but in their PH domains leading to speculation that this might reflect an association with either phosphoinositides and/or proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
ESEVPPRALFPPSVTVKEGYLHKRKAEGVGLVTRFTFKKRYFWLSSETLSYSKSPDWQVRSSIPVQRICA
VERVDENAFQQPNVMQVVTQDGEGQVHTTYIQCKNVNELNQWLSALRKVSLSNERMLPACHPGAFRSA
>gnl|CDD|241521 cd13370, PH_GAP1m_mammal-like, GTPase activating protein 1 m pleckstrin homology (PH) domain. GAP1(m) (also called RASA2/RAS p21 protein activator (GTPase activating protein) 2) is a member of the GAP1 family of GTPase-activating proteins, along with RASAL1, GAP1(IP4BP), and CAPRI. With the notable exception of GAP1(m), they all possess an arginine finger-dependent GAP activity on the Ras-related protein Rap1. GAP1(m) contains two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Its C2 domains, like those of GAP1IP4BP, do not contain the C2 motif that is known to be required for calcium-dependent phospholipid binding. GAP1(m) is regulated by the binding of its PH domains to phophoinositides, PIP3 (phosphatidylinositol 3,4,5-trisphosphate). It suppresses RAS, enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. GAP1(m) binds inositol tetrakisphosphate (IP4). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SSTESKESSGVSESVHLKEGEMHKRAQGRTRIGKKNFKKRWFCLTSRELTYHKQKGKEAIFTIPVKNILA
VEKLEESAFNKKNMFQVIHSEKPLYVQANNCVEANEWIEVLSRVSRCNQKRLSFYHPSAYLGG
>gnl|CDD|241522 cd13371, PH_GAP1_mammal-like, GAP1(IP4BP) pleckstrin homology (PH) domain. GAP1 (also called IP4BP, RASA3/Ras GTPase-activating protein 3, and RAS p21 protein activator (GTPase activating protein) 3/GAPIII/MGC46517/MGC47588)) is a member of the GAP1 family of GTPase-activating proteins, along with RASAL1, GAP1(m), and CAPRI. With the notable exception of GAP1(m), they all possess an arginine finger-dependent GAP activity on the Ras-related protein Rap1. GAP1(IP4BP) contains two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Its C2 domains, like those of GAP1M, do not contain the C2 motif that is known to be required for calcium-dependent phospholipid binding. GAP1(IP4BP) is regulated by the binding of its PH domains to phophoinositides, PIP3 (phosphatidylinositol 3,4,5-trisphosphate) and PIP2 (phosphatidylinositol 4,5-bisphosphate). It suppresses RAS, enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. GAP1(IP4BP) binds tyrosine-protein kinase, HCK. Members here include humans, chickens, frogs, and fish. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SSSGRRDHKSIEQPILLKEGFMIKRAQGRKRFGMKNFKKRWFRLTNHEFTYHKSKGDHPLCSIPIENILA
VERLEEESFKMKNMFQVIQPERALYIQANNCVEAKDWIDILTKVSQCNKKRLTVY
>gnl|CDD|241523 cd13372, PH_CAPRI, Ca2+ promoted Ras inactivator pleckstrin homology (PH) domain. CAPRI (also called RASA4/RAS p21 protein activator (GTPase activating protein) 4/GAPL/FLJ59070/KIAA0538/MGC131890) is a member of the GAP1 family of GTPase-activating proteins. CAPRI contains two fully conserved C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Its catalytic GAP domain has dual RasGAP and RapGAP activities, while its C2 domains bind phospholipids in the presence of Ca2+. Both CAPRI and RASAL are calcium-activated RasGAPs that inactivate Ras at the plasma membrane. Thereby enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS and allowing control of cellular proliferation and differentiation. CAPRI and RASAL differ in that CAPRI is an amplitude sensor while RASAL senses calcium oscillations. This difference between them resides not in their C2 domains, but in their PH domains leading to speculation that this might reflect an association with either phosphoinositides and/or proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
FITKLVDIEEEDELDLTRMLLLQAPMVKEGFLFIHRTKGKGPLMASSFKKLYFTLTKDALSFAKTPHSKK
SSSISLAKIRAAEKVEEKCFGSSNVMQIIYTDDAGQQETLYLQCKSVNELNQWLSALRKVCSNNTNLLSS
>gnl|CDD|270176 cd13373, PH_nGAP, Neuronal growth-associated proteins Pleckstrin homology (PH) domain. nGAP (also called RASAL2/RAS protein activator like-3) is a member of the RasSynGAP family along with DOC-2/DAB2-interacting protein (DAB2IP) and synaptic RasGAP (SynGAP). nGAPs are growth cone markers found in multiple types of neurons. There are many nGAPs including Cap1 (Adenylate cyclase-associated protein 1), Capzb (Capping protein (actin filament) muscle Z-line, beta), Clptm1 (Cleft lip and palate associated transmembrane protein 1), Cotl1 (Coactosin-like 1), Crmp1 (Collapsin response mediator protein 1), Cyfip1 (Cytoplasmic FMR1 interacting protein 1), Fabp7 (Fatty acid binding protein 7, brain), Farp2 (FERM, RhoGEF and pleckstrin domain protein 2), Gap43 (Growth associated protein 43), Gnao1 (Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O), Gnai2 (Guanine nucleotide binding protein (G protein), alpha inhibiting 2), Pacs1 (Phosphofurin acidic cluster sorting protein 1), Rtn1 (Reticulon 1), Sept2 (Septin 2), Snap25 (Synaptosomal-associated protein 25), Strap (Serine/threonine kinase receptor associated protein), Stx7 (Syntaxin 7), and Tmod2 (Tropomodulin 2). PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
PFKVSGFFSKRLKGSIKRTKSQSKLDRNTSFRLPSLRSADDRSRGLPKLKESRSHESLLSPGSAVEALDL
GREEKVSVKPLHSSILGQDFCFEVTYSSGSKCFSCSSAAERDKWMENLRRTVQPNKDNCRRAENVLRL
>gnl|CDD|270177 cd13374, PH_RASAL3, RAS protein activator like-3 Pleckstrin homology (PH) domain. RASAL3 is thought to be a Ras GTPase-activating protein. It is involved in positive regulation of Ras GTPase activity and of small GTPase mediated signal transduction as well as negative regulation of Ras protein signal transduction. It contains a PH domain, a C2 domain, and a Ras-GAP domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
DPDREPGKTEPEAAGPNQGHNVRGLLKRLKEKKKAKAESTGTGRDGPPSALGSRESLATISELDLGAERD
VRVWPLHPSLLGEPHCFQVTWPGGSRCFSCRSAAERDRWIEDLRRSFQPHQDNVEREETWLSVWVHEAKG
LPRAAA
>gnl|CDD|270178 cd13375, PH_SynGAP, Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain. SynGAP is a member of the RasSynGAP family along with DOC-2/DAB2-interacting protein (DAB2IP) and neuronal growth-associated protein (nGAP/RASAL2). SynGAP, a neuronal Ras-GAP, has been shown display both Ras-GAP activity and Ras-related protein (Rap)-GAP activity. Saccharomyces cerevisiae Bud2 and GAP1 members CAPRI (Ca2+-promoted Ras inactivator) and RASAL (Ras-GTPase-activating-like protein) also possess this dual activity. Human DOC-2/DAB2-interacting protein (DAB2IP) is encoded by a tumor suppressor gene and a newly recognized member of the Ras-GTPase-activating family. Members here include mammals, amphibians, and bony fish. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
PTAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSS
AAEALDLNLDEDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVD
NVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRTDTVFWGEHFE
>gnl|CDD|270179 cd13376, PH_DAB2IP, DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain. DAB2IP (also called AIP1/ASK1-interacting protein-1 and DIP1/2) is a member of the RasSynGAP family along with Synaptic Ras-GTPase activating protein (SynGAP) and neuronal growth-associated protein (nGAP/RASAL2). DAB2IP is a critical component of many signal transduction pathways mediated by Ras and tumor necrosis factors including apoptosis pathways, and it is involved in the formation of many types of tumors. DAB2IP participates in regulation of gene expression and pluripotency of cells. Human DAB2IP is expressed in the adrenal gland, pancreas, endocardium, stomach, kidney, testis, small intestine, liver, trachea, skin, ovary, endometrium, lung, esophagus and bladder. No expression was observed in the cerebrum, parotid gland, thymus, thyroid gland and spleen. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VTGFLSRRLKGSIKRTKSQPKLDRNSSFRHILPGFRSVDNERSHLMPRLKESRSHESLLSPSSAVEALDL
SMEEEVVIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVENMLKLWI
IEAKDLPAKKKYLCELCLDDVLYARTTCKLKTDNVFWGEHFE
>gnl|CDD|241529 cd13378, PH_RhoGAP2, Rho GTPase activating protein 2 Pleckstrin homology (PH) domain. RhoGAP2 (also called RhoGap22 or ArhGap22) are involved in cell polarity, cell morphology and cytoskeletal organization. They activate a GTPase belonging to the RAS superfamily of small GTP-binding proteins. The encoded protein is insulin-responsive, is dependent on the kinase Akt, and requires the Akt-dependent 14-3-3 binding protein which binds sequentially to two serine residues resulting in regulation of cell motility. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
EGVLKAGWLKKQRSIMKNWQQRWFVLRGDQLFYYKDEEETKPQGCISLQGSQVNELPPNPEEPGKHLFEI
LPGGAGDREKVPMNHEAFLLMANSQSDMEDWVKAIRRVIWAPFGGG
>gnl|CDD|241530 cd13379, PH_RhoGap24, Rho GTPase activating protein 24 Pleckstrin homology (PH) domain. RhoGap24 (also called ARHGAP24, p73RhoGAp, and Filamin-A-associated RhoGAP) like other RhoGAPs are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LEVIKCGWLRKQGGFVKTWHTRWFVLKGDQLYYFKDEDETKPLGTIFLPGNRVTEHPCNEEEPGKFLFEV
VPGGDRERMTANHETYLLMASTQNDMEDWVKSIRRVIWAPFGGG
>gnl|CDD|270180 cd13380, PH_Skap1, Src kinase-associated phosphoprotein 1 Pleckstrin homology (PH) domain. Adaptor protein Skap1 (also called Skap55/Src kinase-associated phosphoprotein of 55 kDa) and its partner, ADAP (adhesion and degranulation promoting adapter protein) help reorganize the cytoskeleton and/or promote integrin-mediated adhesion upon immunoreceptor activation. Skap1 is also involved in T Cell Receptor (TCR)-induced RapL-Rap1 complex formation and LFA-1 activation. Skap1 has an N-terminal coiled-coil conformation which is proposed to be involved in homodimer formation, a central PH domain and a C-terminal SH3 domain that associates with ADAP. The Skap1 PH domain plays a role in controlling integrin function via recruitment of ADAP-SKAP complexes to integrins as well as in controlling the ability of ADAP to interact with the CBM signalosome and regulate NF-kappaB. SKAP1 is necessary for RapL binding to membranes in a PH domain-dependent manner and the PI3K pathway. Skap adaptor proteins couple receptors to cytoskeletal rearrangements. Skap55/Skap1, Skap2, and Skap-homology (Skap-hom) have an N-terminal coiled-coil conformation, a central PH domain and a C-terminal SH3 domain. Their PH domains bind 3'-phosphoinositides as well as directly affecting targets such as in Skap55 where it directly affecting integrin regulation by ADAP and NF-kappaB activation or in Skap-hom where the dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch that controls ruffle formation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
ILKQGYLEKRSKDHSFFGSEWQKRWCVLTNRAFYYYASEKSKQPKGGFLIKGYSAQMAPHLRKDSRRDSC
FELTTPGRRTYQFTAASPSEARDWVDQIQFLLKDTQ
>gnl|CDD|270181 cd13381, PH_Skap-hom_Skap2, Src kinase-associated phosphoprotein homolog and Skap 2 Pleckstrin homology (PH) domain. Adaptor protein Skap-hom, a homolog of Skap55, which interacts with actin and with ADAP (adhesion and degranulation promoting adapter protein) undergoes tyrosine phosphorylation in response to plating of bone marrow-derived macrophages on fibronectin. Skap-hom has an N-terminal coiled-coil conformation that is involved in homodimer formation, a central PH domain and a C-terminal SH3 domain that associates with ADAP. The Skap-hom PH domain regulates intracellular targeting; its interaction with the DM domain inhibits Skap-hom actin-based ruffles in macrophages and its binding to 3'-phosphoinositides reverses this autoinhibition. The Skap-hom PH domain binds PI[3,4]P2 and PI[3,4,5]P3, but not to PI[3]P, PI[5]P, or PI[4,5]P2. Skap2 is a downstream target of Heat shock transcription factor 4 (HSF4) and functions in the regulation of actin reorganization during lens differentiation. It is thought that SKAP2 anchors the complex of tyrosine kinase adaptor protein 2 (NCK20/focal adhesion to fibroblast growth factor receptors at the lamellipodium in lens epithelial cells. Skap2 has an N-terminal coiled-coil conformation which interacts with the SH2 domain of NCK2, a central PH domain and a C-terminal SH3 domain that associates with ADAP (adhesion and degranulation promoting adapter protein)/FYB (the Fyn binding protein). Skap2 PH domain binds to membrane lipids. Skap adaptor proteins couple receptors to cytoskeletal rearrangements. Src kinase-associated phosphoprotein of 55 kDa (Skap55)/Src kinase-associated phosphoprotein 1 (Skap1), Skap2, and Skap-hom have an N-terminal coiled-coil conformation, a central PH domain and a C-terminal SH3 domain. Their PH domains bind 3'-phosphoinositides as well as directly affecting targets such as in Skap55 where it directly affecting integrin regulation by ADAP and NF-kappaB activation or in Skap-hom where the dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch that controls ruffle formation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VLKAGYLEKRRKDHSFFGFEWQKRWCALSNSVFYYYGSDKDKQQKGEFAIDGYDVKMNNTLRKDAKKDCC
FEICAPDKRVYQFTAASPKEAEEWVQQIKFILQDLG
>gnl|CDD|270182 cd13382, PH_OCRL1, oculocerebrorenal syndrome of Lowe 1 Pleckstrin homology-like domain. OCRL1 (also called INPP5F, LOCR, NPHL2, or phosphatidylinositol polyphosphate 5-phosphatase) hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events. It interact with APPL1, FAM109A and FAM109B and several Rab GTPases which might both target them to the specific membranes and as well as stimulating the phosphatase activity. OCRL1 contains a PH domain and a Rho-GAP domain. Patients with Lowe syndrome suffer primarily from congenital cataracts, neonatal hypotonia, intellectual disability and Fanconi syndrome. Mutations in OCRL are also found in a subset of patients with type 2 Dent disease, who selectively suffer from renal proximal tubular dysfunction. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
CIATVRGHEIRSGQREPRALSLAQRSGQYKLIIQSNEKEPVSQDIIPINSHFRCVQEAEETLLIDIASNT
GCKIRVQGDRTPERLFEIPDEEHCLSFLSHVLAAQ
>gnl|CDD|270183 cd13383, PH_OCRL2, oculocerebrorenal syndrome of Lowe 2 Pleckstrin homology-like domain. OCRL2 (also called IPNNB5, inositol polyphosphate-5-phosphatase, phosphoinositide 5-phosphatase, 5PTase, or type II inositol-1,4,5-trisphosphate 5-phosphatase) hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events. It interact with APPL1, FAM109A and FAM109B and several Rab GTPases which might both target them to the specific membranes and as well as stimulating the phosphatase activity. OCRL2 contains a PH domain and a Rho-GAP domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
CEIAVQGSLIQGWSKASRLLGLVNKRTTHALVIYTHRRMAITYSDVTLERILPIDQDFKCEEVTDDSDLQ
QDGSDVTVNVTSAKLHLVFEMRPGSVTSSLVSEIFRAI
>gnl|CDD|241535 cd13384, PH_Gab2_2, Grb2-associated binding protein family pleckstrin homology (PH) domain. The Gab subfamily includes several Gab proteins, Drosophila DOS and C. elegans SOC-1. They are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. Members here include insect, nematodes, and crustacean Gab2s. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
TEVVYEGWLTKSPPEKRIWRAKWRRRYFVLRQSEIPGQYFLEYYTDRTCRKLKGSIDLDQCEQVDAGLTF
ETKNKLKDQHIFDIRTPKRTYYLVADTEDEMNKWVNCICTVCGLQ
>gnl|CDD|270184 cd13385, PH_Gab3, Grb2-associated binding protein 3 pleckstrin homology (PH) domain. The Gab subfamily includes several Gab proteins, Drosophila DOS and C. elegans SOC-1. They are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. The members in this cd include the Gab1, Gab2, and Gab3 proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
MSAGDVVCTGWLIKSPPERKLKRYAWRKRWFVLRRGRMSGNPDVLEYYRNNHSKKPIRVIDLSECEVLKH
SGPNFIRKEFQNNFVFIVKTTYRTFYLVAKTEEEMQVWVHNISQICNFGHLEDGT
>gnl|CDD|275421 cd13386, PH1_FGD2, FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 2, N-terminal Pleckstrin homology (PH) domain. In general, FGDs have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain. Not much is known about FGD2. FGD1 is the best characterized member of the group with mutations here leading to the X-linked disorder known as faciogenital dysplasia (FGDY). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LLKEGPVLKISFRNNNPKERYLFLFNNMLLYCVPKVIQVGAKFQVHMRIDVDGMKVRELNDAEFPHSFLV
SGKQRTLELQARSQEEMEAWIQAFQEAIDQNEKRTETF
>gnl|CDD|275422 cd13387, PH1_FGD3, FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 3, N-terminal Pleckstrin homology (PH) domain. In general, FGDs have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain. Both FGD1 and FGD3 are targeted by the ubiquitin ligase SCF(FWD1/beta-TrCP) upon phosphorylation of two serine residues in its DSGIDS motif and subsequently degraded by the proteasome. However, FGD1 and FGD3 induced significantly different morphological changes in HeLa Tet-Off cells and while FGD1 induced long finger-like protrusions, FGD3 induced broad sheet-like protrusions when the level of GTP-bound Cdc42 was significantly increased by the inducible expression of FGD3. They also reciprocally regulated cell motility in inducibly expressed in HeLa Tet-Off cells, FGD1 stimulated cell migration while FGD3 inhibited it. FGD1 and FGD3 therefore play different roles to regulate cellular functions, even though their intracellular levels are tightly controlled by the same destruction pathway through SCF(FWD1/beta-TrCP). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LIKEGHIQKLSAKNGTAQDRYLYLFNSMVLYCVPKLRLMGQKFSVREKIDIAGMQVQEIVKQNVPHTFTI
TGKKRSLELQARTEEEKKEWIQVIQATIEKHKQNSETF
>gnl|CDD|275423 cd13388, PH1_FGD1-4_like, FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 1-4 and similar proteins, N-terminal Pleckstrin homology (PH) domain. In general, FGDs have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain. Mutations in the FGD1 gene are responsible for the X-linked disorder known as faciogenital dysplasia (FGDY). Both FGD1 and FGD3 are targeted by the ubiquitin ligase SCF(FWD1/beta-TrCP) upon phosphorylation of two serine residues in its DSGIDS motif and subsequently degraded by the proteasome. They play different roles to regulate cellular functions, even though their intracellular levels are tightly controlled by the same destruction pathway. FGD4 is one of the genes associated with Charcot-Marie-Tooth neuropathy type 4 (CMT4), a group of progressive motor and sensory axonal and demyelinating neuropathies that are distinguished from other forms of CMT by autosomal recessive inheritance. Those affected have distal muscle weakness and atrophy associated with sensory loss and, frequently, pes cavus foot deformity. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LIKEGKILKISARNGDTQERYLFLFNDMLLYCSPRLRLIGQKYKVRARFDVDGMQVLEGDNLETPHTFYV
RGKQRSLELQASTQEEKAEWVDAI
>gnl|CDD|275424 cd13389, PH1_FGD5_FGD6, FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal Pleckstrin Homology (PH) domain. FGD5 regulates promotes angiogenesis of vascular endothelial growth factor (VEGF) in vascular endothelial cells, including network formation, permeability, directional movement, and proliferation. The specific function of FGD6 is unknown. In general, FGDs have a RhoGEF (DH) domain, followed by a PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activate the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the PH domain is involved in intracellular targeting of the DH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LLGQYNIVKPGRKLIKEGELMKVSRKEMQPRYFFLFNDCLLYTTPVQSSGMLKLNNELPLSGMKVKLPED
EEYSNEFQIISTKRSFTLIASSEEERDEWVKALSRAIEEHTKKQRTFAENVSGV
>gnl|CDD|275425 cd13390, PH_LARG, Leukemia-associated Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain. LARG (also called RhoGEF12) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. RhoGEFs activate Rho GTPases regulating cytoskeletal structure, gene transcription, and cell migration. LARG contains a N-terminal extension, followed by Dbl homology (DH)-PH domains which bind and catalyze the exchange of GDP for GTP on RhoA in addition to a RGS domain. The active site of RhoA adopts two distinct GDP-excluding conformations among the four unique complexes in the asymmetric unit. The LARG PH domain also contains a potential protein-docking site. LARG forms a homotetramer via its DH domains. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
DLSSLKQSEYPMIDELRNLDLTKRKMIHEGPLTWKVNRDKTIDLYTLLLEDILVLLQKQDDRLVLRCHSK
ILASTADSKHTFSPVIKLNTVLVRQVATDNKAFFVISMSENGAQIYELVAQTVSEKTVWQDLITRMAA
>gnl|CDD|275426 cd13391, PH_PRG, PDZ Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain. PRG (also called RhoGEF11) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. RhoGEFs activate Rho GTPases regulating cytoskeletal structure, gene transcription, and cell migration. PRG contains an N-terminal PDZ domain, a regulators of G-protein signaling-like (RGSL) domain, a linker region, and a C-terminal Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. As is the case in p115-RhoGEF, it is thought that the PRG activated by relieving autoinhibition caused by the linker region. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RLDATALERASNPLAAEFKNLDLTTRRMIHEGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLVLKCH
SKTAVGSSDSKQTFSPVLKLNSVLIRSVATDKRALFIICTSKLGPQIYELVALTSSEKNTWMELLEEAVR
NA
>gnl|CDD|275427 cd13392, PH_AKAP13, A-kinase anchoring protein 13 Pleckstrin homology (PH) domain. The Rho-specific GEF activity of AKAP13 (also called Brx-1, AKAP-Lbc, and proto-Lbc) mediates signaling downstream of G-protein coupled receptors and Toll-like receptor 2. It plays a role in cell growth, cell development and actin fiber formation. Protein kinase A (PKA) binds and phosphorylates AKAP13, regulating its Rho-GEF activity. Alternative splicing of this gene in humans has at least 3 transcript variants encoding different isoforms (i.e. proto-/onco-Lymphoid blast crisis, Lbc and breast cancer nuclear receptor-binding auxiliary protein, Brx) containing a dbl oncogene homology (DH) domain and PH domain which are required for full transforming activity. The DH domain is associated with guanine nucleotide exchange activation while the PH domain has multiple functions including determine protein sub-cellular localisation via phosphoinositide interactions, while others bind protein partners. Other ligands include protein kinase C which is bound by the PH domain of AKAP13, serving to activate protein kinase D and mobilize a cardiac hypertrophy signaling pathway. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LVRDGPVSLKNTAGRLKEVQAVLLSDVLVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLI
SMGIADPEMVEVHASSKEERNSWMQIIQDTINT
>gnl|CDD|275428 cd13393, PH_ARHGEF2, Rho guanine nucleotide exchange factor 2 Pleckstrin homology (PH) domain. ARHGEF2, also called GEF-H1, acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. ARHGEF2 contains a C1 domain followed by Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RRKLIHDGCLLWKTASGRFKDVQVLLMTDVLVFLQEKDQKYIFPTLDKPAVISLQNLIVRDIANQEKGMF
LISAAPPEMYEVHAASRDDRNTWMRLIQQTVKTCPSREEFPLIETE
>gnl|CDD|240521 cd13394, Syo1_like, Fungal symportin 1 (syo1) and similar proteins. This family of eukaryotic proteins includes Saccharomyces cerevisiae Ydl063c and Chaetomium thermophilum Syo1, which mediate the co-import of two ribosomal proteins, Rpl5 and Rpl11 (which both interact with 5S rRNA) into the nucleus. Import precedes their association with rRNA and subsequent ribosome assembly in the nucleolus. The primary structure of syo1 is a mixture of Armadillo- (ARM, N-terminal part of syo1) and HEAT-repeats (C-terminal part of syo1)
GKSKKKRRNQRARLNPIGKPSSHSGKDAEKDEALREKKILPLLEKLQSPSANDRSMALGAISNLIEDPSM
RKLLLKEKLVQILIERLLDDSNTEVVVEAFGALRNLAIEEGYDVCVHLWRKDILTPLEALLKKISSSLEA
LEEDPSKAKKESQRLLFDFAENVLSLLWNLAEGSDEILSAVNKEDLLLFLLAILINFLTSKLPTSLFNAA
LQCLYTLSEDNPEFIDKLSSDPEILGNLLDIVSSDPSSSNILLKVLVCGILLNILEVLSWLAGKDAAADA
ILLPILSAILSILALEILANICKELDKKDDEAMEDEQSDEDEEEDEDDEASETLVPELSPLEISLDLLTA
LLELIAPTPESVEPILPSSTIEELPPPLSKLLLSLHSRALECLNNLLWLFLSLELGGDWNNSLQQLWDLL
AQLIFKDVISADLELLEAATSVLWALLKSLGGEILLQQNTHDFIQSLIEASKTDADLELRVRCVGVLGSL
AQVPGNIEVNKEIGQFLLELLTKLPNTPPEVLVEALNAIFDIYGDETFDYDPPVFVQGGYLKLLEKLVPK
LKAMFKKIDKRKDPELRERADEALINLTRFIKYKKSE
>gnl|CDD|466846 cd13395, ASKHA_NBD_Arp4_ACTL6-like, nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily. The Arp4-like subfamily includes Arp4, also called actin-like protein 4, from fungi and plants. Saccharomyces cerevisiae Arp4 acts synergistically with Arp8 to depolymerize F-actin; it binds ATP, but unlike conventional actin, does not form filaments. It is a component of the NuA4 histone acetyltransferase complex, the chromatin-remodeling INO80 complex and the SWR1 chromatin remodeling complex. Arabidopsis thaliana Arp4 is involved in several developmental processes including organization of plant organs, flowering time, anther development, flower senescence and fertility, probably by regulating the chromatin structure. This family also includes human homologs of yeast and plant, which are actin-like protein 6A (encoded by the ACTL6A gene; also known as ArpNbeta, 53 kDa BRG1-associated factor A/BRG1-associated factor 53A/BAF35A, and INO80 complex subunit K/INO80K) and actin-like protein 6B (encoded by the ACTL6B gene; also known as ArpNalpha, 53 kDa BRG1-associated factor B/BRG1-associated factor 53B/BAF35B). ACTL6A and ACTL6B are involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). They are components of numerous complexes with chromatin remodeling and histone acetyltransferase activity. ACTL6A is also a putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Schizosaccharomyces pombe actin-related protein 42 (Arp42) is also included in this family. It is also a component of SWI/SNF and RSC complexes
GDEVGALVLDIGSYSTRAGYAGEDTPKAVFPSVVGVVTDDDDAEDYVGGSGEKKRKYYIGTNSIGVPRPN
MEVISPLKDGLIEDWDAFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFL
AKNAVLSAFANGRSTALVVDSGATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIEIIPRY
MIKSKEPVEGGAPAKYTKKDLPNTTSSYHRYMVRRVLQDFKESVCQVSDSPFDESEAASIPTVSYELPDG
YNIEFGAERFKIPELLFDPSLVKGIPAPPSEGNELLGLPQLVYTSIGSCDVDIRPELYGNVVLTGGNSLL
PGFTDRLNRELSEKAPGSLKLKILASGNTVERRFSSWIGGSILASLGSFQQMWISKQEYEEHG
>gnl|CDD|466847 cd13396, ASKHA_NBD_AtArp8-like, nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and similar proteins. Arabidopsis thaliana ARP8, also called F-box protein ARP8, is an F-Box protein localized to the nucleolus. It is ubiquitously expressed in all organs and cell types and has a cell cycle-dependent subcellular pattern of distribution: it is localized to the nucleolus in interphase cells and dispersed in the cytoplasm in mitotic cells
IIIDGGSGYCKFGWSNYASPSGRLATFLEFGNIESPMYARLCHFVFTIMTRMQVKPSRQPVVVSLPLCHS
DDTESAAASRRQLRGTIFNVLFDMNVPAVCAVDQAVLALYAANRTSGIVVNIGFRVTTIVPVYRGRVMHD
IGVEVVGQGALRLTGFLKELMQQNGIRFPSLYTVRTIKEKLCYVAEDYEAELAKDTQASCEVAGEGWFTL
SNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVHSQGDDGWFKTIVLSGGSACLPGLSERLEREL
RKLLPKSLSEGIRIIPPPLGPDSAWQGAKLISNLSNFPDGWCITKKQFRNKP
>gnl|CDD|466848 cd13397, ASKHA_NBD_actin_Arp-T1-3, nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar proteins. The family includes actin and human actin-related proteins T1, T2, and T3. Actin is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. It is a highly dynamic structural protein network involved in processes such as cell contraction, cell motility, vesicle trafficking, intracellular organization, cytokinesis, endocytosis and apoptosis. Arp-T1, encoded by ACTRT1/ARPT1 gene expressed in testis, negatively regulates the Hedgehog (SHH) signaling, binds to the promoter of the SHH signaling mediator, GLI1, and inhibits its expression. Arp-T2 (also called actin-related protein M2; encoded by ACTRT2/ARPM2 gene expressed in testis and various other cell types) and Arp-T3 (also called actin-related protein M1; encoded by ACTRT3/ARPM1 gene expressed in all tested human tissues) play general roles in the organization of the cytoskeleton like other cytoplasmic actin-related proteins
PAVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKYKAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGI
VTNWDDMEKIWHHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSS
GRTTGLVLDSGDGVTHTVPIYEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEK
LCYVALDYEEELKKKSEELEKEYTLPDGQVIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDI
DIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSSTKVKVIAPPERKYSVWIGGSILASLSTFKSMWI
TRAEYDEFG
>gnl|CDD|381602 cd13399, Slt35-like, Slt35-like lytic transglycosylase. Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL)
YGVPPGILAAILGVESGFGPNAGGSPAGAQGIAQFMPSTWKAYGVDGNGDGKADPFNPEDAIASAANYLC
RHGWDLNAFLGEDNFLALAAYNAGPGAYANAVLELAAT
>gnl|CDD|381603 cd13400, LT_IagB-like, Escherichia coli invasion protein IagB and similar proteins. Lytic transglycosylase-like protein, similar to Escherichia coli invasion protein IagB. IagB is encoded within a pathogenicity island in Salmonella enterica and has been shown to degrade polymeric peptidoglycan. IagB-like invasion proteins are implicated in the invasion of eukaryotic host cells by bacteria. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Members of this family resemble the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda
YGVPPRLLRAIAKVESGFNPNAINRNKNGSYDIGLMQINSIWLPELARYGITREELLNDPCTNIYVGAWI
LARNIKRYGNTWKAVGAYNSGTPKKNDKYARKVYRIYRR
>gnl|CDD|381604 cd13401, Slt70-like, 70kDa soluble lytic transglycosylase (Slt70) and similar proteins. Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda
RYPLPYRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLPYYSPR
DLFDPEYNIRLGSAYLAELLDRFDGNPVLALAAYNAGPGRVRRWLKRRGDLDPDLWIETIPFSETRNYVK
RVLENYVVYRAL
>gnl|CDD|381605 cd13402, LT_TF-like, lytic transglycosylase-like domain of tail fiber-like proteins and similar domains. These tail fiber-like proteins are multi-domain proteins that include a lytic transglycosylase (LT) domain. Members of the LT family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, and the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL). LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue
LNALLRQIQTESGGNPNAINNWDSNAKAGHPSKGLMQVIPPTFAAYAPPGHGNILNPLDNILAAINYAKA
RYGSGFALAAGGGGGGYANGGIVTKGLAEVGEGNKPEEVIPLDPAKR
>gnl|CDD|381606 cd13403, MLTF-like, membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins. This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue
FKKYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPSTARELGVNDRLDPEQNIHAGAKYLRY
LRDRFPPDIDEPDRLKFALAAYNAGPGHVRDARRLAKKYGLNPNVWFDNVEVLPLLKSPYYDPVVKYGYA
RGRETVNYVRNIRKYYDAYKQ
>gnl|CDD|259831 cd13404, UreI_AmiS_like, UreI/AmiS family, proton-gated urea channel and putative amide transporters. This family includes UreI proton-gated urea channels as well as putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and CO2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity
GLGLLYVGAVLFVNGLMLLGKVPVKSASVLNLFVGALQCVVPTVMLIQAQGDSSSVLAAAGLLLFGFTYL
YVAINNLAGFDPRGIGWYSLFVACAAVPYAFLSFYSLTVSNGPWFGVIWLAWAVLWTLFFLVLGLKEPLS
RFTGWLAILEGIPTCWIPAFLLLTGNF
>gnl|CDD|276910 cd13405, TNFRSF14_teleost, Tumor necrosis factor receptor superfamily member 14 (TNFRSF14) in teleost; also known as herpes virus entry mediator (HVEM). This subfamily of TNFRSF14 (also known as herpes virus entry mediator or HVEM, ATAR, CD270, HVEA, LIGHTR, TR2) is found in teleosts, many of which are as yet uncharacterized. It regulates T-cell immune responses by activating inflammatory as well as inhibitory signaling pathways. HVEM acts as a receptor for the canonical TNF-related ligand LIGHT (lymphotoxin-like), which exhibits inducible expression, and competes with herpes simplex virus glycoprotein D for HVEM. It also acts as a ligand for the immunoglobulin superfamily proteins BTLA (B and T lymphocyte attenuator) and CD160, a feature distinguishing HVEM from other immune regulatory molecules, thus, creating a functionally diverse set of intrinsic and bidirectional signaling pathways. HVEM is highly expressed in the gut epithelium. Genome-wide association studies have shown that HVEM is an inflammatory bowel disease (IBD) risk gene, suggesting that HVEM could have a regulatory role influencing the regulation of epithelial barrier, host defense, and the microbiota. Mouse models have revealed that HVEM is involved in colitis pathogenesis, mucosal host defense, and epithelial immunity, thus acting as a mucosal gatekeeper with multiple regulatory functions in the mucosa. HVEM plays a critical role in both tumor progression and resistance to antitumor immune responses, possibly through direct and indirect mechanisms. It is known to be expressed in several human malignancies, including esophageal squamous cell carcinoma, follicular lymphoma, and melanoma. HVEM network may therefore be an attractive target for drug intervention. In Asian seabass, the up-regulation of differentially expressed TNFRSF14 gene has been observed
CGPAEYEINGECCPMCPPGSRVSRHCTEDTSTSCVPCPDGTYMDEPNGLEKCFPCTNCDPGFGLRVKQGC
TYTSDTVCEPLEGFYCIDSTKDGCSAAQRHSSCKPGQYIKQ
>gnl|CDD|276911 cd13406, TNFRSF4, Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40. TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus
LHCVGDTYPSGEKCCHECPPGEGMESRCTGTQDTVCSPCEPGFYNEAVNYEPCKPCTQCNQRSGSEEKQK
CTKTSDTVCRCRPGTQPLDSYKPGVDCVPCPPGHFSRGDNQACKPWTNCSLAGKRTLRPGSSTSDAVCED
RS
>gnl|CDD|276912 cd13407, TNFRSF5, Tumor necrosis factor receptor superfamily member 5 (TNFRSF5), also known as CD40. TNFRSF5 (commonly known as CD40 and also as CDW40, p50, Bp50) is widely expressed in diverse cell types including B lymphocytes, dendritic cells, platelets, monocytes, endothelial cells, and fibroblasts. It is essential in mediating a wide variety of immune and inflammatory responses, including T cell-dependent immunoglobulin class switching, memory B cell development, and germinal center formation. Its natural immunomodulating ligand is CD40L, and a primary defect in the CD40/CD40L system is associated with X-linked hyper-IgM (XHIM) syndrome. It is also involved in tumorigenesis; CD40 expression is significantly higher in gastric carcinomas and it is associated with the lymphatic metastasis of cancer cells and their tumor node metastasis (TNM) classification. Upregulated levels of CD40/CD40L on B cells and T cells may play an important role in the immune pathogenesis of breast cancer. Consequently, the CD40/CD40L system serves as a link between tumorigenesis, atherosclerosis, and the immune system, and offers a potential target for drug therapy for related diseases, such as cancer, atherosclerosis, diabetes mellitus, and immunological rejection
CREKQYLHNGRCCSLCPPGQKLVSDCTEATDTECLPCEEGEFQDTWNRERHCHQHRYCDPNLGLRVQTEG
TAETDTTCTCQEGQHCTSEACETCALHTSCKPGFGVKQIATGVSDTICEPCPVGFFSNVSSAFEKCHPWT
SCETKGLVELQAGTNKTDVVC
>gnl|CDD|276913 cd13408, TNFRSF7, Tumor necrosis factor receptor superfamily member 7 (TNFRSF7), also known as CD27. TNFRSF7 (also known as CD27, T14, S152, Tp55, S152, LPFS2) has a key role in the generation of immunological memory via effects on T-cell expansion and survival, and B cell development. It binds to ligand CD70, and plays a key role in regulating B-cell activation and immunoglobulin synthesis. CD27 transduces signals that lead to the activation of NF-kappaB and MAPK8/JNK, and mediates the signaling process through adaptor proteins TRAF2 and TRAF5. CD27-binding protein (SIVA), a pro-apoptotic protein, can bind to CD27 and may play an important role in the apoptosis induced by this receptor. The potential role of the CD27/CD70 pathway in the course of inflammatory diseases, such as arthritis, and inflammatory bowel disease, suggests that CD70 may be a target for immune intervention. The expression of CD27 and CD44 molecules correlates with the differentiation stage of B cell precursors and has been shown to have a biological significance in acute lymphoblastic leukemia
PPPCWLWVLGTLAGLSATPAPKSCPERHYWAQGKLCCQMCEPGTFLVKDCDQHGKAAQCDPCIPGVSFSP
DHHARPHCESCRHCNSGLLIRNCTITANTECACPKGWQCRDKECTECDPLP
>gnl|CDD|276914 cd13409, TNFRSF8, Tumor necrosis factor receptor superfamily member 8 (TNFRSF8), also known as CD30. TNFRSF8 (also known as CD30, Ki-1, D1S166E) is expressed by activated T and B cells. It transduces signals that lead to the activation of NF-kappaB, mediated by the adaptor proteins TRAF2 and TRAF5. This receptor is a positive regulator of apoptosis, and has been shown to limit the proliferative potential of auto-reactive CD8 effector T cells and protect the body against autoimmunity. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported. CD30 is expressed in malignant Hodgkin and Reed-Sternberg cells on the surface of extracellular vesicles, facilitating CD30-CD30L interaction between cell types. This receptor is also associated with anaplastic large cell lymphoma. It is expressed in embryonal carcinoma, but not in seminoma, making it a useful marker in distinguishing between these germ cell tumors. Since CD30 has restricted expression in normal tissues, it is an optimal target for selectively eliminating CD30-expressing neoplastic cells by specific toxin-conjugated monoclonal antibodies (mAbs)
LSLRAKLTLFSPGTLRAPTMRRASAATCDGDPSRYYDEASSKCCYRCPPGLSPQQPCPQGSADCRKQCEP
DYYLDEDGRCTACVSCSGDDLVEKAPCSWNSSRVCECRPGMFCATSATNSCARCVPHSVC
>gnl|CDD|276915 cd13410, TNFRSF9, Tumor necrosis factor receptor superfamily member 9 (TNFRSF9), also known as CD137. TNFRSF9 (also known as CD137, ILA, 4-1BB) plays a role in the immunobiology of human cancer where it is preferentially expressed on tumor-reactive subset of tumor-infiltrating lymphocytes. It can be expressed by activated T cells, but to a larger extent on CD8 than on CD4 T cells. In addition, CD137 expression is found on dendritic cells, follicular dendritic cells, natural killer cells, granulocytes and cells of blood vessel walls at sites of inflammation. It transduces signals that lead to the activation of NF-kappaB, mediated by the TRAF adaptor proteins. CD137 contributes to the clonal expansion, survival, and development of T cells. It can also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. CD137 is modulated by SAHA treatment in breast cancer cells, suggesting that the combination of SAHA with this receptor could be a new therapeutic approach for the treatment of tumors
SVQDSCSNCPAGTFCGKNKDQTCIPCPPNSFSSTGGQQTCDICRKCEGVFRTKKPCSSTSNAECECVPGF
HCLGPGCSMCEPDCKQGQELTKEGCKDCSFGTFNDQEGGVCRPWTNCSLDGKSVLVNGTKERDVVCGP
>gnl|CDD|276916 cd13411, TNFRSF11A, Tumor necrosis factor receptor superfamily member 11A (TNFRSF11A), also known as receptor activator of nuclear factor-kappaB (RANK). TNFRSF11A (also known as RANK, FEO, OFE, ODFR, OSTS, PDB2, CD26, OPTB7, TRANCER, LOH18CR1) induces the activation of NF-kappa B and MAPK8/JNK through interactions with various TRAF adaptor proteins. This receptor and its ligand are important regulators of the interaction between T cells and dendritic cells. The receptor is also an essential mediator for osteoclast and lymph node development. Mutations at this locus have been associated with familial expansile osteolysis, autosomal recessive osteopetrosis, and Juvenile Paget's disease (JPD) of bone. Alternatively spliced transcript variants have been described for this locus. Mutation analysis may improve diagnosis, prognostication, recurrence risk assessment, and perhaps treatment selection among the monogenic disorders of RANKL/OPG/RANK activation
PCSSERHYEYSGRCCSKCEPGKYMSSKCTVTSDSVCLPCGPDEYLDTWNEEDKCLLHKVCDAGKALVAVD
PGNSTAPRRCACTAGYHWSEDCDCCRRNTECAPGFGAQHPVQLNKDTVCEPCLVGYFSDVFSSTDKCKPW
TNCTILGLEEAVPGTNKSDVVCS
>gnl|CDD|276917 cd13412, TNFRSF11B_teleost, Tumor necrosis factor receptor superfamily 11B (TNFRSF11B) in teleost; also known as Osteoprotegerin (OPG). This subfamily of TNFRSF11B (also known as Osteoprotegerin, OPG, TR1, OCIF) is found in teleosts. It is a secreted glycoprotein that regulates bone resorption. It binds to two ligands, RANKL (receptor activator of nuclear factor kappaB ligand, also known as osteoprotegerin ligand, OPGL, TRANCE, TNF-related activation induced cytokine), a critical cytokine for osteoclast differentiation, and TRAIL (TNF-related apoptosis-inducing ligand), involved in immune surveillance. Therefore, acting as a decoy receptor for RANKL and TRAIL, OPG inhibits the regulatory effects of nuclear factor-kappaB on inflammation, skeletal, and vascular systems, and prevents TRAIL-induced apoptosis. Studies in mice counterparts suggest that this protein and its ligand also play a role in lymph-node organogenesis and vascular calcification. Circulating OPG levels have emerged as independent biomarkers of cardiovascular disease (CVD) in patients with acute or chronic heart disease. OPG has also been implicated in various inflammations and linked to diabetes and poor glycemic control. Alternatively spliced transcript variants of this gene have been reported, although their full length nature has not been determined. Genetic analysis of the Japanese rice fish medaka (Oryzias latipes) has shown that entire networks for bone formation are conserved between teleosts and mammals; enabling medaka to be used as a genetic model to monitor bone homeostasis in vivo
CGADAAPTYEHRDPSTGKILTCKKCPPGTHMAAHCTATTQTKCLPCPAAHYTELWNYLPRCLYCNNFCSE
NQEVEIECSATNNRVCRCKEGYYMDSDFCIRHTECGPGYGVKTKGTTKQDTVCEKCPSG
>gnl|CDD|276918 cd13413, TNFRSF12A, Tumor necrosis factor receptor superfamily member 12A (TNFRSFA), also known as receptor fibroblast growth factor inducible 14 (FN14). TNFRSF12A (also known as receptor fibroblast growth factor inducible 14, FN14, CD266, TWEAKR) is induced by a large variety of growth factors including Fibroblast Growth Factor 1 (FGF1), FGF2, Platelet-Derived Growth Factor (PDGF), Epidermal Growth Factor (EGF) and Vascular Endothelial Growth Factor (VEGF), as well as cytokines such as tumor necrosis factor alpha (TNFalpha), Interleukin-1beta (IL-1beta), Interferon gamma (IFNgamma), and transforming growth factor-beta (TGF-beta). FN14 is expressed on a wide variety of different cell types and binds the ligand TWEAK (tumor necrosis factor-like weak inducer of apoptosis) to activate several signaling cascades through activation of NF-kappaB signaling mediated by adaptor TRAF proteins. The FN14/TWEAK pathway controls a range of cellular activities such as proliferation, differentiation, and apoptosis, and has diverse biological functions in pathological mechanisms like inflammation and fibrosis that are associated with cardiovascular diseases (CVDs). The complex is a positive regulator of cardiac hypertrophy and it has been shown that deletion of FN14 receptor protects from right heart fibrosis and dysfunction; the TWEAK/Fn14 axis could be a potential new therapeutic target for achieving cardiac protection in patients with CVDs. FN14 expression is also stimulated under specific atrophic conditions, such as denervation, immobilization, and starvation, leading to activation of TWEAK/Fn14 signaling and eventually skeletal muscle atrophy. FN14 is also a factor that promotes prostate cancer bone metastasis
LPRLLVLGFVLVLLRSAAGQAAATSPCPGGSSWSPDLDKCMDCSSCPARPKSDFCLGCGAAPPPPFPLLW
PILGGALGLVLLLALLSGTLVWRRCRRREKFTTPIEETGGEGCPGVA
>gnl|CDD|276919 cd13414, TNFRSF17, Tumor necrosis factor receptor superfamily member 17 (TNFRSF17), also known as B cell maturation antigen (BCMA), as well as TNFRSF13A. TNFRSF17 (also known as TNFRSF13A, B cell maturation antigen or BCMA, CD269) is predominantly expressed on terminally differentiated B cells, including multiple myeloma cells, and is important for B cell development and autoimmune response. Upon binding to its ligands, B cell activator of the TNF family (BAFF, also known as TNSF13B, TALL-1, BLyS, zTNF4), and a proliferation inducing ligand (APRIL), BCMA activates NF-kappaB and MAPK8/JNK; it has a higher affinity for APRIL than for BAFF. This receptor may transduce signals for cell survival and proliferation by binding to TRAF1, TRAF2, and TRAF3. BCMA expression has also been linked to a number of cancers, autoimmune disorders, and infectious diseases. It has been shown that although BCMA does not play a role in normal B cell homeostasis, it is critical for the long-term survival of bone marrow plasma cells. BCMA is expressed in a number of hematologic malignancies, including both Hodgkin's and non-Hodgkin's lymphomas, as well as primary tumor cells and cell lines of multiple myeloma, playing a critical role in protecting myeloma cells from apoptosis. BCMA has been identified as a promising chimeric antigen receptor (CAR) target for multiple myeloma; CARs are synthetic transmembrane proteins used to redirect autologous T cells with a new specificity for antigens on the surface of cancer cells. BCMA may also be implicated in the context of both viral and fungal infections; peripheral blood B cells isolated from HIV+ viremic patients have increased expression levels of BCMA, and significant decreased levels are found during fungal infection with C. neoformans. BCMA has been linked to mucosal immunity; its signaling in B cells and non-B cells is important for driving protective IgA responses. Also, abnormal expression or signaling of BCMA in the gut may be relevant to diseases, such as irritable bowel disease and ulcerative colitis
MAQQCFQNEYFDSLLHACKPCHLRCSNTPPLPCQSYCNASVTNSVKGTNVILWICLGLSLILSLTVFLLM
FLLRKMSSEPSKDELKNTGITLQNKANALADLSESRIGEEILLPRSLLEYTVEECTCEDCVKSKPKADSD
HFFPLPAMEEGATILVTTKTNDYCK
>gnl|CDD|276920 cd13415, TNFRSF13B, Tumor necrosis factor receptor superfamily member 13B (TNFRSF13B), also known as transmembrane activator and calcium modulator and cyclophilin ligand interactor (TACI). TNFRSF13B (also known as transmembrane activator and calcium modulator and cyclophilin ligand interactor (TACI), CVID, RYZN, CD267, CVID2, TNFRSF14B) is mainly expressed on B cells and binds strongly to B cell activating factor (BAFF) and weakly to a proliferation-inducing ligand (APRIL). TACI-APRIL interactions induce B-cell differentiation, whereas TACI-BAFF ligation negatively regulates B-cell functions. In humans, TACI is expressed on memory B cells and TACI mutations are detected in 8-10% of common variable immunodeficiency (CVID) patients, making it the most frequently mutated gene for the disease. Coexisting morbidities in CVID include bronchiectasis, autoimmunity, and malignancies. However, TNFRSF13B/TACI defects alone do not result in CVID but may also be found frequently in distinct clinical phenotypes, including benign lymphoproliferation and IgG subclass deficiencies. Over-expression of TACI has been detected in multiple myeloma and thyroid carcinoma; correlative analyses suggest that TACI expression is a useful prognostic marker for lymphoma
CPDEQYWDSLVGQCISCSLICSRRSVRTCAAFCKSMSCNKEQGKYYDHLLKDCISCASVCGQHPKQCAPF
CENKLRSRVNLPPPLRRQQSGETETRSDNSGRYQGSEHRGSEAGPALPGPKLSADQLLLVYCTLGLCLCA
IVCCFLVAVACFLRRRGEPLSCQPAAGPCRLRAKSSKDRLVEAGSVGDGVPEPVETCSFCFPEHRSPTQE
SA
>gnl|CDD|276921 cd13416, TNFRSF16, Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271. TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases
EACPSGQYTSSGECCEQCPPGEGVARPCGDNQTVCEPCLDGVTFSDVVSHTEPCQPCTRCPGLMSMRAPC
TATHDTVCECAYGYYLDEDSGTCEPCTVCPPGQGVVQSCGPNQDTVCEACPEGTYSDEDSSTDPCLPCTV
CEDGEVELRECTPVSDTVC
>gnl|CDD|276922 cd13417, TNFRSF18, Tumor necrosis factor receptor superfamily member 18 (TNFRSF18), also known as glucocorticoid-induced tumor necrosis factor receptor family-related protein (GITR). TNFRSF18 (also known as activation-inducible TNF receptor (AITR), glucocorticoid-induced tumor necrosis factor receptor family-related protein (GITR), CD357, GITR-D) has increased expression upon T-cell activation, and is thought to play a key role in dominant immunological self-tolerance maintained by CD25(+)CD4(+) regulatory T cells. In inflammatory cells, GITR expression indicates a possible molecular link between steroid use and complicated acute sigmoid diverticulitis; increased MMP-9 expression by GITR signaling might explain morphological changes in the colonic wall in diverticulitis. Its ligand, GITRL, activates GITR which could then influence the activity of effector and regulatory T cells, participating in the development of several autoimmune and inflammatory diseases, including autoimmune thyroid disease and rheumatoid arthritis. In systemic lupus erythematosus (SLE) patients, serum GITRL levels are increased compared with healthy controls. GITR and its ligand, GITRL, are possibly involved in the pathogenesis of primary Sjogren's syndrome (pSS). GITR is inactivated during tumor progression in Multiple Myeloma (MM); restoration of GITR expression in GITR deficient MM cells leads to inhibition of MM proliferation and induction of apoptosis, thus playing a pivotal role in MM pathogenesis and disease progression. Regulatory T-cells (Tregs) in liver tumor up-regulate the expression of GITR compared with Tregs in tumor-free liver tissue and blood. Regulatory single nucleotide polymorphisms (SNPs) in the promoter regions of the TNFRSF18 gene have been identified in a group of male Gabonese individuals exposed to a wide array of parasitic diseases such as malaria, filariasis and schistosomiasis, and may serve as a basis to study parasite susceptibility in association studies
RCCRKCPSEEADAPCCDAEGDCKCVQPGFHCGDPQCKTCKKHPCPPGQEVQRQGKFDFGFECVPCANGTF
SDGHDGHCKPWTDCSQFGFLTIFPGNKTHNAVCGPGPPPPEEDGHLTILAIPTAACILVL
>gnl|CDD|276923 cd13418, TNFRSF19, Tumor necrosis factor receptor superfamily member 19 (TNFRSF19), also known as TROY. TNFRSF19 (also known as TAJ; TROY; TRADE; TAJ-alpha) is expressed in progenitor cells of the hippocampus, thalamus, and cerebral cortex and highly expressed during embryonic development. It has been shown to interact with TRAF family members, and to activate JNK signaling pathway when overexpressed in cells. It is frequently overexpressed in colorectal cancer cell lines and primary colorectal carcinomas. TNFRSF19 is a beta-catenin target gene, in mesenchymal stem cells, and also activates NF-kappaB signaling, showing that beta-catenin regulates NF-kappaB activity via TNFRSF19. Since Wnt/beta-catenin signaling plays a crucial role in the regulation of colon tissue regeneration and the development of colon tumors, TNFRSF19 may contribute to the development of colorectal tumors. These findings define a role for death receptors DR6 and TROY in CNS-specific vascular development. TNFRSF19 has been shown to promote glioblastoma (GBM) survival signaling and therefore targeting it may increase tumor vulnerability and improve therapeutic response in glioblastoma. It may play an important role in myelin-associated inhibitory factors (MAIFs)-induced inhibition of neurite outgrowth in the postnatal central nervous system (CNS) or on axon regeneration following CNS injury
DCREQEYRDKAGNCIPCRQCGPGMELSKECGFGYGEDAQCVPCRPNRFKEDWGFQKCKPCLDCALLNRFQ
KANCSATSNAVCGDCLPGFYRKTKLVGFQDMECVPCGDPPPPYEPHC
>gnl|CDD|276924 cd13419, TNFRSF19L, tumor necrosis factor receptor superfamily member 19-like (TNFRSF19L), also known as receptor expressed in lymphoid tissues (RELT). TNFRSF19L (also known as receptor expressed in lymphoid tissues (RELT)) is especially abundant in hematologic tissues and can stimulate the proliferation of T-cells. It serves as a substrate for the closely related kinases, odd-skipped related transcription factor 1 (OSR1) and STE20/SPS1-related proline/alanine-rich kinase (SPAK); RELT binds SPAK and uses it to mediate p38 and JNK activation, rather than rely on the canonical TRAF pathways for its function. RELT is capable of stimulating T-cell proliferation in the presence of CD3 signaling, which suggests its regulatory role in immune response. It interacts with phospholipid scramblase 1 (PLSCR1), an interferon-inducible protein that mediates antiviral activity against DNA and RNA viruses; PLSCR1 is a regulator of hepatitis B virus X (HBV X) protein. RELT and PLSCR1 co-localize in intracellular regions of human embryonic kidney-293 cells, with RELT over-expression appearing to alter the localization of PLSCR1
CVPCLQCPPGQEPDRACGQGQGLGVLCRSCPPGTFSDSLGSEPCRPHTSCEVLKRKVATSGTATSDAVCG
DCLPGFHSPAAPPPSTCLPCS
>gnl|CDD|276925 cd13420, TNFRSF25, tumor necrosis factor receptor superfamily member 25 (TNFRSF25), also known as death receptor 3 (DR3). TNFRSF25 (also known as death receptor 3 (DR3), death domain receptor 3 (DDR3), apoptosis-mediating receptor, lymphocyte associated receptor of death (LARD), apoptosis inducing receptor (AIR), APO-3, translocating chain-association membrane protein (TRAMP), WSL-1, WSL-LR or TNFRSF12) is preferentially expressed in thymocytes and lymphocytes, and may play a role in regulating lymphocyte homeostasis. It has been detected in lymphocyte-rich tissues such as colon, intestine, thymus and spleen, as well as in the prostate. Various death domain containing adaptor proteins mediate the signal transduction of this receptor; it activates nuclear factor kappa-B (NFkB) and induces cell apoptosis by associating with TNFRSF1A-associated via death domain (TRADD), which is known to mediate signal transduction of tumor necrosis factor receptors. DR3 associates with tumor necrosis factor (TNF)-like cytokine 1A (TL1A also known as TNFSF15) on activated lymphocytes and induces pro-inflammatory signals; TL1A also binds decoy receptor DcR3 (also known as TNFRSF6B). DR3/DcR3/TL1A expression is increased in both serum and inflamed tissues in autoimmune diseases such as in several autoimmune diseases, including inflammatory bowel disease (IBD), rheumatoid arthritis (RA), allergic asthma, experimental autoimmune encephalomyelitis, type 1 diabetes, ankylosing spondylitis (AS), and primary biliary cirrhosis (PBC), making modulation of TL1A-DR3 interaction a potential therapeutic target
KCDCASEFQKRNGPFCCRGCPAGHYLKAPCTEPCGNSTCLPCPRGTFLARENHHKTDCTRCQACDEQASQ
VALENCSAVSDTHCGCESGWFVECSVKDCVSSSPFSCKPCLDCG
>gnl|CDD|276926 cd13421, TNFRSF_EDAR, Tumor necrosis factor receptor superfamily member ectodysplasin A receptor (EDAR). Ectodysplasin A receptor (EDAR, also known as DL, ED3, ED5, ED1R, EDA3, HRM1, EDA1R, ECTD10A, ECTD10B, EDA-A1R) binds the soluble ligand ectodysplasin A and can activate the nuclear factor-kappaB, JNK, and caspase-independent cell death pathways. It is required for the development of hair, teeth, and other ectodermal derivatives. Mutations in this gene result in autosomal dominant and recessive forms of hypohidrotic ectodermal dysplasia. Patients present defects in the development of ectoderm-derived structures resulting in sparse hair, too few teeth (oligodontia), the absence or reduction in the ability to sweat as well as problems with mucous and saliva and the production and formation of pigment cells
LPFLVVSLMCSASAEYSNCGENEYYNQTTGLCQQCPPCRPGEEPYMSCGYGTKDEDYGCVPCPAEKFSKG
GYQICRRHKDCEGFFRATVLTPGDMENDAECGPCLPGYYMLENRPRNIYGMVCYSCLLAPPNTKEC
>gnl|CDD|276927 cd13422, TNFRSF5_teleost, Tumor necrosis factor receptor superfamily member 5 (TNFRSF5) in teleosts; also known as CD40. TNFRSF5 (commonly known as CD40 and also as CDW40, p50, Bp50) is widely expressed in diverse cell types including B lymphocytes, dendritic cells, platelets, monocytes, endothelial cells, and fibroblasts. It is essential in mediating a wide variety of immune and inflammatory responses, including T cell-dependent immunoglobulin class switching, memory B cell development, and germinal center formation. Its natural immunomodulating ligand is CD40L, and a primary defect in the CD40/CD40L system is associated with X-linked hyper-IgM (XHIM) syndrome. It is also involved in tumorigenesis; CD40 expression is significantly higher in gastric carcinomas and it is associated with the lymphatic metastasis of cancer cells and their tumor node metastasis (TNM) classification. Upregulated levels of CD40/CD40L on B cells and T cells may play an important role in the immune pathogenesis of breast cancer. Consequently, the CD40/CD40L system serves as a link between tumorigenesis, atherosclerosis, and the immune system, and offers a potential target for drug therapy for related diseases, such as cancer, atherosclerosis, diabetes mellitus, and immunological rejection. Salmon CD40 and CD40L are widely expressed, particularly in immune tissues, and their importance for the immune response is indicated by their relatively high expression in salmon lymphoid organs and gills
CDPETQYEKDGECCKMCGPGTRMSSDSGCLDPQCQPCGEDEYQDKYTKENKCKRQPYCDPNKNFEISVNK
SKTSRSVCKCKPGFHCSSEECLTCVPHTTCGPGQGVKSKGNHIRDTVCEECPDGTFSNNSSAEGVCKKWT
ECESGYKVEAAGTNTSDNICV
>gnl|CDD|276928 cd13423, TNFRSF6_teleost, Tumor necrosis factor receptor superfamily member 6 (TNFRSF6) in teleosts; also known as fas cell surface death receptor (FasR). This subfamily of TNFRSF6 (also known as fas cell surface death receptor (FasR) or Fas; APT1; CD95; FAS1; APO-1; FASTM; ALPS1A) is found in teleosts. It contains a death domain and plays a central role in the physiological regulation of programmed cell death. In humans, it has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The receptor interactions with the Fas ligand (FasL), allowing the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10; autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, leading to apoptosis. This receptor has also been shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is involved in transducing the proliferating signals in normal diploid fibroblast and T cells. In channel catfish and the Japanese rice fish, medaka, homologs of Fas receptor (FasR), as well as FADD and caspase 8, have been identified and characterized, and likely constitute the teleost equivalent of the death-inducing signaling complex (DISC). FasL/FasR are involved in the initiation of apoptosis and suggest that mechanisms of cell-mediated cytotoxicity in teleosts are similar to those used by mammals; presumably, the mechanism of apoptosis induction via death receptors was evolutionarily established during the appearance of vertebrates
SCEDGTYQHEGLTCCLCPAGQHVEKHCTNNGTDGECEACEDGTYNSHPNSLDSCEPCTSCDPNANLEVEE
RCTPSSDTVCRCKEGHYCDKGEECKVCYPCDTC
>gnl|CDD|276929 cd13424, TNFRSF9_teleost, Tumor necrosis factor receptor superfamily member 9 (TNFRSF9) in teleosts; also known as CD137. This subfamily of TNFRSF9 (also known as CD137, ILA, 4-1BB) is found in teleosts. CD137 plays a role in the immunobiology of human cancer where it is preferentially expressed on tumor-reactive subset of tumor-infiltrating lymphocytes. It can be expressed by activated T cells, but to a larger extent on CD8 than on CD4 T cells. In addition, CD137 expression is found on dendritic cells, follicular dendritic cells, natural killer cells, granulocytes and cells of blood vessel walls at sites of inflammation. It transduces signals that lead to the activation of NF-kappaB, mediated by the TRAF adaptor proteins. CD137 contributes to the clonal expansion, survival, and development of T cells. It can also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. CD137 is modulated by SAHA treatment in breast cancer cells, suggesting that the combination of SAHA with this receptor could be a new therapeutic approach for the treatment of tumors. Mostly, CD137 in teleosts have not been characterized
CKKWEPSGKNYVCCESCHPGNRLVERCGPDPAELCKPCEPGTYTVKPLDYSCYICTQCIGAQVLLKNCTP
SSDTVCGCKEGLRCGDAECSFCVTECGKGQEPLGKRDCRQCPVGTFNDQIHSKCKEWSTSCPDPNELIVF
KGDATSDITC
>gnl|CDD|240448 cd13425, Peptidase_G1_like, Peptidases of the G1 family and homologs that might lack peptidase activity. Some members of this family had been classified earlier as carboxyl peptidases insensitive to pepstatin, and the family has also been called the eqolisin family, due to the fact that the conserved catalytic dyad of the family consists of a glutamate (E) and glutamine (Q) residue. The family is found in fungi and bacteria. This family also includes homologous uncharacterized proteins that might lack peptidase activity
GAYLNSATGAVVSATIVVPTAKNNDSVSAPYAWVGIDGDTYAGAILQIGLDYYKDYNTYDAWXEWGPKNE
KFTYNKGFRPGDTVQXTVYKTSSGNGRATLENTTTGQIVSEIQGTNSPATLTISNAETIAEDFVSYESQR
DAIKATFSVEFTNCTIDNKGKSYGLVTAVITQDQQDGKVFTKVSVAGNNVTISYV
>gnl|CDD|240449 cd13426, Peptidase_G1, Peptidases of the G1 family, including scytalidoglutamic peptidase and aspergillopepsin. Some members of this family had been classified earlier as carboxyl peptidases insensitive to pepstatin, and the family has also been called the eqolisin family, due to the fact that the conserved catalytic dyad of the family consists of a glutamate (E) and glutamine (Q) residue. The family is found in fungi and bacteria
SSNWAGAVLTGPPGTFTSVSGTFTVPTPSGPPGSSGTYAASAWVGIDGDTCSSALLQAGVDFYIDNGSVS
YSAWYEWYPAAAYDFSGFTVSPGDTVTVTVTATSSTSGTVTIENLSTGQTVTKTLTAPSAPLCGTSAEWI
VEDPTVGGSLVPLANFGTVTFTDASATTASGSSVGLSGATIIDIQQNGTVLTSSSISGDSVTVTYV
>gnl|CDD|240450 cd13427, YncM_like, Uncharacterized proteins similar to Bacillus subtilis YncM. Members of this family share close structural similarity with peptidases of the Peptidase_G1 family and may be homologous. They do not appear to share the peptidases' active site, though a bound sulfate ion in the single available structure suggests a functional site at a matching location
IPDGIGGRVISNSGGSWLTTKIYLPSSAKNTGFTGGTAYIYTGFTGNSGVEVDAGLQYSKPETYNDWAPF
LKVGGGNKETYIEGYDPFTYKNGFKPGQDVQMKIYVNYNGNVRLTLSGTAHCEGTTRLITEIENANTNVG
SGNNWKRLTTIAQSDDSQGTYLGKIRSTFSNIKTDGTANTPWVDAQDFAKCTVSGNNVTIDVVN
>gnl|CDD|259832 cd13428, UreI_AmiS, UreI/Amis family, proton-gated urea channel and putative amide transporters. This subfamily includes UreI proton-gated urea channels as well as putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity
GVVLLFVGIVLISNGIGGLGKIDPKSTAVMNFFTGGLSLIINIVVLVQGNENTAYYAAATGLLFAFTYLY
VAINNIFGLDGRPYGWYCLFVAINTLPCAYISFSTGDMRFAIIWLLWGILWFTGFIELVLKKTLGKFVPY
LTIFEGIVTCWIPGFLMLIGRW
>gnl|CDD|259833 cd13429, UreI_AmiS_like_2, UreI/AmiS family, subgroup 2. Putative transporters related to proton-gated urea channel and putative amide transporters. This subfamily includes putative UreI proton-gated urea channels and putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity
NVGLLFVGAVLFINGLVLLGRVDGKSAGVFNLFVGALQVVTPTYLIFQSDGDPWTIFAASGIFLFGFTYL
YVGITNLFGLDGSGLGWYSLWVAIIALVYAIVSFGQFADPVFGVIWLSWAYLWFLFFLLLGLGKENLGPY
TGWVAIVQSWITATVPALLILTGSW
>gnl|CDD|240445 cd13430, LDT_IgD_like, IgD-like repeat domain of mycobacterial L,D-transpeptidases. Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3-_3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain
MPYVMPGDGEVVGVGAPVAIRFDENIADRGAAEKAITITTDPPVEGAFYWLPDGRRVRWRPEHFWKPGTA
VDVAANTYGLDLGEGMFGADNVQLHFQI
>gnl|CDD|240446 cd13431, LDT_IgD_like_1, IgD-like repeat domain of mycobacterial L,D-transpeptidases. Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3-_3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain; this model represents the first (N-terminal) repeat in LdtMt2 and related proteins
GPAPPLPVPVATVSPADGAVVGVAHPVVVTFADPVADRAAAENAIGITVAGPVAGGFSWTDDEPLGWTPT
YFWPAHATVTVGAGGTRTSFRTGDA
>gnl|CDD|240447 cd13432, LDT_IgD_like_2, IgD-like repeat domain of mycobacterial L,D-transpeptidases. Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3-_3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain; this model represents the repeat adjacent to the catalytic domain
TTASVNPLDGETVGVGMPVIVTFDEPVTDRAAVEKALKVTTSPPVEGAWYWLSDREVHWRPKEYWPPGTK
VTVDANLYGVDLGDGVYGQEDRSTTFTIG
>gnl|CDD|240441 cd13433, Na_channel_gate, Inactivation gate of the voltage-gated sodium channel alpha subunits. This region is part of the intracellular linker between domains III and IV of the alpha subunits of voltage-gated sodium channels. It is responsible for fast inactivation of the channel and essential for proper physiological function
DNFNQLKKKYGGGLDIFLTESQKKYYNAMKKLGSKKPQKPIPRPKNKFQGFIFD
>gnl|CDD|259812 cd13434, SPFH_SLPs, Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes proteins similar to stomatin, podocin, and other members of the stomatin-like protein family (SLPs or slipins). The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome. Bacterial and archaebacterial SLPs and many of the eukaryotic family members remain uncharacterized
VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDEL
LSEREEISQQLQEILDEATDPWGIKVERVEIKDIILPQ
>gnl|CDD|259813 cd13435, SPFH_SLP-4, Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in arthropods. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this divergent slipin subgroup remain largely uncharacterized. It contains Drosophila Mec2, the gene for which was identified in a screen for genes required for nephrocyte function; it may function together with Sns in maintaining nephrocyte diaphragm
SGGARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHS
TRLLAATTLRNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAE
AAREARAKVIAAEGEMKSSRALKEASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELLTPLL
>gnl|CDD|259814 cd13436, SPFH_SLP-1, Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in animals. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. The family contains human SLP-1, which has been found to be expressed in the brain, and Caenorhabditis elegans UNC-24, which is a lipid raft-associated protein required for normal locomotion. It may mediate the correct localization of UNC-1. Mutations in the unc-24 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics
GRLQKPRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLN
TSTRTTAQTSLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKVLK
>gnl|CDD|259815 cd13437, SPFH_alloslipin, Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in some eukaryotes and viruses. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This diverse subgroup of the SLPs remains largely uncharacterized
CCPNPYKQVKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDS
VVYYRIIDPYKAIYRIDNVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVE
SILIKDIVLSKDLQQSLSSAAKAKRIGESKIISAKADVESAKLMREAADILDSKAAMQIRYLETLQAIAK
SANSKVIFLPLD
>gnl|CDD|259816 cd13438, SPFH_eoslipins_u2, Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial SLPs remain uncharacterized
VPPGERGLLYRDGKLVRTLEPGRYAFWKFGRKVQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRV
VDPVKAVETVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKD
IILPGEIREILNQVLEAEKRAQANLIRAREETAATRSLLNAAKLMEENPALLRLRELEALEKIAEKVGHI
SVSGG
>gnl|CDD|240442 cd13439, CamS_repeat, Repeat domain of CamS sex pheromone cAM373 precursor and related proteins. This family includes CamS, from which Staphylococcus aureus sex pheromone staph-cAM373 is processed. The protein contains two structurally similar repeats in a tandem arrangement. The heptapeptide cAM373 is a Streptococcus faecalis pheromone, secreted by recipient cells, which induces a mating response in donor cells that contain particular conjugative plasmids. cAM373 is also excreted by Staphylococcus aureus. The family also contains sex hormone precursors from other bacteria and an uncharacterized protein with a single repeat from Desulfovibrio piger, which is structurally similar and might be homologous
EKFQDLNDNFKNFIEELLARYSDKNFTNVVEQDYYKDGQLKGLNIDLAXNSYGDAETIAQTQYVASQVLR
RLPKTDGLKDVPIQIAIKKQKSAATPGRPIAVITKE
>gnl|CDD|240443 cd13440, CamS_repeat_2, C-terminal repeat domain of CamS sex pheromone cAM373 precursor. This family includes CamS, from which Staphylococcus aureus sex pheromone staph-cAM373 is processed. The protein contains two structurally similar repeats in a tandem arrangement. The heptapeptide cAM373 is a Streptococcus faecalis pheromone, secreted by recipient cells, which induces a mating response in donor cells that contain particular conjugative plasmids. cAM373 is also excreted by Staphylococcus aureus. The family also contains sex hormone precursors from other bacteria
EKYVLFPSSEATELDREDATKFDNFKDDIQNFFPNLSGVTGKGFYKDGKLQKLNIDIPTQFYGKTEIIAF
TQYVAGLASKYFPKDIPVEITIKSVNGPEALIVREAGEEEPFVHI
>gnl|CDD|240444 cd13441, CamS_repeat_1, N-terminal repeat domain of CamS sex pheromone cAM373 precursor. This family includes CamS, from which Staphylococcus aureus sex pheromone staph-cAM373 is processed. The protein contains two structurally similar repeats in a tandem arrangement. The heptapeptide cAM373 is a Streptococcus faecalis pheromone, secreted by recipient cells, which induces a mating response in donor cells that contain particular conjugative plasmids. cAM373 is also excreted by Staphylococcus aureus. The family also contains sex hormone precursors from other bacteria
TDGPYKTSKARGLTASQLNNRLDLDEFETGLMRLSKEYFSTDDYYFQEGQYLSKDTINSWLKRKSKDNPE
GLNPEDNLEEGGKEKNKKNPIYLSHILEQDYLVKNGDKYKLAGISIGLALNSVYYYQKEDGYTYEVEISE
EELEAYGKEIANKIVNRLRKKKGLKDVPIVIALYKQESKDSLVPGNFIAYATVESGSTTIGNWE
>gnl|CDD|412041 cd13442, CDI_toxin_Bp1026b-like, C-terminal (CT) toxin domain of the contact-dependent growth inhibition (CDI) system of Burkholderia pseudomallei 1026b, and related proteins. CDI toxins are expressed by gram-negative bacteria as part of a mechanism to inhibit the growth of neighboring cells. This model represents the C-terminal (CT) toxin domain of CdiA effector proteins. CdiA secretion is dependent on the outer membrane protein CdiB. Upon binding to a receptor on the surface of target bacteria, the CDI toxin is delivered via the C-terminal domain. A wide variety of C-terminal toxin domains appear to exist; this particular example from Burkholderia pseudomallei 1026b and other bacteria appears to function as a Mg2+-dependent RNAse cleaving tRNA, most likely in the aminoacyl acceptor stem. This CdiA-Ct is structurally similar to another CDI toxin domain from B. pseudomallei E479 which is unrelated in sequence but has a similar nuclease domain, and shares similar fold and active-site architecture; it contains a core alpha/beta-fold that is characteristic of PD(D/E)XK superfamily nucleases
PKGKPTKIDGKADPDTLRSLERENESADILAKNGYDVEQNPPVPGKGGKNPDYLIEGEVFDCYAPTGSNK
RNIWSTIRKKVKKQADRIVLNLDDSPLSVEEIRRQLKRWPIKGLKELIVIKDGKIIRIY
>gnl|CDD|259836 cd13443, CDI_inhibitor_Bp1026b_like, Inhibitor of the contact-dependent growth inhibition (CDI) system of Burkholderia pseudomallei 1026b, and related proteins. CDI toxins are expressed by gram-negative bacteria as part of a mechanism to inhibit the growth of neighboring cells. This model represents the inhibitor of the CdiA effector protein from Burkholderia pseudomallei 1026b (which is a tRNAse). CdiA secretion is dependent on the outer membrane protein CdiB. Upon binding to a receptor on the surface of target bacteria, the CDI toxin is delivered. The inhibitors are intracellular proteins that inactivate the toxin/effector protein
SIDLRCYLTIDLSQIKEDLDKIRENYSHLFEGKFLLSEVEDASESTLEIAEEFGLDPKSYFLISVNDKTS
SLLTPEIADLFRDELGEDNILILLNNEDLI
>gnl|CDD|259837 cd13444, CDI_toxin_EC869_like, Zn-dependent DNAse of the contact-dependent growth inhibition (CDI) system of Escherichia coli EC869, and related proteins. CDI toxins are expressed by gram-negative bacteria as part of a mechanism to inhibit the growth of neighboring bacteria. This model represents the C-terminal toxin domain of CdiA effector proteins. CdiA secretion is dependent on the outer membrane protein CdiB. Upon binding to a receptor on the surface of target bacteria, the CDI toxin is delivered. A wide variety of C-terminal toxin domains appear to exist; this particular example from Escherichia coli EC869 and other bacteria appears to function as a Zn2+-dependent DNAse degrading the genome of target cells
SKSGRKVSGIKWGQGIKKQGNPFEDYVGKQLIDGNNLPKNFKTFDYFDPATGTATSVKTLDLQAKTYQNP
KAIYNRLNRYIDKLANFKGDKRGGVELRSSDIKSKELELAVPDKTTKEQWKAINKAIDYANEKGIKVKIT
VVK
>gnl|CDD|259838 cd13445, CDI_inhibitor_EC869_like, Inhibitor of the contact-dependent growth inhibition (CDI) system of Escherichia coli EC869, and related proteins. CDI toxins are expressed by gram-negative bacteria as part of a mechanism to inhibit the growth of neighboring bacteria. This model represents the inhibitor of the CdiA effector protein from Escherichia coli EC869 (which is a DNAse). CdiA secretion is dependent on the outer membrane protein CdiB. Upon binding to a receptor on the surface of target bacteria, the CDI toxin is delivered. The inhibitors are intracellular proteins that inactivate the toxin/effector protein. This domain is also known as DUF1436
KYSASIYKNDKFISIETYSGGGLSFLDPKFPPHYLSPDVDDEELGKAIRKALSNSRTITPEEFEDIFDSE
KIKERYKEWVEKLMKKYGYKSKKALFKNMDSCSIELINDKITISPTHHDKLEGWTGIGDEGDYIILPIDA
SDEELGAALRLAFSRCT
>gnl|CDD|259825 cd13516, HHD_CCM2, harmonin-homology domain (harmonin_N_like domain) of malcavernin (CCM2). CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM) along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signaling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours. CCM2 possesses an N-terminal PTB domain. The C-terminal domain of malcavernin, which is represented here, appears similar to the N-terminal domain of the scaffolding protein harmonin. It has also been referred to as the Karet domain
HSTSASRSDSSIVSADELLQDYMEVLRSKLTPDELQQFAALLREYRTGSPIEEFCQKLLELYGPERKFLL
LGMRPFIPEKDLPYFESFLEKIGIADG
>gnl|CDD|270235 cd13517, PBP2_ModA3_like, Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 periplasmic binding fold superfamily. This subfamily contains molybdate binding protein-like (ModA3) domain of an ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. ModA transporters import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arrangted around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLLVYAGAGLKKPMEEIAKLFEKKTGIKVEVTYGGSGQLLSQIETSKKGDVFIPGSEDYMEKAKEKGLVE
TVKIVAYHVPVIAVPKGNPKNITSLEDLAKPGVKVALGDPKAAAIGKYAKKILEKNGLWEKVKKNVVVYT
ATVNQLLTYVLLGQVDAAIVWEDFAYWNPGKVEVIPIPKEQNRIKTIPIAVLKSSKNKELAKKFVDFVTS
DEGKEIFKKYGFK
>gnl|CDD|270236 cd13518, PBP2_Fe3_thiamine_like, Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 periplasmic binding fold superfamily. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. On the other hand, thiamin is an essential cofactor in all living systems. Thiamin diphosphate (ThDP)-dependent enzymes play an important role in carbohydrate and branched-chain amino acid metabolism. Most prokaryotes, plants, and fungi can synthesize thiamin, but it is not synthesized in vertebrates. These periplasmic domains have high affinities for their respective substrates and serve as the primary receptor for transport. After binding iron and thiamine with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The iron- and thiamine-binding proteins belong to the PBPI2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
ELVVYTASDRDFAEPVLKAFEEKTGIKVKAVYDGTGELANRLIAEKNNPQADVFWGGEIIALEALKEEGL
LEPYTPKVIEAIPADYRDPDGYWVGFAARARVFIYNTDKLKEPDLPKSWDDLLDPKWKGKIVYPTPLRSG
TGLTHVAALLQLMGEEKGGWYLLKLLANNGKPVAGNSDAYDLVAKGEVAVGLTDTYYAARAAAKGEPVEI
VYPDQGALVIPEGVALLKGAPNPEAAKKFIDFLLSPEGQKALAAANAQLP
>gnl|CDD|270237 cd13519, PBP2_PEB3_AcfC, Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a member of the type 2 periplasmic binding fold superfamily. PEB3 is a glycoprotein adhesion from Campylobacter jejuni whose structure suggests a functional role in transport, and resembles PEB1a, an Asp/Glu transporter and an adhesin. The overall structure of PEB3 is a dimer and is similar to that of other type 2 periplasmic transport proteins such as the molybdate/tungstate, sulfate, and ferric iron transporters. PEB3 has high sequence identity to Paa, an Escherichia coli adhesin, and to AcfC, an accessory colonization factor from Vibrio cholera
EINLYGPGGPAPAMKEAAKKFEKKTGVKVNVTAGPQPTWEDKAKQDADIIYGGSEQMMTDFISALPKLFD
SSDIKPLYLRPSAILVRKGNPKKIKGLKDLLKPGVKILVVNGAGQTGLWEDMAGRTGDIETVRAFRKNIV
VFAKNSGAARKAWKQDPNIDAWITWNIWQKANPDIADFVELEKDYVIYRDMNVALTKKGLQNPEAQEFID
YLSSKEAQAIFKKWGWK
>gnl|CDD|270238 cd13520, PBP2_TAXI_TRAP, Substrate binding domain of TAXI proteins of the tripartite ATP-independent periplasmic transporters; the type 2 periplasmic binding protein fold. This group includes Thermus thermophilus GluBP (TtGluBP) of TAXI-TRAP family and closely related proteins. TRAP transporters are ubiquitous in prokaryotes, but absent from eukaryotes. They are comprised of an SBP (substrate-binding protein) of the DctP or TAXI families and two unequally sized integral membrane components. Although TtGluBP is predicted to be an L-glutamate and/or an L-glutamine-binding protein, the substrate spectrum of TAXI proteins remains to be defined. A sequence-homology search also shows that TtGluBP shares low sequence homology with putative immunogenic proteins of uncharacterized function. The substrate-binding domain of TAXI proteins belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and tworeceptor cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
FLTIATGSTGGTYYPLGGALANLLNKKLPGVRATAVSTGGSVENLRLLESGEADFGLAQSDVAYDAYNGT
GPFEGKPIDNLRAVASLYPEYLHLVVRKDSGIKSIADLKGKRVAVGPPGSGTELTARRLLEAYGLTDDDV
KAEYLGLSDAADALKDGQIDAFFWVGGLPASAITELAATRDIRLLPIDDEEIAKLLAEYPYYVPATIPAG
TYPGQDEDVPTVAVPALLVTRADLPEDLVYQLTKALYENRDELAAAHPAAKQLISLETAIDGLPIPLHPG
AERYY
>gnl|CDD|270239 cd13521, PBP2_AlgQ_like, Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold. This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide
PLTLSVLMAFNDNWVDDENWPVAKEIEKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADYLKDKF
IAYGMEGAFLPLSKYIDQYPNLKAFFKQHPDVLRASTASDGKIYLIPYEPPKDVPNQGYFIRKDWLDKLN
LKTPKTLDELYNVLKAFKEKDPNGNGKADEIPFIDRDPLYGAFRLINSWGARSAGGSTDSDWYEDNGKFK
HPFASEEYKDGMKYMNKLYTEGLIDKESFTQKDDQAEQKFSNGKLGGFTHNWFASDNLFTAQLGKEKPMY
ILLPIAPAGNVKGRREEDSPGYTGPDGVAISKKAKNPVAALKFFDWLASEEGRELANFGIEGVHYNKDNG
KKRTKDPVKKSDQPGDNQLYDLPAFIKGGFWNEYTYPRPQWGVLTGDSARLPIDMYIKPKYSPPKPEGAN
LTIEEREQVSIDNTELKDIMMEMTQKWIMGTKEKDEEWDAYQEQLKSAGLYQVTEEVQKAYDR
>gnl|CDD|270240 cd13522, PBP2_ABC_oligosaccharides, The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold. This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TITVWHQYDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFA
AAGLLAPLDEYVSKSGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPKNPPKTWQELIALAQGLK
AKNVWGLVYNQNEPYFFAAWIGGFGGQVFKANNGKNNPTLDTPGAVEALQFLVDLKSKYKIMPPETDYSI
ADALFKAGKAAMIINGPWDLGDYRQALKINLGVAPLPTFSGTKHAAPFVGGKGFGINKESQNKAAAVEFV
KYLTSYQAQLVLFDDAGDIPANLQAYESPAVQNKPAQKASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSV
LAGKVTPEAAAKDAQQEA
>gnl|CDD|270241 cd13523, PBP2_polyamines, The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding proteins that function as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TVVIYTWGGYLPQDIIDPFEKETGIKVVVDTAANSERMIKKLSAGGSGGFDLVTPSDSYTSRQLGVGLMQ
PIDKSLLPSWATLDPHLTLAAVLTVPGKKYGVPYQWGATGLVYNTDKVKAPPKSYAADLDDPKYKGRVSF
SDIPRETFAMALANLGADGNEELYPDFTDAAAALLKELKPNVKKYWSNASQPANLLLNGEVVLAMAWLGS
GFKLKQAGAPIEFVVPKEGAVGWLDTFAVPANAPNKDGAYKLLNALLRPKVAAAVAAT
>gnl|CDD|270242 cd13524, PBP2_Thiaminase_I, Thiaminase-I has high structural homology to the type 2 periplasmic binding proteins of active transport systems. Thiaminase-I, a thiamin-(vitamin B1) degrading enzyme, is a monomer in its biologically active form, with two distinct globular domains (N- and C-domains) separated by a deep groove. It has a structural topology similar to the periplasmic substrate-domains of ABC-type transport systems, such as thiamin-binding protein (TbpA), that possess the type 2 periplasmic binding protein fold. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea
TTLKVALFPYIPDADRFAALITDQWQRQEPGVDLDFVDWAKLDDSYSADPPDLNQLGAGALDVVEIDTIF
LGHLVDAGYLLPFGIDQARDYLPFALQAVSRNGEVYGVPQLLCTNLLFYRSPDLGQATDIASLYKKIGTS
HPSGKGLLINLAGSWTLASMYLDALIDVTGQYTLYDALPDLEPLDAKVIASLRQLVNSCLMAGVNPCQYG
TDGDSYVRVEWFAKGSARAFIGYSERLMRMRKAGDYVEQLRVKSIPLGTGDIPLFFTDALVVNSKCAGTC
PELAKKLANFMASDDVVEQALRARDDGDGAVPRYLLPATHSVFEAEPAADDPLYSELRQLVSGARPYPFR
LGPEVRTWLQDAK
>gnl|CDD|270243 cd13525, PBP2_ATP-Prtase_HisG, The catalytic domain of ATP phosphoribosyltransferase contains the type 2 periplasmic substrate-binding fold. Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea
MLRIAVPKKGRLSDDATELLENAGYKVELTLGRRLTAKTKVPDVEILFGRPNDIPEFVADGIVDLGITGY
DLVEENGFDDVYELLDLGFGQCSLVLAAPPDFSWKGTNFLRGKRIATKYPNLVRKYLAQKGIDFEVIKLE
GSVEIAPVLGLADAIADLVSTGTTLSANGLRVIEKILDSSARLIANRGSFGKFKQDKIDELVERIEGV
>gnl|CDD|270244 cd13526, PBP2_lipoprotein_MetQ_like, The periplasmic-binding component of ABC-type methionine uptake transporter system and its related lipoproteins; the type 2 periplasmic-binding protein fold. This family represents the periplasmic substrate-binding domain of ATP-binding cassette (ABC) transporter involved in uptake of methionine (MetQ) and its related homologs. Members of the MetQ-like family include the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum, the membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus, and Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus. They all function as a receptor for methionine. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea
KLKIGVTAGPSADVVEAAKKEAKKKGYELELVVFTDYVAPNEALNDGSIDANFFQHVPFLDQFNKERNGD
LVKVGKTVIAPIGLYSKKYKSLDELPDGARIAIPNDPSNGARALLLLEDAGLIKLKDGVGLFATVLDITE
NPKNLEIVEVDAAQLPRSLDDVDAAVINGNYAISAGLDPRKDAIFLEDSDASPYVNVLAVREDNKDDPWV
KALVEAYQSEEVRKFLKE
>gnl|CDD|270245 cd13527, PBP2_TRAP, Substrate-binding component of Tripartite ATP-independent Periplasmic transporters and related proteins; contains the type 2 periplasmic-binding protein fold. This family represents the TRAP Transporters that are specific to various ligands, including sialic acid (N-acetyl neuraminic acid), glutamate, ectoine, xylulose, C4-dicarboxylates such as succinate, malate and fumarate, and keto acids such as pyruvate and alpha-ketobutyrate. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. This family also includes some eukaryotic homologs that have not been functionally characterized. TRAP transporters are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
DLRLAMNAPPSSYEYKAAEMFAKEVKEKSQGKLEIKVFSSSQLGDGRNMLKALKQGSVDIGFVLSAYFSG
FDPEFALFALPFVISSYNVIEKAWKAGETGDELNQELDKKLGIVLLSGAPNGPQQITSNRAINSLADMKG
LKLRVPGAANSRYAKLLGASPTSIPFSEVYLALQTGVVDGTENPLATVQSQKLWEVVKYYYDANHFIPTS
LYLVNKRAYDSLPPEIQKLVRDAAENADAEHTQLAVAKEKDLVTFFEKNGVEITPPDPELLQAMRAALKP
YYAEWVKQAGQKGEDALKAIR
>gnl|CDD|270246 cd13528, PBP2_osmoprotectants, Substrate-binding domain of osmoregulatory ABC-type transporters; the type 2 periplasmic-binding protein fold. This family represents the periplasmic substrate-binding component of ABC transport systems that are involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. To counteract the efflux of water, bacteria and archaea accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TIVVGSKNFTEQYILGEMLAQLLEANTDLTVERKLNLGGTEVAFNALKNGDIDLYVEYTGTALLTILKED
APITDPEEVYEKVKKEYEEKFGLTWLDPLGFNNTYALAVRKDTAEKYGLKTISDLAPHSDQLVFGADPEF
YERSDGLPGLKKTYGFDFKEVKTMDPGLTYEALDNGEVDVIDAFSTDGRIKAFDLVVLEDDKNFFPPYNA
APVVREDVLKKHPELEEVLNKLSGKLTDETMQQLNYQVDVEGKDPEEVARDFLK
>gnl|CDD|270247 cd13529, PBP2_transferrin, Transferrin family of the type 2 periplasmic-binding protein superfamily. Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helical and beta sheet domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor
TVRWCVVSEAELKKCEALQKAAYSRGIRPSLECVKATSREECMKAIKNGTADFVTLDGGDVYTAGKDYNL
KPIAAELYGDEGEASYYAVAVVKKSSNITSLKDLRGKKSCHTGYGRTAGWNVPIGYLLENGLISPVTCNY
IKAVSSFFSSSCVPGALRCLLEGAGDVAFVKHTTVKDNTGGSWADNINPDDYELLCPDGTRAPVSEYKSC
NLGKVPSHAVVTRSDTSQSDRNEVQKLLLAAQELFGNKPRSFFMFYGSFNGGKNLLFSDSTKGLVGVPDQ
KTSEYLGMEYFSAIRSSR
>gnl|CDD|270248 cd13530, PBP2_peptides_like, Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold. This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction
TLRVGTDADYPPFEYIDKNGKLVGFDVDLANAIAKRLGVKVEFVDTDFDGLIPALQSGKIDVAISGMTIT
PERAKVVDFSDPYYYTGQVLVVKKDSKITKTVADLKGKKVGVQAGTTGEDYAKKNLPNAEVVTYDNYPEA
LQALKAGRIDAVITDAPVAKYYVKKNGPDLKVVGEPLTPEPYGIAVRKGNPELLDAINKALAELKADGTL
DKLLEKW
>gnl|CDD|270249 cd13531, PBP2_MxaJ, Methanol oxidation system protein MoxJ; the type 2 periplasmic binding fold. This predicted periplasmic protein, called MoxJ or MxaJ, is required for methanol oxidation in Methylobacterium extorquens. Homology suggests it is the substrate-binding protein of an ABC transporter associated with methanol oxidation. Other evidence also suggests that MoxJ is an accessory factor or additional subunit of methanol dehydrogenase itself. Mutational studies show a dependence on this protein for expression of the PQQ-dependent, two-subunit methanol dehydrogenase (MxaF and MxaI) in Methylobacterium extorquens, as if it is a chaperone for enzyme assembly or a third subunit. A homologous N-terminal sequence was found in Paracoccus denitrificans as a 32Kd third subunit. MoxJ may be both, a component of a periplasmic enzyme that converts methanol to formaldehyde and a component of an ABC transporter that delivers the resulting formaldehyde to the cell's interior
ATTLRVCAATDELPYSNAQGAGFENRIAKVLADAMGRKVEFVWLEDARYLVRDGLDKDQCDVLLGVDAGD
PRVLTTKPYYRSGYVFVTRADKGLDITDWQSPYLKEFSTFVIRLPSPAETMLRQIGRYEDNFIYLASLTG
FKSRRNRYVRYDPSRLVNDVATGKADVAVIWAPEAARYVKDSSEPLRMVLVEDNAERSDGEKIPQQYEQS
IGVRKGDTELLKEIEQALQKAKPKIDAILKEE
>gnl|CDD|270250 cd13532, PBP2_PDT_like, Catalytic domain of prephenate dehydratase and similar proteins; the type 2 periplasmic binding protein fold. Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
KPKVAYLGPEGTYSHQAALQLFGDSVELLPLPSISDVFEAVESGEADYGVVPIENSTEGSVVETLDLLRD
RPDVKIVGEVYLPIHHCLLGRPGADLSEIKRVYSHPQALGQCRNFLSEHLPGAERIDVSSTAEAAELVAE
DPSGTAAAIASELAAELYGLEILAENIQDEKDNTTRFLVLGRRE
>gnl|CDD|270251 cd13533, PBP2_Yhfz, Substrate-binding domain of uncharacterized protein Yhfz from Shigella Flexneri; the type 2 periplasmic-binding protein fold. This subfamily contains periplasmic binding protein type II (BPBII). This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBPII proteins share the same architecture as periplasmic binding proteins type I (PBPI), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBPII proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction
DYKKLLEIAGIGSLVGAMPLPYSRRYEGLATGLYAQFEELKIPFNLAYMRGADNRIEALLEGRYDFAVVS
RLAAEQAVDEGKDIEIVLELGPGTYVSQHVLLFRDPEDKEIQDGMRVGIDPSSADQRILTHRECEGKKVE
LVEINYNQLLQLLKSGEIDAAIWNLDEIQSKNLGLNYVPLKDEDARALRATEAVIVIRKGNPFLKRLLRA
LIDFPEVLEIQK
>gnl|CDD|270252 cd13534, PBP2_MqnD_like, Menaquinone biosynthetic enzyme and related hypothetical proteins; the type 2 periplasmic-binding protein fold. This family represents MqnD, an enzyme within the alternative menaquinone biosynthetic pathway, and related conserved hypothetical proteins. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. The members include Ttha1568, MqnD from Thermus thermophiles HB8, and the conserved hypothetical proteins SCO4506 from Streptomyces coelicolor, Af1704 from Archaeoglobus DSM 4304, Dr0370 from Deinococcus radiodurans, and Ca3427 from candida albicans. They all have significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TIRVGHSPDADDLFLFYALKHGWVKETDLIFENVKEDVETLNELALKNELDVSAISFAAYPKIADDYVIL
PTGAVFGDGYGPVLVAKSPLDDKQGKRVAVSGRNTTAYLLLKLLAPQYFRPIVVRFDDIEDAVLEGEVDA
GVLIHESILMTYPRYGLKVVRDLWDLWKESTNLPLPLGVVAIRRDLGEDLIRAFKEAVLLSKAYALAHPD
EAIEYMLQEAREIRLDEEVLKKYLKTYVNEYSNRTGEDQDRAVDKLFELAE
>gnl|CDD|270253 cd13535, PBP2_Osm_BCP_like, Substrate binding domain of osmoregulatory ABC-type glycine betaine/choline/L-proline transport system and related proteins; the type 2 periplasmic binding protein fold. This family is part of a high affinity multicomponent binding-protein-dependent ATP-binding cassette transport system specific to certain quaternary ammonium compounds for osmoregulation. The periplasmic substrate-binding domain, which is often fused to the permease component of the ATP-binding cassette transporter complex, is involved in uptake of osmoprotectants (also termed compatible solutes) such as betaines, choline, and L-proline. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. This domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TVKLAVPSWTGETATTHVLGTILEALGYTVDYVSLNNAVTFQSLANGDIDITVENWLPNHEDFYAKYVEG
KKVVVLGQNLYGAKQGFAVPKKVAELNPITNIADLGRPDAAALADSEGNGKGRLTGCPPGWGCEGAIEVK
LEDYGLLKFVEVVPGSEGAMTAAIKSAIKQGEPIFFYGWSPHWVWFKFDVVYLSEPTYDEACYTMVQPWN
EKSSVGCKFASSTVHIAVNKGLADENPAAAEILENFSLTVDDVNAFMGEISDNGGDPEEAAAEWLKA
>gnl|CDD|270254 cd13536, PBP2_EcModA, Substrate binding domain of ModA from Escherichia coli and its closest homologs;the type 2 periplasmic binding protein fold. This subfamily contains domains found in ModA proteins that serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TVTVFAAASLTDAMQEIATAFEKATGIDVRVSFASSSALARQIEAGAPADLFLSADRDWMDYLVQKGLID
PATRQNLLGNRLVLVAPAASPIQVDPKPGFDLAALLGGGRLAVGDPAHVPAGKYAKEALEKLGLWSSLEP
RLALAEDVRAALALVERGEAPLGIVYATDAAASKGVRVVATFPEDSHKPIEYPVALLKGANNPAARAFLD
FLKSPQAQAIFKRYGFT
>gnl|CDD|270255 cd13537, PBP2_YvgL_like, Substrate binding domain of putative molybdate-binding protein YvgL and similar proteins;the type 2 periplasmic binding protein fold. This subfamily contains domains found in ModA proteins of putative ABC-type transporter. ModA proteins serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate and tungstate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLTVSAAASLKDALDEIATEYEKENPGVKITFNFGGSGTLQKQIESGAPADVFFSAAKKQMDALEDKGLI
DASTRKNLLKNKLVLIVPKDSDSKISSFDLTKDDVKKIAIGEPETVPAGKYAKEALEKLGLWDEIESKLV
YGKDVRQVLTYVETGNADAGFVYKTDALINKKVKVVEEAPEDTHTPIIYPIAVIKNSENKEEAQKFIDFL
KSEEAKKIFEKYGFE
>gnl|CDD|270256 cd13538, PBP2_ModA_like_1, Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding protein fold. This subfamily contains domains found in ModA proteins of putative ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLTVFAAASLTDAFTEIGEQFEKSNPGVKVTFNFAGSQALVTQIEQGAPADVFASADTANMDALVKAGLL
VDTPTIFATNKLVVIVPKDNPAKITSLADLAKPGVKIVIGAPEVPVGTYTRRVLDKAGNDYAYGYKEAVL
ANVVSEETNVRDVVTKVALGEADAGFVYVTDAKAASEKLKVITIPEEYNVTATYPIAVLKASKNPELARA
FVDFLLSEEGQAILAEYGFG
>gnl|CDD|270257 cd13539, PBP2_AvModA, Substrate binding domain of ModA/WtpA from Azotobacter vinelandii and its closest homologs;the type 2 periplasmic binding protein fold. This subfamily contains domains found in ModA proteins that serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arranged around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate is where the central metal atom is in a hexacoordinate configuration. This octahedral geometry was rather unexpected. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLRVAAAANLKYALKEIAAAFEKETGIKVRVSYGSSGKLYAQIRNGAPFDLFLSADEKYPEKLYKAGLAA
AGSPFVYAIGKLVLWSPKPSLLDPSGDVLLDPKVKRIAIANPKLAPYGRAAVEALEHAGLYEAVKPKLVY
GENVSQAAQFAATGNADVGFVALSLALSPKLKEKGSFWLVPPDLYPPIEQGAVILKRGKDNAAAKAFYDF
LLSPEARAILKKYGYV
>gnl|CDD|270258 cd13540, PBP2_ModA_WtpA, Substrate binding domain of ModA/WtpA from Pyrococcus furiosus and its closest homologs;the type 2 periplasmic binding protein fold. This subfamily contains domains found in ModA proteins that serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arranged around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TITVFHAGSLSAPFKALGPAFEKAHTGVRVQGEASGSVGLARKVTDLGKPADVFISADYSLIPKLMIPKY
ADWYVPFASNEMVIAYTNKSKYADEINTDNWYEILLRPDVKIGRSDPNLDPCGYRTLMTLKLAEKYYNQP
DLYSEKLLGNNKKVAQRPKETDLLALLESGQIDYAFIYKSVAKQHGLPYIELPDEINLSDPSYADFYAKS
KYTLGDGGTIHGKPIVYGATIPKNAPNPEAARAFVKFLLSPEGQEILEENGLE
>gnl|CDD|270259 cd13541, PBP2_ModA_like_2, Substrate binding domain of molybdate-binding proteins;the type 2 periplasmic binding protein fold. This subfamily contains domains found in ModA proteins of putative ABC-type transporter. ModA proteins serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate and tungstate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
PLRLYAAGSLRAALTELAAAYQEQTGVAIELEFGPAGLLRERIEAGEKADLFASANMEHPQALAAAGRAS
PVVVFARNRLCLIARPGLGLTSDNLLDLLLDPRLRLGTSTPGADPGGDYAWQLFDRAEKLHPGAGKKLKA
KALKLVGGPDSPPIPGGRNAAHYLIENGQADLFIGYCSNARLLKQVPDLQVVALPDELNIGAEYGLAILS
AAHAAAQRLALFLLSPEGQAILAKYGFL
>gnl|CDD|270260 cd13542, PBP2_FutA1_ilke, Substrate binding domain of ferric iron-binding protein, a member of the type 2 periplasmic binding fold superfamily. FutA1 is the periplasmic component of an ABC-type iron transporter and serves as the primary receptor in Synerchosystis species. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria and is critical for survival of these pathogens within the host. After binding iron with high affinity, FutA1 interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The iron- and thiamine-binding proteins belong to the PBPI2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
EVNVYSSRHYNTDKPLYKAFEKETGIKVNVVFASADELLERLKAEGANSPADVLLTVDAGRLWEAKEAGL
LQPVTSEKLESNVPANLRDPDGNWFGLTKRARVIVYNKDKVNPEELSTYEDLADPKWKGKVCMRSSSNSY
NQSLVASMIAHDGEKETKEWLQGWVNNLAREPQGGDRDQAKAIAAGICDVGIANSYYLGRMLNSEDPEEK
EVAEPVGVFFPNQDNRGTHVNISGIGVTKYAKNKENAIKFLEFLVSEPAQKLYAGGNYEYPVNPGVELSE
LVKSWGPFKPDTLNLSKIGANQSKAIKLMDEVGW
>gnl|CDD|270261 cd13543, PBP2_Fbp, Substrate binding domain of ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic protein (Fbp) has high affinities for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
ELTVYSGRHESLVDPLVEAFEQETGIKVELRYGDTAELANQLVEEGDASPADVFYAEDAGALGALADAGL
LAPLPEDTLTQVPPRFRSPDGDWVGVSGRARVVVYNTDKLSEDDLPKSVLDLAKPEWKGRVGWAPTNGSF
QAFVTAMRVLEGEEATREWLKGLKANGPKAYAKNSAVVEAVNRGEVDAGLINHYYWFRLRAEQGEDAPVA
LHYFKNGDPGALVNVSGAGVLKTSKNQAEAQKFLAFLLSKEGQEFLATANFEYPLVAGVASPPGLPPLEE
LSAPEVDLAQLSDLEGTLKLLREAGL
>gnl|CDD|270262 cd13544, PBP2_Fbp_like_1, Substrate binding domain of a putative ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily. The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
ELTVYTSLEEEEAKAILEAFKKDTGIKVEFVRLSTGEALARLEAEKGNPQADVWFGGTADAHIQAKKEGL
LEPYKSPNADKIPAKFKDPDGYWTGIYLGPLGFGVNTDELKEKGLPVPKSWEDLLNPEYKGEIVMPNPAS
SGTAYTFLASLIQLMGEDEAWEYLKKLNKNVGQYTKSGSAPAKLVASGEAAIGISFLHDALKLKEQGYPI
KIIFPKEGTGYEIEAVAIIKGAKNPEAAKAFIDWALSKEAQELLAKVGSYAIPTNPDAKPPEIAPDLKKD
KLIKYDFEWAGE
>gnl|CDD|270263 cd13545, PBP2_TbpA, Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding fold superfamily. Thiamin-binding protein TbpA is the periplasmic component of ABC-type transporter in E. coli, while the transmembrane permease and ATPase are ThiP and ThiQ, respectively. Thiamin (vitamin B1) is an essential confactor in all living systems that most prokaryotes, plants, and fungi can synthesized thiamin. However, in vertebrates, thiamine cannot be synthesized and must therefore be obtained through dietary absorption. In addition to thiamin biosynthesis, most organisms can import thiamin using specific transporters. After binding thiamine with high affinity, TbpA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The thiamine-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLTVYTYDSFVGEWGPGPEVKAEFEKETGCKVEFVKPGDAGELLNRLILEKNNPRADVVLGLDNNLLSRA
LKEGLFEPYRSPALDVVPEVPVFDPEDRLIPYDYGYLAFNYDKKKFKEPPLSLEDLTAPEYKGLIVVQDP
RTSSPGLGFLLWTIAVFGEEGYLEYWKKLKANGVTVTPGWSEAYGLFTTGEAPMVVSYATSPAYHVYYEK
DLRYTAVIFPEGHYRQVEGAGILKGAKNPELAKKFVDFLLSPEFQEVIPETNWMFPVNK
>gnl|CDD|270264 cd13546, PBP2_BitB, Substrate binding domain of a putative iron transporter BitB, a member of the type 2 periplasmic binding fold superfamily. The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLVVYSPNSEEIIEPIIKEFEEKPGIKVEVVTGGTGELLARIKAEADNPQADVMWGGGIETLEAYKDLFE
PYESPEAAAIPDAYKSPEGLWTGFSVLPVVLMVNTDLVKNIGAPKGWKDLLDPKWKGKIAFADPNKSGSA
YTILYTILKLYGGAWEYIEKLLDNLGVILSSSSAVYKAVADGEYAVGLTYEDAAYKYVAGGAPVKIVYPK
EGTTAVPDGVAIVKGAKNPENAKKFIDFLLSKEVQEILVETLYRRSVR
>gnl|CDD|270265 cd13547, PBP2_Fbp_like_2, Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
KLVVYTSMPEDLANALVEAFEKKYPGVKVEVFRAGTGKLMAKLAAEAEAGNPQADVLWVADPPTAEALKK
EGLLLPYKSPEADAIPAPFYDKDGYYYGTRLSAMGIAYNTDKVPEEAPKSWADLTKPKYKGQIVMPDPLY
SGAALDLVAALADKYGLGWEYFEKLKENGVKVEGGNGQVLDAVASGERPAGVGVDYNALRAKEKGSPLEV
IYPEEGTVVIPSPIAILKGSKNPEAAKAFVDFLLSPEGQELVADAGLLP
>gnl|CDD|270266 cd13548, PBP2_AEPn_like, Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member of the type 2 periplasmic binding fold superfamily. The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
VVTVYSADGLHSWYRDEFAAFTKATGITVNYVEAGSGEVVERAAKEKSNPQADVLVTLPPFIQQAAQMGL
LQPYQSDAAKNPAIIKAEDGTYAPLVNNYFSFIYNSAVLKNAPKTFADLLDPKYKGKIQYSTPGQAGDGM
AVLLLTTHLMGSDAAFAYLAKLQQNNVGPSASTGKLTALVSKGEISVANGDLQMNLAQMEHANPNKKIFW
PAKAGGQRSTFALPYGIGLVKGAPNADNGKKLIDFLLSKEAQSKVPDMAWGMPVRTDVTPSGKNGEAAKA
AIAGVKIWPPNWDQVLSKLPADIKRWKKAT
>gnl|CDD|270267 cd13549, PBP2_Fbp_like_3, Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TVICYNCPPEWADWGTQLKAFKKRTGIQIPYDNKNSGQALAALIAERARPVADVAYYGVAFGIQAVAQGV
VQPYKPAHWDEIPEGLKDPDGKWFAIHSGTLGFIVNVDALGGKPVPKSWADLLKPEYKGMVGYLDPRSAF
VGYVGAVAVNQAMGGSLDNFGPGIDYFKKLHKNGPIVPKQTAYARVLSGEIPILIDYDFNAYRAKYTDKA
NVAFVIPKEGSVVVPYVMSLVKNAPNPNNGKKVLDFIMSDKGQALWANAYLRP
>gnl|CDD|270268 cd13550, PBP2_Fbp_like_4, Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
ELVVYSGRNEALIQPVLEKFRADTGVEVALKHGSNSAIANQLIEEQSNPQADVFISNDVGALGKLSENGV
LQPYTPAGPELIPADGRAEDNTWVALTARARVIMYNKDLIPEEELPKSIEDLTDPKWKGQVAAANSTNGS
MQGQVSAMRQLLGDEKTEEWIKGLMANEVTFLGGHTDVRKAVGAGEFKLGLVNHYYYHLQLAEGSPVGVI
YPDQGEGQMGVVTNAAGVGLVKGGPNPTNAQAFLDFLLLPENQRIFAEENYEYPI
>gnl|CDD|270269 cd13551, PBP2_Fbp_like_5, Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
KLVVYSNSNSNGRGEWIKEQAKKAGFNIKIVNGGGGDLANRLIAEKNNPVADVVFGLNAVSFERLKKQGL
LVPYTPSWAGEIPSALSDGDGYYYPLVQQPIVLAYNPDTMTDPDAPKSWTDLAKPKYKGKYEVPGLLGGT
GQAILAGILVRYLDPKGEYGVSDEGWQVLEDYFANGYPAQEGTDFYAPFADGQVPIGYLWSSGLAGIQKQ
YGVEFKIVDPEIGVPFVTEQVGIVKGTKKEAEAKAFIDWFGSAEIQAEFAKKFGSIP
>gnl|CDD|270270 cd13552, PBP2_Fbp_like_6, Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
KVVIYSTHGKEMLEYVEDAFEEKTGVEVEWLNMGSQELLDRVRAEKENPQADVWWGGPSQLFMQLKEEGL
LEPTEPSWAEKVAAEFKDADGYWYGTIQTPEVIMYNTELLSEEEAPKDWDDLLDPKWKDKIIIRNPLASG
TMRTIFAALIQRELKGTGSLDAGYAWLKKLDANTKEYAASPTMLYLKIGRGEAAISLWNLNDVLDQRENN
KMPFGFIDPASGAPVITDGIALIKGAPHPEAAKAFYEFVGSAEIQALLAEKFNRMP
>gnl|CDD|270271 cd13553, PBP2_NrtA_CpmA_like, Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily. This subfamily includes nitrate (NrtA) and bicarbonate (CmpA) receptors. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLRIGYLPITDHAPLLVAKEKGFFEKEGLDVELVKFPSWADLRDALAAGELDAAHVLAPMPAAATYGKGA
PIKVVAGLHRNGSAIVVSKDSGIKSVADLKGKTIAVPFPGSTHDVLLRYWLAAAGLDPGKDVEIVVLPPP
DMVAALAAGQIDAYCVGEPWNARAVAEGVGRVLADSGDIWPGHPCCVLVVREDFLEENPEAVQALLKALV
EA
>gnl|CDD|270272 cd13554, PBP2_DszB, Substrate binding domain of 2'-hydroxybiphenyl-2-sulfinate desulfinase, a member of the type 2 periplasmic binding fold superfamily. This subfamily includes DszB, which converts 2'-hydroxybiphenyl-2-sulfinate to 2-hydroxybiphenyl and sulfinate at the rate-limiting step of the microbial dibenzothiophene desulfurization pathway. The overall fold of DszB is highly similar to those of periplasmic substrate-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The DszB protein belongs to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TTLRYSNCPVPNALLTAEESGYLDAAGIDLEVVAGTPTGTVDFTYDQGIPADVVFSGAIPPLLAEGLRAP
GRTRLIGITPLDLGRQGLFVRADSPITSAADLEGKRIGMSAGAIRGSWLARALLHNLEIGGLDVEIVPID
SPGRGQAAALDSGDIDALASWLPWATTLQATGGARPLVDLGLVEGNSYYSTWTVRSDFIEQNPEAVKALV
EALVRAGDWIQAHPEAVVIIHAAEIGVSPGAVGRTI
>gnl|CDD|270273 cd13555, PBP2_sulfate_ester_like, Sulfate ester binding protein-like, the type 2 periplasmic binding protein fold. This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
VIRIGSPGQSNGGRPVGSGILGVAHEKGWLEEEFAKDGIKVEWVFFKGAGPAVNEAFANGQIDFAVYGDL
PAIIGRAAGLDTKLLLSSGSGNNAYLVVPPDSTIKSVKDLKGKKVAVQKGTAWQLTFLRILAKNGLSEKD
FKIVNLDAQDAQAALASGDVDAAFTGYEALKLEDQGAGKIIWSTKDKPEDWTTQSGVWARTDFIKENPDV
VQRIVTALVKAARWVSQEENRDEYIQLWSRSGTPEELIKEEYSGDDWKFRFSPLLDDF
>gnl|CDD|270274 cd13556, PBP2_SsuA_like_1, Substrate binding domain of putative sulfonate binding protein, a member of the type 2 periplasmic binding fold superfamily. This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
ELRLDYAYYNPVSLVLKKFGWLEKEFQKDGVKVTWVLSQGSNKALEFLNSGSVDFGSTAGLAALLAKANG
NPIKTVYVYSRPEWTALVVRKDSPIRSVADLKGKKVAVTKGTDPYIFLLRALNTAGLSKNDIEIVNLQHA
DGRTALEKGDVDAWAGLDPFMAQTELENGSRLFYRNPDFNTYGVLNVREDFAKRHPDAVRRVLKVYEKAR
KWAITHPDELAQILASESKLSLAVAKLQLSRTDFSQPIPGPAQIAVLKAAAPILV
>gnl|CDD|270275 cd13557, PBP2_SsuA, Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic binding fold superfamily. This subfamily includes the sulfonate binding domains SsuA found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLRIGYQKGGTLVLLKARGELEKRLKPLGVKVTWSEFPAGPQLLEALNVGSIDFGSTGDTPPIFAQAAGA
PLVYVAVEPPTPKGEAILVPKDSPIKTVADLKGKKIAFQKGSSAHYLLVKALEKAGLTLDDIEPVYLSPA
DARAAFEQGQVDAWAIWDPYLAAAELTGGARVLADGEGLVNNRSFYLAARDFAKDNPEAIQIVLEELNKA
GEWANTNRDEAAKLLAESLGIDAVVLELAVARRTYGIIPIDDEIIAAQQAIADTFYDLGLIPKKV
>gnl|CDD|270276 cd13558, PBP2_SsuA_like_2, Putative substrate binding domain of sulfonate binding protein, the type 2 periplasmic binding protein fold. This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLRVGDQKGGLRALLEAAGELDGLPYKIEWAEFQGGAPLLEALRAGALDIGGAGDTPPLFAAAAGAPIKI
VAALRGDVNGQALLVPKDSPIRSVADLKGKRVAYVRGSISHYLLLKALEKAGLSPSDVELVFLTPADALA
AFASGQVDAWATWGPYVARAERRGGARVLVTGEGLILGLSFVVAARPALLDPAKRAAIADFLARLARAQA
WANAHPDEWAKAYAAETGLPPEVAAAIFARRSAPVVPIDAQVIASQQQTADTFHEAG
>gnl|CDD|270277 cd13559, PBP2_SsuA_like_3, Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold. This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
RVAIGTQDTTINTATGGLLIRELGLLEKYLPELGKYKDVEYEIEWQDFTSGAPLTNEMVAGKLDIGAMGD
FPGLLNGVKFQTSAGYRSVFIAFLGGSPDGSGNAIVVPKDSPVNSLDDLKGKTVSVPFGSSAHGMLLRAL
DRAGLNPDTDVTIINQAPEVGGSALQANKIDAHADFVPFPELFPHRGIARKLYDGSQTKVPTFHGIVVDR
DFAEKHPEVVVAYLRALIEAHRLIREEPEAYSELIEKVTGIEAEVVYK
>gnl|CDD|270278 cd13560, PBP2_taurine, Taurine-binding periplasmic protein; the type 2 periplasmic binding protein fold. This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
EIRIGYQTVPNPQLVAKADGLLEKALGVKVNWRKFDSGADVNAAMASGSIDIGLLGSPPAAVAIAAGLPI
EVIWIADVIGDAEALVVRKGSGIKSLKDLAGKKVAVPFGSTAHYSLLAALKHAGVDPGKVKILDMQPPEI
VAAWQRGDIDAAYVWEPALSQLKKNGKVLLSSKDLAKKGILTFDVWVVRKDFAEKYPDVVAAFLKALGDA
VDLYRNDP
>gnl|CDD|270279 cd13561, PBP2_SsuA_like_4, Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold. This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
PIRIGYLPALAVAGPIFIAKEKGLFAKHGLDPDFIEFTSGPPLVAALGSGSLDVGYTGPVAFNLPASGQA
KVVLINNLENATASLIVRADSGIASIADLKGKKIGTPSGTTADVALDLALRKAGLSEKDVQIVNMDPAEI
VTAFTSGSVDAAALWAPNTATIKEKVPGAVELADNSDFGPDAAVPGAWVARNKYAEENPEELKKFLAALA
EA
>gnl|CDD|270280 cd13562, PBP2_SsuA_like_5, Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold. This subfamily includes sulfonate binding domains found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TIRIGFQPIPPYAPILVAKQKGWLEEELKKAGADVGVKWSQFSAGPPVNEAFAAGELDVGLLGDTPAIIG
RAAGQDTRIVGLASTGPKALALVVRKDSAIKSVKDLKGKKVATTKGSYVHHLLVLVLQEAGLTIDDVEFI
NMQQADMNTALTNGDIDAAVIWEPLITKLLSDGVVRVLRDGTGIKDGLNVIVARGPLIEQNPEVVKALLK
AYQRG
>gnl|CDD|270281 cd13563, PBP2_SsuA_like_6, Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 periplasmic binding protein fold. This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
PLKIGISTWPGYGPWYLADEKGFFKKEGLDVELVWFESYSDSMAALASGQIDAAATTLDDALAMAAKGVP
VKIVLVLDNSNGADGIVAKPGIKSIADLKGKTVAVEEGSVSHFLLLNALEKAGLTEKDVKIVNMTAGDAG
AAFIAGQVDAAVTWEPWLSNALKRGKGKVLVSSADTPGLIPDVLVVREDFIKKNPEAVKAVVKAWFDA
>gnl|CDD|270282 cd13564, PBP2_ThiY_THI5_like, Substrate binding domain of ABC-type transporter for thiamin biosynthetic pathway intermediates and similar proteins; the type 2 periplasmic binding protein fold. ThiY is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are THI5, which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes, and periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport. After binding the ligand, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ThiY/THI5 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TVTVKVGWIPIVYHAPLYLAQQKGYFKEEGLDVEITTPTGGSDIVQLVASGQFDFGLSAVTHTLVAQSKG
VPVKAVASAIRKPFSGVTVLKDSPIKSPADLKGKKVGYNGLKNINETAVRASVRKAGGDPEDVKFVEVGF
DQMPAALDSGQIDAAQGTEPALATLKSQGGDIIASPLVDVAPGDLTVAMLITNTAYVQQNPEVVKAFQAA
IAKA
>gnl|CDD|270283 cd13565, PBP2_PstS, Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 periplasmic-binding fold superfamily. This subfamily contians phosphate binding domain found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
AVTLTGAGATFPAPLYQKWIDEYKKAHPGVKINYQSIGSGAGIKQFIAGTVDFGASDAPLSDAELAKAGG
GLLQIPTVIGAVVVAYNLPGVKGLLLLSGEVLADIFLGKITKWNDPAIAALNPGVNLPDTPITVVHRSDG
SGTTFIFTDYLSAVSPEWKDKVGAGKSVAWPVGLGGKGNEGVAAAVKQTPGSIGYVELSYALQNGLPAAA
LYPIVGFTYILVKKDYKDAEKAKAVKKFLKWALTEGQKFAADLG
>gnl|CDD|270284 cd13566, PBP2_phosphate, Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily. This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
SGTITIAGSSTVAPLAEALAEEFMKKHPGVRVTVQGGGSGAGIKALIAGTADIAMASRPLKDEEKAAAEA
NGIELVEFVIAYDGIAVIVNPDNPVASLTLEQLRDIFTGKITNWSEVGGPDEPIVVYGRDEGSGTRDYFE
ELVLGKGEFIRNAVVAPSNGALVQAVAGDPNAIGYVGLGYVDENKKVKALKVDGVAPTVENIKSGKYPLS
RPLFLYTKGEPSPAVKAFIDFALSPEGQKIIEEVG
>gnl|CDD|270285 cd13567, PBP2_TtGluBP, Substrate binding domain of Thermus thermophilus GluBP (TtGluBP) of TAXI family of the tripartite ATP-independent periplasmic transporters; contains the type 2 periplasmic binding protein fold. This subgroup includes TtGluBP of TAXI-TRAP family and closely related proteins. TRAP transporters are comprised of an SBP (substrate-binding protein) and two unequally sized integral membrane components. Although TtGluBP is predicted to be an L-glutamate and/or an L-glutamine-binding protein, the substrate spectrum of TAXI proteins remains to be defined. A sequence-homology search also shows that TtGluBP shares low sequence homology with putative immunogenic proteins of uncharacterized function
FITIGTGGTSGTYYPLGGAIANIVNKAIPGINASAQSTGASVANINLLGAGEAELALAQNDVAYYAYNGT
GEFEGKPVKNLRALAALYPETVQIVVRADSGIKTVADLKGKRVSVGAPGSGTEVNARQILEAAGLTYDDI
KVVYLSFAEAAEALKDGQIDAAFVTSGLPTAAIEELATTVDIRIVPIDDEAIDKLKEKYPFYSKTTIPAG
TYKGQDEDVETVAVQAMLVVSEDLSEDTVYDLTKALFEHLDELQASHAAAKQIDLETALEGMSIPLHPGA
AKYY
>gnl|CDD|270286 cd13568, PBP2_TAXI_TRAP_like_3, Substrate binding domain of putative TAXI proteins of the tripartite ATP-independent periplasmic transporters; the type 2 periplasmic binding protein fold. This subgroup includes uncharacterized periplasmic binding proteins that are related to Thermus thermophilus GluBP (TtGluBP) of TAXI-TRAP family. TRAP transporters are comprised of an SBP (substrate-binding protein) and two unequally sized integral membrane components. Although TtGluBP is predicted to be an L-glutamate and/or an L-glutamine-binding protein, the substrate spectrum of TAXI proteins remains to be defined. A sequence-homology search also shows that TtGluBP shares low sequence homology with putative immunogenic proteins of uncharacterized function
FLTIGTGSVTGVYYPIGGAICRLINKDRKSHGIRCSVESTGGSVANLNALREGEVDFALVQSDWAYHAYN
GTGSFEAGGPMSELRAVFSLHPEAFTVVARADSGIKSFDDLKGKRVNIGNPGSGQRATMLALLGAKGWTK
KDFALAIELKASEQAEALCDGKIDAMVYVVGHPNGAIQEATTTCDAKLVPIDGETIDALVKDNPYYQKAT
IPGGLYPGNPEDVPTVGVKATLVTTAEVSEDTVYKLVKAVFENFDEFKKLHPALANLLTVEMIKDGLSAP
LHPGAIKYY
>gnl|CDD|270287 cd13569, PBP2_TAXI_TRAP_like_1, Substrate binding domain of putative TAXI proteins of the tripartite ATP-independent periplasmic transporters; the type 2 periplasmic binding protein fold. This subgroup includes uncharacterized periplasmic binding proteins that are related to Thermus thermophilus GluBP (TtGluBP) of TAXI-TRAP family. TRAP transporters are comprised of an SBP (substrate-binding protein) and two unequally sized integral membrane components. Although TtGluBP is predicted to be an L-glutamate and/or an L-glutamine-binding protein, the substrate spectrum of TAXI proteins remains to be defined. A sequence-homology search also shows that TtGluBP shares low sequence homology with putative immunogenic proteins of uncharacterized function
RLTIATGGTGGVYYPFGGGLAEILSKAVPDVRATAEVTGASVENLRLVASGEADLGFALADAALDAYNGE
GPFSGPVPLRALARLYPNYLHLVVRADSGITSLEDLKGKRVSVGAPGSGTEVTAERLLEAAGLDPDKDVK
RERLGLAESVAALKDGQIDAFFWSGGLPTSAITDLARTRDIRLVDLSDELVALREKYGPFYEAVTIPAGT
YPGQVEDVPTLGVPNLLVVRADLPDDLAYEITKTIFENLDDLVAAHPAAEQLDPRTAISTAPIPLHPGAA
RYY
>gnl|CDD|270288 cd13570, PBP2_TAXI_TRAP_like_2, Substrate binding domain of putative TAXI proteins of the tripartite ATP-independent periplasmic transporters; the type 2 periplasmic binding protein fold. This subgroup includes uncharacterized periplasmic binding proteins that are related to Thermus thermophilus GluBP (TtGluBP) of TAXI-TRAP family. TRAP transporters are comprised of an SBP (substrate-binding protein) and two unequally sized integral membrane components. Although TtGluBP is predicted to be an L-glutamate and/or an L-glutamine-binding protein, the substrate spectrum of TAXI proteins remains to be defined. A sequence-homology search also shows that TtGluBP shares low sequence homology with putative immunogenic proteins of uncharacterized function
SLTIGTASQGGTYYVYGGGWANLLEEELGVPASAEVTGGPVQNLALVHNGELDLGMVTMGPAFEAYNGEG
DLTPGVKMDDVRALFPMYPTPFQIWALADSGISSIDDLAGKRVGSGPAGGTSGTYFPAILETLGLKAEVR
NGGWSDLASQLQDGQLDAVAFAAGVPIPAVMELEAQTEINILGVTGEEISKLIEEYPYWSEFTIPAGTYK
ALKEDIQTISMWNFAIAHKDLPEDLVYEITKAVFENNDQMINTHKSAAETVPENVTKNTFLPFHPGAIRY
Y
>gnl|CDD|270289 cd13571, PBP2_PnhD_1, Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold. This subfamily includes putative periplasmic binding components of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
ASSPPLRIGLASVLSPRETLALYDPLAEYLERKLGRPVEFVQRRTYAEINELLKNGKVDLAFVCSGAYVQ
ARDKAGLELLAVPEINGQPTYRSYIIVPADSPAKSLEDLKGKRFAFTDPLSNSGFLVPMYLLAELGLDPE
RFFSRVFFTGSHDKSIQAVANGLVDGAAVDSLVYEYAVEKGPELAANVRIIWRSEPIGNPPVVARPGLDP
ELKAALQEAFLSMHEDPEGRAALEGLGIDRFVPADDSLYDPIR
>gnl|CDD|270290 cd13572, PBP2_PnhD_2, Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold. This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
QAPETLKVGAIPDENPTTLIRLNDPLADYLEKELGVEVELVVVTDYAAMVEAMRNGQLDLAYFGGLTYVQ
ARLKPGAEPIAQLLRDGDPTFHSVFIANTDSGINSLADLKGKRFAFGDPASTSGHLMPRYFLLEAGVLPD
GDFYRVGFSGAHDATALAVANGKVDAGALNEAIWESLVEEGKIDGEKVKVIWRTPPYPDYPWTVRPNLGP
ELKEKVRNAFLSLDDPEVLDIFGASGFIPASDDDYDPIE
>gnl|CDD|270291 cd13573, PBP2_PnhD_3, Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold. This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
VDPDTLVFAYTPVEDPAVYQEIWAPFIAHISKVTGKDVQFYPVQSNAAQTEAMRSGRLHIAGFSTGPTPF
AVNLAGAVPFAVKGYEDGSFGYELEVITRIDSGIQKVKDLKGRKVAHTSPTSNSGHLAPRALFPAQGGIV
PDKDYEVTFSGKHDQSILGVFNGDYDAAPVASDVLERMAERGQVKEEQFRVIYKSFAFPTGPFGYAHNLK
PELREKIKEAFFTYDFAGTKLAEIFAGFDRFAPITYKEHWAVI
>gnl|CDD|270292 cd13574, PBP2_PnhD_4, Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold. This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
AAEPPLRFGVHPYLSPTELVKRFQPLLDYLEEELGRPVEIKVSKDYQEHVDRLGSGKIDIAYLGPAPYVQ
AKDRRYGIKPLLALLETDGKPTYNGVIVVRADSPIKSLADLAGKSFAFGDPLSTMGHLVPRAMLRQAGIT
SLDLAGYDYLGRHDNVALAVLAGEFDAGALKEEVYRKYKGRGLRVLATSPPLPGHALVARATLPEELVKA
LRRALLELDSTGAGLAILTWIEELRHGFVPVTDEDYDLLR
>gnl|CDD|270293 cd13575, PBP2_PnhD, Substrate binding domain of ABC-type phosphonate uptake system; contains the type 2 periplasmic binding fold. This subfamily includes the Escherichia coli PhnD (EcPhnD) which exhibits high affinity for the environmentally abundant 2-aminoethylphosphonate (2-AEP), a precursor in the biosynthesis of phosphonolipids, phosphonoproteins, and phosphonoglycans. The Escherichia coli phn operon encodes 14 genes involved in binding, uptake and metabolism of phosphonate, and is activated under phophophate-limiting conditions. PhnD belongs to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. The PBP2 have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. PhnD is the periplasmic binding component of an ABC-type phosphonate uptake system (PhnCDE) that recognizes and binds phosphonate
EDEKALNFGIISTESQQNLRAQWEPFLAAMEKKLGVKVNAFFAPDYAGIIEGMRFNKVQIAWYGNKSAME
AVDRANGEVFAQTVAADGSPGYYSHLIVNKDSPINSLNDVLAKAKDLTFGNGDPNSTSGFLVPGYYVFAK
NGIDPKKFFKRTVNANHETNALAVANKQVDVATNNTENLDRLKERAPEKLKQLRIIWTSPLIPGDPLVWR
KDLPEAVKKKIADFFFGYGQTAEEKSVLKERLDWSPFKPSSDGQLVPIR
>gnl|CDD|270294 cd13576, PBP2_BugD_Asp, Aspartic acid transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter
YPERPVTIIVPFAAGGPSDALARAVAEQMGTTLGQPVVIENVGGAGGTIGTARAARAAPDGYTLLLGHMG
TATAPALYYKKLYDPVADFEPVGLIADTPMILVARKDFPAKDLKELVAWVKANPAKVTLGNAGVGSASHL
CGVLLQSALGIKATLVPYKGTGPAMNDLIGGQVDLMCDQTTNALPQIQAGKVRAYAVTSTERLASLPDVP
TSAEAGLPGFEATIWNGLFAPKGTPPAVIAKLNAALKTALNDPAVRKRFADLGLEPPPPEQLTPEALQQL
VKAEVERWAPVIKA
>gnl|CDD|270295 cd13577, PBP2_BugE_Glu, Glutamate transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter
YPSRPITLIVPFPPGGSTDIVARVLAERLGQILGQPVVVENKGGAGGAIGTSAVARAAPDGYTLGLATVS
THGANPAVYPKLPYDPIKDFTPVANVVTVPNVLVVHPSVPAKDFKAFVAYLKANPGKYSYASPGAGTLGH
LTAELFKQALGTKIVHVPYRGSGPALTDLLAGQVQVMFDNLPSSLPHIKSGKLRALAVAWPTRLAALPDV
PTFAELGFPDLNQPSWYGLVAPAGTPADVVAKLHDAAVKALADPAVRKRLEELGLVPPGNTPAQFAAQIQ
AQFAKWKPVADK
>gnl|CDD|270296 cd13578, PBP2_Bug27, Aromatic solutes transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold. Bug27 binds non-carboxylated solute nicotinamide, in contrast to BugD (aspartic acid transporter) and BugE (glutamate transporter) which both bind aliphatic carboxylated ligands. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity
YPSKPIRLVVPFAPGGGTDIVARLLAQKLSEKLGQPVVVENRPGAGGNIGTDAVAKAAPDGYTLLLASSS
HAINPALYPKLPYDPVKDFAPVSLIASSPLVLVVNPSSPAKTLAELIAAAKANPGKLNYASSGNGSSPHL
AGELFKSAAGIDMVHVPYKGSGPALTDLLGGQVDLMFDSLPSALPHVKAGKLRALAVTSAKRSPLLPDVP
TVAEAGLPGFEVSSWYGLFAPAGTPAAIVARLNAAVNKALADPDVRARLAAQGVEPVGSTPAEFGAFVAA
EIARWAKVVKE
>gnl|CDD|270297 cd13579, PBP2_Bug_NagM, Uncharacterized NagM-like protein of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter
AAAGPLRILVGFPPGGSADVVARLLAEKLKDALGQTVIVENRPGAGGRIAAQALKAAPPDGSTLLLTPDH
TMTIYPLTYKKLGYDPATDFTPVALVATFPLALAVGPASPVKTLKDFVAWAKAHPGQASVGVPAPGSLPH
FLGLLLGKALGVDLTHVPYRGSAPMVQDLLGGQIAAGVDTLGDLLPHHRAGKLRILAVSGAQRSAALPDV
PTFAELGFKGLEASGWYGFFAPAGTPAAVVDRLSAAIRAALASPDVREKLAELGLEPAGGSPAELARRLK
AERARWGPVVKA
>gnl|CDD|270298 cd13580, PBP2_AlgQ_like_1, Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold. This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide
EPVTITIVANLGGNPKPDPDDNPYTKYLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNDPQL
SITLVKQGALWDLTDYLDKYYPNLKKIIEQEGWDSASVDGKIYGIPRKRPLIGRNGLWIRKDWLDKLGLE
VPKTLDELYEVAKAFTEKDPDGNGKKDTYGLTDTKDLIGSGFTGLFGAFGAPPNNWWKDEDGKLVPGSIQ
PEMKEALKFLKKLYKEGLIDPEFAVNDGTKANEKFISGKAGIFVGNWWDPAWPQASLKKNDPDAEWVAVP
IPSGPDGKYGVWAESGVNGFFVIPKKSKKPEAILKLLDFLSDPEVQKLLDYGIEGVHYTVKDGGPVNIIP
PDKQEVGDATLDYFQGSLALEKYKLTNNGERKSDAKKEALDERVVNANDEENENIAVGPPTETLVSPTEK
YGATLDKLEDDAFTKIIMGQIPLDEFDKFVEEWKKSGGDEITKEVNEWYKE
>gnl|CDD|270299 cd13581, PBP2_AlgQ_like_2, Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold. This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide
KVTLTIFVRKSPLVEDYNENLFFKRLEEKTGIKIEWETVPEDAWAEKKNLMLASGDLPDAFLGAGASDAD
LMTYGKQGLFLPLEDLIDKYAPNLKALFDENPDIKAAITAPDGHIYALPSVNECYHCSYGQRMWINKKWL
DKLGLEMPTTTDELYEVLKAFKEQDPNGNGKADEIPLSFSGLNGGTDDPAFLLNSFGINDGGYGGYGFVV
KDGKVIYTATDPEYKEALAYLNKLYKEGLIDPEAFTQDYDQLAAKGKASTAKVGVFFGWDPGLFFGEERY
EQYVPLPPLKGPNGDQLAWVGNSSGYGRGGFVITSKNKNPEAAIRWADFLYSPEGSLQANFGPEGEDWEK
NPDGEYGVDGPPAAYKILEPSEGEQNVAWADGGPGAIPDEYRLKQVTDEDMDEAEARLDEAKKYYEPYAP
PDNSPPPALLDEEAEKISTIQTDINNYIEQKRAKFITGGGDDKEWDAYVKQLEKMGLDEYLEIYQKAYDR
>gnl|CDD|270300 cd13582, PBP2_AlgQ_like_3, Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold. This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide
PITFTFFSADSNATPDDFKTPVAKKITELTGVTLEIEYLVGGEKQKIGLMIASGDLPDLIYAKGDTDKLI
EAGALVPLDDLIEKYGPNIKKWYGDYLLKKLRSEDGHIYYLPNYRVEDAPWYPNGGFWLQHDVLKELGYP
KIKTLDDYENLIKDYKKKYPTINGQPTIGFTALTDDWRFLISVTNPAFLAGYPNDGEVYVDPKTLKAKFH
YTRPYYKEYYKWLNELWNEGLLDKESFTQKYDQYLAKIASGRVLGFYDAGWDIGNAITALKAKGKDERLY
AYYPVAVGVDDKDYNYGDPGYLGGDGIAITKSCKDPERAFKFLDWLASEEAQKLINWGIEGVDYDVDDGK
RVYLTEEMAAKNKDPDYTKKTGIGKYWYFPPRKGGKFSDGTGNSPTPDPEEEYIYTAVEKKVKAAYKAEL
WKDMFPPFEEFPVKPYGYAWPIGIPDESIAIINQKASDITRKYIPKAIMAKPDDFDSIWDEYLKDLEKAG
YKKLEEYYTKQIKE
>gnl|CDD|270301 cd13583, PBP2_AlgQ_like_4, Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold. This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide
PLTLSMMYRDHPNYPVKDDWLIWKEIEEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDIIPVLYPGEEN
EFVASGALLPISDYLDYMPNYKKYVEKWGLGKELATGRQSDGKYYSLPGLHEDPGVQYSFLYRKDIFEKA
GIKIPTTWDEFYAALKKLKEKYPDSYPYSDRWNSNALLLIAAPAFGTTAGWGFSNYTYDPDTDKFVYGAT
TDEYKDMLQYFNKLYAEGLLDPESFTQTDDQAKAKFLNGKSFVITTNPQTVDELQRNLRAADGGNYEVVS
ITPPAGPAGKAINGSRLENGFMISSKAKDSKNFEALLQFLDWLYSDEGQELATWGVEGETYTKEGDGKVY
LADSNTPALNPSGTKLLQKDFGFSDGVFTDGGGTSGKLSEMTPEEAEFNDTMLENRKPVPPIPPPPMTEE
ELEQLSLLETPLKDFVDEMTAKFITGKRSMDEWDAFVAEVKKLGLDQLLDIYNDAYKR
>gnl|CDD|270302 cd13584, PBP2_AlgQ1_2, Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 periplasmic binding fold. This group represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria such as Sphingomonas sp. A1. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that includes alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide
ELTLWIHMHFRDKWPNDNDLPVYKEMERKTNVKLNFVANPVAQNSQEQFNLMMASGQLPDIIGGDWLKDK
GGFEKYGEDGAFLPLNDLIDQYAPNLKKFLDEHPDVKKAITTDDGNIYGFPYLPDGDVAKEARGYFIRKD
WLDKLGLKTPSTIDEWYTVLKAFKERDPNGNGKADEVPLILTKPGYDETGRLINAWGAYMDFYQENGKVK
YGPLEPGFKDFLKTMNQWYKEGLIDPDFFTRKAKAREQNIMNGNIGGFTHDWFASTGTFNLALLKNVPDF
KLVAVPPPVLNKGQTPYEEDSRQIAKGDGAAITASNKNPVLAIKWLDYAYSEEGRLLSNFGVEGESYTIK
NGKPVFTDDVLKDPQPLVNALSLYYGAQIPGGFWQDYEYEEQWTTPEALESKDIYAKNKYVMPLPPVTLT
EEERSIYDSIMTDIDTYVNEMGQKWIMGKEDADDNWDEYQKKLKSLGLYEALEIQQAAYDR
>gnl|CDD|270303 cd13585, PBP2_TMBP_like, The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold. This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLTFWDWGQPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFA
SNGALLDLDDYIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDEL
LEAAKKLTDKKGGQYGFALRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGV
APSSATTGGDEAVDLFASGKVAMMIDGPWALGTLKDSKVKFKWGVAPLPAGPGGKRASVLGGWGLAISKN
SKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWP
EVYPILSEALQEALLGALGKSPEEALKEAAKEI
>gnl|CDD|270304 cd13586, PBP2_Maltose_binding_like, The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold. This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TITVWTDEDGELEYLKELAEEFEKKYGIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAA
GLLAPIPEYLAVKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALAKKFNDKA
GGKYGFAYDQTNPYFSYPFLAAFGGYVFGENGGDPTDIGLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDI
ADALFKEGKAAMIINGPWDLADYKDAGINFGVAPLPTLPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAE
YLTSDEAQLLLFEKTGRIPALKDALNDAAVKNDPLVKAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVA
SGKATPEEAAKDAVAAI
>gnl|CDD|270305 cd13587, PBP2_polyamine_2, The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold. This family represents the periplasmic binding domain that functions as the primary polyamine receptor of an uncharacterized ABC-type transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLRILTWAGYAPEDLLEKFENETGIKVQVTTSNNNEEMISKLRATGGGGFDLAQPSQRIAPNYEEFGLYQ
PIDESKIKVAQFPPSLLESTKLGTTINGKRYAVPFDWGTEGLTVNSTKAPDVSGFSYGDLWAPEYAGKVA
YRLKSPLTGLGLYADATGEDPFNRYLDYKDEAKYQKILDQVLQFLIERKANVKAYWNNADEALAAFRSGG
CVIGQTWDSTGLKLNRENPPIDYGAPKEGALGWIDTFAIPAKAENVDQAYAFINFMLRPEIAAMFTNATG
YNTAAVGAQEFL
>gnl|CDD|270306 cd13588, PBP2_polyamine_1, The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold. This group represents the periplasmic binding domain that functions as the primary high-affinity receptor of an uncharactertized ABC-type polyamine transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
ELNVLTWPGYADPDWVTAFEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQP
IDTSKIPNYANIDPRLRNLPWLTVDGKVYGVPYDWGANGLAYNTKKVKTPPTSWLALLWDPKYKGRVAAR
DDPIDAIADAALYLGQDPPFNLTDEQLDAVKAKLREQRPLVRKYWSDGAELVQLFANGEVVAATAWSGQV
NALQKAGKPVAYVIPKEGATGWVDTWMILKDAKNPDCAYKWLNYMLSPKVQAAVAEWTGYAPSNPEACA
>gnl|CDD|270307 cd13589, PBP2_polyamine_RpCGA009, The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold. This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLVVATWGGSYEDAQRKAVIEPFEKETGIKVVYDTGTSADRLAKLQAQAGNPQWDVVDLDDGDAARAIAE
GLLEPLDYSKIPNAAKDKAPAALKTGYGVGYTLYSTGIAYNTDKFKEPPTSWWLADFWDVGKFPGPRILN
TSGLALLEAALLADGVDPYPLDVDRAFAKLKELKPNVVTWWTSGAQLAQLLQSGEVDMAPAWNGRAQALI
DAGAPVAFVWPKEGAILGPDTLAIVKGAPNKELAMKFINFALSPEVQAALAEALGYGP
>gnl|CDD|270308 cd13590, PBP2_PotD_PotF_like, The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
ELNIYNWSDYIDPEVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGGSGYDLVVPSDYMVERLIKQGLLE
PLDHSKLPNLKNLDPQFLNPPYDPGNRYSVPYQWGTTGIAYNKDKVKEPPTSWDLDLWDPALKGRIAMLD
DAREVLGAALLALGYSPNTTDPAELAAAAELLIKQKPNVRAFDSDSYVQDLASGEIWLAQAWSGDALQAN
RENPNLKFVIPKEGGLLWVDNMAIPKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELLPPE
LLDNPALYPPIEPLAKLLTFKDVDGEALELYDRIW
>gnl|CDD|270309 cd13591, PBP2_HisGL1, The catalytic domain of hexameric long form HisGL1; contains the type 2 periplasmic binding protein fold. Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea
MLRIAVPNKGSLAEPAAELLVEAGYRQRRDGKELVVRDPDNEVEFFFLRPRDIAIYVSSGILDIGITGRD
LLSDSGANATELLDLGFGRSTFRFAAPPGSTLTVADLAGLRVATSYPNLVRRHLADLGVDATVVRLDGAV
EISVQLGVADAIADVVETGRTLKQAGLRVFGEPILKSEAVLIRRSGAQTNKPAQQQLVRRLQGV
>gnl|CDD|270310 cd13592, PBP2_HisGL2, The catalytic domain of hexameric long form HisGL2; contains the type 2 periplasmic binding protein fold. Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea
RLRIAIQKKGRLSEKSLDLLAGCGIKFRRGNRLLIALAENLPIDLLFLRDDDIPTFVGDGVVDLGITGEN
VLEEAQLAGPNVEEVMDLGFGKCRLSVAVPEDGDYTGPAQLNGKRIATSYPNLLKRYLDELGVKASIVYV
SGSVEVAPRLGLADAICDLVSSGATLRANGLKEVETILESEAVLIGRPNPSKEKKALLDLLLRRIDGV
>gnl|CDD|270311 cd13593, PBP2_HisGL3, The catalytic domain of hexameric long form HisGL3; contains the type 2 periplasmic binding protein fold. Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea
MLRLGIPSKGSLAEATLELLKKAGLKVSRGNPRQYFASIDDLPEVEVLLLRAQEIVRYVADGDLDLGITG
YDWVRESGADVVVVADLGYGPVRLVLAVPEDWIDVSTMADLAAFRAEDGRGLRIATEYPNLTRRFFAEKG
GVKVQIVFSWGATEAKPPEGVADAIVDLTETGTTLRANRLKIIDDGVLESQAVLIANKRALKDPWKREKI
EDLLELLEAA
>gnl|CDD|270312 cd13594, PBP2_HisGL4, The catalytic domain of hexameric long form HisGL4; contains the type 2 periplasmic binding fold. Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea
MIRIAPPNKGRLSEPTLKLLERAGIKVLASDERALFAPTSDPDIELLFARAADIPEYVEDGAADLGITGY
DLVVESGADVEELLDLGFGRAKLVLAVPEDSGIRSPEDDPKGKRVATEFPNITRQYFEELGIDVEIVEVS
GATEIAPHIGIADAIVDLTSTGTTLRVNGLKVIDTVLESSARLIANKNSLAVEKDKIEELVTALKGV
>gnl|CDD|270313 cd13595, PBP2_HisGs, The catalytic domain of hetero-octomeric short form HisGs; contains the type 2 periplasmic binding protein fold. Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea
MLTIALPKGRLLEEVLPLLEKAGIDPSELLEESRKLIFEDEEGDIRFILVKPSDVPTYVEHGAADIGIVG
KDVLLEQERDVYELLDLGIGKCRFSVAGPPGRGLDSPLRRKRVATKYPNIARRYFASKGVDVEIIKLNGS
VELAPLVGLADAIVDIVETGNTLKENGLEELEEIMDISARLIVNRASYKTKRDEIKELIERLREV
>gnl|CDD|270314 cd13596, PBP2_lipoprotein_GmpC, The periplasmic substrate-binding domain of the membrane-associated lipoprotein-9 GmpC; contains the type 2 periplasmic-binding protein fold. This group includes the membrane-associated lipoprotein-9 from Staphylococcus aureus that binds the dipeptide glycylmethionine (GlyMet). The lipoprotein-9 has both structural and sequential homology to the MetQ family of substrate-binding protein. The GlyMet binding protein belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea
TVKIGVTGEDTDIWDKIVEEAEEAGIKLELVNFSDYSQPNKALNDGDIDLNAFQHYAYLVQYNSKNNADL
TAIGDTVIAPMGIYSKKITSVDELPDGAKIAIPNDPSNLSRALFILQAAGLIKLKKDAGDFPTVNDITEN
PKNLEIVPVDADQVYRALNDVDAAVINNTFALDAGLDPKKDAIFLEDPSSYGSKPYINLIAVREEDKDNP
LYKKLVETYHDERVQKAVEE
>gnl|CDD|270315 cd13597, PBP2_lipoprotein_Tp32, The substrate-binding domain of the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum binds L-methionine; the type 2 periplasmic-binding protein fold. This group includes the lipoprotein Tp32, a periplasmic component of a methionine uptake transporter system, and its closely related homologs. The Tp32 has both structural and sequential homology to the MetQ family of substrate-binding protein, and thus it belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea
TLKVGATPVPHAEILEFIKPELKKQGIDLEIVEFTDYVQPNTALADGELDANYFQHVPYLESFNKEKGYD
LVAVAGVHLEPMGLYSKKYKSLEDLPDGATIAIPNDPTNQGRALLLLEEAGLITLKDGAGLTATVKDIVK
NPKNLKFKELEAAQLPRSLDDVDAAVINGNYALEAGLNPKKDALALEDKDNSPYANILVVRKGNEDDPRI
KKLAKALQSDEVKDFIEEKYDGAVVP
>gnl|CDD|270316 cd13598, PBP2_lipoprotein_IlpA_like, Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus and similar lipoproteins; the type 2 periplasmic binding protein fold. This group includes the IlpA protein which has both structural and sequential homology to the MetQ family of substrate-binding protein, and thus belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea
PIKVGVIRGPDAQIWEVVQKVAKEKGLDVELVTFNDYAQPNEALAAGDLDANAFQHKPYLDAQIKARGYK
LVIVGNTFVYPIGLYSKKIKSLAELPNGATVAIPNDPSNEGRALLLLQKEGLIKLKDGVGLLATVRDIAE
NPKKLKIVELDAGQLPRALDDVDLAAINTDYASKAGLTPARDAIAQEDKRSPYANVIAVREDDKDAPWVK
TLVQAYQSEEVKAFALK
>gnl|CDD|270317 cd13599, PBP2_lipoprotein_Gna1946, The membrane-associated lipoprotein Gna1946 from Neisseria meningitidis; the type 2 periplasmic binding protein fold. Gna1946 shares significant structural and sequence homology with the periplasmic substrate-binding domain of ATP-binding cassette (ABC) transporter involved in uptake of methionine (MetQ). The members of the MetQ-like family include the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum, the membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus, and Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus. They all function as a receptor for methionine. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea
TIVIGFTPGPYGDMVKNGVAPYLEKKGYEVKLKEFTDYVQPNNALANGEIDANVFQHKPYLDAFNKENGL
DLVGIVQVPTPPMGLYSNKHKSLEEVKDGATVAIPNDPSNLARALVMLQDLGWITLKDNIDPLKASVNDI
AENPKNIKIVELEAAQLPRSLDDVDFAAIQGNFAISSGIKLTSALALEEMTDPYVNVVAVKTADKDKQFA
KDVTAAYNSDAFKAYIHA
>gnl|CDD|270318 cd13600, PBP2_lipoprotein_like_1, Putative periplasmic-binding component of ABC-type methionine uptake transporter system-like; the type 2 periplasmic binding protein fold. This subgroup shares significant sequence homology with the periplasmic substrate-binding domain of ATP-binding cassette (ABC) transporter involved in uptake of methionine (MetQ). The members of the MetQ-like family include the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum, the membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus, and Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus. They all function as a receptor for methionine. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea
TLKVATNSGPMTEILEYIAAELAPDGITIEPVQVSDYVQANRAVAAGEIDANFFQHQPFMEQFNEANGFE
LVAVQPIYHWAFGFYSKKYKSVEDLPDGAKVAIPNDPANQARALLLLQRAGLITLKPGVDPTTATLADIV
TNPKNLKFTEVDLLALPRALDDVDLAFGYPSYFDAAGLTPKDGILLEEPDAKRFAIQLVAREDNKDSPKI
KKLKEAFTDPRVRKFLET
>gnl|CDD|270319 cd13601, PBP2_TRAP_DctP1_3_4_like, Periplasmic substrate-binding component of uncharacterized TRAP-type C4-dicarboxylate transporter subfamilies; the type 2 periplasmic-binding protein fold. This model includes uncharacterized DctP subfamilies of the TRAP Transporters. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLRVADSFPPQHPVSTEGTKPWMKRVEEATNGAVKFEHYPSGQLGKPKEQLDAVRSGVVDIGYIFPGYVS
DKLPLNGVVQLPGLGTTSVEGSAALWKATGGLLQQEFEKNGVVPLFVHVLPPYQVLTKKPPVDSLADLKG
LKLRSSGGALSLMAESLGAVPVSMPAPEVYEALSRGVVDGTLGPLASVISYKLAEVVKYVTTNGNFGSGS
FSYVMNQDTWDALSDEQRKALDEASGEAEAALAEALDAAVEELVAEAAAEGIEFVELSDEELAALEALLA
AVTDDWIERLDARGLDGQAVLD
>gnl|CDD|270320 cd13602, PBP2_TRAP_BpDctp6_7, Substrate-binding domain of a pyroglutamic acid binding DctP subfamily of the tripartite ATP-independent periplasmic transporters; contains the type 2 periplasmic binding protein fold. DctP6 and DctP7 groups of the TRAP transporters that involved in pyroglutamic acid transport. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLDMAGEYPAGNFHTQEAPFFAELVAEATGGKVKITVHPGGSLGLKGPEILRAVRDGAVDIGDVLLSYLA
GDDPLFEGDSLPFLATSYDEARKLYDAARPYLEKRLAERNAKLLYAVPWPPQGLFSKKPITSLADLKGLK
IRTYDPTTAEFVEALGAAPVTLPFAEVVPALATGVIDCALTSTSSGVDGKWWEVTKHFYPINYGWPLNMV
AVNLDAWNALSPDVQAALLEAAAELEDEGWALSAQETEEALACLRGNGMTVVEPSPADLRQALKAAGEPV
LPEWLKRAGPECAAILNAYR
>gnl|CDD|270321 cd13603, PBP2_TRAP_Siap_TeaA_like, Substrate-binding domain of a sialic acid binding Tripartite ATP-independent Periplasmic transport system (SiaP) and related proteins; the type 2 periplasmic-binding protein fold. This subfamily includes the periplasmic-binding component of TRAP transport systems such as SiaP (a sialic acid binding virulence factor), TeaA (an ectoine binding protein), and an uncharacterized TM0322 from hyperthermophilic bacterium Thermotoga maritima. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLKLAHVAPEGSPYHKAAEKFAELVEEKSNGRIKVEIFPNGQLGGEREMLEGVQLGTIDMAVISTANLSN
FVPEFGVLDLPFLFRDYEHARKVLDGPLGKELLEKLEEKGLKVLGYGENGFRQITNNKPPIKSPEDLKGL
KIRVPPSPIYIATFKALGANPTPMAFGEVYTALQQGVVDGQENPLSTIYSSKFYEVQKYLTLTNHVYSPG
LLLMNKKFWDSLPEELQKAILEAAKEAADYQRELAAEAEEEALEELKEKGVTVTEPDDRAAFREAAAPVY
DEFAKKGGGKELIDAIQ
>gnl|CDD|270322 cd13604, PBP2_TRAP_ketoacid_lactate_like, Substrate-binding domain of an alpha-keto acid binding Tripartite ATP-independent Periplasmic transporter and related proteins; the type 2 periplasmic-binding protein fold. This family constitutes TRAP transporters that bind to ketoacids such as pyruvate and alpha-ketobutyrate, xylulose, and other unknown ligands. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLRMQTSWPALPGLGTGAEELAKRVEEMSGGRIKIEVFPAGSLVPAFETFDAVSNGTLDGGHTWPAYWSG
KDPAFALFGAVPFGMDPLEYLAWLYYGGGKELLDELYAPFNVKPFPCGNTGPEAGGWFKKEIKSVEDLKG
LKIRAPGLGGEVLARLGASPVNLPGGEIYTALERGAIDAAEFSGPANDLALGFHKVAKYYYYPGWHQPAP
VLELIINKDVWEALPPDLQAIIEAACQAANLDMLAEAEAQNAKALKELRAKGGVEVIRFPDEVLEAFRAA
AQEVWEEEAAKDPLFKKVYDSQRAFR
>gnl|CDD|270323 cd13605, PBP2_TRAP_DctP_like_2, Substrate-binding component of uncharacterized Tripartite ATP-independent Periplasmic transporter; the type 2 periplasmic-binding protein fold. This family represents the TRAP Transporters that are specific to various ligands, including sialic acid (N-acetyl neuraminic acid), glutamate, ectoine, xylulose, C4-dicarboxylates such as succinate, malate and fumarate, and keto acids such as pyruvate and alpha-ketobutyrate. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. This CD also included some eukaryotic homologs that have not been functionally characterized. TRAP transporters are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
VLRISVENAPTHVQTRAMRRFAEDVEERSAGRLKVEVFPSAQLYKDKDVVRALAQGAVEMAVPGTWQLSR
IDPEYGLFLLPMFFGATAMQTHRFAQGPLGDELLTRIERKLRVQVLGRWRDGGGYVFFTDKAVDSPEDLA
GLKIRVAGGAANVARLRAFGASPVSIPASDLPLALQQGTIDGILTTPETVASARLWESGIRFVFEDRQYF
AQYVPVVSDRFWAKLPEEQRQVLRETWNEIIAQQRAHAAEAQAEAREQMRANGVTITVPPPAELADWRER
LLLLQPEVVRKLGIDPELIKQVD
>gnl|CDD|270324 cd13606, PBP2_ProX_like, Bacterial substrate-binding protein ProX of ABC-type osmoregulated transporter and its related proteins; the type 2 periplasmic-binding protein fold. This group includes periplasmic substrate-binding component of ABC transport systems from gram-negative and -positive bacteria that are involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TVVVGSADFPESEILAEIYAQALEAAGVKVTRKLNIGSREVYLPALEDGSIDLVPEYTGNLLQYLDKDAT
ATDPEEVYAALKAALPEGLEVLDPSPAEDKDALVVTKETAEKYGLKSIADLAPVAGELTLGGPPEFKTRP
YGLPGLKEVYGVTFKEFKPLDAGGPLTVKALKDGTVQVANIFTTDPAIADNGLVVLEDPKNLFPAQNVVP
LVRKAKLDDKAADALNAVSAKLTTEDLTELNKQVVGDKADPADVAKEWLK
>gnl|CDD|270325 cd13607, PBP2_AfProX_like, Substrate-binding protein ProX of ABC-type osmoregulatory transporter from Archaeoglobus fulgidus and its related proteins; the type 2 periplasmic-binding protein fold. This subfamily includes the periplasmic substrate-binding protein ProX from the hyperthermophilic archaeon Archaeoglobus fulgidus and its related proteins. AfProX is involved in uptake of compatible solutes such as the trimethylammonium compound glycine betaine and the dimethylammonium compound proline betaine, but the relative substrate preference is not known. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. AfProX belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TVVIGSKTFTEQYILAEMIAQLLEEAGYPAEHREGLGGTRVLFEALKSGEIDVYVEYTGTLYAEILKRPE
TWDPAAVLAELKEALAERGIVVAGPLGFENTYALAMREDRAEALGIRTISDLLARAPDLRFGFDPEFLDR
PDGWPALRRVYGLPFKEVRGLDHTLAYRALKSGQVDVIDAYTTDARIDAYDLRVLEDDRGAFPPYDAVLL
YRADLAERAPKAVAALRRLEGRIDADTMRALNAQVDLEKRSEAEVAAEFLA
>gnl|CDD|270326 cd13608, PBP2_OpuCC_like, Substrate-binding protein OpuCC of ABC-type osmoregulatory transporter and related proteins; the type 2 periplasmic-binding protein fold. This subfamily includes the periplasmic substrate-binding protein OpuCC of the ABC transporter OpuC (where Opu is osmoprotectant uptake), which can recognize a broad spectrum of compatible solutes, and its paralog OpuBC that can solely bind choline. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TIRIGSQSTTESQILAEMVKQLIEHYTDLKVELINNLGSSTVQHQAMLNGDANISAARYTGTDLTGELGM
EPIKDPEKALKVVQKEFQKRFDQTWFDSYGFANTYAFMVTKEFAEKYNLKKVSDLKKVADNLKLGVDTSW
LNRKGDGYPGFKETYGFDFGTVYPMQIGLVYDAVASGKMDVVLGYSTDGRIKSYDLVVLEDDKQFFPPYD
ASPVATNEILKKYPELEEILEKLEGKISTETMQELNYQVDNDLKEPSVVAKEFLE
>gnl|CDD|270327 cd13609, PBP2_Opu_like_1, Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 periplasmic-binding protein fold. This group includes the periplasmic substrate-binding component of a putative ABC transport system that is predicted to be involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. The relative substrate preference of this group is not known. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TIVIGSKNFTEQLILGNMYADLIEANTDIKVERKLNLGGSSVCFSALKNGDIDMYVDYTGTILVNILKEP
PISDPDEVYNTVKELMKEKYNLEVLKPLGFNNTYTLAVRKETAEKYNLKTISDLAKVSDELTLGCTLEFL
NREDGLPGLEKTYGLNFKDVKGLDGSLRYTALENGEVDVIDAFSTDGLLKKFDLVVLEDDKNFFPPYYAV
PLVREETLEKYPELEDVLNKLAGKISEETMRELNYKVDELGKDPEDVAHEFLV
>gnl|CDD|270328 cd13610, PBP2_ChoS, Substrate-binding domain ChoS of an osmoregulated ABC-type transporter and related proteins; type 2 periplasmic-binding protein fold. Osmoprotectant binding lipoprotein ChoS of Lactococcus lactis is predicted to be involved in uptake of compatible solutes such as choline and glycine betaine, but the relative substrate preference is not known. To counteract the efflux of water, microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. ChoS belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
SIVIAGKLGSEPDILINMYKLLIEEETPDLQVTLKPNFGKTSFLFNALKSGDIDIYPEFTGTVLETLLKE
PPKSNDPMEVYEQARDGLAKQYQLTYLKPMAYNNTYALAVKKEFAKQHNLKTISDLQKVQDKLKAGFTLE
FMDREDGYKGLQKAYGLNFNVKSMEPALRYQAINNGQVNVIDAYSTDSEIKQYDLVVLKDDKHLFPPYQG
APLMREEFLKKHPELVKALNKLAGKITDEEMQEMNYRVDVKHKSAAKVAKEYLQ
>gnl|CDD|270329 cd13611, PBP2_YehZ, Substrate-binding domain YehZ of an osmoregulated ABC-type transporter; the type 2 periplasmic-binding protein fold. Osmoprotectant binding lipoprotein YehZ of Clostridium sticklandii is predicted to be involved in uptake of compatible solutes such as choline, L-proline and glycine betaine, but the relative substrate preference is not known. To counteract the efflux of water, microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. YehZ belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TITVGSKDFTEQLILGKITVQALQAAGADVTDKTNLGGSASARQALENGQVDVYWEYTGTAWITYLGHTE
PILDPQEQYEAVKDLDAEKGLVWLDPAPLNNTYALAMREATAEELGITTLSDLALAKLPPGDRTFCVDAE
FASRPDGLPPLLEAYGFEFPRANVRQMDTGLVYTATANGQCDFGEVFTTDGRIKALDLVVLEDDKGFFPA
YNAAPVVRTEVLDAHPELAEILNPISAKLDNDTMQELNARVDVDGEDPADVARDWLV
>gnl|CDD|270330 cd13612, PBP2_ProWX, Substrate-binding protein ProWX of ABC-type osmoregulated transporter and its related proteins; the type 2 periplasmic-binding protein fold. Osmoprotectant binding lipoprotein ProWX of Helicobacter pylori is predicted to be involved in uptake of compatible solutes such as choline, L-proline and glycine betaine, but the relative substrate preference is not known. To counteract the efflux of water, microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. ProWX belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TIHIATKPMTEQYILGEMLKQLIEQDTDLKVELTKGVGGGTSNIHPAMVKGEFDLYPEYTGTGWLFVLKK
DGTYSEELFDQLQKEYEEKYNLTWLGLYGFNNTYGLAVRKELAEKYNLKTYSDLAKVSNQLVFGAEYDFF
EREDGYDALQKAYGFNFKKTVDMDIGLKYQAIESGKVDVINVFTTDGQLSDADIVVLEDDKGFFPSYYAG
TVVREETLEKYPELEDVLEKLTGLISDEDMAEMNYQVEIEKKDPKDVAKEFLEEKGL
>gnl|CDD|270331 cd13613, PBP2_Opu_like_2, Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 periplasmic-binding protein fold. This group includes the periplasmic substrate-binding component of a putative ABC transport system that is predicted to be involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. The relative substrate preference of this group is not known. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
RIIIGSKNFTEQVILGELLAQQIEARTDLKVERRFNLGGTFICHQALLSGAIDAYVEYTGTALTAILKQP
PIRDPQRVYEQVKQLYADRFGLEVMPPLGFENTFAILVRGEDARKLGLKTLSDAAPYTPGWRAGFGYEFL
ERADGYPGLAKTYGLKFAKTPRVMDLGLLYRALAQKQVDLIAGNSTDGLIAALDLVILEDDRHYFPPYQA
VPVVRQATLAKYPELRTAIAELAGKISAETMQQMNYQVDGEHRDVAEVAREFLK
>gnl|CDD|270332 cd13614, PBP2_QAT_like, Substrate-binding domain of quaternary amine ABC-type transporter; the type 2 periplasmic-binding protein fold. This group includes the periplasmic substrate-binding component of a putative quaternary amine ABC transport system that is predicted to be involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. The relative substrate preference of this group is not known. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
AIRVGSKNFTEQFILGEMYALALEDAGIKVERKLNLGGTLIAHQALVNGEIDLYPEYTGTALLTVLKGEP
SSDAKQVYKTVKDAYAEQFQLTWLEPAPFNNTYALVMTRETAEKYGIKTLSDLAKAAGELVFGGGPEFQD
REDGLPGLKAKYGAFDFKEFVQVDPLGLRYQALAQGQIDVAVGFGTDGQIAAYGLVVLEDDKNLFPPYQV
APVVRQDVLDANPKIAEVLNKLSALLDNETMQRLNYEVDGNKREPKDVAREFLK
>gnl|CDD|270333 cd13615, PBP2_ProWY, Substrate-binding domain of ABC-type osmoregulated transporter; the type 2 periplasmic-binding protein fold. Osmoprotectant binding lipoprotein ProWY of Streptococcus thermophilus is predicted to be involved in uptake of compatible solutes such as choline, L-proline and glycine betaine, but the relative substrate preference is not known. To counteract the efflux of water, microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. ProWY belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
AIRVGSKDFTENLIVAEIYALALEDAGYKVKRKPNISSSVVHQALTSGQIDLYPEYTGTGLLAVLKKEAI
TDPQKVYATVKDGYAKKFNLVWLDYAPANDGQGLVIRTSVAKKYGIKTISDLQKNASQIRFASQGEFDQR
EDGLPGLEKVYGKFSFKSTKVYDNGLKYQVLANDKADITPAYTTEGQLDTSKFTLLKDDKHVWPPYNLAP
VVRKDVLKANPKIASALNKVSAKLTTKTLTQLNAKVDVDKQEYADVAKDFYL
>gnl|CDD|270334 cd13616, PBP2_OsmF, Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 periplasmic-binding protein fold. Osmoprotectant binding lipoprotein OsmF of an ABC transporter (YehZYXW) from Escherichia coli is predicted to be involved in uptake of compatible solutes such as choline, L-proline and glycine betaine, but the relative substrate preference is not known. To counteract the efflux of water, microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. OsmF belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
PVVVGSKIDTEGALLGNMIVLALEAHGFPVEDKTGLGTTPVVRKALLSGEIDLYPEYTGNGAFFFPEADD
PVWKDARKGYETVKELDAKNNGLVWLDPAPANNTWAIAVRRDLAEKNNLKTLADLAAYVNEGGAFKLAAS
AEFVERPDALPAFEKAYGFKLSKDQLVILSGGNTAQTEQAAAQGTSGVNAAMAYGTDGAIAALGLVVLED
PKGAQPVYAPAPVVRQEVLEAYPEIAEILKPVFATLDLKTLQELNARIAVEGESAEDVARDYLK
>gnl|CDD|270335 cd13617, PBP2_transferrin_C, The C-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily. Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helices and beta sheets domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor
RKRVVWCAVGHEEKLKCDQWSVNSGGKVECASASTTEDCIAKILKGEADAMSLDGGYVYTAGKCGLVPVL
AENYKSSDSSSPDCVDRPEEGYLAVAVVKKSDSDLTWNNLKGKKSCHTAVGRTAGWNIPMGLIYNQTGSC
KFDEFFSQSCAPGSDPNSSLCALCIGSGEGLNKCVPNSKEKYYGYTGAFRCLVEKGDVAFVKHQTVLQNT
DGKNPEDWAKDLKEEDFELLCLDGTRKPVTEARSCHLARAPNHAVVSRPDKAACVKQILLHQQALFGRNG
SDCSDKFCLFQSETKDLLFNDNTECLAKLHGKTTYEKYLGPEYVTAITNLR
>gnl|CDD|270336 cd13618, PBP2_transferrin_N, The N-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily. Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helices and beta sheets domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor
TVRWCAVSEPEATKCQSFRDNMKKVDGPSVSCVKKASYLDCIRAIAANEADAVTLDGGLVYEAGLAPYKL
KPVAAEVYGSKEDPQTHYYAVAVVKKGSGFQLNQLQGKKSCHTGLGRSAGWNIPIGTLRPDLPWTEPREP
LEKAVARFFSASCVPGADGGQFPQLCRGKGEPKCACSSQEPYFGYSGAFKCLKDGAGDVAFVKHSTVFEN
LPDKADRDQYELLCLDNTRKPVDEYKDCHLARVPSHAVVARSVNGKEDLIWELLNQAQEHFGKDKSSEFQ
LFSSPHGKDLLFKDSAIGFLRVPPRMDSGLYLGYEYVTAIRNLR
>gnl|CDD|270337 cd13619, PBP2_GlnP, Glutamine-binding domain of ABC transporter, a member of the type 2 periplasmic binding fold protein superfamily. Periplasmic glutamine binding domain GlnP serves as an initial receptor in the ABC transport of glutamine in eubacteria. GlnP belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TYTIATDSTFAPFEFQNDDGKYVGIDVDLLNAIAKDQGFKVELKPMGFDAAIQAVQSGQADGVIAGMSIT
DERKKTFDFSDPYYDSGLVIAVKKDNTSIKSYEDLKGKTVAVKNGTAGATFAESNKEKYGYTIKYFDDSD
SMYQAVENGNADAAMDDYPVIAYAIKQGQKLKIVGDKETGGSYGFAVKKGQNPELLEKFNKGLKNLKANG
EYDKILNKYL
>gnl|CDD|270338 cd13620, PBP2_GltS, Substrate binding domain of glutamate or arginine ABC transporter, a member of the type 2 periplasmic binding fold protein superfamily. This family comprises of the periplasmic-binding protein component (GltS) of an ABC transporter specific for glutamate or arginine from Lactococcus lactis, as well as its closely related proteins. The GltS domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
KKKGKLVVGTSADYAPFEFQKMKDGKNQVVGADIDIAKAIAKELGVKLEIKSMDFDNLLASLQSGKVDMA
ISGMTPTPERKKSVDFSDVYYEAKQSLLVKKADLDKYKSLDDLKGKKIGAQKGSTQETIAKDQLKNAKLK
SLTKVGDLILELKSGKVDGVIMEEPVAKGYANNNSDLAIADVNLENKPDDGSAVAIKKGSKDLLDAVNKT
IKKLKDSGQIDKFVEDA
>gnl|CDD|270339 cd13621, PBP2_AA_binding_like_3, Substrate-binding domain of putative amino acid-binding protein; the type 2 periplasmic-binding protein fold. This putative amino acid-binding protein belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
LDRVKKRGVLRIGVALGEDPYFKKDPSTGEWTGFGIDMAEDIAKDLGVKVEPVETTWGNAVLDLQAGKID
VAFALDATPERALAIDFSTPLLYYSFGVLAKDGLAAKSWEDLNKPEVRIGVDLGSATDRIATRRLPNAKI
ERFKNRDEAVAAFMTGRADANVLTHPLLVPILSKIPTLGEVQVPQPVLALPTSIGVRREEDKVFKSFLSA
WIQKLRRSGQTQKIILKYL
>gnl|CDD|270340 cd13622, PBP2_Arg_3, Substrate binding domain of an arginine 3rd transport system; the type 2 periplasmic binding fold. This subgroup is similar to the HisJ-like family that comprises the periplasmic substrate-binding proteins, including the lysine-, arginine-, ornithine-binding protein (LAO) and the histidine-binding protein (HisJ), which serve as initial receptors for active transport. HisJ and LAO proteins belong to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
SKPLIVGVGKFNPPFEMQGTNNELFGFDIDLMNEICKRIQRTCQYKPMRFDDLLAALNNGKVDVAISSIS
ITPERSKNFIFSLPYLLSYSQFLTNKDNNISSFLEDLKGKRIGILKGTIYKDYLLQMFVINPKIIEYDRL
VDLLEALNNNEIDAILLDNPIAKYWASNSSDKFKLIGKPIPIGNGLGIAVNKDNAALLTKINKALLEIEN
DGTYLKIYNKYF
>gnl|CDD|270341 cd13623, PBP2_AA_hypothetical, Substrate-binding domain of putative amino-acid transport system; the type 2 periplasmic binding protein fold. This putative amino acid-binding protein belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
APTGTLRVAINLGNPVLAVEDATGGPRGVSVDLAKELAKRLGVPVELVVFPAAGAVVDAASDGEWDVAFL
AIDPARAETIDFTPPYVEIEGTYLVRADSPIRSVEDVDRPGVKIAVGKGSAYDLFLTRELQHAELVRAPT
SDEAIALFKAGEIDVAAGVRQQLEAMAKQHPGSRVLDGRFTAIHQAIAIPKGRPAALEYLNEFVEEAKAS
GLLERALQRA
>gnl|CDD|270342 cd13624, PBP2_Arg_Lys_His, Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 periplasmic binding protein fold. This group includes the periplasmic substrate-binding protein ArtJ of the ATP-binding cassette (ABC) transport system from the thermophilic bacterium Geobacillus stearothermophilus, which is specific for arginine, lysine, and histidine. ArtJ belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLVVGTDATFPPFEFVDENGKIVGFDIDLIKAIAKEAGFEVEFKNMAFDGLIPALQSGKIDIIISGMTIT
EERKKSVDFSDPYYEAGQAIVVRKDSTIIKSLDDLKGKKVGVQIGTTGAEAAEKILKGAKVKRFDTIPLA
FLELKNGGVDAVVNDNPVAAYYVKQNPDKKLKIVGDPLTSEYYGIAVRKGNKELLDKINKALKKIKENGT
YDKIYKKWF
>gnl|CDD|270343 cd13625, PBP2_AA_binding_like_1, Substrate-binding domain of putative amino acid-binding protein; the type 2 periplasmic-binding protein fold. This putative amino acid-binding protein belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
IKKRGTITVATEADYAPFEFVENGKIVGFDRDLLDEMAKKLGVKVEQQDLPWSGILPGLLAGKFDMVATS
VTITKERAKRFAFTLPIAEATAALLKRAGDDSIKTIEDLAGKVVGVQAGSAQLAQLKEFNETLKKKGGNG
FGEIKEYVSYPQAYADLANGRVDAVANSLTNLAYLIKQRPGVFALVGPVGGPTYFAWVIRKGDAELRKAI
NDALLALKKSGKLAALQQKW
>gnl|CDD|270344 cd13626, PBP2_Cystine_like, Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein fold. Cystine-binding domain of periplasmic receptor-dependent ATP-binding cassette (ABC) transporters. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Also, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
KLTVGTEGTYPPFTFKDEDGKLTGFDVEVGREIAKRLGLKVEFKATEWDGLLPGLNSGKFDVIANQVTIT
PEREEKYLFSDPYLVSGAQIIVKKDNTIIKSLEDLKGKVVGVSLGSNYEEVARDLANGAEVKAYGGANDA
LQDLANGRADATLNDRLAALYALKNSNLPLKIVGDIVSTAKVGFAFRKDNPELRKKVNKALAEMKADGTL
KKLSEKWFG
>gnl|CDD|270345 cd13627, PBP2_AA_binding_like_2, Substrate-binding domain of putative amino acid-binding protein; the type 2 periplasmic-binding protein fold. This putative amino acid-binding protein belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
VLRVGMEAAYAPFNWTQETASEYAIPIINGQGGYADGYDVQIAKKLAEKLDMKLVIKKIEWNGLIPALNS
GDIDLIIAGMSKTPEREKTIDFSDPYYISNIVMVVKKDSAYANATNLSDFKGATITGQLGTMYDDVIDQI
PDVVHTTPYDTFPTMVAALQAGTIDGFTVELPSAISALETNPDLVIIKFEQGKGFMQDKEDTNVAIGCRK
GNDKLKDKINEALKGISSEERDEMMDKAVDRQP
>gnl|CDD|270346 cd13628, PBP2_Ala, Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 periplasmic binding protein. This periplasmic substrate component serves as an initial receptor in the ABC transport of glutamine in eubacteria and archaea. After binding the alanine with high affinity, this domain Interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. This alanine specific domain belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLNMGTSPDYPPFEFKIGDRGKIVGFDIELAKTIAKKLGLKLQIQEYDFNGLIPALASGQADLALAGITP
TPERKKVVDFSEPYYEASDTIVSXKDRKIKQLQDLNGKSLGVQLGTIQEQLIKELSQPYPGLKTKLYNRV
NELVQALKSGRVDAAIVEDIVAETFAQKKNXLLESRYIPKEADGSAIAFPKGSPLRDDFNRWLKEMGDSG
ELELMVRRW
>gnl|CDD|270347 cd13629, PBP2_Dsm1740, Amino acid-binding domain of the type 2 periplasmic binding fold superfamily. This subfamily includes the periplasmic binding protein type II (BPBII). This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBPII proteins share the same architecture as periplasmic binding proteins type I (PBPI), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBPII proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction
VLRVGMEAGYPPFEMTDKKGELIGFDVDLAKALAKDLGVKVEFVNTAWDGLIPALQTGKFDLIISGMTIT
PERNLKVNFSNPYLVSGQTLLVNKKSAAGIKSLEDLNKPGVTIAVKLGTTGDQAARKLFPKATILVFDDE
AAAVLEVVNGKADAFIYDQPTPARFAKKNDPTLVALLEPFTYEPLGFAIRKGDPDLLNWLNNFLKQIKGD
GTLDELYDKWF
>gnl|CDD|270348 cd13630, PBP2_PDT_1, Catalytic domain of prephenate dehydratase and similar proteins, subgroup 1; the type 2 periplasmic binding protein fold. Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
PLKVAYLGPEGTFSHQAALKYFGSSVELVPCPTIEDVFRAVEKGEADYGVVPVENSTEGSVNETLDLLLE
SDLKICGEVVLPIHHCLLSRSGDLSDIKRVYSHPQALAQCRKWLRRNLPNAELIPVSSTAEAARLAAEDP
GAAAIASERAAELYGLPVLAENIEDRPDNTTRFLVIGREP
>gnl|CDD|270349 cd13631, PBP2_Ct-PDT_like, Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, subgroup 2; the type 2 periplasmic binding protein fold. Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
MKRVAYQGVPGAYSHLAARKYFGEDEEVPCCKTFEDVFEAVESGEADYGVLPIENSSAGSINEVYDLLLE
YDLYIVGEIFLPIEHCLLALPGAKLEDIKEVYSHPQALAQCSKFLKKHPGIKLVPYYDTAGAAKKVAEEG
DKTVAAIASELAAELYGLEILAENIQDNKNNYTRFLILSRKP
>gnl|CDD|270350 cd13632, PBP2_Aa-PDT_like, Catalytic domain of prephenate dehydratase from Arthrobacter aurescens and similar proteins, subgroup 3; the type 2 periplasmic binding protein fold. Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
MTRLAYLGPEGTFTEAALLQLAGADGAELVPCDSVPAALDAVRSGEADAAVVPIENSVEGGVTATLDALA
DGDPLVIVAEVLVPIAFDLAVRPGTTLADVRTVATHPHALAQCRGWLAENLPGAEFVPASSNAAAARDVA
EGEYDAALAPPIAAELYGLEVLADDVADNPGAVTRFVLVGRPG
>gnl|CDD|270351 cd13633, PBP2_Sa-PDT_like, Catalytic domain of prephenate dehydratase from Staphylococcus aureus and similar proteins, subgroup 4; the type 2 periplasmic binding protein fold. Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
MKKIGYLGPKGTFSEEAALALFGGEEAELVPYPTIPDVIEAVAEGEVDYGVVPIENSIEGSVNLTLDLLA
HEVDLPIQGEIILPIRQNLLVRPGVDLSDITKVYSHPQALAQCRQFLRRNLPGAELEYTGSTAEAARLVA
ESPEGWAAIGTLRAAELYGLEILAEDIQDYPNNFTRFVVLGKED
>gnl|CDD|270352 cd13634, PBP2_Sco4506, The conserved hypothetical protein SCO4506 exhibits the type 2 periplasmic-binidng protein fold. This group includes the SCO4506 protein from Streptomyces coelicolor and related hypothetical proteins. SCO4506 is an ortholog of Ttha1568 (MqnD) from Thermus thermophilies HB8. MqnD is an enzyme within an alternative menaquinone biosynthetic pathway that catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. SCO4506 has significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
MLRVGRISYLNTLPLFYGLEKGKVPPGFELVLGVPSELNRMLLEGELDVGLVSSIEYARNADDYLILPDL
SISSDGPVGSVLLFSKVPLEELEGKRVALTTESATSVALLKILLEEFYGLEPEYVPAPPDLDEMLADADA
ALLIGDDALRARASGRGPYVYDLGEEWKELTGLPFVFAVWAVRRDAAERPEELAELVQALLESKRYGLAN
LEEIIAEAAERLGLSEEFLRDYFTNLRYDLGEEELEGLELFYRYAA
>gnl|CDD|270353 cd13635, PBP2_Ttha1568_Mqnd, A menaquinone biosynthetic enzyme exhibits the type 2 periplasmic-binding protein fold. This group includes Ttha1568 (MqnD) from Thermus thermophilies HB8, an enzyme within an alternative menaquinone biosynthetic pathway that catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. Ttha1568 has significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLSLGISPCPNDTFIFGALLHGLIDTPGLTFDVFLADVETLNRLALEGRLDVTKLSFAALPHLLDDYALL
RSGGALGRGCGPLLVARKPDSIEDLRGKRIAIPGENTTAHLLLRLFYPDDFELVPMRFDEIMPAVLRGEV
DAGVIIHEGRFTYQDYGLHKLLDLGEWWEEETGLPIPLGGIVIRRDLGAALARAIEEAIRRSLEYARAHP
EAARPYIREHAQELDDEVIRQHIDLYVNEFSLDLGEEGRAAVATLLERAE
>gnl|CDD|270354 cd13636, PBP2_Af1704, The conserved hypothetical protein Af1704 exhibits the type 2 periplasmic-binding protein fold. This group includes the Af1704 protein from from Archaeoglobus fulgidus DSM 4304, which is an ortholog of Ttha1568 (MqnD) from Thermus thermophilies HB8. MqnD is an enzyme within an alternative menaquinone biosynthetic pathway that catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. Af1704 has significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
KLRVAHSPDPDDAFMFYALATGKIDTPGFEFEHVLEDIETLNREALEGELDVTAISAHAYAYVADKYALL
SSGASMGDGYGPMVVAKEELTPEELKGKRIAVPGTLTTAYLLLRLYLPKFEVVVVPFDEIPDAVLSGEVD
AGLIIHEGQLTYEREGLKKVVDLGEWWKERTGLPLPLGGNVIRKDLGEEVIREIARLLRESIQYALAHRE
EALEYAMQFARGLDRELADRFVGMYVNDYTLDYGEEGREAVRLLLEMAY
>gnl|CDD|270355 cd13637, PBP2_Ca3427_like, The conserved hypothetical protein Ca3427 exhibits the type 2 periplasmic-binding protein fold. This group includes the Ca3427 protein from candida albicans, which is an ortholog of Ttha1568 (MqnD) from Thermus thermophilies HB8, and other related hypothetical proteins. MqnD is an enzyme within an alternative menaquinone biosynthetic pathway that catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. Ca3427 has significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLRIGGVPEHFNTPWHLAIEEGFFAEHGINVEWVDFPGGTGAMIKALRNGEIDIAIGLTEGFVADIAKGG
NPYKIVGTYVASPLNWAIHTGANSDYNSIEDLKGTKIGISRIGSGSHLMAYVLALQQGWDTEDLKFEVLN
NFDGLRDAVNDGKADAFMWEHFTTKPYVDSGEFKRIGEIPTPWPSFVIAASDELLEENPEALKAFLDALN
QGIAYFKAHPEEAVEYIAKRYDYKEEDAREWLKTVKWASQRQVSEKVLENTLDVLKEAGVLKE
>gnl|CDD|270356 cd13638, PBP2_EcProx_like, Substrate binding domain of Escherichia coli betaine transport system-like; the type 2 periplasmic binding protein fold. This group includes the periplasmic substrate-binding protein ProX. ProX from the Escherichia coli ATP-binding cassette transport system ProU binds the compatible solutes glycine betaine and proline betaine with high affinity and specificity. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. The ProX belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
PGKGVTVRPAKSTWAEEYFQTEIVSKGLEKLGYKVKEPKELDYPLFYVAVANGDADFWADHWFPLHDPFF
EKAGGDAKLVRVGVIIGGGLQGYLIDKKTADAYNITSLDQLKDPKIAKLFDSDGDGKADLTGCNPGWGCE
KVIEHQLDAYGLRDTVNHNQGSYSALMADAIARYKQGKPVLYYTWTPNWVSNVLVPGKDVVWLEVPFTAL
PGDQAGATTGVANGKNLGFPVNDIRIVANKAFLEANPAAKKLFELVQIPLADISAQNLLMNQGEGSPEDI
RRHADEWIAANQDTFDGWI
>gnl|CDD|270357 cd13639, PBP2_OpuAC_like, Substrate binding domain of Lactococcus lactis ABC-type transporter OpuA and related proteins; the type 2 periplasmic binding protein fold. This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to betaine compounds for osmoregulation. The periplasmic substrate-binding domain, which is often fused to the permease component of the ATP-binding cassette transporter complex, is involved in uptake of osmoprotectants (also termed compatible solutes) such as glycine betaine and proline betaine. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. This domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TITIGYVNWDEAIAVTNLAKAVLEEKGYDVELTQADAGPMYQGVASGDIDAFLDAWLPVTHKDYWDKYGD
DLEDLGPWYEGAKLGLAVPSYVDIDSIEELLDHADKFGGKIVGIEPGAGLMKLTEEAIEEYGLLDYELVT
SSTAAMLAELDRAIDNKEPIVVTGWSPHWMFAKYDLKYLEDPKGVYGEAESIHTIARKGFEEDHPEAYEF
LKNFKLTDEDLESLMLEIEDGGDPEEAAEEWIDENPDLVDEWLE
>gnl|CDD|270358 cd13640, PBP2_ChoX, Substrate binding domain of ABC-type choline transport system; the type 2 periplasmic binding protein fold. This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to choline and acetylcholine for osmoregulation. The periplasmic substrate-binding domain, which is often fused to the permease component of the ATP-binding cassette transporter complex, is involved in uptake of osmoprotectants (also termed compatible solutes) such as choline and betaines. Choline is necessary for the biosynthesis of glycine betaine. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. In the case of the Sinorhizobium meliloti choline uptake system ChoVWX, ChoV is the nucleotide-binding domain that provides energy for the transport process via ATP hydrolysis, ChoW is the integral transmembrane protein that forms the substrate translaocation pathway, and ChoX is the substrate-binding domain. ChoX belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TVRFGDVGWTDITVTTAVASQILEALGYETEVKELSVPIIYQGLANGDIDVFLGNWMPSQEPMIDPYLEK
GSIEVVGTNLEGAKYTLAVPTYVYEAGVKSFADLAKFADKFDGKIYGIEPGNDGNEIIQKMIDNNTYGLG
DWKLVESSEQGMLAQVERAIRNKEWIVFLGWEPHPMNVEFDIKYLDGGDDYFGPNYGAATVYTVTRKGYA
EDCPNVAKLLSNLKFSVDMENQWMYEILNKGRDPEDAAREWIKANPDVVDAWLDGV
>gnl|CDD|270359 cd13641, PBP2_HisX_like, Substrate-binding domain of ABC-type histidine transporter involves in betaine and proline uptake; the type 2 periplasmic-binding protein fold. This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to certain quaternary ammonium compounds for osmoregulation. The periplasmic substrate-binding domain, which is often fused to the permease component of the ATP-binding cassette transporter complex, is involved in uptake of osmoprotectants (also termed compatible solutes) such as glycine betaine, proline betaine, choline, and carnitine. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. This domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
PVTFADMNWDSAQFHNRIAGFILEHGYGCQVEVVPGSTPPTLTALARGDIDVAMELWTDNISEAYNKAVE
EGKVLDLGTNFDDARQGWYVPTYVIEGRFYNCPTGWGCEIINTNKLKAYGLDEGYTNFRPGSGAALDAAI
ASAYERGEPWVGYYWEPTWLMGKYDMTLLEEPPYDEECWNCLCADCANPGACAFPSSTVTIAVNTDFAEK
APEIVEFLEKYETSLELTNEALAYMAENKASAEEAAKWFLKNHPDVWTQWV
>gnl|CDD|270360 cd13642, PBP2_BCP_1, Substrate-binding domain of osmoregulatory ABC-type glycine betaine/choline/L-proline transport system-like; the type 2 periplasmic-binding protein fold. This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to certain quaternary ammonium compounds for osmoregulation. The periplasmic substrate-binding domain, which is often fused to the permease component of the ATP-binding cassette transporter complex, is involved in uptake of osmoprotectants (also termed compatible solutes) such as glycine betaine, proline betaine, choline, and carnitine. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. This domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
DVVIGDPNWTGAQAIAHILKAVIEDRLGGEAELQEGNNPIIFAAMDKGDGSIDVHPDVWLPNQQALWDKY
VTGGGTVALNPNPYEGTQGICVPAATADKYGIKSDLDLTAPEAALFDSDGDGKGEIWIGAPGWASTNIEQ
IKAKSYGYDETWELEEMSEAVFYAQLDAAYARGEPIVFYCYTPHWVFALYDLVQLEEPAYDAAKWTTVLP
TEDPDWLEKSNAACAWADASVHIAYSASLEERAPEVAAFLSRIRLTPEEVNAMSYAVDVDGKDPAAVARE
WVAANADRVDEW
>gnl|CDD|270361 cd13643, PBP2_BCP_2, Substrate-binding domain of osmoregulatory ABC-type glycine betaine/choline/L-proline transport system-like; the type 2 periplasmic-binding protein fold. This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to certain quaternary ammonium compounds for osmoregulation. The periplasmic substrate-binding domain, which is often fused to the permease component of the ATP-binding cassette transporter complex, is involved in uptake of osmoprotectants (also termed compatible solutes) such as glycine betaine, proline betaine, choline, and carnitine. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. This domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
PIKLALNDWTGQQVSAHVAGYLLEKEGYKVEYVTADEQAQWEALAAGDVDAQLEVWESSMGDKYEKALAA
GSVVDLGDLGLIGREGWWYPKYVEELCPGLPDWKALNKCAALFATPETGPKGRLLGGPPDWGTNDAARIA
ALGLPFTVVPAGSEAALWAELRAAYARKKPLLIYFWTPHWAFAKYKGVFVELPPYEEACETDPAWGNNPP
AKGDCGYPPGYLKKAAWAGFADKWPAAYELLKNFTLTNEDQAAMAALIDVDGMSVEDAAKKWLAANEATW
KPW
>gnl|CDD|270362 cd13644, PBP2_HemC_archaea, Archaeal HemC of hydroxymethylbilane synthase family; the type 2 periplasmic binding protein fold. Hydroxymethylbilane synthase (HMBS), also known as porphobilinogen deaminase (PBGD), is an intermediate enzyme in the biosynthetic pathway of tetrapyrrolic ring systems, such as heme, chlorophyll, and vitamin B12. HMBS catalyzes the conversion of porphobilinogen (PBG) into hydroxymethylbilane (HMB). This subfamily includes the three domains of HMBS. The enzyme is believed to bind substrate through a hinge-bending motion of domains 1 and 2. The C-terminal domain 3 contains an invariant cysteine that forms the covalent attachment site for the DPM (dipyrromethane) cofactor. HMBS is found in all organisms except viruses. The domains 1 and 2 have the same overall topology as found in the type 2 periplasmic-binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor
KIRVATRGSRLALAQTEEVIEELKERGPVEVEIKIIKTKGDRDSDRPLYSIGGKGVFVKELDRAVLEGEA
DIAVHSLKDVPSEIDPGLVIAAVPKRESPNDVLVSRDGSTLEELPPGAVVGTSSLRRRAQILRLRPDLRV
EPLRGNVDTRIRKLREGEYDAIVLAEAGLKRLGLDVKYSPLSPEDFVPAPGQGILAVVARADDEKVIALL
KKIEDPDSRVEAEAERALLEELGGGCRTPVGVYARATGGMVRLTAEAFSVDGSRFVVVKASGD
>gnl|CDD|270363 cd13645, PBP2_HuPBGD_like, Human porphobilinogen deaminase possess type 2 periplasmic binding protein fold. Hydroxymethylbilane synthase (HMBS), also known as porphobilinogen deaminase (PBGD), is an intermediate enzyme in the biosynthetic pathway of tetrapyrrolic ring systems, such as heme, chlorophyll, and vitamin B12. HMBS catalyzes the conversion of porphobilinogen (PBG) into hydroxymethylbilane (HMB). This subfamily includes the three domains of human PBGD and its closely related proteins. Mutations in human PBGD cause AIP (acute intermittent porphyria), an inherited autosomal dominant disorder. The enzyme is believed to bind substrate through a hinge-bending motion of domains 1 and 2. The C-terminal domain 3 contains an invariant cysteine that forms the covalent attachment site for the DPM (dipyrromethane) cofactor. HMBS is found in all organisms except viruses. The domains 1 and 2 have the same overall topology as found in the type 2 periplasmic-binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor
VIRIGTRKSQLALIQTEYVREELKKLYPDLTFEIITMSTTGDKILDVALSKIGGKGLFTKELEAALLEGE
VDLAVHSLKDLPTVLPPGFELGAILKREDPRDALVFHPGLNYKSLDDLPEGSVIGTSSLRRAAQLKRKYP
HLRFKDIRGNLNTRLAKLDAPESPYDAIILAAAGLERLGLEDRISQDLSPETMLYAVGQGALAVECRAGD
QKILELLKVLDDPETTLRCLAERAFLRHLEGGCSVPIAVHSALKEGGELYLTGIVLSLDGSTSIEDTAKG
PV
>gnl|CDD|270364 cd13646, PBP2_EcHMBS_like, cd00494. Hydroxymethylbilane synthase (HMBS), also known as porphobilinogen deaminase (PBGD), is an intermediate enzyme in the biosynthetic pathway of tetrapyrrolic ring systems, such as heme, chlorophyll, and vitamin B12. HMBS catalyzes the conversion of porphobilinogen (PBG) into hydroxymethylbilane (HMB). This subfamily includes the three domains of Escherichia coli HMBS and its closely related proteins. The enzyme is believed to bind substrate through a hinge-bending motion of domains 1 and 2. The C-terminal domain 3 contains an invariant cysteine that forms the covalent attachment site for the DPM (dipyrromethane) cofactor. HMBS is found in all organisms except viruses. The domains 1 and 2 have the same overall topology as found in the type 2 periplasmic-binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor
TLRIGTRGSKLALWQANHVKDRLKAEHPGLEVELVEITTKGDKILDVPLSKIGGKGLFVKEIEEALLAGR
IDLAVHSLKDVPTVLPEGLTLAAIPKREDPRDALVSRKGKTLEELPEGARVGTSSLRRQAQLLALRPDLE
IKDLRGNVDTRLRKLEEGEYDAIILAAAGLKRLGLESRIREELSPDEMLPAVGQGALGIECRADDEELLE
LLAPLNDEETALCVTAERAFLARLEGGCQVPIGAYAVLEGGELKLRALVGSPDGSRVIRGERTG
>gnl|CDD|270365 cd13647, PBP2_PBGD_2, An uncharacterized subgroup of the PBGD family; the type 2 periplasmic binding protein fold. Hydroxymethylbilane synthase (HMBS), also known as porphobilinogen deaminase (PBGD), is an intermediate enzyme in the biosynthetic pathway of tetrapyrrolic ring systems, such as heme, chlorophyll, and vitamin B12. HMBS catalyzes the conversion of porphobilinogen (PBG) into hydroxymethylbilane (HMB). This subfamily includes the three domains of HMBS. The enzyme is believed to bind substrate through a hinge-bending motion of domains 1 and 2. The C-terminal domain 3 contains an invariant cysteine that forms the covalent attachment site for the DPM (dipyrromethane) cofactor. HMBS is found in all organisms except viruses. The domains 1 and 2 have the same overall topology as found in the type 2 periplasmic-binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor
EIRIGTRKSKLALIQANKVIEALKKKFPEIEVEIKPIKTTGDKILDKPLWKIGGKGLFTKELEKALLNGE
IDIAVHSLKDVPAELPDGLEIVAVLKREDPRDVLVSKKNKSIFNLPSGAKIGTSSLRRKAQLKKFRPDLK
IKPIRGNVDTRLRKLKEGEYDGIILAAAGLKRLGLEDDEINYQILDLVMLPAPGQGAIAVECRKKDQELF
SLLKQINHEETFNAVEAEREFLKELDGGCHTPIGAYAEVKGSIIYLKGLYDTKDFIQKKIDEILKAKELG
SK
>gnl|CDD|270366 cd13648, PBP2_PBGD_1, An uncharacterized subgroup of the PBGD family; the type 2 periplasmic binding protein fold. Hydroxymethylbilane synthase (HMBS), also known as porphobilinogen deaminase (PBGD), is an intermediate enzyme in the biosynthetic pathway of tetrapyrrolic ring systems, such as heme, chlorophyll, and vitamin B12. HMBS catalyzes the conversion of porphobilinogen (PBG) into hydroxymethylbilane (HMB). This subfamily includes the three domains of HMBS. The enzyme is believed to bind substrate through a hinge-bending motion of domains 1 and 2. The C-terminal domain 3 contains an invariant cysteine that forms the covalent attachment site for the DPM (dipyrromethane) cofactor. HMBS is found in all organisms except viruses. The domains 1 and 2 have the same overall topology as found in the type 2 periplasmic-binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor
PIRIGTRGSPLALAQAYETRDKLKEAHPELAEEGAIEIVIIKTTGDKILSQPLADIGGKGLFTKEIDDAL
LNGEIDIAVHSMKDVPTYLPEGTILPCNLPREDVRDAFISPTAASLAELPAGSVVGTASLRRQAQILAKY
PDLKCVNFRGNVQTRLRKLKEGVVDATLLALAGLKRLDMTEHVTSILSLDEMLPAVAQGAIGIACRSDDD
KMAKYLAALNHEETRLAVSCERAFLATLDGSCRTPIAGYARRDDGKLHFRGLIASPDGKKVLETSRVG
>gnl|CDD|270367 cd13649, PBP2_Cae31940, Substrate binding domain of an uncharacterized protein similar to ABC-type transporter for thiamin biosynthetic pathway intermediates; a member of the type 2 periplasmic binding fold superfamily. This subfamily includes the periplamic-binding protein Cae31940 which is phylogenetically similar to the ThiY/THI5 family. ThiY is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are THI5, which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes, and periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport. After binding the ligand, They interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ThiY/THI5 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
EVMFGVGGKPLFYYLPLTIAERKGFFKDEGLDVTINDFGGGSKALQALVGGSVDVVTGAYEHTIRMQARG
QDIKAFCELGRFPGICIGVRKDLAGDIKTIADLKGQNVGVTAPGSSTSLLLNYALIKNGLKPDDVSIIGV
GGGASAVAAIKKGQIDAISNLDPVITRLEVDGDITLLLDTRTEKGTRELFGGTNPAATLYVQQAFIDANP
VTAQRLVNAFVRS
>gnl|CDD|270368 cd13650, PBP2_THI5, Substrate binding domain of ABC-type transporters for thiamin biosynthetic pathway intermediates; a member of the type 2 periplasmic binding fold superfamily. ThiY is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport, as well as THI5 which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes. After binding the ligand, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ThiY/THI5 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
KITFLLNWHATPYHIPIFLAQTKGYFKEEGLDVAILEPTNPSDVTELIGSGKVDMGLKAMIHTLAAKARG
FPVTSIGSLLDEPFTGVIYLKGSGITEDFQSLKGKRIGYVGEFGKIQIDELTKHYGMTPDDYTAVRCGMN
VAKAIIEGTIDAGIGIECMQQVELEEWLAKQGRPASDVKMLRIDKLAELGCCCFCTILYIANDEFLAKNP
EKVKKFLRAIKRATDYMLADPVKAWAEYIDFKPQMNTDLNR
>gnl|CDD|270369 cd13651, PBP2_ThiY, Substrate binding domain of ABC-type transporters for thiamin biosynthetic pathway intermediates; a member of the type 2 periplasmic binding fold superfamily. ThiY is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport, as well as THI5 which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes. After binding the ligand, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ThiY/THI5 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
KVTVLLDWYPNPDHAFLYVAQEKGYFREAGLDVEIVAPADPSDPLKLVAAGKADLAVSYQPQVILARSEG
LPVVSVGALVRSPLNSLMVLKDSGIKSPADLKGKKVGYSVLGFEEALLDTMLKAAGGDPSDVELVNVGFD
LSPALTSGQVDAVIGAYRNHELNQLAKEGLEGKAFFPEEYGVPNYDELVLVANKDKLPENGEKLRRFLRA
AEKG
>gnl|CDD|270370 cd13652, PBP2_ThiY_THI5_like_1, Putative substrate binding domain of an ABC-type transporter similar to ThiY/THI5; the type 2 periplasmic binding protein fold. This subfamily is phylogenetically similar to ThiY, which is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are THI5, which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes, and periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport. After binding the ligand, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ThiY/THI5 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TGKVKFGQIPISDFAPVYIAAEKGYFKEEGLDVEITRFASGAEILAALASGQVDVAGSSPGASLLGALAR
GADLKIVAEGLGTTPGYGPFAIVVRADSGITSPADLVGKKIAVSTLTNILEYTTNAYLKKNGLDPDKVEF
VEVAFPQMVPALENGNVDAAVLAEPFLSRARSSGAKVVASDYADPDPHSQATMVFSADFARENPEVVKKF
LRAYLEA
>gnl|CDD|270371 cd13653, PBP2_phosphate_like_1, Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily. This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
SGTITISGSTTVAPLAEALAEAFMEKHPGVRIEVQGGGSGTGIKALIEGTADIGMASRPLKAEEKAAASG
LVEHVIALDGIAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREEGSGTRETFEELVL
GKKDFAKNAVVVPSNGAVVQAVAKNPNAIGYVSLGYVDDSKVKALSVDGVAPTPENIKSGKYPLSRPLYL
YTKGEPSGLVKAFIDFALSPEGQAIVEKLG
>gnl|CDD|270372 cd13654, PBP2_phosphate_like_2, Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily. This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
RGQIRIDGSSTVYPITEAVAEEFGKSGPGVTVTVGSSGTGGGFKKFCAGETDISNASRPIKDSEAELCEA
NGIEYIELPVAYDGLTVVVNPANDWAKCLTELELKSIWAAESPITTWSDVRPSWPDEPIELYGPGTDSGT
FDYFTEAIVGEGGSIREDYTASEDDNVLVQGVAGDKNALGFFGYAYYEENGDKLKAVKIDGGEGTVAPSA
ETTISGGYYPLSRPLFIYVKKASLAEKPAVAAFVKFYLENAQEAAGEVG
>gnl|CDD|270373 cd13655, PBP2_oligosaccharide_1, The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold. This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLTVWGPQEDQEWLKEMVDAFKEKHPEWKITITIGVVGEADAKDEVLKDPSAAADVFAFANDQLGELVDA
GAIYPLTGSAVDKIKNTNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTEDDVKSLDTMLAKAPDAK
GKVSFDLSNSWYLYAFFFGAGCKLFGNNGGDTAGCDFNNEKGVAVTNYLVDLVANPKFVNDADGDAISGL
KDGTLGAGVSGPWDAANLKKALGDNYAVAKLPTYTLGGKDVQMKSFAGYKAIGVNSNTKNPEAAMALADY
LTNEESQLTRFEKRGIGPTNKEAAESDAVKADPAAKALIAQSNEASVVQPKLPKMSNFWTPAEAFGKGIV
DGTVTAENAQQKL
>gnl|CDD|270374 cd13656, PBP2_MBP, The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold. This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSG
LLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGK
SALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAE
AAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYL
LTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGR
QTVDEALKDAQTRI
>gnl|CDD|270375 cd13657, PBP2_Maltodextrin, The periplasmic binding component of ABC transport system specific for maltodextrin. This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TITIWHALTGAEEDALQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFA
EAGLLVPISDYLSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDH
TDPAAGSYGLAYQVSDAYFVSAWIFGFGGYYFDDETDKPGLDTPETIKGIQFLKDFSWPYMPSDPSYNTQ
TSLFNEGKAAMIINGPWFIGGIKAAGIDLGVAPLPTVDGTNPPRPYSGVEGIYVTKYAERKNKEAALDFA
KFFTTAEASKILADENGYVPAATNAYDDAEVAADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAV
YQGGQDPQEALAAAQQEI
>gnl|CDD|270376 cd13658, PBP2_CMBP, The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold. This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
QLTVWVDEDKKMAFIKKIAKQYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQ
GLLSPIKLSKDKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKDLTKEK
GKQYGFLADATNFYYSYGLLAGNGGYIFKKNGSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGD
VIQGLFKEGKAAAVIDGPWAIQEYQEAGVNYGVAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFM
EFLTSKENLKKRYDETNEIPPRKDVRSDPEIKNNPLTSAFAKQASRAVPMPNIPEMGAVWEPANNALFFI
LSGKKTPKQALNDAVNDIKENI
>gnl|CDD|270377 cd13659, PBP2_PotF, The periplasmic substrate-binding component of an ABC putrescine transport system and related proteins; contains the type 2 periplasmic-binding fold. This group represents the periplasmic substrate-binding domain that serves as the primary polyamine receptor of ABC-type putrescine-preferential transporter from gram-negative bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLNVYNWSDYIAPDTLEDFEKETGIKVVYDTYDSNEELEAKLLAGGSGYDLVVPSANFLGRQIKAGALQK
LDKSKLPNWKNLDPLLLKLLAAVDPGNRYAVPYMWGTTGIAYNVDKVKAALGDDLPDSWDLVFDPENLSK
LKSCGVSVLDSPEEVFPAALNYLGLDPNSTDPEDIKAAEDLLKKVRPYVRYFHSSKYINDLANGEICVAI
GWSGDAVQAAQRAKEAGNGVTLEYVIPKEGANLWFDMFAIPADAKNPDNAYRFINYLMRPEVIAKISNYV
NYANANKAATPLVDEAIKDDPAIYPPEEVLKKLYALPPLSAKVQRALTRAW
>gnl|CDD|270378 cd13660, PBP2_PotD, The periplasmic substrate-binding component of an active spermidine-preferential transport system; contains the type 2 periplasmic binding fold. This group represents the periplasmic binding domain that serves as the primary polyamine receptor of ABC-type spermindine-preferential transport system from gram-negative bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLNFYNWSEYVPPELLEQFTKETGIKVILSTYESNETMYAKVKLYKDGAYDLVVPSTYYVDKMRKEGLIQ
KIDKSKITNFSNIDPDFLNQPFDPNNDYSIPYIWGATALAVNGDAVDGKSVTSWADLWKPEYKGKLLLTD
DAREVFQMALRKLGYSGNTKDPEEIEAAFEELKKLMPNVAAFDSDNPANPYMEGEVALGMIWNGSAFVAR
QANKPIHVVWPKEGGIFWMDSFAIPANAKNKEGALKFINFLLRPDVSKQIAETIGYPTPNLKARKLLSPE
VANNKIVYPSAETIKNGEFQNDVGAASLIYEEYYQ
>gnl|CDD|270379 cd13661, PBP2_PotD_PotF_like_1, The periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold. This group represents the periplasmic binding domain that serves as a primary polyamine receptor of an uncharacterized ABC-type transport system from plants and plant-symbiotic cyanobacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
PLQIVALRGSIPPQWLNEFQQSQGKRVKLSLEFRGQLADLFKELQDWSKNGKATSKSAPAADLVTLGDSW
LGRAIARGQIWAVPYRWGTTVIAYRKDKLKKLGWDPIDWSDLWRPELAGRIAMVDSPREVIGLVLKKLGA
SYNTAEVPGGREALEERLAALRRQVKLYSSNNYLQALLLGDVWVAVGWSQDIIPLARRYSNLAVVIPRSG
TSLWADLWVIPAGSDFGGRVRGPSPLLSQWIDFCLQPARATQFAQLSFGGASPLILDGPSLTPPEATRKL
KLDTNLVLGLPPDEILAKSEFLLPLSEATLAQYRALWQT
>gnl|CDD|270380 cd13662, PBP2_TpPotD_like, The periplasmic substrate-binding component of an ABC-type polyamine transport system from Treponema pallidum and related proteins; contains the type 2 periplasmic binding fold. This group includes the polyamine-binding component of an ABC-type polyamine transport system from Treponema pallidum and closely related proteins, which is homologous to the spermidine-preferring periplasmic substrate-binding protein component (PotD)of ABC transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
VLYIYNWTYYIPDKVIEDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEK
LDKSKLPNVKEEKDNLMEASKIYDPGLEYSVPYMFGATGIAVNKKIVKNYFRKWSIFLREDLAGRMTMLD
DMREVIGAALAYLGYPVDSKDIEQLEEAKEVILSWKKNLAKFDSNSYGKGFASGDFWVVHGYAEDVFYEV
PEEEEEKFDFFIPEGAASMMYIDSFVIPKGSKHKDNAYKFINFILRPENYAEILDVLGNPSIIKEAEKKS
QKKPIIYAEEDLKNSKLPGDVGDALELQNKIW
>gnl|CDD|270381 cd13663, PBP2_PotD_PotF_like_2, The periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold. This group represents the periplasmic substrate-binding domain that serves as a primary polyamine receptor of an uncharacterized ABC-type transport system from gram-negative bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLKVYNWGEYIDPDLIDDFEKETGIKVNYETFDSNEEMYTKIKTGGTSYDVIVPSDYMIEKLIKEDLLQP
LDYSKLPNVDKNINIQPDLLNLAFDPINEYSVPYFWGTLGIVYNKTKVSLEELSWWNILWNKKYKGKILM
YDSPRDAFMVALKALGYSLNTTNPDEIEEAKDWLIKQKPNVKAFVVDEIKDLMINGNADIAVTYSGDAAY
AMEENENLDYVIPKEGSNLWFDNWVIPKNAKNVDLAYKFINFLLRPDNALKNAEYVGYSTPNAAAEELLP
EEESIKDDKIFYPDEDIYKKCEVFKYLGGDAKKEYNDLWLEVK
>gnl|CDD|270382 cd13664, PBP2_PotD_PotF_like_3, TThe periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
ELNLYNWTDYTSPELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEP
LDKSQLTNYDNIDPRWRKPDFDPGNEYSIPWQWGTTGFAVDTAVYDGDIDDYSVIFQPPEELKGKIAMVD
SMNEVVNAAIYYLGGPICTTDPKLMRKVRDLLLEQKPHVKAYDSDGIVERMASGDVAAHVDWNGASLRAR
RQNPSLAYAYPKEGVLIWSDNLVIPKGAPNYENARTFLNFIMEPENAALQSNFAGYANAITGAEKFMDDP
LKDAPALEIPPPEGSRLKFSTLCPPKAEKLQSRIW
>gnl|CDD|270383 cd13665, PBP2_TRAP_Dctp3_4, Periplasmic substrate-binding component of TRAP-type C4-dicarboxylate transport system DctP3 and DctP4; the type 2 periplasmic-binding protein fold. This group includes uncharacterized DctP3 and DctP 4 subfamilies of TRAP Transporters specific to C4-dicarboxylates such as succinate, malate and fumarate. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. This CD also included some eukaryotic homologs that have not been functionally characterized. TRAP transporters are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLRFSHFLPPTHPIVTGVLEPWAEEVEEASGGRVTVEIYPGGTLGKPPQQYDLVRDGVADIGWTVPGYTP
GRFPLTEVVELPFLAPSAEAGSVALWEYEYEGALADEFKDVKVLALFTHGPGQLHTKKPVVRSLEDLKGL
KIRVPGGTAADILEALGATPVGMPAPDVYEALSKGVIDGALLPWEALKSFKLAEVTKYHTEPGGLYTTSF
AVVMNKDKYDSLPDDLQAVIDEVSGEELSRLAGKAWDDADAAGREAARAAGVTIIELSDAEIARWDEALA
PVIDAWVAEVEAKGLDGQAALD
>gnl|CDD|270384 cd13666, PBP2_TRAP_DctP_like_1, Substrate-binding component of an uncharacterized TRAP-type C4-dicarboxylate transport system; the type 2 periplasmic-binding protein fold. This group includes a DctP subfamily of TRAP Transporters specific to C4-dicarboxylates such as succinate, malate and fumarate. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. This CD also included some eukaryotic homologs that have not been functionally characterized. TRAP transporters are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLRYASGLPPVNSAVSAAYEAFAEEVEERTGGELTFEIFWGGALLKAGETLQGVRDGVADIGQVVPLYFP
AELPLQNVLYELPFAGSDPLAAAAAVTELYLTCPECQAEFERNNQVYLGGYATDPYVLLCTKPVESLEDL
KGKKIRAAGAWARWLEALGAVPVNMPLTEVYEALQRGVLDCTIGSASALLAFKLYEVAPYVTLPGGGAVA
GAALVMNKDTWNSLPEEVREALLEAAAEALAAYAEAYEADDEAALEEAEAAGVEIVEPSAELRAALAAFL
PDDAAAWAEEAEAGGEDAQAVVD
>gnl|CDD|270385 cd13667, PBP2_TRAP_DctP1, Periplasmic substrate-binding component of an uncharacterized TRAP-type C4-dicarboxylate transport system DctP1; contains the type 2 periplasmic-binding protein fold. This group includes an uncharacterized DctP1 subfamily of the TRAP Transporters. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLRAVSAFPETLIYTQFFLFVVDVVNEGGGGVVQINVVGGPEAIPPFEQGNAVRNGVVDIAYSPGSFYAG
LVPEADALKLSNVTAAELRANGGFDLMNQIHQEKMNVKYLARVDSGVPYHIYTNKEPSDKLDLTGKKLRS
SPVYRAFFEALGAQPVSTPPGEVYTALERGVVDGYGWPIIGIFDLGWQEFTKYRVEPGFYQTDVSVIMNL
DKWNSLSPEAQAILQDAAIEAEGQSAGWAKAKREAEFAKQAEAGIETVSLEGEAAEKFLGRAYDAGWARM
MEQAPETAAKLKPLF
>gnl|CDD|270386 cd13668, PBP2_TRAP_UehA_TeaA, Periplasmic substrate-binding component of osmoregulatory TRAP transporters TeaA and UehA; the type 2 periplasmic-binding protein fold. This subfamily includes the periplasmic-binding component of the ectoine-specific TRAP transporters TeaA from Halomonas elongata and UehA from Ruegeria pomeroyi. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TWRFALEEIEGDVQDVYAQEFKEEIEEKSDGDVTVDIYPYGTLGDSEDIVEQTQNGAIQFVFTSPGFLGS
LVPEAQVFSLPYLLPDDPEVNAKVLNESKAINEMLAKAYEKQGLKLLAMFPEGWMVWTANKPIRTPADFD
GFKIRTMTSPLLVETYKAYGADPTPLPYGEVYGGLQLGMIDGQENPIFAIEEMKFYEVQDYLTLAGHAPF
VATVVANKDFYDSLPEEDQKMVREAADEAIDWAFEMQQELNDERLEKIKESSPDIEVIELTEEEREAFKE
RAKPVRDKYIEMTGESGKEILDQLL
>gnl|CDD|270387 cd13669, PBP2_TRAP_TM0322_like, Periplasmic component of TRAP-type C4-dicarboxylate transport system TM0322 from Thermotoga maritima and similar proteins; the type 2 periplasmic binding protein fold. This subgroup includes the hyperthermophilic bacterium Thermotoga maritima TRAP-type C4-dicarboxylate transport system TM0322 and its closely related proteins. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
VLKVSHVLTPGEPLDKGMLKWAENVEERTNGRIKIEVFPSSQLGSEKDVIEQARAGANVITVTDGARLGD
YVPDIGILNGPYLFDSYDELLKLTESPLFKEWEKELEKKGIKILSFNWIYGFRHLLTNKPVKTPADLKGL
KIRVPGNPIWIETIEALGATPTPMPWSEVYTALQQGVIDGAENPLPTLYGGKLYEVAKYISLTGHILLIS
GLVVSAKWFDSLPEEYQKILVEEADKAGEYASELTLEEEEEYLKKLKEEGVTVIEVDLEAFKKAAEPVYE
KLGLWEWSPGLYDEIK
>gnl|CDD|270388 cd13670, PBP2_TRAP_Tp0957_like, Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold. This subfamily includes the putative periplasmic substrate-binding protein Tp0957 from Treponema pallidum, which is similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLKIATLAPKGSPWVQELKKLAPEIEEATGGRVKLKIYPGGVMGDDEDVLRKMRIGQLQGAGLSGGGLSE
ICPEMAVLSLPFLFRSYDEVDYVREKMRPVFDELFEKKGFVLLAWSDQGFDYIFSKKPVATLEDLKKQKI
WTWEGGPVEEEALKALGASPVPLPLPEVLTSLQTGLIDAVIAPPLWALALQWYTKVKYVNDLPIRYSPGA
IVISKKAWNKLPAEYQEAVREARAKAFKRLNAKVREDNEKALAAMKKYGLKVVKLSPEELEEWRKAARPV
WEELAGKLYSRELLDEIL
>gnl|CDD|270389 cd13671, PBP2_TRAP_SBP_like_3, Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold. This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
VLKLADNQPEDHPTVIALKAFAELVKERTNGRITIEVYPNGQLGDEKETIEQVQNGAIDMARVSASPLEN
FVPEFGVFSLPYLFRSVEHMYKVLDGEVGDELLDSLEDSGFVGLGWYDAGARSFYTTKPPINTPADLKGL
KIRVQESDVMIDMVEALGASPTPMPYGEVYTALQTGVIDGAENNEPSYYSSKHYEVAKYFSLTEHLRIPD
VLVMSKATWDSLSPEDQEIIKEAAKESAEYQRELWAESEEEARAKAEEAGVEINEVDKAPFQEAVKPLYD
EYLKNPEYKDLIERIQ
>gnl|CDD|270390 cd13672, PBP2_TRAP_Siap, Substrate-binding domain of a sialic acid binding Tripartite ATP-independent Periplasmic transport system (SiaP); the type 2 periplasmic-binding protein fold. This subfamily represents the periplasmic-binding component of TRAP transport system SiaP, a sialic acid binding virulence factor. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLKFGHVAATSSPEYKAAEAFAEEVEEKSGGKITVQVYPSSQLGSERDMLEQLSSGSLDMTYAGSGFFGK
FYPPASVFEAPYLFRDYDHMQKVLNSDLGAELFDKLDEKLGVRILGSAYYGTRQVTSNKPINTPADMKGL
KLRVPNAPSYLALAKALGANPTPMAFSEVYLALQQGAVDGQENPLPTIKAAKFYEVQKYLALTGHIVDDQ
LIVVSEDTWQKLTEEQQAIVTDAAEEAAEYANKLVIDEEAELVEFFKEQGVTVTEPDLEAFREAAAPYYL
EFLAEWGEGLYKRIQ
>gnl|CDD|270391 cd13673, PBP2_TRAP_SBP_like_2, Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold. This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLKLAHVRPTGSPGDKALKKFAEEIEEATGGRVKVRVYPANQLGDYTEVFELVSRGDVDMALQSPSSQYD
KRLDITYLPYLVSNWDEAKKVYGPGGPLNDILDELLADLGLKLLGAYPEGFGGIALNKKVEKPNNPDVAK
GLKIRVPPMKVFKLLAEALGYNTTPIPWSEVFTALQTGVVDGVIGGGAEGAYESFRDVLKYYIPTNDHFE
TWFLIINKDWWNKLSAEDQKVIQTAADEAEAERWAVAEAEDAAYLKKLRDAGIKVVELTDEQLAAFADKV
REEVWPQMEKEVGSEIMDKIR
>gnl|CDD|270392 cd13674, PBP2_TRAP_SBP_like_1, Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold. This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
VIKFSHVVAENTPKGLAANKFAELVEERSGGKVKVEVYPNSQLYGDIEELEALKLGDVQMIAPSLSKLSL
YVPEFQVFDLPFLFKDMEAVHRFTDGEVGDKLLRSLEEKGLVGLAFWDNGFKQFTANKPLIRTPEDLKGL
KFRIMGSDVLEAQFEALGATPVPLPFSEVYQALQTGVVDGQENTWSNIYSQKFYEVQKYLTVSNHGYLGY
AVITSEQFWDSLPPEDRKLLEDALKEATEYENELAAELNERDLERLKQAGNIKIVTLTPEERQAWREAMK
PVYDEFEPRIGKDLLEEAL
>gnl|CDD|270393 cd13675, PBP2_TRAP_SBP_like_5, Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold. This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
VLKLAHALAEDSHYGLAAEAFAEEVEEKTNGRVKVEIFPNSQLGGERELIEGLQLGTVDMAVVSTGPLAN
FVPEFAVFDLPFLFRDREHAYKVLDGEIGQELLAKLSDVGLKGLAWWENGFRNLTNSKRPVNTPDDLKGL
KIRTMENPIHIAAFRALGADPTPMAWTEVFTALQQGTIDGQENPITVIYSSKLYEVQKYLSLTGHVYSPA
VLLMSPDVWDSLSDEQQAIIREAAKEAAEYERALVDEMEEEALETLKEEGMEVVEPDDKAAFREAVAPVY
EKYEDQFGKDLLDRIQ
>gnl|CDD|270394 cd13676, PBP2_TRAP_DctP2_like, Substrate-binding component of Tripartite ATP-independent Periplasmic transporter DctP2 and related proteins; the type 2 periplasmic-binding protein fold. This subgroup includes TRAP transporter DctP2 and its similar proteins. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TIKLAHVGPEDHPTHKAAKAFKEYVEEKTGGRVKVEIFPSGQLGGEREMLEGVQLGTIDMGVIGTGPLSG
FVPKVGVFDLPFLFPSREAAYKVLDGELGQELAELMEKKGLKGLAYWENGFRHFTNNKRPIKTPADMKGL
KIRVMESPVQIATFKALGASPTPIAFGELYTALQQGVVDGQENPLALIVSSKFYEVQKYLSLTGHVYTPA
VLIINKDTWNSLSDDQQKIIQEAAKEARDVQRELNAEKENEGLEKLKAKGMEINELTDKEAFREAVQPVY
DKYEDEVGPELIDKVLK
>gnl|CDD|270395 cd13677, PBP2_TRAP_SBP_like_6, Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold. This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TIKLSHLNPADSFDNPVHAAALVFKNLVESRSNGRVAVEIYPGGQLGSEKECMEQVQKGVIQSFIATVGG
MASLYPPIQVLDLPFAFPNDRVAYAVFDGPFGKALAKDILEKTGLRLLGVGDTGGFRNFTNSKRPIKTPA
DMKGLKIRTMPLPSQQALVKALGASPTPIPWGELYTALQTGVVDGQMNPIPDIIFAKLDEVQKYLTLDNH
LYSPYFWVMNGDFFNSLPEEEQRIVLDAAEEAVVASRGRPKAQEDRGLEFLREKGGEVYTPTPEEREAFR
EAAQPAYDWWLEETYGEEWLELLL
>gnl|CDD|270396 cd13678, PBP2_TRAP_DctP10, Substrate-binding component of Tripartite ATP-independent Periplasmic transporter DctP10; the type 2 periplasmic-binding protein fold. This subgroup includes TRAP transporter DctP10 and its similar proteins. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
ELKLSVPDGENSYWGQAAQKFAELVREKSNGRINIKVYPNGQLSGGDQTKAIEMLRNGSIDLAILSTINY
SPFDPEFNVFSLPFLFDDYDALDAYLNGEGGKELFEILEKKGVTPLGIGENGFRQITNSKRPITTPEDLK
GLKLRVPGSPLFIDFFRALGANPTAMNFSEVYTALQQGTVDGQENPVDVPNSAKFYEVQKYVTLWNYVAD
PWVFGMNSKVWESLSEEDQAIIREAAVEAAQWQKANLAEEDGKILEELEKNGMEVNELTPEQIAAFKEAS
KPLYDKFKDLIGPDLFDAAE
>gnl|CDD|270397 cd13679, PBP2_TRAP_YiaO_like, Substrate-binding domain of 2,3-diketo-L-gulonate-binding Tripartite ATP-independent Periplasmic transport system and related proteins; the type 2 periplasmic-binding protein fold. This subfamily includes the solute receptor protein YiaO of TRAP transport system. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TIKFGHGLSESSPQGLGAKKFAELVEERSGGRIKVKVFPSAQLGNDTQMISALQGGTLEMTVVSTGPLVG
FVKEFAVFDLPFLFNSEEEADAVLDGPVGRKLLAKLEGKGLKGLAFWENGFRHLTNSKRPVNTPEDLKGL
KIRTMPNPVHIDTFKALGANPTPMPFSELYTALEQGAIDGQENPLSTIYSSKFYEVQKYLSLTNHVYSPL
VLVASKKFWDSLSPEDQKLLQEAAAEAALYQRELNREEEAKALAELKEKGMQVNELPDAELAKFREAVKP
VVDKYKAKIGADLVDEIQ
>gnl|CDD|270398 cd13680, PBP2_TRAP_SBP_like_4, Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold. This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
TLRISHQFPGGHHRGKNVQAFAKEVEERSKGELKVQVYPSAQLYKDNEQPQAVASGALEMGVAPLAYWGG
TVPEVNVFLMPFLFPSYEAARKALDSPFRKALDGAIEKKGVKVLAWADYGGAQFSSKKKPLVSPEDFKGL
KIRGYGKAFDEMLKALGASPVSMPGSEVYAALQTGTVDAAMTGSTAAVSRKLYEVAKYLTVTNASWFEFE
VVVNSKWFDGLSEEQQAALTEAAAEAEKFLREAAKKIDADAAKVLEDAGMKVVVLTAEEIKAWQEAAAPV
VDKFFAAAGEGGQKLLDAAL
>gnl|CDD|270399 cd13681, PBP2_TRAP_lactate, Substrate-binding component of a lactate binding Tripartite ATP-independent Periplasmic transporter and related proteins; the type 2 periplasmic-binding protein fold. This subgroup includes a lactate binding TRAP transporter and its similar proteins. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
RWRMQTAWDGGTVGYKTFERFCKRVKELTDGELEIEPFPAGAVVGTFEMFDAVRGGVLDGMNTFTLYWAG
KMPATAFLSSYPMGLPEPDQWEAWFYSLGGLQIAREAYAPQGLYYIGPVQHGPNIIHSKVPLRSIEDFKG
KKLRFPGGMIAEVFAALGVATTLLPGGEVYSALEKGVIDAADFVGPAVNYDLGFHQVAKYIIMGPPGTPG
IHQPVDLMDFVVNRNAWESLPAPYKAALAAAVREYSAAHRAAIQKADGEAWPKYKAAGVEVIRLSPEDLA
KFRAQAIPIWFKWANKDKDAARLFKSQLEVM
>gnl|CDD|270400 cd13682, PBP2_TRAP_alpha-ketoacid, Substrate-binding component of an alpha-keto acid binding Tripartite ATP-independent Periplasmic transporter and related proteins; contains the type 2 periplasmic-binding protein fold. This subgroup includes TRAP transporters that bind to ketoacids such as pyruvate and alpha-ketobutyrate, xylulose, and other unknown ligands. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
RWRMASSFPKSLDTIYGGAEVLAKRVAEMTGGRFEIRVFPAGELVPALQVLDAVQNGTVECGHTASYYYI
GKDPALAFDTAVPFGLTARQQNAWLYHGGGLELLRELYAQFNIINFPGGNTGVQMGGWFRKEIKTVADLK
GLKMRIPGFGGEVMSRLGVVVQNLPGGEIYPALERGAIDAAEWVGPYDDEKLGFNKVAPYYYYPGWWEPG
PELTFYVNKDAWNALPPEYQAILEAAAAEANLDMLARYDALNPPALQRLLAEGTQLRPFPDEIMDAAYKA
ADELYAENSAKNPAFKKIYESWKAFREDIREWFRTAELAYDNF
>gnl|CDD|270401 cd13683, PBP2_TRAP_DctP6_7, Substrate-binding domain of Tripartite ATP-independent Periplasmic transporter DctP6 and DctP7; type 2 periplasmic-binding protein fold. This subgroup includes TRAP-type mannitol/chloroaromatic compound transport system (Dctp6) and similar proteins. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the PBP2 superfamily. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
KWRFQTHLPKGTSEEDVIKEFADRVNEMSNGRLVIEVFHAGELVPTPEVLRAVQRGVVDMALIYGGYWAG
QAPVAALEGGLPGATRSAAEVNALFYEPGLADILREAYAEQGVHYLGPAPVDPLYLVSKKPINSLDDLKG
LKIRASGTAAKFLQKLGASPVSLPASELYTALQTGVIDGAIWGSWAENYLMGLHEVTKYFLYLHILGAQT
GELIVNMKAWESLPDDLKAIVETALDEASYDRAAHAVDWEWEAEAKMEAKGIELIQLPEEDVAILAEAAS
KVWDEYAEKSPRAAKYVEILREYL
>gnl|CDD|270402 cd13684, PBP2_TRAP_Dctp5_like, Substrate-binding component of Tripartite ATP-independent Periplasmic transporter DctP5 and related proteins; the type 2 periplasmic-binding protein fold. This subgroup includes TRAP transporter DctP5 and its similar proteins. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
KWKMATSWPGGPFLQEFAERFAERVKQLTNGRLVIQVFPAGVLVPALEVFDAVKNGVAEAGHSWPGYWVG
KDPAFALFASFPGGMNPEDYLLWLYEGGGKELYQELYGKFGLVYLPCGIGPTEIFAHSNKPIKTLEDLKG
LKLRTSGAWAEILRKLGASVVVLPGGEIYPALQRGVIDAAEFSTPSADYPLGFHEVAKYIMVPGVHQPAS
VFEVVINKKAWDALPPDLKALVEAAAKLTTLESLARFEYQDIEAMEFFKKGGVEIVRLDPETLKELREIG
NKWLDELAAEDPFFAKVLESQIAFRERWKNWKDY
>gnl|CDD|270403 cd13685, PBP2_iGluR_non_NMDA_like, The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate receptors, a member of the type 2 periplasmic-binding fold protein superfamily. This subfamily represents the ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate receptors including AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) receptors (GluR1-4), kainate receptors (GluR5-7 and KA1/2), and orphan receptors delta 1/2. iGluRs form tetrameric ligand-gated ion channels, which are concentrated at postsynaptic sites in excitatory synapses where they fulfill a variety of different functions. While this ligand-binding domain of iGluRs is structurally homologous to the periplasmic binding fold type II superfamily, the N-terminal leucine/isoleucine/valine#binding protein (LIVBP)-like domain belongs to the periplasmic-binding fold type I
NKTLRVTTILEPPFVMKKRDSLSGNPRFEGYCIDLLEELAKILGFDYEIYLVPDGKYGSRDENGNWNGMI
GELVRGEADIAVAPLTITAEREEVVDFTKPFMDTGISILMRKPTPIESLEDLAKQSKIEYGTLKGSSTFT
FFKNSKNPEYRRYEYTKIMSAMSPSVLVASAAEGVQRVRESNGGYAFIGEATSIDYEVLRNCDLTKVGEV
FSEKGYGIAVQQGSPLRDELSLAILELQESGELEKLKEKWWN
>gnl|CDD|270404 cd13686, GluR_Plant, Plant glutamate receptor domain; the type 2 periplasmic binding protein fold. This subfamily contains the glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
KKLRIGVPVKSGFKEFVKVTRDPITNSTSVTGFCIDVFEAAVKRLPYAVPYEFIPFNDAGSYDDLVYQVY
LKKFDAAVGDITITANRSLYVDFTLPYTESGLVMVVPVKDVTDIEELLKSGEYVGYQRGSFVREYLEEVL
FDESRLKPYGSPEEYAEALSKGSIAAAFDEIPYLKLFLAKYCKKYTMVGPTYKTGGFGFAFPKGSPLVAD
VSRAILKVTEGGKLQQIENKWF
>gnl|CDD|270405 cd13687, PBP2_iGluR_NMDA, The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily. The ligand-binding domain of the ionotropic NMDA subtype is structurally homologous to the periplasmic-binding fold type II superfamily, while the N-terminal domain belongs to the periplasmic-binding fold type I. The function of the NMDA subtype receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer comprising two NR1 and two NR2 (A, B, C, and D) or NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain
STHLKVVTLEEAPFVYVKCCYGFCIDLLKKLAEDVNFTYDLYLVTDGKFGTVNKSINGEWNGMIGELVSG
RADMAVASLTINPERSEVIDFSKPFKYTGITILVKKRNELSGINDPRLRNPSPPFRFGTVPNSSTERYFR
RQVELMHRYMEKYNYETVEEAIQALKNGKLDAFIWDSAVLEYEASQDEGCKLVTVGSLFARSGYGIGLQK
NSPWKRNVSLAILQFHESGFMEELDKKWL
>gnl|CDD|270406 cd13688, PBP2_GltI_DEBP, Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic binding protein fold. This subfamily represents the periplasmic-binding protein component of ABC transporter specific for carboxylic amino acids, including GtlI from Escherichia coli. The aspartate-glutamate binding domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
LEKIRRTGTLTLGYREDSVPFSYLDDNGKPVGYSVDLCNAIADALKKKLALPDLKVRYVPVTPQDRIPAL
TSGTIDLECGATTNTLERRKLVDFSIPIFVAGTRLLVRKDSGLNSLEDLAGKTVGVTAGTTTEDALRTVN
PLAGLQASVVPVKDHAEGFAALETGKADAFAGDDILLAGLAARSKNPDDLALIPRPLSYEPYGLMLRKDD
PDFRLLVDRALAQLYQSGEIEKLYDKWF
>gnl|CDD|270407 cd13689, PBP2_BsGlnH, Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 periplasmic-bindig protein fold. This group includes periplasmic glutamine-binding domain GlnP from Bacillus subtilis and its related proteins. The GlnP domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
LDDIKARGVLRCGVFDDVPPFGFIDPKTREIVGFDVDLCKAIAKKLGVKLELKPVNPAARIPELQNGRVD
LVAANLTYTPERAEQIDFSDPYFVTGQKLLVKKGSGIKSLKDLAGKRVGAVKGSTSEAAIREKLPKASVV
TFDDTAQAFLALQQGKVDAITTDETILAGLLAKAPDPGNYEILGEALSYEPYGIGVPKGESALRDFVNET
LADLEKDGEADKIYDKWFG
>gnl|CDD|270408 cd13690, PBP2_GluB, Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein fold. This group includes periplasmic glutamate-binding domain GluB from Corynebacterium efficiens and its related proteins. The GluB domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
LAKIRKRGRLRVGVKFDQPGFSLRNPTTGEFEGFDVDIARAVARAIGGDEPKVEFREVTSAEREALLQNG
TVDLVVATYSITPERRKQVDFAGPYYTAGQRLLVRAGSKIITSPEDLNGKTVCTAAGSTSADNLKKNAPG
ATIVTRDNYSDCLVALQQGRVDAVSTDDAILAGFAAQDPPGLKLVGEPFTDEPYGIGLPKGDDELVAFVN
GALEDMRADGTWQALFDRWLG
>gnl|CDD|270409 cd13691, PBP2_Peb1a_like, Substrate binding domain of an ABC aspartate/glutamate transporter; the type 2 periplasmic-binding protein fold. This group includes periplasmic aspartate/glutamate binding domain Peb1a and its closely related protein. The Peb1a is an important virulence factor in the food-borne human pathogen Campylobacter jejuni, which has a major role in adherence and host colonization. The Peb1a domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
VGKIKKRGVLRVGVKNDVPGFGYQDPETGKYEGMEVDLARKLAKKGDGVKVEFTPVTAKTRGPLLDNGDV
DAVIATFTITPERKKSYDFSTPYYTDAIGVLVEKSSGIKSLADLKGKTVGVASGATTKKALEAAAKKIGI
GVSFVEYADYPEIKTALDSGRVDAFSVDKSILAGYVDDSREFLDDEFAPQEYGVATKKGSTDLSKYVDDA
VKKWLADGTLEALIKKWG
>gnl|CDD|270410 cd13692, PBP2_BztA, Substrate bindng domain of ABC glutamate/glutamine/aspartate/asparagine transporter; the type 2 periplasmic binding protein fold. BztA is the periplamic-binding protein component of ABC transporter specific for carboxylic amino acids, glutamine and asparagine. The BZtA domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
LDEVRARGVLRCGVSEGLPGFSAVDDDGVWRGFDVDLCRAVAAAVLGDATAVEFVPLSASDRFTALASGE
VDVLSRNTTWTLSRDTELGVDFAPVYLYDGQGFLVRKDSGITSAKDLDGATICVQAGTTTETNLADYFKA
RGLKFTPVPFDSQDEARAAYFSGECDAYTGDRSALASERATLSNPDDHVILPEVISKEPLGPAVREGDSQ
WFDIVRWVLYALIAAEELGITSANVD
>gnl|CDD|270411 cd13693, PBP2_polar_AA, Substrate binding domain of polar amino-acid uptake ABC transporter; the type 2 periplasmic binding protein fold. This group includes the periplamic-binding protein component of putative polar amino acid ABC transporter. The polar amino-acid binding domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
LDRIKARGKLIVGVKNDYPPFGFLDPSGEIVGFEVDLAKDIAKRLGVKLELVPVTPSNRIQFLQQGKVDL
LIATMGDTPERRKVVDFVEPYYYRSGGALLAAKDSGINDWEDLKGKPVCGSQGSYYNKPLIEKYGAQLVA
FKGTPEALLALRDGRCVAFVYDDSTLQLLLQEDGEWKDYEIPLPTIEPSPWVIAVRKGETAFQNALDEII
KDWHRTGKLIELEKKWGI
>gnl|CDD|270412 cd13694, PBP2_Cysteine, Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein fold. This subfamily comprises of the periplasmic-binding protein component of ABC transporter specific for cysteine and its closely related proteins. The cysteine-binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
LEQIKQSGVIRIGVFGDKPPFGYVDENGKFQGFDIDLAKQIAKDLFGSGVKVEFVLVEAANRVPYLTSGK
VDLILANFTVTPERAEVVDFANPYMKVALGVVSPKDSNITSVAQLDGKTLLVNKGTTAEKYFTKNHPEIK
LLKYDQNAEAFQALKDGRADAYAHDNILVLAWAKSNPGFKVGIKNLGDTDFIAPGVQKGNKELLEFINAE
IKKLGKENFFKKAYEKTLE
>gnl|CDD|270413 cd13695, PBP2_Mlr3796_like, The substrate-binding domain of putative amino aicd transporter; the type 2 periplasmic binding protein fold. This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Mesorhizobium loti and its related proteins. The putative Mlr3796-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
LDDVLKRGKLIVGTGSTNAPWHFKSADGELQGFDIDMGRIIAKALFGDPQKVEFVNQSSDARIPNLTTDK
VDITCQFMTVTAERAQQVAFTIPYYREGVALLTKADSKYKDYDALKAAGASVTIAVLQNVYAEDLVHAAL
PNAKVAQYDTVDLMYQALESGRADAAAVDQSSIGWLMGQNPGKYRDAGYGWNPQTYGCAVKRGDLDWLNF
VNTALTEAMTGVEFDAYAASFK
>gnl|CDD|270414 cd13696, PBP2_Atu4678_like, The substrate binding domain of putative amino acid transporter; the type 2 periplasmic binding protein fold. This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Agrobacterium tumefaciens and its related proteins. The putative Atu4678-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
LDDILSSGKLRCGVCLDFPPFGFRDAAGNPVGYDVDYAKDLAKALGVKPEIVETPSPNRIPALVSGRVDV
VVANTTRTLERAKTVAFSIPYVVAGMVVLTRKDSGIKSFDDLKGKTVGVVKGSTNEAAVRALLPDAKIQE
YDTSADAILALKQGQADAMVEDNTVANYKASSGQFPSLEIAGEAPYPLDYVAIGVRKGDYDWLRYLNLFV
FQQNASGRYAELYQKWF
>gnl|CDD|270415 cd13697, PBP2_ArtJ_like, Putative substrate-binding domain of ABC arginine transporter; the type 2 periplasmic-binding protein fold. The ArtJ domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
LDEILASKKLVVGVNPNLPPLGAYDDKNVIEGFDVDVAKKLADRLGVKLELVPVSSADRVPFLMAGKIDA
VLGGLTRTPDRAKVIDFSDPVNTEVLGILTTAVKPYKDLDDLADPRVRLVQVRGTTPVKFIQDHLPKAQL
LLLDNYPDAVRAIAQGRGDALVDVLDYMGRYTKNYPAKWRVVDDPAIEVDYDCIGVAQGNTALLEVVNGE
LADLHKDGFIQASYKRWF
>gnl|CDD|270416 cd13698, PBP2_HisGluGlnArgOpine, Substrate binding domain of ABC-type histidine/glutamate/glutamine/arginine/opine transporter; the type 2 periplasmic-binding protein fold. This group includes periplasmic-binding component of His/Glu/Gln/Arg/Opine ATP-binding cassette transport system. This substrate-binding domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GKTIRMGTEGAYPPYNFINDAGEVDGFERELGDELCKRAELTCEWVTNEWDSIIPNLVSGNYDTIIAGMS
ITDERDEVIDFTQNYIPPTASAYVALSDDADDIGGVVAAQTSTIQAGHVAESGATLLEFATPDETVAAVR
NGEADAVFADKDYLVPIVEESGGELMFVGDDVPLGGGIGMGLRESDGELREKFDAAITSMKEDGSLNTLL
KKWF
>gnl|CDD|270417 cd13699, PBP2_OccT_like, Substrate binding domain of ABC-type octopine transporter-like; the type 2 periplasmic-binding protein fold. This group includes periplasmic octopine-binding protein and related proteins. This group belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
EKTLTIATEGAYAPWNLTDPDGKLGGFEIDLANVLCERMKVKCTFVVQDWDGMIPALNAGKFDVIMDAMS
ITAERKKVIDFSTPYAATPNSFAVVTIGVQSGTTYAKFIEKYFKGVADIREYKTTAERDLDLAAGRVDAV
FADATYLAAFLAKPDNADLTLVGPKLSGDIWGEGEGVGLRKGDTELKAKFDSAIKAAVADGTVKKLSEKW
F
>gnl|CDD|270418 cd13700, PBP2_Arg_STM4351, Substrate binding domain of arginine-specific ABC transporter; type 2 periplasmic-binding protein fold. This group includes domains similar to Escherichia coli arginine third transport system. STM4351 is the high arginine specific periplasmic-binding protein of ABC transport system. STM4351 belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
AETIHFGTEATYPPFESIGAKGEIVGFDIDLANALCKQMQAECTFTNQAFDSLIPSLKFKKFDAVISGMD
ITPEREKQVSFSTPYYENSAVVIAKKDTYKTFADLKGKKIGVQNGTTHQKYLQDKHKEITTVSYDSYQNA
FLDLKNGRIDGVFGDTAVVAEWLKTNPDLAFVGEKVTDPNYFGTGLGIAVRKDNQALLEKLNAALAAIKA
NGEYQKIYDKWF
>gnl|CDD|270419 cd13701, PBP2_ml15202_like, Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the type 2 periplasmic-binding protein fold. This group includes uncharacterized periplasmic substrate-binding protein similar to HisJ and LAO proteins which are involved in the ABC transport of histidine-, arginine, and lysine-arginine-ornithine amino acids. This group belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
ADPLKIGISAEPYPPFTSKDASGKWSGWEIDLIDALCARLDARCEITPVAWDGIIPALQSGKIDMIWNSM
SITDERKKVIDFSDPYYETPTAIVGAKSDDRRVTPEDLKGKVIGVQGSTNNATFARKHFADDAELKVYDT
QDEALADLVAGRVDAVLADSLAFTEFLKSDGGADFEVKGTAADDPEFGLGIGAGLRQGDTALREKLNTAI
ASLRADGTYDEISARYF
>gnl|CDD|270420 cd13702, PBP2_mlr5654_like, Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the type 2 periplasmic-binding protein fold. This group includes uncharacterized periplasmic substrate-binding protein similar to HisJ and LAO proteins which serve as initial receptors in the ABC transport of histidine-, arginine, and lysine-arginine-ornithine amino acids. This group belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
AKKIRIGTEGAYPPFNYVDADGKLGGFDVDIANALCAEMKAKCEIVAQDWDGIIPALQAKKFDAIIASMS
ITPERKKQVDFTDPYYTNPLVFVAPKDSTITDVTPDDLKGKVIGAQRSTTAAKYLEENYPDAEVKLYDTQ
EEAYLDLASGRLDAVLSDKFPLLDWLKSPAGKCCELKGEPIADDDGIGIAVRKGDTELREKFNKALAAIR
ADGTYKKINAKYF
>gnl|CDD|270421 cd13703, PBP2_HisJ_LAO, Substrate binding domain of ABC-type histidine- and lysine/arginine/ornithine transporters; the type 2 periplasmic-binding protein fold. This subgroup includes the periplasmic-binding proteins, HisJ and LAO, that serve as initial receptors in the ABC transport of histidine and lysine-arginine-ornithine amino acids. They are belong to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
WKTLRIGTDATYPPFESKDADGELTGFDIDLGNALCAEMKVKCTWVEQDFDGLIPGLLARKFDAIISSMS
ITEERKKVVDFTDKYYHTPSRLVARKGSGIDPTPASLKGKRVGVQRGTTQEAYATDNWAPKGVDIKRYAT
QDEAYLDLVSGRVDAALQDAVAAEEGFLKKPAGKDFAFVGPSVTDKKYFGEGVGIALRKDDTELKAKLNK
AIAAIRADGTYDKIQKKYF
>gnl|CDD|270422 cd13704, PBP2_HisK, The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding fold protein. This subfamily includes the periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
ARTVIVGGDKNYPPYEFLDENGNPTGFNVDLLRAIAEEMGLKVEIRLGPWSEVLQALENGEIDVLIGMAY
SEERAKLFDFSDPYLEVSVSIFVRKGSSIINSLEDLKGKKVAVQRGDIMHEYLKERGLGINLVLVDSPEE
ALRLLASGKVDAAVVDRLVGLYLIKELGLTNVKIVGPPLLPLKYCFAVRKGNPELLAKLNEGLAILKASG
EYDEIYEKWF
>gnl|CDD|270423 cd13705, PBP2_BvgS_D1, The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein. This group contains the first domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a histidine-kinase (HK), a receiver and a histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
KRTLRVGVSAPDYPPFDITSSGGRYEGITADYLGLIADALGVRVEVRRYPDREAALEALRNGEIDLLGTA
NGSEAGDGGLLLSQPYLPDQPVLVTRIGDSRQPPPDLAGKRVAVVPGYLPAEEIKQAYPDARIVLYPSPL
QALAAVAFGQADYFLGDAISANYLISRNYLNNLRIVRFAPLPSRGFGFAVRPDNTRLLRLLNRALAAIPD
EQRDEILRRWS
>gnl|CDD|270424 cd13706, PBP2_HisK_like_1, Putative sensor domain similar to HisK; the type 2 periplasmic binding fold protein. This group includes periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
PQPLVVAMDKDYPPFSFLDEDGEPQGILVDLWRLWSEKTGIPVEFVLLDWNESLEAVRQGEADVHDGLFK
SPEREKYLDFSQPIATIDTYLYFHKDLSGITNLSDLKGFRVGVVKGDAEEEFLRAHGPILSLVYYDNYEA
MIEAAKAGEIDVFVADEPVANYYLYKYGLPDEFRPAFRLYSGQLHPAVAKGNSALLDLINRGFALISPEE
LARIERKWL
>gnl|CDD|270425 cd13707, PBP2_BvgS_D2, The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein. This group contains the second domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
HPVVRVVVNPDLAPLSFFDSNGQFRGISADLLELISLRTGLRFEVVRASSPAEMIEALRSGEADMIAALT
PSPEREDFLLFTRPYLTSPFVLVTRKDAAAPSSLEDLAGKRVAIPAGSALEDLLRRRYPQIELVEVDNTA
EALALVASGKADATVASLISARYLINHYFRDRLKIAGILGEPPAPIAFAVRRDQPELLSILDKALLSIPP
DELLELRNRWR
>gnl|CDD|270426 cd13708, PBP2_BvgS_like_1, Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
KKEITMCVDPDWMPYEGIDEGGKHVGIAADYLKLIAERLGIPIELVPTKSWSESLEAAKEGKCDILSLLN
QTPEREEYLNFTKPYLSDPNVLVTREDHPFIADLSDLGDKTIGVVKGYAIEEILRQKYPNLNIVEVDSEE
EGLKKVSNGELFGFIDSLPVAAYTIQKEGLFNLKISGKLDEDNELRIGVRKDEPLLLSILNKAIASITPE
ERQEILNKWV
>gnl|CDD|270427 cd13709, PBP2_YxeM, Substrate binding domain of an ABC transporter YxeMNO; the type 2 periplasmic binding protein fold. This group contains cystine-binding domain (YxeM) of a periplasmic receptor-dependent ATP-binding cassette transporter and its closely related proteins. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
KVIKVGSSGSSYPFTFKENGKLKGFEVDVWNAIGKRTGYKVEFVTADFSGLFGMLDSGKVDTIANQITIT
PERQEKYDFSEPYVYDGAQIVVKKDNNSIKSLEDLKGKTVAVNLGSNYEKILKAVDKDNKITIKTYDDDE
GALQDVALGRVDAYVNDRVSLLAKIKKRGLPLKLAGEPLVEEEIAFPFVKNEKGKKLLEKVNKALEEMRK
DGTLKKISEKWFGIDIT
>gnl|CDD|270428 cd13710, PBP2_TcyK, Substrate binding domain of an ABC transporter TcyJKLMN; the type 2 periplasmic binding protein fold. This group contains periplasmic cystine-binding domain (TcyK) of an ATP-binding cassette transporter from Bacillus subtilus and its closely related proteins. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
KTVKVATGADTPPFSYEDKKGELTGYDIEVLKAIDKKLPQYKFKFKVTEFSSILTGLDSGKYDMAANNFS
KTKERAKKFLFSKVPYGYSPLVLVVKKDSNDINSLDDLAGKTTIVVAGTNYAKVLEAWNKKNPDNPIKIK
YSGEGINDRLKQVESGRYDALILDKFSVDTIIKTQGDNLKVVDLPPVKKPYVYFLFNKDQQKLQKDIDKA
LKELKKDGTLKKLSKKYFGGDYF
>gnl|CDD|270429 cd13711, PBP2_Ngo0372_TcyA, Substrate binding domain of ABC transporters involved in cystine import; the type 2 periplasmic binding protein fold. This subgroup includes cystine-binding domain of periplasmic receptor-dependent ATP-binding cassette transporters from Neisseria gonorrhoeae and Bacillus subtilis and their related proteins. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
GVLTIGTEGTYAPFTYHDKSGKLTGFDVEVARAVAKKLGVKVEFVETQWDSMIAGLDAGRFDVVANQVGI
TDERKKKYDFSTPYIYSRAVLIVRKDNSDIKSFADLKGKKSAQSLTSNWGKIAKKYGAQVVGVDGFAQAV
ELITQGRADATINDSLAFLDYKKQHPDAPVKIAAETDDASESAFLVRKGNDELVAAINKALKELKADGTL
KKISEKYFGKDV
>gnl|CDD|270430 cd13712, PBP2_FliY, Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic binding protein fold. This group contains cystine binding domain FliY and its related proteins. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLRIGLEGTYPPFNFKDETGQLTGFEVDVAKALAAKLGVKPEFVTTEWSGILAGLQAGKYDVIINQVGIT
PERQKKFDFSQPYTYSGIQLIVRKNDTRTFKSLADLKGKKVGVGLGTNYEQWLKSNVPGIDVRTYPGDPE
KLQDLAAGRIDAALNDRLAANYLVKTSLELPPTGGAFARQKSGIPFRKGNPKLKAAINKAIEDLRADGTL
AKLSEKWFG
>gnl|CDD|270431 cd13713, PBP2_Cystine_like_1, Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 periplasmic binding protein fold. This group contains uncharacterized periplasmic cystine-binding domain of ATP-binding cassette (ABC) transporters. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
ELRFAMSGQYPPFNFLDEDNQLVGFDVDVAKAIAKRLGVKVEPVTTAWDGIIAGLWAGRYDIIIGSMTIT
EERLKVVDFSNPYYYSGAQIFVRKDSTITSLADLKGKKVGVVTGTTYEAYARKYLPGAEIKTYDSDVLAL
QDLALGRLDAVITDRVTGLNAIKEGGLPIKIVGKPLYYEPMAIAIRKGDPELRAAVNKALAEMKADGTLE
KISKKWFG
>gnl|CDD|270432 cd13714, PBP2_iGluR_Kainate, Kainate receptor of the type 2 periplasmic-binding fold superfamily. This group contains glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
NKTLIVTTILEEPYVMLKESAKPLTGNDRFEGFCIDLLKELAKILGFNYTIRLVPDGKYGSYDPETGEWN
GMVRELIDGRADLAVADLTITYERESVVDFTKPFMNLGISILYRKPTPIESADDLAKQTKIKYGTLRGGS
TMTFFRDSNISTYQKMWNFMMSAKPSVFVKSNEEGVARVLKGKYAFLMESTSIEYVTQRNCNLTQIGGLL
DSKGYGIATPKGSPYRDKLSLAILKLQEKGKLEMLKNKWWK
>gnl|CDD|270433 cd13715, PBP2_iGluR_AMPA, The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtypes of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily. This family represents the ligand-binding domain of the AMPA receptor subunits, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current
NRTYIVTTILEEPYVMMKKNHEGEPLEGNERYEGYCVDLADEIAKHLGIKYELRIVKDGKYGARDADTGI
WNGMVGELVRGEADIAIAPLTITLVRERVIDFSKPFMSLGISIMIKKPVPIESAEDLAKQTEIAYGTLDS
GSTKEFFRRSKIAVYDKMWEYMNSAEPSVFVRTTDEGIARVRKSKGKYAYLLESTMNEYINQRKPCDTMK
VGGNLDSKGYGIATPKGSPLRNPLNLAVLKLKENGELDKLKNKWWYDKGEC
>gnl|CDD|270434 cd13716, PBP2_iGluR_delta_like, The ligand-binding domain of the delta family of ionotropic glutamate receptors, a member of the type 2 periplasmic-binding fold protein superfamily. This subfamily represents the ligand-binding domain of an orphan family of delta receptors, GluRdelta1 and GluRdelta2. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of iGluRs belongs to the periplasmic-binding fold type I. Although the delta receptors are members of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetical analysis shows that both GluRdelta1 and GluRalpha2 are more homologous to non-NMDA receptors. GluRdelta2 was shown to function as an AMPA-like receptor by mutation analysis. Moreover, targeted disruption of GluRdelta2 gene caused motor coordination impairment, Purkinje cell maturation, and long-term depression of synaptic transmission. It has been suggested that GluRdelta2 is the receptor for cerebellin 1, a glycoprotein of the Clq, and the tumor necrosis factor family which is secreted from cerebellar granule cells. Furthermore, recent studies have shown that the orphan GluRdelta1 plays an essential role in high-frequency hearing and ionic homeostasis in the basal cochlea and that the locus encoding GluRdelta1 may be involved in congenial or acquired high-frequency hearing loss in humans
GVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALANYLGFKYEIYVAPDHKYGSQQEDGTWNGLI
GELVFKRADIGISALTITPERENVVDFTTRYMDYSVGVLLRKAESIQSLQDLSKQTDIPYGTVLDSAVYE
YVRSKGTNPFERDSMYSQMWRMINRSNGSENNVSESSEGIRKVKYGNYAFVWDAAVLEYVAINDDDCSFY
TVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWP
>gnl|CDD|270435 cd13717, PBP2_iGluR_putative, The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily. This group contains glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
RRVYRIGTVESPPFVYRDRDGSPIWEGYCIDLIEEISEILNFDYEIVEPEDGKFGTMDENGEWNGLIGDL
VRKEADIALAALSVMAEREEVVDFTVPYYDLVGITILMKKPERPTSLFKFLTVLELEVWREFTLKESLWF
CLTSLTPQGGGEAPKNLSGRLLVATWWLFVFIIIASYTANLAAFLTVSRLQTPVESLDDLARQYKIQYTV
VKNSSTHTYFERMKNAEDTLYEMWKDMSLNDSLSPVERAKLAVWDYPVSEKYTKIYQAMQEAGLVANAEE
GVKRVRESTSAGFAFIGDATDIKYEILTNCDLQEVGEEFSRKPYAIAVQQGSPLKDELNYAILELQNDRF
LEKLKAKWWN
>gnl|CDD|270436 cd13718, PBP2_iGluR_NMDA_Nr2, The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily. This group contains the ligand-binding domain of the NR2 subunit of NMDA receptor family. The ionotropic N-methyl-d-asparate (NMDA) subtype of glutamate receptors serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer composed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain
KFHLKIVTLEEAPFVIVEPVDPLTGTCMRNTVPCRKQLNHENSTDADENRYVKKCCKGFCIDILKKLAKD
VGFTYDLYLVTNGKHGKKINGVWNGMIGEVVYKRADMAVGSLTINEERSEVVDFSVPFVETGISVMVARS
NQVSGLSDKKFQRPHDQSPPFRFGTVPNGSTERNIRNNYPEMHQYMRKYNQKGVEDALVSLKTGKLDAFI
YDAAVLNYMAGQDEGCKLVTIGSGKWFAMTGYGIALQKNSKWKRPFDLALLQFRGDGELERLERLWLTGI
CHN
>gnl|CDD|270437 cd13719, PBP2_iGluR_NMDA_Nr1, The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily. This group contains the ligand binding domain of the NR1, an essential channel-forming subunit of the NMDA receptor. The ionotropic N-methyl-d-asparate (NMDA) subtype of glutamate receptors serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer ccomposed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. When co-expressed with NR1, the NR3 subunits form receptors that are activated by glycine alone and therefore can be classified as excitatory glycine receptors. NR1/NR3 receptors are calcium-impermeable and unaffected by ligands acting at the NR2 glutamate-binding site
STHLKIVTIHEEPFVYVRPTPSDGTCREEFTVNCPNFNISGRPTVPFCCYGYCIDLLIKLARKMNFTYEL
HLVADGQFGTQERVNNSNKKEWNGMMGELVSGRADMIVAPLTINPERAQYIEFSKPFKYQGLTILVKKEI
RLTGINDPRLRNPSEKFIYATVKGSSVDMYFRRQVELSTMYRHMEKHNYETAEEAIQAVRDGKLHAFIWD
SSRLEFEASQDCDLVTAGELFGRSGYGIGLQKNSPWTDNVSLAILKMHESGFMEDLDKTWIRYQECE
>gnl|CDD|270438 cd13720, PBP2_iGluR_NMDA_Nr3, The ligand-binding domain of the NR3 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily. This group contains the ligand-binding domain of the NR3 subunit of NMDA receptor family. The ionotropic N-methyl-d-asparate (NMDA) subtype of glutamate receptors serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer composed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain
RPHLRVVTLLEHPFVFTREVDEEGLCPAGQLCLDPMTNDSSTLDALFSSLHSSNDTVPIKFRKCCYGYCI
DLLEKLAEDLGFDFDLYIVGDGKYGAWRNGRWTGLVGDLLSGRAHMAVTSFSINSARSQVIDFTSPFFST
SLGILVRTRDELSGIHDPKLHHPSQGFRFGTVRESSAEYYVKKSFPEMHEHMRRYSLPNTPEGVEYLKND
PEKLDAFIMDKALLDYEVSIDADCKLLTVGKPFAIEGYGIGLPQNSPLTSNISELISQYKSNGFMDLLHD
KWY
>gnl|CDD|270439 cd13721, PBP2_iGluR_Kainate_GluR6, GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily. This group contains glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWN
GMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKGTPIDSADDLAKQTKIEYGAVEDGA
TMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLI
DSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWR
>gnl|CDD|270440 cd13722, PBP2_iGluR_Kainate_GluR5, GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily. This group contains glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
NRTLIVTTILEEPYVMYRKSDKPLYGNDRFEGYCLDLLKELSNILGFLYDVKLVPDGKYGAQNDKGEWNG
MVKELIDHRADLAVAPLTITYVREKVIDFSKPFMTLGISILYRKGTPIDSADDLAKQTKIEYGAVRDGST
MTFFKKSKISTYEKMWAFMSSRQQTALVKNSDEGIQRVLTTDYALLMESTSIEYVTQRNCNLTQIGGLID
SKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMMKEKWWR
>gnl|CDD|270441 cd13723, PBP2_iGluR_Kainate_GluR7, GluR7 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily. This group contains glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap
NRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKGQWNG
MVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLA
YLGVSCVLFVIARFSPYEWYDAHPCNPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIW
WFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMS
SKPSALVKNNEEGIQRALTADYALLMESTTIEYVTQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIA
ILQLQEEDKLHIMKEKWWR
>gnl|CDD|270442 cd13724, PBP2_iGluR_kainate_KA1, The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a member of the type 2 periplasmic-binding fold protein superfamily. This group contains the ligand-binding domain of the KA1 subunit of kainate receptor. While this ligand-binding domain is structurally homologous to the periplasmic binding fold type II superfamily, the N_terminal domain of kainate receptors belongs to the periplasmic-binding fold type I. There are five types of kainate receptors, GluR5, GluR6, GluR7, KA1, and KA2, which are structurally similar to AMPA and NMDA subunits of ionotropic glutamate receptors. KA1 and KA2 subunits can only form functional receptors with one of the GluR5-7 subunits. Moreover, GluR5-7 can also form functional homomeric receptor channels activated by kainate and glutamate when expressed in heterologous systems. Kainate receptors are involved in excitatory neurotransmission by activating postsynaptic receptors and in inhibitory neurotransmission by modulating release of the inhibitory neurotransmitter GABA through a presynaptic mechanism. Kainate receptors are closely related to AMAP receptors. In contrast of AMPA receptors, kainate receptors play only a minor role in signaling at synapses and their function is not well defined
NTTLVVTTILENPYLMLKGNHQEMEGNDRYEGFCVDMLKELAEILRFNYKIRLVGDGVYGVPEANGTWTG
MVGELIARKADLAVAGLTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPGVWLFMLLA
YLAVSCVLFLVARLTPYEWYSPHPCAQGRCNLLVNQYSLGNSLWFPVGGFMQQGSTIAPPIESVDDLADQ
TAIEYGTIHGGSSMTFFQNSRYQTYQRMWNYMYSKQPSVFVKSTEEGIARVLNSNYAFLLESTMNEYYRQ
RNCNLTQIGGLLDTKGYGIGMPVGSVFRDEFDLAILQLQENNRLEILKRKWWE
>gnl|CDD|270443 cd13725, PBP2_iGluR_kainate_KA2, The ligand-binding domain of the kainate subtype KA2 of ionotropic glutamate receptors, a member of the type 2 periplasmic-binding fold protein superfamily. This group contains the ligand-binding domain of the KA2 subunit of kainate receptor. While this ligand-binding domain is structurally homologous to the periplasmic binding fold type II superfamily, the N_terminal domain of kainate receptors belongs to the periplasmic-binding fold type I. There are five types of kainate receptors, GluR5, GluR6, GluR7, KA1, and KA2, which are structurally similar to AMPA and NMDA subunits of ionotropic glutamate receptors. KA1 and KA2 subunits can only form functional receptors with one of the GluR5-7 subunits. Moreover, GluR5-7 can also form functional homomeric receptor channels activated by kainate and glutamate when expressed in heterologous systems. Kainate receptors are involved in excitatory neurotransmission by activating postsynaptic receptors and in inhibitory neurotransmission by modulating release of the inhibitory neurotransmitter GABA through a presynaptic mechanism. Kainate receptors are closely related to AMAP receptors. In contrast of AMPA receptors, kainate receptors play only a minor role in signaling at synapses and their function is not well defined
NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTG
MVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISILYRVHMPVESADDLADQTNIEYGTIHAGST
MTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLNCNLTQIGGLLD
TKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWE
>gnl|CDD|270444 cd13726, PBP2_iGluR_AMPA_GluR2, The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtype GluR2 of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily. This group contains the ligand-binding domain of the AMPA receptor subunit GluR2, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I. The AMPA receptors are the most commonly found receptor in the nervous system and sensitive to the artificial glutamate analog, AMPA. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current
NKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWN
GMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKGTPIESAEDLSKQTEIAYGTLDSGS
TKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVG
GNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC
>gnl|CDD|270445 cd13727, PBP2_iGluR_AMPA_GluR4, The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtype GluR4 of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily. This group contains the ligand-binding domain of the AMPA receptor subunit GluR4, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I.The AMPA receptors are the most commonly found receptor in the nervous system and sensitive to the artificial glutamate analog, AMPA. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current
NRTVVVTTIMESPYVMYKKNHEMFEGNDKFEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDPETKIWN
GMVGELVYGKAEIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQPIESAEDLAKQTEIAYGTLDSGS
TKEFFRRSKIAVYEKMWTYMKSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVG
GNLDSKGYGVATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC
>gnl|CDD|270446 cd13728, PBP2_iGluR_AMPA_GluR3, The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtype GluR3 of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily. This group contains the ligand-binding domain of the AMPA receptor subunit GluR3, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I. The AMPA receptors are the most commonly found receptor in the nervous system and sensitive to the artificial glutamate analog, AMPA. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current
NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWN
GMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQPIESAEDLAKQTEIAYGTLDSGS
TKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVG
GNLDSKGYGVATPKGSALGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC
>gnl|CDD|270447 cd13729, PBP2_iGluR_AMPA_GluR1, The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtype GluR1 of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily. This group contains the ligand-binding domain of the AMPA receptor subunit GluR1, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I. The AMPA receptors are the most commonly found receptor in the nervous system and sensitive to the artificial glutamate analog, AMPA. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current
NRTYIVTTILESPYVMLKKNHEQFEGNDRYEGYCVELAAEIAKHVGYSYKLEIVSDGKYGARDPETKMWN
GMVGELVYGKADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPTSPIESAEDLAKQTEIAYGTLDAG
STKEFFRRSKIAVFEKMWSYMKSADPSVFVKTTDEGVMRVRKSKGKYAYLLESTMNEYIEQRKPCDTMKV
GGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC
>gnl|CDD|270448 cd13730, PBP2_iGluR_delta_1, The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the type 2 periplasmic-binding fold protein superfamily. This group contains the ligand-binding domain of the delta1 receptor of an orphan glutamate receptor family. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of delta receptors belongs to the periplasmic-binding fold type I. Although the delta receptors are a member of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetical analysis shows that both GluRdelta1 and GluRdelta2 are more homologous to non-NMDA receptors. GluRdelta2 was shown to function as an AMPA-like receptor by mutation analysis. Moreover, targeted disruption of GluRdelta2 gene caused motor coordination impairment, Purkinje cell maturation, and long-term depression of synaptic transmission. It has been suggested that GluRdelta2 is the receptor for cerebellin 1, a glycoprotein of the Clq, and the tumor necrosis factor family which is secreted from cerebellar granule cells. Furthermore, recent studies have shown that the orphan GluRdelta1 plays an essential role in high-frequency hearing and ionic homeostasis in the basal cochlea and that the locus encoding GluRdelta1 may be involved in congenial or acquired high-frequency hearing loss in humans
GLTLKVVTVLEEPFVMVAENILGQPKRYKGFSIDVLDALAKALGFKYEIYQAPDGKYGHQLHNTSWNGMI
GELISKRADLAISAITITPERESVVDFSKRYMDYSVGILIKKPEPIRTFQDLSKQVEMSYGTVRDSAVYE
YFRAKGTNPLEQDSTFAELWRTISKNGGADNCVSSPSEGIRKAKKGNYAFLWDVAVVEYAALTDDDCSVT
VIGNSISSKGYGIALQHGSPYRDLFSQRILELQDTGDLDVLKQKWWP
>gnl|CDD|270449 cd13731, PBP2_iGluR_delta_2, The ligand-binding domain of an orphan ionotropic glutamate receptor delta-2, a member of the type 2 periplasmic-binding fold protein superfamily. This group contains the ligand-binding domain of the delta-2 receptor of an orphan glutamate receptor family. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of delta receptors belongs to the periplasmic-binding fold type I. Although the delta receptors are a member of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetical analysis shows that both GluRdelta1 and GluRalpha2 are more homologous to non-NMDA receptors. GluRdelta2 was shown to function as an AMPA-like receptor by mutation analysis. Moreover, targeted disruption of GluRdelta2 gene caused motor coordination impairment, Purkinje cell maturation, and long-term depression of synaptic transmission. It has been suggested that GluRdelta2 is the receptor for cerebellin 1, a glycoprotein of the Clq, and the tumor necrosis factor family which is secreted from cerebellar granule cells. Furthermore, recent studies have shown that the orphan GluRdelta1 plays an essential role in high-frequency hearing and ionic homeostasis in the basal cochlea and that the locus encoding GluRdelta1 may be involved in congenial or acquired high-frequency hearing loss in humans
GVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLV
GELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAESIQSLQDLSKQTDIPYGTVLDSAVYE
HVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFY
TVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWP
>gnl|CDD|467029 cd13732, HFD_CENP-W, histone-fold domain found in centromere protein W (CENP-W) and similar proteins. CENP-W, also called cancer-up-regulated gene 2 protein (CUG2), is a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in the assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENP-A into centromeres. CENP-W is also part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENP-A. Moreover, CENP-W forms a heterodimer with CENP-T. This dimer co-assembles with CENP-S-CENP-X heterodimers at centromeres to form the tetrameric CENP-T-W-S-X complex, which is a subcomplex of the large constitutive centromere-associated network (CCAN, also known as the interphase centromere complex or ICEN). The heterotetrameric CENP-T-W-S-X complex binds and supercoils DNA and plays an important role in kinetochore assembly. CENP-W has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. It is required for normal chromosome organization and normal progress through mitosis
KLYPRSTLKKIIKKHLPGLRLAKNADILVYLDYLLFLQRLAEEARTEARESGSKTIKPEHVRKAAKKVLK
KFRG
>gnl|CDD|293968 cd13733, SPRY_PRY_C-I_1, PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, TRIM10, TRIM11, TRIM17, TRIM20, TRIM21, TRIM27, TRIM35, TRIM38, TRIM41, TRIM50, TRIM58, TRIM60, TRIM62, TRIM69, TRIM72, NF7 and bloodthirsty. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class IV TRIM proteins, including TRIM7, TRIM35, TRIM41, TRIM50, TRIM62, TRIM69, TRIM72, TRIM protein NF7 and bloodthirsty (bty). TRIM7 interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM35 may play a role as a tumor suppressor and is implicated in the cell death mechanism. TRIM41 is localized to speckles in the cytoplasm and nucleus, and functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23. TRIM62 is involved in the morphogenesis of the mammary gland; loss of TRIM62 gene expression in breast is associated with increased risk of recurrence in early-onset breast cancer. TRIM69 is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. TRIM protein NF7, which also contains a chromodomain (CHD) at the N-terminus and an RFP (Ret finger protein)-like domain at the C-terminus, is required for its association with transcriptional units of RNA polymerase II which is mediated by a trimeric B box. In Xenopus oocyte, xNF7 has been identified as a nuclear microtubule-associated protein (MAP) whose microtubule-bundling activity, but not E3-ligase activity, contributes to microtubule organization and spindle integrity. Bloodthirsty (bty) is a novel gene identified in zebrafish and has been shown to likely play a role in in regulation of the terminal steps of erythropoiesis. TRIM72 has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site
DVTLDPDTAHPNLILSEDLKSVRYGDKRQNLPDNPERFDTCVCVLGSEGFSSGRHYWEVEVGGKTDWDLG
VARESVNRKGKITLSPENGYWTVGLRNGNEYKALTSPSTPLSLREKPQKVGVFLDYEEGQVSFYNVDDGS
HIYTFTDCFTEKLYPYFSPCLNDGGKNSAPLIIC
>gnl|CDD|293969 cd13734, SPRY_PRY_C-II, PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67, TRIM76). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67 and TRIM76. TRIM1 (also known as MID2) and its close homolog, TRIM18 (also known as MID1), both contain a B30.2-like domain at their C-terminus and a single fibronectin type III (FN3) motif between it and their N-terminal RBCC domain. Their coiled-coil motifs mediate both homo- and heterodimerization, a prerequisite for association of the rapamycin-sensitive PP2A regulatory subunit Alpha 4 with microtubules. Mutations in TRIM18 have shown to cause Opitz syndrome, a disorder causing congenital anomalies such as cleft lip and palate as well as heart defects. TRIM9 is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. Its immunoreactivity is severely decreased in affected brain areas in Parkinson's disease and dementia with Lewy bodies, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM36 interacts with centromere protein-H, one of the kinetochore proteins and possibly associates with chromosome segregation; an excess of TRIM36 may cause chromosomal instability. TRIM46 has not yet been characterized. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It is possibly involved in protein kinase A signaling as well as vesicular trafficking. It has also been implicated in Duchenne muscular dystrophy and cardiac disease. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site
FKLDPKTAHRKLRLSNDNLTVEYDPEGSKDQAAVLPRRFTGSPAVLGDVAISSGRHYWEVSVSRSTSYRV
GVAYKSAPRDEDLGKNSTSWCLSRDNNRYTARHDGKVVDLRVTGHPARIGVLLDYDNGTLSFYDAESKQH
LYTFHVDFEGPVCPAFAVWNGSLTLH
>gnl|CDD|293970 cd13735, SPRY_HECT_like, SPRY domain in HECT E3. This domain consists of the SPRY subdomain similar to those found at the N-terminus of the HECT (homologous to the E6AP carboxyl terminus) protein, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). HECT E3 binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains. It has a prominent role in protein trafficking and immune response, and is involved in crucial signaling pathways implicated in tumorigenesis
RGVFVYANSPIPAQAPSFYWEVEVVSLGETDDSDGPIISVGFAPPAEDRDGAWTNPVGTCLFHNNGRAVH
YRGSSLTQWKSIRTDVTLSIGDVAGCGWERTDTPPAKGRVYFTHNGQRLPRSLQDVSGGLWPVVHVQKKN
TRVRANFGSR
>gnl|CDD|293971 cd13736, SPRY_PRY_TRIM25, PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM25 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function
VIFDYNTAHNKVSLSENYTKASVSDDPQNYREHPQRFTYCSQVLGLHCFKQGIHYWEVELQKNNFCGVGI
CYGSMDRQGPESRLGRNSESWCVEWFNVKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVQDKVH
LMYKFKVDFTEALYPAFWVFSAGTTLSLC
>gnl|CDD|293972 cd13737, SPRY_PRY_TRIM25-like, PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of proteins similar to TRIM25 (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function
LNFDPNTASEELFLFKETHSVLNMGILLESFFGPCQGFNHWPQVLCTRSLCEGCHYWEAEVSNSWVCLGV
TYSYSHPTGKSCIFYLIGRNPYSWCLEWDSLKFSVWHNNIQTVVHGSYYKTIGVLLDYAAGSLTFYGVAN
TMNLIYRFLTTFTEPLYPAVMVSSGASVTLKQ
>gnl|CDD|293973 cd13738, SPRY_PRY_TRIM14, PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14). This is a TRIM14 domain family contains residues in the N-terminus that form a distinct PRY domain structure such that the B30.2 domain consists of PRY and SPRY subdomains. TRIM14 domains have yet to be characterized. These B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. It belongs to Class IV TRIM protein family which has members involved in antiviral immunity at various levels of interferon signaling cascade
PTLEPDTLHPRLRLSDDRLTVSCGWLGTLGLCPPQRFDKLWQVLSRDSFFSGRHYWEVDLQEAGAGWWVG
AAYPSIGRKGDSEAARLGWNRQSWCLKRYDLEYWAFHDGQRSRLRPEDDPDRLGVFLDYEAGILSFYDVT
GGMTHLHTFRATFQEPLYPALRLWEGSISICKL
>gnl|CDD|293974 cd13739, SPRY_PRY_TRIM1, PRY/SPRY domain of tripartite motif-binding protein 1 (TRIM1) or MID2. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM1 (also known as MID2 or midline 2). MID2 and its close homolog, TRIM18 (also known as MID1), both contain a B30.2-like domain at their C-terminus and a single fibronectin type III (FN3) motif between it and their N-terminal RBCC domain. MID2 and MID1 coiled-coil motifs mediate both homo- and heterodimerization, a prerequisite for association of the rapamycin-sensitive PP2A regulatory subunit Alpha 4 with microtubules. Mutations in MID1 have shown to cause Opitz syndrome, a disorder causing congenital anomalies such as cleft lip and palate as well as heart defects
FKLDPKMAHKKLKISNDGLQMEKDESSLKKSHTPERFSGTGCYGAAGNIFIDSGCHYWEVVVGSSTWYAI
GIAYKSAPKNEWIGKNSSSWVFSRCNNNFVVRHNNKEMLVDVPPQLKRLGVLLDYDNNMLSFYDPANSLH
LHTFEVSFILPVCPTFTIWNKSLMILSGLP
>gnl|CDD|293975 cd13740, SPRY_PRY_TRIM7, PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 7 (TRIM7), also referred to as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90). TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. The GNIP gene encodes at least four distinct isoforms of GNIP, of which three (GNIP1, GNIP2, and GNIP3) have the B30.2 domain
ELTLDPDSANPRLILSLDLKSVRLGERAQDLPNHPCRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFG
VARESVRRKGLTPFTPEEGVWALQLNGGQYWAVTSPERTPLSCGHLSRVRVALDLEVGAVSFYAAEDMRH
IYTFRVNFQERVFPLFSVCSTGTYLRIWP
>gnl|CDD|240499 cd13741, SPRY_PRY_TRIM41, PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 41 (TRIM41). TRIM41 (also known as RING finger-interacting protein with C kinase or RINCK) is localized to speckles in the cytoplasm and nucleus, and functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C
DLTLDPDTAHPALLLSPDRRGVRLAERRQEVPEHPKRFSADCCVLGAQGFRSGRHYWEVEVGGRRGWAVG
AARESTHHKEKVGSGGSSVSSGDASSSRHHHRRRRLHLPQQPLLQREVWCVGTNGKRYQAQSSTEQTLLS
PSEKPRRFGVYLDYEAGRLGFYNAETLAHVHTFSAAFLGERVFPFFRVLSKGTRIKLCP
>gnl|CDD|293976 cd13742, SPRY_PRY_TRIM72, PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM72. Muscle-specific TRIM72 (also known as Mitsugumin 53 or MG53) has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. It is expressed specifically in skeletal muscle and heart, and tethered to the plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. TRIM72 interacts with dysferlin, a sarcolemmal protein whose deficiency causes Miyoshi myopathy (MM) and limb girdle muscular dystrophy type 2B (LGMD2B); this coordination plays an important role in the repair of sarcolemma damage
RKMFRALMPALENLTFDPDTAHPYLVVSSDGKRVECADQKQAVSSDDPNRFDKANCVVSHQSFSEGEHYW
EVIVGDKPRWALGVISAEAGRKGRLHALPSNGFWLLGCKEGKVYEAHVEHKEPRALRVEGRPTRIGVYLS
FSDGVLSFYDASDEDNLVQLFAFHERFPGPLYPFFDVCWHDKGKNSQPLKIF
>gnl|CDD|293977 cd13743, SPRY_PRY_TRIM50, PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM50. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23. It is specifically expressed in gastric parietal cells and may play an essential role in tubulovesicular dynamics. It also interacts with and increases the level of p62, a multifunctional adaptor protein that is implicated in various cellular processes such as the autophagy clearance of polyubiquitinated protein aggregates
KRLHRKVLPAPELLKLDPLTAHPMLELSKGNTVVECGLLAQRLPSNPERFDYSNCVLASRGFSSGKHYWE
VVVGSKSKWRLGLIKGTTSRKGKLNKSPENGVWLIGLKEGRVYEAFANPRVPLPLSTRPQRIGVFLDYEK
GELTFYNADSPDELVPIYTFQAEFQGKLYPLLDVCWHERGANKLPIILP
>gnl|CDD|293978 cd13744, SPRY_PRY_TRIM62, PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM62. It is also called DEAR1 ductal epithelium (associated RING chromosome 1) and is involved in the morphogenesis of the mammary gland; loss of TRIM62 gene expression in breast is associated with increased risk of recurrence in early-onset breast cancer and thus, making TRIM62 a predictive biomarker. Non-small cell lung cancer lesions show a step-wise loss of TRIM62 levels during disease progression, indicating that it may play a role in the evolution of lung cancer. Decreased levels of TRIM62 also represent an independent adverse prognostic factor in AML
KSLFQDIHPVPAALTLDPVTAHQRLILSDDCTIVAYGNLHPQPLQDSPKRFDVEVSVLGSEGFSGGVHYW
EVVVSEKTQWMIGLAHEAVSRKGSIQIQPGRGFYCIVMHDGNQYSACTEPWTRLNVKSKLEKVGVYLDYD
KGLLIFYNADDMSWLYTFREKFPGKLCSYFSPGQSHANGKNVQPLRIN
>gnl|CDD|293979 cd13745, SPRY_PRY_TRIM39, PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of pyrin, several tripartite motif-containing proteins (TRIMs), including E3 ubiquitin-protein ligase (TRIM21), RET finger protein (RFP)/tripartite motif protein 27 (TRIM27), as well as butyrophilin (Btns) and butyrophilin-like (Btnl) family members, with the exception of Btnl2. Btn and Btnl family members are novel regulators of immune responses, with many of the genes located within the MHC. They are implicated in T-cell inhibition and modulation of epithelial cell-T cell interactions. TRIM21 (also known as RO52, SSA1 or RNF81) is a major autoantigen in autoimmune diseases such as rheumatoid arthritis, systemic lupus erythematosus, and Sjorgen's syndrome. TRIM27 (also known as Ret finger protein, RFP or RNF76) negatively regulates CD4 T-cells by ubiquitinating and inhibiting the class II phosphatidylinositol 3 kinase C2beta (PI3K-C2beta), a kinase critical for KCa3.1 channel activation. The PRY/SPRY domain of Pyrin, which is mutated in familial Mediterranean fever patients, interacts with inflammasome components and inhibits proIL-1beta processing
FAVDVTLDPDTAHPNLVLSEDRKSVRHGDTRQDLPDNPERFDTYPCVLGAEGFTGGRHYWEVEVGDKTEW
TLGVCRESVSRKGEVTLSPENGYWTVWLRDGKYEALTSPPTPLPVSVRPSRVGIFLDYEAGEVSFYNVTD
RSHLFTFTDTFSGTLRPYFYPGLNAGGKNAAPLIICP
>gnl|CDD|259839 cd13746, Sir4p-SID_like, The SID domain of Saccharomyces cerevisiae silent information regulator 4, a Sir2p interaction domain; and related domains. Saccharomyces cerevisiae Sir2p, Sir3p, and Sir4p form a heterotrimeric complex which binds chromatin and represses transcription at the homothallic mating type (HM) loci and at subtelomeric regions. This domain model spans residues 742-893 of Sir4p. Sir4p forms a stable heterodimer with Sir2p, mediated by Sir4p residues included in this domain, and a pocket between Sir2p's catalytic domain and its non-conserved N-terminus. Sir4p also interacts with an array of additional factors, including Yku80p, a subunit of the telomeric Ku complex (Yku70p-Yku80p), which binds two sites within Sir4p, one at the N-terminus and one in the C-terminal residues, 731-1358. Other interaction factors include Esc1p (Establishes silent chromatin 1) which binds the Sir4p PAD domain (partitioning and anchoring domain, residues 950-1262), and Sir3p, Yku70p, and Rap1p (Repressor Activator Protein) which bind in its C-terminal coiled-coil (residues 1257-1358). Other Sir4p interacting factors include the Ty5 retrotransposon. Additional roles for Sir4p include roles in DNA repair, and in aging. A SIR4 mutant having a truncated Sir4p lacking a C-terminal coiled-coil domain, has an extended mean life span; deletion of the SIR4 gene leads to a decreased mean life span
TSTGKMEIIYLSDSDDESSDSDDPELERKKIDRELEKYVNKKLADKKTYDKSTIIDLIESGIATHTPLSS
DPKVSVTNNICSVNNYESSHAFYYQQLHKRDRLEYLPLYEPLTPE
>gnl|CDD|259834 cd13747, UreI_AmiS_like_1, UreI/Amis family, subgroup 1. Putative proton-gated urea channel and putative amide transporters. This subfamily includes putative UreI proton-gated urea channels and putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity
GLVLLYVGAVLFLNGLWLLGKIDDKEVAVINLFVGILTFIVALYLAFVHGADAISIKAGALTLLFSFTYL
WVAINRRVNVDGRGLGWYCLFVALTAVPVAINALAGATGDWDIWLGFNWAAWAVLWFLYFLLLVLGRPIQ
RITGYFTILVGIFTGWIPGLLLLQGYW
>gnl|CDD|259840 cd13748, CBM29_CBM65, family 29 and family 65 carbohydrate binding modules. Members of this family bind to polysaccharides that are components of plant cell walls. CBM29 is present in cell-wall degrading multi-enzyme complexes from the anaerobic fungus Piromyces equi, CBM65 can be found in endoglucanases expressed by Eubacterium cellulosolvens and has a preference for xyloglucans
GSMHINFQEWDYGAASLKPNYGSFPNKGGEIKVDYKGEADIVLIVARWEHGKADEWFQVSPYYVSDVDGT
YVFTVDQIAPFDRIDVQDLPSNGDGITVTKIVHSTG
>gnl|CDD|259796 cd13749, Zn-ribbon_TFIIS, domain III/zinc ribbon domain of Transcription Factor IIS. TFIIS is a zinc-containing transcription factor. It has been shown in vitro to have distinct biochemical activities, including binding to RNA polymerases, stimulation of transcript elongation, and activation of a nascent RNA cleavage activity in the RNA polymerase II (Pol II) elongation complex. TFIIS consists of three domains. Domain II and III are sufficient for all known TFIIS activities. Domain III is a zinc ribbon that separated from domain II by a long linker and is indispensable for TFIIS function. The TFIIS homologs, subunits A12.2, B9, and C11, of Pol I, II, and III respectively, are required for RNA cleavage by the polymerases. In a single organism, there are tissue-specific TFIIS related proteins
EGTTTDLFKCGKCKKRKCTYYQLQTRSADEPMTTFVTCLNCGNRWKF
>gnl|CDD|381628 cd13750, TGF_beta_GDNF_like, transforming growth factor beta (TGF-beta) like domain found in the glial cell-line-derived neurotrophic factor (GDNF) family of ligands. GDNF family of ligands includes GDNF, Artemin, Neurturin, and Persephin. They plays an important role in the development and maintenance of the central and peripheral nervous system, renal morphogenesis, and spermatogenesis
GCVLRELHLRVTDLGLGYASEEEVIFRYCAGSCEAARTNYDLILANLRGWRRLRSDRKVGQPCCRPTAYD
DDVSFLDDNSRYHILRKLSAKACGC
>gnl|CDD|381629 cd13751, TGF_beta_GDF8_like, transforming growth factor beta (TGF-beta) like domain found in growth/differentiation factors, GDF8 and GDF11, and similar proteins. The family includes GDF8 and GDF11. GDF8, also termed myostatin, acts specifically as a negative regulator of skeletal muscle growth. GDF11, also termed bone morphogenetic protein 11 (BMP-11), is a secreted signal that acts globally to specify positional identity along the anterior/posterior axis during development
TRCCRYPLTVDFEEFGWDWIIAPKTYDANYCSGECPFVYLQSYPHTHLVQQANPRGSAGPCCTPTKMSPL
SMLYFDEDGNIIYGTLPDMVVERCGC
>gnl|CDD|381630 cd13752, TGF_beta_INHB, transforming growth factor beta (TGF-beta) like domain found in inhibin beta A chain (INHBA), B chain (INHBB), C chain (INHBC), E chain (INHBE) and similar proteins. The family includes inhibin beta A chain (INHBA), B chain (INHBB), C chain (INHBC), and E chain (INHBE). INHBA, also termed activin beta-A chain, or erythroid differentiation protein (EDF), is a component of inhibin A, activin A, or activin AB. Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. INHBB, also termed activin beta-B chain, is a component of inhibin B, activin A, or activin AB. Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. INHBC, also termed activin beta-C chain, might play important roles in carcinogenesis. It may function as a negative regulator of liver growth. INHBE, also termed activin beta-E chain, is a possible insulin resistance-associated hepatokine with hepatic gene expression that positively correlated with insulin resistance and body mass index in humans. It also acts as a possible new marker for drug-induced endoplasmic reticulum stress
CCRESFYVSFTDIGWDDWIIAPSGYYANYCKGSCSGSSSPFRSHHTTILQKYLSKNKAKSELTPCCTPTK
MSPLSLLYYDSDGNIVKKDLPNMIVESCGC
>gnl|CDD|381631 cd13753, TGF_beta_TGFbeta1_2_3, transforming growth factor beta (TGF-beta) like domain found in transforming growth factor beta-1 (TGF-beta-1), beta-2 (TGF-beta-2), beta-3 (TGF-beta-3) and similar proteins. The family includes TGF-beta-1, TGF-beta-2 and TGF-beta-3, which are polypeptide members of the transforming growth factor beta superfamily of cytokines. TGF-beta-1 is a secreted protein that performs many cellular functions, including the control of cell growth, cell proliferation, cell differentiation, and apoptosis. TGF-beta-2 is a secreted protein that performs many cellular functions and has a vital role during embryonic development. It can suppress the effects of interleukin-2 dependent T-cell growth. TGF-beta-3 is involved in embryogenesis and cell differentiation. It regulates molecules involved in cellular adhesion and extracellular matrix (ECM) formation during the process of palate development
CCLRPLYINFRRDLGWKWIHEPKGFNANYCAGACPYLWSADTQHSTVLQLYNRLNPVASAAPCCSPRELE
PLTILYYDGRNPKIETLSNMIVTSCKC
>gnl|CDD|381632 cd13754, TGF_beta_INHA, transforming growth factor beta (TGF-beta) like domain found in inhibin alpha chain (INHA) and similar proteins. INHA is a component of inhibins (inhibin A or inhibin B) that inhibit the secretion of follitropin by the pituitary gland
NCHRASLNISFEELGWGNWIVHPSSFTFHYCHGTCSSSHGLTPALGIQLCCAAVPGTMRSLRVRTTSDGG
YSFKYETVPNILTQDCACI
>gnl|CDD|381633 cd13755, TGF_beta_maverick, transforming growth factor beta (TGF-beta) like domain found in Drosophila melanogaster maverick and similar proteins. Maverick, also termed MAV, is a novel member of the TGF-beta superfamily in Drosophila. It's a bone morphogenetic protein (BMP)/TGF-beta related ligand
TKKCCRHSLKVDFKKLPGFEWIIQPKEFDAGYCKGRCPPRYNYANNHALIQSLLRRMKKKVPRPCCAPSK
LESLEVLHYDESDSSKLKVTKWKGMIVSECAC
>gnl|CDD|381634 cd13756, TGF_beta_BMPs_GDFs, transforming growth factor beta (TGF-beta) like domain found in the BMP/GDF family. The BMP/GDF family consists of bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and similar proteins. BMPs are a group of growth factors also known as cytokines and as metabologens. They induce the formation of bone and cartilage and functions as pivotal morphogenetic signals, orchestrating tissue architecture throughout the body. GDFs have functions predominantly in development
CRRRPLYVDFSDLGWDDWIIAPKGYNANYCAGSCPFPLSSHANATNHAILQALLHSLNPKKSVPKPCCVP
TKYSPLSVLYYDEDGNVVLKTYPDMVVEECGC
>gnl|CDD|381635 cd13757, TGF_beta_AMH, transforming growth factor beta (TGF-beta) like domain found in anti-Muellerian hormone (AMH) and similar proteins. AMH, also termed Muellerian-inhibiting factor, or Muellerian-inhibiting substance (MIS), is a glycoprotein that causes regression of the Muellerian duct. It can also inhibit the growth of tumors derived from tissues of Muellerian duct origin
YCRLRELSVSLRSEKFILSPKRYNINNCQGPCRFPLSDRPRYNNHAVLLLKMQERGLPLQRAPCCVPVAY
EELLVVELSDEGTEISLKPNMVATECGCR
>gnl|CDD|381636 cd13758, TGF_beta_LEFTY1_2, transforming growth factor beta (TGF-beta) like domain found in left-right determination factor 1 (lefty-1), factor 2 (lefty-2) and similar proteins. Lefty-1, also termed left-right determination factor B, or protein lefty-B, is required for left-right axis determination as a regulator of Lefty-2 and NODAL. Lefty-2, also termed endometrial bleeding-associated factor, or left-right determination factor A, or protein lefty-A, or transforming growth factor beta-4 (TGF-beta-4), is required for left-right (L-R) asymmetry determination of organ systems in mammals. It may play a role in endometrial bleeding
TCCRQEYYIDFRELTWTDYWIIEPPGYQAYECVGGCPQPPPPLAWPSLGHRQCGVSESASLPMMYLVKKG
DYTEVEVAEFPNMIVEKCGC
>gnl|CDD|381637 cd13759, TGF_beta_NODAL, transforming growth factor beta (TGF-beta) like domain found in Nodal (NODAL)-related proteins. NODAL is essential for mesoderm formation and axial patterning during embryonic development
SLCRRVDFYVDFDRIGWGSWIVYPKKYNAYRCEGECPSPVDEDFKPTNHAYMQSLLKLYQPDRVPLPCCV
PTKLSPLSMLYYEHGEVVVRHHEDMIVEECGCR
>gnl|CDD|381638 cd13760, TGF_beta_BMP2_like, transforming growth factor beta (TGF-beta) like domain found in bone morphogenetic protein 2 (BMP-2), 4 (BMP-4) and similar proteins. The family includes BMP2 and BMP4 (also known as BMP2B), both of which induce cartilage and bone formation. BMP-2 stimulates the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A- ATF4 pathway. BMP-4 acts in mesoderm induction, tooth development, limb formation and fracture repair
CRRHSLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNPGAVPKACCVPT
ELSPISMLYLDEYDKVVLKNYQDMVVEGCGCR
>gnl|CDD|381639 cd13761, TGF_beta_BMP5_like, transforming growth factor beta (TGF-beta) like domain found in bone morphogenetic proteins BMP-5, BMP-6, BMP-7, BMP-8A/B and similar proteins. The family includes BMP-5, BMP-6, BMP-7 and BMP-8A/B, which may induce cartilage and bone formation
SCRRHNLYVDFRDLGWQDWIIAPDGYNAYYCSGECSFPLNSHMNATNHAIVQTLVHLMNPNRVPKPCCAP
TKLSPISVLYYDDNSNVVLKKYKNMVVESCGCH
>gnl|CDD|381640 cd13762, TGF_beta_GDP9_9B_like, transforming growth factor beta (TGF-beta) like domain found in growth/differentiation factor 9 (GDF-9), growth/differentiation factor 9B (GDF-9B) and similar proteins. The family includes GDF-9B (also known as BMP15) and GDF9. GDF-9B acts as oocyte-specific growth/differentiation factor that stimulates folliculogenesis and granulosa cell (GC) growth. GDF-9 is required for ovarian folliculogenesis. It promotes primordial follicle development and stimulates granulosa cell proliferation
NICRRHRLRVRFRDLKWNGWIIAPTRYTANYCKGTCPRVLGQDLNPTNHAIVQNILHHLLDKSVPRPSCV
PTELHPLSVLYYEEDGSIIYKEYPDMVASSCGCR
>gnl|CDD|381641 cd13763, TGF_beta_BMP3_like, transforming growth factor beta (TGF-beta) like domain found in bone morphogenetic protein 3 (BMP-3), growth/differentiation factor 10 (GDF10) and similar proteins. The family includes BMP-3 (also known as BMP-3A or osteogenin) and GDF10 (also known as BMP-3B). BMP-3 negatively regulates bone density. It antagonizes the ability of certain osteogenic BMPs to induce osteoprogenitor differentitation and ossification. GDF10 is a growth factor involved in osteogenesis and adipogenesis
CSRRPLTVDFADIGWSDWIISPKSFDAYYCAGSCPFPLTKELRPSNHATIQSIVHAVGIQPGVPAPCCVP
DKMSSLTLLYFDENRNVVLKNYPNMTVESCACR
>gnl|CDD|381642 cd13764, TGF_beta_GDF1_3_like, transforming growth factor beta (TGF-beta) like domain found in embryonic growth/differentiation factor 1 (GDF1), factor 3 (GDF3) and similar proteins. The family includes GDF-1 and GDF-3. GDF1 may mediate cell differentiation events during embryonic development. GDF3 is a growth factor involved in early embryonic development and adipose-tissue homeostasis. The family also contains protein DVR-1, also termed vegetal hemisphere VG1 protein (VG-1), which serves to facilitate the differentiation of either mesoderm or endoderm either as a cofactor in an instructive signal or by providing permissive environment
CKKRRLYISFRDVGWQNWIIAPQGYMANYCHGECPFPLTESLNGTNHAILQTLVHSVDPEGTPQPCCVPT
RLSPISMLYYDNNDNVVLRHYEDMVVDECGCR
>gnl|CDD|381643 cd13765, TGF_beta_ADMP, transforming growth factor beta (TGF-beta) like domain found in anti-dorsalizing morphogenetic protein (ADMP) and similar proteins. ADMP is a bone morphogenetic protein (BMP)-like transforming growth factor beta ligand, functions in the trunk organizer to antagonize head formation, thereby regulating organizer patterning. It negatively affects the formation of the organizer, although it is robustly expressed within the organizer itself. The organizer-promoting signal of ADMP is mediated by the activin A type I receptor, ACVR1 (also known as activin receptor-like kinase-2, ALK2)
RSCQRHELYVDFEEIGWSGWIISPKGYNAYHCKGSCPFPLGQNQKPTNHATVQSIVHALKLAKGVEMPCC
VPDKLYSISLLYFDDDENVVLKQYDDMVAASCGCH
>gnl|CDD|381644 cd13766, TGF_beta_GDF5_6_7, transforming growth factor beta (TGF-beta) like domain found in growth/differentiation factor 5 (GDF5), factor 6 (GDF6), factor 7 (GDF7) and similar proteins. The family includes GDF5, GDF6 and GDF7. GDF5, also termed bone morphogenetic protein 14 (BMP-14), or cartilage-derived morphogenetic protein 1 (CDMP-1), or lipopolysaccharide-associated protein 4 (LAP-4), or LPS-associated protein 4, or radotermin, is a growth factor involved in bone and cartilage formation. GDF6, also termed bone morphogenetic protein 13 (BMP-13), or growth/differentiation factor 16, is a growth factor that controls proliferation and cellular differentiation in the retina and bone formation. GDF7, also termed bone morphogenetic protein 12 (BMP-12), may play an active role in the motor area of the primate neocortex
CSRKPLHVNFKDLGWDDWIIAPLDYEAYHCEGVCDFPLRSHLEPTNHAIIQTLMNSMDPESTPPSCCVPT
KLSPISILYIDSANNVVYKQYEDMVVESCGCR
>gnl|CDD|381645 cd13767, TGF_beta_BMP9_like, transforming growth factor beta (TGF-beta) like domain found in bone morphogenetic proteins, BMP-9, BMP-10 and similar proteins. The family includes BMP9 (also known as GDF2) and BMP10. BMP-9 is a potent circulating inhibitor of angiogenesis. It signals through the type I activin receptor ACVRL1 but not other activin receptor-like kinases (ALKs). BMP-10 is required for maintaining the proliferative activity of embryonic cardiomyocytes by preventing premature activation of the negative cell cycle regulator CDKN1C/p57KIP and maintaining the required expression levels of cardiogenic factors such as MEF2C and NKX2-5. It inhibits endothelial cell migration and growth. It may reduce cell migration and cell matrix adhesion in breast cancer cell lines
NSCRRKPLYVNFADIGWDSWIIAPKGYEAYECSGKCFFPLADHLSPTKHAIIQTLVHSKSPEKVSRACCV
PTKLEPISLLYIDENGVLTYKYKYEGMVVAECGCR
>gnl|CDD|259841 cd13768, DSS1_Sem1, proteasome complex subunit DSS1/Sem1. The evolutionarily conserved deleted in split hand/split foot protein 1 (DSS1)/Sem1 is a subunit of the regulatory particle (RP) of the proteasome. It is implicated in ubiquitin-mediated proteolysis, is required for the maintenance of genomic stability, and functions in DNA damage response. DSS1/Sem1 also displays RP-independent functions; it serves as a functional component of the nuclear pore associated TREX-2 transcription-export complex and is required for proper nuclear export of mRNA. In mammalian cells, DSS1 binds and stabilizes the tumor suppressor BRCA2, and contributes to its function in mediating homologous recombinational repair. In yeast, Sem1 also complexes with the COP9 signalosome, which is involved in de-neddylation. DSS1/Sem1 may be a versatile protein which contributes to the functional integrity of multiple protein complexes involved in various biological processes
VDLGALEEDDEFEEFPVEDWTDEETEENSAEEDEHLWEDNWDDDDVEDDFSKQLRAELEKK
>gnl|CDD|259842 cd13769, ApoLp-III_like, Apolipophorin-III and similar insect proteins. Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity
TQLSELIQKAQEAINNLAQQVQKQLGLQNPEEVVNTLKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAW
NEFKTKLSETVPELRKSLPVEEKAQELQAKLQSGLQTLVTESQKLAKAISENSQKAQEELQKATKQAYDI
AVEAAQNLQNQLQTATQK
>gnl|CDD|259817 cd13775, SPFH_eoslipins_u3, Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of the SPFH family (stomatin, prohibitin, flotillin, and HflK/C). This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized
VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAEL
LSRREQIDEELQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEM
FVEAAEVYENNPIALQLRAMNMLYEGLKEKGSMVVVP
>gnl|CDD|260099 cd13777, Aar2_N, N-terminal domain of Aar2, a U5 small nuclear ribonucleoprotein particle assembly factor. This family consists of the N-terminal domain of eukaryotic Aar2 and Aar2-like proteins. Aar2 is a U5 small nuclear ribonucleoprotein (snRNP) particle assembly factor and part of Prp8, which forms a large complex containing U5 snRNA, Snu114, and seven Sm proteins (B, D1, D2, D3, E, F and G). Upon import of the complex into the nucleus, Aar2 phosphorylation leads to its release from Prp8 and replacement by Brr2p, thus playing an important role in Brr2p regulation and possibly safeguarding against non-specific RNA binding to Prp8. Aar2p binds directly with the RNaseH-like domain in the C-terminal region of Prp8p. In yeast, Aar2 protein is involved in splicing pre-mRNA of the a1 cistron and other genes important for cell growth
ATLLLLDLPEGTEFGIDLQSFTVGPRFKGIKMIPPGIHFIHYSSDSSEGSSPRYGFFFNFKPGEVIVRKW
DPEFEDLVEEPDSDEELERLRANLKEDQYLGPYPYEDSKDWKSLTSYITEEVLSRL
>gnl|CDD|260100 cd13778, Aar2_C, C-terminal domain of Aar2, a U5 small nuclear ribonucleoprotein particle assembly factor. This family consists of the C-terminal domain of eukaryotic Aar2 and Aar2-like proteins. Aar2 is a U5 small nuclear ribonucleoprotein (snRNP) particle assembly factor and part of Prp8, which forms a large complex containing U5 snRNA, Snu114, and seven Sm proteins (B, D1, D2, D3, E, F and G). Upon import of the complex into the nucleus, Aar2 phosphorylation leads to its release from Prp8 and replacement by Brr2p, thus playing an important role in Brr2p regulation and possibly safeguarding against non-specific RNA binding to Prp8. Aar2p binds directly with the RNaseH-like domain in the C-terminal region of Prp8p. In yeast, Aar2 protein is involved in splicing pre-mRNA of the a1 cistron and other genes important for cell growth
ELRFTFIPLKRTWPGATGRERTRHSLDKSWYLEEVLLKSYNGDERELLGELQFAFLLFLLLGNYSSFEQW
KNLLELLCSSAEALKKRPSLFLKFLKTLHAQLKYLPEDFFVDLLLNDNFLKRLLSELLENLGDSEVDTPL
KKAVKRLKRLLEEKF
>gnl|CDD|260101 cd13783, SPACA1, Sperm acrosome membrane-associated protein 1. SPACA1 (aka SAMP32, due to its 32kDa M.W.) is localized to the acrosome of spermatozoa. The acrosome is an organelle transformed from the Golgi apparatus to form a cap over the anterior portion of the spermatozoa head, which contains the sperm nucleus. Mammalian acrosomes contain digestive enzymes that degrade the ovum outer membrane (zona pellucida) to allow fusion of the sperm and ovum nuclei via the acrosomal reaction. In mammals, the acrosome releases hyaluronidase and acrosin. Antibodies generated against recombinant SPACA1 have been shown to inhibit human sperm binding and membrane fusion in vitro vs. zona-free hamster ova. Male mice lacking SPACA1 are infertile, and exhibit globozoospermia-like misformed sperm heads. SPACA1 content has been reported to be diminished in a comparison of round-headed vs normal spermatozoa
NVTALQDDVQLAEEASEEEGEEEEENESEVPENPTEAEAEEEVSNRTVVKEVEFGMCTVTCGIGIREVIL
TNGCPGGESKCVVRVEECRGPVDCGWGKPISESLSSVRLACIHISPENRFKYVWKLLRPDQQAVILPNDS
AVLEVHRETHPVAFECDTLDNNEIVASVKFTVYTTSELQMRRSSRPDTDAVLIFVLTIGVIICIFVIFVL
IFIIINWAAVKSFWGSKASTTEIQSELSSMRYKDSTSL
>gnl|CDD|260102 cd13784, SP_1775_like, Uncharacterized protein conserved in Streptococci. Streptococcus pneumoniae SP_1775 and related proteins from other Streptococci; may form homooctamers that may bind hydrophobic ligands
IEITYLDAYKQERTVTFENYEEFERAQSGCVTDLPDYYPVTSVTYKGKDLDYTGTYGDLYFFLLKFD
>gnl|CDD|260079 cd13785, CARD_BinCARD_like, BinCARD (Bcl10-interacting protein with CARD). BinCARD was ubiquitously expressed CRAD (Caspase activation and recruitment domain) protein in all tissues. CARD proteins play important role in apoptosis by functioning as direct regulators of death-inducing caspases. BinCARD interacts with apoptosis inducer CARD protein Bcl10 through CARD. It inhibits Bcl10-mediated activation of NF-kappa B and to suppress Bcl10 phosphorylation. Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. In general, DDs domains are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes
LLQDTPFLTSDGRLSEQLVDRIILQLNRVYPQILTNKEAEKFRNPKAPLRVRLADLLKHLQRKGERDCQE
FYRALHIHAEPLYSDL
>gnl|CDD|259853 cd13831, HU, histone-like DNA-binding protein HU. This subfamily includes HU and HU-like domains. HU is a conserved nucleoid-associated protein (NAP) which binds non-specifically to duplex DNA with a particular preference for targeting nicked and bent DNA. It is highly basic and contributes to chromosomal compaction and maintenance of negative supercoiling, thus often referred to as histone-like protein. HU can induce DNA bends, condense DNA in a fiber and also interact with single stranded DNA. It contains two homologous subunits, alpha and beta, typically forming homodimers (alpha-alpha and beta-beta), except in E. coli and other enterobacteria, which form heterodimers (alpha-beta). In E. coli, HU binds uniformly to the chromosome, with a preference for damaged or distorted DNA structures and can introduce negative supercoils into closed circular DNA in the presence of topoisomerase I. Anabaena HU (AHU) shows preference for A/T-rich region in the center of its DNA binding site
NKAELIDAVAEKAGLSKKDAEKALDAVLETITEALKKGEKVTLVGFGTFEVRERAARTGRNPQTGEKIKI
PASKVPKFKPGKALKD
>gnl|CDD|259854 cd13832, IHF, Integration host factor (IHF) and similar proteins. This subfamily includes integration host factor (IHF) and IHF-like domains. IHF is a nucleoid-associated protein (NAP) that binds and sharply bends many DNA targets in a sequence specific manner. It is a heterodimeric protein composed of two highly homologous subunits IHFA (IHF-alpha) and IHFB (IHF-beta). It is known to act as a transcription factor at many gene regulatory regions in E. coli. IHF is an essential cofactor in phage lambda site-specific recombination, having an architectural role during assembly of specialized nucleoprotein structures (snups). IHF is also involved in formation as well as maintenance of bacterial biofilms since it is found in complex with extracellular DNA (eDNA) within the extracellular polymeric substances (EPS) matrix of many biofilms. This subfamily also includes the protein Hbb from tick-borne spirochete Borrelia burgdorferi, responsible for causing Lyme disease in humans. Hbb, a homodimer, shows DNA sequence preferences that are related, yet distinct from those of IHF
KADLIEEIAEKTGLSKKDVKKVVDAFFDEIKEALKEGERVELRGFGTFEVKKRKARIGRNPKTGEKIVIP
ARKVVKFKPSKELKE
>gnl|CDD|259855 cd13833, HU_IHF_like, Uncharacterized proteins similar to DNA sequence specific (IHF) and non-specific (HU) domains. This subfamily consists of uncharacterized proteins similar to integration host factor (IHF) and HU domains, including hypothetical protein Bvu_2165 from Bacteroides vulgatus. IHF is a nucleoid-associated protein (NAP) that binds and sharply bends many DNA targets in a sequence specific manner. It is a heterodimeric protein composed of two highly homologous subunits IHFA (IHF-alpha) and IHFB (IHF-beta). It is known to act as a transcription factor at many gene regulatory regions in E. coli. IHF is an essential cofactor in phage lambda site-specific recombination, having an architectural role during assembly of specialized nucleoprotein structures (snups). IHF is also involved in formation as well as maintenance of bacterial biofilms since it is found in complex with extracellular DNA (eDNA) within the extracellular polymeric substances (EPS) matrix of many biofilms
DYIARVVRTGSLDLEDIIDRIVAKGSTLRAETIEHILELFDKVVSEALQEGYSVNTGLGYLYIAISGVFE
GETDSFDPAKHSITVSFTPGKLLREAL
>gnl|CDD|259856 cd13834, HU_like, DNA-binding proteins similar to HU domains. This subfamily consists of DNA-binding proteins similar to HU domains. HU is a conserved nucleoid-associated protein (NAP) which binds non-specifically to duplex DNA with a particular preference for targeting nicked and bent DNA. It is highly basic and contributes to chromosomal compaction and maintenance of negative supercoiling, thus often referred to as histone-like protein. HU can induce DNA bends, condense DNA in a fiber and also interact with single stranded DNA. It contains two homologous subunits, alpha and beta, typically forming homodimers (alpha-alpha and beta-beta), except in E. coli and other enterobacteria, which form heterodimers (alpha-beta)
TKSQLINALAEATGLSKKDVKAVLDSLEELITKELKKKGPGEFTLPGLLKIKVVKKPATKARKGRNPFTG
EEMTFKAKPASKVVKVRPLKKLKD
>gnl|CDD|259857 cd13835, IHF_A, Alpha subunit of integration host factor (IHFA). This subfamily consists of the alpha subunit of integration host factor (IHF) and IHF-like domains. IHF is a nucleoid-associated protein (NAP) that binds and sharply bends many DNA targets in a sequence specific manner. It is a heterodimeric protein composed of two highly homologous subunits IHFA (IHF-alpha) and IHFB (IHF-beta). It is known to act as a transcription factor at many gene regulatory regions in E. coli. IHF is an essential cofactor in phage lambda site-specific recombination, having an architectural role during assembly of specialized nucleoprotein structures (snups). IHF is also involved in formation as well as maintenance of bacterial biofilms since it is found in complex with extracellular DNA (eDNA) within the extracellular polymeric substances (EPS) matrix of many biofilms
TKADLAEAIYEKLGLSRKEAAELVESVFEEIKEALERGEDVKISGFGTFEVRDKKARPGRNPKTGEEVTI
SARRVVTFKPSPKLKKRI
>gnl|CDD|259858 cd13836, IHF_B, Beta subunit of integration host factor (IHFB). This subfamily consists of the beta subunit of integration host factor (IHF) and IHF-like domains. IHF is a nucleoid-associated protein (NAP) that binds and sharply bends many DNA targets in a sequence specific manner. It is a heterodimeric protein composed of two highly homologous subunits IHFA (IHF-alpha) and IHFB (IHF-beta). It is known to act as a transcription factor at many gene regulatory regions in E. coli. IHF is an essential cofactor in phage lambda site-specific recombination, having an architectural role during assembly of specialized nucleoprotein structures (snups). IHF is also involved in formation as well as maintenance of bacterial biofilms since it is found in complex with extracellular DNA (eDNA) within the extracellular polymeric substances (EPS) matrix of many biofilms
MTKSELIKRIAEKTPGLSKKDVEAVVDAILDEIKEALARGERIEIRGFGSFSVKKRKARIGRNPKTGEKV
VVPAKYVPHFKPGKELKER
>gnl|CDD|260013 cd13838, RNase_H_like_Prp8_IV, Ribonuclease-like Prp8 domain IV core. This family contains Prp8 domain IV, which adopts a RNase H like fold within its core structure but with little sequence similarity. Prp8, a spliceosome protein, interacts directly with the splice sites and branch regions of precursor-mRNAs and spliceosomal RNAs associated with catalysis of the two steps of splicing. Catalysis of RNA cleavage by RNase H-like proteins involves a two-metal mechanism in which adjacently-bound divalent magnesium ions promote hydrolysis by activation of a water nucleophile and stabilization of the transition-state. However, the Prp8 domain IV contains only one of the canonical metal-binding sites and the coordinating side chains are spatially conserved with respect to Mg2+-coordinating residues within the RNase H fold
QNYGELFSNQIIWFVDDTNVYRVTIHKTFEGNLTTKPINGAIFIFNPRTGQLFLKIIHTSVWAGQKRLGQ
LAKWKTAEEVAALIRSLPVEEQPKQIIVTRKGMLDPLEVHLLDFPNIVIKGSELQLPFQACLKIEKFGDL
ILKATEPQMVLFNLYDDWLKTISSYTAFSRLILILRALHVNNEKAKIILKPDKTVITEPHHIWPTLSDEE
WIKVEVQLKDLILADYGKKNNVNVASLTQSEIRDIILGMEI
>gnl|CDD|260103 cd13839, MEF2_binding, Mycocyte enhancer factor-2 (MEF2) binding domain of the calcineurin-binding protein cabin-1. The myocyte enhancer factor-2 (MEF2) binding domain, as found in the calcineurin-binding protein cabin-1, adopts an amphipathic alpha-helical structure, which allows it to bind to a hydrophobic groove on the MEF2S domain, forming a triple-helical interaction. Interaction of this domain with MEF2 causes repression of transcription. Cabin-1 inhibits calcineurin-mediated signal transduction in T-cell receptor-mediated signalling pathways, by binding to the activated form of calcineurin. Cabin-1 acts as a co-repressor of MEF2, the mycocyte enhancer factor-2, which regulates transcription in a calcium-dependent manner and plays vital roles in T-cell development and function
TLLSPKGSISEETKQKLKNAILSSQSAANVKKDTL
>gnl|CDD|260104 cd13840, SMBP_like, Small metal-binding protein conserved in proteobacteria. This periplasmic protein appears capable of binding multiple equivalents of a variety of divalent and trivalent metals, including Cu(2+) and Fe(3+) but also Mn(2+), Ni(2+), Mg(2+), and Zn(2+). It has been suggested that SMBP is a metal scavenging protein that plays a role in cellular copper management in Nitrosomonas europaea
AEDHLDEAIEHAEAAITHGKAGHAKALAEHAEEALKHAKAAEKEKAEAKKHLDEAIKHLEEAIKHGKMGH
ADVATKHAEEALKHLKAAN
>gnl|CDD|260105 cd13841, ABBA-PTs, ABBA-type aromatic prenyltransferases (PTases). ABBA-type aromatic prenyltransferases (PTases) are a subgroup of prenyltransferases that are characterized by an unusual type of beta/alpha fold with antiparallel beta strands. They lack the (N/D)DxxD motif which is characteristic for many other prenyltransferases. Generally, aromatic prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto aromatic substrates, forming C-C bonds between C-1 or C-3 of the isoprenoid substrate and one of the aromatic carbons of the acceptor substrate by an electrophilic alkylation, or Friedel-Crafts alkylation mechanism
RVAPMLAKMLEVFDVTTYLDKLPPLLEAFLEIYPRGGTPVEFSLNFGRDLSTLRYEFEPNQGTTDPFNLT
PYARSLEKLLSLLKVSPVDELLAAVVEHLTITQNTIALDLGLTGGFVKTYIFPKPEAKTGVEELAGTVRV
PDAVLYNDELLEALGRDDSVXFVGCDLFKPARSRVKLYLAEPGVSMEELKTLGGRLRDLGLAVGSELVRE
FWRLGPLMGAFTLKWGDKIPEPTLYVPTSGIKDLPVKYFEDAETFDRILKSYYSQGDGEGLDAYIAFAYT
PLKTEYLSIYYYYW
>gnl|CDD|259911 cd13842, CuRO_HCO_II_like, Cupredoxin domain of Heme-copper oxidase subunit II. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I
LTVYVTGVQWSWTFIYPNVRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVAD
KPGTYTIICAEYCGLGHSYMLGKVE
>gnl|CDD|259912 cd13843, Azurin_like, Azurin and similar redox proteins. Azurin is a bacterial blue copper-binding protein. It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The copper of Azurin is tetrahedrally coordinated by a cysteine, 2 histidines, and a methionine residue. The electron transfer reactions are carried out with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Azurin can function as tumor suppressor; it forms a complex with p53 that triggers apoptosis in various human cancer cells. Auracyanins A and B are from photosynthetic bacteria. They are very similar blue copper proteins with 38% sequence identity and they are homologous to the bacterial redox protein Azurin. However, auracyanin A is expressed only when C. aurantiacus cells are grown in light, whereas auracyanin B is expressed under dark and in light. Thus, auracyanin A may function as a redox partner in photosynthesis, while auracyanin B may function in aerobic respiration
TVEIGGNDEMQFSKTSITVSASCKEFTVNLKHNGKLPKNVMGHNWVLVKSADAGGVANAGMAAGADNNYL
KPDDSRVIAHTPLIGGGETDSVTFTVSKLEAGEDYTYFCTFPGHFALMKGTLTL
>gnl|CDD|259913 cd13844, CuRO_1_BOD_CotA_like, The first Cupredoxin domain of Bilirubin oxidase (BOD), the bacterial endospore coat component CotA, and similar proteins. Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and it is required for spore resistance against hydrogen peroxide and UV light. Also included in this subfamily are phenoxazinone synthase (PHS), which catalyzes the oxidative coupling of substituted o-aminophenols to produce phenoxazinones. PHS has been shown to participate in diverse biological functions such as spore pigmentation and biosynthesis of the antibiotic grixazone. These are Laccase-like multicopper oxidases (MCOs) that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
GDYYEIEMREFTQQLHPDLPPTTVWGYGGSNSTSYPGPTIEARRGVPVRVTWVNNLPDKHHLPLDDTLPS
TEEATPGAEPPVPPVPTVVHLHGGEVPPESDGYPEAWFTPGGEEGPGFGSATYYYPNDQSAATLWYHDHA
LGITRLNVYAGLAGFYLIRDEA
>gnl|CDD|259914 cd13845, CuRO_1_AAO, The first cupredoxin domain of plant Ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
RHYKWKVEYMFWAPDCVEKLVIGINGQFPGPTIRATAGDTIVVELENKLPTEGVAIHWHGIRQRGTPWAD
GTASVSQCPINPGETFTYQFVVDRPGTYFYHGHYGMQRSAGLYGSLIVDP
>gnl|CDD|259915 cd13846, CuRO_1_AAO_like_1, The first cupredoxin domain of plant Ascorbate oxidase homologs. This subfamily is composed of plant pollen multicopper oxidase homologous to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. This subfamily does not harbor trinuclear copper binding histidines
SFFDWNVSYITASPLGVPQQVIAINGQFPGPTINVTTNDNVVVNVFNSLDEPLLLTWNGIQQRRNSWQDG
VLGTNCPIPPGWNWTYKFQVKDQIGSFFYFPSLHFQRAAGGFGGIRVN
>gnl|CDD|259916 cd13847, CuRO_1_AAO_like_2, The first cupredoxin domain of Ascorbate oxidase homologs. This family includes fungal proteins with similarity to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
PDATLRVSCDPFGPRPSTLINGSFPGPELRVQEGQHLWVRVYNDLEAGNTTMHFHGLSQYMSPFSDGTPL
ASQWPIPPGKFFDYEFPLEAGDAGTYYYHSHVGFQSVTAYGALIVED
>gnl|CDD|259917 cd13848, CuRO_1_CopA, The first cupredoxin domain of CopA copper resistance protein family. CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity, and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
VEYDLVIAETPVNIGGKEGEAITVNGQVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPNDMDGVP
GLSFPGIKPGETFTYRFPVRQSGTYWYHSHSGLQEQTGLYGPIIID
>gnl|CDD|259918 cd13849, CuRO_1_LCC_plant, The first cupredoxin domain of plant laccases. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Plants usually express multiple laccase genes, but their precise physiological/biochemical roles remain largely unclear. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
YTFVVQEKNVTRLCSTKSILTVNGQFPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLRSGWADGPA
YITQCPIQPGQSYTYRFTVTGQEGTLWWHAHISWLRATVYGAFIIRP
>gnl|CDD|259919 cd13850, CuRO_1_Abr2_like, The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
FTLTVTEGSPDGDGGEREVILINGQFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTPWSDGVP
GVTQWPIQPGGSFTYRWKAEDQYGLYWYHSHYRGYYMDGLYGPIYIR
>gnl|CDD|259920 cd13851, CuRO_1_Fet3p, The first Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) and a four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the exocellular space and the carboxyl terminus in the cytoplasm. The periplamic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
VEFDWNITWVTANPDGLFERRVIGINGQWPPPPIEVNKGDTVVIHATNSLGDQPTSLHFHGLFQNGTNYM
DGPVGVTQCPIPPGQSFTYEFTVDTQVGTYWYHSHDGGQYPDGLRGPFIIH
>gnl|CDD|259921 cd13852, CuRO_1_McoP_like, The first cupredoxin domain of multicopper oxidase McoP and similar proteins. This family includes archaeal and bacterial multicopper oxidases (MCOs), represented by the extremely thermostable McoP from the hyperthermophilic archaeon Pyrobaculum aerophilum. McoP is an efficient metallo-oxidase that catalyzes the oxidation of cuprous and ferrous ions. It is noteworthy that McoP has three-fold higher catalytic efficiency when using nitrous oxide as the electron acceptor than when using dioxygen, the typical oxidizing substrate of MCOs. McoP may function as a novel archaeal nitrous oxide reductase that is probably involved in the denitrification pathway in archaea. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
WKYSGKLLKGDPAALQNLPDSYLGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDGHPRYAIDP
GETYVYEFEVLNRAGTYWYHPHPHGLTAKQVYRGLAGLFLVTDE
>gnl|CDD|259922 cd13853, CuRO_1_Tth-MCO_like, The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus. The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
VLEVTLTVEYGRVTLAGLPVTLRTYNGSIPGPTLRVRPGDTLRITLKNDLPPEGAANEAPAPNTPHCPNT
TNLHFHGLHVSPTGNSDNVFLTIAPGESFTYEYDIPADHPPGTYWYHPHLHGSTALQVAGGMAGALVVE
>gnl|CDD|259923 cd13854, CuRO_1_MaLCC_like, The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
GVTRKYTLTITNSTLAPDGVEKEVMLINGQYPGPLIEANWGDTIEVTVINKLQDNGTSIHWHGIRQLNTN
WQDGVPGVTECPIAPGDTRTYRFRATQYGTSWYHSHYSAQYGDGVVGPIVIH
>gnl|CDD|259924 cd13855, CuRO_1_McoC_like, The first cupredoxin domain of a multicopper oxidase McoC and similar proteins. This family includes bacteria multicopper oxidases (MCOs) represented by McoC from pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic multicopper oxidase, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. They are capable of oxidizing a vast range of substrates, varying from aromatic compunds to inorganic compounds such as metals. Most MCOs have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
LFRATLTAAEVRIRLLPGKPTEFWAYNGSVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG
NPHDPVAPGNDRVYRFTLPQDSAGTYWYHPHPHGHTAEQVYRGLAGAFVVK
>gnl|CDD|259925 cd13856, CuRO_1_Tv-LCC_like, The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor. This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
PTYTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTMRRSTSIHWHGIFQHGT
NYADGPAFVTQCPIAPNHSFTYDFTAGDQAGTFWYHSHLSTQYCDGLRGPLVIYD
>gnl|CDD|259926 cd13857, CuRO_1_Diphenol_Ox, The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
REYNFTISEITGAPDGFVRPMLVINGQFPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTNWMDG
TAGITQCPIPPGGSFTYNFTVDGQYGTYWYHSHYSTQYADGLVGPLIVH
>gnl|CDD|259927 cd13858, CuRO_1_tcLCC2_insect_like, The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum. This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi, plants and insects. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
DGVERPVITVNGQLPGPSIEVCEGDTVVVDVKNRLPGESTTIHWHGIHQRGTPYMDGVPMVTQCPILPGQ
TFRYKFKADPAGTHWYHSHSGTQRADGLFGALIVR
>gnl|CDD|259928 cd13859, CuRO_D1_2dMcoN_like, The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins. This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. Its biological function has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals
REFEMTIDETVITVVPGLDFKTFAFNGQVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSWKMD
GVPGVTQPAIEPGESFTYKFKAERPGTLWYHCHVNVNEHVGMRGMWGPLIVD
>gnl|CDD|259929 cd13860, CuRO_1_2dMco_1, The first cupredoxin domain of bacteria two domain multicopper oxidase. This subfamily includes bacterial two domain multicopper oxidases (2dMCOs) with similarity to McoN from Nitrosomonas europaea. 2dMCO is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals
KVFHLVAEPVKWEIAPGVKVEAWGYNGSVPGPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV
PGITQPPIQPGETFTYEFTAKQAGTYMYHSHVDEAKQEDMGLYGAFIVH
>gnl|CDD|259930 cd13861, CuRO_1_CumA_like, The first cupredoxin domain of CumA like multicopper oxidase. This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida, which is involved in the oxidation of Mn(II). However, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCO catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
VEYTLTAAPAELLDLGGPTTRTWGYNGQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV
PGLTQPPVPPGESFTYEFTPPDAGTYWYHPHVGSQEQLDRGLYGPLIVE
>gnl|CDD|259931 cd13862, CuRO_1_MCO_like_1, The first cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
ADVTLRIAPVTVELAPGRTISTLGYNGQVPGPLLRMRQGVSVTVDVFNDTDIPEYVHWHGLPLPADVDGA
MEEGTPSVPPHGHRRYRMTPRPAGFRWYHTHVMTMDDLTRGQYSGLFGFVYIE
>gnl|CDD|259932 cd13864, CuRO_1_MCO_like_2, The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
ETLLIILRISVEYNKDGKQIISINGSNDTIGPTIRVKSGDTLNLLVTNHLCNEQELSKIWQDYCPTSIHF
HGLVLENFGKQLANLVDGVPGLTQYPIGVGESYWYNFTIPEDTCGTFWYHSHSSVQYGDGLRGVFIVDC
>gnl|CDD|259933 cd13865, CuRO_1_LCC_like_3, The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
TVLTVASRTIEVNGKAATVYGIRQPDGTEGLRLTEGDRFDVELENRLDEPTTIHWHGLIPPNLQDGVPDV
TQPPIPPGQSQRYDFPLVQPGTFWMHSHYGLQEQKLLAAPLIIRS
>gnl|CDD|259934 cd13866, CuRO_2_BOD, The second cupredoxin domain of Bilirubin oxidase (BOD). Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. It is used in diagnosing jaundice through the determination of bilirubin in serum. BOD is a member of the multicopper oxidase (MCO) family that also includes laccase, ascorbate oxidase and ceruloplasmin. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
SGDYDIPLVLADKQFDPNGQLMFDEFNLDGLLGDVILVNGVPWPFLNVEPRKYRFRLLNASVSRFFQLAL
VDGDNPTRIPFTVIASDGGLLSHPVETTLLRLGMAERYDIVVDFSKYAAGTRLYLVNRLEHDDGRGPDND
YPATDKVMRFRV
>gnl|CDD|259935 cd13867, CuRO_2_CueO_FtsP, The second Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins. CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the second domain. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
DDIPLILQDRRFDEDGQLDYRMMDDMDGFLGDTLLVNGTINPYLDVPRGWVRLRLLNGSNARTYNLGFSD
NRPFYQIASDGGLLPAPVELKRLLLAPGERAEILVDFSDGEPVSLRSGPDEGGLGMIGFGDSGEDDDFDL
LTLRVG
>gnl|CDD|259936 cd13868, CuRO_2_CotA_like, The second Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat component. CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and it is required for spore resistance against hydrogen peroxide and UV light. Laccase is composed of three cupredoxin-like domains and includes one mononuclear and one trinuclear copper center. It is a member of the multicopper oxidase (MCO) family, which couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
YEIPLLIQDRSFNADGSLFYPATGANPSPHPSWVPEFFGDTIVVNGKAWPYLEVEPRRYRFRILNGSNAR
FYNLSLSNGDGLPFWQIGTDGGFLPKPVPLDSLLIGPAERADVIVDFSDYAGQTLILKNDAPAPYPGGGA
ADPDTTGQVMQFRVA
>gnl|CDD|259937 cd13869, CuRO_2_PHS, The second Cupredoxin domain of phenoxazinone synthase (PHS). Phenoxazinone synthase (PHS, 2-aminophenol:oxygen oxidoreductase) catalyzes the oxidative coupling of substituted o-aminophenols to produce phenoxazinones. PHS participates in diverse biological functions such as spore pigmentation and biosynthesis of the antibiotic grixazone. It is a member of the multicopper oxidase (MCO) family, which couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
EVPLVIRDRNLDTDADGALTGRLLHKLLYKQAGVGTGDAALEIPFTGPYTLVNGVIWPYLEVRPGWYRLR
LLNASNARIYRLALLDETDEHPVPGALVVIGTDAGLLPRPVPVPGGAVNLGPGERADVLVDFAALRGRRL
RLVNESPGALNGQPGQTDPDVMQFRV
>gnl|CDD|259938 cd13870, CuRO_2_CopA_like_1, The second cupredoxin domain of CopA copper resistance protein like family. The members of this family are copper resistance protein (CopA) homologs. CopA is multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. CopA is involved in copper resistance in bacteria. CopA mutant causes a loss of function, including copper tolerance and oxidase activity, and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
TPSGPLGGDAGDVRYPYYLINGRPPEDPAVFTARPGDRLRLRLINAAGDTAFRVALAGHRLTVTHTDGFP
VEPVEVDALLIGMGERYDAIVTANNGIWPLVALPEGKDGQARAVLRY
>gnl|CDD|259939 cd13871, CuRO_2_AAO, The second cupredoxin domain of plant Ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. MCOs couple oxidation of substrates with reduction of dioxygen to water. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
DGELNILLSDWWHKSIYEQETGLSSKPFRWVGEPQSLLIEGRGRYNCSLAPAYPSSLPSPVCNKSNPQCA
PFILHVSPGKTYRLRIASVTALSSLNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTADQDP
SRNYWVSVNVRGRRPNTPPGLAILNY
>gnl|CDD|259940 cd13872, CuRO_2_AAO_like_1, The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate oxidase. The proteins in this subfamily are expressed in plant pollen. They share homology to ascorbate oxidase and other members of the blue copper oxidase family. The expression of the protein is detected during germination and pollen tube growth. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It is a member of the multicopper oxidase (MCO) family that couples oxidation of substrates with reduction of dioxygen to water. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
DEYTVLIGDWYKTDHKTLRQSLDKGRTLGRPDGILINGKGPYGYGANETSFTVEPGKTYRLRISNVGLRT
SLNFRIQGHKMLLVETEGSYTAQNTYDSLDVHVGQSYSVLVTADQSPKDYYIVASSRFLSPELTGVAILH
Y
>gnl|CDD|259941 cd13873, CuRO_2_AAO_like_2, The second cupredoxin domain of plant Ascorbate oxidase homologs. This family includes plant laccases similar to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couples oxidation of substrates with reduction of dioxygen to water. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
EERILLFSDYFPKTDSTIETGLTATPFVWPGEPNALLVNGKSGGTCNKSATEGCTTSCHPPVIDVEPGKT
YRFRFIGATALSFVSLGIEGHDNLTIIEADGSYTKPAETDHLQLGSGQRYSFLLKTKSLEELAALNKTTF
WIQIETRWRPTNDTGYAVLRY
>gnl|CDD|259942 cd13874, CuRO_2_CopA, The second cupredoxin domain of CopA copper resistance protein family. CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
MDPMDISDVYYDTYLINGKPPEDNWTGLFKPGERVRLRFINAAASTYFDVRIPGGKMTVVAADGQDVRPV
EVDEFRIGVAETYDVIVTIPENGAYTIRATSQDRSGYASGTL
>gnl|CDD|259943 cd13875, CuRO_2_LCC_plant, The second cupredoxin domain of the plant laccases. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Plants usually express multiple laccase genes, but their precise physiological/biochemical roles remain largely unclear. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
VPIILGEWWNRDVNDVEDQALLTGGGPNISDAYTINGQPGDLYNCSSKDTFVLTVEPGKTYLLRIINAAL
NEELFFKIANHTLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTADQPPGRYYMAARPYQSAPPVPFDNT
TATAILEY
>gnl|CDD|259944 cd13876, CuRO_2_Abr2_like, The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
QPIILSDWRHLTSEEYWKIMRASGIEPFCYDSILINGKGRVYCLIVIVDPGERWVSLNFINAGGFHTLAF
SIDEHPMWVYAVDGGYIEPQLVDAISITNGERYSVLVKLDKPPGDYTIRVASTGAPQVISGYAILRYK
>gnl|CDD|259945 cd13877, CuRO_2_Fet3p_like, The second Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
EEVTLTLSDWYHDQSPDLLRDFLSPYNPTGAEPIPDSSLFNDTQNATINFEPGKTYLLRIINMGAFASQY
FHIEGHDMTIIEVDGVYVKPYPVDTLYIAVGQRYSVLVKAKNDTDRNYAIINGMDKDMLDTVPDDLYLNK
TNWLVYDS
>gnl|CDD|259946 cd13879, CuRO_2_McoP_like, The second cupredoxin domain of multicopper oxidase McoP and similar proteins. This family includes archaeal and bacterial multicopper oxidases (MCOs), represented by the extremely thermostable McoP from the hyperthermophilic archaeon Pyrobaculum aerophilum. McoP is an efficient metallo-oxidase that catalyzes the oxidation of cuprous and ferrous ions. It is noteworthy that McoP has three-fold higher catalytic efficiency when using nitrous oxide as electron acceptor than when using dioxygen, the typical oxidizing substrate of multicopper oxidases. McoP may function as a novel archaeal nitrous oxide reductase that is probably involved in the denitrification pathway in archaea. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
YDLPLVIQDRRFDANNQLVYLPNGMDRMMGFLGDRILVNGTPDPTLSVATRAYRLRLLNGSNARIYKLAW
SDGSPLTVIGTDGGLLEAPKTVPYVMLAPGERVDLWVDFSGRPVGTELKLKSLPFSGGGMGMGMMGGGGG
MMGMSSGLPDGAEFDLLTFRVT
>gnl|CDD|259947 cd13880, CuRO_2_MaLCC_like, The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
LGPVLLTDWYHRSAFELFSEELPTGGPPPMDNILINGKGKFPCSTGAGSYFETTFTPGKKYRLRLINTGV
DTTFRFSIDGHNLTVIAADFVPIVPYTTDSLNIGIGQRYDVIVEANQDPVGNYWIRAEPATGCSGTNNNP
DNRTGILRYDGASPTLDPSSTANVTAD
>gnl|CDD|259948 cd13881, CuRO_2_McoC_like, The second cupredoxin domain of a multicopper oxidase McoC and similar proteins. This family includes bacterial multicopper oxidases (MCOs) represented by McoC from the pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic MCO, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with the reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. They are composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
ERVLVLSDLTLDGDGQLAEPSAADWMFGREGDLVLVNGQLNPTITVRPGEVQRWRIVNAASARYFRLALD
GHKFRLIGTDGGLLEAPREVDELLLAPGERAEVLVTAGEPGGRLVLLALPYDRGHMGGMEPRPPLTLATL
EV
>gnl|CDD|259949 cd13882, CuRO_2_Tv-LCC_like, The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor. This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Laccase is a multicopper oxidase (MCO) composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
TVITLGDWYHTAAPDLLATTAGVPPVPDSGTINGKGRFDGGPTSPLAVINVKRGKRYRFRVINISCIPSF
TFSIDGHNLTVIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWIRAPPTGGTPANNGGQLNRAI
LRYKGAPEVEPTTESTAGI
>gnl|CDD|259950 cd13883, CuRO_2_Diphenol_Ox, The second cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Laccase is a multicopper oxidase (MCO) composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
RVLFISDWYHDQSEVIVAGLLSPQGYKGSPAAPSPDSALINGIGQFNCSAADPGTCCTQTSPPEIQVEAG
KRTRFRLINAGSHAMFRFSVDNHTLNVVEADDTPVYGPTVVHRIPIHNGQRYSVIIDTTSGKAGDSFWLR
ARMATDCFAWDLQQQTGKAILRYV
>gnl|CDD|259951 cd13884, CuRO_2_tcLCC_insect_like, The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum. This multicopper oxidase (MCO) subfamily includes the majority of insect laccases. One member is laccase 2 from Tribolium castaneum, which is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi, plants and insects. Laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
EHVILIQDWTHELSSERFVGRGHNGGGQPPDSILINGKGRYYDPKTGNTNNTPLEVFTVEQGKRYRFRLI
NAGATNCPFRVSIDGHTLTVIASDGNDVEPVEVDSIIIYPGERYDFVLNANQPIGNYWIRARGLEDCDNR
RLQQLAILRY
>gnl|CDD|259952 cd13885, CuRO_2_CumA_like, The second cupredoxin domain of CumA like multicopper oxidase. This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida. CumA is involved in the oxidation of Mn(II) in Pseudomonas putida; however, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCOs catalyze the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. The MCOs in this subfamily are composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
RDLVWVLDDWRLDPDGQAVPGFGTPHDAAHAGRIGNLYTINGRVQPDFTVRAGERVRLRLINAANARVFA
LKFPGHEARVIALDGQPAEPFVARNGAVVLAPGMRIDLVIDAPQAAGTRFAVLDHDGRRAAP
>gnl|CDD|259953 cd13886, CuRO_2_MCO_like_1, The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
VVVMVNDYYHDPSSVLLARYLAPGNEGDEPVPDNGLINGIGQFDCASATYKIYCCASNGTYYNFTLEPNK
TYRLRLINAGSFADFTFSVDGHPLTVIEADGTLVEPVEVHSITISVAQRYSVILTTNQPTGGNFWMRAEL
NTDCFTYDNPNLDPDVRAIVSYT
>gnl|CDD|259954 cd13887, CuRO_2_MCO_like_2, The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
MGMDLNDVDYDAFLANDRTLDDPEVVRVEPGGRVRLRVINGSTATNFHIDLGDLKGTLIAVDGNPVQPVE
GRRFPLATAQRLDLLVTIPAEGGAFPVLALREGSNKRTGIVLAT
>gnl|CDD|259955 cd13888, CuRO_3_McoP_like, The third cupredoxin domain of multicopper oxidase McoP and similar proteins. This subfamily includes archaeal and bacterial multicopper oxidases (MCOs), represented by the extremely thermostable McoP from the hyperthermophilic archaeon Pyrobaculum aerophilum. McoP is an efficient metallo-oxidase that catalyzes the oxidation of cuprous and ferrous ions. It is noteworthy that McoP has three-fold higher catalytic efficiency when using nitrous oxide as electron acceptor than when using dioxygen, the typical oxidizing substrate of multicopper oxidases. McoP may function as a novel archaeal nitrous oxide reductase that is probably involved in the denitrification pathway in archaea. Members of this subfamily contain three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
ATPRRIHLSMGRMQWTINGETWADDPDAFPVERVGGTVEIWELVNDAASMPHPMHIHGFQFQVLERSDSP
PQVAELAVAPSGRTATDLGWKDTVLVWPGETVRIAVDFTHDYPGDQLYLLHCHNLEHEDDGMMVNVRVP
>gnl|CDD|259956 cd13889, CuRO_3_BOD, The third cupredoxin domain of Bilirubin oxidase (BOD). Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. It is used in diagnosing jaundice through the determination of bilirubin in serum. BOD is a member of the multicopper oxidase (MCO) family that also includes laccase, ascorbate oxidase and ceruloplasmin. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
ARVRTFRFGRGNGMWTINGKTWADPNRIDAAPQLGTVEIWTLINGGGGWSHPIHIHLEDFQILSRNGGSR
AVPPYERGRKDVVYLGPGEEVRVLMRFRPFRGKYMMHCHNLVHEDHDMMLRFEV
>gnl|CDD|259957 cd13890, CuRO_3_CueO_FtsP, The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins. CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. FtsP does not contain any copper binding sites
PTQERTFTLSGDPHAFTINGKRFDMNRIDFTVKLGTTEIWEVTNTDGMPHPFHIHGVQFRILSRNGQPPP
PNEAGWKDTVWVPPGETVRILVKFDHYADPTGPFMYHCHILEHEDNGMMGQFVV
>gnl|CDD|259958 cd13891, CuRO_3_CotA_like, The third Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat component. CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and is required for spore resistance against hydrogen peroxide and UV light. CotA belongs to the laccase-like multicopper oxidase (MCO) family, which are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
TRTRQLTLGETVDSGGRLTHLLNNLLGWHDPVTETPRLGSTEIWEIINLTPDAHPIHLHLVQFQVLDRQP
FDVDEYNATGEIYYTGPPRPPAPNERGWKDTVRAYPGEVTRIIVRFDGPEGGYVWHCHILEHEDNEMMRP
FRV
>gnl|CDD|259959 cd13892, CuRO_3_PHS, The third Cupredoxin domain of phenoxazinone synthase (PHS). Phenoxazinone synthase (PHS, 2-aminophenol:oxygen oxidoreductase) catalyzes the oxidative coupling of substituted o-aminophenols to produce phenoxazinones. PHS has been shown to participate in diverse biological functions such as spore pigmentation and biosynthesis of the antibiotic grixazone. PHS is a member of the laccase-like multicopper oxidase (MCO) family, which are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
PDERLDVVTPVLKKGGNGDPELWEMEEVECPGKVQVVANIVIIGDAGGTVRTLRRIAKLFDDDVNFTAAA
GSWERWTFVNLGEGHPHPMHIHLAEFQVLERQPYDVTGFDTTVGGTDRPITPGEAAPLEPVELGWKDTVV
VGPGELVTVLVQFDGATGRFMYHCHILEHEDHDMMRPFVVQPPH
>gnl|CDD|259960 cd13893, CuRO_3_AAO, The third cupredoxin domain of plant Ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
ATRTLLLLNTQNLINGQLRWAINNVSYVPPPTPYLAALPVYPFKGGDVVDVILQNANTNTRNASEQHPWH
LHGHDFWVLGYGLGGFDPAADPSSLNLVNPPMRNTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGM
GVVFAEGVERVGRLP
>gnl|CDD|259961 cd13894, CuRO_3_AAO_like_1, The third cupredoxin domain of plant Ascorbate oxidase homologs. This subfamily is composed of plant pollen multicopper oxidase homologous to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. This subfamily does not harbor T1 copper or trinuclear copper binding sites
NPDTPLKLADYFKIKGVFQLDSIPDPPTRKTPYLGTSVINGTYRGFIEIVFQNNEDTVQSWHLDGYSFFV
VGMGFGDWTPEKRKSYNLLDAVSRSTTQVYPGSWTAILLELDNVGMWNVRSQN
>gnl|CDD|259962 cd13895, CuRO_3_AAO_like_2, The third cupredoxin domain of Ascorbate oxidase homologs. This family includes fungal proteins with similarity to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
EVTRRIIITIQQLNADGGVLWAQNGLTWTETLPSVPYLVQLYEYGTSLLPDYEAALANGGFDPETNTFPA
KLGEVLDIVWQNTASPTGGLDAHPWHAHGAHYYDLGSGLGTYSATALANEEKLRGYNPIRRDTTMLYRYG
GKGYYPPPGTGSGWRAWRLRVDDPGVWMLHCHILQHMIMGMQTVWVFG
>gnl|CDD|259963 cd13896, CuRO_3_CopA, The third cupredoxin domain of CopA copper resistance protein family. CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
DREIELHLTGNMERYVWTINGKAYPDADPLRVREGERVRIVFVNDTMMAHPMHLHGHFFQVENGNGEYGP
RKDTVLVPPGETVSVDFDADNPGRWAFHCHNLYHMEAGMMRVVEY
>gnl|CDD|259964 cd13897, CuRO_3_LCC_plant, The third cupredoxin domain of the plant laccases. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Plants usually express multiple laccase genes, but their precise physiological/biochemical roles remain largely unclear. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
VYTTDFPDRPPVPFDYTGNAPNENTPTSRGTKVKVLEYGSTVEIVLQGTSLLAAENHPMHLHGFDFYVVG
RGFGNFDPSTDPATFNLVDPPLRNTVGVPRGGWAAIRFVADNPGVWFMHCHFERHTSWGMATVFIVKNG
>gnl|CDD|259965 cd13898, CuRO_3_Abr2_like, The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
DQTLILTLGRVGSAYSWTLNGTELYPLDEEAYPPLLFLPDPATALDSALTISTKNGTWVDLIFQVTGPPQ
PPHPIHKHGNKAFVIGTGTGPFNWSSVAEAAEAAPENFNLVNPPLRDTFTTPPSTEGPSWLVIRYHVVNP
GAWLLHCHIQSHLAGGMAVVLLDG
>gnl|CDD|259966 cd13899, CuRO_3_Fet3p, The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
DHSITLNVDFDTFDDGVNRAAFNNITYVSPKVPTLYTALSMGDDALDPAIYGPQTNAFVLNHGEVVELVV
NNWDAGKHPFHLHGHKFQVVQRSPDVASDDPNPPINEFPENPMRRDTVMVPPGGSVVIRFRADNPGVWFF
HCHIEWHLEAGLAATFIEAP
>gnl|CDD|259967 cd13900, CuRO_3_Tth-MCO_like, The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus. The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
AGTRRLVFSEGMSPGGGGAFTINGKPFDPDRPDRTVRLGTVEEWTLINTSGEDHPFHIHVNPFQVVSING
KPGLPPVWRDTVNVPAGGSVTIRTRFRDFTGEFVLHCHILDHEDQGMMQVVEI
>gnl|CDD|259968 cd13901, CuRO_3_MaLCC_like, The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
PPVPDPSPTQTLTIDLGPNATGVFLWTLNGSSFRVDWNDPTLLLVADGNTSTFPPEWNVIELPKANKWVY
IVIQNNSPLPHPIHLHGHDFYILAQGTGTFDDDGTILNLNNPPRRDVAMLPAGGYLVIAFKTDNPGAWLM
HCHIAWHASGGLALQFL
>gnl|CDD|259969 cd13902, CuRO_3_McoC_like, The third cupredoxin domain of a multicopper oxidase McoC and similar proteins. This family includes bacteria multicopper oxidases (MCOs) represented by McoC from pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic multicopper oxidase, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. They are capable of oxidizing a vast range of substrates, varying from aromatic compunds to inorganic compounds such as metals. Most MCOs have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
AATRRVVFSEGMSMGAGGMMFLINGKTFDMNRIDFVAKVGEVEVWEVTNTSHMDHPFHLHGTQFQVLEID
GNPQKPEYRAWKDTVNLPPGEAVRIATRQDDPGMWMYHCHILEHEDAGMMGMLHV
>gnl|CDD|259970 cd13903, CuRO_3_Tv-LCC_like, The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor. This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
DVNITLTFGLNGTTGLFTINGVSYVSPTVPVLLQILSGATSAEDLLPTESTIILPRNKVVEITIPGGAIG
GPHPFHLHGHAFSVVRSAGSNTYNYVNPVRRDVVSVGTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLA
VVFAEDP
>gnl|CDD|259971 cd13904, CuRO_3_Diphenol_Ox, The third cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
RGVFNSSFGTFVDPNGNALGRFFVNNVTWTNYIYQPLLHQVASGGGGTLNSSEVASVTFPTDGWYDIVIN
NLDPAIDHPYHLHGVDFHIVARGSGTLTLEQLANVQYNTTNPLRRDTIVIPGGSWAVLRIPADNPGVWAL
HCHIGWHLAAGFAGVVVV
>gnl|CDD|259972 cd13905, CuRO_3_tcLLC2_insect_like, The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum. This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi, plants and insects. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
SINGISFVFPSSPLLSQPEDLSDSSSCDFCNVPSKCCTEPCECTHVIKLPLNSVVEIVLINEGPGPGLSH
PFHLHGHSFYVLGMGFPGYNSTTGEILSQNWNNKLLDRGGLPGRNLVNPPLKDTVVVPNGGYVVIRFRAD
NPGYWLLHCHIEFHLLEGMALVLKVGEPSDPPPP
>gnl|CDD|259973 cd13906, CuRO_3_CumA_like, The third cupredoxin domain of CumA like multicopper oxidase. This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida, which is involved in the oxidation of Mn(II). However, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCO catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
AEFHLFAFQGGMMGAPPDGGSGVAGGTFWAINGTSWTGGDHSHLPPPLATLKRGRSYVLRLVNETAFLHP
MHLHGHFFRVLSRNGRPVPEPFWRDTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMGVIRVA
>gnl|CDD|259974 cd13907, CuRO_3_MCO_like_1, The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
PLPRTIKLSMQHMEWTINGRSFEMDDVTPDETVKLNTTEVWEIINDLGGMGGGGGMMGGGGMMMGGMMAM
PHPIHLHGVQFQVLERSVGPKDRAYWATVKDGFIDEGWKDTVLVMPGERVRIIKPFDDYKGLFLYHCHNL
EHEDMGMMRNFLVE
>gnl|CDD|259975 cd13908, CuRO_3_MCO_like_2, The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
DETIDMTFEKRNAGDGGFNLWTINGKSYPDEDPPLVVQQGRRYRLVFRNASDDAHPMHLHRHTFEVTRID
GKPTSGLRKDVVMLGGYQRVEVDFVADNPGLTLFHCHQQLHMDYGFMALFKY
>gnl|CDD|259976 cd13909, CuRO_3_MCO_like_3, The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
RSLDLDMEGGAMGWMQSATMGGQEMSMRELIQLGQFWAFNGVAGRPDDPLLEARRGETVRIEMVNNTGFP
HGMHLHGHHFRAILPNGALGPWRDTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGMMSWFRVT
>gnl|CDD|259977 cd13910, CuRO_3_MCO_like_4, The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
YVLYVSFEILAYNNLPRGFFNGTSWRPLPGPATLLLALDADNAEEVAAGNGLSTFDGNQLVITVDDIDKV
VDLVINNLDDGDHPFHLHGHKFWVLGSGDGRYGGGGYTAPDGTSLNTTNPLRRDTVSVPGFGWAVLRFVA
DNPGLWAFHCHILWHMAAGMLMQFAV
>gnl|CDD|259978 cd13911, CuRO_3_MCO_like_5, The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3
VARRRFSFAGDGQGDMWTVNGKVFDPDHIAARPRLGTTEIWVFSSDGRHPVHLHGAHFQVVSRTGGRPGE
WDAGWKDTVLLRPRESVTVIIRFDGYRGRYVFHCHNLEHEDMGMMANFQ
>gnl|CDD|259979 cd13912, CcO_II_C, C-terminal domain of Cytochrome c Oxidase subunit II. Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I
PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHS
WAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW
>gnl|CDD|259980 cd13913, ba3_CcO_II_C, C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively
PGVRKIGPNEYEVYVVAQAFAFNPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYT
FDKPGEYLIICNEYCGAGHHNMYGKIIVE
>gnl|CDD|259981 cd13914, CuRO_HCO_II_like_3, Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I
VEIEVEAYQWGWEFSYPEANVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTE
ATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL
>gnl|CDD|259982 cd13915, CuRO_HCO_II_like_2, Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I
ALEIQVTGRQWMWEFTYPNGKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFE
ATKPGEYDLFCTEYCGTGHSGMIGKVRV
>gnl|CDD|259983 cd13916, CuRO_HCO_II_like_1, Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I
QVVAVTGHQWYWELSRTEIPAGKPVEFRVTSADVNHGFGIYDPDMRLLAQTQAMPGYTNVLRYTFDKPGT
YTILCLEYCGLAHHVMMAEFTVV
>gnl|CDD|259984 cd13917, CuRO_HCO_II_like_4, Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I
GDVYLVARAWQWRPVLVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIIC
NEYCGIGHHTMHGRIIVE
>gnl|CDD|259985 cd13918, CuRO_HCO_II_like_6, Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I
GLSAIIVISLIVWTYGMLLYVEDPPDEADEDALEVEVEGFQFGWQFEYPNGVTTGNTLRVPADTPIALRV
TSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY
>gnl|CDD|259986 cd13919, CuRO_HCO_II_like_5, Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I
ALVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPG
RTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKVV
>gnl|CDD|259987 cd13920, Stellacyanin, Stellacyanin is a subclass of phytocyanins, a plant type I copper protein. Stellacyanin is a subclass of the phytocyanins, a ubiquitous family of plant cupredoxins. Stellacyanin is involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. The copper is tetrahedrally coordinated by a cysteine, 2 histidines, and a glutamine residue. The glutamine residue substitutes for a methione ligand typically found in other blue copper proteins. The exact function of stellacyanin is unknown. However, stellacyanin appears to be associated with the plant cell wall; it may be involved in oxidative reactions to build polymeric material making up the cell wall
TDHIVGGSLGWSIPPNASFYTDWAANRTFRVGDSLVFNFEAGVHNVVEVSKEEYDNCTTTNPIKVFTTGP
VIITLNETGTRYFICTVGNHCSLGQKVSINV
>gnl|CDD|259988 cd13921, Amicyanin, Amicyanin is a type I blue copper protein that plays an essential role in electron transfer. In Paracoccus denitrificans bacteria, amicyanin acts as an intermediary of a three-member redox complex along with methylamine dehydrogenase (MADH) and cytochrome c-551i. The electron is transferred from the active site of MADH via the amicyanin copper ion to the cytochrome heme iron. The electron transfer from MADH to cytochrome c-551i does not involve a ternary complex but occurs via a ping-pong mechanism in which amicyanin uses the same interface for the reactions with MADH and cytochrome c-551i
THVVTIEDFKFNPAEVTVKVGDTVTWTNKDSVPHTVTAEDGAFDSGMLATGKSFSYTFTAAGTYDYFCTI
HPFMKGTVTVE
>gnl|CDD|259989 cd13922, Azurin, Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase. Azurin is a bacterial blue copper-binding protein. It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The copper of Azurin is tetrahedrally coordinated by a cysteine, 2 histidines, and a methionine residue. The electron transfer reactions are carried out with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Azurin can function as a tumor suppressor; it forms a complex with p53 that triggers apoptosis in various human cancer cells
CEVTIEGNDQMKFDTKEITVKAGCKEFTVTLKHTGKLPKNVMGHNWVLLKTGDVQAVANDGAAAGADNDY
VPPGDARVIAHTKLIGGGESDSVTFTVSKLAAGGDYTFFCSFPGHYAMMKGKLVV
>gnl|CDD|381607 cd13925, RPF, core lysozyme-like domain of resuscitation-promoting factor proteins. Resuscitation-promoting factor (RPF) proteins, found in various (G+C)-rich Gram-positive bacteria, act to reactivate cultures from stationary phase. This protein shares elements of the structural core of lysozyme and related proteins. Furthermore, it shares a conserved active site glutamate which is required for activity, and has a polysaccharide binding cleft that corresponds to the peptidoglycan binding cleft of lysozyme. Muralytic activity of Rpf in Micrococcus luteus correlates with resuscitation, supporting a mechanism dependent on cleavage of peptidoglycan by RPF
SQWDAIAQCESGGNWNAVNTGNGYYGGLQFLQGTWKSVGGLGYPDDATRAEQITRAERLYARQGAGAWPC
C
>gnl|CDD|381608 cd13926, N-acetylmuramidase_GH108, N-acetylmuramidase domain of the glycosyl hydrolase 108 family. This domain acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It contains a conserved EGGY motif near the N-terminus, the glutamic acid within this motif is essential for catalytic activity. In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion. It is frequently found at the N-terminus of proteins containing a peptidoglycan binding domain
ATFDQAIERVLAHEGGYVNDPKDPGGETNYGITKRTARALGYRTVTKGDIKALTREQAVEIYRRDYWDAP
RCDELPAGVALEVFDAAVNSG
>gnl|CDD|260106 cd13929, PT-DMATS_CymD, aromatic prenyltransferases (PTases) of the DMATS/CymD familiy. Members of the DMATS/CymD family of ABBA prenyltransferases prenylate indole, tyrosine, and xanthone derivatives. This family of fungal proteins includes cyclic dipeptide N-prenyltransferase (CdpNPT), Brevianamide F prenyltransferase (ftmPT1), fumigaclavine C synthase (FgaPT1), dimethylallyltryptophan synthase (DMATS) and related proteins. CdpNPT accepts a variety of tryptophan-containing cyclic dipeptides, including L-tryptophan itself, and prenylates these substrates inverse at the N-1 position of the indole group. FtmPT1 catalyzes the prenylation of brevianamide F in the biosynthesis of fumitremorgin-type alkaloids. FgaPT1 catalyses the prenylation of fumigaclavine A. Dimethylallyltryptophan synthases (DMATS) catalyzes the prenylation of L-tryptophan at C-4 of the indole ring during the biosynthesis of ergot alkaloids
FWWHTTGPMLARLLEAAGYSTEQQYEHLLFFYHHVIPHLGPYPTSGRPPWKSFLTDDGSPIELSWNWQSS
GKPTVRFAIEPIGPLAGTELDPFNQQATRELLARLAALLPGVDLEWFDHFASALFLSEEEAASLLEESLP
PGPRKSQTFLAFDLKGGGISLKAYFFPRLKALATGVSSLDLVFDAIRKLPGGAGLSPALDMLEEYLATLP
AGLTLEPELLAIDCVDPSKSRLKIYVRTPSTSFASVRDVMTLGGRLTDPETLKGLELLRELWHLLLGEPG
DRPDDEEKPLPDPPHLTAGLLFYFELRPGSPLPEPKVYIPVRHYGENDLEIAEALTEFFERLGWGEAAKS
YLEALQSLFPHRDLSKTTGLHTYISFAYKKGGPYVTSYLSPE
>gnl|CDD|260107 cd13930, PT-Tnase, Aromatic Prenyltransferases (PTases) associated with tryptophanase. This group of bacterial and fungal proteins shows homology to the DMATS/CymD family of ABBA prenyltransferases, which prenylates indole, tyrosine, and xanthone derivatives. Some of the members, mostly fungal proteins, are associated with tryptophanase-like domains (Tnase) which catalyzes the degradation of L-tryptophan to yield indole, pyruvate and ammonia, or the degradation of L-tyrosine to yield phenol, pyruvate and ammonia. This suggest that these otherwise uncharacterized proteins may exhibit multiple functions
TFRDFAAGQLRRLCDALGLNDADLEEIVAALRALLGPWGARPVSEPPSWPSFVSDDGTPVEFSVSIDGGT
KPELRVLFEPQGDEPTLAANQRAGLELNRTLARRYGVSLDRFDAIADLFLPDDPQGKFAVWHSLVFRPGK
RPRFKVYLNPQARGPDRAPAVVREALERLGLHHAWDTLEKAAARRGGDELEFFALDLADGPEARVKVYLR
HHGATAADLAAAAAAVPGADPGEIREFCRVMSGGDRGFSGKPPMTCFAFTEGADVPSEATLYVPVRSYAR
DDAEARDRVATYLRRHGADLSRYDRALAALAPRPLEDGVGLHAWVSLRTGRGGRPRVTVYLSSEAYDV
>gnl|CDD|260108 cd13931, PT-CloQ_NphB, Aromatic Prenyltransferases (PTases) of the CloQ/NphB family. Members of the CloQ/NphB family of ABBA prenyltransferases catalyze the prenylation of phenols, naphthalenes, and phenazines. This family of fungal and bacterial proteins includes dihydrophenazine-1-carboxylate dimethylallyltransferase PpzP, the aromatic prenyltransferase from the clorobiocin biosynthetic pathway CloQ, and related proteins. CloQ catalyzes the attachment of a dimethylallyl moiety to 4-hydroxyphenylpyruvate, part of the biosynthetic pathway of the Streptomyces roseochromogenes antibiotic clorobiocin. PpzP, as well as EpzP, are important for the biosynthesis of endophenazines; they catalyze the prenylation of 5,10-dihydrophenazine-1-carboxylic acid (dhPCA). Streptomyces NphB catalyzes the addition of a 10-carbon geranyl group to small organic aromatic substrates and is involved in the biosynthesis of the antioxidant naphterpin. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto aromatic substrates in biosynthetic pathways of microbial secondary metabolites
RLYSDIEEAARLLGVPYSRDKVWPVLSAFEDVFAQGVVSFRTTTRPGADDLDYRFTVRPKPVDPYATALS
HGLLPKTDHPVGTLLAEVSSLLPIDGYGVDFGVVGGFKKTWAFFPGDLQPVSDLAALPSMPDSVAANAEF
FERYGLDKVSFVGVDYRHRTVNLYFTVPPPGCLEPETVAALLRELGLPPPSEEMLEFCKRAFGIYTTLSW
DSPKIERVCFAVLTPDGNALPVHLHPRLEKFAKGAPSADETRKFVYAWAFGPEGEYYKLESYYQ
>gnl|CDD|259826 cd13932, HN_RTEL1, harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL). Mouse Rtel is an essential protein required for the maintenance of both telomeric and genomic stability. RTEL1 appears to maintain genome stability by suppressing homologous recombination (HR). In vitro, purified human and insect RTEL1 have been shown to promote the disassembly of D loop recombination intermediates, in a reaction dependent upon ATP hydrolysis. Human RTEL1 is implicated in the etiology of Dyskeratosis congenital (DC, is an inherited bone marrow failure and cancer predisposition syndrome). Point mutations in its helicase domains, and truncations which result in loss of its C-terminus have been discovered in DC families. RTEL1 is also a candidate gene influencing glioma susceptibility. The C-terminal domain of RTEL1, represented here, appears similar to the N-terminal domain of the scaffolding protein harmonin
KKSSVSASSSSGAKPAPESASAFLREVKQKLSAAEYRQFSAALQAYKTGDDFEQLLAVLAELFAEPERHP
LLRGFRRFVRPHHKKEFDERCKSLTGAGC
>gnl|CDD|259827 cd13933, harmonin_N_like_u1, domain similar to the N-terminal protein-binding module of harmonin; uncharacterized subgroup. This domain is a putative protein-binding module based on its sequence similarity to the N-terminal domain of harmonin. Harmonin (not belonging to this group) is a postsynaptic density-95/discs-large/ZO-1 (PDZ) domain-containing scaffold protein, which organizes the Usher protein network of the inner ear and the retina. This domain is also related to domains found in several other scaffold proteins which organize supramolecular complexes
RNQHLSSFITNARLLLNEAEREVLCTLLKEYKQSRSVDRLVLCLTHVLDTPAKLDLLKDLRHLIPAELLA
KFDRLAPY
>gnl|CDD|260014 cd13934, RNase_H_Dikarya_like, Fungal (dikarya) Ribonuclease H, uncharacterized. This family contains dikarya RNase H, many of which are uncharacterized. Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication
LVYIDGACRNNGRPDARAGYGVYFGPDSSYNVSGRLEDTGGHPQTSQRAELRAAIAALRFRSWIIDPDGE
GLKTVVIATDSEYVVKGATEWIPKWKRNGWRTSKGKPVKNRDLFELLLDEIEDLEEGGVEVQFWHVPREL
NKEADRLAKAAAE
>gnl|CDD|260015 cd13935, RNase_H_bacteria_like, RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. This family includes bacterial ribonuclease H (RNase H) enzymes. RNases are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription
IWESLCVDAACSGNPGIVEYRGVDTKTGEVLFHRGPFPGGTNNMGEFLAIVHALRYLKEKNSRKPIYSDS
QTAIAWVKKKKAKSTLVRNEKNAEIFKLVDRAEEWLSTHTYPNPILKWQTDKWGEIPADFGRK
>gnl|CDD|260110 cd13936, PANDER_like, Domains similar to the Pancreatic-derived factor. FAM3B or PANDER (PANcreatic DERived factor) has been identifed as a regulator of glucose homeostasis and beta cell function. The protein is expressed in the endocrine pancreas and co-secreted with insulin in response to glucose, particularly under conditions of insulin resistance. The protein had initially been predicted to be a member of the four-helical cytokine family, hence the FAM3B designation. This wider family contains FAM3B and FAM4C, N-terminal domains of N-acetylglucosaminyltransferases, and domains in poorly characterized proteins that have been associated with deafness and the progression of cancer
LEVKIASGGGGNYAKICVNGGVLFDGDKSGRGINVVVINGDTGKVIATKTFDTYGAGASNDMIDFLNSVP
PGSIVLIATKDDASKSLKDEARRALESLGSSLIQNLGFRDSWAFVGQKGIKRPSTEQHEISPKNSSWGGP
ALIQTCFPL
>gnl|CDD|260111 cd13937, PANDER_GnT-1_2_like, PANDER-like domain of N-acetylglucosaminyltransferases. O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 participates in O-mannosyl glycosylation and may be responsible for creating GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moieties on alpha dystroglycan and other O-mannosylated proteins. The domain characterized by this model lies N-terminal to the catalytic domain. Its function has not been determined
LDIEVYSSKSKVSVSVDGTTVLEDEEAEAGRGIHVVVLNQATGSVMAQRVFDTYSPGEDEAMILFLNMVS
DGRILIFTIKDEGSFHLKDEARSLLKKLGSQKVSKLGWRDMWAMVTRKGGPVYGEKHSKSPDLSSWGEPV
LLKAEVPL
>gnl|CDD|260112 cd13938, PANDER_like_TMEM2, PANDER-like domain of the transmembrane protein TMEM2. TMEM2 has been characterized as a transmembrane protein that maps to the DFNB7-DFNB11 deafness locus on human chromosome 9. It contains a domain similar to the Pancreatic-derived factor PANDER, C-terminal to a glycine rich G8-domain. The function of the PANDER-like domain in TMEM2 has not been characterized
KFIGVGAGGTLEIHGKKKLSWTLLTKTVLHPGLPKGGGYSFERSWGSRGINVRVIDEDTGEVLESDRFDT
YESEDESKRLAEFLDQIPPGRIVALAVGDEASKNLEDSARKKIRELGSKEIDHLGYRQPWAFVGVKGGPS
SAVEDRREYEGHSTTGTALAAREFFTVF
>gnl|CDD|260113 cd13939, PANDER_FAM3B, Pancreatic derived factor. FAM3B or PANDER (PANcreatic DERived factor) has been identifed as a regulator of glucose homeostasis and beta cell function. The protein is expressed in the endocrine pancreas and co-secreted with insulin in response to glucose, particularly under conditions of insulin resistance. The protein had initially been predicted to be a member of the four-helical cytokine family, hence the FAM3B designation. PANDER induces apoptosis of insulin-secreting beta-cells when over-expressed in vitro. It has been associated with the progression of type 2 diabetes by downregulating beta cell function as well as insulin sensitivity in the liver
KRQKCDHWSPCAPNQYAYRIRSGGGKDIMPEICFEDNMLITGKEGNSNRGINIAVVSYETGKVVATKYFD
MYEGDFSGPMIEFINKIPKKSLVFVVTHDDGSTKLKDPAKKAIEDLGSKEIRNLKFRSAWVFIAAKGFQL
PDNIEKEKINHSDGSKNRYSGWPAEIQIEGCIPKP
>gnl|CDD|260114 cd13940, ILEI_FAM3C, Interleukin-like EMT inducer. The secreted factor FAM3C or ILEI (InterLeukin-like Emt Inducer) has been identifed as a protein involved in the epithelial-mesenchymal transition (EMT) and in processes associated with metastasis formation and the progression of cancer. The protein had initially been predicted to be a member of the four-helical cytokine family, hence the FAM3C designation. ILEI has been found to be widely expressed, and to be involved in retinal development
KPKYKCGLSKPCPEDHFAFRIISGAANVVGPKICFEGKIIMSSVLNNVGRGLNIALVNGETGEVLKTGFF
DMYSGDVKPLLEFLKSIKPGSIVLVASFDDPATKLNDEARKLFAELGSSSIKSLGFRDNWVFVGGKGIKT
KSPFEKHIKNDKDTNKYEGWPEMIEMEGCIP
>gnl|CDD|260115 cd13941, PANDER_like_KIAA1199, PANDER-like domain of KIAA1199 and similar proteins. KIAA1199 has been characterized as a protein associated with poor survival when upregulated in human cancer, as well as with nonsyndromic loss of hearing when mutated. It contains a C-terminal domain similar to the Pancreatic-derived factor PANDER; the function of this PANDER-like domain has not been characterized
KTKDHFLEVKIESYKTRYFHLKDDFAYIEVDGKKFFLSEDGIQVVVIDGHSGKVVDTTSFRNSILQGIPA
QLENYVTNIKDNSIVLITSKGRLVSRGPWTKVLEKLGADQGFKLKEKMAFVGFKGSFRPVWVKLVTDDEA
AKIFQALPIPVVKKMKL
>gnl|CDD|260116 cd13944, lytB_ispH, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase. The 4-hydroxy-3-methylbut-2-enyl diphosphate (HMBPP) reductase (called lytB or ispH) is the terminal enzyme of the mevalonate-independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway, one of the two metabolic routes for isoprenoid biosynthesis. The MEP pathway is essential in many eubacteria, plants, and the malaria parasite. LytB converts HMBPP into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP)
IILAKPAGFCFGVKRAIDIAEKALEEYGGPVYTLGPIIHNPQVVERLEKKGVKFVDDLDEVPEGGTVIIR
AHGVSPEVYEEAKERGLEVIDATCPLVKKVQKIVKKLAKEGYQVVIIGDKGHPEVIGILGYAPGKAIVVE
SLEEAEKLPLYDLKKVGVVSQTTQSVDEFEEIVEALKKRFPEIEVFNTICYATQNRQEAARELAKEVDLM
IVVGGKNSSNTKRLAEIAKEAGPPTYLIETADELDPEWLKGVKKIGITAGASTPDWIIEEVIDRL
>gnl|CDD|260117 cd13945, Chs5_N, N-terminal dimerization domain of Chs5 and similar proteins. Chs5/6 is a multi-protein complex conserved in fungi that interacts with chitin synthase III (Chs3p) and is involved in its transport to the cell surface from the trans-Golgi network, functioning as an exomer cargo adapter. Chs5p appears to form a complex with Chs6p and its paralogs Bch1p, Bud7p, and Bch2p. In this complex, Chs5p may act as a central scaffold. The N-terminal domain characterized by this model forms a homodimer and has been shown to interact with Chs6p and Bch1p. It may function as a flexible hinge domain that allows the exomer to interact with both proteins and the Golgi membrane as the latter undergoes changes in curvature during the formation of transport vesicles. The dimerization domain sits N-terminally to a conserved FBE (FN3-BRCT) unit, which binds Arf1 an is involved in the recruitment of the exomer to the membrane
VEVSLTVGKLDAGLAILLTSDHHLIEFPSVLLPPGIKAGSIVKITVSRNLEAEKKEEEEFQSLQKEILET
YGT
>gnl|CDD|260118 cd13946, LysW, Lysine biosynthesis protein LysW. LysW functions as a carrier protein in the biosynthesis pathway of lysine. The C-terminal glutamate sidechain of LysW attaches to the amino group of alpha-aminoadipate (AAA); this peptide bond formation is catalyzed by the ligase LysX. AAA remains associated with LysW throughout its biosynthetic conversion to lysine. LysW also acts to protect the amino group of glutamate in arginine biosynthesis
AKCPECGAEIELPDDALVGEIVECPDCGAELEVVKLGDPVELKEAPEVEEDWGE
>gnl|CDD|320087 cd13949, 7tm_V1R_pheromone, vomeronasal organ pheromone receptor type-1 family, member of the seven-transmembrane G protein-coupled receptor superfamily. This family represents vomeronasal type-1 receptors (V1Rs) that are specifically expressed in the vomeronasal organ (VNO), which is the sensory organ of the accessory olfactory system present in amphibians, reptiles, and non-primate mammals such as mice and rodents, but it is non-functional or absent in humans, apes and monkeys. The VNO detects pheromones, chemicals released from animals that can influence social and reproductive behaviors, such as male-male aggression or sexual mating, in other members of the same species. On the other hand, the olfactory epithelium, which contains olfactory receptor neurons inside the nasal cavity, is responsible for detecting odor molecules (smells). There are two types of vertebrate pheromones: (1) small volatile molecules such as 2-heptanone, a substance in the urine of both male and female that extends estrous cycle length in female mice; and (2) water-soluble molecules such as the major histocompatibility complex (HMC) class-I peptide, which can induce the pregnancy block effect, the tendency for female rodents to abort their pregnancies upon exposure to the scent of an unknown male. While V1Rs and G-alpha(i2) protein are co-expressed in the apical neurons of the VNO, V2Rs (type-2 vomeronasal receptors) and G-alpha(o) protein are coexpressed in the basal layer of the VNO. Activation of V1R or V2R causes stimulation of phospholipase pathway, generating diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). V1Rs have a short N-terminal extracellular domain, whereas V2Rs contain a long N-terminal extracellular domain, which is believed to bind pheromones. Although V1Rs share the seven-transmembrane domain structure with V1Rs and olfactory receptors, they share little sequence similarity with each other
SNIRITFFSEVGVGISANSILLLFHIFMFFRGHRPRSTDLIIGHLSLIHLLLLLTMGIIATDAFFSWGGW
DDITCKFLIYLHRVLRGLSLCTTCLLSVLQAITLSPRSSCLAKFKHKSPHHISGAFLFLWVLYMLISSHL
LVSIIATPNLTSNNFIYVTQSCSILPMSYSMQSLFSTLLAFRDVFLIGLMLLSSGYMVALLHRHKKQVQH
LHSTSLSPKASPEQRATQTILLLMSFFVVMYILDSIVFYSRTKFKNDSILYCVQIIVSHSYATVSPFVFL
MTEKHIIKFLRSMCG
>gnl|CDD|320088 cd13950, 7tm_TAS2R, mammalian taste receptors type 2, member of the seven-transmembrane G protein-coupled receptor superfamily. This group represents a family of mammalian taste receptors (TAS2Rs), which function as bitter taste receptors. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
IFLIIIVGEFLIGILGNGFIVLVNCIDWIKSRKLSSIDFILTSLAISRIGLLWTIILNSILSVFYPDIYL
SGNVLRTLDILWMFLNHSSLWFATCLSVFYCLKIANFSHPFFLWLKWRINRVVPWLLLGSLLISLLISLP
IVWVIYSVYQNNSKEESNNTSKFQVKKTSYFYSFILLNLGSLIPFILSLISFFLLIFSLWRHTRQMQLNA
TGSRDPSTEAHIRAMKSMISFLILFIIYFLALIITILSYSFLENKLAVLFCEVLMALYPSGHSFILILGN
PKLKQAFL
>gnl|CDD|320089 cd13951, 7tmF_Frizzled_SMO, class F frizzled/smoothened family, member of the 7-transmembrane G protein-coupled receptor superfamily. The class F G protein-coupled receptors includes the frizzled (FZD) family of seven-transmembrane proteins consisting of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. Also included in the class F family is the closely related smoothened (SMO), which is a transmembrane G protein-coupled receptor that acts as the transducer of the hedgehog (HH) signaling pathway. SMO is activated by the hedgehog (HH) family of proteins acting on the 12-transmembrane domain receptor patched (PTCH), which constitutively inhibits SMO. Thus, in the absence of HH proteins, PTCH inhibits SMO signaling. On the other hand, binding of HH to the PTCH receptor activates its internalization and degradation, thereby releasing the PTCH inhibition of SMO. This allows SMO to trigger intracellular signaling and the subsequent activation of the Gli family of zinc finger transcriptional factors and induction of HH target gene expression (PTCH, Gli1, cyclin, Bcl-2, etc). The WNT and HH signaling pathways play critical roles in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
GLFTSSEKKFAEIWISAWSALCFLLTLFTLLTFLIDPSRFRYPERPIIFLALCYNFYSLGYLVRLVVGRE
GIACGKDEGKPYLLLVDGSGNAPCAIVFLLTYYFGMAASIWWVILTLTWFLSAGLKWSSEAIEKKSSYFH
LVAWGLPAVLTIAVLVLRKVDGDELTGICFVGNQNLDALRGFVLAPLFLYLILGTVFLLCGFLSLFRIRS
ILSNDGKKTDKLEKLMLRIGIFAVLYTLPALIVIACYFYEYANRPDWLRSWEPHSCCSPDCEILSRPSLA
VFLLKYFMQLVIGITTGVWVWSKKTLLSWRRLLR
>gnl|CDD|410627 cd13952, 7tm_classB, class B family of seven-transmembrane G protein-coupled receptors. The class B of seven-transmembrane GPCRs is classified into three major subfamilies: subfamily B1 (secretin-like receptor family), B2 (adhesion family), and B3 (Methuselah-like family). The class B receptors have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi or prokaryotes. The B1 subfamily comprises receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the subfamily B1 receptors preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The subfamily B2 consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Furthermore, the subfamily B3 includes Methuselah (Mth) protein, which was originally identified in Drosophila as a GPCR affecting stress resistance and aging, and its closely related proteins
DLALSIITYIGCSLSLVGLLLTIITYLLFPKLRNLRGKILINLCLSLLLAQLLFLIGQLLTSSDRPVLCK
ALAILLHYFLLASFFWMLVEAFDLYRTFVKVFGSSERRRFLKYSLYGWGLPLLIVIITAIVDFSLYGPSP
GYGGEYCWLSNGNALLWAFYGPVLLILLVNLVFFILTVRILLRKLRETPKQSERKSDRKQLRAYLKLFPL
MGLTWIFGILAPFVGGSLVFWYLFDILNSLQGFFIFLIFCLKNKEVRRLL
>gnl|CDD|320091 cd13953, 7tm_classC_mGluR-like, metabotropic glutamate receptor-like class C family of seven-transmembrane G protein-coupled receptors superfamily. The class C GPCRs consist of glutamate receptors (mGluR1-8), the extracellular calcium-sensing receptors (caSR), the gamma-amino-butyric acid type B receptors (GABA-B), the vomeronasal type-2 pheromone receptors (V2R), the type 1 taste receptors (TAS1R), and the promiscuous L-alpha-amino acid receptor (GPRC6A), as well as several orphan receptors. Structurally, these receptors are typically composed of a large extracellular domain containing a Venus flytrap module which possesses the orthosteric agonist-binding site, a cysteine-rich domain (CRD) with the exception of GABA-B receptors, and the seven-transmembrane domains responsible for G protein activation. Moreover, the Venus flytrap module shows high structural homology with bacterial periplasmic amino acid-binding proteins, which serve as primary receptors in transport of a variety of soluble substrates such as amino acids and polysaccharides, among many others. The class C GPCRs exist as either homo- or heterodimers, which are essential for their function. The GABA-B1 and GABA-B2 receptors form a heterodimer via interactions between the N-terminal Venus flytrap modules and the C-terminal coiled-coiled domains. On the other hand, heterodimeric CaSRs and Tas1Rs and homodimeric mGluRs utilize Venus flytrap interactions and intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD), which can also acts as a molecular link to mediate the signal between the Venus flytrap and the 7TMs. Furthermore, members of the class C GPCRs bind a variety of endogenous ligands, ranging from amino acids, ions, to pheromones and sugar molecules, and play important roles in many physiological processes such as synaptic transmission, calcium homeostasis, and the sensation of sweet and umami tastes
PLAIVLLVLAALGLLLTIFIWVVFIRYRNTPVVKASNRELSYLLLFGILLCFLLAFLFLLPPSDVLCGLR
RFLFGLSFTLVFSTLLVKTNRIYRIFKSGLRSSLRPKLLSNKSQLLLVLFLLLVQVAILIVWLILDPPKV
EKVIDSDNKVVELCCSTGNIGLILSLVYNILLLLICTYLAFKTRKLPDNFNEARYIGFSSLLSLVIWIAF
IPTYFTTSGPYRDAILSFGLLLNATVLLLCLFLPKIYIILF
>gnl|CDD|320092 cd13954, 7tmA_OR, olfactory receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
ILLFVLFLLIYLLTLLGNLLIILLVRLDSRLHTPMYFFLSNLSFLDICYTSVTVPKMLANLLSGDKTISF
SGCLTQLYFFFSLGGTECFLLAVMAYDRYVAICHPLHYPTIMNKRVCILLAAGSWLIGFLNSLIHTVLIS
QLPFCGSNVINHFFCDIPPLLKLSCSDTSLNELVIFILAGFVGLGSFLLTLVSYIYIISTILKIPSAEGR
QKAFSTCASHLTVVSLFYGTIIFMYVRPSSSYSSDLDKVVSVFYTVVTPMLNPIIYSLRN
>gnl|CDD|260119 cd13956, PT_UbiA, UbiA family of prenyltransferases (PTases). Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways
LRLMRPYTLLYVLAPALAGAALAGAFAGPLPALLLLALLAVFLGAGAGYALNDYTDRELDAINKPDRPLP
SGRLSPRQALAFAAALLLVGLALALALGPLALLLLLAGLLLGLAYSLGLKRLKLGGWGVLGYATGLALLP
GLGAVAAGGLVPLALLLALVFLLLGLGINLYNDLPDVEGDRAAGIRTLPVRLGPRRARRLAAGLLLAALI
LVVLLAVAGLLGPLALLALLAVALLALRARFARADRLPALPRGFLLLAVYRLLLFAALLLA
>gnl|CDD|260120 cd13957, PT_UbiA_Cox10, Protoheme IX farnesyltransferase. Protoheme IX farnesyltransferase (also called heme O synthase, heme A:farnesyltransferase, cytochrome c oxidase subunit X [Cox10]) converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of the heme B porphyrin ring with a hydroxyethyl farnesyl side group. It is localized at the mitochondrial inner membrane. Eukaryotic Cox10 is important for the maturation of the heme A prosthetic group of cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, that catalyzes the electron transfer from reduced cytochrome c to oxygen. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways
LELTKPRITLLVLLTALAGYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPL
PSGRISPKHALIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIP
PLIGWAAATGSLDLGAWLLFLILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLL
VPLSLLLYLLGLTGWIYLVVALLLGLYFLYLAIKLYRSPDDKWARKLFFASLIYLPLLFLL
>gnl|CDD|260121 cd13958, PT_UbiA_chlorophyll, Bacteriochlorophyll/chlorophyll synthetase. Chlorophyll synthase catalyzes the last step of chlorophyll (Chl) biosynthesis, the addition of the tetraprenyl (phytyl or geranylgeranyl) side chain. In plant chloroplast, the chlorophyll synthase is located in thylakoid membrane and has been shown to also have a regulatory or channeling function. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways
RLELLKPVTWFPPMWAFLCGAAASGAFQWSNWDVWLLLLGMLLAGPLLTGTSQTINDYYDREVDAINEPY
RPIPSGRISEREALWNIWVLLLLSLLVALFLDGPWVFAAAVVGLVLAYIYSAPPLKLKQNGWWGNAAVGL
SYEGLPWWAGAAAFAGLLTWESLALALLYSIGAHGIMTLNDFKSIEGDRQLGLRSLPVALGVDTAAWIAC
GVIDVPQLAVAALLLAWGETWYAAVVGALLLAQIPLQFKLLLDPPAKAVWYNATAQPFYVLGMMVAA
>gnl|CDD|260122 cd13959, PT_UbiA_COQ2, 4-Hydroxybenzoate polyprenyltransferase. 4-Hydroxybenzoate polyprenyltransferase, also known as Coq2, catalyzes the prenylation of p-hydroxybenzoate with an all-trans polyprenyl group, an important step in ubiquinone (CoQ) biosynthesis. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways
MRLDKPIGTLLLLPPALWGLLLAAGGLPLPLLKLLLLFLLGAFLMRSAGCTINDIADRDIDAKVPRTKNR
PLASGAISVKEALLFLAVQLLLGLALLLQLNPLTILLSPIALLLVLIYPLMKRFTYWPQLVLGLAFGWGP
LMGWAAVTGSLPLPALLLYLAVIFWTAGYDTIYAHQDREDDRKIGVKSTAVLFGDRTKLILALLLHLFVA
LLLLAGGLAGLGWPYYLGLGAAAHLLWQEHRLDLPDPLRSCLAFFLSNGWVGLLLFAGLLLD
>gnl|CDD|260123 cd13960, PT_UbiA_HPT1, Tocopherol phytyltransferase. Tocopherol polyprenyltransferase (TPT1), also known as homogentisate phytyltransferase 1 (HPT1), tocopherol phytyltransferase, or VTE2, catalyzes the first step in the biosynthesis of the tocopherol forms of vitamin E, which involves the prenylation of homogentisate using phytyl diphosphate (PDP) as the prenyl donor. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways
FWKFSRPHTIIGTILSVTSLSLLALESNSDLLLLFLLPGALQALVALLLGNVYIVGLNQIYDVEIDKINK
PYLPLASGELSVRTAWAIVASCGILGLALGALLGSPLLLTLLLLSLLLGTAYSVPPPRLKRFPLLAALCI
LTVRGFLVNLGFYLHFQAALGLPFAWPPSLWFLTAFMTVFAIVIALFKDIPDVEGDRKFGIRTFSVRLGV
KRVFWLCVGLLLMNYAGAILVGLTSPALFSKIFMVVGHAVLAAVLWYRSKRVDLESKESIYSFYMFIWKL
FYAEYLLLP
>gnl|CDD|260124 cd13961, PT_UbiA_DGGGPS, Geranylgeranylglycerol-phosphate geranylgeranyltransferase. Digeranylgeranylglyceryl phosphate synthase (DGGGPS) transfers a geranylgeranyl group from geranylgeranyl diphosphate to (S)-3-O-geranylgeranylglyceryl phosphate to form (S)-2,3-di-O-geranylgeranylglyceryl phosphate, as part of the isoprenoid ether lipid biosynthesis. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways
AYLELIRPPNLLMAALAQYLGALFALGPLLSLNDLELLLLFLSVFLIAAAGYIINDYFDVEIDRINKPDR
PIPSGRISRREALILSILLNALGLILAFLLSPLALLIALLNSLLLWLYSHKLKRTPLIGNLLVALLTGLP
FLFGGLAAGNLLLIILLLALFAFLITLGREIVKDIEDVEGDRAEGARTLPIVYGIKKAKKIAALLLLLAI
LLSPLPYLLGGLGILYLILIIIADLLFLYSAIRLAKSPKDYSKLSKLLKLAMLLGLLAFL
>gnl|CDD|260125 cd13962, PT_UbiA_UBIAD1, 1,4-Dihydroxy-2-naphthoate octaprenyltransferase. Human UBIAD1 is an enzyme involved in the synthesis of MK-4. Menaquinones (MKs, also called bacterial forms) are one of the two forms of natural vitamin K, the other being the plant form, phylloquinone (PK). All forms of vitamin K have a 2-methyl-1,4-naphthoquinone (menadione; K3) ring structure in common. At the 3-position of the ring, PK has a phytyl side chain while MKs have several repeating prenyl units. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways
LLAARPRTLPASLAPVLLGTALAYYLGGFFNWLLFLLALLAALLLQIGVNLANDYFDYKKGTDTEPRSGP
SRVLVSGLLSPRQVLRAALVLLLLAALLGLYLVALGGWLLLLLGLLGILAGYFYTGGPFPLSYRGLGELF
VFLFFGLLAVLGTYYVQTGSLSWEVLLAALPLGLLIAAILLANNIRDIEADRAAGKRTLAVRLGRKRARR
LYAALLLLAYLLLLLLVLLGLLPLWSLLALLSLPLAIKLLRRLLRKADKPLLLIALKLTALLTLLFGLLL
ALG
>gnl|CDD|260126 cd13963, PT_UbiA_2, UbiA family of prenyltransferases (PTases), Unknown subgroup. Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown
LLKLLRPHQWVKNLLVFAPLLFAGQLFDPDLLLAALLAFVAFCLAASAVYILNDLLDLEADRLHPTKRNR
PIASGRLSIPAALALAVVLLLAGLALALLLSPAFLLVLLAYLVLNLAYSLKLKRIPLLDVFVIAAGFVLR
VLAGAVAIGVPLSPWLLLFTFFLFLFLALGKRRAELRLLGDAGSHRKVLRGYSVEDLDQLLSIGAAATLV
SYSLYTLYIESPAYAHPELLWLTVPFVLYGIFRYLLLAHRGEMGGDPVEFLLKDRPLLLTGLLWGALV
>gnl|CDD|260127 cd13964, PT_UbiA_1, UbiA family of prenyltransferases (PTases), Unknown subgroup. Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown
YLQLVRLPNLFTVPADVLAGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIP
SGRVSRGAALALGAGLLAAGVALAALVGRLSGLVALLLAAAILLYDAWLKHTPLGPLLMGLCRGLNLLLG
ASAAAAGGLGPALLAALALGVYIAGVTYIARGEVHGGPRRLLPLALLAVLLVIGLALALAAPRGGRVLLA
LLFLALFAAWVGRPLLRAYRDPSPPNIGKAVGAGILSLIPLDAALAAAFGGPALALLVLALLPLALLLAR
KF
>gnl|CDD|260128 cd13965, PT_UbiA_3, UbiA family of prenyltransferases (PTases), Unknown subgroup. Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown
LWLFTKSDIKTIVLPITIFALAAAPSGSLLTAELALPLLLGFLWIWLHLYQFDNQNQPESVEEDRINKPW
RPIPSGRITPRQARRLRWLLVPLCLALSAYLGVLEESLLLIVLTWLYNELGLADHWLTRNLLNALGYAAF
LAGATRIAGGGPHPLDPTAWAWILLSAAIILTTIHAQDFRDVEGDRARGRRTLPLVFGDAAARWLIAAGV
VAWSVVLPYFWGLPPLLAALLVALGAVVAVRFLLLRSVEADRVTFKLYNLWLSVLYLLPLYSR
>gnl|CDD|260129 cd13966, PT_UbiA_4, UbiA family of prenyltransferases (PTases), Unknown subgroup. Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown
LLKVSRPRFWINTAGPFAVGYLLAGSGFDDLLRLILGLLYFLFPANLLIYGVNDVFDYESDARNPRKGGI
EGALLDPAEHRPLLWAVAVSNVPFLLYLVLVGPPAALLLLALFLFLVVAYSAPPLRFKERPFLDSLSNGL
YFLPPALVGLLASGTLPPWLALAAFFLWGMAMHAFGAIQDIEADREAGIRTTATVLGARGTLRLALALWL
LAAVLVLPLSLPLPLSYLALVYPAISLADALAGRTNPRGYWRFPWINTVVGFVLTVLLIWRA
>gnl|CDD|260130 cd13967, PT_UbiA_5, UbiA family of prenyltransferases (PTases), Unknown subgroup. Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown
RRVLDLLVYSSLYLALGAASLVYAASLLLGLPISLPALLIAGLVVYSVYTLNRLTDSEEDAYNDPERAAF
YEKYKKLLLALAIAAGLLALALAFILGLLAFAILLLPLLLGLLYSLPIKPGKLRLRRRKDIPGSKNLVVA
LAWAVVIALLPALYGQPSTPSVLVVFLFFFLKVFVNTAIFDIRDVEGDRIVGIETLPVLLGEERTRLLLL
VLNILLALLLVAGVLLGLLASEFLVLLLSLIYGLIYIIFFSRDENEEGLRLELLAGEEFILAGLVAL
>gnl|CDD|270870 cd13968, PKc_like, Catalytic domain of the Protein Kinase superfamily. The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine
MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDILRRLKGLELNIPKVLVTEDVDGPNILL
MELVKGGTLIAYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG
>gnl|CDD|270871 cd13969, ADCK1-like, aarF domain containing kinase 1 and similar proteins. This subfamily is composed of uncharacterized ABC1 kinase-like proteins including the human protein called aarF domain containing kinase 1 (ADCK1). Eukaryotes contain at least three ABC1-like proteins: in humans, these are ADCK3 and the putative protein kinases named ADCK1 and ADCK2. Yeast Abc1p and its human homolog ADCK3 are atypical protein kinases required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Plant subfamilies 14 and 15 (ABC1K14-15) belong to the same group of ABC1 kinases as human ADCK1. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family
VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQF
AGDLATMEFLVNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLS
SKRVLTMEFIDGIKIDDVEALKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGKPQ
IVLLDHGLYRELDEEFRLNYCRLWKALILGDEKKIKKYSKALG
>gnl|CDD|270872 cd13970, ABC1_ADCK3, Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3. This subfamily is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Subfamily 13 (ABC1K13) of plant ABC1 kinases belongs in this subfamily with yeast Abc1p and human ADCK3. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family
EALARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLKDGREVAVKVQYPGV
AESIDSDLNNLRRLLKLTGLLPKGLDLDALIAELREELLEECDYEREAANQRRFRELLADDPRFVVPEVI
PELSTKRVLTTEFVDGVPLDEAADLSQEERNRIGELLLRLCLRELFEFGFMQTDPNPGNFLYDPEDGRLG
LLDFGAVREYPPEFVDGYRRLVRAALEGDREALLEASVELG
>gnl|CDD|270873 cd13971, ADCK2-like, aarF domain containing kinase 2 and similar proteins. This subfamily is composed of uncharacterized ABC1 kinase-like proteins including the human protein called aarF domain containing kinase 2 (ADCK2). Eukaryotes contain at least three ABC1-like proteins; in humans, these are ADCK3 and the putative protein kinases named ADCK1 and ADCK2. Yeast Abc1p and its human homolog ADCK3 are atypical protein kinases required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Plant subfamily 10 (ABC1K10) belong to the same group of ABC1 kinases as human ADCK2. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family
KLHSNAPPHSWAHTERALEAAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKPDYGGDGGGPRVVAVKVL
HPGVREQIERDLAILRLFAKLLEAIPPLRWLSLPESVEQFASLMLRQLDLRVEAANLERFRENFKDRKDV
SFPKPLYPLVTEEVLVETFEEGVPISRTVLAHGGEPLKRKLARIGLDAFLKMLFVDNFVHGDLHPGNILV
RFNDSNRPSLLVSLDARGSPPRLVFLDAGLVTELSPQDRRNFIDLFKAVARGDGYKAAELMLERSRSSQT
CPDPEGFKSEMEELVNDA
>gnl|CDD|270874 cd13972, UbiB, Ubiquinone biosynthetic protein UbiB. UbiB is the prokaryotic homolog of yeast Abc1p and human ADCK3 (aarF domain containing kinase 3). It is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is required in the first monooxygenase step in Q biosynthesis. Mutant strains with disrupted ubiB genes lack Q and accumulate octaprenylphenol, a Q biosynthetic intermediate
KLQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLLDGREVAVKVLRPGIEKRI
ERDLELLRFLARLAERLLPEARRLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYW
ELTSKNVLTMEWIDGIPISDIEALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGRII
AVDFGIMGRLDKKDRRYLAEILYGFLTRDYRRVAELH
>gnl|CDD|270875 cd13973, PK_MviN-like, Pseudokinase domain of the peptidoglycan biosynthetic protein MviN. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This family is composed of the mycobacterial protein MviN and similar proteins. MviN is an integral membrane protein that is essential for growth and is required for cell wall integrity and peptidogylcan (PG) biosynthesis. It comprises of 14 predicted transmembrane (TM) helices at the N-terminus, followed by an intracellular pseudokinase domain linked through a single TM helix to a carbohydrate binding extracellular domain. Phosphorylation of the MviN pseudokinase domain by the PG-sensitive serine/threonine protein kinase PknB recruits a forkhead associated (FHA) domain protein FhaA, which modulates local PG synthesis at cell poles and the septum. The MviN pseudokinase forms a canonical receptor kinase dimer
RYRLLEDHGGVPGARFWRARDTVLGRDVALTFVDPGGAAAAARRAAEVLRAARRLARLNDPGLARVLDAV
AYRGGVYVVAEWVPGSSLADVAESGPLDPEAAARAVAELAEALAAAHRAGLALGIDHPDRVRISSDGRVV
LAFPAVLAALSPATDVRALGALLYALLTGRWPLPEGGAALAAAPADAAEPVPPRDVRAGVPEDLDALAVR
ALAPEGDPGDRPATTPAALARALAPA
>gnl|CDD|270876 cd13974, STKc_SHIK, Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GPRLGNSPVRSIVQCLARKEGTDDFYTLKILTLEEKGEETQEDRQGKMLLHTEYSLLSLLHDQDGVVHHH
GLFQDRACEIKEDKSSNVYTGRVRKRLCLVLDCLCAHDFSDKTADLINLQHYVIREKRLSEREALVIFYD
VVRVVEALHKKNIVHRDLKLGNMVLNKRTRKITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVLSGKPY
LGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEDGRVSENTVCLIRKLLVLNPQKRLT
ASEVLDSLES
>gnl|CDD|270877 cd13975, PKc_Dusty, Catalytic domain of the Dual-specificity Protein Kinase, Dusty. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KPKLGRELGRGQYGVVYACDSWGGHFPCALKSVVPPDDKHWNDLALEFHYTRSLPKHERIVSLHGSVIDY
SYGGGSSIAVLLIMERLHRDLYTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNR
AKITDLGFCKPEAMMSGSIVGTPIHMAPELFSGKYDNSVDVYAFGILFWYLCAGHVKLPEAFEQCASKDH
LWNNVRKGVRPERLPVFDEECWNLMEACWSGDPSQRPLLGIVQPKLQGIMDR
>gnl|CDD|270878 cd13976, PK_TRB, Pseudokinase domain of Tribbles Homolog proteins. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LEPAEGSSLYRCVDIHTGEELVCKVVPVPECHAVLRAYFRLPSHPNISGVHEVIAGETKAYVFFERDHGD
LHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLESLEDAVILEGED
DSLSDKHGCPAYVSPEILNSGATYSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPET
LSPRARCLIRSLLRREPSERLTAEDILLHPWL
>gnl|CDD|270879 cd13977, STKc_PDIK1L, Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K)
KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVELALREFWALSSIQRQHPNVIQLEECVLQ
RDGLAQRMSHGSSKSDLYLLLVETSLKGERCFDPRSACYLWFVMEFCDGGDMNEYLLSRRPDRQTNTSFM
LQLSSALAFLHRNQIVHRDLKPDNILISHKRGEPILKVADFGLSKVCSGSGLNPEEPANVNKHFLSSACG
SDFYMAPEVWEGHYTAKADIFALGIIIWAMVERITFRDGETKKELLGTYIQQGKEIVPLGEALLENPKLE
LQIPLKKKKSMNDDMKQLLRDMLAANPQERPDAFQLELRLRQ
>gnl|CDD|270880 cd13978, STKc_RIP, Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLV
MEYMENGSLKSLLEREIQDVPWSLRFRIIHEIALGMNFLHNMDPPLLHHDLKPENILLDNHFHVKISDFG
LSKLGMKSISANRRRGTENLGGTPIYMAPEAFDDFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAINPLL
IMQIVSKGDRPSLDDIGRLKQIENVQELISLMIRCWDGNPDARPTFLECLDRL
>gnl|CDD|270881 cd13979, STKc_Mos, Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DWEPLRLQEPLGSGGFGSVYKATYKGETVAVKIVRRRRKNRASRQSFWAELNAARLRHENIVRVLAAETG
TDFASLGLIIMEYCGNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQG
VCKLCDFGCSVKLGEGNEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLR
QHVLYAVVAKDLRPDLSGLEDSEFGQRLRSLISRCWSAQPAERPNADESLLKSLE
>gnl|CDD|270882 cd13980, STKc_Vps15, Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K
DYLYDKSLGSTRFLKVARARHDEGLVVVKVFVKPDPALPLRSYKQRLEEIRDRLLELPNVLPFQKVIETD
KAAYLIRQYVKYNLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTD
FASFKPTYLPEDNPADFSYFFDTSRRRTCYIAPERFVDALTLDAESERRDGELTPAMDIFSLGCVIAELF
TEGRPLFDLSQLLAYRKGEFSPEQVLEKIEDPNIRELILHMIQRDPSKRLSAEDYLKKYRGKVFPEYF
>gnl|CDD|270883 cd13981, STKc_Bub1_BubR1, Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
TYVISKELGEGGYASVYLAKDDDEQSDGSLVALKVEKPPSIWEFYICDQLHSRLKNSRLRESISGAHSAH
LFQDESILVMDYSSQGTLLDVVNKMKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLR
LEICADWPGEGENGWLSKGLKLIDFGRSIDMSLFPKNQSFKADWHTDSFDCIEMREGRPWTYQIDYFGIA
ATIHVMLFGKYMELTQESGRWKINQNLKRYWQRDIWNKFFDTLLNPEPSCNTLPLLEELRKILEEMEAWF
EASLCNNLVVLRKLREIL
>gnl|CDD|270884 cd13982, STKc_IRE1, Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KLTFSPKVLGYGSEGTIVFRGTFDGRPVAVKRLLPEFFDFADREVQLLRESDEHPNVIRYFCTEKDRQFL
YIALELCAASLQDLVESPRESKLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAHGN
VRAMISDFGLCKKLDVGRSSFSRRSGVAGTSGWIAPEMLSGSTKRRQTRAVDIFSLGCVFYYVLSGGSHP
FGDKLEREANILKGKYSLDKLLSLGEHGPEAQDLIERMIDFDPEKRPSAEEVLNHPFFW
>gnl|CDD|270885 cd13983, STKc_WNK, Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYLKFNEVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWE
SKSKKEVIFITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDPPIIHRDLKCDNIFINGN
TGEVKIGDLGLATLLRQSFAKSVIGTPEFMAPEMYEEHYDEKVDIYAFGMCLLEMATGEYPYSECTNAAQ
IYKKVTSGIKPESLSKVKDPELKDFIEKCLKPPDERPSARELLEHPFF
>gnl|CDD|270886 cd13984, PK_NRBP1_like, Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKIFKAQEEKIRAVFDNLIQLDHPNIVKFHRYWTDVQEE
KARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKSWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQH
NGLIKIGSVAPDAIHNHVKTCREEHRNLHFFAPEYGYLEDVTTAVDIYSFGMCALEMAALEIQSNGEKVS
ANEEAIIRAIFSLEDPLQKDFIRKCLSVAPQDRPSARDLLFHPVLF
>gnl|CDD|270887 cd13985, STKc_GAK_like, Catalytic domain of cyclin G-Associated Kinase-like proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIKEIEIMKRLCGHPNIVQYYDSAILS
SEGRKEVLLLMEYCPGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSPPIIHRDIKIENILFSN
TGRFKLCDFGSATTEHYPLERAEEVNIIEEEIQKNTTPMYRAPEMIDLYSKKPIGEKADIWALGCLLYKL
CFFKLPFDESSKLAIVAGKYSIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVINIITKDTK
>gnl|CDD|270888 cd13986, STKc_16, Catalytic domain of Serine/Threonine Kinase 16. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIVKE
AGGKKEVYLLLPYYKRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPELVPYAHRDIKPGNV
LLSEDDEPILMDLGSMNPARIEIEGRREALALQDWAAEHCTMPYRAPELFDVKSHCTIDEKTDIWSLGCT
LYALMYGESPFERIFQKGDSLALAVLSGNYSFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSRVHDL
IP
>gnl|CDD|270889 cd13987, STKc_SBK1, Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSVHPHIIKTYDVAFETEDYYVFAQ
EYAPYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLT
RRVGSTVKRVSGTIPYTAPEVCEAKKNEGFVVDPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFYEEFVR
WQKRKNTAVPSQWRRFTPKALRMFKKLLAPEPERRCSIKEVFKYLGDRW
>gnl|CDD|270890 cd13988, STKc_TBK1, Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQMREFEVLKKLNHKNIVKLFAIEEELTTRHKVL
VMELCPCGSLYTVLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYK
LTDFGAARELEDDEQFVSLYGTEEYLHPDMYERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPF
EGPRRNKEVMYKIITGKPSGAISGVQKSENGPIEWSGELPVSCSLSQGLQTLLTPVLANILEADQEKCWG
FDQFFAETSDILSRKVIHVFSVQQMTAHKIYIHSYE
>gnl|CDD|270891 cd13989, STKc_IKK, Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K)
LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDKNRERWCLEVQIMKKLNHPNVVSARDVPPELEKLSP
NDLPLLAMEYCSGGDLRKVLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGG
RVIYKLIDLGYAKELDQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLPNWQP
VQWHGKVKQKKPEHICAYEDLTGEVKFSSELPSPNHLSSILKEYLESWLQLMLRWDPRQRGGGPQNNPGC
FQLLDSILD
>gnl|CDD|270892 cd13990, STKc_TLK, Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYLLLNLLGKGGFSEVYKAFDLVEQRYVACKIHQLNKDWSEEKKQNYIKHALREYEIHKSLDHPRIVKLY
DVFEIDTDSFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKPPIIHYDLKPGNILL
HSGNVSGEIKITDFGLSKIMDDESYNSDGMELTSQGAGTYWYLPPECFVVGKTPPKISSKVDVWSVGVIF
YQMLYGRKPFGHNQSQEAILEENTILKATEVEFPSKPVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY
>gnl|CDD|270893 cd13991, STKc_NIK, Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YREEVHWATHQLRIGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMACAGLTSPRVVPLYGAVREG
PWVNIFMDLKEGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAFL
CDFGHAECLDPDGLGKSLFTGDYIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSG
PLCLKIANEPPPLREIPPSCAPLTAQAIQAGLRKEPVHRASAAELRRKTNRALQEVGG
>gnl|CDD|270894 cd13992, PK_GC, Pseudokinase domain of membrane Guanylate Cyclase receptors. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ASCGSGASSHTGEPKYVKKVGVYGGRTVAIKHITFSRTEKRTILQELNQLKELVHDNLNKFIGICINPPN
IAVVTEYCTRGSLQDVLLNREIKMDWMFKSSFIKDIVKGMNYLHSSSIGYHGRLKSSNCLVDSRWVVKLT
DFGLRNLLEEQTNHQLDEDAQHKKLLWTAPELLRGSLLEVRGTQKGDVYSFAIILYEILFRSDPFALERE
VAIVEKVISGGNKPFRPELAVLLDEFPPRLVLLVKQCWAENPEKRPSFKQIKKTLTEN
>gnl|CDD|270895 cd13993, STKc_Pat1_like, Catalytic domain of Fungal Pat1-like Serine/Threonine kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFQKLPQLREIDLHRRVSRHPNIITL
HDVFETEVAIYIVLEYCPNGDLFEAITENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILL
SQDEGTVKLCDFGLATTEKISMDFGVGSEFYMAPECFDEVGRSLKGYPCAAGDIWSLGIILLNLTFGRNP
WKIASESDPIFYDYYLNSPNLFDVILPMSDDFYNLLRQIFTVNPNNRILLPELQLLV
>gnl|CDD|270896 cd13994, STKc_HAL4_like, Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGKGATSVVRIVTKKNPRSGVLYAVKEYRRRDDESKRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQDLH
GKWCLVMEYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLT
DFGTAEVFGMPAEKESPMSAGLCGSEPYMAPEVFTSGSYDGRAVDVWSCGIVLFALFTGRFPWRSAKKSD
SAYKAYEKSGDFTNGPYEPIENLLPSECRRLIYRMLHPDPEKRITIDEALNDPWV
>gnl|CDD|270897 cd13995, STKc_MAP3K8, Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KLTYRNIGSDFIPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDVEIQACFRHENIAELYGALLWEET
VHLFMEAGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLVDFG
LSVQMTEDVYVPKDLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYI
IHKQAPPLEDIAQDCSPAMRELLEAALERNPNHRSSAAELLKHEAL
>gnl|CDD|270898 cd13996, STKc_EIF2AK, Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NSRYLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYY
TAWVEEPPLYIQMELCEGGTLRDWIDRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFL
DNDDLQVKIGDFGLATSIGNQKRELNNLNNNNNGNTSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGI
ILFEMLHPFKTAMERSTILTDLRNGILPESFKAKHPKEADLIQSLLSKNPEERPSAEQLLRSL
>gnl|CDD|270899 cd13997, PKc_Wee1_like, Catalytic domain of the Wee1-like Protein Kinases. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAHAALGQHPNIVRYYSSWE
EGGHLYIQMELCENGSLQDALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKG
TCKIGDFGLATRLETSGDVEEGDSRYLAPELLNENYTHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQL
RQGKLPLPPGLVLSQELTRLLKVMLDPDPTRRPTADQLLAHD
>gnl|CDD|270900 cd13998, STKc_TGFbR-like, Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EVIGKGRFGEVWKASLKNEPVAVKIFSSRDKQSWFREKEIYRTPMLKHENILQFIAADERDTALRTELWL
VTAFHPNGSLXDYLSLHTIDWVSLCRLALSVARGLAHLHSEIPGCTQGKPAIAHRDLKSKNILVKNDGTC
CIADFGLAVRLSPSTGEEDNANNGQVGTKRYMAPEVLEGAINLRDFESFKRVDIYAMGLVLWEMASRCTD
LFGIVEEYKPPFYSEVPNHPSFEDMQEVVVRDKQRPNIPNRWLSHPGLQSLAETIEECWDHDAEARLTAQ
CIEERLSEF
>gnl|CDD|270901 cd13999, STKc_MAP3K-like, Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway
IGSGSFGEVYKGKWRGTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTE
YMPGGSLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRI
KNSTTEKMTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRP
PIPPDCPPELSKLIKRCWNEDPEKRPSFSEIVKRL
>gnl|CDD|270902 cd14000, STKc_LRRK, Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LLGDGGFGSVYRASYKGEPVAVKIFNKHTSSNFANVPADTMLRHLRATDAMKNFRLLRQELTVLSHLHHP
SIVYLLGIGIHPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKS
HNVLVWTLYPNSAIIIKIADYGISRQCCRMGAKGSEGTPGFRAPEIARGNVIYNEKVDVFSFGMLLYEIL
SGGAPMVGHLKFPNEFDIHGGLRPPLKQYECAPWPEVEVLMKKCWKENPQQRPTAVTVVSILNSP
>gnl|CDD|270903 cd14001, PKc_TOPK, Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SPFMKKLGYGTGVNVYLMKRSPRGGSSRSPWAVKKINSKCDKGQRSLYQERLKEEAKILKSLNHPNIVGF
RAFTKSEDGSLCLAMEYGGKSLNDLIEERYEAGLGPFPAATILKVALSIARALEYLHNEKKILHGDIKSG
NVLIKGDFESVKLCDFGVSLPLTENLEVDSDPKAQYVGTEPWKAKEALEEGGVITDKADIFAYGLVLWEM
MTLSVPHLNLLDIEDDDEDESFDEDEEDEEAYYGTLGTRPALNLGELDDSYQKVIELFYACTQEDPKDRP
SAAHIVEALEAH
>gnl|CDD|270904 cd14002, STKc_STK36, Catalytic domain of Serine/Threonine Kinase 36. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFE
TKKEFVVVTEYAQGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKL
CDFGFARAMSCNTLVLTSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQM
IVKDPVKWPSNMSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV
>gnl|CDD|270905 cd14003, STKc_AMPK-like, Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIET
ENKIYLVMEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKI
IDFGLSNEFRGGSLLKTFCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRK
ILKGKYPIPSHLSPDARDLIRRMLVVDPSKRITIEEILNHPW
>gnl|CDD|270906 cd14004, STKc_PASK, Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRDRKLGTVPLEIHILDTLNKRSHPNI
VKLLDFFEDDEFYYLVMEKHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENV
ILDGNGTIKLIDFGSAAYIKSGPFDTFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFKENPFYN
IEEILEADLRIPYAVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL
>gnl|CDD|270907 cd14005, STKc_PIM, Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMINGPVPVPLEIALLLKASKPGVPGVIR
LLDWYERPDGFLLIMERPEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLI
NLRTGEVKLIDFGCGALLKDSVYTDFDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFEND
EQILRGNVLFRPRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF
>gnl|CDD|270908 cd14006, STKc_MLCK-like, Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILEL
CSGGELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIKIIDFGLARK
LNPGEELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFS
EEYFSSVSQEAKDFIRKLLVKEPRKRPTAQEALQHPW
>gnl|CDD|270909 cd14007, STKc_Aurora, Catalytic domain of the Serine/Threonine kinase, Aurora kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFE
DKKRIYLILEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELK
LADFGWSVHAPSNRRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRI
QNVDIKFPSSVSPEAKDLISKLLQKDPSKRLSLEQVLNHPWIK
>gnl|CDD|270910 cd14008, STKc_LKB1_CaMKK, Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKRREGKNDRGKIKNALDDVRREIAIMKKLDHPNIVRLY
EVIDDPESDKLYLVLEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLL
LTADGTVKISDFGVSEMFEDGNDTLQKTAGTPAFLAPELCDGDSKTYSGKAADIWALGVTLYCLVFGRLP
FNGDNILELYEAIQNQNDEFPIPPELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV
>gnl|CDD|270911 cd14009, STKc_ATG1_ULK_like, Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLV
LEYCAGGDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFG
FARSLQPASMAETLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSD
AVIPFPIAAQLSPDCKDLLRRLLRRDPAERISFEEFFAHPF
>gnl|CDD|270912 cd14010, STKc_ULK4, Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NYVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLW
LVVEYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGL
ARREGEILKELFGQFSDEGNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPF
VAESFTELVEKILNEDPPPPPPKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPFW
>gnl|CDD|270913 cd14011, PK_SCY1_like, Pseudokinase domain of Scy1-like proteins. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VASAGPGLPWKIYNGSKKSTKQEVSVFVFEKKQLEEYSKRDREQILELLKRGVKQLTRLRHPRILTVQHP
LEESRESLAFATEPVFASLANVLGERDNMPSPPPELQDYKLYDVEIKYGLLQISEALSFLHNDVKLVHGN
ICPESVVINSNGEWKLAGFDFCISSEQATDQFPYFREYDPNLPPLAQPNLNYLAPEYILSKTCDPASDMF
SLGVLIYAIYNKGKPLFDCVNNLLSYKKNSNQLRQLSLSLLEKVPEELRDHVKTLLNVTPEVRPDAEQLS
KIPFFDD
>gnl|CDD|270914 cd14012, PK_eIF2AK_GCN2_rpt1, Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SSESPSGTFYLVYEVVLDNSKKPGKFLTSQEYFKTSNGKKQIQLLEKELESLKKLRHPNLVSYLAFSIER
RGRSDGWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRD
AGTGIVKLTDYSLGKTLLDMCSRGSLDEFKQTYWLPPELAQGSKSPTRKTDVWDLGLLFLQMLFGLDVLE
KYTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTALELLPHEF
>gnl|CDD|270915 cd14013, STKc_SNT7_plant, Catalytic domain of the Serine/Threonine kinase, Plant SNT7. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KKLGEGGFGTVYKGSLLQKDPGGEKRRVVLKKAKEYGEVEIWMNERVRRACPSSCAEFVGAFLDTTSKKF
TKPSLWLVWKYEGDATLADLMQGKEFPYNLEPIIFGRVLIPPRGPKRENVIIKSIMRQILVALRKLHSTG
IVHRDVKPQNIIVSEGDGQFKIIDLGAAADLRIGINYIPKEFLLDPRYAPPEQYIMSTQTPSAPPAPVAA
ALSPVLWQMNLPDRFDMYSAGVILLQMAFPNLRSDSNLIAFNRQLKQCDYDLNAWRMLVEPRASADLREG
FEILDLDDGAGWDLVTKLIRYKPRGRLSASAALAHPYF
>gnl|CDD|270916 cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGE
DDGRPYIVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVK
LTDFGIARALGDSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVL
AKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA
>gnl|CDD|270917 cd14015, STKc_VRK, Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GEVLTDVTKRQWKLGKSIGQGGFGEIYLASDDSTLSVGKDAKYVVKIEPHSNGPLFVEMNFYQRVAKPEM
IKKWMKAKKLKHLGIPRYIGSGSHEYKGEKYRFLVMPRFGRDLQKIFEKNGKRFPEKTVLQLALRILDVL
EYIHENGYVHADIKASNLLLGFGKNKDQVYLVDYGLASRYCPNGKHKEYKEDPRKAHNGTIEFTSRDAHK
GVAPSRRGDLEILGYNMLQWLCGKLPWEDNLKNPEYVQKQKEKYMDDIPLLLKKCFPGKDVPEELQKYLK
YVASLEYEEKPDYEKLRKIL
>gnl|CDD|270918 cd14016, STKc_CK1, Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQLEYEAKVYKLLQGGPGIPRLYWFGQEGDY
NVMVMDLLGPSLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNKVYL
IDFGLAKKYRDPRTGKHIPYREGKSLTGTARYASINAHLGIEQSRRDDLESLGYVLIYFLKGSLPWQGLK
AQSKKEKYEKIGEKKMNTSPEELCKGLPKEFAKYLEYVRSLKFEEEPDYDYLRQLF
>gnl|CDD|270919 cd14017, STKc_TTBK, Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKMEVAVLKKLQGKPHFCRLIGCGRTERY
NYIVMTLLGPNLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDERTV
YILDFGLARQYTNKDGEVERPPRNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRK
LKDKEEVGKMKEKIDHEELLKGLPKEFFQILKHIRSLSYFDTPDYKKLHSLLE
>gnl|CDD|270920 cd14018, STKc_PINK1, Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGKGCNAAVYEAALFPLAIKMMWNISAGSSSEAILRSMGNELVPAPNVALLGEYGEVTRLGLQNGRKLLA
PHPNIIRVQRAFTDSVPLLPGAIEDYPDVLPARLNPSGLGHNRTLFLVMKNYPCTLRQYLWVNTPSYRLA
RVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWLVIADFGCCLADDSIGLQLPFSSWYVDRGG
NACLMAPEVSTAVPGPGVVINYSKADAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQESQLPALPSAVP
PDVRQVVKDLLQRDPNKRVSARVAANVLHLSLW
>gnl|CDD|270921 cd14019, STKc_Cdc7, Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NKYRIIEKIGEGTFSSVYKAEDKLHDLYDRNKGRLVALKHIYPTSSPSRILNELECLERLGGSNNVSGLI
TAFRNEDQVVAVLPYIEHDDFRDFYRKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGK
GVLVDFGLAQREEDRPEQRAPRAGTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGRFPFFFSSDDI
DALAEIATIFGSDEAYDLLDKLLELDPSKRITAEEALKHPFF
>gnl|CDD|270922 cd14020, STKc_KIS, Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LWEVQSRLGQGSSASVYRVSSGRGADQPTSALKEFQLDHQGSQESGDYGFAKERAALEQLQGHRNIVTLY
GVFTNHYSANVPSRCLLLELLDVSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRN
ILWSAEDECFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELQNCLAQAGLQSETECTSAVDLWSLGIVLL
EMFSGMKLKHTVRSQEWKDNSSAIIDHIFASNAVVNPAIPAYHLRDLIKSMLHNDPGKRATAEAALCSPF
FSIPF
>gnl|CDD|270923 cd14021, ChoK-like_euk, Euykaryotic Choline Kinase and similar proteins. This group is composed of eukaryotic choline kinase, ethanolamine kinase, and similar proteins. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K)
ILVIRILSGLTNQVYKVSLKDESDSLEPKKVLFRIYGKYLSTLYDREKESEVFKILSEQGLGPKLIYKFD
GGRIEEYIDGRPLTTDELRNPSVLTSIAKLLAKFHKIKTPPVVFCHNDLQENNILLTNDQDGLRLIDFEY
SGFNYRGYDIANFFNESMIDYDHPEPPYFKIYKENYISEEEKRLFVSVYLSEYLEKNVLPSLDKLVEQFL
QEVEIFTLGSHLYWGLWSI
>gnl|CDD|270924 cd14022, PK_TRB2, Pseudokinase domain of Tribbles Homolog 2. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LEPLEGDHVFRAVHLHSGEELVCKVFDIGCYQESLAPCFCLPAHSNINQITEIILGETKAYVFFERSYGD
MHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDAYILRGHD
DSLSDKHGCPAYVSPEILNTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPET
LSPKAKCLIRSILRREPSERLTSQEILDHPWF
>gnl|CDD|270925 cd14023, PK_TRB1, Pseudokinase domain of Tribbles Homolog 1. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LPTGGREHVYRALQLHSGAELQCKVFPLKHYQDKIRPYIQLPSHRNITGIVEVILGDTKAYVFFEKDFGD
MHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLESLEDTHIMKGED
DALSDKHGCPAYVSPEILNTTGTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDH
VSPKARCLIRSLLRREPSERLTAPEILLHPWF
>gnl|CDD|270926 cd14024, PK_TRB3, Pseudokinase domain of Tribbles Homolog 3. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LEPWEGQELYRAEHYQTEKEYTCKVLSLRSYQECLAPYDRLGPHEGVCSVLEVVIGQDRAYAFFSRHYGD
MHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPLNGDD
DSLTDKHGCPAYVGPEILSSRRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAW
LSPGARCLVSCMLRRSPAERLKASEILLHPWL
>gnl|CDD|270927 cd14025, STKc_RIP4_like, Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
WEKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEPVGL
VMEYMETGSLEKLLASEPLPWELRFRIIHETAVGMNFLHCMKPPLLHLDLKPANILLDAHYHVKISDFGL
AKWNGLSHSHDLSRDGLRGTIAYLPPERFKEKNRCPDTKHDVYSFAIVIWGILTQKKPFAGENNILHIMV
KVVKGHRPSLSPIPRQRPSECQQMICLMKRCWDQDPRKRPTFQDITSETENLLSLLE
>gnl|CDD|270928 cd14026, STKc_RIP2, Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DLRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPE
FLGIVTEYMTNGSLNELLHEKDIYPDVAWPLRLRILYEIALGVNYLHNMSPPLLHHDLKTQNILLDGEFH
VKIADFGLSKWRQLSISQSRSSKSAPEGGTIIYMPPEEYEPSQKRRASVKHDIYSYAIIMWEVLSRKIPF
EEVTNPLQIMYSVSQGHRPDTGEDSLPVDIPHRATLINLIESGWAQNPDERPSFLKCLIELEPVLRTFDE
IDVL
>gnl|CDD|270929 cd14027, STKc_RIP1, Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LDSGGFGKVSLCFHRTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVM
EYMEKGNLMHVLKKVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFK
MWSKLTKEEHNEQREVDGTAKKNAGTLYYMAPEHLNDVNAKPTEKSDVYSFAIVLWAIFANKEPYENAIN
EDQIIMCIKSGNRPDVDDITEYCPREIIDLMKLCWEANPEARPTFPGIEEKFRPFYL
>gnl|CDD|270930 cd14028, STKc_Bub1_vert, Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint protein Bub1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Bub1 (Budding uninhibited by benzimidazoles 1) contains an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding, a GLEBS motif for Bub3/kinetochore binding, and a C-terminal kinase domain. It is involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Bub1 contributes to the inhibition of APC/C by phosphorylating its crucial cofactor, Cdc20, rendering it unable to activate APC/C. In addition, Bub1 facilitates the localization to kinetochores of other SAC and motor proteins including Mad1, Mad2, BubR1, and Plk1. It acts as the master organizer of the functional inner centromere. Bub1 also play roles in protecting sister chromatid cohesion and normal metaphase congression. The Bub1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SVYVDHLLGEGAFAQVYQATQLDLNDAKSNQKFVLKVQKPANPWEFYIGTQLMERLKPSMRHLFIKFYSA
HLFQNGSVLVGELYNYGTLLNAINLYKKLPEKVMPQPLVIYFAMRILYMVEQLHDCEIIHGDIKPDNFIL
GERFLENDDCEEDDLSHGLALIDLGQSIDMKLFPKGTAFTAKCETSGFQCTEMLSNKPWNYQTDYFGVAA
TVYCMLFGTYMKVKNEGGVWKPEGSFRRLPHLELWNEFFHVMLNIPDCHSLPSLDALREKLKKVFQQHYT
NKIRALRNRL
>gnl|CDD|270931 cd14029, STKc_BubR1_vert, Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint protein BubR1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BubR1 (Budding uninhibited by benzimidazoles R1) is also called Bub1 beta (Bub1b). It contains an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. It is involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. BubR1 inhibits APC/C through direct binding. It also plays an important role in stabilizing kinetochore-microtubule attachments. Mutant mice expressing only 10% normal BubR1 protein are viable and develop into adult mice, but display many early aging-associated phenotypes including reduced lifespan, muscle atrophy, cataracts, impaired wound healing, and infertility. The BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
MPDLEEEKEIELGNETYCIKREYILHENYKLFMGAPVNWDMEEAKAFAIKVDSQPVPWDFYITLQLKERL
NDDFDTFFSEQTNCFLYQNGCISLHKDINRFTLQDILLDSEEIIKEVIVLVTYNLLSLVEKLHKAEIVHG
DLRPETLLLDDRIFDPSSSNELEGALKIVDFSHSMDLRLQPTVSSLRGFPIAQSESGQQFLAPQSSPYQV
DLLGIADLAHLMLFREHLQVNQENSVWKISQNVSRLRGGNLWNKFFTKILNAAEGPTVCVLRELKGEMME
LFDSGFQDKLCNYLIQLGMRLNPL
>gnl|CDD|270932 cd14030, STKc_WNK1, Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EERNKQQDEIEELETKAVGXSPDGRFLKFDIEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQR
FKEEAGMLKGLQHPNIVRFYDSWESTVKGKKCIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKG
LQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEKYDESVD
VYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGVKPASFDKVAIPEVKEIIEGCIRQNKDERYAIKDLL
NHAFFQEET
>gnl|CDD|270933 cd14031, STKc_WNK3, Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KAVATSPGGRFLKFDIELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPN
IVRFYDSWESVLKGKKCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTPPIIHRD
LKCDNIFITGPTGSVKIGDLGLATLMRTSFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSE
YPYSECQNAAQIYRKVTSGIKPASFNKVTDPEVKEIIEGCIRQNKSERLSIKDLLNHAFFAEDTG
>gnl|CDD|270934 cd14032, STKc_WNK2_like, Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RFLKFDIELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWE
SCAKGKRCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTPPIIHRDLKCDNIFIT
GPTGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNA
AQIYRKVTCGIKPASFEKVTDPEIKEIIGECICKNKEERYEIKDLLSHAFFAEDTG
>gnl|CDD|270935 cd14033, STKc_WNK4, Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RFLKFNIEIGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWK
STVRGHKCIILVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCPPILHRDLKCDNIFIT
GPTGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEKYDEAVDVYAFGMCILEMATSEYPYSECQNA
AQIYRKVTSGIKPDSFYKVKVPELKEIIEGCIRTDKDERFTIQDLLEHRFF
>gnl|CDD|270936 cd14034, PK_NRBP1, Pseudokinase domain of Nuclear Receptor Binding Protein 1. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ESPCGRWQKRREEVNQRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNFKLQEEKVKAVFDNLIQLEHL
NIVKFHKYWADVKENRARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPP
IIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVANVTTAVDIYSFGMCAL
EMAVLEIQGNGESSYVPQEAINSAIQLLEDPLQREFIQKCLEVDPSKRPTARELLFHQALFEVPSLK
>gnl|CDD|270937 cd14035, PK_MADML, Pseudokinase domain of MLF1-ADaptor Molecule-Like. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QGNMPGIESTFLAMDTEEGVEVVWNELFFQDKKAFKAHEDKIKTMFENLTLVDHPNIVKFHKYWLDVKDN
HARVVFITEYVSSGSLKQFLKKTKKNHKTMNARAWKRWCTQILSALSYLHSCEPPIIHGNLTSDTIFIQH
NGLIKIGSVWHRLFVNVLPEGGVRGPLRQEREELRNLHFFPPEYGSCEDGTAVDIFSFGMCALEMAVLEI
QANGDTRVSEEAIARARHSLEDPNMREFILSCLRHNPCKRPTAHDLLFHRVLF
>gnl|CDD|270938 cd14036, STKc_GAK, Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KLRIKRVIAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIQEINFMKKLSGHPNIVQFCSAASIG
KEESDQGQAEYLLLTELCKGQLVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSPPIIHRDLKIEN
LLIGNQGQIKLCDFGSATTEAHYPDYSWSAQKRSLVEDEITRNTTPMYRTPEMIDLYSNYPIGEKQDIWA
LGCILYLLCFRKHPFEDGAKLRIINAKYTIPPNDTQYTVFHDLIRSTLKVNPEERLSITEIVEQLQELAA
AR
>gnl|CDD|270939 cd14037, STKc_NAK_like, Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GSHHVTIEKYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVCKREIEIMKRLSGHKNIVGYIDSS
ANRSGNGVYEVLLLMEYCKGGGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHYLKPPLIHRDLKVEN
VLISDSGNYKLCDFGSATTKILPPQTKQGVTYVEEDIKKYTTLQYRAPEMIDLYRGKPITEKSDIWALGC
LLYKLCFYTTPFEESGQLAILNGNFTFPDNSRYSKRLHKLIRYMLEEDPEKRPNIYQVSYEAFELAG
>gnl|CDD|270940 cd14038, STKc_IKK_beta, Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RLGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLAPN
DLPLLAMEYCQGGDLRKYLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQR
LIHKIIDLGYAKELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNWQPV
QWHGKVRQKSNEDIVVYEDLTGAVKFSSVLPTPNNLNGILAGKLERWLQCMLMWHPRQRGTDPPQNPNGC
FQALDSILNL
>gnl|CDD|270941 cd14039, STKc_IKK_alpha, Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLVNDV
PLLAMEYCSGGDLRKLLNKPENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIV
HKIIDLGYAKDLDQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLHNLQPFTW
HEKIKKKDPKHIFAVEEMNGEVRFSTHLPQPNNLCSLIVEPMEGWLQLMLNWDPVQRGGGLDTDSKQPRC
FVLMDQILS
>gnl|CDD|270942 cd14040, STKc_TLK1, Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HPTLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHP
RIVKLYDYFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLK
PGNILLVDGTACGEIKITDFGLSKIMDDDSYGVDGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVW
SVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQL
ASDPYLLPHMRRSNSSGNL
>gnl|CDD|270943 cd14041, STKc_TLK2, Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K)
HPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHP
RIVKLYDYFSLDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLK
PGNILLVNGTACGEIKITDFGLSKIMDDDSYNSVDGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDV
WSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQ
LACDPYLLPHIRKSVSTSSPAGAAVASTS
>gnl|CDD|270944 cd14042, PK_GC-A_B, Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SLSSSSYGSLMTAASFDQSQIFTKTGYYKGNLVAIKKVNKKRIDLTREVLKELKHMRDLQHDNLTRFIGA
CVDPPNICILTEYCPKGSLQDILENEDIKLDWMFRYSLIHDIVKGMHYLHDSEIKSHGNLKSSNCVVDSR
FVLKITDFGLHSFRSGQEPPDDSHAYYAKLLWTAPELLRDPNPPPPGTQKGDVYSFGIILQEIATRQGPF
YEEGPDLSPKEIIKKKVRNGEKPPFRPSLDELECPDEVLSLMQRCWAEDPEERPDFSTLRNKLKKLNKG
>gnl|CDD|270945 cd14043, PK_GC-2D, Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PSSPSSTSSVNATSSNTGVAYEGDWVWLKKFPGGSHTELRPSTKNVFSKLRELRHENVNLFLGLFVDCGI
LAIVSEHCSRGSLEDLLRNDDMKLDWMFKSSLLLDLIKGMRYLHHRGIVHGRLKSRNCVVDGRFVLKITD
YGYNEILEAQNLPLPEPAPEELLWTAPELLRDPRLERRGTFPGDVFSFAIIMQEVIVRGAPYCMLGLSPE
EIIEKVRSPPPLCRPSVSMDQAPLECIQLMKQCWSEAPERRPTFDQIFDQFKSINKG
>gnl|CDD|270946 cd14044, PK_GC-C, Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ETKETSHVSLKIDEDKRRDSIQRLRQGKYDKKVVILKDLKNNEGNFTEKQKIELNKLLQIDYYNLTKFYG
TVKLDTMIFGVIEYCERGSLRDVLNDKISYPDGTFMDWEFKISVMYDIAKGMSYLHSSKTEVHGRLKSTN
CVVDSRMVVKITDFGCNSILPPSKDLWTAPEHLRQAGTSQKGDVYSYGIIAQEIILRKETFYTAACSDRK
EKIYRVQNPKGMKPFRPDLNLESAGEREREVYGLVKNCWEEDPEKRPDFKKIENTLAKIFS
>gnl|CDD|270947 cd14045, PK_GC_unk, Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NTSCITVLSSCTTAHNAQKKPFTQTGIYDGRTVAIKKIAKKSFTLSKRIRKEVKQVRELDHPNLCKFIGG
CIEVPNVAIITEYCPKGSLNDVLLNEDIPLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRW
VCKIADYGLTTYRKEDGSENASGYQQRLMQVYLPPENHSNTDTEPTQATDVYSYAIILLEIATRNDPVPE
DDYSLDEAWCPPLPELISGKTENSCPCPADYVELIRRCRKNNPAQRPTFEQIKKTLHKI
>gnl|CDD|270948 cd14046, STKc_EIF2AK4_GCN2_rpt2, Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FSRYLTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYY
QAWIERANLYIQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSN
GNVKIGDFGLATSNKLNVELATQDINKSTSAALGSSGDLTGNVGTALYVAPEVQSGTKSTYNEKVDMYSL
GIIFFEMCYPFSTGMERVQILTALRSVSIEFPPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKSE
>gnl|CDD|270949 cd14047, STKc_EIF2AK2_PKR, Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DERFRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAEREVKALAKLDHPNIVRYNGCWDG
FDYDPETSSSNSSRSKTKCLFIQMEFCEKGTLESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIH
RDLKPSNIFLVDTGKVKIGDFGLVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELL
HVCDSAFEKSKFWTDLRNGILPDIFDKRYKIEKTIIKKMLSKKPEDRPNASEILRTL
>gnl|CDD|270950 cd14048, STKc_EIF2AK3_PERK, Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
TSRFLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRYF
NAWLERPPEGWQEKMDEVYLYIQMQLCRKENLKDWMNRRCTMESRELFVCLNIFKQIASAVEYLHSKGLI
HRDLKPSNVFFSLDDVVKVGDFGLVTAMDQGEPEQTVLTPMPAYAKHTGQVGTRLYMSPEQIHGNQYSEK
VDIFALGLILFELIYSFSTQMERIRTLTDVRKLKFPALFTNKYPEERDMVQQMLSPSPSERPEAHEVIEH
A
>gnl|CDD|270951 cd14049, STKc_EIF2AK1_HRI, Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
TSRYLNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGY
HTAWMEHVQLMLYIQMQLCELSLWDWIVERNKRPCEEEFKSAPYTPVDVDVTTKILQQLLEGVTYIHSMG
IVHRDLKPRNIFLHGSDIHVRIGDFGLACPDILQDGNDSTTMSRLNGLTHTSGVGTCLYAAPEQLEGSHY
DFKSDMYSIGVILLELFQPFGTEMERAEVLTQLRNGQIPKSLCKRWPVQAKYIKLLTSTEPSERPSASQL
LESE
>gnl|CDD|270952 cd14050, PKc_Myt1, Catalytic domain of the Dual-specificity protein kinase, Myt1. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QCFTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVERHEKLGEHPNCVRFIKAW
EEKGILYIQTELCDTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCK
LGDFGLVVELDKEDIHDAQEGDPRYMAPELLQGSFTKAADIFSLGITILELACNLELPSGGDGWHQLRQG
YLPEEFTAGLSPELRSIIKLMMDPDPERRPTAEDLLALP
>gnl|CDD|270953 cd14051, PTKc_Wee1, Catalytic domain of the Protein Tyrosine Kinase, Wee1. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EFHEVEKIGSGEFGSVYKCINRLDGCVYAIKKSKKPVAGSVDEQNALNEVYAHAVLGKHPHVVRYYSAWA
EDDHMIIQNEYCNGGSLADAISENEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRT
PNPVSSEEEEEDFEGEEDNPESNEVTYKIGDLGHVTSISNPQVEEGDCRFLANEILQENYSHLPKADIFA
LALTVYEAAGGGPLPKNGDEWHEIRQGNLPPLPQCSPEFNELLRSMIHPDPEKRPSAAALLQHPV
>gnl|CDD|270954 cd14052, PTKc_Wee1_fungi, Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RFANVELIGSGEFSQVYKVSERVPTGKVYAVKKLKPNYAGAKDRLRRLEEVSILRELTLDGHDNIVQLID
SWEYHGHLYIQTELCENGSLDVFLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLIT
FEGTLKIGDFGMATVWPLIRGIEREGDREYIAPEILSEHMYDKPADIFSLGLILLEAAANVVLPDNGDAW
QKLRSGDLSDAPRLSSTDLHSASSPSSNPPPDPPNMPILSGSLDRVVRWMLSPEPDRRPTADDVLATP
>gnl|CDD|270955 cd14053, STKc_ACVR2, Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EIKARGRFGAVWKAQYLNRLVAVKIFPLQEKQSWLTEREIYSLPGMKHENILQFIGAEKHGESLEAEYWL
ITEFHERGSLCDYLKGNVISWNELCKIAESMARGLAYLHEDIPATNGGHKPSIAHRDFKSKNVLLKSDLT
ACIADFGLALKFEPGKSCGDTHGQVGTRRYMAPEVLEGAINFTRDAFLRIDMYAMGLVLWELLSRCSVHD
GPVDEYQLPFEEEVGQHPTLEDMQECVVHKKLRPQIRDEWRKHPGLAQLCETIEECWDHDAEARLSAGCV
EERLSQLSRS
>gnl|CDD|270956 cd14054, STKc_BMPR2_AMHR2, Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QLIGQGRYGTVWKGSLDERPVAVKVFPARHRQNFQNEKDIYELPLMEHSNILRFIGADERPTADGRMEYL
LVLEYAPKGSLCSYLRENTLDWMSSCRMALSLTRGLAYLHTDLRRGDQYKPAIAHRDLNSRNVLVKADGS
CVICDFGLAMVLRGSSLVRGRPGAAENASISEVGTLRYMAPEVLEGAVNLRDCESALKQVDVYALGLVLW
EIAMRCSDLYPGESVPPYQMPYEAELGNHPTFEDMQLLVSREKARPKFPDAWKENSLAVRSLKETIEDCW
DQDAEARLTALCVEERLAEL
>gnl|CDD|270957 cd14055, STKc_TGFbR2_like, Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KLVGKGRFAEVWKAKLKQNASGQYETVAVKIFPYEEYASWKNEKDIFTDASLKHENILQFLTAEERGVGL
DRQYWLITAYHENGSLQDYLTRHILSWEDLCKMAGSLARGLAHLHSDRTPCGRPKIPIAHRDLKSSNILV
KNDGTCVLADFGLALRLDPSLSVDELANSGQVGTARYMAPEALESRVNLEDLESFKQIDVYSMALVLWEM
ASRCEASGEVKPYELPFGSKVRERPCVESMKDLVLRDRGRPEIPDSWLTHQGMCVLCDTITECWDHDPEA
RLTASCVAERFNELK
>gnl|CDD|270958 cd14056, STKc_TGFbR_I, Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KTIGKGRYGEVWLGKYRGEKVAVKIFSSRDEDSWFRETEIYQTVMLRHENILGFIAADIKSTGSWTQLWL
ITEYHEHGSLYDYLQRNTLDTEEALRLAYSAASGLAHLHTEIVGTQGKPAIAHRDLKSKNILVKRDGTCC
IADLGLAVRYDSDTNTIDIPPNPRVGTKRYMAPEVLDDSINPKSFESFKMADIYSFGLVLWEIARRCEIG
GIAEEYQLPYFGMVPSDPSFEEMRKVVCVEKLRPPIPNRWKSDPVLRSMVKLMQECWSENPHARLTALRV
KKTLAKL
>gnl|CDD|270959 cd14057, PK_ILK, Pseudokinase domain of Integrin Linked Kinase. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
TKINETHSGELWKGRWQGNDIVAKILKVRDVTTRISRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVI
SQYMPYGSLYNVLHEGTGVVVDQSQAVKFALDIARGMAFLHTLEPLIPRHHLNSKHVMIDEDMTARINMA
DVKFSFQEPGKMYNPAWMAPEALQKKPEDINRRSADMWSFAILLWELVTREVPFADLSNMEIGMKIALEG
LRVTIPPGISPHMCKLMKICMNEDPGKRPKFDMIVPILEKM
>gnl|CDD|270960 cd14058, STKc_TAK1, Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VGRGSFGVVCKARWRNQIVAVKIIESESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEG
GSLYNVLHGKEPKPIYTAAHAMSWALQCAKGVAYLHSMKPKALIHRDLKPPNLLLTNGGTVLKICDFGTA
CDISTHMTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAVHNGERP
PLIKNCPKPIESLMTRCWSKDPEKRPSMKEIVKIMSHLMQFFP
>gnl|CDD|270961 cd14059, STKc_MAP3K12_13, Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGSGAQGAVFLGKFRGEEVAVKKVRDEKETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYE
VLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKMSF
AGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLQLPVPSTCPDGFK
LLMKQCWNSKPRNRPSFRQILMHLDIA
>gnl|CDD|270962 cd14060, STKc_MLTK, Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
CGGGSFGSVYRAIWVSQDKEVAVKKLLKIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLF
DYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHT
THMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERPTIPSSC
PRSFAELMRRCWEADVKERPSFKQIIGILESM
>gnl|CDD|270963 cd14061, STKc_MLK, Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VIGVGGFGKVYRGIWRGEEVAVKAARQDPDEDISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCL
VMEYARGGALNRVLAGRKIPPHVLVDWAIQIARGMNYLHNEAPVPIIHRDLKSSNILILEAIENEDLENK
TLKITDFGLAREWHKTTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLAVA
YGVAVNKLTLPIPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI
>gnl|CDD|270964 cd14062, STKc_Raf, Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGSGSFGTVYKGRWHGDVAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLAIVTQWC
EGSSLYKHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKT
RWSGSQQFEQPTGSILWMAPEVIRMQDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQILFMVGRG
YLRPDLSKVRSDTPKALRRLMEDCIKFQRDERPLFPQILASLE
>gnl|CDD|270965 cd14063, PK_KSR, Pseudokinase domain of Kinase Suppressor of Ras. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ELEIKEVIGKGRFGRVHRGRWHGDVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPH
LAIVTSLCKGRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVVITDF
GLFSLSGLLQPGRREDTLVIPNGWLCYLAPEIIRALSPDLDFEESLPFTKASDVYAFGTVWYELLAGRWP
FKEQPAESIIWQVGCGKKQSLSQLDIGREVKDILMQCWAYDPEKRPTFSDLLRMLERLPKK
>gnl|CDD|270966 cd14064, PKc_TNNI3K, Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGSGSFGKVYKGRCRNKIVAIKRYRANTYCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDPSQFAIV
TQYVSGGSLFSLLHEQKRVIDLQSKLIIAVDVAKGMEYLHNLTQPIIHRDLNSHNILLYEDGHAVVADFG
ESRFLQSLDEDNMTKQPGNLRWMAPEVFTQCTRYSIKADVFSYALCLWELLTGEIPFAHLKPAAAAADMA
YHHIRPPIGYSIPKPISSLLMRGWNAEPESRPSFVEIVALLEPC
>gnl|CDD|270967 cd14065, PKc_LIMK_like, Catalytic domain of the LIM domain kinase-like protein kinases. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYV
NGGTLEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLAR
EMPDEKTKKPDRKKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVPADPDYLPRTMDFGL
DVRAFRTLYVPDCPPSFLPLAIRCCQLDPEKRPSFVELEHHL
>gnl|CDD|270968 cd14066, STKc_IRAK, Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGSGGFGTVYKGVLENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYE
YMPNGSLEDRLHCHKGSPPLPWPQRLKIAKGIARGLEYLHEECPPPIIHGDIKSSNILLDEDFEPKLTDF
GLARLIPPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDL
VEWVESKGKEELEDILDKRLVDDDGVEEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL
>gnl|CDD|270969 cd14067, STKc_LRRK1, Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGQGGSGTVIYRARYQGQPVAVKRFHIKKCKKRTDGSADTMLKHLRAADAMKNFSEFRQEASMLHSLQHP
CIVYLIGISIHPLCFALELAPLGSLNTVLEENHKGSSFMPLGHMLTFKIAYQIAAGLAYLHKKNIIFCDL
KSDNILVWSLDVQEHINIKLSDYGISRQSFHEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYEL
LSGQRPSLGHHQLQIAKKLSKGIRPVLGQPEEVQFFRLQALMMECWDTKPEKRPLACSVVEQMKDP
>gnl|CDD|270970 cd14068, STKc_LRRK2, Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LLGDGGFGSVYRAVYRGEDVAVKIFNKHTSFRLLRQELVVLSHLHHPSLVALLAAGTAPRMLVMELAPKG
SLDALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIIAKIADYGIAQY
CCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDELAIQGKLP
DPVKEYGCAPWPGVEALIKDCLKENPQCRPTSAQVFDILNSA
>gnl|CDD|270971 cd14069, STKc_Chk1, Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRR
EGEFQYLFLEYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLK
ISDFGLATVFRYKGKERLLNKMCGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGELPWDQPSDSC
QEYSDWKENKKTYLTPWKKIDTAALSLLRKILTENPNKRITIEDIKKHPWY
>gnl|CDD|270972 cd14070, STKc_HUNK, Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VGSYLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVTKNLRREGRIQQMIRHPNITQLLD
ILETENSYYLVMELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDEND
NIKLIDFGLSNCAGILGYSDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPF
SLRALHQKMVDKEMNPLPTDLSPGAISFLRSLLEPDPLKRPNIKQALANRWL
>gnl|CDD|270973 cd14071, STKc_SIK, Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FYDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMET
KDMLYLVTEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKI
ADFGFSNFFKPGELLKTWCGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDR
VLSGRFRIPFFMSTDCEHLIRRMLVLDPSKRLTIEQIKKHKWM
>gnl|CDD|270974 cd14072, STKc_MARK, Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIET
EKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKI
ADFGFSNEFTPGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRER
VLRGKYRIPFYMSTDCENLLKKFLVLNPSKRGTLEQIMKDRWM
>gnl|CDD|270975 cd14073, STKc_NUAK, Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HRYELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVF
ENKDKIVIVMEYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNA
KIADFGLSNLYSKDKLLQTFCGSPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLV
KQISSGDYREPTQPSDASGLIRWMLTVNPKRRATIEDIANHWWV
>gnl|CDD|270976 cd14074, STKc_SNRK, Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IAGLYDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEV
IDTQTKLYLILELGDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQ
GLVKLTDFGFSNKFQPGEKLETSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDS
ETLTMIMDCKYTVPAHVSPECKDLIRRMLIRDPKKRASLEEIENHPWL
>gnl|CDD|270977 cd14075, STKc_NIM1, Catalytic domain of the Serine/Threonine Kinase, NIM1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGFYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVV
ETLSKLHLVMEYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCV
KVGDFGFSTHAKRGETLNTFCGSPPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGVMPFRAETVAKLK
KCILEGTYTIPSYVSEPCQELIRGILQPVPSDRYSIDEIKNSEWL
>gnl|CDD|270978 cd14076, STKc_Kin4, Catalytic domain of the yeast Serine/Threonine Kinase, Kin4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GPYILGRTLGEGEFGKVKLGWPLPKANHRSGVQVAIKLIRRDTQQENCQTSKIMREINILKGLTHPNIVR
LLDVLKTKKYIGIVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLD
KNRNLVITDFGFANTFDHFNGDLMSTSCGSPCYAAPELVVSDSMYAGRKADIWSCGVILYAMLAGYLPFD
DDPHNPNGDNVPRLYRYICNTPLIFPEYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL
>gnl|CDD|270979 cd14077, STKc_Kin1_2, Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GNWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKEREKRLEKEISRDIRTIREAALSSLL
NHPHICRLRDFLRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLK
IENILISKSGNIKIIDFGLSNLYDPRRLLRTFCGSLYFAAPELLQAQPYTGPEVDVWSFGVVLYVLVCGK
VPFDDENMPALHAKIKKGKVEYPSYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM
>gnl|CDD|270980 cd14078, STKc_MELK, Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LLKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGDDLPRVKTEIEALKNLSHQHICRLYHVI
ETDNKIFMVLEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNL
KLIDFGLCAKPKGGMDHHLETCCGSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMA
LYRKIQSGKYEEPEWLSPSSKLLLDQMLQVDPKKRITVKELLNHPWV
>gnl|CDD|270981 cd14079, STKc_AMPK_alpha, Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGNYILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEV
IETPTDIFMVMEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMN
VKIADFGLSNIMRDGEFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGSLPFDDEHIPNL
FKKIKSGIYTIPSHLSPGARDLIKRMLVVDPLKRITIPEIRQHPWF
>gnl|CDD|270982 cd14080, STKc_TSSK-like, Catalytic domain of testis-specific serine/threonine kinases and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GYRLGKTIGEGSYSKVKLAEYTKSGLKEKVACKIIDKKKAPKDFLEKFLPRELEILRKLRHPNIIQVYSI
FERGSKVFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNN
VKLSDFGFARLCPDDDGDVLSKTFCGSAAYAAPEILQGIPYDPKKYDIWSLGVILYIMLCGSMPFDDSNI
KKMLKDQQNRKVRFPSSVKKLSPECKDLIDQLLEPDPTKRATIEEILNHPWL
>gnl|CDD|270983 cd14081, STKc_BRSK1_2, Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GPYRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVY
ENKKYLYLVLEYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNI
KIADFGMASLQPEGSLLETSCGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLL
EKVKRGVFHIPHFISPDAQDLLRRMLEVNPEKRITIEEIKKHPWF
>gnl|CDD|270984 cd14082, STKc_PKD, Catalytic domain of the Serine/Threonine kinase, Protein Kinase D. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QLYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECM
FETPERVFVVMEKLHGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAE
PFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDED
INDQIQNAAFMYPPNPWKEISPDAIDLINNLLQVKMRKRYSVDKSLSHPW
>gnl|CDD|270985 cd14083, STKc_CaMKI, Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IRDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDIY
ESKSHLYLVMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDED
SKIMISDFGLSKMEDSGVMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKL
FAQILKAEYEFDSPYWDDISDSAKDFIRHLMEKDPNKRYTCEQALEHPW
>gnl|CDD|270986 cd14084, STKc_Chk2, Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PKELRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREINKPRNIETEIEILKKLSH
PCIIKIEDFFDAEDDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPE
NVLLSSQEEECLIKITDFGLSKILGETSLMKTLCGTPTYLAPEVLRSFGTEGYTRAVDCWSLGVILFICL
SGYPPFSEEYTQMSLKEQILSGKYTFIPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL
>gnl|CDD|270987 cd14085, STKc_CaMKIV, Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETP
TEISLVLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPL
KIADFGLSKIVDQQVTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMF
KRILNCDYDFVSPWWDDVSLNAKDLVKKLIVLDPKKRLTTQQALQHPWVTGKAANFAHMDTAQKKLQEFN
ARRKLKAAVKAVVA
>gnl|CDD|270988 cd14086, STKc_CaMKII, Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSIS
EEGFHYLVFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGA
AVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHR
LYAQIKAGAYDYPSPEWDTVTPEAKDLINQMLTVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCL
KKFNARRKLKGA
>gnl|CDD|270989 cd14087, STKc_PSKH1, Catalytic domain of the Protein Serine/Threonine kinase H1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
AKYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRHTNIIQLIEVFETKE
RVYMVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIM
ITDFGLASTRKKGPNCLMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLY
RQILRAKYSYSGEPWPSVSNLAKDFIDRLLTVNPGERLSATQALKHPWI
>gnl|CDD|270990 cd14088, STKc_CaMK_like, Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFET
RKEYFIFLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSK
IVISDFHLAKLENGLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYEN
HDKNLFRKILAGDYEFDSPYWDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI
>gnl|CDD|270991 cd14089, STKc_MAPKAPK, Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DYTISKQVLGLGINGKVLECFHKKTGEKFALKVLRDNPKARREVELHWRASGCPHIVRIIDVYENTYQGR
KCLLVVMECMEGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNA
ILKLTDFGFAKETTTKKSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAI
SPGMKKRIRNGQYEFPNPEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW
>gnl|CDD|270992 cd14090, STKc_Mnk, Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DLYKLTGELLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFREVETLHQCQGHPNILQLIEYFE
DDERFYLVFEKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVS
PVKICDFDLGSGIKLSSTSMTPVTTPELLTPVGSAEYMAPEVVDAFVGEALSYDKRCDLWSLGVILYIML
CGYPPFYGRCGEDCGWDRGEACQDCQELLFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTA
EQVLQHPWV
>gnl|CDD|270993 cd14091, STKc_RSK_C, C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVY
LVTELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPESLRIC
DFGFAKQLRAENGLLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGPNDTPEVIL
ARIGSGKIDLSGGNWDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQRQLTDPQDAALVK
GAVAATFRAIN
>gnl|CDD|270994 cd14092, STKc_MSK_C, C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FFQNYELDLREEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTSREVQLLRLCQGHPNIVKLHEVFQD
ELHTYLVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAE
IKIVDFGFARLKPENQPLKTPCFTLPYAAPEVLKQALSTQGYDESCDLWSLGVILYTMLSGQVPFQSPSR
NESAAEIMKRIKSGDFSFDGEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSSTPLMT
PGVLSSSAAAVSTALRATFDAFHLAFREGFR
>gnl|CDD|270995 cd14093, STKc_PhKG, Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENEAEELREATRREIEILRQVSGHPN
IIELHDVFESPTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENI
LLDDNLNVKISDFGFATRLDEGEKLRELCGTPGYLAPEVLKCSMYDNAPGYGKEVDMWACGVIMYTLLAG
CPPFWHRKQMVMLRNIMEGKYEFGSPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF
>gnl|CDD|270996 cd14094, STKc_CASK, Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVEL
LETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCV
LLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCL
PFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIH
LPETVEQLRKFNARRKLKGA
>gnl|CDD|270997 cd14095, STKc_DCKL, Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHMIENEVAILRRVKHPNIVQLIEEYDTD
TELYLVMELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKS
LKLADFGLATEVKEPLFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDQEELF
DLILAGEFEFLSPYWDNISDSAKDLISRMLVVDPEKRYSAGQVLDHPW
>gnl|CDD|270998 cd14096, STKc_RCK1-like, Catalytic domain of RCK1-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ENYRLINKIGEGAFSNVYKAVPLRNTGKPVAIKVVRKADLSSDNLKGSSRANILKEVQIMKRLSHPNIVK
LLDFQESDEYYYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFE
PIPFIPSIVKLRKADDDETKVDEGEFIPGVGGGGIGIVKLADFGLSKQVWDSNTKTPCGTVGYTAPEVVK
DERYSKKVDMWALGCVLYTLLCGFPPFYDESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDP
AKRYDIDEFLAHPWI
>gnl|CDD|270999 cd14097, STKc_STK33, Catalytic domain of Serine/Threonine Kinase 33. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KIYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFE
TPKRMYLVMELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDN
NDKLNIKVTDFGLSVQKYGLGEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVA
KSEEKLFEEIRKGDLTFTQSVWQSVSDAAKNVLQQLLKVDPAHRMTASELLDNPWI
>gnl|CDD|271000 cd14098, STKc_Rad53_Cds1, Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFQREINILKSLEHPGIVRLIDWY
EDDQHIYLVMEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPV
IVKISDFGLAKVIHTGTFLVTFCGTMAYLAPEILMSKEQNLQGGYSNLVDMWSVGCLVYVMLTGALPFDG
SSQLPVEKRIRKGRYTQPPLVDFNISEEAIDFILRLLDVDPEKRMTAAQALDHPW
>gnl|CDD|271001 cd14099, STKc_PLK, Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest
KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCF
EDEENVYILLELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNV
KIGDFGLAARLEYDGERKKTLCGTPNYIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKET
YKRIKKNEYSFPSHLSISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF
>gnl|CDD|271002 cd14100, STKc_PIM1, Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QYQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELPNGTRVPMEIVLLKKVGSGFRGVIRL
LDWFERPDSFVLVLERPEPVQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILID
LNTGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEHDE
EIIRGQVFFRQRVSSECQHLIKWCLALRPSDRPSFEDIQNHPWM
>gnl|CDD|271003 cd14101, STKc_PIM2, Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QYTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKLPGVNPVPNEVALLQSVGGGPGHRGVI
RLLDWFEIPEGFLLVLERPQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENIL
VDLRTGDIKLIDFGSGATLKDSMYTDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPFER
DTDILKAKPSFNKRVSNDCRSLIRSCLAYNPSDRPSLEQILLHPWMM
>gnl|CDD|271004 cd14102, STKc_PIM3, Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VYQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEIVLLKKVGSGFRGVIKLL
DWYERPDGFLIVMERPEPVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDL
RTGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEE
ILRGRLYFRRRVSPECQQLIKWCLSLRPSDRPTLEQIFDHPWM
>gnl|CDD|271005 cd14103, STKc_MLCK, Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVME
YVAGGELFERVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIKIIDFGLA
RKYDPDKKLKVLFGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWD
FDDEAFDDISDEAKDFISKLLVKDPRKRMSAAQCLQHPWL
>gnl|CDD|271006 cd14104, STKc_Titin, Catalytic domain of the Giant Serine/Threonine Kinase Titin. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNIARHRNILRLHESFESHEE
LVMIFEFISGVDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKI
IEFGQSRQLKPGDKFRLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENI
RNAEYAFDDEAFKNISIEALDFVDRLLVKERKSRMTAQEALNHPWLKQGMETVSSKDIKTTRHRRYY
>gnl|CDD|271007 cd14105, STKc_DAPK, Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ENVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRRGVSREDIEREVSILRQVLHPNI
ITLHDVFENKTDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIM
LLDKNVPIPRIKLIDFGLAHKIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASP
FLGDTKQETLANITAVNYDFDDEYFSNTSELAKDFIRQLLVKDPRKRMTIQESLRHPWI
>gnl|CDD|271008 cd14106, STKc_DRAK, Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
STENINEVYTVESTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLELCKDCPRV
VNLHEVYETRSELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNIL
LTSEFPLGDIKLCDFGISRVIGEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPF
GGDDKQETFLNISQCNLDFPEELFKDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL
>gnl|CDD|271009 cd14107, STKc_obscurin_rpt1, Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HSVYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQERDILARLSHRRLTCLLDQFETR
KTLILILELCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTREDIK
ICDFGFAQEITPSEHQFSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLN
VAEGVVSWDTPEITHLSEDAKDFIKRVLQPDPEKRPSASECLSHEWF
>gnl|CDD|271010 cd14108, STKc_SPEG_rpt1, Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
TDYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAELDHKSIVRFHDAFEKR
RVVIIVTELCHEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQVRI
CDFGNAQELTPNEPQYCKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNI
RNYNVAFEESMFKDLCREAKGFIIKVLVSDRLRPDAEETLEHPWF
>gnl|CDD|271011 cd14109, PK_Unc-89_rpt1, Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VRELYEIGEEDEKRAAQGAPFHVTERSTGRNFLAQLRYGDPFLMREVDIHNSLDHPNIVQMHDAYDDEKL
AVTVIDNLASTIELVRDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDDKLKLA
DFGQSRRLLRGKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVR
SGKWSFDSSPLGNISDDARDFIKKLLVYIPESRLTVDEALNHPWF
>gnl|CDD|271012 cd14110, STKc_obscurin_rpt2, Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
TEKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLS
PRHLVLIEELCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKI
VDLGNAQPFNQGKVLMTDKKGDYVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDR
NIRKGKVQLSRCYAGLSGGAVNFLKSTLCAKPWGRPTASECLQNPWL
>gnl|CDD|271013 cd14111, STKc_SPEG_rpt2, Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PQKPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQEYEILKSLHHERIMALHEAYIT
PRYLVLIAEFCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKI
VDFGSAQSFNPLSLRQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEA
KILVAKFDAFKLYPNVSQSASLFLKKVLSSYPWSRPTTKDCFAHAWL
>gnl|CDD|271014 cd14112, STKc_Unc-89_rpt2, Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PTGRFSFGSEIFRGRFSVIVKAVDSTTETDAHCAVKIFEVSDEASEAVREFESLRTLQHENVQRLIAAFK
PSNFAYLVMEKLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQV
KLVDFGRAQKVSKLGKVPVDGDTDWASPEFHNPETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDEEET
KENVIFVKCRPNLIFVEATQEALRFATWALKKSPTRRMRTDEALEHRWL
>gnl|CDD|271015 cd14113, STKc_Trio_C, C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
WKDNFDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQHPQLVGLLD
TFETPTSYILVLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSL
SKPTIKLADFGDAVQLNTTYYIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESV
EETCLNICRLDFSFPDDYFKGVSQKAKDFVCFLLQMDPAKRPSAALCLQEQWL
>gnl|CDD|271016 cd14114, STKc_Twitchin_like, The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDAFED
DNEMVLILEFLSGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNE
VKLIDFGLATHLDPKESVKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETL
RNVKSCDWNFDDSAFSGISEEAKDFIRKLLLADPNKRMTIHQALEHPWL
>gnl|CDD|271017 cd14115, STKc_Kalirin_C, C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLEL
MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAV
QISGHRHVHHLLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSF
PDEYFGDVSQAARDFINVILQEDPRRRPTAATCLQHPW
>gnl|CDD|271018 cd14116, STKc_Aurora-A, Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRL
YGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGS
AGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQE
TYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWIT
>gnl|CDD|271019 cd14117, STKc_Aurora-B_like, Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RKFTIDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILR
LYNYFHDRKRIYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMG
YKGELKIADFGWSVHAPSLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHT
ETYRRIVKVDLKFPPFLSDGSRDLISKLLRYHPSERLPLKGVMEHPWVKANSRRVLPPVY
>gnl|CDD|271020 cd14118, STKc_CAMKK, Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EIGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKQAGFFRRPPPRRKPGALGKPLDPLDRVYREIAILKK
LDHPNVVKLVEVLDDPNEDNLYMVFELVDKGAVMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRD
IKPSNLLLGDDGHVKIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRKKFSGKALDIWAMGVTLYC
FVFGRCPFEDDHILGLHEKIKTDPVVFPDDPVVSEQLKDLILRMLDKNPSERITLPEIKEHPWVT
>gnl|CDD|271021 cd14119, STKc_LKB1, Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRIPNGEANVKREIQILRRLNHRNVIKLVDVLYNEEKQK
LYMVMEYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISD
FGVAEALDLFAEDDTCTTSQGSPAFQPPEIANGQDSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLF
ENIGKGEYTIPDDVDPDLQDLLRGMLEKDPEKRFTIEQIRQHPWF
>gnl|CDD|271022 cd14120, STKc_ULK1_2-like, Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGHGAFAVVFKGRHRKKPDLPVAIKCITKKNLSKSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLV
MEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKPSPNDIRL
KIADFGFARFLQDGMMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKA
FYEKNANLRPNIPSGTSPALKDLLLGLLKRNPKDRIDFEDFFSHPF
>gnl|CDD|271023 cd14121, STKc_ULK3, Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EKLGSGTYATVYKAYRKSGAREVVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHI
YLIMEYCSGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLAD
FGFAQHLKPNDEAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRS
SKPIEIPTRPELSADCRDLLLRLLQRDPDRRISFEEFFAHPF
>gnl|CDD|271024 cd14122, STKc_VRK1, Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. Vertebrates contain three VRK proteins. Human VRK1 is implicated in the regulation of many cellular processes including cell cycle progression and proliferation, stress responses, nuclear envelope assembly and chromatin condensation. It regulates cell cycle progression during the DNA replication period by inducing cyclin D1 expression. VRK1 also phosphorylates and regulates some transcription factors including p53, c-Jun, ATF2, and nuclear factor BAF. VRK1 stabilizes p53 by interfering with its mdm2-mediated degradation. Accumulation of p53, which blocks cell growth and division, is modulated by an autoregulatory loop between p53 and VRK1 (accumulated p53 downregulates VRK1). This autoregulatory loop has been found to be nonfunctional in some lung carcinomas. The VRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GEVLTDMAKKEWKLGLPIGQGGFGRLYLADENSSESVGSDAPYVVKVEPSDNGPLFTELKFYMRAAKPDQ
IQKWIKSHKLKYLGVPKYWGSGLHEKNGKSYRFMIMDRFGSDLQKIYEANAKRFSRKTVLQLGLRILDIL
EYIHEHEYVHGDIKASNLLLSYKNPDQVYLVDYGLAYRYCPEGVHKEYKEDPKRCHDGTIEFTSIDAHKG
VAPSRRGDLEILGYCMIQWLCGHLPWEDNLKDPNYVRDSKIRYRDNISELMEKCFPGKNKPGEIRKYMET
VKLLGYTEKPLYPHLREILLQ
>gnl|CDD|271025 cd14123, STKc_VRK2, Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK2 exists as two alternative splice forms, A and B, which differ in their C-terminal regions. VRK2A, the predominant isoform, contains a hydrophobic tail and is anchored to the ER and mitochondria. It is expressed in all cell types. VRK2B lacks a membrane-anchor tail and is detected in the cytosol and the nucleus. Like VRK1, it can stabilize p53. VRK2B functionally replaces VRK1 in the nucleus of cell types where VRK1 is absent. VRK2 modulates hypoxia-induced stress responses by interacting with TAK1, an atypical MAPK kinase kinase which triggers cascades that activate JNK following oxidative stress. VRK2 also interacts with JIP1, a scaffold protein that assembles three consecutive members of a MAPK pathway. This interaction prevents the association of JNK with the signaling complex, leading to reduced phosphorylation and AP1-dependent transcription. The VRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PEGCILTDTEKKNWRLGKMIGKGGFGLIYLASPQVNVPVEDDAVHVIKVEYHENGPLFSELKFYQRAAKP
DTISKWMKSKQLDYLGIPTYWGSGLTEFNGTSYRFMVMDRLGTDLQKILIDNGGQFKKTTVLQLGIRMLD
VLEYIHENEYVHGDIKAANLLLGYRNPNEVYLADYGLSYRYCPNGNHKEYKENPRKGHNGTIEFTSLDAH
KGVAPSRRGDLEILGYCMLHWLCGKLPWEQNLKNPVAVQEAKAKLLSNLPDSVLKWSTGGSSSMEIAQFL
SRVKDLAYDEKPDYQALKKILS
>gnl|CDD|271026 cd14124, PK_VRK3, Pseudokinase domain of Vaccinia Related Kinase 3. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK3 is an inactive pseudokinase that is unable to bind ATP. It achieves its regulatory function through protein-protein interactions. It negatively regulates ERK signaling by binding directly and enhancing the activity of the MAPK phosphatase VHR (vaccinia H1-related), which dephosphorylates and inactivates ERK. The VRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GTVLTDTSGRKWKLAKFLTRDNQGILYGAAQTSQLAGSQEQKYILKLDAKDGRLFNEQNFFQRAAKPLQV
DKWKKLHSTDLLGIPSCVGFGVHDSYRFLVFPSLGQSLQSALDEGKGVLSEKAVLQLACRLLDALEFIHE
NEYVHGDITAENIFVDPEDQSEVYLAGYGFAFRYCPGGKHVEYREGSRSPHEGDIEFISLDSHKGAGPSR
RSDLQSLGYCMLKWLTGSLPWSNLLHNTEDIMKQKERFMDDVPGFLGPCFHQKKVSEALQKYLKVVMALQ
YEEKPDYAMLRNGLSAAL
>gnl|CDD|271027 cd14125, STKc_CK1_delta_epsilon, Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDY
NVMVMDLLGPSLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGLGKKGNLVYI
IDFGLAKKYRDPRTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLK
AATKKQKYEKISEKKMSTPIEVLCKGFPSEFATYLNYCRSLRFDDKPDYSYLRRLFRDLFHREGF
>gnl|CDD|271028 cd14126, STKc_CK1_gamma, Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKLLGQAEGLPQVYYFGPCGKY
NAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQSTKKQHVI
HIIDFGLAKEYIDPETNKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG
LKADTLKERYQKIGDTKRATPIEVLCENFPEEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDD
YEFDWTGK
>gnl|CDD|271029 cd14127, STKc_CK1_fungal, Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HYKVGKKIGEGSFGVIFEGTNLLNGQQVAIKFEPRKSDAPQLRDEYRTYKLLAGCPGIPNVYYFGQEGLH
NILVIDLLGPSLEDLFDLCGRKFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIGRPGTKNANVI
HVVDFGMAKQYRDPKTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFMYFLRGSLPWQG
LKAATNKQKYEKIGEKKQSTPIRDLCEGFPEEFAQYLEYVRNLGFDETPDYDYLRGLFSKALKDLGE
>gnl|CDD|271030 cd14128, STKc_CK1_alpha, Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KYRLVRKIGSGSFGDIYLGINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDY
NVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMGIGRHCNKLFL
IDFGLAKKYRDSRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRGSLPWQGLK
AATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLF
>gnl|CDD|271031 cd14129, STKc_TTBK2, Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RWKVLRKIGGGGFGEIYDALDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRF
NYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKC
YMLDFGLARQFTNSCGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKI
KDKEQVGSIKERYEHRLMLKHLPPEFSVFLDHISGLDYFTKPDYQLLVSVFD
>gnl|CDD|271032 cd14130, STKc_TTBK1, Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKF
NYVVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKC
YMLDFGLARQYTNTTGEVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKI
KDKEQVGMIKEKYEHRMLLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFE
>gnl|CDD|271033 cd14131, PKc_Mps1, Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK). Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KPYEILKQLGKGGSSKVYKVLNPKKKIYALKRVDLEGADEQTLQSYKNEIELLKKLKGSDRIIQLYDYEV
TDEDDYLYMVMECGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGR
LKLIDFGIAKAIQNDTTSIVRDSQVGTLNYMSPEAIKDTSASGEGKPKSKIGRPSDVWSLGCILYQMVYG
KTPFQHITNPIAKLQAIIDPNHEIEFPDIPNPDLIDVMKRCLQRDPKKRPSIPELLNHPFL
>gnl|CDD|271034 cd14132, STKc_CK2_alpha, Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PPEYWDYENLNVEWGSQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKKKIKREIKILQNLR
GGPNIVKLLDVVKDPQSKTPSLIFEYVNNTDFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKP
HNIMIDHEKRKLRLIDWGLAEFYHPGQEYNVRVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRK
EPFFHGHDNYDQLVKIAKVLGTDDLYAYLDKYGIELPPRLNDILGRHSKKPWERFVNSENQHLVTPEALD
LLDKLLRYDHQERITAKEAMQHPYFD
>gnl|CDD|271035 cd14133, PKc_DYRK_like, Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLDEIRLLELLNKKDKADKYHIVRLKDVF
YFKNHLCIVFELLSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSR
CQIKIIDFGSSCFLTQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQL
ARIIGTIGIPPAHMLDQGKADDELFVDFLKKLLEIDPKERPTASQALSHPWL
>gnl|CDD|271036 cd14134, PKc_CLK, Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HLIYKPGDLLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKYREAAKIEIDVLETLAEKDP
NGKSHCVQLRDWFDYRGHMCIVFELLGPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTD
LKPENILLVDSDYVKVYNPKKKRQIRVPKSTDIKLIDFGSATFDDEYHSSIVSTRHYRAPEVILGLGWSY
PCDVWSIGCILVELYTGELLFQTHDNLEHLAMMERILGPLPKRMIRRAKKGAKYFYFYHGRLDWPEGSSS
GRSIKRVCKPLKRLMLLVDPEHRLLFDLIRKMLEYDPSKRITAKEALKHPFF
>gnl|CDD|271037 cd14135, STKc_PRP4, Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYRVYGYLGKGVFSNVVRARDLARGNQEVAIKIIRNNELMHKAGLKELEILKKLNDADPDDKKHCIRLLR
HFEHKNHLCLVFESLSMNLREVLKKYGKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNE
KKNTLKLCDFGSASDIGENEITPYLVSRFYRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNN
HMLKLMMDLKGKFPKKMLRKGQFKDQHFDENLNFIYREVDKVTKKEVRRVMSDIKPTKDLKTLLIGKQRL
PDEDRKKLLQLKDLLDKCLMLDPEKRITPNEALQHPFI
>gnl|CDD|271038 cd14136, STKc_SRPK, Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PVKIGEVYNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAALDEIKLLKCVREADPKD
PGREHVVQLLDDFKHTGPNGTHVCMVFEVLGPNLLKLIKRYNYRGIPLPLVKKIARQVLQGLDYLHTKCG
IIHTDIKPENVLLCISKIEVKIADLGNACWTDKHFTEDIQTRQYRSPEVILGAGYGTPADIWSTACMAFE
LATGDYLFDPHSGEDYSRDEDHLALIIELLGRIPRSIILSGKYSREFFNRKGELRHISKLKPWPLEDVLV
EKYKWSKEEAKEFASFLLPMLEYDPEKRATAAQCLQHPWL
>gnl|CDD|271039 cd14137, STKc_GSK3, The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKHPNIVKLKYFFYSSG
EKKDEVYLNLVMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVD
PETGVLKLCDFGSAKRLVPGEPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGE
SSVDQLVEIIKVLGTPTREQIKAMNPNYTEFKFPQIKPHPWEKVFPKRTPPDAIDLLSKILVYNPSKRLT
ALEALAHPFFDEL
>gnl|CDD|271040 cd14138, PTKc_Wee1a, Catalytic domain of the Protein Tyrosine Kinase, Wee1a. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SRYATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHSHVVRY
YSAWAEDDHMLIQNEYCNGGSLADAISENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNI
FISRTSIPNAASEEGDEDEWASNKVIFKIGDLGHVTRVSSPQVEEGDSRFLANEVLQENYTHLPKADIFA
LALTVVCAAGAEPLPTNGDQWHEIRQGKLPRIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKHSV
>gnl|CDD|271041 cd14139, PTKc_Wee1b, Catalytic domain of the Protein Tyrosine Kinase, Wee1b. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EFLELEKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGSSNEQLALHEVYAHAVLGHHPHVVRYYSAWA
EDDHMIIQNEYCNGGSLQDAISENTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHK
MQSSSGVGEEVSNEEDEFLSANVVYKIGDLGHVTSINKPQVEEGDSRFLANEILQEDYRHLPKADIFALG
LTVALAAGAEPLPTNGAAWHHIRKGNFPDVPQELPESFSSLLKNMIQPDPEQRPSATALARHTV
>gnl|CDD|271042 cd14140, STKc_ACVR2b, Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EIKARGRFGCVWKAQLMNEYVAVKIFPIQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEMELWL
ITAFHDKGSLTDYLKGNIVSWNELCHIAETMARGLSYLHEDVPRCKGEGHKPAIAHRDFKSKNVLLKNDL
TAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRDSFLRIDMYAMGLVLWELVSRCKAA
DGPVDEYMLPFEEEIGQHPSLEDLQEVVVHKKMRPVFKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGC
VEERISQIRRS
>gnl|CDD|271043 cd14141, STKc_ACVR2a, Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EIKARGRFGCVWKAQLLNEYVAVKIFPIQDKLSWQNEYEIYSLPGMKHENILQFIGAEKRGTNLDVDLWL
ITAFHEKGSLTDYLKANVVSWNELCHIAQTMARGLAYLHEDIPGLKDGHKPAIAHRDIKSKNVLLKNNLT
ACIADFGLALKFEAGKSAGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELASRCTASD
GPVDEYMLPFEEEVGQHPSLEDMQEVVVHKKKRPVLRECWQKHAGMAMLCETIEECWDHDAEARLSAGCV
EERIIQMQRL
>gnl|CDD|271044 cd14142, STKc_ACVR1_ALK1, Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RTVARQITLVECIGKGRYGEVWRGQWQGESVAVKIFSSRDEKSWFRETEIYNTVLLRHENILGFIASDMT
SRNSCTQLWLITHYHENGSLYDYLQRTTLDHQEMLRLALSAASGLVHLHTEIFGTQGKPAIAHRDLKSKN
ILVKSNGQCCIADLGLAVTHSQETNQLDVGNNPRVGTKRYMAPEVLDETINTDCFESYKRVDIYAFGLVL
WEVARRCVSGGIVEEYKPPFYDVVPSDPSFEDMRKVVCVDQQRPNIPNRWSSDPTLTAMAKLMKECWYQN
PSARLTALRIKKTLLKIL
>gnl|CDD|271045 cd14143, STKc_TGFbR1_ACVR1b_ACVR1c, Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWL
VSDYHEHGSLFDYLNRYTVTVEGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCC
IADLGLAVRHDSATDTIDIAPNHRVGTKRYMAPEVLDDTINMKHFESFKRADIYALGLVFWEIARRCSIG
GIHEDYQLPYYDLVPSDPSIEEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRI
KKTLSQLS
>gnl|CDD|271046 cd14144, STKc_BMPR1, Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RSVGKGRYGEVWKGKWRGEKVAVKIFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYL
ITDYHENGSLYDFLRGNTLDTQSMLKLAYSAACGLAHLHTEIFGTQGKPAIAHRDIKSKNILVKKNGTCC
IADLGLAVKFISETNEVDLPPNTRVGTKRYMAPEVLDESLNRNHFDAYKMADMYSFGLVLWEIARRCISG
GIVEEYQLPYYDAVPSDPSYEDMRRVVCVERRRPSIPNRWSSDEVLRTMSKLMSECWAHNPAARLTALRV
KKTLGKL
>gnl|CDD|271047 cd14145, STKc_MLK1, Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LEIDFSELVLEEIIGIGGFGKVYRAIWIGDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIAL
RGVCLKEPNLCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIVPVIHRDLKSSNILI
LEKVENGDLSNKILKITDFGLAREWHRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGE
VPFRGIDGLAVAYGVAMNKLSLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQLTAI
>gnl|CDD|271048 cd14146, STKc_MLK4, Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IIGVGGFGKVYRATWKGQEVAVKAARQDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCL
VMEFARGGTLNRALAAANAAPGPRRARRIPPHILVNWAVQIARGMLYLHEEAVVPILHRDLKSSNILLLE
KIEHDDICNKTLKITDFGLAREWHRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVP
YRGIDGLAVAYGVAVNKLTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQLTAI
>gnl|CDD|271049 cd14147, STKc_MLK3, Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAV
CLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLLQP
IENDDMEHKTLKITDFGLAREWHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPY
RGIDCLAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL
>gnl|CDD|271050 cd14148, STKc_MLK2, Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K)
IIGVGGFGKVYKGLWRGEEVAVKAARQDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCL
VMEYARGGALNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAIVPIIHRDLKSSNILILEPIENDDLSGK
TLKITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVA
YGVAMNKLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEDI
>gnl|CDD|271051 cd14149, STKc_C-Raf, Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNI
LLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIF
LHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSILWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGE
LPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCIKKVKEERPLFPQILSSIELLQHSLPK
INR
>gnl|CDD|271052 cd14150, STKc_A-Raf, Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EVSMLKRIGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNF
AIITQWCEGSSLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDF
GLATVKTRWSGSQQVEQPSGSILWMAPEVIRMQDTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQI
IFMVGRGYLSPDLSKLSSNCPKAMKRLLIDCLKFKREERPLFPQILVSIELLQRL
>gnl|CDD|271053 cd14151, STKc_B-Raf, Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFM
GYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHED
LTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYS
NINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSL
>gnl|CDD|271054 cd14152, STKc_KSR1, Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QIELGELIGQGRWGKVHRGRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPH
LAIITSFCKGRTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDF
GLFGISGVVQEGRRENELKLPHDWLCYLAPEIVREMTPGKDEDCLPFSKAADVYAFGTIWYELQARDWPL
KNQPAEALIWQIGSGEGMKQVLTTISLGKEVTEILSACWAFDLEERPSFTLLMDMLEKLPKLNRRLSHP
>gnl|CDD|271055 cd14153, PK_KSR2, Pseudokinase domain of Kinase Suppressor of Ras 2. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPH
LAIITSLCKGRTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDF
GLFTISGVLQAGRREDKLRIQSGWLCHLAPEIIRQLSPETEEDKLPFSKHSDVFAFGTIWYELHAREWPF
KTQPAEAIIWQVGSGMKPNLSQIGMGKEISDILLFCWAYEQEERPTFSKLMEMLEKLPKR
>gnl|CDD|271056 cd14154, STKc_LIMK, Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITE
YIPGGTLKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARL
IVEERLPSGNMSPSETLRHLKSPDRKKRYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRVEA
DPDYLPRTKDFGLNVDSFREKFCAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEALYLHL
>gnl|CDD|271057 cd14155, PKc_TESK, Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYI
NGGNLEQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVGDFGLAEK
IPDYSDGKEKLAVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEIIARIQADPDYLPRTEDFGLDYDAF
QHMVGDCPPDFLQLAFNCCNMDPKSRPSFHDIVKTLEEILEKL
>gnl|CDD|271058 cd14156, PKc_LIMK_like_unk, Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGSGFFSKVYKVTHGATGKVMVVKIYKNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYV
SGGCLEELLAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAR
EVGEMPANDPERKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIPADPEVLPRTGDFGLDV
QAFKEMVPGCPEPFLDLAASCCRMDAFKRPSFAELLDELEDIAETL
>gnl|CDD|271059 cd14157, STKc_IRAK2, Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ISEGTFADIYKGYRHGKQYVIKRLKETECESPKSTERFFQTEVQICFRCCHPNILPLLGFCVESDCHCLI
YPYMPNGSLQDRLQQQGGSHPLPWEQRLSISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSG
LRLCPVDKKSVYTMMKTKVLQISLAYLPEDFVRHGQLTEKVDIFSCGVVLAEILTGIKAMDEFRSPVYLK
DLLLEEIQRAKEGSQSKHKSPESLAAKEICSKYLDKRAGLLPENVAFSLAFAACLCLRKKNPLLPEVYEI
VEKAEQCLR
>gnl|CDD|271060 cd14158, STKc_IRAK4, Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FHELKNMTNNFDERPISVGGNKLGEGGFGVVFKGYINDKNVAVKKLAAMVDISTEDLTKQFEQEIQVMAK
CQHENLVELLGYSCDGPQLCLVYTYMPNGSLLDRLACLNDTPPLSWHMRCKIAQGTANGINYLHENNHIH
RDIKSANILLDETFVPKISDFGLARASEKFSQTIMTERIVGTTAYMAPEALRGEITPKSDIFSFGVVLLE
IITGLPPVDENRDPQLLLDIKEEIEDEEKTIEDYVDKKMGDWDSTSIEAMYSVASQCLNDKKNRRPDIAK
VQQLLQEL
>gnl|CDD|271061 cd14159, STKc_IRAK1, Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGEGGFGCVYQAVMRNTEYAVKRLKEDSELDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLI
YVYLPNGSLEDRLHCQVSCPCLSWSQRLHVLLGTARAIQYLHSDSPSLIHGDVKSSNILLDAALNPKLGD
FGLARFSRRPKQPGMSSTLARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVDSC
SPTKYLKDLVKEEEEAQHTPTTMTHSAEAQAAQLATSICQKHLDPQAGPCPPELGIEISQLACRCLHRRA
KKRPPMTEVFQELERL
>gnl|CDD|271062 cd14160, PK_IRAK3, Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3. The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGEGEIFEVYRVRIGNRSYAVKLFKQEKKMQWKKHWKRFLSELEVLLLFQHPNILELAAYFTETEKFCLV
YPYMQNGTLFDRLQCHGVTKPLSWHERINILIGIAKAIHYLHNSQPCTVICGNISSANILLDDQMQPKLT
DFALAHFRPHLEDQSCTINMTTALHKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLTGCKVVLDDPKH
LQLRDLLHELMEKRGLDSCLSFLDLKFPPCPRNFSAKLFRLAGRCTATKAKLRPDMDEVLQRLEST
>gnl|CDD|271063 cd14161, STKc_NUAK2, Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LKHRYEFLETLGKGTYGRVKKARDSSGRLVAIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEV
FENSSKIVIVMEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGN
IKIADFGLSNLYNQDKFLQTYCGSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKIL
VKQISSGAYREPTKPSDACGLIRWLLMVNPERRATLEDVASHWWV
>gnl|CDD|271064 cd14162, STKc_TSSK4-like, Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GYIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKFLPREIEVIKGLKHPNLICFYEAIE
TTSRVYIIMELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLK
ITDFGFARGVMKTKDGKPKLSETYCGSYAYASPEILRGIPYDPFLSDIWSMGVVLYTMVYGRLPFDDSNL
KVLLKQVQRRVVFPKNPTVSEECKDLILRMLSPVKKRITIEEIKRDPWF
>gnl|CDD|271065 cd14163, STKc_TSSK3-like, Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GYQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRFLPRELQIVERLDHKNIIHVYEMLE
SADGKIYLVMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFTLK
LTDFGFAKQLPKGGRELSQTFCGSTAYAAPEVLQGVPHDSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKM
LCQQQKGVSLPGHLGVSRTCQDLLKRLLEPDMVLRPSIEEVSWHPWL
>gnl|CDD|271066 cd14164, STKc_TSSK6-like, Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GYTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIE
VANGRLYIVMEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRKI
KIADFGFARFVEDYPELSTTFCGSRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPFDETNVRRL
RLQQRGVLYPSGVALEEPCRALIRTLLQFNPSTRPSIQQVAGNSWL
>gnl|CDD|271067 cd14165, STKc_TSSK1_2-like, Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RGYILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKFLPRELEILARLNHKSIIKTYEIF
ETSDGKVYIVMELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFN
IKLTDFGFSKRCLRDENGRIVLSKTFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYDDS
NVKKMLKIQKEHRVRFPRSKNLTSECKDLIYRLLQPDVSQRLCIDEVLSHPWL
>gnl|CDD|271068 cd14166, STKc_CaMKI_gamma, Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IRETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYE
STTHYYLVMQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENS
KIMITDFGLSKMEQNGIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLF
EKIKEGYYEFESPFWDDISESAKDFIRHLLEKNPSKRYTCEKALSHPWIIGNTALHRDIYPSVSEQIQKN
FAKSK
>gnl|CDD|271069 cd14167, STKc_CaMKI_alpha, Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IRDIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIY
ESGGHLYLIMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDED
SKIMISDFGLSKIEGSGSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAK
LFEQILKAEYEFDSPYWDDISDSAKDFIQHLMEKDPEKRFTCEQALQHPWIAG
>gnl|CDD|271070 cd14168, STKc_CaMKI_delta, Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
WKKQVEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENI
VALEDIYESPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLL
YFSQDEESKIMISDFGLSKMEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF
YDENDSKLFEQILKADYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQALRHPWIAGDTALCKNIHE
SVSAQIRKNFAKSKWRQAFNA
>gnl|CDD|271071 cd14169, STKc_CaMKI_beta, Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
INSVYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVENEIAVLRRINHENIVSLEDIY
ESPTHLYLAMELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFED
SKIMISDFGLSKIEAQGMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSEL
FNQILKAEYEFDSPYWDDISESAKDFIRHLLERDPEKRFTCEQALQHPWISGDTALDRDIHGSVSEQ
>gnl|CDD|271072 cd14170, STKc_MAPKAPK2, Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAG
RKCLLIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPN
AILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLA
ISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSR
VLKEDKERWEDVKEEMTSALATM
>gnl|CDD|271073 cd14171, STKc_MAPKAPK5, Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SILEEYEVNWTQKLGTGISGPVRVCVKKSTGERFALKILLDRPKARTEVRLHMMCSGHPNIVQIYDVYAN
SVQFPGESSPRARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENL
LLKDNSEDAPIKLCDFGFAKVDQGDLMTPQFTPYYVAPQVLEAQRRHRKERSGIPTSPTPYTYDKSCDMW
SLGVIIYIMLCGYPPFYSEHPSRTITKDMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTI
EEVLHHPWL
>gnl|CDD|271074 cd14172, STKc_MAPKAPK3, Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VTDDYKLSKQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHHWRASGGPHIVHILDVYENMH
HGKRCLLIIMECMEGGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKE
KDAVLKLTDFGFAKETTVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTG
QAISPGMKRRIRMGQYGFPNPEWAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI
>gnl|CDD|271075 cd14173, STKc_Mnk2, Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DVYQLQEEVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREVEMLYQCQGHRNVLELIEFFE
EEDKFYLVFEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVS
PVKICDFDLGSGIKLNSDCSPISTPELLTPCGSAEYMAPEVVEAFNEEASIYDKRCDLWSLGVILYIMLS
GYPPFVGRCGSDCGWDRGEACPACQNMLFESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAA
QVLQHPWV
>gnl|CDD|271076 cd14174, STKc_Mnk1, Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DLYRLTDELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQGNKNILELIEFFE
DDTRFYLVFEKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVS
PVKICDFDLGSGVKLNSACTPITTPELTTPCGSAEYMAPEVVEVFTDEATFYDKRCDLWSLGVILYIMLS
GYPPFVGHCGTDCGWDRGEVCRVCQNKLFESIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAA
QVLQHPWVQ
>gnl|CDD|271077 cd14175, STKc_RSK1_C, C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHV
YLVTELMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNPESLRI
CDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEI
LTRIGSGKFTLSGGNWNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWITQKDKLPQSQLNHQDVQLVK
GAMAATYSALN
>gnl|CDD|271078 cd14176, STKc_RSK2_C, C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYG
QHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLK
PSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTM
LTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVH
WDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQRRGIKKITSTAL
>gnl|CDD|271079 cd14177, STKc_RSK4_C, C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QFTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVYDDG
RYVYLVTELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANADS
IRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTP
EEILLRIGSGKFSLSGGNWDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWIACRDQLPHYQLNRQDAP
HLVKGAMAATYSALN
>gnl|CDD|271080 cd14178, STKc_RSK3_C, C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FTDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGK
FVYLVMELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNPESI
RICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANGPDDTPE
EILARIGSGKYALSGGNWDSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWIVNREYLSQNQLSRQDVHL
VKGAMAATYFALN
>gnl|CDD|271081 cd14179, STKc_MSK1_C, C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PFYQHYELDLKDKPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQREIAALKLCEGHPNIVKLHEV
YHDQLHTFLVMELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESD
NSEIKIIDFGFARLKPPDNQPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDK
SLTCTSAEEIMKKIKQGDFSFEGEAWKNVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQDGSQLSSNP
LMTPDILGSSGASVHTCVKATFHAFNKYKR
>gnl|CDD|271082 cd14180, STKc_MSK2_C, C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FFQCYELDLEEPALGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQREVAALRLCQSHPNIVALHEVL
HDQYHTYLVMELLRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDG
AVLKVIDFGFARLRPQGSRPLQTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGK
MFHNHAADIMHKIKEGDFSLEGEAWKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQGGSALSSTPL
MTPDVLESSGPAVRTGVNATFMAFNRGKR
>gnl|CDD|271083 cd14181, STKc_PhKG2, Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DWAGAKEFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERLSPEQLEEVRSSTLKEIHILR
QVSGHPSIITLIDSYESSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHR
DLKPENILLDDQLHIKLSDFGFSCHLEPGEKLRELCGTPGYLAPEILKCSMDETHPGYGKEVDLWACGVI
LFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPFF
>gnl|CDD|271084 cd14182, STKc_PhKG1, Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FYEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSPEEVQELREATLKEIDILRKVSGHP
NIIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPEN
ILLDDDMNIKLTDFGFSCQLDPGEKLREVCGTPGYLAPEIIECSMDDNHPGYGKEVDMWSTGVIMYTLLA
GSPPFWHRKQMLMLRMIMSGNYQFGSPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQY
>gnl|CDD|271085 cd14183, STKc_DCKL1, Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PASISERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLI
EEMDMPTELYLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEH
QDGSKSLKLGDFGLATVVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGD
DQEVLFDQILMGQVDFPSPYWDNVSDSAKELITMMLQVDVDQRYSALQVLEHPWVNDD
>gnl|CDD|271086 cd14184, STKc_DCKL2, Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLIEEMDT
PAELYLVMELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTK
SLKLGDFGLATVVEGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDL
FDQILLGKLEFPSPYWDNITDSAKELISHMLQVNVEARYTAEQILSHPW
>gnl|CDD|271087 cd14185, STKc_DCKL3, Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3). STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HYEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIESEILIIKSLSHPNIVKLFEVYETE
KEIYLILEYVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKSTT
LKLADFGLAKYVTGPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERDQEELF
QIIQLGHYEFLPPYWDNISEAAKDLISRLLVVDPEKRYTAKQVLQHPW
>gnl|CDD|271088 cd14186, STKc_PLK4, Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYF
EDSNYVYLVLEMCHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMN
IKIADFGLATQLKMPHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNT
LNKVVLADYEMPAFLSREAQDLIHQLLRKNPADRLSLSSVLDHPFM
>gnl|CDD|271089 cd14187, STKc_PLK1, Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VDPRTRRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVV
GFHGFFEDNDFVYVVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFL
NDDMEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETS
CLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGY
>gnl|CDD|271090 cd14188, STKc_PLK2, Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KRYCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYF
EDKENIYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMEL
KVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETY
RCIREARYSLPSSLLAPAKHLIASMLSKNPEDRPSLDEIIRHDFF
>gnl|CDD|271091 cd14189, STKc_PLK3, Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RSYCKGRLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHF
EDAENIYIFLELCSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMEL
KVGDFGLAARLEPPEQRKKTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETY
RCIKQVKYTLPASLSLPARHLLAGILKRNPGDRLTLDQILEHEFF
>gnl|CDD|271092 cd14190, STKc_MLCK2, Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SSTFSIHSKEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAI
ETPNEIVLFMEYVEGGELFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTG
HQVKIIDFGLARRYNPREKLKVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTE
TLNNVLMGNWYFDEETFEHVSDEAKDFVSNLIIKERSARMSATQCLKHPWL
>gnl|CDD|271093 cd14191, STKc_MLCK1, Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEE
KANIVMVLEMVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTK
IKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETL
ANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKARLTCTQCLQHPWL
>gnl|CDD|271094 cd14192, STKc_MLCK3, Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NSYYAVCPHEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQLNHVNLIQLYDAF
ESKTNLTLIMEYVDGGELFDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTG
NQIKIIDFGLARRYKPREKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAE
TMNNIVNCKWDFDAEAFENLSEEAKDFISRLLVKEKSCRMSATQCLKHEWL
>gnl|CDD|271095 cd14193, STKc_MLCK4, Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
NSYYNVNKEEILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQLNHANLIQLYDAF
ESRNDIVLVMEYVDGGELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREA
NQVKIIDFGLARRYKPREKLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNE
TLNNILACQWDFEDEEFADISEEAKDFISKLLIKEKSWRMSASEALKHPWL
>gnl|CDD|271096 cd14194, STKc_DAPK1, Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNV
ITLHEVYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIM
LLDRNVPKPRIKIIDFGLAHKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASP
FLGDTKQETLANVSAVNYEFEDEYFSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI
>gnl|CDD|271097 cd14195, STKc_DAPK3, Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SMVEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVNILREIQHPNI
ITLHDIFENKTDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIM
LLDKNVPNPRIKLIDFGIAHKIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASP
FLGETKQETLTNISAVNYDFDEEYFSNTSELAKDFIRRLLVKDPKKRMTIAQSLEHSWIKA
>gnl|CDD|271098 cd14196, STKc_DAPK2, Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHPNI
ITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIM
LLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASP
FLGDTKQETLANITAVSYDFDEEFFSHTSELAKDFIRKLLVKETRKRLTIQEALRHPWI
>gnl|CDD|271099 cd14197, STKc_DRAK1, Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RSEPFQERYSLSPGRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQANPW
VINLHEVYETASEMILVLEYAAGGEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQ
NILLTSESPLGDIKIVDFGLSRILKNSEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGI
SPFLGDDKQETFLNISQMNVSYSEEEFEHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL
>gnl|CDD|271100 cd14198, STKc_DRAK2, The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
SMDNFNNFYILTSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSNPRV
VNLHEVYETTSEIILILEYAAGGEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQN
ILLSSIYPLGDIKIVDFGMSRKIGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHES
PFVGEDNQETFLNISQVNVDYSEETFSSVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL
>gnl|CDD|271101 cd14199, STKc_CaMKK2, Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LNQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRQAGFPRRPPPRGARAAPEGCTQPRGPIE
RVYQEIAILKKLDHPNVVKLVEVLDDPSEDHLYMVFELVKQGPVMEVPTLKPLSEDQARFYFQDLIKGIE
YLHYQKIIHRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSETRKIFSGKAL
DVWAMGVTLYCFVFGQCPFMDERILSLHSKIKTQPLEFPDQPDISDDLKDLLFRMLDKNPESRISVPEIK
LHPWVT
>gnl|CDD|271102 cd14200, STKc_CaMKK1, Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
QYKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKQYGFPRRPPPRGSKAAQGEQAKPLAPLERV
YQEIAILKKLDHVNIVKLIEVLDDPAEDNLYMVFDLLRKGPVMEVPSDKPFSEDQARLYFRDIVLGIEYL
HYQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQSFSGKALDV
WAMGVTLYCFVYGKCPFIDEFILALHNKIKNKPVEFPEEPEISEELKDLILKMLDKNPETRITVPEIKVH
PWVT
>gnl|CDD|271103 cd14201, STKc_ULK2, Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
EVVGDFEYSRKDLVGHGAFAVVFKGRHRKKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVAL
YDVQEMPNSVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSY
ASRKKSSVSGIRIKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGK
PPFQANSPQDLRMFYEKNKNLQPSIPRETSPYLADLLLGLLQRNQKDRMDFEAFFSHPFLE
>gnl|CDD|271104 cd14202, STKc_ULK1, Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KFEFSRKDLIGHGAFAVVFKGRHKEKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQ
EIANSVYLVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGR
KSNPNNIRIKIADFGFARYLQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQ
ASSPQDLRLFYEKNKSLSPNIPRETSSHLRQLLLGLLQRNQKDRMDFDEFFHHPFLD
>gnl|CDD|271105 cd14203, PTKc_Src_Fyn_like, Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
VKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEF
MSKGSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARL
IEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYR
MPCPPGCPESLHELMCQCWRKDPEERPTFEYLQSFLED
>gnl|CDD|271106 cd14204, PTKc_Mer, Catalytic Domain of the Protein Tyrosine Kinase, Mer. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DVMIDRNLLSLGKVLGEGEFGSVMEGELQQPDGTNHKVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPN
VIRLLGVCLEVGSQRIPKPMVILPFMKYGDLHSFLLRSRLGSGPQHVPLQTLLKFMIDIALGMEYLSSRN
FLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGV
TMWEIATRGMTPYPGVQNHEIYDYLLHGHRLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLL
ESLP
>gnl|CDD|271107 cd14205, PTKc_Jak2_rpt2, Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
FEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKY
KGVCYSAGRRNLRLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNIL
VENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEK
SKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRV
DQIR
>gnl|CDD|271108 cd14206, PTKc_Aatyk3, Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K)
YLQEIGNGWFGKVILGEIFSDYTPAQVVVKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETI
PFLLIMEFCQLGDLKRYLRAQRKADGMTPDLPTRDLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLL
TSDLTVRIGDYGLSHNNYKEDYYLTPDRLWIPLRWVAPELLDELHGNLIVVDQSKESNVWSLGVTIWELF
EFGAQPYRHLSDEEVLTFVVREQQMKLAKPRLKLPYADYWYEIMQSCWLPPSQRPSVEELHLQLSY
>gnl|CDD|271109 cd14207, PTKc_VEGFR1, Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
KWEFARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCRVVAVKMLKEGATASEYKALMTELKILIHIGHH
LNVVNLLGACTKSGGPLMVIVEYCKYGNLSNYLKSKRDFFVTNKDTSLQEELIKEKKEAEPTGGKKKRLE
SVTSSESFASSGFQEDKSLSDVEEEEEDSGDFYKRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARN
ILLSENNVVKICDFGLARDIYKNPDYVRKGDARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGA
SPYPGVQIDEDFCSKLKEGIRMRAPEFATSEIYQIMLDCWQGDPNERPRFSELVERLGDL
>gnl|CDD|271110 cd14208, PTK_Jak3_rpt1, Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit, common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LTFMESLGKGSFTKIYRGLRTDEEDDERCETEVLLKVMDPTHGNCQESFLEAASIMSQISHKHLVLLHGV
CVGKDSIMVQEFVCHGALDLYLKKQQQKGPVAISWKLQVVKQLAYALNYLEDKQLVHGNVSAKKVLLSRE
GDKGSPPFIKLSDPGVSIKVLDEELLAERIPWVAPECLSDPQNLALEADKWGFGATLWEIFSGGHMPLSA
LDPSKKLQFYNDRKQLPAPHWIELASLIQQCMSYNPLLRPSFRAIIRDLN
>gnl|CDD|271111 cd14209, STKc_PKA, Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSF
KDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYI
KVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI
VSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKG
PGDTSNFDDY
>gnl|CDD|271112 cd14210, PKc_DYRK, Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase. Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis
GDYKVVLGDHIAYRYEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQALVEVKILKHLNDND
PDDKHNIVRYKDSFIFRGHLCIVFELLSINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHC
DLKPENILLKQPSKSSIKVIDFGSSCFEGEKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYT
GYPLFPGENEEEQLACIMEVLGVPPKSLIDKASRRKKFFDSNGKPRPTTNSKGKKRRPGSKSLAQVLKCD
DPSFLDFLKKCLRWDPSERMTPEEALQHPWI
>gnl|CDD|271113 cd14211, STKc_HIPK, Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQENADEFNFVRAYECFQ
HKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQ
PYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSSEYD
QIRYISQTQGLPAEHLLNAATKTSRFFNRDPDSPYPLWRLKTPEEHEAETGIKSKEARKYIFNCLDDMAQ
VNGPSDLEGSELLAEKADRREFIDLLKRMLTIDQERRITPGEALNHPFV
>gnl|CDD|271114 cd14212, PKc_YAK1, Catalytic domain of the Dual-specificity protein kinase, YAK1. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAMLEIAILTLLNTKYDPEDKHHIVRLLDH
FMHHGHLCIVFELLGVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLD
SPEIKLIDFGSACFENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQ
LSRIIEMLGMPPDWMLEKGKNTNKFFKKVAKSGGRSTYRLKTPEEFEAENNCKLEPGKRYFKYKTLEDII
MNYPMKKSKKEQIDKEMETRLAFIDFLKGLLEYDPKKRWTPDQALNHPFI
>gnl|CDD|271115 cd14213, PKc_CLK1_4, Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HLICQSGDVLRARYEIVDTLGEGAFGKVVECIDHKMGGMHVAVKIVKNVDRYREAARSEIQVLEHLNTTD
PNSTFRCVQMLEWFDHHGHVCIVFELLGLSTYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHT
DLKPENILFVQSDYVVKYNPKMKRDERTLKNPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWS
QPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFHHDQLDWDEHSSAGR
YVRRRCKPLKEFMLSQDVDHEQLFDLIQKMLEYDPAKRITLDEALKHPFF
>gnl|CDD|271116 cd14214, PKc_CLK3, Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
GHLVCRIGDWLQERYEIVGDLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEK
DKENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHIRHMAYQLCHALKFLHENQLTH
TDLKPENILFVNSEFDTLYNESKSCEEKSVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGW
AQPCDVWSLGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHMIHRTRKQKYFYKGSLVWDENSSDG
RYVSENCKPLMSYMLGDSLEHTQLFDLLRRMLEFDPALRITLKEALLHPFF
>gnl|CDD|271117 cd14215, PKc_CLK2, Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
HLIYRSGDWLQERYEIVSTLGEGTFGRVVQCIDHRRGGARVALKIIKNVEKYKEAARLEINVLEKINEKD
PENKNLCVQMFDWFDYHGHMCISFELLGLSTFDFLKENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHT
DLKPENILFVNSDYELTYNLEKKRDERSVKSTAIRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWS
QPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERILGPIPSRMIRKTRKQKYFYHGRLDWDENTSAGR
YVRENCKPLRRYLTSEAEEHHQLFDLIESMLEYEPSKRLTLAAALKHPFF
>gnl|CDD|271118 cd14216, STKc_SRPK1, Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHYTETALDEIKLLKSVRNSDPND
PNREMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIRQVLQGLDYLHTKCR
IIHTDIKPENILLSVNEQYIRRLAAEATEWQRNFLVNPLEPKNAEKLKVKIADLGNACWVHKHFTEDIQT
RQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIALIIELLGKVPRKLIVAG
KYSKEFFTKKGDLKHITKLKPWGLFEVLVEKYEWSQEEAAGFTDFLLPMLELIPEKRATAAECLRHPWL
>gnl|CDD|271119 cd14217, STKc_SRPK2, Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLRCVRESDP
EDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPIRCVKSIIRQVLQGLDYLHSK
CKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPDLLVNPLDPRNADKIRVKIAD
LGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIA
HIIELLGCIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMV
PEKRASAGECLRHPWL
>gnl|CDD|271120 cd14218, STKc_SRPK3, Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PVKIGDLFNGRYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAVHYTETAVDEIKLLKCVRDSDPSD
PKRETIVQLIDDFKISGVNGVHVCMVLEVLGHQLLKWIIKSNYQGLPLPCVKSILRQVLQGLDYLHTKCK
IIHTDIKPENILMCVDEGYVRRLAAEATIWQQAGAPPPSGSSVSFGASDFLVNPLEPQNADKIRVKIADL
GNACWVHKHFTEDIQTRQYRALEVLIGAEYGTPADIWSTACMAFELATGDYLFEPHSGEDYTRDEDHIAH
IVELLGDIPPHFALSGRYSREYFNRRGELRHIKNLKHWGLYEVLVEKYEWPLEQAAQFTDFLLPMMEFLP
EKRATAAQCLQHPWL
>gnl|CDD|271121 cd14219, STKc_BMPR1b, Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RTIAKQIQMVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIK
GTGSWTQLYLITDYHENGSLYDYLKSTTLDTKAMLKLAYSSVSGLCHLHTEIFSTQGKPAIAHRDLKSKN
ILVKKNGTCCIADLGLAVKFISDTNEVDIPPNTRVGTKRYMPPEVLDESLNRNHFQSYIMADMYSFGLIL
WEVARRCVSGGIVEEYQLPYHDLVPSDPSYEDMREIVCIKRLRPSFPNRWSSDECLRQMGKLMTECWAHN
PASRLTALRVKKTLAKMSESQDIKL
>gnl|CDD|271122 cd14220, STKc_BMPR1a, Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYL
ITDYHENGSLYDFLKCTTLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGTCC
IADLGLAVKFNSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHFQAYIMADIYSFGLIIWEMARRCVTG
GIVEEYQLPYYDMVPSDPSYEDMREVVCVKRLRPTVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRI
KKTLAKM
>gnl|CDD|271123 cd14221, STKc_LIMK1, Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITE
YIKGGTLRGIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARL
MVDEKTQPEGLRSLKKPDRKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLP
RTMDFGLNVRGFLDRYCPPNCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETLRMHL
>gnl|CDD|271124 cd14222, STKc_LIMK2, Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTE
FIEGGTLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLI
VEEKKKPPPDKPTTKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEIIGQVYAD
PDCLPRTLDFGLNVRLFWEKFVPKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFEALSLYL
>gnl|CDD|271125 cd14223, STKc_GRK2, Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSY
AFHTPDKLSFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFG
HVRISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK
HEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRLGCMGRGAQEVKEEPFFRGLDWQMVFLQKYPPP
LIPPRGEVNAADAFDIGSFDEEDTKGIKLLESDQELYRNFP
>gnl|CDD|271126 cd14224, PKc_DYRK2_3, Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
PEQAMKQYMHKLTAYEHHEIFNYPEIYFVGPNAKKRQGVIGGPNNGGYDDEQGSYIHVPHDHIAYRYEVL
KVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILEHLKKQDKDNTMNVIHMLESFTFRN
HICMTFELLSMNLYELIKKNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGIK
VIDFGSSCYEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMI
ELLGMPPQKLLETSKRAKNFISSKGYPRYCTVTTLPDGSVVLNGGRSRRGKMRGPPGSKDWVTALKGCDD
PLFLDFLKRCLEWDPAARMTPSQALRHPWL
>gnl|CDD|271127 cd14225, PKc_DYRK4, Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YPEIWFLGLEAKKIEGVPGAPQNNGYDDENGSYLKVLHDHIAYRYEILEVIGKGSFGQVVKALDHKTNEH
VAIKIIRNKKRFHHQALVEVKILDALRRKDRDNSHNVIHMKEYFYFRNHLCITFELLGMNLYELIKKNNF
QGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSSIKVIDFGSSCYEHQRVYTYIQSRF
YRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVLGLPPPELIENAQRRRLFFD
SKGNPRCITNSKGKKRRPNSKDLASALKTSDPLFLDFIRRCLEWDPSKRMTPDEALQHEWI
>gnl|CDD|271128 cd14226, PKc_DYRK1, Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
YDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHD
TENKYYIVRLKRHFMFRNHLCLVFELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPELSII
HCDLKPENILLCNPKRSAIKIIDFGSSCQLGQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEM
HTGEPLFSGANEVDQMNKIVEVLGMPPVHMLDQAPKARKFFEKLPDGTYYLKKTKDGKKYKPPGSRKLHE
ILGVETGGPGGRRAGEPGHTVEDYLKFKDLILRMLDYDPKTRITPAEALQHSFFKRTAD
>gnl|CDD|271129 cd14227, STKc_HIPK2, Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DYQLVQHEVLCSMTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLST
ESADDYNFVRAYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIH
ADLKPENIMLVDPSRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIA
ELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFNRDTDSPYPLWRLKTPEDHEAETGIKS
KEARKYIFNCLDDMAQVNMTTDLEGSDMLVEKADRREFIDLLKKMLTIDADKRITPIETLNHPFVTMTHL
LDFPH
>gnl|CDD|271130 cd14228, STKc_HIPK1, Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
DYQLVQHEILCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSS
ENADEYNFVRSYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIH
ADLKPENIMLVDPVRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIA
ELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTSRFFNRDPNLGYPLWRLKTPEEHELETGIKS
KEARKYIFNCLDDMAQVNMSTDLEGTDMLAEKADRREYIDLLKKMLTIDADKRITPLKTLNHPFVTMTHL
LDFPH
>gnl|CDD|271131 cd14229, STKc_HIPK3, Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K)
TYEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILARLSNENADEFNFVRAYECF
QHRNHTCLVFEMLEQNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVR
QPYRVKVIDFGSASHVSKTVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEY
DQIRYISQTQGLPGEQLLNVGTKTSRFFCRETDAPYSSWRLKTLEEHEAETGMKSKEARKYIFNSLDDIA
HVNMVMDLEGSDLLAEKADRREFVALLKKMLLIDADLRITPADTLSHPFV
>gnl|CDD|410578 cd14230, GAT_GGA, canonical GAT domain found in metazoan and fungal ADP-ribosylation factor (Arf)-binding proteins (GGAs). GGAs, also called Golgi-localized gamma-ear-containing Arf-binding proteins, belong to a family of ubiquitously expressed, monomeric, motif-binding cargo/clathrin adaptor proteins that regulate clathrin-mediated trafficking of cargo proteins from the trans-Golgi network (TGN) to endosomes. GGAs also play important roles in ubiquitin-dependent sorting of cargo proteins both in biosynthetic and endocytic pathways. The family includes three GGAs (GGA1, GGA2, and GGA3) identified in mammals and two GGAs (Gga1p and Gga2p) identified in the budding yeast Saccharomyces cerevisiae. All these GGAs have a multidomain structure consisting of: an N-terminal VHS (Vps27/Hrs/Stam) domain that binds acidic-cluster dileucine (DxxLL)-type sorting signals (where x is any amino acid) found in the cytoplasmic tail of TGN sorting receptors; a GAT (GGA and TOM) domain that interacts with class I GTP-bound form of Arf proteins, Rabaptin-5, ubiquitin, and the tumor susceptibility gene 101 product (TSG101); a largely unstructured hinge region that contains clathrin-binding motifs; and a C-terminal GAE (gamma-adaptin ear homology) domain that binds accessory proteins. In contrast to other GGAs-like proteins, members of this family contain a GAT N-terminal region, a helix-loop-helix in the complex with Arf1-GTP
TLEEAKNNVDLLDEMLLSYSQEDSSDGDNELMKELYDQLENMRPTLFKLASETEENDNSLGDVLQASDNV
NRVINKYKDI
>gnl|CDD|410579 cd14231, GAT_GGA-like_plant, canonical GAT domain found in uncharacterized Golgi-localized gamma ear-containing Arf-binding protein (GGA)-like proteins mainly found in plants. The family includes a group of uncharacterized plant proteins containing an N-terminal VHS (Vps27p/Hrs/STAM)-domain and a GAT (GGA and TOM1) domain. Both domains are also present in Golgi-localized gamma ear-containing Arf-binding proteins (GGAs), which belong to a family of ubiquitously expressed, monomeric, motif-binding cargo/clathrin adaptor proteins that regulate clathrin-mediated trafficking of cargo proteins from the trans-Golgi network (TGN) to endosomes. In contrast to GGA proteins, members in this family do not have either a GAE (gamma-adaptin ear homology) domain or a clathrin-binding motif. The canonical GAT domain is a monomeric three-helix bundle that binds ubiquitin
DLQVARNSLELLSDMLNAVDPRDPEALKDELTVDLVEQCRQSQPRVMQLVESTGDEGLLFQALELNDELQ
RVLSKHDAI
>gnl|CDD|410580 cd14232, GAT_LSB5, canonical GAT domain found in yeast LAS seventeen-binding protein 5 (Lsb5p) and similar proteins. Lsb5p, also called LAS17-binding protein 5, is a Golgi-localized gamma ear-containing Arf-binding protein (GGA)-like protein located to the plasma membrane in an actin-independent manner. It plays important roles in membrane-trafficking events through association with the actin regulators, the yeast Wiskott-Aldrich syndrome protein (WASP) homologue Las17p and the cortical protein Sla1p, the yeast Arf3p (orthologous with mammalian Arf6), and ubiquitin. Lsb5p contains an N-terminal VHS (Vps27p/Hrs/STAM)-domain and a GAT (GGA and TOM1) domain. In contrast to GGA proteins, Lsb5p harbors a C-terminal NPF (Asn-Pro-Phe) motif, but does not have either a GAE (gamma-adaptin ear homology) domain or a clathrin-binding motif. The canonical GAT domain is a monomeric three-helix bundle that binds ubiquitin
IADASQAATNLVNALQLVNRETERVSDDAEVQERFEKCKQLRRKILRYIQLVEDEEYLGSLLHANEELVA
ALEAYDEL
>gnl|CDD|410581 cd14233, GAT_TOM1_like, canonical GAT domain found in target of myb protein 1 (Tom1) protein family. Tom1 and its related proteins, Tom1L1 and Tom1L2, form a protein family sharing an N-terminal VHS (Vps27p/Hrs/STAM)-domain followed by a GAT (GGA and TOM1) domain, both of which are also conserved in Golgi-localized gamma ear-containing Arf-binding proteins (GGAs). In contrast to GGAs, the Tom1 family proteins bind to ubiquitin, ubiquitinated proteins, and Toll-interacting protein (Tollip) through its GAT domain, but do not associate with Arf GTPases through its GAT domain nor with acidic cluster-dileucine sequences through its VHS domain. In addition, the Tom1 family proteins recruit clathrin onto endosomes through their C-terminal region. In their C-terminal clathrin-binding regions, Tom1 and Tom1L2 are similar to each other, but distinguishable from Tom1L1. The yeast S. cerevisiae does not contain homologous proteins of the Tom1 family. The canonical GAT domain is a monomeric three-helix bundle that binds ubiquitin
IAKLRSELDVVEGNLKVMSEMLTELVPGQENPDDLELLQELNSTCRAMQQRVVELISQVSNEEVTEELLR
VNDDLNNVFLRYERFER
>gnl|CDD|410582 cd14234, GAT_GGA_meta, canonical GAT domain found in metazoan ADP-ribosylation factor (Arf)-binding proteins (GGAs). GGAs, also called Golgi-localized gamma-ear-containing Arf-binding proteins, belong to a family of ubiquitously expressed, monomeric, motif-binding cargo/clathrin adaptor proteins that regulate clathrin-mediated trafficking of cargo proteins from the trans-Golgi network (TGN) to endosomes. Moreover, GGAs play important roles in ubiquitin-dependent sorting of cargo proteins both in biosynthetic and endocytic pathways. Three GGAs (GGA1, GGA2, and GGA3) have been identified in mammals. They may appear to behave similarly, since all of them have a multidomain structure consisting of: an N-terminal VHS (Vps27/Hrs/Stam) domain that binds the acidic-cluster dileucine (DxxLL)-type sorting signals (where x is any amino acid) found in the cytoplasmic tail of TGN sorting receptors; a GAT (GGA and TOM) domain that interacts with class I GTP-bound form of Arf proteins, Rabaptin-5, ubiquitin, and the tumor susceptibility gene 101 product (TSG101); a largely unstructured hinge region that contains clathrin-binding motifs; and a C-terminal GAE (gamma-adaptin ear homology) domain that binds accessory proteins. However, the three GGAs have some differences, which suggest they may possess their own distinct roles. For instance, both GGA1 and GGA3, but not GGA2, contains an internal DxxLL motif that binds to it own VHS domain. Only a portion of the VHS domain of GGA2 possesses distant structural homology to that of GGA1 or GGA3. Moreover, the binding affinity of GGA2 to ubiquitin is quite lower than that of GGA1 or GGA3. In addition, GGA3 has a short splicing variant that is predominantly expressed in human cell lines and tissues except the brain. It does have a VHS domain, but it is unable to bind to the DxxLL motif. GGA2 and GGA3 undergo epidermal growth factor (EGF)-induced phosphorylation
KRLLELEEVNNNVKLLNEMLDHYSPGESSQDELELMKELYESCEKMRPTLFRLASETDDDDEGLADILQA
NDELTRVMQRYKNL
>gnl|CDD|410583 cd14235, GAT_GGA_fungi, canonical GAT domain found in fungal ADP-ribosylation factor (Arf)-binding proteins (GGAs). GGAs, also called Golgi-localized gamma-ear-containing Arf-binding proteins, belong to a family of ubiquitously expressed, monomeric, motif-binding cargo/clathrin adaptor proteins that regulate clathrin-mediated trafficking of cargo proteins from the trans-Golgi network (TGN) to endosomes. Two GGAs (Gga1p and Gga2p) have been identified in the budding yeast Saccharomyces cerevisiae. Yeast GGAs play important roles in the carboxypeptidase Y (CPY) pathway, vacuole biogenesis, alpha-factor maturation, and interactions with clathrin. They have a multidomain structure consisting of VHS (Vps27/Hrs/ STAM), GAT (GGA and TOM), hinge, and GAE (gamma-adaptin ear) domains. Both Gga1p and Gga2p function as effectors of Arf in yeast. They interact with Arf1p and Arf2p in a GTP-dependent manner. Moreover, Gga2p mediates sequential ubiquitin-independent and ubiquitin-dependent steps in the trafficking of ARN1, a ferrichrome transporter in S. cerevisiae, from the TGN to the vacuole. It also acts as a phosphatidylinositol 4-phosphate effector at the Golgi exit, which binds directly to the TGN PtdIns(4)-kinase Pik1p and contributes to Pik1p recruitment. In addition, Gga2p is required for sorting of the yeast siderophore iron transporter1 (Sit1) to the vacuolar pathway. The GAT domain of GGAs interacts with class I GTP-bound form of Arf proteins, Rabaptin-5, ubiquitin, and/or the tumor susceptibility gene 101 product (TSG101)
DYKAQVAEELEKLKRKAILLNEMLNNATPGEIDVEGDTYDELASSLKSAQPKIQKIIEEESEDEESVQKL
LELNDLINSLLERYDLLKKGDA
>gnl|CDD|260094 cd14236, GAT_TOM1, canonical GAT domain found in target of Myb protein 1 (Tom1). Tom1 was originally identified by its induced expression by the v-Myb oncogene. It is predominantly present in the cytosol and can interact with clathrin, endofin, Toll-interacting protein (Tollip), and ubiquitinated proteins. It acts as a linker protein to regulate the ability of endofin to recruit clathrin onto the sorting endosome. Moreover, Tom1 functions as a negative regulator of IL-1beta and tumor necrosis factor (TNF)-alpha-induced signaling pathways. It also plays a role in the TLR2/4 signaling pathways. Tom1 contains an N-terminal VHS (Vps27p/Hrs/STAM)-domain, a GAT (GGA and TOM1) domain and a C-terminal clathrin-binding region, both of which are conserved in Golgi-localized gamma ear-containing Arf-binding proteins (GGAs). In contrast to GGAs, Tom1 binds to ubiquitin, ubiquitinated proteins, and Tollip through its GAT domain, but does not associate with Arf GTPases through its GAT domain nor with acidic cluster-dileucine sequences through its VHS domain. The canonical GAT domain is a monomeric three-helix bundle that binds ubiquitin
PEQIGKLRSELEMVSGNVRVMSEMLTELVPTQAEPADLELLQELNRTCRAMQQRVLELIPQIANEQLTEE
LLIVNDNLNNVFLRHERFERFRTGQ
>gnl|CDD|410584 cd14237, GAT_TM1L1, canonical GAT domain found in target of Myb-like protein 1 (Tom1L1). Tom1L1, also called Src-activating and signaling molecule protein (Srcasm), was identified as a substrate of the Src family of protein kinases. It is tyrosine-phosphorylated by Src family kinases and modulates growth factor and Src-mediated signaling pathways. It also plays a potential role in endosomal sorting and ligand-stimulated endocytosis of EGF receptors (EGFR). Tom1L1 is predominantly present in the cytosol and can interact with Toll-interacting protein (Tollip), Hrs or TSG101, clathrin, and ubiquitinated proteins. It contains an N-terminal VHS (Vps27p/Hrs/STAM)-domain, a GAT (GGA and TOM1) domain, and a C-terminal clathrin-binding region, both of which are conserved in Golgi-localized gamma ear-containing Arf-binding proteins (GGAs). It interacts with Tollip through their GAT domain and recuits clathrin onto endosomes through their C-terminal region. However, in the C-terminal clathrin-binding region, Tom1 and Tom1L2 are similar to each other, but distinguishable from Tom1L1. The canonical GAT domain is a monomeric three-helix bundle that binds ubiquitin
PEQIGKLYSELDIVKMNVRVMSAILLENTPGAENPEDMELLEKLYKTCREMQERIMKLLETVENEDVIIE
LIQVNDDLNNVFLRHERFSRNR
>gnl|CDD|410585 cd14238, GAT_TM1L2, canonical GAT domain found in target of Myb-like protein 2 (Tom1L2). Tom1L2, together with Myb protein 1 (Tom1) and target of Myb-like protein 1 (Tom1L1), constitute the Tom1 family. Tom1L2 can interact with Toll-interacting protein (Tollip), clathrin, and ubiquitin. It may play a potential role in endosomal sorting, as well as in the regulation of membrane trafficking that is linked to immunity and cell proliferation. Tom1L2 contains an N-terminal VHS (Vps27p/Hrs/STAM)-domain, a GAT (GGA and TOM1) domain, and a C-terminal clathrin-binding region, both of which are conserved in Golgi-localized gamma ear-containing Arf-binding proteins (GGAs). It interacts with Tollip through their GAT domain and recuits clathrin onto endosomes through their C-terminal region. However, in the C-terminal clathrin-binding region, Tom1 and Tom1L2 are similar to each other, but distinguishable from Tom1L1. The canonical GAT domain is a monomeric three-helix bundle that binds ubiquitin
SEQIARLRSELDIVRGNTKVMSEMLTEMVPGQEDPSDLELLQELNRTCRAMQQRIVELISRVSNEEVTEE
LLHVNDDLNNVFLRYERFERYR
>gnl|CDD|410586 cd14239, GAT_GGA1_GGA2, canonical GAT domain found in ADP-ribosylation factor (Arf)-binding proteins GGA1 and GGA2. This subfamily includes GGA1 and GGA2, both of which belong to a family of ubiquitously expressed, monomeric, motif-binding cargo/clathrin adaptor proteins that regulate clathrin-mediated trafficking of cargo proteins from the trans-Golgi network (TGN) to endosomes. GGA1, also called gamma-adaptin-related protein 1, or Golgi-localized gamma ear-containing Arf-binding protein 1, regulates the low-density lipoprotein and sorting receptor LR11/SorLA endocytic traffic and further alters amyloid-beta precursor protein (APP) intracellular distribution and amyloid-beta production. It is also critical for the effects of beta-site APP-cleaving enzyme-1 (BACE1) on amyloid-beta generation. It interacts with BACE1 and promotes its traffic from early endosomes to late endocytic compartments or the TGN. Moreover, GGA1 acts as a clathrin assembly protein with the ability to polymerize clathrin into tubules. GGA2, also called gamma-adaptin-related protein 2, Golgi-localized gamma ear-containing Arf-binding protein 2, or VHS domain and ear domain of gamma-adaptin (Vear), interacts with the acidic cluster-dileucine motif in the cytoplasmic tail of the cation-independent mannose 6-phosphate receptor (CI-MPR) and further plays a major role in the sorting of lysosomal enzymes. It also mediates a vital function that cannot be compensated for by GGA1 and/or GGA3. Both GGA1 and GGA2 have a multidomain structure consisting of an N-terminal VHS (Vps27/Hrs/Stam) domain, a GAT (GGA and TOM) domain, a largely unstructured hinge region that contains clathrin-binding motifs, and a C-terminal GAE (gamma-adaptin ear homology) domain. The GAT domain of GGAs interacts with class I GTP-bound form of Arf proteins, Rabaptin-5, ubiquitin, and/or the tumor susceptibility gene 101 product (TSG101)
KVSKRVNAIEEVNNNVKLLTEMLMSYSRGELSESSEELMKELYQRCEKMRPTLFRLASDTEDNDEALAEI
LQANDNLTQVINLYKQLV
>gnl|CDD|410587 cd14240, GAT_GGA3, canonical GAT domain found in ADP-ribosylation factor-binding protein GGA3. GGA3, also called Golgi-localized gamma ear-containing Arf-binding protein 3, belongs to a family of ubiquitously expressed, monomeric, motif-binding cargo/clathrin adaptor proteins that regulate clathrin-mediated trafficking of cargo proteins from the trans-Golgi network (TGN) to endosomes. GGA3 interacts selectively with the Met/Hepatocyte Growth Factor receptor tyrosine kinase (RTK) when stimulated. It functions as a specific cargo adaptor to target the Met RTK into recycling tubules, and further coordinates the recycling, signaling and degradative fates of the Met RTK. Moreover, GGA3, together with PACS-1 and the protein kinase CK2, forms a complex that regulates cation-independent mannose-6-phosphate receptor (CI-MPR) trafficking. Furthermore, GGA3 has been identified as an interacting protein of the beta-site APP-cleaving enzyme-1 (BACE1), a stress-related protease that is involved in Alzheimer's disease (AD) pathology. GGA3 has a multidomain structure consisting of an N-terminal VHS (Vps27/Hrs/Stam) domain, a GAT (GGA and TOM) domain, a largely unstructured hinge region that contains clathrin-binding motifs, and a C-terminal GAE (gamma-adaptin ear homology) domain. The GAT domain of GGAs interacts with class I GTP-bound form of Arf proteins, Rabaptin-5, ubiquitin, and/or the tumor susceptibility gene 101 product (TSG101)
KRLHTLEEVNNNVRLLNEMLAHYSKEDSSDGDKELMKELYDRCEKKRRTLFKLASETEDNDNSLGDILQA
SDDLSRVINSYKKIVEG
>gnl|CDD|260131 cd14241, PAD, Phenolic Acid Decarboxylase. This family of bacterial and fungal phenolic acid decarboxylases catalyzes the non-oxidative decarboxylation of phenolic acids to produce 4-vinyl derivates. Phenolic acid, like ferulic, p-coumaric, and caffeic acids, are important lignin-related aromatic acids and are natural constituents of plant cell walls. They act as crosslinkers between lignin polymers and hemicellulose/cellulose in plants. Their degradation is important from a biotechnological viewpoint
FVGKHFVYTYDNGWEYEIYVKNENTIDYRIHGGPVGGRWVKDQTVYIVRIREGVYKISWTEPTGTDVSLI
FNLVEKRIHGTIFFPKWVWEHPEKTVCYQNDHIDLMRAYREAGPTYPKYVVPEFATITFIEDCGGDDETV
IACA
>gnl|CDD|260109 cd14243, PT-AcyF_like, Putative ABBA-type prenyltransferases acting on cyanobactins. Members of this family are found in gene clusters responsible for the production and posttranslational modification of cyanobactins, small ribosomal cyclic peptides produced by cyanobacteria. The AcyF_like proteins are structurally similar to the ABBA-type aromatic prenyltransferases, and may be responsible for the reverse- and forward-O-prenylation of tyrosine, serine, and theronine in cyanobactins. ABBA-type aromatic prenyltransferases (PTases) are a subgroup of prenyltransferases that are characterized by an unusual type of beta/alpha fold with antiparallel beta strands. They lack the (N/D)DxxD motif which is characteristic for many other prenyltransferases
YLKEQRLQFIRTHQEAFDVEPVFPLPLFEDFVLEVEGDCTIEASCKVEGDKLIASRFLVFFKQKTWPKSL
TQALKFFDKVESRVGVQINRSLLQQFLGLHFDSSKIEVNTTGIDLRPNLADSSLKIHIRLEDEEDPEELV
RTALALDGADYSDELTQVLLKDTSLIGFDFFLDGRSEIELYAEVPGKKYFQKPEGQYLLWYIFKNFSPKV
LSPLKVSDLFGVGFSKANPNPVLYYHLKNIKDLPKYFKFNDLGDRVYSFYQHQDCITYAWVGVAEQELEK
TRLENFRLYYYKSF
>gnl|CDD|271203 cd14244, GH_101_like, Endo-a-N-acetylgalactosaminidase and related glcyosyl hydrolases. This family contains the enzymatically active domain of cell surface proteins that specifically cleave Gal-beta-1,3-GalNAc-alpha-Ser/Thr (T-antigen, galacto-N-biose), the core 1 type O-linked glycan common to mucin glycoproteins (EC:3.2.1.97). It has been classified as glycosyl hydrolase family 101 in the Cazy resource. Virulence of pathogenic organisms such as the Gram-positive Streptococcus pneumoniae and other commensal human bacteria is largely determined by their ability to degrade host glycoproteins and to metabolize the resultant carbohydrates
PPYDKDVPQKVVSRIPFNFGSQAQNPFLRTLDGVKKIYLHTDGLGQIVYLKGYQSEGHDSAHPDYGGVRN
ERAGGLEDLNTLIEEGKKYNATFGVHVNATEAYPEAPTFDEDLARDRNDGGIPSHAGWAWGDQSYLIDQR
ADLYSGGVKRRFDQLKEEGPKELDFIYVDVFTCECGWPAHRLTRELNDEGWRKAFEYLLSKEIDSTWEHW
ADDEVYGTNKGINSAPYRFMRNSQKDVWNGDPVPLFGLAPWPLLGGSDEEDFEGWAGNNDYNYFIRNFYT
HNLPTKFLQHYPIMKWED
>gnl|CDD|271204 cd14245, DMP12, Putative DNA mimic protein DMP12. The Neisseria sp. protein DMP12 has been shown to interact with the bacterial histone-like protein HU and may do so by acting as a DNA mimic. It is likely to play a regulatory role, but not via direct competition for binding of HU, which is involved in maintenance of the bacterial nucleoid structure
NLLIFCLKDNVSISEYTEMIDWAYKNIQSETVVEITENQIIEYQNRGLWRLVSEITDNWLFGPSEGDWLI
DKESILAVKEKLQNSDFSTEPLVKNIIHVLEYAIKNQKSVVFYF
>gnl|CDD|271205 cd14246, ADAM17_MPD, Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17). ADAM17 is a multi-domain protein that acts as a sheddase; is involved in the cleavage and release of the soluble ectodomain of tumor necrosis factor alpha from the cell surface and in the trans-Golgi network, as well as in the release of various other targets such as cytokines and cell adhesion molecules. This links ADAM17 to a variety of biological processes, including cellular differentiation and the progression of cancer. It was shown that the enzymatic activity of ADAM17 is regulated via a protein-disulfide isomerase (PDI). Specifically, the disulfide bridges within a CxxC motif of the membrane-proximal domain (MPD) are isomerized by PDI; the conversion triggers a conformational change between a closed and an opened form of the MPD, which may constitute a molecular switch that triggers the shedding activity of ADAM17
PFCERENLQSCACNEVENSCKRCCRDSNGTCSPYVDAGPFLYLRDGKPCTVGFCDSGKCE
>gnl|CDD|271206 cd14247, Lmo2686_like, Uncharacterized hexameric protein conserved in Bacilli. This family conserved in bacilli contains proteins that form an unusual hexameric arrangement via circular domain-swapping of a beta-hairpin-beta unit
NIAQEKEIENEDGTEGTLGVEPIIDNRPLLKGTYSLGNGTSTWKIYWYSGTYNCSFNAKINVSSKGKGKI
TSAYNPWYQFYSPLTVKKDKLSKTRKTSTASLPADAKYKLEYKVDFGSNWTVTLKASVKGKTLTTGFK
>gnl|CDD|271207 cd14248, ESP, Exocrine gland-secreting peptide 1 (ESP1) and similar pheromones. ESP1 is a peptide pheromone found in male mouse tear fluid, which is recognized by a specific G-protein-coupled receptor in the vomeronasal sensory neurons and affects female mouse sexual receptive behaviour. This small family appears restricted to rodents. ESP36 is expressed only in the female mouse extraorbital lacrimal gland. The juvenile pheromone ESP22 is secreted from the lacrimal gland and released into the tears of 2-3 week old mice; it activates the vomeronasal response pathway, and inhibits male sexual behavior. Information regarding other members of this family is not yet available
EQEVSAAHKRILCALLEMLVCGELRKLVEDVAHAGQQEFKLPIDFTGLSKCR
>gnl|CDD|271208 cd14249, ESP1_like, Exocrine gland-secreting peptide 1 (ESP1) and similar pheromones. ESP1 is a peptide pheromone found in male mouse tear fluid, which is recognized by a specific G-protein-coupled receptor in the vomeronasal sensory neurons and affects female mouse sexual receptive behaviour. This small family appears restricted to rodents; the functions of members other than mouse ESP1 have not yet been determined
EGNIQEALERTLCASGQDQTLNEDQANANQHKLNLSKILTSLSKCC
>gnl|CDD|271209 cd14250, ESP36_like, Exocrine gland-secreting peptide 36 (ESP36) and similar pheromones. ESP36 is a peptide pheromone expressed only in the female mouse extraorbital lacrimal gland. This family also includes the juvenile pheromone ESP22 which is secreted from the lacrimal gland and released into the tears of 2-3 week old mice. ESP22 activates the vomeronasal response pathway, and inhibits male sexual behavior. This small family appears restricted to rodents; the functions of other members have not yet been determined
TQKEPTISADHKTNFKIVLEEIVCQYIRNDIEDVGMIFLGSNQDNILFEGLPNEF
>gnl|CDD|271210 cd14251, PL-6, Polysaccharide Lyase Family 6. Polysaccharide Lyase Family 6 is a family of beta-helical polysaccharide lyases. Members include alginate lyase (EC 4.2.2.3) and chondroitinase B (EC 4.2.2.19). Chondroitinase B is an enzyme that only cleaves the beta-(1,4)-linkage of dermatan sulfate (DS), leading to 4,5-unsaturated dermatan sulfate disaccharides as the product. DS is a highly sulfated, unbranched polysaccharide belonging to a family of glycosaminoglycans (GAGs) composed of alternating hexosamine (gluco- or galactosamine) and uronic acid (D-glucuronic or L-iduronic acid) moieties. DS contains alternating 1,4-beta-D-galactosamine (GalNac) and 1,3-alpha-L-iduronic acid units. The related chondroitin sulfate (CS) contains alternating GalNac and 1,3-beta-D-glucuronic acid units. Alginate lyases (known as either mannuronate (EC 4.2.2.3) or guluronate lyases (EC 4.2.2.11) catalyze the degradation of alginate, a copolymer of alpha-L-guluronate and its C5 epimer beta-D-mannuronate
VSNSEELQAAIANAKPGDTIVLANGTYTDVELIFIGKGTTEAPITLKAETPGKVVITGASSLRIGGEYLV
VEGLVFKDGYTPKGAISFRANSLELANHCRLTNCVIDDFNTPDRGDGDKWVTLYGQHNRVDHNYFAGKSN
LGPTLAVRLDGNGSIANYHRIDHNYFGDRPPLGGNGGETIRIGTSGSSLSDSNTTVENNLFERCDGEVEI
ISVKSSGNTIRYNTFRESRGSLTLRHGNRNTVEGNFFIGNGKPGTGGIRIIGEGHTIYNNYFEGLTGTGF
RAALVVMNGVPNSPLNRYDQVKNALIANNTFVNCKSPIFIGGGDNERSLPPINVTFANNLIYGDTGALPI
EAPDNTDGITFKGNVVFGS
>gnl|CDD|271211 cd14252, Dockerin_like, Dockerin repeat domains and domains resembling dockerin repeats. Dockerins are modules in the cellulosome complex that often anchor catalytic subunits by binding to cohesin domains of scaffolding proteins. Three types of dockerins and their corresponding cohesin have been described in the literature. This alignment models two consecutive dockerin repeats, the functional unit
LDADFNNGISTTDLVLLQKHILNKAGLLTPYQYIAADVNNDGKINAGDLAILRRIIL
>gnl|CDD|271212 cd14253, Dockerin, Dockerin repeat domain. Dockerins are modules in the cellulosome complex that often anchor catalytic subunits by binding to cohesin domains of scaffolding proteins. Three types of dockerins and their corresponding cohesin have been described in the literature. This alignment models two consecutive dockerin repeats, the functional unit
GDVNGDGTVDITDATAVKRYVAATITPDDDSKARGDVNGDGGINAIDAMIIAKYLL
>gnl|CDD|271213 cd14254, Dockerin_II, Type II dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type II dockerins, which are responsible for mediating attachment of the cellulosome complex to the bacterial cell wall
GDVNGDGVVDIADLALVSQHFGKTSDAGYVPAADLNGDGVIDAADLALLAQNFG
>gnl|CDD|271214 cd14255, Dockerin_III, Type III dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. Two specific calcium-dependent interactions between cohesin and dockerin appear to be essential for cellulosome assembly, type I and type II. This subfamily represents the atypical type III dockerins and related domains
GDVNGDGIIDGRDATAVLTYYAKTSVGKEGGLDDLQQFAADVNGDGIIDGRDATAILTYYAKSSV
>gnl|CDD|271215 cd14256, Dockerin_I, Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex
YGDVNGDGKVNSADAALLKKYLLGKITLTEAQLKAADVNGDGKVNAIDLALLKKYLL
>gnl|CDD|271221 cd14257, CttA_X, X module of the carbohydrate-binding protein CttA and similar proteins. This model represents a putative carbohydrate-binding domain conserved in Ruminococcus, which sits N-terminal to a dockerin repeat; the protein may be a component of the Ruminococcus cellulosome system. This X module does not share similarities with other known X modules from cellulolytic bacteria and may have a structural role
TVTTKLVKSYAEIETQPGFYFSTEGGFDKAQVSNLVLHDVYIEGYVEEPGVAPVLREDENETKDITADYN
FGTATPANTYSITRTSFKYDVPVYYNGTVLKDKDGNDLTVTVYIGV
>gnl|CDD|271222 cd14259, PUFD_like, PCGF Ub-like fold discriminator and related domains. The PUFD domain binds the RAWUL (RING finger and WD40-associated ubiquitin-like) domain of the polycomb-group RING finger homologs PCGF1 and PCGF3. PUFD was characterized as a domain of the BCL6 corepressor BCOR. It does not appear to bind to PCGF2 and PCGF4. PCGF1 is a component of the Polycomb group (PcG) multi-protein BCOR complex, which is involved in repressing the transcription of BCL6 and CDKN1A. The BCL-6 corepressor (BCOR) is a transcriptional repressor required for germinal center formation and is possibly involved in apoptosis
DDFEFEFSDEPLPPLYNLRISPNDGPRNWHLLSDVLTRLKLKSRDFLLKQICLELTSIPIEDFLEQASCL
QLLCAGEKLTNNVSSSKVELVEYNDSLRSLLGIEVE
>gnl|CDD|271223 cd14260, PUFD_like_1, PCGF Ub-like fold discriminator of BCOR-like 1. The PUFD domain binds the RAWUL (RING finger and WD40-associated ubiquitin-like) domain of the polycomb-group RING finger homologs PCGF1 and PCGF3. PUFD was characterized as a domain of the BCL6 corepressor BCOR. It does not appear to bind to PCGF2 and PCGF4. PCGF1 is a component of the Polycomb group (PcG) multi-protein BCOR complex, which is involved in repressing the transcription of BCL6 and CDKN1A. The BCL-6 corepressor-like protein 1 (BCoR-L1) is largely uncharacterized; it contains ankyrin repeats
TEEDDFMFEFSDKPLLPCYNLQVSVSRGPCNWFLFSDVLKRLKLSSRIFQARFPHFEIATMPKAEFYRQV
LSSQLLTPAERPGGLDDRSPQGSSETVELVRYEPELLRLLGSAVE
>gnl|CDD|271224 cd14261, PUFD, PCGF Ub-like fold discriminator of BCOR. The PUFD domain binds the RAWUL (RING finger and WD40-associated ubiquitin-like) domain of the polycomb-group RING finger homologs PCGF1 and PCGF3. PUFD was characterized as a domain of the BCL6 corepressor BCOR. It does not appear to bind to PCGF2 and PCGF4. PCGF1 is a component of the Polycomb group (PcG) multi-protein BCOR complex, which is involved in repressing the transcription of BCL6 and CDKN1A. The BCL-6 corepressor (BCOR) is a transcriptional repressor required for germinal center formation and is possibly involved in apoptosis
DDAYSDVFEFEFSDRPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRCNFPNVEVVTIAEAEFYR
QVSLSQLFSCPKDLEAFNPDSKELLDLVEFTNELQTLLGSSLEWLHP
>gnl|CDD|271354 cd14262, VirB5_like, VirB5 protein family. This family contains VirB5 domains, including TraC, a VirB5 homolog encoded by the pKM101 plasmid, and similar proteins. VirB5 is one of 11 conserved proteins (VirB1-VirB11) in Agrobacterium tumefaciens, the causative agent of crown gall disease, that span the inner and the outer membrane, and is involved in type IV DNA secretion systems (T4SS) which mediate the translocation of virulence factors (proteins and/or DNA) from Gram-negative bacteria into eukaryotic cells. VirB5 assembles extracellular pili by interacting with several essential proteins. VirB2-VirB5 complex formation precedes incorporation into pili; it depends on the inner membrane protein VirB4 to interact directly with and stabilize VirB8 in order for VirB5 to bind to VirB8 and VirB10. Mutagenesis studies show that VirB5 proteins participate in protein-protein interactions important for pilus assembly and function
QQLAQLKQQLEQLKQQLEQAKKQYDSITGSRGLGDLLNNPNLRSLLPLDPQSIYSAAKGGGSSGSSGSLA
AIISQNEEERRLDSVGEAREAIDKRSQYAAQDKAVSLQAYEEAEQRLKQIQSLLQQINTTQDPKAIADLQ
ARIQAEQAMIQNEQTKLQMLAMLQQAEEALIAQ
>gnl|CDD|260132 cd14263, DAGK_IM_like, Integral membrane diacylglycerol kinase and similar enzymes. This mostly bacterial family of homo-trimeric integral membrane enzymes, the products of the dgkA gene, catalyzes the ATP-dependent phosphorylation of substrates such as diacylglycerol to phosphatidic acid or of undecaprenol to undecaprenyl phosphate. They are not related other cytosolic or membrane-associated kinases, including the eukaryotic diacylglycerol kinases
RKSFRYALRGLKYAFRTERNFRIHLVAALLVLILALFLGLSLVEWALLILAIGLVLVAELINTAIERLVD
LLSPEYHPLAKIAKDIAAGAVLVAALAAVVVGLLIF
>gnl|CDD|260133 cd14264, DAGK_IM, Integral membrane diacylglycerol kinase. This mostly bacterial family of homo-trimeric integral membrane enzymes, the products of the dgkA gene, catalyzes the ATP-dependent phosphorylation of diacylglycerol to phosphatidic acid. Escherichia coli DAGK participates in the membrane-derived oligosaccharide cycle (MDO cycle) by recycling lipids to restore phosphatidylglycerols that were used up in the biosynthesis of MDOs. DAGK also recycles diacylglycerols that are produced during the biosynthesis of lipopolysaccharides (LPS) back to phospholipids. DAGK is not the main source of phosphatidic acid in de-novo biosynthesis of glycerophospholipids. Escherichia coli DAGK has low activity as an undecaprenol kinase
KRLIKATGYSLQGLKAAWKNEAAFRQELLLALILIPLAFFLGVSLLERLLLIGSLLLVLIVELLNSAIEA
VVDRISLEHHELSKRAKDLGSAAVFLSLLLAALVWLAIL
>gnl|CDD|260134 cd14265, UDPK_IM_like, Integral membrane undecaprenol kinase and similar enzymes. This mostly bacterial family of homo-trimeric integral membrane enzymes, the products of the dgkA gene, catalyzes the ATP-dependent phosphorylation of undecaprenol to undecaprenyl phosphate. C55-isoprenyl (undecaprenyl) pyroposphate acts as a scaffold for the assembly of peptidoglycan components; undecaprenol kinase (UDPK) is involved in recycling undecaprenyl units for re-use in the peptidoglycan biosynthesis. UDPK does not participate in the de-novo biosynthesis of undecaprenyl phosphate. Gram-positive bacteria have a large pool of free undecaprenol, in contrast to gram-negative bacteria. UDPK may also play a role in a stress-induced pathway that affects the function of ribosomes. In Streptococcus mutans, UDPK has been shown to be required for biofilm formation, such as in the case of smooth surface dental caries. Members of the UDPK family have low activity as diacylglycerol kinases (DAGK), and many of them are annotated as DAGKs
LKSFRYAFRGIKYAFRTERNFRIHLVAAVLVIILGFFLGLSRLEWLLLLLAIGLVLAAELINTAIEALVD
LVSPEYHPLAKIAKDVAAGAVLVAAIFAVIVGLIIF
>gnl|CDD|260135 cd14266, UDPK_IM_PAP2_like, Integral membrane undecaprenol kinase domain co-occurring with type 2 phosphatidic acid phosphatase-like domains. This bacterial family of homo-trimeric integral membrane enzyme domains catalyzes the ATP-dependent phosphorylation of of undecaprenol to undecaprenyl phosphate. They sit N-terminally to phosphatase domains that are members of the type 2 phosphatidic acid phosphatase superfamily, and the function of members of this domain architecture was determined to be undecaprenyl pyrophosphate phosphatases. The bi-functional enzymes might generate undecaprenyl phosphate via two mechanisms - the phosphorylation of undecaprenol or the cleavage of the terminal phosphate group of undecaprenyl pyrophosphate
IDSFNYAIEGIIYAIKTERNMKIHFLAAILVLILSLFFDLSKVELLILFITITLVIAAELINTAIEATVD
LITDEYHPLAKIAKDVAAGAVLVAALNALIVGYLIF
>gnl|CDD|341312 cd14267, Rif1_CTD_C-II_like, Saccharomyces cerevisiae Rap1-interacting factor 1 CTD domain, metazoan Rif1 C-II domains and related domains. This model includes Saccharomyces cerevisiae Rif1_CTD (carboxy-terminal domain) and metazoan Rif1 C-II (C-terminal subdomain II). Rif1 was originally identified in S. cerevisiae where it negatively regulates telomere length homeostasis via interaction with the C-terminal domain of Rap1. A protective capping structure (telosome) comprised of Rap1, Rif1, and Rif2, inhibits telomerase, counteracts SIR-mediated transcriptional silencing, and prevents inadvertent recognition of telomeres as DNA double-strand breaks (DSBs). S. cerevisiae Rif1 has two Rap1 binding sites: the Rap1-binding module (RBM), and the CTD domain. The latter, represented here, has a lower Rap1 affinity, and provides trans binding through tetramerization. In mammals, Rif1 has been implicated in various cellular processes including pluripotency of stem cells, breast cancer development, and DSB repair pathway choice. A mutual antagonism between the nonhomologous end joining factors (53BP1-RIF1) and the homologous recombination factors (BRCA1 -CtIP) ensures correct repair pathway choice
PFWSRGLRQLVRALNIKTIGDLAQLSPEEKYNLPIKLLTFMMALRH
>gnl|CDD|270456 cd14270, UBA, UBA domain found in proteins involved in ubiquitin-mediated proteolysis. The ubiquitin-associated (UBA) domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only the bind UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains
LAQLVEMGFSREQARRALRATNGDVEAAVE
>gnl|CDD|270457 cd14271, UBA_YLR419W_like, UBA domain found in Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and similar proteins. The group includes some uncharacterized hypothetical proteins which show a high level of sequence similarity with Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W. All family members contain a ubiquitin-associated (UBA) domain, RWD domain, DEAD-box (DEXDc), helicase superfamily c-terminal domain (HELICc), Helicase associated domain (HA2), and a C-terminal oligonucleotide/oligosaccharide-binding (OB)-fold
RNMIERLTESGVSKDEALLALEECNFNEAEAAGKLTRSILP
>gnl|CDD|270458 cd14272, UBA_AMPK-RKs, UBA domain of AMPK related kinases. The AMPK-RK family comprises AMP-activated protein kinases (AMPKs), MAP/microtubule affinity-regulating kinases (MARKs), Brain-specific kinases (BRSKs), Salt inducible kinases (SIKs), maternal embryonic leucine zipper kinase (MELK), and SNF-related serine/threonine-protein kinase (SNRK). It is the only kinase family in the human genome containing an ubiquitin-associated (UBA) or UBA-like domain which is located immediately C-terminal to their N-terminal protein kinase catalytic domain. In addition, most of family members contain a C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK), but some are lack of this region. AMPK-RKs play central roles in metabolic control, energy homeostasis and stress responses in eukaryotes. They require phosphorylation by liver kinase B1 (LKB1) for full activity. Normally, AMPK-RKs appear to exist as heterotrimeric complexes consisting of a catalytic alpha-subunit and regulatory beta- and gamma-subunits. This model corresponds to the catalytic subunit. The UBA domain, previously called SNF1 homology (SNH) domain, regulates the conformation, LKB1-mediated phosphorylation and activation, and localization of the AMPK-RKs, but does not interact with ubiquitin-like molecules. In AMPKalpha subunits, the UBA-like autoinhibitory domain (AID) is responsible for AMPKalpha subunit autoinhibition. Due to the lack of UBA domain, NUAK1 kinase, also called ARK5 (AMPK-related kinase 5), and NUAK2 kinase, also called SNARK (SNF1/AMPK-related kinase), are not included in this family
DDEILQEMVELGYDREEIVESLRNNRYNDLAATYYLLL
>gnl|CDD|270459 cd14273, UBA_TAP-C_like, UBA-like domain found in the NXF family of mRNA nuclear export factors and similar proteins. This family includes nuclear RNA export factors (NXF1/NXF2), FAS-associated factors (FAF1/2), tyrosyl-DNA phosphodiesterase 2 (TDP2), OTU domain-containing proteins (OTU7A/OTU7B), NSFL1 cofactor p47, defective in cullin neddylation protein 1 (DCN1)-like protein (DCNL1/DCNL2), yeast defective in cullin neddylation protein 1 (DCN1) and similar proteins. NXF proteins can stimulate nuclear export of mRNAs and facilitate the export of unspliced viral mRNA containing the constitutive transport element. FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF2 is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. Its biological function remains unclear. TDP2 is a 5'-Tyr-DNA phosphodiesterase required for the efficient repair of topoisomerase II-induced DNA double strand breaks. OTU7A and OTU7B are zinc finger proteins that function as deubiquitinating enzymes. p47 is a major cofactor of the cytosolic AAA ATPase p97. It is required for the p97-regulated membrane reassembly of the endoplasmic reticulum (ER), the nuclear envelope and the Golgi apparatus. DCNL1 plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. The biological function of DCNL2 remains unclear. Yeast DCN1 is a scaffold-type E3 ligase for cullin neddylation. It can bind directly to cullins and the ubiquitin-like protein Nedd8-specific E2 (Ubc12), and regulate cullin neddylation and thus display ubiquitin ligase activity
FMEITGADPETARQYLESNNWDLEAAINLYF
>gnl|CDD|270460 cd14274, UBA_ACK1, UBA domain found in activated Cdc42 kinase 1 (ACK1) and similar proteins. ACK1, also called tyrosine kinase non-receptor protein 2, is an intracellular non-receptor tyrosine kinase that specifically interacts with Cdc42 and act as Cdc42 effectors. It forms a signaling complex with Cdc42, p130(Cas), and Crk, and mediates Cdc42-dependent cell migration and signaling to p130(Cas). Ack1 also stimulates prostate tumorigenesis in part by inhibiting the proapoptotic tumor suppressor WW domain containing oxidoreductase (Wwox). Moreover, ACK1 associates directly with the heavy chain of clathrin and further participates in trafficking, underlying an ability to increase receptor-mediated transferrin uptake. It may functions as a regulator of the guanine nucleotide exchange factor Dbl that can activate Rho family proteins. ACK1 consists of an N-terminal tyrosine kinase catalytic domain followed by an SH3 domain, a Cdc42/Rac interactive binding (CRIB) domain, a proline-rich region, and a C-terminal ubiquitin-association (UBA) domain. The proline-rich region of ACK1 is responsible for the binding to the adaptor proteins Nck, Grb2, sorting nexin protein 9 (SH3PX1), and Hck
ESITQVQEAVHGVTLEECQAALQNHGWNVQRAVQYLKVEQLFCLG
>gnl|CDD|270461 cd14275, UBA_EF-Ts, UBA domain found in elongation factor Ts (EF-Ts) from bacteria, chloroplasts and mitochondria of eukaryotes. EF-Ts functions as a nucleotide exchange factor in the functional cycle of EF-Tu, another translation elongation factor that facilitates the binding of aminoacylated transfer RNAs (aminoacyl-tRNA) to the ribosomal A site as a ternary complex with guanosine triphosphate during the elongation cycle of protein biosynthesis, and then catalyzes the hydrolysis of GTP and release itself in GDP-bound form. EF-Ts forms complex with EF-Tu and catalyzes the nucleotide exchange reaction promoting the formation of EF-Tu in GTP-bound form from EF-Tu in GDP-bound form. EF-Ts from Thermus thermophiles is shorter than EF-Ts from Escherichia coli, but it has higher thermostability. The mitochondrial translational EF-Ts from chloroplasts and mitochondria display high similarity to the bacterial EF-Ts. The majority of family members contain one ubiquitin-associated (UBA) domain, but some family members from plants harbor two tandem UBA domains
ELIKELREKTGAGIMDCKKALEEANGDLEKAIEWLRK
>gnl|CDD|270462 cd14276, UBA_UBP25_like, UBA domain found in ubiquitin carboxyl-terminal hydrolase UBP25, UBP28, and similar proteins. UBP25, also called deubiquitinating enzyme 25, USP on chromosome 21, ubiquitin thioesterase 25, or ubiquitin-specific-processing protease 25, belongs to the deubiquitinating enzyme (DUB) family that specifically hydrolyzes ubiquitin chains on ubiquitin-conjugated proteins. USP25 has one muscular isoform and two ubiquitous isoforms. The longer muscular isoform can bind to muscle-restricted cytoskeletal and sarcomeric proteins, such as myosin binding protein C1 (MyBPC1), actin alpha-1 (ACTA1) and filamin C (FLNC), and further prevent their degradation. USP25 harbors three potential ubiquitin-binding domains (UBDs), one ubiquitin-associated (UBA) domain and two ubiquitin-interacting motifs (UIMs) in the N-terminal region. Its C-terminal tyrosine-rich region is responsible for the binding of the second SH2 domain of SYK, a non-receptor tyrosine kinase that specifically phosphorylates USP25 and alters its cellular levels. UBP28, also called deubiquitinating enzyme 28, ubiquitin thioesterase 28, or ubiquitin-specific-processing protease 28, is also an ubiquitin-specific protease belonging to the DUB family. UBP28 can form a ternary complex with nucleoplasmic Fbw7alpha, an F-box protein that is part of an SCF-type ubiquitin ligase, and MYC, a transcription factor encoded by MYC proto-oncogene. UBP28 is required for the stability of MYC, and this stabilization is necessary for tumour-cell proliferation. Besides, UBP28 plays a critical role in the regulation of the Chk2-p53-PUMA pathway. It specifically interacts with 53BP1 and is essential to stabilize Chk2 and 53BP1 in response to DNA damage
QLINQLKEITGIQDPQILQQALEASNGDLTQAVSLLTE
>gnl|CDD|270463 cd14277, UBA_UBP2_like, UBA domain found in ubiquitin-associated protein 2 (UBAP-2) like proteins. The family contains some uncharacterized ubiquitin-associated proteins, including UBAP-2 and its homolog, UBAP2-like [UBP2L, also called protein NICE-4 (for newly identified cDNA from the epidermal differentiation complex EDC)], both of which contain an N-terminal ubiquitin-associated (UBA) domain along with a highly conserved, but function unknown domain (DUF3697)
IQEKVKQVMELTGRSEDEAVVALHDCDNDVNRAINFLL
>gnl|CDD|270464 cd14278, UBA_NAC_like, UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. The family contains nascent polypeptide-associated complex subunit alpha (NACA), putative NACA-like protein (NACP1), nascent polypeptide-associated complex subunit alpha domain-containing protein 1 (NACAD), and similar proteins found in archaea and bacteria. NACA, also called NAC-alpha or Alpha-NAC, together with BTF3, also called Beta-NAC, form the nascent polypeptide-associated complex (NAC) which is a cytosolic protein chaperone that contacts the nascent polypeptide chains as they emerge from the ribosome. Besides, NACA has a high affinity for nucleic acids and exists as part of several protein complexes playing a role in proliferation, apoptosis, or degradation. It is a cytokine-modulated specific transcript in the human TF-1 erythroleukemic cell line. It also acts as a transcriptional co-activator in osteoblasts by binding to phosphorylated c-Jun, a member of the activator-protein-1 (AP-1) family. Moreover, NACA binds to and regulates the adaptor protein Fas-associated death domain (FADD). In addition, NACA functions as a novel factor participating in the positive regulation of human erythroid-cell differentiation. The biological function of NACP1 (also called Alpha-NAC pseudogene 1 or NAC-alpha pseudogene 1) and NACAD remain unclear. The family also includes huntingtin-interacting protein K (HYPK), also called Huntingtin yeast partner K or Huntingtin yeast two-hybrid protein K. It is an intrinsically unstructured Huntingtin (HTT)-interacting protein with chaperone-like activity. It may be involved in regulating cell growth, cell cycle, unfolded protein response and cell death. All members in this family contain an ubiquitin-associated (UBA) domain
EEDIELVMSQTGVSREEAIKALRENKGDVVDAILELT
>gnl|CDD|270465 cd14279, CUE, CUE domain found in ubiquitin-binding CUE proteins. This family includes many coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domain containing proteins that are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. CUE domains form three-helix bundle structures and are distantly related to the ubiquitin-associated (UBA) domains which are widely occurring ubiquitin-binding motifs found in a broad range of cellular proteins in species ranging from yeast to human. The majority of family members contain one CUE domain, but some family members from fungi harbor two CUE domains
DEKLEQLQEMFPDLDEEVLEDVLEANNGDVEAAIDALL
>gnl|CDD|270466 cd14280, UBA1_Rad23_like, UBA1 domain of Rad23 proteins found in eukaryotes. The Rad23 family includes the yeast nucleotide excision repair (NER) proteins, Rad23p (in Saccharomyces cerevisiae) and Rhp23p (in Schizosaccharomyces pombe), their mammalian orthologs HR23A and HR23B, and putative DNA repair proteins from plants. Rad23 proteins play dual roles in DNA repair as well as in proteosomal degradation. They have affinity for both the proteasome and ubiquitinylated proteins and participate in translocating polyubiquitinated proteins to the proteasome. Rad23 proteins carry a ubiquitin-like (UBL) and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. UBL domain is responsible for the binding to proteasome. UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates which suggests Rad23 proteins might be involved in certain pathways of ubiquitin metabolism. Both UBL domain and XPC-binding domain are necessary for efficient NER function of Rad23 proteins. This model corresponds to the UBA1 domain
ELEATINNIMSMGFEREQVVRALRAAFNNPDRAVEYLLS
>gnl|CDD|270467 cd14281, UBA2_Rad23_like, UBA2 domain of Rad23 proteins found in eukaryotes. The Rad23 family includes the yeast nucleotide excision repair (NER) proteins, Rad23p (in Saccharomyces cerevisiae) and Rhp23p (in Schizosaccharomyces pombe), their mammalian orthologs HR23A and HR23B, and putative DNA repair proteins from plants. Rad23 proteins play dual roles in DNA repair as well as in proteosomal degradation. They have affinity for both the proteasome and ubiquitinylated proteins and participate in translocating polyubiquitinated proteins to the proteasome. Rad23 proteins carry a ubiquitin-like (UBL) and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. UBL domain is responsible for the binding to proteasome. UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates which suggests Rad23 proteins might be involved in certain pathways of ubiquitin metabolism. Both UBL domain and XPC-binding domain are necessary for efficient NER function of Rad23 proteins. This model corresponds to the UBA2 domain
EEREAIERLVALGFSRDQAIEAYLACDKNEELAANYLF
>gnl|CDD|270468 cd14282, UBA_TDRD3, UBA domain of Tudor domain-containing protein 3 (TDRD3) and similar proteins. TDRD3 is a modular protein containing Tudor domain, a DUF/OB-fold motif and a ubiquitin-associated (UBA) domain. It shows both nucleic acid- and methyl-binding properties and can interact with methylated RNA-binding proteins, such as fragile X mental retardation protein (FMRP) and DEAD/H box-3 (also known as DDX3X/Y, DBX/Y, HLP2 and DDX14) which is implicated in human genetic diseases. At this point, TDRD3 may play a central role in RNA processing regulatory pathways involving arginine methylation. TDRD3 localizes predominantly to the cytoplasm stress granules (SGs). The Tudor domain is essential and sufficient for its recruitment to SGs
VDEKALRHITEMGFSKEAARQALMDNNNNLEAALNFLLT
>gnl|CDD|270469 cd14283, UBA_TNR6C, UBA domain found in trinucleotide repeat-containing gene 6C protein (TNRC6C) and similar proteins. TNRC6C is one of three GW182 paralogs in mammalian genomes. It is enriched in P-bodies and important for efficient miRNA-mediated repression. TNRC6C is composed of an N-terminal glycine/tryptophan (G/W)-rich region containing an Ago hook responsible for Ago protein-binding; a ubiquitin-associated (UBA) domain and a glutamine (Q)-rich region in the middle region; a middle G/W-rich region, a RNA recognition motif (RRM), also called RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal G/W-rich region, at the C-terminus. A bipartite C-terminal region including the middle and C-terminal G/W-rich regions is referred as silencing domain that triggers silencing of bound transcripts by inhibiting protein expression and promoting mRNA decay via deadenylation. The C-terminal half containing the RRM domain functions as a key effector domain mediating protein synthesis repression by TNRC6C
SRLLKQLTDMGFKREPAEEALKSNNMNLEQAVSALLSK
>gnl|CDD|270470 cd14284, UBA_GAWKY, UBA domain found in Drosophila melanogaster protein Gawky (GW) and similar proteins. GW is the D. melanogaster GW182 homolog (dGW182) which belongs to the GW182 protein family. The GW182 proteins directly interact with Argonaute (Ago) proteins, and thus function as downstream effectors in the miRNA pathway, responsible for inhibition of translation and acceleration of mRNA decay. They are characterized by an abnormally high content of glycine/tryptophan (G/W) repeats, one or more glutamine (Q)-rich motifs, and a C-terminal RNA recognition motif (RRM), also called RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The GW182 proteins are recruited to miRNA targets through an interaction between their N-terminal domain and an Argonaute protein. Then they promote translational repression and/or degradation of miRNA targets through their C-terminal silencing domain. In addition to a G/W repeats region, a Q-rich region, and a RRM domain, GW also contains a ubiquitin-associated domain (UBA)
SKQFRILSEMGFKKEDVENALRSANMNMEEALEIL
>gnl|CDD|270471 cd14285, UBA_scEDE1_like, UBA domain found in Saccharomyces cerevisiae EH domain-containing and endocytosis protein 1 (Ede1) and similar proteins. Ede1, also bud site selection protein 15, is the mammalian protein Eps15 homolog found in yeast and functions at the internalization step of endocytosis. Both Ede1 and Eps15 are endocytic scaffold proteins that may involve in stabilization of the adaptor-cargo complex. They both contain contains three N-terminal Eps15 homology (EH) domains and C-terminal ubiquitin-binding motifs. Whereas Eps15 has two ubiquitin interacting motifs (UIM), Ede1 harbors a single ubiquitin-associated (UBA) domain. This model corresponds to Ede1 UBA domain that is responsible for the binding of monoubiquitinated proteins and negatively regulates EH domain-mediated protein-protein interactions
AIEELSGMGFTEEEARKALEKCNWDLEAATNFLLD
>gnl|CDD|270472 cd14286, UBA_UBP24, UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins. UBP24, also called deubiquitinating enzyme 24, ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24, is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal peptidase C19 domain
EEHVTTLLCMGFSDPEEIRKALRLAKNDLNEAVAILT
>gnl|CDD|270473 cd14287, UBA_At3g58460_like, UBA domain found in uncharacterized protein At3g58460 from Arabidopsis thaliana and its homologs from other plants. The uncharacterized protein At3g58460 from Arabidopsis thaliana is also known as rhomboid-like protein 15 which is encoded by RBL15 gene. Although the biological function of the family members remains unclear, they all contain an N-terminal rhomboid-like domain and a C-terminal ubiquitin-associated (UBA) domain
EALVQSLVAMGFEKHRARRALDAAGGDINTAVEILM
>gnl|CDD|270474 cd14288, UBA_HUWE1, UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins. HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein
VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP
>gnl|CDD|270475 cd14289, UBA_RHBD3, UBA domain found in vertebrate rhomboid domain-containing protein 3 (RHBD3). RHBD3 is encoded by a novel chromosome 22 CpG island-associated gene (C22orf3) that is not expressed in a significant proportion of pituitary tumors. C22orf3 is also called pituitary tumor apoptosis gene (PTAG) or RHBDD3 which is located directly upstream of EWSR1. Although its biological function remains unclear, RHBD3 contains an N-terminal rhomboid domain and a C-terminal ubiquitin-associated (UBA) domain
LRLQQLERMGFPTEKAVVALAATGRVEGAVSLLIGGQIGEETVV
>gnl|CDD|270476 cd14290, UBA_PUB_plant, UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins. This family includes some uncharacterized hypothetical proteins found in plants. Although their biological function remain unclear, all family members contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal PUB domain. UBA domain, along with UBL (ubiquitin-like) domain, has been implicated in proteasomal degradation by associating with substrates destined for degradation as well as with subunits of the proteasome, thus regulating protein turnover. PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins
EVNADLLKELEAMGFPRARAVRALHHTGNTSVEAAVNWIVEHENDPDID
>gnl|CDD|270477 cd14291, UBA1_NUB1_like, UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins. NUB1, also called negative regulator of ubiquitin-like proteins 1, renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) which may function in the regulation of cell cycle progression. NUB1 contains three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif. This model corresponds to UBA1 domain
DEDKLQQLMEMGFSEAEARLALRACNGNVERAVDYI
>gnl|CDD|270478 cd14292, UBA2_NUB1, UBA2 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins. NUB1, also called negative regulator of ubiquitin-like proteins 1, renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) which may function in the regulation of cell cycle progression. NUB1 contains three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif. This model corresponds to UBA2 domain
EDINTLKEMGYSERAAQRALHQADGNVDRAYKILL
>gnl|CDD|270479 cd14293, UBA3_NUB1, UBA3 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins. NUB1, also called negative regulator of ubiquitin-like proteins 1, renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) which may function in the regulation of cell cycle progression. NUB1 contains three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif. This model corresponds to UBA3 domain
EKLDQLVYMGFERDVAESALRLTGGDVQQATQLLLD
>gnl|CDD|270480 cd14294, UBA1_UBP5_like, UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins. UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13, is an ortholog of UBP5. It has similar domain architecture, but functions differently from USP5 in cellular deubiquitination processes. It exhibits a weak deubiquitinating activity preferring to Lys63-linked polyubiquitin in a non-activation manner. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA1 domain
EAVVSQLAEMGFPLEACRKAVYHTNNSGLEAAMNWIMEHMDDPD
>gnl|CDD|270481 cd14295, UBA1_atUBP14, UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins. atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain
DQELVAQLMEMGFPKVRAEKALFFTQNKGLEEAMEWLEEHSEDAD
>gnl|CDD|270482 cd14296, UBA1_scUBP14_like, UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins. scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain
EEAVSQLMSMGFSENAAKRALYYTGNSSVEAAMNWLFEH
>gnl|CDD|270483 cd14297, UBA2_spUBP14_like, UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins. spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain
EDLVKQLVDMGFTEAQARKALRKTNNNVERAVDWLFEGP
>gnl|CDD|270484 cd14298, UBA2_scUBP14_like, UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins. scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain
DEALAQLVSMGFDPEVARKALILTNGNVERAIEWLFSN
>gnl|CDD|270485 cd14300, UBA_UBS3A_like, UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and similar proteins. UBS3A, also called Cbl-interacting protein 4 (CLIP4), suppressor of T-cell receptor signaling 2 (Sts-2), or T-cell ubiquitin ligand 1 (TULA-1), is a lymphoid protein only detected in thymus, spleen, and bone marrow. UBS3A exhibits extremely low phosphatase activity, but is capable of promoting T-cell apoptosis independent of either T cell receptor (TCR)/CD3-mediated signaling or caspase activity. It functions as a negative regulator of TCR signaling. UBS3A can also inhibit HIV-1 biogenesis through the binding of ATP-binding cassette protein family E member 1 (ABCE-1), a host factor of HIV-1 assembly. Moreover, UBS3A acts as the Cbl- and ubiquitin-interacting protein that can inhibit endocytosis and downregulation of ligand-activated epidermal growth factor receptor (EGFR) by impairing Cbl-induced ubiquitination, as well as inhibit clathrin-dependent endocytosis in general. This family also includes Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and some uncharacterized AAA-type ATPase-like proteins found in plants
LETLLAMGFPEDVARKALKATGGKSIEKATDWLLSHC
>gnl|CDD|270486 cd14301, UBA_UBS3B, UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and similar proteins. UBS3B, or Cbl-interacting protein p70, suppressor of T-cell receptor signaling 1 (Sts-1), T-cell ubiquitin ligand 2 (TULA-2), or tyrosine-protein phosphatase STS1/TULA2, is ubiquitously expressed in mammalian tissues in a variety of cell types. It exhibits high phosphatase activity, but demonstrates no proapoptotic activity. It negatively regulates the tyrosine kinase Zap-70 activation and T cell receptor (TCR) signaling pathways that modulate T cell activation. Moreover, UBS3B acts as a Cbl- and ubiquitin-interacting protein that inhibits endocytosis of epidermal growth factor receptor (EGFR) and platelet-derived growth factor receptor
SALEVLLSMGFPKHRAEKALAATGGRSVQLASDWLLSH
>gnl|CDD|270487 cd14302, UBA_UBXN1, UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins. UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain
SELQTLIEMGFSRNRAEKALAKTGNQGVEAAMEWLLAHEDD
>gnl|CDD|270488 cd14303, UBA1_KPC2, UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins. KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA1 domain
VDPEALKQLTEMGFPEARATKALLLNRMSPTQAMEWLLEHE
>gnl|CDD|270489 cd14304, UBA2_KPC2, UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins. KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA2 domain
PNPRAVQSLMEMGFEEEDVLEALRVTRNNQNAACEWLLG
>gnl|CDD|270490 cd14305, UBA_UBAC2, UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar proteins. UBAC2, also called phosphoglycerate dehydrogenase-like protein 1, is a ubiquitin-associated domain (UBA)-domain containing protein encoded by gene UBAC2 (or PHGDHL1), a risk gene for Behcet's disease (BD). It may play an important role in the development of BD through its transcriptional modulation. Members in this family contain an N-terminal rhomboid-like domain and a C-terminal UBA domain
PSEEQVQQLVDMGFSREDVLEALRQSNNDVNAATNLLL
>gnl|CDD|270491 cd14306, UBA_VP13D, UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins. VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required
VAKLMELGFPEEDCIRALRACGGNVEEAANWLLENA
>gnl|CDD|270492 cd14307, UBA_RUP1p, UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins. RUP1p is a ubiquitin-associated (UBA) domain-containing protein encoded by a nonessential yeast gene RUP1. It can mediate the association of Rsp5 and Ubp2. The N-terminal UBA domain is responsible for antagonizing Rsp5 function, as well as bridging the Rsp5-Ubp2 interaction. No other characterized functional domains or motifs are found in RUP1p
EEAVASLLEMGIPREVAIEALRETNGDVEAAANYIFSN
>gnl|CDD|270493 cd14308, UBA_Mud1_like, UBA domain found in Schizosaccharomyces pombe UBA domain-containing protein mud1 and similar proteins. Schizosaccharomyces pombe mud1 is an ortholog of the Saccharomyces cerevisiae DNA-damage response protein Ddi1. S. cerevisiae Ddi1, also called v-SNARE-master 1 (Vsm1), belongs to a family of proteins known as the ubiquitin receptors which can bind ubiquitinated substrates and the proteasome. It is involved in the degradation of the F-box protein Ufo1, involved in the G1/S transition. It also participates in Mec1-mediated degradation of Ho endonuclease. Both S. pombe mud1 and S. cerevisiae Ddi1 contain an N-terminal ubiquitin-like (UBL) domain, an aspartyl protease-like domain, and a C-terminal ubiquitin-associated (UBA) domain. S. pombe mud1 binds to K48-linked polyubiquitin (polyUb) through UBA domain
PEKVRQLVDMGFTPTDAGRALKAANGDVTVAAEWLL
>gnl|CDD|270494 cd14309, UBA_scDdi1_like, UBA domain found in Saccharomyces cerevisiae DNA-damage response protein Ddi1 and similar proteins. Ddi1, also called v-SNARE-master 1 (Vsm1), is a ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as a ubiquitin association domain (UBA)- ubiquitin-like-domain (UBL) shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. Ddi1 contains an N-terminal UBL domain and a C-terminal UBA domain. It also harbors a central retroviral aspartyl-protease-like domain (RVP) which may be important in cell-cycle control. At this point, Ddi1 may function proteolytically during regulated protein turnover in the cell. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also called transporter regulator RS1 (RS1) which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1
EEKIAQLMDLGFSREEAIQALEATNGNVELAASLLF
>gnl|CDD|270495 cd14310, UBA_cnDdi1_like, UBA domain found in Cryptococcus neoformans DNA-damage response protein Ddi1 and similar proteins. The family includes some uncharacterized Ddi and similar proteins which show a high level of sequence similarity with yeast Ddi1. Ddi1, also called v-SNARE-master 1 (Vsm1), is a ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in yeast. It functions as a ubiquitin association domain (UBA)- ubiquitin-like-domain (UBL) shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. Ddi1 contains an N-terminal UBL domain and a C-terminal UBA domain. It also harbors a central retroviral aspartyl-protease-like domain (RVP) which may be important in cell-cycle control. At this point, Ddi1 may function proteolytically during regulated protein turnover in the cell
IQTLVNLGATREQAINLLNAAGGNVDLAAS
>gnl|CDD|270496 cd14311, UBA_II_E2_UBC1, UBA domain of yeast ubiquitin-conjugating enzyme E2 1 (UBC1) and similar proteins. UBC1, also called ubiquitin-conjugating enzyme E2-24 kDa, or ubiquitin-protein ligase, is the yeast homolog of mammalian ubiquitin-conjugating enzyme E2 K (UBE2K or E2-25K). UBC1 and UBE2K are unique class II E2 conjugating enzymes, both of which contain a C-terminal ubiquitin-associated (UBA) domain in addition to an N-terminal catalytic ubiquitin-conjugating enzyme E2 (UBCc) domain. The yeast UBC1 plays an important role in the degradation of short-lived proteins especially during the G0-G1 transition accompanying spore germination
GLEHEHVQQFVDMGFPRDKVIEVLKRLNYRGNNVDKITDDVVLEELLR
>gnl|CDD|270497 cd14312, UBA_II_E2_UBC27_like, UBA domain found in plant ubiquitin-conjugating enzyme E2 27 and similar proteins. UBC27, also called ubiquitin carrier protein 27, functions as a class II ubiquitin-conjugating (UBC) enzyme (E2). E2, together with E1 (ubiquitin-activating enzyme UBA) and E3 (ubiquitin ligase), is required in the multi-step reaction of ubiquitin conjugation. Unlike other Arabidopsis UBCs, in addition to an N-terminal ubiquitin-conjugating enzyme E2 catalytic domain (UBCc), UBC27 has an additional C-terminal ubiquitin-associated domain (UBA)
EEKVQRLVEMGFPRDQAVVALESAGGDENAALEKLL
>gnl|CDD|270498 cd14313, UBA_II_E2_UBE2K_like, UBA domain found in vertebrate ubiquitin-conjugating enzyme E2 K (UBE2K), Drosophila melanogaster ubiquitin-conjugating enzyme E2-22 kDa (UbcD4) and similar proteins. UBE2K, also called Huntingtin-interacting protein 2 (HIP-2), ubiquitin carrier protein, ubiquitin-conjugating enzyme E2-25 kDa (E2-25K), or ubiquitin-protein ligase, is a multi-ubiquitinating enzyme with the ability to synthesize Lys48-linked polyubiquitin chains which is involved in the ubiquitin (Ub)-dependent proteolytic pathway. It interacts with the frameshift mutant of ubiquitin B and functions as a crucial factor regulating amyloid-beta neurotoxicity. It has also been characterized as Huntingtin-interacting protein that modulates the neurotoxicity of Amyloid-beta (Abeta), the principal protein involved in Alzheimer's disease pathogenesis. Moreover, E2-25K increases aggregate the formation of expanded polyglutamine proteins and polyglutamine-induced cell death in the pathology of polyglutamine diseases. UbcD4, also called ubiquitin carrier protein, or ubiquitin-protein ligase, is encoded by Drosophila E2 gene which is only expressed in pole cells in embryos. It is a putative E2 enzyme homologous to the Huntingtin interacting protein-2 (HIP2) of human. UbcD4 specifically interacts with the polyubiquitin-binding subunit of the proteasome. This family also includes a putative ubiquitin conjugating enzyme from plasmodium Yoelii (pyUCE). It shows a high level of sequence similarity with UBE2K and may also plays a role in the ubiquitin-mediated protein degradation pathway. All family members are class II E2 conjugating enzymes which contain a C-terminal ubiquitin-associated (UBA) domain in addition to an N-terminal catalytic ubiquitin-conjugating enzyme E2 (UBCc) domain
KKKVDKLVDMGFDRDEAIVALSSNNWNLERATEYLF
>gnl|CDD|270499 cd14314, UBA_II_E2_pyUCE_like, UBA domain found in a putative ubiquitin conjugating enzyme from plasmodium Yoelii (pyUCE) and similar proteins. P. Yoelii ubiquitin-conjugating enzyme and other uncharacterized family members show high sequence similarity to the human Huntingtin interacting protein-2 (HIP2) which belongs to a class II E2 ubiquitin-conjugating enzyme family. These proteins may play roles in the ubiquitin-mediated protein degradation pathway. They all contain a C-terminal ubiquitin-associated (UBA) domain in addition to an N-terminal catalytic ubiquitin-conjugating enzyme E2 (UBCc) domain
KEEKIKKLLEMGFPRDQARKALEKNGWDETLALNTLL
>gnl|CDD|270500 cd14315, UBA1_UBAP1, UBA1 domain found in vertebrate ubiquitin-associated protein 1 (UBAP-1). UBAP-1, also called nasopharyngeal carcinoma-associated gene 20 protein, is a ubiquitously expressed protein that may play an important role in the ubiquitin pathway and cell progression. It co-localizes with TDP-43 proteins in neuronal cytoplasmic inclusions and acts as a genetic risk factor for frontotemporal lobar degeneration (FTLD). Moreover, UBAP-1, together with VPS37A, forms an endosome-specific endosomal sorting complexes I required for transport (ESCRT-I) complex that displays a restricted cellular function, ubiquitin-dependent endosomal sorting and multivesicular body (MVB) biogenesis. UBAP-1 contains an N-terminal UBAP-1-MVB12-associated (UMA) domain, and two tandem ubiquitin-associated (UBA) domains that may be responsible for the binding of ubiquitin-conjugating enzymes. This model corresponds to UBA1 domain
LSPSERQCVETVVGMGYSYECVLKAMKKKGQNIEQILEYLFAH
>gnl|CDD|270501 cd14316, UBA2_UBAP1_like, UBA2 domain found in ubiquitin-associated protein 1 (UBAP-1) and similar proteins. UBAP-1, also called nasopharyngeal carcinoma-associated gene 20 protein, is a ubiquitously expressed protein that may play an important role in the ubiquitin pathway and cell progression. It co-localizes with TDP-43 proteins in neuronal cytoplasmic inclusions and acts as a genetic risk factor for frontotemporal lobar degeneration (FTLD). Moreover, UBAP-1, together with VPS37A, forms an endosome-specific endosomal sorting complexes I required for transport (ESCRT-I) complex that displays a restricted cellular function, ubiquitin-dependent endosomal sorting and multivesicular body (MVB) biogenesis. UBAP-1 contains an N-terminal UBAP-1-MVB12-associated (UMA) domain, and two tandem ubiquitin-associated (UBA) domains that may be responsible for the binding of ubiquitin-conjugating enzymes. This model corresponds to UBA2 domain
FLKLLNQLHELGFPEDKIKEALLKHNNDRDKALDELV
>gnl|CDD|270502 cd14317, UBA_DHX57, UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins. DHX57, also called DEAH box protein 57, is a multi-domain protein with an N-terminal ubiquitin-association (UBA) domain, a Zinc finger domain, a RWD domain, a DEAD-like helicase domain and two C-terminal helicase associated domains. Although the precise biological function of DHX57 remains unclear, it may function as a putative ATP-dependent RNA helicase
VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL
>gnl|CDD|270503 cd14318, UBA_Cbl_like, UBA domain found in casitas B-lineage lymphoma (Cbl) proteins. The Cbl adaptor proteins family contains a small class of RING-type E3 ubiquitin ligases with oncogenic activity which is represented by three mammalian members, c-Cbl, Cbl-b and Cbl-3. Cbl proteins function as potent negative regulators of various signaling cascades in a wide range of cell types. They play roles in ubiquitinating the activated tyrosine kinases and targeting them for degradation. Cbl proteins in this family consists of a highly conserved N-terminal half that includes a tyrosine-kinase-binding (TKB) domain and a RING finger domain, both of which are required for Cbl-mediated downregulation of RTKs, and a C-terminal half that includes a ubiquitin-associated (UBA) domain and other protein interaction motifs. The UBA domain contains leucine/isoleucine repeats and may play a role in dimerization of Cbl proteins. In addition, although both c-Cbl and Cbl-b have the C-terminal UBA domain, only the UBA domain from Cbl-b can bind ubiquitin
LLSYIAKLVGEGYSKEDVIRALGIARNNVEMARDILREFA
>gnl|CDD|270504 cd14319, UBA_NBR1, UBA domain of next to BRCA1 gene 1 protein (NBR1) and similar proteins. NBR1, also called cell migration-inducing gene 19 protein, membrane component chromosome 17 surface marker 2, neighbor of BRCA1 gene 1 protein, or protein 1A1-3B, is a scaffold protein that may be involved in signal transmission downstream of the serine/protein kinase from the giant muscle protein titin. Moreover, NBR1 functions as an autophagic receptor for ubiquitinated cargo. It interacts with ATG8-family proteins for its degradation by autophagy. NBR1 contains an N-terminal Phox and Bem1p (PB1) domain that plays a critical role in mediating protein-protein interactions with both titin kinase and with another scaffold protein, p62. NBR1 also has a LC3-interaction region (LIR) and a ubiquitin-associated (UBA) domain. The LIR is required for the autophagic clearance of NBR1. UBA domain is responsible for the ubiquitin binding which is necessary for the puromycin-induced formation of ubiquitinated protein aggregates
EWDSELEQLFEMGFTDRDLNQELLKKHNGDLDRVVDELL
>gnl|CDD|270505 cd14320, UBA_SQSTM, UBA domain of sequestosome-1 (SQSTM) and similar proteins. SQSTM, also called EBI3-associated protein of 60 kDa (EBIAP /p60), phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa, or ubiquitin-binding protein p62, is a widely expressed multifunctional cytoplasmic protein that is able to noncovalently bind ubiquitin and several signaling proteins, suggesting a regulatory role connected to the ubiquitin-proteasome pathway. It functions as a scaffolding protein that regulates a diverse range of signaling pathways leading to activation of the nuclear factor kappa B (NF-kappaB) family of transcription factors. It also plays a novel role in connecting receptor signals with the endosomal signaling network required for mediating TrkA-induced differentiation. SQSTM contains a PB1 dimerization domain, a tumor necrosis factor receptor-associated factor 6 (TRAF6) binding site, and a C-terminal ubiquitin-associated (UBA) domain that mediates the recognition of polyubiquitin chains and ubiquitylated substrates
KIEEALSQMLAMGFSNEGGWLTRLLEAKNGDIGKVLDVIQ
>gnl|CDD|270506 cd14321, UBA_IAPs, UBA domain found in inhibitor of apoptosis proteins (IAPs). IAPs are frequently overexpressed in cancer and associated with tumor cell survival, chemoresistance, disease progression and poor prognosis. They function primarily as negative regulators of cell death. They regulate caspases and apoptosis through the inhibition of specific members of the caspase family of cysteine proteases. In addition, IAPs has been implicated in a multitude of other cellular processes, including inflammatory signalling and immunity, mitogenic kinase signalling, proliferation and mitosis, as well as cell invasion and metastasis. IAPs in this family includes cellular inhibitor of apoptosis protein c-IAP1 and c-IAP2, XIAP, and BIRC8, all of which contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of binds polyubiquitin (polyUb), and a RING domain at the carboxyl terminus that is required for ubiquitin ligase activity. c-IAPs contains an additional caspase activation and recruitment domain (CARD) between UBA and RING domains. CARD domain may serve as a protein interaction surface
PVVQSALEMGFDRDRVRRAIERRLEETGRPFSTAEELVEAVLNA
>gnl|CDD|270507 cd14322, UBA_LATS, UBA domain found in serine/threonine-protein kinase LATS and similar proteins. The LATS proteins family consists of two isoforms, LATS1 and LATS2, both of which are mammalian homologs of the Drosophila tumor suppressor gene lats/warts. LATS1, also called large tumor suppressor homolog 1, or WARTS protein kinase (warts), is a serine/threonine-protein kinase that highly conserved from fly to human. LATS2, also called kinase phosphorylated during mitosis protein, or large tumor suppressor homolog 2, or serine/threonine-protein kinase KPM, or Warts-like kinase, inhibits the G1/S transition and is essential for embryonic development, proliferation control and genomic integrity. LATS proteins contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal protein kinase domain
NQMLQQLVAAGYSEEISMRALKKSGARTIEAAIEFIELM
>gnl|CDD|270508 cd14323, UBA_PLCs_like, UBA domain of eukaryotic protein linking integrin-associated protein with cytoskeleton (PLIC) proteins, Saccharomyces cerevisiae proteins Dsk2p and Gts1p, and similar proteins. The PLIC proteins (or ubiquilins) family contains human homologs of the yeast ubiquitin-like Dsk2 protein, PLIC-1 (also called ubiquilin-1), PLIC-2 (also called ubiquilin-2 or Chap1), PLIC-3 (also called ubiquilin-3) and PLIC-4 (also called ubiquilin-4, Ataxin-1 interacting ubiquitin-like protein, A1Up, Connexin43-interacting protein of 75 kDa, or CIP75), and mouse PLIC proteins. They are ubiquitin-binding adaptor proteins involved in all protein degradation pathways through delivering ubiquitinated substrates to proteasomes. They also promote autophagy-dependent cell survival during nutrient starvation. Saccharomyces cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Gts1p, also called protein LSR1, is encoded by a pleiotropic gene GTS1 in budding yeast. The formation of Gts1p-mediated protein aggregates may induce reactive oxygen species (ROS) production and apoptosis. Gts1p also plays an important role in the regulation of heat and other stress responses under glucose-limited or -depleted conditions in either batch or continuous culture
RYQQQLATLKEMGFNDTEKNLQALSATGGNINLAIERLF
>gnl|CDD|270509 cd14324, UBA_Dsk2p_like, UBA domain of Saccharomyces cerevisiae proteasome interacting protein Dsk2p and its homologs found in fungi. The family contains several fungal multi-ubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (UBL) and with ubiquitin (Ub) through their C-terminal ubiquitin-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is a ubiquitin receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect ubiquitin chains against disassembly by deubiquitinating enzymes
PEERYEEQLRQLNEMGFFDFDRNVRALRRSGGSVQGAVESLL
>gnl|CDD|270510 cd14325, UBA_RNF31, UBA domain found in E3 ubiquitin-protein ligase RING finger protein 31 and similar proteins. RNF31, also called HOIL-1-interacting protein (HOIP), or zinc in-between-RING-finger ubiquitin-associated domain protein, together with HOIL-1 and SHARPIN, forms the E3-ligase complex (also known as linear-ubiquitin-chain assembly complex LUBAC) that regulates NF-kappaB activity and apoptosis. RNF31 contains a central ubiquitin-associated (UBA) domain that is responsible for the interaction with the N-terminal ubiquitin-like domain (UBL) of HOIL-1L. In addition, RNF31 can interact with the atypical mammalian orphan receptor DAX-1, trigger DAX-1 ubiquitination and stabilization, and participate in repressing steroidogenic gene expression
QCLRDRRVKVKELGSLGFGDATRCLQALRQSGGDVRGALVLLQRQLLEPFHQRLW
>gnl|CDD|270511 cd14326, UBA_UBL7, UBA domain found in ubiquitin-like protein 7 (UBL7) and similar proteins. UBL7, also called bone marrow stromal cell ubiquitin-like protein (BMSC-UbP), or ubiquitin-like protein SB132, is a novel ubiquitin-like protein that may play roles in regulation of bone marrow stromal cell (BMSC) function or cell differentiation via an evocator-associated and cell-specific pattern. UBL7 contains an N-terminal ubiquitin domain (UBQ) and a C-terminal ubiquitin-associated (UBA) domain. UBQ domain interacts with 26S proteasome-dependent degradation, and UBA domain links cellular processes and the ubiquitin system
LQSQLQQLREMGITDDSLSLRALQATGGDVQAALNLLF
>gnl|CDD|270512 cd14327, UBA_atUPL1_2_like, UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins. The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins
EAVAQLVEMGFSRERAEEALRAVGTNSVELAMEWLFTN
>gnl|CDD|270513 cd14328, UBA_TNK1, UBA domain found in non-receptor tyrosine-protein kinase TNK1 and similar proteins. TNK1, also called CD38 negative kinase 1, is a non-receptor protein tyrosine kinase (NRPTK) that has been implicated in the regulation of apoptosis, cell growth, nuclear factor-kappaB, and Ras. It associates with phospholipase C (PLC)-gamma1 and may play a role in phospholipid signal transduction. TNK1 contains an NH2-terminal kinase, a Src Homology 3 (SH3) domain, a proline-rich (PR) region, and a C-terminal ubiquitin-association (UBA) domain
AVRYLKVEQLFRLGLASREECEKALERTNWNLELASSLLL
>gnl|CDD|270514 cd14329, UBA_SWA2p_like, UBA domain found in yeast auxilin-like clathrin uncoating factor SWA2 (Swa2p) and similar proteins. The lineage specific group includes Swa2p and other uncharacterized hypothetical proteins from Saccharomyces. Swa2p, also called bud site selection protein 24, DnaJ-related protein SWA2, or synthetic lethal with ARF1 protein 2, is the yeast auxilin ortholog that is a multifunctional protein with three N-terminal clathrin-binding (CB) motifs, a ubiquitin-association (UBA) domain, a tetratricopeptide repeat (TPR) domain, and a C-terminal J-domain. It is required for disassembly of clathrin-coated vesicles (CCVs) in an ATP-dependent manner, as well as for cortical endoplasmic reticulum (ER) inheritance
DMEIAKLMSLGLSIDKANEYYERGILYEDLLEKRKE
>gnl|CDD|270515 cd14330, UBA_atDRM2_like, UBA domain found in Arabidopsis thaliana DNA (cytosine-5)-methyltransferase DRM2 (atDRM2) and similar proteins. atDRM2, also called protein domains rearranged methylase 2, is a homolog of the mammalian de novo methyltransferase DNMT3. It is the major de novo methyltransferase targeted to DNA by small interfering RNAs (siRNAs) in the RNA-directed DNA methylation (RdDM) pathway in Arabidopsis thaliana. atDRM2 is a part of the RdDM effector complex and plays a catalytic role in RdDM. It contains an N-terminal UBA domains and a C-terminal methyltransferase domain, both of which are required for normal RdDM
EEKIKTLVSMGFSESDARRALERCGYDVAAAADFLFS
>gnl|CDD|270516 cd14331, UBA_HERC1_2, UBA domain found in probable E3 ubiquitin-protein ligase HERC1, HERC2 and similar proteins. HERC1, also called HECT domain and RCC1-like domain-containing protein 1, p532, or p619, is an ubiquitously expressed giant protein involved in ubiquitin-dependent intracellular membrane trafficking through its interaction with vesicle coat proteins such as clathrin and ARF. Moreover, it has been identified as a tuberous sclerosis complex TSC2-interacting protein that may play a role in TSC-mTOR (mammalian target of rapamycin) pathway. HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. HERC1 and HERC2 are multi-domain proteins with different domain organizations. Both of them contain a ubiquitin-association (UBA) domain, more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain
IVQLMEMGFSRRQIEMAMQALGSESDAPNIENLVNWLLEH
>gnl|CDD|270517 cd14332, UBA_RuvA_C, C-terminal UBA-like domain of holliday junction ATP-dependent DNA helicase RuvA. RuvA, along with RuvB and RuvC proteins, is involved in branch migration of heteroduplex DNA in homologous recombination that is a crucial process for maintaining genomic integrity and generating biological diversity in all living organisms. RuvA has a tetrameric architecture in which each subunit comprised of three distinct domains. This model corresponds to the C-terminal domain of RuvA which is distantly related to the ubiquitin-associated (UBA) domain. It plays a significant role in the ATP-dependent branch migration of the hetero-duplex through direct contact with RuvB. Within the Holliday junction, the C-terminal domain makes no interaction with DNA
PVLEDAVSALVALGYSRKEAEKAVKKVLAEAPGLSVEELIREALK
>gnl|CDD|270518 cd14333, UBA_unchar_Eumetazoa, UBA domain found in some hypothetical proteins from Eumetazoa. The family includes some uncharacterized Eumetazoan proteins. Although their biological function remain unclear, they all contain a very conserved ubiquitin-associated (UBA) domain which is a commonly occurring sequence motif found in proteins involved in ubiquitin-mediated proteolysis
TVDSLLACLASMGFDLDDCQEAIQAGKLTVESAIEWLL
>gnl|CDD|270519 cd14334, UBA_SNF1_fungi, UBA domain of yeast carbon catabolite-derepressing protein kinases (Snf1) and similar proteins found in fungi. Snf1, also called yeast adenosine monophosphate (AMP)-activated protein kinase (AMPK), is a global regulator of carbon metabolism in the yeast Saccharomyces cerevisiae. Its phosphorylation is essential for the regulation by carbon catabolite repression in eukaryotic cells. Snf1 is involved in the cellular responses to nutrient stress, as well as other environmental stresses, including sodium ion stress, heat shock, alkaline pH, oxidative stress, and genotoxic stress. It plays roles in various nutrient-responsive, cellular developmental processes, including meiosis and sporulation, aging, haploid invasive growth, and diploid pseudohyphal growth. It is required for transcription of glucose-repressed genes, glycogen storage, thermotolerance, and peroxisome biogenesis. The catalytic activity of Snf1 can be regulated by upstream kinases, Sak1, Elm1, and Tos3, by the Reg1-Glc7 protein phosphatase 1, and by autoinhibition. In addition to an N-terminal protein kinase domain and a C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK), Snf1 contains an ubiquitin-associated (UBA) domain, previously called SNF1 homology (SNH) domain, in the middle region
IDDDVVSKLSETMGYSKEEILEALRRPEDNEIKDAYMLVKENRRLLKD
>gnl|CDD|270520 cd14335, UBA_SnRK1_plant, UBA domain found in the plant sucrose nonfermenting-1-related kinase (SnRK1) proteins. The plant SnRK1 proteins (also known as AKIN10/11) family contains plant orthologs of the yeast sucrose non-fermenting (Snf1) kinase and mammalian AMP-activated protein kinase (AMPK), including two catalytic alpha-subunits of plant Snf1-related kinases (SnRKs): SNF1-related protein kinase catalytic subunit alpha KIN10 (also called AKIN10 or AKIN alpha2) and SNF1-related protein kinase catalytic subunit alpha KIN11 (also called AKIN11 or AKIN alpha1). AKIN10 and AKIN11 function as central integrators of sugar, metabolic, stress, and developmental signals in plants. They form different complexes with the regulatory AKINbeta2, a plant ortholog of conserved Snf1/AMPK beta-subunits. In addition to an N-terminal protein kinase domain and a C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK), Snf1 contains an ubiquitin-associated (UBA) domain, previously called SNF1 homology (SNH) domain, in the middle region
IDEEIVQEVVQLGFDREYLVESLRNRKQNHATVTYYLLLDK
>gnl|CDD|270521 cd14336, UBA_AID_AMPKalpha, UBA-like autoinhibitory domain (AID) found in vertebrate 5'-AMP-activated protein kinase catalytic alpha (AMPKalpha) subunits. The family corresponds to the catalytic subunits of adenosine monophosphate (AMP)-activated protein kinase (AMPK) which includes two isoforms encoded by two distinct genes, AMPKalpha-1 (PRKAA1) and AMPKalpha-2 (PRKAA2). Skeletal muscle predominantly expresses the AMPKalpha-2, whereas the liver expresses approximately equal amounts of both AMPKalpha subunits. One AMPKalpha subunit and two regulatory subunits, beta (beta1, beta2, beta3) and gamma (gamma1, gamma2, gamma3) form a heterotrimeric AMPK complex that plays a central role in the regulation of cellular energy metabolism, activates energy-producing pathways and inhibits energy-consuming processes through responding to a fall in intracellular ATP levels. It is activated in beta-cells at low glucose concentrations, but inhibited as glucose levels increase. AMPKalpha subunits show significant similarity in the catalytic core region, but have divergent COOH-terminal tails, suggesting they may interact with different proteins within this region. Both of AMPKalpha subunits have an N-terminal Ser/Thr kinase domain followed by an ubiquitin-associated (UBA)-like AID, and a C-terminal AMPK regulatory domain. The Ser/Thr kinase domain contains a conserved Thr residue that must be phosphorylated for activity in the activation loop. The AID is responsible for AMPKalpha subunits autoinhibition. The C-terminal regulatory domain of the alpha-subunit is essential for binding the beta- and gamma-subunits
ASIVDDEAVKEVCEKFGVTEEEVLSALLSGDPHDQLVIAYHLIVDNKRIADEAAKFSLEDFYPAS
>gnl|CDD|270522 cd14337, UBA_MARK_Par1, UBA domain found in microtubule-associated protein (MAP)/microtubule affinity-regulating kinase (MARK)/ partitioning-defective 1 (Par-1) and similar proteins. The MARK/Par-1 subfamily contains serine/threonine-protein kinases including mammal MARKs, and polarity kinases Par-1 found in Caenorhabditis elegans and Drosophila melanogaster. Those proteins are frequently found associated with membrane structures and participate in diverse processes from control of the cell cycle and polarity to intracellular signaling and microtubule stability. They are involved in nematode embryogenesis, cell cycle control, epithelial cell polarization, cell signaling, and neuronal migration and differentiation. The mammals MARKs have been implicated in carcinomas, Alzheimer's disease (through tau hyperphosphorylation), and autism. Four MARK isoforms exist in humans. Members in this subfamily contain an N-terminal protein kinase catalytic domain, followed by an ubiquitin-associated (UBA) domain and a C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK)
PDPKRIEIMVSMGFNREEIEESLKNRKFDEVMATYLLLGR
>gnl|CDD|270523 cd14338, UBA_SIK, UBA domain found in salt-inducible kinase SIK1, SIK2, SIK3 and similar proteins. Salt-inducible kinase SIK1, SIK2, SIK3 are serine/threonine kinases that belong to the AMP-activated protein kinases (AMPK) family involved in the regulation of metabolism during energy stress. SIK1, also called serine/threonine-protein kinase SNF1-like kinase 1 (SNF1LK), is required for myogenic differentiation. It is degraded by the proteasome in myoblasts which is regulated by cAMP signaling. Moreover, SIK1 acts as a class II histone deacetylase (HDAC) kinase, triggering the cytoplasmic export of the HDACs and activation of myocyte enhancer factor 2 (MEF2)-dependent transcription. It also regulates transcription through inhibitory phosphorylation of a family of cAMP responsive element binding protein (CREB) coactivators, called TORCs/CRTCs. In addition, SIK1 links LKB1 to p53-dependent anoikis and suppresses metastasis. It is also involved in a cell sodium-sensing network that regulates active sodium transport through a calcium-dependent process. SIK2, also called Qin-induced kinase or serine/threonine-protein kinase SNF1-like kinase 2 (SNF1LK2), plays an important role in the insulin-signaling pathway during adipocyte differentiation, as well as in autophagy progression. Moreover, SIK2 plays a critical role in neuronal survival and modulates cAMP responsive element binding protein (CREB)-mediated gene expression in response to hormones and nutrients. SIK2 acts as a critical determinant in autophagy progression. In addition, SIK2 localizes at the centrosome and functions as a centrosome kinase required for bipolar mitotic spindle formation. It is involved in the initiation of mitosis, and regulates the localization of the centrosome linker protein, C-Nap1, through S2392 phosphorylation. SIK3, also called salt-inducible kinase 3 or serine/threonine-protein kinase QSK, acts as a novel energy regulator that modulates cholesterol and bile acid metabolism by coupling with retinoid metabolism. It also play an essential role in facilitating chondrocyte hypertrophy during skeletogenesis and growth plate maintenance. Members in this family contain an N-terminal protein kinase catalytic domain followed by an ubiquitin-associated (UBA) domain
NEQVLRHMASLGIDRDRTLESVKNDSYDHVSAIYHLLLDKLRQHR
>gnl|CDD|270524 cd14339, UBA_SNRK, UBA domain of SNF-related serine/threonine-protein kinase (SNRK) and similar proteins mainly found in metazoa. SNRK, also called Sucrose nonfermenting 1 (Snf1)-related kinase, is a serine/threonine kinase highly expressed in the testis. It is a distant member of the largely adenosine monophosphate (AMP)-activated protein kinase (AMPK) family. SNRK can be phosphorylated and activated by LKB1 and may mediate cellular effects regulated by LKB1. It is also involved in the regulation of colon cancer cell proliferation and beta-catenin signaling. It inhibits colon cancer cell proliferation through calcyclin-binding protein (CacyBP)-dependent reduction of beta-catenin. In addition to an N-terminal protein kinase domain, it harbors an ubiquitin-associated (UBA) domain, previously called SNF1 homology (SNH) domain which is conserved in other Snf1-related kinases, but not in any other protein kinase
ENLPEEEHELILQKMESGGIASREAILESLEKDAYDHITATYYLLAER
>gnl|CDD|270525 cd14340, UBA_BRSK, UBA domain found in serine/threonine-protein kinase BRSK1, BRSK2 and similar proteins. The family includes brain-specific kinases BRSK1 and BRSK2. They are AMP-activated protein kinase (AMPK)-related kinases that are highly expressed in mammalian forebrain and crucial for establishing neuronal polarity.BRSK1, also called brain-selective kinase 1, brain-specific serine/threonine-protein kinase 1, BR serine/threonine-protein kinase 1, serine/threonine-protein kinase SAD-B, or synapses of Amphids Defective homolog 1 (SAD1 homolog), is associated with synaptic vesicles and is tightly associated with the presynaptic cytomatrix in nerve terminals. It can regulate neurotransmitter release presynaptically. BRSK2, also called brain-selective kinase 2, brain-specific serine/threonine-protein kinase 2, BR serine/threonine-protein kinase 2, serine/threonine-protein kinase 29, or serine/threonine-protein kinase SAD-A is an AMP-activated protein kinase (AMPK)-related kinase exclusively expressed in brain and pancreas. It plays an essential role in neuronal polarization. It interacts with CDK-related protein kinase PCTAIRE1, a kinase involved in neurite outgrowth and neurotransmitter release, and further negatively regulates glucose-stimulated insulin secretion (GSIS) in pancreatic beta-cells through activation of p21-activated kinase-1 (PAK1). BRSK2 also regulates cell-cycle progression controlled by APC/C(Cdh1) through the ubiquitin-proteasome pathway. Moreover, BRSK2 is regulated by endoplasmic reticulum (ER) stress in protein level and involved in ER stress-induced apoptosis. Both BRSK1 and BRSK2 contain an N-terminal protein kinase catalytic domain followed by an ubiquitin-associated (UBA) domain
DIDPDVLDSMTSLGCFKDKEKLVQELLSPEHNTEKVIYFLLLDRKERKPSCEDD
>gnl|CDD|270526 cd14341, UBA_MELK, UBA domain found in maternal embryonic leucine zipper kinase (MELK) and similar proteins. MELK, also called protein kinase Eg3 (pEg3 kinase), protein kinase PK38 (PK38), or tyrosine-protein kinase MELK, is a cell cycle dependent protein kinase involved in diverse cell processes including stem cell renewal, cell cycle progression, cell proliferation, apoptosis and mRNA processing. It is expressed in normal tissues and especially in cancer cells. It is upregulated in cancer tissues and thus may act as potential anticancer target in diverse tumor entities. MELK comprises an N-terminal protein kinase catalytic domain, followed by an ubiquitin-associated (UBA) domain, and a C-terminal autoinhibitory domain of 5'-AMP-activated protein kinase (AMPK)
ELDEDCITELSVYYGKSREEMEQLIKEWKYDYLTATYLLLLDKKRRGKPVRL
>gnl|CDD|270527 cd14342, UBA_TAP-C, UBA-like domain found in nuclear RNA export factor NXF1, NXF2 and similar proteins. The NXF family of mRNA nuclear export factors including vertebrate NXF1 (also called tip-associated protein or mRNA export factor TAP), NXF2 (also called cancer/testis antigen CT39 or TAP-like protein TAPL-2), Caenorhabditis elegans NXF1 (ceNXF1), Saccharomyces cerevisiae mRNA nuclear export factor Mex67p and similar proteins. NXF proteins can stimulate nuclear export of mRNAs and facilitate the export of unspliced viral mRNA containing the constitutive transport element. It is a multi-domain protein with a nuclear localization sequence (NLS), a non-canonical mRNA-binding domain, and four leucine-rich repeats (LLR) at the N-terminal region. Its C-terminal part contains a NTF2-like domain and a ubiquitin-associated (UBA)-like domain, joined by flexible Pro-rich linker. Caenorhabditis elegans NXF1 are essential for the nuclear export of poly(A)+mRNA. In budding yeast, Mex67p binds mRNAs through its adaptor Yra1/REF. It also interacts directly with Nab2, an essential shuttling mRNA-binding protein required for export. Moreover, Mex67p associates with both nuclear pore protein (nucleoporin) FG repeats and Hpr1, a component of the TREX/THO complex linking transcription and export
QQQMVQQLSAQTGMNLEWSQKCLEDNGWDYEKALANFEELKAQGKIPPEAF
>gnl|CDD|270528 cd14343, UBA_F100B_like, UBA-like domain found in protein FAM100B. The family corresponds to the uncharacterized protein FAM100B and its homologs mainly found in Metazoa. Although their biological roles remain unclear, all family members contain a ubiquitin-associated (UBA)-like domain that may be involved in the binding of ubiquitin
EQVMINQFVLAAGCAADQAKQLLQAAHWQFETALSAFFQ
>gnl|CDD|270529 cd14344, UBA_TYDP2, UBA-like domain found in tyrosyl-DNA phosphodiesterase 2 (TDP2) and similar proteins. TDP2, also called ETS1-associated protein II (EAPII) or TRAF and TNF receptor-associated protein (Ttrap), is a 5'-Tyr-DNA phosphodiesterase, a member of the Mg(2+)/Mn(2+)-dependent family of phosphodiesterases which contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal phosphodiesterase domain. TDP2 is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini needed for subsequent DNA ligation and hence repair of the break. Tyrosyl-DNA phosphodiesterase 1 (TDP1), an enzyme that cleaves 3'-phosphotyrosyl bonds, and TDP2 are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TDP2 has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation. It can associate with CD40, tumor necrosis factor receptor-75 (TNF-R75) and TNF receptor-associated factors (TRAFs) and may inhibit the activation of nuclear factor-kappa B (NF-kappaB)
LLCLEFANVTSCDEAVAQRYLAENGWHMERALNAYFE
>gnl|CDD|270530 cd14345, UBA_UBXD7, UBA-like domain found in UBX domain-containing protein 7 (UBXD7) and similar proteins. UBXD7, also known as UBXN7, functions as a ubiquitin-binding adaptor that mediates the interaction between the AAA+ ATPase p97 (also known as VCP or Cdc48) and the transcription factor HIF1alpha. It binds only to the active, NEDD8- or Rub1-modified form of cullins. UBXD7 contains the ubiquitin-associated (UBA), ubiquitin-associating (UAS), ubiquitin regulatory X (UBX), and ubiquitin-interacting motif (UIM) domains. Either UBA or UIM could serve as a docking site for neddylated-cullins. Moreover, UBA-like domain is required for binding ubiquitylated-protein substrates, UIM motif is responsible for the binding to cullin RING ligases (CRLs), and UBX domain is essential for p97 binding
ALIEQFTSITGADDTVARHMLEACNGNLEMAVNMHLD
>gnl|CDD|270531 cd14346, UBA_Ubx5_like, UBA-like domain found in Saccharomyces cerevisiae UBX domain-containing protein 5 (Ubx5) and similar proteins. Ubx5 is a ubiquitin regulatory X (UBX) domain-containing protein encoded by the open reading frame (ORF) YDR330W in yeast. As the yeast ortholog of mammalian UBXD7, Ubx5 functions as the cofactor of AAA+ ATPase p97, also known as VCP or Cdc48. It binds only to the active, NEDD8- or Rub1-modified form of cullins. Ubx5 contains the ubiquitin-associated (UBA), ubiquitin-associating (UAS), ubiquitin regulatory X (UBX) and ubiquitin-interacting motif (UIM) domains and its UIM domain is required to promote UV-dependent degradation of polyubiquitinated Rpb1
DEQISTFLAITGSEDAAVARQFLEMAGGDLETAVSLFFE
>gnl|CDD|270532 cd14347, UBA_Cezanne_like, UBA-like domain found in OTU domain-containing proteins OTU7A, OTU7B and similar proteins. OTU7A, also called zinc finger protein Cezanne 2, belongs to a family of proteins that have been characterized as highly specific ubiquitin iso-peptidases removing ubiquitin from proteins. OTU7B, also called cellular zinc finger anti-NF-kappaB protein, zinc finger A20 domain-containing protein 1, or zinc finger protein Cezanne, is a novel deubiquitinating enzyme that acts as a negative regulator of NF-kappaB and may play a role in the control of the inflammatory process. Both OTU7A and OTU7B contain an N-terminal ubiquitin-associated (UBA)-like domain, followed by an ovarian tumor (OTU) domain and a ubiquitin binding domain, A20-like zinc finger. In addition, they both display proteolytic activity
DMDAVLSDFVRSTGAEPGLARDLLEGKNWDLTAALSDYEQLRQ
>gnl|CDD|270533 cd14348, UBA_p47, UBA-like domain found in NSFL1 cofactor p47 and similar proteins. p47, also called UBX domain-containing protein 2C, is a major cofactor of the cytosolic AAA ATPase p97. It is required for the p97-regulated membrane reassembly of the endoplasmic reticulum (ER), the nuclear envelope and the Golgi apparatus. p47, together with p97, forms the p97-p47 complex that plays an important role in regulation of membrane fusion events. p47 contains an N-terminal ubiquitin-associated (UBA)-like domain, a central SEP (named after shp1, eyc and p47) domain, and a ubiquitin-like (UBX) domain. UBA-like domain is responsible for forming a highly stable complex with ubiquitin. SEP domain and UBX domain may involve in p47 trimerization or forms a stable complex with the p97 N-terminal domain
DELIAQFVSVTGADEDRAKFFLESAGWDLEAALSSFFESG
>gnl|CDD|270534 cd14349, UBA_CF106, UBA-like domain found in uncharacterized protein C6orf106 and similar proteins. The family corresponds to a group of uncharacterized protein C6orf106 and its homologs mainly found in Metazoa. All family members contain a ubiquitin-associated (UBA)-like domain
DHEELISQFQSILGAQNESEAAFFLEMNNWNLQAAVGAYFD
>gnl|CDD|270535 cd14350, UBA_DCNL, UBA-like domain found in DCN1-like protein DCNL1, DCNL2 and similar proteins. DCNL1 (defective in cullin neddylation protein 1-like protein 1), also called DCUN1 domain-containing protein 1, is encoded by squamous cell carcinoma-related oncogene SCCRO (DCUN1D1). It interacts with known cullin isoforms as well as ROC1, Ubc12 and CAND1, the components of the neddylation pathway. It plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. DCNL1 contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal cullin binding domain that binds to cullins and Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. DCNL2 (defective in cullin neddylation protein 1-like protein 2), also called DCUN1 domain-containing protein 2, is encoded by gene DCUN1D2. Although its biological function remains unclear, DCNL2 shows high sequence similarity with DCNL1 and may also contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Like DCNL1, DCNL2 contains an N-terminal UBA-like domain and a C-terminal cullin binding domain
SQKDKVRQFMSITQANEKTAIQCLKDADWNLELAVDAYFQNP
>gnl|CDD|270536 cd14351, UBA_Ubx1_like, UBA-like domain found in yeast UBX domain-containing protein 1 (Ubx1) and similar proteins. Ubx1, also called suppressor of high-copy PP1 protein (Shp1), is the substrate-recruiting cofactor of AAA-adenosine triphosphatase Cdc48 in Saccharomyces cerevisiae. In concert with ubiquitin-like Atg8, Cdc48 and Ubx1 are involved in the regulation of autophagosome biogenesis. Ubx1 also functions as a regulator of phosphoprotein phosphatase 1 (PP1) with differential effects on glycogen metabolism, meiotic differentiation, and mitotic cell cycle progression. All family members contain an N-terminal ubiquitin-associated (UBA)-like domain
DEAIQQFMELTGASPEVAQQYLEEYGGDLNDAINAYF
>gnl|CDD|270537 cd14352, UBA_DCN1, UBA-like domain found in yeast defective in cullin neddylation protein 1 (DCN1) and similar proteins. DCN1 is a scaffold-type E3 ligase for cullin neddylation. It can bind directly to cullins and the ubiquitin-like protein Nedd8-specific E2 (Ubc12), and regulate cullin neddylation and thus display ubiquitin ligase activity. It contains an N-terminal ubiquitin-associated (UBA)-like domain and a unique C-terminal PONY domain that is essential for the neddylation function of DCN1
ELIKQFREITATSPEVARDYLQRSNWNLNYAVDDFY
>gnl|CDD|270538 cd14353, UBA_FAF, UBA-like domain found in FAS-associated factor FAF1, FAF2 and similar proteins. FAF1, also called UBX domain-containing protein 12 or UBX domain-containing protein 3A, is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF1 is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kappaB (NF-kappaB) by interfering with the nuclear translocation of the p65 subunit. Although the precise role of FAF1 in the ubiquitination pathway remains unclear, FAF1 interacts with valosin-containing protein (VCP) which is involved in the ubiquitin-proteosome pathway. FAF2, also called protein ETEA, UBX domain-containing protein 3B, or UBX domain-containing protein 8, is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. FAF2 shows homology to Fas-associated factor 1 (FAF1). Both of them contain N-terminal ubiquitin-associated (UBA)-like domain, UAS and ubiquitin-like (UBX) domains. Compared to FAF1, however, FAF2 lacks the nuclear targeting domain. The function of FAF2 remains unclear. A yeast two-hybrid assay showed that it can interact with Fas. Because of its homology to FAF1, it is postulated that FAF2 could be involved in modulating Fas-mediated apoptosis of T-cells and eosinophils of atopic dermatitis patients, making them more resistant to apoptosis
FQSITGIEDSDQCRQILEAHNWDLEAAIQTAL
>gnl|CDD|270539 cd14354, UBA_UBP25, UBA domain found in ubiquitin carboxyl-terminal hydrolase 25 (UBP25) and similar proteins. UBP25, also called deubiquitinating enzyme 25, USP on chromosome 21, ubiquitin thioesterase 25, or ubiquitin-specific-processing protease 25, belongs to the deubiquitinating enzyme (DUB) family that specifically hydrolyzes ubiquitin chains on ubiquitin-conjugated proteins. USP25 has one muscular isoform and two ubiquitous isoforms. The longer muscular isoform can bind to muscle-restricted cytoskeletal and sarcomeric proteins, such as myosin binding protein C1 (MyBPC1), actin alpha-1 (ACTA1) and filamin C (FLNC), and further prevent their degradation. USP25 harbors three potential ubiquitin-binding domains (UBDs), one ubiquitin-associated (UBA) domain and two ubiquitin-interacting motifs (UIMs) in the N-terminal region. Its C-terminal tyrosine-rich region is responsible for the binding of the second SH2 domain of SYK, a non-receptor tyrosine kinase that specifically phosphorylates USP25 and alters its cellular levels
KHQQTFLNQLREITGINDVQVLQQALKDSNGNLELAVAFLTAKNAK
>gnl|CDD|270540 cd14355, UBA_UBP28, UBA domain found in ubiquitin carboxyl-terminal hydrolase 28 (UBP28) and similar proteins. UBP28, also called deubiquitinating enzyme 28, ubiquitin thioesterase 28, or ubiquitin-specific-processing protease 28, is an ubiquitin-specific protease that belongs to the deubiquitinating enzyme (DUB) family which specifically hydrolyzes ubiquitin chains on ubiquitin-conjugated proteins. UBP28 can form a ternary complex with nucleoplasmic Fbw7alpha, an F-box protein that is part of an SCF-type ubiquitin ligase, and MYC, a transcription factor encoded by MYC proto-oncogene. UBP28 is required for the stability of MYC, and this stabilization is necessary for tumour-cell proliferation. Besides, UBP28 plays a critical role in the regulation of the Chk2-p53-PUMA pathway. It specifically interacts with 53BP1 and is essential to stabilize Chk2 and 53BP1 in response to DNA damage
MLLNQLREITGIQDPDFLHEALKAANGNLTQAVGVLTEERDK
>gnl|CDD|270541 cd14358, UBA_NAC_euk, UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and its homologs mainly found in eukaryotes. The subfamily contains nascent polypeptide-associated complex subunit alpha (NACA), putative NACA-like protein (NACP1), nascent polypeptide-associated complex subunit alpha domain-containing protein 1 (NACAD), and similar proteins. NACA, also called NAC-alpha or Alpha-NAC, together with BTF3, also called Beta-NAC, form the nascent polypeptide-associated complex (NAC) which is a cytosolic protein chaperone that contacts the nascent polypeptide chains as they emerge from the ribosome. Besides, NACA has a high affinity for nucleic acids and exists as part of several protein complexes playing a role in proliferation, apoptosis, or degradation. It is a cytokine-modulated specific transcript in the human TF-1 erythroleukemic cell line. It also acts as a transcriptional co-activator in osteoblasts by binding to phosphorylated c-Jun, a member of the activator-protein-1 (AP-1) family. Moreover, NACA binds to and regulates the adaptor protein Fas-associated death domain (FADD). In addition, NACA functions as a novel factor participating in the positive regulation of human erythroid-cell differentiation. The biological function of NACP1 (also called Alpha-NAC pseudogene 1 or NAC-alpha pseudogene 1) and NACAD remain unclear. All family members contain an NAC domain and a C-terminal ubiquitin-associated (UBA) domain
PKDIELVMQQANVSRAKAVKALKENDNDIVNAIMELT
>gnl|CDD|270542 cd14359, UBA_AeNAC, UBA-like domain found in archaeal nascent polypeptide-associated complex homolog from Methanothermobacter marburgensis (AeNAC) and similar proteins. AeNAC is a functional archaeal homolog of eukaryotic nascent polypeptide-associated complex (NAC). Both AeNAC and eukaryotic NAC function as the cytosolic chaperone that can bind to ribosomal RNA, interact with the nascent polypeptide chains as they emerge from the ribosome, and assist in post-translational processes. They all contain a NAC domain and an ubiquitin-associated (UBA) domain in the C-terminus. However, unlike eukaryotic NAC, AeNAC forms a ribosome associated homodimer, but not heterodimer. The NAC domain of AeNAC is responsible for the homodimer formation
EISEEDIELVMEQTGVSREEARKALEESGGDLAEAILKLT
>gnl|CDD|270543 cd14360, UBA_NAC_like_bac, UBA-like domain found in uncharacterized bacteria proteins similar to eukaryotic nascent polypeptide-associated complex proteins (NAC). This subfamily contains a group of uncharacterized proteins found in bacteria. They all contain an N-terminal ubiquitin-associated (UBA) that shows high sequence similarity with that of eukaryotic nascent polypeptide-associated complex proteins (NAC) which is one of the cytosolic chaperones that contact the nascent polypeptide chains as they emerge from the ribosome and assist in post-translational processes
LEKVDILRERTNISYEEAKEALEKCNGDLLDALIYLER
>gnl|CDD|270544 cd14361, UBA_HYPK, UBA-like domain found in Huntingtin-interacting protein K (HYPK) and similar proteins. HYPK, also called Huntingtin yeast partner K or Huntingtin yeast two-hybrid protein K, is an intrinsically unstructured Huntingtin (HTT)-interacting protein with chaperone-like activity. It is involved in regulating cell growth, cell cycle, unfolded protein response, and cell death. All members in this subfamily contain an N-terminal ubiquitin-associated (UBA) that shows high sequence similarity with that of eukaryotic nascent polypeptide-associated complex proteins (NAC) which is one of the cytosolic chaperones that contact the nascent polypeptide chains as they emerge from the ribosome and assist in post-translational processes
VKVKKEDVELIVNELEVSKAQAERALREHNGDVVKALRALI
>gnl|CDD|270545 cd14362, CUE_TAB2_TAB3, CUE domain found in the N-terminal of TGF-beta-activated kinase 1 and MAP3K7-binding proteins TAB2, TAB3 and similar proteins. TAB2, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 2, TAK1-binding protein 2, or TGF-beta-activated kinase 1-binding protein 2, is an adaptor protein that regulates activation of TAK1, a MAP kinase kinase kinase (MAPKKK), through linking TAK1 to TRAF6 in the Interleukin-1 (IL-1) induced NF-kappaB activation pathway. TAB3, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 3, NF-kappa-B-activating protein 1, TAK1-binding protein 3, or TGF-beta-activated kinase 1-binding protein 3, is a TAB2-like TAK1-binding protein that activates NF-kappaB similar to TAB2. It activates TAK1 and regulates its association with TRAF2 and TRAF6. Moreover, TAB3 interacts with TRAF6 and TRAF2 in an IL-1- and a TNF-dependent manner, respectively. In summary, TAB2 and TAB3 function redundantly as mediators of TAK1 activation in IL-1 and TNF signal transduction. Both of them contain an N-terminal CUE domain, a coiled-coil (CC) region, a TAK1-binding domain and a C-terminal Npl4 zinc finger (NZF) ubiquitin-binding domain (UBD)
DMQLFHELKQRFPEVPDAVVSQCMLQNNHNREACCAALQKES
>gnl|CDD|270546 cd14363, CUE_TOLIP, CUE domain found in the C-terminal of toll-interacting protein (Tollip) and similar proteins. Tollip is a new component of the IL-1RI pathway which contains an N-terminal C2 domain and a C-terminal CUE domain. Tollip binds to the cytoplasmic TIR domain of IL-1Rs after IL-1 stimulation. It is sufficient for recruitment of IRAK to IL-1Rs and negatively regulates IL-1-induced signaling by inhibiting IRAK phosphorylation. In addition, Tollip directly interacts with toll-like receptors TLR2 and TLR4, and plays an inhibitory role in TLR-mediated cell activation through suppressing phosphorylation and kinase activity of IRAK. Moreover, Tollip can associate with GAT domains of Tom1 and its related proteins Tom1L1 and Tom1L2, and facilitate the recruitment of clathrin onto endosomes
TEEDLKQIQEMFPNVDKEVIKSVLEANRGNKDAAINSLLQM
>gnl|CDD|270547 cd14364, CUE_ASCC2, CUE domain found in activating signal cointegrator 1 complex subunit 2 (ASCC2) and similar proteins. ASCC2, also called ASC-1 complex subunit p100 or Trip4 complex subunit p100, together with ASCC1 (also called p50) and ASCC3 (also called p300), form the activating signal cointegrator complex (ASCC). ASCC plays an essential role in activating protein 1 (AP-1), serum response factor (SRF), and nuclear factor kappaB (NF-kappaB) transactivation. It acts as a transcriptional coactivator of nuclear receptors and regulates the transrepression between nuclear receptors and either AP-1 or NF-kappaB in vivo. Members in this family all contain a CUE domain
DSLISQVKDILPDLGEGFIEACLEHYNGNVERVINALLEG
>gnl|CDD|270548 cd14365, CUE_N4BP2, CUE domain found in NEDD4-binding protein 2 (N4BP2) and similar proteins. N4BP2 has been identified as an oncogene bcl-3 coding protein BCL-3-binding protein (B3BP) that participates in connecting transcriptional activation and genetic recombination of the Ig gene. In addition to BCL-3, it also interacts with p300/CBP histone acetyltransferases. N4BP2 shows intrinsic ATP binding and hydrolyzing activity. It contains an N-terminal ATP-binding region that is responsible for the interaction with BCL-3 and p300/CBP. N4BP2 also functions as a 5'-polynucleotide kinase that can transfer a phosphate group to the 5' end of DNA and RNA substrates. Moreover, N4BP2 contains a C-terminal MutS-related domain that possesses nicking endonuclease activity and may play a role in DNA mismatch repair (MMR). This model corresponds to CUE domain in the N-terminus of N4BP2
QEELFQQLQEMFSGKLDPSVVYMVLSECDFKVDNAMDTLLNL
>gnl|CDD|270549 cd14366, CUE_CUED1, CUE domain found in CUE domain-containing protein 1 (CUED1) and similar proteins. The subfamily includes a group of uncharacterized CUE domain-containing protein termed CUED1. Their biological function remains unknown
EFEQAMEDLKTMFPNMDREVIEAVLRANNGHVEATIDQLLAM
>gnl|CDD|270550 cd14367, CUE_CUED2, CUE domain found in CUE domain-containing protein 2 (CUED2) and similar proteins. CUEDC2 is a novel negative regulator of progesterone receptor (PR) and functions to promote the progesterone-induced PR degradation by the ubiquitin-proteasome pathway. It also acts as the regulator of JAK1/STAT3 signaling through inhibiting cytokine-induced phosphorylation of JAK1 and STAT3 and the subsequent STAT3 transcriptional activity. All members in this subfamily contain a CUE domain
LKDQVDLLLEMFPSCSSLEAKHCLAVAKGDLEEAVQLLLERQ
>gnl|CDD|270551 cd14368, CUE_DEF1_like, CUE domain found in fungal RNA polymerase II degradation factor 1 (DEF1) and similar proteins. DEF1, also called RRM3-interacting protein 1, is a RNA Polymerase II (RNAPII) degradation factor that may be required to couple arrested RNAPII to the proteasome to facilitate its degradation. It contains a CUE domain that is responsible for the binding of ubiquitin. The family also includes many uncharacterized hypothetical proteins. They show a high level of sequence similarity with DEF1
YSSKLASLKELFPDWTDEDLLSALQEVNGDLEVAIDRISEG
>gnl|CDD|270552 cd14369, CUE_VPS9_like, CUE domain found in vacuolar protein sorting-associated protein 9 (VPS9) and similar proteins. VPS9, also called vacuolar protein-targeting protein 9, is a cytosolic yeast protein required for localization of vacuolar proteins, such as the soluble vacuolar hydrolases CPY and PrA. It may bind and act as an effector of a rab GTPase and plays a role in vacuolar protein sorting (VPS) pathway. VPS9 contains a region called GBH domain that is related to mammalian Ras-binding proteins, Rin1 and JC265, and may negatively regulate Ras-mediated signaling in yeast Saccharomyces cerevisiae. This model corresponds to the N-terminal CUE domain that interacts specifically with monoubiquitin and regulates intramolecular monoubiquitylation
EHKETLNTLQEMFPDLDKEIIKDVVIAKKGRIGECVDACLQL
>gnl|CDD|270553 cd14370, CUE_DMA, CUE-like DMA domain found in the DM domain gene family encodes putative transcription factors DMRTA1, DMRTA2 and DMRTA3. The DM domain proteins are related to the sexual regulators doublesex from Drosophila melanogaster and MAB-3 from Caenorhabditis elegans. Thus, they have been named as doublesex- and mab-3-related transcription factors and may be involved in sexual development or in somite development. All DM domain proteins contain a DM domain which is an unusual zinc finger motif. In addition to an N-terminal DM domain, members in this family, including DMRTA1, DMRTA2 and DMRTA3, also harbor additional CUE-like DMA domain. DMRTA1 is encoded by gene DMRT1, a vertebrate equivalent of the D. melanogaster master sex regulator gene, doublesex. In D. melanogaster, doublesex controls the terminal switch of the pathway leading to sex fate choice. DMRT1 may function as regulator of sex differentiation in vertebrate. Especially, it is required for testis differentiation, but is not involved in the gonadal sex fate choice. DMRTA2, also called Doublesex- and mab-3-related transcription factor 5 (DMRT5), is encoded by gene DMRT2. In the zebrafish, DMRT2 is involved in somite development. DMRTA2 may act as an activator of cyclin-dependent kinase inhibitor 2C (cdkn2c) during spermatogenesis. It may also play significant roles in embryonic neurogenesis. DMRTA3 is encoded by tumor suppressor gene DMRT3 which serves as a novel potential target for homozygous deletion in squamous cell carcinoma of the lung
SRRSPIELLTRLFPHQKRSVLELILQGCGGDLVQAIEQVL
>gnl|CDD|270554 cd14371, CUE_CID7_like, CUE domain found in CTC-interacting domain proteins CID5, CID6, CID7 and similar proteins. CID7 is encoded by ubiquitously expressed gene CID7. It contains an N-terminal PABC-interacting domain (PAM2 or PABP-interacting motif 2) which is also found in the human Paip1 and Paip2. At this point, it functions as an interaction partner of the PABC domain of Arabidopsis thaliana Poly(A)-binding proteins. It also harbors an ubiquitin-associated (UBA)-like CUE domain and a C-terminal small MutS-related (SMR) domain. CID5 and CID6 are encoded by gene CID5, CID6, respectively. CID5 is only expressed in immature siliques. The biological function of CID5 and CID6 remain unclear
LADVELLSSMFPGVSADSIAEVYEANGGDLDLTIDMLTQLESQ
>gnl|CDD|270555 cd14372, CUE_Cue5p_like, CUE domain found in yeast ubiquitin-binding protein CUE5 (Cue5p), donuts protein 1 (DON1p) and similar proteins. Cue5p, also called coupling of ubiquitin conjugation to ER degradation protein 5, is encoded by the open reading frame (ORF) Yor042. It contains a CUE domain which exhibits weak ubiquitin binding properties. Donuts protein 1 (DON1p) is encoded by the ORF YDR273w. It localizes specifically to the prospore membrane and is expressed exclusively during meiosis. DON1p may function as a unique marker to investigate the defects associated with the impaired function of the meiotic plaque in the mpc- mutants
EQESAIKILKEAFPDVDDKVIKAILIASQGDLEPAFNALLGLTDP
>gnl|CDD|270556 cd14373, CUE_Cue3p_like, CUE domain found in yeast ubiquitin-binding protein CUE3 (Cue3p) and similar proteins. Cue3p, also called coupling of ubiquitin conjugation to ER degradation protein 3, is encoded by the open reading frame (ORF) YGL110C. It is involved in the intramolecular monoubiquitination that serves as a regulatory signal in a variety of cellular processes in yeast. Cue3p contains a CUE domain
EEDISTLSELFPDLTEYQIKTLLKKYDNNVELVTNILLENP
>gnl|CDD|270557 cd14374, CUE1_Cue2p_like, CUE1 domain found in yeast ubiquitin-binding protein CUE2 (Cue2p) and similar proteins. Cue2p, also called coupling of ubiquitin conjugation to ER degradation protein 2, is encoded by the open reading frame (ORF) YKL090W. It is involved in the intramolecular monoubiquitination that serves as a regulatory signal in a variety of cellular processes in yeast. Cue2p contains two tandem CUE domains at the N-terminus. Both of them can bind monoubiquitin independently. This model corresponds to the first CUE domain
ESKISTLRDMFPNLSIDQAVDALKTNNNDLDQTIDYLLANNA
>gnl|CDD|270558 cd14375, CUE2_Cue2p_like, CUE2 domain found in yeast ubiquitin-binding protein CUE2 (Cue2p) and similar proteins. Cue2p, also called coupling of ubiquitin conjugation to ER degradation protein 2, is encoded by the open reading frame (ORF) YKL090W. It is involved in the intramolecular monoubiquitination that serves as a regulatory signal in a variety of cellular processes in yeast. Cue2p contains two tandem CUE domains at the N-terminus. Both of them can bind monoubiquitin independently. This model corresponds to the second CUE domain
SNDLDELKDMFPNLDSEVIEDCYVLCEKNVERTVSALL
>gnl|CDD|270559 cd14376, CUE_AUP1_AMFR_like, CUE domain found in ancient ubiquitous protein 1 (AUP1), autocrine motility factor receptor (AMFR) and similar proteins. AUP1 is a component of the HRD1-SEL1L endoplasmic reticulum (ER) quality control complex and is essential for US11-mediated dislocation of class I MHC heavy chains. AMFR is an internalizing cell surface glycoprotein that is localized in both plasma membrane caveolae and the ER, and involves in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. Cue1p is an N-terminally membrane-anchored endoplasmic reticulum (ER) protein essential for the activity of the two major yeast RING finger ubiquitin ligases (E3s) implicated in ER-associated degradation (ERAD). This family also includes plant E3 ubiquitin protein ligases RIN2, RIN3, and similar proteins. Comparing with other CUE domain-containing proteins, some family members from higher eukaryotes do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains
EEMVEQVQEVFPHIPREAIRRDLQRTNSVDLTINNIL
>gnl|CDD|270560 cd14377, UBA1_Rad23, UBA1 domain of Rad23 proteins found in metazoa. The family includes mammalian orthologs of yeast nucleotide excision repair (NER) proteins, Rad23p (in Saccharomyces cerevisiae) and Rhp23p (in Schizosaccharomyces pombe). Rad23 proteins play dual roles in DNA repair as well as in proteosomal degradation. They have affinity for both the proteasome and ubiquitinylated proteins and participate in translocating polyubiquitinated proteins to the proteasome. Rad23 proteins carry a ubiquitin-like (UBL) and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. UBL domain is responsible for the binding to proteasome. UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates which suggests Rad23 proteins might be involved in certain pathways of ubiquitin metabolism. Both UBL domain and XPC-binding domain are necessary for efficient NER function of Rad23 proteins. This model corresponds to the UBA1 domain
EYENMVTEIMSMGFERDQVVRALRASFNNPDRAVEYLLSG
>gnl|CDD|270561 cd14378, UBA1_Rhp23p_like, UBA1 domain of Schizosaccharomyces pombe UV excision repair protein Rhp23p and its homologs. The subfamily contains several fungal multi-ubiquitin receptors, including Schizosaccharomyces pombe Rhp23p and Saccharomyces cerevisiae Rad23p, both of which are orthologs of human HR23A. They play roles in nucleotide excision repair (NER) and in cell cycle regulation. They also function as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. For instance, S. pombe Rhp23p forms a complex with Rhp41p to recognize photolesions and help initiate DNA repair, and it also protects ubiquitin chains against disassembly by deubiquitinating enzymes. Like human HR23A, members in this subfamily interact with the proteasome through their N-terminal ubiquitin-like domain (UBL), and with ubiquitin (Ub), or multi-ubiquitinated substrates, through their two ubiquitin-associated domains (UBA), termed internal UBA1 and C-terminal UBA2. In addition, they contain a xeroderma pigmentosum group C (XPC) protein-binding domain that might be necessary for its efficient NER function. This model corresponds to the UBA1 domain
LVVGLDYNQTVQNIMEMGYEREQVERALRASFNNPDRAVEYLLTGIP
>gnl|CDD|270562 cd14379, UBA1_Rad23_plant, UBA1 domain of putative DNA repair proteins Rad23 found in plant. The radiation sensitive 23 (Rad23) subfamily consists of four isoforms of putative DNA repair proteins from Arabidopsis thaliana and similar proteins from other plants. The nuclear-enriched Rad23 proteins function in the cell cycle, morphology, and fertility of plants through their delivery of ubiquitin (Ub)/26S proteasome system (UPS) substrates to the 26S proteasome. Rad23 proteins contain an N-terminal ubiquitin-like (UBL) domain that associates with the 26S proteasome Ub receptor RPN10, and two C-terminal ubiquitin-associated (UBA) domains that bind Ub conjugates. This model corresponds to the UBA1 domain
LVAGSSLEQTVQQIMDMGGGSWDRDTVVRALRAAYNNPERAVEYLYSGIP
>gnl|CDD|270563 cd14380, UBA2_Rad23, UBA2 domain of Rad23 proteins found in metazoa. The family includes mammalian orthologs of yeast nucleotide excision repair (NER) proteins, Rad23p (in Saccharomyces cerevisiae) and Rhp23p (in Schizosaccharomyces pombe). Rad23 proteins play dual roles in DNA repair as well as in proteosomal degradation. They have affinity for both the proteasome and ubiquitinylated proteins and participate in translocating polyubiquitinated proteins to the proteasome. Rad23 proteins carry a ubiquitin-like (UBL) and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. UBL domain is responsible for the binding to proteasome. UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates which suggests Rad23 proteins might be involved in certain pathways of ubiquitin metabolism. Both UBL domain and XPC-binding domain are necessary for efficient NER function of Rad23 proteins. This model corresponds to the UBA2 domain
EEREAIERLKALGFPEGLVIQAYFACDKNENLAANFLLS
>gnl|CDD|270564 cd14381, UBA2_Rhp23p_like, UBA2 domain of Schizosaccharomyces pombe UV excision repair protein Rhp23p and its fungal homologs. The subfamily contains several fungal multiubiquitin receptors, including Schizosaccharomyces pombe Rhp23p and Saccharomyces cerevisiae Rad23p, both of which are orthologs of human HR23A. They play roles in nucleotide excision repair (NER) and in cell cycle regulation. They also function as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. For instance, S. pombe Rhp23p forms a complex with Rhp41p to recognize photolesions and help initiate DNA repair, and it also protects ubiquitin chains against disassembly by deubiquitinating enzymes. Like human HR23A, members in this subfamily interact with the proteasome through their N-terminal ubiquitin-like domain (UBL), and with ubiquitin (Ub), or multi-ubiquitinated substrates, through their two ubiquitin-associated domains (UBA), termed internal UBA1 and C-terminal UBA2. In addition, they contain a xeroderma pigmentosum group C (XPC) protein-binding domain that might be necessary for its efficient NER function. This model corresponds to the UBA2 domain
EEDQAIDRLCELGFDRDLVIQAYLACDKNEEMAANFLFEN
>gnl|CDD|270565 cd14382, UBA2_RAD23_plant, UBA2 domain of putative DNA repair proteins RAD23 found in plant. The radiation sensitive 23 (RAD23) subfamily consists of four isoforms of putative DNA repair proteins from Arabidopsis thaliana and similar proteins from other plants. The nuclear-enriched RAD23 proteins function in the cell cycle, morphology, and fertility of plants through their delivery of ubiquitin (Ub)/26S proteasome system (UPS) substrates to the 26S proteasome. RAD23 proteins contain an N-terminal ubiquitin-like (UBL) domain that associates with the 26S proteasome Ub receptor RPN10, and two C-terminal ubiquitin-associated (UBA) domains that bind Ub conjugates. This model corresponds to the UBA2 domain
VTPEEREAIERLEAMGFDRALVIEAFLACDKNEELAANYLLEH
>gnl|CDD|270566 cd14383, UBA1_UBP5, UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5). UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA1 domain
MLDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFA
>gnl|CDD|270567 cd14384, UBA1_UBP13, UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13). UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13, is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA1 domain
DIDESSVMQLAEMGFPLEACRKAVYYTGNMGAEVAFNWIIAHMEEPDFA
>gnl|CDD|270568 cd14385, UBA1_spUBP14_like, UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins. spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain
NAEALAQLLGMGFPEVRCKKALLATGNSDAEAAMNWLFEHMDDPDID
>gnl|CDD|270569 cd14386, UBA2_UBP5, UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5). UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA2 domain
VPEEAVAMLVSMGFTRDQAIKALKATDNNVERAADWIFSHPDE
>gnl|CDD|270570 cd14387, UBA2_UBP13, UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13). UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13 is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA2 domain
EESIAILMSMGFPRNRAIEALKRTNNNLDRALDWL
>gnl|CDD|270571 cd14388, UBA2_atUBP14, UBA2 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins. atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain which show a high level of sequence similarity with mammalian ubiquitin-associated and SH3 domain-containing protein A (UBS3A)
SSVDTLVSFGFAADVARKALKATGGDIERAAEWIFNNS
>gnl|CDD|270572 cd14389, UBA_AAA_plant, UBA domain found in plant AAA-type ATPase-like proteins. This family includes some uncharacterized AAA-type ATPase-like proteins found in plant. The AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. Members in this family contains an N-terminal ubiquitin-association (UBA) domain, a AAA-type ATPase domain and a C-terminal MgsA AAA+ ATPase domain. This model corresponds to the UBA domain which show a high level of sequence similarity with mammalian ubiquitin-associated and SH3 domain-containing protein A (UBS3A)
MEQLVDMGFSSDLAAEALAATGGKSTQKATEWILSHR
>gnl|CDD|270573 cd14390, UBA_II_E2_UBE2K, UBA domain of vertebrate ubiquitin-conjugating enzyme E2 K (UBE2K). UBE2K, also called Huntingtin-interacting protein 2 (HIP-2), ubiquitin carrier protein, ubiquitin-conjugating enzyme E2-25 kDa (E2-25K), or ubiquitin-protein ligase is a multi-ubiquitinating enzyme with the ability to synthesize Lys48-linked polyubiquitin chains which is involved in the ubiquitin (Ub)-dependent proteolytic pathway. It interacts with the frameshift mutant of ubiquitin B and functions as a crucial factor regulating amyloid-beta neurotoxicity. It has also been characterized as Huntingtin-interacting protein that modulates the neurotoxicity of Amyloid-beta (Abeta), the principal protein involved in Alzheimer's disease pathogenesis. Moreover, E2-25K increases aggregate the formation of expanded polyglutamine proteins and polyglutamine-induced cell death in the pathology of polyglutamine diseases. UBE2K and its yeast homolog UBC1 are unique class II E2 conjugating enzymes, both of which contain a C-terminal ubiquitin-associated (UBA) domain in addition to an N-terminal catalytic ubiquitin-conjugating enzyme E2 (UBCc) domain
TKKIENLCAMGFDRNAVIVALSSKSWDVETATELLLSN
>gnl|CDD|270574 cd14391, UBA_II_E2_UBCD4, UBA domain found in Drosophila melanogaster ubiquitin-conjugating enzyme E2-22 kDa (UbcD4) and similar proteins. UbcD4, also called ubiquitin carrier protein or ubiquitin-protein ligase, is a class II E2 ubiquitin-conjugating enzyme encoded by Drosophila E2 gene which is only expressed in pole cells in embryos. It is a putative E2 enzyme homologous to the Huntingtin interacting protein-2 (HIP2) of human. UbcD4 specifically interacts with the polyubiquitin-binding subunit of the proteasome. It contains a C-terminal ubiquitin-associated (UBA) domain in addition to an N-terminal catalytic ubiquitin-conjugating enzyme E2 (UBCc) domain
DAKIRQLMDMGFDEHKARVALSSHNWDLEKATESLF
>gnl|CDD|270575 cd14392, UBA_Cbl-b, UBA domain found in E3 ubiquitin-protein ligase Cbl-b and similar proteins. Cbl-b, also called casitas B-lineage lymphoma proto-oncogene b, RING finger protein 56, SH3-binding protein Cbl-b, or signal transduction protein Cbl-b, has been identified as a regulator of antigen-specific, T cell-intrinsic, peripheral immune tolerance (a state also called clonal anergy). It may inhibit activation of the p85 subunit of phosphoinositide 3-kinase (PI3K), protein kinase C-theta (PKC-theta), and phospholipase C-gamma1 (PLC-gamma1) and negatively regulates T-cell receptor-induced transcription factor nuclear factor-kappaB (NF-kappaB) activation. In addition, Cbl-b may target multiple signaling molecules involved in transforming growth factor (TGF)-beta-mediated transactivation pathways. Cbl-b contains a proline rich domain, a nuclear localization signal, a C3HC4 zinc finger and a ubiquitin-associated (UBA) domain
NVDAKIAKLMGEGYSFEEVKRALEIAQNNVEVARSILREFA
>gnl|CDD|270576 cd14393, UBA_c-Cbl, UBA domain found in E3 ubiquitin-protein ligase Cbl and similar proteins. Cbl, also called casitas B-lineage lymphoma proto-oncogene, proto-oncogene c-Cbl, RING finger protein 55, or signal transduction protein Cbl, is a multi-domain protein that acts as a key negative regulator of various receptor and non-receptor tyrosine kinases signaling. It contains a tyrosine kinase-binding domain (TKB), a proline-rich domain, a RING domain, and a ubiquitin-associated (UBA) domain. The TKB is responsible for the interactions with many tyrosine kinases, such as the colony-stimulating factor-1 (CSF-1) receptor, Syk/ZAP-70 and Src-family of protein tyrosine kinases. The proline-rich domain can recruit proteins with SH3 domain. Moreover, Cbl functions as an E3 ubiquitin ligase that can bind ubiquitin-conjugating enzymes (E2s) through RING domain
LSSEIENLMSQGYSYQDIQKALVIAQNNIEMAKNILREFV
>gnl|CDD|270577 cd14394, UBA_BIRC2_3, UBA domain found in baculoviral IAP repeat-containing protein BIRC2, BIRC3 and similar proteins. The subfamily includes cellular inhibitor of apoptosis protein 1 (c-IAP1) and c-IAP2. c-IAPs function as ubiquitin E3 ligases that mediate the ubiquitination of the substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB)signaling, and oncogenesis. Unlike other apoptosis proteins (IAPs), such as XIAP, c-IAPs exhibit minimal binding to caspases and may not play an important role in the inhibition of these proteases. c-IAP1, also called baculoviral IAP repeat-containing protein BIRC2, IAP-2, RING finger protein 48, or TNFR2-TRAF-signaling complex protein 2, is a potent regulator of the tumor necrosis factor (TNF) receptor family and NF-kappaB signaling pathways in the cytoplasm. It can also regulate E2F1 transcription factor-mediated control of cyclin transcription in the nucleus. c-IAP2, also called BIRC3, IAP-1, apoptosis inhibitor 2 (API2), or IAP homolog C, also influences ubiquitin-dependent pathways that modulate innate immune signalling by activation of NF-kappaB. c-IAPs contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of binds polyubiquitin (polyUb), a caspase activation and recruitment domain (CARD) that serves as a protein interaction surface, and a RING domain at the carboxyl terminus that is required for ubiquitin ligase activity
MNTPVVKSALEMGFNRRLVKQTVQSKILTSGENYKTVNDLVSDLLSAEDE
>gnl|CDD|270578 cd14395, UBA_BIRC4_8, UBA domain found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP repeat-containing protein 8 (BIRC8) and similar proteins. XIAP, also called baculoviral IAP repeat-containing protein 4 (BIRC4), IAP-like protein (ILP), inhibitor of apoptosis protein 3 (IAP-3), or X-linked inhibitor of apoptosis protein (X-linked IAP), is a potent suppressor of apoptosis that directly inhibits specific members of the caspase family of cysteine proteases, including caspase-3, -7, and -9. It promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. The ubiquitin-protein ligase (E3) activity of XIAP also exhibits in the ubiquitination of second mitochondria-derived activator of caspases (Smac). The mitochondrial proteins, Smac/DIABLO and Omi/HtrA2, can inhibit the antiapoptotic activity of XIAP. XIAP has also been implicated in several intracellular signaling cascades involved in the cellular response to stress, such as the c-Jun N-terminal kinase (JNK) pathway, the nuclear factor-kappaB (NF-kappaB) pathway, and the transforming growth factor-beta (TGF-beta) pathway. Moreover, XIAP can regulate copper homeostasis through interacting with MURR1. BIRC8, also called inhibitor of apoptosis-like protein 2 (IAP-like protein 2 or ILP-2), or testis-specific inhibitor of apoptosis, is a tissue-specific homolog of E3 ubiquitin-protein ligase XIAP. It has been implicated in the control of apoptosis in the testis by direct inhibition of caspase 9. Both XIAP and BIRC8 contain three N-terminal baculoviral IAP repeat (BIR) domains, a ubiquitin-association (UBA) domain and a RING domain at the carboxyl terminus
ILQNPLVQEAIRMGFSFKEIKKIMEEKLKTSGSNYTSLEVLVADLVSAQK
>gnl|CDD|270579 cd14396, UBA_XtBIRC7_like, UBA domain found in Xenopus tropicalis baculoviral IAP repeat-containing protein BIRC7, BIRC71A and similar proteins. X. tropicalis BIRC7, also called E3 ubiquitin-protein ligase EIAP, embryonic/Egg IAP (xEIAP/XLX), inhibitor of apoptosis (IAP)-like protein, XIAP homolog XLX, is a weak apoptosis inhibitor that exhibits caspase inhibition and autoubiquitylation. It is uniquely modified by MAPK- and Cdc2/Cyclin B-dependent phosphorylation during oocyte maturation. Its caspase-dependent cleavage is altered when it is phosphorylated. X. tropicalis BIRC7 contains two N-terminal baculoviral IAP repeats (BIRs) and a C-terminal RING domain. Based on sequence homology, it also harbors a ubiquitin-associated (UBA) domain which is not detected in human BIRC7
SVVQAVLQMGFDQSLVESLVQNKYLLTGPAYTSVSQLVSDLLQE
>gnl|CDD|270580 cd14397, UBA_LATS1, UBA domain found in vertebrate serine/threonine-protein kinase LATS1. LATS1, also called large tumor suppressor homolog 1 or WARTS protein kinase (warts), is a serine/threonine-protein kinase that highly conserved from fly to human. It plays a crucial role in the prevention of tumor formation by controlling mitosis progression. Human LATS1 is the mammalian homologs of Drosophila lats/warts gene that could suppress tumor growth and rescue all developmental defects in flies, including embryonic lethality. It forms a regulatory complex with zyxin, a regulator of actin filament assembly. The LATS1/zyxin complex plays a role in controlling mitosis progression on mitotic apparatus. LATS1 is phosphorylated in a cell-cycle-dependent manner and complexes with CDC2 in early mitosis. It can negatively modulates tumor cell growth by inducing G(2)/M cell cycle transition or apoptosis. It also functions as a mitotic exit network kinase interacting with MOB1A, a protein whose homolog in budding yeast associates with kinases involved in mitotic exit. Moreover, LATS1 acts as a novel cytoskeleton regulator that affects cytokinesis by regulating actin polymerization through inhibiting LIMK1. LATS1 can also inhibit transcription regulation and transformation functions of oncogene YAP by inhibiting its nuclear translocation through phosphorylation. In addition, LATS1 can regulate the transcriptional activity of forkhead L2 (FOXL2) via phosphorylation. It also acts as an acting-binding protein that can negatively regulate the actin polymerization. LATS1 contains an N-terminal ubiquitin-associated (UBA) domain and a C-terminal protein kinase domain
RQMLQDLQAAGFDEDMVIQALQQTNNRSIEAAIEFISKMSY
>gnl|CDD|270581 cd14398, UBA_LATS2, UBA domain found in vertebrate serine/threonine-protein kinase LATS2. LATS2, also called kinase phosphorylated during mitosis protein, or large tumor suppressor homolog 2, or serine/threonine-protein kinase KPM, or Warts-like kinase, is a novel mammalian homolog of the Drosophila tumor suppressor gene lats/warts. It inhibits the G1/S transition and is essential for embryonic development, proliferation control, and genomic integrity. LATS2 is a serine/threonine kinase that negatively regulates CyclinE/CDK2 and plays a role in tumor suppression. It also acts as the negative regulator of androgen receptor (AR) through inhibiting androgen-regulated gene expression and thus plays an important role in AR -regulated transcription and in the development of prostate cancer. Moreover, LATS2 induces apoptosis via down-regulation of anti-apoptotic proteins, BCL-2 and BCL-x(L), in human lung cancer cells. It is a centrosomal protein and forms a complex with Ajuba, a LIM protein, to regulate organization of the spindle apparatus through recruitment of gamma-tubulin to the centrosome during mitosis. Furthermore, LATS2 interacts with Mdm2 to inhibit p53 ubiquitination and promote p53 activation. It stabilizes the cellular protein level of Snail1, a central regulator of epithelial cell adhesion and movement in epithelial-to-mesenchymal transitions (EMTs) during embryo development, and enhances its EMT activity. LATS2 contains an N-terminal ubiquitin-associated (UBA) domain and a C-terminal protein kinase domain
RQMLQELVNAGCDQEMAVRALKQTGSRSIEAALEYISKMSY
>gnl|CDD|270582 cd14399, UBA_PLICs, UBA domain of eukaryotic protein linking integrin-associated protein (IAP, also known as CD47) with cytoskeleton (PLIC) proteins. The PLIC proteins (or ubiquilins) family contains human homologs of the yeast ubiquitin-like Dsk2 protein, PLIC-1 (also called ubiquilin-1), PLIC-2 (also called ubiquilin-2 or Chap1), PLIC-3 (also called ubiquilin-3) and PLIC-4 (also called ubiquilin-4, Ataxin-1 interacting ubiquitin-like protein, A1Up, Connexin43-interacting protein of 75 kDa, or CIP75), and mouse PLIC proteins. They are ubiquitin-binding adaptor proteins involved in all protein degradation pathways through delivering ubiquitinated substrates to proteasomes. They also promote autophagy-dependent cell survival during nutrient starvation. PLIC-1 regulates the function of the thrombospondin receptor CD47 and G protein signaling. It plays a role in TLR4-mediated signaling through interacting with the Toll/interleukin-1 receptor (TIR) domain of TLR4. It also inhibits the TLR3-Trif antiviral pathway by reducing the abundance of Trif. Moreover, PLIC-1 binds to gamma-aminobutyric acid receptors (GABAARs) and modulates the ubiquitin-dependent, proteasomal degradation of GABAARs. Furthermore, PLIC-1 acts as a molecular chaperone regulating amyloid precursor protein (APP) biosynthesis, trafficking, and degradation by stimulating K63-linked polyubiquitination of lysine 688 in the APP intracellular domain. In addition, PLIC-1 is involved in the protein aggregation-stress pathway via associating with the ubiquitin-interacting motif (UIM) proteins ataxin 3, HSJ1a, and epidermal growth factor substrate 15 (EPS15). PLIC-2 is a protein that binds the ATPase domain of the HSP70-like Stch protein. It functions as a negative regulator of G protein-coupled receptor (GPCR) endocytosis. It also involved in amyotrophic lateral sclerosis (ALS)-related dementia. PLIC-3 is encoded by UBQLN3, a testis-specific gene. It shows high sequence similarity with the Xenopus protein XDRP1, a nuclear phosphoprotein that binds to the N-terminus of cyclin A and inhibits Ca2+-induced degradation of cyclin A, but not cyclin B. PLIC-4 is a ubiquitin-like nuclear protein that interacts with ataxin-1 and further links ataxin-1 with the chaperone and ubiquitin-proteasome pathways. It also binds to the non-ubiquitinated gap junction protein connexin43 (Cx43) and regulates the turnover of Cx43 through the proteasomal pathway. PLIC proteins contain an N-terminal ubiquitin-like (UBL) domain that is responsible for the binding of ubiquitin-interacting motifs (UIMs) expressed by proteasomes and endocytic adaptors, and C-terminal ubiquitin-associated (UBA) domain that interacts with ubiquitin chains present on proteins destined for proteasomal degradation. In addition, mammalian PLIC2 proteins have an extra collagen-like motif region which is absent in other PLIC proteins and the yeast Dsk2 protein
RYASQLEQLQAMGFVDRQANIQALIATGGNVNAAIERLLG
>gnl|CDD|270583 cd14400, UBA_Gts1p_like, UBA domain found in Saccharomyces cerevisiae protein GTS1 (Gts1p) and similar proteins. Gts1p, also called protein LSR1, is encoded by a pleiotropic gene GTS1 in budding yeast. The formation of Gts1p-mediated protein aggregates may induce reactive oxygen species (ROS) production and apoptosis. Gts1p also plays an important role in the regulation of heat and other stress responses under glucose-limited or -depleted conditions in either batch or continuous culture. Gts1p contains an N-terminal zinc finger motif similar to that of GATA-transcription factors, a ubiquitin-associated (UBA) domain and a C-terminal glutamine-rich strand. The zinc finger is responsible for the binding to the glycolytic enzyme glyceraldehydes-3-phosphate dehydrogenase (GAPDH) which is required for the maintenance of the metabolic oscillations of budding yeast. The polyglutamine sequence is indispensable for the pleiotropy and nuclear localization of Gts1p. It is essential for the transcriptional activation, whereas Gts1p lacks DNA binding activity
KYSRQLRFLKEMGFTNEDNNLEALSQANGNINRAIDILL
>gnl|CDD|270584 cd14401, UBA_HERC1, UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins. HERC1, also called HECT domain and RCC1-like domain-containing protein 1, or p532, or p619, is an ubiquitously expressed multi-domain protein involved in ubiquitin-dependent intracellular membrane trafficking through its interaction with vesicle coat proteins such as clathrin and ARF. Moreover, it has been identified as a tuberous sclerosis complex TSC2-interacting protein that may play a role in TSC-mTOR (mammalian target of rapamycin) pathway. In addition to a ubiquitin-association (UBA) domain, HERC1 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain. At this point, it may function as both E3 ubiquitin ligases and guanine nucleotide exchange factors (GEFs)
IAVPLLEMGFSLRHITRAMEATGTRGEADARNINVLATWMIEHP
>gnl|CDD|270585 cd14402, UBA_HERC2, UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins. HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. In addition to a ubiquitin-association (UBA) domain, HERC2 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain
PIVQQLMEMGFPRKNVEFALKSLSGSSGGLPTPEALVAWLLEHPD
>gnl|CDD|270586 cd14403, UBA_AID_AAPK1, UBA-like autoinhibitory domain (AID) found in vertebrate 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPKalpha-1). AMPKalpha-1, also called acetyl-CoA carboxylase kinase (ACACA kinase), hydroxymethylglutaryl-CoA reductase kinase (HMGCR kinase), or Tau-protein kinase PRKAA1, is one of the catalytic subunits of adenosine monophosphate (AMP)-activated protein kinase (AMPK). It has been implicated in a number of important cellular processes. For instance, it functions as a glucose sensor controlling CD8 T-cell memory, as well as a new kinase for RhoA and a new mediator of the vasoprotective effects of estrogen. It also plays a significant role in cervical malignant growth, in regulating oxidative stress and life span in erythrocytes, in modulating the antioxidant status of vascular endothelial cells, in limiting skeletal muscle overgrowth during hypertrophy through inhibition of the mammalian target of rapamycin (mTOR)-signaling pathway. AMPKalpha-1 has an N-terminal Ser/Thr kinase domain followed by an ubiquitin-associated (UBA)-like AID and a C-terminal AMPK regulatory domain. The Ser/Thr kinase domain contains a conserved Thr residue that must be phosphorylated for activity in the activation loop. The AID is responsible for AMPKalpha subunit autoinhibition. The C-terminal regulatory domain of the alpha1-subunit is essential for binding the beta1- and gamma1-subunits
SNMIDDEALKEVCEKCECTEEEVLSCLYSRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDS
>gnl|CDD|270587 cd14404, UBA_AID_AAPK2, UBA-like autoinhibitory domain (AID) found in vertebrate 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPKalpha-2). AMPKalpha-2, also called acetyl-CoA carboxylase kinase (ACACA kinase) or hydroxymethylglutaryl-CoA reductase kinase (HMGCR kinase), is one of the catalytic subunits of adenosine monophosphate (AMP)-activated protein kinase (AMPK). It shows a wide expression pattern and is highly expressed in skeletal muscle, heart, and liver. It may be involved in the regulation of glucose and lipid metabolism and protein synthesis in peripheral tissues, as well as in regulation of energy intake and body weight. AMPKalpha-2 has an N-terminal Ser/Thr kinase domain followed by an ubiquitin-associated (UBA)-like AID, and a C-terminal AMPK regulatory domain. The Ser/Thr kinase domain contains a conserved Thr residue that must be phosphorylated for activity in the activation loop. The AID is responsible for AMPKalpha subunit autoinhibition. The C-terminal regulatory domain is essential for binding the beta- and gamma-subunits
ATVIDDEAVREVCEKFECTESEVMNSLYSGDPQDQLAVAYHLIIDNRRIMNQASEFYLASSPPTG
>gnl|CDD|270588 cd14405, UBA_MARK1, UBA domain found in serine/threonine-protein kinase MARK1 and similar proteins. MARK1, also called MAP/microtubule affinity-regulating kinase 1 or PAR1 homolog c (Par-1c), is a kinase-regulating microtubule-dependent transport in axons and dendrites. It is involved in the specification of neuronal polarity, in axon-dendrite specification, and in the synaptic plasticity in adult neurons. It has been implicated in Alzheimer's disease, cancer, and autism
NDTKRIDIMVTMGFSRDEINEALVNQKYDEVMATYLLLGRK
>gnl|CDD|270589 cd14406, UBA_MARK2, UBA domain found in serine/threonine-protein kinase MARK2 and similar proteins. MARK2, also called ELKL motif kinase 1 (EMK-1), MAP/microtubule affinity-regulating kinase 2, PAR1 homolog, or PAR1 homolog b (Par-1b), is enriched in brain. It belongs to the AMPK family of Ser/Thr kinases. MARK2 has been implicated in regulating fertility, immune homeostasis, learning, and memory as well as adiposity, insulin hypersensitivity, and glucose metabolism. The activity of MARK2 is necessary for the outgrowth of cell processes, neurites, and dendritic spines. It is a TORC2 (also known as Crtc2) Ser-275 kinase that blocks TORC2-induced cAMP response element binding protein (CREB) activity. It regulates axon formation via phosphorylation of a kinesin-like motor protein GAKIN/KIF13B. It also acts as a positive regulator of Wnt-beta-catenin signaling
DYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGY
>gnl|CDD|270590 cd14407, UBA_MARK3_4, UBA domain found in MAP/microtubule affinity-regulating kinase MARK3, MARK4, and similar proteins. MARK3, also called C-TAK1, Cdc25C-associated protein kinase 1, ELKL motif kinase 2 (EMK-2), protein kinase STK10, Ser/Thr protein kinase PAR-1 (Par-1a), or serine/threonine-protein kinase p78, is a known regulator of KSR1, a molecular scaffold of the Raf/MEK/ERK MAP kinase cascade that regulates the intensity and duration of ERK activation. It binds plakophilin 2 (PKP2), phosphorylates human Cdc25C on serine 216, and promotes 14-3-3 protein binding and protein localization. It also interacts with microphthalmia-associated transcription factor, Mitf which is necessary for regulating genes involved in osteoclast differentiation. Moreover, MARK3 is involved in regulating localization and activity of class IIa histone deacetylases. The lack of MARK3 leads to reduced adiposity, resistance to hepatic steatosis, and defective gluconeogenesis. MARK4, also called MAP/microtubule affinity-regulating kinase-like 1 (MARKL1), or Par-1d, is a member of the AMP-activated protein kinase (AMPK)-related family of kinases. It plays a key role in energy metabolism and may act as a novel drug target for the treatment of obesity and type 2 diabetes. MARK4 also functions as the substrate of ubiquitin specific protease-9 (USP9X) and can be regulated by unusual Lys(29)/Lys(33)-linked polyubiquitin chains. Furthermore, MARK4 may play some role in hepatocellular carcinogenesis
DISDQKRIDIMVGMGYSQEEIQESLSKMKYDEITATYLLLGRK
>gnl|CDD|270591 cd14408, UBA_SIK1, UBA domain found in salt-inducible kinase 1 (SIK1). SIK1, also called serine/threonine-protein kinase SNF1-like kinase 1 (SNF1LK), is a serine/threonine kinase abundant in adrenal glands. It belongs to the AMP-activated protein kinases (AMPK) family involved in the regulation of metabolism during energy stress. SIK1 is required for myogenic differentiation. It is degraded by the proteasome in myoblasts which is regulated by cAMP signaling. Moreover, SIK1 acts as a class II histone deacetylase (HDAC) kinase, triggering the cytoplasmic export of the HDACs and activation of myocyte enhancer factor 2 (MEF2)-dependent transcription. It also regulates transcription through inhibitory phosphorylation of a family of cAMP responsive element binding protein (CREB) coactivators, called TORCs/CRTCs. In addition, SIK1 links LKB1 to p53-dependent anoikis and suppresses metastasis. It is also involved in a cell sodium-sensing network that regulates active sodium transport through a calcium-dependent process. SIK1 contains an N-terminal protein kinase catalytic domain followed by an ubiquitin-associated (UBA) domain and a putative PEST domain
NLGDYSEQVLGIMQTLGIDRQRTVESLQNSSYNHFAAIYYLLLERLKEYR
>gnl|CDD|270592 cd14409, UBA_SIK2, UBA domain found in salt-inducible kinase 2 (SIK2). SIK2, also called Qin-induced kinase or serine/threonine-protein kinase SNF1-like kinase 2 (SNF1LK2), is a serine/threonine kinase highly expressed in adipocytes. It belongs to the AMP-activated protein kinases (AMPK) family involved in the regulation of metabolism during energy stress. It plays an important role in the insulin-signaling pathway during adipocyte differentiation, as well as in autophagy progression. Moreover, SIK2 plays a critical role in neuronal survival and modulates cAMP responsive element binding protein (CREB)-mediated gene expression in response to hormones and nutrients. SIK2 acts as a critical determinant in autophagy progression. In addition, SIK2 localizes at the centrosome and functions as a centrosome kinase required for bipolar mitotic spindle formation. It is involved in the initiation of mitosis, and regulates the localization of the centrosome linker protein, C-Nap1, through S2392 phosphorylation. SIK2 contains an N-terminal protein kinase catalytic domain followed by an ubiquitin-associated (UBA) domain
NEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAIYYLLVERLKSHR
>gnl|CDD|270593 cd14410, UBA_SIK3, UBA domain found in salt-inducible kinase 3 (SIK3). SIK3, also called salt-inducible kinase 3 or serine/threonine-protein kinase QSK, is a serine/threonine kinase ubiquitously expressed. It belongs to the AMP-activated protein kinases (AMPK) family involved in the regulation of metabolism during energy stress. It acts as a novel energy regulator that modulates cholesterol and bile acid metabolism by coupling with retinoid metabolism. It also play an essential role in facilitating chondrocyte hypertrophy during skeletogenesis and growth plate maintenance. SIK3 contains an N-terminal protein kinase catalytic domain followed by an ubiquitin-associated (UBA) domain
NEQVLLAMAEMGLDRERTLQSLRADAYDHYSAIYSLLCDRLKRHK
>gnl|CDD|270594 cd14411, UBA_DCNL1, UBA-like domain found in DCN1-like protein 1 (DCNL1) and similar proteins. DCNL1 (defective in cullin neddylation protein 1-like protein 1), also called DCUN1 domain-containing protein 1, is encoded by squamous cell carcinoma-related oncogene SCCRO (DCUN1D1). It interacts with known cullin isoforms as well as ROC1, Ubc12 and CAND1, the components of the neddylation pathway. It plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. DCNL1 contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal cullin binding domain that binds to cullins and Rbx-1, components of an E3 ubiquitin ligase complex for neddylation
MNKLKSSQKDKVRQFMIFTQSSEKTAVSCLSQNDWKLDVATDNFFQNPELY
>gnl|CDD|270595 cd14412, UBA_DCNL2, UBA-like domain found in DCN1-like protein 2 (DCNL2) and similar proteins. DCNL2 (defective in cullin neddylation protein 1-like protein 2), also called DCUN1 domain-containing protein 2, is encoded by gene DCUN1D2. Although its biological function remains unclear, DCNL2 shows high sequence similarity with DCNL1, a protein that plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. At this point, DCNL2 may also contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Like DCNL1, DCNL2 contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal cullin binding domain that is responsible for the binding to cullins and Rbx-1, components of an E3 ubiquitin ligase complex for neddylation
HKLKSSQKDKVRQFMAFTQAGERTAIYCLTQNEWKLEVATDNYFQNP
>gnl|CDD|270596 cd14413, UBA_FAF1, UBA-like domain found in FAS-associated factor 1 (FAF1) and similar proteins. FAF1, also called UBX domain-containing protein 12 or UBX domain-containing protein 3A, is a multi-functional Fas associating protein that contains an N-terminal ubiquitin-associated (UBA)-like domain, UAS and ubiquitin-like (UBX) domains, p150 subunit of a chromatin assembly factor like domain (CAF) and a novel nuclear localization signal (NLS). FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF1 is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kappaB (NF-kappaB) by interfering with the nuclear translocation of the p65 subunit. Although the precise role of FAF1 in the ubiquitination pathway remains unclear, FAF1 interacts with valosin-containing protein (VCP) which is involved in the ubiquitin-proteosome pathway
FQACTGIEDIDECIMLLEQNNWNLVAAVNAVIP
>gnl|CDD|270597 cd14414, UBA_FAF2, UBA-like TAP-C domain found in FAS-associated factor 2 (FAF2) and similar proteins. FAF2, also called protein ETEA, UBX domain-containing protein 3B, or UBX domain-containing protein 8, is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. FAF2 shows homology to Fas-associated factor 1 (FAF1). Both of them contain N-terminal ubiquitin-associated (UBA)-like domain, UAS and ubiquitin-like (UBX) domains. Compared to FAF1, however, FAF2 lacks the nuclear targeting domain. The function of FAF2 remains unclear. A yeast two-hybrid assay showed that it can interact with Fas. Because of its homology to FAF1, it is postulated that FAF2 could be involved in modulating Fas-mediated apoptosis of T-cells and eosinophils of atopic dermatitis patients, making them more resistant to apoptosis
EKLLQFQDLTGIEDMDQCREVLERHNWDIEAAVQDRLN
>gnl|CDD|270598 cd14415, UBA_NACA_NACP1, UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and putative NACA-like protein (NACP1). NACA, also called NAC-alpha or alpha-NAC, together with BTF3, also called Beta-NAC, form the nascent polypeptide-associated complex (NAC) which is a cytosolic protein chaperone that contacts the nascent polypeptide chains as they emerge from the ribosome. Besides, NACA has a high affinity for nucleic acids and exists as part of several protein complexes playing a role in proliferation, apoptosis, or degradation. It is a cytokine-modulated specific transcript in the human TF-1 erythroleukemic cell line. It also acts as a transcriptional co-activator in osteoblasts by binding to phosphorylated c-Jun, a member of the activator-protein-1 (AP-1) family. Moreover, NACA binds to and regulates the adaptor protein Fas-associated death domain (FADD). In addition, NACA functions as a novel factor participating in the positive regulation of human erythroid-cell differentiation. Both NACA and BTF3 harbor an NAC domain that mediates the dimerization of the two subunits. By contrast, NACA has an extra ubiquitin-associated (UBA) domain in the C-terminus. In addition to NACA, the family includes NACP1, also called Alpha-NAC pseudogene 1 or NAC-alpha pseudogene 1. The biological function of NACP1 remains unclear
EEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELT
>gnl|CDD|270599 cd14416, UBA_NACAD, UBA-like domain found in nascent polypeptide-associated complex subunit alpha domain-containing protein 1 (NACAD). The subfamily includes a group of uncharacterized proteins mainly found in vertebrates. Their biological function remains unknown, but they show high sequence similarity to the nascent polypeptide-associated complex (NAC) subunit alpha (NACA) that exists as part of several protein complexes playing a role in proliferation, apoptosis, or degradation. Like NACA, NACAD contains an NAC domain and a C-terminal ubiquitin-associated (UBA) domain
DETGLEVRDIELVMAQANVSRAKAVRALRHNNNDIVNAIMELTM
>gnl|CDD|270600 cd14417, CUE_DMA_DMRTA1, CUE-like DMA domain found in doublesex- and mab-3-related transcription factor A1 (DMRTA1) and similar proteins. DMRTA1 is encoded by gene DMRT1, a vertebrate equivalent of the Drosophila melanogaster master sex regulator gene, doublesex. In D. melanogaster, doublesex controls the terminal switch of the pathway leading to sex fate choice. DMRT1 may function as regulator of sex differentiation in vertebrate. Especially, it is required for testis differentiation, but is not involved in the gonadal sex fate choice
RHRDPLDILTRVFPNHKRNALESILRRCRGDVVQAIEQLL
>gnl|CDD|270601 cd14418, CUE_DMA_DMRTA2, CUE-like DMA domain found in doublesex- and mab-3-related transcription factor A2 (DMRTA2). DMRTA2, also called Doublesex- and mab-3-related transcription factor 5 (DMRT5), is encoded by gene DMRT2. In the zebrafish, DMRT2 is involved in somite development. DMRTA2 may act as an activator of cyclin-dependent kinase inhibitor 2C (cdkn2c) during spermatogenesis. It may also play significant roles in embryonic neurogenesis
RQRTPIDILTRVFPGHKRSVLELVLQGCGGDVVQAIEQILNN
>gnl|CDD|270602 cd14419, CUE_DMA_DMRTA3, CUE-like DMA domain found in doublesex- and mab-3-related transcription factor 3 (DMRTA3). DMRTA3 is encoded by tumor suppressor gene DMRT3 which serves as a novel potential target for homozygous deletion in squamous cell carcinoma of the lung
ANRPPLEVLKKIFPSHKPTVLELILKGCGGDLVSAIEVLLSSR
>gnl|CDD|270603 cd14420, CUE_AUP1, CUE domain found in ancient ubiquitous protein 1 (AUP1) and similar proteins. AUP1 is a component of the HRD1-SEL1L endoplasmic reticulum (ER) quality control complex and is essential for US11-mediated dislocation of class I MHC heavy chains. It also binds to the membrane-proximal KVGFFKR motif of the cytoplasmic tail of the integrin alphaCTs that plays a crucial role in the inside-out signaling of alpha(IIb)beta(3). AUP1 is found in both the ER and in lipid droplets. It contains two conserved cytoplasmic domains, an acyltransferase domain, a CUE domain and an E2 ubiquitin conjugase G2 (Ube2g2)-binding domain (G2BR). The acyltransferase domain transfers fatty acids onto phospholipids and CUE domain participates in ubiquitin binding or in recruitment of ubiquitin-conjugating enzymes to the site of dislocation
RLARMAQQVKEVLPHVPLHVIRRDLEKTRNVDTTITNILEGRVKF
>gnl|CDD|270604 cd14421, CUE_AMFR, CUE domain found in autocrine motility factor receptor (AMFR) and similar proteins. AMFR is an internalizing cell surface glycoprotein that is localized in both plasma membrane caveolae and the endoplasmic reticulum (ER), and involves in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. It is also called ER-protein gp78 that has been identified as a RING finger-dependent ubiquitin protein ligase (E3) implicated in degradation from the ER. AMFR contains an N-terminal RING-finger domain and a C-terminal CUE domain
DAMAHQVQEMFPQVPLSVILADLRLTRSVEVTIENILEGRL
>gnl|CDD|270605 cd14422, CUE_RIN3_plant, CUE domain found in plant E3 ubiquitin protein ligases RIN2, RIN3 and similar proteins. RIN2 and RIN3 are two closely related RPM1-interacting proteins conserved in higher eukaryotes. They are orthologs of the mammalian autocrine motility factor receptor (AMFR), a cytokine receptor localized in both plasma membrane caveolae and the endoplasmic reticulum (ER). RIN2 and RIN3 have been identified as membrane-bound RING-finger type ubiquitin ligases with six apparent transmembrane domains, a RING-finger domain and a CUE domain. They act as positive regulators of RPM1- and RPS2-dependent hypersensitive response (HR)
ILAMVGMVREVLPHVPDEIIFQDLQRTNSVTATVNNLL
>gnl|CDD|270606 cd14423, CUE_UBR5, CUE domain found in E3 ubiquitin-protein ligase UBR5 and similar proteins. UBR5, also called E3 ubiquitin-protein ligase, HECT domain-containing 1, hyperplastic discs protein homolog (HYD), progestin-induced protein, EDD, or Rat100, belongs to the E3 protein family of HECT (homologous to E6-AP C-terminus) ligases. It is frequently overexpressed in breast and ovarian cancer, suggesting a role in cancer development. UBR5 is involved in DNA-damage signaling. It can ubiquitinate DNA topoisomerase II-binding protein 1 (TopBP1) in the presence of the E2 enzyme UBCH4. It also activates the DNA-damage checkpoint kinase CHK2. Moreover, UBR5 interacts with the calcium and integrin-binding protein (CIB) in a DNA-damage-dependent manner. It functions as the substrate of the extracellular signal-regulated kinases (ERKs) 1 and 2. It also acts as a ubiquitin ligase that controls the levels of poly(A)-binding protein-interacting protein 2. In addition, UBR5 ubiquitinates and up-regulates beta-catenin, regulates transcription, and activates smooth-muscle differentiation through its ability to stabilize myocardin. UBR5 contains an N-terminal CUE domain, a zinc-finger-like domain termed the ubiquitin-recognin (UBR) box, a MLLE (mademoiselle) domain, and a C-terminal catalytic HECT domain
VVPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSRDDED
>gnl|CDD|270607 cd14424, CUE_Cue1p_like, CUE domain found in yeast ubiquitin-binding protein CUE1 (Cue1p), CUE4 (Cue4p) and similar proteins. Cue1p, also called coupling of ubiquitin conjugation to ER degradation protein 1 or kinetochore-defect suppressor 4, is encoded by the open reading frame (ORF) YMR264W in yeast. It is an N-terminally membrane-anchored endoplasmic reticulum (ER) protein essential for the activity of the two major yeast RING finger ubiquitin ligases (E3s) implicated in ER-associated degradation (ERAD). It interacts with the ERAD ubiquitin-conjugating enzyme (E2) Ubc7p in vivo, stimulates Ubc7p E2 activity, and further activates ER-associated protein degradation. Cue1p contains a CUE domain which binds ubiquitin much more weakly than those of other CUE domain containing proteins. It also has an Ubc7p binding-domain at the C-terminal region which is required for Ubc7p-dependent ubiquitylation and for degradation of substrates in the ER. This family also includes Cue4p, also called coupling of ubiquitin conjugation to ER degradation protein 4. It is encoded by the open reading frame (ORF) YML101C in yeast. Cue4p contains a CUE domain which shows high level of similarity with that of Cue1p
PAMIESVQTMFPQLSVAQIRYDLLRTGSVEATVERIL
>gnl|CDD|270608 cd14425, UBA1_HR23A, UBA1 domain of UV excision repair protein RAD23 homolog A (HR23A) found in vertebrates. HR23A, also called Rad23A, is a DNA repair protein that binds to 19S subunit of the 26S proteasome and shuttles ubiquitinated proteins to the proteasome for degradation which is required for efficient nucleotide excision repair (NER), a primary mechanism for removing UV-induced DNA lesions. HR23A also plays a critical role in the interaction of HIV-1 viral protein R (Vpr) with proteasome, especially facilitating Vpr to promote protein poly-ubiquitination. HR23A contains an N-terminal ubiquitin-like (UBL) domain that binds proteasomes and two C-terminal ubiquitin-associated (UBA) domains that bind ubiquitin or multi-ubiquitinated substrates. In addition, it has a XPC protein-binding domain that might be necessary for its efficient NER function. This model corresponds to the UBA1 domain
EYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTG
>gnl|CDD|270609 cd14426, UBA1_HR23B, UBA1 domain of UV excision repair protein RAD23 homolog B (HR23B) found in vertebrates. HR23B, also called xeroderma pigmentosum group C (XPC) repair-complementing complex 58 kDa protein (p58), is tightly complexed with XPC protein to form the XPC-HR23B complex. Although it displays a high affinity for both single- and double-stranded DNA, the XPC-HR23B complex functions as a global genome repair (GGR)-specific repair factor that is specifically involved in global genome but not transcription-coupled nucleotide excision repair (NER). HR23B also interacts specifically with S5a subunit of the human 26 S proteasome, and plays an important role in shuttling ubiquitinated cargo proteins to the proteasome. HR23B contains an N-terminal ubiquitin-like (UBL) domain that binds proteasomes and two C-terminal ubiquitin-associated (UBA) domains that bind ubiquitin or multi-ubiquitinated substrates. In addition, it has a XPC protein-binding domain that might be necessary for its efficient NER function. This model corresponds to the UBA1 domain
VTGQSYENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLMGIP
>gnl|CDD|270610 cd14427, UBA2_HR23A, UBA2 domain of UV excision repair protein RAD23 homolog A (HR23A) found in vertebrates. HR23A, also called Rad23A, is a DNA repair protein that binds to 19S subunit of the 26S proteasome and shuttles ubiquitinated proteins to the proteasome for degradation which is required for efficient nucleotide excision repair (NER), a primary mechanism for removing UV-induced DNA lesions. HR23A also plays a critical role in the interaction of HIV-1 viral protein R (Vpr) with proteasome, especially facilitating Vpr to promote protein poly-ubiquitination. HR23A contains an N-terminal ubiquitin-like (UBL) domain that binds proteasomes and two C-terminal ubiquitin-associated (UBA) domains that bind ubiquitin or multi-ubiquitinated substrates. In addition, it has a XPC protein-binding domain that might be necessary for its efficient NER function. This model corresponds to the UBA2 domain
QEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQN
>gnl|CDD|270611 cd14428, UBA2_HR23B, UBA2 domain of UV excision repair protein RAD23 homolog B (HR23B) found in vertebrates. HR23B, also called xeroderma pigmentosum group C (XPC) repair-complementing complex 58 kDa protein (p58), is tightly complexed with XPC protein to form the XPC-HR23B complex. Although it displays a high affinity for both single- and double-stranded DNA, the XPC-HR23B complex functions as a global genome repair (GGR)-specific repair factor that is specifically involved in global genome but not transcription-coupled nucleotide excision repair (NER). HR23B also interacts specifically with S5a subunit of the human 26 S proteasome, and plays an important role in shuttling ubiquitinated cargo proteins to the proteasome. HR23B contains an N-terminal ubiquitin-like (UBL) domain that binds proteasomes and two C-terminal ubiquitin-associated (UBA) domains that bind ubiquitin or multi-ubiquitinated substrates. In addition, it has a XPC protein-binding domain that might be necessary for its efficient NER function. This model corresponds to the UBA2 domain
QEKEAIERLKALGFPEGLVIQAYFACEKNENLAANFLLQQNFDDD
>gnl|CDD|259859 cd14435, SPO1_TF1_like, Bacteriophage SPO1-encoded TF1 binds and bends DNA. This group contains proteins related to bacillus phage SPO1-encoded transcription factor 1 (TF1), a type II DNA-binding protein related to the DNA sequence specific (IHF) and non-specific (HU) domains. Type II DNA-binding proteins bind and bend DNA as dimers. Like IHF, TF1 binds DNA specifically and bends DNA sharply. Bacteriophage SPO1-encoded TF1 recognizes SPO1 phage DNA containing 5-(hydroxymethyl)-2'-deoxyuridine as opposed to thymine, Related family members includes integration host factor (IHF) and HU, also called type II DNA-binding proteins (DNABII), which are small dimeric proteins that specifically bind the DNA minor groove, inducing large bends in the DNA and serving as architectural factors in a variety of cellular processes such as recombination, initiation of replication/transcription and gene regulation. IHF binds DNA in a sequence specific manner while HU displays little or no sequence preference. IHF homologs are usually heterodimers, while HU homologs are typically homodimers (except HU heterodimers from E. coli and other enterobacteria). HU is highly basic and contributes to chromosomal compaction and maintenance of negative supercoiling, thus often referred to as histone-like protein. IHF is an essential cofactor in phage lambda site-specific recombination, having an architectural role during assembly of specialized nucleoprotein structures (snups)
NKTELVAAIAQKAGLTQAQVSKVLDAFEDVLTEAVAKGEKVTLPGLLTFERVERAARTGRNPQTGEAIQI
PAGYGVKFSAGSKLKKA
>gnl|CDD|271226 cd14436, LepB, Legionella Rab1-specific GAP LepB. LepB of Legionella, a human pathogen, is a specific RabGAP for Rab1, a member of the largest subfamily of small GTPases. RabGTPases play a role in the control of vesicular trafficking and are switched off by GTPase-activating enzymes (GAPs) that stimulate the intrinsic GTP hydrolysis activity. Legionella LepB is unrelated to the TBC family of human Rab1 RabGAPs
FSELINIWANILSLSDERSSFDFNSIDFAKLAQKFNFYVDSLARQAEKINSWSHDRGQTMNILAKDMGLS
GKALHGHAFVGQYKESSVLRRLFTVDPATLGTLRFKPFESPSTKYCVSHPDSYWQKIQTLLTAGFNIIVT
LRILQDTQNSVMKDEAMHELLDALKKALHDFSLANEAVEYFLKNSPNDPVEVFESVFFYEIDENALCKMS
GSQLATICLEELNAPNPSVLIGRILKNPNLWQRMNWALTETAFERIDDPEKKANKIMKLQQL
>gnl|CDD|271227 cd14437, nt01cx_1156_like, Uncharacterized proteins conserved in Clostridia. Some members of this uncharacterized protein family have been annotated as putative lipoproteins. The structure resembles that of a partial beta-propeller (3 out of 6 blades), suggesting that family members might form dimers
SQEQRANYNANKKKVKTANVNPPSEQKNGEVKKETNKSEKTSFIKFIKKELPDKTLQGFNTVWKSSPNKK
YSACIEGKGSEALEEGIGKIYIKNSKNNSWWELQLNQEGQKTSPKYIEWFDDNNLLVIIGSAHGTVSKGG
NLYKLNVATGEAEILYPAKDKKQQVVSAFKQGDKLNLKINVYDDDGYNKSHKEEWTIPS
>gnl|CDD|271228 cd14438, Hip_N, N-terminal dimerization domain of the Hsp70-interacting protein (Hip) and similar proteins. The Hsc70/Hsp70-interacting protein (Hip, also p48 or suppressor of tumorigenicity ST13) functions as a regulator of the cyclic action of Hsp70. Hip forms homodimers, and this model characterizes the N-terminal dimerization domain, which may not be directly involved in its regulatory function. A central domain of Hip that contains TPR repeats binds the ATPase domain of Hsp70 and slows the release of ADP
PEKLKELKAFVELCKQNPSILHTPELSFFKEYLESLGAKIP
>gnl|CDD|270205 cd14439, AlgX_N_like, N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins. The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. This wider family includes AlgX, AlgJ, AlgV, and a number of uncharacterized families, some of which may have been mis-annotated in sequence databases
GNLRTVLASLLADQNSLRDFWRAQSLLLLAGNRGSGGVLIGKDGWLFLKPDLYDARTDLDAPAENVEAIA
EFRKQLDKRGIRLLVLPVPAKAKIYPERLPAYVTPPDAVNPNYRAFLSRLRKAGVDVLDLRPVLAQAKEG
EQLFYRTDHHWTPLGARLAAQQVAEALKKKPGYEVPPEKYDTSKVEESRSRLGDLAKRLGLDELLKEDLI
YLERVVLNAGSPQSALFSDSGAPKVVLLGDSFSNVFILELLIKDGFAQHLAPALGRPVDEIAKNGGGSGS
RRDYLAREEFKGPPKKVVIWEFAEREAADNAWRQVD
>gnl|CDD|270206 cd14440, AlgX_N_like_3, Uncharacterized proteins similar to putative alginate O-acetyltransferase. The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this uncharacterized protein family resemble AlgX_N
FSDHFGFRDQLISADSALLYSLLGESSNPRVIIGKDGWLFLGEDYMLEDYCGRDPLSEEDLRRWVALLER
RRDWLAARGIPFVVVVAPNKHTIYPEHLPSWYPGKSPTRLDQLLALLLSAAGVGVVDLRPALLEAKATGA
PVYYKTDTHWNFYGAYVAYRAIAEALGPGVPALWPLASVEYDESTVGGDLANMLGLPEALEEDRLPDESK
PPLQARRIDDDTATLPFPLDKPKLTTNSPAGNNKSALVFRDSFGEALSPYLAETFSRVVYLWSPEIDQAL
IEAEKPDVVVLEIVERVLRQLPEAAPPLEASPNGR
>gnl|CDD|270207 cd14441, AlgX_N, N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX. The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. This N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains
CDLCPAAADPSSYDCLETKGFFTLVEGKDGWLFRSNADLRSQFGLSPETLAALAALSDALKARGTELVLV
PQPTRGLVHAEKLPPAAYAYGFDAAVARQSYRATLARLRDAGILVPDLLPLMDTKAGGEPFFFKRDHHWT
PEGARASAKAVAETIRGLPAYADLPKQAFETEPGGLLPKSGSLGKALQAICGQKYPTEYVDRYETVPVSD
GASDLFGDGPDPEIALVGTSFSARPNYNFAGFLEQYLGLDVLNYSISGGGPTGSLLGYLLSDDFQAKPPK
LLIWELPYYYDLNSVSFYRQLIAAVGGGCS
>gnl|CDD|270208 cd14442, AlgJ_like, putative alginate O-acetyltranferases AlgJ, AlgV, and similar proteins. The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this family have been annotated as AlgJ or AlgV, and they closely resemble AlgX in sequence and function, although they lack the C-terminal carbohydrate binding domain of AlgX
KLARAFEAHYDKEFPLRDPATNLWAAAQYLLFGEGRPGVVVGKDGWLFTDEEFKPAADLEANLEDNLALI
AEVRRALARHGVRLVLAPVPAKARLYPEHLGGARPPAAMRSLYDRFRAALAAAGITAPDLLPALLAAKAG
GPVFLRTDTHWTPAGAEVAARALAAQVRELGGLDPELQEAATEAIPPEPHKGDLLNFLPLDPLFPQLGPP
PEEPRYRTTSQEGSAGADDLFGDSQIPVALVGTSYSANERWNFAGALRQALGADLLNVAEEGRGPFLPML
KFLQSEALRDSPPQLVIWEFPERYLPMRPDLSEFDAPAIAQ
>gnl|CDD|270209 cd14443, AlgX_N_like_2, Uncharacterized proteins similar to putative alginate O-acetyltranferase. The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Some members of this uncharacterized family, which resembles AlgX_N, have been annotated as twin-arginine translocation signal, although they share little or no similarity with experimentally characterized proteins that bear the same name
RTRRRLLLALAAAGLAASPAAAQAASSAVIEGKDGWLFPGWESLTDVDTPGIDRSVALIREARDALAARG
IKLVVLVLPDKARFYADKLPDGKAMSPAVRKRYAQVLDKLRQAGVDTVDDEAVLKRVKTGGQTVFYRADQ
HWTAAAAEATADATADVIRQNVPLLGGPGGGGALGDWINERRYGDLAELFLTPEQRKAVGREIYTVRRQA
DEQGLLDDAPAPVHVTGNSMVQPYLGFPQKLSNVLDRPVSLTWKPGNVGPWATLLEYLESPAFKQQKPQV
LVWQFNEPQFHQGPDARGQWDNASLMSAAQWRA
>gnl|CDD|270210 cd14444, AlgX_N_like_1, Uncharacterized proteins similar to putative alginate O-acetyltranferase. The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such those as by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this uncharacterized family similar to AlgX_N have been annotated as cell division proteins FtsQ, although they share little or no similarity with experimentally characterized members of the FtsQ family
LPLAPALAALERGLRWRLLGDLGPQVRQGCPGWLFLADELRPNPGAEANADARARLVRRLARQLAARGIA
LLVVVVPDKSRIEADHLCGLPRPAVLQARLDAWQQALQAAGVAALDLAPALQPLGADAYLRTDTHWNEAG
AAAAAAAVAAAVLPLGGGAGPQRFFTESAGPPAPRPGDLVRLAGLDWLPDGWRPAPESDRAVPEAAEPSR
SGGLLDDAPLPEVALIGSSFSRNSNFAGFLQQALGAEVGNFAKDGGGFSGAALAYFDSRAFWPTPPKLVI
WEIPERDLQTPLTDAERA
>gnl|CDD|271220 cd14445, RILP-like, Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2). This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va
GAESALDKSPSELTVVDVYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIE
ELRLEVDRLELEKRERAQK
>gnl|CDD|271219 cd14446, bt3222_like, Uncharacterized proteins similar to Bacteriodes thetaiotaomicron bt3222. This family appears to be specific to Bacteroidetes; the two-domain protein forms a homodimer
SRVSVVNENALSFKSEEVYQETLRELSSMSEEERLAYFSGLGFKSFTSLYDEADEELEKIGDAADSSEFR
EKYEEYKEKYSDVFYFNEYDKDDLSPYLPVSDETLAYLVNINGYVVIGNEVKNIKDIKDYEELDELGSSL
SAEALPDEAGVSGYKETSDNTIKNKKYDKKMTLGRIVNGNSVKVEFNAQKKGWGGWKKYPKTTYYAKLGL
ASGPVNGFGNVGSPKGGKGVSILNLPIEPYGKVYAAETYGTITGGNDTVGFKNVNL
>gnl|CDD|269894 cd14447, SPX, Domain found in Syg1, Pho81, XPR1, and related proteins. This region has been named the SPX domain after (Syg1, Pho81 and XPR1). This domain is found at the amino terminus of a variety of proteins. In the yeast protein Syg1, the N-terminus directly binds to the G-protein beta subunit and inhibits transduction of the mating pheromone signal. Similarly, the N-terminus of the human XPR1 protein binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that members of this family are involved in G-protein associated signal transduction. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors Pho81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. The SPX domain of S. cerevisiae low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2. NUC-2 contains several ankyrin repeats. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with xenotropic and polytropic murine leukaemia viruses (MLV). Infection by these retroviruses can inhibit XPR1-mediated cAMP signaling and result in cell toxicity and death. The similarity between Syg1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, S. cerevisiae, and many other diverse organisms
KFGKRLREEAVPEWRDKYVDYKALKKLIKNLVASADEASNSSEALELSESGGEEFESEFFEALDAELEKV
NEFYQELLEELQELLKRLEALEPDLPALRGSLKEELEDLRKELVESYSELEELERFVELNYTAFRKILKK
YDK
>gnl|CDD|259990 cd14448, CuRO_2_BOD_CotA_like, Cupredoxin domain 2 of Bilirubin oxidase (BOD), the bacterial endospore coat component CotA, and similar proteins. Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and is required for spore resistance against hydrogen peroxide and UV light. Also included in this subfamily are phenoxazinone synthase (PHS), which catalyzes the oxidative coupling of substituted o-aminophenols to produce phenoxazinones, and FtsP (also named SufI), which is a component of the cell division apparatus. These proteins are laccase-like multicopper oxidases (MCOs) that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper
DLPLVITDRQFNADGTLYYPSPPTNMEWVPGFFGDVILVNGKIWPYLEVEPGWYRLRLLNASNARHYNLA
LSDGLPFHVIGSDGGLLEAPVKVKELVLAPAERIDVVVDFSQYAGEEVELVNLGGASMAILPTDYDTDVM
QFRV
>gnl|CDD|259991 cd14449, CuRO_1_2DMCO_NIR_like_2, The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase. The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers, and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities. This subfamily has lost the type 1 (T1) copper binding site in domain 1 that is present in other two-domain laccases
ARHLEMYAEKLTDDAWGYGLKGGVATVPGPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGM
NASIVAPGDTRIYTWRTHGGYRRADGSWAEGTAGYWHYHDHVFGTEHGTEGLSRGLYGALIVRRV
>gnl|CDD|259992 cd14450, CuRO_3_FV_like, The third cupredoxin domain of coagulation factor V and similar proteins. Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 3 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom
KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKEEG
ILGPVIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNI
LETDEPTARDPRCLTRMYHSAVDITRDIASGLIGPLLICKS
>gnl|CDD|259993 cd14451, CuRO_5_FV_like, The fifth cupredoxin domain of coagulation factor V and similar proteins. Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 5 of unprocessed Factor V or the first cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom
KRRYYIAAEEEEWDYAGYGKSRLDKTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAE
VDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENN
GSDCRTWAYYSAVNPEKDIHSGLIGPLLICRKG
>gnl|CDD|259994 cd14452, CuRO_1_FVIII_like, The first cupredoxin domain of coagulation factor VIII and similar proteins. Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 1 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins
RRYYIAAVEIGWDYIHSDLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAE
VGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGS
DPECLTYSYSSQVDPVKDVNSGLIGALLVCRMG
>gnl|CDD|259995 cd14453, CuRO_2_FV_like, The second cupredoxin domain of coagulation factor V and similar proteins. Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 2 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom
YKEYVLMFGVFDENKSWYKQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNG
QVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI
>gnl|CDD|259996 cd14454, CuRO_4_FV_like, The fourth cupredoxin domain of coagulation factor V and similar proteins. Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 4 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom
DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQW
HISSVGTQDEIITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFT
DVIC
>gnl|CDD|259997 cd14455, CuRO_6_FV_like, The sixth cupredoxin domain of coagulation factor V and similar proteins. Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 6 of unprocessed Factor V or the second cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom
RREFVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLIN
MGGPKDLHVVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV
>gnl|CDD|271218 cd14456, Menin, Scaffolding protein menin encoded by the MEN1 gene. MEN1 is the gene responsible for multiple endocrine neoplasia type 1, and it has been characterized as a tumor suppressor gene that encodes a protein called menin. Menin is mostly found in the nucleus and can regulate gene expression in a positive and in a negative way, and it has been shown to interact with transcription activators, transcription repressors, cell signaling proteins, and various other proteins. It plays major roles in DNA repair, the regulation of the cell cycle, and chromatin remodeling
FRDDDKKLFPLRSISDVVSLFRAQLESPGEPDLALLSIVLGYIENSLTVNRASPTNVDALDPSGGEPPFP
VVELEEIEALYEKFMALIKGSVDLSLYAEGDDYATRELVKKVSDVIWNSLSRSYYKDRAHLQSLYSFLTG
NKLDCFGVAFAVVAACQVLGYSDVHLALSEDHAWVVFGPDGEETAEVTWHGKGNEDKRGQSISAGVTERS
WLYLNGCPVVCTRGMEVAALVSAINPSIDATTDSLELAQLQQKLLWLLYDAGHLKRYPMALGNLGDLEEI
SPTPGRPPCLKLFNEAISSARKYYRNHHVYPYTYLGGYYYRHGKYREALRSWAEAADVIRKYNYSREDEE
IYKEFLEIANELIPQLLKEESSGSSADQPRSILQDPECFANLLRFYDGICKWEEGSPTPVLHIGWAKPLV
QSLSKFDADVRAQVVIK
>gnl|CDD|271217 cd14458, DP_DD, Dimerization domain of DP. DP functions as a binding partner for E2F transcription factors. DP and E2F form heterodimers and play important roles in regulating genes involved in DNA synthesis, cell cycle progression, proliferation and apoptosis. The transcriptional activity of E2F is inhibited by the retinoblastoma protein (Rb) which binds to the E2F-DP heterodimer, blocks the transactivation domain, and negatively regulates the G1-S transition. DP is distantly related to E2F. In humans, there are at least six closely related E2F and two DP family members, all containing a DNA binding domain, a coiled-coil (CC) region, and a marked-box domain. E2F1 to E2F5 also contain a C-terminal transactivation domain
SLEECEQLEEEKERRRERIEKKKAQLQELILQQIALKNLVERNREREAQGEAPAPNSKIQLPFIIVNTSK
DAVIDCEISEDRSEYLFNFNSPFEIHDDIEILKRM
>gnl|CDD|270615 cd14472, mltA_B_like, Domain B insert of mltA_like lytic transglycosylases. Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic, cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct
IQARHTRQGEFQYPIYRIPPKRGRLSSRAEIYAGALSDKYILAYSNSLVDNFIADVQGSGYIDFGDGSPL
NFFSYAGKNGHAYRSIGKVLIDRGEVKKEDISSQAIRHWGETHSEAEVRELLEQNPSFVFFKPQ
>gnl|CDD|271216 cd14473, FERM_B-lobe, FERM domain B-lobe. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites
TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLKQRKPEEWE
KRIVELHKKLRGLSPAEAKLKYLKIARKL
>gnl|CDD|269895 cd14474, SPX_YDR089W, SPX domain of the yeast protein YDR089W and related proteins. This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The uncharacterized yeast protein YDR089W has not been shown to be involved in phosphate homeostasis, in contrast to most of the other SPX-domain containing proteins
KFGEQLLQRSVPEWKLYNIDYNELKHLIKEHTTRDQGTAIAIPSALEKFEDSLYNEFCEQFDRVNLFVSS
KADEISRRLEHLESSILRLLERSASNSGSRRRQKRRLAKIEQELLRCGEELQKLSRFIIAQKIAFRKILK
KYKK
>gnl|CDD|269896 cd14475, SPX_SYG1_like, SPX domain of the yeast plasma protein Syg1 and related proteins. This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. In the yeast protein Syg1, the N-terminus binds directly to the G-protein beta subunit and inhibits transduction of the mating pheromone signal, and it co-occurs with a C-terminal domain from the EXS family
KFAKYLEENLVPEWRKKYLDYKGGKKKIKAREFFEFLDSELDKVESFYKEKEDEARERLDLLRDQLHELR
DHRIQEADDGRRDYSRRPEQNAHDPVSYRSARRKLKKALQEYYRGLELLKSYRLLNRTAFRKINKKFDK
>gnl|CDD|269897 cd14476, SPX_PHO1_like, SPX domain of the plant protein PHOSPHATE1 (PHO1). This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The PHO1 gene family conserved in plants is involved in a variety of processes, most notably the transport of inorganic phosphate from the root to the shoot of the plant and mediating the response to low levels of inorganic phosphate. More recently it has become evident that PHO1 gene families have diverged in various plants and may play roles in stress response as well as the stomatal response to abscisic acid
KFGKEFESQMVPEWQEAYVDYKQLKKDLKRIQKFRDEYETTFLEAAEEGGEYELVFFRRLDDELNKVNKF
YRSKVEEVLKEAAALNKQMDALIAFRVKVENPQFYRKLRLLKSYSFLNMLAFSKILKKYDKVTSRNASK
>gnl|CDD|269898 cd14477, SPX_XPR1_like, SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins. This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The N-terminus of the human XPR1 protein (xenotropic and polytropic retrovirus receptor 1) binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that all members of this family are involved in G-protein associated signal transduction. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with xenotropic and polytropic murine leukaemia viruses (MLV). Infection by these retroviruses can inhibit XPR1-mediated cAMP signaling and result in cell toxicity and death. Similarity between Syg1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, and Saccharomyces cerevisiae, and many other diverse organisms
KFGEHLSAHITPEWRKQYINYEELKAMLYAAVEQAPSPEVTDEDVVKRYFAKFEEEFFQECDKELAKVNT
FFSEKLAEAQRKFATLKNELLSSLEAQGESGAASSLIRRVFALLRKERVKPRKLRDLKLAFSEFYLSLIL
LQNYQNLNFTGFRKILKKHDK
>gnl|CDD|269899 cd14478, SPX_PHO87_PHO90_like, SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins. This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The SPX domain of the Saccharomyces cerevisiae membrane-localized low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2. Pho91 is involved in the export of inorganic phosphate from the vacuole to the cytosol. While both, Pho87 and Pho90, transport phosphate into the cell, only Pho87 appears to also function as a sensor for high extracellular phosphate concentrations
KFSHSLQFNAVPEWSDHYIAYSNLKKLIYQLEKDQLQLQNGGDDEEEEESSLLLLSTDEDPDDVFVRALD
KELEKIDSFYKEKEAELYAEVDELLKDVEEFEEENYLYDSRISLKKRIINLYVSLSELKSYIELNRTGFS
KILKKYDK
>gnl|CDD|269900 cd14479, SPX-MFS_plant, SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain. This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The SPX domain is found at the amino terminus of a variety of proteins. This family, mostly found in plants, contains a C-terminal MFS domain (major facilitator superfamily), suggesting a function as a secondary transporter. The function of this N-terminal region is unclear, although it might be involved in regulating transport
VNFGKKLKEDQIPEWEGYYINYKLLKKKVKQYVQQTQDGGQDRRDVLKDFSKLLDDQIEKIVLFLLEQQG
LLASRLEKLGEQREALQEQPDLSQISELREAYRAVGLDLLKLLKFVELNATGLRKILKKFDKRFGYRFTD
>gnl|CDD|269901 cd14480, SPX_VTC2_like, SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins. This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. Vtc2 is part of the Saccharomyces cerevisiae membrane-integral VTC complex, together with Vtc1, Vtc3, and Vtc4. It contains an N-terminal SPX domain next to a central polyphosphate polymerase domain and a C-terminal domain of unknown function
KFGKTLKSSIYPPWKDYYIDYDKLKKLLKERETDRGWWTEDDERFFVELLEVELEKVYTFQKEKYSELRR
RIDACEKKVKELVSNLDSSEDDPSEEDFKELEEELDDILADVHDLAKFTRLNYTGFLKIVKKHDK
>gnl|CDD|269902 cd14481, SPX_AtSPX1_like, SPX domain of the plant protein SPX1 and similar proteins. This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. This family of plant proteins contains a single SPX domain. Arabidopsis thaliana SPX1 and SPX3 have been reported to play roles in the adaptation to low-phosphate conditions, SPX3 may be involved in the regulation of SPX1 activity. Oryza sativa SPX1 suppresses the regulation of expression of OsPT2, a low-affinity phosphate transporter, by the MYB-like OsPHR2
KFGKSLKRQIEETLPEWRDKFLSYKELKKLLKLISPGNADKPNSKRDRRGGGAARAMTKEEADFVRLLNA
ELDKFNAFFVEKEEEYVIRLKELQDRVAEAKETPRDSNEELMRIRREIVDFHGEMVLLENYSSLNYTGLV
KILKKYDKR
>gnl|CDD|269903 cd14482, SPX_BAH1-like, SPX domain of the E3 ubiquitin-protein ligase BAH1/NLA and similar proteins. This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. BAH1 (benzoic acid hypersensitive 1) appears to function as an E3 ubiquitin ligase; the protein contains an SPX and a RING finger domain. It has been suggested that BAH1/NLA is involved in the regulation of plant immune responses, probably via a pathway of salicylic acid biosynthesis that includes benzoic acid as an intermediate
KFGKTYEEYLRGEQEKFLEKCSHVEYKRLKKVLKKCRSDRSLQADDTNDDQASSDSSASCCPGSCPVCDG
MFFPELLKEMSDIVGCFNSRAQKLLELHLASGFQRYLLWFRQCFKDDHQALIQEGRDLVNYATMNAIAIR
KILKKYDKVHSSVNGR
>gnl|CDD|269904 cd14483, SPX_PHO81_NUC-2_like, SPX domain of Pho81, NUC-2, and similar proteins. This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors Pho81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. NUC-2 plays an important role in the phosphate-regulated signal transduction pathway in N. crassa. It shows high similarity to a cyclin-dependent kinase inhibitory protein Pho81, which is part of the phosphate regulatory cascade in S. cerevisiae. Both, NUC-2 and Pho81, have multi-domain architecture, including the SPX N-terminal domain following by several ankyrin repeats and a putative C-terminal glycerophosphodiester phosphodiesterase domain (GDPD) with unknown function
KFGKYIQARQLELPEYSAYFLDYKALKKLIKSLAAPRVAAAAALLAGGRPLSPDGTDESDAQTSLQANKA
AFFFKLERELEKVNAFYLQKEAELKLRLDTLLDKKRVLQSRGKLASKKSASFVTLEEGFRQFERDLNKLQ
QFVELNATGFSKILKKWDKRSK
>gnl|CDD|269905 cd14484, SPX_GDE1_like, SPX domain of Gde1 and similar proteins. This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors Pho81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. The yeast protein Gde1/Ypl110c is similar to both, NUC-2 and Pho81, in sharing their multi-domain architecture, which includes the SPX N-terminal domain followed by several ankyrin repeats and a C-terminal glycerophosphodiester phosphodiesterase domain (GDPD). Gde1 hydrolyzes intracellular glycerophosphocholine into glycerolphosphate and choline, and plays a role in the utilization of glycerophosphocholine as a source for phosphate
KFGKNLPRNQVPEWSSSYINYKGLKKLIKAIAEQQKEGVKVDLAEFFFALDRNLEDVDTFYNKKFAEYSR
RLKLLLDRYGFSPDLVQNLDSDELEELMGALLELRSQLRNLQWFGELNRRGFVKILKKLDKKVP
>gnl|CDD|270618 cd14485, mltA_like_LT_A, Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B. Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic, cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct
LPALRRSLAYLRRRPPDRVFPLGGLALTWGDLRASLEALLAFLLARLDAAPEALADFFQWVDGSGEGLFT
GYYEPGVPLTPGRSLAVDRSLIPLGAPVWLETPLPDANGGGKPLRRLVIAQDTGGAIKGPVRADLFWGSG
DEAGELAGRMKHPGRLWVL
>gnl|CDD|270619 cd14486, 3D_domain, 3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic transglycosylases and numerous other contexts. This family contains the 3D domain, named for its 3 conserved aspartates. It is found in conjunction with numerous other domains such as MltA (membrane-bound lytic murein transglycosylase A). These aspartates are critical active site residues of mltA-like lytic transglycosylases. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. MltA has 2 domains, separated by a large groove, where the peptidoglycan strand binds. The C-terminus has a double-psi beta barrel fold within the 3D domain, which forms the larger A domain along with the N-terminal region of Mlts, but is also found in various other domain architectures. Peptigoglycan (also known as murein) chains, the primary structural component of bacterial cells walls, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc); lytic transglycosylases (LTs) cleave this beta-1-4 bond. Typically, LTs are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, membrane-bound lytic murein transglycosylase E (MltE) is endolytic, cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane- bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and family 4 of bacteriophage origin. While most LTs are related members of the lysozyme-like lytic transglycosylase family, MltA represents a distinct fold and sequence conservation
FQATGYTEWDDGKRPSPPDEFSFSFRLTASGRPPVPYRTIAVDPSVIPLGSVVYIPELRGLPNDGVFVAE
DTGGAIKGNHIDVYTGDGPDARSNALKTVTVYVV
>gnl|CDD|271153 cd14487, AlgX_C, C-terminal carbohydrate-binding domain of the alginate O-acetyltranferase AlgX. The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. This N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains
RQLLPLVNNGCEGRPALLSGKTTLPPGKNEVLVNGAGNRLLELRNSALQLDLTFSDPSVKELYATVWYDN
GRREKVRIRRPARVDTDGRFVFELRPDADWADANLLSVDLEPPEPLTEPLEVEARLCL
>gnl|CDD|271154 cd14488, CBM6-CBM35-CBM36_like_2, uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily. Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules
NGVVVDNSDAGFSASGNWTTSTSIAGYYGTDYRYAEPVKGSDPATFTFKIPATGSYEVYVWYPANPNRNS
AAPYVVETAGGTSTVRVDQTTGGGTWVSLGTFEFKAGDQNKVTVSNWTTGGGYVIADAVRVV
>gnl|CDD|271155 cd14489, CBM_SBP_bac_1_like, Putative Carbohydrate Binding Module (CBM) of extracellular solute-binding protein family 1. Domains in this family co-occur with extracellular solute-binding domains which are periplasmic components of ABC-type sugar transport systems involved in carbohydrate transport and metabolism. Carbohydrate binding modules of family 6 (CBM6), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36) are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of co-occuring (catalytic) modules to their insoluble substrates
GILIVIQAEDPTLKSDPTLYPISDRSSPVTPPYSPSKLRLNTIGGENWRSSGQWIEWEFEVPEDGLYKIA
FKAKQNYKRGIPVFRRIYIDGRVPFKEAKNYAFEYDSDWQFKTLGDGGNPYLFYLTKGKHTLRLEVTLGP
FADVIQELQD
>gnl|CDD|271156 cd14490, CBM6-CBM35-CBM36_like_1, uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily. Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules
GATVPFTEYEAENATTNGTAIGPDRTYGTIASEASGRRAVRLDATGQYVEFTLTAPANAIVVRYSIPDSP
AGGGITATLSLYVNGVKVQTLNLTSKYSWLYGGYPWSNDPSGGKPHHFYDEARLLLDQTYPAGTKIKLQK
DSGDTASYYTIDFVDF
>gnl|CDD|381186 cd14491, lipocalin_MxiM-like, Shigella pilot protein MxiM and similar proteins. Shigella flexneri MxiM, is a pilot protein for S. flexneri MxiD, an outer membrane (OM)-associated ring-forming secretin and component of the type-III secretion system. MxiM, also an OM protein, binds lipids and MxiD. MxiM binds and affects several features of the secretin MxiD, including its stability in the periplasm, OM association, as well as assembly into multimeric structure. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
FSEKTWKLVPITKDYFKEQFYQGLWSEAEEKASRELLSITNDLLWSFNTTDVNGEVTGTISVYSKCISGK
AVYSFNGKAGKFMGSFNVKEVASDILAKKFISGLKNGVVYKGDKDNLLLYKKGGNTTVKLKFIR
>gnl|CDD|381187 cd14492, lipocalin_MxiM-like, MxiM-like lipocalin found in Bacteroidetes. Uncharacterized proteins in this family conserved in Bacteroidetes are similar to Shigella flexneri MxiM, a pilot protein for S. flexneri MxiD, an outer membrane (OM)-associated ring-forming secretin and component of the type-III secretion system. MxiM, also an OM protein, binds lipids and MxiD. This subgroup belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
NDEDDVNEIFTGKTWKLTYITEAGGWEQYDNWSNEAAAYQSKKDLKGLGAFTITFNGDEEDNIIGGTFNG
TGVNGTFTGTWSANGKSNTISISIKKTTTSLDGLAKEFIEGLKNAKKYEGDSRNLYLYYEDGQTTTYIQF
TH
>gnl|CDD|381188 cd14493, lipocalin_MxiM, Shigella Pilot protein MxiM. Shigella flexneri MxiM is a pilot protein for S. flexneri MxiD, an outer membrane (OM)-associated ring-forming secretin. MxiM, also an OM protein, binds lipids and MxiD. MixD is a component of the type-III secretion system that translocates proteins through both membranes of gram-negative bacterial pathogens into host cells and requires the formation of an integral OM secretin ring. MxiM binds and affects several features of the secretin MxiD, including its stability in the periplasm, OM association, as well as assembly into multimeric structure. MxiM belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
SSSNSEKEWHIVPVSKDYFSIPNDLLWSFNTTNKSINVYSKCISGKAVYSFNAGKFMGNFNVKEVDGCFM
DAQKIAIDKLFSMLKDGVVLKGNKINDTILIEKDGEVKLKLIRGI
>gnl|CDD|350344 cd14494, PTP_DSP_cys, cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily. This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases
FNWIDPLRLIAGALPLSPLEADSRFLKQLGVTTIVDLTLAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRT
GTLVACYLVLLGGMSAEEAVRIVRLIRPGGIPQTIEQLDFLIK
>gnl|CDD|350345 cd14495, PTPLP-like, Protein tyrosine phosphatase-like domains of phytases and similar domains. This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates
VWRLDAKNKAQLPRNFRTSNDAFKLPLGKVPSRKGLDTLRLSGSAQFSEKQLKAILKKLKEKAKGPIYVV
DLRQESHGFLNGIAVSWYGPRDWANLGKSQSEVLADERNRLQALLGKKVVSIPLGKDKKKSPSQPKTVKV
ESVRTEEELVKKKGAHYVRIAATDHVWPDDEEIDAFVAFYRSLPADAWLHFHCRAGKGRTTTFMVMYDML
KNPKDVSFDDIIARQYLIGGNYLAYEVDKDKNWKRPYYEERAQFLQKFYQYVQENPAGGKTSWSEWLK
>gnl|CDD|350346 cd14496, PTP_paladin, protein tyrosine phosphatase-like domains of paladin. Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two protein tyrosine phosphatase (PTP)-like domains. This model represents both repeats
RSGSVLGAGTILKSDHFPGCQSLTLPERVEGAPNFRRVPGLPVYGVAQPTIDGIRRVLSRLGAAPDGRGR
VVWVNLREEPVVYINGRPFVLREVERRVDYHRIPITDEKAPEPGDFDALLEVILSTDDPTTAFVFNCQMG
RGRTTTGMVIASLVRGEYVVIRKLVRVLDHGKEAKRLVDRAIDAC
>gnl|CDD|350347 cd14497, PTP_PTEN-like, protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins. Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity
DLSYITPRIIAMSFPATGYPESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDDSKFEGRVLHYGFPD
HHPPPLGLLLEIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKE
GLPGVTIPSQLRYLQYFERL
>gnl|CDD|350348 cd14498, DSP, dual-specificity phosphatase domain. The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase
PSEILPGLYLGSLDAAQDKELLKKLGITHILNVAGEPPPNKFPDGIKYLRIPIEDSPDEDILSHFEEAIE
FIEEALKKGGKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRPIISPNPGFLKQLKE
>gnl|CDD|350349 cd14499, CDC14_C, C-terminal dual-specificity phosphatase domain of CDC14 family proteins. The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif
TFDLEEYEHYERVENGDLNWIVPGKFLAFSGPHDTRKDENGYPTHTPEDYIPYFKKLGVTTVVRLNKKLY
DAKRFTDAGIRHYDLYFPDGSTPSDDIVKKFLDICENEKGAIAVHCKAGLGRTGTLIACYLMKHYGFTAR
EAIAWLRICRPGSVIGPQQQFLEEKEARLWRAGD
>gnl|CDD|350350 cd14500, PTP-IVa, protein tyrosine phosphatase type IVA family. Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3
LRPAPTLIEYKGMRFLITDAPTDSNLPLYIKELKKYNVTDLVRVCEPTYDKEPLEKAGIKVHDWPFDDGS
PPPDDVVDDWLDLLKTRFKEEGKPGACIAVHCVAGLGRAPVLVAIALIELGMKPEDAVEFIRKKRRGAIN
SKQLQFLEKYKPKKKL
>gnl|CDD|350351 cd14501, PFA-DSP, plant and fungi atypical dual-specificity phosphatase. Plant and fungi atypical dual-specificity phosphatases (PFA-DSPs) are a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds. They share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The PFA-DSP group is composed of active as well as inactive phosphatases. The best characterized member is Saccharomyces Siw14, also known as Oca3, which plays a role in actin filament organization and endocytosis. Siw14 has been shown to be an inositol pyrophosphate phosphatase, hydrolyzing the beta-phosphate from 5-diphosphoinositol pentakisphosphate (5PP-IP5or IP7)
VPPLNFSIVEPGLYRSAYPTPANFPFLKTLGLKTIILLSPEPPPKPVLSFLTENGIKLIHLGMLSSKRAD
SVPWDPLAYELVKRALEILLDKTNYPVLVHCSLGEHRTGVVVGCLRKLQGWSLASILDEYRLFAGSKERY
VDEQFIELF
>gnl|CDD|350352 cd14502, RNA_5'-triphosphatase, RNA 5'-triphosphatase domain. This family of RNA-specific cysteine phosphatases includes baculovirus RNA 5'-triphosphatase, dual specificity protein phosphatase 11 (DUSP11), and the RNA triphosphatase domains of metazoan and plant mRNA capping enzymes. RNA/polynucleotide 5'-triphosphatase (EC 3.1.3.33) catalyzes the removal of the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end. mRNA capping enzyme is a bifunctional enzyme that catalyzes the first two steps of cap formation. DUSP11 has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity
KWLDCPPVGQPVGPTRFIPMKTPLSDDYEHLFAPEIRFTPSALAEKFRQDRKVGLVIDLTNTDRYYDPND
LDDDGYVYYKKVCVRKEPPDAEEVNKFIELVDKFLAEDNPDKLIAVHCTHGFNRTGFMIVSYLVERLGLT
VEQALEAFAQARPPGIYKPHYIDELYR
>gnl|CDD|350353 cd14503, PTP-bact, bacterial tyrosine-protein phosphataseS similar to Neisseria NMA1982. This subfamily is composed of bacterial tyrosine-protein phosphatases similar to Neisseria meningitidis NMA1982, which displays phosphatase activity but whose biological function is still unknown
NFRKISDRLATAGQPTPEQFAALAAAGFKTVINLRPDGEENALPNEAAAVTAAGMEYVHIPVDWDNPTPE
DVERFFEVMDAAQGKPVLVHCASNMRASAFWYLYRALDGGVSEEEAIQLMRSAGFPLPAWQPFIEQ
>gnl|CDD|350354 cd14504, DUSP23, dual specificity phosphatase 23. Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin
FSWVIPGKLAGMAFPRLPEHYAYLNENGIRHVVTLTEEPPPEHSDTCPGLRYHHIPIEDYTPPTLEQIDE
FLDIVEEANAKNEAVLVHCLAGKGRTGTMLACYLVKTGKISAVDAINEIRRIRPGSIETSEQEKFVIQFA
KT
>gnl|CDD|350355 cd14505, CDKN3-like, cyclin-dependent kinase inhibitor 3 and similar proteins. This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function
IDWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQ
AGITWHHLPIPDGGVPSDIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTLDPEQA
IAAVRALRPGAIQTPKQENFLHQ
>gnl|CDD|350356 cd14506, PTP_PTPDC1, protein tyrosine phosphatase domain of PTP domain-containing protein 1. protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia
QAIKGLYSSWITDDILAMARPSTELIDKYGIIEQFKEKGIKTVINLQEPGEHASCGPGLEPESGFSYLPE
AFMRAGIYFYNFGWKDYGVPSLTTILDIVKVMAFALQEGGKVAVHCHAGLGRTGVLIACYLVYALRMSAD
QAIRLVRSKRPNSIQTRGQVLCVREFAQFLLPLRNVFACPDPKAAVTLRQYLIRQRHLLHGYEARN
>gnl|CDD|350357 cd14507, PTP-MTM-like, protein tyrosine phosphatase-like domain of myotubularins. Myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. Not all members are catalytically active proteins, some function as adaptors for the active members
GRIPVLSWRHPRNGAVICRSSQPLVGLTGSRSKEDEKLLNAIRKASPSSKKLYIVDARPKLNAVANRAKG
GGYENTEYYPNCELEFLNIENIHAMRDSLNKLRDACLSPNDEESNWLSALESSGWLEHIRLILKGAVRVA
DLLEKEGTSVLVHCSDGWDRTSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDKNSSD
EERSPIFLQFLDCVWQ
>gnl|CDD|350358 cd14508, PTP_tensin, protein tyrosine phosphatase-like domain of tensins. The tensin family of intracellular proteins (tensin-1, -2, -3 and -4) act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Dysregulation of tensin expression has been implicated in human cancer. Tensin-1, -2, and -3 contain an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. In addition, tensin-2 contains a zinc finger N-terminal to its PTP domain. Tensin-4 is not included in this model as it does not contain a PTP-like domain
DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNLSERRHDLRSLNPKVLDFGWPELH
APPLEKLCSICKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRFYDDK
VGPLGQPSQKRYVGYFSGL
>gnl|CDD|350359 cd14509, PTP_PTEN, protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog. Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain
DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSERSYDPSKFNGRVAEYPFDDH
NPPPLELIKPFCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNK
KGVTIPSQRRYVYYYSRL
>gnl|CDD|350360 cd14510, PTP_VSP_TPTE, protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology. Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain
SENKRRYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLCSERGYDPK
YFHNRVERVPIDDHNVPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAK
EALEYFGERRTDKSVSSKFQGVETPSQSRYVGYFEKL
>gnl|CDD|350361 cd14511, PTP_auxilin-like, protein tyrosine phosphatase-like domain of auxilin and similar proteins. This subfamily contains proteins similar to auxilin, characterized by also containing a J domain. It includes auxilin, also called auxilin-1, and cyclin-G-associated kinase (GAK), also called auxilin-2. Auxilin-1 and -2 facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, while auxilin-1 which is nerve-specific. Both proteins contain a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. In addition, GAK contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2
QQSYARNDLDISYITSRIIVMPFPAEGIESTYRKNNIEDVRAFLDSRHPQKYSVYNLSPRSYPTLRLPSR
VVECSWPYRRAPSLHALYALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQM
FAVKRCPPGLSPSELRYLYYFSDI
>gnl|CDD|350362 cd14512, DSP_MKP, dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase. Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs, which are involved in gene regulation, cell proliferation, programmed cell death and stress responses, as an important feedback control mechanism that limits MAPK cascades. MKPs, also referred to as typical DUSPs, function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III)
PTRILPNLYLGSQRDSLNLELMQQLGIGYVLNVSNTCPNPDFIGLFHYKRIPVNDSFCQNISPWFDEAIE
FIEEAKASNGGVLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRPTISPNFNFMGQLLDF
>gnl|CDD|350363 cd14513, DSP_slingshot, dual specificity phosphatase domain of slingshot family phosphatases. The slingshot (SSH) family of dual specificity protein phosphatases is composed of Drosophila slingshot phosphatase and its vertebrate homologs: SSH1, SSH2 and SSH3. Its members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. In Drosophila, loss of ssh gene function causes prominent elevation in the levels of P-cofilin and filamentous actin and disorganized epidermal cell morphogenesis, including bifurcation phenotypes of bristles and wing hairs. SSH family phosphatases contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. In addition, many members contain a C-terminal tail. The SSH-N domain plays critical roles in P-cofilin recognition, F-actin-mediated activation, and subcellular localization of SSHs
ASKIFDHLYLGSEWNASNLEELQNNGVKYILNVTREIDNFFPGRFTYHNIRVWDEESTNLLPYWNETYRF
IKEARRKGSKVLVHCKMGVSRSASTVIAYAMKEYGWSLEQALEHVKERRSCIKPNPGFLRQLITYEGML
>gnl|CDD|350364 cd14514, DUSP14-like, dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins. This family is composed of dual specificity protein phosphatase 14 (DUSP14, also known as MKP-6), 18 (DUSP18), 21 (DUSP21), 28 (DUSP28), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses. DUSP18 has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane. DUSP28 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells
ISQITPHLFLSGASAATPPLLLSRGITCIINATTELPDPSYPGIEYLRVPVEDSPHADLSPHFDEVADKI
HQVKRRGGRTLVHCVAGVSRSATLCLAYLMKYEGMTLREAYKHVKAARPIIRPNVGFWRQLIE
>gnl|CDD|350365 cd14515, DUSP3-like, dual specificity protein phosphatases 3, 13, 26, 27, and similar domains. This family is composed of dual specificity protein phosphatase 3 (DUSP3, also known as VHR), 13B (DUSP13B, also known as TMDP), 26 (DUSP26, also known as MPK8), 13A (DUSP13A, also known as MDSP), dual specificity phosphatase and pro isomerase domain containing 1 (DUPD1), and inactive DUSP27. In general, DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Members of this family are atypical DUSPs; they contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Inactive DUSP27 contains a dual specificity phosphatase-like domain with the active site cysteine substituted to serine
VDEVWPGIYIGDESTAKNKAKLKKLGITHVLNAAEGKKNGEVNTNAKFYKGSGIIYLGIPASDLPTFDIS
QYFDEAADFIDKALSDPGGKVLVHCVEGVSRSATLVLAYLMIYQNMTLEEAIRTVRKKREIRPNRGFLQQ
LCELNDKL
>gnl|CDD|350366 cd14516, DSP_fungal_PPS1, dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like. This subfamily contains fungal proteins with similarity to dual specificity protein phosphatase PPS1 from Saccharomyces cerevisiae, which has a role in the DNA synthesis phase of the cell cycle. As a dual specificity protein phosphatase, PPS1 functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It contains a C-terminal catalytic dual specificity phosphatase domain
KFDGSLPSRILPHLYLGSLNHASNATLLESLGITHIVSVGESPSWFSNLKIKYIFDFSLQDLSNLDSNSE
GSLWAAEYKGLISVLYIHNLKDDGIDSLLPQLTDALDFIQKARLLGGKTLVHCRVGVSRSATVVIAEVMK
HLRMSLVDAYLFVRVRRLNIIIQPNLRFFYELFKWEE
>gnl|CDD|350367 cd14517, DSP_STYXL1, dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1. Serine/threonine/tyrosine interacting like 1 (STYXL1), also known as DUSP24 and MK-STYX, is a catalytically inactive phosphatase with homology to the mitogen-activated protein kinase (MAPK) phosphatases (MKPs). STYXL1 plays a role in regulating pathways by competing with active phosphatases for binding to MAPKs. Similar to MKPs, STYXL1 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, however its C-terminal dual specificity phosphatase-like domain is a pseudophosphatase missing the catalytic cysteine
PRELDNLKTYPVEILPGFLYMGNYKQACDKKIQKDLKIKAHINVSMDADELFKSGNDQVLHIPVEDSVEA
DLLSFFERACSFIDKHKNNGSRVLVFSTLGISRSVAVAIAYLMYHYKWSLKDAWKYLLKCKNNMRPNRGF
VKQLSEWEEKLLGTT
>gnl|CDD|350368 cd14518, DSP_fungal_YVH1, dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase. This family is composed of Saccharomyces cerevisiae dual specificity protein phosphatase Yvh1 and similar fungal proteins. Yvh1 could function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It regulates cell growth, sporulation, and glycogen accumulation. It plays an important role in ribosome assembly. Yvh1 associates transiently with late pre-60S particles and is required for the release of the nucleolar/nuclear pre-60S factor Mrt4, which is necessary to construct a translation-competent 60S subunit and mature ribosome stalk. Yvh1 contains an N-terminal catalytic dual specificity phosphatase domain and a C-terminal tail
LSRILGGLYLGGIEPLNRNRLLKAENITHILSVIPGDVPEEYFKGYEHKQIEIDDVEDENILQHFPETNR
FIDSALFGNGKDEDEEKKHGGAVLVHCAMGKSRSVTVVIAYLMYKYNLSVSQALHAVRRKRPIAEPNDGF
MEQLELYHEMGCP
>gnl|CDD|350369 cd14519, DSP_DUSP22_15, dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and similar proteins. Dual specificity protein phosphatase 22 (DUSP22, also known as VHX) and 15 (DUSP15, also known as VHY) function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). They are atypical DUSPs; they contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. The both contain N-terminal myristoylation recognition sequences and myristoylation regulates their subcellular location. DUSP22 negatively regulates the estrogen receptor-alpha-mediated signaling pathway and the IL6-leukemia inhibitory factor (LIF)-STAT3-mediated signaling pathway. DUSP15 has been identified as a regulator of oligodendrocyte differentiation. DUSP22 is a single domain protein containing only the catalytic dual specificity phosphatase domain while DUSP15 contains a short C-terminal tail
MNKILPGLYVGNFRDAKDAEQLRENGITHILSIHDSARPLLEDIKYLCIPAADTPEQNISQHFRECINFI
HEARLNGGNVLVHCLAGVSRSVTIVAAYLMTVTDLGWRDALKAVRAARPCANPNFGFQRQLQEFEK
>gnl|CDD|350370 cd14520, DSP_DUSP12, dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar proteins. Dual specificity protein phosphatase 12 (DUSP12), also called YVH1, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP12 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It targets p38 MAPK to regulate macrophage response to bacterial infection. It also ameliorates cardiac hypertrophy in response to pressure overload through c-Jun N-terminal kinase (JNK) inhibition. DUSP12 has been identified as a modulator of cell cycle progression, a function independent of phosphatase activity and mediated by its C-terminal zinc-binding domain
MKLVRPGLYIGNADDAADYLSLREAGITHVLTVDSEEPIDAPPVGKLVRKFVPALDEESTDLLSRLDECL
DFIDEGRAEGAVLVHCHAGVSRSAAVVTAYLMKTEQLSFEEALASLRECKPDVKPNDGFLKQLKLYEAMG
CKVD
>gnl|CDD|350371 cd14521, DSP_fungal_SDP1-like, dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, and similar proteins. This family is composed of fungal dual specificity protein phosphatases (DUSPs) including Saccharomyces cerevisiae SDP1 and MSG5, and Schizosaccharomyces pombe Pmp1. function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. SDP1 is oxidative stress-induced and dephosphorylates MAPK substrates such as SLT2. MSG5 dephosphorylates the Fus3 and Slt2 MAPKs operating in the mating and cell wall integrity (CWI) pathways, respectively. Pmp1 is responsible for dephosphorylating the CWI MAPK Pmk1. These phosphatases bind to their target MAPKs through a conserved IYT motif located outside of the dual specificity phosphatase domain
YPDGPVCVLPPNIYLYSEPTLEEASSFDVVINVAKEVKNPFLSDASLAEKEKTILPGQQVKNPEYIHVPW
DHNSQIQKDLPKLTSIIEDATQSGKKVLIHCQCGVSRSASLIIAYIMKKLGLSLNDAYDLLKSRSPWIGP
NMSLIFQLMEFEKVL
>gnl|CDD|350372 cd14522, DSP_STYX, dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein. Serine/threonine/tyrosine-interacting protein (STYX), also called protein tyrosine phosphatase-like protein, is a catalytically inactive member of the protein tyrosine phosphatase family that plays an integral role in regulating pathways by competing with active phosphatases for binding to MAPKs. It acts as a nuclear anchor for MAPKs, affecting their nucleocytoplasmic shuttling
MRREMQEILPGLYLGPYSAAMKSKLEVLLKHGITHIVCVRQNIEANFIKPNFPDHFRYLVLDVADNPTEN
IIRHFPTVKEFIDDCLQTGGKVLVHGNAGISRSAALVIAYIMETYGLSYRDAFAYVQQRRFCINPNEGFV
HQLKEYEAIYL
>gnl|CDD|350373 cd14523, DSP_DUSP19, dual specificity phosphatase domain of dual specificity protein phosphatase 19. Dual specificity protein phosphatase 19 (DUSP19), also called low molecular weight dual specificity phosphatase 3 (LMW-DSP3) or stress-activated protein kinase (SAPK) pathway-regulating phosphatase 1 (SKRP1), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP19 interacts with the MAPK kinase MKK7, a JNK activator, and inactivates the JNK MAPK pathway
QVGVIKPWLLLSSQDVAHDLETLKKHKVTHILNVAYGVENAFPDDFTYKTISILDLPETDITSYFPECFE
FIDEAKSQDGVVLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNARPSIRPNPGFMEQLKEYQ
>gnl|CDD|350374 cd14524, PTPMT1, protein-tyrosine phosphatase mitochondrial 1. Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates
WYDRIDDTVILGALPFRSMTVALVAKENVRGVITMNEEYETRFFCNSKEEWKALGVEQLRLPTVDFTGVP
SLEDLEKGVDFILKHREKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRPHILLRLSQR
EVLEEFYRK
>gnl|CDD|350375 cd14526, DSP_laforin-like, dual specificity phosphatase domain of laforin and similar domains. This family is composed of glucan phosphatases including vertebrate dual specificity protein phosphatase laforin, also called lafora PTPase (LAFPTPase), and plant starch excess4 (SEX4). Laforin is a glycogen phosphatase; its gene is mutated in Lafora progressive myoclonus epilepsy or Lafora disease (LD), a fatal autosomal recessive neurodegenerative disorder characterized by the presence of progressive neurological deterioration, myoclonus, and epilepsy. One characteristic of LD is the accumulation of insoluble glucans. Laforin prevents LD by at least two mechanisms: by preventing hyperphosphorylation of glycogen by dephosphorylating it, allowing proper glycogen formation, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with malin. Laforin contains an N-terminal CBM20 (carbohydrate-binding module, family 20) domain and a C-terminal catalytic dual specificity phosphatase (DSP) domain. Plant SEX4 regulate starch metabolism by selectively dephosphorylating glucose moieties within starch glucan chains. It contains an N-terminal catalytic DSP domain and a C-terminal Early (E) set domain
LNYSRILPNLIVGSCPQNPEDVDRLKKEGVTAVLNLQTDSDMEYWGVDIDSIRKACKESGIRYVRLPIRD
FDTEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPD
EEAIRG
>gnl|CDD|350376 cd14527, DSP_bac, unknown subfamily of bacterial and plant dual specificity protein phosphatases. This subfamily is composed of uncharacterized bacterial and plant dual-specificity protein phosphatases. DUSPs function as a protein-serine/threonine phosphatases (EC 3.1.3.16) and a protein-tyrosine-phosphatases (EC 3.1.3.48)
RLPAYDEVLPGLYLGRWPSADELPPGVPAVLDLTAELPRPRKRQAYRCVPLLDLVAPTPEQLERAVAWIE
ELRAQGGPVLVHCALGYGRSATVVAAWLLAYGRAKSVAEAEALIRAARPQVVLNPAQRKALEAWSG
>gnl|CDD|350377 cd14528, PFA-DSP_Siw14, atypical dual specificity phosphatases similar to yeast Siw14. This subfamily contains Saccharomyces Siw14 and a novel phosphatase from the Arabidopsis thaliana gene locus At1g05000. Siw14, also known as Oca3, plays a role in actin filament organization and endocytosis. Siw14 has been shown to be an inositol pyrophosphate phosphatase, hydrolyzing the beta-phosphate from 5-diphosphoinositol pentakisphosphate (5PP-IP5or IP7). The At1g05000 protein, also called AtPFA-DSP1, has been shown to have highest activity toward olyphosphate (poly-P(12-13)) and deoxyribo- and ribonucleoside triphosphates, and less activity toward phosphoenolpyruvate, phosphotyrosine, phosphotyrosine-containing peptides, and phosphatidylinositols. This subfamily belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs)
LLIPPLNFSMVDKGVYRSGYPNKKNFPFLRTLGLRSILYLCPEDYPESNLEFLKENGIKLFQFGIEGNKE
PFVDIPEELIRDALKVLLDPRNHPVLIHCNKGKHRTGCLVGCLRKLQNWSLTSIFDEYRRFAGPKARMLD
QQFIELFD
>gnl|CDD|350378 cd14529, TpbA-like, bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA. This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs
DGANNFRDVTPYVLYRSAQLSPDEDRALLKKLGIKTVIDLRGADERAASEEAAAKIDGVKYVNLPLSATR
PTESDVQSFLLIMDLKLAPGPVLIHCKHGKDRTGLVSALYRIVYGGSKEEANEDYRLSNRHLEGLRSGIA
LDSKGGVKGRYLAAYFER
>gnl|CDD|350379 cd14531, PFA-DSP_Oca1, atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 1. Oxidant-induced cell-cycle arrest protein 1 (Oca1) is an atypical dual specificity phosphatase whose gene is required for G1 arrest in response to the lipid oxidation product linoleic acid hydroperoxide. It may function in linking growth, stress responses, and the cell cycle. Oca1 belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs)
SFIPPLNFGMVEEDLYRSGQPTPINFPFLERLKLKTIIYLAPDEPSDQFLEFCEDQNINLVHLGGDDSTE
SRQNPLSEELVLAALHIILDPDNYPLLVMCNLGRHRTGTVVGCLRKLQRWNLSSIFEEYRRFAGSKVRLL
NEQFIELFD
>gnl|CDD|350380 cd14532, PTP-MTMR6-like, protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases 6, 7, and 8. This subgroup of enzymatically active phosphatase domains of myotubularins consists of MTMR6, MTMR7 and MTMR8, and related domains. Beside the phosphatase domain, they contain a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. MTMR6, MTMR7 and MTMR8 form complexes with catalytically inactive MTMR9, and display differential substrate preferences. In cells, the MTMR6/R9 complex significantly increases the cellular levels of PtdIns(5)P, the product of PI(3,5)P(2) dephosphorylation, whereas the MTMR8/R9 complex reduces cellular PtdIns(3)P levels. The MTMR6/R9 complex serves to inhibit stress-induced apoptosis while the MTMR8/R9 complex inhibits autophagy
LESEYTRMGVPNDNWTLSDINKDYELCDTYPRELFVPTSASTPVLVGSSKFRSKGRLPVLSYLHKDNQAA
ICRCSQPLSGFSARCVEDEQLLQAIRKANPNSKFMYVVDTRPKINAMANKAAGKGYENEDNYSNIKFQFF
GIENIHVMRSSLQKLLEVCELKNPSMSAFLSGLESSGWLKHIKAVMDTSVFIAKAVSEGASVLVHCSDGW
DRTAQTCSLASLLLDPYYRTIKGFQVLIEKEWLSFGHKFTDRCGHLQGDAKEVSPVFTQFLDCVWQLMQQ
FPRAFEFNERFLLTLHDHVYS
>gnl|CDD|350381 cd14533, PTP-MTMR3-like, protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases 3 and 4. This subgroup of enzymatically active phosphatase domains of myotubularins consists of MTMR3, also known as ZFYVE10, and MTMR4, also known as ZFYVE11, and related domains. Beside the phosphatase domain, they contain a C-terminal FYVE domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively
SKRIPSVVWRHQRNGAVIARCSQPEVGWLGWRNAEDENLLQAIAEACASNASPKKLLIVDARSYAAAVAN
RAKGGGCECPEYYPNCEVVFMNLANIHAIRKSFHSLRALCSSAPDQPNWLSNLESTKWLHHLSGLLKAAL
LVVNAVDEEGRPVLVHCSDGWDRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFGHKFADRCGHGVNS
EDINERCPVFLQWLDCVHQ
>gnl|CDD|350382 cd14534, PTP-MTMR5-like, protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatases 5 and 13. This subgroup of enzymatically inactive phosphatase domains of myotubularins consists of MTMR5, also known as SET binding factor 1 (SBF1) and MTMR13, also known as SET binding factor 2 (SBF2), and similar domains. Beside the pseudophosphatase domain, they contain a variety of other domains, including a DENN and a PH-like domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR5 and MTMR13 are pseudophosphatases that lack the catalytic cysteine in their catalytic pocket. Mutations in MTMR13 causes Charcot-Marie-Tooth type 4B2, a severe childhood-onset neuromuscular disorder, characterized by demyelination and redundant loops of myelin known as myelin outfoldings, a similar phenotype as mutations in MTMR2. Mutations in the MTMR5 gene cause Charcot-Marie-tooth disease type 4B3. MTMR5 and MTMR13 interact with MTMR2 and stimulate its phosphatase activity
FRISTANRDYSICRSYPALVVVPQSVSDESLRKVARCYRQGRFPVVTWRHPRTKALLLRSGGFHGKGVMG
MLKSANTSTSSPTVSSSETSSSLEQEKYLSALVLYVLGEKSQMKGVKAESDPKCEFIPVEYPEVRQVKAS
FKKLLRACVPSSAPTEPEQSFLKAVEDSEWLQQLQCLMQLSGAVVDLLDVQGSSVLLCLEDGWDVTTQVS
SLSQLLLDPYYRTLEGFRVLVEKEWLAFGHRFSHRSNLTAASQSSGFAPVFLQFLDAVHQIHRQ
>gnl|CDD|350383 cd14535, PTP-MTM1-like, protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related phosphoinositide phosphatases 1 and 2. This subgroup of enzymatically active phosphatase domains of myotubularins consists of MTM1, MTMR1 and MTMR2. All contain an additional N-terminal PH-GRAM domain and C-terminal coiled-coiled domain and PDZ binding site. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively
NRIPVLSWIHPESQATITRCSQPLVGVSGKRSKDDEKYLQLIMDANAQSHKLFIMDARPSVNAVANKAKG
GGYESEDAYQNAELVFLDIHNIHVMRESLRKLKDICFPNIDDSHWLSNLESTHWLEHIKLILAGAVRIAD
KVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGHGDKNHSDA
DRSPVFLQFIDCVWQMTRQFPNAFEFNEHFLITILDHLY
>gnl|CDD|350384 cd14536, PTP-MTMR9, protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 9. Myotubularin related phosphoinositide phosphatase 9 (MTMR9) is enzymatically inactive and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. Mutations have been associated with obesity and metabolic syndrome. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR9 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket. It forms complexes with catalytically active MTMR6, MTMR7 and MTMR8, and regulates their activities; the complexes display differential substrate preferences. The MTMR6/R9 complex serves to inhibit stress-induced apoptosis while the MTMR8/R9 complex inhibits autophagy
GRFPVLSYYHKKNGMVLMRSSQPLTGPNGKRCKEDEKLLNAVLGGGKRGYIIDTRSKNVAQQARAKGGGF
EPEAHYPQWRRIHKPIERYNVLQESLIKLVEACNDQGHSMDKWLSKLESSNWLSHVKEILTTACLVAQCI
DREGASVLVHGSEGMDSTLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRCAKSAYSNSKQKF
ESPVFLLFLDCVWQ
>gnl|CDD|350385 cd14537, PTP-MTMR10-like, protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatases 10, 11, and 12. This subgroup of enzymatically inactive phosphatase domains of myotubularins consists of MTMR10, MTMR11, MTMR12, and similar proteins. Beside the phosphatase domain, they contain an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR10, MTMR11, and MTMR12 are pseudophosphatases that lack the catalytic cysteine in their catalytic pocket. MTMR12 functions as an adapter for the catalytically active myotubularin to regulate its intracellular location
GRPPVWCWSHPNGAALVRMAELLPTITDRTQENKMLEAIRKSHPNLKKPKVIDLDKLLPSLQDVQAAYLK
LRELCTPDSSEQFWVQDSKWYSLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQESDGRDLSCVVSS
LVQLLLDPHFRTITGFQSLIQKEWVALGHPFCDRLGHVKPNKTESEESPVFLLFLDCVWQ
>gnl|CDD|350386 cd14538, PTPc-N20_13, catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13. Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness
YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPL
ICGGRLEVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNS
GPIVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL
>gnl|CDD|350387 cd14539, PTP-N23, PTP-like domain of tyrosine-protein phosphatase non-receptor type 23. Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence
YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALV
YGAITVSLQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQR
SLQTPIVVHCSSGVGRTGAFCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE
>gnl|CDD|350388 cd14540, PTPc-N21_14, catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14. Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence
YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHD
ALTFGEYKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRR
HTNQDVAGHNRNPPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKF
VYNVLIQYL
>gnl|CDD|350389 cd14541, PTPc-N3_4, catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14. Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses
DYINANYVNMEIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE
TMQFGNLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRV
GMVEPTVVHCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVY
EE
>gnl|CDD|350390 cd14542, PTPc-N22_18_12, catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12. Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling
YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQF
GPFKISLEKEKRVGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVP
ICVHCSAGCGRTGTICAIDYVWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR
>gnl|CDD|350391 cd14543, PTPc-N9, catalytic domain of tyrosine-protein phosphatase non-receptor type 9. Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer
QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQ
KNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVEN
KEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPG
PPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK
>gnl|CDD|350392 cd14544, PTPc-N11_6, catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6. Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events
NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIRNENEGPTTDENAKTYIATQGCLENTVSDFWS
MVWQENSRVIVMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIR
EIWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKG
LDCDIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAVAQYIET
>gnl|CDD|350393 cd14545, PTPc-N1_2, catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2. Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner
LNRYRDRDPYDHDRSRVKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIML
NKLMEKGQIKCAQYWPQGEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWP
DFGVPESPAAFLNFLQKVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSSVDVKKVLL
EMRKYRMGLIQTPDQLRFSYL
>gnl|CDD|350394 cd14546, R-PTP-N-N2, PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2. Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion
YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYH
IYEVHLVSEHIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSC
PIVVHCSDGAGRTGTYILIDMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEVN
>gnl|CDD|350395 cd14547, PTPc-KIM, catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases. The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation
NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIV
MITNLTEAKEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTP
EAAQPLLSLVQEVEEARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRG
GMVQTAEQYEFVHR
>gnl|CDD|350396 cd14548, R3-PTPc, catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins. R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation
RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVML
TQCMEKGRVKCDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVP
EAPDSLLRFVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLM
VQTEAQYIFLHQ
>gnl|CDD|350397 cd14549, R5-PTPc-1, catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1. The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1)
YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGN
IQVTLLSTEVLATYTVRTFSLKNLKLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANP
PGAGPIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD
>gnl|CDD|350398 cd14550, R5-PTP-2, PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2. The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2)
YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKEKPLECETF
KVTLSGEDHSCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDG
PIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK
>gnl|CDD|350399 cd14551, R-PTPc-A-E-1, catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1. Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1)
YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGN
LRVRVEDTVVLVDYTTRKFCIQKVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPR
AGPIVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ
>gnl|CDD|350400 cd14552, R-PTPc-A-E-2, catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2. Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2)
YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGD
ITVELKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNHP
ITVHCSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ
>gnl|CDD|350401 cd14553, R-PTPc-LAR-1, catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1. The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1)
EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQR
SATIVMMTKLEERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFT
AWPDHGVPEHPTPFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTC
LRAQRNYMVQTEDQYIFIHDALLEAVTC
>gnl|CDD|350402 cd14554, R-PTP-LAR-2, PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2. The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2)
ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLW
EHNSTIIVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQF
QFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVF
QTVKLLRTQRPAMVQTEDQYQFCYRAAL
>gnl|CDD|350403 cd14555, R-PTPc-typeIIb-1, catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1. The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain
YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDI
KVTLVETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIV
VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL
>gnl|CDD|350404 cd14556, R-PTPc-typeIIb-2, PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2. The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain
YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSGTYGPI
QVEFVSTTIDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQSGE
GPIVVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD
>gnl|CDD|350405 cd14557, R-PTPc-C-1, catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1. Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1
YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAF
GDVVVKINEEKICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFS
GPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ
>gnl|CDD|350406 cd14558, R-PTP-C-2, PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2. Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2
YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDI
EVELKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHG
RSVPIVVHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD
>gnl|CDD|350407 cd14559, PTP_YopH-like, YopH and related bacterial protein tyrosine phosphatases. Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain
NRFTNIQTRVSTPVGKNLNANRVQIGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKG
LPPYFRQSGTYGSVTVKSKKTGKDELVDGLKADMYNLKITDGNKTITIPVVHVTNWPDHTAISSEGLKEL
ADLVNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDIVSDMRTS
RNGKMVQKDEQLDTLKE
>gnl|CDD|350408 cd14560, PTP_tensin-1, protein tyrosine phosphatase-like domain of tensin-1. Tensin-1 (TNS1) is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. It plays an essential role in TGF-beta-induced myofibroblast differentiation and myofibroblast-mediated formation of extracellular fibronectin and collagen matrix. It also positively regulates RhoA activity through its interaction with DLC1, a RhoGAP-containing tumor suppressor; the tensin-1-DLC1-RhoA signaling axis is critical in regulating cellular functions that lead to angiogenesis. Tensin-1 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains
DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLH
APALEKICSICKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFYEDK
VVPVGQPSQKRYVHYFSGL
>gnl|CDD|350409 cd14561, PTP_tensin-3, protein tyrosine phosphatase-like domain of tensin-3. Tensin-3 (TNS3) is also called tensin-like SH2 domain-containing protein 1 (TENS1) or tumor endothelial marker (TEM6). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-3 contributes to cell migration, anchorage-independent growth, tumorigenesis, and metastasis of cancer cells. It cooperates with Dock5, an exchange factor for the small GTPase Rac, for osteoclast activity to ensure the correct organization of podosomes. Tensin-3 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains
DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVGWPDLH
APPLDKMCTICKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKKFYDDK
VSALMQPSQKRYVQFLSGL
>gnl|CDD|350410 cd14562, PTP_tensin-2, protein tyrosine phosphatase-like domain of tensin-2. Tensin-2 (TNS2) is also called tensin-like C1 domain-containing phosphatase (TENC1) or C1 domain-containing phosphatase and tensin homolog (C1-TEN). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-2 is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It also modulates cell contractility and remodeling of collagen fibers through the DLC1, a RhoGAP that binds to tensins in focal adhesions. Tensin-2 may have phosphatase activity; it reduces AKT1 phosphorylation. It contains an N-terminal region with a zinc finger, a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains
DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQDFGWPDLH
APPLDKICSICKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKFCEDK
VATSLQPSQRRYISYFGGL
>gnl|CDD|350411 cd14563, PTP_auxilin_N, N-terminal protein tyrosine phosphatase-like domain of auxilin. Auxilin, also called auxilin-1 or DnaJ homolog subfamily C member 6 (DNAJC6), is a J-domain containing protein that recruits the ATP-dependent chaperone Hsc70 to newly budded clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles, driving the clathrin assembly#disassembly cycle. Mutations in the DNAJC6 gene, encoding auxilin, are associated with early-onset Parkinson's disease. Auxilin contains an N-terminal protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN, a phosphoinositide 3-phosphatase, and a C-terminal region with clathrin-binding and J domains
VASYTKGELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRV
SECSWPVRQAPSLHNLFAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLL
NAKRPGIGLWPSHRRYIGYICDL
>gnl|CDD|350412 cd14564, PTP_GAK, protein tyrosine phosphatase-like domain of cyclin-G-associated kinase. cyclin-G-associated kinase (GAK), also called auxilin-2, contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor
VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRV
SECGWPARRAPNLQNLYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMF
SMKRCPPGIWPSHKRYIEYMCDM
>gnl|CDD|350413 cd14565, DSP_MKP_classI, dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase. Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class I MKPs consist of DUSP1/MKP-1, DUSP2 (PAC1), DUSP4/MKP-2 and DUSP5. They are all mitogen- and stress-inducible nuclear MKPs. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain
PVEILPFLYLGSAYHASRREVLKALGITAVLNVSRNCPNHFEDHFQYKSIPVEDSHNADISSWFEEAIGF
IDKVKASGGRVLVHCQAGISRSATICLAYLMTTRRVRLNEAFDYVKQRRSVISPNFNFMGQLLQYESQ
>gnl|CDD|350414 cd14566, DSP_MKP_classII, dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase. Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class II MKPs consist of DUSP6/MKP-3, DUSP7/MKP-X and DUSP9/MKP-4, and are ERK-selective cytoplasmic MKPs. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain
PVEILPFLYLGNAKDSANIDLLKKYNIKYILNVTPNLPNTFEEDGGFKYLQIPIDDHWSQNLSAFFPEAI
SFIDEARSKKCGVLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKRKSNISPNFNFMGQLLDF
>gnl|CDD|350415 cd14567, DSP_DUSP10, dual specificity phosphatase domain of dual specificity protein phosphatase 10. Dual specificity protein phosphatase 10 (DUSP10), also called mitogen-activated protein kinase (MAPK) phosphatase 5 (MKP-5), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP10/MKP-5 coordinates skeletal muscle regeneration by negatively regulating mitochondria-mediated apoptosis. It is also an important regulator of intestinal epithelial barrier function and a suppressor of colon tumorigenesis. DUSP10/MKP-5 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain
LTPILPFLYLGNERDAQDIDTLQRLNIGYVLNVTTHLPLYHEGKGGFRYKRLPATDSNKQNLRQYFEEAF
EFIEEAHQSGKGVLVHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKRPIISPNLNFMGQLLEFEED
LNNGVTPRILTP
>gnl|CDD|350416 cd14568, DSP_MKP_classIII, dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase. Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class III MKPs consist of DUSP8, DUSP10/MKP-5 and DUSP16/MKP-7, and are JNK/p38-selective phosphatases, which are found in both the cell nucleus and cytoplasm. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain
PTRILPHLYLGSQRDVLDKDLMQRNGISYVLNVSNTCPKPDFIPDSHFLRIPVNDSYCEKLLPWLDKAVE
FIEKARASNKRVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRPTISPNFNFLGQLLEFEKKL
>gnl|CDD|350417 cd14569, DSP_slingshot_2, dual specificity phosphatase domain of slingshot homolog 2. Dual specificity protein phosphatase slingshot homolog 2 (SSH2), also called SSH-like protein 2, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. SSH2 has been identified as a target of protein kinase D1 that regulates cofilin phosphorylation and remodeling of the actin cytoskeleton during neutrophil chemotaxis. There are at least two human SSH2 isoforms reported: hSSH-2L (long) and hSSH-2. As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. In addition, hSSH-2L contains a long C-terminal tail while hSSH-2 does not
MDSPTQIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREIDNFFPGLFEYHNIRVYDEEATDLLAYWNDT
YKFISKAKKHGSKCLVHCKMGVSRSASTVIAYAMKEYGWNLDRAYDYVKERRTVTKPNPSFMRQLEEYQG
ILLA
>gnl|CDD|350418 cd14570, DSP_slingshot_1, dual specificity phosphatase domain of slingshot homolog 1. Dual specificity protein phosphatase slingshot homolog 1 (SSH1), also called SSH-like protein 1, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. SSH1 links NOD1 signaling to actin remodeling, facilitating the changes that leads to NF-kappaB activation and innate immune responses. There are at least two human SSH1 isoforms reported: hSSH-1L (long) and hSSH-1S (short). As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. They also contain C-terminal tails, differing in the lengths of the tail
MDKASLIFDHLYLGSEWNASNLEELQGSGVGYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNDA
YHFINKAKKNHSKCLVHCKMGVSRSASTVIAYAMKEFGWSLEKAYNFVKQKRSITRPNAGFMRQLLEYEG
ILDA
>gnl|CDD|350419 cd14571, DSP_slingshot_3, dual specificity phosphatase domain of slingshot homolog 3. Dual specificity protein phosphatase slingshot homolog 3 (SSH3), also called SSH-like protein 3, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. The Xenopus homolog (xSSH) is involved in the gastrulation movement. Mouse SSH3 dephosphorylates actin-depolymerizing factor (ADF) and cofilin but is dispensable for development. There are at least two human SSH3 isoforms reported: hSSH-3L (long) and hSSH-3. As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. In addition, hSSH-3L contains a C-terminal tail while hSSH-3 does not
MDRPSRIFPYLYLGSEWNAANLEELQRNRVSHILNVTREIDNFFPERFTYMNIRVYDEEATQLLPHWKET
HRFIEAARAQGTRVLVHCKMGVSRSASTVIAYAMKQYGWTLEQALRHVRERRPIVQPNPGFLRQLQTYQG
ILTA
>gnl|CDD|350420 cd14572, DUSP14, dual specificity protein phosphatase 14. dual specificity protein phosphatase 14 (DUSP14), also called mitogen-activated protein kinase (MAPK) phosphatase 6 (MKP-6) or MKP-1-like protein tyrosine phosphatase (MKP-L), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP14 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 dephosphorylates JNK, ERK, and p38 in vitro. It also directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses
SEGDLGGIAQITPSLYLSRGNVASNRHLLLSRGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPISLY
FDSVADKIHSVGRKHGATLVHCAAGVSRSATLCIAYLMKYHRVSLLEAYNWVKARRPVIRPNVGFWRQLI
DYERKLFGKS
>gnl|CDD|350421 cd14573, DUSP18_21, dual specificity protein phosphatases 18 and 21. This subfamily contains dual specificity protein phosphatase 18 (DUSP18), dual specificity protein phosphatase 21 (DUSP21), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP18, also called low molecular weight dual specificity phosphatase 20 (LMW-DSP20), is a catalytically active phosphatase with a preference for phosphotyrosine over phosphoserine/threonine oligopeptides in vitro. In vivo, it has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP21 is also called low molecular weight dual specificity phosphatase 21 (LMW-DSP21). Its gene has been identified as a potential therapeutic target in human hepatocellular carcinoma. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane
RLSRITESLYLSNGVAANNRTLLAANRITCVINVSLEVANGLPPGIEYLHVPVADSPDTRLRDYFDPIAD
KIHTVEARGGRTLLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTWVKSCRPIIRPNNGFWEQLIHYEFEL
FGKNTVHMITSPVGMIPD
>gnl|CDD|350422 cd14574, DUSP28, dual specificity protein phosphatase 28. Dual specificity protein phosphatase 28 (DUSP28), also called VHP, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It is an atypical DUSP that contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells. DUSP28 has an exceptionally low phosphatase activity due to the presence of bulky residues in the active site pocket resulting in low accessibility
LCRVTDSLFISNARAACNEELLAREGVTLCVNVSRQQPFPRAPRVSTLRVPVFDDPAEDLYRHFEQCADA
IEAAVRRGGKCLVYCKNGRSRSAAVCIAYLMKHRGLSLQDAFQVVKAARPVAEPNPGFWSQLQRYEEELQ
>gnl|CDD|350423 cd14575, DUPD1, dual specificity phosphatase and pro isomerase domain containing 1. Dual specificity phosphatase and pro isomerase domain containing 1 (DUPD1) was initially named as such because computational prediction appeared to encode a protein of 446 amino acids in length that included two catalytic domains: a proline isomerase and a dual specificity phosphatase (DUSP). However, it was subsequently shown that the true open reading frame only encompassed the DUSP domain and the gene product was therefore renamed DUSP27. This is distinct from inactive DUSP27. DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). DUPD1/DUSP27 has been shown to have catalytic activity with preference for phosphotyrosine over phosphothreonine and phosphoserine residues. It associates with the short form of the prolactin (PRL) receptor and plays a role in PRL-mediated MAPK inhibition in ovarian cells
FWKGGPKYTHVNEVWPGLYIGDEKTALDRYSLQKLGITHILNAAHGKWNVDTGAEYYKDMTIHYYGVEAD
DLPTFNLSQFFYSAAEFIHQALSDPHNKLLVHCVMGRSRSATLVLAYLMIYKNMTVVDAIEQVAQRRCIL
PNRGFLKQLRELDIQLAEER
>gnl|CDD|350424 cd14576, DSP_iDUSP27, dual specificity phosphatase-like domain of inactive dual specificity protein phosphatase 27. Inactive dual specificity protein phosphatase 27 (DUSP27) may play a role in myofiber maturation. It is a pseudophosphatase containing a substitution of the active site cysteine into a serine. It is a large protein of more than 1000 amino acids in length with an N-terminal dual specificity phosphatase-like domain
KDRLEAPRNAVDEVWPNVFIAEKSVAVNKGRLKRLGITHVLNAAHGTGVYTGPEFYSGMNIQYMGIEVDD
FPDVDISKHFRKGAEFLDEALLTYRGKVLVSSEMGISRSAVLVAAYLMIFHNMTIMEALMTLRKKRAIYP
NEGFLKQLRELNEKLLEER
>gnl|CDD|350425 cd14577, DUSP13B, dual specificity protein phosphatase 13 isoform B. Dual specificity protein phosphatase 13 isoform B (DUSP13B), also called testis- and skeletal-muscle-specific DSP (TMDP) or dual specificity phosphatase SKRP4, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP13B is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP13B inactivates MAPK activation in the order of selectivity, JNK = p38 _ ERK in cells. It may play a role in protection from external stress during spermatogenesis
LAELQRLLWVRRAPTGHVNEVWPNLYLGDAYAARDKSVLIQLGITHIVNAASGKFHVNTGPKFYRDMNID
YYGVEADDNPFFDLSVYFYPVARFIRAALSSPNGRVLVHCAMGISRSATLVLAFLMICEDLTLVDAIQTV
RAHRDICPNSGFLRQLRELDNRL
>gnl|CDD|350426 cd14578, DUSP26, dual specificity protein phosphatase 26. Dual specificity protein phosphatase 26 (DUSP26), also called mitogen-activated protein kinase (MAPK) phosphatase 8 (MKP-8) or low-molecular-mass dual-specificity phosphatase 4 (LDP-4), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP26 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is a brain phosphatase highly overexpressed in neuroblastoma and has also been identified as a p53 phosphatase, dephosphorylating phospho-Ser20 and phospho-Ser37 in the p53 transactivation domain
ADEVWPGLYLGDQDIAANRRELRRLGITHILNASHSKWRGGAEYYEGLNIRYLGIEAHDSPAFDMSIHFY
PAADFIHRALSQPGGKILVHCAVGVSRSATLVLAYLMIHHHMTLVEAIKTVKDHRGIIPNRGFLRQLLAL
DRRL
>gnl|CDD|350427 cd14579, DUSP3, dual specificity protein phosphatase 3. Dual specificity protein phosphatase 3 (DUSP3), also called vaccinia H1-related phosphatase (VHR), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP3 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It favors bisphosphorylated substrates over monophosphorylated ones, and prefers pTyr peptides over pSer/pThr peptides. Reported physiological substrates includes MAPKs ERK1/2, JNK, and p38, as well as STAT5, EGFR, and ErbB2. DUSP3 has been linked to breast and prostate cancer, and may also play a role in thrombosis
QELNDLLADGSGCYSLPSQHCNEVYPRIYVGNASVAQNIMRLQRLGITHVLNAAEGKSFMHVNTNAEFYE
DTGITYHGIKANDTQHFNLSAYFEEAADFIDKALAQKNGRVLVHCREGYSRSPTLVIAYLMLRQKMDVKS
ALSTVRQKREIGPNDGFLKQLCQLNDKL
>gnl|CDD|350428 cd14580, DUSP13A, dual specificity protein phosphatase 13 isoform A. Dual specificity protein phosphatase 13 isoform A (DUSP13A), also called branching-enzyme interacting DSP or muscle-restricted DSP (MDSP), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP13A is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP13A also functions as a regulator of apoptosis signal-regulating kinase 1 (ASK1), a MAPK kinase kinase, by interacting with its N-terminal domain and inducing ASK1-mediated apoptosis through the activation of caspase-3. This function is independent of phosphatase activity
VDEVWPNLFLGDLATAHNRFGLWKLGITHVLNAAHGKLFCQGGDDFYGTSVDYYGVPANDLPDFDISPYF
YSAAEFIHRALNTPGAKVLVHCAVGVSRSATLVLAYLMIYHQLSLVQAIKTVKERRWIFPNRGFLKQLRK
LDQQL
>gnl|CDD|350429 cd14581, DUSP22, dual specificity protein phosphatase 22. Dual specificity protein phosphatase 22 (DUSP22), also called JNK-stimulatory phosphatase-1 (JSP-1), low molecular weight dual specificity phosphatase 2 (LMW-DSP2), mitogen-activated protein kinase phosphatase x (MKP-x) or VHR-related MKPx (VHX), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP22 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP22 negatively regulates the estrogen receptor-alpha-mediated signaling pathway and the IL6-leukemia inhibitory factor (LIF)-STAT3-mediated signaling pathway. It also regulates cell death by acting as a scaffold protein for the ASK1-MKK7-JNK signal transduction pathway independently of its phosphatase activity
GNGMNKVLPGLYLGNFKDARDREQLSKNNITHILSVHDSARPMLEGMTYLCIPAADSPSQNLTQHFKESI
KFIHECRLRGEGCLVHCLAGVSRSVTLVVAYIMTVTDFGWEDALSAVKAARSCANPNMGFQRQLQEFEKH
EVHQYRQWL
>gnl|CDD|350430 cd14582, DSP_DUSP15, dual specificity phosphatase domain of dual specificity protein phosphatase 15. Dual specificity protein phosphatase 15 (DUSP15), also called Vaccinia virus VH1-related dual-specific protein phosphatase Y (VHY) or VH1-related member Y, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). DUSP15 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is highly expressed in the testis and is located in the plasma membrane in a myristoylation-dependent manner. It may be involved in the regulation of meiotic signal transduction in testis cells. It is also expressed in the brain and has been identified as a regulator of oligodendrocyte differentiation. DUSP15 contains an N-terminal catalytic dual specificity phosphatase domain and a short C-terminal tail
MGNGMTKVLPGLYLGNFIDAKDLEQLSRNKITHIISIHESPQPLLQDITYLRIPLPDTPEAPIKKHFKEC
ISFIHQCRLNGGNCLVHCLAGISRSTTIVVAYVMAVTELSWQEVLEAIRAVRPIANPNPGFKQQLEEFGW
AAARKL
>gnl|CDD|350431 cd14583, PTP-MTMR7, protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 7. Myotubularin related phosphoinositide phosphatase 7 (MTMR7) is enzymatically active and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. In neuronal cells, MTMR7 forms a complex with catalytically inactive MTMR9 and dephosphorylates phosphatidylinositol 3-phosphate and Ins(1,3)P2
LKAEYNRMGLPNSLWQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYYCKDNNAS
ICRSSQPLSGFSARCLEDEQMLQAIRKANPGSDFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFI
GIENIHVMRNSLQKMLEVCELRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDG
WDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKFNHRYGHLDGDPKEVSPVIDQFIECVWQLME
QFPCAFEFNERFLIHIHHHIYS
>gnl|CDD|350432 cd14584, PTP-MTMR8, protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 8. Myotubularin related phosphoinositide phosphatase 8 (MTMR8) is enzymatically active and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. MTMR8 forms a complex with catalytically inactive MTMR9 and preferentially dephosphorylates PtdIns(3)P; the MTMR8/R9 complex inhibits autophagy. In zebrafish, it cooperates with PI3K to regulate actin filament modeling and muscle development
GWKLIDLKVDFQRMGIPNDYWEITDANKNYEICSTYPPELVVPKSASKATVVGSSKFRSRGRFPVLSYLY
KENNAAICRCSQPLSGFSARCVEDEQMLQAISKANPGSPFMYVVDTRPKLNAMANRAAGKGYENEDNYSN
IRFQFIGIENIHVMRSSLQKLLEVCEMKSPSMSDFLTGLENSGWLRHIKAVMDAGVFLAKAVKEEKASVL
VHCSDGWDRTAQVCSLASLLLDPFYRTIKGLMVLIEKEWISMGHKFSQRCGHLDGDPKEVSPVFTQFLEC
VWQLMEQFPCAFEFNEHFLLEIHDHVFS
>gnl|CDD|350433 cd14585, PTP-MTMR6, protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 6. Myotubularin related phosphoinositide phosphatase 6 is enzymatically active and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. MTMR6 forms a complex with catalytically inactive MTMR9 and preferentially dephosphorylates PtdIns(3,5)P(2); the MTMR6/R9 complex serves to inhibit stress-induced apoptosis
LAEEYKRMGVPNDYWQLSDVNRDYKICDTYPRDLYVPITASKPIIVGSSKFRSKGRFPVLSYYHQEKKAA
ICRCSQPLSGFSARCLEDEHMLQAISKANPNNRYMYVMDTRPKLNAMANRAAGKGYENEDNYSNIRFQFV
GIENIHVMRSSLQKLLEVCGTKALSVNDFLSGLESSGWLRHIKAVLDAAVFLAKAVAVEGASVLVHCSDG
WDRTAQVCSLGSLLLDPYYRTIKGFMVLIEKDWISFGHKFSDRCGQLDGDPKEISPVFTQFLECVWQLTE
QFPRAFEFSEAFLLQIHEHIHS
>gnl|CDD|350434 cd14586, PTP-MTMR3, protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 3. Myotubularin related phosphoinositide phosphatase 3 (MTMR3), also known as FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1) or Zinc finger FYVE domain-containing protein 10 (ZFYVE10), is enzymatically active and contains a C-terminal FYVE domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. Together with phosphoinositide 5-kinase PIKfyve, phosphoinositide 3-phosphatase MTMR3 constitutes a phosphoinositide loop that produces PI(5)P via PI(3,5)P2 and regulates cell migration
GFDMQNAWRISNINEKYKLCGSYPQELIVPAWITDKELESVASFRSWKRIPAVVYRHQSNGAVIARCGQP
EVSWWGWRNADDEHLVQSVAKACASDSSSCKSVLMTGNCSRDFPNGGDLSDVEFDSSMSNASGVESLAIQ
PQKLLILDARSYAAAVANRAKGGGCECPEYYPNCEVVFMGMANIHSIRKSFQSLRLLCTQMPDPANWLSA
LESTKWLQHLSMLLKSALLVVHAVDRDQRPVLVHCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETE
WLDFGHKFADRCGHGENSDDLNERCPVFLQWLDCVHQ
>gnl|CDD|350435 cd14587, PTP-MTMR4, protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 4. Myotubularin related phosphoinositide phosphatase 4 (MTMR4), also known as FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2) or zinc finger FYVE domain-containing protein 11 (ZFYVE11), is enzymatically active and contains a C-terminal FYVE domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. MTMR4 localizes at the interface of early and recycling endosomes to regulate trafficking through this pathway. It plays a role in bacterial pathogenesis by stabilizing the integrity of bacteria-containing vacuoles
NVWRVSEINSNYKLCSSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAVIARCSQPEISWW
GWRNADDEYLVTSIAKACALDPGTRAPGGSPSKGNSDGSDASDTDFDSSLTACSAVESGAAPQKLLILDA
RSYTAAVANRAKGGGCECEEYYPNCEVMFMGMANIHSIRNSFQYLRAVCSQMPDPGNWLSALESTKWLQH
LSVMLKAAVLVASAVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFG
DRCGHQENVEDQNEQCPVFLQWLDCVHQ
>gnl|CDD|350436 cd14588, PTP-MTMR5, protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 5. Myotubularin related phosphoinositide phosphatase 5 (MTMR5), also known as SET binding factor 1 (SBF1), is enzymatically inactive and contains a variety of other domains, including a DENN and a PH-like domain. Mutations in the MTMR5 gene cause Charcot-Marie-tooth disease type 4B3. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR5 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket. It interacts with MTMR2, an active myotubularin related phosphatidylinositol phosphatase, regulates its enzymatic activity and subcellular location
FRISTVNRMYAVCRSYPGLLIVPQSIQDNTIQRISRCYRQNRFPVVCWRNSRTKAVLLRSGGLHGKGVVG
LFKSQNAPAAGQSQTDSTSLEQEKYLQAVINSMPRYADASGRNTLSGFRAALYIIGDKSQLKGVKQDPLQ
QWEVVPIEVFDVRQVKASFKKLMKACVPSCPSTDPSQTYLRTLEESEWLSQLHKLLQVSVLVVELLDSGS
SVLVSLEDGWDITTQVVSLVQLLSDPYYRTIEGFRLLVEKEWLSFGHRFSHRGAQTLASQSSGFTPVFLQ
FLDCVHQIHLQ
>gnl|CDD|350437 cd14589, PTP-MTMR13, protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 13. Myotubularin related phosphoinositide phosphatase 13 (MTMR13), also known as SET binding factor 2 (SBF2), is enzymatically inactive and contains a variety of other domains, including a DENN and a PH-like domain. Mutations in MTMR13 causes Charcot-Marie-Tooth type 4B2, a severe childhood-onset neuromuscular disorder, characterized by demyelination and redundant loops of myelin known as myelin outfoldings, a similar phenotype as mutations in MTMR2. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR13 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket. It is believed to interact with MTMR2 and stimulate its phosphatase activity. It is also a guanine nucleotide exchange factor (GEF) which may activate RAB28, promoting the exchange of GDP to GTP and converting inactive GDP-bound Rab proteins into their active GTP-bound form
FRITAVNRMYSLCRSYPGLLVVPQSVQDSSLQKVARCYRHNRLPVVCWKNSKTKAVLLRSGGFHGKGVVG
LFKSQNPHSAAPASSESSSSIEQEKYLQALLNAISVHQKMNGNSTLLQSQLLKRQAALYIFGEKSQLRGF
KLDFALNCEFVPVEFHDIRQVKASFKKLMRACVPSTIPTDSEVTFLKALGESEWFLQLHRIMQLAVVISE
LLESGSSVMVCLEDGWDITTQVVSLVQLLSDPFYRTLEGFQMLVEKEWLSFGHKFSQRSNLTPNSQGSGF
APIFLQFLDCVHQIHNQ
>gnl|CDD|350438 cd14590, PTP-MTMR2, protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 2. Myotubularin related phosphoinositide phosphatase 2 (MTMR2) is enzymatically active and contains an additional N-terminal PH-GRAM domain and C-terminal coiled-coiled domain and PDZ binding site. Mutations in MTMR2 causes Charcot-Marie-Tooth type 4B1, a severe childhood-onset neuromuscular disorder, characterized by demyelination and redundant loops of myelin known as myelin outfoldings, a similar phenotype as mutations in MTMR13. MTMR13, an inactive phosphatase, is believed to interact with MTMR2 and stimulate its phosphatase activity. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively
DEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFDA
RPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEESHWLSNLESTHWLEH
IKLILAGALRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQ
LRVGHGDKNHADADRSPVFLQFIDCVWQMTRQFPTAFEFNEYFLITILDHLY
>gnl|CDD|350439 cd14591, PTP-MTM1, protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1. Myotubularin phosphoinositide phosphatase 1 (MTM1), also called myotubularin, is enzymatically active and contains an N-terminal PH-GRAM domain and C-terminal coiled-coiled domain and PDZ binding site. Mutations in MTM1 cause X-linked myotubular myopathy. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively
NRIPVLSWIHPENQAVIMRCSQPLVGMSGKRNKDDEKYLDIIREANGQTSKLTIYDARPSVNAVANKATG
GGYEGDDAYQNAELVFLDIHNIHVMRESLKKLKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVAD
KVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGHGDKNHADA
DRSPIFLQFIDCVWQMSKQFPTAFEFNEQFLITILDHLY
>gnl|CDD|350440 cd14592, PTP-MTMR1, protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 1. Myotubularin-related phosphoinositide phosphatase 1 (MTMR1) is enzymatically active and contains an N-terminal PH-GRAM domain, a C-terminal coiled-coiled domain and a PDZ binding site. MTMR1 is associated with myotonic dystrophy. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively
GRVPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYLQTIMDANAQSHKLIIFDARQNSVADTNKTKG
GGYESESAYPNAELVFLEIHNIHVMRESLRKLKEIVYPSIDEARWLSNVDGTHWLEYIRMLLAGAVRIAD
KIESGKTSVVVHCSDGWDRTAQLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGHGDDNHADA
DRSPIFLQFIDCVWQMTRQFPSAFEFNELFLITILDHLY
>gnl|CDD|350441 cd14593, PTP-MTMR10, protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 10. Myotubularin related phosphoinositide phosphatase 10 (MTMR10) is enzymatically inactive and contains an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR10 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket
RRIPLWCWNHPNGSALVRMANIKDLLQQRKIDQRICNAITRSHPLRSDVYKSDLDKTLPNIQEIQAAFVK
LKQLCVNEPFEETEEKWLSSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLVQ
VMLDPYFRTITGFQSLIQKEWVMAGYRFLDRCNHLKKSSKKESPLFLLFLDCVWQ
>gnl|CDD|350442 cd14594, PTP-MTMR12, protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 12. Myotubularin related phosphoinositide phosphatase 12 (MTMR12), also called phosphatidylinositol 3 phosphate 3-phosphatase adapter subunit (3-PAP), is enzymatically inactive and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR12 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket. It functions as an adapter for the catalytically active myotubularin to regulate its intracellular location
RGIPIWCWSCHNGCALLKMSALPKEQDDVALQDQKSFLDRIYKTLSRPPYESVKTEDLSASLPSLQEIQT
AYNRFKQLFLIDNSTDFWDTDVKWFSSLESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCC
VISSLVQIMMDPYCRTKSGFQSLIQKEWVMGGHCFLDRCNHLRQNDKEEVPVFLLFLDCVWQL
>gnl|CDD|350443 cd14595, PTP-MTMR11, protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 11. Myotubularin related phosphoinositide phosphatase 11 (MTMR11), also called cisplatin resistance-associated protein (hCRA) in humans, is enzymatically inactive and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR11 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket
GRIPRWCWHHPGGSDLLRMAGFYTNSDPEKEDIRSVELLLQAGHSQCVIVDTSEELPSPADIQLAYLKLR
TLCLPDISVSVSDEKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQL
LSDPHARTISGFQSLVQKEWVVAGHPFLQRLNLTRESDKEESPVFLLFLDCVWQL
>gnl|CDD|350444 cd14596, PTPc-N20, catalytic domain of tyrosine-protein phosphatase non-receptor type 20. Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization
YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPM
ELENYQLRLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTG
PIVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ
>gnl|CDD|350445 cd14597, PTPc-N13, catalytic domain of tyrosine-protein phosphatase non-receptor type 13. Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane
KENRKKNRYKNILPYDTTRVPLGDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTV
IAMMTQEVEGGKIKCQRYWPEILGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFT
AWPDHDTPSQPEQLLTFISYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMR
LQRHGMVQTEDQYIFCYQVILYVL
>gnl|CDD|350446 cd14598, PTPc-N21, catalytic domain of tyrosine-protein phosphatase non-receptor type 21. Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence
YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHN
TVTYGRFKITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRR
HTNSTIDPKSPNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTF
VYKVLIQFLK
>gnl|CDD|350447 cd14599, PTPc-N14, catalytic domain of tyrosine-protein phosphatase non-receptor type 14. Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence
RCKTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINA
SHIKVTVGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATY
GKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNS
MLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQ
VLIQFLK
>gnl|CDD|350448 cd14600, PTPc-N3, catalytic domain of tyrosine-protein phosphatase non-receptor type 3. Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation
EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGNEDYINASY
VNMEIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGF
RVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENEPVLV
HCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE
>gnl|CDD|350449 cd14601, PTPc-N4, catalytic domain of tyrosine-protein phosphatase non-receptor type 4. Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4
DYINANYINMEIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSG
SSSYGGFQVTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRA
GKDEPVVVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVY
EE
>gnl|CDD|350450 cd14602, PTPc-N22, catalytic domain of tyrosine-protein phosphatase non-receptor type 22. Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus
KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIV
MACMEFEMGKKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDH
DVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMR
TQRPSLVQTKEQYELVYNAVIELF
>gnl|CDD|350451 cd14603, PTPc-N18, catalytic domain of tyrosine-protein phosphatase non-receptor type 18. Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway
AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVD
GSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKR
LNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRT
GVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF
>gnl|CDD|350452 cd14604, PTPc-N12, catalytic domain of tyrosine-protein phosphatase non-receptor type 12. Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase
EQVEILKKFIERVQAMKSTDHNGEDNFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFD
HSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRK
KCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILD
MISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKE
QYELVHRAIAQLFEKQL
>gnl|CDD|350453 cd14605, PTPc-N11, catalytic domain of tyrosine-protein phosphatase non-receptor type 11. Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties
ENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDF
WRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNT
ERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIRE
KGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIET
>gnl|CDD|350454 cd14606, PTPc-N6, catalytic domain of tyrosine-protein phosphatase non-receptor type 6. Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties
KQEVKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKNQLLGPDENAKTYI
ASQGCLEATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKL
RTLQVSPLDNGELIREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGT
IIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIET
>gnl|CDD|350455 cd14607, PTPc-N2, catalytic domain of tyrosine-protein phosphatase non-receptor type 2. Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis
QPLYLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQRSYILTQG
PLPNTCCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYYTVH
LLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFS
LVDTCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV
>gnl|CDD|350456 cd14608, PTPc-N1, catalytic domain of tyrosine-protein phosphatase non-receptor type 1. Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor
WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQ
GPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTV
RQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTF
CLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWK
>gnl|CDD|350457 cd14609, R-PTP-N, PTP-like domain of receptor-type tyrosine-protein phosphatase N. Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion
HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRS
DYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLY
HIYEVNLVSEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRS
CPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNA
I
>gnl|CDD|350458 cd14610, R-PTP-N2, PTP-like domain of receptor-type tyrosine-protein phosphatase N2. Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain
TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHS
HSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSN
LYHIYEVNLVSEHIWCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRG
RSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV
NAI
>gnl|CDD|350459 cd14611, R-PTPc-R, catalytic domain of receptor-type tyrosine-protein phosphatase R. Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia
TKNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSP
VIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHK
TPDSAQPLLQLMLDVEEDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVD
RGGMVQTSEQYEFVHH
>gnl|CDD|350460 cd14612, PTPc-N7, catalytic domain of tyrosine-protein phosphatase non-receptor type 7. Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia
PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDGKEKAYIATQGPML
NTVSDFWEMVWQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEE
SRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKD
TGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLALY
>gnl|CDD|350461 cd14613, PTPc-N5, catalytic domain of tyrosine-protein phosphatase non-receptor type 5. Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome
FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEK
VYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRL
RLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFI
ATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVLSLY
>gnl|CDD|350462 cd14614, R-PTPc-O, catalytic domain of receptor-type tyrosine-protein phosphatase O. Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer
DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRND
FWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQ
DVMHFNYTAWPDHGVPTANAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHE
FVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQLM
>gnl|CDD|350463 cd14615, R-PTPc-J, catalytic domain of receptor-type tyrosine-protein phosphatase J. Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2
NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVML
TKCVEQGRTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGV
PETTDLLINFRHLVREYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHR
PLMVQTEDQYVFLNQCALD
>gnl|CDD|350464 cd14616, R-PTPc-Q, catalytic domain of receptor-type tyrosine-protein phosphatase Q. Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates
NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVM
LTQCFEKGRIRCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHG
VPESSAPLIHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERM
CMVQNLAQYIFLHQ
>gnl|CDD|350465 cd14617, R-PTPc-B, catalytic domain of receptor-type tyrosine-protein phosphatase B. Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis
NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVM
VTQCVEKGRVKCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPD
HGVPETTQSLIQFVRTVRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLR
LHRVHMVQTECQYVYLHQ
>gnl|CDD|350466 cd14618, R-PTPc-V, catalytic domain of receptor-type tyrosine-protein phosphatase V. Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene
NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIM
LTVGMENGRVLCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDH
GIPESTSSLMAFRELVREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRM
HRYLMIQTLSQYIFLHSCIL
>gnl|CDD|350467 cd14619, R-PTPc-H, catalytic domain of receptor-type tyrosine-protein phosphatase H. Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility
NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVM
LTNCMEAGRVKCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDH
GVPSSTDTLLAFRRLLRQWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRE
NRPLMVQTESQYVFLHQCILDFL
>gnl|CDD|350468 cd14620, R-PTPc-E-1, catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1. Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1)
YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLT
NLKERKEEKCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAPRLVTQLHFTSWPDF
GVPFTPIGMLKFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQR
PQMVQTDMQYSFIYQALLE
>gnl|CDD|350469 cd14621, R-PTPc-A-1, catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1. Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1)
TNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVH
LTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQY
WPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKF
LKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVF
IYQALLEHYLYGDTEL
>gnl|CDD|350470 cd14622, R-PTPc-E-2, catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2. Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2)
DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHG
EITIEIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNH
PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF
>gnl|CDD|350471 cd14623, R-PTPc-A-2, catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2. Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2)
RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVML
TELEERGQEKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGI
PSDGKGMINIIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRP
HMVQTLEQYEFCYKVVQE
>gnl|CDD|350472 cd14624, R-PTPc-D-1, catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1. Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1)
HPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIE
GIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRG
TETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNP
PDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV
TCGN
>gnl|CDD|350473 cd14625, R-PTPc-S-1, catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1. Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1)
HPPIPISELAEHTERLKANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIE
GIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRG
TETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNP
PDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV
AC
>gnl|CDD|350474 cd14626, R-PTPc-F-1, catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1. Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1)
SDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSD
YINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGM
IQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPM
VVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC
>gnl|CDD|350475 cd14627, R-PTP-S-2, PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2. Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG
NTEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRV
CLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQ
YWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ
VHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFC
YQAALEYLGS
>gnl|CDD|350476 cd14628, R-PTP-D-2, PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2. Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG
TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVC
LQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQY
WPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQV
HKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCY
RAALEYLGSFDH
>gnl|CDD|350477 cd14629, R-PTP-F-2, PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2. Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG
NTEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRV
CLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQ
YWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQ
VHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLC
YRAALEYLGSF
>gnl|CDD|350478 cd14630, R-PTPc-T-1, catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1. Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain
DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQEN
SASVVMVTNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTS
WPDHGVPCYATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVREL
RAQRVNMVQTEEQYVFVHDAILEACLC
>gnl|CDD|350479 cd14631, R-PTPc-K-1, catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1. Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain
RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKC
YKYWPDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIR
RVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH
DAILEACL
>gnl|CDD|350480 cd14632, R-PTPc-U-1, catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1. Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain
YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDI
KITLLKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVV
VHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC
>gnl|CDD|350481 cd14633, R-PTPc-M-1, catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1. Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain
DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDY
INGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIK
VTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVV
HCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL
>gnl|CDD|350482 cd14634, R-PTPc-T-2, PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2. Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain
YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQ
VEFVSADIDEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGR
EGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE
>gnl|CDD|350483 cd14635, R-PTPc-M-2, PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2. Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain
YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQ
VEFVSADLEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGG
EGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE
>gnl|CDD|350484 cd14636, R-PTPc-K-2, PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2. Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain
YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQ
VECMSCSMDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEG
EGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE
>gnl|CDD|350485 cd14637, R-PTPc-U-2, PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2. Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain
YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYG
PMEVEFVSGSADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRES
GEGRTVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE
>gnl|CDD|350486 cd14638, DSP_DUSP1, dual specificity phosphatase domain of dual specificity protein phosphatase 1. Dual specificity protein phosphatase 1 (DUSP1), also called mitogen-activated protein kinase (MAPK) phosphatase 1 (MKP-1), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. Human MKP-1 dephosphorylates MAPK1/ERK2, regulating its activity during the meiotic cell cycle. Although initially MKP-1 was considered to be ERK-specific, it has been shown that MKP-1 also dephosphorylates both JNK and p38 MAPKs. DUSP1/MKP-1 is involved in various functions, including proliferation, differentiation, and apoptosis in normal cells. It is a central regulator of a variety of functions in the immune, metabolic, cardiovascular, and nervous systems. It contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain
PVEILPFLYLGSAYHASRKDMLDTLGITALINVSANCPNHFEGHYQYKSIPVEDNHKADISSWFNEAIDF
IDSVKNAGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQVL
APSCSAEAGSP
>gnl|CDD|350487 cd14639, DSP_DUSP5, dual specificity phosphatase domain of dual specificity protein phosphatase 5. Dual specificity protein phosphatase 5 (DUSP5) functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (MKPs), it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP5 preferentially dephosphorylates extracellular signal-regulated kinase (ERK), and is involved in ERK signaling and ERK-dependent inflammatory gene expression in adipocytes. It also plays a role in regulating pressure-dependent myogenic cerebral arterial constriction, which is crucial for the maintenance of constant cerebral blood flow to the brain. DUSP5 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain
PVEILPFLYLGSAYHASKCEFLANLHITALLNVSRRSSEACKGQYHYKWIPVEDSHTADISSHFQEAIDF
IDCVRRAGGKVLVHCEAGISRSPTICMAYLMKTKRFRLEEAFDYIKQRRSLISPNFGFMGQLLQYESE
>gnl|CDD|350488 cd14640, DSP_DUSP4, dual specificity phosphatase domain of dual specificity protein phosphatase 4. Dual specificity protein phosphatase 4 (DUSP4), also called mitogen-activated protein kinase (MAPK) phosphatase 2 (MKP-2), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP4 regulates either ERK or c-JUN N-terminal kinase (JNK), depending on the cell type. It dephosphorylates nuclear JNK and induces apoptosis in diffuse large B cell lymphoma (DLBCL) cells. It acts as a negative regulator of macrophage M1 activation and inhibits inflammation during macrophage-adipocyte interaction. It has been linked to different aspects of cancer: it may have a role in the development of ovarian cancers, oesophagogastric rib metastasis, and pancreatic tumours; it may also be a candidate tumor suppressor gene, with its deletion implicated in breast cancer, prostate cancer, and gliomas. DUSP4/MKP-2 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain
PVEILPFLYLGSAYHAARRDMLDALGITALLNVSSDCPNHFEGHYQYKCIPVEDNHKADISSWFMEAIEY
IDSVKDCNGRVLVHCQAGISRSATICLAYLMMKKRVRLEEAFEFVKQRRSIISPNFSFMGQLLQFESQVL
A
>gnl|CDD|350489 cd14641, DSP_DUSP2, dual specificity phosphatase domain of dual specificity protein phosphatase 2. Dual specificity protein phosphatase 2 (DUSP2), also called dual specificity protein phosphatase PAC-1, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (MKPs), it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP2 can preferentially dephosphorylate ERK1/2 and p38, but not JNK in vitro. It is predominantly expressed in hematopoietic tissues with high T-cell content, such as thymus, spleen, lymph nodes, peripheral blood and other organs such as the brain and liver. It has a critical and positive role in inflammatory responses. DUSP2 mRNA and protein are significantly reduced in most solid cancers including breast, colon, lung, ovary, kidney and prostate, and the suppression of DUSP2 is associated with tumorigenesis and malignancy. DUSP2 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain
QGGPVEILPFLFLGSAHHSSRRETLESLGITAVLNVSSSCPNYFEGQFQYKSIPVEDSHMADISAWFQEA
IDFIDSVKNSGGRVLVHCQAGISRSATICLAYLIQSQRVRLDEAFDFVKQRRGVISPNFSFMGQLLQFET
QVLC
>gnl|CDD|350490 cd14642, DSP_DUSP6, dual specificity phosphatase domain of dual specificity protein phosphatase 6. Dual specificity protein phosphatase 6 (DUSP6), also called mitogen-activated protein kinase (MAPK) phosphatase 3 (MKP-3) or dual specificity protein phosphatase PYST1, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class II subfamily and is an ERK-selective cytoplasmic MKP. DUSP6/MKP-3 plays an important role in obesity-related hyperglycemia by promoting hepatic glucose output. MKP-3 deficiency attenuates body weight gain induced by a high-fat diet, protects mice from developing obesity-related hepatosteatosis, and reduces adiposity, possibly by repressing adipocyte differentiation. It also contributes to p53-controlled cellular senescence. It contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain
SFPVEILPYLYLGCAKDSTNLDVLEEFGIKYILNVTPNLPNLFENAGEFKYKQIPISDHWSQNLSQFFPE
AISFIDEARGKNCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFE
RTL
>gnl|CDD|350491 cd14643, DSP_DUSP7, dual specificity phosphatase domain of dual specificity protein phosphatase 7. Dual specificity protein phosphatase 7 (DUSP7), also called mitogen-activated protein kinase (MAPK) phosphatase X (MKP-X) or dual specificity protein phosphatase PYST2, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class II subfamily and is an ERK-selective cytoplasmic MKP. DUSP7 has been shown as an essential regulator of multiple steps in oocyte meiosis. Due to alternative promoter usage, the PYST2 gene gives rise to two isoforms, PYST2-S and PYST2-L. PYST2-L is over-expressed in leukocytes derived from AML and ALL patients as well as in some solid tumors and lymphoblastoid cell lines; it plays a role in cell-crowding. It contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain
SQPAFPVQILPYLYLGCAKDSTNLDVLGKYGIKYILNVTPNLPNMFEHDGEFKYKQIPISDHWSQNLSQF
FPEAISFIDEARSKKCGILVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDFVKRKKSNISPNFNFMGQLL
DFERTLGLN
>gnl|CDD|350492 cd14644, DSP_DUSP9, dual specificity phosphatase domain of dual specificity protein phosphatase 9. Dual specificity protein phosphatase 9 (DUSP9), also called mitogen-activated protein kinase (MAPK) phosphatase 4 (MKP-4), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class II subfamily and is an ERK-selective cytoplasmic MKP. DUSP9 is a mediator of bone morphogenetic protein (BMP) signaling to control the appropriate ERK activity critical for the determination of embryonic stem cell fate. Down-regulation of DUSP9 expression has been linked to severe pre-eclamptic placenta as well as cancers such as hepatocellular carcinoma. DUSP9 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain
SFPVQILPNLYLGSARDSANLETLAKLGIRYILNVTPNLPNFFEKNGDFHYKQIPISDHWSQNLSQFFPE
AIEFIDEALSQNCGVLVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDLVKRKKSNISPNFNFMGQLLDFE
KSLGL
>gnl|CDD|350493 cd14645, DSP_DUSP8, dual specificity phosphatase domain of dual specificity protein phosphatase 8. Dual specificity protein phosphatase 8 (DUSP8), also called DUSP hVH-5 or M3/6, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP8 controls basal and acute stress-induced ERK1/2 signaling in adult cardiac myocytes, which impacts contractility, ventricular remodeling, and disease susceptibility. It also plays a role in decreasing ureteric branching morphogenesis by inhibiting p38MAPK. DUSP8 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain
SQPCLPVANVGPTRILPHLYLGSQKDVLNKDLMAQNGITYVLNASNSCPKPDFICESHFMRIPVNDNYCE
KLLPWLDKSIEFIDKAKVSNCRVIVHCLAGISRSATIAIAYIMKTMGLSSDDAYRFVKDRRPSISPNFNF
LGQLLEYEKSL
>gnl|CDD|350494 cd14646, DSP_DUSP16, dual specificity phosphatase domain of dual specificity protein phosphatase 16. Dual specificity protein phosphatase 16 (DUSP16), also called mitogen-activated protein kinase (MAPK) phosphatase 7 (MKP-7), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP16/MKP-7 plays an essential role in perinatal survival and selectively controls the differentiation and cytokine production of myeloid cells. It is acetylated by Mycobacterium tuberculosis Eis protein, which leads to the inhibition of JNK-dependent autophagy, phagosome maturation, and ROS generation, and thus, initiating suppression of host immune responses. DUSP16/MKP-7 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain
IGPTRILPHLYLGCQRDVLNKELMQQNGIGYVLNASNTCPKPDFIPESHFLRVPVNDSFCEKILPWLDKS
VDFIEKAKASNGRVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPTISPNFNFLGQLLDFEK
KIKNQ
>gnl|CDD|271236 cd14651, ZIP_Put3, Leucine zipper Dimerization domain of transcription factor Put3. Put3p activates the transcription of PUT1 and PUT2 genes in the presence of proline, allowing yeast cells to use proline as a nitrogen source. These genes encode for proteins that convert proline to glutamate, which is a metabolically more useful form of nitrogen. Put3p is a member of the Gal4p family of transcriptional activators which contain an N-terminal DNA-binding domain with a Zn2Cys6 binuclear cluster that interact with CCG triplets and a leucine zipper-like heptad repeat that dimerizes. Dimerization allows binding of targets which contain two CCG motifs oriented in an inverted (CGG-CCG), direct (CCG-CCG), or everted (CCG-CGG) manner
VVSTKYLQQLQKDLNDKTEENNRLKALLLEK
>gnl|CDD|271237 cd14653, ZIP_Gal4p-like, Leucine zipper Dimerization domain of Gal4p-like transcription factors. The Gal4p family of transcriptional activators contain an N-terminal DNA-binding domain with a Zn2Cys6 binuclear cluster that interact with CCG triplets and a leucine zipper-like heptad repeat that dimerizes. Dimerization allows binding of targets which contain two CCG motifs oriented in an inverted (CGG-CCG), direct (CCG-CCG), or everted (CCG-CGG) manner. Included in this family are Saccharomyces cerevisiae Gal4p, Hap1p, Put3p, Ppr1p and Sip4p, Neurospora crassa acu-15, and Colletotrichum acutatum Nir1, among others. Gal4p functions in the induction of GAL genes in the presence of galactose; GAL proteins are responsible for the transport of galactose into the cell and for its metabolism through the glycolytic pathway. Hap1p promotes transcription of genes required for respiration and controlling oxidative damage in response to heme. Put3p activates the transcription of the PUT1 and PUT2 genes in the presence of proline, allowing yeast cells to use proline as a nitrogen source. Ppr1p activates transcription of the URA1, URA3, and URA4 genes, which encode enzymes involved in the regulation of pyrimidine levels. Sip4p activates target genes under conditions of glucose deprivation. Acu-15 is involved in regulating acetate utilization while Nir1 plays a role during nitrogen-starvation conditions
PRGYIEELEERVARLEQLLRELEP
>gnl|CDD|271238 cd14654, ZIP_Gal4, Leucine zipper Dimerization domain of transcription factor Gal4 and similar fungal proteins. Gal4p is one of several GAL proteins required for the growth of yeast on galactose; GAL proteins are responsible for the transport of galactose into the cell and for its metabolism through the glycolytic pathway. Gal4p functions in the induction of GAL genes in the presence of galactose through an upstream activating sequence (UAS) present in their promoters. The Gal4p family of transcriptional activators contain an N-terminal DNA binding domain with a Zn2Cys6 binuclear cluster that interact with CCG triplets and a leucine zipper-like heptad repeat that dimerizes. Dimerization allows binding of targets which contain two CCG motifs oriented in an inverted (CGG-CCG), direct (CCG-CCG), or everted (CCG-CGG) manner
TRAHLTEVENRLEKLEALLRQLLPGVDIDELLESPSELEDDDPLDDP
>gnl|CDD|271239 cd14655, ZIP_Hap1, Leucine zipper Dimerization domain of transcription factor Hap1 and similar fungal proteins. Hap1p mediates oxygen sensing and heme signaling in yeast. In response to heme, it promotes transcription of genes required for respiration and controlling oxidative damage. It is a member of the Gal4/Gal4p family of transcriptional activators which contain an N-terminal DNA binding domain with a Zn2Cys6 binuclear cluster that interact with CCG triplets and a leucine zipper-like heptad repeat that dimerizes. Dimerization allows binding of targets which contain two CCG motifs oriented in an inverted (CGG-CCG), direct (CCG-CCG), or everted (CCG-CGG) manner. Hap1p binds to DNA containing a direct repeat of two CGG triplets. It is a large protein that contains repression modules (RPMs) and heme-responsive motifs (HRMs) in addition to the DNA-binding and dimerization domains
PWIEPVMKELAKGEEIKSLREEVKSLQKNRKK
>gnl|CDD|271139 cd14656, Imelysin-like_EfeO, EfeO is a component of the EfeUOB operon. This family includes the EfeO domain, an essential component of the EfeUOB operon which is highly conserved in bacteria. However, its biochemical function is unknown. EfeO contains an N-terminal cupredoxin (CUP)-like domain and C-terminal imelysin-like domain that may bind iron. Algp7, a member of EfeO family protein from Sphingomonas sp. A1, is found to bind alginate at neutral pH, but does not contain the CUP domain, thus having a role that does not seem to be related to iron uptake. Some members of this family are fused to an N-terminal putative EfeU ion permease domain. The imelysin-like domain of this family also contains the GxHxxE sequence motif and a highly conserved functional site, suggesting a similar role to other imelysin family proteins containing the same motif
LAGAVAEYKAYVAGQLDELVTATEALAAAIKAGDLAAAKAAYAPARLAYERIEPIAESFGDLDPAIDARA
DDLEDGEQDPEFTGFHRIEYGLWHGKSTAGLAPVADQLVADVKALRARLRTLDLDPADLANGAHELLEEV
ATSKITGEEDRYSHTDLADFAANLEGARKALDLLRPLLEKKDPALLAQIDAAFAALDALLAAYRTGGGGY
VPYDALTAADRKALAAALGALAEPLAQLA
>gnl|CDD|271140 cd14657, Imelysin_IrpA-like, Imelysin-like iron-regulated protein A-like. This family includes putative iron-regulated protein A (IrpA) mainly from Bacteriodes, proteobacteria and cyanobacteria, as well as uncharacterized proteins with domains similar to insulin-cleaving membrane protease (imelysin, ICMP) protein. IrpA has been shown to be essential for growth under iron-deficient conditions in the cyanobacteria Synechococcus sp. The conserved GxHxxE motif is similar to other known imelysin-like proteins that are regulated by iron, such as ICMP, IrpA and EfeO. Imelysin is a membrane protein with the active site outside the cell envelope. The tertiary structure shows a fold consisting of two domains, each of which consists of a bundle of four helices that are similar to each other, implying an ancient gene duplication and fusion event
YADIAYASYSDALTDAKALQTAIDAFVANPSEANLEAAKNAWLAAREPYGQTEAFRFYNGPIDGDIDDED
GPEGQINAWPLDEAYIDYVIGDYGAGIIGNIINKAIDYPTITPELLAELNEAGGEANVSTGYHAIEFLLW
GQDLNGTGPGAGGPYTDYATTGNCTAGNADRRRQYLKAVTDLLVDDLETVRDAWAPGSSNNYRTFLAADP
DAALKNILTGMGSLSKGELAGERMTVALDTNSQEDEHSCFSDNTHRDIYYNAQGIQNVYTGSYTRTDGTV
VSGPSLSDLVAADDPALAAELSAALAATEAAVKAIDDPADDQLIDIENAAGNAAVQNAIDALGDQ
>gnl|CDD|271141 cd14658, Imelysin-like_IrpA, Imelysin-like domain in iron-regulated protein A. This family includes putative iron-regulated protein A (IrpA) mainly from Bacteriodes, proteobacteria and cyanobacteria, with domain similar to insulin-cleaving membrane protease (imelysin, ICMP) protein. It has been shown to be essential for growth under iron-deficient conditions in the cyanobacteria Synechococcus sp. The conserved GxHxxE motif is similar to other known imelysin-like proteins that are regulated by iron, such as ICMP, IrpA and EfeO. Imelysin is a membrane protein with the active site outside the cell envelope. The tertiary structure shows a fold consisting of two domains, each of which consists of a bundle of four helices that are similar to each other, implying an ancient gene duplication and fusion event
AVIKDYVDNVVIPTYKDLAAKTEALYKALQALKASPTQANLAAACDAWLAARAPWEQSEAFLFGPAADYG
IDPHLDSWPLDRTDLDNLLASGDPDIPYAVNNLGQELRGFHAIEYLLFGDGGPRKAADLTPRELEYLAAV
AEDLRNQCAQLEAAWIVQGCIGIADEVGDTKIGEPLNGDDPNYIESPYSHNSLTDFRDNIRSIENAYLGG
LDGKRGASSSSALVASKNPVLDAEVRAAIDDAIAAINAIPEPFVEANNNGRAAVKAAIDACQELSETLEK
AV
>gnl|CDD|271142 cd14659, Imelysin-like_IPPA, Imelysin-like protein. This family includes insulin-cleaving membrane protease (imelysin, ICMP)-like protein (IPPA from Psychrobacter arcticus), the Pseudomonas aeruginosa PA4372 and Vibrio cholera VC1266 Fur-regulated imelysin-like protein. They share the overall fold and a similar functional site as the insulin-cleaving membrane protease (ICMP). However, IPPA adopts a structure distinctive from the known HxxE metallopeptidases or iron-binding proteins, suggesting this protein may not be a peptidase; the histidine in the GxHxxE motif region is no longer conserved (GxxxxE), indicating a possible loss of enzymatic function or a change in substrate preference (compared to imelysin and IrpA families). A putative functional site for this non-peptidase homolog is located at the domain interface. The tertiary structure shows a fold consisting of two domains, each of which consists of a bundle of four helices that are similar to each other, implying an ancient gene duplication and fusion event
ALLTNLADNVILPAYAALAEAAAALATAAQAFCAAPSAATLAALRAAWRAAYLAWQRVEFLRFGPAEEEN
RRERIQFWPDRKGTTGRQIEALIASGDPILADALASKSVAAQGLPALEYLLFDDAADDAAIAAAAAYRCA
YLQAVAANLAALAQELLAAWQAGYGNFLAAAGPGPFRSSGEALQELVNALLYGLEFLRDQKLGRPLGKFG
GPARPPKRAEAWRSGLSLALLRANLEALRALYLGGGGGGLDDDLLRAKGGADLADRINAQFDAALAALAA
LPDPLLAVADPADRAKLEALYDELQALVRLLKTDLAPALGVTLGFNSADGD
>gnl|CDD|271137 cd14660, E2F_DD, Dimerization domain of E2F transcription factors. E2F transcription factors are involved in the regulation of DNA synthesis, cell cycle progression, proliferation and apoptosis. It associates with the retinoblastoma (Rb) protein, negatively regulating the G1-S transition until cyclin-dependent kinases phosphorylate Rb, which causes E2F release. E2F forms heterodimers with DP, a distantly related protein. Heterodimerization enhances the Rb binding, DNA binding, and transactivation activities of E2Fs. In humans, there are at least six closely related E2F and two DP family members, all containing a DNA-binding domain, a coiled-coil (CC) region, and a marked-box domain. E2F1 to E2F5 also contain a C-terminal transactivation domain
DRLSKLKEEIEELEAEEKELDELIRWCQQSLKNLTEDPENQKLAYVTYEDIRSIPSFKEQTVIAIKAPPG
TTLEVPDPEEGMRSYQIHLKSTKGPIDVYLCPKE
>gnl|CDD|271136 cd14661, Imelysin_like_PIBO, Permuted imelysin-like protein from Bacteroides ovatus (PIBO) and similar proteins. This family includes imelysin-like proteins such as imelysin-like protein from gut bacteria Bacteroides ovatus (PIBO) that have a circularly permuted topology compared with the canonical imelysin fold, such that the N-terminal and C-terminal regions are swapped in the primary sequence. PIBO is highly similar to imelysin-like protein from Psychrobacter arcticus (IPPA) despite low sequence similarity and circular permutation. PIBO is functionally equivalent to insulin-cleaving membrane protease (ICMP or imelysin), although the permutation results in the conserved GxHxxE motif to be at the C-terminus. It may have a conserved role in iron uptake although it adopts a structure distinctive from known metallopeptidases or iron-binding proteins
NLDYTAENASSWGNYMRNVASLLKNDATTLYDDWNTSYNGGESYASLFKNHNAGAYKSSALSCVEQIVDG
CAEIANEVGSAKIGDPYDKYTAGNTEEALYAVESWYSWHSRDDYSNNIISIRNAYYGTRDGNDADDIAAN
SLYKVVESNNPALDTKVKAAIDKAAKAIQAIPQPFRNHINSAETVAAQDACAELESLLKNELKSFIENKG
NNNTDAVLDAVVSQYVDAVVLPTYKDLKEKNAALYNAVVAFQANPSNSAFEAACEAWITAREPWEKSEAF
LFGPVADKGLDPNMDSWPLDQDGIVNILNSGNWSDLEWEEGDDDEAIGSAQNVRGFHTLEFLLFKDG
>gnl|CDD|271132 cd14662, STKc_SnRK2, Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREIINHRSLRHPNIIRFKEVVLTPTH
LAIVMEYAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKIC
DFGYSKSSVLHSQPKSTVGTPAYIAPEVLSRKEYDGKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKT
IQRIMSVQYKIPDYVRVSQDCRHLLSRIFVANPAKRITIPEIKNHPW
>gnl|CDD|271133 cd14663, STKc_SnRK3, Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMA
TKTKIFFVMELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLK
ISDFGLSALSEQFRQDGLLHTTCGTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFDDENLMA
LYRKIMKGEFEYPRWFSPGAKSLIKRILDPNPSTRITVEQIMASPW
>gnl|CDD|271134 cd14664, STK_BAK1_like, Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
IGRGGAGTVYKGVMPNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYE
YMPNGSLGELLHSRPESQPPLDWETRQRIALGSARGLAYLHHDCSPLIIHRDVKSNNILLDEEFEAHVAD
FGLAKLMDDKDSHVMSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAFLDDGVDIV
DWVRGLLEEKKVEALVDPDLQGVYKLEEVEQVFQVALLCTQSSPMERPTMREVVRMLEGD
>gnl|CDD|271135 cd14665, STKc_SnRK2-3, Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase
RYELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREIINHRSLRHPNIVRFKEVILTPTH
LAIVMEYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKIC
DFGYSKSSVLHSQPKSTVGTPAYIAPEVLLKKEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKT
IQRILSVQYSIPDYVHISPECRHLISRIFVADPATRITIPEIRNHEW
>gnl|CDD|270620 cd14667, 3D_containing_proteins, Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues. This family contains the 3D domain, named for its 3 conserved aspartates, including similar uncharacterized proteins. These proteins contain the critical active site aspartate of mltA-like lytic transglycosylases where the 3D domain forms a larger domain with the N-terminal region. This domain is also found in conjunction with numerous other domains such as the Escherichia coli MltA, a membrane-bound lytic transglycosylase comprised of 2 domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, corresponding to the 3D domain and Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial LTs, which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond
FTATAYTSCEGCCGGGPGGTASGGLPVGGGTIAVDPSVIPLGTKVYIEGYGVYVVEDTGGAIKGNRIDIY
MDSHAEALAFGRRYVEVYIL
>gnl|CDD|270616 cd14668, mlta_B, Domain B insert of mltA_like lytic transglycosylases. Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic, cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct
LEGSRTPTAEYRYPLYGRPPDLVTVDLGEFYPELKGKRLRGRVEGGRLVPYYTRAEIEAGALLGRGLELA
WLDDPVDAFFLQIQGSGRLRLPDGSVVRVGYAGKNGHPYRSIGRVLIDRGELPKEQMSMQAIRAWLRANP
ERARELLNENPSYVFFREL
>gnl|CDD|270617 cd14669, mlta_related_B, putative domain B insert of mltA_type lytic transglycosylases. Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic, cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct
VLIGSRTYPGGAFLYPVYGNPGDMIVPYYTRAEIERGALWEAKVIAYVKDPTDLYLMQLQGSGKVKLPDG
TVFRIAYAEQNGRPFLPPVASAKGSLTPSEAANCIALNPPEVAAFAISDPSYVFFRKE
>gnl|CDD|270614 cd14670, BslA_like, Bacterial immunoglobulin-like hydrophobin BslA and similar proteins. BslA (YuaB) is a protein from Bacillus subtilis acting as a hydrophobin, which forms surface layers around biofilms and participates in biofilm assembly. BslA contains an unusually hydrophobic "cap structure", which is essential for its activity and for the ability of bacteria to form hydrophobic, non-wetting biofilms. A number of domains in various proteins from Bacilli and other bacterial lineages appear related to BslA, but do not conserve the hydrophobic cap
PAALSGTLTLSPANGTAGTTSDIVLTYTAGQRSPNGTVEFTLPAGITATLTDTTTVNIVGLKTLTKQSIG
RTGTTYSYSKVGALLAASGIVLTLSNKDRPAAGTYTFKVIVDADGIGDYTFPAEYTTT
>gnl|CDD|269821 cd14671, PAAR_like, proline-alanine-alanine-arginine (PAAR) repeat superfamily. This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat superfamily, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. The PAAR-repeat proteins form a diverse superfamily with several subgroups extended both N- and C-terminally by domains with various predicted functions; the termini are exposed to solution, and do not distort the VgrG binding site. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli
PAARVGDPTAHTPGGPVISGSPNVFINGRPAARVGDVGDHPGGGNAIVSGSGTVFINGKPAARVGDRTSC
GGVIVSG
>gnl|CDD|270612 cd14672, UBA_ceTYDP2_like, UBA-like domain found in Caenorhabditis elegans tyrosyl-DNA phosphodiesterase 2 (TDP2) and similar proteins. The family includes C. elegans TDP2 and its homologs found in bilateria. TDP2 (also known as TTRAP or EAPII) belongs to the Mg(2+)/Mn(2+)-dependent family of phosphodiesterases which contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal phosphodiesterase domain. It required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini needed for subsequent DNA ligation and hence repair of the break. Tyrosyl-DNA phosphodiesterase 1 (TDP1), an enzyme that cleaves 3'-phosphotyrosyl bonds, and TDP2 are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TDP2 has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation
QLCEEFAEITGTDEALAQFYLQDRDWDLEKALDVYFG
>gnl|CDD|270192 cd14673, PH_PHLDB1_2, Pleckstrin homology-like domain-containing family B member 2 pleckstrin homology (PH) domain. PHLDB2 (also called LL5beta) and PHLDB1 (also called LL5alpha) are cytoskeleton- and membrane-associated proteins. PHLDB2 has been identified as a key component of the synaptic podosomes that play an important role in in postsynaptic maturation. Both are large proteins containing an N-terminal pleckstrin (PH) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SSKRCRGFLTKMGGKIKTWKKRWFVFDRNKRTLSYYVDKHEKKLKGVIYFQAIEEVYYDHLRSAAKSPNP
ALTFCVKTHDRLYYMVAPSPEAMRIWMDVIVTGAE
>gnl|CDD|270193 cd14674, PH_PLEKHM3_1, Pleckstrin homology domain-containing family M member 3 Pleckstrin homology domain 1. PLEKHM3 (also called differentiation associated protein/DAPR) exists as three alternatively spliced isoforms that participate in metal ion binding. It contains 2 PH domains and 1 phorbol-ester/DAG-type zinc finger domain. PLEKHM3 is found in Humans, canines, bovine, mouse, rat, chicken and zebrafish. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2, or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KKGYLEIRIDPDSYWQGCYAELSPYELYIYGLDSSGNQNLTDTYHLSHFQSITVTGSHEAKLVNVVLTDN
RQLQLKAESAWEALDWGQKL
>gnl|CDD|270194 cd14675, PH-SEC3_like, PH-like domain of Sec3-like protein. Fungal Sec3, as well as its homolog in higher eukaryotes Exocyst complex component 1 (EXOC1) are part of the exocyst is a conserved octameric complex involved in the docking of post-Golgi transport vesicles to sites of membrane remodeling during cellular processes such as polarization, migration, and division. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
AIKQAIQRSLFSPAHERLIEDVEVSKGGKKKRILFLCVSVTKPGQVRLHKVKKNDNGSFKIGKTWNLKDL
KKVDGKDPDKDTPEFDLHFDKTYKWEASSVAEKEAFISSLVKLYR
>gnl|CDD|270195 cd14676, PH_DOK1,2,3, Pleckstrin homology (PH) domain of Downstream of tyrosine kinase 1, 2, and 3. The Dok family adapters are phosphorylated by different protein tyrosine kinases. Dok proteins are involved in processes such as modulation of cell differentiation and proliferation, as well as in control of the cell spreading and migration The Dok protein contains an N-terminal pleckstrin homology (PH) domain followed by a central phosphotyrosine binding (PTB) domain, which has a PH-like fold, and a proline- and tyrosine-rich C-terminal tail. The PH domain is binds to acidic phospholids and localizes proteins to the plasma membrane. There are 7 mammalian Dok members: Dok-1 to Dok-7. Dok-1 and Dok-2 act as negative regulators of the Ras-Erk pathway downstream of many immunoreceptor-mediated signaling systems, and it is believed that recruitment of p120 rasGAP by Dok-1 and Dok-2 is critical to their negative regulation. Dok-3 is a negative regulator of the activation of JNK and mobilization of Ca2+ in B-cell receptor-mediated signaling, interacting with SHIP-1 and Grb2. In general, PH domains have diverse functions, but are generally involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
KEGQLYLQQQKFFGKKWRKFWAVLYPASPCGVARLEFFEGKGGPSGGKPSKRESDRKVIRLSDCVSVAPA
GGESSPPRDTAAFLLETTEKLYLLAAEAAERADWVQKLCELAF
>gnl|CDD|270196 cd14677, PH_DOK7, Pleckstrin homology (PH) domain of Downstream of tyrosine kinase 7. The Dok family adapters are phosphorylated by different protein tyrosine kinases. Dok proteins are involved in processes such as modulation of cell differentiation and proliferation, as well as in control of the cell spreading and migration The Dok protein contains an N-terminal pleckstrin homology (PH) domain followed by a central phosphotyrosine binding (PTB) domain, which has a PH-like fold, and a proline- and tyrosine-rich C-terminal tail. The PH domain is binds to acidic phospholids and localizes proteins to the plasma membrane. There are 7 mammalian Dok members: Dok-1 to Dok-7. Dok-7 is the key cytoplasmic activator of MuSK (Muscle-Specific Protein Tyrosine Kinase). In general, PH domains have diverse functions, but are generally involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LVEGQVKLRDGKKWKSRWLVLRKPSPVADCLLLLVYKDKSSRRKGLKEKASLTLEHFCGLESGFPLEKES
NTLAIICLTQVVVLGFDSREALLEWDARIRYA
>gnl|CDD|270197 cd14678, PH_DOK4_DOK5_DOK6, Pleckstrin homology (PH) domain of Downstream of tyrosine kinase 4, 5, and 6 proteins. The Dok family adapters are phosphorylated by different protein tyrosine kinases. Dok proteins are involved in processes such as modulation of cell differentiation and proliferation, as well as in control of the cell spreading and migration The Dok protein contains an N-terminal pleckstrin homology (PH) domain followed by a central phosphotyrosine binding (PTB) domain, which has a PH-like fold, and a proline- and tyrosine-rich C-terminal tail. The PH domain binds to acidic phospholids and localizes proteins to the plasma membrane, while the PTB domain mediates protein-protein interactions by binding to phosphotyrosine-containing motifs. The C-terminal part of Dok contains multiple tyrosine phosphorylation sites that serve as potential docking sites for Src homology 2-containing proteins such as ras GTPase-activating protein and Nck, leading to inhibition of ras signaling pathway activation and the c-Jun N-terminal kinase (JNK) and c-Jun activation, respectively. There are 7 mammalian Dok members: Dok-1 to Dok-7. Dok-1 and Dok-2 act as negative regulators of the Ras-Erk pathway downstream of many immunoreceptor-mediated signaling systems, and it is believed that recruitment of p120 rasGAP by Dok-1 and Dok-2 is critical to their negative regulation. Dok-3 is a negative regulator of the activation of JNK and mobilization of Ca2+ in B-cell receptor-mediated signaling, interacting with SHIP-1 and Grb2. Dok-4- 6 play roles in protein tyrosine kinase(PTK)-mediated signaling in neural cells and Dok-7 is the key cytoplasmic activator of MuSK (Muscle-Specific Protein Tyrosine Kinase). In general, PH domains have diverse functions, but are generally involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VKQGYVRIRSRKLGIYRRCWLVFRKASSKGPKRLEKYPDERAAYLRACHKVTELSNVKNITRLPKETKRH
AVAIIFTDDSSKTFACDSELEAEEWCKVLSMECLG
>gnl|CDD|275429 cd14679, PH_p115RhoGEF, Rho guanine nucleotide exchange factor Pleckstrin homology domain. p115RhoGEF (also called LSC, GEF1 or LBCL2) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. In addition to the Dbl homology (DH)-PH domain, p115RhoGEF contains an N-terminal RGS (Regulator of G-protein signalling) domain. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
FKNIDITKKKLVHEGPLTWRVTKDKAIEVHVLLLDDLLVLLQKQDERLVLKCHSRTTTPTPDGKQMLSPI
IKLNSAMTREVATDRKAFYVIFTWEQGAQIYELVAQTVSERKNWCALISETAGLL
>gnl|CDD|275430 cd14680, PH_p190RhoGEF, Rho guanine nucleotide exchange factor Pleckstrin homology domain. p190RhoGEF (also called RIP2 or ARHGEF28) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. In addition to the Dbl homology (DH)-PH domain, p190RhoGEF contains an N-terminal C1 (Protein kinase C conserved region 1) domain. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LLHEGLVYWKTATGRFKDILALLLTDVLLFLQEKDQKYIFAAVDQKPPVICLQKLIVREVANEERGMFLI
SASSAGPEMYEIHTSSKEERNNWMRLIQEAV
>gnl|CDD|270200 cd14681, PH-STXBP6, PH-like domain of Syntaxin binding protein 6. Syntaxin binding protein 6 (STXBP6, also called Amisyn) contains, beside the N-terminal PH-like domain, a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, with STXBP6 being a R-SNARE. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SAKSAISKEIFAPRDERMLGAVQVKRRTKKKIPFLATGGQGEYLTYICLSVTNKKPAQVFITKVKQFEGS
TSFVRRSQWMLEQLRQVNGIDPNKDSPEFDLVFDNGFDQWVASSASEKCTFFQILHHTCQ
>gnl|CDD|270201 cd14682, PH-EXOC1_like, PH-like domain of Exocyst complex component 1-like. Exocyst complex component 1-like proteins are short, higher eukaryotic proteins that show homology to the PH-domain of higher eukaryotic EXOC1 and yeast SEC3 which are part of the exocyst complex involved in the docking of post-Golgi transport vesicles to sites of membrane remodeling during cellular processes such as polarization, migration, and division. Their function is unknown. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
SSLVKEDMQKKLFRPLGQTLYEFIEIEEQSHGRHYLCASVAKDKEVQISMVKHYRVCLDEKYERTEIWSL
KDLEMIDGKDADTDNPCFDMHFEEVRSVEAYSCASKYAFARTLNKLND
>gnl|CDD|270202 cd14683, PH-EXOC1, PH-like domain of Exocyst complex component 1. Exocyst complex component 1 (EXOC1, also known as SEC3) is the higher eukaryotes homolog of yeast Sec3. The Exocyst is a conserved octameric complex involved in the docking of post-Golgi transport vesicles to sites of membrane remodeling during cellular processes such as polarization, migration, and division. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
AIRHALQREVFTPNDERLLAVVNVSKAGKKKKTSFLCVAVTTERPVQVRLYQVKKSDKGVYKKKRSWLLR
DLKTVDGKNPKKETPEFDLHFDKVYKWVASNVQEKNAFISCLWKLCH
>gnl|CDD|270203 cd14684, RanBD1_RanBP2-like, Ran-binding protein 2, Ran binding domain repeat 1. RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 1 is present in this hierarchy
TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLK
PNAGSDKSFVWNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ
>gnl|CDD|270204 cd14685, RanBD3_RanBP2-like, Ran-binding protein 2, Ran binding domain repeat 3. RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 3 is present in this hierarchy
SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQ
PMKGSERAWVWTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK
>gnl|CDD|269834 cd14686, bZIP, Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain. Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KERRRERNREAARRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE
>gnl|CDD|269835 cd14687, bZIP_ATF2, Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar proteins: a DNA-binding and dimerization domain. ATF-2 is a sequence-specific DNA-binding protein that belongs to the Basic leucine zipper (bZIP) family of transcription factors. In response to stress, it activates a variety of genes including cyclin A, cyclin D, and c-Jun. ATF-2 also plays a role in the DNA damage response that is independent of its transcriptional activity. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KRKRFLERNRIAASKCRQRKKQWVQQLEEKVRKLESENKALKAEVDKLREEVLDLKNLLLA
>gnl|CDD|269836 cd14688, bZIP_YAP, Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a DNA-binding and dimerization domain. This subfamily is composed predominantly of AP-1-like transcription factors including Saccharomyces cerevisiae YAPs, Schizosaccharomyces pombe PAP1, and similar proteins. Members of this subfamily belong to the Basic leucine zipper (bZIP) family of transcription factors. The YAP subfamily is composed of eight members (YAP1-8) which may all be involved in stress responses. YAP1 is the major oxidative stress regulator and is also involved in iron metabolism (like YAP5) and detoxification of arsenic (like YAP8). YAP2 is involved in cadmium stress responses while YAP4 and YAP6 play roles in osmotic stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
DPKERRRAQNREAQRAFRERKKERIKELEQRVAELEEELAELEEELQELRAELRELESELQSL
>gnl|CDD|269837 cd14689, bZIP_CREB3, Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) and similar proteins: a DNA-binding and dimerization domain. This subfamily is composed of CREB3 (also called LZIP or Luman), and the CREB3-like proteins CREB3L1 (or OASIS), CREB3L2, CREB3L3 (or CREBH), and CREB3L4 (or AIbZIP). They are type II membrane-associated members of the Basic leucine zipper (bZIP) family of transcription factors, with their N-termini facing the cytoplasm and their C-termini penetrating through the ER membrane. They contain an N-terminal transcriptional activation domain followed bZIP and transmembrane domains, and a C-terminal tail. They play important roles in ER stress and the unfolded protein response (UPR), as well as in many other biological processes such as cell secretion, bone and cartilage formation, and carcinogenesis. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
LKKVRRKIRNKISAQESRRRKKEYIDGLESRVAACTAENQELKKKVEELEKQNRSLLSQLR
>gnl|CDD|269838 cd14690, bZIP_CREB1, Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) and similar proteins: a DNA-binding and dimerization domain. CREB1 is a Basic leucine zipper (bZIP) transcription factor that plays a role in propagating signals initiated by receptor activation through the induction of cAMP-responsive genes. Because it responds to many signal transduction pathways, CREB1 is implicated to function in many processes including learning, memory, circadian rhythm, immune response, and reproduction, among others. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KRQLRLEKNREAARECRRKKKEYVKCLENRVAVLENENKELREELKILKELLCQE
>gnl|CDD|269839 cd14691, bZIP_XBP1, Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a DNA-binding and dimerization domain. XBP1, a member of the Basic leucine zipper (bZIP) family, is the key transcription factor that orchestrates the unfolded protein response (UPR). It is the most conserved component of the UPR and is critical for cell fate determination in response to ER stress. The inositol-requiring enzyme 1 (IRE1)-XBP1 pathway is one of the three major sensors at the ER membrane that initiates the UPR upon activation. IRE1, a type I transmembrane protein kinase and endoribonuclease, oligomerizes upon ER stress leading to its increased activity. It splices the XBP1 mRNA, producing a variant that translocates to the nucleus and activates its target genes, which are involved in protein folding, degradation, and trafficking. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
EEKDLRRKLKNRVAAQTARDRKKARMDELEERVRELEEENQKLRAENESLRARNEDLL
>gnl|CDD|269840 cd14692, bZIP_ATF4, Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar proteins: a DNA-binding and dimerization domain. ATF-4 was also isolated and characterized as the cAMP-response element binding protein 2 (CREB2). It is a Basic leucine zipper (bZIP) transcription factor that has been reported to act as both an activator or repressor. It is a critical component in both the unfolded protein response (UPR) and amino acid response (AAR) pathways. Under certain stress conditions, ATF-4 transcription is increased; accumulation of ATF-4 induces the expression of genes involved in amino acid metabolism and transport, mitochondrial function, redox chemistry, and others that ensure protein synthesis and recovery from stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
EKKERKREQNKNAATRYRQKKREEKEELLSEEEELEDRNRELKDEVEELQREINYLKDLLREV
>gnl|CDD|269841 cd14693, bZIP_CEBP, Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP) and similar proteins: a DNA-binding and dimerization domain. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate the cell cycle, differentiation, growth, survival, energy metabolism, innate and adaptive immunity, and inflammation, among others. They are also associated with cancer and viral disease. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. Each possesses unique properties to regulate cell type-specific growth and differentiation. The sixth isoform, CEBPZ (zeta), lacks an intact DNA-binding domain and is excluded from this subfamily. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
DSEEYRQKRERNNIAVRKSREKAKQRQLETQQKVQELRKENERLQKRVELLTKELSVLKS
>gnl|CDD|269842 cd14694, bZIP_NFIL3, Basic leucine zipper (bZIP) domain of Nuclear factor interleukin-3-regulated protein (NFIL3): a DNA-binding and dimerization domain. NFIL3, also called E4 promoter-binding protein 4 (E4BP4), is a Basic leucine zipper (bZIP) transcription factor that was independently identified as a transactivator of the IL3 promoter in T-cells and as a transcriptional repressor that binds to a DNA sequence site in the adenovirus E4 promoter. Its expression levels are regulated by cytokines and it plays crucial functions in the immune system. It is required for the development of natural killer cells and CD8+ conventional dendritic cells. In B-cells, NFIL3 mediates immunoglobulin heavy chain class switching that is required for IgE production, thereby influencing allergic and pathogenic immune responses. It is also involved in the polarization of T helper responses. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KDDKYWEKRRKNNEAAKRSREKRRLNDLVLENRILELTEENAVLRAELAALKRRFGLLLD
>gnl|CDD|269843 cd14695, bZIP_HLF, Basic leucine zipper (bZIP) domain of Hepatic leukemia factor (HLF) and similar proteins: a DNA-binding and dimerization domain. HLF, also called vitellogenin gene-binding protein (VBP) in birds, is a circadian clock-controlled Basic leucine zipper (bZIP) transcription factor which is a direct transcriptional target of CLOCK/BMAL1. It is implicated, together with bZIPs DBP and TEF, in the regulation of genes involved in the metabolism of endobiotic and xenobiotic agents. Triple knockout mice display signs of early aging and suffer premature death, likely due to impaired defense against xenobiotic stress. A leukemogenic translocation results in the chimeric fusion protein E2A-HLF that results in a rare form of pro-B-cell acute lymphoblastic leukemia (ALL). bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KDDKYWERRRKNNLAAKRSRDARRLKENQIAIRAAFLEKENAALRAEIAKLKKELEDLRK
>gnl|CDD|269844 cd14696, bZIP_Jun, Basic leucine zipper (bZIP) domain of Jun proteins and similar proteins: a DNA-binding and dimerization domain. Jun is a member of the activator protein-1 (AP-1) complex, which is mainly composed of Basic leucine zipper (bZIP) dimers of the Jun and Fos families, and to a lesser extent, the activating transcription factor (ATF) and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. There are three Jun proteins: c-Jun, JunB, and JunD. c-Jun is the most potent transcriptional activator of the AP-1 proteins. Both c-Jun and JunB are essential during development; deletion of either results in embryonic lethality in mice. c-Jun is essential in hepatogenesis and liver erythropoiesis, while JunB is required in vasculogenesis and angiogenesis in extraembryonic tissues. While JunD is dispensable in embryonic development, it is involved in transcription regulation of target genes that help cells to cope with environmental signals. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KLERKRARNRIAASKCRKRKLERIARLEDKVKELKNQNSELTSTASLLREQVCQLKQKVME
>gnl|CDD|269845 cd14697, bZIP_Maf, Basic leucine zipper (bZIP) domain of musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain. Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, and a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. The small Mafs (MafF, MafK, MafG) do not contain a transactivation domain. They form dimers with cap'n'collar (CNC) proteins that harbor transactivation domains, and they act either as activators or repressors depending on their dimerization partner. They play roles in stress response and detoxification pathways. They have been implicated in various diseases such as diabetes, neurological diseases, thrombocytopenia and cancer. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KEEVIQLKQKRRTLKNRGYAQSCRAKRVQQKEQLENEKAELRSQIEELKEENSELQQELDYYKQKFEALA
>gnl|CDD|269846 cd14698, bZIP_CNC, Basic leucine zipper (bZIP) domain of Cap'n'Collar (CNC) transcription factors: a DNA-binding and dimerization domain. CNC proteins form a subfamily of Basic leucine zipper (bZIP) transcription factors that are defined by a conserved 43-amino acid region (called the CNC domain) located N-terminal to the bZIP DNA-binding domain. This subfamily includes Drosophila Cnc and four vertebrate counterparts, NFE2 (nuclear factor, erythroid-derived 2), NFE2-like 1 or NFE2-related factor 1 (NFE2L1 or Nrf1), NFE2L2 (or Nrf2), and NFE2L3 (or Nrf3). It also includes BACH1 and BACH2, which contain an additional BTB domain (Broad complex###Tramtrack###Bric-a-brac domain, also known as the POZ [poxvirus and zinc finger] domain). CNC proteins function during development and/or contribute in maintaining homeostasis during stress responses. In flies, Cnc functions both in development and in stress responses. In vertebrates, several CNC proteins encoded by distinct genes show varying functions and expression patterns. NFE2 is required for the proper development of platelets while the three Nrfs function in stress responses. Nrf2, the most extensively studied member of this subfamily, acts as a xenobiotic-activated receptor that regulates the adaptive response to oxidants and electrophiles. BACH1 forms heterodimers with small Mafs such as MafK to function as a repressor of heme oxygenase-1 (HO-1) gene (Hmox-1) enhancers. BACH2 is a B-cell specific transcription factor that plays a critical role in oxidative stress-mediated apoptosis. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
QLQLIRDIRRRGKNKVAAQNCRKRKLDQISTLEDEVDELKEEKEKLLKERDELEAETREMKDKYSQLY
>gnl|CDD|269847 cd14699, bZIP_Fos_like, Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a DNA-binding and dimerization domain. This subfamily is composed of Fos proteins (c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2), Activating Transcription Factor-3 (ATF-3), and similar proteins. Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of bZIP dimers of the Jun and Fos families, and to a lesser extent, ATF and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. ATF3 is induced by various stress signals such as cytokines, genotoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
RRRKRRERNKVAAAKCRQRRRELMEELQAEVEQLEDENEKLQSEIANLRSEKEQLEELL
>gnl|CDD|269848 cd14700, bZIP_ATF6, Basic leucine zipper (bZIP) domain of Activating Transcription Factor-6 (ATF-6) and similar proteins: a DNA-binding and dimerization domain. ATF-6 is a type I membrane-bound Basic leucine zipper (bZIP) transcription factor that binds to the consensus ER stress response element (ERSE) and enhances the transcription of genes encoding glucose-regulated proteins Grp78, Grp94, and calreticulum. ATF-6 is one of three sensors of the unfolded protein response (UPR) in metazoans; the others being the kinases Ire1 and PERK. It contains an ER-lumenal domain that detects unfolded proteins. In response to ER stress, ATF-6 translocates from the ER to the Golgi with simultaneous cleavage in a process called regulated intramembrane proteolysis (Rip) to its transcriptionally competent form, which enters the nucleus and upregulates target UPR genes. The three UPR sensor branches cross-communicate to form a signaling network. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
RQQRMIKNRESACLSRKKKKEYVQSLETKLEQLKQENQKLKSENETLRERLS
>gnl|CDD|269849 cd14701, bZIP_BATF, Basic leucine zipper (bZIP) domain of BATF proteins: a DNA-binding and dimerization domain. Basic leucine zipper (bZIP) transcription factor ATF-like (BATF or SFA2), BATF2 (or SARI) and BATF3 form heterodimers with Jun proteins. They function as inhibitors of AP-1-driven transcription. Unlike most bZIP transcription factors that contain additional domains, BATF and BATF3 contain only the the bZIP DNA-binding and dimerization domain. BATF2 contains an additional C-terminal domain of unknown function. BATF:Jun hetrodimers preferentially bind to TPA response elements (TREs) with the consensus sequence TGA(C/G)TCA, and can also bind to a TGACGTCA cyclic AMP response element (CRE). In addition to negative regulation, BATF proteins also show positive transcriptional activities in the development of classical dendritic cells and T helper cell subsets, and in antibody production. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
DQKKVRRREKNRDAAQRSRQKQTEKADKLHEESESLERANAALRKEIKDLTEELKYLT
>gnl|CDD|269850 cd14702, bZIP_plant_GBF1, Basic leucine zipper (bZIP) domain of Plant G-box binding factor 1 (GBF1)-like transcription factors: a DNA-binding and dimerization domain. This subfamily is composed of plant bZIP transciption factors including Arabidopsis thaliana G-box binding factor 1 (GBF1), Zea mays Opaque-2 and Ocs element-binding factor 1 (OCSBF-1), Triticum aestivum Histone-specific transcription factor HBP1 (or HBP-1a), Petroselinum crispum Light-inducible protein CPRF3 and CPRF6, and Nicotiana tabacum BZI-3, among many others. bZIP G-box binding factors (GBFs) contain an N-terminal proline-rich domain in addition to the bZIP domain. GBFs are involved in developmental and physiological processes in response to stimuli such as light or hormones. Opaque-2 plays a role in affecting lysine content and carbohydrate metabolism, acting indirectly on starch/amino acid ratio. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
RRRRKQSNRESARRSRMRKQAHLEELEAQVEQLRAENSTLRAELNALSQEYR
>gnl|CDD|269851 cd14703, bZIP_plant_RF2, Basic leucine zipper (bZIP) domain of Plant RF2-like transcription factors: a DNA-binding and dimerization domain. This subfamily is composed of plant bZIP transciption factors with similarity to Oryza sativa RF2a and RF2b, which are important for plant development. They interact with, as homodimers or heterodimers with each other, and activate transcription from the RTBV (rice tungro bacilliform virus) promoter, which is regulated by sequence-specific DNA-binding proteins that bind to the essential cis element BoxII. RF2a and RF2b show differences in binding affinities to BoxII, expression patterns in different rice organs, and subcellular localization. Transgenic rice with increased RF2a and RF2b display increased resistance to rice tungro disease (RTD) with no impact on plant development. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
RAKRILANRQSAQRSRERKLQYISELERKVQTLQTEVATLSAQLALLEQEKA
>gnl|CDD|269852 cd14704, bZIP_HY5-like, Basic leucine zipper (bZIP) domain of Plant Elongated/Long Hypocotyl5 (HY5)-like transcription factors and similar proteins: a DNA-binding and dimerization domain. This subfamily is predominantly composed of plant Basic leucine zipper (bZIP) transcription factors with similarity to Solanum lycopersicum and Arabidopsis thaliana HY5. Also included are the Dictyostelium discoideum bZIP transcription factors E and F. HY5 plays an important role in seedling development and is a positive regulator of photomorphogenesis. Plants with decreased levels of HY5 show defects in light responses including inhibited photomorphogenesis, loss of alkaloid organization, and reduced carotenoid accumulation. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
RQRRLLRNRESAQLSRQRKKEYLSELEAKCRELEAENAELEARVELLQAENA
>gnl|CDD|269853 cd14705, bZIP_Zip1, Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding and dimerization domain. This subfamily is composed of fungal bZIP transcription factors including Schizosaccharomyces pombe Zip1, Saccharomyces cerevisiae Methionine-requiring protein 28 (Met28p), and Neurospora crassa cys-3, among others. Zip1 is required for the production of key proteins involved in sulfur metabolism and also plays a role in cadmium response. Met28p acts as a cofactor of Met4p, a transcriptional activator of the sulfur metabolic network; it stabilizes DNA:Met4 complexes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
LEEKRRRNTAASARFRAKKKQREQELEEKLKELEERIKELERRLDELESENKFLK
>gnl|CDD|269854 cd14706, bZIP_CREBZF, Basic leucine zipper (bZIP) domain of CREBZF/Zhangfei transcription factor and similar proteins: a DNA-binding and dimerization domain. CREBZF (also called Zhangfei, ZF, LAZip, or SMILE) is a neuronal bZIP transcription factor that is involved in the infection cycle of herpes simplex virus (HSV) and related cellular processes. It suppresses the ability of the HSV transactivator VP16 to initiate the viral replicative cycle. CREBZF has also been implicated in the regulation of the human nerve growth factor receptor trkA and the tumor suppressor p53. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
SPEVMSKNAIAARENRLKKKEYVENLEKSVDKLKSENKELKKANKKLQKLVEEL
>gnl|CDD|269855 cd14707, bZIP_plant_BZIP46, Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a DNA-binding and dimerization domain. This subfamily is composed of uncharacterized plant bZIP transciption factors with similarity to Glycine max BZIP46, which may be a drought-responsive gene. Plant bZIPs are involved in developmental and physiological processes in response to stimuli/stresses such as light, hormones, and temperature changes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
RRQRRMIKNRESAARSRARKQAYTNELELEVAHLKEENARLKRQQEELLLALAAS
>gnl|CDD|269856 cd14708, bZIP_HBP1b-like, Basic leucine zipper (bZIP) domain of uncharaterized BZIP transcription factors with similarity to Triticum aestivum HBP-1b: a DNA-binding and dimerization domain. This subfamily is composed primarily of uncharacterized bZIP transciption factors from flowering plants, mosses, clubmosses, and algae. Included in this subfamily is wheat HBP-1b, which contains a C-terminal DOG1 domain, which is a specific plant regulator for seed dormancy. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KVLRRLAQNREAARKSRLRKKAYVQQLEESVEKLKQLEQELQRARQQGRELGT
>gnl|CDD|269857 cd14709, bZIP_CREBL2, Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein-like 2 (CREBL2): a DNA-binding and dimerization domain. CREBL2 is a bZIP transcription factor that interacts with CREB and plays a critical role in adipogenesis and lipogenesis. Its overexpression upregulates the expression of PPARgamma and CEBPalpha to promote adipogenesis as well as accelerate lipogenesis by increasing GLUT1 and GLUT4. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KKKAKLERNRQSARESRDRKKLRYQYLEQLVADREREILLLREELEMYKQWCEELD
>gnl|CDD|269858 cd14710, bZIP_HAC1-like, Basic leucine zipper (bZIP) domain of Fungal HAC1-like transcription factors: a DNA-binding and dimerization domain. HAC1 (also called Hac1p or HacA) is a bZIP transcription factor that plays a critical role in the unfolded protein response (UPR). The UPR is initiated by the ER-resident protein kinase and endonuclease IRE1, which promotes non-conventional splicing of the HAC1 mRNA, facilitating its translation. HAC1 binds to and activates promoters of genes that encode chaperones and other targets of the UPR. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
RRIERILRNRRAAHQSRERKRLHVEFLEKKCDLLEALLQRLQDLLAQLEEKLA
>gnl|CDD|269859 cd14711, bZIP_CEBPA, Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein alpha (CEBPA): a DNA-binding and dimerization domain. CEPBA is a critical regulator of myeloid development; it directs granulocyte and monocyte differentiation. It is highly expressed in early myeloid progenitors and is found mutated in over half of patients with acute myeloid leukemia (AML). It is also a key regulator in energy homeostasis; mice deficient of CEBPA show abnormalities in glycogen/lipid synthesis and storage. CEPBA is the longest CEBP protein containing two transactivation domains at the N-terminus followed by a regulatory domain, a bZIP domain, and C-terminal tail. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTSDNDRLRKRVEQLSRELETLRG
>gnl|CDD|269860 cd14712, bZIP_CEBPB, Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein beta (CEBPB): a DNA-binding and dimerization domain. CEBPB is a key regulator of metabolism, adipocyte differentiation, myogenesis, and macrophage activation. It is expressed as three distinct isoforms from an intronless gene through alternative translation initiation: CEBPB1 (or liver-enriched activator protein 1, LAP1); CEBPB2 (OR LAP2); and CEBPB3 (or liver-enriched inhibitory protein, LIP). LAP1/2 function as transcriptional activators while LIP is a repressor due to its lack of a transactivation domain. The relative expression of LAP and LIP has effects on inflammation, ER stress, and insulin resistance. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQ
L
>gnl|CDD|269861 cd14713, bZIP_CEBPG, Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein gamma (CEBPG): a DNA-binding and dimerization domain. CEBPG is an important regulator of cellular senescence; mouse embryonic fibroblasts deficient of CEBPG proliferated poorly, entered senescence prematurely, and expressed elevated levels of proinflammatory genes. It is also the primary transcription factor that regulates antioxidant and DNA repair transcripts in normal bronchial epithelial cells. In a subset of AML patients with CEBPA hypermethylation, CEBPG is significantly overexpressed. CEBPG is the shortest CEBP protein and it lacks a transactivation domain. It acts as a regulator and buffering reservoir against the transcriptional activities of other CEBP proteins. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KDSDEYRKRRERNNLAVKKSREKSKQKAQETLQRVNQLKEENERLEAKIKLLSKELSVLKD
>gnl|CDD|269862 cd14714, bZIP_CEBPD, Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein delta (CEBPD): a DNA-binding and dimerization domain. CEBPD is an inflammatory response gene that is induced by Toll-like receptor 4 (TLR4) and is essential in the expression of many lipopolysaccharide (LPS)-induced genes and the clearance of bacterial infection. Its expression is increased in response to various extracellular stimuli and it induces growth arrest and apoptosis in cancer cells. It is thought to function as a tumor suppressor and its expression is found reduced by site-specific methylation in many cancers including breast, cervical, and hepatocellular carcinoma. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
DRHSPEYRQRRERNNIAVRKSRDKAKRRNQDMQQKLLELSAENEKLHKKIEQLTRDLSSLRHFFK
>gnl|CDD|269863 cd14715, bZIP_CEBPE, Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein epsilon (CEBPE): a DNA-binding and dimerization domain. CEBPE is a critical regulator of terminal granulocyte differentiation or granulopoiesis. It is expressed only in myeloid cells. Mice deficient with CEBPE are normal at birth and fertile, but they do not produce normal neutrophils or eosinophils, and show impaired inflammatory and bacteriocidal responses. Functional loss of CEBPE causes the rare congenital disorder, Neutrophil-specific granule deficiency (SGD), which is characterized by patients' neutrophils with atypical nuclear morphology, abnormal migration and bactericidal activity, and the lack of specific granules. Patients with SGD suffer from severe and frequent bacterial infections. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KDSLEYRLRRERNNIAVRKSRDKAKRRVLETQQRMLEYMAENERLRSRVEQLTQELDTLRD
>gnl|CDD|269864 cd14716, bZIP_CEBP-like_1, Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP)-like proteins: a DNA-binding and dimerization domain. This group is an uncharacterized subfamily of CEBP-like proteins. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate the cell cycle, differentiation, growth, survival, energy metabolism, innate and adaptive immunity, and inflammation, among others. They are also associated with cancer and viral disease. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. Each possesses unique properties to regulate cell type-specific growth and differentiation. The sixth isoform, CEBPZ (zeta), lacks an intact DNA-binding domain and is excluded from this subfamily. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
ESDEYRKRRERNNIAVRKSRDKAKLRNLETQQKLIELHNETKTQKEAIIHMPQSCMEWET
>gnl|CDD|269865 cd14717, bZIP_Maf_small, Basic leucine zipper (bZIP) domain of small musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain. Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The small Mafs (MafF, MafK, and MafG) do not contain a transactivation domain but do harbor the anxillary DNA-binding domain and a C-terminal bZIP domain. They form dimers with cap'n'collar (CNC) proteins that harbor transactivation domains, and they act either as activators or repressors depending on their dimerization partner. CNC transcription factors include NFE2 (nuclear factor, erythroid-derived 2) and similar proteins NFE2L1 (NFE2-like 1), NFE2L2, and NFE2L3, as well as BACH1 and BACH2. Small Mafs play roles in stress response and detoxification pathways. They also regulate the expression of betaA-globin and other genes activated during erythropoiesis. They have been implicated in various diseases such as diabetes, neurological diseases, thrombocytopenia and cancer. Triple deletion of the three small Mafs is embryonically lethal. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KEEIIRLKQRRRTLKNRGYAASCRIKRVTQKEELEKQKAELQQEVEKLARENASMRLELDALRSKYEALQ
>gnl|CDD|269866 cd14718, bZIP_Maf_large, Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain. Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, and neural retina leucine zipper or NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. MafA and MafB also play crucial roles in islet beta cells; they regulate genes essential for glucose sensing and insulin secretion cooperatively and sequentially. Large Mafs are also implicated in oncogenesis; MafB and c-Maf chromosomal translocations result in multiple myelomas. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KEEVIRLKQKRRTLKNRGYAQSCRSKRVQQRHVLESEKCQLQQQVEQLKQEVSRLARERDAYKEKYEKLA
>gnl|CDD|269867 cd14719, bZIP_BACH, Basic leucine zipper (bZIP) domain of BTB and CNC homolog (BACH) proteins: a DNA-binding and dimerization domain. BACH proteins are Cap'n'Collar (CNC) Basic leucine zipper (bZIP) transcription factors that are defined by a conserved 43-amino acid region (called the CNC domain) located N-terminal to the bZIP DNA-binding domain. In addition, they contain a BTB domain (Broad complex-Tramtrack-Bric-a-brac domain, also known as the POZ [poxvirus and zinc finger] domain) that is absent in other CNC proteins. Veterbrates contain two members, BACH1 and BACH2. BACH1 forms heterodimers with small Mafs such as MafK to function as a repressor of heme oxygenase-1 (HO-1) gene (Hmox-1) enhancers. It has also been implicated as the master regulator of breast cancer bone metastasis. The BACH1 bZIP transcription factor should not be confused with the protein originally named as BRCA1-Associated C-terminal Helicase1 (BACH1), which has been renamed BRIP1 (BRCA1 Interacting Protein C-terminal Helicase1) and also called FANCJ. BACH2 is a B-cell specific transcription factor that plays a critical role in oxidative stress-mediated apoptosis. It plays an important role in class switching and somatic hypermutation of immunoglobulin genes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
TPEQLEFIHDVRRRSKNRIAAQRCRKRKLDCIQNLECEIKKLVCEKEKLLGERNQLKASMGELRENFSCL
C
>gnl|CDD|269868 cd14720, bZIP_NFE2-like, Basic leucine zipper (bZIP) domain of Nuclear Factor, Erythroid-derived 2 (NFE2) and similar proteins: a DNA-binding and dimerization domain. This subfamily is composed of NFE2 and NFE2-like proteins including NFE2-like 1 or NFE2-related factor 1 (NFE2L1 or Nrf1), NFE2L2 (or Nrf2), and NFE2L3 (or Nrf3). These are Cap'n'Collar (CNC) Basic leucine zipper (bZIP) transcription factors that are defined by a conserved 43-amino acid region (called the CNC domain) located N-terminal to the bZIP DNA-binding domain. NFE2 functions in development; it is required for the proper development of platelets. The three Nrfs function in stress responses. Nrf2, the most extensively studied member of this subfamily, acts as a xenobiotic-activated receptor that regulates the adaptive response to oxidants and electrophiles. As the master regulator of the antioxidant defense pathway, it plays roles in the biology of inflammation, obesity, and cancer. Nrf1 is an essential protein that binds to the antioxidant response element (ARE) and is also involved in regulating oxidative stress. In addition, it also regulates genes involved in cell and tissue differentiation, inflammation, and hepatocyte homeostasis. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
QLALIRDIRRRGKNKVAAQNCRKRKLDNIVGLEDEVEQLQRQREKLLREKAENAKSLREMKQKLNDLY
>gnl|CDD|269869 cd14721, bZIP_Fos, Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization domain. Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of Basic leucine zipper (bZIP) dimers of the Jun and Fos families, and to a lesser extent, the activating transcription factor (ATF) and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. There are four Fos proteins: c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2. In addition, FosB also exists as smaller splice variants FosB2 and deltaFosB2. They all contain an N-terminal region and a bZIP domain. c-Fos and FosB also contain a C-terminal transactivation domain which is absent in Fra-1/2 and the smaller FosB variants. Fos proteins can only heterodimerize with Jun and other AP-1 proteins, but cannot homodimerize. Fos:Jun heterodimers are more stable and can bind DNA with more affinity that Jun:Jun homodimers. Fos proteins can enhance the trans-activating and transforming properties of Jun proteins. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KRRVRRERNKLAAAKCRQRRVDLTNTLQAETEQLEDEKSSLQNEIANLQKQKEQLEFLLAAH
>gnl|CDD|269870 cd14722, bZIP_ATF3, Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar proteins: a DNA-binding and dimerization domain. ATF-3 is a Basic leucine zipper (bZIP) transcription factor that is induced by various stress signals such as cytokines, genetoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. Mice deficient with ATF3 display increased susceptibility to endotoxic shock induced death. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
RRRRRRERNKVAAAKCRNKKKERTDCLQKESEKLETQNAELKRQIEELKNEKQHLIDMLNLH
>gnl|CDD|271240 cd14723, ZIP_Ppr1, Leucine zipper Dimerization coil of Ppr1-like transcription factors. Ppr1/Ppr1p activates transcription of the URA1, URA3, and URA4 genes, which encode enzymes involved in the regulation of pyrimidine levels. Also included in this subfamily is Colletotrichum acutatum Nir1 which plays a role during nitrogen-starvation conditions. Proteins in this subfamily are members of the Gal4p family of transcriptional activators which contain an N-terminal DNA-binding domain with a Zn2Cys6 binuclear cluster that interact with CCG triplets and a leucine zipper-like heptad repeat that dimerizes. Dimerization allows binding of targets which contain two CCG motifs oriented in an inverted (CGG-CCG), direct (CCG-CCG), or everted (CCG-CGG) manner
VPRSYVVYLEDRVAELEAQLASHGI
>gnl|CDD|271241 cd14724, ZIP_Gal4-like_1, Leucine zipper Dimerization domain of Gal4-like transcription factors. The Gal4p family of transcriptional activators contain an N-terminal DNA-binding domain with a Zn2Cys6 binuclear cluster that interact with CCG triplets and a leucine zipper-like heptad repeat that dimerizes. Dimerization allows binding of targets which contain two CCG motifs oriented in an inverted (CGG-CCG), direct (CCG-CCG), or everted (CCG-CGG) manner. Gal4p family members are involved in the activation of genes in response to a specific signal. Gal4p functions in the induction of GAL genes in the presence of galactose; GAL proteins are responsible for the transport of galactose into the cell and for its metabolism through the glycolytic pathway. Hap1p promotes transcription of genes required for respiration and controlling oxidative damage in response to heme. Put3p activates the transcription of PUT1 and PUT2 genes in the presence of proline, allowing yeast cells to use proline as a nitrogen source. Sip4p activates target genes under conditions of glucose deprivation while Nir1 plays a role during nitrogen-starvation conditions. This subfamily is composed of uncharacterized members of the Gal4p family
LQSELDYLRERIRELEASLEEQSR
>gnl|CDD|271242 cd14725, ZIP_Gal4-like_2, Leucine zipper Dimerization coil of Gal4-like transcription factors. The Gal4p family of transcriptional activators contain an N-terminal DNA-binding domain with a Zn2Cys6 binuclear cluster that interact with CCG triplets and a leucine zipper-like heptad repeat that dimerizes. Dimerization allows binding of targets which contain two CCG motifs oriented in an inverted (CGG-CCG), direct (CCG-CCG), or everted (CCG-CGG) manner. Gal4p family members are involved in the activation of genes in response to a specific signal. Gal4p functions in the induction of GAL genes in the presence of galactose; GAL proteins are responsible for the transport of galactose into the cell and for its metabolism through the glycolytic pathway. Hap1p promotes transcription of genes required for respiration and controlling oxidative damage in response to heme. Put3p activates the transcription of the PUT1 and PUT2 genes in the presence of proline, allowing yeast cells to use proline as a nitrogen source. Sip4p activates target genes under conditions of glucose deprivation while Nir1 plays a role during nitrogen-starvation conditions. This subfamily is composed of uncharacterized members of the Gal4p family
SKSRTQLLREKIARLEARIRELES
>gnl|CDD|350608 cd14726, TraB_PrgY-like, TraB/PryY confer plasmid-borne pheromone resistance. TraB/PrgY proteins, identified in gut bacterium Enterococcus faecalis, are plasmid-borne homologs that are induced by pheromones. Induction rends the host bacterium insensitive to self-induction by its own pheromones, and prevents the transfer of the pheromone-inducible conjugative plasmids to bacteria that already contain it. Based on homology to Tiki activity, it has been proposed that TraB acts as a protease in the inactivation of mating pheromone, cleaving at the amino-terminus. The pheromones are small peptides (7-8 residues) encoded by the bacterial genome, and are specific for particular plasmids, or class of plasmids, which may contain several virulence factors and disseminate rapidly. Plasmid-borne antibiotic resistance and virulence determinants make these elements important contributors to medical problems. Trab/PrygY is a member of a Tiki-like superfamily. Tiki is a membrane-associated metalloprotease (MEROPS family M96) that inhibits Wnt via the cleavage of its amino terminus. Wnt is essential in animal development and homeostasis. In Xenopus, Tiki is critical in head development. In human cells, Tiki inhibits Wnt-signaling. Tiki proteins are also related to erythromycin esterase, gumN plant pathogens, RtxA containing toxins, and Campylobacter Jejuni ChaN heme-binding protein
VYLVGTAHVSKESAEEVREVIREVKPDVVAVELCESRYEALLDPERWKNTDIKKVIKEKKGFLLLANLLL
SSFQKKIGKELGVKPGAEFRAAIEEAEEVGAPVVLGDRDIQITLKRAWDVLEELLSELAEEFPELKEVLI
DERDQYLAHSLRRAAAGGKKVVAVVGAGHVPGIERLL
>gnl|CDD|350609 cd14727, ChanN-like, ChaN is an iron-regulated, heme-binding protein. This family represents a domain found in ChaN, a heme-binding/iron-regulated lipoprotein from Campylobacter jejuni. ChaN, possibly involved in the uptake of heme-iron, contains a pair of cofacial heme groups situated between two ChaN monomers. A single tyrosine residue contacts the heme-bound iron atom while the heme-binding regions of each monomer also have contacts to the heme in the complementary monomer. ChaN presumably associates with an outer membrane-associated receptor, ChaR. Campylobacter jejuni is an important cause of food-borne illness, and is dependent on iron uptake from the host. ChaN like proteins are related to the Tiki/TraB like family of proteases. Proteins containing this domain also include protein reticulata-related from Arabidopsis which may play a role in leaf development
DVVLLGEVHDNPAHHRLQLELLRALAARGPRLALGLEMFERDQQPVLDEYLAGEISEEELELLDWARGWP
NYFTLYRPLFEFARENGLPVVALNVPREYVRKVAREGLESLDEEERALLPLDIDLPDPAYRARLEAVFGG
HCGGLPEEMFENFVEAQALWDATMAESIAEALKANPGGPVVVIAGSGHVRYGLGIPARLARRAPPKVAVV
L
>gnl|CDD|350610 cd14728, Ere-like, Erythromycin esterase and succinoglycan biosynthesis related proteins. This group contains erythromycin esterase, which shares conserved active site residues of the Tiki/TraB family. Erythromycin esterases (EreA and EreB) disrupt erythromycin via the hydrolysis of the macrolactone ring. A critical catalytic histidine acts as a general base in the activation of a water molecule. Macrolides act by inhibiting bacterial protein synthesis by binding at the exit tunnel of ribosomal subunit 50s, blocking the translation of the polypeptide. Erythromycin esterase, typically found in integrons and transposons, confers antibiotic resistance through the disruption of the drug ring structure. EreB substrate profile is substantially broader than that for EreA, being able to also metabolize semisynthetic derivatives such as azalide azithromycin
LGDARIVGLGEATHGTREFFQLKHRLFRYLVEEKGFRVFALEADFGEALAVNDYVRGGEGDLDEALKSLG
FWIWRTEEMLDLLEWLREYNATRPEDKVRFYGFDMQSPRPSLDAVLDYLRKVDPELLAELEELLAALAPF
GDDSAAYAAAALDEAEADELRALLDDLRARLAALAPEREEYALALQNARVLEQALEYYRAMAKGGAESWN
LRDRAMAENLLWLLEHEGPGGKIIVWAHNGHIAKAPSTDMGDLGYKSMGQLLRERLGDDYYSIGFTFGSG
SFAAADPWGGPMRVFPLPPPPPGSLEALLAQAGLPDFFLDLRARRLLRRPRLLRAIGVGYRPRTERGEGY
VPADLAEAFDGLIFIDE
>gnl|CDD|350611 cd14729, RtxA-like, C2-2 like domain of various multidomain toxins, including RTX-containing like proteins. This group contains mostly poorly-characterized C2-2 like domains of multidomain bacterial toxins, including Pasteurella multocida toxin PMT (also known as dermonecrotic toxin), MARTX (multifunctional-autoprocessing repeats-in-toxin holotoxin RtxA) proteins from Vibrio vulnificus, as well as bacterial effector protein from Pseudomonas syringae (type III effector HopAC1). MARTX domains at the N- and C- termini act in the translocation of the central domain across the eukaryotic plasma membrane, where it is proteolytically released. These are related to Pasteurella multicida toxin, which has structural and sequence similarity to the TIKI/TraB family of proteases. However, while this group of multidomain proteins shows fairly strong conservation of the active site residues of this family, the Pasteurella multicida toxin does not
GLVIGESHGSIASKRFLIDNMAALKRQGVKTLYLEHLLTDLHQADLDDFNRTGEMSPALKDYLRTLDRGH
GTDPDGPYTYLELVEAARKHGIRVVALDCAASYRLKGALDDSPRRLKEFNYYAHRVIEQDQAANGPEKWV
ALVGAAHANTFEGVPGLAELTGAISLRVED
>gnl|CDD|269830 cd14730, LodA_like, L-lysine epsilon-oxidase from Marinomonas mediterranea and similar proteins. L-lysine epsilon-oxidase is responsible for oxidative deamination of L-lysine, producing L-2-aminoadipate-6-semialdehyde. Hydrogen peroxide is a side-product of this enzymatic reaction, which requires the cofactor CTQ (cysteine tryptophylquinone). CTQ most likely forms a Schiff base with the free amino acid substrate. The protein is also called marinocine, for its broad-spectrum antibacterial activity; the latter is most likely caused by hydrogen peroxide synthesis. Homologs of LodA have been detected in various gram-negative bacteria, and they appear to be associated with the formation of biofilms
TRYRIHPAIGIARLGNSEDEYFLGPEVPGGPPSPPGGPVEGGFRDSAGRIKRQAARFRVFAYDDDDKVLG
EVTLDSVATIEWTVHLANKKAAWYTFRGPYGADPTALRNPNQQSKATGPARDGLIIDPGPRSISGANEIA
TNLDGTFDDGSFPGSTPVELGELRTDDAGRLIVLGGYGKSGSPTGGPPIISYANNDGWYDDTSDGPVTAT
VTLPDGTTVPAAGGAWVVVAPPDFAPGIGNVVTLYDVIEDVAVRAFGLPPPDAVPSFYRDIYPILQRASL
YRWVNSEANQGHKPGGHGNFLPDELALADPSEAGKAARQRIFNRLRAPDNKDPDALPELPLMPRLSGDGG
DALPPGPPRQFLALTRLQYDRLRKWADGNFEADWPPDPPGDVDLDIQPEALDRAALENCVGGPFFPGIEM
TWIARDPSTYAEPFRIDHDPEISNHTTVEPGDLTAGMALPWQADFLQCNTEWWPAYWDMVRPWSRLGFVV
KTKDTVIGGGEVFVETERD
>gnl|CDD|269831 cd14731, LodA_like_1, Uncharacterized proteins similar to L-lysine epsilon-oxidase from Marinomonas mediterranea. L-lysine epsilon-oxidase is responsible for oxidative deamination of L-lysine, producing L-2-aminoadipate-6-semialdehyde. Hydrogen peroxide is a side-product of this enzymatic reaction, which requires the cofactor CTQ (cysteine tryptophylquinone). CTQ most likely forms a Schiff base with the free amino acid substrate. The protein is known for its broad-spectrum antibacterial activity; the latter is most likely caused by hydrogen peroxide synthesis. Although members of this related family share features of the active site, their functions are not known. Homologs of LodA have been detected in various gram-negative bacteria, and they appear to be associated with the formation of biofilms
DSEIVRAAIYPAIGIARVGNSPDEYFIGPEVPGPPPAPPGGYRDATGAIKRQAARFRIYGYNAAGEVVRE
LTADDADIEWTVHVANKKAAWYQFQNALDIPEAAPAPPGLRNPNVPSTRRNPLVIDPGPRSISGRNTNLG
GEYAFDDGKFMGKTVYLGELRTDDQGRLLVLGGDGVSASPTPGAPPTTFANNDGWYDDTSDGPVTATVTL
DGGDLPVEPAWVVVAPPNYAPGIKSVRTMYDLMRDVAVEAGWLPRPTRPSFTRDILPILERLSGLQWVNA
GFAAGFGWGGPFDFTSPALIARLADPSDANAELRRQVFNSFRDPDNDGASPLKWPWLYGDAVGYPPAGSP
RQWLALTPTQYAHLEQWAEGDFTADWDPDAPPPRSLDDVPLAEQPAMLTRAALEFCLGGAFHPGCELTWP
MRHASMYSAPFRIRHRAPAGEPEQDYGPTLTPATALGPDGPLYAQGPGDLTRWMAVPWQTDTASCRSGYD
PEYDPYLPTFWPARVPNQVLSEEDYEIVMDTALPREERLKAFARRADWLLRHLGGGYTDQLNNMITLWDK
LGVVEPRPGPKDDPDFPAVVYVESGRG
>gnl|CDD|269832 cd14732, LodA, L-lysine epsilon-oxidase from Marinomonas mediterranea and similar proteins. L-lysine epsilon-oxidase is responsible for oxidative deamination of L-lysine, producing L-2-aminoadipate-6-semialdehyde. Hydrogen peroxide is a side-product of this enzymatic reaction, which requires the cofactor CTQ (cysteine tryptophylquinone). CTQ most likely forms a Schiff base with the free amino acid substrate. The protein is also called marinocine, for its broad-spectrum antibacterial activity; the latter is most likely caused by hydrogen peroxide synthesis. The dimerization interface observed in the available 3D structure does not seem to be conserved. Homologs of LodA have been detected in various gram-negative bacteria, and they appear to be associated with the formation of biofilms
TTYRIHPAIGIARVGNSSEEFYLAPETIAGLPIECDAQGNGLPTESTPITSDDFRDAQGRIKRQAARFRI
YAYDDESGQGREVTLGSPVDGKKVKDIEWTVHLANKKAAWYEFVELQGELGYGPGNSYPLRNPLRNADPT
DPARRQKLIIDPGPRAISGTTGQVRFDRATVGTITIPPDYPGSFPPDGLAPPGGPIDTLGELRTDAKGRL
LVLGGYGRAGGFDKGDGAPPITGYANNDGWFDDTSDGPVTAVLVFDDGSIEVELPAWVVVGDPAYAPQIL
NVVTLWDTIYDTWVRKFGLVPDLYDNGGKAFNPDYKPNFDRDILPILRRASLYQWVANLPSMAIFAQFDA
HDASDANRANRQYILDYLRKPGEDNPNQSISGSGAPLMPLNSGDNSVSNTTISKFLTLTDTQYFLLQQWA
AGKFVNEPPEKLGPGEALDRAVLGNCVGGPFSPGIEVTWIVRNPAIYQEPYRIKGAGPFRIFAQTLDYAN
QPYLGLSPSPDPDEGGGLEPGDLTKFMAIPWQADFNECSTQTINPNPPSVNKLAGTGIPGPPTTLYWWWP
AQRPVAVYTGDDTQNDQLLLQRQSVRGHGPAGQQVNYARGFQSYSDMVTNWSKLGFIIQGNAIDDDSYGF
PYFLEVERN
>gnl|CDD|350515 cd14733, BACK, BACK (BTB and C-terminal Kelch) domain. The BACK domain is found in architectures C-terminal to a BTB domain, in a diverse set of architectures together with Kelch, MATH, and/or TAZ domains. It is involved in interactions with the Cullin3 (Cul3) ubiquitin ligase complex, as well as in homo-oligomerization. Most proteins containing the BACK domain are understood to function as adaptor proteins that play a role in ubiquitination of various substrates
DPENCLGILELADLYNLEELKEKALKFILENFEEVSKSEEFLELSVELLLELLSS
>gnl|CDD|350516 cd14736, BACK_AtBPM-like, BACK (BTB and C-terminal Kelch) domain found in plant BTB/POZ-MATH (BPM) protein family. The BPM protein family includes Arabidopsis thaliana BTB/POZ and MATH domain-containing proteins, AtBPM1-6, and similar proteins. BPM protein, also termed protein BTB-POZ and MATH domain, may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins
CEGVDVNTVATTLALAEQHHASQLKAVCLKFVARNLAAVMQTDGFEYLKESCPSLQSELLKT
>gnl|CDD|269822 cd14737, PAAR_1, proline-alanine-alanine-arginine (PAAR) domain. This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli
PAAARLGDICTGHGGFPPTPVIAGSPDVTVNGKPVLRQGDALAPHTCPKHPPHGGVIASGSSTVFINGKP
AARVGDPVSCGGTVAGGSPNVFIG
>gnl|CDD|269823 cd14738, PAAR_2, proline-alanine-alanine-arginine (PAAR) domain. This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli
PAARIGDMHVCPMVVTGPVPHVGGPIVGPGPTTVLIGGLPAARVGDMCVCVGPPDTIVQGSSTVLIGGKP
AARMGDSTAHGGVIVSGVPTVLIG
>gnl|CDD|269824 cd14739, PAAR_3, proline-alanine-alanine-arginine (PAAR) domain. This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli
AAARVGDPTTHGGTITGPGVPTVLIGGMPAAVVGDMHACVIPPPPAHPPASPFPPGSATVLIGGRPAARV
GDACGCGATIVVGAPTVLIG
>gnl|CDD|269825 cd14740, PAAR_4, proline-alanine-alanine-arginine (PAAR) domain. This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family of bacteria, and forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). A few members contains C-terminal domain extensions corresponding to Rearrangement hotspot (Rhs) protein repeats and conserved Rhs repeat-associated unique core sequences as well as uncharacterized domains such as DUF4150. However, these terminal domains are exposed to solution, and do not distort the binding site of VgrG. Rhs and related YD-peptide repeat proteins are widely distributed in bacteria. Rhs shares similar architecture with distantly related WapA proteins of Bacillus and Listeria species, suggesting intercellular growth inhibition as its primary function. Additionally, a plasmid-encoded Rhs protein has been implicated in bacteriocin production in Pseudomonas savastanoi. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes
PAARLGDPVVGDDIHIVLSPPGPVPTPLPHPGAGLIVGGLSPTVLIGGMPAATVGSTAGNTPGGVPGGPS
VPPANPGTIVMGSSTVFINGKPAARMGDMTATCNDPAPAPVGTVVPPGATV
>gnl|CDD|269826 cd14741, PAAR_5, proline-alanine-alanine-arginine (PAAR) domain. This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family in bacteria as well as some archaea, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli
PPAARIGDSTAHGGPLTPGPGSPNVLIGGFPAWRAGGDGHVCPLVTGPVPHVGGVVAAGSTTVLINGLPA
ARMGDMIVEGGPPNTIAMGAPTVLI
>gnl|CDD|269827 cd14742, PAAR_RHS, proline-alanine-alanine-arginine (PAAR) domain, also containing C-terminal Rearrangement hotspot (Rhs) extensions. This PAAR (proline-alanine-alanine-arginine) repeat subfamily, which forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS), contains C- and N-terminal domain extensions. These include Rearrangement hotspot (Rhs) protein repeats and conserved Rhs repeat-associated unique core sequences at the C-terminal, and various predicted functions at N- and C-terminal extensions. However, these terminal domains are exposed to solution, and do not distort the binding site of VgrG. Rhs and related YD-peptide repeat proteins are widely distributed in bacteria. Rhs shares similar architecture with distantly related WapA proteins of Bacillus and Listeria species, suggesting intercellular growth inhibition as its primary function. Additionally, a plasmid-encoded Rhs protein has been implicated in bacteriocin production in Pseudomonas savastanoi. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes
PAARVGDPIAHTGTITSGSPNVFINGKPAARAADSTVACSKHPPPPQLIAEGSETVFINGQPAARKGDKT
TCSAVISEGSPNVFIG
>gnl|CDD|269828 cd14743, PAAR_CT_1, proline-alanine-alanine-arginine (PAAR) domain with C-terminal extension. This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family of mostly gamma-proteobacteria, and forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). Some members contains C-terminal domain extensions corresponding to Rearrangement hotspot (Rhs) protein repeats and conserved Rhs repeat-associated unique core sequences as well as uncharacterized domains. However, these terminal domains are exposed to solution, and do not distort the binding site of VgrG. Rhs and related YD-peptide repeat proteins are widely distributed in bacteria. Rhs shares similar architecture with distantly related WapA proteins of Bacillus and Listeria species, suggesting intercellular growth inhibition as its primary function. Additionally, a plasmid-encoded Rhs protein has been implicated in bacteriocin production in Pseudomonas savastanoi. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes
PAARVGDPHACPLPGHGSTPIGSSSADFFDGLPAARVGDKTSCGATIVSGSINVLINGKPAAVLGSTTSH
GGVVIGGS
>gnl|CDD|269829 cd14744, PAAR_CT_2, proline-alanine-alanine-arginine (PAAR) domain with uncharacterized C-terminal extension. This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family of mostly beta- and gamma-proteobacteria, and forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). Most members contain C-terminal domain extensions corresponding to several uncharacterized domains such as S-type pyocin, DUF2235, DUF2345 and cytotoxic proteins. However, these terminal domains are exposed to solution, and do not distort the binding site of VgrG. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes
RGIIRLGDKTTHGGVVISGSSTFTIDGRPVARVGDKVTCPKCKGTGPIVEGGPTFTVDGRPVALDGDRVA
CGCPLIPS
>gnl|CDD|270613 cd14745, GH66, Glycoside Hydrolase Family 66. Glycoside Hydrolase Family 66 contains proteins characterized as cycloisomaltooligosaccharide glucanotransferase (CITase) and dextranases from a variety of bacteria. CITase cyclizes part of a (1-6)-alpha-D-glucan (dextrans) chain by formation of a (1-6)-alpha-D-glucosidic bond. Dextranases catalyze the endohydrolysis of (1-6)-alpha-D-glucosidic linkages in dextran. Some members contain Carbohydrate Binding Module 35 (CBM35) domains, either C-terminal or inserted in the domain or both
RFPRYGFLSDFDSDSEEDIEKEIDQLNRYHINGLQFYDWMYRHHKPLPGTVGQPAETWKDWANRPVSLST
VKGYINAAHSKGMKAMAYNMIYAALKDYEDDGVSPEWALYKDDGHTDQDSHDLPDDWKSNLYIMNPANPG
WQNYIIAQYKKVYKVFGFDGWHIDQLGDRGTVYDYDGNSVDLSDGYASFINAAKEALPDKYLVFNAVSGY
GQEEIAGSKVDFLYTEVWPPDETYGDLKRVIDQNRELSNGKSTVLAAYMNYFKADGLTSGEFNTPSVLLT
DAVIFASGGSHLELGEGNHMLLTEYFPNNNLSMSEELKAALRRYYDFLVAY
>gnl|CDD|270450 cd14747, PBP2_MalE, Maltose-binding protein MalE; possesses type 2 periplasmic binding fold. This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TLTVWAMGNSAEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFA
AMGALEDLTPYLEDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPKTWDELE
AAAKKIKADGPDVSGFAIPGKNDVWHNALPFVWGAGGDLATKDKWKATLDSPEAVAGLEFYTSLYQKGLS
PKSTLENSADVEQAFANGKVAMIISGPWEIGAIREAGPDLAGKWGVAPLPGGPGGGSPSFAGGSNLAVFK
GSKNKDLAWKFIEFLSSPENQAAYAKATGMLPANTSAWDDPSLANDPLLAVFAEQLKTGKATPATPEWGE
IEAELVLVLEEVWIGVGADVEDALDKAAAEINEILN
>gnl|CDD|270451 cd14748, PBP2_UgpB, The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold. This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
EITFWHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQL
ADSGALEPLDDYIDKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTW
DELEEAAKKLKDKGGKTGRYGFALPPGDGGWTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLV
GKDGVSPLNDWGDAQDAFISGKVAMTINGTWSLAGIRDKGAGFEYGVAPLPAGKGKKGATPAGGASLVIP
KGSSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAEDPEEFLAENPNYKVAVDQLDYAKPWGPPV
PNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI
>gnl|CDD|270452 cd14749, PBP2_XBP1_like, The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold. This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose _ xylobiose _ xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TITYWQYFTGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAE
FVKAGLLLPLTDYLDPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPKTWDE
LIEAAKKDKFKAKGQTGFGLLLGAQGGHWYFQYLVRQAGGGPLSDDGSGKATFNDPAFVQALQKLQDLVK
AGAFQEGFEGIDYDDAGQAFAQGKAAMNIGGSWDLGAIKAGEPGGKIGVFPFPTVGKGAQTSTIGGSDWA
IAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLLPAKEVVAKDEDPDPVAILGPFADVLNAAGSTPFL
DEYWPAAAQVHKDAVQKLLTGKIDPEQVVKQAQSAAAK
>gnl|CDD|270453 cd14750, PBP2_TMBP, The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold. This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TITFAAGSDGQEGELLKKAIAAFEKKHPDIKVEIEELPASSDDQRQQLVTALAAGSSAPDVLGLDVIWIP
EFAEAGWLLPLTEYLKEEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEPPKTWDEL
LEAAKKRKAGEPGIWGYVFQGKQYEGLVCNFLELLWSNGGDIFDDDSGKVTVDSPEALEALQFLRDLIGE
GISPKGVLTYGEEEARAAFQAGKAAFMRNWPYAYALLQGPESAVAGKVGVAPLPAGPGGGSASTLGGWNL
AISANSKHKEAAWEFVKFLTSPEVQKRRAINGGLPPTRRALYDDPEVLEAYPFLPALLEALENAVPRPVT
PKYPEVSTAIQIALSAALSGQATPEEALKQAQEKL
>gnl|CDD|270454 cd14751, PBP2_GacH, The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold. This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis
TITFWHTSSDEEKVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFA
KLGYLQPLDGTPAFDDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVPKTMDELVAA
AKAIKKKKGRYGLYISGDGPYWLLPFLWSFGGDLTDEKKATGYLNSPESVRALETIVDLYDEGAITPCAS
GGYPNMQDGFKSGRYAMIVNGPWAYADILGGKEFKDPDNLGIAPVPAGPGGSGSPVGGEDLVIFKGSKNK
DAAWKFVKFMSSAEAQALTAAKLGLLPTRTSAYESPEVANNPMVAAFKPALETAVPRPPIPEWGELFEPL
TLAFAKVLRGEKSPREALDEAAKQWD
>gnl|CDD|270212 cd14752, GH31_N, N-terminal domain of glycosyl hydrolase family 31 (GH31). This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite-1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket
DIVRVRITPLRLSFKLPPDEHFYGLGERFGGLNKRGKRYRLWNTDQGGYRGSTDPLYGSIPFYLSSKGYG
VFLDNPSRTEFDFGSEDSDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG
>gnl|CDD|271288 cd14755, GS_BA2291-HK-like, Non-heme globin sensor domain of BA2291 histidine kinase and related domains. This subfamily includes the sensor domain of Bacillus anthracis BA2291 histidine kinase. BA2291 is one of the most active kinases in promoting sporulation, and is found in most members of the Bacillus cereus subfamily of the genus Bacillus, which includes B. anthracis and Bacillus thuringiensis, but not Bacillus subtilis. This subfamily also includes two sensor-only plasmid encoded sporulation inhibitors pXO1-118 and pXO2-61 found only in B. anthracis and various strains of Bacillus cereus having similar plasmids. The pXO1-118 and pXO2-61 sensor domains form homodimers, and in vitro bind fatty acid and halide, and not heme; there may be roles for fatty acid (or similar molecule), chloride ion, and possibly pH, as signaling cues. It has been proposed that BA2291 senses the same environmental cue in vivo, and that pXO1-118 and pXO2-61 act by titrating out an environmental signal that might cause an ill-timed sporulation
AKKRLLDFLEEHQENFLSEWEKRILISEDDPFKEEIRKNGEAMLELVIEYLREEISEEYIKQLAYKVAEE
RVDANINIGDFVYNVNLGRSLIFKYLFKLNLPWDELQPIIDKINQCFDKFLYYAVSKYTELK
>gnl|CDD|381270 cd14756, TrHb, Truncated Mb-fold globins, T family. The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. They are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). Typical of the TrHb1s (N) group is a protein matrix tunnel. An example of a TrHb1 is Mycobacterium tuberculosis TrHb1/Mt-trHbN which is expressed during the Mycobacterium stationary phase, and plays a specific defense role against nitrosative stress. TrHb2s include the dimeric Arabidopsis thaliana TrHb2 AtGLB3. GLB3 is likely to have a function distinct from other plant globins: it exhibits a low O2 affinity, an unusual concentration-independent binding of O2 and CO, and does not respond to any of the treatments that induce plant 3-on-3 globins. TrHb3s include Campylobacter jejuni Ctb, encoded by Cj0465c, which may play a role in moderating O2 flux within C. jejuni
EKIGGEEAIEALVEIFYEKVLADPRLKPIFPNTDMKEHKAKQGDFLAGYLGGPNDHGGPMMRRRHLGLPI
TNEHFDAWLSLLADALDEVGVNPEMRNEILAVIEMTARHMQ
>gnl|CDD|381271 cd14757, GS_EcDosC-like_GGDEF, Globin sensor domain of Escherichia coli Direct Oxygen Sensing Cyclase and related proteins; coupled to a C-terminal GGDEF domain. Globin-coupled-sensors belonging to this subfamily have a C-terminal diguanylate cyclase (DGC/GGDEF) domain coupled to the globin sensor domain. DGC/GGDEF likely functions as a c-di-GMP cyclase in the synthesis of the second messenger cyclic-di-GMP (c-di-GMP). Members include Escherichia coli DosC (also known as YddV), the gene for which is found in a two-gene operon, dosCP. In DosC, the sensory globin domain is coupled to a GGDEF-class diguanylate cyclase, while in DosP, a heme-containing PAS domain is coupled to an EAL-class c-di-GMP phosphodiesterase. DosP and DosC associate in a di-GMP-responsive Escherichia coli RNA processing complex along with polynucleotide phosphorylase (PNPase), enolase, RNase E, and RNA
ERLAAEWQALLQQVSPAVRALVAALVQAHADALAAEFYDTMLADPEASPFLSHEQVQTRLHASLQRWLIE
LFSAADDEDLEALVARQRKVGEVHARIGIPVHLVMRGARVLKRRLAELLAASALSRAELLQAVRYVSEVI
DLAMEIMSR
>gnl|CDD|381272 cd14758, GS_GGDEF_1, Globin sensor domain, coupled to DGC/GGDEF domains; uncharacterized subgroup. Globin-coupled-sensors belonging to this subfamily have a sensor domain coupled to a C-terminal diguanylate cyclase (DGC/GGDEF) domain. DGC/GGDEF likely functions as a c-di-GMP cyclase in the synthesis of the second messenger cyclic-di-GMP (c-di-GMP)
EIEQRKSLLSLTEEDLAQLRALKPLIEPNLDDIVDEFYDHQTSVPEIALLIGDADTLQRLKNAQRQYVLD
LFSGEYDLEYVNNRLRIGLVHKRIGVEPKLYLSAINTLKEILFEYIREYIEDCLPANQILESLEKLMLFD
ITLVFDTY
>gnl|CDD|381273 cd14759, GS_GGDEF_2, Globin sensor domain, coupled to DGC/GGDEF domains; uncharacterized subgroup. The majority of globin-coupled-sensors in this subfamily have diguanylate cyclase (DGC/GGDEF) domains N-terminal to the globin sensor domain and/or C-terminal EAL domains, DGC/GGDEF and EAL domains are involved in the synthesis and degradation of the secondary messenger c-di-GMP, respectively. Some members have GAF small-molecule-binding domains in addition
GALEEEFDPYGPEAAALLGRHRPLLERAAEDFVEAFYDDLAADPEARAILSALSPEELEHLKARQAEHLR
FLLSPDLTREAHRTRARRVGRIHALVGVDASLLLEAMSLYRRLLAELLDQSGLSPRDRYRLLLIAEARLQ
DDLQWQLEAA
>gnl|CDD|271293 cd14760, GS_PAS-GGDEF-EAL, Globin sensor domain; coupled to PAS, DGC/GGDEF and EAL domains. In addition to the N-terminal sensing domain, globin-coupled-sensors in this bacterial subfamily have a signal-sensing PAS domain, and diguanylate cyclase (DGC/GGDEF) and EAL domains. The latter two domains are involved in the synthesis and degradation of c-di-GMP, respectively, and may be involved in regulating cell surface adhesiveness, and in the transition between planktonic and biofilm growth modes
IRRRKAFLGFTEADASRLRALHAALSSFSPTFADSFYAHLLSFEETRRFLPDEDTLERLQRAQTAYFDSL
TAGRYDSDYIRERLRVGLTHQRIGLSPQWYLGAYVKYLSDLLPEIRQLLGADPDEFIAALQSLLKVVMLD
MGLALDTY
>gnl|CDD|381274 cd14761, GS_GsGCS-like, Globin sensor domain of Geobacter sulfurreducens globin-coupled-sensor and related proteins. GsGCS is a GCS of unknown function, comprised of an N-terminal globin sensor domain and a C- terminal transmembrane signal-transduction domain. For GCSs in general, the first signal O2 binds to/dissociates from the heme iron complex inducing a structural change in the globin domain, which is then transduced to the functional domain, switching on (or off) the function of the latter. Ferric GsGCS is bis-histidyl hexa-coordinated (provided by a His residue located at the E11 topological site, as distinct from the E7 site). Ferrous GsGCS is a penta- and hexa-coordinated mixture. The C-terminal domains of other members of this subfamily include histidine kinase, and PsiE domains
ENIEEIKAHYNFTEEDAENLKSLKPLMEKNKDRFVEDFYEYLFKFPDTAKFLKDDEVLKRHKEKLKVWFI
RLFSGKYDNQYFDYLQRIGQVHVRIGLPTHYVNAAMNFVRRFFHEKIFQEFSDDEKRKKLLESVEKILDI
NLDIMTSSY
>gnl|CDD|381275 cd14762, GS_STAS, Globin sensor domain; coupled to a STAS domain. Globin-coupled-sensors in this subfamily have a C-terminal sulphate transporter and anti-sigma factor antagonist (STAT) domain coupled to the globin sensor domain
ASYYKQQFFISDEDLELIRSAGQQILDQKDWIFDEFYDWMRSQPEYSEYFSEEVIKRLKSLQDIFWEDFL
SGRVDDEYIERRRRIGEVHARIGLPLEAYLAGVAAFHELIEEAFRRLGLASFELMQAFKKFIQLDIAIVT
DVY
>gnl|CDD|381276 cd14763, SSDgbs_1, Sensor single-domain globins; uncharacterized bacterial subgroup. This subfamily of sensor single-domain globins, belongs to a family that includes GCSs (globin-coupled-sensors) and single-domain protoglobins (Pgbs). For GCSs, an N-terminal heme-bound oxygen-sensing/binding globin domain is coupled to a C-terminal functional/signaling domain. The first signal O2 binds to/dissociates from the heme in its sensor domain inducing a conformational change in that domain and ultimately in the signaling domain. It has been demonstrated that the Pgbs and other single domain globins can function as sensors, when coupled to an appropriate regulatory domain
LAELLRRVGLTPEDAQLLGSLAPIAKEIAPQMADAFYDYLGRDPETAEILAAVPGRVERLHKTFANWFRE
LFSGQYDAAYAERRLRIGLVHVRIGLPPRYPIPAMGVVVPLGLQHLRAAAEPEAAVEAFGKILALDIALF
EQAY
>gnl|CDD|381277 cd14764, SSDgbs_2, Sensor single-domain globins; uncharacterized subgroup. This subfamily of sensor single-domain globins, belongs to a family that includes GCSs (globin-coupled-sensors) and single-domain protoglobins (Pgbs). For GCSs, an N-terminal heme-bound oxygen-sensing/binding globin domain is coupled to a C-terminal functional/signaling domain. The first signal O2 binds to/dissociates from the heme in its sensor domain inducing a conformational change in that domain and ultimately in the signaling domain. It has been demonstrated that the Pgbs and other single domain globins can function as sensors, when coupled to an appropriate regulatory domain
LEQMPPETRFRPEDAEIIRRHRPLLLSWADELVQGFYDTLFAHPPTRAVFREGERPEREKTLRDWWRRTV
EGPFDEHYWAWQALVGLVHVRRKVTNPMMLGMWSWVVNFVLKKALEHLSQNEALVVTGAFQRLAATVGAL
IAEGY
>gnl|CDD|381278 cd14765, Hb, Hemoglobins. Hb is the oxygen transport protein of erythrocytes. It is an allosterically modulated heterotetramer. Hemoglobin A (HbA) is the most common Hb in adult humans, and is formed from two alpha-chains and two beta-chains (alpha2beta2). An equilibrium exists between deoxygenated/unliganded/T(tense state) Hb having low oxygen affinity, and oxygenated /liganded/R(relaxed state) Hb having a high oxygen affinity. Various endogenous heterotropic effectors bind Hb to modulate its oxygen affinity and cooperative behavior, e.g. hydrogen ions, chloride ions, carbon dioxide and 2,3-bisphosphoglycerate. Hb is also an allosterically regulated nitrite reductase; the plasma nitrite anion may be activated by hemoglobin in areas of hypoxia to bring about vasodilation. Other Hb types are: HbA2 (alpha2delta2) which, in normal individuals, is naturally expressed at a low level; Hb Portland-1 (zeta2gamma2), Hb Gower-1 (zeta2epsilon2), and Hb Gower-2 (alpha2epsilon2), which are Hbs present during the embryonic period; and fetal hemoglobin (HbF, alpha2gamma2), the primary Hb throughout most of gestation. These Hb types have differences in O2 affinity and in their interactions with allosteric effectors
EKSTIKALWGKVNVEEYGAEALARLFVVYPWTKRYFPKFDDSSSGNPKVKAHGKKVLGALGDAVKHLDDL
KNTFSDLSELHADKLHVDPENFKLLSDCLIVVLAAHLGKEFTPEVHAAWDKFLAVVAAALS
>gnl|CDD|381279 cd14766, CeGLB25-like, Caenorhabditis elegans globin GLB-25, and related globins. The C. elegans genome contains 33 genes encoding globins that are all transcribed. These are very diverse in gene and protein structure and are localized in a variety of cells. The C. elegans globin GLB-25 (locus tag T06A1.3), like the majority of them, was expressed in neuronal cells in the head and tail portions of the body and in the nerve cord
LKKSWKGIARKIDETGKTMFLRMLTENPELKELFPKLKNLEDEEDELRSSEILENHAARVMDTLDEAISN
IENVDYVIDLLHKVGKMHAKKPGFRPEMFWKIEEPFLEAVSETLGDRYTDNMENIYRKTIKFILQTL
>gnl|CDD|271300 cd14767, PE_beta-like, Phycoerythrin beta subunit, a component of the phycobilisome rod; and related proteins. phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). This subfamily also includes the beta subunits of Cryptophyte phycobiliproteins which represent another type of biliprotein antenna with different structure and organization. The beta subunits of cryptophyte PBPs share a high degree of sequence identity with both the alpha and beta subunits of the cyanobacterial and red algal PBPs, however the alpha cryptophyte subunits are shorter, and unrelated. There is only one type of PBP present in a single species, either phycocyanin or phycoerythrin, but not allophycocyanin. Structurally, phycoerythrin in cryptophytes is an alpha1alpha2betabeta dimer and not a trimer as in the PBS
MLDAFSRVVVNADSKAAYVGGSDLQALKTFISDGNKRLDAVNYIVSNASCIVSDAVSGMICENPGLISPG
GXCYTNRRMAACLRDGEIILRYVSYALLAGDASVLEDRCLNGLKETYIALGVPTNSNIRAVSIMKATAVA
FINNTASQRKLETPQGDCSALASEAASYFDKVTAAI
>gnl|CDD|271301 cd14768, PC_PEC_beta, Beta subunits of phycoerythrin and phycoerythrocyanin; phycobilisome rod components. phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC)
MLDAFTKVVAQADARGEFLSNAQIDALSAMVAEGNKRLDVVNRITSNASTIVSNAARALFAEQPQLIAPG
GXAYTNRRMAACLRDMEIILRYVTYAVFAGDASVLDDRCLNGLRETYQALGTPGSSVAVGVQKMKEAALA
IVNDPNGITPGDCSALMSEIATYFDRAAAAV
>gnl|CDD|271302 cd14769, PE_alpha, Phycoerythrin alpha subunit, a phycobilisome rod component. phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC)
MKSVITTVISAADAAGRFPSSSDLESVQGNIQRAAARLEAAEKLAANHEAVVKEAGDACFAKYPYLKNPG
EAGENQEKINKCYRDIDHYMRLINYCLVVGGTGPLDEWGIAGAREVYRALNLPTSAYVAAFAFTRDRLCV
PRDMSAQAGVEFSTALDYVINSLS
>gnl|CDD|271303 cd14770, PC-PEC_alpha, Alpha subunits of phycoerythrin and phycoerythrocyanin; phycobilisome rod components. phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC)
MKTPLTEAIAAADSQGRFLSNTELQAAFGRFRRATASLEAARALTSNADSLISGAAQAVYNKFPYTTQMQ
GPQYASTQTGKAKCARDIGYYLRMVTYCLVAGGTGPMDEYLIAGLDEINRTFDLSPSWYIEALKYIKANH
GLSGDAANEANTYIDYAINALS
>gnl|CDD|381280 cd14771, TrHb2_Mt-trHbO-like_O, Truncated hemoglobins, group 2 (O); Mycobacterium tuberculosis hemoglobin O like. The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). This group includes a Mycobacterium tuberculosis TrHb2, Mt-trHbO, encoded by the Mycobacterium tuberculosis glbO gene, which is expressed throughout the Mycobacterium growth phase. It also includes a TrHb2 from the thermophilic Thermobifida fusca (Tf-trHb) which has a high thermostability and at the optimal growth temperature for Thermobifida fusca (between 55 and 60 degrees C), it is capable of efficient O2 binding and release. Tf-trHb shares a relatively slow rate of oxygen binding with Mt-trHbO
FYEEVGGEDTFRRLVDAFYEGVAADEVLRPMYPEDDLEGAEERLRLFLEQYWGGPTTYSEERGHPRLRMR
HAPFPIGPAARDRWLEHMAAALDEVELPDPLREELWDYFERAAHAMINR
>gnl|CDD|381281 cd14772, TrHb2_Bs-trHb-like_O, Truncated hemoglobins, group 2 (O); Bacillus subtilis TrHb like. The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). TrHb2's belonging to this group include monomeric Bacillus subtilis trHb (Bs-trHb), which exhibits an extremely high oxygen affinity, and a dimeric TrHb2 from the thermophilic aerobic spore forming bacterium Geobacillus stearothermophilus(Gs-trHb)
YERIGGEETLSRLVEAFYPRVAAHPLLAPIFPDDLTETARKQKQFLTQFFGGPPLYTDEYGHPMLRARHL
PFPITPTRAEAWLACMAEALDEIGLEEPIREELYARLTYTAHHMVN
>gnl|CDD|381282 cd14773, TrHb2_PhHbO-like_O, Truncated hemoglobins, group 2 (O); Pseudoalteromonas haloplanktis PhHbO like. The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). TrHb2's belonging to this group include Pseudoalteromonas haloplanktis PhHbO (encoded by the PSHAa0030 gene) which appears to be involved in oxidative and nitrosative stress resistance
YERIGGEEGVRALVDRFYDLMDTLPEAAELRAMHPDDLTPSREKLFEFLSGWLGGPRLYSEKYGHPRLRS
RHAPFPIGPAERDQWLLCMRKALDEVVLDPDLREYLLAAFARLADHMRN
>gnl|CDD|381283 cd14774, TrHb2_HGbIV-like_O, hell's gate globin IV and similar truncated hemoglobins, group 2 (O). The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P)
VRPPVTKPNPKILQEVGEEGLRKLVSDHYDLLKKSSIKHLFPQDEEELEKAKQKSADFFIQICGGPPYYS
QNRGHPRMRARHFPFSIDEKARDIWLACYKKVLKDLKFPEELKESFWNYIEIFSIWMVNTR
>gnl|CDD|381284 cd14775, TrHb2_O-like, Truncated hemoglobins, group 2 (O); uncharacterized subgroup. The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P)
YEWAGGEEALRRLTEAFYARVLADPLLAPVFAHMSPDHVEHVAAFLAEVFGGPARYTDELGGHEHMLRHH
AGLGITEEQRRRWVELMLEAADEAGLPDDPEFRSAFVGYLEWGSRIAVI
>gnl|CDD|271309 cd14776, HmpEc-globin-like, Globin domain of Escherichia coli flavohemoglobin (Hmp) and related proteins. Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. This subfamily includes Vibrio fischeri Hmp and E.coli Hmp. NO scavenging by flavoHb affects the swarming behavior of Escherichia coli, and protects against NO during initiation of the squid-Vibrio symbiosis. E.coli Hmp can catalyze the reduction of several alkylhydroperoxide substrates into their corresponding alcohols using NADH as an electron donor, and it has been suggested that it participates in the repair of the lipid membrane oxidative damage generated during oxidative/nitrosative stress
LSAETIRIVKATIPLLAAAGPALTQHFYQRMLTHNPELKNIFNLAHQRTGRQPKALFDAVAAYAQNIRNL
QALLPAVERIAQKHTSFNIQPEQYQIVGEHLLATIEELAPPDKDVLAAWAKAYQFLADIFIDREGEIY
>gnl|CDD|381285 cd14777, Yhb1-globin-like, Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains. FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. S. cerevisiae Yhb1p has been shown to protect against nitrosative stress and to control ferric reductase activity; it may participate in regulating the activity of plasma membrane ferric reductase(s). Also included in this subfamily is Dictyostelium discoideum FlavoHb, the expression of which affects D. discoideum development
LSEKTIQIVKSTVPVLKEKGTEITKRFYKRMFEEHPELLNIFNQTNQKKGLQQTALANTVYAAAKHIDNL
EVILPVVKQIAHKHRALGVKPEHYPIVGENLLAAIKEVLGDAATDEILEAWEKAYGVIADVFIEVEKEMY
>gnl|CDD|381286 cd14778, VtHb-like_SDgb, Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins. VtHb is homodimeric, and may both transport oxygen to terminal respiratory oxidases, and provide resistance to nitrosative stress. It has medium oxygen affinity and displays cooperative ligand-binding properties. VHb has biotechnological application, its expression in heterologous hosts (bacteria and plants) has improved growth and productivity under microaerobic conditions. Another member of this subfamily Campylobacter jejuni hemoglobin (Cgb) is monomeric, and plays a role in detoxifying NO. Along with a truncated globin Ctb, it is up-regulated by the transcription factor NssR in response to nitrosative stress
LDQQTIEIIKSTVPVLKEHGVEITTEFYKNMFTEYPEVRPMFDMEKQKSGEQPKALAMTVLAAAQNIENL
EKIRPAVEKIGKTHVNLNVKPEHYPIVGACLLGAIKEVLGDTATDEILEAWEKAYGEIAKIFIDVEKKLY
>gnl|CDD|381287 cd14779, FHP_Ae-globin-like, Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins. Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb maintains Medicago truncatula-Sinorhizobium meliloti symbiosis. Alcaligenes eutrophus FHP contains a phospholipid-binding site
LTEQQKDLVKATVPVLKEHGVALTKHFYQRMFEHNPELKNVFNMGHQESGKQQQALAMAVLAYAENIDDP
EVLLPVLKLIAHKHVSLGIRAEQYPIVGEHLLASIKEVLGDAATDELISAWAAAYGQLADILIGMESKLY
>gnl|CDD|381288 cd14780, HmpPa-globin-like, Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins. Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. The physiological role of HmpPa is thought to be detoxification of NO under aerobic conditions
LSPHQIAIIKATVPALEAHGEAITTHFYPLMFEEYPEVRALFNQAHQASGAQPRALANAVLAYARHIDRL
EVLGGAVSLIVNKHVSLNILPEHYPIVGTCLLRAIREVLGDAATDEVIEAWGAAYQQLADLLIAAEEAVY
>gnl|CDD|381289 cd14781, FHb-globin_1, Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup. FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. This subfamily may contain some single-domain goblins (SDgbs)
LSPHTIAIVKATVPALEEHGVAITAAMYKRLFEDPEIKALFNQAAQKSGEQPRALAGAILAYAKNIDNLG
ALGSAVERIAQKHVGLHIKPEHYPHVATALLGAIKDVLGDAATDEVLEAWGEAYWFLADILINREKQLY
>gnl|CDD|381290 cd14782, FHb-globin_2, Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup. FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways
LSAESAEVIRATLPVVGEHIEEITPLFYRRMFGEHPELLRNLFNRGNQASGEQQKALAASVAAFATHLVD
PDAPPPDSVLSRIAHKHASLGITPEQYTIVHRHLFAAIAEVLGAAVTPEVAAAWDEVYWLMADQLIATEA
RLY
>gnl|CDD|271316 cd14783, FHb-globin_3, Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup. FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways
LSQKTIDIVKSTAPILEENGETLTRHFYKRMFEHNPEVKPFFNPAHQHSGSQQRALAAAICAYAANIDNL
EVLGNAVELIAQKHASLGIKPEHYPIVGSNLLASIREVLGDAATDDIIEAWSEAYGFLADILIGREKQIY
>gnl|CDD|381291 cd14784, class1_nsHb-like, Class 1 nonsymbiotic hemoglobins and related proteins. Class1 nsHbs include the dimeric hexacoordinate Trema tomentosa nsHb and the dimeric hexacoordinate nsHb from monocot barley. This subfamily also includes ParaHb, a dimeric pentacoordinate Hb from the root nodules of Parasponia andersonii, a non-legume capable of symbiotic nitrogen fixation. ParaHb is unusual in that it has different heme redox potentials for each subunit
FSEEQEALVKKSWAVMKKDAAELGLKFFLKIFEIAPSAKQLFSFLRDSTVPLEKNPKLKPHAMSVFVMTC
EAAVQLRKAGKVTVRESKLKRLGATHVKYGVVDEHFEVVKFALLETIKEAVPDMWSPEMKSAWGEAYDQL
VAAIKAEMK
>gnl|CDD|270211 cd14785, V-ATPase_C, Subunit C of vacuolar H+-ATPase (V-ATPase). This family contains subunit C of vacuolar H+-ATPase (V-ATPase), a protein that plays a crucial role in the vacuolar system of eukaryotic cells. The main function of V-ATPase is to generate a proton-motive force at the expense of ATP and to cause limited acidification in the internal space (lumen) of several organelles of the vacuolar system. V-ATPases are multi-subunit protein complexes made up of two distinct structures: a peripheral catalytic sector (V1) and a hydrophobic membrane sector (V0) responsible for driving protons; subunit C is one of five polypeptides composing V1. The key function of the C subunit is intimately involved in the reversible dissociation of the V1 and V0 structures. It has also been identified as a mediator of the acidic microenvironment of tumors which it controls by proton extrusion to the extracellular medium. The acidic environment causes tissue damage, activates destructive enzymes in the extracellular matrix, and acquires metastatic cell phenotypes
YWLVSLPLDKTKEQTLEELRQALGKSNLDVSKFDIPEFKVGTLDSLIALSDDLGKLDAQVESVLRKIARQ
LRDLLEDDSDKLQENLLVNGVSLEEYLTRFQWDEAKYPTKRSLRELVEIISKEVSKIDEDLKTKSAAYNE
AKGNLQALERKQTGSLSTRSLADVVKEEDFVLDSEYLTTLLVVVPKNSEKEWLNSYETLTDMVVPRSSKK
IAEDEEYALYSVTLFKKVVDEFKNAAREKKFIVRDFKYDEEAYEEEKEELEKLEAEEKEQETELLRWCRT
NFSELFSAWIHLKALRLFVESVLRYGLPPNFQAFLLKPKKKKEKKLRKILNKLYGHLGSAGGNATSEDIP
GLLEEGDQEYYPYVSFEI
>gnl|CDD|341075 cd14786, STAT_CCD, Coiled-coil domain of Signal Transducer and Activator of Transcription (STAT), also called alpha domain. This family consists of the coiled-coil (alpha) domain of the STAT proteins (Signal Transducer and Activator of Transcription, or Signal Transduction And Transcription), which are latent cytoplasmic transcriptional factors that play an important role in cytokine and growth factor signaling. STAT proteins regulate several aspects of growth, survival and differentiation in cells. The transcription factors of this family are activated by JAK (Janus kinase) and dysregulation of this pathway is frequently observed in primary tumors and leads to immunosuppression, increased angiogenesis and enhanced survival of tumors. There are seven mammalian STAT family members that have been identified: STAT1, STAT2, STAT3, STAT4, STAT5A, STAT5B and STAT6. STAT proteins consist of six structural regions: N-domain (ND)/protein interaction domain, coiled-coil domain (CCD)/STAT all alpha domain, DNA-binding domain (DBD), linker domain (LK), a Src homology 2 (SH2) domain, and C-terminal transcriptional activation domain (TA) that includes two conserved phosphorylation sites (tyrosine and serine residues). The coiled-coil or alpha domain is an interacting region with other proteins, including IRF-9/p48 for STAT1, c-Jun, StIP1, and GRIM-19 for STAT3, and SMRT with STAT5A and STAT5B. A functional STAT1 mutant (phenylalanine to serine) in this domain region shows significantly decreased protein expression caused by translational/post-translational mechanisms independent of proteasome machinery. The phenylalanine is not conserved in STAT4 and STAT6 that have tight specificity, suggesting a novel potential mechanism of specific activation of STAT proteins. Specifically, STAT3, STAT5, and STAT6, which are continually imported to the nucleus independent of tyrosine phosphorylation, require the conformational structure of their coiled-coil domains
YELEQQILQLRNEFQILWEELKSLQQKRKEVLVKLLRRLLMAEEIQQELIIEELKNWKRRQQLAGNGAPR
EQSLDELQNWFESLAEFLWQLRQQVKKLLELFGDPIDPQLNDLLERVQELQKNLV
>gnl|CDD|350612 cd14787, Tiki_TraB-like, diverse proteins related to the Tiki and TraB protease domains. The extracellular domain of Tiki family proteins shares homology with bacterial TraB/PrgY proteins which are known for their roles in the inhibition of mating pheromones. Tiki and TraB/PrgY proteins share limited sequence identity, but their predicted secondary structures reveal that several catalytic residues are anchored in a similar manner, consistent with a common evolutionary origin. Tiki domains are related to the erythromycin esterase, gumN plant pathogens, RtxA toxins, and Campylobacter Jejuni heme-binding, ChaN-like proteins. Tiki is a membrane-associated metalloprotease (MEROPS family M96) that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. Wnt is essential in animal development and homeostasis. In Xenopus, Tiki is critical in head development. In human cells, Tiki inhibits Wnt-signaling, which is important in embryogenesis, homeostasis, and regeneration. Deregulation of Wnt contributes to birth defects, cancer and various diseases. TraB/PrgY protein has been identified in gut bacterium Enterococcus faecalis, but its function has not been well characterized. Plasmid-borne TraB has been implicated in the regulation of pheromone sensitivity and specificity. Based on homology to Tiki activity, it has been proposed that TraB acts as a metalloprotease in the inactivation of mating pheromone. Pasteurella multicida toxin has structural and sequence similarity to the Tiki/TraB family of proteases. However, unlike related multidomain toxins in this family, they do not exhibit conservation of the typical active site residues
GVLLGTSHKSPKVKDFQADNVKELIGQGSTIVALEDLLTVQAELSQFLKGSKMPKALEAMLFNLTKVDYD
VLFRDLLKSAKDNKARYNIRDRGIDHSFSLKKDGRIADEAKEKEGEKFIVLAGSSHL
>gnl|CDD|350613 cd14788, GumN, poorly characterized family of proteins related to gumN pathogenicity factor of Xanthomonas. GumN, a poorly characterized protein, is part of the large gum cluster of pathogenicity factors of the plant pathogen Xanthomonas. Except for GumN, the gum cluster is conserved, and proteins of this operon are involved in the production of xanthan, an extracellular polysaccharide that promotes plant disease. Xanthomonas campestri is responsible for 'black rot' disease in certain crop plants. GumN has sequence similarity to the Tiki/TraB protease family, but lacks the typical conserved residues of the active site
LWKVSKGDHVLWVLGTLSPLPKKMEWRSDEVERALAGSQEVLLPPGVSVKAGVGFFGRLLLLPSLLGARK
NPDGATLADVLPPDLYARWEALKARYIGRDDGVERWRPIFAALELYSAALKKAGLTSGGGVTPVVEKLAK
KHGVKVTPVGVELRIDDPRAALKEFKKSPLDDLACLAATLDRLEADLDAMRARANAWAVGDVAALRALPR
ADQRCACLDALTNAGLARKPGLADLPERVRAAWLAAAEAALATNGVTFAVLPLRDLLAPDGVLARLRARG
YTVEAP
>gnl|CDD|350614 cd14789, Tiki, Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues. Tiki is a membrane-associated metalloprotease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. Wnt is essential in animal development and homeostasis. In xenopus, tiki is critical in head development. In human cells, TIKI inhibits Wnt-signaling, which is important in embryogenesis, homeostasis, and regeneration. Deregulation of WNT contributes to birth defects, cancer and various diseases. TIKI homology domains are part of the TraB family and are related to the Erythromycin esterase, GumN plant pathogens, RtxA toxins, and Campylobacter Jejuni heme-binding, Chan-like proteins. TraB/PrgY are identified in gut bacterium Enterococcus faecalis, but its function has not been well characterized. Plasmid-borne, TraB has been implicated in the regulation of pheromone sensitivity and specificity. Based on homology to TIKI activity, it has been proposed that TraB acts as a metalloprotease in the inactivation of mating pheromone. The TIKI/TraB family has 2 conserved GxxH motifs and conserved glutamate and arginine residues that may be catalytic
LWKISKGGLTSYLFGTIHVGDPDVYPLPPAVEQALAASDALVLELDLTDPAALAALQAAMALPPDGKTLK
DLLSPEDYARLKAALAELGLPLAALDKLKPWLLALTLSQLQLQKLGYDPEYGVDLYLAQRAKAAGKPVLG
LETVEEQLDLLDSLPEEEQLALLRSTLDELEEAEAELETLIEAWKAGDLDALEELLDESMKEDDPELYER
LLVDRNRNWAPKIEALLKKGGTVFVAVGAGHLVGEDGLLALLRKKGYTV
>gnl|CDD|269891 cd14790, GH_D, Glycoside hydrolases, clan D. This group of glycosyl hydrolase families is comprised of glycosyl hydrolase family 31 (GH31), family 36 (GH36), and family 27 (GH27). These structurally and mechanistically related protein families are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively. They have a wide range of functions including alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase, alpha-N-acetylgalactosaminidase, stachyose synthase, raffinose synthase, and alpha-1,4-glucan lyase
PPMGWLTWERYRQDIDEMLFMEMADRIAEDELPYKVFNIDDCWAKKDAEGDFVPDPERFPRGEAMARRLH
ARGLKLGIWGDPFRLDWVEDDLQTLAEWGVDMFKLDFGESSGTPVQWFPQKMPNKEQAQGYEQMARALNA
TGEPIVYSGSWSAYQGGGEICNLWRNYDDIQDSWDAVLSIVDWFFTNQDVLQAGGFHFNDPDMLIIGNFG
LSAEQSRSQMALWTIMDAPLLMSTDLSTISPSDKKILVNRLMI
>gnl|CDD|269892 cd14791, GH36, glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively
ARPVGWNSWYAYYFDITEEKLLELADAAAELGVELFVIDDGWFGARNDDYAGLGDWLVDPEKFPDGLKAL
ADRIHALGMKFGLWLEPEMVGPDSELYREHPDWLLKDPGGPPVTGRNQYVLDLSNPEVRDYLREVIDRLL
REWGIDYLKWDFNRAGAEGGSRALDSQGEGLHRYVEALYRLLDRLREAFPDVLIEGCSSGGGRPDLGMLG
YVDQFRISDNTDALERLRIQAGRSLLYPPEAMDPDVVLLPNHQTGRLEPLETRAAVAMLGGRLGLSDDLT
KLSEEELELLKEAIALYKK
>gnl|CDD|269893 cd14792, GH27, glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively
PPMGWNSWNAFGCNINEKLIKATADAMVSSGLRDAGYEYVNIDDGWQAKRRDADGRLVPDPTRFPSGMKA
LADYVHSKGLKFGIYSDAGTPTCADGGYPGSLGHEDSDAATFASWGVDYLKYDGCGAPSGRLDAQERYTA
MSDALNATGRPIVLSLSWWGYPDPWGWAAEIANSWRTTGDIWDSWTSVLSIIDQFADLAEYAAPAGPGHW
NDPDMLEVGNGGLGTDDEQRTHFSLWAIMASPLILGNDLRNLDDETLALLTNPEVIAVNQD
>gnl|CDD|269816 cd14793, DUF302_like, Domains similar to DUF302 and the N-terminal domains found in some bacterial RNAses. DUF302 is an uncharacterized domain with widespread phylogenetic distribution. It appears homologous to the N-terminal domains of RNAse H3 and the Escherichia coli toxin RnlA
VDLSPVAEKIQFVLENSIKMESGFTFGAHPGNVSTPLWALESTRPGFMPKKVTVFKTDGKTQIQYLGYAN
RKLSEKVLDIV
>gnl|CDD|269817 cd14794, RNLA_N_1, N-terminal repeat domain of toxin RnlA; first out of two repeats. The Escherichia coli toxin RnlA functions as an mRNA endoribonuclease and is part of a two-component toxin-antitoxin system that promotes resistance to phage infections, together with the antitoxin RnlB. RNAse activity is located in the C-terminal domain. This N-terminal domain appears to participate in homodimerization and is the first out of two repeats
KNLNLNREKIEQHIDKFLEVSNLLSKDGDTPGFQNGKRVVFGSTGSDFATVDIYFNQDGTTTIQYKTGKN
QELGEELADFLYETINPAEF
>gnl|CDD|269818 cd14795, RNLA_N_2, N-terminal repeat domain of toxin RnlA; second out of two repeats. The Escherichia coli toxin RnlA functions as an mRNA endoribonuclease and is part of a two-component toxin-antitoxin system that promotes resistance to phage infections, together with the antitoxin RnlB. RNAse activity is located in the C-terminal domain. This N-terminal domain appears to participate in homodimerization and is the second out of two repeats
SVNLVLKGILEEEFDPVLELTNEELADIEIKIHTDEPRKKVWKLKSKKYQDELTVTFHKTTRKLQIQGRP
LSCYRQLIFLLTELLDL
>gnl|CDD|269819 cd14796, RNAse_HIII_N, N-terminal domain of ribonuclease H3. RNAse H3 (HIII) is a bacterial type 2 ribonuclease, which endonucleolytically hydrolyzes an RNA strand when it is annealed to a complementary DNA strand in the presence of divalent cations, and plays a role in DNA replication and repair. The N-terminal domain characterized by this model has been shown to be important in substrate binding; it might form initial contacts with the substrate and not be part of the active complex that involves the C-terminal ribonuclease domain. This domain has also been characterized as DUF3378
IVLKLTTSQIEKLKTYLQTYLTPKPPYALFAAKKPGVTVTAYKSGKVLFQGKGAEAEAAFWLEPEI
>gnl|CDD|269820 cd14797, DUF302, Uncharacterized domain family DUF302. These domains are mostly found in bacterial single-domain proteins and have been shown to form homodimers; they may also bind zinc. Also characterized as COG3439
LITVTSPYSFDETVERLKEALKEEGFGVLAEIDHQATLKELGLDLPPYTILGFCNPKLATPLLQADPRIG
LLLPCRVLVYEDDDGKVWVSYMDPSALAALFGNPELKEVAKEVEEKLEKIIDAA
>gnl|CDD|271353 cd14798, RX-CC_like, Coiled-coil domain of the potato virux X resistance protein and similar proteins. The potato virus X resistance protein (RX) confers resistance against potato virus X. It is a member of a family of resistance proteins with a domain architecture that includes an N-terminal coiled-coil domain (modeled here), a nucleotide-binding domain, and leucine-rich repeats (CC-NB-LRR). These intracellular resistance proteins recognize pathogen effector proteins and will subsequently trigger a response that may be as severe as localized cell death. The N-terminal coiled-coil domain of RX has been shown to interact with RanGAP2, which is a necessary co-factor in the resistance response
AEAAVSFLLEKLGELLEQEADLLSGVKEEIESLKDELESMQAFLKDADAKQDEDEELKDWVKQVRDVAYD
AEDIIDSFLLKLVPDKRRGGFLKRLFSLLKELKELHQVAKEIQSIKSRIKDISS
>gnl|CDD|438995 cd14799, BRcat_Rcat_RBR, BRcat (benign-catalytic) and Rcat (required-for-catalysis) domains, part of the RBR (RING1-BRcat-Rcat) domain. The RBR family of RING-type E3 ligases are characterized by containing an RBR (RING1-BRcat-Rcat) domain, which was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. It is composed of an extended RING domain (RING1) followed by an in-between RING (IBR) domain and the catalytic domain, which is structurally an IBR domain but is commonly designated as RING2. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBRs has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis), where the IBR and RING2 domains have been renamed as BRcat and Rcat domains, respectively. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. The BRcat domain adopts the same fold as the Rcat domain while lacking the catalytic cysteine residue and ubiquitination activity. RBR family members play roles in protein quality control and can indirectly regulate transcription. Evidence suggests that RBR proteins are often parts of cullin-containing ubiquitin ligase complexes
NTKWCPKCHFGFEKERGCMHATCPQCRQEFCWRCKRQ
>gnl|CDD|341082 cd14801, STAT_DBD, DNA-binding domain of Signal Transducer and Activator of Transcription (STAT). This family consists of the DNA binding domain (DBD) of the STAT proteins (Signal Transducer and Activator of Transcription, or Signal Transduction And Transcription), which are latent cytoplasmic transcriptional factors that play an important role in cytokine and growth factor signaling. STAT proteins regulate several aspects of growth, survival and differentiation in cells. The transcription factors of this family are activated by JAK (Janus kinase) and dysregulation of this pathway is frequently observed in primary tumors and leads to immunosuppression, increased angiogenesis and enhanced survival of tumors. There are seven mammalian STAT family members that have been identified: STAT1, STAT2, STAT3, STAT4, STAT5A, STAT5B and STAT6. STAT proteins consist of six structural regions: N-terminal domain (ND)/protein interaction domain, coiled-coil domain (CCD)/STAT all alpha domain, DNA-binding domain (DBD), linker domain (LK), a Src homology 2 (SH2) domain, and C-terminal transcriptional activation domain (TA) that includes two conserved phosphorylation sites (tyrosine and serine residues). STAT1 and STAT3 have the greatest diversity of biological functions among the 7 known members of the STAT family. The DNA binding domain of STAT has an Ig-like fold. DNA binding specificity experiments of different STAT proteins show that STAT5A specificity is more similar to that of STAT6 than that of STAT1, as also seen from the evolutionary relationships
FVVEKQPPQVLKTGTKFTATVRLLVGDKLGIHLNLPKVKASIISEEQAKSLVENKTLGGFRSGEILGNNT
KVMEYEESTGGLSAEFKNLSLKKIKRGDRKSGDESVTEEKFALLFTTQFTIGGLTIDLWTLSLPVVVIVH
GNQEPSAWATILWDNAF
>gnl|CDD|269812 cd14803, RAP, Receptor-associated protein (RAP). Receptor-associated protein, RAP, is an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. RAP associates with (LDL) receptor-related protein (LRP) early in the secretory pathway, reducing its ligand binding capacity, and then dissociates from LRP in the low-pH environment of the Golgi; studies have shown that histidine residues in RAP D3 serve as a switch that facilitates its uncoupling from the receptor. RAP is a modular protein identified as having an internal triplication, with domains, D1, D2, and D3, each thought to have distinct functions; these domains are independent and do not interact. The carboxyl-terminal domain (D3) of RAP is required for folding and trafficking of LRP, while the amino-terminal tandem D1D2 domains of RAP are essential for blocking LRP from binding of certain ligands, such as activated forms of alpha2-macroglobulin
FRMPRLNQLWEKAQRLHLPPVELAELHAELKHQERKELAWNKLKLDLEIAEEIHEHAESPGDLSDIKGEK
HALGLDEDKEKEARLIRNLNVLLAKYG
>gnl|CDD|271351 cd14804, Tra_M, TraM mediates signalling between transferosome and relaxosome. TraM is a plasmid encoded DNA-binding protein that is essential for conjugative transfer of F-like plasmids (e.g. F, R1, R100 and pED208) between bacterial cells. Bacterial conjugation, a form of horizontal gene transfer between cells, is an important contributor to bacterial genetic diversity, enabling virulence and antibiotics resistance factors to rapidly spread in medically important human pathogens. Mutation studies have shown that TraM is required for normal levels of transfer gene expression as well as for efficient site-specific single-stranded DNA cleavage at the origin of transfer (oriT). TraM tetramers bridge oriT to a key component of the conjugative pore, the coupling protein TraD. The N-terminal ribbon-helix-helix (RHH) domain of TraM is able to cooperatively bind DNA in a staggered arrangement without interaction between tetramers. This allows the C-terminal TraM tetramerization domains to be free to make multiple interactions with TraD, thus driving plasmid recruitment to the conjugative pore
MPRVQIYVKQKVLEEIRDIVDERIQEGATPAEANISSVCSELLELGLRVYEAQQEKKESGFNQMEFNKLL
LENVLKTRFLVQKILAMMSELQEIKEDSRFNYEEIKEAIKELIQEKLSAFFP
>gnl|CDD|271348 cd14805, Translin-like, Translin and translin-associated factor-X (TRAX). Translin (also known as TB-RBP), and its binding partner protein TRAX (translin-associated factor-X) are a paralogous pair of conserved proteins, and oligomeric complexes of TRAX and translin are known as C3PO proteins (for component 3 promoter of RNA-induced silencing complex or RISC). The Translin-Trax complex enhances the removal of the passenger strand in RNAi and the formation of active RISC. Translin and Trax participate in a variety of nucleic acid metabolism pathways in addition to RNAi and have been implicated in a wide range of biological activities, including mRNA processing, cell growth regulation, spermatogenesis, neuronal development/function, genome stability regulation and carcinogenesis; however, their precise role in some of the processes remains unclear. It has been shown that Trax subunit, but not Translin, possesses a Glu-Glu-Asp catalytic center with the capacity to digest RNA as well as DNA; this catalytic activity is required for passenger-strand removal and RISC activation in RNAi. In Archaeoglobus fulgidus, Trax-like-subunits assemble into an octameric structure, highly similar to human C3PO; its complex with duplex RNA reveals that the octamer entirely encapsulates a single 13-base-pair RNA duplex inside a large inner cavity
YQGELDAEQDIRERIRKVVRDIEQESKEIIFLLQGIHSGKGDIEKRCLEAREHLNTVKQKLTSLATELPA
EQYYRFHEHWTFGLQRLVFAAAFVVYLETETLVTREEVTEILGIEPDREKGFHLDVEDYLLGVLDLASEL
SRLCINSVTAGDYDRPLHISTFINELYSGFRLLNLKNDELRKRYDTLKYDVKKVEEV
>gnl|CDD|269813 cd14806, RAP_D1, Receptor-associated protein (RAP), Domain 1. This subfamily is the N-terminal domain (D1) of receptor-associated protein, RAP, an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. D1 as well as domain 2 (D2) are essential for blocking low-density lipoprotein receptor-related protein (LRP) from binding of certain ligands, such as activated forms of alpha2-macroglobulin; D1 and D2 each bind LRP weakly but the tandem D1D2 binds much more tightly, suggesting the avidity effects arising from amino acid residues contributed from each domain. The double module of complement type repeats, CR56, of LRP binds many ligands including alpha2-macroglobulin, which promotes the catabolism of the Abeta-peptide implicated in Alzheimer's disease
FRMAKLNQLWEKAQRLLLSPVKLAELYADLKIQEKDELAWKKLKAEGLDEDGEKEAKLRRNLNVILAKYG
L
>gnl|CDD|269814 cd14807, RAP_D2, Domain 2 of receptor-associated protein (RAP). This subfamily is the N-terminal domain (D2) of receptor-associated protein, RAP, an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. D2, along with RAP domain 1 (D1), is essential for blocking low-density lipoprotein receptor-related protein (LRP) from binding of certain ligands, such as alpha2-macroglobulin; D1 and D2 each bind LRP weakly but the tandem D1D2 binds much more tightly to the second and the fourth ligand-binding clusters present on LRP, suggesting the avidity effects arising from amino acid residues contributed from each domain. Also, RAP has regions that interact weakly with heparin, one located in D2 and two located in D3. The double module of complement type repeats, CR56, of LRP binds many ligands including alpha2-macroglobulin, which promotes the catabolism of the Abeta-peptide implicated in Alzheimer's disease
FDDPRLEKLWNKAKTSGKFSDEELQKLHREFQHHKEKIHEYNILLETVSRTEEIHKNVISPSLEEDIKES
VLHNKHTDLKERLRSINQGFERLRKVSH
>gnl|CDD|269815 cd14808, RAP_D3, C-terminal receptor-associated protein (RAP), Domain 3. This subfamily is the C-terminal domain (D3) of receptor-associated protein, RAP, an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. D3 is required for folding and trafficking of low-density lipoprotein receptor-related protein (LRP). In the mildly acidic pH of the Golgi, unfolding of RAP-D3 helical bundle facilitates dissociation of RAP from the LDL receptor type A (LA) repeats of LDLR family proteins. Also, RAP has 3 regions that interact weakly with heparin, two regions located in D3 and one in RAP domain 2 (D2). The double module of complement type repeats, CR56, of LRP binds many ligands including alpha2-macroglobulin, which promotes the catabolism of the Abeta-peptide implicated in Alzheimer's disease
FEEPRVQDLWKLAQKANFTPEELESFKEELKHFEKRLEKHRHYQKELELSHEKLEHKEKVGRKPEKHAEL
EEKTKKLGRKVKKLHQDLESRISKARHTEL
>gnl|CDD|269871 cd14809, bZIP_AUREO-like, Basic leucine zipper (bZIP) domain of blue light (BL) receptor aureochrome (AUREO) and similar bZIP domains. AUREO is a BL-activated transcription factor specific to phototrophic stramenopiles. It has a bZIP and a BL-sensing light-oxygen voltage (LOV) domain. It has been shown to mediate BL-induced branching and regulate the development of the sex organ in Vaucheria frigida. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. This subgroup also includes the Epstein-Barr virus (EBV) immediate-early transcription factor ZEBRA (BZLF1, Zta, Z, EB1). ZEBRA exhibits a variant of the bZIP fold, it has a unique dimer interface and a substantial hydrophobic pocket; it has a C-terminal moiety which stabilizes the coiled coil involved in dimer formation. ZEBRA functions to trigger the switch of EBV's biphasic infection cycle from latent to lytic infection. It activates the promoters of EBV lytic genes by binding ZEBRA response elements (ZREs) and inducing a cascade of expression of over 50 viral genes. It also down regulates latency-associated promoters, is an essential replication factor, induces host cell cycle arrest, and alters cellular immune responses and transcription factor activity
AERRRERNREHARKTRLRKKAYLESLKEQVAALQAENQRLRQQIRQAAPASA
>gnl|CDD|269872 cd14810, bZIP_u1, Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily. Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KEKRQLRNKISARNFRARRKEYITQLEEQVADRDAEIEQLRAELRALRNENK
>gnl|CDD|269873 cd14811, bZIP_u2, Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily. Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
RQKKLARNRESARNSRKRKKIYLELLENKVKELQQELEKLKRLREGSASSIN
>gnl|CDD|269874 cd14812, bZIP_u3, Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily. Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
KEARLIRNRAAAQLSRQRKKEEVEELEARVKELEAENRRLRQLLAQPEAEAS
>gnl|CDD|269875 cd14813, bZIP_BmCbz-like, Basic leucine zipper (bZIP) domain of Bombyx mori chorion b-ZIP transcription factor and similar bZIP domains. Bombyx mori chorion b-ZIP transcription factor, is encoded by the Cbz gene. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription
YREKRDKNNEASRRSRLNRKQKEQEMQKEAEELERENEALKVKVEELEKELK
>gnl|CDD|350615 cd14814, Peptidase_M15, Metalloproteases including zinc D-Ala-D-Ala carboxypeptidase, L-Ala-D-Glu peptidase, L,D-carboxypeptidase, bacteriophage endolysins, and related proteins. This family summarizes zinc-binding metallopeptidases which are mostly carboxypeptidases and dipeptidases, and includes zinc-dependent D-Ala-D-Ala carboxypeptidases, VanX, L-Ala-D-Glu peptidase, L,D-carboxypeptidase and bacteriophage endolysins, amongst other family members. These peptidases belong to MEROPS family M15 which are involved in bacterial cell wall biosynthesis and metabolism
PDAAEALARMIAAAGAEGRTLTINSGYRTYAQQLRLFAAKGKGSGGRRWAAPPGTSNHQWGLAIDLGDGG
GWRETQGYRWLKANAPRYGFDNPGGARRGGAFQEPWHWEYV
>gnl|CDD|271352 cd14815, BA_2398_like, Putative Bacillus anthracis lipoprotein and related proteins. Uncharacterized protein family found in Bacilli and Gammaproteobacteria
KSRTPEIYLIPEGYEGKLYIVFNVPGGKPLKKEDGFRVYEIPPSGVLVTQTKDNEGWYGTVNVQYYYVDD
NGKRTKIINSCETFPSTGVESRIGNQHGVISFPFIGCEVTSQLFFVGTNADGREVDYQNHTGLEALRDLN
PDKYP
>gnl|CDD|350616 cd14817, D-Ala-D-Ala_dipeptidase_VanX, D-Ala-D-Ala dipeptidase VanX. D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine dipeptidase vanX; VanX; EC 3.4.13.22) is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. It belongs in the MEROPS peptidase family M15, subfamily D
AGFVYLADVIPDIVQDIRYAGSDNFVGRPIDGYEAPRCILTREAAEALAKVQAELAKQGLGLKVYDCYRP
QRAVDHFVRWAKDPDDTRMKAEFYPDVDKKDLFELGYIAEKSGHSRGSTVDLTLVDLDTGEELDMGTPFD
FFDPLSHTDSPGITAQQRANRLLLRSLMEKHGFKPYPKEWWHFTLKDEPYPDTYFDFPV
>gnl|CDD|341426 cd14818, longin-like, Longin-like domains. Longin-like domains are small protein domains present in a variety of proteins and members of protein complexes involved in or required for different steps during the transport of proteins from the ribosome to the ER to the plasma membrane, via the Golgi apparatus. Examples are mu and sigma subunits of the heterotetrameric adaptor protein (AP) complex, zeta and delta subunits of the heterotetrameric F-COPI complex, a subgroup of R-SNARE proteins, a subfamily of the transport protein particle (TRAPP), and the signal recognition particle receptor subunit alpha (SR-alpha)
LQLAVFDPQGQVLAASNWLGKKPSVKFSLIQIKSFFSKLITSGFDFLTLTIGSYTFHYYLNKGLYFVVIT
DEQELRQELFQTLNLLLKEFNSLHGSEVITKNIEDDLEEFESYLDIK
>gnl|CDD|271349 cd14819, Translin, Translin, also known as TB-RBP (testis brain RNA-binding protein). Translin (also known as TB-RBP for Testis Brain RNA-binding protein, a mouse ortholog), is a paralog of its binding partner protein TRAX (translin-associated factor-X) and together they form oligomeric complexes known as C3PO proteins (for component 3 promoter of RNA-induced silencing complex or RISC). DNA damage has been proposed to stimulate transport of Translin into nuclei. It binds to RNA and single-stranded DNA, and its selectivity is modulated by interactions with GTP and TRAX. Translin may also regulate dendritic trafficking of BDNF RNAs as well as function as a key activator of siRNA-mediated silencing in drosophila. Translin and Trax participate in a variety of nucleic acid metabolism pathways in addition to RNAi and have been implicated in a wide range of biological activities, including mRNA processing, cell growth regulation, spermatogenesis, neuronal development/function, genome stability regulation and carcinogenesis; however, their precise role in some of the processes remains unclear
LQEELEKEQELREEIREIVRELDQTLREIQAILQRIHSTPSSQVPELCESARELIEEVKETLAELAELIP
PHQYYKYNDLWRRILQRAVFLIALRHFLETGRLLTLEEVAEILGVPVNLKDGFHLDLEDYLHGLLSLVNE
LSRLAVNSVTLGDYERPLKISAFVKDLHAGFQLLNLKNDSLRKRFDGLKYDVKKVEEVVYDLSLRG
>gnl|CDD|271350 cd14820, TRAX, Translin-associated factor-X (TRAX). TRAX (translin-associated factor-X) is a paralog of its binding partner protein Translin and together they form oligomeric complexes known as C3PO proteins (for component 3 promoter of RNA-induced silencing complex or RISC). TRAX complexed with Translin is possibly involved in dendritic RNA processing and in DNA double-strand break repair as an interacting partner with C1D, an activator of the DNA-dependent protein kinase involved in the repair of DNA-double strand breaks. It has been shown that Trax subunit, but not Translin, possesses a Glu-Glu-Asp catalytic center with the capacity to digest RNA; this catalytic activity is required for passenger-strand removal and RISC activation in RNAi. In Archaeoglobus fulgidus, Trax-like-subunits assemble into an octameric structure, highly similar to human C3PO; its complex with duplex RNA reveals that the octamer entirely encapsulates a single 13-base-pair RNA duplex inside a large inner cavity. Translin and Trax participate in a variety of nucleic acid metabolism pathways in addition to RNAi and have been implicated in a wide range of biological activities, including mRNA processing, cell growth regulation, spermatogenesis, neuronal development/function, genome stability regulation and carcinogenesis; however, their precise role in some of the processes remains unclear
FESIRKELDEKDDKRERLIKLSRDITRLSKRAIFALHRGDLEEAEELLKEARELLEELRELLKEEPDLLY
SGAVSPALQEYVEALSFYHFLKEGRLPTPDEELGVTPEDYLLGLADLTGELMRYAIDSLRKGDLEEAEKY
LEFMEEIYEGLMSFDYPDALELRKKLDVDRQSLLKEETRCYE
>gnl|CDD|350517 cd14821, BACK_SPOP_like, BACK (BTB and C-terminal Kelch) domain found in speckle-type POZ protein (SPOP) and similar proteins. This family includes speckle-type POZ protein (SPOP), speckle-type POZ protein-like (SPOPL), TD and POZ domain-containing proteins (TDPOZ), Drosophila melanogaster protein roadkill, and similar proteins. Both SPOP and SPOPL serve as adaptors of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and proteasomal degradation of target proteins. TDPOZ is a family of bipartite animal and plant proteins that contain a tumor necrosis factor receptor-associated factor (TRAF) domain (TD) and a POZ/BTB domain. TDPOZ proteins may be nuclear scaffold proteins involved in transcription regulation in early development and other cellular processes. Drosophila melanogaster protein roadkill, also termed Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor
LSVENAAEVLVLADLHSAEQLKTHAIDFINSHATDVMETEGWKSMVRSHPHLVAEAFRA
>gnl|CDD|350518 cd14822, BACK_BTBD9, BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 9 (BTBD9). BTBD9 is a risk factor for Restless Legs Syndrome (RLS) encoding a Cullin-3 substrate adaptor. The BTBD9 gene may be associated with antipsychotic-induced RLS in schizophrenia. Mutations in BTBD9 lead to reduced dopamine, increased locomotion and sleep fragmentation
LNIRNVCLIYDVASLYSLDDLCQTCCQFMDRNAQEVLSSEGFLTLSKSALKELLSRDSFCAPEVDIFNAV
RRWCEHNPDSKEDAKEILEAVRLPLMSLTEL
>gnl|CDD|341427 cd14823, AP_longin-like, Longin-like domains of AP complex subunits. AP complex sigma subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals
KAILVLDNDGKRLFAKYYDDTYPSVKEQKAFEKNIFNKKHRTDSEIVLLEGLRVVYKSSIDLYFVVIGSK
NENELLLLEVLNCLVDVLSEYFRKVEERAILENFEGLYFALDEIVDGGYIQETDPKQVVHF
>gnl|CDD|341428 cd14824, Longin, longin domain. Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including VAMP7, Ykt6, and Sec22. Longin is one of the approximately 26 components required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus. It is necessary for the steps of the transfer from the ER to the Golgi complex. Longins are the only R-SNAREs that are common to all eukaryotes, and they are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain
LYALIARGSDGLILAEYTDLSSFSSVKENFKFVAKTILERTPPSGQRQSVEEGDYVFHYLVEDGLCYLCI
TDKEYPKRVAFAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKKY
>gnl|CDD|341429 cd14825, TRAPPC2_sedlin, Trafficking protein particle complex subunit 2. Trafficking protein particle complex subunit 2 (TRAPPC2), also known as Sedlin (SEDL) or TRS20, has been identified as a component of the transport protein particle (TRAPP), required for tethering endoplasmic reticulum (ER)-derived vesicles to Golgi membranes and for Golgi traffic. In humans, deletions or point mutations in the SEDL gene cause the genetic disease spondyloepiphyseal dysplasia tarda (SEDT), an X-linked skeletal disorder
SYYFVIVGPNDNPLYEAEFGSSKKSEFRDDHRHLNQFIAHAALDLVDELQWTTNNMYLKSVDRFNEWSVS
AFVTAGNIRFLLLHDNKNDDGIKNFFQEVYELYVKILMNPFYEPNTPIRSPAFDRRVRALAKKYL
>gnl|CDD|341430 cd14826, SR_alpha_SRX, SRX domain of signal recognition particle receptor subunit alpha. Signal recognition particle receptor subunit alpha (SR-alpha) is part of the membrane-associated heterodimeric receptor for the signal recognition particle (SRP). The signal recognition particle (SRP) pathway is highly conserved and plays an important role in the translocation of proteins across and insertion into membranes by targeting the translating ribosome to the endoplasmic reticulum. The N-terminal SRX domain of SR-alpha has a profilin-like fold and has been shown to be the interaction site with the second subunit, SR-beta
DQFSIFTKGGIVLWSFNFTGLFKGSPINALIKDVLLEERSGESSFTYDSYTLKWTLDNELGLVFVVVYQK
ILQLQYIDELLDLVKKLFVSLYKNELKNKNALGIDDDLFKFDEYFKQK
>gnl|CDD|341431 cd14827, AP_sigma, AP complex subunit sigma. AP complex sigma subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals
RFILLFNRQGKTRLAKWYMQFDDDERQKLIEEIVQVVLSRDAKHCNFVEFRNYKLIYRRYASLYFCICVD
SNDNELAILEAIHNFVETLDKYFENVCELDLIFNFEKVYFIVDEMVLGGEIRETSQTKILKQIEMLDK
>gnl|CDD|341432 cd14828, AP_Mu_N, AP complex subunit mu N-terminal domain. AP complex mu subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal
SCLYILDENLEPLISRNYRADINLQSVVQDFFKAYKKLNPEERPPIISSNGWNFIYIKRDDLYFVSVTQT
NVNLMSVLVFLDQFYDLLKDYFGVKKLDKNSIIDNFVLIYELIDESIDFGIIQLTDYNILKDYIKV
>gnl|CDD|341433 cd14829, Zeta-COP, zeta subunit of the F-COPI complex. Zeta subunit of the heterotetrameric F-COPI complex, which consists of one beta-, one gamma-, one delta-, and one zeta subunit, where beta- and gamma- subunits are related to the large adaptor protein (AP) complex subunits, and delta- and zeta- subunits are related to the medium and small AP subunits, respectively. F-COPI forms a coatomer together with the B-COPI subcomplex, which assembles with a small GTPase, ADP-ribosylation factor 1 (ARF1), playing an important role in the formation of COPI complex-coated vesicles. COPI complex-coated vesicles function in the early secretory pathway mediating the retrograde transport from the Golgi to the ER, and intra-Golgi transport
KAILILDNDGKRVLAKYYDDTFPTVKEQKAFEKKLFDKTHKANAEIILLDGLTVVYKSNIDLTFYVVGSS
DENELILASVLNCLYDALSLLLRKNVEKRALLENLDLVLLALDEIVDGGIILETDPTAIASR
>gnl|CDD|341434 cd14830, Delta_COP_N, delta subunit of the F-COPI complex, N-terminal domain. Delta subunit of the heterotetrameric F-COPI complex, which consists of one beta-, one gamma-, one delta-, and one zeta subunit, where beta- and gamma- subunits are related to the large adaptor protein (AP) complex subunits, and delta- and zeta- subunits are related to the medium and small AP subunits, respectively. F-COPI forms a coatomer together with the B-COPI subcomplex, which assembles with a small GTPase, ADP-ribosylation factor 1 (ARF1), playing an important role in the formation of COPI complex-coated vesicles. COPI complex-coated vesicles function in the early secretory pathway mediating the retrograde transport from the Golgi to the ER, and intra-Golgi transport
LSAAICTKGGKILVSRQFVEISRSRIEGLLAAFPKLVGSGSQHTYVETENVRYVYQPLEDLYLVLITTKN
SNILEDLETLRLLSRVVPEYCPSVDEEEILKNAFDLIFAFDEVISLGYRENVTLSQIKTF
>gnl|CDD|341435 cd14831, AP1_sigma, AP-1 complex subunit sigma. AP-1 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large gamma-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-1 the coat protein is clathrin. AP-1 binds the phospholipid PI(4)P which plays a role in its localisation to the trans-Golgi network (TGN)/endosome. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals
HFLLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEWRDLKIVYKRYASLYFVCCVD
KDDNELITLEIIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLGGELQETSKKNVLRAIEAQDLLQ
EEE
>gnl|CDD|341436 cd14832, AP4_sigma, AP-4 complex subunit sigma. AP-4 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large epsilon-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-4 does not bind the coat protein clathrin, it is associated with nonclathrin coats. Its phospholipid binding partner is unknown and it is localized in the trans-Golgi network (TGN). The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals
KFILMVNKQGQTRLAQYYEFLSIEERVALEGEIIRKCLSRSEKQCSFLEYRGYKLVYRRYASLYFIVGVD
EDENELAILEFIHNLVETLDKYFENVCELDIMFNLEKAHFILDEMVMNGCIVETNKSNILAPILLMDK
>gnl|CDD|341437 cd14833, AP2_sigma, AP-2 complex subunit sigma. AP-2 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-2 complex which consists of one large alpha-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-2 the coat protein is clathrin. AP-2 binds the phospholipid PI(4,5)P2 which is important for its localisation to the plasma membrane. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals
MIRFILIQNRQGKTRLAKWYVPYDDDEKQKLEEEVHRLVTSRDKKHTNFVEFRNYKLVYRRYAGLFFCIC
VDVNDNELAYLEAIHLFVEVLDEYFGNVCELDLVFNFYKVYAILDEMFLAGEIQETSKKVILERLKELDK
L
>gnl|CDD|341438 cd14834, AP3_sigma, AP-3 complex subunit sigma. AP-3 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large delta-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-3 binds the coat protein clathrin and the phospholipid PI(3)P and it is localized in the endosome. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals
MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEGGSLIGGSDTKLIYRHYAT
LYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILTA
IEEQNK
>gnl|CDD|341439 cd14835, AP1_Mu_N, AP-1 complex subunit mu N-terminal domain. AP-1 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large gamma-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-1 the coat protein is clathrin. AP-1 binds the phospholipid PI(4)P which plays a role in its localisation to the trans-Golgi network (TGN)/endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal
SAIFILDLKGKVLISRNYRGDVPMSVIEKFMPLLMEKEEEGNLTPILTDGGVTYIYIKHNNLYLLAVTKK
NANAAMVLSFLYKLVEVFKEYFKELEEESIRDNFVIIYELLDEMMDFGYPQTTESKILQEYITQESHKL
>gnl|CDD|341440 cd14836, AP2_Mu_N, AP-2 complex subunit mu N-terminal domain. AP-2 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-2 complex which consists of one large alpha-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-2 the coat protein is clathrin. AP-2 binds the phospholipid PI(4,5)P2 which is important for its localisation to the plasma membrane. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal
MISALFIYNLKGDVLISRTYRDDVKRSVADAFRVQVINAKEQVRSPVLTIGSTSFFHVRHGNLYLVAVTR
SNVNAAMVFEFLYKLVQLFKSYFGKFNEDSIKNNFVLIYELLDEILDFGYPQNTEPEALKTYITQEGVKS
>gnl|CDD|341441 cd14837, AP3_Mu_N, AP-3 complex subunit mu N-terminal domain. AP-3 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large delta-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-3 binds the coat protein clathrin and the phospholipid PI(3)P and it is localized in the endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal
DSLFILNKSGEVILEKHWRGRIPRSVLDPFNEALTKPSRPEDVPPVIYTPPYYLFHILRNNLYFLAVVTS
EVPPLLVIEFLHRIVDVLEDYFGSLSESTIKENFVVVYQLLEEMLDNGFPLTTEPNALKELVPPPSLLN
>gnl|CDD|341442 cd14838, AP4_Mu_N, AP-4 complex subunit mu N-terminal domain. AP-4 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large epsilon-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-4 does not bind the coat protein clathrin, it is associated with nonclathrin coats. Its phospholipid binding partner is unknown and it is localized in the trans-Golgi network (TGN). The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal
SQFFILSPRGDTIIFRDYRGDVPKGSPEIFYRKVKFWKGDAPPVFNVDGVNYLHVKRNGLYFVATTRFNV
SPSYVLELLNRIAKLIKDYCGVLNEESIRKNFVLIYELLDEILDFGYPQTTSTEQLKSFVYNEPIVV
>gnl|CDD|350617 cd14840, D-Ala-D-Ala_dipeptidase_Aad, D-Ala-D-Ala dipeptidase (includes Lactobacillus plantarum Aad peptidase). D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine dipeptidase vanX; VanX; EC 3.4.13.22) is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. This subfamily includes Lactobacillus Aad peptidase and belongs in the MEROPS peptidase family M15, subfamily D
DLRYATTDNFTGKKLYPSARAYLRKEAAEKLAKAQKELKKPGYRLKIFDAYRPLSVQKKLWEAVPDPRYV
ANPAKGSRHNRGAAVDLTLVDLKGGELDMGTGFDDFSERAHHDYEGLSEEALKNRLLLREVMEKAGFKPI
PTEWWHFDDPDWKKYPLL
>gnl|CDD|350618 cd14843, D-Ala-D-Ala_dipeptidase_like, D-Ala-D-Ala dipeptidase, includes uncharacterized enzymes. This subfamily of D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine dipeptidase vanX; VanX; EC 3.4.13.22) also includes several uncharacterized proteins. This is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. It belongs in the MEROPS peptidase family M15, subfamily D
LRESVAERLLQAQSLLPKGLRLLIFDGYRPLAVQKFLFERYYQKIRKRHPGRSPEELIEEVRKFVAPPSK
DPLTPPPHSTGGAVDLTLADEDGKELDMGGPIDDDTEASEAYEEALTDSTGISEEARNNRRLLYDAMESA
GFVNYPTEWWHFSYGDQLWA
>gnl|CDD|350619 cd14844, Zn-DD-carboxypeptidase_like, Proteins similar to the zinc-containing D-Ala-D-Ala dipeptidase. The zinc D-Ala-D-Ala carboxypeptidase (Streptomyces-type) (also known as D-alanyl-D-alanine hydrolase; D-alanyl-D-alanine-cleaving carboxypeptidase; DD-carboxypeptidase; DD-carboxypeptidase-transpeptidase; Zn2+ G peptidase; G enzyme; EC 3.4.17.14) is a zinc enzyme that belongs to the peptidase M15 subfamily A. The enzyme catalyzes carboxypeptidation but not transpeptidation reactions involved in bacterial cell wall metabolism. Its specificity with substrates of the type Xaa-Yaa-Zaa shows that the enzyme requires the substrate N-terminus to be blocked and C-terminus to be free, and Yaa and Zaa should be in the D-configuration. It is weakly inhibited by beta-lactams most likely caused by the enzyme active site geometry
DFRTAEARRIDPRLMDQLYALRHKLGSDKPIQIISGYRSPKTNAMLRKTSGGVAKKSLHMYGQAIDIRLP
GVSLAHLRKAAGFLEIGGVGYYPHSDFVHIDTGPVRFW
>gnl|CDD|350620 cd14845, L-Ala-D-Glu_peptidase_like, L-Ala-D-Glu peptidase, also known as L-alanyl-D-glutamate endopeptidase. This L-Ala-D-Glu peptidase family includes L-alanyl-D-glutamate peptidase (bacteriophage T5) (also known as L-alanoyl-D-glutamate endopeptidase), and Ply118 and Ply500 L-Ala-D-Glu peptidase. Bacteriophage endolysin degrades the peptidoglycan of the bacterial host from within, leading to cell lysis and release of progeny virions. The bacteriophage endolysin Ply118 cleaves between L-Ala and D-Glu residues of Listeria cell wall peptidoglycan. This family belongs to the MEROPS peptidase M15 subfamily C
SERRIAGLHPEVRAVVKELIELAEEEGIDFRITEGYRSPARQAALYAQGRTKPGLIVTNARGGQSYHNYG
LAVDIVPLVNGKLSTGGADPWVSKAYQKLGEIAKSLGLEWGGDWKSFKDYPHFQLR
>gnl|CDD|350621 cd14846, Peptidase_M15_like, Uncharacterized family of the peptidase family M15, subfamily B. This family of uncharacterized proteins, similar to endolysin lys (Clavibacter phage CMP1) and VanYn peptidase, are zinc-binding enzymes that belong to the peptidase M15 subfamily B, involved in bacterial cell wall metabolism
LDPALLAALTAAATAAAADGVTLRITSGWRSPAEQQRLLDDAVRTYGSEEEARRWVAPPEDSAHVTGEAV
DIGPADAAQWLERHGARYGLCRIYANEWWHFELR
>gnl|CDD|350622 cd14847, DD-carboxypeptidase_like, Uncharacterized proteins of the MEROPS peptidase family M15, subfamily B. This family of uncharacterized proteins similar to D-Ala-D-Ala carboxypeptidase pdcA (Myxococcus-type) are zinc-binding enzymes that belong to the peptidase M15 subfamily B. The enzyme D-Ala-D-Ala carbozypeptidase catalyzes carboxypeptidation reactions involved in bacterial cell wall metabolism
LHPDAAEAFLALQAAAAKDGFDLQIASSFRSFERQLAIWNRKWSGERPVLDDNGQPLDISSLSPEEKIHA
ILRWSALPGASRHHWGTDIDVYDANALPAGYQLQLTPSEYEEGGPFAKLYQWLDENAAKFGFFRPYTQDR
GGVAPEPWHLSYAPLAQKYLQA
>gnl|CDD|350623 cd14849, DD-dipeptidase_VanXYc, D-Ala-D-Ala dipeptidase/D-Ala-D-Ala carboxypeptidase (VanXYc) and related proteins. VanXYc peptidase (also known as vanXY(C) peptidase, D-alanyl-D-alanine carboxypeptidase D,D-dipeptidase/D,D-carboxypeptidase, vancomycin resistance D,D-dipeptidase) is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci. Some of the vancomycin resistance operons encode VanXY D,D-carboxypeptidase which hydrolyzes both, dipeptide (D-Ala-D-Ala) or pentapeptide (UDP-MurNac-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala). It is a bifunctional enzyme that catalyzes D,D-peptidase and D,D-carboxypeptidase activities. VanXY has higher sequence similarity to VanY than with VanX and hydrolyzes D,D-dipeptides such as D-Ala-D-Ala, whereas VanY is inactive against this substrate; thus having a less restrictive active site to accommodate larger substrates such as UDP-MurNAc-pentapeptide[Ala]. This family belongs to the MEROPS family M15, subfamily B, and includes the D,D-dipeptidases VanXYg and VanXYe
LEKEVARQLKKLLEAIGGEDEIVPVSGYRSKEEQTAIYDDSLNENGEEFTEKYVALPGHSEHQTGLAIDL
GLNKKDIDFICPSFPDSGICDLFREQAADYGFIERYPKDKEEITGISYEPWHFRYVG
>gnl|CDD|350624 cd14852, LD-carboxypeptidase, L,D-carboxypeptidase DacB and LdcB, and related proteins. This L,D-carboxypeptidase family includes LdcB LD-Carboxypeptidase from Streptococcus pneumoniae, Bacillus anthracis, and Bacillus subtilis, and L,D-carboxypeptidase DacB from Streptococcus pneumonia and Lactococcus lactis. These enzymes are active against cell-wall-derived tetrapeptides and synthetic tetrapeptides lacking the sugar moiety but are inactive against tetrapeptides terminating in L-alanine. L,D-carboxypeptidase DacB plays a key role in the remodeling of S. pneumoniae peptidoglycan during cell division. It adopts a zinc-dependent carboxypeptidase fold and acts as an L,D-carboxypeptidase towards the tetrapeptide L-Ala-D-iGln-L-Lys-D-Ala of the peptidoglycan stem. This family also includes vanY D-Ala-D-Ala carboxypeptidase which is vancomycin-inducible and penicillin-resistant. VanY hydrolyzes depsipeptide- and D-alanyl-D-alanine-containing peptidoglycan precursors; it is insensitive to beta-lactams. All these enzymes belong to the MEROPS family M15 subfamily B
VLVNKDHPLPEDYVPEDLVPYVLLDNGLYLRKEAAEALEEMFDAAKKDGIDLTIVSGYRSYEYQQELYNN
YVARYGKEEADRYSARPGYSEHQTGLAVDIGSTDGPCLEESFEDTPAGKWLAENAHKYGFILRYPKGKEN
ITGYSYEPWHFRYVGKEAAKKI
>gnl|CDD|341443 cd14853, TRAPPC_longin-like, Longin-like domains of Trafficking protein particle complex. Longin-like domains of a subfamily of core components of the trafficking protein particle complex (TRAPP), including TRAPPC2, TRAPPC4, TRAPPC1 and a TRAPPC2L, whose function is not known. TRAPP complexes are required for tethering endoplasmic reticulum (ER)-derived vesicles to Golgi membranes and for Golgi traffic
FYFVVVGHHGNPLYEREFTPPGQAEDDNEEEYKLLAGMLHSVRSINSKLSPNVEKYLKLSDKTNEYKVHA
YVTATGLKFVMLTDVLMDRIEDVLKNFFSDLYVLYVKKNPNPFYEPNSPIRSRLFDSKVQSL
>gnl|CDD|341444 cd14854, TRAPPC2L, Trafficking protein particle complex subunit 2-like. Trafficking protein particle complex subunit 2-like (TRAPPC2L) is related to TRAPPC2. Its function is not known, but there are indications that it is part of the TRAPP II complex, which is required for distinct tethering events at Golgi membranes. TRAPPC2 has been identified as a general component of transport protein particle (TRAPP), required for tethering endoplasmic reticulum (ER)-derived vesicles to Golgi membranes and for Golgi traffic
VCVAVIGKQNNPLYLRTFPSGEDNDLKLHYIAHSSLDVVEEKLSASKKGGDTSDMYLGLLYPTEDYKVYG
YVTNTKVKFILVLEDTNTPLRDNDVRTLFRRLHNAYVDAVSNPFYPPGTPITSKKFDRRVDSLVS
>gnl|CDD|341445 cd14855, TRAPPC1_MUM2, Trafficking protein particle complex subunit 1. Trafficking protein particle complex subunit 1 (TRAPPC1), also known as MUM2 and BET5, has been identified as a component of the transport protein particle (TRAPP), required for tethering endoplasmic reticulum (ER)-derived vesicles to Golgi membranes and for Golgi traffic
YSFYIFDRHGNCIYYREWNRPKQSSNGKSEEEEQKLMFGLLFSLKSFVRKISPTDDTCGFHSYTTNKYKL
HYYETPTGLKFVLLTDPNVGDLRDVLQQIYSNIYVEYVVKNPLYPPGEPITSELFRSKLDQY
>gnl|CDD|341446 cd14856, TRAPPC4_synbindin, Trafficking protein particle complex subunit 4. Trafficking protein particle complex subunit 4 (TRAPPC4), also known as synbindin or TRS23, has been identified as a component of the transport protein particle (TRAPP), required for tethering endoplasmic reticulum (ER)-derived vesicles to Golgi membranes and for Golgi traffic
YSLYIINKAGGLIYQKDFSDALAKLSSNDYLRLASTFHGLHAIAAQLSPVPGSSGIELLETDTFRLHCFQ
TLTGIKFVLVADPKQPGLDALLRRVYELYADYVLKNPFYELEMPIRCELFDENLQKL
>gnl|CDD|410986 cd14858, TrmE_N, N-terminal domain of TrmE, a tRNA modification GTPase. This family contains the N-terminal domain of TrmE (also known as MnmE, ThdF, MSS1), a guanine nucleotide-binding protein conserved in all three kingdoms of life. It is involved in the modification of uridine bases (U34) at the first anticodon (wobble) position of tRNAs decoding two-family box triplets. TrmE is a three-domain protein comprising an N-terminal alpha/beta domain, a helical domain, and the GTPase domain which is nested within the helical domain. The N-terminal domain induces dimerization for self-assembly and is topologically homologous to the tetrahydrofolate (THF)-binding domain of N,N-dimethylglycine oxidase (DMGO). However, the THF-binding site in DMGO is encoded on a single polypeptide, while homodimerization would be required to create a similar THF-binding site in TrmE. Dimerization also creates a second, symmetry-related THF-binding site. Biochemical and structural studies show that TrmE indeed binds formyl-THF. A cysteine residue, necessary for modification of U34, is located close to the C1-group donor 5-formyl-tetrahydrofolate, suggesting a direct role of TrmE in the modification analogous to DNA modification enzymes
DTIAALATPPGRGAIAVIRISGPDALEILKKLFGPKKSEPKPRTAYLGKIYDPDGELIDEVLVLYFPAPH
SFTGEDVVEIHCHGGPAVVRAILEALLKLGARLAEPGEFTRRAFLNG
>gnl|CDD|275438 cd14859, PMEI_like, pectin methylesterase inhibitor and related proteins. Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) catalyzes the demethylesterification of homogalacturonans in the cell wall. Its activity is regulated by the proteinaceous PME inhibitor (PMEI) which inhibits PME and invertase through formation of a non-covalent 1:1 complex. Depending on the mode of demethylesterification, PMEI activity results in either loosening or rigidification of the cell wall. PMEI has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. Thus, PMEI probably plays an important physiological role in PME regulation in plants, possessing several potential applications in a food-technological context. CIF (cell-wall inhibitor of beta-fructosidase from tobacco) is structurally similar to PMEI and these members are also included in this model. Comparison of the CIF/INV1 structure with the complex between PMEI/PME suggests a common targeting mechanism in PMEI and CIF. However, CIF and PMEI use distinct surface areas to selectively inhibit very different enzymatic scaffolds
CKKTSYYKLCVSSLSSDPRSSTADLKGLANIALDAALANASDTQAFIAKLLKSTKDPALKKALRDCADDY
DDAVDDLEDAINALLSGDYDDAKTHVSAALDDADTCEEAFKESSGLPSPLTTRNDDLKRLCSIALAIILL
>gnl|CDD|341482 cd14860, 4HBD_NAD, 4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway. 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source
MKEFRIKPEIYQFDTCKEFAEEFKLGKDDLVLTNEYIYEPYFEPLNLDCAVIFQEKYGTGEPSDEMVEAI
YKDIKKYGYKRVIAIGGGTVIDIAKLLALKGISPVLDLFDGKIPLIKEKELIIVPTTCGTGSEVTNISIV
ELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEM
ILEGYQEIAEKGEEARFPLLGDFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLK
NYQEKNPDGEIKKLNEFLAKILGCDEEDVYDELEELLNKILPKKPLHEYGMKEEEIDEFADSVMENQQRL
LANNYVPLDREDVAEIYKELY
>gnl|CDD|341483 cd14861, Fe-ADH-like, Iron-containing alcohol dehydrogenases-like. This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions
NYPTRIRFGAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEAD
VEAGVAAYREGGCDGIIALGGGSAIDAAKAIALMATHPGPLWDYEDGEGGPAAITPAVPPLIAIPTTAGT
GSEVGRAAVITDDDTGRKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMA
DGIALEGLRLISEWLPRAVADGSDLEARGEMMMAALMGAVAFQKGLGAVHALAHALGALYGLHHGLLNAI
LLPYVLRFNRPAVEDKLARLARALGLGLGGFDDFIAWVEDLNERLGLPATLSELGVTEDDLDELAELALA
DPCHATNPRPVTAEDYRALLREAL
>gnl|CDD|341484 cd14862, Fe-ADH-like, iron-containing alcohol dehydrogenases (Fe-ADH)-like. This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized
MWYFSSPKIVFGEDALSHLEQLSGKRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETV
LKGAEAMREFEPDLIIALGGGSVMDAAKAAWVLYERPDLDPEDISPLDLLGLRKKAKLIAIPTTSGTGSE
ATWAIVLTDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDAL
ALKAIELIFKYLPRAYKDGDDLEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFL
PYVIEFYAKVTDERYDLLKLLGIEARDEEEALKKLVEAIRELYKEVGQPLSIKDLGISEEEFEEKLDELV
EYAMEDSCTITSPRPPSEEDLKKLF
>gnl|CDD|341485 cd14863, Fe-ADH-like, iron-containing alcohol dehydrogenases (Fe-ADH)-like. This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized
TYSQLTPVIFGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPD
EIVDEAAEIAREEGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDYALAGPPVPKPGIPLIAIPTTAGTG
SEVTPIAVITDEENGVKKSLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTD
ALALQAIRLIVKNLPRAVKDGDNLEARENMLLASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACAL
ALPVVLEFNAEAYPEKVKKIAKALGVSFPGESDEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKI
AEAVLKDPFAMFNPRPITEEEVAEILEAIY
>gnl|CDD|341486 cd14864, Fe-ADH-like, iron-containing alcohol dehydrogenases (Fe-ADH)-like. This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized
FKIPPNIVFGADSLERIGEEVKEYGSRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDT
IDEAAELARKAGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEF
SDRFPVVDSRSREVKLLKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALA
LKAIELVSENLDGALADPKNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLP
HVIEYAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGVRRLIAQLNLPTRLKDLDLASSLEQLAAIA
EDAPKLNGLPRSMSSDDIFDILKAAF
>gnl|CDD|341487 cd14865, Fe-ADH-like, iron-containing alcohol dehydrogenases (Fe-ADH)-like. This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized
FEFFNPTKIVSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSS
VAVVNEAAARAREAGADGIIAVGGGSVIDTAKGVNILLSEGGDDLDDYGGANRLTRPLKPLIAIPTTAGT
GSEVTLVAVIKDEEKKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPIS
DALALQAIRLISENLPKAVKNGKDLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANS
ILLPHVMRYNLDAAAERYAELALALAYGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQL
EAIAELALNDGAILFNPREVDPEDILAILEAAY
>gnl|CDD|341488 cd14866, Fe-ADH-like, iron-containing alcohol dehydrogenases (Fe-ADH)-like. This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized
HDYPPLRLFSGRGALARLGRELDRLGARRALVVCGSSVGANPDLMDPVRAALGDRLAGVFDGVRPHSPLE
TVEAAAEALREADADAVVAVGGGSAIVTARAASILLAEDRDVRELCTRRAEDGLMVSPRLDAPKLPIFVV
PTTPTTADVKAGSAVTDPPAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRH
ADPLADATLMHALRLLADGLPRLADDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNG
VVHAILLPHVLRFNAPATDGRLDRLAEALGVADAGDEASAAAVVDAVEALLDALGVPTRLRDLGVSREDL
PAIAEAAMDDWFMDNNPRPVPTAEELEALLEAAW
>gnl|CDD|271246 cd14867, uS7_Eukaryote, Eukaryota homolog of Ribosomal Protein S7. uS7, also known as Ribosomal protein (RP)S7, is an important part of the translation process which is universally present in the small subunit of prokaryotic and eukaryotic ribosomes. Eukaryotic RPS7 (also named RPS5) have variable N-terminal regions that affect the efficiency of initiation translation process by impacting small ribosomal subunit to function. The ribosome small subunit is one of the two subunits of ribosome organelles that use mRNA as a template for protein synthesis in a process called translation. The small subunits of bacteria and eukaryotes have the same shape of head, body, platform, beak, and shoulder. RPS7 is located at the head of the small subunit which is a primary ribosomal RNA (rRNA) binding protein that assists in rRNA folding and the binding of other proteins during small subunit assembly in all species. RPS7 is also involved in the formation of the mRNA exit channel at the interface of the large and small subunits. Some ribosomal proteins have extra ribosomal functions in cell differentiation and apoptosis
KLFGKWSYDDVEVKDPSLKDYINLKYPVYVPHTAGRYQKKRFRKAQCPIVERLINSLMMHGRNTGKKLMA
YRIVKHAFEIIHLLTGKNPIQVLVDAIENSGPREDTTRIGYGGTVRRQAVDVSPLRRVNQALRLIATGAR
EAAFRNIKSIAECLADELINAAKGSSNSYAIKKKDELERVAKSNR
>gnl|CDD|271247 cd14868, uS7_Mitochondria_Fungi, Fungal Mitochondrial homolog of Ribosomal Protein S7. uS7, also known as Ribosomal protein (RP)S7, is an important part of the translation process which is universally present in the small subunit of prokaryotic and eukaryotic ribosomes. Fungal and plants mitochondrial RPS7 shows less homology to the mammalian than to bacterial RPS7. The ribosome small subunit is one of the two subunits of ribosome organelles that use mRNA as a template for protein synthesis in a process called translation. The small subunits of bacteria and eukaryotes have the same shape of head, body, platform, beak, and shoulder. RPS7 is located at the head of the small subunit. RPS7 is a primary ribosomal RNA (rRNA) binding protein that assists in rRNA folding and the binding of other proteins during small subunit assembly in all species. RPS7 is also involved in the formation of the mRNA exit channel at the interface of the large and small subunits. Some ribosomal proteins have extra ribosomal functions in cell differentiation and apoptosis
AAPALPAPPLPAQFLNIPPREDPLLEQLTNLIMKHGKKAKAQRIVSRALLHIHTLTRADPLPLLRQAIDS
AAPLVKIKSQKKGAKNVQVPVPLNERQRRRKAIKWILEASDKRPGKSFSERLAEEIIAVVEGTSSALEKK
EQVHKLAVANR
>gnl|CDD|271248 cd14869, uS7_Bacteria, Bacterial homolog of Ribosomal Protein S7. uS7, also known as Ribosomal protein (RP)S7, is an important part of the translation process which is universally present in the small subunit of prokaryotic and eukaryotic ribosomes. Prokaryotic RPS7 is lacking the variable N-terminal region of eukaryotic RPS7. The ribosome small subunit is one of the two subunits of ribosome organelles that use mRNA as a template for protein synthesis in a process called translation. The small subunits of bacteria and eukaryotes have the same shape of head, body, platform, beak, and shoulder. RPS7 is located at the head of the small subunit which is a primary ribosomal RNA (rRNA) binding protein that assists in rRNA folding and the binding of other proteins during small subunit assembly in all species. RPS7 is also involved in the formation of the mRNA exit channel at the interface of the large and small subunits. Some ribosomal proteins have extra ribosomal functions in cell differentiation and apoptosis
ILPDPKYNSVLVSKFINKLMKDGKKSVAEKIVYDALEIIKKKTGKDPLEVFEKALENVKPLVEVRSRRVG
GATYQVPVEVRPERRQSLALRWIIEAARKRKEKSMAEKLAAELLDAANNTGAAVKKKEDTHKMAEANK
>gnl|CDD|271249 cd14870, uS7_Mitochondria_Mammalian, Mammalian Mitochondrial homolog of Ribosomal Protein S7. uS7, also known as Ribosomal protein (RP)S7, is an important part of the translation process which is universally present in the small subunit of prokaryotic and eukaryotic ribosomes. MRPS7 shows more homology to bacterial RPS7 than mitochondrial proteins from plants and fungi. The ribosome small subunit is one of the two subunits of ribosome organelles that use mRNA as a template for protein synthesis in a process called translation. The ribosomes present in mammalian mitochondria have more proteins and low percentage of ribosomal RNA than bacterial ribosomes. The small subunits of bacteria and eukaryotes have the same shape of head, body, platform, beak, and shoulder. RPS7 is located at the head of the small subunit. RPS7 is a primary ribosomal RNA (rRNA) binding protein that assists in rRNA folding and the binding of other proteins during small subunit assembly in all species. RPS7 is also involved in the formation of the mRNA exit channel at the interface of the large and small subunits. Some ribosomal proteins have extra ribosomal functions in cell differentiation and apoptosis
SVYPPHYVEPVYDKQEQEKLLDSGDERELAHRPIKAAKSDETSSVFYDPLVSKFINMMMKKGNKELAREI
VEKTLENIKRIQLEKYHKATDEEKESIELNPLVIFHKAVENCKPLLGLTSVKRGGKTYQVPVPITPNRAR
FLAMKWLIEACREKKRKIRFPEKLARELLDASNNQGKVVKKKQELHKQCEANRAYAHYR
>gnl|CDD|271250 cd14871, uS7_Chloroplast, Chloroplast homolog of Ribosomal Protein S7. Chloroplast RPS7 has both general and specific regulatory roles in chloroplast translation process. uS7, also known as Ribosomal protein (RP)S7, is universally present in the small subunit of prokaryotic and eukaryotic ribosomes. The chloroplasts of plants and algae have bacterial ancestry, but it has adopted novel mechanisms in order to execute its roles within a eukaryotic cell. Chloroplast RPS7 is more homologous to bacterial RPS7 than other eukaryotic mitochondrial proteins. The ribosome small subunit is one of the two subunits of ribosome organelles that use mRNA as a template for protein synthesis in a process called translation. The chloroplast translation regulation is more complex than in bacteria with additional RNA and chloroplast-unique proteins. The small subunits of bacteria and eukaryotes have the same shape of head, body, platform, beak, and shoulder. RPS7 is located at the head of the small subunit. RPS7 is a primary ribosomal RNA (rRNA) binding protein that assists in rRNA folding and the binding of other proteins during small subunit assembly in all species. RPS7 is also involved in the formation of the mRNA exit channel at the interface of the large and small subunits. Some ribosomal proteins have extra ribosomal functions in cell differentiation and apoptosis
KRPIKPDPIYNSRLVNMLVNRILKSGKKSLAYRIVYEALKEIKQKTKQDPLEVLEQAIRNVTPLVEVKAR
RVGGSTYQVPVEVRSERGTALAIRWLLKASRKRSGRSMASKLANEIIDAAKNTGNAIRKKEETHRMAEAN
KAFAHF
>gnl|CDD|276839 cd14872, MYSc_Myo4, class IV myosin, motor domain. These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVD
AMNQSILISGESGAGKTEATKQCLSFFAEVAGSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVE
IHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAAYGYLSLSGCIEVE
GVDDVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEVATLL
GVDAATLEEALTSRLMEIKGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTF
IGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDFIDNQPVLDLIEKK
QPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKD
TLQKDLYVLLSSSKNKLIAVLFPPSEGDQKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRA
RLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRVGPDDRQRCDLLLKSLKQD
FSKVQVGKTRVLYR
>gnl|CDD|276840 cd14873, MYSc_Myo10, class X myosin, motor domain. Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWK
RHDNQCILISGESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNN
NSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENY
HYLNQSGCVEDKTISDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALG
RSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKED
FKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLI
EKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRD
TFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRC
IKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGKCTSL
LQLYDASNSEWQLGKTKVFLR
>gnl|CDD|276841 cd14874, MYSc_Myo12, class XXXIII myosin, motor domain. Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKCHISGVAENALDRIKSMSSNAESIVFG
GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTG
LNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFK
HLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNVEQDVVEIGNMSEVKWVAFLLEVDFDQLV
NFLLPKSEDGTTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGVISILDHYGFEKYNNNGV
EEFLINSVNERIENLFVKHSFHDQLVDYAKDGISVDYKVPNSIENGKTVELLFKKPYGLLPLLTDECKFP
KGSHESYLEHCNLNHTDRSSYGKARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNP
IIGLLFESYSSNTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLL
LAELLSFRIKGYPVKISKTTFARQYRCLLPGDIAMCQNEKEIIQDILQGQGVKYENDFKIGTEYVFLR
>gnl|CDD|276842 cd14875, MYSc_Myo13, class XIII myosin, motor domain. These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ATLLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLLPPHIWQVAHKAFNAIF
VQGLGNQSVVISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKIDENLKWSNPVMESFGNARTV
RNDNSSRFGKYIKLYFDPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLK
TAQDYKCLNGGNTFVRRGVDGKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN
DKAQIADETPFLTACRLLQLDPAKLRECFLVKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFV
NASITPQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKI
EFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPKSTIPNQFGVNHYAA
FVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRKQTVAIRFQRQLTDLRTELESTET
QFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQE
KYSEAAKDFLAYYQRLYGWAKPNYAVGKTKVFLR
>gnl|CDD|276843 cd14876, MYSc_Myo14, class XIV myosin, motor domain. These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLTKLPPHVFYTARRALENLHG
VNKSQTIIVSGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGR
FMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKC
LDVPGIDDVADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLEVFK
EACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGG
FKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDV
LCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSNINFIVVHTIGDIQYNAEGFLFK
NKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPN
ETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLE
SSGLSEDEYAIGKTMVFLK
>gnl|CDD|276844 cd14878, MYSc_Myo16, class XVI myosin, motor domain. These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSSSGQLCSSLPPHLFSCAERAFHQL
FQERRPQCFILSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFI
KYFELQFCERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ
TMREDVSTAERSLNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLL
EQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQD
EQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQ
TGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAVYSPMKDGNGNVALKDQGTAFTV
MHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLVTIASQLRKSLADIIGKLQKCTPH
FIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGEKKKQSA
EERCRLVLQQCKLQGWQMGVRKVFLK
>gnl|CDD|276845 cd14879, MYSc_Myo17, class XVII myosin, motor domain. This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PSDDAITSHLASRFRSDLPYTRLGSSALVAVNPYKYLSSNSDASLGEYGSEYYDTTSGSKEPLPPHAYDL
AARAYLRMRRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTKLSSQISAAEFVLDSFGNAKT
LTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDD
PSDYALLASYGCHPLPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGE
ESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKTKLVRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVV
ETINQKLCAPEDDFATFISLLDFPGFQNRSSTGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGV
SVPATSYFDNSDCVRLLRGKPGGLLGILDDQTRRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGSA
SFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGATQLNAALSELLDTLDRTRLWSVFCIRPNDSQLP
NSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLRGSAAERIRQCARANGWWEGRDYVL
GNTKVFLSYAAWRMLED
>gnl|CDD|276846 cd14880, MYSc_Myo19, class XIX myosin, motor domain. Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPQLYSPELMREYHAAPQPQKLKPHIFTVGEQTYRNVK
SLIEPVNQSIVVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTL
RNNNSSRFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEG
AAFSWLPNPERNLEEDCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTK
ESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVFKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSS
ICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQD
NQTCLDLIEGSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSREPSFIVVHYAGPVRY
HTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPVLTVVSKFKASLEQLLQV
LHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRRLRPH
TSSGPHSPYPAKGLSEPVHCGRTKVFMT
>gnl|CDD|276847 cd14881, MYSc_Myo20, class XX myosin, motor domain. These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
DAVMKCLQARFYAKEFFTNVGPILLSVNPYRDVGNPLTLTSTRSSPLAPQLLKVVQEAVRQQSETGYPQA
IILSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV
TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPANLRYLSHGDTRQNE
AEDAARFQAWKACLGILGIPFLDVVRVLAAVLLLGNVQFIDGGGLEVDVKGETELKSVAALLGVSGAALF
RGLTTRTHNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSLKRLGSTLGTHATDGFIGILD
MFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVEVDYVDNVPCIDLISSLRTGL
LSMLDVECSPRGTAESYVAKIKVQHRQNPRLFEAKPQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDL
VAVFYKQNCNFGFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLET
VNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILQFLEAQPPSKLSSVSTSWALGKRHI
FLS
>gnl|CDD|276848 cd14882, MYSc_Myo21, class XXI myosin, motor domain. The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ENILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHH
EEPQHIILSGESYSGKTTNARLLIKHLCYLGDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQ
LTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRLKEYNLKAGRNYRYLRIPPEV
PPSKLKYRRDDPEGNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGYAELENTEIAS
RVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRA
VFGDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTA
VDQLMTKPDGLFYIIDDASRSCQDQNYIMDRIKEKHSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRD
FVPPEMIETMRSSLDESVKLMFTNSQVRNMRTLAATFRATSLELLKMLSIGANSGGTHFVRCIRSDLEYK
PRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDFDETVEMTKDNCRLLLIRLKME
GWAIGKTKVFLK
>gnl|CDD|276849 cd14883, MYSc_Myo22, class XXII myosin, motor domain. These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
EGINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQED
GKNQSVIISGESGAGKTETTKLILQYLCAVTNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIE
VCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHSKELKEKLKLGEPEDYHYLNQSGC
IRIDNINDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEILKIVAK
LLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRF
IGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFTDNQECLDLIEKP
PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKD
TQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTSRGTSKGKPTVGDTFKHQLQSLVDVLSA
TQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADH
KETCGAVRALMGLGGLPEDEWQVGKTKVFLR
>gnl|CDD|276850 cd14884, MYSc_Myo23, class XXIII myosin, motor domain. These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKELYDQDVMNVYLHKKSNSAASAAPFPKAHIYDIANM
AYKNMRGKLKRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNN
NSSRCGRINLLIFEEVENTQKNMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLAR
RNLVRNCGVYGLLNPDESHQKRSVKGTLRLGSDSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFF
DIIAGILHLGNRAYKAAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFN
KIIEDINRNVLKCKEKDESDNEDIYSINEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIE
KEKRIYARENIICCSDVAPSYSDTLIFIAKIFRRLDDITKLKNQGQKKTDDHFFRYLLNNERQQQLEGKV
SYGFVLNHDADGTAKKQNIKKNIFFIRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLREANNG
GNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRG
LSHKIPKKETAAALKEQIAKELEKCNSNTDIEYQRRLAALDVQFIPDGRLYAFMK
>gnl|CDD|276851 cd14886, MYSc_Myo25, class XXV myosin, motor domain. These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRNLYGTEVIGRYRQADTSRGFPSDLPPHSYAVAQSAL
NGLISDGISQSCIVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSS
RFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFL
NASKCYDAPGIDDQKEFAPVRSQLEKLFSKNEIDSFYKCISGILLAGNIEFSEEGDMGVINAAKISNDED
FGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFD
ADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFTDNSNVL
AVFDKPNLSIFSFLEEQCLIQTGSSEKFTSSCKSKIKNNSFIPGKGSQCNFTIVHTAATVTYNTEEFVDK
NKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKGKFLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQ
DKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQNAGEDLVEAVKSIL
ENLGIPCSDYRIGKTKVFLR
>gnl|CDD|276852 cd14887, MYSc_Myo26, class XXVI myosin, motor domain. These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X, XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PNLLENLYQRYNKAYINKENRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEF
AYCRLVRDRRSQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQGLEARLLQSGPVLEAFGNAHTV
LNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEG
DPESTDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADR
SHSSEVKCLSSGLKVTEASRKHLKTVARLLGLPPGVEGEEMLRLALVSRSVRETRSFFDLDGAAAARDAA
CKNLYSRAFDAVVARINAGLQRSAKPSESDSDEDTPSTTGTQTIGILDLFGFEDLRNHSKNRLEQLCINY
ANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFSFPLASTLTSSPSSTSPFSPTPSFRSSSAFATS
PSLPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNKNIINSAKYKNITPALSRENLEFTVSHFACDVTYD
ARDFCRANREATSDELERLFLACSTYTRLVGSKKNSGVRAISSRRSTLSAQFASQLQQVLKALQETSCHF
IRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREALTPKMF
CKIVLMFLEINSNSYTFGKTKIFFR
>gnl|CDD|276853 cd14888, MYSc_Myo27, class XXVII myosin, motor domain. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPGLYSDEMLLKFIQPSISKSPHVFSTASSAYQGMCNN
KKSQTILISGESGAGKTESTKYVMKFLACAGSEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFG
KFIELQFSKLKSKRMSGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEEN
DEKLAKGADAKPISIDMSSFEPHLKFRYLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIV
AAILYLGNILFENNEACSEGAVVSASCTDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEA
EDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFF
NNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGH
KRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAYLRRGTDGNTK
KKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYP
VRLSHAEFYNDYRILLNGEGKKQLSIWAVGKTLCFFK
>gnl|CDD|276854 cd14889, MYSc_Myo28, class XXVIII myosin, motor domain. These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
KVLLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGR
LARGPKNQCIVISGESGAGKTESTKLLLRQIMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFG
KYIQLRFRNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGA
GCKREVQYWKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGWLKAAA
GQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSV
ELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITYKDNKPILDL
FLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKSPKFTVNHYAGKVTYNASGFLEKN
RDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDNFNSTRKQSVGAQFKHSLGVLMEK
MFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEPAL
PGTKQSCLRILKATKLVGWKCGKTRLFFK
>gnl|CDD|276855 cd14890, MYSc_Myo29, class XXIX myosin, motor domain. Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQ
SGVLDPSNQSIIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEQTLGSLEDRVLSSNP
LLESFGNAKTLRNDNSSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADE
ALRERLKLQTPVEYFYLRGECSSIPSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFES
ENDTTVLEDATTLQSLKLAAELLGVNEDALEKALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSL
FLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEG
IDWQYITFNDNQACLELIEGKVNGKPGIFITLDDCWRFKGEEANKKFVSQLHASFGRKSGSGGTRRGSSQ
HPHFVHPKFDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIREVSVGAQFRTQLQEL
MAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPT
AENIEQLVAVLSKMLGLGKADWQIGSSKIFLK
>gnl|CDD|276856 cd14891, MYSc_Myo30, class XXX myosin, motor domain. Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
AGILHNLEERSKLDNQRPYTFMANVLIAVNPLRRLPEPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGS
GRMQNQSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKRKLSVTSLDERLMDTNPILE
SFGNAKTLRNHNSSRFGKFMKLQFTKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAEL
LKELLLLSPEDFIYLNQSGCVSDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEE
DTSEGEAEIASESDKEALATAAELLGVDEEALEKVITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYE
RLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFETKNDFEQLLINYANEALQATFNQQVFIAEQELYK
SEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSDAKLNETLHKTHKRHPCFPRPHPKDMRE
MFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKV
GVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLTQAILWAFRV
PSDAYRLGRTRVFFR
>gnl|CDD|276857 cd14892, MYSc_Myo31, class XXXI myosin, motor domain. Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASSPPPHVFSIAERAYRAM
KGVGKGQGTPQSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEA
FGNAKTIRNDNSSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENA
ALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENAD
DEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTSTARGSVLEIKLTAREAKNALDALCKYLYGELF
DWLISRINACHKQQTSGVTGGAASPTFSPFIGILDIFGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVL
EQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKRKTTDKQLLTIYHQTHLDKHPHYAK
PRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSKFRTQLAELMEVLWSTTPSYIKCIKP
NNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNKAGVAASPDACDATTAR
KKCEEIVARALERENFQLGRTKVFLR
>gnl|CDD|276858 cd14893, MYSc_Myo32, class XXXII myosin, motor domain. Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQTPLYEKDTVNDAPPHVFALA
QNALRCMQDAGEDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTI
LEAFGNAATRQNRNSSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHD
PTLRDSLEMNKCVNEFVMLKQADPLATNFALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVD
FVPDPEGGKSVGGANSTTVSDAQSCALKDPAQILLAAKLLEVEPVVLDNYFRTRQFFSKDGNKTVSSLKV
VTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRYEKSNIVINSQGVHVLDMVGFENLTPSQNSF
DQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVENRLTVNSNVDITSEQEKCLQLFEDKPFGIFDLLT
ENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSK
NMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNITDSAAT
DVYNQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFF
RRYKNVCGHRGTLESLLRSLSAIGVLEEEKFVVGKTKVYLT
>gnl|CDD|276859 cd14894, MYSc_Myo33, class myosin, motor domain. Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
EELVDALTSRFDDDRIYTYINHHTMAVMNPYRLLQTARFTSIYDEQVVLTYADTANAETVLAPHPFAIAK
QSLVRLFFDNEHTMPLPSTISSNRSMTEGRGQSLFLCGESGSGKTELAKDLLKYLVLVAQPALSKGSEET
CKVSGSTRQPKIKLFTSSTKSTIQMRTEEARTIALLEAKGVEKYEIVLLDLHPERWDEMTSVSRSKRLPQ
VHVDGLFFGFYEKLEHLEDEEQLRMYFKNPHAAKKLSIVLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQ
VAFGLHPWEFQICGCHISPFLLEKSRVTSERGRESGDQNELNFHILYAMVAGVNAFPFMRLLAKELHLDG
IDCSALTYLGRSDHKLAGFVSKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLWLGNIELDY
REVSGKLVMSSTGALNAPQKVVELLELGSVEKLERMLMTKSVSLQSTSETFEVTLEKGQVNHVRDTLARL
LYQLAFNYVVFVMNEATKMSALSTDGNKHQMDSNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSE
KLYAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAQQEEKRNKLFVRN
IYDRNSSRLPEPPRVLSNAKRHTPVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSS
HFCRMLNESSQLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQP
SLVNNDLVEQQCRSQRLIRQMEICRNSSSSYSAIDISKSTLLTRYGSLLREPYILDDVAGDNSNLMNWLR
DLLHSDDCSTPRINISASSMVQFKSINLVER
>gnl|CDD|276860 cd14895, MYSc_Myo34, class XXXIV myosin, motor domain. Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYDLHKYREEMPGWTALPPHVFSIAEGAYRSLRRR
LHEPGASKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGSELLSANPILESFGN
ARTLRNDNSSRFGKFVRMFFEGHELDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDM
KLELQLELLSAQEFQYISGGQCYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLF
VASSEDEGEEDNGAASAPCRLASASPSSLTVQQHLDIVSKLFAVDQDELVSALTTRKISVGGETFHANLS
LAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNPNKAANKDTTPCIAVLDIFGFEEFEVNQFEQ
FCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIFSLLDEECVVPKGSD
AGFARKLYQRLQEHSNFSASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDAHLR
ELFEFFKASESAELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQF
DMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAELGKTR
VFLR
>gnl|CDD|276861 cd14896, MYSc_Myo35, class XXXV myosin, motor domain. This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQST
GQDQCILLSGHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVL
RLHLQHGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACR
LQGKEDAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEIHTAARL
LQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDA
TIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEECQRELLPWVPIPQPPRESCLDLLVD
QPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLPVFTVRHYAGTVTYQVHKFLNRNRDQ
LDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKL
PGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDRERCGAILSQVLGAE
SPLYHLGATKVLLK
>gnl|CDD|276862 cd14897, MYSc_Myo36, class XXXVI myosin, motor domain. This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQRPPHLFWIADQAYRRLLE
TGRNQCILVSGESGAGKTESTKYMIKHLMKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKF
IELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNR
NRPVFNDSEELEYYRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPL
HAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDK
DFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYHDN
DDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASPGNRVAFGIRHYAEQVTYDAD
GFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDE
LVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVRSDDLGKCQKILKTAGIKGYQFGKT
KVFLK
>gnl|CDD|276863 cd14898, MYSc_Myo37, class XXXVII myosin, motor domain. The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
NATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNYSHVEPHVYDVAEASVQDLLVHGNQ
TIVISGESGSGKTENAKLVIKYLVERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD
GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFIDTSSTAGNKESIVQLSEKYKMTC
SAMKSLGIANFKSIEDCLLGILYLGSIQFVNDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKG
ETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERSISVLDIFGFEIFESNGLDQLCINW
TNEKIQNDFIKKMFRAKQGMYKEEGIEWPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVK
IKKYLNGFINTKARDKIKVSHYAGDVEYDLRDFLDKNREKGQLLIFKNLLINDEGSKEDLVKYFKDSMNK
LLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI
TLFEVVDYRKGRTRYFMK
>gnl|CDD|276864 cd14899, MYSc_Myo38, class XXXVIII myosin. The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ASILNALRLRYERHAIYTHIGDILISINPFQDLPQLYGDEILRGYAYDHNSQFGDRVTSTDPREPHLFAV
ARAAYIDIVQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPASPSRTTIEEQV
LQSNPILEAFGNARTVRNDNSSRFGKFIELRFRDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYEL
LSADNNCVSKEQKQVLALSGGPQSFRLLNQSLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIV
AAVLHMGNVDFEQIPHKGDDTVFADEARVMSSTTGAFDHFTKAAELLGVSTEALDHALTKRWLHASNETL
VVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWGADESDVDDEEDATDFIGLLDIFGFE
DMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHRPIGIFSLTDQ
ECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA
QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPR
YVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRRVLLSLYKWGDNDFE
RQMRCGVSLGKTRVFFR
>gnl|CDD|276865 cd14900, MYSc_Myo39, class XXXIX myosin, motor domain. The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
TTILSALETRFYAQKIYTNTGAILLAVNPFQKLPGLYSSDTMAKYLLSFEARSSSTRNKGSDPMPPHIYQ
VAGEAYKAMMLGLNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIAAKVLQ
TNILLESFGNARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIG
ASEAARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSSIWSR
DAAATLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDD
SSKSHGGLHFIGILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDN
QDCVNLISQRPTGILSLIDEECVMPKGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYS
TDGFLEKNKDVLHQEAVDLFVYGLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRC
NGVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNRLLAKKQGTSLPDTDSDHGPAVVSPEARDLLK
>gnl|CDD|276866 cd14901, MYSc_Myo40, class XL myosin, motor domain. The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYYEHGERRAAGERKLPPHVYAVADKAF
RAMLFASRGQKCDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAF
GNARTNRNNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHA
LGLTHVEEYKYLNSSQCYDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDG
EGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDW
LVDRINESIAYSESTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAI
PWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASFSVSKLQQGKRQFVI
HHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSSTVVAKFKVQLSSLLEVLNATEPHFIRCIKP
NDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMS
QLQHSELNIEHLPPFQVGKTKVFLL
>gnl|CDD|276867 cd14902, MYSc_Myo41, class XLI myosin, motor domain. The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
AALLQALSERFEHDQIYTSIGDILVALNPLKPLPDLYSESQLNAYKASMTSTSPVSQLSELPPHVFAIGG
KAFGGLLKPERRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVEIGKRILQTNPILES
FGNAQTIRNDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD
LLGLQKGGKYELLNSYGPSFARKRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT
AENGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIY
GRLFTWLVRRLSDEINYFDSAVSISDEDEELATIGILDIFGFESLNRNGFEQLCINYANERLQAQFNEFV
FVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALSTKFYRYHGGLGQFV
VHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSPGADNGAAGRRRYSMLRAPS
VSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHA
SFIELFSGFKCFLSTRDRAAKMNNHDLAQALVTVLMDRVLLEDGVEREEKNPGALTAVTGDGSGTAFEND
CRRKDVQVGRTLVFCK
>gnl|CDD|276868 cd14903, MYSc_Myo42, class XLII myosin, motor domain. The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKR
SGRNQSILVSGESGAGKTETTKILMNHLATIAGGLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKF
TQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTGANKTIK
IEGMSDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGDQGAVYATKL
LGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHI
GVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDFADNQDVLAVIEDRL
GIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTYESLGFLEKHKDALL
PDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNV
HYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNTDVPVA
ERCEALMKKLKLESPEQYQMGLTRIYFQ
>gnl|CDD|276869 cd14904, MYSc_Myo43, class XLIII myosin, motor domain. The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLT
NEMNQSILVSGESGAGKTETTKIVMNHLASVAGGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKF
TQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLA
QMQIPGLDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQVAKM
LGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQ
IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQDNQGIVEVIDGK
MGIIALMNDHLRQPRGTEEALVNKIRTNHQTKKDNESIDFPKVKRTQFIINHYAGPVTYETVGFMEKHRD
TLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEGKSGKGTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVR
CIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSKDVRRTCSV
FMTAIGRKSPLEYQIGKSLIYFK
>gnl|CDD|276870 cd14905, MYSc_Myo44, class XLIV myosin, motor domain. There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
DTLINIIQARYKKEIIYTYIGPILVSVNPLRYLPFLHSQELVRNYNQRRGLPPHLFALAAKAISDMQDFR
RDQLIFIGGESGSGKSENTKIIIQYLLTTDLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFE
MFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSIS
VESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNGKTEVKDRTLIESLSHNITFD
STKLENILISDRSMPVNEAVENRDSLARSLYSALFHWIIDFLNSKLKPTQYSHTLGILDLFGQESSQLNG
YEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWMTPISFKDNEESVEMMEKIINLLDQESKNINSSD
QIFLEKLQNFLSRHHLFGKKPNKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSRDGV
FNINATVAELNQMFDAKNTAKKSPLSIVKVLLSCGSNNPNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYT
TYSSTNKAINNSNCDFHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDR
FSFFFQNQRNFQNLFEKLKENDINIDSILPPPIQVGNTKIFLR
>gnl|CDD|276871 cd14906, MYSc_Myo45, class XLV myosin, motor domain. The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISSIYSNLILNEYKDINQNKSPIPHIYAVALRAYQSMV
SEKKNQSIIISGESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTT
KNHNSSRFGKFLKIEFRSSDGKIDGASIETYLLEKSRISHRPDNINLSYHIFYYLVYGASKDERSKWGLN
NDPSKYRYLDARDDVISSFKSQSSNKNSNHNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHL
GNIEFEEDSDFSKYAYQKDKVTASLESVSKLLGYIESVFKQALLNRNLKAGGRGSVYCRPMEVAQSEQTR
DALSKSLYVRLFKYIVEKINRKFNQNTQSNDLAGGSNKKNNLFIGVLDIFGFENLSSNSLEQLLINFTNE
KLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMPKGSEQSLLEKYN
KQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITST
TNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKV
RKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNKKKNNSNSNSNTTN
DKPLFQIGKTKIFIS
>gnl|CDD|276872 cd14907, MYSc_Myo46, class XLVI myosin, motor domain. The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDNLFSEEVMQMYKEQIIQNGEYFDIKKEPPHIYAIAA
LAFKQLFENNKKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATSKSTKSIEQKI
LSCNPILEAFGNAKTVRNDNSSRFGKYVSILVDKKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHL
LYGADQQLLQQLGLKNQLSGDRYDYLKKSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAI
LLLGNLQFDDSTLDDNSPCCVKNKETLQIIAKLLGIDEEELKEALTTKIRKVGNQVITSPLSKKECINNR
DSLSKELYDRLFNWLVERLNDTIMPKDEKDQQLFQNKYLSIGLLDIFGFEVFQNNSFEQLCINYTNEKLQ
QLYISYVFKAEEQEFKEEGLEDYLNQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKLATGTDEKLLNKIKK
QHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDGSQ
QQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLE
SIRVRKQGYPYRKSYEDFYKQYSLLKKNVLFGKTKIFMK
>gnl|CDD|276873 cd14908, MYSc_Myo47, class XLVII myosin, motor domain. The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQEGLLRSQGIESPQALGPHVFAIAD
RSYRQMMSEIRASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGKLSIMDRVLQSNPIL
EAFGNARTLRNDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEE
HEKYEFHDGITGGLQLPNEFHYTGQGGAPDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHL
GQLEFESKEEDGAAEIAEEGNEKCLARVAKLLGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDA
LAKTIYGALFLWVVATVNSSINWENDKDIRSSVGVLDIFGFECFAHNSFEQLCINFTNEALQQQFNQFIF
KLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDECRLGIRGSDANYASRLYETYLPEKNQT
HSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCEKNKDEIPLTADSLFESGQQFKAQLHSLIEMIE
DTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPLIPEVV
LSWSMERLDPQKLCVKKMCKDLVKGVLSPAMVSMKNIPEDTMQLGKSKVFMR
>gnl|CDD|276874 cd14909, MYSc_Myh1_insects_crustaceans, class II myosin heavy chain 1, motor domain. Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTN
HVNQSMLITGESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDN
SSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDY
YIVSQGKVTVPNVDDGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEE
GGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQ
QKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLAC
IDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAGCVSYN
ITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSL
MTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPA
GIQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR
>gnl|CDD|276875 cd14910, MYSc_Myh1_mammals, class II myosin heavy chain 1, motor domain. Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTD
RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTV
RNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTN
PYDYAFVSQGEITVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPD
GTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQ
LDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMD
LAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAHFSLIHYAGTV
DYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKGGKKKGSSFQTVSALFRENL
NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL
NASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK
>gnl|CDD|276876 cd14911, MYSc_Myh2_insects_mollusks, class II myosin heavy chain 2, motor domain. Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGD
REDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFG
NAKTVKNDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKF
ILDDVKSYAFLSNGSLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQ
ATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNR
INRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFI
DFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGVADFAIVHYAGR
VDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRKGMFRTVSHLY
KEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR
YELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR
>gnl|CDD|276877 cd14912, MYSc_Myh2_mammals, class II myosin heavy chain 2, motor domain. Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTD
RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTV
RNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTN
PYDYPFVSQGEISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPD
GTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQ
LDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMD
LAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAHFSLIHYAGVV
DYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGGKKKGSSFQTVSALFRE
NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK
VLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK
>gnl|CDD|276878 cd14913, MYSc_Myh3, class II myosin heavy chain 3, motor domain. Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTD
RENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRN
DNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPY
DYPFISQGEILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGT
EVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD
TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLA
ACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFSLIHYAGTVDY
SVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKL
MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAS
AIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK
>gnl|CDD|276879 cd14915, MYSc_Myh4, class II myosin heavy chain 4, motor domain. Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTD
RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTV
RNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTN
PYDFAFVSQGEITVPSIDDQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPD
GTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQ
LDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMD
LAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAHFSLVHYAGTV
DYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSFQTVSALFRENL
NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL
NASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK
>gnl|CDD|276880 cd14916, MYSc_Myh6, class II myosin heavy chain 6, motor domain. Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTD
RENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVR
NDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNP
YDYAFVSQGEVSVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDG
TEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATL
ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDL
QACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHFSLVHYAGTVD
YNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENLN
KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN
PAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK
>gnl|CDD|276881 cd14917, MYSc_Myh7, class II myosin heavy chain 7, motor domain. Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTD
RENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRN
DNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPY
DYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGT
EEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE
TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQ
ACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFSLIHYAGTVDY
NIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL
MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA
AIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK
>gnl|CDD|276882 cd14918, MYSc_Myh8, class II myosin heavy chain 8, motor domain. Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTD
RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRN
DNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPY
DYAFVSQGEITVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT
EVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD
TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLA
ACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFSLIHYAGTVDY
NITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKL
MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS
AIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK
>gnl|CDD|276883 cd14919, MYSc_Myh9, class II myosin heavy chain 9, motor domain. Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQD
REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSR
FGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS
NGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKV
SHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQG
ASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDL
IEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEW
LMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQL
AKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL
TPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR
>gnl|CDD|276952 cd14920, MYSc_Myh10, class II myosin heavy chain 10, motor domain. Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQD
REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDN
SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYR
FLSNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVA
QKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTK
RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPC
IDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKA
DEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK
ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY
EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR
>gnl|CDD|276885 cd14921, MYSc_Myh11, class II myosin heavy chain 11, motor domain. Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQD
REDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDN
SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYT
FLSNGFVPIPAAQDDEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAA
QKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTH
RQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPC
IELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSIIHYAGKVDYNA
SAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK
EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY
EILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR
>gnl|CDD|276887 cd14923, MYSc_Myh13, class II myosin heavy chain 13, motor domain. Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTD
RDNQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVR
NDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNP
FDFPFVSQGEVTVASIDDSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDG
TEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQL
DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDL
AACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHFSLVHYAGTVD
YNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGSKKGGKKKGSSFQTVSAVFRENL
NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL
NASAIPEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK
>gnl|CDD|276953 cd14927, MYSc_Myh7b, class II myosin heavy chain 7b, motor domain. Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRN
RENQSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAK
TLRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVS
MNPYDYHFCSQGVTTVDNMDDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAE
ADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRIN
QTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFG
LDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKYEAHFEVVHYA
GVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKSGVKEKRKKAASFQTVSQL
HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQ
RYRILNPSAIPDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK
>gnl|CDD|276892 cd14929, MYSc_Myh15_mammals, class II myosin heavy chain 15, motor domain. Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHN
RENQSILFTGESGAGKTVNTKHIIQYFATIAAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSR
FGKFIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCS
CGAVAVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKA
AFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQ
FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLI
EKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFELVHYAGVVPYNISGWL
EKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLHKENLNKLMTNLKS
TAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSK
FVSSRKAAEELLGSLEIDHTQYRFGITKVFFK
>gnl|CDD|276893 cd14930, MYSc_Myh14_mammals, class II myosin heavy chain 14 motor domain. Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations
ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQD
REDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDN
SSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYR
FLTNGPSSSPGQERELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQ
KLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPR
QGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCI
DLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVLHYAGKVDYKAN
EWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESL
SRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL
TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR
>gnl|CDD|276895 cd14932, MYSc_Myh18, class II myosin heavy chain 18, motor domain. Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQD
REDQSILCTGESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTV
KNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDY
SKYRFLSNGNVTIPGQQDKELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPD
DTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKAL
DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLD
LQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDADFCIIHYAGKV
DYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHGAFKTRKGMFRTVGQ
LYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR
QRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR
>gnl|CDD|276896 cd14934, MYSc_Myh16, class II myosin heavy chain 16, motor domain. Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations
ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMD
RENQSMLITGESGAGKTENTKKVIQYFANIGGTGKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSS
RFGKFIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHW
VSQGVTVVDNMDDGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVAD
KVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQ
RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACID
LLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGPEAHFELVHYAGTVGYNIT
GWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGSKKQKRGSSFMTVSNFYREQLNKLMTTLHSTA
PHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFVD
NKKASELLLGSIDLDVNEYKIGHTKVFFR
>gnl|CDD|276897 cd14937, MYSc_Myo24A, class XXIV A myosin, motor domain. These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQ
SIIISGESGSGKTEASKLVIKYYLSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELD
EYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEID
DAKDFGNLMISFDKMNMHDMKDDLFLTLSGLLLLGNVEYQEIEKGGKTNCSELDKNNLELVNEISNLLGI
NYENLKDCLVFTEKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGIL
DIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTNESIIDLLRGKTSII
SILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNI
VRLLKVSNNKLVRSLYEDVEVSESLGRKNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQ
KKVFPQLFSLSIIETLNISFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQNTVDPDLYKVG
KTMVFLK
>gnl|CDD|276898 cd14938, MYSc_Myo24B, class XXIV B myosin, motor domain. These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEDLSLNEYHVVHNALKNLNE
LKRNQSIIISGESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDNIHNEENTDYQFNMSEMLKHVN
VVMEAFGNAKTVKNNNSSRFSKFCTIHIENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSD
KFKKMYFLKNIENYSMLNNEKGFEKFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVK
AFRKKSLLMGKNQCGQNINYETILSELENSEDIGLDENVKNLLLACKLLSFDIETFVKYFTTNYIFNDSI
LIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININTNYINVLDMAYFENSKDNSLEQLL
INTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTEGSLFSLLENVSTKTIFDK
SNLHSSIIRKFSRNSKYIKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSENEYM
RQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKP
NESKRELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNEDLKEKVEALIKSYQISN
YEWMIGNNMIFLS
>gnl|CDD|320093 cd14939, 7tmD_STE2, fungal alpha-factor pheromone receptor STE2, member of the class D family of seven-transmembrane G protein-coupled receptors. This subfamily represents the alpha-factor pheromone receptor encoded by the STE2 gene, which is required for pheromone sensing and mating in haploid cells of the yeast Saccharomyces cerevisiae. The STE2-encoded seven-transmembrane domain receptor is a member of the class D GPCRs. Class D receptors are composed of two major subfamilies: Ste2 and Ste3. These two GPCRs (Ste2 and Ste3) sense the polypeptide mating pheromones, alpha-factor and a-factor, which activate a G protein-coupled receptors on the surface of the opposite yeast-mating haploid-types (MATa and MAT-alpha), respectively. Activation of these receptors by pheromones leads to activation of the mitogen-activated protein kinase (MAPK) signal transduction cascades, G1 cell cycle arrest, and polarized cell growth in the direction of the partner cell (a process called shmooing), which ultimately induces cell-cell fusion and the formation of a diploid zygote. Like all GPCRs, these pheromone mating factor receptors possess the same basic architecture of seven-transmembrane (7TM) domains and share common signaling mechanisms; however, there is no significant sequence similarity either between Ste2 and Ste3, or between these two receptors and the other 7TM GPCRs. Thus, STE2 and STE3 represent phylogenetically distinct groups
LDAFVQYNIRTSINYGVQIGACLLMLLVLLLLTKKKKRRSPIFILNQLSLLLNIIRSLLLLLYFTSPFSS
FYFYFTGDYSRVPRSDYAVSVAANVLSVLLVALIEASLVLQVWVMFKLWPRKWRIILTALSALLALVTVG
FRFASAVLNIRAILNLSTSVSYSWLRSAALILFAASINFFSLLFVVKLVLAIRTRRYLGLKQFGPMHILF
IMSGQTMIIPSIFAILQYALSVSNFELGSLTLTLVVLSLPLSSLWAQRANNSSSS
>gnl|CDD|320094 cd14940, 7tmE_cAMP_R_Slime_mold, slime mold cyclic AMP receptor, member of the class E family of seven-transmembrane G protein-coupled receptors. This family represents the class E of seven-transmembrane G-protein coupled receptors found in soil-living amoebas, commonly referred to as slime molds. The class E family includes cAMP receptors (cAR1-4) and cAMP receptors-like proteins (CrlA-C) from Dictyostelium discoideum, and their highly homologous cAMP receptors (TasA and TasB) from Polysphondylium pallidum. So far, four subtypes of cAMP receptors (cAR1-4) have been identified that play an essential role in the detection and transmit of the periodic extracellular cAMP waves that regulate chemotactic cell movement during Dictyostelium development, from the unicellular amoeba aggregate into many multicellular slugs and then differentiate into a sporocarp, a fruiting body with cells specialized for different functions. These four subtypes differ in their expression levels and patterns during development. cAR1 is high-affinity receptor that is the first one to be expressed highly during early aggregation and continues to be expressed at low levels during later developmental stages. cAR1 detects extracellular cAMP and is coupled to G-alpha2 protein. Cells lacking cAR1 fail to aggregate, demonstrating that cAR1 is responsible for aggregation. During later aggregation the high-affinity cAR3 receptor is expressed at low levels. Nonetheless, cells lacking cAR3 do not show an obviously altered pattern of development and are still able to aggregate into fruiting bodies. In contrast, cAR2 and cAR4 are low affinity receptors expressed predominantly after aggregation in pre-stalk cells. cAR2 is essential for normal tip formation and deletion of the receptor arrests development at the mound stage. On the other hand, CAR4 regulates axial patterning and cellular differentiation, and deletion of the receptor results in defects during culmination. Furthermore, three cAMP receptor-like proteins (CrlA-C) were identified in Dictyostelium that show limited sequence similarity to the cAMP receptors. Of these CrlA is thought to be required for normal cell growth and tip formation in developing aggregates
ALYAILLFADFSSIIGCLFVLVGFWLLKLLRNHITRVISCFCLTSLLKDIIYTMLTLTQSARPDGFLCYL
YAIVITYGSLSCWLWTLCLAISIYLLIVKREPEPEKFEKYYHFVCWGLPLISTIIMLIKHHYGPVGNWCW
IGNQYTGYRFGLFYGPFFIIFGISAVLVGLTSHYTYQVIHNWVSDNKDLHKTYQFKLVNYIIVFLLCWIF
AVINRIQNALNPFPFALNLLHTYLSPSHGFYASVVFIYNNPLMWRY
>gnl|CDD|271344 cd14941, TRAPPC_bet3-like, Bet3-like domains of TRAPP. Bet3-like domains of a subfamily of core components of the trafficking protein particle complex (TRAPP) include TRAPPC3, TRAPPC5, and TRAPPC6A. TRAPP complexes play a key role in the regulation of ER-to-Golgi and intra-Golgi transport by tethering the vesicle membrane to the target membrane. TRAPPs are large multimeric protein complexes which contain six core subunits that belong to two distinct structural families, the bet3-like family and the sedlin-like family
SVSLFALLFGEMVSQLCKDYESVGDVNTKLADMGFNIGARLIEDFLARKNGKRCTKVLDILLFIKKNAWK
ALFGKTPDILNWSHDDDTYSLIDNEPPLNDFISLPDENSSLNYSAFTCGIIRGILENVGFPCKVTAHWDK
LGGDPGTEIMIK
>gnl|CDD|271345 cd14942, TRAPPC3_bet3, Bet3-TRAPPC3 subunit of the TRAPP complex. Bet3 (also known as TRAPPC3) subunit of the trafficking protein particle complex (TRAPP). Bet3 is one of the six core subunits of TRAPP complexes which play a key role in the regulation of ER-to-Golgi and intra-Golgi transport by tethering the vesicle membrane to the target membrane. TRAPPC3 has also been shown to be additionally important for membrane fusion during the formation of vesicular tubular clusters (VTC). In its core, Bet3 forms a hydrophobic channel that also contains a conserved acylation site
NAELFTLTYGALVAQLLKDYEDVEEVNKQLDKMGYNIGVRLIEEFLAKSGVGRCKDFRETAEVIAKVAFK
MFLGVTAEVTNWSSDGDEFSLILEENPLADFVELPPELSGLWYSNILCGVIRGALEMVQMRVEVTFVQDT
LRGDDVTEIRVKLIE
>gnl|CDD|271346 cd14943, TRAPPC5_Trs31, Trs31 subunit of the TRAPP complex. TRS31 (also known as TRAPPC5) subunit of the trafficking protein particle complex (TRAPP). TRS31 is one of the six core subunits of TRAPP complexes which play a key role in the regulation of ER-to-Golgi and intra-Golgi transport by tethering the vesicle membrane to the target membrane
VSLSAFAFLFSEMVQYAQRRVKSISELEQRLSELGYRVGIRLLELLSLREKGPKRETRILSILQFIKTTV
WKYLFGKEADSLEKSTDDDNEYMIIDNEPLVNKFISVPKDMGGLNCAAFVAGIIEGVLDSAGFPAKVTAH
TVPDEGFPPRTTFLIKFD
>gnl|CDD|271347 cd14944, TRAPPC6A_Trs33, Trs33 subunit of the TRAPP complex. TRS33 (also known as TRAPPC6A) subunit of the trafficking protein particle complex (TRAPP). TRS33 is one of the six core subunits of TRAPP complexes which play a key role in the regulation of ER-to-Golgi and intra-Golgi transport by tethering the vesicle membrane to the target membrane. In mammals, mutations in TRAPPC6a cause mosaic loss of coat pigment
SESLFDFLLIEMVPYLLASASELKESEELDDAEEEDDEAVLSRLEAIGFRVGLRLAERLTKDRPRFSDPL
DVIKFICKDFWTAVFGKQIDNLRTNHRGVYVLQDNSFRWLSRLSSGDGAAQSLEEAPPYLAFPCGIIRGA
LANLGIPSTVTAEVTSLPGCTFQIRIQ
>gnl|CDD|271253 cd14945, Myo5-like_CBD, Cargo binding domain of myosin 5 and similar proteins. Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5 a,b,c) in vertebrates and two (myo2 and myo4) in fungi and related to plant class XI myosins. Their C-terminal cargo binding domains is important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. MyoV-CBDs interact with several adaptor proteins that in turn interact with the cargo
SEEDSLLRGIVTDFEPSSGDHKLTPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQHNDDMQLL
AFWLSNASELLYFLKQDSKLYGAAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQPK
IRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWSRGMQIRANISRLEEWC
EGRGLEHLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYGESPVPKEIL
RTLAAEVS
>gnl|CDD|380670 cd14946, Tet_JBP, oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and similar proteins. TET proteins are involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. Alterations in TET protein function have been linked to cancer, and TETs influence many cell differentiation processes. J binding protein (JBP) 1 and JBP2 are thymidine hydroxylases that catalyze the first step of base J biosynthesis: the hydroxylation of thymine in DNA to form 5-hydroxymethyluracil (hmU). Base J (beta-d-glucopyranosyloxymethyluracil) is a hyper-modified DNA base found in the DNA of kinetoplastids (Trypanosoma brucei, Trypanosoma cruzi, and Leishmania). JBP1 and JBP2 each contain a J-DNA binding domain and a thymidine hydroxylase domain. Members of this TET/JBP family of dioxygenases require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity
LLENMLSKCGTQQSFANANITLKYEGKEGKSQGCPKALKNVRTSKLAYFVCDHDGSVILAYVPEVLPKEL
VEEFTEKLESIQTKRGTLDPETKGDTGYSGILDNSMPFNYVTADLSQELGQYLSEIVNPQISYYISKLLT
CVSPRTINYLVEYEHRSLNDSYYALNNCLYPSTAFNSLKRIRKPHKDNLDIQNGPSSLFYFGNFQNTEGY
LELTLKKVIGNCAVFVQPGDVLFFKGNEYKHVVTNITNPNNHGWRISLVYYAHK
>gnl|CDD|271343 cd14947, NBR1_like, Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins. NBR1 has been characterized as a specific late endosomal protein, which might play a role in receptor (RTK) trafficking. Specifically, NBR1 was shown to inhibit ligand-mediated receptor internalization from the cell surface. The region covered by this domain model may be involved in that function, as the C-terminus (which contains a UBA domain) was shown to be essential but not sufficient by itself. In an earlier yeast two-hybrid study, the region in mouse NBR1 covered by this domain has been shown to interact with CIB (calcium and integrin-binding protein) and FEZ1 (fasciculation and elongation protein zeta-1). Thus, NBR1 may play a role in cellular signalling pathways and possibly in neural development
PGLSAAFVEDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSAPERVPVPSTVPGE
EVDVSVELRAPSEPGRYISYWRLVTPDGLPFGDRLWVDITVE
>gnl|CDD|271342 cd14948, BACON, Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes
TLSVSPSELTFDAEGGTQTITVTSNGDWTATSDADWLTVSPTSGTGDGTVTVTVAANTTGEERTATITVT
AGGLSKTITVTQE
>gnl|CDD|271340 cd14949, Asparaginase_2_like_3, Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family. The wider family of Asparaginase 2-like enzymes includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue
PKLIIHGGFGSESSTNGETKAAKQEALAEIVEEVYEYLKSHSALEAVVYAVSLLEDDPLFNAGTGSQIQS
DGQIRMSASLMDGQTQRFSGVINIENVKNPIEVAQKLQQEDDRVLSGEGATEFARENGFPEYNPETPQRR
QEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATVAGNYANAFAGVSCTGIGEDI
VSEALAAKIVTRVTDGMSLQEAFEKSFAEAKPRDGFAGAIGIDSKGNIYHGDTHPVMVYASYDGEKIGVF
>gnl|CDD|271341 cd14950, Asparaginase_2_like_2, Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family. The wider family of Asparaginase 2-like enzymes includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue
ALVVHGGAGSWKNSDDEEKALRALREALERGYEALRRGSALEAVVEAVAYMEDSGVFNAGVGSVLNLEGE
VEMDAGIMDGRTLRVGAVAAVRAVKNPIRLARKVMEKTDHVLIVGEGADELAKRLGGDTVGAVALDKDGN
LAAATSTGGVWLKLPGRVGDSPIPGAGFYATNGVAVSATGIGEVIIRSLPALRADELVSMGGDIEEAVRA
VVNKVTETFGKDTAGIIGIDARGNIAAAFNTEAMPRGYIDD
>gnl|CDD|271321 cd14951, NHL-2_like, NHL repeat domain of NHL repeat-containing protein 2 and similar proteins. NHL repeat-containing protein 2 (NHLRC2) and related bacterial proteins; members of this eukaryotic and bacterial family are uncharacterized, the NHL repeat domain is found C-terminally of a thioredoxin domain. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures
IGSGERGLKDGSFAEASFNEPQGLALLPGNILYVADTENHALRKIDLETGTVTTLAGTGEQGRDGEGGGP
GREQPLSSPWDVAWGPEDDILYIAMAGTHQIWAYDLDTGTCRVFAGSGNEGNRNGPYPHEAWFAQPSGLS
LAGWGELFVADSESSAIRAVSLKDGGVKTLVGGTRVGTGLFDFGDRDGPGAEALLQHPLGVAALPDGSVY
VADTYNHKIKRVDPATGEVSTLAGTGKAGYKDLEAQFSEPSGLVVDGDGRLYVADTNNHRIRRLDLPTEA
LEVLTLAHRTLRPATPPAPGPLRLRVRFTAPAGQKLDDRWGPSTRLKLSISPPE
>gnl|CDD|271322 cd14952, NHL_PKND_like, NHL repeat domain of the protein kinase PknD. PknD is a mycobacterial transmembrane protein with a cytosolic kinase domain and an extracellular sensor domain that contains NHL repeats. It plays a key role in the development of central nervous system tuberculosis, by mediating the invasion of host brain endothelia. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures
QTVLPFTGLDGPGGVAVDAAGNVYVADSGNNRVLKLAAGSTTQTVLPFTGLYQPQGVAVDAAGTVYVTDF
GNNRVLKLAAGSTTQTVLPFTGLNDPTGVAVDAAGNVYVADTGNNRVLKLAAGSNTQTVLPFTGLSNPDG
VAVDGAGNVYVTDTGNNRVLKLAAGSTTQTVLPFTGLNSPSGVAVDTAGNVYVTDHGNNRVLKLAAGSTT
PTVLPFTGLNGPLGVAVDAAGNVYVADRGNDRVVKLP
>gnl|CDD|271323 cd14953, NHL_like_1, Uncharacterized NHL-repeat domain in bacterial proteins. This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures
VSTVAGSGTAGFSGGGGTAARFNSPSGVAVDAAGNLYVADRGNHRIRKITPDGVVTTVAGTGTAGFADGG
GAAAQFNTPSGVAVDAAGNLYVADTGNHRIRKITPDGVVSTLAGTGTAGFSDDGGATAAQFNYPTGVAVD
AAGNLYVADTGNHRIRKITPDGVVTTVAGTGGAGYAGDGPATAAQFNNPTGVAVDAAGNLYVADRGNHRI
RKITPDGVVTTVAGTGTAGFSGDGGATAAQLNNPTGVAVDAAGNLYVADSGNHRIRKITPAGVVTTVAGG
GAGFSGDGGPATSAQFNNPTGVAVDAAGNLYVADTGNNRIRKI
>gnl|CDD|271324 cd14954, NHL_TRIM71_like, NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins. The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures
RDYRAKGRPLLSFGKEGSKDGELCRPWGVAVDKDGRIIVADRSNNRVQVFDPDGKFLRKFGSYGSRDGQF
DRPAGVAVNSRGRIIVADKDNHRIQVFDLNGRFLLKFGERGTKNGQFNYPWGVAVDSEGRIYVSDTRNHR
VQVFDSDGQFIRKFGFEGAGPGQLDSPRGVAVNPDGNIVVSDFNNHRLQVFDPDGQFLRFFGSEGSGNGQ
FKRPRGVAVDDEGNIIVADSGNHRVQVFSPDGEFLCSFGTEGNGEGQFDRPSGVAVTPDGRIVVVDRGNH
RIQVF
>gnl|CDD|271325 cd14955, NHL_like_4, Uncharacterized NHL-repeat domain in bacterial and archaeal proteins. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures
FVTQWGSYGSGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDSTGTFLTKWGSSGSGDGQFYSPTGIAV
DSDGNVYVADTGNHRIQKFDSTGTFLTKWGSSGSGDGQFNSPSGIAVDSAGNVYVTDSGNNRIQKFDSSG
TFITKWGSFGSGDGQFNSPTGIAVDSAGNVYVADTGNNRIQKFTSTGTFLTKWGSEGSGDGQFNAPYGIA
VDSAGNVYVADTGNNRIQKFDSSGTFITKWGSEGSGDGQFNSPSGIAVDSAGNVYVADSGNNRIQKFAP
>gnl|CDD|271326 cd14956, NHL_like_3, Uncharacterized NHL-repeat domain in bacterial proteins. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures
SWGGRGSGPGQFKDPRGIAVDADDNVYVADARNGRIQVFDKDGTFLRRFGTTGDGPGQFGRPRGLAVDKD
GWLYVADYWGDRIQVFTLTGELQTIGGSSGSGPGQFNAPRGVAVDADGNLYVADFGNQRIQKFDPDGSFL
RQWGGTGIEPGSFNYPRGVAVDPDGTLYVADTYNDRIQVFDNDGAFLRKWGGRGTGPGQFNYPYGIAIDP
DGNVFVADFGNNRIQKFTADGTFLTSWGSPGTGPGQFKNPWGVVVDADGTVYVADSNNNRVQRF
>gnl|CDD|271327 cd14957, NHL_like_2, Uncharacterized NHL-repeat domain in bacterial and archaeal proteins. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures
ASFSYAFGSNGSGNGQFNTPRGIAVDSAGNIYVADTGNNRIQVFTSSGVYSYSIGSGGTGSGQFNSPYGI
AVDSNGNIYVADTDNNRIQVFNSSGVYQYSIGTGGSGDGQFNGPYGIAVDSNGNIYVADTGNHRIQVFTS
SGTFSYSIGSGGTGPGQFNGPQGIAVDSDGNIYVADTGNHRIQVFTSSGTFQYTFGSSGSGPGQFSDPYG
IAVDSDGNIYVADTGNHRIQVFTSSGAYQYSIGTSGSGNGQFNYPYGIAVDNDGKIYVADSNNNRIQVFN
>gnl|CDD|271328 cd14958, NHL_PAL_like, Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5). PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures
MVSSWPSASLKLGQVSGVAVDSLGNGVVFHRGGRVWDANSFDANVYVFKGPIEEDTILVFDPDGGFLRSW
GAGLFYMPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEPGSDQTHFCKPTDVAVAPDGD
IFVADGYCNSRIVKFSPDGKLLKSWGEPGSGPGQFNLPHSIALDEDGRVYVADRENGRIQVFDADGKFLT
EWTNPELGRPYALAIDPDGLLYVVDGPPRLNRSLPVRGFVIRIGKGLILGRFGPGGKAPGQFQNPHDIAV
DSGGDIYVGELGPNRVQKFV
>gnl|CDD|271329 cd14959, NHL_brat_like, NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins. Drosophila brain-tumor (brat) has been identified as a tumor suppressor that negatively regulates cell proliferation during development of the Drosophila larval brain. It appears to be recruited to the 3'-untranslated region of hunchback RNA and regulates its translation by forming a complex with Pumilio (Pum) and Nanos (Nos). The NHL domain of brat appears to be involved by interacting with the RNA-binding Puf repeats of Pumilio, a sequence-specific RNA binding protein. This family also contains the Caenorhabditis elegans homolog NCL-1. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures
KRSKMIIHCKFGESGSGEGQFNSPSGFCLGEDEDILVADTNNHRIQVFDKEGEFKFQFGIPGKRDGQLWY
PNKVAVCRVTGRYVVTDRGNPRHRMQIFTKRGQFVRKFGARYLQHVRGLTVDAAGHIIVVESKVMRVFIF
DESGNVLKWFDCSKYLEEPSDVAVNDNEIYICDNKGHCVVVFNYDGQFLRRIGGEGITNYPIGVDISSAG
DVLVADNHGNHFHVTVFTRDGQLISEFECPRVKHSRCCGLALTSEGSIVTLSKHNHHVLVFNTL
>gnl|CDD|271330 cd14960, NHL_TRIM2_like, NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins. The E3 ubiquitin-protein ligase TRIM2 is responsible for ubiquinating the apoptosis-inducing Bcl-2-interacting mediator of cell death (Bim), when the latter is phosphorylated by p42/p44 MAPK. TRIM2 regulates the ubiquitination of neurofilament light subunit (NF-L), deficiencies in TRIM2 result in increased NF-L levels in axons and subsequent axonopathy. TRIM2 is also involved in regulating axon outgrowth during development; it contains RING and BBOX domains, the NHL repeat domain is located at its C-terminus. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures
DLIFRIGTKGRNKGEFTNLQGVAASSSGRLVIADSNNQCVQVFSNDGQFKLRFGVRGRSPGQLQRPTGVA
VTLNGDIIIADYDNKWVSIFSPDGKFKSKIGAGKLMGPKGVAVDRNGHIIVVDNKACCVFIFQPNGKLVT
RFGSRGNGDRQFAGPHFAAVNNNNEIIVTDFHNHSVKVFNAEGEFLFKFGSNGEGNGQFNAPTGVAVDSN
GNIIVADWGNSRIQVFDSSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ
>gnl|CDD|271331 cd14961, NHL_TRIM32_like, NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins. The E3 ubiquitin-protein ligase TRIM32 (HT2A) is widely expressed and is responsible for ubiquinating a large variety of targets, including dysbindin (DTNBP1), NPHP7/Glis2, TAp73, and others. TRIM32 promotes disassociation of the plakoglobin-PI3K complex and reduces PI3K-Akt-FoxO signaling. Mutations in TRIM32 have been implemented in the two diverse diseases limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11 (BBS11). The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures
GSFGGWPGTLNNPTGVAVTPTGRVVVADDGNKRIQVFDSDGNCLQQFGPKGDAGQDIRYPLDVAVTPDGH
IVVTDAGDRSVKVFSFDGRLKLFVRKSFSLPWGVAVNPSGEILVTDSEAGKLFVLTVDFKLGILKKGQKL
CSQLCRPRFVAVSRLGAVAVTEHLFANGTRSSSTRVKVFSSGGQLLGQIDSFGLNLVFPSLICASGVAFD
SEGNVIVADTGSGAILCLGKPEGFPILKPIVTQGLSRPVGLAVTPDGSLVVLDSGNHCVKIYK
>gnl|CDD|271332 cd14962, NHL_like_6, Uncharacterized NHL-repeat domain in bacterial proteins. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures
VTGEERPKEALTRPYGVAADGRGRIYVADTGRGAVFVFDLPNGKVFVIGNAGPNRFVSPIGVAIDANGNL
YVSDAELGKVFVFDRDGKFLRAIGAGALFKRPTGIAVDPAGKRLYVVDTLAHKVKVFDLDGRLLFDIGKR
GSGPGEFNLPTDLAVDRDGNLYVTDTMNFRVQIFDADGKFLRSFGERGDGPGSFARPKGIAVDSEGNIYV
VDAAFDNVQIFNPEGELLLTVGGPGSGPGEFYLPSGIAIDKDDRIYVVDQFNRRIQVFQYL
>gnl|CDD|271333 cd14963, NHL_like_5, Uncharacterized NHL-repeat domain in bacterial proteins. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures
IYGPFGDPLNKPMGVAVSDGRIYVADTNNHRVQVFDYEGKFKKSFGGPGTGPGEFKYPYGIAVDSDGNIY
VADLYNGRIQVFDPDGKFLKYFPEKKDRVKLISPAGLAIDDGKLYVSDVKKHKVIVFDLEGKLLLEFGKP
GSEPGELSYPNGIAVDEDGNIYVADSGNGRIQVFDKNGKFIKELNGSPDGKSGFVNPRGIAVDPDGNLYV
VDNLSHRVYVFDEQGKELFTFGGRGKDDGQFNLPNGLFIDDDGRLYVTDRENNRVAVY
>gnl|CDD|410628 cd14964, 7tm_GPCRs, seven-transmembrane G protein-coupled receptor superfamily. This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections
TTIILSLLTCLGLLGNLLVLLSLVRLRKRPRSTRLLLASLAACDLLASLVVLVLFFLLGLTEASSRPQAL
CYLIYLLWYGANLASIWTTLVLTYHRYFALCGPLKYTRLSSPGKTRVIILGCWGVSLLLSIPPLVGKGAI
PRYNTLTGSCYLICTTIYLTWGFLLVSFLLPLVAFLVIFSRIVLRLRRRVRAIRSAASLNTDKNLKATKS
LLILVITFLLCWLPFSIVFILHALVAAGQGLNLLSILANLLAVLASTLNPFIYCLGN
>gnl|CDD|410629 cd14965, 7tm_Opsins_type1, type 1 opsins, member of the seven-transmembrane GPCR superfamily. This group represents the microbial rhodopsin family, also known as type 1 rhodopsins, which can function as light-dependent ion pumps, cation channels, and sensors. They have been found in various single-celled microorganisms from all three domains of life, including halophile archaea, gamma-proteobacteria, cyanobacteria, fungi, and green algae. Members of the type I rhodopsin family include: light-driven inward chloride pump halorhodopsin (HR); light-driven outward proton pump bacteriorhodopsin (BR); light-gated cation channel channelrhodopsin (ChR); light-sensor activating transmembrane transducer proteins, sensory rhodopsin I and II (SRI and II); light-sensor activating soluble transducer protein Anabaena sensory rhodopsin (ASR); and other light-driven proton pumps such as blue-light-absorbing and green-light absorbing proteorhodopsins, among others. While microbial (type 1) and animal (type 2) rhodopsins have no sequence similarity with each other, they share a common architecture consisting of seven-transmembrane alpha-helices (TM) connected by extracellular loops and intracellular loops. Both types of rhodopsins consist of opsin and a covalently attached retinal (the aldehyde of vitamin A), a photoreactive chromophore, via a protonated Schiff base linkage to an amino group of lysine in the middle of the seventh transmembrane helix (TM7). Upon the absorption of light, microbial rhodopsins undergo light-induced photoisomerization of all-trans retinal into the 13-cis isomer, whereas the photoisomerization of 11-cis retinal to all-trans isomer occurs in the animal rhodopsins. While animal visual rhodopsins are activated by light to catalyze GDP/GTP exchange in the alpha subunit of the retinal G protein transducin (Gt), microbial rhodopsins do not activate G proteins
GVIFLWIGFAIMALGTLIFLVLTFSAPVEARKFYYIATLICGIAAIAYFAMASGQGWTAVSGCRQIFYAR
YIDWLLTTPLILLDLGLLAGADRATILALIGADVIMIVTGLIGALSIVTTVKWLWFLIGLCAFIVVLYGL
AKNYREAAKAKSPEVASLYTKLAWLTIVLWIAYPIVWIFGEGGAVLSVSFETLLYTILDLFSKVGFGFIL
LSAH
>gnl|CDD|320097 cd14966, 7tmD_STE3, fungal a-factor pheromone receptor STE3, member of the class D family of seven-transmembrane G protein-coupled receptors. This subfamily represents the a-factor pheromone receptor encoded by the STE3 gene, which is required for pheromone sensing and mating in haploid cells of the yeast Saccharomyces cerevisiae. The STE3-encoded seven-transmembrane domain receptor is a member of the class D GPCRs. Class D receptors are composed of two major subfamilies: Ste2 and Ste3. These two GPCRs (Ste2 and Ste3) sense the polypeptide mating pheromones, alpha-factor and a-factor, which activate a G protein-coupled receptors on the surface of the opposite yeast-mating haploid-types (MATa and MAT-alpha), respectively. Activation of these receptors by pheromones leads to activation of the mitogen-activated protein kinase (MAPK) signal transduction cascades, G1 cell cycle arrest, and polarized cell growth in the direction of the partner cell (a process called shmooing), which ultimately induces cell-cell fusion and the formation of a diploid zygote. Like all GPCRs, these pheromone mating factor receptors possess the same basic architecture of seven-transmembrane (7TM) domains and share common signaling mechanisms; however, there is no significant sequence similarity either between Ste2 and Ste3, or between these two receptors and the other 7TM GPCRs. Thus, STE2 and STE3 represent phylogenetically distinct groups
IAFPIFSFLAFILVIPPLPWHLRARNVGACLLIFWLFLLNLINFVNAIIWPGDDINRAPDKVWCDISTKL
IIGASVGIPAASLCINRRLYRIASTRRVTLTRADKRRRIIIDLLICLGLPILVMALHYIVQGHRYDIFED
VGCYPAIYNSWPALVLVYIWPLIISLIAAVYAVLTLRRFFRRRKQFRDLLSSSNSGLTTSRFLRLMALAL
VEILITLPLSIYVLVLGSLELDRWIPVASAFLFFAFFGFGSEARKMYRR
>gnl|CDD|320098 cd14967, 7tmA_amine_R-like, amine receptors and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. Amine receptors of the class A family of GPCRs include adrenoceptors, 5-HT (serotonin) receptors, muscarinic cholinergic receptors, dopamine receptors, histamine receptors, and trace amine receptors. The receptors of amine subfamily are major therapeutic targets for the treatment of neurological disorders and psychiatric diseases. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
LLAVFLSLIILVTVFGNLLVILAVYRNRRLRTVTNYFIVSLAVADLLVALLVMPFSAVYTLLGYWPFGPV
LCRFWIALDVLCCTASILNLCAISLDRYLAITRPLRYRQLMTKKRALIMIAAVWVYSLLISLPPLVGWRD
ETQPSVVDCECEFTPNKIYVLVSSVISFFIPLLIMIVLYARIFRVARRELKAAKTLAIIVGAFLLCWLPF
FIIYLVSAFCPPDCVPPILYAVFFWLGYLNSALNPIIYALFNRDFRRAF
>gnl|CDD|341316 cd14968, 7tmA_Adenosine_R, adenosine receptor subfamily, member of the class A family of seven-transmembrane G protein-coupled receptors. The adenosine receptors (or P1 receptors), a family of G protein-coupled purinergic receptors, bind adenosine as their endogenous ligand. There are four types of adenosine receptors in human, designated as A1, A2A, A2B, and A3. Each type is encoded by a different gene and has distinct functions with some overlap. For example, both A1 and A2A receptors are involved in regulating myocardial oxygen consumption and coronary blood flow in the heart, while the A2A receptor also has a broad spectrum of anti-inflammatory effects in the body. These two receptors also expressed in the brain, where they have important roles in the release of other neurotransmitters such as dopamine and glutamate, while the A2B and A3 receptors found primarily in the periphery and play important roles in inflammation and immune responses. The A1 and A3 receptors preferentially interact with G proteins of the G(i/o) family, thereby lowering the intracellular cAMP levels, whereas the A2A and A2B receptors interact with G proteins of the G(s) family, activating adenylate cyclase to elevate cAMP levels
AVYIVLEVLIAVLSVLGNVLVIWAVKLNRALRTVTNYFIVSLAVADILVGALAIPLAILISLGLPTNFHG
CLFMACLVLVLTQSSIFSLLAIAIDRYLAIKIPLRYKSLVTGRRAWGAIAVCWVLSFLVGLTPMFGWNNG
APLESGCGEGGIQCLFEEVIPMDYMVYFNFFACVLVPLLIMLVIYLRIFRVIRKQLRQIESLLRSRRSRS
TLQKEVKAAKSLAIILFLFALCWLPLHIINCITLFCPECKVPKILTYIAILLSHANSAVNPIVYAYRIRK
FRQTF
>gnl|CDD|381741 cd14969, 7tmA_Opsins_type2_animals, type 2 opsins in animals, member of the class A family of seven-transmembrane G protein-coupled receptors. This rhodopsin family represents the type 2 opsins found in vertebrates and invertebrates except sponge. Type 2 opsins primarily function as G protein coupled receptors and are responsible for vision as well as for circadian rhythm and pigment regulation. On the contrary, type 1 opsins such as bacteriorhodopsin and proteorhodopsin are found in both prokaryotic and eukaryotic microbes, functioning as light-gated ion channels, proton pumps, sensory receptors and in other unknown functions. Although these two opsin types share seven-transmembrane domain topology and a conserved lysine reside in the seventh helix, type 1 opsins do not activate G-proteins and are not evolutionarily related to type 2. Type 2 opsins can be classified into six distinct subfamilies including the vertebrate opsins/encephalopsins, the G(o) opsins, the G(s) opsins, the invertebrate G(q) opsins, the photoisomerases, and the neuropsins
YVLAVYLSLIGVLGVVLNGLVIIVFLKKKKLRTPLNLFLLNLALADLLMSVVGYPLSFYSNLSGRWSFGD
PGCVIYGFAVTFLGLVSISTLAALAFERYLVIVRPLKAFRLSKRRALILIAFIWLYGLFWALPPLFGWSS
YVPEGGGTSCSVDWYSKDPNSLSYIVSLFVFCFFLPLAIIIFCYYKIYRTLRKMSKRAARRKNSAITKRT
KKAEKKVAKMVLVMIVAFLIAWTPYAVVSLYVSFGGESTIPPLLATIPALFAKSSTIYNPIIYVFMNKQF
RRAL
>gnl|CDD|320101 cd14970, 7tmA_Opioid_R-like, opioid receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes opioid receptors, somatostatin receptors, melanin-concentrating hormone receptors (MCHRs), and neuropeptides B/W receptors. Together they constitute the opioid receptor-like family, members of the class A G-protein coupled receptors. Opioid receptors are coupled to inhibitory G proteins of the G(i/o) family and are involved in regulating a variety of physiological functions such as pain, addiction, mood, stress, epileptic seizure, and obesity, among many others. G protein-coupled somatostatin receptors (SSTRs), which display strong sequence similarity with opioid receptors, binds somatostatin (somatotropin release inhibiting factor), a polypeptide hormone that regulates a wide variety of physiological functions such as neurotransmission, cell proliferation, contractility of smooth muscle cells, and endocrine signaling as well as inhibition of the release of many secondary hormones. MCHR binds melanin concentrating hormone and is presumably involved in the neuronal regulation of food intake. Despite strong homology with somatostatin receptors, MCHR does not appear to bind somatostatin. Neuropeptides B/W receptors are primarily expressed in the CNS and stimulate the cortisol secretion by activating the adenylate cyclase- and the phospholipase C-dependent signaling pathways
IVIPAVYSVVCVVGLTGNSLVIYVILRYSKMKTVTNIYILNLAVADELFLLGLPFLATSYLLGYWPFGEV
MCKIVLSVDAYNMFTSIFCLTVMSVDRYLAVVHPVKSLRFRTPRKAKLVSLCVWALSLVLGLPVIIFART
LQEEGGTISCNLQWPDPPDYWGRVFTIYTFVLGFAVPLLVITVCYSLIIRRLRSSRNLSTSGAREKRRAR
RKVTRLVLVVVAVFVVCWLPFHVFQIVRLLIDPPETLTVVGVFLFCIALSYANSCLNPILYAFLDENFRK
SF
>gnl|CDD|320102 cd14971, 7tmA_Galanin_R-like, galanin receptor and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This subfamily includes G-protein coupled galanin receptors, kisspeptin receptor and allatostatin-A receptor (AstA-R) in insects. These receptors, which are members of the class A of seven transmembrane GPCRs, share a high degree of sequence homology among themselves. The galanin receptors bind galanin, a neuropeptide that is widely expressed in the brain, peripheral tissues, and endocrine glands. Galanin is implicated in numerous neurological and psychiatric diseases including Alzheimer's disease, eating disorders, and epilepsy, among many others. KiSS1-derived peptide receptor (also known as GPR54 or kisspeptin receptor) binds the peptide hormone kisspeptin (metastin), which encoded by the metastasis suppressor gene (KISS1) expressed in various endocrine and reproductive tissues. AstA-R is a G-protein coupled receptor that binds allatostatin A. Three distinct types of allatostatin have been identified in the insects and crustaceans: AstA, AstB, and AstC. They both inhibit the biosynthesis of juvenile hormone and exert an inhibitory influence on food intake. Therefore, allatostatins are considered as potential targets for insect control
WIVPLFFALIFLLGLVGNSLVILVVARNKPMRSTTNLFILNLAVADLTFLLFCVPFTATIYPLPGWVFGD
FMCKFVHYFQQVSMHASIFTLVAMSLDRFLAVVYPLRSLHIRTPRNALAASGCIWVVSLAVAAPVLALHR
LRNYTPGNRTVCSEAWPSRAHRRAFALCTFLFGYLLPLLLICVCYAAMLRHLWRVAVRPVLSEGSRRAKR
KVTRLVLVVVVLFAACWGPIHAILLLVALGPFPLTYATYALRIWAHCLAYSNSAVNPVLYAFLSEHFRKA
F
>gnl|CDD|341317 cd14972, 7tmA_EDG-like, endothelial differentiation gene family, member of the class A family of seven-transmembrane G protein-coupled receptors. This group represents the endothelial differentiation gene (Edg) family of G-protein coupled receptors, melanocortin/ACTH receptors, and cannabinoid receptors as well as their closely related receptors. The Edg GPCRs bind blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). Melanocortin receptors bind a group of pituitary peptide hormones known as melanocortins, which include adrenocorticotropic hormone (ACTH) and the different isoforms of melanocyte-stimulating hormones. Two types of cannabinoid receptors, CB1 and CB2, are activated by naturally occurring endocannabinoids, cannabis plant-derived cannabinoids such as tetrahydrocannabinol, or synthetic cannabinoids. The CB receptors are involved in the various physiological processes such as appetite, mood, memory, and pain sensation. CB1 receptor is expressed predominantly in central and peripheral neurons, while CB2 receptor is found mainly in the immune system
VLVVAIVLGVFIVVENSLVLAAIIKNRRLHKPMYILIANLAAADLLAGIAFVFTFLSVLLVSLTPSPATW
LLRKGSLVLSLLASAYSLLAIAVDRYISIVHGLTYVNNVTNKRVKVLIALVWVWSVLLALLPVLGWNCVL
CDQESCSPLGPGLPKSYLVLILVFFFIALVIIVFLYVRIFWCLWRHANAIAARQEAAVPAQPSTSRKLAK
TVVIVLGVFLVCWLPLLILLVLDVLCPSVCDIQAVFYYFLVLALLNSAINPIIYAFRLKEMRRAV
>gnl|CDD|320104 cd14973, 7tmA_Mrgpr, mas-related G protein-coupled receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. The Mas-related G-protein coupled receptor (Mrgpr) family constitutes a group of orphan receptors exclusively expressed in nociceptive primary sensory neurons and mast cells in the skin. Members of the Mrgpr family have been implicated in the modulation of nociception, pruritus (itching), and mast cell degranulation. The Mrgpr family in rodents and humans contains more than 50 members that can be grouped into 9 distinct subfamilies: MrgprA, B, C (MrgprX1), D, E, F, G, H (GPR90), and the primate-specific MrgprX subfamily. Some Mrgprs can be activated by endogenous ligands such as beta-alanine, adenine (a cell metabolite and potential transmitter), RF-amide related peptides, or salusin-beta (a bioactive peptide). However, the effects of these agonists are not clearly understood, and the physiological role of the individual receptor family members remains to be determined. Also included in this family is Mas-related G-protein coupled receptor 1-like (MAS1L) which is only found in primates. The angiotensin-II metabolite angiotensin is an endogenous ligand for MAS1L
LVIFSLTVLLSLCGLVGNGLVLWLLGFRIKRNPFSVYILNLAAADFLFLSCQAIQSLEDLLGGSLPGFAL
CRLLATLMFFSYTVGLSLLAAISTERCLSVLFPIWYRCHRPKHLSAVVCALLWALSLLLSVLESYFCGFL
FWKFNESACRTFNFLSALLFLLLFLVMCVSSLTLLIRVQCSSQRRPPTRLYVVILLTVLVFLLCGLPLGI
YWFLLLWFSNYLFHTFHPISDLLSCVNSSANPIIYFFVGSLRGRRLREPLRVVLQRALRDEP
>gnl|CDD|320105 cd14974, 7tmA_Anaphylatoxin_R-like, anaphylatoxin receptors and related G protein-coupled chemokine receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. This subfamily of G-protein coupled receptors includes anaphylatoxin receptors, formyl peptide receptors (FPR), prostaglandin D2 receptor 2, GPR1, and related chemokine receptors. The anaphylatoxin receptors are a group of G-protein coupled receptors that bind anaphylatoxins. The members of this group include C3a and C5a receptors. The formyl peptide receptors (FPRs) are chemoattractant GPCRs that involved in mediating immune responses to infection. They are expressed mainly on polymorphonuclear and mononuclear phagocytes and bind N-formyl-methionyl peptides (FMLP), which are derived from the mitochondrial proteins of ruptured host cells or invading pathogens. Chemokine receptor-like 1 (also known as chemerin receptor 23) is a GPCR for the chemoattractant adipokine chemerin, also known as retinoic acid receptor responder protein 2 (RARRES2), and for the omega-3 fatty acid derived molecule resolvin E1. Interaction with chemerin induces activation of the MAPK and PI3K signaling pathways leading to downstream functional effects, such as a decrease in immune responses, stimulation of adipogenesis, and angiogenesis. On the other hand, resolvin E1 negatively regulates the cytokine production in macrophages by reducing the activation of MAPK1/3 and NF-kB pathways. Prostaglandin D2 receptor, also known as CRTH2, is a chemoattractant G-protein coupled receptor expressed on T helper type 2 cells that binds prostaglandin D2 (PGD2). PGD2 functions as a mast cell-derived mediator to trigger asthmatic responses and also causes vasodilation. PGD2 exerts its inflammatory effects by binding to two G-protein coupled receptors, the D-type prostanoid receptor (DP) and PD2R2 (CRTH2). PD2R2 couples to the G protein G(i/o) type which leads to a reduction in intracellular cAMP levels and an increase in intracellular calcium. GPR1 is an orphan receptor that can be activated by the leukocyte chemoattractant chemerin, thereby suggesting that some of the anti-inflammatory actions of chemerin may be mediated through GPR1
IVSLVLYALIFLLGLPGNGLVIWVAGFKMKRTVNTVWFLNLALADFLFCLFLPFLIVYIAMGHHWPFGSV
LCKLNSFVISLNMFASVFLLTAISLDRCLLVLHPVWAQNHRTVRLASVVCVGIWILALVLSVPYFVFRDT
VTHHNGRSCNLTCVEDYDLRRSRHKALTVIRFLCGFLLPLLIIAICYSVIAVKLRRKRLAKSSKPLRVLL
AVVVAFFLCWLPYHVFALLELVAAAGLPEVVLLGLPLATGLAYFNSCLNPILYVFMGQDFRKRL
>gnl|CDD|320106 cd14975, 7tmA_LTB4R, leukotriene B4 receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Leukotriene B4 (LTB4), a metabolite of arachidonic acid, is a powerful chemotactic activator for granulocytes and macrophages. Two receptors for LTB4 have been identified: a high-affinity receptor (LTB4R1 or BLT1) and a low-affinity receptor (TB4R2 or BLT2). Both BLT1 and BLT2 receptors belong to the rhodopsin-like G-protein coupled receptor superfamily and primarily couple to G(i) proteins, which lead to chemotaxis, calcium mobilization, and inhibition of adenylate cyclase. In some cells, they can also couple to the G(q)-like protein, G16, and activate phospholipase C. LTB4 is involved in mediating inflammatory processes, immune responses, and host defense against infection. Studies have shown that LTB4 stimulates leukocyte extravasation, neutrophil degranulation, lysozyme release, and reactive oxygen species generation
VLGCTLLSLAFAIGLPGNSFVIWSILIKVKQRSVTMLLVLNLALADLAVLLTLPVWIYFLATGTWDFGLA
ACKGCVYVCAVSMYASVFLITLMSLERFLAVSRPFVSQGWRAKALAHKVLAIIWLLAVLLATPVIAFRHV
EETVENGMCKYRHYSDGQLVFHLLLETVVGFAVPFTAVVLCYSCLLRRLRRRRFRRRRRTGRLIASVVVA
FAACWLPYHVGNLLEVVSELIGGSKMAGTLGKVAEAGRPIAGALAFLSSSINPLLYAFAARGLFRSAG
>gnl|CDD|320107 cd14976, 7tmA_RNL3R, relaxin-3 like peptide receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. This G protein-coupled receptor subfamily is composed of the relaxin-3 like peptide receptors, RNL3R1 and RNL3R2, and similar proteins. The relaxin-3 like peptide family includes relaxin-1, -2, -3, as well as insulin-like (INSL) peptides 3 to 6. RNL3/relaxin-3 and INSL5 are the endogenous ligands for RNL3R1 and RNL3R2, respectively. RNL3R1, also called GPCR135 or RXFP3, is predominantly expressed in the brain and is implicated in stress, anxiety, feeding, and metabolism. Insulin-like peptide 5 (INSL5), the endogenous ligand for RNL3R2 (also called GPCR142 or RXFP4), plays a role in fat and glucose metabolism. INSL5 is highly expressed in human rectal and colon tissues. Both RNL3R1 and RNL3R2 signal through G(i) protein and inhibit adenylate cyclase, thereby inhibit cAMP accumulation. RNL3R1 is shown to activate Erk1/2 signaling pathway
NLVSVVYMVVFTVGLLGNLLVLYLLKSNKKLRQQSESNKFVFNLALTDLIFVLTLPFWAVEYALDFVWPF
GTAMCKVVRYVTKLNMYSSIFFLTALSVTRYIAVARALKHGWIRKAFGAFATTIAIWAAAALAAIPEAIF
STDTWSSVNHTLCLLRFPKNSSVTRWYNWLGMYQLQKVVLGFFLPLGIITLSYLLLLRFLQRKRGGSKRR
KSRVTKSVFIVVLSFFICWLPNQALSLWSALIKFDDVPFSDAFFAFQTYAFPVAICLAHSNSCLNPVLYC
LVRREFRDAL
>gnl|CDD|320108 cd14977, 7tmA_ET_R-like, endothelin receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This subfamily of G-protein coupled receptors includes endothelin receptors, bombesin receptor subtype 3 (BRS-3), gastrin-releasing peptide receptor (GRPR), neuromedin B receptor (NMB-R), endothelin B receptor-like 2 (ETBR-LP-2), and GRP37. The endothelin receptors and related proteins are members of the seven transmembrane rhodopsin-like G-protein coupled receptor family (class A GPCRs) which activate multiple effectors via different types of G protein
YVIMSLSLVIFAVGIIGNLMVLCIVCTNYYMRSVPNILIASLALGDLLLLLLCVPLNAYNLLTKDWLFGD
VMCKLVPFIQVTSLGVTVFSLCALSIDRYRAAVNSMPMQTIGACLSTCVKLAVIWVGSVLLAVPEAVLST
VARESSLDNSSLTVCIMKPSTPFAETYPKARSWWLFGCYFCLPLAFTAVCYLLMARTLIRAAKEYTRGTK
KHMKQRRQLAKTVLCLVLVFAFCWLPEHISNILRATLYNEVLIDTRSTLDILDLIGQFLSFFNSCVNPIA
LYLLSEPFRRAF
>gnl|CDD|410630 cd14978, 7tmA_FMRFamide_R-like, FMRFamide (Phe-Met-Arg-Phe) receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes Drosophila melanogaster G-protein coupled FMRFamide (Phe-Met-Arg-Phe-NH2) receptor DrmFMRFa-R and related invertebrate receptors, as well as the vertebrate proteins GPR139 and GPR142. DrmFMRFa-R binds with high affinity to FMRFamide and intrinsic FMRFamide-related peptides. FMRFamide is a neuropeptide from the family of FMRFamide-related peptides (FaRPs), which all containing a C-terminal RFamide (Arg-Phe-NH2) motif and have diverse functions in the central and peripheral nervous systems. FMRFamide is an important neuropeptide in many types of invertebrates such as insects, nematodes, molluscs, and worms. In invertebrates, the FMRFamide-related peptides are involved in the regulation of heart rate, blood pressure, gut motility, feeding behavior, and reproduction. On the other hand, in vertebrates such as mice, they play a role in the modulation of morphine-induced antinociception. Orphan receptors GPR139 and GPR142 are very closely related G protein-coupled receptors, but they have different expression patterns in the brain and in other tissues. These receptors couple to inhibitory G proteins and activate phospholipase C. Studies suggested that dimer formation may be required for their proper function. GPR142 is predominantly expressed in pancreatic beta-cells and mediates enhancement of glucose-stimulated insulin secretion, whereas GPR139 is mostly expressed in the brain and is suggested to play a role in the control of locomotor activity. Tryptophan and phenylalanine have been identified as putative endogenous ligands of GPR139
VLYGYVLPVICIFGIIGNILNLVVLTRKSMRSSTNVYLAALAVSDILVLLSALPLFLLPYIADYSSSFLS
YFYAYFLPYIYPLANTFQTASVWLTVALTVERYIAVCHPLKARTWCTPRRARRVILIIIIFSLLLNLPRF
FEYEVVECENCNNNSYYYVIPTLLRQNETYLLKYYFWLYAIFVVLLPFILLLILNILLIRALRKSKKRRR
LLRRRRRLLSRSQRRERRTTIMLIAVVIVFLICNLPAGILNILEAIFGESFLSPIYQLLGDISNLLVVLN
SAVNFIIYCLFSSKFRRTF
>gnl|CDD|320110 cd14979, 7tmA_NTSR-like, neurotensin receptors and related G protein-coupled receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. This subfamily includes the neurotensin receptors and related G-protein coupled receptors, including neuromedin U receptors, growth hormone secretagogue receptor, motilin receptor, the putative GPR39 and the capa receptors from insects. These receptors all bind peptide hormones with diverse physiological effects. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VLVTAIYVAIFVVGIVGNLLTCIVIARHKSLRTTTNYYLFSLAVSDLLILLVGLPVELYNFWWQYPWAFG
DGGCKLYYFLFEACTYATVLTIVALSVERYVAICHPLKAKTLVTKRRVKRFILAIWLVSILCAIPILFLM
GIQYLNGPLPGPVPDSAVCTLVVDRSTFKYVFQVSTFIFFVLPMFVISILYFRIGVKLRSMRNIKKGTRA
QGTRNVELSLSQQARRQVVKMLGAVVIAFFVCWLPFHAQRLMFSYASKEDTFLFDFYQYLYPISGILFYL
SSAINPILYNLMSSRFRVAF
>gnl|CDD|320111 cd14980, 7tmA_Glycoprotein_LRR_R-like, glycoprotein hormone receptors and leucine-rich repeats containing G protein-coupled receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. This subfamily includes the glycoprotein hormone receptors (GPHRs), vertebrate receptors containing 17 leucine-rich repeats (LGR4-6), and the relaxin family peptide receptors (also known as LGR7 and LGR8). They are seven transmembrane domain receptors with a very large extracellular N-terminal domain containing many leucine-rich repeats responsible for hormone recognition and binding. The glycoprotein hormone receptor family contains receptors for the pituitary hormones, thyrotropin (thyroid-stimulating hormone receptor), follitropin (follicle-stimulating hormone receptor), and lutropin (luteinizing hormone receptor). Glycoprotein hormone receptors couple primarily to the G(s)-protein and promotes cAMP production, but also to the G(i)- or G(q)-protein. Two orphan GPCRs, LGR7 and LGR8, have been recently identified as receptors for the relaxin peptide hormones
ISLRIFIWIIGILALIGNILVIIWHISSKKKKKKVPKLLIINLAIADFLMGIYLLIIAIADQYYRGRYAQ
YSEEWLRSPPCLLACFLVSLSSLMSVLMMLLITLDRYICIVYPFSNKRLSYKSAKIILILGWLFSIIFAA
IPILYSINQPGDNRLYGYSSICMPSNVSNPYYRGWLIAYLLLTFIAWIIICILYILIFISVRKSRKSARR
SSSKRDKRIAIRLALILITDLICWLPYYIVIFSGLLTSTEIDIHVLQFIAILALPLNSAINPYLYTLTTP
TFKRDF
>gnl|CDD|320112 cd14981, 7tmA_Prostanoid_R, G protein-coupled receptors for prostanoids, member of the class A family of seven-transmembrane G protein-coupled receptors. Prostanoids are the cyclooxygenase (COX) metabolites of arachidonic acid, which include the prostaglandins (PGD2, PGE2, PGF2alpha), prostacyclin (PGI2), and thromboxane A2 (TxA2). These five major bioactive prostanoids acts as mediators or modulators in a wide range of physiological and pathophysiological processes within the kidney and play important roles in inflammation, platelet aggregation, and vasoconstriction/relaxation, among many others. They act locally by preferentially interacting with G protein-coupled receptors designated DP, EP. FP, IP, and TP, respectively. The phylogenetic tree suggests that the prostanoid receptors can be grouped into two major branches: G(s)-coupled (DP1, EP2, EP4, and IP) and G(i)- (EP3) or G(q)-coupled (EP1, FP, and TP), forming three clusters
GESPAPPALMFVFGVLGNLLALIVLARSSKSHKWSVFYRLVAGLAITDLLGILLTSPVVLAVYASNFEWD
GGQPLCDYFGFMMSFFGLSSLLIVCAMAVERFLAITHPFFYNSHVKKRRARLMLGAVWAFALLIASLPLL
GLGSYVLQYPGTWCFLDFYSKNTGDAAYAYLYSILGLLILLVTLLCNLLVIITLLRMRRRKKRHRRSRRS
ARRQKRNEIQMVVLLLAITVVFSVCWLPLMIRVLINATGDSEKNGKTDLLAVRMASWNQILDPWVYILLR
KEVLRRLY
>gnl|CDD|341318 cd14982, 7tmA_purinoceptor-like, purinoceptor and its related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. Members of this subfamily include lysophosphatidic acid receptor, P2 purinoceptor, protease-activated receptor, platelet-activating factor receptor, Epstein-Barr virus induced gene 2, proton-sensing G protein-coupled receptors, GPR35, and GPR55, among others. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
TLFPIVYSLIFILGLLGNILALWVFLRKMKKRSPTTIYMINLALADLLFVLTLPFRIYYYLNGGWWPFGD
FLCRLTGLLFYINMYGSILFLTCISVDRYLAVVHPLKSRRLRRKRYAVGVCAGVWILVLVASVPLLLLRS
TIAKENNSTTCFEFLSEWLASAAPIVLIALVVGFLIPLLIILVCYSLIIRALRRRSKQSQKSVRKRKALR
MILIVLAVFLVCFLPYHVTRILYLLVRLSFIADCSARNSLYKAYRITLCLASLNSCLDPLIYYFLSKTFR
KRL
>gnl|CDD|320114 cd14983, 7tmA_FFAR, free fatty acid receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. This subfamily includes the free fatty acid receptors (FFARs) which bind free fatty acids (FFAs). They belong to the class A G-protein coupled receptors and are composed of three members, each encoded by a separate gene (FFAR1, FFAR2, and FFAR3). These genes and a fourth pseudogene, GPR42, are localized together on chromosome 19. FFAR1 is a receptor for medium- and long-chain FFAs, whereas FFAR2 and FFAR3 are receptors for short chain FFAs (SCFAs), which have different ligand affinities. FFAR1 directly mediates FFA stimulation of glucose-stimulated insulin secretion and also indirectly increases insulin secretion by enhancing the release of incretin. FFAR2 activation by SCFA suppresses adipose insulin signaling, which leads to the inhibition of fat accumulation in adipose tissue. FAAR3 is expressed in intestinal L cells, which produces glucagon-like peptide 1 (GLP-1) and peptide YY (PYY), suggesting that this receptor may be involved in energy homeostasis. FFARs are considered important components of the body's nutrient sensing mechanism, and therefore, these receptors are potential therapeutic targets for the treatment of metabolic disorders, such as type 2 diabetes and obesity
QLSLMVYVLTILLGLPSNLLALYAFVNRARLRLTPNVIYMINLCLSDLVFILSLPIKIVEALSSAWTLPA
VLCPLYNLAHFSTLYASTCFLTAISAGRYLGVAFPIKYQLYKKPLYSCLVCVAIWALVIFHVTLVFILET
SGGTLDINTPVGNSSTCYENFTPEQLALLAPVRLELSLVLFFLPLAITAFCYVRCIRILVRSRLHERRKR
RAVRVAVSTLLTFVVCFGPYNISHVVGFVRHESVWWRKLALLTSTCNAFLDPLIFYFLSSSMERGFVH
>gnl|CDD|341319 cd14984, 7tmA_Chemokine_R, classical and atypical chemokine receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines. In addition to these classical chemokine receptors, there exists a subfamily of atypical chemokine receptors (ACKRs) that are unable to couple to G-proteins and, instead, they preferentially mediate beta-arrestin dependent processes, such as receptor internalization, after ligand binding. The classical chemokine receptors contain a conserved DRYLAIV motif in the second intracellular loop, which is required for G-protein coupling. However, the ACKRs lack this conserved motif and fail to couple to G-proteins and induce classical GPCR signaling. Five receptors have been identified for the ACKR family, including CC-chemokine receptors like 1 and 2 (CCRL1 and CCRL2), CXCR7, Duffy antigen receptor for chemokine (DARC), and D6. Both ACKR1 (DARC) and ACKR3 (CXCR7) show low sequence homology to the classic chemokine receptors
VFLPVLYSLVFLLGLVGNSLVLLVLLYYRKLRSMTDVYLLNLALADLLFVLTLPFWAVYAADGWVFGSFL
CKLVSALYTINFYSGILFLACISIDRYLAIVHAVSALRARTLLHGKLTCLGVWALALLLSLPEFIFSQVS
EENGSSICSYDYPEDTATTWKTLLRLLQNILGFLLPLLVMLFCYSRIIRTLLRARNHKKHRALRVIFAVV
VVFFLCWLPYNIVLLLDTLQLLGIISRSCELSKSLDYALQVTESLAFSHCCLNPVLYAFVGVKFRKYL
>gnl|CDD|341320 cd14985, 7tmA_Angiotensin_R-like, angiotesin receptor family and its related G protein-coupled receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes the angiotensin receptors, the bradykinin receptors, apelin receptor as well as putative G-protein coupled receptors (GPR15 and GPR25). Angiotensin II (Ang II), the main effector in the renin-angiotensin system, plays a crucial role in the regulation of cardiovascular homeostasis through its type 1 (AT1) and type 2 (AT2) receptors. Ang II contributes to cardiovascular diseases such as hypertension and atherosclerosis via AT1R activation. Ang II increases blood pressure through Gq-mediated activation of phospholipase C, resulting in phosphoinositide (PI) hydrolysis and increased intracellular calcium levels. Through the AT2 receptor, Ang II counteracts the vasoconstrictor action of AT1R and thereby induces vasodilation, sodium excretion, and reduction of blood pressure. Bradykinins (BK) are pro-inflammatory peptides that mediate various vascular and pain responses to tissue injury through its B1 and B2 receptors. Apelin (APJ) receptor binds the endogenous peptide ligands, apelin and Toddler/Elabela. APJ is an adipocyte-derived hormone that is ubiquitously expressed throughout the human body, and Toddler/Elabela is a short secretory peptide that is required for normal cardiac development in zebrafish. Activation of APJ receptor plays key roles in diverse physiological processes including vasoconstriction and vasodilation, cardiac muscle contractility, angiogenesis, and regulation of water balance and food intake. Orphan receptors, GPR15 and GPR25, share strong sequence homology to the angiotensin II type AT1 and AT2 receptors
VVIPALYIAIFLVGLLGNLFVVWVFLFPRGPKRVADIFIANLAAADLVFVLTLPLWATYTANQYDWPFGA
FLCKVSSYVISVNMFASIFLLTCMSVDRYLAIVHPVASRRLRRRRQARVTCALIWVVACLLSLPTFLLRS
LQAIENLNKTACIMLYPHEAWHFGLSLELNILGFVLPLLIILTCYFHIARSLRKRYERTGKNGRKRRKSL
KIIFALVVAFLVCWLPFHFFKFLDFLAQLGAIRPCFWELFLDLGLPIATCLAFTNSCLNPFIYVFVDRRF
RQKV
>gnl|CDD|320117 cd14986, 7tmA_Vasopressin-like, vasopressin receptors and its related G protein-coupled receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Members of this group form a subfamily within the class A G-protein coupled receptors (GPCRs), which includes the vasopressin and oxytocin receptors, the gonadotropin-releasing hormone receptors (GnRHRs), the neuropeptide S receptor (NPSR), and orphan GPR150. These receptors share significant sequence homology with each other, suggesting that they have a common evolutionary origin. Vasopressin, also known as arginine vasopressin or anti-diuretic hormone, is a neuropeptide synthesized in the hypothalamus. The actions of vasopressin are mediated by the interaction of this hormone with three tissue-specific subtypes: V1AR, V1BR, and V2R. Although vasopressin differs from oxytocin by only two amino acids, they have divergent physiological functions. Vasopressin is involved in regulating osmotic and cardiovascular homeostasis, whereas oxytocin plays an important role in the uterus during childbirth and in lactation. GnRHR, also known as luteinizing hormone releasing hormone receptor (LHRHR), plays an central role in vertebrate reproductive function; its activation by binding to GnRH leads to the release of follicle stimulating hormone (FSH) and luteinizing hormone (LH) from the pituitary gland. Neuropeptide S (NPS) promotes arousal and anxiolytic-like effects by activating its cognate receptor NPSR. NPSR has also been associated with asthma and allergy. GPR150 is an orphan receptor closely related to the oxytocin and vasopressin receptors
VSRVAVLGVLFVFTLVGNGLVILVLRRKRKKRSRVNIFILNLAIADLVVAFFTVLTQIIWEATGEWVAGD
VLCRIVKYLQVVGLFASTYILVSMSLDRYQAIVKPMSSLKPRKRARLMIVVAWVLSFLFSIPQLVIFVER
ELGDGVHQCWSSFYTPWQRKVYITWLATYVFVIPLIILSYCYGRILRTIWIRSRQKTDRPIAPTAMSCRS
VSCVSSRVSLISRAKIKTIKMTLVIILAFILCWTPYFIVQLLDVYAGMQQLENDAYVVSETLASLNSALN
PLIYGFFSSHLSFEH
>gnl|CDD|320118 cd14987, 7tmA_ACKR3_CXCR7, CXC chemokine receptor 7, member of the class A family of seven-transmembrane G protein-coupled receptors. ACKR3, also known as CXCR7, is an atypical chemokine receptor for CXCL12 and CXCR11. Unlike the classical chemokine receptors, ACKR3 contains a DRYLSIT-sequence instead of the conserved DRYLAIV motif in the second intracellular loop, which is required for G-protein coupling. Thus, ACKR3 does not activate classical GPCR signaling, instead induces beta-arrestin recruitment which is leading to ligand internalization and MAP-kinase activation. It is acting as a scavenger for CXCL12 and, to a lesser degree, for CXCL11. ACKR3 is highly expressed by blood vascular endothelial cells in brain, in numerous embryonic and neonatal tissues, in inflamed tissues and in a variety of cancers such as lymphomas, sarcomas, prostate and breast cancers, and gliomas. Five receptors have been identified for the ACKR family, including CC-Chemokine Receptors like 1 and 2 (CCRL1 and CCRL2), CXCR7, DARC, and D6. Both ACKR1 (DARC) and ACKR3 (CXCR7) show low sequence homology to the classic chemokine receptors
YTLSFFYIFIFVIGLLANSVVVWVNLQAKRTGYETHLYILNLAIADLCVVATLPVWVVSLVQHNQWPMGE
FTCKITHLIFSINLFGSIFFLTCMSVDRYLSVTLFGNTSSRRKKIVRRIICVLVWLLAFVASLPDTYFLK
TVTSPSNNETYCRSFYPEESFKEWLIGMELVSIVLGFVIPFPIIAVFYFLLARAISASSDQERKSSRKII
FSYVVVFLVCWLPYHTVVLLDILSFLHLIPFSCQLENFLYAALHVTQCFSLVHCCVNPILYSFINRNYRY
EL
>gnl|CDD|320119 cd14988, 7tmA_GPR182, G protein-coupled receptor 182, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR182 is an orphan G-protein coupled receptor that belongs to the class A of seven-transmembrane GPCR superfamily. When GPR182 gene was first cloned, it was proposed to encode an adrenomedullin receptor. However when the corresponding protein was expressed, it was found not to respond to adrenomedullin (ADM). All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VVLFILYLVIFVVGLVENVLVIWVNWHRWGSKNLVNLYILNMAIADLGVVLTLPVWMLEVMLDYTWLWGS
FLCKFTHYFYFANMYSSIFFLTCLSVDRYLTLTSSSPFWQQHQHRIRRALCAGIWVLSAIIPLPEVVHMQ
LLDGVEPMCLFLAPFETYDEWALAVSLLTLIIGFLIPFSIIAVFNVLTARYIRTAGRPESRRHCLLIYAY
ILVFVVCWLPYHVTLLLLTLHGSHISLHCNLVHFLYFFYDVIDCFSLLHCVANPILYNFLSKSFRGKL
>gnl|CDD|320120 cd14989, 7tmA_GPER1, G protein-coupled estrogen receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. G-protein coupled estrogen receptor 1 (GPER1), also known as the G-protein coupled receptor 30 (GPR30), is a high affinity receptor for estrogen. This receptor is a member of the class A of seven-transmembrane GPCRs. Estrogen binding results in intracellular calcium mobilization and synthesis of phosphatidylinositol (3,4,5)-trisphosphate in the nucleus. GPR30 plays an important role in development of tamoxifen resistance in breast cancer cells. The distribution of GPR30 is well established in the rodent, with high expression observed in the hypothalamus, pituitary gland, adrenal medulla, kidney medulla and developing follicles of the ovary. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
FLSCLYTIFLFPIGFIGNILILVVNLSFREKMTIPDLYFVNLAVADLILVADSLIEVFNLNEKYYDIAVL
CTFMSLFLQINMYSSIFFLTWMSFDRYIALAKVMKSSPLRTMQHARLSCGLIWMASISATLLPFTAVQAQ
HTGEVHFCFADVREIQWLEVTLGFIIPFSIIGLCYSLIVRVLVRAQKHRRLRPRRQKALRMILVVVLVFF
ICWLPENVFISIQLLQGTQEPSESYDESFRHNHPLTGHIVNLAAFSNSCLNPLIYSFLGETFRDKL
>gnl|CDD|320121 cd14990, 7tmA_GPR146, G protein-coupled receptor 146, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR146 is an orphan G-protein coupled receptor that belongs to the class A of seven-transmembrane GPCR superfamily. The endogenous ligand for GPR146 is not known. It has been suggested that GPR146 may be a part of the C-peptide signaling complex. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VLSLLYLIICFPVGLCYNALLVLVNLYNKASMTMPDVYFVNMAIAGLVLNAVAPVQLLGPDNTRWPLWNS
NNEVYITLLILFNVSSLVSMYSTTLLSLDYYIERALPRTYMSSVYNTKHVCGFIWGGAVLTSFSSLLFYI
CSHVSTKIIECSKMQNKEAADAIMVFIGYVVPALAVLYALVLILRIRKEATPLDQDSGRLDPSAHRLLLA
TVCTQFLLWTPYYMILLVHTVQASRGKKVDAGYLRVFHFLKGLSKLLAFSSSFVVPLLYRYMNKNFSSKL
>gnl|CDD|320122 cd14991, 7tmA_HCAR-like, hydroxycarboxylic acid receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes the hydroxycarboxylic acid receptors (HCARs) as well as their closely related receptors, GPR31 and oxoeicosanoid receptor 1 (OXER1). HCARs are members of the class A family of G-protein coupled receptors (GPCRs). HCAR subfamily contain three receptor subtypes: HCAR1, HCAR2, and HCAR3. The endogenous ligand of HCAR1 (also known as lactate receptor 1, GPR104, or GPR81) is L-lactic acid. The endogenous ligands of HCAR2 (also known as niacin receptor 1, GPR109A, nicotinic acid receptor) and HCAR3 (also known as niacin receptor 2, orGPR109B) are 3-hydroxybutyric acid and 3-hydroxyoctanoic acid, respectively. All three HCA receptors are expressed in adipocytes, and are coupled to G(i)-proteins mediating anti-lipolytic effects in fat cells. OXER1 is a receptor for eicosanoids and polyunsaturated fatty acids such as 5-oxo-6E,8Z,11Z,14Z-eicosatetraenoic acid (5-OXO-ETE), 5(S)-hydroperoxy-6E,8Z,11Z,14Z-eicosatetraenoic acid (5(S)-HPETE) and arachidonic acid, whereas GPR31 is a high-affinity receptor for 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid (12-S-HETE)
SILPPLLILEFVLGLPGNVVALWIFCFHSRTWKANTVYLFNLVLADFLLLICLPFRIDYYLRGEHWIFGE
AWCRVNLFMLSVNRSASIAFLTAVALDRYFKVVHPHHRVNRMSVKAAAGVAGLLWALVLLLTLPLLLSTL
LTVNSNKSSCHSFSSYTKPSLSIRWHNALFLLEFFLPLGLIVFCSVRIACNLRIRQSLGKQARVQRAIRL
VFLVVIVFVLCFLPSIIAGLLALVFKNLGSCRCLNSVAQLFHISLAFTYLNSALDPVIYCFSSPWFRNSL
>gnl|CDD|320123 cd14992, 7tmA_TACR_family, tachykinin receptor and closely related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This subfamily includes G-protein coupled receptors for a variety of neuropeptides of the tachykinin (TK) family as well as closely related receptors. The tachykinins are widely distributed throughout the mammalian central and peripheral nervous systems and act as excitatory transmitters on neurons and cells in the gastrointestinal tract. The TKs are characterized by a common five-amino acid C-terminal sequence, Phe-X-Gly-Leu-Met-NH2, where X is a hydrophobic residue. The three major mammalian tachykinins are substance P (SP), neurokinin A (NKA), and neurokinin B (NKB). The physiological actions of tachykinins are mediated through three types of receptors: neurokinin receptor type 1 (NK1R), NK2R, and NK3R. SP is a high-affinity endogenous ligand for NK1R, which interacts with the Gq protein and activates phospholipase C, leading to elevation of intracellular calcium. NK2R is a high-affinity receptor for NKA, the tachykinin neuropeptide substance K. SP and NKA are found in the enteric nervous system and mediate in the regulation of gastrointestinal motility, secretion, vascular permeability, and pain perception. NK3R is activated by its high-affinity ligand, NKB, which is primarily involved in the central nervous system and plays a critical role in the regulation of gonadotropin hormone release and the onset of puberty
IILGVALVVIILVSVVGNFIVIAALARHKNLRGATNYFIASLAISDLLMALFCTPFNFTYVVSLSWEYGH
FLCKIVNYLRTVSVYASSLTLTAIAFDRYFAIIHPLKPRHRQSYTTTVIIIITIWVVSLLLAIPQLYYAT
TEVLFSVKNQEKIFCCQIPPVDNKTYEKVYFLLIFVVIFVLPLIVMTLAYARISRELWFRKVPGFSIKEV
ERKRLKCKRRVIKMLVCVVVLFVICWLPFHLFFLLRDFFPLIMKEKHTLQVYYFLHWIAMSNSMYNPIIY
VTLNNNFRKNF
>gnl|CDD|320124 cd14993, 7tmA_CCKR-like, cholecystokinin receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group represents four G-protein coupled receptors that are members of the RFamide receptor family, including cholecystokinin receptors (CCK-AR and CCK-BR), orexin receptors (OXR), neuropeptide FF receptors (NPFFR), and pyroglutamylated RFamide peptide receptor (QRFPR). These RFamide receptors are activated by their endogenous peptide ligands that share a common C-terminal arginine (R) and an amidated phenylanine (F) motif. CCK-AR (type A, alimentary; also known as CCK1R) is found abundantly on pancreatic acinar cells and binds only sulfated CCK-peptides with very high affinity, whereas CCK-BR (type B, brain; also known as CCK2R), the predominant form in the brain and stomach, binds CCK or gastrin and discriminates poorly between sulfated and non-sulfated peptides. CCK is implicated in regulation of digestion, appetite control, and body weight, and is involved in neurogenesis via CCK-AR. There is some evidence to support that CCK and gastrin, via their receptors, are involved in promoting cancer development and progression, acting as growth and invasion factors. Orexins (OXs; also referred to as hypocretins) are neuropeptide hormones that regulate the sleep-wake cycle and potently influence homeostatic systems regulating appetite and feeding behavior or modulating emotional responses such as anxiety or panic. OXs are synthesized as prepro-orexin (PPO) in the hypothalamus and then proteolytically cleaved into two forms of isoforms: orexin-A (OX-A) and orexin-B (OX-B). OXA is a 33 amino-acid peptide with N-terminal pyroglutamyl residue and two intramolecular disulfide bonds, whereas OXB is a 28 amino-acid linear peptide with no disulfide bonds. OX-A binds orexin receptor 1 (OX1R) with high-affinity, but also binds with somewhat low-affinity to OX2R, and signals primarily to Gq coupling, whereas OX-B shows a strong preference for the orexin receptor 2 (OX2R) and signals through Gq or Gi/o coupling. The 26RFa, also known as QRFP (Pyroglutamylated RFamide peptide), is a 26-amino acid residue peptide that exerts similar orexigenic activity including the regulation of feeding behavior in mammals. It is the ligand for G-protein coupled receptor 103 (GPR103), which is predominantly expressed in paraventricular (PVN) and ventromedial (VMH) nuclei of the hypothalamus. GPR103 shares significant protein sequence homology with orexin receptors (OX1R and OX2R), which have recently shown to produce a neuroprotective effect in Alzheimer's disease by forming a functional heterodimer with GPR103. Neuropeptide FF (NPFF) is a mammalian octapeptide that has been implicated in a wide range of physiological functions in the brain including pain sensitivity, insulin release, food intake, memory, blood pressure, and opioid-induced tolerance and hyperalgesia. The effects of NPFF are mediated through neuropeptide FF1 and FF2 receptors (NPFF1-R and NPFF2-R) which are predominantly expressed in the brain. NPFF induces pro-nociceptive effects, mainly through the NPFF1-R, and anti-nociceptive effects, mainly through the NPFF2-R
IVLIVLYVVVFLLALVGNSLVIAVVLRNKHMRTVTNYFLVNLAVADLLVSLFCMPLTLLENVYRPWVFGE
VLCKAVPYLQGVSVSASVLTLVAISIDRYLAICYPLKARRVSTKRRARIIIVAIWVIAIIIMLPLLVVYE
LEEIISSEPGTITIYICTEDWPSPELRKAYNVALFVVLYVLPLLIISVAYSLIGRRLWRRKPPGDRGSAN
STSSRRILRSKKKVARMLIVVVVLFALSWLPYYVLSILLDFGPLSSEESDENFLLILPFAQLLGYSNSAI
NPIIYCFMSKKFRRGF
>gnl|CDD|320125 cd14994, 7tmA_GPR141, orphan G protein-coupled receptor 141, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup represents the G-protein coupled receptor 141 of unknown function. Several ESTs for GPR141 were found in marrow and cancer cells. GPR141 is a member of the rhodopsin-like, class A GPCRs, which is a widespread protein family that includes the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
TYSLIFLYSVVLIGGVIGVILMSFLLVKMNTRSVTTTAVINLIVVHSLFLLTVPFRIYYYASKTWKFGMP
LCKMVSAMIHIHMHLTFLFYVIILVIRYLIFFQRKDKMEFYRKLHAVAASAVVWVLVLLIVVPVFVKEYG
SSSSYNSDQCFKFHKELEVHYVKVLNYIIICIVLIVTLALLGFQVFILGHVYRKLRASLLSHQEFWAQMK
SLFFIVVIIVCFVPYNLFRIYYLSQVIQNEKLDPYNEIFLAVTALSCLDLLTFVGRGSPICKQKC
>gnl|CDD|320126 cd14995, 7tmA_TRH-R, thyrotropin-releasing hormone receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. TRH-R is a member of the class A rhodopsin-like G protein-coupled receptors, which binds the tripeptide thyrotropin releasing hormone. The TRH-R activates phosphoinositide metabolism through a pertussis-toxin-insensitive G-protein, the G(q)/G(11) class. TRH stimulates the synthesis and release of thyroid-stimulating hormone in the anterior pituitary. TRH is produced in many other tissues, especially within the nervous system, where it appears to act as a neurotransmitter/neuromodulator. It also stimulates the synthesis and release of prolactin. In the CNS, TRH stimulates a number of behavioral and pharmacological actions, including increased turnover of catecholamines in the nucleus accumbens. There are two thyrotropin-releasing hormone receptors in some mammals, thyrotropin-releasing hormone receptor 1 (TRH1) which has been found in a number of species including rat, mouse, and human and thyrotropin-releasing hormone receptor 2 (TRH2) which has, only been found in rodents. These TRH receptors are found in high levels in the anterior pituitary, and are also found in the retina and in certain areas of the brain
VVATFLVLLICGVGIVGNIMVVLVVLRTRHMRTPTNCYLVSLAVADLMVLVAAGLPNEIESLLGPDSWIY
GYAGCLLITYLQYLGINASSLSITAFTIERYIAICHPMKAQFICTVSRAKKIICFVWIFTSLYCSPWLFL
LDLSIKHYGDDIVVRCGYKVSRHYYLPIYLADFVLFYVIPLLLAIVLYGLIGRILFSSRKQVTKMLAVVV
VLFALLWMPYRTLVVYNSFASPPYLDLWFLLFCRTCIYLNSAINPILYNLMSQKFRAAF
>gnl|CDD|320127 cd14996, 7tmA_GPR82, orphan G protein-coupled receptor 82, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup represents the G-protein coupled receptor 82 of unknown function. GPR82 is a member of the rhodopsin-like, class A GPCRs, which is a widespread protein family that includes the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VALPIIYSFLFVTGVFGNLLSLWVFLTKISKKTSTHIYLINLVTANLLVCSAMPFQAAYFLKGFYWKYQS
TQCRIANFFGTLVIHVSMCVSILILSWIAISRYATLMKHDSATQKQSCYEKIFYGHFLKRFRQPKFARYL
CIYIWGVVLCIIIPVVVYYSVREADEDGESLCYNRQVELGAKGSQIAGLIATTFFFLFFLVVLLSYYSFV
NHLRRIQKNTCISEKDLIYRSVKRNILIIQALLVVCFLPYHIFKPVFYVLHQREDCQQLNYLIETKNILT
CLASARSSTDPIMYLLLDKTFKKTL
>gnl|CDD|320128 cd14997, 7tmA_ETH-R, ecdysis-triggering hormone receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup represents the ecdysis-triggering hormone receptors found in insects, which are members of the class A family of seven-transmembrane G-protein coupled receptors. Ecdysis-triggering hormones are vital regulatory signals that govern the stereotypic physiological sequence leading to cuticle shedding in insects. Thus, the ETH signaling system has been a target for the design of more sophisticated insect-selective pest control strategies. Two subtypes of ecdysis-triggering hormone receptor were identified in Drosophila melanogaster. Blood-borne ecdysis-triggering hormone (ETH) activates the behavioral sequence through direct actions on the central nervous system. In insects, ecdysis is thought to be controlled by the interaction between peptide hormones; in particular between ecdysis-triggering hormone (ETH) from the periphery and eclosion hormone (EH) and crustacean cardioactive peptide (CCAP) from the central nervous system. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VLVSVVYGVIFVVGVLGNVLVGIVVWKNKDMRTPTNIFLVNLSVADLLVLLVCMPVALVETWAREPWLLG
EFMCKLVPFVELTVAHASVLTILAISFERYYAICHPLQAKYVCTKRRALVIIALIWLLALLTSSPVLFIT
EFKEEDFNDGTPVAVCRTPADTFWKVAYILSTIVVFFVVPLAILSGLYSVICRRLVGHPALESRRADAAN
RHTLRSRRQVVYMLITVVVLFFVCLLPFRVVTLWIIFAPDEDLQALGLEGYLNLLVFCRVMVYLNSALNP
ILYNLMSTKFRSAF
>gnl|CDD|320129 cd14998, 7tmA_GPR153_GPR162-like, orphan G protein-coupled receptors 153 and 162, member of the class A family of seven-transmembrane G protein-coupled receptors. This group contains the G-protein coupled receptor 153 (GPR153), GPR162, and similar proteins. These are orphan GCPRs with unknown endogenous ligand and function. GPR153 and GPR163 are widely expressed in the central nervous system (CNS) and share a common evolutionary ancestor due to a gene duplication event. Although categorized as members of the rhodopsin-like class A GPCRs, both GPR162 and GPR153 contain an HRM-motif instead of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors which is important for efficient G protein-coupled signal transduction. Moreover, the LPxF motif, a variant of NPxxY motif that plays a crucial role during receptor activation, is found at the end of TM7 in both GPR162 and GPR153. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
PGNALSWLACGGLSLLANAWGILSISAKQQKHKPLELLLCFLAGTHMLMVAVPLTTYSVVQLRRQASDYD
WNEGLCKVFVSTFYTLTLATCFTVTSLSYHRMWMVRWPVNYRLSNAKKQALHAVMGIWMVSFILSTLPSI
GWHDNSERYYTHGCRFIVSKIGLGFGVCFSLLLGGGIAMGVVCVAITFFQTLAAQVRRQADRRAFTVPTI
VVEDAQGKRRSSIDGSESAKTSLQTTNLVTAIVFIYDSLTGFPILVVSFSSLKADAAPPWMVLCVLWCSM
AQTLLLPSFLWSCERYRADVK
>gnl|CDD|320130 cd14999, 7tmA_UII-R, urotensin-II receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The urotensin-II receptor (UII-R, also known as the hypocretin receptor) is a member of the class A rhodopsin-like G-protein coupled receptors, which binds the peptide hormone urotensin-II. Urotensin II (UII) is a vasoactive somatostatin-like or cortistatin-like peptide hormone. However, despite the apparent structural similarity to these peptide hormones, they are not homologous to UII. Urotensin II was first identified in fish spinal cord, but later found in humans and other mammals. In fish, UII is secreted at the back part of the spinal cord, in a neurosecretory centre called uroneurapophysa, and is involved in the regulation of the renal and cardiovascular systems. In mammals, urotensin II is the most potent mammalian vasoconstrictor identified to date and causes contraction of arterial blood vessels, including the thoracic aorta. The urotensin II receptor is a rhodopsin-like G-protein coupled receptor, which binds urotensin-II. The receptor was previously known as GPR14, or sensory epithelial neuropeptide-like receptor (SENR). The UII receptor is expressed in the CNS (cerebellum and spinal cord), skeletal muscle, pancreas, heart, endothelium and vascular smooth muscle. It is involved in the pathophysiological control of cardiovascular function and may also influence CNS and endocrine functions. Binding of urotensin II to the receptor leads to activation of phospholipase C, through coupling to G(q/11) family proteins. The resulting increase in intracellular calcium may cause the contraction of vascular smooth muscle
AIGTVLSLMCVVGVAGNVYTLVVMCLSMRPRASMYVYILNLALADLLYLLTIPFYVSTYFLKKWYFGDVG
CRLLFSLDFLTMHASIFTLTVMSTERYLAVVKPLDTVKRSKSYRKLLAGVIWLLSLLLTLPMAIMIRLVT
VEDKSGGSKRICLPTWSEESYKVYLTLLFSTSIVIPGLVIGYLYIRLARKYWLSQAAASNSSRKRLPKQK
VLKMIFTIVLVFWACFLPFWIWQLLYLYSPSLSLSPRTTTYVNYLLTCLTYSNSCINPFLYTLLTKNYKE
YL
>gnl|CDD|320131 cd15000, 7tmA_BNGR-A34-like, putative neuropeptide receptor BNGR-A34 and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup includes putative neuropeptide receptor BNGR-A34 found in silkworm and its closely related proteins from invertebrates. They are members of the class A rhodopsin-like GPCRs, which represent a widespread protein family that includes the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
IKSSMFLPVVLFGIFGNFVLLYILASNRSLRTPTNLLIGNMALADLLTLLVCPWMFLVHDFFQNYVLGSV
GCKLEGFLEGSLLLASVLALCAVSYDRLTAIVLPSEARLTKRGAKIVIVITWIVGLLLALPLAIYRSYRE
RQWKNFLETYCAENTQVLPIYWHVIITVLVWLPLGIMLICYSAIFWKLDKYERRVLRREHPSVVRYKKKA
AKTLFIVLITFVVCRIPFTALIFYRYKLVPNDNTQNSVSGSFHILWFASKYLMFLNAAVNPLIYGFTNEN
FRKAF
>gnl|CDD|320132 cd15001, 7tmA_GPRnna14-like, GPRnna14 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes the orphan G-protein coupled receptor GPRnna14 found in body louse (Pediculus humanus humanus) as well as its closely related proteins of unknown function. These receptors are members of the class A rhodopsin-like G-protein coupled receptors. As an obligatory parasite of humans, the body louse is an important vector for human diseases, including epidemic typhus, relapsing fever, and trench fever. GPRnna14 shares significant sequence similarity with the members of the neurotensin receptor family. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
PVIIVYVITFVLGLIGNSLVIFVVARFRRMRSVTNVFLASLATADLLLLVFCVPLKTAEYFSPTWSLGAF
LCKAVAYLQLLSFICSVLTLTAISIERYYVILHPMKAKSFCTIGRARKVALLIWILSAILASPVLFGQGL
VRYESENGVTVYHCQKAWPSTLYSRLYVVYLAIVIFFIPLIVMTFAYARDTRKQVIKMLISVVVLFAVCW
GPLLIDNLLVSFDVISTLHTQALKYMRIAFHLLSYANSCINPIIYAFMSKNFRSSF
>gnl|CDD|320133 cd15002, 7tmA_GPR151, G protein-coupled receptor 151, member of the class A family of seven-transmembrane G protein-coupled receptors. G-protein coupled receptor 151 (GRP151) is an orphan receptor of unknown function. Its expression is conserved in habenular axonal projections of vertebrates and may be a promising novel target for psychiatric drug development. GPR151 shows high sequence similarity with galanin receptors (GALR). GPR151 is a member of the class A rhodopsin-like GPCRs, which represent a widespread protein family that includes the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
LVPILLGVICLLGFAGNLMVIGILLNNARKGKPSLIDSLILNLSAADLLLLLFSVPFRAAAYSKGSWPLG
WFVCKTADWFGHACMAAKSFTIAVLAKACYMYVVNPTKQVTIKQRRITAVVASIWVPACLLPLPQWLFRT
VKQSEGVYLCILCIPPLAHEFMSAFVKLYPLFVFCLPLTFALFYFWRAYGQCQRRGTKTQNLRNQIRSRK
LTHMLLSVVLAFTILWLPEWVAWLWLIHIKSSGSSPPQLFNVLAQLLAFSISSVNPIIFLLMSEEFREGF
>gnl|CDD|320134 cd15005, 7tmA_SREB-like, super conserved receptor expressed in brain and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. The SREB (super conserved receptor expressed in brain) subfamily consists of at least three members, named SREB1 (GPR27), SREB2 (GPR85), and SREB3 (GPR173). They are very highly conserved G protein-coupled receptors throughout vertebrate evolution, however no endogenous ligands have yet been identified. SREB2 is greatly expressed in brain regions involved in psychiatric disorders and cognition, such as the hippocampal dentate gyrus. Genetic studies in both humans and mice have shown that SREB2 influences brain size and negatively regulates hippocampal adult neurogenesis and neurogenesis-dependent cognitive function, all of which are suggesting a potential link between SREB2 and schizophrenia. All three SREB genes are highly expressed in differentiated hippocampal neural stem cells. Furthermore, all GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
ALKLTTLGLILCVSLAGNLLFSVLIVRDRSLHRAPYYFLLDLCLADGLRSLACFPFVMASVRHGSGWIYG
ALSCKVIAFLAVLFCFHSAFTLFCIAVTRYMAIAHHRFYAKRMTFWTCLAVICMAWTLSVAMAFPPVFDV
GTYTFIREEDQCTFEHRSYKANDTLGFMLVLAVVIAATHLVYLKLLIFLRHHRKMKPAQLVPAISQNWTF
HGPGATGQAAANWTAGFGRGPTPPTLLGIRQAFHSGARRLLVLDEFKMEKRLTRMFYAITLLFLLLWSPY
IVACYIRVFVRGYAVPQGFLTAAVWMTFAQAGVNPIVCFFFNRELRKCL
>gnl|CDD|320135 cd15006, 7tmA_GPR176, orphan G protein-coupled receptor 176, member of the rhodopsin-like class A GPCR family. GPR176 is a putative G protein-coupled receptor that belongs to the class A GPCR superfamily; no endogenous ligand for GPR176 has yet been identified. The class A rhodopsin-like GPCRs represent a widespread protein family that includes the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
FTTTVQVVIFVGSLLGNFMVLWSTCRTSVFKSVTNRFIKNLACSGICASLVCVPFDIVLSASPHCCWWIY
TLLFCKVIKFLHKVFCSVTVLSFAAIALDRYYSVLYPLERKISDAKSRDLVIYIWAHAVVASVPVFAVTN
VTDIYAMSTCTESWGYSLGHLVYVIIYNITTVILPVAVVFLFMILIRRALSASQKKKVIIAALRTPQNTI
SIPYVSQREAELHAMLLSMVLVFILCSVPYATLVIYRTILNISDISVFLLLTAIWLPKVSLLANPLLFLT
VNKSVRKCL
>gnl|CDD|320136 cd15007, 7tmA_GPR75, G protein-coupled receptor 75, member of the class A family of seven-transmembrane G protein-coupled receptors. G-protein coupled receptor 75 (GPR75) is an atypical chemokine receptor that is expressed by mouse and human islets. Although GPR75 shows low sequence homology to C-C chemokine receptors, chemokine (C-C motif) ligand 5 (CCL5) has been shown to act as an endogenous ligand for GPR75. CCL5 plays a key role in recruiting lymphocytes to sites of inflammatory and infection through promiscuous binding to the C-C chemokine G-protein-coupled receptors. Although categorized as a member of the rhodopsin-like class A GPCRs, GPR75 contains HRL-motif instead of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors and important for efficient G protein-coupled signal transduction. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, which then activate the heterotrimeric G proteins. GPR75 is coupled to the G-protein G(q), which elevates intracellular calcium
TCTFLLAFIFCLGSYGNLVVFLSFFDPAFRKFRTNFDFMILNLSFCDLFICCVTAPMFAFVLFLDSGGGV
PDAFCFTFHLTSSGFIIMSLKTVAVIALHRLRMVLGQQPNRTASFPCTLLLTLLLWTTSFTLATLATLRT
RKSRLCLPMSSLIGGEGKIILYLYVADFTFCVAVVSVSYIMIAQTLRAKDSKAVVTCVVIVLSVLVCCLP
LGISLVQDVLSSNSSFILYQFELCGFTLIFFKSGLNPFIYSRNSAGLRRRV
>gnl|CDD|320137 cd15008, 7tmA_GPR19, G protein-coupled receptor 19, member of the class A family of seven-transmembrane G protein-coupled receptors. G-protein coupled receptor 19 is an orphan receptor that is expressed predominantly in neuronal cells during mouse embryogenesis. Its mRNA is found frequently over-expressed in patients with small cell lung cancer. GPR19 shares a significant amino acid sequence identity with the D2 dopamine and neuropeptide Y families of receptors. Human GPR19 gene, intronless in the coding region, also has a distribution in brain overlapping that of the D2 dopamine receptor gene, and is located on chromosome 12. GPR19 is a member of the class A family of GPCRs, which represents a widespread protein family that includes the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
AASLVFGVLWLVSVFGNSLVCLVIHRSRRTQSTTNYFVVSMACADLLLSVASAPFVLLQFTSGRWTLGSA
MCKLVRYFQYLTPGVQIYVLLSICVDRFYTIVYPLSFKVSREKAKKMIAASWLFDAAFVSPALFFYGSNW
GPHCNFFLPDSWDGAAYAIIHLLVGFLVPSILIILFYQKVIKYIWRIGTDGRTVRRTMNIVPRTKVKTIK
MFLMLNSMFLLSWLPFYVVQLWHPRESDYRQSSLVFLAVTWISFSSSASKPTLYSVYNANFRRGM
>gnl|CDD|410631 cd15010, 7tmA_ACKR1_DARC, Duffy antigen receptor for chemokines, member of the class A family of seven-transmembrane G protein-coupled receptors. Atypical chemokine receptor 1 (ACKR1), also known as DARC (Duffy antigen receptor for chemokines) or Fy glycoprotein (GpFy), was originally identified on erythrocytes. ACKR1 is also ubiquitously expressed by endothelial cells of venules and is highly promiscuous among all chemokine receptor. It binds many proinflammatory chemokines from both the CC and CXC subfamilies, including CCL2, CCL5, CCL7, CCL11, CXCL1, CXCL2, CXCL3, and CXCL5. Erythrocyte ACKR1 is thought to act as a chemokine sink, limiting the levels of circulating chemokines, thereby controlling leukocyte activation. ACKR1-deficient erythrocytes are shown to confer resistance to the malarial parasite, Plasmodium vivax. On the other hand, ACKR1-expressing endothelial cells can internalize chemokines. ACKR1-internalized chemokines can be moved intact across the endothelium and promotes neutrophil transmigration. Unlike the classical chemokine receptors that contain a conserved DRYLAIV motif in the second intracellular loop, which is required for G-protein coupling, the ACKRs lack this conserved motif and fail to couple to G-proteins and induce classical GPCR signaling. Five receptors have been identified for the ACKR family, including CC-Chemokine Receptors like 1 and 2 (CCRL1 and CCRL2), CXCR7, DARC, and D6. Both ACKR1 (DARC) and ACKR3 (CXCR7) show low sequence homology to the classic chemokine receptors
SALPFFALTSALGILASGALLVALLRPLFRWQWPPSRPLLAQLAVGSALFSIVVPILAPGLSQGWGTGLC
KLAYLVWYGSAFAQALLVGCHACLGPWLGWGQVPGLTLGLAVGLWGAAALLALPVALASGTSGGPCTLRS
SRDLEALYLTHLAACLAIFVLLPLGLLGAKGLKTALRVGPGPWVGVLWLWFIFWWPYGVVLGLDFLVRSK
LLLLSTCGAQEALDYMLGLSEALGILHCVATPLLLALVCHQATHTSP
>gnl|CDD|320139 cd15011, 7tmA_GPR149, G protein-coupled receptor 149, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR149 is predominantly expressed in the ovary and is present at low levels in the brain and the digestive tract (stomach and small intestine). GPR149-null mice are viable and have normal maturation of the ovarian follicle, but show enhanced fertility and ovulation. Additionally, the null mice showed increased expression levels of growth differentiation factor 9 (Gdf9) in oocytes, and upregulated expression of cyclin D2, a downstream target of FSH (follicle-stimulating hormone) receptor signaling pathways that promotes granulosa cell proliferation. GPR149 is an orphan receptor with no known endogenous ligand as yet identified. Although categorized as a member of the class A GPCRs, GPR149 lacks the first two charged amino acids of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors which is important for efficient G protein-coupled signal transduction. Moreover, the transmembrane domains and carboxyl terminus of GPR149 show low similarities to other GPCRs. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
LLFCLTLIIALLTLLGSIYSLLSLLKMRNKTTLSVLVASLSVDDLLSVVPVSIFMLMQWETDGLPQPLCT
TSALLYLFQGLSSNLKASLIASYNFYTTKKLGWLQTTKRSVRVPWAVLTIWAASLLLSALPLCGWGSFVP
TSWGCLVDCQSSYILFLFSLYSLCFCILVVLSVPLTYQLLCSDETVSFAQKRFSLILALTKVILWLPMMI
QMVVQHVTGFQSLSLETLSFLLTLLAAAVTPLFVLSERWIHLPCGC
>gnl|CDD|320140 cd15012, 7tmA_Trissin_R, trissin receptor and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup represents the Drosophila melanogaster trissin receptor and closely related invertebrate proteins which are a member of the class A family of seven-transmembrane G-protein coupled receptors. The cysteine-rich trissin has been shown to be an endogenous ligand for the orphan CG34381 in Drosophila melanogaster. Trissin is a peptide composed of 28 amino acids with three intrachain disulfide bonds with no significant structural similarities to known endogenous peptides. Cysteine-rich peptides are known to have antimicrobial or toxicant activities, although frequently their mechanism of action is poorly understood. Since the expression of trissin and its receptor is reported to predominantly localize to the brain and thoracicoabdominal ganglion, trissin is predicted to behave as a neuropeptide. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
IFIILYTLVFCCCFFGNLLVILVVTSHRRMRTITNFFLANLAVADLCVGIFCVLQNLSIYLIPSWPFGEV
LCRMYQFVHSLSYTASIGILVVISVERYIAILHPLRCKQLLTAARLRVTIVTVWLTSAVYNTPYFVFSQT
VEILVTQDGQEEEICVLDREMFNSKLYDTINFIVWYLIPLLIMTVLYSKISIVLWKSSSIEARRKVVRLL
VAVVVSFALCNLPYHARKMWQYWSEPYRCDSNWNALLTPLTFLVLYFNSAVNPLLYAFLSKRFRQSM
>gnl|CDD|320141 cd15013, 7tm_TAS2R4, mammalian taste receptor 2, subtype 4, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (TAS2R) subtype 4, which functions as a bitter taste receptor. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
IFVFIASVVFNFVGIVANLFIIVVNCKTWVKSHRISSSDRILFSLAITRFLMLGLFLLNTIYIATFPGSR
SVYFSTFFLLCWKFLDSNSLWFVTLLNILYCVKITNFQHSVFLLLKRNLSPKTPWLLLACLLISAFTTLL
YIVLSQISPFPEHIIGRNNTSFDISDGILTLVASLILSSSLQFILNVTSASLLIHSLRRHIQKMQKNATS
FWNPQTEAHVGAMKLMIYFLILYIPYSIATLLYFLPSYMGKNLRAQSICMIFTTLYSPGHSVLIIITHPK
LKAKAK
>gnl|CDD|320142 cd15014, 7tm_TAS2R40, mammalian taste receptor 2, subtype 40, member of the seven-transmembrane G-protein coupled receptor superfamily. This group includes the mammalian taste receptor 2 (T2R) subtype 40, which functions as a bitter taste receptor. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (taste of glutamate MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
IIPFVVSTIECIVGIIGNGFITVIYGTEWVRSKRLPTGERLMLMLSFSRLLLQIWMMVEITYSLLFPIIY
NHNAMYKLFKVISVFLNYCNLWFAAWLNVFYCLKIVNFAHPLFLLMKQKIIVLMPRLLSLSVLVSLSLSS
FFSKDIFNVYVNTSVPIPSSNSTKMKYFFETNVLNLAFLYYMGIFVPLFMFIMAATLLITSLKRHTLHME
SSTTGSRDSSMEAHIGAIKSTSYSLILYIINALALFISMSNIFGAYSSWNSLCKIIMTAYPAGQSVHLIL
RNPGLRRAWR
>gnl|CDD|320143 cd15015, 7tm_TAS2R39, mammalian taste receptor 2, subtype 39, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (T2R) subtype 39, which functions as a bitter taste receptor. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (taste of glutamate MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
ILILTLVATECTIGIIASGIIMAVNAVSWVQKKAVSITTRILLLLSVSRIGLQSIMLIEITSSIFNLSFY
NSVLYRVSKVSFVFLNYCSLWFAALLSFFHFVKIANFSYPLFFKLKWRISELMPWLLWLSVFISFSSSMF
FINHKTTVCNNSSLSSNICNFTMKLYVSEINVVNVAFLFNLGILPPLTMFIATATLLIFSLRRHTLHMRN
NATGSRNPSMEAHMQAIKETSCFLFLYILNAAALFLSTSNIFDASLFWSNVCRIILPVYPAGHSVLLIQD
NPGLRRTWK
>gnl|CDD|320144 cd15016, 7tm_TAS2R1, mammalian taste receptor 2, subtype 1, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (TAS2R) subtype 1, which functions as a bitter taste receptor. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
IIHLLFAVIQFLTGIFANGFIVVVNGIDLIKQRKMAPLDLLLSCLATSRICLQLFIFYLNLAVLSLIKFS
VFAENFVIFMFVNELGLWFATWLGVFYCAKIATIAHPLFLWLKMRISKLVPWLILGSLLYASITSVFHSK
YTWPISQKLLLSFFSSNATTQIKEISALQLSLLIFELSLPLLIFLVAVLLLIFSLGRHTRQMRTTAAGTR
DPSRSAHISALLSILSFLILYLSHYMAAALLSSQIFQFGSLFFLFCILVIGAYPSGHSIILILGNPKLKQ
NAK
>gnl|CDD|320145 cd15017, 7tm_TAS2R16, mammalian taste receptor 2, subtype 16, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (TAS2R) subtype 16, which functions as a bitter taste receptor. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
LFFMIIFVLESLAAIVQNGFIVTVLGREWVRCRRLPPGDMILACLGISRFCLQWISILNNFLSYFDFNYV
FWYFGIIWDFFNTLTFWLTSLLAVFYCVKISSFTHPIFLWLKWRISRLVPWLLLGSLIISCLSIIPSIVG
NYIQAQLITSGNSSGNSTLIYRLQAFQQYYFIPHQMVMLSIPFLLFLVSIILLMFSLCQHLGQMRHHSPG
PCDPSTQAHTTALKSLAFFLIFFTSYFLTLIISIIKIIFVKNSWFWAWEAVIYAGISIHSTSLMLSSPKL
RKALK
>gnl|CDD|320146 cd15018, 7tm_TAS2R41-like, mammalian taste receptor 2, subtype 41, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (TAS2R) subtype 41, which functions as a bitter taste receptor. Also included is the closely related TAS2R60. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
IFLVLILFLLCLVAIVGNGFIVVALGREWLLRRTLLPCDKLLVSLGASRFCLQWVVMGKNIYVFLHPVAF
PYNPVLQFLSFHWDFLNSATLWFCTWLSVFYCVKIATFTHPVFLWLKWRFSGWVPWLLLGSVGISSLTTI
LFFIGNHSIYQNYLRRGLSSNNTTYNWRRSLEKFYFFSLKLITWSIPTSVFLISMVLLINSLRRHTKKML
HNLSSLQDPSTQAHIKALKALISFLILFASYFLSLVLSAAGVFPSQEVRYWVWQIVIYLCIAVHPFILLF
SNPKLRGVFR
>gnl|CDD|320147 cd15019, 7tm_TAS2R14-like, mammalian taste receptor 2, subtype 14, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (TAS2R) subtype 14, which functions as a bitter taste receptor. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
IFTIILSVEFIIGNLGNGFIALVNCMDWVKRRKISSVDQILTALAISRIGLLWLVFISWLISVLYPALLM
TEKMLRIINISWTVTNHFSIWLATCLSIFYFLKIANFSNSIFLYLKWRVKKVVSVTLLVSLVLLFLNIVL
INTHIDVWIDGYKRNMSYSSSSSNSAQFSKLLLFTNTMFTFIPFTVSLTTFLLLIFSLWKHLKKMQHNAK
GSRDASTTAHIKALQTVIAFLLLYTIFFLSLLVQVWSSELLEKNLIILFCQVIGIAFPSGHSCVLILGNS
KLRQASLSVL
>gnl|CDD|320148 cd15020, 7tm_TAS2R3, mammalian taste receptor 2, subtype 3, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (TAS2R) subtype 3, which functions as a bitter taste receptor. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
IVFLVLTITEFILGIWVNGFIGLVNCIHWIKSKKISLSDFIITNLALSRIILLCIIITDSLLLVFYPHFH
DSGIIMQIIDIFWTFANHLSIWLVTCLSVFYCLKIANFSHPAFLWLKWRVSRVVVWILLGSVLFSFFSTA
ALIKKFKIYSALRQMRLTENCTEDIRRKEIEYYVAHILGALWSVIPFIVSLISYLLLILSLRRHTQQMQH
HTTGSRDPSTEAHVRATKIILSFLLLFIFYFVAFFIGSSSFFLPDTKLAIMIGELITAAYPSVHSFILIL
QNNKLKQAFL
>gnl|CDD|320149 cd15021, 7tm_TAS2R10, mammalian taste receptor 2, subtype 10, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (TAS2R) subtype 10, which functions as a bitter taste receptor. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
GILLFVVTSEAVLGVLGNGFIALVNCIDYARNKKLSKIGFILTGLAISRIFLIWIIILDAYVKLFSPHML
ASGNLIEYISYIWVIINHLSVWFATSLSIFYFLKIANFSHYIFLWLKRRIDVVFIFLIGCLLISWLISFP
QVAKIINDIKMKYRNTSWQLHLEKSEFFINYVFTNLGVIFFFMVALITCFLLIISLWRHNRQMQSNVSGF
RDLNTEAHVKAMKVLISFIILFILYFIGISIETLCFFLPENKLLFIFGLTTACMYPCCHSFILILANSQL
KQASL
>gnl|CDD|320150 cd15022, 7tm_TAS2R8, mammalian taste receptor 2, subtype 8, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (TAS2R) subtype 8, which functions as a bitter taste receptor. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
NIFIILITGEFIIGILGNGYIALVNWIDWIKKKKISSIDYILTSLAISRICLISVIVVNGIVIVLYPDVY
ENDKLQIVISTFWTFANYLSMWFATCLNVFYLLKIANFSHPLFLWLKWRIDRVVHWILLGCFAISLLVSL
ILAIVLSDDYRFHAIAKHKRNITEMFHVSKIQYFEPLTLFNLFAIVPFTVSLISFFLLIRSLWRHTKQMK
LSATGGRDPSTEAHVRAIKTVTSFLFFFFLYYLSSLLVTFSYLMTEYKLAMMFGEIVAILYPLGHSLILI
IGNNKLRQASVR
>gnl|CDD|320151 cd15023, 7tm_TAS2R7-like, mammalian taste receptor 2, subtypes 7 and 9, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (TAS2R) subtypes 7 and 9, which function as bitter taste receptors. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
TIYMILIAGELTIGIWGNGFIVLVNCIGWLKRRDIALIDIILISLAISRICLLCVISLDGFIMVLFPDTY
GNGKLMSIIDVFWTFTNHSSIWFTSCLSIFYLLKIANISHPLFLWLKWRINKVILAILLGSLVLSLIISV
PKTENLWDDFRKCVKTKHEENITLKFKVSKTQGASKQVFLNLGVLVPFILSLISFLLLLFSLVRHTKQMQ
LHATGFRDPSTEAHMRAIKAVIIFLLLLIVYYLAFLVATSSYLIPQGKLVVMFGEIITLIFPSSHSFILI
MGNSKLREAFL
>gnl|CDD|320152 cd15024, 7tm_TAS2R42, mammalian taste receptor 2, subtype 42, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (TAS2R) subtype 42, which functions as a bitter taste receptor. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
IFLILAIGEFIIGMLGNGFIGLVNCSDWVKNRKISLADCILTCLAISRIGQLLVILFDSFILVLWPHLYG
TYKLAKVVSILWTLTNHLTTWFATCLSIFYFLKIANFSHPLFLWLKWRISRVLLVLLLGSLFLLFFDFLL
LETFSDFWLNIYTIDEGNLTLSSEESKTLYVKSLILFSLIYLIPFLLSLTSLLLLFLSLVRHTRNLQLNS
LGSRDSSTEAHKRAMKMVMSFLLLFIIHFFSIQLAGWIFFFLWKKQAILFVMLTSNIFPSGHSFILILGN
SKLRQTAL
>gnl|CDD|320153 cd15025, 7tm_TAS2R38, mammalian taste receptor 2, subtype 38, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (T2R) subtype 38, which functions as a bitter taste receptor. Genetic variants of human TAS2R38 influence the ability to taste synthetic compounds 6-n-propylthiouracil (PROP) and phenylthiocarbamide (PTC). Thus, sensitivity to the bitter taste of PROP is often used as a marker for individual differences in taste perception that can affect food preferences and intake. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
ITFLFLSVLEFAVGILANAFIVLVNFWDVVKRQPLNNCDIVLLCLSITRLFLQGLLFLDAIQLTHFQQMK
DPLSHSYQAIIMLWMIANQVSLWLAACLSLLYCSKIARFSHTFLLCLASWVSRRIPQMLLGSLLFSCICT
VLCVWDFFSRSHSTVTSSLHMNNTELNLQIEKLNFFYSFLFCNVGSVPPFLLFLVSSGVLIISLGRHMRT
MKAQTSGSRDPSLEAHIRALKSLVSFLCFYVVSFCAALISVPLLLLWHNKIGVMVCVGIMAACPSGHAAI
LISGNAKLRRVVK
>gnl|CDD|320154 cd15026, 7tm_TAS2R13, mammalian taste receptor 2, subtype 13, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (TAS2R) subtype 13, which functions as a bitter taste receptor. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
NILTLIIIAEFIFGNLSNGFIVLINCIDWVKKRKLSSIDKILLILAISRIGLIWETLVYWFKAQYYSSFF
ITGTELRIIVFSWILSNHFSLWLATILSIFYLLKIANFSWPIFLYLKWRIKKVILMMLLGSLVFLFLNLI
QINIHIEDWFYQYERNTTWNSMESDFAKFSELVLFNMTMFSVIPFTVALISFLLLIFSLWKHLQKMQLNS
RGHRDPSTKAHRNALRIMVSFLLLYASYFLSLLISWIAQKHQSELAYIICIITGLFYPSSHSFILILGNS
KLRQASL
>gnl|CDD|320155 cd15027, 7tm_TAS2R43-like, mammalian taste receptor 2, subtype 43, and related proteins, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (T2R) subtype 43, which functions as a bitter taste receptor. Also included are the closely related taste receptors TAS2R19, TAS2R20, TAS2R30, TAS2R31, TAS2R45 and TAS2R50. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
SLLLIILSILVMAEFVLGNFANGFIALVNCIDWVKRQKISSVDQILTALAVSRIGLLWVILINWYATVFN
PALYSLEVRIIIHIAWAVTNHFSTWLATSLSIFYLLKIANFSNLIFLYLKRRVKSVILVILLGSLVFLVF
HLAVVNIDENVWVNEYEGNVTWKTKLRDIIHLSNMTVFTLANFIPFTMSLISFLLLIFSLCKHLKKMQLH
GKGSQDPSTKVHIKALQTVISFLLLFAIYFLSLIISVWSSNRLQNKPVLLLCQAIGILYPSSHSFILIWG
NKKLKQAFLSFL
>gnl|CDD|320156 cd15028, 7tm_Opsin-1_euk, proton pumping rhodopsins in fungi and algae, member of the seven-transmembrane GPCR superfamily. This subgroup represents uncharacterized proton pumping rhodopsins found in fungi and algae. They belong to the microbial rhodopsin family, also known as type I rhodopsins, consisting of the light-driven inward chloride pump halorhodopsin (HR), the outward proton pump bacteriorhodopsin (BR), the light-gated cation channel channelrhodopsin (ChR), the light-sensor activating transmembrane transducer protein sensory rhodopsin II (SRII), and the other light-driven proton pumps such as blue-light absorbing and green-light absorbing proteorhodopsins, among others. Microbial rhodopsins have been found in various single-celled microorganisms from all three domains of life, including halophile archaea, gamma-proteobacteria, cyanobacteria, fungi, and green algae. While microbial (type 1) and animal (type 2) rhodopsins have no sequence similarity with each other, they share a common architecture consisting of seven-transmembrane alpha-helices (TM) connected by extracellular loops and intracellular loops. Both types of rhodopsins consist of opsin and a covalently attached retinal (the aldehyde of vitamin A), a photoreactive chromophore, via a protonated Schiff base linkage to an amino group of lysine in the middle of the seventh transmembrane helix (TM7). Upon the absorption of light, microbial rhodopsins undergo light-induced photoisomerization of all-trans retinal into the 13-cis isomer, whereas the photoisomerization of 11-cis retinal to all-trans isomer occurs in the animal rhodopsins. While animal visual rhodopsins are activated by light to catalyze GDP/GTP exchange in the alpha subunit of the retinal G protein transducin (Gt), microbial rhodopsins do not activate G proteins, but instead can function as light-dependent ion pumps, cation channels, and sensors
HTGHRTLWVVFVLMLLSSLVFYILSWRVPVQKRLFHVLTTLITTIAALSYFAMATGQGITYVHISVRHKH
HVPDTHHHVFRQVFWARYVDWALTTPLLLLDLALLAGLPGADILVAIVADVIMVLTGLFAAFGHSTGQKW
GWFTISCIAFLTVVYHLGVNGRRAARARSSKTRRLFGAIAVYTLVLWTLYPIVWALGDGARKISVDAEII
AYAVLDVLAKPVFGFWLLLAH
>gnl|CDD|320157 cd15029, 7tm_SRI_SRII, light-sensor activating transmembrane transducer protein sensory rhodopsin I and II; member of the seven-transmembrane GPCR superfamily. This subgroup includes the light-sensor activating transmembrane transducer proteins, sensory rhodopsin I (SRI) and II (SRII, also called phoborhodopsin). SRI and SRII are responsible for positive (attractive) and negative (repellent) phototaxis in halobacteria, respectively, thereby controlling the cell's directional movement in response to changes in light intensity by swimming either towards or away from the light. Both sensory rhodopsins belong to the family of microbial rhodopsins, also known as type I rhodopsins, consisting of the light-driven inward chloride pump halorhodopsin (HR), the outward proton pump bacteriorhodopsin (BR), the light-gated cation channel channelrhodopsin (ChR), and the other light-driven proton pumps such as blue-light absorbing and green-light absorbing proteorhodopsins, among others. Microbial rhodopsins have been found in various single-celled microorganisms from all three domains of life, including halophile archaea, gamma-proteobacteria, cyanobacteria, fungi, and green algae. While microbial (type 1) and animal (type 2) rhodopsins have no sequence similarity with each other, they share a common architecture consisting of seven-transmembrane alpha-helices (TM) connected by extracellular loops and intracellular loops. Both types of rhodopsins consist of opsin and a covalently attached retinal (the aldehyde of vitamin A), a photoreactive chromophore, via a protonated Schiff base linkage to an amino group of lysine in the middle of the seventh transmembrane helix (TM7). Upon the absorption of light, microbial rhodopsins undergo light-induced photoisomerization of all-trans retinal into the 13-cis isomer, whereas the photoisomerization of 11-cis retinal to all-trans isomer occurs in the animal rhodopsins. While animal visual rhodopsins are activated by light to catalyze GDP/GTP exchange in the alpha subunit of the retinal G protein transducin (Gt), microbial rhodopsins do not activate G proteins, but instead can function as light-dependent ion pumps, cation channels, and sensors
AITTWFWLGALGMLVGTVIFAWLYRSEPSSRRRYYALLAAIPGIAAVAYVLMALGIGTVTVAGRTVFLPR
YVDWLLTTPLLVGYLAYLAGASRRTIAGVVAADAVMIVFGFAAAVTSGTLRWALFGVGAAAFLGLLYLLY
GPFPRSAPADDPRVRSLFRLLRNHTVVLWLAYPVVWLLGPAGVGLLTAEGTALVIAYLDVVAKVGFVYIA
LAAR
>gnl|CDD|320158 cd15030, 7tmF_SMO_homolog, class F smoothened family membrane region, a homolog of frizzled receptors. This group represents smoothened (SMO), a transmembrane G protein-coupled receptor that acts as the transducer of the hedgehog (HH) signaling pathway. SMO is activated by the hedgehog (HH) family of proteins acting on the 12-transmembrane domain receptor patched (PTCH), which constitutively inhibits SMO. Thus, in the absence of HH proteins, PTCH inhibits SMO signaling. On the other hand, binding of HH to the PTCH receptor activates its internalization and degradation, thereby releasing the PTCH inhibition of SMO. This allows SMO to trigger intracellular signaling and the subsequent activation of the Gli family of zinc finger transcriptional factors and induction of HH target gene expression (PTCH, Gli1, cyclin, Bcl-2, etc). SMO is closely related to the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate family of G-protein coupled receptors. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The WNT and HH signaling pathways play critical roles in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
PLFTEDEHRQIHKFIAVFASVCLLCTLFTVLTFFIDWKNSNRYPAVILFYINACFFIGSIGWLAQFLPGA
REDIVCRKDGTMRLGEPSAGENLSCVVIFVLVYYFLMAGCVWFVILTYAWHMSFKALGTIQDRLDKKTAY
FHLIAWSLPLVLTITIMALGQVDGDSVSGICFVGYKNHMYRAGFVLAPVGLVLVIGGYFLVRGLYTLIKL
KISSPEILSEKASSKIRETIVRLGIFAFLALGFVLITFACHVYEFFNQAEWEKSFRDYIVCEANVTIAEQ
TNGDIPECELKSRPSLAMLQLHLLALFGAGIAMSSWVWTRATLETWKRFWR
>gnl|CDD|320159 cd15031, 7tmF_FZD3_insect, class F insect frizzled subfamily 3, member of 7-transmembrane G protein-coupled receptors. This group represents subfamily 3 of the frizzled (FZD) family of seven transmembrane-spanning G protein-coupled proteins that is found in insects such as Drosophila melanogaster. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
AFYTTRQKKLVESWMLVLSAVSFILTLFALVTFWAEPTRFGYPERPVLFMALCYNLISLCYLERGILGTF
TNCSARSLAIDCDDRYLRQDCLLTPQCLASFIITYYLSLSAASWWLIFALCWYLSSAKKWSSEALEKKSG
LFHVLAWVPPLAPPIAALLLERVSASELTGTCTASGFVESSISELPALILLLLGLYLTIAALRSLLSLQQ
QLQSRLAHAPQRILARVSIFSLLYLIPAAAALICKLCERWLQPVPECNALQEDCAPPATDNEFLSALPAL
LRVFFFLIGGTATGLWLWSRKSCESWRSRLV
>gnl|CDD|320160 cd15032, 7tmF_FZD6, class F frizzled subfamily 6, member of 7-transmembrane G protein-coupled receptors. This group includes subfamily 6 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of GPCRs, and its closely related proteins. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
MYFKSDELDFAKSFIGIVSIFCLCATLFTFLTFLIDVKRFRYPERPIIYYSVCYSIVSLMYFIGFLLGNS
TACNKADEKLELGDTVVLGSQNKACTVLFMLLYFFTMAGTIWWVILTITWFLAAGRKWSCEAIEQKALWF
HAVAWGIPGFLTIMLLAMNKVEGDNISGVCFVGLYDLDASRYFVLLPLCLCVFVGLSLLLAGIISLNHVR
QVIQHDGRNQEKLKKFMIRIGVFSGLYLVPLVTLLGCYVYEQVYRRTWEITWVSDHCQQYHIPCPYQAKA
VARPELALFLIKYLMTLIVGISAVFWVGSKKTCSEWASFFN
>gnl|CDD|320161 cd15033, 7tmF_FZD3, class F frizzled subfamily 3, member of 7-transmembrane G protein-coupled receptors. This group includes subfamily 3 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of GPCRs, and its closely related proteins. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
MYFRREELSFARYFIGVISIVCLSATLFTFLTFLIDVTRFRYPERPIIFYAVCYMMVSLIFFIGFLLEDR
VACNAASPGQYKASTVTQGSHNKACTMLFMVLYFFTMAGSVWWVILTITWFLAAVPKWGSEAIEKKALLF
HASAWGIPGTLTIILLAMNKIEGDNISGVCFVGLYDVDALRYFVLAPLCLDVVVGVSLLLAGIISLNRVR
IEIPLEKENQDKLVKFMIRIGVFSVLYLVPLLVVIGCYFYEQAYRGVWETTWVQERCREYHIPCPYKVTQ
TSRPDLILFLMKYLMALVVGIPSVFWVGSKKTCFEWASFFH
>gnl|CDD|320162 cd15034, 7tmF_FZD1_2_7-like, class F frizzled subfamilies 1, 2 and 7; member of 7-transmembrane G protein-coupled receptors. This group includes subfamilies 1, 2 and 7 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of G-protein coupled receptors, as well as their closely related proteins. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
MFFTEKEREFARLWIGIWSVLCAASTLFTVLTFLIDMDRFRYPERPIIFLSGCYFMVSIAYIVGFFLGDK
VACNGPFPPGGPKTVTQGTKKEGCTILFMMLYFFSMASSIWWVILTLTWFLAAGLKWGHEAIEANSQYFH
LAAWAVPAIKTIAILAMGKVDGDVLSGVCFVGLSDVDALRGFVLAPLFVYLLIGTSFLLAGFVSLFRIRT
VMKHDGTKTDKLEKLMVRIGVFSVLYTVPATIVIACYFYEQANRESWEKSWLSQNCKKYEDPCPCPPTPH
PLDRPDFTVFMIKYLMTLIVGITSGFWIWSGKTLQSWRQFYA
>gnl|CDD|320163 cd15035, 7tmF_FZD5_FZD8-like, class F frizzled subfamilies 5, 8 and related proteins; member of 7-transmembrane G protein-coupled receptors. This group includes subfamilies 5 and 8 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of GPCRs, as well as their closely related proteins. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
PFFSEDEKTFATFWIGLWSILCFISTLITVLTFLIDMQRFQYPERPIIFLSFCYFMVSVGYIIRLIVGHE
AVACDGGIIRYATTGPALCTVVFLLTYFFGMASSIWWVILSLTWFLAAGLKWGNEAISSYSQYFHLVAWL
IPAVQTIAILALSAVDGDPISGICYVGNQNLNNLRGFVLAPLVVYLILGTSFLLAGFVSLFRIRNVIKQQ
GGDKTDKLEKLMIRIGIFSVLYTVPATIVIACYFYEQHYREIWEKSLNCPCSPGSIKSRPEYSIFMLKYF
MSLVVGITSGFWIWSGKTLDSWKRFCR
>gnl|CDD|320164 cd15036, 7tmF_FZD9, class F frizzled subfamily 9, member of 7-transmembrane G protein-coupled receptors. This group includes subfamily 9 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of GPCRs, and its closely related proteins. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
VYWSRGDKDFALVWMAVWSTLCFVSTAFTVLTFLLDPHRFQYPERPIIFLSMCYNVYSVAFLIRAVAGAE
SIACDRENGALYIIQEGLESTGCTLVFLILYYFGMASSLWWVVLTLTWFLAAGKKWGHEAIESHGSYFHM
AAWGIPALKTIVILTMRKVAGDELTGLCYVGSMDVSALTGFVLVPLSCYLVTGTSFLLTGFVALFHIRKV
MKTGGTNTEKLEKLMVKIGVFSILYTVPATCVIVCYFYERLNMDYWDLRALEESCRTVPGRRRPDCSLPH
SVPTVAVFMLKIFMSLVVGITSGVWVWSSKTLQTWQGLCC
>gnl|CDD|320165 cd15037, 7tmF_FZD10, class F frizzled subfamily 10, member of 7-transmembrane G protein-coupled receptors. This group includes subfamily 10 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of GPCRs, and its closely related proteins. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
VYWSKDDKRFAVVWIAIWSILCFFSSAFTVLTFLIDPQRFKYPERPIIFLSMCYCVYSVGYIIRLFAGAE
SIACDRDSGQLYVIQEGLESTGCTIVFLILYYFGMASSLWWVILTLTWFLAAGKKWGHEAIEANSSYFHL
AAWAIPAVKTIMILVMRRVAGDELTGVCYVGSMDVNALTGFVLIPLACYLIIGTSFILSGFVALFHIRRV
MKTGGENTDKLEKLMVRIGVFSVLYTVPATCVIACYFYERLNMDYWKILATQQKCKMDNQTKTLDCVMTS
SIPAVEIFMVKIFMLLVVGITSGMWIWTSKTLQSWQNVFS
>gnl|CDD|320166 cd15038, 7tmF_FZD4, class F frizzled subfamily 4, member of 7-transmembrane G protein-coupled receptors. This group includes subfamily 4 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of GPCRs, and its closely related proteins. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
GLFTQSDKEFADIWMAIWAGLCFISTLFTVLTFLIDSGRFKYPERPIIFLSMCYNIYSIAYIVRLLAGRE
SISCDLDSQTAVSILIQEGLENTGCAIVFLLLYFFGMASSIWWVILTLTWFLAAGLKWGHEAIQMHSSYF
HIAAWALPAVKTIVILVMRVVDADELTGLCYVGNQNLDALLGFVVAPLFTYLVIGTLFLIAGFVALFRIR
SQLQRDGTKTDKLERLMVRIGIFSVLYTVPATCVIACYFYEYSNRDLWYYGGSAARPNMEVFMLKIFMSL
VVGITSGMWIWSAKTLSSWRNFFN
>gnl|CDD|410632 cd15039, 7tmB3_Methuselah-like, Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G protein-coupled receptors. The subfamily B3 of class B GPCRs consists of Methuselah (Mth) and its closely related proteins found in bilateria. Mth was originally identified in Drosophila as a GPCR affecting stress resistance and aging. In addition to the seven transmembrane helices, Mth contains an N-terminal extracellular domain involved in ligand binding, and a third intracellular loop (IC3) required for the specificity of G-protein coupling. Drosophila Mth mutants showed an increase in average lifespan by 35% and greater resistance to a variety of stress factors, including starvation, high temperature, and paraquat-induced oxidative toxicity. Moreover, mutations in two endogenous peptide ligands of Methuselah, Stunted A and B, showed an increased in lifespan and resistance to oxidative stress induced by dietary paraquat. These results strongly suggest that the Stunted-Methuselah system plays important roles in stress response and aging
SSILGILTLIGLIISLVFLLLTLAVYALLPELRNLHGKCLMCLVLSLFVAYLLLLIGQLLSSGDSTLCVA
LGILLHFFFLAAFFWLNVMSFDIWRTFRGKRSSSSRSKERKRFLRYSLYAWGVPLLLVAVTIIVDFSPNT
DSLRPGYGEGSCWISNPWALLLYFYGPVALLLLFNIILFILTAIRIRKVKKETAKVQSRLRSDKQRFRLY
LKLFVIMGVTWILEIISWFVGGSSVLWYIFDILNGLQGVFIFLIFVCKRRVLRLLKKKIR
>gnl|CDD|320168 cd15040, 7tmB2_Adhesion, adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G protein-coupled receptors. The B2 subfamily of class B GPCRs consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
EKALSIITYIGCGLSLLGLLLTIITYILFRKLRKRKPTKILLNLCLALLLANLLFLFGINSTDNPVLCTA
VAALLHYFLLASFMWMLVEALLLYLRLVKVFGTYPRHFILKYALIGWGLPLIIVIITLAVDPDSYGNSSG
YCWLSNGNGLYYAFLGPVLLIILVNLVIFVLVLRKLLRLSAKRNKKKRKKTKAQLRAAVSLFFLLGLTWI
FGILAIFGARVVFQYLFAIFNSLQGFFIFIFHCLRNKEVRKAW
>gnl|CDD|341321 cd15041, 7tmB1_hormone_R, The subfamily B1 of hormone receptors (secretin-like), member of the class B family seven-transmembrane G protein-coupled receptors. The B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of this subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. Moreover, the B1 subfamily receptors play key roles in hormone homeostasis and are promising drug targets in various human diseases including diabetes, osteoporosis, obesity, neurodegenerative conditions (Alzheimer###s and Parkinson's), cardiovascular disease, migraine, and psychiatric disorders (anxiety, depression). Furthermore, the subfamilies B2 and B3 consist of receptors that are capable of interacting with epidermal growth factors (EGF) and the Drosophila melanogaster Methuselah gene product (Mth), respectively. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes
LLVVYYIYLVGYSLSLVALLPAIVIFLYFRSLRCTRIRLHINLFLSFILRAVFWIIWDLLVVYDRLTSSG
VETVLMQNPVGCKLLSVLKRYFKSANYFWMLCEGLYLHRLIVVAFFSEPSSLKLYYAIGWGLPLVIVVIW
AIVRALLSNESCWISYNNGHYEWILYGPNLLALLVNLFFLINILRILLTKLRSHPNAEPSNYRKAVKATL
ILIPLFGIQYLLTIYRPPDGSEGELVYEYFNAILNSSQGFFVAVIYCFLNGEVQSELKRKWSR
>gnl|CDD|320170 cd15042, 7tmC_Boss, Bride of sevenless, member of the class C family of seven-transmembrane G protein-coupled receptors. Bride of Sevenless (Boss) is a putative Drosophila melanogaster G protein-coupled receptor that functions as a glucose-responding receptor to regulate energy metabolism. Boss is expressed predominantly in the fly's fat body, a nutrient-sensing tissue functionally analogous to the mammalian liver and adipose tissues, and in photoreceptor cells. Boss, which is expressed on the surface of R8 photoreceptor cell, binds and activates the Sevenless receptor tyrosine kinase on the neighboring R7 precursor cell. Activation of Sevenless results in phosphorylation of the Sevenless, triggering a signaling transduction cascade through Ras pathway that ultimately leads to the differentiation of the R7 precursor into a fully functional R7 photoreceptor, the last of eight photoreceptors to differentiate in each ommatidium of the developing Drosophila eye. In the absence of either of Sevenless or Boss, the R7 precursor fails to differentiate as a photoreceptor and instead develops into a non-neuronal cone cell. Moreover, Boss mutants in Drosophila showed elevated food intake, but reduced stored triglyceride levels, suggesting that Boss may play a role in regulating energy homeostasis in nutrient sensing tissues. Furthermore, GPRC5B, a mammalian Boss homolog, activates obesity-associated inflammatory signaling in adipocytes, and that the GPRC5B knockout mice showed resistance to high-fat diet-induced obesity and insulin resistance
VWVPAFLTAAILGILFCCAILVFIVVRVTTKDVLEGNPVLTILLLLALIFTFLSFLPFSMEDDYFGKNSL
CAVRILLTTLAFGFTFSLMLSRALFLALSTGEGGFLSHVNGYLQSVMCLFSFGVQVAMSVQYFVLNHANS
AVIYRGLWFIALLGYDIFLLIALFVLCPFIFRSQRNYREGKYFFGASIGLLVIWVIWLPCFLLMGPEWRD
AVISFGLVATAYAILVGILVPRTYLMTR
>gnl|CDD|320171 cd15043, 7tmC_RAIG_GPRC5, retinoic acid-inducible orphan G-protein-coupled receptors; class C family of seven-transmembrane G protein-coupled receptors, group 5. Retinoic acid-inducible G-protein-coupled receptors (RAIGs), also referred to as GPCR class C group 5, are a group consisting of four orphan receptors RAIG1 (GPRC5A), RAIG2 (GPRC5B), RAIG3 (GPRC5C), and RAIG4 (GPRC5D). Unlike other members of the class C GPCRs which contain a large N-terminal extracellular domain, RAIGs have a shorter N-terminus. Thus, it is unlikely that RAIGs bind an agonist at its N-terminus domain. Instead, agonists may bind to the seven-transmembrane domain of these receptors. In addition, RAIG2 and RAIG3 contain a cleavable signal peptide whereas RAIG1 and RAIG4 do not. Although their expression is induced by retinoic acid (vitamin A analog), their biological function is not clearly understood. To date, no ligand is known for the members of RAIG family. Three receptor types (RAIG1-3) are found in vertebrates, while RAIG4 is only present in mammals. They show distinct tissue distribution with RAIG1 being primarily expressed in the lung, RAIG2 in the brain and placenta, RAIG3 in the brain, kidney and liver, and RAIG4 in the skin. RAIG1 is evolutionarily conserved from mammals to fish. RAIG1 has been to shown to act as a tumor suppressor in non-small cell lung carcinoma as well as oral squamous cell carcinoma, but it could also act as an oncogene in breast cancer, colorectal cancer, and pancreatic cancer. Studies have shown that overexpression of RAIG1 decreases intracellular cAMP levels. Moreover, knocking out RAIG1 induces the activation of the NF-kB and STAT3 signaling pathways leading to cell proliferation and resistance to apoptosis. RAIG2 (GPRC5B), a mammalian Boss (Bride of sevenless) homolog, activates obesity-associated inflammatory signaling in adipocytes, and GPRC5B knockout mice show resistance to high-fat diet-induced obesity and insulin resistance. The specific functions of RAIG3 and RAIG4 are unknown; however, they may play roles in mediating the effects of retinoic acid on embryogenesis, differentiation, and tumorigenesis through interactions with G-protein signaling pathways
AWGIVLEAVAGAGVVTTVALMLILPILLPFVQDSNKRSMLGTQFLFLLGTLGLFGLTFAFIIGLDGSTCP
TRRFLFGVLFAICFSCLLAHAVSLTKLVRGRKGPSGWVILGLALGLSLVQVIIAIEWLVLTMNRTNVNVF
SELSCARRNMDFVMALIYVMFLLALTFLMASFTLCGSFKRWKRHGAFILLTMLLSVAIWVAWITMYMLGN
VLQFDRRWDDPTLAIALAANGWVFVLFYVIPEFWLLTK
>gnl|CDD|320172 cd15044, 7tmC_V2R_AA_sensing_receptor-like, vomeronasal type-2 pheromone receptors, amino acid-sensing receptors and closely related proteins; member of the class C family of seven-transmembrane G protein-coupled receptors. This group is composed of vomeronasal type-2 pheromone receptors (V2Rs), a subgroup of broad-spectrum amino-acid sensing receptors including calcium-sensing receptor (CaSR) and GPRC6A, as well as their closely related proteins. Members of the V2R family of vomeronasal GPCRs are involved in detecting protein pheromones for social and sexual cues between the same species. V2Rs and G-alpha(o) protein are co-expressed in the basal layer of the vomeronasal organ (VNO), which is the sensory organ of the accessory olfactory system present in amphibians, reptiles, and non-primate mammals such as mice and rodents, but it is non-functional or absent in humans, apes, and monkeys. On the other hand, members of the V1R receptor family and G-alpha(i2) protein are co-expressed in the apical neurons of the VNO. Activation of V1R or V2R causes activation of phospholipase pathway, producing the second messengers diacylglycerol (DAG) and IP3. However, in contrast to V1Rs, V2Rs contain the long N-terminal extracellular domain, which is believed to bind pheromones. CaSR is a widely expressed GPCR that is involved in sensing small changes in extracellular levels of calcium ion to maintain a constant level of the extracellular calcium via modulating the synthesis and secretion of calcium regulating hormones, such as parathyroid hormone (PTH), in order to regulate Ca(2+)transport into or out of the extracellular fluid via kidney, intestine, and/or bone. For instance, when Ca2+ is high, CaSR downregulates PTH synthesis and secretion, leading to an increase in renal Ca2+ excretion, a decrease in intestinal Ca2+ absorption, and a reduction in release of skeletal Ca2+. GRPC6A (GPCR, class C, group 6, subtype A) is a widely expressed amino acid-sensing GPCR that is most closely related to CaSR. GPRC6A is most potently activated by the basic amino acids L-arginine, L-lysine, and L-ornithine and less potently by small aliphatic amino acids. Moreover, the receptor can be either activated or modulated by divalent cations such as Ca2+. GPRC6A is expressed in the testis, but not the ovary and specifically also binds to the osteoblast-derived hormone osteocalcin (OCN), which regulates testosterone production by the testis and male fertility independently of the hypothalamic-pituitary axis. Furthermore, GPRC6A knockout studies suggest that GRPC6A is involved in regulation of bone metabolism, male reproduction, energy homeostasis, glucose metabolism, and in activation of inflammation response, as well as prostate cancer growth and progression, among others
PLGILLVILSILGIIFVLVVGGVFVRYRNTPIVKANNRELSYLILLSLFLCFSSSLFFIGEPQDWTCKLR
QTMFGVSFTLCISCILTKTLKVLLAFSADKPLTQKFLMCLYLPILIVFTCTGIQVVICTVWLIFAPPTVE
VNVSPLPRVIILECNEGSILAFGTMLGYIAFLAFLCFLFAFKARKLPDNYNEAKFITFGMLVFFIVWISF
VPAYLSTKGKFVVAVEIIAILASSYGLLGCIFLPKCYVILL
>gnl|CDD|320173 cd15045, 7tmC_mGluRs, metabotropic glutamate receptors, member of the class C family of seven-transmembrane G protein-coupled receptors. The metabotropic glutamate receptors (mGluRs) are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group I mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to (Gi/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity
PWAIGAMAFASLGILLTLFVLVVFVRYRDTPVVKASGRELSYVLLAGILLSYVMTFVLVAKPSTIVCGLQ
RFGLGLCFTVCYAAILTKTNRIARIFRLGKKSAKRPRFISPRSQLVITGLLVSVQVLVLAVWLILSPPRA
THHYPTRDKNVLVCSSALDASYLIGLAYPILLIILCTVYAFKTRKIPEGFNEAKYIGFTMYTTCIIWLAF
VPLYFTTASNIEVRITTLSVSISLSATVQLACLFAPKVYIILF
>gnl|CDD|320174 cd15046, 7tmC_TAS1R, type 1 taste receptors, member of the class C of seven-transmembrane G protein-coupled receptors. This subfamily represents the type I taste receptors (TAS1Rs) that belongs to the class C family of G protein-coupled receptors. The functional TAS1Rs are obligatory heterodimers built from three known members, TAS1R1-3. TAS1R1 combines with TAS1R3 to form an umami taste receptor, which is responsible for the perception of savory taste, such as the food additive mono-sodium glutamate (MSG); whereas the combination of TAS1R2-TAS1R3 forms a sweet-taste receptor for sugars and D-amino acids. On the other hand, the type II taste receptors (TAS2Rs), which belong to the class A family of GPCRs, recognize bitter tasting compounds. In the case of sweet, for example, the TAS1R2-TAS1R3 heterodimer activates phospholipase C (PLC) via alpha-gustducin, a heterodimeric G protein that is involved in perception of sweet and bitter tastes. This activation leads to generation of inositol (1, 4, 5)-trisphosphate (IP3) and diacylglycerol (DAG), and consequently increases intracellular Ca2+ mobilization and activates a cation channel, TRPM5. In contrast to the TAS1R2-TAS1R3 heterodimer, TAS1R3 alone could activate adenylate cyclase leading to cAMP formation in the absence of alpha-gustducin. Each TAS1R contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD) and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TAS1R receptors
APTVAVLLLAALGLLSTLAILVIFWRNFNTPVVRSAGGPMCFLMLTLLLVAYMSVPVYFGPPKVSTCLLR
QALFPLCFTVCLACIAVRSFQIVCIFKMASRFPRAYSYWVKYHGPYVSIAFITVLKMVIVVIGMLATPPS
PTTDTDPDPKITIVSCNPNYRNSSLFNTSLDLLLSVVCFSFSYMGKDLPTNYNEAKFITFSLTFYFTSWI
SFCTFMLAYSGVLVTIVDLLATLLSLLAFSLGYFLPKCYIILF
>gnl|CDD|320175 cd15047, 7tmC_GABA-B-like, gamma-aminobutyric acid type B receptor and related proteins, member of the class C family of seven-transmembrane G protein-coupled receptors. The type B receptor for gamma-aminobutyric acid, GABA-B, is activated by its endogenous ligand GABA, the principal inhibitory neurotransmitter. The functional GABA-B receptor is an obligatory heterodimer composed of two related subunits, GABA-B1, which is primarily involved in GABA ligand binding, and GABA-B2, which is responsible for both G-protein coupling and trafficking of the heterodimer to the plasma membrane. Activation of GABA-B couples to G(i/o)-type G proteins, which in turn modulate three major downstream effectors: adenylate cyclase, voltage-sensitive Ca2+ channels, and inwardly-rectifying K+ channels. Consequently, GABA-B receptor produces slow and sustained inhibitory responses by decreased neurotransmitter release via inhibition of Ca2+ channels and by postsynaptic hyperpolarization via the activation of K+ channels through the G-protein beta-gamma dimer. The GABA-B is expressed in both pre- and postsynaptic sites of glutamatergic and GABAergic neurons in the brain where it regulates synaptic activity. Thus, the GABA-B receptor agonist, baclofen, is used to treat muscle tightness and cramping caused by spasticity in multiple sclerosis patients. Moreover, GABA-B antagonists improves cognitive performance in mammals, while GABA-B agonists suppress cognitive behavior. In most of the class C family members, the extracellular Venus-flytrap domain in the N-terminus is connected to the seven-transmembrane (7TM) via a cysteine-rich domain (CRD). However, in the GABA-B receptor, the CRD is absent in both subunits and the Venus-flytrap ligand-binding domain is directly connected to the 7TM via a 10-15 amino acids linker, suggesting that GABA-B receptor may utilize a different activation mechanism. Also included in this group are orphan receptors, GPR156 and GPR158, which are closely related to the GABA-B receptor family
PLFIVFTVLSGIGILLALVFLIFNIKFRKNRVIKMSSPLFNNLILLGCILCYISVILFGLDDSKPSSFLC
TARPWLLSIGFTLVFGALFAKTWRIYRIFTNKKLKRIVIKDKQLLKIVGILLLIDIIILILWTIVDPLKP
TRVLVLSEISDDVKYEYVVHCCSSSNGIIWLGILLAYKGLLLLFGCFLAWKTRNVDIEEFNESKYIGISI
YNVLFLSVIGVPLSFVLTDSPDTSYLIISAAILFCTTATLCLLFVPKFWLLKR
>gnl|CDD|320176 cd15048, 7tmA_Histamine_H3R_H4R, histamine receptor subtypes H3R and H4R, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes histamine subtypes H3R and H4R, members of the histamine receptor family, which belong to the class A of GPCRs. Histamine plays a key role as chemical mediator and neurotransmitter in various physiological and pathophysiological processes in the central and peripheral nervous system. Histamine exerts its functions by binding to four different G protein-coupled receptors (H1-H4). The H3 and H4 receptors couple to the G(i)-proteins, which leading to the inhibition of cAMP formation. The H3R receptor functions as a presynaptic autoreceptors controlling histamine release and synthesis. The H4R plays an important role in histamine-mediated chemotaxis in mast cells and eosinophils. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
IVLAVLISVLILVTVIGNLLVILAFIKDKKLRTVSNFFLLNLAVADFLVGLVSMPFYIPYTLTGKWPFGK
VFCKAWLVVDYTLCTASALTIVLISLDRYLSVTKAVKYRAKQTKRRTVLLMALVWILAFLLYGPAIIGWD
LWTGYSIVPTGDCEVEFFDHFYFTFITSVLEFFIPFISVSFFNLLIYLNIRKRSRRRPLRSVPILPASQN
PSRARSQREQVKLRRDRKAAKSLAILVLVFLICWAPYTILTIIRSFCSGSCVDSYLYEFTFWLLWTNSAI
NPFLYAACHPRFRKAF
>gnl|CDD|341322 cd15049, 7tmA_mAChR, muscarinic acetylcholine receptor subfamily, member of the class A family of seven-transmembrane G protein-coupled receptors. Muscarinic acetylcholine receptors (mAChRs) regulate the activity of many fundamental central and peripheral functions. The mAChR family consists of 5 subtypes M1-M5, which can be further divided into two major groups according to their G-protein coupling preference. The M1, M3 and M5 receptors selectively interact with G proteins of the G(q/11) family, whereas the M2 and M4 receptors preferentially link to the G(i/o) types of G proteins. Activation of mAChRs by agonist (acetylcholine) leads to a variety of biochemical and electrophysiological responses. In general, the exact nature of these responses and the subsequent physiological effects mainly depend on the molecular and pharmacological identity of the activated receptor subtype(s). All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VLICIATGSLSLVTVGGNILVILSFRVNRQLRTVNNYFLLSLACADLIIGLVSMNLYTVYLVMGYWPLGP
LLCDLWLALDYVASNASVMNLLLISFDRYFSVTRPLTYRAKRTPKRAILMIALAWVISFVLWAPAILGWQ
YFVGERTVPDGQCYIQFLDDPAITFGTAIAAFYLPVLVMTILYWRIYRETARERKAARTLSAILLAFIIT
WTPYNILVLVSTFCAKCIPDTLWSFGYWLCYINSTINPFCYALCNKTFRKTF
>gnl|CDD|320178 cd15050, 7tmA_Histamine_H1R, histamine subtype H1 receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes histamine receptor subtype H1R, a member of histamine receptor family, which belongs to the class A of GPCRs. Histamine plays a key role as chemical mediator and neurotransmitter in various physiological and pathophysiological processes in the central and peripheral nervous system. Histamine exerts its functions by binding to four different G protein-coupled receptors (H1-H4). H1R selectively interacts with the G(q)-type G protein that activates phospholipase C and the phosphatidylinositol pathway. Antihistamines, a widely used anti-allergy medication, act on the H1 subtype and produce drowsiness as a side effect. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
APLGIALSTISLITVILNLLVLYAVRTERKLHTVGNLYIVSLSVADLIVGAVVMPLNIVYLLESKWILGR
PVCLFWLSMDYVASTASIFSLFILCIDRYRSVQQPLKYLKYRTKTRASLMISGAWLLSFLWVIPILGWHH
FARGGERVVLEDKCETDFHDVTWFKVLTAILNFYIPSLLMLWFYAKIFKAVNRERKAAKQLGFIMAAFIL
CWIPYFILFMVIAFCKNCCNENLHMFTIWLGYINSTLNPFIYPLCNENFKKTF
>gnl|CDD|320179 cd15051, 7tmA_Histamine_H2R, histamine subtype H2 receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes histamine receptor subtype H2R, a member of histamine receptor family, which belongs to the class A of GPCRs. Histamine plays a key role as chemical mediator and neurotransmitter in various physiological and pathophysiological processes in the central and peripheral nervous system. Histamine exerts its functions by binding to four different G protein-coupled receptors (H1-H4). The H2R subtype selectively interacts with the G(s)-type G protein that activates adenylate cyclase, leading to increased cAMP production and activation of Protein Kinase A. H2R is found in various tissues such as the brain, stomach, and heart. Its most prominent role is in histamine-induced gastric acid secretion. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
IVLGVVLAVIILLTVIGNVLVCLAVAVNRRLRNLTNYFIVSLAVTDLLLGLLVLPFSAIYELRGEWPLGP
VFCNIYISLDVMLCTASILNLFAISLDRYLAITAPLRYPSRVTPRRVAIALAAIWVVSLAVSFLPIHLGW
NTPDGRVQNGDTPNQCRFELNPPYVLLVAIGTFYLPLLIMCGVYLRIFRIAREQAKRINALTPASTANSS
KSAATAREHKATVTLAAVLGAFIICWFPYFTYFTYRGLCGDNINETALSVVLWLGYANSALNPILYAFLN
RDFRRAF
>gnl|CDD|320180 cd15052, 7tmA_5-HT2, serotonin receptor subtype 2, member of the class A family of seven-transmembrane G protein-coupled receptors. The 5-HT2 receptors are a subfamily of serotonin receptors that bind the neurotransmitter serotonin (5HT; 5-hydroxytryptamine) in the central nervous system (CNS). The 5-HT2 subfamily is composed of three subtypes that mediate excitatory neurotransmission: 5-HT2A, 5-HT2B, and 5-HT2C. They are selectively linked to G proteins of the G(q/11) family and activate phospholipase C, which leads to activation of protein kinase C and calcium release. In the CNS, serotonin is involved in the regulation of appetite, mood, sleep, cognition, learning and memory, as well as implicated in diseases such as migraine, schizophrenia, and depression. Indeed, 5-HT2 receptors are attractive targets for a variety of psychoactive drugs, ranging from atypical antipsychotic drugs, antidepressants, and anxiolytics, which have an antagonistic action on 5-HT2 receptors, to hallucinogens, which act as agonists at postsynaptic 5-HT2 receptors. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
NWAALLLLLLVIATIGGNILVCLAISLEKRLQNVTNYFLMSLAIADLLVGLLVMPLSILTELFGGVWPLP
LVLCLLWVTLDVLFCTASIMHLCTISLDRYMAIRYPLRTRRNKSRTTVFLKIAIVWLISIGISSPIPVLG
IIDTTNVLNNGTCVLFNPNFVIYGSIVAFFIPLLIMVVTYALTIRLLSNEQKASKVLGIVFAVFVICWCP
FFITNILTGLCEECNCRISPWLLSVFVWLGYVSSTINPIIYTIFNKTFRRAF
>gnl|CDD|320181 cd15053, 7tmA_D2-like_dopamine_R, D2-like dopamine receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Dopamine receptors are members of the class A G protein-coupled receptors that are involved in many neurological processes in the central nervous system (CNS). The neurotransmitter dopamine is the primary endogenous agonist for dopamine receptors. Dopamine receptors consist of at least five subtypes: D1, D2, D3, D4, and D5. The D1 and D5 subtypes are members of the D1-like family of dopamine receptors, whereas the D2, D3 and D4 subtypes are members of the D2-like family. The D1-like family receptors are coupled to G proteins of the G(s) family, which activate adenylate cyclase, causing cAMP formation and activation of protein kinase A. In contrast, activation of D2-like family receptors is linked to G proteins of the G(i) family, which inhibit adenylate cyclase. Dopamine receptors are major therapeutic targets for neurological and psychiatric disorders such as drug abuse, depression, schizophrenia, or Parkinson's disease
NYWALFLLLLPLLTVFGNVLVIMSVFRERSLQTATNYFIVSLAVADLLVAILVMPFAVYVEVNGGKWYLG
PILCDIYIAMDVMCSTASIFNLCAISIDRYIAVTQPIKYARQKNSKRVLLTIAIVWVVSAAIACPLLFGL
NNVPYRDPEECRFYNPDFIIYSSISSFYIPCIVMLLLYYRIFRALRREKKATKTLAIVLGVFLFCWLPFF
TLNILNAICPKLQNQSCHVGPALFSLTTWLGYVNSFLNPIIYTIFNIEFRKAF
>gnl|CDD|320182 cd15054, 7tmA_5-HT6, serotonin receptor subtype 6, member of the class A family of seven-transmembrane G protein-coupled receptors. The 5-HT6 receptors are a subfamily of serotonin receptors that bind the neurotransmitter serotonin (5HT; 5-hydroxytryptamine) in the mammalian central nervous system (CNS). 5-HT6 receptors are selectively linked to G proteins of the G(s) family, which positively stimulate adenylate cyclase, causing cAMP formation and activation of protein kinase A. The 5-HT6 receptors mediates excitatory neurotransmission and are involved in learning and memory; thus they are promising targets for the treatment of cognitive impairment. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
GWVAAFLCLIILLTVAGNSLLILLIFTQRSLRNTSNYFLVSLFMSDLMVGLVVMPPAMLNALYGRWVLAR
DFCPIWYAFDVMCCSASILNLCVISLDRYLLIISPLRYKLRMTPPRALALILAAWTLAALASFLPIELGW
HELGHERTLPNLTSGTVEGQCRLLVSLPYALVASCLTFFLPSGAICFTYCRILLAARKALKASLTLGILL
GMFFVTWLPFFVANVVQAVCDCVSPGLFDVLTWLGYCNSTMNPIIYPLFMRDFKRAL
>gnl|CDD|320183 cd15055, 7tmA_TAARs, trace amine-associated receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. The trace amine-associated receptors (TAARs) are a distinct subfamily within the class A G protein-coupled receptor family. Trace amines are endogenous amines of unknown function that have strong structural and metabolic similarity to classical monoamine neurotransmitters (serotonin, noradrenaline, adrenaline, dopamine, and histamine), which play critical roles in human and animal physiological activities such as cognition, consciousness, mood, motivation, perception, and autonomic responses. However, trace amines are found in the mammalian brain at very low concentrations compared to classical monoamines. Trace amines, including p-tyramine, beta-phenylethylamine, and tryptamine, are also thought to act as chemical messengers to exert their biological effects in vertebrates. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VLLYIVLSSISLLTVLGNLLVIISISHFKQLHTPTNLLLLSLAVADFLVGLLVMPFSMIRSIETCWYFGD
TFCKLHSSLDYILTSASIFNLVLIAIDRYVAVCDPLLYPTKITIRRVKICICLCWFVSALYSSVLLYDNL
NQPGLIRYNSCYGECVVVVNFIWGVVDLVLTFILPCTVMIVLYMRIFVVARSQARAIRSHTAQVSLEGSS
KKVSKKSERKAAKTLGIVVGVFLLCWLPYYIVSLVDPYISTPSSVFDVLIWLGYFNSCLNPLIYALFYPW
FRKAL
>gnl|CDD|320184 cd15056, 7tmA_5-HT4, serotonin receptor subtype 4, member of the class A family of seven-transmembrane G protein-coupled receptors. The 5-HT4 subtype is a member of the serotonin receptor family that belongs to the class A G protein-coupled receptors, and binds the neurotransmitter serotonin (5HT; 5-hydroxytryptamine) in the mammalian central nervous system (CNS). 5-HT4 receptors are selectively linked to G proteins of the G(s) family, which positively stimulate adenylate cyclase, causing cAMP formation and activation of protein kinase A. 5-HT4 receptor-specific agonists have been shown to enhance learning and memory in animal studies. Moreover, hippocampal 5-HT4 receptor expression has been reported to be inversely correlated with memory performance in humans. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VVLSTFLSLVILLTILGNLLVIVAVCTDRQLRKKTNYFVVSLAVADLLVAVLVMPFGAIELVNNRWIYGE
TFCLVRTSLDVLLTTASIMHLCCIALDRYYAICCQPLVYKMTPLRVAVMLGGCWVIPTFISFLPIMQGWN
HIGIEDLIAFNCASGSTSCVFMVNKPFAIICSTVAFYIPALLMVLAYYRIYVAAREQAHQIRSLQRAGSS
NHEADQHRNSRMRTETKAAKTLGIIMGCFCVCWAPFFVTNIVDPFIGYRVPYLLWTAFLWLGYINSGLNP
FLYAFFNKSFRRAF
>gnl|CDD|320185 cd15057, 7tmA_D1-like_dopamine_R, D1-like family of dopamine receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Dopamine receptors are members of the class A G protein-coupled receptors that are involved in many neurological processes in the central nervous system (CNS). The neurotransmitter dopamine is the primary endogenous agonist for dopamine receptors. Dopamine receptors consist of at least five subtypes: D1, D2, D3, D4, and D5. The D1 and D5 subtypes are members of the D1-like family of dopamine receptors, whereas the D2, D3 and D4 subtypes are members of the D2-like family. The D1-like family receptors are coupled to G proteins of the G(s) family, which activate adenylate cyclase, causing cAMP formation and activation of protein kinase A. In contrast, activation of D2-like family receptors is linked to G proteins of the G(i) family, which inhibit adenylate cyclase. Dopamine receptors are major therapeutic targets for neurological and psychiatric disorders such as drug abuse, depression, schizophrenia, or Parkinson's disease. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
IITGCILYLLVLLTLLGNALVIAAVLRFRHLRSKVTNYFIVSLAVSDLLVAILVMPWAAVNEVAGYWPFG
SFCDVWVSFDIMCSTASILNLCVISVDRYWAISSPFRYERRMTRRRAFIMIAVAWTLSALISFIPVQLGW
HRADDTSEALALYADPCQCDSSLNRTYAISSSLISFYIPVAIMIVTYTRIYRIARRQIRRIAALERAAQE
STNPDSSLRSSLRRETKALKTLSIIMGVFVCCWLPFFILNCVLPFCDLRTAQFPCVPDTTFIVFVWLGWA
NSSLNPIIYAFNADFRKAF
>gnl|CDD|320186 cd15058, 7tmA_Beta_AR, beta adrenergic receptors (adrenoceptors), member of the class A family of seven-transmembrane G protein-coupled receptors. The beta adrenergic receptor (beta adrenoceptor), also known as beta AR, is activated by hormone adrenaline (epinephrine) and plays important roles in regulating cardiac function and heart rate, as well as pulmonary physiology. The human heart contains three subtypes of the beta AR: beta-1 AR, beta-2 AR, and beta-3 AR. Beta-1 AR and beta-2 AR, which expressed at about a ratio of 70:30, are the major subtypes involved in modulating cardiac contractility and heart rate by positively stimulating the G(s) protein-adenylate cyclase-cAMP-PKA signaling pathway. In contrast, beta-3 AR produces negative inotropic effects by activating inhibitory G(i) proteins. The aberrant expression of beta-ARs can lead to cardiac dysfunction such as arrhythmias or heart failure. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
PGLLLLLALIILAIVVGNLLVIIAIARTSRLQTMTNIFITSLACADLVMGLLVVPLGATIVVTGKWQLGN
FWCELWTSVDVLCVTASIETLCVIAVDRYIAITRPLRYQVLLTKRRARVIVCVVWIVSALVSFVPIMNQW
WRANDPEANDCYQDPTCCDFRTNMAYAIASSVVSFYIPLLIMIFVYARVFLIATRQLQLIDKRRLRFQSE
CPAPQTTSPEGKRSSGRRPSRLTVVKEHKALKTLGIIMGTFTLCWLPFFIANIINVFNRNLPPGEVFLLL
NWLGYINSGLNPIIYCRSPEFRTAF
>gnl|CDD|320187 cd15059, 7tmA_alpha2_AR, alpha-2 adrenergic receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. The alpha-2 adrenergic receptors (or adrenoceptors) are a subfamily of the class A rhodopsin-like GPCRs that share a common architecture of seven transmembrane helices. This subfamily consists of three highly homologous receptor subtypes that have a key role in neurotransmitter release: alpha-2A, alpha-2B, and alpha-2C. In addition, a fourth subtype, alpha-2D is present in ray-finned fishes and amphibians, but is not found in humans. The alpha-2 receptors are found in both central and peripheral nervous system and serve to produce inhibitory functions through the G(i) proteins. Thus, the alpha-2 receptors inhibit adenylate cyclase, which decreases cAMP production and thereby decreases calcium influx during the action potential. Consequently, lowered levels of calcium will lead to a decrease in neurotransmitter release by negative feedback. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VAISSIVSVVILLIIVGNVLVIVAVLTSRKLRAPQNWFLVSLAVADILVGLLIMPFSLVNELMGYWYFGS
VWCEIWLALDVLFCTASIVNLCAISLDRYWSVTQAVEYNLKRTPRRAKAMIAAVWIISAVISLPPLFGWK
DEQPWHGAEPQCELSDDPGYVLFSSIGSFYIPLLIMIIVYARIYRAAKRKERRFTLVLGVVMGAFVLCWL
PFFFTYPLVVVCKTCGVPELLFKFFFWLGYCNSALNPVIYTIFNKDFRRAF
>gnl|CDD|320188 cd15060, 7tmA_tyramine_octopamine_R-like, tyramine/octopamine receptor-like, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes tyramine/octopamine receptors and similar proteins found in insects and other invertebrates. Both octopamine and tyramine mediate their actions via G protein-coupled receptors (GPCRs) and are the invertebrate equivalent of vertebrate adrenergic neurotransmitters. In Drosophila, octopamine is involved in ovulation by mediating an egg release from the ovary, while a physiological role for tyramine in this process is not fully understood. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VVTTILLSVIIAFTIVGNILVILSVFTYRPLRIVQNFFIVSLAVADLAVAIFVLPLNVAYFLLGKWLFGI
HLCQMWLTCDILCCTASILNLCAIALDRYWAIHDPINYAQKRTLKRVLLMIVVVWALSALISVPPLIGWN
DWPENFTETTPCTLTEEKGYVIYSSSGSFFIPLLIMTIVYVKIFIATSKERRAARTLGIIMGVFVVCWLP
FFLMYVILPFCETCSPSAKVVNFITWLGYVNSALNPVIYTIFNLDFRRAF
>gnl|CDD|320189 cd15061, 7tmA_tyramine_R-like, tyramine receptors and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes tyramine-specific receptors and similar proteins found in insects and other invertebrates. These tyramine receptors form a distinct receptor family that is phylogenetically different from the other tyramine/octopamine receptors which also found in invertebrates. Both octopamine and tyramine mediate their actions via G protein-coupled receptors (GPCRs) and are the invertebrate equivalent of vertebrate adrenergic neurotransmitters. In Drosophila, octopamine is involved in ovulation by mediating an egg release from the ovary, while a physiological role for tyramine in this process is not fully understood. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
ILISFLILAIIFTIFGNLLVILAVATTRRLRTITNCYIVSLATADLLVGVLVLPLAIIRQLLGYWPLGSH
LCDFWISLDVLLCTASILNLCCISLDRYFAITYPLKYRTKRSRRLAITMILAVWVISLLITSPPLVGPSW
HGRRGLGSCYYTYDKGYRIYSSMGSFFLPLLLMLFVYLRIFRVIAKERKTAKTLAIVVGCFIVCWLPFFI
MYLIEPFCDCQFSEALSTAFTWLGYFNSVINPFIYAFYNKDFRRAF
>gnl|CDD|320190 cd15062, 7tmA_alpha1_AR, alpha-1 adrenergic receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. The alpha-1 adrenergic receptors (or adrenoceptors) are a subfamily of the class A rhodopsin-like GPCRs that share a common architecture of seven transmembrane helices. This subfamily consists of three highly homologous receptor subtypes that primarily mediate smooth muscle contraction: alpha-1A, alpha-1B, and alpha-1D. Activation of alpha-1 receptors by catecholamines such as norepinephrine and epinephrine couples to the G(q) protein, which then activates the phospholipase C pathway, leading to an increase in IP3 and calcium. Consequently, the elevation of intracellular calcium concentration leads to vasoconstriction in smooth muscle of blood vessels. In addition, activation of alpha-1 receptors by phenylpropanolamine (PPA) produces anorexia and may induce appetite suppression in rats
IVVGVALGAFILFAIGGNLLVILSVACNRHLRTPTHYFIVNLAVADLLLSFTVLPFSATLEVLGYWAFGR
IFCDVWAAVDVLCCTASIMSLCVISVDRYIGVRYPLNYPTIVTARRATVALLIVWVLSLVISIGPLLGWK
EPAPADEQACGVNEEPGYVLFSSLGSFYLPLAIILVMYCRVYVVAFKFSREKKAAKTLGIVVGAFVLCWF
PFFVVLPLGSLFSTLKPPEPVFKVVFWLGYFNSCLNPIIYPCSSREFKRAF
>gnl|CDD|320191 cd15063, 7tmA_Octopamine_R, octopamine receptors in invertebrates, member of the class A family of seven-transmembrane G protein-coupled receptors. G-protein coupled receptor for octopamine (OA), which functions as a neurotransmitter, neurohormone, and neuromodulator in invertebrate nervous system. Octopamine (also known as beta, 4-dihydroxyphenethylamine) is an endogenous trace amine that is highly similar to norepinephrine, but lacks a hydroxyl group, and has effects on the adrenergic and dopaminergic nervous systems. Based on the pharmacological and signaling profiles, the octopamine receptors can be classified into at least two groups: OA1 receptors elevate intracellular calcium levels in muscle, whereas OA2 receptors activate adenylate cyclase and increase cAMP production
LISLLVLTFLNVLVVLGNLLVIAAVLCSRKLRTVTNLFIVSLACADLLVGTLVLPFSAVNEVLDVWIFGH
TWCQIWLAVDVWMCTASILNLCAISLDRYLAITRPIRYPSLMSTKRAKCLIAGVWVLSFVICFPPLVGWN
DGKDGIMDYSGSSSLPCTCELTNGRGYVIYSALGSFYIPMLVMLFFYFRIYRAARMETKAAKTVAIIVGC
FIFCWLPFFTVYLVRAFCEDCIPPLLFSVFFWLGYCNSALNPCIYALFSRDFRFAF
>gnl|CDD|320192 cd15064, 7tmA_5-HT1_5_7, serotonin receptor subtypes 1, 5 and 7, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes serotonin receptor subtypes 1, 5, and 7 that are activated by the neurotransmitter serotonin. The 5-HT1 and 5-HT5 receptors mediate inhibitory neurotransmission by coupling to G proteins of the G(i/o) family. The 5-HT1 receptor subfamily includes 5-HT1A, 5-HT1B, 5-HT1D, 5-HT1E, and 5-HT1F. There is no 5-HT1C receptor subtype, as it has been reclassified as 5-HT2C receptor. The 5-HT5A and 5-HT5B receptors have been cloned from rat and mouse, but only the 5-HT5A isoform has been identified in human because of the presence of premature stop codons in the human 5-HT5B gene, which prevents a functional receptor from being expressed. The 5-HT7 receptor is coupled to Gs, which positively stimulates adenylate cyclase activity, leading to increased intracellular cAMP formation and calcium influx. In the CNS, serotonin is involved in the regulation of appetite, mood, sleep, cognition, learning and memory, as well as implicated in neurologic disorders such as migraine, schizophrenia, and depression
VLISVLLSLIILATILGNALVIAAILLTRKLHTPANYLIASLAVADLLVAVLVMPLSAVYELTGRWILGQ
VLCDIWISLDVTCCTASILHLCVIALDRYWAITDAVEYAHKRTPKRAAVMIALVWTLSICISLPPLFGWR
TPDSEDPSECLISQDIGYTIFSTFGAFYIPLLLMLILYWKIYRAAARERKAAKTLGIILGAFIVCWLPFF
LVALIVPLCSHCWIPLALKSFFLWLGYFNSLINPLIYTFFNKDFRKAF
>gnl|CDD|320193 cd15065, 7tmA_Ap5-HTB1-like, serotonin receptor subtypes B1 and B2 from Aplysia californica and similar proteins; member of the class A family of seven-transmembrane G protein-coupled receptors. This subfamily includes Aplysia californica serotonin receptors Ap5-HTB1 and Ap5-HTB2, and similar proteins from bilateria including insects, mollusks, annelids, and worms. Ap5-HTB1 is one of the several different receptors for 5-hydroxytryptamine (5HT, serotonin). In Aplysia, serotonin plays important roles in a variety of behavioral and physiological processes mediated by the central nervous system. These include circadian clock, feeding, locomotor movement, cognition and memory, synaptic growth and synaptic plasticity. Both Ap5-HTB1 and Ap5-HTB2 receptors are coupled to G-proteins that stimulate phospholipase C, leading to the activation of phosphoinositide metabolism. Ap5-HTB1 is expressed in the reproductive system, whereas Ap5-HTB2 is expressed in the central nervous system
LIGIFLSLIIVLAIFGNVLVCLAIFTDRRLRKKSNLFIVSLAVADLLVALLVMTFAVVNDLLGYWLFGET
FCNIWISFDVMCSTASILNLCAISLDRYIHIKKPLKYERWMTTRRALVVIASVWILSALISFLPIHLGWH
RLSQDEIKGLNHASNPKPSCALDLNPTYAVVSSLISFYIPCLVMLLIYSRLYLYARKHVVNIKSQKLPSE
SGSKFQVPSLSSKHNNQGVSDHKAAVTLGIIMGVFLICWLPFFIINIIAAFCKTCIPPKCFKILTWLGYF
NSCLNPIIYSIFNSEFRRAF
>gnl|CDD|320194 cd15066, 7tmA_DmOct-betaAR-like, Drosophila melanogaster beta-adrenergic receptor-like octopamine receptors and similar receptors in bilateria; member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes Drosophila beta-adrenergic-like octopamine receptors and similar proteins. The biogenic amine octopamine is the invertebrate equivalent of vertebrate adrenergic neurotransmitters and exerts its effects through different G protein-coupled receptor types. Insect octopamine receptors are involved in the modulation of carbohydrate metabolism, muscular tension, cognition and memory. The activation of octopamine receptors mediating these actions leads to an increase in adenylate cyclase activity, thereby increasing cAMP levels. In Drosophila melanogaster, three subgroups have been classified on the basis of their structural homology and functional equivalents with vertebrate beta-adrenergic receptors: DmOctBeta1R, DmOctBeta2R, and DmOctBeta3R
LKGFAMTLIILAAIFGNLLVIISVMRHRKLRVITNYFVVSLAMADMLVALCAMTFNASVEITGRWMFGYF
MCDVWNSLDVYFSTASILHLCCISVDRYYAIVQPLEYPSKMTKRRVAIMLANVWISPALISFLPIFLGWY
TTEEHLQYRKTHPDQCEFVVNKIYALISSSVSFWIPCIVMIFTYYRIYLEAKREHKAAKTLGIIMGAFIL
CWLPFFLWYVTTTLCGDACPYPPILVSILFWIGYFNSTLNPLIYAYFNRDFREAF
>gnl|CDD|320195 cd15067, 7tmA_Dop1R2-like, dopamine 1-like receptor 2 from Drosophila melanogaster and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. G protein-coupled dopamine 1-like receptor 2 is expressed in Drosophila heads and it shows significant sequence similarity with vertebrate and invertebrate dopamine receptors. Although the Drosophila Dop1R2 receptor does not cluster into the D1-like structural group, it does show pharmacological properties similar to D1-like receptors. As shown in vertebrate D1-like receptors, agonist stimulation of Dop1R2 activates adenylyl cyclase to increase cAMP levels and also generates a calcium signal through stimulation of phospholipase C
LLGVVLSLFCLVTVAGNLLVILAVLRERYLRTVTNYFIVSLAVADLLVGSIVMPFSILHEMTGGYWLFGR
DWCDVWHSFDVLASTASILNLCVISLDRYWAITDPISYPSRMTKRRALIMIALVWICSALISFPAIAWWR
AVDPGPSPPNQCLFTDDSGYLIFSSCVSFYIPLVVMLFTYYRIYRAAAKEQKAAKTLGIVMGVFILCWLP
FFVTNILIGFCPSNCVSNPDILFPLVTWLGYINSGMNPIIYACSSRDFRRAF
>gnl|CDD|320196 cd15068, 7tmA_Adenosine_R_A2A, adenosine receptor subtype A2A, member of the class A family of seven-transmembrane G protein-coupled receptors. The A2A receptor, a member of the adenosine receptor family of G protein-coupled receptors, binds adenosine as its endogenous ligand and is involved in regulating myocardial oxygen consumption and coronary blood flow. High-affinity A2A and low-affinity A2B receptors are preferentially coupled to G proteins of the stimulatory (Gs) family, which lead to activation of adenylate cyclase and thereby increasing the intracellular cAMP levels. The A2A receptor activation protects against tissue injury and acts as anti-inflammatory agent. In human skin endothelial cells, activation of A2B receptor, but not the A2A receptor, promotes angiogenesis. Alternatively, activated A2A receptor, but not the A2B receptor, promotes angiogenesis in human umbilical vein and lung microvascular endothelial cells. The A2A receptor alters cardiac contractility indirectly by modulating the anti-adrenergic effect of A1 receptor, while the A2B receptor exerts direct effects on cardiac contractile function, but does not modulate beta-adrenergic or A1 anti-adrenergic effects
SVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADIAVGVLAIPFAITISTGFCAACHG
CLFIACFVLVLTQSSIFSLLAIAIDRYIAIRIPLRYNGLVTGTRAKGIIAICWVLSFAIGLTPMLGWNNC
GQPKEGKNHSQGCGEGQVACLFEDVVPMNYMVYFNFFACVLVPLLLMLGVYLRIFLAARRQLKQMESQPL
PGERARSTLQKEVHAAKSLAIIVGLFALCWLPLHIINCFTFFCPDCSHAPLWLMYLAIVLSHTNSVVNPF
IYAYRIREFRQTF
>gnl|CDD|320197 cd15069, 7tmA_Adenosine_R_A2B, adenosine receptor subtype 2AB, member of the class A family of seven-transmembrane G protein-coupled receptors. The A2B receptor, a member of the adenosine receptor family of G protein-coupled receptors, binds adenosine as its endogenous ligand and is involved in regulating myocardial oxygen consumption and coronary blood flow. High-affinity A2A and low-affinity A2B receptors are preferentially coupled to G proteins of the stimulatory (Gs) family, which lead to activation of adenylate cyclase and thereby increasing the intracellular cAMP levels. The A2A receptor activation protects against tissue injury and acts as anti-inflammatory agent. In human skin endothelial cells, activation of A2B receptor, but not the A2A receptor, promotes angiogenesis. Alternatively, activated A2A receptor, but not the A2B receptor, promotes angiogenesis in human umbilical vein and lung microvascular endothelial cells. The A2A receptor alters cardiac contractility indirectly by modulating the anti-adrenergic effect of A1 receptor, while the A2B receptor exerts direct effects on cardiac contractile function, but does not modulate beta-adrenergic or A1 anti-adrenergic effects
ATYVALELIIAALSVAGNVLVCAAVGTNSTLQTPTNYFLVSLAAADVAVGLFAIPFAITISLGFCTDFHS
CLFLACFVLVLTQSSIFSLLAVAVDRYLAIKVPLRYKSLVTGKRARGVIAVLWVLAFGIGLTPFLGWNKA
MSATNNSTNPADHGTNHSCCLISCLFENVVPMSYMVYFNFFGCVLPPLLIMLVIYIKIFLVACRQLQRTE
LMDHSRTTLQREIHAAKSLAIIVGIFALCWLPVHILNCITLFQPEFSKSKPKWAMNVAILLSHANSVVNP
IVYAYRNRDFRYTF
>gnl|CDD|320198 cd15070, 7tmA_Adenosine_R_A3, adenosine receptor subtype A3, member of the class A family of seven-transmembrane G protein-coupled receptors. The A3 receptor, a member of the adenosine receptor family of G protein-coupled receptors, is coupled to G proteins of the inhibitory G(i) family, which lead to inhibition of adenylate cyclase and thereby lowering the intracellular cAMP levels. The A3 receptor has a sustained protective function in the heart during cardiac ischemia and contributes to inhibition of neutrophil degranulation in neutrophil-mediated tissue injury. Moreover, activation of A3 receptor by adenosine protects astrocytes from cell death induced by hypoxia
VTYISIEILIGLCAVVGNVLVIWVVKLNPSLRTTTFYFIVSLALADIAVGVLVIPLAIVVSLGVTIHFYS
CLFMSCLLVVFTHASIMSLLAIAVDRYLRVKLTVRYRIVTTQRRIWLALGLCWLVSFLVGLTPMFGWNRK
PSLESVNTTPLQCQFTSVMRMDYMVYFSFFTWILIPLVIMCALYVDIFYIIRNKLSQNATGFRETGAFYG
REFKTAKSLALVLFLFAVCWLPLSIINCVVYFNPKVPKIALYLGILLSHANSMMNPIVYACKIKKFKETY
>gnl|CDD|341323 cd15071, 7tmA_Adenosine_R_A1, adenosine receptor subtype A1, member of the class A family of seven-transmembrane G protein-coupled receptors. The adenosine A1 receptor, a member of the adenosine receptor family of G protein-coupled receptors, binds adenosine as its endogenous ligand. The A1 receptor has primarily inhibitory function on the tissues in which it is located. The A1 receptor slows metabolic activity in the brain and has a strong anti-adrenergic effects in the heart. Thus, it antagonizes beta1-adrenergic receptor-induced stimulation and thereby reduces cardiac contractility. The A1 receptor preferentially couples to G proteins of the G(i/o) family, which lead to inhibition of adenylate cyclase and thereby lowering the intracellular cAMP levels
AAYIGIEVLIALVSVPGNVLVIWAVKVNQALRDATFCFIVSLAVADVAVGALVIPLAIIINIGPQTEFYS
CLMVACPVLILTQSSILALLAIAVDRYLRVKIPTRYKSVVTPRRAAVAIAGCWILSFLVGLTPMFGWNNL
NAVERAWAANSSMGELVIKCQFETVISMEYMVYFNFFVWVLPPLLLMLLIYLEVFYLIRKQLNKKVSSSS
SDPQKYYGKELKIAKSLALILFLFALSWLPLHILNCITLFCPSCKKPMILTYIAIFLTHGNSAMNPIVYA
FRIKKFRTTF
>gnl|CDD|320200 cd15072, 7tmA_Retinal_GPR, retinal G protein coupled receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. This group represents the retinal G-protein coupled receptor (RGR) found exclusively in retinal pigment epithelium (RPE) and Muller cells. RGR is a member of the class A rhodopsin-like receptor family. As with other opsins, RGR binds all-trans retinal and contains a conserved lysine reside on the seventh helix. RGR functions as a photoisomerase to catalyze the conversion of all-trans-retinal to 11-cis-retinal. Two mutations in RGR gene are found in patients with retinitis pigmentosa, indicating that RGR is essential to the visual process
FAVGSILLVEALVGFSLNGLTILSFCKTRELRTPSNLLVLSLAVADMGISLNALVAASSSLLRRWPYGSE
GCQAHGFQGFFTALASICSSAAIAWDRYHHYCTRSKLQWSTAISLVLFVWLFSAFWAAMPLLGWGEYDYE
PLGTCCTLDYSKGDRNYVSYLFTMAFFNFILPLFILLTSYSSIEQKLKKEGHLRFNTGLPLLTLLICWGP
YAILALYAAITDVTSISPKLRMVPALLAKTSPTINAILYALGNENYRGGI
>gnl|CDD|320201 cd15073, 7tmA_Peropsin, retinal pigment epithelium-derived rhodopsin homolog, member of the class A family of seven-transmembrane G protein-coupled receptors. Peropsin, also known as a retinal pigment epithelium-derived rhodopsin homolog (RRH), is a visual pigment-like protein found exclusively in the apical microvilli of the retinal pigment epithelium. Peropsin belongs to the type 2 opsin family of the class A G-protein coupled receptors. Peropsin presumably plays a physiological role in the retinal pigment epithelium either by detecting light directly or monitoring the levels of retinoids, the primary light absorber in visual perception, or other pigment-related compounds in the eye
NIVAAYLIVAGIISTISNGIVLVTFVKFRELRTPTNALIINLAVTDLGVSIIGYPFSAASDLHGSWKFGY
AGCQWYAFLNIFFGMASIGLLTVVAVDRYLTICRPDLGRKMTTNTYTVMILLAWTNAFFWAAMPLVGWAS
YALDPTGATCTINWRKNDSSFVSYTMSVIVVNFIVPLAVMFYCYYNVSRFVKKVLASDCLESVNIDWTDQ
NDVTKMSVIMIVMFLVAWSPYSIVCLWASFGEPKKIPPWMAIIPPLFAKSSTFYNPCIYVIANKKFRRAI
>gnl|CDD|320202 cd15074, 7tmA_Opsin5_neuropsin, neuropsin (Opsin-5), member of the class A family of seven-transmembrane G protein-coupled receptors. Neuropsin, also known as Opsin-5, is a photoreceptor protein expressed in the retina, brain, testes, and spinal cord. Neuropsin belongs to the type 2 opsin family of the class A G-protein coupled receptors. Mammalian neuropsin activates Gi protein-mediated photo-transduction pathway in a UV-dependent manner, whereas, in non-mammalian vertebrates, neuropsin is involved in regulating the photoperiodic control of seasonal reproduction in birds such as quail. As with other opsins, it may also act as a retinal photoisomerase
IIIGIYLTVIGILSTLGNGTVLFVLYRRRSKLKPAELLTVNLAVSDLGISVFGYPLAIISAFAHRWLFGD
IGCVFYGFCGFLFGCCSINTLTAISIYRYLKICHPPYGPKLSRRHVCIVIVAIWLYALFWAVAPLVGWGS
YGPEPFGTSCSIDWTGASASVGGMSYIISIFIFCYLLPVLIIVFSYVKIIRKVKSSRKRVAGFDSRSKRQ
HKIERKVTKVAVLICAGFLIAWTPYAVVSMWSAFGSPDSVPILASILPALFAKSSCMYNPIIYLLFSSKF
RQDL
>gnl|CDD|320203 cd15075, 7tmA_Parapinopsin, non-visual parapinopsin, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes the non-visual pineal pigment, parapinopsin, which is a member of the class A of the seven transmembrane G protein-coupled receptors. Parapinopsin serves as a UV-sensitive pigment for the wavelength discrimination in the pineal-related organs of lower vertebrates such as reptiles, amphibians, and fish. Although parapinopsin is phylogenetically related to vertebrate visual pigments such as rhodopsin, which releases its retinal chromophore and bleaches, the parapinopsin photoproduct is stable and does not bleach. The vertebrate non-visual opsin family includes pinopsins, parapinopsin, VA (vertebrate ancient) opsins, and parietopsins. These non-visual opsins are expressed in various extra-retinal tissues and/or in non-rod, non-cone retinal cells
TILSIIMAVFSIASVVLNATVIIVTLRHKQLRQPLNYALVNLAVADLGTTVFGGLLSVVTNAVGYFNLGR
VGCVLEGFAVAFFGIAALCTVAVIAVDRLFVVCKPLGTLTFQTRHALAGIASSWLWSLIWNTPPLFGWGS
YQLEGVMTSCAPDWYSRDPVNVSYILCYFSFCFAIPFAIILVSYGYLLWTLRQVAKLGVAEGGSTAKAEV
QVARMVVVMVMAFLLCWLPYAAFALTVVSKPDVYINPLIATVPMYLAKSSTVYNPIIYIFMNKQFRDCA
>gnl|CDD|320204 cd15076, 7tmA_SWS1_opsin, short wave-sensitive 1 opsins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes Short Wave-Sensitive opsin 1 (SWS1), which mediates visual transduction in response to light at short wavelengths (ultraviolet to blue). Vertebrate cone opsins are expressed in cone photoreceptor cells of the retina and involved in mediating photopic vision, which allows color perception. The cone opsins can be classified into four classes according to their peak absorption wavelengths: SWS1 (ultraviolet sensitive), SWS2 (short wave-sensitive), MWS/LWS (medium/long wave-sensitive), and RH2 (medium wave-sensitive, rhodopsin-like opsins). Members of this group belong to the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops
YLQAAFMGFVFIVGTPLNAIVLFVTIKYKKLRQPLNYILVNISLAGFIFCIFSVFPVFVASAQGYFFFGR
TVCALEAFVGSLAGLVTGWSLAFLAFERYIVICKPFGNFRFGSKHALGAVVATWIIGIGVSLPPFFGWSR
YIPEGLQCSCGPDWYTVGTKYRSEYYTWFLFIFCFIVPLSIIIFSYSQLLGALRAVAAQQQESASTQKAE
REVSRMVVVMVGSFCLCYVPYAALAMYMVNNRDHGLDLRLVTIPAFFSKSSCVYNPIIYCFMNKQFRACI
>gnl|CDD|320205 cd15077, 7tmA_SWS2_opsin, short wave-sensitive 2 opsins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes Short Wave-Sensitive opsin 2 (SWS2), which mediates visual transduction in response to light at short wavelengths (violet to blue). Vertebrate cone opsins are expressed in cone photoreceptor cells of the retina and involved in mediating photopic vision, which allows color perception. The cone opsins can be classified into four classes according to their peak absorption wavelengths: SWS1 (ultraviolet sensitive), SWS2 (short wave-sensitive), MWS/LWS (medium/long wave-sensitive), and RH2 (medium wave-sensitive, rhodopsin-like opsins). Members of this group belong to the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops
MGMSAFMLFLVIAGFPINVLTIICTIKYKKLRSHLNYILVNLAVANLIVVCFGSTTAFYSFSQMYFVLGP
LACKIEGFTATLGGMVSLWSLAVVAFERFLVICKPLGNFTFRGTHAIIGCIATWVFGLAASLPPLFGWSR
YIPEGLQCSCGPDWYTTNNKWNNESYVMFLFCFCFGVPLSIIVFSYGRLLLTLRAVAKQQEQSASTQKAE
REVTKMVVVMVLGFLVCWLPYASFALWVVTNRGEPFDLRLASIPSVFSKASTVYNPVIYVFMNKQFRSCM
>gnl|CDD|320206 cd15078, 7tmA_Encephalopsin, encephalopsins (opsin-3), member of the class A family of seven-transmembrane G protein-coupled receptors. Encephalopsin, also called Opsin-3 or Panopsin, is a mammalian extra-retinal opsin that is highly localized in the brain. It is thought to play a role in encephalic photoreception. Encephalopsin belongs to the class A of the G protein-coupled receptors and shows strong homology to the vertebrate visual opsins
ELLALLIATIGFLGVCNNLLVLILYYKFKRLRTPTNLLLVNISLSDLLVSLLGVTFTFMSCVRGRWVFDV
AGCVWDGFSNSLFGIVSIMTLTVLAYERYIRVVHAKVVNFSWSWRAITYIWLYSLAWTGAPLLGWNRYTL
EVHGLGCSFDWKSKDPNDTSFVLLFFLGCLVVPLGIMAYCYGHILYEIRMLRSVEDLQTFQVIKILKYEK
KVAKMCLLMISTFLICWMPYAVVSLLVTSGYSKLVTPTIAIIPSLFAKSSTAYNPVIYIFMIRKFRQCL
>gnl|CDD|320207 cd15079, 7tmA_photoreceptors_insect, insect photoreceptors R1-R6 and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes the insect photoreceptors and their closely related proteins. The Drosophila eye is composed of about 800 unit eyes called ommatidia, each of which contains eight photoreceptor cells (R1-R8). The six outer photoreceptors (R1-R6) function like the vertebrate rods and are responsible for motion detection in dim light and image formation. The R1-R6 photoreceptors express a blue-absorbing pigment, Rhodopsin 1(Rh1). The inner photoreceptors (R7 and R8) are considered the equivalent of the color-sensitive vertebrate cone cells, which express a range of different pigments. The R7 photoreceptors express one of two different UV absorbing pigments, either Rh3 or Rh4. Likewise, the R8 photoreceptors express either the blue absorbing pigment Rh5 or green absorbing pigment Rh6. These photoreceptors belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops
YLLGFIYIFLGIVSLLGNGLVIYIFSTTKSLRTPSNMLVVNLAISDFLMMIKMPIFIYNSFYEGWALGPL
GCQIYAFLGSLSGIGSIWTNAAIAYDRYNVIVKPLNGNPLTRGKALLLILFIWLYALPWALLPLLFGWGR
YVPEGFLTSCSFDYLTRDWNTRSFVATIFVFAYVIPLIIIIYCYSFIVKAVFAHEKALREQAKKMNVVSL
RSNADANKQSAEIRIAKVALTNVFLWFIAWTPYAVVALIGAFGNQSLLTPLVSMIPALFAKTAACYNPIV
YAISHPKYRLEL
>gnl|CDD|381742 cd15080, 7tmA_MWS_opsin, medium wave-sensitive opsins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes Medium Wave-Sensitive opsin, which mediates visual transduction in response to light at medium wavelengths (green). Vertebrate cone opsins are expressed in cone photoreceptor cells of the retina and involved in mediating photopic vision, which allows color perception. The cone opsins can be classified into four classes according to their peak absorption wavelengths: SWS1 (ultraviolet sensitive), SWS2 (short wave-sensitive), MWS/LWS (medium/long wave-sensitive), and RH2 (medium wave-sensitive, rhodopsin-like opsins). Members of this group belong to the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops
SALAAYMFLLILLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTMYTSMHGYFVFGP
TGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSR
YIPEGMQCSCGIDYYTLKPEVNNESFVIYMFVVHFTIPLIVIFFCYGRLVCTVKEAAAQQQESATTQKAE
KEVTRMVIIMVIAFLICWVPYASVAFYIFTHQGSDFGPIFMTIPAFFAKSSAVYNPVIYILMNKQFRNCM
>gnl|CDD|320209 cd15081, 7tmA_LWS_opsin, long wave-sensitive opsins, member of the class A family of seven-transmembrane G protein-coupled receptors. Long Wave-Sensitive opsin is also called red-sensitive opsin or red cone photoreceptor pigment, which mediates visual transduction in response to light at long wavelengths. Vertebrate cone opsins are expressed in cone photoreceptor cells of the retina and involved in mediating photopic vision, which allows color perception. The cone opsins can be classified into four classes according to their peak absorption wavelengths: SWS1 (ultraviolet sensitive), SWS2 (short wave-sensitive), MWS/LWS (medium/long wave-sensitive), and RH2 (medium wave-sensitive, rhodopsin-like opsins). Members of this group belong to the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops
GPNYHIAPRWVYNLTSVWMIFVVFASVFTNGLVLVATLKFKKLRHPLNWILVNLAIADLGETVIASTISV
VNQIFGYFILGHPMCVLEGFTVSVCGITGLWSLTIISWERWVVVCKPFGNIKFDGKLAIVGIIFSWVWSA
VWCAPPIFGWSRYWPHGLKTSCGPDVFSGSSDPGVQSYMIVLMITCCIIPLAIIILCYLQVWLAIRAVAQ
QQKESESTQKAEKEVSRMVVVMIFAYCFCWGPYTFFACFAAANPGYAFHPLAAALPAYFAKSATIYNPII
YVFMNRQFRNCI
>gnl|CDD|320210 cd15082, 7tmA_VA_opsin, non-visual VA (vertebrate ancient) opsins, member of the class A family of seven-transmembrane G protein-coupled receptors. The vertebrate ancient (VA) opsin photopigments were originally identified in salmon and they appear to have diverged early in the evolution of vertebrate opsins. VA opsins are localized in the inner retina and the brain in teleosts. The vertebrate non-visual opsin family includes pinopsins, parapinopsin, VA (vertebrate ancient) opsins, and parietopsins. These non-visual opsins are expressed in various extraretinal tissues and/or in non-rod, non-cone retinal cells. They are thought to be involved in light-dependent physiological functions such as photo-entrainment of circadian rhythm, photoperiodicity, and body color change. The VA opsins belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops
FSGPLKSIAPWNFTVLAALMFVVTSLSLAENFAVMLVTFRFKQLRQPLNYIIVNLSVADFLVSLTGGTIS
FLTNARGYFFLGVWACVLEGFAVTFFGIVALWSLAVLAFERFFVICRPLGNIRLQGKHAALGLLFVWTFS
FIWTIPPVLGWSSYTVSKIGTTCEPNWYSGNMHDHTYIITFFTTCFILPLGVIFVSYGKLLQKLRKVSNT
QGRLGNARKPERQVTRMVVVMIVAFMVCWTPYAAFSILVTAHPTIHLDPRLAAIPAFFSKTAAVYNPIIY
VFMNKQFRKCL
>gnl|CDD|320211 cd15083, 7tmA_Melanopsin-like, vertebrate melanopsins and related opsins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group represent the Gq-coupled rhodopsin subfamily consists of melanopsins, insect photoreceptors R1-R6, invertebrate Gq opsins as well as their closely related opsins. Melanopsins (also called Opsin-4) are the primary photoreceptor molecules for non-visual functions such as the photo-entrainment of the circadian rhythm and pupillary constriction in mammals. Mammalian melanopsins are expressed only in the inner retina, whereas non-mammalian vertebrate melanopsins are localized in various extra-retinal tissues such as iris, brain, pineal gland, and skin. The outer photoreceptors (R1-R6) are the insect Drosophila equivalent to the vertebrate rods and are responsible for image formation and motion detection. The invertebrate G(q) opsins includes the arthropod and mollusk visual opsins as well as invertebrate melanopsins, which are also found in vertebrates. Arthropods possess color vision by the use of multiple opsins sensitive to different light wavelengths. Members of this subfamily belong to the class A of the G protein-coupled receptors and have seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops
YVLGIFILIIGLIGVVGNGLVIYAFCRFKSLRTPANYLIINLAISDFLMCILNCPLMVISSFSGRWIFGK
TGCDMYGFSGGLFGIMSINTLAAIAVDRYLVITRPMKASVRISHRRALIVIAVVWLYSLLWVLPPLFGWS
RYVLEGLLTSCSFDYLSRDDANRSYVICLLIFGFVLPLLIIIYCYSFIFRAVRRHEKAMKEMAKRFSKSE
LSSPKARRQAEVKTAKIALLLVLLFCLAWTPYAVVALIGQFGYLEVLTPLATAIPAAFAKTSAIYNPVIY
AFSHPKFRRAL
>gnl|CDD|320212 cd15084, 7tmA_Pinopsin, non-visual pinopsins, member of the class A family of seven-transmembrane G protein-coupled receptors. Pinopsins are found in the pineal organ of birds, reptiles and amphibians, but are absent from teleosts and mammals. The vertebrate non-visual opsin family includes pinopsins, parapinopsin, VA (vertebrate ancient) opsins, and parietopsins. These non-visual opsins are expressed in various extra-retinal tissues and/or in non-rod, non-cone retinal cells. They are thought to be involved in light-dependent physiological functions such as photo-entrainment of circadian rhythm, photoperiodicity and body color change. Pinopsins belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops
WPHLAPRSTYLTVAVLMGMVVALASFVNGLVIVVSIKYKKLRSPLNYILVNLAVADLLVTLFGSSVSFSN
NIVGFFVFGKTMCEFEGFMVSLTGIVGLWSLAILAFERYLVICKPMGDFRFQQRHAVSGCAFTWGWSLLW
TSPPLFGWSSYVPEGLRTSCGPNWYTGGTNNNSYILALFVTCFALPLSTIIFSYSNLLLTLRAVAAQQKE
SETTQRAEKEVTRMVIAMVMAFLICWLPYATFAMVVATNKDVVIQPTLASLPSYFSKTATVYNPIIYVFM
NKQFRSCLLELLCCG
>gnl|CDD|320213 cd15085, 7tmA_Parietopsin, non-visual parietopsins, member of the class A family of seven-transmembrane G protein-coupled receptors. Parietopsin is a non-visual green light-sensitive opsin that was initially identified in the parietal eye of lizards. The vertebrate non-visual opsin family includes pinopsins, parapinopsin, VA (vertebrate ancient) opsins, and parietopsins. These non-visual opsins are expressed in various extra-retinal tissues and/or in non-rod, non-cone retinal cells. They are thought to be involved in light-dependent physiological functions such as photo-entrainment of circadian rhythm, photoperiodicity and body color change. Parietopsin belongs to the class A of the G protein-coupled receptors and shows strong homology to the vertebrate visual opsins
SILSFLMFLNATFSIFNNVLVIAVTLKNPQLRNPINIFILNLSFSDLMMALCGTTIVTVTNYEGYFYLGD
AFCIFQGFAVNYFGIVSLWSLTLLAYERYNVVCKPMGGLKLSTKRGYQGLLFIWLFCLFWAVAPLFGWSS
YGPEGVQTSCSIGWEERSWSNYSYLILYFLMCFVIPVAIIGFSYGNVLRSLHKLNKKIEQQGGKNCPEEE
ERAVIMVLAMVIAFLICWLPYTVFALIVVVNPELSISPLAATMPTYFAKTSPVYNPIIYIFLNKQFRESA
>gnl|CDD|320214 cd15086, 7tmA_tmt_opsin, teleost multiple tissue (tmt) opsin, member of the class A family of seven-transmembrane G protein-coupled receptors. Teleost multiple tissue (tmt) opsins are homologs of encephalopsin. Mouse encephalopsin (or panopsin) is highly expressed in the brain and testes, whereas the teleost homologs are localized to multiple tissues. The exact functions of the encephalopsins and tmt-opsins are unknown. The vertebrate non-visual opsin family includes pinopsins, parapinopsin, VA (vertebrate ancient) opsins, and parietopsins. These non-visual opsins are expressed in various extra-retinal tissues and/or in non-rod, non-cone retinal cells. They are thought to be involved in light-dependent physiological functions such as photo-entrainment of circadian rhythm, photoperiodicity and body color change. Tmt opsins belong to the class A of the G protein-coupled receptors and show strong homology to the vertebrate visual opsins
TVVAVFLGFILTFGFLNNLLVLVLFCKYKVLRSPINLLLLNISLSDLLVCVLGTPFSFAASTQGRWLIGE
HGCRWYGFANSLFGIVSLISLAVLSYERYCTLLRPTEADVSDYRKAWLGVGGSWLYSLLWTLPPLLGWSS
YGPEGPGTTCSVQWTSRSANSISYIICLFIFCLLLPFLVMVYCYGRLLYAIKQVGKINKSTARKREQHVL
LMVVTMVICYLLCWLPYGVMALLATFGKPGLVTPVASIVPSILAKSSTVVNPIIYVFMNKQFYRCF
>gnl|CDD|320215 cd15087, 7tmA_NPBWR, neuropeptide B/W receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Neuropeptide B/W receptor 1 and 2 are members of the class A G-protein coupled receptors that bind the neuropeptides B and W, respectively. NPBWR1 (previously known as GPR7) is expressed predominantly in cerebellum and frontal cortex, while NPBWR2 (previously known as GPR8) is located mostly in the frontal cortex and is present in human, but not in rat and mice. These receptors are suggested to be involved in the regulation of food intake, neuroendocrine function, and modulation of inflammatory pain, among many others. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VALPVIYSVICAVGLTGNTAVIYVILRAPKMKTVTNVFILNLAIADDLFTLVLPINIAEHLLQQWPFGEL
LCKLILSIDHYNIFSSIYFLTVMSVDRYLVVLATVRSRRMPYRTYRAAKIVSLCVWLLVTIIVLPFTVFA
GVYSNELGRKSCVLSFPSPESLWFKASRIYTLVLGFAIPVSTICILYTMMLYKLRNMRLNSNAKALDKAK
KKVTLMVLVVLAVCLFCWTPFHLSTVVALTTDLPQTPLVIGISYFITSLSYANSCLNPFLYAFLDDSFRK
SF
>gnl|CDD|320216 cd15088, 7tmA_MCHR-like, melanin concentrating hormone receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Melanin-concentrating hormone receptor (MCHR) binds melanin concentrating hormone and is presumably involved in the neuronal regulation of food intake and energy homeostasis. Despite strong homology with somatostatin receptors, MCHR does not appear to bind somatostatin. Two MCHRs have been characterized in vertebrates, MCHR1 and MCHR2. MCHR1 is expressed in all mammals, whereas MCHR2 is only expressed in the higher order mammals, such as humans, primates, and dogs, and is not found in rodents. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VIMPSVFGCICVVGLVGNGIVLYVLVRCSKLRTAPDIFIFNLAVADLLFMLGMPFLIHQFAIDGQWYFGE
VMCKIITALDANNQFTSTYILTAMSVDRYLAVVHPIRSTKYRTRFVAKLVNVGLWAASFLSILPVWVYSS
LIYFPDGTTFCYVSLPSPDDLYWFTIYHFILGFAVPLVVITVCYILILHRLARGVAPGNQSHGSSRTKRV
TKMVILIVVVFIVCWLPFHVVQLVNLAMNRPTLAFEVAYFLSICLGYANSCLNPFVYILVSENFRKRL
>gnl|CDD|320217 cd15089, 7tmA_Delta_opioid_R, opioid receptor subtype delta, member of the class A family of seven-transmembrane G protein-coupled receptors. The delta-opioid receptor binds the endogenous pentapeptide ligands such as enkephalins and produces antidepressant-like effects. The opioid receptor family is composed of four major subtypes: mu (MOP), delta (DOP), kappa (KOP) opioid receptors, and the nociceptin/orphanin FQ peptide receptor (NOP). They are distributed widely in the central nervous system and respond to classic alkaloid opiates, such as morphine and heroin, as well as to endogenous peptide ligands, which include dynorphins, enkephalins, endorphins, endomorphins, and nociceptin. Opioid receptors are coupled to inhibitory G proteins of the G(i/o) family and involved in regulating a variety of physiological functions such as pain, addiction, mood, stress, epileptic seizure, and obesity, among many others
IAITALYSVVCVVGLLGNVLVMYGIVRYTKMKTATNIYIFNLALADALATSTLPFQSAKYLMETWPFGEL
LCKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLSSGVGVPIMVMAVT
KTPRDGAVVCMLQFPSPSWYWDTVTKICVFIFAFVVPILVITVCYGLMILRLRSVRLLSGSKEKDRNLRR
ITRMVLVVVAAFIICWTPIHIFVIVWTLVDIDRRNPLVVAALHLCIALGYANSSLNPVLYAFLDENFKRC
F
>gnl|CDD|320218 cd15090, 7tmA_Mu_opioid_R, opioid receptor subtype mu, member of the class A family of seven-transmembrane G protein-coupled receptors. The mu-opioid receptor binds endogenous opioids such as beta-endorphin and endomorphin. The opioid receptor family is composed of four major subtypes: mu (MOP), delta (DOP), kappa (KOP) opioid receptors, and the nociceptin/orphanin FQ peptide receptor (NOP). They are distributed widely in the central nervous system and respond to classic alkaloid opiates, such as morphine and heroin, as well as to endogenous peptide ligands, which include dynorphins, enkephalins, endorphins, endomorphins, and nociceptin. Opioid receptors are coupled to inhibitory G proteins of the G(i/o) family and involved in regulating a variety of physiological functions such as pain, addiction, mood, stress, epileptic seizure, and obesity, among many others
ITIMALYSIVCVVGLFGNFLVMYVIVRYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGNI
LCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIVNVCNWILSSAIGLPVMFMATT
KYRQGSIDCTLTFSHPSWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRI
TRMVLVVVAVFIVCWTPIHIYVIIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCF
>gnl|CDD|320219 cd15091, 7tmA_Kappa_opioid_R, opioid receptor subtype kappa, member of the class A family of seven-transmembrane G protein-coupled receptors. The kappa-opioid receptor binds the opioid peptide dynorphin as the primary endogenous ligand. The opioid receptor family is composed of four major subtypes: mu (MOP), delta (DOP), kappa (KOP) opioid receptors, and the nociceptin/orphanin FQ peptide receptor (NOP). They are distributed widely in the central nervous system and respond to classic alkaloid opiates, such as morphine and heroin, as well as to endogenous peptide ligands, which include dynorphins, enkephalins, endorphins, endomorphins, and nociceptin. Opioid receptors are coupled to inhibitory G proteins of the G(i/o) family and involved in regulating a variety of physiological functions such as pain, addiction, mood, stress, epileptic seizure, and obesity, among many others
VIITAVYSVVFVVGLVGNSLVMFVIIRYTKMKTATNIYIFNLALADALVTTTMPFQSTVYLMNSWPFGDV
LCKIVISIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPLKAKIINICIWLLSSSVGISAIVLGGT
KVREDVDSTECSLQFPDDDYSWWDTFMKICVFIFAFVIPVLIIIVCYTLMILRLKSVRLLSGSREKDRNL
RRITRLVLVVVAVFVVCWTPIHIFILVEALGSVSHSTAAVSSYYFCIALGYTNSSLNPILYAFLDENFKR
CF
>gnl|CDD|320220 cd15092, 7tmA_NOFQ_opioid_R, nociceptin/orphanin FQ peptide receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The nociceptin (NOP) receptor binds nociceptin or orphanin FQ, a 17 amino acid endogenous neuropeptide. The NOP receptor is involved in the modulation of various brain activities including instinctive and emotional behaviors. The opioid receptor family is composed of four major subtypes: mu (MOP), delta (DOP), kappa (KOP) opioid receptors, and the nociceptin/orphanin FQ peptide receptor (NOP). They are distributed widely in the central nervous system and respond to classic alkaloid opiates, such as morphine and heroin, as well as to endogenous peptide ligands, which include dynorphins, enkephalins, endorphins, endomorphins, and nociceptin. Opioid receptors are coupled to inhibitory G proteins of the G(i/o) family and involved in regulating a variety of physiological functions such as pain, addiction, mood, stress, epileptic seizure, and obesity, among many others
VTIVVVYLIVCVVGLVGNCLVMYVILRHTKMKTATNIYIFNLALADTLVLLTLPFQGTDIFLGFWPFGNA
LCKTVIAIDYYNMFTSTFTLTAMSVDRYVAICHPIKALDVRTPHKAKVVNVCIWALASVVGVPVMVMGSA
QVEDEEIECLVEIPTPQDYWDPVFGICVFLFSFIIPVLIISVCYSLMIRRLRGVRLLSGSKEKDRNLRRI
TRLVLVVVAVFVGCWTPIQIFVLAQGLGVQPSSETAVAILRFCTALGYVNSSLNPVLYAFLDENFKACF
>gnl|CDD|320221 cd15093, 7tmA_SSTR, somatostatin receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. G protein-coupled somatostatin receptors (SSTRs) are composed of five distinct subtypes (SSTR1-5) that display strong sequence similarity with opioid receptors. All five receptor subtypes bind the natural somatostatin (somatotropin release inhibiting factor), a polypeptide hormone that regulates a wide variety of physiological functions such as neurotransmission, cell proliferation, contractility of smooth muscle cells, and endocrine signaling as well as inhibition of the release of many secondary hormones. They share common signaling cascades such as inhibition of adenylyl cyclase, activation of phosphotyrosine phosphatase activity, and G-protein-dependent regulation of MAPKs
VLIPCIYAVVCLVGLCGNSLVIYVVLRYAKMKTVTNIYILNLAIADELFMLGLPFLAASNALRHWPFGSV
LCRLVLSVDGINMFTSIFCLTVMSVDRYLAVVHPIKSARWRRPRVAKVVNLAVWVASLLVILPVVVFAGT
RENQDGSSACNMQWPEPAAAWSAGFIIYTFVLGFLLPLLIICLCYLLIVIKVKSAGLRAGWQQRKRSERK
VTRMVVMVVVVFVICWLPFYVLQLVNVFVQLPETPALVGVYHFVVILSYANSCANPILYGFLSDNFKKSF
>gnl|CDD|320222 cd15094, 7tmA_AstC_insect, somatostatin-like receptor for allatostatin C, member of the class A family of seven-transmembrane G protein-coupled receptors. G protein-coupled somatostatin receptors (SSTRs) are composed of five distinct subtypes (SSTR1-5) that display strong sequence similarity with opioid receptors. All five receptor subtypes bind the natural somatostatin (somatotropin release inhibiting factor), a polypeptide hormone that regulates a wide variety of physiological functions such as neurotransmission, cell proliferation, contractility of smooth muscle cells, and endocrine signaling as well as inhibition of the release of many secondary hormones. In Drosophila melanogaster and other insects, a 15-amino-acid peptide named allatostatin C(AstC) binds the somatostatin-like receptors. Two AstC receptors have been identified in Drosophila with strong sequence homology to human somatostatin and opioid receptors
LISAVLYGLICIVGLVGNGLVIYVVLRYAKMKTVTNLYILNLAVADECFLIGLPFLIVTMILKYWPFGAA
MCKIYMVLTSINQFTSSFTLTVMSADRYLAVCHPIRSMRYRTPFIAKVVCATTWSISFLVMLPIILYAST
VPDSGRYSCTIVWPDSSAVNGQKAFTLYTFLLGFAIPLLLISVFYTLVILRLRTVGPKNKSKEKRRSHRK
VTRLVLTVISVYIICWLPYWAFQVHLIFLPPGTDMPKWEILMFLLLTVLSYANSMVNPLLYAFLSENFRK
SF
>gnl|CDD|320223 cd15095, 7tmA_KiSS1R, KiSS1-derived peptide (kisspeptin) receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The G protein-coupled KiSS1-derived peptide receptor (GPR54 or kisspeptin receptor) binds the peptide hormone kisspeptin (previously known as metastin), which encoded by the metastasis suppressor gene (KISS1) expressed in various endocrine and reproductive tissues. The KiSS1 receptor is coupled to G proteins of the G(q/11) family, which lead to activation of phospholipase C and increase of intracellular calcium. This signaling cascade plays an important role in reproduction by regulating the secretion of gonadotropin-releasing hormone
WLVPLIFAIIFLVGLAGNSLVIYVVSRHREMRTVTNYYIVNLAVTDLAFLVCCVPFTAALYATPSWVFGD
FMCKFVNYMMQVTVQATCLTLTALSVDRYYAIVHPIRSLRFRTPRVAVVVSACIWIVSFLLSIPVAIYYR
LEEGYWYGPQTYCREVWPSKAFQKAYMIYTVLLTYVIPLAIIAVCYGLILRRLWRRSVDGNNQSEQLSER
ALRQKRKVTRMVIVVVVLFAICWLPNHVLNLWQRFDPNFPETYATYALKIAALCLSYANSAVNPFVYAFM
GENFRKYF
>gnl|CDD|320224 cd15096, 7tmA_AstA_R_insect, allatostatin-A receptor in insects, member of the class A family of seven-transmembrane G protein-coupled receptors. The G protein-coupled AstA receptor binds allatostatin A. Three distinct types of allatostatin have been identified in the insects and crustaceans: AstA, AstB, and AstC. They both inhibit the biosynthesis of juvenile hormone and exert an inhibitory influence on food intake. Therefore, allatostatins are considered as potential targets for insect control
IVVPVIFGLIFIVGLIGNSLVILVVLSNQQMRSTTNILILNLAVADLLFVVFCVPFTATDYVLPTWPFGD
VWCKIVQYLVYVTAYASVYTLVLMSLDRYLAVVHPITSMSIRTERNTLIAIVGIWIVILVANIPVLFLHG
VVSYGFSSEAYSYCTFLTEVGTAAQTFFTSFFLFSYLIPLTLICVLYMLMLRRLRRQKSPGGRRSAESQR
GKRRVTRLVVVVVVVFAICWLPIHIILLLKYYGVLPETVLYVVIQILSNCLAYGNSCVNPILYAFLSQNF
RKAF
>gnl|CDD|320225 cd15097, 7tmA_Gal2_Gal3_R, galanin receptor subtypes 2 and 3, member of the class A family of seven-transmembrane G protein-coupled receptors. The G protein-coupled galanin receptors bind galanin, a neuropeptide that is widely expressed in the brain, peripheral tissues, and endocrine glands. Three receptors subtypes have been so far identified: GAL1, GAL2, and GAL3. The specific functions of each subtype remains mostly unknown, although galanin is thought to be involved in a variety of neuronal functions such as hormone release and food intake. Galanin is implicated in numerous neurological and psychiatric diseases including Alzheimer's disease, depression, eating disorders, epilepsy and stroke, among many others
VIVPVVFSLIFLLGTVGNSLVLAVLLRSGQSGHNTTNLFILNLSVADLCFILFCVPFQATIYSLEGWVFG
SFLCKAVHFFIYLTMYASSFTLAAVSVDRYLAIRYPLRSRELRTPRNAVAAIALIWGLSLLFAGPYLSYY
DLIDYANSTVCMPGWEEARRKAMDTCTFAFGYLIPVLVVSLSYTRTIKYLWTAVDPLEAMSESKRAKRKV
TKMIIIVTALFCLCWLPHHVVILCYLYGDFPFNQATYAFRLLSHCMAYANSCLNPIVYALVSKHFRKGF
>gnl|CDD|320226 cd15098, 7tmA_Gal1_R, galanin receptor subtype 1, member of the class A family of seven-transmembrane G protein-coupled receptors. The G protein-coupled galanin receptors bind galanin, a neuropeptide that is widely expressed in the brain, peripheral tissues, and endocrine glands. Three receptors subtypes have been so far identified: GAL1, GAL2, and GAL3. The specific functions of each subtype remains mostly unknown, although galanin is thought to be involved in a variety of neuronal functions such as hormone release and food intake. Galanin is implicated in numerous neurological and psychiatric diseases including Alzheimer's disease, depression, eating disorders, epilepsy and stroke, among many others
VIVPVVFGLIFCLGVLGNSLVITVLARVKPGKRRSTTNVFILNLSIADLFFLLFCVPFQATIYSLPEWVF
GAFMCKFVHYFFTVSMLVSIFTLVAMSVDRYIAVVHSRTSSSLRTRRNALLGVLVIWVLSLAMASPVAVH
QDLVHHWTASNQTFCWENWPEKQQKPVYVVCTFVFGYLLPLLLITFCYAKVLNHLHKKLKNMSKKSERSK
KKTAQTVLVVVVVFGISWLPHHIIHLWVEFGDFPLTQASFVLRITAHCLAYANSCVNPIIYAFLSENFRK
AY
>gnl|CDD|320227 cd15099, 7tmA_Cannabinoid_R, cannabinoid receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Cannabinoid receptors belong to the class A G-protein coupled receptor superfamily. Two types of cannabinoid receptors, CB1 and CB2, have been identified so far. They are activated by naturally occurring endocannabinoids, cannabis plant-derived cannabinoids such as tetrahydrocannabinol, or synthetic cannabinoids. The CB receptors are involved in the various physiological processes such as appetite, mood, memory, and pain sensation. CB1 receptor is expressed predominantly in central and peripheral neurons, while CB2 receptor is found mainly in the immune system
KAIAVLCFLAGPVTFLENILVLLTILSSTALRRRPSYLFIGSLALADMLASVIFTISFLDFHVFHQRDSR
NLFLFKLGGVTMAFTASVGSLLLTALDRYLCIYQPSNYKLLVTRTRAKVAILLMWCVTIIISFLPLMGWR
CKTWDSPCSRLFPYIDRHYLASWTGLQLVLLFLIIYAYPYILWKAHRHEANMGGPKLGRQQVKGQARMRM
DIRLAKTLSLILLVLAICWLPVLAFMLVDVRVTLTNKQKRMFAFCSMLCLVNSCVNPIIYALRSRELRGA
M
>gnl|CDD|320228 cd15100, 7tmA_GPR3_GPR6_GPR12-like, G protein-coupled receptors 3, 6, 12, and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR3, GPR6, and GPR12 form a subfamily of constitutively active G-protein coupled receptors with dual coupling to G(s) and G(i) proteins. These three orphan receptors are involved in the regulation of cell proliferation and survival, neurite outgrowth, cell clustering, and maintenance of meiotic prophase arrest. They constitutively activate adenylate cyclase to a similar degree as that seen with fully activated G(s)-coupled receptors, and are also able to constitutively activate inhibitory G(i/o) proteins. Lysophospholipids such as sphingosine 1-phosphate (S1P) and sphingosylphosphorylcholine have been detected as the high-affinity ligands for Gpr6 and Gpr12, respectively, which show high sequence homology with GPR3. Also included in this subfamily is GPRx, also known as GPR185, which involved in the maintenance of meiotic arrest in frog oocytes
NPWDIVLCVSGTLIACENAIVVAIIFSTPSLRAPMFLLIGSLALADLLAGLGLILHFVFRYCVYSEALSL
VSVGLLVAAFSASVCSLLAITVDRYLSLYNALTYYSERTLTFTYVMLALLWTLALGLGLLPVLGWNCLRE
GSSCSVVRPLTKNHLAVLAVAFLLVFALMLQLYAQICRIVLRHAHQIALQRHFLAPSHYVATRKGVSTLA
LILGTFAACWIPFAVYCLLGDGSSPALYTYATLLPATYNSMINPIIYAFRNQDIQKVL
>gnl|CDD|341325 cd15101, 7tmA_LPAR, lysophosphatidic acid receptor subfamily, member of the class A family of seven-transmembrane G protein-coupled receptors. The endothelial differentiation gene (Edg) family of G-protein coupled receptors binds blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). The Edg receptors couple and activate at least three different G protein subtypes including G(i/o), G(q/11), and G(12/13)
VLVMGLGITVCIFIMLANLLVIAAIYKNRRFHFPIYYLLANLAAADFFAGLAYFFLMFNTGPNTRRLTVS
TWFLRQGLLDTSLTASVANLLAIAVERHISVMRMQLHSRLSNRRVVVLIVLVWTMAIVMGAIPSVGWNCL
CAIDACSNMAPLYSRSYLVFWAISNLVTFLVMVVVYARIFVYVRRRTNRMSPHTSGSIRNRDTMMSLLKT
VVIVLGAFVVCWTPGLVVLLLDGLCCRQCNVLAVEKFFLLLAEFNSAVNPIIYSYRDKEMSGTF
>gnl|CDD|320230 cd15102, 7tmA_S1PR, sphingosine-1-phosphate receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. The endothelial differentiation gene (Edg) family of G-protein coupled receptors binds blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). The Edg receptors couple and activate at least three different G protein subtypes including G(i/o), G(q/11), and G(12/13)
GATSVVFVAICCFIVLENLLVLIAIWRHMKFHRPMYYFLGNLALSDLLAGAAYLANILLSGARTLRLSPA
QWFLREGSMFVALSASVFSLLAIAIERHLTMAKMKPYGASKTSRVLLLIGACWLISLLLGGLPILGWNCL
GALDACSTVLPLYSKHYVLFCVTIFAGILAAIVALYARIYCLVRASGRKATRASASPRSLALLKTVLIVL
LVFIACWGPLFILLLLDVACPVKTCPILYKADWFLALAVLNSALNPIIYTLRSRELRRAV
>gnl|CDD|320231 cd15103, 7tmA_MCR, melanocortin receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. The melanocortin receptor (MCR) subfamily is a member of the class A family of seven-transmembrane G-protein coupled receptors. MCRs bind a group of pituitary peptide hormones known as melanocortins, which include adrenocorticotropic hormone (ACTH) and the different isoforms of melanocyte-stimulating hormones. There are five known subtypes of the MCR subfamily. MC1R is involved in regulating skin pigmentation and hair color. ACTH (adrenocorticotropic hormone) is the only endogenous ligand for MC2R, which shows low sequence similarity with other melanocortin receptors. Mutations in MC2R cause familial glucocorticoid deficiency type 1, in which patients have elevated plasma ACTH and low cortisol levels. MC3R is expressed in many parts of the brain and peripheral tissues and involved in the regulation of energy homeostasis. MC4R is expressed primarily in the central nervous system and involved in both eating behavior and sexual function. MC5R is widely expressed in peripheral tissues and is mainly involved in the regulation of exocrine gland function
FISPEVFLTLGIVSLLENILVILAIAKNKNLHSPMYFFICSLAVADMLVSVSNALETIVIILLNNGYLVP
RDSFEQHIDNVIDSMICSSLLASICSLLAIAVDRYITIFYALRYHSIMTVRRAGVIITAIWVFCTVCGIL
FIIYSDSVPVIICLISMFFAMLVLMASLYVHMFLLARSHVKKIAALPGQRSTRQRANMKGAVTLTILLGV
FIFCWAPFFLHLTLMISCPSNPYCACYMSHFNVYLILIMCNSVIDPLIYAFRSQELRKTF
>gnl|CDD|320232 cd15104, 7tmA_GPR119_R_insulinotropic_receptor, G protein-coupled receptor 119, also called glucose-dependent insulinotropic receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR119 is activated by oleoylethanolamide (OEA), a naturally occurring bioactive lipid with hypophagic and anti-obesity effects. Immunohistochemistry and double-immunofluorescence studies revealed the predominant GPR119 localization in pancreatic polypeptide (PP)-cells of islets. In addition, GPR119 expression is elevated in islets of obese hyperglycemic mice as compared to control islets, suggesting a possible involvement of this receptor in the development of obesity and diabetes. GPR119 has a significant sequence similarity with the members of the endothelial differentiation gene family. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
AAGVILAVLSPLIITGNLLVIVALLKLIRKKDTKSNCFLLNLAIADFLVGLAIPGLATDELLSDGENTQK
VLCLLRMCFVITSCAASVLSLAAIAFDRYLALKQPLRYKQIMTGKSAGALIAGLWLYSGLIGFLPLISPQ
FQQTSYKGKCSFFAAFHPRVLLVLSCMVFFPALLLFVFCYCDILKIARVHSRAIYKVEHALARQIHPRRT
LSDFKAARTVAVLIGCFLLSWLPFQITGLVQALCDECKLYDVLEDYLWLLGLCNSLLNPWIYAFWQKEVR
RAL
>gnl|CDD|320233 cd15105, 7tmA_MrgprA, mas-related G protein-coupled receptor subtype A, member of the class A family of seven-transmembrane G protein-coupled receptors. The Mas-related G-protein coupled receptor (Mrgpr) family constitutes a group of orphan receptors exclusively expressed in nociceptive primary sensory neurons and mast cells in the skin. Members of the Mrgpr family have been implicated in the modulation of nociception, pruritus (itching), and mast cell degranulation. The Mrgpr family in rodents and humans contains more than 50 members that can be grouped into 9 distinct subfamilies: MrgprA, B, C (MrgprX1), D, E, F, G, H (GPR90), and the primate-specific MrgprX subfamily. Some Mrgprs can be activated by endogenous ligands such as beta-alanine, adenine (a cell metabolite and potential transmitter), RF-amide related peptides, or salusin-beta (a bioactive peptide). However, the effects of these agonists are not clearly understood, and the physiological role of the individual receptor family members remains to be determined
LIPNLMIIIFGLVGLTGNAIVFWLLGFRLHRNAFSVYILNLALADFLFLLCHIIDSTLLLLKVFYPNIIF
LPCFYTIMMVLYITGLSMLSAISTERCLSVLCPIWYRCRRPEHTSTVMCAVIWVLSLLICILNRYFCGFL
DTKYENDSVCLASNFFTAAYLMFLFVVLCLSSLALLARLFCGAGQMKLTRLYVTIMLTVLVFLLCGLPFG
IYWFLLFWIKDDFHVLDYGLYLASVVLTAVNSCANPIIYFFVGSFRHRLKHQTLKMVLQSALQDTP
>gnl|CDD|320234 cd15106, 7tmA_MrgprX-like, primate-specific mas-related G protein-coupled receptor subtype X-like, member of the class A family of seven-transmembrane G protein-coupled receptors. The Mas-related G-protein coupled receptor (Mrgpr) family constitutes a group of orphan receptors exclusively expressed in nociceptive primary sensory neurons and mast cells in the skin. Members of the Mrgpr family have been implicated in the modulation of nociception, pruritus (itching), and mast cell degranulation. The Mrgpr family in rodents and humans contains more than 50 members that can be grouped into 9 distinct subfamilies: MrgprA, B, C (MrgprX1), D, E, F, G, H (GPR90), and the primate-specific MrgprX subfamily. Some Mrgprs can be activated by endogenous ligands such as beta-alanine, adenine (a cell metabolite and potential transmitter), RF-amide related peptides, or salusin-beta (a bioactive peptide). However, the effects of these agonists are not clearly understood, and the physiological role of the individual receptor family members remains to be determined
LSLTFLTCIISLVGLTGNAVVLWLLGFRMRRNAFSVYILNLAAADFLFLCCHIIDSLLRLINIFHIISIP
KILTNVMTFPYFAGLSMLSAISTERCLSVLWPIWYRCHRPRHLSAVVCVLLWALSLLLSILEWKFCGFLF
SGADSHWCQTFDFITTAWLIFLFVVLCGSSLALLVRILCGSRKMPLTRLYVTILLTVLVFLLCGLPFGIQ
WFLLLWIHIDLEVLFCHVYLVSVVLSCLNSSANPIIYFFVGSFRQRQNRQNLKLVLQRALQDIP
>gnl|CDD|320235 cd15107, 7tmA_MrgprB, mas-related G protein-coupled receptor subtype B, member of the class A family of seven-transmembrane G protein-coupled receptors. The Mas-related G-protein coupled receptor (Mrgpr) family constitutes a group of orphan receptors exclusively expressed in nociceptive primary sensory neurons and mast cells in the skin. Members of the Mrgpr family have been implicated in the modulation of nociception, pruritus (itching), and mast cell degranulation. The Mrgpr family in rodents and humans contains more than 50 members that can be grouped into 9 distinct subfamilies: MrgprA, B, C (MrgprX1), D, E, F, G, H (GPR90), and the primate-specific MrgprX subfamily. Some Mrgprs can be activated by endogenous ligands such as beta-alanine, adenine (a cell metabolite and potential transmitter), RF-amide related peptides, or salusin-beta (a bioactive peptide). However, the effects of these agonists are not clearly understood, and the physiological role of the individual receptor family members remains to be determined
NTMNFLSIIIALVGLAGNAIVLWLLGFHMHRNAFSVYILNLAGADFLFLCTQIVFSLEIVLQFHSIDIHI
PLFLLTVTMFAYLAGLSMITAISIERCLSVMWPIWYHCQRPRHTSAVICTLLWVLSLLLSLLEGKGCGFL
FSTYDYYWCWTLDLITTAWLIVLFVVLSGSSLALLVRIFCGSHRIPVTRLYVTIALTVLVFLIFGLPFGI
YWFLLKWIEEFYIVPCCGFYEVILFLSCVNSCANPIIYFLVGSIRHHRFQRKTLKLLLQRAMQDTP
>gnl|CDD|320236 cd15108, 7tmA_MrgprD, mas-related G protein-coupled receptor subtype D, member of the class A family of seven-transmembrane G protein-coupled receptors. The Mas-related G-protein coupled receptor (Mrgpr) family constitutes a group of orphan receptors exclusively expressed in nociceptive primary sensory neurons and mast cells in the skin. Members of the Mrgpr family have been implicated in the modulation of nociception, pruritus (itching), and mast cell degranulation. The Mrgpr family in rodents and humans contains more than 50 members that can be grouped into 9 distinct subfamilies: MrgprA, B, C (MrgprX1), D, E, F, G, H (GPR90), and the primate-specific MrgprX subfamily. Some Mrgprs can be activated by endogenous ligands such as beta-alanine, adenine (a cell metabolite and potential transmitter), RF-amide related peptides, or salusin-beta (a bioactive peptide). However, the effects of these agonists are not clearly understood, and the physiological role of the individual receptor family members remains to be determined
EVLSALVMFTCVCGMAGNGLVVWLLSCRGRRTPFCVYVLHLAVADLLFLLCMASTLSLETSPLVITHDLA
YEVVRRVKYFAYTASLSLLTAISTQRCLSVLFPIWYKCHQPRHLSAVVCALLWALSLLMNVLASFFCSEF
WHPDEWQCFKVDMVFSFLIMGIFTPVMALSSLILFVRVRRSSRQWRRRPTRLYVVVLASVLVFLACALPL
GIYWFLLYWLDLPQEVKTLFSCLSRLSSSVSSSANPVIYFLVGSRGSRRLREPLGAVLQRALREEP
>gnl|CDD|320237 cd15109, 7tmA_MrgprF, mas-related G protein-coupled receptor subtype F, member of the class A family of seven-transmembrane G protein-coupled receptors. The Mas-related G-protein coupled receptor (Mrgpr) family constitutes a group of orphan receptors exclusively expressed in nociceptive primary sensory neurons and mast cells in the skin. Members of the Mrgpr family have been implicated in the modulation of nociception, pruritus (itching), and mast cell degranulation. The Mrgpr family in rodents and humans contains more than 50 members that can be grouped into 9 distinct subfamilies: MrgprA, B, C (MrgprX1), D, E, F, G, H (GPR90), and the primate-specific MrgprX subfamily. Some Mrgprs can be activated by endogenous ligands such as beta-alanine, adenine (a cell metabolite and potential transmitter), RF-amide related peptides, or salusin-beta (a bioactive peptide). However, the effects of these agonists are not clearly understood, and the physiological role of the individual receptor family members remains to be determined
AVMNYIFLLLCLCGLVGNGLVLWFFGFSIKRNPFSIYFLHLASADVGYLFSKAVFSILNTGGFLGTFADY
IRSVSRILGLCTFLTGVSLLPAISIERCVSVIFPTWYWRRRPKRLSAVVCALLWMLSLLVTCIHNYFCVF
LGREAPGAACRHMDIFLGILLFLLFCPLMVLPCLALILHVECRARRRQRSAKLNHVILAMVSVFLVSSIY
LGIDWFLFWVFQIPAPFPEYVTDLCICINSSAKPIVYFLAGRDKSQRLWEPLRVVFQRALRDGA
>gnl|CDD|320238 cd15110, 7tmA_MrgprH, mas-related G protein-coupled receptor subtype H, member of the class A family of seven-transmembrane G protein-coupled receptors. The Mas-related G-protein coupled receptor (Mrgpr) family constitutes a group of orphan receptors exclusively expressed in nociceptive primary sensory neurons and mast cells in the skin. Members of the Mrgpr family have been implicated in the modulation of nociception, pruritus (itching), and mast cell degranulation. The Mrgpr family in rodents and humans contains more than 50 members that can be grouped into 9 distinct subfamilies: MrgprA, B, C (MrgprX1), D, E, F, G, H (GPR90), and the primate-specific MrgprX subfamily. Some Mrgprs can be activated by endogenous ligands such as beta-alanine, adenine (a cell metabolite and potential transmitter), RF-amide related peptides, or salusin-beta (a bioactive peptide). However, the effects of these agonists are not clearly understood, and the physiological role of the individual receptor family members remains to be determined
LIEVWVSLIICLLGLVGNGIVLWFLGFRIRRNPFTVYILHLAIADFTFLLCIFILSIMYIGPFNFSHSRD
YVAMLIFIILFLFGYNTGLYLLTAISVERCLSVLYPIWYRCHRPKHQSAIVCGLLWALSVLMTSLEYLMC
IDEGFHVRNECRAVLIFIGILTFLVFTPLMLISSLILFIKVRCNSQRRHPGKLYIIIMLTVIFFLIFAMP
MRVLLLLNYLHHSSFLFSNPVPFLLSTVNSSINPIVYFLVGSLRRKRIKKSLKVALQRVFEDKA
>gnl|CDD|320239 cd15111, 7tmA_MrgprG, mas-related G protein-coupled receptor subtype G, member of the class A family of seven-transmembrane G protein-coupled receptors. The Mas-related G-protein coupled receptor (Mrgpr) family constitutes a group of orphan receptors exclusively expressed in nociceptive primary sensory neurons and mast cells in the skin. Members of the Mrgpr family have been implicated in the modulation of nociception, pruritus (itching), and mast cell degranulation. The Mrgpr family in rodents and humans contains more than 50 members that can be grouped into 9 distinct subfamilies: MrgprA, B, C (MrgprX1), D, E, F, G, H (GPR90), and the primate-specific MrgprX subfamily. Some Mrgprs can be activated by endogenous ligands such as beta-alanine, adenine (a cell metabolite and potential transmitter), RF-amide related peptides, or salusin-beta (a bioactive peptide). However, the effects of these agonists are not clearly understood, and the physiological role of the individual receptor family members remains to be determined
KVVFYLTLIVSLAGLVGNGLVLWHLGFHIKKGPFSNYLLHLAAADFLFLSCQVGFSIAQAALGSEDTLYF
VVTFLWFAAGLWLLAAFSVERCLSYLFPACCQGCRPRWTSAVLCAVVWVLTLPAVLLPANACGLLRNGSR
LLVCLRYHAASVTWLLVLACVACGAGLVLFIWVCCCSQRPRPKFYGIVLGSGLLLLFCGLPFVLYWSLRP
LLNFLLPMFPPLATLLACIDSSSKPLIYYLMGRQPGKREPLRVVLQRALGEGA
>gnl|CDD|320240 cd15112, 7tmA_MrgprE, mas-related G protein-coupled receptor subtype E, member of the class A family of seven-transmembrane G protein-coupled receptors. The Mas-related G-protein coupled receptor (Mrgpr) family constitutes a group of orphan receptors exclusively expressed in nociceptive primary sensory neurons and mast cells in the skin. Members of the Mrgpr family have been implicated in the modulation of nociception, pruritus (itching), and mast cell degranulation. The Mrgpr family in rodents and humans contains more than 50 members that can be grouped into 9 distinct subfamilies: MrgprA, B, C (MrgprX1), D, E, F, G, H (GPR90), and the primate-specific MrgprX subfamily. Some Mrgprs can be activated by endogenous ligands such as beta-alanine, adenine (a cell metabolite and potential transmitter), RF-amide related peptides, or salusin-beta (a bioactive peptide). However, the effects of these agonists are not clearly understood, and the physiological role of the individual receptor family members remains to be determined
LFILSLTELLGLGGLLGNGLVLWLLSSNVYRNPFSIYLLDVACADLIFLCCHMVAIIPELLQNHLSFPHF
VYDSLLALRFFCYIVGLSLLAAISAEQCLATLFPAWYQCRRPRHLTTCVCALLWALCLLLHLLLSGACTQ
FFGGPSGHLCGRLWLVRAVLLALLCCTMCVSSLVLLLRVERGPPRQRPRGFPALVLLTVLLFLFCGLPFG
IYWLSLNLLWRIPHYFYHFSFLMAAVHSAAKPPIYFCLGSLRGGRFREPLRLVLQRALGDEA
>gnl|CDD|320241 cd15113, 7tmA_MAS1L, mas-related G protein-coupled receptor 1-like (MAS1L), member of the class A family of seven-transmembrane G protein-coupled receptors. MAS1L is also called MAS1 oncogene-like (MAS1-like) or mas-related G-protein coupled receptor MRG. MAS1L is a G protein-coupled receptor that only found in primates. The angiotensin-II metabolite angiotensin is an endogenous ligand for MAS1L. The Mas-related G-protein coupled receptor (Mrgpr) family constitutes a group of orphan receptors exclusively expressed in nociceptive primary sensory neurons and mast cells in the skin. Members of the Mrgpr family have been implicated in the modulation of nociception, pruritus (itching), and mast cell degranulation. The Mrgpr family in rodents and humans contains more than 50 members that can be grouped into 9 distinct subfamilies: MrgprA, B, C (MrgprX1), D, E, F, G, H (GPR90), and the primate-specific MrgprX subfamily. Some Mrgprs can be activated by endogenous ligands such as beta-alanine, adenine (a cell metabolite and potential transmitter), RF-amide related peptides, or salusin-beta (a bioactive peptide). However, the effects of these agonists are not clearly understood, and the physiological role of the individual receptor family members remains to be determined
NVVFPLAVLVSLCGLVGNGVVFWLLCCGVRSNPYMVYILNLAAADVINLSCSAVILLEVTLLLYHGVTLF
VADFLEPVSYFSDTVGLCLLVAISTESCLCVLFPIWCCHRPKYTSAVVSTLSWGLPLSLHIVKSLCLYWE
HGLACDIFHKGFGIFHALISLVMCVSSLTLTIRSLCCSQQCSATRIYHVVRISAIMFLLWGLPLVVAPLL
PDFEYLTTTFDLLLLLSIIVSSANPIIYFLVGSLRRKRLKESLKVILQRALADKM
>gnl|CDD|320242 cd15114, 7tmA_C5aR, complement component 5a anaphylatoxin chemotactic receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. The anaphylatoxin receptors are a group of G-protein coupled receptors which bind anaphylatoxins; members of this group include C3a receptors and C5a receptors. Anaphylatoxins are also known as complement peptides (C3a, C4a and C5a) that are produced from the activation of the complement system cascade. These complement anaphylatoxins can trigger degranulation of endothelial cells, mast cells, or phagocytes, which induce a local inflammatory response and stimulate smooth muscle cell contraction, histamine release, and increased vascular permeability. They are potent mediators involved in chemotaxis, inflammation, and generation of cytotoxic oxygen-derived free radicals. In humans, a single receptor for C3a (C3AR1) and two receptors for C5a (C5AR1 and C5AR2, also known as C5L2 or GPR77) have been identified, but there is no known receptor for C4a
VVALVLYAVVFLVGVPGNALVAWVTGFEAKRSVNAVWFLNLAVADLLCCLSLPILAVPIAQDGHWPFGAA
ACKLLPSLILLNMYASVLLLTAISADRCLLVLRPVWCQNHRRARLAWIACGAAWLLALLLTVPSFIYRRI
HQEHFPEKTVCVVDYGGSTGVEWAVAIIRFLLGFLGPLVVIASCHGVLLVRTWSRRRQKSRRTLKVVTAV
VVGFFLCWTPYHVVGLIIAASAPNSRLLANALKADPLTVSLAYINSCLNPIIYVVAGRGFRKSL
>gnl|CDD|320243 cd15115, 7tmA_C3aR, complement component 3a anaphylatoxin chemotactic receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. The anaphylatoxin receptors are a group of G-protein coupled receptors which bind anaphylatoxins; members of this group include C3a receptors and C5a receptors. Anaphylatoxins are also known as complement peptides (C3a, C4a and C5a) that are produced from the activation of the complement system cascade. These complement anaphylatoxins can trigger degranulation of endothelial cells, mast cells, or phagocytes, which induce a local inflammatory response and stimulate smooth muscle cell contraction, histamine release, and increased vascular permeability. They are potent mediators involved in chemotaxis, inflammation, and generation of cytotoxic oxygen-derived free radicals. In humans, a single receptor for C3a (C3AR1) and two receptors for C5a (C5AR1 and C5AR2, also known as C5L2 or GPR77) have been identified, but there is no known receptor for C4a
ILSLVVLSLTFLLGVPGNGLVIWVAGLKMKRTVNTIWFLNLAVADLLCCLSLPFSIAHLLLNGHWPYGRF
LCKLLPSIIVLNMFASVFTLTAISLDRFLLVIKPVWAQNHRSVLLACLLCGCIWILALLLCLPVFIYRTT
VTDGNHTRCGYDFLVAITITRAVFGFLLPLLIIAACYSFIAFRMQRGRFAKSQSKTFRVIIAVVVAFFVC
WAPYHIIGILSLYGDPPLSKVLMSWDHLSIALAYANSCLNPVLYVFMGKDFKKKA
>gnl|CDD|320244 cd15116, 7tmA_CMKLR1, chemokine-like receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. Chemokine receptor-like 1 (also known as Chemerin receptor 23) is a GPCR for the chemoattractant adipokine chemerin, also known as retinoic acid receptor responder protein 2 (RARRES2), and for the omega-3 fatty acid derived molecule resolvin E1. Interaction with chemerin induces activation of the MAPK and PI3K signaling pathways leading to downstream functional effects, such as a decrease in immune responses, stimulation of adipogenesis, and angiogenesis. On the other hand, resolvin E1 negatively regulates the cytokine production in macrophages by reducing the activation of MAPK1/3 and NF-kB pathways. CMKLR1 is prominently expressed in dendritic cells and macrophages
ILSMVIYSVVFVLGVLGNGLVIFITGFKMKKTVNTVWFLNLAVADFLFTFFLPFSIAYTAMDFHWPFGRF
MCKLNSFLLFLNMFTSVFLLTVISIDRCISVVFPVWSQNHRSVRLASLVSLAVWVVAFFLSSPSFIFRDT
APSQNNNKIICFNNFSLSGDNSSPEVNQLRNMRHQVMTITRFLLGFLIPFTIIICCYAAIVLKLKRNRLA
KSSKPFKIIAAVIVTFFLCWAPYHILNLLEMEATRSPASVFKIGLPITSSLAFINSCLNPILYVFMGQDF
KKFK
>gnl|CDD|320245 cd15117, 7tmA_FPR-like, N-formyl peptide receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. The formyl peptide receptors (FPRs) are chemoattractant GPCRs that involved in mediating immune responses to infection. They are expressed at elevated levels on polymorphonuclear and mononuclear phagocytes. FPRs bind N-formyl peptides, which are derived from the mitochondrial proteins of ruptured host cells or invading pathogens. Activation of FPRs by N-formyl peptides such as N-formyl-Met-Leu-Phe (FMLP) triggers a signaling cascade that stimulates neutrophil accumulation, phagocytosis and superoxide production. These responses are mediated through a pertussis toxin-sensitive G(i) protein that activates a PLC-IP3-calcium signaling pathway. While FPRs are involved in host defense responses to bacterial infection, they can also suppress the immune system under certain conditions. Yet, the physiological role of the FPR family is not fully understood
ILSLVIYSSAFVLGTLGNGLVIWVTGFRMTRTVTTVCFLNLAVADFAFCLFLPFSVVYTALGFHWPFGWF
LCKLYSTLVVFNLFASVFLLTLISLDRCVSVLWPVWARNHRTPARAALVAVGAWLLALALSGPHLVFRDT
RKENGCTHCYLNFDPWNETAEDPVLWLETVVQRLSAQVITRFVLGFLVPLVIIGGCYGLIAARLWREGWV
HSSRPFRVLTAVVAAFFLCWFPFHLVSLLELVVILNQKEDLNPLLILLLPLSSSLACVNSCLNPLLYVFV
GRDFRERL
>gnl|CDD|320246 cd15118, 7tmA_PD2R2_CRTH2, prostaglandin D2 receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Prostaglandin D2 receptor, also known as CRTH2, is a chemoattractant G-protein coupled receptor expressed on T helper type 2 cells that binds prostaglandin D2 (PGD2). PGD2 functions as a mast cell-derived mediator to trigger asthmatic responses and also causes vasodilation. PGD2 exerts its inflammatory effects by binding to two G-protein coupled receptors, the D-type prostanoid receptor (DP) and PD2R2 (CRTH2). PD2R2 couples to the G protein G(i/o) type which leads to a reduction in intracellular cAMP levels and an increase in intracellular calcium. PD2R2 is involved in mediating chemotaxis of Th2 cells, eosinophils, and basophils generated during allergic inflammatory processes. CRTH2 (PD2R2), but not DP receptor, undergoes agonist-induced internalization which is one of key processes that regulates the signaling of the GPCR
VATICLHGIVSTLGIVENLLILWVVGFRLRRTVISIWILNLALSDLLATLSLPFFTYYLASGHTWELGTT
FCRIHSSIFFLNMFVSGFLLAAISLDRCLLVVKPVWAQNHRNVAAAKKICGVIWAMALINTIPYFVFRDV
IERKDGRKLCYYNFALFSPSPDNNHPICKQRQEGLAISKLLLAFLIPLVIIAVSYAVVSLIIRHRCRRRP
GRFVRLVVSVVVSFALCWAPYHIFSIIEVMAHNQHSLRPLVIQGLPFATTLAFLNSVLNPVLYVFSCPDF
CNKI
>gnl|CDD|320247 cd15119, 7tmA_GPR1, G protein-coupled receptor 1 for chemerin, member of the class A family of seven-transmembrane G protein-coupled receptors. G-protein coupled receptor 1 (GPR1) belongs to the class A of the seven transmembrane domain receptors. This is an orphan receptor that can be activated by the leukocyte chemoattractant chemerin, thereby suggesting that some of the anti-inflammatory actions of chemerin may be mediated through GPR1. GPR1 is most closely related to another chemerin receptor CMKLR1. In an in-vitro study, GPR1 has been shown to act as a co-receptor to allow replication of HIV viruses
IVSIVIYIVAFVLGVPGNAIVIWVTGFKWKKTVNTLWFLNLAIADFVFVLFLPLHITYVALDFHWPFGVW
LCKINSFVAVLNMFASVLFLTVISLDRYISLAHPVWSHRYRTLKSALILCGIVWLSAAAISGPALYFRDT
MELSINVTICFNNFHKHDGDLIVMRHTILVWVRFFFGFLFPLLTMVVCYSLLAIKVKRRTLLISSKFFWT
ISAVIVAFFVCWTPYHIFSILELSIHHSSYLHNVLRAGIPLATSLAFINSCLNPILYVLIGKKFKAHL
>gnl|CDD|320248 cd15120, 7tmA_GPR33, orphan receptor GPR33, member of the class A family of seven-transmembrane G protein-coupled receptors. G-protein coupled receptor GPR33, an orphan member of the chemokine-like receptor family, was originally identified as a pseudogene in humans as well as in several apes and rodent species. Although the intact GPR33 allele is still present in a small fraction of the human population, the human GPR33 contains a premature stop codon. The amino acid sequence of GPR33 shares a high degree of sequence identity with the members of the chemokine and chemoattractant receptors that control leukocyte chemotaxis. The human GPR33 is expressed in spleen, lung, heart, kidney, pancreas, thymus, gonads, and leukocytes
VLIAVALFVTFLVGLVVNGLYLWVLGFKMRRTVNTLWFLHLILSNLIFTLILPFMAVHVLMDNHWAFGTV
LCKVLNSTLSVGMFTSVFLLTAISLDRYLLTLHPVWSRQHRTNRWASAIVLGVWISAILLSIPYLAFRET
RLDEKGKTICQNNYALSTNWESAEVQASRQWIHVAMFVFRFLLGFLLPFLIITFCYVRMALKMKERGLAR
SSKPFKVMFTAVVSFFVCWLPYHLHSGLVLTRGRPPSLTDITLLLTVGTTCFNTCFTPVLYLFVGENFKK
VL
>gnl|CDD|320249 cd15121, 7tmA_LTB4R1, leukotriene B4 receptor subtype 1 (LTB4R1 or BLT1), member of the class A family of seven-transmembrane G protein-coupled receptors. Leukotriene B4 (LTB4), a metabolite of arachidonic acid, is a powerful chemotactic activator for granulocytes and macrophages. Two receptors for LTB4 have been identified: a high-affinity receptor (LTB4R1 or BLT1) and a low-affinity receptor (TB4R2 or BLT2). Both BLT1 and BLT2 receptors belong to the rhodopsin-like G-protein coupled receptor superfamily and primarily couple to G(i) proteins, which lead to chemotaxis, calcium mobilization, and inhibition of adenylate cyclase. In some cells, they can also couple to the Gq-like protein, G16, and activate phospholipase C. LTB4 is involved in mediating inflammatory processes, immune responses, and host defense against infection. Studies have shown that LTB4 stimulates leukocyte extravasation, neutrophil degranulation, lysozyme release, and reactive oxygen species generation
QLGIAILSLAFILGFPGNLFVVWSVLCRMKKRSVTCILVLNLALADAAVLLTAPFFLHFLSGGGWEFGSV
VCKLCHYVCGVSMYASIFLITLMSMDRCLAVAKPFLSQKMRTKRSVRALLLAIWIVAFLLSLPMPFYRTV
LKKNINMKLCIPYHPSVGHEAFQYLFETITGFLLPFTAIVTCYSTIGRRLRSARFRRKRRTNRLVVLIIA
TFALFWLPYHVVNLIQVAGALQNQAGNASVLKAAKLARPNVTALAFLSSSVNPVLYAFAGGSLIRSAG
>gnl|CDD|320250 cd15122, 7tmA_LTB4R2, leukotriene B4 receptor subtype 2 (LTB4R2 or BLT2), member of the class A family of seven-transmembrane G protein-coupled receptors. Leukotriene B4 (LTB4), a metabolite of arachidonic acid, is a powerful chemotactic activator for granulocytes and macrophages. Two receptors for LTB4 have been identified: a high-affinity receptor (LTB4R1 or BLT1) and a low-affinity receptor (TB4R2 or BLT2). Both BLT1 and BLT2 receptors belong to the rhodopsin-like G-protein coupled receptor superfamily and primarily couple to G(i) proteins, which lead to chemotaxis, calcium mobilization, and inhibition of adenylate cyclase. In some cells, they can also couple to the Gq-like protein, G16, and activate phospholipase C. LTB4 is involved in mediating inflammatory processes, immune responses, and host defense against infection. Studies have shown that LTB4 stimulates leukocyte extravasation, neutrophil degranulation, lysozyme release, and reactive oxygen species generation
ATGTIFLLLAALLGLPGNGFIIWSILWKMKARGRSVTCILILNLAVADGAVLLLTPFFITFLTRKTWPFG
QAVCKAVYYLCCLSMYASIFIIGLMSLDRCLAVTRPYLAQSLRKKALVRKILLAIWLLALLLALPAFVYR
HVWKDEGMNDRICEPCHASRGHAIFHYTFETLVAFVLPFGVILFSYSVILVRLKGARFRRRARVEKLIAA
IVVAFALLWVPYHVVNLLQVVANLAPGEVLEKLGGAAKAARAGATALAFFSSSVNPLLYVFAAGDLIKTS
G
>gnl|CDD|320251 cd15123, 7tmA_BRS-3, bombesin receptor subtype 3, member of the class A family of seven-transmembrane G protein-coupled receptors. BRS-3 is classified as an orphan receptor and belongs to the bombesin subfamily of G-protein coupled receptors, whose members also include neuromedin B receptor (NMBR) and gastrin-releasing peptide receptor (GRPR). Bombesin is a tetradecapeptide, originally isolated from frog skin. Mammalian bombesin-related peptides are widely distributed in the gastrointestinal and central nervous systems. The bombesin family receptors couple primarily to the G proteins of G(q/11) family. BRS-3 interacts with known naturally-occurring bombesin-related peptides with low affinity; however, no endogenous high-affinity ligand to the receptor has been identified. BRS-3 is suggested to play a role in sperm cell division and maturation
CAIYVTYAVIISVGILGNAILIKVFFKIKSMQTVPNIFITSLAFGDLLLLLTCVPVDATRYIADTWLFGR
IGCKLLSFIQLTSVGVSVFTLTVLSADRYRAIVKPLELQTSDAVLKTCCKAGCVWIVSMLFAIPEAVFSD
LYSFRDPEKNTTFEACAPYPVSEKILQEIHSLLCFLVFYIIPLSIISVYYFLIARTLYKSTFNMPAEEHS
HARKQIESRKRVAKTVLVLVALFAFCWLPNHILYLYRSFTYHTSVDSSAFHLIATIFSRVLAFSNSCVNP
FALYWLSKSFRQHF
>gnl|CDD|320252 cd15124, 7tmA_GRPR, gastrin-releasing peptide receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The gastrin-releasing peptide receptor (GRPR) is a G-protein coupled receptor whose endogenous ligand is gastrin releasing peptide. GRP shares high sequence homology with the neuropeptide neuromedin B in the C-terminal region. This receptor is high glycosylated and couples to a pertussis-toxin-insensitive G protein of the family of Gq/11, which leads to the activation of phospholipase C. Gastrin-releasing peptide (GRP) is a potent mitogen for neoplastic tissues and involved in regulating multiple functions of the gastrointestinal and central nervous systems. These include the release of gastrointestinal hormones, the contraction of smooth muscle cells, and the proliferation of epithelial cells. GRPR belongs to the bombesin subfamily of G-protein coupled receptors, whose members also include neuromedin B receptor (NMBR) and bombesin receptor subtype 3 (BRS-3). Bombesin is a tetradecapeptide, originally isolated from frog skin
YAIPTVYGIIILIGLIGNITLIKIFCTVKSMRNVPNLFISSLALGDLLLLVTCAPVDASRYLADEWLFGR
VGCKLIPFIQLTSVGVSVFTLTALSADRYKAIVRPMDIQASNALMKICLKAALIWILSMLLAIPEAVFSD
LHPFYDKSTNKTFVSCAPYPHSNELHPKIHSMASFLIFYVIPLSIISVYYYFIAKNLIRSAYNLPVEGNV
HVRRQIESRKRLAKTVLVFVGLFAFCWLPNHIIYLYRSYHYSEVDTSMLHFVSSICARILAFTNSCVNPF
ALYLLSKSFRKQF
>gnl|CDD|320253 cd15125, 7tmA_NMBR, neuromedin B receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The neuromedin B receptor (NMBR), also known as BB1, is a G-protein coupled receptor whose endogenous ligand is the neuropeptide neuromedin B. Neuromedin B is a potent mitogen and growth factor for normal and cancerous lung and for gastrointestinal epithelial tissues. NMBR is widely distributed in the CNS, with especially high levels in olfactory nucleus and thalamic regions. The receptor couples primarily to a pertussis-toxin-insensitive G protein of the Gq/11 family, which leads to the activation of phospholipase C. NMBR belongs to the bombesin subfamily of G-protein coupled receptors, whose members also include gastrin-releasing peptide receptor (GRPR) and bombesin receptor subtype 3 (BRS-3). Bombesin is a tetradecapeptide, originally isolated from frog skin
CVIPSLYLLIITVGLLGNITLVKIFITNSAMRSVPNIFISSLAAGDLLLLVTCVPVDASRYFYEEWMFGT
VGCKLIPVIQLTSVGVSVFTLTALSADRYKAIVNPMDIQTSSAVLRTCLKAIAIWVVSVLLAVPEAVFSE
VAHIMPDDNTTFTACIPYPQTDEMHPKIHSVLIFLVYFLIPLAIISIYYYHIAKTLIKSAHNIPGEYSEH
SKRQMETRKRLAKIVLVFVGLFAFCWFPNHVLYMYRSFNYNEIDSSLGHMIVTLVARVLSFCNSCVNPFA
LYLLSESFRRHF
>gnl|CDD|320254 cd15126, 7tmA_ETBR-LP2, endothelin B receptor-like protein 2, member of the class A family of seven-transmembrane G protein-coupled receptors. Endothelin B receptor-like protein 2, also called GPR37L1, is almost exclusively expressed in the nervous system. It has recently been shown to act as a receptor for the neuropeptide prosaptide, the active fragment of the secreted neuroprotective and glioprotective factor prosaposin (also called sulfated glycoprotein-1). Both prosaptide and prosaposin protect primary astrocytes against oxidative stress. GPR37L1 is part of the class A family of GPCRs that includes receptors for hormones, neurotransmitters, sensory stimuli, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
YGILLLALVVFAVGIVGNLSVMCIVWHSYYLKSAWNSILASLALWDFLVLFFCLPVVVFNEITKKRLLGD
VSCRVVPYMEVTSLGVTTFSLCALGIDRFHAATSPQPKARPVERCQSILAKLAVIWVGSMTLAVPELLLW
QLAQETSPGSGMVIDTCIMKPSPNLPESLYSLVLTYQNARMWWYFGCYFCLPILFTVTCQLVTLRVSGTS
GSSKECKDIKHGQCERQLNCTVAGLAVVYGVCTLPENVCNIVVAYTSLEVSDQTLDLLSLINQFFLFFKC
AVTPVLLLCLCKPLGQAF
>gnl|CDD|320255 cd15127, 7tmA_GPR37, G protein-coupled receptor 37, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR37, also called parkin-associated endothelin-like receptor (Pael-R), was isolated from a set of human brain frontal lobe expressed sequence tags. It is highly expressed in the mammalian CNS. It is a substrate of parkin and is involved in the pathogenesis of Parkinson's disease. GPR37 has recently been shown to act as a receptor for the neuropeptide prosaptide, the active fragment of the secreted neuroprotective and glioprotective factor prosaposin (also called sulfated glycoprotein-1). Both prosaptide and prosaposin protect primary astrocytes against oxidative stress. GPR37 is part of the class A family of GPCRs that includes receptors for hormones, neurotransmitters, sensory stimuli, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
YAVMCLSVVIFGIGIMGNVAVMCIVCHNYYMRSISNSLLANLAFWDFLIIFFCLPLVIFHELTKKWLLGD
FSCKIVPYIEVASLGVTTFTLCALCIDRFRAATNVQMYYEMIENCTSTTAKLAVIWVGALLLALPEVVLR
QLSKEDGGSGAPPAERCVVKISTELPDTIYVLALTYDGARLWWYFGCYFCLPTLFTITCSLVTARKIRRA
EKACTRGNKRQIQLESQMNCTVVALTILYGFCIIPENICNIVTAYMATGVSRQTMDLLHLISQFLLFFKS
CVTPVLLFCLCRPFSRAF
>gnl|CDD|320256 cd15128, 7tmA_ET_R, endothelin receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Endothelins are 21-amino acid peptides which able to activate a number of signal transduction processes including phospholipase A2, phospholipase C, and phospholipase D, as well as cytosolic protein kinase activation. They play an important role in the regulation of the cardiovascular system and are the most potent vasoconstrictors identified, stimulating cardiac contraction, regulating the release of vasoactive substances, and stimulating mitogenesis in blood vessels. Two endothelin receptor subtypes have been isolated and identified in vertebrates, endothelin A receptor (ET-A) and endothelin B receptor (ET-B), and are members of the seven transmembrane class A G-protein coupled receptor family which activate multiple effectors via different types of G protein. Some vertebrates contain a third subtype, endothelin A receptor (ET-C). ET-A receptors are mainly located on vascular smooth muscle cells, whereas ET-B receptors are present on endothelial cells lining the vessel wall. Endothelin receptors have also been found in the brain
YINTVVSCLIFIVGIIGNSTLLRIIYQNKCMRNGPNALIASLALGDLLYIVIDLPINVYKLLAMDWPFGD
QPFGQFLCKLVPFIQKASVGITVLNLCALSVDRYRAVASWSRIQGIGIPMWTAVEIVMIWMLSAVLAVPE
AIGFDMVRFNYKGVTLRTCLLRPETSFMKFYIDVKDWWLFGFYFCLPLVCTAIFYTLMTCEMLRKRNGML
RIALNEHLKQRREVAKTVFCLVVIFALCWLPLHLSRILKLTVYDQNDPNRCELLSFLLVLDYFGINLATL
NSCINPIALYFVSRKFKNCF
>gnl|CDD|320257 cd15129, 7tmA_GPR142, G-protein-coupled receptor GPR142, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR142, a vertebrate orphan receptor, is very closely related to GPR139, but they have different expression patterns in the brain and in other tissues. These receptors couple to inhibitory G proteins and activate phospholipase C. Studies suggested that dimer formation may be required for their proper function. GPR142 is predominantly expressed in pancreatic beta-cells and plays an important role in mediating enhancement of glucose-stimulated insulin secretion and maintaining glucose homeostasis, whereas GPR139 is expressed almost exclusively in the brain and is suggested to play a role in the control of locomotor activity. These orphan receptors are phylogenetically clustered with invertebrate FMRFamide receptors such as Drosophila melanogaster DrmFMRFa-R
VIPVIYYSVLLCLGLPVNILTAVALSRLAVRTKKSSYYYLLALTASDILTQVFIIFVGFILQTAILAREV
PHALIHTVSVLEFAANHASIWITVLLTVDRYVALCHPLRYRAVSYPERTRRIIAAVFVAALATGIPFYWW
SDMWRDSHPPTTLDKVLKWTHCFIIYFIPCTIFLVTNSVIIHKLRRRKGRSGPQRRSGKTTAILLAITTV
FAVLWAPRTVVIIYHLYVSSVNRDWRVHLALDLANMLAMLNTAVNFFLYCFVSKRFRRTV
>gnl|CDD|320258 cd15130, 7tmA_NTSR, neurotensin receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Neurotensin (NTS) is a 13 amino-acid neuropeptide that functions as both a neurotransmitter and a hormone in the nervous system and peripheral tissues, respectively. NTS exerts various biological activities through activation of the G protein-coupled neurotensin receptors, NTSR1 and NTSR2. In the brain, NTS is involved in the modulation of dopamine neurotransmission, opioid-independent analgesia, hypothermia, and the inhibition of food intake, while in the periphery NTS promotes the growth of various normal and cancer cells and acts as a paracrine and endocrine modulator of the digestive tract. The third neurotensin receptor, NTSR3 or also called sortilin, is not a G protein-coupled receptor
VLVTAIYLALFVVGTVGNSVTLFTLARKKSLQSLQSTVRYHLGSLALSDLLILLLAMPVELYNFIWVHHP
WAFGDAGCRGYYFLRDACTYATALNVASLSVERYLAICHPFKAKTLMSRSRTKKFISAIWLASALLAIPM
LFTMGLQNESDDGTHPGGLVCTPIVDTATLKVVIQVNTFMSFLFPMLVTSILNTVIANKLVQALRRGVLV
LRAVVIAFVVCWLPYHVRRLMFCYISDEQWTTFLFDFYHYFYMLTNALFYVSSAINPILYNLVSANFRQV
F
>gnl|CDD|320259 cd15131, 7tmA_GHSR, growth hormone secretagogue receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Growth hormone secretagogue receptor, GHSR, is also known as GH-releasing peptide receptor (GHRP) or Ghrelin receptor. Ghrelin, the endogenous ligand for GHSR, is an acylated 28-amino acid peptide hormone produced by ghrelin cells in the gastrointestinal tract. Ghrelin, also called hunger hormone, is involved in the regulation of growth hormone release, appetite and feeding, gut motility, lipid and glucose metabolism, and energy balance. It also plays a role in the cardiovascular, immune, and reproductive systems. GHSR couples to G-alpha-11 proteins. Both ghrelin and GHSR are expressed in a wide range of cancer tissues. Recent studies suggested that ghrelin may play a role in processes associated with cancer progression, including cell proliferation, metastasis, apoptosis, and angiogenesis
TGITVTCVLLFVVGVTGNLMTMLVVSKYRDMRTTTNLYLSSMAFSDLLIFLCMPLDLYRLWQYRPWNFGD
LLCKLFQFVSESCTYSTILNITALSVERYFAICFPLRAKVVVTKRRVKLVILVLWAVSFLSAGPIFVLVG
VEHENGTNPIDTNECKATEYAVRSGLLTIMVWVSSVFFFLPVFCLTVLYSLIGRKLWRRRRENIGPNASH
RDKNNRQTVKMLAVVVFAFVLCWLPFHVGRYLFSKSFEAGSLEIALISQYCNLVSFVLFYLSAAINPILY
NIMSKKYRVAA
>gnl|CDD|320260 cd15132, 7tmA_motilin_R, motilin receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Motilin receptor, also known as GPR38, is a G-protein coupled receptor that binds the endogenous ligand motilin. Motilin is a 22 amino acid peptide hormone expressed throughout the gastrointestinal tract and stimulates contraction of gut smooth muscle. Motilin is also called as the housekeeper of the gut because it is responsible for the proper filling and emptying of the gastrointestinal tract in response to food intake, and for stimulating the production of pepsin. Motilin receptor shares significant amino acid sequence identity with the growth hormone secretagogue receptor (GHSR) and neurotensin receptors (NTS-R1 and 2)
IPVTIVCLILFVVGVTGNTMTVLIIRRYKDMRTTTNLYLSSMAVSDLLILLCLPFDLYRLWKSRPWIFGE
FLCRLYHYISEGCTYATILHITALSIERYLAICFPLRAKVLVTRRRVKCVIAALWAFALLSAGPFLFLVG
VEQDNNIHPDDFSRECKHTPYAVSSGLLGIMIWVTTTYFFLPMLCLSFLYGFIGRKLWKSKNDLRGPNAA
ARERSHRQTVRILAVVVLAFIICWLPFHIGRILFANTEDYRTMMFSQYFNIVAMQLFYLSASINPILYNL
ISRKYRAAA
>gnl|CDD|320261 cd15133, 7tmA_NMU-R, neuromedin U receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Neuromedin U (NMU) is a highly conserved neuropeptide with a common C-terminal heptapeptide sequence (FLFRPRN-amide) found at the highest levels in the gastrointestinal tract and pituitary gland of mammals. Disruption or replacement of residues in the conserved heptapeptide region can result in the reduced ability of NMU to stimulate smooth-muscle contraction. Two G-protein coupled receptor subtypes, NMU-R1 and NMU-R2, with a distinct expression pattern, have been identified to bind NMU. NMU-R1 is expressed primarily in the peripheral nervous system, while NMU-R2 is mainly found in the central nervous system. Neuromedin S, a 36 amino-acid neuropeptide that shares a conserved C-terminal heptapeptide sequence with NMU, is a highly potent and selective NMU-R2 agonist. Pharmacological studies have shown that both NMU and NMS inhibit food intake and reduce body weight, and that NMU increases energy expenditure
FPVCLTYLLIFVVGVVGNVLTCLVIARHKAMRTPTNYYLFSLAVSDLLVLLLGMPLELYELWQNYPFLLG
SGGCYFKTFLFETVCLASILNVTALSVERYIAVVHPLAARTCSTRPRVTRVLGCVWGVSMLCALPNTSLH
GIKFLGSGVPASAQCTVRKPQAIYNMIPQHTGHLFFVLPMAVISVLYLLMALRLARERGLDATGAGSKIG
TRTGQLLQHPRTRAQVTKMLFILVVVFAICWAPFHIDRLMWSFISDWTDNLHEVFQYVHIISGVFFYLSS
AVNPILYNLMSTRFREMF
>gnl|CDD|320262 cd15134, 7tmA_capaR, neuropeptide capa receptor and similar invertebrate proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. CapaR is a G-protein coupled receptor for the Drosophila melanogaster capa neuropeptides (Drm-capa-1 and -2), which act on the Malpighian tubules to increase fluid transport. The capa peptides are evolutionarily related to vertebrate Neuromedin U neuropeptide and contain a C-terminal FPRXamide motif. CapaR regulates fluid homeostasis through its ligands, thereby acts as a desiccation stress-responsive receptor. CapaR undergoes desensitization, with internalization mediated by beta-arrestin-2
IPITIIYGIIFVTGVVGNLCTCIVIARNRSMHTATNYYLFSLAVSDLLLLILGLPFELYTIWQQYPWVFG
EVFCKLRAFLSEMSSYASVLTITAFSVERYLAICHPLRSHTMSKLSRAIRIIIAIWIIAFVCALPFAIQT
RIVYLEYPPTSGEALEESAFCAMLNEIPPITPVFQLSTFLFFIIPMIAIIVLYVLIGLQLRRSTLLRRGQ
RSVSGGRRSSQSRRTVLRMLVAVVVAFFICWAPFHAQRLLTVYAKNMTPPYLFINRILFYISGVLYYVSS
TVNPILYNVMSAKYRQAF
>gnl|CDD|320263 cd15135, 7tmA_GPR39, G protein-coupled receptor 39, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR39 is an orphan G protein-coupled receptor that belongs to the growth hormone secretagogue and neurotensin receptor subfamily. GPR39 is expressed in peripheral tissues such as pancreas, gut, gastrointestinal tract, liver, kidney as well as certain regions of the brain. The divalent metal ion Zn(2+) has been shown to be a ligand capable of activating GPR39. Thus, it has been suggested that GPR39 function as a G(q)-coupled Zn(2+)-sensing receptor which involved in the regulation of endocrine pancreatic function, body weight, gastrointestinal mobility, and cell death
ITLTLLYSLILVAGILGNSATIKVTQVLQKKGYLQKSVTDHMVSLACSDLLVLLLGMPVELYSAIWDPFA
TPSGNIACKIYNFLFEACSYATILNVATLSFERYIAICHPFKYKALSGSRVRLLICFVWLTSALVALPLL
FAMGTEDPLEAFPSYRGTRHHCQDQKSNLTICTSLSSKWTVFQASIFSAFVLYLLVLASVAFMCRRMMRA
LMGSKKGAVAVKGPGGSVQLLRKHESAEGKTARKQTILFLGLIVGTLAVCWMPNQIRRIMAAAKPKDDWT
RSYFRAYIILLPIADTFFYLSSVLNPLLYNLSSQQFRSVF
>gnl|CDD|320264 cd15136, 7tmA_Glyco_hormone_R, glycoprotein hormone receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. The glycoprotein hormone receptors (GPHRs) are seven transmembrane domain receptors with a very large extracellular N-terminal domain containing many leucine-rich repeats responsible for hormone recognition and binding. The glycoprotein hormone family includes three gonadotropins: luteinizing hormone (LH), follicle-stimulating hormone (FSH), chorionic gonadotropin (CG) and a pituitary thyroid-stimulating hormone (TSH). The glycoprotein hormones exert their biological functions by interacting with their cognate GPCRs. Both LH and CG bind to the same receptor, the luteinizing hormone-choriogonadotropin receptor (LHCGR); FSH binds to FSH-R and TSH to TSH-R. GPHRs couple primarily to the G(s)-protein and promotes cAMP production, but also to the G(i)- or G(q)-protein
WWLRIGVWFVFLLALVGNIIVLLVLLTSRTKLTVPRFLMCNLAFADFCMGIYLGLLAIVDAKTLGEYYNY
AIDWQTGAGCKTAGFLAVFSSELSVFTLTVITLERWYAITHAMHLNKRLSLRQAAIIMLGGWIFALIMAL
LPLVGVSSYSKTSICLPFETETPVSKAYVIFLLLFNGLAFLIICGCYIKIYLSVRGSGRAANSNDTRIAK
RMALLVFTDFLCWAPIAFFGLTAAFGLPLISVSNAKILLVFFYPLNSCANPFLYAIFTKQFRRDC
>gnl|CDD|320265 cd15137, 7tmA_Relaxin_R, relaxin family peptide receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes relaxin/insulin-like family peptide receptor 1 (RXFP1 or LGR7) and 2 (RXFP2 or LGR8), which contain a very large extracellular N-terminal domain with numerous leucine-rich repeats responsible for hormone recognition and binding. Relaxin is a member of the insulin superfamily that has diverse actions in both reproductive and non-reproductive tissues. The relaxin-like peptide family includes relaxin-1, relaxin-2, and the insulin-like (INSL) peptides such as INSL3, INSL4, INSL5 and INSL6. The relaxin family peptides share high structural but low sequence similarity, and exert their physiological functions by activating a group of four GPCRs, RXFP1-4. Relaxin and INSL3 are the endogenous ligands for RXFP1 and RXFP2, respectively. Upon receptor binding, relaxin activates a variety of signaling pathways to produce second messengers such as cAMP
PVLRVFIWVVGIIALLGNLFVLIWRLKYKEENKVHSFLIKNLAIADFLMGVYLLIIASVDLYYRGVYIKH
DEEWRSSWLCTFAGFLATLSSEVSVLILTLITLDRFICIVFPFSGRRLGLRRAIIVLACIWLIGLLLAVL
PLLPWDYFGNFYGRSGVCLPLHITDERPAGWEYSVFVFLGLNFLAFVFILLSYIAMFISIRRTRKAAASR
KSKRDMAVAKRFFLIVLTDFLCWIPIIVIGILALSGVPIPGEVYAWVAVFVLPINSALNPILYTLSTPKF
RKKL
>gnl|CDD|320266 cd15138, 7tmA_LRR_GPR, orphan leucine-rich repeat-containing G protein-coupled receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes leucine-rich repeat-containing G-protein coupled receptor 4 (LGR4), 5 (LGR5), and 6 (LGR6). These receptors contain a subfamily of receptors related to the glycoprotein hormone receptor family, which includes the luteinizing hormone (LH) receptor, the follicle-stimulating hormone (FSH) receptor, and the pituitary thyroid-stimulating hormone (TSH) receptor. LGR4-6 are receptors for the R-spondin (Rspo) family of secreted proteins containing two N-terminal furin-like repeats and a thrombospondin domain. The RSPO proteins are involved in regulating proliferation and differentiation of adult stem cells by potently enhancing the WNT-stimulated beta-catenin signaling. LGR4 is broadly expressed in proliferating cells, and its deficient mice display development defects in multiple organs. LGR5 acts as a marker for resident stem cell in numerous epithelial cell layers, including small intestine, colon, stomach, and kidney. LGR6 also serves as a marker of multipotent stem cells in the hair follicle that generate all skin cell lineages. Members of this group are characterized by a very large extracellular N-terminal domain containing 17 leucine-rich repeats (LRRs), flanked by cysteine-rich N- and C-terminal capping domains, and the extracellular domain is responsible for high-affinity binding with the Rspo proteins
WMIRLTVWFIFLLALFCNLLVILTVFASCTSLPPSKLFIGLIAVSNLLTGISTGILAFVDAVTFGRFAEF
GAWWETGSGCKVAGFLAVFSSESSVFLLTLAAVERSLSVKDIMKNGKSNHLKSFRVAALLCFLLATVAAA
FPLFHRGEYGASPLCLPFPTGEPPSLGFTVALVLLNSLCFLLMAVAYTKLYCNLEKGDLEENWDCSMVKH
VAWLIFTNCILFCPVAFLSFASLITLISISPEIMKSVLLVVFPLPACLNPLLYVLFNPHFKEDL
>gnl|CDD|320267 cd15139, 7tmA_PGE2_EP2, prostaglandin E2 receptor EP2 subtype, member of the class A family of seven-transmembrane G protein-coupled receptors. Prostaglandin E2 receptor EP2, also called prostanoid EP2 receptor, is one of four receptor subtypes whose endogenous physiological ligand is prostaglandin E2 (PGE2). Each of these subtypes (EP1-EP4) have unique but overlapping tissue distributions that activate different intracellular signaling pathways. Stimulation of the EP2 receptor by PGE2 causes cAMP accumulation through G(s) protein activation, which subsequently produces smooth muscle relaxation and mediates the systemic vasodepressor response to PGE2. Prostanoids are the cyclooxygenase (COX) metabolites of arachidonic acid, which include the prostaglandins (PGD2, PGE2, PGF2alpha), prostacyclin (PGI2), and thromboxane A2 (TxA2). These five major bioactive prostanoids acts as mediators or modulators in a wide range of physiological and pathophysiological processes within the kidney and play important roles in inflammation, platelet aggregation, and vasoconstriction/relaxation, among many others. They act locally by preferentially interacting with G protein-coupled receptors designated DP, EP. FP, IP, and TP, respectively. The phylogenetic tree suggests that the prostanoid receptors can be grouped into two major branches: G(s)-coupled (DP1, EP2, EP4, and IP) and G(i)- (EP3) or G(q)-coupled (EP1, FP, and TP), forming three clusters
GGSPAISALMFSAGVLGNVLALVLLERRRRKEVGRRQSLFHVLVTSLVITDLLGTCLISPVVLASYSRNT
TLVGMSPNRLVCGYFGFAMTFFSLATMLILLAMALERCLSIGHPYFYERYVSKRCGYVTIPLIYLLCALF
CLFPFLGFGKYVQYCPGTWCFIDMNPEASEHRAYANLYATLLLLLIVAVVLCNASVIYHLVRMYRRRKRN
RSSVGGRARSHRRRFSMAEEVEHLILLVFMTIIFVICSLPLTIQVYMNTFSDSENHKWDLIALRFLSVNP
IIDPWVFIILSPPVLRLLW
>gnl|CDD|320268 cd15140, 7tmA_PGD2, prostaglandin D2 receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Prostaglandin D2 receptor (also called prostanoid DP receptor, DP1, or PGD2R1) is a G-protein coupled receptor whose endogenous ligand is prostaglandin D2 (PGD2). PGD2, the major cyclooxygenase metabolite of arachidonic acid produced by mast cells, mediates inflammatory reactions in response to allergen challenge and causes peripheral vasodilation. PGD2 exerts its biological effects by binding to two types of cell surface receptors: a DP1 receptor that belongs to the prostanoid receptor family and a chemoattractant receptor-homologous molecule expressed on the T-helper type 2 cells (CRTH2 or PD2R2)
GSSVVSSSLLFAAGLLGNLLALGLLWLHKLHAKKQRGGRPRTSVFYVLVTVLTVTDLLGKCLLSPVVLAA
YAQNRSLVGLTPAGNLNLCQVFAFLMIFFGLASTFILLAMALECWLSLGHPFFYQRHINKRLGALVSLIL
YAFCLGFCALPFFGFGRYVQYCPGTWCFIQMTAEESSTSALAYSVLYGSLMGLLVLAIVLCNLGIMRNLY
QMYRRENEKGIPSTDLQGAAAFPRQQEPAGMEELEHLILLALMTVLFTACSLPVIARAYVGAFKGEKNEA
ADLTALRFLSVNSIVDPWIFIIFRTSKFRGFL
>gnl|CDD|320269 cd15141, 7tmA_PGI2, prostaglandin I2 receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Prostaglandin I2 receptor (also called prostacyclin receptor or prostanoid IP receptor) is a class A, G protein-coupled receptor whose endogenous ligand is prostacyclin, which is the major product of cyclooxygenase metabolite of arachidonic acid that found predominantly in platelets and vascular smooth muscle cells (VSMCs). The PGI2 receptor is coupled to both G(s) and G(q) protein subtypes, resulting in increased cAMP formation, phosphoinositide turnover, and Ca2+ signaling. PGI2 receptor activation by prostacyclin induces VSMC differentiation and produces a potent vasodilation and inhibition of platelet aggregation
DGHPATSTLMFAAGVVGNLLALGILGVHRKERRTKSSAFCVLVTGLAATDLLGTCFLSPMVFVSYAQNSS
LLGLAAGQPLCHLFAFAMTFFGLASMLILFAMAVERCLAISHPYFYAQHSGRRLAKLALPAIYAFGALFC
ALPLLGVGRHKQYCPGTWCFIRMTVPGHREPGSLAFSLLYASLMALLIAAIFLCNGSVTVSLCRMYRGQK
ARRGSLRRCGRLGWWLGQGEEEVDHLILLALMTVIFVVCSLPLTIRAFLGAIAPDGNESGDLLAFRFSAF
NPILDPWIFIIFRKAVFRKLR
>gnl|CDD|320270 cd15142, 7tmA_PGE2_EP4, prostaglandin E2 receptor EP4 subtype, member of the class A family of seven-transmembrane G protein-coupled receptors. Prostaglandin E2 receptor EP4, also called prostanoid EP4 receptor, is one of four receptor subtypes whose endogenous physiological ligand is prostaglandin E2 (PGE2). Each of these subtypes (EP1-EP4) have unique but overlapping tissue distributions that activate different intracellular signaling pathways. Like the EP2 receptor, stimulation of the EP4 receptor by PGE2 causes cAMP accumulation through G(s) protein activation. Knockout studies in mice suggest that EP4 receptor may be involved in the maintenance of bone mass and fracture healing. Prostanoids are the cyclooxygenase (COX) metabolites of arachidonic acid, which include the prostaglandins (PGD2, PGE2, PGF2alpha), prostacyclin (PGI2), and thromboxane A2 (TxA2). These five major bioactive prostanoids acts as mediators or modulators in a wide range of physiological and pathophysiological processes within the kidney and play important roles in inflammation, platelet aggregation, and vasoconstriction/relaxation, among many others. They act locally by preferentially interacting with G protein-coupled receptors designated DP, EP. FP, IP, and TP, respectively. The phylogenetic tree suggests that the prostanoid receptors can be grouped into two major branches: G(s)-coupled (DP1, EP2, EP4, and IP) and G(i)- (EP3) or G(q)-coupled (EP1, FP, and TP), forming three clusters
ATPPTIPAVMFIFGVVGNLIAIVVLCKSRKEQKETTFYTLVCGLAVTDLLGTCLASPVTIATYLKGRWPG
GQPLCEYFSFILLFFSLSGLSIICAMSIERYLAINHAYFYNHYVDKRLAGLTLFAIYASNILFCALPSMG
LGKSKLQYPKTWCFIDWRTNVSVHAAYSYMYAGFSSLLILVTVLCNVLVCGALIRMHRQFVRRTSLGTDQ
RLSDFRRRRSFRRMAGAEIQMVILLIATSVVVLICSIPLVVRVFVNQLYQPAVEKDLDKNPDLQAIRIAS
VNPILDPWIYILLRKTVLSKLI
>gnl|CDD|320271 cd15143, 7tmA_TXA2_R, thromboxane A2 receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The thromboxane receptor, also known as the prostanoid TP receptor, is a class A G-protein coupled receptor whose endogenous ligand is thromboxane A2 (TXA2). TXA2 is the major product of cyclooxygenase metabolite of arachidonic acid that found predominantly in platelets and stimulates platelet aggregation, Ca2+ influx into platelets, and also causes vasoconstriction. TXA2 has been shown to be involved in immune regulation, angiogenesis and metastasis, among many others. Activation of TXA2 receptor is coupled to G(q) and G(13), resulting in the activations of phospholipase C and RhoGEF, respectively. TXA2 receptor is widely distributed in the body and is abundantly expressed in thymus and spleen
ITSVWFSTIFSAIGLASNLFAFIVLVKSSRKTKSRSRSSFLIFLCGLVVTDFLGLLVTGTIVISFHLTNF
NWRVVDPDCYLCNFMGLSMVFYGLCPLLLGATMAVERFFGINRPFSRSTAMSKRRAWYMVGMVWAFAFLL
GLLPILGLGRYTLQYPGSWCFLTLLFDSKDVAFGLLFSFLGILSVGLSFLLNTVSVVTLCRVYHDRESVQ
RRRDSEVEMMVQLLGIMVIASVCWLPLLVFIAQTVLQKPPAMLLAGQIPRLTEKKLLIYLRFATWNQILD
PWVYILFRRAVLKRLY
>gnl|CDD|320272 cd15144, 7tmA_PGE2_EP1, prostaglandin E2 receptor EP1 subtype, member of the class A family of seven-transmembrane G protein-coupled receptors. Prostaglandin E2 receptor EP1, also called prostanoid EP1 receptor, is one of four receptor subtypes whose endogenous physiological ligand is prostaglandin E2 (PGE2). Each of these subtypes (EP1-EP4) have unique but overlapping tissue distributions that activate different intracellular signaling pathways. It has been shown that stimulation of the EP1 receptor by PGE2 causes smooth muscle contraction and increased intracellular Ca2+ levels; however, it is still unclear whether EP1 receptor is exclusively coupled to G(q/11), which leading to activation of phospholipase C and phosphatidylinositol hydrolysis. Prostanoids are the cyclooxygenase (COX) metabolites of arachidonic acid, which include the prostaglandins (PGD2, PGE2, PGF2alpha), prostacyclin (PGI2), and thromboxane A2 (TxA2). These five major bioactive prostanoids acts as mediators or modulators in a wide range of physiological and pathophysiological processes within the kidney and play important roles in inflammation, platelet aggregation, and vasoconstriction/relaxation, among many others. They act locally by preferentially interacting with G protein-coupled receptors designated DP, EP. FP, IP, and TP, respectively. The phylogenetic tree suggests that the prostanoid receptors can be grouped into two major branches: G(s)-coupled (DP1, EP2, EP4, and IP) and G(i)- (EP3) or G(q)-coupled (EP1, FP, and TP), forming three clusters
PASPAMPIFSMTLGALSNIVALVILAQSYARFRRRSKATFLLFASSLVLTDLAGHVIPGALVLRLYLSGQ
MPAEEPRGALCQFFGACMVFFGLCPLFLGCAMAVERCVGVTRPLLHSSVVTTTRTKLSLLAIWAVALAVA
LLPLFRFGRYKPQFPGTWCFIKVQPPGSWADVAFALLFSLLGLASLLVSLVCNTISGLTLVRARLRKKCS
CSNRRAKSHDIEMVVQLVGIMVVSCICWSPLLIFVLISVSRSYERPKHQYEKLLFLGVRLASWNQILDPW
VYILLRRAVLRKVL
>gnl|CDD|320273 cd15145, 7tmA_FP, prostaglandin F2-alpha receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The PGF2-alpha receptor, also called prostanoid FP receptor, is a class A G-protein coupled receptor whose endogenous ligand is prostaglandin F2-alpha. PGF2-alpha binding to this receptor is coupled to the stimulation of phospholipase C (PLC) pathway via G-protein subunit G(q). This leads to the release of inositol trisphosphate (IP3) and diacylglycerol (DAG) which results in increased intracellular Ca2+ levels and activation of PKC. The receptor activation primarily induces uterine contraction and bronchoconstriction, and stimulates luteolysis. Like most prostanoid receptors, the PGF2-alpha receptor has also been implicated in tumor angiogenesis and metastasis
KLSVFFSIIFMTVGILSNSLAIAILMKAYQRFRQKSKASFLLLASGLVITDFFGHLINGTIAVFVYASDK
DWIRFDQSNILCSVFGICMVFFGLCPLLLGSVMAVERCIGVTKPIFHSTKMTSKHVKMMLSGVCLFAVLV
ALLPILGHRDYQIQASRTWCFYKTEHIEDWEDRFYLLLFSFLGLLALAISFLCNAITGITLLRVKFRSQQ
HRQGRSHHFEMVIQLLAIMCVSCICWSPFLVTMANIGINGRDSLESCETILFALRMATWNQILDPWVYIL
LRKAVLKNLY
>gnl|CDD|320274 cd15146, 7tmA_PGE2_EP3, prostaglandin E2 receptor EP3 subtype, member of the class A family of seven-transmembrane G protein-coupled receptors. Prostaglandin E2 receptor EP3, also called prostanoid EP3 receptor, is one of four receptor subtypes whose endogenous physiological ligand is prostaglandin E2 (PGE2). Each of these subtypes (EP1-EP4) have unique but overlapping tissue distributions that activate different intracellular signaling pathways. Stimulation of the EP3 receptor by PGE2 preferentially couples to G(i) protein. This leads to a decrease in adenylate cyclase activity, thereby decreasing cAMP levels, which subsequently produces smooth muscle contraction. Knockout mice studies suggest that the EP3 receptor may act as a systemic vasopressor. Prostanoids are the cyclooxygenase (COX) metabolites of arachidonic acid, which include the prostaglandins (PGD2, PGE2, PGF2alpha), prostacyclin (PGI2), and thromboxane A2 (TxA2). These five major bioactive prostanoids acts as mediators or modulators in a wide range of physiological and pathophysiological processes within the kidney and play important roles in inflammation, platelet aggregation, and vasoconstriction/relaxation, among many others. They act locally by preferentially interacting with G protein-coupled receptors designated DP, EP. FP, IP, and TP, respectively. The phylogenetic tree suggests that the prostanoid receptors can be grouped into two major branches: G(s)-coupled (DP1, EP2, EP4, and IP) and G(i)- (EP3) or G(q)-coupled (EP1, FP, and TP), forming three clusters
SVSVAFPITMMITGMVGNALAMLLVYRSYRKKENKRKRSFLLCIGSLALTDLFGQLLTSPIVISVYLSDR
KWERVDPSGRLCPFFGLCMTVFGLCPLFIASAMAIERALAIRAPHWYSSHMKTRVTKAVLLGIWLAVLAF
ALLPIAGVGQYTLQWPGTWCFISTGDGEPGNNFFASTFASLGLFSLCVTFSCNLATIRALVSRCKTKAGA
SVSSKQWERITTETLIQLLGIMCVLSACWSPLLVLMLKMISNHTSSEHCKSATAPPQSTELQKDCNFFLT
AVRLASLNQILDPWVYLLLRKILLRKFC
>gnl|CDD|320275 cd15147, 7tmA_PAFR, platelet-activating factor receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The platelet-activating factor receptor is a G(q/11)-protein coupled receptor, which is linked to p38 MAPK and PI3K signaling pathways. PAF is a phospholipid (1-0-alkyl-2-acetyl-sn-glycero-3-phosphorylcholine) which is synthesized by cells especially involved in host defense such as platelets, macrophages, neutrophils, and monocytes. PAF is well-known for its ability to induce platelet aggregation and anaphylaxis, and also plays important roles in allergy, asthma, and inflammatory responses, among many others
TLFPIVYSIIFVLGLIANCYVLWVFARLYPSKKLNEIKIFMVNLTIADLLFLITLPFWIVYYHNEGNWIL
PKFLCNVAGCLFFINTYCSVAFLGVISYNRYQAVTRPIKTAQSTTRKRGIIISVAIWVIIVASASYFLFM
DSTNTVKIDSGNFTRCFEGYEKDNSKPVLIIHFIIIGLFFLVFLLILVCNLVIARTLLSQPVQGQRNAGV
KRRALWMVCTVLAVFVICFVPHHVVQGPWTLAVLQQWRYWDCQFRQALNDAHQITLCLMSTNCVLDPVIY
CFLTKKFRKHL
>gnl|CDD|320276 cd15148, 7tmA_GPR34-like, putative G protein-coupled receptor 34, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup represents the G-protein coupled receptor 34 of unknown function. Orphan GPR34 is a member of the rhodopsin-like, class A GPCRs, which is a widespread protein family that includes the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
LPLAVFYSLIFLFGLVGNLLALWVFLFIHRKRNSVRIFLINVAIADLLLIICLPFRILYHVNNNQWTLGP
LLCKVVGNLFYMNMYISIILLGFISLDRYLKINRSSRRQKFLTRKWSIVACGVLWAVALVGFVPMIVLTE
KNEESTKCFQYKDRKNAKGKAIFNFLIVAMFWLVFLLLILSYGKIAKKLLRISRDKPDFPNAAKYNRTAR
KSFFVLFIFTVCFVPYHAFRIFYITSQLQNNSCYWKEILHKTNEIMLLLSAFNSCLDPVMYFLLSSSIRK
VT
>gnl|CDD|320277 cd15149, 7tmA_P2Y14, P2Y purinoceptor 14, member of the class A family of seven-transmembrane G protein-coupled receptors. The P2Y14 receptor is activated by UDP-sugars and belongs to the G(i) class of the P2Y family of purinergic G-protein coupled receptors. The P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-sugars. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5 and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12 and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-sugars (P2Y14). P2Y14 receptor has been reported to be involved in a diverse set of physiological responses in many epithelia as well as in immune and inflammatory cells
RVIPVFYSLVFIVGILLNGVNFWIFFYVPSNKSFIVYLKNIVFADLLMSLTFPFKILSDVELGPWQLNVI
VCRYSAVIFYLNMYVGIIFFGLIGFDRYYKIVKPLHTSFVQNVGYSKALSVVVWMLMAVLSVPNIILTNQ
SFHEANYTKCARLKSELGIQWHKASNYICVSIFWVVFLLLIIFYVAISRKIYKSNQKFRRNSTNMKAKSS
RNIFSILFVFFVCFVPYHALRIPYTLSQTGADYSCQSKTILYYMKEFTLLLSAANVCLDPIIYFFLCQPF
REML
>gnl|CDD|341326 cd15150, 7tmA_P2Y12, P2Y purinoceptor 12, member of the class A family of seven-transmembrane G protein-coupled receptors. The P2Y12 receptor (P2Y12R) is found predominantly on the surface of blood platelets and is activated by adenosine diphosphate (ADP). P2Y12R plays an important role in the regulation of blood clotting and belongs to the G(i) class of the P2Y family of purinergic G protein-coupled receptors. P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-sugars. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5 and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12 and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-sugars (P2Y14)
VIFPLLYTVLFIVGLTMNGLAMRVFFQIPSKSNFIIFLKNTVISDLLMILTFPFKILSDAKLGSWPLRGF
VCQVTSVIFYFTMYISILFLGLITIDRYQKTTRPFKTSNPKNLLGAKILSTVIWASMFALSLPNMILTNR
QPTPKNVKKCSLLKSEFGLVWHEIVNYICQVIFWVNFLIVIVCYTLITKELYKSYKRTRGVGKVSRKKVN
VKVFIIIAVFFICFVPFHFARIPYTLSQTRDVFDCTAKNTLFYVKESTLWLTSLNACLDPFIYFFLCKSF
RNSLI
>gnl|CDD|341327 cd15151, 7tmA_P2Y13, P2Y purinoceptor 13, member of the class A family of seven-transmembrane G protein-coupled receptors. The P2Y13 receptor (P2Y13R) is activated by adenosine diphosphate (ADP) and belongs to the G(i) class of the P2Y family of purinergic G protein-coupled receptors. P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-sugars. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5 and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12 and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-sugars (P2Y14)
VVFPVLYTVLFLVGLILNSVAAWIFFHIPSTSTFIVYLKNTLVADLIMTLMLPFKILSDSGLGPWQLRAF
VCRFSAVVFYITMYISIILLGLISFDRYLKIVRPFGKSWVQRVRFAKILSGAVWLVMFLLSVPNMILSNK
PATPISVKKCASLKSPLGLKWHEVVNYICQFIFWGVFALMVLFYTIISKKVYESYKKSRSKDNKASKKTK
AKVFIIVAVFFVCFAPFHFVRVPYTLSQTGKITDCQLQNLLYIAKEITLWLAATNVCLDPLIYIFLCKSF
RQRL
>gnl|CDD|320280 cd15152, 7tmA_GPR174-like, putative purinergic receptor GPR174, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR174 has been recently identified as a lysophosphatidylserine receptor that enhances intracellular cAMP formation by coupling to a G(s) protein. GPR174 is a member of the rhodopsin-like, class A GPCRs, which is a widespread protein family that includes the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
FIYAVTYTVILIPGLIGNVLALWVFYAYVKETKRAVIFMINLAIADLLQVLSLPLRIFYYLNKSWPFGKF
LCMFCFYLKYVNMYASIYFLVCISVRRCLYLIYPFRYNDCKRKCDVYISIAGWLVVCVGCLPFPLLRQSQ
DTNPTCCFADLPLRNVGLTTSVIMLTIAELTGFVTPLLIVLYCSWKTVMSLREKTPVLQDLGEKKKALKM
ILTCAVVFLICFAPYHISFPLDFLVKSNKIKSCTARKVILIFHPVALCLASLNSCLDPVIYYFTTDEFKR
RL
>gnl|CDD|320281 cd15153, 7tmA_P2Y10, P2Y purinoceptor 10, member of the class A family of seven-transmembrane G protein-coupled receptors. P2Y10 receptor is a G-protein coupled receptor that is activated by both sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA). Phylogenetic analysis of the class A GPCRs shows that P2Y10 is grouped into the cluster comprising nucleotide and lipid receptors. Although the mouse P2Y10 was found to be expressed in brain, lung, reproductive organs, and skeletal muscle, the physiological function of this receptor is not yet known. S1P and LPA are bioactive lipid molecules that induce a variety of cellular responses through G proteins: adhesion, invasion, cell migration and proliferation, among many others
SLYATTYIIIFIPGLLANSAALWVLCRFISKKNKAIIFMINLAVADLAHVLSLPLRIHYYIQHTWPFGRF
LCLLCFYLKYLNMYASICFLTCISIQRCFFLLHPFKARDWKRRYDVGISAAVWIVVGLACLPFPLLRSKS
LSNNNRSCFADLGMKKLNFGAAIAMMTVAELFGFVIPLFIIAWCTWKTENSLRQRNKQQQSTSEKQKALR
MVRMCAAVFFICFAPYHINFLFYLMVSESIITNCEVSQVILQFHPISLCLASLNCCLDPILYYFMTSEFQ
DQL
>gnl|CDD|320282 cd15154, 7tmA_LPAR5, lysophosphatidic acid receptor 5, member of the class A family of seven-transmembrane G protein-coupled receptors. Lysophosphatidic acid receptor 5 (LPAR5) is a G protein-coupled receptor that binds the bioactive lipid lysophosphatidic acid (LPA) and is involved in maintenance of human hair growth. Phylogenetic analysis of the class A GPCRs shows that LAPR5 is classified into the cluster consisting receptors that are preferentially activated by adenosine and uridine nucleotides. Although LPA6 (P2Y5) is expressed in human hair follicle cells, LPA4 and LPA5 are not. These three receptors are highly homologous and mediate an increase in intracellular cAMP production. Activation of LPAR5 is coupled to G(q) and G(12/13) proteins
TLHLVGYSLLFPVGLLLNAVALWVFVRYLRLHSVVSIYMCNLALSDLLFTLSLPLRIYYYANHYWPFGNF
LCQFSGSIFQMNMYGSCLFLMCINVDRYLAIVHPLRFRHLRRPKVARLLCLAVWALILGGSVPAAIVHSS
SDCLLHGEKVYRCFESFSDNDWKGLLPLVVLAEILGFLLPLAAVLYCSCRIFVELCRTQEPQQGRRRKTV
RLLLVNLVIFLICFVPYNTTLAVYGLLRANLVEDTWNIKDTLRKVLSVTVLLASTNCALDPLVYYFSTEG
FRNTL
>gnl|CDD|320283 cd15155, 7tmA_LPAR4, lysophosphatidic acid receptor 4, member of the class A family of seven-transmembrane G protein-coupled receptors. Lysophosphatidic acid receptor 4 (LPAR4) is a G protein-coupled receptor that binds and is activated by the bioactive lipid lysophosphatidic acid (LPA), which is released by activated platelets and constitutively found in serum. Phylogenetic analysis of the class A GPCRs shows that LAPR4 is classified into the cluster consisting receptors that are preferentially activated by adenosine and uridine nucleotides. Although LPA6 (P2Y5) is expressed in human hair follicle cells, LPA4 and LPA5 are not. These three receptors are highly homologous and mediate an increase in intracellular cAMP production. Activation of LPAR5 is coupled to G(12/13) proteins, leading to neurite retraction and stress fiber formation, whereas coupling to G(q) protein leads to increases in calcium levels
NLYGAVYSVVFILGLITNCASLFVFCFRMKMRNETAIFMTNLAVSDLLFVFTLPFKIFYNFNRHWPFGDS
LCKISGTAFLTNIYGSMLFLTCISVDRFLAIVYPFRSRTIRTRRNSAIVCAGVWILVLSGGISASLFSTT
NVSNTSTTCFEGFSKSIWKTYLSKITIFIEVVGFIIPLLLNLTCSSLVLRTLRKPATLSQIGTNKEKVLK
MILVHVAIFVVCFVPYNSILFLYALVRSQAIANCGVERFARTMYPITLCLATLNCCFDPFVYYFTSESFQ
KSF
>gnl|CDD|320284 cd15156, 7tmA_LPAR6_P2Y5, lysophosphatidic acid receptor 6, member of the class A family of seven-transmembrane G protein-coupled receptors. Lysophosphatidic acid receptor 6 (LPAR6), also known as P2Y5, is a G(i), G(12/13) G protein-coupled receptor that is activated by the bioactive lipid lysophosphatidic acid (LPA), which is released by activated platelets and constitutively present in serum. LPAR6 plays an important role in maintenance of human hair growth. Thus, mutations in the receptor are responsible for both autosomal recessive wooly hair and hypotrichosis. Phylogenetic analysis of the class A GPCRs shows that LAPR6 (P2Y5) is classified into the cluster consisting of receptors that are preferentially activated by adenosine and uridine nucleotides. Although LPA6 (P2Y5) is expressed in human hair follicle cells, LPA4 and LPA5 are not. These three receptors are highly homologous and mediate an increase in intracellular cAMP production
TLYGCVFSMVFVLGLIANCVAIYIFMCTLKVRNETTTYMINLAISDLLFVFTLPFRIFYFVQRNWPFGDL
LCKISVTLFYTNMYGSILFLTCISVDRFLAIVYPFRSKTLRTKRNAKIVCAAVWLTVLAGSLPASFFQST
NNQLNNNSETCFENFSSKTWKTYLSKIVIFIEIVGFFIPLILNVTCSTMVLKTLRRPNTLSRSKLNKKKV
LKMIFVHLFIFCFCFIPYNVNLVLYSLVRTQTFKNCSVVAAVRTMYPITLCIAVSNCCFDPIVYYFTSET
IQNSI
>gnl|CDD|320285 cd15157, 7tmA_CysLTR2, cysteinyl leukotriene receptor 2, member of the class A family of seven-transmembrane G protein-coupled receptors. Cysteinyl leukotrienes (LTC4, LTD4, and LTE4) are the most potent inflammatory lipid mediators that play an important role in human asthma. They are synthesized in the leucocytes (cells of immune system) from arachidonic acid by the actions of 5-lipoxygenase and induce bronchial constriction through G protein-coupled receptors, CysLTR1 and CysLTR2. Activation of CysLTR1 by LTD4 induces airway smooth muscle contraction and proliferation, eosinophil migration, and damage to the lung tissue. They belong to the class A GPCR superfamily, which all have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VIYPTVYLIIFVLGVVGNGLSIYVFLQPSKKKTSVNIFMLNLAVSDLMFVSTLPFRADYYLMGSHWVFGD
IACRIMSYSLYVNMYCSIYFLTVLSIVRFLAIVHPFKLWKVTSIKYARILCAVIWIFVMAASSPLLSKGT
SKYNSQTKCLDLHPSKIDKLLILNYIVLVVGFILPFCTLSICYILIIKALLKPRVPQSKLRVSHKKALLT
IIITLILFLLCFLPYHILRTVHLMQWSEGQCNLRLHKAVVITLCLAAANSCLDPLLYYFAGENFKERL
>gnl|CDD|320286 cd15158, 7tmA_CysLTR1, cysteinyl leukotriene receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. Cysteinyl leukotrienes (LTC4, LTD4, and LTE4) are the most potent inflammatory lipid mediators that play an important role in human asthma. They are synthesized in the leucocytes (cells of immune system) from arachidonic acid by the actions of 5-lipoxygenase and induce bronchial constriction through G protein-coupled receptors, CysLTR1 and CysLTR2. Activation of CysLTR1 by LTD4 induces airway smooth muscle contraction and proliferation, eosinophil migration, and damage to the lung tissue. They belong to the class A GPCR superfamily, which all have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
QVYSTLYSVITVFGLVGNGFALYVLIKTYRQKSAFHIYMLNLAVSDLLCVCTLPLRVVYYVHKGQWLFGD
FLCRISSYALYVNLYCSIYFMTAMSFTRFLAIVFPVQNLNLVTVKKARIVCVGIWIFVTLTSSPFLMSGS
HDTETNKTKCFEPPQSNQQLTKLLVLNYISLVVGFIIPFLVILICYAMIIRTLLKNTMKARKQQSSRKKA
IRMIIIVLLAFLVSFMPYHIQRTIHLHFLSRKDSTCEEVLYMQKSVVITLCLAAANCCFDPLLYFFSGEN
FRRRL
>gnl|CDD|320287 cd15159, 7tmA_EBI2, Epstein-Barr virus (EBV)-induced gene 2, member of the class A family of seven-transmembrane G protein-coupled receptors. Epstein-Barr virus-induced G-protein coupled receptor 2 (EBI2), also called GPR183, is activated by 7alpha, 25-dihydroxyxcholesterol (7alpha, 25-OHC), an oxysterol. EBI2 was originally identified as one of major genes induced in the Burkitt's lymphoma cell line BL41by EBV infection. EBI2 is involved in regulating B cell migration and responses, and is also implicated in human diseases such as type I diabetes, multiple sclerosis, and cancers
VLLPLFYSLILVFGLLGNTLALHVICQKRKKINSTTLYLINLAVSDILFTLALPGRIAYYALGFDWPFGD
WLCRLTALLFYINTYAGVNFMTCLSVDRYIAVVHPLRRHRLRKVKVVRYICVFVWVLVFLQTLPLLFMPM
TKEMGGRITCMEYPNFEKIKRLPLILLGACVIGFGVPVGIILFCYSQITLKLCRTAKENPLTEKSGHHKK
ACNVILLVLLVFVVCFSPYHLNIIQFMIRKLLYQPSCSELKAFKISLQITVCLMNLNCCLDPFIYFFACK
GYKKKV
>gnl|CDD|320288 cd15160, 7tmA_Proton-sensing_R, proton-sensing G protein-coupled receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Proton/pH-sensing G-protein coupled receptors sense pH of 7.6 to 6.0. They mediate a variety of biological activities in neutral and mildly acidic pH conditions, whereas the acid-sensing ionotropic ion channels typically sense strong acidic pH. The proton/pH-sensing receptor family includes the G2 accumulation receptor (G2A, also known as GPR132), the T cell death associated gene-8 (TDAG8, GPR65) receptor, ovarian cancer G-protein receptor 1 (OGR-1, GPR68), and G-protein-coupled receptor 4 (GPR4)
IFLPVVYSFVFVVGLPANCLALWVLYLQIKKENVLGVYLLNLSLSDLLYILTLPLWIDYTANHHNWTFGP
LSCKVVGFFFYTNIYASIGFLCCIAVDRYLAVVHPLRFRGLRTRRFALKVSASIWVLELGTHSVFLGHDE
LFRDEPNHTLCYEKYPMEGWQASYNYARFLVGFLIPLSLILFFYRRVLRAVRQSPSLEREEKRKIIGLLL
SIVVIFLLCFLPYHVVLLVRSVIELVQNGLCGFEKRVFTAYQISLCLTSLNCVADPILYIFVTEDVRQDL
>gnl|CDD|320289 cd15161, 7tmA_GPR17, G protein-coupled receptor 17, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR17 is a Forkhead box protein O1 (FOXO1) target and abundantly expressed in agouti-related peptide (AGRP) neurons. FOXO1 is a transcription factor that plays key roles in regulation of gluconeogenesis and glycogenolysis by insulin signaling. For instance, food intake and body weight increase when hypothalamic FOXO1 is activated, whereas they both decrease when FOXO1 is inhibited. However, a recent study has been reported that GPR17 deficiency in mice did not affect food intake or glucose homeostasis. Thus, GPR17 may not play a role in the control of food intake, body weight, or glycemic control. GPR17 is phylogenetically closely related to purinergic P2Y and cysteinyl-leukotriene receptors
ILFALFYILVFILAFPGNTLALWLFIHDRKSGTPSNVFLMHLAVADLSYVLILPMRLVYHLSGNHWPFGE
VPCRLAGFLFYLNMYASLYFLACISVDRFLAIVHPVKSMKIRKPLYAHVVCGFLWVIVTVAMAPLLVSPQ
TVEVNNTTVCLQLYREKASRGALVSLAVAFTIPFVTTVTCYLLIIRSLRTGKREEKPLKDKAIKMIILVL
TIFLICFVPYHISRYIYILSHNGAGASCSSRRGLALANRITSCLTCLNGALDPVMYFFVAEKFRETL
>gnl|CDD|341328 cd15162, 7tmA_PAR, protease-activated receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. This subfamily includes purinergic receptor P2Y8 and protease-activated receptors. P2Y8 (or P2RY8) expression is often increased in leukemia patients, and it plays a role in the pathogenesis of acute leukemia. P2Y8 is phylogenetically closely related to the protease-activated receptors (PARs), which are activated by serine proteases such as thrombin, trypsin, and tryptase. These proteases cleave the extracellular domain of the receptor to form a new N-terminus, which in turn functions as a tethered ligand. The newly-formed tethered ligand binds intramolecularly to activate the receptor and triggers G-protein binding and intracellular signaling. Four different types of the protease-activated receptors have been identified (PAR1-4) and are predominantly expressed in platelets. PAR1, PAR3, and PAR4 are activated by thrombin, whereas PAR2 is activated by trypsin. The PARs are known to couple with several G-proteins including Gi (cAMP inhibitory), G12/13 (Rho and Ras activation), and Gq (calcium signaling) to activate downstream signaling messengers which induces numerous cellular and physiological effects
VFLPAVYTLVFVVGLPANGMALWVLLFRTKKKAPAVIYMANLAIADLLLVIWLPFKIAYHIHGNNWIFGE
ALCRLVTVAFYGNMYCSILLLTCISIDRYLAIVHPMGHRRLRARRYALGTCLAIWLLALLVTLPLYLVKQ
TIFLPALDITTCHDVLPEQLLVGDWFYYFLSLAIVGFLIPFILTASCYVATIRTLAALEDENSEKKKKRA
IKLAATVLAIFIICFAPSNLLLLAHYSLISSSGTGHLYFAYLLALCLSTLNSCIDPFIYYFVSKEFRDHV
>gnl|CDD|320291 cd15163, 7tmA_GPR20, G protein-coupled receptor 20, member of the class A family of seven-transmembrane G protein-coupled receptors. Orphan GPR20 is phylogenetically related to the P2Y family of purinergic G protein-coupled receptors. The P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. GPR20 has been shown to constitutively activate G(i) proteins in the absence of a ligand; however its functional role is not known. GPR20 is a member of the class A G protein-coupled receptor superfamily, which all have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A common feature of GPCR signaling is agonist-induced conformational changes in the receptors, which then activate the heterotrimeric G proteins. G-proteins regulate a variety of cellular functions including metabolic enzymes, ion channels, and transporters, among many others
LALMVINTLIFLVGIVLNSLALYVFCFRTKTKTTSVIYTINLVVTDLLVGLSLPTRIVMYYSAGNCLTCS
FVHIFSYFVNMYCSILFLTCICVDRYLAIVQVEASRRWRNPNYAKGICVFIWLFAIVVTFSILTTAIKFA
SCCLSKLFALTVFEFFLPLLIITFFTIRIMCALSRPGLMHQSRERRMRAVQLLITVLIIFMICFTPFHVR
QVAVAFNPDIPHHTSLIVYHVTVTLSSLNSCMDPIVYCFVTNNFQSTM
>gnl|CDD|320292 cd15164, 7tmA_GPR35-like, G protein-coupled receptor 35 and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR35 shares closest homology with GPR55, and they belong to the class A G protein-coupled receptor superfamily, which all have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A number of studies have suggested that GPR35 may play important physiological roles in hypertension, atherosclerosis, nociception, asthma, glucose homeostasis and diabetes, and inflammatory bowel disease. GPR35 is thought to be responsible for brachydactyly mental retardation syndrome, which is associated with a deletion comprising chromosome 2q37 in human, and is also implicated as a potential oncogene in stomach cancer. Several endogenous ligands for GPR35 have been identified including kynurenic acid, 2-oleoyl lysophosphatidic acid, and zaprinast. GPR35 couples to G(13) and G(i/o) proteins
LIQLIIYIPILFFGLLFNVLALWVFCCKMKKWTETRVYMINLAVADCCLLFSLPFVLYFLKHSWPDDELC
LVLQSIYFINRYMSIYIITAIAVDRYIAIKYPLKAKSLRSPRKAALTCGLLWVLVIISVSLRLAWEEQEE
NFCFGKTSTRPSKRTLIFSLLGFFIPLIILSFCSIQVIRSLKKKKKTNPHEEKLIQKAIYIVSANLIVFI
VCFLPLHIGLLVRFVMESNKASCSLIQNIRNFIYVASCLANANCCLDAICYYFVAKEFQEAS
>gnl|CDD|320293 cd15165, 7tmA_GPR55-like, G protein-coupled receptor 55 and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR55 shares closest homology with GPR35, and they belong to the class A G protein-coupled receptor superfamily, which all have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. GPR55 has been reported to couple to G(13), G(12), or G(q) proteins. Activation of GPR55 leads to activation of phospholipase C, RhoA, ROCK, ERK, p38MAPK, and calcium release. Lysophosphatidylinositol (LPI) is currently considered as the endogenous ligand for GPR55, although the receptor was initially de-orphanized as a cannabinoid receptor and binds many cannabinoid ligands
SLQLVVYIPTFVLGLLLNLMALWVFLFKIKKWTESTIYMINLALNDLLLLLSLPFKMHSSKKQWPLGRTL
CSFLESLYFVNMYGSILIIVCISVDRYIAIRHPFLAKRLRSPRKAAIVCLTIWVFVWAGSIPIYSFHDKP
TNNTRCFHGFSNKTWSKKVIVVVEEFGFLIPMAVMVFCSVQIIRTLLDMRRPEQPKVKQNKSVKIVLSNL
VVFLVCFTPYHLGIFLQFLVKNDIINDCSTKQSIRLFVQVSMCLANVNCCLDAICYYFILKEFRESA
>gnl|CDD|320294 cd15166, 7tmA_NAGly_R_GPR18, N-arachidonyl glycine receptor, GPR18, member of the class A family of seven-transmembrane G protein-coupled receptors. N-arachidonyl glycine (NAGly), an endogenous metabolite of the endocannabinoid anandamide, has been identified as an endogenous ligand of the G(i/o) protein-coupled receptor 18 (GPR18). NAGly is involved in directing microglial migration in the CNS through activation of GPR18. NAGly-GPR18 signaling is thought to play an important role in microglial-neuronal communication. Recent studies also show that GPR18 functions as the abnormal cannabidiol (Abn-CBD) receptor. Abn-CBD is a synthetic isomer of cannabidiol and is inactive at cannabinoid receptors (CB1 or CB2), but acts as a selective agonist at GPR18. The NAGly receptor is a member of the class A G protein-coupled receptor superfamily, which all have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, which then activate the heterotrimeric G proteins. G-proteins regulate a variety of cellular functions including metabolic enzymes, ion channels, and transporters, among many others
IAALVFYSFIFIIGLFVNITALWVFSCTTKKRTTVTVYMMNVALVDLIFILSLPFRMVYYAKDEWPFGDY
FCRILGALTVFYPSIALWLLAFISADRYMAIVQPKHAKELKNTPKAVLACVGVWIMTLASTFPLLFLYED
PDKASNFTTCLKMLDIIHLKEVNVLNFTRLIFFFLIPLFIMIGCYLVIIHNLVHGRTSKLKPKVKEKSIR
IIITLIVQVLVCFVPFHICFAFLMLQNGDNSYNPWAAFTTFLMNLSTCLDVILYYIVSKQFQARV
>gnl|CDD|320295 cd15167, 7tmA_GPR171, orphan G protein-coupled receptor 171, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR171 is phylogenetically related to the P2Y family of purinergic G protein-coupled receptors. The P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. A recent study has been reported that the peptide LENSSPQAPARRLLPP (BigLEN) activates GPR17 to regulate body weight in mice; however the biological role of the receptor remains unknown. GPR171 is a member of the class A G protein-coupled receptor superfamily, which all have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A common feature of GPCR signaling is agonist-induced conformational changes in the receptors, which then activate the heterotrimeric G proteins. G-proteins regulate a variety of cellular functions including metabolic enzymes, ion channels, and transporters, among many others
EPFTYFYYLIFLIGFIGSCFALWAFIQKRSSRKCINIYLINLLTADFLLTLALPVKIAVDLGIAPWKLKI
FHCQVTACLIYINMYLSIIFLGFVSIDRYLQLTHSSKLYRIQEPGFAKMISAVVWTLVLFIMVPNMAIPI
KTIEEKPGVGCADFKTEFGRHWHVLTNFICMAIFLNFSAIILISNFLVIRKLYRNKDSEEYRNARQALVN
ILLVTAGYVICFVPYHIVRIPYTLSQSEVITDCSLKRSLFLAKESTLLLAVLNLCFDPILYFHLSKAFRS
KI
>gnl|CDD|341329 cd15168, 7tmA_P2Y1-like, P2Y purinoceptors 1, 2, 4, 6, 11 and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. The P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5, and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12, and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-glucose (P2Y14). This cluster only includes P2Y1-like receptors as well as other closely related orphan receptors, such as GPR91 (a succinate receptor) and GPR80/GPR99 (an alpha-ketoglutarate receptor)
IFLPIVYGVVFLVGLLLNSVVLYRFIFHLKPWNSSAIYMFNLAVSDLLYLLSLPFLIYYYANGDHWIFGD
FMCKLVRFLFYFNLYGSILFLTCISVHRYLGICHPLRSLGKLKKRHAVAISVAVWILVLLQLLPILFFAT
TGRKNNRTTCYDTTSPEELNDYVIYSMVLTGLGFLLPLLIILACYGLIVRALIRKLGEGVTSALRRKSIR
LVIIVLALFAVCFLPFHVTRTINLAARLLSGTASCATLNGIYVAYKVTRPLASLNSCLNPLLYFLAGDKF
RRRL
>gnl|CDD|320297 cd15169, 7tmA_FFAR1, free fatty acid receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup includes the mammalian free fatty acid receptor 1 (FFAR1), also called GPR40. FFAR1 is a cell-surface receptor for medium- and long-chain free fatty acids (FFAs). The receptor is most potently activated by eicosatrienoic acid (C20:3), but can also be activated at micromolar concentrations of various fatty acids. FFAR1 directly mediates FFA stimulation of glucose-stimulated insulin secretion and indirectly increases insulin secretion by enhancing the release of incretin. Free fatty acid receptors (FFARs) belong to the class A G-protein coupled receptors and are comprised of three members, each encoded by a separate gene (FFAR1, FFAR2, and FFAR3). These genes and a fourth pseudogene, GPR42, are localized together on chromosome 19. FFARs are considered important components of the body's nutrient sensing mechanism, and therefore, these receptors are potential therapeutic targets for the treatment of metabolic disorders, such as type 2 diabetes and obesity
QLSFGLYVAAFALGFPLNVLAIRGATAHARLRLTPSLVYALNLGCSDLLLTVSLPLKAVEALASGAWPLP
ASLCPVFAVAHFAPLYAGGGFLAALSAGRYLGAAFPLGYQAFRRPCYSWGVCAAIWALVLCHLGLVFGLE
APGGWLDHSNTSLGINTPVNGSPVCLEAWDPASAGPARFSLSLLLFFLPLAITAFCYVGCLRALARSGLT
HRRKLRAAWVAGGALLTLLLCVGPYNASNVASFLYPNLGGSWRKLGLITGAWSVVLNPLVTGYLGRGPGL
KTVC
>gnl|CDD|320298 cd15170, 7tmA_FFAR2_FFAR3, free fatty acid receptors 2, 3, and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup includes free fatty acid receptor 2 (FFAR2), FFAR3, and similar proteins. They are a member of the class A G-protein coupled receptors that bind free fatty acids. The FFAR subfamily is composed of three receptors, each encoded by a separate gene (FFAR1, FFAR2, and FFAR3). These genes and a fourth pseudogene, GPR42, are localized together on chromosome 19. FFAR2 and FFAR3 are cell-surface receptors for short chain FFAs (SCFAs) with different ligand affinities, whereas FFAR1 is a receptor for medium- and long-chain FFAs. FFAR2 activation by SCFA suppresses adipose insulin signaling, which leads to inhibition of fat accumulation in adipose tissue. FAAR3 is expressed in intestinal L cells, which produces glucagon-like peptide 1 (GLP-1) and peptide YY (PYY), thus suggesting that this receptor may be involved in energy homeostasis. FFARs are considered important components of the body's nutrient sensing mechanism, and therefore, these receptors are potential therapeutic targets for the treatment of metabolic disorders, such as type 2 diabetes and obesity
WLVLAVYIITFLIGLPANLLAFYTFIRKVRRKPTPIDILLLNLTVSDLIFLLFLPFKMAEAASGMIWPLP
YFLCPLSSFIFFSTIYISTLFLTAISVERYLGVAFPIKYKLRRRPLYAVIASVFFWVLAFSHCSIVYIVE
YHIDSENTSVTNNSRCYDNFTPEQLKILLPVRLELFLVLFCIPFLITCFCYINFIRILSSLPHISRQRKQ
RAIGLAVATLLNFIVCFAPYNISHVVGFIQRKSPEWRMYALLLSTLNACLDPIIFYFSSSAVRRAFKE
>gnl|CDD|320299 cd15171, 7tmA_CCRL2, CC chemokine receptor-like 2, member of the class A family of seven-transmembrane G protein-coupled receptors. Chemokine (CC-motif) receptor-like 2 (CCRL2) is a member of the atypical chemokine receptor family. CCRL2, like other atypical receptors, has an alteration in the conserved DRYLAIV motif in the third intracellular loop, which is essential for GPCR coupling and signaling. CCR2L is expressed in most hematopoietic cells and many lymphoid organs as well as in heart and lung. CCRL2 was initially reported to promote chemotaxis and calcium fluxes in responses to chemokines (CCL2, CCL5, CCL7, and CCL8); however, these results are still controversial. More recently, chemerin, a chemotactic agonist of CMKLR1 (chemokine-like receptor-1) and GPR1, was identified as a novel non-signaling ligand for both human and mouse CCRL2. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C)
QLVPQLCSAVFLVGLLDNGLVVFILVKYKGLKHVENIYFLNLAVSNLCFLLTLPFWAHAAWHGGSLGNPT
CKVLVALSSVGLHSEALFNVLLTVQASRVFFHGRLASSARRVAPCGIIASVLAWLTAFLVTLPEFVFYKP
QMDSQKSKCAFSRPHFLPAEETFWKYFLTLKMNIVVLVFPLLVFIICCVQLRKTQRFRERQRDLSKLVFA
IMVVFLLMWAPYNIALFLSAFKEHFSLRDCKSSYHLDASVQVTKLIATTHCCVNPLLYALLDPAFRRRL
>gnl|CDD|341330 cd15172, 7tmA_CCR6, CC chemokine receptor type 6, member of the class A family of seven-transmembrane G protein-coupled receptors. CCR6 is the only known receptor identified for the chemokine CCL20 (also known as macrophage inflammatory protein-3alpha, MIP-3alpha). CCR6 is expressed by all mature human B cells, effector memory T-cells, and dendritic cells found in the gut mucosal immune system. CCL20 contributes to recruitment of CCR6-expressing cells to Peyer's patches and isolated lymphoid follicles in the intestine, thereby promoting the assembly and maintenance of organized lymphoid structures. Also, CCL20 expression is highly inducible in response to inflammatory signals. Thus, CCL20 is involved in both inflammatory and homeostatic functions in the immune system. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines. The CC chemokine receptors are all activating the G protein Gi
VFVPVIYSLICVVGLIGNSLVVITYAFYKRTKSMTDVYLLNMAIADILFVLTLPFWAVYEAHQWIFGNFS
CKLLRGIYAINFYSGMLLLACISVDRYIAIVQATKSFRLRSRTLAYSKLICAAVWLLAILISLPTFIFSE
VYDFGLEEQYVCEPKYPKNSTAIMWKLLVLSLQVSLGFFIPLLVMIFCYSFIIKTLLQAQNSQRHKAVRV
VVAVVLVFLVCQVPYNIVLLIEAINLGEQQSCSSEKAVAYAKTITECLAFFHCCLNPVLYAFIGVKFRNY
F
>gnl|CDD|320301 cd15173, 7tmA_CXCR6, CXC chemokine receptor type 6, member of the class A family of seven-transmembrane G protein-coupled receptors. CXCR6 binds specifically to the chemokine CXCL16, which is expressed on dendritic cells, monocyte/macrophages, activated T cells, fibroblastic reticular cells, and cancer cells. CXCR6 is phylogenetically more closely related to CC-type chemokine receptors (CCR6 and CCR9) than other CXC receptors. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines
YFLPCMYSVMFVTGLVGNSLVIVIYIFYEKLRTLTDIFLVNLAVADLLFLCTLPFWAYSAAHEWIFGTVM
CKITNGLYTINLYSSMLILTCITVDRFIVIVQATKAHNCHAKKMRWGKVVCTLVWVISLLLSLPQFIYSE
VRNLSSKICSMVYPPDAIEVVVNIIQMTVGFFLPLLAMIICYSVIIKTLLHAKGFQKHKSLKIIFVVVAV
FILTQLPYNIMKLIRTLHIENTDSTNFKYAILITEAIAYLHACLNPILYAFVGVKFRKNF
>gnl|CDD|320302 cd15174, 7tmA_CCR9, CC chemokine receptor type 9, member of the class A family of seven-transmembrane G protein-coupled receptors. CCR9 is a homeostatic receptor specific for CCL25 (formerly known as thymus expressed chemokine) and is highly expressed on both immature and mature thymocytes as well as on intestinal homing T Lymphocytes and mucosal Lymphocytes. In cutaneous melanoma, activation of CCR9-CCL25 has been shown to stimulate metastasis to the small intestine. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines. The CC chemokine receptors are all activating the G protein Gi
YFLPPLYWLIFLVGAVGNSLVVLIYTYYRRRKTMTDVYLLNLAIADLLFLCTLPFWATAASSGWVFGTFL
CKVVNSMYKINFYSCMLLLTCISVDRYIAIVQATKAHNSKNKRLLYSKLVCFFVWLLSTILSLPEILFSQ
SKEEESVTTCTMVYPSNESNRFKVAVLALKVTVGFFLPFVVMVICYTLIIHTLLQAKRFQKHKALKVIIA
VVTVFVLSQLPYNSILLIKTINAYNITITDCATSQNLDIAGQVTQSIAFLHSCLNPFLYVFVGVRFRKDL
>gnl|CDD|341331 cd15175, 7tmA_CCR7, CC chemokine receptor type 7, member of the class A family of seven-transmembrane G protein-coupled receptors. CCR7 is a major homeostatic receptor responsible for lymph node development and effective adaptive immune responses and plays a critical role in trafficking of dendritic cells and B and T lymphocytes. Its only two ligands, CCL and CCl21, are primarily produced by stromal cells in the T cell zones of lymph nodes and spleen. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines. The CC chemokine receptors are all activating the G protein Gi
WFLPAMYSVICFLGLLGNGLVILTYIYFKRLKTMTDIYLLNLALADILFLLTLPFWAASAAKKWVFGEEM
CKAVYCLYKMSFFSGMLLLMCISIDRYFAIVQAASAHRHRSRAVFISKVSSLGVWVLAFILSIPELLYSG
VNNNDGNGTCSIFTNNKQTLSVKIQISQMVLGFLVPLVVMSFCYSVIIKTLLQARNFEKNKAIKVIIAVV
VVFVVFQLPYNSVMLVSTLSSFKGNTTDCDYSKNLDFALDVTYSLACFRCCLNPFLYAFIGVKFRNDL
>gnl|CDD|320304 cd15176, 7tmA_ACKR4_CCR11, atypical chemokine receptor 4, member of the class A family of seven-transmembrane G protein-coupled receptors. ACKR4 was first reported to bind several CC chemokines including CCL19, CCL21, and CCL25 and was originally designated CCR11. AKCR4 is unable to couple to G-protein and, instead, it preferentially mediates beta-arrestin dependent processes, such as receptor internalization, after ligand binding. Thus, ACKR4 may act as a scavenger receptor to suppress the effects of proinflammatory chemokines. Unlike the classical chemokine receptors that contain a conserved DRYLAIV motif in the second intracellular loop, which is required for G-protein coupling, the ACKRs lack this conserved motif and fail to couple to G-proteins and induce classical GPCR signaling. Five receptors have been identified for the ACKR family, including CC-chemokine receptors like 1 and 2 (CCRL1 and CCRL2), CXCR7, Duffy antigen receptor for chemokine (DARC), and D6. Both ACKR1 (DARC) and ACKR3 (CXCR7) show low sequence homology to the classic chemokine receptors
LFLPVFYTIALVVGLAGNSLVVAIYAYYKKLKTKTDVYILNLAVADLLLLFTLPFWAADAVNGWVLGTAM
CKITSALYTMNFSCGMQFLACISVDRYVAITKATSRQFTGKHCWIVCLCVWLLAILLSIPDLVFSTVREN
SDRYRCLPVFPPSLVTSAKATIQILEVLLGFVLPFLVMVFCYSRVARALSRTPNVKKSRALKVLLAVVGV
FIVTQLPYNVVKFYRAIDVIYLLITDCSMSKTLDIAIQVTESIALFHSCLNPVLYVFMGASFKSHI
>gnl|CDD|341332 cd15177, 7tmA_CCR10, CC chemokine receptor type 10, member of the class A family of seven-transmembrane G protein-coupled receptors. CCR10 is a homeostatic receptor specific for two C-C motif chemokines, CCL27 and CCL28. Activation of CCR10 by its two ligands mediates diverse activities, ranging from leukocyte trafficking to skin cancer. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines. The CC chemokine receptors are all activating the G protein Gi
VFQPCVYLVVFVLGLVGNGLVLATHTRYRRLRSMTDVYLLNLALADLLLLLTLPFAAAETLQGWIFGNAM
CKLIQGLYAINFYSGFLFLTCISVDRYVVIVRATSAHRLRPKTLFYSVLTSLIVWLLSILFALPQLIYSR
VENRSELSSCRMIFPEVVSRTVKGATALTQVVLGFAIPLIVMAVCYAAIGRTLLAARGWERHRALRVIAA
LVVAFVLFQLPYSVVLLLDTADLLATLELSCSQSKRKDIALLVTSGLAYVRCCLNPLLYAFVGVRFRRDI
>gnl|CDD|341333 cd15178, 7tmA_CXCR1_2, CXC chemokine receptor types 1 and 2, member of the class A family of seven-transmembrane G protein-coupled receptors. CXCR1 and CXCR2 are closely related chemotactic receptors for a group of CXC chemokines distinguished by the presence of the amino acid motif ELR immediately adjacent to their CXC motif. Expression of CXCR1 and CXCR2 is strictly controlled in neutrophils by external stimuli such as lipopolysaccharide (LPS), tumor necrosis factor (TNF)-alpha, Toll-like receptor agonists, and nitric oxide. CXCL8 (formerly known as interleukin-8) binds with high-affinity and activates both receptors. CXCR1 also binds CXCL7 (neutrophil-activating protein-2), whereas CXCR2 non-selectively binds to all seven ELR-positive chemokines (CXCL1-7). Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines
LALCVIYVLVFLLSLPGNSLVVLVILYNRRSRSSTDVYLLHLAIADLLFALTLPFWAVSVVKGWIFGTFM
CKLVSLLQEANFYSGILLLACISVDRYLAIVHATRALTQKRHLVKFVCAGVWLLSLLLSLPALLNRDAFK
PPNSGRTVCYENLGNESADKWRVVLRILRHTLGFLLPLVVMLFCYGFTIKTLLQTRSFQKHRAMRVIFAV
VLAFLLCWLPYNVTVLIDTLMRTKLITETCELRNHVDVALYVTQILGFLHSCINPVLYAFIGQKFRNNL
>gnl|CDD|341334 cd15179, 7tmA_CXCR4, CXC chemokine receptor type 4, member of the class A family of seven-transmembrane G protein-coupled receptors. CXCR4 is the only known G protein-coupled chemokine receptor for the key homeostatic ligand CXCL12, which is constitutively secreted by bone marrow stromal cells. Atypical chemokine receptor CXCR7 (ACKR3) also binds CXCL12, but activates signaling in a G protein-independent manner. CXCR4 is also a co-receptor for HIV infection and plays critical roles in the development of immune system during both lymphopoiesis and myelopoiesis. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines
IFLPTVYSIIFLLGIVGNGLVILVMGYQKKSRTMTDKYRLHLSVADLLFVLTLPFWAVDAAANWYFGNFL
CKAVHVIYTVNLYSSVLILAFISLDRYLAIVHATNSQRPRKLLAEKVVYVGVWLPALLLTVPDLVFAKVS
ELDDRYICDRIYPEDTFELWVVAFRFQHILVGLVLPGLVILTCYCIIISKLSHSKGHQKRKALKTTVILI
LAFFACWLPYYIGISIDTFMLLEIIKQSCEMEQTVHKWISITEALAFFHCCLNPILYAFLGAKFKTSA
>gnl|CDD|341335 cd15180, 7tmA_CXCR3, CXC chemokine receptor type 3, member of the class A family of seven-transmembrane G protein-coupled receptors. CXCR3 is an inflammatory chemotactic receptor for a group of CXC chemokines distinguished by the presence of the amino acid motif ELR immediately adjacent to their CXC motif. CXCR3 specifically binds three chemokines CXCL9 (monokine induced by gamma-interferon), CXCL10 (interferon induced protein of 10 kDa), and CXCL11 (interferon inducible T-cell alpha-chemoattractant, I-TAC). CXC3R is expressed on CD4+ Th1 and CD8+ cytotoxic T lymphocytes as well as highly on innate lymphocytes, such as NK cells and NK T cells, where it may mediate the recruitment of these cells to the sites of infection and inflammation. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines
VFLPVLYSLVFLLGLLGNGLVLAVLLQKRRNLSVTDTFILHLALADILLLVTLPFWAVQAVHGWIFGTGL
CKLAGAVFKINFYCGIFLLACISFDRYLSIVHAVQMYSRKKPMLVHLSCLIVWLFCLLLSIPDFIFLEAT
KDPRQNKTECVHNFPQSDTYWWLALRLLYHIVGFLLPLAVMVYCYTSILLRLLRSSQGFQKQRAIRVIVA
VVVVFFLCWTPYNIALLVDTLIDLSVLDRNCGTESRLDIALSVTSSLGYFHCCLNPLLYAFVGVKFRRKL
>gnl|CDD|341336 cd15181, 7tmA_CXCR5, CXC chemokine receptor type 5, member of the class A family of seven-transmembrane G protein-coupled receptors. CXCR5 is a B-cell selective receptor that binds specifically to the homeostatic chemokine CXCL13 and regulates adaptive immunity. The receptor is found on all peripheral blood and tonsillar B cells and is involved in lymphocyte migration (homing) to specific tissues and development of normal lymphoid tissue. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines
VFIPLAYSLVFLLGVVGNGLVLTILLRRRRSRRTTENYLLHLALADLLLLLTFPFSVVESIAGWVFGTFL
CKLVGAIHKLNFYCSSLLLACISVDRYLAIVHAIHSYRHRRLRSVHLTCGSIWLVCFLLSLPNLVFLEVE
TSTNANRTSCSFHQYGIHESNWWLTSRFLYHVVGFFLPLLIMGYCYATIVVTLCQSSRRLQKQKAIRVAI
LVTLVFCLCWLPYNIVIFLDTLDDLKAVVKNCKLNDLLDAAITVTESLGFSHCCLNPILYAFIGVKFRND
L
>gnl|CDD|341337 cd15182, 7tmA_XCR1, XC chemokine receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. XCR1 is a chemokine receptor specific for XCL1 and XCL2 (previously called lymphotactin alpha/beta), which differ in only two amino acids. XCL1/2 is the only member of the C chemokine subfamily, which is unique as containing only two of the four cysteines that are found in other chemokine families. Human XCL1/2 has been shown to be secreted by activated CD8+ T cells and upon activation of the innate immune system. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling
AFLPVFYYLVFLLSLLGNGLVLWILVKYEKLKTLTNIFILNLAISDLLFTFTLPFWASYHSSGWIFGEIL
CKAVTSIFYIGFYSSILFLTLMTIDRYLAVVHPLSALRSRKLRYASLVSVAVWVISILASLPELILSTVM
KSDEDGSLCEYSSIKWKLGYYYQQNLFFLIPLGIIVYCYVRILQTLMRTRTMRKHRTVKLIFVIVLVFFL
SWAPYNIVIFLRSLKDLTIPICECSKQLDYAFYICRNIAFSHCCLNPVFYVFVGVKFRNHL
>gnl|CDD|320311 cd15183, 7tmA_CCR1, CC chemokine receptor type 1, member of the class A family of seven-transmembrane G protein-coupled receptors. CCR1 is widely expressed on both hematopoietic and non-hematopoietic cells and binds to the inflammatory CC chemokines CCL3, CCL5, CCL6, CCL9, CCL15, and CCL23. CCR1 activates the typical chemokine signaling pathway through the G(i/o) type of G proteins, causing inhibition of adenylate cyclase and stimulation of phospholipase C, PKC, calcium flux, and PLA2. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines
TLLPPLYSLVFIIGVVGNVLVVLVLIQHKRLRNMTSIYLFNLAISDLVFLFTLPFWIDYKLKDDWIFGDA
MCKFLSGFYYLGLYSEIFFIILLTIDRYLAIVHAVFALRARTVTFGIITSIITWALAILASMPCLYFFKS
QWEFTHHTCSAHFPRKSLIRWKRFQALKLNLLGLILPLLVMIICYTGIINILLRRPNEKKAKAVRLIFVI
TLLFFLLWTPYNLAAFVSAFQDVLFTPSCEQSQQLDLALQVTEVIAYTHCCVNPVIYVFVGERFRKYL
>gnl|CDD|341338 cd15184, 7tmA_CCR5_CCR2, CC chemokine receptor types 5 and 2, member of the class A family of seven-transmembrane G protein-coupled receptors. CCR2 and CCR5 share very high amino acid sequence identity. Both receptors play important roles in the trafficking of monocytes/macrophages and are implicated in the pathogenesis of immunologic diseases (rheumatoid arthritis, celiac disease, and transplant rejection) and cardiovascular diseases (atherosclerosis and autoimmune hepatitis). CCR2 is a receptor specific for members of the monocyte chemotactic protein family, including CCL2, CCL7, and CCL13. Conversely, CCR5 is a major co-receptor for HIV infection and binds many CC chemokine ligands, including CC chemokine ligands including CCL2, CCL3, CCL4, CCL5, CCL11, CCL13, CCL14, and CCL16. CCR2 is expressed primarily on blood monocytes and memory T cells, whereas CCR5 is expressed on antigen-presenting cells (macrophages and dendritic cells) and activated T effector cells. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines
RLLPPLYSLVFIFGFVGNMLVVLILINCKKLKSMTDIYLLNLAISDLLFLLTLPFWAHYAANEWVFGNAM
CKLLTGLYHIGFFSGIFFIILLTIDRYLAIVHAVFALKARTVTFGVVTSVVTWVVAVFASLPGIIFTKSQ
KEGSHYTCSPHFPPSQYQFWKNFQTLKMNILGLVLPLLVMIICYSGILKTLLRCRNEKKRHKAVRLIFTI
MIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPVIYAFVGEKFRSYL
>gnl|CDD|341339 cd15185, 7tmA_CCR3, CC chemokine receptor type 3, member of the class A family of seven-transmembrane G protein-coupled receptors. CCR3 is a highly promiscuous receptor that binds a variety of inflammatory CC-type chemokines, including CCL11 (eotaxin-1), CCL3L1, CCL5 (regulated on activation, normal T cell expressed and secreted; RANTES), CCL7 (monocyte-specific chemokine 3 or MCP-3), CCL8 (MCP-2), CCL11, CCL13 (MCP-4), CCL15, CCL24 (eotaxin-2), CCL26 (eotaxin-3), and CCL28. Among these, the eosinophil chemotactic chemokines (CCL11, CCL24, and CCL26) are the most potent and specific ligands. In addition to eosinophil, CCR3 is expressed on cells involved in allergic responses, such as basophils, Th2 lymphocytes, and mast cells. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines
QFLPPLYSLVFIVGLLGNVVVVVILIKYRRLRIMTNIYLLNLAISDLLFLFTLPFWIHYVRWNNWVFGHG
MCKLLSGFYYLGLYSEIFFIILLTIDRYLAIVHAVFALRARTVTFGIITSIITWGLAVLAALPEFIFYET
QELFEEFLCSPLYPEDTEDSWKRFHALRMNIFGLALPLLIMVICYTGIIKTLLRCPSKKKYKAIRLIFVI
MVVFFIFWTPYNLVLLLSAFQSIFFETDCERSKHLDLAMQVTEVIAYTHCCINPVIYAFVGERFRKYL
>gnl|CDD|320314 cd15186, 7tmA_CX3CR1, CX3C chemokine receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. CX3CR1 is an inflammatory receptor specific for CX3CL1 (also known as fractalkine in human), which is involved in the adhesion and migration of leukocytes. The CX3C chemokine subfamily is only represented by CX3CL1, which exists in both soluble and membrane-anchored forms. Membrane-anchored form promotes strong adhesion of receptor-bearing leukocytes to CX3CL1-expressing endothelial cells. On the other hand, soluble CX3CL1, which is released by the proteolytic cleavage of membrane-anchored CX3CL1, is a potent chemoattractant for CX3CR1-expressing T cells and monocytes. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling
IFLSIFYSLVFAFGLVGNLLVVLALTNSGKSKSITDIYLLNLALSDLLFVATLPFWTHYLINEWGLHNAM
CKLTTAFFFIGFFGGIFFITVISIDRYLAIVLAANSMNNRTVQHGVTISLGVWAAAILVAVPQFMFTKMK
ENECLGDYPEVLQEIWPVLRNVELNFLGFLLPLLIMSYCYFRIIQTLFSCKNHKKARAIKLILLVVIVFF
LFWTPYNVMIFLETLKLYDFFPSCDMKKDLRLALSVTETIAFSHCCLNPLIYAFAGEKFRRYL
>gnl|CDD|320315 cd15187, 7tmA_CCR8, CC chemokine receptor type 8, member of the class A family of seven-transmembrane G protein-coupled receptors. CCR8, the receptor for the CC chemokines CCL1 and CC16, is highly expressed on allergen-specific T-helper type 2 cells, and is implicated in the pathogenesis of human asthma. CCL1- and CCR8-expressing CD4+ effector T lymphocytes are shown to have a critical role in lung mucosal inflammatory responses. CCR8 is also a functional receptor for CCL16, a liver-expressed CC chemokine that involved in attracting lymphocytes, dendritic cells, and monocytes. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines
LFLPVLYCLLFVFGLLGNSLVIWVLVACKKLRSMTDVYLLNLAASDLLFVFSLPFQAYYLLDQWVFGNAM
CKIVSGAYYIGFYSSMFFITLMSIDRYLAIVHAVYALKVRTASHGTILSLALWLVAILASVPLLVFYQVA
SEDGRLQCIPFYPGQGNSWKVFTNFEVNILGLLIPFSILIFCYHNILRNLRRCHNQNKTKAIKLVFIVVI
VFFLFWTPFNVVLFLDSLHSLHIIDGCQNSQRLTLALHLTETISFTHCCLNPVIYAFVGEKFKKHL
>gnl|CDD|320316 cd15188, 7tmA_ACKR2_D6, atypical chemokine receptor 2, member of the class A family of seven-transmembrane G protein-coupled receptors. ACKR2 (also known as D6) binds non-selectively to all inflammatory CC-chemokines, but not to homeostatic CC-chemokines involved in controlling the migration of cells. Unlike the classical chemokine receptors that contain a conserved DRYLAIV motif in the second intracellular loop, which is required for G-protein coupling, the ACKRs lack this conserved motif and fail to couple to G-proteins and induce classical GPCR signaling. Five receptors have been identified for the ACKR family, including CC-chemokine receptors like 1 and 2 (CCRL1 and CCRL2), CXCR7, Duffy antigen receptor for chemokine (DARC), and D6. Both ACKR1 (DARC) and ACKR3 (CXCR7) show low sequence homology to the classic chemokine receptors
VFLPVFYTLVFLLGLAGNLLLFVVLLLYVPKKKKMTEVYLLNLAVSDLLFLVTLPFWAMYVAWHWVFGSF
LCKFVSTLYTINFYSGIFFVSCMSLDKYLEIVHAQSPHRLRTRRKSLLVLVAVWVLSIALSVPDMVFVQT
HHTNNGVWVCHADYGGHHTIWKLVFQFQQNLLGFLFPLLAMVFFYSRIACVLTRLRPPGQGRALRFVAAL
VVVFFVLWFPYNLTLFLHSLQDLHVIGNCERSRHLDYALQVTESLAFVHCCLNPLLYAFVSKRFRLYL
>gnl|CDD|320317 cd15189, 7tmA_Bradykinin_R, bradykinin receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. The bradykinin receptor family is a group of the seven transmembrane G-protein coupled receptors, whose endogenous ligand is the pro-inflammatory nonapeptide bradykinin that mediates various vascular and pain responses. Two major bradykinin receptor subtypes, B1 and B2, have been identified based on their pharmacological properties. The B1 receptor is rapidly induced by tissue injury and inflammation, whereas the B2 receptor is ubiquitously expressed on many tissue types. Both receptors contain three consensus sites for N-linked glycosylation in extracellular domains and couple to G(q) protein to activate phospholipase C, leading to phosphoinositide hydrolysis and intracellular calcium mobilization. They can also interact with G(i) protein to inhibit adenylate cyclase and activate the MAPK (mitogen-activated protein kinase) pathways
RIIPPFIFSLCLFGLLGNLFVLLVFLLHRRRLTVAEIYLGNLAAADLVFVSGLPFWAMNILNQFNWPFGE
LLCRVVNGVIKVNLYTSIYLLVMISQDRYLALVKTMAARRLRRRRYAKLICVLIWVVGLLLSIPTFLLRK
IKAIPDLNITACVLLYPHEAWHFAHIVLLNIVGFLLPLLVITFCNYNILQALRTREESTRCEDRNDSKAT
ALVLAVTLLFLVCWGPYHFFTFLDFLFDVGVLDECFWEHFIDIGLQLAVFLAFSNSCLNPVLYVFVGRYF
RRKV
>gnl|CDD|341340 cd15190, 7tmA_Apelin_R, apelin receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Apelin (APJ) receptor is a G protein-coupled receptor that binds the endogenous peptide ligands, apelin and Toddler/Elabela. APJ is an adipocyte-derived hormone that is ubiquitously expressed throughout the human body and Toddler/Elabela is a short secretory peptide that is required for normal cardiac development in zebrafish. Activation of APJ receptor plays key roles in diverse physiological processes including vasoconstriction and vasodilation, cardiac muscle contractility, angiogenesis, and regulation of water balance and food intake
CDYTEWKPSYALIPVIYMLVFVLGLSGNGLVLWTVFRSKRKRRRSADTFIANLALADLTFVVTLPLWAVY
TALGYHWPFGSFLCKLSSYLVFVNMYASVFCLTGLSFDRYLAIVRSLASAKLRSRTSGIVALGVIWLLAA
LLALPALILRTTSDLEGTNKVICDMDYSGVVSNESEWAWIAGLGLSSTVLGFLLPFLIMLTCYFFIGRTV
ARHFSKLRRKEDKKKRRLLKIIITLVVTFALCWLPFHLVKTLYALMYLGILPFSCGFDLFLMNAHPYATC
LAYVNSCLNPFLYAFFDPRFRQQC
>gnl|CDD|341341 cd15191, 7tmA_AT2R, type 2 angiotensin II receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Angiotensin II (Ang II), the main effector in the renin-angiotensin system, plays a crucial role in the regulation of cardiovascular homeostasis through its type 1 (AT1) and type 2 (AT2) receptors. Ang II contributes to cardiovascular diseases such as hypertension and atherosclerosis via AT1R activation. Ang II increases blood pressure through Gq-mediated activation of phospholipase C, resulting in phosphoinositide (PI) hydrolysis and increased intracellular calcium levels. Through the AT2R, Ang II counteracts the vasoconstrictor action of AT1R and thereby induces vasodilation, sodium excretion, and reduction of blood pressure. Moreover, AT1R promotes cell proliferation, whereas AT2R inhibits proliferation and stimulates cell differentiation. The AT2R is highly expressed during fetal development, however it is scarcely present in adult tissues and is induced in pathological conditions. Generally, the AT1R mediates many actions of Ang II, while the AT2R is involved in the regulation of blood pressure and renal function
TAIPVLYSIIFILGFLGNSLVVCVFCHQSGPKTVASIYIFNLAVADLLFLATLPLWATYYSYGYNWLFGS
VMCKICGSLLTLNLFASIFFITCMSVDRYLAVVYPLRSQRRRSWQARLVCLLVWVLACLSSLPTFYFRDT
YYIEELGVNACIMAFPNEKYAQWSAGLALMKNTLGFLIPLIVIATCYFGIGRHLLKTKGFGKNKQRRDKV
LKMVAAVVLAFLICWFPFHVLTFLDALARMGVINNCWVITVIDKALPFAICLGFSNSCINPFLYCFVGNH
FREKL
>gnl|CDD|320320 cd15192, 7tmA_AT1R, type 1 angiotensin II receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Angiotensin II (Ang II), the main effector in the renin-angiotensin system, plays a crucial role in the regulation of cardiovascular homeostasis through its type 1 (AT1) and type 2 (AT2) receptors. Ang II contributes to cardiovascular diseases such as hypertension and atherosclerosis via AT1R activation. Ang II increases blood pressure through Gq-mediated activation of phospholipase C, resulting in phosphoinositide (PI) hydrolysis and increased intracellular calcium levels. Through the AT2R, Ang II counteracts the vasoconstrictor action of AT1R and thereby induces vasodilation, sodium excretion, and reduction of blood pressure. Moreover, AT1R promotes cell proliferation, whereas AT2R inhibits proliferation and stimulates cell differentiation. The AT2R is highly expressed during fetal development, however it is scarcely present in adult tissues and is induced in pathological conditions. Generally, the AT1R mediates many actions of Ang II, while the AT2R is involved in the regulation of blood pressure and renal function
IMIPTVYSIIFVVGIFGNSLVVIVIYCYMKLKTVANIFLLNLALADLCFLITLPLWAAYTAMEYHWPFGN
FLCKIASALVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTLVVARVTCIVIWLLAGVASLPAIIHRD
VFFIENTNITVCAFHYPSQNSTLLVGLGLMKNLLGFLIPFLIILTCYTLIGKALKKAYEIQRNKPRNDEI
FKMIMAVVLFFFFCWIPHQIFTFLDVLIQLKVIQDCHIADIVDTAMPFTICIAYFNSCLNPILYGFVGKN
FRKKF
>gnl|CDD|320321 cd15193, 7tmA_GPR25, G protein-coupled receptor 25, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR25 is an orphan G-protein coupled receptor that shares strong sequence homology to GPR15 and the angiotensin II receptors. These closely related receptors form a group within the class A G-protein coupled receptors (GPCRs). GPR15 controls homing of T cells, especially FOXP3(+) regulatory T cells, to the large intestine mucosa and thereby mediates local immune homeostasis. Moreover, GRP15-deficient mice were shown to be prone to develop more severe large intestine inflammation. Angiotensin II (Ang II), the main effector in the renin-angiotensin system, plays a crucial role in the regulation of cardiovascular homeostasis through its type 1 (AT1) and type 2 (AT2) receptors
IYIPILYLIIFFTGLLGNLFVIALMSKRSTTKRLVDTFVLNLAVADLVFVLTLPFWAASTALGGQWLFGE
GLCKLSSFIIAVNRCSSILFLTGMSVDRYLAVVKLLDSRPLRTRRCALITCCIIWAVSLVLGIPSLVYRN
LINESVCVEDSSSRFFQGISLATLFLTFVLPLIVILFCYCSILVRLRRHFHGAKRTGRRRRNSLRIVFAI
VTAFVLSWLPFNTLKAVRLLLELGGGVLPCHTTVAIRQGLTITACLAFVNSCVNPLIYSLLDRHFRRRA
>gnl|CDD|320322 cd15194, 7tmA_GPR15, G protein-coupled receptor 15, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR15, also called as Brother of Bonzo (BOB), is an orphan G-protein coupled receptor that was originally identified as a co-receptor for human immunodeficiency virus. GPR15 is upregulated in patients with rheumatoid arthritis and shares high sequence homology with angiotensin II type AT1 and AT2 receptors; however, its endogenous ligand is unknown. GPR15 controls homing of T cells, especially FOXP3(+) regulatory T cells, to the large intestine mucosa and thereby mediates local immune homeostasis. Moreover, GRP15-deficient mice were shown to be prone to develop more severe large intestine inflammation
GFLPILYCLVFLVGAVGNAILMGALVFKRGVRRLIDIFISNLAASDFIFLVTLPLWVDKEVVLGPWRSGS
FLCKGSSYIISVNMYCSVFLLTCMSLDRYLAIVLPLVSRKFRTKHNAKVCCTCVWMLSCLLGLPTLLSRE
LKKYEEKEYCNEDAGTPSKVIFSLVSLIVAFFLPLLSILTCYCTIIWKLCHHYQKSGKHQKKLRKSIKIV
FIVVAAFVFSWMPFNLFKALAIASGLQVEVTCLPYTLAQLGMEVSAPLAFANSCANPFIYYFFDRYIRRA
I
>gnl|CDD|320323 cd15195, 7tmA_GnRHR-like, gonadotropin-releasing hormone and adipokinetic hormone receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Gonadotropin-releasing hormone (GnRH) and adipokinetic hormone (AKH) receptors share strong sequence homology to each other, suggesting that they have a common evolutionary origin. GnRHR, also known as luteinizing hormone releasing hormone receptor (LHRHR), plays an central role in vertebrate reproductive function; its activation by binding to GnRH leads to the release of follicle stimulating hormone (FSH) and luteinizing hormone (LH) from the pituitary gland. Adipokinetic hormone (AKH) is a lipid-mobilizing hormone that is involved in control of insect metabolism. Generally, AKH behaves as a typical stress hormone by mobilizing lipids, carbohydrates and/or certain amino acids such as proline. Thus, it utilizes the body's energy reserves to fight the immediate stress problems and subdue processes that are less important. Although AKH is known to responsible for regulating the energy metabolism during insect flying, it is also found in insects that have lost its functional wings and predominantly walk for their locomotion. Both GnRH and AKH receptors are members of the class A of the seven-transmembrane, G-protein coupled receptor (GPCR) superfamily
LVRVLVTWVLFVISAAGNLTVLIQLFRRRRAKSHIQILIMHLALADLMVTFFNMPMDAVWNYTVEWLAGD
LMCRVMMFLKQFGMYLSSFMLVVIALDRVFAILSPLSANQARKRVKIMLTVAWVLSALCSIPQSFIFSVL
RKMPEQPGFHQCVDFGSAPTKKQERLYYFFTMILSFVIPLIITVTCYLLILFEISKMAKRARDTPISNRR
RSRTNSLERARMRTLRMTALIVLTFIVCWGPYYVLGLWYWFDKESIKNLPPALSHIMFLLGYLNPCLHPI
IYGVFMKEIRNWI
>gnl|CDD|320324 cd15196, 7tmA_Vasopressin_Oxytocin, vasopressin and oxytocin receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Vasopressin (also known as arginine vasopressin or anti-diuretic hormone) and oxytocin are synthesized in the hypothalamus and are released from the posterior pituitary gland. The actions of vasopressin are mediated by the interaction of this hormone with three receptor subtypes: V1aR, V1bR, and V2R. These subtypes are differ in localization, function, and signaling pathways. Activation of V1aR and V1bR stimulate phospholipase C, while activation of V2R stimulates adenylate cyclase. Although vasopressin and oxytocin differ only by two amino acids and stimulate the same cAMP/PKA pathway, they have divergent physiological functions. Vasopressin is involved in regulating blood pressure and the balance of water and sodium ions, whereas oxytocin plays an important role in the uterus during childbirth and in lactation
KVEIAVLATILVLALFGNSCVLLVLYRRRRKLSRMHLFILHLSVADLLVALFNVLPQLIWDITYRFYGGD
LLCRLVKYLQVVGMYASSYVLVATAIDRYIAICHPLSSHRWTSRRVHLMVAIAWVLSLLLSIPQLFIFSY
QEVGSGVYDCWATFEPPWGLRAYITWFTVAVFVVPLIILAFCYGRICYVVWRAKIKTVKLTLVVVACYIV
CWTPFFVVQMWAAWDPTAPIEGPAFVIIMLLASLNSCTNPWIYLAFSGNLRRAL
>gnl|CDD|320325 cd15197, 7tmA_NPSR, neuropeptide S receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Neuropeptide S (NPS) promotes arousal and anxiolytic-like effects by activating its cognate receptor NPSR. NPSR is widely expressed in the brain, and its activation induces an elevation of intracellular calcium and cAMP concentrations, presumably by coupling to G(s) and G(q) proteins. Mutations in NPSR have been associated with an increased susceptibility to asthma. NPSR was originally identified as an orphan receptor GPR154 and is also known as G protein receptor for asthma susceptibility (GPRA) or vasopressin receptor-related receptor 1 (VRR1)
TEQLATLWVLFVFIVVGNSSVLFALWMRKAKKSRMNFFITQLAIADLCVGLINVLTDIIWRITVEWRAGD
FACKVIRYLQVVVTYASTYVLVALSIDRYDAICHPMNFSQSGRQARVLICVAWILSALFSIPMLIIFEKT
GLSNGEVQCWILWPEPWYWKVYMTIVAFLVFFIPATIISICYIIIVRTIWKKSKIQVTINKAGLHDGSSR
RSSSRGIIPRAKIKTIKMTFVIVTVFIICWSPYFVFDLLDVFGLLPRSKTKIAAATFIQSLAPLNSAINP
LIYCLFSTHLCRPL
>gnl|CDD|320326 cd15198, 7tmA_GPR150, G protein-coupled receptor 150, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR150 is an orphan receptor closely related to the oxytocin and vasopressin receptors. Its endogenous ligand is not known. These receptors share a significant amino acid sequence similarity, suggesting that they have a common evolutionary origin
RTRLIFLGVILVAGVAGNTTVLCWLCGGRRRKSRMNFLLLQLALADLLVIGGTALSQIIWELLGDRWMAG
DVACRLLKLLQASARGASANLVVLLALDRHQAIRAPLGQPLRAWKLAALGWLLALLLALPQAYVFRVDFP
DDPASAWPGHTLCRGIFAPLPRWHLQVYATYEAVVGFVAPVVILGVCYGRLLLKWWERANQAPGAKKPWK
KPSKSHLRATAPSALPRAKVKTLKMTLVIALLFVGCSLPYFIAELAAAFGSGDWEPEKVAAALGVMAVAN
SATNPFVFLFFNAGDCRLR
>gnl|CDD|320327 cd15199, 7tmA_GPR31, G protein-coupled receptor 31, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR31, also known as 12-(S)-HETE receptor, is a high-affinity receptor for 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid. Phylogenetic analysis showed that GPR31 and oxoeicosanoid receptor 1 (OXER1, GPR170) are the most closely related receptors to the hydroxycarboxylic acid receptor family (HCARs). GPR31, like OXER1, activates the ERK1/2 (MAPK3/MAPK1) pathway of intracellular signaling, but unlike the OXER1, does not cause increase in the cytosolic calcium level. GPR31 is also shown to activate NFkB. 12-(S)-HETE is a 12-lipoxygenase metabolite of arachidonic acid produced by mammalian platelets and tumor cells. It promotes tumor cells adhesion to endothelial cells and sub-endothelial matrix, which is a critical step for metastasis
IAYASLLILEFGLGLPGNAIALWTFIFRLKVWKPYAVYLLNLVLADVLLLICLPFKAYFYLNGNRWSLGG
GTCKALLFMLSLSRGVSIAFLTAVALDRYFRVVHPRGKKNSLSLQAAPYISFLVWLLLVGLTIPTLLASQ
PKNFTECNSFSPKDDEDFSDTWQEAVFFLQFLLPFGLIVFCTVRIIRRLKKRLRDVGKQPKLQRAMALVT
SVVVVFGFCFLPCFLARVLMLIFQNKESCNALNIAVHTYDVTMCLTYLNSVLDPIVYCFSSPTFRSSY
>gnl|CDD|320328 cd15200, 7tmA_OXER1, oxoeicosanoid receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. OXER1, also called GPR170, is a receptor for eicosanoids and polyunsaturated fatty acids such as 5-oxo-6E,8Z,11Z,14Z-eicosatetraenoic acid (5-OXO-ETE), 5(S)-hydroperoxy-6E,8Z,11Z,14Z-eicosatetraenoic acid (5(S)-HPETE) and arachidonic acid. OXER1 is a member of the class A family of seven-transmembrane G-protein coupled receptors and appears to be coupled to the G(i/o) protein. The receptor is expressed in various tissues except brain. Phylogenetic analysis showed that GPR31 and OXER1 are the most closely related receptors to the hydroxycarboxylic acid receptor family (HCARs). OXER1, like GPR31, activates the ERK1/2 (MAPK3/MAPK1) pathway of intracellular signaling, but unlike GPR31, does cause increase in the cytosolic calcium level
AFLAPVLGIEFVLGLVGNGIALFIFCFHRRPWKSNTMYLLSLVVADFFLIINLPFRIDYYLRNEVWRFGA
TACQVNLFMLSMNRTASIVFLTAIALNRYLKVVHPHHQLSKASVGCAAKVAAGLWILILLLNIHLLLLDH
VQSNSTCLSYDHGTDPSASDRWHRILFFLEFFLPLGIILFCIFSIILTLKQRKLAKQAGPQRAVKVLAVI
VLVYTVCFLPSILFALASLVAFKVSQCRSLDLCTQLFHGSLAFTYLNSALDPVLYCFSSPSFLNQS
>gnl|CDD|320329 cd15201, 7tmA_HCAR1-3, hydroxycarboxylic acid receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Hydroxycarboxylic acid receptor (HCAR) subfamily, a member of the class A G-protein coupled receptors (GPCRs), contains three receptor subtypes: HCAR1, HCAR2, and HCAR3. The endogenous ligand of HCAR1 (also known as lactate receptor 1, GPR104, or GPR81) is L-lactic acid. The endogenous ligands of HCAR2 (also known as niacin receptor 1, GPR109A, or nicotinic acid receptor) and HCAR3 (also known as niacin receptor 2 or GPR109B) are 3-hydroxybutyric acid and 3-hydroxyoctanoic acid, respectively. Because nicotinic acid is capable of stimulating HCAR2 at higher concentrations only (in the range of sub-micromolar concentration), it is unlikely that nicotinic acts as a physiological ligand of HCAR2. All three receptors are expressed in adipocytes and mediate anti-lipolytic effects in fat cells through G(i) type G protein-dependent inhibition of adenylate cyclase
YVLPPVLILEFVLGLLGNGLALWIFCFHLKSWKSSTVYLFNLAVADFLLIICLPFRTDYYLRGKHWKFGD
IPCRIVLFMLAMNRAGSIFFLTAVAVDRYFRVVHPHHRINSISVRKAAIIACGLWLLTIAMTVYLLTKKH
LFPRGNATQCESFNICTGTDSSSNWHEAMFLLEFFLPLAIILYCSVRIIWQLRGRQLDRHAKIKRAVQFI
MVVAIVFIICFLPSNVTRIAIWILKHTSNEDCQYYRSVDLAFYITISFTYFNSMLDPVVYYFSSPSFKNF
Y
>gnl|CDD|320330 cd15202, 7tmA_TACR-like, tachykinin receptors and related receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes the neurokinin/tachykinin receptors and its closely related receptors such as orphan GPR83 and leucokinin-like peptide receptor. The tachykinins are widely distributed throughout the mammalian central and peripheral nervous systems and act as excitatory transmitters on neurons and cells in the gastrointestinal tract. The TKs are characterized by a common five-amino acid C-terminal sequence, Phe-X-Gly-Leu-Met-NH2, where X is a hydrophobic residue. The three major mammalian tachykinins are substance P (SP), neurokinin A (NKA), and neurokinin B (NKB). The physiological actions of tachykinins are mediated through three types of receptors: neurokinin receptor type 1 (NK1R), NK2R, and NK3R. SP is a high-affinity endogenous ligand for NK1R, which interacts with the Gq protein and activates phospholipase C, leading to elevation of intracellular calcium. NK2R is a high-affinity receptor for NKA, the tachykinin neuropeptide substance K. SP and NKA are found in the enteric nervous system and mediate in the regulation of gastrointestinal motility, secretion, vascular permeability, and pain perception. NK3R is activated by its high-affinity ligand, NKB, which is primarily involved in the central nervous system and plays a critical role in the regulation of gonadotropin hormone release and the onset of puberty
VLLIVAYSFIIVFSLFGNVLVCWIIFKNQRMRTVTNYFIVNLAVADIMITLFNTPFTFVRAVNNTWIFGL
FMCHFSNFAQYCSVHVSAYTLTAIAVDRYQAIMHPLKPRISKTKAKFIIAVIWTLALAFALPHAICSKLE
TFKYSEDIVRSLCLEDWPERADLFWKYYDLALFILQYFLPLLVISFAYARVGIKLWASNMPGDATTERYF
ALRRKKKKVIKMLMVVVVLFALCWLPFNIYVLLLSSKPDYLIKTINAVYFAFHWLAMSSTCYNPFIYCWL
NERFRIEF
>gnl|CDD|320331 cd15203, 7tmA_NPYR-like, neuropeptide Y receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. NPY is a 36-amino acid peptide neurotransmitter with a C-terminal tyrosine amide residue that is widely distributed in the brain and the autonomic nervous system of many mammalian species. NPY exerts its functions through five, G-protein coupled receptor subtypes including NPY1R, NPY2R, NPY4R, NPY5R, and NPY6R; however, NPY6R is not functional in humans. NYP receptors are also activated by its two other family members, peptide YY (PYY) and pancreatic polypeptide (PP). They typically couple to Gi or Go proteins, which leads to a decrease in adenylate cyclase activity, thereby decreasing intracellular cAMP levels, and are involved in diverse physiological roles including appetite regulation, circadian rhythm, and anxiety. Also included in this subgroup is prolactin-releasing peptide (PrRP) receptor (previously known as GPR10), which is activated by its endogenous ligand PrRP, a neuropeptide possessing C-terminal Arg-Phe-amide motif. There are two active isoforms of PrRP in mammals: one consists of 20 amino acid residues (PrRP-20) and the other consists of 31 amino acid residues (PrRP-31). PrRP receptor shows significant sequence homology to the NPY receptors, and a micromolar level of NPY can bind and completely inhibit the PrRP-evoked intracellular calcium response in PrRP receptor-expressing cells, suggesting that the PrRP receptor shares a common ancestor with the NPY receptors
IILILLYGLIIVLGVVGNLLVIYVVLRNKSMQTVTNIFILNLAVSDLLLCLVSLPFTLIYTLTKNWPFGS
ILCKLVPSLQGVSIFVSTLTLTAIAIDRYQLIVYPTRPRMSKRHALLIIALIWILSLLLSLPLAIFQELS
DVPIEILPYCGYFCTESWPSSSSRLIYTISVLVLQFVIPLLIISFCYFRISLKLRKRVKKKRGKRTLSSR
RRRSELRRKRRTNRLLIAMVVVFAVCWLPLNLFNLLRDFEPLPQIDGRHFYLIFLICHLIAMSSACVNPL
LYGWLNDNFRKEF
>gnl|CDD|320332 cd15204, 7tmA_prokineticin-R, prokineticin receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Prokineticins 1 (PROK1) and 2 (PROK2), also known as endocrine gland vascular endothelial factor and Bombina varigata 8, respectively, are multifunctional chemokine-like peptides that are highly conserved across species. Prokineticins can bind with similar affinities to two closely homologous 7-transmembrane G protein coupled receptors, PROKR1 and PROKR2, which are phylogenetically related to the tachykinin receptors. Prokineticins and their GPCRs are widely distributed in human tissues and are involved in numerous physiological roles, including gastrointestinal motility, generation of circadian rhythms, neuron migration and survival, pain sensation, angiogenesis, inflammation, and reproduction. Moreover, different point mutations in genes encoding PROK2 or its receptor (PROKR2) can lead to Kallmann syndrome, a disease characterized by delayed or absent puberty and impaired olfactory function
IVLGVVYVLIMLVCGVGNLLLIAVLARYKKLRTLTNLLIANLALSDFLVAVFCLPFEMDYYVVRQRSWTH
GDVLCAVVNYLRTVSLYVSTNALLVIAIDRYLVIVHPLKPRMKRRTACVVIALVWVVSLLLAIPSAVYSK
TTPYANQGKIFCGQIWPVDQQAYYKAYYLFLFVLEFVLPVLIMTLCYLRIVRKVWFRRVPGQQTEQIRRR
LRRRRRKVRLLVVILTAFVLCWAPYYGYAIVRDFFPTLLSKEKLNTTIFYIVEALAMSNSMINTVVYVAF
NNNIRKYL
>gnl|CDD|320333 cd15205, 7tmA_QRFPR, pyroglutamylated RFamide peptide receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. 26RFa, also known as QRFP (Pyroglutamylated RFamide peptide), is a 26-amino acid residue peptide that belongs to a family of neuropeptides containing an Arg-Phe-NH2 (RFamide) motif at its C-terminus. 26Rfa/QRFP exerts similar orexigenic activity including the regulation of feeding behavior in mammals. It is the ligand for G-protein coupled receptor 103 (GPR103), which is predominantly expressed in paraventricular (PVN) and ventromedial (VMH) nuclei of the hypothalamus. GPR103 shares significant protein sequence homology with orexin receptors (OX1R and OX2R), which have recently shown to produce a neuroprotective effect in Alzheimer's disease by forming a functional heterodimer with GPR103
TAFVITYVLIFVLALFGNSLVIYVVTRKRAMRTATNIFICSLALSDLLITFFCIPFTLLQNISSNWLGGA
FMCKMVPFVQSTAVVTSILTMTCIAVERHQGIVHPLKMKWQYTNRRAFTMLGLVWIVSVIVGSPMLFVQQ
LEVKYDFLYEKRHVCCLERWYSPTQQKIYTTFILVILFLLPLTTMLFLYSRIGYELWIKKRVGDASVLQT
IHGIEMSKISRKKKRAVKMMVTVVLLFAVCWAPFHVVHMMIEYSNLENKYDGVTIKLIFAIVQLIGFSNS
FNNPIVYAFMNENFKKNF
>gnl|CDD|320334 cd15206, 7tmA_CCK_R, cholecystokinin receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Cholecystokinin receptors (CCK-AR and CCK-BR) are a group of G-protein coupled receptors which bind the peptide hormones cholecystokinin (CCK) or gastrin. CCK, which facilitates digestion in the small intestine, and gastrin, a major regulator of gastric acid secretion, are highly similar peptides. Like gastrin, CCK is a naturally-occurring linear peptide that is synthesized as a preprohormone, then proteolytically cleaved to form a family of peptides with the common C-terminal sequence (Gly-Trp-Met-Asp-Phe-NH2), which is required for full biological activity. CCK-AR (type A, alimentary; also known as CCK1R) is found abundantly on pancreatic acinar cells and binds only sulfated CCK-peptides with very high affinity, whereas CCK-BR (type B, brain; also known as CCK2R), the predominant form in the brain and stomach, binds CCK or gastrin and discriminates poorly between sulfated and non-sulfated peptides. CCK is implicated in regulation of digestion, appetite control, and body weight, and is involved in neurogenesis via CCK-AR. There is some evidence to support that CCK and gastrin, via their receptors, are involved in promoting cancer development and progression, acting as growth and invasion factors
ELIIPLYSVIFLLAVVGNILVIVTLVQNKRMRTVTNVFLLNLAVSDLLLAVFCMPFTLVGQLLRNFIFGE
VMCKLIPYFQAVSVSVSTFTLVAISLERYFAICHPLKSRVWQTLSHAYKVIAGIWLLSFLIMSPILVFSN
LIPMSRPGGHKCREVWPNEIAEQAWYVFLDLMLLVIPGLVMSVAYGLISWTLLEAKKRVIRMLFVIVVEF
FICWTPLYVINTWKAFDPPSAARYVSSTTISLIQLLAYISSCVNPITYCFMNKRFRQAF
>gnl|CDD|320335 cd15207, 7tmA_NPFFR, neuropeptide FF receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Neuropeptide FF (NPFF) is a mammalian octapeptide that belongs to a family of neuropeptides containing an RF-amide motif at their C-terminus that have been implicated in a wide range of physiological functions in the brain including pain sensitivity, insulin release, food intake, memory, blood pressure, and opioid-induced tolerance and hyperalgesia. The effects of these peptides are mediated through neuropeptide FF1 and FF2 receptors (NPFF1-R and NPFF2-R) which are predominantly expressed in the brain. NPFF induces pro-nociceptive effects, mainly through the NPFF1-R, and anti-nociceptive effects, mainly through the NPFF2-R. NPFF has been shown to inhibit adenylate cyclase via the Gi protein coupled to NPFF1-R
VLFIVSYSLIFLLCVVGNVLVCLVVAKNPRMRTVTNYFILNLAVSDLLVGVFCMPFTLVDNILTGWPFGD
VMCKLSPLVQGVSVAASVFTLVAIAVDRYRAVVHPTEPKLTNRQAFVIIVAIWVLALAIMIPQALVLEVK
EYQFFRGQTVHICVEFWPSDEYRKAYTTSLFVLCYVAPLLIIAVLYVRIGYRLWFKPVPGGGSASREAQA
AVSKKKVRVIKMLIVVVVLFALSWLPLHTVTMLDDFGNLSPNQREVLYVYIYPIAHWLAYFNSCVNPIVY
GYFNRNFRKGF
>gnl|CDD|320336 cd15208, 7tmA_OXR, orexin receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Orexins (OXs, also referred to as hypocretins) are neuropeptide hormones that regulate the sleep-wake cycle and potently influence homeostatic systems regulating appetite and feeding behavior or modulating emotional responses such as anxiety or panic. OXs are synthesized as prepro-orexin (PPO) in the hypothalamus and then proteolytically cleaved into two forms of isoforms: orexin-A (OX-A) and orexin-B (OX-B). OXA is a 33 amino-acid peptide with N-terminal pyroglutamyl residue and two intramolecular disulfide bonds, whereas OXB is a 28 amino-acid linear peptide with no disulfide bonds. OX-A binds orexin receptor 1 (OX1R) with high-affinity, but also binds with somewhat low-affinity to OX2R, and signals primarily to Gq coupling, whereas OX-B shows a strong preference for the orexin receptor 2 (OX2R) and signals through Gq or Gi/o coupling. Thus, activation of OX1R or OX2R will activate phospholipase activity and the phosphatidylinositol and calcium signaling pathways. Additionally, OX2R activation can also lead to inhibition of adenylate cyclase
WVLIALYILVFIVGLVGNVLVCFAVWRNHHMRTVTNYFIVNLSLADFLVIIICLPATLLVDVTETWFFGQ
VLCKIIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARVSILIIWIVSLLIMIPQAIVMECS
RVVPLANKTILLTVCDERWSDSIYQKVYHICFFLVTYLLPLCLMILAYFQIFRKLWCRQIPGTSSVVQRK
WNKPRKSAVAAEEKQLRSRRKTAKMLIVVVIMFAICYLPVHLLNILRYVFGLFTVDRETIYAWFLFSHWL
VYANSAINPIIYNFMSGKFREEF
>gnl|CDD|320337 cd15209, 7tmA_Mel1, melatonin receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. Melatonin (N-acetyl-5-methoxytryptamine) is a naturally occurring sleep-promoting chemical found in vertebrates, invertebrates, bacteria, fungi, and plants. In mammals, melatonin is secreted by the pineal gland and is involved in regulation of circadian rhythms. Its production peaks during the nighttime, and is suppressed by light. Melatonin is shown to be synthesized in other organs and cells of many vertebrates, including the Harderian gland, leukocytes, skin, and the gastrointestinal (GI) tract, which contains several hundred times more melatonin than the pineal gland and is involved in the regulation of GI motility, inflammation, and sensation. Melatonin exerts its pleiotropic physiological effects through specific membrane receptors, named MT1A, MT1B, and MT1C, which belong to the class A rhodopsin-like G-protein coupled receptor family. MT1A and MT1B subtypes are present in mammals, whereas MT1C subtype has been found in amphibians and birds. The melatonin receptors couple to G proteins of the G(i/o) class, leading to the inhibition of adenylate cyclase
SALACVLIVTIVVDVLGNLLVILSVLRNKKLRNAGNIFVVSLSVADLVVAIYPYPLILHAIFHNGWTLGQ
LHCQASGFIMGLSVIGSIFNITAIAINRYCYICHSLQYDRLYSLRNTCCYLCLTWLLTVLAVLPNFFIGS
LQYDPRIYSCTFAQTVSTVYTITVVVIHFLLPLLIVSFCYLRIWVLVLQVRQRVKPDQRPKLKPADVRNF
LTMFVVFVLFAVCWAPLNFIGLAVAINPKEMAPKIPEWLFVASYFMAYFNSCLNAIIYGLLNQNFRKEY
>gnl|CDD|320338 cd15210, 7tmA_GPR84-like, G protein-coupled receptor 84 and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR84, also known as the inflammation-related G-Protein coupled receptor EX33, is a receptor for medium-chain free fatty acid (FFA) with carbon chain lengths of C9 to C14. Among these medium-chain FFAs, capric acid (C10:0), undecanoic acid (C11:0), and lauric acid (C12:0) are the most potent endogenous agonists of GPR84, whereas short-chain and long-chain saturated and unsaturated FFAs do not activate this receptor. GPR84 contains a [G/N]RY-motif instead of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of the rhodopsin-like class A receptors and important for efficient G protein-coupled signal transduction. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, which then activate the heterotrimeric G proteins. In the case of GPR84, activation of the receptor couples to a pertussis toxin sensitive G(i/o)-protein pathway. GPR84 knockout mice showed increased Th2 cytokine production including IL-4, IL-5, and IL-13 compared to wild-type mice. It has been also shown that activation of GPR84 augments lipopolysaccharide-stimulated IL-8 production in polymorphonuclear leukocytes and TNF-alpha production in macrophages, suggesting that GPR84 may function as a proinflammatory receptor
YFAAVWGIVFMVVGVPGNLLTVLALLRSKKLRTRTNAFIINLSISDLLFCAFNLPLAASTFLHQAWIHGE
TLCRVFPLLRYGLVAVSLLTLVLITLNRYILIAHPSLYPRIYTRRGLALMIAGTWIFSFGSFLPLWLGIW
GRFGLDPKVCSCSILRDKKGRSPKTFLFVFGFVLPCLVIIICYARREDRRLTRMMLVIFLCFLVCYLPIT
LVNVFDDEVAPPVLHIIAYVLIWLSSCINPIIYVAMNRQYRQAY
>gnl|CDD|320339 cd15211, 7tmA_GPR88-like, G protein-coupled receptor 88, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR88, an orphan G protein-coupled receptor, is predominantly and almost exclusively expressed within medium spiny neurons (MSNs) of the brain's striatum in both human and rodents; thus it is also called Striatum-specific GPCR (STRG). The striatum is known to involve in motor coordination, reward-based decision making, and response learning. GPR88 is shown to co-localize with both dopamine D1 and D2 receptors and displays the highest sequence similarity to receptors for biogenic amines such as dopamine and serotonin. GPR88 knockout mice showed abnormal behaviors observed in schizophrenia, such as disrupted sensorimotor gating, increased stereotypic behavior and locomotor activity in response to treatment with dopaminergic compounds such as apomorphine and amphetamine, respectively, suggesting a role for GPR88 in dopaminergic signaling. Furthermore, the transcriptional profiling studies showed that GPR88 expression is altered in a number of psychiatric disorders such as depression, drug addiction, bipolar and schizophrenia, providing further evidence that GPR88 plays an important role in CNS signaling pathways related to psychiatric disorder. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
SLSTVYSFLAVSGTLANVLVIYLVVSFKKLQTTSNAFIVNGCVADLLVCAFWMPQEAVLGSTGTLLVLGY
RLFREGLLFLGLTVSLLSHSLIALNRYVLITKLPAVYQALYQKRNTEWMIALSWALALGLLLPWLTSFRY
PTKSCHDSADGSFAVVSVLSSRYPALLLAFTVLGQTALVLHCYFGIFRRVQISVKRVSVLNFQIVNNLPY
SRPRKDKRLGLYVLLVCCVFLLTTEPLVWVSLAGLFVPVPVALQTASWLLFCTLFVLNPFLYTWKNEEFR
RSF
>gnl|CDD|320340 cd15212, 7tmA_GPR135, G protein-coupled receptor 135, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR135, also known as the somatostatin- and angiotensin-like peptide receptor (SALPR), is found in various tissues including eye, brain, cervix, stomach, and testis. Pharmacological studies have shown that relaxin-3 (R3) is a high-affinity endogenous ligand for GPR135. R3 has recently been identified as a new member of the insulin/relaxin family of peptide hormones and is exclusively expressed in the brain neurons. In addition to GPR135, R3 also acts as an agonist for GPR142, a pseudogene in the rat, and can activate LGR7 (leucine repeat-containing G-protein receptor-7), which is the main receptor for relaxin-1 (R1) and relaxin-2 (R2). While R1 and R2 are hormones primarily associated with reproduction and pregnancy, R3 is involved in neuroendocrine and sensory processing. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
AAQALVLLAIFLLSSLGNCAVIGVIVKHRQLRTVTNAFILSLSLSDLLTALLCLPFAFLTLFSRPGWLFG
DRLCLANGFFNACFGIVSTLTMTLISFDRYYAIVRQPQGKIGRRRALQLLAAAWLTALGFSLPWYLLASA
PEYYEKLGFYHCLYVLHSGPSRLGAAYSSVLIVLCYLLPFALMCFCHYNICKTVRLSESRVRPVTTYAHL
LRFYSEMRTATTVLIMIVFIICCWGPYCLLGLVAAAGGYQFPPLMDTVAIWMAWANGAINPLIYAIRNPN
ISMLL
>gnl|CDD|320341 cd15213, 7tmA_PSP24-like, G protein-coupled receptor PSP24 and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes two human orphan receptors, GPR45 and GPR65, and their closely related proteins found in vertebrates and invertebrates. GPR45 and GPR 65 are also called PSP24-alpha (or PSP24-1) and PSP24-beta (or PSP24-2) in other vertebrates, respectively. These receptors exhibit the highest sequence homology to each other. PSP24 was originally identified as a novel, high-affinity lysophosphatidic acid (LPA) receptor in Xenopus laevis oocytes; however, PSP24 receptors (GPR45 and GPR63) have not been shown to be activated by LPA. Instead, sphingosine 1-phosphate and dioleoylphosphatidic acid have been shown to act as low affinity agonists for GPR63. PSP24 receptors are highly expressed in neuronal cells of cerebellum and their expression level remains constant from the early embryonic stages to adulthood, suggesting the important role of PSP24s in brain neuronal functions. Members of this subgroup contain the highly conserved Asp-Arg-Tyr/Phe (DRY/F) motif found in the third transmembrane helix (TM3) of the rhodopsin-like class A receptors which is important for efficient G protein-coupled signal transduction. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
ITLAILMILMIFVGFLGNSIVCLIVYQKPAMRSAINLLLANLAFSDIMLSLVCMPFAAVTIITGRWIFGD
IFCRISAMLYWFFVLEGVAILLIISVDRYLIIVQRQDKLNPHRAKILIAVSWVLSFCVSFPPLVGWGKYE
FPPRAPQCVLGYTESPADRIYVVLLLVAVFFIPFLIMLYSYFCILNTVRSFKTRAFTTILILFIGFSVCW
LPYTVYSLLSVFSRYSSSFYVISTCLLWLSYLKSAFNPVIYCWRIKKFREAC
>gnl|CDD|320342 cd15214, 7tmA_GPR161, orphan G protein-coupled receptor 161, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR161, an orphan GPCR, is a negative regulator of Sonic hedgehog (Shh) signaling, which promotes the processing of zinc finger protein GLI3 into its transcriptional repressor form (GLI3R) during neural tube development. In the absence of Shh, this proteolytic processing is normally mediated by cAMP-dependent protein kinase A (PKA). GPR161 is recruited to primary cilia by a mechanism depends on TULP3 (tubby-related protein 3) and the intraflagellar complex A (IFT-A). Moreover, Gpr161 knockout mice show phenotypes observed in Tulp3/IFT-A mutants, and cause increased Shh signaling in the neural tube. Taken together, GPR161 negatively regulates the PKA-dependent GLI3 processing in the absence of Shh signal by coupling to G(s) protein, which causes activation of adenylate cyclase, elevated cAMP levels, and activation of PKA. Conversely, in the presence of Shh, GPR161 is removed from the cilia by internalization into the endosomal recycling compartment, leading to downregulation of its activity and thereby allowing Shh signaling to proceed. In addition, GPR161 is over-expressed in triple-negative breast cancer (lacking estrogen receptor, progesterone receptor, and human epidermal growth factor receptor 2 (HER2) expression) and correlates with poor prognosis. Mutations of GPR161 have also been implicated as a novel cause for pituitary stalk interruption syndrome (PSIS), a rare congenital disease of the pituitary gland. GPR161 is a member of the class A family of GPCRs, which contains receptors for hormones, neurotransmitters, sensory stimuli, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
TESIAIIIIAILICLGNLVIVVTLYKKSYLLTLSNKFVFSLTLSNLLLSVLVLPFVVTSSIRREWIFGVV
WCNFSALLYLLISSASMLTLGAIAIDRYYAVLYPMVYPMKITGNRAVLALVYIWLHSLIGCLPPLFGWSS
LEFDRFKWMCVAAWHKEAGYTAFWQVWCALLPFVVMLVCYGFIFRVARANQCKAFITILVVLGAFVTTWG
PYMVVISTEALWGKNSVSPQLETLATWLSFTSAVCHPLIYGLWNKTVRKEL
>gnl|CDD|320343 cd15215, 7tmA_GPR101, orphan G protein-coupled receptor 101, member of the class A family of seven-transmembrane G protein-coupled receptors. Gpr101, an orphan GPCR, is predominantly expressed in the brain within discrete nuclei and is predicted to couple to the stimulatory G(s) protein, a potent activator of adenylate cyclase. GPR101 has been implicated in mediating the actions of GnRH-(1-5), a pentapeptide formed by metallopeptidase cleavage of the decapeptide gonadotropin-releasing hormone (GnRH), which plays a critical role in the regulation of the hypothalamic-pituitary-gonadal axis. GnRH-(1-5) acts on GPR101 to stimulate epidermal growth factor (EFG) release and EFG-receptor (EGFR) phosphorylation, leading to enhanced cell migration and invasion in the Ishikawa endometrial cancer cell line. Furthermore, these effects of GnRH-(1-5) are also dependent on enzymatic activation of matrix metallopeptidase-9 (MMP-9). GPR101 is a member of the class A family of GPCRs, which includes receptors for hormones, neurotransmitters, sensory stimuli, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
IRSVLIVIFLCASLFGNIVLLLVFQRKPQLLQVANRFIFNLLVADLLQTVLVMPWVIATSVPLFWPLDSH
LCTALVVLMHLFAFAGVNTIVVVSVDRYLAIIHPLSYPTKMTPRRGYLLIYGTWIVSVLQSTPPLYGWGQ
AAFDERNALCSVIWGSSYSYTILSVVSSFVLPVIIMLACYSMVFRAARRCYHCKAAKVIFIIIFSYVLSM
GPYSFLSVLAVWVDTQVPQWVISIILWLFFLQCCIHPYIYGYMHKSIKKEF
>gnl|CDD|320344 cd15216, 7tmA_SREB1_GPR27, super conserved receptor expressed in brain 1 (or GPR27), member of the class A family of seven-transmembrane G protein-coupled receptors. The SREB (super conserved receptor expressed in brain) subfamily consists of at least three members, named SREB1 (GPR27), SREB2 (GPR85), and SREB3 (GPR173). They are very highly conserved G protein-coupled receptors throughout vertebrate evolution, however no endogenous ligands have yet been identified. SREB2 is greatly expressed in brain regions involved in psychiatric disorders and cognition, such as the hippocampal dentate gyrus. Genetic studies in both humans and mice have shown that SREB2 influences brain size and negatively regulates hippocampal adult neurogenesis and neurogenesis-dependent cognitive function, all of which are suggesting a potential link between SREB2 and schizophrenia. All three SREB genes are highly expressed in differentiated hippocampal neural stem cells. Furthermore, all GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
GLRLATLSLLLCVSLAGNVLFALLIVRERSLHRAPYYLLLDLCLADGLRALACLPAVMLAARRAAAAAGT
PPGALGCKLLAFLAALFCFHAAFLLLGVGVTRYLAIAHHRFYAERLAGWPCAAMLVCAAWALALAAAFPP
VLDGGGADDEDAPCALEQRPDGAPGALGFLLLLAAVVGATHLVYLRLLFFIHDRRKMRPARLVPAVSHDW
TFHGPGATGQAAANWTAGFGRGPTPPALVGIRPAGPGRGARRLLVLEEFKTEKRLCKMFYAITLLFLLLW
GPYVVASYLRVLVRPGAVPQAYLTASVWLTFAQAGINPVVCFLFNRELRDCF
>gnl|CDD|320345 cd15217, 7tmA_SREB3_GPR173, super conserved receptor expressed in brain 3 (or GPR173), member of the class A family of seven-transmembrane G protein-coupled receptors. The SREB (super conserved receptor expressed in brain) subfamily consists of at least three members, named SREB1 (GPR27), SREB2 (GPR85), and SREB3 (GPR173). They are very highly conserved G protein-coupled receptors throughout vertebrate evolution, however no endogenous ligands have yet been identified. SREB2 is greatly expressed in brain regions involved in psychiatric disorders and cognition, such as the hippocampal dentate gyrus. Genetic studies in both humans and mice have shown that SREB2 influences brain size and negatively regulates hippocampal adult neurogenesis and neurogenesis-dependent cognitive function, all of which are suggesting a potential link between SREB2 and schizophrenia. All three SREB genes are highly expressed in differentiated hippocampal neural stem cells. Furthermore, all GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
YVKLVLLGLIICVSLAGNLIVSLLVLKDRALHKAPYYFLLDLCLADTIRSAVCFPFVLVSIRNGSAWTYS
VLSCKIVAFMAVLFCFHAAFMLFCISVTRYMAIAHHRFYSKRMTFWTCIAVICMVWTLSVAMAFPPVFDV
GTYKFIREEDQCIFEHRYFKANDTLGFMLMLAVLIVATHIVYGKLLLFEYRHRKMKPVQMVPAISQNWTF
HGPGATGQAAANWIAGFGRGPMPPTLLGIRQNAHTANRRLLGMEEFKAEKRLGRMFYVITLSFLVLWSPY
IVACYWRVFVKACSIPHRYLSTAVWMSFAQAGVNPIVCFLLNKDLKKCL
>gnl|CDD|320346 cd15218, 7tmA_SREB2_GPR85, super conserved receptor expressed in brain 2 (or GPR85), member of the class A family of seven-transmembrane G protein-coupled receptors. The SREB (super conserved receptor expressed in brain) subfamily consists of at least three members, named SREB1 (GPR27), SREB2 (GPR85), and SREB3 (GPR173). They are very highly conserved G protein-coupled receptors throughout vertebrate evolution, however no endogenous ligands have yet been identified. SREB2 is greatly expressed in brain regions involved in psychiatric disorders and cognition, such as the hippocampal dentate gyrus. Genetic studies in both humans and mice have shown that SREB2 influences brain size and negatively regulates hippocampal adult neurogenesis and neurogenesis-dependent cognitive function, all of which are suggesting a potential link between SREB2 and schizophrenia. All three SREB genes are highly expressed in differentiated hippocampal neural stem cells. Furthermore, all GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
FLKLTSLGFIIGVSVVGNLLISILLVKDKTLHRAPYYFLLDLCCSDILRSAICFPFVFTSVKNGSTWTYG
TLTCKVIAFLGVLSCFHTAFMLFCISVTRYLAIAHHRFYTKRLTFWTCLAVICMVWTLSVAMAFPPVLDV
GTYSFIREEDQCTFQHRSFRANDSLGFMLLLALILLATQLVYLKLIFFVHDRRKMKPVQFVAAVSQNWTF
HGPGASGQAAANWLAGFGRGPTPPTLLGIRQNANTTGRRRLLVLDEFKMEKRISRMFYIMTFLFLTLWGP
YLVACYWRVFARGPVVPGGFLTAAVWMSFAQAGINPFVCIFSNRELRRCF
>gnl|CDD|320347 cd15219, 7tmA_GPR26_GPR78-like, G protein-coupled receptors 26 and 78, member of the class A family of seven-transmembrane G protein-coupled receptors. Orphan G-protein coupled receptor 26 (GPR26) and GPR78 are constitutively active and coupled to increased cAMP formation. They are closely related based on sequence homology and comprise a conserved subgroup within the class A G-protein coupled receptor (GPCR) superfamily. Both receptors are widely expressed in selected tissues of the brain but their endogenous ligands are unknown. GPR26 knockout mice showed increased levels of anxiety- and depression-like behaviors, whereas GPR78 has been implicated in susceptibility to bipolar affective disorder and schizophrenia. Members of this subgroup contain the highly conserved Asp-Arg-Tyr/Phe (DRY/F) motif found in the third transmembrane helix (TM3) of the rhodopsin-like class A receptors which is important for efficient G protein-coupled signal transduction. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
LLAVLLVVVLVVSLLSNLLVLLCFLYSAELRKQVPGIFLLNLSFCNLLLTVLNMPFTLLGVVRNRQPFGD
GFCQAVGFLETFLTSNAMLSMAALSIDRWIAVVFPLSYTSKMRYRDAALMVGYSWLHSLTFSLVALFLSW
LGYSSLYASCTLHLPREEERRRFAVFTAFFHAFTFLLSLLVLCVTYLKVLKVRRRQRATKKISIFIGTFV
LCFAPYVITRLVELLPFVTINRYWGIVSKCLTYSKAASDPFVYSLLRQQYRKVL
>gnl|CDD|410633 cd15220, 7tmA_GPR61_GPR62-like, G protein-coupled receptors 61 and 62, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup includes the orphan receptors GPR61 and GPR62, which are both constitutively active and predominantly expressed in the brain. While GPR61 couples to G(s) subtype of G proteins, the signaling pathway and function of GPR 62 are unknown. GPR61-deficient mice displayed significant hyperphagia and heavier body weight compared to wild-type mice, suggesting that GPR61 is involved in the regulation of food intake and body weight. GPR61 transcript expression was found in the caudate, putamen, and thalamus of human brain, whereas GPR62 transcript expression was found in the basal forebrain, frontal cortex, caudate, putamen, thalamus, and hippocampus. Both receptors share the highest sequence homology with each other and comprise a conserved subgroup within the class A family of GPCRs, which includes receptors for hormones, neurotransmitters, sensory stimuli, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, which then activate the heterotrimeric G proteins. Members of this subgroup contain [A/E]RY motif, a variant of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of the class A GPCRs and important for efficient G protein-coupled signal transduction
VGLFCMVLLDLTALVGNTAVMVVIAKTPHLRKFAFVCHLCVVDLLAALLLMPLGILSSSPFFLGVVFGEA
ECRVYIFLSVCLVSASILTISAISVERYYYIVHPMRYEVKMTIGLVAAVLVGVWVKALLLGLLPVLGWPS
YGGPAPIAARHCSLHWSHSGHRGVFVVLFALVCFLLPLLLILVVYCGVFKVFGGGKAALTLAAIVGQFLC
CWLPYFAFHLYSALAASPVSGGEAEEVVTWLAYSCFAVNPFFYGLLNRQIREEL
>gnl|CDD|320349 cd15221, 7tmA_OR52B-like, olfactory receptor subfamily 52B and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor (OR) subfamilies 52B, 52D, 52H and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
VWISIPFCSMYIVALLGNSLLLFVIVTERSLHEPMYLFLSMLAVTDLLLSTTTVPKMLAIFWFGAGEISF
DGCLTQMFFVHFVFVTESAILLAMAFDRYVAICYPLRYTTILTHSVIGKIGVAAVARSFCIVFPFVFLLK
RLPYCGHNVIPHTYCEHMGIARLACADITVNIWYGLTVALLTVGLDVVLIAVSYALILRAVFRLPSKDAR
LKALSTCGSHVCVILMFYTPAFFSFLTHRFGRHIPRHVHILLANLYVLVPPMLNPIVYGVKTKQI
>gnl|CDD|320350 cd15222, 7tmA_OR51-like, olfactory receptor family 51 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor family 51 and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
HWISIPFCLLYLVALLGNSTILFVIKTEPSLHEPMYYFLSMLAVTDLGLSLSTLPTVLGIFWFNAREISF
DACLAQMFFIHTFSFMESSVLLAMAFDRFVAICNPLRYASILTNSRIAKIGLAIVLRSVLLLLPLPFLLK
RLPFCHSNVLSHSYCLHQDVMKLACSDTRVNSIYGLFVVLSTMGLDSLLILLSYVLILKTVLGIASREER
LKALNTCVSHICAVLIFYVPMIGLSMVHRFGKHASPLVHVLMANVYLLVPPVLNPIIYSVKTKQI
>gnl|CDD|320351 cd15223, 7tmA_OR56-like, olfactory receptor family 56 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor family 56 and related proteins in other mammals, sauropsids, and fishes. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
HWLSLPFLLLYLVALVANSLLLLIIKLERSLHQPMYILLGILAAVDIVLATTILPKMLAIFWFDANTISL
PGCFAQMFFIHFFTAMESSILLVMALDRYVAICKPLRYPSIITKSFILKLVLFALIRSGLLVLPIVVLAS
QLSYCSSNVIEHCYCDHMALVSLACGDTTINSIYGLAVAWLIVGSDIILIFFSYALILRAVLRLASGEAR
SKALNTCGSHLIVILFFYTAVLVSSLTYRFGKTIPPDVHVLLSVLYILIPPALNPIIYGVRTKEIRQGF
>gnl|CDD|320352 cd15224, 7tmA_OR6B-like, olfactory receptor subfamily 6B and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor 6B, 6A, 6Y, 6P, and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
LLLFLLFLIAYVLTLLENLLIILTIWLNSQLHKPMYFFLSNLSFLEIWYISVTVPKLLAGFLSQNKSISF
VGCMTQLYFFLSLACTECVLLAVMAYDRYVAICHPLRYPVIMTHQLCVQLAAGSWLSGFLISMIKVYFIS
QLSFCGPNVINHFFCDISPLLNLSCTDMSLAELVDFILALIILLVPLLVTVASYICIISTVLRIPSATGR
QKAFSTCASHLTVVIIFYSATLFMYARPKAISSFDSNKLVSVLYTVVTPLLNPIIYCLRN
>gnl|CDD|320353 cd15225, 7tmA_OR10A-like, olfactory receptor subfamily 10A and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor 10A, 10C, 10H, 10J, 10V, 10R, 10J, 10W, among others, and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
LLLFVVFLLIYLVTLLGNLLIILITKVDPALHTPMYFFLRNLSFLEICYTSVIVPKMLVNLLSEDKTISF
LGCATQMFFFLFLGGTECFLLAAMAYDRYVAICNPLRYTLIMNRRVCLQLVAGSWLSGILVSLGQTTLIF
SLPFCGSNEINHFFCDIPPVLKLACADTSLNEIAIFVASVLVILVPFLLILVSYIFIISTILKIPSAEGR
RKAFSTCSSHLIVVTLFYGCASFTYLRPKSSYSPETDKLLSLFYTVVTPMLNPIIYSLRNKEVKGAL
>gnl|CDD|320354 cd15226, 7tmA_OR4-like, olfactory receptor family 4 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor family 4 and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
LFLFVFFSLFYVATVLGNLLIVVTVTSDPHLHSPMYFLLANLSFIDLCLSSFATPKMICDLLREHKTISF
GGCMAQIFFLHFFGGSEMVLLIAMAFDRYVAICKPLHYLTIMSPRMCILLVVASWIIGFIHSLSQLAFVV
NLPFCGPNVVDSFFCDLPLVIKLACTDTYVLELMVVANSGLISLVCFLLLLISYIVILVTVRKHSSGGSS
KALSTCSAHITVVVLFFGPCIFIYVWPFSTFPVDKFLAVFYTVITPLLNPIIYTLRN
>gnl|CDD|320355 cd15227, 7tmA_OR14-like, olfactory receptor family 14 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor family 14 and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
ILHFVLFLLIYLAALTGNLLIITVVTLDHHLHTPMYFFLKNLSFLDLCYISVTVPKSIANSLTNTRSISF
LGCVAQVFLFIFFAASELALLTVMAYDRYVAICHPLHYEVIMNRGACVQMAAASWLSGLLYGALHTANTF
SLPFCGSNVIHQFFCDIPQLLKLSCSDTYLNEIGVLVLSVCLGLGCFVFIIVSYVHIFSTVLRIPSAQGR
SKAFSTCLPHLIVVSLFLSTGSFAYLKPPSDSPSLLDLLLSVFYSVVPPTLNPIIYSLRN
>gnl|CDD|320356 cd15228, 7tmA_OR10D-like, olfactory receptor subfamily 10D and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 10D and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
TILFVLFLAFYLCTLLGNLLILSAILSDPRLHTPMYFFLCNLSVFDIGFSSVSTPKMLAYLWGQSRVISL
GGCMSQVFFYHFLGSTECLLYTVMAYDRYVAICHPLRYLLIMNRRVCALLAAGTWITSSFHATILTSLTF
TLPYCGSNVVDYFFCDIFPVLKLACADTSIAETVSFTNVGLVPLTCFLLILASYVRIVISILKMRSAEGR
RKAFSTCSSHLTVVTLFFGPCALIYTQPTPSPVLVTPVQIFNNVVTPMLNPLIYTLRNKEVKAAL
>gnl|CDD|320357 cd15229, 7tmA_OR8S1-like, olfactory receptor subfamily 8S1 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor 8S1 and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
IFLFLVFLVIYLLTLLGNLLIMLVIRADSHLHTPMYFFLSHLSFLDICYSSVTVPKMLENLLSERKTISV
EGCIAQIFFFFFFAGTEAFLLSAMAYDRYAAICHPLHYVQIMSKQVCVQLVGGAWALGFLYALINTLLLL
NLHFCGPNEINHFSCELPSLLPLSCSDTFANKMVLLTSSVIFGLGSFLLTLVSYIHIISTILRIRSAEGR
SKAFSTCSSHLTVVGLFYGTGFFRYLRPNSASSSVLDRVFSIQYSILTPMLNPIIYSLKNKEVKAAL
>gnl|CDD|320358 cd15230, 7tmA_OR5-like, olfactory receptor family 5 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor family 5, some subfamilies from families 8 and 9, and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
VPLFVLFLLIYLITLVGNLGMIVLIRIDSRLHTPMYFFLSNLSFVDICYSSVITPKMLVNFLSEKKTISF
AGCAAQFFFFAVFGTTECFLLAAMAYDRYVAICNPLLYTVIMSKRVCIQLVAGSYLCGFVNSIVHTSSTF
SLSFCGSNVINHFFCDIPPLLKLSCSDTHINELVLFAFSGFIGLSTLLIILISYLYILITILRIRSAEGR
RKAFSTCASHLTAVSLFYGTLIFMYLRPSSSYSLDQDKVVSVFYTVVIPMLNPLIYSLRN
>gnl|CDD|320359 cd15231, 7tmA_OR5V1-like, olfactory receptor subfamily 5V1 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 5V1 and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
LLLFLIFLIIYLVTLLGNLLIITLVLLDSHLHTPMYFFLSNLSFLDICYTSVTVPKMLVNLLRERKTISY
IGCLAQLFFFVSFVGTECLLLAVMAYDRYVAICNPLHYAVIMSRKVCLQLAAASWLCGFLNSAVHTVLTF
RLSFCGSNQISHFFCDIPPLLKLSCSDTSLNEVLLLVASVFIGLTPFLFIVISYVYIISTILKIRSAEGR
RKAFSTCASHLTVVTLFYGTAIFNYNRPSSGYSLDKDTLISVLYSIVTPMLNPIIYSLRNKEVKGAL
>gnl|CDD|320360 cd15232, 7tmA_OR13-like, olfactory receptor family 13 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor family 13 (subfamilies 13A1 and 13G1) and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
VLLFWLFLFLYAAALTGNSLIILAISTSPKLHTPMYFFLVNLSLVDIICTSTVVPKLLQNLLTERKTISF
GGCMAQLYFFTWSLGSELLLLTAMAYDRYVAICHPLHYSTIMRKEVCVGLATGVWAIGMLNSAVHTGLML
RLSFCGPNIINHFFCEIPPLLLLSCSDTSLNEIMAFVADVFFGVGNFLLTLTSYGFIIRSILRIRSTEGK
KKAFSTCSSHLIVVSLYYSTVIYTYIRPSSSYSPEKDKVVAVLYSVVTPTLNPLIYSLRN
>gnl|CDD|320361 cd15233, 7tmA_OR3A-like, olfactory receptor subfamily 3A3 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 3A3 and 3A4, and related proteins in other mammals. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
PVLFVTFLLAYIVTIGGNLSILAAILLEPKLHTPMYFFLGNLSLLDIGCISVTVPQMLVHLLSHKRTISY
AACLSQLFFFHLLAGADCFLLTAMAYDRYLAICQPLTYSVRMSWRVQTALVGISCACAFTNALTHTVAMS
TLKFCGPNVINHFFCDLPPLFQLSCSSTHLNELLLFVFAFFMALAPCVLIVVSYAHVVAAVLRIRSAEGR
RKAFSTCGSHLTVVCIFYGTGVFSYMRLGSVYSSDKDKVIGILNTVLSPMLNPLIYSLRNKDVKGAL
>gnl|CDD|320362 cd15234, 7tmA_OR7-like, olfactory receptor family 7 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor family 7 and related proteins in other mammals. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
PLLFGLFLSMYLVTVLGNLLIILAVSSDSHLHTPMYFFLSNLSFADICFSSTTVPKMLVNIQTQSKSISY
TGCLTQMCFFLLFGGLDNFLLAVMAYDRYVAICHPLHYTVIMNPCLCGLLVLLSLLISILDSLLHSLMVL
QLSFCTDVEIPHFFCELAQVLKLACSDTLINNILIYLATVIFGGIPLSGIIFSYYKIVSSILRIPSSGGK
YKAFSTCGSHLSVVSLFYGTGLGVYISSAVTHSSRKTAVASVMYTVVTPMLNPFIYSLRNKDMKGAL
>gnl|CDD|320363 cd15235, 7tmA_OR1A-like, olfactory receptor subfamily 1A and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 1A, 1B, 1K, 1L, 1Q and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
QPLLFLLFLAMYLLTLLGNLLIVLLIRSDPRLHTPMYFFLSHLSLVDICFTSTTVPKMLANLLSGSKTIS
YAGCLAQMYFFIAFGNTDSFLLAVMAYDRYVAICHPLHYATVMSPKRCLLLVAGSWLLSHLHSLLHTLLM
SRLSFCGSNEIPHFFCDLQPLLKLSCSDTSLNELLIFTEGAVVVLGPFLLIVLSYARILAAVLKVPSAAG
RRKAFSTCGSHLTVVALFYGTIIGVYFQPSSSYSADKDRVATVMYTVVTPMLNPFIYSLRNKDVKGAL
>gnl|CDD|320364 cd15236, 7tmA_OR1E-like, olfactory receptor subfamily 1E and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 1E, 1J, and related proteins in other mammals. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
GVFFALFLAMYLTTVLGNLLIILLIRLDSHLHTPMYFFLSHLAFTDVSFSSVTVPKMLMNMQTQDQSIPY
AGCISQMYFFIFFGCLDSFLLAVMAYDRYVAICHPLHYTAIMRPELCVLLVAGSWVLTCFHALLHTLLLA
RLSFCADNVIPHFFCDLVALLKLSCSSTSLNELVIFTEGGLLFVLPLLLILGSYIRIAATILKVPSTKGI
CKAFSTCGSHLSVVFLYYGTIIGVYFFPSSNNSSDKDIVASVMYTVVTPMLNPFIYSLRNRDIKGAL
>gnl|CDD|320365 cd15237, 7tmA_OR2-like, olfactory receptor family 2 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor families 2 and 13, and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
ILLFILFLLIYLLTLLGNGLIILLIWLDSRLHTPMYFFLSNLSLLDICYTTSTVPQMLVHLLSEHKTISF
VGCAAQMFFFLALGVTECVLLAVMAYDRYVAICNPLRYSVIMSRRVCVRLAATSWASGFLNSLVLTSLTL
RLPFCGPNHINHFFCEAPAVLKLACADTSLNEAVIFVTSVLVLLIPFSLILASYIRILATILRIQSAEGR
KKAFSTCASHLTVVTLFYGTAIFMYMRPHSTHSPDQDKMISVFYTIVTPMLNPLIYSLRN
>gnl|CDD|320366 cd15238, 7tm_ARII-like, Acetabularia rhodopsin II and similar proteins, member of the seven-transmembrane GPCR superfamily. This subgroup includes the eukaryotic light-driven proton-pumping Acetabularia rhodopsin II from the giant unicellular marine alga Acetabularis acetabulum, as well as its closely related proteins. They belong to the microbial rhodopsin family, also known as type I rhodopsins, comprising the light-driven inward chloride pump halorhodopsin (HR), the outward proton pump bacteriorhodopsin (BR), the light-gated cation channel channelrhodopsin (ChR), the light-sensor activating transmembrane transducer protein sensory rhodopsin II (SRII), and the other light-driven proton pumps such as blue-light absorbing and green-light absorbing proteorhodopsins, among others. Microbial rhodopsins have been found in various single-celled microorganisms from all three domains of life, including halophile archaea, gamma-proteobacteria, cyanobacteria, fungi, and green algae. While microbial (type 1) and animal (type 2) rhodopsins have no sequence similarity with each other, they share a common architecture consisting of seven-transmembrane alpha-helices (TM) connected by extracellular loops and intracellular loops. Both types of rhodopsins consist of opsin and a covalently attached retinal (the aldehyde of vitamin A), a photoreactive chromophore, via a protonated Schiff base linkage to an amino group of lysine in the middle of the seventh transmembrane helix (TM7). Upon the absorption of light, microbial rhodopsins undergo light-induced photoisomerization of all-trans retinal into the 13-cis isomer, whereas the photoisomerization of 11-cis retinal to all-trans isomer occurs in the animal rhodopsins. While animal visual rhodopsins are activated by light to catalyze GDP/GTP exchange in the alpha subunit of the retinal G protein transducin (Gt), microbial rhodopsins do not activate G proteins, but instead can function as light-dependent ion pumps, cation channels, and sensors
EGGLVAQWVVFALMAFAAIAFAVAVFFRPLNLRSHYYINIAICTIAATAYYAMAVNGGDALVSNPDGNER
QVYYARYIDWVFTTPLLLLDLILLTGMPIGMILWIVGADIAMIMFGIFGAFSTNSYKWGYFGVGCAMFAV
LLWGMFNPGAKGALAKGGEYPGLYFGLLGYLALLWVGYPIVWGLGEGSDYISVDAEAISMGILDILAKPL
FGWGVLISH
>gnl|CDD|320367 cd15239, 7tm_YRO2_fungal-like, fungal YRO2 and related proteins, member of the seven-transmembrane GPCR superfamily. This subgroup includes the yeast YRO2 protein and it closely related proteins. Although the exact function of these proteins is unknown, they show strong sequence homology to the family of microbial rhodopsins, also known as type I rhodopsins, comprising the light-driven inward chloride pump halorhodopsin (HR), the outward proton pump bacteriorhodopsin (BR), the light-gated cation channel channelrhodopsin (ChR), the light-sensor activating transmembrane transducer protein sensory rhodopsin II (SRII), and the other light-driven proton pumps such as blue-light absorbing and green-light absorbing proteorhodopsins, among others. Microbial rhodopsins have been found in various single-celled microorganisms from all three domains of life, including halophile archaea, gamma-proteobacteria, cyanobacteria, fungi, and green algae. While microbial (type 1) and animal (type 2) rhodopsins have no sequence similarity with each other, they share a common architecture consisting of seven-transmembrane alpha-helices (TM) connected by extracellular loops and intracellular loops. Both types of rhodopsins consist of opsin and a covalently attached retinal (the aldehyde of vitamin A), a photoreactive chromophore, via a protonated Schiff base linkage to an amino group of lysine in the middle of the seventh transmembrane helix (TM7). Upon the absorption of light, microbial rhodopsins undergo light-induced photoisomerization of all-trans retinal into the 13-cis isomer, whereas the photoisomerization of 11-cis retinal to all-trans isomer occurs in the animal rhodopsins. While animal visual rhodopsins are activated by light to catalyze GDP/GTP exchange in the alpha subunit of the retinal G protein transducin (Gt), microbial rhodopsins do not activate G proteins, but instead can function as light-dependent ion pumps, cation channels, and sensors
THGSDWLWAVFAVFGLSALVFLALSFRAPRGERIFHYLPIAILLVAAIAYFTMASNLGWTPIQAEFNHST
QGEHPGTRQIFYARYIGWFLAFPLLLLALLLTSGVPWSTILFNIFLTEVWVVSLLVGALVHSTYKWGYFT
FGCVALLYVAYSLLTRGRRSARRLGLDVRRFYLILAGWLMLIWLLYPIAWGLSEGGNVIQPDSEAIFYGI
LDLLAFPVFPFALLFLA
>gnl|CDD|320368 cd15240, 7tm_ASR-like, Anabaena sensory rhodopsin and similar proteins, member of the seven-transmembrane GPCR superfamily. This subgroup includes eubacterial sensory rhodopsin from the freshwater cyanobacterium Anabaena and its closely related proteins. Unlike other sensory rhodopsins (SRI and SRII), the Anabaena sensory rhodopsin (ASR) activates a soluble transducer protein (ASRT), which may leading to transcriptional control of several genes. Although ASRT was shown to interact with DNA in vitro, the exact mechanism of photosensory transduction is not clearly understood. Moreover, the regulation of CRP (cAMP receptor protein) expression by ASR has been reported demonstrating a direct interaction of the C-terminal region of ASR with DNA, suggesting that ASR itself may also work as a transcription factor. ASR belongs to the microbial rhodopsin family, also known as type I rhodopsins, comprising the light-driven inward chloride pump halorhodopsin (HR), the outward proton pump bacteriorhodopsin (BR), the light-gated cation channel channelrhodopsin (ChR), the light-sensor activating transmembrane transducer protein sensory rhodopsin II (SRII), and the other light-driven proton pumps such as blue-light absorbing and green-light absorbing proteorhodopsins, among others. Microbial rhodopsins have been found in various single-celled microorganisms from all three domains of life, including halophile archaea, gamma-proteobacteria, cyanobacteria, fungi, and green algae. While microbial (type 1) and animal (type 2) rhodopsins have no sequence similarity with each other, they share a common architecture consisting of seven-transmembrane alpha-helices (TM) connected by extracellular loops and intracellular loops. Both types of rhodopsins consist of opsin and a covalently attached retinal (the aldehyde of vitamin A), a photoreactive chromophore, via a protonated Schiff base linkage to an amino group of lysine in the middle of the seventh transmembrane helix (TM7). Upon the absorption of light, microbial rhodopsins undergo light-induced photoisomerization of all-trans retinal into the 13-cis isomer, whereas the photoisomerization of 11-cis retinal to all-trans isomer occurs in the animal rhodopsins. While animal visual rhodopsins are activated by light to catalyze GDP/GTP exchange in the alpha subunit of the retinal G protein transducin (Gt), microbial rhodopsins do not activate G proteins, but instead can function as light-dependent ion pumps, cation channels, and sensors
NTEQTWLWIGFAGMAIGALVILFLAKRRTPVEEYDGLVHGIVPIIAALAYLAMAIGQGKIELDAGQIFYF
ARYIDWTFTTPLLLLGLAWTAMHSGRKPGTVIGFLMSDQIMIVTALLFGLSSERAWVKWTWYACSCGAFL
GVLYGIWVPLREETRTERSDLANAYRKNVAFLTVVWIIYPIVLIVGPDGLGWISPTLDTALFAVLDFFAK
VVFGFLALHEL
>gnl|CDD|320369 cd15241, 7tm_ChRs, channelrhodopsins, member of the seven-transmembrane GPCR superfamily. Channelrhodopsins (ChRs) are light-gated ion channels acting as sensory photoreceptors in unicellular green algae, controlling phototaxis (directional movement toward or away from light). ChRs are large seven-transmembrane proteins with large C-terminal extensions, which have been implicated in localizing the channel to the algal eyespot, a single layer of pigmented granules, overlaying part of the plasma membrane but are not required for ion channel function. ChRs are belongs to the microbial rhodopsin family, also known as type I rhodopsins, comprising the light-driven inward chloride pump halorhodopsin (HR), the outward proton pump bacteriorhodopsin (BR), the light-sensor activating transmembrane transducer protein sensory rhodopsin II (SRII), the light-sensor activating soluble transducer protein Anabaena sensory rhodopsin (ASR), and the other light-driven proton pumps such as blue-light absorbing and green-light absorbing proteorhodopsins, among others. Microbial rhodopsins have been found in various single-celled microorganisms from all three domains of life, including halophile archaea, gamma-proteobacteria, cyanobacteria, fungi, and green algae. While microbial (type 1) and animal (type 2) rhodopsins have no sequence similarity with each other, they share a common architecture consisting of seven-transmembrane alpha-helices (TM) connected by extracellular loops and intracellular loops. Both types of rhodopsins consist of opsin and a covalently attached retinal (the aldehyde of vitamin A), a photoreactive chromophore, via a protonated Schiff base linkage to an amino group of lysine in the middle of the seventh transmembrane helix (TM7). Upon the absorption of light, microbial rhodopsins undergo light-induced photoisomerization of all-trans retinal into the 13-cis isomer, whereas the photoisomerization of 11-cis retinal to all-trans isomer occurs in the animal rhodopsins. While animal visual rhodopsins are activated by light to catalyze GDP/GTP exchange in the alpha subunit of the retinal G protein transducin (Gt), microbial rhodopsins do not activate G proteins, but instead can function as light-dependent ion pumps, cation channels, and sensors
KAARGCQWFAFALSVLFLLFYAYATWKATCGWEEVYVCTIELIKVCIEIFHEFDSPATLYLSTGNFVLWL
RYAEWLLTCPVILIHLSNLTGLKDDYSKRTMGLLVSDIGTIVFGVTAALSTGYLKIIFFFIGLCYGAYTF
FHAAKVYIESYHTVPKGICRKLVRAMAWVYFVSWSMFPILFILGPEGFGHISAYGSTIGHTIADLLSKNL
WGLLGHFLR
>gnl|CDD|320370 cd15242, 7tm_Proteorhodopsin, green- and blue-light absorbing proteorhodopsins, member of the seven-transmembrane GPCR superfamily. This subgroup represents blue-light absorbing and green-light absorbing proteorhodopsins (PRs), which act as a light-driven proton pump that plays a major role in supplying light energy for phototropic marine microorganisms, by a mechanism similar to that of bacteriorhodopsin. PRs are found in most marine bacteria in surface waters, as well as in archaea and eukaryotes. They belong to the microbial rhodopsin family, also known as type 1 rhodopsins, comprising the light-driven inward chloride pump halorhodopsin (HR), the light-gated cation channel channelrhodopsin (ChR), the light-sensor activating transmembrane transducer protein sensory rhodopsin II (SRII), the light-sensor activating soluble transducer protein Anabaena sensory rhodopsin (ASR), and the other light-driven proton pumps such as bacteriorhodopsin (BR). They have been found in various single-celled microorganisms from all three domains of life, including halophile archaea, gamma-proteobacteria, cyanobacteria, fungi, and green algae. While microbial (type 1) and animal (type 2) rhodopsins have no sequence similarity with each other, they share a common architecture consisting of seven-transmembrane alpha-helices (TM) connected by extracellular loops and intracellular loops. Both types of rhodopsins consist of opsin and a covalently attached retinal (the aldehyde of vitamin A), a photoreactive chromophore, via a protonated Schiff base linkage to an amino group of lysine in the middle of the seventh transmembrane helix (TM7). Upon the absorption of light, microbial rhodopsins undergo light-induced photoisomerization of all-trans retinal into the 13-cis isomer, whereas the photoisomerization of 11-cis retinal to all-trans isomer occurs in the animal rhodopsins. While animal visual rhodopsins are activated by light to catalyze GDP/GTP exchange in the alpha subunit of the retinal G protein transducin (Gt), microbial rhodopsins do not activate G proteins, but instead can function as light-dependent ion pumps, cation channels, and sensors
DLVYNSFSFGIAAMLAATLFFFLERSQVAPKYRTALTVSGLVTFIAAYHYFRMFDSWVDAYTLVDGVVPT
GGPFNTAYRYVDWLLTVPLLLIEFYLVLALAGAETSSLLWRLGGASALMIVLGYPGEIGADLGTRWLWGV
LSMIPFLYIIYELFVGLAKAIARQPAAVRGAVNTLRWIVLVGWAIYPIGYMAGYLGLTGGGAQVAVQVGY
NIADIVNKAGFGLLIYAIA
>gnl|CDD|320371 cd15243, 7tm_Halorhodopsin, light-driven inward chloride pump halorhodopsin, member of the seven-transmembrane GPCR superfamily. Halorhodopsin (HR) acts as a light-driven inward-directed chloride pump. When activated by yellow light, HR pumps chloride ions into the cell cytoplasm, generating a negative-inside membrane potential which drives proton uptake. The resulting electrochemical ion gradient provides an energy source to the cell and contributes to pH homeostasis. HR is found in phylogenetically ancient archaea, known as halobacteria which live in high salty environments. HR belongs to the microbial rhodopsin family, also known as type I rhodopsins, comprising light-driven retinal-binding outward pump bacteriorhodopsin (BR), light-gated cation channel channelrhodopsin (ChR), light-sensor activating transmembrane transducer protein sensory rhodopsin II (SRII), light-sensor activating soluble transducer protein Anabaena sensory rhodopsin (ASR), and other light-driven proton pumps such as blue-light absorbing and green-light absorbing proteorhodopsins, among others. They have been found in various single-celled microorganisms from all three domains of life, including halophile archaea, gamma-proteobacteria, cyanobacteria, fungi, and green algae. While microbial (type 1) and animal (type 2) rhodopsins have no sequence similarity with each other, they share a common architecture consisting of seven-transmembrane alpha-helices (TM) connected by extracellular loops and intracellular loops. Both types of rhodopsins consist of opsin and a covalently attached retinal (the aldehyde of vitamin A), a photoreactive chromophore, via a protonated Schiff base linkage to an amino group of lysine in the middle of the seventh transmembrane helix (TM7). Upon the absorption of light, microbial rhodopsins undergo light-induced photoisomerization of all-trans retinal into the 13-cis isomer, whereas the photoisomerization of 11-cis retinal to all-trans isomer occurs in the animal rhodopsins. While animal visual rhodopsins are activated by light to catalyze GDP/GTP exchange in the alpha subunit of the retinal G protein transducin (Gt), microbial rhodopsins do not activate G proteins, but instead can function as light-dependent ion pumps, cation channels, and sensors
ALLASSLWVNIALAGLTILVFVYMGRGIEDPRAKLIWVATLMIPLVSISSYTGLASGLTVSFLEMPAGHA
LAGQEVLSMWGRYLTWALSTPMILLALGLLAGSNTTKLFTAIAADIGMCVTGLAAALTTSSHLMRWVWYA
ISCAFFVVVLYVLLVEWAADADAAGTADIFSTLKVLTVVLWLGYPIVWALGVEGLALLSVGATSWAYSGL
DIFAKYVFAFLLLRWV
>gnl|CDD|320372 cd15244, 7tm_bacteriorhodopsin, light-driven outward proton pump bacteriorhodopsin, member of the seven-transmembrane GPCR superfamily. Bacteriorhodopsin (BR) serves as a light-driven retinal-binding outward proton pump, generating an outside positive membrane potential and thus creating an inwardly directed proton motive force (PMF) necessary for ATP synthesis. BR belongs to the microbial rhodopsin family, also known as type I rhodopsins, comprising light-driven inward chloride pump halorhodopsin (HR), light-gated cation channel channelrhodopsin (ChR), light-sensor activating transmembrane transducer protein sensory rhodopsin II (SRII), light-sensor activating soluble transducer protein Anabaena sensory rhodopsin (ASR), and other light-driven proton pumps such as blue-light absorbing and green-light absorbing proteorhodopsins, among others. They have been found in various single-celled microorganisms from all three domains of life, including halophile archaea, gamma-proteobacteria, cyanobacteria, fungi, and green algae. While microbial (type 1) and animal (type 2) rhodopsins have no sequence similarity with each other, they share a common architecture consisting of seven-transmembrane alpha-helices (TM) connected by extracellular loops and intracellular loops. Both types of rhodopsins consist of opsin and a covalently attached retinal (the aldehyde of vitamin A), a photoreactive chromophore, via a protonated Schiff base linkage to an amino group of lysine in the middle of the seventh transmembrane helix (TM7). Upon the absorption of light, microbial rhodopsins undergo light-induced photoisomerization of all-trans retinal into the 13-cis isomer, whereas the photoisomerization of 11-cis retinal to all-trans isomer occurs in the animal rhodopsins. While animal visual rhodopsins are activated by light to catalyze GDP/GTP exchange in the alpha subunit of the retinal G protein transducin (Gt), microbial rhodopsins do not activate G proteins, but instead can function as light-dependent ion pumps, cation channels, and sensors
GPEWIWLWIGTALMGLGTLYFLVRGWGVSDPEAQEFYIITTLITAIAAAAYLSMATGYGLTEVPLGGEGR
DIYWARYADWLFTTPLLLLDLALLAGADRNTIATLIGLDVIMIVTGLVAALTKVPAARIVWWAISTAAFL
AVLYFLVVGLTAEASSRSPEVASTFNTLRNLTLVLWACYPIVWLIGTEGFGIVGLNIETLLFMVLDLTAK
VGFGFILLRSR
>gnl|CDD|320373 cd15245, 7tmF_FZD2, class F frizzled subfamily 2, member of 7-transmembrane G protein-coupled receptors. This group includes subfamily 2 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of G-protein coupled receptors. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
MFFSQDEIRFARIWILIWSVLCCASTFFTVTTYLVDMQRFRYPERPIIFLSGCYTMVSVAYIAGFVLGDK
VVCNERFSEDGYKTVVQGTKKEGCTILFMMLYFFSMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFH
LAAWAVPAVKTITILAMGQIDGDLLSGVCFVGLNNIDPLRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRT
IMKHDGTKTEKLERLMVRIGVFSVLYTVPATIVIACYFYEQAFRQHWERSWISQNCKSLAIPCPLQYTPR
MTPDFTVYMIKYLMTLIVGITSGFWIWSGKTLHSWRKFYTRLTNSRQGET
>gnl|CDD|320374 cd15246, 7tmF_FZD7, class F frizzled subfamily 7, member of 7-transmembrane G protein-coupled receptors. This group includes subfamily 7 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of G-protein coupled receptors. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
MYFKEEEVRFARLWVGIWSILCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAYAAGFLLEDR
VVCVERFSDDGYRTVAQGTKKEGCTILFMVLYFFGMASSIWWVILSLTWFLSAGMKWGHEAIEANSQYFH
LAAWAVPAVKTITILAMGQVDGDLLSGVCYVGIYSVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRT
IMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVLACYFYEQAFRETWEKTWLLQTCKRYAVPCPNNNFAP
MSPDFTVFMIKYLMTMIVGITSGFWIWSGKTLQSWRRFYHRLSNGSKGETA
>gnl|CDD|320375 cd15247, 7tmF_FZD1, class F mammalian frizzled subfamily 1, member of 7-transmembrane G protein-coupled receptors. This group includes subfamily 1 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of G-protein coupled receptors. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
PCEPGRVHGLMYFGPEELRFARIWIGIWSVLCCASTLFTVLTYLVDMKRFSYPERPIIFLSGCYTMVAIA
YIAGFLLEDKVVCNDKFAEDGIKTVAQGTKKEGCTILFMMLYFFSMASSIWWVILSLTWFLAAGMKWGHE
AIEANSQYFHLAAWAVPAIKTITILAVGQVDGDVLSGVCFVGINNVDALRGFVLAPLFVYLFIGTSFLLA
GFVSLFRIRTIMKHDGTKTEKLEKLMVRIGIFSVLYTVPATIVIACYFYEQAFREQWERSWISQSCKTYA
IPCPAHSHPPMSPDFTVFMIKYLMTLIVGITSGFWIWSGKTLNSWRKFYTRLTNSKQGETT
>gnl|CDD|320376 cd15248, 7tmF_FZD1_insect, class F insect frizzled subfamily 1, member of 7-transmembrane G protein-coupled receptors. This group includes subfamily 1 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of G-protein coupled receptors, found in insects such as Drosophila melanogaster. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
MFFPERERTFSRYWIGSWAAVCMASCLFTVLTFLIDSSRFRYPERPIVFLSVCYLMVAAAYVAGLGAGDS
VSCNEPFPPPVKLGRLQMVSTITQGTKTESCTVLFMVLYFFSMAASIWWVVLTLTWFLAAGLKWGHEAIE
AKSHYFHLVAWAVPALKTISILAMGKVEGDVLSGVCYVGLWDMHALRGFVLAPLCVYLSLGTIFLLAGFI
SLFRIRTVMKHDGTKTDKLEKLMLRIGIFSFLYTLPALIVLACLFYEQAHFDSWMLQWHRDICKPPSWSI
PACRATGSPEARPEFQVFMIKYLMSMIVGITSSVWIWSSKTLVSWRNFYERL
>gnl|CDD|320377 cd15249, 7tmF_FZD5, class F frizzled subfamily 5, member of 7-transmembrane G protein-coupled receptors. This group includes subfamily 5 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of GPCRs, and its closely related proteins. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
PYFSQDERTFATFWIGLWSVLCFISTFTTVATFLIDMERFRYPERPIIFLSACYLFVSLGYIVRLVVGHE
SVACNREHNHIHYETTGPALCTIVFLLIYFFGMASSIWWVILSFTWFLAAGMKWGNEAIAGYSQYFHLAA
WLIPSVKSIAVLALSSVDGDPVAGICYVGNQNLNNLRGFVLAPLVVYLFTGTLFLLAGFVSLFRIRSVIK
QGGTKTDKLEKLMIRIGIFTVLYTVPATIVVACYVYEQHYRESWEAALNCSCPGDDTQPRARPDYAVFML
KYFMCLVVGITSGVWIWSGKTLESWRRFTG
>gnl|CDD|320378 cd15250, 7tmF_FZD8, class F frizzled subfamily 8, member of 7-transmembrane G protein-coupled receptors. This group includes subfamily 8 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of GPCRs, and its closely related proteins. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
PYFSQEERTFTAFWIGLWSVLCFLSTFATVSTFLIDMERFKYPERPIIFLSACYLFVSLGYLVRLIAGHE
KVACSRGALAEVEHIHYETTGPALCTVVFLLIYFFGMASSIWWVILSLTWFLAAGMKWGNEAIAGYSQYF
HLAAWLIPSVKSIAVLALSSVDGDPVAGICYVGNQNLDNLRGFVLAPLVIYLFIGTMFLLAGFVSLFRIR
SVIKQGGTKTDKLEKLMIRIGIFTVLYTVPATIVVACYFYEQHNRQRWEITHNCNCLRDQPDQARRPDYA
VFMLKYFMCLVVGITSGVWTWSGKTLESWRALCT
>gnl|CDD|320379 cd15251, 7tmB2_BAI_Adhesion_VII, brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors. Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediate direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions
AGSPSVTLIVGCGVSCLALLTLLAIYAAFWRYIRSERSIILINFCLSIISSNILILVGQTQTLNKGVCTM
TAAFLHFFFLSSFCWVLTEAWQSYMAVTGRMRTRLIRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYC
WLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSRDGISDNAMASLWSSCVVLPLLALTWMSAVLAMT
DRRSVLFQILFAVFDSLQGFVIVMVHCILRREVQDAVKCRMGV
>gnl|CDD|320380 cd15252, 7tmB2_Latrophilin_Adhesion_I, Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors. Group I adhesion GPCRs consist of latrophilins (also called lectomedins or latrotoxin receptors) and ETL (EGF-TM7-latrophilin-related protein. These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
YNILTRITQVGIIISLVCLAICIFTFWFFRGLQSDRTTIHKNLCISLFLAELVFLIGINTTTNKIFCSVI
AGLLHYFFLAAFAWMFIEGIQLYLMLVEVFENEGSRHKNFYIFGYGSPAVIVGVSAALGYRYYGTTKVCW
LSTENYFIWSFIGPATLIILLNLIFLGVAIYKMFRHTAGLKPEVSCLENIRSWARGAIALLFLLGLTWIF
GVLHINHASVVMAYLFTVSNSLQGMFIFLFHCVLSRKVRKEYYKLFR
>gnl|CDD|320381 cd15253, 7tmB2_GPR113, orphan adhesion receptor GPR113, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR113 is an orphan receptor that belongs to group VI adhesion-GPCRs along with GPR110, GPR111, GPR115, and GPR116. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR113 contains a hormone binding domain and one EGF (epidermal grown factor) domain, and is primarily expressed in a subset of taste receptor cells. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS
SFWLDFLSQVGLGASILALLLCLGIYRLVWRSVVRNKISYFRHMTLVNIAFSLLLADTCFLGATFLSAGH
ESPLCLAAAFLCHFFYLATFFWMLVQALMLFHQLLFVFHQLAKRSVLPLMVTLGYLCPLLIAAATVAYYY
PKRQYLHEGACWLNGESGAIYAFSIPVLAIVLVNLLVLFVVLMKLMRPSVSEGPPPEERKALLSIFKALL
VLTPVFGLTWGLGVATLTGESSQVSHYGFAILNAFQGVFILLFGCLMDKKVREALLKRLCK
>gnl|CDD|320382 cd15254, 7tmB2_GPR116_Ig-Hepta, The immunoglobulin-repeat-containing receptor Ig-hepta/GPR116, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR116 (also known as Ig-hepta) is an orphan receptor that belongs to group VI adhesion-GPCRs along with GPR110, GPR111, GPR113, and GPR115. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR116 has four I-set immunoglobulin-like repeats, which is found in the members of the immunoglobulin superfamily of cell surface proteins, and a SEA (sea urchin sperm protein, enterokinase, and a grin)-box, which is present in the extracellular domain of the transmembrane mucin (MUC) family and known to enhance O-glycosylation. GPR116 is highly expressed in fetal and adult lung, and it has been shown to regulate lung surfactant levels as well as to stimulate breast cancer metastasis through a G(q)-p63-RhoGEF-Rho GTPase signaling pathway. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS
LDELDYITYIGLSISILSLAICIVIESLVWKSVTKNRTSYMRHVCILNIAVSLLIADIWFIVVAAIQDQN
YAVNGNVCVAATFFIHFFYLCVFFWMLALGLMLFYRLVFILHDTSKTIQKAVAFCLGYGCPLIISVITIA
VTLPRDSYTRKKVCWLNWEDSKALLAFVIPALIIVAVNSIITVVVIVKILRPSIGEKPSKQERSSLFQII
KSIGVLTPLLGLTWGFGLATVIKGSSIVFHILFTLLNAFQGLFILVFGTLWDKKVQEALLNKYSF
>gnl|CDD|320383 cd15255, 7tmB2_GPR144, orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR144 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR133. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS
EATLRTLSFIGCGVSLCALIVTFILFLAVGVPKSERTTVHKNLIFALAAAEFLLMFSEWAKGNQVACWAV
TALLHLFFLAAFSWMLVEGLLLWSKVVAVNMSEDRRMKFYYVTGWGLPVVIVAVTLATSFNKYVADQHCW
LNVQTDIIWAFVGPVLFVLTVNTFVLFRVVMVTVSSARRRAKMLTPSSDLEKQIGIQIWATAKPVLVLLP
VLGLTWLCGVLVHLSDVWAYVFITLNSFQGLYIFLVYAIYNSEVRNAIQRMQE
>gnl|CDD|320384 cd15256, 7tmB2_GPR133, orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR133 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR144. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS
QVALSSITYVGCSLSIFCLAITLVTFAVLSSVSTIRNQRYHIHANLSFAVLVAQILLLISFRFEPGTLPC
KIMAILLHFFFLSAFAWMLVEGLHLYSMVIKVFGSEESKHFYYYGIGWGSPLLICIISLTSALDSYGESD
NCWLSLENGAIWAFVAPALFVIVVNIGILIAVTRVISRISADNYKVHGDANAFKLTAKAVAVLLPILGSS
WVFGVLAVNTHALVFQYMFAIFNSLQGFFIFLFHCLLNSEVRAAFKHKTK
>gnl|CDD|320385 cd15257, 7tmB2_GPR128, orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR128 is an orphan receptor of the adhesion family (subclass B2) that belongs to the class B GPCRs. Expression of GPR128 was detected in the mouse intestinal mucosa and is thought to be involved in energy balance, as its knockout mice showed a decrease in body weight gain and an increase in intestinal contraction frequency compared to wild-type controls. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
AKTLDIISTIGCVLSIAGLVITIIFHLHTRKLRKSSVTWVLLNLCSSLLLFNIIFTSGVENTNNDYEIST
VPDRETNTVLLSEEYVEPDTDVCTAVAALLHYFLLVTFMWNAVYSAQLYLLLIRMMKPLPEMFILQASAI
GWGIPAVVVAITLGATYRFPTSLPVFTRTYRQEEFCWLAALDKNFDIKKPLLWGFLLPVGLILITNVILF
IMTSQKVLKKNNKKLTTKKRSYMKKIYITVSVAVVFGITWILGYLMLVNNDLSKLVFSYIFCITNTTQGV
QIFILYTWRTPEFRKLVSKLSLK
>gnl|CDD|320386 cd15258, 7tmB2_GPR126-like_Adhesion_VIII, orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors. Group VIII adhesion GPCRs include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, GPR114, and GPR126. GPR56 is involved in the regulation of oligodendrocyte development and myelination in the central nervous system via coupling to G(12/13) proteins, which leads to the activation of RhoA GTPase. GPR126, on the other hand, is required for Schwann cells, but not oligodendrocyte myelination in the peripheral nervous system. Gpr64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also over-expressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. GPR97 is identified as a lymphatic adhesion receptor that is specifically expressed in lymphatic endothelium, but not in blood vascular endothelium, and is shown to regulate migration of lymphatic endothelial cells via the small GTPases RhoA and cdc42. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. GPR114 is mainly found in granulocytes (polymorphonuclear leukocytes), and GPR114-transfected cells induced an increase in cAMP levels via coupling to G(s) protein. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
LHILTFISYVGCGISAIFLAITILTYIAFRKLRRDYPSKIHMNLCAALLLLNLAFLLSSWIASFGSDGLC
IAVAVALHYFLLACLTWMGLEAFHLYLLLVKVFNTYIRRYILKLCLVGWGLPALLVTLVLSVRSDNYGPI
TIPNGEGFQNDSFCWIRDPVVFYITVVGYFGLTFLFNMVMLATVLVQICRLREKAQATPRKRALHDLLTL
LGLTFLLGLTWGLAFFAWGPFNLPFLYLFAIFNSLQGFFIFIWYCSMKENVRKQWRA
>gnl|CDD|320387 cd15259, 7tmB2_GPR124-like_Adhesion_III, orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors. group III adhesion GPCRs include orphan GPR123, GPR124, GPR125, and their closely related proteins. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. GPR123 is predominantly expressed in the CNS including thalamus, brain stem and regions containing large pyramidal cells. GPR124, also known as tumor endothelial marker 5 (TEM5), is highly expressed in tumor vessels and in the vasculature of the developing embryo. GPR124 is essentially required for proper angiogenic sprouting into neural tissue, CNS-specific vascularization, and formation of the blood-brain barrier. GPR124 also interacts with the PDZ domain of DLG1 (discs large homolog 1) through its PDZ-binding motif. Recently, studies of double-knockout mice showed that GPR124 functions as a co-activator of Wnt7a/Wnt7b-dependent beta-catenin signaling in brain endothelium. Furthermore, WNT7-stimulated beta-catenin signaling is regulated by GPR124's intracellular PDZ binding motif and leucine-rich repeats (LRR) in its N-terminal extracellular domain. GPR125 directly interacts with dishevelled (Dvl) via its intracellular C-terminus, and together, GPR125 and Dvl recruit a subset of planar cell polarity (PCP) components into membrane subdomains, a prerequisite for activation of Wnt/PCP signaling. Thus, GPR125 influences the noncanonical WNT/PCP pathway, which does not involve beta-catenin, through interacting with and modulating the distribution of Dvl
FELLHPVVYAGAALCLLCLLATIITYIVFHRLIRISRKGRHMLVNLCLHLLLTCVVFVGGINRTANQLVC
QAVGILLHYSTLCTLLWVGVTARNMYKQVTKTAKPPQDEDQPPRPPKPMLRFYLIGWGIPLIICGITAAV
NLDNYSTYDYCWLAWDPSLGAFYGPAALIVLVNCIYFLRIYCQLKGAPVSFQSQLRGAVITLFLYVAMWA
CGALAVSQRYFLDLVFSCLYGATCSSLGLFVLIHHCLSREDVRQSWRQCC
>gnl|CDD|320388 cd15260, 7tmB1_NPR_B4_insect-like, insect neuropeptide receptor subgroup B4 and related proteins, member of the class B family of seven-transmembrane G protein-coupled receptors. This subgroup includes a neuropeptide receptor found in Nilaparvata lugens (brown planthopper) and its closely related proteins from mollusks and annelid worms. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes
RQFVNYVYIGGYSVSLIALIISLAIFFSFRSLRCTRITIHMNLFISFALNNLLWIVWYKLVVDNPEVLLE
NPIWCQALHVLLQYFMVCNYFWMFCEGLYLHTVLVVAFISEKSLMRWFIAIGWGVPLVITAIYAGVRASL
PDDTERCWMEESSYQWILIVPVVLSLLINLIFLINIVRVLLTKLRATSPNPAPAGLRKAVRATLILIPLL
GLQFLLIPFRPEPGAPLETIYQYVSALLTSLQGLCVAVLFCFCNGEVIAAIKRKWRR
>gnl|CDD|320389 cd15261, 7tmB1_PDFR, The pigment dispersing factor receptor, member of the class B seven-transmembrane G protein-coupled receptors. The pigment dispersing factor receptor (PDFR) is a G protein-coupled receptor that binds the circadian clock neuropeptide PDF, a functional ortholog of the mammalian vasoactive intestinal peptide (VIP), on the pacemaker neurons. The PDFR is implicated in regulating flight circuit development and in modulating acute flight In Drosophila melanogaster. The PDFR activation stimulates adenylate cyclase, thereby increasing cAMP levels in many different pacemakers, and the receptor signaling has been shown to regulate behavioral circadian rhythms and geotaxis in Drosophila. The PDFR belongs to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. . These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. They play key roles in hormone homeostasis in mammals and are promising drug targets in various human diseases including diabetes, osteoporosis, obesity, neurodegenerative conditions (Alzheimer###s and Parkinson's), cardiovascular disease, migraine, and psychiatric disorders (anxiety, depression)
ARGTRTLEIVGLCLSLVSLIISLFIFSYFRTLRNHRTRIHKNLFLAILLQVIIRLVLYIDQAITRSRGSH
TNAATTEGRTINSTPILCEGFYVLLEYAKTVMFMWMFIEGLYLHNIIVVSVFSGKPNYLFYYILGWGIPI
VHTSAWAIVTLIKMKVNRCWFGYYLTPYYWILEGPRLAVILINLFFLLNIIRVLVSKLRESHSREIEQVR
KAVKAAIVLLPLLGITNILQMIPPPLTSVIVGFAVWSYSTHFLTSFQGFFVALIYCFLNGEVKNVLKKFW
RR
>gnl|CDD|320390 cd15262, 7tmB1_NPR_B3_insect-like, insect neuropeptide receptor subgroup B3 and related proteins belong to subfamily B1 of hormone receptors; member of the class B secretin-like seven-transmembrane G protein-coupled receptors. This subgroup includes a neuropeptide receptor found in Bombyx mori (silk worm) and its closely related proteins from arthropods. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes
LKQRYRFHVAALSVSVVTSLPAVFIFYSYKRLRITRVILHRNLLISIIIRNILVIISKVFVILDALTSSG
DDTVMNQNAVVCRLLSIFERAARNAVFACMFVEGFYLHRLIVAVFAEKSSIRFLYVIGAVLPLFPVIIWA
IIRALHNDHSCWVVDIEGVQWVLDTPRLFILLVNTVLLVDIIRVLVTKLRNTEENSQTKSTTRATLFLVP
LFGLHFVITAYRPSTDDCDWEDIYYYANYLIEGLQGFLVAILFCYINKEVHYLIKNTYRK
>gnl|CDD|320391 cd15263, 7tmB1_DH_R, insect diuretic hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors. This group includes G protein-coupled receptors that specifically bind to insect diuretic hormones found in Manduca sexta (moth) and Acheta domesticus (the house cricket), among others. Insect diuretic hormone and their GPCRs play critical roles in the regulation of water and ion balance. Thus they are attractive targets for developing new insecticides. Activation of the diuretic hormone receptors stimulate adenylate cyclase, thereby increasing cAMP levels in Malpighian tube. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of Gs family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx
VEVTTTIYFIGYSLSLVALSLALWIFLYFKDLRCLRNTIHTNLMFTYILADLTWILTLTLQVSIGEDQKS
CIILVVLLHYFHLTNFFWMFVEGLYLYMLVVETFSGENIKLRVYAFIGWGIPAVVIVIWAIVKALAPTAP
NTALDPNGLLKHCPWMAEHIVDWIFQGPAILVLAVNLVFLVRIMWVLITKLRSANTVETQQYRKAAKALL
VLIPLLGITYILVIAGPTEGIAANIFEYVRAVLLSTQGFTVALFYCFLNTEVRNTLRHHFER
>gnl|CDD|320392 cd15264, 7tmB1_CRF-R, corticotropin-releasing factor receptors, member of the class B family of seven-transmembrane G protein-coupled receptors. The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways
YKVALIIYYLGFSISLVALAVALIIFLYFRSLRCLRNNIHCNLIVTFILRNVTWFIMQNTLTEIHHQSNQ
WVCRLIVTVYNYFQVTNFFWMFVEGLYLHTMIVWAYSADKIRFWYYIVIGWCIPCPFVLAWAIVKLLYEN
EHCWLPKSENSYYDYIYQGPILLVLLINFIFLFNIVWVLITKLRASNTLETIQYRKAVKATLVLLPLLGI
TYMLFFINPGDDKTSRLVFIYFNTFLQSFQGLFVAVFYCFLNGEVRSAIRKKFSR
>gnl|CDD|320393 cd15265, 7tmB1_PTHR, parathyroid hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors. The parathyroid hormone (PTH) receptor family has three subtypes: PTH1R, PTH2R and PTH3R. PTH1R is expressed in bone and kidney and is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to a G(s)-protein that in turn activates adenylate cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple intracellular signaling pathways. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39), but not by PTHrP. PTH also strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs, suggesting that TIP-39 is a natural ligand for PTH2R. On the other hand, PTH3R binds and responds to both PTH and PTHrP, but not the TIP-39. Moreover, the PTH3R is more closely related to the PTH1R than PTH2R. PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. The PTH3R is found in chicken and fish, but it is absent in mammals. The PTH receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways
FERLYLIYTVGYSISLVSLTVAVFILGYFRRLHCTRNYIHMHLFVSFMLRAVSIFVKDAVLYSGSGLDEL
ERPSMEDLKSIVEAPPVDKSQYVGCKVAVTLFLYFLATNYYWILVEGLYLHSLIFMAFFSDKKYLWGFTL
IGWGFPAVFVIPWASVRATLADTRCWDLSAGNYKWIYQVPILAAIVVNFILFLNIVRVLATKLRETNAGR
CDTRQQYRKLAKSTLVLIPLFGVHYIVFMGMPYTEVGLLWQIRMHYELFFNSFQGFFVAIIYCFCNGEVQ
AEIKKRWER
>gnl|CDD|320394 cd15266, 7tmB1_GLP2R, glucagon-like peptide-2 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors. Glucagon-like peptide-2 receptor (GLP2R) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon receptor (GCGR) and GLP1R. GLP2R is activated by glucagon-like peptide 2, which is derived from the large proglucagon precursor. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. GLP2R belongs to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways
LLTLQLIYTIGYSLSLISLSLALLILLLLRKLHCTRNYIHMNLFASFILRALAVLIKDIVLYSTYSKRPD
DETGWISYLSEESSTSCRVAQVFMHYFVGANYFWLLVEGLYLHTLLVTAVLSERRLLKKYMLIGWGTPVL
FVVPWGVAKILLENTGCWGRNENMGIWWIIRGPILLCITVNFYIFLKILKLLLSKLKAQQMRFTDYKYRL
ARSTLVLIPLLGIHEVVFSFITDEQVEGFSRHIRLFIQLTLSSFQGFLVAVLYCFANGEVKAELKKRWQL
>gnl|CDD|320395 cd15267, 7tmB1_GCGR, glucagon receptor, member of the class B family of seven-transmembrane G protein-coupled receptors. Glucagon receptor (GCGR) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon-like peptide-1 receptor (GLP1R) and GLP2R. GCGR is activated by glucagon, which is derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR belongs to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways
KTYSSFQVMYTVGYSLSLGALLLALAILGGFSKLHCMRNAIHMNLFASFILKASSVLVIDGLLRTRYSQK
IEDDLSSTWLSDEAVAGCRVAAVFMQYGIVANYCWLLVEGIYLHNLLVLAVFPERSYFSLYLCIGWGAPA
LFVVPWVVVKCLYENVQCWTSNDNMGFWWILRFPVFLAILINFFIFVRIIQILVSKLRARQMHYTDYKFR
LAKSTLTLIPLLGIHEVVFAFVTDEHAQGTLRSAKLFFDLFLSSFQGLLVAVLYCFLNKEVQSELRRRWH
R
>gnl|CDD|341342 cd15268, 7tmB1_GLP1R, glucagon-like peptide-1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors. Glucagon-like peptide-1 receptor (GLP1R) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon receptor and GLP2R. GLP1R is activated by glucagon-like peptide 1 (GLP1), which is derived from the large proglucagon precursor. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways
LLFLYIIYTVGYALSFSALVIASAILLGFRHLHCTRNYIHLNLFASFILRALSVFIKDAALKWMYSTAAQ
QHQWDGLLSYQDSLSCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVFSEQRIFRLYLSIGWGVPLLF
VIPWGIVKYLYEDEGCWTRNSNMNYWLIIRLPILFAIGVNFLIFIRVICIVVSKLKANLMCKTDIKCRLA
KSTLTLIPLLGTHEVIFAFVMDEHARGTLRFVKLFTELSFTSFQGLMVAILYCFVNNEVQMEFRKSWER
>gnl|CDD|320397 cd15269, 7tmB1_VIP-R1, vasoactive intestinal polypeptide (VIP) receptor 1, member of the class B family of seven-transmembrane G protein-coupled receptors. Vasoactive intestinal peptide (VIP) receptor 1 is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. VIP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. However, depending on its cellular location, VIP-R1 is also capable of coupling to additional G proteins such as G(q) protein, thus leading to the activation of phospholipase C and intracellular calcium influx
FGTVKTGYTIGHSLSLISLTAAMIILCLFRKLHCTRNYIHMHLFMSFILRAIAVFIKDAVLFESGEEDHC
SVASVGCKAAMVFFQYCIMANFFWLLVEGLYLHTLLAVSFFSERKYFWWYILIGWGAPSVFITAWSVARI
YFEDVGCWDTIIESLLWWIIKTPILVSILVNFILFICIIRILVQKLHSPDIGRNESSQYSRLAKSTLLLI
PLFGIHYIMFAFFPDNFKAEVKLVFELILGSFQGFVVAVLYCFLNGEVQAELKRKWRR
>gnl|CDD|320398 cd15270, 7tmB1_GHRHR, growth-hormone-releasing hormone receptor, member of the class B family of seven-transmembrane G protein-coupled receptors. Growth hormone-releasing hormone receptor (GHRHR) is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, pituitary adenylate cyclase activating polypeptide (PACAP), and vasoactive intestinal peptide. These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. GHRH is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. GHRHR is found in mammals as well as zebrafish and chicken, whereas the GHRHR type 2, an ortholog of the GHRHR, has only been identified in ray-finned fish, chicken and Xenopus. Xenopus laevis GHRHR2 has been shown to interact with both endogenous GHRH and PACAP-related peptide (PRP)
FSTVKIIYTVGYSISIVSLCVAVAILVAFRRLHCPRNYIHIQLFFTFILKAIAVFIKDAALFQEDDTDHC
SMSTVLCKVSVVFCHYCVMTNFFWLLVEAVYLNCLLASSFPRGKRYFWWLVLLGWGLPTLCTGTWILCKL
YFEDTECWDINNDSPYWWIIKGPIVISVGVNFLLFLNIIRILLKKLDPRQINFNNSAQYRRLSKSTLLLI
PLFGTHYIIFNFLPDYAGLGIRLYLELCLGSFQGFIVAVLYCFLNQEVQTEISRKWYG
>gnl|CDD|320399 cd15271, 7tmB1_GHRHR2, growth-hormone-releasing hormone receptor type 2, member of the class B family of seven-transmembrane G protein-coupled receptors. Growth hormone-releasing hormone receptor type 2 (GHRHR2) is found in non-mammalian vertebrates such as chicken and frog. It is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, pituitary adenylate cyclase activating polypeptide (PACAP), vasoactive intestinal peptide, and mammalian growth hormone-releasing hormone. These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Mammalian GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. Mammalian GHRH is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. GHRHR is found in mammals as well as zebrafish and chicken, whereas the GHRHR type 2, an ortholog of the GHRHR, has only been identified in ray-finned fish, chicken and Xenopus. Xenopus laevis GHRHR2 has been shown to interact with both endogenous GHRH and PACAP-related peptide (PRP)
FSTVKLLYTVGYGTSLTSLITAVLIFCTFRKLHCTRNYIHINLFVSFILRALAVFIKDAVLFADESVDHC
TMSTVACKAAVTFFQFCVLANFFWLLVEGMYLQTLLLLTFTSDRKYFWWYILIGWGAPSVTVTVWVLTRL
QYDNRGCWDDLESRIWWIIKTPILLSVFVNFLIFINVIRILVQKLKSPDVGGNDTSHYMRLAKSTLLLIP
LFGVHYVVFAFFPEHVGVEARLYFELVLGSFQGFIVALLYCFLNGEVQAEIKKRLGK
>gnl|CDD|320400 cd15272, 7tmB1_PTH-R_related, invertebrate parathyroid hormone-related receptors, member of the class B family of seven-transmembrane G protein-coupled receptors. This group includes parathyroid hormone (PTH)-related receptors found in invertebrates such as mollusks and annelid worms. The PTH family receptors are members of the B1 subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. The parathyroid hormone type 1 receptor (PTH1R) is found in all vertebrate species and is activated by two polypeptide ligands: parathyroid hormone (PTH), an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to G(s)- protein that in turn activates adenylyl cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple signaling pathways
LPSIRLMYNIGYGLSLVSLLIAVIIMLYFKKLHCPRNTIHINLFVSFILRAVLSFIKENLLVQGVGFPGD
VYYDSNGVIEFKDEGSHWECKLFFTMFNYILGANYMWIFVEGLYLHMLIFVAVFSENSRVKWYILLGWLS
PLLFVLPWVFVRATLEDTLCWNTNTNKGYFWIIRGPIVISIAINFLFFINIVRVLFTKLKASNTQESRPF
RYRKLAKSTLVLIPLFGVHYMVFVVLPDSMSSDEAELVWLYFEMFFNSFQGFIVALLFCFLNGEVQSEIK
KKWQR
>gnl|CDD|320401 cd15273, 7tmB1_NPR_B7_insect-like, insect neuropeptide receptor subgroup B7 and related proteins, member of the class B family of seven-transmembrane G protein-coupled receptors. This subgroup includes a neuropeptide receptor found in Nilaparvata lugens (brown planthopper) and its closely related proteins from invertebrates. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes
LPIIKGISQIGYIVSLITLIIAFAIFLSFKKLHCARNKLHMHLFASFILRAFMTLLKDSLFIDGLGLLAD
IVERNGGGNEVIANIGSNWVCKAITSLWQYFIIANYSWILMEGLYLHNLIFLALFSDENNIILYILLGWG
LPLIFVVPWIVARILFENSLCWTTNSNLLNFLIIRIPIMISVLINFILFLNIVRVLLVKLRSSVNEDSRR
YKKWAKSTLVLVPLFGVHYTIFLILSYLDDTNEAVELIWLFCDQLFASFQGFFVALLYCFLNGEVRAEIQ
RKWRR
>gnl|CDD|341343 cd15274, 7tmB1_calcitonin_R, calcitonin receptor, member of the class B family of seven-transmembrane G protein-coupled receptors. This group includes G protein-coupled receptors for calcitonin (CT) and calcitonin gene-related peptides (CGRPs). Calcitonin, a 32-amino acid peptide hormone, is involved in calcium metabolism in many mammalian species and acts to reduce blood calcium levels and directly inhibits bone resorption by acting on osteoclast. Thus, CT acts as an antagonist to parathyroid hormone and is commonly used in the treatment of bone disorders. The CT receptor is predominantly found in osteoclasts, kidney, and brain, and is primarily coupled to stimulatory G(s) protein, which leads to activation of adenylate cyclase, thereby increasing cAMP production. CGRP, a member of the calcitonin family of peptides, is a potent vasodilator and may contribute to migraine. It is expressed in the peripheral and central nervous system and exists in two forms in humans (alpha-CGRP and beta-CGRP). CGRP meditates its physiological effects through calcitonin receptor-like receptor (CRLR) and receptor activity-modifying protein 1 (RAMP1), a single transmembrane domain protein. Thus, the CRLR/RAMP1 complex serves as a functional CGRP receptor. On the other hand, the CRLR/RAMP2 and CRLR/RAMP3 complexes function as adrenomedullin-specific receptors. The CT and CGRP receptors belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide
AYNLYYLAIVGHSLSIATLLISLGIFFFFRSLSCQRVTLHKNLFLSYILNSIIIIIHLVAVVPNGELVAR
NPVSCKILHFIHQYMMGCNYFWMLCEGIYLHTLIVVAVFAEKQRLMWYYLLGWGFPLIPTTIHAITRAVY
YNDNCWLSSETHLLYIIHGPIMAALVVNFFFLLNIVRVLVTKLRETHEAESHMYLKAVKATLILVPLLGI
QFVLFPWRPSGKILGKIYDYVMHSLIHFQGFFVATIFCFCNGEVQATLKRQWNQYKIQFGVRFG
>gnl|CDD|320403 cd15275, 7tmB1_secretin, secretin receptor, member of the class B family of seven-transmembrane G protein-coupled receptors. Secretin receptor is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include vasoactive intestinal peptide (VIP), growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors, and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Secretin, a polypeptide secreted by entero-endocrine S cells in the small intestine, is involved in maintaining body fluid balance. This polypeptide regulates the secretion of bile and bicarbonate into the duodenum from the pancreatic and biliary ducts, as well as regulates the duodenal pH by the control of gastric acid secretion. Studies with secretin receptor-null mice indicate that secretin plays a role in regulating renal water reabsorption. Secretin mediates its biological actions by elevating intracellular cAMP via G protein-coupled secretin receptor, which is expressed in the brain, pancreas, stomach, kidney, and liver
FMYLKTMYTVGYSVSLVSLAIALAILCSFRRLHCTRNYIHMQLFLSFILRAISIFIKDAVLFSSEDDNHC
DIYTVGCKVAMVFSNYCIMANYSWLLVEGLYLHSLLSISFFSERKHLWWYIALGWGSPLIFIISWAIARY
LHENEGCWDTRRNAWIWWIIRGPVILSIFVNFILFLNILRILMRKLRAPDMRGNEFSQYKRLAKSTLLLI
PLFGLHYILFAFFPEDVSSGTMEIWLFFELALGSFQGFVVAVLYCFLNGEVQLEIQRKWRR
>gnl|CDD|320404 cd15277, 7tmC_RAIG3_GPRC5C, retinoic acid-inducible orphan G-protein-coupled receptor 3; class C family of seven-transmembrane G protein-coupled receptors, group 5, member C. Retinoic acid-inducible G-protein-coupled receptors (RAIGs), also referred to as GPCR class C group 5, are a group consisting of four orphan receptors RAIG1 (GPRC5A), RAIG2 (GPRC5B), RAIG3 (GPRC5C), and RAIG4 (GPRC5D). Unlike other members of the class C GPCRs which contain a large N-terminal extracellular domain, RAIGs have a shorter N-terminus. Thus, it is unlikely that RAIGs bind an agonist at its N-terminus domain. Instead, the agonists may bind to the seven-transmembrane domain of these receptors. In addition, RAIG2 and RAIG3 contain a cleavable signal peptide whereas RAIG1 and RAIG4 do not. Although their expression is induced by retinoic acid (vitamin A analog), their biological function is not clearly understood. To date, no ligand is known for the members of RAIG family. Three receptor types (RAIG1-3) are found in vertebrates, while RAIG4 is only present in mammals. They show distinct tissue distribution with RAIG1 being primarily expressed in the lung, RAIG2 in the brain and placenta, RAIG3 in the brain, kidney and liver, and RAIG4 in the skin. The specific function of RAIG3 is unknown; however, this protein may play a role in mediating the effects of retinoic acid on embryogenesis, differentiation, and tumorigenesis through interaction with a G-protein signaling cascade
AWGIVLEAVAGAGVVTSFVLTIVLVASLPFVQDKKKKSLLGTQVFFLLGTLGLFCLVFAFIVGPNFATCA
SRRFLFGVLFAICFSCLLAHAVRLNFLARRNRGPRGWVIFLLALGLWLVEVIINTEWLIITIVRGNAGSA
PVLGDPCNIANQDFVMALIYVMFLLLAAFITAWPALCGKYKHWRKHGAFILVTGFLSVAIWVAWIVMYVY
GNQKVGQPYWDDPTLAIALVSNAWVFLFFYIIPEICQLTK
>gnl|CDD|320405 cd15278, 7tmC_RAIG2_GPRC5B, retinoic acid-inducible orphan G-protein-coupled receptor 2; class C family of seven-transmembrane G protein-coupled receptors, group 5, member B. Retinoic acid-inducible G-protein-coupled receptors (RAIGs), also referred to as GPCR class C group 5, are a group consisting of four orphan receptors RAIG1 (GPRC5A), RAIG2 (GPRC5B), RAIG3 (GPRC5C), and RAIG4 (GPRC5D). Unlike other members of the class C GPCRs which contain a large N-terminal extracellular domain, RAIGs have a shorter N-terminus. Thus, it is unlikely that RAIGs bind an agonist at its N-terminus domain. Instead, the agonists may bind to the seven-transmembrane domain of these receptors. In addition, RAIG2 and RAIG3 contain a cleavable signal peptide whereas RAIG1 and RAIG4 do not. Although their expression is induced by retinoic acid (vitamin A analog), their biological function is not clearly understood. To date, no ligand is known for the members of RAIG family. Three receptor types (RAIG1-3) are found in vertebrates, while RAIG4 is only present in mammals. They show distinct tissue distribution with RAIG1 being primarily expressed in the lung, RAIG2 in the brain and placenta, RAIG3 in the brain, kidney and liver, and RAIG4 in the skin. RAIG2 (GPRC5B), a mammalian Boss (Bride of sevenless) homolog, has been shown to activate obesity-associated inflammatory signaling in adipocytes, and that the GPRC5B knockout mice have been shown to be resistance to high-fat diet-induced obesity and insulin resistance
IWGIVVEAVAGAGVLITLLLMLILLVRLPFIKEKEKKSPVGPHFLFLLGTLGLFGLTFAFIIQEDETICS
LRRFLWGVLFALCFSCLLAQGWRLRRLVRHGKGPSGWHLTGLALCLMLVQVIIAVEWLILTVLRDGRPAC
QYEPMDFVMALIYVMVLLVATLGLALFTLCGKFQKWKKNGICLLITCFLSVLIWVAWMTMYLYGNDELGR
SDDWNDPTLAIALVASGWVFLIFHAIPEVHCTLL
>gnl|CDD|320406 cd15279, 7tmC_RAIG1_4_GPRC5A_D, retinoic acid-inducible orphan G-protein-coupled receptors 1 and 4; class C family of seven-transmembrane G protein-coupled receptors, group 5, member A and D. Retinoic acid-inducible G-protein-coupled receptors (RAIGs), also referred to as GPCR class C group 5, are a group consisting of four orphan receptors RAIG1 (GPRC5A), RAIG2 (GPRC5B), RAIG3 (GPRC5C), and RAIG4 (GPRC5D). Unlike other members of the class C GPCRs which contain a large N-terminal extracellular domain, RAIGs have a shorter N-terminus. Thus, it is unlikely that RAIGs bind an agonist at its N-terminus domain. Instead, the agonists may bind to the seven-transmembrane domain of these receptors. In addition, RAIG2 and RAIG3 contain a cleavable signal peptide whereas RAIG1 and RAIG4 do not. Although their expression is induced by retinoic acid (vitamin A analog), their biological function is not clearly understood. To date, no ligand is known for the members of RAIG family. Three receptor types (RAIG1-3) are found in vertebrates, while RAIG4 is only present in mammals. They show distinct tissue distribution with RAIG1 being primarily expressed in the lung, RAIG2 in the brain and placenta, RAIG3 in the brain, kidney and liver, and RAIG4 in the skin. RAIG1 is evolutionarily conserved from mammals to fish. RAIG1 has been to shown to act as a tumor suppressor in non-small cell lung carcinoma as well as oral squamous cell carcinoma, but it could also act as an oncogene in breast cancer, colorectal cancer, and pancreatic cancer. Studies have shown that overexpression of RAIG1 decreases intracellular cAMP levels. Moreover, knocking out RAIG1 induces the activation of the NF-kB and STAT3 signaling pathways leading to cell proliferation and resistance to apoptosis. The specific function of RAIG4 is unknown; however, this protein may play a role in mediating the effects of retinoic acid on embryogenesis, differentiation, and tumorigenesis through interaction with a G-protein signaling cascade
AWGIVLETLAAAGIVVTIALILALLFLMCKVQDSNKRKMLPTQFLFLLGVLGIFGLTFAFIIELNGQTGP
TRFFLFGVLFAICFSCLLAHASNLVKLVRGRKPFSWLVILLLAVGFSLVQVVIAIEYIVLTMVRTNVNVF
SEMTAPQLNEDFVLLLIYVLFLMALTFLVSKFTFCGSCKGWKRHGAHIFVTMLFSIAIWVAWITMLLRGN
PFQRNRQWDDPVLSIALVANGWVFLLMYIVPELCLLTR
>gnl|CDD|320407 cd15280, 7tmC_V2R-like, vomeronasal type-2 receptor-like proteins, member of the class C family of seven-transmembrane G protein-coupled receptors. This group represents vomeronasal type-2 receptor-like proteins that are closely related to the V2R family of vomeronasal GPCRs. Members of the V2R family of vomeronasal GPCRs are involved in detecting protein pheromones for social and sexual cues between the same species. V2Rs and G-alpha(o) protein are coexpressed in the basal layer of the vomeronasal organ (VNO), which is the sensory organ of the accessory olfactory system present in amphibians, reptiles, and non-primate mammals such as mice and rodents, but it is non-functional or absent in humans, apes, and monkeys. On the other hand, members of the V1R receptor family and G-alpha(i2) protein are co-expressed in the apical neurons of the VNO. Activation of V1R or V2R causes activation of phospholipase pathway, generating the secondary messengers diacylglycerol (DAG) and IP3. However, in contrast to V1Rs, V2Rs contain the long N-terminal extracellular domain, which is believed to bind pheromones. Human V2R1-like protein, also known as putative calcium-sensing receptor-like 1 (CASRL1), is not included here because it is a nonfunctional pseudogene
ALGITLIALSIFGALVVLAVTVVYIMHRHTPLVKANDRELSFLIQMSLVITFLTSILFIGKPENWSCMAR
QITLALGFSLCLSSILGKTISLFLRYRASKSETRLDSMHPIYQKIIVLICVLIEVGICTAYLILEPPRMY
KNTEVQNVKIIFECNEGSIEFLCSIFGFDVFLALLCFLTAFVARKLPDNFNEGKFITFGMLVFFIVWISF
VPAYLSTRGKFKVAVEIFAILASSFGLLGCIFVPKCYIILLKP
>gnl|CDD|320408 cd15281, 7tmC_GPRC6A, class C of seven-transmembrane G protein-coupled receptors, subtype 6A. GRPC6A (GPCR, class C, group 6, subtype A) is a widely expressed amino acid-sensing GPCR that is most closely related to CaSR. GPRC6A is most potently activated by the basic amino acids L-arginine, L-lysine, and L-ornithine and less potently by small aliphatic amino acids. Moreover, the receptor can be either activated or modulated by divalent cations such as Ca2+ and Mg2+. GPRC6A is expressed in the testis, but not the ovary and specifically also binds to the osteoblast-derived hormone osteocalcin (OCN), which regulates testosterone production by the testis and male fertility independently of the hypothalamic-pituitary axis. Furthermore, GPRC6A knockout studies suggest that GRPC6A is involved in regulation of bone metabolism, male reproduction, energy homeostasis, glucose metabolism, and in activation of inflammation response, as well as prostate cancer growth and progression, among others. GPRC6A has been suggested to couple to the Gq subtype of G proteins, leading to IP3 production and intracellular calcium mobilization. GPRC6A contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD), and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B, GPRC6A, mGlu, and TAS1R receptors
GFAIVLLILSALGVLLIFFISALFTKNLNTPVVKAGGGPLCYVILLSHFGSFISTVFFIGEPSDLTCKTR
QTLFGISFTLCVSCILVKSLKILLAFSFDPKLQELLKCLYKPIMIVFICTGIQVIICTVWLVFYKPFVDK
NFSLPESIILECNEGSYVAFGLMLGYIALLAFICFIFAFKGRKLPENYNEAKFITFGMLIYFIAWITFIP
IYATTFGKYVPAVEMIVILISNYGILSCTFLPKCYIILY
>gnl|CDD|320409 cd15282, 7tmC_CaSR, calcium-sensing receptor, member of the class C of seven-transmembrane G protein-coupled receptors. CaSR is a widely expressed GPCR that is involved in sensing small changes in extracellular levels of calcium ion to maintain a constant level of the extracellular calcium via modulating the synthesis and secretion of calcium regulating hormones, such as parathyroid hormone (PTH), in order to regulate Ca(2+)transport into or out of the extracellular fluid via kidney, intestine, and/or bone. For instance, when Ca2+ is high, CaSR downregulates PTH synthesis and secretion, leading to an increase in renal Ca2+ excretion, a decrease in intestinal Ca2+ absorption, and a reduction in release of skeletal Ca2+. CaSR is coupled to both G(q/11)-dependent activation of phospholipase and, subsequently, intracellular calcium mobilization and protein kinase C activation as well as G(i/o)-dependent inhibition of adenylate cyclase leading to inhibition of cAMP formation. CaSR is closely related to GRPC6A (GPCR, class C, group 6, subtype A), which is an amino acid-sensing GPCR that is most potently activated by the basic amino acids L-arginine, L-lysine, and L-ornithine. These receptors contain a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD), and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TASR1 receptors
PFGIALTLFAVLGIFLTAFVLGVFIKFRNTPIVKATNRELSYLLLFSLICCFSSSLIFIGEPQDWTCRLR
QPAFGISFVLCISCILVKTNRVLLVFEAKIPTSLHRKWWGLNLQFLLVFLCTFVQIVICVIWLYTAPPSS
YRNHELEDEIIFITCNEGSLMALGFLIGYTCLLAAICFFFAFKSRKLPENFNEAKFITFSMLIFFIVWIS
FIPAYASTYGKFVSAVEVIAILASSFGLLACIFFNKVYIILF
>gnl|CDD|320410 cd15283, 7tmC_V2R_pheromone, vomeronasal type-2 pheromone receptors, member of the class C family of seven-transmembrane G protein-coupled receptors. This group represents vomeronasal type-2 pheromone receptors (V2Rs). Members of the V2R family of vomeronasal GPCRs are involved in detecting protein pheromones for social and sexual cues between the same species. V2Rs and G-alpha(o) protein are coexpressed in the basal layer of the vomeronasal organ (VNO), which is the sensory organ of the accessory olfactory system present in amphibians, reptiles, and non-primate mammals such as mice and rodents, but it is non-functional or absent in humans, apes, and monkeys. On the other hand, members of the V1R receptor family and G-alpha(i2) protein are coexpressed in the apical neurons of the VNO. Activation of V1R or V2R causes activation of phospholipase pathway, producing the second messengers diacylglycerol (DAG) and IP3. However, in contrast to V1Rs, V2Rs contain the long N-terminal extracellular domain, which is believed to bind pheromones
PLGIALTVLSLLGSVLTAAVLVVFIKHRDTPIVKANNSELSYLLLLSLKLCFLCSLLFIGQPSTWTCMLR
QTAFGISFVLCISCILAKTIVVVAAFKATRPGSNIMKWFGPGQQRAIIFICTLVQVVICAIWLATSPPFP
DKNMHSEHGKIILECNEGSVVAFYCVLGYIGLLALVSFLLAFLARKLPDNFNEAKFITFSMLVFCAVWVA
FVPAYISSPGKYMVAVEIFAILASSAGLLGCIFAPKCYIILL
>gnl|CDD|320411 cd15284, 7tmC_mGluR_group2, metabotropic glutamate receptors in group 2, member of the class C family of seven-transmembrane G protein-coupled receptors. The metabotropic glutamate receptors (mGluRs) in group 2 include mGluR 2 and 3. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity
AWAIGPVTIACLGFLCTLFVIGVFIKHNNTPLVKASGRELCYILLFGVFLCYCMTFIFIAKPSPAICTLR
RLGLGTSFAVCYSALLTKTNRIARIFSGVKDGAQRPRFISPSSQVFICLALISVQLLVVSVWLLVEAPGT
RRYTLPEKRETVILKCNVRDSSMLISLTYDVVLVILCTVYAFKTRKCPENFNEAKFIGFTMYTTCIIWLA
FLPIFYVTSSDYRVQTTTMCISVSLSGFVVLGCLFAPKVHIILF
>gnl|CDD|320412 cd15285, 7tmC_mGluR_group1, metabotropic glutamate receptors in group 1, member of the class C family of seven-transmembrane G protein-coupled receptors. Group 1 mGluRs includes mGluR1 and mGluR5, as well as their closely related invertebrate receptors. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity
TEAIVAMVFACVGILATLFVTVVFIRHNDTPVVKASTRELSYIILAGILLCYASTFALLAKPSTISCYLQ
RILPGLSFAMIYAALVTKTNRIARILAGSKKKILTRKPRFMSASAQVVITGILISVEVAIIVVMLILEPP
DATLDYPTPKRVRLICNTSTLGFVVPLGFDFLLILLCTLYAFKTRNLPENFNEAKFIGFTMYTTCVIWLA
FLPIYFGSDNKEITLCFSVSLSATVALVFLFFPKVYIILF
>gnl|CDD|320413 cd15286, 7tmC_mGluR_group3, metabotropic glutamate receptors in group 3, member of the class C family of seven-transmembrane G protein-coupled receptors. The metabotropic glutamate receptors (mGluRs) in group 3 include mGluRs 4, 6, 7, and 8. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity
PWAAVPVALAVLGIIATLFVLVTFVRYNDTPIVRASGRELSYVLLTGIFLCYAITFLMVAEPGVGVCSLR
RLFLGLGMSLSYAALLTKTNRIYRIFEQGKKSVTPPRFISPTSQLVITFSLISVQLLGVLAWFAVDPPHA
LIDYEEGRTPDPEQARGVLRCDMSDLSLICCLGYSLLLMVTCTVYAIKARGVPETFNEAKPIGFTMYTTC
IVWLAFIPIFFGTAQSAEKLYIQTATLTVSMSLSASVSLGMLYMPKVYVILFHPEQNVQKR
>gnl|CDD|320414 cd15287, 7tmC_TAS1R2a-like, type 1 taste receptor subtype 2a and similar proteins, member of the class C of seven-transmembrane G protein-coupled receptors. This group includes TAS1R2a and its similar proteins found in fish. They are members of the type I taste receptor (TAS1R) family that belongs to the class C of G protein-coupled receptors. The functional TAS1Rs are obligatory heterodimers built from three known members, TAS1R1-3. TAS1R1 combines with TAS1R3 to form an umami taste receptor, which is responsible for the perception of savory taste, such as the food additive mono-sodium glutamate (MSG); whereas the combination of TAS1R2-TAS1R3 forms a sweet-taste receptor for sugars and D-amino acids. On the other hand, the type II taste receptors (TAS2Rs), which belong to the class A family of GPCRs, recognize bitter tasting compounds. In the case of sweet, for example, the TAS1R2-TAS1R3 heterodimer activates phospholipase C (PLC) via alpha-gustducin, a heterodimeric G protein that is involved in perception of sweet and bitter tastes. This activation leads to generation of inositol (1, 4, 5)-trisphosphate (IP3) and diacylglycerol (DAG), and consequently increases intracellular Ca2+ mobilization and activates a cation channel, TRPM5. In contrast to the TAS1R2-TAS1R3 heterodimer, TAS1R3 alone could activate adenylate cyclase leading to cAMP formation in the absence of alpha-gustducin. Each TAS1R contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD) and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TAS1R receptors
IVAILIMVGACVLVGLTLAVSVLFAINYNTPVVRSAGGPMCFLILGCLSLCSVSVFFYFGKPTVASCILR
YFPFLLFYTVCLACFVVRSFQIVCIFKIAAKFPKLHSWWVKYHGQWLLIAVAFVIQALLLITGFSFSPPK
PYNDTSWYPDKIILSCDINLKATSMSLVLLLSLCCLCFIFSYMGKDLPKNYNEAKAITFCLLLLILTWII
FATEYMLYRGKYIQLLNALAVLSSLYSFLLWYFLPKCYIIIF
>gnl|CDD|320415 cd15288, 7tmC_TAS1R2, type 1 taste receptor subtype 2, member of the class C of seven-transmembrane G protein-coupled receptors. This group represents TAS1R2, which is a member of the type I taste receptor (TAS1R) family that belongs to the class C of G protein-coupled receptors. The functional TAS1Rs are obligatory heterodimers built from three known members, TAS1R1-3. TAS1R1 combines with TAS1R3 to form an umami taste receptor, which is responsible for the perception of savory taste, such as the food additive mono-sodium glutamate (MSG); whereas the combination of TAS1R2-TAS1R3 forms a sweet-taste receptor for sugars and D-amino acids. On the other hand, the type II taste receptors (TAS2Rs), which belong to the class A family of GPCRs, recognize bitter tasting compounds. In the case of sweet, for example, the TAS1R2-TAS1R3 heterodimer activates phospholipase C (PLC) via alpha-gustducin, a heterodimeric G protein that is involved in perception of sweet and bitter tastes. This activation leads to generation of inositol (1, 4, 5)-trisphosphate (IP3) and diacylglycerol (DAG), and consequently increases intracellular Ca2+ mobilization and activates a cation channel, TRPM5. In contrast to the TAS1R2-TAS1R3 heterodimer, TAS1R3 alone could activate adenylate cyclase leading to cAMP formation in the absence of alpha-gustducin. Each TAS1R contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD) and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TAS1R receptors
GPTIVVALLAALGFLSTLAILVIFGRHFQTPVVRSAGGRMCFLMLAPLLVAYVNVPVYVGIPTVFTCLCR
QTLFPLCFTVCISCIAVRSFQIVCIFKMARRLPRAYSYWVKYNGPYVFVALITLLKVVIVVINVLAHPTA
PTTRADPDDPQVMILQCNPNYRLALLFNTSLDLLLSVLGFCFAYMGKELPTNYNEAKFITLCMTFYFASS
VFLCTFMSVYEGVLVTIFDALVTVINLLGISLGYFGPKCYMILF
>gnl|CDD|320416 cd15289, 7tmC_TAS1R1, type 1 taste receptor subtype 1, member of the class C of seven-transmembrane G protein-coupled receptors. This group represents TAS1R1, which is a member of the type I taste receptor (TAS1R) family that belongs to the class C of G protein-coupled receptors. The functional TAS1Rs are obligatory heterodimers built from three known members, TAS1R1-3. TAS1R1 combines with TAS1R3 to form an umami taste receptor, which is responsible for the perception of savory taste, such as the food additive mono-sodium glutamate (MSG); whereas the combination of TAS1R2-TAS1R3 forms a sweet-taste receptor for sugars and D-amino acids. On the other hand, the type II taste receptors (TAS2Rs), which belong to the class A family of GPCRs, recognize bitter tasting compounds. In the case of sweet, for example, the TAS1R2-TAS1R3 heterodimer activates phospholipase C (PLC) via alpha-gustducin, a heterodimeric G protein that is involved in perception of sweet and bitter tastes. This activation leads to generation of inositol (1, 4, 5)-trisphosphate (IP3) and diacylglycerol (DAG), and consequently increases intracellular Ca2+ mobilization and activates a cation channel, TRPM5. In contrast to the TAS1R2-TAS1R3 heterodimer, TAS1R3 alone could activate adenylate cyclase leading to cAMP formation in the absence of alpha-gustducin. Each TAS1R contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD) and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TAS1R receptors
PVSWALLTALTLLLLLLAGTALLFALNLTTPVVKSAGGRTCFLMLGSLAAASCSLYCHFGEPTWLACLLK
QPLFSLSFTVCLSCIAVRSFQIVCIFKLASKLPRFYETWAKNHGPELFILISSAVQLLISLLWLVLNPPV
PTKDYDRYPDLIVLECSQTLSVGSFLELLYNCLLSISCFVFSYMGKDLPANYNEAKCITFSLLIYFISWI
SFFTTYSIYRGKYLMAINVLAILSSLLGIFGGYFLPKVYIILL
>gnl|CDD|320417 cd15290, 7tmC_TAS1R3, type 1 taste receptor subtype 3, member of the class C of seven-transmembrane G protein-coupled receptors. This group represents TAS1R3, which is a member of the type I taste receptor (TAS1R) family that belongs to the class C of G protein-coupled receptors. The functional TAS1Rs are obligatory heterodimers built from three known members, TAS1R1-3. TAS1R1 combines with TAS1R3 to form an umami taste receptor, which is responsible for the perception of savory taste, such as the food additive mono-sodium glutamate (MSG); whereas the combination of TAS1R2-TAS1R3 forms a sweet-taste receptor for sugars and D-amino acids. On the other hand, the type II taste receptors (TAS2Rs), which belong to the class A family of GPCRs, recognize bitter tasting compounds. In the case of sweet, for example, the TAS1R2-TAS1R3 heterodimer activates phospholipase C (PLC) via alpha-gustducin, a heterodimeric G protein that is involved in perception of sweet and bitter tastes. This activation leads to generation of inositol (1, 4, 5)-trisphosphate (IP3) and diacylglycerol (DAG), and consequently increases intracellular Ca2+ mobilization and activates a cation channel, TRPM5. In contrast to the TAS1R2-TAS1R3 heterodimer, TAS1R3 alone could activate adenylate cyclase leading to cAMP formation in the absence of alpha-gustducin. Each TAS1R contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD) and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TAS1R receptors
PESLGLLLLGVLLLVLQCSVGVLFLKHRGTPLVQASGGPLSIFALLSLMGACLSLLLFLGQPSDVVCRLQ
QPLNALFLTVCLSTILSISLQIFLVTEFPKCAASHLHWLRGPGSWLVVLICCLVQAGLCGWYVQDGPSLS
EYDAKMTLFVEVFLRCPVEPWLGFGLMHGFNGALALISFMCTFMAQKPLKQYNLARDITFSTLIYCVTWV
IFIPIYAGLQVKLRSIAQVGFILLSNLGLLAAYYLPKCYLLLR
>gnl|CDD|320418 cd15291, 7tmC_GABA-B-R1, gamma-aminobutyric acid type B receptor subunit 1, member of the class C family of seven-transmembrane G protein-coupled receptors. The type B receptor for gamma-aminobutyric acid, GABA-B, is activated by its endogenous ligand GABA, the principal inhibitory neurotransmitter. The functional GABA-B receptor is an obligatory heterodimer composed of two related subunits, GABA-B1, which is primarily involved in GABA ligand binding, and GABA-B2, which is responsible for both G-protein coupling and trafficking of the heterodimer to the plasma membrane. Activation of GABA-B couples to G(i/o)-type G proteins, which in turn modulate three major downstream effectors: adenylate cyclase, voltage-sensitive Ca2+ channels, and inwardly-rectifying K+ channels. Consequently, GABA-B receptor produces slow and sustained inhibitory responses by decreased neurotransmitter release via inhibition of Ca2+ channels and by postsynaptic hyperpolarization via the activation of K+ channels through the G-protein beta-gamma dimer. The GABA-B is expressed in both pre- and postsynaptic sites of glutamatergic and GABAergic neurons in the brain where it regulates synaptic activity. Thus, the GABA-B receptor agonist, baclofen, is used to treat muscle tightness and cramping caused by spasticity in multiple sclerosis patients. Moreover, GABA-B antagonists improves cognitive performance in mammals, while GABA-B agonists suppress cognitive behavior. In most of the class C family members, the extracellular Venus-flytrap domain in the N-terminus is connected to the seven-transmembrane (7TM) via a cysteine-rich domain (CRD). However, in the GABA-B receptor, the CRD is absent in both subunits and the Venus-flytrap ligand-binding domain is directly connected to the 7TM via a 10-15 amino acids linker, suggesting that GABA-B receptor may utilize a different activation mechanism
KLFISMCLLASLGIFAAVFLLIFNIYNRHRRYIQLSQPHCNNVMLVGCILCLASVFLLGLDGRHVSRSHF
PLVCQARLWLLCLGFTLAYGSMFTKVWRVHRLTTKKKEKKETRKTLEPWKLYAVVGILLVVDVIILAIWQ
IVDPLHRTIEEFPLEEPKDTDEDVKILPQLEHCSSKKQNTWLGIVYGYKGLLLLFGLFLAYETRNVKVEK
INDSRFVGMSIYNVVVLCLITAPVTMIISSQQDASFAFVSLAILFSSYITLVLIFVPKIRELIR
>gnl|CDD|320419 cd15292, 7tmC_GPR156, orphan GPR156, member of the class C family of seven-transmembrane G protein-coupled receptors. This subgroup represents orphan GPR156 that is closely related to the type B receptor for gamma-aminobutyric acid (GABA-B), which is activated by its endogenous ligand GABA, the principal inhibitory neurotransmitter. The functional GABA-B receptor is an obligatory heterodimer composed of two related subunits, GABA-B1, which is primarily involved in GABA ligand binding, and GABA-B2, which is responsible for both G-protein coupling and trafficking of the heterodimer to the plasma membrane. Activation of GABA-B couples to G(i/o)-type G proteins, which in turn modulate three major downstream effectors: adenylate cyclase, voltage-sensitive Ca2+ channels, and inwardly-rectifying K+ channels. Consequently, GABA-B receptor produces slow and sustained inhibitory responses by decreased neurotransmitter release via inhibition of Ca2+ channels and by postsynaptic hyperpolarization via the activation of K+ channels through the G-protein beta-gamma dimer. The GABA-B is expressed in both pre- and postsynaptic sites of glutamatergic and GABAergic neurons in the brain where it regulates synaptic activity. Thus, the GABA-B receptor agonist, baclofen, is used to treat muscle tightness and cramping caused by spasticity in multiple sclerosis patients. Moreover, GABA-B antagonists improves cognitive performance in mammals, while GABA-B agonists suppress cognitive behavior. In most of the class C family members, the extracellular Venus-flytrap domain in the N-terminus is connected to the seven-transmembrane (7TM) via a cysteine-rich domain (CRD). However, in the GABA-B receptor, the CRD is absent in both subunits and the Venus-flytrap ligand-binding domain is directly connected to the 7TM via a 10-15 amino acids linker, suggesting that GABA-B receptor may utilize a different activation mechanism
VLLGVMWTLLSCGILLALFFLAFTIRFRNNRIVKMSSPNLNVVTLLGSILTYTSGFLFGIQEPGTSMETI
FQVRIWLLCIGTSLVFGPILGKSWRLYRVFTQRVPDKRVIIKDIQLLGLVAGLIFADVLLLLTWVLTDPV
QCARSLSAVIKAMEKGISYSVSRMDFCASLYSDLWIILISGFKGSLLLYGTYLAGLTSNVSSPPVNQSLT
IMVGVNLVTLTAGVVFPVTRFLHSWPNLVYGTTSGGIFVCTTTINCLIFIPQLKQWKQ
>gnl|CDD|320420 cd15293, 7tmC_GPR158-like, orphan GPR158 and similar proteins, member of the class C family of seven-transmembrane G protein-coupled receptors. This group includes orphan receptors GPR158, GPR158-like (also called GPR179) and similar proteins. These orphan receptors are closely related to the type B receptor for gamma-aminobutyric acid (GABA-B), which is activated by its endogenous ligand GABA, the principal inhibitory neurotransmitter. The functional GABA-B receptor is an obligatory heterodimer composed of two related subunits, GABA-B1, which is primarily involved in GABA ligand binding, and GABA-B2, which is responsible for both G-protein coupling and trafficking of the heterodimer to the plasma membrane. Activation of GABA-B couples to G(i/o)-type G proteins, which in turn modulate three major downstream effectors: adenylate cyclase, voltage-sensitive Ca2+ channels, and inwardly-rectifying K+ channels. Consequently, GABA-B receptor produces slow and sustained inhibitory responses by decreased neurotransmitter release via inhibition of Ca2+ channels and by postsynaptic hyperpolarization via the activation of K+ channels through the G-protein beta-gamma dimer. The GABA-B is expressed in both pre- and postsynaptic sites of glutamatergic and GABAergic neurons in the brain where it regulates synaptic activity. Thus, the GABA-B receptor agonist, baclofen, is used to treat muscle tightness and cramping caused by spasticity in multiple sclerosis patients. Moreover, GABA-B antagonists improves cognitive performance in mammals, while GABA-B agonists suppress cognitive behavior. In most of the class C family members, the extracellular Venus-flytrap domain in the N-terminus is connected to the seven-transmembrane (7TM) via a cysteine-rich domain (CRD). However, in the GABA-B receptor, the CRD is absent in both subunits and the Venus-flytrap ligand-binding domain is directly connected to the 7TM via a 10-15 amino acids linker, suggesting that GABA-B receptor may utilize a different activation mechanism
VLRIAVLAVQAICILLCLVLALVVFRFRKVKVIKAASPILLELILFGALLLYFPVFILYFEPSVFRCILR
PWFRHLGFAIVYGALILKTYRILVVFRSRSARRVHLTDRDLLKRLGLIVLVVLGYLAAWTAVNPPNVEVG
LTLTSSGLKFNVCSLDWWDYVMAIAELLFLLWGVYLCYAVRKAPSAFNESRYISLAIYNELLLSVIFNII
RFFLLPSLHPDLLFLLFFLHTQLTVTVTLLLIFGPKFYLVLR
>gnl|CDD|320421 cd15294, 7tmC_GABA-B-R2, gamma-aminobutyric acid type B receptor subunit 2, member of the class C family of seven-transmembrane G protein-coupled receptors. The type B receptor for gamma-aminobutyric acid, GABA-B, is activated by its endogenous ligand GABA, the principal inhibitory neurotransmitter. The functional GABA-B receptor is an obligatory heterodimer composed of two related subunits, GABA-B1, which is primarily involved in GABA ligand binding, and GABA-B2, which is responsible for both G-protein coupling and trafficking of the heterodimer to the plasma membrane. Activation of GABA-B couples to G(i/o)-type G proteins, which in turn modulate three major downstream effectors: adenylate cyclase, voltage-sensitive Ca2+ channels, and inwardly-rectifying K+ channels. Consequently, GABA-B receptor produces slow and sustained inhibitory responses by decreased neurotransmitter release via inhibition of Ca2+ channels and by postsynaptic hyperpolarization via the activation of K+ channels through the G-protein beta-gamma dimer. The GABA-B is expressed in both pre- and postsynaptic sites of glutamatergic and GABAergic neurons in the brain where it regulates synaptic activity. Thus, the GABA-B receptor agonist, baclofen, is used to treat muscle tightness and cramping caused by spasticity in multiple sclerosis patients. Moreover, GABA-B antagonists improves cognitive performance in mammals, while GABA-B agonists suppress cognitive behavior. In most of the class C family members, the extracellular Venus-flytrap domain in the N-terminus is connected to the seven-transmembrane (7TM) via a cysteine-rich domain (CRD). However, in the GABA-B receptor, the CRD is absent in both subunits and the Venus-flytrap ligand-binding domain is directly connected to the 7TM via a 10-15 amino acids linker, suggesting that GABA-B receptor may utilize a different activation mechanism
PLYSILSSLTIIGIILASAFLAFNIKFRNHRYIKMSSPYMNNLIILGCMLTYASVILLGLDGSLVSEKTF
ETLCTARTWILCVGFTLAFGAMFSKTWRVHSIFTNVKLNKKAIKDYKLFIIVGVLLLIDICILITWQIVD
PFYRTVKELEPEPDPAGDDILIRPELEYCESTHMTIFLGIIYAYKGLLMVFGCFLAWETRNVSIPALNDS
KYIGMSVYNVVIMCVIGAAVSFILRDQPNVQFCIISLFIIFCTTITLCLVFVPKLIELRR
>gnl|CDD|320422 cd15295, 7tmA_Histamine_H4R, histamine receptor subtype H4R, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes histamine subtype H4R, a member of the histamine receptor family, which belong to the class A of GPCRs. Histamine plays a key role as chemical mediator and neurotransmitter in various physiological and pathophysiological processes in the central and peripheral nervous system. Histamine exerts its functions by binding to four different G protein-coupled receptors (H1-H4). The H3 and H4 receptors couple to the G(i)-proteins, which leading to the inhibition of cAMP formation. The H3R receptor functions as a presynaptic autoreceptors controlling histamine release and synthesis. The H4R plays an important role in histamine-mediated chemotaxis in mast cells and eosinophils. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VVLLFLMSLLALVIVLGNALVIIAFVVDKNLRHRSNYFFLNLAISDFFVGAISIPLYIPYTLTNRWDFGR
GLCVFWLVIDYLLCTASVYNIVLISYDRYQSVSNAVSYRNQQTATLRIVTQMVAVWVLAFLVHGPAILVS
DSWKTEDGECEPEFFSNWYILAITSVLEFLVPVILVAYFNTQIYWSLWKRLRDRKLAKSLAIILGTFAIC
WAPYSLFTIIRAACEKHRGSPWYNFAFWLQWFNSFINPFLYPLCHKRFRKAFLKIFC
>gnl|CDD|320423 cd15296, 7tmA_Histamine_H3R, histamine receptor subtypes H3R and H3R-like, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes histamine subtypes H3R and H3R-like, members of the histamine receptor family, which belong to the class A of GPCRs. Histamine plays a key role as chemical mediator and neurotransmitter in various physiological and pathophysiological processes in the central and peripheral nervous system. Histamine exerts its functions by binding to four different G protein-coupled receptors (H1-H4). The H3 and H4 receptors couple to the G(i)-proteins, which leading to the inhibition of cAMP formation. The H3R receptor functions as a presynaptic autoreceptors controlling histamine release and synthesis. The H4R plays an important role in histamine-mediated chemotaxis in mast cells and eosinophils. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VILAVLMALLVVATVLGNALVILAFVVDSSLRTQGNFFFLNLAISDFLVGGFCIPLYIPYVLTGRWKFGR
GLCKLWLVVDYLLCTASVFNIVLISYDRFLSVTRAVSYRAQKGMTRQAVLKMVLVWVLAFLLYGPAIISW
EYIAGGSIIPEGECYAEFFYNWYFLMTASTLEFFTPFISVTYFNLSIYLNIQKRRFRLSRDKKVAKSLAI
IVCVFGLCWAPYTLLMIIRAACHGHCVPDYWYETSFWLLWVNSAINPVLYPLCHMSFRRAF
>gnl|CDD|320424 cd15297, 7tmA_mAChR_M2, muscarinic acetylcholine receptor subtype M2, member of the class A family of seven-transmembrane G protein-coupled receptors. Muscarinic acetylcholine receptors (mAChRs) regulate the activity of many fundamental central and peripheral functions. The mAChR family consists of 5 subtypes M1-M5, which can be further divided into two major groups according to their G-protein coupling preference. The M1, M3 and M5 receptors selectively interact with G proteins of the G(q/11) family, whereas the M2 and M4 receptors preferentially link to the G(i/o) types of G proteins. Activation of M2 receptor causes a decrease in cAMP production, generally leading to inhibitory-type effects. This causes an outward current of potassium in the heart, resulting in a decreased heart rate. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VFIVLVAGSLSLVTIIGNILVMVSIKVNRHLQTVNNYFLFSLACADLIIGVFSMNLYTLYTVIGYWPLGP
VVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPVKRTTKMAGMMIAAAWVLSFILWAPAILFWQ
FIVGGRTVPEGECYIQFFSNAAVTFGTAIAAFYLPVIIMTVLYWQISRASSREKKVTRTILAILLAFIIT
WTPYNVMVLINTFCASCIPNTVWTIGYWLCYINSTINPACYALCNATFKKTF
>gnl|CDD|341344 cd15298, 7tmA_mAChR_M4, muscarinic acetylcholine receptor subtype M4, member of the class A family of seven-transmembrane G protein-coupled receptors. Muscarinic acetylcholine receptors (mAChRs) regulate the activity of many fundamental central and peripheral functions. The mAChR family consists of 5 subtypes M1-M5, which can be further divided into two major groups according to their G-protein coupling preference. The M1, M3 and M5 receptors selectively interact with G proteins of the G(q/11) family, whereas the M2 and M4 receptors preferentially link to G(i/o) types of G proteins. The M4 receptor is mainly found in the CNS and function as an inhibitory autoreceptor regulating acetycholine release. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VFIATVTGSLSLVTVVGNILVMLSIKVNRQLQTVNNYFLFSLACADLIIGAFSMNLYTVYIIKGYWPLGA
VVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPARRTTKMAGLMIAAAWVLSFVLWAPAILFWQ
FVVGKRTVPDNQCFIQFLSNPAVTFGTAIAAFYLPVVIMTVLYIHISLASARERKVTRTIFAILLAFILT
WTPYNVMVLVNTFCQSCIPDTVWSIGYWLCYVNSTINPACYALCNATFKKTF
>gnl|CDD|320426 cd15299, 7tmA_mAChR_M3, muscarinic acetylcholine receptor subtype M3, member of the class A family of seven-transmembrane G protein-coupled receptors. Muscarinic acetylcholine receptors (mAChRs) regulate the activity of many fundamental central and peripheral functions. The mAChR family consists of 5 subtypes M1-M5, which can be further divided into two major groups according to their G-protein coupling preference. The M1, M3 and M5 receptors selectively interact with G proteins of the G(q/11) family, whereas the M2 and M4 receptors preferentially link to the G(i/o) types of G proteins. The M3 receptor is mainly located in smooth muscle, exocrine glands and vascular endothelium. It induces vomiting in the central nervous system and is a critical regulator of glucose homeostasis by modulating insulin secretion. Generally, M3 receptor causes contraction of smooth muscle resulting in vasoconstriction and increased glandular secretion. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
WQVVLIAFLTGILALVTIIGNILVIVSFKVNKQLKTVNNYFLLSLACADLIIGVISMNLFTTYIIMNRWA
LGNLACDLWLSIDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTTKRAGVMIGLAWVISFVLWAPAIL
FWQYFVGKRTVPPDECFIQFLSEPIITFGTAIAAFYLPVTIMTILYWRIYKETIKEKKAAQTLSAILLAF
IITWTPYNIMVLVNTFCDSCIPKTYWNLGYWLCYINSTVNPVCYALCNKTFRTTFKMLLLCQCD
>gnl|CDD|320427 cd15300, 7tmA_mAChR_M5, muscarinic acetylcholine receptor subtype M5, member of the class A family of seven-transmembrane G protein-coupled receptors. Muscarinic acetylcholine receptors (mAChRs) regulate the activity of many fundamental central and peripheral functions. The mAChR family consists of 5 subtypes M1-M5, which can be further divided into two major groups according to their G-protein coupling preference. The M1, M3 and M5 receptors selectively interact with G proteins of the G(q/11) family, whereas the M2 and M4 receptors preferentially link to the G(i/o) types of G proteins. M5 mAChR is primarily found in the central nervous system and mediates acetylcholine-induced dilation of cerebral blood vessels. Activation of M5 receptor triggers a variety of cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides, and modulation of potassium channels. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
ITIAAVTAVVSLITIVGNVLVMISFKVNSQLKTVNNYYLLSLACADLIIGIFSMNLYTSYILMGYWALGS
LACDLWLALDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTPKRAGIMIGLAWLISFILWAPPILCWQ
YFVGKRTVPERECQIQFLSEPTITFGTAIAAFYIPVSVMTILYCRIYKETIKERKAAQTLSAILLAFIIT
WTPYNIMVLVSTFCSDCIPLTLWHLGYWLCYVNSTVNPMCYALCNKTFRKTF
>gnl|CDD|320428 cd15301, 7tmA_mAChR_DM1-like, muscarinic acetylcholine receptor DM1, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup includes muscarinic acetylcholine receptor DM1-like from invertebrates. Muscarinic acetylcholine receptors (mAChRs) regulate the activity of many fundamental central and peripheral functions. The mAChR family consists of 5 subtypes M1-M5, which can be further divided into two major groups according to their G-protein coupling preference. The M1, M3 and M5 receptors selectively interact with G proteins of the G(q/11) family, whereas the M2 and M4 receptors preferentially link to the G(i/o) types of G proteins. Activation of mAChRs by agonist (acetylcholine) leads to a variety of biochemical and electrophysiological responses. In general, the exact nature of these responses and the subsequent physiological effects mainly depend on the molecular and pharmacological identity of the activated receptor subtype(s). All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VLIVIVAAVLSLVTVGGNVMVMISFKIDKQLQTISNYFLFSLAVADFAIGVISMPLFTVYTALGYWPLGY
EVCDTWLAIDYLASNASVLNLLIISFDRYFSVTRPLTYRARRTTKKAAVMIASAWIISLLLWPPWIYSWP
YIEGKRTVPAGTCYIQFLETNPYVTFGTALAAFYVPVTIMCILYWRIWRETKKRQKKQESKAAKTLSAIL
LAFIVTWTPYNVLVLIKAFFPCSDTIPTELWDFSYYLCYINSTINPLCYALCNAAFRRTY
>gnl|CDD|320429 cd15302, 7tmA_mAChR_GAR-2-like, muscarinic acetylcholine receptor GAR-2 and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. Muscarinic acetylcholine receptors (mAChRs) regulate the activity of many fundamental central and peripheral functions. The mAChR family consists of 5 subtypes M1-M5, which can be further divided into two major groups according to their G-protein coupling preference. The M1, M3 and M5 receptors selectively interact with G proteins of the G(q/11) family, whereas the M2 and M4 receptors preferentially link to the G(i/o) types of G proteins. Activation of mAChRs by agonist (acetylcholine) leads to a variety of biochemical and electrophysiological responses. In general, the exact nature of these responses and the subsequent physiological effects mainly depend on the molecular and pharmacological identity of the activated receptor subtype(s). All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
ILLALITAILSIITVIGNILVLLSFYVDRNIRQPSNYFIASLAVSDLLIGLESMPFYTVYVLNGDYWPLG
WVLCDLWLSVDYTVCLVSIYTVLLITIDRYCSVKIPAKYRNWRTPRKVLLIIAITWIIPALLFFISIFGW
QYFTGQGRSLPEGECYVQFMTDPYFNMGMYIGYYWTTLIVMLILYAGIYRAANRARKALRTITFILGAFV
ICWTPYHILATIYGFCEAPPCVNETLYTISYYLCYMNSPINPFCYALANQQFKKTF
>gnl|CDD|341345 cd15304, 7tmA_5-HT2A, serotonin receptor subtype 2A, member of the class A family of seven-transmembrane G protein-coupled receptors. The 5-HT2 receptors are a subfamily of serotonin receptors that bind the neurotransmitter serotonin (5HT; 5-hydroxytryptamine) in the central nervous system (CNS). The 5-HT2 subfamily is composed of three subtypes that mediate excitatory neurotransmission: 5-HT2A, 5-HT2B, and 5-HT2C. They are selectively linked to G proteins of the G(q/11) family and activate phospholipase C, which leads to activation of protein kinase C and calcium release. In the CNS, serotonin is involved in the regulation of appetite, mood, sleep, cognition, learning and memory, as well as implicated in diseases such as migraine, schizophrenia, and depression. Indeed, 5-HT2 receptors are attractive targets for a variety of psychoactive drugs, ranging from atypical antipsychotic drugs, antidepressants, and anxiolytics, which have an antagonistic action on 5-HT2 receptors, to hallucinogens, which act as agonists at postsynaptic 5-HT2 receptors. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
NWPALLTVIVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLP
SKLCAVWIYLDVLFSTASIMHLCAISLDRYIAIRNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFG
LQDDSKVFKEGSCLLADENFVLIGSFVAFFIPLTIMVITYFLTIKSLQQSISNEQKASKVLGIVFFLFVV
MWCPFFITNVMAVICKESCNEVVIGGLLNVFVWIGYLSSAVNPLVYTLFNKTYRSAF
>gnl|CDD|341346 cd15305, 7tmA_5-HT2C, serotonin receptor subtype 2C, member of the class A family of seven-transmembrane G protein-coupled receptors. The 5-HT2 receptors are a subfamily of serotonin receptors that bind the neurotransmitter serotonin (5HT; 5-hydroxytryptamine) in the central nervous system (CNS). The 5-HT2 subfamily is composed of three subtypes that mediate excitatory neurotransmission: 5-HT2A, 5-HT2B, and 5-HT2C. They are selectively linked to G proteins of the G(q/11) family and activate phospholipase C, which leads to activation of protein kinase C and calcium release. In the CNS, serotonin is involved in the regulation of appetite, mood, sleep, cognition, learning and memory, as well as implicated in diseases such as migraine, schizophrenia, and depression. Indeed, 5-HT2 receptors are attractive targets for a variety of psychoactive drugs, ranging from atypical antipsychotic drugs, antidepressants, and anxiolytics, which have an antagonistic action on 5-HT2 receptors, to hallucinogens, which act as agonists at postsynaptic 5-HT2 receptors. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
NWPALLILIIIILTIGGNILVIMAVSLEKKLQNATNFFLMSLAVADMLVGILVMPVSLIAILYDYAWPLP
RYLCPIWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAMMKIAAVWTISIGISMPIPVIG
LQDDEKVFVNGTCVLNDENFVLIGSFVAFFIPLIIMVITYCLTIQVLQRQQAINNERRASKVLGIVFFLF
LIMWCPFFITNILSVLCKEACDQKLMEELLNVFVWVGYVSSGINPLVYTLFNKTYRRAFSNYIRC
>gnl|CDD|341347 cd15306, 7tmA_5-HT2B, serotonin receptor subtype 2B, member of the class A family of seven-transmembrane G protein-coupled receptors. The 5-HT2 receptors are a subfamily of serotonin receptors that bind the neurotransmitter serotonin (5HT; 5-hydroxytryptamine) in the central nervous system (CNS). The 5-HT2 subfamily is composed of three subtypes that mediate excitatory neurotransmission: 5-HT2A, 5-HT2B, and 5-HT2C. They are selectively linked to G proteins of the G(q/11) family and activate phospholipase C, which leads to activation of protein kinase C and calcium release. In the CNS, serotonin is involved in the regulation of appetite, mood, sleep, cognition, learning and memory, as well as implicated in diseases such as migraine, schizophrenia, and depression. Indeed, 5-HT2 receptors are attractive targets for a variety of psychoactive drugs, ranging from atypical antipsychotic drugs, antidepressants, and anxiolytics, which have an antagonistic action on 5-HT2 receptors, to hallucinogens, which act as agonists at postsynaptic 5-HT2 receptors. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
HWAALLILMVIIPTIGGNILVILAVSLEKKLQYATNYFLMSLAVADLLVGLFVMPIALLTILFEAMWPLP
LVLCPIWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQASQYNSRATAFIKITVVWLISIGIAIPVPIKG
IETDVDNPNNITCVLTKERFGDFILFGSLAAFFTPLAIMIVTYFLTIHALRKQTITNEQRASKVLGIVFF
LFLLMWCPFFITNITSVLCDSCNQTTLQMLMEIFVWIGYVSSGVNPLVYTLFNKTFRDAFGRYITCN
>gnl|CDD|320433 cd15307, 7tmA_5-HT2_insect-like, serotonin receptor subtype 2 from insects, member of the class A family of seven-transmembrane G protein-coupled receptors. The 5-HT2 receptors are a subfamily of serotonin receptors that bind the neurotransmitter serotonin (5HT; 5-hydroxytryptamine) in the central nervous system (CNS). The 5-HT2 subfamily is composed of three subtypes that mediate excitatory neurotransmission: 5-HT2A, 5-HT2B, and 5-HT2C. They are selectively linked to G proteins of the G(q/11) family and activate phospholipase C, which leads to activation of protein kinase C and calcium release. In the CNS, serotonin is involved in the regulation of appetite, mood, sleep, cognition, learning and memory, as well as implicated in diseases such as migraine, schizophrenia, and depression. Indeed, 5-HT2 receptors are attractive targets for a variety of psychoactive drugs, ranging from atypical antipsychotic drugs, antidepressants, and anxiolytics, which have an antagonistic action on 5-HT2 receptors, to hallucinogens, which act as agonists at postsynaptic 5-HT2 receptors. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
NYWALLALVLVLGTAAGNILVCLAIAWERRLQNVTNYFLMSLAITDLMVAVLVMPLGILTLVKGHFPLSS
EHCLTWICLDVLFCTASIMHLCTISVDRYLSLRYPMRFGRNKTRRRVTLKIVFVWLLSIAMSLPLSLMYS
KDHASVLVNGTCQIPDPVYKLVGSIVCFYIPLGVMLLTYCLTVRLLARQRSRHGRIIRLEQKATKVLGVV
FFTFVILWSPFFVLNLLPTVCAECEERISHWVFDVVTWLGYASSMVNPIFYTIFNKVFRQAFKKVLLCR
>gnl|CDD|320434 cd15308, 7tmA_D4_dopamine_R, D4 dopamine receptor of the D2-like family, member of the class A family of seven-transmembrane G protein-coupled receptors. Dopamine receptors are members of the class A G protein-coupled receptors that are involved in many neurological processes in the central nervous system (CNS). The neurotransmitter dopamine is the primary endogenous agonist for dopamine receptors. Dopamine receptors consist of at least five subtypes: D1, D2, D3, D4, and D5. The D1 and D5 subtypes are members of the D1-like family of dopamine receptors, whereas the D2, D3 and D4 subtypes are members of the D2-like family. Activation of D2-like family receptors is linked to G proteins of the G(i) family. This leads to a decrease in adenylate cyclase activity, thereby decreasing cAMP levels. Dopamine receptors are major therapeutic targets for neurological and psychiatric disorders such as drug abuse, depression, schizophrenia, or Parkinson's disease
AAALVGGVLLILAIIAGNVLVCLSVCTERALKTTTNYFIVSLAVADLLLALLVLPLYVYSEFQGGVWTLS
PVLCDALMTMDVMLCTASIFNLCAISVDRFIAVSVPLNYNRRQGSVRQLLLISATWILSFAVASPVIFGL
NNVPNRDPAVCKLEDNNYVVYSSVCSFFIPCPVMLVLYCAMFRGLGRERKAMRVLPVVVGAFLFCWTPFF
VVHITRALCESCSIPPQLISIVTWLGYVNSALNPVIYTVFNAEFRNVF
>gnl|CDD|320435 cd15309, 7tmA_D2_dopamine_R, D2 subtype of the D2-like family of dopamine receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Dopamine receptors are members of the class A G protein-coupled receptors that are involved in many neurological processes in the central nervous system (CNS). The neurotransmitter dopamine is the primary endogenous agonist for dopamine receptors. Dopamine receptors consist of at least five subtypes: D1, D2, D3, D4, and D5. The D1 and D5 subtypes are members of the D1-like family of dopamine receptors, whereas the D2, D3 and D4 subtypes are members of the D2-like family. Activation of D2-like family receptors is linked to G proteins of the G(i) family. This leads to a decrease in adenylate cyclase activity, thereby decreasing cAMP levels. Dopamine receptors are major therapeutic targets for neurological and psychiatric disorders such as drug abuse, depression, schizophrenia, or Parkinson's disease
NYYAMLLTLLIFVIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWRFSR
IHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMISVVWVLSFAISCPLLFGL
NNTDQNECIIANPAFVVYSSIVSFYVPFIVTLLVYVQIYIVLQKEKKATQMLAIVLGVFIICWLPFFITH
ILNMHCDCNIPPALYSAFTWLGYVNSAVNPIIYTTFNIEFRKAF
>gnl|CDD|320436 cd15310, 7tmA_D3_dopamine_R, D3 subtype of the D2-like family of dopamine receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Dopamine receptors are members of the class A G protein-coupled receptors that are involved in many neurological processes in the central nervous system (CNS). The neurotransmitter dopamine is the primary endogenous agonist for dopamine receptors. Dopamine receptors consist of at least five subtypes: D1, D2, D3, D4, and D5. The D1 and D5 subtypes are members of the D1-like family of dopamine receptors, whereas the D2, D3 and D4 subtypes are members of the D2-like family. Activation of D2-like family receptors is linked to G proteins of the G(i) family. This leads to a decrease in adenylate cyclase activity, thereby decreasing cAMP levels. Dopamine receptors are major therapeutic targets for neurological and psychiatric disorders such as drug abuse, depression, schizophrenia, or Parkinson's disease
AYYALSYCALILAIVFGNVLVCMAVLRERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFS
RICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVSLMITAVWVLAFAVSCPLL
FGFNTTGDPTVCSISNPDFVIYSSVVSFYLPFGVTLLVYVRIYVVLLREKKATQMLAIVLGAFIVCWLPF
FLTHILNTHCQACHVPPELYSATTWLGYVNSALNPVIYTTFNIEFRRAF
>gnl|CDD|320437 cd15312, 7tmA_TAAR2_3_4, trace amine-associated receptors 2, 3, 4, and similar receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. TAAR2, TAAR3, and TAAR4 are among the 15 identified trace amine-associated receptor subtypes, which form a distinct subfamily within the class A G protein-coupled receptor family. Trace amines are endogenous amines of unknown function that have strong structural and metabolic similarity to classical monoamine neurotransmitters (serotonin, noradrenaline, adrenaline, dopamine, and histamine), which play critical roles in human and animal physiological activities such as cognition, consciousness, mood, motivation, perception, and autonomic responses. However, trace amines are found in the mammalian brain at very low concentrations compared to classical monoamines. Trace amines, including p-tyramine, beta-phenylethylamine, and tryptamine, are also thought to act as chemical messengers to exert their biological effects in vertebrates. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VAMYLFMAGAILLTVFGNLMVIISISHFKQLHSPTNFLILSLAITDFLLGFLVMPYSMVRSVESCWYFGD
LFCKIHSSLDMMLSTTSIFHLCFIAVDRYYAVCDPLHYRTKITTPVIKVFLVISWSVPCLFAFGVVFSEV
NLEGIEDYVALVSCTGSCVLIFNKLWGVIASLIAFFIPGTVMIGIYIKIFFVARKHAKVINNRPSVTKGD
SKNKLSKKKERKAAKTLSIVMGVFLLCWLPFFVATLIDPFLNFSTPVDLFDALVWLGYFNSTCNPLIYGF
FYPWFQKAF
>gnl|CDD|320438 cd15314, 7tmA_TAAR1, trace amine-associated receptor 1 and similar receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. The trace amine-associated receptor 1 (TAAR1) is one of the 15 identified trace amine-associated receptor subtypes, which form a distinct subfamily within the class A G protein-coupled receptor family. Trace amines are endogenous amines of unknown function that have strong structural and metabolic similarity to classical monoamine neurotransmitters (serotonin, noradrenaline, adrenaline, dopamine, and histamine), which play critical roles in human and animal physiological activities such as cognition, consciousness, mood, motivation, perception, and autonomic responses. However, trace amines are found in the mammalian brain at very low concentrations compared to classical monoamines. TAAR1 is coupled to the Gs protein, which leads to activation of adenylate cyclase, and is thought to play functional role in the regulation of brain monoamines. TAAR1 is also shown to be activated by psychoactive compounds such as Ecstasy (MDMA), amphetamine and LSD. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VLLYIFLGLISLVTVCGNLLVIISIAHFKQLHTPTNYLILSLAVADLLVGGLVMPPSMVRSVETCWYFGD
LFCKIHSSFDITLCTASILNLCFISIDRYYAVCQPLLYRSKITVRVVLVMILISWSVSALVGFGIIFLEL
NIKGIYYNHVACEGGCLVFFSKVSSVVGSVFSFYIPAVIMLCIYLKIFLVAQRQARSIQSARTKSGASSS
KMERKATKTLAIVMGVFLLCWTPFFLCNIIDPFINYSIPPVLIEVLNWLGYSNSTLNPFIYAFFYSWFRK
AF
>gnl|CDD|320439 cd15316, 7tmA_TAAR6_8_9, trace amine-associated receptors 6, 8, and 9, member of the class A family of seven-transmembrane G protein-coupled receptors. Included in this group are mammalian TAAR6, TAAR8, TAAR9, and similar proteins. They are among the 15 identified amine-associated receptors (TAARs), a distinct subfamily within the class A G protein-coupled receptors. Trace amines are endogenous amines of unknown function that have strong structural and metabolic similarity to classical monoamine neurotransmitters (serotonin, noradrenaline, adrenaline, dopamine, and histamine), which play critical roles in human and animal physiological activities such as cognition, consciousness, mood, motivation, perception, and autonomic responses. However, trace amines are found in the mammalian brain at very low concentrations compared to classical monoamines. Trace amines, including p-tyramine, beta-phenylethylamine, and tryptamine, are also thought to act as chemical messengers to exert their biological effects in vertebrates. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VILYIVLGFGAVLAVFGNLLVMISILHFKQLHSPTNFLIASLACADFLVGVTVMPFSTVRSVESCWYFGE
SFCTFHTCCDVSFCYASLFHLCFISVDRYIAVTDPLVYPTKFTVSVSGICISVSWIFSLTYSFSVFYTGV
NDDGLEELVNALNCVGGCQIILNQNWVLVDFLLFFIPTFAMIILYGKIFLVAKQQARKIEMTSSKAESSS
ESYKDRVARRERKAAKTLGITVIAFLVSWLPYLIDVLIDAFMNFITPPYIYEICCWCAYYNSAMNPLIYA
LFYPWFRKAI
>gnl|CDD|320440 cd15317, 7tmA_TAAR5-like, trace amine-associated receptor 5 and similar receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Included in this group are mammalian TAAR5, TAAR6, TAAR8, TAAR9, and similar proteins. They are among the 15 identified trace amine-associated receptors (TAARs), a distinct subfamily within the class A G protein-coupled receptors. Trace amines are endogenous amines of unknown function that have strong structural and metabolic similarity to classical monoamine neurotransmitters (serotonin, noradrenaline, adrenaline, dopamine, and histamine), which play critical roles in human and animal physiological activities such as cognition, consciousness, mood, motivation, perception, and autonomic responses. However, trace amines are found in the mammalian brain at very low concentrations compared to classical monoamines. Trace amines, including p-tyramine, beta-phenylethylamine, and tryptamine, are also thought to act as chemical messengers to exert their biological effects in vertebrates. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VIIYIVLVLAMLITVSGNLVVIISISHFKQLHSPTNMLVLSLATADFLLGLCVMPFSMIRTVETCWYFGD
LFCKFHTGLDLLLCTTSIFHLCFIAIDRYYAVCDPLRYPSKITVQVAWRFIAIGWLVPGIYTFGLIYTGA
NDEGLEEYSSEISCVGGCQLLFNKIWVLLDFLTFFIPCLIMIGLYAKIFLVARRQARKIQNMEDKFRSSE
ENSSKASASRERKAAKTLAIVMGIFLFCWLPYFIDTIVDEYSNFITPAIVFDAVIWLGYFNSAFNPFIYA
FFYPWFRKAF
>gnl|CDD|320441 cd15318, 7tmA_TAAR5, trace amine-associated receptor 5, member of the class A family of seven-transmembrane G protein-coupled receptors. The trace amine-associated receptor 5 is one of the 15 identified amine-activated G protein-coupled receptors (TAARs), a distinct subfamily within the class A G protein-coupled receptors. Trace amines are endogenous amines of unknown function that have strong structural and metabolic similarity to classical monoamine neurotransmitters (serotonin, noradrenaline, adrenaline, dopamine, and histamine), which play critical roles in human and animal physiological activities such as cognition, consciousness, mood, motivation, perception, and autonomic responses. However, trace amines are found in the mammalian brain at very low concentrations compared to classical monoamines. Trace amines, including p-tyramine, beta-phenylethylamine, and tryptamine, are also thought to act as chemical messengers to exert their biological effects in vertebrates. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
LVIYLACAIGMLIIVLGNLFVVVTVSHFKALHTPTNFLLLSLALADMLLGLTVLPFSTIRSVESCWYFGD
SFCRLHTCLDTLFCLTSIFHLCFISIDRHCAICDPLLYPSKFTIRVACIFIAAGWLVPTVYTSVFLYTKA
VEEGLAELLTSVPCVGSCQLLYNKLWGWLNFPVFFIPCLIMIGLYVKIFIVAKRQARAIASLLSDTNGAS
KRERKAAKTLGIAVGVYLLCWLPFTIDTMVDSLLNFITPPLLFDIIIWFAYFNSACNPLIYVFSYPWFRK
AL
>gnl|CDD|320442 cd15319, 7tmA_D1B_dopamine_R, D1B (or D5) subtype dopamine receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Dopamine receptors are members of the class A G protein-coupled receptors that are involved in many neurological processes in the central nervous system (CNS). The neurotransmitter dopamine is the primary endogenous agonist for dopamine receptors. Dopamine receptors consist of at least five subtypes: D1, D2, D3, D4, and D5. The D1 and D5 subtypes are members of the D1-like family of dopamine receptors, whereas the D2, D3 and D4 subtypes are members of the D2-like family. The D1-like family receptors are coupled to G proteins of the G(s) family, which activate adenylate cyclase, causing cAMP formation and activation of protein kinase A. Dopamine receptors are major therapeutic targets for neurological and psychiatric disorders such as drug abuse, depression, schizophrenia, or Parkinson's disease
VVTGCLLSLLILWTLLGNILVCAAVVRFRHLRSKVTNIFIVSLAVSDLFVALLVMPWKAVAEVAGYWPFG
AFCDVWVAFDIMCSTASILNLCVISVDRYWAISSPFRYERKMTQRVALVMISVAWTLSVLISFIPVQLNW
HKDSGDDWVGLHNSSISRQVEENCDSSLNRTYAISSSLISFYIPVAIMIVTYTRIYRIAQIQIRRISSLE
RAAEHAQSCRSNRIDCHHHTSLRTSIKKETKVLKTLSVIMGVFVCCWLPFFILNCMVPFCDRPPADPDAG
LPCVSETTFDVFVWFGWANSSLNPIIYAFNADFRKVF
>gnl|CDD|320443 cd15320, 7tmA_D1A_dopamine_R, D1A (or D1) subtype dopamine receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Dopamine receptors are members of the class A G protein-coupled receptors that are involved in many neurological processes in the central nervous system (CNS). The neurotransmitter dopamine is the primary endogenous agonist for dopamine receptors. Dopamine receptors consist of at least five subtypes: D1, D2, D3, D4, and D5. The D1 and D5 subtypes are members of the D1-like family of dopamine receptors, whereas the D2, D3 and D4 subtypes are members of the D2-like family. The D1-like family receptors are coupled to G proteins of the G(s) family, which activate adenylate cyclase, causing cAMP formation and activation of protein kinase A. Dopamine receptors are major therapeutic targets for neurological and psychiatric disorders such as drug abuse, depression, schizophrenia, or Parkinson's disease
RVLTGCFLSVLILSTLLGNTLVCAAVIRFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVAEIAGFWPF
GSFCNIWVAFDIMCSTASILNLCVISVDRYWAISSPFRYERKMTPKVAFIMISVAWTLSVLISFIPVQLN
WHKAKPTSFLDLNASLRDLTMDNCDSSLNRTYAISSSLISFYIPVAIMIVTYTRIYRIAQKQIRRISALE
RAAVHAKNCQNSTGNRGSGDCQQPESSFKMSFKRETKVLKTLSVIMGVFVCCWLPFFILNCMVPFCKPTS
TEPFCISSTTFDVFVWFGWANSSLNPIIYAFNADFRKAF
>gnl|CDD|320444 cd15321, 7tmA_alpha2B_AR, alpha-2 adrenergic receptors subtype B, member of the class A family of seven-transmembrane G protein-coupled receptors. The alpha-2 adrenergic receptors (or adrenoceptors) are a subfamily of the class A rhodopsin-like GPCRs that share a common architecture of seven transmembrane helices. This subfamily consists of three highly homologous receptor subtypes that have a key role in neurotransmitter release: alpha-2A, alpha-2B, and alpha-2C. In addition, a fourth subtype, alpha-2D is present in ray-finned fishes and amphibians, but is not found in humans. The alpha-2 receptors are found in both central and peripheral nervous system and serve to produce inhibitory functions through the G(i) proteins. Thus, the alpha-2 receptors inhibit adenylate cyclase, which decreases cAMP production and thereby decreases calcium influx during the action potential. Consequently, lowered levels of calcium will lead to a decrease in neurotransmitter release by negative feedback
YSVQATAAIAAAITFLILFTIFGNVLVIIAVLTSRSLRAPQNLFLVSLAAADILVATLIIPFSLANELMG
YWYFRKTWCEIYLALDVLFCTSSIVHLCAISLDRYWSVSRAIEYNSKRTPRRIKCIILIVWLIAAVISLP
PLIYKGKQKDEQGGLPQCKLNEEAWYILSSSIGSFFAPCLIMILVYLRIYLIAKNREKRFTFVLAVVIGV
FVLCWFPFFFSYSLGAICPELCKVPHSLFQFFFWIGYCNSSLNPVIYTIFNQDFRRAF
>gnl|CDD|320445 cd15322, 7tmA_alpha2A_AR, alpha-2 adrenergic receptors subtype A, member of the class A family of seven-transmembrane G protein-coupled receptors. The alpha-2 adrenergic receptors (or adrenoceptors) are a subfamily of the class A rhodopsin-like GPCRs that share a common architecture of seven transmembrane helices. This subfamily consists of three highly homologous receptor subtypes that have a key role in neurotransmitter release: alpha-2A, alpha-2B, and alpha-2C. In addition, a fourth subtype, alpha-2D is present in ray-finned fishes and amphibians, but is not found in humans. The alpha-2 receptors are found in both central and peripheral nervous system and serve to produce inhibitory functions through the G(i) proteins. Thus, the alpha-2 receptors inhibit adenylate cyclase, which decreases cAMP production and thereby decreases calcium influx during the action potential. Consequently, lowered levels of calcium will lead to a decrease in neurotransmitter release by negative feedback
LTLIILVGLLMLLTVFGNVLVIIAVFTSRALKAPQNLFLVSLASADILVATLVIPFSLANEVMGYWYFGK
VWCEIYLALDVLFCTSSIVHLCAISLDRYWSITQAIEYNLKRTPRRIKCIIFIVWVISAVISFPPLITIE
KKSGQPEGPICKINDEKWYIISSCIGSFFAPCLIMVLVYIRIYQIAKNREKRFTFVLAVVIGVFVICWFP
FFFTYTLTAVCDCSVPETLFKFFFWFGYCNSSLNPVIYTIFNHDFRRAF
>gnl|CDD|320446 cd15323, 7tmA_alpha2C_AR, alpha-2 adrenergic receptors subtype C, member of the class A family of seven-transmembrane G protein-coupled receptors. The alpha-2 adrenergic receptors (or adrenoceptors) are a subfamily of the class A rhodopsin-like GPCRs that share a common architecture of seven transmembrane helices. This subfamily consists of three highly homologous receptor subtypes that have a key role in neurotransmitter release: alpha-2A, alpha-2B, and alpha-2C. In addition, a fourth subtype, alpha-2D is present in ray-finned fishes and amphibians, but is not found in humans. The alpha-2 receptors are found in both central and peripheral nervous system and serve to produce inhibitory functions through the G(i) proteins. Thus, the alpha-2 receptors inhibit adenylate cyclase, which decreases cAMP production and thereby decreases calcium influx during the action potential. Consequently, lowered levels of calcium will lead to a decrease in neurotransmitter release by negative feedback
AGLAAVVGFLIVFTIVGNVLVVIAVLTSRALRAPQNLFLVSLASADILVATLVMPFSLANELMGYWYFGQ
VWCNIYLALDVLFCTSSIVHLCAISLDRYWSVTQAVEYNLKRTPRRVKAIIVTVWLISAVISFPPLISMY
RDPEGDVYPQCKLNDETWYILSSCIGSFFAPCLIMILVYIRIYRVAKAREKRFTFVLAVVMGVFVVCWFP
FFFSYSLYGICREACEVPEPLFKFFFWIGYCNSSLNPVIYTIFNQDFRRSF
>gnl|CDD|320447 cd15324, 7tmA_alpha-2D_AR, alpha-2 adrenergic receptors subtype D, member of the class A family of seven-transmembrane G protein-coupled receptors. The alpha-2 adrenergic receptors (or adrenoceptors) are a subfamily of the class A rhodopsin-like GPCRs that share a common architecture of seven transmembrane helices. This subfamily consists of three highly homologous receptor subtypes that have a key role in neurotransmitter release: alpha-2A, alpha-2B, and alpha-2C. In addition, a fourth subtype, alpha-2D is present in ray-finned fishes and amphibians, but is not found in humans. The alpha-2 receptors are found in both central and peripheral nervous system and serve to produce inhibitory functions through the G(i) proteins. Thus, the alpha-2 receptors inhibit adenylate cyclase, which decreases cAMP production and thereby decreases calcium influx during the action potential. Consequently, lowered levels of calcium will lead to a decrease in neurotransmitter release by negative feedback
ALIVLVVVVIILVTIVGNVLVVVAVFTSRALRAPQNLFLVSLASADILVATLVIPFSLANEVMGYWYFGS
TWCAFYLALDVLFCTSSIVHLCAISLDRYWSVTKAVSYNLKRTPKRIKRMIAVVWVISAVISFPPLLMTK
HDEWECLLNDETWYILSSCTVSFFAPGLIMILVYCKIYRVAKMREKRFTFVLAVVMGVFVLCWFPFFFTY
SLHAVCRKRCGIPDALFNLFFWIGYCNSSVNPIIYTIFNRDFRKAF
>gnl|CDD|320448 cd15325, 7tmA_alpha1A_AR, alpha-1 adrenergic receptors subtype A, member of the class A family of seven-transmembrane G protein-coupled receptors. The alpha-1 adrenergic receptors (or adrenoceptors) are a subfamily of the class A rhodopsin-like GPCRs that share a common architecture of seven transmembrane helices. This subfamily consists of three highly homologous receptor subtypes that primarily mediate smooth muscle contraction: alpha-1A, alpha-1B, and alpha-1D. Activation of alpha-1 receptors by catecholamines such as norepinephrine and epinephrine couples to the G(q) protein, which then activates the phospholipase C pathway, leading to an increase in IP3 and calcium. Consequently, the elevation of intracellular calcium concentration leads to vasoconstriction in smooth muscle of blood vessels. In addition, activation of alpha-1 receptors by phenylpropanolamine (PPA) produces anorexia and may induce appetite suppression in rats
IVLGVILGGFILFGVLGNILVILSVACHRHLQTVTHYFIVNLAVADLLLTSTVLPFSAIFEILGYWAFGR
VFCNIWAAVDVLCCTASIMSLCIISIDRYIGVSYPLRYPSIMTERRGLLALLCVWVLSLVISIGPLFGWK
EPAPEDETICQITEEPGYALFSALGSFYLPLAIILVMYCRVYVVALKFSREKKAAKTLGIVVGCFVLCWL
PFFLVMPIGSIFPAYKPSDTVFKITFWLGYFNSCINPIIYPCSSQEFKKAF
>gnl|CDD|320449 cd15326, 7tmA_alpha1B_AR, alpha-1 adrenergic receptors subtype B, member of the class A family of seven-transmembrane G protein-coupled receptors. The alpha-1 adrenergic receptors (or adrenoceptors) are a subfamily of the class A rhodopsin-like GPCRs that share a common architecture of seven transmembrane helices. This subfamily consists of three highly homologous receptor subtypes that primarily mediate smooth muscle contraction: alpha-1A, alpha-1B, and alpha-1D. Activation of alpha-1 receptors by catecholamines such as norepinephrine and epinephrine couples to the G(q) protein, which then activates the phospholipase C pathway, leading to an increase in IP3 and calcium. Consequently, the elevation of intracellular calcium concentration leads to vasoconstriction in smooth muscle of blood vessels. In addition, activation of alpha-1 receptors by phenylpropanolamine (PPA) produces anorexia and may induce appetite suppression in rats
ILLGLVLGAFILFAIVGNILVILSVVCNRHLRIPTNYFIVNLAIADLLLSFTVLPFSATLEILGYWVFGR
IFCDIWAAVDVLCCTASILSLCAISIDRYIGVRHSLQYPTIVTRKRAILALLGVWVLSTVISIGPLLGWK
EPAPPDDKVCEITEEPFYALFSSLGSFYIPLIVILVMYCRVYIVALKFSREKKAAKTLGIVVGMFILCWL
PFFIALPLGSLFSHLKPPETLFKIIFWLGYFNSCLNPIIYPCSSKEFKRAF
>gnl|CDD|320450 cd15327, 7tmA_alpha1D_AR, alpha-1 adrenergic receptors subtype D, member of the class A family of seven-transmembrane G protein-coupled receptors. The alpha-1 adrenergic receptors (or adrenoceptors) are a subfamily of the class A rhodopsin-like GPCRs that share a common architecture of seven transmembrane helices. This subfamily consists of three highly homologous receptor subtypes that primarily mediate smooth muscle contraction: alpha-1A, alpha-1B, and alpha-1D. Activation of alpha-1 receptors by catecholamines such as norepinephrine and epinephrine couples to the G(q) protein, which then activates the phospholipase C pathway, leading to an increase in IP3 and calcium. Consequently, the elevation of intracellular calcium concentration leads to vasoconstriction in smooth muscle of blood vessels. In addition, activation of alpha-1 receptors by phenylpropanolamine (PPA) produces anorexia and may induce appetite suppression in rats
VGVGVFLAIFILMAIVGNILVILSVACNRHLQTVTNYFIVNLAIADLLLSTTVLPFSATLEVLGFWAFGR
VFCDIWAAVDVLCCTASILSLCVISVDRYVGVKHSLKYPTIMTERKAGVILVLLWVSSMVISIGPLLGWK
EPPPPDESICSITEEPGYALFSSLFSFYLPLMVILVMYFRVYVVALKFSREKKAAKTLAIVVGVFILCWF
PFFFVLPLGSFFPALKPSEMVFKVIFWLGYFNSCVNPIIYPCSSKEFKRAF
>gnl|CDD|320451 cd15328, 7tmA_5-HT5, serotonin receptor subtype 5, member of the class A family of seven-transmembrane G protein-coupled receptors. 5-HT5 receptor, one of 14 mammalian 5-HT receptors, is activated by the neurotransmitter and peripheral signal mediator serotonin (also known as 5-hydroxytryptamine or 5-HT). The 5-HT5A and 5-HT5B receptors have been cloned from rat and mouse, but only the 5-HT5A isoform has been identified in human because of the presence of premature stop codons in the human 5-HT5B gene, which prevents a functional receptor from being expressed. 5-HT5 receptors mediate inhibitory neurotransmission by coupling to G proteins of the G(i/0) family, which lead to a decrease in adenylate cyclase activity, thereby decreasing intracellular cAMP levels and calcium influx. In the CNS, serotonin is involved in the regulation of appetite, mood, sleep, cognition, learning and memory, as well as implicated in neurologic disorders such as migraine, schizophrenia, and depression
VLVLTLLAMLVVATFLWNLLVLVTILRVRTFHRVPHNLVASMAVSDVLVAALVMPLSLVHELSGRRWQLG
RSLCQVWISFDVLCCTASIWNVTAIALDRYWSITRHLEYTLRTRRRISNVMIALTWALSAVISLAPLLFG
WGETYSEDSEECQVSQEPSYTVFSTFGAFYLPLCVVLFVYWKIYKAAQKEKRAALMVGILIGVFVLCWIP
FFLTELISPLCSCDIPPIWKSIFLWLGYSNSFFNPLIYTAFNKNYNNAF
>gnl|CDD|320452 cd15329, 7tmA_5-HT7, serotonin receptor subtype 7, member of the class A family of seven-transmembrane G protein-coupled receptors. The 5-HT7 receptor, one of 14 mammalian serotonin receptors, is a member of the class A of GPCRs and is activated by the neurotransmitter serotonin (5-hydroxytryptamine, 5-HT). 5-HT7 receptor mainly couples to Gs protein, which positively stimulates adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. 5-HT7 receptor is expressed in various human tissues, mainly in the brain, the lower gastrointestinal tract and in vital blood vessels including the coronary artery. In the CNS, serotonin is involved in the regulation of appetite, mood, sleep, cognition, learning and memory, as well as implicated in neurologic disorders such as migraine, schizophrenia, and depression
VLIGIVLLIIILGTVVGNALVIIAVCLVKKLRTPSNYLIVSLAVSDLLVALLVMPLAIIYELSGYWPFGE
ILCDVWISFDVLLCTASILNLCAISVDRYLVITRPLTYAVKRTPKRMALMIAIVWLLSALISIPPLFGWK
NKVNDPGVCQVSQDFGYQIYATFGAFYIPLIVMLVLYYKIYRAAKSERKAIKTLGIIMGAFTLCWLPFFI
LALLRPFLKPIKCSCIPLWLSRLFLWLGYANSFLNPIIYAKFNREFRTPF
>gnl|CDD|320453 cd15330, 7tmA_5-HT1A_vertebrates, serotonin receptor subtype 1A from vertebrates, member of the class A family of seven-transmembrane G protein-coupled receptors. The 5-HT1 receptors, one of 14 mammalian 5-HT receptors, is a member of the class A of GPCRs and is activated by the endogenous neurotransmitter and peripheral signal mediator serotonin (5-hydroxytryptamine, 5-HT). The 5-HT1 receptors mediate inhibitory neurotransmission by coupling to G proteins of the G(i/o) family, which lead to a decrease in adenylate cyclase activity, thereby decreasing intracellular cAMP levels and calcium influx. The 5-HT1 receptor subfamily includes 5 subtypes: 5-HT1A, 5-HT1B, 5-HT1D, 5-HT1E, and 5-HT1F. There is no 5-HT1C receptor subtype, as it has been reclassified as the 5-HT2C receptor. In the CNS, serotonin is involved in the regulation of appetite, mood, sleep, cognition, learning and memory, as well as implicated in neurologic disorders such as migraine, schizophrenia, and depression
IITSLFLGTLILCAIFGNACVVAAIALERSLQNVANYLIGSLAVTDLMVSVLVLPMAALYQVLNKWTLGQ
VTCDLFIALDVLCCTSSILHLCAIALDRYWAITDPIDYVNKRTPRRAAVLISLTWLIGFSISIPPMLGWR
TPEDRSDPDACTISKDPGYTIYSTFGAFYIPLILMLVLYGRIFKAAARERKTVKTLGIIMGTFILCWLPF
FIVALVLPFCESTCHMPELLGAIINWLGYSNSLLNPIIYAYFNKDFQSAF
>gnl|CDD|320454 cd15331, 7tmA_5-HT1A_invertebrates, serotonin receptor subtype 1A from invertebrates, member of the class A family of seven-transmembrane G protein-coupled receptors. The 5-HT1 receptors, one of 14 mammalian 5-HT receptors, is a member of the class A of GPCRs and is activated by the endogenous neurotransmitter and peripheral signal mediator serotonin (5-hydroxytryptamine, 5-HT). The 5-HT1 receptors mediate inhibitory neurotransmission by coupling to G proteins of the G(i/o) family, which lead to a decrease in adenylate cyclase activity, thereby decreasing intracellular cAMP levels and calcium influx. The 5-HT1 receptor subfamily includes 5 subtypes: 5-HT1A, 5-HT1B, 5-HT1D, 5-HT1E, and 5-HT1F. There is no 5-HT1C receptor subtype, as it has been reclassified as the 5-HT2C receptor. In the CNS, serotonin is involved in the regulation of appetite, mood, sleep, cognition, learning and memory, as well as implicated in neurologic disorders such as migraine, schizophrenia, and depression
VLTSIILGLLILATIIGNVFVIAAILLERSLQGVSNYLILSLAVADLMVAVLVMPLSAVYEVSQHWFLGP
EVCDMWISMDVLCCTASILHLVAIALDRYWAVTNIDYIRRRTAKRILIMIAVVWFVSLIISIAPLFGWKD
EDDLDRVLKTGVCLISQDYGYTIFSTVGAFYVPLLLMIIIYWKIYQAAKRERKAARTLAIITGAFVVCWL
PFFLVALVMPFCGAWQISRFLESFFLWLGYFNSLLNPIIYTIFSPDFRGAF
>gnl|CDD|320455 cd15333, 7tmA_5-HT1B_1D, serotonin receptor subtypes 1B and 1D, member of the class A family of seven-transmembrane G protein-coupled receptors. The 5-HT1 receptors, one of 14 mammalian 5-HT receptors, is a member of the class A of GPCRs and is activated by the endogenous neurotransmitter and peripheral signal mediator serotonin (5-hydroxytryptamine, 5-HT). The 5-HT1 receptors mediate inhibitory neurotransmission by coupling to G proteins of the G(i/o) family, which lead to a decrease in adenylate cyclase activity, thereby decreasing intracellular cAMP levels and calcium influx. The 5-HT1 receptor subfamily includes 5 subtypes: 5-HT1A, 5-HT1B, 5-HT1D, 5-HT1E, and 5-HT1F. There is no 5-HT1C receptor subtype, as it has been reclassified as the 5-HT2C receptor. In the CNS, serotonin is involved in the regulation of appetite, mood, sleep, cognition, learning and memory, as well as implicated in neurologic disorders such as migraine, schizophrenia, and depression
LGLKISLAVLLALITLATTLSNAFVIATIYLTRKLHTPANYLIASLAVTDLLVSILVMPISIVYTVTGTW
TLGQVVCDIWLSSDITCCTASILHLCVIALDRYWAITDAVEYSKKRTPKRAAVMIALVWVISISISLPPF
FWRQAKAEEEVSECVVNTDHILYTVYSTVGAFYIPTLLLIALYGRIYVEARARERKATKTLGIILGAFIV
CWLPFFIISLVLPICKDACWFHLAIFDFFTWLGYLNSLINPIIYTMSNEDFKQAF
>gnl|CDD|320456 cd15334, 7tmA_5-HT1F, serotonin receptor subtype 1F, member of the class A family of seven-transmembrane G protein-coupled receptors. The 5-HT1 receptors, one of 14 mammalian 5-HT receptors, is a member of the class A of GPCRs and is activated by the endogenous neurotransmitter and peripheral signal mediator serotonin (5-hydroxytryptamine, 5-HT). The 5-HT1 receptors mediate inhibitory neurotransmission by coupling to G proteins of the G(i/o) family, which lead to a decrease in adenylate cyclase activity, thereby decreasing intracellular cAMP levels and calcium influx. The 5-HT1 receptor subfamily includes 5 subtypes: 5-HT1A, 5-HT1B, 5-HT1D, 5-HT1E, and 5-HT1F. There is no 5-HT1C receptor subtype, as it has been reclassified as the 5-HT2C receptor. In the CNS, serotonin is involved in the regulation of appetite, mood, sleep, cognition, learning and memory, as well as implicated in neurologic disorders such as migraine, schizophrenia, and depression
ILISLTLSILALMTTAINSLVITAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIMYIVKETWIMGQ
VVCDIWLSVDITCCTCSILHLSAIALDRYRAITDAVEYARKRTPKHAGIMIAVVWIISIFISMPPLFWRH
QTTSREDECIIKHDHIVFTIYSTFGAFYIPLALILILYYKIYRAATRERKAATTLGLILGAFVICWLPFF
VKEVIVNTCDSCYISEEMSNFLTWLGYINSLINPLIYTIFNEDFKKAFQ
>gnl|CDD|320457 cd15335, 7tmA_5-HT1E, serotonin receptor subtype 1E, member of the class A family of seven-transmembrane G protein-coupled receptors. The 5-HT1 receptors, one of 14 mammalian 5-HT receptors, is a member of the class A of GPCRs and is activated by the endogenous neurotransmitter and peripheral signal mediator serotonin (5-hydroxytryptamine, 5-HT). The 5-HT1 receptors mediate inhibitory neurotransmission by coupling to G proteins of the G(i/o) family, which lead to a decrease in adenylate cyclase activity, thereby decreasing intracellular cAMP levels and calcium influx. The 5-HT1 receptor subfamily includes 5 subtypes: 5-HT1A, 5-HT1B, 5-HT1D, 5-HT1E, and 5-HT1F. There is no 5-HT1C receptor subtype, as it has been reclassified as the 5-HT2C receptor. In the CNS, serotonin is involved in the regulation of appetite, mood, sleep, cognition, learning and memory, as well as implicated in neurologic disorders such as migraine, schizophrenia, and depression
MLIVLTLALITILTTVLNSAVIAAICTTKKLHQPANYLICSLAVTDFLVAVLVMPLSITYIVMDTWTLGY
FICEIWLSVDMTCCTCSILHLCVIALDRYWAITDAIEYARKRTAKRAGLMILTVWTISIFISIPPLFWRN
HHDANIPSQCIIQHDHVIYTIYSTFGAFYIPLTLILILYYRIYHAASRERKAARILGLILGAFILSWLPF
FIKELIVGLSVMTVSPEVADFLTWLGYVNSLVNPLLYTSFNEDFKLAF
>gnl|CDD|320458 cd15336, 7tmA_Melanopsin, vertebrate melanopsins (Opsin-4), member of the class A family of seven-transmembrane G protein-coupled receptors. Melanopsin (also called Opsin-4) is the G protein-coupled photopigment that mediates non-visual responses to light. In mammals, these photoresponses include the photo-entrainment of circadian rhythm, pupillary constriction, and acute nocturnal melatonin suppression. Mammalian melanopsins are expressed only in the inner retina, whereas non-mammalian vertebrate melanopsins are localized in various extra-retinal tissues such as iris, brain, pineal gland, and skin. Melanopsins belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops
YTVGSVILIIGITGMLGNALVIYAFCRSKKLRTPANYFIINLAVSDFLMSLTQSPIFFVNSLHKRWIFGE
KGCELYAFCGALFGITSMITLLAISLDRYLVITKPLASIRWVSKKRAMIIILLVWLYSLAWSLPPLFGWS
AYVPEGLLTSCTWDYMTFTPSVRAYTMLLFCFVFFIPLGIIIYCYLFIFLAIRSTGREVQKLGSQDRKEK
AKQYQRMKNEWKMAKIAFVVILLFVLSWSPYACVALIAWAGYAHLLTPYMKSVPAVIAKASAIYNPIIYA
ITHPKYREAI
>gnl|CDD|320459 cd15337, 7tmA_Opsin_Gq_invertebrates, invertebrate Gq opsins, member of the class A family of seven-transmembrane G protein-coupled receptors. The invertebrate Gq-coupled opsin subfamily includes the arthropod and mollusc visual opsins. Like the vertebrate visual opsins, arthropods possess color vision by the use of multiple opsins sensitive to different light wavelengths. The invertebrate Gq opsins are closely related to the vertebrate melanopsins, the primary photoreceptor molecules for non-visual responses to light, and the R1-R6 photoreceptors, which are the fly equivalent to the vertebrate rods. The Gq opsins belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops
YLIGIYIAIVGILGVIGNLLVIYLFSKTKSLRTPSNMFIINLAISDFGFSAVNGFPLKTISSFNKKWIWG
KVACELYGFAGGIFGFMSITTLAAISIDRYLVIAKPLEAMKKMTFKRAFIMIIIIWLWSLLWSIPPFFGW
GRYVPEGFQTSCTFDYLSRDLNNRLFILGLFIFGFLCPLLIIIFCYVNIIRAVRNHEKEMTQTAKSGMGK
DTEKNDARKKAEIRIAKVAIILISLFLLSWTPYAVVALLGQFGPAYWITPYVSELPVMFAKASAIYNPII
YALSHPKFRAAL
>gnl|CDD|320460 cd15338, 7tmA_MCHR1, melanin concentrating hormone receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. Melanin-concentrating hormone receptor (MCHR) binds melanin concentrating hormone and is presumably involved in the neuronal regulation of food intake and energy homeostasis. Despite strong homology with somatostatin receptors, MCHR does not appear to bind somatostatin. Two MCHRs have been characterized in vertebrates, MCHR1 and MCHR2. MCHR1 is expressed in all mammals, whereas MCHR2 is only expressed in the higher order mammals, such as humans, primates, and dogs, and is not found in rodents. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VIMPSVFGVICFLGIIGNSIVIYTIVKKSKFRCQQTVPDIFIFNLSIVDLLFLLGMPFLIHQLLGNGVWH
FGETMCTLITALDTNSQITSTYILTVMTLDRYLATVHPIRSTKIRTPRVAVAVICLVWILSLLSITPVWM
YAGLMPLPDGSVGCALLLPNPETDTYWFTLYQFFLAFALPLVVICVVYFKILQNMASTVAPLPQRSLRVR
TKKVTRMAVAICLAFFICWAPFYILQLAHLSIDRPSLAFLYAYNVAISMGYANSCINPFLYIMLSETFKR
QF
>gnl|CDD|320461 cd15339, 7tmA_MCHR2, melanin concentrating hormone receptor 2, member of the class A family of seven-transmembrane G protein-coupled receptors. Melanin-concentrating hormone receptor (MCHR) binds melanin concentrating hormone and is presumably involved in the neuronal regulation of food intake and energy homeostasis. Despite strong homology with somatostatin receptors, MCHR does not appear to bind somatostatin. Two MCHRs have been characterized in vertebrates, MCHR1 and MCHR2. MCHR1 is expressed in all mammals, whereas MCHR2 is only expressed in the higher order mammals, such as humans, primates, and dogs, and is not found in rodents. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VILPSFIGILCSTGLVGNILVLFTIIRSRKKTVPDIYVCNLAVADLVHIIVMPFLIHQWARGGEWVFGSP
LCTIITSLDTCNQFACSAIMTAMSLDRYIALVHPFRLTSLRTRSKTIRINLLVWAASFILVLPVWVYAKV
IKFRDGLESCAFNLTSPDDVLWYTLYQTITTFFFPLPLILICYILILCYTWEMYRKNKKAGRYNTSIPRQ
RVMRLTKMVLVLVGVFLVSAAPYHVIQLVNLSVSQPTLAFYVSYYLSICLSYASSSINPFLYILLSGNFR
KRL
>gnl|CDD|320462 cd15340, 7tmA_CB1, cannabinoid receptor subtype 1, member of the class A family of seven-transmembrane G protein-coupled receptors. Cannabinoid receptors belong to the class A G-protein coupled receptor superfamily. Two types of cannabinoid receptors, CB1 and CB2, have been identified so far. They are activated by naturally occurring endocannabinoids, cannabis plant-derived cannabinoids such as tetrahydrocannabinol, or synthetic cannabinoids. The CB receptors are involved in the various physiological processes such as appetite, mood, memory, and pain sensation. CB1 receptor is expressed predominantly in central and peripheral neurons, while CB2 receptor is found mainly in the immune system
LAIAVLSLTLGTFTVLENLLVLCVILHSRSLRCRPSYHFIGSLAVADLLGSVIFVYSFLDFHVFHRKDSP
NVFLFKLGGVTASFTASVGSLFLTAIDRYISIHRPLAYKRIVTRTKAVIAFCVMWTIAIVIAVLPLLGWN
CKKLNSVCSDIFPLIDETYLMFWIGVTSVLLLFIVYAYMYILWKAHHHAVRMLQRGTQKSIIVYTSEDGK
VQTTRPDQTRMDIRLAKTLVLILVVLIICWGPLLAIMVYDVFGKMNKLIKTVFAFCSMLCLLNSTVNPII
YALRSKDLRHAF
>gnl|CDD|320463 cd15341, 7tmA_CB2, cannabinoid receptor subtype 2, member of the class A family of seven-transmembrane G protein-coupled receptors. Cannabinoid receptors belong to the class A G-protein coupled receptor superfamily. Two types of cannabinoid receptors, CB1 and CB2, have been identified so far. They are activated by naturally occurring endocannabinoids, cannabis plant-derived cannabinoids such as tetrahydrocannabinol, or synthetic cannabinoids. The CB receptors are involved in the various physiological processes such as appetite, mood, memory, and pain sensation. CB1 receptor is expressed predominantly in central and peripheral neurons, while CB2 receptor is found mainly in the immune system
IAIAVLCTLCGLLCILENVAVLYLILSSPKLRRKPSYLFIGSLALADFLASVVFACSFVDFHVFHGVDSS
AIFLLKLGGVTMSFTASLGSLLLMAFDRYVCIYYPSEYKALVTRKRALVALAVMWVLTALIAYLPLMGWN
CCPLNSPCSELFPLIPNDYLLSWLLLVAILLSGIIYTYGHVLWKAHKHVVYMEKHQDQQGPGNARMRLDV
RLAKTLGLVLAVLLICWSPVLALMMHSLFTSLSDHIKKAFAFCSTLCLVNSMVNPIIYALRSRELRSSL
>gnl|CDD|320464 cd15342, 7tmA_LPAR2_Edg4, lysophosphatidic acid receptor subtype 2 (LPAR2 or LPA2), also called Endothelial differentiation gene 4 (Edg4), member of the class A family of seven-transmembrane G protein-coupled receptors. The endothelial differentiation gene (Edg) family of G-protein coupled receptors binds blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). The Edg receptors couple and activate at least three different G protein subtypes including G(i/o), G(q/11), and G(12/13)
YAVVALGLTVSVIVLLTNLLVIAAIFINRRFHYPIYYLLGNLAAADLFAGVAYLFLMFHTGPWTAKLSLY
QWFLRQGLLDTSLTASVANLLAIAVERHQTIFTMQLHSKMSNQRVVILIFGIWMVALILGLIPAMGWNCL
CDLKRCSTMAPLYSRSYLVFWALSNLLTFLIMVAVYTRIFIYVRRKSQRMSEHHSSHPRYRETVLGLMKT
VVIILGAFVVCWTPGQVVLLLDGLGCESCNVLAYEKYFLLLAEINSLVNPIVYSYRDKEMRKTF
>gnl|CDD|320465 cd15343, 7tmA_LPAR3_Edg7, lysophosphatidic acid receptor subtype 3 (LPAR3 or LPA3), also called endothelial differentiation gene 7 (Edg7), member of the class A family of seven-transmembrane G protein-coupled receptors. The endothelial differentiation gene (Edg) family of G-protein coupled receptors binds blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). The Edg receptors couple and activate at least three different G protein subtypes including G(i/o), G(q/11), and G(12/13)
IIVLCVGTFCCLFIFVSNSLVIAAVVKNKRFHYPFYYLLANLAAADFFAGIAYVFLMFNTGPVSKTLTVN
RWFLRQGLLDTSLSASLTNLLVIAVERHISIMRMKVHSNLTKRRVTLLIALVWAIAIFMGAVPTLGWNCI
CNISACSSLAPIYSRSYLVFWSVSNLVVFLIMVVVYLRIYVYVQRKTNVLSPHTSGSINRRRTPIKLMKT
VMTVLGAFVICWTPGLVVLLLDGLNCTRCGVQHVKRWFLLLALLNSVMNPIIYSYKDEEMWGTM
>gnl|CDD|341348 cd15344, 7tmA_LPAR1_Edg2, lysophosphatidic acid receptor subtype 1 (LPAR1 or LPA1), also called endothelial differentiation gene 2 (Edg2), member of the class A family of seven-transmembrane G protein-coupled receptors. The endothelial differentiation gene (Edg) family of G-protein coupled receptors binds blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). The Edg receptors couple and activate at least three different G protein subtypes including G(i/o), G(q/11), and G(12/13)
KLVMGLGITVCIFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVS
TWLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGAIPSVGWNCI
CDIENCSNMAPLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRMSRHSSGPRRNRDTMMSLLKT
VVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLLAEFNSAMNPIIYSYRDKEMSATF
>gnl|CDD|320467 cd15345, 7tmA_S1PR3_Edg3, sphingosine-1-phosphate receptor subtype 3 (S1PR3 or S1P3), also called endothelial differentiation gene 3 (Edg3), member of the class A family of seven-transmembrane G protein-coupled receptors. The endothelial differentiation gene (Edg) family of G-protein coupled receptors binds blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). The Edg receptors couple and activate at least three different G protein subtypes including G(i/o), G(q/11), and G(12/13)
DLTTIFFLVICSFIVLENLMVLIAIWKNNRFHNRMYFFIGNLALCDLLAGIAYKVNILMSGKKTFSLSPT
QWFLREGSMFVALGASTFSLLAIAIERHLTMIKMRPYDANKRYRVFLLIGTCWLISVLLGALPILGWNCL
DNLPDCSTILPLYSKKYVAFCISIFIAILVAIVILYARIYILVKSSSRRVTNHRNSERSMALLRTVVIVV
GVFIACWSPLFILLLIDVACEVKQCPILYKADWFIALAVLNSAMNPIIYTLASKEMRRAF
>gnl|CDD|320468 cd15346, 7tmA_S1PR1_Edg1, sphingosine-1-phosphate receptor subtype 1 (S1PR1 or S1P1), also called endothelial differentiation gene 1 (Edg1), member of the class A family of seven-transmembrane G protein-coupled receptors. The endothelial differentiation gene (Edg) family of G-protein coupled receptors binds blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). The Edg receptors couple and activate at least three different G protein subtypes including G(i/o), G(q/11), and G(12/13)
KLTSVVFIIICCFIILENIFVLLTIWKTKKFHRPMYYFIGNLALSDLLAGVAYTANLLLSGATTYKLTPT
QWFLREGSMFVALSASVFSLLAIAIERYITMLKMKLHNGSNSFRSFLLISACWVISLILGGLPIMGWNCI
SALSSCSTVLPLYHKHYILFCTTVFTLLLLSIVILYCRIYSLVRTRSRRLTFRKNIRKASRSSEKSMALL
KTVIIVLSVFIACWAPLFILLLLDVGCKVKTCSILFKAEYFLVLAVLNSATNPIIYTLTNKEMRRAF
>gnl|CDD|320469 cd15347, 7tmA_S1PR2_Edg5, sphingosine-1-phosphate receptor subtype 2 (S1PR2 or S1P2), also called endothelial differentiation gene 5 (Edg5), member of the class A family of seven-transmembrane G protein-coupled receptors. The endothelial differentiation gene (Edg) family of G-protein coupled receptors binds blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). The Edg receptors couple and activate at least three different G protein subtypes including G(i/o), G(q/11), and G(12/13)
QVASIFIVILCCIIVLENLLVLIAVARNKKFHSAMFFFIGNLAFSDLLAGVAFIANILLSGSVTFRLTPV
QWFIREGTAFITLSASVFSLLAIAIERHVAITKVKLYGSDKNCRMVLLIGACWVISIVLGGLPILGWNCI
GNLEDCSTVLPLYSKHYILFVVTIFSIILLSIVILYVRIYCIVRSSHAEMAAPQTLALLKTVTIVLGVFI
VCWLPAFIILLLDTSCKVKSCPILYKADYFFSVATLNSALNPVIYTLRSKDMRKEF
>gnl|CDD|320470 cd15348, 7tmA_S1PR5_Edg8, sphingosine-1-phosphate receptor subtype 5 (S1PR5 or S1P5), also called endothelial differentiation gene 8 (Edg8), member of the class A family of seven-transmembrane G protein-coupled receptors. The endothelial differentiation gene (Edg) family of G-protein coupled receptors binds blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). The Edg receptors couple and activate at least three different G protein subtypes including G(i/o), G(q/11), and G(12/13)
KADAVAFLAVCAFIVLENLIVLLALWRNKKFHSPMFYLLGSLTLSDLLAGAAYAANILMSGANTLKLTPA
LWFLREGGVFITLTASVFSLLAIAIERHITMVRMKPYPGDKRGRMFLLIGAAWLVSILLGVLPILGWNCL
GNLDACSTVLPLYAKSYILFCITVFLAILAAIVVLYARIYRIVKANSQRLGALPTRKGRARRSQKYLALL
KTVTIVLGTFVACWLPLFLLLLLDVSCPAQACPVLLKADYFLGLAMINSLLNPIIYTLTSRDMRRAI
>gnl|CDD|320471 cd15349, 7tmA_S1PR4_Edg6, sphingosine-1-phosphate receptor subtype 4 (S1PR4 or S1P4), also called endothelial differentiation gene 6 (Edg6), member of the class A family of seven-transmembrane G protein-coupled receptors. The endothelial differentiation gene (Edg) family of G-protein coupled receptors binds blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). The Edg receptors couple and activate at least three different G protein subtypes including G(i/o), G(q/11), and G(12/13)
GALTVLFICISVLIILENLLVLLAILRRVRLRRWVYICLANIALSDLLTGTSYLVNICLSGERTFRLTPA
LWFLREGLLFTALAASTFSLLVTAVERYATMVRPVAENTATKTYRVYGMIVLCWILAFLIGFLPLLGWNC
LCDFRSCSSLLPLYSKSYILFCLVIFFIILLTIIGLYFAIYCLVRASGQRVISARSRRRSLRLLKTVLMI
LGAFMVCWGPLFILLLVDFFCSSRSCKPLFGMEWVLALAVLNSAINPLIYSFRSLEVRRAV
>gnl|CDD|320472 cd15350, 7tmA_MC2R_ACTH_R, melanocortin receptor subtype 2, also called adrenocorticotropic hormone receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The melanocortin receptor (MCR) subfamily is a member of the class A family of seven-transmembrane G-protein coupled receptors. MCRs bind a group of pituitary peptide hormones known as melanocortins, which include adrenocorticotropic hormone (ACTH) and the different isoforms of melanocyte-stimulating hormones. There are five known subtypes of the MCR subfamily. MC1R is involved in regulating skin pigmentation and hair color. ACTH (adrenocorticotropic hormone) is the only endogenous ligand for MC2R, which shows low sequence similarity with other melanocortin receptors. Mutations in MC2R cause familial glucocorticoid deficiency type 1, in which patients have elevated plasma ACTH and low cortisol levels. MC3R is expressed in many parts of the brain and peripheral tissues and involved in the regulation of energy homeostasis. MC4R is expressed primarily in the central nervous system and involved in both eating behavior and sexual function. MC5R is widely expressed in peripheral tissues and is mainly involved in the regulation of exocrine gland function
VVPEEVFFTIAAVGLLENLLVLVAVIKNKNLHSPMYFFICSLAVSDMLGSLYKTLENILIILADMGYLNR
RGPFETKLDDIMDSLFCLSLLGSIFSILAIAADRYITIFHALRYHNIMTMRRTLVILAIIWTFCGGSGIL
MILFFHFVATVICFTVLFFLMLVLILCLYVHMFLLARSHARKIASLPNHHAQHQRSNMRGAITLTILLGV
FVCCWAPFVLHLLLMMFCPMNPYCACYRSLFQVNGTLIMSHAVIDPAIYAFRSPELRNTF
>gnl|CDD|320473 cd15351, 7tmA_MC1R, melanocortin receptor subtype 1, member of the class A family of seven-transmembrane G protein-coupled receptors. The melanocortin receptor (MCR) subfamily is a member of the class A family of seven-transmembrane G-protein coupled receptors. MCRs bind a group of pituitary peptide hormones known as melanocortins, which include adrenocorticotropic hormone (ACTH) and the different isoforms of melanocyte-stimulating hormones. There are five known subtypes of the MCR subfamily. MC1R is involved in regulating skin pigmentation and hair color. ACTH (adrenocorticotropic hormone) is the only endogenous ligand for MC2R, which shows low sequence similarity with other melanocortin receptors. Mutations in MC2R cause familial glucocorticoid deficiency type 1, in which patients have elevated plasma ACTH and low cortisol levels. MC3R is expressed in many parts of the brain and peripheral tissues and involved in the regulation of energy homeostasis. MC4R is expressed primarily in the central nervous system and involved in both eating behavior and sexual function. MC5R is widely expressed in peripheral tissues and is mainly involved in the regulation of exocrine gland function
EIPKGLFLFLGLVSLVENILVVVAIAKNRNLHSPMYYFICCLAVSDMLVSVSNLIETLFMLLLEHGVLVC
RAPMLQHMDNVIDTMICSSVVSSLSFLGAIAVDRYITIFYALRYHSIMTLQRAVNAIAGIWLASTVSSTL
FIVYYNSNAVILCLIVFFLFMLVLMLVLYIHMFILACRHSQSISSQQRRQCPHQQTASLKGAITLTILLG
IFFLCWGPFFLHLTLIVTCPTHPFCLCYFKYFNLFLILIICNSIIDPLIYAFRSQELRKTL
>gnl|CDD|320474 cd15352, 7tmA_MC3R, melanocortin receptor subtype 3, member of the class A family of seven-transmembrane G protein-coupled receptors. The melanocortin receptor (MCR) subfamily is a member of the class A family of seven-transmembrane G-protein coupled receptors. MCRs bind a group of pituitary peptide hormones known as melanocortins, which include adrenocorticotropic hormone (ACTH) and the different isoforms of melanocyte-stimulating hormones. There are five known subtypes of the MCR subfamily. MC1R is involved in regulating skin pigmentation and hair color. ACTH (adrenocorticotropic hormone) is the only endogenous ligand for MC2R, which shows low sequence similarity with other melanocortin receptors. Mutations in MC2R cause familial glucocorticoid deficiency type 1, in which patients have elevated plasma ACTH and low cortisol levels. MC3R is expressed in many parts of the brain and peripheral tissues and involved in the regulation of energy homeostasis. MC4R is expressed primarily in the central nervous system and involved in both eating behavior and sexual function. MC5R is widely expressed in peripheral tissues and is mainly involved in the regulation of exocrine gland function
FIKAEVFLTLGIVSLLENILVILAVVKNKNLHSPMYFFLCSLAVADMLVSVSNSLETIMIAVLNSGYLVI
SDQFIQHMDNVFDSMICISLVASICNLLAIAVDRYVTIFYALRYHSIMTVRKALVLIAVIWVVCIVCGIV
FIVYSESKTVIVCLITMFFAMLVLMATLYVHMFLFARLHVKRIAALPPAVDGAPQQRSCMKGAVTITILL
GVFIVCWAPFFLHLILIISCPHNPYCLCYTSHFNTYLVLIMCNSVIDPLIYAFRSLEMRKTF
>gnl|CDD|320475 cd15353, 7tmA_MC4R, melanocortin receptor subtype 4, member of the class A family of seven-transmembrane G protein-coupled receptors. The melanocortin receptor (MCR) subfamily is a member of the class A family of seven-transmembrane G-protein coupled receptors. MCRs bind a group of pituitary peptide hormones known as melanocortins, which include adrenocorticotropic hormone (ACTH) and the different isoforms of melanocyte-stimulating hormones. There are five known subtypes of the MCR subfamily. MC1R is involved in regulating skin pigmentation and hair color. ACTH (adrenocorticotropic hormone) is the only endogenous ligand for MC2R, which shows low sequence similarity with other melanocortin receptors. Mutations in MC2R cause familial glucocorticoid deficiency type 1, in which patients have elevated plasma ACTH and low cortisol levels. MC3R is expressed in many parts of the brain and peripheral tissues and involved in the regulation of energy homeostasis. MC4R is expressed primarily in the central nervous system and involved in both eating behavior and sexual function. MC5R is widely expressed in peripheral tissues and is mainly involved in the regulation of exocrine gland function
FVSPEVFVTLGIVSLLENILVIAAIAKNKNLHSPMYFFICSLAVADMLVSVSNGSETVVITLLNGNDTDA
QSFTVNIDNVIDSVICSSLLASICSLLSIAVDRYFTIFYALQYHNIMTVRRAGVIITCIWTACTVSGVLF
IIYSDSSVVIICLISMFFTMLALMASLYVHMFLLARLHIKRIAVLPGTGPIRQGANMKGAITLTILLGVF
VVCWAPFFLHLIFYISCPRNPYCVCFMSHFNMYLILIMCNSVIDPLIYAFRSQELRKTF
>gnl|CDD|320476 cd15354, 7tmA_MC5R, melanocortin receptor subtype 5, member of the class A family of seven-transmembrane G protein-coupled receptors. The melanocortin receptor (MCR) subfamily is a member of the class A family of seven-transmembrane G-protein coupled receptors. MCRs bind a group of pituitary peptide hormones known as melanocortins, which include adrenocorticotropic hormone (ACTH) and the different isoforms of melanocyte-stimulating hormones. There are five known subtypes of the MCR subfamily. MC1R is involved in regulating skin pigmentation and hair color. ACTH (adrenocorticotropic hormone) is the only endogenous ligand for MC2R, which shows low sequence similarity with other melanocortin receptors. Mutations in MC2R cause familial glucocorticoid deficiency type 1, in which patients have elevated plasma ACTH and low cortisol levels. MC3R is expressed in many parts of the brain and peripheral tissues and involved in the regulation of energy homeostasis. MC4R is expressed primarily in the central nervous system and involved in both eating behavior and sexual function. MC5R is widely expressed in peripheral tissues and is mainly involved in the regulation of exocrine gland function
VIAAEVFLTLGIISLLENILVILAIVKNKNLHSPMYFFVCSLAVADMLVSVSNAWETITIYLLNNRHLVI
EDAFVRHIDNVFDSLICISVVASMCSLLAIAVDRYVTIFYALRYHNIMTVRRAGIIIACIWTFCTGCGII
FILYSESTYVIICLITMFFAMLFLMVSLYIHMFLLARTHVKRIAALPGYNSVRQRTSMKGAVTLTILLGI
FIVCWAPFFLHLILMISCPQNLYCVCFMSHFNMYLILIMCNSVIDPLIYAFRSQEMRKTF
>gnl|CDD|320477 cd15355, 7tmA_NTSR1, neurotensin receptor subtype 1, member of the class A family of seven-transmembrane G protein-coupled receptors. Neurotensin (NTS) is a 13 amino-acid neuropeptide that functions as both a neurotransmitter and a hormone in the nervous system and peripheral tissues, respectively. NTS exerts various biological activities through activation of the G protein-coupled neurotensin receptors, NTSR1 and NTSR2. In the brain, NTS is involved in the modulation of dopamine neurotransmission, opioid-independent analgesia, hypothermia, and the inhibition of food intake, while in the periphery NTS promotes the growth of various normal and cancer cells and acts as a paracrine and endocrine modulator of the digestive tract. The third neurotensin receptor, NTSR3 or also called sortilin, is not a G protein-coupled receptor
VLVTAIYLALFVVGTVGNSITLYTLARKKSLQHLQSTVHYHLASLALSDLLILLLAMPVELYNFIWVHHP
WAFGDAACRGYYFLRDACTYATALNVASLSVERYLAICHPFKAKSLMSRSRTKKFISAIWLASALLAIPM
LFTMGEQNRSGTHPGGLICTPIVDTSTLKVVIQVNAFLSFLFPMLVISVLNTLIANQLTVMVNQAEQENQ
VCTIGGQRTVLSVSMEPGRVQSLRHGVLVLRAVVIAFVVCWLPYHVRRLMFCYVSDEQWTTFLYDFYHYF
YMLTNVLFYVSSAINPILYNLVSANFRQIF
>gnl|CDD|320478 cd15356, 7tmA_NTSR2, neurotensin receptor subtype 2, member of the class A family of seven-transmembrane G protein-coupled receptors. Neurotensin (NTS) is a 13 amino-acid neuropeptide that functions as both a neurotransmitter and a hormone in the nervous system and peripheral tissues, respectively. NTS exerts various biological activities through activation of the G protein-coupled neurotensin receptors, NTSR1 and NTSR2. In the brain, NTS is involved in the modulation of dopamine neurotransmission, opioid-independent analgesia, hypothermia, and the inhibition of food intake, while in the periphery NTS promotes the growth of various normal and cancer cells and acts as a paracrine and endocrine modulator of the digestive tract. The third neurotensin receptor, NTSR3 or also called sortilin, is not a G protein-coupled receptor
VLFTAVYALIWALGAAGNALTIHLVLKKRSLRGLQGTVHYHLVSLALSDLLILLISVPIELYNFVWFHYP
WVFGDLVCRGYYFVRDICSYATVLNIASLSAERYLAICQPLRAKRLLSKRRTKWLLALIWASSLGFALPM
AFIMGQKYELETADGEPEPSSRVCTVLVSRATLKVFIQVNAFVSFVLPLALIAFLNGVTVSHLRIQSLQH
SVQVLRAIVIAYVICWLPYHARRLMFCYVPDDAWTDSLYNFYHYFYMLTNTLFYVSSAVNPLLYNVVSSS
FRKLF
>gnl|CDD|320479 cd15357, 7tmA_NMU-R2, neuromedin U receptor subtype 2, member of the class A family of seven-transmembrane G protein-coupled receptors. Neuromedin U (NMU) is a highly conserved neuropeptide with a common C-terminal heptapeptide sequence (FLFRPRN-amide) found at the highest levels in the gastrointestinal tract and pituitary gland of mammals. Disruption or replacement of residues in the conserved heptapeptide region can result in the reduced ability of NMU to stimulate smooth-muscle contraction. Two G-protein coupled receptor subtypes, NMU-R1 and NMU-R2, with a distinct expression pattern, have been identified to bind NMU. NMU-R1 is expressed primarily in the peripheral nervous system, while NMU-R2 is mainly found in the central nervous system. Neuromedin S, a 36 amino-acid neuropeptide that shares a conserved C-terminal heptapeptide sequence with NMU, is a highly potent and selective NMU-R2 agonist. Pharmacological studies have shown that both NMU and NMS inhibit food intake and reduce body weight, and that NMU increases energy expenditure
LPMSLVYAVIFVVGVIGNLLVCLVILKHQNMKTPTNYYLFSLAVSDLLVLLFGMPLEVYEMWSNYPFLFG
PVGCYFKTALFETVCFASILSVTTVSVERYVAILHPFRAKLNSTRERALKIIVVLWVLSVLFSIPNTSIH
GIKLQYFPNGTLIPDSATCTVVKPLWIYNLIIQITSLLFYVLPMGVISVLYYLMGLKLRGDKSLEADEMN
VNIQRPSRKSVTKMLFVLVLVFAICWAPFHVDRLFFSFVVEWTEPLANVFNLIHVVSGVFFYLSSAVNPI
IYNLLSRRFRTAF
>gnl|CDD|320480 cd15358, 7tmA_NMU-R1, neuromedin U receptor subtype 1, member of the class A family of seven-transmembrane G protein-coupled receptors. Neuromedin U (NMU) is a highly conserved neuropeptide with a common C-terminal heptapeptide sequence (FLFRPRN-amide) found at the highest levels in the gastrointestinal tract and pituitary gland of mammals. Disruption or replacement of residues in the conserved heptapeptide region can result in the reduced ability of NMU to stimulate smooth-muscle contraction. Two G-protein coupled receptor subtypes, NMU-R1 and NMU-R2, with a distinct expression pattern, have been identified to bind NMU. NMU-R1 is expressed primarily in the peripheral nervous system, while NMU-R2 is mainly found in the central nervous system. Neuromedin S, a 36 amino-acid neuropeptide that shares a conserved C-terminal heptapeptide sequence with NMU, is a highly potent and selective NMU-R2 agonist. Pharmacological studies have shown that both NMU and NMS inhibit food intake and reduce body weight, and that NMU increases energy expenditure
TPVCVTYLLIFVVGAVGNGLTCIVILRHKVMRTPTNYYLFSLAVSDLLVLLLGMPLELYEMWSNYPFLLG
AGGCYFKTLLFETVCFASILNVTALSVERYIAVVHPLKAKYVVTRTHAKRVIGAVWVVSILCSIPNTSLH
GIFQLTVPCRGPVPDSATCMLVKPRWMYNLIIQITTLLFFFLPMGTISVLYLLIGLQLKREKMLLVLEAK
GSKAGDSYQHRRIQQEKRRRRQVTKMLFVLVVVFGICWAPFHTDRLMWSFISQWTGELHLAFQYVHIISG
VFFYLSSAANPVLYNLMSTRFREMF
>gnl|CDD|320481 cd15359, 7tmA_LHCGR, luteinizing hormone-choriogonadotropin receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The glycoprotein hormone receptors are seven transmembrane domain receptors with a very large extracellular N-terminal domain containing many leucine-rich repeats responsible for hormone recognition and binding. The glycoprotein hormone family includes the three gonadotropins: luteinizing hormone (LH), follicle-stimulating hormone (FSH), chorionic gonadotropin (CG), and a pituitary thyroid-stimulating hormone (TSH). The glycoprotein hormones exert their biological functions by interacting with their cognate GPCRs. Both LH and CG bind to the same receptor, the luteinizing hormone-choriogonadotropin receptor (LHCGR); FSH binds to FSH-R and TSH to TSH-R. LHCGR is expressed predominantly in the ovary and testis, and plays an essential role in sexual development and reproductive processes. LHCGR couples primarily to the G(s)-protein and activates adenylate cyclase, thereby promoting cAMP production
DFLRVLIWFINILAIAGNLIVLFVLLTSRYKLTVPRFLMCNLSFADFCMGLYLLLIASVDSQTKSQYYNH
AIDWQTGSGCSTAGFFTVFASELSVYTLTVITLERWHTITYAMQLDRKLRLRHAILIMLGGWVFSLLIAV
LPLVGVSNYMKVSICLPMDIETLLSQAYILLILVLNVIAFLVICACYIKIYLAVQNPELVAKNKDTKIAK
RMAILIFTDFTCMAPISFFAISAAFKVPLITVTNSKILLVLFYPINSCANPFLYAIFTKAFRRDF
>gnl|CDD|320482 cd15360, 7tmA_FSH-R, follicle-stimulating hormone receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The glycoprotein hormone receptors are seven transmembrane domain receptors with a very large extracellular N-terminal domain containing many leucine-rich repeats responsible for hormone recognition and binding. The glycoprotein hormone family includes the three gonadotropins: luteinizing hormone (LH), follicle-stimulating hormone (FSH), chorionic gonadotropin (CG), and a pituitary thyroid-stimulating hormone (TSH). The glycoprotein hormones exert their biological functions by interacting with their cognate GPCRs. Both LH and CG bind to the same receptor, the luteinizing hormone-choriogonadotropin receptor (LHCGR); FSH binds to FSH-R and TSH to TSH-R. FSH-R functions in gonad development and is found in the ovary, testis, and uterus. Defects in this receptor cause ovarian dysgenesis type 1, and also ovarian hyperstimulation syndrome. The FSH-R activation couples to the G(s)-protein and stimulates adenylate cyclase, thereby promoting cAMP production
NILRVLIWFINILAITGNIVVLAILLTSQYKLTVPRFLMCNLAFADLCMGIYLLLIASVDIRTKSQYYNY
AIDWQTGAGCAAAGFFTVFASELSVYTLTVITLERWHTITYAMQLDRKVRLRHAAVIMVGGWIFAFTVAL
LPIFGISSYMKVSICLPMDIESPLSQAYIIFILVLNVLAFLIICACYIKIYLTVRNPNFVSSNSDTKIAK
RMAVLIFTDFLCMAPISFFAISASLKVPLITVSKSKILLVLFYPINSCANPFLYAIFTKTFRRDF
>gnl|CDD|320483 cd15361, 7tmA_LGR4, leucine-rich repeats-containing G protein-coupled receptor 4, member of the class A family of seven-transmembrane G protein-coupled receptors. The leucine-rich repeat containing G-protein coupled receptor Lgr4 (formerly known as Gpr48), together with its close family members LGR5 and LGR6, is structurally related to the glycoprotein hormone receptor family, which includes the luteinizing hormone (LH) receptor, the follicle-stimulating hormone (FSH) receptor, and the pituitary thyroid-stimulating hormone (TSH) receptor. LGR4-6 are receptors for the R-spondin (Rspo) family of secreted proteins containing two N-terminal furin-like repeats and a thrombospondin domain. The Rspo proteins are involved in regulating proliferation and differentiation of adult stem cells by potently enhancing the WNT-stimulated beta-catenin signaling. LGR4 is broadly expressed in proliferating cells, and its deficient mice display development defects in multiple organs. LGR5 acts as a marker for resident stem cell in numerous epithelial cell layers, including small intestine, colon, stomach, and kidney. LGR6 also serves as a marker of multipotent stem cells in the hair follicle that generate all skin cell lineages. Members of this group are characterized by a very large extracellular N-terminal domain containing 17 leucine-rich repeats (LRRs), flanked by cysteine-rich N- and C-terminal capping domains, and the extracellular domain is responsible for high-affinity binding with the Rspo proteins
WMIRLTVWFIFLVALFFNLLVILTTFASCTSLPSSKLFVGLIAVSNLFMGVYTGILTFLDTVSWGRFAEF
GIWWETGSGCKVAGFLAVFSSESAIFLLMLAAVERSLSAKDIMKKGKSNRLRQFQIAALLAFLVATAAGC
LPLFHGGEYSASPLCLPFPTGETPSLGFTVTLVLLNSLAFLLMAVIYTKLYCNLEKEDLSENSQSSMIKH
VAWLIFTNCIFFCPVAFFSFAPLITAISISPEIMKSVTLIFFPLPACLNPVLYVFFNPKFKEDW
>gnl|CDD|320484 cd15362, 7tmA_LGR6, leucine-rich repeats-containing G protein-coupled receptor 6, the class A of 7-transmembrane GPCRs. The leucine-rich repeat containing G-protein coupled receptor LGR5, together with its family members LGR4 and LGR6, is structurally related to the glycoprotein hormone receptor family, which includes the luteinizing hormone (LH) receptor, the follicle-stimulating hormone (FSH) receptor, and the pituitary thyroid-stimulating hormone (TSH) receptor. LGR4-6 are receptors for the R-spondin (Rspo) family of secreted proteins containing two N-terminal furin-like repeats and a thrombospondin domain. The Rspo proteins are involved in regulating proliferation and differentiation of adult stem cells by potently enhancing the WNT-stimulated beta-catenin signaling. LGR5 serves as a marker for resident stem cell in numerous epithelial cell layers, including small intestine, colon, stomach, and kidney. LGR6 is a marker for multipotent stem cells in the hair follicle that generate all skin cell lineages. In addition, LGR4 is broadly expressed in proliferating cells, and its deficient mice display development defects in multiple organs. Members of this group are characterized by a very large extracellular N-terminal domain containing 17 leucine-rich repeats (LRRs), flanked by cysteine-rich N- and C-terminal capping domains, and the extracellular domain is responsible for high-affinity binding with the Rspo proteins
WVVRLGVWAIVLVSVLCNGLVILTVFASPGYLSPVKFVIGSIAGANLLTGICTGTLALVDALTFGQFAKY
GARWETGLGCRATGFLSVFASEASILLLTLAAVQCSVSVSCVRAYGKSPSLGSVRAAALCCLALSLTAAA
LPLFSVGEYGASPLCLPSPLPDGKPSTLGFTVALIMMNTLCFLVITGTYIKLYCDLLKGEFDAIWDCAMI
KHVAWLIFTNCLLYCPVAFLTFSSLLNLFPISPEVIKSVLLVVLPLPACLNPLLYLLFNPHFRDDL
>gnl|CDD|320485 cd15363, 7tmA_LGR5, leucine-rich repeats-containing G protein-coupled receptor 5, member of the class A family of seven-transmembrane G protein-coupled receptors. The leucine-rich repeat containing G-protein coupled receptor LGR6, together with its family members LGR4 and LGR5, is structurally related to the glycoprotein hormone receptor family, which includes the luteinizing hormone (LH) receptor, the follicle-stimulating hormone (FSH) receptor, and the pituitary thyroid-stimulating hormone (TSH) receptor. LGR4-6 are receptors for the R-spondin (Rspo) family of secreted proteins containing two N-terminal furin-like repeats and a thrombospondin domain. The Rspo proteins are involved in regulating proliferation and differentiation of adult stem cells by potently enhancing the WNT-stimulated beta-catenin signaling. LGR6 serves as a marker of multipotent stem cells in the hair follicle that generate all skin cell lineages, whereas LGR5 is a marker for resident stem cell in numerous epithelial cell layers, including small intestine, colon, stomach, and kidney. In addition, LGR4 is broadly expressed in proliferating cells, and its deficient mice display development defects in multiple organs. Members of this group are characterized by a very large extracellular N-terminal domain containing 17 leucine-rich repeats (LRRs), flanked by cysteine-rich N- and C-terminal capping domains, and the extracellular domain is responsible for high-affinity binding with the Rspo proteins
WLIRIGVWTIAVLALVCNALVTATVFRSPLYISSIKLLIGLIAIVNMLMGVSSAVLAGVDAFTFGSFAQH
GAWWESGVGCQITGFLSIFASESSVFLLTLAALERGFSVKCSTKFETKSPFLSLKAIILLCFLLALTIAV
IPLLGGSEYGASPLCLPLPFGEPSAMGYMVALVLLNSLCFLVMTIAYTKLYCSLEKGELENIWDCSMVKH
IALLLFTNCILYCPVAFLSFSSLLNLTFISPEVIKFILLVIVPLPACLNPLLYILFNPHFKEDL
>gnl|CDD|320486 cd15364, 7tmA_GPR132_G2A, proton-sensing G protein-coupled receptor 132, member of the class A family of seven-transmembrane G protein-coupled receptors. The G2 accumulation receptor (G2A, also known as GPR132) is a member of the proton-sensing G-protein-coupled receptor (GPCR) family which also includes the T cell death associated gene-8 (TDAG8, GPR65) receptor, ovarian cancer G-protein receptor 1 (OGR-1, GPR68), and G-protein-coupled receptor 4 (GPR4). Proton-sensing G-protein coupled receptors sense pH of 7.6 to 6.0 and mediates a variety of biological activities in neutral and mildly acidic pH conditions, whereas the acid-sensing ionotropic ion channels typically sense strong acidic pH. G2A was originally identified as a stress-inducible receptor that causes the cell cycle arrest at G2/M phase when serum is deprived. Lysophosphatidylcholine was identified as a ligand for G2A, and whose overexpression was shown to induce cell proliferation, oncogenic transformation, and apoptosis
IFLVVVYSVVFALGFPANCLTLWLTLLQVRRKNVLAVYLFSLSLCELLYLGTLPLWTIYVSNNHKWPWGS
LACKITGYIFFCNIYISILLLCCISIDRFVAVVYALESRGRRRQRIAAFISFLIFIVVGLVHSPVFIMRE
GQTEGSHTCFETLQMDTQVAGFYYARFCIGFAIPLAILIFTNYRIFRSIQTSTSLTPHQKAKVKYLAIAV
IVIFLICFAPYHLVLLVRAIAFSLYPNGMCGFEERIYTPSVIFLCLSTVNSVADPIIYVLVSENVRQDI
>gnl|CDD|320487 cd15365, 7tmA_GPR65_TDAG8, proton-sensing G protein-coupled receptor 65, member of the class A family of seven-transmembrane G protein-coupled receptors. The T cell death associated gene-8 receptor (TDAG8, also known as GPR65) is a member of the proton-sensing G-protein-coupled receptor (GPCR) family which also includes the G2 accumulation receptor (G2A, also known as GPR132), ovarian cancer G-protein receptor 1 (OGR-1, GPR68), and G-protein-coupled receptor 4 (GPR4). Proton-sensing G-protein coupled receptors sense pH of 7.6 to 6.0 and mediates a variety of biological activities in neutral and mildly acidic pH conditions, whereas the acid-sensing ionotropic ion channels typically sense strong acidic pH. Activation of TDAG8 by extracellular acidosis increases the cAMP production, stimulates Rho, and induces stress fiber formation. TDAG8 has also been shown to regulate the extracellular acidosis-induced inhibition of pro-inflammatory cytokine production in peritoneal macrophages
YLFPFVYIFVIVISIPSNCISLYVSCLQIRKKNELGVYLFNLSLSDLLYIVILPLWIDYLWNGDNWTLSG
FVCIFSAFLLYTNFYTSTALLTCIALDRYLAVVHPLKFMHLRTIRTALSVSVAIWLLEICFNAVILTWED
SFHESSSHTLCYDKFPLEDWQARLNLFRICLGYLLPLLIILFCYWKIYQAVRSNQATEDQEKKKIFKLLL
LITVTFVICFTPYHVVLLIRSIVEPCDCRNAKWLYTLYKITVALTSLNCIADPFLYCFVTESGRADI
>gnl|CDD|320488 cd15366, 7tmA_GPR4, proton-sensing G protein-coupled receptor 4, member of the class A family of seven-transmembrane G protein-coupled receptors. G-protein-coupled receptor 4 (GPR4) is a member of the proton-sensing G-protein-coupled receptor (GPCR) family which also includes the G2 accumulation receptor (G2A, also known as GPR132), the T cell death associated gene-8 receptor (TDAG8, GPR65), ovarian cancer G-protein receptor 1 (OGR-1, GPR68), and G-protein-coupled receptor 4 (GPR4). Proton-sensing G-protein coupled receptors sense pH of 7.6 to 6.0 and mediates a variety of biological activities in neutral and mildly acidic pH conditions, whereas the acid-sensing ionotropic ion channels typically sense strong acidic pH. GPR4 overexpression in melanoma cells was shown to reduce cell migration, membrane ruffling, and cell spreading under acidic pH conditions. Activation of GPR4 via extracellular acidosis is coupled to the G(s), G(q), and G(12/13) pathways
LFPPTLYIIVIVLGLPTNCLALWAAYLQVRQRNELGVYLLNLSVSDLLYIATLPLWIDYFLHRDNWIHGP
ESCKLFGFIFYTNIYISIAFLCCISVDRYLAVAHPLRFAKVRRVKTAVAVSAVVWAIEIGANSAPLFHDE
LFRDRYNHTFCFEKYPMEDWVAWMNLYRVFVGFLFPWVLMLFSYRGILRAVRGNVSTEQQEKAKIKRLAL
SLIAIVLLCFAPYHVLLLSRSVVYLGKPCDCGFEERVFTAYHVSLALTSLNCVADPILYCLVNEGARSDV
>gnl|CDD|320489 cd15367, 7tmA_GPR68_OGR1, G protein-coupled receptor 68, member of the class A family of seven-transmembrane G protein-coupled receptors. The ovarian cancer G-protein receptor 1 (OGR1, also known as GPR68) is a member of the proton-sensing G-protein-coupled receptor (GPCR) family which also includes the G2 accumulation receptor (G2A, also known as GPR132), the T cell death associated gene-8 receptor (TDAG8, GPR65), and the G-protein-coupled receptor 4 (GPR4). Proton-sensing G-protein coupled receptors sense pH of 7.6 to 6.0 and mediates a variety of biological activities in neutral and mildly acidic pH conditions, whereas the acid-sensing ionotropic ion channels typically sense strong acidic pH. Knock-out mice studies have suggested that OGR1 plays a role in the regulation of insulin secretion and glucose metabolism. OGR1 couples to G(q/11) proteins and activates phospholipase C and Ca2+ signaling pathways
TLFPVVYILVLVVGLPANCLSLYYGYLQIKAKNELGIYLCNLTVADLLYIFSLPFWLQYVLQHDNWTYSE
LLCKICGILLYENIYISIGFLCCISVDRYLAVVHPFRFHAFRTMKAATLVSTVIWLKELMTCVFFFLHGE
ISKDKENHSVCFEHYPIKAWEHNINYYRFYAGFLFPIFLLSFSYCRILRAVRKSHGTQKSQKIQIKRLVL
STVVIFLVCFGPYHILLLVRSVFERDCNFAEGIFNYYHFSLLLTSFNCVADPVLYCFASESTYHDF
>gnl|CDD|320490 cd15368, 7tmA_P2Y8, purinergic receptor P2Y8, member of the class A family of seven-transmembrane G protein-coupled receptors. P2Y8 (or P2RY8) expression is often increased in leukemia patients, and it plays a role in the pathogenesis of acute leukemia. P2Y8 is phylogenetically closely related to the protease-activated receptors (PARs), which are activated by serine proteases such as thrombin, trypsin, and tryptase. These proteases cleave the extracellular domain of the receptor to form a new N-terminus, which in turn functions as a tethered ligand. The newly-formed tethered ligand binds intramolecularly to activate the receptor and triggers G-protein binding and intracellular signaling. Four different types of the protease-activated receptors have been identified (PAR1-4) and are predominantly expressed in platelets. PAR1, PA3, and PAR4 are activated by thrombin, whereas PAR2 is activated by trypsin. The PARs are known to couple with several G-proteins including Gi (cAMP inhibitory), G12/13 (Rho and Ras activation), and Gq (calcium signaling) to activate downstream signaling messengers which induces numerous cellular and physiological effects
VILPVVYSLVALISIPGNLFSLWLLCFHTKPKTPSIIFMINLSLTDLMLACFLPFQIVYHIQRNHWIFGK
PLCNVVTVLFYANMYSSILTMTCISIERYLGVVYPMRSMRWRKKRYAVAACIGMWLLVLTALSPLERTDL
TYYVKELNITTCFDVLKWTMLPNIAAWAAFLFTLFILLFLIPFIITVYCYVLIILKLVQTSERYGREQKR
RAIYLALIVLLVFITCFAPNNFILLAHMVSRLFYGKSLYHAYKLTLSLSCLNSCLDPFIYYFASKEFRKK
L
>gnl|CDD|320491 cd15369, 7tmA_PAR1, protease-activated receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. Protease-acted receptors (PARs) are seven-transmembrane proteins that belong to the class A G-protein coupled receptor (GPCR) family. Four different types of the protease-activated receptors have been identified: PAR1, PAR2, PAR3, and PAR4. PARs are predominantly expressed in platelets and are activated by serine proteases such as thrombin, trypsin, and tryptase. These proteases cleave the extracellular domain of the receptor to form a new N-terminus, which in turn functions as a tethered ligand. The newly-formed tethered ligand binds intramolecularly to activate the receptor and triggers G-protein binding and intracellular signaling. PAR1, PA3, and PAR4 are activated by thrombin, whereas PAR2 is activated by trypsin. The PARs are known to couple with several G-proteins including Gi (cAMP inhibitory), G12/13 (Rho and Ras activation), and Gq (calcium signaling) to activate downstream signaling messengers which induces numerous cellular and physiological effects
RFVPSVYTIVFVISLPLNILALVVFLRKMRVKKPAVIYMLNLACADLLFVLLLPFKIAYHFSGNDWLFGE
AMCRVVTAAFYCNMYCSILLMTCISVDRFLAVVYPMQSLSWRTLRRASFTCAAIWLLSIAGVVPLLLSEQ
TIQIPDLGITTCHDVLNEQLLMGYYVYYFSIFSCLFFFVPLIITTVCYVSIIRCLSSSSDVANSSKKTRA
LFMAVAVFCVFVICFGPTNVLLLAHYVRFAYTSTNDASYFAYLLCVCVGSISCCLDPLIYYYGSSQCQKQ
L
>gnl|CDD|341349 cd15370, 7tmA_PAR2, protease-activated receptor 2, member of the class A family of seven-transmembrane G protein-coupled receptors. Protease-acted receptors (PARs) are seven-transmembrane proteins that belong to the class A G-protein coupled receptor (GPCR) family. Four different types of the protease-activated receptors have been identified: PAR1, PAR2, PAR3, and PAR4. PARs are predominantly expressed in platelets and are activated by serine proteases such as thrombin, trypsin, and tryptase. These proteases cleave the extracellular domain of the receptor to form a new N-terminus, which in turn functions as a tethered ligand. The newly-formed tethered ligand binds intramolecularly to activate the receptor and triggers G-protein binding and intracellular signaling. PAR1, PA3, and PAR4 are activated by thrombin, whereas PAR2 is activated by trypsin. The PARs are known to couple with several G-proteins including Gi (cAMP inhibitory), G12/13 (Rho and Ras activation), and Gq (calcium signaling) to activate downstream signaling messengers which induces numerous cellular and physiological effects
VFLPIVYIIVFVVGLPSNAMALWVFLFRTKKKHPAVIYMANLALADLLFVIWFPLKIAYHINGNNWIYGE
ALCKVLIGFFYGNMYCSILFMTCLSVQRYWVIVNPMSHSRKKANIAIGISLAIWLLILLVTIPLYLVKQT
VFIPALDITTCHDVLPEQLLVGDMFNYFLSLAIGVFLFPAFLTAVAYVLMIRALKSSINDESIEKKRKRA
IKLIVTVLVMYLICFTPSNLLLVVHYFLLKNQGQSSVYAFYITALCLSTLNSCIDPFVYYFVSHDFRDHV
>gnl|CDD|320493 cd15371, 7tmA_PAR3, protease-activated receptor 3, member of the class A family of seven-transmembrane G protein-coupled receptors. Protease-acted receptors (PARs) are seven-transmembrane proteins that belong to the class A G-protein coupled receptor (GPCR) family. Four different types of the protease-activated receptors have been identified: PAR1, PAR2, PAR3, and PAR4. PARs are predominantly expressed in platelets and are activated by serine proteases such as thrombin, trypsin, and tryptase. These proteases cleave the extracellular domain of the receptor to form a new N-terminus, which in turn functions as a tethered ligand. The newly-formed tethered ligand binds intramolecularly to activate the receptor and triggers G-protein binding and intracellular signaling. PAR1, PA3, and PAR4 are activated by thrombin, whereas PAR2 is activated by trypsin. The PARs are known to couple with several G-proteins including Gi (cAMP inhibitory), G12/13 (Rho and Ras activation), and Gq (calcium signaling) to activate downstream signaling messengers which induces numerous cellular and physiological effects
KLIPAVYIIVVVLGVPSNAIILWMLFFRLRSVCTAIFYANLAISDLLFCITLPFKIVYHLNGNNWVFGET
MCRIITITFYGNMYCSILLLTCISINRYLAIVHPFIYRSLPKKTYAVLICALVWTIVFLYMLPFFILKQT
YYLKELNITTCHDVLPECEQNSNFQFYYFISMAVFGFLIPLVITIFCYISIIRTLNAYEHKWFWYVKITA
LVLIIFTICFAPSNVILIIHHFNYYYFNNDNLYSIYLIALCLGSLNSCLDPFLYFLMSKWRSQS
>gnl|CDD|320494 cd15372, 7tmA_PAR4, protease-activated receptor 4, member of the class A family of seven-transmembrane G protein-coupled receptors. Protease-acted receptors (PARs) are seven-transmembrane proteins that belong to the class A G-protein coupled receptor (GPCR) family. Four different types of the protease-activated receptors have been identified: PAR1, PAR2, PAR3, and PAR4. PARs are predominantly expressed in platelets and are activated by serine proteases such as thrombin, trypsin, and tryptase. These proteases cleave the extracellular domain of the receptor to form a new N-terminus, which in turn functions as a tethered ligand. The newly-formed tethered ligand binds intramolecularly to activate the receptor and triggers G-protein binding and intracellular signaling. PAR1, PA3, and PAR4 are activated by thrombin, whereas PAR2 is activated by trypsin. The PARs are known to couple with several G-proteins including Gi (cAMP inhibitory), G12/13 (Rho and Ras activation), and Gq (calcium signaling) to activate downstream signaling messengers which induces numerous cellular and physiological effects
RLVPSLYTLVFLVGLPANGLALWVLATQVKRLPSTIFLINLAVADLLLILVLPFKISYHFLGNNWPFGEG
LCRVVTAFFYGNMYCSVLLLMCISLDRYLAVVHPFFARTLRSRRFALCMCTAIWLIAAALTLPLTLQRQS
YPLERLNITLCHDVLPLDEQDTYLFYYFACLAVLGFLLPLVVILFCYGSVLHTLLRSGQRYGHAMKLTVL
VLVSFVLCFTPSNLLLLLHYSDPTLDDGGNLYIVYMVSLAISTLNSCVDPFIYYYVSEEFRDKV
>gnl|CDD|320495 cd15373, 7tmA_P2Y2, P2Y purinoceptor 2, member of the class A family of seven-transmembrane G protein-coupled receptors. P2Y2 belongs to the P2Y receptor family of purinergic G-protein coupled receptors and is implicated to play a role in the control of the cell cycle of endometrial carcinoma cells. The P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5, and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12, and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-glucose (P2Y14)
ILLPVSYGIVFVVGLVLNILALYVFLFRTKPWNASTTYMFNLAISDTLYVLSLPLLVYYYADENDWPFSE
ALCKIVRFLFYTNLYCSILFLLCISVHRFLGVCYPVRSLRWLKVRYARIVSVVVWVIVLACQSPVLYFVT
TSDKGGNITCHDTSSPELFDQFVVYSSVMLVLLFCVPFVVILVCYALMVRKLLKPSAGTSTNSRSKKKSV
KMIIIVLAVFILCFLPFHVTRTLYYSFRSMDLSCGTLNAINLAYKVTRPLASANSCLDPILYFLAGQSFR
SNL
>gnl|CDD|320496 cd15374, 7tmA_P2Y4, P2Y purinoceptor 4, member of the class A family of seven-transmembrane G protein-coupled receptors. P2Y4 belongs to the P2Y receptor family of purinergic G-protein coupled receptors. This family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5, and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12, and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-glucose (P2Y14)
ILLPVSYGLVFVVGLPLNATALWLFIKRMRPWNPTTVYMFHLALSDTLYVLSLPTLIYYYADHNHWPFGV
VACKIVRFLFYANLYCSILFLTCISVHRYVGICHPIRALRWVKPRHAYLICASVWLVVTVCLVPNLIFVT
TSRKDNITLCHDTTRPEEFDHYVHYSSAVMVLLFGIPCLVIVVCYGLMARRLCKPRVGSSRQQGPSSKKR
SLKTIIMVLTVFAICFVPFHITRTLYYVARLLKADCDTLNIINVTYKVTRPLASANSCLDPILYFLAGDK
YRRRL
>gnl|CDD|320497 cd15375, 7tmA_OXGR1, 2-oxoglutarate receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. 2-oxoglutarate receptor 1 (OXGR1) is also known as GPR80, GPR99, or P2Y15. OXGR1 functions as a receptor for alpha-ketoglutarate, a citric acid cycle intermediate, and acts exclusively through a G(q)-dependent pathway. OXGR1 belongs to the class A GPCR superfamily and is phylogenetically related to the purinergic P2Y1-like receptor subfamily, whose members are coupled to G(q) protein to activate phospholipase C (PLC). OXGR1 has also been reported as a potential third cysteinyl leukotriene receptor with specificity for leukotriene E4
YYLPVMYSIIFIVGFPGNIIAIFVYLFKMRPWKSSTIIMLNLALTDLLYVTSLPFLIYYYINGESWIFGE
FMCKFIRFIFHFNLYGSILFLTCFSIFRYVVIVHPLRAFQVQKRRWAIVACAVVWVISLAEVSPMTFLIT
TKEKNNRTICLDFTSSDNLNTIWWYNWILTVLGFLLPLVIVTLCYTRIIYTLAKGPHTGSASKQKARRLI
ILILLVFYVCFLPFHILRVVRIETRLPPVSCCLKHQVHAIYIITRPLAALNTFGNLLLYVVSGDNFQQAF
>gnl|CDD|320498 cd15376, 7tmA_P2Y11, P2Y purinoceptor 11, member of the class A family of seven-transmembrane G protein-coupled receptors. P2Y11 belongs to the P2Y receptor family of purinergic G-protein coupled receptors. The activation of P2Y11 is a major pathway of macrophage activation that leads to the release of cytokines. The P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5, and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12, and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-glucose (P2Y14)
DFLWPILGVEFLVAVLGNGLALWLFVTRERRPWHTGVVFSFNLAVSDLLYALSLPLLAAYYYPPKNWRFG
EAACKLERFLFTCNLYGSIFFITCISLNRYLGIVHPFFTRSHVRPKHAKLVSLAVWLLVAALSAPVLSFS
HLEVERHNKTECLGTAVDSRLPTYLPYSLFLAVVGCGLPFLLTLASYLAIVWAVLRSPGITTLEKRKVAA
LVAVVVALYAVSFVPYHILRNLNLYRRLQWLKAAASLRIYFAYQVTKGLVTLNMCIHPLLYMAVADSIRL
CCCG
>gnl|CDD|341350 cd15377, 7tmA_P2Y1, P2Y purinoceptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. P2Y1 belongs to the P2Y receptor family of purinergic G-protein coupled receptors. This family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5, and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12, and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-glucose (P2Y14)
YYLPAVYILVFITGFLGNSVAIWMFVFHMKPWSGISVYMFNLALADFLYVLTLPALIFYYFNKTDWIFGD
AMCKLQRFIFHVNLYGSILFLTCISVHRYTGVVHPLKSLGRLKKKNAICISVLVWLIVVVAISPILFYSG
TGVRKNKTITCYDTTSDEYLRSYFIYSMCTTVAMFCVPFILILGCYGLIVRALIYKDMKYTEENNAPLRR
KSIYLVIIVLTVFAVSYLPFHVMKTLNLRARLDFQTPAMCAFNDRVYATYQVTRGLASLNSCVDPILYFL
AGDTFRRRL
>gnl|CDD|320500 cd15378, 7tmA_SUCNR1_GPR91, succinate receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. Succinate receptor (SUCNR1) GPR91 exclusively couples to G(i) protein to inhibit cAMP production and also activates PLC-beta to increase intracellular calcium concentrations in an inositol phosphate dependent mechanism. Succinate, an intermediate molecule of the citric cycle, is shown to cause cardiac hypertrophy via GPR91 activation. Furthermore, succinate-induced GPR91 activation is involved in the regulation of renin-angiotensin system and is suggested to play an important role in the development of renovascular hypertension and diabetic nephropathy. SUCNR1 belongs to the class A GPCR superfamily and is phylogenetically related to the purinergic P2Y1-like receptor subfamily, whose members are coupled to G(q) protein to activate phospholipase C (PLC)
YYLPTMYSIEFVLGFIGNTIVILGYIFCLKNWKSSNIYLFNLSVSDLAFLCTLPMLVYSYSNGQWLFGDF
LCKSNRYLLHANLYSSILFLTFISIDRYLLIKYPFREHILQKKRSAVAISLAIWVLVTLELLPILTFIGP
NLKDNVTKCKDYASSGDATNSLIYSLFLTVTGFLIPLCVMCFFYYKIALFLKNRNRQLANATSFEKPLTL
VILAVVIFSVLFTPYHVMRNVRIASRLDSIGVSECTLIIIKSLYIVTRPIAFLNSVINPVFYFLMGDHFR
EML
>gnl|CDD|320501 cd15379, 7tmA_P2Y6, P2Y purinoceptor 6, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes mammalian P2Y6, avian P2Y3, and similar proteins. P2Y3 is the avian homolog of mammalian P2Y6. They belong to the G(i) class of a family of purinergic G-protein coupled receptors. The P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5, and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12, and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-glucose (P2Y14)
VLLPLVYSVVFLLGLPLNAVVIGQIWATRQALSRTTIYMLNLATADLLYVCSLPLLIYNYTQKDYWPFGD
FTCRLVRFQFYTNLHGSILFLTCISVQRYLGICHPLASWHKKKGKKLTWLVCGAVWLVVIAQCLPTFVFA
STGTQRNRTVCYDLSPPARSTAYFPYGITLTRTGFLLPFAARLACYCSMATILCRVVIAVAVVAAPGEKR
GKAARMIIVVAAVFLISFLPFHYTKTRYLQVRSWDGGPCTTRQAFAEAYKRTRPFASMNSVLDPILFYFT
QSKFRPRT
>gnl|CDD|320502 cd15380, 7tmA_BK-1, bradykinin receptor B1, member of the class A family of seven-transmembrane G protein-coupled receptors. The bradykinin receptor family is a group of the seven transmembrane G-protein coupled receptors, whose endogenous ligand is the pro-inflammatory nonapeptide bradykinin that mediates various vascular and pain responses. Two major bradykinin receptor subtypes, B1 and B2, have been identified based on their pharmacological properties. The B1 receptor is rapidly induced by tissue injury and inflammation, whereas the B2 receptor is ubiquitously expressed on many tissue types. Both receptors contain three consensus sites for N-linked glycosylation in extracellular domains and couple to G(q) protein to activate phospholipase C, leading to phosphoinositide hydrolysis and intracellular calcium mobilization. They can also interact with G(i) protein to inhibit adenylate cyclase and activate the MAPK (mitogen-activated protein kinase) pathways
RVLPTFIIAICFFGLLGNLFVLFVFLLPRRRLTIAEIYLANLAASDLVFVLGLPFWAENIRNQFNWPFGN
FLCRVISGVIKANLFISIFLVVAISQDRYRTLVHTMTSRRQRSRRQAQVICLLIWVFGGLLSIPTFLFRS
VKHVPDLNISACILLFPHEAWHFARRVELNIVGFLLPLAAIVFFNFHIIASLRERTEESRKRCGGLKDTK
ATRLILTLVLMFLVCWTPYHFFAFLDFLFQVEVIQGCFWEEFIDLGLQLANFFAFANSCLNPVIYVFAGK
LFRTKV
>gnl|CDD|320503 cd15381, 7tmA_BK-2, bradykinin receptor B2, member of the class A family of seven-transmembrane G protein-coupled receptors. The bradykinin receptor family is a group of the seven transmembrane G-protein coupled receptors, whose endogenous ligand is the pro-inflammatory nonapeptide bradykinin that mediates various vascular and pain responses. Two major bradykinin receptor subtypes, B1 and B2, have been identified based on their pharmacological properties. The B1 receptor is rapidly induced by tissue injury and inflammation, whereas the B2 receptor is ubiquitously expressed on many tissue types. Both receptors contain three consensus sites for N-linked glycosylation in extracellular domains and couple to G(q) protein to activate phospholipase C, leading to phosphoinositide hydrolysis and intracellular calcium mobilization. They can also interact with G(i) protein to inhibit adenylate cyclase and activate the MAPK (mitogen-activated protein kinase) pathways
TFQPIYLWIIFVLGTIENAFVLIVFCLHKSSCTVAEIYLGNLAAADLLLVCCLPFWAINISNGFNWPFGE
FLCKSVNAVIYMNLYSSIYFLMMVSIDRYLALVKTMSSGRMRRPACAKLNCLIIWMFGLLMSTPMIVFRT
VMYFPEYNITACVLDYPSEGWHVALNILLNVVGFLIPLSIITFCSTQIIQVLRNNKMQKFKEIQTERKAT
VLVLAVLLMFFICWLPFHIFTFLDTLHKLGLISGCRWEDILDIGTQIATFLAYSNSCLNPLLYVIVGKHF
RKKA
>gnl|CDD|320504 cd15382, 7tmA_AKHR, adipokinetic hormone receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Adipokinetic hormone (AKH) is a lipid-mobilizing hormone that is involved in control of insect metabolism. Generally, AKH behaves as a typical stress hormone by mobilizing lipids, carbohydrates and/or certain amino acids such as proline. Thus, it utilizes the body's energy reserves to fight the immediate stress problems and subdue processes that are less important. Although AKH is known to responsible for regulating the energy metabolism during insect flight, it is also found in insects that have lost its functional wings and predominantly walk for their locomotion. AKH is structurally related to the mammalian gonadotropin-releasing hormone (GnRH) and they share a common ancestor. Both GnRH and AKH receptors are members of the class A of the seven-transmembrane, G-protein coupled receptor (GPCR) superfamily
LVSIIVYSVLFLIAAVGNLTVLLILLRNRRRKRSRVNILLMHLAIADLLVTFIMMPLEIGWAATVAWLAG
DFLCRLMLFFRAFGLYLSSFVLVCISLDRYFAILKPLRLSDARRRGRIMLAVAWVISFLCSIPQSFIFHV
ESHPCVTWFSQCVTFNFFPSHDHELAYNIFNMITMYALPLIIIVFCYSLILCEISRKSKEKKEDVSEKSS
SVRLRRSSVGLLERARSRTLKMTIVIVLVFIICWTPYFIMSLWYWFDRESASKVDPRIQKGLFLFAVSNS
CMNPIVYGYFSIDLRREL
>gnl|CDD|320505 cd15383, 7tmA_GnRHR_vertebrate, vertebrate gonadotropin-releasing hormone receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. GnRHR, also known as luteinizing hormone releasing hormone receptor (LHRHR), plays an central role in vertebrate reproductive function; its activation by binding to GnRH leads to the release of follicle stimulating hormone (FSH) and luteinizing hormone (LH) from the pituitary gland. GnRHR is expressed predominantly in the gonadotrope membrane of the anterior pituitary as well as found in numerous extrapituitary tissues including lymphocytes, breast, ovary, prostate, and cancer cell lines. There are at least two types of GnRH receptors, GnRHR1 and GnRHR2, which couple primarily to G proteins of the Gq/11 family. GnRHR is closely related to the adipokinetic hormone receptor (AKH), which binds to a lipid-mobilizing hormone that is involved in control of insect metabolism. They share a common ancestor and are members of the class A of the seven-transmembrane, G-protein coupled receptor (GPCR) superfamily
KVRVAVTFVLFVLSACSNLAVLWSATRNRRRKLSHVRILILHLAAADLLVTFVVMPLDAAWNVTVQWYAG
DLACRLLMFLKLFAMYSSAFVTVVISLDRHAAILNPLAIGSARRRNRIMLCAAWGLSALLALPQLFLFHT
VTATPPVNFTQCATHGSFPAHWQETLYNMFTFFCLFLLPLLIMIFCYTRILLEISRRMKEKKDSAKNEVA
LRSSSDNIPKARMRTLKMTIVIVSSFIVCWTPYYLLGLWYWFSPEMLEQTVPESLSHILFLFGLLNACLD
PLIYGLFTISFRRGL
>gnl|CDD|320506 cd15384, 7tmA_GnRHR_invertebrate, invertebrate gonadotropin-releasing hormone receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. GnRHR, also known as luteinizing hormone releasing hormone receptor (LHRHR), plays an central role in vertebrate reproductive function; its activation by binding to GnRH leads to the release of follicle stimulating hormone (FSH) and luteinizing hormone (LH) from the pituitary gland. GnRHR is expressed predominantly in the gonadotrope membrane of the anterior pituitary as well as found in numerous extrapituitary tissues including lymphocytes, breast, ovary, prostate, and cancer cell lines. There are at least two types of GnRH receptors, GnRHR1 and GnRHR2, which couple primarily to G proteins of the Gq/11 family. GnRHR is closely related to the adipokinetic hormone receptor (AKH), which binds to a lipid-mobilizing hormone that is involved in control of insect metabolism. They share a common ancestor and are members of the class A of the seven-transmembrane, G-protein coupled receptor (GPCR) superfamily
LLKIVVLAVMFVISFIGNLLTIIQIYRLRRSRRTIYSLLLHLAIADLLVTFFCIPSEAIWAYTVAWLAGN
TMCKLVKYLQVFGLYLSTYITVLISLDRCVAILYPMKRNQAPERVRRMVTVAWILSPIFSIPQAVIFHVE
RGPFVEDFHQCVTYGFYTAEWQEQLYNMLSLVFMFPIPLVIMVTCYVLIFITLSKSSRDFQGLEIYTRNR
GPNRQRLFHKAKVKSLRMSAVIVTAFILCWTPYYVIMIWFLFFNPYPLNDILFDVIFFFGMSNSCVNPLI
YGAFHITKKKGGK
>gnl|CDD|320507 cd15385, 7tmA_V1aR, vasopressin receptor subtype 1A, member of the class A family of seven-transmembrane G protein-coupled receptors. V1a-type receptor is a G(q/11)-coupled receptor that mediates blood vessel constriction. Vasopressin (also known as arginine vasopressin or anti-diuretic hormone) is synthesized in the hypothalamus and is released from the posterior pituitary gland. The actions of vasopressin are mediated by the interaction of this hormone with three receptor subtypes: V1aR, V1bR, and V2R. These subtypes are differ in localization, function, and signaling pathways. Activation of V1aR and V1bR stimulate phospholipase C, while activation of V2R stimulates adenylate cyclase. Although vasopressin and oxytocin differ only by two amino acids and stimulate the same cAMP/PKA pathway, they have divergent physiological functions. Vasopressin is involved in regulating blood pressure and the balance of water and sodium ions, whereas oxytocin plays an important role in the uterus during childbirth and in lactation
KLEIAVLAVIFAVAVIGNSSVLLALYKTKKKASRMHLFIKHLSLADLVVAFFQVLPQLCWDITYRFYGPD
FLCRIVKHLQVLGMFASTYMLVMMTADRYIAICHPLKTLQQPTKRSYLMIGSAWALSFILSTPQYFIFSL
SEIENGSGVYDCWANFIVPWGIKAYITWITISIFVVPVIILLTCYGFICYNIWRNIKCKTRRGLSDNALK
NILLAVCVSSVKTISRAKIRTVKMTFVIVLAYIVCWAPFFTIQMWSVWDQNFPWDESENTAVTITALLAS
LNSCCNPWIYMFFSGHLLQDF
>gnl|CDD|320508 cd15386, 7tmA_V1bR, vasopressin receptor subtype 1B, member of the class A family of seven-transmembrane G protein-coupled receptors. The V1b receptor is specifically expressed in corticotropes of the anterior pituitary and plays a critical role in regulating the activity of hypothalamic-pituitary-adrenal axis, a key part of the neuroendocrine system that controls reactions to stress, by maintaining adrenocorticotropic hormone (ACTH) and corticosterone levels. Vasopressin (also known as arginine vasopressin or anti-diuretic hormone) is synthesized in the hypothalamus and is released from the posterior pituitary gland. The actions of vasopressin are mediated by the interaction of this hormone with three receptor subtypes: V1aR, V1bR, and V2R. These subtypes are differ in localization, function, and signaling pathways. Activation of V1aR and V1bR stimulate phospholipase C, while activation of V2R stimulates adenylate cyclase. Although vasopressin and oxytocin differ only by two amino acids and stimulate the same cAMP/PKA pathway, they have divergent physiological functions. Vasopressin is involved in regulating blood pressure and the balance of water and sodium ions, whereas oxytocin plays an important role in the uterus during childbirth and in lactation
KVEIGVLAAILVVATAGNLAVLLAMYRMRRKMSRMHLFVLHLALTDLVVALFQVLPQLIWEITYRFQGPD
LLCRAVKYLQVLSMFASTYMLIMMTVDRYIAVCHPLRTLQQPSRQAYLMIGATWLLSCILSLPQVFIFSL
REVDQGSGVLDCWADFGFPWGAKAYITWTTLSIFVLPVAILIVCYSLICYEICKNLKGKTQTSRSEGGGW
RTQGMPSRVSSVRTISRAKIRTVKMTFVIVLAYIACWAPFFSVQMWSVWDENAPDEDSSDFAFTITMLLA
SLSSCCNPWIYMFFSGHLLQDV
>gnl|CDD|320509 cd15387, 7tmA_OT_R, oxytocin receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Oxytocin is a peptide of nine amino acids synthesized in the hypothalamus and is released from the posterior pituitary gland. Oxytocin plays an important role in sexual reproduction of both sexes and is structurally very similar to vasopressin. Although vasopressin and oxytocin differ only by two amino acids and stimulate the same cAMP/PKA pathway, they have divergent physiological functions. Vasopressin is involved in regulating blood pressure and the balance of water and sodium ions, whereas oxytocin plays an important role in the uterus during childbirth and in lactation
KVEVTVLALILFLALTGNICVLLAIHTTRHKHSRMYFFMKHLSIADLVVAVFQVLPQLIWDITFRFYGPD
FLCRLVKYLQVVGMFASTYMLLLMSIDRCLAICQPLRSLHRRSDRVYVLFSWLLSLVFSIPQVHIFSLRE
VGNGVYDCWADFIQPWGPKAYITWITLSVYIIPVLILSVCYGLISFKIWQNVKLKTRRETKTPLSSAASG
GAALARVSSVKLISKAKIRTVKMTFVIVLAYIVCWTPFFFVQMWSVWDPNAPKEASPFIIAMLLASLNSC
CNPWIYMFFTGHLFHDL
>gnl|CDD|320510 cd15388, 7tmA_V2R, vasopressin receptor 2, member of the class A family of seven-transmembrane G protein-coupled receptors. The vasopressin type 2 receptor (V2R) is a G(s)-coupled receptor that controls balance of water and sodium ion by regulating their reabsorption in the renal collecting duct. Mutations of V2R is responsible for nephrogenic diabetes insipidus. Vasopressin (also known as arginine vasopressin or anti-diuretic hormone) is synthesized in the hypothalamus and is released from the posterior pituitary gland. The actions of vasopressin are mediated by the interaction of this hormone with three receptor subtypes: V1aR, V1bR, and V2R. These subtypes are differ in localization, function, and signaling pathways. Activation of V1aR and V1bR stimulate phospholipase C, while activation of V2R stimulates adenylate cyclase. Although vasopressin and oxytocin differ only by two amino acids and stimulate the same cAMP/PKA pathway, they have divergent physiological functions. Vasopressin is involved in regulating blood pressure and the balance of water and sodium ions, whereas oxytocin plays an important role in the uterus during childbirth and in lactation
QVEIAVLAIIFACALLSNSLVLLVLWRRRKQLARMHVFMLHLCIADLVVAFFQVLPQLVWDITDRFRGPD
VLCRLVKYLQVVGMFASSYMIVAMTFDRHQAICRPMVTFQKGRARWNGPVCVAWAISLILSLPQVFIFSK
VEVAPGVYECWACFIEPWGLKAYVTWITLVVFVLPTLIITVCQVLIFKEIHINIYLKSQIIVAVVKKKQL
LSSRASSVAEVSKAMIKTVKMTLVIVLVYVLCWAPFFLVQLWSVWDPKAPTEGATFTILMLLASLNSCTN
PWIYMAFSSSVSKEL
>gnl|CDD|320511 cd15389, 7tmA_GPR83, G protein-coupled receptor 83, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR83, also known as GPR72, is widely expressed in the brain, including hypothalamic nuclei which is involved in regulating energy balance and food intake. The hypothalamic expression of GPR83 is tightly regulated in response to nutrient availability and is decreased in obese mice. A recent study suggests that GPR83 has a critical role in the regulation of systemic energy metabolism via ghrelin-dependent and ghrelin-independent mechanisms. GPR83 shares a significant amino acid sequence identity with the tachykinin receptors, however its endogenous ligand is unknown
ALLIVAYSIIIVISLFGNSLVCHVIFKNKRMHTATNLFIVNLAVSDILITLLNTPFTLVRFVNSTWVFGK
IMCHLSRFAQYCSVYVSTLTLTAIALDRHRVILHPLKPRITPCQGVVVIAIIWIMASCLSLPHAIYQKLV
EFEYSNERTRSRCLPSFPEPSDLFWKYLDLATFILQYVLPLLIIGVAYTRVAKKLWLRNAIGDVTTEQYV
AQRRKKKKTIKMLMLVVLLFAICWLPLNCYHVLLSSHPIRSNSALFFAFHWLAMSSTCYNPFIYCWLNDS
FRSEL
>gnl|CDD|320512 cd15390, 7tmA_TACR, neurokinin receptors (or tachykinin receptors), member of the class A family of seven-transmembrane G protein-coupled receptors. This group represents G-protein coupled receptors for a variety of neuropeptides of the tachykinin (TK) family. The tachykinins are widely distributed throughout the mammalian central and peripheral nervous systems and act as excitatory transmitters on neurons and cells in the gastrointestinal tract. The TKs are characterized by a common five-amino acid C-terminal sequence, Phe-X-Gly-Leu-Met-NH2, where X is a hydrophobic residue. The three major mammalian tachykinins are substance P (SP), neurokinin A (NKA), and neurokinin B (NKB). The physiological actions of tachykinins are mediated through three types of receptors: neurokinin receptor type 1 (NK1R), NK2R, and NK3R. SP is a high-affinity endogenous ligand for NK1R, which interacts with the Gq protein and activates phospholipase C, leading to elevation of intracellular calcium. NK2R is a high-affinity receptor for NKA, the tachykinin neuropeptide substance K. SP and NKA are found in the enteric nervous system and mediate in the regulation of gastrointestinal motility, secretion, vascular permeability, and pain perception. NK3R is activated by its high-affinity ligand, NKB, which is primarily involved in the central nervous system and plays a critical role in the regulation of gonadotropin hormone release and the onset of puberty
VLWSIVFVVMVLVAIGGNLIVIWIVLAHKRMRTVTNYFLVNLAVADLLISAFNTVFNFTYLLYNDWPFGL
FYCKFSNFVAITTVAASVFTLMAISIDRYIAIVHPLRPRLSRRTTKIAIAVIWLASFLLALPQLLYSTTE
TYYYYTGSERTVCFIAWPDGPNSLQDFVYNIVLFVVTYFLPLIIMAVAYTRVGVELWGSKTIGENTPRQL
ESVRAKRKVVKMMIVVVVIFAICWLPYHLYFILTYLYPDINSWKYIQQIYLAIYWLAMSNSMYNPIIYCW
MNKRFRYGF
>gnl|CDD|320513 cd15391, 7tmA_NPR-like_invertebrate, invertebrate neuropeptide receptor-like, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup includes putative neuropeptide receptor found in invertebrates, which is a member of class A of 7-transmembrane G protein-coupled receptors. This orphan receptor shares a significant amino acid sequence identity with the neurokinin 1 receptor (NK1R). The endogenous ligand for NK1R is substance P, an 11-amino acid peptide that functions as a vasodilator and neurotransmitter and is released from the autonomic sensory nerve fibers
PHLINLYQSTIFLSVGGNYSVIVVFYDGRRSRTDLNYYLINLAVSDLIMALFCMPFTFTQIMLGHWVFPA
PMCPIVLYVQLVSVTASVLTNTAIGIDRFFAVIFPLRSRHTKSRTKCIIASIWAISFSLSSVQLFAGRTQ
RYGQYSEGRVLCGESWPGPDTSRSAYTVFVMLLTYIIPLLILTSTYGYVGFRLWNRTAPGNADKGRDDMQ
IKSKRKVIKMLVFVVLMFGICWLPLHLFNLVQDFSTVFRNMPQHTTRLIYGACHWIAMSNSFVNPIIYLF
MNDSFRSIL
>gnl|CDD|320514 cd15392, 7tmA_PR4-like, neuropeptide Y receptor-like found in insect and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup includes a novel G protein-coupled receptor (also known as PR4 receptor) from Drosophila melanogaster, which can be activated by the members of the neuropeptide Y (NPY) family, including NPY, peptide YY (PYY) and pancreatic polypeptide (PP), when expressed in Xenopus oocytes. These homologous peptides of 36-amino acids in length contain a hairpin-like structural motif, which referred to as the pancreatic polypeptide fold, and function as gastrointestinal hormones and neurotransmitters. The PR4 receptor also shares strong sequence homology to the mammalian tachykinin receptors (NK1R, NK2R, and NK3R), whose endogenous ligands are substance P (SP), neurokinin A (NKA), and neurokinin B (NKB), respectively. The tachykinins function as excitatory transmitters on neurons and cells in the gastrointestinal tract
VIIILMYSTIFVLAVGGNGLVCYIVVSYPRMRTVTNYFIVNLALSDILMAVFCVPFSFIALLILQYWPFG
EFMCPVVNYLQAVSVFVSAFTLVAISIDRYVAIMWPLRPRMTKRQALLLIAVIWIFALATALPIAITSRL
FEDSNASCGQYICTESWPSDTNRYIYSLVLMILQYFVPLAVLVFTYTRIGIVVWAKRTPGEAENNRDQRM
AESKRKLVKMMITVVAIFALCWLPLNILNLVGDHDESIYSWPYIPYLWLAAHWLAMSHCCYNPFIYCWMN
AKFRNGF
>gnl|CDD|320515 cd15393, 7tmA_leucokinin-like, leucokinin-like peptide receptor from tick and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup includes a leucokinin-like peptide receptor from the Southern cattle tick, Boophilus microplus, a pest of cattle world-wide. Leucokinins are invertebrate neuropeptides that exhibit myotropic and diuretic activity. This receptor is the first neuropeptide receptor known from the Acari and the second known in the subfamily of leucokinin-like peptide G-protein-coupled receptors. The other known leucokinin-like peptide receptor is a lymnokinin receptor from the mollusc Lymnaea stagnalis
VLLSILYGIISLVAVVGNFLVIWVVAKNRRMRTVTNIFIANLAVADIIIGLFSIPFQFQAALLQRWVLPR
FMCPFCPFVQVLSVNVSVFTLTVIAVDRYRAVIHPLKARCSKKSAKIIILIIWILALLVALPVALALRVE
ELTDKTNNGVKPFCLPVGPSDDWWKIYNLYLVCVQYFVPLVIICYAYTRIAVKIWGTKAPGNAQDVRDDE
ILKNKKKVIKMLIIVVALFALCWLPLQTYNLLNEIKPEINKYKYINIIWFCSHWLAMSNSCYNPFIYGLY
NEKFKREF
>gnl|CDD|320516 cd15394, 7tmA_PrRP_R, prolactin-releasing peptide receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Prolactin-releasing peptide (PrRP) receptor (previously known as GPR10) is expressed in the central nervous system with the highest levels located in the anterior pituitary and is activated by its endogenous ligand PrRP, a neuropeptide possessing a C-terminal Arg-Phe-amide motif. There are two active isoforms of PrRP in mammals: one consists of 20 amino acids (PrRP-20) and the other consists of 31 amino acids (PrRP-31), where PrRP-20 is a C-terminal fragment of PrRP-31. Binding of PrRP to the receptor coupled to G(i/o) proteins activates the extracellular signal-related kinase (ERK) and it can also couple to G(q) protein leading to an increase in intracellular calcium and activation of c-Jun N-terminal protein kinase (JNK). The PrRP receptor shares significant sequence homology with the neuropeptide Y (NPY) receptor, and micromolar levels of NPY can bind and completely inhibit the PrRP-evoked intracellular calcium response in PrRP receptor-expressing cells, suggesting that the PrRP receptor shares a common ancestor with the NPY receptors. PrRP has been shown to reduce food intake and body weight and modify body temperature when administered in rats. It also has been shown to decrease circulating growth hormone levels by activating somatostatin-secreting neurons in the hypothalamic periventricular nucleus
PLIIPLYSLVVLVGVVGNYLLIYVICRTKKMHNVTNFLIGNLAFSDMLMCATCVPLTLAYAFEPRGWVFG
RFMCYFVFLMQPVTVYVSVFTLTAIAVDRYYVTVYPLRRRISRRTCAYIVAAIWLLSCGLALPAAAHTYY
VEFKGLDFSICEEFWFGQEKQRLAYACSTLLITYVLPLLAISLSYLRISVKLRNRVVPGSMTQSQAEWDR
ARRRKTFRLLVVVVVAFAICWLPLHIFNVIRDIDIDLIDKQYFNLIQLLCHWLAMSSACYNPFLYAWLHD
SFRGEL
>gnl|CDD|320517 cd15395, 7tmA_NPY1R, neuropeptide Y receptor type 1, member of the class A family of seven-transmembrane G protein-coupled receptors. NPY is a 36-amino acid peptide neurotransmitter with a C-terminal tyrosine amide residue that is widely distributed in the brain and the autonomic nervous system of many mammalian species. NPY exerts its functions through five, G-protein coupled receptor subtypes including NPY1R, NPY2R, NPY4R, NPY5R, and NPY6R; however, NPY6R is not functional in humans. NYP receptors are also activated by its two other family members, peptide YY (PYY) and pancreatic polypeptide (PP). They typically couple to G(i) or G(o) proteins, which leads to a decrease in adenylate cyclase activity, thereby decreasing intracellular cAMP levels, and are involved in diverse physiological roles including appetite regulation, circadian rhythm, and anxiety. When NPY signals through NPY2R in concert with NPY5R, it induces angiogenesis and consequently plays an important role in revascularization and wound healing. On the other hand, when NPY acts through NPY1R and NPYR5, it acts as a vascular mitogen, leading to restenosis and atherosclerosis
FTLALAYSAVIILGVSGNLALIIIILKQKEMHNVTNILIVNLSFSDLLMTIMCLPFTFVYTLMDHWVFGE
AMCKLNSMVQCISITVSIFSLVLIAIERHQLIINPRGWRPNNRHAYVGIAVIWVLAVLTSLPFLIFQVLT
DEPFKNVNVSLDAYKGKYVCLDQFPSDTIRLSYTTCLLVLQYFGPLCFIFICYLKIYIRLKRRNNMMDKM
RDNKYRSSETKRINIMLISIVVAFAVCWLPLNIFNAVFDWNHEAIATCNHNLLFLICHLTAMISTCVNPI
FYGFLNKNFQRDL
>gnl|CDD|320518 cd15396, 7tmA_NPY6R, neuropeptide Y receptor type 6, member of the class A family of seven-transmembrane G protein-coupled receptors. NPY is a 36-amino acid peptide neurotransmitter with a C-terminal tyrosine amide residue that is widely distributed in the brain and the autonomic nervous system of many mammalian species. NPY exerts its functions through five, G-protein coupled receptor subtypes including NPY1R, NPY2R, NPY4R, NPY5R, and NPY6R; however, NPY6R is not functional in humans. NYP receptors are also activated by its two other family members, peptide YY (PYY) and pancreatic polypeptide (PP). They typically couple to G(i) or G(o) proteins, which leads to a decrease in adenylate cyclase activity, thereby decreasing intracellular cAMP levels, and are involved in diverse physiological roles including appetite regulation, circadian rhythm, and anxiety
FLLIIAYSVVTIVGLFGNLCLITIIKKQKEEHNVTNILIANLSLSDVLVCVMCIPFTAVYTLMDHWIFGE
TMCKLTSFVQSVSVSVSIFSLVLIAIERYQLIVNPRGWKPSASHAYWGIVLIWLFSLMISIPFLIFHQLT
DEPFRNLSSHSDFYKDKVVCIEAWPSETERLIFTTSLLVFQYFVPLGFIFICYLKIFVCLKKRNSKIDRM
RENESRLSENKRINTMLISIVVTFAACWLPLNIFNVVFDWNHEVLMSCHHNLVFTLCHLVAMVSTCINPI
FYGFLNKNFQKDL
>gnl|CDD|320519 cd15397, 7tmA_NPY4R, neuropeptide Y receptor type 4, member of the class A family of seven-transmembrane G protein-coupled receptors. NPY is a 36-amino acid peptide neurotransmitter with a C-terminal tyrosine amide residue that is widely distributed in the brain and the autonomic nervous system of many mammalian species. NPY exerts its functions through five, G-protein coupled receptor subtypes including NPY1R, NPY2R, NPY4R, NPY5R, and NPY6R; however, NPY6R is not functional in humans. NYP receptors are also activated by its two other family members, peptide YY (PYY) and pancreatic polypeptide (PP). They typically couple to G(i) or G(o) proteins, which leads to a decrease in adenylate cyclase activity, thereby decreasing intracellular cAMP levels, and are involved in diverse physiological roles including appetite regulation, circadian rhythm, and anxiety
VFLVVSYSLVMAVGLLGNICLICVIARQKEKTNVTNILIANLSFSDILVCLVCLPFTVVYTLMDYWIFGE
VLCKMTPFIQCMSVTVSILSLVLIALERHQLIINPTGWKPSVSQAYLAVVVIWMLACFISLPFLAFHILT
DEPYKNLSHFFAPLADKAVCTESWPSEHHKLAYTTWLLLFQYCLPLLFILVCYLRIYLRLRRRKDMLERR
GEYNRRAGHSKRINVMLVSLVAAFALCWLPLNVFNAIADWNHEAIPHCQHNLIFSLCHLAAMASTCVNPI
IYGFLNSNFKKEV
>gnl|CDD|320520 cd15398, 7tmA_NPY5R, neuropeptide Y receptor type 5, member of the class A family of seven-transmembrane G protein-coupled receptors. NPY is a 36-amino acid peptide neurotransmitter with a C-terminal tyrosine amide residue that is widely distributed in the brain and the autonomic nervous system of many mammalian species. NPY exerts its functions through five, G-protein coupled receptor subtypes including NPY1R, NPY2R, NPY4R, NPY5R, and NPY6R; however, NPY6R is not functional in humans. NYP receptors are also activated by its two other family members, peptide YY (PYY) and pancreatic polypeptide (PP). They typically couple to G(i) or G(o) proteins, which leads to a decrease in adenylate cyclase activity, thereby decreasing intracellular cAMP levels, and are involved in diverse physiological roles including appetite regulation, circadian rhythm, and anxiety. When NPY signals through NPY2R in concert with NPY5R, it induces angiogenesis and consequently plays an important role in revascularization and wound healing. On the other hand, when NPY acts through NPY1R and NPYR5, it acts as a vascular mitogen, leading to restenosis and atherosclerosis
YFLIGLYTFISLLGFLGNLLILTALTKKWKQKTIINFLIGNLAFSDILVVLFCSPFTLTCVLLDQWIFGE
VMCHIVPFLQCVSVMVSTLMLMSIAIVRYHMIKHPLSNHLTANHGYFLLGTVWTLGFTICSPLPVFHKIV
DLSETFNLESLKNKYLCIESWPSDSYRIAFTISLLFVQYILPLVCLTVSHTSVCRSVKRSRSVFYRLTIV
ILAFAVSWMPLHLFHLVTDFNANLISNRHFKLVYCICHLLGMLSCCLNPILYGFLNNGIKSDL
>gnl|CDD|320521 cd15399, 7tmA_NPY2R, neuropeptide Y receptor type 2, member of the class A family of seven-transmembrane G protein-coupled receptors. NPY is a 36-amino acid peptide neurotransmitter with a C-terminal tyrosine amide residue that is widely distributed in the brain and the autonomic nervous system of many mammalian species. NPY exerts its functions through five, G-protein coupled receptor subtypes including NPY1R, NPY2R, NPY4R, NPY5R, and NPY6R; however, NPY6R is not functional in humans. NYP receptors are also activated by its two other family members, peptide YY (PYY) and pancreatic polypeptide (PP). They typically couple to G(i) or G(o) proteins, which leads to a decrease in adenylate cyclase activity, thereby decreasing intracellular cAMP levels, and are involved in diverse physiological roles including appetite regulation, circadian rhythm, and anxiety. When NPY signals through NPY2R in concert with NPY5R, it induces angiogenesis and consequently plays an important role in revascularization and wound healing. On the other hand, when NPY acts through NPY1R and NPYR5, it acts as a vascular mitogen, leading to restenosis and atherosclerosis
IVLILAYCSIILLGVVGNSLVIYVVIKFKNMRTVTNFFIANLAVADLMVNTLCLPFTLVYTLLDEWKFGA
VLCHLVPYAQALAVHVSTVTLTVIALDRHRCIVYHLESKISKKISFLIIGLTWAASALLASPLAIFREYS
VIEISPDFKIQACSEKWPNGTLNDGTIYSVSMLLIQYVLPLAIISYAYIRIWTKLKNHVSPGGGNDHYHQ
RRRKTTKMLVCVVVVFAVSWLPFHAFQLASDIDSKVLDLKEYKLIYTIFHVIAMCSTFANPLLYGWMNNN
YRTAF
>gnl|CDD|320522 cd15400, 7tmA_Mel1B, melatonin receptor subtype 1B, member of the class A family of seven-transmembrane G protein-coupled receptors. Melatonin (N-acetyl-5-methoxytryptamine) is a naturally occurring sleep-promoting chemical found in vertebrates, invertebrates, bacteria, fungi, and plants. In mammals, melatonin is secreted by the pineal gland and is involved in regulation of circadian rhythms. Its production peaks during the nighttime, and is suppressed by light. Melatonin is shown to be synthesized in other organs and cells of many vertebrates, including the Harderian gland, leukocytes, skin, and the gastrointestinal (GI) tract, which contains several hundred times more melatonin than the pineal gland and is involved in the regulation of GI motility, inflammation, and sensation. Melatonin exerts its pleiotropic physiological effects through specific membrane receptors, named MT1A, MT1B, and MT1C, which belong to the class A rhodopsin-like G-protein coupled receptor family. MT1A and MT1B subtypes are present in mammals, whereas MT1C subtype has been found in amphibians and birds. The melatonin receptors couple to G proteins of the G(i/o) class, leading to the inhibition of adenylate cyclase
TALSSVLIFTTVVDILGNLLVIISVFRNRKLRNSGNVFVVSLALADLVVALYPYPLVLVAIFHNGWALGE
MHCKVSGFVMGLSVIGSIFNITGIAINRYCYICHSFAYDKLYSRWNTLLYVCLIWALTVVAIVPNFFVGS
LEYDPRIYSCTFVQTASSSYTIAVVVIHFIVPITVVSFCYLRIWVLVIQVRRKVKSESKPRLKPSDFRNF
LTMFVVFVIFAICWAPLNLIGLAVAINPQEMAPKVPEWLFVVSYFMAYFNSCLNAIIYGLLNQNFRKEY
>gnl|CDD|320523 cd15401, 7tmA_Mel1C, melatonin receptor subtype 1C, member of the class A family of seven-transmembrane G protein-coupled receptors. Melatonin (N-acetyl-5-methoxytryptamine) is a naturally occurring sleep-promoting chemical found in vertebrates, invertebrates, bacteria, fungi, and plants. In mammals, melatonin is secreted by the pineal gland and is involved in regulation of circadian rhythms. Its production peaks during the nighttime, and is suppressed by light. Melatonin is shown to be synthesized in other organs and cells of many vertebrates, including the Harderian gland, leukocytes, skin, and the gastrointestinal (GI) tract, which contains several hundred times more melatonin than the pineal gland and is involved in the regulation of GI motility, inflammation, and sensation. Melatonin exerts its pleiotropic physiological effects through specific membrane receptors, named MT1A, MT1B, and MT1C, which belong to the class A rhodopsin-like G-protein coupled receptor family. MT1A and MT1B subtypes are present in mammals, whereas MT1C subtype has been found in amphibians and birds. The melatonin receptors couple to G proteins of the G(i/o) class, leading to the inhibition of adenylate cyclase
SVLAGVLIFTIVVDVLGNLLVILSVLRNKKLRNAGNIFVVSLSVADLVVAVYPYPLILLAIFHNGWTLGN
IHCQISGFLMGLSVIGSVFNITAIAINRYCYICHSLRYDKLYNMKKTCCYVCLTWVLTLAAIVPNFFVGS
LQYDPRIYSCTFAQTVSSSYTITVVVVHFIVPLSIVTFCYLRIWVLVIQVKHRVRQDSKQKLKANDIRNF
LTMFVVFVLFAVCWGPLNFIGLAVAINPLKVAPKIPEWLFVLSYFMAYFNSCLNAVIYGVLNQNFRKEY
>gnl|CDD|320524 cd15402, 7tmA_Mel1A, melatonin receptor subtype 1A, member of the class A family of seven-transmembrane G protein-coupled receptors. Melatonin (N-acetyl-5-methoxytryptamine) is a naturally occurring sleep-promoting chemical found in vertebrates, invertebrates, bacteria, fungi, and plants. In mammals, melatonin is secreted by the pineal gland and is involved in regulation of circadian rhythms. Its production peaks during the nighttime, and is suppressed by light. Melatonin is shown to be synthesized in other organs and cells of many vertebrates, including the Harderian gland, leukocytes, skin, and the gastrointestinal (GI) tract, which contains several hundred times more melatonin than the pineal gland and is involved in the regulation of GI motility, inflammation, and sensation. Melatonin exerts its pleiotropic physiological effects through specific membrane receptors, named MT1A, MT1B, and MT1C, which belong to the class A rhodopsin-like G-protein coupled receptor family. MT1A and MT1B subtypes are present in mammals, whereas MT1C subtype has been found in amphibians and birds. The melatonin receptors couple to G proteins of the G(i/o) class, leading to the inhibition of adenylate cyclase
TALACILIFTIVVDILGNLLVILSVYRNKKLRNAGNIFVVSLAVADLVVAIYPYPLVLTSIFHNGWNLGY
LHCQISGFLMGLSVIGSIFNITGIAINRYCYICHSLKYDKLYSDKNSLCYVLLIWVLTVAAIVPNLFVGS
LQYDPRIYSCTFAQSVSSAYTIAVVFFHFILPIIIVTFCYLRIWILVIQVRRRVKPDNKPKLKPHDFRNF
VTMFVVFVLFAVCWAPLNFIGLAVAVDPETIVPRIPEWLFVASYYMAYFNSCLNAIIYGLLNQNFRREY
>gnl|CDD|320525 cd15403, 7tmA_GPR45, G protein-coupled receptor 45, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup includes the human orphan receptor GPR45 and closely related proteins found in vertebrates. GPR45 is also called PSP24 in Xenopus and PSP24-alpha (or PSP24-1) in mammals. GPR45 shows the highest sequence homology with GPR63 (PSP24-beta, or PSP24-2). PSP24 was originally identified as a novel, high-affinity lysophosphatidic acid (LPA) receptor in Xenopus laevis oocytes; however, PSP24 receptors (GPR45 and GPR63) have not been shown to be activated by LPA. Mammalian PSP24 receptors are highly expressed in neuronal cells of cerebellum and their expression level remains constant from the early embryonic stages to adulthood, suggesting the important role of PSP24s in brain neuronal functions. Members of this subgroup contain the highly conserved Asp-Arg-Tyr/Phe (DRY/F) motif found in the third transmembrane helix (TM3) of the rhodopsin-like class A receptors which is important for efficient G protein-coupled signal transduction. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
ILLAIVMILMIAIGFLGNAIVCLIVYQKPAMRSAINLLLATLAFSDIMLSLLCMPFTAVTIITVDWHFGA
HFCRISAMLYWFFVLEGVAILLIISVDRFLIIVQRQDKLNPHRAKVMIAISWVLSFCISFPSVVGWTLVE
VPARAPQCVLGYTESPADRVYAVLLVVAVFFVPFSIMLYSYLCILNTVRRNAVRIHNHADSLCLSQVSKL
GLMGLQRPHQMNVDMSFKTRAFTTILILFVGFSLCWLPHTVFSLLSVFSRRFYYSSSFYPISTCVLWLSY
LKSVFNPVIYCWRIKKFREAC
>gnl|CDD|320526 cd15404, 7tmA_GPR63, G protein-coupled receptor 63, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup includes the human orphan receptor GPR63, which is also called PSP24-beta or PSP24-2, and its closely related proteins found in vertebrates. GPR63 shares the highest sequence homology with GPR45 (Xenopus PSP24, mammalian PSP24-alpha or PSP24-1). PSP24 was originally identified as a novel, high-affinity lysophosphatidic acid (LPA) receptor in Xenopus laevis oocytes; however, PSP24 receptors (GPR45 and GPR63) have not been shown to be activated by LPA. Mammalian PSP24 receptors are highly expressed in neuronal cells of cerebellum and their expression level remains constant from the early embryonic stages to adulthood, suggesting the important role of PSP24s in brain neuronal functions. Members of this subgroup contain the highly conserved Asp-Arg-Tyr/Phe (DRY/F) motif found in the third transmembrane helix (TM3) of the rhodopsin-like class A receptors which is important for efficient G protein-coupled signal transduction. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VILSAVMIFILLVSFLGNFVVCLMVYQKAAMRSAINILLASLAFADMMLAVLNMPFALVTIITTRWIFGD
AFCRVSAMFFWLFVMEGVAILLIISIDRFLIIVQKQDKLNPYRAKVLIAVSWAVSFCVAFPLAVGSPDLQ
IPSRAPQCVFGYTTNPGYQAYVILIMLIFFFIPFMVMLYSFMGILNTVRSFKTRAFTTILILFIVFTVCW
APFTTYSLVATFNSHFYHKHNFFEISTWLLWLCYLKSALNPLIYYWRIKKFRDAC
>gnl|CDD|320527 cd15405, 7tmA_OR8B-like, olfactory receptor subfamily 8B and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 8B and related proteins in other mammals. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
IPLFFLFLGIYVVTVVGNLGLITLICLNSHLHTPMYFFLFNLSFIDLCYSSVFTPKMLMNFVSEKNTISY
AGCMTQLFFFCFFVISECYVLTAMAYDRYVAICNPLLYTVTMSPQVCSLLMLGSYVMGFAGAMAHTGCML
RLTFCDSNIINHYMCDILPLLQLSCTSTYVNELVVFVVVGINIIVPSVTIFISYALILSNILHISSTEGR
SKAFSTCSSHIIAVSLFFGSGAFMYLKPSSVGSVNQGKVSSVFYTNVVPMLNPLIYSLRNKDVKLAL
>gnl|CDD|320528 cd15406, 7tmA_OR8D-like, olfactory receptor subfamily 8D and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 8D and related proteins in other mammals. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
GLTDQPELQLPLFLLFLGIYVVTVVGNLGMILLITLSSQLHTPMYYFLSNLSFIDLCYSSVITPKMLVNF
VSEKNIISYPECMTQLFFFCVFAIAECYMLTAMAYDRYVAICNPLLYNVTMSPRVCSLLVAGVYIMGLIG
ATVHTSCMLRLSFCGDNVINHYFCDILPLLKLSCSSTYINELLLFIVGGFNVLATTLAILISYAFILSSI
LRIRSAEGRSKAFSTCSSHLAAVGVFYGSIIFMYLKPSSSSSMTQEKVSSVFYTTVIPMLNPLIYSLRNK
DVKNALKKVL
>gnl|CDD|320529 cd15407, 7tmA_OR5B-like, olfactory receptor subfamily 5B and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 5B and related proteins in other mammals. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
IPLFIIFTLIYLITLVGNLGMILLILLDSRLHTPMYFFLSNLSLVDIGYSSAVTPKVMAGLLTGDKVISY
NACAAQMFFFVVFATVENFLLASMAYDRHAAVCKPLHYTTTMTTKVCACLTIGCYVCGFLNASIHTGNTF
RLSFCKSNVINHFFCDIPPVLALSCSDIHISEIVLFFLASFNVFFALLVILISYLFIFITILRMRSAEGH
QKAFSTCASHLTAVSIFYGTVIFMYLQPSSSHSMDTDKMASVFYTMVIPMLNPLVYSLRNKEVKSAFKK
>gnl|CDD|320530 cd15408, 7tmA_OR5AK3-like, olfactory receptor subfamily 5AK3, 5AU1, and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 5AK3, 5AU1, and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
FILLGFTDQPELQVLLFVVFLLIYVITLVGNLGMILLIRLDSRLHTPMYFFLSHLSFLDICYSSTITPKT
LLNLLAERKVISFTGCLTQLYFYAVFATTECYLLAAMAYDRYVAICNPLLYTVIMSQRVCVSLVAGSYLA
GFLNSTVHTGFILRLSFCGSNVINHFFCDGPPLLALSCSDTSLNEMLLFAFVGFNVLTTTLVILISYTYI
LATILRMRSAEGRHKAFSTCASHLTAVTLFYGSLAFMYLRPSSRYSLDLDKVASVFYTVVIPMLNPLIYS
LRNKEVK
>gnl|CDD|320531 cd15409, 7tmA_OR5H-like, olfactory receptor subfamily 5H and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 5H, 5K, 5AC, 5T and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
VPLFLVFLAIYLITLVGNLGLIALIWKDSHLHTPMYFFLGNLAFADACTSSSVTPKMLVNFLSKNKMISF
SGCAAQFFFFGFSATTECFLLAAMAYDRYVAICNPLLYPVVMSNRLCVQLITASYIGGFLHSMIHVGLTF
RLSFCGSNEINHFFCDIPPLLKISCTDPSINELVLFIFSGSIQVFTILTVLISYSYILFTILKMKSAEGR
RKAFSTCGSHLLSVSLFYGSLFFMYVRPSSLYALDQDMMDSLFYTIVIPLLNPFIYSLRNKEVIDALRK
>gnl|CDD|320532 cd15410, 7tmA_OR5D-like, olfactory receptor subfamily 5D and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 5D, 5L, 5W, and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
FILLGFTDYPELQVPLFLVFLAIYGITLLGNLGMIVLIKIDPKLHTPMYFFLSHLSFVDFCYSSVIAPKM
LVNFLAEDKAISYSGCMLQFFFFCTFVVTESFLLAVMAYDRYVAICNPLLYTVIMSRKLCVLLVAGSYLW
GIVCSLIHTCGLLRLSFCGSNVINHFFCDLPPLLSLSCSDTYLNELLLFIFGSLNEASTLLIILTSYVFI
IVTILRIRSAEGRQKAFSTCASHLTAITIFHGTILFMYCRPSSSYSLDTDKVASVFYTVVIPMLNPLIYS
LRNKDVKDALRKLI
>gnl|CDD|320533 cd15411, 7tmA_OR8H-like, olfactory receptor subfamily 8H and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 8H, 8I, 5F and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
VPLFVLFLVIYVITVMGNLGMILLIRADSQLHTPMYFFLSNLSFVDFCYSSTITPKALENFLSGRKAISF
AGCFVQMYFFIALATTECFLLGLMAYDRYVAICNPLLYTVVMSRRVCLKLAAGSYAAGFLNSLIHTTLIS
RLSFCGSNVINHFFCDTPPLLKLSCSDTHVNEMLIFILAGLTLVGSLLIILVSYTYILSTILKIRSAEGR
RKAFSTCASHLTAVTIFYGTGIFTYLRPSSSYSLGQDKVASVFYTVVIPMLNPLIYSLRNKEVKNALRR
>gnl|CDD|320534 cd15412, 7tmA_OR5M-like, olfactory receptor subfamily 5M and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 5M and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
PLLFVLFLVIYLITLLGNLGMILLIRLDSRLHTPMYFFLSHLSFVDLCYSSNVTPKMLVNFLSEKKTISF
AGCFTQCYFFIALVITEYYMLAVMAYDRYMAICNPLLYSVKMSRRVCISLVTFPYIYGFLNGLIQTILTF
RLSFCGSNVINHFYCADPPLIKLSCSDTYVKETAMFIVAGFNLSSSLLIILISYLFILIAILRIRSAEGR
CKAFSTCGSHLTAVTIFYGTLFCMYLRPPSEESVEQSKIVAVFYTFVSPMLNPLIYSLRNKDVKQALKK
>gnl|CDD|320535 cd15413, 7tmA_OR8K-like, olfactory receptor subfamily 8K and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 8K, 8U, 8J, 5R, 5AL and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
IPLFGLFLVIYLTTVMGNLGMIILTRLDSRLQTPMYFFLRHLAFVDLGYSTAVTPKMLVNFVVEQNTISF
YACATQLAFFLTFIISELFLLSAMAYDRYVAICNPLLYTVIMSQRVCIVLVAIPYLYSFFVALFHTIKTF
RLSFCGSNVINHFYCDDLPLLALSCSDTHEKELIILIFAGFNLISSLLIVLVSYLFILSAILRIRSAEGR
QKAFSTCGSHLTVVTIFYGTLIFMYLQPKSSHSLDTDKMASVFYTLVIPMLNPLIYSLRNKEVKDALKK
>gnl|CDD|320536 cd15414, 7tmA_OR5G-like, olfactory receptor subfamily 5G and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 5G and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
IPLFLLFLLVYLITLLGNLGMIILIQVDSRLHTPMYFFLSHLSFVDLCYSSVVTPKMLSDFFVEKKAISF
LGCAAQMWFFGLFVAAECFLLASMAYDRYVAICNPLLYTVIMSQRVCVQLVVGPYVVGLLNTTTHTTAAF
FLPFCGPNVINHFFCDIPPLLSLSCADTQINKWVLFIMAGALGVLSGLIILVSYIYILIAILRIRSAEGR
RKAFSTCSSHLTAVSILYGTLFFIYVRPSSSSSLDLDKVVSVFYTAVIPMLNPLIYSLRNKEVKDALRRT
IRRKM
>gnl|CDD|320537 cd15415, 7tmA_OR5J-like, olfactory receptor subfamily 5J and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 5J and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
VPLFMLFLLIYFITLLGNLGMIVLIRINPQLHTPMYFFLSNLSFVDLCYSSVFAPRLLVNFLVEKKTISY
SACIAQHFFFAVFVTTEGFLLAVMAYDRYVAICNPLLYTVAMTKRVCVQLVAGSYLGGLINSLTHTIGLL
KLSFCGPNVINHYFCDIPPLLKLSCSDTHINELLLLTFSGVIAMSTLLTIIISYIFILFAILRIRSAEGR
RKAFSTCASHLTAVTLFYGSVSFSYIQPSSQYSLEQEKVSAVFYTLVIPMLNPLIYSLRNKDVKDALKR
>gnl|CDD|320538 cd15416, 7tmA_OR5P-like, olfactory receptor subfamily 5P and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 5P and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
IILFVLFLVIYSVTLLGNLSIILLIRISSQLHTPMYFFLSHLAFSDICYSSSVTPKMLVNFLVEKTTISY
PGCAAQLCSAATFGTVECFLLAAMAYDRYVAICNPLLYSTIMSQKVCVLLVAASYLGGCLNALVFTTCVF
SLSFCGPNEINHFFCDFPPLLKLSCSDIRLAKILPSISSGIIILVTVLTIIISYLYILIAILRIRSTEGR
HKAFSTCASHLTAVTLFYGTITFIYVMPNSSYSMDQNKVVSVFYMVVIPMLNPLIYSLRNKEVKGALKR
>gnl|CDD|320539 cd15417, 7tmA_OR5A1-like, olfactory receptor subfamily 5A1 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 5A1, 5A2, 5AN1, and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
IILFVLFLGIYLVTLLWNLGLIILIRMDSHLHTPMYFFLSNLSFVDICYSSSITPKMLSDFFREQKTISF
VGCATQYFVFSGMGLTECFLLAAMAYDRYVAICNPLLYSVIMSPRLCVQLVAGAYLGGFLNSLIQTVSMF
QLSFCGPNVIDHFFCDIPPLLSLSCSDTFISQVVLFLVAVLFGVFSVLVVLISYGYIISTILKIRSAKGR
SKAFNTCASHLTAVTLFYGTGLFVYLRPSSSHSQDQDKVASVFYTVVIPMLNPLIYSLRNKEIKDALKR
>gnl|CDD|320540 cd15418, 7tmA_OR9G-like, olfactory receptor subfamily 9G and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 9G and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
QLILFVVFLLSYILTLVGNLTLIALICLDSRLHTPMYFFVGNLSFLDLWYSSVYTPKILADCISKDKSIS
FAGCAAQFFFSAGLAYSECFLLAAMAYDRYVAICNPLLYSSAMSKKLCMGLVAASYLGGFANAIIHTSNT
FRLHFCGDNIIDHFFCDLPPLVKLACDDTRVYELILYFILGFNVIAPTALILASYTFILAAILRIHSASG
RHKAFSTCSAHLTSVTLYYGSILFIYSRPSSSHTPDRDKVVALFYTVVNPLLNPLIYSLRNKDVKEALKK
L
>gnl|CDD|320541 cd15419, 7tmA_OR9K2-like, olfactory receptor subfamily 9K2 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes transmembrane olfactory receptor subfamily 9K2 and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
VLLFLLFLVIYMVTVLGNIGMIIIISTDSRLHTPMYFFLMNLSFLDLCYSSVIAPKALANFLSESKTISY
NGCAAQFFFFSLFGTTEGFLLAAMAYDRFIAICNPLLYPVIMSRRVCVQLVAGSYLCGCINSIIQTSFTF
SLSFCGSNEIDHFFCDVPPLLKLSCSDTFINELVMFVLCGLIIVSTILVILVSYAYILSTILRIPSAEGR
KKAFSTCASHLTAVSLFYGTVFFMYAQPGAVSSPEQSKVVSVFYTLVIPMLNPLIYSLRNKDVKEALKR
>gnl|CDD|320542 cd15420, 7tmA_OR2A-like, olfactory receptor subfamily 2A and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 2A and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
LLLFGLFSLLYIFTLLGNGLILGLIWLDSRLHTPMYFFLSHLAVVDICYASSTVPHMLGNLLKQRKTISF
AGCGTQMYLFLALAHTECVLLAVMSYDRYVAICHPLRYTVIMNWRVCTTLAATSWACGFLLALVHVVLLL
RLPFCGPNEVNHFFCEILAVLKLACADTWINEILIFAGCVFILLGPFSLILISYLHILAAILKIQSAEGR
RKAFSTCSSHLCVVGLFYGTAMFMYMVPGSSNSAEQEKILSLFYSLFNPMLNPLIYSLRNKQVKGAL
>gnl|CDD|320543 cd15421, 7tmA_OR2T-like, olfactory receptor subfamily 2T and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamilies 2T, 2M, 2L, 2V, 2Z, 2AE, 2AG, 2AK, 2AJ, and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
LFLFSLILLIFLVALTGNALLILLIWLDSRLHTPMYFLLSQLSLMDLMLISTTVPKMATNFLSGRKSISF
VGCGTQIFFFLTLGGAECLLLALMAYDRYVAICHPLRYPVLMSPRVCLLMAAGSWLGGSLNSLIHTVYTM
HFPYCGSREIHHFFCEVPALLKLSCADTSAYETVVYVSGVLFLLIPFSLILASYALILLTVLRMRSAEGR
KKALATCSSHLTVVSLYYGPAIFTYMRPGSYHSPEQDKVVSVFYTILTPMLNPLIYSLRNKEVLGAL
>gnl|CDD|320544 cd15424, 7tmA_OR2_unk, olfactory receptor family 2, unknown subfamily, member of the class A family of seven-transmembrane G protein-coupled receptors. This group represents an unknown subfamily, conserved in some mammalia and sauropsids, in family 2 of olfactory receptors. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
ILLFVVILIIYLLTILGNLVIIILVQTDSRLHTPMYFFLSHLAGLEICYVTSTLPQMLAHLLAGNGAISF
ARCTTQMYIALSLGSTECLLLGAMAYDRYLAICHPLLYAAAMGRWRQLQLALSCWAIGFLLSVINVGCTL
RHPFCGPNHINHFFCELPVVLKLACADTHITEAIVFGAGVLILLVPLSVILTSYGLILASVLQMQSAAGR
HKAFSTCASHLAVVTLFYGTVISMYMRPRSGSTPDRDKQIAVFYIVITPLLNPIIYTLRNKDVHGAA
>gnl|CDD|320545 cd15428, 7tmA_OR2D-like, olfactory receptor subfamily 2D and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 2D and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
ILLFILFLIIYLMTVLGNLLLVLLVIVDSHLHTPMYFFLSNLSVLELCYTTTVVPQMLVHLLSERKIISF
IRCAAQLYFFLSFGITECALLSVMSYDRYVAICLPLRYSLIMTWKVCISLATGSWVGGLLVSAVDTAFTL
NLSFGGHNKINHFLCEMPALLKLASTDTHQAEMAMFIMCVFTLVLPVLLILASYTRIIYTVFGMQSLTGR
LKAFSTCSSHLMVVSLFYGSVLSTYMRPKSSTSKEYDKMISVFYIIVTPMLNPLIYSLRNKEVKHAL
>gnl|CDD|320546 cd15429, 7tmA_OR2F-like, olfactory receptor subfamily 2F and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 2F and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
LGLFVLFLVMYLLTLLGNFLIILLIRLDPRLHTPMYFFLSHLSFLDICYTTSVVPQMLAHFLAEHKTISF
ASCVAQLFISLALGGTEFILLAVMAYDRYVAVCHPLRYTVIMSGGLCIQLAAASWTSGFLNSLVQTAFTF
RLPFCGHNTINHFSCELLAVVRLACVDTSLNEVAILVSSVVVLLTPCFLVLLSYIHIISAILRIRSSEGR
HKAFSTCASHLTVVSLCYGTAIFTYMRPRSGSSALQEKMISLFYAVVTPMLNPLIYSLRNKEVKGAL
>gnl|CDD|320547 cd15430, 7tmA_OR13-like, olfactory receptor family 13 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor family 13 (subfamilies 13C, 13D, 13F, and 13J), some subfamilies from OR family 2 (2K and 2S), and related proteins in other mammals. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
ILLFVLCLIMYLVILLGNGVLIIITILDSHLHTPMYFFLGNLSFLDICYTSSSVPLMLVNFLSERKTISF
SGCAVQMYLSLAMGSTECVLLAVMAYDRYVAICNPLRYPIIMNKRLCVQMAAGSWVTGFLNSLVETVLAM
QLPFCGNNVINHFTCEILAVLKLACVDISLNEIIMLVGNIIFLVIPLLLICISYIFILSTILRINSAEGR
KKAFSTCSAHLTVVIIFYGTILFMYMKPKSKNAQISDKLITLFYGVVTPMLNPIIYSLRN
>gnl|CDD|320548 cd15431, 7tmA_OR13H-like, olfactory receptor subfamily 13H and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 13H and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
IILFVLLLIVYLVTLLGNGLIILLIRVDSQLHTPMYFFLSNLSFLDICYTTSSVPQMLVNCLSDRPTISY
SRCLAQMYISLFLGITECLLLAVMAYDRFVAICNPLRYTLIMSWRVCIQLAAGSWVSAFLLTVIPVLTMP
LHFCGPNVINHFFCEVQALLKLACSDTSLNEILMFATSIFTLLLPFSFILVSYIRIGVAVLRIRSAEGRR
KAFSTCGSHLTVVTIFYGTAIFMYLRPQSKSSSDQDKIISVFYGVVTPMLNPLIYSLRN
>gnl|CDD|320549 cd15432, 7tmA_OR2B2-like, olfactory receptor subfamily 2B2 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes transmembrane olfactory receptor subfamily 2B2 and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
MVLFVVFLIFYILTLLGNLAIILVSRLDPQLHTPMYFFLSNLSLLDLCYTTSTVPQMLVNLRSPQKTISY
GGCVAQLFIFLGLGSTECVLLAVMAFDRFAAICQPLHYSVIMHQRLCQQLAAGAWISGFANSLVQSTLTL
KMPRCGRRRVDHFFCEVPALLKLSCVDTTANEAELFVISVLLLLIPLGLILISYIFIVRAVLRIRSAEGR
RKAFNTCGSHLLVVSLFYGTAISMYLQPPSNSSHDRGKMVALFYGIITPMLNPLIYTLRNKDVKEAL
>gnl|CDD|320550 cd15433, 7tmA_OR2Y-like, olfactory receptor subfamily 2Y and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 2Y, 2I, and related protein in other mammals. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
PVLFVVVLIFYLLTLVGNTIIILLSVRDLRLHTPMYYFLCHLSFVDLCFTTSTVPQLLANLRGPALTITR
GGCVAQLFISLALGSAECVLLAVMAFDRYAAVCRPLHYAALMSPRLCQTLASISWLSGFVNSVAQTGLLA
ERPLCGHRLLDHFFCEMPVFLKLACGDDETTEVQMFVARVVILLLPAALILGSYGHVAHAVLRIKSSAGR
RRAFGTCGSHLMVVFLFYGSAIYTYLQPIHRYSQAHGKFVSLFYTVMTPALNPLIYTLRNKDVKGAL
>gnl|CDD|320551 cd15434, 7tmA_OR2W-like, olfactory receptor subfamily 2W and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 2W and related proteins in other mammals. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
KILSVVVLIFYLLTLVGNTTIILVSCLDSRLHTPMYFFLANLSFLDLCFTTSIIPQMLVNLWGPDKTISY
VGCAIQLFIALGLGGTECVLLAVMAYDRYAAVCQPLHYTVVMHPRLCWKLVAMSWLIGFGNSLVLSPLTL
SLPRCGHHRVDHFFCEMPALIKLACVDTTAYEATIFALGVFILLFPLSLILVSYGYIARAVLKIKSAAGR
KKAFGTCGSHLTVVSLFYGTIIYMYLQPKNSVSQDQGKFLTLFYTIVTPSLNPLIYTLRNKDVKGAL
>gnl|CDD|320552 cd15436, 7tmB2_Latrophilin, Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors. Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
ELLLFVITWVGIVISLVCLLICIFTFCFFRGLQTDRNTIHKNLCINLFIAELLFLIGINRTQYTIACPIF
AGLLHFFFLAAFCWLCLEGVQLYLLLVEVFESEYSRRKYFYLCGYSFPALVVAVSAAIDYRSYGTEKACW
LRVDNYFIWSFIGPVTFVITLNLVFLVITLHKMVSHSDLLKPDSSRLDNIKSWALGAIALLFLLGLTWSF
GLMFINEESVVMAYLFTIFNAFQGVFIFIFHCALQKKVRKEYSKCLRH
>gnl|CDD|320553 cd15437, 7tmB2_ETL, Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; member of the class B2 family of seven-transmembrane G protein-coupled receptors. ETL (EGF-TM7-latrophilin-related protein) belongs to Group I adhesion GPCRs, which also include latrophilins (also called lectomedins or latrotoxin receptors). All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. ETL, for instance, contains EGF-like repeats, which also present in other EGF-TM7 adhesion GPCRs, such as Cadherin EGF LAG seven-pass G-type receptors (CELSR1-3), EGF-like module receptors (EMR1-3), CD97, and Flamingo. ETL is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
YNVLTRITQLGIIISLICLSMCIFTFWFFSEIQSTRTTIHKNLCCSLFLAELIFLIGINMNANKLFCSII
AGLLHYFFLAAFAWMCIEGIHLYLIVVGVIYNKGFLHKNFYIFGYGSPAVVVGISAALGYKYYGTTKVCW
LSTENNFIWSFIGPACLIILVNLLAFGVIIYKVFRHTAMLKPEVSCYENIRSCARGALALLFLLGATWIF
GVLHVVYGSVVTAYLFTISNAFQGMFIFIFLCVLSRKIQEEYYRLFKN
>gnl|CDD|320554 cd15438, 7tmB2_CD97, CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors. group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment
DWPLTLITKVGLSVSLFCLFLCILTFLFCRSIRGTRNTIHLHLCLSLFLAHLIFLLGINNTNNQVACAVV
AGLLHYFFLAAFCWMSLEGVELYLMVVQVFNTQSLKKRYLLLIGYGVPLVIVAISAAVNSKGYGTQRHCW
LSLERGFLWSFLGPVCLIILVNAIIFVITVWKLAEKFSSINPDMEKLRKIRALTITAIAQLCILGCTWIF
GFFQFSDSTLVMSYLFTILNSLQGLFIFLLHCLLSKQVREEYSRWLCAIAR
>gnl|CDD|320555 cd15439, 7tmB2_EMR, epidermal growth factor-like module-containing mucin-like hormone receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors. group II adhesion GPCRs, including the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4) and the leukocyte cell-surface antigen CD97, are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying number of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of EMR2, alternative splicing results in four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment
DLALTVITYVGLIISLLCLFLAILTFLLCRSIRNTSTSLHLQLSLCLFLADLLFLVGIDRTDNKVLCSII
AGFLHYLFLACFAWMFLEAVHLFLTVRNLKVVNYFSSHRFKKRFMYPVGYGLPAVIVAISAAVNPQGYGT
PKHCWLSMEKGFIWSFLGPVCVIIVINLVLFCLTLWILREKLSSLNAEVSTLKNTRLLTFKAIAQLFILG
CTWILGLFQVGPVATVMAYLFTITNSLQGVFIFLVHCLLNRQVREEYRRWITG
>gnl|CDD|320556 cd15440, 7tmB2_latrophilin-like_invertebrate, invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors. This subgroup includes latrophilin-like proteins that are found in invertebrates such as insects and worms. Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of vertebrate latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
QSALTFITYIGCIISIVCLLLAFITFTCFRNLQCDRNTIHKNLCLCLLIAEIVFLLGIDQTENRTLCGVI
AGLLHYFFLAAFSWMLLEGFQLYVMLVEVFEPEKSRIKWYYLFGYGLPALIVAVSAGVDPTGYGTEDHCW
LSTENGFIWSFVGPVIVVLLANLVFLGMAIYVMCRHSSRSASKKDASKLKNIRGWLKGSIVLVVLLGLTW
TFGLLFINQESIVMAYIFTILNSLQGLFIFIFHCVLNEKVRKELRRWLR
>gnl|CDD|320557 cd15441, 7tmB2_CELSR_Adhesion_IV, cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors. The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuron migration and axon guidance in the CNS
VLLLKIVTYIGIGISLVLLVIAFLVLSCLRGLQSNSNSIHKNLVACLLLAELLFLLGINQTENLFPCKLI
AILLHYFYLSAFSWLLVESLHLYRMLTEPRDINHGHMRFYYLLGYGIPAIIVGLSVGLRPDGYGNPDFCW
LSVNETLIWSFAGPIAFVIVITLIIFILALRASCTLKRHVLEKASVRTDLRSSFLLLPLLGATWVFGLLA
VNEDSELLHYLFAGLNFLQGLFIFLFYCIFNKKVRRELKNALLR
>gnl|CDD|320558 cd15442, 7tmB2_GPR97, orphan adhesion receptor GPR97, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR97 is an orphan receptor that has been classified into the group VIII of adhesion GPCRs. Other members of the Group VII include GPR56, GPR64, GPR112, GPR114, and GPR126. GPR97 is identified as a lymphatic adhesion receptor that is specifically expressed in lymphatic endothelium, but not in blood vascular endothelium, and is shown to regulate migration of lymphatic endothelial cells via the small GTPases RhoA and cdc42. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
AQTLVTISSAGCGVSMVFLIFTIILYFFLRFTYQKFKSEDAPKIHVNLSSSLLLLNLAFLLNSGVSSRAH
PGLCKALGGVTHYFLLCCFTWMAIEAFHLYLLAIKVFNTYIHHYFAKLCLVGWGFPALVVTITGSINSYG
AYTIMDMANRTTLHLCWINSKHLTVHYITVCGYFGLTFLFNTVVLGLVAWKIFHLQSATAGKEKCQAWKG
GLTVLGLSCLLGVTWGLAFFTYGSMSVPTVYIFALLNSLQGLFIFIWFVILYYPKMEETTSSSSHIT
>gnl|CDD|320559 cd15443, 7tmB2_GPR114, orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR114 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include GPR56, GPR64, GPR97, GPR112, and GPR126. GPR114 is mainly found in granulocytes (polymorphonuclear leukocytes), and GPR114-transfected cells induced an increase in cAMP levels via coupling to G(s) protein. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
LEPLTYISIVGCSISAAASLLTILLHFFSRKQPKDSTTRIHMNLLGSLFLLNGSFLLSPPLATSQSTWLC
RAAAALLHYSLLCCLTWMAIEGFHLYLLLVKVYNIYIRRYVLKLCVLGWGLPALIVLLVLIFKREAYGPH
TIPTGTGYQNASMCWITSSKVHYVLVLGYAGLTSLFNLVVLAWVVRMLRRLRSRKQELGERARRDWVTVL
GLTCLLGTTWALAFFSFGVFLIPQLFLFTIINSLYGFFICLWYCTQRRRSDASAKSST
>gnl|CDD|320560 cd15444, 7tmB2_GPR64, orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B secretin-like receptors of seven-transmembrane G protein-coupled receptors. GPR64 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR97, GPR112, GPR114, and GPR126. GPR64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also over-expressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
MLILTFITYIGCGLSAIFLSVTLVTYIAFEKIRRDYPSKILIQLCVALLLLNLVFLLDSWIALYKDIVGL
CISVAVFLHYFLLVSFTWMGLEAFHMYLALVKVFNTYIRKYILKFCIVGWGVPAVVVAIVLAVSKDNYGL
GSYGKSPNGSTDDFCWINNNIVFYITVVGYFCVIFLLNISMFIVVLVQLCRIKKQKQLGAQRKTSLQDLR
SVAGITFLLGITWGFAFFAWGPVNLAFMYLFAIFNTLQGFFIFIFYCVAKENVRKQWRRYL
>gnl|CDD|320561 cd15445, 7tmB1_CRF-R1, corticotropin-releasing factor receptor 1, member of the class B family of seven-transmembrane G protein-coupled receptors. The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways
YHIAVIINYLGHCISLVALLVAFVLFLRLRSIRCLRNIIHWNLITAFILRNATWFVVQLTMSPEVHQSNV
VWCRLVTAAYNYFHVTNFFWMFGEGCYLHTAIVLTYSTDKLRKWMFICIGWCIPFPIIVAWAIGKLYYDN
EKCWFGKRAGVYTDYIYQGPMILVLLINFIFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGI
TYMLFFVNPGEDEISRIVFIYFNSFLESFQGFFVSVFYCFLNSEVRSAVRKRWHR
>gnl|CDD|320562 cd15446, 7tmB1_CRF-R2, corticotropin-releasing factor receptor 2, member of the class B family of seven-transmembrane G protein-coupled receptors. The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways
YKIALIINYLGHCISVGALVVAFLLFLCLRSIRCLRNIIHWNLITTFILRNVMWFLLQMIDHNIHESNEV
WCRCITTIYNYFVVTNFFWMFVEGCYLHTAIVMTYSTDKLRKWVFLFIGWCIPCPIIVAWAIGKLYYENE
QCWFGKEPGKYIDYIYQGPVILVLLINFVFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGIT
YMLFFVNPGEDDISQIVFIYFNSFLQSFQGFFVSVFYCFLNGEVRSAARKRWHR
>gnl|CDD|320563 cd15447, 7tmC_mGluR2, metabotropic glutamate receptor 2 in group 2, member of the class C family of seven-transmembrane G protein-coupled receptors. The metabotropic glutamate receptors (mGluRs) in group 2 include mGluR 2 and 3. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity
AWAIGPVTISCLGILSTLFVVGVFVKNNETPVVKASGRELCYILLLGVLLCYLMTFIFIAKPSTAVCTLR
RLGLGTSFAVCYSALLTKTNRIARIFSGAKDGAQRPRFISPASQVAICLALISCQLLVVLIWLLVEAPGT
RKETAPERRYVVTLKCNSRDSSMLISLTYNVLLIILCTLYAFKTRKCPENFNEAKFIGFTMYTTCIIWLA
FLPIFYVTSSDYRVQTTTMCISVSLSGSVVLGCLFAPKLHIILF
>gnl|CDD|320564 cd15448, 7tmC_mGluR3, metabotropic glutamate receptor 3 in group 2, member of the class C family of seven-transmembrane G protein-coupled receptors. The metabotropic glutamate receptors (mGluRs) in group 2 include mGluR 2 and 3. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity
AWAIGPVTIACLGFICTCMVITVFIKHNNTPLVKASGRELCYILLFGVFLSYCMTFFFIAKPSPVICTLR
RLGLGTSFAVCYSALLTKTNCIARIFDGVKNGAQRPKFISPSSQVFICLSLILVQIVVVSVWLILEAPGT
RRYTLPEKRETVILKCNVKDSSMLISLTYDVVLVILCTVYAFKTRKCPENFNEAKFIGFTMYTTCIIWLA
FLPIFYVTSSDYRVQTTTMCISVSLSGFVVLGCLFAPKVHIILF
>gnl|CDD|320565 cd15449, 7tmC_mGluR1, metabotropic glutamate receptor 1 in group 1, member of the class C family of seven-transmembrane G protein-coupled receptors. Group 1 mGluRs includes mGluR1 and mGluR5, as well as their closely related invertebrate receptors. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity
IESIIAVAFSCLGILVTMFVTLIFVLYRDTPVVKSSSRELCYIILAGIFLGYVCPFTLIAKPTTTSCYLQ
RLLVGLSSAMCYSALVTKTNRIARILAGSKKKICTRKPRFMSAWAQVVIASILISVQLTLVVTLIIMEPP
MPILSYPSIKEVYLICNTSNLGVVAPLGYNGLLIMSCTYYAFKTRNVPANFNEAKYIAFTMYTTCIIWLA
FVPIYFGSNYKIITTCFAVSLSVTVALGCMFTPKMYIIIA
>gnl|CDD|320566 cd15450, 7tmC_mGluR5, metabotropic glutamate receptor 5 in group 1, member of the class C family of seven-transmembrane G protein-coupled receptors. Group 1 mGluRs includes mGluR1 and mGluR5, as well as their closely related invertebrate receptors. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity
PEPIAAVVFACLGLLATLFVTVIFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQ
RIGIGLSPAMSYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPP
DIMHDYPSIREVYLICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLA
FVPIYFGSNYKIITMCFSVSLSATVALGCMFVPKVYIILA
>gnl|CDD|320567 cd15451, 7tmC_mGluR7, metabotropic glutamate receptor 7 in group 3, member of the class C family of seven-transmembrane G protein-coupled receptors. The receptors in group 3 include mGluRs 4, 6, 7, and 8. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity
PWAVIPVFLAMLGIIATIFVMATFIRYNDTPIVRASGRELSYVLLTGIFLCYIITFLMIAKPDVAVCSFR
RIFLGLGMCISYAALLTKTNRIYRIFEQGKKSVTAPRLISPTSQLAITSSLISVQLLGVLIWFAVDPPNI
IIDYDEQKTMNPEQARGVLKCDITDLQIICSLGYSILLMVTCTVYAIKTRGVPENFNEAKPIGFTMYTTC
IVWLAFIPIFFGTAQSAEKLYIQTTTLTISMNLSASVALGMLYMPKVYIIIFHPELNVQKRKRSFKAVVT
AATMSSRLSHKPSDRPNGEAKTELCEN
>gnl|CDD|320568 cd15452, 7tmC_mGluR4, metabotropic glutamate receptor 4 in group 3, member of the class C family of seven-transmembrane G protein-coupled receptors. The receptors in group 3 include mGluRs 4, 6, 7, and 8. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity
PWAVVPLLLAVLGIIATLFVVVTFVRYNDTPIVKASGRELSYVLLTGIFLCYATTFLMIAEPDLGTCSLR
RIFLGLGMSISYAALLTKTNRIYRIFEQGKRSVSAPRFISPASQLVITFSLISLQLLGVCVWFLVDPSHS
VVDYEDQRTPDPQFARGVLKCDISDLSLICLLGYSMLLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTC
IIWLAFIPIFFGTSQSAEKMYIQTTTLTISVSLSASVSLGMLYMPKVYVILFHPEQNVPKRKRSLKAVVT
AATMSNKFTQKGSFRPNGEAKSELCENLETQALATKQTYVSYSNHAI
>gnl|CDD|320569 cd15453, 7tmC_mGluR6, metabotropic glutamate receptor 6 in group 3, member of the class C family of seven-transmembrane G protein-coupled receptors. The receptors in group 3 include mGluRs 4, 6, 7, and 8. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity
PWAAPPLLLAVLGILATTTVVITFVRFNNTPIVRASGRELSYVLLTGIFLIYAITFLMVAEPGAAVCAFR
RLFLGLGTTLSYSALLTKTNRIYRIFEQGKRSVTPPPFISPTSQLVITFSLTSLQVVGVIAWLGAQPPHS
VIDYEEQRTVDPEQARGVLKCDMSDLSLIGCLGYSLLLMVTCTVYAIKARGVPETFNEAKPIGFTMYTTC
IIWLAFVPIFFGTAQSAEKIYIQTTTLTVSLSLSASVSLGMLYVPKTYVILFHPEQNVQKRKR
>gnl|CDD|320570 cd15454, 7tmC_mGluR8, metabotropic glutamate receptor 8 in group 3, member of the class C family of seven-transmembrane G protein-coupled receptors. The receptors in group 3 include mGluRs 4, 6, 7, and 8. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity
PWAVVPVFVAILGIIATTFVIVTFVRYNDTPIVRASGRELSYVLLTGIFLCYAITFLMIATPDTGICSFR
RVFLGLGMCFSYAALLTKTNRIHRIFEQGKKSVTAPKFISPASQLVITFSLISVQLLGVFVWFAVDPPHT
IVDYGEQRTLDPEKARGVLKCDISDLSLICSLGYSILLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTC
IIWLAFIPIFFGTAQSAERMYIQTTTLTISMSLSASVSLGMLYMPKVYIIIFHPEQNVQKRKRSFKAVVT
AATMQSKLIQKGNDRPNGEVKTELCESLETN
>gnl|CDD|271319 cd15457, NADAR, Escherichia coli swarming motility protein YbiA and related proteins. This family of uncharacterized domains was initially classified as Domain of Unknown Function (DUF1768). It contains members such as the E. coli swarming motility protein YbiA. Mutations in YbiA cause defects in Escherichia coli swarming, but not necessarily in motility. More recently, this family has been predicted to be involved in NAD-utilizing pathways, likely to act on ADP-ribose derivatives, and has been named the NADAR (NAD and ADP-ribose) superfamily
KIIFFYGHTDPYGCLSNFYPSPFEVDGVTYPTAEHYMQAQKALLFGDPEIAEKILAAKTPKEAKKLGRKV
RGFDRPDWEEVRLDVMREALRAKFSQNPELRELLLSTGDRELVEASPRDRIWGIGLDADPRKWRGQNLLG
KILMEVRE
>gnl|CDD|271230 cd15464, HN_like, Haemagglutinin-neuraminidase (HN) of paramyxoviridae and similar proteins. Most paramyxoviridae have two membrane-anchored glycoproteins that mediate entry of the virus into the host cell. The protein characterized by this model is called hemagglutinin-neuraminidase (HN), hemagglutinin glycoprotein (H), or glycoprotein (G). Typically it has a variety of functions during viral infection; it participates in virus attachment to host cells, may cleave sialic acid off host oligosaccharides, and has a stimulating effect on membrane fusion during the entry of the virus into the host cell
PNLIPADTGLLSGECVRQPSFAISSGIYAYTYLVRKGSCQDHRSLYRYFEVGVIRDDGLGDPVFSPLNVW
TLPNPNDLDSCSVAVGNLGGAALCTVTTVGPEIDQNSGKSPSLALVKLGVDGEYHQRWIPLSTDLLDPQI
DSLYTGAGRGVIQDNRLYFFVYGVSRSDEPRDAKCEGQACQGANQELCDNSEKAGLDGNYIISYGILSVD
LSASYEPKIVLAVIPPTQYYQGSGGDLYTSNEGDVYLLYLAPSSWLSLPIIGRLLWIDRFVVSPYTFTVP
SRPGQCHCPTVLGCPVDCVVGVYSDFYPLDFQDLQYVGVTLDSSRNEENPVITVFSDTSRSYSKQIPSSD
TTAIESSTECFKLVNKLWCLSIAEITDTEDGGHRTQLLAVK
>gnl|CDD|275386 cd15465, bS6_mito, Mitochondrial Ribosomal Protein (MRP) S6. bS6_MRPS6 is one of the proteins of the small subunit of the mitochondrial ribosome. Mitochondrial and chloroplastic ribosomes are similar to bacterial ribosomes. The ribosome is a ribonucleoprotein organelle that decodes the genetic information in messenger RNA and forms peptide bonds to synthesize the corresponding polypeptide. Ribosomes consist of a large and a small subunit, which assemble during the initiation stage of protein synthesis. Prokaryotic ribosomes consist of three molecules of RNA and more than 50 proteins. The small subunits of bacterial and eukaryotic ribosomes have the same overall shapes (with structural elements described as head, body, platform, beak and shoulder). Mitochondrial and chloroplastic ribosomes synthesize proteins that are involved in oxidative phosphorylation (ATP generation) and photosynthesis. bS6_MRPS6 is one of the fourteen mitochondrial ribosomal proteins that is known to have significant sequence homology with their bacterial counterpart
LYELVLIARALAEKAELKELLKRTAKAILDNGGVVRKIENLGTRDLPYRIKKHQERHTEGRYFLMDFDAS
PTVVKELREELRRDPDVIRWSIVKL
>gnl|CDD|271318 cd15466, CLU-central, An uncharacterized central domain of CLU mitochondrial proteins. Mutations in the mitochondrial CLU proteins have been shown to result in clustered mitochondria. CLU proteins include Saccharomyces cerevisiae clustered mitochondria protein (Clu1p, alias translation initiation factor 31/TIF31p), Dictyostelium discoideum clustered mitochondria protein homolog (CluA), Caenorhabditis elegans clustered mitochondria protein homolog (CLUH/ Protein KIAA0664), Drosophila clueless (alias clustered mitochondria protein homolog), Arabidopsis clustered mitochondria protein (CLU, alias friendly mitochondria protein/FMT), and human clustered mitochondria protein homolog (CLUH). Dictyostelium CluA is involved in mitochondrial dynamics and is necessary for both, mitochondrial fission and fusion. Drosophila clueless is essential for cytoplasmic localization and function of cellular mitochondria. The Drosophila clu gene interacts genetically with parkin (park, the Drosophila ortholog of a human gene responsible for many familial cases of Parkinson's disease). Arabidopsis CLU/FMT is required for correct mitochondrial distribution and morphology. The specific role CLU proteins play in mitochondrial processes in not yet known. In an early study, S. cerevisiae Clu1/TIF31p was reported as sometimes being associated with the elF3 translation initiation factor. The authors noted, however, that its tentative assignment as a subunit of elf3 was uncertain, and to date there has been no direct evidence for a role of this protein in translation
PIDGASLTELLHRRGINMRYLGKVAELISKLPKLPHLKRLLLTEMVARAAKHILRAYLRSVPLAELSAAV
AHFLNCLLGSSSNPAPSAEIDEELKPAADTSWASLTPSFLWKEIKKEVKKRFRYDLPEESLDEGLRKLSL
LRELCLKVGIQLLARDYDF
>gnl|CDD|271231 cd15467, MV-h, Measles virus hemagglutinin. The hemagglutinin (H) of measles virus plays several roles during viral infection; it participates in virus attachment to host cells via binding to a proteinaceous receptor and it has a stimulating effect on membrane fusion during the entry of the virus into the host cell by interacting with the fusion protein F. This model characterizes the globular ectodomain of measles hemagglutinin, minus the stalk region. Receptors for measles virus have been identified as the signaling lymphocyte activation molecule (SLAM, in particular its distal ectodomain), CD46, and nectin-4 in epithelial cells
NCSGPTTTRGQFSNMSLSLLDLYLGRGYNVSSMVTMTSQGMYGGTYLVEKPNLSSKRSELSQLQMYRVFE
VGVIRNPGLGAPVFHMTNYLEQPVSNDLSNCMLAVGELKLAALCHGESSVTLPYQGSGKGVSFQVVKLGV
WSATPMNSWVPLSTDDDPVIERLYLSSHRGIIADNQAKWAVPTTRTDDKLRMGTCFQQACKGKPPPLCNN
TEWEPLKDNRIPSYGVLSVDLSLTVDLKIKIASGFGPLITHGSGMDLYKSPHNNVYWLTIPPMKNSALGV
INTLEWIPRFKVSPHLLTVPIREAGGDCHAPTYLSAEVDGDVKLSSNLVILPTQDLQYVLATYDTSRVEH
AIVYYVYDPGRSSSYFYPFRLPIKGVPIELRIECFPWDRKLWCHHFCVLADSESGEHVTHSGLVG
>gnl|CDD|271232 cd15468, HeV-G, Glycoprotein G, or hemagglutinin-neuraminidase of Hendravirus and Nipah virus. The glycoprotein (G) of Nendravirus and Nipah virus has a variety of functions during viral infection; it participates in virus attachment to host cells and has a stimulating effect on membrane fusion during the entry of the virus into the host cell. This models characterizes the globular ectodomain of glycoprotein G. The receptors for Hendravirus and Nipah virus have been identified as ephrin B2 (EFNB2) and ephrin B3 (EFNB3)
ICLQKSSNPILKPKLISYTLPVVGQSGTCITNPLLAISEGFFAYSHLERIGSCTRGVSKQRLIGVGEILD
RGDKVPSLFMTSVWTPPNPNTVHHCSPVYNNEFYYVLCAVSTVGDPLLNSTYSSGSLMLTRLAVKPKSNG
GGINQMQLANRSIEGRYDKVMPYGGGGIKQGDTLYFPAVGFLVRTEFKYNDSNCPITKCQYSKPENCRLS
MGIRPNSHYILRNGLLKINLSDGENPKVQFIEISDNRLSIGSPSRIYDSLGQPVFYQSSFSWDTMLKFGD
VLTVDPLVVNWRNNTVISRPGQSQCPRFNTCPEICWEGTYNDAFLLDRINDISVGVYLDSNQTAENPVFT
VFKDNEILYRAPLASDDTNARKTTTSCFLFKNEIWCISLLEIYRTNDNVIRPKLYSVKIPEQC
>gnl|CDD|271233 cd15469, HN, Hemagglutinin-neuraminidase (HN) of parainfluenza virus 5, Newcastle disease virus, and related paramyxoviridiae. The hemagglutinin-neuraminidase (HN) found in this family of viruses has a variety of functions during viral infection; it participates in virus attachment to host cells, cleaves sialic acid off host oligosaccharides, and has a stimulating effect on membrane fusion during the entry of the virus into the host cell. This model characterizes the global ectodomain of HN. Hemagglutinin-neuraminidase ectodomains of these viruses attaches the virion to sialic acid receptors on host cells; the neuraminidase cleaves sialic acid moieties from host cell molecules as well as virus particles, this removal may happen in the trans Golgi network
PSFIPGPTTPKGCTRIPSFSLSDTHWCYTHNVILSGCQDHSKSNQYLSLGVIKTNSDGPPDFKTLASHYL
DDGLNRKSCSIAATPYGCYLLCSTVTVTETDDYASPGPTPMVLGRLDFDGTYTETRITNSEIDQPWAALY
PGVGSGVYYGGRLLFPVYGGLKFPSPLKNNIAGKYFCPQNSNDCKGCQSKQQSNAKSAYYPPYFGGRQIV
NGILVCPLSENLPPNCSVQTISNSQVMMGAEGRLYYIGNKLYLYQRSSSWWPYPQLYIIDLTLTNNQYSA
ISISWIPITSFTRPGNGPCSASNRCPAVCVTGVYQDPWPLSSPSSNSNVLFAGAYLDSETARVNPTIALA
NQTCIINELLITNSTTSAAYTTTTCFKDTGTNKVYCLSIVELSSSLLGEFQIVPFLYE
>gnl|CDD|271254 cd15470, Myo5_CBD, Cargo binding domain of myosin 5. Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins, in case of Myo5a, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin, and in case of Myo5b, Rab11-family interacting protein 2
EDESRLIKNLITDLKPRGAVGLLPGLPAYILFMCIRHADYVNDEAKVRSLLTATINAIKKVLKKHSEDFE
MLSFWLVNTCRLLNCLKQYSGEEEFMKHNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYQQLIKRAEEILQ
PTLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRYNVSQLEE
WLRDKGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTPVDDFEERVTP
SFIRKVQARLNERADSNQLQLLMDTKYIFPVTFPFNPSPVALEELQIPPSLH
>gnl|CDD|271255 cd15471, Myo5p-like_CBD_afadin, cargo binding domain of myosin 5-like of afadin. Afadin is an actin filament (F-actin) and Rap1 small G protein-binding protein, found in cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. It interacts with cell adhesion molecules and signaling molecules and plays a role in the formation of cell junctions, cell polarization, migration, survival, proliferation, and differentiation. Afadin is a multi domain protein, that contains beside a myosin5-like CBD, two Ras-associated domains, a forkhead-associated domain, a PDZ domain, three proline-rich domains, and an F-actin-binding domain
FHEEPFLSAVITYTNSSTPHFKLSPAYTLYLAARYRLSTHYRPELTPTERAHKLTAFLNKIASLIQQVIQ
EQRNIAGALAFWMANASELLNFLKQDRDLSAFSVQAQDVLAEAVQSAFSYLVRCLQEELERSLPAFLDSL
VSLDDEPAIGDVLHTLSSAMRLLRRCRVNAALTIQLFSQLFHFINAWLFNSLVSNPDSGLCTRYWGKRLR
QRLAHVEAWAERQGLELAADCHLDRIVQAANLLTAPKYSAEDVANLSSTCFKLNSLQLRALLSHYQPPPG
EPPIPPDLIERVVRLAESQADELTRADGREVRLEEDPDLHLP
>gnl|CDD|271256 cd15472, Myo5p-like_CBD_Rasip1, cargo binding domain of myosin 5-like of Ras-interacting protein 1. Ras-interacting protein 1 (Rasip1 or RAIN) is an effector of the small G protein Rap1 and plays an important role in endothelial junction stabilization. Rasip1, like afadin, is a multi domain protein, that contains beside a myosin5-like CBD, a Ras-associated domain and a PDZ domain
AHEDALLRRILTLIEPGGDDHKLTPAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVWEKTKELAEK
QPEHQDPASLSLLSIAELAPDLQPLLFWMSNSIELLYFIQQKVPLYEQSMEEELDVGSKESLLSSTLTAS
EEAMTVLEEVIMYTFQQCVYYLTKTLYVALPALLDSNPFTAEERESWSGGSRLPEGVRRVLEIYQATLDL
LRQYQVHPEIASQMFAYLFFFSNASLFNQLMEKGSGGGFFQWSRGVQIRANLDLLLDWLQGAGLGDLAEE
FFRKLSSTVNLLATPKEQLLQMSWSSLRAEFPALNPAQLHHLLRQYQLGSGRGPPWAQPSPEDAPAAVRT
EDILESFDNHPPLVLP
>gnl|CDD|271257 cd15473, Myo5p-like_CBD_DIL_ANK, cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein. DIL and ankyrin domain-containing protein are a group of fungal proteins that contain a domain homologous to the cargo binding domain of class V myosins and ankyrin repeats. Their function is unknown
QMFVFSEDELPRILDLLITNMTPQRSPSQRPVPANLLFLCARYAHYHCSPELLEDLLLGALDRIEDVVEA
NPWDMTLLAFWLSNVTLLLHYLKKDAGLVEATPEFQQELAELINEIFVLIIRDAERRIDKLLDASPRNIT
SLLSSTLYVLELYDVHPAIIIQALSQLFYWLGCELFNRILTNKKYLCRSKAMQIRMNLSALEDWARSNNL
QPEKGESPPRIARSHLAPVIQLLQWLQCLSSLDDFESLIATIQQLDALNPLQLLRAVKDYRYEVNEGRMP
EECVKYLAQLQKDWLDSRYMLPFSLPTDTEMLVAYG
>gnl|CDD|271258 cd15474, Myo5p-like_CBD_fungal, cargo binding domain of fungal myosin V -like proteins. Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum). Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site
DYTLEFTEGLLKSVEVLELKDISDEVSGDNLLFLGHVNFLIYSQMWKSLLELLTQSERFLSHVLSYIASI
VDSLPKKETIPDGAFWLANLHELRSFVVYLLSLIEHSSSDEFSKESEEYWNTLFDKTLKHLSNIYSTWID
KLNKHLSPKIEGAVLVLLTSLDLSELIDLNKEFFNKPKKKMADLITFLNEVYDLLQSFSVQPELLNAIVS
STLQYINVEAFNSLITKRSALSWKRGSQISYNVSRLKEWCHQHGLSDANLQLEPLIQASKLLQLRKDDEN
DFKIILSVCYALNPAQIQKLLDKYQPANYEAPVPKEFLNALEKLIKKENLSLPGRKNNSKMEIPESSNFD
VL
>gnl|CDD|271259 cd15475, MyosinXI_CBD, cargo binding domain of myosin XI. Class XI myosins are a plant specific group, homologous to class V myosins. C-terminal domain of Arabidopsis myosin XI has been shown to be homologous to the cargo-binding domain of yeast myosin V myo2p, which targets myosin to vacuole- and mitochondria, as well as secretory vesicle
ERQQENVDALIKCVSENLGFSEGKPVAAFTIYKCLLHWKSFEAEKTSVFDRIIQTIGSAIEDQDNNDHLA
YWLSNTSTLLFLLQRSLPALLFKQQLTAYVEKIYGIIRDNLKKELSPLLSLCIQAPRTSRGSSSKSSSSA
NSLGQQSPSSHWQSIIKSLNSLLSTLKENHVPPFLVQKIFTQVFSFINVQLFNSLLLRRECCSFSNGEYV
KAGLAELELWCSQATEEYAGSSWDELKHIRQAVGFLVIHQKSRKSYDEITNDLCPVLSVQQLYRICTMYW
DDKYGTQSVSPEVISSMRVLMTEDSNNAVSNSFLLDDDSSIPFSVE
>gnl|CDD|271260 cd15476, Myo5c_CBD, Cargo binding domain of myosin 5C. Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins.MyoVb and myoVc areprimarily expressed in epithelial cells, and have been implicated as motors involved in recycling endosomes
EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRHADYLNDANKLKSLMNAIITGVKQVIKEHQEDF
EMLSFWLSNTYHFLNCLKQYSGEEEFMKHNTPRQNKNCLKNFDLSEHRQILSDLAIRIYHQFISVMENNL
QPTISSILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRCNISYLE
EWLKEKNLQNSNAKETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTPIDDFEKRVT
PSFVRKVQSLLQNREGSSQLMLDTKYRFQVTFPFCPSPQALEMLQVPSSLKL
>gnl|CDD|271261 cd15477, Myo5b_CBD, Cargo binding domain of myosin 5b. Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5b-CBD, Rab11-family interacting protein 2
KEDEALLIRNLVTDLKPQAVSATVPCLPAYILYMCIRHADYINDDQKVHSLLTSTINGIKKVLKKHNDDF
EMTSFWLANTCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGIL
QPMIVSAMLENESIQGLSGVKPMGYRKRSSSMADGDNSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFK
QLFYMINAVTLNNLLLRKDVCSWSTGMQLRYNISQLEEWLRGRNLHQSGAAQTMEPLIQAAQLLQLKKKT
SEDAEAICSLCTALSTQQIVKILNLYTPLNEFEERVTVSFIRTIQAQLQERNDPPQLLLDTKHMFPVLFP
FNPSALTLDSIHIPASLNLDFL
>gnl|CDD|271262 cd15478, Myo5a_CBD, Cargo binding domain of myosin 5a. Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5a-CBD, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin. Mutations in human Myo5a (many of which map to the cargo binding domain) lead to Griscelli syndrome, a severe neurological disease
KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDD
FETVSFWLSNTCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENI
LQPMIVSGMLEHETIQGVSGVKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVK
QMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKT
DDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFIRTIQMRLRDRKDSPQLLMDAKHIFPVTFP
FNPSSLALETIQIPASLGLGFISRV
>gnl|CDD|271263 cd15479, fMyo4p_CBD, cargo binding domain of fungal myosin 4. Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum)
CYTLEVTEGYLKKVNVTEVNGDNVLGPIHVITTVVSSLVRNGLLIQSSKFISKVLLTVESIVMSLPKDET
MLGGIFWLSNLSRLPAFAANQKTLYEANGGDEKDKLTLIYLNDLENETLKVFDKIYSTWLVKFMKHASAH
IEIFDMVLNEKLFKNSGDEKFAKLFTFLNEFDAVLCKFQVVDSMHTKIFNDTLKYLNVMLFNDLITKCPA
LNWKYGYEVDRNIERLVSWFEPRIEDVRPNLIQIIQAVKILQLKISNLNEFKLLFDFWYALNPAQIQAIL
LKYKPANKGEAGVPNEILNYLANVIKRENLSLPGKMEIMLSAQFDSAKN
>gnl|CDD|271264 cd15480, fMyo2p_CBD, cargo binding domain of fungal myosin 2. Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site
DDINDELIRLLEDEEALNEEVLEGLIKGLKIPLPSVANPLSRKEVLFPAHLIILILSEMWRLGLTKESER
FLANVMQTIQQHVMSLKGEDAIVPGAFWLSNVHELLSFVCLAESDILQGIGPGKDMREEEWEEYERLVTV
VKHDLESLEYNIYHTWMKELKKRLEKTMDDILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVTAFND
LLMRRNFLSWKRGLQINYNITRLEEWCKSHDIPEGTLQLEHLMQATKLLQLKKATLEDIEIIYDVCWILT
PAQIQKLISQYYVADYENPISPEILKAVAARVKPEDKSDHLLLIPLVEEVGPFEDPFPREIAGLEAYIPA
WLNLPHIRRLVEL
>gnl|CDD|271252 cd15481, SRP68-RBD, RNA-binding domain of signal recognition particle subunit 68. Signal recognition particles (SRPs) are ribonucleoprotein complexes that target particular nascent pre-secretory proteins to the endoplasmic reticulum. SRP68 is one of the two largest proteins found in SRPs (the other being SRP72), and it forms a heterodimer with SRP72. Heterodimer formation is essential for SRP function. This model characterizes the N-terminal RNA-binding domain SRP68-RBD, a tetratricopeptide-like module. Interactions between SRP68-RBD and SRP RNA (7SL RNA) are thought to facilitate a conformation of SRP RNA that is required for interactions with ribosomal RNA
SPLQLTKGARLQHGLRHGDYARYRKYCSRRLHRLRRRLGLTTKDTKKYKATKKITTEDYAKDKRYLLLLL
LEAERAWAYAMELKSQARQRGKLKKSERKHLISRLRKAVKYAEQLLELAQDEADARTRLEALAYAALMRG
ELAFERKNWEKALKALSLARAILEALAKAASEELDEALKELIEDTIDPSLRYCAY
>gnl|CDD|271234 cd15482, Sialidase_non-viral, Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases
VLLFVPGDEGSDSYRIPSLVTTPNGTLLAFADGRYEGAGDLGGDIDIVVRRSTDGGKTWSEPVTVVDGGG
SGGASYGDPSLVVDPDTGRIFLFYTSGPGGGGEALTGDGTVRVRLSTSDDDGKTWSEPRDLTPQVKPSGW
KFFFTGPGRGIQLSDGRLVFPAYARNGGGGGDGAVVIYSDDGGKTWTRGGGVPSSGAGGDEPSIVELSDG
RLLMNARNSGGGGGRAVAESTDGGETWSEPVPTPSLPDPGCQGSLIRLPDGGRKVLLFSNPASPGKGRTN
LTLRLSDDGGKTWPDVRVLEDGPGSGYSSLTQLPDGTIGLLYEEGRGGGYEGIKFARLT
>gnl|CDD|271235 cd15483, Influenza_NA, Sialidase or neuraminidase (EC 3.2.1.18) of Influenza viruses A and B. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates. Viral neuraminidases, such as this family from Influenza viruses A and B, play a vital role in pathogenesis. Influenza neuraminidase cleaves an alpha-ketosidic linkage between sialic acid and a neighboring sugar residue. During budding of virus particles from the infected cell, the sialidase helps to prevent the newly formed viral particles from aggregating. The viral sialidase cleaves terminal sialic acid from glycan structures on the infected cell surface, promoting virus release and the spread of virus to neighboring cells that are not yet infected. Also, sialidase modifies mucins in the respiratory tract and may improve access of the viral particle to its target cells. Sialidases have a six-bladed beta-propeller fold
EFLNWTKPLCQISGFAIYSKDNGIRIGEGGDVLVIREPFVSCDPGECRTFALTQGATLNGKHSNGTVHDR
SPYRTLISVPLGSPPTVYNSRFECIAWSSSACHDGKAWLHIGISGPDNNATAVIKYGGRPTDTIGSWANN
ILRTQESECVCINGTCYVVMTDGSASGQASTRILKIKEGKITKEIPLSGSAQHIEECSCYPRYGKVECVC
RDNWKGSNRPVVDIDMEDLTYESGYICSGVVTDTPRPDDSSSTGSCRDPNNGRGNNGVKGFSFRQGNGVW
MGRTISKSSRSGYEMLKVPDGWTPDSKSQVNRQVIVDNKNWSGYSGSFSIEGKEGSCIVPCFYVELIRGR
PKETRVWWTSNSIVVFCGVSSTYGGWSWPDGANIPF
>gnl|CDD|271251 cd15484, uS7_plant, plant ribosomal protein S7. uS7, also known as Ribosomal protein (RP)S7, is an important part of the translation process which is universally present in the small subunit of prokaryotic and eukaryotic ribosomes. The ribosome small subunit is one of the two subunits of ribosome organelles that use mRNA as a template for protein synthesis in a process called translation. The small subunits of bacteria and eukaryotes have the same shape of head, body, platform, beak, and shoulder. RPS7 is located at the head of the small subunit. RPS7 is a primary ribosomal RNA (rRNA) binding protein that assists in rRNA folding and the binding of other proteins during small subunit assembly in all species. RPS7 is also involved in the formation of the mRNA exit channel at the interface of the large and small subunits. Some ribosomal proteins have extra ribosomal functions in cell differentiation and apoptosis
KLLIKKFVNFLMKKGKKTKARTILFKTFHLLKQKQSAQTEDVLVILVTAVENVKPSFEVRKVRIAGTTQL
IPAALSPNKQETLAIRWILEAAKKKQRKQSKKRYSFAYCLADEILDASKKQGKARQKRDELHKLAEANRS
LAHYRWW
>gnl|CDD|271243 cd15485, ZIP_Cat8, Leucine zipper Dimerization domain of transcription factor Cat8 and similar proteins. Cat8p binds to carbon source-responsive element (CSRE) motifs and activates target genes under conditions of glucose deprivation. It mediates the transcriptional control of at least nine genes (ACS1, FBP1, ICL1, IDP2, JEN1, MLS1, PCK1, SFC1, and SIP4) under non-fermentative growth conditions in yeast. Studies show another 25 genes or open reading frames whose expression at the transition between the fermentative and the oxidative metabolism (diauxic shift) is altered in the absence of Cat8p. This Cat8p-dependent control results in a parallel alteration in mRNA and protein synthesis. The biochemical functions of proteins encoded by Cat8p-dependent genes are essentially related to the first steps of ethanol utilization, the glyoxylate cycle, and gluconeogenesis. Cat8p is a member of the Gal4p family of transcriptional activators which contain an N-terminal DNA-binding domain with a Zn2Cys6 binuclear cluster that interact with CCG triplets and a leucine zipper-like heptad repeat that dimerizes. Dimerization allows binding of targets which contain two CCG motifs oriented in an inverted (CGG-CCG), direct (CCG-CCG), or everted (CCG-CGG) manner
FPRGYTESLEERVRILEDENQVLKAEL
>gnl|CDD|271244 cd15486, ZIP_Sip4, Leucine zipper Dimerization domain transcription factor Sip4p and similar fungal proteins. Sip4p binds to carbon source-responsive element (CSRE) motifs and activates transcription of target genes under conditions of glucose deprivation. Its function is modulated through phosphorylation by SNF1 protein kinase, a protein essential for expression of glucose-repressed genes in response to glucose deprivation. Sip4p is a member of the Gal4p family of transcriptional activators which contain an N-terminal DNA-binding domain with a Zn2Cys6 binuclear cluster that interact with CCG triplets and a leucine zipper-like heptad repeat that dimerizes. Dimerization allows binding of targets which contain two CCG motifs oriented in an inverted (CGG-CCG), direct (CCG-CCG), or everted (CCG-CGG) manner
PRGYTEVLENRVARLEALLSKLGANVD
>gnl|CDD|275387 cd15487, bS6_chloro_cyano, 30S ribosomal protein S6 of chloroplasts and cyanobacteria. bS6 is one of the components of the small subunit of the prokaryotic ribosome, a ribonucleoprotein organelle that decodes the genetic information in messenger RNA and forms peptide bonds to synthesize the corresponding polypeptides. Mitochondrial and chloroplastic ribosomes are similar to bacterial ribosomes. Ribosomes consist of a large and a small subunit, which assemble during the initiation stage of protein synthesis. Prokaryotic ribosomes consist of three molecules of RNA and more than 50 proteins. The small subunits of bacterial and eukaryotic ribosomes have the same overall shapes (with structural elements described as head, body, platform, beak and shoulder). The bacterial ribosomal protein S6 is important for the assembly of the central domain of the small subunit via heterodimerization with ribosomal protein S18
MLRSYETMYILRPDLTEEQVEQLINKYQELLTENGAENIEVQNRGKRRLAYEIKKFRDGIYVQMNYTADG
SAVAPLERAMRLSEEVIRYLTIKV
>gnl|CDD|350626 cd15488, Tm-1-like, ATP-binding domain found in plant Tm-1-like (Tm-1L) and similar proteins. Members of this family have been annotated as UPF0261-domain containing proteins. They are found in plants, fungi, bacteria, and archaea. A three-dimensional structure of a complex between the tomato resistance gene product Tm-1 and tomato mosaic virus helicase reveals an organization encompassing two distinct structurally similar domains and an ATP-binding site present in the N-terminal subdomain. The Tm-1-like domain is found co-occurring with a C-terminal TIM-barrel signal transduction (TBST) domain in some plant proteins like Tm-1, and with an N-terminal ABC-transporter ATP-binding domain in a few bacterial proteins
TVLLIGTLDTKGEELAYLRDRIEARGVKVLLIDVGVLGEPPFAPDISREEVAAAAGGTLEELRASGDRGE
AVEAMAEGAAKLVRELYAEGKIDGVIGLGGSGGTSLATAAMRALPIGVPKLMVSTVASGDTSPYVGTSDI
TMMPSVVDIAGLNRISRRVLSNAAGAIAGMAKAYEPRAAKEDKPLIAITMFGVTTPCVTRARELLEEKGY
EVLVFHATGTGGRAMEELIREGLFDGVLDLTTTELADELVGGVLSAGPDRLEAAGRAGIPQVVSPGALDM
VNFGPPETVPERFKGRKLYEHNPQVTLMRTTPEENRELGRIIAEKLNRAKGPVAVLIPLRGFSALDRPGG
PFYDPEADAALFDALKANLRPDIEVIEVDAHINDPEFAEAAVEALLELL
>gnl|CDD|276966 cd15489, PHD_SF, PHD finger superfamily. The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies
SCIVCGKGGDLGGELLQCDGCGKWFHADCLGPPLSSFVPNGKWICPVC
>gnl|CDD|294011 cd15490, eIF2_gamma_III, Domain III of eukaryotic initiation factor eIF2 gamma. This family represents the C-terminal domain of the gamma subunit of eukaryotic translation initiation factor 2 (eIF2-gamma) found in eukaryotes and archaea. eIF2 is a G protein that delivers the methionyl initiator tRNA to the small ribosomal subunit and releases it upon GTP hydrolysis after the recognition of the initiation codon. eIF2 is composed three subunits, alpha, beta and gamma. Subunit gamma shows strongest conservation, and it confers both tRNA binding and GTP/GDP binding
PPVYTELEIEYHLLERVVGVKEEIKVEKIKKGEVLMLNIGSATTGGVVTSVKKDEAEVELKRPVCAEIGE
RVAISRRIDGRWRLIGWGII
>gnl|CDD|294012 cd15491, selB_III, Domain III of selenocysteine-specific translation elongation factor. This family represents domain III of bacterial selenocysteine (Sec)-specific elongation factor (EFSec), homologous to domain III of EF-Tu. SelB is a specialized translation elongation factor responsible for the co-translational incorporation of selenocysteine into proteins by recoding of a UGA stop codon in the presence of a downstream mRNA hairpin loop, called Sec insertion sequence (SECIS) element
RPTYRIDVRLTLLKSAPRPLKHRTRVRLHLGTSEVLGRVVLLDRDELAPGEEALAQLRLEEPVVAKRGDR
FILRSYSPMRTIGGGRV
>gnl|CDD|276967 cd15492, PHD_BRPF_JADE_like, PHD finger found in BRPF proteins, Jade proteins, protein AF-10, AF-17, and similar proteins. The family includes BRPF proteins, Jade proteins, protein AF-10 and AF-17. BRPF proteins are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a canonical Cys4HisCys3 plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. PHD and ePHD fingers both bind to lysine 4 of histone H3 (K4H3), bromodomains interact with acetylated lysines on N-terminal tails of histones and other proteins, and PWWP domains show histone-binding and chromatin association properties. Jade proteins are required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6, to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. AF-10, also termed ALL1 (acute lymphoblastic leukemia)-fused gene from chromosome 10 protein, is a transcription factor that has been implicated in the development of leukemia following chromosomal rearrangements between the AF10 gene and one of at least two other genes, MLL and CALM. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is a putative transcription factor that may play a role in multiple signaling pathways. All Jade proteins, AF-10, and AF-17 contain a canonical PHD finger followed by a non-canonical ePHD finger. This model corresponds to the canonical PHD finger
VCDVCLDGESEDDNEIVFCDGCNVAVHQSCYGIPLIPEGDWFCRKC
>gnl|CDD|276968 cd15493, PHD_JMJD2, PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone demethylases. JMJD2 proteins, also termed lysine-specific demethylase 4 histone demethylases (KDM4), have been implicated in various cellular processes including DNA damage response, transcription, cell cycle regulation, cellular differentiation, senescence, and carcinogenesis. They selectively catalyze the demethylation of di- and trimethylated H3K9 and H3K36. This model contains only three JMJD2 proteins, JMJD2A-C, which all contain jmjN and jmjC domains in the N-terminal region, followed by a Cys4HisCys3 canonical PHD finger, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a Tudor domain. JMJD2D is not included in this family, since it lacks both PHD and Tudor domains and has a different substrate specificity. JMJD2A-C are required for efficient cancer cell growth. This model corresponds to the Cys4HisCys3 canonical PHD finger
HCAICSLFRLLVCSRCCVCVHASCYGVPDIPGDGEGWKCDRC
>gnl|CDD|276969 cd15494, PHD_ATX1_2_like, PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like protein ATX1, ATX2, and similar proteins. The family includes A. thaliana ATX1 and ATX2, both of which are sister paralogs originating from a segmental chromosomal duplication. They are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also termed protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also termed protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain containing proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical Cys4HisCys3 plant homeodomain (PHD) finger, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a C-terminal SET domain; this model corresponds to the Cys4HisCys3 canonical PHD finger
KCSVCGEDEEYEDNLLLQCDKCRMMVHMRCYGVLEPPPGALWLCNLC
>gnl|CDD|276970 cd15495, PHD_ATX3_4_5_like, PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like protein ATX3, ATX4, ATX5, and similar proteins. The family includes A. thaliana ATX3 (also termed protein SET domain group 14, or trithorax-homolog protein 3), ATX4 (also termed protein SET domain group 16, or trithorax-homolog protein 4) and ATX5 (also termed protein SET domain group 29, or trithorax-homolog protein 5), which belong to the histone-lysine methyltransferase family. They show distinct phylogenetic origins from the ATX1 and ATX2 family. They are multi-domain containing proteins that consist of an N-terminal PWWP domain, a canonical Cys4HisCys3 plant homeodomain (PHD) finger, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a C-terminal SET domain; this model corresponds to the Cys4HisCys3 canonical PHD finger
RCAVCNEGEDDDNNPLITCNRCQISVHQKCYGIREVDPDGSWVCRAC
>gnl|CDD|276971 cd15496, PHD_PHF7_G2E3_like, PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3). PHF7, also termed testis development protein NYD-SP6, is a testis-specific plant homeodomain (PHD) finger-containing protein that associates with chromatin and binds histone H3 N-terminal tails with a preference for dimethyl lysine 4 (H3K4me2). It may play an important role in stimulating transcription involved in testicular development and/or spermatogenesis. PHF7 contains a canonical Cys4HisCys3 PHD finger and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which may be involved in activating transcriptional regulation. G2E3 is a dual function ubiquitin ligase (E3) that may play a possible role in cell cycle regulation and the cellular response to DNA damage. It is essential for prevention of apoptosis in early embryogenesis. It is also a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization. G2E3 contains two distinct RING-like ubiquitin ligase domains that catalyze lysine 48-linked polyubiquitination, and a C-terminal catalytic HECT domain that plays an important role in ubiquitin ligase activity and in the dynamic subcellular localization of the protein. The RING-like ubiquitin ligase domains consist of a PHD finger and an ePHD finger. This model corresponds to the Cys4HisCys3 canonical PHD finger
RCDARKCLCPQGREYNEPEGKWELVLCQSCGSRGTHRACSSLRSWEQSWECVEC
>gnl|CDD|276972 cd15497, PHD1_Snt2p_like, PHD finger 1 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins. Snt2p is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical Cys4HisCys3 plant homeodomain (PHD) fingers, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain; this model corresponds to the first canonical Cys4HisCys3 PHD finger
SCKVCKEWCASDDSVRCDECKVSYHLLCVDPPLTKKPNRGFVWSCAPC
>gnl|CDD|276973 cd15498, PHD2_Snt2p_like, PHD finger 2 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins. This group corresponds to Snt2p and similar proteins. Snt2p is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical Cys4HisCys3 plant homeodomain (PHD) fingers, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain; this model corresponds to the second canonical Cys4HisCys3 PHD finger
KCSVCSEQFASNFNTSLSCYNCGLNVHASCYGITVPGKMNKVKNLKSYKWLCDPC
>gnl|CDD|276974 cd15499, PHD1_MTF2_PHF19_like, PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) family proteins MTF2, PHF19, and similar proteins. The family includes two PCL family proteins, metal-response element-binding transcription factor 2 (MTF2/PCL2) and PHF19/PCL3, which are homologs of PHD finger protein1 (PHF1). PCL family proteins are accessory components of the polycomb repressive complex 2 (PRC2) core complex and all contain an N-terminal Tudor domain followed by two PHD fingers, and a C-terminal MTF2 domain. They specifically recognize tri-methylated H3K36 (H3K36me3) through their N-terminal Tudor domains. The interaction between their Tudor domains and H3K36me3 is critical for both the targeting and spreading of PRC2 into active chromatin regions and for the maintenance of optimal repression of poised developmental genes where PCL proteins, H3K36me3, and H3K27me3 coexist. Moreover, unlike other PHD finger-containing proteins, the first PHD fingers of PCL proteins do not display histone H3K4 binding affinity and they do not affect the Tudor domain binding to histones. This model corresponds to the first PHD finger
TCSICGGAEARDGNEILICDKCDKGYHQLCHSPKVRTSPLEGDEKWFCSRCVF
>gnl|CDD|276975 cd15500, PHD1_PHF1, PHD finger 1 found in PHD finger protein1 (PHF1). PHF1, also termed polycomb-like protein 1 (PCL1), together with JARID2 and AEBP2, associates with the polycomb repressive complex 2 (PRC2), which is the major H3K27 methyltransferase that regulates pluripotency, differentiation, and tumorigenesis through catalysis of histone H3 lysine 27 trimethylation (H3K27me3) on chromatin. PHF1 is essential in epigenetic regulation and genome maintenance. It acts as a dual reader of Lysine trimethylation at Lysine 36 of Histone H3 and Lysine 27 of Histone variant H3t. PHF1 consists of an N-terminal Tudor domain followed by two PHD fingers, and a C-terminal MTF2 domain. Its Tudor domain selectively binds to histone H3K36me3. Moreover, PHF1 is required for efficient H3K27me3 and Hox gene silencing. It can mediate deposition of the repressive H3K27me3 mark and acts as a cofactor in early DNA-damage response. This model corresponds to the first PHD finger
ICCVCDSETVSPKNPLVNCEKCHHAYHQECHVPRVPLESAGDGDSWMCRQC
>gnl|CDD|276976 cd15501, PHD_Int12, PHD finger found in integrator complex subunit 12 (Int12) and similar proteins. Int12, also termed IntS12, or PHD finger protein 22, is a component of integrator, a multi-protein mediator of small nuclear RNA processing. The integrator complex directly interacts with the C-terminal domain of RNA polymerase II (RNAPII) largest subunit and mediates the 3' end processing of small nuclear RNAs (snRNAs) U1 and U2. Different from other components of integrator, Int12 contains a PHD finger, which is not required for snRNA 3' end cleavage. Instead, Int12 harbors a small microdomain at its N-terminus which is necessary and sufficient for Int12 function; this microdomain facilitates Int12 binding to Int1 and promotes snRNA 3' end formation
SCVVCKQMDVTSGNQLVECQECHNLYHQECHKPPVTDKDVNDPRLVWYCSRC
>gnl|CDD|276977 cd15502, PHD_Phf1p_Phf2p_like, PHD finger found in Schizosaccharomyces pombe SWM histone demethylase complex subunits Phf1 (Phf1p) and Phf2 (Phf2p). Phf1p and Phf2p are components of the SWM histone demethylase complex that specifically demethylates histone H3 at lysine 9 (H3K9me2), a specific tag for epigenetic transcriptional activation. They function as corepressors and play roles in regulating heterochromatin propagation and euchromatic transcription. Both Phf1p and Phf2p contain a plant homeodomain (PHD) finger
VCIVCQRGHSPKSNRIVFCDGCNTPYHQLCHDPSIDDEVVEDPDAEWFCKKC
>gnl|CDD|276978 cd15503, PHD2_MTF2_PHF19_like, PHD finger 2 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) family proteins MTF2, PHF19, and similar proteins. The PCL family includes PHD finger protein1 (PHF1) and its homologs metal-response element-binding transcription factor 2 (MTF2/PCL2) and PHF19/PCL3, which are accessory components of the Polycomb repressive complex 2 (PRC2) core complex and all contain an N-terminal Tudor domain followed by two plant homeodomain (PHD) fingers, and a C-terminal MTF2 domain. PCL proteins specifically recognize tri-methylated H3K36 (H3K36me3) through their N-terminal Tudor domains. The interaction between their Tudor domains and H3K36me3 is critical for both the targeting and spreading of PRC2 into active chromatin regions and for the maintenance of optimal repression of poised developmental genes where PCL proteins, H3K36me3, and H3K27me3 coexist. Moreover, unlike other PHD finger-containing proteins, the first PHD finger of PCL proteins do not display histone H3K4 binding affinity and they do not affect the Tudor domain binding to histones. This model corresponds to the second PHD finger
YCYCGGPGEWNLKMLQCCKCRQWFHEACLQCLKKPLLYGDRFYNFCCSVCNN
>gnl|CDD|276979 cd15504, PHD_PRHA_like, PHD finger found in Arabidopsis thaliana pathogenesis-related homeodomain protein (PRHA) and similar proteins. PRHA is a homeodomain protein encoded by a single-copy Arabidopsis thaliana homeobox gene, prha. It shows the capacity to bind to TAATTG core sequence elements but requires additional adjacent bases for high-affinity binding. PRHA contains a plant homeodomain (PHD) finger, a homeodomain, peptide repeats and a putative leucine zipper dimerization domain
FCAKCQSGEASPDNDILLCDGGCNRAYHQKCLEPPLLTEDIPPEDEGWLCPLC
>gnl|CDD|276980 cd15505, PHD_ING, PHD finger found in the inhibitor of growth (ING) protein family. The ING family includes a group of tumor suppressors, ING1-5, which act as readers and writers of the histone epigenetic code, affecting DNA damage response, chromatin remodeling, cellular senescence, differentiation, cell cycle regulation and apoptosis. They may have a general role in mediating the cellular response to genotoxic stress through binding to and regulating the activities of histone acetyltransferase (HAT) and histone deacetylase (HDAC) chromatin remodeling complexes. All ING proteins contain an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger
YCICNQVSYGEMVACDNPNCPIEWFHFECVGLTAKPKGKWYCPEC
>gnl|CDD|276981 cd15506, PHD1_KMT2A_like, PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B). This family includes histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A (MLL1) and KMT2B (MLL2), which comprise the mammalian Trx branch of the COMPASS family, and are both essential for mammalian embryonic development. KMT2A regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex. KMT2B is a second human homolog of Drosophila trithorax, located on chromosome 19 and functions as the catalytic subunit in the MLL2 complex. It plays a critical role in memory formation through mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. Both KMT2A and KMT2B contain a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the first PHD finger
LCFLCGSAGLNELLYCSVCCEPYHTFCLEEAERPLNINKDNWCCRRC
>gnl|CDD|276982 cd15507, PHD2_KMT2A_like, PHD finger 2 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B). This family includes histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A (MLL1) and KMT2B (MLL2), which comprise the mammalian Trx branch of the COMPASS family, and are both essential for mammalian embryonic development. KMT2A regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex. KMT2B is a second human homolog of Drosophila trithorax, located on chromosome 19 and functions as the catalytic subunit in the MLL2 complex. It plays a critical role in memory formation through mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. Both KMT2A and KMT2B contain a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the second PHD finger
FCHVCGRKGQAQKQLLECEKCQRGYHVDCLGPSYPTKPTRKKKTWICSKC
>gnl|CDD|276983 cd15508, PHD3_KMT2A_like, PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B). This family includes histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A (MLL1) and KMT2B (MLL2), which comprise the mammalian Trx branch of the COMPASS family, and are both essential for mammalian embryonic development. KMT2A regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex. KMT2B is a second human homolog of Drosophila trithorax, located on chromosome 19 and functions as the catalytic subunit in the MLL2 complex. It plays a critical role in memory formation through mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. Both KMT2A and KMT2B contain a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the third PHD finger
YCPLCEKCYDDDDYDSKMMQCSQCDHWVHAKCEGLSDEMYEILSYLPESIEYTCSLC
>gnl|CDD|276984 cd15509, PHD1_KMT2C_like, PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D). KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3) or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, several plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the first PHD finger
NCAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVRPTPLVRAGWQCPEC
>gnl|CDD|276985 cd15510, PHD2_KMT2C_like, PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D). KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3) or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions. This model corresponds to the second PHD finger
VCQACRQPGDDTKMLVCETCDKGYHTSCLRPVMSSIPKYGWKCKNC
>gnl|CDD|276986 cd15511, PHD3_KMT2C, PHD finger 3 found in Histone-lysine N-methyltransferase 2C (KMT2C). KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3) or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains several plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains. This model corresponds to the third PHD finger
PCPACKKNLDPELQKDMLHCHVCKRWIHLECEKPNDNELLDQLKEDYICSLC
>gnl|CDD|276987 cd15512, PHD4_KMT2C_like, PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD domain 3 found in KMT2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3) or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, several plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, two extended PHD (ePHD) fingers, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the fourth PHD finger of KMT2C and the third domain of KMT2D
MCVSCGSFGRGAEGRLIACSQCGQCYHPYCVNVKVTKVILSKGWRCLDC
>gnl|CDD|276988 cd15513, PHD5_KMT2C_like, PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in KMT2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, several plant homeodomain (PHD) fingers, extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the fifth PHD finger of KMT2C and the fourth PHD finger of KMT2D
VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV
>gnl|CDD|276989 cd15514, PHD6_KMT2C_like, PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 5 found in KMT2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, several plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the sixth PHD finger of KMT2C and the fifth PHD finger of KMT2D
KCPVCSRSYNEGELIIQCSQCERWLHGACDSLRTEEEAERAADNGYRCLLC
>gnl|CDD|276990 cd15515, PHD1_KDM5A_like, PHD finger 1 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and similar proteins. The JARID subfamily within the JmjC proteins includes Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and a Drosophila homolog, protein little imaginal discs (Lid). KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. KDM5C is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me2 and H3K4me3), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. This family also includes Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent H3K4me3 demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as two or three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger
ICQVCGRGDDEDKLLLCDGCDDSYHTFCLIPPLPDIPPGDWRCPKC
>gnl|CDD|276991 cd15516, PHD2_KDM5A_like, PHD finger 2 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D, and similar proteins. The JARID subfamily within the JmjC proteins includes Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and a Drosophila homolog protein, little imaginal discs (Lid). KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. KDM5C is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me3 and H3K4me2), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. The family also includes Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as two or three plant homeodomain (PHD) fingers. This model corresponds to the second PHD finger
ICLCGKALAAGMLQCELCQDWFHGSCVAVPRISSSPRPLAWWEGDRKFLCPLC
>gnl|CDD|276992 cd15517, PHD_TCF19_like, PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and KDM5B, and other similar proteins. TCF-19 was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interaction with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. This family also includes Caenorhabditis elegans Lysine-specific demethylase 7 homolog (ceKDM7A). ceKDM7A (also termed JmjC domain-containing protein 1.2, PHD finger protein 8 homolog, or PHF8 homolog) is a plant homeodomain (PHD)- and JmjC domain-containing protein that functions as a histone demethylase specific for H3K9me2 and H3K27me2. The binding of the PHD finger to H3K4me3 guides H3K9me2- and H3K27me2-specific demethylation by its catalytic JmjC domain in a trans-histone regulation mechanism. In addition, this family includes plant protein OBERON 1 and OBERON 2, Alfin1-like (AL) proteins, histone acetyltransferases (HATs) HAC, and AT-rich interactive domain-containing protein 4 (ARID4)
VCGICNLETAAVDELWVQCDGCDKWFHQFCLGLSNERYADEDKFKCPNC
>gnl|CDD|276993 cd15518, PHD_Ecm5p_Lid2p_like, PHD finger found in Saccharomyces cerevisiae extracellular matrix protein 5 (Ecm5p), Schizosaccharomyces pombe Lid2 complex component Lid2p, and similar proteins. The family includes Saccharomyces cerevisiae Ecm5p, Schizosaccharomyces pombe Lid2 complex component Lid2p, and similar proteins. Ecm5p is a JmjC domain-containing protein that directly removes histone lysine methylation via a hydroxylation reaction. It associates with the yeast Snt2p and Rpd3 deacetylase, which may play a role in regulating transcription in response to oxidative stress. Ecm5p promotes oxidative stress tolerance, while Snt2p ultimately decreases tolerance. Ecm5p contains an N-terminal ARID domain, a JmjC domain, and a C-terminal plant homeodomain (PHD) finger. Lid2p is a trimethyl H3K4 (H3K4me3) demethylase responsible for H3K4 hypomethylation in heterochromatin. It interacts with the histone lysine-9 methyltransferase, Clr4, through the Dos1/Clr8-Rik1 complex, and mediates H3K9 methylation and small RNA production. It also acts cooperatively with the histone modification enzymes Set1 and Lsd1 and plays an essential role in cross-talk between H3K4 and H3K9 methylation in euchromatin. Lid2p contains a JmjC domain, three PHD fingers and a JmjN domain. This model includes the second PHD finger of Lid2p
YCFCRQGEGGTMIECEICKEWYHVKCIKNGRWKLDDDDKFVCPIC
>gnl|CDD|276994 cd15519, PHD1_Lid2p_like, PHD finger 1 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar proteins. Lid2p is a trimethyl H3K4 (H3K4me3) demethylase responsible for H3K4 hypomethylation in heterochromatin. It interacts with the histone lysine-9 methyltransferase, Clr4, through the Dos1/Clr8-Rik1 complex, and mediates H3K9 methylation and small RNA production. It also acts cooperatively with the histone modification enzymes Set1 and Lsd1 and plays an essential role in cross-talk between H3K4 and H3K9 methylation in euchromatin. Lid2p contains a JmjC domain, three PHD fingers and a JmjN domain. This model corresponds to the first PHD finger
GCEVCGLDDNEGEVLLCDGCDAEYHTSCLDPPLGEIPPGTWFCPSC
>gnl|CDD|276995 cd15520, PHD3_Lid2p_like, PHD finger 3 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar proteins. Lid2p is a trimethyl H3K4 (H3K4me3) demethylase responsible for H3K4 hypomethylation in heterochromatin. It interacts with the histone lysine-9 methyltransferase, Clr4, through the Dos1/Clr8-Rik1 complex, and mediates H3K9 methylation and small RNA production. It also acts cooperatively with the histone modification enzymes Set1 and Lsd1, and plays an essential role in cross-talk between H3K4 and H3K9 methylation in euchromatin. Lid2p contains a JmjC domain, three PHD fingers and a JmjN domain. The family corresponds to the third PHD finger
RCGCGEGFNIADRMIFCDRCERTVHLDCVGLSDRIVDSPSEFFCPEC
>gnl|CDD|276996 cd15521, PHD_VIN3_plant, PHD finger found in Arabidopsis thaliana protein Vernalization Insensitive 3 (VIN3) and similar proteins. The lineage specific VIN3 family of proteins includes VIN3, VIN3-like1 (VIL1, or Vernalization5 (VRN5)), VIN3-like2 (VIL2, or Vernalization5/VIN3-like protein 1 (VEL1)), VIN3-like3 (VIL3 or Vernalization5/VIN3-like protein 2 (VEL2)), and similar proteins. They contain a plant homeodomain (PHD) finger, and collectively repress different sets of members of the Flowering LOCUS C (FLC) gene family during the course of vernalization. Both VIN3 and VIL1 are required for modifying the histone architecture of the MADS box floral repressor FLC in response to prolonged cold exposure in Arabidopsis. VIN3 is required for both Histone H3 Lys 9 (H3K9) and Histone H3 Lys 27 (H3K27) methylation at FLC chromatin, ultimately leading to its repression. It is regulated by the components of Polycomb Response Complex2 (PRC2), which trimethylates histone H3 Lys 27 (H3K27me3). VIL1 appears to play a prominent role in regulating FLC by vernalization. VIL2 acts together with PRC2 to repress the floral repressor MAF5, an FLC clade member, in a photoperiod-dependent manner to accelerate flowering under non-inductive photoperiods
SCCICRKFDDNKDPSLWLTCGSEKGFDVESCGLSCHLECALKSEKSGVGKNSIDLDGCFYCVSC
>gnl|CDD|276997 cd15522, PHD_TAF3, PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3). TAF3 (also termed 140 kDa TATA box-binding protein-associated factor, TBP-associated factor 3, transcription initiation factor TFIID 140 kDa subunit (TAF140), or TAFII-140, is an integral component of TFIID) is a general initiation factor (GTF) that plays a key role in preinitiation complex (PIC) assembly through core promoter recognition. The interaction of H3K4me3 with TAF3 directs global TFIID recruitment to active genes, which regulates gene-selective functions of p53 in response to genotoxic stress. TAF3 is highly enriched in embryonic stem cells and is required for endoderm lineage differentiation and prevents premature specification of neuroectoderm and mesoderm. Moreover, TAF3, along with TRF3, forms a complex that is essential for myogenic differentiation. TAF3 contains a plant homeodomain (PHD) finger. This family also includes Drosophila melanogaster BIP2 (Bric-a-brac interacting protein 2) protein, which functions as an interacting partner of D. melanogaster p53 (Dmp53)
ICPICKKPDDGSPMIGCDECDDWYHWECVGITDEPPEEDDWFCPKC
>gnl|CDD|276998 cd15523, PHD_PHF21A, PHD finger found in PHD finger protein 21A (PHF21A). PHF21A (also termed BHC80a or BRAF35-HDAC complex protein BHC80) along with HDAC1/2, CtBP1, CoREST, and BRAF35, is associated with LSD1, a lysine (K)-specific histone demethylase. It inhibits LSD1-mediated histone demethylation in vitro. PHF21A is predominantly present in the central nervous system and spermatogenic cells and is one of the six components of BRAF-HDAC complex (BHC) involved in REST-dependent transcriptional repression of neuron-specific genes in non-neuronal cells. It acts as a scaffold protein in BHC in neuronal as well as non-neuronal cells and also plays a role in spermatogenesis. PHF21A contains a C-terminal plant homeodomain (PHD) finger that is responsible for the binding directly to each of five other components of BHC, and of organizing BHC mediating transcriptional repression
FCSVCRKSGELLMCDTCSLVYHLDCLDPPLKTIPKGMWICPKC
>gnl|CDD|276999 cd15524, PHD_PHF21B, PHD finger found in PHD finger protein 21B (PHF21B). PHF21B is a plant homeodomain (PHD) finger-containing protein whose biological function remains unclear. It shows high sequence similarity with PHF21A, which is associated with LSD1, a lysine (K)-specific histone demethylase and inhibits LSD1-mediated histone demethylation in vitro. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins
HCAACKRGGNLQPCGTCPRAYHLDCLDPPLKTAPKGVWVCPKC
>gnl|CDD|277000 cd15525, PHD_UHRF1_2, PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and UHRF2. UHRF1 is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumour suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of transcription factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF2 was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. Both UHRF1 and UHRF2 contain an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal RING finger
ACHVCGGKQDPEKQLLCDECDMAYHLYCLDPPLTSLPDDDEWYCPDC
>gnl|CDD|277001 cd15526, PHD1_MOZ_d4, PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ), its factor (MORF), and d4 gene family proteins. MOZ is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity and to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ-related factor (MORF) is a ubiquitously expressed transcriptional regulator with intrinsic HAT activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. Both MOZ and MORF are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are implicated in human leukemias. MOZ is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphoma genesis and bone development, and its homologs. This family also includes three members of the d4 gene family, DPF1 (neuro-d4), DPF2 (ubi-d4/Requiem), and DPF3 (cer-d4), which function as transcription factors and are involved in transcriptional regulation of genes via changing the condensed/decondensed state of chromatin in nucleus. DPF2 is ubiquitously expressed and it acts as a transcription factor that may participate in developmentally programmed cell death. DPF1 and DPF3 are expressed predominantly in neural tissues, and they may be involved in the transcription regulation of neuro specific gene clusters. All family members contain two plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger
ICDFCLGTDEKNNKTGEPEELISCADCGSSGHPSCLKFSPGLTDAVKSYRWQCIEC
>gnl|CDD|277002 cd15527, PHD2_KAT6A_6B, PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF). MOZ, also termed histone acetyltransferase KAT6A, YBF2/SAS3, SAS2 and TIP60 protein 3 (MYST-3), or runt-related transcription factor-binding protein 2, or zinc finger protein 220, is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ-related factor (MORF), also termed MOZ2, or histone acetyltransferase KAT6B, or MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4 (MYST4), is a ubiquitously expressed transcriptional regulator with intrinsic HAT activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. Both MOZ and MORF are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are also implicated in human leukemias. MOZ is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphomagenesis and bone development, and its homologs. MOZ contains a linker histone 1 and histone 5 domains and two plant homeodomain (PHD) fingers. In contrast, MORF contains an N-terminal region containing two PHD fingers, a putative HAT domain, an acidic region, and a C-terminal Ser/Met-rich domain. The family corresponds to the first PHD finger
TCSVCQDSGNADNLLFCDACDKGFHMECHDPPLTRMPKGKWVCQIC
>gnl|CDD|277003 cd15528, PHD1_PHF10, PHD finger 1 found in PHD finger protein 10 (PHF10) and similar proteins. PHF10, also termed BRG1-associated factor 45a (BAF45a), or XAP135, is a ubiquitously expressed transcriptional regulator that is required for maintaining the undifferentiated status of neuroblasts. It contains a SAY (supporter of activation of yellow) domain and two adjacent plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger
VCGICEKGGKSNKGEPEELIHCSQCGNSGHPSCLEMSDEMVAVIKTYPWQCMEC
>gnl|CDD|277004 cd15529, PHD2_PHF10, PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins. PHF10, also termed BRG1-associated factor 45a (BAF45a), or XAP135, is a ubiquitously expressed transcriptional regulator that is required for maintaining the undifferentiated status of neuroblasts. It contains a SAY (supporter of activation of yellow) domain and two adjacent plant homeodomain (PHD) fingers. This model corresponds to the second PHD finger
TCTKCGDPHDEDKMMFCDQCDRGYHTFCVGLRSIPDGRWICPLC
>gnl|CDD|277005 cd15530, PHD2_d4, PHD finger 2 found in d4 gene family proteins. The family includes proteins coded by three members of the d4 gene family, DPF1 (neuro-d4), DPF2 (ubi-d4/Requiem), and DPF3 (cer-d4), which function as transcription factors and are involved in transcriptional regulation of genes by changing the condensed/decondensed state of chromatin in the nucleus. DPF2 is ubiquitously expressed and it acts as a transcription factor that may participate in developmentally programmed cell death. DPF1 and DPF3 are expressed predominantly in neural tissues, and they may be involved in the transcription regulation of neuro-specific gene clusters. The d4 family proteins show distinct domain organization with domain 2/3 in the N-terminal region, a Cys2His2 (C2H2) zinc finger or Kruppel-type zinc finger in the central part and two adjacent plant homeodomain (PHD) fingers (d4-domain) in the C-terminal part of the molecule. This model corresponds to the second PHD finger
SCSLCGTSENDDQLLFCDDCDRGYHMYCLSPPMSEPPEGSWSCHLC
>gnl|CDD|277006 cd15531, PHD1_CHD_II, PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins. Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the first PHD finger
YCEVCQQGGEIILCDTCPRAYHLVCLDPELEKAPEGKWSCPHC
>gnl|CDD|277007 cd15532, PHD2_CHD_II, PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins. Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the second PHD finger
FCRVCKDGGELLCCDGCPSSYHLHCLNPPLAEIPDGDWFCPRC
>gnl|CDD|277008 cd15533, PHD1_PHF12, PHD finger 1 found in PHD finger protein 12 (PHF12). PHF12, also termed PHD factor 1 (Pf1), is a plant homeodomain (PHD) zinc finger-containing protein that bridges the transducin-like enhancer of split (TLE) corepressor to the mSin3A-histone deacetylase (HDAC)-complex, and further represses transcription at targeted genes. PHF12 also interacts with MRG15 (mortality factor-related genes on chromosome 15), a member of the mortality factor (MORF) family of proteins implicated in regulating cellular senescence. PHF12 contains two plant-homeodomain (PHD) zinc fingers followed by a polybasic region. The PHD fingers function downstream of phosphoinositide signaling triggered by the interaction between polybasic regions and phosphoinositides. This model corresponds to the first PHD finger
YCDSCGEGGDLLCCDRCPASFHLQCCNPPLDEEDLPPGEWLCHRC
>gnl|CDD|277009 cd15534, PHD2_PHF12_Rco1, PHD finger 2 found in PHD finger protein 12 (PHF12), yeast Rco1, and similar proteins. PHF12, also termed PHD factor 1 (Pf1), is a plant homeodomain (PHD) zinc finger-containing protein that bridges the transducin-like enhancer of split (TLE) corepressor to the mSin3A-histone deacetylase (HDAC)-complex, and further represses transcription at targeted genes. PHF12 also interacts with MRG15 (mortality factor-related genes on chromosome 15), a member of the mortality factor (MORF) family of proteins implicated in regulating cellular senescence. PHF12 contains two plant homeodomain (PHD) zinc fingers followed by a polybasic region. The PHD fingers function downstream of phosphoinositide signaling triggered by the interaction between polybasic regions and phosphoinositides. This subfamily also includes yeast transcriptional regulatory protein Rco1 and similar proteins. Rco1 is a component of the Rpd3S histone deacetylase complex that plays an important role at actively transcribed genes. Rco1 contains two PHD fingers, which are required for the methylation of histone H3 lysine 36 (H3K36) nucleosome recognition by Rpd3S. This model corresponds to the second PHD finger
VCFKCNRSCRVAPLIQCDYCPLLFHLDCLDPPLTHPPATGRWMCPNH
>gnl|CDD|277010 cd15535, PHD1_Rco1, PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and similar proteins. Rco1 is a component of the Rpd3S histone deacetylase complex that plays an important role at actively transcribed genes. Rco1 contains two plant homeodomain (PHD) fingers, which are required for the methylation of histone H3 lysine 36 (H3K36) nucleosome recognition by Rpd3S. This model corresponds to the first PHD finger
FCSACGGYGSFLCCDGCPRSFHFSCLDPPLEEDNLPDDEWFCNEC
>gnl|CDD|277011 cd15536, PHD_PHRF1, PHD finger found in PHD and RING finger domain-containing protein 1 (PHRF1). PHRF1, also termed KIAA1542, or CTD-binding SR-like protein rA9, is a ubiquitin ligase that induces the ubiquitination of TGIF (TG-interacting factor) at lysine 130. It acts as a tumor suppressor that promotes the transforming growth factor (TGF)-beta cytostatic program through selective release of TGIF-driven promyelocytic leukemia protein (PML) inactivation. PHRF1 contains a plant homeodomain (PHD) finger and a RING finger
YCEVCGRSDREDRLLLCDGCDAGYHMECLTPPLDEVPIEEWFCPEC
>gnl|CDD|277012 cd15537, PHD_BS69, PHD finger found in protein BS69. Protein BS69, also termed zinc finger MYND domain-containing protein 11 (ZMYND11 or ZMY11), is a ubiquitously expressed nuclear protein acting as a transcriptional co-repressor in association with various transcription factors. It was originally identified as an adenovirus 5 E1A-binding protein that inhibits E1A transactivation, as well as c-Myb transcription. It also mediates repression, at least in part, through interaction with the co-repressor N-CoR. Moreover, it interacts with Toll-interleukin 1 receptor domain (TIR)-containing adaptor molecule-1 (TICAM-1, also named TRIF) to facilitate NF-kappaB activation and type I IFN induction. It associates with PIAS1, a SUMO E3 enzyme, and Ubc9, a SUMO E2 enzyme, and plays an inhibitory role in muscle and neuronal differentiation. Moreover, BS69 regulates Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1)/C-terminal activation region 2 (CTAR2)-mediated NF-kappaB activation by interfering with the complex formation between TNFR-associated death domain protein (TRADD) and LMP1/CTAR2. It also cooperates with tumor necrosis factor receptor (TNFR)-associated factor 3 (TRAF3) in the regulation of EBV-derived LMP1/CTAR1-induced NF-kappaB activation. Furthermore, BS69 is involved in the p53-p21Cip1-mediated senescence pathway. BS69 contains a plant homeodomain (PHD) finger, a bromodomain, a proline-tryptophan-tryptophan-proline (PWWP) domain, and a Myeloid translocation protein 8, Nervy and DEAF-1 (MYND) domain
YCFECHAPGEVLPCSGCFRVYHSDCLSEDFRPDSTSHWTCPVC
>gnl|CDD|277013 cd15538, PHD_PRKCBP1, PHD finger found in protein kinase C-binding protein 1 (PRKCBP1). PRKCBP1, also termed cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), or Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor; the RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a plant homeodomain (PHD) finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain
FCWRCHKEGQVLCCSLCPRVYHKKCLKLTSEPDEDWVCPEC
>gnl|CDD|277014 cd15539, PHD1_AIRE, PHD finger 1 found in autoimmune regulator (AIRE). AIRE, also termed autoimmune polyendocrinopathy candidiasis ectodermal dystrophy (APECED) protein, functions as a regulator of gene transcription in the thymus. It is essential for prevention of autoimmunity. AIRE plays a critical role in the induction of central tolerance. It promotes self-tolerance through tissue-specific antigen (TSA) expression. It also acts as an active regulator of chondrocyte differentiation. AIRE contains a homogeneously-staining region (HSR) or caspase-recruitment domain (CARD), a nuclear localization signal (NLS), a SAND (for Sp100, AIRE, nuclear phosphoprotein 41/75 or NucP41/75, and deformed epidermal auto regulatory factor 1 or Deaf1) domain, two plant homeodomain (PHD) fingers, and four LXXLL (where L stands for leucine) motifs. This model corresponds to the first PHD finger that recognizes the unmethylated tail of histone H3 and targets AIRE-dependent genes
ECAVCGDGGELLCCDGCPRAFHLACLVPPLTLIPSGTWRCSSC
>gnl|CDD|277015 cd15540, PHD2_AIRE, PHD finger 2 found in autoimmune regulator (AIRE). AIRE, also termed autoimmune polyendocrinopathy candidiasis ectodermal dystrophy (APECED) protein, functions as a regulator of gene transcription in the thymus. It is essential for prevention of autoimmunity. AIRE plays a critical role in the induction of central tolerance. It promotes self-tolerance through tissue-specific antigen (TSA) expression. It also acts as an active regulator of chondrocyte differentiation. AIRE contains a homogeneously-staining region (HSR) or caspase-recruitment domain (CARD), a nuclear localization signal (NLS), a SAND (for Sp100, AIRE, nuclear phosphoprotein 41/75 or NucP41/75, and deformed epidermal auto regulatory factor 1 or Deaf1) domain, two plant homeodomain (PHD) fingers, and four LXXLL (where L stands for leucine) motifs. This model corresponds to the second PHD finger that may play a critical role in the activation of gene transcription
RCGVCRGGRGDLLRCPQCLQAFHWHCHFPSGSSGGRMRCKSC
>gnl|CDD|277016 cd15541, PHD_TIF1_like, PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar proteins. The TIF1 family of transcriptional cofactors includes TIF1alpha (TRIM24), TIF1beta (TRIM28), TIF1gamma (TRIM33), and TIF1delta (TRIM66), which are characterized by an N-terminal RING-finger B-box coiled-coil (RBCC/TRIM) motif and plant homeodomain (PHD) finger followed by a bromodomain in the C-terminal region. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1alpha, TIF1beta, and TIF1delta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. TIF1alpha and TIF1beta bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. In contrast, TIF1delta appears to lack nuclear receptor- and KRAB-binding activity. Moreover, TIF1delta is specifically involved in heterochromatin-mediated gene silencing during postmeiotic phases of spermatogenesis. TIF1gamma is structurally closely related to TIF1alpha and TIF1beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatinic proteins HP1alpha, beta, and gamma. It cannot bind to nuclear receptors (NRs). This family also includes Sp100/Sp140 family proteins, the nuclear body SP100 and SP140. Sp110 is a leukocyte-specific component of the nuclear body. It may function as a nuclear hormone receptor transcriptional coactivator that may play a role in inducing differentiation of myeloid cells. It is also involved in resisting intracellular pathogens and functions as an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers. SP140 is an interferon inducible nuclear leukocyte-specific protein involved in primary biliary cirrhosis and a risk factor in chronic lymphocytic leukemia. It is also implicated in innate immune response to human immunodeficiency virus type 1 (HIV-1) by binding to the virus viral infectivity factor (Vif) protein. Both Sp110 and Sp140 contain a SAND domain, a plant homeodomain (PHD) finger, and a bromodomain (BRD)
WCAVCQNGGELLCCDKCPRVFHLDCHIPPIPEFPSGEWSCSLC
>gnl|CDD|277017 cd15542, PHD_UBR7, PHD finger found in putative E3 ubiquitin-protein ligase UBR7. UBR7, also termed N-recognin-7, is a UBR box-containing protein that belongs to the E3 ubiquitin ligase family that recognizes N-degrons or structurally related molecules for ubiquitin-dependent proteolysis or related processes through the UBR box motif. In addition to the UBR box, UBR7 also harbors a plant homeodomain (PHD) finger. The biochemical properties of UBR7 remain unclear
YCTCDRPYPDPEDEVEDEMIQCVLCEDWFHGRHLGLTPPEPDPDEFDEMICSGC
>gnl|CDD|277018 cd15543, PHD_RSF1, PHD finger found in Remodeling and spacing factor 1 (Rsf-1). Rsf-1, also termed HBV pX-associated protein 8, or Hepatitis B virus X-associated protein alpha (HBxAPalpha), or p325 subunit of RSF chromatin-remodeling complex, is a novel nuclear protein with histone chaperon function. It is a subunit of an ISWI chromatin remodeling complex, remodeling and spacing factor (RSF), and plays a role in mediating ATPase-dependent chromatin remodeling and conferring tumor aggressiveness in common carcinomas. As an ataxia-telangiectasia mutated (ATM)-dependent chromatin remodeler, Rsf-1 facilitates DNA damage checkpoints and homologous recombination repair. It regulates the mitotic spindle checkpoint and chromosome instability through the association with serine/threonine kinase BubR1 (BubR1) and Hepatitis B virus (HBV) X protein (HBx) in the chromatin fraction during mitosis. It also interacts with cyclin E1 and promotes tumor development. Rsf-1 contains a plant homeodomain (PHD) finger
PCRKCGLSDHPEWILLCDRCDAGYHTACLRPPLMIIPDGNWFCPPC
>gnl|CDD|277019 cd15544, PHD_BAZ1A_like, PHD finger found in bromodomain adjacent to zinc finger domain protein BAZ1A and BAZ1B. BAZ1A, also termed ATP-dependent chromatin-remodeling protein, or ATP-utilizing chromatin assembly and remodeling factor 1 (ACF1), or CHRAC subunit ACF1, or Williams syndrome transcription factor-related chromatin-remodeling factor 180 (WCRF180), or WALp1, is a subunit of the conserved imitation switch (ISWI)-family ATP-dependent chromatin assembly and remodeling factor (ACF)/chromatin accessibility complex (CHRAC) chromatin remodeling complex, which is required for DNA replication through heterochromatin. It alters the remodeling properties of the ATPase motor protein sucrose nonfermenting-2 homolog (SNF2H). Moreover, BAZ1A and its complexes play important roles in DNA double-strand break (DSB) repair. It is essential for averting improper gene expression during spermatogenesis. It also regulates transcriptional repression of vitamin D3 receptor-regulated genes. BAZ1B, also termed Tyrosine-protein kinase BAZ1B, or Williams syndrome transcription factor (WSTF), or Williams-Beuren syndrome chromosomal region 10 protein, Williams-Beuren syndrome chromosomal region 9 protein, or WALp2, is a multifunctional protein implicated in several nuclear processes, including replication, transcription, and the DNA damage response. BAZ1B/WSTF, together with the imitation switch (ISWI) ATPase, forms a WSTF-ISWI chromatin remodeling complex (WICH), which transiently associates with the human inactive X chromosome (Xi) during late S-phase prior to BRCA1 and gamma-H2AX. Moreover, BAZ1B/WSTF, SNF2h, and nuclear myosin 1 (NM1) forms the chromatin remodeling complex B-WICH that is involved in regulating rDNA transcription. Both BAZ1A and BAZ1B contain a WAC motif, a DDT domain, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain
RCKVCRKKGDPDNMILCDGCDKAFHLYCLRPALREVPSGDWFCPAC
>gnl|CDD|277020 cd15545, PHD_BAZ2A_like, PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A) and 2B (BAZ2B). BAZ2A, also termed transcription termination factor I-interacting protein 5 (TTF-I-interacting protein 5, or Tip5), or WALp3, is an epigenetic regulator. It has been implicated in epigenetic rRNA gene silencing, as the large subunit of the SNF2h-containing chromatin-remodeling complex NoRC that induces nucleosome sliding in an ATP- and histone H4 tail-dependent fashion. BAZ2A has also been shown to be broadly overexpressed in prostate cancer, to regulate numerous protein-coding genes and to cooperate with EZH2 (enhancer of zeste homolog 2) to maintain epigenetic silencing at genes repressed in prostate cancer metastasis. Its overexpression is tightly associated with a prostate cancer subtype displaying CpG island methylator phenotype (CIMP) in tumors and with prostate cancer recurrence in patients. BAZ2B, also termed WALp4, is a bromodomain-containing protein whose biological role is still elusive. It shows high sequence similarly with BAZ2A. Both BAZ2A and BAZ2B contain a TAM (TIP5/ARBP/MBD) domain, a DDT domain, four AT-hooks, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain. BAZ2B also harbors an extra Apolipophorin-III like domain in its N-terminal region
SCQICRSGDNEDQLLLCDGCDRGYHTYCFKPKMTNVPEGDWFCPEC
>gnl|CDD|277021 cd15546, PHD_PHF13_like, PHD finger found in PHD finger proteins PHF13 and PHF23. PHF13, also termed survival time-associated PHD finger protein in ovarian cancer 1 (SPOC1), is a novel plant homeodomain (PHD) finger-containing protein that shows strong expression in spermatogonia and ovarian cancer cells, modulates chromatin structure and mitotic chromosome condensation, and is important for proper cell division. It is also required for spermatogonial stem cell differentiation and sustained spermatogenesis. The overexpression of PHF13 associates with unresectable carcinomas and shorter survival in ovarian cancer. PHF23, also termed PHD-containing protein JUNE-1, is a hypothetical protein with a PHD finger. It is encoded by gene PHF23 that acts as a candidate fusion partner for the nucleoporin gene NUP98. The NUP98-PHF23 fusion results from a cryptic translocation t(11;17)(p15;p13) in acute myeloid leukemia (AML)
TCFCGKPFAGRPMIECSECLTWIHLSCAKIRKNNVPEVFICQKC
>gnl|CDD|277022 cd15547, PHD_SHPRH, PHD finger found in E3 ubiquitin-protein ligase SHPRH. SHPRH, also termed SNF2, histone-linker, PHD and RING finger domain-containing helicase, belongs to the SWI2/SNF2 family of ATP-dependent chromatin remodeling enzymes, containing the Cys3HisCys4 RING-finger characteristic of E3 ubiquitin ligases. It plays a key role in the error-free branch of DNA damage tolerance. As functional homologs of Saccharomyces cerevisiae Rad5, SHPRH and its closely-related protein, helicase like transcription factor (HLTF), act as ubiquitin ligases that cooperatively mediate Ubc13-Mms2-dependent polyubiquitination of proliferating cell nuclear antigen (PCNA) and maintain genomic stability. SHPRH contains a SNF2 domain, a H1.5 (linker histone H1 and H5) domain, a plant homeodomain (PHD) finger, a Cys3HisCys4 RING-finger, and a C-terminal helicase domain
ECICGELDEIDNKHRVQCLKCGLWQHAECVNYDEESDKREPYLCPHC
>gnl|CDD|277023 cd15548, PHD_ASH1L, PHD finger found in histone-lysine N-methyltransferase ASH1L. ASH1L, also termed ASH1-like protein, or absent small and homeotic disks protein 1 homolog, or lysine N-methyltransferase 2H, is a protein belonging to the Trithorax family. It methylates Lys36 of histone H3 independently of transcriptional elongation to promote the establishment of Hox gene expression by counteracting Polycomb silencing. It can suppress interleukin-6 (IL-6), and tumor necrosis factor (TNF) production in Toll-like receptor (TLR)-triggered macrophages, and inflammatory autoimmune diseases by inducing the ubiquitin-editing enzyme A20. ASH1L contains an associated with SET domain (AWS), a SET domain, a post-SET domain, a bromodomain, a bromo-adjacent homology domain (BAH), and a plant homeodomain (PHD) finger
IRCICGLYKDEGLMIQCEKCMVWQHCDCMGVNDDVEHYLCEQC
>gnl|CDD|277024 cd15549, PHD_PHF20_like, PHD finger found in PHD finger protein 20 (PHF20) and PHD finger protein 20-like protein 1 (P20L1). PHF20, also termed Glioma-expressed antigen 2, or hepatocellular carcinoma-associated antigen 58, or novel zinc finger protein, or transcription factor TZP (referring to Tudor and zinc finger domain containing protein), is a regulator of NF-kappaB activation by disrupting recruitment of PP2A to p65. It also functions as a transcription factor that binds Akt and plays a role in Akt cell survival/growth signaling. Moreover, it transcriptionally regulates p53. The phosphorylation of PHF20 on Ser291 mediated by protein kinase B (PKB) is essential in tumorigenesis via the regulation of p53 mediated signaling. P20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (Cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. Both PHF20 and PHF20L1 contain an N-terminal MBT domain, two Tudor domains, a plant homeodomain (PHD) finger and the putative DNA-binding domains, AT hook and Cys2His2-type zinc finger
HCICGVNEENGLMIQCELCLCWQHGVCMGIEEEESVPERYVCYVC
>gnl|CDD|277025 cd15550, PHD_MLL5, PHD finger found in mixed lineage leukemia 5 (MLL5). MLL5 is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It contains a single plant homeodomain (PHD) finger followed by a catalytic SET domain. MLL5 can be recruited to E2F1-responsive promoters to stimulate H3K4 trimethylation and transcriptional activation by binding to the cell cycle regulator host cell factor (HCF-1), thereby facilitating the cell cycle G1 to S phase transition. It is also involved in mitotic fidelity and genomic integrity by modulating the stability of the chromosomal passenger complex (CPC) via the interaction with Borealin. Moreover, MLL5 is a component of a complex associated with retinoic acid receptor that requires GlcN Acylation of its SET domain in order to activate its histone lysine methyltransferase activity. It also participates in the camptothecin (CPT)-induced p53 activation. Furthermore, MLL5 indirectly regulates H3K4 methylation, represses cyclin A2 (CycA) expression, and promotes myogenic differentiation
RCICGFEHDDGFMICCDKCSVWQHGDCMGIDRENIPDSYLCEQC
>gnl|CDD|277026 cd15551, PHD_PYGO, PHD finger found in PYGO proteins. The family includes Drosophila melanogaster protein pygopus (dPYGO) and its two homologs, PYGO1 and PYGO2. dPYGO is a fundamental Wnt signaling transcriptional component in Drosophila. PYGO1 is essential for the association with Legless (Lgs)/Bcl9 that acts an adaptor between Pygopus (Pygo) and Arm/beta-catenin. dPYGO and PYGO2 function as context-dependent beta-catenin coactivators, and they bind di- and trimethylated lysine 4 of histone H3 (H3K4me2/3). Moreover, PYGO2 acts as a histone methylation reader, and a chromatin remodeler in a testis-specific and Wnt-unrelated manner. It also mediates chromatin regulation and links Wnt signaling and Notch signaling to suppress the luminal/alveolar differentiation competence of mammary stem and basal cells. PYGO2 also plays a new role in rRNA transcription during cancer cell growth. It regulates mammary tumor initiation and heterogeneity in MMTV-Wnt1 mice. All family members contain a plant homeodomain (PHD) finger
PCGICNNEVNDDDDAILCESSCNKWFHRTCTGLTESAYDLLTSEESAEWVCDSC
>gnl|CDD|277027 cd15552, PHD_PHF3_like, PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, Dido2, and Dido3. PHF3 is a human homolog of yeast protein bypass of Ess1 (Bye1), a nuclear protein with a domain resembling the central domain in the transcription elongation factor TFIIS. It is ubiquitously expressed in normal tissues including brain, but its expression is significantly reduced or lost in glioblastomas. PHF3 contains an N-terminal plant homeodomain (PHD) finger, a central RNA polymerase II (Pol II)-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain. This family also includes Dido gene encoding three alternative splicing variants (Dido1, 2, and 3), which have been implicated in a number of cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. Dido1 is important for maintaining embryonic stem (ES) cells and directly regulates the expression of pluripotency factors. It is the shortest isoform that contains only a highly conserved PHD finger responsible for the binding of histone H3 with a higher affinity for trimethylated lysine4 (H3K4me3). Gene Dido1 is a Bone morphogenetic protein (BMP) target gene and promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. Dido3 is the largest isoform and is ubiquitously expressed in all human tissues. It is dispensable for ES cell self-renewal and pluripotency, but is involved in the maintenance of stem cell genomic stability and tumorigenesis. Dido3 contains a PHD finger, a transcription elongation factor S-II subunit M (TFSIIM) domain, a SPOC module, and a long C-terminal region (CT) of unknown homology
YCICRKPHNNRFMICCDRCEEWFHGDCVGITEAQGKEMEENIEEYVCPKC
>gnl|CDD|277028 cd15553, PHD_Cfp1, PHD finger found in CXXC-type zinc finger protein 1 (Cfp1). Cfp1, also termed CpG-binding protein, or PHD finger and CXXC domain-containing protein 1 (PCCX1), is a specificity factor that binds to unmethylated CpGs and links H3K4me3 with CpG islands (CGIs). It integrates both promoter CpG content and gene activity for accurate trimethylation of histone H3 Lys 4 (H3K4me3) deposition in embryonic stem cells. Moreover, Cfp1 is an essential component of the SETD1 histone H3K4 methyltransferase complex and functions as a critical regulator of histone methylation, cytosine methylation, cellular differentiation, and vertebrate development. Cfp1 contains a plant homeodomain (PHD) finger, a CXXC domain, and a CpG binding protein zinc finger C-terminal domain. Its CXXC domain selectively binds to non-methylated CpG islands, following by a preference for a guanosine nucleotide
YCICRSSDISRFMIGCDNCEEWYHGDCINITEKEAKAIKEWYCQQC
>gnl|CDD|277029 cd15554, PHD_PHF2_like, PHD finger found in PHF2, PHF8 and KDM7. This family includes PHF2, PHF8, KDM7, and similar proteins. PHF2, also termed GRC5, or PHD finger protein 2, is a histone lysine demethylase ubiquitously expressed in various tissues. PHF8, also termed PHD finger protein 8, or KDM7B, is a monomethylated histone H4 lysine 20(H4K20me1) demethylase that transcriptionally regulates many cell cycle genes. It also preferentially acts on H3K9me2 and H3K9me1. PHF8 is modulated by CDC20-containing anaphase-promoting complex (APC (cdc20)) and plays an important role in the G2/M transition. It acts as a critical molecular sensor for mediating retinoic acid (RA) treatment response in RAR alpha-fusion-induced leukemia. Moreover, PHF8 is essential for cytoskeleton dynamics and is associated with X-linked mental retardation. KDM7, also termed JmjC domain-containing histone demethylation protein 1D (JHDM1D), or KIAA1718, is a dual histone demethylase that catalyzes demethylation of monomethylated and dimethylated H3K9 (H3K9me2/me1) and H3K27 (H3K27me2/me1), which functions as an eraser of silencing marks on chromatin during brain development. It also plays a tumor-suppressive role by regulating angiogenesis. All family members contain a plant homeodomain (PHD) finger and a JmjC domain
YCICRQPYDVTRFMIECDVCKDWFHGSCVGVEEHQANDIERYHCPNC
>gnl|CDD|277030 cd15555, PHD_KDM2A_2B, PHD finger found in Lysine-specific demethylase KDM2A, KDM2B, and similar proteins. This family includes KDM2A, KDM2B, and F-box and leucine-rich repeat protein 19 (FBXL19). KDM2A is a ubiquitously expressed histone H3 lysine 36 (H3K36) demethylase that has been implicated in gene silencing, cell cycle, cell growth, and cancer development. KDM2B is a ubiquitously expressed histone H3 lysine 4 (H3K4me2) or histone H3 lysine 36 (H3K36me2) demethylase that functions as a regulator of chemokine expression, cellular morphology, and the metabolome of fibroblasts. Both KDM2A and KDM2B belong to the JmjC-domain-containing histone demethylase family. They consist of two Jumonji C (JmjC) domains, and FBXHA and FBXHB domains. A CXXC zinc-finger domain, followed by a plant homeodomain (PHD) finger, is located within the FBXHA domain, and an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain, is located within the FBXHB domain. FBXL19 belongs to the Skp1-Cullin-F-box (SCF) family of E3 ubiquitin ligases. It mediates ubiquitination and interleukin 33 (IL-33)-induced degradation of ST2L receptor in lung epithelia, blocks IL-33-mediated apoptosis, and prevents endotoxin-induced acute lung injury. FBXL19 consists of FBXHA and FBXHB domains, similar to KDM2A and KDM2B
VCLICGEDGKEDEFETTLMECSICWEIVHPECLKEQGEGGVVNEDLPNSWECPKC
>gnl|CDD|277031 cd15556, PHD_MMD1_like, PHD finger found in Arabidopsis thaliana PHD finger protein MALE MEIOCYTE DEATH 1 (MMD1), PHD finger protein MALE STERILITY 1 (MS1), and similar proteins. MMD1 is a plant homeodomain (PHD) finger protein expressed in male meiocytes. It is encoded by the gene DUET, which is required for male meiotic chromosome organization and progression. MMD1 has been implicated in the regulation of gene expression during meiosis. The mmd1 mutation triggers cell death in male meiocytes. MS1 is a nuclear transcriptional activator that is important for tapetal development and pollen wall biosynthesis. It contains a Leu zipper-like domain and a PHD finger motif, both of which are essential for its function
DCSCGTRDDDGERMIACDVCEVWQHTRCVGIADNEEPPDHFLCRRC
>gnl|CDD|277032 cd15557, PHD_CBP_p300, PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300. This p300/CBP family includes two highly homologous histone acetyltransferases (HATs), CREB-binding protein (CBP) and p300. CBP is also known as KAT3A or CREBBP. It specifically interacts with the phosphorylated form of cyclic adenosine monophosphate-responsive element-binding protein (CREB). p300, also termed as KAT3B, or E1A-associated protein p300 (EP300), is a paralog of CBP. and is involved in E1A function in cell cycle progression and cellular differentiation. Both CBP and p300 are co-activator proteins that have been implicated in cell cycle regulation, apoptosis, embryonic development, cellular differentiation and cancer. They associate with a number of DNA-binding transcription activators as well as general transcription factors (GTFs), thus mediating recruitment of basal transcription machinery to the promoter. They contain a cysteine-histidine rich region, KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain
YCCGQFVECKECGRKWHQICVLHNDEIWPNGFICDNC
>gnl|CDD|277033 cd15558, PHD_Hop1p_like, PHD finger found in Schizosaccharomyces pombe meiosis-specific protein hop1 (Hop1p) and similar proteins. Fission yeast Hop1p, also termed linear element-associated protein hop1, is an S. pombe homolog of the synaptonemal complex (SC)-associated protein Hop1 in Saccharomyces cerevisiae. In contrast to S. cerevisiae, S. pombe forms thin threads, known as linear elements (LinEs), in meiotic nuclei, instead of a canonical synaptonemal complex. LinEs contain Rec10 protein and are evolutionary relics of SC axial elements. Fission yeast Hop1p is a linear element (LinE)-associated protein. It also associates with Rec10, which plays a role in recruiting the recombination machinery to chromatin. Hop1p contains an N-terminal HORMA (for Hop1p, Rev7p, and MAD2) domain and a C-terminal plant homeodomain (PHD) finger
RCECGDWGEDGAMIQCAFCDTWQHLLCYGFESAKDPRIPDIHVCYRC
>gnl|CDD|277034 cd15559, PHD1_BPTF, PHD finger 1 found in bromodomain and PHD finger-containing transcription factor (BPTF). BPTF, also termed nucleosome-remodeling factor subunit BPTF, or fetal Alz-50 clone 1 protein (FAC1), or fetal Alzheimer antigen, functions as a transcriptional regulator that exhibits altered expression and subcellular localization during neuronal development and neurodegenerative diseases such as Alzheimer's disease. It interacts with the human orthologue of the Kelch-like Ech-associated protein (Keap1). Its function and subcellular localization can be regulated by Keap1. Moreover, BPTF is a novel DNA-binding protein that recognizes the DNA sequence CACAACAC and represses transcription through this site in a phosphorylation-dependent manner. Furthermore, BPTF interacts with the Myc-associated zinc finger protein (ZF87/MAZ) and alters its transcriptional activity, which has been implicated in gene regulation in neurodegeneration. Some family members contain two or three plant homeodomain (PHD) fingers, which may be involved in complex formation with histone H3 trimethylated at K4 (H3K4me3). This family corresponds to the first PHD finger
HCRVCHKLGDLLCCETCSAVYHLECVDPPLEEVPEEDWQCEVC
>gnl|CDD|277035 cd15560, PHD2_3_BPTF, PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF). BPTF, also termed nucleosome-remodeling factor subunit BPTF, or fetal Alz-50 clone 1 protein (FAC1), or fetal Alzheimer antigen, functions as a transcriptional regulator that exhibits altered expression and subcellular localization during neuronal development and neurodegenerative diseases such as Alzheimer's disease. It interacts with the human orthologue of the Kelch-like Ech-associated protein (Keap1). Its function and subcellular localization can be regulated by Keap1. Moreover, BPTF is a novel DNA-binding protein that recognizes the DNA sequence CACAACAC and represses transcription through this site in a phosphorylation-dependent manner. Furthermore, BPTF interacts with the Myc-associated zinc finger protein (ZF87/MAZ) and alters its transcriptional activity, which has been implicated in gene regulation in neurodegeneration. Some family members contain two or three plant homeodomain (PHD) fingers, which may be involved in complex formation with histone H3 trimethylated at K4 (H3K4me3). This family corresponds to the second and third PHD fingers
YCICRTPYDESQFYIGCDRCQDWFHGRCVGILQSEAEKIDEYVCPQC
>gnl|CDD|277036 cd15561, PHD1_PHF14, PHD finger 1 found in PHD finger protein 14 (PHF14) and similar proteins. PHF14 is a novel nuclear transcription factor that controls the proliferation of mesenchymal cells by directly repressing platelet-derived growth factor receptor-alpha (PDGFRalpha) expression. It also acts as an epigenetic regulator and plays an important role in the development of multiple organs in mammals. PHF14 contains three canonical plant homeodomain (PHD) fingers and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His. It can interact with histones through its PHD fingers. The model corresponds to the first PHD finger
ICCVCLGDRSNDADEIIECDKCGISVHEGCYGVIDESDSSSSASSSSTEPWFCEPC
>gnl|CDD|277037 cd15562, PHD2_PHF14, PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins. PHF14 is a novel nuclear transcription factor that controls the proliferation of mesenchymal cells by directly repressing platelet-derived growth factor receptor-alpha (PDGFRalpha) expression. It also acts as an epigenetic regulator and plays an important role in the development of multiple organs in mammals. PHF14 contains three canonical plant homeodomain (PHD) fingers and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His. It can interact with histones through its PHD fingers. The model corresponds to the second PHD finger
SCGICKKSNDQHLLALCDTCKLYYHLGCLDPPLTRMPKKTKNSGWQCSEC
>gnl|CDD|277038 cd15563, PHD3_PHF14, PHD finger 3 found in PHD finger protein 14 (PHF14) and similar proteins. PHF14 is a novel nuclear transcription factor that controls the proliferation of mesenchymal cells by directly repressing platelet-derived growth factor receptor-alpha (PDGFRalpha) expression. It also acts as an epigenetic regulator and plays an important role in the development of multiple organs in mammals. PHF14 contains three canonical plant homeodomain (PHD) fingers and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His. It can interact with histones through its PHD fingers. The model corresponds to the third PHD finger
ECCVCKQTGDNSQLVRCDECKLCYHFGCLDPPLKKSPKQRGYGWVCEEC
>gnl|CDD|277039 cd15564, PHD1_NSD, PHD finger 1 found in nuclear receptor-binding SET domain-containing (NSD) proteins. The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the first PHD finger
VCQICEKPGKLLTCEGPCCGHFHLDCLGLSEQPDEPFKCDECT
>gnl|CDD|277040 cd15565, PHD2_NSD, PHD finger 2 found in nuclear receptor-binding SET domain-containing (NSD) proteins. The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the second PHD finger
SCFVCKKLGSVGGEVFKCSVASCGKFYHEECLKKWPLTTISDSKKFRCPLH
>gnl|CDD|277041 cd15566, PHD3_NSD, PHD finger 3 found in nuclear receptor-binding SET domain-containing (NSD) proteins. The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the third PHD finger
TCATCEASGDGSSGKLVRCIRCPRAYHAGCIPAGSKLLNKKLIICPKH
>gnl|CDD|277042 cd15567, PHD4_NSD, PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins. The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the fourth PHD finger
WCFICSEGGSLICCESCPASFHPECLGLEPPPEGKFYCEDC
>gnl|CDD|277043 cd15568, PHD5_NSD, PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins. The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the fifth PHD finger
ECFRCGDGGDLVLCDFKGCPKVYHLSCLGLEKPPGGKWICPWH
>gnl|CDD|277044 cd15569, PHD_RAG2, PHD finger found in V(D)J recombination-activating protein 2 (RAG-2) and similar proteins. RAG-2 is an essential component of the lymphoid-specific recombination activating gene RAG1/2 V(D)J recombinase mediating antigen-receptor gene assembly. It contains an acidic hinge region implicated in histone-binding, a non-canonical plant homeodomain (PHD) finger followed by a C-terminal extension of 40 amino acids that is essential for phosphoinositide (PtdIns)-binding. The PHD finger is a chromatin-binding module that specifically recognizes histone H3 trimethylated at lysine 4 (H3K4me3) and influences V(D)J recombination
YWIKCCPSCDVDINTWVPFYSTELNKPAMIFCSHGGGHWVHAQCMDLSESMLLQLSQGNNKYFCNEH
>gnl|CDD|277045 cd15570, PHD_Bye1p_SIZ1_like, PHD domain found in Saccharomyces cerevisiae bypass of ESS1 protein 1 (Bye1p), the E3 Sumo Ligase SIZ1, and similar proteins. Yeast Bye1p is a nuclear transcription factor with a domain resembling the central domain in the transcription elongation factor TFIIS and plays an inhibitory role during transcription elongation. It functions as a multicopy suppressor of Ess1, a peptidyl-prolyl cis-trans isomerase involved in proline isomerization of the C-terminal domain (CTD) of RNA polymerase II (Pol II). Bye1p contains an N-terminal plant homeodomain (PHD) finger, a central Pol II-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain. The PHD domain binds to a histone H3 tail peptide containing trimethylated lysine 4 (H3K4me3). The TLD domain is responsible for the association with chromatin. Plant SIZ1 protein is a SUMO (small ubiquitin-related modifier) E3 ligase that facilitates conjugation of SUMO to substrate target proteins (sumoylation) and belongs to the protein inhibitor of activated STAT (PIAS) protein family. It negatively regulates abscisic acid (ABA) signaling, which is dependent on the bZIP transcripton factor ABI5. It also modulates plant growth and plays a role in drought stress response likely through the regulation of gene expression. SIZ1 functions as a floral repressor that not only represses the salicylic acid (SA)-dependent pathway, but also promotes FLOWERING LOCUS C (FLC) expression by repressing FLOWERING LOCUS D (FLD) activity through sumoylation. SIZ1 contains a PHD finger, which specifically binds methylated histone H3 at lysine 4 and arginine 2
RCPCGSSMEDGSMIQCEGCKTWQHMDCVLIPDKPADGLPELPSKFYCELC
>gnl|CDD|277046 cd15571, ePHD, Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His. PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. The extended PHD finger is characterized as Cys2HisCys5HisCys2His, which has been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors
CALCPRSGGALKGGGALKTTSDGLWVHVVCALWSPEVYFDDGTLLEVEGVSKIPKRRKKLKCSICGKRGG
ACIQCSYPGCPRSFHVSCAIRAGCLFEFEDGPGNFVVYCPKH
>gnl|CDD|277047 cd15572, PHD_BRPF, PHD finger found in bromodomain and PHD finger-containing (BRPF) proteins. The family of BRPF proteins includes BRPF1, BRD1/BRPF2, and BRPF3. They are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a canonical Cys4HisCys3 plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. PHD and ePHD fingers both bind to lysine 4 of histone H3 (K4H3), bromodomains interact with acetylated lysines on N-terminal tails of histones and other proteins, and PWWP domains show histone-binding and chromatin association properties. This model corresponds to the canonical Cys4HisCys3 PHD finger
DAVCCICLDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRRCLQSPSR
>gnl|CDD|277048 cd15573, PHD_JADE, PHD finger found in proteins Jade-1, Jade-2, Jade-3, and similar proteins. This family includes proteins Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16), each of which is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. This family also contains Drosophila melanogaster PHD finger protein rhinoceros (RNO). It is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating transcription of key EGFR/Ras pathway regulators in the Drosophila eye. All Jade proteins contain a canonical Cys4HisCys3 PHD finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger
VCDVCRSPDSEEGNEMVFCDKCNICVHQACYGIQKIPEGSWLCRTC
>gnl|CDD|277049 cd15574, PHD_AF10_AF17, PHD finger found in protein AF-10 and AF-17. This family includes protein AF-10 and AF-17. AF-10, also termed ALL1 (acute lymphoblastic leukemia)-fused gene from chromosome 10 protein, is a transcription factor encoded by gene AF10, a translocation partner of the MLL (mixed-lineage leukemia) oncogene in leukemia. AF-10 has been implicated in the development of leukemia following chromosomal rearrangements between the AF10 gene and one of at least two other genes, MLL and CALM. It plays a key role in the survival of uncommitted hematopoietic cells. Moreover, AF-10 functions as a follistatin-related gene (FLRG)-interacting protein. The interaction with FLRG enhances AF10-dependent transcription. It interacts with the human counterpart of the yeast Dot1, hDOT1L, and may act as a bridge for the recruitment of hDOT1L to the genes targeted by MLL-AF10. It also interacts with the synovial sarcoma associated SYT protein and may play a role in synovial sarcomas and acute leukemias. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is encoded by gene AF17 that has been identified in hematological malignancies as translocation partners of the mixed lineage leukemia gene MLL. It is a putative transcription factor that may play a role in multiple signaling pathways. It is involved in chromatin-mediated gene regulation mechanisms. It functions as a component of the multi-subunit Dot1 complex (Dotcom) and plays a role in the Wnt/Wingless signaling pathway. It also seems to be a downstream target of the beta-catenin/T-cell factor pathway, and participates in G2-M progression. Moreover, it may function as an important regulator of ENaC-mediated Na+ transport and thus blood pressure. Both AF-10 and AF-17 contain an N-terminal canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His. The PHD finger is involved in their homo-oligomerization. In the C-terminal region, they possess a leucine zipper domain and a glutamine-rich region. This family also includes ZFP-1, the Caenorhabditis elegans AF10 homolog. It was originally identified as a factor promoting RNAi interference in C. elegans. It also acts as a Dot1-interacting protein that opposes H2B ubiquitination to reduce polymerase II (Pol II) transcription. This model corresponds to the canonical Cys4HisCys3 PHD finger
GCCVCSDERGWAENPLVYCDGHGCNVAVHQACYGIVQVPTGPWFCRKC
>gnl|CDD|277050 cd15575, PHD_JMJD2A, PHD finger found in Jumonji domain-containing protein 2A (JMJD2A). JMJD2A, also termed lysine-specific demethylase 4A (KDM4A), or JmjC domain-containing histone demethylation protein 3A (JHDM3A), catalyzes the demethylation of di- and trimethylated H3K9 and H3K36. It is involved in carcinogenesis and functions as a transcription regulator that may either stimulate or repress gene transcription. It associates with nuclear receptor co-repressor complex or histone deacetylases. Moreover, JMJD2A forms complexes with both the androgen and estrogen receptor (ER) and plays an essential role in growth of both ER-positive and -negative breast tumors. It is also involved in prostate, colon, and lung cancer progression. JMJD2A contains jmjN and jmjC domains in the N-terminal region, followed by a canonical Cys4HisCys3 PHD finger, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a Tudor domain. This model corresponds to the canonical Cys4HisCys3 PHD finger
HCAVCMLFQTYQVDCWGGHNSSSGVAASEARIKKKTKPLIPEMCFTSTGCNTDLNLSTPYLEEDGTSILV
TCKKCCVCVHASCYGVSPEKAAEDWMCSRC
>gnl|CDD|277051 cd15576, PHD_JMJD2B, PHD finger found in Jumonji domain-containing protein 2B (JMJD2B). JMJD2B, also termed lysine-specific demethylase 4B (KDM4B), or JmjC domain-containing histone demethylation protein 3B (JHDM3B), specifically antagonizes the trimethyl group from H3K9 in pericentric heterochromatin and reduces H3K36 methylation in mammalian cells. It plays an essential role in the growth regulation of cancer cells by modulating the G1-S transition and promotes cell-cycle progression through the regulation of cyclin-dependent kinase 6 (CDK6). It interacts with heat shock protein 90 (Hsp90) and its stability can be regulated by Hsp90. JMJD2B also functions as a direct transcriptional target of p53, which induces its expression through promoter binding. Moreover, JMJD2B expression can be controlled by hypoxia-inducible factor 1alpha (HIF1alpha) in colorectal cancer and estrogen receptor alpha (ERalpha) in breast cancer. It is also involved in bladder, lung, and gastric cancer. JMJD2B contains jmjN and jmjC domains in the N-terminal region, followed by a canonical Cys4HisCys3 PHD finger, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a Tudor domain. This model corresponds to the canonical Cys4HisCys3 PHD finger
YCAICTLFYPYTQSLQDPKEISDMSGLVSKVGQKTRPLIPEMCFTAGGENTEPLPSNSYIGDDGTSVLLS
CAKCCLQVHASCYGVNPDLVNEGWTCSRC
>gnl|CDD|277052 cd15577, PHD_JMJD2C, PHD finger found in Jumonji domain-containing protein 2C (JMJD2C). JMJD2C, also termed lysine-specific demethylase 4C (KDM4C), or gene amplified in squamous cell carcinoma 1 protein (GASC-1 protein), or JmjC domain-containing histone demethylation protein 3C (JHDM3C), is an epigenetic factor that catalyzes the demethylation of di- and trimethylated H3K9 and H3K36, and may be involved in the development and/or progression of various types of cancer including esophageal squamous cell carcinoma (ESC) and breast cancer. It selectively interacts with hypoxia-inducible factor 1alpha (HIF1alpha) and plays a role in breast cancer progression. Moreover, JMJD2C may play an important role in the treatment of obesity and its complications through modulating the regulation of adipogenesis by nuclear receptor peroxisome proliferator-activated receptor gamma (PPARgamma). JMJD2C contains jmjN and jmjC domains in the N-terminal region, followed by a canonical Cys4HisCys3 plant homeodomain (PHD) finger, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a Tudor domain. This model corresponds to the canonical Cys4HisCys3 PHD finger
HCAICTLFMPYYKPDALNEENSAQWEMELPAAPCISMRKTKPLIPEMCFIYREENCEPSPPNALLQEDGT
SLLISCAKCCVQVHASCYGVPSHEIHDGWLCARC
>gnl|CDD|277053 cd15578, PHD1_MTF2, PHD finger 1 found in metal-response element-binding transcription factor 2 (MTF2). MTF2, also termed metal regulatory transcription factor 2, or metal-response element DNA-binding protein M96, or polycomb-like protein 2 (PCL2), complexes with the polycomb repressive complex-2 (PRC2) in embryonic stem cells and regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation. It recruits the PRC2 complex to the inactive X chromosome and target loci in embryonic stem cells. Moreover, MTF2 is required for PRC2-mediated Hox cluster repression. It activates the Cdkn2a gene and promotes cellular senescence, thus suppressing the catalytic activity of PRC2 locally. MTF2 consists of an N-terminal Tudor domain followed by two PHD fingers, and a C-terminal MTF2 domain. This model corresponds to the first PHD finger
VCTVCQDGSSESPNEIVLCDKCGQGYHQLCHNPKIDSSVLDPDVPWLCRQCVF
>gnl|CDD|277054 cd15579, PHD1_PHF19, PHD finger 1 found in PHD finger protein 19 (PHF19). PHF19, also termed Polycomb-like protein 3 (PCL3), is a component of the polycomb repressive complex 2 (PRC2), which is the major H3K27 methyltransferase that regulates pluripotency, differentiation, and tumorigenesis through catalysis of histone H3 lysine 27 trimethylation (H3K27me3) on chromatin. PHF19 consists of an N-terminal Tudor domain followed by two PHD fingers, and a C-terminal MTF2 domain. It binds trimethylated histone H3 Lys36 (H3K36me3) through its Tudor domain and recruits the PRC2 complex and the H3K36me3 demethylase NO66 to embryonic stem cell genes during differentiation. Moreover, PHF19 and its upstream regulator, Akt, play roles in the phenotype switch of melanoma cells from proliferative to invasive states. This model corresponds to the first PHD finger
KCNVCLGKSSGPLNEILICGKCGLGYHQQCHIPVVDSSDDPPLTPWFCRRCIF
>gnl|CDD|277055 cd15580, PHD2_MTF2, PHD finger 2 found in metal-response element-binding transcription factor 2 (MTF2). MTF2, also termed metal regulatory transcription factor 2, or metal-response element DNA-binding protein M96, or Polycomb-like protein 2 (PCL2), complexes with the Polycomb repressive complex-2 (PRC2) in embryonic stem cells and regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation. It recruits the PRC2 complex to the inactive X chromosome and target loci in embryonic stem cells. Moreover, MTF2 is required for PRC2-mediated Hox cluster repression. It activates the Cdkn2a gene and promotes cellular senescence, thus suppressing the catalytic activity of PRC2 locally. MTF2 consists of an N-terminal Tudor domain followed by two plant homeodomain (PHD) fingers, and a C-terminal MTF2 domain. This model corresponds to the second PHD finger
YCYCGGPGDWYLKMLQCCKCKQWFHEACVQCLEKPMLFGDRFYTFICSVCNS
>gnl|CDD|277056 cd15581, PHD2_PHF19, PHD finger 2 found in PHD finger protein 19 (PHF19). PHF19, also termed Polycomb-like protein 3 (PCL3), is a component of the Polycomb repressive complex 2 (PRC2), which is the major H3K27 methyltransferase that regulates pluripotency, differentiation, and tumorigenesis through catalysis of histone H3 lysine 27 trimethylation (H3K27me3) on chromatin. PHF19 consists of an N-terminal Tudor domain followed by two plant homeodomain (PHD) fingers, and a C-terminal MTF2 domain. It binds H3K36me3 through its Tudor domain and recruits the PRC2 complex and the H3K36me3 demethylase NO66 to embryonic stem cell genes during differentiation. Moreover, PHF19 and its upstream regulator, Akt, play roles in the phenotype switch of melanoma cells from proliferative to invasive states. This model corresponds to the second PHD finger
YCYCGGPGEWYLKMLQCYRCRQWFHEACTQCLNDPMMFGDRFYLFFCAVCNQ
>gnl|CDD|277057 cd15582, PHD2_PHF1, PHD finger 2 found in PHD finger protein1 (PHF1). PHF1, also termed Polycomb-like protein 1 (PCL1), together with JARID2 and AEBP2, associates with the Polycomb repressive complex 2 (PRC2), which is the major H3K27 methyltransferase that regulates pluripotency, differentiation, and tumorigenesis through catalysis of histone H3 lysine 27 trimethylation (H3K27me3) on chromatin. PHF1 is essential in epigenetic regulation and genome maintenance. It acts as a dual reader of Lysine trimethylation at Lysine 36 of Histone H3 and Lysine 27 of Histone variant H3t. PHF1 consists of an N-terminal Tudor domain followed by two plant homeodomain (PHD) fingers, and a C-terminal MTF2 domain. Its Tudor domain selectively binds to histone H3K36me3. Moreover, PHF1 is required for efficient H3K27me3 and Hox gene silencing. It can mediate deposition of the repressive H3K27me3 mark and acts as a cofactor in early DNA-damage response. This model corresponds to the second PHD finger
YCYCGGPGEWNLKMLQCCSCLQWFHEACTQCLSKPLLYGDRFYVFECSVCTG
>gnl|CDD|277058 cd15583, PHD_ash2p_like, PHD finger found in Schizosaccharomyces pombe Set1 complex component ash2 (spAsh2p) and similar proteins. spAsh2p, also termed Set1C component ash2, or COMPASS component ash2, or complex proteins associated with set1 protein ash2, or Lid2 complex component ash2, or Lid2C component ash2, is orthologous to Drosophila melanogaster Ash2 protein. Both spAsh2p and D. melanogaster Ash2 contain a plant homeodomain (PHD) finger and a SPRY domain. In contrast, its counterpart in Saccharomyces cerevisiae, Bre2p, has no PHD finger and is not included in this family. spAsh2p shows histone H3 Lys4 (H3K4) methyltransferase activity through its PHD finger. It also interacts with Lid2p in S. pombe. Human Ash2L contains an atypical PHD finger that lacks part of the Cys4HisCys3 signature characteristic of PHD fingers, it binds to only one zinc ion through the second half of the motif and does not have histone tail binding activity
YCYCGKDRNLGEVELQCSICLKWFHAKCVSIDNGSCLPFMTNYQFVCKRC
>gnl|CDD|277059 cd15584, PHD_ING1_2, PHD finger found in inhibitor of growth protein 1 (ING1) and 2 (ING2). ING1 is an epigenetic regulator and a type II tumor suppressor that impacts cell growth, aging, apoptosis, and DNA repair, by affecting chromatin conformation and gene expression. It acts as a reader of the active chromatin mark, the trimethylation of histone H3 lysine 4 (H3K4me3). It binds and directs Growth arrest and DNA damage inducible protein 45 a (Gadd45a) to target sites, thus linking the histone code with DNA demethylation. It interacts with the proliferating cell nuclear antigen (PCNA) via the PCNA-interacting protein (PIP) domain in a UV-inducible manner. It also interacts with a PCNA-interacting protein, p15 (PAF). Moreover, ING1 associates with members of the 14-3-3 family, which is necessary for cytoplasmic relocalization. Endogenous ING1 protein specifically interacts with the pro-apoptotic BCL2 family member BAX and colocalizes with BAX in a UV-inducible manner. It stabilizes the p53 tumor suppressor by inhibiting polyubiquitination of multi-monoubiquitinated forms via interaction with and colocalization of the herpesvirus-associated ubiquitin-specific protease (HAUSP)-deubiquitinase with p53. It is also involved in trichostatin A-induced apoptosis and caspase 3 signaling in p53-deficient glioblastoma cells. In addition, tyrosine kinase Src can bind and phosphorylate ING1 and further regulates its activity. ING2, also termed inhibitor of growth 1-like protein (ING1Lp), or p32, or p33ING2, belongs to the inhibitor of growth (ING) family of type II tumor suppressors. It is a core component of a multi-factor chromatin-modifying complex containing the transcriptional co-repressor SIN3A and histone deacetylase 1 (HDAC1). It has been implicated in the control of cell cycle, in genome stability, and in muscle differentiation. ING2 independently interacts with H3K4me3 (Histone H3 trimethylated on lysine 4) and PtdIns(5)P, and modulates crosstalk between lysine methylation and lysine acetylation on histone proteins through association with chromatin in the presence of DNA damage. It collaborates with SnoN to mediate transforming growth factor (TGF)-beta-induced Smad-dependent transcription and cellular responses. It is upregulated in colon cancer and increases invasion by enhanced MMP13 expression. It also acts as a cofactor of p300 for p53 acetylation and plays a positive regulatory role during p53-mediated replicative senescence. Both ING1 and ING2 contain an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger
YCLCNQVSYGEMIGCDNDECPIEWFHFSCVGLTHKPKGKWYCPKC
>gnl|CDD|277060 cd15585, PHD_ING3, PHD finger found in inhibitor of growth protein 3 (ING3) and similar proteins. ING3, also termed p47ING3, is one member of the inhibitor of growth (ING) family of type II tumor suppressors. It is ubiquitously expressed and has been implicated in transcription modulation, cell cycle control, and the induction of apoptosis. It is an important subunit of human NuA4 histone acetyltransferase complex, which regulates the acetylation of histones H2A and H4. Moreover, ING3 promotes ultraviolet (UV)-induced apoptosis through the Fas/caspase-8-dependent pathway in melanoma cells. It physically interacts with subunits of E3 ligase Skp1-Cullin-F-boxprotein complex (SCF complex) and is degraded by the SCF (F-box protein S-phase kinase-associated protein 2, Skp2)-mediated ubiquitin-proteasome system. It also acts as a suppression factor during tumorigenesis and progression of hepatocellular carcinoma (HCC). ING3 contains an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger
YCICNQVSYGEMVGCDNDDCPIEWFHYGCVGLTEAPKGKWYCPQC
>gnl|CDD|277061 cd15586, PHD_ING4_5, PHD finger found in inhibitor of growth protein 4 (ING4) and 5 (ING5). ING4, also termed p29ING4, and ING5, also termed p28ING5, belong to the inhibitor of growth (ING) family of type II tumor suppressors. ING4 acts as an E3 ubiquitin ligase to induce ubiquitination of the p65 subunit of NF-kappaB and inhibit the transactivation of NF-kappaB target genes. It also induces apoptosis through a p53 dependent pathway, including increasing p53 acetylation, inhibiting Mdm2-mediated degradation of p53 and enhancing the expression of p53 responsive genes both at the transcriptional and post-translational levels. Moreover, ING4 can inhibit the translation of proto-oncogene MYC by interacting with AUF1. It also regulates other transcription factors, such as hypoxia-inducible factor (HIF). ING5 is a Tip60 cofactor that acetylates p53 at K120 and subsequently activates the expression of p53-dependent apoptotic genes in response to DNA damage. Aberrant ING5 expression may contribute to pathogenesis, growth, and invasion of gastric carcinomas and colorectal cancer. ING5 can physically interact with p300 and p53 in vivo, and its overexpression induces apoptosis in colorectal cancer cells. It also associates with cyclin A1 (INCA1) and functions as a growth suppressor with suppressed expression in Acute Myeloid Leukemia (AML). Moreover, ING5 translocation from the nucleus to the cytoplasm might be a critical event for carcinogenesis and tumor progression in human head and neck squamous cell carcinoma. Both ING4 and ING5 contain an N-terminal ING histone-binding domain and a C-terminal plant homeodomain (PHD) finger. They associate with histone acetyltransferase (HAT) complexes containing MOZ (monocytic leukemia zinc finger protein)/MORF (MOZ-related factor) and HBO1, and further direct the MOZ/MORF and HBO1 complexes to chromatin
YCLCHQVSYGEMIGCDNPDCPIEWFHFACVGLTTKPKGKWFCPRC
>gnl|CDD|277062 cd15587, PHD_Yng1p_like, PHD finger found in yeast orthologs of ING tumor suppressor family. The yeast orthologs of the plant homeodomain (PHD) finger-containing ING tumor suppressor family consists of chromatin modification-related protein YNG1 (Yng1p), YNG2 (Yng2p), and transcriptional regulatory protein PHO23 (Pho23p). Yng1p, also termed ING1 homolog 1, is one of the components of the NuA3 histone acetyltransferase (HAT) complex. Its PHD finger binding to H3 Trimethylated at K4 (H3K4me3) promotes NuA3 H3 HAT activity at K14 of H3 on chromatin. Yng2p, also termed ESA1-associated factor 4, or ING1 homolog 2, is a subunit of the NuA4 HAT complex. It plays a critical role in intra-S-phase DNA damage response. Pho23p is part of the Rpd3/Sin3 histone deacetylase (HDAC) complex. It is required for the normal function of Rpd3 in the silencing of rDNA, telomeric, and mating-type loci. Yng1p and Pho23p inhibit p53-dependent transcription. In contrast, Yng2p has the opposite effect. All family members contain an N-terminal ING histone-binding domain and a C-terminal PHD finger
YCYCRRVSFGEMVACDNPDCKIEWFHFECVGLTETPKGKWYCSDCKV
>gnl|CDD|277063 cd15588, PHD1_KMT2A, PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A). KMT2A (also termed ALL-1, CXXC-type zinc finger protein 7, myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (Htrx), or zinc finger protein HRX) is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4 methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, a Bromodomain domain, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the first PHD finger
VCFLCASSGHVEFVYCQVCCEPFHKFCLEEAERPLEDQLENWCCRRC
>gnl|CDD|277064 cd15589, PHD1_KMT2B, PHD finger 1 found in Histone-lysine N-methyltransferase 2B (KMT2B). KMT2B, also termed trithorax homolog 2 or WW domain-binding protein 7 (WBP-7), is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3 lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B plays a critical role in memory formation through mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. KMT2B contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the first PHD finger
VCLLCASKGQHELLFCQVCCEPFHRFCLEESERPLPEQEENWCCRRC
>gnl|CDD|277065 cd15590, PHD2_KMT2A, PHD finger 2 found in histone-lysine N-methyltransferase 2A (KMT2A). KMT2A (also termed ALL-1, CXXC-type zinc finger protein 7, myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (Htrx), or zinc finger protein HRX) is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4 methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, a Bromodomain domain, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the second PHD finger
FCHVCGRQHQATKQLLECNKCRNSYHPECLGPNYPTKPTKKKRVWICTKC
>gnl|CDD|277066 cd15591, PHD2_KMT2B, PHD domain 2 found in Histone-lysine N-methyltransferase 2B (KMT2B). KMT2B, also termed trithorax homolog 2 or WW domain-binding protein 7 (WBP-7), is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B plays a critical role in memory formation through mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. KMT2B contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD), an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the second PHD finger
FCHVCGRKNKESKPLLECERCRNCYHPACLGPNYPKPANRKKRPWICSAC
>gnl|CDD|277067 cd15592, PHD3_KMT2A, PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A). KMT2A (also termed ALL-1, CXXC-type zinc finger protein 7, myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (Htrx), or zinc finger protein HRX) is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4 methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, a Bromodomain domain, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the third PHD finger
FCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCINC
>gnl|CDD|277068 cd15593, PHD3_KMT2B, PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B). KMT2B, also termed trithorax homolog 2 or WW domain-binding protein 7 (WBP-7), is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3 lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B plays a critical role in memory formation through mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. KMT2B contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the third PHD finger
YCPICLKCYEDNDYESKMMQCAKCDHWVHAKCEGLSDELYEILSSLPDSVVYSCAPC
>gnl|CDD|277069 cd15594, PHD2_KMT2C, PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C). KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3) or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains several plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains. This model corresponds to the second PHD finger
VCQTCRQPGDDNKMLVCDTCDKGYHTFCLQPVMTTIPKNGWKCKNC
>gnl|CDD|277070 cd15595, PHD2_KMT2D, PHD finger 2 found in Histone-lysine N-methyltransferase 2D (KMT2D). KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such asHOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the second PHD finger
VCQTCRKPGEDSKMLVCEACDKGYHTFCLKPAMESLPTDSWKCKAC
>gnl|CDD|277071 cd15596, PHD4_KMT2C, PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C). KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3) or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains several plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains. This model corresponds to the fourth PHD finger
KFTLNQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECT
>gnl|CDD|277072 cd15597, PHD3_KMT2D, PHD finger 3 found in Histone-lysine N-methyltransferase 2D (KMT2D). KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the third PHD finger
DMCVVCGSFGRGSEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVECI
>gnl|CDD|277073 cd15600, PHD6_KMT2C, PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C). KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains several plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains. This model corresponds to the sixth PHD finger
TCPICYRNYREEELILQCRQCDRWMHASCQNLNTEEEVENAADNGFDCTMC
>gnl|CDD|277074 cd15601, PHD5_KMT2D, PHD finger 5 found in Histone-lysine N-methyltransferase 2D (KMT2D). KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such asHOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is downregulated in cholestasis. KMT2D contains the catalytic domain SET, five plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the fifth PHD finger
TCPVCRAKYVEEDLLIQCRHCDRWVHAVCESLFTEDEVEQAADEGFDCSSC
>gnl|CDD|277075 cd15602, PHD1_KDM5A, PHD finger 1 found in Lysine-specific demethylase 5A (KDM5A). KDM5A (also termed Histone demethylase JARID1A, Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2)) was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as a trimethylated histone H3 lysine 4 (H3K4me3) demethylase that belongs to the JARID subfamily within the JmjC proteins. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5A contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger
VCLFCGRGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKCVAE
>gnl|CDD|277076 cd15603, PHD1_KDM5B, PHD finger 1 found in lysine-specific demethylase 5B (KDM5B). KDM5B (also termed Cancer/testis antigen 31 (CT31), Histone demethylase JARID1B, Jumonji/ARID domain-containing protein 1B (JARID1B), PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A)) is a member of the JARID subfamily within the JmjC proteins. It has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of pregnant females and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well as TIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. KDM5B contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger
VCLVCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKC
>gnl|CDD|277077 cd15604, PHD1_KDM5C_5D, PHD finger 1 found in Lysine-specific demethylase 5C (KDM5C) and 5D (KDM5D). The family includes KDM5C and KDM5D, both of which belong to the JARID subfamily within the JmjC proteins. KDM5C (also termed Histone demethylase JARID1C, Jumonji/ARID domain-containing protein 1C, SmcX, or Xe169) is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D (also termed Histocompatibility Y antigen (H-Y), Histone demethylase JARID1D, Jumonji/ARID domain-containing protein 1D, or SmcY) is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me3 andH3K4me2), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. Both KDM5C and KDM5D contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as two plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger
VCRMCSRGDEDDKLLLCDGCDDNYHTFCLLPPLPEPPKGIWRCPKC
>gnl|CDD|277078 cd15605, PHD1_Lid_like, PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar proteins. Drosophila melanogaster Lid, also termed Retinoblastoma-binding protein 2 homolog, is identified genetically as a trithorax group (trxG) protein that is a Drosophila homolog of the human protein JARID1A/kdm5A, a member of the JARID subfamily within the JmjC proteins. Lid functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Lid contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger of Lid
VCHTCGRGDGEESMLLCDGCDDSYHTFCLLPPLSEVPKGDWRCPKC
>gnl|CDD|277079 cd15606, PHD2_KDM5A, PHD finger 2 found in Lysine-specific demethylase 5A (KDM5A). KDM5A (also termed Histone demethylase JARID1A, Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2)) was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5A functions as a trimethylated histone H3 lysine 4 (H3K4me3) demethylase that belongs to the JARID subfamily within the JmjC proteins. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5A contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the second PHD finger
YCICRKPFSGFMLQCELCKDWFHSSCVPLPKSSSQKKGGNGSGQGAKELKFLCPLC
>gnl|CDD|277080 cd15607, PHD2_KDM5B, PHD finger 2 found in lysine-specific demethylase 5B (KDM5B). KDM5B (also termed Cancer/testis antigen 31 (CT31), Histone demethylase JARID1B, Jumonji/ARID domain-containing protein 1B (JARID1B), retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), or PLU-1) is a member of the JARID subfamily within the JmjC proteins. It has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well as TIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. KDM5B contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the second PHD finger
VCVCQKAPMAPMIQCELCRDAFHSGCVTAPSDPQGPQAWLCPQC
>gnl|CDD|277081 cd15608, PHD2_KDM5C_5D, PHD finger 2 found in Lysine-specific demethylase 5C (KDM5C) and 5D (KDM5D). The family includes KDM5C and KDM5D, both of which belong to the JARID subfamily within the JmjC proteins. KDM5C (also termed Histone demethylase JARID1C, Jumonji/ARIDdomain-containing protein 1C, SmcX, or Xe169) is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D (also termed Histocompatibility Y antigen (H-Y), Histone demethylase JARID1D, Jumonji/ARID domain-containing protein 1D, or SmcY) is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me3 and H3K4me2), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. Both KDM5C and KDM5D contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as two plant homeodomain (PHD) fingers. This model corresponds to the second PHD finger
VCVCGQPPRPGMLRCHLCQDWFHGGCVSFPRLLSSSGPHSSPSLAWWEWDTRFLCPLC
>gnl|CDD|277082 cd15609, PHD_TCF19, PHD finger found in Transcription factor 19 (TCF-19) and similar proteins. TCF-19, also termed transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3
PCASPSCCLPQDETVSWVQCDDCDQWYHVACVGCDYNAVKDPDADFHCGC
>gnl|CDD|277083 cd15610, PHD3_KDM5A_like, PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A), 5B (KDM5B), and similar proteins. The family includes KDM5A and KDM5B, both of which belong to the JARID subfamily within the JmjC proteins. KDM5A, also termed Histone demethylase JARID1A, or Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2), was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as the trimethylated histone H3 lysine 4 (H3K4me3) demethylase. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5B, also termed Cancer/testis antigen 31 (CT31), or Histone demethylase JARID1B, or Jumonji/ARID domain-containing protein 1B (JARID1B), or PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well asTIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. The family also includes the Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the third PHD finger
SCSAKQCLKPTGDEVNWVQCDGCEEWFHLLCVGLSPEEVAEDEDYICPSC
>gnl|CDD|277084 cd15612, PHD_OBE1_like, PHD finger found in Arabidopsis thaliana protein OBERON 1, OBERON 2, and similar proteins mainly found in plants. Included in this family are OBERON 1 (OBE1, or potyvirus VPg-interacting protein 2) and OBERON 2 (OBE2, or potyvirus VPg-interacting protein 1), which have been involved in the maintenance and/or establishment of the meristems in Arabidopsis. They interact with potyvirus VPg-interacting proteins (PVIP1 and 2) and act as central regulators in auxin-mediated control of development. Both OBE1and OBE2 contain a plant homeodomain (PHD) finger. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins
MCPICSKFDFAVNTCSWIGCDVCSHWTHTDCAIRSGEISMGVSLKGVEGSTEMEFHCRAC
>gnl|CDD|277085 cd15613, PHD_AL_plant, PHD finger found in plant Alfin1-like (AL) proteins. AL proteins are ubiquitously expressed nuclear proteins existing only in plants. They are involved in chromatin regulation by binding to tri- and dimethylated histone H3 at lysine 4 (H3K4me3/2), the active histone markers, through their plant homeodomain (PHD) fingers
QCGSCGGNYTADEFWICCDVCEKWYHGKCVKITPAKAEHIKQYKCPSCSNK
>gnl|CDD|277086 cd15614, PHD_HAC_like, PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar proteins. This family includes A. thaliana HACs (HAC1/2/4/5/12), which are histone acetyltransferases of the p300/CREB-binding protein (CBP) co-activator family. CBP-type HAT proteins are also found in animals, but absent in fungi. The domain architecture of CBP-type HAT proteins differs between plants and animals. Members in this family contain an N-terminal partially conserved KIX domain, a Zf-TAZ domain, a Cysteine rich CBP-type HAT domain that harbors a plant homeodomain (PHD) finger, a Zf-ZZ domain, and a Zf-TAZ domain. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins
WCSPCYNELKGENILIGGVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNGRRNADETAEYVC
PLC
>gnl|CDD|277087 cd15615, PHD_ARID4_like, PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 (ARID4) and similar proteins. This family includes A. thaliana ARID4 (ARID domain-containing protein 4) and similar proteins. Their biological roles remain unclear, but they all contain an AT-rich interactive domain (ARID) and a plant homeodomain (PHD) finger at the C-terminus. ARID is a helix-turn-helix motif-based DNA-binding domain conserved in all eukaryotes. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins
FCILCGQVYEENEGDEKEWVQCDSCSEWVHFECDGRTGLGAFKYAKSDGLQYVCPRC
>gnl|CDD|277088 cd15616, PHD_UHRF1, PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1). UHRF1 (also termed inverted CCAAT box-binding protein of 90 kDa, nuclear protein 95, nuclear zinc finger protein Np95 (Np95), RING finger protein 106, transcription factor ICBP90, or E3 ubiquitin-protein ligase UHRF1) is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumour suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of transcription factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF1 contains an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET and RING finger associated (SRA) domain, and a C-terminal RING-finger domain. It specifically binds to hemimethylated DNA, double-stranded CpG dinucleotides, and recruits the maintenance methyltransferase DNMT1 to its hemimethylated DNA substrate through its SRA domain. UHRF1-dependent H3K23 ubiquitylation has an essential role in maintaining DNA methylation and replication. The tandem Tudor domain directs UHRF1 binding to the heterochromatin mark histone H3K9me3 and the PHD finger targets UHRF1 to unmodified histone H3 in euchromatic regions. The RING-finger domain exhibit both autocatalytic E3 ubiquitin (Ub) ligase activity and activity against histone H3 and DNMT1
ACHVCGGKQDPDKQLMCDECDMAFHIYCLNPPLSSIPDDEDWYCPEC
>gnl|CDD|277089 cd15617, PHD_UHRF2, PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2). UHRF2 (also termed Np95/ICBP90-like RING finger protein (NIRF), Np95-like RING finger protein, nuclear protein 97, nuclear zinc finger protein Np97, RING finger protein 107, or E3 ubiquitin-protein ligase UHRF2) was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs,p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. UHRF2 contains an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal RING finger
SCYVCGGKQDAHMQLLCDECNMAYHIYCLNPPLDKIPEDEDWYCPSC
>gnl|CDD|277090 cd15618, PHD1_MOZ_MORF, PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF). MOZ (also termed histone acetyltransferase KAT6A, YBF2/SAS3, SAS2 and TIP60protein 3 (MYST-3), runt-related transcription factor-binding protein 2, or zinc finger protein 220) is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ-related factor (MORF), also termed MOZ2, or histone acetyltransferase KAT6B, or MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4 (MYST4), is a ubiquitously expressed transcriptional regulator with intrinsic HAT activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. Both MOZ and MORF are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are also implicated in human leukemias. MOZ is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphomagenesis and bone development, and its homologs. MOZ contains a linker histone 1 and histone 5 domains and two plant homeodomain (PHD) fingers. In contrast, MORF contains an N-terminal region containing two PHD fingers, a putative HAT domain, an acidic region, and a C-terminal Ser/Met-rich domain. The model corresponds to the first PHD finger
PIPICSFCLGTAEKNRDGKPEELLSCADCGNSGHPSCLKYSPELTERVKALRWQCIEC
>gnl|CDD|277091 cd15619, PHD1_d4, PHD finger 1 found in d4 gene family proteins. The family includes proteins coded by three members of the d4 gene family, DPF1 (neuro-d4), DPF2 (ubi-d4/Requiem), and DPF3 (cer-d4), which function as transcription factors and are involved in transcriptional regulation of genes by changing the condensed/decondensed state of chromatin in the nucleus. DPF2 is ubiquitously expressed and it acts as a transcription factor that may participate in developmentally programmed cell death. DPF1 and DPF3 are expressed predominantly in neural tissues, and they may be involved in the transcription regulation of neuro-specific gene clusters. The d4 family proteins show distinct domain organization with domain 2/3 in the N-terminal region, a Cys2His2 (C2H2) zinc finger or Kruppel-type zinc finger in the central part and two adjacent plant homeodomain (PHD) fingers (d4-domain) in the C-terminal part of the molecule. This model corresponds to the first PHD finger
YCDFCLGDAKENKKTGQPEELVSCSDCGRSGHPSCLQFTPNMTISVKKYRWQCIEC
>gnl|CDD|277092 cd15622, PHD_TIF1alpha, PHD finger found in transcription intermediary factor 1-alpha (TIF1-alpha). TIF1-alpha, also termed tripartite motif-containing protein 24 (TRIM24), or E3 ubiquitin-protein ligase TRIM24, or RING finger protein 82, belongs to the TRIM/RBCC protein family. It interacts specifically and in a ligand-dependent manner with the ligand binding domain (LBD) of several nuclear receptors (NRs), including retinoid X (RXR), retinoic acid (RAR), vitamin D3 (VDR), estrogen (ER), and progesterone (PR) receptors. It also associates with heterochromatin-associated factors HP1alpha, MOD1 (HP1beta) and MOD2 (HP1gamma), as well as vertebrate Kruppel-type (C2H2) zinc finger proteins that contain transcriptional silencing domain KRAB. TIF1-alpha is a ligand-dependent co-repressor of retinoic acid receptor (RAR) that interacts with multiple nuclear receptors in vitro via an LXXLL motif, and further acts as a gatekeeper of liver carcinogenesis. It also functions as an E3-ubiquitin ligase targeting p53 and is broadly associated with chromatin silencing. Moreover, it is a chromatin regulator that recognizes specific, combinatorial histone modifications through its C-terminal plant homeodomain (PHD)-Bromodomain (Bromo) region. In addition, it interacts with chromatin and estrogen receptor to activate estrogen-dependent genes associated with cellular proliferation and tumor development. TIF1-alpha contains an N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), a plant homeodomain (PHD) finger, followed by a bromodomain in the C-terminal region
WCAVCQNGGELLCCEKCPKVFHLSCHVPTLMNFPSGEWICTFC
>gnl|CDD|277093 cd15623, PHD_TIF1beta, PHD finger found in transcription intermediary factor 1-beta (TIF1-beta). TIF1-beta, also termed Kruppel-associated Box (KRAB)-associated protein 1 (KAP-1), or KRAB-interacting protein 1 (KRIP-1), or nuclear co-repressor KAP-1, or RING finger protein 96, or tripartite motif-containing protein 28 (TRIM28), or E3 SUMO-protein ligase TRIM28, acts as a nuclear co-repressor that plays a role in transcription and in DNA damage response. Upon DNA damage, the phosphorylation of KAP-1 on serine 824 by the ataxia telangiectasia-mutated (ATM) kinase enhances cell survival and facilitates chromatin relaxation and heterochromatic DNA repair. It also regulates CHD3 nucleosome remodeling during DNA double-strand break (DSB) response. Meanwhile, KAP-1 can be dephosphorylated by protein phosphatase PP4C in the DNA damage response. In addition, KAP-1 is a co-activator of the orphan nuclear receptor NGFI-B (or Nur77) and is involved in NGFI-B-dependent transcription. It is also a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase. TIF1-beta contains an N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), which can interact with KRAB zinc finger proteins (KRAB-ZFPs), MDM2, MM1, C/EBPbeta, and mediates homo- and heterodimerization, a plant homeodomain (PHD) finger followed by a bromodomain in the C-terminal region, which interact with SETDB1, Mi-2alpha and other proteins to form complexes with histone deacetylase or methyltransferase activity
CCRVCQKAGALVMCDQCEFCFHLDCHLPALQEVPGEDWKCLLC
>gnl|CDD|277094 cd15624, PHD_TIF1gamma, PHD finger found in transcriptional intermediary factor 1 gamma (TIF1gamma). TIF1gamma, also termed tripartite motif-containing 33 (trim33), or ectodermin, or RFG7, or PTC7, is an E3-ubiquitin ligase that functions as a regulator of transforming growth factor beta (TGFbeta) signaling; it inhibits the Smad4-mediated TGFbeta response by interaction with Smad2/3 or ubiquitylation of Smad4. Moreover, TIF1gamma is an important regulator of transcription during hematopoiesis, as well as a key factor of tumorigenesis. Like other TIF1 family members, TIF1gamma also contains an intrinsic transcriptional silencing function. It can control erythroid cell fate by regulating transcription elongation. It can bind to the anaphase-promoting complex/cyclosome (APC/C) and promotes mitosis. TIF1gamma contains an N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), a plant homeodomain (PHD) finger, followed by a bromodomain in the C-terminal region
WCAVCQNGGDLLCCEKCPKVFHLTCHVPTLLSFPSGDWICTFCRDI
>gnl|CDD|277095 cd15625, PHD_TIF1delta, PHD finger found in transcriptional intermediary factor 1 delta (TIF1delta). TIF1delta, also termed tripartite motif-containing protein 66 (TRIM66), is a novel heterochromatin protein 1 (HP1)-interacting member of the transcriptional intermediary factor1 (TIF1) family expressed by elongating spermatids. Like other TIF1 proteins, TIF1delta displays a potent trichostatin A (TSA)-sensitive repression function; TSA is a specific inhibitor of histone deacetylases. Moreover, TIF1delta plays an important role in heterochromatin-mediated gene silencing during postmeiotic phases of spermatogenesis. It functions as a negative regulator of postmeiotic genes acting through HP1 isotype gamma (HP1gamma) complex formation and centromere association. TIF1delta contains an N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), a plant homeodomain (PHD) finger, followed by a bromodomain in the C-terminal region
NEDFCAVCLNGGELLCCDRCPKVFHLSCHVPALLSFPVGEWVCTLCRNL
>gnl|CDD|277096 cd15626, PHD_SP110_140, PHD finger found in the Sp100/Sp140 family of nuclear body components. The Sp100/Sp140 family includes nuclear body proteins SP100, SP140, and similar proteins. Sp110, also termed interferon-induced protein 41/75, or speckled 110 kDa, or transcriptional coactivator Sp110, is a leukocyte-specific component of the nuclear body. It may function as a nuclear hormone receptor transcriptional coactivator that may play a role in inducing differentiation of myeloid cells. It is also involved in resisting intracellular pathogens and functions as an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers. Sp110 gene polymorphisms may be associated with susceptibility to tuberculosis in Chinese population. Sp110 contains a Sp100-like domain, a SAND domain, a plant homeodomain (PHD) finger, and a bromodomain (BRD). SP140, also termed lymphoid-restricted homolog of Sp100 (LYSp100), or nuclear autoantigen Sp-140, or speckled 140 kDa, is an interferon inducible nuclear leukocyte-specific protein involved in primary biliary cirrhosis and a risk factor in chronic lymphocytic leukemia. It is also implicated in innate immune response to human immunodeficiency virus type 1 (HIV-1) by binding to the virus's viral infectivity factor (Vif) protein. Sp140 contains a nuclear localization signal, a dimerization domain (HSR or CARD domain), a SAND domain, a PHD finger, and a BRD
KCEVCGQEGKLFCCCTCSRVFHEDCHIPPVEAQRSPWSCTFC
>gnl|CDD|277097 cd15627, PHD_BAZ1A, PHD finger found in bromodomain adjacent to zinc finger domain protein 1A (BAZ1A). BAZ1A, also termed ATP-dependent chromatin-remodeling protein, or ATP-utilizing chromatin assembly and remodeling factor 1 (ACF1), or CHRAC subunit ACF1, or Williams syndrome transcription factor-related chromatin-remodeling factor 180 (WCRF180), or WALp1, is a subunit of the conserved imitation switch (ISWI)-family ATP-dependent chromatin assembly and remodeling factor (ACF)/chromatin accessibility complex (CHRAC) chromatin remodeling complex, which is required for DNA replication through heterochromatin. It alters the remodeling properties of the ATPase motor protein sucrose nonfermenting-2 homolog (SNF2H). Moreover, BAZ1A and its complexes play important roles in DNA double-strand break (DSB) repair. It is essential for averting improper gene expression during spermatogenesis. It also regulates transcriptional repression of vitamin D3 receptor-regulated genes. BAZ1A contains a WAC motif, a DDT domain, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain
RCRICRRKGDAEKMLLCDGCDRGHHMYCLRPPLKKVPEGDWFCPDC
>gnl|CDD|277098 cd15628, PHD_BAZ1B, PHD finger found in bromodomain adjacent to zinc finger domain protein 1B (BAZ1B). BAZ1B, also termed Tyrosine-protein kinase BAZ1B, or Williams syndrome transcription factor (WSTF), or Williams-Beuren syndrome chromosomal region 10 protein, Williams-Beuren syndrome chromosomal region 9 protein, or WALp2, is a multifunctional protein implicated in several nuclear processes, including replication, transcription, and the DNA damage response. BAZ1B/WSTF, together with the imitation switch (ISWI) ATPase, forms a WSTF-ISWI chromatin remodeling complex (WICH), which transiently associates with the human inactive X chromosome (Xi) during late S-phase prior to BRCA1 and gamma-H2AX. Moreover, BAZ1B/WSTF, SNF2h, and nuclear myosin 1 (NM1) forms the chromatin remodeling complex B-WICH that is involved in regulating rDNA transcription. BAZ1B contains a WAC motif, a DDT domain, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain
KCKVCRKKGEDDKLILCDECNQAFHLFCLRPALYEVPDGEWMCPAC
>gnl|CDD|277099 cd15629, PHD_BAZ2A, PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A). BAZ2A, also termed transcription termination factor I-interacting protein 5 (TTF-I-interacting protein 5, or Tip5), or WALp3, is an epigenetic regulator. It has been implicated in epigenetic rRNA gene silencing, as the large subunit of the SNF2h-containing chromatin-remodeling complex NoRC that induces nucleosome sliding in an ATP- and histone H4 tail-dependent fashion. BAZ2A has also been shown to be broadly overexpressed in prostate cancer, to regulate numerous protein-coding genes and to cooperate with EZH2 (enhancer of zeste homolog 2) to maintain epigenetic silencing at genes repressed in prostate cancer metastasis. Its overexpression is tightly associated with a prostate cancer subtype displaying CpG island methylator phenotype (CIMP) in tumors and with prostate cancer recurrence in patients. It contains a TAM (TIP5/ARBP/MBD) domain, a DDT domain, four AT-hooks, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain
TCLVCRKGDNDEYLLLCDGCDRGCHMYCHRPKMLQVPEGDWFCPNCV
>gnl|CDD|277100 cd15630, PHD_BAZ2B, PHD finger found in bromodomain adjacent to zinc finger domain protein 2B (BAZ2B). BAZ2B, also termed WALp4, is a bromodomain-containing protein whose biological role is still elusive. It shows high sequence similarly with BAZ2A, which is the large subunit of the SNF2h-containing chromatin-remodeling complex NoRC that induces nucleosome sliding in an ATP-and histone H4 tail-dependent fashion. BAZ2B contains a TAM (TIP5/ARBP/MBD) domain, an Apolipophorin-III like domain, a DDT domain, four AT-hooks, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain
VYCQICRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPEGDWFCPACIA
>gnl|CDD|277101 cd15631, PHD_PHF23, PHD finger found in PHD finger protein 23 (PHF23). PHF23, also termed PHD-containing protein JUNE-1, is a hypothetical protein with a plant homeodomain (PHD) finger. It is encoded by gene PHF23 that acts as a candidate fusion partner for the nucleoporin gene NUP98. The NUP98-PHF23 fusion results from a cryptic translocation t(11;17)(p15;p13) in acute myeloid leukemia (AML)
TCYCGKPFAGRPMIECSQCGTWIHLSCAKIKKSNVPDFFYCQKC
>gnl|CDD|277102 cd15632, PHD_PHF13, PHD finger found in PHD finger protein 13 (PHF13). PHF13, also termed survival time-associated PHD finger protein in ovarian cancer 1 (SPOC1), is a novel plant homeodomain (PHD) finger-containing protein that shows strong expression in spermatogonia and ovarian cancer cells, modulates chromatin structure and mitotic chromosome condensation, and is important for proper cell division. It is also required for spermatogonial stem cell differentiation and sustained spermatogenesis. The overexpression of PHF13 associates with unresectable carcinomas and shorter survival in ovarian cancer
LVTCFCMKPFAGRPMIECNECHTWIHLSCAKIRKSNVPEVYVCQKCR
>gnl|CDD|277103 cd15633, PHD_PHF20L1, PHD finger found in PHD finger protein 20-like protein 1 (P20L1). P20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (Cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. In addition to the MBT domain, PHF20L1 also contains two Tudor domains, a plant homeodomain (PHD) finger and the putative DNA-binding domains, AT hook and Cys2His2-type zinc finger
RCICEMDEENGFMIQCEECLCWQHSVCMGLLEESIPEQYICYICRD
>gnl|CDD|277104 cd15634, PHD_PHF20, PHD finger found in PHD finger protein 20 (PHF20). PHF20, also termed Glioma-expressed antigen 2, or hepatocellular carcinoma-associated antigen 58, or novel zinc finger protein, or transcription factor TZP (referring to Tudor and zinc finger domain containing protein), is a regulator of NF-kappaB activation by disrupting recruitment of PP2A to p65. It also functions as a transcription factor that binds Akt and plays a role in Akt cell survival/growth signaling. Moreover, it transcriptionally regulates p53. The phosphorylation of PHF20 on Ser291 mediated by protein kinase B (PKB) is essential in tumorigenesis via the regulation of p53 mediated signaling. PHF20 contains an N-terminal malignant brain tumor (MBT) domain, two Tudor domains, a plant homeodomain (PHD) finger and the putative DNA-binding domains, AT hook and Cys2His2-type zinc finger
RCICEVQEENDFMIQCEECLCWQHGVCMGLLEDNVPEKYTCYIC
>gnl|CDD|277105 cd15635, PHD_PYGO1, PHD finger found in pygopus homolog 1 (PYGO1). PYGO1 is a homolog of Drosophila melanogaster protein pygopus (dPYGO), which is a fundamental Wnt signaling transcriptional component in Drosophila. It functions as a context-dependent beta-catenin coactivator, and binds di- and trimethylated lysine 4 of histone H3 (H3K4me2/3). PYGO1 is essential for the association with Legless (Lgs)/Bcl9 that acts as an adaptor between Pygopus (Pygo) and Arm/beta-catenin. PYGO1 contains a plant homeodomain (PHD) finger, which is important for Lgs/Bcl9 recognition as well as for the regulation of the Wnt/beta-catenin signaling pathway
YPCGICTNEVNDDQDAILCEASCQKWFHRICTGMTETAYGLLTAEASAVWGCDTCMA
>gnl|CDD|277106 cd15636, PHD_PYGO2, PHD finger found in pygopus homolog 2 (PYGO2). PYGO2 is a homolog of Drosophila melanogaster protein pygopus (dPYGO), which is a fundamental Wnt signaling transcriptional component in Drosophila. It functions as a context-dependent beta-catenin coactivator, as well as a histone methylation reader that binds di-and trimethylated lysine 4 of histone H3 (H3K4me2/3). Moreover, PYGO2 acts as a chromatin remodeler in a testis-specific and Wnt-unrelated manner. It also mediates chromatin regulation and links Wnt signaling and Notch signaling to suppress the luminal/alveolar differentiation competence of mammary stem and basal cells. Furthermore, PYGO2 plays a new role in rRNA transcription during cancer cell growth. It regulates mammary tumor initiation and heterogeneity in MMTV-Wnt1 mice. PYGO2 contains a plant homeodomain (PHD) finger, which is important for Lgs/Bcl9 recognition as well as for the regulation of the Wnt/beta-catenin signaling pathway
PCGACRSEVNDDQDAILCEASCQKWFHRECTGMTESAYGLLTTEASAVWACDFC
>gnl|CDD|277107 cd15637, PHD_dPYGO, PHD finger found in Drosophila melanogaster protein pygopus (dPYGO) and similar proteins. dPYGO, also termed protein gammy legs, is a nuclear adapter protein encoded by pygopus (pygo). It is a fundamental Wnt signaling transcriptional component in Drosophila, and has both Wnt-related and Wnt-independent functions. It plays a critical role in aging-related cardiac dysfunction that is canonical Wnt signaling independent. dPYGO contains a plant homeodomain (PHD) finger, which is important for Lgs/Bcl9 recognition as well as for the regulation of the Wnt/beta-catenin signaling pathway
PCGKCHKEVHDNDQAILCESGCNFWFHRTCTGLTEAAFHMLTKEVYAEWVCDKC
>gnl|CDD|277108 cd15638, PHD_PHF3, PHD finger found in PHD finger protein 3 (PHF3). PHF3 is a human homolog of yeast protein bypass of Ess1 (Bye1), a nuclear protein with a domain resembling the central domain in the transcription elongation factor TFIIS. It is ubiquitously expressed in normal tissues including brain, but its expression is significantly reduced or lost in glioblastomas. PHF3 contains an N-terminal plant homeodomain (PHD) finger, a central RNA polymerase II (Pol II)-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain
QCGFCKKPHGNRFMVGCGRCDDWFHGDCVGLSLSQAQQMEEEDKEYVCVKC
>gnl|CDD|277109 cd15639, PHD_DIDO1_like, PHD finger found in death-inducer obliterator variants Dido1, Dido2, and Dido3. This family includes three alternative splicing variants (Dido1, 2, and 3) encoded by the Dido gene, which have been implicated in a number of cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. Dido1, also termed DIO-1, or death-associated transcription factor 1 (DATF-1), is important for maintaining embryonic stem (ES) cells and directly regulates the expression of pluripotency factors. It is the shortest isoform that contains only a highly conserved plant homeodomain (PHD) finger responsible for the binding of histone H3 with a higher affinity for trimethylated lysine 4 (H3K4me3). Gene Dido is a Bonemorphogenetic protein (BMP) target gene, which promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. Dido3 is the largest isoform ubiquitously expressed in all human tissues. It is dispensable for ES cell self-renewal and pluripotency, but involved in the maintenance of stem cell genomic stability and tumorigenesis. Dido3 contains a PHD finger, a transcription elongation factor S-II subunit M (TFSIIM) domain, aspen paralog and ortholog (SPOC) module, and a long C-terminal region (CT) of unknown homology. Its PHD finger interacts with H3K4me3
PNALYCICRQPHNNRFMICCDRCEEWFHGDCVGITEARGRLLERNGEDYICPNC
>gnl|CDD|277110 cd15640, PHD_KDM7, PHD finger found in lysine-specific demethylase 7 (KDM7). KDM7, also termed JmjC domain-containing histone demethylation protein 1D (JHDM1D), or KIAA1718, is a dual histone demethylase that catalyzes demethylation of monomethylated and dimethylated H3K9 (H3K9me2/me1) and H3K27 (H3K27me2/me1), which functions as an eraser of silencing marks on chromatin during brain development. It also plays a tumor-suppressive role by regulating angiogenesis. KDM7 contains a plant homeodomain (PHD) that binds Lys4-trimethylated histone 3 (H3K4me3) and a jumonji domain that demethylates either H3K9me2 or H3K27me2
YCVCRQPYDVNRFMIECDICKDWFHGSCVQVEEHHAADIDLYHCPNCEVL
>gnl|CDD|277111 cd15641, PHD_PHF2, PHD finger found in lysine-specific demethylase PHF2. PHF2, also termed GRC5, or PHD finger protein 2, is a histone lysine demethylase ubiquitously expressed in various tissues. It contains a plant homeodomain (PHD) finger and a JmjC domain and plays an important role in adipogenesis. The PHD finger domain can recognize trimethylated histone H3 lysine 4 (H3K4me3). PHF2 also has dimethylated histone H3 lysine 9(H3K9me2) demethylase activity and acts as a coactivator of several metabolism-related transcription factors. Moreover, it can demethylate ARID5B and further forms a complex with demethylated ARD5B to bind the promoter regions of target genes. The overexpression of PHF2 is involved in the progression of esophageal squamous cell carcinoma (ESCC)
YCICRLPYDVTRFMIECDACKDWFHGSCVGVEEEEAPDIDIYHCPNCEKT
>gnl|CDD|277112 cd15642, PHD_PHF8, PHD finger found in histone lysine demethylase PHF8. PHF8, also termed PHD finger protein 8, or KDM7B, is a monomethylated histone H4 lysine 20 (H4K20me1) demethylase that transcriptionally regulates many cell cycle genes. It also preferentially acts on H3K9me2 and H3K9me1. PHF8 is modulated by CDC20-containing anaphase-promoting complex (APC (cdc20)) and plays an important role in the G2/M transition. It acts as a critical molecular sensor for mediating retinoic acid (RA) treatment response in RAR alpha-fusion-induced leukemia. Moreover, PHF8 is essential for cytoskeleton dynamics and is associated with X-linked mental retardation. PHF8 contains an N-terminal plant homeodomain (PHD) finger followed by a JmjC domain. The PHD finger mediates binding to nucleosomes at active gene promoters and the JmjC domain catalyzes the demethylation of mono- or dimethyl-lysines
VYCLCRLPYDVTRFMIECDVCQDWFHGSCVGVEEEKAAEIDLYHCPNCQVTH
>gnl|CDD|277113 cd15643, PHD_KDM2A, PHD finger found in Lysine-specific demethylase 2A (KDM2A). KDM2A, also termed CXXC-type zinc finger protein 8, or F-box and leucine-rich repeat protein 11 (FBXL11), or F-box protein FBL7, or F-box protein Lilina, or F-box/LRR-repeat protein 11, or JmjC domain-containing histone demethylation protein 1A (Jhdm1a), or [Histone-H3]-lysine-36 demethylase 1A, is a ubiquitously expressed histone H3 lysine 36 (H3K36) demethylase that has been implicated in gene silencing, cell cycle, cell growth, and cancer development. It acts as a key negative regulator of gluconeogenic gene expression and plays a critical role in the invasiveness, proliferation, and anchorage-independent growth of non-small cell lung cancer (NSCLC) cells, as well as in the osteo/dentinogenic differentiation of Mesenchymal stem cells (MSCs). It regulates rRNA transcription in response to starvation. Meanwhile, it is a negative regulator of NFkappaB. Moreover, KDM2A is a heterochromatin-associated and HP1-interacting protein that promotes HP1 localization to chromatin. It is specifically recruited to CpG islands to define a unique chromatin architecture, which requires direct and specific interaction with linker DNA. It also functions as a H3K4 demethylase that regulates cell proliferation through p15 (INK4B) and p27 (Kip1) in stem cells from apical papilla (SCAPs). KDM2A belongs to the JmjC-domain-containing histone demethylase family. KDM2A consists of two Jumonji C (JmjC) domains, and FBXHA and FBXHB domains. A CXXC zinc-finger domain, followed by a plant homeodomain (PHD) finger, is located within the FBXHA domain, and an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain, is located within the FBXHB domain
TCALCGEVDQNEDTQDFEKKLMECCICNEIVHPGCLQMDGEGLLNDELPNCWECPKC
>gnl|CDD|277114 cd15644, PHD_KDM2B, PHD finger found in Lysine-specific demethylase 2B (KDM2B). KDM2B, also termed Ndy1, or CXXC-type zinc finger protein 2, or F-box and leucine-rich (LRR) repeat protein 10 (FBXL10), or F-box protein FBL10, or JmjC domain-containing histone demethylation protein 1B (Jhdm1b), or Jumonji domain-containing EMSY-interactor methyltransferase motif protein (Protein JEMMA), or [Histone-H3]-lysine-36 demethylase 1B, is a ubiquitously expressed histone H3 lysine 4 (H3K4me2) or histone H3 lysine 36 (H3K36me2) demethylase that functions as a regulator of chemokine expression, cellular morphology, and the metabolome of fibroblasts. It regulates the differentiation of Mesenchymal Stem Cells (MSCs) and has been implicated in cell cycle regulation by de-repressing cyclin-dependent kinase inhibitor 2B (CDKN2B or p15INK4B). It also plays a role in recruiting polycomb repressive complex 1 (PRC1) to CpG islands (CGIs) of developmental genes and regulates lysine 119 monoubiquitylation on H2A (H2AK119ub1) in embryonic stem cells (ESCs). Moreover, it acts as an oncogene that plays a critical role in leukemia development and maintenance. KDM2B consists of two Jumonji C (JmjC) domains, and FBXHA and FBXHB domains. A CXXC zinc-finger domain, followed by a plant homeodomain (PHD) finger, is located within the FBXHA domain, and an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain, is located within the FBXHB domain
VCLVCGEAGKEDTVEEEEGKFNLMLMECSICNEIIHPGCLKVKESDGVVNDELPNCWECPKC
>gnl|CDD|277115 cd15645, PHD_FXL19, PHD finger found in F-box and leucine-rich repeat protein 19 (FBXL19). FBXL19, also termed F-box/LRR-repeat protein 19, is a novel homolog of KDM2A and KDM2B. It belongs to the Skp1-Cullin-F-box (SCF) family of E3 ubiquitin ligases. FBXL19 mediates ubiquitination and interleukin 33 (IL-33)-induced degradation of ST2L receptor in lung epithelia, blocks IL-33-mediated apoptosis, and prevents endotoxin-induced acute lung injury. It also functions as a RhoA antagonist during cell proliferation and cytoskeleton rearrangement, and regulates RhoA ubiquitination and degradation in lung epithelial cells. Moreover, FBXL19 regulates cell migration by targeting Rac1 for its polyubiquitination and proteasomal degradation. It plays an essential role in regulating TGFbeta1-induced E-cadherin down-regulation by mediating Rac3 site-specific ubiquitination and stability. FBXL19 consists of FBXHA and FBXHB domains. A CXXC zinc-finger domain, followed by a plant homeodomain (PHD) finger, is located within the FBXHA domain, and an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain, is located within the FBXHB domain
VCLACGEAGKEDTAEGEEEKFDLSLMECTICNEIIHPGCLKMGKAEGVINAEIPNCWECPKC
>gnl|CDD|277116 cd15646, PHD_p300, PHD finger found in histone acetyltransferase p300. p300, also termed KAT3B, or E1A-associated protein p300 (EP300), is a paralog of CREB-binding protein (CBP). It is involved in E1A function in cell cycle progression and cellular differentiation. It functions as an intrinsic HAT, as well as a factor acetyltransferase (FAT) for many transcription regulators. And thus, p300 serves as a scaffold or bridge for transcription factors and other components of the basal transcription machinery to facilitate chromatin remodeling and to activate gene transcription. p300 contains a cysteine-histidine rich region, KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain
YCCGRLFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK
>gnl|CDD|277117 cd15647, PHD_CBP, PHD finger found in CREB-binding protein (CBP). CBP, also termed as KAT3A, is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CBP is also known as CREBBP, since it specifically interacts with the phosphorylated form of cyclic adenosine monophosphate-responsive element-binding protein (CREB). It augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. CBP contains a cysteine-histidine rich region, a KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain
YCCGRPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK
>gnl|CDD|277118 cd15648, PHD1_NSD1_2, PHD finger 1 found in nuclear receptor-binding SET domain-containing protein NSD1 and NSD2. NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or Lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein, is a lysine methyltransferase that preferentially methylates H3 on Lysine36 (H3-K36) and H4 on Lysine20 (H4-K20), which is primarily associated with active transcription. It plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. It can alter transcription by interacting with the protein NSD1-interacting zinc finger protein 1 (NIZP1). It also mitigates caspase-1 activation by listeriolysin o (LLO) in macrophages, and requires functional LLO for the regulation of IL-1beta secretion. Moreover, NSD1 regulates RNA polymerase II (RNAP II) recruitment to bone morphogenetic protein 4 (BMP4). NSD2, also termed histone-lysine N-methyltransferase NSD2, or multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). Both NSD1 and NSD2 contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). In addition, NSD2 harbors a high mobility group (HMG) box. The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the first PHD finger
VCQVCEKPGELLLCEGQCCGAFHLDCIGLSEMPSGKFICDECI
>gnl|CDD|277119 cd15649, PHD1_NSD3, PHD finger 1 found in nuclear SET domain-containing protein 3 (NSD3). NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant-homeodomain (PHD) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the first PHD finger
VCQVCESFGESLVTCEGECCGLFHLECLGLTSLPDEKFICQECK
>gnl|CDD|277120 cd15650, PHD2_NSD1, PHD finger 2 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1). NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or LysineN-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein, is a lysine methyltransferase that preferentially methylates H3 on Lysine36 (H3-K36) and H4 on Lysine20 (H4-K20), which is primarily associated with active transcription. It plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. It can alter transcription by interacting with the protein NSD1-interacting zinc finger protein 1 (NIZP1). It also mitigates caspase-1 activation by listeriolysin o (LLO) in macrophages, and requires functional LLO for the regulation of IL-1beta secretion. Moreover, NSD1 regulates RNA polymerase II (RNAP II) recruitment to bone morphogenetic protein 4 (BMP4). NSD1 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the second PHD finger
TCFVCKKSDEDVRRCMLPLCGKFYHEECVLKYPPTVMQNRGFRCSLH
>gnl|CDD|277121 cd15651, PHD2_NSD2, PHD finger 2 found in nuclear SET domain-containing protein 2 (NSD2). NSD2, also termed histone-lysine N-methyltransferase NSD2, or multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). NSD2 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, a high mobility group (HMG) box, five PHD (plant homeodomain) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the second PHD finger
SCFVCKESKGDVKRCVVLHCGKFYHEACVRKYPLTVFENRGFRCPLH
>gnl|CDD|277122 cd15652, PHD2_NSD3, PHD finger 2 found in nuclear SET domain-containing protein 3 (NSD3). NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant homeodomain (PHD) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the second PHD finger
PCFSCKVPGKDVKRCSVNACGRFYHEACVRKYTTSAFESKGFRCPQH
>gnl|CDD|277123 cd15653, PHD3_NSD1, PHD finger 3 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1). NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or Lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein, is a lysine methyltransferase that preferentially methylates H3 on Lysine36 (H3-K36) and H4 on Lysine20 (H4-K20), which is primarily associated with active transcription. It plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. It can alter transcription by interacting with the protein NSD1-interacting zinc finger protein 1 (NIZP1). It also mitigates caspase-1 activation by listeriolysin o (LLO) in macrophages, and requires functional LLO for the regulation of IL-1beta secretion. Moreover, NSD1 regulates RNA polymerase II (RNAP II) recruitment to bone morphogenetic protein 4 (BMP4). NSD1 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the third PHD finger
ICLTCHATNPSNPSASKGRLMRCVRCPVAYHANDFCLAAGSVILASNSIICPNH
>gnl|CDD|277124 cd15654, PHD3_NSD2, PHD finger 3 found in nuclear SET domain-containing protein 2 (NSD2). NSD2, also termed histone-lysine N-methyltransferase NSD2, or multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). NSD2 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, a high mobility group (HMG) box, five PHD (plant homeodomain) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the third PHD finger
SCVSCHASNPSNPRATKGKMMRCVRCPVAYHGGDLCIAAGCAVLTSNSIICTNH
>gnl|CDD|277125 cd15655, PHD3_NSD3, PHD finger 3 found in nuclear SET domain-containing protein 3 (NSD3). NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant homeodomain (PHD) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the third PHD finger
CCTTCSMDKDIHKASKGRMMRCLRCPVAYHTGDGCVAAGSVLVTPHIIICSNH
>gnl|CDD|277126 cd15656, PHD4_NSD1, PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1). NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or Lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein, is a lysine methyltransferase that preferentially methylates H3 on Lysine36 (H3-K36) and H4 on Lysine20 (H4-K20), which is primarily associated with active transcription. It plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. It can alter transcription by interacting with the protein NSD1-interacting zinc finger protein 1 (NIZP1). It also mitigates caspase-1 activation by listeriolysin o (LLO) in macrophages, and requires functional LLO for the regulation of IL-1beta secretion. Moreover, NSD1 regulates RNA polymerase II (RNAP II) recruitment to bone morphogenetic protein 4 (BMP4). NSD1 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fourth PHD finger
WCFVCSEGGSLLCCESCPAAFHRECLNIDMPEGSWYCNDC
>gnl|CDD|277127 cd15657, PHD4_NSD2, PHD finger 4 found in nuclear SET domain-containing protein 2 (NSD2). NSD2, also termed histone-lysine N-methyltransferase NSD2, or multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). NSD2 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, a high mobility group (HMG) box, five PHD (plant-homeodomain) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the fourth PHD finger
WCFVCSKGGSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCR
>gnl|CDD|277128 cd15658, PHD4_NSD3, PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3). NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant-homeodomain (PHD) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fourth PHD finger
FCFVCARGGRLLCCESCPASFHPECLSIEMPEGCWNCNEC
>gnl|CDD|277129 cd15659, PHD5_NSD1, PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1). NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or Lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein, is a lysine methyltransferase that preferentially methylates H3 on Lysine36 (H3-K36) and H4 on Lysine20 (H4-K20), which is primarily associated with active transcription. It plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma and glioblastoma formation. It can alter transcription by interacting with the protein NSD1-interacting zinc finger protein 1 (NIZP1). It also mitigates caspase-1 activation by listeriolysin o (LLO) in macrophages, and requires functional LLO for the regulation of IL-1beta secretion. Moreover, NSD1 regulates RNA polymerase II (RNAP II) recruitment to bone morphogenetic protein 4 (BMP4). NSD1 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fifth PHD finger
ECFSCGDGGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH
>gnl|CDD|277130 cd15660, PHD5_NSD2, PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2). NSD2, also termed histone-lysine N-methyltransferase NSD2, or multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). NSD2 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, a high mobility group (HMG) box, five PHD (plant-homeodomain) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the fifth PHD finger
ECFRCGDGGQLVLCDRKSCTKAYHLSCLGLTKRPFGKWECPWH
>gnl|CDD|277131 cd15661, PHD5_NSD3, PHD finger 5 found in nuclear SET domain-containing protein 3 (NSD3). NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant-homeodomain (PHD) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fifth PHD finger
YCFQCGDGGELVMCDKKDCPKAYHLLCLNLTQPPYGKWECPWH
>gnl|CDD|277132 cd15662, ePHD_ATX1_2_like, Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of A. thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like proteins ATX1, -2, and similar proteins. ATX1 and -2 are sister paralogs originating from a segmental chromosomal duplication; they are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1 (also known as protein SET domain group 27, or trithorax-homolog protein 1/TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1 regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2 (also known as protein SET domain group 30, or trithorax-homolog protein 2/TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical PHD finger, this non-canonical ePHD finger, and a C-terminal SET domain
CCLCPVVGGALKPTTDGRWAHLACAIWIPETCLLDVKTMEPVDGINAISKERWELSCTICKQRYGACIQC
SNNSCRVAYHPLCARAAGLCMEVADEGGEDPGDQGLRLLSYCPRH
>gnl|CDD|277133 cd15663, ePHD_ATX3_4_5_like, Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of A. thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like proteins ATX3 (also termed protein SET domain group 14, or trithorax-homolog protein 3), ATX4 (also termed protein SET domain group 16, or trithorax-homolog protein 4) and ATX5 (also termed protein SET domain group 29, or trithorax-homolog protein 5), which belong to the histone-lysine methyltransferase family. These proteins show distinct phylogenetic origins from the family of ATX1 and ATX2. They are multi-domain proteins that consist of an N-terminal PWWP domain, a canonical PHD finger, this non-canonical extended PHD finger, and a C-terminal SET domain
CCLCPVKGGALKPTDVEGLWVHVTCAWFRPEVCFKNEEKMEPAVGLLRIPLSTFLKACVICKQIHGSCTQ
CCKCATYFHAMCASRAGYHMELHCLEKNGVQITRMVSYCSFH
>gnl|CDD|277134 cd15664, ePHD_KMT2A_like, Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A/MLL1 and KMT2B/MLL2. KMT2A and KMT2B comprise the mammalian Trx branch of COMPASS family, and are both essential for mammalian embryonic development. KMT2A regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex. KMT2B is a second human homolog of Drosophila trithorax, located on chromosome 19 and functions as the catalytic subunit in the MLL2 complex. It plays a critical role in memory formation by mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. Both KMT2A and KMT2B contain a CxxC (x for any residue) zinc finger domain, three PHD fingers, this extended PHD (ePHD) finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain
CALCGVYGDDEPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGAT
VGCCLKSCPANYHFMCARKAECVFQDDKKVFCPAH
>gnl|CDD|277135 cd15665, ePHD1_KMT2C_like, Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMTC2C and KMTC2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five plant PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions
CALCNLGEVYAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPC
AAAAGCFQDIKTLTLFCPEH
>gnl|CDD|277136 cd15666, ePHD2_KMT2C_like, Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2C, and KMT2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions
CVLCGGEGDGDTDGPGRLLNLDVDKWVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGAT
VPCFKPRCANVYHLPCAIKDGCMFFKDKTMLCPSH
>gnl|CDD|277137 cd15667, ePHD_Snt2p_like, Extended PHD finger found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Snt2p. Sntp2 is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical PHD fingers, a non-canonical ePHD finger, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain
CSLCNAKESNYELAKKQSPRTRPDALKCTSNGTWCHVLCALFNEDIKFGNSKSLQPILNTESVLLKGSRQ
KCEICKVSGGGLVKCEVCDDRFHVSCAQDTPGFKLGFKKEYLSDDTENPFITDKVDNESYTLKPIIVCPK
H
>gnl|CDD|277138 cd15668, ePHD_RAI1_like, Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 (TCF-20) and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of RAI1 and TCF-20. RAI1, a homolog of stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPBP, also termed TCF-20), is a chromatin-binding protein implicated in the regulation of gene expression. TCF-20 is involved in transcriptional activation of the MMP3 (matrix metalloprotease 3) promoter. It also functions as a transcriptional co-regulator that enhances or represses the transcriptional activity of certain transcription factors/cofactors, such as specificity protein 1 (Sp1), E twenty-six 1 (Ets1), paired box protein 6 (Pax6), small nuclear RING-finger (SNURF)/RNF4, c-Jun, androgen receptor (AR) and estrogen receptor alpha (ERalpha). Both RAI1 and TCF-20 are strongly enriched in chromatin in interphase HeLa cells, and display low nuclear mobility, and have been implicated in Smith-Magenis syndrome and Potocki-Lupski syndrome
CVFCKRGPHYKGLGDLFGPYYEVWVHEDCAVWAPGVYLVGGKLYGLEEAVWVAKQSVCSSCQQTGATIGC
LHKGCKAKYHYPCAVESGCQLDEENFSLLCPKH
>gnl|CDD|277139 cd15669, ePHD_PHF7_G2E3_like, Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF7 and G2E3. PHF7, also termed testis development protein NYD-SP6, is a testis-specific PHD finger-containing protein that associates with chromatin and binds histone H3 N-terminal tails with a preference for dimethyl lysine 4 (H3K4me2). It may play an important role in stimulating transcription involved in testicular development and/or spermatogenesis. PHF7 contains a PHD finger and a non-canonical ePHD finger, both of which may be involved in activating transcriptional regulation. G2E3 is a dual function ubiquitin ligase (E3) that may play a possible role in cell cycle regulation and the cellular response to DNA damage. It is essential for prevention of apoptosis in early embryogenesis. It is also a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization. G2E3 contains two distinct RING-like ubiquitin ligase domains that catalyze lysine 48-linked polyubiquitination, and a C-terminal catalytic HECT domain that plays an important role in ubiquitin ligase activity and in the dynamic subcellular localization of the protein. The RING-like ubiquitin ligase domains consist of a PHD finger and an ePHD finger
CVLCGRSDDDPDKYGEKLQKDGICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCK
KKGASIGCAVKGCRRSFHFPCGLENGCVTQFFGEYRSFCWEH
>gnl|CDD|277140 cd15670, ePHD_BRPF, Extended PHD finger found in BRPF proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the ePHD finger of the family of BRPF proteins, which includes BRPF1, BRD1/BRPF2, and BRPF3. These are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a plant homeodomain (PHD) zinc finger followed by a non-canonical ePHD finger, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. This PHD finger binds to lysine 4 of histone H3 (K4H3), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties
CVLCPNKGGAFKQTDDGRWAHVVCALWIPEVSFANTVFLEPIDGIQNIPKARWKLTCYICKKRMGACIQC
HKKNCYTAFHVTCAQQAGLYMKIEPVKDPGNGTSDSVRKEAYCDKH
>gnl|CDD|277141 cd15671, ePHD_JADE, Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16); each of these proteins is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, has reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. This family also contains Drosophila melanogaster PHD finger protein rhinoceros (RNO). It is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating transcription of key EGFR/Ras pathway regulators in the Drosophila eye. All Jade proteins contain a canonical PHD finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs
CVLCPKKGGAMKSTKSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPMSRWALVCVLCKEKTGACIQ
CSVKSCKTAFHVTCAFQHGLEMKTILEDEDDEVKFKSYCPKH
>gnl|CDD|277142 cd15672, ePHD_AF10_like, Extended PHD finger found in protein AF-10 and AF-17. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of AF-10 and AF-17. AF-10, also termed ALL1 (acute lymphoblastic leukaemia)-fused gene from chromosome 10 protein, is a transcription factor encoded by gene AF10, a translocation partner of the MLL (mixed-lineage leukaemia) oncogene in leukaemia. AF-10 has been implicated in the development of leukemia following chromosomal rearrangements between the AF10 gene and one of at least two other genes, MLL and CALM. It plays a key role in the survival of uncommitted hematopoietic cells. Moreover, AF-10 functions as a follistatin-related gene (FLRG)-interacting protein. The interaction with FLRG enhances AF10-dependent transcription. It interacts with the human counterpart of yeast Dot1, hDOT1L, and may act as a bridge for the recruitment of hDOT1L to the genes targeted by MLL-AF10. It also interacts with the synovial sarcoma associated protein SYT protein and may play a role in synovial sarcomas and acute leukemias. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is encoded by gene AF17 that has been identified in hematological malignancies as translocation partners of the mixed lineage leukemia gene MLL. It is a putative transcription factor that may play a role in multiple signaling pathways. It is involved in chromatin-mediated gene regulation mechanisms. It functions as a component of the multi-subunit Dot1 complex (Dotcom) and plays a role in the Wnt/Wingless signaling pathway. It also seems to be a downstream target of the beta-catenin/T-cell factor pathway, and participates in G2-M progression. Moreover, it may function as an important regulator of ENaC-mediated Na+ transport and thus blood pressure. Both AF-10 and AF-17 contain an N-terminal plant homeodomain (PHD) finger followed by this non-canonical ePHD finger. The PHD finger is involved in their homo-oligomerization. In the C-terminal region, they possess a leucine zipper domain and a glutamine-rich region. This family also includes ZFP-1, the Caenorhabditis elegans AF10 homolog. It was originally identified as a factor promoting RNAi interference in C. elegans. It also acts as Dot1-interacting protein that opposes H2B ubiquitination to reduce polymerase II (Pol II) transcription
CELCPHKDGALKRTDNGGWAHVVCALYIPEVRFGNVATMEPIILQDVPQDRFNKTCYICEEQGRESKAST
GACMQCNKSGCKQSFHVTCAQMAGLLCEEAGNYSDNVKYCGYCSYH
>gnl|CDD|277143 cd15673, ePHD_PHF6_like, Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the two ePHD fingers of PFH6 and the single ePHD finger of PFH11. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4. PHF6 contains two non-canonical ePHD fingers. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema
CGFCKSGEENKETGGKLASGEKIAAHHNCMLFSSGLVQYVSPNENDFGGFDIEDVKKEIKRGRKLKCNLC
KKTGATIGCDVKQCKKTYHYHCAKKDDAKIIERNSQGIYRVYCKNH
>gnl|CDD|277144 cd15674, ePHD_PHF14, Extended PHD finger found in PHD finger protein 14 (PHF14) and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF14. PHF14 is a novel nuclear transcription factor that controls the proliferation of mesenchymal cells by directly repressing platelet-derived growth factor receptor-alpha (PDGFRalpha) expression. It also acts as an epigenetic regulator and plays an important role in the development of multiple organs in mammals. PHF14 contains three canonical plant homeodomain (PHD) fingers and this non-canonical ePHD finger. It can interact with histones through its PHD fingers
CELCPNRGGIFKETDTGRWVHLVCALYTPGVAFGDVDKLSPVTLTEMNYSKWGARECSLCEDPRFARTGV
CISCDAGMCKSYFHVTCAQREGLLSEATDEEDIADPFYAYCKQH
>gnl|CDD|277145 cd15675, ePHD_JMJD2, Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone demethylases. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2 proteins. JMJD2 proteins, also termed lysine-specific demethylase 4 histone demethylases (KDM4), have been implicated in various cellular processes including DNA damage response, transcription, cell cycle regulation, cellular differentiation, senescence, and carcinogenesis. They selectively catalyze the demethylation of di- and trimethylated H3K9 and H3K36. This model contains three JMJD2 proteins, JMJD2A-C, which all contain jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain. JMJD2D is not included in this family, since it lacks both PHD and Tudor domains and has a different substrate specificity. JMJD2A-C are required for efficient cancer cell growth
CCLCCLRGGALKPTTDGRWAHVVCAIAIPEVRFSNVPERGPIDISKIPPARLKLKCIYCSKITKSMSHMG
ACIQCSTGKCTTSFHVTCAHAAGVQMEPDDWPYPVYVTCTKH
>gnl|CDD|277146 cd15676, PHD_BRPF1, PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar proteins. BRPF1, also termed peregrin or protein Br140, is a multi-domain protein that binds histones, mediates monocytic leukemic zinc-finger protein (MOZ)-dependent histone acetylation, and is required for Hox gene expression and segmental identity. It is a close partner of the MOZ histone acetyltransferase (HAT) complex and a novel Trithorax group (TrxG) member with a central role during development. BRPF1 is primarily a nuclear protein that has a broad tissue distribution and is abundant in testes and spermatogonia. It contains a canonical Cys4HisCys3 plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. PHD and ePHD fingers both bind to lysine 4 of histone H3 (K4H3), bromodomains interact with acetylated lysines on N-terminal tails of histones and other proteins, and PWWP domains show histone-binding and chromatin association properties. BRPF1 may be involved in chromatin remodeling. This model corresponds to the canonical Cys4HisCys3 PHD finger
NALIDEDAVCCICNDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRRCLQSPSRAV
>gnl|CDD|277147 cd15677, PHD_BRPF2, PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar proteins. BRPF2, also termed bromodomain-containing protein 1 (BRD1), or BR140-like protein, is encoded by BRL (BR140 Like gene). It is responsible for the bulk of the acetylation of H3K14 and forms a novel monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with HBO1 and ING4. The complex is required for full transcriptional activation of the erythroid-specific regulator genes essential for terminal differentiation and survival of erythroblasts in fetal liver. BRPF2 shows widespread expression and localizes to the nucleus within spermatocytes. It contains a cysteine rich region harboring a canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. This model corresponds to the canonical Cys4HisCys3 PHD finger
DAVCCICMDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRHCLQSRSR
>gnl|CDD|277148 cd15678, PHD_BRPF3, PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and similar proteins. BRPF3 is a homolog of BRPF1 and BRPF2. It is a scaffold protein that forms a novel monocytic leukemic zinc finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with other regulatory subunits. BRPF3 contains a canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. This model corresponds to the canonical Cys4HisCys3 PHD finger
DAFCCVCLDDECHNSNVILFCDICNLAVHQECYGVPYIPEGQWLCRCCLQSPSRP
>gnl|CDD|277149 cd15679, PHD_JADE1, PHD finger found in protein Jade-1 and similar proteins. Jade-1, also termed PHD finger protein 17 (PHF17), is a novel binding partner of von Hippel-Lindau (VHL) tumor suppressor Pvhl, a key regulator of the cellular oxygen sensing pathway. It is highly expressed in renal proximal tubules. Jade-1 functions as an essential regulator of multiple cell signaling pathways. It may be involved in the serine/threonine kinase AKT/AKT1 pathway during renal cancer pathogenesis and normally prevents renal epithelial cell proliferation and transformation. It also acts as a pro-apoptotic and growth suppressive ubiquitin ligase to inhibit canonical Wnt downstream effector beta-catenin for proteasomal degradation, and as a transcription factor associated with histone acetyltransferase activity and with increased abundance of cyclin-dependent kinase inhibitor p21. Moreover, Jade-1 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex, and plays a role in epithelial cell regeneration. It has also been identified as a novel component of the nephrocystin protein (NPHP) complex and interacts with the ciliary protein nephrocystin-4 (NPHP4). Jade-1 contains a canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger
VCDVCQSPDGEDGNEMVFCDKCNICVHQACYGILKVPEGSWLCRTC
>gnl|CDD|277150 cd15680, PHD_JADE2, PHD finger found in protein Jade-2 and similar proteins. Jade-2, also termed PHD finger protein 15 (PHF15), is a plant homeodomain (PHD) zinc finger protein that is closely related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-2 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-2 contains a canonical Cys4HisCys3 PHD finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger
VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC
>gnl|CDD|277151 cd15681, PHD_JADE3, PHD finger found in protein Jade-3 and similar proteins. Jade-3, also termed PHD finger protein 16 (PHF16), is a plant homeodomain (PHD) zinc finger protein that is closely related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-3 is required for ING4 and ING5 to associate with histone acetyl transferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-3 contains a canonical Cys4HisCys3 PHD domain followed by a non-canonical extended PHD (ePHD) domain, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger
ICDVCRSPDSEEGNDMVFCDKCNICVHQACYGILKVPEGSWLCRTCVLGI
>gnl|CDD|277152 cd15682, PHD_ING1, PHD finger found in inhibitor of growth protein 1 (ING1). ING1 is an epigenetic regulator and a type II tumor suppressor that impacts cell growth, aging, apoptosis, and DNA repair, by affecting chromatin conformation and gene expression. It acts as a reader of the active chromatin mark, the trimethylation of histone H3 lysine 4 (H3K4me3). It binds and directs Growth arrest and DNA damage inducible protein 45 a (Gadd45a) to target sites, thus linking the histone code with DNA demethylation. It interacts with the proliferating cell nuclear antigen (PCNA) via the PCNA-interacting protein (PIP) domain in a UV-inducible manner. It also interacts with a PCNA-interacting protein, p15 (PAF). Moreover, ING1 associates with members of the 14-3-3 family, which is necessary for the cytoplasmic relocalization. Endogenous ING1 protein specifically interacts with the pro-apoptotic BCL2 family member BAX and colocalizes with BAX in a UV-inducible manner. It stabilizes the p53 tumor suppressor by inhibiting polyubiquitination of multi-monoubiquitinated forms via interaction with and colocalization of the herpesvirus-associated ubiquitin-specific protease (HAUSP)-deubiquitinase with p53. It is also involved in trichostatin A-induced apoptosis and caspase 3 signaling in p53-deficient glioblastoma cells. In addition, tyrosine kinase Src can bind phosphorylate ING1 and further regulates its activity. ING1 contains an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger
TYCLCNQVSYGEMIGCDNDECPIEWFHFSCVGLNHKPKGKWYCPKCRGE
>gnl|CDD|277153 cd15683, PHD_ING2, PHD finger found in inhibitor of growth protein 2 (ING2). ING2, also termed inhibitor of growth 1-like protein (ING1Lp), or p32, or p33ING2, is one member of the inhibitor of growth (ING) family of type II tumor suppressors. It is a core component of a multi-factor chromatin-modifying complex containing the transcriptional co-repressor SIN3A and histone deacetylase 1 (HDAC1). It has been implicated in the control of cell cycle, in genome stability, and in muscle differentiation. ING2 independently interacts with H3K4me3 (Histone H3 trimethylated on lysine 4) and PtdIns(5)P, and modulates crosstalk between lysine methylation and lysine acetylation on histone proteins through association with chromatin in the presence of DNA damage. It collaborates with SnoN to mediate transforming growth factor (TGF)-beta-induced Smad-dependent transcription and cellular responses. It is upregulated in colon cancer and increases invasion by enhanced MMP13 expression. It also acts as a cofactor of p300 for p53 acetylation and plays a positive regulatory role during p53-mediated replicative senescence. ING2 contains an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger
TYCLCNQVSYGEMIGCDNEQCPIEWFHFSCVGLTYKPKGKWYCPKCRGD
>gnl|CDD|277154 cd15684, PHD_ING4, PHD finger found in inhibitor of growth protein 4 (ING4). ING4, also termed p29ING4, is one member of the inhibitor of growth (ING) family of type II tumor suppressors. It acts as an E3 ubiquitin ligase to induce ubiquitination of the p65 subunit of NF-kappaB and inhibit the transactivation of NF-kappaB target genes. It also induces apoptosis through a p53 dependent pathway, including increasing p53 acetylation, inhibiting Mdm2-mediated degradation of p53 and enhancing the expression of p53 responsive genes both at the transcriptional and post-translational levels. Moreover, ING4 can inhibit the translation of proto-oncogene MYC by interacting with AUF1. It also regulates other transcription factors, such as hypoxia-inducible factor (HIF). In addition, ING4 associates with histone acetyltransferase (HAT) complexes containing MOZ (monocytic leukemia zinc finger protein)/MORF (MOZ-related factor) and HBO1, and further directs the MOZ/MORF and HBO1 complexes to chromatin. ING4 contains an N-terminal ING histone-binding domain and a C-terminal plant homeodomain (PHD) finger
TYCLCHQVSYGEMIGCDNPDCSIEWFHFACVGLTTKPRGKWFCPRCSQ
>gnl|CDD|277155 cd15685, PHD_ING5, PHD finger found in inhibitor of growth protein 5 (ING5). ING5, also termed p28ING5, is one member of the inhibitor of growth (ING) family of type II tumor suppressors. It acts as a Tip60 cofactor that acetylates p53 at K120 and subsequently activates the expression of p53-dependent apoptotic genes in response to DNA damage. Aberrant ING5 expression may contribute to pathogenesis, growth, and invasion of gastric carcinomas and colorectal cancer. ING5 can physically interact with p300 and p53 in vivo, and its overexpression induces apoptosis in colorectal cancer cells. It also associates with cyclin A1 (INCA1) and functions as a growth suppressor with suppressed expression in Acute Myeloid Leukemia (AML). Moreover, ING5 translocation from the nucleus to the cytoplasm might be a critical event for carcinogenesis and tumor progression in human head and neck squamous cell carcinoma. In addition, ING5 associates with histone acetyltransferase (HAT) complexes containing MOZ (monocytic leukemia zinc finger protein)/MORF (MOZ-related factor) and HBO1, and further directs the MOZ/MORF and HBO1 complexes to chromatin. ING5 contains an N-terminal ING histone-binding domain and a C-terminal plant homeodomain (PHD) finger
TYCLCHQVSYGEMIGCDNPDCPIEWFHFACVDLTTKPKGKWFCPRCTQE
>gnl|CDD|277156 cd15686, PHD3_KDM5A, PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A). KDM5A, also termed Histone demethylase JARID1A, or Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2), was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as a trimethylated histone H3 lysine 4 (H3K4me3) demethylase that belongs to the JARID subfamily within the JmjC proteins. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5A contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the third PHD finger
AVCAAQNCQRPCKDKVDWVQCDGGCDEWFHQVCVGVSPEMAENEDYICINCA
>gnl|CDD|277157 cd15687, PHD3_KDM5B, PHD finger 3 found in lysine-specific demethylase 5B (KDM5B). KDM5B, also termed Cancer/testis antigen 31 (CT31), or Histone demethylase JARID1B, or Jumonji/ARID domain-containing protein 1B (JARID1B), or PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), is a member of the JARID subfamily within the JmjC proteins. It has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well as TIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. KDM5B contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the third PHD finger
LCPAVSCLQPEGEEVDWVQCDGSCNRWFHQVCVGVSAEMAEKEDYICVSC
>gnl|CDD|277158 cd15688, PHD1_MOZ, PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ). MOZ, also termed histone acetyltransferase KAT6A, YBF2/SAS3, SAS2 and TIP60 protein 3 (MYST-3), or runt-related transcription factor-binding protein 2, or zinc finger protein 220, is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ and MOZ-related factor (MORF) are catalytic subunits of histone acetyltransferase (HAT) complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and implicated in human leukemias. It is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphomagenesis and bone development, and its homologs. MOZ contains a linker histone 1 and histone 5 domains and two plant homeodomain (PHD) fingers. The model corresponds to the first PHD finger
PIPICSFCLGTKEQNREKKPEELISCADCGNSGHPSCLKFSPELTVRVKALRWQCIECK
>gnl|CDD|277159 cd15689, PHD1_MORF, PHD finger 1 found in monocytic leukemia zinc finger protein-related factor (MORF). MORF, also termed MOZ2, or histone acetyltransferase KAT6B, or MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4 (MYST4), is a ubiquitously expressed transcriptional regulator with intrinsic histone acetyltransferase (HAT) activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. MORF and monocytic leukemia zinc-finger protein (MOZ) are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are also implicated in human leukemias. MORF contains an N-terminal region containing two plant homeodomain (PHD) fingers, a putative HAT domain, an acidic region, and a C-terminal Ser/Met-rich domain. The model corresponds to the first PHD finger
PIPICSFCLGTKESNREKKPEELLSCADCGSSGHPSCLKFCPELTANVKALRWQCIECK
>gnl|CDD|277160 cd15690, PHD1_DPF1, PHD finger 1 found in D4, zinc and double PHD fingers family 1 (DPF1). DPF1, also termed zinc finger protein neuro-d4, or BRG1-associated factor 45B (BAF45B), is encoded by a neuro specific gene, neuro-d4. It may be involved in the transcription regulation of neuro specific gene clusters. DPF1 contains a nuclear localization signal in the N-terminal region, a Cys2His2 (C2H2) zinc finger or Kruppel-type zinc-finger and a sequence of negatively charged amino acids in the central, and a cysteine/histidine-rich region that is composed of two adjacent plant homeodomain (PHD)-fingers (d4-domain) in the C-terminal part of the molecule. The family corresponds to the first PHD finger
IPNGYCDFCLGGAKKTGCPEDLISCADCGRSGHPSCLQFTVNMTAAVRTYRWQCIECK
>gnl|CDD|277161 cd15691, PHD1_DPF2_like, PHD finger 1 found in D4, zinc and double PHD fingers family 2 (DPF2). DPF2 (also termed zinc finger protein ubi-d4, apoptosis response zinc finger protein, BRG1-associated factor 45D (BAF45D), or protein requiem) is a transcription factor that is encoded by the ubiquitously expressed gene, ubi-d4, and may be involved in leukemia or other cancers with other genes connected with cancer. It recognizes acetylated histone H3 and suppresses the function of estrogen-related receptor alpha (ERRalpha) through histone deacetylase 1 (HDAC1). Moreover, DPF2 functions as a linker protein between the SWI/SNF complex and RelB/p52 NF-kappaB heterodimer and plays important roles in NF-kappaB transactivation via its non-canonical pathway. It is also required as a transcriptional coactivator in SWI/SNF complex-dependent activation of NF-kappaB RelA/p50 heterodimer. DPF2 contains a nuclear localization signal in the N-terminal region, a Cys2His2 (C2H2) zinc finger or Kruppel-type zinc-finger and a sequence of negatively charged amino acids in the central region, and a cysteine/histidine-rich region that is composed of two adjacent plant homeodomain (PHD) fingers (d4-domain) in the C-terminal part of the molecule. This subfamily also includes DPF3 from zebrafish. This model describes the first PHD finger
YCDFCLGDSKINKKTGQPEELVSCSDCGRSGHPSCLQFTPVMMAAVKTYRWQCIEC
>gnl|CDD|277162 cd15692, PHD1_DPF3, PHD finger 1 found in D4, zinc and double PHD fingers family 3 (DPF3). DPF3, also termed BRG1-associated factor 45C (BAF45C), or zinc finger protein cer-d4, is encoded by a neuro-specific gene, cer-d4. It functions as a new epigenetic key factor for heart and muscle development and may be involved in the transcription regulation of neuro-specific gene clusters. It interacts with the BAF chromatin remodeling complex and binds methylated and acetylated lysine residues of histone 3 and 4. DPF3 contains a nuclear localization signal in the N-terminal region, a Cys2His2 (C2H2) zinc finger or Kruppel-type zinc-finger and a sequence of negatively charged amino acids in the central region, and a cysteine/histidine-rich region that is composed of two adjacent plant homeodomain (PHD) fingers (d4-domain) in the C-terminal part of the molecule. This model corresponds to the first PHD finger
YCDFCLGGSNMNKKSGRPEELVSCADCGRSGHPTCLQFTVNMTEAVKTYQWQCIECK
>gnl|CDD|277163 cd15693, ePHD_KMT2A, Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of KMT2A. KMT2A also termed ALL-1, or CXXC-type zinc finger protein 7, or myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), or trithorax-like protein (Htrx), or zinc finger protein HRX, is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three PHD fingers, a Bromodomain domain, this extended PHD finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain
RQCALCLKYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPG
ATVGCCLTSCTSNYHFMCSRAKNCVFLEDKKVYCQRHKDLIKG
>gnl|CDD|277164 cd15694, ePHD_KMT2B, Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of KMT2B. KMT2B is also called trithorax homolog 2 or WW domain-binding protein 7 (WBP-7). KMT2B is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3 lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B plays a critical role in memory formation by mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. KMT2B contains a CxxC (x for any residue) zinc finger domain, three PHD fingers, this ePHD finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain
CALCLKYGDADSKDAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGAT
VGCCLSACLSNFHFMCARASRCCFQDDKKVFCQKH
>gnl|CDD|277165 cd15695, ePHD1_KMT2D, Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMT2D. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 at Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions
CALCNCGECWVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPC
AAASGSFQSMKTLLLLCPEH
>gnl|CDD|277166 cd15696, ePHD1_KMT2C, Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMT2C. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains several PHD fingers, two ePHD fingers, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains
CAFCYCGECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPC
AAGAGTFQDFSRRLLLCPTH
>gnl|CDD|277167 cd15697, ePHD2_KMT2C, Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2C. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains PHD fingers, two ePHD fingers, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains
CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGAT
SGCHRLRCTNVYHFTCAIKAQCMFFKDKTMLCPMH
>gnl|CDD|277168 cd15698, ePHD2_KMT2D, Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2D. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions
CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGAT
NSCNRLRCPNVYHFACAIRAKCMFFKDKTMLCPMHKL
>gnl|CDD|277169 cd15699, ePHD_TCF20, Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of TCF-20. TCF-20, also termed nuclear factor SPBP, or protein AR1, or stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPRE-binding protein), is involved in transcriptional activation of the MMP3 (matrix metalloprotease 3) promoter. It is strongly enriched on chromatin in interphase HeLa cells, and displays low nuclear mobility, and has been implicated in Smith-Magenis syndrome and Potocki-Lupski syndrome. As a chromatin-binding protein, TCF-20 plays a role in the regulation of gene expression. It also functions as a transcriptional co-regulator that enhances or represses the transcriptional activity of certain transcription factors/cofactors, such as specificity protein 1 (Sp1), E twenty-six 1 (Ets1), paired box protein 6 (Pax6), small nuclear RING-finger (SNURF)/RNF4, c-Jun, androgen receptor (AR) and estrogen receptor alpha (ERalpha). TCF-20 contains an N-terminal transactivation domain, a novel DNA-binding domain with an AT-hook motif, three nuclear localization signals (NLSs) and a C-terminal ePHD/ADD domain
CCLCGKWANYRNLGDLFGPFYEFWVHEGCILWANGIYLVCGRLYGLQEALDIAREMKCSHCQEAGATLGC
YNKGCSFRYHYPCAIDADCLLNEENFSVRCPKH
>gnl|CDD|277170 cd15700, ePHD_RAI1, Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of RAI1. RAI1, a homolog of stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPBP, also termed TCF-20), is a chromatin-binding protein implicated in the regulation of gene expression. It is strongly enriched on chromatin in interphase HeLa cells, and displays low nuclear mobility, and has been implicated in Smith-Magenis syndrome, Potocki-Lupski syndrome, and non-syndromic autism. RAI1 contains a region with homology to the novel nucleosome-binding region SPBP and an ePHD/ADD domain with ability to bind nucleosomes
CCLCRNPANYKDLGDLCGPYYPEHWVHEACAVWTTGVYLVAGKLFGLQEAVQKAADAKCSSCQGAGATVG
CCHKGCTQSYHYICAVEAGCLFEEENFSLRCPKH
>gnl|CDD|277171 cd15701, ePHD_BRPF1, Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF1. BRPF1, also termed peregrin, or protein Br140, is a multi-domain protein that binds histones, mediates monocytic leukemic zinc-finger protein (MOZ) -dependent histone acetylation, and is required for Hox gene expression and segmental identity. It is a close partner of the MOZ histone acetyltransferase (HAT) complex and a novel Trithorax group (TrxG) member with a central role during development. BRPF1 is primarily a nuclear protein that has a broad tissue distribution and is abundant in testes and spermatogonia. It contains a plant homeodomain (PHD) zinc finger followed by a non-canonical ePHD finger, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. This PHD finger binds to methylated lysine 4 of histone H3 (H3K4me), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties. BRPF1 may be involved in chromatin remodeling
CALCPNKGGAFKQTDDGRWAHVVCALWIPEVCFANTVFLEPIDSIEHIPPARWKLTCYICKQRGSGACIQ
CHKANCYTAFHVTCAQQAGLYMKMEPVRETGANGTSFSVRKTAYCDIHTPP
>gnl|CDD|277172 cd15702, ePHD_BRPF2, Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF2. BRPF2 also termed bromodomain-containing protein 1 (BRD1), or BR140-likeprotein, is encoded by BRL (BR140 Like gene). It is responsible for the bulk of the acetylation of H3K14 and forms a novel monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with HBO1 and ING4. The complex is required for full transcriptional activation of the erythroid-specific regulator genes essential for terminal differentiation and survival of erythroblasts in fetal liver. BRPF2 shows widespread expression and localizes to the nucleus within spermatocytes. It contains a cysteine rich region harboring a plant homeodomain (PHD) finger followed by a non-canonical ePHD finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain
CVLCPNKGGAFKKTDDDRWGHVVCALWIPEVGFANTVFIEPIDGVRNIPPARWKLTCYLCKQKGVGACIQ
CHKANCYTAFHVTCAQKAGLYMKMEPVKEVTGGGTTFSVRKTAYCDAH
>gnl|CDD|277173 cd15703, ePHD_BRPF3, Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF3. BRF3 is a homolog of BRPF1 and BRPF2. It is a scaffold protein that forms a novel monocytic leukemic zinc finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with other regulatory subunits. BRPF3 contains a plant homeodomain (PHD) finger followed by this non-canonical ePHD finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain
CVLCPNKGGAFKQTSDGRWAHVVCAIWIPEVCFANTVFLEPVEGVNNIPPARWKLTCYLCKQKGRGAAIQ
CHKVNCYTAFHVTCAQRAGLFMKIEPVRETGLNGTTFTVRKTAYCENH
>gnl|CDD|277174 cd15704, ePHD_JADE1, Extended PHD finger found in protein Jade-1 and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1. Jade-1, also termed PHD finger protein 17 (PHF17), is a novel binding partner of von Hippel-Lindau (VHL) tumor suppressor Pvhl, a key regulator of cellular oxygen sensing pathway. It is highly expressed in renal proximal tubules. Jade-1 functions as an essential regulator of multiple cell signaling pathways. It may be involved in the Serine/threonine kinase AKT/AKT1 pathway during renal cancer pathogenesis and normally prevents renal epithelial cell proliferation and transformation. It also acts as a pro-apoptotic and growth suppressive ubiquitin ligase to inhibit canonical Wnt downstream effector beta-catenin for proteasomal degradation and ASA transcription factor associated with histone acetyltransferase activity and with increased abundance of cyclin-dependent kinase inhibitor p21. Moreover, Jade-1 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex, and plays a role in epithelial cell regeneration. It has also been identified as a novel component of the nephrocystin protein (NPHP) complex and interacts with the ciliary protein nephrocystin-4 (NPHP4). Jade-1 contains a canonical plant homeodomain (PHD) finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs
QPKCLLCPKKGGAMKPTRSGTKWVHVSCALWIPEVSIGSPEKMEPITKVSHIPSSRWALVCSLCNEKVGA
SIQCSVKNCRTAFHVTCAFDRGLEMKTILAENDEVKFKSYCPKHSSTK
>gnl|CDD|277175 cd15705, ePHD_JADE2, Extended PHD finger found in protein Jade-2 and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-2. Jade-2, also termed PHD finger protein 15 (PHF15), is a plant homeodomain (PHD) zinc finger protein that is closely related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-2 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-2 contains a canonical PHD finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs
CLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQ
CSMPSCITAFHVTCAFDHGLEMRTTLADNDEVKFKSFCLEH
>gnl|CDD|277176 cd15706, ePHD_JADE3, Extended PHD finger found in protein Jade-3 and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-3. Jade-3, also termed PHD finger protein 16 (PHF16), is a plant homeodomain (PHD) zinc finger protein that is close related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-3 is required for ING4 and ING5 to associate with histone acetyl transferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-3 contains a canonical PHD domain followed by this non-canonical ePHD domain, both of which are zinc-binding motifs
CLLCPKTGGAMKATRTGTKWAHVSCALWIPEVSIACPERMEPITKVSHIPPSRWALVCSLCKLKTGACIQ
CSVKSCITAFHVTCAFEHSLEMKTILDEGDEVKFKSYCLKH
>gnl|CDD|277177 cd15707, ePHD_RNO, Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Drosophila melanogaster RNO. RNO is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating the transcription of key EGFR/Ras pathway regulators in the Drosophila eye. RNO contains a canonical PHD domain followed by this non-canonical ePHD domain, both of which are zinc-binding motifs
CILCPNKGGAMKSTRSGTKWAHVSCALWIPEVSIGCVEKMEPITKISSIPASRWALICVLCRERTGACIQ
CSVKTCKTAYHVTCGFQHGLEMKTILDEESEDGVKLRSYCQKH
>gnl|CDD|277178 cd15708, ePHD_AF10, Extended PHD finger found in protein AF-10 and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of AF-10. AF-10, also termed ALL1 (acute lymphoblastic leukaemia)-fused gene from chromosome 10 protein, is a transcription factor encoded by gene AF10, a translocation partner of the MLL (mixed-lineage leukaemia) oncogene in leukaemia. AF-10 has been implicated in the development of leukemia following chromosomal rearrangements between the AF10 gene and one of at least two other genes, MLL and CALM. It plays a key role in the survival of uncommitted hematopoietic cells. Moreover, AF-10 functions as a follistatin-related gene (FLRG)-interacting protein. The interaction with FLRG enhances AF10-dependent transcription. It interacts with human counterpart of the yeast Dot1, hDOT1L, and may act as a bridge for the recruitment of hDOT1L to the genes targeted by MLL-AF10. It also interacts with the synovial sarcoma associated protein SYT protein and may play a role in synovial sarcomas and acute leukemias. AF-10 contains an N-terminal plant homeodomain (PHD) finger followed by this non-canonical ePHD finger
ARVRCELCPHKDGALKRTDNGGWAHVVCALYIPEVQFANVSTMEPIVLQSVPHERYNKTCYICDEQGRES
KAATGACMTCNKHGCRQAFHVTCAQLAGLLCEEEGNGADNVQYCGYCKYHYSKLKKSKR
>gnl|CDD|277179 cd15709, ePHD_AF17, Extended PHD finger found in protein AF-17 and similar proteins. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of AF-17. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is encoded by gene AF17 that has been identified in hematological malignancies as a translocation partner of the mixed lineage leukemia gene MLL. It is a putative transcription factor that may play a role in multiple signaling pathways. It is involved in chromatin-mediated gene regulation mechanisms. It functions as a component of the multi-subunit Dot1 complex (Dotcom) and plays a role in the Wnt/Wingless signaling pathway. It also seems to be a downstream target of the beta-catenin/T-cell factor pathway, and participates in G2-M progression. Moreover, it may function as an important regulator of ENaC-mediated Na+ transport and thus blood pressure. AF-17 contains an N-terminal plant homeodomain (PHD) finger followed by a non-canonical ePHD finger
ARVRCELCPHKDGALKRTDNGGWAHVVCALYIPEVQFANVLTMEPIVLQYVPHDRFNKTCYICEEQGRES
KAASGACMTCNRHGCRQAFHVTCAQMAGLLCEEEVLEVDNVKYCGYCKYHFNKMK
>gnl|CDD|277180 cd15710, ePHD1_PHF6, Extended PHD finger 1 found in PHD finger protein 6 (PHF6). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the first ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4
CGFCRSNREKECGQLLISENQKVAAHHKCMLFSSALVSSHSDSENLGGFSIEDVQKEIKRGTKLMCSLCH
CPGATIGCDVKTCHRTYHYYCALHDKAQIRENPSQGIYMIYCRKH
>gnl|CDD|277181 cd15711, ePHD2_PHF6, Extended PHD finger 2 found in PHD finger protein 6 (PHF6). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the second ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4
CGFCHAGEEENETRGKLHIFNAKKAAAHYKCMLFSSGTVQLTTTSRAEFGDFDIKTVIQEIKRGKRMKCT
LCSQLGATIGCEIKACVKTYHYHCGVQDKAKYIENMSRGIYKLYCKNH
>gnl|CDD|277182 cd15712, ePHD_PHF11, Extended PHD finger found in PHD finger protein 11 (PHF11). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF11. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema
CAFCPKGEEYSIMYFAQEQNIAAHQNCLLYSSGFVESEEYNPLNLDRRFDVESVLNEIKRGKRLKCNFCR
KKGATVGCEERACRRSYHYFCALCDDAAIETDEVRGIYRVFCQKH
>gnl|CDD|277183 cd15713, ePHD_JMJD2A, Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2A. JMJD2A, also termed lysine-specific demethylase 4A (KDM4A), or JmjC domain-containing histone demethylation protein 3A (JHDM3A), catalyzes the demethylation of di- and trimethylated H3K9 and H3K36. It is involved in carcinogenesis and functions as a transcription regulator that may either stimulate or repress gene transcription. It associates with nuclear receptor co-repressor complex or histone deacetylases. Moreover, JMJD2A forms complexes with both the androgen and estrogen receptor (ER) and plays an essential role in growth of both ER-positive and -negative breast tumors. It is also involved in prostate, colon, and lung cancer progression. JMJD2A contains jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain
CCLCSLRGGALQRANDDKWVHVMCAVAVLEARFVNIAERSPVDVSKIPLQRFKLKCIFCKKRRKRTAGCC
VQCSHGRCPTSFHASCAQAAGVMMQPDDWPFVVFITCFRH
>gnl|CDD|277184 cd15714, ePHD_JMJD2B, Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2B. JMJD2B, also termed lysine-specific demethylase 4B (KDM4B), or JmjC domain-containing histone demethylation protein 3B (JHDM3B), specifically antagonizes the trimethyl group from H3K9 in pericentric heterochromatin and reduces H3K36 methylation in mammalian cells. It plays an essential role in the growth regulation of cancer cells by modulating the G1-S transition and promotes cell-cycle progression through the regulation of cyclin-dependent kinase 6 (CDK6). It interacts with heat shock protein 90 (Hsp90) and its stability can be regulated by Hsp90. JMJD2B also functions as a direct transcriptional target of p53, which induces its expression through promoter binding. Moreover, JMJD2B expression can be controlled by hypoxia-inducible factor 1alpha (HIF1alpha) in colorectal cancer and estrogen receptor alpha (ERalpha) in breast cancer. It is also involved in bladder, lung, and gastric cancer. JMJD2B contains jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain
CCLCNLRGGALQMTTDERWVHVICAIAVPEARFLNVIERHPVDVSAIPEQRWKLKCVYCRKRMKKVSGAC
IQCSYDHCSTSFHVTCAHAAGVVMEPDDWPYVVSITCFKH
>gnl|CDD|277185 cd15715, ePHD_JMJD2C, Extended PHD finger found in Jumonji domain-containing protein 2C (JMJD2C). The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2C. JMJD2C, also termed lysine-specific demethylase 4C (KDM4C), or gene amplified in squamous cell carcinoma 1 protein (GASC-1 protein), or JmjC domain-containing histone demethylation protein 3C (JHDM3C), is an epigenetic factor that catalyzes the demethylation of di- and trimethylated H3K9 and H3K36, and may be involved in the development and/or progression of various types of cancer including esophageal squamous cell carcinoma (ESC) and breast cancer. It selectively interacts with hypoxia-inducible factor 1alpha (HIF1alpha) and plays a role in breast cancer progression. Moreover, JMJD2C may play an important role in the treatment of obesity and its complications by modulating the regulation of adipogenesis by nuclear receptor peroxisome proliferator-activated receptor gamma (PPARgamma). JMJD2C contains jmjN and jmjC domains in the N-terminal region, followed by a canonical plant homeodomain (PHD) finger, this non-canonical ePHD finger, and a Tudor domain
CCLCNLRGGALKQTSDDKWAHVMCAVALPEVRFINVVERTPIDISRIPLQRLKLKCIFCRNRIKRVSGAC
IQCSYGRCPASFHVTCAHAAGVLMEPDDWPYVVFITCFRH
>gnl|CDD|277256 cd15716, FYVE_RBNS5, FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and similar proteins. Rbsn-5, also termed zinc finger FYVE domain-containing protein 20, is a novel Rab5 effector that is complexed to the Sec1-like protein VPS45 and recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. It also binds to Rab4 and EHD1/RME-1, two regulators of the recycling route, and is involved in cargo recycling to the plasma membrane. Moreover, Rbsn-5 regulates endocytosis at the apical side of the wing epithelium and plays a role of the apical endocytic trafficking of Fmi in the establishment of planar cell polarity (PCP)
VVPWVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKCSQFLPLHIRCCHHCKDLLERR
>gnl|CDD|277257 cd15717, FYVE_PKHF, FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), and similar proteins. This family includes protein containing both PH and FYVE domains 1 (phafin-1) and 2 (phafin-2). Phafin-1 is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway. Phafin-2 is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion
VWVPDSEAPVCMHCKKTKFTAINRRHHCRKCGAVVCGACSSKKFLLPHQSSKPLRVCDTCY
>gnl|CDD|277258 cd15718, FYVE_WDFY1_like, FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and similar proteins. This family includes WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2. WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. Both WDFY1 and WDFY2 contain a FYVE domain and multiple WD-40 repeats
PEWAESDNCQKCSRPFFWNFKQMWEKKTLGVRQHHCRKCGKAVCDKCSSNRSTIPVMGFEFPVRVCNECY
>gnl|CDD|277259 cd15719, FYVE_WDFY3, FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins. WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain
DHWVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRLRISRPVRVCQACYNIL
>gnl|CDD|277260 cd15720, FYVE_Hrs, FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins. Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites
EWKDGDECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKFGIEKEVRVCDPCYEKL
>gnl|CDD|277261 cd15721, FYVE_RUFY1_like, FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins. This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between
WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY
>gnl|CDD|277262 cd15723, FYVE_protrudin, FYVE-related domain found in protrudin and similar proteins. Protrudin, also termed zinc finger FYVE domain-containing protein 27 (ZFY27 or ZFYVE27), is a FYVE domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia (HSP). It is involved in neurite outgrowth through binding to spastin. Moreover, it functions as a key regulator of the Rab11-dependent membrane trafficking during neurite extension. It serves as an adaptor molecule that links its associated proteins, such as Rab11-GDP, VAP-A and -B, Surf4, and RTN3, to KIF5, a motor protein that mediates anterograde vesicular transport in neurons, and thus plays a key role in the maintenance of neuronal function. The FYVE domain of protrudin resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. In addition, unlike canonical FYVE domains that is located to early endosomes and specifically binds to phosphatidylinositol 3-phosphate (PtdIns3P or PI3P), the FYVE domain of protrudin is located to plasma membrane and preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). In addition to FYVE-related domain, protrudin also contains a Rab11-binding domain (RBD11), two hydrophobic domains, HP-1 and HP-2, an FFAT motif, and a coiled-coil domain
NCTGCGASFSVLLKKRRSCNNCGNAFCSRCCSKKVPRSVMGATAPAAQRETVFVCSGCNDKL
>gnl|CDD|277263 cd15724, FYVE_ZFY26, FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26). ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody
WVPDEAVSVCMVCQVERFSMFNRRHHCRRCGRVVCSSCSTKKMLVEGYRENPVRVCDQCYE
>gnl|CDD|277264 cd15725, FYVE_PIKfyve_Fab1, FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins. PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate Epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human ether-a-go-go (hERG) channels. This family also includes the yeast and plant orthologs of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal lipid kinase domain related to PtdInsP kinases
YWMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGDLRVCTYCCK
>gnl|CDD|277265 cd15726, FYVE_FYCO1, FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins. FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus
WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKACF
>gnl|CDD|277266 cd15727, FYVE_ZF21, FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins. ZF21 is phosphoinositide-binding protein that functions as a regulator of focal adhesions and cell movement through interaction with focal adhesion kinase. It can also bind to the cytoplasmic tail of membrane type 1 matrix metalloproteinase, a potent invasion-promoting protease, and play a key role in regulating multiple aspects of cancer cell migration and invasion. ZF21 contains a FYVE domain, which corresponds to this model
EPPWVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPRMCFVDPVRVCNECAL
>gnl|CDD|277267 cd15728, FYVE_ANFY1, FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins. ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain
EPPWADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFDVL
>gnl|CDD|277268 cd15729, FYVE_endofin, FYVE domain found in endofin and similar proteins. Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes
GKVAPVWVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCSLKARLEYLDNKEARVCVPCYQTL
>gnl|CDD|277269 cd15730, FYVE_EEA1, FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins. EEA1, also termed endosome-associated protein p162, or zinc finger FYVE domain-containing protein 2, is an essential component of the endosomal fusion machinery and required for the fusion and maturation of early endosomes in endocytosis. It forms a parallel coiled-coil homodimer in cells. EEA1 serves as the p97 ATPase substrate and the p97 ATPase may regulate the size of early endosomes by governing the oligomeric state of EEA1. It can interact with the GTP-bound form of Rab22a and be involved in endosomal membrane trafficking. EEA1 also functions as an obligate scaffold for angiotensin II-induced Akt activation in early endosomes. It can be phosphorylated by p38 mitogen-activated protein kinase (MAPK) and further regulate mu opioid receptor endocytosis. EEA1 consists of an N-terminal C2H2 Zn2+ finger, four long heptad repeats, and a C-terminal region containing a calmodulin binding (IQ) motif, a Rab5 interaction site, and a FYVE domain. This model corresponds to the FYVE domain that is responsible for binding phosphatidyl inositol-3-phosphate (PtdIns3P or PI3P) on the membrane
RKWADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACFDDL
>gnl|CDD|277270 cd15731, FYVE_LST2, FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins. Lst2, also termed zinc finger FYVE domain-containing protein 28, is a monoubiquitinylated phosphoprotein that functions as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Unlike other FYVE domain-containing proteins, Lst2 displays primarily non-endosomal localization. Its endosomal localization is regulated by monoubiquitinylation. Lst2 physically binds Trim3, also known as BERP or RNF22, which is a coordinator of endosomal trafficking and interacts with Hrs and a complex that biases cargo recycling
DPPLWVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGQMKPVRVCNHCFM
>gnl|CDD|277271 cd15732, FYVE_MTMR3, FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins. MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides
RWVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQLFEPSRVCKSCF
>gnl|CDD|277272 cd15733, FYVE_MTMR4, FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins. MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain
WVPDHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQLYDPVRVCNSCY
>gnl|CDD|277273 cd15734, FYVE_ZFYV1, FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins. ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop
YWVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRGWDHPVRVCDPCA
>gnl|CDD|277274 cd15735, FYVE_spVPS27p_like, FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins. spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs
PEWVDSDVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQPVRVCDGCY
>gnl|CDD|277275 cd15736, FYVE_scVPS27p_Vac1p_like, FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins. The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins
CCHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIPLNLSAYDPRNGKWYRCCHSCF
>gnl|CDD|277276 cd15737, FYVE2_Vac1p_like, FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the second FYVE domain that is responsible for the ability of Pep7p to efficiently interact with Vac1p and Vps45p
PWEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVCDDRRTKCSTEVPLDLLSSALPDLPFVFKEPQSDIP
DDTKSVRVCRDCK
>gnl|CDD|277277 cd15738, FYVE_MTMR_unchar, FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from eumetazoa. This family includes a group of uncharacterized myotubularin-related proteins mainly found in eumetazoa. Although their biological functions remain unclear, they share similar domain architecture that consists of an N-terminal pleckstrin homology (PH) domain, a highly conserved region related to myotubularin proteins, a C-terminal FYVE domain. The model corresponds to the FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch
LDWKSFRNVTECSCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRALPGHLSQRPVPVCRACY
>gnl|CDD|277278 cd15739, FYVE_RABE_unchar, FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria. This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site
EVRWQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCHTLLVKDSAP
YFS
>gnl|CDD|277279 cd15740, FYVE_FGD3, FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins. FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities
REKEKQTCKGCNESFNSITKRRHHCKQCGAVICGKCSEFKDLASRHNRVCRDCF
>gnl|CDD|277280 cd15741, FYVE_FGD1_2_4, FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia FGD1, FGD2, FGD4. This family represents a group of Rho GTPase cell division cycle 42 (Cdc42)-specific guanine nucleotide exchange factors (GEFs), including FYVE, RhoGEF and PH domain-containing protein FGD1, FGD2 and FGD4. FGD1, also termed faciogenital dysplasia 1 protein, or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF), or zinc finger FYVE domain-containing protein 3, is a central regulator of extracellular matrix remodeling and belongs to the DBL family of GEFs that regulate the activation of the Rho GTPases. FGD1 is encoded by gene FGD1. Disabling mutations in the FGD1 gene cause the human X-linked developmental disorder faciogenital dysplasia (FGDY, also known as Aarskog-Scott syndrome). FGD2, also termed zinc finger FYVE domain-containing protein 4, is expressed in antigen-presenting cells, including B lymphocytes, macrophages, and dendritic cells. It localizes to early endosomes and active membrane ruffles. It plays a role in leukocyte signaling and vesicle trafficking in cells specialized to present antigen in the immune system. FGD4, also termed actin filament-binding protein frabin, or FGD1-related F-actin-binding protein, or zinc finger FYVE domain-containing protein 6, functions as an F-actin-binding (FAB) protein showing significant homology to FGD1. It induces the formation of filopodia through the activation of Cdc42 in fibroblasts. Those FGD proteins possess a similar domain organization that contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus. However, each FGD has a unique N-terminal region that may directly or indirectly interact with F-actin. FGD1 and FGD4 have an N-terminal proline-rich domain (PRD) and an N-terminal F-actin binding (FAB) domain, respectively. This model corresponds to the FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site. FGD1 possesses a FYVE-like domain that lack the N-terminal WxxD motif. Moreover, FGD2 is the only known RhoGEF family member shown to have a functional FYVE domain and endosomal binding activity
PRWVRDNEVTMCMRCKEPFNALTRRRHHCRACGYVVCWKCSDYKATLEYDGNKLNRVCKHCYVIL
>gnl|CDD|277281 cd15742, FYVE_FGD5, FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar proteins. FGD5, also termed zinc finger FYVE domain-containing protein 23, is an endothelial cell (EC)-specific guanine nucleotide exchange factor (GEF) that regulates endothelial adhesion, survival, and angiogenesis by modulating phosphatidylinositol 3-kinase signaling. It functions as a novel genetic regulator of vascular pruning by activation of endothelial cell-targeted apoptosis. FGD5 is a homologue of FGD1 and contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. The FYVE domain of FGD5 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities
PTLVPVSHVMMCMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYPLKYLKDRPAKVCDGCFAELRKR
>gnl|CDD|277282 cd15743, FYVE_FGD6, FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins. FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site
PIWIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKAPLEYLKNKSARVCDECF
>gnl|CDD|277283 cd15744, FYVE_RUFY3, FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins. RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue)
SCSLCQEDFASLALPKHNCYNCGGTFCDACSSNELPLPSSIYEPARVCDVCY
>gnl|CDD|277284 cd15745, FYVE_RUFY4, FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins. RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear
ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVPDTCIYLRVCKTCY
>gnl|CDD|277285 cd15746, FYVE_RP3A_like, FYVE-related domain found in rabphilin-3A, Rab effector Noc2, and similar proteins. This family includes rabphilin-3A and Rab effector Noc2. Rabphilin-3A, also termed exophilin-1, is an effector protein that binds to the GTP-bound form of Rab3A, which is one of the most abundant Rab proteins in neurons and predominantly localized to synaptic vesicles. Rabphilin-3A is homologous to alpha-Rab3-interacting molecules (RIMs). It is a multi-domain protein containing an N-terminal Rab3A effector domain, a proline-rich linker region, and two tandem C2 domains. The effector domain binds specifically to the activated GTP-bound state of Rab3A and harbors a conserved FYVE zinc finger. The C2 domains are responsible for the binding of phosphatidylinositol-4,5-bisphosphate (PIP2), a key player in the neurotransmitter release process. Thus, Rabphilin-3A has also been implicated in vesicle trafficking. Rab effector Noc2, also termed No C2 domains protein, or rabphilin-3A-like protein (RPH3AL), is a Rab3 effector that mediates the regulation of secretory vesicle exocytosis in neurons and certain endocrine cells. It also functions as a Rab27 effector and is involved in isoproterenol (IPR)-stimulated amylase release from acinar cells. Noc2 contains an N-terminal Rab3A effector domain which only harbors a conserved FYVE zinc finger. The FYVE domains of Rabphilin-3A and Noc2 resemble a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif
GNGVTQCILCGDEFGLLGASPVLCKDCRKAVCTKCGVETTNSNKQPIWLCKICSE
>gnl|CDD|277286 cd15747, FYVE_Slp3_4_5, FYVE-related domain found in the synaptotagmin-like proteins 3, 4, 5. The synaptotagmin-like proteins 1-5 (Slp1-5) family belongs to the carboxyl-terminal-type (C-type) tandem C2 proteins superfamily, which also contains the synaptotagmin and the Doc2 families. Slp proteins are putative membrane trafficking proteins that are characterized by the presence of a unique N-terminal Slp homology domain (SHD), and C-terminal tandem C2 domains (known as the C2A domain and C2B domain). The SHD consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2. The SHD1 and SHD2 of Slp3, Slp4 and Slp5 are separated by a putative FYVE zinc finger. By contrast, Slp1 and Slp2 lack such zinc finger and their SHD1 and SHD2 are linked together. This model corresponds to the FYVE zinc finger. At this point, Slp1 and Slp2 are not included in this model. Moreover, the FYVE domains of Slp3, Slp4 and Slp5 resemble a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif
RICARCREKLGFIFNRGARCPKCSHKVCKKCRVLTSNTGKWLCTVCHK
>gnl|CDD|277287 cd15748, FYVE_SPIR, FYVE-related domain found in Spir proteins, Spire1 and Spire2. Spir proteins were originally discovered as the protein products of the Drosophila spire gene. They are Jun N-terminal kinase (JNK)-interacting proteins that have exclusively been identified in metazoans. They may play roles in membrane trafficking and cortical filament crosslinking. This family includes Spire1 and Spire2, which function as new essential factors in asymmetric division of oocytes. They mediate asymmetric spindle positioning by assembling a cytoplasmic actin network. They are also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, they cooperate synergistically with Fmn2 to assemble F-actin in oocytes. Both Spire1 and Spire2 contain an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. Their FYVE domains resemble FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically bind the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)
KGKVCFCCKKKKFSFFTWPNTCKLCKRVVCSKCCRDVCCDCK
>gnl|CDD|277288 cd15749, FYVE_ZFY19, FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins. ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear
RCFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRKGNQKQKVCKQCH
>gnl|CDD|277289 cd15750, FYVE_CARP, FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2. CARP1 and CARP2 are a novel group of caspase regulators by the presence of a FYVE-type zinc finger domain. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains
MPCESCGAKFSVFKRKRTCADCKRYFCSNCLSKEERGRRRCRRCRAL
>gnl|CDD|277290 cd15751, FYVE_BSN_PCLO, FYVE-related domain found in protein bassoon and piccolo. This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif
SACPLCGTSELPLGSKSPPNYNTCTDCKNRVCNQCGFNSTPPVTKVKEWLCLNCQKKRALGA
>gnl|CDD|277291 cd15752, FYVE_SlaC2-a, FYVE-related domain found in Slp homolog lacking C2 domains a (SlaC2-a) and similar proteins. SlaC2-a, also termed melanophilin, or exophilin-3, is a GTP-bound form of Rab27A-, myosin Va-, and actin-binding protein present on melanosomes. It is involved in the control of transferring of melanosomes from microtubules to actin filaments. It also functions as a melanocyte type myosin Va (McM5) binding partner and directly activates the actin-activated ATPase activity of McM5 through forming a tripartite protein complex with Rab27A and an actin-based motor myosin Va. SlaC2-a belongs to the Slp homolog lacking C2 domains (Slac2) family. It contains an N-terminal Slp homology domain (SHD), but lacks tandem C2 domains. The SHD consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2, which may function as protein interaction sites. The SHD1 and SHD2 of SlaC2-a are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. Moreover, Slac2-a has a middle myosin-binding domain and a C-terminal actin-binding domain
THCARCLQPFQFLLNSGRQCLDCGLRTCKSCSRYHPEEQGWVCDPCHLARVVKIGSLEWYYNHVRARFKR
FGSAKV
>gnl|CDD|277292 cd15753, FYVE_SlaC2-c, FYVE-related domain found in Slp homolog lacking C2 domains c (SlaC2-c) and similar proteins. SlaC2-c, also termed Rab effector MyRIP, or exophilin-8, or myosin-VIIa- and Rab-interacting protein, or synaptotagmin-like protein lacking C2 domains c, is a GTP-bound form of Rab27A-, myosin Va/VIIa-, and actin-binding protein mainly present on retinal melanosomes and secretory granules. It may play a role in insulin granule exocytosis. It is also involved in the control of isoproterenol (IPR)-induced amylase release from parotid acinar cells. SlaC2-c belongs to the Slp homolog lacking C2 domains (Slac2) family. It contains an N-terminal Slp homology domain (SHD), but lacks tandem C2 domains. The SHD consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2, which may function as protein interaction sites. The SHD1 and SHD2 of SlaC2-c are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. Moreover, Slac2-c has a middle myosin-binding domain and a C-terminal actin-binding domain
CCMRCCSPFTFLFNRKRQCRDCKFNVCKSCASYDKKEKGWTCNVCQKQR
>gnl|CDD|277293 cd15754, FYVE_PKHF1, FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins. Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway
PWIPDKATDICMRCTQTNFSLLTRRHHCRKCGFVVCHECSRQRFLIPRLSPKPVRVCSLCYRKL
>gnl|CDD|277294 cd15755, FYVE_PKHF2, FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins. Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion
VWVPDSEATVCMRCQKAKFTPVNRRHHCRKCGFVVCGPCSEKKFLLPSQSSKPVRVCDFCYDLL
>gnl|CDD|277295 cd15756, FYVE_WDFY1, FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar proteins. WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. In addition to FYVE domain, WDFY1 harbors multiple WD-40 repeats
PQWLESDSCQKCEQPFFWNIKQMWDTKTLGLRQHHCRKCGQAVCGKCSSKRSSYPIMGFEFQVRVCDSCF
ETIKDE
>gnl|CDD|277296 cd15757, FYVE_WDFY2, FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2). WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. WDFY2 contains WD40 motifs and a FYVE domain
PEWLDSDSCQKCDQPFFWNFKQMWDSKKIGLRQHHCRKCGKAVCGKCSSKRSTIPLMGFEFEVRVCDSCH
>gnl|CDD|277297 cd15758, FYVE_RUFY1, FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins. RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between
LKGHAWLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRC
S
>gnl|CDD|277298 cd15759, FYVE_RUFY2, FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins. RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions
GQVWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSS
N
>gnl|CDD|277299 cd15760, FYVE_scVPS27p_like, FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and similar proteins. scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif
HWKPDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPLPHLGPLGVPQRVCDRCF
>gnl|CDD|277300 cd15761, FYVE1_Vac1p_like, FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch
RSHWKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRNRIKLNNSAEYDPKNGKWCRCCEKCFTS
RPGYND
>gnl|CDD|277301 cd15762, FYVE_RP3A, FYVE-related domain found in rabphilin-3A and similar proteins. Rabphilin-3A, also termed exophilin-1, is an effector protein that binds to the GTP-bound form of Rab3A, which is one of the most abundant Rab proteins in neurons and predominantly localized to synaptic vesicles. Rabphilin-3A is homologous to alpha-Rab3-interacting molecules (RIMs). It is a multi-domain protein containing an N-terminal Rab3A effector domain, a proline-rich linker region, and two tandem C2 domains. The effector domain binds specifically to the activated GTP-bound state of Rab3A and harbors a conserved FYVE zinc finger. The C2 domains are responsible for the binding of phosphatidylinositol-4,5-bisphosphate (PIP2), a key player in the neurotransmitter release process. Thus, Rabphilin-3A has also been implicated in vesicle trafficking. The FYVE domain of Rabphilin-3A resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif
GDGVNRCILCGEQLGGAGSACVVCEDCKKNVCTKCGVQTNNRPHSVWLCKICSEQREVWKRSGAWFFKGL
PKQVLPQPMP
>gnl|CDD|277302 cd15763, FYVE_RPH3L, FYVE-related domain found in Rab effector Noc2 and similar proteins. Rab effector Noc2, also termed No C2 domains protein, or rabphilin-3A-like protein (RPH3AL), is a Rab3 effector that mediates the regulation of secretory vesicle exocytosis in neurons and certain endocrine cells. It also functions as a Rab27 effector and is involved in isoproterenol (IPR)-stimulated amylase release from acinar cells. Noc2 contains an N-terminal Rab3A effector domain which harbors a conserved zinc finger, but lacks tandem C2 domains. The FYVE domain of Noc2 resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif
NVMGNGLSQCLLCGELLGFLGSSSVFCQDCRKKVCTKCGIETSGSQKRPLWLCKICSEQREVWK
>gnl|CDD|277303 cd15764, FYVE_Slp4, FYVE-related domain found in synaptotagmin-like protein 4 (Slp4) and similar proteins. Slp4, also termed exophilin-2, or granuphilin, has been characterized as a regulator of the release of insulin granules from pancreatic beta-cells and dense core granules from PC12 neuronal cells by binding to Rab27A, and amylase granules from parotid gland acinar cells through interaction with syntaxin-2/3 in a Munc18-2-dependent manner on the apical plasma membrane. It can binds to syntaxin 2 in parotid acinar cells. It is also involved in granule transport by recruitment of the motor protein myosin Va. Moreover, it requires Rab8 to increase granule release in platelets. Slp4 contains an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains. The Slp homology domain (SHD) consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2, which may function as protein interaction sites. The SHD1 and SHD2 of Slp4 are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif
YSERSCGRCQESLGRLSPKANQCRGCNHLVCRDCRAVRPNGSWVCSVCAK
>gnl|CDD|277304 cd15765, FYVE_Slp3, FYVE-related domain found in synaptotagmin-like protein 3 (Slp3) and similar proteins. Slp3, also termed exophilin-6, functions as a Rab27A-specific effector in cytotoxic T lymphocytes. It binds to kinesin-1 motor through interaction with the tetratricopeptide repeat of the kinesin-1 light chain (KLC1). The kinesin-1/Slp3/Rab27a complex plays a role in mediating the terminal transport of lytic granules to the immune synapse. Slp3 contains an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains. The Slp homology domain (SHD) consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2, which may function as protein interaction sites. The SHD1 and SHD2 of Slp3 are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. In addition, the Slp3 C2A domain showed Ca2+-dependent phospholipid binding activity. At this point, Slp3 is a Ca2+-dependent isoform in Slp proteins family
ERSCARCQKPLGKLLNRGAVCNGCSHRVCSECRVFLGREIWKCTVCHA
>gnl|CDD|277305 cd15766, FYVE_Slp5, FYVE-related domain found in synaptotagmin-like protein 5 (Slp5) and similar proteins. Slp5 is a novel Rab27A-specific effector that is highly expressed in placenta and liver. Slp5 specifically interacted with the GTP-bound form of Rab27A and is involved in Rab27A-dependent membrane trafficking in specific tissues. Slp5 contains an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains. The Slp homology domain (SHD) consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2, which may function as protein interaction sites. The SHD1 and SHD2 of Slp5 are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif
RLCVRCLKNLGLIFDRGDLCQECQLRVCSECRVLGANGKWKCTVCAK
>gnl|CDD|277306 cd15767, FYVE_SPIR1, FYVE-related domain found in protein spire homolog 1 (Spire1) and similar proteins. Spire1 is encoded by gene spir-1, which is primarily found to be expressed in the developing nervous system and in neuronal cells of the adult brain, as well as in the fetal liver and in the adult spleen. It functions as a new essential factor in asymmetric division of oocytes. It mediates asymmetric spindle positioning by assembling a cytoplasmic actin network. It is also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, it cooperates synergistically with Fmn2 to assemble F-actin in oocytes. Spire1 contains an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. The FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically binds the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)
LKKGKLCFSCRSKRFSLFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPIFSLGPDWSTMEVCVDCKKF
ISDIISSSR
>gnl|CDD|277307 cd15768, FYVE_SPIR2, FYVE-related domain found in protein spire homolog 2 (Spire2) and similar proteins. Spire2 is encoded by gene spir-2, which is expressed in the nervous system and highly expressed in the colonic epithelium. It functions as a new essential factor in asymmetric division of oocytes. It mediates asymmetric spindle positioning by assembling a cytoplasmic actin network. It is also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, it cooperates synergistically with Fmn2 to assemble F-actin in oocytes. Spire2 contains an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. The FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically binds the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)
LKKGKICCCCRVKFPLFSWPSNCLFCKRSVCSSCSMKMKMPSKKLAHIPVYTVGFESPPRSTSAKANARR
WTDSLHGPSWRSVEEEFPHIYAQGSVLKDVCSDCTGFVADVV
>gnl|CDD|277308 cd15769, FYVE_CARP1, FYVE-like domain found in caspase regulator CARP1 and similar proteins. CARP1, also termed E3 ubiquitin-protein ligase RNF34, or caspases-8 and -10-associated RING finger protein 1, or FYVE-RING finger protein Momo, or RING finger homologous to inhibitor of apoptosis protein (RFI), or RING finger protein 34, or RING finger protein RIFF, is a nuclear protein that functions as a specific E3 ubiquitin ligase for the transcriptional coactivator PGC-1alpha, a master regulator of energy metabolism and adaptive thermogenesis in the brown fat cell, and negatively regulates brown fat cell metabolism. It is preferentially expressed in esophageal, gastric and colorectal cancers, suggesting a possible association with the development of the digestive tract cancers. It regulates the p53 signaling pathway through degrading 14-3-3 sigma and stabilizing MDM2. CARP1 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, CARP1 has an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus it belongs to a family of unique FYVE-type domains called FYVE-like domains. In addition to the N-terminal FYVE-like domain, CARP1 harbors a C-terminal RING domain
NIVCKACGLAFSVFRKKHVCCDCKKDFCSVCSVLQENLRRCSTCHLL
>gnl|CDD|277309 cd15770, FYVE_CARP2, FYVE-like domain found in caspase regulator CARP2 and similar proteins. CARP2, also termed E3 ubiquitin-protein ligase rififylin, or caspases-8 and -10-associated RING finger protein 2, or FYVE-RING finger protein Sakura (Fring), or RING finger and FYVE-like domain-containing protein 1, or RING finger protein 189, or RING finger protein 34-like, is a novel caspase regulator containing a FYVE-type zinc finger domain. It regulates the p53 signaling pathway through degrading 14-3-3 sigma and stabilizing MDM2. CARP2 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, CARP2 has an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus it belongs to a family of unique FYVE-type domains called FYVE-like domains. In addition to the N-terminal FYVE-like domain, CARP2 harbors a C-terminal RING domain
EISCKACGIRFASCARKHPCMDCKKNYCTACSSQAENGPSLCQLCQRFR
>gnl|CDD|277310 cd15771, FYVE1_BSN_PCLO, FYVE-related domain 1 found in protein bassoon and piccolo. This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. This model corresponds to the first FYVE-related domain
TLCPLCNTTELTLHVPKPNFNTCTQCHTTVCNQCGFNPNPHLTEVKEWLCLNCQMQRALGM
>gnl|CDD|277311 cd15772, FYVE2_BSN_PCLO, FYVE-related domain 2 found in protein bassoon and piccolo. This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. This model corresponds to the second FYVE-related domain
VTCPLCKTELNVGSKEPPNYNTCTQCHTQVCNLCGFNPTPHLVEKKEWLCLNCQTQRLMSGGLG
>gnl|CDD|277312 cd15773, FYVE1_BSN, FYVE-related domain 1 found in protein bassoon. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Bassoon contains two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif
PSSTLCPICNTTELTSFPSQPNFNTCTQCHNKVCNQCGFNPNPHLTEVKEWLCLNCQMQRALGM
>gnl|CDD|277313 cd15774, FYVE1_PCLO, FYVE-related domain 1 found in protein piccolo. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif
TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG
>gnl|CDD|277314 cd15775, FYVE2_BSN, FYVE-related domain 2 found in protein bassoon. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Bassoon contains two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif
RVTCPLCKTELNVGSTEPPNYNTCTSCRTQVCNLCGFNPTPHLVEKNEWLCLNCQTQRLLEGSLG
>gnl|CDD|277315 cd15776, FYVE2_PCLO, FYVE-related domain 2 found in protein piccolo. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif
LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG
>gnl|CDD|276940 cd15777, CRBN_C_like, Thalidomide-binding C-terminal domain of cereblon (CRBN) and similar protein domains. Cereblon is part of an E3 ubiquitin ligase complex, together with damaged DNA-binding protein 1 (DDB1), CUL4A and ROC1. Cereblon interacts directly with DDB1, although the C-terminal domain characterized here does not contribute to that interaction. Ubiquination of cellular targets by this complex increases levels of FGF8 and FGF10, which was shown to affect the development of limbs and auditory vesicles in embryogenesis. The C-terminal domain of Cereblon was shown to contain the binding site for thalidomide and its analogs, a class of teratogenic drugs that exhibit an antiproliferative effect on myelomas. Mutations in CRBN, some of which map onto the C-terminal domain, were associated with autosomal recessive mental retardation, which may have to do with interactions between CRBN and ion channels in the brain
LLCRSCGAPITRKSDIFSMSGEGHVHTFVNPHGYVFEIGTFSKAPGCALVGPPSTEFSWFPGYAWTIALC
ARCGSHLGWKFTAVEKNLSPKSFYGLILDRL
>gnl|CDD|275446 cd15778, Lreu_0056_like, Proteins similar to Lactobacillus reuteri ORF 0056. This family of Lactobacillus proteins has not been characterized. The 3D structure has been solved for a hypothetical protein with a predicted signal peptide, as part of a wider examination of the structural biology of commensal human gut flora and pathogens
LTNQQLGVLVALLIYPDWFGEDVANDPMSYGTVKDSNDGRYYIGAGGDGTSTIFFKIDGDTVTIKYLDPS
GGTSVAEAKYTTKTVSLSDLINEYYSTNSQKQTVDGYASKLK
>gnl|CDD|294014 cd15783, SA1633_like, Uncharacterized protein family conserved in Staphylococci. Some proteins in this family have been described as putative beta-lactamases. They are structurally similar to the C-terminal beta-grasp domains of Staphylococcal and Streptococcal superantigens
DGQLWKKVKDSLIDANIISGNENENVKVSYKLKNGQSNSVESTANLDGDTSSTPINFSKLTQIDIKKVNI
PGDDFNTRLDANNTWKKLTKKLKEKGLVKNGQKVTIHSKDPTDPSITGKVGEDLNDHKGRTLNKRDINKI
TIE
>gnl|CDD|275431 cd15784, PH_RUTBC, Rab-binding Pleckstrin homology domain (PH) of small G-protein signaling modulator 1 and similar proteins. Small G-protein signaling modulator 1, or RUN and TBC1 domain containing 2 (RUTBC2), as well as RUTBC1, bind to Rab9A via their Pleckstrin homology (PH) domain. They do not seem to act as GAP proteins that stimulate GTP hydrolysis by Rab9A, and RUTBC2 has been shown to also interact with Rab9B, most likely in a similar manner. RUTBC1 does stimulate GTP hydrolysis by Rab32 and Rab33B, however, while RUTBC2 appears to be a GAP for Rab36. Rab9A and associated proteins control the recycling of mannose-6-phosphate receptors from late endosomes to the trans-Golgi
STLLYGKNNVLVQPRDDKEPIKGYLSLHQTGRGNLTLKWTPNQLMNGSSQASSAKSNSLDSSVYWDYALS
VNLDDIVYIHCHQQDDSGGTVVLVGQDGVQRPPLHFPQGGHLLAFLSCLENGLLPHGQLDPPLWSQRGKG
KVLPKLRKRSSLTSSKLSEVKEEQATDYVFRIIYPG
>gnl|CDD|276946 cd15785, YycH_N_like, N-terminal domain of YycH and structurally similar proteins conserved in Firmicutes. These protein domains appear to be members of a somewhat larger structural family conserved in Firmicutes, including the N-terminal domain of YycH. YycH plays a role in signal transduction and is found immediately downstream of the essential histidine kinase YycG. YycG forms a two-component system together with its cognate response regulator YycF. YycH functions as a modulator of YycG activity, possibly by interacting with YchI. All three molecules (YchG, YchH, and YchI) have been characterized as membrane proteins, and they may be able to form homodimers
PRDIFIHDFSDGAHYKVDDNELYEEIWSDLPSLDTIDVIGIKDISDYGIGKSEYKIDLQLSDTIPEYSSF
DHILIPINETKANIKIYLVSQLILEVTVELANNYRNIMNDLKN
>gnl|CDD|276947 cd15786, CPF_1278_like, Uncharacterized protein conserved in Clostridia. This protein appears to be a member of a somewhat larger structural family conserved in Firmicutes. The 3D structure is available for one protein, CPF_1278, which has been labelled a putative lipoprotein. CPF_1278 displays structural similarity to the N-terminal domain of YycH, which plays a role in signal transduction and is found immediately downstream of the essential histidine kinase YycG. YycG forms a two-component system together with its cognate response regulator YycF. YycH functions as a modulator of YycG activity, possibly by interacting with YchI. All three molecules (YchG, YchH, and YchI) have been characterized as membrane proteins, and they may be able to form homodimers
KPNNFYYTNLLKKKLNSNESYKLSLFDTNFYKEIDLDKEDIEIIKNFIKSLKKENFINEPKDLPEKPPYK
LFITFDNEKYVINVYNDKYISVYPWDGNYPEDYISMENIPLSYNLYNFCKYIFN
>gnl|CDD|276948 cd15787, YycH_N, N-terminal domain of YycH and similar proteins. This protein appears to be a member of a somewhat larger structural family conserved in Firmicutes. YycH plays a role in signal transduction and is found immediately downstream of the essential histidine kinase YycG. YycG forms a two-component system together with its cognate response regulator YycF. YycH functions as a modulator of YycG activity, possibly by interacting with YchI. All three molecules (YchG, YchH, and YchI) have been characterized as membrane proteins, and they may be able to form homodimers. This model describes the N-terminal domain of YycH
GEEKKLEDVILPTQIIYHDNGKHYGLNDENLINEIYKELKKWEFSDFERVSNNSEEYLKLLNKKNGIELI
FPDPIPLSLFQSLFQIEDKKLPNFSFDRIVIDLDESKNEVYLYFVSTDEQTVYEATVSDSSLEDLKKLLK
KND
>gnl|CDD|276949 cd15788, Clospo_01618_like, Uncharacterized protein conserved in Clostridia. This protein appears to be a member of a somewhat larger structural family conserved in Firmicutes. It displays structural similarity to the N-terminal domain of YycH, which plays a role in signal transduction and is found immediately downstream of the essential histidine kinase YycG. YycG forms a two-component system together with its cognate response regulator YycF. YycH functions as a modulator of YycG activity, possibly by interacting with YchI. All three molecules (YchG, YchH, and YchI) have been characterized as membrane proteins, and they may be able to form homodimers
GRXEISSLSSIDVFKFNSFSKFSNDKIGVIYDEEKLSKFKVIXNSLDTSEGIKKIEVPKDANIESFKYSY
HIQPNLKYVEDNNVYDGYFLLYILVGDSEGKSYIIFSGTELSYVLDKNNTNILKEIFLN
>gnl|CDD|275432 cd15789, PH_ARHGEF2_18_like, rho guanine nucleotide exchange factor. RhoGEFs belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. The members here all contain Dbl homology (DH)-PH domains. In addition some members contain N-terminal C1 (Protein kinase C conserved region 1) domains, PDZ (also called DHR/Dlg homologous regions) domains, ANK (ankyrin) domains, and RGS (Regulator of G-protein signalling) domains or C-terminal ATP-synthase B subunit. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. RhoGEF2/Rho guanine nucleotide exchange factor 2, p114RhoGEF/p114 Rho guanine nucleotide exchange factor, p115RhoGEF, p190RhoGEF, PRG/PDZ Rho guanine nucleotide exchange factor, RhoGEF 11, RhoGEF 12, RhoGEF 18, AKAP13/A-kinase anchoring protein 13, and LARG/Leukemia-associated Rho guanine nucleotide exchange factor are included in this CD. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LKFEGTAWLKQARGKTKDVLVVVLTDVLFFLQEKDQKYVFVSPDNKAGVVSLQKLLVREKAGQEKRMFLI
SASPDGMPEMYELKVQKPKDKNTWIQTIRQAV
>gnl|CDD|275433 cd15790, PH-GRAM_MTMR11, Myotubularian (MTM) related 11 protein (MTMR11) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain. MTMR10, MTMR11, and MTMR12 are catalytically inactive phosphatases that play a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. They contains a Glu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. They contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, a SET interaction domain, and a C-terminal coiled-coil domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold
LPGEHILEEAVRVRKLVQWRDGEGFLSGTLYCTNFRVAFVPEHIQKDENDHDTVLNSEHDIALPSIDRVV
AVQGPTTMKAVTASSGLKFIPEELVIYCRDFRLLRFQFEQSTLEPQAFQITTA
>gnl|CDD|275434 cd15791, PH1_FDG4, FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 4, N-terminal Pleckstrin homology (PH) domain. In general, FGDs have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain. FGD4 is one of the genes associated with Charcot-Marie-Tooth neuropathy type 4 (CMT4), a group of progressive motor and sensory axonal and demyelinating neuropathies that are distinguished from other forms of CMT by autosomal recessive inheritance. Those affected have distal muscle weakness and atrophy associated with sensory loss and, frequently, pes cavus foot deformity. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LIKEGQILKLAARNTSAQERYLFLFNNMLLYCVPKFSLVGSKYTVRTRIGIDGMKVVETQNEDYPHTFQV
SGKERTLELQASSEQDKEEWIKAL
>gnl|CDD|275435 cd15792, PH1_FGD5, FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 5, N-terminal Pleckstrin Homology (PH) domain. FGD5 regulates promotes angiogenesis of vascular endothelial growth factor (VEGF) in vascular endothelial cells, including network formation, permeability, directional movement, and proliferation. In general, FGDs have a RhoGEF (DH) domain, followed by a PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activate the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the PH domain is involved in intracellular targeting of the DH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
VRGQRDLLQPGREFVKEGTLMKVSGKNRHPRHLFLMNDVLLYTYPQKDGKYRLKNTLAVSGMKVSRPVIE
KAQNVLKIEVSEVCLTLSASSCSERDEWYSCLSRTIPDDYKAQNASSSHSSAE
>gnl|CDD|275436 cd15793, PH1_FGD6, FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 6, N-terminal Pleckstrin Homology (PH) domain. FGD5 regulates promotes angiogenesis of vascular endothelial growth factor (VEGF) in vascular endothelial cells, including network formation, permeability, directional movement, and proliferation. The specific function of FGD6 is unknown. In general, FGDs have a RhoGEF (DH) domain, followed by a PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activate the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the PH domain is involved in intracellular targeting of the DH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
LNGHHEIVQPGRVFLKEGTLMKLSRKVMQPRMFFLFNDALLYTTPVQSGMYKLNNMLSLAGMKVSKPSQE
AYQNELNIESVERSFILSASSATERDEWLEAISRAIEEYAKKKITFNPSRSLE
>gnl|CDD|275437 cd15794, PH_ARHGEF18, Rho guanine nucleotide exchange factor 18 Pleckstrin homology (PH) domain. ARHGEF18, also called p114RhoGEF, is a key regulator of RhoA-Rock2 signaling that is crucial for maintenance of polarity in the vertebrate retinal epithelium, and consequently is essential for cellular differentiation, morphology and eventually organ function. ARHGEF18 contains Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes
RRQLLLEGMLYWKAASGRLKDILALLLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAM
FLISASLNGPEMYEIHTNSKEDRNTWMAHIRRAVESCPDEEEGLFSEPE
>gnl|CDD|275439 cd15795, PMEI-Pla_a_1_like, Pollen allergen Pla a 1 and similar plant proteins. The major Platanus acerifolia pollen allergen Pla a 1 belongs to a class of allergens related to proteinaceous invertase and pectin methylesterase inhibitors. Platanus acerifolia is an important cause of pollinosis; Pla a 1 has a prevalence of about 80% among plane tree pollen-allergic patients. Recombinant Pla a 1 binds IgE in vitro, similar to its natural counterpart, rendering it suitable for specific diagnosis and structural studies. Invertase inhibitors are structurally similar to those of pectin methylesterase (PMEIs), an enzyme that is involved in the control of pectin metabolism and is structurally unrelated to invertases. All inhibitors share a size of about 18 kDa, two strictly conserved disulfide bridges and only moderate sequence homology (about 20% sequence identity)
CKKAAAGDPNVDYDFCVSSLQSDPRSRTAADLKGLAVIATKLAIANATATKAKIEKLLKSKKYPSDLKKA
LRDCLSLYSDAVDSLKSALDALKSGDYGDANYDLSAATDAPVTCEDAFKEAKIVVSPLTKENDELFQLAL
IALAITSM
>gnl|CDD|275440 cd15796, CIF_like, Cell-wall inhibitor of beta fructosidase and similar proteins. Cell-wall invertases (CWIs) are secreted apoplastic enzymes belonging to the glycoside hydrolase family 32 (EC 3.2.1.26) that catalyze the hydrolytic cleavage of the disaccharide sucrose into glucose and fructose. Their activity is tightly regulated by compartment-specific inhibitor proteins at transcriptional and post-transcriptional levels. Invertase inhibitors are structurally similar to those of pectin methylesterase (PMEIs), an enzyme that is involved in the control of pectin metabolism and is structurally unrelated to invertases. All inhibitors share a size of about 18 kDa, two strictly conserved disulfide bridges and only moderate sequence homology (about 20% sequence identity). Interaction of invertase inhibitor Nt-CIF (Nicotiana tabacum cell-wall inhibitor of beta-fructosidase) with CWI is strictly pH-dependent, modulated between pH 4 and 6, with rapid dissociation at neutral pH mediated by structure rearrangement or surface charge pattern in the binding interface. Comparison of the CIF/INV1 structure with the complex between the structurally CIF-related pectin methylesterase inhibitor (PMEI) and pectin methylesterase indicates a common targeting mechanism in PMEI and CIF
ADLIDETCKKTPNYDLCVSILRSDPRSTTAADVKGLALIMLDAVLAKANDTLRKIGELLKKTTDPALKRA
LSSCAEEYGVIVEDDLPQAIEALKKGDYKAAKDSMYDAGKEADSCEEQFKGSSSSPLTDRNKAVHDLAVV
AAAIVRQL
>gnl|CDD|275441 cd15797, PMEI, Pectin methylesterase inhibitor. Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) catalyzes the demethylesterification of homogalacturonans in the cell wall. Its activity is regulated by the proteinaceous PME inhibitor (PMEI) which inhibits PME and invertase through formation of a non-covalent 1:1 complex. Depending on the mode of demethylesterification, PMEI activity results in either loosening or rigidification of the cell wall. PMEI has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. Thus, PMEI probably plays an important physiological role in PME regulation in plants, possessing several potential applications in a food-technological context
TEELIDTICKKTENPSFCLQILNSDPRSASADLVGLAQIAIDLAQSNATNTLKLIQSLIKSTTDPKLKNR
YESCSKNYNDAIDALEEAKKSLSSGDYDGLNKAASAALDAVSTCEDELSKPPKDPSPLAKYNRDVEDLCD
IILVISDLL
>gnl|CDD|275442 cd15798, PMEI-like_3, Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains. This subfamily contains inhibitors similar to those of pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) that catalyzes the demethylesterification of homogalacturonans in the cell wall. The proteinaceous PME inhibitor (PMEI) inhibits PME and invertase through formation of a non-covalent 1:1 complex. Depending on the mode of demethylesterification, PMEI activity results in either loosening or rigidification of the cell wall. PMEI has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. Thus, PMEI probably plays an important physiological role in PME regulation in plants, possessing several potential applications in a food-technological context
AICSSTPYPDLCKSSLSSYASSSSTDPKELAKAALNAALDEAKKALALLSSLLKSSGSNPREKAALEDCL
ELLDDAVDDLNRSLSELNSLSKDKFSERVDDVQTWLSAALTNQDTCLDGFEETGSTVKKELRASLKNVSK
LTSNALALVNALAK
>gnl|CDD|275443 cd15799, PMEI-like_4, plant invertase/pectin methylesterase inhibitor domain-containing protein. This subfamily contains inhibitors similar to those of pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) that catalyzes the demethylesterification of homogalacturonans in the cell wall, and cell-wall invertases (CWIs) that catalyze the hydrolytic cleavage of the disaccharide sucrose into glucose and fructose. The proteinaceous PME inhibitor (PMEI) inhibits PME and invertase through formation of a non-covalent 1:1 complex. Cell-wall inhibitor of beta-fructosidase from tobacco (CIF) interacts with CWI in a strictly pH-dependent manner, modulated between pH 4 and 6, with rapid dissociation at neutral pH mediated by structure rearrangement or surface charge pattern in the binding interface. Comparison of the CIF/INV1 structure with the complex between the structurally CIF-related pectin methylesterase inhibitor (PMEI) and pectin methylesterase indicates a common targeting mechanism in PMEI and CIF
SSTLIFLLLCLAIPSVSSSANALSAQCLKVPLDVFLAALKTTVDRIQSALSMVSKLRNGSDDPRLSNALS
DCLELLDFSADRLSWSLSALQNPKGDSGSDARTWLSAALTNHDTCLDGLEETGVVKSLVAAALSNLTSLL
REALAMVASVS
>gnl|CDD|275444 cd15800, PMEI-like_2, Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors. This subfamily contains inhibitors similar to those of pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) that catalyzes the demethylesterification of homogalacturonans in the cell wall, and cell-wall invertases (CWIs) that catalyze the hydrolytic cleavage of the disaccharide sucrose into glucose and fructose. The proteinaceous PME inhibitor (PMEI) inhibits PME and invertase through formation of a non-covalent 1:1 complex. Cell-wall inhibitor of beta-fructosidase from tobacco (CIF) interacts with CWI in a strictly pH-dependent manner, modulated between pH 4 and 6, with rapid dissociation at neutral pH mediated by structure rearrangement or surface charge pattern in the binding interface. Comparison of the CIF/INV1 structure with the complex between the structurally CIF-related pectin methylesterase inhibitor (PMEI) and pectin methylesterase indicates a common targeting mechanism in PMEI and CIF
DPSVKDICKKTDYPALCLSTVKPFLTKGKIDPVSALEAAIKALIAKTKQAKALAKKLAKSPSTSPEVKSA
LDVCKESYDDALDNLKKALKAIKSRDIGTLNSMLSAAITDYSTCDDAFAESGLVSPLAKINDLLKKLASN
CLAIATLL
>gnl|CDD|275445 cd15801, PMEI-like_1, Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors. This subfamily contains inhibitors similar to those of pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) that catalyzes the demethylesterification of homogalacturonans in the cell wall, and cell-wall invertases (CWIs) that catalyze the hydrolytic cleavage of the disaccharide sucrose into glucose and fructose. The proteinaceous PME inhibitor (PMEI) inhibits PME and invertase through formation of a non-covalent 1:1 complex. Cell-wall inhibitor of beta-fructosidase from tobacco (CIF) interacts with CWI in a strictly pH-dependent manner, modulated between pH 4 and 6, with rapid dissociation at neutral pH mediated by structure rearrangement or surface charge pattern in the binding interface. Comparison of the CIF/INV1 structure with the complex between the structurally CIF-related pectin methylesterase inhibitor (PMEI) and pectin methylesterase indicates a common targeting mechanism in PMEI and CIF
LIEEACKKTLDPDLCVSALSSDPESKKADLRGLAELALKAAAENATATASYVSELLNTAKDPYVQQCLED
CSENYEDAVEQLNDSLAALDSKAYGDVKTWVTAALADAETCEDAFKEKPGDKSPLTARNGDFSKLCSIAL
AIIKLL
>gnl|CDD|276805 cd15802, RING_CBP-p300, atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases. CBP and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This ring domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902
FEPQVLYCSGKCTIPRKRNAVYYSYQNLDNRYHFCEKCFNEIRGDEITLGDDQGTSISKSQFEKKKNDEL
DEE
>gnl|CDD|276941 cd15803, RLR_C_like, C-terminal domain of Retinoic acid-inducible gene (RIG)-I-like Receptors, Cereblon (CRBN), and similar protein domains. Retinoic acid-inducible gene (RIG)-I-like Receptors (RLRs) are cytoplasmic RNA receptors that recognize non-self RNA and act as molecular sensors to detect viral pathogens. They play crucial roles in innate antiviral responses, including the production of proinflammatory cytokines and type I interferon. There are three RLRs in vertebrates, RIG-I, LGP2, and MDA5. They are characterized by a central DExD/H-box helicase domain and a C-terminal domain, both of which are responsible for binding viral RNA. Cereblon is part of an E3 ubiquitin ligase complex, together with damaged DNA binding protein 1 (DDB1), CUL4A and ROC1. Cereblon interacts directly with DDB1, although the C-terminal domain characterized here does not contribute to that interaction. The C-terminal domain of Cereblon was shown to contain the binding site for thalidomide and its analogs, a class of teratogenic drugs that exhibit an antiproliferative effect on myelomas. Mutations in CRBN, some of which map onto the C-terminal domain, were associated with autosomal recessive mental retardation, which may have to do with interactions between CRBN and ion channels in the brain. RLRs and Cereblon contain a common conserved zinc binding site in their C-terminal domains
LLCKNCSALACTGEDIRVIELCHHVVYKPAFKNNYNVIGRPSTVHKWFDGYAWGIISCKICSSHWGWHFT
YKPQKLPVLKRESF
>gnl|CDD|276942 cd15804, RLR_C, C-terminal domain of Retinoic acid-inducible gene (RIG)-I-like Receptors. Retinoic acid-inducible gene (RIG)-I-like Receptors (RLRs) are cytoplasmic RNA receptors that recognize non-self RNA and act as molecular sensors to detect viral pathogens. They play crucial roles in innate antiviral responses, including the production of proinflammatory cytokines and type I interferon. There are three RLRs in vertebrates, RIG-I, LGP2, and MDA5. They are characterized by a central DExD/H-box helicase domain and a C-terminal domain, both of which are responsible for binding viral RNA. The helicase domain catalyzes the unwinding of double stranded RNA in an ATP-dependent manner. RIG-I and MDA5 also contain two N-terminal caspase activation and recruitment domains (CARDs), which initiate downstream signaling upon viral RNA sensing. They may detect partially overlapping viral substrates, including dengue virus, West Nile virus (WNV), reoviruses, and several paramyxoviruses (such as measles virus and Sendai virus). LGP2 lacks CARD and may play a regulatory role in RLR signaling. It may cooperate with either RIG-I or MDA5 to sense viral RNA
FTLLCKKCSAFACNSDDIRKIEGSHHVVIDPDFLERVKIEEDPKKKKKFEDTQILGKIKCKKCGHDWGTM
MKYKGVELPVLKIKNFVFVDEDEERATKKKWKDVPFAIPEI
>gnl|CDD|276943 cd15805, RIG-I_C, C-terminal domain of Retinoic acid-inducible gene (RIG)-I protein, a cytoplasmic viral RNA receptor. Retinoic acid-inducible gene (RIG)-I protein, also called DEAD box protein 58 (DDX58), is one of three members of the RIG-I-like Receptor (RLR) family. RLRs are cytoplasmic RNA receptors that recognize non-self RNA and act as molecular sensors to detect viral pathogens. RIG-I is activated by blunt-ended double-stranded RNA with or without a 5'-triphosphate (ppp), by single-stranded RNA marked by a 5'-ppp and by polyuridine sequences. It has been found to confer resistance to many negative-sense RNA viruses, including orthomyxoviruses, rhabdoviruses, bunyaviruses, and paramyxoviruses, as well as the positive-strand hepatitis C virus. RLRs are characterized by a central DExD/H-box helicase domain and a C-terminal domain, both of which are responsible for binding viral RNA. The helicase domain catalyzes the unwinding of double stranded RNA in an ATP-dependent manner. RIG-I and MDA5 also contain two N-terminal caspase activation and recruitment domains (CARDs), which initiate downstream signaling upon viral RNA sensing
SYKLLCGKCKTFACNSDDIRVIKESHHVVIDPSFKERYTTKPHPKPKTFDGFEKKGKIFCKKCGHDWGIM
ASYKIQNLPVLKIESFVVENPVTGQQLLFRKWKDVPFAIKEF
>gnl|CDD|276944 cd15806, LGP2_C, C-terminal domain of Laboratory of Genetics and Physiology 2 (LGP2), a cytoplasmic viral RNA receptor. Laboratory of Genetics and Physiology 2 (LGP2) is one of three members of the RIG-I-like Receptor (RLR) family. RLRs are cytoplasmic RNA receptors that recognize non-self RNA and act as molecular sensors to detect viral pathogens. They are characterized by a central DExD/H-box helicase domain and a C-terminal domain, both of which are responsible for binding viral RNA. LGP2 lacks the caspase activation and recruitment domains (CARDs) that are present in other RLRs, which initiate downstream signaling upon viral RNA sensing. LGP2 may play a regulatory role in RLR signaling, and may cooperate with either RIG-I or MDA5 to sense viral RNA
VQLLCRNCFVAVAHGSDLRKVEGTHHVNINPNFSRYYKVGGKPILIRTFEDWEPGGTISCSNCGQVWGME
MIYKSVLLPVLSIKNFVLETPEGRRQAKKWKDVPFSVEEFDF
>gnl|CDD|276945 cd15807, MDA5_C, C-terminal domain of Melanoma differentiation-associated protein 5, a cytoplasmic viral RNA receptor. Melanoma differentiation-associated protein 5 (MDA5) is also called Interferon-induced helicase C domain-containing protein 1 (IFIH1) or RIG-I-like receptor 2 (RLR-2). It is one of three members of the RLR family. RLRs are cytoplasmic RNA receptors that recognize non-self RNA and act as molecular sensors to detect viral pathogens. It has been shown to detect viruses from the Picornaviridae and Caliciviridae families. RLRs are characterized by a central DExD/H-box helicase domain and a C-terminal domain, both of which are responsible for binding viral RNA. The helicase domain catalyzes the unwinding of double stranded RNA in an ATP-dependent manner. RIG-I and MDA5 also contain two N-terminal caspase activation and recruitment domains (CARDs), which initiate downstream signaling upon viral RNA sensing
PSLITFLCKNCSVLVCSGEDIQVIEKMHHVNVTPEFKELYIKRENKALQEKLADYQTNGEIICKTCGQAW
GTMMVHKGLELPCLKIRNFVVTFKNNSTKKTYKKWVELPITFPAFDY
>gnl|CDD|293980 cd15808, SPRY_PRY_TRIM47, PRY/SPRY domain in tripartite motif-containing protein 47 (TRIM47), also known as RING finger protein 100 (RNF100) or Gene overexpressed in astrocytoma protein (GOA). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM47, also known as GOA (Gene overexpressed in astrocytoma protein) or RNF100 (RING finger protein 100). TRIM47 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is highly expressed in kidney tubular cells, but lowly expressed in most tissue. It is overexpressed in astrocytoma tumor cells and plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis; astrocytoma, also known as cerebral astrocytoma, is a malignant glioma that arises from astrocytes. Genome wide studies on white matter lesions have identified a novel locus on chromosome 17q25 harboring several genes such as TRIM47 and TRIM65 which pinpoints to possible novel mechanisms leading to these lesions
DYFLKFAFIVDLDSDTADKFLQLFGTKGVKRVLCPISYPESPTRFTHCEQVLGEGALDRGTYYWEVEIIE
GWVSVGVMAEDFSPREPYDRGRLGRNAHSCCLQWNGRNFSVWFHGLEAPLPHPFSPTVGVCLEYADRALA
FYAVRDGKVSLLRRLKASRPRRGGPPASPLDPFQSRLDSHFPGLFSHRLKPAFFLESVDAHLQIGP
>gnl|CDD|293981 cd15809, SPRY_PRY_TRIM4, PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger protein 87 (RNF87). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM4 which is also known as RING finger protein 87 (RNF87). TRIM4 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It is a positive regulator of RIG-I-mediated interferon (IFN) induction. It regulates virus-induced IFN induction and cellular antiviral innate immunity by targeting RIG-I for K63-linked poly-ubiquitination. Over-expression of TRIM4 enhances virus-triggered activation of transcription factors IRF3 and NF-kappaB, as well as IFN-beta induction. Expression of TRIM4 differs significantly in Huntington's Disease (HD) neural cells when compared with wild-type controls, possibly impacting down-regulation of the Huntingtin (HTT) gene, which is involved in the regulation of diverse cellular activities that are impaired in Huntington's Disease (HD) cells
FQVAVNLAEDTAHPKLVFSQEGRYVKNGASASSWPLFSTAWSYFTGWRNPQKTTQFVERFQHLPCVLGKN
VFTSGKHYWEVENRDSLEIAVGVCREDVMGITDGSEMSPHVGIWAICWSSAGYRPLTSSPVSPTKQEPAL
HRVGVFLDHGAGEVSFYSAVDGVHLHTFSCPLVSRLRPFFWLSPLASLVIP
>gnl|CDD|293982 cd15810, SPRY_PRY_TRIM5_6_22_34, PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and TRIM34). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of very close paralogs, TRIM5, TRIM6, TRIM22 and TRIM34. These domains are composed of RING/B-box/coiled-coil core and are also known as RBCC proteins. They form a locus of four closely related TRIM genes within an olfactory receptor-rich region on chromosome 11 of the human genome. Genetic analysis of this locus indicates that these four genes have evolved by gene duplication from a common ancestral gene. All genes in the TRIM6/TRIM34/TRIM5/TRIM22 locus are type I interferon inducible, with TRIM5 and TRIM22 possessing antiviral properties. TRIM5 promotes innate immune signaling by activating the TAK1 kinase complex by cooperating with the heterodimeric E2, UBC13/UEV1A. It also stimulates NFkB and AP-1 signaling, and the transcription of inflammatory cytokines and chemokines, amplifying these activities upon retroviral infection. Interaction of its PRY-SPRY or cyclophilin domains with the retroviral capsid lattice stimulates the formation of a complementary lattice by TRIM5, with greatly increased TRIM5 E3 activity, and host cell signal transduction. TRIM6 is selectively expressed in embryonic stem (ES) cells and interacts with the proto-oncogene product Myc, maintaining the pluripotency of the ES cells. TRIM6, together with E2 Ubiquitin conjugase (UbE2K) and K48-linked poly-Ub chains, is critical for the IkappaB kinase epsilon (IKKepsilon) branch of type I interferon (IFN-I) signaling pathway and subsequent establishment of a protective antiviral response. TRIM22 plays an integral role in the host innate immune response to viruses; it has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. Altered TRIM22 expression has also been associated with multiple sclerosis, cancer, and autoimmune disease. While the PRY-SPRY domain of TRIM5a provides specificity and the capsid recognition motif to retroviral restriction, TRIM34 binds HIV-1 capsid but does not restrict HIV-1 infection
DVTLNPVNISLNIVISEDQRQVRIVPPQTSGQALTNNNYDFGVLGSQYFSSGKHYWEVDVSKKSAWILGV
CSHKRSDAMTKSNANQINHQNVYSRYQPQYGYWVIGLQNESEYNAFEDSSSFNPHVLTLSVTVPPHRVGV
FLDYEAGTVSFFNVTNHGSLIYKFSKCCFSTTVCPYFNPWNCPVPMTLC
>gnl|CDD|293983 cd15811, SPRY_PRY_TRIM11, PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger protein 92 (RNF92). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM11, also known as RING finger protein 92 (RNF92) or BIA1. TRIM11 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It localizes to the nucleus and the cytoplasm; it is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 increases expression of dopamine beta-hydroxylase gene by interacting with the homeodomain transcription factor, PHOX2B, via the B30.2/SPRY domain, thus playing a potential role in the specification of noradrenergic (NA) neuron phenotype. It has also been shown that TRIM11 plays a critical role in the clearance of mutant PHOX2B, which causes congenital central hypoventilation syndrome, via the proteasome. TRIM11 binds a key component of the activator-mediated cofactor complex (ARC105), and destabilizes it, through the ubiquitin-proteasome system; ARC105 mediates chromatin-directed transcription activation and is a key regulatory factor for transforming growth factor beta (TGFbeta) signaling
DVTLDPDTANPELVLSEDRRSVRRGDLRQALPDSPERFDPGPCVLGRERFTSGRHYWEVEVGDRTSWALG
VCKENVNRKEKGELSAGNGFWILVFLGNYYSSERRTFAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLF
IFPETPFSGTLRPLFSPLSSSPTPMTICR
>gnl|CDD|293984 cd15812, SPRY_PRY_TRIM17, PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING finger protein (terf). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (terf). TRIM17 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein, expressed almost exclusively in the testis. It exhibits E3 ligase activity, causing protein degradation of ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates proliferation of breast cancer cells. TRIM17 undergoes ubiquitination in COS7 fibroblast-like cells but is inhibited and stabilized by TRIM44
DVVPDPSTAYPYLLLYESRQRRYLSTPPDGTPCSKDRFLAYPCAVGQETFSSGRHYWEVGMNLTGDALWA
LGVCRDNVSRKDRVPKSPENGFWVVQLSKGKKYLSAMSALTPVTLTEPPSHMGIFLDFEAGEVSFYSVND
GSHLHTYSQAAFPGPLQPFFCLGAPKSGQMVISTVT
>gnl|CDD|293985 cd15813, SPRY_PRY_TRIM20, PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM20, which is also known as pyrin or marenostrin. Unlike TRIM domains that are composed of RING/B-box/coiled-coil core, the N-terminal RING domain in TRIM20 is exchanged by a PYRIN domain (PYD), a prime mediator of protein interactions necessary for apoptosis, inflammation and innate immune signaling pathway, and it also harbors a C-terminal B30.2 domain. Mutations in pyrin (TRIM20) are associated with familial Mediterranean fever (FMF), a recessively hereditary periodic fever syndrome, characterized by episodes of inflammation and fever. These mutations cluster in the C-terminal B30.2 domain and therefore it is assumed that pyrin plays a role in the innate immune system by possibly effecting caspase-1-dependent IL-1beta maturation
LRAAQAHAVNVTLDPETAHPNLIFSDDLKSVRLGNKWDRLPDNPERFDSCIIVLGSPSFTSGRHYWEVEV
GDKTGWILGVCKASVSRKGSMTLSPENGYWVVMMTKRNEYQASTSPPTRLWLREPPRRVGIFLDYEAGDI
SFYNVTAKSHIYTFTSFSSSGPLQPIFSPGTHDGGKNMDPLTIC
>gnl|CDD|293986 cd15814, SPRY_PRY_TRIM27, PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger protein 76 (RNF76). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM27, also known as RING finger protein 76 (RNF76) or RET finger protein (RFP). TRIM27 domain is composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is highly expressed in the spleen, thymus and in cells of the hematopoietic compartment. TRIM27 exhibits either nuclear or cytosolic localization depending on the cell type. TRIM27 negatively regulates nucleotide-binding oligomerization domain containing 2 (NOD2)-mediated signaling by proteasomal degradation of NOD2, suggesting that TRIM27 could be a new target for therapeutic intervention in NOD2-associated diseases such as Crohn's. High expression of TRIM27 is observed in several human cancers, including breast and endometrial cancer, where elevated TRIM27 expression predicts poor prognosis. Also, TRIM27 forms an oncogenic fusion protein with Ret proto-oncogene. It is involved in different stages of spermatogenesis and its significant expression in male germ cells and seminomas, suggests that TRIM27 may be associated with the regulation of testicular germ cell proliferation and histological-type of germ cell tumors. TRIM27 could also be a predictive marker for chemoresistance in ovarian cancer patients. In the neurotoxin model of Parkinson's disease (PD), deficiency of TRIM27 decreases apoptosis and protects dopaminergic neurons, making TRIM27 an effective potential target during the treatment of PD
SVDVTLDPDTAYPSLILSDNLRQVRYSYLQQDLPDNPERFNLFPCVLGSPCFIAGRHYWEVEVGDKAKWT
IGVCEDSVCRKGGVTSAPQNGFWAVSLWYGKEYWALTSPMTALPLRTPLQRVGIFLDYDAGEVSFYNVTE
RCHTFTFSHATFCGPVRPYFSLSYSGGKSAAPLIICP
>gnl|CDD|293987 cd15815, SPRY_PRY_TRIM38, PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger protein 15 (RNF15). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM38, which is also known as RING finger protein 15 (RNF15) or RORET. TRIM38 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM38 has been shown to act as a suppressor in TOLL-like receptor (TLR)-mediated interferon (IFN)-beta induction by promoting degradation of TRAF6 and NAP1 through the ubiquitin-proteasome system. Another study has shown that TRIM38 may act as a novel negative regulator for TLR3-mediated IFN-beta signaling by targeting TRIF for degradation. TRIM38 has been identified as a critical negative regulator in TNFalpha- and IL-1beta-triggered activation of NF-kappaB and MAP Kinases (MAPKs); it causes degradation of two essential cellular components, TGFbeta-associated kinase 1 (TAK1)-associating chaperones 2 and 3 (TAB2/3). The degradation is promoted through a lysosomal-dependent pathway, which requires the C-terminal PRY-SPRY of TRIM38. Enterovirus 71 infection induces degradation of TRIM38, suggesting that TRIM38 may play a role in viral infections
YFDVKKMLRRHQVSVTLDPDTAHPELTLSKDQRQVTYGRCQENLDASPKRFTVLPCVLGCEGFTSGRHYF
EVDVGEGTGWDVGVCLENVQRGFGMKQEPEFGFWTIRLCEEDGYVALTSPPTPLPLREKPLVVGVFLDYE
AGLVSFYNMTTGSHIFTFPKASFSDTLRPYFQVYQYSPLFLP
>gnl|CDD|293988 cd15816, SPRY_PRY_TRIM58, PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM58, also known as BIA2. TRIM58 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins.It is implicated by genome-wide association studies (GWAS) to regulate erythrocyte traits, including cell size and number. Trim58 facilitates erythroblast enucleation by inducing proteolytic degradation of the microtubule motor dynein
DVKLDPATAHPSLLLTADLRSVQDGELWRDVPGNPERFDTWPCVLGLQSFSSGRHYWEVAVGEKAEWGLG
VCQDSAPRKGETTPSPENGVWAVWLLKGNEYMVLASPSVPLLQLRRPRRVGVFLDYEAGEISFYNVTAGS
HIYTFRQLFSGILRPYFFVCDTTPLTLP
>gnl|CDD|293989 cd15817, SPRY_PRY_TRIM60_75, PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM60 and TRIM75, both composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM60 domain is also known as RING finger protein 33 (RNF33) or 129 (RNF129). Based on its expression profile, RNF33 likely plays an important role in the spermatogenesis process, the development of the pre-implantation embryo, and in testicular functions; Rnf33 is temporally transcribed in the unfertilized egg and the pre-implantation embryo, and is permanently silenced before the blastocyst stage. Mice experiments have shown that RNF33 associates with the cytoplasmic motor proteins, kinesin-2 family members 3A (KIF3A) and 3B (KIF3B), suggesting possible contribution to cargo movement along the microtubule in the expressed sites. TRIM75, also known as Gm794, has a single site of positive selection in its RING domain associated with E3 ubiquitin ligase activity. It has not been detectably expressed experimentally due to their constant turnover by the proteasome, and therefore not been characterized
DLILDPETAHPNLIVSEDRKAVRYRRMKPNCPYDPRRFTVYPAVLGSEGFDSGRHFWEVEVGGKGEWILG
VCKDSLPRNAQDPPSPLGGCWQIGRYMSGYVASGPKTTQLLPVVKPSRIGIFLDYELGEVSFYNMNDRSH
LYTFTDTFTGKLIPYFYVGPDSEPLTIC
>gnl|CDD|293990 cd15818, SPRY_PRY_TRIM69, PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger protein 36 (RNF36). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM69, which is also known as RING finger protein 36 (RNF36) or testis-specific ring finger (Trif). TRIM69 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. The mouse ortholog of this gene is specifically expressed in germ cells at the round spermatid stages during spermatogenesis and, when overexpressed, induces apoptosis. TRIM69 has been shown to be a novel regulator of mitotic spindle assembly in tumor cells; it associates with spindle poles and promotes centrosomal clustering, and is therefore essential for formation of a bipolar spindle
WKEMKSILNPGLSLITLDPKTAHPNLILSEDLTCVWHGDTKQMLPDNPERFDSSVAVLGSEGFTSGKHYW
EVEVAKKTKWTLGVVRESINRKGNCPLSPEDGFWLLRLRNQNELKALDVPSFSLTLTSNLNKVGIYLDYE
GGQVSFYNANTMSHIYTFSDTFTEKIYPYFCPCLNDSGENKEPLKIL
>gnl|CDD|293991 cd15819, SPRY_PRY_BTN1_2, butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of butyrophilin family 1A and 2A (BTN1A and BTN2A). BTNs belong to receptor glycoproteins of immunoglobulin (Ig) superfamily, characterized by the presence of extracellular Ig-like domains (IgV and/or IgC). BTN1A plays a role in the secretion, formation and stabilization of milk fat globules. The B30.2 domain of BTN1A1 binds the enzyme xanthine oxidoreductase (XOR) in order to participate in milk fat globule secretion; this interaction may lead to the production of reactive oxygen species, which have immunomodulatory and antimicrobial functions. Duplication events have led to three paralogs of BTN2A in primates: BTN2A1, BTN2A2, and BTN2A3. In humans, only BTN2A1 has been functionally characterized; it has been detected on epithelial cells and leukocytes, and identified as a novel ligand of dendritic cell-specific ICAM-3 grabbing nonintegrin (DCSIGN), a C-type lectin receptor that acts as an internalization receptor for HIV-1, HCV, and other pathogens. BTN2A2 mRNA has been shown to be expressed in circulating human immune cells
AVNVTLDPDTAHPALILSEDGRSVTWGETRQDLPENPERFDSLPCVLGQEGFTSGRHYWEVEVGDRTSWD
LGVCRDNVMRKGRVTLSPENGFWAIRLYGNEYWALTSPETPLTLKEPPRRVGIFLDYEAGDVSFYNMTDG
SHIYTFPQTAFSGPLRPFFRLWSSDSGPLTIC
>gnl|CDD|293992 cd15820, SPRY_PRY_BTN3, PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like 3 (BTNL3); BTN3A also known as CD277. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of butyrophilin family 3A (BTN3A); duplication events have led to three paralogs in primates: BTN3A1, BTN3A2, and BTN3A3. BTNs belong to receptor glycoproteins of immunoglobulin (Ig) superfamily, characterized by the presence of extracellular Ig-like domains (IgV and/or IgC). BTN3 transcripts are ubiquitously present in all immune cells (T cells, B cells, NK cells, monocytes, dendritic cells, and hematopoietic precursors) with different expression levels; BTN3A1 and BTN3A2 are expressed mainly by CD4+ and CD8+ T cells, BTN3A2 is the major form expressed in NK cells, and BTN3A3 is poorly expressed in these immune cells. The PRY/SPRY domain of the BTN3A1 isoform mediates phosphoantigen (pAg)-induced activation by binding directly to the pAg
FQPADVILDPDTANPILLISEDQRSLQWADEPQNLPDNPKRFDWHYCVLGCKSFTSGRHFWEVEVGDRKE
WYVGVCRENVERKLWVKMAPENGFWTIGLSDGNDYQALTDPRTKLTIANPPQRVGVFLDYETGEVSFYNA
MDGSHIYTFPHTSFSGPLYPVFRLLSWDPTALTICP
>gnl|CDD|293993 cd15821, SPRY_PRY_RFPL, Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of RFPL protein family, which includes RFPL1, RFPL2, RFPL3 and RFPL4. In humans, RFPL transcripts can be detected at the onset of neurogenesis in differentiating human embryonic stem cells, and in the developing human neocortex. The human RFPL1, 2, 3 genes have a role in neocortex development. RFPL1 is a primate-specific target gene of Pax6, a key transcription factor for pancreas, eye and neocortex development; human RFPL1 decreases cell number through its RFPL-defining motif (RDM) and SPRY domains. The RFPL4 (also known as RFPL4A) gene encodes a putative E3 ubiquitin-protein ligase expressed in adult germ cells and interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway
KFQVDMTLDVDTANNYLIISEDLRSVRCGCFRQNRKELAERFDDALCVLGSPRFTSGRHYWEVDVGTSTE
WDLGVCRESVNRQGPIELSPEHGFWTVSLRDGSVFFASTVPLTVLWVNPRLHRVGIFLDMEMGTISFYDV
SDGSHIFTFTKISAEEPLRPFFAPANPYGDDQGVLSIC
>gnl|CDD|293994 cd15822, SPRY_PRY_TRIM5, PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger protein 88 (RNF88). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM5 which is also known as RING finger protein 88 (RNF88) or TRIM5alpha (TRIM5a), an antiretroviral restriction factor and a retrovirus capsid sensor in immune signaling. TRIM5 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It blocks retrovirus infection soon after the virion core enters the cell cytoplasm by recognizing the capsid protein lattice that encases the viral genomic RNA; the SPRY domain provides the capsid recognition motif that dictates specificity to retroviral restriction. TRIM5a, an E3 ubiquitin ligase, promotes innate immune signaling by activating the TAK1 kinase complex by cooperating with the heterodimeric E2, UBC13/UEV1A. It also stimulates NFkB and AP-1 signaling, and the transcription of inflammatory cytokines and chemokines, and amplifies these activities upon retroviral infection. Interaction of its PRY-SPRY or cyclophilin domains with the retroviral capsid lattice stimulates the formation of a complementary lattice by TRIM5, with greatly increased TRIM5 E3 activity, and host cell signal transduction
FNELTDVQRYWVHVTLDPSNNKNIVISEDRRQVRYVRKQQRYNSNGNNEDYGVLGSPSITSGKHYWEVDV
SKKRAWILGVCGGKYPNSTLKDFNKQGKNNQKQCSNYQPKYGYWVIGLQNKSEYNAFEDSSSSDPLILTL
SLTVPPCRVGVFLDYEAGTVSFFNVTNHGFLIYKFSSCSFSQEVFPYFNPMKCPVPMTLC
>gnl|CDD|293995 cd15823, SPRY_PRY_TRIM6, PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger protein 89 (RNF89). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM6, also known as RING finger protein 89 (RNF89). TRIM6 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It is selectively expressed in embryonic stem (ES) cells and interacts with the proto-oncogene product Myc, maintaining the pluripotency of the ES cells. TRIM6, together with E2 Ubiquitin conjugase (UbE2K) and K48-linked poly-Ub chains, is critical for the IkappaB kinase epsilon (IKKepsilon) branch of type I interferon (IFN-I) signaling pathway and subsequent establishment of a protective antiviral response
YWVDVTLNPHTANLNLVLSKNRRQVRFVGAKLSGPSYLEEHYDCSVLGSQHFSSGKHYWEVDVTKKTAWI
LGVCSHSLGPTFSFNQYAQNHNAYSRYQPQSGYWVIGLQHNHEYRAYEDSSTSLLLSMTVPPRRVGVFLD
YEAGTVSFYNVTNHGFPIYTFSKYYFPTTLCPYFNPCNCVVPMTLRRP
>gnl|CDD|293996 cd15824, SPRY_PRY_TRIM22, PRY/SPRY domain in tripartite motif-containing protein 22 (TRIM22), also known as RING finger protein 94 (RNF94) or Stimulated trans-acting factor of 50 kDa (STAF50). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM22, also known as RING finger protein 94 (RNF94) or STAF50 (Stimulated trans-acting factor of 50 kDa). TRIM6 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. TRIM22 is an interferon-induced protein, predominantly expressed in peripheral blood leukocytes, in lymphoid tissue such as spleen and thymus, and in the ovary.TRIM22 plays an integral role in the host innate immune response to viruses; it has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 inhibits influenza A virus (IAV) infection by targeting the viral nucleoprotein for degradation; it represents a novel restriction factor up-regulated upon IAV infection that curtails its replicative capacity in epithelial cells. Altered TRIM22 expression has also been associated with multiple sclerosis, cancer, and autoimmune disease. A large number of high-risk non-synonymous (ns)SNPs have been identified in the highly polymorphic TRIM22 gene, most of which are located in the SPRY domain and could possibly alter critical regions of the SPRY structural and functional residues, including several sites that undergo post-translational modification. TRIM22 is a direct p53 target gene and inhibits the clonogenic growth of leukemic cells. Its expression in Wilms tumors is negatively associated with disease relapse. It is greatly under-expressed in breast cancer cells as compared to non-malignant cell lines; p53 dysfunction may be one of the mechanisms for its down-regulation
YWVDVMLNPVNAVSNVVVSADQRQVTVVHICMFRNSNPCDFSAFDVLGCQYFSSGKYYWEVDVSGKIAWI
LGVYSKRNNLNKRKSSGFAFDPNVNHPNVYSRYRPQNGYWVIGLQNESEYNAFEDSSSSDPKVLTLSMAV
PPHRVGVFLDYEAGTVSFFNVTNHGSLIYKFSKCCFSQPVYPYFNPWNCPAPMTLCPP
>gnl|CDD|293997 cd15825, SPRY_PRY_TRIM34, PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM34, also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1). TRIM34 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. The TRIM21 cDNA possesses at least three kinds of isoforms, due to alternative splicing, of which only the long and medium forms contain the SPRY domain. It is an interferon-induced protein, predominantly expressed in the testis, kidney, and ovary. The SPRY domain provides the capsid recognition motif that dictates specificity to retroviral restriction. While the PRY-SPRY domain provides specificity and the capsid recognition motif to retroviral restriction, TRIM34 binds HIV-1 capsid but does not restrict HIV-1 infection
WVDFTLNPVNLNLNLVLSEDQRQVTSVPIWPFKCYNYGILGSQYFSSGKHYWEVDVSKKTAWILGVYCRK
RSRTFKYVRQGKNHPNVYSRYRPQYGYWVIGLQNKSEYYAFEDSSTSDPKVLTLSVATPPHRVGVFLDYE
AGTVSFFNVTNHGSLIYKFSKCCFSQPVYPYFNPWNCPAPMTLCP
>gnl|CDD|293998 cd15826, SPRY_PRY_TRIM15, PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 15 (TRIM15), also referred to as RING finger protein 93 (RNF93) or Zinc finger protein B7 or 178 (ZNFB7 or ZNF178). TRIM15 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. The PRY and SPRY/B30.2 domains can function as immune defense components and in pathogen sensing. TRIM15 has been shown to regulate inflammatory and innate immune signaling, in addition to displaying antiviral activities. Down-regulation of TRIM15, as well as TRIM11, enhances virus release, suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. TRIM15 is also a regulatory component of focal adhesion turnover and cell migration
SVTLDPQTASGSLVLSEDRKSVRYTRQKQNLPDSPLRFDGLPAVLGSPGFSSGRHRWQVEVQLGDGGGCT
VGVAGESVRRKGEMGLSAEDGVWAVILSHQQCWASTSPGTDLPLSEIPRRVGVALDYEAGTVTLTNAETQ
EPIFTFTASFSGKVFPFFAVWKKGSRLTLK
>gnl|CDD|293999 cd15827, SPRY_PRY_TRIM10, PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic RING finger 1 (HERF1). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM10, also known as RING finger protein 9 (RNF9) or hematopoietic RING finger 1 (HERF1). TRIM10 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. TRIM10/HERF1 is predominantly expressed during definitive erythropoiesis and in embryonic liver, and minimally expressed in adult liver, kidney, and colon. It is critical for erythroid cell differentiation and its down-regulation leads to cell death; inhibition of TRIM10 expression blocks terminal erythroid differentiation, while its over-expression in erythroid cells induces beta-major globin expression and erythroid differentiation
PAHISLDPQTSHPKLLLSEDHQRARFSYKWQNSPDNPQRFDRATCVLAHDGFTGGRHTWVVSVDLAHGGS
CTVGVVSEDVRRKGELRLRPEEGVWAVRLAWGFVSALGSFPTRLALEEQPRQVRVSLDYEVGWVTFVNAV
TQEPIYTFTASFTQKVFPFFGLWGRGSSFSLS
>gnl|CDD|294000 cd15828, SPRY_PRY_TRIM60, PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger protein 33 (RNF33). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM60, which is also known as RING finger protein 33 (RNF33) or 129 (RNF129). TRIM60 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. Based on its expression profile, RNF33 likely plays an important role in the spermatogenesis process, the development of the pre-implantation embryo, and in testicular functions; Rnf33 is temporally transcribed in the unfertilized egg and the pre-implantation embryo, and is permanently silenced before the blastocyst stage. Mice experiments have shown that RNF33 associates with the cytoplasmic motor proteins, kinesin-2 family members 3A (KIF3A) and 3B (KIF3B), suggesting possible contribution to cargo movement along the microtubule in the expressed sites
LDRIIKRFQVDVTLDPETAHPQLTVSEDRKSVLYGEMKQNVCYNPRRFYLCPAVLGSEGFHSGRQYWEVE
VGDKPEWTLGVCQDCLPRNWSNQPSVQDGLWAIGRYSESNYVALGPKKIQLLPKVRPSKIGIFLDYELGE
VSFYNMNDRSLLYTFSDSFTGTLWPYFYTGTDSEPLKICT
>gnl|CDD|294001 cd15829, SPRY_PRY_TRIM75, PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75). This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM75, also known as Gm794. TRIM75 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM75 has a single site of positive selection in its RING domain associated with E3 ubiquitin ligase activity. It has not been detectably expressed experimentally due to their constant turnover by the proteasome, and therefore not been characterized
CSFPPQYSALQKIIKKFRVDVTLDPETAHPNLLVSEDKKCVTFTKKKQRVPDSPKRFTVNPVVLGFPGFH
SGRHFWEVEVGDKPEWAVGVCKDSLSTKARRPPSGQQGCWRIQLQGGDYDAPGAVPPPLLLEVKPRGIGV
FLDYELGEISFYNMPEKSHIHTFTDTFSGPLRPYFYVGPDSKPLRIC
>gnl|CDD|276939 cd15830, BamD, BamD lipoprotein, a component of the beta-barrel assembly machinery. BamD, also called YfiO, is part of the beta-barrel assembly machinery (BAM), which is essential for the folding and insertion of outer membrane proteins (OMPs) in the OM of Gram-negative bacteria. Transmembrane OMPs carry out important functions including nutrient and waste management, cell adhesion, and structural roles. The BAM complex is composed of the beta-barrel OMP BamA (also called Omp85/YaeT) and four lipoproteins BamBCDE. BamD is the only BAM lipoprotein required for viability. Both BamA and BamD are broadly distributed in Gram-negative bacteria, and may constitute the core of the BAM complex. BamD contains five Tetratricopeptide repeats (TPRs). The three TPRs at the N-terminus may participate in interaction with substrates, while the two TPRs in the C-terminus may be involved in binding with other BAM components
MPAQELYEKAQTALQKGNYDGAIKYLEALDSRYPFGPYAEQAQLDLIYAYYKNADYELALASAERFIRLY
PRHPNIDYVYYMRGLSNYKLDRSFLQRFFPIDRSDRDQSYAREAFQDFKDLIQRYPNSEYATDAKQRMIY
LRNRLAEHELSIARYYLKRGAYIAAINRAEEVLENYPDTPATEEALARLEEAYLALGLTDLAEKYRKVLG
LNY
>gnl|CDD|276938 cd15831, BTAD, Bacterial Transcriptional Activation (BTA) domain. The Bacterial Transcriptional Activation (BTA) domain is present in the putative transcriptional regulator Mycobacterium EmbR and the related Streptomyces antibiotic regulatory protein (SARP) family of transcription factors, which includes DnrI and AfsR, among others. Members of this family contain an N-terminal DNA-binding domain, followed by the BTA domain, and many have diverse domains at the C-terminus. EmbR contains an C-terminal forkhead-associated (FHA) domain, which mediates binding to threonine-phosphorylated sites in a sequence-specific manner. The BTA domain of EmbR contains three Tetratricopeptide repeats (TPRs) and two C-terminal helices. The TPR motif typically contains 34 amino acids, and 5 or 6 tandem repeats of the motif generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein
VDLQRFERLVAEGRRALAAGDPEEAARLLRAALALWRGPALADVRAGPVLEAEAARLEELRLRALEARIE
ADLALGRHRELVAELRALVAEHPLRERLHRQLMLALYRSGRQAEALRVYRRLRRRLAEELGVEPGPELRR
LHQAIL
>gnl|CDD|276937 cd15832, SNAP, Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family. Members of the soluble NSF attachment protein (SNAP) family are involved in intracellular membrane trafficking, including vesicular transport between the endoplasmic reticulum and Golgi apparatus. Higher eukaryotes contain three isoforms of SNAPs: alpha, beta, and gamma. Alpha-SNAP is universally present in eukaryotes and acts as an adaptor protein between SNARE (integral membrane SNAP receptor) and NSF for recruitment to the 20S complex. Beta-SNAP is brain-specific and shares high sequence identity (about 85%) with alpha-SNAP. Gamma-SNAP is weakly related (about 20-25% identity) to the two other isoforms, and is ubiquitous. It may help regulate the activity of the 20S complex. The X-ray structures of vertebrate gamma-SNAP and yeast Sec17, a SNAP family member, show similar all-helical structures consisting of an N-terminal extended twisted sheet of four Tetratricopeptide repeat (TPR)-like helical hairpins and a C-terminal helical bundle
KAEELMAKAEKKLKGSGGFFFGSGGSKYEEAAELYEKAANAFKLAKNWEEAGDAFLKAAECQLKLDSKHD
AANAYVEAAKCYKKVDPQEAVNCLEKAIEIYTEMGRFRQAAKHLKEIAELYENELGDLDKAIEAYEQAAD
YYEGEGANSLANKCYLKVADLAAQLEDYDKAIEIYEQVARSSLENNLLKYSAKDYFLKAGLCHLAAGDVV
AAQRALEKYAELDPSFAGSRECKLLEDLLEAVEEGDVEAFTDAVKEYDSISKLDKWKTTMLLKIKKSI
>gnl|CDD|276930 cd15834, TNFRSF1A_teleost, Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) in teleosts; also known as TNFR1. This subfamily of TNFRSF1 ((also known as type I TNFR, TNFR1, DR1, TNFRSF1A, CD120a, p55) is found in teleosts. It binds TNF-alpha, through the death domain (DD), and activates NF-kappaB, mediates apoptosis and activates signaling pathways controlling inflammatory, immune, and stress responses. It mediates signal transduction by interacting with antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRAF2 and TRADD that play regulatory roles. The human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS), or periodic fever syndrome, is associated with germline mutations of the extracellular domains of this receptor, possibly due to impaired receptor clearance. Serum levels of TNFRSF1A are elevated in schizophrenia and bipolar disorder, and high levels are also associated with cognitive impairment and dementia. Knockout studies in zebrafish embryos have shown that a signaling balance between TNFRSF1A and TNFRSF1B is required for endothelial cell integrity. TNFRSF1A signals apoptosis through caspase-8, whereas TNFRSF1B signals survival via NF-kappaB in endothelial cells. Thus, this apoptotic pathway seems to be evolutionarily conserved, as TNFalpha promotes apoptosis of human endothelial cells and triggers caspase-2 and P53 activation in these cells via TNFRSF1A
CLDSEYLSENGICCNKCHPGYKLKEECTAPGERSQCTPCPEGTYLEQINYSPNCRRCTLCKVKNEEEVSP
CKKSSNTVCRCKKGYYKSRIDSETRECLKCKTCGPGEIEIQPCTPESNTVCECKDNYYRNNNKCKPCQKC
SLDCQHLCTT
>gnl|CDD|276931 cd15835, TNFRSF1B_teleost, Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B) in teleost; also known as TNFR2. This subfamily of TNFRSF1B (also known as TNFR2, type 2 TNFR, TNFBR, TNFR80, TNF-R75, TNF-R-II, p75, CD120b) is found in teleosts. It binds TNF-alpha, but lacks the death domain (DD) that is associated with the cytoplasmic domain of TNFRSF1A (TNFR1). It is inducible and expressed exclusively by oligodendrocytes, astrocytes, T cells, thymocytes, myocytes, endothelial cells, and in human mesenchymal stem cells. TNFRSF1B protects oligodendrocyte progenitor cells (OLGs) against oxidative stress, and induces the up-regulation of cell survival genes. While pro-inflammatory and pathogen-clearing activities of TNF are mediated mainly through activation of TNFRSF1A, a strong activator of NF-kappaB, TNFRSF1B is more responsible for suppression of inflammation. Although the affinities of both receptors for soluble TNF are similar, TNFRSF1B is sometimes more abundantly expressed and thought to associate with TNF, thereby increasing its concentration near TNFRSF1A receptors, and making TNF available to activate TNFRSF1A (a ligand-passing mechanism). Knockout studies in zebrafish embryos have shown that a signaling balance between TNFRSF1A and TNFRSF1B is required for endothelial cell integrity. TNFRSF1A signals apoptosis through caspase-8, whereas TNFRSF1B signals survival via NF-kB in endothelial cells. In goldfish (Carassius aurutus L.), TNFRSF1B expression is substantially higher than that of TNFRSF1 in tissues and various immune cell types. Both receptors are most robustly expressed in monocytes; mRNA levels of TNFRSF1B are lowest in peripheral blood leukocytes
SDGNCRNTTTEYYNDGSNLCCSKCRPGTRLKTKCSETSDTVCEPCPSGQYSENWNYYPNCFSCPKCKERK
GLQYAQNCSSTTNAVCVCKPGMYCIMGFDHPSCSECKKYRTCKPGYGVSVPGTPTSDVKC
>gnl|CDD|276932 cd15836, TNFRSF11A_teleost, Tumor necrosis factor receptor superfamily member 11A (TNFRSF11A) in teleost; also known as RANK. TNFRSF11A (also known as RANK, FEO, OFE, ODFR, OSTS, PDB2, CD26, OPTB7, TRANCER, LOH18CR1) induces the activation of NF-kappa B and MAPK8/JNK through interactions with various TRAF adaptor proteins. This receptor and its ligand are important regulators of the interaction between T cells and dendritic cells. This receptor is also an essential mediator for osteoclast and lymph node development. Mutations at this locus have been associated with familial expansile osteolysis, autosomal recessive osteopetrosis, and Juvenile Paget's disease (JPD) of bone. Alternatively spliced transcript variants have been described for this locus. Mutation analysis may improve diagnosis, prognostication, recurrence risk assessment, and perhaps treatment selection among the monogenic disorders of RANKL/OPG/RANK activation
SPTCNQTQYLKDGKCCRKCEPGSFVFAHCSGSSDTICRDCGRNEYQPDWTSEMKCIPQKFCDEGKGFNRT
RPHNPTALEPCQCKPGFQCSPLNCEFCEKIPTCPPGYGLEGEENGRKICVPC
>gnl|CDD|276933 cd15837, TNFRSF26, Tumor necrosis factor receptor superfamily member 26 (TNFRSF26), also known as tumor necrosis factor receptor homolog 3 (TNFRH3). TNFRSF26 (also known as tumor necrosis factor receptor homolog 3 (TNFRH3) or TNFRSF24) is predominantly expressed in embryos and lymphoid cell types, along with its closely related TNFRSF22 and TNFRSF23 orthologs, and is developmentally regulated. Unlike TNFRSF22/23, TNFRSF26 does not serve as a TRAIL decoy receptor; it remains an orphan receptor
CGPGEYKSANLCCQLCPAGHYVSEPCQENHGVGECAPCEPGTFTAHPNGETSCFPCSQCRDDQEVVAECS
ATSDRQCQCKQGHFYCDENCLESCFRCSRCPGGRVVLQPCNATRDTVC
>gnl|CDD|276934 cd15838, TNFRSF27, Tumor necrosis factor receptor superfamily member 27 (TNFRSF27), also known as ectodysplasin A2 receptor (EDA2R) or X-linked ectodermal dysplasia receptor (XEDAR). TNFRSF27 (also known as ectodysplasin A2 receptor (EDA2R), X-linked ectodermal dysplasia receptor (XEDAR), EDAA2R, EDA-A2R) has two isoforms, EDA-A1 and EDA-A2, that are encoded by the anhidrotic ectodermal dysplasia (EDA) gene. It is highly expressed during embryonic development and binds to ectodysplasin-A2 (EDA-A2), playing a crucial role in the p53-signaling pathway. EDA2R is a direct p53 target that is frequently down-regulated in colorectal cancer tissues due to its epigenetic alterations or through the p53 gene mutations. Mutations in the EDA-A2/XEDAR signaling give rise to ectodermal dysplasia, characterized by loss of hair, sweat glands, and teeth. A non-synonymous SNP on EDA2R, along with genetic variants in human androgen receptor is associated with androgenetic alopecia (AGA)
CQEKEYLDEHGKCVPCRECGPGQELSKDCGYGEGGDAYCTACPPRRFKDSWGHHGCKTCLSCALINRVQK
SNCTATSNAVCGDCLPGFYRKTRIGGLQDQECIPCTKQTPSSEVQC
>gnl|CDD|276935 cd15839, TNFRSF_viral, Tumor necrosis factor receptor superfamily members, virus-encoded. This family contains viral TNFR homologs that include vaccinia virus (VACV) cytokine response modifier E (CrmE), an encoded TNFR that shares significant sequence similarity with mammalian type 2 TNF receptors (TNFSFR1B, p75, TNFR type 2), a cowpox virus encoded cytokine-response modifier B (crmB), which is a secreted form of TNF receptor that can contribute to the modification of TNF-mediated antiviral processes, and a myxoma virus (MYXV) T2 (M-T2) protein that binds and inhibits rabbit TNF-alpha. The CrmE structure confirms that the canonical TNFR fold is adopted, but only one of the two "ligand-binding" loops of TNFRSF1A is conserved, suggesting a mechanism for the higher affinity of poxvirus TNFRs for TNFalpha over lymphotoxin-alpha. CrmB protein specifically binds TNF-alpha and TNF-beta indicating that cowpox virus seeks to invade antiviral processes mediated by TNF. Intracellular M-T2 blocks virus-induced lymphocyte apoptosis via a highly conserved viral preligand assembly domain (vPLAD), which controls receptor signaling competency prior to ligand binding
CNGNDYNSNSNNLCCKSCPPGTYASHLCDTTSNTKCDPCPSDTFTSIPNHIPACLSCRGRCSSNQVETKS
CSNTQNRICSCAPGYYCLLKGSDGCVACAPKTKCGVGYGVSGHTSTGDVICKKCP
>gnl|CDD|277193 cd15840, SNARE_Qa, SNARE motif, subgroup Qa. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qa SNAREs are syntaxin 18, syntaxin 5, syntaxin 16, and syntaxin 1
IEEREEEIREIESSIGEVNEIFKDLATLVTEQGEQIDNIENNIEEAAANTEEANKELRK
>gnl|CDD|277194 cd15841, SNARE_Qc, SNARE motif, subgroup Qc. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qc SNAREs are C-terminal domains of SNAP23 and SNAP25, syntaxin 8, syntaxin 6, and Bet1
MKEQDEQLDELSGSVGRLKNIALAINEELDLQNRLLDDLDEDVDKTQSRLKKVNKKLKK
>gnl|CDD|277195 cd15842, SNARE_Qb, SNARE motif, subgroup Qb. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27
DQLSDQSTESLRRSHRGMEELKQAGIETLEMLDEQREQLERTEERINSINGDIKLSRKILRK
>gnl|CDD|277196 cd15843, R-SNARE, SNARE motif, subgroup R-SNARE. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). In contrast to Qa-, Qb- and Qc-SNAREs that are localized to target organelle membranes, R-SNAREs are localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qa SNAREs are syntaxin 18, syntaxin 5, syntaxin 16, and syntaxin 1
DKLSKVQEQVDEVKDVMQENIDKVLERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW
>gnl|CDD|277197 cd15844, SNARE_syntaxin5, SNARE motif of syntaxin 5. Syntaxin 5 (Syn5) regulates the transport from the ER to the Golgi, as well as the early/recycling endosomes to the trans-Golgi network and participates in the assembly of transitional ER and the Golgi, lipid droplet fusion, and cytokinesis. Syn5 exists in 2 isoforms, long (42 kDa) and short (35 kDa). The short form is localized in the Golgi complex, whereas the long form is additionally found in the endoplasmic reticulum (ER). The syntaxin-5 SNARE complexes, which also contain Bet1 (Qc) and either GS27 (Qb) and Sec22B (R-SNARE) or GS28 (Qb) and Ykt6 (R-SNARE), regulate the early secretory pathway of eukaryotic cells at the level of endoplasmic reticulum (ER) to Golgi transport. The syntaxin-5 SNARE complex, which also contains GS15 (Qc), GS28 (Qb) and Ykt6 (R-SNAREs) is involved in the transport from the trans-Golgi network to the cis-Golgi. Syn5 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
LQSRADAVQNIESTIVELGQIFQQLATMVAEQGEMVQRIDENVEDALANVEAAHSELLKYYRSISSNRWL
ILKIFGVLIVFIVIFV
>gnl|CDD|277198 cd15845, SNARE_syntaxin16, SNARE motif of syntaxin 16. Syntaxin 16 is located in trans-Golgi network (TGN) and regulated by the SM protein Vps45p. It forms a complex with syntaxin 6 (Qc), Vti1a (Qb) and VAMP4 (R-SNARE) and is involved in the regulation of recycling of early endosomes to the trans-Golgi network (TGN). Syntaxin 16 is a member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
IQERDREIAKIVESINELAEIFKDLATLVIEQGTILDRIDYNIEQTATRVEKGVKELKK
>gnl|CDD|277199 cd15846, SNARE_syntaxin17, SNARE motif of syntaxin 17. Synthaxin 17 (STX17) belongs to the Qa subgroup of SNAREs and interacts with SNAP29 (Qb/Qc) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials, including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
LPQRQACLESWETLQQDLEDLHGLFTDFHQLVHDQGEQVDTIEDNVEEALENVQEGTKNLRK
>gnl|CDD|277200 cd15847, SNARE_syntaxin7_like, SNARE motif of syntaxin 7, 12 and related sequences. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. This subgroup of the Qa SNAREs includes syntaxin 7, syntaxin 12, TSNARE1 and related proteins
LLEREERIRQIESDILDVNQIFKDLATLVHEQGETIDSIEANIESAYVNVESGNSQLAKA
>gnl|CDD|277201 cd15848, SNARE_syntaxin1-like, SNARE motif of syntaxin 1 and related proteins. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. This subgroup of the Qa SNAREs includes syntaxin 1, syntaxin 11, syntaxin 19, syntaxin 2, syntaxin 3, syntaxin 4 and related proteins
ALADIEERHQDILKLEKSIRELHQMFLDMAVLVESQGELIDNIEYNVEKAKDYVEKGNEELKK
>gnl|CDD|277202 cd15849, SNARE_Sso1, SNARE motif of Sso1. Saccharomyces cerevisiae SNARE protein Sso1p forms a complex with synaptobrevin homolog Snc1p (R-SNARE) and the SNAP-25 homolog Sec9p (Qb/c) which is involved in exocytosis. Sso1 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
LGEVQARHNEIQRIEQTLTELAQLFNDMATLVEQQDEVIQQIEQNAEEVETDLEKGNVHLEKAV
>gnl|CDD|277203 cd15850, SNARE_syntaxin18, SNARE motif, subgroup Qa. Syntaxin18 (also known as Ufe1p) is involved in retrograde transport of CopI coatomer coated vesicles from the Golgi to the ER. It forms a complex with USE1 (SLT1, Qc), Bnip1 (Sec20p, Qb) and Sec22b (R-SNARE). Syntaxin18 is a member of the Qa subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family. SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
KNSQLDKVRQIEKTVVEIASLQEEFAEKLLVQEQNIDSLLDLVVDTTENVKKGNEELRK
>gnl|CDD|277204 cd15851, SNARE_Syntaxin6, SNARE motif of syntaxin 6. Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and VAMP4 (R-SNARE) and is involved in the regulation of recycling of early endosomes to the trans-Golgi network (TGN). Syntaxin 6 and its yeast homolog TLG1 are members of the Qc subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
MREQDEQLDGVGGTVGNLREQAQLIGDELEEQAELLDDLDHEVDRTESRLDRGMKKMAKVIRKNED
>gnl|CDD|277205 cd15852, SNARE_Syntaxin8, SNARE motif of syntaxin 8. Syntaxin 8 forms a complex with syntaxin 7 (Qa), Vti1b (Qb) and either VAMP7 or VAMP8 (R-SNARE) and is involved in the transport from early endosomes to the lysosome. Syntaxin 8 is a member of the Qc subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
IQEQDQGLDALSSIISRQKQIGQAIGDEVDDQNEIIDDLADGMDRTDARLRRETRHVGI
>gnl|CDD|277206 cd15853, SNARE_Bet1, SNARE motif of Bet1. Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B (R-SNARE) or GS28 (Qb), syntaxin-5 (Qa) and Ykt6 (R-SNARE). These complexes regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) and from ERGIC to the cis-Golgi, respectively. Bet1 is a member of the Qc subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
ESQNDRRLDELSSKVSALKSLTIDIGDEVRDQNKLLDGMGDDFDSTGGLLGGTMKRLKR
>gnl|CDD|277207 cd15854, SNARE_SNAP47C, C-terminal SNARE motif of SNAP47. C-terminal SNARE motif of SNAP47, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. The exact funtion of SNAP47 is unknown. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP29 and SEC9
PIVSEAETQELKQILRKLKSLALEAETELERQDEALDVLSDSVDRATLNIDKHNRRMKK
>gnl|CDD|277208 cd15855, SNARE_SNAP25C_23C, C-terminal SNARE motif of SNAP25 and SNAP23. C-terminal SNARE motifs of SNAP25 and SNAP23, members of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with STX4 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP29, SNAP47 and SEC9
EDEMDENLQQVSGILGNLRHMALDMGNEIDTQNRQLDRIDEKADSNKTRIEAANDRATK
>gnl|CDD|277209 cd15856, SNARE_SNAP29C, C-terminal SNARE motif of SNAP29. C-terminal SNARE motif of SNAP29, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP29 interacts with STX17 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SEC9
DQQLDENLDEMSSGLSRLKGLALGLGTEIDSQNDLLDRITDKADKADIKIKKQNKQMNK
>gnl|CDD|277210 cd15857, SNARE_SEC9C, C-terminal SNARE motif of SEC9. C-terminal SNARE motif of fungal SEC9, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SEC9 interacts with Sso1(Qa) and the lysosomal R-SNARE Snc1. The complex plays a role in post-Golgi transport. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SNAP29
EDEIDDNLDEIGGVVGRLKALAMAMGEEVDSQNKRLDRIEEKTDRLDDKVHMNTERLKR
>gnl|CDD|277211 cd15858, SNARE_VAM7, SNARE motif of VAM7. Fungal VAM7 (vacuolar morphogenesis protein 7) is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family involved in vacuolar protein transport and membrane fusion. SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
MQEQDQQLEQLRKIVQRQKELGLAINQELEEQNELLDELDEDVDRTGGKLRVANKRAKR
>gnl|CDD|277212 cd15859, SNARE_SYN8, SNARE motif of SYN8. Fungal SYN8 is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family presetn in the endosomes. SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
LLEQDEHLDHLSASIRRQHELSLQINDELDEQNELLDDLENGVDRTGRRLNRARRRLDKFRRKARENG
>gnl|CDD|277213 cd15860, SNARE_USE1, SNARE motif of USE1. USE1 (unconventional SNARE in the ER 1 homolog, also known as SNARE-like tail-anchored protein 1 or SLT1) is involved in retrograde transport of CopI coatomer coated vesicles from the Golgi to the ER. It forms a complex with syntaxin18 (Ufe1p, Qa), Bnip1 (Sec20p, Qb) and Sec22b (R-SNARE). USE1 is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family. SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
HRNLQEELAEELLSLARQLKENALAFSNILKEDNKVLEATEKLADRNLDKLKRESGRLEE
>gnl|CDD|277214 cd15861, SNARE_SNAP25N_23N_29N_SEC9N, N-terminal SNARE motif of SNAP25, SNAP23, SNAP29, and SEC9. N-terminal SNARE motif of members of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP29, SNAP47 and SEC9
QEADKTQDETTESIRRALRLAEETKEIGADTLEELHRQGEQLERIHNDVDDIDSNLKRAEKLLKE
>gnl|CDD|277215 cd15862, SNARE_Vti1, SNARE motif of Vti1. Vti1 (vesicle transport through interaction with t-SNAREs homolog 1) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1b interacts with syntaxin 7 (Qa), syntaxin 8 (Qc), and the lysosomal R-SNARE VAMP8 or VAMP7 to form the endosomal SNARE core complex that mediates transport from the early endosomes and the MVBs (multivesicular bodies), and from the MVBs to the lysosomes, respectively. Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27
TDRLDRSSDRLEDSRRIAAETEEVGANILEDLGRQRETLLRARDRLRETDGNLDRSRRILKS
>gnl|CDD|277216 cd15863, SNARE_GS27, SNARE motif of GS27. GS27 (also known as Bos1, EPM6, golgi SNAP receptor complex member 2 or GOSR2) is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. GS27 forms a complex together with Bet1 (Qc), syntaxin-5 (Qa) and Sec22B (R-SNARE). This complex regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC). SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
IDGLLQENSSLQNSHRQLDDLLESGSAILENLRDQRSTLKGAQRKLLDIANTLGLSNTVMRLIERR
>gnl|CDD|277217 cd15864, SNARE_GS28, SNARE motif of GS28. GS28 (also known as golgi SNAP receptor complex member 1 or GOSR1) forms complexes with syntaxin-5 (Qa), Ykt6 (R-SNARE) and either Bet1 (Qc) or GS15 (Qc). These complexes regulate the early secretory pathway of eukaryotic cells at the level of the transport from the ER-Golgi intermediate compartment (ERGIC) to the cis-Golgi and transport from the trans-Golgi network to the cis-Golgi, respectively. GS28 is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
TELYLKEHEHLRNSDRLIDEQISIAMATKENLTSQRGMLKSITSRMNTLANRFPAINSLIQKINLR
>gnl|CDD|277218 cd15865, SNARE_SEC20, SNARE motif of SEC20. SEC20 (also known as BNIP1, NIP1, or TRG-8) forms a complex with syntaxin 18 (Qa), SEC22 (R-SNARE)and USE1 (Qc), and is involved in the transport from cis-Golgi to the endoplasmic reticulum (ER). SEC20 is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
AKTSSQITENLLRISRMLASQVQQSELTLQELASSSNTVTETHEEFKNMSGVIQTSAKLLTKYNRRELTD
KLLIFLALLFFLATVLYVLKKRL
>gnl|CDD|277219 cd15866, R-SNARE_SEC22, SNARE motif of SEC22. SEC22 forms complexes with syntaxin 18 (Qa), Sec20 (Qb) and USE1 (Qc), and with syntaxin 5 (Qa), GS27 (Qb) and Bet1 (Qc). These complexes are involved in the transport from cis-Golgi to the endoplasmic reticulum (ER) and in the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC), respectively. SEC22 is a member of the R-SNARE subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
RRNLSKLNDELQDVQRIMTKNIDDVLGRGEKLDDLSDKSSNLSSESKKYKKDAKKLNLQALYRK
>gnl|CDD|277220 cd15867, R-SNARE_YKT6, SNARE motif of YKT6. Ykt6 forms complexes with syntaxin-5 (Qa), GS28 (Qb) and either Bet1 (Qc) or GS15 (Qc). This complex regulates the early secretory pathway of eukaryotic cells at the level of the transport from the ER-Golgi intermediate compartment (ERGIC) to the cis-Golgi and transport from the trans-Golgi network to the cis-Golgi, respectively. Ykt6 is a member of the R-SNARE subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
ADKIMKVQSELDETKIILHKTIESVLERGEKLDDLVEKSEDLSDQSKMFYKTAKKQNAVCR
>gnl|CDD|277221 cd15868, R-SNARE_VAMP8, SNARE motif of VAMP8. The lysosomal VAMP8 (vesicle-associated membrane protein 8, also called endobrevin) protein belongs to the R-SNARE subgroup of SNAREs and interacts with STX17 (Qa) and SNAP29 (Qb/Qc). The complex plays a role in autophagosome-lysosome fusion via regulating the transport from early endosomes to multivesicular bodies. Autophagosome transports cytoplasmic materials including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
NDKVSALQSQVDEVKNIMTQNIDKILARGERLDDLMDKTEDLEATSKTFQKTSQKVARKYWWKNTKMI
>gnl|CDD|277222 cd15869, R-SNARE_VAMP4, SNARE motif of VAMP4. The VAMP-4 (vesicle-associated membrane protein 4) protein belongs to the R-SNARE subgroup of SNAREs and interacts with syntaxin 16 (Qa), Vti1a (Qb) and syntaxin 6 (Qc). This complex plays a role in maintenance of Golgi ribbon structure and normal retrograde trafficking from the early endosome to the trans-Golgi network (TGN). SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
DDKIRRVQNQVDEVVDVMQDNITKVIDRGEKLEDLQDKSESLSDNASAFRSRSKQLRRKMWWQNCKM
>gnl|CDD|277223 cd15870, R-SNARE_VAMP2, SNARE motif of VAMP2. The VAMP-2 (vesicle-associated membrane protein 2, also called synaptobrevin-2) protein belongs to the R-SNARE subgroup of SNAREs and interacts with Syntaxin-1 (Qa) and SNAP-25(Qb/Qc), as well as syntaxin 12 (Qa) and SNAP23 (Qb/Qc). The complexes play a role in transport of secretory granule from trans-Golgi network to the plasma membrane, and in the transport from early endosomes to and from the plasma membrane, respectively. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
KRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAGKLKRKYWWKN
>gnl|CDD|277224 cd15871, R-SNARE_VAMP7, SNARE motif of VAMP7. The VAMP-7 (vesicle-associated membrane protein 7, also called synaptobrevin-like protein 1) protein belongs to the R-SNARE subgroup of SNAREs and interacts with syntaxin 7(Qa), syntaxin 8 (Qc) and Vti1b (Qb). The complex is involved in the transport from early endosomes to the lysosome via regulating the transport from multivesicular bodies to the lysosomes. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
DKVSKVQGQLDELKGIMVKNIDSIAQRGEKLELLVDKTEDLSSSSVTFKKTSRNLARAMCMKNIK
>gnl|CDD|277225 cd15872, R-SNARE_VAMP5, SNARE motif of VAMP5. The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to the R-SNARE subgroup of SNAREs. Its function is unknown. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles
KNRLERCQREAEEVKVIMLDNLNKALEREGKLSDLEDRADELLNMSKAFEKTTQTVAQKKRWENIKYK
>gnl|CDD|277226 cd15873, R-SNARE_STXBP5_6, SNARE domain of STXBP5, STXBP6 and related proteins. Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as its relative Syntaxin binding protein 6 (STXBP6, also called Amisyn) contains a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. In general, SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK
>gnl|CDD|277227 cd15874, R-SNARE_Snc1, SNARE motif of Snc1. Saccharomyces cerevisiae SNARE protein Snc1p forms a complex with synaptobrevin homolog Sso1p (Qa) and the SNAP-25 homolog Sec9p (Qb/c) which is involved in exocytosis. Snc1 is a member of the R-SNARE subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
SRTEALQKEIDGAVGIMRHNIEKVAQRGERLDSLQDKTDNLAVSAQGFRRGANRVRKQMW
>gnl|CDD|277228 cd15875, SNARE_syntaxin7, SNARE motif of syntaxin 7. Syntaxin 7 forms a complex with syntaxin 8 (Qc), Vti1b (Qb) and either VAMP7 or VAMP8 (R-SNARE) and is involved in the transport from early endosomes to the lysosome. Syntaxin 7 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
LEERERSIRQLESDIMDVNQIFKDLGMLVHEQGEVIDSIEANVETAAVHVEEANQQLSQA
>gnl|CDD|277229 cd15876, SNARE_syntaxin12, SNARE motif of syntaxin 12. Syntaxin 12 (STX12, also known as STX13 and STX14) forms a complex with SNAP25 (Qb/Qc) or SNAP29 (Qb/Qc) and VAMP2 or VAMP3 (R-SNARE) and plays a role in plasma membrane to early endosome transport. Syntaxin 12 is a member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
IKERETAIQQLEADILDVNQIFKDLAMMIHDQGDMIDSIEANVESAEVHVERASEQLQRAAYYQKKS
>gnl|CDD|277230 cd15877, SNARE_TSNARE1, SNARE motif of TSNARE1. TSNARE1 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. Its function is unknown, but polymorphisms in human TSNARE1 have been associated with schizophrenia susceptibility. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. TSNARE1 is part of a subgroup of the Qa SNAREs that also includes syntaxin 7, syntaxin 12 and related proteins
LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDSIEANIEAASSHVESANQQLAKAS
>gnl|CDD|277231 cd15878, SNARE_syntaxin11, SNARE motif of syntaxin 11. Syntaxin 11 (also known as STX11, FHL4, HLH4, HPLH4) is present on endosomal membranes, including late endosomes and lysosomes in macrophages, and has been shown to bind Vti1b and regulate the availability of Vti1b to form other SNARE-complexes. Mutations in human STX11 has been linked to familial hemophagocytic lymphohistiocytosis type-4 (FHL-4), an autosomal recessive disorder of immune dysregulation. Syntaxin 11 is a member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
ALNEIETRHKELLELESRIREVHELFLQMALLVEEQADTLNNIELNVEKTQDYVGKAKAQVKK
>gnl|CDD|277232 cd15879, SNARE_syntaxin19, SNARE motif of syntaxin 19. Syntaxin 19 has been shown to have the potential to form SNARE complexes with SNAP-23, 25 and 29 (Qb/Qc) and VAMP3 and VAMP8 (R-SNARE), indicating a role in post-Golgi trafficking or plasma membrane fusion. Syntaxin 19 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
QLSEIEQRHKELVSLENQIKDLKDLFIQISLLVEEQGEMINNIEISVNNTQEYVQASKEKFGL
>gnl|CDD|277233 cd15880, SNARE_syntaxin1, SNARE motif of syntaxin 1. Syntaxin-1 belongs to the Qa subgroup of SNAREs and interacts with SNAP-25 (Qb/Qc) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in exocytosis of synaptic vesicles. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
ALSEIEARHNDIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQS
>gnl|CDD|277234 cd15881, SNARE_syntaxin3, SNARE motif of syntaxin 3. Syntaxin 3 (STX3) has been shown to form a complex with VAMP8 (R-SNARE) and SNAP-23 (Qb/c) in mast cells. Mutations have been implicated in human microvillus inclusion disease (MVID), a disorder of the differentiation of intestinal epithelium. Syntaxin 3 is a member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
ALSEIEGRHKDIVRLESSIKELHDMFVDIAMLVENQGEMLDNIELNVMKTVDHVEKARDETKKAVKYQS
>gnl|CDD|277235 cd15882, SNARE_syntaxin2, SNARE motif of syntaxin 2. Syntaxin 2 (STX2), also known as epimorphin (EPM or EPIM), may interact with SNAP-23 (Qb/c) and genetic varioations are associated with type 1 von Willebrand disease (VWD). Syntaxin 2 is a member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
ALNEIESRHKDIMKLESSIRELHDMFVDMAMLVETQGEMINNIEKNVHNAVEYVEHAKEETKKAVKYQS
>gnl|CDD|277236 cd15883, SNARE_syntaxin4, SNARE motif of syntaxin 4. Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, VAMP2 and VAMP7 which plays a role in exocytosis of secetory granule. Syntaxin 4 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
ALNEIEARHSEIQKLERSIRELHDMFTYLAMEVEAQGEMIDRIEKNILSSADYVEKAQEHVKT
>gnl|CDD|277237 cd15884, SNARE_SNAP23C, C-terminal SNARE motif of SNAP23. C-terminal SNARE motifs of SNAP23, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with Syntaxin-4 (Qa) and the R-SNARE VAMP8. The complex plays a role in exocytosis of secretory granule. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP25, SNAP29, SNAP47 and SEC9
EDEMDENLTQVGSILGNLKSMALDMGNELDKQNKQIGRINEKADMNSDRIDEANVRAKK
>gnl|CDD|277238 cd15885, SNARE_SNAP25C, C-terminal SNARE motif of SNAP25. C-terminal SNARE motifs of SNAP25, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP29, SNAP47 and SEC9
EDEMEENLGQVSGMIGNLRNMAIDMGSEIESQNRQIDRINEKAESNETRIDSANKRATK
>gnl|CDD|277239 cd15886, SNARE_SEC9N, N-terminal SNARE motif of SEC9. N-terminal SNARE motif of fungal SEC9, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SEC9 interacts with Sso1(Qa) and the lysosomal R-SNARE Snc1. The complex plays a role in post-Golgi transport. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SNAP29
QEIRFTKQESVASTRNALRMAREAEETGRNTLAKLGQQSERLHNTEKNLDLAKNQNKIADEKAKELKKLN
>gnl|CDD|277240 cd15887, SNARE_SNAP29N, N-terminal SNARE motif of SNAP29. N-terminal SNARE motif of SNAP29, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP29 interacts with STX17 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SEC9
QEIRRSEQRTLDSTQRSLGLLYESEQIGVATAEELVRQGEQLERTEKNLDKINQDLKTSQRHINS
>gnl|CDD|277241 cd15888, SNARE_SNAP47N, N-terminal SNARE motif of SNAP47. N-terminal SNARE motif of SNAP47, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. The exact funtion of SNAP47 is unknown. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP29 and SEC9
PYGAHEASEPTTRGKELLGLAAGSQRRLEDTAKVLHHQGEQLDSVMKGLDKMESDLDVADRLLTE
>gnl|CDD|277242 cd15889, SNARE_SNAP25N_23N, N-terminal SNARE motif of SNAP25 and SNAP23. N-terminal SNARE motifs of SNAP25 and SNAP23, members of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with STX4 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP29, SNAP47 and SEC9
MRANQVTDESLESTRRMLQLCEESQDAGIKTLVMLDEQGEQLDRIEEGMDQINADMKEAEKNLTG
>gnl|CDD|277243 cd15890, SNARE_Vti1b, SNARE motif of Vti1b-like. Vti1b (vesicle transport through interaction with t-SNAREs homolog 1B) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1b interacts with syntaxin 7 (Qa), syntaxin 8 (Qc), and the lysosomal R-SNARE VAMP8 or VAMP7 to form the endosomal SNARE core complexes that mediate transport from the early endosomes and the MVBs (multivesicular bodies), and from the MVBs to the lysosomes, respectively. SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27
TESLNRTSDSLARSQRIAAETEQIGTEIIEELGEQREQLLRTRDRLEETDANLSRARRILRS
>gnl|CDD|277244 cd15891, SNARE_Vti1a, SNARE motif of Vti1b-like. Vti1a (vesicle transport through interaction with t-SNAREs homolog 1A) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27
TERLERSSRRLEDGYRIAVETEQIGAQILDDLHSQRETIQRSRDRLRETDSELGKSSRVLSG
>gnl|CDD|277245 cd15892, R-SNARE_STXBP6, SNARE domain of STXBP6. Syntaxin binding protein 6 (STXBP6, also called Amisyn), as well as its relative Syntaxin binding protein 5 (STXBP5, also called Tomosyn), contains a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. In general, SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
MGGNSILHSAADSVTSAVQKASQALNERGERLGRAEEKTEDMKNSAQQFAETAHKLAMKHKC
>gnl|CDD|277246 cd15893, R-SNARE_STXBP5, SNARE domain of STXBP5. Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as its relative Syntaxin binding protein 6 (STXBP6, also called Amisyn) contains a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. Tomosyn contains an N-terminal WD40 repeat region and has been shown to form complexes with SNAP-25 and syntaxin 1a, as well as SNAP-23 and syntaxin 4. In general, SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle
PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK
>gnl|CDD|277247 cd15894, SNARE_SNAP25N, N-terminal SNARE motif of SNAP25. N-terminal SNARE motifs of SNAP25, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP29, SNAP47 and SEC9
ELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLDRVEEGMNHINQDMKEAEKNLK
DLG
>gnl|CDD|277248 cd15895, SNARE_SNAP23N, N-terminal SNARE motif of SNAP23. N-terminal SNARE motifs of SNAP23, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with Syntaxin-4 (Qa) and the R-SNARE VAMP8. The complex plays a role in exocytosis of secretory granule. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP25, SNAP29, SNAP47 and SEC9
IQLRANQVTDESLESTRRILGLAIESQDAGIKTITMLDEQGEQLNRIEEGMDQINKDMREAEKTLTE
>gnl|CDD|276899 cd15896, MYSc_Myh19, class II myosin heavy chain19, motor domain. Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy
ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQD
REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTV
KNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENY
NNYRFLSNGNVTIPGQQDKDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPD
NTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKAL
DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLD
LQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEADFCIIHYAGKV
DYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMPGAFKTRKGMFRTVGQL
YKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ
RYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR
>gnl|CDD|320054 cd15897, EFh_PEF, The penta-EF hand (PEF) family. The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+
QLRNVFQAVAGDDGEISATELQQALSNVGWTHFDLGFSLETCRSMIAMMDRDHSGKLNFSEFKGLWNYIK
AWQEIFRTYDTDGSGTIDSNELRQALSGAGYRLSEQTYDIIIRRYDRGRGNIDFDDFIQCCVRLQRLTDA
FRRYDKDQDGQIQVNYDEFLQGTMS
>gnl|CDD|320029 cd15898, EFh_PI-PLC, EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes. PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear
WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERPE
LEPIFKKYAGTNRDYMTLEEFIRFLREEQGENVSEEECEELIEKYEPERENRQLSFEGFTNFLLSPE
>gnl|CDD|320021 cd15899, EFh_CREC, EF-hand, calcium binding motif, found in CREC-EF hand family. The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin (also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes
HEMDGHLNSDYDHEAFLGKEEAEEFDQLTPEESKRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAM
EESKEQFRAVDPDEDGHVSWDEYKNDTYGSVGDDEENVADNIKEDEEYKKLLLKDKKRFEAADQDGDLIL
TLEEFLAFLHPEESPYMLDFVIKETLEDLDKNGDGFISLEEFISDPYSADENEEEPEWVKVEKERFVELR
DKDKDGKLDGEELLSWVDPSNQEIALEEAKHLIAESDENKDGKLSPEEILDNHELFV
>gnl|CDD|320080 cd15900, EFh_MICU, EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, MICU3, and similar proteins. This family includes mitochondrial calcium uptake protein MICU1 and its two additional paralogs, MICU2 and MICU3. MICU1 localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and MICU2 are physically associated within the uniporter complex and are co-expressed across all tissues. They may play non-redundant roles in the regulation of the mitochondrial calcium uniporter. At present, the precise molecular function of MICU2 and MICU3 remain unclear. MICU2 may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU3 likely has a role in mitochondrial calcium handling. All members in this family contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices
HFEIAFKMFDLDGDGELDKEEFNKVQSIIRSQTSVGQRHRDHTNGESTKLGMNSTLARYFFGKDGKQKLS
IEKFLEFQENLQEEIDDVDTALTFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIFDEDGDGILS
HKEFISVMKDRL
>gnl|CDD|319999 cd15901, EFh_DMD_DYTN_DTN, EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family. The dystrophin/dystrobrevin/dystrotelin family has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize
DLSTVLSVFDRHGLSGSQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGC
IRLLSVKIALITLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAV
ESCFQLARSRVGVSEDTFLSWLL
>gnl|CDD|320075 cd15902, EFh_HEF, EF-hand, calcium binding motif, found in the hexa-EF hand proteins family. The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding
FMEVWMHFDADGNGYIEGKELDSFLRELLKALNGKDKTDDEVAEKKKEFMEKYDENEDGKIEIRELANIL
PTEENFLLLFRREQPLISSVEFMKIWRKYDTDGSGFIEAKELKGFLKDLLLKNKKHVSPPKLDEYTKLIL
KEFDANKDGKLELDEMAKLLPVQENFLLKFQILGAMDLTKEDFEKVFEHYDKDNNGVIEGNELDALLKDL
LEKNKADIDKPDLENFRDAILRACDKNKDGKIQKTELALFLSAK
>gnl|CDD|277191 cd15903, Dicer_PBD, Partner-binding domain of the endoribonuclease Dicer. The endoribonuclease Dicer plays a central role in RNA interference by breaking down RNA molecules into fragments of about 22 nucleotides (miRNAs and siRNAs). Loading of RNA onto Dicer and the enzymatic cleavage are supported by dsRNA-binding proteins, including trans-activation response (TAR) RNA-binding protein (TRBP) or protein activator of PKR (PACT). Together with Argonaute, this constitutes the RNA-induced silencing complex (RISC) which functions to load the small RNA fragments onto Argonaute. The Partner-binding domain of Dicer is responsible for interactions with the dsRNA-binding proteins. This helical domain can be found inserted in a subset of SF2-type DEAD-box related helicases
LSLLDEIIEFLNDCKLFDPEVYIESLLLDRDPDPKKKLKNILNDILYVLDELGPWGASKAALAFIIQLEK
LKKKSTDEKHRLFLRYVITQLRKIRKLLEDEMKN
>gnl|CDD|320706 cd15904, TSPO_MBR, Translocator protein (TSPO)/peripheral-type benzodiazepine receptor (MBR) family. This family contains tryptophan-rich translocator protein (TSPO), an integral membrane protein that is highly conserved from bacteria to mammals. In eukaryotes, it is mainly found in the outer mitochondrial membranes of steroid-synthesizing cells of the nervous system where it transports cholesterol into mitochondria. It is known to be highly expressed in metastatic cancer, steriodogenic tissues, as well as inflammatory and neurological diseases such as Alzheimer's and Parkinson's. TSPO is also known as the peripheral benzodiazepine receptor (MBR) and its ligands include benzodiazepine drugs, implicated in regulating apoptosis. In human, a single polymorphism A147T is associated with psychiatric disorders; the mutation causes structural changes in a region implicated in cholesterol binding. TSPO is homologous to bacterial tryptophan-rich sensory proteins, and their tryptophan residues are believed to be functionally important. In bacteria, TSPO acts as a negative regulator of expression of specific photosynthesis genes in response to oxygen/light; it catalyzes a photooxidative degradation of Proto porphyrine (PpIX). R. sphaeroides TSPO (RsTSPO) is involved in porphyrin transport, similar to human, while Arabidopsis translocator protein (AtTSPO) is regulated at multiple levels in response to salt stress and perturbations in tetrapyrrole metabolism
LALALAVGLLGGLLTGSSIGEWYASLNKPSWTPPNWVFGPVWTILYILMGIAAYLVWRAGGFAGRKLALA
LYAVQLALNLLWSPLFFGLHRPGLALVVILALWLLILATIVAFWRVSRLAALLLLPYLAWVSFATYLNYS
IW
>gnl|CDD|320571 cd15905, 7tmA_GPBAR1, G protein-coupled bile acid receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. The G-protein coupled bile acid receptor GPBAR1 is also known as BG37, TGR5 (Takeda G-protein-coupled receptor 5), M-BAR (membrane-type receptor for bile acids), and GPR131. GPBAR1 is highly expressed in the gastrointestinal tract, but also found at many other tissues including liver, colon, heart, skeletal muscle, and brown adipose tissue. GPBAR1 functions as a membrane-bound receptor specific for bile acids, which are the end products of cholesterol metabolism that facilitate digestion and absorption of lipids or fat-soluble vitamins. Bile acids act as liver-specific metabolic signaling molecules and stimulate liver regeneration by activating GPBAR1 and nuclear receptors such as the farnesoid X receptor (FXR). Upon bile acids binding, GPBAR1 activation causes release of the G-alpha(s) subunit and activation of adenylate cyclase. The increase in intracellular cAMP level then stimulates the expression of many genes via the PKA-mediated phosphorylation of cAMP-response element binding protein (CREB). Thus, GPAR1-signalling exerts various biological effects in immune cells, liver, and metabolic tissues. For example, GPBAR1 activation leads to enhanced energy expenditure in brown adipose tissue and skeletal muscle; stimulation of glucagon-like peptide-1 (GLP-1) production in enteroendocrine L-cells; and inhibition of pro-inflammatory cytokine production in macrophages and attenuation of atherosclerosis development. GPBAR1 is a member of the class A rhodopsin-like family of GPCRs, which comprises receptors for hormones, neurotransmitters, sensory stimuli, and a variety of other ligands
IFWLSVPLSSLIIFANLFIILGIACNRKLHNTANYFFLSLLLADLLTGVALPFIPGMSNESRRGYHSCLF
VYVAPNFLFLSFLANLLMVHYERYLCIVYPLQYHNFWVHRWVPLALLLTWALPLLFACLPALGWNNWTPG
SNCSYKQVFPAAYIYLEVYGLVLPSILAIAFMSVRVLAVARRQLQDICKLLRAVQRDGPSELEQQLNLRY
AKCIAGVSLTFLVCWVPYIAYLLMSVLAIEQRPPLSPGTLLILSCVGSGSAAAVPVILGLGN
>gnl|CDD|320572 cd15906, 7tmA_GPR162, G protein-coupled receptor 162, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup represents the orphan G-protein coupled receptor 162 (GPR162), also called A-2 or GRCA, with unknown endogenous ligand and function. Phylogenetic analysis indicates that GPR162 and GPR153 share a common evolutionary ancestor due to a gene duplication event. Although categorized as members of the rhodopsin-like class A GPCRs, both GPR162 and GPR153 contain HRM-motif instead of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors and important for efficient G protein-coupled signal transduction. Moreover, the LPxF motif, a variant of NPxxY motif that plays a crucial role during receptor activation, is found at the end of TM7 in GPR162 and GPR153. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
QNNSLSWLACGALALLANGWIILSIAAKQQKHKPLELLLCFLAGTHILMAAVPLTTFAVVQLRRKHSGYD
WNESICKVFVSTYYTLALATCFTVASLSYHRMWMVRWPVNYRLSNAKKQALHAVMGIWMVSFILSTLPSI
GWHNNGERYYARGCQFIVSKIGLGFGVCFSLLLLGGIVMGLVCVGITFYQTLWAPARRQRGGHQRPEEAA
GEGGVEGKFEVPAIVVEDARGKRRSSLDGSESAKTSLQVTNLVSAIVFLYDALTGVPILVVSFFSLRYDS
APPWMVLAVLWCSMAQTLLLPSFIWSCERYRADLR
>gnl|CDD|320573 cd15907, 7tmA_GPR153, orphan G protein-coupled receptor 153, member of the class A family of seven-transmembrane G protein-coupled receptors. This subgroup represents the G-protein coupled receptor 153 (GPR153) with unknown endogenous ligand and function. GPR153 shares a common evolutionary origin with GPR162 and is highly expressed in central nervous system (CNS) including the thalamus, cerebellum, and the arcuate nucleus. Although categorized as a member of the rhodopsin-like class A GPCRs, GPR153 contains HRM-motif instead of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors and important for efficient G protein-coupled signal transduction. Moreover, the LPxFL motif, a variant of NPxxY motif that plays a crucial role during receptor activation, is found at the end of TM7 in GPR153. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
HNNAVAWLVCSGVSLLANTWGILSVSAKQKKWKPLEFLICTLAGTHILNVAIPITMYSVIQLRRQHSDYE
WNEGLCKVFVSTFYTLTLVTCFSVTSLSYHRMWMVRWPVNYRLSNTKKQAVHTVMGIWMVSFILSTLPAV
GWHDTTERFYTRDCRFIVTEIGLGFGVCFLLLISGSVAMGVVCIGIALFQTFSIQTGHNIDKNKFNVPTI
VVEDAQGKRRSSIDGSEPIKTSLQITYLISGIVFIYDFLMGFPILVVSFASLKADKSYNWMVLCVLWCSV
AQSLLLPMFLWACDRYRADIK
>gnl|CDD|320574 cd15908, 7tm_TAS2R40-like, taste receptor 2, subtypes 39 and 40, and similar receptors, member of the seven-transmembrane G protein-coupled receptor superfamily. This group includes the mammalian taste receptor 2 (TAS2R) subtypes 39 and 40, which function as bitter taste receptors. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (taste of glutamate MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release
FYLVILGIESIIGILGNGFIVAINLTEWVRSKRLSTSDRILIFLSLSRLCLQSWMMLENVCSLFFPSFYN
EDNVYKTFKVIFMFLNYSSLWFAAWLSVFYCVKIANFTHPLFLWLKWRITSLMPWLLILSVLISFSTSLP
FSWDVYNVYCNSSIPLPSSNSTKKKYIKETNLVNLIFLYNVGIFLPLIMFILSATLLILSLKRHTLQMQN
NATGSRDPSMEAHMGAIKAISSFLILYIFNFVALILTLSNIFDTNSTWNILCKIIMAAYPAGHSILLILG
NPKLRRAWK
>gnl|CDD|320575 cd15909, 7tmF_FZD4_9_10-like, class F frizzled subfamilies 4, 9, 10, and related proteins; member of 7-transmembrane G protein-coupled receptors. This group includes subfamilies 4, 9 and 10 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of GPCRs, and their closely related proteins. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
VMFSRSDKNFAEIWMAVWASLCFASTAFTVLTFLIDTSRFRYPERPIIFLSMCYFIYSLGYLIRLFLGRE
RIACDSLNSGVSYLIQEGLESTWCTIVFLLLYYFGMASALWWVILTFTWYLAAGRKWGPEAIEAASSYFH
LVAWALPAVKTIVILIMHKVDADELTGLCYVGNHDSDALLGFVLVPLAIYLLIGTLFILAGFVSMFRIRR
NLKTRGTDTSKLEKLMVKIGVFSVLYTVPATCVIACYFYEYLNMDQWRIAAIECKCQSPNAIGSDCCLQP
SIPSVEIYMLKIFMSLVVGITSGMWVWSSKTLQSWQRFIC
>gnl|CDD|320576 cd15910, 7tmF_FZD3_FZD6-like, class F frizzled subfamilies 3, 6 and related proteins; member of 7-transmembrane G protein-coupled receptors. This group includes subfamilies 3 and 6 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of GPCRs, and their closely related proteins. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others
MYFGDDELMFARYFIGVVSILCLLATLFTFLTFLIDVNRFRYPERPIIFYAVCYFVVSLIFFVGFLLGDD
VACNHAIMDENNGATVVEGSRNKACTILFMILYFFTMAGTVWWVILTITWFLAAGFKWGSEAIEKKALYF
HALAWGIPGVLTMVLLATNKIEGDNISGVCFVGLYDSDGLRFFVLLPLCLYVLVGMSLLLAGIICLNRVR
KSIHDDETNQEKLAKFMIRIGVFSILYLVPLLTLIGCYAYEQSNRKSWESTWVVRNCRRYHIPCPQLAQG
NPRPGLFLFCIKYLMTLIVGIPPVFWVGSKKTCAEWAGFFT
>gnl|CDD|320577 cd15911, 7tmA_OR11A-like, olfactory receptor subfamily 11A and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor 11A and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
ILLFLLFLVIYIVTMAGNILIIVLVVADRHLHTPMYFFLGNLSCLEICYTSTILPRMLASLLTGDRTISV
SGCIVQFYFFGSLAATECYLLAVMSYDRYLAICKPLHYASLMNGRLCLQLAAGSWISGFLASTITVILMS
QLTFCGPNEIDHFFCDFAPLLKLSCSDTSLVELVTFILSSIVTLPPFLLTLTSYICIISTILRIPSTTGR
QKAFSTCSSHLIVVTIFYGTLIIVYVVPSTNTSRDLNKVFSLFYTVLTPLVNPLIYSLRN
>gnl|CDD|320578 cd15912, 7tmA_OR6C-like, olfactory receptor subfamily 6C and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor 6C, 6X, 6J, 6T, 6V, 6M, 9A, and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
ILLFLLLLLTYLLTLLGNLLIITITLVDHRLHTPMYFFLRNFSFLEILFTSVVIPKMLANLLSGKKTISF
AGCFAQSFFYFFLGTTEFFLLAVMSFDRYVAICNPLHYPTIMNSRVCLQLVLGSWVGGFLLILPPTILVF
QLPFCGPNVINHFFCDSGPLLKLSCSDTRLIELLDFILASVVLLGSLLLTIVSYIYIISTILRIPSASGR
QKAFSTCASHLTVVSIFYGSCIFMYVRPSQSSSLDLNKVVALLNTVVTPLLNPFIYTLRN
>gnl|CDD|320579 cd15913, 7tmA_OR11G-like, olfactory receptor OR11G and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor 11G, 11H, and related proteins in other mammals, and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
ILLFSFFSVIYILTLLGNGAIICAVWWDRRLHTPMYILLGNFSFLEICYVTSTVPNMLVNFLSETKTISF
SGCFLQFYFFFSLGTTECFFLSVMAFDRYLAICRPLHYPTIMTGQLCGKLVAFCWVCGFLWFLIPVVLIS
QLPFCGPNIIDHFLCDPGPLLALSCVPAPGTELICYTLSSLIIFGTFLFILGSYTLVLRAVLRVPSAAGR
HKAFSTCGSHLAVVSLFYGSVMVMYVSPGSGNSTGMQKIVTLFYSVVTPLLNPLIYSLRN
>gnl|CDD|320580 cd15914, 7tmA_OR6N-like, olfactory receptor OR6N and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor 6N, 6K, and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
LLLFILLLLIYLFIITGNLLIFTVVRLDTHLHTPMYFFISILSFLEIWYTTVTIPKMLSNLLSEEKTISF
NGCLLQMYFFHSLGITECYLLTAMAYDRYLAICNPLHYPSIMTPKLCTQLAAGCWLCGFLGPVPEIILIS
TLPFCGPNQIQHIFCDFPPLLSLACTDTSLNVLVDFVIHAVIILLTFLLILLSYVKIISVVLKIPSAEGR
QKAFSTCAAHLTVVLLFFGSVSFMYLRLSKSYSLDYDRAIAVVYAVLTPFFNPIIYSLRN
>gnl|CDD|320581 cd15915, 7tmA_OR12D-like, olfactory receptor subfamily 12D and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 12D and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
IFLFVLFLLLYLASLLGNGAILAVVIAEPRLHSPMYFFLGNLSCLDIFYSSVTVPKMLAGLLSEHKTISF
QGCISQLHFFHFLGSSEAMLLAVMAYDRYVAICNPLRYTVIMNPQVCLLLAVACWVTGFFHALMHTVMTS
RLPFCGPNKINHFFCDIKPLLKLACGDTSLNLWLLNIVTGSIALGTFILTLLSYIYIISFLLLKVRSKEG
RHKAFSTCASHLTVVLLLYGPALFTYIRPSSGDSLEQDRIVALLYTVVTPVLNPLIYTLRN
>gnl|CDD|320582 cd15916, 7tmA_OR10G-like, olfactory receptor subfamily 10G and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 10G, 10S, and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
SLLFLIFLIIYLLTVLGNLLILLTVWVDSHLHRPMYIFLGHLSFLDMWLSTVTVPKMLAGFLEPGGKVIS
FGGCVAQLYFFHFLGSTECFLYTLMAYDRYLAICHPLHYPTIMTGRLCTRLATGTWVAGSLHSAIHTSLT
FRLPFCGPNRIDYFFCDIPPLLKLACADTTINELVIFASIGVVALGCFILILLSYGNIVRAILRIRTAEG
RRRAFSTCASHLIVVLCFYVPCVFIYLRPGSKEALDGVIAVFYTVVTPLLNPLIYTLRNKEVKTAL
>gnl|CDD|341351 cd15917, 7tmA_OR51_52-like, olfactory receptor family 51, 52, 56 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor families 51, 52, 56, and related proteins in other mammals, sauropsids, amphibians, and fishes. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
IWLSIPFCAMYLVALLGNITILFVIKIESSLHEPMYLFLAMLAATDLVLSTSTVPKMLGIFWFNAREISF
DACLAQMFFIHSFTAMESGVLLAMAFDRYVAICYPLRYTTILTNTVVGKIGLAILLRAVALIIPLPLLVR
RLPYCGSNVISHSYCEHMAVVKLACGDTRVNSIYGLFVALLIVGFDLLFIALSYVLILRAVLQLPSKEAR
LKALSTCGSHICVILIFYTPALFSFLTHRFGHHVPPHVHILLANLYLLLPPMLNPIVYGVRTKQI
>gnl|CDD|320584 cd15918, 7tmA_OR1_7-like, olfactory receptor families 1, 7, and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor families 1 and 7, and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
QLLFGLFLGMYLVTVLGNLLIILAIGSDSHLHTPMYFFLANLSLVDICFTSTTVPKMLVNIQTQSKSISY
AGCLTQMYFFLLFGDLDNFLLAVMAYDRYVAICHPLHYTTIMSPRLCILLVAASWVITNLHSLLHTLLMA
RLSFCASNEIPHFFCDLNPLLKLSCSDTHLNELVILVLGGLVGLVPFLCILVSYVRIVSAVLRIPSAGGK
WKAFSTCGSHLSVVSLFYGTVIGVYLSPPSSHSASKDSVAAVMYTVVTPMLNPFIYSLRN
>gnl|CDD|320585 cd15919, 7tmA_GPR139, G-protein-coupled receptor GPR139, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR139, a vertebrate orphan receptor, is very closely related to GPR142, but they have different expression patterns in the brain and in other tissues. These receptors couple to inhibitory G proteins and activate phospholipase C. Studies suggested that dimer formation may be required for their proper function. GPR142 is predominantly expressed in pancreatic beta-cells and plays an important role in mediating insulin secretion and maintaining glucose homeostasis, whereas GPR139 is expressed almost exclusively in the brain and is suggested to play a role in the control of locomotor activity. Tryptophan and phenylalanine have been identified as putative endogenous ligands of GPR139. These orphan receptors are phylogenetically clustered with invertebrate FMRFamide receptors such as Drosophila melanogaster DrmFMRFa-R
FVPVIYYSLLLCLGLPANILTVIILSQLVARRQKSSYNYLLALAAADILVLFFIVFVDFLLEDFILNKQM
PQVLDKIIEVLEFSSIHTSIWITVPLTIDRYIAVCHPLKYHTVSYPARTRKVIVSVYITCFLTSIPYYWW
PNIWIEDYTSTSMHHVLIWIHCFTVYLVPCSIFFVLNSIIVYKLRRKSNFRLRGYSTGKTTAILFTITSI
FAILWAPRIIMILYHLYVSPINNSWLVHIVSDIANMLALLNTAINFFLYCFISKRFRTMA
>gnl|CDD|320586 cd15920, 7tmA_GPR34-like, P2Y-like receptor and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR34 is phylogenetically related to the P2Y family of purinergic G protein-coupled receptors. The P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. GPR34 is shown to couple to G(i/o) protein and is highly expressed in microglia. Recently, lysophosphatidylserine has been identified as a ligand for GPR34. This group belongs to the class A G protein-coupled receptor superfamily, which all have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, which then activate the heterotrimeric G proteins. G-proteins regulate a variety of cellular functions including metabolic enzymes, ion channels, and transporters, among many others
VTLPVMYSIICIVGLLSNTLALWVFFLRQQRETSISVYMRNLALADLLLVLCLPFRVAYQNTAGPLSFCK
IVGAFFYLNMYASILFLSLISLDRYLKIIKPLQQFKIHTVPWSSAASGGVWLLLLACMIPFLFESRNEGP
CDNKCFHFRSKGLTAGGINLTAVVIFYILSLLFLYFYAKISHKLYKVSLGNAQQQIKKASKRAIIKTFIV
LAIFIVCFVPYHIVRVPYVLAQIDVISSLPWKQTLHIANELVLCLSALNSCLDPIIYFFLSSSFRRAV
>gnl|CDD|320587 cd15921, 7tmA_CysLTR, cysteinyl leukotriene receptors, member of the class A family of seven-transmembrane G protein-coupled receptors. Cysteinyl leukotrienes (LTC4, LTD4, and LTE4) are the most potent inflammatory lipid mediators that play an important role in human asthma. They are synthesized in the leucocytes (cells of immune system) from arachidonic acid by the actions of 5-lipoxygenase and induce bronchial constriction through G protein-coupled receptors, CysLTR1 and CysLTR2. Activation of CysLTR1 by LTD4 induces airway smooth muscle contraction and proliferation, eosinophil migration, and damage to the lung tissue. They belong to the class A GPCR superfamily, which all have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
LFYPTAYILIFILGLTGNSISVYVFLSQYRSQTPVSVLMVNLAISDLLLVCTLPLRLTYYVLNSHWPFGD
IACRIILYVLYVNMYSSIYFLTALSVFRYLALVWPYLYLRVQTHSVAGIICGLIWILMGLASSPLLFAKS
KQHDEGSTRCLELAHDAVDKLLLINYVTLPVGFVVPFMTVIFCYIFIIKNLLKPSPALGRTRPSRRKACA
LIIISLGIFLVCFLPYHIVRTIHLITERQIKESCGYILRVRKAAVITLCLAASNSCFDPLLYFFVGENFR
SRL
>gnl|CDD|320588 cd15922, 7tmA_P2Y-like, P2Y purinoceptor-like proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. P2Y-like proteins are an uncharacterized group that is phylogenetically related to a family of purinergic G protein-coupled receptors. The P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5 and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12 and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-glucose (P2Y14)
PAIPVFLSLVFLGGFLLNSFSLWIFWFRIKQWSSGTILQFNLALSDAIITPAAPLLIAYFSLGSHWPFGQ
FLCQLKVFLLSTHMYGSIYFLMLISIHRYVTVVHYNWKSLWKKKSFMKKLCLGVWLLLFVQGLPFFFVLK
TSVIDGKTKCLSIHQSELSLLYFVWNFVLLILGFLLPFGVSLTCYALLGASIAKMNSNNARGRAMKAKSL
QMIGISLVIFIICFVPLHVTRTVGVVVKLFYPESCTLLHKVEVAYYISWVLTGVNCCLDPLLYCFASEKF
RKSF
>gnl|CDD|320589 cd15923, 7tmA_GPR35_55-like, G protein-coupled receptor 35, GPR55, and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This subfamily is composed of GPR35, GPR55, and similar proteins. GPR35 shares closest homology with GPR55, and they belong to the class A G protein-coupled receptor superfamily, which all have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A number of studies have suggested that GPR35 may play important physiological roles in hypertension, atherosclerosis, nociception, asthma, glucose homeostasis and diabetes, and inflammatory bowel disease. GPR35 is thought to be responsible for brachydactyly mental retardation syndrome, which is associated with a deletion comprising chromosome 2q37 in human, and is also implicated as a potential oncogene in stomach cancer. GPR35 couples to G(13) and G(i/o) proteins, whereas GPR55 has been reported to couple to G(13), G(12), or G(q) proteins. Activation of GPR55 leads to activation of phospholipase C, RhoA, ROCK, ERK, p38MAPK, and calcium release. Recently, lysophosphatidylinositol (LPI) has been identified as an endogenous ligand for GPR55, while several endogenous ligands for GPR35 have been identified including kynurenic acid, 2-oleoyl lysophosphatidic acid, and zaprinast
LLQYAIYIPTFVLGLLLNILALWVFCWRLKKWTETNIYMTNLAVADLLLLISLPFKMHSYRRESAGLQKL
CNFVLSLYYINMYVSIFTITAISVDRYVAIRYPLRARELRSPRKAAVVCAVIWVLVVTISIPYFLLDSSN
EKTMCFQRTKQTESLKVFLLLEIFGFLLPLIIMTFCSARVIHTLQKRLDDVGSRSETKQCIRVIMANLIV
FIVCFLPVHVGFFVKFIVGKSYSCDSKLIIHFFLQSAFCLSDMNCCLDAFCYYFATKEFREAY
>gnl|CDD|341352 cd15924, 7tmA_P2Y12-like, P2Y purinoceptors 12, 13, 14, and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. The P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5 and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12 and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-glucose (P2Y14). This cluster only includes P2Y12-like receptors as well as closely related orphan receptor, GPR87
QLFPVLYTVIFFAGILLNGLAMWIFFHIPSKSSFIIYLKNTVVADLLMILTFPFKILSDAGLGPWQLRTF
VCRVTSVLFYFTMYTSIVFLGLISIDRYLKIVRPFKTSFPKSVSFAKILSVVVWALMFLLSLPNMILTNQ
QPREKNVKKCSFLKSELGLKWHEIVNYICQVIFWIVFLLMIVCYTAITKKVYRSYRRVFRSSSSRRKKSN
VKIFIIVAVFFVCFVPYHFARIPYTLSQTRDVFDCTAENILFYVKEATLFLSALNVCLDPIIYFFLCKSF
RESL
>gnl|CDD|320591 cd15925, 7tmA_RNL3R2, relaxin-3 receptor 2 (RNL3R2), member of the class A family of seven-transmembrane G protein-coupled receptors. The G protein-coupled receptor RNL3R2 is also known as GPR100, GPR142, and relaxin family peptide receptor 4 (RXFP4). Insulin-like peptide 5 (INSL5) is an endogenous ligand for RNL3R2 and plays a role in fat and glucose metabolism. INSL5 is highly expressed in human rectal and colon tissues. RNL3R2 signals through G(i) protein and inhibit adenylate cyclase, thereby inhibit cAMP accumulation
ILVALAYGLVCAIGLLGNLAVMYLLRNCARRAPPPIDVFVFNLALADFGFALTLPFWAVESALDFHWPFG
GAMCKMVLTATVLNVYASVFLLTAMSVTRYWVVASAAGPGTHLSTFWAKIITLALWAAALLATVPTAIFA
TEGEVCGVELCLLKFPSNYWLGAYHLQRVVVAFVVPLGVITTSYLLLLSFLQQHKVNQNNRQRQSVIARS
VRLVVASFFLCWFPNHVVTFWGVLVKFRAVPWNSTFYFIHTYVFPVTTCLAHSNSCLNPVLYCLMRREFR
QAL
>gnl|CDD|320592 cd15926, 7tmA_RNL3R1, relaxin 3 receptor 1 (RNL3R1), member of the class A family of seven-transmembrane G protein-coupled receptors. The G protein-coupled receptor RNL3R1 is also known as GPCR135, relaxin family peptide receptor 3 (RXFP3), and somatostatin- and angiotensin-like peptide receptor (SALPR). RNL3/relaxin-3, a member of the insulin superfamily, is an endogenous neuropeptide ligand for RNL3R1. RNL3R1 is predominantly expressed in brain regions and implicated in stress, anxiety, and feeding, and metabolism. RNL3R1 signals through G(i) protein and inhibit adenylate cyclase, thereby inhibit cAMP accumulation, and also activates Erk1/2 signaling pathway
IIISIVYSVVCALGLVGNLLVLYLMKSKQGWKKSSINLFVTSLAVTDFQFVLTLPFWAVENALDFTWLFG
KAMCKIVSYVTAMNMYASVFFLTAMSVARYHSVASALKSKRRRGCCSAKWLCVLIWVLAILASLPNAIFS
TTATVSNEELCLVKFPDNRGNAQFWLGLYHAQKVLLGFLIPLGIISLCYLLLVRFITDKNITGSSTKRRS
KVTKSVTIVVLSFFLCWLPNQALTTWGILIKLNVVHFSYEYFTTQVYIFPITVCLAHSNSCLNPILYCLM
RREFRKAL
>gnl|CDD|320593 cd15927, 7tmA_Bombesin_R-like, bombesin receptor subfamily, member of the class A family of seven-transmembrane G protein-coupled receptors. This bombesin subfamily of G-protein coupled receptors consists of neuromedin B receptor (NMBR), gastrin-releasing peptide receptor (GRPR), and bombesin receptor subtype 3 (BRS-3). Bombesin is a tetradecapeptide, originally isolated from frog skin. Mammalian bombesin-related peptides are widely distributed in the gastrointestinal and central nervous systems. The bombesin family receptors couple mainly to the G proteins of G(q/11) family. NMBR functions as the receptor for the neuropeptide neuromedin B, a potent mitogen and growth factor for normal and cancerous lung and for gastrointestinal epithelial tissues. Gastrin-releasing peptide is an endogenous ligand for GRPR and shares high sequence homology with NMB in the C-terminal region. Both NMB and GRP possess bombesin-like biochemical properties. BRS-3 is classified as an orphan receptor and suggested to play a role in sperm cell division and maturation. BRS-3 interacts with known naturally-occurring bombesin-related peptides with low affinity; however, no endogenous high-affinity ligand to the receptor has been identified. The bombesin receptor family belongs to the seven transmembrane rhodopsin-like G-protein coupled receptors (class A GPCRs), which perceive extracellular signals and transduce them to guanine nucleotide-binding (G) proteins
YVVPILFALIFLVGVLGNGTLILIFLRNKSMRNVPNIFILSLALGDLLLLLTCVPFTSTIYTLDSWPFGE
FLCKLSEFLKDTSIGVSVFTLTALSADRYFAIVNPMRKHRSQATRRTLVTAASIWIVSILLAIPEAIFSH
VVTFTLTDNQTIQICYPYPQELGPNYPKIMVLLRFLVYYLIPLLIIGVFYVLMARHLIRSTRNIGSGQNQ
AAQRQIEARKKVAKTVLAFVVLFAVCWLPRHVFMLWFHFAPNGLVDYNAFWHVLKIVGFCLSFINSCVNP
VALYLLSGSFRRHF
>gnl|CDD|320594 cd15928, 7tmA_GHSR-like, growth hormone secretagogue receptor, motilin receptor, and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This subfamily includes growth hormone secretagogue receptor (GHSR or ghrelin receptor), motilin receptor (also called GPR38), and related proteins. Both GHSR and GPR38 bind peptide hormones. Ghrelin, the endogenous ligand for GHSR, is an acylated 28-amino acid peptide hormone produced by ghrelin cells in the gastrointestinal tract. Ghrelin is also called the hunger hormone and is involved in the regulation of growth hormone release, appetite and feeding, gut motility, lipid and glucose metabolism, and energy balance. Motilin, the ligand for GPR38, is a 22 amino acid peptide hormone expressed throughout the gastrointestinal tract and stimulates contraction of gut smooth muscle. It is involved in the regulation of digestive tract motility
AAVTAVCSVLMLVGASGNLLTVLVIGRSRDMRTTTNLYLSSLAVSDLLIFLVLPLDLYRLWRYRPWRFGD
LLCRLMYFFSETCTYASILHITALSVERYLAICHPLRAKVLVTRGRVKLLIAVIWAVAIVSAGPALVLVG
VEHIQGQQTPRGFECTVVNVSSGLLSVMLWVSTSFFFVPMVCLSLLYGLIGRALWDRRQRSRTAGASRRD
NNHRQTVRMLAVIVLAFVLCWLPFHVGRVIFNHSRASTKHLHYVSQYFNLVSFVLFYLSAAINPILYNLM
SKRYRYAV
>gnl|CDD|341353 cd15929, 7tmB1_GlucagonR-like, glucagon receptor-like subfamily, member of the class B family of seven-transmembrane G protein-coupled receptors. This group represents the glucagon receptor family of G protein-coupled receptors, which includes glucagon receptor (GCGR), glucagon-like peptide-1 receptor (GLP1R), GLP2R, and closely related receptors. These receptors are activated by the members of the glucagon (GCG) peptide family including GCG, glucagon-like peptide 1 (GLP1), and GLP2, which are derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways
LSSLQVMYTVGYSLSLAALVLALAILLGLRKLHCTRNYIHANLFASFILRALSVLVKDALLPRRYSQKGD
QDLWSTLLSNQASLGCRVAQVLMQYCVAANYYWLLVEGLYLHTLLVLAVFSERSIFRLYLLLGWGAPVLF
VVPWGIVKYLYENTGCWTRNDNMAYWWIIRLPILLAILINFFIFVRILKILVSKLRANQMCKTDYKFRLA
KSTLTLIPLLGVHEVVFAFVTDEQARGTLRFIKLFFELFLSSFQGLLVAVLYCFANKEVQSELRKKWHR
>gnl|CDD|320596 cd15930, 7tmB1_Secretin_R-like, secretin receptor-like group of hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors. This group represents G protein-coupled receptors for structurally similar peptide hormones that include secretin, growth-hormone-releasing hormone (GHRH), pituitary adenylate cyclase activating polypeptide (PACAP), and vasoactive intestinal peptide (VIP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Secretin, a polypeptide secreted by entero-endocrine S cells in the small intestine, is involved in maintaining body fluid balance. This polypeptide regulates the secretion of bile and bicarbonate into the duodenum from the pancreatic and biliary ducts, as well as regulates the duodenal pH by the control of gastric acid secretion. Studies with secretin receptor-null mice indicate that secretin plays a role in regulating renal water reabsorption. Secretin mediates its biological actions by elevating intracellular cAMP via G protein-coupled secretin receptors, which are expressed in the brain, pancreas, stomach, kidney, and liver. GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. All B1 subfamily GPCRs are able to increase intracellular cAMP levels by coupling to adenylate cyclase via a stimulatory Gs protein. However, depending on its cellular location, some members of subfamily B1 are also capable of coupling to additional G proteins such as G(i/o) and/or G(q) proteins, thereby leading to activation of phospholipase C and intracellular calcium influx
YLTVKIIYTVGYSLSLTSLTTAMIILCLFRKLHCTRNYIHMNLFVSFILRAIAVFIKDAVLFSSEDVDHC
FVSTVGCKASMVFFQYCVMANFFWLLVEGLYLHTLLVISFFSERRYFWWYVLIGWGAPTVFVTVWIVARL
YFEDTGCWDINDESPYWWIIKGPILISILVNFVLFINIIRILLQKLRSPDIGGNESSQYKRLARSTLLLI
PLFGIHYIVFAFFPENISLGIRLYFELCLGSFQGFVVAVLYCFLNGEVQAEIKRKWRS
>gnl|CDD|320597 cd15931, 7tmB2_EMR_Adhesion_II, EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors. group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. On the other hand, EMR2 generates four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment
DPFLEWINRVGVIVSLFCLGLAIFTFLLCRWIPKINTTAHLHLCLCLSMSHTLFLAGIEYVENELACTVM
AGLLHYLFLASFVWMLLEALQLHLLVRRLTKVQVIQRDGLPRPLLCLIGYGVPFLIVGVSALVYSDGYGE
AKMCWLSQERGFNWSFLGPVIAIIGINWILFCATLWCLRQTLSNMNSDISQLKDTRLLTFKAVAQLFILG
CTWVLGLFQTNPVALVFQYLFTILNSLQGAFLFLVHCLLNKEVREEYIKWLT
>gnl|CDD|320598 cd15932, 7tmB2_GPR116-like_Adhesion_VI, orphan GPR116 and related proteins, group IV adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors. group VI adhesion GPCRs consist of orphan receptors GPR110, GPR111, GPR113, GPR115, GPR116, and closely related proteins. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR110 possesses a SEA box in the N-terminal has been identified as an oncogene over-expressed in lung and prostate cancer. GPR113 contains a hormone binding domain and one EGF (epidermal grown factor) domain. GPR112 has extremely long N-terminus (about 2,400 amino acids) containing a number of Ser/Thr-rich glycosylation sites and a pentraxin (PTX) domain. GPR116 has two C2-set immunoglobulin-like repeats, which is found in the members of the immunoglobulin superfamily of cell surface proteins, and a SEA (sea urchin sperm protein, enterokinase, and a grin)-box, which is present in the extracellular domain of the transmembrane mucin (MUC) family and known to enhance O-glycosylation. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS
SPALDYITYVGLGISILSLVLCLIIEALVWKSVTKNKTSYMRHVCLVNIALSLLIADIWFIIGAAISTPP
NPSPACTAATFFIHFFYLALFFWMLTLGLLLFYRLVLVFHDMSKSTMMAIAFSLGYGCPLIIAIITVAAT
APQGGYTRKGVCWLNWDKTKALLAFVIPALAIVVVNFIILIVVIFKLLRPSVGERPSKDEKNALVQIGKS
VAILTPLLGLTWGFGLGTMIDPKSLAFHIIFAILNSFQGFFILVFGTLLDSKVREALL
>gnl|CDD|320599 cd15933, 7tmB2_GPR133-like_Adhesion_V, orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors. group V adhesion GPCRs include orphan receptors GPR133, GPR144, and closely related proteins. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the G(s) protein, leading to activation of adenylate cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS
ERALSIISYIGCGISIACLALTLIIFLVLRVLSSDRFQIHKNLCVALLLAQILLLAGEWAEGNKVACKVV
AILLHFFFMAAFSWMLVEGLHLYLMIVKVFNYKSKMRYYYFIGWGLPAIIVAISLAILFDDYGSPNVCWL
SLDDGLIWAFVGPVIFIITVNTVILILVVKITVSLSTNDAKKSQGTLAQIKSTAKASVVLLPILGLTWLF
GVLVVNSQTIVFQYIFVILNSLQGLMIFLFHCVLNSEVRSAF
>gnl|CDD|320600 cd15934, 7tmC_mGluRs_group2_3, metabotropic glutamate receptors in group 2 and 3, member of the class C family of seven-transmembrane G protein-coupled receptors. The metabotropic glutamate receptors (mGluRs) are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. The mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group I mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to (Gi/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity
PWAIVPVVFALLGILATLFVIVVFIRYNDTPVVKASGRELSYVLLTGILLCYLMTFVLLAKPSVITCALR
RLGLGLGFSICYAALLTKTNRISRIFNSGKRSAKRPRFISPKSQLVICLGLISVQLIGVLVWLVVEPPGT
RIDYPRRDQVVLKCKISDSSLLISLVYNMLLIILCTVYAFKTRKIPENFNEAKFIGFTMYTTCIIWLAFV
PIYFGTSNDFKIQTTTLCVSISLSASVALGCLFAPKVYIILF
>gnl|CDD|320601 cd15935, 7tmA_OR4Q3-like, olfactory receptor 4Q3 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor 4Q3 and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
LLLFVLVLACYAAILLGNLLIVVTVHADPHLLQSPMYFFLANLSLIDMTLGSVAVPKVLADLLTCGRTIS
FGGCMAQLFFLHFLGGSEMLLLTLMAYDRYVAICHPLRYLAVMNRQLCIKLLAACWAGGFLHSATQAALV
LRLPFCGPNELDNFYCDVPQVIKLACMDTYVVEVLMVANSGLLSLVCFLVLLVSYGIILTTLRGRFREGG
GKALSTCSSHLTVVSLIFVPCIFVYLRPFSSSSVDKVASVFYTLITPALNPLIYTLRN
>gnl|CDD|320602 cd15936, 7tmA_OR4D-like, olfactory receptor 4D and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 4D and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
FFLFLVFLLVYLTTWLGNLLIIITVISDPHLHTPMYFLLANLAFLDISFSSVTAPKMLSDLLSQTKTISF
NGCMAQMFFFHFTGGAEVFLLSVMAYDRYIAIHKPLHYLTIMNQGVCTGLVAGSWLGGFAHSIVQVALLL
QLPFCGPNVLDNFYCDVPQVIKLACTDTFLLELLMVSNSGLVTLLIFFILLISYTVILVKIRTHVTEGKR
KALSTCASQITVVTLIFVPCIYIYARPFQTFPMDKAVSVLYTVITPMLNPMIYTLRN
>gnl|CDD|320603 cd15937, 7tmA_OR4N-like, olfactory receptor 4N, 4M, and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 4N, 4M, and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
LLLFVLFLLFYLIILPGNILIILTIQGDPQLGSPMYFFLANLALLDICYSSITPPKMLADFFSERKTISY
GGCMAQLFFLHFLGAAEMFLLVAMAYDRYVAICKPLHYTTVVNRRVCCVLVGASWAGGFIHSIIQVALII
RLPFCGPNVLDNFFCDITQVIKLACTNTYTVELLMFSNSGLVILLCFLLLLISYAFLLAKLRTHSSKGKS
KAASTCITHIIIVFVMFGPAIYIYARPFRSFPMDKVVAVFHTVIFPLLNPMIYTLRN
>gnl|CDD|320604 cd15938, 7tmA_OR4Q2-like, olfactory receptor 4Q2 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor 4Q2 and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
ALLFALFLLAYTMVLVGNLLIMVTVRSDPKLSSPMYFLLGNLSFLDLCYSTVTCPKMLVDFLSQRKAISY
EACIAQLFFLHFVGAAEMFLLTVMAYDRYVAICKPLHYTTIMSRRLCWVLVAASWAGGFLHSIVQTLLTI
QLPFCGPNQVNNFFCDVPPVIKLACTDTCVTELLMVSNSGLISTVCFVVLVTSYTTILVTIRSTEGRRKA
LSTCASHLMVVTLFFGPCIFIYARPFSTFPVDKHVSVLYNVITPMLNPLIYTLRN
>gnl|CDD|320605 cd15939, 7tmA_OR4A-like, olfactory receptor 4A and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 4A, 4C, 4P, 4S, 4X and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
KICFVVFLLIYLATVLGNLLIVVTIKASQTLGSPMYFFLSYLSFIDICYSSTTAPKLIVDLLSERKTISF
NGCMTQLFAEHFFGGAEIFLLTVMAYDRYVAICKPLHYTTIMNRRVCGLLVGVAWVGGFLHSTIQILLTL
QLPFCGPNVIDHFFCDLFPLLKLACTDTYVIGLLVVANSGLICLLSFLILLISYIVILYSLRTHSSEGRR
KALSTCGSHITVVVLFFVPCIFIYMRPVTTFPIDKVVAVFYTIITPMLNPLIYTLRN
>gnl|CDD|320606 cd15940, 7tmA_OR4E-like, olfactory receptor 4E and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 4E and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
LAFFMLFLVLYLLTLSGNILIMITIVMDPRLHTPMYFFLSNLSFIDICHSSVTVPKMLSDLLSEEKTISF
NGCVTQLFFLHLFACTEIFLLTIMAYDRYVAICNPLHYPTVMNHKVCLWLVAALWLGGTVHSLAQTFLTI
RLPYCGPNEIDSFFCDVPPVIKLACTDTYLIDILIVSNSGLISLVCFVALLGSYIVILVSLRKRSTEGRR
KALSTCASHLTVVTLFFGPCIFIYTRPSTSFSEDKVVSVFYTVVTPLLNPIIYTLRN
>gnl|CDD|320607 cd15941, 7tmA_OR10S1-like, olfactory receptor subfamily 10S1 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor 10S1 and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
SLFFLLFLLIYLLTVLGNLLILLTIGSDPHLHGLPMYHFLGHLSFLDACLSSVTVPKVLAGLLTLSGRTI
SFEGCVVQLYAFHFLASTECFLYTVMAYDRYLAICHPLHYPTAMNRRMCAGLAGGTWATGATHAAIHTSL
TFRLPYCGPCQIAYFFCDIPPVLKLACADTTINELVILANIGIVAAGCFLLIVISYIYIVAAVLRIRTAE
GRQRAFSTCSAHLTGVLLYYVPSVFIYLQPSSSQAGAGAPAVFYTIVTPMLNPFIYTLRNKEVKRAL
>gnl|CDD|320608 cd15942, 7tmA_OR10G6-like, olfactory receptor subfamily 10G6 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor 10G6 and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
APLFLFFLVVYLLTLSGNSLIILVVISDLQLHKPMYWFLCHLSILDMAVSTVVVPKVIAGFLSGGRIISF
GGCVTQLFFFHFLGCAECFLYTVMAYDRFLAICKPLHYSTIMNHRACLCLSLGTWLGGCLHSTFQTSLTF
RLPYGQKNEVDYIFCDIPAMLKLACADTAFNELVTFIDIGLVAMTCFLLILMSYVYIVSAILKIPSAEGQ
RRAFSTCTAHLTVVVIYYVPLTFIYLRPGSQDPLDGVVAVFYTTVTPLLNPVIYTLRNKEMKDAL
>gnl|CDD|320609 cd15943, 7tmA_OR5AP2-like, olfactory receptor subfamily 5AP2 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 5AP2 and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
EFILLGLTDNPELQVILFAVFLVIYLITLVGNLGMIVLIRLDSRLHTPMYFFLSHLSFLDLCYSSAITPK
MLVNFLAENKTISFTGCAAQMYFFVAFATTECFLLAVMAYDRYVAICNPLLYTVIMSPRVCIQLVAGSYL
IGFVNALIQTICTFRLPFCGSNVINHFFCDVPPLLKLSCSDTHVNEIVLFAFAIFLGIFTSLEILVSYVY
ILSAILRIHSSEGRRKAFSTCASHLMAVTIFYGTTLFMYLRPSSSYSLDQDKVVSVFYTVVIPMLNPLIY
SLRNKEVKDALRRIL
>gnl|CDD|320610 cd15944, 7tmA_OR5AR1-like, olfactory receptor subfamily 5AR1 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 5AR1 and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
FILLGFTQDPQMQIILFVVFLIIYLVNVVGNLGMIILITTDSQLHTPMYFFLCNLSFCDLGYSSAIAPRM
LADFLTKHKVISFSGCATQFAFFVGFVDAECYVLAAMAYDRYVAICNPLLYSTLMSKRVCLQLMAGSYLA
GLVNLVIHTTATFSLSFCGSNIINHFFCDVPPLLALSCSDTHINEILLYVFCGFVEMSSLSIILISYLFI
LVAILRMRSAEGRRKAFSTCASHFTGVTLFYGTVIFMYLRPTSVYSLDQDKWASVFYTVVIPMLNPLIYS
LRNKDVKEAFKKLI
>gnl|CDD|320611 cd15945, 7tmA_OR5C1-like, olfactory receptor subfamily 5C1 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 5C1 and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
FILLGFTDYLSLKVTLFLVFLLVYLLTLVGNVGMIILIRMDSQLHTPMYYFLSNLSFLDLCYSTAIGPKM
LVDLLAKRKSIPFYGCALQMFFFAAFADAECLLLAVMAYDRYVAICNPLLYTTAMSRRVCYLLLVGAYLS
GMATSLVHTTLTFRLSFCGSNTINHFFCDIPPLLALSCSDTQINELLLFALCGFIQTSTFLAIIISYCYI
IITVLKIRSAEGRFKAFSTCASHLTAVGLFYGTLLFMYLRPSSSYSLDTDKMTSVFYTLVIPMLNPLIYS
LRNKDVKEALKK
>gnl|CDD|320612 cd15946, 7tmA_OR1330-like, olfactory receptor 1330 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes olfactory receptors 1330 from mouse, Olr859 from rat, and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
SILFAVFLLIYLSILLGNGLIITLICLDSRLHTPMYFFLSVLSLLDMSYVTTTVPQMLVHLLSHKKTISF
TGCVAQMYIFLALGITECTLFSVMAYDRYVAICHPLRYKVIMSWGLCILMVAGSWVCGVFSSLLHTFFTM
RLPYCGPNEINHYFCEVPAVLKLACADTSLNEMVDFVLGVIVLVVPLSLILASYVNIFKAILKIRSTQGR
CKAFSTCASHITVVTMFYGPAMFMYMRPGSNYSPERDKKISLFYNVFTALLNPVIYSLRN
>gnl|CDD|320613 cd15947, 7tmA_OR2B-like, olfactory receptor subfamily 2B and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor family 2 (subfamilies 2B, 2C, 2G, 2H, 2I, 2J, 2W, 2Y) and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
MPLFVVVLIFYLLTLLGNTAIILLSLLDPRLHTPMYFFLSNLSFLDLCFTTSIVPQMLVNLWGPDKTISY
GGCVTQLYIFLWLGSTECVLLAVMAFDRYVAVCRPLHYTVIMHPRLCVQLAALSWLSGLANSLLQTTLTL
QLPLCGHHTLDHFFCEVPALIKLACVDTTFNELELFVASVFFLLVPLSLILVSYGFIARAVLRIKSAEGR
RKAFGTCSSHLLVVSLFYGTAIYMYLQPPSSYSQDQGKFISLFYTVVTPTLNPLIYTLRN
>gnl|CDD|320614 cd15948, 7tmA_OR52K-like, olfactory receptor subfamily 52K and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 52K and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
HPWISIPFCSAFTVALLGNCTLLYVIKTEPSLHEPMFYFLAMLAVIDLVLSTTTVPKILSIFWFNSREIN
FNACLVQMFFLHSFSIMESAVLLAMAFDRYVAICNPLRYATILTNSVITKIGLAALARAVTLMTPLPFLL
RRLPYCRSHVIAHCYCEHMAVVKLACGDTRFNNIYGIAVALFIVGLDLMFIILSYVFILRAVLSLASKEE
QLKAFGTCGSHICAILVFYTPVVLSSTMHRFARHVAPHVHILLANFYLLFPPMMNPIVYGVKTKQIR
>gnl|CDD|320615 cd15949, 7tmA_OR52M-like, olfactory receptor subfamily 52M and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 52M and related proteins in other mammals, sauropsids, and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
PSTFILLGIPGLEPLHVWISIPFCSMYLIAVLGNCTILFIIKSEPSLHQPMYFFLSMLAIIDLVLSTSTM
PKLLAIFWFSSNEIPLHACLLQMFLIHSFSAIESGIFLAMAFDRYVAICNPLRHKTILTNTTVIRIGLAA
VIRGVLYISPLPLLVRRLPWYRTNIIAHSYCEHMAVVGLACGDVSINNHYGLTIGFLVLIMDSLFIVLSY
IMILRVVQRLATSEARLKTFGTCVSHVCAILAFYVPIAVSSLIHRFGQNVPPPTHILLANFYLLIPPMLN
PIVYGVRTKQIQ
>gnl|CDD|320616 cd15950, 7tmA_OR52I-like, olfactory receptor subfamily 52I and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 52I and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
FWIAIPFCSMYVIALLGNGTILLVIKLDPSLHEPMYYFLCMLAVIDLVMSTSIVPKMLSIFWLGSAEISF
EACFTQMFFVHSFTAVESGVLLAMAFDRYVAICHPLRYSAILTSQVIAQIGLAIVLRALLFMTPLTCLVT
SLPYCGSRVVPHSYCEHMAVVKLACADPRPSSLYSITGSTLVVGTDSAFIAVSYGLILRAVLGLSSKEAR
LKAFSTCGSHVCVILLFYIPGLLSIYTQRFGQGVPPHTQVLLADLYLLVPPMLNPIIYGMRTKQI
>gnl|CDD|320617 cd15951, 7tmA_OR52R_52L-like, olfactory receptor subfamily 52R, 52L, and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamilies 52R, 52L and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
VWISIPFCIMYAVALLGNFTILFIVKTEPSLHEPMYLFLCMLAITDLVLSTSTLPKMLSIFWFNSREIDF
SACLTQMFFIHSFSTMESGIFVAMALDRYVAICNPLRHSTILTNSVVAKIGLAVVLRGGILVSPHPFLLR
RLPYCRTNIIPHTYCEHMAVVKLACADTRVSRAYGLSVAFLVGGLDVIFIAVSYIQILRAVFKLPSKEAR
LKTFGTCGSHICVILVFYIPALFSFLTHRFGHNVPPHVHILIANVYLLVPPMLNPIIYGVRTKQI
>gnl|CDD|320618 cd15952, 7tmA_OR52E-like, olfactory receptor subfamily 52E and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 52E and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
FWIGFPFCAVYLIALLGNCTILFVIKTEQSLHQPMFYFLAMLSTIDLGLSTATIPKMLGIFWFNLREISF
GGCLAQMFFIHTFTGMESAVLVAMAFDRYVAICNPLRYTTILTNKVISVIALGIVLRPLLLVLPFVFLIL
RLPFCGHNIIPHTYCEHMGIAKLACASIRINIIYGLFAISVLVLDVILIALSYVLILRAVFRLPSHDARL
KALSTCGSHVCVILAFYTPALFSFLTHRFGHNIPRYIHILLANLYVVLPPMLNPVIYGVRTKQI
>gnl|CDD|341354 cd15953, 7tmA_OR52P-like, olfactory receptor subfamily 52P and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 52P and related proteins in other mammals, sauropsids and amphibians. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
IWISIPFCLMYIVTLLGNCTILFVVGKEQSLHKPMYLLLCMLALTDLVLSTSVVPKALCIFWFNLKEITF
SGCLTQMFFIHTLSIMESAVLVAMAFDRYVAICNPLRYATILTNSRIAKLGLVGLIRGVLLILPLPLLLS
RLPFCANRIIPHTYCEHMAVVKLACGDTTINRIYGLVVALLVVGLDLLLIALSYALIIRAVLRLSSKKAR
QKALNTCTAHICVILMSYTPALFSFLTHRFGQGIAPHIHIILANLYLLVPPMLNPIIYGVKTKEI
>gnl|CDD|320620 cd15954, 7tmA_OR52N-like, olfactory receptor subfamily 52N and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 52N and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
IWISIPFCFMYIIAMVGNCGLLYLIWIEEALHRPMYYFLSMLSFTDITLCTTMVPKAMCIFWFNLKEISF
NACLVQMFFVHTFTGMESGVLMLMALDRYVAICYPLRYATILTNPVITKAGLATFLRGVMLIIPFPLLTK
RLPYCRGNFIPHTYCDHMSVVKLACANIRVDAIYGLMVALLIGGFDILCISVSYAMILRAVVSLSSKEAR
SKAFSTCTAHICAIVITYTPAFFTFFAHRFGGHHITPHIHIIMANLYLLLPPMMNPIVYGVKTKQI
>gnl|CDD|320621 cd15955, 7tmA_OR52A-like, olfactory receptor subfamily 52A and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 52A and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
HWIGIPFCIMFLLAVLGNCTLLIVIKRERSLHQPMYIFLAMLAATDLGLCPCILPKMLAIFWFQLREISF
NACLAQMFFIHTLQAFESGILLAMALDRYVAICHPLRHSSILTPQVLLGIGVLVVVRAVVLIIPCPLLIK
LRLHHFRSTVISHSYCEHMAVVKLAADDVRVNKIYGLFVAFSILGFDIIFITTSYALIFRAVFRLPQKEA
RLKAFNTCTAHIFVFLLFYTLAFFSFFAHRFGHHVAPYVHILLSNLYLLVPPVLNPIVYGVKTKQI
>gnl|CDD|320622 cd15956, 7tmA_OR52W-like, olfactory receptor subfamily 52W and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes human olfactory receptor subfamily 52W and related proteins in other mammals and sauropsids. Olfactory receptors (ORs) play a central role in olfaction, the sense of smell. ORs belong to the class A rhodopsin-like family of G protein-coupled receptors and constitute the largest multigene family in mammals of approximately 1,000 genes. More than 60% of human ORs are non-functional pseudogenes compared to only about 20% in mouse. Each OR can recognize structurally similar odorants, and a single odorant can be detected by several ORs. Binding of an odorant to the olfactory receptor induces a conformational change that leads to the activation of the olfactory-specific G protein (Golf). The G protein (Golf and/or Gs) in turn stimulates adenylate cyclase to make cAMP. The cAMP opens cyclic nucleotide-gated ion channels, which allow the influx of calcium and sodium ions, resulting in depolarization of the olfactory receptor neuron and triggering an action potential which transmits this information to the brain. A consensus nomenclature system based on evolutionary divergence is used here to classify the olfactory receptor family. The nomenclature begins with the root name OR, followed by an integer representing a family, a letter denoting a subfamily, and an integer representing the individual gene within the subfamily
VWLSLPFCFIYVLSLLGNGVLLSVVWKEHRLHQPMFLFLAMLAATDLVLALSTAPKLLAILWFGATAISS
YVCLSQMFLVHAFSAMESGVLVAMALDRFVAICNPLHYATILTLEVVAKAGLLLALRGVAIVIPFPLLVC
RLSFCASHTIAHTYCEHMAVVKLACGATTVDSLYGLALALFIGGGDVLFIAYSYGLIVKTVLRLPSPEAR
GKAFSTCSAHICVILFFYIPGLLSVLMHRFGHSVPSAAHVLLSNLYLLLPPALNPIVYGIRTKQI
>gnl|CDD|341355 cd15957, 7tmA_Beta2_AR, beta-2 adrenergic receptors (adrenoceptors), member of the class A family of seven-transmembrane G protein-coupled receptors. Beta-2 AR is activated by adrenaline that plays important roles in cardiac function and pulmonary physiology. While beta-1 AR and beta-2 AR are the major subtypes involved in modulating cardiac contractility and heart rate by positively stimulating the G(s) protein-adenylate cyclase-cAMP-PKA signaling pathway, beta-2 AR can couple to both G(s) and G(i) proteins in the heart. Moreover, beta-2 AR activation leads to smooth muscle relaxation and bronchodilation in the lung. The beta adrenergic receptors are a subfamily of the class A rhodopsin-like G protein-coupled receptors
VGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILLKTWTFGN
FWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHW
YRATHQEAINCYAEETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRFHNQ
NIDQNGSGGGGGNRRRSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIG
YVNSGFNPLIYCRSPDFRIAF
>gnl|CDD|320624 cd15958, 7tmA_Beta1_AR, beta-1 adrenergic receptors (adrenoceptors), member of the class A family of seven-transmembrane G protein-coupled receptors. The beta-1 adrenergic receptor (beta-1 adrenoceptor), also known as beta-1 AR, is activated by adrenaline (epinephrine) and plays important roles in regulating cardiac function and heart rate. The human heart contains three subtypes of the beta AR: beta-1 AR, beta-2 AR, and beta-3 AR. Beta-1 AR and beta-2 AR, which expressed at about a ratio of 70:30, are the major subtypes involved in modulating cardiac contractility and heart rate by positively stimulating the G(s) protein-adenylate cyclase-cAMP-PKA signaling pathway. In contrast, beta-3 AR produces negative inotropic effects by activating inhibitory G(i) proteins. The aberrant expression of betrayers can lead to cardiac dysfunction such as arrhythmias or heart failure
AGMSLLMALIVLLIVAGNVLVIVAIGRTQRLQTLTNLFITSLACADLVMGLLVVPFGATLVVRGRWLYGS
FFCELWTSVDVLCVTASIETLCVIAIDRYLAITSPFRYQSLLTRARAKGIVCTVWAISALVSFLPIMMHW
WRDEDDQALKCYEDPGCCDFVTNRAYAIASSIISFYIPLLIMIFVYLRVYREAKKQIKKIDKCEGRFHNT
LTGLGRKCKRRPSRILALREQKALKTLGIIMGVFTLCWLPFFLVNVVNVFNRELVPDWLFVFFNWLGYAN
SAFNPIIYCRSPDFRKAF
>gnl|CDD|320625 cd15959, 7tmA_Beta3_AR, beta-3 adrenergic receptors (adrenoceptors), member of the class A family of seven-transmembrane G protein-coupled receptors. The beta-3 adrenergic receptor (beta-3 adrenoceptor), also known as beta-3 AR, is activated by adrenaline and plays important roles in regulating cardiac function and heart rate. The human heart contains three subtypes of the beta AR: beta-1 AR, beta-2 AR, and beta-3 AR. Beta-1 AR and beta-2 AR, which expressed at about a ratio of 70:30, are the major subtypes involved in modulating cardiac contractility and heart rate by positively stimulating the G(s) protein-adenylate cyclase-cAMP-PKA signaling pathway. In contrast, beta-3 AR produces negative inotropic effects by activating inhibitory G(i) proteins. The aberrant expression of betrayers can lead to cardiac dysfunction such as arrhythmias or heart failure
WLAGALLSLAILVIVGGNLLVIVAIAKTPRLQTMTNVFVTSLACADLVMGLLVVPPGATILLTGHWPLGT
TVCELWTSVDVLCVTASIETLCAIAVDRYLAITNPLRYEALVTKRRARTAVCLVWAISAAISFLPIMNQW
WRDGADEEAQRCYDNPRCCDFVTNMPYAIVSSTVSFYVPLLVMIFVYVRVFVVATRQVRLIRKDKVRFPP
EESPPAESRPACGRRPSRLLAIKEHKALKTLGIIMGTFTLCWLPFFVANIIKVFCRSLVPDPAFLFLNWL
GYANSAFNPIIYCRSPDFRSAF
>gnl|CDD|320626 cd15960, 7tmA_GPR185-like, G protein-coupled receptor 185 and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR185, also called GPRx, is a member of the constitutively active GPR3/6/12 subfamily of G protein-coupled receptors. It plays a role in the maintenance of meiotic arrest in Xenopus laevis oocytes through G(s) protein, which leads to increased cAMP levels. In Xenopus laevis, GPR185 is primarily expressed in brain, ovary, and testis; however, its ortholog has not been identified in other vertebrate genomes. GPR3, GPR6, and GPR12 form a subfamily of constitutively active G-protein coupled receptors with dual coupling to G(s) and G(i) proteins. These three orphan receptors are involved in the regulation of cell proliferation and survival, neurite outgrowth, cell clustering, and maintenance of meiotic prophase arrest
SPWDIALCVTGTVMACENAIVIAILFYTPSLRAPMFILIGSLALADLLAGLGLIANFVAIYVMNSEAVTL
CSAGLLLAAFSASVCSLLAITVDRYLSLYNALTYHTERTLTFTYGLLALLWLTCIGIGLLPAMGWNCLRA
PASCSVLRPVTKNNAAVLAVSFLLLFALMMQLYLQICRIAFRHAQQIAVQHQFVNFCLASSTRKGVSTLS
LILATFAFCWVPFAVYSMVADSSYPMIYTYYLVLPAACNSVINPIIYAFRNPDIQKSL
>gnl|CDD|320627 cd15961, 7tmA_GPR12, G protein-coupled receptor 12, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR3, GPR6, and GPR12 form a subfamily of constitutively active G-protein coupled receptors with dual coupling to G(s) and G(i) proteins. These three orphan receptors are involved in the regulation of cell proliferation and survival, neurite outgrowth, cell clustering, and maintenance of meiotic prophase arrest. They constitutively activate adenylate cyclase to a similar degree as that seen with fully activated G(s)-coupled receptors, and are also able to constitutively activate inhibitory G(i/o) proteins. Lysophospholipids such as sphingosine 1-phosphate (S1P) and sphingosylphosphorylcholine have been detected as the high-affinity ligands for Gpr6 and Gpr12, respectively, which show high sequence homology with GPR3
NPWDIVLCTSGTLISCENAIVVLIIFQNPSLRAPMFLLIGSLALADLLAGIGLILNFIFAYLLQSEAAKL
VTVGLIVASFSASVCSLLAITVDRYLSLYYALTYNSERTVTFTYVMLVLLWGASICLGLLPVMGWNCLAD
ESTCSVVRPLTKNNAAILSVSFLLMFALMLQLYIQICKIVMRHAHQIALQHHFLATSHYVTTRKGVSTLA
IILGTFAACWMPFTLYSLIADYTYPSIYTYATLLPATYNSIINPVIYAFRNQEIQKAL
>gnl|CDD|320628 cd15962, 7tmA_GPR6, G protein-coupled receptor 6, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR3, GPR6, and GPR12 form a subfamily of constitutively active G-protein coupled receptors with dual coupling to G(s) and G(i) proteins. These three orphan receptors are involved in the regulation of cell proliferation and survival, neurite outgrowth, cell clustering, and maintenance of meiotic prophase arrest. They constitutively activate adenylate cyclase to a similar degree as that seen with fully activated G(s)-coupled receptors, and are also able to constitutively activate inhibitory G(i/o) proteins. Lysophospholipids such as sphingosine 1-phosphate (S1P) and sphingosylphosphorylcholine have been detected as the high-affinity ligands for Gpr6 and Gpr12, respectively, which show high sequence homology with GPR3
NPWDIMLCISGTVIACENAIVVAIIFYTPTLRTPMFVLIGSLATADLLAGCGLILNFVFQYVIQSETISL
ITVGFLVASFTASVSSLLAITVDRYLSLYNALTYYSEKTVLGVHLMLAATWGVSLCLGLLPVLGWNCLEE
RASCSIVRPLTKSNVTLLSASFFFIFILMLHLYIKICKIVCRHAHQIALQQHFLTASHYVATKKGVSTLA
IILGTFGASWLPFAIYCVVGDHEYPAVYTYATLLPATYNSMINPIIYAYRNQEIQRSM
>gnl|CDD|320629 cd15963, 7tmA_GPR3, G protein-coupled receptor 3, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR3, GPR6, and GPR12 form a subfamily of constitutively active G-protein coupled receptors with dual coupling to G(s) and G(i) proteins. These three orphan receptors are involved in the regulation of cell proliferation and survival, neurite outgrowth, cell clustering, and maintenance of meiotic prophase arrest. They constitutively activate adenylate cyclase to a similar degree as that seen with fully activated G(s)-coupled receptors, and are also able to constitutively activate inhibitory G(i/o) proteins. Lysophospholipids such as sphingosine 1-phosphate (S1P) and sphingosylphosphorylcholine have been detected as the high-affinity ligands for Gpr6 and Gpr12, respectively, which show high sequence homology with GPR3
NPWDVVLCISGTVISCENAIVVAVIFYTPAFRAPMFLLIGSLATADLLAGLGLILHFAFVYCIQSAPVNL
VTVGLLAPSFTASVSSLLAITIDRYLSLYNALTYYSERTVTRTYIMLILTWGASLCLGLLPVVGWNCLKD
PSTCSVVKPLTKNHLVILSISFFMVFALMLQLYAQICRIVCRHAHQIALQRHFLPTSHYVTTRKGIATLA
VILGTFASCWLPFAVYCLLGDYTYPALYTYATLLPATYNSMINPIIYAFRNQEIQKVL
>gnl|CDD|320630 cd15964, 7tmA_TSH-R, thyroid-stimulating hormone receptor (or thyrotropin receptor), member of the class A family of seven-transmembrane G protein-coupled receptors. The glycoprotein hormone receptors are seven transmembrane domain receptors with a very large extracellular N-terminal domain containing many leucine-rich repeats responsible for hormone recognition and binding. The glycoprotein hormone family includes the three gonadotropins: luteinizing hormone (LH), follicle-stimulating hormone (FSH), chorionic gonadotropin (CG), and a pituitary thyroid-stimulating hormone (TSH). The glycoprotein hormones exert their biological functions by interacting with their cognate GPCRs. Both LH and CG bind to the same receptor, the luteinizing hormone-choriogonadotropin receptor (LHCGR); FSH binds to FSH-R and TSH to TSH-R. TSH-R plays an important role thyroid physiology, and its activation stimulates the production of thyroxine (T4) and triiodothyronine (T3). Defects in TSH-R are a cause of several types of hyperthyroidism. The receptor is predominantly found on the surface of the thyroid epithelial cells and couples to the G(s)-protein and activates adenylate cyclase, thereby promoting cAMP production. TSH and cAMP stimulate thyroid cell proliferation, differentiation, and function
KFLRIVVWFVNLLAILGNVFVLLILLTSHYKLTVPRFLMCNLAFADFCMGIYLLLIASVDLHTRSEYYNH
AIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHASAIMLGGWVFCFLLAL
LPLVGVSSYAKVSICLPMDTETPLAQAYIVFVLMLNIIAFVIICACYIKIYITVRNPQYKSGDKDTKIAK
RMAVLIFTDFICMAPISFYALSAILNKPLITVSNSKILLVLFYPLNSCANPFLYAIFTKAFRRDV
>gnl|CDD|320631 cd15965, 7tmA_RXFP1_LGR7, relaxin receptor 1 (or LGR7), member of the class A family of seven-transmembrane G protein-coupled receptors. Relaxin is a member of the insulin superfamily that has diverse actions in both reproductive and non-reproductive tissues. The relaxin-like peptide family includes relaxin-1, relaxin-2, and the insulin-like (INSL) peptides such as INSL3, INSL4, INSL5 and INSL6. The relaxin family peptides share high structural but low sequence similarity, and exert their physiological functions by activating a group of four G protein-coupled receptors, RXFP1-4. Relaxin is the endogenous ligand for RXFP1, which has a large extracellular N-terminal domain containing 10 leucine-rich repeats and a unique low-density lipoprotein type A (LDLa) module which is necessary for receptor activation. Upon receptor binding, relaxin activates a variety of signaling pathways to produce second messengers such as cAMP and nitric oxide. RXFP1 is expressed in various tissues including uterus, ovary, placenta, cerebral cortex, heart, lung and kidney, among others
IVQRVFVWVVSAVTCFGNIFVICMRPYIRSENKLHAMSIISLCCADCLMGIYLFVIGAFDLKYRGEYNKH
AQLWMDSTQCQLVGSLAILSTEVSVLLLTYLTLEKYICIVYPFRCLTPGKCRTITILILIWIIGFIIAFI
PLSNKEFFRNYYGTNGVCFPLHSEQPESTGAQIYSVVIFLGLNLAAFIIIVFSYGSMFYSIHQTAIMATE
ISNHIKKEMTLAKRFFFIVFTDALCWIPIFILKLLSLLQVEIPGTISSWVVIFILPINSALNPILYTLTT
RPFKEMI
>gnl|CDD|320632 cd15966, 7tmA_RXFP2_LGR8, relaxin receptor 2 (or LGR8), member of the class A family of seven-transmembrane G protein-coupled receptors. Relaxin is a member of the insulin superfamily that has diverse actions in both reproductive and non-reproductive tissues. The relaxin-like peptide family includes relaxin-1, relaxin-2, and the insulin-like (INSL) peptides such as INSL3, INSL4, INSL5 and INSL6. The relaxin family peptides share high structural similarity, but low sequence similarity, and exert their physiological functions by activating a group of four G protein-coupled receptors, RXFP1-4. INSL3 is the endogenous ligand for RXFP2, which couples to the G(s) protein to increase intracellular cAMP levels, but also to the GoB protein to decrease cAMP formation. RXFP2 (or LGR8) is expressed in various tissues including the brain, kidney, muscle, testis, thyroid, uterus, and peripheral blood cells, among others
NILRVFVWVMAFITCFGNLFVIGMRSFIRAENKTHAMCIKILCCADCLMGVYLFFVGIFDVKYRGEYNKY
ALLWMESLQCRIIGFLAMLSTEVSVLLLTYLTLEKYLVIVFPFSNIRPGKCQTLIILISIWLVGFIIAVI
PFWNEDFFGNYYGKNGVCFPLHSDQTEKIGAKGYSTGIFLGLNLLAFIIIVFSYSSMFCSIQKTGLQTTE
VRSHIHRDVAVANRFFFIVFSDAICWIPIFLLKILSLFQVEIPGTITSWIVIFILPINSALNPILYTLTT
SFFKEKL
>gnl|CDD|320633 cd15967, 7tmA_P2Y1-like, P2Y purinoceptor 1-like. P2Y1-like is an uncharacterized group that is phylogenetically related to a family of purinergic G protein-coupled receptors. The P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5, and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12, and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-glucose (P2Y14)
QFLPPVYILVFVVGLVGNVWGLKSLLANWKKLGNINVFVLNLGLADLLYLLTLPFLVVYYLKGRKWIFGQ
VFCKITRFCFNLNLYGSIGFLTCISVYRYLAIVHPMRVMGRITTTHSVVISALVWLLVVIQSLPDLFFSK
TNSNGTKCFDTTFNDYLESYLTYSLGWTVTGFVIPLLIILGCYGHVVVVLCRNNNVDKGLKQRCLKLVII
LIVLFSVCYIPYHVFRNLNLLSRILQKQGSCTQWFRGIYIAHQVSRGLVCLNSALNPLVYLMGSEDILSR
I
>gnl|CDD|320634 cd15968, 7tmA_P2Y6_P2Y3-like, P2Y purinoceptors 6 and 3, and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. This group includes P2Y receptor 6 (P2Y6), P2Y3, and P2Y3-like proteins. These receptors belong to the G(i) class of a family of purinergic G-protein coupled receptors. In the CNS, P2Y6 plays a role in microglia activation and phagocytosis, and is involved in the secretion of interleukin from monocytes and macrophages in the immune system. The P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5, and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12, and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-glucose (P2Y14)
ILLPICYSFVFLLGLPLNSVVLTRCCRHTKAWTRTAIYMVNLALADLLYALSLPLLIYNYAMRDRWLFGD
FMCRLVRFLFYFNLYGSILFLTCISVHRYLGICHPMRPWHKETRRAAWLTCVLVWILVFAQTLPILIFAR
TGIIRNRTVCYDLAPPALFPHYVPYGMALTVSGFLLPFSIILWCYCLVVRTLCRTLGPAEPPAQARRRKS
IRTIVTVTLLFALCFLPFHITRTIYLAVRVTPGVPCHVLEAVAACYKITRPLASANSVLNPLLYFLTKKK
FGRRP
>gnl|CDD|320635 cd15969, 7tmA_GPR87, G protein-coupled receptor 87, member of the class A family of seven-transmembrane G protein-coupled receptors. GPR87 acts as one of multiple receptors for lysophosphatidic acid (LPA). This orphan receptor has been shown to be over-expressed in several malignant tumors including lung squamous cell carcinoma and regulated by p53. GPR87 is phylogenetically closely related to the G(i) class of the P2Y family of purinergic G protein-coupled receptors. P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-sugars. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase
IVFPVLYLIIFIGSILLNGLAVWIFFHIRNKTSFIFYLKNIVIADLLMTLTFPFKIIQDSGLGPWNFNFF
LCRYTSVLFYASMYTSIVFLGLISLDRYLKVVKPFGDSRMYSITFTKVLSACVWLIMAFLSLPNIILTNG
QPTEDNIHDCSKLKSPLGVKWHTAVSYINICIFVAVLVILIVCYISISRYIYKSSKQFISSSSRTRKHNQ
SIRVVVAVFFVCFLPYHLCRIPFTFSQLDKILDCTIKTILYYCKEATLFLSACNVCLDPIIYFFMCRSFS
QRL
>gnl|CDD|320636 cd15970, 7tmA_SSTR1, somatostatin receptor type 1, member of the class A family of seven-transmembrane G protein-coupled receptors. G protein-coupled somatostatin receptors (SSTRs) are composed of five distinct subtypes (SSTR1-5) that display strong sequence similarity with opioid receptors. All five receptor subtypes bind the natural somatostatin (somatotropin release inhibiting factor), a polypeptide hormone that regulates a wide variety of physiological functions such as neurotransmission, cell proliferation, contractility of smooth muscle cells, and endocrine signaling as well as inhibition of the release of many secondary hormones. SSTR1 is coupled to a Na/H exchanger, voltage-dependent calcium channels, and AMPA/kainate glutamate channels. SSTR1 is expressed in the normal human pituitary and in nearly half of all pituitary adenoma subtypes
ILISFIYSVVCLVGLCGNSMVIYVILRYAKMKTATNIYILNLAIADELLMLSVPFLVTSTLLRHWPFGSL
LCRLVLSVDAINMFTSIYCLTVLSIDRYIAVVHPIKAARYRRPTVAKMVNLGVWVFSILVILPIIIFSNT
APNSDGSVACNMQMPEPSQRWLAVFVVYTFLMGFLLPVIAICLCYILIIVKMRVVALKAGWQQRKRSERK
ITLMVMMVVTVFVICWMPFYVVQLVSVFVGQHDATVSQLSVILGYANSCANPILYGFLSDNFKRSF
>gnl|CDD|320637 cd15971, 7tmA_SSTR2, somatostatin receptor type 2, member of the class A family of seven-transmembrane G protein-coupled receptors. G protein-coupled somatostatin receptors (SSTRs), which display strong sequence similarity with opioid receptors, binds somatostatin, a polypeptide hormone that regulates a wide variety of physiological such as neurotransmission, endocrine secretion, cell proliferation, and smooth muscle contractility. SSTRs are composed of five distinct subtypes (SSTR1-5) which are encoded by separate genes on different chromosomes. SSTR2 plays critical roles in growth hormone secretion, glucagon secretion, and immune responses. SSTR2 is expressed in the normal human pituitary and in nearly all pituitary growth hormone adenomas
AFLTFIYFVVCIIGLCGNTLVIYVILRYAKMKTVTNIYILNLAIADELFMLGLPFLAIQVALVHWPFGKA
ICRVVMTVDGINQFTSIFCLTVMSIDRYLAVVHPIKSAKWRKPRTAKMINMAVWGVSLLVILPIMIYAGV
QTKHGRSSCTIIWPGESSAWYTGFIIYTFILGFFVPLTIICLCYLFIIIKVKSSGIRVGSSKRKKSEKKV
TRMVSIVVAVFVFCWLPFYIFNVSSVSVSISPTPGLKGMFDFVVVLSYANSCANPILYAFLSDNFKKSF
>gnl|CDD|320638 cd15972, 7tmA_SSTR3, somatostatin receptor type 3, member of the class A family of seven-transmembrane G protein-coupled receptors. G protein-coupled somatostatin receptors (SSTRs) are composed of five distinct subtypes (SSTR1-5) that display strong sequence similarity with opioid receptors. All five receptor subtypes bind the natural somatostatin (somatotropin release inhibiting factor), a polypeptide hormone that regulates a wide variety of physiological functions such as neurotransmission, cell proliferation, contractility of smooth muscle cells, and endocrine signaling as well as inhibition of the release of many secondary hormones. SSTR3 is coupled to inward rectifying potassium channels. SSTR3 plays critical roles in growth hormone secretion, endothelial cell cycle arrest and apoptosis. Furthermore, SSTR3 is expressed in the normal human pituitary and in nearly half of pituitary growth hormone adenomas
VLIPLVYLVVCVVGLGGNTLVIYVVLRYSASESVTNIYILNLALADELFMLGLPFLAAQNALSYWPFGSF
MCRLVMTVDAINQFTSIFCLTVMSVDRYLAVVHPIRSSKWRKPPVAKTVNATVWALSFLVVLPVVIFSGV
PGGMGTCHIAWPEPAQVWRAGFIIYTATLGFFCPLLVICLCYLLIVVKVRSSGRRVRATSTKRRGSERKV
TRMVVIVVAAFVLCWLPFYALNIVNLVCPLPEEPSLFGLYFFVVVLSYANSCANPIIYGFLSDNFKQGF
>gnl|CDD|320639 cd15973, 7tmA_SSTR4, somatostatin receptor type 4, member of the class A family of seven-transmembrane G protein-coupled receptors. G protein-coupled somatostatin receptors (SSTRs) are composed of five distinct subtypes (SSTR1-5) that display strong sequence similarity with opioid receptors. All five receptor subtypes bind the natural somatostatin (somatotropin release inhibiting factor), a polypeptide hormone that regulates a wide variety of physiological functions such as neurotransmission, cell proliferation, contractility of smooth muscle cells, and endocrine signaling as well as inhibition of the release of many secondary hormones. SSTR4 plays a critical role in mediating inflammation. Unlike other SSTRs, SSTR4 subtype is not detected in all pituitary adenomas while it is expressed in the normal human pituitary
VVIQFIYALVCLVGLIGNSMVIFVILRYAKMKTATNIYILNLAIADELFMLSVPFLAASAALQHWPFGSA
MCRTVLSVDGINMFTSVFCLTVLSVDRYIAVVHPLRAARYRRPTVAKMINICVWILSLLVISPIIIFADT
ATRKGQAVACNLIWPHPAWSAAFVIYTFLLGFLLPVLAIGLCYILIIGKMRAVALKAGWQQRRKSEKKIT
RMVLMVVTVFVICWMPFYVVQLLNLFLPRLDATVNHASLILSYANSCANPILYGFLSDNFRRSF
>gnl|CDD|320640 cd15974, 7tmA_SSTR5, somatostatin receptor type 5, member of the class A family of seven-transmembrane G protein-coupled receptors. G protein-coupled somatostatin receptors (SSTRs) are composed of five distinct subtypes (SSTR1-5) that display strong sequence similarity with opioid receptors. All five receptor subtypes bind the natural somatostatin (somatotropin release inhibiting factor), a polypeptide hormone that regulates a wide variety of physiological functions such as neurotransmission, cell proliferation, contractility of smooth muscle cells, and endocrine signaling as well as inhibition of the release of many secondary hormones. SSTR5 is coupled to inward rectifying K channels and phospholipase C, and plays critical roles in growth hormone and insulin secretion. SSTR5 acts as a negative regulator of PDX-1 (pancreatic and duodenal homeobox-1) expression, which is a conserved homeodomain-containing beta cell-specific transcription factor essentially involved in pancreatic development, among many other functions
VLIPVIYLLVCAIGLSGNTLVIYVVLRYAKMKTVTNIYILNLAVADELFMLGLPFLATQNAISYWPFGSF
LCRLVMTVDGVNQFTSIFCLTVMSIDRYLAVVHPIKSTKWRRPRVAKLINATVWTLSFLVVLPVIIFSDV
QPDLNTCNISWPEPVSVWSTAFIIYTAVLGFFGPLLVICLCYLLIVIKVKSSGLRVGSTKRRKSERKVTR
MVVIIVVVFVFCWLPFYMLNIVNLIVILPEEPAFVGVYFFVVVLSYANSCANPILYGFLSDNFKQSF
>gnl|CDD|320641 cd15975, 7tmA_ET-AR, endothelin A (or endothelin-1) receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Endothelins are able to activate a number of signal transduction processes including phospholipase A2, phospholipase C, and phospholipase D, as well as cytosolic protein kinase activation. They play an important role in the regulation of the cardiovascular system and are the most potent vasoconstrictors identified, stimulating cardiac contraction, regulating the release of vasoactive substances, and stimulating mitogenesis in blood vessels. Two endothelin receptor subtypes have been isolated and identified in vertebrates, endothelin A receptor (ET-A) and endothelin B receptor (ET-B), and are members of the seven transmembrane class A G-protein coupled receptor family which activate multiple effectors via different types of G protein. Some vertebrates contain a third subtype, endothelin A receptor (ET-C). ET-A receptors are mainly located on vascular smooth muscle cells, whereas ET-B receptors are present on endothelial cells lining the vessel wall. Endothelin receptors have also been found in the brain
YINTVLSCIIFIVGMVGNATLLRIIYQNKCMRNGPNALIASLALGDLIYIVIDIPINVYKLLAQKWPFDD
SSFGVFLCKLVPFLQKASVGITVLNLCALSVDRYRAVASWSRVQGIGIPLITAIEIFSIWVLSFILAIPE
AIGFVMVPFEYNGEQYRTCMLNATTKFMNFYVDAKDWWLFGFYFCVPLACTAIFYTLMTCEMLNRRKGSL
RIALSEHLKQRREVAKTVFCLVVIFALCWFPLHLSRILKKTVYNENDPRRCELLSFLLVMDYISINLATM
NSCINPIALYFVSKKFKNCF
>gnl|CDD|320642 cd15976, 7tmA_ET-BR, endothelin B receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Endothelins are able to activate a number of signal transduction processes including phospholipase A2, phospholipase C, and phospholipase D, as well as cytosolic protein kinase activation. They play an important role in the regulation of the cardiovascular system and are the most potent vasoconstrictors identified, stimulating cardiac contraction, regulating the release of vasoactive substances, and stimulating mitogenesis in blood vessels. Two endothelin receptor subtypes have been isolated and identified in vertebrates, endothelin A receptor (ET-A) and endothelin B receptor (ET-B), and are members of the seven transmembrane class A G-protein coupled receptor family which activate multiple effectors via different types of G protein. Some vertebrates contain a third subtype, endothelin A receptor (ET-C). ET-A receptors are mainly located on vascular smooth muscle cells, whereas ET-B receptors are present on endothelial cells lining the vessel wall. Endothelin receptors have also been found in the brain
YINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIIIDIPINVYKLLAEDWPFGV
EMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSIILAVPEAIGFD
MITMDYKGELLRICLLHPIQKTAFMQFYKTAKDWWLFSFYFCLPLACTAVFYTLMTCEMLRKKNGMQIAL
NDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTIYDEKDPNRCELLSFFLVLDYIGINMASLNSCI
NPIALYLVSKRFKNCF
>gnl|CDD|320643 cd15977, 7tmA_ET-CR, endothelin C receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. Endothelins are able to activate a number of signal transduction processes including phospholipase A2, phospholipase C, and phospholipase D, as well as cytosolic protein kinase activation. They play an important role in the regulation of the cardiovascular system and are the most potent vasoconstrictors identified, stimulating cardiac contraction, regulating the release of vasoactive substances, and stimulating mitogenesis in blood vessels. Two endothelin receptor subtypes have been isolated and identified in vertebrates, endothelin A receptor (ET-A) and endothelin B receptor (ET-B), and are members of the seven transmembrane class A G-protein coupled receptor family which activate multiple effectors via different types of G protein. Some vertebrates contain a third subtype, endothelin A receptor (ET-C). ET-A receptors are mainly located on vascular smooth muscle cells, whereas ET-B receptors are present on endothelial cells lining the vessel wall. Endothelin receptors have also been found in the brain. The ET-C receptor is specific for endothelin-3 on frog dermal melanophores; its activation causes dispersion of pigment granules
YVNTILSCVIFLVGIIGNSTLLRIIYKNKCMRNGPNVLIASLALGDLLYILIAIPINVIKLIAEDWPFGV
HVCKLYPFIQKASVGITVLSLCALSIDRYRAVASWSRIRGIGIPVWKAVEVTLIWAVAIIVAVPEAIAFD
MVEIDYRGQTLLVCMLPMEQTSSFMRFYQDVKDWWLFGFYFCLPLACTGVFYTLMSCEMLSIKNGMRIAL
NDHMKQRREVAKTVFCLVVIFALCWLPLHLSRILKKTIYDVKDPQRCELLSFLLVMDYTGINMASLNSCI
NPVALYFVSRKFKNCF
>gnl|CDD|320644 cd15978, 7tmA_CCK-AR, cholecystokinin receptor type A, member of the class A family of seven-transmembrane G protein-coupled receptors. Cholecystokinin receptors (CCK-AR and CCK-BR) are a group of G-protein coupled receptors which bind the peptide hormones cholecystokinin (CCK) or gastrin. CCK, which facilitates digestion in the small intestine, and gastrin, a major regulator of gastric acid secretion, are highly similar peptides. Like gastrin, CCK is a naturally-occurring linear peptide that is synthesized as a preprohormone, then proteolytically cleaved to form a family of peptides with the common C-terminal sequence (Gly-Trp-Met-Asp-Phe-NH2), which is required for full biological activity. CCK-AR (type A, alimentary; also known as CCK1R) is found abundantly on pancreatic acinar cells and binds only sulfated CCK-peptides with very high affinity, whereas CCK-BR (type B, brain; also known as CCK2R), the predominant form in the brain and stomach, binds CCK or gastrin and discriminates poorly between sulfated and non-sulfated peptides. CCK is implicated in regulation of digestion, appetite control, and body weight, and is involved in neurogenesis via CCK-AR. There is some evidence to support that CCK and gastrin, via their receptors, are involved in promoting cancer development and progression, acting as growth and invasion factors
TVRILLYSLIFLLSVLGNSLIIAVLIRNKRMRTVTNIFLLSLAVSDLMLCLFCMPFTLIPNLLKDFIFGS
AVCKTATYFMGISVSVSTFNLVAISLERYSAICKPLKSRVWQTKSHALKVIAATWCLSFTIMLPYPIYSN
LVPFTRINNSTGNMCRLLWPNDVTQQSWYIFLLLILFLIPGIVMMTAYGLISLELYRGIKFLMAKKRVIR
MLIVIVILFFLCWTPIFSANAWRAFDTRSADRLLSGAPISFIHLLSYTSACVNPIIYCFMNKRFRMGF
>gnl|CDD|320645 cd15979, 7tmA_CCK-BR, cholecystokinin receptor type B, member of the class A family of seven-transmembrane G protein-coupled receptors. Cholecystokinin receptors (CCK-AR and CCK-BR) are a group of G-protein coupled receptors which bind the peptide hormones cholecystokinin (CCK) or gastrin. CCK, which facilitates digestion in the small intestine, and gastrin, a major regulator of gastric acid secretion, are highly similar peptides. Like gastrin, CCK is a naturally-occurring linear peptide that is synthesized as a preprohormone, then proteolytically cleaved to form a family of peptides with the common C-terminal sequence (Gly-Trp-Met-Asp-Phe-NH2), which is required for full biological activity. CCK-AR (type A, alimentary; also known as CCK1R) is found abundantly on pancreatic acinar cells and binds only sulfated CCK-peptides with very high affinity, whereas CCK-BR (type B, brain; also known as CCK2R), the predominant form in the brain and stomach, binds CCK or gastrin and discriminates poorly between sulfated and non-sulfated peptides. CCK is implicated in regulation of digestion, appetite control, and body weight, and is involved in neurogenesis via CCK-AR. There is some evidence to support that CCK and gastrin, via their receptors, are involved in promoting cancer development and progression, acting as growth and invasion factors
TVRILLYSVIFLLSVFGNMLIIVVLGLNKRLRTVTNSFLLSLALSDLMLAVFCMPFTLIPNLMGTFIFGE
VICKAVAYLMGVSVSVSTFSLVAIAIERYSAICNPLQSRVWQTRSHAYRVIAATWLLSGLIMIPYPVYSV
TVPVPVGDRPRGHQCRHAWPSAQVRQAWYVLLLLILFFIPGVVMIVAYGLISRELYRGLLAKKRVIRMLV
VIVAMFFLCWLPIFSANTWRAFDPLSAHRALSGAPISFIHLLSYTSACVNPLVYCFMNRRFRKAF
>gnl|CDD|320646 cd15980, 7tmA_NPFFR2, neuropeptide FF receptor 2, member of the class A family of seven-transmembrane G protein-coupled receptors. Neuropeptide FF (NPFF) is a mammalian octapeptide that belongs to a family of neuropeptides containing an RF-amide motif at their C-terminus that have been implicated in a wide range of physiological functions in the brain including pain sensitivity, insulin release, food intake, memory, blood pressure, and opioid-induced tolerance and hyperalgesia. The effects of these peptides are mediated through neuropeptide FF1 and FF2 receptors (NPFF1-R and NPFF2-R) which are predominantly expressed in the brain. NPFF induces pro-nociceptive effects, mainly through the NPFF1-R, and anti-nociceptive effects, mainly through the NPFF2-R. NPFF has been shown to inhibit adenylate cyclase via the Gi protein coupled to NPFF1-R
AVFIASYLLIFLLCMMGNGVVCFIVLRSKHMRTVTNLFILNLAISDLLVGIFCMPTTLLDNIIAGWPFGS
TVCKMSGMVQGISVSASVFTLVAIAVDRFRCIVYPFKQKLTISTAVVIIVIIWVLAIAIMCPSAVMLHVQ
EEKNYRVVLGSQNKTSPVYWCREDWPNQEMRKIYTTVLFANIYLAPLSLIVIMYARIGITLFKTAMPHTG
KHNQEQRHVVSRKKQKVIKMLLIVALLFILSWLPLWTLMMLSDYANLSPNQLQIINIYIYPFAHWLAFFN
SSVNPIIYGFFNENFRRGF
>gnl|CDD|320647 cd15981, 7tmA_NPFFR1, neuropeptide FF receptor 1, member of the class A family of seven-transmembrane G protein-coupled receptors. Neuropeptide FF (NPFF) is a mammalian octapeptide that belongs to a family of neuropeptides containing an RF-amide motif at their C-terminus that have been implicated in a wide range of physiological functions in the brain including pain sensitivity, insulin release, food intake, memory, blood pressure, and opioid-induced tolerance and hyperalgesia. The effects of these peptides are mediated through neuropeptide FF1 and FF2 receptors (NPFF1-R and NPFF2-R) which are predominantly expressed in the brain. NPFF induces pro-nociceptive effects, mainly through the NPFF1-R, and anti-nociceptive effects, mainly through the NPFF2-R. NPFF has been shown to inhibit adenylate cyclase via the Gi protein coupled to NPFF1-R
AMFILAYLFIFLLCMVGNGLVCFIVLKNRQMRTVTNMFILNLAVSDLLVGIFCMPTTLVDNLITGWPFDN
AMCKMSGLVQGMSVSASVFTLVAIAVERFRCIVHPFRQKLTLRKAIVTIVIIWVLALIIMCPSAVTLTVT
REEHHFMVDDYNNSYPLYSCWEAWPDTEMRKIYTTVLFSHIYLAPLTLIVIMYARIAFKLFKSSAPIRGS
QGEEEEGRRVSKRKIKVINMLIIVALFFTLSWLPLWTLMLLTDYGHLSEDQLNLVTVYVFPFAHWLAFFN
SSVNPIIYGYFNENFRRGF
>gnl|CDD|320648 cd15982, 7tmB1_PTH2R, parathyroid hormone 2 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors. The parathyroid hormone 2 receptor (PTH2R), one of the three subtypes of PTH receptor family, is found in mammals and fish, but not in chicken or frog. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39) but not by PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs. These results suggest that TIP-39 is a natural ligand for PTH2R. Conversely, PTH1R is activated by PTH and PTHrP, but not by TIP-39. The PTH family receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways
FERLYIMYTVGYSISFSSLAVAIFIIGYFRRLHCTRNYIHMHLFVSFMLRAASIFVKDKVVHTHIGVKEL
DAVLMNDFQNAVDAPPVDKSQYVGCKIAVVMFIYFLATNYYWILVEGLYLHSLIFVAFFSDTKYLWGFTL
IGWGFPAVFVAAWAVVRATLADARCWELSAGDIKWIYQAPILAAIGLNFILFLNTVRVLATKIWETNAVG
YDTRKQYRKLAKSTLVLVLVFGVHYIVFVCLPHTFTGLGWEIRMHCELFFNSFQGFFVSIIYCYCNGEVQ
TEIKKTWTR
>gnl|CDD|320649 cd15983, 7tmB1_PTH3R, parathyroid hormone 3 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors. The parathyroid hormone 3 receptor (PTH3R), one of the three subtypes of PTH receptor family, is found in chicken and fish, but it is absent in mammals. On the other hand, the PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. PTH1R is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39), but not by PTHrP. PTH also strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs, suggesting that TIP-39 is a natural ligand for PTH2R. Conversely, PTH3R binds and responds to both PTH and PTHrP, but not the TIP-39. The PTH family receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways
FERLHLMYTIGYSISLAALLVAVCILCYFKRLHCTRNYIHIHLFASFICRAGSIFVKDAVLYSGTNEGEA
LDEKIEFGLSPGTRLQWVGCKVTVTLFLYFLATNHYWILVEGLYLHSLIFMAFLSDKNYLWALTIIGWGL
PAVFVSVWASVRVSLADTQCWDLSAGNLKWIYQVPILAAILVNFFLFLNIVRVLASKLWETNTGKLDPRQ
QYRKLLKSTLVLMPLFGVHYVLFMAMPYTDVTGLLWQIQMHYEMLFNSSQGFFVAFIYCFCNGEVQAEIK
KAWLR
>gnl|CDD|320650 cd15984, 7tmB1_PTH1R, parathyroid hormone 1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors. The parathyroid hormone (PTH) receptor family has three subtypes: PTH1R, PTH2R and PTH3R. PTH1R is expressed in bone and kidney and is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to G(s)-protein that in turn activates adenylate cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple intracellular signaling pathways. PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. PTH3R is found in chicken and fish, but it is absent in mammals. The PTH receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways
FDRLYLIYTVGYSISLGSLTVAVLILGYFRRLHCTRNYIHMHLFLSFMLRAVSIFVKDAVLYSGSALEEM
ERITEEDLKSITEAPPADKAQFVGCKVAVTFFLYFLATNYYWILVEGLYLHSLIFMAFFSEKKYLWGFTL
FGWGLPAVFVTIWASVRATLADTGCWDLSAGNLKWIIQVPILAAIVVNFILFINIVRVLATKLRETNAGR
CDTRQQYRKLLKSTLVLMPLFGVHYIVFMAMPYTEVSGILWQVQMHYEMLFNSFQGFFVAIIYCFCNGEV
QAEIKKSWSR
>gnl|CDD|320651 cd15985, 7tmB1_GlucagonR-like_1, uncharacterized group of glucagon receptor-like proteins, member of the class B family of seven-transmembrane G protein-coupled receptors. This group consists of uncharacterized proteins with similarity to members of the glucagon receptor family of G protein-coupled receptors, which include glucagon receptor (GCGR), and glucagon-like peptide-1 receptor (GLP1R), and GLP2R. The glucagon receptors are activated by the members of the glucagon (GCG) peptide family including GCG, glucagon-like peptide 1 (GLP1), and GLP2, which are derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways
MVSFRMLYTVGYTLSLLTLVSALLILTSIRKLHCTRNYIHANLFASFILRAVSVIVKDTLLERRWGREIM
RVADWGELLSHKAAIGCRMAQVVMQYCILANHYWFFVEAVYLYKLLIGAVFSEKNYYLLYLYLGWGTPVL
FVVPWMLAKYLKENKECWALNENMAYWWIIRIPILLASLINLLIFMRILKVILSKLRANQKGYADYKLRL
AKATLTLIPLFGIHEVVFIFATDEQTTGILRYIKVFFTLFLNSFQGFLVAVLYCFANKEVKSELLKKWRL
>gnl|CDD|320652 cd15986, 7tmB1_VIP-R2, vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of seven-transmembrane G protein-coupled receptors. Vasoactive intestinal peptide (VIP) receptor 2 is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. VIP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. However, depending on its cellular location, VIP-R1 is also capable of coupling to additional G proteins such as G(q) protein, thus leading to the activation of phospholipase C and intracellular calcium influx
YIVVKTIYTLGHSVSLIALTTGSTILCLFRKLHCTRNYIHLNLFFSFILRAISVLVKDDILYSSSNTEHC
TVPPSLIGCKVSLVILQYCIMANFYWLLVEGLYLHTLLVVIFSENRHFIVYLLIGWGIPTVFIIAWIVAR
IYLEDTGCWDTNDHSVPWWVIRIPIIISIILNFILFISIIRILLQKLRSPDVGGNDQSQYKRLAKSTLLL
IPLFGVHYIVFVYFPDSSSSNYQIFFELCLGSFQGLVVAILYCFLNSEVQGELKRKWRS
>gnl|CDD|320653 cd15987, 7tmB1_PACAP-R1, pituitary adenylate cyclase-activating polypeptide type 1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors. Pituitary adenylate cyclase-activating polypeptide type 1 receptor (PACAP-R1) is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and vasoactive intestinal peptide (VIP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. PACAP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level
YLSVKALYTVGYSTSLVSLTTAMVILCRFRKLHCTRNFIHMNLFVSFILRAISVFIKDGVLYAEQDSDHC
FVSTVECKAVMVFFHYCVMSNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTICVTVWAVLRL
HFDDTGCWDMNDNTALWWVIKGPVVGSIMINFVLFIGIIIILVQKLQSPDIGGNESSIYLRLARSTLLLI
PLFGIHYTVFAFSPENVSKRERLVFELGLGSFQGFVVAVLYCFLNGEVQSEIKRKWRS
>gnl|CDD|320654 cd15988, 7tmB2_BAI2, brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors. Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions
TGSPSVPLMIGCAVSCMALLILLAIYAAFWRFIRSERSIILLNFCLSILASNILILVGQSQTLSKGVCTM
TAAFLHFFFLSSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTASYC
WLSLEGGLLYAFVGPAAVIVLVNMLIGIIVFNKLMSRDGISDKSKKQRAGSEAEPCSSLLLKCSKCGVVS
SAAMSSATASSAMASLWSSCVVLPLLALTWMSAVLAMTDRRSILFQVLFAVFNSVQGFVIITVHCFLRRE
VQDVVKCQMGG
>gnl|CDD|320655 cd15989, 7tmB2_BAI3, brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors. Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions
ESSGTPSVTLIVGCGLSCLALITLAVVYAALWRYIRSERSIILINFCLSIISSNILILVGQTQTHNKGIC
TMTTAFLHFFFLASFCWVLTEAWQSYMAVTGKIRTRLIRKRFLCLGWGLPALVVAISMGFTKAKGYGTPH
YCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSRDGILDKKLKHRAGQMSEPHSGLTLKCAKCGV
VSTTALSATTASNAMASLWSSCVVLPLLALTWMSAVLAMTDKRSILFQILFAVFDSLQGFVIVMVHCILR
REVQDAFRCRLRN
>gnl|CDD|320656 cd15990, 7tmB2_BAI1, brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors. Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions
MEKALLPSVTLIVGCGVSSLTLLLLIIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVV
CTLVAAFLHFFFLSSFCWVLTEAWQSYMAVTGRLRNRIIRKRFLCLGWGLPALVVAISVGFTKAKGYGTV
NYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSKDGITDKKLKERAGASLWSSCVVLPLLALTW
MSAVLAITDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRVVDRQEEGN
>gnl|CDD|320657 cd15991, 7tmB2_CELSR1, Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of seven-transmembrane G protein-coupled receptors. The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
VLPLKIITYTTVSLSLVALLITFILLVLIRTLRSNLHSIHKNLVAALFFSELIFLIGINQTENPFVCTVV
AILLHYFYMSTFAWMFVEGLHIYRMLTEVRNINTGHMRFYYVVGWGIPAIITGLAVGLDPQGYGNPDFCW
LSVQDTLIWSFAGPIGIVVIINTVIFVLAAKASCGRRQRYFEKSGVISMLRTAFLLLLLISATWLLGLMA
VNSDTLSFHYLFAIFSCLQGIFIFFFHCIFNKEVRKHLKNVLTG
>gnl|CDD|320658 cd15992, 7tmB2_CELSR2, Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of seven-transmembrane G protein-coupled receptors. The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
ILPLKTLTWSSVGVTLGFLLLTFLFLLCLRALRSNKTSIRKNGATALFLSELVFILGINQADNPFACTVI
AILLHFFYLCTFSWLFLEGLHIYRMLSEVRDINYGPMRFYYLIGWGVPAFITGLAVGLDPEGYGNPDFCW
LSIYDTLIWSFAGPVAFAVSMNVFLYILSSRASCSAQQQSFEKKKGPVSGLRTAFTVLLLVSVTCLLALL
SVNSDVILFHYLFAGFNCLQGPFIFLSHVVLLKEVRKALKTLCGP
>gnl|CDD|320659 cd15993, 7tmB2_CELSR3, Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of seven-transmembrane G protein-coupled receptors. The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuronal migration and axon guidance in the CNS. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
LETLAIVTYSSVSASLAALVLTFSVLTCLRGLKSNTRGIHSNIAAALFLSELLFLLGINRTENQFLCTVV
AILLHYFFLSTFAWLFVQGLHIYRMQTEARNVNFGAMRFYYAIGWGVPAIITGLAVGLDPEGYGNPDFCW
ISIHDKLVWSFAGPIVVVIVMNGVMFLLVARMSCSPGQKETKKTSVLMTLRSSFLLLLLISATWLFGLLA
VNNSVLAFHYLHAILCCLQGLAVLLLFCVLNEEVQEAWKLACLG
>gnl|CDD|320660 cd15994, 7tmB2_GPR111_115, orphan adhesion receptors GPR111 and GPR115, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR111 and GPR115 are highly homologous orphan receptors that belong to group VI adhesion-GPCRs along with GPR110, GPR113, and GPR116. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS. Both GPR111 and GPR5 are present only in land-living animals and are predominantly expressed in the developing skin
NAVLDYITRIGLGLSIFSLALCLTIEAVVWSHVTKTEITYMRHVCIVNIATSLLIADVWFILASIVHNTA
LNYPLCVAATFFLHFFYLSLFFWMLTKALLILYGILLVFFKITKSVFIATAFSIGYGCPLVIAVLTVAIT
EPKKGYLRPEACWLNWDETKALLAFIIPALSIVVVNLIVVGVVVVKTQRSSIGESCKQDVSNIIRISKNV
AILTPLLGLTWGFGLATIIDSRSLPFHIIFALLNAFQGFFILLFGTILDRKIRIALY
>gnl|CDD|320661 cd15995, 7tmB2_GPR56, orphan adhesion receptor GPR56, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR56 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR64, GPR97, GPR112, GPR114, and GPR126. GPR56 is involved in the regulation of oligodendrocyte development and myelination in the central nervous system via coupling to G(12/13) proteins, which leads to the activation of RhoA GTPase. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
KHYLTILTYVGCIISALASVFTIAFYLCSRRKPRDYTIYVHMNLLLAIFLLDTSFLISEPLALTGSEAAC
RAGGMFLHFSLLACLTWMGIEGYNLYRLVVEVFNTYVPHFLLKLCAVGWGLPIFLVTLIFLVDQDNYGPI
ILAVHRSPEKVTYATICWITDSLISNITNLGLFSLVFLFNMAMLATMVVEILRLRPRTHKWSHVLTLLGL
SLVLGIPWALAFFSFASGTFQLVIVYLFTIINSLQGFLIFLWYWSMVLQARGGPSPLKS
>gnl|CDD|320662 cd15996, 7tmB2_GPR126, orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR126 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, and GPR114. GPR126 is required in Schwann cells for proper differentiation and myelination via G-Protein Activation. GPR126 is believed to couple to G(s)-protein, which leads to activation of adenylate cyclase for cAMP production. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
TRVLTFITYIGCGISAIFSAATLLTYIAFEKLRRDYPSKILMNLSTALLFLNLVFLLDGWIASFEIDELC
ITVAVLLHFFLLATFTWMGLEAIHMYIALVKVFNTYIRRYILKFCIIGWGLPALIVSIVLASTNDNYGYG
YYGKDKDGQGGDEFCWIKNPVVFYVTCAAYFGIMFLMNVAMFIVVMVQICGRNGKRSNRTLREEILRNLR
SVVSLTFLLGMTWGFAFFAWGPVNLAFMYLFTIFNSLQGLFIFVFHCALKENVQKQWRRHL
>gnl|CDD|320663 cd15997, 7tmB2_GPR112, Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR112 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR114, and GPR126. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
ERILTLITYLGCGISSIFLGITLVTYLAFEKLRRDYPSKILINLCTALLMLNLVFLLNSWLSSFNNYGLC
ITVAAFLHYFLLASFTWMGLEAVHMYFALVKVFNIYIPNYILKFCIAGWGIPAVVVALVLAINKDFYGNE
LSSDSLHPSTPFCWIQDDVVFYISVVAYFCLIFLCNISMFITVLIQIRSMKAKKPSRNWKQGFLHDLKSV
ASLTFLLGLTWGFAFFAWGPVRIFFLYLFSICNTLQGFFIFVFHCLMKENVRKQWRIHL
>gnl|CDD|320664 cd15998, 7tmB2_GPR124, G protein-coupled receptor 124, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR124 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, which also includes orphan GPR123 and GPR125. GPR124, also known as tumor endothelial marker 5 (TEM5), is highly expressed in tumor vessels and in the vasculature of the developing embryo. GPR124 is essentially required for proper angiogenic sprouting into neural tissue, CNS-specific vascularization, and formation of the blood-brain barrier. GPR124 interacts with the PDZ domain of DLG1 (discs large homolog 1) through its PDZ-binding motif. Recently, studies of double-knockout mice showed that GPR124 functions as a co-activator of Wnt7a/Wnt7b-dependent beta-catenin signaling in brain endothelium. Moreover, WNT7-stimulated beta-catenin signaling is regulated by GPR124's intracellular PDZ binding motif and leucine-rich repeats (LRR) in its N-terminal extracellular domain. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
GAGLHPVVYPCTALLLLCLFSTIITYILNHSSIHVSRKGWHMLLNLCFHIAMTSAVFAGGITLTNYQMVC
QAVGITLHYSSLSTLLWMGVKARVLHKELTWRAPPPQEGDPALPTPRPMLRFYLIAGGIPLIICGITAAV
NIHNYRDHSPYCWLVWRPSLGAFYIPVALILLVTWIYFLCAGLHLRGPSADGDSVYSPGVQLGALVTTHF
LYLAMWACGALAVSQRWLPRVVCSCLYGVAASALGLFVFTHHCARRRDVRASWRACCP
>gnl|CDD|320665 cd15999, 7tmB2_GPR125, G protein-coupled receptor 125, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR125 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, which also includes orphan receptors GPR123 and GPR124. GPR125 directly interacts with dishevelled (Dvl) via its intracellular C-terminus, and together, GPR125 and Dvl recruit a subset of planar cell polarity (PCP) components into membrane subdomains, a prerequisite for activation of Wnt/PCP signaling. Thus, GPR125 influences the noncanonical WNT/PCP pathway, which does not involve beta-catenin, through interacting with and modulating the distribution of Dvl. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
ADLLHPVVYATAVVLLLCLLTIIVSYIYHHSLVRISRKSWHMLVNLCFHIFLTCAVFVGGINQTRNASVC
QAVGIILHYSTLATVLWVGVTARNIYKQVTRKAKRCQDPDEPPPPPRPMLRFYLIGGGIPIIVCGITAAA
NIKNYGSRPNAPYCWMAWEPSLGAFYGPAGFIIFVNCMYFLSIFIQLKRHPERKYELKEPTEEQQRLAAS
EHGELNHQDSGSSSASCSLVSTSALENEHSFQAQLLGASLALFLYVALWIFGALAVSLYYPMDLVFSCLF
GATCLSLGAFLVVHHCVNREDVRRAWIATCCP
>gnl|CDD|320666 cd16000, 7tmB2_GPR123, G protein-coupled receptor 123, member of the class B2 family of seven-transmembrane G protein-coupled receptors. GPR123 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, and also includes orphan receptors GPR124 and GPR125. GPR123 is predominantly expressed in the CNS including thalamus, brain stem and regions containing large pyramidal cells, yet its biological function remains to be determined. Adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
GEFLHPVVYACTAVMLLCLFASIITYIVHHSTIRISRKGWHMLLNFCFHTALTFAVFAGGINRTKYPIIC
QAVGIVLHYSTLSTMLWIGVTARNIYKQVTKKPHLCQDTDQPPYPKQPLLRFYLVSGGVPFIICGITAAT
NINNYGTEDEDTPYCWMAWEPSLGAFYGPVAFIVLVTCIYFLCTYVQLRRHPERKYELKNEHSFKAQLRA
AAFTLFLFTATWAFGALAVSQGHFLDMIFSCLYGAFCVTLGLFILIHHCAKRDDVWHCWWSCCPS
>gnl|CDD|320667 cd16001, 7tmA_P2Y3-like, P2Y purinoceptor 3-like proteins, member of the class A family of seven-transmembrane G protein-coupled receptors. P2Y3-like proteins are an uncharacterized group that belongs to the G(i) class of a family of purinergic G-protein coupled receptors. The P2Y receptor family is composed of eight subtypes, which are activated by naturally occurring extracellular nucleotides such as ATP, ADP, UTP, UDP, and UDP-glucose. These eight receptors are ubiquitous in human tissues and can be further classified into two subfamilies based on sequence homology and second messenger coupling: a subfamily of five P2Y1-like receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11Rs) that are coupled to G(q) protein to activate phospholipase C (PLC) and a second subfamily of three P2Y12-like receptors (P2Y12, P2YR13, and P2Y14Rs) that are coupled to G(i) protein to inhibit adenylate cyclase. Several cloned subtypes, such as P2Y3, P2Y5, and P2Y7-10, are not functional mammalian nucleotide receptors. The native agonists for P2Y receptors are: ATP (P2Y2, P2Y12), ADP (P2Y1, P2Y12, and P2Y13), UTP (P2Y2, P2Y4), UDP (P2Y6, P2Y14), and UDP-glucose (P2Y14)
ILLPVTYSVVFVLGLPLNGTVLWLSWCRTKRWTCSTIYLVNLAVADLLYVCSLPLLIVNYAMRDRWPFGD
FLCKLVRFLFYTNLYGSILFLTCISVHRFLGVCYPIRSLAYRTRRLAVIGSAATWILVVLQLLPTLVYAR
TGSINNRTVCYDLTSPDNFGNYFPYGMVLTVTGFLIPFLIILLCYCLMIKSLIRSEEAAGVGKAARAKSI
RTILLVCGLFALCFVPFHITRTIYLFVRVYLVQDCPLLQFVSLAYKIWRPLVSFNSCINPLLYFLSGDSN
RLRL
>gnl|CDD|320668 cd16002, 7tmA_NK1R, neurokinin 1 receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The neurokinin 1 receptor (NK1R), also known as tachykinin receptor 1 (TACR1) or substance P receptor (SPR), is a G-protein coupled receptor found in the mammalian central nervous and peripheral nervous systems. The tachykinins act as excitatory transmitters on neurons and cells in the gastrointestinal tract. The TKs are characterized by a common five-amino acid C-terminal sequence, Phe-X-Gly-Leu-Met-NH2, where X is a hydrophobic residue. The three major mammalian tachykinins are substance P (SP), neurokinin A (NKA), and neurokinin B (NKB). The physiological actions of tachykinins are mediated through three types of receptors: neurokinin receptor type 1 (NK1R), NK2R, and NK3R. SP is a high-affinity endogenous ligand for NK1R, which interacts with the Gq protein and activates phospholipase C, leading to elevation of intracellular calcium. SP is an extremely potent vasodilator through endothelium dependent mechanism and is released from the autonomic sensory nerves. NK2R is a high-affinity receptor for NKA, the tachykinin neuropeptide substance K. SP and NKA are found in the enteric nervous system and mediate in the regulation of gastrointestinal motility, secretion, vascular permeability, and pain perception
ALWAVAYSVIVVVSVVGNIIVMWIILAHKRMRTVTNYFLVNLAFAEASMSAFNTVINFTYAIHNEWYYGL
EYCKFHNFFPIAAVFASIYSMTAIALDRYMAIIHPLQPRLSATATKVVICVIWVLAFLLAFPQGYYSDTE
EMPGRVVCYVEWPEHEERKYETVYHVCVTVLIYFLPLLVIGCAYTVVGITLWASEIPGDSSDRYHEQVSA
KRKVVKMMIVVVCTFAICWLPYHIYFLLQYFHPELYEQKFIQQVYLAIMWLAMSSTMYNPIIYCCLNDRF
RVGF
>gnl|CDD|320669 cd16003, 7tmA_NKR_NK3R, neuromedin-K receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The neuromedin-K receptor (NKR), also known as tachykinin receptor 3 (TACR3) or neurokinin B receptor or NK3R, is a G-protein coupled receptor that specifically binds to neurokinin B. The tachykinins (TKs) act as excitatory transmitters on neurons and cells in the gastrointestinal tract. The TKs are characterized by a common five-amino acid C-terminal sequence, Phe-X-Gly-Leu-Met-NH2, where X is a hydrophobic residue. The three major mammalian tachykinins are substance P (SP), neurokinin A (NKA), and neurokinin B (NKB). The physiological actions of tachykinins are mediated through three types of receptors: neurokinin receptor type 1 (NK1R), NK2R, and NK3R. NK3R is activated by its high-affinity ligand, NKB, which is primarily involved in the central nervous system and plays a critical role in the regulation of gonadotropin hormone release and the onset of puberty
ALWSLAYGFVVAVAVFGNLIVIWIILAHKRMRTVTNYFLVNLAFSDASMAAFNTLINFIYALHSEWYFGE
AYCRFHNFFPITSVFASIYSMTAIAVDRYMAIIDPLKPRLSATATKVVIGSIWILAFLLAFPQCLYSKTK
VMPGRTLCFVAWPGGPDQHFTYHIIVIVLVYCLPLLVMGITYTIVGITLWGGEIPGDTSDKYHEQLRAKR
KVVKMMIIVVLTFAICWLPYHIYFIVTGLYQQLNRWKYIQQVYLASFWLAMSSTMYNPIIYCCLNKRFRA
GF
>gnl|CDD|320670 cd16004, 7tmA_SKR_NK2R, substance-K receptor, member of the class A family of seven-transmembrane G protein-coupled receptors. The substance-K receptor (SKR), also known as tachykinin receptor 2 (TACR2) or neurokinin A receptor or NK2R, is a G-protein coupled receptor that specifically binds to neurokinin A. The tachykinins are widely distributed throughout the mammalian central and peripheral nervous systems and act as excitatory transmitters on neurons and cells in the gastrointestinal tract. The TKs are characterized by a common five-amino acid C-terminal sequence, Phe-X-Gly-Leu-Met-NH2, where X is a hydrophobic residue. The three major mammalian tachykinins are substance P (SP), neurokinin A (NKA), and neurokinin B (NKB). The physiological actions of tachykinins are mediated through three types of receptors: neurokinin receptor type 1 (NK1R), NK2R, and NK3R. SP is a high-affinity endogenous ligand for NK1R, which interacts with the Gq protein and activates phospholipase C, leading to elevation of intracellular calcium. NK2R is a high-affinity receptor for NKA, the tachykinin neuropeptide substance K. SP and NKA are found in the enteric nervous system and mediate the regulation of gastrointestinal motility, secretion, vascular permeability, and pain perception
ALWAIAYSLIVLVAVTGNATVIWIILAHRRMRTVTNYFIVNLALADLSMAAFNTAFNFVYASHNDWYFGL
EFCRFQNFFPITAMFVSIYSMTAIAADRYMAIIHPFKPRLSAGSTKVVIAGIWLVALALAFPQCFYSTVT
MDQGRTKCIVAWPGDSGGKHQLTYHLAVIVLIYLLPLAVMFVTYSIIGITLWRSAVPGHQAHGAYHRQLQ
AKKKFVKTMVVVVVTFAICWLPYHLYFILGSFNEDIYCQKYIQQVYLAIFWLAMSSTMYNPIIYCCLNQR
FRSGF
>gnl|CDD|320671 cd16005, 7tmB2_Latrophilin-3, Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled receptors. Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
DLLLDVITWVGILLSLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVF
AALLHFFFLAAFTWMFLEGVQLYIMLVEVFESEHSRRKYFYLVGYGMPALIVAVSAAVDYRSYGTDKVCW
LRLDTYFIWSFIGPATLIIMLNVIFLGIALYKMFHHTAILKPESGCLDNIKSWVIGAIALLCLLGLTWAF
GLMYINESTVIMAYLFTIFNSLQGMFIFIFHCVLQKKVRKEYGKCLRT
>gnl|CDD|320672 cd16006, 7tmB2_Latrophilin-2, Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled receptors. Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
ELLLTVITWVGIVISLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTEYKIACPIF
AGLLHFFFLAAFAWMCLEGVQLYLMLVEVFESEYSRKKYYYVAGYLFPATVVGVSAAIDYKSYGTEKACW
LRVDNYFIWSFIGPVTFIILLNLIFLVITLCKMVKHSNTLKPDSSRLENIKSWVLGAFALLCLLGLTWSF
GLLFINEETIVMAYLFTIFNAFQGMFIFIFHCALQKKVRKEYSKCFRH
>gnl|CDD|320673 cd16007, 7tmB2_Latrophilin-1, Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled receptors. Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions
ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLIGIDKTQYQIACPIF
AGLLHFFFLAAFSWLCLEGVQLYLMLVEVFESEYSRKKYYYLCGYCFPALVVGISAAIDYRSYGTEKACW
LRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAITLLFLLGLTWAF
GLLFINKESVVMAYLFTTFNAFQGMFIFIFHCALQKKVHKEYSKCLRH
>gnl|CDD|293733 cd16009, PPM, Bacterial phosphopentomutase. Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate). This reaction bridges glucose metabolism and RNA biosynthesis. PPM is a Mn(2+)-dependent enzyme and protein phosphorylation activates the enzyme
KRVILIVLDSFGIGAMPDAAKFGDEGANTLGHIAEAVPGLNLPNLEKLGLGNIVGIEGGPPKENPIAAYG
KMREASAGKDTTTGHWEIMGLKPKKPFPTFPNGFPKELIDEFEKATGRKGLGNKPASGTEIIKELGEEHL
KTGAPIVYTSADSVFQIAAHEEVIPLEELYRICEIAREILDGEYKVGRVIARPFVGETGVYFKRTSNRHD
YALVPPGKTVLDILKEAGIPVIGIGKIADIFAGRGITESIHTKSNADGMEKTLEALKEDFNGLIFTNLVD
FDMLYGHRRDPEGYAEALEEFDRRLPELLAKLKEDDLLIITADHGNDPTIGGTDHTREYVPLLVYGKGLK
GVNLGTRETFADIGATIADNFGVEPPENGTSF
>gnl|CDD|293734 cd16010, iPGM, 2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM. The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity
KPVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGR
IVYQDLTRINKAIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKK
VYVHAFTDGRDTPPKSALKYLKELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGEKA
ESAEEAIEASYAKGITDEFIPPTVIGDEGGTIKDGDAVIFFNFRADRARQITRAFTDPDFDGFDRKKPKN
LYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKAGLKQLRIAETEKYAHVTYFFNGGREEPFPGEDRIL
IPSPKVATYDLKPEMSAYEVTDKLIEAIKSGKYDFIVVNFANPDMVGHTGNLEAAVKAVEAVDECLGRIV
EAVLENGGTLLITADHGNAEEMIDPETGGPHTAHTTNPVPFIIVDPGLKRKLLKDGGLADVAPTILDLLG
IEKPKEMTGKSLI
>gnl|CDD|293735 cd16011, iPGM_like, uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) and bacterial phosphopentomutases. The proteins in this subfamily of alkaline phosphatase are not characterized. Their sequences show similarity to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) which catalyzes the interconversion of 3-phosphoglycerate to 2-phosphoglycerate, and to bacterial phosphopentomutases (PPMs) which interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate)
MKYVLLILDGLGDRPIPELGGKTPLEAAKTPNLDRLAAEGICGLMDPVPPGIAPGSDTAHLSLLGYDPEE
YYTGRGPLEALGAGIDLKPGDVAFRCNFATVDDEDGIIVDRRAGRISTEEAAELIAILNLEFGGVEVRFK
PGVEHRHVLVLRAELLNEFLEKAYEILKDHPVNKKRRAKGKPPANAILLRGAGKRPALPPFEERYGLKGA
VIAAVDLIKGIGRLAGMDVIEVPGATGYLDTDYEGKAEAALEALKDYDFVFVHVKAPDEAGHDGDPEAKV
KAIERIDKAIVGPLLELLDGEDFVIVVTPDHSTPCSLKTHSGDPVPFLIYGPGVRRDGVTRFDEISAAAG
GLGRIRGHELMPLLLNYA
>gnl|CDD|293736 cd16012, ALP, Alkaline Phosphatase. Alkaline phosphatases are non-specific membrane-bound phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Mammalian alkaline phosphatase is divided into four isozymes depending upon the site of tissue expression. They are Intestinal ALP, Placental ALP, Germ cell ALP and tissue nonspecific alkaline phosphatase or liver/bone/kidney (L/B/K) ALP
KNVILFIGDGMGLAQVTAARIYKGGKLGGKGTLLLMEDFPVVGLVKTYSADSLVTDSAAAATALATGVKT
NNGAIGVDPDGGKPLETILEAAKEAGKATGIVTTTRITHATPAAFYAHVPSRDWEDDIAEQLLESGIDVI
LGGGRKYFKLLGLFADSHLPYEIDRDETDEPSLAEMTEKAIEVLSKNPKGFFLMVEGGRIDWAGHANDAA
RAIEETLAFDKAVKVALDFAKKDGDTLVIVTADHETGHTGEDVPVFAYGPGAELFGGVYDNTDIFHKIAE
ALG
>gnl|CDD|293737 cd16013, AcpA, acid phosphatase A. Acid phosphatase A catalyzes the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at low pH. AcpA hydrolyzes a variety of substrates, including p-nitrophenylphosphate (pNPP), p-nitrophenylphosphorylcholine (pNPPC), peptides containing phosphotyrosine, inositol phosphates, AMP, ATP, fructose 1,6-bisphosphate, glucose and fructose 6-phosphates, NADP, and ribose 5-phosphate. AcpA is distinct from histidine ACPs and purple ACPs, as well as class A, B, and C bacterial nonspecific ACPs
TPIKHVVVIMQENRSFDNYFGTYPGANGPPGANLFSAGPGTNLGIPPGPDSDPLTGLPNNPFRLDRTVGL
GAVTPDPVHRFYQEQQQINGGKMDGFVAGSGGTTGDGGQVMGYYDGNDLPFLWDLAQEYTLADNFFASVF
GGTFPNRLYLIAAQSPGFTNAGPSSAAPLDPLDDTASTPPLPPQTQPTIGDRLSAAGVSWGWYSGGWNPA
LAGAPKSTFPFPYFFFTFIGTTAGANHLKDLTDFYADAKAGTLPAVSFVKPSGLNDGHPGYSDVLAGQAF
LADVINALQKSPQWNSTAIIITYDEHGGFYDHVPPPKADAPDPGRWGPGFRVPAIVISPYAKRGYVDHTV
YDHTSILKFIEDRWGLPPLT
>gnl|CDD|293738 cd16014, PLC, non-hemolytic phospholipase C. Nonhemolytic Phospholipases C is produced by pathogenic bacterial. The toxic phospholipases C can interact with eukaryotic cell membranes and hydrolyze phosphatidylcholine and sphingomyelin, leading to cell lysis
IEHVVIFMQENRSFDHYFGTLAGVRGFNDSNSWNNNHAAWNGGLNDNWILAKTPYSMGYFTREDIPFHYA
LADAFTICDMYHCSVLGSTDPNRLYLWSGTIDPPGGNGGPQATPGPATNNLDCFPLTWTTYPEYLEDAGV
SWRVYQDLDAFKADAANGTLPQVSWIVAPQELSEHPPNTPADGAWLVKQVLDALASSPDVWNKTVFIINY
DENGGFFDHVTPPVPPPGTAGEWLTPPYETGGGTPIGLGFRVPMLVISPWSRGGNVFSEVFDHTSVIRFL
EEWAGVR
>gnl|CDD|293739 cd16015, LTA_synthase, Lipoteichoic acid synthase like. Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain
PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGEFEVLTGLPPLPLGSG
SYTLYKLNPLPSLPSILKEQGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEKETNGWGVSDE
SLFDQALEELEELKKKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTELENYLNAIHYTDKALGEFIE
KLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLYRTPLLIYSPGLKKPKKIDRVGSQIDIAPTLLD
LLG
>gnl|CDD|293740 cd16016, AP-SPAP, SPAP is a subclass of alkaline phosphatase (AP). Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP
RPKLVVGIVVDQMRADYLYRYRDRFGEGGFKRLLNEGFVFENAHYNYAPTDTAPGHATIYTGTTPAIHGI
IGNDWYDRETGREVYCVEDSTVTTVGGNSTAGKMSPRNLLVTTIGDELKLATNGRSKVIGVALKDRAAIL
PAGHAADAAYWFDDETGKFITSTYYMKELPAWVEKFNAKKLPFGNTLTLDFAKAALENEKLGKDDVTDLL
AVSFSATDYIGHAFGPNSVEMEDTYLRLDRDLARLLDALDKKVGKGNYLVFLTADHGAADNPEFLKDHKI
PAGRFDPKRLKALLNAYLMAKYGLGKWVLGYSNGQVYLNHKLIEEKGLDLAEVQAAAAEFLLQMPGVAAA
YTADELLAGPEPTGIRERLRNGYNPKRSGDLIVVLKPGWIEGDGSGKGTTHGSPYDYDTHVPLLFYGWGI
KPGEIPRPVEITDIAPTLAALLGIQPPNGCIGKPLLE
>gnl|CDD|293741 cd16017, LptA, Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase. Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane
KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLKKNLIVFDNVISCGTSTAVSLPCMLSFANRENYDRA
YYQENLIDLAKKAGYKTYWISNQGGCGGYDTRISAIAKIETVFTNKGSCNSSNCYDEALLPLLDEALADS
SKKKLIVLHLMGSHGPYYDRYPEEFAKFTPDCDNELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKD
KDAALIYFSDHGESLGENGLYLHGAPYAPKEQYHVPFIIWSSDSYKQRYPVERLRANKDRPFSHDNLFHT
LLGLLGIK
>gnl|CDD|293742 cd16018, Enpp, Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin. Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles
PPLIVISIDGFRWDYLDRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFY
DPKTNEEFSDSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPIPLGGYWQPYNDSFP
FEERVDTILEWLDLERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNI
IVVSDHGMTDVGTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG
>gnl|CDD|293743 cd16019, GPI_EPT, GPI ethanolamine phosphate transferase. Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation
PTKYDKVVLIVIDGLRYDLAVNVNKQSSFFSFLQKLNEQPNNSFLALSFADPPTVTGPRLKALTTGNPPT
FLDLISNFASSEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDPIFYNHI
NDNLDENIYYDNWDFIILHFLGLDHLGHKHNTTSSPELEKKLDQMDNLIRDIYDRMDNDTLLVVVSDHGM
NNDGNHGGSSTEETSSFFFFISKKGFFKKRPIDQIEKIKQNNEQQKIDPSEYIRIIYQIDILPTICYLLG
IPIPFNNIGIII
>gnl|CDD|293744 cd16020, GPI_EPT_1, GPI ethanolamine phosphate transferase 1; PIG-N. Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation
PPPAKRLVVFVADGLRADTFFENNCSRAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYEDPSAV
TKGWKENPVEFDSVFNRSRRSWAWGSPDILPMFPKGATGGKVLTYIYPEEDFDSTDASELDEWVFDKVEE
FLANASSNKTELLNQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAY
IFTSDHGMTDWGSHGDGSPDETETPFIAWGAGIKHPTPGRGPSFSANWGGLRLPRHDLDQADLAPLMSAL
LGLPPPVNSVGILP
>gnl|CDD|293745 cd16021, ALP_like, uncharacterized Alkaline phosphatase subfamily. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity
PNVLILGIDSVSRLNFKRSLPKTLKFLKSELGAVEFKGYNKVGDNTFPNLLPLLTGKSEEELPEARRKES
CKGYLDNCPFIWKDFKKAGYVTAFAEDWPKIGTFNYRKKGFKKPPTDHYLRPFWLAAEKTTSYSTKSYCT
GCRPSHKALLDYLEDFIEAYKDRPKFSFFWLSELTHDYLNGLSLADEDLLEFLKRLKENGLLDNTFVIFM
SDHGLRFGKIRETLQGKLEERLPFLSISLPKWFREKYPEAVANLKKNSNRLTTPFDLHATLLDILNLQ
>gnl|CDD|293746 cd16022, sulfatase_like, sulfatase. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN
VGNGGGLPPDEPTLAELLKEAGYRTALIGKWHDEAIDFIERRDKDKPFFLYVSFNAPHPPFAYYAMVSAI
DDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDAL
VSLLDLLPTLLDLAGIEPPEGLDGRS
>gnl|CDD|293747 cd16023, GPI_EPT_3, GPI ethanolamine phosphate transferase 3, PIG-O. Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation
PPRFDKVVLLLIDALRYDFVLPDDENPPSENSLYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRL
KGLTTGSLPTFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLD
TVDNGVLKHLFPELQSEDDWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLV
FGDHGMTETGDHGGDSDEEVDAALFAYSKRPFNNSDEPIESNGPGDPSKVRSVPQIDLVPTLSLLLGLPI
PFSNLGTVI
>gnl|CDD|293748 cd16024, GPI_EPT_2, GPI ethanolamine phosphate transferase 2; PIG-G. Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation
KPAFDKLVFMVIDALRADFVFGPDSNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDV
VLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSEL
SRDDWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQSSNNPTLLVVCGDHGMTDAG
NHGGSSPGETSVPLLFISPKFSSKPSNADGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI
>gnl|CDD|293749 cd16025, PAS_like, Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
GRPNILLILADDLGFSDLGCFGGEIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTM
AELATGKPGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPDDYYSTDDLTDKAIEYIDEQKAPDKPFF
LYLAFGAPHAPLQAPKEWIDKYKGKYDAGWDALREERLERQKELGLIPADTKLTPRPPGVPAWDSLSPEE
KKLEARRMEVYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEPGWANASNTPFRLYKQASH
EGGIRTPLIVSWPKGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNGVPQLPLDGVSLLPTLDGAAA
PSRRRTQYFELFGNRAIRKGGWKAVALHPPPGWGDQWELYDLAKDPSETHDL
>gnl|CDD|293750 cd16026, GALNS_like, galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS). Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A
KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPG
VVGPPGSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRN
DPPGPLPPLMENEEVIEQPADQSSLTQRYTDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGA
GLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHGGSAGPLRGGKGTTWEGGVRVPF
IAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDL
QAVRSGRWKLHLPTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGETYNVA
>gnl|CDD|293751 cd16027, SGSH, N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase). N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities
PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR
SRGFPLPDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRAKK
GQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPYLPDTPEVREDLADYYDEIERLDQQVGEILDELE
EDGLLDNTIVIFTSDHGMPFPRAKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIE
PPEYLQGRSFLPLLKGEKDPGRDYVFAERDRHDETYDPIRSVRTGRYKYIRNYMPEELYDLKNDPDELNN
LADDPEYAEVLEELRAALDAWMK
>gnl|CDD|293752 cd16028, PMH, Phosphonate monoester hydrolase/phosphodiesterase. Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile
RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN
GTPLDARHLTLALELRKAGYDPALFGYTDTSPDPRGLAPLDPRLLSYELAMPGFDPVDRLDEYPAEDSDT
AFLTDRAIEYLDERQDEPWFLHLSYIRPHPPFVAPAPYHALYDPADVPPPIRAESLAAEAAQHPLLAAFL
ERIESLSFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLG
DHWLWGKDGFFDQAYRVPLIVRDPRREADATRGQVVDAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLL
AGAQPSDWRDAVHYEYDFRDVSTRRPQEALGLSPDECSLAVIRDERWKYVHFAALPPLLFDLKNDPGELR
DLAADPAYAAVVLRYAQKLLSWRMRHADR
>gnl|CDD|293753 cd16029, 4-S, N-acetylgalactosamine 4-sulfatase, also called arylsulftase B. Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme
PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHGV
ILAGEPYGLPLNETLLPQYLKELGYATHLVGKWHLGFYTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGGA
NDYGNDDLRDNEEPAWDYNGTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPYEDK
FAHIKDEDRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGGSNYPLRGGKNTLW
EGGVRVPAFVWSPLLPPKRGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEI
LLNIDDITRTTGGAAIRVGDWKLIVGKPLFNIENDPCERNDLA
>gnl|CDD|293754 cd16030, iduronate-2-sulfatase, iduronate-2-sulfatase. Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome
KKPNVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYD
NNSYFRKVAPDAVTLPQYFKENGYTTAGVGKIFHPGIPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKG
GKGGGGGPAWEAADVPDEAYPDGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLES
IPLPNPFDPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDA
LEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLA
ELAGLPAPPCLEGKSLVPLLKNPSAKWKDAAFSQYPRPSIMGYSIRTERYRYTEWVDFDKVGAEELYDHK
NDPNEWKNLANDPEY
>gnl|CDD|293755 cd16031, G6S_like, unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS). N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease
KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVT
DNNGPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENGKRVGQ
KGYVTDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPETFDDDDYAGRPEW
AREQRNRIRGVLDGRFDTPEKYQRYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGE
HGLFDKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEGEK
PVDWRKEFYYEYYEEPNFHNVPTHEGVRTERYKYIYYYGVWDEEELYDLKKDPLELNNLANDPEYAEVLK
ELRKRLEEL
>gnl|CDD|293756 cd16032, choline-sulfatase, choline-sulfatase. Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon
PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDN
AAEFPADIPTFAHYLRAAGYRTALSGKMHFVGPDQLHGFDYDEEVAFKAVQKLYDLARGEDGRPFFLTVS
FTHPHDPYVIPQEYWDLYVRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGL
WYKMSFFEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPPLDGRSLLPLLEGGDS
GGEDEVISEYLAEGAVAPCVMIRRGRWKFIYCPGDPDQLFDLEADPL
>gnl|CDD|293757 cd16033, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNN
VENAGAYSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEETPLDYGFDEYLPVETTIEYFLADRAIEML
EELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYRRERKRWGVDTEDEE
DWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKGPFMYEETYRIPLI
IKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPEDWRDEVVTEYNGHEFYL
PQRMVRTDRYKYVFNGFDIDELYDLESDPYELNNLIDDPEYEEILREMRTRLYEWMEETGD
>gnl|CDD|293758 cd16034, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFG
NDVPLPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYTPPPERRHGFDYWKGYECNHDHNNPH
YYDDDGKRIYIKGYSPDAETDLAIEYLENQADKDKPFALVLSWNPPHDPYTTAPEEYLDMYDPKKLLLRP
NVPEDKKEEAGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLMNKQVPY
EESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKDDEPDSVLLQ
CFVPFGGGSARDGGEWRGVRTDRYTYVRDKNGPWLLFDNEKDPYQLNNL
>gnl|CDD|293759 cd16035, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDT
LGSPMQPLLSPDVPTLGHMLRAAGYYTAYKGKWHLSGAAGGGYKRDPGIAAQAVEWLRERGAKNADGKPW
FLVVSLVNPHDIMFPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGA
HGLRGKGFNAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATEAPPLPGRDLS
PLLTDADADAVRDGILFTYDRYKFARYFDPP
>gnl|CDD|293760 cd16037, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDN
ADPYDGDVPSWGHALRAAGYETVLIGKLHFRGEDQRHGFRYDRDVTEAAVDWLREEAADDKPWFLFVGFV
APHFPLIAPQEFYDLYVRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWG
KSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEGPDDPDRVV
FSEYHAHGSPSGAFMLRKGRWKYIYYVGYPPQLFDLENDPE
>gnl|CDD|277186 cd16039, PHD_SPP1, PHD finger found in Set1 complex component SPP1. Set1C component SPP1, also called COMPASS component Spp1, or Complex proteins associated with set1 protein Spp1, or Suppressor of PRP protein 1, is a component of the COMPASS complex that links histone methylation to initiation of meiotic recombination. It induces double-strand break (DSB) formation by tethering to recombinationally cold regions. SPP1 interacts with H3K4me3 and Mer2, a protein required for DSB formation, to promote recruitment of potential meiotic DSB sites to the chromosomal axis. SPP1 contains a PHD finger, a zinc binding motif
YCICQKPDDGRWMIACDGCDEWYHFTCVNIPEADVELVDSFFCPPC
>gnl|CDD|294002 cd16040, SPRY_PRY_SNTX, Stonustoxin subunit alpha or SNTX subunit alpha. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of Stonustoxin alpha proteins. Stonustoxin (SNTX) is a multifunctional lethal protein isolated from venom elaborated by the stonefish. It comprises two subunits, termed alpha and beta. SNTX elicits an array of biological responses, particularly a potent hypotension and respiratory difficulties
REEFLKYACQLTLDPNTAHRNLSLSEGNRKVTRVKEEQPYPDHPERFDYWPQVLCREGLSGRCYWEVEWS
GGGVDIAVAYKGISRKGDGDDSRFGYNDKSWSLECSPSGYSFWHNNKKTEISVPSSSSSRVGVYLDHSAG
TLSFYSVSDTMTLLHTVQTTFTEPLYPGFGVGYGSSVKLC
>gnl|CDD|293880 cd16074, OCRE, OCRE domain. The OCRE (OCtamer REpeat) domain contains 5 repeats of an 8-residue motif, which were shown to form beta-strands. Based on the architectures of proteins containing OCRE domains, a role in RNA metabolism and/or signalling has been proposed
GSPDPSGFVFDPNSGYYYDPSTGLYYDPNTGYYYDPTSGTYYIWDDELGAYVPV
>gnl|CDD|293922 cd16075, ORC6_CTD, C-terminal domain of the eukaryotic origin recognition complex subunit ORC6. In eukaryotes, a complex consisting of six subunits promotes the onset of DNA replication. The 6th subunit, ORC6, does not belong to the wider AAA+ family of nucleotide hydrolases, but contains a tandemly repeated domain resembling the transcription factor TFIIB, as well as this C-terminal domain which harbors a helical segment that is responsible for interactions with the complex by binding to ORC3. Mutations in this C-terminal helix interfere with the formation of the ORC and have been linked to Meier-Gorlin syndrome, a dwarfism disorder
KRQKTLKERYFEEKEKEEEVERSKQQKSEKETIEDYEEWKRRILENAAKALKE
>gnl|CDD|293923 cd16076, TSPcc, Coiled coil region of thrombospondin. This domain family contains coiled coil region of subgroup B of thrombospondins, comprising TSP-3, TSP-4, and TSP-5, that assemble as pentamers. This region is located adjacent to the N-terminal domain (NTD) of thrombospondin (TSP), that mediates co-translational oligomerization via formation of a left-handed super-helix which binds hydrophilic signaling molecules such as vitamin D3 and vitamin A. Pentameric TSPs are stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end. TSP-5 is also known as cartilage oligomeric matrix protein (COMP). TSPs comprise a conserved family of extracellular, oligomeric, multidomain, calcium-binding glycoproteins. In mammals, they have several complex tissue-specific roles, including activities in wound healing and angiogenesis, connective tissue organization, vessel wall biology, and synaptogenesis, all mechanistically derived from interactions with cell surfaces, cytokines, growth factors, or components of the extracellular matrix (ECM) that together regulate many aspects of cell phenotype. In invertebrates, TSPs may have ancient functions such as bridging activities in cell-cell and cell-ECM interactions. Most protostomes and inferred basal metazoa encode a single TSP with the general domain organization of subgroup B TSPs and with a pentamerizing coiled coil
QLARQLTELNQMLQELREEMRQQVKETAFLRNTIMECQAC
>gnl|CDD|293924 cd16077, TSP-5cc, Coiled coil region of thrombospondin-5 (TSP-5). This family contains the N-terminal coiled coil region of TSP-5, also known as cartilage oligomeric matrix protein (COMP). It forms a pentameric left-handed coiled coil (COMPcc) with a channel that is a unique carrier for lipophilic compounds. It is known to bind hydrophilic signaling molecules such as vitamin D3 and vitamin A, making it a possible targeted drug delivery system. TSP-5/COMP is expressed in all types of cartilage as well as in the vitreous of the eye, tendons, vascular smooth muscle cells, and heart. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-5 is essential for modulating the phenotypic transition of vascular smooth muscle cells and vascular remodeling. Mutations in TSP-5 result in two different inherited chondrodysplasias and osteoarthritic phenotypes: pseudoachondroplasia and multiple epithelial dysplasia. Deficiency of TSP-5 causes dilated cardiomyopathy (DCM), a common cause of congestive heart failure. Early increase in serum TSP-5 is associated with joint damage progression in patients with rheumatoid arthritis, thus representing a novel indicator of an activated destructive process in the joint
LAPQMLSEMQETNQALAEVKELLKQQVKEITFLKNTVMECDAC
>gnl|CDD|293925 cd16079, TSP-3cc, Coiled coil region of thrombospondin-3 (TSP-3). This family contains the N-terminal coiled coil region of TSP-3, which is highly expressed in osteosarcomas and associated with metastasis. TSP-3, along with TSP-5 and type IX collagen, is also expressed in the growth plate and all operate in concert and participate in growth plate organization that directly modulates linear growth. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-3 knockout mice have been shown to display accelerated endochondral ossification and increased trabecular bone in the femoral head
HTKALITQLTLFNQILGELREDIRDQVKEMSLIRNTIMECQVC
>gnl|CDD|293926 cd16080, TSP-4cc, Coiled coil region of thrombospondin-4 (TSP-4). This family contains the N-terminal coiled coil region of TSP-4, which is abundantly expressed in tendon and muscle, as well as in neural and osteogenic tissues, and has also been detected in brain capillaries. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-4 regulates the composition of the deposition of extracellular matrix (ECM) in tendon and skeletal muscle. The absence of TSP-4 alters the organization, composition and physiological functions of these tissues. TSP-4 deficiency causes incorrect modification of heparan-sulfate (HS), resulting in decreased activity of lipoprotein lipase (LpL) and loss of beta-glycan; HS is involved in a wide variety of cellular functions, LpL is an endothelial enzyme responsible for the uptake and hydrolysis of lipoproteins, and beta-glycan has inhibiting effect on TGF-beta signaling in skeletal muscle. The human gene THBS4 that encodes for TSP-4 contains a single nucleotide polymorphism (SNP), which is expressed at high frequency in Caucasians and associated with a significantly increased risk of premature myocardial infarction. TSP-4 also binds stromal interaction molecule 1 (STIM1), a transmembrane protein that functions in the endoplasmic reticulum (ER), and regulates calcium channel activity. Studies show that TSP-4 may act as an organizer of adhesive and axon outgrowth-promoting molecules in the ECM to optimize retinal ganglion cell responses. TSP-4 is also involved in the post-translational modification of collagen and may assist in collagen fibril assembly
VGRQLLGQMTQLNQVLGEVKDLLRQQVKETSFLRNTIAECQACG
>gnl|CDD|293927 cd16081, TSPcc_insect, Coiled coil region of thrombospondin in protostomes. This family contains the N-terminal coiled coil region of thrombospondin (TSP) in some protostomes, which suggest ancient functions that include bridging activities in cell-cell and cell-ECM interactions. It appears that most protostomes and inferred basal metazoa encode a single TSP with the general domain organization of subgroup B TSPs and with a pentamerizing coiled coil. This region has heparin-binding activity and is a component of extracellular matrix (ECM), showing that the pentameric TSPs are of earlier origin and that the trimeric TSP subfamily A form is associated with higher chordates. The left-handed coiled coil pentamer forms a channel that is a unique carrier for lipophilic compounds, and is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. Several heparan sulphate (HS) proteoglycans are known in D. melanogaster, including both transmembrane and matrix forms, which could contribute to its retention in pericellular matrix
DELLAKTLNELIEAIKKLREEVERNRQETRYLRELIENCAAC
>gnl|CDD|409504 cd16082, IgC_CRIg, Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg). The members here are composed of the Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also referred to as Z39Ig and V-set and Ig domain-containing 4 (VSIG4)) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. CRIg plays a role in the complement system, an inhibitor of the alternative pathway convertases, and a negative regulator of T cell activation. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond
TTGSGYGFTVPQGMRISLQCQAWGSPPISYVWYKEQTNNQEPIKVAALSTLLFKPAVVADSGSYFCTAKG
RVGSEQRSDIVKFVVK
>gnl|CDD|409505 cd16083, IgC1_CD80, Immunoglobulin constant (IgC)-like domain of antigen receptor Cluster of Differentiation (CD) 80; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin constant (IgC)-like domain of the antigen receptor Cluster of Differentiation (CD) 80. CD80 (also known as glycoprotein B7-1) and CD86 (also known as glycoprotein B7-2) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. CD80 contains two Ig-like domains, an amino-terminal immunoglobulin variable (IgV)-like domain characteristic of adhesion molecules, and a membrane proximal immunoglobulin constant (IgC)-like domain similar to the constant domains of antigen receptors. Members of the Ig family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and major histocompatibility complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, and the IgC domain is involved in oligomerization and molecular interactions
FPVPSITEFGNPSPNIKRIICSTSGGFPEPRLSWLENGEELNAINTTVSQDPETELYTVSSELDFNVTYN
HSIVCLIKYGDSRVSKNFTWE
>gnl|CDD|409506 cd16084, IgC1_CH2_IgD, CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin delta chain; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin constant domain (IgC) in delta heavy chains. The IgC family includes immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and major histocompatibility complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, and the IgC domain is involved in oligomerization and molecular interactions
GVYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPR
SLWNAGTSVTCTLNHPSLPPQRLMALR
>gnl|CDD|409507 cd16085, IgC1_SIRP_domain_3, Signal-regulatory protein (SIRP) immunoglobulin-like domain 3; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the immunoglobulin (Ig)-like domain in Signal-Regulatory Protein (SIRP), domain 3 (C1 repeat 2). The SIRPs belong to the "paired receptors" class of membrane proteins that comprise several genes coding for proteins with similar extracellular regions but very different transmembrane/cytoplasmic regions with different (activating or inhibitory) signaling potentials. They are commonly on NK cells, but are also on many myeloid cells. Their extracellular region contains three Immunoglobulin superfamily domains a single V-set and two C1-set IgSF domains. Their cytoplasmic tails that contain either ITIMs or transmembrane regions that have positively charged residues that allow an association with adaptor proteins, such as DAP12/KARAP, containing ITAMs. There are 3 distinct SIRP members: alpha, beta, and gamma. SIRP alpha (also known as CD172a or SRC homology 2 domain-containing protein tyrosine phosphatase substrate 1/Shps-1) is a membrane receptor that interacts with a ligand CD47 expressed on many cells and gives an inhibitory signal through immunoreceptor tyrosine-based inhibition motifs in the cytoplasmic region that interact with phosphatases SHP-1 and SHP-2. SIRP beta has a short cytoplasmic region and associates with a transmembrane adapter protein DAP12 containing immunoreceptor tyrosine-based activation motifs to give an activating signal. SIRP gamma contains a very short cytoplasmic region lacking obvious signaling motifs but also binds CD47, but with much less affinity
VPPTLEVTQQPTMVWNQVNVTCQVEKFYPQRLQLTWLENGNVSRTETPSTLTVNKDGTYNWTSWLLVNVS
AHREDVVLTCQVEHDGQPAVTKNHTL
>gnl|CDD|319335 cd16086, IgV_CD80, Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80. The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 80). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as cluster of differentiation 152/CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. CD80 contains two Ig-like domains, an amino-terminal immunoglobulin variable (IgV)-like domain characteristic of adhesion molecules and a membrane proximal immunoglobulin constant (IgC)-like domain similar to the constant domains of antigen receptors. Members of the Ig family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and Major Histocompatibility Complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, and the IgC domain is involved in oligomerization and molecular interactions
IIQVTKSVKEKALLSCDYNVSVDELAQVRIYWQKDDKMVLTIISGDVKVWPEYKNRTLFDITNNLSIVIL
ALRLSDRGTYTCVVQKKERGAYKREHLASVTLSVR
>gnl|CDD|409508 cd16087, IgV_CD86, Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86. The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 86). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. The CTLA-4 and B7-2 monomers are both two-layer beta-sandwiches that display the chain topology characteristic of the immunoglobulin variable (V-type) domains present in antigen receptors. The front and back sheets of B7-2 are composed of AGFCC'C" and BED strands, respectively. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond
LKIQAYFNETAYLPCQFKNPQNISLSELVVFWQDQKKLVLYELYLGKEKLDNVNSKYIGRTSFDQENWTL
QLHNVQIKDQGTYQCFIHHKSPKGLVLIHQMSSELSVI
>gnl|CDD|409509 cd16088, IgV_PD1, Immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1). The members here are composed of the immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1; also known as CD279/cluster of differentiation 279). PD1 is a cell surface receptor that is expressed on T cells and pro-B cells. The protein's structure includes an extracellular IgV domain followed by a transmembrane region and an intracellular tail. Activation of CD4+ T cells, CD8+ T cells, NKT cells, B cells, and monocytes induces PD-1 expression, immediately after which it binds two distinct ligands, PD-L1 (also known as B7-H1 or CD274/cluster of differentiation 274) and PD-L2, also known as B7-DC. PD-1 plays an important role in down regulating the immune system by preventing the activation of T-cells, reducing autoimmunity and promoting self-tolerance. The inhibitory effect of PD-1 is accomplished by promoting apoptosis in antigen specific T-cells in lymph nodes while simultaneously reducing apoptosis in regulatory T cells. A class of drugs that target PD-1, known as the PD-1 inhibitors, activate the immune system to attack tumors and treat cancer. Comparisons between the mouse PD-1 (mPD-1) and human PD-1 (hPD-1) reveals that unlike the mPD-1 which has a conventional IgSF V-set domain, hPD-1 lacks a C" strand, and instead the C' and D strands are connected by a long and flexible loop. In addition, the BC loop is not stabilized by disulfide bonding to the F strand of the ligand binding beta sheet. These differences result in different binding affinities of human and mouse PD-1 for their ligands
PPTFSPALLVVTEGANATFTCSFSNTSESFVLNWYRLSPSNQTDKLAAFPEDRSQPGQDWRFRVTQLPNG
RDFHMSVVRARRNDSGTYLCGAISLAPKAQIKESPRAELRVT
>gnl|CDD|409510 cd16089, IgV_CRIg, Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin superfamily (CRIg). The members here are composed of the immunoglobulin variable (IgV) region of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also known as Z39Ig and V-set and Ig domain-containing 4 (VSIG4) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. Like all members of this family, the CRIg domain contains two beta-sheets: one composed of strands A', G, F, C, C' and C", and the other of strands B, E and D. The complement system is an important part of the innate immune system and is required for removal of pathogens from the bloodstream. After exposure to pathogens, the third component of the complement system, C3, is cleaved to C3b which, after recruitment of factor B, initiates formation of the alternative pathway convertases. CRIg, a complement receptor expressed on macrophages, binds to C3b and iC3b mediating phagocytosis of the particles. It is also a potent inhibitor of the alternative pathway convertases and a negative regulator of T cell activation. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond
PILEGPESITGPWKGSVNLPCTYVPEEGYTQVLVKWLVQRDSDPVTIFLRDSSGDHIQQAKYRGRLEVSK
DTPGDVSLQLDTLEMDDRGHYTCQVTWQTPDGNLIVREKTTELRVQK
>gnl|CDD|409511 cd16090, IgV_CD47, Immunoglobulin variable region (IgV) in Cluster of Differentiation (CD) 47. The members here are composed of immunoglobulin variable (IgV) region in the Cluster of Differentiation (CD) 47 (also known as integrin associated protein/IAP). CD47 partners with membrane integrins and binds thrombospondin-1 (TSP-1) and signal-regulatory protein alpha (SIRP alpha). It is involved in apoptosis, proliferation, adhesion, migration, and immune and angiogenic responses. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond
LLFNKIKSVEITDCNKTVVLPCYVTNLEANNINEMFVKWKFQGKDIFSFDGAENKVTRNPAFSSANILSS
DLLKGNASLTLSKAEAVLGNYTCEVTELNREGETTVELKYRS
>gnl|CDD|409512 cd16091, IgV_HHLA2, Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2). The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells
AVSEVIVVCLLSEDCILPCSFTPGSEVVIHWYKQDSDIKVHSYYYGKDQLESQDQRYRNRTSLFKDQISN
GNASLLLRRVQLQDEGRYKCYTSTIIGNQESFVNLKV
>gnl|CDD|319341 cd16092, IgC1_CH1_IgD, CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin delta chain; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the first immunoglobulin constant-1 set domain of delta chains. It belongs to a family composed of the first immunoglobulin constant-1 set domain of alpha, delta, epsilon, gamma, and mu heavy chains. This domain is found on the Fab antigen-binding fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. This group belongs to the C1-set of IgSF domains, which are classical Ig-like domains resembling the antibody constant domain. C1-set domains are found almost exclusively in molecules involved in the immune system, such as in immunoglobulin light and heavy chains, in the major histocompatibility complex (MHC) class I and II complex molecules, and in various T-cell receptors
APDVFPIISGCRHPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPL
QQWRQGEYKCVVQHTASKSKKEIFRW
>gnl|CDD|409513 cd16093, IgC1_CH2_Mu, CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member of the C1-set of Ig superfamily (IgSF) domains. The members here are composed of the second immunoglobulin constant domain (IgC) of mu heavy chains. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns
PPTVSLHAPSREEFLGNRTATFVCLATGFSPKTISFKWLRNGKEVTSSTGAVVEEPKEDGKTLYSATSFL
TITESEWKSQTEFTCEFKHKGEIVEKNAS
>gnl|CDD|319343 cd16094, IgC1_CH3_IgD, CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin delta chain; member of the C1-set of Ig superfamily domains. The members here are composed of the third immunoglobulin constant domain (IgC) of delta heavy chains. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. C1-set Ig domains have one beta sheet that is formed by strands A, B, E, and D and the other strands by G, F, C, and C'
KLSLNLLASSDPPEAASWLLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQPGSTTFWAWSVLRVP
APPSPQPATYTCVVSHEDSRTLLNASRSLE
>gnl|CDD|409514 cd16095, IgV_H_TCR_mu, T-cell receptor Mu, Heavy chain, variable (V) domain. The members here are composed of the immunoglobulin (Ig) heavy chain (H), variable (V) domain of the T-cell receptor Mu. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which can associate with any of the heavy chains. This family includes alpha, gamma, delta, epsilon, and mu heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology
ETQLEESGGGSHPAGKTLSLKCQTSGFQFNTSQLSWYLWVPGHAPLWLTSLDHISTKVSEDRITSSREDT
NSQIFLQIKGLGLRDSGQYHCARRVGYGDDTDKLIFGPGTDVIVE
>gnl|CDD|409515 cd16096, IgV_CD79b_beta, Immunoglobulin variable domain (IgV) Cluster of Differentiation (CD) 79B. The members here are composed of the immunoglobulin variable domain (IgV) of the Cluster of Differentiation (CD) 79B (also known as CD79b molecule, immunoglobulin-associated beta (Ig-beta), and B29). The B lymphocyte antigen receptor is a multimeric complex that includes the antigen-specific component, surface immunoglobulin (Ig). Surface Ig non-covalently associates with two other proteins, Ig-alpha and Ig-beta, which are necessary for expression and function of the B-cell antigen receptor. This gene encodes the Ig-beta protein of the B-cell antigen component. Alternatively spliced transcript variants encoding different isoforms have been described. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology
IWQHPRFAAKKRSSMVKFHCYTNYSGVMTWFRKKGNQRPQELFPEDGRISQTQNGSVYTLTIQNIQYEDN
GIYFCQQKCNSTEPDVTDGCGTELLV
>gnl|CDD|409516 cd16097, IgV_SIRP, Immunoglobulin (Ig)-like variable (V) domain of the Signal-Regulatory Protein (SIRP). The members here are composed of the immunoglobulin (Ig)-like domain of the Signal-Regulatory Protein (SIRP). The SIRPs belong to the "paired receptors" class of membrane proteins that comprise several genes coding for proteins with similar extracellular regions, but very different transmembrane/cytoplasmic regions with different (activating or inhibitory) signaling potentials. They are commonly on NK cells, but are also on many myeloid cells. Their extracellular region contains three immunoglobulin superfamily domains, a single V-set, and two C1-set IgSF domains. Their cytoplasmic tails that contain either ITIMs or transmembrane regions have positively charged residues that allow an association with adaptor proteins, such as DAP12/KARAP, containing ITAMs. There are 3 distinct SIRP members: alpha, beta, and gamma. SIRP alpha (also known as CD172a or SRC homology 2 domain-containing protein tyrosine phosphatase substrate 1/Shps-1) is a membrane receptor that interacts with a ligand CD47 expressed on many cells and gives an inhibitory signal through immunoreceptor tyrosine-based inhibition motifs in the cytoplasmic region that interact with phosphatases SHP-1 and SHP-2. SIRP beta has a short cytoplasmic region and associates with a transmembrane adapter protein DAP12 containing immunoreceptor tyrosine-based activation motifs to give an activating signal. SIRP gamma contains a very short cytoplasmic region lacking obvious signaling motifs, but also binds CD47 with much less affinity. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology
QVIQPEKSVSVAAGESATLHCTVTSLIPVGPIQWFRGAGPGRELIYNQKEGHFPRVTTVSDLTKRNNMDF
SIRISNITPADAGTYYCVKFRKGSPDDVEFKSGAGTELSVR
>gnl|CDD|294015 cd16098, FliS, flagellar export chaperone FliS. This family contains flagellar export chaperone FliS, a protein critical for flagellar assembly and bacterial colonization. FliS prevents premature polymerization of flagellins, the major protein of the filament, by regulating interactions between structural components of the bacterial flagellum in the cytosol. It binds specifically to FliC (flagellin) which is sequentially secreted in large numbers through the central channel of the flagellum and polymerized to form the tail filament. FliS protects FliC from degradation and aggregation by binding to the FliC C-terminal helical domain, which contributes to stabilization of flagellin subunit interactions during polymerization. FliS has been shown to interact specifically with FlgM, whose role is to inhibit FliA, a flagellum-specific RNA polymerase responsible for flagellin transcription; FliA competes with FliS for FlgM binding
PHQLVVMLYDGAIRFLKRAKEAIEEGDIEEKGEALSKAQDIIGELLSSLDFEKGGEIAKNLDALYDYMLR
RLLEANLKNDAEKLDEVIELLTELREAWKEAA
>gnl|CDD|381691 cd16099, TenA_PqqC-like, TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone (PQQ) synthesis protein C. TenA proteins participate in thiamin metabolism and can be classified into two classes: TenA_C which has an active site Cys, and TenA_E which does not; TenA_E proteins often have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product amino-HMP (4-amino-5-amino-methyl-2-methylpyrimidine) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Arabidopsis thaliana TenA_E hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP, but does not hydrolyze thiamin. Bacillus subtilis TenA_C can hydrolyze amino-HMP to AMP and can catalyze the hydrolysis of thiamin. Saccharomyces cerevisiae THI20 includes a C-terminal tetrameric TenA-like domain fused to an N-terminal ThiD domain, and participates in thiamin biosynthesis, degradation and salvage; the TenA-like domain catalyzes the production of HMP from thiamin degradation products (salvage). Bacillus halodurans TenA_C participates in a salvage pathway where the thiamine degradation product 2-methyl-4-formylamino-5-aminomethylpyrimidine (formylamino-HMP) is hydrolyzed first to amino-HMP by the YlmB protein, and the amino-HMP is then hydrolyzed by TenA to produce HMP. Helicobacter pylori TenA_C is also thought to catalyze a salvage reaction but the pyrimidine substrate has not yet been identified. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect; Pyrococcus furiosus TenA_E lacks appropriate surface charges for DNA interactions. This family also includes bacterial coenzyme pyrroloquinoline quinone (PQQ) synthesis protein C (PQQC), an oxidase involved in the final step of PQQ biosynthesis, and CADD, a Chlamydia protein that interacts with death receptors
IWDAILNHPFVQELAAGTLPREKFRYYLAQDYYYLKDFARALALAAAKAPDLELRTFLAELINVLDDELE
LHEKLLAELGISEEDLSEAEPNPATLAYTNHLLRVAARGTPAEGLAALLPCYWSYGEIGRRLAASLPEHP
PYRFWIDFYASDEYQELVEELLQLLDQLAAAGEEEKEELKEIFLTSLRYELMFWDA
>gnl|CDD|350627 cd16100, ARID, ARID/BRIGHT DNA binding domain family. The AT-rich interaction domain (ARID) family of transcription factors, found in a broad array of organisms from fungi to mammals, is characterized by a highly conserved, helix-turn-helix DNA binding domain that binds to the major groove of DNA. The ARID domain, also called BRIGHT, was first identified in the mouse B-cell-specific transcription factor Bright and in the product of the dead ringer (dri) gene of Drosophila melanogaster. ARID family members are implicated in normal development, differentiation, cell cycle regulation, transcriptional activation and chromatin remodeling. Different family members exhibit different DNA-binding properties. Drosophila Dri, mammalian ARID3A/3B/3C and ARID5A/5B, selectively bind AT-rich sites. However, ARID1A/1B, Drosophila Osa, yeast SWI1, ARID2, ARID4A/4B, JARID1A/1B/1C/1D, and JARID2, bind DNA without sequence specificity
EREEFLEQLRAFLESRGTPLLKPPTIGGKPLDLYKLYRAVVSRGGYEKVTEKKLWKEVARKLGLPTSSTS
AAQALKRIYEKYLLPFE
>gnl|CDD|341089 cd16101, ING, Inhibitor of growth (ING) domain family. The Inhibitor of growth (ING) family includes a group of tumor suppressors, ING1-5, which act as readers and writers of the histone epigenetic code, affecting DNA damage response, chromatin remodeling, cellular senescence, differentiation, cell cycle regulation, and apoptosis. They may have a general role in mediating the cellular response to genotoxic stress through binding to and regulating the activities of histone acetyltransferase (HAT) and histone deacetylase (HDAC) chromatin remodeling complexes. All ING proteins contain an N-terminal leucine zipper-like (LZL) motif-containing ING domain that binds unmodified H3 tails, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain, which binds lysine 4-tri-methylated histone H3 (H3K4me3). Although these two regions can bind histones independently, together they increase the apparent association of the ING domain for the H3 tail. The ING family also includes three yeast orthologs, chromatin modification-related protein YNG1 (Yng1p), YNG2 (Yng2p), and transcriptional regulatory protein PHO23 (Pho23p). Yng1p, also termed ING1 homolog 1, is one of the components of the NuA3 histone acetyltransferase (HAT) complex. Yng2p, also termed ESA1-associated factor 4, or ING1 homolog 2, is a subunit of the NuA4 HAT complex. It plays a critical role in intra-S-phase DNA damage response. Pho23p is part of Rpd3/Sin3 histone deacetylase (HDAC) complex. It is required for the normal function of Rpd3 in the silencing of rDNA, telomeric, and mating-type loci. Yng1p and Pho23p inhibit p53-dependent transcription. In contrast, Yng2p has the opposite effect
LSHLPFELRRLLTLIRELDEKKTELQKEIDELAKELLKSARIESHQQKRRLLDEIRQLYEKSIELSDEKV
QLSSQAYELVDNHIRKLD
>gnl|CDD|340519 cd16102, RAWUL_PCGF_like, RRING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in PCGF1-6, RING1 and -2, DRIP and similar proteins; structurally similar to a beta-grasp ubiquitin-like fold. The family includes six Polycomb Group (PcG) RING finger homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) that use epigenetic mechanisms to maintain or repress expression of their target genes. They were first discovered in fruit flies that can remodel chromatin such that epigenetic silencing of genes takes place, and are well known for silencing Hox genes through modulation of chromatin structure during embryonic development in fruit flies. PCGF homologs play important roles in cell proliferation, differentiation, and tumorigenesis. They all have been found to associate with ring finger protein 2 (RNF2). The RNF2-PCGF heterodimer is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF homologs are critical components in the assembly of distinct Polycomb Repression Complex 1 (PRC1) related complexes which are involved in the maintenance of gene repression and target different genes through distinct mechanisms. The Drosophila PRC1 core complex is formed by the Polycomb (Pc), Polyhomeotic (Ph), Posterior sex combs (Psc), and Sex combs extra (Sce, also known as Ring) subunits. In mammals, the composition of PRC1 is much more diverse and varies depending on the cellular context. All PRC1 complexes contain homologs of the Drosophila Ring protein. Ring1A/RNF1 and Ring1B/RNF2 are E3 ubiquitin ligases that mark lysine 119 of histone H2A with a single ubiquitin group (H2AK119ub). Mammalian homologs of the Drosophila Psc protein, such as PCGF2/Mel-18 or PCGF4/BMI1, regulate PRC1 enzymatic activity. PRC1 complexes can be divided into at least two classes according to the presence or absence of CBX proteins, which are homologs of Drosophila Pc. Canonical PRC1 complexes contain CBX proteins that recognize and bind H3K27me3, the mark deposited by PRC2. Therefore, canonical PRC1 complexes and PRC2 can act together to repress gene transcription and maintain this repression through cell division. Non-canonical PRC1 complexes, containing RYBP (together with additional proteins, such as L3mbtl2 or Kdm2b) rather than the CBX proteins, have recently been described in mammals. PCGF homologs contain a C3HC4-type RING-HC finger, and a RAWUL domain that might be responsible for interaction with Cbx members of the Polycomb repression complexes
QVSLSLEPSESNLGGKLPQLEKPYLRCSARATVGHLKKFLRRKLKLDSEQDLDILCRGELLGKEHTLKFI
WRTRWRKQDGPLVLQYR
>gnl|CDD|340520 cd16103, Ubl2_OASL, ubiquitin-like (Ubl) domain 2 found in 2'-5'-oligoadenylate synthase-like protein (OASL) and similar proteins. OASL, also termed 2'-5'-OAS-related protein (2'-5'-OAS-RP), or 59 kDa 2'-5'-oligoadenylate synthase-like protein, or thyroid receptor-interacting protein 14, or TR-interacting protein 14 (TRIP-14), or p59 OASL (p59OASL), is an interferon (IFN)-induced antiviral protein that plays an important role in the IFNs-mediated antiviral signaling pathway. It inhibits respiratory syncytial virus replication and is targeted by the viral nonstructural protein 1 (NS1). It also displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L. Moreover, OASL does not have 2'-5'-OAS activity, but can bind double-stranded RNA (dsRNA) to enhance RIG-I signaling. OASL belongs to the 2'-5' oligoadenylate synthase (OAS) family. While each member of this family has a conserved N-terminal OAS catalytic domain, only OASL has two tandem C-terminal ubiquitin-like (Ubl) repeats, which are required for its antiviral activity. This family corresponds to the second Ubl domain
EIQIFVKFPDGTSKPYAINPEDTILDLKEKIEEQGGPPVEDQILLFQGQELRDKKSLKYYGIKDGDTLQL
SL
>gnl|CDD|340521 cd16104, Ubl_USP14_like, ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and similar proteins. USP14 (EC 3.4.19.12), also termed deubiquitinating enzyme 14, or ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, or ubiquitin carboxyl-terminal hydrolase 14, is a component of proteasome regulatory subunit 19S that regulates deubiquitinated proteins entering inside the proteasome core 20S, which plays an inhibitory role in protein degradation. USP14 is also associated with various signal transduction pathways and tumorigenesis, and thus plays an essential role in the development of various types of cancer. Moreover, USP14 mediates the development of cardiac hypertrophy by promoting GSK-3beta phosphorylation, suggesting a role in cardiac hypertrophy treatment. USP14 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-specific protease (USP) domain
TYKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSKLKLKDGQTLML
MGSAE
>gnl|CDD|340522 cd16105, Ubl_ASPSCR1_like, Ubiquitin-like (Ubl) domain found at the N-terminus of mammalian ASPSCR1 (alveolar soft part sarcoma chromosomal region candidate gene 1 protein), Saccharomyces cerevisie Ubx4p, and similar proteins. ASPSCR1 (alveolar soft part sarcoma chromosomal region candidate gene 1 protein) is also known as alveolar soft part sarcoma locus protein (ASPL), tether containing UBX domain for GLUT4, TUG, UBX domain protein 9, UBXD9, UBXN9 or renal papillary cell carcinoma protein 17 (RCC17). The majority of members of this family contain two beta-grasp ubiquitin-like fold domains: the N-terminal UBL domain (described in this CD), and a C-terminal UBX domain. This UBL domain lacks the characteristic C-terminal double glycine motif. ASPSCR1 functions as a cofactor of the hexameric AAA (ATPase associated with various activities) ATPase complex, known as p97 or VCP in mammals and Cdc48p in yeast. In mammalian cells, ASPSCR1 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4 and assembly of the Golgi apparatus; ASPSCR1 also plays a role in controlling vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. Ubx4p and ASPSCR1 have only partially overlapping functions: both interact with p97/Cdc48p; however, Ubx4p is important for the ERAD (endoplasmic reticulum-associated protein degradation) pathway while ASPSCR1 appears not to be
LTVLYPNGRRQTVKVTPNTPLSQVLEEACKKFGLDPSSEYSLKHNRKPLDLSLPFRLSNLPNNAKLELVK
S
>gnl|CDD|340523 cd16106, Ubl_Dsk2p_like, ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins. The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes
IKVTVKCSNGKKFTVEVEPDATVLELKELIAEKSDIPAEQQRLIYKGKILKDEETLSSYKIQDGHTVHLV
KGA
>gnl|CDD|340524 cd16107, Ubl_AtUPL5_like, ubiquitin-like (Ubl) domain found in Arabidopsis thaliana ubiquitin-protein ligase 5 (AtUPL5) and similar proteins. Arabidopsis thaliana AtUPL5, also termed HECT-type E3 ubiquitin transferase UPL5, is an E3 ubiquitin-protein ligase that contains a ubiquitin-like domain (Ubl), a C-type lectin-binding domain, a leucine zipper and a HECT domain. HECT domain containing-ubiquitin-protein ligases have more than one member in different genomes, these proteins have been classified into four sub-families (UPL1/2, UPL3/4, UPL5 and UPL6/7). AtUPL5 fUPL5 regulates leaf senescence in Arabidopsis through degradation of the transcription factor WRKY53
QIFVRTYCGKTIVLHAKASDTVESLHQQIEARTGIPSLEQRLIFGGRQLQHSQSLESCKMENDATLFLVA
>gnl|CDD|340525 cd16108, Ubl_ATG8_like, ubiquitin-like (Ubl) domain found in autophagy-related 8 (ATG8) and similar proteins. The ATG8 family of proteins constitute a single member in Saccharomyces cerevisiae, Atg8p, and multiple homologs in higher eukaryotes, they are multifunctional ubiquitin-like (Ubl) key regulators of autophagy. The ATG8 system is a Ubl conjugation system that is essential for autophagosome formation. In the ATG8 system, a cysteine protease (ATG4) cleaves a C-terminal arginine from ATG8, and then the exposed C-terminal glycine is conjugated to phosphatidylethanolamine (PE) by ATG7, an E1-like enzyme, and ATG3, an E2-like enzyme. The mammalian ATG8 family is classified into three subfamilies: i) MAP1LC3 (microtubule associated protein 1 light chain 3) which includes MAP1LC3A, MAP1LC3B, MAP1LC3B2, and MAP1LC3C, ii) GABARAP (GABA type A receptor associated protein) which includes GABARAP, GABARAPL1, and GABARAPL3, and iii) GABARAPL2 (GABA type A receptor associated protein like 2), also known as GATE-16 (golgi-associated adenosine triphosphatase enhancer of 16 kDa)
DRIPVIVEKAPKSDLPDIDKKKFLVPSDLTVGQFMYIIRKRIKLSPEKAIFLFVNNTLPPTSALMSEVYE
EYKDEDGFLYVKYSG
>gnl|CDD|340526 cd16109, DCX1, Dublecortin-like domain 1. Members of the doublecortin (DCX) gene family are microtubule-associated proteins (MAPs). Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its protein domains can occur in double tandem or single repeats. The family represents the first repeat of the DCX domain which has a stable ubiquitin-like tertiary fold. Proteins with DCX double tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK)
KAKKVRFYRNGDRFFKGIVYAVSSERFRSFEALLADLTRSLSDNVNLPQGVRTIFTIDGSRKITSLDELE
DGESYVCASTDAFKK
>gnl|CDD|340527 cd16110, DCX1_RP_like, Doublecortin-like domain 1 found in retinitis pigmentosa (RP)-like protein. RP-like protein family is part of doublecortin (DCX) family. It has double tandem DCX repeats that are associated with retinitis pigmentosa. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. RP-like proteins are colocalized to the photoreceptor and share a function in outer segment disc morphogenesis
KNVTFYKDGDVHFSGVRVAINPRRYRTFDALLDELSRKVPLPFGVRSITTPRGRHSITSLEQLEDGGKYV
CSSKR
>gnl|CDD|340528 cd16111, DCX_DCLK3, Doublecortin-like domain found in doublecortin-like kinase 3 (DCLK3). DCLK3 is a member of doublecortin (DCX) protein family. It functions as a microtubule-associated protein (MAP). DCLK3 contains only one N-terminal doublecortin domain (DCX), unlike DCLK1 and DCLK2 which each have two conserved DCX domains. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule binding domains, DCLK3 has a serine/threonine kinase domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases
KPKVITVVRNGGQPRTKITILLNRRSVQTFEQLMADISEALGFPRWKNDRVRKLYSLRGREVRSVSDFFR
EDDVFIATGREQLTL
>gnl|CDD|340529 cd16112, DCX1_DCX, Dublecortin-like domain 1 found in neuronal migration protein doublecortin (DCX). DCX, also termed doublin or lissencephalin-X (Lis-XDCX), is a microtubule-associated protein (MAP). It belongs to the doublecortin (DCX) family, has double tandem DCX repeats, and is expressed in migrating neurons. Structure studies show that the N-terminal DCX domain has a stable ubiquitin-like fold. DCX is not only a unique MAP in terms of structure, it also interacts with multiple additional proteins. Mutations in the human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation
KAKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLTRSLSDNINLPQGVRYIYTIDGSRKIGSMDELE
EGESYVCSSDNFFKKVEYT
>gnl|CDD|340530 cd16113, DCX2_DCDC2_like, Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2). DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of a ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with
PKTIHVFPNGDLLHPPSKVLLTKRRLPNWDTVLEEVTEKVKLQTGAVRKLYTLDGKRISDPDELVNGGQY
VAVG
>gnl|CDD|340531 cd16114, Ubl_SUMO1, ubiquitin-like (Ubl) domain found in small ubiquitin-related modifier 1 (SUMO-1) and similar proteins. SUMO (also known as "Smt3" and "sentrin" in other organisms) resembles ubiquitin (Ub) in structure, ligation to other proteins and the mechanism of ligation. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of Ub and the epsilon-amino group of a substrate lysine. SUMOs, like Ub, are covalently conjugated to lysine residues in a wide variety of target proteins in eukaryotic cells and regulate numerous cellular processes, such as transcription, epigenetic gene control, genomic instability, and protein degradation. Four SUMO paralogs exist in mammals, SUMO1 through SUMO4. SUMO2-SUMO4 are more closely related to each other than they are to SUMO1. SUMO1 is a binding partner of the RAD51/52 nucleoprotein filament proteins, which mediate DNA strand exchange. SUMO1 conjugation to cellular proteins has been implicated in multiple important cellular processes, such as nuclear transport, cell cycle control, oncogenesis, inflammation, and the response to virus infection
YIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRINDNHTPKELGMEEEDVIEV
YQEQTG
>gnl|CDD|340532 cd16115, Ubl_SUMO2_3_4, ubiquitin-like (Ubl) domain found in small ubiquitin-related modifier SUMO-2, SUMO-3, SUMO-4, and similar proteins. SUMO (also known as "Smt3" and "sentrin" in other organisms) resembles ubiquitin (Ub) in structure, ligation to other proteins and the mechanism of ligation. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of Ub and the epsilon-amino group of a substrate lysine. SUMOs, like Ub, are covalently conjugated to lysine residues in a wide variety of target proteins in eukaryotic cells and regulate numerous cellular processes, such as transcription, epigenetic gene control, genomic instability, and protein degradation. The mammalian SUMOs have four paralogs, SUMO1 through SUMO4. SUMO2 and SUMO3 are more closely related to each other than they are to SUMO1. SUMO2/3 are capable of forming chains on substrate proteins through internal lysine residues. The basic biology of SUMO4 remains unclear. A M55V polymorphism in SUMO4 has been associated with susceptibility to type I diabetes in some genetic studies
HINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCDRQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDV
FQ
>gnl|CDD|340533 cd16116, Ubl_Smt3_like, ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae ubiquitin-like protein Smt3p and similar proteins. Smt3 (Suppressor of Mif Two 3) was originally isolated as a high-copy suppressor of a mutation in MIF2, the gene of a centromere binding protein in S. cerevisiae. Smt3p is the yeast homolog of small ubiquitin-related modifier (SUMO) proteins that are involved in post-translational protein modification called SUMOylation, covalently attaching to and detaching from other proteins in cells to modify their function. SUMO resembles ubiquitin (Ub) in its structure, its ability to be ligated to other proteins, as well as in the mechanism of ligation. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of Ub and the epsilon-amino group of a substrate lysine. Smt3p plays essential roles in cell-cycle regulation and chromosome segregation in budding yeast. It interacts with different modification enzymes, and regulates their functions through linking covalently to its targets
EHINLKVKDQDGNEVFFKIKRTTPLRKLMEAYCKRQGKSMDSVRFLFDGERIREDQTPEDLGMEDGDEID
AMVE
>gnl|CDD|340534 cd16117, UBX_UBXN4, Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins. UBXN4, also termed ERAD (endoplasmic-reticulum-associated protein degradation) substrate erasing protein (erasin), or UBX domain-containing protein 2 (UBXD2), or UBXDC1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN4 is an endoplasmic reticulum (ER) localized protein that interacts with p97 (also known as VCP or Cdc48) via its UBX domain. Erasin exists in a complex with other p97/VCP-associated factors involved in endoplasmic-reticulum-associated protein degradation (ERAD). p97 is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The overexpression of UBXN4 increases degradation of a classical ERAD substrate and UBXN4 levels are increased in ER stressed cells. Anti-UBXN4 staining is increased in neuropathological lesions in brains of patients with Alzheimer's disease
TARIQFRLPDGSSFTNQFPSDAPLEEARQFVAQTVGPAYGPFSLATTFPRREFTDDDYQKTLLELELAPS
AALVVLP
>gnl|CDD|340535 cd16118, UBX2_UBXN9, Ubiquitin regulatory domain X (UBX) 2 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) and similar proteins. UBXN9, also termed tether containing UBX domain for GLUT4 (TUG), or alveolar soft part sarcoma chromosomal region candidate gene 1 protein (ASPSCR1), or alveolar soft part sarcoma locus (ASPL), or renal papillary cell carcinoma protein 17 (RCC17), belongs to the UBXD family of proteins that contains two ubiquitin regulatory domains X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, UBXN9 contains an N-terminal ubiquitin-like (Ubl) domain. UBXN9 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. However, high-affinity interacting protein ASPL efficiently promotes p97 hexamer disassembly, resulting in the formation of stable p97:ASPL heterotetramers; the extended UBX domain (eUBX) in ASPL is critical for p97 hexamer disassembly and facilitates the assembly of p97:ASPL heterotetramers.UBXN9 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4, assembly of the Golgi apparatus. In addition to GLUT4, UBXN9 also controls vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. UBXN9 and its budding yeast ortholog, Ubx4p, are multifunctional proteins that share some, but not all functions. Yeast Ubx4p is important for endoplasmic reticulum-associated protein degradation (ERAD) but UBXN9 appears not to share this function
AVIRVQFPDRLVLQAFFRPLETVRALYDFVKSHLADPDLPFYLYTTPPKRVLKDKNKTLYQAGLVPAALV
YFGL
>gnl|CDD|340536 cd16119, UBX_UBXN6, Ubiquitin regulatory domain X (UBX) found in UBX domain protein 6 (UBXN6) and similar proteins. UBXN6, also termed UBX domain-containing protein 1 (UBXD1), and UBXDC2, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN6 acts as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. Unlike other p97 cofactors that binds the N-domain of p97 through their UBX domain, UBXN6 binds p97 in two regions, at the p97 C terminus via a PUB domain and at the p97 N-domain with a short linear interaction motif termed VIM. Its UBX domain is not functional for the binding of p97. The UBXN6-p97 complex regulates the endolysosomal sorting of ubiquitylated plasma membrane protein caveolin-1 (CAV1), as well as the trafficking of ERGIC-53-containing vesicles by controlling the interaction of transport factors with the cytoplasmic tail of ERGIC-53. In addition, UBXN6 is a regulatory component of endoplasmic reticulum-associated degradation (ERAD) that may modulate the adaptor binding to p97
YTLIRVRFPDGVILQGTFYAREKLSAVREFVREALANDWLPFELVTPGGQKLTDEDATLAELGLVPAALL
NFS
>gnl|CDD|340537 cd16120, UBX_UBXN3B, Ubiquitin regulatory domain X (UBX) found in FAS associated factor 2 (FAF2, also known as UBXN3B) and similar proteins. UBX domain-containing protein 3B (UBXN3B), also termed protein ETEA, or FAF2, or UBX domain-containing protein 8 (UBXD8), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. FAF2 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The p97-UBXD8 complex destabilizes mRNA by promoting release of ubiquitinated the RNA-binding protein HuR from messenger ribonucleoprotein (mRNP). Moreover, FAF2 is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. A yeast two-hybrid assay showed that FAF2 can interact with Fas
VKILFKLPNGTRLERRFLKSDSLKVLYDFVFSHEDSPDKFQLVTNFPRRVLPCQPTEEQPNPPTLEEAGL
GKSEVLFVQD
>gnl|CDD|340538 cd16121, FERM_F1_SNX17, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 17 (SNX17). SNX17 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. It localizes to early endosomes, and plays an important role in mediating endocytic internalization, recycling, and/or protection from lysosomal degradation of NPxY-motif containing cell surface proteins including amyloid precursor protein (APP), P-selectin, beta1-integrin, low density lipoprotein receptor (LDLR), LDLR related protein (Lrp1), ApoER2, and FEEL1. SNX17 also affects T cell activation by regulating T cell receptor and integrin recycling. SNX17 contains a PX (Phox homology) domain and a FERM (Band 4.1, ezrin, radixin, moesin) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
EEVSLDVFLMNGQKITVNISSTDQTDDVLEAVASKLGLPEELVYYFALFLVKKDDDGNNTIVRKLQDFES
PYLSLKSAGKGSHRIVLRKSYWD
>gnl|CDD|340539 cd16122, FERM_F1_SNX31, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 31 (SNX31). SNX31 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. It is a novel sorting nexin associated with the uroplakin-degrading multivesicular bodies in terminally differentiated urothelial cells. SNX31 binds multiple beta integrin cytoplasmic domains and regulates beta1 integrin surface levels and stability. SNX31 contains a PX (Phox homology) domain and a FERM (Band 4.1, ezrin, radixin, moesin) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
IHTLKAVLDVYLPDGRSVRIDVKTSDTAERVLEVVLDRIGLSRELRGYFSLFLVKGKGKGDFSVVKKLAP
FELPYVTLESGEMERCKLGIRKWYMDPS
>gnl|CDD|340540 cd16123, RA_RASSF7_like, Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, RASSF9, and RASSF10. The RASSF family of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain either in the C-terminus (RASSF1-6) or N-terminus (RASSF7-10). RASSF7-10 lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The structural differences between the C-terminus and N-terminus RASSF subgroups have led to the suggestion that they are two distinct families. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ras proteins are small GTPases that are involved in cellular signal transduction. The N-terminus RASSF proteins are potential Ras effectors that have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia
ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQTNDTGRYVLVERWRGIERPLPPRTRILKVWKAWGE
EQSNVQFVLRR
>gnl|CDD|340541 cd16124, RA_GRB7_10_14, Ras-associating (RA) domain found in growth factor receptor-bound (Grb) protein 7/10/14. The RA domain is highly conserved among the members of the Grb proteins family which includes Grb7, Grb10 and Grb14. Grb7/10/14 are multi-domain cytoplasmic adaptor proteins that are recruited to activated receptor tyrosine kinases. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Grb7 and its related family members Grb10 and Grb14 share a conserved domain architecture that includes an amino-terminal proline-rich region, a central segment termed the GM region (for Grb and Mig) which includes the RA, PIR, and pleckstrin homology (PH) domains, and a carboxyl-terminal SH2 domain. The tandem RA and PH domains of Grb7/10/14 are also found in a second adaptor family, Rap1-interacting adaptor molecule (RIAM) and lamellipodin, which is involved in actin-cytoskeleton rearrangement. Grb7/10/14 family proteins are phosphorylated on serine/threonine as well as tyrosine residues and are mainly localized to the cytoplasm
KQVVKVYSEDGTSRSVEVAADATARDVCQLLVQKAHALDDESWTLVEHHPHLGLERGLEDHELVVEVQSA
WPVGGESKFVFRKNY
>gnl|CDD|340542 cd16125, RA_ASPP1_2, Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2. The ASPP protein (apoptosis-stimulating protein of p53; also called ankyrin repeat-, Src homology 3 domain- and Pro-rich region-containing protein) plays a critical role in regulating apoptosis. The ASPP family consists of three members, ASPP1, ASPP2 and iASPP, all of which bind to p53 and regulate p53-mediated apoptosis. ASPP1 and ASPP2, have a RA domain at their N-terminus and have pro-apoptotic functions, while iASPP is involved in anti-apoptotic responses. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin
VILKVYLSDNNQTVTEVPITPETTCQDVVDCCKEPGEENCHLVEVWRGCERPLPEEENPYEILQQWGSHR
DEVKFFLRHE
>gnl|CDD|340543 cd16126, Ubl_HR23B, ubiquitin-like (Ubl) domain found in UV excision repair protein RAD23 homolog B (HR23B). HR23B, also termed xeroderma pigmentosum group C (XPC) repair-complementing complex 58 kDa protein (p58), is tightly complexed with XPC protein to form the XPC-HR23B complex. Although it displays a high affinity for both single- and double-stranded DNA, the XPC-HR23B complex functions as a global genome repair (GGR)-specific repair factor that is specifically involved in global genome but not transcription-coupled nucleotide excision repair (NER). HR23B also interacts specifically with S5a subunit of the human 26S proteasome, and plays an important role in shuttling ubiquitinated cargo proteins to the proteasome. HR23B contains an N-terminal ubiquitin-like (Ubl) domain that binds proteasomes and two C-terminal ubiquitin-associated (UBA) domains that bind ubiquitin or multi-ubiquitinated substrates. In addition, it has a XPC protein-binding domain that might be necessary for its efficient NER function
MQITLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAGKILNDDTALKEYKIDEKNFV
VVMVTKPK
>gnl|CDD|340544 cd16127, Ubl_ATG8_GABARAP_like, ubiquitin-like (Ubl) domain found in gamma-aminobutyric acid receptor-associated protein (GABARAP) and similar proteins; sub-family of the autophagy-related 8 (ATG8) protein family. GABARAP (also termed GABA(A) receptor-associated protein, ATG8A, or MM46) has been implicated in intracellular protein trafficking. It is a cytosolic protein, localized to transport vesicles, the Golgi network and the endoplasmic reticulum. It interacts with the intracellular domain of the gamma2 subunit of GABA(A) receptors, and thus, functions as a trafficking modulator implicated in the intracellular trafficking of GABA(A) receptor. GABARAP also acts as a Ubl modifier belonging to the ATG8 (autophagy-related 8) protein family which is essential for autophagosome biogenesis and maturation. GABARAP recruits phosphatidylinositol 4-kinase II alpha (PI4KIIalpha) as a specific downstream effector, and regulates phosphatidylinositol 4-phosphate (PI4P)-dependent autophagosome lysosome fusion. This sub-family also includes GABARAPL1 (also termed GABA(A) receptor-associated protein-like, or GEC1), GABARAPL2/GATE-16, and GABARAPL3. GABARAPL1 has been involved in the intracellular transport of receptors via interactions with tubulin and GABA(A) or kappa opioid receptors. GABARAPL1 is also a Ubl modifier that functions as a mediator involved in androgen-regulated autophagy process. It is transcriptionally modulated by androgen receptor (AR) and has a repressive role in autophagy. In addition, GABARAPL1 is required for increased membrane expression of epidermal growth factor receptor (EGFR) during hypoxia, suggesting a possible role in the trafficking of these membrane proteins. GABARAPL1 may also play a key role in several important biological processes such as cancer or neurodegenerative diseases. Low expression of GABARAPL1 is associated with poor prognosis of patients with hepatocellular carcinoma
YKEDHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARVADLDKKKYLVPSDLTVGQFYFLIRKRIHLRPED
ALFFFVNNVIPPTSATMGQLYQEHHEEDFFLYIAYSD
>gnl|CDD|340545 cd16128, Ubl_ATG8, ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae Atg8p and related proteins; sub-family of the autophagy-related 8 (ATG8) family. The ATG8 family of proteins constitutes a single member in Saccharomyces cerevisiae, Atg8p, and multiple homologs in higher eukaryotes. These proteins are multifunctional ubiquitin-like (Ubl) key regulators of autophagy. ATG8 is characterized by a C-terminal ubiquitin-like (Ubl) domain with a short N-terminal extension. The covalent attachment of ATG8 to phosphatidylethanolamine (PtdEth) at the autophagosomal membrane places it at a crucial juncture during autophagosome formation. ATG Ubl proteins such as Saccharomyces cerevisiae Atg8p undergo a unique Ubl conjugation, a process essential for autophagosome formation
FEKRKAEAERIRDKYPDRIPVICEKAEKSDIPDIDKKKYLVPADLTVGQFVYVIRKRIKLSPEKAIFIFV
NNVLPPTAALMSAIYEEHKDEDGFLYVTYSGEN
>gnl|CDD|340546 cd16129, Ubl_ATG8_MAP1LC3, ubiquitin-like (Ubl) domain found in microtubule associate protein 1 light chain 3 (MAP1LC3). Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. MAP1LC3 (also known as LC3) has a ubiquitin-like (Ubl) fold and belongs to the ATG8 autophagy protein family. A Ubl conjugation of MAP1LC3 by the phospholipid phosphatidylethanolamine (PE) is an essential process for the formation of autophagosomes. MAP1LC3 is cleaved by the cysteine protease ATG4 and is then conjugated with PE by E1-like enzyme ATG7 and ATG3, an E2-like enzyme. The Ubl conversion of MAP1LC3 is known as a marker of autophagy-induction. This sub-family includes MAP1LC3A, MAP1LC3B, and MAP1LC3C, each encoded by a different MAP1LC3 gene
QRKKDVEEIREKHPNKIPVIIERYKGEKQLPLLDKTKFLVPDHVTMSELVKIIRRRLQLNPTQAFFLLVN
QRSMVSVSTPMSEVYRREKDEDGFLYMVYASQETF
>gnl|CDD|340547 cd16130, RA_Rin3, Ras-associating (RA) domain found in Ras and Rab interactor 3 (Rin3). Rin3, also termed Ras interaction/interference protein 3, is a RAS effector and a RAB5-activating guanine nucleotide exchange factor (GEF) specifically for GTPase Rab31. It functions as a negative regulator of mast cell responses to Stem Cell Factor (SCF). Rin3 contains the Vps9p-like guanine nucleotide exchange factor and Ras-association (RA) domains
QDFISVSFLEPGSNTRTLAIRPDTTAEDLCKQCAEKFEVLDPENYGLFVLVDGRCLQLADDALPHHIKSD
LLKSEPRKDFHFLYKQLS
>gnl|CDD|340548 cd16131, RA_Rin2, Ras-associating (RA) domain found in Ras and Rab interactor 2 (Rin2). Rin2, also termed Ras association domain family 4, or Ras inhibitor JC265, or Ras interaction/interference protein 2, is a Rab5 GDP/GTP exchange factor with the Vps9p-like guanine nucleotide exchange factor and Ras-association (RA) domains. Rin2 connects three GTPases, R-Ras, Rab5 and Rac1, to promote endothelial cell adhesion through the regulation of integrin internalization and Rac1 activation. Rin2 is involved in the regulation of Rab5-mediated early endocytosis. The deficiency of Rin2 can cause the RIN2 syndrome, an autosomal recessive connective tissue disorder
FQNYLRVAFQEVNSGCTAKTLLVRPYTTTEEVCQLCAQKFKVQDPENYSLFLLIDDTWQQLAEDTYPQKI
KAELHSRPQPQIFHFVYKRIP
>gnl|CDD|340549 cd16132, RA_RASSF10, Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10). RASSF10 is a member of a family of N-terminus RASSF7-10 proteins. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF10 is expressed in a wide variety of tissues and its expression in human thyroid, pancreas, placenta, heart, lung and kidney has been observed. RASSF10 is the most frequently methylated of the N-terminal RASSFs in some cancers such as in childhood acute lymphoblastic leukemia and both, thyroid cancer cell lines and primary thyroid carcinomas
KISVWLCQEEKLVSGLSRRTTCADVVRVLLEDQNRSQQEEEEEEGERDGGMLSGPPQSYCIVEKWRGFER
ILPNKTKILRLWAAWGEEQENVRFVLVRSEAS
>gnl|CDD|340550 cd16133, RA_RASSF9, Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9). RASSF9, also termed PAM COOH-terminal interactor protein 1 (P-CIP1), or peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor, is a member of N-terminus RASSF7-10 protein family. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of the N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF9 was formerly known as PAM COOH-terminal interactor-1 (P-CIP1) because of its interaction with peptidylglycine alpha-amidating mono-oxygenase (PAM) and possibility of its role in regulating the trafficking of integral membrane PAM. RASSF9 is widely expressed in multiple organs such as testis, kidney, skeletal muscle, liver, lung, brain, and heart. Cloned RASSF9 showed preferential binding to N-Ras and K-Ras
EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEHEATFGEKRFLLGQPSDYCIVEKWRGFERVLPPLTKIL
RLWKAWGDEQPNLQFVLVKADAF
>gnl|CDD|340551 cd16134, RA_RASSF8, Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8). RASSF8, also termed carcinoma-associated protein HOJ-1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF8 has been described as a potential tumor suppressor. RASSF8 might have a role in the regulation of cell-cell adhesion and cell growth
ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYAS
DVQFILRRTGPS
>gnl|CDD|340552 cd16135, RA_RASSF7, Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7). RASSF7, also termed HRAS1-related cluster protein 1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF7 is a potential Ras effector as its function has been linked to some key biological processes including the regulation of cell death and proliferation; for example, RASSF7 is up-regulated in pancreatic cancer
MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYA
NDVQFILRRTGPS
>gnl|CDD|340553 cd16136, RA_MRL_Lpd, Ras-associating (RA) domain found in the adapter protein lamellipodin (Lpd). Lpd, also termed Ras-associated and pleckstrin homology domains-containing protein 1 (RAPH1), or amyotrophic lateral sclerosis 2 chromosomal region candidate gene 18 protein, or amyotrophic lateral sclerosis 2 chromosomal region candidate gene 9 protein, or proline-rich EVH1 ligand 2 (PREL-2), or protein RMO1, is a member of MRL (Mig10/RIAM/Lpd) family proteins that regulates cell migration and promote lamellipodia protrusion in fibroblast by interacting with Ena/VASP proteins. MRL proteins share a common structural architecture, including a central structural unit consisting of an RA domain and a pleckstrin homology (PH) domain, an upstream coiled-coil region, and a number of polyproline motifs. Lpd also contains a helical region at the amino terminus for talin binding. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. RA and PH domain in Lpd form a tandem domain pair (RA-PH), and serve tightly coordinated functions in both Ras GTPase signaling via the RA domain and membrane translocalization via the PH domain. Lpd also exhibits other unique enzymatic functions including its catalytic activity of butyrylcholinesterase, a potent therapeutic treatment targeting cocaine abuse
QVKKLVIRVHMSDDSSKTMMVDERQTVRQVLDNLMDKSHCGYSLDWSLVETISELQMERIFEDHENLVEN
LLNWTRDSQNKLMFVERIEK
>gnl|CDD|340554 cd16137, RA_MRL_RIAM, Ras-associating (RA) domain found in Rap1-GTP-interacting adapter molecule (RIAM). RIAM, also termed amyloid beta A4 precursor protein-binding family B member 1-interacting protein, or APBB1-interacting protein 1, or proline-rich EVH1 ligand 1 (PREL-1), or proline-rich protein 73, or retinoic acid-responsive proline-rich protein 1 (RARP-1), is a member of MRL (Mig10/RIAM/Lpd) family proteins that regulates cell migration and promote lamellipodia protrusion in fibroblast by interacting with Ena/VASP proteins. RIAM regulates cell migration and mediates Rap1-induced cell adhesion. MRL proteins share a common structural architecture, including a central structural unit consisting of an RA domain and a pleckstrin homology (PH) domain, an upstream coiled-coil region, and a number of polyproline motifs. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. RIAM also contains a helical region at the amino terminus for talin binding. RA and PH form a tandem domain pair (RA-PH), and serve tightly coordinated functions in both Ras GTPase signaling via the RA domain and membrane translocalization via the PH domain
KKLVVKVHMNDSSTKTLMVDERQTVRDVLDNLFEKTHCDCNVDWCLYEVNPELQIERFFEDHENVVEVLS
DWTRDSENKVLFLEKKEKY
>gnl|CDD|340555 cd16138, RA_MRL_MIG10, Ras-associating (RA) domain found in Caenorhabditis elegans abnormal cell migration protein 10 (MIG-10) and similar proteins. MIG-10 is lamellipodin (Lpd) found in C. elegans. It stabilizes invading cell adhesion to basement membrane and is a negative transcriptional target of Evi-1 proto-oncogene, EGL-43, in C. elegans. It also shows netrin-independent functions and is a transcriptional target of FOS-1A, a transcription factor that promotes basement membrane breaching, during anchor cell invasion in C. elegans. MIG-10 is a member of MRL (Mig10/RIAM/Lpd) family of proteins that is involved in antero-posterior migration of embryonic neurons CAN (canalassociated neurons), ALM (anterior lateral microtubule cells) and HSN (hermaphrodite-specific neurons). MRL proteins share a common structural architecture, including a central structural unit consisting of an RA domain and a pleckstrin homology (PH) domain, an upstream coiled-coil region, and a number of polyproline motifs. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. RA and PH form a tandem domain pair (RA-PH), and serve tightly coordinated functions in both Ras GTPase signaling via the RA domain and membrane translocalization via the PH domain
KKLFVKAFTEDGSAKSLLVDERMTVGHVTRLLADKNHVAMMPDWAIVEHIPDLYMERVYEDHEKLVENLM
MWTRDSPNRLLFMERP
>gnl|CDD|340556 cd16139, RA_GRB14, Ras-associating (RA) domain found in growth factor receptor-bound (Grb) protein 14. Grb14, a member of cytoplasmic adaptor proteins, is a tissue-specific negative regulator of insulin signaling. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub). Ubi is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. A novel function of Grb14 RA domain is to interact with the nucleotide binding pocket of a cyclic nucleotide gated channel alpha subunit (CNGA1) and inhibits its activity. Grb7 and its related family members Grb10 and Grb14 share a conserved domain architecture that includes an amino-terminal proline-rich region, a central segment termed the GM region (for Grb and Mig) which includes the RA, PIR, and PH domains, and a carboxyl-terminal SH2 domain. Grb7/10/14 family proteins are phosphorylated on serine/threonine as well as tyrosine residues and are mainly localized to the cytoplasm
KQVIKVYSEDDTSRALEVPNDITARDVCQLFILKNHYIDDHSWTLFEHLPHIGLERIIEDHESVIEVQSN
WGMETDSRLYFRKNY
>gnl|CDD|340557 cd16140, RA_GRB7, Ras-associating (RA) domain found in growth factor receptor-bound (Grb) protein 7. GRB7, also termed B47, or epidermal growth factor receptor GRB-7, or GRB7 adapter protein, is a signal-transducing cytoplasmic adaptor protein that is co-opted by numerous tyrosine kinases involved in various cellular signaling and functions. Grb7 and its related family members Grb10 and Grb14 share a conserved domain architecture that includes an amino-terminal proline-rich region, a central segment termed the GM region (for Grb and Mig) which includes the RA, PIR, and pleckstrin homology (PH) domains, and a carboxyl-terminal SH2 domain. The tandem RA and PH domains of Grb7/10/14 are also found in a second adaptor family, Rap1-interacting adaptor molecule (RIAM) and lamellipodin, which is involved in actin-cytoskeleton rearrangement. Grb7/10/14 family proteins are phosphorylated on serine/threonine as well as tyrosine residues and are mainly localized to the cytoplasm. Grb7 could interact with activated N-Ras in transfected cells
GPHVVKVYSEDGTCRSLEVTAGATARHVCEMLVQRAHCLDDESWSLVELHPHLALERCLEDHESVVEVQA
TWPAGGDSRFVFRKNFAK
>gnl|CDD|340558 cd16141, RA_GRB10, Ras-associating (RA) domain found in growth factor receptor-bound (Grb) protein 10. GRB10, also termed insulin receptor-binding protein Grb-IR, is a multi-domain cytoplasmic adaptor protein that binds to the insulin-like growth factor 1 receptor (IGF-1R) and inhibits insulin signaling. Grb10 and its related family members Grb7 and Grb14 share a conserved domain architecture that includes an amino-terminal proline-rich region, a central segment termed the GM region (for Grb and Mig) which includes the RA, PIR, and pleckstrin homology (PH) domains, and a carboxyl-terminal SH2 domain. The tandem RA and PH domains of Grb7/10/14 are also found in a second adaptor family, Rap1-interacting adaptor molecule (RIAM) and lamellipodin, which is involved in actin-cytoskeleton rearrangement. Grb7/10/14 family proteins are phosphorylated on serine/threonine as well as tyrosine residues and are mainly localized to the cytoplasm. Grb14 binds to both GTPase-defective mutant Rab5 as well as CNGA1, whereas Grb10 binds only to GTP-bound form of active Rab5
EKHIVKVFSEDGTSKVVEILADMTARDLCQLLVYKSHCVDDNSWTLVEHHPHLGLERCLEDHELVVQVQS
TMGSESKFLFRKNYAKYEFFKN
>gnl|CDD|293761 cd16142, ARS_like, uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNILVILGDDIGWGDLGCYGGGIGRGAPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGLT
TVGLPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYHTIDEEIVDKAI
DFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSSGKGKYADSMVELDDHVGQILDALDELGIADNTI
VIFTTDNGPEQDVWPDGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAG
APDPKDKLLGKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKNWKVHFKAQEDTGGPTGEPF
YVLTFPLIFNLRRDPKERYDVT
>gnl|CDD|293762 cd16143, ARS_like, uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNIVIILADDLGYGDISCYNPDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKG
GVLGGFSPPLIEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAATGTGKDVDYSKPIKGGPLDH
GFDYYFGIPASEVLPTLTDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYEL
DWVVGRILDALKELGLAENTLVIFTSDNGPSPYADYKELEKFGHDPSGPLRGMKADIYEGGHRVPFIVRW
PGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGSFAIR
KGDWKLIDGTGSGGFSYPRGKEKLGLPPGQLYNLSTDPGESNNLY
>gnl|CDD|293763 cd16144, ARS_like, uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDV
IPGRRGPPDNTKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIGGTGN
GGPPSYYFPPGKPNPDLEDGPEGEYLTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELIEKYE
KKKKGLRKGQKNPVYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTSNAPLRGGK
GSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLP
RRALFWHFPHYHGQGGRPASAIRKGDWKLIEFYEDGRVELYNLKNDIGETNNLAAEMPEKAAELKKKLDA
W
>gnl|CDD|293764 cd16145, ARS_like, uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGN
SEPGGQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHPTKQGFDYFYGYLDQVHAHNYYPEYLW
RNGEKVPLPNNVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDDGP
YKYKPKDPGIYAYLPWPQPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSEGGSEHDP
DFFDSNGPLRGYKRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLL
PTLLGKPQQQQHDYLYWEFYEGGGAQAVRMGGWKAVRHGKKDGPFELYDLSTDPGETNNLAAQHP
>gnl|CDD|293765 cd16146, ARS_like, uncharacterized arylsulfatase. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTGVWHTI
LGRERMRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGGGIGQYPDYWGNDYFDD
TYYHNGKFVKTEGYCTDVFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAF
YGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRFNAGMRGKKGSVYEGGHRVPFFIRWP
GKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLFTHSGRWPPPPKK
KRNAAVRTGRWRLVSPKGFQPELYDIENDPGEENDVADEHPEVVKRLKAAYEAWWDDVK
>gnl|CDD|293766 cd16147, G6S, glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1). N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs)
RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPP
GGGYPKFWQNGLERSTLPVWLQEAGYRTAYAGKYLNGYGVPGGVSYVPPGWDEWDGLVGNSTYYNYTLSN
GGNGKHGVSYPGDYLTDVIANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPPRPP
PNNPDVSDKPHWLRRLPPLNPTQIAYIDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNG
YHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGAPPPSDMDGRSCGDS
NNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL
>gnl|CDD|293767 cd16148, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGG
PLEPDDPTLAEILRKAGYYTAAVSSNPHLFGGPGFDRGFDTFEDFRGQEGDPGEEGDERAERVTDRALEW
LDRNADDDPFFLFLHYFDPHEPYLYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLY
WGHGSNLYDEQLHVPLIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP
>gnl|CDD|293768 cd16149, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDW
IVEGSHGKTKKPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLGDDAADFLRRRAEAEKPFFLSVNYTAPHS
PWGYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKGNGTFPLNMYDNSVKVPFI
IRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPGRSFAD
>gnl|CDD|293769 cd16150, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTL
HHLLRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYCDSDEACVRTAIDWLRNRRPDKPFCLYLPL
IFPHPPYGVEEPWFSMIDREKLPPRRPPGLRAKGKPSMLEGIEKQGLDRWSEERWRELRATYLGMVSRLD
HQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALV
ELVDIPPTLLDLAGIPLSHTHFGRSLLPVLAGETEEHRDAVFSEGGRLHGEEQAMEGGHGPYDLKWPRLL
QQEEPPEHTKAVMIRTRRYKYVYRLYEPDELYDLEADPLELHNLIGDPAYAEIIAEMKQRLLRWMVETSD
VVP
>gnl|CDD|293770 cd16151, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVFGY
LDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGDYPHEFGFDEYCLWQLTETGEKYSRPATPTFNIRNG
KLLETTEGDYGPDLFADFLIDFIERNKDQPFFAYYPMVLVHDPFVPTPDSPDWDPDDKRKKDDPEYFPDM
VAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTNGREVRGGKGKTTDAGTHVPLIVNWPGL
IPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWYYRNPHKKFGSRF
VRTKRYKLYADGRFFDLREDPLEKNPL
>gnl|CDD|293771 cd16152, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFR
NGIPLPADEKTLAHYFRDAGYETGYVGKWHLAGYRVDALTDFAIDYLDNRQKDKPFFLFLSYLEPHHQND
RDRYVAPEGSAERFANFWVPPDLAALPGDWAEELPDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTS
DHGCHFRTRNAEYKRSCHESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLL
PLVDGKVEDWRNEVFIQISESQVGRAIRTDRWKYSVAAPDKDGWKDSGSDVYVEDYLYDLEADPYELVNL
IGRPEYREVAAELRERLLARMAE
>gnl|CDD|293772 cd16153, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
KPNILWIITDDQRVDSLSCYNNAHTGKSESRLGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTG
RYPHRTGVYGFEAAHPALDHGLPTFPEVLKKAGYQTASFGKSHLEAFQRYLKNANQSYKSFWGKIAKGAD
SDKPFFVRLSFLQPHTPVLPPKEFRDRFDYYAFCAYGDAQVGRAVEAFKAYSLKQDRDYTIVYVTGDHGW
HLGEQGILAKFTFWPQSHRVPLIVVSSDKLKAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL
FE
>gnl|CDD|293773 cd16154, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNILLIIADDQGLDSSAQYSLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGVLA
VPDELLLSEETLLQLLIKDATTAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGILGGGVQDYYNWNLTNN
GQTTNSTEYATTKLTNLAIDWIDQQTKPWFLWLAYNAPHTPFHLPPAELHSRSLLGDSADIEANPRPYYL
AAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGTPGQVVDLPYTRNHAKGSLYEGGINVPLIVSGAGVE
RANERESALVNATDLYATIAELAGVDAAEIHDSVSFKPLLSDVNASTRQYNYTEYESPTTTGWATRNQYY
KLIESENGQEELYDLINDPSEQ
>gnl|CDD|293774 cd16155, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWSGAVCVPSRAMLMTGRTLFH
APEGGKAAIPSDDKTWPETFKKAGYRTFATGKWHNGFADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQA
PPEYLDMYPPETIPLPENFLPQHPFDNGEGTVRDEQLAPFPRTPEAVRQHLAEYYAMITHLDAQIGRILD
ALEASGELDNTIIVFTSDHGLAVGSHGLMGKQNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLC
ELAGIEIPESVEGKSLLPVIRGEKKAVRDTLYGAYRDGQRAIRDDRWKLIIYVPGVKRTQLFDLKKDPDE
LNNLADEPEYQERLKKLLAELK
>gnl|CDD|293775 cd16156, sulfatase_like, uncharacterized sulfatase subfamily; includes Escherichia coli YidJ. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTN
CMALGDNVKTIGQRLSDNGIHTAYIGKWHLDGGDYFGNGICPQGWDPDYWYDMRNYLDELTEEERRKSRR
GLTSLEAEGIKEEFTYGHRCTNRALDFIEKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENA
YDDLENKPLHQRLWAGAKPHEDGDKGTIKHPLYFGCNSFVDYEIGRVLDAADEIAEDAWVIYTSDHGDML
GAHKLWAKGPAVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIE
DPEIPENRGVFVEFGRYEVDHDGFGGFQPVRCVVDGRYKLVINLLSTDELYDLEKDPYEMHNLIDDPDYA
DVRDQLHDELLDYMNETRDPFRGYYWECRPWRKDARRPSWDYTGYTRQ
>gnl|CDD|293776 cd16157, GALNS, galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS). Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A
KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYT
TNAHARNAYTPQNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCHFGP
YDNKAYPNIPVYRDWEMIGRYYEEFKIDKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAP
VYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALISAPEQGGSNGPFLC
GKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKEK
DRPIFYYRGDELMAVRLGQYKAHFWTWSNSWEEFRKGINFCPGQNVPGVTTHNQTDHTKLPLLFHLGRDP
GEKYPISFKSAEYKQAMPRISKVVQQHQKTLVPGEPQLNVCDLAVM
>gnl|CDD|293777 cd16158, ARSA, Arylsulfatase A or cerebroside-sulfatase. Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form
PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYP
GVFYPGSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGTYLPTHQGFDHYLGIPYSHDQGPCQNL
TCFPPNIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTH
YPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRKSRGGNAGLLK
CGKGTTYEGGVREPAIAYWPGRIKPGVTHELASTLDILPTIAKLAGAPLPNVTLDGVDMSPILFEQGKSP
RQTFFYYPTSPDPDKGVFAVRWGKYKAHFYTQGAAHSGTTPDKDCHPSAELTSHDPPLLFDLSQDPSENY
NLLGLPEYNQVLKQIQQVKERFEASMKFGESEINKGEDPALEPCCKPGCTPKPSCCQCH
>gnl|CDD|293778 cd16159, ES, Estrone sulfatase. Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen
KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMAS
SHGMRVILFTASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLT
NLKDCGDGSNGEYDLSFDPLFPLLTAFVLITALTIFLLLYLGAVSKRFFVFLLILSLLFISLFFLLLITN
RYFNCILMRNHEVVEQPMSLENLTQRLTKEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGR
YGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLEEISVGGEYGGGNGGIYGGKKMGGWEGGIR
VPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLMPLLTGQEKRSPHEFLFHYCG
AELHAVRYRPRDGGAVWKAHYFTPNFYPGTEGCCGTLLCRCFGDSVTHHDPPLLFDLSADPSESNPLDPT
DEPYQEIIKKILEAVAEHQSSIEPVESQLSF
>gnl|CDD|293779 cd16160, spARS_like, sea urchin arylsulfatase-like. This family includes sea urchin arylsulfatase and its homologous proteins. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG
GTRVFLPWDIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFDFVGTNLPFTNS
WACDDTGRHVDFPDRSACFLYYNDTIVEQPIQHEHLTETLVGDAKSFIEDNQENPFFLYFSFPQTHTPLF
ASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKGGKG
NSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDD
ILYYCCSRLMAVRYGSYKIHFKTQPLPSQESLDPNCDGGGPLSDYIVCYDCEDECVTKHNPPLIFDVEKD
PGEQYPLQPSVYEHMLEAVEKLIAH
>gnl|CDD|293780 cd16161, ARSG, arylsulfatase G. Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder
KPNFLLLFADDLGWGDLGANWAPNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVG
HNFLPTSVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHDSSLADRYAQ
FATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRGPYGDALQEMDDLVGQIMDAVKHAGLKD
NTLTWFTSDNGPWEVKCELAVGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVST
LDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAGAGALSAVRCGDYKAHYATGG
ALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT
>gnl|CDD|293881 cd16162, OCRE_RBM5_like, OCRE domain found in RNA-binding protein RBM5, RBM10, and similar proteins. RBM5 is a known modulator of apoptosis. It may also act as a tumor suppressor or an RNA splicing factor; it specifically binds poly(G) RNA. RBM10, a paralog of RBM5, may play an important role in mRNA generation, processing, and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. Both RBM5 and RBM10, contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), an OCtamer REpeat (OCRE) domain, two C2H2-type zinc fingers, and a G-patch/D111 domain
PPPDPSTYQYDETSGYYYDPTTGLYYDPNSQYFYNSQTQQYLYWDQTKKTYVPVPT
>gnl|CDD|293882 cd16163, OCRE_RBM6, OCRE domain found in RNA-binding protein 6 (RBM6) and similar proteins. RBM6, also called lung cancer antigen NY-LU-12, or protein G16, or RNA-binding protein DEF-3, has been predicted to be a nuclear factor based on its nuclear localization signal. It shows high sequence similarity to RNA-binding protein 5 (RBM5 or LUCA15 or NY-REN-9). Both specifically binds poly(G) RNA. RBM6 contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), an OCtamer REpeat (OCRE) domain, two C2H2-type zinc fingers, a nuclear localization signal, and a G-patch/D111 domain. In contrast to RBM5, RBM6 has an additional unique domain, the POZ (poxvirus and zinc finger) domain, which may be involved in protein-protein interactions and inhibit binding of target sequences by zinc fingers
EGSGPAPTYRSDPDSGYIYDPETGYYYDPVTGLYYDPATGEYVDPDTGTLPYDPSTG
>gnl|CDD|293883 cd16164, OCRE_VG5Q, OCRE domain found in angiogenic factor VG5Q and similar proteins. VG5Q, also called angiogenic factor with G patch and FHA domains 1 (AGGF1), or G patch domain-containing protein 7, or vasculogenesis gene on 5q protein, functions as a potent angiogenic factor in promoting angiogenesis through interacting with TWEAK (also known as TNFSF12), which is a member of the tumor necrosis factor (TNF) superfamily that induces angiogenesis in vivo. VG5Q can bind to the surface of endothelial cells and promote cell proliferation, suggesting that it may act in an autocrine fashion. The chromosomal translocation t(5;11) and the E133K variant in VG5Q are associated with Klippel-Trenaunay syndrome (KTS), a disorder characterized by diverse effects in the vascular system. In addition to a forkhead-associated (FHA) domain and a G-patch motif, VG5Q contains an N-terminal OCtamer REpeat (OCRE) domain that is characterized by a 5-fold, imperfectly repeated octameric sequence
AAVSQSGFVYDEATGMYYDPSTGYYYDSETQLYYDPNTGTYYYYDEESGSYQFH
>gnl|CDD|293884 cd16165, OCRE_ZOP1_plant, OCRE domain found in Zinc-finger and OCRE domain-containing Protein 1 (ZOP1) and similar proteins found in plant. ZOP1 is a novel plant-specific nucleic acid-binding protein required for both RNA-directed DNA methylation (RdDM) and pre-mRNA splicing. It promotes RNA polymerase IV (Pol IV)-dependent siRNA accumulation, DNA methylation, and transcriptional silencing. As a pre-mRNA splicing factor, ZOP1 associates with several typical splicing proteins as well as with RNA polymerase II (RNAP II and Pol II). It also shows both RdDM-dependent and -independent roles in transcriptional silencing. ZOP1 contains an N-terminal C2H2-type ZnF domain and an OCtamer REpeat (OCRE) domain that is usually related to RNA processing
SADGAGDWVLDSKSGYYYNAATRYYYDPKTGMYYSDETGKWTTQPPEHAEALKSA
>gnl|CDD|293885 cd16166, OCRE_SUA_like, OCRE domain found in Suppressor of ABI3-5 (SUA) and similar proteins. SUA is an RNA-binding protein located in the nucleus and expressed in all plant tissues. It functions as a splicing factor that influences seed maturation by controlling alternative splicing of ABI3. The suppression of the cryptic ABI3 intron indicates a role of SUA in mRNA processing. SUA also interacts with the prespliceosomal component U2AF65, the larger subunit of the conserved pre-mRNA splicing factor U2AF. SUA contains two RNA recognition motifs surrounding a zinc finger domain, an OCtamer REpeat (OCRE) domain, and a Gly-rich domain close to the C-terminus
KAAPPSGFVYDPASGYYYDASSGYYYDANTGLYYDAASGRWYSYDEETGQYVEV
>gnl|CDD|293886 cd16167, OCRE_RBM10, OCRE domain found in RNA-binding protein 10 (RBM10) and similar proteins. RBM10, also called G patch domain-containing protein 9, or RNA-binding protein S1-1 (S1-1), is a paralogue of putative tumor suppressor RNA-binding protein 5 (RBM5 or LUCA15 or H37). It may play an important role in mRNA generation, processing and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. RBM10 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), an OCtamer REpeat (OCRE) domain, two C2H2-type zinc fingers, and a G-patch/D111 domain
YPVPDVSTYQYDETSGYYYDPQTGLYYDPNSQYYYNAQTQQYLYWDGERRTYVPASEQGADGHK
>gnl|CDD|293887 cd16168, OCRE_RBM5, OCRE domain found in RNA-binding protein 5 (RBM5) and similar proteins. RBM5 is also called protein G15, H37, putative tumor suppressor LUCA15, or renal carcinoma antigen NY-REN-9. It is a known modulator of apoptosis. It acts as a tumor suppressor or an RNA splicing factor. RBM5 shows high sequence similarity to RNA-binding protein 6 (RBM6 or NY-LU-12 or g16 or DEF-3). Both of them specifically binds poly(G) RNA. RBM5 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), an OCtamer REpeat (OCRE) domain, two C2H2-type zinc fingers, a nuclear localization signal, and a G-patch/D111 domain
AVPDTSTYQYDESSGYYYDPITGLYYDPNSQYYYNSLTQQYLYWDGEKQTYLPAAE
>gnl|CDD|320085 cd16169, Tau138_eWH, extended winged-helix domain of tau138 and related proteins. Tau138 is one of three subunits of the tauB subcomplex of yeast transcription factor IIIC. This extended winged-helix domain of tau138 appears to interact with the TPR (tetratricopeptide repeat) array of tauA subunit tau131, and may therefore play a role in linking tauA, tauB, and TFIIIB to regulate the formation of the RNA polymerase III pre-initiation complex
SLRSLRRENEILEVLKELGGVVNLEKKFLEEHEKLLGSLTRMDKKTLKRDLNKLEEEGKLKVITTSVPAV
GDGRSRTVLYLPDPSVEPLDPLLLSLI
>gnl|CDD|320084 cd16170, MvaT_DBD, DNA-binding domain of the bacterial xenogeneic silencer MvaT. MvaT is a xenogeneic silencer conserved in Pseudomonas which assists in distinguishing foreign from self DNA. It prefers binding to flexible DNA segments with multiple TpA steps, and forms nucleoprotein filaments through cooperative polymerization
REVKVYKNPHTGETVETKGGNHKTLKAWKAQYGAETVESWRQ
>gnl|CDD|293781 cd16171, ARSK, arylsulfatase family, member K ....arylsulfatase k short ask flags precursor. ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases
PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNN
YKGLDPNYPTWMDRLEKHGYHTQKYGKLDYTSGHHSVSNRVEAWTRDVPFLLRQEGRPTVNLVGDRSTVR
VMLKDWQNTDKAVHWIRKEAPNLTQPFALYLGLNLPHPYPSPSMGENFGSIRNIRAFYYAMCAETDAMLG
EIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMYEGSSHVPLLIMGPGIKAGQQVSDVVSLVDIY
PTMLDIAGVPQPQNLSGYSLLPLLSESSIKESPSRVPHPDWVLSEFHGCNVNASTYMLRTNSWKYIAYAD
GNSVPPQLFDLSKDPD
>gnl|CDD|293930 cd16172, TorS_sensor_domain, sensor domain of the sensor histidine kinase TorS. TorS is part of the trimethylamine-N-oxide (TMAO) reductase (Tor) pathway, which consists TorT, a periplasmic binding protein that binds TMAO; TorS, a sensor histidine kinase that forms a complex with TorT, and TorR, the response regulator. The Tor pathway is involved in regulating a cellular response to trimethylamine-N-oxide (TMAO), a terminal electron receptor in anaerobic respiration. TorS consists of a periplasmic sensor domain, as well as a HAMP domain, a histidine kinase domain, and a receiver domain
ARQLSELSSRIIASAQLLANADSEAERQQQGRQLTAQLEALLRLLKALGQDSFDSFLLSRLEQTVQEIID
NLAQLGELVGQRLQLRQQFQQLFERLRAAAGELAQLARTQVANASTIAVANVSGLYDLIEQNDKEAAYQA
LDRLIEVDLDLLERMHELRLLALQLGNLINELRTASDIARLAELRQQFNANLAILQRRVQAVEDPGRRAQ
MAQLLSDLEQGQGLFALRRQLLALEQRLQALMQNNLVLFTQLNQTVNALVD
>gnl|CDD|320081 cd16173, EFh_MICU1, EF-hand, calcium binding motif, found in calcium uptake protein 1, mitochondrial (MICU1) and similar proteins. MICU1, also termed atopy-related autoantigen CALC (ara CALC), or calcium-binding atopy-related autoantigen 1 (CBARA1), or Hom s 4, or EFHA3, localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and its paralog, MICU2, are physically associated within the uniporter complex and are co-expressed across all tissues. They may operate together with MCU to regulate the channel. The mutations in MICU1 are associated with neuromuscular abnormalities in children. MICU1 contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices
NFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRSTTGNTLKTGFSSALTTYFFGADLKGKL
TIKNFLEFQRKLQHDVNDVDTALSFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGEL
SNKEFVAIMKQRL
>gnl|CDD|320082 cd16174, EFh_MICU2, EF-hand, calcium binding motif, found in calcium uptake protein 2, mitochondrial (MICU2) and similar proteins. MICU2, also termed EF-hand domain-containing family member A1 (EFHA1), is a mitochondrial-localized paralog of MICU1. MICU2 and its paralog, MICU1, are physically associated within the mitochondrial calcium uniporter (MCU) complex and are co-expressed across all tissues. They may operate together with MCU to regulate the channel. At present, the precise molecular function of MICU2 remains unclear. It may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU2 contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices
GFHIAFKMLDTDGNEQVEKREFFKLQKIIGKKDDLMTQGGTETYQEASDNSDEVNTTLQVHFFGKDGNEK
LQYKEFCRFMENLQTEVEDFAIAMKMFSEANRPIKLAEFKRAVKVATGQELSDNVLDTVFKIFDLDGDDC
LSHGEFLGVLKNRV
>gnl|CDD|320083 cd16175, EFh_MICU3, EF-hand, calcium binding motif, found in calcium uptake protein 3, mitochondrial (MICU3) and similar proteins. MICU3, also termed EF-hand domain-containing family member A2 (EFHA2), is a paralog of MICU1 and notably found in the central nervous system (CNS) and skeletal muscle. At present, the precise molecular function of MICU3 remains unclear. It likely has a role in mitochondrial calcium handling. MICU3 contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices
GFRIAFNMFDTDGNEMVDKKEFLVLQEIFRTLLVHFFGKKGKAELNFEDFYRFMDNLQTEVEDFTIAMRM
YTFADRSISQDEFARAVKVCTGLKLSPHLVNTVFKIFDVDGDGQLSYKEFIGIMKDRL
>gnl|CDD|320076 cd16176, EFh_HEF_CB, EF-hand, calcium binding motif, found in calbindin (CB). CB, also termed calbindin D28, or D-28K, or avian-type vitamin D-dependent calcium-binding protein, is a unique intracellular calcium binding protein that functions as both a calcium sensor and buffer in eukaryotic cells, which undergoes a conformational change upon calcium binding and protects cells against insults of high intracellular calcium concentration. CB is highly expressed in brain and sensory neurons. It plays essential roles in neural functioning, altering synaptic interactions in the hippocampus, modulating calcium channel activity, calcium transients, and intrinsic neuronal firing activity. It prevents a neuronal death, as well as maintains and controls calcium homeostasis. CB also modulates the activity of proteins participating in the development of neurodegenerative disorders such as Alzheimer's disease, Huntington's disease, and bipolar disorder. Moreover, CB interacts with Ran-binding protein M, a protein known to involve in microtubule function. It also interacts with alkaline phosphatase and myo-inositol monophosphatase, as well as caspase 3, an enzyme that plays an important role in the regulation of apoptosis. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions with high affinity
FLEIWHHYDNDGNGYIEGKELQSFIQELQQARKKAGLELSDQMKAFVDQYGQSTDGKIGIVELAQILPTE
ENFLLFFRQQLKSSEEFMQTWRKYDADHSGFIEADELKSFLKDLLKKANKPFDESKLEEYTHTMLKMFDS
NNDGKLGLTEMARLLPVQENFLLKFQGVKMCGKEFNKIFELYDQDGNGYIDENELDALLKDLCEKNKKDL
DINNISTYKKSIMALSDGGKLYRTELALILCAE
>gnl|CDD|320077 cd16177, EFh_HEF_CR, EF-hand, calcium binding motif, found in calretinin (CR). CR, also termed 29 kDa calbindin, is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t specific neurons of the central and peripheral nervous system. It possibly functions as a calcium buffer, calcium sensor, and apoptosis regulator, which may be implicated in many biological processes, including cell proliferation, differentiation, and cell death. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. CR I-II consists of EF-hand motifs 1 and 2, and CR III-VI consists of EF-hand motifs 3-6. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. Thus, CR has two pairs of cooperative binding sites (I-II and III-IV), which display high affinity calcium-binding sites, and one independent calcium ion-binding site (V), which displays lower affinity binding
FLEIWKHFDADGNGYIEGKELENFFRELERARRGAGVDSKSANFGEKMKEFMQKYDKNADGRIEMAELAQ
ILPTEENFLLCFRQHVGSSSEFMEAWRKYDTDRSGYIEANELKGFLSDLLKKANRPYDEKKLQEYTQTIL
RMFDLNGDGKLGLSEMARLLPVQENFLLKFQGMKLSSEEFNAIFAFYDKDGSGYIDENELDALLKDLYEK
NKKEMDIQQLTNYKKSIMSLSDGGKLYRKELEMVLCSE
>gnl|CDD|320078 cd16178, EFh_HEF_SCGN, EF-hand, calcium binding motif, found in secretagogin (SCGN). SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a calcium sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. It also serves as a calcium buffer in neurons. Thus, SCGN may be linked to the pathogenesis of neurological diseases such as Alzheimer's, and also acts as a serum marker of neuronal damage, or as a tumor biomarker. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. All six EF hand motifs of SCGN in some eukaryotes, including D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, could potentially bind six calcium ions. In contrast, SCGNs from higher eukaryotes have at least one non-functional EF-hand motif due to the mutation(s) or deletions. For instance, the EF1 loop does not coordinate calcium ion due to the key residue asparagine replaced by lysine in SCGNs of many mammalian species. Moreover, the EF2 loop seems to be competent for calcium-binding in most mammalian SCGNs except for human and chimpanzee orthologs
FAEIWQHFDADESGYIEGKELDNFFKDLLKKLGTKDTISADEVQDVKECFMSAYDVTGDGRIQIQELANI
ILPDDENFLLFFRREEPLDSSVEFMRIWRKYDADSSGYISAAELKNFLRDLFLQHKKVITEDKLDEYTDT
MMKIFDKNKDGRLDLNDMARILALQENFLLQFKMDAMSEEERKRDFEKIFAHYDVSKTGALEGPEVDGFV
KDMMELVKPSISGVQLDKFKEIILNHCDVNKDGKIQKSELALCLGLK
>gnl|CDD|320079 cd16179, EFh_HEF_CBN, EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and similar proteins. CBN, the product of the cbn gene, is a Drosophila homolog to vertebrate neuronal six EF-hand calcium binding proteins. It is expressed through most of ontogenesis with a selective distribution in the nervous system and in a few small adult thoracic muscles. Its precise biological role remains unclear. CBN contains six EF-hand motifs, but some of them may not bind calcium ions due to the lack of key residues
FMDVWNHYDTDGNGYIEGTELDGFLREFVSSVNPEDVGPEVVSETALEELKEEFMEAYDENQDGRIDIRE
LAQLLPTEENFLLLFRRDNPLDSSVEFMKVWREYDKDNSGYIEADELKNFLKHLLKEAKRDNDVSEDKLI
EYTDTILQLFDRNKDGKLQLSEMARLLPVKENFLCRPIFKGAGKLTREDIDRVFALYDRDNNGTIENEEL
TGFLKDLLELVQEDYDEQDLEEFKEIILRGWDFNNDGKISRKELTMLLLQL
>gnl|CDD|320055 cd16180, EFh_PEF_Group_I, Penta-EF hand, calcium binding motifs, found in Group I PEF proteins. The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+
ELRRIFQAVDRDRSGRISAKELQRALSNGDWTPFSIETVRLMINMFDRDRSGTINFDEFVGLWKYIQDWR
RLFRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFVEACVTLKRLTDAFR
KYDTNRTGYATISYEDFLTMVLSI
>gnl|CDD|320056 cd16181, EFh_PEF_Group_II_sorcin_like, Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins. The family corresponds to the second group of penta-EF hand (PEF) proteins that includes sorcin, grancalcin, and similar proteins. Sorcin, also termed 22 kDa Ca2+-binding protein, CP-22, or V19, is a soluble resistance-related calcium-binding protein that is expressed in normal mammalian tissues, such as the liver, lungs and heart. It contains a flexible glycine and proline-rich N-terminal extension and five EF-hand motifs that associate with membranes in a calcium-dependent manner. It may harbor three potential Ca2+ binding sites through its EF1, EF2 and EF3 hands. However, binding of only two Ca2+/monomer suffices to trigger the conformational change that exposes hydrophobic regions and leads to interaction with the respective targets. Sorcin forms homodimers through the association of the unpaired EF5 hand. Among the PEF proteins, sorcin is unique in that it contains potential phosphorylation sites by cAMP-dependent protein kinase (PKA), and it can form a tetramer at slightly acid pH values although remaining a stable dimer at neutral pH. Grancalcin (GCA) is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It can strongly interact with sorcin to form a heterodimer and further modulate the function of sorcin. GCA exists as homodimers in solution. It contains five EF-hand motifs attached to an N-terminal region of an approximately 50 residue-long segment rich in glycines and prolines. In contrast with sorcin, GCA binds two Ca2+ ions through its EF1 and EF3 hands
PLYGYFSAVAGQDGQIDADELQRCLTQSGISGNYQPFSLETCRLMIAMLDRDHSGKMGFNEFKELWAALN
QWKTTFMQYDRDRSGTVEPQELQQAIRSFGYNLSPQALNVIVKRYSKNGRITFDDFVACAVRLRALTDRF
RRRDTQQNGTATFQYDDFIQVTMSI
>gnl|CDD|320057 cd16182, EFh_PEF_Group_II_CAPN_like, Penta-EF hand, calcium binding motifs, found in PEF calpain family. The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding
QVRELFEKLAGEDEEIDAVELQKLLNASLLKDMPKFDGFSLETCRSLIALMDTNGSGRLDLEEFKTLWSD
LKKWQAIFKKFDTDRSGTLSSYELRKALESAGFHLSNKVLQALVLRYADSTGRITFEDFVSCLVRLKTAF
ETFSALDKKNEGVIPLTLEEWLLLTLY
>gnl|CDD|320058 cd16183, EFh_PEF_ALG-2, EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination
FLWNVFQRVDKDRSGQISATELQQALSNGTWTPFNPETVRLMIGMFDRDNSGTINFQEFAALWKYITDWQ
NCFRSFDRDNSGNIDKNELKQALTSFGYRLSDQFYDILVRKFDRQGRGTIAFDDFIQCCVVLQTLTDSFR
RYDTDQDGWIQISYEQFLEMVFSNV
>gnl|CDD|320059 cd16184, EFh_PEF_peflin, EF-hand, calcium binding motif, found in peflin and similar proteins. Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation
EVQQWFQAVDRDRSGKISAKELQQALVNGNWSHFNDETCRLMIGMFDKDKSGTIDIYEFQALWNYIQQWK
QVFQQFDRDRSGSIDENELHQALSQMGYRLSPQFVQFLVSKYDPRARRSLTLDQFIQVCVQLQSLTDAFR
QRDTQMTGTITISYEDFLTMALLNK
>gnl|CDD|320060 cd16185, EFh_PEF_ALG-2_like, EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2). The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD)
ELRQWFRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAALHQFLSNMQN
GFEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDYIELCIFLASARNLFQA
FDRQRTGRVTLDFNQFVYAAANL
>gnl|CDD|320061 cd16186, EFh_PEF_grancalcin, Penta-EF hand, calcium binding motifs, found in grancalcin. Grancalcin (GCA) is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It displays a Ca2+-dependent translocation to granules and plasma membrane upon neutrophil activation, suggesting roles in granule-membrane fusion and degranulation of neutrophils. It may also play a role in the regulation of vesicle/granule exocytosis through the reversible binding of secretory vesicles and plasma membranes upon the presence of calcium. Moreover, GCA is involved in inflammation, as well as in the process of adhesion of neutrophils to fibronectin. It plays a key role in leukocyte-specific functions that are responsible for host defense, and affects the function of integrin receptors on immune cells through binding to L-plastin in the absence of calcium. Furthermore, GCA can strongly interact with sorcin to form a heterodimer, and further modulate the function of sorcin. GCA exists as homodimers in solution. It contains five EF-hand motifs attached to an N-terminal region of an approximately 50 residue-long segment rich in glycines and prolines. GCA binds two Ca2+ ions through its EF1 and EF3 hands
PMWGYFSAVAGQDGEVDAEELQRCLTQSGINGTYTPFSLETCRIMIAMLDRDHTGKMGFNEFKELWAALN
AWKQNFMTVDQDRSGTVEPHELRQAIGAMGYRLSPQTLTTIVKRYSKNGRIYFDDYVACCVKLRALTDFF
RRRDHMQQGSVNFIYDDFLQCTMAI
>gnl|CDD|320062 cd16187, EFh_PEF_sorcin, Penta-EF hand, calcium binding motifs, found in sorcin. Sorcin, also termed 22 kDa Ca2+-binding protein, CP-22, or V19, is a soluble resistance-related calcium-binding protein that is expressed in normal mammalian tissues, such as the liver, lungs and heart. The up-regulation of sorcin is correlated with a number of cancer types, including colorectal, gastric and breast cancer. It may represent a therapeutic target for reversing tumor multidrug resistance (MDR). Sorcin participates in the regulation of calcium homeostasis in cells and is necessary for the activation of mitosis and cytokinesis. It enhances metastasis and promotes epithelial-to-mesenchymal transition of colorectal cancer. Moreover, sorcin has been implicated in the regulation of intracellular Ca2+ cycling and cardiac excitation-contraction coupling. It displays the anti-apoptotic properties via the modulation of mitochondrial Ca2+ handling in cardiac myocytes. It can target and activate the sarcolemmal Na+/Ca2+ exchanger (NCX1) in cardiac muscle. Meanwhile, sorcin modulates cardiac L-type Ca2+ current by functional interaction with the alpha1C subunit. It also associates with calcium/calmodulin-dependent protein kinase IIdeltaC (CaMKIIdelta(C)) and further modulates ryanodine receptor (RyR) function in cardiac myocytes. Furthermore, sorcin may act as a Ca2+ sensor for glucose-induced nuclear translocation and the activation of carbohydrate-responsive element-binding protein (ChREBP)-dependent genes. As a mitochondrial chaperone TRAP1 interactor, sorcin involves in mitochondrial metabolism through the TRAP1 pathway. In addition, sorcin may regulate the inhibition of type I interferon response in cells through interacting with foot-and-mouth disease virus (FMDV) VP1. Sorcin contains a flexible glycine and proline-rich N-terminal extension and five EF-hand motifs that associate with membranes in a calcium-dependent manner. It may harbor three potential Ca2+ binding sites through its EF1, EF2 and EF3 hands. However, binding of only two Ca2+/monomer suffices to trigger the conformational change that exposes hydrophobic regions and leads to interaction with the respective targets. Sorcin forms homodimers through the association of the unpaired EF5 hand. Among the PEF proteins, sorcin is unique in that it contains potential phosphorylation sites by cAMP-dependent protein kinase (PKA), and it can form a tetramer at slightly acid pH values although remaining a stable dimer at neutral pH
PLYGYFAAVAGQDGQIDADELQRCLTQSGIAGGYKPFNLETCRLMISMLDRDMSGTMGFNEFKELWAVLN
GWRQHFISFDSDRSGTVDPQELQKALTTMGFRLSPQAVNSIAKRYSTNGKITFDDYIACCVKLRALTDSF
RRRDTSQQGVVNFPYDDFIQCVMSI
>gnl|CDD|320063 cd16188, EFh_PEF_CPNS1_2, Penta-EF hand, calcium binding motifs, found in calcium-dependent protease small subunit CAPNS1 and CAPNS2. CAPNS1, also termed calpain small subunit 1 (CSS1), or calcium-activated neutral proteinase small subunit (CANP small subunit), or calcium-dependent protease small subunit (CDPS), or calpain regulatory subunit, is a common 28-kDa regulatory calpain subunit encoded by the calpain small 1 (Capns1, also known as Capn4) gene. It acts as a binding partner to form a heterodimer with the 80 kDa calpain large catalytic subunit and is required in maintaining the activity of calpain. CAPNS1 plays a significant role in tumor progression of human cancer, and functions as a potential therapeutic target in human hepatocellular carcinoma (HCC), nasopharyngeal carcinoma (NPC), glioma, and clear cell renal cell carcinoma (ccRCC). It may be involved in regulating migration and cell survival through binding to the SH3 domain of Ras GTPase-activating protein (RasGAP). It may also modulate Akt/FoxO3A signaling and apoptosis through PP2A. CAPNS1 contains an N-terminal glycine rich domain and a C-terminal PEF-hand domain. CAPNS2, also termed calpain small subunit 2 (CSS2), is a novel tissue-specific 30 kDa calpain small subunit that lacks two oligo-Gly stretches characteristic of the N-terminal Gly-rich domain of CAPNS1. CAPNS2 acts as a chaperone for the calpain large subunit, and appears to be the functional equivalent of CAPNS1. However, CAPNS2 binds the large subunit much more weakly than CAPNS1 and it does not undergo the autolytic conversion typical of CAPNS1
QFRRLFVQLAGDDMEVSATELMNILNKVVTRHPDLKTDGFGIDTCRSMVAVMDSDTTGKLGFEEFKYLWN
NIKKWQGIYKQFDTDRSGTIGSQELPGAFEAAGFHLNEQLYQMIIRRYSDEDGNMDFDNFISCLVRLDAM
FRAFKSLDKDGTGQIQVNIQEWLQLTMYS
>gnl|CDD|320064 cd16189, EFh_PEF_CAPN1_like, Penta-EF hand, calcium binding motifs, found in mu-type calpain (CAPN1), m-type calpain (CAPN2), and similar proteins. The family includes mu-type calpain (CAPN1) and m-type calpain (CAPN2), both of which are ubiquitously expressed 80-kDa Ca2+-dependent intracellular cysteine proteases that contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The catalytic subunit CAPN1 or CAPN2 in complex with a regulatory subunit encoded by CAPNS1 forms a mu- or m-calpain heterodimer, respectively
NFRNLFTQLAGEDSEISAFELQTILNKVLSKRKDIKTDGFSLETCRNMVNLLDKDGSGKLGLVEFQILWT
KIQKYLKIYKKFDTDGSGTMSSYEMRLALEEAGFKLNNQLHQVLVARYADQELTIDFDNFVRCLVRLELL
FKIFKQLDKDNTGTIELDLIQWLSFSLL
>gnl|CDD|320065 cd16190, EFh_PEF_CAPN3, Calcium-activated neutral. CAPN3, also termed calcium-activated neutral proteinase 3 (CANP 3), or calpain L3, or calpain p94, or muscle-specific calcium-activated neutral protease 3, or new calpain 1 (nCL-1), is a calpain large subunit that is mainly expressed in skeletal muscle, or lens. The skeletal muscle-specific CAPN3 are pathologically associated with limb girdle muscular dystrophy type 2A (LGMD2A). Its autolytic activity can be positively regulated by calmodulin (CaM), a known transducer of the calcium signal. CAPN3 is also involved in human melanoma tumorigenesis and progression. It impairs cell proliferation and stimulates oxidative stress-mediated cell death in melanoma cells. Moreover, it plays an important role in sarcomere remodeling and mitochondrial protein turnover. Furthermore, the phosphorylated skeletal muscle-specific CAPN3 acts as a myofibril structural component and may participate in myofibril-based signaling pathways. In the eye, the lens-specific CAPN3, together with CAPN2, is responsible for proteolytic cleavages of alpha and beta-crystallin. Overactivated alpha and beta-crystallin can lead to cataract formation. CAPN3 exists as a homodimer, rather than a heterodimer with the calpain small subunit. It may also form heterodimers with other calpain large subunits. CAPN3 contains a long N-terminal region, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. Ca2+ binding at EF5 of the CAPN3 PEF domain is a distinct feature not observed in other calpain isoforms
QFRNIFQQIAGDDMEISADELRSVLNRVVKKHKDLKTEGFTLESCRSMIALMDTDGSGKLNLQEFRHLWN
KIKQWQKIFKRYDTDKSGTINSYEMRNAVNDAGFRLNNQLYDIITMRYADKHMNIDFDSFICCFVRLEGM
FRAFHAFDKDGDGIIKLNVLEWLQLTMYA
>gnl|CDD|320066 cd16191, EFh_PEF_CAPN8, Penta-EF hand, calcium binding motifs, found in calpain-8 (CAPN8). CAPN8, also termed new calpain 2 (nCL-2), or stomach-specific M-type calpain, is a calpain large subunit predominantly expressed in the stomach. It appears to be involved in membrane trafficking in the gastric surface mucus cells (pit cells), via its location at the Golgi and interaction with the beta-subunit of coatomer complex (beta-COP) of vesicles derived from the Golgi. Moreover, CAPN8, together with CAPN9, forms an active protease complex, G-calpain, in which both proteins are essential for stability and activity. The G-Calpain has been implicated in gastric mucosal defense. CAPN8 exists as both a monomer and homo-oligomer, but not as a heterodimer with the conventional calpain regulatory subunit (30K). The monomer and homodimer forms predominate. CAPN8 contains a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain
EFKNIFQKLAGKKCEVTANELQTILNRVLSKRKDIKSDGFTINTCREMISLLDTDGTGTLGLVEFRILWM
KIQKYLAIYKKVDSDRSGTIDAHEMRNALQEAGFTLNNKIQQSIVQRYASNKLTINFDGFIACMIRLETL
FKMFQLLDKDKSGVVQLSLAEWLCCTLV
>gnl|CDD|320067 cd16192, EFh_PEF_CAPN9, Penta-EF hand, calcium binding motifs, found in calpain-9 (CAPN9). CAPN9, also termed digestive tract-specific calpain, or new calpain 4 (nCL-4), or protein CG36, is a calpain large subunit predominantly expressed in gastrointestinal tract. It plays a physiological role in the suppression of tumorigenesis. It acts as an important biomolecule link for the regression of colorectal cancer via intracellular calcium homeostasis. CAPN9 may also play a critical role in lumen formation. Moreover, CAPN9, together with CAPN8, forms an active protease complex, G-calpain, in which both proteins are essential for stability and activity. The G-Calpain has been implicated in gastric mucosal defense. Furthermore, down-regulation of calpain 9 has been linked to hypertensive heart and kidney disease in salt-sensitive Dahl rats. CAPN9 contains a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain
QFRKLFEQISGEDLEISAEELQYVLNAVLARTKEIKFKKLSLLSCKNIISLMDTSGNGKLGFSEFKVFWD
KLKKWIGLFLKYDADRSGTMSSYELRSALKAAGFQLNNQLLQLIVLRYADDYLQIDFDDFLNCLVRLENS
FRVFQALDTKNTGEISLNMLEFILLTMNI
>gnl|CDD|320068 cd16193, EFh_PEF_CAPN11, Penta-EF hand, calcium binding motifs, found in calpain-11 (CAPN11). CAPN11, also termed calcium-activated neutral proteinase 11 (CANP 11), is a mammalian orthologue of micro/m calpain. It is one of the calpain large subunits that appears to be exclusively expressed in certain cells of the testis. It may be involved in regulating calcium-dependent signal transduction events during meiosis and sperm functional processes. CAPN11 contains a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain
DSLHLFKIVANEDKEVDMYELQKLLNRMAIKFKSFKTKGFSLDVCRRMINLMDKDGSGKLGLHEFKILWK
KIKKWMEIFKECDQDRSGNLNSYEMRLAIEKAGIKMNNRVTEVVVARYADDNMIVDFDSFINCFLRLKAM
FAFFLSMDTKKTGSICLSINQWLQITMWG
>gnl|CDD|320069 cd16194, EFh_PEF_CAPN12, Penta-EF hand, calcium binding motifs, found in calpain-12 (CAPN12). CAPN12, also termed calcium-activated neutral proteinase 12 (CANP 12), is a calpain large subunit mainly expressed in the cortex of the hair follicle. It may affect apoptosis regulation. CAPN12 contains a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain
ELEQLFQELAGEDEEINASELQKILSIALERAHTSKPREFGLRTCRQLIQCFDHGQNGKLALEEFQQLWG
YLLEWQAIFTKFDEDTSGTMDSYELRLALNAAGFHLNNQLTETLTSRYRDSRLRVDFESFLSCLAHLTCI
FCQCSQHDDGGEGVICLTHRQWLELATFS
>gnl|CDD|320070 cd16195, EFh_PEF_CAPN13_14, Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and similar proteins. CAPN13, also termed calcium-activated neutral proteinase 13 (CANP 13), a 63.6 kDa calpain large subunit that exhibits a restricted tissue distribution with low levels of expression detected only in human testis and lung. In calpain family, CAPN13 is most closely related to calpain-14 (CAPN14). CAPN14, also termed calcium-activated neutral proteinase 14 (CANP 14), is a 76.7 kDa calpain large subunit that is most highly expressed in the oesophagus. Its expression and calpain activity can be induced by IL-13. Both CAPN13 and CAPN14 contain a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain
SSRALFLKYADQGGELDAEQLQKLLNENLLKGLAGSGGGFSLDACRSMVALMDLSVNGRLSLEEFSRLWK
KLRKYKDIFQKADVSKSGFLSLSELRNAIQAAGIRVSDDLLNLMALRYGDSSGRISFESFICLMLRLECM
AKIFRNLSKDGGGIYLTESEWMQLTMYS
>gnl|CDD|320071 cd16196, EFh_PEF_CalpA_B, Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), calpain-B (CalpB), and similar proteins. The family contains two calpains that have been found in Drosophila, CalpA and CalpB. CalpA, also termed calcium-activated neutral proteinase A (CANP A), or calpain-A catalytic subunit, is a Drosophila calpain homolog specifically expressed in a few neurons in the central nervous system, in scattered endocrine cells in the midgut, and in blood cells. CalpB, also termed calcium-activated neutral proteinase B (CANP B), contains calpain-B catalytic subunit 1 and calpain-B catalytic subunit 2. Both CalpA and CalpB are closely related to that of vertebrate calpains, and they share similar domain architecture, which consists of four domains: the N-terminal domain I, the catalytic domain II carrying the three active site residues, Cys, His and Asn, the Ca2+-regulated phospholipid-binding domain III, and penta-EF-hand Ca2+-binding domain IV. Besides, CalpA and CalpB display some distinguishing structural features that are not found in mammalian typical calpains. CalpA harbors a 76 amino acid long hydrophobic stretch inserted in domain IV, which may be involved in membrane attachment of this enzyme. CalpB has an unusually long N-terminal tail of 224 amino acids, which belongs to the class of intrinsically unstructured proteins (IUP) and may become ordered upon binding to target protein(s). Moreover, they do not need small regulatory subunits for their catalytic activity, and their proteolytic function is not regulated by an intrinsic inhibitor as the Drosophila genome contains neither regulatory subunit nor calpastatin orthologs. As a result, they may exist as a monomer or perhaps as a homo- or heterodimer together with a second large subunit. Furthermore, both CalpA and CalpB are dispensable for viability and fertility and do not share vital functions during Drosophila development. Phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol, and phosphatidic acid can stimulate the activity and the rate of activation of CalpA, but not CalpB. Calpain A modulates Toll responses by limited Cactus/IkappaB proteolysis. CalpB directly interacts with talin, an important component of the focal adhesion complex, and functions as an important modulator in border cell migration within egg chambers, which may act via the digestion of talin. CalpB can be phosphorylated by cAMP-dependent protein kinase (protein kinase A, PKA; EC 2.7.11.11) at Ser240 and Ser845, as well as by mitogen-activated protein kinase (ERK1 and ERK2; EC 2.7.11.24) at Thr747. The activation of the ERK pathway by extracellular signals results in the phosphorylation and activation of calpain B. In Schneider cells (S2), calpain B was mainly in the cytoplasm and upon a rise in Ca2+ the enzyme adhered to intracellular membranes
RLRRLFDKIAGEDMEIDAYELQDILNTAFKKDFPFDGFSLDACRSMVAMMDVDRSGKLGFEEFKKLWEDL
RSWKRVFKLFDTDGSGSFSSFELRNALNSAGFRLSNATLNALVLRYSNKDGRISFDDFIMCAVKLKTMFE
IFKEKDPRGGGRATFNLDEFLESTMYS
>gnl|CDD|320072 cd16197, EFh_PEF_CalpC, Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-C (CalpC) and similar proteins. CalpC, also termed calcium-activated neutral proteinase homolog C (CANP C), is a catalytically inactive homolog of CalpA and CalpB found in Drosophila. It is strongly expressed in the salivary glands. In contrast with CalpA and CalpB, both of which are closely related to that of vertebrate calpains, and they share similar domain architecture, which consists of four domains: the N-terminal domain I, the catalytic domain II carrying the three active site residues, Cys, His and Asn, the Ca2+-regulated phospholipid-binding domain III, and penta-EF-hand Ca2+-binding domain IV. CalpC is a truncated calpain form missing domain I and about 20 residues from domain II. Moreover, due to all three mutated active site residues (Cys to Arg, His to Val and Asn to Ser), it may not have proteolytic activity
QYEPVFLQLADEHRTVNAFELQELLEACLPNDYIKSCANIDVCRQVVLLMDNSGLGRLKFQDFKDFMCSL
KWWQGVFKMHTKEKTGILRAERLRDALEDVGFQLNTDVLSILILRYMRKDGTLRFGDFVSAVLHLTAAFG
SFEKKDPLQNGFIKLSLTEWLKSCLM
>gnl|CDD|320073 cd16198, EFh_PEF_CAPN1, Penta-EF hand, calcium binding motifs, found in mu-type calpain (CAPN1). CAPN1, also termed calpain-1 80-kDa catalytic subunit, or calpain-1 large subunit, or micromolar-calpain (muCANP), or calcium-activated neutral proteinase 1 (CANP 1), or cell proliferation-inducing gene 30 protein, is a ubiquitously expressed 80-kDa Ca2+-dependent intracellular cysteine protease that contains a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The catalytic subunit CAPN1 in complex with a regulatory subunit encoded by CAPNS1 forms a mu-calpain heterodimer. CAPN1 plays a central role in postmortem proteolysis and meat tenderization processes, as well as in regulation of proliferation and survival of skeletal satellite cells. It also acts as a novel regulator in IgE-mediated mast cell activation and could serve as a potential therapeutic target for the management of allergic inflammation. Moreover, CAPN1 is involved in neutrophil motility and functions as a potential target for intervention in inflammatory disease. It also facilitates age-associated aortic wall calcification and fibrosis through the regulation of matrix metalloproteinase 2 activity in vascular smooth muscle cells, and thus plays a role in hypertension and atherosclerosis. The proteolytic cleavage of beta-amyloid precursor protein and tau protein by CAPN1 may be involved in plaque formation. Furthermore, CAPN1 is activated in the brains of individuals with Alzheimer's disease. It is involved in the maintenance of a proliferative neural stem cell pool. The activation and macrophage inflammation of CAPN1 in hypercholesterolemic nephropathy is promoted by nicotinic acetylcholine receptor alpha1 (nAChRalpha1). In addition, CAPN1 displays a functional role in hemostasis, as well as in sickle cell disease
NFKNLFRQLAGEDMEISVFELKTILNRIISKHKDLRTDGFSLESCRSMVNLMDKDGNGKLGLVEFNILWN
KIRNYLTIFRKFDLDKSGSMSAYEMRLALESAGFKLNNRLHQVIVARYADPNLAIDFDNFVCCLVRLETM
FRFFKQLDTEETGTIEMDLFEWLQLTMFG
>gnl|CDD|320074 cd16199, EFh_PEF_CAPN2, Penta-EF hand, calcium binding motifs, found in m-type calpain (CAPN2). CAPN2, also termed millimolar-calpain (m-calpain), or calpain-2 catalytic subunit, or calcium-activated neutral proteinase 2 (CANP 2), or calpain large polypeptide L2, or calpain-2 large subunit, is a ubiquitously expressed 80-kDa Ca2+-dependent intracellular cysteine protease that contains a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The catalytic subunit CAPN2 in complex with a regulatory subunit encoded by CAPNS1 forms an m-calpain heterodimer. CAPN2 acts as the key protease responsible for N-methyl-d-aspartic acid (NMDA)-induced cytoplasmic polyadenylation element-binding protein 3 (CPEB3) degradation in neurons. It cleaves several components of the focal adhesion complex, such as FAK and talin, triggering disassembly of the complex at the rear of the cell. The stimulation of CAPN2 activity is required for Golgi antiapoptotic proteins (GAAPs) to promote cleavage of FA kinase (FAK), cell spreading, and enhanced migration. calpain 2 is also involved in the onset of glial differentiation. It regulates proliferation, survival, migration, and tumorigenesis of breast cancer cells through a PP2A-Akt-FoxO-p27(Kip1) signaling cascade. Its expression is associated with response to platinum based chemotherapy, progression-free and overall survival in ovarian cancer. Moreover, CAPN2 may play a role in fundamental mitotic functions, such as the maintenance of sister chromatid cohesion. The activation of CAPN2 plays an essential role in hippocampal synaptic plasticity and in learning and memory. In the eye, CAPN2, together with a lens-specific variant of CAPN3, is responsible for proteolytic cleavages of alpha and beta-crystallin. Overactivated alpha and beta-crystallin can lead to cataract formation. Sometimes, CAPN2 compensates for loss of CAPN1, and both calpain isoforms are involved in AngII-induced aortic aneurysm formation. The main phosphorylation sites in m-calpain are Ser50 and Ser369/Thr370
GFRRLFAQLAGEDAEISAFELQTILRRVLAKREDIKSDGFSIETCKIMVDMLDSDGSGKLGLKEFYILWT
KIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKLPCQLHQVIVARFADDDLIIDFDNFVRCLVRLETL
FKIFKQLDPENTGTIELDLISWLSFSVL
>gnl|CDD|320030 cd16200, EFh_PI-PLCbeta, EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta isozymes. PI-PLC-beta isozymes represent a class of metazoan PI-PLCs that hydrolyze the membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2) to propagate diverse intracellular responses that underlie the physiological action of many hormones, neurotransmitters, and growth factors (EC 3.1.4.11). They have been implicated in numerous processes relevant to central nervous system (CNS), including chemotaxis, cardiovascular function, neuronal signaling, and opioid sensitivity. Like other PI-PLC isozymes, PI-PLC-beta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, they have a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are four PI-PLC-beta isozymes (1-4). PI-PLC-beta1 and PI-PLC-beta3 are expressed in a wide range of tissues and cell types, whereas PI-PLC-beta2 and PI-PLC-beta4 have been found only in hematopoietic and neuronal tissues, respectively. All PI-PLC-beta isozymes are activated by the heterotrimeric G protein alpha subunits of the Gq class through their C2 domain and long C-terminal extension. They are GTPase-activating proteins (GAPs) for these G alpha(q) proteins. PI-PLC-beta2 and PI-PLC-beta3 can also be activated by beta-gamma subunits of the G alpha(i/o) family of heterotrimeric G proteins and the small GTPases such as Rac and Cdc42. This family also includes two invertebrate homologs of PI-PLC-beta, PLC21 from cephalopod retina and No receptor potential A protein (NorpA) from Drosophila melanogaster
KKLYTKLKLSVNITGKIPVKNIIKCFSSDKKRKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLC
PRPDIDEIFKELGGKRKPYLTLEQLVDFLNEEQRDPRLNEILFPFHTKEQAKKLIDKYEPNEKNKKKGQL
TLEGFLRYLMSDE
>gnl|CDD|320031 cd16201, EFh_PI-PLCgamma, EF-hand motif found in phosphoinositide phospholipase C gamma isozymes (PI-PLC-gamma). PI-PLC-gamma isozymes represent a class of metazoan PI-PLCs that hydrolyze the membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2) to propagate diverse intracellular responses that underlie the physiological action of many hormones, neurotransmitters, and growth factors. They can form a complex with the phosphorylated cytoplasmic domains of the immunoglobulin Ig-alpha and Ig-beta subunits of the B cell receptor (BCR), the membrane-tethered Src family kinase Lyn, phosphorylated spleen tyrosine kinase (Syk), the phosphorylated adaptor protein B-cell linker (BLNK), and activated Bruton's tyrosine kinase (Btk). Like other PI-PLC isozymes, PI-PLC-gamma isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unique to PI-PLC-gamma, a second PH domain, which is split by two SH2 (Src homology 2) domains, and one SH3 (Src homology 3) domain, are present within this linker. The SH2 and SH3 domains are responsible for the binding of phosphotyrosine-containing sequences and proline-rich sequences, respectively. There are two PI-PLC-gamma isozymes (1-2), both of which are activated by receptor and non-receptor tyrosine kinases due to the presence of SH2 and SH3 domains
WLRKEFYSMDRTRRETVTLKDLKAFLPRVNCKISTNKLREKFQEVDTRRRGELGFDDFAQLYHKLMFDQK
IIEDFFKKYSYSSDGQTVTLEDFQRFLLEEQKEPWANDPNAVREFMRDFLQDPLRDVQEPYFTLDEFLDY
LFSKE
>gnl|CDD|320032 cd16202, EFh_PI-PLCdelta, EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta). PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants
WLKDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQFYNRLTKRPE
IEELFKKYSGDDEALTVEELRRFLQEEQKVKDVTLEWAEQLIETYEPSEDLKAQGLMSLDGFTLFLLSPD
>gnl|CDD|320033 cd16203, EFh_PI-PLCepsilon, EF-hand motif found in phosphoinositide phospholipase C epsilon 1 (PI-PLC-epsilon1). PI-PLC-epsilon1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1, or pancreas-enriched phospholipase C, or phospholipase C-epsilon-1 (PLC-epsilon-1), is dominant in connective tissues and brain. It has been implicated in carcinogenesis, such as in bladder and intestinal tumor, oesophageal squamous cell carcinoma, gastric adenocarcinoma, murine skin cancer, head and neck cancer. PI-PLC-epsilon1 contains an N-terminal CDC25 homology domain with a guanyl-nucleotide exchange factor (GFF) activity, a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and at least one and perhaps two C-terminal predicted RA (Ras association) domains that are implicated in the binding of small GTPases, such as Ras or Rap, from the Ras family. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There is only one PI-PLC-epsilon isozyme. It is directly activated by G alpha(12/13), G beta gamma, and activated members of Ras and Rho small GTPases
GGLKGFSIGEVQDTQLTFVEFVELFKSFSLRMRKDLKDLFDQFAVPYSRSGSNAAPLKRSLSISESYSGL
FPDLDLLTRNTSLDGLFISKKQQKKIYDAIAAASIVTNGAGVDSSRSSVLTISQLKDFLENHQMEHITEE
EAIKIIQRHEPDPILRSKNCLSFEGFARYLMDKD
>gnl|CDD|320034 cd16204, EFh_PI-PLCzeta, EF-hand motif found in phosphoinositide phospholipase C zeta 1 (PI-PLC-zeta1). PI-PLC-zeta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1, or phospholipase C-zeta-1 (PLC-zeta-1), or testis-development protein NYD-SP27, is only found in the testis. The sperm-specific PI-PLC plays a fundamental role in vertebrate fertilization by initiating intracellular calcium oscillations that trigger the embryo development. However, the mechanism of its activation still remains unclear. PI-PLC-zeta1 contains an N-terminal four atypical EF-hand motifs, a PLC catalytic core domain, and a C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unlike other PI-PLCs, PI-PLC-zeta is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. There is only one PLC-zeta isozyme. Aside from PI-PLC-zeta identified in mammals, its eukaryotic homologs have been classified with this family
MENRWFLSIIQDRFRKGKINLESTLKLLEKLDIPFDYIHVKYIFKKNDSFKAGNITIEDFRAIYRAIAHR
CEIHEIFNTYSENRKILSAPNLVGFLKKEQFQDEADETIASELIAKYEPIEEVRKRKQMSFEGFIRYMTS
ED
>gnl|CDD|320035 cd16205, EFh_PI-PLCeta, EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta). PI-PLC-eta isozymes represent a class of neuron-specific metazoan PI-PLCs that are most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. They are phosphatidylinositol 4,5-bisphosphate-hydrolyzing enzymes that are more sensitive to Ca2+ than other PI-PLC isozymes. They function as calcium sensors activated by small increases in intracellular calcium concentrations. They are also activated through G-protein-coupled receptor (GPCR) stimulation, and further mediate GPCR signalling pathways. PI-PLC-eta isozymes contain an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases. There are two PI-PLC-eta isozymes (1-2). Aside from the PI-PLC-eta isozymes identified in mammals, their eukaryotic homologs are also present in this family
WLKQTFEEADKNGDGLLSIGEILQLMHKLNVNLPRRKVRQMFKEADTDDNQGTLDFEEFCAFYKMMSTRR
ELYLLLLSYSNKKDYLTLEDLARFLEVEQKMTNVTLEYCLDIIEKFEPSEENKKNGLLGIDGFTNYMRSP
A
>gnl|CDD|320036 cd16206, EFh_PRIP, EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP). This family represents a class of metazoan phospholipase C related, but catalytically inactive proteins (PRIP), which belong to a group of novel inositol 1,4,5-trisphosphate (InsP3) binding protein. PRIP has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP do not have PLC enzymatic activity. PRIP consists of two subfamilies, PRIP-1(also known as p130 or PLC-L1), which is predominantly expressed in the brain, and PRIP-2 (also known as PLC-L2), which exhibits a relatively ubiquitous expression. Experiments show both, PRIP-1 and PRIP-2, are involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. In addition, PRIP-2 acts as a negative regulator of B-cell receptor signaling and immune responses
WLESVFEEADTNKSGFLDEEEAVQLIKQLNPGLSTSRIKQKLKELQKKKDGARGRVSSDEFVELFKELAT
RPEIYFLLVRYASNKDYLTVDDLMLFLEAEQGMTGVTKEKCLEIINKYEPSEEGREKGQLGIDGFTRYLL
SEE
>gnl|CDD|320037 cd16207, EFh_ScPlc1p_like, EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar proteins. This family represents a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this family is protein Plc1p (also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1) encoded by PLC1 genes from Saccharomyces cerevisiae. ScPlc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that ScPlc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like SCPlc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily
LRIHWKRADSKKQDGDERLDFEDVEKLCRRLHINCSESYLRELFDKADTDKKGYLNFEEFQEFVKLLKRR
KDIKAIFKQLTKPGSDGLTLEEFLKFLRDVQKEDVDRETWEKIFEKFARRIDDSDSLTMTLEGFTSFLLS
SY
>gnl|CDD|320038 cd16208, EFh_PI-PLCbeta1, EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1). PI-PLC-beta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1, or PLC-154, or phospholipase C-I (PLC-I), or phospholipase C-beta-1 (PLC-beta1), is expressed at highest levels in specific regions of the brain, as well as in the cardiovascular system. It has two splice variants, PI-PLC-beta1a and PI-PLC-beta1b, both of which are present within the nucleus. Nuclear PI-PLC-beta1 is a key molecule for nuclear inositide signaling, where it plays a role in cell cycle progression, proliferation and differentiation. It also contributes to generate cell-specific Ca2+ signals evoked by G protein-coupled receptor stimulation. PI-PLC-beta1 acts as an effector and a GTPase activating protein (GAP) specifically activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It regulates neuronal activity in the cerebral cortex and hippocampus, and has been implicated for participations in diverse critical functions related to forebrain diseases such as schizophrenia. It may play an important role in maintenance of the status epilepticus, and in osteosarcoma-related signal transduction pathways. PI-PLC-beta1 also functions as a regulator of erythropoiesis in kinamycin F, a potent inducer of gamma-globin production in K562 cells. The G protein activation and the degradation of PI-PLC-beta1 can be regulated by the interaction of alpha-synuclein. As a result, it may reduce cell damage under oxidative stress. Moreover, PI-PLC-beta1 works as a new intermediate in the HIV-1 gp120-triggered phosphatidylcholine-specific phospholipase C (PC-PLC)-driven signal transduction pathway leading to cytoplasmic CCL2 secretion in macrophages. PI-PLC-beta1 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence
EKAYTKLKLQVNPEGRIPVKNIYRLFSADRKRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPR
PEIDHIFSEFGAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISV
DGFMRYLSGEE
>gnl|CDD|320039 cd16209, EFh_PI-PLCbeta2, EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2). PI-PLC-beta2, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2, or phospholipase C-beta-2 (PLC-beta2), is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits (G alpha(q)) through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins. PI-PLC-beta2 has two cellular binding partners, alpha- and gamma-synuclein. The binding of either alpha- and gamma-synuclein inhibits PI-PLC-beta2 activity through preventing the binding of its activator G alpha(q). However, the binding of gamma-synuclein to PI-PLC-beta2 does not affect its binding to G beta(gamma) subunits or small G proteins, but enhances these signals. Meanwhile, gamma-synuclein may protect PI-PLC-beta2 from protease degradation and contribute to its over-expression in breast cancer. In leukocytes, the G beta(gamma)-mediated activation of PI-PLC-beta2 can be promoted by a scaffolding protein WDR26, which is also required for the translocation of PI-PLC-beta2 from the cytosol to the membrane in polarized leukocytes. PI-PLC-beta2 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence
EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPR
PEIDEIFTSYHAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSP
EGMVWFLCGPE
>gnl|CDD|320040 cd16210, EFh_PI-PLCbeta3, EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3). PI-PLC-beta3, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3, or phospholipase C-beta-3 (PLC-beta3), is widely expressed at highest levels in brain, liver, and parotid gland. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins. PI-PLC-beta3 associates with CXC chemokine receptor 2 (CXCR2) and Na+/H+ exchanger regulatory factor-1 (NHERF1) to form macromolecular complexes at the plasma membrane of pancreatic cancer cells, which functionally couple chemokine signaling to PI-PLC-beta3-mediated signaling cascade. Moreover, PI-PLC-beta3 directly interacts with the M3 muscarinic receptor (M3R), a prototypical G alpha-q-coupled receptor that promotes PI-PLC-beta3 localization to the plasma membrane. This binding can alter G alpha-q-dependent PLC activation. Furthermore, PI-PLC-beta3 inhibits the proliferation of hematopoietic stem cells (HSCs) and myeloid cells through the interaction of SH2-domain-containing protein phosphatase 1 (SHP-1) and signal transducer and activator of transcription 5 (Stat5), and the augment of the dephosphorylating activity of SHP-1 toward Stat5, leading to the inactivation of Stat5. It is also involved in atopic dermatitis (AD) pathogenesis via regulating the expression of periostin in fibroblasts and thymic stromal lymphopoietin (TSLP) in keratinocytes. In addition, PI-PLC-beta3 mediates the thrombin-induced Ca2+ response in glial cells. PI-PLC-beta3 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence
RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLR
PDIDKILLEIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSM
EGFSRYLGGEE
>gnl|CDD|320041 cd16211, EFh_PI-PLCbeta4, EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4). PI-PLC-beta4, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4, or phospholipase C-beta-4 (PLC-beta4), is expressed in high concentrations in cerebellar Purkinje and granule cells, the median geniculate body, and the lateral geniculate nucleus. It may play a critical role in linking anxiety behaviors and theta rhythm heterogeneity. PI-PLC-beta4 is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It contributes to generate cell-specific Ca2+ signals evoked by G protein-coupled receptor stimulation. PI-PLC-beta4 functions as a downstream signaling molecule of type 1 metabotropic glutamate receptors (mGluR1s). The thalamic mGluR1-PI-PLC-beta4 cascade is essential for formalin-induced inflammatory pain by regulating the response of ventral posterolateral thalamic nucleus (VPL) neurons. Moreover, PI-PLC-beta4 is essential for long-term depression (LTD) in the rostral cerebellum, which may be required for the acquisition of the conditioned eyeblink response. Besides, PI-PLC-beta4 may play an important role in maintenance of the status epilepticus. The mutations of PI-PLC-beta4 has been identified as the major cause of autosomal dominant auriculocondylar syndrome (ACS). PI-PLC-beta4 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence
KKHWMRLCFLVNPNGKIPVRSITRTFASGKTEKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKIC
PRTDIEELFKKINGDKKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQL
SSDGFCRYLMSDE
>gnl|CDD|320042 cd16212, EFh_NorpA_like, EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and similar proteins. NorpA, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase, is an eye-specific phosphoinositide phospholipase C (PI-PLC) encoded by norpA gene in Drosophila. It is expressed predominantly in photoreceptors and plays an essential role in the phototransduction pathway of Drosophila. A mutation within the norpA gene can render the fly blind without affecting any of the obvious structures of the eye. Like beta-class of vertebrate PI-PLCs, NorpA contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence
KKHWMRLGFMVDSGGKIPVKHIARTFASGKTEKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKIC
PRNDIEELFTSITKGKGEHISLAQLINFMNDKQRDPRLNEILYPLYDEKRCTEIIKAYEQNEENIKNKRM
SKDGFIRYLMSDE
>gnl|CDD|320043 cd16213, EFh_PI-PLC21, EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins. The family includes invertebrate homologs of phosphoinositide phospholipase C beta (PI-PLC-beta) named PLC21 from cephalopod retina. It also includes PLC21 encoded by plc-21 gene, which is expressed in the central nervous system of Drosophila. Like beta-class of vertebrate PI-PLCs, PLC21 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence
EKAYTKLTLQTDKEGKIPVKNIVKMFAQHKDDRKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRL
TGRQEVEKIFDELGAKKKPYLTTEQFVDFLNKTQRDPRLNEILYPYANPKRARDLINQYEPNKSFAKKGH
LSVEGFLRYLMSED
>gnl|CDD|320044 cd16214, EFh_PI-PLCgamma1, EF-hand motif found in phosphoinositide phospholipase C gamma 1 (PI-PLC-gamma1). PI-PLC-gamma1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1, or PLC-148, or phospholipase C-II (PLC-II), or phospholipase C-gamma-1 (PLC-gamma-1), is abundantly expressed in embryonal cortical structures, neurons, oligodendrocytes and astrocytes, and is involved in various cellular events, including proliferation, differentiation, migration, survival, and cell death. It also associates with many diseases, including epilepsy, Huntington's disease (HD), depression, Alzheimer's disease (AD) and bipolar disorder. PI-PLC-gamma1 plays a critical role in cell migration and tumor cell invasiveness and metastasis. It can mediate the cell motility effects of growth factors, including platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin-like growth factor (IGF) and hepatocyte growth factor (HGF), as well as adhesion receptors. Moreover, PI-PLC-gamma1 can modulate neurite outgrowth, neuronal cell migration and synaptic plasticity through the Trk receptor. PI-PLC-gamma1 contains an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Besides, PI-PLC-gamma1 has a second PH domain, two SH2 (Src homology 2) regions, and one SH3 (Src homology 3) region, which are present within this linker. PI-PLC-gamma1 is activated by receptor and non-receptor tyrosine kinases via its two SH2 and a single SH3 domain
WLRKQFYSVDRNREDRISVKDLKNMLSQVNYRVPNMKFLREKLTDLELRSGDITYGQFAQLYRSLMFDAQ
KTMEVPFLERFEEREECKISLEDFQKFLLDYQKELWATDTNQVQEFMFNFLRDPLREIEEPYFSLDEFLT
FLFSKE
>gnl|CDD|320045 cd16215, EFh_PI-PLCgamma2, 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2. PI-PLC-gamma2, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2, or phospholipase C-IV (PLC-IV), or phospholipase C-gamma-2 (PLC-gamma-2), is highly expressed in cells of hematopoietic origin. It has been implicated in cell motility important to invasion and dissemination of tumor cells. As an important component of the B cell receptor (BCR) signaling pathway, PI-PLC-gamma2 is required for efficient formation of germinal center (GC) and memory B cells. It works as a critical effector stimulating the increase of intracellular Ca2+ and activates various signaling pathways downstream of the BCR. Moreover, PI-PLC-gamma2 has been implicated in Fc receptor-mediated degranulation of mast cells, integrin signaling in platelets, as well as integrin and Fc receptor-mediated neutrophil functions. It also acts as a crucial signaling mediator modifying DC gene expression program to activate DC responses to beta-glucan-containing pathogens. PI-PLC-gamma2 contains an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Besides, PI-PLC-gamma2 has a second PH domain, two SH2 (Src homology 2) regions, and one SH3 (Src homology 3) region, which are present within this linker. PI-PLC-gamma2 is activated by receptor and non-receptor tyrosine kinases via its two SH2 and a single SH3 domain. Unlike PI-PLC-gamma1, the activation of PI-PLC-gamma2 may require concurrent stimulation of PI 3-kinase
WLRKQIYSVDQTRRNSISVRELKTILPQVNFKVPSAKFLKDKFQEIGAKKDELTFEQFHLFYKKLMFEQQ
KSILDEFKKDSSVFILGNTDRPDASAVHLHDFQRFLVHEQKESWAQDLNKVRERMTKFIDDTMRETAEPF
LFVDEFLTYLFSKE
>gnl|CDD|320046 cd16216, EFh_PI-PLCgamma1_like, EF-hand motif found in 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1-like proteins. This family corresponds to a small group of uncharacterized 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1-like (PI-PLC-gamma1-like) proteins. Although their biological function remains unclear, they shows high sequence similarity with other phosphoinositide phospholipase C gamma proteins. They contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. A second PH domain, which is split by two SH2 (Src homology 2) domains, and one SH3 (Src homology 3) domain, are present within this linker
WLRKQFDGMDRSREGSITVKDLKALLPQVNYRVPNMRFLRDKLVEVEARSELTFPHFIQFYKNLMFDAQK
SIIEQLELSFPLRNVDRPELCQISLYDFQKFLQHDQKESWASDVGRVRDYLCGYLKESSNEAPEPSLQLD
EFLTYLFSKE
>gnl|CDD|320047 cd16217, EFh_PI-PLCdelta1, EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1). PI-PLC-delta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 (PLCD1), or phospholipase C-III (PLC-III), or phospholipase C-delta-1 (PLC-delta-1), is present in high abundancy in the brain, heart, lung, skeletal muscle and testis. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. PI-PLC-delta1 is required for maintenance of homeostasis in skin and metabolic tissues. Moreover, it is essential in trophoblasts for placental development. Simultaneous loss of PI-PLC-delta1 may cause placental vascular defects, leading to embryonic lethality. PI-PLC-delta1 can be positively or negatively regulated by several binding partners, including p122/Rho GTPase activating protein (RhoGAP), Gha/Transglutaminase II, RalA, and calmodulin. It is involved in Alzheimer's disease and hypertension. Furthermore, PI-PLC-delta1 regulates cell proliferation and cell-cycle progression from G1- to S-phase by control of cyclin E-CDK2 activity and p27 levels. It can be activated by alpha1-adrenoreceptors (AR) in a calcium-dependent manner and may be important for G protein-coupled receptors (GPCR) responses in vascular smooth muscle (VSM). PI-PLC-delta1 may also be involved in noradrenaline (NA)-induced phosphatidylinositol-4,5-bisphosphate (PIP2) hydrolysis and modulate sustained contraction of mesenteric small arteries. In addition, it inhibits thermogenesis and induces lipid accumulation, and therefore contributes to the development of obesity. PI-PLC-delta1 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. In addition, PI-PLC-delta1 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, as well as a nuclear localization signal within its linker region, both of which may be responsible for translocating PI-PLC-delta1 into and out of the cell nucleus
WIHSCLRKADKNKDNKMSFKELKDFLKEINIEVDDDYAEKLFKECDKSKSGFLEGEEIEEFYKLLTKREE
IDVIFGEYAKSDGTMSRNNLLNFLQEEQREEVAPAYALSLIEKYEPDETAKAQRQMTKDGFLMYLLSPE
>gnl|CDD|320048 cd16218, EFh_PI-PLCdelta3, EF-hand motif found in phosphoinositide phospholipase C delta 3 (PI-PLC-delta3). PI-PLC-delta3, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 (PLCD3), phospholipase C-delta-3 (PLC-delta-3), is expressed abundantly in brain, skeletal muscle and heart. PI-PLC-delta3 gene expression is down-regulation by cAMP and calcium. PI-PLC-delta3 acts as anchoring of myosin VI on plasma membrane, and further modulates Myosin IV expression and microvilli formation in enterocytes. It negatively regulates RhoA expression, inhibits RhoA/Rho kinase signaling, and plays an essential role in normal neuronal migration by promoting neuronal outgrowth in the developing brain. Moreover, PI-PLC-delta3 is essential in trophoblasts for placental development. Simultaneous loss of PI-PLC-delta3 may cause placental vascular defects, leading to embryonic lethality. PI-PLC-delta3 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. In addition, PI-PLC-delta3 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, which may be responsible transporting PI-PLC-delta3 from the cell nucleus
WIHEYLRRADLNKDGKMSFEEIKDLLQMINIDLNEQYAYQLFKECDRSNDDRLEEHEIEEFCRRLMQRPE
LEEIFHQYSGEDCVLSAEELREFLKDQGEDASLVHAKELIQTYELNEKAKQHQLMTLDGFTMYMLSKD
>gnl|CDD|320049 cd16219, EFh_PI-PLCdelta4, EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4). PI-PLC-delta4, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 (PLCD4), or phospholipase C-delta-4 (PLC-delta-4), is expressed in various tissues with the highest levels detected selectively in the brain, skeletal muscle, testis and kidney. It plays a significant role in cell growth, cell proliferation, tumorigenesis, and in an early stage of fertilization. PI-PLC-delta4 may function as a key enzyme in the regulation of PtdIns(4,5)P2 levels and Ca2+ metabolism in nuclei in response to growth factors, and its expression may be partially regulated by an increase in cytoplasmic Ca2+. Moreover, PI-PLC-delta4 binds glutamate receptor-interacting protein1 (GRIP1) in testis and is required for calcium mobilization essential for the zona pellucida-induced acrosome reaction in sperm. Overexpression or dysregulated expression of PLCdelta4 may initiate oncogenesis in certain tissues through upregulating erbB1/2 expression, extracellular signal-regulated kinase (ERK) signaling pathway, and proliferation in MCF-7 cells. PI-PLC-delta4 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, and a C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unlike PI-PLC-delta 1 and 3, a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1 and 3 from the cell nucleus, is not present in PI-PLC-delta4
WIRDWFQKADKNKDGRMNFKEVRDLLKMMNVDMNEEHALRLFQMADKSESGTLEGEEFVLFYKALTQRED
VLKIFQDFSADGQKLTLLEFVDFLQQEQLERENTEELAMELIDRYEPSDTAKKLHALSIDGFLMYLCSPE
>gnl|CDD|320050 cd16220, EFh_PI-PLCeta1, EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1). PI-PLC-eta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1, or phospholipase C-eta-1 (PLC-eta-1), or phospholipase C-like protein 3 (PLC-L3), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the zona incerta and in the spinal cord. PI-PLC-eta1 may perform a fundamental role in the brain. It may also act in synergy with other PLC subtypes. For instance, it is activated via intracellular Ca2+ mobilization and then plays a role in the amplification of GPCR (G-protein-coupled receptor)-mediated PLC-beta signals. In addition, its activity can be stimulated by ionomycin. PI-PLC-eta1 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases
WVKQTFEEADKNGDGLLNIEEIYQLMHKLNVNLPRRKVRQMFQEADTDENQGTLTFEEFCVFYKMMSLRR
DLYLLLLSYSDKKDHLTVEELAQFLKVEQKMNNVTTEYCLDIIKKFEVSEENKEQNVLGIEGFTNFMRSP
A
>gnl|CDD|320051 cd16221, EFh_PI-PLCeta2, EF-hand motif found in phosphoinositide phospholipase C eta 2 (PI-PLC-eta2). PI-PLC-eta2, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2, or phosphoinositide phospholipase C-like 4, or phospholipase C-like protein 4 (PLC-L4), or phospholipase C-eta-2 (PLC-eta2), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the pituitary gland, pineal gland, retina, and lung, as well as in neuroendocrine cells. PI-PLC-eta2 has been implicated in the regulation of neuronal differentiation/maturation. It is required for retinoic acid-stimulated neurite growth. It may also in part function downstream of G-protein-coupled receptors and play an important role in the formation and maintenance of the neuronal network in the postnatal brain. Moreover, PI-PLC-eta2 acts as a Ca2+ sensor that shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Its activation can be triggered either by intracellular calcium mobilization or by G beta-gamma signaling. PI-PLC-eta2 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases
WLKQTFDEADKNGDGSLSIGEVLQLLHKLNVNLPRQKVKQMFKEADTDDNQGTLGFEEFCAFYKMMSTRR
DLYLLMLTYSNHKDHLDTNDLQRFLEVEQKMAGVTREHCLEIISQFEPCSENKQNGALGIDGFTNYMRSP
A
>gnl|CDD|320052 cd16222, EFh_PRIP1, EF-hand motif found in phospholipase C-related but catalytically inactive protein 1 (PRIP-1). PRIP-1, also termed phospholipase C-deleted in lung carcinoma, or inactive phospholipase C-like protein 1 (PLC-L1), or p130, is a novel inositol 1,4,5-trisphosphate (InsP3) binding protein that is predominantly expressed in the brain. It is involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. It interacts with the catalytic subunits of protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A), and functions as a scaffold to regulate the activities and subcellular localizations of both PP1 and PP2A in phospho-dependent cellular signaling. It also promotes the translocation of phosphatases to lipid droplets to trigger the dephosphorylation of hormone-sensitive lipase (HSL) and perilipin A, thus reducing protein kinase A (PKA)-mediated lipolysis. Moreover, PRIP-1 plays an important role in insulin granule exocytosis through the association with GABAA-receptor-associated protein (GABARAP) to form a complex to regulate KIF5B-mediated insulin secretion. It also inhibits regulated exocytosis through direct interactions with syntaxin 1 and synaptosomal-associated protein 25 (SNAP-25) via its C2 domain. Furthermore, PRIP-1 has been implicated in the negative regulation of bone formation. PRIP-1 has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP-1 does not have PLC enzymatic activity
WLSAVFEAADVDGYGIMLEDTAVELIKQLNPGIKEAKIRLKFKEIQKSKEKLTTRVTEEEFCEAYSELCT
RPEVYFLLVQISKNKEYLDAKDLMLFLEAEQGMTHITEEMCLDIIRRYEPSQEGRLKGFLGIDGFTQYLL
SSE
>gnl|CDD|320053 cd16223, EFh_PRIP2, EF-hand motif found in phospholipase C-related but catalytically inactive protein 2 (PRIP-2). PRIP-2, also termed phospholipase C-L2, or phospholipase C-epsilon-2 (PLC-epsilon-2), or inactive phospholipase C-like protein 2 (PLC-L2), is a novel inositol 1,4,5-trisphosphate (InsP3) binding protein that exhibits a relatively ubiquitous expression. It functions as a novel negative regulator of B-cell receptor (BCR) signaling and immune responses. PRIP-2 has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP-2 does not have PLC enzymatic activity
WLSQMFVEADTDNVGHITLCRAVQFIKNLNPGLKTSKIELKFKELHKSKEKGGTEVTKEEFIEVFHELCT
RPEIYFLLVQFSSNKEFLDTKDLMMFLEAEQGMAHVTEEISLDIIHKYEPSKEGQEKGWLSLDGFTNYLM
SPEC
>gnl|CDD|320022 cd16224, EFh_CREC_RCN2, EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2). RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER)
HYPNGEHNAEYDKEAFLGGEEDADEFAKLSPEEQQKRLKSIIKKIDTDSDGFLTEEELSSWIQQSFRHYA
LEDAKQQFPEYDKDGDGAVTWDEYNMQMYDRVIDYDEDTVLDDEEEESFRQLHLKDKKRFDKANTDGGPG
LNLTEFIAFEHPEEVDYMTEFVIQEALEEHDKDGDGFISLEEFLGDYRKDPTANEDPEWIIVEKDRFVND
YDKDNDGKLDPQELLPWVVPNNYGIAQEEALHLIDEMDLNGDGRLSEEEILENQDLFL
>gnl|CDD|320023 cd16225, EFh_CREC_cab45, EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45). Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN
LERDGHLNKEFHKEVFLGNEKEEFEEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQEHFQE
AVEENEQIFKAVDTDKDGNVSWEEYRVHFLLSKGYSEEEAEEKIKNNEELKLDEDDKEVLDRYKDRWSQA
DEPEDGLLDVEEFLSFRHPEHSRGMLKNMVKEILHDLDQDGDEKLTLDEFVSLPPGTVEEQQAEDDDEWK
KERKKEFEEVIDLNHDGKVTKEELEEYMDPRNERHALNEAKQLIAVADENKDGKLSLEEILKNSDLFT
>gnl|CDD|320024 cd16226, EFh_CREC_Calumenin_like, EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4
HDDDGEHNPEYDHEAFLGKEEAKEFDQLTPEESKERLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIR
EDVDRQWKEYDPNKDGKLSWEEYKKATYGFLDDEEEDDDLHESYKKMIRRDERRWKAADQDGDGKLTKEE
FTAFLHPEEFPHMRDIVVQETLEDIDKNKDGFISLEEYIGDMYRDDDEEEDPDWVKSEREQFKEFRDKNK
DGKMDREEVKDWILPEDYDHAEAEAKHLIYEADDDKDGKLTKEEILDKYDLFVG
>gnl|CDD|320025 cd16227, EFh_CREC_RCN2_like, EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes. This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER)
HAKDGEHNPEFDHEAVLGSRKEAEEFDELPPEEAKRRLAVLAKKMDLNDDGFIDRKELKAWILRSFKMLD
EEEANERFEEADEDGDGKVTWEEYLADSFGYDDEDNEEMIKDSTEDDLKLLEDDKEMFEAADLNKDGKLD
KTEFSAFQHPEEYPHMHPVLIEQTLRDKDKDNDGFISFQEFLGDRAGHEDKEWLLVEKDRFDEDYDKDGD
GKLDGEEILSWLVPDNEEIAEEEVDHLFASADDDHDDRLSFDEILDHHEIFVG
>gnl|CDD|320026 cd16228, EFh_CREC_Calumenin, EF-hand, calcium binding motif, found in calumenin. Calumenin, also termed crocalbin, or IEF SSP 9302, is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It is highly expressed in various brain regions. Thus it plays an important role in migration and differentiation of neurons, and/or in Ca2+ signaling between glial cells and neurons. Calumenin is involved in Ca2+ homeostasis through interacting with ryanodine receptor RyR2 and SERCA2. It acts as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. Calumenin also forms a Ca2+-dependent complex with thrombospondin-1, which is broadly involved in haemostasis and thrombosis. Moreover, calumenin is a molecular chaperone that endogenously regulates the vitamin K-dependent gamma-carboxylation of several proteins, including blood coagulation factors (such as FII, FVII, FIX, FX, and proteins C, S and Z), cell survival factors (Gas6) and bone metabolism proteins (such as matrix Gla protein or MGP, osteocalcin and periostin), through targeting the gamma-glutamyl carboxylase. It also functions as a charged F508del-cystic fibrosis transmembrane regulator (CFTR) folding modulator, as well as a G551D-CFTR associated protein. Furthermore, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. It binds to and stabilizes fibulin-1, and further inactivates extracellular signal-regulated kinases 1 and 2 (ERK1/2) signaling
KVHDDAQNFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIY
EDVERQWKGHDLNEDGLVSWEEYKNATYGYILDDPDPDDGFNYKQMMVRDERRFKMADKDGDLRATKEEF
TAFLHPEEYDYMKDIVVLETMEDIDKNGDGFIDLEEYIGDMYSQDGDADEPEWVKTEREQFTEFRDKNKD
GKMDKEETKDWILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIVDKYDLFVG
>gnl|CDD|320027 cd16229, EFh_CREC_RCN1, EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1). RCN-1 is an endoplasmic reticulum resident low-affinity Ca2+-binding protein with six EF-hand motifs and a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It is expressed at the cell surface. RCN-1 acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signaling cascade. It also plays a key role in the development of doxorubicin-associated resistance
QLHEDNQSFQYDHEAFLGKEEAKTFDQLTPEESKERLGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIY
ENVAKVWKDYDLNKDNKISWEEYKQATYGYYLGNPEEFQDATDQFSFKKMLPRDERRFKAADLDGDLAAT
REEFTAFLHPEEFEHMKDIVVLETLEDIDKNGDGFVDEDEYIADMFSHEEGGPEPDWVKTEREQFSDFRD
LNKDGKMDKEEIRHWILPQDYDHAQAEARHLVYESDKDKDQKLTKEEILDNWNMFVG
>gnl|CDD|320028 cd16230, EFh_CREC_RCN3, EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3). RCN-3, also termed EF-hand calcium-binding protein RLP49, is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal His-Asp-Glu-Leu (HDEL) tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4
PHDDAHGNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRH
IRDSVSAAWQTYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMA
TREELTAFLHPEEFPHMRDIVVAETLEDLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQTERQQFRQFR
DLNKDGRLDGSEVGHWVLPPSQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVG
>gnl|CDD|320010 cd16231, EFh_SPARC_like, EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC) and similar proteins. This family includes secreted protein acidic and rich in cysteine (SPARC), secreted protein, acidic and rich in cysteine-like 1 (SPARCL1), and similar proteins. SPARC is a prototypic collagen-binding matricellular protein that is involved in extracellular matrix (ECM) assembly and fibrosis through binding both fibrillar collagen and basal lamina collagen IV. It regulates the activity of matrix metalloproteinases (MMPs), as well as the growth factor signaling mediated by cell surface receptors including vascular endothelial growth factor (VEGF) receptor, basic fibroblast growth factor (bFGF), and transforming growth factor (TGF) beta1. It also shows survival activity in tumor progression. SPARC contains an N-terminal acidic 52-residue segment followed by a follistatin-like (FS) domain, and an alpha-helical EC domain with 2 unusual calcium-binding EF-hands and the collagen-binding site. SPARCL1 is the closest family member to SPARC. It shares the three primary domains contained within SPARC with an expanded N-terminal domain. SPARCL1 may function as both a tumor suppressor and as a regulator of angiogenesis. It can bind to collagens and be counter-adhesive to wild-type dermal fibroblasts, but do not influence rates of cell proliferation. Moreover, SPARCL1 can influence central nervous system (CNS) development and synaptic rearrangement
CLDEELSEFPLRMRDWLKNVMVQLAERDELHEGLTEKELEDFQKNYKMYVYPVHWKFCDLDQHPHDRYLS
HHELAPLRAPLVPMEHCTTPFLETCDADNDKLISLKEWGACLGLKE
>gnl|CDD|320011 cd16232, EFh_SPARC_TICN, EF-hand, extracellular calcium-binding (EC) motif, found in testicans. Testicans are nervous system-expressed proteoglycans that play important roles in the regulation of protease activity, as well as in the determination of age at menarche. Testican-1 (TICN1, also termed protein SPOCK) is a secreted chimeric proteoglycan that is highly expressed in brain and carries both chondroitin and heparan sulfate glycosaminoglycan side chains. It has been implicated in autoimmune disease. It also acts as a regulator of bone morphogenetic protein (BMP) signaling and show critical functions in the nervous system. Testican-2 (TICN2, also termed protein SPOCK2) is an extracellular heparan sulphate proteoglycan highly expressed in brain. It may play regulatory roles in the development of the central nervous system. It also participates in diverse steps of neurogenesis. TICN1, but not TICN2, inhibits cathepsin L. TICN1 also inhibits attachment and neurite outgrowth in cultures of N2A neuroblastoma cells, While TICN2 is able to inhibit neurite outgrowth from primary cerebellar cells. Testicans contain an N-terminal signal peptide, a testican-specific domain followed by a follistatin-like (FS) domain, an extracellular calcium-binding (EC) domain including a pair of EF hands, a thyroglobulin-like domain (TY), and a C-terminal region with two putative glycosaminoglycan attachment sites. The substitution of a ligating Asp residue by Tyr orTyr in the +Y position of EF hand 2 in testican-2 could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ with low affinity. The substitution of a ligating Asp residue by Phe or Tyr in the +Y position of EF-hand 2 in testicans could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ ion with low affinity
CTESELSEMGDRLLDWFSVLHEQSNKAKKTSSSKRFDKSHLPECKPSVGWMFNQLDTNNDLHLSQSELYD
LELDKYEPCIKPFLDSCDRNKDGKISSDEWCDCFQRAD
>gnl|CDD|320012 cd16233, EFh_SPARC_FSTL1, EF-hand, extracellular calcium-binding (EC) motif, found in follistatin-related protein 1 (FRP-1). FRP-1, also termed follistatin-like protein 1 (fstl-1), TGF-beta-stimulated clone 36 (TSC-36/Flik), or TGF-beta inducible protein, is a secreted glycoprotein that is overexpressed in certain inflammatory diseases and has been implicated in many autoimmune diseases. FRP-1 functions as an important proinflammatory factor in the pathogenesis of osteoarthritis (OA) by activating the canonical NF-kappaB-mediated inflammatory cytokines, including tumor necrosis factor alpha (TNF-alpha), interleukin-1beta (IL-1beta) and interleukin-6 (IL-6), and enhancing fibroblast like synoviocytes proliferation. It also acts as a critical mediator of collagen-induced arthritis (CIA), juvenile rheumatoid arthritis (JRA), as well as Lyme arthritis observed after Borrelia burgdorferi infection. Meanwhile, it enhances nod-like receptor family, pyrin domain containing 3 (NLRP3) inflammasome-mediated IL-1beta secretion from monocytes and macrophages. Moreover, FRP-1 shows critical functions in the nervous system. It differentially regulates transforming growth factor beta (TGF-beta) and bone morphogenetic protein (BMP) signaling, leading to epithelial injury and fibroblast activation. Furthermore, FRP-1 functions as a cardiokine with cardioprotective properties. It may play a potential role in ischemic stroke through decreasing neuronal apoptosis and improving neurological deficits via disco-interacting protein 2 homolog A (DIP2A)/Akt pathway after middle cerebral artery occlusion (MCAO). Plasma FRP-1 is elevated in Kawasaki disease (KD) and thus may play a possible role in the formation of coronary artery aneurysm (CAA). FRP-1 contains a follistatin-like (FS) domain, an extracellular calcium-binding (EC) domain including a pair of EF hands, and a von Willebrand factor type C (VWC) domain. The EC domain does not undergo characteristic structural changes upon calcium addition or depletion and therefore is not a functional calcium binding domain
CYQSDRDELRRRVIDWLQTEVIPDGWFTKGSSYSDILDKYFKKYDNGDSQLDSNELLKFVEQNETATNLT
LYQDEETNKLLRGLCVDALIELSDENADWKLNFEEFLKCLNPSF
>gnl|CDD|320013 cd16234, EFh_SPARC_SMOC, EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding protein SMOC-1, SMOC-2, and similar proteins. SMOC proteins corresponds to a group matricellular proteins that are involved in direct or indirect modulation of growth factor signaling pathways and play diverse roles in physiological processes involving extensive tissue remodeling, migration, proliferation, and angiogenesis. They may mediate intercellular signaling and cell type-specific differentiation during gonad and reproductive tract development. SMOC-1 is localized in basement membranes. Its mutations have been found to be associated with individuals with Warrdenburg Anopthalmia Syndrome. SMOC-2 is ubiquitously expressed and is involved in angiogenesis and the regulation of cell cycle progression. It enhances the angiogenic effect of basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF). It has also been implicated in generalized vitiligo. SMOC proteins consist of a follistatin-like (FS) domain, two thyroglobulin-like (TY) domains, a novel domain conserved only in SMOC proteins, and an extracellular calcium-binding (EC) domain with two EF-hand calcium-binding motifs
CPEAKKTEFLNNLIDALKTEMVRSGNSNSSAPDKSSEEQVLDWKFSQLDKNKNGVLERKEWKPFKRLLKK
AVKPKKCARKFPKYCDVNKDKKISLTEWLNCLGV
>gnl|CDD|320014 cd16235, EFh_SPARC_SPARC, EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC). SPARC, also termed basement-membrane protein 40 (BM-40), or osteonectin (ON), is a prototypic collagen-binding matricellular protein that is essential for embryo development in invertebrates and highly expressed in bone. It participates in normal tissue remodeling as it regulates the deposition of extracellular matrix, as well as in neoplastic transformation. It is involved in extracellular matrix (ECM) assembly and fibrosis through binding both fibrillar collagen and basal lamina collagen IV. It regulates the activity of matrix metalloproteinases (MMPs), as well as the growth factor signaling mediated by cell surface receptors including vascular endothelial growth factor (VEGF) receptor, basic fibroblast growth factor (bFGF), and transforming growth factor (TGF) beta1. SPARC shows survival activity in tumor progression. It plays a role in metastatic process to the lung during melanoma progression. It can suppress prostate cancer cell growth and survival. Moreover, SPARC is a bone- associated protein that has a major role in bone development and mineralisationis. It is involved in the initiation and progression of vascular calcification and upregulated by adiponectin. Furthermore, SPARC may be one of the molecules that govern the uptake and delivery of proteins from blood to the cerebrospinal fluid (CSF) during brain development. SPARC contains an N-terminal acidic 52-residue segment followed by a follistatin-like (FS) domain, and an alpha-helical EC domain with 2 unusual calcium-binding EF-hands and the collagen-binding site. Platelet-derived growth factor (PDGF) also interacts with its EC domain, but in a calcium-independent manner, whereas collagen binding is calcium-dependent
CLDSELTEFPLRMRDWLKNVLVTLYERDYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAPLIPMEHCTTR
FFETCDLDNDKYIALDEWAGCFGIKQ
>gnl|CDD|320015 cd16236, EFh_SPARC_SPARCL1, EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein, acidic and rich in cysteine-like 1 (SPARCL1). SPARCL1, also termed SPARC-like protein 1, or high endothelial venule protein (Hevin), or MAST 9, or SC-1, or RAGS-1, or QR1, or ECM 2, is a diversely expressed and developmentally regulated extracellular matrix glycoprotein involved in tissue repair and remodeling via interaction with the surrounding extracellular matrix (ECM) proteins. It plays a pivotal role in the corneal wound healing. SPARCL1 may function as both a tumor suppressor and as a regulator of angiogenesis. It regulates cell migration/invasion and suppresses metastasis in many cancers, including prostate cancer, colorectal cancer, gastric cancer, and breast cancer. It can bind to collagens and be counter-adhesive to wild-type dermal fibroblasts, but do not influence rates of cell proliferation. Moreover, SPARCL1 contributes to neural development and participates in remodeling events associated with neuronal degeneration following neural injury. It can influence central nervous system (CNS) development and synaptic rearrangement. SPARCL1 is the closest family member to secreted protein acidic and rich in cysteine (SPARC), but does not compensate for the absence of SPARC in the CNS. SPARC contains an N-terminal acidic 52-residue segment followed by a follistatin-like (FS) domain, and an alpha-helical EC domain with 2 unusual calcium-binding EF-hands and the collagen-binding site. SPARCL1 shares the three primary domains contained within SPARC with an expanded N-terminal domain
CTDSEVVQFPLRMRDWLKNILMQLYYIYPVHWQFAQLDQHPSDRFLTHSELAPLRASLVPMEHCITRFFQ
ECDADKDKLITLKEWCHCFGIKE
>gnl|CDD|320016 cd16237, EFh_SPARC_TICN1, EF-hand, extracellular calcium-binding (EC) motif, found in testican-1 (TICN1). TICN1, also termed protein SPOCK, or SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 1 (Spock1), is a secreted chimeric proteoglycan that is highly expressed in brain and carries both chondroitin and heparan sulfate glycosaminoglycan side chains. It promotes resistance against Pseudomonas aeruginosa-induced keratitis through regulation of matrix metalloproteinase (MMP)-2 expression and activation. It also acts as a potential cancer prognostic marker that promotes the proliferation and metastasis of gallbladder cancer cells by activating the PI3K/Akt pathway. Moreover, TICN1 corresponding gene SPOCK1 is a novel transforming growth factor-beta target gene that regulates lung cancer cell epithelial-mesenchymal transition. It is also up-regulated by chromodomain helicase/adenosine triphosphatase DNA binding protein 1-like (CHD1L), and promotes human hepatocellular carcinoma (HCC) cell invasiveness and metastasis. Furthermore, TICN1 inhibits the lysosomal cysteine protease cathepsin L in intracellular vesicles and in the extracellular milieu. TICN1 contains an N-terminal signal sequence known to direct nascent polypeptides to the extracellular space, an unique region to the testicans, a follistatin (FS)-like domain generally involving five disulfide bridges, an extracellular calcium-binding (EC) domain including a pair of EF hands, and a thyroglobulin type-1 (TY) domain followed by a C-terminal acidic region with high density of negatively charged amino acids. The substitution of a ligating Asp residue by Phe291 in the +Y position of EF-hand 2 in TICN1 could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ ion with low affinity
CTDKELRNLASRLKDWFGALHEDANRVIKPTSSFTAQGRFDTSILPICKDSLGWMFNKLDMNYDLLLDPS
EISAIYLDKYEPCMKPLFNSCDSFKDGKLSNNEWCYCFQKPG
>gnl|CDD|320017 cd16238, EFh_SPARC_TICN2, EF-hand, extracellular calcium-binding (EC) motif, found in testican-2 (TICN2). TICN2, also termed SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 2 (Spock2), is an extracellular heparan sulphate proteoglycan expressed in brain, lung, and testis. It inhibits neurite extension from cultured primary cerebellar neurons and may play regulatory roles in the development of the central nervous system. It also participates in diverse steps of neurogenesis. Moreover, TICN2 may contribute to ECM remodeling by regulating function(s) of other testican family members, which possess membrane-type matrix metalloproteinases (MT-MMPs) inhibitory function. Furthermore, TICN2 corresponding gene SPOCK2 acts as a susceptibility gene for bronchopulmonary dysplasia. TICN2 contains an N-terminal signal peptide, a testican-specific domain followed by a follistatin-like (FS) domain, an extracellular calcium-binding (EC) domain including a pair of EF hands, a thyroglobulin-like domain (TY), and a C-terminal region with two putative glycosaminoglycan attachment sites. The substitution of a ligating Asp residue by Tyr292 in the +Y position of EF-hand 2 in TICN2 could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ ion with low affinity
CTGQDLADLGDRLRDWFQLLHENSKQNGSGSPPASPASALDRSLVASCKDSIGWMFSKLDTSGDLFLDQA
ELAAINLDKYEVCIRPFFNSCDTYRDGRVSTAEWCFCFWREK
>gnl|CDD|320018 cd16239, EFh_SPARC_TICN3, EF-hand, extracellular calcium-binding (EC) motif, found in testican-3 (TICN3). TICN3, also termed SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 3 (Spock3), is a brain-specific heparan sulfate proteoglycan that shows a widespread distribution within the extracellular matrix of the brain. It plays an important role in the formation or maintenance of major neuronal structures in the brain. It also functions as a novel regulator to reduce the activity of matrix metalloproteinase (MMP) in adult T-cell leukemia (ATL). It suppresses membrane-type 1 MMP-mediated MMP-2 activation and tumor invasion. Moreover, TICN3 corresponding gene SPOCK3 acts as a risk gene for adult attention-deficit/hyperactivity disorder (ADHD) and personality disorders. TICN3 contains an N-terminal signal peptide, a testican-specific domain followed by the follistatin-like (FS) and extracellular calcium-binding (EC) domains characteristic of the BM-40 family. Towards the C-terminus they contain a thyroglobulin-like domain (TY) and a novel sequence (domain V), which includes two potential glycosaminoglycan attachment sites. The substitution of a ligating Asp residue by Tyr295 in the +Y position of EF-hand 2 in testican-3 could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ ion with low affinity
CSDLEFREVANRLRDWFKALHESGSQNKKTKIVRRPERSRFDTSILPICKDSLGWMFNRLDTNYDLLLDQ
SELGSIYLDKNEQCTKAFFNSCDTYKDSLISNNEWCYCFQRQQ
>gnl|CDD|320019 cd16240, EFh_SPARC_SMOC1, EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding protein 1 (SMOC-1). SMOC-1, also termed SPARC-related modular calcium-binding protein 1, or smooth muscle-associated protein 1 (SMAP-1), is an Arf6 GTPase-activating protein (GAP) that directly interacts with clathrin and regulates the clathrin-dependent endocytosis of transferrin receptors from the plasma membrane. It is predominantly localized in basement membranes. SMOC-1 acts as a regulator of osteoblast differentiation and is involved in inhibition of transforming growth factor-beta (TGF-beta) signaling through production of nitric oxide. It also plays an essential role in ocular and limb development and functions as a regulator of bone morphogenic protein (BMP) signaling. It interacts with a matricellular protein, tenascin C in addition to the serum proteins, fibulin-1 and C-reactive protein, but not collagens. Two point mutations in the SMOC1 gene may cause Waardenburg Anophtalmia Syndrome. Moreover, SMOC-1 is involved in direct or indirect modulation of growth factor signaling pathways and plays a role in physiological processes involving extensive tissue remodeling. SMOC-1 contains a follistatin-like (FS) domain, two thyroglobulin-like (TY) domains, a novel domain, which is found only in the homologous SMOC-2, and an extracellular calcium-binding (EC) domain with two EF-hand calcium-binding motifs
CPEGKKLEFITSLLDALTTDMVQAINSAAPTGGGRFSEPDPSHTLEERVVHWYFSQLDNNSSNDINKKEL
KPFKRYVKKKAKPKKCARRFTDYCDLNKDKSISLQELKGCLGVSK
>gnl|CDD|320020 cd16241, EFh_SPARC_SMOC2, EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding protein 2 (SMOC-2). SMOC-2, also termed SPARC-related modular calcium-binding protein 2, or smooth muscle-associated protein 2 (SMAP-2), is a ubiquitously expressed matricellular protein that enhances the response to angiogenic growth factors, mediate cell adhesion, keratinocyte migration, and metastasis. It is also associated with vitiligo and craniofacial and dental defects. Moreover, SMOC-2 acts as an Arf1 GTPase-activating protein (GAP) that interacts with clathrin heavy chain (CHC) and clathrin assembly protein CALM and functions in the retrograde, early endosome/trans-Golgi network (TGN) pathway in a clathrin- and AP-1-dependent manner. It also contributes to mitogenesis via activation of integrin-linked kinase (ILK). SMOC-2 contains a follistatin-like (FS) domain, two thyroglobulin-like (TY) domains, a novel domain, which is found only in the homologous SMOC-1, and an extracellular calcium-binding (EC) domain with two EF-hand calcium-binding motifs
CPGAKKTEFLTSVLDALSTDMVHAVSDPSASSRRLSEPDPSHTLEERVVHWYFKQLDKNSSGDIGKKEIK
PFKRFLRKKSKPKKCVKKFVEYCDVNNDKSLSVQELMGCLGVTK
>gnl|CDD|320000 cd16242, EFh_DMD_like, EF-hand-like motif found in the dystrophins subfamily. This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils
SLSTAIEAFDQHGLRAQNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVDLCLNWLLNVYDSGRSGK
IRVLSFKVGLVLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPSV
RSCFEKAGEKPEISAAHFLDWLK
>gnl|CDD|320001 cd16243, EFh_DYTN, EF-hand-like motif found in dystrotelin and similar proteins. Dystrotelin is the vertebrate orthologue of Drosophila DAH, which is involved in the synchronised cellularization of thousands of nuclei in the syncytial early fly embryo (a specialised form of cytokinesis). Dystrotelin is mainly expressed in the developing central nervous system (CNS) and adult nervous and muscular tissues. Heterologously expressed dystrotelin protein localizes spontaneously to the cytoplasmic membrane, and possibly to the endoplasmic reticulum (ER). Dystrotelin is not critical for mammalian development. It may be involved in other forms of cytokinesis. Its N-terminal region contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. The C-terminal region is extremely divergent. Unlike other superfamily members, dystrophin or dystrobrevin, the residues directly involved in beta-dystroglycan binding are not conserved in dystrotelin, which makes it unlikely that dystrotelin interacts with this ligand. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize
DLRLIKPILNSLGGSIERTISLSVEEVSQALERLFQSASQEVPGQVSAEATEQTCRLLFRLYDREQTGFV
SLRSVEAALIALSGDTLSAKYRALFQLYESGQGGSSGSITRSGLRVLLQDLSQIPAVVQESHVFGNVETA
VRSCFSGVLTASISEEHFLSWLQ
>gnl|CDD|320002 cd16244, EFh_DTN, EF-hand-like motif found in dystrobrevins and similar proteins. Dystrobrevins are part of the dystrophin-glycoprotein complex (DGC). They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. The family includes two paralogs dystrobrevins, alpha- and beta-dystrobrevin, both of which are cytoplasmic components of the dystrophin-associated protein complex that function as scaffold proteins in signal transduction and intracellular transport. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. The dystrobrevins subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrobrevins contain one or two syntrophin binding sites (SBSs)
DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEA
TGRLTVFSVKVALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESA
ARSCFPGQSKVTVNDFLDVMM
>gnl|CDD|320003 cd16245, EFh_DAH, EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and similar proteins. DAH, the product of the dah (discontinuous actin hexagon) gene, is a Drosophila homolog to vertebrate dystrotelin. It is tightly membrane-associated and highly phosphorylated in a time-dependent fashion. DAH plays an essential role in the process of cellularization, and is associated with vesicles that convene at the cleavage furrow. The absence of DAH leads the severe disruption of the cleavage furrows around the nuclei and development stalls. DAH contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils
PLKLIMGVFDRHQLSNSENNLCLPPDELEAVLHDIYFAAEKLGNFNIDVDLATELLANLFLNVFDPERKK
SISVLELKVFLTLLCGSSLQEKYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELA
VEQCFENSPGLVGLTEYQFIGWWT
>gnl|CDD|320004 cd16246, EFh_DMD, EF-hand-like motif found in dystrophin. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection
SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRI
RVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVR
SCFQFANNKPEIEAALFLDWMR
>gnl|CDD|320005 cd16247, EFh_UTRO, EF-hand-like motif found in utrophin. Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, Utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs) and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs
DLNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKI
RVLSLKIGLMSLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVR
SCFQHANNKPEIDVKQFIDWMR
>gnl|CDD|320006 cd16248, EFh_DRP-2, EF-hand-like motif found in dystrophin-related protein 2 (DRP-2). DRP-2 is a dystrophin homologue mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. Like dystrophin, DRP-2 has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises only two spectrin repeats (SRs) and a WW domain
TLSSATEIFTEHELQMSERVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMCLNWLLNVYDSGRNGKI
RVLSFKTGIVCLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSNVEPSVR
SCFRFAPGKPVIELSQFLEWMN
>gnl|CDD|320007 cd16249, EFh_DTNA, EF-hand-like motif found in alpha-dystrobrevin. Alpha-dystrobrevin, also termed dystrobrevin alpha (DTN-A), or dystrophin-related protein 3 (DRP-3), is the mammalian ortholog of the Torpedo 87 kDa postsynaptic protein that tightly associates with dystrophin. It is a cytoplasmic protein expressed predominantly in skeletal muscle, heart, lung, and brain. Alpha-dystrobrevin has been implicated in the regulation of acetylcholine receptor (AChR) aggregate density and patterning. It is also essential in the pathogenesis of dystrophin-dependent muscular dystrophies. It plays a critical role in the full functionality of dystrophin through increasing dystrophin's binding to the dystrophin-glycoprotein complex (DGC), and provides protection during cardiac stress. Alpha-dystrobrevin binds to the intermediate filament proteins syncoilin and beta-synemin, thereby linking the dystrophin-associated protein complex (DAPC) to the intermediate filament network. Moreover, alpha-dystrobrevin involves in cell signaling via interaction with other proteins such as syntrophin, a modular adaptor protein that coordinates the assembly of the signaling proteins nitric oxide synthase, stress-activated protein kinase-3, and Grb2 to the DAPC. Furthermore, alpha-dystrobrevin plays an important role in muscle function, as well as in nuclear morphology maintenance through specific interaction with the nuclear lamina component lamin B1. In addition, alpha-dystrobrevin is required in dystrophin-associated protein scaffolding in brain. Absence of glial alpha-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema. Alpha-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, alpha-dystrobrevin contain two syntrophin binding sites (SBSs)
DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQINVEQSISLLLNFLLAAFDPEG
HGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQS
ARSCFSQQKKVTLNGFLDTLM
>gnl|CDD|320008 cd16250, EFh_DTNB, EF-hand-like motif found in beta-dystrobrevin. Beta-dystrobrevin, also termed dystrobrevin beta (DTN-B), is a dystrophin-related protein that is restricted to non-muscle tissues and is abundantly expressed in brain, lung, kidney, and liver. It may be involved in regulating chromatin dynamics, possibly playing a role in neuronal differentiation, through the interactions with the high mobility group HMG20 proteins iBRAF/HMG20a and BRAF35 /HMG20b. It also binds to and represses the promoter of synapsin I, a neuronal differentiation gene. Moreover, beta-dystrobrevin functions as a kinesin-binding receptor involved in brain development via the association with the extracellular matrix components pancortins. Furthermore, beta-dystrobrevin binds directly to dystrophin and is a cytoplasmic component of the dystrophin-associated glycoprotein complex, a multimeric protein complex that links the extracellular matrix to the cortical actin cytoskeleton and acts as a scaffold for signaling proteins such as protein kinase A. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. Beta-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, beta-dystrobrevin contain two syntrophin binding sites (SBSs)
DIWNMIEAFRDNGLNTLDHSTEISVSRLETIISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEG
HGKLTVFSVKAMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYTEHS
VRTCFPQQKKIMLNMFLDTMM
>gnl|CDD|319994 cd16251, EFh_parvalbumin_like, EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family. The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI _ 5 for alpha; pI
AKDIEKAPSAFRAHGSFNYKKFFEHVGLKQKSEDQIKKVFQILDKDKSGFIEEEELKYILKGFSIAGRDL
TDEETKALLAAGDTDGDGKIGVEEFATLVAG
>gnl|CDD|319995 cd16252, EFh_calglandulin_like, EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins. The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix)
DKDIDLLPSEMRHHGSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSM
PVAPLSDEEAEAMIQAADTDGDGRIDFQEFSDMVKK
>gnl|CDD|319996 cd16253, EFh_parvalbumins, EF-hand, calcium binding motif, found in parvalbumins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI _ 5 for alpha; pI
ANDIDIALAACQAADSFDHKAFFKAVGLSKKSPADIKKVFNILDQDKSGFIEEEELKLFLKNFSDGARVL
SDKETKNFLAAGDSDGDGKIGVDEFKSMVKA
>gnl|CDD|319997 cd16254, EFh_parvalbumin_alpha, EF-hand, calcium binding motif, found in alpha-parvalbumin. Alpha-parvalbumin is cytosolic Ca2+/Mg2+-binding protein expressed mainly in fast-twitch skeletal myofibrils, where it may act as a soluble relaxing factor facilitating the Ca2+-mediated relaxation phase. It is also expressed in rapidly firing neurons, particularly GABA-ergic neurons, and thus may confer protection against Ca2+ toxicity. The major role of alpha-parvalbumin is metal buffering and transport of Ca2+. It binds different metal cations, and exhibits very high affinity for Ca2+ and physiologically significant affinity for Mg2+. Alpha-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Both metal ion-binding sites in alpha-parvalbumin are high-affinity sites. Additionally, in contrast to beta-parvalbumin, alpha-parvalbumin is less acidic and has an additional residue in the C-terminal helix
AEDIKKAVGAFAAADSFDYKKFFEMVGLKKKSADDVKKVFHILDKDKSGFIEEDELKFVLKGFSPDGRDL
SDKETKALLAAGDKDGDGKIGIDEFATLVAE
>gnl|CDD|319998 cd16255, EFh_parvalbumin_beta, EF-hand, calcium binding motif, found in beta-parvalbumin. Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59)
AADIAAALSQCQAADSFNFKKFFATSGLSKKSADDVKKVFEIIDQDKSGFIEEEELKLFLQNFSSGAREL
TDAETKAFLKAGDSDGDGKIGVEEFQALVKA
>gnl|CDD|293929 cd16256, LumP, lumazine protein. Lumazine protein (LumP) is involved in the bioluminescence of certain marine bacteria. It serves as an optical transponder in bioluminescence emission. The intense fluorescence of LumP is caused by non-covalently bound 6,7- dimethyl-8-ribityllumazine. Though its amino acid sequence is very similar to riboflavin synthase it functions as a monomer, unlike the riboflavin synthases from eubacteria, yeasts and plants which act as trimers
MFKGIVQGTGIIEKISKNDDLQRHGINFPEDILEDVEKGTSIAVNGCSLTVVRISGDFVYFDIDQALNLT
TFRELKVGDRVNLERAPKFGEEVGSGLLTGIISGVAQVISIIENEDRLSVLIEIPKNLTENLDSKDLIGI
DGVSLSIDEISDNIIFINYPKELLITTNLGWRKKGDKVNVEILNMI
>gnl|CDD|293914 cd16257, EFG_III-like, Domain III of Elongation factor G (EF-G) and related proteins. Bacterial Elongation factor G (EF-G) and related proteins play a role in translation and share a similar domain architecture. Elongation factor EFG participates in the elongation phase during protein biosynthesis on the ribosome by stimulating translocation. Its functional cycles depend on GTP binding and its hydrolysis. Domain III is involved in the activation of GTP hydrolysis. This domain III, which is different from domain III in EF-TU and related elongation factors, is found in several translation factors, like bacterial release factors RF3, elongation factor 4, elongation factor 2, GTP-binding protein BipA and tetracycline resistance protein Tet
PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREYGVELVV
S
>gnl|CDD|293915 cd16258, Tet_III, Domain III of Tetracycline resistance protein Tet. Tetracycline resistance proteins, including TetM and TetO, catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA
PMLQTTIRPRKPEQRERLLDALTELSDEDPLLKYRVDSTTHEIILSLYGEVQMEVISALLEEKYGVEVEF
K
>gnl|CDD|293916 cd16259, RF3_III, Domain III of bacterial Release Factor 3 (RF3). The class II RF3 is a member of one of two release factor (RF) classes required for the termination of protein synthesis by the ribosome. RF3 is a GTPase that removes class I RFs (RF1 or RF2) from the ribosome after release of the nascent polypeptide. RF3 in the GDP state binds to the ribosomal class I RF complex, followed by an exchange of GDP for GTP and release of the class I RF. Sequence comparison of class II release factors with elongation factors shows that prokaryotic RF3 is more similar to EF-G whereas eukaryotic eRF3 is more similar to eEF1A, implying that their precise function may differ
PEHFRRVRLKDPMKAKQLRKGLEQLAEEGAVQVFRPMDGSDPIVGAVGPLQFEVLQARLENEYGVEVVFE
>gnl|CDD|293917 cd16260, EF4_III, Domain III of Elongation Factor 4 (EF4). Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis
PMVFAGLYPVDGSDYEELRDALEKLTLNDASVTFEPETSSALGFGFRCGFLGLLHMEVFQERLEREYGLD
LIITAP
>gnl|CDD|293918 cd16261, EF2_snRNP_III, Domain III of Elongation Factor 2 (EF2). This model represents domain III of Elongation factor 2 (EF2) found in eukaryotes and archaea, and the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis are important for the function of the U5-116 kD/Snu114p
PVVRVAVEPKNPSDLPKLVEGLKKLAKSDPTVQVKIEEEGEHLIAGAGELHLEICLKDLKEDFAGIEIKV
SD
>gnl|CDD|293919 cd16262, EFG_III, Domain III of Elongation Factor G (EFG). This model represents domain III of bacterial Elongation factor G (EF-G), and mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2), which play an important role during peptide synthesis and tRNA site changes. In bacteria, this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects, and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants of the yeast homolog of mtEFG2, MEF2
PEPVISLAIEPKTKADEDKLSKALARLAEEDPTLRVSRDEETGQTILSGMGELHLEIIVERLKREYGVEV
EVGKPQ
>gnl|CDD|293920 cd16263, BipA_III, Domain III of GTP-binding protein BipA (TypA). BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios. It is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion
PTVSMTFGVNTSPFAGREGKFVTSRKIRDRLEKELETNVALRVEETESPDSFIVSGRGELHLSILIETMR
REGFELQVS
>gnl|CDD|293921 cd16264, snRNP_III, Domain III of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component. Domain III of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p is homologous to domain III of the eukaryotic translational elongation factor EF-2. U5-116 kD is a GTPase component of the spliceosome complex which functions in the processing of precursor mRNAs to produce mature mRNAs
SVFKIAVEPLNPSELPKMLDGLRKVNKSYPLLITKVEESGEHVILGTGELYMDCVMHDLRKMYSEIEIKV
AD
>gnl|CDD|293910 cd16265, Translation_Factor_II, Proteins related to domain II of EF-Tu and related translation factors. Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2
GKFRVEKVFKILGRQVLTGEVESGVIYVGYKVKGDKGVALIRAIEREHRKVDFAVAGDEVALILEGKIKV
KEGDVLEVYQ
>gnl|CDD|293911 cd16266, IF2_aeIF5B_IV, Domain IV of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5. This family represents the domain IV of prokaryotic Initiation Factor 2 (IF2) and its archaeal and eukaryotic homologs IF5B. IF2, the largest initiation factor is an essential GTP binding protein. In E. coli three natural forms of IF2 exist in the cell, IF2alpha, IF2beta1, and IF2beta2. Disruption of the eIF5B gene (FUN12) in yeast causes a severe slow-growth phenotype, associated with a defect in translation. eIF5B has a function analogous to prokaryotic IF2 in mediating the joining of the 60S ribosomal subunit. The eIF5B consists of three N-terminal domains (I, II, II) connected by a long helix to domain IV. Domain I is a G domain, domain II and IV are beta-barrels and domain III has a novel alpha-beta-alpha sandwich fold. The G domain and the beta-barrel domain II display a similar structure and arrangement to the homologous domains in EF1A, eEF1A and aeIF2gamma
AKIRILPGCVFRQSKPAIVGVEVLEGTLKPGVPLIVPDGKDVGRVKSIQDNGENVKEAKKGQEVAVSIEG
PTVGRHIEEGDILYVDI
>gnl|CDD|293912 cd16267, HBS1-like_II, Domain II of Hbs1-like proteins. S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes
PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTG
IDPNHLRVGSILCD
>gnl|CDD|293913 cd16268, EF2_II, Domain II of Elongation Factor 2. This subfamily represents domain II of elongation factor 2 (EF-2) found in eukaryotes and archaea. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site
PLVMYVSKMVPTDKGAGFVAFGRVFSGTVRRGQEVYILGPKYVPGKKDDLKKKRIQQTYLMMGREREPVD
EVPAGNIVGLVGLDDFLAKSGTTTSS
>gnl|CDD|293879 cd16269, GBP_C, Guanylate-binding protein, C-terminal domain. Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines
GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAA
CEKEALEVFMKRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISQGSYSV
PGGYQLYLEDREKLVEKYRQVPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAA
EQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQA
ELLQEEIRSLK
>gnl|CDD|293878 cd16270, Apc5_N, N-terminal domain of the anaphase-promoting complex subunit Apc5 (or Anapc5). The N-terminal domain of Apc5 interacts with subunits Apc4, Apc15, and CDC23. Apc5 is a subunit of the eukaryotic anaphase-promoting complex/cyclosome (APC/C) which is a multi-subunit ubiquitin ligase that mediates the proteolysis of cell cycle proteins in mitosis and G1. Although Apc5 does not contain a classical RNA binding domain, it binds the poly(A) binding protein (PABP), which directly binds the internal ribosome entry site (IRES) of growth factor 2 mRNA. PABP was found to enhance IRES-mediated translation, whereas Apc5 over-expression counteracted this effect. In addition to its association with the APC/C complex, Apc5 binds much heavier complexes and co-sediments with the ribosomal fraction. The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC
PHKIAVLVLIKEYCRLKDSAWTLSPKERRDFCILLLKLIQGPDMTLKELIKLIEEVCYLPQLLDSFLERL
KLIAEEGIDDLLDFFDSLERLLSGSEEEVEPALLHKSSVLGLFLRRMLLAFNKLSFSQVVKLYKSFQQYY
ESG
>gnl|CDD|293830 cd16272, RNaseZ_MBL-fold, Ribonuclease Z; MBL-fold metallo-hydrolase domain. The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
LTFLGTGGAVPSLTRNTSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTL
LFARRYGGRKKPLTIYGPKGIKEFLEKLLNFPVEILPLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSV
ESLGYRIEAEGKSIVYSGDTGPCENLVELAKGADLLIHEC
>gnl|CDD|293831 cd16273, SNM1A-1C-like_MBL-fold, SNM1A, artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain. Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) and Saccharomyces cerevisiae Pso2 protein (PSOralen derivative sensitive 2, also known as SNM1, sensitive to nitrogen mustard 1), both proteins are 5'-exonucleases and function in interstrand cross-links (ICL) repair. Also includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein, and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
KSSKKKPKRKKPCPFYKIIPGTSFVVDAFKYGKIPGISAYFLSHFHSDHYGGLTKSWSHGPIYCSEITAN
LVKLKLKVDEEYIVVLPMNTPVEIDGDVSVTLLDANHCPGAVMFLFELPDGRRILHTGDFRANPEMLEHP
LLLGKRRIDTVYLDTTYCNP
>gnl|CDD|293832 cd16274, PQQB-like_MBL-fold, Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold metallo hydrolase domainhydrolase domain. PQQB is essential for the synthesis of the cofactor pyrroloquinoline quinone (PQQ) in Klebsiella pneumonia. PqqB is not directly involved in the PQQ biosynthesis but may serve as a carrier for PQQ when PQQ is released from PqqC. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
MRIKVLGSAAGGGFPQWNCNCPNCALARAGDGRATARTQSSIAVSADGENWVLINASPDIRQQIEATPEL
QPRPGLRDTPIAAVLLTDAEIDHTTGLLSLREGQPLTVYATAPVLEDLTTNFPFFVLLHAYGGVRRHRIL
PGEPFTLAGCPGLTVTPFPVPGKAPLYSEHRDAPEPGDTIGLRIEDGRTGGRLFYAPGCAAVTDELRARL
AGADCLLFDG
>gnl|CDD|293833 cd16275, BaeB-like_MBL-fold, Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain. Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
FVIRVKAGPMINYSYIIIDKATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAK
YDAPVYMSKEEIDYYGFRCPNLIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDSLFTGDTLFIEGC
GRCDLPGGDPEEMYESLQRLKKLPPPNTRVYPGH
>gnl|CDD|293834 cd16276, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
GVYWVTDGGYQSMFLVTDKGVIVVDAPPSLGENLLAAIRKVTDKPVTHVVYSHNHADHIGGASIFKDEGA
TIIAHEATAELLKRNPDPKRPVPTVTFDDEYTLEVGGQTLELSYFGPNHGPGNIVIYLPKQKVLMAVDLI
NPGWVPFFNFAGSEDIPGYIEALDELLEYDFDTFVGGHGNRLGTREDV
>gnl|CDD|293835 cd16277, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
VGDVTITRIVELIHSWLVRTPGRTILVDTGIGNDKPRPGPPAFHNLNTPYLERLAAAGVRPEDVDYVLCT
HLHVDHVGWNTRLVDGRWVPTFPNARYLFSRAEYDHWSSPDAGGPPNRGVFEDSVLPVIEAGLADLVDDD
HEILDGIRLEPTPGHTPGHVSVELESGGERALFTGDVMHHPIQVARPDWSSVFDEDPAQAAATRRRLLER
AADTDTLLFPAH
>gnl|CDD|293836 cd16278, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
GVRRVLAPNPSPMTLDGTNTYLLGAPDGVVVIDPGPDDPAHLDALLAALGGGRVSAILVTHTHRDHSPGA
ARLAERTGAPVRAFGPHRAGGQDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFT
GDHVMGWSTTVIAPPDGDLGDYLASLERLLALDDRLLLPGHGPPI
>gnl|CDD|293837 cd16279, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B)
MKLTFLGTGTSSGVPVIGCDCGVCDSSDPKNRRLRSSILIETGGKNILIDTGPDFRQQALRAGIRKLDAV
LLTHAHADHIHGLDDLRPFNRLQQRPIPVYASEETLDDLKRRFPYFFAATGGGGVPKLDLHIIEPDEPFT
IGGLEITPLPVLHGKLPSLGFRFGDFAYLTDVSEIPEESLEKLRGLDVLILDA
>gnl|CDD|293838 cd16280, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
KKGYVEPFQVFDNLYYVGNKWVSAWAIDTGDGLILIDALNNNEAADLIVDGLEKLGLDPADIKYILITHG
HGDHYGGAAYLKDLYGAKVVMSEADWDMMEEPPEEGDNPRWGPPPERDIVIKDGDTLTLGDTTITVYLTP
GHTPGTLSLIFPVKDGGKTHRAGLWGGTGLNTGPNLERREQYIASLERFKKIAEEAGVDVFLSNHPFQDG
SLEKREALRNRKPGEPNPFVDGQAWVDFYDEVLALCARVLA
>gnl|CDD|293839 cd16281, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
MQLHSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMRCLLIETGGRNILIDTGIGDKQDPKFR
SIYVQHSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGGATRADDDGLVELLFPNATYWVQKRHWEWAL
NPNPRERASFLPENIEPLEESGRLKLIDGSDAELGPGIRFHLSDGHTPGQMLPEISTPGGTVVFAADLIP
TSAHIPLPWVMGYDRRPLLTIEEKERLLDEAVEEGGRLFFEH
>gnl|CDD|293840 cd16282, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
GVYALIGPDGGGFISNIGFIVGDDGVVVIDTGASPRLARALLAAIRKVTDKPVRYVVNTHYHGDHTLGNA
AFADAGAPIIAHENTREELAARGEAYLELMRRLGGDAMAGTELVLPDRTFDDGLTLDLGGRTVELIHLGP
AHTPGDLVVWLPEEGVLFAGDLVFNGRIPFLPDGSLAGWIAALDRLLALDATVVVPGHGPVGDKADLRA
>gnl|CDD|293841 cd16283, RomA-like_MBL-fold, Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain. Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKR
LGGRPPYLVPLGLKKWFLKKGITNVVELDWWQSTEIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGE
GFRIYFAGDTGYFPGFREIGRRFGPIDLALLPIGAYEPRWF
>gnl|CDD|293842 cd16284, UlaG-like_MBL-fold, UlaG a putative l-ascorbate-6-P lactonase and related proteins; MBL-fold metallo hydrolase domain. UlaG is essential for L-ascorbate utilization under anaerobic conditions; it is a putative l-ascorbate-6-P lactonase thought to catalyze the hydrolysis of L-ascorbate-6-phosphate to 3-keto-L-gulonate-6-phosphate. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
TFAMWWLGCTGIWLKSEGNTNICIDFWCFVLDPFAIKQIDAVLATHDHNDHIDVNVAAAVLQNCAPDVPF
IGPQACVDLWIGWGVPKERCIVVKPGDVVKIKDIEIHVLDSFDRTALVTLPADQKLAGKMPDDMDERAVN
YLFKTPGGSLYHSGDSHYSNYYAKHGNDHKIDVALGSY
>gnl|CDD|293843 cd16285, MBL-B1, metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1
LRIRPLADNVWVHTSLAEFNGGAVPSNGLIVIDGKGLVLIDTPWTEAQTATLLDWIEKKLGKPVTAAIST
HSHDDRTGGIKALNARGIPTYATALTNELAKKEGKPVPTHSLKGALTLGFGPLEVFYPGPGHTPDNIVVW
LPKSKILFGGCLVKSASATSLGNVGDADVEAWPKSIENLKAKYPEARMVVPGHGAPGGTELLDHTLDLAK
>gnl|CDD|293844 cd16286, SPM-1-like_MBL-B1-B2-like, Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain. SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL
VDLPYNLTAREIDPDVFVITHRDPWSSNVLVVKMLDGTVVIVDSPYTNLATQTVLDWIAKTMGPRKVVAI
NTHFHLDGTGGNEALKKRGIPTWGSDLTKQLLLERGKADRIKAAEFLKNEDLKRRIESSPPVPPDNVFDL
KEGKVFSFGNELVEVSFPGPAHAPDNVVVYFPERKILFGGCMIKPGKELGNLGDANMKAWPDSVRRLKKF
DAKIVIPGHGERGDPGMVNKTIKVLE
>gnl|CDD|293845 cd16287, CphS_ImiS-like_MBL-B2, metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain. Includes Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis
LTLTHFKGPLYIVEDKEYVQENSMVYIGTDGITIIGATWTPETAETLYKEIRKVSPLPINEVINTNYHTD
RAGGNAYWKTLGAKIVATQMTYDLQKSQWGSIVNFTRQGNNKYPNLEKSLPDTVFPGDFNLQNGSIRAMY
LGEAHTKDGIFVYFPAERVLYGNCILKENLGNMSFANRTEYPKTLEKLKGLIEQGELKVDSIIAGHDTPI
HDVGLIDHYLTLLEKA
>gnl|CDD|293846 cd16288, BJP-1_FEZ-1-like_MBL-B3, BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain. This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His)
WNAPFEPFRIAGNVYYVGTSGLASYLITTPQGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAH
LDHAGGLAALKKLTGAKLMASAEDAALLASGGKSDFHYGDDSLAFPPVKVDRVLKDGDRVTLGGTTLTAH
LTPGHTRGCTTWTMTVKDDGKVYQVVFADSLTVNPGYKLVGNPTYPGIAEDYRHSFATLRALQCDIFLAS
HAEYFDLKEKRARLAAGQPNAFIDPEGYRNFIEKAKADFEKQLA
>gnl|CDD|293847 cd16289, L1_POM-1-like_MBL-B3, Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of L1- and Pom-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His)
WLQPMAPLQIADHTWYIGTESLTALLVKTPDGAVLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAH
ADHAGPLAALKRATGARVAANAESAVLLARGGSDDIHFGDGITFPPVQADRIVMDGEVVTLGGVTFTAHF
TPGHTPGSTSWTWTDTRDGKPVRIAYADSLSAPGYQLLGNPRYPRIVEDYRRTFATVRALPCDVLLTPHP
GASGWDYAAGAAPHAKPMTCKAYADAAEQ
>gnl|CDD|293848 cd16290, AIM-1_SMB-1-like_MBL-B3, AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain. This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of AIM-1-,SMB-1-, EVM-1-, THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His)
WNQPQAPFRIHGNTYYVGTGGLSAVLITSPQGLILIDGALPQSAPQIEANIRALGFRLEDVKLILNSHAH
FDHAGGIAALQRDSGATVAASPAGAAALRSGGVDPDDPQAGAADPFPPVAKVRVVADGEVVKLGPLAVTA
HATPGHTPGGTSWTWRSCEGGRCLDIVYADSLTAVSADGFRFSDDAHPARVAAFRRSIATVAALPCDILI
SAHPDASGLWEKLARRAREPGPNPFIDPNACRAYAAAAEARLEARL
>gnl|CDD|293849 cd16291, INTS11-like_MBL-fold, Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain. Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCG
ALPYFTEVVGYDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVD
DELEIKAYYAGHVLGAAMFYVRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES
>gnl|CDD|293850 cd16292, CPSF3-like_MBL-fold, cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain. CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALP
YFLQKTNFKGRVFMTHPTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKF
TAYNAGHVLGAAMFMVEIAGVRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES
>gnl|CDD|293851 cd16293, CPSF2-like_MBL-fold, cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; MBL-fold metallo-hydrolase domain. CPSF2, also known as cleavage and polyadenylation specificity factor 100 kDa subunit (CPSF-100), is a component of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. This subgroup includes Ydh1p, the yeast homolog of CPSF2. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
FTPLSGAGDESPLCYLLEIDDVTILLDCGWDESFDMEYLESLKRIAPTIDAVLLSHPDLEHLGALPYLVG
KLGLTCPVYATLPVHKMGRMFMYDLYQSRGLEEDFNLFTLDDVDEAFDRITQLKYSQPVNLRGKGDGLTI
TAYNAGHTLGGTIWKITKDSEDIVYAVDWNHKKERHLNGAVLDSFGGLRPSLLITDADN
>gnl|CDD|293852 cd16294, Int9-like_MBL-fold, integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain. Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
MKLYCLSGHPTLPCNVLKFKSTTIMLDCGLDCPPETELIDLSTVDVILISNYHCMLALPFITEYTGFTGV
VYATEPTVQIGRLLMEELVQALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISYVSG
SSVLTTHPQPMDQTSLKNSDVLILTG
>gnl|CDD|293853 cd16295, TTHA0252-CPSF-like_MBL-fold, Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain. Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFPFDPKEIDAVILTHAHLDHSGRLPL
LVKEGFRGPIYATPATKDLAELLLLDSAKIQEEEAEHPPAEPLYTEEDVEKALKHFRPVEYGEPFEIGPG
VKVTFYDAGHILGSASVELEIGGGKRILFSGDLGRKNTPLLRDPAPPPEADYLIMES
>gnl|CDD|293854 cd16296, RNaseZ_ELAC2-N-term-like_MBL-fold, Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase domain. The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. This eukaryotic subgroup includes the N-terminus of human ELAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLK
ETGLPKCVLSGPNKQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNFLVLKAKELGLPVGTAAIAPIIA
AVKDGKSITFEGREILAEELCTPPDPGIVFIVVEC
>gnl|CDD|293855 cd16297, artemis-SNM1C-like_MBL-fold, artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain. Includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Inactivation of Artemis causes severe combined immunodeficiency (SCID). Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
MSSFGGRMKEYPYISIDRFDRENLRARAYFLSHCHKDHMKGLRAPGLKRRLKASLKVKLYCSPVTKELLL
TNPKYAFWENHIVSLEIDTPTQISLVDEATGEKEDVVVTLLPAGHCPGSVMFLFQGNNGTVLYTGDFRLA
VGEAARMELLHSGDRVKDIQSVYLDTTFCDP
>gnl|CDD|293856 cd16298, SNM1A-like_MBL-fold, 5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain. Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) which is a 5'-exonuclease and functions in interstrand cross-links (ICL) repair. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions
SSTNGEGKRKKTCPFYKKIPGTGFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKFPIYCSKITGNL
VKSKLKVEEQYINVLPMNTECIVNGVKVVLLDANHCPGAVMILFRLPSGTLVLHTGDFRADPSMERYPEL
IGQKIHTLYLDTTYCSP
>gnl|CDD|293857 cd16299, IND_BlaB-like_MBL-B1, IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain. Includes the chromosome-encoded metallo-beta-lactamases Chryseobacterium indologenes IND-1, IND-2, and IND-7, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB, Chryseobacterium gleum CGB-1, and Empedobacter brevis EBR-1. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile
LKIEKLNDNLYIYTTYNEFNGVKYSANAMYLVTKKGVILFDTPWDKDQYQPLLDSIRKKHNLPVIAVIAT
HSHEDRAGGLGYFNKIGIPTYATAMTNSILKKENKPQATYLIETDKTYKIGGEKFVVYFFGEGHTADNVV
VWFPKEKVLDGGCLIKSAEATDLGYIGEANVKEWPKTIHKLKQKFKKAKVVIPGHDEWKDQGHIENTLKL
LN
>gnl|CDD|293858 cd16300, NDM_FIM-like_MBL-B1, NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain. Includes the ISCR-mediated MBLs NDM-1 (NDM (New Delhi metallo-beta-lactamase) and FIM-1 (Florence imipenemase). MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile
VVFRQLAPGVWMHTSYLDMPGFGAVPSNGLIVRDGDRVLLVDTAWTDDQTAQILNWAKQELNLPVRLAVV
THAHQDKMGGMDALHAAGIATYANALSNQLAPQEGLVPAQHSLTFAAEPSTAPNFPLKVFYPGPGHTRDN
IVVGIDGTGIAFGGCLIRPSKATSLGNLADADTEHWAASARAFGAAFPDASMIVPSHGAPDGRAAITHTA
RLAD
>gnl|CDD|293859 cd16301, IMP_DIM-like_MBL-B1, IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain. Includes the acquired MBLs IMP-1(a beta-lactamase that is active on imipenem), DIM-1 (Dutch imipenemase), GIM-1 (German imipenemase), KHM-1 (Kyorin Health Science MBL 1), SIM-1 (Seoul imipenemase), and TMB-1 (Tripoli metallo-beta-lactamase). IMP-1, DIM-1, GIM-1, SIM-1, and TMB-1 are Class 1 integron-mediated MBLs, KMH-1 is plasmid-mediated. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of acquired MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile
PKLKIEKLSDGVYLHTSYKEVEGWGLVDANGLVVVDGKEAYLIDTPWSESDTEKLVEWIKAQGLTLKASI
STHFHEDRTGGIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDEFWLLKGKIEVFYPGAGHTKDNL
VVWLPKEKILFGGCLVKSLESKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGDVSLLEHTRK
LAKKA
>gnl|CDD|293860 cd16302, CcrA-like_MBL-B1, Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile
LEIIKLSDHVYVHVSYLETETFGKVPCNGMIVINGGEAVVFDTPTNDSQSEELIDWIENSLKAKVKAVVP
THFHDDCLGGLKAFHRRGIPSYANQKTIALAKEKGLPVPQHGFSDSLTLKLGGKKIVCRYFGEGHTKDNI
VVYFPSEKVLFGGCMVKSLGAGKGNLEDANVEAWPKTVEKVKAKYPDVKIVIPGHGKIGGSELLDYTIDL
FK
>gnl|CDD|293861 cd16303, VIM_type_MBL-B1, VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain. VIM (Verona integron-encoded metallo-beta-lactamase)-type MBLs are integron-associated and are widely distributed acquired MBLs. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of VIM-type MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile
GEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELLLIDTAWGAKNTAALLAEIEKQIGLPVTRAV
STHFHDDRVGGVDVLRAAGVATYASPSTRRLAEAEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHST
DNLVVYVPSARVLYGGCAVRELSSTSAGNVADADLAEWPTSIERIQKHYPEAEFVIPGHGLPGGLDLLHH
TKNVVKAH
>gnl|CDD|293862 cd16304, BcII-like_MBL-B1, Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain. Bacillus cereus Beta-lactamase 2, also called BcII. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile
LEVTKLNKNVWVHTSYGLFNGTPVPSNGLIVETSKGVVLIDTPWDDEQTEELLDWIKKKLKKPVTLAIVT
HAHDDRIGGIKALQKRGIPVYSTKLTAQLAKKQGYPSPDGILKDDTTLKFGNTKIETFYPGEGHTADNIV
VWLPQSKILFGGCLVKSLEAKDLGNTADANLKEWPTSIRNVLKRYPNAEIVVPGHGEWGDKQLLRHTLDL
LK
>gnl|CDD|293863 cd16305, Sfh-1-like_MBL-B2, Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis
LTLTHFKGPLYIVEDKEYVQENSMVYIGTDGITIIGATWTPETAETLEKEIRKVSPLPIKEVINTNYHTD
RAGGNAYWKTLGASIVSTQMTYDLEKSQWGSIVDFTRQGNNKYPNLEKSLPDTVYPGDFNLQNGSVRALY
LGEAHTEDGIFVYFPAERVLYGNCILKEKLGNMSFANRTEYPKTLKKLKGLIEQGELKVESIIAGHDTPI
HDVELIDHYLTLLEKA
>gnl|CDD|293864 cd16306, CphA_ImiS-like_MBL-B2, Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis
MSLTQVSGPVYVVEDNYYVQENSMVYFGAKGVTVVGATWTPDTARELHKLIKRVSRKPVLEVINTNYHTD
RAGGNAYWKSIGAKVVSTRQTRDLMKSDWAEIVAFTRKGLPEYPDLPLVLPNVVHDGDFTLQEGKVRAFY
LGPAHTPDGIFVYFPDEQVLYGNCILKEKLGNLSFADVKAYPQTLERLKAMKLPIKTVIGGHDSPLHGPE
LIDHYEALIKAA
>gnl|CDD|293865 cd16307, FEZ-1-like_MBL-B3, Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of FEZ-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His)
WTTPFPPFRIAGNLYYVGSRDLASYLITTPRGNILINSNLESSVPQIKASIEKLGFKFSDTKILLISHAH
FDHAAGSALIKRETHAKYMVMDGDVDVVESGGKSDFFYGNDPSTYFPPAHVDKVLHDGEQVELGGTVLTA
HLTAGHTKGCTTWTMKVKDHGKTYDVVIVGSPNVNPGAKLVNNITYPGIAEDYAHTFAVLRSLPCDIFLG
AHGGYFDLKNKYVRLQKGGANPFIDPEGYKAYVAEKEQAFRTELE
>gnl|CDD|293866 cd16308, GOB1-like_MBL-B3, Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of GOB-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His)
WSQPYAPFRIAGNLYYVGTYDLACYLIVTPKGNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAH
YDHVGAMAAIKQQTGAKMMVDEKDAKVLADGGKSDYEMGGYGSTFAPVKADKLLHDGDTIKLGGTKLTLL
HHPGHTKGSCSFLFDVKDEKRTYRVLIANMPTILPDTKLSGMPGYPGIAKDYAYTFEAMKALSFDIWLAS
HASQFDLHQKHKPGAPYNPAAFADRAGYDKALAGLEKSYDKKIK
>gnl|CDD|293867 cd16309, BJP-1-like_MBL-B3, Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of BJP-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His)
WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAH
FDHAGGLAELKKATGAQLVASAADKPLLESGYVGSGDTKNLQFPPVRVDRVIGDGDKVTLGGTTLTAHLT
PGHSPGCTSWTTTVKDTAGPPREVLFFCSATVAGNQLVGPPTYPGIVDDYRATFAKARAMKADVFLANHP
EFFGLVAKRARQSAGEPDAFVDAGELQRFNTKMEDDFEKALA
>gnl|CDD|293868 cd16310, Mbl1b-like_MBL-B3, Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His)
WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAH
YDHAGGLAQLKADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATL
TPGHTKGCTTWSTTVKENGRPLRVVFPCSLSVAGNVLVGNKTYPTIVEDYRASFARLRAMKADIVLTSHP
EVADLLARKAKQDAGQANAFVDPGELARIVDQSEAAFNKELA
>gnl|CDD|293869 cd16311, THIN-B2-like_MBL-B3, Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of THIN-B2-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His)
WNADQAPFRIFGNTYYVGVKGLSSVLVTSPQGHVLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGH
IDHAGGLAELQRRSGALVAASPSAALDLASGEVGPDDPQYHALPKYPPVKDMRLARDGGQFNVGPVSLTA
HATPGHTPGGLSWTWQSCDGPRCLNMVYADSQNAVSRPGFKFSASSEYPNAVADLRRSFETLEKLPCDVL
ISAHPEASQLWERLEASDRSARPALVDREACRRYASRAREALEKRIA
>gnl|CDD|293870 cd16312, THIN-B-like_MBL-B3, Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His)
WNQPVKPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAH
WDHAGGIAALQKASGATVAASAHGAQVLQSGTNGKDDPQYQAKPVVHVAKVAKVKEVGEGDTLKVGPLRL
TAHMTPGHTPGGTTWTWTSCEGQRCLDVVYADSLNPYSSGDFYYTGKGGYPDISASFRASIAKVAALPCD
IIIAVHPGFTDVLDKAKRRSGDTNPFIDAEACRAYAAGAAKSLEKRLA
>gnl|CDD|293871 cd16313, SMB-1-like_MBL-B3, SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of SMB-1- and THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His)
WNAPQEPFQIYGNTYYVGTGGISAVLITSPQGHILIDGGFPKSPEQIAASIRQLGFKLEDVKYILSSHDH
WDHAGGIAALQKLTGAQVLASPATVAVLRSGSMGKDDPQFGGLTPMPPVASVRAVRDGEVVKLGPLAVTA
HATPGHTTGGTSWTWQSCEQGRCANMVFADSLTAVSADGYRFSAHPAVLADVEQSIAAVEKLACDILVSA
HPEFSDMWTRVKRGAAEGNAAFIDGGGCRAYAAKAREKLNKRLA
>gnl|CDD|293872 cd16314, AIM-1-like_MBL-B3, Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup AIM-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His)
WDDPAPPRRIYGNTWYVGTCGISALLVTSDAGHILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEH
FDHAGGIARLQRATGAPVVAREPAATTLERGRSDRSDPQFLVVEKFPPVASVQRIGDGEVLRVGPLALTA
HATPGHTPGGTSWTWRSCEGAVCRDMVYADSVTAISDDIYRYSDHPGMVAAFRNTLDTVAALPCDILVTP
HPSASGLWERLGPAAGIPLADTGACRAYAQTGRARLDARLADEAA
>gnl|CDD|293873 cd16315, EVM-1-like_MBL-B3, Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup EVM-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His)
WDKPAPPARIFGNTYYVGTCGISAILITGDDGHVLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEH
FDHVGGLAALQRATGARVAASAAAAPVLESGKPAPDDPQAGLHEPFPPVRVDRIVEDGDTVALGSLRLTA
HATPGHTPGALSWTWRSCEGADCRTIVYADSLSPVSADGYRFSDHPDYVAAYRAGLAKVAALPCDILLTP
HPSASDMFERLSGGAPLADPDACAAYAAGAEKRLDERL
>gnl|CDD|293874 cd16316, BlaB-like_MBL-B1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain. Includes the chromosome-encoded MBL Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related MBLs. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile
LKISHLTGDLYVYTTYNTYKGTKTAANAVYVVTDKGVVVIDAPWDETQFQPFLDSIQKKHHKKVIMNIAT
HSHDDRAGGLEYFGKKGAKTYTTKLTDSILKKNNKPRAEYTFDNDTTFKVGKYEFQVYYPGKGHTADNIV
VWFPKEKVLYGGCLIKSADAKDLGYLGEAYVNDWTQSIHNIQQKFPNPQYVIAGHDDWKDQTSLQHTLKL
ISEY
>gnl|CDD|293875 cd16317, IND_MBL-B1, Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain. Includes the chromosome-encoded MBLs Chryseobacterium indologenes IND-1, IND-2, and IND-7 and related MBLs. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile
DFVIEPPIKPNLYIYKTFGVFGGKEYSANAVYLVTKKGVVLFDVPWQKVQYQSLMDTIQKRHHLPVIAVF
ATHSHDDRAGDLSFYNNKGIKTYATAKTNEFLKKDGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADN
VVVWFPKYKVLDGGCLVKSNSATDLGYTGEANVEQWPKTMNKLKAKYAQATLIIPGHDEWKGGGHVEHTL
DLLNK
>gnl|CDD|293876 cd16318, MUS_TUS_MBL-B1, Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain. Includes the chromosome-encoded MBLs Myroides odoratimimus MUS-1 and related MBLs. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile
LKIKQLNDNMYIYTTYQEFQGVTYSSNSMYVLTDEGVILIDTPWDKDQYEPLLEYIRSNHNKEVKWVITT
HFHEDRSGGLGYFNSIGAQTYTYALTNEILKERNEPQAQFSFNKEKQFTFGNEKLAVYFLGEGHSLDNTV
VWFPKEEVLYGGCLIKSAEATTIGNIADGNVIAWPKTIEAVKQKFKNAKVIIPGHDEWDMSGHIENTERI
LSAY
>gnl|CDD|293782 cd16319, MraZ, protein domain of unknown function (UPF0040) includes MraZ. This family contains proteins of unknown function (UPF0040), implicated in a cellular function of bacterial cell division. It includes protein MraZ which is present in almost all bacteria and appears to be essential for survival. It is found in gene clusters associated with the cellular function of cell division and cell wall biosynthesis. Members of this family contain two tandem copies of the domain; the crystal structure of a member of this family (MPN314) reveals that the two subdomains are related by a pseudo two-fold axis, with each subdomain containing a highly conserved DXXXR sequence motif in close proximity to each other, suggested to form the functional site
AFFIDLDAAGRILIPAKLIADAELDGEIVIIGGFEDCLEIRDKKDFEDYFANF
>gnl|CDD|293783 cd16320, MraZ_N, N-terminal subdomain of transcriptional regulator MraZ. This family contains the N-terminal domain of proteins of unknown function (UPF0040), implicated in a cellular function of bacterial cell division. It includes protein MraZ which is present in almost all bacteria and appears to be essential for survival. It is found in gene clusters associated with the cellular function of cell division and cell wall biosynthesis, including mraW, ftsI, murE, murF, ftsW and murG. Members of this family contain two tandem copies of the domain; the crystal structure of a member of this family (MPN314) reveals that the two subdomains are related by a pseudo two-fold axis, with each subdomain containing a highly conserved DXXXR sequence motif in close proximity to each other, suggested to form the functional site
LGTYEHKLDAKGRLSIPAKFREELGAGGEGLVLTRGLDGCLELYPLEEWEKLEEKLEALP
>gnl|CDD|293784 cd16321, MraZ_C, C-terminal subdomain of transcriptional regulator MraZ. This family contains the C-terminal domain of proteins of unknown function (UPF0040), implicated in a cellular function of bacterial cell division. It includes protein MraZ which is present in almost all bacteria and appears to be essential for survival. It is found in gene clusters associated with the cellular function of cell division and cell wall biosynthesis, including mraW, ftsI, murE, murF, ftsW and murG. Members of this family contain two tandem copies of the domain; the crystal structure of a member of this family (MPN314) reveals that the two subdomains are related by a pseudo two-fold axis, with each subdomain containing a highly conserved DXXXR sequence motif in close proximity to each other, suggested to form the functional site
RALLRLFLGGAEEVELDKQGRILLPQRLREYAGLEKEVVFVGVGDRFEIWDPERWEAYLAEA
>gnl|CDD|293877 cd16322, TTHA1623-like_MBL-fold, uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain. Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode
VRPFTLGPLQENTYLVADEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHP
GAPVYLHPDDLPLYEAADLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEE
EGLLFSGDLLFQGSIGRTDLPGGDPKAMAASLRRLLTLPDETRVFPGHGPPTTLGEERRTNPFL
>gnl|CDD|319993 cd16323, Syd, Syd, a SecY-interacting protein. This family contains the Syd protein that has been implicated in the Sec-dependent transport of polypeptides across the inner membrane in bacteria. Syd has been shown to bind the SecY subunit of membrane-embedded SecYEG heterotrimer (also known as core translocon or SecY complex) which is a conserved protein-conducting channel essential for the biogenesis of most of the secretory and integral membrane proteins. The SecY-binding site of Syd is a conserved concave and electronegative groove that forms interactions with the electropositive loops of the SecY subunit. Syd is also known to verify the proper assembly of the SecY complex in the membrane by interfering with protein translocation only when the channel displays abnormal SecY-SecE associations. Operon analysis has shown that Syd protein may function as immunity protein in bacterial toxin systems
KQALEQFFERYIQAWQEQLGSLPKTEYDEEWPSPCEGEEDEEGYVYWQPVEREPPADFSNLEQALEITLH
PDIKAFYGSYYAGDLPATFQGGELELLQVWNEDDFERLQQNLIGHLLMKRRLKQPPTLFIGLTDDDDLLI
SVDNETGEVWLEDVGKEPHEVLADSLAEFLSQL
>gnl|CDD|319982 cd16324, LolA_fold-like, family containing periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the periplasmic protein RseB. This family contains the periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the N-terminal domain of periplasmic protein RseB, all of which have similar unclosed beta-barrel structures that resemble a baseball glove-like scaffold consisting of an 11-stranded antiparallel sheet. There are five Lol proteins (LolA, LolB, LolC, LolD, and LolE) involved in the sorting and membrane localization of lipoprotein and are highly conserved in Gram-negative bacteria. LolA accepts outer membrane (OM)-specific lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB. It is proposed that the LolA/LolB complex forms a tunnel-like structure, where the hydrophobic insides of LolA and LolB are connected, which enables lipoproteins to transfer from LolA to LolB. RseB exerts a crucial role in modulating the stability of RseA, the transmembrane anti-sigma-factor that is degraded during sigma-E-dependent transcription caused by bacterial envelope stress. Its structural similarity to LolA and LolB suggests that RseA may act as a sensor of periplasmic stress with a dual functionality, detecting mislocalized lipoproteins as well as propagating the signal to induce the sigma-E-response
QWSARFSFRVTGPSGGAQEADGRLKAIPPRDLARILFTQPDALADNEVVSDGKEVWNYLPLTNQVTTQPL
AKATIPGLGLLFSTIAGDTSLLSDQYDVKLDGTEVIPGGEARKLVGTPKDNDAGFATVTVWIDKASWRPL
RMQLLDGDGGQLADLNFSNFKT
>gnl|CDD|319983 cd16325, LolA, LolA, a periplasmic chaperone. This family contains periplasmic molecular chaperone LolA which binds to outer-membrane specific lipoproteins and transports them from inner membrane to outer membrane (OM) through LolB, a lipoprotein anchored to outer membranes. There are five Lol proteins (LolA, LolB, LolC, LolD, and LolE) involved in the sorting and membrane localization of lipoprotein and are highly conserved in Gram-negative bacteria. LolA accepts OM-specific lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB. Studies have shown that hydrophobic surface patches large enough to accommodate acyl chains of the OM lipoproteins and the structural flexibility of LolA are important factors for its role as a periplasmic chaperone
LDRLQAKLASIKTLSADFTQTVTDAGLKKPQTSSGTLYLKRPGKFRWEYTKPEEQLIVSDGKTLWIYDPD
LEQVTISSLDDALSSTPLALLSGYKKGLLFEVVFVVKKDGKAWVLELTPKDKDSGFKKITLTFDKDTGLL
RSIEIVDAQGDRTTITFSNIKLNPKL
>gnl|CDD|319984 cd16326, LolB, LolB, an outer membrane lipoprotein receptor. This family contains the outer membrane lipoprotein receptor, LolB, which catalyzes the last step of lipoprotein transfer from the inner to the outer membrane. There are five Lol proteins (LolA, LolB, LolC, LolD, and LolE) involved in the sorting and membrane localization of lipoprotein and are highly conserved in Gram-negative bacteria. LolA transports lipoproteins through the periplasm to LolB, which then localizes them to outer membranes; the protruding loop of LolB has been shown to be essential for the localization of lipoproteins in the anchoring of bacterial triacylated proteins to the outer membrane
QAHQAQLAQLQQWQLSGRLAVRTPDDGGSANFDWQQQGDRYQLRLSGPLGQTVARLEGDPGGATLTTSDG
KTYTADDAEALLQQLLGWSLPVSGLRYWVRGLPAPAPAALEADAQGRLGRLEQDGWQIEYSDYQDVDGLA
LPRRIELTRGDLRIKLVIDQWQL
>gnl|CDD|319985 cd16327, RseB, RseB, a sensor in periplasmic stress. This family contains the periplasmic protein RseB (also known as MucB or Mucb/RseB) which exerts a crucial role in modulating the stability of RseA, the transmembrane anti-sigma-factor that is degraded during sigma-E-dependent transcription caused by bacterial envelope stress. RseB binds to RseA and inhibits its sequential cleavage, thereby functioning as a negative modulator of this response. The protein is composed of two domains, the larger N-terminal domain resembling an unclosed beta-barrel that is remarkably similar structurally to LolA and LolB, proteins capable of binding the lipid anchor of lipoproteins, suggesting that RseA acts as a sensor of periplasmic stress with a dual functionality, detecting mislocalized lipoproteins as well as propagating the signal to induce the sigma-E-response
SAEQWLERMAQAARQLNYEGTFVYQRGGRLESLRIVHAVDDGGEYERLESLDGPPREVLRRGDEVSCFLP
GDEPVSVESRRILGPFPALLPSDLERLADYYDFRLGGRERVAGRPAQVIRLVPKDDLRYGYRLWLDRETG
LLLKSDLLDEDGEVLEQFQFTSLEIG
>gnl|CDD|319992 cd16328, RseA_N, N-terminal domain of RseA. This family contains the cytoplasmic (N-terminal) domain of RseA, the transmembrane anti-sigma-E factor. RseA is degraded during sigma-E-dependent transcription caused by bacterial envelope stress such as heat shock. It is an inner membrane protein with an N-terminal cytoplasmic domain that binds sigma-E and blocks its transcriptional activity, and a C-terminal periplasmic domain that binds RseB, an auxiliary negative regulator. Under inducing conditions, RseA is rapidly degraded and sigma-E is released into the cytoplasm, where it can bind core RNAP and induce its regulon. It has been shown that just the N-terminal domain is sufficient to bind and inhibit sigma-E. The C-terminal domain may interact with other proteins that signal periplasmic stress
KEQLSALMDGELDELELDRLLADLDSDPELRATWQRYHLIGDVLRGELLAAASADFAARVAAALA
>gnl|CDD|319986 cd16329, LolA_like, proteins similar to periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the periplasmic protein RseB. This family contains uncharacterized proteins similar to the periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the periplasmic protein RseB, all of which have similar unclosed beta-barrel structures that resemble a baseball glove-like scaffold consisting of an 11-stranded antiparallel sheet. There are five Lol proteins (LolA, LolB, LolC, LolD, and LolE) involved in the sorting and membrane localization of lipoprotein and are highly conserved in Gram-negative bacteria. LolA accepts outer membrane (OM)-specific lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB. It is proposed that the LolA/LolB complex forms a tunnel-like structure, where the hydrophobic insides of LolA and LolB are connected, which enables lipoproteins to transfer from LolA to LolB. RseB exerts a crucial role in modulating the stability of RseA, the transmembrane anti-sigma-factor that is degraded during sigma-E-dependent transcription caused by bacterial envelope stress. Its structural similarity to LolA and LolB suggests that RseA may act as a sensor of periplasmic stress with a dual functionality, detecting mislocalized lipoproteins as well as propagating the signal to induce the sigma-E-response
SAEEILEKVDDRRRGDSSADVSTMTLTDKNGKERTRELRVYSKDGGDDKSLIRFLSPADVKGTAFLTLDY
DDKDDDQWLYLPALRRVRRISSSDKSQSFMGSDFSYEDLSRSRLLEDYTYKLLGEEEVDGRDCYVLELTP
KDGADSGYSKRVLWVDKDTFLPLKAEYYDRSGKLLKTLTFSDIKKIGGYWRPTRMEMKDLLTGHKTVLEY
SDIKFNVGLPDSLFT
>gnl|CDD|319987 cd16330, LolA_VioE, Proteins similar to violacein biosynthetic enzyme VioE that shares fold with periplasmic molecular chaperone LolA. This family includes the violacein biosynthetic enzyme VioE which shares a core fold with lipoprotein transporter proteins that include lipoprotein transporter proteins LolA and LolB. VioE is an enzyme with no characterized homologs that plays a key role in the biosynthesis of violacein, a naturally occurring bisindole product with various biological activities, including antitumor activity as well as antibacterial and cytotoxic properties. In Chromobacterium violaceum, VioE catalyzes the third step in violacein biosynthesis from a pair of Trp residues (i.e. mediates a 1,2 shift of an indole ring and oxidative chemistry) to generate prodeoxyviolacein, a precursor to violacein. Structural and mutagenesis studies suggest that VioE acts as a catalytic chaperone, using this fold associated with lipoprotein transporters to catalyze the production of its prodeoxyviolacein product
EPPLLPAQWSSSYVSYWSPMLGDDQLTSGYCWFDYERNVCRIDGLFNPWSEKETGHRLWMSEVGQPGSGE
TWKQKVAYAREGTALGEQLCARPLDDEVDPFHELFLPRDVLVRHGARHVGRRVVLGREADGWRYERPGKG
PSTYYFDAGTNHLLRMVTGDPNSHASIRDFPNFSE
>gnl|CDD|319991 cd16331, YjgA-like, uncharacterized proteins similar to Escherichia coli YjgA. Family of conserved uncharacterized proteins similar to Escherichia coli YjgA, which has been identified as comigrating with the 50S ribosome
RPSKSQLKREAHALQDLGEELVELSPAQLAKLPLPEELREAILEAKRIKSHEARRRQLQYIGKLMRDEDP
EAIRAALDALKNGSRAENARFHRLERWRDRLIAEGDAALTELLAEYPDADRQQLRQLIRNARKEREANKP
PKASRELFRYLRE
>gnl|CDD|381747 cd16332, Prp-like, ribosomal-processing cysteine protease Prp and similar proteins. This model represents a family of cysteine proteases that include members found to cleave the N-terminus extension of ribosomal subunit L27 in eubacteria. Proteins in this family are distinguished by a pair of invariant histidine and cysteine residues with conserved spacing that form the classic catalytic dyad of a cysteine protease. Dependence of Staphylococcus aureus on L27 cleavage by Prp makes the enzyme a target for antibiotic development
MIKVTIYRKNDKIVGFEISGHAGYAEYGKDIVCAAVSALVITTVNSLEELLGDKPDVEVDEGGYLSVELP
DSDDEKAQLLLETLLLGLKSIEEQYPKYIKIK
>gnl|CDD|319989 cd16333, RELM, resistin-like molecule (RELM) hormone family. RELMs, secreted proteins with roles including insulin resistance and the activation of inflammatory processes, are also known as found in inflammatory zone (FIZZ), and include four members in mouse (RELM-alpha/FIZZ1/HIMF, RELM-beta/FIZZ2, Resistin/FIZZ3, and RELM-gamma/FIZZ4) and two members in human (resistin and RELM-beta). Little is yet known about the differences and similarities in function of the different isoforms. RELMs are potentially implicated in a wide range of physiological and pathological processes including obesity-associated diabetes, cardiovascular system function, cancer development and metastasis. There are significant differences between human and rodent RELMs with respect to gene and protein structure, differential gene regulation, different tissue distribution profiles, and insulin resistance induction. Resistin appears to convey insulin resistance in rodents, and to instigate inflammatory processes in humans. In the pathophysiology of obesity-associated diabetes, mouse resistin is secreted by adipocytes and increases hepatic gluconeogenesis, thereby promoting insulin resistance, human resistin is secreted by macrophages and may play a role through inflammatory contributions. Elevated levels of human resistin have been reported in various cancers including colorectal, endometrial, and postmenopausal breast cancers, and may initiate the production of further inflammatory cytokines, to promote tumor cell progression; contrary to this, in vitro overexpression of human RELM-beta abolishes invasion, metastasis and angiogenesis of gastric cancer cells. Resistin circulates as hexamers and trimers; structural similarity has been noted between the resistin homotrimer and the proprotein convertase subtilisin/kexin type 9, C-terminal cysteine-rich domain
CSIESVVDKKIKEALSSLEPRPSVNKTLSCTSVKSRGRLASCPAGYAVTGCACGYGCGSWDIRTGTTCHC
QCAGIDWTAARCCKLV
>gnl|CDD|319988 cd16334, LppX-like, family includes lipoproteins LppX, LprA, LprF and LprG from Mycobacterium tuberculosis. This family includes the homologous lipoproteins LppX, LprA, LprF and LprG from Mycobacterium tuberculosis (Mtb), all of which share a core fold with lipoprotein transporter proteins LolA and LolB. Mtb contains components such as glycolipids, lipoglycans and lipoproteins that play critical roles in regulating host responses and promoting survival of the pathogen. Mtb LprA is a lipoprotein agonist of Toll-like receptor 2 (TLR2) that regulates innate immunity and APC function. LprF, which is also found in Mycobacterium bovis but not in the nonpathogenic Mycobacterium smegmatis, has a central hydrophobic cavity that binds a diacylated glycolipid that it transfers from the plasma membrane to the cell wall, which might be related to the pathogenesis of the bacteria. Similarly, LprG functions as a carrier of glycolipids and lipoglycans, such as lipoarabinomannan (LAM), during their trafficking and delivery to the mycobacterial cell wall, contributing to virulence; LAM inhibits fusion of phagosomes with lysosomes as a means for mycobacteria to evade host defense. In addition, LprG has potent TLR2 agonist activity that modulates antigen processing of dendritic cells and macrophages. LppX is required for the translocation of the key virulence factors, the phthiocerol dimycocerosates (PDIMs), to the surface of Mtb
GTGPLPDAAALLAAAAAATRALTSVHFTLTVSGKPPGLPVRSAEGDLTRTPAGAAKGTATVQLGGQLVEV
EFVVVGGTLYAKGPTGGYQDLGPAQAGIYDPSALLDPERGLANLLASATDPKTEGRETVDGVDTYRVTGT
VPADAVAGLVPGVDTGDVPVTVWIAKGDHRLVRATLTVPPFNGGTVTLTLSDYNKP
>gnl|CDD|319981 cd16335, MukF_N, bacterial condensin complex subunit MukF, N-terminal domain. MukF is part of the MukBEF condensin complex that is mainly found in proteobacteria and is involved in chromosome organization and condensation. The complex is believed to serve as a part of the chromosome scaffold rather than a bulk DNA packing protein. MukE and MukF form a stable complex with each other and dynamically associate with MukB, a member of the SMC protein family. MukEF does not bind DNA on its own but modulates MukB-DNA activity. The stoichiometry of the MukEF complex is MukE4F2
AWLLRRGLSLDLGPDDLAFLAAIHAWAEDEVDPEFDEEELRDIFRYVDELFGGDSDTTDKRANNAINRLV
EQRLLSRADGSGVNREGEYRLTPLAHDIVEYFIDDRELTRESLSLLLGRIRGELAELLAAARAAGDEEEW
RAEVVAPLRPTVKDLLEGIDRRQRGLDAQQQQLRAEIASLLSQDWFAAIDQCEELLQETAGTLRDLQDLL
LASADKLLALLLEIQEAAEQAGPEEAQNAVQDLQDQLDRIRAWGNQRLRDWSEYHRRVHRFIRTVIRLDP
NRALRQRLRDAIRRFDEHPWSLRIASADPLLRLRE
>gnl|CDD|319980 cd16336, MukE, bacterial condensin complex subunit MukE. MukE is part of the MukBEF condensin complex that is mainly found in proteobacteria and is involved in chromosome organization and condensation. The complex is believed to serve as a part of the chromosome scaffold rather than a bulk DNA packing protein. MukE and MukF form a stable complex with each other and dynamically associate with MukB, a member of the SMC protein family. MukEF does not bind DNA on its own but modulates MukB-DNA activity. The stoichiometry of the MukEF complex is MukE4F2
QYNTLADVIADPLFPEVDLRLRRGRHIDRDDLDLYAFLNDAQDLLEEFYRRYGVELVQAPEGYFYLRPQR
RTLLGRRHLSELEMLVGQTLALMYLDPETLEQSGWITRDALLERLEGLLGEERLLELLNRRRGGDTRDDA
KKVREVVRKALRLLRRLGFIRLGNDAARFRPTAALMRFIEPVRGLADPREALERLVRLGEVGLL
>gnl|CDD|319979 cd16337, MukF_C, bacterial condensin complex subunit MukF, C-terminal domain. MukF is part of the MukBEF condensin complex that is mainly found in proteobacteria and is involved in chromosome organization and condensation. The complex is believed to serve as a part of the chromosome scaffold rather than a bulk DNA packing protein. MukE and MukF form a stable complex with each other and dynamically associate with MukB, a member of the SMC protein family. MukEF does not bind DNA on its own but modulates MukB-DNA activity. The stoichiometry of the MukEF complex is MukE4F2
LPEELEFEEMTDLEDQLKELIEEMLEDFKPVGGPLDLGEVLREYLAQYPPYRHFDVARLLVDQAVRLGHA
QEDQSAIQPEWVPINDYGAEVEAHVID
>gnl|CDD|319976 cd16338, CpcT, T-type phycobiliprotein (PBP) lyase. This family contains the T-type phycobiliprotein (PBP) lyase (includes CpcT/CpeT, also known as CpcT bilin lyase). PBP lyases are employed by cyanobacteria, red algae, cryptophytes and glaucophytes for light-harvesting. Pigmentation of light-harvesting phycobiliproteins of cyanobacteria and cryptophytes requires covalent attachment of open-chain tetrapyrrole chromophores, the phycobilins, to the apoproteins. PBP lyases mediate this covalent attachment of phycobilin chromophores to apo-PBPs and also ensure the correct binding of the chromophore with regard to the specific attachment site and stereospecificity. The T-type lyase is distantly related to CpcS and is responsible for covalent attachment of phycocyanobilin (PCB) or phycoerythrobilin to a specific cysteine residue in the beta-subunit of phycocyanin (CpcB) and the beta-subunit of phycoerythrocyanin (PecB), and with a different stereochemistry than CpcS. In CpcT (All5339) from Nostoc (Anabaena) sp. PCC7120, sequential binding studies indicate that beta-subunit chromophorylation with PCB at a specific C- terminal cysteine residue in cyanobacterial phycocyanin and phycoerythrocyanin is hindered by a preceding chromophorylation at a specific N-terminal cysteine residue by CpcS. T-type PBP lyases adopt a beta-barrel structure with a modified lipocalin fold, similar to S-type PBP lyases
AELAQWLAGEFSNQEQAAADPPWFAHIRLWTRPLPVEALGGYWLYVEQAYAGDPDKPYRQRVLRLTPDPD
GAIRLENYTLKDPERFAGAWRDPERLATLTPDDLELLPGCDLILRRQGKGRFRGSTPPGGCRFNVKGGAT
YLTSTFELSKDEFWSWDRGFDATGEQVWGAEAGPYEFRRV
>gnl|CDD|319977 cd16339, CpcS, S-type phycobiliprotein (PBP) lyase. This family contains the S-type phycobiliprotein (PBP) lyase (denoted CpcS/CpcU or CpeS/CpeU). PBP lyases are employed by cyanobacteria, red algae, cryptophytes and glaucophytes for light-harvesting. Pigmentation of light-harvesting phycobiliproteins of cyanobacteria and cryptophytes requires covalent attachment of open-chain tetrapyrrole chromophores, the phycobilins, to the apoproteins. PBP lyases mediate this covalent attachment of phycobilin chromophores to apo-PBPs and also ensure the correct binding of the chromophore with regard to the specific attachment site and stereospecificity. The S-type lyase is distantly related to CpcT and similarly adopts a beta-barrel structure with a modified lipocalin fold. Many members of the CpcS/CpcU family ligate phycocyanobilin (PCB) to a specific cysteine residue in the beta-subunits of phycocyanin (CpcB) or phycoerythrocyanin (PecB) and to a related cysteine residue in the alpha and beta subunits of allophycocyanin (AP); they are typically given the designation of "CpcS" or "CpcU". Other members which attach phycoerythrobilin (PEB) to the beta-subunit of phycoerythrin (PE) are given the designation "CpeS" or "CpeU". In Guillardia theta, a Cryptophyte, which has adopted phycoerythrobilin (PEB) biosynthesis from cyanobacteria, phycobiliprotein lyase has been shown to provide structural requirements for the transfer of this chromophore to the specific cysteine residue of the apophycobiliprotein
EFFELSAGKWFSQRTTHHLAWHQSERGKSELTIELLEADDPEVVQLCQQHGIDPTAALGGAKVSWDGSSD
WGKPKQTGSTLLVLLPDPDNPNTGKLLRDRGYAEARPVVGRYRLGEDGALTLTTEYGGTSSEERIWFASP
NLRLRTSIVKRADGVSQASFCSEIRR
>gnl|CDD|319978 cd16340, CpcS_T, S- and T-type phycobiliprotein (PBP) lyases. This family contains the S- and T-type phycobiliprotein (PBP) lyases. PBP lyases are employed by cyanobacteria, red algae, cryptophytes and glaucophytes for light-harvesting. Pigmentation of light-harvesting phycobiliproteins of cyanobacteria and cryptophytes requires covalent attachment of open-chain tetrapyrrole chromophores, the phycobilins, to the apoproteins. PBP lyases mediate this covalent attachment of phycobilin chromophores to apo-PBPs. These lyases are distinguishable in the clades of E/F-, S/U-, and T-type lyases; T-type lyases (which include CpcT) are distantly related to S-type lyases (which include CpcS and CpcU). S- and T-type PBP lyases differ in mechanistic details; the conformation and protonation state in which the chromophore is presented account for their differences in stereochemistry of the chromophore selectivity as well as corresponding binding sites. On the other hand, both lyases carry out the main functions of assisting site selectivity in the apo-PBP, protecting the chromophore and ensuring the regio- and stereoselectivity of the addition. The S- and T-type PBP lyases adopt a beta-barrel structure with a modified lipocalin fold
TFFRWSAGDWSSQRQSHENAFAQPEYAHSRVCIRPLPWDDSEFLDICKTYNFEPELAGVGFRVSWAGDYX
WENEDPYGSTVLVLXIDEGDRGKLLRYTGYQEENPPGGNXIVEWDGKGTLETGYGKTYLEERFWFAEPEL
RIRLSIGKDLETDGHIWASPFYEVRL
>gnl|CDD|319975 cd16341, FdhE, formate dehydrogenase accessory protein FdhE and similar proteins. This family contains formate dehydrogenase accessory protein FdhE and FdhE-like protein, found largely in gamma- and some beta-Proteobacteria, where the fdhE genes are almost always genetically-linked to the structural genes for formate dehydrogenases. FdhE is required for the assembly of formate dehydrogenase although not present in the final complex. In E. coli, FdhE interacts with the catalytic subunits of the respiratory formate dehydrogenases. Purification of recombinant FdhE demonstrates the protein is an iron-binding rubredoxin that can adopt monomeric and homodimeric forms. E. coli FdhE interacts with the catalytic subunits, FdnG and FdoG, of the Tat- dependent respiratory formate dehydrogenases. Site-directed mutagenesis has shown that conserved cysteine motifs are essential for the physiological activity of the FdhE protein and are also involved in Fe(III) ligation. The iron likely is redox active, suggesting that the switch from aerobic to anaerobic conditions may be important in modulating FdhE function. Alternatively, FdhE may be involved in an electron transfer reaction, similar to other rubredoxins
AEYLDFFAELAEAQAELLAALAPLALPDADALARAREAGMPLLARADLPIDPEAWRAALRALLAALAEAG
ELPEAARALLAALAAADDDLEALARALLAGDDAAFEALAEELGLDPAALAFLLAAALQPFLAALAAALAA
ALLALPWQKGYCPVCGSPPVASVLRGGGEEGLRYLHCSLCGTEWHFVRIKCPFCGNTDPEKLSYFTLEGE
PAYRAEVCDKCKGYLKTVDLRKDPRELDPVADDLATLHLDLLAQEEG
>gnl|CDD|319974 cd16342, FusC_FusB, Fusidic acid resistance protein (FusC/FusB). The fusidic acid resistance protein FusC (FusB) mediates resistance to the antibiotic fusidic acid. Its C-terminal domain, which contains a zinc-binding site, interacts with EF-G with high affinity, promoting the dissociation of stalled ribosome#EF-G#GDP complexes that form in the presence of fusidic acid, thus allowing the ribosomes to resume translation
RNHQYNFIKKQVKQLVNAYSTVNDPKVLEAVKALALEKILELFPELTEEQKELLEPILDVKDEEEAEKFL
EELKPYVIPFPQVTEKQIKKLFPKVKKLKLPDLEEIDLRELTYLGWNDIGSNRKYIVYELDGKLIGIEGT
FSPSNKKGICAICNRHSEVGLFTAKTKGSGDGTYTKRGNYICLDSEKCNQNITDLDKLEDFIET
>gnl|CDD|319971 cd16343, LMWPTP, Low molecular weight protein tyrosine phosphatase. Low molecular weight protein tyrosine phosphatases (LMW-PTP) are a family of small soluble single-domain enzymes that are characterized by a highly conserved active site motif (V/I)CXGNXCRS and share no sequence similarity with other types of protein tyrosine phosphatases (PTPs). LMW-PTPs play important roles in many biological processes and are widely distributed in prokaryotes and eukaryotes
KKILFVCLGNICRSPMAEAVLRHLLPKAGGDDVEVDSAGTSAWHGGEPPDPRARAVLKEHGIDLSGHRAR
QLTAEDFDEFDLILAMDESNLRDLRRLAPAEARGKVFLLGDFDPEGGKDVPDPYYGGREGFEEVYDLIER
ACEGLLE
>gnl|CDD|319972 cd16344, LMWPAP, low molecular weight protein arginine phosphatase. Low molecular weight protein arginine phosphatases are part of the low molecular weight phosphatase (LMWP) family. They share a highly conserved active site motif (V/I)CXGNTCRS. It has been shown that the conserved threonine, which in many LMWPTPs is an isoleucine, confers specificity to phosphoarginine over phosphotyrosine
MKILFVCTGNTCRSPMAEAILKKLLEELDVEVKSAGIFAVDGSPASPNAVEVLKEKGIDLSGHRSQQLTE
ELLEWADLILTMTESHKQALLSLYPEAADKVFTLKEYVGGEDGDISDPFGGSLEVYRQTAEELEELIEKL
LK
>gnl|CDD|319973 cd16345, LMWP_ArsC, Arsenate reductase of the LMWP family. Arsenate reductase plays an important role in the reduction of intracellular arsenate to arsenite, an important step in arsenic detoxification. The reduction involves three different thiolate nucleophiles. In arsenate reductases of the LMWP family, reduction can be coupled with thioredoxin (Trx)/thioredoxin reductase (TrxR) or glutathione (GSH)/glutaredoxin (Grx)
KVLFLCTGNSARSQMAEALLRHLGGDRFEAYSAGSEPAGVNPLAIEVMKEIGIDISGQRSKSLDEFLGQE
FDYVITVCDNAAEVCPVFPGAVKRLHWGFPDPAAAEGSEEEKLEAFRRVRDEIKERIEALLA
>gnl|CDD|319957 cd16347, VOC_like, uncharacterized subfamily of the vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
AQALNMALFADLLQRVPSGRRYVEEVAAGGRKVVFDHGALRTVRAAGGGALPAGEAAFTRILEPLGYTLA
GVYPLPRLKMTGRAYRHIDDPENIPQFFVSELHVEQFSPEFQQAVTRVVGQSPALADYEALLAESAEMAW
IATEGNAFNHATDRVADVEALAEALRALGRPIKDKVEVSASGRVRQTAFRADKVTRLFRGADGGQVEREV
PGSFYEFITRD
>gnl|CDD|319958 cd16348, VOC_YdcJ_like, uncharacterized metal-dependent enzyme similar to Shigella flexneri YdcJ. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
DELRARFSAAMSAMYRAEVPLYGDLLDLVAEVNADVLARDPALRERLERTGELARLGVERHGAIRLGTAE
ELATIRRLFAVMGMHPVGYYDLSVAGVPVHSTAFRPIDSEALAKNPFRVFTSLLRLELIEDADLRARAEE
ILARRQIFTPRLLELLDIAEAQGGLTEAQAEEFVAEALETFRWHGEATVSLEEYEALHAEHPLIADIVCF
KGPHINHLTPRTLDIDAVQQAMAARGIPAKDVIEGPPRRKCPILLRQTSFKALEEPVRFVGADGSLVPGT
HTARFGEIEQRGAALTPKGRALYDRLLAEA
>gnl|CDD|319959 cd16349, VOC_like, uncharacterized subfamily of the vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
GTVSRAELAQALNMALFADLLDRVPSGRRYVEEVLARGEKVVFDHGALRTVRWPGTGALPAGEAAFTRIL
EPLGYTLAGVYPLPRLKMTGRAYRHADLPETIAQFFVSELHPEQFSPAFQAAVTRVVGTSRDPLTPEAKA
LLARLEADGSLPLADAAALLPVLVGCFARQHGVPALADYEALLAESAEMAWIATEGNAFNHATDRVADVE
ALAEEQRALGRPIKDKVEVSASGRVRQTAFRADSVKRQFRDADGTVVEREVPGSFYEFITRDRDPDEPGT
GRLDLRFDSGNAQGIFKMTAA
>gnl|CDD|319960 cd16350, VOC_like, uncharacterized subfamily of the vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
LDALFDQLWQDYLQRTPQARKIHDLLEEKGETVINDHIAFRTFNLPGLGIASLAKIFLALGYERRGEYHF
PEKKLRARHYEHPDPTLPKIFISELLVEELSPEAQEIIRKLVAQIPPDALLEPLLFLSGRPWPLPSYEDY
EALLKESEYAAWVLAHGYRANHFTVSVNHLKKFNDLEKVNQFLKEAGFKLNSSGGEIKGSPDGLLEQSST
LADKVEVTFADGGEYEIPSCYYEFAERYPLPDGKLYQGFVAASA
>gnl|CDD|319750 cd16351, CheB_like, methylesterase CheB domain family. This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain, a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. CheB family members may also contain an N-terminal regulatory (REC) domain, which blocks the active site of the C-terminal domain until it is phosphorylated, or a CheR domain; typically cheB and cheR occur in the same operon. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR
IVGIGASTGGLEALEHLFEQLPIHSGLVYVVIQHMPPGFTSSMAERLGKKTKVGVKEAEDGEPVEPGTIY
IAPGDTHINLENGKGFKVQELSNDTGINNLRPPVDHFFSSLAKYNKEKSIAVILTGMGNDGSSGLSYVYD
TGGTVIAQTEESCVVFGMPNYAIQTGKVDHVVRPEEMASLFEQI
>gnl|CDD|319352 cd16352, CheD, chemotaxis protein CheD stimulates methylation of methyl-accepting chemotaxis proteins. This family contains bacterial chemotaxis protein CheD that stimulates methylation of methyl-accepting chemotaxis proteins (MCPs). The CheD chemotaxis gene is not found in the Escherichia coli genome, but is present in many other organisms, including B. subtilis, where CheD appears to have two separate roles; it binds to chemoreceptors to activate them as part of the CheC/CheD/CheYp adaptation system, and it deamidates selected residues to activate chemoreceptors, enabling them to mediate amino acid chemotaxis. CheD has been shown to catalyze amide hydrolysis of specific glutaminyl side chains of the B. subtilis chemoreceptors McpA, McpB and McpC; deamination by CheD is required for the chemoreceptors to effectively transduce signals to the CheA kinase. CheD's ability to bind the receptors is controlled by CheC via a competitive binding mechanism; substituting Gln into the receptor motif of the signal-terminating phosphatase, CheC, turns the inhibitor into a receptor-modifying deamidase CheD substrate. Also, CheYp increases the affinity of CheD for CheC, controlling CheD binding to the receptors through its interactions with CheC. Thus, high levels of CheYp means CheC is a better binding target for CheD than the receptors, resulting in decreased CheA activity. The CheD structure reveals a distant homology with a class of bacterial toxins represented by the cytotoxic necrotizing factor 1 (CNF1) as well as a class of proteins of unknown function represented by B. subtilis YfiH. An invariant Cys-His pair forming a catalytic dyad is observed, and is required by the toxins for deamidation activity
EIFVGPGEYYVSRGPTVLSTLLGSCVAVCLYDPVAKIGGMNHFMLPESSGDKEASNPGKYADTAIELLLN
ELLKLGARRSRLEAKLFGGANMFPGSSGLLNIGERNIEAARELLAKEGIPIVAEDVGGNYGRTVRFDPAT
GEVLVK
>gnl|CDD|381732 cd16353, CheC_CheX_FliY, CheC/CheX/FliY (CXY) family phosphatases. The CXY family includes CheY-P-hydrolyzing proteins that function in bacterial chemotaxis, which involves cellular processes that control the movement of organisms toward favorable environments via rotating flagella, which in turn determines the sense of rotation by the intracellular response regulator CheY. When phosphorylated, CheY-P interacts directly with the flagellar motor, and this signal is terminated by the CXY family of phosphatases (Escherichia coli uses CheZ). CheC acts as a weak CheY-P phosphatase but increases activity in the presence of CheD. Bacillus subtilis has only CheC and FliY while many systems also have CheX. CheC and CheX appear to be primarily involved in restoring normal CheY-P levels, whereas FliY seems to act on CheY-P constitutively. Unlike CheC and CheX, FliY is localized in the flagellar switch complex, which also contains the stator-coupling protein FliG and the target of CheY-P, FliM. CheC, CheX, and FliY phosphatases share a consensus sequence ([DS]xxxExxNx(22)P) with four conserved residues thought to form the phosphatase active site. CheC class I and FliY each have two active sites, while CheC class II and III, and CheX have only one. This family also includes FliM, a component of the flagellar switch complex and a target of CheY, which lacks the phosphatase active site consensus sequence, and is not a CheY phosphatase
QEIGNIFGGAAATTLSGRLRTGIEPEVGSPDQVKYEEVIRDVMIPSVVVVVGITGGIEGSAILEMRKDLA
YKVLDIXMGGPGEPNRPLDEIELSAVGEEGNNMLGLLAQALSDFGQTFDISPPNVEIGPQFVIIDNPEEI
VLLVPFSVSWEEFTSFFYVCWS
>gnl|CDD|319961 cd16354, BAT, Bleomycin N-Acetyltransferase and similar proteins. BlmB, encodes a bleomycin N-acetyltransferase, designated BAT, which inactivates Bm using acetyl-coenzyme A (AcCoA). BAT forms a dimer structure via interaction of its C-terminal domains in the monomers. The N-terminal domain of BAT has a tunnel with two entrances: a wide entrance that accommodates the metal-binding domain of Bm and a narrow entrance that accommodates acetyl-CoA (AcCoA). A groove formed on the dimer interface of two BAT C-terminal domains forms the DNA-binding domain of Bm. In a ternary complex of BAT, BmA(2), and CoA, a thiol group of CoA is positioned near the primary amine of Bm at the midpoint of the tunnel and ensures efficient transfer of an acetyl group from AcCoA to the primary amine of Bm. BAT belongs to vicinal oxygen chelate (VOC) superfamily that is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including thiocoraline, bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
VEPVLPVRDVAATLDLLEAVLGARVGFEVGDPPEFAGAVLGPWSVGPGLRLVATPGGPIAPVTLHLDAGV
EFDSLHRRALAAGARVDGPPVRQPWGRREFVLRLPEGHRLVVSG
>gnl|CDD|319962 cd16355, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
LTPVLNVSDIPASFAWFEKVLGFQKDWDWGDPPTFGSVGSGECEIFLCQGGQGGSLRLGPCGDALPSYGA
WMSVWVDDVDALHRECRARGADIRQPPTDMPWGMREMHVRHPDGHRFRVGQ
>gnl|CDD|319963 cd16356, PsjN_like, Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme and similar proteins. Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme and similar proteins. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
YVNIFTADIVALSDFYSELFGLEEIFEIRSPIFRGLRTGDSCLGFNAPEAYELLGLPEFSDTPGIRILLT
FDVDDVEAVDRLVPRAAALGATLIKPPYDTYYGWYQAVLLDPEGNVFRI
>gnl|CDD|319964 cd16357, GLOD4_C, C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins. Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
KVSLAVSDLEKSIDYWSDLLGMKVFEKSEKSALLGYGEDQAKLELVDIPEPVDHGTAFGRIAFSCPADEL
PPIEEKVKAAGQTILTPLVSLDTPGKATVQVVILADPDGHEICF
>gnl|CDD|319965 cd16358, GlxI_Ni, Glyoxalase I that uses Ni(++) as cofactor. This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event
MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAY
GHIAIGVEDVYETCERIRKKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI
>gnl|CDD|319966 cd16359, VOC_BsCatE_like_C, C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily. Uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
GHIHLRVSDLKAASHFYHQVLGFDIKSRRPGALFLSAGGYHHHIGLNTWAGRGLPLPPEDATGLAYFTIV
LPDQEALAAILERLDLAGYDVEALDDGLELTDPWGITVKF
>gnl|CDD|319967 cd16360, ED_TypeI_classII_N, N-terminal domain of type I, class II extradiol dioxygenases. This family contains the N-terminal non-catalytic domain of type I, class II extradiol dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site; extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon, whereas intradiol enzymes cleave the aromatic ring between two hydroxyl groups. Extradiol dioxygenases are classified into type I and type II enzymes. Type I extradiol dioxygenases include class I and class II enzymes. These two classes of enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. The extradiol dioxygenases represented in this family are type I, class II enzymes, and are composed of the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. A catalytically essential metal, Fe(II) or Mn(II), presents in all the enzymes in this family
YAELGVPDLEKALEFYTDVLGLQVAKRDGNSVYLRGYEDEHHSLVLYEAPEAGLKHFAFEVASEEDLERA
AASLTALGCDVTWGPDGEVPGGGKGFRFQDPSGHLLELFVE
>gnl|CDD|319968 cd16361, VOC_ShValD_like, vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein. This subfamily of vicinal oxygen chelate (VOC) family protein includes Streptomyces hygroscopicus ValD protein and similar proteins. ValD protein functions in validamycin biosynthetic pathway. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping
GVNHVGITVPDLDAAVEFYTDVLGAEVVYRSTPLAEGDRGGGEMRAAGFVPGFARARIAMLRLGPGPGIE
LFEYKGPEQRAPVPRNSDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLRDPW
GTLIELVSHP
>gnl|CDD|319969 cd16362, TflA, Toxoflavin Lyase. Toxoflavin lyase (TflA) is metalloenzyme degrading toxoflavin at the presence of oxygen, Mn(II), and dithiothreitol. TflA is structurally homologous to proteins of the vicinal oxygen chelate superfamily. The structure of TflA contains fold that displays a rare rearrangement of the structural modules indicative of domain permutation. Moreover, unlike the 2-His-1-carboxylate facial triad commonly utilized by vicinal oxygen chelate dioxygenases and other dioxygen-activating non-heme Fe(II) enzymes, the metal center in TflA consists of a 1-His-2-carboxylate facial triad. Toxoflavin is an azapteridine that is toxic to various plants, fungi, animals, and bacteria
SQLTLYAPNLERSLAFYTNFLGAQHVHESNDAFTVLLNVSSIQLVAAAEGTASSPFYHIAINISANHFQE
GKAALSGGGELLTENDEDQNASSCYVEDPSGNLIELIGRA
>gnl|CDD|319897 cd16363, Col_Im_like, inhibitory immunity (Im) protein of colicin (Col) deoxyribonuclease (DNase) and pyocins. This family contains inhibitory immunity (Im) proteins that bind to colicin endonucleases (DNases) or pyocins with very high affinity and specificity; this is critical for the neutralization of endogenous DNase catalytic activity and for protection against exogenous DNase bacteriocins. The DNase colicin family (ColE2, ColE7, ColE8 and ColE9) in E. coli, and pyocin family (S1, S2, S3 and AP41) in P. aeruginosa, are potent bacteriocins where the immunity proteins (Ims) protect the colicin/pyocin producing (i.e. colicinogenic) bacteria by binding and inactivating colicin nucleases. The binding affinities between cognate and non-cognate nucleases by Im proteins can vary up to 10 orders of magnitude
KNKLSDYTESEFLELVEEIFNADYGSEEELDDLLDHFEKITEHPAGSDLIFYPEDGADDSPEGIVEEVKE
WRAANGLPGFK
>gnl|CDD|409301 cd16364, T3SC_I-like, class I type III secretion system (T3SS) chaperones and similar proteins. This family contains class I type III secretion system (T3SS) chaperones mainly found in Gram-negative bacteria such as Pseudomonas, Yersinia, Salmonella, Escherichia and Erwinia, among others. A wide variety of these bacterial pathogens and symbionts require a T3SS to inject eukaryotic host cells with effector proteins important for suppressing host defenses and establishing infection. Many of these effector proteins interact with specific type III secretion chaperones prior to secretion. These T3SS chaperones have been classified as class I type III secretion chaperones (T3SC), which are small structurally conserved dimers that interact specifically with T3SS effector proteins. Class I T3SC consists of two subclasses: IA and IB. Class IA T3SC binds a single effector, whereas class IB T3SC binds to several effectors. Class IA and Class IB T3SCs typically exhibit little sequence similarities, but share a common overall heart-shaped structure fold (alpha-beta-beta-beta-alpha-beta-beta-alpha) and features, such as a small size, an acidic pI and an amphipathic C-terminal alpha-helix. Chaperone protein CesT serves a chaperone function for the enteropathogenic Escherichia coli (EPEC) translocated intimin receptor (Tir) protein, which confers upon EPEC the ability to alter host cell morphology following intimate bacterial attachment. In Pseudomonas aeruginosa, chaperone ExsC binds small secreted protein ExsE as well as the non-secreted anti-activator protein ExsD; it relieves repression of the transcriptional activator ExsA (which activates expression of T3SS genes) by ExsD. P. aeruginosa SpcU binds the cytotoxin ExoU, which is a broad-specificity phospholipase A2 (PLA2) and lysophospholipase, and maintains the N-terminus of ExoU in an unfolded state which is required for secretion. Salmonella enterica chaperone SicP forms a complex with effector protein SptP at an early stage of its secretion process in order to avoid premature degradation, while chaperone SigE binds to effector SigD, which, upon translocation into the host cell, preferentially dephosphorylates specific inositol phospholipids that are thought to be crucial for subsequent activation of the host cell Ser-Thr kinase Akt. This family also includes Yersinia chaperone/escortee pairs SycE/YopE, SycH/YopH, SycT/YopT and SycN+YscB/YopN, all of which bind to specific Yersinia outer proteins (Yops). Also included are several DspF and related sequences from several plant pathogenic bacteria. The "disease-specific" (dsp) region next to the hrp gene cluster of Erwinia amylovora is required for pathogenicity but not for elicitation of the hypersensitive reaction. In addition, a group of proteins including Escherichia coli YbjN, Erwinia amylovora AmyR, and their homologs, are included in this family. They share a class I T3SC-like fold with T3SS chaperone proteins but appear to function independently of the T3SS
LLAELGQELGLPLLALDEDGVCSLTFDGDEVTIELEEDDDRLLLYAVLGPLPPDDREALLLLLLEANLFG
QGTGGATLGLDPDTGELVLSRRLPLAGLDAEELEAALERFVEAAEAW
>gnl|CDD|319887 cd16365, NarH_like, beta FeS subunits DMSOR NarH-like family. This subfamily contains beta FeS subunits of several DMSO reductase superfamily, including nitrate reductase A, ethylbenzene dehydrogenase and selenate reductase. DMSO Reductase (DMSOR) family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. . The beta subunits of DMSOR contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Nitrate reductase A contains three subunits (the catalytic subunit NarG, the catalytic subunit NarH with four [Fe-S] clusters, and integral membrane subunit NarI) and often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Ethylbenzene dehydrogenase oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. Selenate reductase catalyzes reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor
KQFAAVFNLNKCIGCQTCTVACKNAWTYRKGQEYMWWNNVETKPGGGYPQDWEVKTIDNGGNTRFFFYLQ
RLCNHCTNPACLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRI
EGGDPTRCMSACVGRIRLQGFLDDNPKSPVTKLIRHWKVALPLHPEYGTEPNIYYVPPRWA
>gnl|CDD|319888 cd16366, FDH_beta_like, beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins. This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate
FLVDTSRCTGCRACQVACKQWNGLPAEKTEFTGSYQNPPDLTAHTWTLVRFYEVEKPGGDLSWLFRKDQC
MHCTDAGCLAACPTGAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGL
QPACVKTCPTGALTFG
>gnl|CDD|319889 cd16367, DMSOR_beta_like, uncharacterized subfamily of DMSO Reductase beta subunit family. This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system
FLVDYGLIQGTNLLVIDLDRCIRCDNCEKACADTHDGHSRLDRNGLRFGNLLVPTACRHCVDPVCMIGCP
TGAIHRDDGGEVVISDACCGCGNCASACPYGAIQMVRAVKCDLCAGYAGPACVSACPTGAAIRVNPEE
>gnl|CDD|319890 cd16368, DMSOR_beta_like, uncharacterized subfamily of DMSO Reductase beta subunit family. This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system
LATLIDLTKCDGCPGESIPACVRACREKNQARFPEPVSKPIQPYWPRKRIEDWSDKRDVTDRLTPYNWLY
VQKLTVDTAGGEKEVFIPRRCMHCDNPPCAKLCPFGAARKTPEGAVYIDDDLCFGGAKCRDVCPWHIPQR
QAGVGIYLHLAPEYAGGGVMYKCDLCKDLLAQGKPPACIEACPKGAQYFGPRKEMVALAR
>gnl|CDD|319891 cd16369, DMSOR_beta_like, uncharacterized subfamily of DMSO Reductase beta subunit family. This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system
EKEFFIDPSRCIGCRACVAACRECGTHRGKSMIHVDYIDRGESTQTAPTVCMHCEDPTCAEVCPADAIKV
TEDGVVQSALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPMCASVCPSGALFYGTR
EEIQALRPGSTPVNTFVFGPQEVETRVHIMLP
>gnl|CDD|319892 cd16370, DMSOR_beta_like, uncharacterized subfamily of DMSO Reductase beta subunit family. This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system
KRLRVKDMERCIGCYSCMLACSRRVHKSASLSKSAIRVRTRGGLEGGFTVVVCRACEDPPCAEACPTGAL
EPRKGGGVVLDKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHCGYCARYCPHDVLAMEE
>gnl|CDD|319893 cd16371, DMSOR_beta_like, uncharacterized subfamily of DMSO Reductase beta subunit family. This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system
GFYFDQERCIGCKACEIACKDKNDLPPGVNWRRVYEYEGGEFPEVFAYFLSMSCNHCENPACVKVCPTGA
ITKREDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRALDFG
>gnl|CDD|319894 cd16372, DMSOR_beta_like, uncharacterized subfamily of DMSO Reductase beta subunit family. This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system
KLLVTDPEKCIGCLQCEEACSKTFFKEEDREKSCIRITETEGGYAINVCNQCGECIDVCPTGAITRDANG
VVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIACGICVKACPTGALELVE
>gnl|CDD|319895 cd16373, DMSOR_beta_like, uncharacterized subfamily of DMSO Reductase beta subunit family. This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system
LRPPGALDEEEFLALCIRCGLCVEACPTGVIQPAGLEDGLEGGRTPYLDPREGPCDLCCDACVEVCPTGA
LRPLDLEEQKVKMGVAVIDKDRCLAWQGGTDCGVCVEACPTEAIAIVLEDDVLRPVVDEDKCVGCGLCEY
VCPVEPPKAIVVEP
>gnl|CDD|319896 cd16374, DMSOR_beta_like, uncharacterized subfamily of DMSO Reductase beta subunit family. This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system
VYVDPERCIGCRACEIACAREHSGKPRISVEVVEDLASVPVRCRHCEDAPCMEVCPTGAIYRDEDGAVLV
DPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLPACVEACPTGALKFGDIEELLKEKR
>gnl|CDD|319867 cd16375, Avd_IVP_like, proteins similar to the diversity-generating retroelement protein bAvd. A superfamily of four-helix bundles that form homopentamers, including the bacterial accessory variability determinant (bAvd) protein and a family of functionally uncharacterized bacterial proteins, some of which are encoded by an atypically large intervening sequence present within some 23S rRNA genes
AVEDSEELIEMLYPITESFPDQEHGGAREQFLKALLGQPELFAEGAARNQSRFLSAADAGLAELDFQLQF
AAGIGASTPEDDESAQRLIAEVFAILGALIAAL
>gnl|CDD|319868 cd16376, Avd_like, diversity-generating retroelement protein bAvd and similar proteins. The bacterial accessory variability determinant (bAvd) protein, together with a reverse transcriptase, is involved in retrohoming processes as part of a diversity-generating retroelement (DGR), a type of system that is involved in generating sequence variation in bacterial proteins by inserting coding information from a template region into a variable region of a protein coding gene. bAvd forms homopentamers and interacts with the reverse transcriptase as well as with DNA and/or RNA
IYKKTYDLLKYLYPILKKFPKSERYTLGQRIENLALDLLELIIEANKSPKREKLPLLREADVKLELLKFL
LRLAYELKLISNKKYEVLSEKLDEIGKMLGGWIKSL
>gnl|CDD|319869 cd16377, 23S_rRNA_IVP_like, 23S rRNA-intervening sequence protein and similar proteins. A family of functionally uncharacterized bacterial proteins, some of which are encoded by an atypically large intervening sequence present within some 23S rRNA genes. The distantly related bAvd protein, which also forms a homopentamer of four-helix bundles, has been suggested to interact with nucleic acids and a reverse transcriptase
IVWQKAHELVLEIYKLTKKFPKEERYGLTSQIRRAAVSIPSNIAEGFGRRSKKEFLRFLYIARGSLAELE
TQLILAKDLGYISEEEFEELLELLEEIGKMLNGLIKSL
>gnl|CDD|319866 cd16378, CcmH_N, N-terminal domain of cytochrome c-type biogenesis protein CcmH and related proteins. Cytochrome c-type biogenesis protein CcmH is a membrane-anchored thiol-oxidoreductase that is essential in the maturation of c-type cytochromes. CcmH consists of an N-terminal catalytic domain with the active site CXXC motif and a C-terminal domain of unknown function which is predicted to contain TPR-like repeats. Other members of this family include NrfF, CycL, and Ccl2
QEARARELAKELRCPVCQNQSLADSNAPIARDLRAEIREMLAEGKSDEEILDYLVARYGEFVLYAPP
>gnl|CDD|319863 cd16379, YitT_C_like, C-terminal domain of Bacillus subtilis YitT and similar protein domains. This domain, found in various bacterial proteins, has no known function. It has been given the designation DUF2179 and occurs at the C-terminus of the Bacillus subtilis membrane protein YitT as well as in single-domain proteins
YKTVRIISDKSEEILAEILRELGRGVTILDGEGGYGGERKVLYIVVKRKELPKLKKIIKEIDPKAFITIE
DVREVLGGGF
>gnl|CDD|319864 cd16380, YitT_C, C-terminal domain of Bacillus subtilis YitT and similar protein domains. This domain, found in various bacterial proteins, has no known function. It has been given the designation DUF2179 and occurs at the C-terminus of the Bacillus subtilis membrane protein YitT
GFNQAKAVMIISDKSEEIAEAILEELGRGVTILKGEGGYTGEEKKVLYCVVSRRELVKLKRIVKEIDPKA
FVIVSDVHEVLGEGF
>gnl|CDD|319865 cd16381, YitT_C_like_1, Proteins similar to the C-terminal domain of Bacillus subtilis YitT. This domain, characteristic of various bacterial proteins, has no known function. It has been given the designation DUF2179 and is similar to the C-terminus of the Bacillus subtilis membrane protein
GYVLVRVITREDAEELAEALREEGFGVTVVDGEGRDGPVLILFIVVKRKDLKELLKIIKEYDPKAFYTIE
DVRSVSGGYF
>gnl|CDD|341357 cd16382, XisI-like, XisI is FdxN element excision controlling factor protein. This family contains XisI proteins, also known as FdxN element excision controlling factors, and similar proteins. FdxN element is excised from the chromosome during heterocyst differentiation in cyanobacteria. This is accomplished by the large serine recombinase XisF (fdxN element site-specific recombinase). The xisH as well as the xisF and xisI genes are required. XisI may function as recombination directionality factor (RDF), and needs XisH which may function as an endonuclease
LTKYRQIIKQILQEYAKLPPSYGDIETQLIFDDERDHYLLLRVGWDGDRRVHGCLIHIDIKDGKIWIQRD
GTEDGIAEELVEAGIPKEDIVLGFHPPEVRQYTGFAV
>gnl|CDD|319862 cd16383, GUN4, porphyrin-binding protein domain GUN4. GUN4 is a porphyrin-binding protein involved in chlorophyll biosynthesis regulation and intracellular signaling, found in aerobic photosynthetic organisms. It has been implicated in retrograde signalling between the chloroplast and nucleus. GUN4 can bind protoporphyrin IX (PIX) and magnesium protoporphyrin IX (MgPIX), substrate and product of the Mg-chelatase, as well as heme and cobalt protoporphyrin IX (CoPIX). It may play a role in protecting plants from reactive oxygen species (ROS)-mediated damage
SEVGIDYTKLRDLLAAGKWKEADEETARLMLKIAGREKEGWLDFEDIENFPCEDLRTIDQLWVKYSNGRF
GFSVQKQIWQSLGGKLDYDYEDWEKFGDRVGWRKNGSWLSYDELTFSLDAPKGHLPALGWLGGGGGGRLL
LL
>gnl|CDD|319760 cd16384, VirB8_like, virulence protein VirB8. This family contains bacterial virulence protein VirB8 and similar proteins which consist of cytoplasmic, transmembrane, and periplasmic regions. VirB8 is an essential assembly factor of type IV secretion system (T4SS) channel proteins that are highly diverse in function relative to other bacterial secretion systems. T4SS proteins are important virulence factors for many Gram-negative pathogens, such as Agrobacterium, Brucella, Legionella, and Helicobacter. This family also includes the conjugal transfer protein family TrbF, a family of proteins known to be involved in conjugal transfer. The TrbF protein is thought to compose part of the pilus required for transfer. This domain has a similar fold to the nuclear transport factor-2 (NTF2) protein
EVVHASVLAFYVDLRETYDIDTIQRAYDMLSNNSATAVAQEYFNSSEASNPRDFKLAETQRVNVEIISVI
PQSPGTWQVRWLEKVYDRQGHLTEPPFKMRATLRYYNVPTTQSEEQRLNNPLGIYITSYSWSK
>gnl|CDD|319861 cd16385, IcmL, inner membrane protein IcmL/DotI. This family contains the periplasmic domain of the inner membrane protein DotI of the Dot/Icm (defect in organelle trafficking/intracellular multiplication) type IVB secretion system, including its ortholog in the conjugation system of plasmid R64, TraM, and similar proteins. These domains share striking structural similarity to the type IV secretion system (T4ASS) component VirB8 suggesting DotI/TraM to be its functional counterpart. DotI is essential for intracellular growth of Legionella pneumophila (causing agent of Legionnaires' disease) within mammalian and protozoan cells; it translocates numerous effector proteins into its eukaryotic host
SDADVLNWAADAVIEAFTLDFVNYREQLQSARPYFTDEGWKSFLNALQKSGNLDAIKDKKLVLSAVPTGA
PVIVEEGGVNGRYAWKVQVPILVTYQGGSERITQNLIVTVTIVRVPTLENPDGLAISQIIAT
>gnl|CDD|319860 cd16386, TcpC_N, N-terminal domain of conjugative transposon protein TcpC. This family contains the N-terminal domain of conjugation protein TcpC and similar proteins. TcpC is required for efficient conjugative transfer, localizing to the cell membrane independently of other conjugation proteins, where membrane localization is important for its function, oligomerization and interaction with the conjugation proteins TcpA, TcpH, and TcpG. N-terminal region (sometimes referred to as central domain) of TcpC is required for efficient conjugation, oligomerization and protein-protein interactions. TcpC has low level sequence identity to proteins encoded by the conjugative transposon Tn916, which is responsible for a large proportion of the tetracycline resistance in different pathogens
EENLADTPAAESFAENFAKEYFTWSNDDEAQEERAERLKKYLAEGLDEQNGDDVRSDLPTSSSVQLWSVE
ENSEAQYRVTYKVEQKITEEEEKKEVTSYLNVPVYVDGGSFVVVGLPYFTAVP
>gnl|CDD|319246 cd16387, ParB_N_Srx, ParB N-terminal domain and sulfiredoxin protein-related families. The ParB N-terminal domain/Sulfiredoxin (Srx) superfamily contains proteins with diverse activities. Many of the families are involved in segregation and competition between plasmids and chromosomes. Several families share similar activities with the N-terminal domain of ParB (Spo0J in Bacillus subtilis), a DNA-binding component of the prokaryotic parABS partitioning system. Also within this superfamily is sulfiredoxin (Srx; reactivator of oxidatively inactivated 2-cys peroxiredoxins), RepB N-terminal domain (plasmid segregation replication protein B like protein), nucleoid occlusion protein, KorB N-terminal domain partition protein of low copy number plasmid RK2, irbB (immunoglobulin-binding regulator that activates eib genes), N-terminal domain of sopB protein (promotes proper partitioning of F1 plasmid), fertility inhibition factors OSA and FiwA,DNA sulfur modification protein DndB, and a ParB-like toxin domain. Other activities includes a StrR (regulator in the streptomycin biosynthetic gene cluster), and a family containing a Pyrococcus furiosus nuclease and putative transcriptional regulators sbnI (Staphylococcus aureus siderophore biosynthetic gene cluster). Nuclease activity has also been reported in Arabidopsis Srx
DEEELEELAESIREHGVLQPIIVRPLPDGRYEIIAGERRWRAAKLAGLTTIPVV
>gnl|CDD|319247 cd16388, SbnI_like_N, N-terminal domain of transcriptional regulators similar to SbnI. Siderophore staphylobactin biosynthesis protein SbnI of Staphylococcus aureus is a ParB/Spo0J like protein required for the expression of genes in the sbn operon, which is responsible for staphyloferrin B (SB) biosynthesis. SnbI forms dimers and binds DNA upstream of sdnD. SbnI binds heme, which inhibits DNA binding of SbnI, leading to a suppression of sbn operon expression
LKLVPIEQIRLHEEHEPNRLEKLVERIEAEGVLRNPPIVTPLQDGRYLILDGAHRTTALKKLGCKRIPVQ
VVDEEDP
>gnl|CDD|319248 cd16389, FIN, fertility inhibition factors, including OSA and FiwA, related to the ParB/Srx superfamily. Osa and FiwA are fertility inhibition factors (FIN), which are employed by plasmids to block import of rival plasmids. Osa (oncogenic suppressive activity) of IncW group plasmid pSa gene inhibits the oncogenic properties of Agrobacterium tumefaciens. Osa is structurally similar to the ParB N-terminal domain/Srx superfamily of proteins: ParB acts in the bacterial and plasmid parABS partitioning systems. Osa has been shown to have ATPase and DNAse activities, an can block T-DNA transfer into plants. FiwA is encoded by plasmid RP1 and blocks the transfer of plasmid R388. The gene product of Haemophilus influenzae p1056.10c also blocks T-DNA transfer
TAGMANDERFVVIVDADAFLRLWLRSGFEIPKQLSCGNRKDWPNDYKFHHAEAGFAHGRENPVPLADVSC
RIEEEGNPIVSFTDGVTRTIWLLANGVKSFPVSVYNEESAELLAKLAGIGGSPI
>gnl|CDD|319249 cd16390, ParB_N_Srx_like, uncharacterized family distantly related to the N-terminal domain of the ParB/Srx superfamily. Uncharacterized proteins distantly related to the N-terminal domain of the ParB superfamily, primarily involved in bacterial and plasmid parABS-related partitioning systems. A small minority of proteins in this family include a C-terminal inorganic pyrophosphatase domain. Also within the ParB superfamily is sulfiredoxin (Srx), which is a reactivator of oxidatively inactivated 2-cys peroxiredoxins. Other families includes a putative regulator in the biosynthetic gene cluster and a family containing a Pyrococcus furiosus nuclease and putative transcriptional regulators SbnI (Staphylococcus aureus siderophore biosynthetic gene cluster) and EdeB (Brevibacillus brevis antimicrobial peptide edeine biosynthetic cluster). Nuclease activity has also been reported in Arabidopsis Srx
LLSVPLDDLRPTQAAVGYDEVYYKLGRYRALSKKDLAGYLKKHMVPVVIGPGGRLYLTDGHHLLRALLEL
GVGGLKVPVRVVADLSDLSPAAFWQEMEARGWVWLYDAEGRRIPPADLPKSLGDLADDPYRSLAYFLRDA
GGYKKDAVPFAEFYWADFLRRR
>gnl|CDD|319250 cd16392, toxin-ParB, toxin domain of the ParB/Srx superfamily. toxin domain with similarity to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system and related proteins. Toxin found, for example, at the C-terminus of polymorphic toxin system members
IKSTQEGLGKPQIVDNYKEQMLNGTYFNKKGGIAGFIDHKGVYYLTDGNHRMNAAIEYYLETGDAKYING
LI
>gnl|CDD|319251 cd16393, SPO0J_N, Thermus thermophilus stage 0 sporulation protein J-like N-terminal domain, ParB family member. Spo0J (stage 0 sporulation protein J) is a ParB family member, a critical component of the ParABS-type bacterial chromosome segregation system. The Spo0J N-terminal region acts in protein-protein interaction and is adjacent to the DNA-binding domain that binds to parS sites. Two Spo0J bind per parS site, and Spo0J interacts with neighbors via the N-terminal domain to form oligomers via an Arginine-rich patch (RRXR). This superfamily represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci
VQEIPIDKIRPNPYQPRKEFDEEALKELAESIKEHGLLQPIVVRKVGDGRYEIIAGERRWRAAKLAGLTE
IPAIVRDLDDEEALELALIENIQREDL
>gnl|CDD|319252 cd16394, sopB_N, N-terminal domain of sopB protein, which promotes proper partitioning of F1 plasmid. Escherichia coli SopB acts in the equitable partitioning of the F plasmid in the SopABC system. SopA binds to the sopAB promoter, while SopB binds SopC and helps stimulate polymerization of SopA in the presence of ATP and Mg(II). Mutation of SopA inhibits proper plasmid segregation. This N-terminal domain is related to the ParB N-terminal domain of bacterial and plasmid parABS partitioning systems, which binds parA
VSSLNGRDQELLTEEAVSDIIPSIKENGQFVPAIGYRVDGKIELLDGSRRRRAAILAGLDLRVLVSK
>gnl|CDD|319253 cd16395, Srx, Sulfiredoxin reactivates peroxiredoxins after oxidative inactivation. Sulfiredoxin reduces and thereby re-activates 2-cys peroxiredoxins. Peroxiredoxins act as molecular switches, inactivating in response to hyperoxidation from hydrogen peroxide and other free radicals. Sulfiredoxin reactivates Prx-SO(2)(-) via ATP-Mg(2+)-dependent reduction. Arabidopsis sulfiredoxin has been described as a dual function enzyme, having nuclease activity in addition to the sulfiredoxin activity. This protein is similar to ParB N-terminal-like domain of bacterial and plasmid parABS partitioning systems
VHEVPLSVIRRPLPPVLDENKVQSLMETIKGIAPGLLPPIDVLWVKGEGGGYYYSFGGCHRYEAHKRLGR
ETIRCKIIKSTPSDLRVYLG
>gnl|CDD|319254 cd16396, Noc_N, nucleoid occlusion protein, N-terminal domain, and related domains of the ParB partitioning protein family. Nucleoid occlusion protein has been shown in Bacillus subtilis to bind to specific DNA sequences on the chromosome (Noc-binding DNA sequences, NBS), inhibiting cell division near the nucleoid and thereby protecting the chromosome. This N-terminal domain is related to the N-terminal domain of ParB/repB partitioning system proteins
GEVLEIPVADIIPNPYQPRKEFDEEEIEELAESIKEHGLLQPIVVRKTKDGGYEIVAGERRWRAAKLLGW
EKIPAIIRDLSDKEALEIALIENLQ
>gnl|CDD|319255 cd16397, IbrB_like, immunoglobulin-binding regulator IbrB activates eib genes. IbrB (along with IbrA) activates immunoglobulin-binding eib genes in Escherichia coli. IbrB is related to the ParB N-terminal domain family, which includes DNA-binding proteins involved in chromosomal/plasmid segregation and transcriptional regulation, consistent with a possible mechanism for IbrB in DNA binding-related regulation of eib expression. The ParB like family is a diverse domain superfamily with structural and sequence similarity to ParB of bacterial chromosomes/plasmid parABS partitioning system and Sulfiredoxin (Srx), which is a reactivator of oxidatively inactivated 2-cys peroxiredoxins. Other families includes proteins related to StrR, a putative regulator in the biosynthetic gene cluster and a family containing a Pyrococcus furiosus nuclease and putative transcriptional regulators SbnI (Staphylococcus aureus siderophore biosynthetic gene cluster) and EdeB (Brevibacillus brevis antimicrobial peptide edeine biosynthetic cluster). Nuclease activity has also been reported in arabidopsis Srx
PVDNVQWVPIEKVQANDYNPNKVAPPEMKLLKLSILEDGFTQPIVVYYDEEDDKYVIVDGFHRYTLAKKK
PLIERLKGYLPVVVLDKDLEERMASTIRHN
>gnl|CDD|319256 cd16398, KorB_N_like, ParB-like partition protein of low copy number plasmid RK2, N-terminal domain and related domains. KorB, a member of the ParB like family, is present on the low copy number, broad host range plasmid RK2. KorB encodes a gene product involved in segregation of RK2 and acts as a transcriptional regulator, down-regulating at least 6 RK2 operons. KorB binds RNA polymerase and acts cooperatively with several co-repressors in modulating transcription. KorB is comprised of 3 domains, including a beta-strand C-terminal domain similar to SH3 domains and an alpha helical central domain that interacts with operator DNA. In ParB of P1 and SopB of F, the N-terminal region is responsible for interaction with the parA component. However, korB interaction with the RK2 parA-equivalent IncC has been mapped to the central HTH motif. This family is related to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci
LDKIDEDPDNPRTEFDEEKIEELAASIKERGVKSPISVRPHPEKPGKYIINHGARRYRASKWAGLKTIPA
FIDNDHDDFDQVIENIQREDL
>gnl|CDD|319257 cd16400, ParB_Srx_like_nuclease, ParB/Srx_like nuclease and putative transcriptional regulators related to SbnI. This family contains a Pyrococcus Furiosus enzyme reported to have DNA nuclease activity and resembles the N-terminal domain of ParB proteins of the parABS bacterial chromosome partitioning system. This sub-family also includes siderophore staphylobactin biosynthesis protein SbnI. 60% of the P. furiosus nuclease activity was retained at 90 degree C, suggesting a physiological role in the organism, which can grow in temperatures as high as 100 degrees Celsius. The protein has endo- and exo-nuclease activity vs. single- and double-stranded DNA, and nuclease activity was lost in methylated proteins prepared for structure solution. This family has a fairly well-conserved DGHHR motif that corresponds to the same structural position as the phosphorylation site (a portion of the ATP-Mg-binding site) of sulfiredoxin and the arginine-rich ParB BoxII of ParB
LLPISDLRPHEEVDPDRVEELIEKILEEGVWTKPIIVDKNTGIILDGHHRLEAAKRLGLKRVPCVLLDYD
DD
>gnl|CDD|319258 cd16401, ParB_N_like_MT, ParB N-terminal-like domain, some attached to C-terminal S-adenosylmethionine-dependent methyltransferase domain. This family represents domains related to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system, fused to a variety of C-terminal domains, including S-adenosylmethionine-dependent methyltransferase-like domains. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci
PAPYNPRKDLKPGDKEYEKLKESIEEFGLVDPLIVNKRTNVLIGGHQRLKVLKELGYTEVPVVVVDLDEE
KEKALNIALNKISGE
>gnl|CDD|319259 cd16402, ParB_N_like_MT, ParB N-terminal-like domain, some attached to C-terminal S-adenosylmethionine-dependent methyltransferase domain. This family represents domains related to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system, fused to a variety of C-terminal domains, including S-adenosylmethionine-dependent methyltransferase-like domains and DUF4417. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci
KISELKPYENNPRNNDKAVEKVAESIKEFGFLVPIVVDKNNVIVAGHTRYKAAKRLGLEEVPCIVADDLT
EEQIKAFRLADNKTSEF
>gnl|CDD|319260 cd16403, ParB_N_like_MT, ParB N-terminal-like domain, some attached to C-terminal S-adenosylmethionine-dependent methyltransferase. This family represents domains related to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system, fused to a variety of C-terminal domains, including S-adenosylmethionine-dependent methyltransferase-like domains. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci
PIDDLKPYPRNARTHSEKQIEQLAASIREFGFTNPILVDEDGVIIAGHGRLLAAKLLGLKEVPVIRLDHL
SEAQKRAYRIADNRLAEN
>gnl|CDD|319261 cd16404, pNOB8_ParB_N_like, pNOB8 ParB-like N-terminal domain, plasmid partitioning system protein domain. archaeal pNOB8 ParB acts in a plasmid partitioning system made up of 3 parts: AspA, ParA motor protein, and ParB, which links ParA to the protein-DNA superhelix. As demonstrated in Sulfolobus, AspA spreads along DNA, which allows ParB binding, and links to the Walker-motif containing ParA motor protein. The Sulfolobus ParB C-terminal domain resembles eukaryotic segregation protein CenpA, and other histones. This family is related to the N-terminal domain of ParB (Spo0J in Bacillus subtilis), a DNA-binding component of the prokaryotic parABS partitioning system and related proteins
LKEDEEFRTPNPTNEEFEELKESIRKNGIIVPIIVDQDGVIIDGHHRYRIAKELGIKEVPVIVYDFDDE
>gnl|CDD|319262 cd16405, RepB_like_N, plasmid segregation replication protein B like protein, N-terminal domain. RepB, found on plasmids and secondary chromosomes, works along with repA in directing plasmid segregation, and has been shown in Rhizobium etli to require the parS centromere-like sequence for full transcriptional repression of the repABC operon, inducing plasmid incompatibility. RepA is a Walker-type ATPase that complexes with RepB to form DNA-protein complexes in the presence of ATP/ADP. RepC is an initiator protein for the plasmid. repA and repB are homologous to the parA and ParB genes of the parABS partitioning system found on primary chromosomes
LDPDLIDPSFIADRLEDDFDDDEFEELKESIRESGQQVPILVRPHPEEGGRYEIVYGHRRLRACRELGLP
VRAIVRELSDEELVVAQGQEN
>gnl|CDD|319263 cd16406, ParB_N_like, ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning systems. This family represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci
FDPAGIEELAASIAAHGLLQNLVVRPAKKKGRYEVVAGGRRLRALQLLAERGRLPADYPVPVKVVPDADA
LEASLAENVQRE
>gnl|CDD|319264 cd16407, ParB_N_like, ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning systems. This family represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci
LSELHPFPNHPFKVRDDEEMEELVESIKENGVLTPIIVRPREDGGYEIISGHRRKRACELAGLETIPVIV
REMDDDEAVIAMVDSN
>gnl|CDD|319265 cd16408, ParB_N_like, ParB N-terminal, parA -binding, -like domain of bacterial and plasmid parABS partitioning systems. This family represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci
LVPFSDHPFKLYTGERLEDMVESIKENGVLQPIIVRPIEDGKYEILAGHNRVNAAKLAGLTTIPAIIKEN
LTDEEAKLIVVETN
>gnl|CDD|319266 cd16409, ParB_N_like, ParB N-terminal-like domain of bacterial and plasmid parABS partitioning systems. This family represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci
VDPEHVEALAQSIAEHGLLTPITVRQDPGGRYTLIAGAHRLAAAKLLGWDTIDAIIVKADDLEAELLEID
ENLI
>gnl|CDD|319267 cd16410, ParB_N_like, ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning systems. This family represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci
IEDIKVKKRIRKDLGDIEALAESIKRHGLLNPIVVTPDNELIAGERRLEAAKLLGWETIEVRVMDIEDEK
EKLELEIEEN
>gnl|CDD|319268 cd16411, ParB_N_like, ParB N-terminal, parA -binding, domain of bacterial and plasmid parABS partitioning systems. This family represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci
IPIDDIRVLNPRSRNRKIFREIVESIATVGLKRPITVRRRSSDDGGYKYDLVCGQGRLEAFKALGETEIP
AIVVDVDEEDALLMSLVENI
>gnl|CDD|319269 cd16412, dndB, DNA sulfur modification protein DndB. dndB acts in the regulation of DNA modifications, including DNA phosphorothioation. DndB may act by binding near the phosphorothioate modification site and regulating access of the Dnd modification machinery to DNA. These proteins show similarity to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system, and other members of the ParB/Srx superfamily
FPAIRGIQAGREYYVAMCPLRLLPKLFTFDEEELPNPELRAQRPLNKSRIPEIKEYILENPDNYILSALT
ASVDGEIEFEPPGEGGGRKLGLLVIPMDARFLINDGQHRRAAIEEALEERPELGDETISVVFFLDLGLER
SQQMFADLNRNAVPPSKSLNLLYDHRDPLNRLAKELVEQVPFFKGLTDKEKSSLSKRSKKLFTLSAIKNA
VKELLGGISDDDKSEEKEKLAIEFWEAVVDNIPEWQLVDNRRVSAAELREDYIHAHGVGLQALGRLGNYL
LENPPDNWKEKLAKLSKIDWSRSNPLWEGRIIVGGGKISKSRAAIKLTANALK
>gnl|CDD|319270 cd16413, DGQHR_domain, DGQHR motif containing domain. Uncharacterized diverse domain family with conserved DGQHR motif, in addition to QR and FXXXN motifs. Some proteins have been identified as parts of DNA phosphorothioation systems. Related to dndB, which acts in the regulation of DNA modifications, including DNA phosphorothioation. These proteins show similarity to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system, and other members of the ParB/Srx superfamily
LLKIAFVSRRDDDDESLEGYQRPLDKKRVKEIAKYIDTGDATFPNSIILAANSDVEFEPIQDDEGYDGIG
GILEIPDEDKPAWIIDGQHRLYGLADAERKDFDLLVVVIFVDLDVEEQAELFITINSKQKKVPKSLIYDL
FGLADSRSPRKLCRHEIARALNTDPDSPLYGRIKMLGKAGINKKGIISQATFVEANKLPLRNLFIELNDL
EEKIYEILNNYFSAVKEVF
>gnl|CDD|319271 cd16414, dndB_like, DNA-sulfur modification-associated domain. Family of proteins related to dndB. dndB acts in the regulation of DNA modifications, including DNA phosphorothioation. Both have a conserved DGQHR sequence motif. These proteins show similarity to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system, and other members of the ParB/Srx superfamily
QVLLADELADDESLDDRVQRELNPKRAKKIADYLLNNEERFFPSLVVAIRGGEPEWPEFEPEYADGSVGV
LTLPGDEKLFALDGQHRLAGIKEALKEIPDEELEAIDILEIIIVIFVGHTLEEEQRQLFSDINKNAKKVS
ASLIASLDEDDVLAILARELIEEHPLLLKGRVDFESNRISAKSEKLFTLKTLYDANKILLEGKKGSKTKR
REKDEELEEYLELLEEFWDALAELFPEL
>gnl|CDD|319852 cd16415, HAD_dREG-2_like, uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3. The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LITFDVTGTLLAVETLKDLKEKGLKLAVVSNFDRRLRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQK
ALERLGVSPEEALHVGDDLKNDYLGARAVGWHALLVDREGALHELPSLANLLERLLEL
>gnl|CDD|319853 cd16416, HAD_BsYqeG-like, Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG. The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
GVITDLDNTLLAWDNPDLTPEVKAWLADLKEAGIKVVLVSNNNERRVAKVIEKLDLPFVARAGKPRPRAF
RRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTILV
>gnl|CDD|319854 cd16417, HAD_PGPase, Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily. Phosphoglycolate phosphatase (PGP; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LVAFDLDGTLVDSAPDLAEAANAMLAALGLPPLPEETVRTWIGNGADVLVERALTGAREAEPDEELFKEA
RALFDRHYAETLSVHSHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLP
EKKPDPAPLLHACEKLGIAPAQMLMVGDSRNDILAARAAGCPSVGLTYGYNYGEDIAASGPDAVIDSLAE
LL
>gnl|CDD|319855 cd16418, HAD_Pase, phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid dehalogenase-like superfamily. This family includes phosphatases with different substrate specificities. Human PHOSPHO1 is a phosphoethanolamine/phosphocholine phosphatase associated with high levels of expression at mineralizing regions of bone and cartilage and is thought to be involved in the generation of inorganic phosphate for bone mineralization. Human PHOSPHO2 is a putative phosphatase which shows high specific activity toward pyridoxal-5-phosphate; PHODPHO2 is not specific to bone but is expressed in a wide range of soft tissues. These belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LLVFDFDRTIIMVDLIKFLAKNDGFELIIISDANSFFIEEWLEAAGFHDLFSKIFTNPASFDANGNLTVR
PYFHSHSCLLCPSNMCKGKVLEEYVASRAQDSVHYERVIYVGDGANDFCPVLRLRKGDVA
>gnl|CDD|319856 cd16419, HAD_SPS, sucrose-phosphate synthase; belongs to the haloalcanoic acid dehalogenase (HAD) superfamily. Sucrose phosphate synthase (SPS; EC 2.4.1.14) also known as UDP-glucose-fructose-phosphate glucosyltransferase, catalyzes the transfer of a hexosyl group from UDP-glucose to D-fructose 6-phosphate to form UDP and D-sucrose-6-phosphate, this is the rate limiting step of sucrose synthesis. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LFVIAVDCYDSSGLPALRVIKNILKAVRSDSGGGSTGFVLSTSLTLSETVSLLKSAGISVTDFDALICNS
GSELYYPSPSGDDDSDYELIPDPVKELRKLLRMRGLRCHLVYCRNGTRLHVLPLLASRSQALRYLFVRWG
IDLSNMVVFVGESGDTDYEELLGGLHKTVILKGV
>gnl|CDD|319857 cd16421, HAD_PGPase, Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily. Phosphoglycolate phosphatase (PGPase; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
AVIFDLDGTLLILELLKALRQKGIKLAVLSNKPNEAVQVLVEELFPGSFDFVLGEKEGIRRKPDPTXALE
CAKVLGVPPDEVLYVGDSGVDMQTARNAGMDEIGV
>gnl|CDD|319858 cd16422, HAD_Pase_UmpH-like, uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily. This uncharacterized subfamily belongs to the UmpH/NagD phosphatase family and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
LFIFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEA
TIDHLKKEFIKPKIFLLGTKSLREEFEKAGFTLDGDDIDVVVLGFDTELTYEKLRTACLLLRRGIPYIAT
HPDINCPSEEGPIPDAGSIIALIETSTGRRPDLVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVL
GINAGVDSILVLSGETTREDLEDLERKPTYVFDNVGE
>gnl|CDD|319859 cd16423, HAD_BPGM-like, uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW. This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases
AVIFDFDGVIVDTEPLWYEAWQELLNERRNELIKRQFSEKTDLPPIEGVKELLEFLKEKGIKLAVASSSP
RRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEECVVIEDSRNGVLAAKAAGMKC
VGVPNPVTGSQDFSKADLVLSSFAEKEIL
>gnl|CDD|319761 cd16424, VirB8, periplasmic domain of VirB8 protein. This family contains the periplasmic domain of VirB8 protein which is an essential assembly factor of type IV secretion system (T4SS) channel proteins that are highly diverse in function relative to other bacterial secretion systems. T4SS proteins are important virulence factors for many Gram-negative pathogens, such as Agrobacterium, Brucella, Legionella, and Helicobacter. VirB8 is a bacterial virulence protein with cytoplasmic, transmembrane, and periplasmic regions. It is thought that VirB8 is a primary constituent of a DNA transporter. It is a crucial structural and functional component of the T4SS, with interactions between VirB8 and many other T4SS proteins, including VirB10, VirB9, VirB1, VirB4, and VirB11, as well as with itself
TYDEALDKYFLAQYVRARESYDWATLQEDYDTVRLMSSPDVAAEYRALFNGDNPPSPKVLGKNARVEVKI
LSISFLGGDNTAQVRFTKTIRDKGGGEPTPTYWIATITFDYVPAPMTEEDRLINPLGFQVTSYRVDP
>gnl|CDD|319762 cd16425, TrbF, conjugal transfer protein TrbF. This family includes the conjugal transfer protein family TrbF, a family of proteins known to be involved in conjugal transfer. The TrbF protein is thought to compose part of the pilus required for transfer. This domain is similar to the type IV secretion system (T4ASS) component VirB8 and possibly has a similar fold to the nuclear transport factor-2 (NTF-2)-like superfamily
PDERVIRYFLADFIENVRTVSPDPVAQKKNIKRAYAFLTGGAAAKLNEYYRENNPFERAGKETVSVEITS
VLPLSDNTWQVEWTETTRDRGGGVISTERYRATFTVKIVPPTTEEQLLKNPLGIYITDFSWSK
>gnl|CDD|319754 cd16426, VirB10_like, VirB10 and similar proteins form part of core complex in Type IV secretion system (T4SS). This family contains VirB10, a component of the type IV secretion system (T4SS) and its homologs, including TraB, TraF, IcmE, and similar proteins. T4S system is employed by pathogenic bacteria to export virulence DNAs and/or proteins directly from the bacterial cytoplasm into the host cell. It forms a large multiprotein complex consisting of 12 proteins termed VirB1-11 and VirD4. VirB10 interacts with VirB7 and VirB9, forming the membrane-spanning 'core complex' (CC), around which all other components assemble. The CC is inserted in both the outer and inner membranes, playing a fundamental role as a scaffold for the rest of the T4SS components and actively participating in T4S substrate transfer through the bacterial envelope via conformational changes regulating channel opening and closing. In Gram-negative bacterial pathogen Helicobacter pylori, an important aetiological agent of gastroduodenal disease in humans, the comB3 gene encodes protein with best homologies to TraS/TraB from the Pseudomonas aeruginosa conjugative plasmid RP1 and TrbI of plasmid RP4 and VirB10 from the Ti plasmid of Agrobacterium tumefaciens, as well as DotG/IcmE of Legionella pneumophila
LLPGTIIPAVLLTGIDSDLPGPVLARVTRDVYDPNGGRLLIPKGSRLIGEYYGDLSSQERVLVRWTRLIC
PDGVSIDLDSVAGADALGRAGLRGDVDNHFGERFGGALLASLLSGQLAQQYLQRAENIPPTITVNAGTRV
NIVVARDVDLP
>gnl|CDD|319758 cd16427, TraM-like, C-terminal domain of transfer protein TraM. This family contains the C-terminal domain of transfer protein TraM of the G+ broad host range Enterococcus conjugative plasmid pIP501 and similar proteins. The protein localizes to the cell envelope and is part of the plasmid transfer system that is accessible from outside of the cell. TraM displays a fold similar to the type IV secretion system (T4SS) VirB8 proteins from A. tumefaciens and B. suis (G-) and to the transfer protein TcpC from C. perfringens plasmid pCW3 (G+), reinforcing the prediction that TraM performs a key role in the secretion process, which is underlined by its surface accessibility. It is also structurally related to members of the nuclear transport factor-2 (NTF-2)-like superfamily with a high similarity to the NTF-2 protein from Rattus norvegicus. TraM (categorized as T4SS VirB8-like class GAMMA) does not possess the binding pocket of classic VirB8 class ALPHA proteins, recognized by VirB8 interaction inhibitors
KELQEEQGKIDVFSRYFLPNYYSGNKENLKDFLSKDLAKDIEPKKGQLQSVILEKIKKTKKGYTVTYVLS
VKEEETVKTKRLTFTVKEDKKAKYGYLVTKQPKESDYP
>gnl|CDD|319759 cd16428, TcpC_C, C-terminal domain of conjugative transposon protein TcpC. This family contains the C-terminal domain of conjugation protein TcpC and similar proteins. TcpC is required for efficient conjugative transfer, localizing to the cell membrane independently of other conjugation proteins, where membrane localization is important for its function, oligomerization and interaction with the conjugation proteins TcpA, TcpH, and TcpG. C-terminal domain is critical for interactions with these other conjugation proteins. TcpC has low level sequence identity to proteins encoded by the conjugative transposon Tn916, which is responsible for a large proportion of the tetracycline resistance in different pathogens
VDAEEKEEIEEFLETFFKAYATGSEEELSYYMKDKDPEGLNGDYTFVSLDNPVYKGKGDGYIVTVTVTFK
DKDTGIEQTEQYTLTLVKKDGRWYVKK
>gnl|CDD|319755 cd16429, VirB10, VirB10 forms part of core complex in Type IV secretion system (T4SS). This family contains VirB10, a component of the type IV secretion system (T4SS), including homologs TrbI, TraF, TrwE and TraL. T4S system is employed by pathogenic bacteria to export virulence DNAs and/or proteins directly from the bacterial cytoplasm into the host cell. It forms a large multiprotein complex consisting of 12 proteins termed VirB1-11 and VirD4. VirB10, interacts with VirB7 and VirB9, forming the membrane-spanning 'core complex' (CC), around which all other components assemble. The CC is inserted in both, the outer and inner membranes, playing a fundamental role as a scaffold for the rest of the T4SS components and actively participating in T4S substrate transfer through the bacterial envelope via conformational changes regulating channel opening and closing. TrwE in R33 plasmid has been shown to be anchored to the inner membrane and its C-terminal is necessary for conjugation; the transmembrane domains of TrwB and TrwE are involved in TrwB-TrwE interactions. TraF protein of the RP4 plasmid is involved in circularization of pilin subunits of P-type pili. In gonococcal genetic island (GGI) of Neisseria gonorrhoeae, T4SS encodes TrbI and circularization occurs via a covalent intermediate between the C terminus of putative pilin protein TraA and TrbI
LPAGTVIPAVLETAINSDLPGQVRAQVTRDVYDSTGRVLLIPKGSRLIGEYNSGVAQGQSRVFVVWTRLI
TPDGVSIDLDSMPGADALGRAGLKGDVDNHFWERFGGALLLSLISDGAQAASSSASNSNSAGQAAGSNTG
QSLGQVASQILERNLNIPPTITIRQGTRINIFVARDLDFS
>gnl|CDD|319756 cd16430, TraB, TraB is a homolog of VirB10 which forms part of core complex in Type IV secretion system (T4SS). This family contains TraB (VirB10 homolog) and a component of the type IV secretion system (T4SS), and similar proteins. T4S system is employed by pathogenic bacteria to export virulence DNAs and/or proteins directly from the bacterial cytoplasm into the host cell. It forms a large multiprotein complex consisting of 12 proteins termed VirB1-11 and VirD4. VirB10, interacts with VirB7 and VirB9, forming the membrane-spanning 'core complex' (CC), around which all other components assemble. The CC is inserted in both the outer and inner membranes, playing a fundamental role as a scaffold for the rest of the T4SS components and actively participating in T4S substrate transfer through the bacterial envelope via conformational changes regulating channel opening and closing. TraB is localized similarly to related proteins in other systems, but unlike in other systems, Neisseria gonorrhoeae TraB does not require the presence of other T4SS components for proper localization. It has been shown to be expressed with TraK (VirB9 homolog) at low levels in wild-type cells, suggesting that gonococcal T4SS may be present in single copy per cell and the small amounts of these proteins are sufficient for DNA secretion
YLPAGSFARAVLLTGVDAPTGVQAQSNPVPVLLRIKDDAILPNGFRSDLKGCFVLGSAYGDLSSERAYIR
LESLSCIRKDGKVIEVPVKGYVVGEDGKAGIRGRVVSKQGQLLARALLAGFLSGLGQAFQQAATTTSTTS
GLGTTQTIDPGDALKAGAGGGASSALDKLADYYLKLAEQMFPVIEVDAGREVDVVFTEGFSLE
>gnl|CDD|319757 cd16431, IcmE, DotG/IcmE is a homolog of VirB10 which forms part of core complex in Type IV secretion system. This family contains DotG/IcmE (VirB10 homolog) and a component of the type IV secretion system (T4SS), and similar proteins. The Dot/Icm system is a T4SS found in the pathogens Legionella and Coxiella and the conjugative apparatus of IncI plasmids; T4SS is employed by pathogenic bacteria to export virulence DNAs and/or proteins directly from the bacterial cytoplasm into the host cell. Similar to T4SS VirB/D components, the Legionella Dot/Icm secretion apparatus contains a critical five-protein sub-assembly that forms the membrane-spanning 'core-complex' (CC), around which all other components assemble. This transmembrane connection is mediated by protein dimer pairs consisting of two inner membrane proteins, DotF and DotG, each independently associating with DotH/DotC/DotD in the outer membrane
LIPAGTIVYAVLDTAVNSDEPGPVLATIRSGPLKGARLIGSFERSGDGVVITFTTMVLPGGKSYPIDAYA
LDDRTLSAVASDVDNHYLSRYGLPAAAAFLQGLGQAYQQAGTTTTSTSGGTVTVTTGTPDGKQAAGAAAG
GVGQQLGQVLAQDANRPPTVTVPAGTPIGILFMSDVTDP
>gnl|CDD|319751 cd16432, CheB_Rec, Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC domain. This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain with a REC domain at the N-terminus. CheB is a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. The N-terminal regulatory (REC) domain blocks the active site of the C-terminal domain until it is phosphorylated. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR
LVAIGASTGGPQALQEILSALPADFPAPILIVQHMPPGFTKSFAERLNRLSALPVKEAEDGEPLEPGTVY
IAPGGYHLVVERRGGGGRIRLSDGPPVNGHRPSVDVLFRSAAEVYGARALGVILTGMGRDGAEGLLALKE
AGGYTIAQDEASSVVYGMPKAAIEAGAADEVLPLDEIAAAILRL
>gnl|CDD|319752 cd16433, CheB, Chemotaxis response regulator protein-glutamate methylesterase, CheB. This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain, a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. cheR and cheB have a strong preference to occur in the same operon, and a subgroup contains multidomain proteins with CheB-CheR fusions. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR
IVVIGASAGGLEALLELLSALPADFPAPVLVVLHRPPDSPSVLPELLSRRTPLPVKEAEDGEPIEPGTIY
VAPPDYHLLVEDDGTFSLSRGPKVNFSRPSIDVLFRSAADAYGPRVIGVVLTGANDDGAAGLAAIKRAGG
LTIVQDPATAEVPSMPRAALAAVAVDHVLPLAEIAALLVRL
>gnl|CDD|319753 cd16434, CheB-CheR_fusion, Chemotaxis response regulator protein-glutamate methylesterase, CheB, fused with CheR domain. This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain, a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors, fused with a CheR domain as well as other domains. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. cheB and cheR are typically found in the same operon. However, CheB and CheR are fused in multi-domain proteins in this subgroup. The CheR protein/domain includes an all-alpha N-terminal domain and an S-adenosylmethionine-dependent methyltransferase C-terminal domain. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR
VVGIGASAGGLEALEEFFSALPADSGMAFVVVQHLSPDHKSLLAELLARHTSMPVVEAEDGMRVEPNHVY
VIPPGKDLTIEDGRLRLSPPDEPRGPRLPIDVFFRSLAEDQGERAIGVILSGTGSDGTLGLKAIKEAGGL
VLAQDPETAKFDGMPRSAIATGLVDFVLPPEEIAAELLAY
>gnl|CDD|319740 cd16435, BPL_LplA_LipB, biotin-lipoate ligase family. This family includes biotin protein ligase (BPL), lipoate-protein ligase A (LplA) and octanoyl-[acyl carrier protein]-protein acyltransferase (LipB). Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LplA) catalyses the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes
FVEVLDSVDYESAWAAQEKSLRENVSNQSSTLLLWEHPTTVTLGRLDRELPHLELAKKIERGYELVVRNR
GGRAVSHDPGQLVFSPVIGPNVEFMISKFNLIIEEGIRDAIADFGQSAEVKWGRNDLWIDNRKVCGIAVR
VVKEAIFHGIALNLNQDLENFTEIIPCGYKPERVTSLSLELGRKVTVEQVLERVLAAF
>gnl|CDD|319744 cd16436, beta_Kdo_transferase, beta-3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)-transferase. KpsC and KpsS are retaining beta-3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)-transferases. They are part of the ATP-binding cassette transporter dependent capsular polysaccharides (CPSs) synthesis pathway, one of two CPS synthesis pathways present in Escherichia coli. The poly-Kdo linker is thought to be the common feature of CPSs synthesized via this pathway. CPSs are high-molecular-mass cell-surface polysaccharides that are important virulence factors for many pathogenic bacteria
VVGWGDRRPGQRAAAWALRAGVPVWRFEDGFLRSVSLGVLGDRPLSIVLDKLGIYYDASRPSRLEMLLKD
KAFLVPLQVSGDVQVRLGGAVASSFLHVLASFLEHNPDTPIIIKHHPDVRGGKDYGYLIDETLSLERRVL
LVHDVSLPSLLKRAGGVVTVNSTSGFEALLHGKPVKVLGLPWYAGWGLTDDRHLAAFWVAARLGNATLHY
LFGATQINYNFY
>gnl|CDD|319745 cd16437, beta_Kdo_transferase_KpsC, beta-3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)-transferase KpsC. KpsC is a beta-3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)-transferase. It is part of the ATP-binding cassette transporter dependent capsular polysaccharides (CPSs) synthesis pathway, one of two CPS synthesis pathways present in Escherichia coli. The poly-Kdo linker is thought to be the common feature of CPSs synthesized via this pathway. CPSs are high-molecular-mass cell-surface polysaccharides, that are important virulence factors for many pathogenic bacteria. KpsC contains a domain duplication
IAVWGHRPSAAKPVIAQRHGLPLWRMEDGFLRSLGLGVDLEPPLSLVVDDYGIYYDASRPSDLEKLLNDA
AFNTALLSRAEELRHRLVTGKLSKYNLAPDFVADESKRRDIILVPGQVENDASITTGNASIHSNAALLRA
VREENPDAEIWYKVHPDVLEGKRTGYFLALRATQLVDLIAEDVDIQSLLRRVDRVHTMTSLYGFEALLAG
KQVHCYGLPFYAGWGLTDDRHPCPRRRGSLTLEELFAATLIRYPRY
>gnl|CDD|319746 cd16438, beta_Kdo_transferase_KpsS_like, beta-3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)-transferase KpsS like. KpsS is a beta-3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)-transferase. It is part of the ATP-binding cassette transporter dependent capsular polysaccharides (CPSs) synthesis pathway, one of two CPS synthesis pathways present in Escherichia coli. The poly-Kdo linker is thought to be the common feature of CPSs synthesized via this pathway. CPSs are high-molecular-mass cell-surface polysaccharides that are important virulence factors for many pathogenic bacteria
VVVWNGSKLPQSVAAAAARRLGIPVLFFENGLLPGTTTLDPKGVNYANSVPRDPAFYRNYSIDQEPPLKA
LVRRPLRKKKKKQADPVELPERYVFVPFQVPTDTQILLHSPWIKDMEQLYEVLVEAADRLNPDLKIVFKE
HPSDPKSYDYKELYKKHPRVIFANGNDTQELIEGAEAVITINSTVGIEALLLGKPVITLGNAFYNIEGLV
LHARSPQELAAALARLLQWQPDRELRRKFLYYLRNHYLVPGSWQ
>gnl|CDD|319747 cd16439, beta_Kdo_transferase_KpsC_2, beta-3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)-transferase KpsC, repeat 2. KpsC is a beta-3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)-transferase. It is part of the ATP-binding cassette transporter dependent capsular polysaccharides (CPSs) synthesis pathway, one of two CPS synthesis pathways present in Escherichia coli. The poly-Kdo linker is thought to be the common feature of CPSs synthesized via this pathway. CPSs are high-molecular-mass cell-surface polysaccharides that are important virulence factors for many pathogenic bacteria. KpsC contains a domain duplication
GRVVVWGSREPPELLAAAAAAGIPVWRVEDGFIRSVGLGADLTPPLSLVLDDRGIYYDPTRPSDLETLLN
THDFDDALLARARRLRELLVELGISKYNLGGDAPLPAPPKGRRVILVPGQVEDDASIRLGSPDIKTNLEL
LRAVRAENPDAFIIYKPHPDVLAGLRKGAVPEAEALKLADEVVTDASIADLLEQVDEVHTMTSLTGFEAL
LRGKKVTTYGLPFYAGWGLTDDRLPLPRRTRRLTLDELVAGALILYPRY
>gnl|CDD|319748 cd16440, beta_Kdo_transferase_KpsC_1, beta-3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)-transferase KpsC, repeat1. KpsC is a beta-3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)-transferase. It is part of the ATP-binding cassette transporter dependent capsular polysaccharides (CPSs) synthesis pathway, one of two CPS synthesis pathways present in Escherichia coli. The poly-Kdo linker is thought to be the common feature of CPSs synthesized via this pathway. CPSs are high-molecular-mass cell-surface polysaccharides that are important virulence factors for many pathogenic bacteria. KpsC contains a domain duplication
VVGWGRKPSARRARAYAARHGLPYLALEDGFLRSLGLGVDGEPPLSLVVDDLGIYYDATRPSRLEQLLNS
PLFLDAALLARARRAIALIREHRLSKYNHAPDLPPLLGPPPRPRVLVVDQTAGDASIAYGGASAASFRRM
LEAALEENPDAEILVKTHPDVLAGKKKGYLLELAADPRVTLLAEDVNPISLLEHADAVYTVTSQMGFEAL
LAGKPVHCFGMPFYAGWGLTDDRLPCPRRRRKRSLEQLFAAAYILYPRYVDP
>gnl|CDD|319749 cd16441, beta_Kdo_transferase_KpsS, beta-3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)-transferase KpsS. KpsS is a beta-3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)-transferase. It is part of the ATP-binding cassette transporter dependent capsular polysaccharides (CPSs) synthesis pathway, one of two CPS synthesis pathways present in Escherichia coli. The poly-Kdo linker is thought to be the common feature of CPSs synthesized via this pathway. CPSs are high-molecular-mass cell-surface polysaccharides that are important virulence factors for many pathogenic bacteria
IVLFGDCRPYHRIAIEVARELGIRVHVFEEGYLRPDWITLERGGVNGHSRLPRDPAFYRELAAALPPPPP
PRPVGSSFRRRAWYAVLYYLANVLGRPLFPHYRHHRPYNPLEEYLGWLRRLLRKRLYRRRERALLRLLLE
SGGPYFLVPLQLDNDSQIRVHSPFGSMEDFIEEVIASFARHAPADTRLVIKHHPLDRGLRNYRRLIRRLA
RRLGVAGRVHYIHGGHLPTLLRHARGVVTVNSTVGLSALYHGKPVKVLGDAIYDIPGLTFQGPLDDFWQA
PQPPDPELFEAFRRYLIATTQINGSFY
>gnl|CDD|319741 cd16442, BPL, biotin protein ligase. Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an activated form of biotin, biotinyl-5'-AMP, from substrates biotin and ATP followed by biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine
KLIVLDEIDSTNDEAKELARSGAPEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPL
LTLLAAVAVAEALEKLGGIPVQIKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNTPPPEPL
PDTSLATSLGKEVDRNELLEELLAALENRLELF
>gnl|CDD|319742 cd16443, LplA, lipoate-protein ligase. Lipoate-protein ligase A (LplA) catalyzes the formation of an amide linkage between free lipoic acid and a specific lysine residue of the lipoyl domain in lipoate dependent enzymes, similar to the biotinylation reaction mediated by biotinyl protein ligase (BPL). The two step reaction includes activation of exogenously supplied lipoic acid at the expense of ATP to lipoyl-AMP and then transfer to the epsilon-amino group of a specific lysine residue of the lipoyl domain of the target protein
MRLIDSSGDPPAENLALDEALLRSVAAPPTLRLYLWQNPPTVVIGRFQNPLEEVNLEYAEEDGIPVVRRP
SGGGAVFHDLGNLNYSLILPKEHPSIDESYRALSQPVIKALRKLGVEAEFGGVGRNDLVVGGKKISGSAQ
RRTKGRILHHGTLLVDVDLEKLARVLNVPYEKLKSKGPKSVRSRVTNLSELLGRDITVEEVKNALLEAF
>gnl|CDD|319743 cd16444, LipB, lipoyl/octanoyl transferase. Lipoate-protein ligase B is a octanoyl-[acyl carrier protein]-protein acyltransferase the catalyzes the first step of lipoic acid synthesis. It transfers endogenous octanoic acid attached via a thioester bond to acyl carrier protein (ACP) onto lipoyl domains, which is later converted by lipoate synthase LipA into lipoylated derivatives
IVRDLGLIPYEEAWELQKRLVAERIAGETPDTLWLLEHPPVYTLGRRGKPENLLNNGGIPVVRTDRGGQV
TYHGPGQLVGYPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRRPGAPGVWVGDRKIASIGIRVRR
GVTYHGLALNVNTDLSPFNRINPCGIKGKGVTSLSDLGGREVDMEEVKQKLVEEFAKIF
>gnl|CDD|438112 cd16448, RING-H2, H2 subclass of RING (RING-H2) fingers and its variants. The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates
CVICLEEFEEGDVVRLLPCGHVFHLACILRWLESGNNTCPLCR
>gnl|CDD|438113 cd16449, RING-HC, HC subclass of RING (RING-HC) finger and its variants. The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates
LECPICLERLKDPVLLPCGHVFCRECIRRLLESGSIKCPIC
>gnl|CDD|438114 cd16450, mRING-C3HGC3_RFWD3, Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing protein 3 (RFWD3) and similar proteins. RFWD3, also known as RING finger protein 201 (RNF201) or FLJ10520, is an E3 ubiquitin-protein ligase that forms a complex with Mdm2 and p53 to synergistically ubiquitinate p53 and acts as a positive regulator of p53 stability in response to DNA damage. It is phosphorylated by checkpoint kinase ATM/ATR and the phosphorylation mutant fails to stimulate p53 ubiquitination. RFWD3 also functions as a novel replication protein A (RPA)-associated protein involved in DNA replication checkpoint control. RFWD3 contains an N-terminal SQ-rich region followed by a RING finger domain that exhibits robust E3 ubiquitin ligase activity toward p53, a coiled-coil domain and three WD40 repeats in the C-terminus, the latter two of which may be responsible for protein-protein interaction. The RING finger in this family is a modified C3HGC3-type RING finger, but not a canonical C3H2C3-type RING-H2 finger or C3HC4-type RING-HC finger
EGNTCPICFEPWTSSGEHRLVSLKCGHLFGYSCIEKWLKGKGKKCPQCNKKAKRSDIRPLY
>gnl|CDD|438115 cd16451, mRING_PEX12, Modified RING finger found in peroxin-12 (PEX12) and similar proteins. PEX12, also known as peroxisome assembly protein 12 or peroxisome assembly factor 3 (PAF-3), is a RING finger domain-containing integral membrane peroxin required for protein import into peroxisomes. Mutations in human PEX12 result in the peroxisome deficiency Zellweger syndrome of complementation group III (CG-III), a lethal neurological disorder. PEX12 also functions as an E3-ubiquitin ligase that facilitates the PEX4-dependent monoubiquitination of PEX5, a key player in peroxisomal matrix protein import, to control PEX5 receptor recycling or degradation. PEX12 contains a modified RING finger that lacks the third, fourth, and eighth zinc-binding residues of the consensus RING finger motif, suggesting PEX12 may only bind one zinc ion
GICPLCRKKRTNPTALATSGYVFCYPCIYRYVKEHGRCPVTGYPASLDHLIKLY
>gnl|CDD|438116 cd16452, SP-RING-like, SP-RING finger and SPL-RING finger, variants of RING fingers. This family corresponds to a group of proteins with variants of RING fingers that are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. They include SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases and SPL-RING finger found in E3 SUMO-protein ligase NSE2. The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress
LKCPITQKRMKDPVRGKHCGHCFDLEAILQYLKRRKKKWKCPVCS
>gnl|CDD|438117 cd16453, RING-Ubox, U-box domain, a modified RING finger. The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms
FLCPISGELMKDPVITPSGITYDRSAIERWLLSDNTDPFTREPL
>gnl|CDD|438118 cd16454, RING-H2_PA-TM-RING, RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family. The PA-TM-RING family represents a group of transmembrane-type E3 ubiquitin ligases, which has been characterized by an N-terminal transient signal peptide, a PA (protease-associated) domain, a TM (transmembrane) domain, as well as a C-terminal C3H2C3-type RING-H2 finger domain. It includes RNF13, RNF167, ZNRF4 (zinc and RING finger 4), GRAIL (gene related to anergy in lymphocytes)/RNF128, RNF130, RNF133, RNF148, RNF149 and RNF150 (which are more closely related), as well as RNF43 and ZNRF3, which have substantially longer C-terminal tail extensions compared with the others. PA-TM-RING proteins are expressed at low levels in all mammalian tissues and species, but they are not present in yeast. They play a common regulatory role in intracellular trafficking/sorting, suggesting that abrogation of their function may result in dysregulation of cellular signaling events in cancer
TCAICLEEFKEGEKVRVLPCNHLFHKDCIDPWLEQHNTCPLCR
>gnl|CDD|438119 cd16455, RING-H2_AMFR, RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar proteins. AMFR, also known as AMF receptor, or RING finger protein 45, or ER-protein gp78, is an internalizing cell surface glycoprotein localized in both plasma membrane caveolae and the endoplasmic reticulum (ER). It is involved in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. AMFR also functions as a RING finger-dependent ubiquitin protein ligase (E3) implicated in the degradation from the ER. AMFR contains an N-terminal RING-H2 finger and a C-terminal ubiquitin-associated (UBA)-like CUE domain
DDCAICWESMQSARKLPCGHLFHNSCLRSWLEQDTSCPTCRMSL
>gnl|CDD|438120 cd16456, RING-H2_APC11, RING finger, H2 subclass, found in anaphase-promoting complex subunit 11 (APC11) and similar proteins. APC11, also known as cyclosome subunit 11, or hepatocellular carcinoma-associated RING finger protein, is a C3H2C3-type RING-H2 protein that facilitates ubiquitin chain formation by recruiting ubiquitin-charged ubiquitin conjugating enzymes (E2) through its RING-H2 domain. APC11 and its partner, the cullin-like subunit APC2, form the dynamic catalytic core of the gigantic, multisubunit 1.2-MDa anaphase-promoting complex/cyclosome (APC), also known as the cyclosome, which is a ubiquitin-protein ligase (E3) composed of at least 12 subunits and controls cell division by ubiquitinating cell cycle regulators, such as cyclin B and securin, to drive their timely degradation. APC11 can be inhibited by hydrogen peroxide, which may contribute to the delay in cell cycle progression through mitosis that is characteristic of cells subjected to oxidative stress. APC11 contains a canonical RING-H2-finger that coordinate two Zn2+ ions. In addition, it contains a third Zn2+-binding site that is not essential for its ligase activity
DDVCGICRMAFDGCCPDCKFPGDDCPLVWGKCSHCFHMHCILKWLNSQQVQQHCPMCRQEWKF
>gnl|CDD|438121 cd16457, RING-H2_BRAP2, RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins. BRAP2, also known as impedes mitogenic signal propagation (IMP), RING finger protein 52, or renal carcinoma antigen NY-REN-63, is a novel cytoplasmic protein interacting with the two functional nuclear localization signal (NLS) motifs of BRCA1, a nuclear protein linked to breast cancer. It also binds to the SV40 large T antigen NLS motif and the bipartite NLS motif found in mitosin. BRAP2 serves as a cytoplasmic retention protein and plays a role in the regulation of nuclear protein transport. It contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C3H2C3-type RING-H2 finger and a UBP-type zinc finger
PTCPVCLERMDESVSGILTILCNHSFHCSCLSKWGDSSCPVCRY
>gnl|CDD|319372 cd16458, RING-H2_Dmap-like, RING finger, H2 subclass, found in defective in mitotic arrest proteins (Dmap) and similar proteins. This subfamily includes Schizosaccharomyces pombe protein Dma1 (SpDma1p), Saccharomyces cerevisiae proteins Dma1 (ScDma1p) and Dma2 (ScDma2p), and their homologs from fungi. SpDma1p was originally isolated as a multicopy suppressor of the temperature-sensitive growth phenotype caused by cdc16 mutations. It functions to prevent mitotic exit and cytokinesis during spindle checkpoint arrest by inhibiting septation initiation network (SIN) signaling. ScDma1p and ScDma2p, also known as checkpoint forkhead associated with RING domains-containing protein 1 and 2 respectively, seem to be functionally redundant. They are involved in proper septin ring positioning and cytokinesis. The simultaneous lack of Dma1 and Dma2 leads to spindle mispositioning and defects in the spindle position checkpoint. All members of this family contain a forkhead-associated (FHA) domain and a C3H2C3-type RING-H2 finger, the latter suggesting they may possess E3 ubiquitin-ligase activities
PDCSICLFPVLPCQALFVSPCAHSWHFKCIRPLLEASYPQFSCPNCR
>gnl|CDD|438122 cd16459, RING-H2_DTX1-like, RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex1 (DTX1), Deltex2 (DTX2), Deltex4 (DTX4), and similar proteins. This subfamily contains the vertebrate homologs of Drosophila melanogaster Deltex, specifically DTX1, DTX2, and DTX4, and other similar proteins mainly from eumetazoa. The vertebrate homologs of Deltex are involved in Notch signaling and neurogenesis. Mammalian DTX1 is most closely related to the Drosophila Deltex. Both of them bind to SH3-domain containing protein Grb2 and further inhibit E2A. DTX1 functions as a Notch downstream transcription regulator. It interacts with the transcription coactivator p300 and inhibits transcription activation mediated by the neural specific transcription factor MASH1. It is also a transcription target of nuclear factor of activated T cells (NFAT) and participates in T cell anergy and Foxp3 protein level maintenance in vivo. Moreover, DTX1 promotes protein kinase C theta degradation and sustains Casitas B-lineage lymphoma expression. DTX4, also known as RING finger protein 155, shares the highest degree of sequence similarity with DTX1. So it likely interacts with the intracellular domain of Notch as well. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. In contrast to other DTXs, DTX3 does not contain two Notch-binding WWE domains at the N-terminus, but rather a short unique N-terminal domain. It does not interact with the intracellular domain of Notch. In addition, it has a different class of RING finger (C3HC4 type or RING-HC subclass), compared with the other DTXs which harbor a C3H2C3-type RING-H2 finger. Thus DTX3 is not included in this subfamily. Drosophila melanogaster Deltex also does not belong to this subfamily
DCPICCEPLCVASGYEESKLEGSKVVVRLKKCSHMYHKACLVAMYSNGAKDGSLQCPTCKTIYG
>gnl|CDD|438123 cd16460, RING-H2_DZIP3, RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) and similar proteins. DZIP3, also known as RNA-binding ubiquitin ligase of 138 kDa (RUL138) or 2A-HUB protein, is an RNA-binding E3 ubiquitin-protein ligase that interacts with coactivator-associated arginine methyltransferase 1 (CARM1) and acts as a transcriptional coactivator of estrogen receptor (ER) alpha. It is also a histone H2A ubiquitin ligase that catalyzes monoubiquitination of H2A at lysine 119, functioning as a combinatorial component of the repression machinery required for repressing a specific chemokine gene expression program, critically modulating migratory responses to Toll-like receptors (TLR) activation. DZIP3 contains a C3H2C3-type RING-H2 finger at the C-terminus
TPCVICHEAFSDGDRLLVLPCAHKFHTQCIGPWLDGQQTCPTCRLHV
>gnl|CDD|438124 cd16461, RING-H2_EL5-like, RING finger, H2 subclass, found in rice E3 ubiquitin-protein ligase EL5 and similar proteins. EL5, also known as protein ELICITOR 5, is an E3 ubiquitin-protein ligase containing an N-terminal transmembrane domain and a C3H2C3-type RING-H2 finger that is a binding site for ubiquitin-conjugating enzyme (E2). It can be rapidly induced by N-acetylchitooligosaccharide elicitor. EL5 catalyzes polyubiquitination via the Lys48 residue of ubiquitin, and thus plays a crucial role as a membrane-anchored E3 in the maintenance of cell viability after the initiation of root primordial formation in rice. It also acts as an anti-cell death enzyme that might be responsible for mediating the degradation of cytotoxic proteins produced in root cells after the actions of phytohormones. Moreover, EL5 interacts with UBC5b, a rice ubiquitin carrier protein, through its RING-H2 finger. EL5 is an unstable protein, and its degradation is regulated by the C3H2C3-type RING-H2 finger in a proteasome-independent manner
ECAICLSDYENGEELRRLPECKHAFHKECIDEWLKSNSTCPLCR
>gnl|CDD|438125 cd16462, RING-H2_Pep3p-like, RING finger, H2 subclass, found in Saccharomyces cerevisiae vacuolar membrane protein PEP3 (Pep3p) and similar proteins. Pep3p, also known as carboxypeptidase Y-deficient protein 3, vacuolar morphogenesis protein 8, vacuolar protein sorting-associated protein 18 (Vps18p), or vacuolar protein-targeting protein 18, is a vacuolar membrane protein that affects late Golgi functions required for vacuolar protein sorting and efficient alpha-factor prohormone maturation. It is required for vacuolar biogenesis and for trafficking of hydrolase precursors to the vacuole. The disruption of PEP3 may cause hypersensitivity to heat shock and ethanol stresses, probably due to disappearance of normal vacuoles. As a component of the homotypic fusion and vacuole protein sorting (HOPS) and class C core vacuole/endosome tethering (CORVET) complexes, its overexpression shortens lag phase but does not alter growth rate in Saccharomyces cerevisiae exposed to acetic acid stress. Moreover, Pep3p forms the Class C Vps protein complex (C-Vps complex) with Pep5p (also known as Vps11), Vps16, and Vps33, and is necessary for trafficking of hydrolase precursors to the vacuole by promoting vesicular docking reactions with SNARE proteins. Pep3p contains a C3H2C3-type RING-H2 finger at the C-terminus
EKCAVCGRPLLTRQFYVFPCQHAFHADCLIEEVLDDLIASECPLCGELMI
>gnl|CDD|438126 cd16463, RING-H2_PHR, RING finger, H2 subclass, found in the PHR (Pam/Highwire/RPM-1) protein family. The PHR protein family represents an evolutionally conserved family of large proteins including human E3 ubiquitin ligase protein associated with Myc (Pam) and its homologs, Phr1 in mouse, Highwire (HIW) in Drosophila, RPM-1 (regulator of presynaptic morphology 1) in Caenorhabditis elegans, and Esrom in zebrafish. Those proteins are large E3 ubiquitin ligases containing regulator of chromosome condensation (RCC) homology domains (RHD-1 and RHD-2) with inferred guanine exchange factor (GEF) activity, a Myc-binding domain, a B-box zinc finger, and a C-terminal C3H2C3-type RING-H2 finger with E3 ubiquitin (Ub) ligase activity. They play an important role in axon guidance and synaptogenesis. They regulate synapse formation and growth in mammals, zebrafish, Drosophila, and Caenorhabditis elegans, and may control a variety of signaling pathways, including cAMP signaling in mammalian cells, JNK/p38 MAPK signaling in Drosophila and C. elegans, and bone morphogenetic protein signaling in Drosophila. Pam also known as Myc-binding protein 2 (MYCBP2), or Pam/highwire/rpm-1 protein (PHR1), negatively regulates neuronal growth, synaptogenesis and synaptic plasticity by modulating several signaling pathways including the p38 MAPK signaling cascade. It also participates in receptor and ion channel internalization, such as regulating internalization of transient receptor potential vanilloid receptor 1 (TRPV1) in peripheral sensory neurons, as well as duration of thermal hyperalgesia through p38 MAPK. It interacts with neuron-specific electroneutral potassium (K+) and chloride (Cl-) cotransporter KCC2 and modulates its function. Moreover, Pam genetically interacts with Robo2 to modulate axon guidance in the olfactory system. It also associates with tuberous sclerosis complex (TSC) proteins, ubiquitinating TSC2 and regulating mammalian/mechanistic target of rapamycin (mTOR) signaling. Furthermore, Pam is the longest lasting nontranscriptional regulator of adenylyl cyclase activity, and can mediate sustained inhibition of cAMP signaling by sphingosine-1-phosphate. It is also involved in spinal nociceptive processing. Phr1 is an essential regulator of retinal ganglion cell projection during both dorsal lateral geniculate nucleus (dLGN) and superior colliculus (SC) topographic map development. RPM-1 positively regulates a Rab GTPase pathway to promote vesicular trafficking via late endosomes, thereby regulating synapse formation and axon termination. Esrom has E3 ligase activity and modulates the amount of phosphorylated Tuberin, a tumor suppressor, in growth cones. It is required for the formation of the retinotectal projection
DDMCMICFTEALSAAPAIQLDCGHVFHLHCCRRVLENRWPGPRITFGFLKCPICK
>gnl|CDD|438127 cd16464, RING-H2_Pirh2-like, RING finger, H2 subclass, found in p53-induced RING-H2 protein (Pirh2) and similar proteins. Pirh2, also known as RING finger and CHY zinc finger domain-containing protein 1 (Rchy1), androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, RING finger protein 199 (RNF199), or zinc finger protein 363 (ZNF363), is a p53 inducible E3 ubiquitin-protein ligase that functions as a negative regulator of p53. It preferably ubiquitylates the tetrameric form of p53 in vitro and in vivo, suggesting a role of Pirh2 in downregulating the transcriptionally active form of p53 in the cell. Moreover, Pirh2 inhibits the transcriptional activity of p73, a homolog of the tumor suppressor p53, by promoting its ubiquitination. It also monoubiquitinates DNA polymerase eta (PolH) to suppress translesion DNA synthesis. Furthermore, Pirh2 functions as a negative regulator of the cyclin-dependent kinase inhibitor p27(Kip1) function by promoting ubiquitin-dependent proteasomal degradation. Pirh2 enhances androgen receptor (AR) signaling through inhibition of histone deacetylase 1 (HDAC1) and is overexpressed in prostate cancer. It interacts with TIP60 and this association may regulate Pirh2 stability. In addition, the oncoprotein pleomorphic adenoma gene like 2 (PLAGL2) can bind to the Pirh2 dimer and therefore control the stability of Pirh2. Pirh2 contains a total of nine zinc-binding sites with six located at the N-terminal region, two in the C3H2C3-type RING-H2 domain, and one in the C-terminal region. Nine zinc binding sites comprise three different zinc coordination schemes, including RING type cross-brace zinc coordination, C4 zinc finger, and a novel left-handed beta-spiral zinc-binding motif formed by three recurrent CCHC sequence motifs. This subfamily also includes Drosophila melanogaster Deltex, a ubiquitously expressed cytoplasmic ubiquitin E3 ligase that mediates Notch activation in Drosophila. It selectively suppresses T-cell activation through degradation of a key signaling molecule, MAP kinase kinase kinase 1 (MEKK1). It also inhibits Jun-mediated transcription at the stage of Ras-dependent Jun N-terminal protein kinase (JNK) activation. Deltex contains N-terminal two Notch-binding WWE domains that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a RING finger at the C-terminus
NCPVCLEDLFTSREPVHVLPCGHLMHSTCFEEYLKSGNYRCPLCS
>gnl|CDD|438128 cd16465, RING-H2_PJA1_2, RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and similar proteins. This family includes two highly similar E3 ubiquitin-protein ligases, Praja-1 and Praja-2. Praja-1, also known as RING finger protein 70, is a RING-H2 finger ubiquitin ligase encoded by gene PJA1, a novel human X chromosome gene abundantly expressed in the brain. It has been implicated in bone and liver development, as well as memory formation and X-linked mental retardation (MRX). Praja-1 interacts with and activates the ubiquitin-conjugating enzyme UbcH5B, and shows E2-dependent E3 ubiquitin ligase activity. It is a 3-deazaneplanocin A (DZNep)-induced ubiquitin ligase that directly ubiquitinates individual polycomb repressive complex 2 (PRC2) subunits in a cell free system, which leads to their proteasomal degradation. It also plays an important role in neuronal plasticity, which is the basis for learning and memory. Moreover, Praja-1 ubiquitinates embryonic liver fodrin (ELF) and Smad3, but not Smad4, in a transforming growth factor-beta (TGF-beta)-dependent manner. It controls ELF abundance through ubiquitin-mediated degradation, and further regulates TGF-beta signaling, which plays a key role in the suppression of gastric carcinoma. Praja-1 also regulates the transcription function of the homeodomain protein Dlx5 by controlling the stability of Dlxin-1, via a ubiquitin-dependent degradation pathway. Praja-2, also known as RING finger protein 131, NEURODAP1, or KIAA0438, is an E2-dependent E3 ubiquitin ligase that interacts with and activates the ubiquitin-conjugating enzyme UbcH5B. It functions as an A-kinase anchoring protein (AKAP)-like E3 ubiquitin ligase that plays a critical role in controlling cyclic AMP (cAMP)-dependent PKA activity and pro-survival signaling, and further promotes cell proliferation and growth. Praja-2 is also involved in protein sorting at the postsynaptic density region of axosomatic synapses and possibly plays a role in synaptic communication and plasticity. Together with the AMPK-related kinase SIK2 and the CDK5 activator CDK5R1/p35, it forms a SIK2-p35-PJA2 complex that plays an essential role for glucose homeostasis in pancreatic beta cell functional compensation. Praja-2 ubiquitylates and degrades Mob, a core component of NDR/LATS kinase and a positive regulator of the tumor-suppressor Hippo signaling. Both Praja-1 and Praja-2 contain a potential nuclear localization signal (NLS) and a C-terminal C3H2C3-type RING-H2 motif
CCPICCSEYVKDEIATELPCHHLFHKPCITAWLQKSGTCPVCRHVL
>gnl|CDD|438129 cd16466, RING-H2_RBX2, RING finger, H2 subclass, found in RING-box protein 2 (RBX2) and similar proteins. RBX2, also known as CKII beta-binding protein 1 (CKBBP1), RING finger protein 7 (RNF7), regulator of cullins 2 (ROC2), or sensitive to apoptosis gene protein (SAG), is an E3 ubiquitin-protein ligase that protects cells from apoptosis, confers radioresistance, and plays an essential and non-redundant role in embryogenesis and vasculogenesis. It promotes ubiquitination and degradation of a number of protein substrates, including c-JUN, DEPTOR, HIF-1alpha, IkappaBalpha, NF1, NOXA, p27, and procaspase-3, thus regulating various signaling pathways and biological processes. RBX2 is necessary for ubiquitin ligation activity of the multimeric cullin (Cul)-RING E3 ligases (CRLs). RBX2-containing CRLs are involved in the NEDD8 pathway and RBX2 specifically regulates NEDD8ylation of Cul5. It can bind and activate the HIV-1 Vif-Cullin5 E3 ligase complex in vitro. It is also a substrate of NEDD4-1 E3 ubiquitin ligase and mediates NEDD4-1 induced chemosensitization. The inactivation of RBX2 E3 ubiquitin ligase activity triggers senescence and inhibits Kras-induced immortalization. Endothelial deletion of RBX2 causes embryonic lethality and blocks tumor angiogenesis, and may have potential use in anti-angiogenesis therapy of human cancers. Moreover, as a component of the Cullin 5-RING E3 ubiquitin ligase (CRL5) complex, RBX2 regulates neuronal migration through different CRL5 adaptors, such as SOCS7. RBX2 also functions as a redox inducible antioxidant protein that scavenges oxygen radicals by forming inter- and intra-molecular disulfide bonds when acting alone. It contains a C-terminal C3H2C3-type RING-H2 finger that is essential for its ligase activity
CDTCAICRVQVMDACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDW
>gnl|CDD|438130 cd16467, RING-H2_RNF6-like, RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6, RNF12, and similar proteins. RNF6 is an androgen receptor (AR)-associated protein that induces AR ubiquitination and promotes AR transcriptional activity. RNF6-induced ubiquitination may regulate AR transcriptional activity and specificity by modulating cofactor recruitment. RNF6 is overexpressed in hormone-refractory human prostate cancer tissues and required for prostate cancer cell growth under androgen-depleted conditions. RNF6 also regulates local serine/threonine kinase LIM kinase 1 (LIMK1) levels in axonal growth cones. RNF6-induced LIMK1 polyubiquitination is mediated via K48 of ubiquitin and leads to proteasomal degradation of the kinase. RNF6 binds and upregulates the Inha promoter, and functions as a transcription regulatory protein in the mouse sertoli cell. It acts as a potential tumor suppressor gene involved in the pathogenesis of esophageal squamous cell carcinoma (ESCC). RNF12, also known as LIM domain-interacting RING finger protein, or RING finger LIM domain-binding protein (R-LIM), is an E3 ubiquitin-protein ligase encoded by gene RLIM that is crucial for normal embryonic development in some species and for normal X inactivation in mice. It thus functions as a major sex-specific epigenetic regulator of female mouse nurturing tissues. RNF12 is widely expressed during embryogenesis, and mainly localizes to the cell nucleus, where it regulates the levels of many proteins, including CLIM, LMO, HDAC2, TRF1, SMAD7, and REX1, by proteasomal degradation. Both RNF6 and RNF12 contain a well conserved C3H2C3-type RING-H2 finger
ECTICLGEYETGEKLRRLPCSHEFHSECVDRWLKENSSCPICR
>gnl|CDD|438131 cd16468, RING-H2_RNF11, RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins. RNF11 is an E3 ubiquitin-protein ligase that acts both as an adaptor and a modulator of itch-mediated control of ubiquitination events underlying membrane traffic. It acts downstream of an enzymatic cascade for the ubiquitination of specific substrates. It is also a molecular adaptor of homologous to E6-associated protein C-terminus (HECT)-type ligases. RNF11 has been implicated in the regulation of several signaling pathways. It enhances transforming growth factor receptor (TGFR) signaling by both abrogating Smurf2-mediated receptor ubiquitination and by promoting the Smurf2-mediated degradation of AMSH (associated molecule with the SH3 domain of STAM), a de-ubiquitinating enzyme that enhances TGF-beta signaling and epidermal growth factor receptor (EGFR) endosomal recycling. It also acts directly on Smad4 to enhance Smad4 function, and plays a role in prolonged TGF-beta signaling. RNF11 also functions as a critical component of the A20 ubiquitin-editing protein complex that negatively regulates tumor necrosis factor (TNF)-mediated nuclear factor (NF)-kappaB activation. It interacts with Smad anchor for receptor activation (SARA) and the endosomal sorting complex required for transport (ESCRT)-0 complex, thus participating in the regulation of lysosomal degradation of EGFR. RNF11 acts as a novel GGA cargo actively participating in regulating the ubiquitination of the GGA protein family. RNF11 functions together with TAX1BP1 to target TANK-binding kinase 1 (TBK1)/IkappaB kinase IKKi, and further restricts antiviral signaling and type I interferon (IFN)-beta production. RNF11 contains an N-terminal PPPY motif that binds WW domain-containing proteins such as AIP4/itch, Nedd4 and Smurf1/2 (SMAD-specific E3 ubiquitin-protein ligase 1/2), and a C-terminal C3H2C3-type RING-H2 finger that functions as a scaffold for the coordinated transfer of ubiquitin to substrate proteins together with the E2 enzymes UbcH527 and Ubc13
ECVICMADFVVGDPIRYLPCMHIYHVDCIDDWLMRSFTCPSCM
>gnl|CDD|438132 cd16469, RING-H2_RNF24-like, RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins. This subfamily includes RNF24, RNF122, and similar proteins. RNF24 is an intrinsic membrane protein localized in the Golgi apparatus. It specifically interacts with the ankyrin-repeats domains (ARDs) of TRPC1, -3, -4, -5, -6, and -7, and affects TRPC intracellular trafficking without affecting their activity. RNF122 is a RING finger protein associated with HEK 293T cell viability. It is localized to the endoplasmic reticulum (ER) and the Golgi apparatus, and overexpressed in anaplastic thyroid cancer cells. RNF122 functions as an E3 ubiquitin ligase that can ubiquitinate itself and undergo degradation through its RING finger in a proteasome-dependent manner. Both RNF24 and RNF122 contain an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger
DTCAVCLEEFKLKEELGVCPCGHAFHTKCLKKWLEVRNSCPICKSPV
>gnl|CDD|438133 cd16470, RING-H2_RNF25, RING finger, H2 subclass, found in RING finger protein 25 (RNF25) and similar proteins. RNF25, also known as AO7, is a putative E3 ubiquitin-protein ligase that was initially identified as an interacting protein of the E2 ubiquitin-conjugating enzyme, Ubc5B. It is ubiquitously expressed in various tissues and predominantly localized in the nucleus. RNF25 activates the nuclear factor (NF)-kappaB-dependent gene expression upon stimulation with Interleukin-1 beta (IL-1beta), or tumor necrosis factor (TNF), or overexpression of NF-kappaB-inducing kinase. It interacts with the p65 transactivation domain (TAD) and modulates its transcriptional activity. RNF25 contains an N-terminal RWD domain, a C3H2C3-type RING-H2 finger, and a C-terminal Pro-rich region. Both the RING-H2 finger and the C-terminal regions of RNF25 are necessary for transcriptional activation
PHGQCVICLYGFQEGDAFTKTPCYHYFHSHCLARYIQHMEENLKEEQEEQEERPRAQTEQEQFQVLCPVC
REPL
>gnl|CDD|438134 cd16471, RING-H2_RNF32, RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins. RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, proteins with double RING-H2 fingers may act as scaffolds for binding several proteins that function in the same pathway
ECPICLCAFKGRKCTLLSCSHVFHEACLSAFEKFIESKNQKCPLCR
>gnl|CDD|438135 cd16472, RING-H2_RNF38-like, RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins. This subfamily includes RING finger proteins RNF38, RNF44, and similar proteins. RNF38 is a nuclear E3 ubiquitin protein ligase that plays a role in regulating p53. RNF44 is an uncharacterized RING finger protein that shows high sequence similarity to RNF38. Both RNF38 and RNF44 contain a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C3-type RING-H2 finger. In addition, RNF38 harbors two potential nuclear localization signals
DQTQCVVCMCDYEKRQLLRVLPCSHEFHAKCIDKWLKTNRTCPICR
>gnl|CDD|438136 cd16473, RING-H2_RNF103, RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins. RNF103, also known as KF-1 or zinc finger protein 103 homolog (Zfp-103), is an endoplasmic reticulum (ER)-resident E3 ubiquitin-protein ligase that is widely expressed in many different organs, including brain, heart, kidney, spleen, and lung. It is involved in the ER-associated degradation (ERAD) pathway by interacting with components of the ERAD pathway, including Derlin-1 and VCP. RNF103 contains several hydrophobic regions at its N-terminal and middle regions, as well as a C-terminal C3H2C3-type RING-H2 finger
MLECEECAICLENYQNGDLLRGLPCGHVFHQNCIDVWLERDNHCCPVCRWPVYKD
>gnl|CDD|438137 cd16474, RING-H2_RNF111-like, RING finger, H2 subclass, found in RING finger proteins RNF111, RNF165, and similar proteins. The family includes RING finger proteins RNF111, RNF165, and similar proteins. RNF111, also known as Arkadia, is a nuclear E3 ubiquitin-protein ligase that targets intracellular effectors and modulators of transforming growth factor beta (TGF-beta)/Nodal-related signaling for polyubiquitination and proteasome-dependent degradation. It also interacts with the clathrin-adaptor 2 (AP2) complex and regulates endocytosis of certain cell surface receptors, leading to modulation of epidermal growth factor (EGF) and possibly other signaling pathways. The N-terminal half of RNF111 harbors three SUMO-interacting motifs (SIMs). It thus functions as a SUMO-targeted ubiquitin ligase (STUbL) that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response, as well as triggers degradation of signal-induced polysumoylated proteins, such as the promyelocytic leukemia protein (PML). RNF165, also known as Arkadia-like 2, Arkadia2, or Ark2C, is an E3 ubiquitin ligase with homology to the C-terminal half of RNF111. It is expressed specifically in the nervous system, and can serve to amplify neuronal responses to specific signals. It acts as a positive regulator of bone morphogenetic protein (BMP)-Smad signaling that is involved in motor neuron (MN) axon elongation. Both RNF165 and RNF111 contain a C-terminal C3H2C3-type RING-H2 finger
EKCTICLSDFEEGEDVRRLPCMHLFHQECVDQWLSTNKRCPICRVD
>gnl|CDD|438138 cd16475, RING-H2_RNF121-like, RING finger, H2 subclass, found in RING finger proteins RNF121, RNF175 and similar proteins. This subfamily includes RNF121, RNF175 and similar proteins. RNF121 is an E3-ubiquitin ligase present in the endoplasmic reticulum (ER) and cis-Golgi compartments. It is a novel regulator of apoptosis. It also facilitates the degradation and membrane localization of voltage-gated sodium (NaV) channels, and thus plays a role in the quality control of NaV channels during their synthesis and subsequent transport to the membrane. Moreover, RNF121 acts as a broad regulator of nuclear factor kappaB (NF-kappaB) signaling since its silencing also dampens NF-kappaB activation following stimulation of toll-like receptors (TLRs), nod-like receptors (NLRs), RIG-I-like Receptors (RLRs) or after DNA damage. RNF121 contains five conserved transmembrane (TM) domains and a C3H2C2-type RING-H2 finger. RNF175 is an uncharacterized RING finger protein that shows high sequence similarity with RNF121. This family also includes Arabidopsis RING finger E3 ligase RHA2A, RHA2B, and their homologs. RHA2A is a positive regulator of abscisic acid (ABA) signaling during seed germination and early seedling development. RHA2B may play a role in the ubiquitin-dependent proteolysis pathway that respond to proteasome inhibition. All subfamily members contain a C3H2C3-type RING-H2 finger, which is responsible for E3-ubiquitin ligase activity
NVCAVCGQKLDVDDNEEGIIEKTYKLSCNHVFHEFCIRGWCIVGKKQTCPYCKEK
>gnl|CDD|438139 cd16476, RING-H2_RNF139-like, RING finger, H2 subclass, found in RING finger proteins RNF139, RNF145, and similar proteins. RNF139, also known as translocation in renal carcinoma on chromosome 8 protein (TRC8), is an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. It is a tumor suppressor that has been implicated in a novel regulatory relationship linking the cholesterol/lipid biosynthetic pathway with cellular growth control. A mutation in RNF139 has been identified in families with hereditary renal (RCC) and thyroid cancers. RNF145 is an uncharacterized RING finger protein encoded by the RNF145 gene, which is expressed in T lymphocytes, and its expression is altered in acute myelomonocytic and acute promyelocytic leukemias. Although its biological function remains unclear, RNF145 shows high sequence similarity with RNF139. Both RNF139 and RNF145 contain a C3H2C3-type RING-H2 finger with possible E3-ubiquitin ligase activity
DVCAICYQEMKEARITPCNHFFHGLCLRKWLYVQDTCPLCH
>gnl|CDD|438140 cd16477, RING-H2_RNF214, RING finger, H2 subclass, found in RING finger protein 214 (RNF214) and similar proteins. RNF214 is an uncharacterized RING finger protein containing a C3H2C3-type RING-H2 finger, suggesting it may have E3-ubiquitin ligase activity
KLCLMCQKLVQPSDLHPMSCSHTVHKECIKFWAQSNKNNTCPFCP
>gnl|CDD|438141 cd16478, RING-H2_Rapsyn, RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) and similar proteins. Rapsyn, also known as acetylcholine receptor (AChR)-associated 43 kDa protein or RING finger protein 205 (RNF205), is a 43 kDa postsynaptic protein that plays an essential role in the clustering and maintenance of AChR in the postsynaptic membrane of the motor endplate. AChRs enable the transport of rapsyn from the Golgi complex to the plasma membrane through a molecule-specific interaction. Rapsyn also mediates subsynaptic anchoring of protein kinase A (PKA) type I in close proximity to the postsynaptic membrane, which is essential for synapse maintenance. Its mutations in humans cause endplate AChR deficiency and myasthenic syndrome. Rapsyn contains an N-terminal myristoylation signal required for membrane association, seven tetratricopeptide repeats (TPRs) that subserve rapsyn self-association, a coiled-coil domain responsible for the binding of determinants within the long cytoplasmic loop of each AChR subunit, a C3H2C3-type RING-H2 finger that binds to the cytoplasmic domain of beta-dystroglycan and to S-NRAP and links rapsyn to the subsynaptic cytoskeleton, and a serine phosphorylation site
ELFCGMCGESIGEKNEQLQALPCSHIFHLKCLQTNLRGGTRGCPNCRR
>gnl|CDD|438142 cd16479, RING-H2_synoviolin, RING finger, H2 subclass, found in synoviolin and similar proteins. Synoviolin, also known as synovial apoptosis inhibitor 1 (Syvn1), Hrd1, or Der3, is an endoplasmic reticulum (ER)-anchoring E3 ubiquitin ligase that functions as a suppressor of ER stress-induced apoptosis and plays a role in homeostasis maintenance. It also targets tumor suppressor gene p53 for proteasomal degradation, suggesting crosstalk between ER associated degradation (ERAD) and p53 mediated apoptotic pathway under ER stress. Moreover, synoviolin controls body weight and mitochondrial biogenesis through negative regulation of the thermogenic coactivator peroxisome proliferator-activated receptor coactivator (PGC)-1beta. It upregulates amyloid beta production by targeting a negative regulator of gamma-secretase, Retention in endoplasmic reticulum 1 (Rer1), for degradation. It is also involved in the degradation of endogenous immature nicastrin, and affects amyloid beta-protein generation. Moreover, synoviolin is highly expressed in rheumatoid synovial cells and may be involved in the pathogenesis of rheumatoid arthritis (RA). It functions as an anti-apoptotic factor that is responsible for the outgrowth of synovial cells during the development of RA. It promotes inositol-requiring enzyme 1 (IRE1) ubiquitination and degradation in synovial fibroblasts with collagen-induced arthritis. Furthermore, the upregulation of synoviolin may represent a protective response against neurodegeneration in Parkinson's disease (PD). In addition, synoviolin is involved in liver fibrogenesis. Synoviolin contains a C3H2C2-type RING-H2 finger
DNTCIICREEMTVGAKKLPCGHIFHLSCLRSWLQRQQTCPTCR
>gnl|CDD|438143 cd16480, RING-H2_TRAIP, RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins. TRAIP, also known as RING finger protein 206 (RNF206) or TRIP, is a ubiquitously expressed nucleolar E3 ubiquitin ligase important for cellular proliferation and differentiation. It is found near mitotic chromosomes and functions as a regulator of the spindle assembly checkpoint. TRAIP interacts with tumor necrosis factor (TNF)-receptor-associated factor (TRAF) proteins and inhibits TNF-alpha-mediated nuclear factor (NF)-kappaB activation. It also interacts with two tumor suppressors CYLD and spleen tyrosine kinase (Syk), and DNA polymerase eta, which facilitates translesional synthesis after DNA damage. TRAIP contains an N-terminal C3H2C2-type RING-H2 finger and an extended coiled-coil domain
YCTICSDFFDNSRDVAAIHCGHTFHYDCLLQWFDTSRTCPQCR
>gnl|CDD|438144 cd16481, RING-H2_TTC3, RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar proteins. TTC3, also known as protein DCRR1, TPR repeat protein D, TPR repeat protein 3, or RING finger protein 105 (RNF105), is an E3 ubiquitin-protein ligase encoded by a gene within the Down syndrome (DS) critical region on chromosome 21. It affects differentiation and Golgi compactness in neurons through specific actin-regulating pathways. It inhibits the neuronal-like differentiation of pheocromocytoma cells by activating RhoA and by binding to Citron proteins. TTC3 is an Akt-specific E3 ligase that binds to phosphorylated Akt and facilitates its ubiquitination and degradation within the nucleus. It contains four N-terminal TPR motifs, a potential coiled-coil region and a Citron binding region in the central part, and a C-terminal C3H2C2-type RING-H2 finger
PCIICHDDLKPDQLAKLECGHIFHKECIKQWLKEQSTCPTCRVHV
>gnl|CDD|438145 cd16482, RING-H2_UBR1-like, RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), and similar proteins. Two UBR family members, UBR1 and UBR2, are major N-recognin ubiquitin ligases that both function in the N-end rule degradation pathway. They can recognize substrate proteins with type-1 (basic) and type-2 (bulky hydrophobic) N-terminal residues as part of N-degrons and an internal lysine residue for ubiquitin conjugation. They also function in a quality control pathway for degradation of unfolded cytosolic proteins. Their action is stimulated by Hsp70. Moreover, UBR1 and UBR2 are negative regulators of the leucine-mTOR signaling pathway. Leucine might activate this pathway in part through inhibition of their ubiquitin ligase activity. In yeast, only one E3, encoded by UBR1, mediates the recognition of substrates by the N-end rule pathway. Saccharomyces cerevisiae UBR1 also functions as an additional E3 ligase in the endoplasmic reticulum-associated protein degradation (ERAD). It can provide ubiquitin ligation activity for the ERAD substrate mutated Ste6 (sterile). Schizosaccharomyces pombe UBR1 is a critical regulator that influences the oxidative stress response via degradation of active Pap1 basic leucine zipper (bZIP) transcription factor in the nucleus. Both UBR1 and UBR2 contain an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain
TCILCQEGLHISSCGHVMHYDCWQRYFDSVRLREQRRPAFRRHHSEDVSKGEFLCPLCKSLSNTVLP
>gnl|CDD|438146 cd16483, RING-H2_UBR3, RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins. UBR3, also known as N-recognin-3, E3alpha-III, or zinc finger protein 650, is an E3 ubiquitin-protein ligase targeting the essential DNA repair protein APE1, also known as Ref-1, for ubiquitylation. It regulates cellular levels of APE1 and is required for genome stability. It also plays a regulatory role in sensory pathways, including olfaction. In Drosophila, UBR3 also regulates apoptosis by controlling the activity of Drosophila inhibitor of apoptosis protein 1 (DIAP1), which is required to prevent caspase activation. UBR3 contains an N-terminal ubiquitin-recognin (UBR) box, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain
YDCVICGQSGVHVQTCGHYIHIDCHKSYLESLRQDQVGLQLLSVRRGEFTCPLCRQLSNSVLP
>gnl|CDD|438147 cd16484, RING-H2_Vps, RING finger, H2 subclass, found in vacuolar protein sorting-associated proteins Vps8, Vps11, Vps18, Vps41, and similar proteins. This subfamily corresponds to a group of vacuolar protein sorting-associated proteins containing a C-terminal C3H2C3-type RING-H2 finger, which includes Vps8, Vps11, Vps18, and Vps41. Vps11 and Vps18 associate with Vps16 and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form
KCPICTLPLKESDVGANSPVVVFFCGHMFHKFCLPELSMTEAACPICL
>gnl|CDD|438148 cd16485, mRING-H2-C3H2C2D_RBX1, modified RING finger, H2 subclass (C3H2C2D-type), found in RING-box protein 1 (RBX1) and similar proteins. RBX1, also known as Hrt1, protein ZYP, RING finger protein 75 (RNF75), or regulator of cullins 1 (ROC1), is an E3 ubiquitin-protein ligase necessary for ubiquitin ligation activity of multimeric cullin (Cul)-RING E3 ligases (CRLs). RBX1-containing CRLs are involved in the NEDD8 pathway; RBX1 specifically regulates NEDD8ylation of Cul1-4. It can also bind and activate HIV-1 Vif-Cullin5 E3 ligase complex in vitro. Moreover, RBX1 is an essential element of Skp1/Cullin/F-box (SCF) E3-ubiquitin ligase complexes that target diverse proteins for proteasome-mediated degradation. It is a direct functional target of miR-194 and plays an important role in proliferation and migration of gastric cancer (GC) cells. RBX1 is also an essential component of KEAP1/CUL3/RBX1 E3-ubiquitin ligase complex that functions as a regulator of NFE2-related factor 2 (NRF2) and plays a key role in NRF2 pathway deregulation in multiple tumor types, including ovarian carcinomas (OVCA) and papillary thyroid carcinoma (PTC). Furthermore, RBX1 associates with DDB1, Cul4A, and Fbxw5 to form the Fbxw5-DDB1-Cul4A-Rbx1 complex that may function as a dual SUMO/ubiquitin ligase suppressing c-Myb activity through sumoylation or ubiquitination. RBX1 contains a C-terminal modified RING-H2 finger that is of C3H2C2D-type, rather than the canonical C3H2C3-type. The modified RING-H2 finger is essential for its ligase activity
DNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREW
>gnl|CDD|438149 cd16486, mRING-H2-C3H2C2D_ZSWM2, Modified RING finger, H2 subclass (C3H2C2D-type), found in zinc finger SWIM domain-containing protein 2 (ZSWIM2) and similar proteins. ZSWIM2, also known as MEKK1-related protein X (MEX) or ZZ-type zinc finger-containing protein 2, is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis through Fas, death receptor (DR) 3 and DR4 signaling. ZSWIM2 is self-ubiquitinated and targeted for degradation through the proteasome pathway. It acts as an E3 ubiquitin ligase, through the E2, Ub-conjugating enzymes UbcH5a, UbcH5c, or UbcH6. ZSWIM2 contains four putative zinc-binding domains including an N-terminal SWIM (SWI2/SNF2 and MuDR) domain critical for its ubiquitination, and two modified RING-H2 fingers separated by a ZZ zinc finger domain, which was required for interaction with UbcH5a and its self-association. This model corresponds to the second RING-H2 finger, which is not a canonical C3H2C3-type, but a modified C3H2C2D-type
QCRICLKAFQLGQHVRTLPCRHKFHRDCIDNWLLHSRNSCPIDGQVVYN
>gnl|CDD|438150 cd16487, mRING-H2-C3DHC3_ZFPL1, Modified RING finger, H2 subclass (C3DHC3-type), found in zinc finger protein-like 1 (ZFPL1) and similar proteins. ZFPL1, also known as zinc finger protein MCG4, is a novel mitotic Golgi phosphoprotein required for cis-Golgi integrity and efficient endoplasmic reticulum (ER)-to-Golgi transport via directly interacting with the cis-Golgi matrix protein GM130. ZFPL1 is a widely expressed integral membrane protein with two predicted zinc fingers at its N-terminus. One is a novel type of zinc finger, and the other is a modified RING-H2 finger that lacks the fourth zinc-binding residue of the consensus C3H2C3-type RING-H2 finger. It also contains a bipartite nuclear localization signal (NLS), and a leucine zipper at the C-terminus
DPNCTLCNTSLANGDVVRLVCYDLFHWSCLNEYAAQLPANTAPAGYTCPQCKGPIFP
>gnl|CDD|438151 cd16488, mRING-H2-C3H3C2_Mio-like, Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and its homologs. This subfamily contains Mio, WDR24, WDR59, and their counterparts Sea4, Sea2, and Sea3 from yeast, respectively. Mio/Sea4, Sea2/WDR24, and Sea3/WDR59 are components of the GATOR2 complex, which also includes another two subunits, Seh1and Sec13. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. All subfamily members contain an N-terminal WD40 domain and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type
SCAICHLPVKGLSSFCLNCGHGGHAECIREWFEDHTECPTGCGC
>gnl|CDD|438152 cd16489, mRING-CH-C4HC2H_ZNRF, Modified RING-CH finger, H2 subclass (C4HC2H-type), found in the ZNRF family. The ZNRF family includes zinc/RING finger proteins ZNRF1, ZNRF2, and similar proteins. It has been characterized by containing a unique combination of zinc finger-RING finger motifs in the C-terminal region, which is evolutionarily conserved in a wide range of species, including Caenorhabditis elegans and Drosophila. ZNRF proteins function as E3 ubiquitin ligases and are highly expressed in central nervous system (CNS) and peripheral nervous system (PNS) neurons, particularly during development and in adulthood. ZNRF1 and ZNRF2 are differentially localized within the synaptic region. ZNRF1 is associated with synaptic vesicle membranes, whereas ZNRF2 is present in presynaptic plasma membranes. They are N-myrisotoylated and also located in the endosome-lysosome compartment in fibroblasts. ZNRF proteins may play a role in the establishment and maintenance of neuronal transmission and plasticity via their ubiquitin ligase activity, as well as in regulating Ca2+-dependent exocytosis. The RING fingers found in ZNRF proteins are modified as C4HC2H-type RING-CH finger, rather than the typical C4HC3-type RING-CH finger, which is a variant of the RING-H2 finger
ECVICLEELEAGDTIARLPCLCIYHKKCIDDWFEVNRSCPEHP
>gnl|CDD|438153 cd16490, RING-CH-C4HC3_FANCL, RING-CH finger, H2 subclass (C4HC3-type), found in Fanconi anemia group L protein (FANCL) and similar proteins. FANCL, also known as fanconi anemia-associated polypeptide of 43 kDa (FAAP43) or PHF9, is a monomeric RING E3 ubiquitin-protein ligase that monoubiquitinates FANCD2 and FANCI. The monoubiquitinated FANCD2-FANCI heterodimer complex in turn recruits key proteins involved in homologous recombination and DNA repair. FANCL is also one of seven components in Fanconi anemia (FA) nuclear core complex, which provides the essential E3 ligase function for spatially defined FANCD2 ubiquitination and FA pathway activation. In the FA core complex, FANCL associates with FANCB and FAAP100 to constitute a catalytic subcomplex that functions as the monoubiquitination module. FANCL specifically interacts with the E2 ubiquitin-conjugating (UBC) enzyme Ube2T to make an E3-E2 pair, which is the catalytic center of the Fanconi Anemia (FA) pathway required for DNA interstrand crosslink repair. Moreover, FANCL has a noncanonical function to regulate the Wnt/beta-catenin signaling, a pathway involved in hematopoietic stem cell self-renewal. It functionally enhances beta-catenin activity by ubiquitinating beta-catenin, with atypical ubiquitin chains (K11 linked). FANCL contains an N-terminal E2-like fold (ELF) domain, a novel double-RWD (DRWD) domain with a clear hydrophobic core, and a C-terminal C4HC3-type RING-CH finger. The DRWD domain is required for substrate binding. The RING-CH finger, also known as vRING or RINGv, is predicted to facilitate E2 binding. It has an unusual arrangement of zinc-coordinating residues. Its cysteines and histidines are arranged in the sequence as C4HC3-type, rather than the C3H2C3-type in canonical RING-H2 finger
ECGICYAYRLDGEVPDQVCDNARCGQPFHQSCLYEWLRSLPSTRQSFNTIFGECPYCS
>gnl|CDD|438154 cd16491, RING-CH-C4HC3_LTN1, RING-CH finger, H2 subclass (C4HC3-type), found in E3 ubiquitin-protein ligase listerin and similar proteins. Listerin, also known as RING finger protein 160 or zinc finger protein 294, is the mammalian homolog of yeast Ltn1. It is widely expressed in all tissues, but motor and sensory neurons and neuronal processes in the brainstem and spinal cord are primarily affected in the mutant. Listerin is required for embryonic development and plays an important role in neurodegeneration. It also functions as a critical E3 ligase involving quality control of nonstop proteins. It mediates ubiquitylation of aberrant proteins that become stalled on ribosomes during translation. Ltn1 works with several cofactors to form a large ribosomal subunit-associated quality control complex (RQC), which mediates the ubiquitylation and extraction of ribosome-stalled nascent polypeptide chains for proteasomal degradation. It appears to first associate with nascent chain-stalled 60S subunits together with two proteins of unknown function, Tae2 and Rqc1. Listerin contains a long stretch of HEAT (Huntingtin, Elongation factor 3, PR65/A subunit of protein phosphatase 2A, and TOR) or ARM (Armadillo) repeats in the N terminus and middle region, and a catalytic RING-CH finger, also known as vRING or RINGv, with an unusual arrangement of zinc-coordinating residues in the C-terminus . Its cysteines and histidines are arranged in the sequence as C4HC3-type, rather than the C3H2C3-type in canonical RING-H2 finger
EECPICYSVIHGSNHSLPKLKCKTCKNKFHSACLYKWFRSSNKSTCPLCR
>gnl|CDD|438155 cd16492, RING-CH-C4HC3_NFX1-like, RING-CH finger, H2 subclass (C4HC3-type), found in transcriptional repressor NF-X1, NF-X1-type zinc finger protein NFXL1, and similar proteins. NF-X1, also known as nuclear transcription factor, X box-binding protein 1, is a novel cysteine-rich sequence-specific DNA-binding protein that interacts with the conserved X-box motif of the human major histocompatibility complex (MHC) class II genes via a repeated Cys-His domain. It functions as a cytokine-inducible transcriptional repressor that plays an important role in regulating the duration of an inflammatory response by limiting the period in which class II MHC molecules are induced by interferon gamma (IFN- gamma). NFXL1, also known as NF-X1-type zinc finger protein NFXL1 or ovarian zinc finger protein (OZFP), is encoded by a novel human cytoplasm-distribution zinc finger protein (CDZFP) gene. This subfamily also includes NF-X1 homologs from insects, plants, and fungi. Drosophila melanogaster shuttle craft (STC) is a DNA- or RNA-binding protein required for proper axon guidance in the central nervous system. It functions as a putative transcription factor and plays an essential role in the completion of embryonic development. In contrast to NF-X1, STC contains an RD domain. The Arabidopsis genome encodes two NF-X1 homologs, AtNFXL1 and AtNFXL2, both of which function as regulators of salt stress responses. The AtNFXL1 protein is a nuclear factor that positively affects adaptation to salt stress. It also functions as a negative regulator of the type A trichothecene phytotoxin-induced defense response. AtNFXL2 controls abscisic acid (ABA) levels and suppresses ABA responses. It may also prevent unnecessary and costly stress adaptation under favorable conditions. FKBP12-associated protein 1 (FAP1) is a dosage suppressor of rapamycin toxicity in budding yeast. It is localized in the cytoplasm, but upon rapamycin treatment translocates to the nucleus. FAP1 interacts with FKBP12 in a rapamycin-sensitive manner. It is a proline-rich protein containing a novel cysteine-rich DNA-binding motif. Unique structural features of the NFX1 and NFXL proteins are the Cys-rich region and a specific RING-CH finger motif with an unusual arrangement of zinc-coordinating residues. The Cys-rich region is required for binding to specific promoter elements. It frequently comprises more than 500 amino acids and harbors several NFX1-type zinc finger domains, characterized by the pattern C-X(1-6)-H-X-C-X3-C(H/C)-X(3-4)-(H/C)-X(1-10)-C. The RING-CH finger, also known as vRING or RINGv, may have E3 ligase activity. It is characterized by a C4HC3-type Zn ligand signature and additional conserved amino acids, rather than the C3H2C3-type cysteines and histidines arrangement in canonical RING-H2 finger. In addition to the Cys-rich region and RING-CH finger, NFX1 contains a PAM2 motif in the N-terminus and a R3H domain in the C-terminus
YECMICTENVGRNQSIWSCSRCYRVFHLSCIKKWAKNSEEKAEQVKNDDDSWRCPGCQ
>gnl|CDD|438156 cd16493, RING-CH-C4HC3_NSE1, RING-CH finger, H2 subclass (C4HC3-type), found in non-structural maintenance of chromosomes (SMC) element 1 homolog (NSE1) and similar proteins. NSE1, also known as non-SMC element 1 homolog (NSMCE1), is an E3 ubiquitin ligase that contains a C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger. Together with its partner proteins NSE3 and NSE4, it forms a tight subcomplex of the SMC5-6 complex, which includes another two subcomplexes, SMC6-SMC5-NSE2 and NSE5-NSE6. The vRING finger is essential for normal NSE1-NSE3-NSE4 trimer formation in vitro and for damage-induced recruitment of NSE4 and SMC5 to subnuclear foci in vivo. Thus it functions as a protein-protein interaction domain required for SMC5-6 holocomplex integrity and recruitment to, or retention at, DNA lesions. The C-terminal half of NSE1, including the vRING finger, is required for DNA damage resistance and mitotic fidelity of SMC5-6 complex in the fission yeast Schizosaccharomyces pombe. The RING-CH finger may play an important role in Rad52-dependent post-replication repair of UV-damaged DNA in Saccharomyces cerevisiae
KSCNICHEIVIQGQSCPNEDCGIRLHLYCAKRYFRRRAEPRCPSCNTPW
>gnl|CDD|438157 cd16494, RING-CH-C4HC3_ZSWM2, RING-CH finger, H2 subclass (C4HC3-type), found in zinc finger SWIM domain-containing protein 2 (ZSWIM2) and similar proteins. ZSWIM2, also known as MEKK1-related protein X (MEX) or ZZ-type zinc finger-containing protein 2, is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis through Fas, death receptor (DR) 3, and DR4 signaling. ZSWIM2 is self-ubiquitinated and targeted for degradation through the proteasome pathway. It also acts as an E3 ubiquitin ligase, through the E2, Ub-conjugating enzymes UbcH5a, UbcH5c, or UbcH6. ZSWIM2 contains four putative zinc-binding domains including an N-terminal SWIM (SWI2/SNF2 and MuDR) domain critical for its ubiquitination and two RING fingers separated by a ZZ zinc finger domain, which was required for interaction with UbcH5a and its self-association. This model corresponds to the first RING finger, which is a C4HC3-type RING-CH finger, also known as vRING or RINGv, rather than the canonical C3H2C3-type RING-H2 finger
EDDCPICYEEMLEKGEPLTYCRFGCGNNVHIHCMKVWAEHQRQSDEPVTCPLCRSDW
>gnl|CDD|438158 cd16495, RING_CH-C4HC3_MARCH, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING-CH proteins (MARCH). This family of membrane-associated E3 ubiquitin ligases consists of 11 members in mammals (MARCH1-11), which are characterized by containing an N-terminal C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of the C3H2C3-type RING-H2 finger). Most family members have hydrophobic transmembrane regions and are localized to the plasma membrane and intracellular organelle membrane. Only MARCH7 and MARCH10 are predicted to have no transmembrane spanning region. MARCH proteins have been implicated in mediating the ubiquitination and subsequent down-regulation of cell-surface immune regulatory molecules, such as major histocompatibility complex class II and CD86, as well as in endoplasmic reticulum-associated degradation, endosomal protein trafficking, mitochondrial dynamics, and spermatogenesis
CRICLEEEEEGEPLISPCRCKGSLKYVHRECLKRWLTESGNRSNTKCEICK
>gnl|CDD|438159 cd16496, RING-HC_BARD1, RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar proteins. BARD-1 is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an C3HC4-type RING-HC finger that binds BRCA1 at its N-terminus and three tandem ankyrin repeats and tandem BRCT repeat domains at its C-terminus. The BRCT repeats bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage
KWARTRAALDELENLLRCSRCASILKEPVTLGGCEHVFCRSCVGDRLGNGCPVCDTPAWARDLQINRQLD
SMVQLCRKLRNLLNDN
>gnl|CDD|438160 cd16497, RING-HC_BAR, RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR). BAR, also known as RING finger protein 47, was originally identified as an inhibitor of Bax-induced apoptosis. It participates in the block of apoptosis induced by TNF-family death receptors (extrinsic pathway) and mitochondria-dependent apoptosis (intrinsic pathway). BAR is predominantly expressed by neurons in the central nervous system and is involved in the regulation of neuronal survival. It is an endoplasmic reticulum (ER)-associated RING-type E3 ubiquitin ligase that interacts with BI-1 protein and post-translationally regulates its stability, as well as functioning in ER stress. BAR contains an N-terminal C3HC4-type RING-HC finger, a SAM domain, a coiled-coil domain, and a C-terminal transmembrane (TM) domain. This model corresponds to the RING-HC finger responsible for the binding of ubiquitin conjugating enzymes (E2s)
EFLCHCCYDLLVNPTTLNCGHSFCRHCLALWWKSSKKTECPECRQKWEGFPK
>gnl|CDD|438161 cd16498, RING-HC_BRCA1, RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins. BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by the tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus
SRIERVQEVISAMQKNLECPICLELLKEPVSTKCDHQFCRFCILKLLQKKKKPAPCPLCKKSVTKRSLQE
STRFKQLVEAVKKLIDAFELDTGL
>gnl|CDD|438162 cd16499, RING-HC_Bre1-like, RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes. Bre1 is an E3 ubiquitin-protein ligase that catalyzes monoubiquitination of histone H2B in concert with the E2 ubiquitin-conjugating enzyme, Rad6. The Rad6-Bre1-mediated histone H2B ubiquitylation modulates the formation of double-strand breaks (DSBs) during meiosis in yeast. it is also required, indirectly, for the methylation of histone 3 on lysine 4 (H3K4) and 79. RNF20, also known as BRE1A and RNF40, also known as BRE1B, are the mammalian homologs of Bre1. They work together to form a heterodimeric Bre1 complex that facilitate the K120 monoubiquitination of histone H2B (H2Bub1), a DNA damage-induced histone modification that is crucial for recruitment of the chromatin remodeler SNF2h to DNA double-strand break (DSB) damage sites. Moreover, the Bre1 complex acts as a tumor suppressor, augmenting expression of select tumor suppressor genes and suppressing select oncogenes. Deficiency in the mammalian histone H2B ubiquitin ligase Bre1 leads to replication stress and chromosomal instability. All subfamily members contain a C3HC4-type RING-HC finger at its C-terminus
KDLRELLKCSVCNDRFKDVIITKCGHVFCNECVQKRLETRQRKCPGCGKAFGANDVQRI
>gnl|CDD|438163 cd16500, RING-HC_CARP, RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, CARP-2 and similar proteins. The CARP subfamily includes CARP-1 and CARP-2 proteins, both of which are E3 ubiquitin ligases that ubiquitinate apical caspases and target them for proteasome-mediated degradation. As a novel group of caspase regulators with a FYVE-type zinc finger domain, they do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8, and caspase 10. Moreover, they stabilize MDM2 by inhibiting MDM2 self-ubiquitination, as well as by targeting 14-3-3sigma for degradation. They work together with MDM2 to enhance p53 degradation, thereby inhibiting p53-mediated cell death. CARPs contain an N-terminal FYVE-like domain that can serve as a membrane-targeting or endosome localizing signal and a C-terminal C3HC4-type RING-HC finger domain
DLCKICMDAAIDCVLLECGHMVTCTDCGKKLSECPICRQYVVRVVHFF
>gnl|CDD|438164 cd16501, RING-HC_CblA-like, RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and similar proteins. CblA is a Dictyostelium homolog of the Cbl proteins which are multi-domain proteins acting as key negative regulators of various receptor and non-receptor tyrosine kinase signaling. CblA upregulates STATc tyrosine phosphorylation by downregulating PTP3, the protein tyrosine phosphatase responsible for dephosphorylating STATc. STATc is a signal transducer and activator of transcription protein. Like other Cbl proteins, CblA contains a tyrosine-kinase-binding domain (TKB), a proline-rich domain, a C3HC4-type RING-HC finger, and an ubiquitin-associated (UBA) domain. TKB, also known as a phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain. This family also includes Drosophila melanogaster defense repressor 1 (Dnr1) that was identified as an inhibitor of Dredd activity in the absence of a microbial insult in Drosophila S2 cells. It inhibits the Drosophila initiator caspases Dredd and Dronc. Moreover, Dnr1 acts as a negative regulator of the Imd (immune deficiency) innate immune-response pathway. Its mutations cause neurodegeneration in Drosophila by activating the innate immune response in the brain. Dnr1 contains a FERM N-terminal domain followed by a region rich in glutamine and serine residues, a central FERM domain, and a C-terminal C3HC4-type RING-HC finger
SGADADLCVVCMDAPIDTVFLECGHLACCRLCSKRLRVCPICRQPISRVVRIF
>gnl|CDD|438165 cd16502, RING-HC_Cbl-like, RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins. The Cbl adaptor protein family contains a small class of RING-type E3 ubiquitin ligases with oncogenic activity, which is represented by three mammalian members, c-Cbl, Cbl-b and Cbl-c, as well as two invertebrate Cbl-family proteins, D-Cbl in Drosophila and Sli-1 in C. elegans. Cbl proteins function as potent negative regulators of various signaling cascades in a wide range of cell types. They play roles in ubiquitinating activated tyrosine kinases and targeting them for degradation. D-Cbl associates with the Drosophila epidermal growth factor receptor (EGFR) and overexpression of D-Cbl in the eye of Drosophila embryos inhibits EGFR-dependent photoreceptor cell development. Sli-1 is a negative regulator of the Let-23 receptor tyrosine kinase, an EGFR homolog, in vulva development. Cbl proteins in this subfamily consist of a highly conserved N-terminal half that includes a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain) and a C3HC4-type RING-HC finger, both of which are required for Cbl-mediated downregulation of RTKs, and a divergent C-terminal region
FQLCKICAENDKDVRIEPCGHLLCTPCLTSWQDSDGQTCPFCR
>gnl|CDD|438166 cd16503, RING-HC_CHFR, RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein (CHFR). CHFR, also known as RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22, and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression, and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated (FHA) domain and a C3HC4-type RING-HC finger
ENLTCSICQDLLHDCVSLQPCMHNFCAACYSDWMERSNTECPTCRATVQRVNKNH
>gnl|CDD|438167 cd16504, RING-HC_COP1, RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and similar proteins. COP1, also known as RING finger and WD repeat domain protein 2 (RFWD2) or RING finger protein 200 (RNF200), is a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. It is localized predominantly in the nucleus, but may also be present in the cytosol. Mammalian COP1 functions as an E3 ubiquitin-protein ligase that interacts with Jun transcription factors and modulates their transcriptional activity. It also interacts with and negatively regulates the tumor-suppressor protein p53. Moreover, COP1 associates with COP9 signalosome subunit 6 (CSN6), and is involved in 14-3-3sigma ubiquitin-mediated degradation. The CSN6-COP1 link enhances ubiquitin-mediated degradation of p27(Kip1), a critical CDK inhibitor involved in cell cycle regulation, to promote cancer cell growth. Furthermore, COP1 functions as the negative regulator of ETV1 and influences prognosis in triple-negative breast cancer. COP1 contains an N-terminal extension, a C3HC4-type RING-HC finger, a coiled coil domain, and seven WD40 repeats. In human COP1, a classic leucine-rich NES, and a novel bipartite NLS is bridged by the RING-HC finger
NDFLCPICFDIIKEAFVTKCGHSFCYKCIVKHLEQKNRCPKCNFYLT
>gnl|CDD|438168 cd16505, RING-HC_CYHR1, RING finger, HC subclass, found in cysteine and histidine-rich protein 1 (CYHR1) and similar proteins. CYHR1, also known as cysteine/histidine-rich protein (Chrp), shows sequence similarity with the Drosophila RING finger protein Seven-in-Absentia (sina) and its murine and human siah homologs. It is a novel prognostic marker that may work as a therapeutic target in patients with esophageal squamous cell carcinoma. It is also a biomarker of the response to erythropoietin in hemodialysis patients. CYHR1 contains an N-terminal C3HC4-type RING-HC finger and a C-terminal tumor necrosis factor (TNF) receptor associated factor (TRAF)-like substrate-binding domain (SBD)
KLEERLNGILCCTVCLDLPKSAVYQCTNGHLMCAGCFNHLLADARLKDEQATCPNCRCEISK
>gnl|CDD|438169 cd16506, RING-HC_DTX3-like, RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like (DTX3L) and similar proteins. This subfamily contains Deltex3 (DTX3) and Deltex-3-like (DTX3L), both of which are E3 ubiquitin-protein ligases belonging to the Deltex (DTX) family. DTX3, also known as RING finger protein 154 (RNF154), has a biological function that remains unclear. DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. In contrast to other DTXs, both DTX3 and DTX3L contain a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N termini and further enhance self-ubiquitination
DTCPICLDEIQNKKTLEKCKHSFCEDCIDRALQVKPVCPVCGVVY
>gnl|CDD|438170 cd16507, RING-HC_GEFO-like, RING finger, HC subclass, found in Dictyostelium discoideum Ras guanine nucleotide exchange factor O (RasGEFO) and similar proteins. RasGEFO, also known as RasGEF domain-containing protein O, functions as a Ras guanine-nucleotide exchange factor (RasGEFs), activating Ras by catalyzing the replacement of GDP with GTP. RasGEFs are particularly important for signaling in development and chemotaxis in many organisms, including Dictyostelium. RasGEFO contains a C3HC4-type RING-HC finger that may be responsible for E3 ubiquitin ligase activity
SKSLNLLQSLTCGICQNLFKDPNTLIPCGHAFCLDCLTTNASIKNCIQCKVEYTTYIP
>gnl|CDD|438171 cd16508, RING-HC_HAKAI-like, RING finger, HC subclass, found in E3 ubiquitin-protein ligase Hakai, zinc finger protein 645 (ZNF645), and similar proteins. Hakai, also known as Casitas B-lineage lymphoma-transforming sequence-like protein 1, RING finger protein 188 (RNF188), or c-Cbl-like protein 1 (CBLL1), is an E3 ubiquitin ligase that disrupts cell-cell contacts in epithelial cells and is upregulated in human colon and gastric adenocarcinomas. It was identified to mediate the posttranslational downregulation of E-cadherin (CDH1), a major component of adherens junctions in epithelial cells and a potent tumor suppressor. It also promotes ubiquitination of several other tyrosine-phosphorylated Src substrates, including cortactin (CTTN) and DOK1. Hakai acts as a homodimer arranged in an anti-parallel configuration with a novel HYB (Hakai pTyr-binding) domain that forms a phosphotyrosine-binding pocket. Each monomer contains a C3HC4-type RING-HC finger and a short pTyr-B domain that incorporates a novel, atypical C2H2-type Zn-finger coordination motif. Both domains are important for dimerization. ZNF645 is a novel testis-specific E3 ubiquitin-protein ligase that plays a role in sperm production and quality control. It has a structure similar to that of the c-Cbl-like protein Hakai. In contrast to Hakai, its HYB domain demonstrates different target specificities. It interacts with v-Src-phosphorylated E-cadherin, but not to cortactin
HFCDKCDLPIKIYGRMIPCKHVFCLDCARLHDKICPRCDDPVQRIEQCTRG
>gnl|CDD|438172 cd16509, RING-HC_HLTF, RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar proteins. HLTF, also known as DNA-binding protein/plasminogen activator inhibitor 1 regulator, HIP116, RING finger protein 80, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3, or sucrose nonfermenting protein 2-like 3, is a yeast RAD5 homolog found in mammals. It has both E3 ubiquitin ligase and DNA helicase activities, and plays a pivotal role in the template-switching pathway of DNA damage tolerance. It is involved in Lys-63-linked poly-ubiquitination of proliferating cell nuclear antigen (PCNA) at Lys-164 and in the regulation of DNA damage tolerance. It shows double-stranded DNA translocase activity with 3'-5' polarity, thereby facilitating regression of the replication fork. HLTF contains an N-terminal HIRAN (HIP116 and RAD5 N-terminal) domain, a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA
GSDEECAICLDSLTNPVITPCAHVFCRRCICEVIQREKAKCPMCRAPLSASDL
>gnl|CDD|438173 cd16510, RING-HC_IAPs, RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs). IAPs are frequently overexpressed in cancer and associated with tumor cell survival, chemoresistance, disease progression, and poor prognosis. They function primarily as negative regulators of cell death. They regulate caspases and apoptosis through the inhibition of specific members of the caspase family of cysteine proteases. In addition, IAPs has been implicated in a multitude of other cellular processes, including inflammatory signalling and immunity, mitogenic kinase signalling, proliferation and mitosis, as well as cell invasion and metastasis. IAPs in this family includes cellular inhibitor of apoptosis protein c-IAP1 (BIRC2) and c-IAP2 (BIRC3), XIAP (BIRC4), BIRC7, and BIRC8, all of which contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of polyubiquitin (polyUb), and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. The UBA domain is only absent in mammalian homologs of BIRC7. Moreover, c-IAPs contains an additional caspase activation and recruitment domain (CARD) between the UBA and C3HC4-type RING-HC domains. The CARD domain may serve as a protein interaction surface
EKLCKICMDREVNIVFLPCGHLVTCAQCAASLRKCPICRT
>gnl|CDD|438174 cd16511, vRING-HC_IRF2BP1-like, variant of RING finger, HC subclass, found in interferon regulatory factor 2-binding protein IRF-2BP1, IRF-2BP2, and similar proteins. This subfamily includes IRF-2BP1, IRF-2BP2, and their homolog, IRF-2BP-like, also known as IRF-2BPL or C14orf4. IRF-2BP1 and IRF-2BP2 are nuclear proteins that bind to the C-terminal repression domain of IRF-2 and act as IRF-2-dependent transcriptional corepressors, both enhancer-activated and basal transcription. IRF-2BPL is expressed in the mediobasal hypothalamus and plays a critical function in regulating the female reproductive neuroendocrine axis. All subfamily members contain a C-terminal variant C3HC4-type RING-HC finger
LCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRDSIKRQGAGGEVYCPSGEKCPLVG
>gnl|CDD|438175 cd16512, RING-HC_LNX3-like, RING finger, HC subclass, found in ligand of Numb protein LNX3, LNX4, and similar proteins. The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4, or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for the substrate-binding. This family corresponds to LNX3/LNX4-like proteins, which contains a C3HC4-type RING-HC finger and two PDZ domains
LKCKLCLGVLEEPLATPCGHVFCAGCVLPWVVRNGSCPLKCEP
>gnl|CDD|438176 cd16513, RING-HC_LONFs_rpt1, first RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger protein family. The LON peptidase N-terminal domain and RING finger protein family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192, RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and an ATP-dependent protease La (LON) substrate-binding domain at the C-terminus. Their biological functions remain unclear. This model corresponds to the first RING-HC finger
DLLSCPLCRGLLFEPVTLPCGHTFCKRCLERDPSSRCRLCRLKLSPG
>gnl|CDD|438177 cd16514, RING-HC_LONFs_rpt2, second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger protein family. The LON peptidase N-terminal domain and RING finger protein family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192, RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and an ATP-dependent protease La (LON) substrate-binding domain at the C-terminus. Their biological functions remain unclear. This model corresponds to the second RING-HC finger
DLECSLCLRLLYEPVTTPCGHTFCRACLERCLDHSPKCPLCRTSL
>gnl|CDD|438178 cd16515, RING-HC_LRSAM1, RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing protein 1 (LRSAM1) and similar proteins. LRSAM1, also known as Tsg101-associated ligase (TAL), or RIFLE, is an E3 ubiquitin-protein ligase that physically associates with, and selectively ubiquitylates, Tsg101, an E2-like molecule that regulates vesicular trafficking processes in yeast and mammals. It regulates a Tsg101-associated complex responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the multivesicular body and at the plasma membrane. LRSAM1 is a multidomain protein containing an N-terminal leucine-rich repeat (LRR), followed by several recognizable motifs, including an ezrin-radixin-moezin (ERM) domain, a coiled-coil (CC) region, a SAM domain, and a C-terminal C3HC4-type RING-HC finger domain
ESECVVCMDAESQVIFLPCGHVCCCQTCSSSLSTCPLCRADITQRVRI
>gnl|CDD|438179 cd16516, RING-HC_malin, RING finger, HC subclass, found in malin and similar proteins. Malin ("mal" for seizure in French), also known as NHL repeat-containing protein 1 (NHLRC1), or EPM2B, is a nuclear E3 ubiquitin-protein ligase that ubiquitinates and promotes the degradation of laforin (EPM2A encoding protein phosphatase). Malin and laforin operate as a functional complex that play key roles in regulating cellular functions such as glycogen metabolism, unfolded cellular stress response, and proteolytic processes. They act as pro-survival factors that negatively regulate the Hipk2-p53 cell death pathway. They also negatively regulate cellular glucose uptake by preventing plasma membrane targeting of glucose transporters. Moreover, they degrade polyglucosan bodies in concert with glycogen debranching enzyme and brain isoform glycogen phosphorylase. Furthermore, they, together with Hsp70, form a new functional complex that suppress the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system. Defects in either malin or laforin may cause Lafora disease (LD), a fatal form of teenage-onset autosomal recessive progressive myoclonus epilepsy. In addition, malin may have function, independent of laforin, in lysosomal biogenesis and/or lysosomal glycogen disposal. Malin contains six NHL-repeat protein-protein interaction domains and a C3HC4-type RING-HC finger
LECKVCFEKYSHQQEHRPRNLPCGHVLCRECVTALAHPRRSKLECPFCRKAC
>gnl|CDD|438180 cd16517, RING-HC_MAT1, RING finger, HC subclass, found in RING finger protein MAT1. MAT1, also known as CDK-activating kinase assembly factor MAT1, CDK7/cyclin-H assembly factor, cyclin-G1-interacting protein, menage a trois, RING finger protein 66 (RNF66), p35, or p36, is involved in cell cycle control and in RNA transcription by RNA polymerase II. It associates primarily with the catalytic subunit cyclin-dependent kinase 7 (CDK7) and the regulatory subunit cyclin H to form the CDK-activating kinase (CAK) complex that can further associate with the core-TFIIH to form the transcription factor IIH (TFIIH) basal transcription/DNA repair factor, which activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter, and elongation of the transcripts. MAT1 contains an N-terminal C3HC4-type RING-HC finger, a central coiled coil domain, and a C-terminal domain rich in hydrophobic residues
QYCPRCKTTKYRNPSLKLMVNVCGHTLCESCVDLLFVRGSGPCPECGTPLRRSNF
>gnl|CDD|438181 cd16518, RING-HC_MEX3, RING finger, HC subclass, found in RNA-binding proteins of the evolutionarily-conserved MEX-3 family. MEX-3 phosphoproteins are found in vertebrates. They are mediators of post-transcriptional regulation in different organisms, and have been implicated in many core biological processes, including embryonic development, epithelial homeostasis, immune responses, metabolism, and cancer. They contain two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. They shuttle between the nucleus and the cytoplasm via the CRM1-dependent export pathway. The RNA-binding protein MEX-3 from nematode Caenorhabditis elegans is the founding member of the MEX-3 family. Due to the lack of a RING-HC finger, it is not included here
RDCVVCFESEVVAALVPCGHNLFCMECANRICEKSDPECPVCHTPVTQAIRIF
>gnl|CDD|438182 cd16519, RING-HC_MIBs, RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins. MIBs are large, multi-domain E3 ubiquitin-protein ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. They are also responsible for TBK1 K63-linked ubiquitination and activation, promoting interferon production and controlling antiviral immunity. Moreover, MIBs selectively control responses to cytosolic RNA and regulate type I interferon transcription. Both MIB1 and MIB2 have similar domain architectures, which consist of two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region, where MIB1 and MIB2 contain three and two C3HC4-type RING-HC fingers, respectively. This model corresponds to the first RING-HC finger of MIB1 and MIB2, as well as the second RING-HC finger of MIB1
EECRVCSDKKALVLFQPCGHVVACEECSLRMKKCLQCK
>gnl|CDD|438183 cd16520, RING-HC_MIBs-like, RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins. MIBs are large, multi-domain E3 ubiquitin-protein ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. They are also responsible for TBK1 K63-linked ubiquitination and activation, promoting interferon production and controlling antiviral immunity. Moreover, MIBs selectively control responses to cytosolic RNA and regulate type I interferon transcription. Both MIB1 and MIB2 have similar domain architectures, which consist of two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region, where MIB1 and MIB2 contain three and two C3HC4-type RING-HC fingers, respectively. This model corresponds to the third RING-HC finger of MIB1, as well as the second RING-HC finger of MIB2. In addition to MIB1 and MIB2, the RING-HC fingers of RING domain ligase RGLG1, RGLG2 and similar proteins from plant are also included in this model. RGLG1 is a ubiquitously expressed E3 ubiquitin-protein ligase that interacts with UBC13 and, together with UBC13, catalyzes the formation of K63-linked polyubiquitin chains, which is involved in DNA damage repair. RGLG1 mediates the formation of canonical, K48-linked polyubiquitin chains that target proteins for degradation. It also regulates apical dominance by acting on the auxin transport proteins abundance. RGLG1 has overlapping functions with its closest sequelog, RGLG2. They both function as RING E3 ligases that interact with ethylene response factor 53 (ERF53) in the nucleus and negatively regulate the plant drought stress response. All RGLG proteins contain a Von Willebrand factor type A (vWA) domain and a C3HC4-type RING-HC finger
ILCPICMERKKNVVFLCGHGTCQKCAEKLKKCPICRKPI
>gnl|CDD|438184 cd16521, RING-HC_MKRN, RING finger, HC subclass, found in the makorin (MKRN) proteins. The MKRN protein subfamily includes ribonucleoproteins that are characterized by a variety of zinc-finger motifs, including typical arrays of one to four C3H1-type zinc fingers and a C3HC4-type RING-HC finger. Another motif rich in Cys and His residues (CH), with so far unknown function, is also generally present in MKRN proteins. MKRN proteins may have E3 ubiquitin ligase activity
IECGICMEVVLEKERRFGILSNCNHVFCLECIREWRSSKDFENSIVRSCPICR
>gnl|CDD|438185 cd16522, RING-HC_MSL2, RING finger found in Drosophila melanogaster male-specific lethal-2 (MSL2) and similar proteins. MSL2, also known as RING finger protein 184 (RNF184), is a putative DNA-binding protein required for X chromosome dosage compensation in Drosophila males. Its expression is sex specifically regulated by Sex-lethal. Drosophila dosage compensation proteins MOF, MSL1, MSL2, and MSL3 are essential for elevating transcription of the single X chromosome in the male (X chromosome dosage compensation). MSL2 plays a critical role in translation and/or stability of MSL1 in males. In complex with MSL1, it acts as an E3 ubiquitin ligase that promotes ubiquitination of histone H2B. MSL2 contains a C3HC4-type RING-HC finger and a metallothionein-like domain with eight conserved and two non-conserved cysteines, as well as a positively and a negatively charged amino acid residue cluster and a coiled coil domain that may be involved in protein-protein interactions. This subfamily also includes many male-specific lethal-2 homologs from bilaterians
YLRQALSCCVCGQLLVDPIGPTNSTCQHNVCKGCKGGKMRLKPSCSWCKDYSQFEENKQL
>gnl|CDD|438186 cd16523, RING-HC_MYLIP, RING finger, HC subclass, found in myosin regulatory light chain interacting protein (MYLIP) and similar proteins. MYLIP, also known as inducible degrader of the low-density lipoprotein (LDL)-receptor (IDOL), or MIR, is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR, and LRP8. Its activity depends on E2 ubiquitin-conjugating enzymes of the UBE2D family. MYLIP stimulates clathrin-independent endocytosis and acts as a sterol-dependent inhibitor of cellular cholesterol uptake by binding directly to the cytoplasmic tail of the LDLR and promoting its ubiquitination via the UBE2D1/E1 complex. The ubiquitinated LDLR then enters the multivesicular body (MVB) protein-sorting pathway and is shuttled to the lysosome for degradation. Moreover, MYLIP has been identified as a novel ERM-like protein that affects cytoskeleton interactions regulating cell motility, such as neurite outgrowth. The ERM proteins includes ezrin, radixin, and moesin, which are cytoskeletal effector proteins linking actin to membrane-bound proteins at the cell surface. MYLIP contains an ERM-homology domain and a C-terminal C3HC4-type RING-HC finger
EAMLCMVCCEEEINSAFCPCGHMVCCESCAAQLQSCPVCRSRVEHVQHVYLP
>gnl|CDD|438187 cd16524, RING-HC_NHL-1-like, RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and similar proteins. NHL-1 functions as an E3 ubiquitin-protein ligase in the presence of both UBC-13 and UBC-1 within the ubiquitin pathway of Caenorhabditis elegans. It acts in chemosensory neurons to promote stress resistance in distal tissues by the transcription factor DAF-16 activation but is dispensable for the activation of heat shock factor 1 (HSF-1). NHL-1 belongs to the TRIM (tripartite motif)-NHL family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain
QIEQLLTCPICLDRYRRPKLLPCQHTFCLSPCLEGLVDYVTRKLKCPECRAEH
>gnl|CDD|438188 cd16525, RING-HC_PCGF, RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and 6), and similar proteins. This subfamily includes six Polycomb Group (PcG) RING finger homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) that use epigenetic mechanisms to maintain or repress expression of their target genes. They were first discovered in fruit flies and are well known for silencing Hox genes through modulation of chromatin structure during embryonic development. PCGF homologs play important roles in cell proliferation, differentiation, and tumorigenesis. They all have been found to associate with ring finger protein 2 (RNF2). The RNF2-PCGF heterodimer is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF homologs are critical components in the assembly of distinct Polycomb Repression Complex 1 (PRC1) related complexes which is involved in the maintenance of gene repression and which target different genes through distinct mechanisms. The Drosophila PRC1 core complex is formed by the Polycomb (Pc), Polyhomeotic (Ph), Posterior sex combs (Psc), and Sex combs extra (Sce, also known as Ring) subunits. In mammals, the composition of PRC1 is much more diverse and varies depending on the cellular context. All PRC1 complexes contain homologs of the Drosophila Ring protein. Ring1A/RNF1 and Ring1B/RNF2 are E3 ubiquitin ligases that mark lysine 119 of histone H2A with a single ubiquitin group (H2AK119ub). Mammalian homologs of the Drosophila Psc protein, such as PCGF2/Mel-18 or PCGF4/BMI1, regulate PRC1 enzymatic activity. PRC1 complexes can be divided into at least two classes according to the presence or absence of CBX proteins, which are homologs of Drosophila Pc. Canonical PRC1 complexes contain CBX proteins that recognize and bind H3K27me3, the mark deposited by PRC2. Therefore, canonical PRC1 complexes and PRC2 can act together to repress gene transcription and maintain this repression through cell division. Non-canonical PRC1 complexes, containing RYBP (together with additional proteins, such as L3mbtl2 or Kdm2b) rather than the CBX proteins have recently been described in mammals. PCGF homologs contain a C3HC4-type RING-HC finger
LTCSLCKGYLIDATTITECLHSFCKSCIVRHLETSKNCPVCD
>gnl|CDD|438189 cd16526, RING-HC_PEX2, RING finger, HC subclass, found in peroxin-2 (PEX2) and similar proteins. PEX2, also known as peroxisome biogenesis factor 2, 35 kDa peroxisomal membrane protein, peroxisomal membrane protein 3, peroxisome assembly factor 1 (PAF-1), or RING finger protein 72 (RNF72), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It may be involved in the biogenesis of peroxisomes, as well as in peroxisomal matrix protein import. Mutations in the PEX2 gene are the primary defect in a subset of patients with Zellweger syndrome and related peroxisome biogenesis disorders. Moreover, PEX2 functions as an E3-ubiquitin ligase that mediates the UBC4-dependent polyubiquitination of PEX5, a key player in peroxisomal matrix protein import, to control PEX5 receptor recycling or degradation
LTECAICGEWPTNNPYSTGCGHVYCYYCIKSNLLADDSFTCPRCGSPVS
>gnl|CDD|438190 cd16527, RING-HC_PEX10, RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins. PEX10, also known as peroxisome biogenesis factor 10, peroxisomal biogenesis factor 10, peroxisome assembly protein 10, or RING finger protein 69 (RNF69), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It plays an essential role in peroxisome assembly, import of target substrates, and recycling or degradation of protein complexes and amino acids. It is an essential component of the spinal locomotor circuit, and thus its mutations may be involved in peroxisomal biogenesis disorders (PBD). Mutations in human PEX10 also result in autosomal recessive ataxia. Moreover, PEX10 functions as an E3-ubiquitin ligase with an E2, UBCH5C. It mono- or poly-ubiquitinates PEX5, a key player in peroxisomal matrix protein import, in a UBC4-dependent manner, to control PEX5 receptor recycling or degradation. It also links the E2 ubiquitin conjugating enzyme PEX4 to the protein import machinery of the peroxisome
RKCSLCLEERRHPTATPCGHLFCWSCITEWCNEKPECPLCREPFQPQRLVPL
>gnl|CDD|438191 cd16528, RING-HC_prokRING, RING finger, HC subclass, found in prokaryotic RING finger family proteins. The family corresponds to a group of uncharacterized prokaryotic C3HC4-type RING-HC finger containing proteins. The RING finger is fused to an N-terminal alpha-helical domain, ROT/Trove-like repeats, and a C-terminal TerD domain, suggesting a possible role in an RNA-processing complex
QPCLHCGKVGTVHALSPCAHLVCDACFDGSDHSACPICHRRT
>gnl|CDD|438192 cd16529, RING-HC_RAD18, RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins. RAD18, also known as HR18 or RING finger protein 73 (RNF73), is an E3 ubiquitin-protein ligase involved in post replication repair of UV-damaged DNA via its recruitment to stalled replication forks. It associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on K164. It also interacts with another E2 ubiquitin conjugating enzyme RAD6 to form a complex that monoubiquitinates proliferating cell nuclear antigen at stalled replication forks in DNA translesion synthesis. Moreover, Rad18 is a key factor in double-strand break DNA damage response (DDR) pathways via its association with K63-linked polyubiquitylated chromatin proteins. It can function as a mediator for DNA damage response signals to activate the G2/M checkpoint in order to maintain genome integrity and cell survival after ionizing radiation (IR) exposure. RAD18 contains a C3HC4-type RING-HC finger, a ubiquitin-binding zinc finger domain (UBZ), a SAP (SAF-A/B, Acinus and PIAS) domain, and a RAD6-binding domain (R6BD)
LDDLLRCPICFEYFNTAMMITQCSHNYCSLCIRRFLSYKTQCPTCRAAVTESDL
>gnl|CDD|319444 cd16530, RING-HC_RAG1, RING finger, HC subclass, found in recombination activating gene-1 (RAG-1) and similar proteins. RAG-1, also known as V(D)J recombination-activating protein 1, RING finger protein 74 (RNF74), or endonuclease RAG1, is the catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. RAG1 is a lymphoid-specific factor that mediates DNA-binding to conserved recombination signal sequences (RSS) and catalyzes DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. It also functions as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3, which is required for the joining step of V(D)J recombination. RAG-1 contains an N-terminal C3HC4-type RING-HC finger that mediates monoubiquitylation of histone H3, an adjacent C2H2-type zinc finger, and a nonamer binding (NBD) DNA-binding domain
KSVSCQVCEHILADPVQTPCKHLFCRTCILKCLKVMGSYCPSCRYP
>gnl|CDD|438193 cd16531, RING-HC_RING1-like, RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and similar proteins. RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), is a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. Both RING1 and RING2 are core components of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING2 acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Members of this family contain a C3HC4-type RING-HC finger
ELMCPICLGIIKNTMTVKECLHRFCAECIEKALRLGNKECPTCRKHLPSRRSLRPDPNFDALISKI
>gnl|CDD|438194 cd16532, RING-HC_RNFT1-like, RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins. Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear
DICPICQDEFKDPVVLRCKHIFCEDCVSEWFERERTCPLCR
>gnl|CDD|438195 cd16533, RING-HC_RNF4, RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins. RNF4, also known as small nuclear ring finger protein (SNURF), is a SUMO-targeted E3 ubiquitin-protein ligase with a pivotal function in the DNA damage response (DDR) by interacting with the deubiquitinating enzyme ubiquitin-specific protease 11 (USP11), a known DDR-component, and further facilitating DNA repair. It plays a novel role in preventing the loss of intact chromosomes and ensures the maintenance of chromosome integrity. Moreover, RNF4 is responsible for the UbcH5A-catalyzed formation of K48 chains that target SUMO-modified promyelocytic leukemia (PML) protein for proteasomal degradation in response to arsenic treatment. It also interacts with telomeric repeat binding factor 2 (TRF2) in a small ubiquitin-like modifier (SUMO)-dependent manner and preferentially targets SUMO-conjugated TRF2 for ubiquitination through SUMO-interacting motifs (SIMs). Furthermore, RNF4 can form a complex with a Ubc13-ubiquitin conjugate and Ube2V2. It catalyzes K63-linked polyubiquitination by the Ube2V2-Ubc13 (ubiquitin-loaded) complex. Meanwhile, RNF4 negatively regulates nuclear factor kappa B (NF-kappaB) signaling by down-regulating transforming growth factor beta (TGF-beta)-activated kinase 1 (TAK1)-TAK1-binding protein2 (TAB2). RNF4 contains four SIMs followed by a C3HC4-type RING-HC finger at the C-terminus
SGTVSCPICMDGYSEIVQSGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKLNHK
>gnl|CDD|438196 cd16534, RING-HC_RNF5-like, RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins. RNF5 and RNF185 are E3 ubiquitin-protein ligases that are anchored to the outer membrane of the endoplasmic reticulum (ER). RNF5 acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis, and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. RNF185 controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical endoplasmic reticulum-associated degradation (ERAD) model substrates. Moreover, both RNF5 and RNF185 play important roles in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) are also included in this family. They possess E3 ubiquitin-protein ligase activity and may play a role in the growth and development of Arabidopsis. All members of this family contain a C3HC4-type RING-HC finger
FECNICLDTASDPVVTMCGHLFCWPCLYQWLETRPDRQTCPVCK
>gnl|CDD|438197 cd16535, RING-HC_RNF8, RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins. RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal forkhead-associated (FHA) domain and a C-terminal C3HC4-type RING-HC finger
ELQCSICSELFIEAVTLNCSHSFCSYCITEWMKRKKECPICRKPITSKTRSLVLDNCIDKMVEN
>gnl|CDD|438198 cd16536, RING-HC_RNF10, RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins. RNF10 is an E3 ubiquitin-protein ligase that interacts with mesenchyme Homeobox 2 (MEOX2) transcription factor, a regulator of the proliferation, differentiation and migration of vascular smooth muscle cells and cardiomyocytes; it enhances Meox2 activation of the p21 promoter. It also regulates the expression of myelin-associated glycoprotein (MAG) genes and is required for myelin production in Schwann cells of the peripheral nervous system. Moreover, RNF10 regulates retinoic acid-induced neuronal differentiation and the cell cycle exit of P19 embryonic carcinoma cells. RNF10 contains a C3HC4-type RING-HC finger and three putative nuclear localization signals
PQCPICLEPPVAPRITRCGHIFCWPCILRYLSLSEKKWRKCPICFESIHKKDLR
>gnl|CDD|438199 cd16537, RING-HC_RNF37, RING finger, HC subclass, found in RING finger protein 37 (RNF37). RNF37, also known as KIAA0860, U-box domain-containing protein 5 (UBOX5), UbcM4-interacting protein 5 (UIP5), or ubiquitin-conjugating enzyme 7-interacting protein 5, is an E3 ubiquitin-protein ligase found exclusively in the nucleus as part of a nuclear dot-like structure. It interacts with the molecular chaperone VCP/p97 protein. RNF37 contains a U-box domain followed by a potential nuclear location signal (NLS) and a C-terminal C3HC4-type RING-HC finger. The U-box domain is a modified RING finger domain that lacks the hallmark metal-chelating cysteines and histidines of the latter, and is likely to adopt a RING finger-like conformation. The presence of the U-box, but not of the RING finger, is required for the E3 activity. The U-box domain can directly interact with several E2 enzymes, including UbcM2, UbcM3, UbcM4, UbcH5, and UbcH8, suggesting a similar function as the RING finger in the ubiquitination pathway. This model corresponds to the RING-HC finger
QGCASCSRAFSPYFKTEPVYRLPCGHLLCRPCLAEKQKSLAILCPTCNRPVA
>gnl|CDD|438200 cd16538, RING-HC_RNF112, RING finger, HC subclass, found in RING finger protein 112 (RNF112) and similar proteins. RNF112, also known as brain finger protein (BFP), zinc finger protein 179 (ZNF179), or neurolastin, is a peripheral membrane protein that is predominantly expressed in the central nervous system and localizes to endosomes. It contains functional GTPase and C3HC4-type RING-HC finger domains and has been identified as a brain-specific dynamin family GTPase that affects endosome size and spine density. Moreover, RNF112 acts as a downstream target of sigma-1 receptor (Sig-1R) regulation and may play a novel role in neuroprotection by mediating the neuroprotective effects of dehydroepiandrosterone (DHEA) and its sulfated analog (DHEAS)
EPPTCSICLERLREPISLDCGHDFCIRCFSTHRIPGCEPPCCPECRKICKQR
>gnl|CDD|438201 cd16539, RING-HC_RNF113A_B, RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins. RNF113A, also known as zinc finger protein 183 (ZNF183), is an E3 ubiquitin-protein ligase that physically interacts with the E2 protein, UBE2U. A nonsense mutation in RNF113A is associated with an X-linked trichothiodystrophy (TTD). Its yeast ortholog Cwc24p is predicted to have a spliceosome function and acts in a complex with Cef1p to participate in pre-U3 snoRNA splicing, indirectly affecting pre-rRNA processing. It is also important for the U2 snRNP binding to primary transcripts and co-migrates with spliceosomes. Moreover, the ortholog of RNF113A in fruit flies may also act as a spliceosome and is hypothesized to be involved in splicing, namely within the central nervous system. The ortholog in Caenorhabditis elegans is involved in DNA repair of inter-strand crosslinks. RNF113B, also known as zinc finger protein 183-like 1, shows high sequence similarity with RNF113A. Both RNF113A and RNF113B contain a CCCH-type zinc finger, which is commonly found in RNA-binding proteins involved in splicing, and a C3HC4-type RING-HC finger, which is frequently found in E3 ubiquitin ligases
EEDLPFACFICRKPFKNPVVTKCGHYFCEKCALKHYRKSKKCFVCGKQTNGVFN
>gnl|CDD|438202 cd16540, RING-HC_RNF114, RING finger, HC subclass, found in RING finger protein 114 (RNF114) and similar proteins. RNF114, also known as zinc finger protein 228 (ZNF228) or zinc finger protein 313 (ZNF313), is a p21(WAF1)-targeting ubiquitin E3 ligase that interacts with X-linked inhibitor of apoptosis (XIAP)-associated factor 1 (XAF1) and may play a role in p53-mediated cell-fate decisions. It is involved in the immune response to double-stranded RNA in disease pathogenesis. Moreover, RNF114 interacts with A20 and modulates its ubiquitylation. It negatively regulates nuclear factor-kappaB (NF-kappaB)-dependent transcription and positively regulates T-cell activation. RNF114 may play a putative role in the regulation of immune responses, since it corresponds to a novel psoriasis susceptibility gene, ZNF313. RNF114, together with three closely related proteins: RNF125, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM)
RFTCPVCLEIFETPVRVPCGHVFCNACLQECLKPKKPVCAVCRSPL
>gnl|CDD|438203 cd16541, RING-HC_RNF123, RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins. RNF123, also known as Kip1 ubiquitination-promoting complex protein 1 (KPC1), is an E3 ubiquitin-protein ligase that mediates ubiquitination and proteasomal processing of the nuclear factor-kappaB 1 (NF-kappaB1) precursor p105 to the p50 active subunit that restricts tumor growth. It also regulates degradation of heterochromatin protein 1alpha (HP1alpha) and 1beta (HP1beta) in lamin A/C knock-down cells. Moreover, RNF123, together with Kip1 ubiquitylation-promoting complex 2 (KPC2), forms the Kip1 ubiquitination-promoting complex (KPC), acting as a cytoplasmic ubiquitin ligase that regulates degradation of the cyclin-dependent kinase inhibitor p27 (Kip1) at the G1 phase of the cell cycle. RNF123 may also function as a clinically relevant, peripheral state marker of depression. RNF123 contains a C3HC4-type RING-HC finger at the C-terminus
DLCPICYAHPIDAVFLPCGHKSCRSCINRHLMNNKECFFCKATI
>gnl|CDD|438204 cd16542, RING-HC_RNF125, RING finger, HC subclass, found in RING finger protein 125 (RNF125). RNF125, also known as T-cell RING activation protein 1 (TRAC-1), is an E3 ubiquitin-protein ligase that is predominantly expressed in lymphoid cells, and functions as a positive regulator of T cell activation. It also down-modulates HIV replication and inhibits pathogen-induced cytokine production. It negatively regulates type I interferon signaling, which conjugates Lys(48)-linked ubiquitination to retinoic acid-inducible gene-I (RIG-I) and subsequently leads to the proteasome-dependent degradation of RIG-I. Further, RNF125 conjugates ubiquitin to melanoma differentiation-associated gene 5 (MDA5), a family protein of RIG-I. It thus acts as a negative regulator of RIG-I signaling, and is a direct target of miR-15b in the context of Japanese encephalitis virus (JEV) infection. Moreover, RNF125 binds to and ubiquitinates JAK1, prompting its degradation and inhibition of receptor tyrosine kinase (RTK) expression. It also negatively regulates p53 function through physical interaction and ubiquitin-mediated proteasome degradation. Mutations in RNF125 may lead to overgrowth syndromes (OGS). RNF125, together with three closely related proteins: RNF114, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM). The UIM of RNF125 binds K48-linked poly-ubiquitin chains and is, together with the RING domain, required for auto-ubiquitination
NFDCAVCLEVLHQPVRTRCGHVFCRPCIATSLRNNTWTCPYCRAYLSSEG
>gnl|CDD|438205 cd16543, RING-HC_TRIM77_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar proteins. TRIM77 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including two consecutive zinc-binding domains, a C3HC4-type RING-HC finger and Bbox2, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain
EDQLTCSICLDLLKDPVTIPCGHSFCMNCITLLWDRKQGVPSCPQCRESFPPRP
>gnl|CDD|438206 cd16544, RING-HC_RNF138, RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins. RNF138, also known as Nemo-like kinase-associated RING finger protein (NARF) or NLK-associated RING finger protein, is an E3 ubiquitin-protein ligase that plays an important role in glioma cell proliferation, apoptosis, and cell cycle. It specifically cooperates with the E2 conjugating enzyme E2-25K (Hip-2/UbcH1), regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF), and further suppresses Wnt-beta-catenin signaling. RNF138, together with three closely related proteins: RNF114, RNF125 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM)
AELTCPVCQEVLKDPVELPPCRHIFCKACILLALRSSGARCPLCRGPVGKTER
>gnl|CDD|438207 cd16545, RING-HC_RNF141, RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins. RNF141, also known as zinc finger protein 230 (ZNF230), is a RING finger protein present primarily in the nuclei of spermatogonia, the acrosome, and the tail of spermatozoa. It may have a broad function during early development of vertebrates. It plays an important role in spermatogenesis, including spermatogenic cell proliferation and sperm maturation, as well as motility and fertilization. It also exhibits DNA binding activity. RNF141/ZNF230 gene mutations may be associated with azoospermia. RNF141 contains a C3HC4-type RING finger domain that may function as an activator module in transcription
EECCICMDRKADLILPCAHSYCQKCIDKWSDRHRTCPICR
>gnl|CDD|438208 cd16546, RING-HC_RNF146, RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins. RNF146, also known as dactylidin, or iduna, is a cytoplasmic E3 ubiquitin-protein ligase that is responsible for PARylation-dependent ubiquitination (PARdU). It displays neuroprotective property due to its inhibition of Parthanatos, a PAR dependent cell death, via binding with Poly(ADP-ribose) (PAR). It also modulates PAR polymerase-1 (PARP-1)-mediated oxidative cell injury in cardiac myocytes. Moreover, RNF146 mediates tankyrase-dependent degradation of axin, thereby positively regulating Wnt signaling. It also facilitates DNA repair and protects against cell death induced by DNA damaging agents or gamma-irradiation by translocating to the nucleus after cellular injury and promoting the ubiquitination and degradation of various nuclear proteins involved in DNA damage repair. Furthermore, RNF146 is implicated in neurodegenerative disease and cancer development. It regulates the development and progression of non-small cell lung cancer (NSCLC) by enhancing cell growth, invasion, and survival. RNF146 contains an N-terminal C3HC4-type RING-HC finger followed by a WWE domain with a poly(ADP-ribose) (PAR) binding motif at the tail
PECPICLQTCIHPVKLPCGHIFCYLCVKGVAWQSKRCALCRQEIPEDFLD
>gnl|CDD|438209 cd16547, RING-HC_RNF151, RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins. RNF151 is a testis-specific RING finger protein that interacts with dysbindin, a synaptic and microtubular protein that binds brain snapin, a SNARE-binding protein that mediates intracellular membrane fusion in both neuronal and non-neuronal cells. Thus, it may be involved in acrosome formation of spermatids by interacting with multiple proteins participating in membrane biogenesis and microtubule organization. RNF151 contains a C3HC4-type RING finger domain, a putative nuclear localization signal (NLS), and a TNF receptor associated factor (TRAF)-type zinc finger domain
DDDLICSICHGVLRCPVRLSCSHIFCKKCILQWLKRQETCPCCRKEVKG
>gnl|CDD|438210 cd16548, RING-HC_RNF152, RING finger, HC subclass, found in RING finger protein 152 (RNF152) and similar proteins. RNF152 is a lysosome-anchored E3 ubiquitin-protein ligase involved in apoptosis. It is polyubiquitinated through K48 linkage. It negatively regulates the activation of the mTORC1 pathway by targeting RagA GTPase for K63-linked ubiquitination. It interacts with and ubiquitinates RagA in an amino-acid-sensitive manner. The ubiquitination of RagA recruits its inhibitor GATOR1, a GAP complex for Rag GTPases, to the Rag complex, thereby inactivating mTORC1 signaling. RNF152 contains an N-terminal C3HC4-type RING-HC finger and a C-terminal transmembrane domain, both of which are responsible for its E3 ligase activity
LECQICFNYYSPRRRPKLLDCKHTCCSVCLQQMRTSQKDLRCPWCR
>gnl|CDD|438211 cd16549, RING-HC_RNF166, RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins. RNF166 is encoded by the gene RNF166 targeted by thyroid hormone receptor alpha1 (TRalpha1), which is important in brain development. It plays an important role in RNA virus-induced interferon-beta production by enhancing the ubiquitination of TRAF3 and TRAF6. RNF166, together with three closely related proteins: RNF114, RNF125 and RNF138, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM)
QFSCPICLEVYHKPVVITSCGHTFCGECLQPCLQVASPLCPLCRMPF
>gnl|CDD|438212 cd16550, RING-HC_RNF168, RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins. RNF168 is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. It, together with RNF8, functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates, such as H2A and H2AX with H2AK13/15 ubiquitylation, facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. Moreover, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF168 contains an N-terminal C3HC4-type RING-HC finger that catalyzes H2A-K15ub and interacts with H2A, and two MIU (motif interacting with ubiquitin) domains responsible for the interaction with K63 linked poly-ubiquitin
CLCPICLEILVEPVTLPCNHTLCMPCFQSTVEKASLCCPLCRLRISSW
>gnl|CDD|438213 cd16551, RING-HC_RNF169, RING finger, HC subclass, found in RING finger protein 169 (RNF169) and similar proteins. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to regulation of the DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. RNF169 contains an N-terminal C3HC4-type RING-HC finger and a C-terminal MIU (motif interacting with ubiquitin) domain
ELTCAGCLEVPVEPATLPCGHTLCRGCANRALDAAEAGPTCPRCRAPLPGWAPRL
>gnl|CDD|438214 cd16552, RING-HC_NEURL3, RING finger, HC subclass, found in neuralized-like protein 3 (NEURL3) and similar proteins. NEURL3, also known as lung-inducible neuralized-related C3HC4 RING domain protein (LINCR), is a novel inflammation-induced E3 ubiquitin-protein ligase encoded by LINCR, a glucocorticoid-attenuated response gene induced in the lung during endotoxemia. It is expressed in alveolar epithelial type II cells, preferentially interacts with the ubiquitin-conjugating enzyme UbcH6, and generates polyubiquitin chains linked via non-canonical lysine residues. Overexpression of NEURL3 in the developing lung epithelium inhibits distal differentiation and induces cystic changes in the Notch signaling pathway. NEURL3 contains an N-terminal neuralized homology repeat (NHR) domain similar to the SPRY (SPla and the RYanodine receptor) domain and a C-terminal C3HC4-type RING-HC finger
GEECAICFHHTANTRLVPCGHSHFCGSCAWHIFRDTARCPVCRWQIEEVA
>gnl|CDD|438215 cd16553, RING-HC_RNF170, RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins. RNF170, also known as putative LAG1-interacting protein, is an endoplasmic reticulum (ER) membrane-bound E3 ubiquitin-protein ligase that mediates ubiquitination-dependent degradation of type-I inositol 1,4,5-trisphosphate (IP3) receptors (ITPR1) via the endoplasmic-reticulum-associated protein degradation (ERAD) pathway. A point mutation (arginine to cysteine at position 199) in the RNF170 gene is linked with autosomal-dominant sensory ataxia (ADSA), a disease characterized by neurodegeneration in the posterior columns of the spinal cord. RNF170 contains a C3HC4-type RING-HC finger
DMECPICLQDARFPVETNCGHLFCGPCIITYWRHGSWLGAVSCPVCRQTVTLLLPVF
>gnl|CDD|438216 cd16554, RING-HC_RNF180, RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins. RNF180, also known as Rines, is a membrane-bound E3 ubiquitin-protein ligase well conserved among vertebrates. It is a critical regulator of the monoaminergic system, as well as emotional and social behavior. It interacts with brain monoamine oxidase A (MAO-A) and targets it for ubiquitination and degradation. It also functions as a novel tumor suppressor in gastric carcinogenesis. The hypermethylated CpG site count of the RNF180 DNA promoter can be used to predict survival of gastric cancer. RNF180 contains a novel conserved dual specificity protein phosphatase Rines conserved (DSPRC) domain, a basic coiled-coil domain, a C3HC4-type RING-HC finger, and a C-terminal hydrophobic region that is predicted to be a transmembrane domain
ESLTCPVCLDLYYDPYMCYPCGHIFCEPCLRQLAKSSPKNTPCPLCRTTIRRVFFQEEL
>gnl|CDD|438217 cd16555, RING-HC_RNF182, RING finger, HC subclass, found in RING finger protein 182 (RNF182) and similar proteins. RNF182 is a brain-enriched E3 ubiquitin-protein ligase that stimulates E2-dependent polyubiquitination in vitro. It is upregulated in Alzheimer"s disease (AD) brains and neuronal cells exposed to injurious insults. It interacts with ATP6V0C and promotes its degradation by the ubiquitin-proteosome pathway, suggesting a very specific role in controlling the turnover of an essential component of the neurotransmitter release machinery. RNF182 contains an N-terminal C3HC4-type RING-HC finger, and a C-terminal transmembrane domain
ELECKICYNRYDLRQRRPKVLECCHRVCAKCLYKIVDLGDSSPSVLVCPFCRFET
>gnl|CDD|438218 cd16556, RING-HC_RNF183-like, RING finger, HC subclass, found in RING finger protein RNF183, RNF223, RNF225 and similar proteins. RNF183 is an E3 ubiquitin-protein ligase that is upregulated during intestinal inflammation and is negatively regulated by miR-7. It promotes intestinal inflammation by increasing the ubiquitination and degradation of inhibitor of kappa B, thereby resulting in secondary activation of the Nuclear factor-kappaB (NF-kB) pathway. The interaction between RNF183-mediated ubiquitination and miRNA may be an important novel epigenetic mechanism in the pathogenesis of inflammatory bowel disease (IBD). The biological function of RNF223 and RNF225 remains unclear. Members of this family contain an N-terminal C3HC4-type RING-HC finger
LECSICFSSYDNTFKTPKLLDCGHTFCLECLARLSLASPPQAERVPCPLCRQPTVLP
>gnl|CDD|438219 cd16557, RING-HC_RNF186, RING finger, HC subclass, found in RING finger protein 186 (RNF186) and similar proteins. RNF186 is an E3 ubiquitin-protein ligase with an N-terminal C3HC4-type RING-HC finger and two putative C-terminal transmembrane domains which enable it to localize in a certain organelle. It regulates RING-dependent self-ubiquitination, as well as endoplasmic reticulum (ER) stress-mediated apoptosis through interaction with the Bcl-2 family protein BNip1
DLECLVCRNPYSCFVRKPKLLACQHAFCAICLKLILCEQDGTWSVTCPLCRR
>gnl|CDD|438220 cd16558, RING-HC_RNF207, RING finger, HC subclass, found in RING finger protein 207 (RNF207) and similar proteins. RNF207 is a cardiac-specific E3 ubiquitin-protein ligase that plays an important role in the regulation of cardiac repolarization. It regulates action potential duration, likely via effects on human ether-a-go-go-related gene (HERG) trafficking and localization in a heat shock protein-dependent manner. RNF207 contains a C3HC4-type RING-HC finger, Bbox 1 and Bbox C-terminal (BBC) domain, as well as a C-terminal non-homologous region (CNHR)
PLVCYLCHEQYEHPCLLDCYHTFCASCLRGRAADGRLTCPLCG
>gnl|CDD|438221 cd16559, RING-HC_RNF208, RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins. RNF208 is an E3 ubiquitin-protein ligase whose activity can be modulated by S-nitrosylation. It contains a C3HC4-type RING-HC finger
PLLCPTCGHSYNFTNKRPRILSCLHSVCEECLQILYESCPKYKFISCPTCKRETVL
>gnl|CDD|438222 cd16560, RING-HC_RNF212-like, RING finger, HC subclass, found in RING finger proteins RNF212, RNF212B and similar proteins. This subfamily includes RING finger protein RNF212, RNF212B, and their homologs. RNF212 is a dosage-sensitive regulator of crossing-over during mammalian meiosis. It plays a central role in designating crossover sites and coupling chromosome synapsis to the formation of crossover-specific recombination complexes. It also functions as an E3 ligase for small ubiquitin-related modifier (SUMO) modification. RNF212B shows high sequence similarity with RNF212, but its biological function remains unclear. Members of this subfamily contain an N-terminal C3HC4-type RING-HC finger. Also included are two homologs of RNF212, meiotic procrossover factors Zip3 and ZHP-3, which have been identified in Saccharomyces cerevisiae and Caenorhabditis elegans, respectively. Budding yeast Zip3 is a small ubiquitin-related modifier (SUMO) E3 ligase implicated in the SUMO pathway of post-translational modification. It sumoylates chromosome axis proteins, thus promoting synaptonemal complex polymerization. It also acts as an Smt3 E3 ligase. Zip3 includes a SUMO Interacting Motif (SIM) and a modified C3HCHC2-type RING-HC finger that are important for Zip3 in vitro E3 ligase activity and necessary for SC polymerization and correct sporulation. ZHP-3 acts at crossovers to couple meiotic recombination with synaptonemal complex disassembly and chiasma formation in Caenorhabditis elegans. It possesses a C3HC4-type RING-HC finger
VHCNTCFQLPGDTSKFFLTSCGHIYCDACVGKGKRNKCKICG
>gnl|CDD|438223 cd16561, RING-HC_RNF213, RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins. RNF213, also known as ALK lymphoma oligomerization partner on chromosome 17 or Moyamoya steno-occlusive disease-associated AAA+ and RING finger protein (mysterin), is an intracellular soluble protein that functions as an E3 ubiquitin-protein ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. It plays a unique role in endothelial cells for proper gene expression in response to inflammatory signals from the environment. Mutations in RNF213 may be associated with Moyamoya disease (MMD), an idiopathic cerebrovascular occlusive disorder prevalent in East Asia. It also acts as a nuclear marker for acanthomorph phylogeny. RNF213 contains two tandem enzymatically active AAA+ ATPase modules and a C3HC4-type RING-HC finger. It can form a huge ring-shaped oligomeric complex
GEQECSICLEDLNDPVKLPCDHVFCEECIRQWLPGQMSCPLCRTELPDDF
>gnl|CDD|438224 cd16562, RING-HC_RNF219, RING finger, HC subclass, found in RING finger protein 219 (RNF219) and similar proteins. RNF219 may function as a modulator of late-onset Alzheimer's disease (LOAD) associated amyloid beta A4 precursor protein (APP) endocytosis and metabolism. It genetically interacts with apolipoprotein E epsilon4 allele (APOE4). Thus, a genetic variant of RNF219 was found to affect amyloid deposition in human brain and LOAD age-of-onset. Moreover, common genetic variants at the RNF219 locus had been associated with alternations in lipid metabolism, cognitive performance and central nervous system ventricle volume. RNF219 contains a C3HC4-type RING-HC finger
PISCHICLGKVRQPVICSNNHVFCSSCMDVWLKNNNQCPACRVPI
>gnl|CDD|438225 cd16563, RING-HC_RNF220, RING finger, HC subclass, found in RING finger protein 220 (RNF220) and similar proteins. RNF220 is an E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of Sin3B, a scaffold protein of the Sin3/HDAC (histone deacetylase) corepressor complex. It can also bind E2 and mediate auto-ubiquitination of itself. Moreover, RNF220 specifically interacts with beta-catenin, and enhances canonical Wnt signaling through ubiquitin-specific protease 7 (USP7)-mediated deubiquitination and stabilization of beta-catenin, which is independent of its E3 ligase activity. RNF220 contains a characteristic C3HC4-type RING-HC finger at its C-terminus
YKCLICMDSYTMPLVSIQCWHVHCEECWLRTLGAKKLCPQCNTITSPADLRR
>gnl|CDD|438226 cd16564, RING-HC_RNF222, RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins. RNF222 is an uncharacterized C3HC4-type RING-HC finger-containing protein. It may function as an E3 ubiquitin-protein ligase
SECPVCYEDFDDAPRILSCGHSFCEDCLVKQLVSMTISCPICRRVTFISK
>gnl|CDD|438227 cd16565, RING-HC_RNF224, RING finger, HC subclass, found in RING finger protein RNF224 and similar proteins. RNF224 is uncharacterized C3HC4-type RING-HC finger-containing proteins. It may function as an E3 ubiquitin-protein ligase
LDCIICYSAYDLSTRLPRRLYCGHTFCQACLKRLDTVINEQRWIPCPQCRQNTPTPRGG
>gnl|CDD|438228 cd16566, RING-HC_RSPRY1, RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) and similar proteins. RSPRY1 is a hypothetical RING and SPRY domain-containing protein of unknown physiological function. Mutations in its corresponding gene RSPRY1 may associate with a distinct skeletal dysplasia syndrome. RSPRY1 contains a B30.2/SPRY domain and a C3HC4-type RING-HC finger
REDSCTLCFDKVADTELRPCGHSGFCMECALQLETCPLCRQPI
>gnl|CDD|438229 cd16567, RING-HC_RAD16-like, RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, Schizosaccharomyces pombe rhp16, and similar proteins. Budding yeast RAD16, also known as ATP-dependent helicase RAD16, is encoded by a yeast excision repair gene homologous to the recombinational repair gene RAD54 and to the SNF2 gene involved in transcriptional activation. It is a component of the global genome repair (GGR) complex that promotes global genome nucleotide excision repair (GG-NER) by removing DNA damage from non-transcribing DNA. RAD16 is involved in differential repair of DNA after UV damage, and repairs preferentially the MAT-alpha locus compared with the HML-alpha locus. Fission yeast rhp16, also known as ATP-dependent helicase rhp16, is a RAD16 homolog. It is involved in GGR via nucleotide excision repair (NER), in conjunction with rhp7, after UV irradiation. Both RAD16 and rhp16 contain a C3HC4-type RING-HC finger, as well as a DEAD-like helicase domain and a helicase superfamily C-terminal domain
LVCGICHEEAEDPVVARCHHVFCRACVKEYIESAPGGKVTCPTCHKPL
>gnl|CDD|438230 cd16568, RING-HC_ScPSH1-like, RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1) and similar proteins. ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain
ILETQECIICHEYLYEPMVTTCGHTYCYTCLNTWFKSNRSLSCPDCRTKITTQP
>gnl|CDD|438231 cd16569, RING-HC_SHPRH-like, RING finger, HC subclass, found in SNF2 histone-linker PHD finger RING finger helicase (SHPRH) and similar proteins. SHPRH is a yeast RAD5 homolog found in mammals. It functions as an E3 ubiquitin-protein ligase that associates with proliferating cell nuclear antigen (PCNA), RAD18, and the ubiquitin-conjugating enzyme UBC13 (E2), and suppresses genomic instability by proliferating methyl methanesulfonate (MMS)-induced PCNA polyubiquitination. SHPRH contains a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a linker histone domain (H15), a PHD-finger, and a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA. This subfamily also includes tripartite motif-containing protein 15 (TRIM15). TRIM15, also known as RING finger protein 93 (RNF93), zinc finger protein 178 (ZNF178), or zinc finger protein B7 (ZNFB7), is a focal adhesion protein that regulates focal adhesion disassembly. It localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. TRIM15 can also associate with coronin 1B, cortactin, filamin binding LIM protein1, and vasodilator-stimulated phosphoprotein, which are involved in actin cytoskeleton dynamics. As an additional component of the integrin adhesome, it regulates focal adhesion turnover and cell migration. TRIM15 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain
PEPCPICARPLGKQWSVLPCGHCFCLECIAILIDQYAQSRRRSLKCPICRETT
>gnl|CDD|438232 cd16570, RING-HC_SH3RFs, RING finger, HC subclass, found in SH3 domain-containing RING finger proteins SH3RF1, SH3RF2, SH3RF3, and similar proteins. SH3RF1, also known as plenty of SH3s (POSH), RING finger protein 142 (RNF142), or SH3 multiple domains protein 2 (SH3MD2), is a trans-Golgi network-associated pro-apoptotic scaffold protein with E3 ubiquitin-protein ligase activity. SH3RF2, also known as heart protein phosphatase 1-binding protein (HEPP1), plenty of SH3s (POSH)-eliminating RING protein (POSHER), protein phosphatase 1 regulatory subunit 39, or RING finger protein 158 (RNF158), is a putative E3 ubiquitin-protein ligase that acts as an anti-apoptotic regulator for the c-Jun N-terminal kinase (JNK) pathway by binding to and promoting the proteasomal degradation of SH3RF1 (or POSH) that is required for pro-apoptotic JNK activation. SH3RF3, also known as plenty of SH3s 2 (POSH2) or SH3 multiple domains protein 4 (SH3MD4), is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2) and may play a role in regulating c-Jun N-terminal kinase (JNK) mediated apoptosis in certain conditions. Members of this subfamily contain an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs
LECPVCLERLDVSAKVLPCQHTFCKRCLQIIVASRGELRCPECR
>gnl|CDD|438233 cd16571, RING-HC_SIAHs, RING finger, HC subclass, found in Drosophila melanogaster protein Seven-in-Absentia (sina) and its homologs. This subfamily includes the Drosophila melanogaster protein Seven-in-Absentia (sina), its mammalian orthologs, SIAH1 and SIAH2, plant SINA-related proteins, and similar proteins. Sina plays an important role in the phyllopod-dependent degradation of the transcriptional repressor tramtrack to allow the formation of the R7 photoreceptor in the developing eye of Drosophila melanogaster. Both SIAH1 and SIAH2 are E3 ubiquitin-protein ligases, mediating the ubiquitinylation and subsequent proteasomal degradation of biologically important target proteins that regulate general functions, such as cell cycle control, apoptosis, and DNA repair. They are inducible by the tumor suppressor and transcription factor p53. SIAH2 can also be regulated by sex hormones and cytokine signaling. Moreover, they share high sequence similarity, but possess contrary roles in cancer, with SIAH1 more often acting as a tumor suppressor while SIAH2 functions as a proto-oncogene. Plant SINAT1-5 are putative E3 ubiquitin ligases involved in the regulation of stress responses. All subfamily members possess two characteristic domains, an N-terminal C3HC4-type RING-HC finger and a C-terminal tumor necrosis factor (TNF) receptor associated factor (TRAF)-like substrate-binding domain (SBD)
LECPVCFEPLLPPIYQCSNGHLLCSSCRSKLTNKCPTCR
>gnl|CDD|438234 cd16572, RING-HC_SpRad8-like, RING finger, HC subclass, found in Schizosaccharomyces pombe DNA repair protein Rad8 (SpRad8) and similar proteins. SpRad8 is a conserved protein homologous to Saccharomyces cerevisiae DNA repair protein Rad5 and human helicase-like transcription factor (HLTF) that is required for error-free postreplication repair by contributing to polyubiquitylation of PCNA. SpRad8 contains a C3HC4-type RING-HC finger responsible for the E3 ubiquitin ligase activity, a SNF2-family helicase domain including an ATP binding site, and a family-specific HIRAN domain (HIP116, Rad5p N-terminal domain) that contributes to nuclear localization
EDAENECPICAEEPISELALTRCWHSACKDCLLDHIEFQKSKNEVPLCPTCRQPINEQDIF
>gnl|CDD|438235 cd16573, RING-HC_TFB3-like, RING finger, HC subclass, found in RNA polymerase II transcription factor B subunit 3 (TFB3) from fungi. TFB3, also known as RNA polymerase II transcription factor B 38 kDa subunit, RNA polymerase II transcription factor B p38 subunit, or Rig2, is a component of the general transcription and DNA repair factor IIH (TFIIH or factor B), which is essential for both basal and activated transcription and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has CTD kinase and DNA-dependent ATPase activities, and is essential for polymerase II transcription in vitro. TFB3 is a homolog of MAT1 of higher eukaryotes which forms a ternary complex with MO15 (cdk7) and cyclin H. It physically interacts with Ubc4 and the Nedd8-conjugating enzyme Ubc12 as well as the Hrt1/Rtt101 complex. It targets the yeast Cul4-type cullin Rtt101 for its neddylation and ubiquitylation, and regulates neddylation and activity of cullin-3, but not Cdc53. TFB3 contains an N-terminal C3HC4-type RING-HC finger and a C-terminal MAT1 domain responsible for the interaction with the transcription factor TFIIH
DEKCPVCKSDRYLNPDMKFLINPECYHKMCESCVDRIFTLGPAQCPYKGCGKILRK
>gnl|CDD|438236 cd16574, RING-HC_Topors, RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein (Topors) and similar proteins. Topors, also known as topoisomerase I-binding RING finger protein, tumor suppressor p53- binding protein 3, or p53-binding protein 3 (p53BP3), is a ubiquitously expressed nuclear E3 ubiquitin-protein ligase that can ligate both ubiquitin and small ubiquitin-like modifier (SUMO) to substrate proteins in the nucleus. It contains an N-terminal C3HC4-type RING-HC finger which ligates ubiquitin to its target proteins including DNA topoisomerase I, p53, NKX3.1, H2AX, and the AAV-2 Rep78/68 proteins. As a RING-dependent E3 ubiquitin ligase, Topors works with the E2 enzymes UbcH5a, UbcH5c, and UbcH6, but not with UbcH7, CDC34, or UbcH2b. Topors acts as a tumor suppressor in various malignancies. It regulates p53 modification, suggesting it may be responsible for astrocyte elevated gene-1 (AEG-1, also known as metadherin, or LYRIC) ubiquitin modification. Plk1-mediated phosphorylation of Topors inhibits Topors-mediated sumoylation of p53, whereas p53 ubiquitination is enhanced, leading to p53 degradation. It also functions as a negative regulator of the prostate tumor suppressor NKX3.1. Moreover, Topors is associated with promyelocytic leukemia nuclear bodies, and may be involved in the cellular response to camptothecin. It also plays a key role in the turnover of H2AX protein, discriminating the type of DNA damaging stress. Furthermore, Topors is a cilia-centrosomal protein associated with autosomal dominant retinal degeneration. Mutations in TOPORS cause autosomal dominant retinitis pigmentosa (adRP)
DSSCPICLDRFENEKAFLDGCFHAFCFTCILEWSKVKNECPLCKQPF
>gnl|CDD|438237 cd16575, RING-HC_MID_C-I, RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins. MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. They also play a central role in the regulation of granule exocytosis. Functional redundancy exists between MID1 and MID2 in cytotoxic lymphocytes (CTL). Both MID1 and MID2 belong to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
LTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCASNESVESITAFQCPTCRY
>gnl|CDD|438238 cd16576, RING-HC_TRIM9-like_C-I, RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM67, and similar proteins. Tripartite motif-containing proteins TRIM9 and TRIM67 belong to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, consisting of three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM9 (the human ortholog of rat Spring), also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in neurodegenerative disorders through its ligase activity. TRIM67, also known as TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H, also known as glucosidase II beta, a protein kinase C substrate
EEELKCPVCGSLFTEPVILPCSHNLCLGCALNIQLTCPICHK
>gnl|CDD|438239 cd16577, RING-HC_MuRF_C-II, RING finger, HC subclass, found in muscle-specific RING finger proteins TRIM63/MuRF-1, TRIM55/MuRF-2 and TRIM54/MuRF-3. This subfamily corresponds to a group of striated muscle-specific tripartite motif (TRIM) proteins, including TRIM63/MuRF-1, TRIM55/MuRF-2, and TRIM54/MuRF-3, which function as E3 ubiquitin ligases in ubiquitin-mediated muscle protein turnover. They are tightly developmentally regulated in skeletal muscle and associate with different cytoskeleton components, such as microtubules, Z-disks and M-bands, as well as with metabolic enzymes and nuclear proteins. They also cooperate with diverse proteins implicated in selective protein degradation by the proteasome and autophagosome, and target proteins of metabolic regulation, sarcomere assembly and transcriptional regulation. Moreover, MURFs display variable fibre-type preferences. TRIM63/MuRF-1 is predominantly fast (type II) fibre-associated in skeletal muscle. TRIM55/MuRF-2 is predominantly slow-fibre associated. TRIM54/MuRF-3 is ubiquitously present. They play an active role in microtubule-mediated sarcomere assembly. MuRFs belong to the C-II subclass of the TRIM family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain positioned C-terminal to the RBCC domain. They also harbor a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains
LICPICLEMFTKPVVILPCQHNLCRKCANDIFQARNPYWPTTTMGSGGRFRCPSCR
>gnl|CDD|438240 cd16578, RING-HC_TRIM42_C-III, RING finger, HC subclass, found in tripartite motif-containing protein 42 (TRIM42) and similar proteins. TRIM42 belongs to the C-III subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain. It also has a novel cysteine-rich motif N-terminal to the RBCC domain, as well as a COS (carboxyl-terminal subgroup one signature) box and a fibronectin type-III (FN3) domain positioned C-terminal to the RBCC domain. TRIM42 can interact with TRIM27, a known cancer-associated protein. Its precise biological function remains unclear
QLVNHLVCPLCKRLRLHSFMLPCNHSLCEKCLRQLQKHAEVTENFFILVCPVCDRSHC
>gnl|CDD|438241 cd16579, RING-HC_PML_C-V, RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins. Protein PML, also known as RING finger protein 71 (RNF71) or tripartite motif-containing protein 19 (TRIM19), is predominantly a nuclear protein with a broad intrinsic antiviral activity. It is the eponymous component of PML nuclear bodies (PML NBs) and has been implicated in a wide variety of cell processes, including DNA damage signaling, apoptosis, and transcription. PML interferes with the replication of many unrelated viruses, including human immunodeficiency virus 1 (HIV-1), human foamy virus (HFV), poliovirus, influenza virus, rabies virus, EMCV, adeno-associated virus (AAV), and vesicular stomatitis virus (VSV). It also selectively interacts with misfolded proteins through distinct substrate recognition sites and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. PML belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain
EFKFLRCPGCKAEYKCPKLLPCLHTVCSGCLEALAEQASETTEFQCPICKAS
>gnl|CDD|438242 cd16580, RING-HC_TRIM8_C-V, RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar proteins. TRIM8, also known as glioblastoma-expressed RING finger protein (GERP) or RING finger protein 27 (RNF27), is a probable E3 ubiquitin-protein ligase that may promote proteasomal degradation of suppressor of cytokine signaling 1 (SOCS1) and further regulate interferon-gamma signaling. It functions as a new p53 modulator that stabilizes p53 impairing its association with MDM2 and inducing the reduction of cell proliferation. TRIM8 deficit dramatically impairs p53 stabilization and activation in response to chemotherapeutic drugs. TRIM8 also modulates tumor necrosis factor-alpha (TNFalpha) and interleukin-1beta (IL-1beta)-triggered nuclear factor-kappaB (NF- kappa B) activation by targeting transforming growth factor beta (TGFbeta) activated kinase 1 (TAK1) for K63-linked polyubiquitination. Moreover, TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. It also interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation of STAT3. TRIM8 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The coiled coil domain is required for homodimerization and the region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1
AENWKNCFEEELICPICLHVFVEPVQLPCKHNFCRGCIGEAWAKDAGLVRCPECNQAYNQKPSLEKN
>gnl|CDD|438243 cd16581, RING-HC_TRIM13_like_C-V, RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and similar proteins. TRIM13 and TRIM59, two closely related tripartite motif-containing proteins, belong to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, followed by a C-terminal transmembrane domain. TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis
EELTCSICYNIFDDPKILPCSHTFCKNCLEKLLAASGYYLLASLKCPTCR
>gnl|CDD|438244 cd16582, RING-HC_TRIM31_C-V, RING finger, HC subclass, found in tripartite motif-containing protein 31 (TRIM31) and similar proteins. TRIM31 is an E3 ubiquitin-protein ligase that primarily localizes to the cytoplasm, but is also associated with the mitochondria. It can negatively regulate cell proliferation and may be a potential biomarker of gastric cancer as it is overexpressed from the early stage of gastric carcinogenesis. TRIM31 is downregulated in non-small cell lung cancer and serves as a potential tumor suppressor. It interacts with p52 (Shc) and inhibits Src-induced anchorage-independent growth. TRIM31 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain
EVICPICLDILQKPVTIDCGHNFCLQCITQIGETSCGFFKCPLC
>gnl|CDD|438245 cd16583, RING-HC_TRIM40-C-V, RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar proteins. TRIM40, also known as probable E3 NEDD8-protein ligase or RING finger protein 35 (RNF35), is highly expressed in the gastrointestinal tract including the stomach, small intestine, and large intestine. It enhances neddylation of inhibitor of nuclear factor kappaB kinase subunit gamma (IKKgamma), inhibits the activity of nuclear factor-kappaB (NF-kappaB)-mediated transcription, and thus prevents inflammation-associated carcinogenesis in the gastrointestinal tract. TRIM40 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain
DSDEEGVCPICQEPLKEAVSTDCGHLFCRMCLTQHAKKASASGVFSCPVCRKPCSEGVLGDGY
>gnl|CDD|438246 cd16584, RING-HC_TRIM56_C-V, RING finger, HC subclass, found in tripartite motif-containing protein 56 (TRIM56) and similar proteins. TRIM56, also known as RING finger protein 109 (RNF109), is a virus-inducible E3 ubiquitin ligase that restricts pestivirus infection. It positively regulates the Toll-like receptor 3 (TLR3) antiviral signaling pathway, and possesses antiviral activity against bovine viral diarrhea virus (BVDV), a ruminant pestivirus classified within the family Flaviviridae shared by tick-borne encephalitis virus (TBEV). It also possesses antiviral activity against two classical flaviviruses, yellow fever virus (YFV) and dengue virus (DENV), as well as a human coronavirus, HCoV-OC43, which is responsible for a significant share of common cold cases. It may not act on positive-strand RNA viruses indiscriminately. Moreover, TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses. TRIM56 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain
FLACKICLEQLRAPKTLPCLHTYCQDCLAQLADGGRVRCPECRETVPVPPEGVASF
>gnl|CDD|438247 cd16585, RING-HC_TIF1_C-VI, RING finger, HC subclass, found in the transcriptional inknown asiary factor 1 (TIF1) subfamily and similar proteins. The TIF1 subfamily of transcriptional cofactors containing RING-HC fingers includes TIF1alpha (TRIM24), TIF1beta (TRIM28), and TIF1gamma (TRIM33), which belong to the C-VI subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1alpha and TIF1beta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. They bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. TIF1gamma is structurally closely related to TIF1alpha and TIF1beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatin proteins HP1alpha, beta and gamma. It cannot bind to nuclear receptors (NRs). TIF1delta (TRIM66) doesn't have a RING-HC finger and is not included in this model
LDTCAVCKQSFQSREPKLLPCLHSFCKRCLPPADRAAANPSPSGGAAGQVGVIRCPVCKQEC
>gnl|CDD|438248 cd16586, RING-HC_TRIM2_like_C-VII, RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and similar proteins. TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It also plays an important role in the central nervous system (CNS). In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. Both TRIM2 and TRIM3 belong to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain
FLSCGICLERYKNPKVLPCLHTFCERCLQNYIPAESLSLSCPVCR
>gnl|CDD|438249 cd16587, RING-HC_TRIM32_C-VII, RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar proteins. TRIM32, also known as 72 kDa Tat-interacting protein, zinc finger protein HT2A, or BBS11, is an E3 ubiquitin-protein ligase that promotes degradation of several targets, including actin, PIASgamma, Abl interactor 2, dysbindin, X-linked inhibitor of apoptosis (XIAP), p73 transcription factor, thin filaments and Z-bands during fasting. It plays important roles in neuronal differentiation of neural progenitor cells, as well as in controlling cell fate in skeletal muscle progenitor cells. It reduces PI3K-Akt-FoxO signaling in muscle atrophy by promoting plakoglobin-PI3K dissociation. It also functions as a pluripotency-reprogramming roadblock that facilitates cellular transition towards differentiation by modulating the levels of Oct4 and cMyc. Moreover, TRIM32 is an intrinsic influenza A virus (IAV) restriction factor which senses and targets the polymerase basic protein 1 (PB1) for ubiquitination and protein degradation. It also plays a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo, binds specifically to the activation domain of HIV-1 Tat, and can also interact with the HIV-2 and EIAV Tat proteins in vivo. Furthermore, TRIM32 regulates myoblast proliferation by controlling turnover of NDRG2 (N-myc downstream-regulated gene). It negatively regulates tumor suppressor p53 to promote tumorigenesis. It also facilitates degradation of MYCN on spindle poles and induces asymmetric cell division in human neuroblastoma cells. In addition, TRIM32 plays important roles in regulation of hyperactivities and positively regulates the development of anxiety and depression disorders induced by chronic stress. It also plays a role in regeneration by affecting satellite cell cycle progression via modulation of the SUMO ligase PIASy (PIAS4). Defects in TRIM32 leads to limb-girdle muscular dystrophy type 2H (LGMD2H), sarcotubular myopathies (STM) and Bardet-Biedl syndrome. TRIM32 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The NHL domain mediates the interaction with Argonaute proteins and consequently allows TRIM32 to modulate the activity of certain miRNAs
LECPICLESFDEGQLRPKLLHCGHTICEQCLEKLLASLSINGVRCPFCRKV
>gnl|CDD|438250 cd16588, RING-HC_TRIM45_C-VII, RING finger, HC subclass, found in tripartite motif-containing protein 45 (TRIM45) and similar proteins. TRIM45, also known as RING finger protein 99 (RNF99), is a novel receptor for activated C-kinase (RACK1)-interacting protein that suppresses transcriptional activities of Elk-1 and AP-1 and downregulates mitogen-activated protein kinase (MAPK) signal transduction through inhibiting RACK1/PKC (protein kinase C) complex formation. It also negatively regulates tumor necrosis factor alpha (TNFalpha)-induced nuclear factor-kappaB (NF-kappa B)-mediated transcription and suppresses cell proliferation. TRIM45 belongs to the C-VII subclass of the TRIM (tripartite motif) family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a filamin-type immunoglobulin (IG-FLMN) domain and NHL repeats positioned C-terminal to the RBCC domain
TRCPVCGKLFQEPRLLPCLHTLCSPCLRQLEPFSVCGLRGGDRSEKSNYSVLCPVCDSE
>gnl|CDD|438251 cd16589, RING-HC_TRIM71_C-VII, RING finger, HC subclass, found in tripartite motif-containing protein 71 (TRIM71) and similar proteins. TRIM71, also known as protein lineage variant 41 (lin-41), is an E3 ubiquitin-protein ligase that may play essential roles in embryonic stem cells, cellular reprogramming and the timing of embryonic neurogenesis. It was first identified in the nematode Caenorhabditis elegans as a target of the differentiation-associated microRNA (miRNA) let-7 (lethal 7) and is therefore part of a heterochronic gene network that controls larval development. In humans, it regulates let-7 microRNA biogenesis via modulation of Lin28B protein polyubiquitination. TRIM71 localizes to cytoplasmic P-bodies and directly interacts with the miRNA pathway proteins Argonaute 2 (AGO2) and DICER. It represses miRNA activity by promoting degradative ubiquitination of AGO2. Moreover, TRIM71 associates with SHCBP1, a novel component of the fibroblast growth factor (FGF) signaling pathway, and regulates its non-degradative polyubiquitination. It is also involved in the post-transcriptional regulation of the CDKN1A, RBL1 and RBL2 or EGR1 mRNAs by mediating RNA-binding in embryonic stem cells. TRIM71 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain
MASFPESDFQRCPLCKEMCGSPAPLSSNSSTSSTSSGGGGGSAGAATRRLHVLPCLHAFCRQCLEAQRSP
GAGPALKLRCPVCDQKVVLSE
>gnl|CDD|438252 cd16590, RING-HC_TRIM4_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar proteins. TRIM4 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM4, also known as RING finger protein 87 (RNF87), is a cytoplasmic E3 ubiquitin-protein ligase that has recently evolved and is present only in higher mammals. It transiently interacts with mitochondria, induces mitochondrial aggregation and sensitizes the cells to hydrogen peroxide (H2O2) induced death. Its interaction with peroxiredoxin 1 (PRX1) is critical for the regulation of H2O2 induced cell death. Moreover, TRIM4 functions as a positive regulator of RIG-I-mediated type I interferon induction. It regulates the K63-linked ubiquitination of RIG-1 and assembly of antiviral signaling complex at the mitochondria
EDIQEELTCPICLDYFQDPVSIECGHNFCRGCLHRNWAPGGGPFPCPECRHPSAPAALRPN
>gnl|CDD|438253 cd16591, RING-HC_TRIM5-like_C-IV, RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins. TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections
VNIKEEVTCPICLELLTEPLSLDCGHSFCQACITANHKESVNQEGESSCPVCRTSYQPENLRPNRHLANI
VE
>gnl|CDD|438254 cd16592, RING-HC_RNF39, RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins. RNF39, also called protein HZFw, may play a role in prolonged long term-potentiation (LTP) maintenance. It is involved in the etiology of Behcet's disease (BD). It may also be involved in HIV-1 replication. RNF39 acts as an E3 ubiquitin ligase that inhibits retinoic acid-inducible gene-I (RIG-I)-like receptor (RLR) pathways by mediating K48-linked ubiquitination and proteasomal degradation of DDX3X (DEAD-box RNA helicase 3, X-linked). RNF39 contains a typical C3HC4-type RING-HC finger
LQEETTCPICLGYFKDPVILDCEHSFCRACIARHWGQEAMEGNGAEGVFCPQCGEPCP
>gnl|CDD|438255 cd16593, RING-HC_TRIM10_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar proteins. TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM10 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
SLADEVNCPICQGTLREPVTIDCGHNFCRACLTRYCEIPGPDLEEPPTCPLCKEPFRPGEF
>gnl|CDD|438256 cd16594, RING-HC_TRIM7-like_C-IV, RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and TRIM27, and similar proteins. TRIM7, TRIM11 and TRIM27, closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) by mediating the degradation of CCHS-associated polyalanine-expanded Phox2b. TRIM11 modulates the function of neurogenic transcription factor Pax6 through the ubiquitin-proteosome system, and thus plays an essential role for Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM27, also known as RING finger protein 76 (RNF76), RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. In addition, it inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. TRIM27 promotes a non-canonical polyubiquitination of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. TRIM27 also forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is a component of an estrogen receptor 1 (ESR1) regulatory complex that is involved in estrogen receptor-mediated transcription in MCF-7 cells
SLQEELTCPICLDYFTDPVTLDCGHSFCRACIARCWEEPETSASCPQCRETCPQRNLRPNR
>gnl|CDD|438257 cd16595, RING-HC_TRIM17_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar proteins. TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (Terf), is a crucial E3 ubiquitin ligase that is necessary and sufficient for neuronal apoptosis and contributes to Mcl-1 ubiquitination in cerebellar granule neurons (CGNs). It interacts in a SUMO-dependent manner with nuclear factor of activated T cell NFATc3 transcription factor, and thus inhibits the activity of NFATc3 by preventing its nuclear localization. In contrast, it binds to and inhibits NFATc4 transcription factor in a SUMO-independent manner. Moreover, TRIM17 stimulates degradation of kinetochore protein ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates cell proliferation. TRIM17 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
RLQEEATCSICLDYFTDPVMTTCGHNFCRACIQLSWEKARGKKGRRKQKGSFPCPECREMSPQRNLRPNR
>gnl|CDD|438258 cd16596, RING-HC_TRIM21_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar proteins. TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting it may be a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated with uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
ARLTMMWEEVTCPICLDPFVEPVSIECGHSFCQECISQVGKGGGSVCPVCRQRFLLKNLRPNRQLANMVN
NLKEISQ
>gnl|CDD|438259 cd16597, RING-HC_TRIM25_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar proteins. TRIM25, also known as estrogen-responsive finger protein (EFP), RING finger protein 147 (RNF147), or RING-type E3 ubiquitin transferase, is an E3 ubiquitin/ISG15 ligase that is induced by estrogen and is therefore particularly abundant in placenta and uterus. TRIM25 regulates various cellular processes through E3 ubiquitin ligase activity, transferring ubiquitin and ISG15 to target proteins. It mediates K63-linked polyubiquitination of retinoic acid inducible gene I (RIG-I) that is crucial for downstream antiviral interferon signaling. It is also required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF-kappaB) and interferon production. Upon UV irradiation, TRIM25 interacts with mono-ubiquitinated PCNA and promotes its ISG15 modification (ISGylation), suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also functions as a novel regulator of p53 and Mdm2. It enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. Meanwhile, it inhibits p53's transcriptional activity and dampens the response to DNA damage, and is essential for medaka development and this dependence is rescued by silencing of p53. Moreover, TRIM25 is involved in the host cellular innate immune response against retroviral infection. It interferes with the late stage of feline leukemia virus (FeLV) replication. Furthermore, TRIM25 acts as an oncogene in gastric cancer. Its blockade by RNA interference inhibits migration and invasion of gastric cancer cells through transforming growth factor-beta (TGF-beta) signaling, suggesting it presents a novel target for the detection and treatment of gastric cancer. In addition, TRIM25 acts as an RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
DLEEELTCSICLELFKDPVTLPCGHNFCGVCIEKTWDSQHGSEYSCPQCRATFPRRPELHKNTVLRNIVE
Q
>gnl|CDD|438260 cd16598, RING-HC_TRIM26_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar proteins. TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM26 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
LEEEVTCSICLDYLRDPVTIDCGHNFCRSCITDYCPISGGHERPVCPLCRKPFKKENIRPNWQL
>gnl|CDD|438261 cd16599, RING-HC_TRIM35_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar proteins. TRIM35, also known as hemopoietic lineage switch protein 5 (HLS5), is a putative hepatocellular carcinoma (HCC) suppressor that inhibits phosphorylation of pyruvate kinase isoform M2 (PKM2), which is involved in aerobic glycolysis of cancer cells and further suppresses the Warburg effect and tumorigenicity in HCC. It also negatively regulates Toll-like receptor 7 (TLR7)- and TLR9-mediated type I interferon production by suppressing the stability of interferon regulatory factor 7 (IRF7). Moreover, TRIM35 regulates erythroid differentiation by modulating globin transcription factor 1 (GATA-1) activity. TRIM35 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
FKEELLCPICYEPFREAVTLRCGHNFCKGCVSRSWERQPRAPCPVCKEASSSDDLRTNHTLNNLVE
>gnl|CDD|438262 cd16600, RING-HC_TRIM38_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein 38 (TRIM38) and similar proteins. TRIM38, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is an E3 ubiquitin-protein ligase that promotes K63- and K48-linked ubiquitination of cellular proteins and also catalyzes self-ubiquitination. It negatively regulates Tumor necrosis factor alpha (TNF-alpha)- and interleukin-1beta-triggered Nuclear factor-kappaB (NF-kappaB) activation by mediating lysosomal-dependent degradation of transforming growth factor beta (TGFbeta)-activated kinase 1 (TAK1)-binding protein (TAB)2/3, two critical components of the TAK1 kinase complex. It also inhibits TLR3/4-mediated activation of NF-kappaB and interferon regulatory factor 3 (IRF3) by mediating ubiquitin-proteasomal degradation of TNF receptor-associated factor 6 (Traf6) and NAK-associated protein 1 (Nap1), respectively. Moreover, TRIM38 negatively regulates TLR3-mediated interferon beta (IFN-beta) signaling by targeting ubiquitin-proteasomal degradation of TIR domain-containing adaptor inducing IFN-beta (TRIF). It functions as a valid target for autoantibodies in primary Sjogren's Syndrome. TRIM38 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
KMREEATCSICLQLMTEPVSINCGHSYCKRCIVSFLENQSQLEPGLETFSCPQCRAPF
>gnl|CDD|438263 cd16601, RING-HC_TRIM39_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins. TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcription, which is induced by inflammatory stimulants such as tumor necrosis factor alpha. Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
EASCSLCKEYLKDPVIIECGHNFCRACITRFWEELDGDFPCPQC
>gnl|CDD|438264 cd16602, RING-HC_TRIM41-like_C-IV, RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and similar proteins. TRIM41 and TRIM52, two closely related tripartite motif-containing proteins, have dramatically expanded RING domains compared with the rest of the TRIM family proteins. TRIM41 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of the TRIM family that contains only RBCC domains. TRIM41, also known as RING finger-interacting protein with C kinase (RINCK), is an E3 ubiquitin-protein ligase that promotes the ubiquitination of protein kinase C (PKC) isozymes in cells. It specifically recognizes the C1 domain of PKC isozymes. It controls the amplitude of PKC signaling by controlling the amount of PKC in the cell. TRIM52, also known as RING finger protein 102 (RNF102), is encoded by a novel, noncanonical antiviral TRIM52 gene in primate genomes with unique specificity determined by the rapidly evolving RING domain
QEEAVCAICLDYFKDPVSIGCGHNFCRVCVTQLWGFTCPQCRKSFPRRSFRPN
>gnl|CDD|438265 cd16603, RING-HC_TRIM43-like_C-IV, RING finger, HC subclass, found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, TRIM51, TRIM64 and similar proteins. The family includes a group of closely related uncharacterized tripartite motif-containing proteins, TRIM43, TRIM43B, TRIM48/RNF101, TRIM49/RNF18, TRIM49B, TRIM49C/TRIM49L2, TRIM49D/TRIM49L, TRIM51/SPRYD5, TRIM64, TRIM64B, and TRIM64C, whose biological function remain unclear. TRIM49, also known as testis-specific RING-finger protein, has moderate similarity with SS-A/Ro52 antigen, suggesting it may be one of the target proteins of autoantibodies in the sera of patients with these autoimmune disorders. All family members belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. In RBCC region, they all have a C3HC4-type RING-HC finger
FQRELTCPICMNYFIDPVTIDCGHSFCRPCLYLNWQDIPFLAQCPECRKTTEQRNLKTN
>gnl|CDD|438266 cd16604, RING-HC_TRIM47-like_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar proteins. TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. It plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. This subfamily also includes RING finger protein 135 (RNF135). RNF135, also known as RIG-I E3 ubiquitin ligase (REUL) or Riplet, is a widely expressed E3 ubiquitin-protein ligase that consists of an N-terminal C3HC4-type RING-HC finger and C-terminal B30.2/SPRY and PRY motifs, but lacks the B-box and coiled-coil domains that are also typically present in TRIM proteins. RNF135 serves as a specific retinoic acid-inducible gene-I (RIG-I)-interacting protein that ubiquitinates RIG-I and specifically stimulates RIG-I-mediated innate antiviral activity to produce antiviral type-I interferon (IFN) during the early phase of viral infection. It also has been identified as a bio-marker and therapy target of glioblastoma. It associates with the ERK signal transduction pathway and plays a role in glioblastoma cell proliferation, migration and cell cycle
LSCPICLDLLKDPVTLPCGHSFCMGCLGALWGAGRGGRASCPLCRQTFP
>gnl|CDD|438267 cd16605, RING-HC_TRIM50_like_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 and similar proteins. TRIM50 is a stomach-specific E3 ubiquitin-protein ligase, encoded by the Williams-Beuren syndrome (WBS) TRIM50 gene, which regulates vesicular trafficking for acid secretion in gastric parietal cells. It colocalizes, interacts with, and increases the level of p62/SQSTM1, a multifunctional adaptor protein implicated in various cellular processes including the autophagy clearance of polyubiquitinated protein aggregates. It also promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through the interaction with histone deacetylase 6 (HDAC6), a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. TRIM50 can be acetylated by PCAF and p300. TRIM50 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. This subfamily also includes two paralogs of TRIM50, tripartite motif-containing protein 73 (TRIM73), also known as tripartite motif-containing protein 50B (TRIM50B), and tripartite motif-containing protein 74 (TRIM74), also known as tripartite motif-containing protein 50C (TRIM50C), both of which are WBS-related genes encoding proteins that may also act as E3 ligases. In contrast with TRIM50, TRIM73 and TRIM74 belong to the C-V subclass of TRIM family of proteins that are defined by N-terminal RBCC domains only
LLCPICLEVFKEPLMLQCGHSYCKSCLVSLSGELDGQLLCPVCRQ
>gnl|CDD|438268 cd16606, RING-HC_TRIM58_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar proteins. TRIM58, also known as protein BIA2, is an erythroid E3 ubiquitin-protein ligase induced during late erythropoiesis. It binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. It may participate in the erythroblast enucleation process through regulation of nuclear polarization. TRIM58 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
EEARCPVCLDFLQEPVSVDCGHSFCLRCISEFCEKSDSAQGGVYACPQCRGPF
>gnl|CDD|438269 cd16607, RING-HC_TRIM60-like_C-IV, RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61, TRIM75 and similar proteins. TRIM60, also known as RING finger protein 129 (RNF129) or RING finger protein 33 (RNF33), is a cytoplasmic protein expressed in the testis. It may play an important role in the spermatogenesis process, the development of the preimplantation embryo, and in testicular functions. RNF33 interacts with the cytoplasmic kinesin motor proteins KIF3A and KIF3B suggesting possible contribution to cargo movement along the microtubule in the expressed sites. It is also involved in spermatogenesis in Sertoli cells under the regulation of nuclear factor-kappaB (NF-kappaB). TRIM75 mainly localizes within spindles, suggesting it may function in spindle organization and thereby affect meiosis. Both TRIM60 and TRIM75 belong the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B2-box, and two coiled coil domains, as well as a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM61 belongs to the C-V subclass of the TRIM family that contains RBCC domains only. Its biological function remains unclear
EASCPICLDYLKDPVTINCGHNFCRSCISMSWKDLQDTFPCPVCRFCC
>gnl|CDD|438270 cd16608, RING-HC_TRIM62_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar proteins. TRIM62, also known as Ductal Epithelium Associated Ring Chromosome 1 (DEAR1), is a cytoplasmic E3 ubiquitin-protein ligase that was identified as a dominant regulator of acinar morphogenesis in the mammary gland. It is implicated in the inflammatory response of immune cells by regulating the Toll-like receptor 4 (TLR4) signaling pathway, leading to increased activity of the activator protein 1 (AP-1) transcription factor in primary macrophages. It is also involved in muscular protein homeostasis, especially during inflammation-induced atrophy, and may play a role in the pathogenesis of ICU-acquired weakness (ICUAW) by activating and maintaining inflammation in myocytes. Moreover, TRIM62 facilitates K27-linked poly-ubiquitination of CARD9 and also regulates CARD9-mediated anti-fungal immunity and intestinal inflammation. It also functions as a chromosome 1p35 tumor suppressor and negatively regulates transforming growth factor beta (TGFbeta)-driven epithelial-mesenchymal transition (EMT) by binding to and promoting the ubiquitination of SMAD3, a major effector of TGFbeta-mediated EMT. TRIM62 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
SSLKDELLCSICLSIYQDPVSLGCEHYFCRQCITEHWSRSEHRDCPECRRTF
>gnl|CDD|438271 cd16609, RING-HC_TRIM65_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins. TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5, enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into the development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
EEELTCSICLGLYQDPVTLPCQHSFCRACIEDHWRQKDEGSFSCPECRAPFPEGPTLE
>gnl|CDD|438272 cd16610, RING-HC_TRIM68_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar proteins. TRIM68, also known as RING finger protein 137 (RNF137) or SSA protein SS-56 (SS-56), is an E3 ubiquitin-protein ligase that negatively regulates Toll-like receptor (TLR)- and RIG-I-like receptor (RLR)-driven type I interferon production by degrading TRK fused gene (TFG), a novel driver of IFN-beta downstream of anti-viral detection systems. It also functions as a cofactor for androgen receptor-mediated transcription by regulating ligand-dependent transcription of androgen receptor in prostate cancer cells. Moreover, TRIM68 is a cellular target of autoantibody responses in Sjogre's syndrome (SS), as well as systemic lupus erythematosus (SLE). It is also an auto-antigen for T cells in SS and SLE. TRIM68 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
EVACPICMTFLREPVSIDCGHSFCHSCLSGLWEVPGESQNWGYTCPLCR
>gnl|CDD|438273 cd16611, RING-HC_TRIM69_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar proteins. TRIM69, also known as RFP-like domain-containing protein trimless or RING finger protein 36 (RNF36), is a testis E3 ubiquitin-protein ligase that plays a specific role in apoptosis and may also play an important role in germ cell homeostasis during spermatogenesis. TRIM69 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
LTEELHCPLCLDFFRDPVMLSCGHNFCQSCITGFWELQAEDTTCPECRELCQYRNLTPN
>gnl|CDD|438274 cd16612, RING-HC_TRIM72_C-IV, RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar proteins. TRIM72, also known as Mitsugumin-53 (MG53), is a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at muscle injury sites. It is required in repair of alveolar epithelial cells under plasma membrane stress failure. It interacts with dysferlin to regulate sarcolemmal repair. Upregulation of TRIM72 develops obesity, systemic insulin resistance, dyslipidemia, and hyperglycemia, as well as induces diabetic cardiomyopathy through transcriptional activation of the peroxisome proliferation-activated receptor alpha (PPAR-alpha) signaling pathway. Compensation for the absence of AKT signaling by ERK signaling during TRIM72 overexpression leads to pathological hypertrophy. Moreover, TRIM72 functions as a novel negative feedback regulator of myogenesis by targeting insulin receptor substrate-1 (IRS-1). It is transcriptionally activated by the synergism of myogenin (MyoD) and myocyte enhancer factor 2 (MEF2). TRIM72 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
MHQDLSCPLCLKLFQSPVTTECGHTFCQDCLSRVPKEEDGGSTSCPTCQAPTKPEQLSIN
>gnl|CDD|438275 cd16613, RING-HC_UHRF, RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing proteins, UHRF1 and UHRF2, and similar proteins. UHRF1 is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of transcription factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF2 was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation, but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. Both UHRF1 and UHRF2 contain an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal C3HC4-type RING-HC finger
FTCICCQELVYKPITTPCKHNICKSCLQRSFKAEVYTCPACRHDLG
>gnl|CDD|438276 cd16614, RING-HC_UNK-like, RING finger, HC subclass, found in RING finger protein unkempt (UNK), unkempt-like (UNKL), and similar proteins. UNK, also known as zinc finger CCCH domain-containing protein 5, is a metazoan-specific zinc finger protein enriched in embryonic brains. It may play a broad regulatory role during the formation of the central nervous system (CNS). It is a sequence-specific RNA-binding protein required for early neuronal morphology. UNK is a neurogenic component of the mTOR pathway, and functions as a negative regulator of the timing of photoreceptor differentiation. It also specifically binds to Brg/Brm-associated factor BAF60b and promotes its ubiquitination in a Rac1-dependent manner. UNKL, also known as zinc finger CCCH domain-containing protein 5-like, is a putative E3 ubiquitin-protein ligase that may participate in a protein complex showing an E3 ligase activity regulated by RAC1. Both UNK and UNKL contain several tandem CCCH-type zinc fingers at the N-terminus, and a C3HC4-type RING-HC finger at its C-terminus
KKCMKCEERNRSVAVLPCQHYVLCEQCAETATECPYCH
>gnl|CDD|438277 cd16615, RING-HC_ZNF598, RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins. ZNF598 associates with eukaryotic initiation factor 4E (eIF4E) homologous protein from mammals (m4EHP) by binding to Grb10-interacting GYF protein 2 (GIGYF2). The m4EHP-GIGYF2 complex functions as a translational repressor and is essential for normal embryonic development of mammalian. ZNF598 harbors a C3HC4-type RING-HC finger at its N-terminus
ETCVICCEEIEYFAVGPCNHPVCYKCSLRMRVLYKDKYCPICRTELDKVIF
>gnl|CDD|438278 cd16616, mRING-HC-C4C4_Asi1p-like, Modified RING finger, HC subclass (C4C4-type), found in Saccharomyces cerevisiae amino acid sensor-independent protein Asi1p, Asi3p and similar proteins. Asi1p and Asi3p are inner nuclear membrane proteins that act as negative regulators of SPS (Ssy1-Ptr3-Ssy5)-sensor signaling in yeast. Together with Asi2p, they assemble into an Asi complex that functions in the SPS amino acid sensing pathway involved in degradation of Stp1 and Stp2 transcription factors. Both Asi1p and Asi3p contain five membrane-spanning domains, as well as highly conserved RING fingers at their extreme C termini, which are C4C4-type RING finger motifs whose overall folding is similar to that of the C3HC4-type RING-HC finger
DLSCVICKSNPRNIVLWPCRCLALCDDCRLSLAMRGFHTCVCCRREVKGYSKI
>gnl|CDD|438279 cd16617, mRING-HC-C4C4_CesA, Modified RING finger, HC subclass (C4C4-type), found in Arabidopsis thaliana cellulose synthase A (CesA) catalytic subunits 1-10, and similar proteins from plants. This subfamily includes plant catalytic subunits of cellulose synthase terminal complexes ("rosettes") required for beta-1,4-glucan microfibril crystallization, a major mechanism of cell wall formation. CesA1, also known as protein RADIALLY SWOLLEN 1 (RSW1), is required during embryogenesis for cell elongation, orientation of cell expansion and complex cell wall formations, such as interdigitated pattern of epidermal pavement cells, stomatal guard cells, and trichomes. It plays a role in lateral roots formation, but seems unnecessary for the development of tip-growing cells such as root hairs. CesA2, also known as Ath-A, is involved in the primary cell wall formation. It forms a homodimer. CesA3, also known as constitutive expression of VSP1 protein 1, isoxaben-resistant protein 1, Ath-B, protein ECTOPIC LIGNIN 1, or protein RADIALLY SWOLLEN 5 (RSW5), is involved in primary cell wall formation, especially in roots. CesA4, also known as protein IRREGULAR XYLEM 5 (IRX5), is involved in the secondary cell wall formation, and required for xylem cell wall thickening. CesA5 may be partially redundant with CesA6. CesA6, also known as AraxCelA, isoxaben-resistant protein 2, protein PROCUSTE 1, or protein QUILL, is involved in primary cell wall formation. Like CesA1, CesA6 is critical for cell expansion. CESA6-dependent cell elongation seems to be independent of gibberellic acid, auxin, and ethylene. CesA6 interacts with and moves along cortical microtubules for the process of cellulose deposition. CesA7, also known as protein FRAGILE FIBER 5, or protein IRREGULAR XYLEM 3 (IRX3), and CesA8, also known as protein IRREGULAR XYLEM 1 (IRX1) or protein LEAF WILTING 2, are both involved in secondary cell wall formation and also required for xylem cell wall thickening. The biological function of CesA9 and CesA10 remain unclear. CesA1, CesA3, and CesA6 form a functional complex essential for primary cell wall cellulose synthesis, while CesA4, CesA7, and CesA8 form a functional complex located in secondary cell wall deposition sites. All family members contain an N-terminal C4C4-type RING-HC finger and a C-terminal glycosyltransferase family A (GT-A) domain
QICQICGDEIGLTVNGELFVACNECGFPVCRPCYEYERKEGNQCCPQCKTR
>gnl|CDD|438280 cd16618, mRING-HC-C4C4_CNOT4, Modified RING finger, HC subclass (C4C4-type), found in CCR4-NOT transcription complex subunit 4 (NOT4) and similar proteins. NOT4, also known as CCR4-associated factor 4, E3 ubiquitin-protein ligase CNOT4, or potential transcriptional repressor NOT4, is a component of the multifunctional CCR4-NOT complex, a global regulator of RNA polymerase II transcription. It associates with polysomes and contributes to the negative regulation of protein synthesis. NOT4 functions as an E3 ubiquitin-protein ligase that interacts with a specific E2, Ubc4/5 in yeast, and the ortholog UbcH5B in humans, and ubiquitylates a wide range of substrates, including ribosome-associated factors. Thus, it plays a role in cotranslational quality control (QC) through ribosome-associated ubiquitination and degradation of aberrant peptides. NOT4 contains a C4C4-type RING finger motif, whose overall folding is similar to that of the C3HC4-type RING-HC finger, a central RNA recognition motif (RRM), and a C-terminal domain predicted to be unstructured
PECPLCMEELDITDLNFFPCPCGYQICLFCWHRIREDENGRCPACRK
>gnl|CDD|438281 cd16619, mRING-HC-C4C4_TRIM37_C-VIII, Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 (TRIM37) and similar proteins. TRIM37, also known as mulibrey nanism protein, or MUL, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro
FRCFICMEKLRDPRLCPHCSKLFCKGCIRRWLSEQRSSCPHCR
>gnl|CDD|438282 cd16620, vRING-HC-C4C4_RBBP6, Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) and similar proteins. RBBP6, also known as proliferation potential-related protein, protein P2P-R, retinoblastoma-binding Q protein 1 (RBQ-1), or p53-associated cellular protein of testis (PACT), is a nuclear E3 ubiquitin-protein ligase involved in multiple processes, such as the control of gene expression, mitosis, cell differentiation, and cell apoptosis. It plays a role in both promoting and inhibiting apoptosis in many human cancers, including esophageal, lung, hepatocellular, and colon cancers, familial myeloproliferative neoplasms, as well as in human immunodeficiency virus-associated nephropathy (HIVAN). It functions as an Rb- and p53-binding protein that plays an important role in chaperone-mediated ubiquitination and possibly in protein quality control. It acts as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in an increase of MDM2-mediated ubiquitination and degradation of p53/TP53, and leading to both apoptosis and cell growth. It is also a double-stranded RNA-binding protein that plays a role in mRNA processing by regulating the human polyadenylation machinery and modulating expression of mRNAs with AU-rich 3' untranslated regions (UTRs). Moreover, RBBP6 ubiquitinates and destabilizes the transcriptional repressor ZBTB38 that negatively regulates transcription and levels of the MCM10 replication factor on chromatin. Furthermore, RBBP6 is involved in tunicamycin-induced apoptosis by mediating protein kinase (PKR) activation. RBBP6 contains an N-terminal ubiquitin-like domain and a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger. RBBP6 interacts with chaperones Hsp70 and Hsp40 through its N-terminal ubiquitin-like domain. It promotes the ubiquitination of p53 by Hdm2 in an E4-like manner through its RING finger. It also interacts directly with the pro-proliferative transcription factor Y-box-binding protein-1 (YB-1) via its RING finger
PDELKCPICKDLMKDAVLTPCCGNSFCDECIRTALLEEDFTCPTCKEPDVSPDAL
>gnl|CDD|438283 cd16621, vRING-HC-C4C4_RFPL, Variant RING finger, HC subclass (C4C4-type), found in Ret finger protein-like (RFPL) family. The RFPL family, also known as the RING-B30 family, represents a group of RFPL gene products, RFPL1, RFPL2, RFPL3, and RFPL4A, which are characterized by containing an N-terminal RFPL1, 2, 3-specifying helix (RSH), a C4C4- or a variant C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger, an RFPL-defining motif (RDM), and C-terminal PRY/SPRY-forming B30.2 domain. RFPL1, also known as RING finger protein 78 (RNF78), is expressed during cell differentiation. RFPL2, also known as RING finger protein 79 (RNF79), shows high sequence similarity with other RFPL gene products. Its biological role remains unclear. RFPL3 interacts directly with CREB binding protein (CBP) in the nucleus of lung cancer cells. RFPL3 and CBP synergistically upregulate TERT activity and promote lung cancer growth. Moreover, RFPL3 acts as a novel E3 ubiquitin ligase modulating the integration activity of human immunodeficiency virus, type 1 (HIV-1) preintegration complex. RFPL4A, also known as RING finger protein 210 (RNF210), is a novel factor that increases the G1 population and decreases sensitivity to chemotherapy in human colorectal cancer cells. This model corresponds to the C4C4-type RING finger. RFPL4A lacks the fourth conserved zinc-binding residue, cysteine, and the eighth zinc-binding residue, cysteine; in RFPL2, it is replaced by serine
SSCPVCSDYLEKPVSLECGYACCLQCLNSLQKEPHGEGLLCCCCSVVS
>gnl|CDD|438284 cd16622, vRING-HC-C4C4_RBR_RNF217, Variant RING finger, HC subclass (C4C4-type), found in RING finger protein 217 (RNF217) and similar proteins. RNF217, also known as IBR domain-containing protein 1 (IBRDC1), is a transmembrane (TM) domain-containing RBR-type E3 ubiquitin-protein ligase mainly expressed in testis and skeletal muscle, as different splice variants. It interacts with the anti-apoptotic protein HAX1, and is adjacent to a translocation breakpoint involving ETV6 in childhood acute lymphoblastic leukemia (ALL). RNF217 contains a RBR domain followed by TMs. The RBR domain was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a variant C4C4-type RING finger whose overall folding is similar to that of the C3HC4-type RING-HC finger. It is required for RBR-mediated ubiquitination
LTCRVCLEDKQIKPLPCCKKAVCEECLKRYLSSQVQLGQAEIMCPITEC
>gnl|CDD|438285 cd16623, RING-HC_RFPL4B, RING finger, HC subclass, found in Ret finger protein-like 4B (RFPL4B) and similar proteins. RFPL4B, also called RING finger protein 211 (RNF211), is an uncharacterized RING finger protein containing a typical C3HC4-type RING-HC finger
MANRLEMEATCPICLDFFSHPISLSCAHIFCFDCIQKWMTKREDSILTCPLCRKEQKKPVLEE
>gnl|CDD|438286 cd16624, RING-HC_RBR_CUL9, RING finger, HC subclass, found in cullin-9 (CUL-9) and similar proteins. CUL-9, also known as UbcH7-associated protein 1 (H7-AP1), p53-associated parkin-like cytoplasmic protein, or PARC, is a cytoplasmic RBR-type E3 ubiquitin-protein ligase that is a tumor suppressor and promotes p53-dependent apoptosis. It mediates the ubiquitination and degradation of cytosolic cytochrome c to promote survival in neurons and cancer cells. It is also a critical downstream effector of the 3M complex in the maintenance of microtubules and genome integrity. Moreover, CUL-9, together with CUL-7, forms homodimers and heterodimers, as well as some atypical cullin RING ligase complexes, which may exhibit ubiquitin ligase activity. CUL-9 contains a CPH domain (Cul7, PARC, and HERC2), a DOC (DOC1/APC10) domain, cullin homology (CH) domains linked with E3 ligase function, and a C-terminal RBR domain previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination
THCPVCVSQLSPDEPLPTLCCMHYCCKSCWKEYLTTRIEQNLVLNCTCPITDC
>gnl|CDD|438287 cd16625, RING-HC_RBR_HEL2-like, RING finger, HC subclass, found in Saccharomyces cerevisiae histone E3 ligase 2 (HEL2) and similar proteins. HEL2 is an E3 ubiquitin-protein ligase that interacts with the E2 ubiquitin-conjugating enzyme UBC4 and histones H3 and H4. It plays an important role in regulating histone protein levels and also likely to contribute to the maintenance of genomic stability in the budding yeast. HEL2 can be phosphorylated by the DNA damage checkpoint kinase and histone protein regulator Rad53. This subfamily also includes Schizosaccharomyces pombe histone E3 ligase 1 (HEL1), also known as DNA-break-localizing protein 4 (dbl4), and Dictyostelium discoideum Ariadne-like ubiquitin ligase (RbrA). RbrA may act as an E3 ubiquitin-protein ligase that appears to be required for normal cell-type proportioning and cell sorting during multicellular development, and is also necessary for spore cell viability. Members of this subfamily contain an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination
FECPICCDDGELETFSLECGHEFCVDCYSQYLTSKIKEEGEGCRITCPGEKCNLILD
>gnl|CDD|438288 cd16626, RING-HC_RBR_HHARI, RING finger, HC subclass, found in human homolog of Drosophila ariadne (HHARI) and similar proteins. This subfamily includes Drosophila melanogaster protein ariadne-1 (ARI-1), and its eukaryotic homologs, such as HHARI. ARI-1 is a widely expressed Drosophila RING-finger protein that localizes mainly in the cytoplasm and is required for neural development. It interacts with a novel ubiquitin-conjugating enzyme, UbcD10. HHARI, also known as H7-AP2, monocyte protein 6 (MOP-6), protein ariadne-1 homolog, Ariadne RBR E3 ubiquitin protein ligase 1 (ARIH1), ariadne-1 (ARI-1), UbcH7-binding protein, UbcM4-interacting protein, or ubiquitin-conjugating enzyme E2-binding protein 1, is an RBR-type E3 ubiquitin-protein ligase highly expressed in nuclei, where it is co-localized with nuclear bodies including Cajal, PML, and Lewy bodies. It interacts with the E2 conjugating enzymes UbcH7, UbcH8, UbcM4, and UbcD10 in human, mouse, and fly, and modulates the ubiquitylation of substrate proteins including single-minded 2 (SIM2) and translation initiation factor 4E homologous protein (4EHP). It functions as a potent mediator of DNA damage-induced translation arrest, which protects stem and cancer cells against genotoxic stress by initiating a 4EHP-mediated mRNA translation arrest. HHARI contains an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination
MPCDICYLNYPNSYMTGLECGHKFCMQCWKEYLTTKIMEEGMGQTISCPAHGCDILVDD
>gnl|CDD|438289 cd16627, RING-HC_RBR_parkin, RING finger, HC subclass, found in parkin and similar proteins. Parkin, also known as Parkinson juvenile disease protein 2, is an RBR-type E3 ubiquitin-protein ligase that is associated with recessive early onset Parkinson"s disease (PD), and exerts a protective effect against dopamine-induced alpha-synuclein-dependent cell toxicity. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Parkin functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPT5, TOMM20, USP30, ZNF746, and AIMP2. It mediates monoubiquitination, as well as Lys-6-, Lys-11-, Lys-48- and Lys-63-linked polyubiquitination of substrates depending on the context. Parkin may enhance cell viability and protect dopaminergic neurons from oxidative stress-mediated death by regulating mitochondrial function. It also limits the production of reactive oxygen species (ROS) and regulates cyclin-E during neuronal apoptosis. Moreover, parkin displays a ubiquitin ligase-independent function in transcriptional repression of p53. Parkin contains an N-terminal ubiquitin-like domain and a C-terminal RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination
VPCITCTDVRSPVLVFPCESRHVICLDCFHLYCVTRLNDRQFVHDPQLGYTLPCPAGCE
>gnl|CDD|438290 cd16628, RING-HC_RBR_RNF14, RING finger, HC subclass, found in RING finger protein 14 (RNF14) and similar proteins. RNF14, also known as androgen receptor-associated protein 54 (ARA54), HFB30, or Triad2 protein, is an RBR-type E3 ubiquitin-protein ligase that is highly expressed in the testis and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3). Its differential localization may play an important role in testicular development and spermatogenesis in humans. RNF14 functions as a transcriptional regulator of mitochondrial and immune function in muscle. It is a ligand-dependent androgen receptor (AR) co-activator and may also may participate in enhancing cell cycle progression and cell proliferation via induction of cyclin D1. Moreover, RNF14 is crucial for colon cancer cell survival. It acts as a new enhancer of the Wnt-dependent transcriptional outputs that acts at the level of the T-cell factor/lymphoid enhancer factor (TCF/LEF)-beta-catenin complex. RNF14 contains an N-terminal RWD domain and a C-terminal RBR domain. The RBR domain was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination
FNSKIFTCNICFLDKLGSECMYFKDCGHVYCKECLKEYFEVQIRDGNVTSLNCPEPKCA
>gnl|CDD|438291 cd16629, RING-HC_RBR_RNF19, RING finger, HC subclass, found in the family of RING finger proteins RNF19A, RNF19B and similar proteins. The family includes RING finger protein RNF19A and RNF19B, both of which are transmembrane (TM) domain-containing RBR-type E3 ubiquitin-protein ligases. RNF19A, also known as double ring-finger protein (Dorfin) or p38, localizes to the ubiquitylated inclusions in Parkinson's disease (PD), dementia with Lewy bodies, multiple system atrophy, and amyotrophic lateral sclerosis (ALS). It interacts with Psmc3, a protein component of the 19S regulatory cap of the 26S proteasome, and further participates in the ubiquitin-proteasome system in acrosome biogenesis, spermatid head shaping, and development of the head-tail coupling apparatus and tail. It modulates the ubiquitination and degradation of calcium-sensing receptor (CaR), which may contribute to a general mechanism for CaR quality control during biosynthesis. Moreover, RNF19A can also ubiquitylate mutant superoxide dismutase 1 (SOD1), the causative gene of familial ALS. It may associate with endoplasmic reticulum-associated degradation (ERAD) pathway, which is related to the pathogenesis of neurodegenerative disorders, such as PD or Alzheimer's disease. RNF19B, also known as IBR domain-containing protein 3 or natural killer lytic-associated molecule (NKLAM), plays a role in controlling tumor dissemination and metastasis. It is involved in the cytolytic function of natural killer (NK) cells and cytotoxic T lymphocytes (CTLs). It interacts with ubiquitin conjugates UbcH7 and UbcH8, and ubiquitinates uridine kinase like-1 (URKL-1) protein, targeting it for degradation. Moreover, RNF19B is a novel component of macrophage phagosomes and plays a role in macrophage anti-bacterial activity. It functions as a novel modulator of macrophage inducible nitric oxide synthase (iNOS) expression. Both RNF19A and RNF19B contain an RBR domain followed by three TMs. The RBR domain was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination
LECPLCLDDLSPEFFPILLSCEHRSCRDCLRQYLTIEISESRVNISCPECSERFHP
>gnl|CDD|438292 cd16630, RING-HC_RBR_RNF216, RING finger, HC subclass, found in RING finger protein 216 (RNF216) and similar proteins. RNF216, also known as Triad domain-containing protein 3 (Triad3A), ubiquitin-conjugating enzyme 7-interacting protein 1, or zinc finger protein inhibiting NF-kappa-B (ZIN), is a RBR-type E3 ubiquitin-protein ligase that interacts with several components of Toll-like receptor (TLR) signaling and promotes their proteolytic degradation. It negatively regulates the RIG-I RNA sensing pathway through Lys48-linked, ubiquitin-mediated degradation of the tumor necrosis factor receptor-associated factor 3 (TRAF3) adapter following RNA virus infection. It also controls ubiquitination and proteasomal degradation of receptor-interacting protein 1 (RIP1), a serine/threonine protein kinase that is critically involved in tumor necrosis factor receptor-1 (TNF-R1)-induced NF-kappa B activation, following disruption of Hsp90 binding. Moreover, RNF216 is involved in inflammatory diseases through strongly inhibiting autophagy in macrophages. It interacts with and ubiquitinates BECN1, a key regulator in autophagy, thereby contributing to BECN1 degradation. It regulates synaptic strength by ubiquitination of Arc, resulting in its rapid proteasomal degradation. It is also a key negative regulator of sustained Killer cell Ig-like receptor (KIR) with two Ig-like domains and a long cytoplasmic domain 4 (2DL4)-mediated NF-kappaB signaling from internalized 2DL4, which functions by promoting ubiquitylation and degradation of endocytosed receptor from early endosomes. Furthermore, RNF216 interacts with human immunodeficiency virus type 1 (HIV-1) Virion infectivity factor (Vif) protein, which is essential for the productive infection of primary human CD4 T lymphocytes and macrophages. Mutations in RNF216 may result in Gordon Holmes syndrome, a condition defined by hypogonadotropic hypogonadism and cerebellar ataxia, as well as in autosomal recessive Huntington-like disorder. RNF216 contains a RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain use an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This family corresponds to the RING domain, a C3HC4-type RING-HC finger motif required for RBR-mediated ubiquitination
IECGCCFGDYPFEEMVQCPEGHLFCKECVRRYAEEAVGGQGWSELKCMSSSGCTAGFP
>gnl|CDD|438293 cd16631, mRING-HC-C4C4_RBR_HOIP, Modified RING finger, HC subclass (C4C4-type), found in HOIL-1-interacting protein (HOIP) and similar proteins. HOIP, also known as RING finger protein 31 (RNF31) or zinc in-between-RING-finger ubiquitin-associated domain protein, together with HOIL-1 and SHARPIN, forms the E3-ligase complex (also known as linear-ubiquitin-chain assembly complex LUBAC) that regulates NF-kappaB activity and apoptosis. It also interacts with the atypical mammalian orphan receptor DAX-1, trigger DAX-1 ubiquitination and stabilization, and participate in repressing steroidogenic gene expression. HOIP contains three Npl4 zinc fingers, a central ubiquitin-associated (UBA) domain responsible for the interaction with the N-terminal ubiquitin-like domain (UBL) of HOIL-1L, an RBR domain, and a C-terminal linear chain determining domain (LDD). The RBR domain was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C4C4-type RING finger motif whose overall folding is similar to that of the C3HC4-type RING-HC finger. It is required for RBR-mediated ubiquitination
QECPICFNSFPRNKMVSLTSCECKICPDCFKQYFTVVIKEKHIRDLVCPACGLP
>gnl|CDD|438294 cd16632, mRING-HC-C4C4_RBR_RNF144, Modified RING finger, HC subclass (C4C4-type), found in RNF144 proteins. This group includes RNF144A and RNF144B, both of which are transmembrane (TM) domain-containing RBR-type E3 ubiquitin-protein ligases. RNF144A, also known as UbcM4-interacting protein 4 (UIP4) or ubiquitin-conjugating enzyme 7-interacting protein 4, targets DNA-dependent protein kinase catalytic subunit (DNA-PKcs), and thus promote DNA damage-induced cell apoptosis. It is transcriptionally repressed by metastasis-associated protein 1 (MTA1) and inhibits MTA1-driven cancer cell migration and invasion. RNF144B, also known as PIR2, IBR domain-containing protein 2 (IBRDC2), or p53-inducible RING finger protein (p53RFP), induces p53-dependent but caspase-independent apoptosis. It interacts with E2 ubiquitin-conjugating enzymes UbcH7 and UbcH8, but not with UbcH5. It is involved in ubiquitination and degradation of p21, a p53 downstream protein promoting growth arrest and antagonizing apoptosis, suggesting a role in switching a cell from p53-mediated growth arrest to apoptosis. Moreover, RNF144B regulates the levels of Bax, a pro-apoptotic protein from the Bcl-2 family, and protects cells from unprompted Bax activation and cell death. It also regulates epithelial homeostasis by mediating degradation of p21WAF1 and p63. Both RNF144A and RNF144B contain an RBR domain followed by a potential single-TM domain. The RBR domain was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C4C4-type RING finger whose overall folding is similar to that of the C3HC4-type RING-HC finger. It is required for RBR-mediated ubiquitination
ITCKLCLEEVPLREMYTLQSCGCIFCLQCLKQYVEVLIREGNVSSITCPDAAC
>gnl|CDD|438295 cd16633, mRING-HC-C3HC3D_RBR_HOIL1, Modified RING finger, HC subclass (C3HC3D-type), found in heme-oxidized IRP2 ubiquitin ligase 1 (HOIL-1) and similar proteins. HOIL-1, also known as RBCK1, HOIL-1L, RanBP-type and C3HC4-type zinc finger-containing protein 1, HBV-associated factor 4, Hepatitis B virus X-associated protein 4, RING finger protein 54 (RNF54), ubiquitin-conjugating enzyme 7-interacting protein 3, or UbcM4-interacting protein 28 (UIP28), together with E3 ubiquitin-protein ligase RNF31 (also known as HOIP) and SHANK-associated RH domain interacting protein (SHARPIN), form the E3-ligase complex (also known as linear-ubiquitin-chain assembly complex LUBAC) that regulates NF-kappaB activity and apoptosis through conjugation of linear polyubiquitin chains to NF-kappaB essential modulator (also known as NEMO or IKBKG). HOIL-1 plays a crucial role in TNF-alpha-mediated NF-kappaB activation. It also functions as an ubiquitin-protein ligase E3 that interacts with not only PKCbeta, but also PKCzeta. It can recognize heme-oxidized IRP2 (iron regulatory protein2) and is thought to affect the turnover of oxidatively damaged proteins. HOIL-1 contains an N-terminal ubiqutin-like (UBL) domain and an Npl4 zinc-finger (NZF) domain, which regulate the interaction with the LUBAC subunit RNF31 and ubiquitin, respectively. The NZF domain belongs to the RanBP2-type zinc finger (zf-RanBP2) domain superfamily. In addition, HOIL-1 has an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a modified C3HC3D-type RING-HC finger required for RBR-mediated ubiquitination
LVPNQEPFECPICFDDVPPGEGVVLRECLHSFCRECLRGAIQNSEEAEVKCPFRDD
>gnl|CDD|438296 cd16634, mRING-HC-C3HC3D_Nrdp1, Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation protein-1 (Nrdp1) and similar proteins. Nrdp1 (referred to as FLRF in mice), also known as RING finger protein 41 (RNF41), is an E3 ubiquitin-protein ligase that plays a critical role in the regulation of cell growth and apoptosis, inflammation and production of reactive oxygen species (ROS), as well as in doxorubicin (DOX)-induced cardiac injury. It promotes the degradation of the epidermal growth factor receptor (EGFR/ErbB) family member, ErbB3, which is independent of growth factor stimulation. It also promotes M2 macrophage polarization by ubiquitinating and activating transcription factor CCAAT/enhancer-binding protein beta (C/EBPbeta) via Lys-63-linked ubiquitination. Moreover, Nrdp1 interacts with and modulates the activity of Parkin, a causative protein for early onset recessive juvenile parkinsonism (AR-JP). It also interacts with ubiquitin-specific protease 8 (USP8), which is involved in trafficking of various transmembrane proteins. Furthermore, Nrdp1 inhibits basal lysosomal degradation and enhances ectodomain shedding of JAK2-associated cytokine receptors. Its phosphorylation by the kinase Par-1b (also known as MARK2) is required for epithelial cell polarity. Nrdp1 contains an N-terminal modified C3HC3D-type RING-HC finger required for enhancing ErbB3 degradation, a B-box, a coiled-coil domain responsible for Nrdp1 oligomerization, and a C-terminal ErbB3-binding domain
ELICPICSGVLEEPLQAPHCEHAFCNACITEWLSRQQTCPVDR
>gnl|CDD|438297 cd16635, mRING-HC-C3HC3D_PHRF1, Modified RING finger, HC subclass (C3HC3D-type), found in PHD and RING finger domain-containing protein 1 (PHRF1) and similar proteins. PHRF1, also known as KIAA1542, or CTD-binding SR-like protein rA9, is a ubiquitin ligase which induces the ubiquitination of TGIF (TG-interacting factor) at lysine 130. It acts as a tumor suppressor that promotes the transforming growth factor (TGF)-beta cytostatic program through selective release of TGIF-driven promyelocytic leukemia protein (PML) inactivation. PHRF1 contains a plant homeodomain (PHD) finger and a modified C3HC3D-type RING-HC finger
DDESESCPICLNTFRDQAVGTPESCDHIFCLDCILEWSKNANTCPVDRIVF
>gnl|CDD|438298 cd16636, mRING-HC-C3HC3D_SCAF11, Modified RING finger, HC subclass (C3HC3D-type), found in SR-related and CTD-associated factor 11 (SCAF11) and similar proteins. SCAF11, also known as CTD-associated SR protein 11 (CASP11), renal carcinoma antigen NY-REN-40, SC35-interacting protein 1 (Sip1), Serine/arginine-rich splicing factor 2 (SRSF2)-interacting protein, or splicing regulatory protein 129 (SRrp129), is a novel arginine-serine-rich (RS) domain-containing protein essential for pre-mRNA splicing. It functions as an auxiliary splice factor interacting with the spliceosomal component SC35, promoting RNAPII elongation. In addition to SR proteins, such as SC35, ASF/SF2, SRp75, and SRp20, SCAF11 also associates with U1-70K and U2AF65, proteins associated with 5' and 3' splice sites, respectively. SCAF11 contains an N-terminal modified C3HC3D-type RING-HC finger, an internal serine-arginine rich domain (SR domain), and a C-terminal SRI domain
DRCPICLNCLLEQEVAFPENCSHVFCLTCILKWAETVTSCPIDRKPFQAVYK
>gnl|CDD|438299 cd16637, mRING-HC-C3HC3D_LNX1-like, Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, and similar proteins. The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4 or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for substrate-binding. LNX1/LNX2-like proteins contain a modified C3HC3D-type RING-HC finger and four PDZ domains. This model corresponds to the RING finger
DLTCHICLQPLVEPLDTPCGHTFCYKCLTNYLKIQQCCPLDR
>gnl|CDD|438300 cd16638, mRING-HC-C3HC3D_Roquin, Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1, Roquin-2, and similar proteins. The ROQUIN family includes Roquin-1, Roquin-2, and similar proteins, which localize to the cytoplasm and upon stress, are concentrated in stress granules. They may play essential roles in preventing T-cell-mediated autoimmune disease and in microRNA-mediated repression of inducible costimulator (Icos) mRNA. They function as E3 ubiquitin ligases consisting of an N-terminal modified C3HC3D-type RING-HC finger with a potential E3 activity, a highly conserved ROQ domain required for RNA binding and localization to stress granules, and a CCCH-type zinc finger involved in RNA recognition
FLSCPVCTNEFDGTQRKPISLGCGHTVCKTCLSKLHRKQCPFDQ
>gnl|CDD|438301 cd16639, RING-HC_TRAF2, RING finger, HC subclass, found in tumor necrosis factor (TNF) receptor-associated factor 2 (TRAF2) and similar proteins. TRAF2, also known as tumor necrosis factor type 2 receptor-associated protein 3, is an E3 ubiquitin-protein ligase that was identified as a 75 kDa tumor necrosis factor receptor (TNF-R2)-associated signaling protein. It interacts with members of the TNF receptor superfamily and connects the receptors to downstream signaling proteins. It also mediates K63-linked polyubiquitination of RIP1, a kinase pivotal in TNFalpha-induced NF-kappaB activation. Moreover, TRAF2 regulates peripheral CD8(+) T-cell and NKT-cell homeostasis by modulating sensitivity to IL-15. It also acts as an important biological suppressor of necroptosis. It inhibits TNF-related apoptosis inducing ligand (TRAIL)- and CD95L-induced apoptosis and necroptosis. TRAF2 contains an N-terminal domain with a typical C3HC4-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain
KYLCSDCRNILRRPFQAQCGHRYCSYCLKKILSSGPQKCAACI
>gnl|CDD|438302 cd16640, RING-HC_TRAF3, RING finger, HC subclass, found in tumor necrosis factor (TNF) receptor-associated factor 3 (TRAF3) and similar proteins. TRAF3, also known as CAP-1, CD40 receptor-associated factor 1 (CRAF1), CD40-binding protein (CD40BP), or LMP1-associated protein 1 (LAP1), is a member of the TRAF protein family, which mainly functions in the immune system, where it mediates signaling through tumor necrosis factor receptors (TNFRs) and interleukin-1/Toll-like receptors (IL-1/TLRs). It also plays a unique cell type-specific and critical role in the restraint of B-cell homeostatic survival, a role with important implications for both B-cell differentiation and the pathogenesis of B-cell malignancies. TRAF3 differentially regulates differentiation of specific T cell subsets. It is required for iNKT cell development, restrains Treg cell development in the thymus, and plays an essential role in the homeostasis of central memory CD8+ T cells. TRAF3 contains an N-terminal domain with a typical C3HC4-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain, and a conserved TRAF-C domain
YKCEKCRLVLCNPKQTECGHRFCESCMNALLSSSNPQCPACE
>gnl|CDD|438303 cd16641, mRING-HC-C3HC3D_TRAF4, Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 4 (TRAF4) and similar proteins. TRAF4, also known as cysteine-rich domain associated with RING and Traf domains protein 1, metastatic lymph node gene 62 protein (MLN 62), or RING finger protein 83 (RNF83), is a member of the TRAF protein family, which mainly function in the immune system, where they mediate signaling through tumor necrosis factor receptors (TNFRs) and interleukin-1/Toll-like receptors (IL-1/TLRs). It also plays a critical role in nervous system, as well as in carcinogenesis. TRAF4 promotes the growth and invasion of colon cancer through the Wnt/beta-catenin pathway. It contributes to the TNFalpha-induced activation of the 70 kDa ribosomal protein S6 kinase (p70s6k) signaling pathway, and activation of transforming growth factor beta (TGF-beta)-induced SMAD-dependent signaling and non-SMAD signaling in breast cancer. It also enhances osteosarcoma cell proliferation and invasion by the Akt signaling pathway. Moreover, TRAF4 is a novel phosphoinositide-binding protein modulating tight junctions and favoring cell migration. TRAF4 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain
RLLCPLCRLPMREPVQISTCGHRFCDTCLQEFLSEGVFKCPEDQL
>gnl|CDD|438304 cd16642, mRING-HC-C3HC3D_TRAF5, Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 5 (TRAF5) and similar proteins. TRAF5, also known as RING finger protein 84 (RNF84), is an important signal transducer for a wide range of TNF receptor superfamily members, including tumor necrosis factor receptor 1 (TNFR1), TNFR2, CD40, and other lymphocyte costimulatory receptors, RANK/TRANCE-R, ectodysplasin-A Receptor (EDAR), lymphotoxin-beta receptor (LT-betaR), latent membrane protein 1 (LMP1), and IRE1. It functions as an activator of NF-kappaB, MAPK, and JNK, and is involved in both RANKL- and TNFalpha-induced osteoclastogenesis. It mediates CD40 signaling by associating with the cytoplasmic tail of CD40. It also negatively regulates Toll-like receptor (TLR) signaling and functions as a negative regulator of the interleukin 6 (IL-6) receptor signaling pathway that limits the differentiation of inflammatory CD4(+) T cells. TRAF5 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain
LEDRYKCATCHFVLHNPHQTGCGHRFCQHCILSLLELNTTPICPIDKETIKSDEVF
>gnl|CDD|438305 cd16643, mRING-HC-C3HC3D_TRAF6, Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 6 (TRAF6) and similar proteins. TRAF6, also known as interleukin-1 signal transducer or RING finger protein 85 (RNF85), is a cytoplasmic adapter protein that mediates signals induced by the tumor necrosis factor receptor (TNFR) superfamily and Toll-like receptor (TLR)/interleukin-1 receptor (IL-1R) family. It functions as a mediator involved in the activation of mitogen-activated protein kinase (MAPK), phosphoinositide 3-kinase (PI3K), and interferon regulatory factor pathways, as well as in IL-1R-mediated activation of NF-kappaB. TRAF6 is also an oncogene that plays a vital role in K-RAS-mediated oncogenesis. TRAF6 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain
KYECPICLMALREPVQTPCGHRFCKACILKSIREAGHKCPVDNEPLLENQLFPDNFAK
>gnl|CDD|438306 cd16644, mRING-HC-C3HC3D_TRAF7, Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 7 (TRAF7) and similar proteins. TRAF7, also known as RING finger and WD repeat-containing protein 1 or RING finger protein 119 (RNF119), is an E3 ubiquitin-protein ligase involved in signal transduction pathways that lead either to activation or repression of NF-kappaB transcription factor by promoting K29-linked ubiquitination of several cellular targets, including the NF-kappaB essential modulator (NEMO) and the p65 subunit of NF-kappaB transcription factor. It is also involved in K29-linked polyubiquitination that has been implicated in lysosomal degradation of proteins. Moreover, TRAF7 is required for K48-linked ubiquitination of p53, a key tumor suppressor and a master regulator of various signaling pathways, such as those related to apoptosis, cell cycle and DNA repair. It is also required for tumor necrosis factor alpha (TNFalpha)-induced Jun N-terminal kinase activation and promotes cell death by regulating polyubiquitination and lysosomal degradation of c-FLIP protein. Furthermore, TRAF7 functions as small ubiquitin-like modifier (SUMO) E3 ligase involved in other post-translational modification, such as sumoylation. It binds to and stimulates sumoylation of the proto-oncogene product c-Myb, a transcription factor regulating proliferation and differentiation of hematopoietic cells. It potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis. Meanwhile, TRAF7 mediates MyoD1 regulation of the pathway and cell-cycle progression in myoblasts. It also plays a role in Toll-like receptors (TLR) signaling. TRAF7 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and an adjacent zinc finger, and a unique C-terminal domain that comprises a coiled coil domain and seven WD40 repeats
PPSVKLYCPLCQRVFKDPVITSCGHTFCRRCALTAPGEKCPVDNMKL
>gnl|CDD|438307 cd16645, mRING-HC-C3HC3D_TRIM23_C-IX, Modified RING finger, HC subclass (C3HC3D-type), found in tripartite motif-containing protein 23 (TRIM23) and similar proteins. TRIM23, also known as ADP-ribosylation factor domain-containing protein 1, GTP-binding protein ARD-1, or RING finger protein 46 (RNF46), is an E3 ubiquitin-protein ligase belonging to the C-IX subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a modified C3HC3D-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as C-terminal ADP ribosylation factor (ARF) domains. TRIM23 is involved in nuclear factor (NF)-kappaB activation. It mediates atypical lysine 27 (K27)-linked polyubiquitin conjugation to NF-kappaB essential modulator NEMO, also known as IKKgamma, which plays an important role in the NF-kappaB pathway, and this conjugation is essential for TLR3- and RIG-I/MDA5-mediated antiviral innate and inflammatory responses. It also regulates adipocyte differentiation via stabilization of the adipogenic activator peroxisome proliferator-activated receptor gamma (PPARgamma) through atypical ubiquitin conjugation to PPARgamma. Moreover, TRIM23 interacts with and polyubiquitinates yellow fever virus (YFV) NS5 to promote its binding to STAT2 and trigger type I interferon (IFN-I) signaling inhibition
VLECGVCEDVFSLQGDKVPRLLLCGHTVCHDCLTRLPLHGRAVRCPFDRQ
>gnl|CDD|438308 cd16646, mRING-HC-C2H2C4_MDM2-like, Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2, protein MDM4 and similar proteins. MDM2 (also known as HDM2) and MDM4 (also known as MDMX or HDMX) are the primary p53 tumor suppressor negative regulators. They have non-redundant roles in the regulation of p53. MDM2 mainly functions to control p53 stability, while MDM4 controls p53 transcriptional activity. Both MDM2 and MDM4 contain an N-terminal p53-binding domain, a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region, and a C-terminal modified C2H2C4-type RING-HC finger. Mdm2 can form homo-oligomers through its RING domain and displays E3 ubiquitin ligase activity that catalyzes the attachment of ubiquitin to p53 as an essential step in the regulation of its levels in cells. Despite its RING domain and structural similarity with MDM2, MDM4 does not homo-oligomerize and lacks ubiquitin-ligase function, but inhibits the transcriptional activity of p53. In addition, both their RING domains are responsible for the hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. Moreover, MDM2 and MDM4 can be phosphorylated and destabilized in response to DNA damage stress. In response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through the interaction with ribosomal proteins L5, L11, and L23. However, MDM4 is not bound to ribosomal proteins, suggesting its different response to regulation by small basic proteins such as ribosomal proteins and ARF
DLCVICLSRPRTAAIVHGKTGHQVACYTCAKKLKRRGKPCPVCRRPIQNVIK
>gnl|CDD|438309 cd16647, mRING-HC-C3HC5_NEU1, Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, NEURL1B, and similar proteins. This subfamily includes Drosophila neuralized (D-neu) protein, and its two mammalian homologs, NEURL1A and NEURL1B. D-neu is a regulator of the developmentally important Notch signaling pathway. NEURL1A, also known as NEURL1, NEU, neuralized 1, or RING finger protein 67 (RNF67), is a mammalian homolog of D-neu. It functions as an E3 ubiquitin-protein ligase that directly interacts with and monoubiquitinates cytoplasmic polyadenylation element-binding protein 3 (CPEB3), an RNA binding protein and a translational regulator of local protein synthesis, which facilitates hippocampal plasticity and hippocampal-dependent memory storage. It also acts as a potential tumor suppressor that causes apoptosis and downregulates Notch target genes in medulloblastoma. NEURL1B, also known as neuralized-2 (NEUR2) or neuralized-like protein 3, is another mammalian homolog of D-neu protein. It functions as an E3 ubiquitin-protein ligase that interacts with and ubiquitinates Delta. Thus, it plays a role in the endocytic pathways for Notch signaling by working cooperatively with another E3 ligase, Mind bomb-1 (Mib1), in Delta endocytosis to hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)-positive vesicles. Members of this subfamily contain two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain
GSECVICYERPVDTVLYRCGHMCMCYDCALQLKRRGGSCPICRAPIKDVIKIY
>gnl|CDD|438310 cd16648, mRING-HC-C3HC5_MAPL, Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase (MAPL) and similar proteins. MAPL, also known as MULAN, mitochondrial ubiquitin ligase activator of NFKB 1, E3 SUMO-protein ligase MUL1, E3 ubiquitin-protein ligase MUL1, growth inhibition and death E3 ligase (GIDE), putative NF-kappa-B-activating protein 266, or RING finger protein 218 (RNF218), is a multifunctional mitochondrial outer membrane protein involved in several processes specific to metazoan (multicellular animal) cells, such as NF-kappaB activation, innate immunity and antiviral signaling, suppression of PINK1/parkin defects, mitophagy in skeletal muscle, and caspase-dependent apoptosis. MAPL contains a unique BAM (beside a membrane)/GIDE (growth inhibition death E3 ligase) domain and a C-terminal modified cytosolic C3HC5-type RING-HC finger which is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain
DNACVICLSNPRSCVFLECGHVCSCIECYEALPSPKKCPICRSFIKRVVPLY
>gnl|CDD|438311 cd16649, mRING-HC-C3HC5_CGRF1-like, Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 (CGRRF1), RNF156 (MGRN1), RNF157 and similar proteins. This subfamily corresponds to a group of RING finger proteins containing a modified C3HC5-type RING-HC finger, which is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain. Cell growth regulator with RING finger domain protein 1 (CGRRF1), also known as cell growth regulatory gene 19 protein (CGR19) or RING finger protein 197 (RNF197), functions as a novel biomarker to monitor endometrial sensitivity and response to insulin-sensitizing drugs, such as metformin, in the context of obesity. RNF26 is an E3 ubiquitin ligase that temporally regulates virus-triggered type I interferon induction by increasing the stability of Mediator of IRF3 activation, MITA, also known as STING, through K11-linked polyubiquitination after viral infection and promoting degradation of IRF3, another important component required for virus-triggered interferon induction. Mahogunin ring finger-1 (MGRN1), also known as RING finger protein 156 (RNF156), is a cytosolic E3 ubiquitin-protein ligase that inhibits signaling through the G protein-coupled melanocortin receptors-1 (MC1R), -2 (MC2R) and -4 (MC4R) via ubiquitylation-dependent and -independent processes. It suppresses chaperone-associated misfolded protein aggregation and toxicity. RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in the brain. It is a homolog of the E3 ligase MGRN1. In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis
GLCVVCLENPASVLLLPCRHLCLCEVCAKGLRGKTCPICR
>gnl|CDD|438312 cd16650, SP-RING_PIAS-like, SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases. The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. PIAS proteins modulate the activity of several transcription factors and act as E3 ubiquitin ligases in the sumoylation pathway. There are four members: PIAS1, PIAS2 (also known as PIASx), PIAS3, and PIAS4 (also known as PIASy). PIAS proteins were initially identified as inhibitors of activated STAT only, but are now known to interact with and modulate several other proteins, including androgen receptor (AR), tumor suppressor p53, and the transforming growth factor-beta (TGF-beta) signaling protein SMAD. They interact with STATs in a cytokine-dependent manner. PIAS proteins have SUMO E3-ligase activity and interaction of PIAS proteins with transcription factors often results in sumoylation of that protein. Zmiz1 (Zimp10) and its homolog Zmiz2 (Zimp7) were initially identified in humans as androgen receptor (AR) interacting proteins that function as transcriptional co-activators. They interact with BRG1, the catalytic subunit of the SWI-SNF remodeling complex. They also associate with other hormone nuclear receptors and transcription factors such as p53 and Smad3/Smad4, and regulate transcription of specific target genes by altering their chromatin structure. SIZ1 proteins from plants and fungi are also founding members of this family. SIZ1-mediated conjugation of SUMO1 and SUMO2 to other intracellular proteins is essential in Arabidopsis. Yeast SIZ proteins are SUMO E3 ligases involved in a novel pathway of chromosome maintenance. They enhance SUMO modification to many substrates in vivo, but also exhibit unique substrate specificity. PIAS proteins contain a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, which is essential for SUMO ligase activity. The SP-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers
SLRCPLSLKRIKTPARGKHCKHLQCFDLDSYLEFNKRKPTWKCPICDK
>gnl|CDD|438313 cd16651, SPL-RING_NSE2, SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins. NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity
LKCPITQQLMVDPVRNKKCGHTYEKAAILQYLQSRKKKAKCPVAGCRNTVSKSDLVPDPELKRRIER
>gnl|CDD|438314 cd16652, dRING_Rmd5p-like, Degenerated RING (dRING) finger found in Saccharomyces cerevisiae required for meiotic nuclear division protein 5 (Rmd5p) and similar proteins. Rmd5p, also known as glucose-induced degradation protein 2 (Gid2) or sporulation protein RMD5, is an E3 ubiquitin ligase containing a Lissencephaly type-1-like homology motif (LisH), a C-terminal to LisH motif (CTLH) domain, and a degenerated RING finger that is characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. It forms the heterodimeric E3 ligase unit of the glucose induced degradation deficient (GID) complex with Gid9 (also known as Fyv10), which has a degenerated RING finger as well. The GID complex triggers polyubiquitylation and subsequent proteasomal degradation of the gluconeogenic enzymes fructose-1, 6-bisphosphate by fructose-1, 6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase (PEPCK), and cytoplasmic malate dehydrogenase (c-MDH). Moreover, Rmd5p can form the GID complex with the other six Gid proteins, including Gid1/Vid30, Gid4/Vid24, Gid5/Vid28, Gid7, Gid8, and Gid9/Fyv10. The GID complex in which the seven Gid proteins reside functions as a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism
FACPVSREQSTEENPPMRLPCGHVISKDSLKKLSKNNGNKFKCPYCPVE
>gnl|CDD|438315 cd16653, RING-like_Rtf2, RING-like Rtf2 domain, C2HC2-type, found in the replication termination factor 2 (Rtf2) protein family. The Rtf2 protein family includes a group of conserved proteins found in eukaryotes ranging from fission yeast to humans. The defining member of the family is Schizosaccharomyces pombe Rtf2 (SpRtf2), which is a proliferating cell nuclear antigen-interacting protein that functions as a key requirement for efficient replication termination at the site-specific replication barrier RTS1. It promotes termination at RTS1 by preventing replication restart. SpRtf2 contains a RING-like Rtf2 domain that is characterized by a C2HC2 motif similar to C3HC4 RING-HC finger motif known to bind two Zn2+ ions and mediate protein-protein interactions. The C2HC2 motif lacks three of the seven conserved cysteines of the C3HC4 motif, and forms only one functional Zn2+ ion-binding site. The RING-like Rtf2 domain in fission yeast is required to stabilize a paused DNA replication fork during imprinting at the mating type locus, possibly by facilitating sumoylation of PCNA. The family also includes Arabidopsis RTF2 (AtRTF2), an essential nuclear protein required for both normal embryo development and for proper expression of the GFP reporter gene. It plays a critical role in splicing the GFP pre-mRNA, and may also have a more transient regulatory role during the spliceosome cycle. The biological function of Rtf2 homologs found in eumetazoa remains unclear. They contain a variant C2HC2 motif where the middle conserved histidine has been replaced by cysteine
FICPITGLEMNGKYKFVYLWPCGCVFSERALKELKGSKKCPVCGKPF
>gnl|CDD|438316 cd16654, RING-Ubox_CHIP, U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins. CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase
VPDYLCCKISFELMRDPVITPSGITYERKDIEEHLQRVGHFDPITREPLTQDQLIPNLALKEAIEAFLEE
N
>gnl|CDD|438317 cd16655, RING-Ubox_WDSUB1-like, U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins. WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis
PDEFLCPITQELMRDPVVAADGHTYERSAIEEWLETHNTSPMTRLPLSSTDLVPN
>gnl|CDD|438318 cd16656, RING-Ubox_PRP19, U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins. Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment
MVCAISGEVPEEPVVSPKSGHVFEKRLIEKYIAENGTDPVTGEPLTEEDLIEIK
>gnl|CDD|438319 cd16657, RING-Ubox_UBE4A, U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and similar proteins. This subfamily includes yeast ubiquitin fusion degradation protein 2 (UFD2p) and its mammalian homolog, UBE4A. Yeast UFD2p, also known as ubiquitin conjugation factor E4 or UB fusion protein 2, is a polyubiquitin chain conjugation factor (E4) in the ubiquitin fusion degradation (UFD) pathway which catalyzes elongation of the ubiquitin chain through Lys48 linkage. It binds to substrates conjugated with one to three ubiquitin molecules and catalyzes the addition of further ubiquitin moieties in the presence of ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2) and ubiquitin ligase (E3), yielding multiubiquitylated substrates that are targets for the 26S proteasome. UFD2p is implicated in cell survival under stress conditions and is essential for homoeostasis of unsaturated fatty acids. It interacts with UBL-UBA proteins Rad23 and Dsk2, which are involved in the endoplasmic reticulum-associated degradation, ubiquitin fusion degradation, and OLE-1 gene induction pathways. UBE4A is a U-box-type ubiquitin-protein ligase that is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. It may have a specific role in different biochemical processes other than ubiquitination, including growth or differentiation. Members of this family contain an N-terminal ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus
DEFLDPIMYTLMKDPVILPSSKVTVDRSTIKRHLLSDQTDPFNRSPLTLDMVIPNEELKQKIEEFLAEKK
>gnl|CDD|438320 cd16658, RING-Ubox_UBE4B, U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and similar proteins. UBE4B, also known as UFD2a, is a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain. It is a mammalian homolog of yeast UFD2 ubiquitination factor and it participates in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. It is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. UBE4B has contradictory functions upon tumorigenesis as an oncogene or tumor suppressor in different types of cancers. It is essential for Hdm2 (also known as Mdm2)-mediated p53 degradation. It mediates p53 polyubiquitination and degradation, as well as inhibits p53-dependent transactivation and apoptosis, and thus plays an important role in regulating phosphorylated p53 following DNA damage. UBE4B is also associated with other pathways independent of the p53 family, such as polyglutamine aggregation and Wallerian degeneration, both of which are critical in neurodegenerative diseases. Moreover, UBE4B acts as a regulator of epidermal growth factor receptor (EGFR) degradation. It is recruited to endosomes in response to EGFR activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0, and then regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. UBE4B contains a ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus
LGDAPDEFLDPLMDTLMTDPVILPSGTIMDRSIILRHLLNSQTDPFNRQPLTEDMLEPVPELKERIQAWI
REKQ
>gnl|CDD|438321 cd16659, RING-Ubox_Emp, U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and similar proteins. Emp, also known as cell proliferation-inducing gene 5 protein or macrophage erythroblast attacher (MAEA), is a key protein which functions in normal differentiation of erythroid cells and macrophages. It is a potential biomarker for hematopoietic evaluation of Hematopoietic stem cell transplantation (HSCT) patients. Emp was initially identified as a heparin-binding protein involved in the association of erythroblasts with macrophages. It promotes erythroid proliferation and maturation. It also plays an important role in erythroblastic island formation. Absence of Emp leads to failure of erythroblast nuclear extrusion. It is required in definitive erythropoiesis and plays a cell intrinsic role in the erythroid lineage. Emp contains a Lissencephaly type-1-like homology (LisH) motif, a C-terminal to LisH (CTLH) domain, and a RING-like U-box domain at the C-terminus
SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMAEKNDGKVVCPRTGESF
>gnl|CDD|438322 cd16660, RING-Ubox_RNF37, U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37). RNF37, also known as KIAA0860, U-box domain-containing protein 5 (UBOX5), UbcM4-interacting protein 5 (UIP5), or ubiquitin-conjugating enzyme 7-interacting protein 5, is an E3 ubiquitin-protein ligase found exclusively in the nucleus as part of a nuclear dot-like structure. It interacts with the molecular chaperone VCP/p97 protein. RNF37 contains a U-box domain followed by a potential nuclear location signal (NLS), and a C-terminal C3HC4-type RING-HC finger. The U-box domain is a modified RING finger domain that lacks the hallmark metal-chelating cysteines and histidines of the latter, but is likely to adopt a RING finger-like conformation. The presence of the U-box, but not of the RING finger, is required for the E3 activity. The U-box domain can directly interact with several E2 enzymes, including UbcM2, UbcM3, UbcM4, UbcH5, and UbcH8, suggesting a similar function as the RING finger in the ubiquitination pathway. This model corresponds to the U-box domain
PEEFLDPITCELMTLPVLLPSGKVVDQSTLEKYIKEEATWGRLPSDPFTGVPF
>gnl|CDD|438323 cd16661, RING-Ubox1_NOSIP, U-box domain 1, a modified RING finger, found in nitric oxide synthase-interacting protein (NOSIP) and similar proteins. NOSIP, also known as endothelial NO synthase (eNOS)-interacting protein, p33RUL, is an E3 ubiquitin-protein ligase implicated in the control of airway and vascular diameter, mucosal secretion, NO synthesis in ciliated epithelium, and, therefore, of mucociliary and bronchial function. The loss of NOSIP may cause holoprosencephaly and facial anomalies, including cleft lip/palate, cyclopia, and facial midline clefting. NOSIP interacts with neuronal nitric oxide synthase (nNOS) and eNOS by inhibiting the nitric oxide (NO) production. It acts as a novel type of modulator that promotes translocation of eNOS from the plasma membrane to intracellular sites, thereby uncoupling eNOS from plasma membrane caveolae and inhibiting NO synthesis. NOSIP also interacts with protein phosphatase PP2A and mediates the monoubiquitination of the PP2A catalytic subunit. Thus, it is a critical modulator of brain and craniofacial development in mice and a candidate gene for holoprosencephaly in humans. Moreover, NOSIP associates with the erythropoietin (Epo) receptor (EpoR), mediates ubiquitination of EpoR, and plays an essential role in erythropoietin-induced proliferation. NOSIP contains an atypical N-terminal RING-like U-box domain that is split into two parts by an interjacent stretch of 104 amino acid residues, as well as a C-terminal RING-like U-box domain. This model corresponds to the first U-box domain
FDCCCLTLQPCRDPVVTPDGYLYDKEAILEYILHQKKECPMSGKPL
>gnl|CDD|438324 cd16662, RING-Ubox2_NOSIP, U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein (NOSIP) and similar proteins. NOSIP, also known as endothelial NO synthase (eNOS)-interacting protein, p33RUL, is an E3 ubiquitin-protein ligase implicated in the control of airway and vascular diameter, mucosal secretion, NO synthesis in ciliated epithelium, and, therefore, of mucociliary and bronchial function. The loss of NOSIP may cause holoprosencephaly and facial anomalies including cleft lip/palate, cyclopia and facial midline clefting. NOSIP interacts with neuronal nitric oxide synthase (nNOS) and eNOS by inhibiting nitric oxide (NO) production. It acts as a novel type of modulator that promotes translocation of eNOS from the plasma membrane to intracellular sites, thereby uncoupling eNOS from plasma membrane caveolae and inhibiting NO synthesis. NOSIP also interacts with protein phosphatase PP2A and mediates the monoubiquitination of the PP2A catalytic subunit. Thus, it is a critical modulator of brain and craniofacial development in mice and a candidate gene for holoprosencephaly in humans. Moreover, NOSIP associates with the erythropoietin (Epo) receptor (EpoR), mediates ubiquitination of EpoR, and plays an essential role in erythropoietin-induced proliferation. NOSIP contains an atypical N-terminal RING-like U-box domain that is split into two parts by an interjacent stretch of 104 amino acid residues, as well as a C-terminal RING-like U-box domain. This model corresponds to the second U-box domain
RYMCAVTKDVLTNSVPCAVLRPSGDVVTMECVEKLIKKDMIDPVTGKKLKEKDIIPLQRGGTGFAASN
>gnl|CDD|438325 cd16663, RING-Ubox_PPIL2, U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2) and similar proteins. PPIL2 (EC 5.2.1.8), also known as PPIase, CYC4, cyclophilin-60 (Cyp60), cyclophilin-like protein Cyp-60, or Rotamase PPIL2, is a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c and regulates gene expression. PPIL2 belongs to the cyclophilin family of peptidylprolyl isomerases and catalyzes cis-trans isomerization of proline-peptide bonds, which is often a rate-limiting step in protein folding. It positively regulates beta-site amyloid precursor protein cleaving enzyme (BACE1) expression and beta-secretase activity. Moreover, PPIL2 plays an important role in the translocation of CD147 to the cell surface, and thus may present a novel target for therapeutic interventions in diseases where CD147 functions as a pathogenic factor in cancer, human immunodeficiency virus infection, or rheumatoid arthritis. PPIL2 contains an N-terminal RING-like U-box domain and a C-terminal cyclophilin (Cyp)-like chaperone domain
PFDCCALSLQPFENPVCTPDGIVFDLLNIVPYLKKYGKNPVTGEPLEAKDLIKLNFHKNAEGEYHCPVTF
KVF
>gnl|CDD|438326 cd16664, RING-Ubox_PUB, U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins. The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain
PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL
>gnl|CDD|438327 cd16665, RING-H2_RNF13-like, RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), and similar proteins. This subfamily includes RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), Zinc/RING finger protein 4 (ZNRF4), and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane domain (TM), and a C-terminal C3H2C3-type RING-H2 finger followed by a putative PEST sequence. RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that functions in the regulation of cancer development, muscle cell growth, and neuronal development. Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in the ubiquitination of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR). It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA, also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. ZNRF4, also known as RING finger protein 204 (RNF204), or Nixin, is an endoplasmic reticulum (ER) membrane-anchored ubiquitin ligase that physically interacts with the ER-localized chaperone calnexin in a glycosylation-independent manner, inducing calnexin ubiquitination, and p97-dependent degradation. The murine protein sperizin (spermatid-specific ring zinc finger) is a homolog of human ZNRF4. It is specifically expressed in Haploid germ cells and is involved in spermatogenesis
DVCAICLDDYEEGDKLRILPCSHAYHCKCIDPWLTKNKRTCPVCKR
>gnl|CDD|438328 cd16666, RING-H2_RNF43-like, RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins. RNF43 and ZNRF3 (also known as RNF203) are transmembrane E3 ubiquitin-protein ligases that belong to the PA-TM-RING ubiquitin ligase family, characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger followed by a long C-terminal region. Both RNF43 and RNF203 function as tumor suppressors involved in the regulation of Wnt/beta-catenin signaling. They negatively regulate Wnt signaling by interacting with complexes of frizzled (FZD) receptors and low-density lipoprotein receptor-related protein (LRP) 5/6, which leads to ubiquitination of FZD and endocytosis of the Wnt receptor. Dishevelled (DVL), a positive Wnt regulator, is required for ZNRF3/RNF43-mediated ubiquitination and degradation of FZD. They also associate with R-spondin 1 (RSPO1). This interaction may block FZD ubiquitination and enhances Wnt signaling
VCAICLEEYEEGQELRVLPCQHEFHRKCVDPWLLQNHTCPLCLFN
>gnl|CDD|438329 cd16667, RING-H2_RNF126-like, RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins. This subfamily includes RING finger proteins RNF126, RNF115, and similar proteins. RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation; this inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a cofactor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. RNF115 and RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. Both of them contain an N-terminal BCA2 Zinc-finger domain (BZF), AKT-phosphorylation sites, and a C-terminal C3H2C3-type RING-H2 finger
ECAVCKEDFEVGEEVRQLPCKHLFHPDCIVPWLELHNSCPVCR
>gnl|CDD|438330 cd16668, RING-H2_RNF130-like, RING finger, H2 subclass, found in RING finger proteins, RNF130, RNF149, RNF150 and similar proteins. This subfamily includes RING finger proteins, RNF130, RNF149 and RNF150, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF130, also known as Goliath homolog (H-Goliath), is a paralog of RNF128. It is a transmembrane E3 ubiquitin-protein ligase expressed in leukocytes. It has a self-ubiquitination property and controls the development of T cell clonal anergy by ubiquitination. RNF133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase that may play a role in sperm maturation through an ER-associated degradation (ERAD) pathway. RNF149, also known as DNA polymerase-transactivated protein 2, is an E3 ubiquitin-protein ligase that induces the ubiquitination of wild-type v-Raf murine sarcoma viral oncogene homolog B1 (BRAF) and promotes its proteasome-dependent degradation. RNF150 polymorphisms may be associated with chronic obstructive pulmonary disease (COPD) risk in the Chinese population. This subfamily also includes Drosophila melanogaster protein goliath (d-goliath), also known as protein g1, which is one of the founding members of the group. It was originally identified as a transcription factor involved in the embryo mesoderm formation
CCAVCIEPYKPSDVIRILPCKHIFHKSCVDPWLLEHRTCPMCKLDI
>gnl|CDD|438331 cd16669, RING-H2_RNF181, RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins. RNF181, also known as HSPC238, is a platelet E3 ubiquitin-protein ligase containing a C3H2C3-type RING-H2 finger. It interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3, suggesting a role for RNF181-mediated ubiquitination in integrin and platelet signaling. It also suppresses the tumorigenesis of hepatocellular carcinoma (HCC) through the inhibition of extracellular signal-regulated kinase/mitogen-activated protein kinase (ERK/MAPK) signaling in the liver
KCPICLLEFEEGETVKQLPCKHSFHSDCILPWLGKTNSCPLCRHEL
>gnl|CDD|438332 cd16670, RING-H2_RNF215, RING finger, H2 subclass, found in RING finger protein 215 (RNF215) and similar proteins. This family includes uncharacterized protein RNF215 and similar proteins. Although its biological function remains unclear, RNF215 shares high sequence similarity with PA-TM-RING ubiquitin ligases, which have been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger
ESCAVCLDQFYKNQCLRVLPCLHEFHRDCVDPWLLLQQTCPLCKRNILGN
>gnl|CDD|438333 cd16671, RING-H2_DTX1_4, RING finger, H2 subclass, found in E3 ubiquitin-protein ligase deltex1 (DTX1), deltex4 (DTX4), and similar proteins. DTX1 functions as a Notch downstream transcription regulator that mediates a Notch signal to block differentiation of neural progenitor cells. It interacts with the transcription coactivator p300 and inhibits transcription activation mediated by the neural specific transcription factor MASH1. It is also a transcription target of nuclear factor of activated T cells (NFAT) and participates in T cell anergy and Foxp3 protein level maintenance in vivo. Moreover, DTX1 appears to promote B-cell development at the expense of T-cell development. It also promotes protein kinase C theta degradation and sustains Casitas B-lineage lymphoma expression. DTX4, also known as RING finger protein 155, shares the highest degree of sequence similarity with DTX1 and likely interacts with the intracellular domain of Notch as well. Both DTX1 and DTX4 contain two Notch-binding WWE domains at the N-terminus that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a C3H2C3-type RING-H2 finger at the C-terminus. They also harbor two nuclear localization signals
DEDCTICMERLVTPSGYEGVLSHKGVKPELVGKLSRCGHMYHLLCLVAMYNNGNKDGSLQCPTCKAIYG
>gnl|CDD|438334 cd16672, RING-H2_DTX2, RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar proteins. DTX2, also known as RING finger protein 58, together with DTX1 and DTX4, forms a family of related proteins that are the mammalian homologs of Drosophila Deltex, a known regulator of Notch signals. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. DTX2 contains two Notch-binding WWE domains at the N-terminus that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a C3H2C3-type RING-H2 finger at the C-terminus. It also harbors two nuclear localization signals
DCIICMEKLSCASGYSDVSESKTIQPSAVGKLTKCGHTFHLLCMLAMYNNGNKDGSLQCPSCKTIYGEKT
GT
>gnl|CDD|438335 cd16673, RING-H2_RNF6, RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6 and similar proteins. RNF6 is an androgen receptor (AR)-associated protein that induces AR ubiquitination and promotes AR transcriptional activity. RNF6-induced ubiquitination may regulate AR transcriptional activity and specificity by modulating cofactor recruitment. RNF6 is overexpressed in hormone-refractory human prostate cancer tissues and required for prostate cancer cell growth under androgen-depleted conditions. Moreover, RNF6 regulates local serine/threonine kinase LIM kinase 1 (LIMK1) levels in axonal growth cones. RNF6-induced LIMK1 polyubiquitination is mediated via K48 of ubiquitin and leads to proteasomal degradation of the kinase. RNF6 also binds and upregulates the Inha promoter, and functions as a transcription regulatory protein in the mouse sertoli cell. RNF6 also acts as a potential tumor suppressor gene involved in the pathogenesis of esophageal squamous cell carcinoma (ESCC). RNF6 contains an N-terminal coiled-coil domain, a Lys-X-X-Leu/Ile-X-X-Leu/Ile (KIL) motif, and a C-terminal C3H2C3-type RING-H2 finger which is responsible for its ubiquitin ligase activity. The KIL motif is present in a subset of RING-H2 proteins from organisms as evolutionarily diverse as human, mouse, chicken, Drosophila, Caenorhabditis elegans, and Arabidopsis thaliana
KTCSVCINEYATGNKLRRLPCAHEFHIHCIDRWLSENSTCPICRQPVLGSNN
>gnl|CDD|438336 cd16674, RING-H2_RNF12, RING finger, H2 subclass, found in RING finger protein 12 (RNF12) and similar proteins. RNF12, also known as LIM domain-interacting RING finger protein or RING finger LIM domain-binding protein (R-LIM), is an E3 ubiquitin-protein ligase encoded by gene RLIM that is crucial for normal embryonic development in some species and for normal X inactivation in mice. It thus functions as a major sex-specific epigenetic regulator of female mouse nurturing tissues. RNF12 is widely expressed during embryogenesis, and mainly localizes to the cell nucleus, where it regulates the levels of many proteins, including CLIM, LMO, HDAC2, TRF1, SMAD7, and REX1, by proteasomal degradation. Its functional activity is regulated by phosphorylation-dependent nucleocytoplasmic shuttling. It is negatively regulated by pluripotency factors in embryonic stem cells. p53 represses its transcription through Sp1. RNF12 is the primary factor responsible for X chromosome inactivation (XCI) in female placental mammals. It is an indispensable factor in up-regulation of Xist transcription, thereby leading to initiation of random XCI. It also targets REX1, an inhibitor of XCI, for proteasomal degradation. RNF12 also acts as a co-regulator for a range of transcription factors, particularly those containing a LIM homeodomain, and modulates the formation of transcriptional multiprotein complexes. It is a negative regulator of Smad7, which in turn negatively regulates the signaling of type I receptors from the transforming growth factor beta (TGF-beta) superfamily. In addition, paternal RNF12 is a critical survival factor for milk-producing alveolar cells. RNF12 contains an nuclear localization signal (NLS) and a C3H2C3-type RING-H2 finger
KTCSVCITEYTEGNKLRKLPCSHEYHVHCIDRWLSENSTCPICRRAVLASG
>gnl|CDD|438337 cd16675, RING-H2_RNF24, RING finger, H2 subclass, found in RING finger protein 24 (RNF24) and similar proteins. RNF24 is an intrinsic membrane protein localized in the Golgi apparatus. It specifically interacts with the ankyrin-repeats domains (ARDs) of TRPC1, -3, -4, -5, -6, and -7, and affects TRPC intracellular trafficking without affecting their activity. RNF24 contains an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger
EICAVCLEEFKPKDELGICPCKHAFHRKCLIKWLEVRKVCPLCNMPVLQLAQLH
>gnl|CDD|438338 cd16676, RING-H2_RNF122, RING finger, H2 subclass, found in RING finger protein 122 (RNF122) and similar proteins. RNF122 is a RING finger protein associated with HEK 293T cell viability. It is localized to the endoplasmic reticulum (ER) and the Golgi apparatus, and overexpressed in anaplastic thyroid cancer cells. RNF122 functions as an E3 ubiquitin ligase that can ubiquitinate itself and undergo degradation through its RING finger in a proteasome-dependent manner. It interacts with calcium-modulating cyclophilin ligand (CAML), which is not a substrate, but a stabilizer of RNF122. RNF122 contains an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger
QTCAVCLEDFKTKDELGVLPCQHAFHRKCLVKWLEIRCVCPMCNKPI
>gnl|CDD|438339 cd16677, RING-H2_RNF32_rpt1, first RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins. RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, proteins with double RING-H2 fingers may act as scaffolds for binding several proteins that function in the same pathway. This model corresponds to the first RING-H2 finger
PCPICLEDFGLQQQVLLSCSHVFHRACLESFERFSGKKTCPMCRKEQYQ
>gnl|CDD|438340 cd16678, RING-H2_RNF32_rpt2, second RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins. RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, proteins with double RING-H2 fingers may act as scaffolds for binding several proteins that function in the same pathway. This model corresponds to the second RING-H2 finger
DCPICLTPLQSSGDSSDAKRVSSRPTVLLSCSHVFHATCLEAFEEFSVGEELVCPVCRSHY
>gnl|CDD|438341 cd16679, RING-H2_RNF38, RING finger, H2 subclass, found in RING finger protein 38 (RNF38) and similar proteins. RNF38 is a nuclear E3 ubiquitin protein ligase that is widely expressed throughout the human body, and is especially highly expressed in the heart, brain, placenta and the testis. It recognizes p53 as a substrate for ubiquitination, and thus plays a role in regulating p53. The overexpression of RNF38 increases p53 ubiquitination and alters p53 localization. It is also capable of autoubiquitination. RNF38 expression is negatively regulated by the serotonergic system. Induction of RNF38 may be involved in the anxiety-like behavior or non-cell autonomy in Oryzias latipes by the decline of serotonin (5-HT) levels. RNF38 contains a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), a C3H2C3-type RING-H2 finger, as well as two potential nuclear localization signals
ADIEQLPSYRFNPNNHQSEQTLCVVCMCDFESRQLLRVLPCNHEFHAKCVDKWLKANRTCPICRADA
>gnl|CDD|438342 cd16680, RING-H2_RNF44, RING finger, H2 subclass, found in RING finger protein 44 (RNF44) and similar proteins. RNF44 is an uncharacterized RING finger protein that shows high sequence similarity with RNF38, which is a nuclear E3 ubiquitin protein ligase that plays a role in regulating p53. RNF44 contains a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C2-type RING-H2 finger
ENHQSEQTLCVVCFSDFESRQLLRVLPCNHEFHTKCVDKWLKTNRTCPICRADASEVHRDAE
>gnl|CDD|438343 cd16681, RING-H2_RNF111, RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins. RNF111, also known as Arkadia, is a nuclear E3 ubiquitin-protein ligase that targets intracellular effectors and modulators of transforming growth factor beta (TGF-beta)/Nodal-related signaling for polyubiquitination and proteasome-dependent degradation. It acts as an amplifier of Nodal signals, and enhances the dorsalizing activity of limiting amounts of Xnr1, a Nodal homolog, and requires Nodal signaling for its function. The loss of RNF111 results in early embryonic lethality, with defects attributed to compromised Nodal signaling. RNF111 also regulates tumor metastasis by modulation of the TGF-beta pathway. Its ubiquitination can be modulated by the four and a half LIM-only protein 2 (FHL2) that activates TGF-beta signal transduction. Furthermore, RNF111 interacts with the clathrin-adaptor 2 (AP2) complex and regulates endocytosis of certain cell surface receptors, leading to modulation of epidermal growth factor (EGF) and possibly other signaling pathways. In addition, RNF111 has been identified as a small ubiquitin-like modifier (SUMO)-binding protein with clustered SUMO-interacting motifs (SIMs) that together form a SUMO-binding domain (SBD). It thus functions as a SUMO-targeted ubiquitin ligase (STUbL) that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response, as well as triggers degradation of signal-induced polysumoylated proteins, such as the promyelocytic leukemia protein (PML). The N-terminal half of RNF111 harbors three SIMs. Its C-terminal half show high sequence similarity with RING finger protein 165 (RNF165), where it contains two serine rich domains, two nuclear localization signals, an NRG-TIER domain, and a C-terminal C3H2C3-type RING-H2 finger that is required for polyubiqutination and proteasome-dependent degradation of phosphorylated forms of Smad2/3 and three major negative regulators of TGF-beta signaling, Smad7, SnoN and c-Ski
GEEGTEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQL
>gnl|CDD|438344 cd16682, RING-H2_RNF165, RING finger, H2 subclass, found in RING finger protein 165 (RNF165) and similar proteins. RNF165, also known as Arkadia-like 2, Arkadia2, or Ark2C, is an E3 ubiquitin ligase with homology to the C-terminal half of RNF111. It is expressed specifically in the nervous system, and can serve to amplify neuronal responses to specific signals. It acts as a positive regulator of bone morphogenetic protein (BMP)-Smad signaling that is involved in motor neuron (MN) axon elongation. RNF165 contains two serine rich domains, a nuclear localization signal, an NRG-TIER domain, and a C-terminal C3H2C3-type RING-H2 finger that is responsible for the enhancement of BMP-Smad1/5/8 signaling in the spinal cord
GEESDTDEKCTICLSMLEDGEDVRRLPCMHLFHQLCVDQWLAMSKKCPICRVDIETQLG
>gnl|CDD|438345 cd16683, RING-H2_RNF139, RING finger, H2 subclass, found in RING finger protein 139 (RNF139) and similar proteins. RNF139, also known as translocation in renal carcinoma on chromosome 8 protein (TRC8), is an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. It is a tumor suppressor that has been implicated in a novel regulatory relationship linking the cholesterol/lipid biosynthetic pathway with cellular growth control. A mutation in RNF139 has been identified in families with hereditary renal (RCC) and thyroid cancers. RNF139 physically and functionally interacts with von Hippel-Lindau (VHL), which is part of an SCF related E3-ubiquitin ligase complex with "gatekeeper" function in renal carcinoma and is defective in most sporadic clear-cell renal cell carcinomas (ccRCC). It suppresses growth and functions with VHL in a common pathway. RNF139 also suppresses tumorigenesis by targeting heme oxygenase-1 for ubiquitination and degradation. Moreover, RNF139 is a target of Translin (TSN), a posttranscriptional regulator of genes transcribed by the transcription factor CREM-tau in postmeiotic male germ cells, suggesting a role of RNF139 in dysgerminoma. In addition, RNF139 forms an integral part of a novel multi-protein ER complex, containing MHC I, US2, and signal peptide peptidase, which is associated with the ER-associated degradation (ERAD) pathway. It is required for the ubiquitination of MHC class I molecules before dislocation from the ER. As a novel sterol-sensing ER membrane protein, RNF139 hinders sterol regulatory element-binding protein-2 (SREBP-2) processing through interaction with SREBP-2 and SREBP cleavage-activated protein (SCAP), regulating its own turnover rate via its E3 ubiquitin ligase activity. RNF139 shows two regions of similarity with the receptor for sonic hedgehog (SHH), Patched. The first region corresponds to the second extracellular domain of Patched, which is involved in binding SHH. The second region is a putative sterol-sensing domain (SSD). The C-terminal half of RNF139 contains a C3H2C3-type RING-H2 finger with E3-ubiquitin ligase activity in vitro
REIDDVCAICYQEFTTSARITPCNHYFHALCLRKWLYIQDTCPMCHQKVYIEDD
>gnl|CDD|319598 cd16684, RING-H2_RNF145, RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins. RNF145 is an uncharacterized RING finger protein encoded by the RNF145 gene, which is expressed in T lymphocytes, and its expression is altered in acute myelomonocytic and acute promyelocytic leukemias. Although its biological function remains unclear, RNF145 shows high sequence similarity with RNF139, an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. Like RNF139, RNF145 contains a C3H2C3-type RING-H2 finger with possible E3-ubiquitin ligase activity
HNDICSICYQDMKSAVITPCSHFFHAGCLKKWLYVQETCPLCH
>gnl|CDD|438346 cd16685, RING-H2_UBR1, RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1) and similar proteins. UBR1, also known as N-recognin-1 or E3alpha-I, is an E3 ubiquitin-protein ligase component of the N-end rule pathway. It also promotes degradation of proteins via distinct mechanism that detects a misfolded conformation. UBR1 associates with the RAD6-encoded E2 enzyme to form an E2-E3 complex that catalyzes the synthesis of a substrate-linked multi-ubiquitin chain and may also mediate the delivery of substrates to the 26S proteasome. Moreover, UBR1 promotes the degradation of misfolded proteins in the cytosol. It promotes protein kinase quality control and sensitizes cells to heat shock protein 90 (Hsp90) inhibition. Furthermore, UBR1 functions as a polyubiquitylation-enhancing component of the UBR1-UFD4 complex in its targeting of ubiquitin-fusion degradation (UFD) substrates. UBR1 harbors at least three distinct substrate-binding sites and functions in association with Ubc2/Rad6 and also Ubc4. It contains an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain. A missense mutation in UBR1 is responsible for Johanson-Blizzard syndrome leads to UBR box unfolding and loss of function
EVLTCILCQEEQEVKLDKMAMVLTACVQKSTALTQNRGKVVELTGENFDPLFMNPDLAYGTHTGSCGHVM
HAVCWQKYFEAVQNSTRQRLHVELIFDLENGEYLCPLCKSLCNTVIPIIP
>gnl|CDD|438347 cd16686, RING-H2_UBR2, RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar proteins. UBR2, also known as N-recognin-2 or E3alpha-II, is an E3 ubiquitin-protein ligase that plays an important role in maintaining genome integrity and in homologous recombination repair. It regulates the level of the transcription factor Rpn4 (also known as Son1 and Ufd5) through ubiquitylation. The ubiquitin-conjugating enzyme Rad6, another binding partner of URB2, and an additional factor Mub1, are required for the ubiquitin-dependent degradation of Rpn4. UBR2 associates with Mub1 to form a Mub1/Ubr2 complex that regulates the conserved Dsn1 kinetochore protein levels, which is a part of a quality control system that monitors kinetochore integrity, thus ensuring genomic stability. As the recognition component of a major cellular proteolytic system, UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both spermatocytes and somatic cells. UBR2 also mediates transcriptional silencing during spermatogenesis via histone ubiquitination. It functions as a scaffold E3 promoting HR6B/UbcH2-dependent ubiquitylation of H2A and H2B, but not H3 and H4. It also binds to Tex19.1, also known as Tex19, a germ cell-specific protein, and metabolically stabilizes it during spermatogenesis. Furthermore, UBR2 is involved in skeletal muscle (SKM) atrophy. Its expression can be modulated by the mouse ether-a-gogo-related gene 1a (MERG1a) potassium channel. In addition, UBR2 up-regulation in cachectic muscle is mediated by the p38beta-CCAAT/enhancer binding protein (C/EBP)-beta signaling pathway responsible for the bulk of tumor-induced muscle proteolysis. UBR2 contains an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain
TCILCQEEQEIKVDNKAMVLAAFVQRSTVMSKNRSRVIHDPEKYDPLFMHPDLSCGTHTGSCGHIMHAHC
WQRYFDAVQAKEQRRQQRLRVHTSYDVENGEFLCPLCECLSNTVIP
>gnl|CDD|438348 cd16687, RING-H2_Vps8, RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 8 (Vps8) and similar proteins. Vps8 is the Rab-specific subunit of the endosomal tethering complex CORVET (class C core vacuole/endosome transport) that also includes Vps3 and a Class C Vps core complex composed of Vps11, Vps16, Vps18, and Vps33. CORVET operates at endosomes, controls traffic into late endosomes, and interacts with the Rab5/Vps21-GTP form. The CORVET-specific Vps3 and Vps8 subunits belong to the class D Vps. They form a subcomplex that interact with Rab5/Vps21, and is critical for localization and function of the CORVET tethering complex on endosomes. Vps8 contains an N-terminal WD40 repeat and a C-terminal C3H2C3-type RING-H2 finger
DSCCICLKPYKRREDNDEVIVFSCGHAYHSTCLRSKGSGVVTDGQERWTCYLCN
>gnl|CDD|438349 cd16688, RING-H2_Vps11, RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog (Vps11) and similar proteins. Vps11, also known as RING finger protein 108 (RNF108), is a soluble protein involved in regulation of glycolipid degradation and retrograde toxin transport. It is highly expressed in heart and pancreas. Vps11 associates with Vps16, Vps18, and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. Vps11 is a central scaffold protein upon which both HOPS and CORVET assemble. The HOPS and CORVET complexes disassemble in the absence of Vps11, resulting in massive fragmentation of vacuoles. Vps11 contains a clathrin repeat domain and a C-terminal C3H2C3-type RING-H2 finger. This subfamily also includes Vps11 homologs found in fungi, such as Saccharomyces cerevisiae vacuolar membrane protein Pep5p, also known as carboxypeptidase Y-deficient protein 5, vacuolar morphogenesis protein 1, or vacuolar biogenesis protein END1. Pep5p is essential for vacuolar biogenesis. It associates with Pep3p to form a core Pep3p/Pep5p complex that promotes vesicular docking/fusion reactions in conjunction with SNARE proteins at multiple steps in transport routes to the vacuole
TKCSACGSTLDLPSVHFLCGHSFHQHCLEDYEENDRECPLCAPE
>gnl|CDD|438350 cd16689, RING-H2_Vps18, RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 18 (Vps18) and similar proteins. Vps18 is an ubiquitin ligase E3 that is highly expressed in heart. It induces the ubiquitylation and degradation of serum-inducible kinase. Vps18 associates with Vps11, Vps16, and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. Vps18 deficiency inhibits dendritogenesis in Purkinje cells by blocking the lysosomal degradation of lysyl oxidase. Vps18 contains a clathrin heavy chain repeat, a coiled-coil domain, and a C3H2C3-type RING-H2 finger domain close to its C-terminus. This subfamily also includes Vps18 homologs found in insects and fungi, such as Drosophila melanogaster protein Dor (encoded by deep orange (dor) gene), and Saccharomyces cerevisiae vacuolar membrane protein Pep3p, also known as carboxypeptidase Y-deficient protein 3, or vacuolar morphogenesis protein 8. Drosophila Dor is part of a protein complex, that also includes the Sep1p homolog carnation (car), which localizes to endosomal compartments and is required not only for the biogenesis of pigment granules but also for the normal delivery of proteins to lysosomes. Pep3p is a vacuolar peripheral membrane protein that is required for vacuolar biogenesis in Saccharomyces cerevisiae. Pep3p associates with Pep5p to form a core Pep3p/Pep5p complex that promotes vesicular docking/fusion reactions in conjunction with SNARE proteins at multiple steps in transport routes to the vacuole
EKCAACDFPLLNRPFYLFLCGHMFHYDCLEQIDDIIAAECVYCGE
>gnl|CDD|438351 cd16690, RING-H2_Vps41, RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 41 (Vps41) and similar proteins. Vps41, also known as S53, is a protein involved in trafficking of proteins from the late Golgi to the vacuole. It interacts with caspase-8, suggesting a potential role of Vps41 beyond lysosomal trafficking. It has been identified as a potential therapeutic target for human Parkinson's disease (PD). Vps41 and the soluble N-ethylmaleimide-sensitive factor attachment protein receptors protein VAMP7 are specifically involved in the fusion of the trans-Golgi network-derived lysosome-associated membrane protein carriers with late endosomes. Vps41 is a specific subunit of the lysosomal tethering complex HOPS (homotypic vacuole fusion and protein sorting) that also includes Vps39 and a Class C Vps core complex composed of Vps11, Vps16, Vps18, and Vps33. HOPS operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. The HOPS-specific Vps39 and Vps41 subunits belong to the class B Vps. They form a subcomplex that interacts with Rab7/Ypt7 and is are required for homotypic and heterotypic late endosome fusion. Vps41 contains an N-terminal WD40 repeat, one or two clathrin repeats and a C3H2C3-type RING-H2 finger domain close to its C-terminus
EEQICEACHRPLLVSDLRKAFNVVVFFCRHAFHEDCLPAQNVEFCNICSAQ
>gnl|CDD|438352 cd16691, mRING-H2-C3H3C2_Mio, Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and simialr proteins. This family contains Mio,its counterpart Sea4 from yeast, and other homologs. Mio/Sea4 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea2/WDR24, and Sea3/WDR59. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. Mio interacts with endogenous RagA and RagC, and plays an essential role in the activation of mTOR Complex 1 (mTORC1) by amino acids. In GATOR2, Mio and Seh1 localize to lysosomes and autolysosomes, and form a heterodimer that is required to oppose the TORC1 inhibitory activity of the Iml1/GATOR1 complex to prevent the constitutive down-regulation of TORC1 activity in later stages of oogenesis. A tissue-specific requirement is necessary for Mio to be involved in cell growth in the female germ line. Mio contains an N-terminal WD40 domain and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type
LPRCSLCLIPMGTPSSSLPGATASDVDLSSDKKLAPFSSWFTWCQTCRHGGHAGHLQEWFRDHSECPVSG
CDCKC
>gnl|CDD|438353 cd16692, mRING-H2-C3H3C2_WDR59, Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 (WDR59) and similar proteins. WDR59 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea2/WDR24, and Mio/Sea4. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. WDR59 contains an N-terminal WD40 domain followed by a RWD domain, and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type. Sea3 is the yeast counterpart of WDR59. It is not included in this subfamily
LQCAICHVAVRGSSNFCLACGHGGHTSHMMEWFRTQDVCPTGCGCHC
>gnl|CDD|438354 cd16693, mRING-H2-C3H3C2_WDR24, Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 (WDR24) and similar proteins. WDR24 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea3/WDR59, and Mio/Sea4. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. WDR24 contains an N-terminal WD40 domain and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type. Sea2 is the yeast counterpart of WDR24. It is not included in this subfamily
MCSVCHLPVKGLYVWCQGCGHGGHLEHMKEWFSTNSHCPAGCGHLC
>gnl|CDD|438355 cd16694, mRING-CH-C4HC2H_ZNRF1, Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 1 (ZNRF1) and similar proteins. ZNRF1, also known as Nerve injury-induced gene 283 protein (nin283), or peripheral nerve injury protein (PNIP), is an E3 ubiquitin-protein ligase that is highly expressed in the nervous system during development and is associated with synaptic vesicle membranes. It is N-myrisotoylated and is also located in the endosome-lysosome compartment in fibroblasts, suggesting it may participate in ubiquitin-mediated protein modification. It contains an N-terminal MAGE domain, and a special C-terminal domain that combines a zinc finger and a modified C4HC2H-type RING-CH finger, rather than the typical C4HC3-type RING-CH finger, which is a variant of the RING-H2 finger. Only the RING finger of the zinc finger-RING finger motif is required for its E3 ubiquitin ligase activity. ZNRF1 regulates Schwann cell differentiation by proteasomal degradation of glutamine synthetase (GS). It also mediates regulation of neuritogenesis via interaction with beta-tubulin type 2 (Tubb2). Moreover, ZNRF1 promotes Wallerian degeneration by degrading AKT to induce glycogen synthase kinase-3beta (GSK3B)-dependent CRMP2 phosphorylation. Furthermore, ZNRF1 and its sister protein ZNRF2 regulate the ubiquitous Na+/K+ pump (Na+/K+ATPase). In addition, ZNRF1 may be associated with leukemogenesis of acute lymphoblastic leukemia (ALL) with paired box domain gene 5 (PAX5) alteration
ECVICLEELLQGDTIARLPCLCIYHKSCIDSWFEVNRSCPEHPSD
>gnl|CDD|438356 cd16695, mRING-CH-C4HC2H_ZNRF2, Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 2 (ZNRF2) and similar proteins. ZNRF2, also known as protein Ells2 or RING finger protein 202 (RNF202), is an E3 ubiquitin-protein ligase that is highly expressed in the nervous system during development and is present in presynaptic plasma membranes. It is N-myrisotoylated and is also located in the endosome-lysosome compartment in fibroblasts. It contains an N-terminal MAGE domain, and a special C-terminal domain that combines a zinc finger and a modified C4HC2H-type RING-CH finger, rather than the typical C4HC3-type RING-CH finger, which is a variant of RING-H2 finger. Only the RING finger of the zinc finger-RING finger motif is required for its E3 ubiquitin ligase activity. Together with its sister protein ZNRF1, ZNRF2 regulates the ubiquitous Na+/K+ pump (Na+/K+ATPase)
YNEDVLSKDAGECAICLEELQQGDTIARLPCLCIYHKGCIDEWFEVNRSCPEHPSD
>gnl|CDD|438357 cd16696, RING-CH-C4HC3_NFX1, RING-CH finger, H2 subclass (C4HC3-type), found in transcriptional repressor NF-X1 and similar proteins. NF-X1, also known as nuclear transcription factor, X box-binding protein 1, is a novel cysteine-rich sequence-specific DNA-binding protein that interacts with the conserved X-box motif of the human major histocompatibility complex (MHC) class II genes via a repeated Cys-His domain. It functions as a cytokine-inducible transcriptional repressor that plays an important role in regulating the duration of an inflammatory response by limiting the period in which class II MHC molecules are induced by interferon gamma (IFN- gamma). NFX1 contains an N-terminal PAM2 motif, a C4HC3-type RING-CH finger, a Cys-rich region that harbors several NFX1-type zinc fingers, and a C-terminal R3H domain
YECMVCCEVVRVMAPVWSCSSCYHVFHLNCIKKWARSPAAQAEDNSGGWRCPACQ
>gnl|CDD|438358 cd16697, RING-CH-C4HC3_NFXL1, RING-CH finger, H2 subclass (C4HC3-type), found in nuclear transcription factor, X-box binding-like 1 (NFXL1) and similar proteins. NFXL1, also known as NF-X1-type zinc finger protein NFXL1, or ovarian zinc finger protein (OZFP), is encoded by the novel human cytoplasm-distribution zinc finger protein (CDZFP) gene. It is a putative zinc finger protein with a C4HC3-type RING-CH finger and a Cys-rich region that harbors several NFX1-type zinc fingers
STCLICIESIKRNDAIWSCSGCFCIFHLPCIQKWAKDSIFLVSLRSASDFPQKELPWHCPKCR
>gnl|CDD|438359 cd16698, RING_CH-C4HC3_MARCH1-like, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING finger protein MARCH1, MARCH8, and similar proteins. This subfamily includes the closely related MARCH1 and MARCH8, both of which are located on endosomes and the plasma membrane and are implicated in regulating cell surface expression of their substrates. They ubiquitylate and downregulate many targets, including major histocompatibility complex class II (MHCII), CD86, transferrin receptor, HLA-DM, and Fas from the cell surface. MARCH1 is mainly expressed in cells of the immune system, while MARCH8 is more broadly expressed. Both of them contain an N-terminal C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, and two transmembrane domains. The cytoplasmic RING-CH finger participates in the ubiquitin transfer from the E2 to its substrate. The transmembrane domains are implicated in target recognition and dimer formation
ICRICHCEGDPENPLITPCYCSGSLKYVHQACLQQWIKSSDTKSCELCKFEF
>gnl|CDD|438360 cd16699, RING_CH-C4HC3_MARCH2-like, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING finger proteins MARCH2, MARCH3, and similar proteins. MARCH2 and MARCH3 contain a C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, in the N-terminal cytoplasmic region, two transmembrane domains in the middle region, and a PDZ-binding motif at the C-terminus. MARCH2 is a Golgi-localized, membrane-associated E3 ubiquitin-protein ligase that is involved in endosomal trafficking through the binding of syntaxin 6 (STX6). It is involved in the cystic fibrosis transmembrane conductance regulator (CFTR)-associated ligand (CAL)-mediated ubiquitination and lysosomal degradation of mature CFTR through the association with adaptor proteins CAL and STX6. It also reduces the surface expression of CD86 and the transferrin receptor TFRC and regulates cell surface carvedilol-bound beta2-adrenergic receptor (beta2ARs) expression. Moreover, MARCH2 interacts with and ubiquitinates PDZ domains polarity determining scaffold protein DLG1 through its PDZ-binding motif, suggesting it may function as a molecular bridge with ubiquitin ligase activity connecting endocytic tumor suppressor proteins such as syntaxins to DLG1. MARCH3 is an E3 ubiquitin-protein ligase that is broadly expressed at relatively high levels in spleen, colon, and lung. It is localized to early endosomes, binds to MARCH2 and syntaxin 6, and is involved in the regulation of vesicular trafficking and fusion of the transport vesicles in endosomes. Its E2 specificity significantly overlaps that of MARCH2
FCRICHEGESTEDLLSPCECTGTLGLVHRSCLEQWLSSSNTNSCEICHFEY
>gnl|CDD|319614 cd16700, RING_CH-C4HC3_MARCH4-like, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING finger proteins MARCH4, MARCH9, MARCH11, and similar proteins. MARCH4 and MARCH9 are closely related to each other. They downregulate major histocompatibility complex-I (MHC-I). Moreover, MARCH4 and MARCH9, but not other MARCH proteins, can associate with Mult1 and prevent Mult1 expression at the cell surface in a lysine-dependent manner that can be reversed by heat shocking the cells. MARCH11 is a transmembrane RING-finger ubiquitin ligase that is predominantly expressed in developing spermatids in a stage-specific manner and is localized to trans-Golgi network (TGN) vesicles and multivesicular bodies (MVBs). It mediates selective protein sorting via the TGN-MVB transport pathway through its ubiquitin ligase activity. SAMT family proteins have been identified as substrates of MARCH11 in mouse spermatids, suggesting that MARCH11 plays a role in mammalian spermiogenesis. Moreover, MARCH11 targets CD4 for ubiquitination. It also forms complexes with the adaptor protein complex-1 and with fucose-containing glycoproteins including ubiquitinated forms. All subfamily members contain an N-terminal C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, followed by two transmembrane regions
LCRICFQGAEQGELLSPCRCDGSVRCTHQPCLLKWISERGSWSCELCYYRY
>gnl|CDD|438361 cd16701, RING_CH-C4HC3_MARCH5, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING-CH5 (MARCH5). MARCH5, also known as membrane-associated RING finger protein 5, membrane-associated RING-CH protein V (MARCH-V), RING finger protein 153 (RNF153), or mitochondrial ubiquitin ligase (MITOL), is a mitochondrial outer membrane-associated E3 ubiquitin-protein ligase that regulates mitochondrial dynamics including mitochondrial morphology, transport, and interaction with endoplasmic reticulum (ER), at least in part, through the ubiquitination of mitochondrial fission factor Drp1, microtubule-associated protein 1B (MAP1B) and mitofusin 2 (Mfn2), respectively. MARCH5 also mediates the cell cycle-dependent degradation of Mitofusin 1 (Mfn1) in G2/M phase, and thus serves as an upstream quality controller of Mitofusin 1 (Mfn1), preventing excessive accumulation of Mfn1 protein under stress conditions, which is crucial for mitochondrial homeostasis and cell viability. Moreover, MARCH5 is involved in maintaining mouse-embryonic stem cell (mESC) pluripotency via suppression of ERK signalling. It is also a positive regulator of Toll-like receptor 7 (TLR7)-mediated NF-kappaB activation in mammals. MARCH5 contains an N-terminal C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, and four C-terminal transmembrane spans
RTCWVCFATDEDDRSAEWVRPCRCRGTTKWVHQACLQRWIDEKQKGNSTAKVSCPQCNTEY
>gnl|CDD|438362 cd16702, RING_CH-C4HC3_MARCH6, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING-CH6 (MARCH6). MARCH6, also known as membrane-associated RING finger protein 6, membrane-associated RING-CH protein VI (MARCH-VI), RING finger protein 176 (RNF176), protein TEB-4, or Doa10 homolog, is an endoplasmic reticulum (ER)-localized E3 ubiquitin ligase that ubiquitinates ER-associated proteins with a cytoplasmic domain in a ubiquitin-conjugating enzyme 7 (UBC7)-dependent manner), such as Mps2, UBC6, and Ste6. It also regulates its own UBC7-mediated degradation. MARCH6 interacts with ubiquitin-specific protease USP19, which deubiquitinates and stabilizes MARCH6 and inhibits p97-dependent proteasomal degradation. It is also involved in the cholesterol synthesis pathway by controlling the degradation of squalene monooxygenase (SM), and affects 3-hydroxy-3-methyl-glutaryl coenzyme A reductase (HMGCR). Furthermore, it may be a key regulator of thyroid hormone activation in a number of tissues, since it mediates the proteasomal degradation of type 2 iodothyronine deiodinase (D2). MARCH6 contains 14 transmembrane helices and a conserved N-terminal C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, that catalyzes ubiquitin Lys48-specific ligation
ICRVCRGEGTPDRPLFHPCKCSGSIKYVHQECLLQWLKHSRKEYCELCKH
>gnl|CDD|438363 cd16703, RING_CH-C4HC3_MARCH7-like, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated MARCH7, MARCH10, and similar proteins. This subfamily includes two closely related membrane-associated RING-CH proteins, MARCH7 and MARCH10, both of which are predicted to have no transmembrane spanning region, but do harbor a C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, that is responsible for E3 activity. MARCH7, also known as MARCH-VII, RNF177, or axotrophin, is a ubiquitin E3 ligase expressed in multiple types of cells and tissues, including stem cells and precursor cells, and is predominantly localized on the plasma membrane, and cytoplasm. MARCH7 is involved in T cell proliferation and neuronal development. It also participates in the regulation of cytoskeleton re-organization, cellular migration and invasion, cell proliferation, and tumorigenesis in ovarian carcinoma cells. Moreover, MARCH7 modulates nuclear factor kappaB (NF-kappaB) and Wnt/beta-catenin pathways. It has been identified as an authentic target of miR-101. It ubiquitinates tau protein in vitro, impairing microtubule binding. MARCH10, also known as MARCH-X or RNF190, is a microtubule-associated E3 ubiquitin ligase of developing spermatids and is involved in spermiogenesis by regulating the formation and maintenance of the flagella. It is localized to the principal piece of elongating spermatids. in developing spermatids
EGDLCRICQTAGDSTSNQLIEPCQCTGSLQLVHQECLKKWLISKIQSGAELDAVKTCEMCK
>gnl|CDD|438364 cd16704, RING-HC_RNF20-like, RING finger, HC subclass, found in RING finger protein RNF20, RNF40, and similar proteins. RNF20, also known as BRE1A, and RNF40, also known as BRE1B, are E3 ubiquitin-protein ligases that work together to form a heterodimeric complex that facilitate the K120 monoubiquitination of histone H2B (H2Bub1), a DNA damage-induced histone modification that is crucial for recruitment of the chromatin remodeler SNF2h to DNA double-strand break (DSB) damage sites. RNF20 regulates the cell cycle and differentiation of neural precursor cells (NPCs) and links histone H2B ubiquitylation with inflammation and inflammation-associated cancer. RNF40, also known as 95 kDa retinoblastoma-associated protein (RBP95), was identified as a novel leucine zipper retinoblastoma protein (pRb)-associated protein that may function as a regulation factor in RNA polymerase II-mediated transcription and/or transcriptional processing. All subfamily members contain a C3HC4-type RING-HC finger at its C-terminus
LEEIKEYKARLTCPCCNTRKKDAVLTKCFHVFCFECLKTRYETRQRKCPKCNAAFGANDFHRIYI
>gnl|CDD|438365 cd16705, RING-HC_dBre1-like, RING finger, HC subclass, found in Drosophila melanogaster Bre1 (dBre1) and similar proteins. dBre1 is the functional homolog of yeast Bre1, an E3 ubiquitin ligase required for the monoubiquitination of histone H2B and, indirectly, for H3K4 methylation. dBre1 acts as a nuclear component required for the expression of Notch target genes in Drosophila development. dBre1 contains a C3HC4-type RING-HC finger at its C-terminus
DEVLMEEIREYKEQLTCPSCKVKRKDAVLTKCFHVFCLDCLRTRYETRQRKCPKCNAAFGANDYHRLYL
>gnl|CDD|438366 cd16706, RING-HC_CARP1, RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 1 (CARP1) and similar proteins. CARP1, also known as caspase regulator CARP1, FYVE-RING finger protein Momo, RING finger homologous to inhibitor of apoptosis protein (RFI), RING finger protein 34 (RNF34), or RING finger protein RIFF, is a nuclear protein that functions as a specific E3 ubiquitin ligase for the transcriptional coactivator PGC-1alpha, a master regulator of energy metabolism and adaptive thermogenesis in the brown fat cell which negatively regulates brown fat cell metabolism. It is preferentially expressed in esophageal, gastric, and colorectal cancers, suggesting a possible association with the development of digestive tract cancers. It regulates the p53 signaling pathway by degrading 14-3-3 sigma and stabilizing MDM2. CARP1 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10. CARP1 contains an N-terminal FYVE-like domain and a C-terminal C3HC4-type RING-HC finger domain
GSDDNLCRICMDAVIDCVLLECGHMVTCTKCGKRMSECPICRQYVVRAVHVFKS
>gnl|CDD|438367 cd16707, RING-HC_CARP2, RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 2 (CARP-2) and similar proteins. CARP-2, also known as rififylin, caspase regulator CARP2, FYVE-RING finger protein Sakura (Fring), RING finger and FYVE-like domain-containing protein 1, RING finger protein 189 (RNF189), or RING finger protein 34-like, is an endosome-associated E3 ubiquitin-protein ligase that targets internalized receptor interacting kinase (RIP) for proteasome-mediated degradation. It acts as a negative regulator of tumor necrosis factor (TNF)-induced nuclear factor (NF)-kappaB activation. It also regulates the p53 signaling pathway by degrading 14-3-3sigma and stabilizing MDM2. As a caspase regulator, CARP2 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10. CARP2 contains an N-terminal FYVE-like domain and a C-terminal C3HC4-type RING-HC finger domain
DENLCKICMDSPIDCVLLECGHMVTCTKCGKRMSECPICRQYVIRAVHVF
>gnl|CDD|438368 cd16708, RING-HC_Cbl, RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl and similar proteins. Cbl, also known as Casitas B-lineage lymphoma proto-oncogene, proto-oncogene c-Cbl, RING finger protein 55 (RNF55), or signal transduction protein Cbl, is a multi-domain protein that acts as a key negative regulator of various receptor and non-receptor tyrosine kinase signaling. It contains a tyrosine kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a proline-rich domain, a C3HC4-type RING-HC finger, and an ubiquitin-associated (UBA) domain. TKB is responsible for the interactions with many tyrosine kinases, such as the colony-stimulating factor-1 (CSF-1) receptor, Syk/ZAP-70, and Src-family of protein tyrosine kinases. The proline-rich domain can recruit proteins with a SH3 domain. Moreover, Cbl functions as an E3 ubiquitin ligase that can bind ubiquitin-conjugating enzymes (E2s) through the RING-HC finger
QDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQESEGQGCPFCRCEIKGTE
PIVVDPF
>gnl|CDD|438369 cd16709, RING-HC_Cbl-b, RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-b and similar proteins. Cbl-b, also known as Casitas B-lineage lymphoma proto-oncogene b, RING finger protein 56 (RNF56), SH3-binding protein Cbl-b, or signal transduction protein Cbl-b, has been identified as a regulator of antigen-specific, T cell-intrinsic, peripheral immune tolerance, a state also known as clonal anergy. It may inhibit activation of the p85 subunit of phosphoinositide 3-kinase (PI3K), protein kinase C-theta (PKC-theta), and phospholipase C-gamma1 (PLC-gamma1) and negatively regulates T-cell receptor-induced transcription factor nuclear factor kappaB (NF-kappaB) activation. In addition, Cbl-b may target multiple signaling molecules involved in transforming growth factor (TGF)-beta-mediated transactivation pathways. Cbl-b contains a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a proline rich domain, a nuclear localization signal, a C3HC4-type RING-HC finger and an ubiquitin-associated (UBA) domain
DHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEP
IIVDPF
>gnl|CDD|438370 cd16710, RING-HC_Cbl-c, RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins. Cbl-c, also known as RING finger protein 57 (RNF57), SH3-binding protein Cbl-3, SH3-binding protein Cbl-c, or signal transduction protein Cbl-c, is an E3 ubiquitin-protein ligase expressed exclusively in epithelial cells. It contains a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a C3HC4-type RING-HC finger, and a short proline-rich region, but lacks the ubiquitin-associated (UBA) leucine zipper motif that are present in Cbl and Cbl-b. Cbl-c acts as a regulator of epidermal growth factor receptor (EGFR)-mediated signal transduction. It also suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation. Moreover, Cbl-c ubiquitinates and downregulates RETMEN2A and implicates Enigma (PDLIM7) as a positive regulator of RETMEN2A by blocking Cbl-mediated ubiquitination and degradation. The ubiquitin ligase activity of Cbl-c is increased via the interaction of its RING-HC finger domain with a LIM domain of the paxillin homolog, hydrogen peroxide induced construct 5 (Hic-5)
EQLQLYQAMNSTFELCKICAERDKDVRIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGREAVS
>gnl|CDD|438371 cd16711, RING-HC_DTX3, RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar proteins. DTX3, also known as RING finger protein 154 (RNF154), is an E3 ubiquitin-protein ligase that belongs to the Deltex (DTX) family. In contrast to other DTXs, DTX3 does not contain two N-terminal Notch-binding WWE domains, but a short unique N-terminal domain, suggesting it does not interact with the intracellular domain of Notch. Its C-terminal region includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain
EETCPICLGEIQNKKTLDKCKHSFCEDCITRALQVKKACPMCGEFYGQLIGNQP
>gnl|CDD|438372 cd16712, RING-HC_DTX3L, RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins. DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), is a RING-domain E3 ubiquitin-protein ligase that regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. DTX3L has a unique N-terminus, but lacks the highly basic N-terminal motif and the central proline-rich motif present in other Deltex (DTX) family members, such as DTX1, DTX2, and DTX4. Moreover, its C-terminal region is highly homologous to DTX3. It includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N-terminus and further enhance self-ubiquitination
QEEDECPICMDRISNKKVLPKCKHVFCAACIDKAMKYKPVCPVCGTIYGVIKGNQP
>gnl|CDD|438373 cd16713, RING-HC_BIRC2_3_7, RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar proteins. The cellular inhibitor of apoptosis protein c-IAPs function as ubiquitin E3 ligases that mediate the ubiquitination of substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB) signaling, and oncogenesis. Unlike other IAPs, such as XIAP, c-IAPs exhibit minimal binding to caspases and may not play an important role in the inhibition of these proteases. c-IAP1, also known as baculoviral IAP repeat-containing protein BIRC2, IAP-2, RING finger protein 48, or TNFR2-TRAF-signaling complex protein 2, is a potent regulator of the tumor necrosis factor (TNF) receptor family and NF-kappaB signaling pathways in the cytoplasm. It can also regulate E2F1 transcription factor-mediated control of cyclin transcription in the nucleus. c-IAP2, also known as BIRC3, IAP-1, apoptosis inhibitor 2 (API2), or IAP homolog C, also influences ubiquitin-dependent pathways that modulate innate immune signalling by activation of NF-kappaB. c-IAPs contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of polyubiquitin (polyUb), a caspase activation and recruitment domain (CARD) that serves as a protein interaction surface, and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. Livin, also known as baculoviral IAP repeat-containing protein 7 (BIRC7), kidney inhibitor of apoptosis protein (KIAP), melanoma inhibitor of apoptosis protein (ML-IAP), or RING finger protein 50, was identified as the melanoma IAP. It plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is regulated by the inhibition of caspase-3, -7, and -9. Its E3 ubiquitin-ligase-like activity promotes degradation of Smac/DIABLO, a critical endogenous regulator of all IAPs. Unlike other family members, mammalian livin contains a single BIR domain and a C3HC4-type RING-HC finger. The UBA domain can be detected in non-mammalian homologs of livin
LRRLQEERTCKVCMDKEVSIVFIPCGHLVVCTECAPSLRKCPICRATIKGTVRTFLS
>gnl|CDD|438374 cd16714, RING-HC_BIRC4_8, RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP repeat-containing protein 8 (BIRC8) and similar proteins. XIAP, also known as baculoviral IAP repeat-containing protein 4 (BIRC4), IAP-like protein (ILP), inhibitor of apoptosis protein 3 (IAP-3), or X-linked inhibitor of apoptosis protein (X-linked IAP), is a potent suppressor of apoptosis that directly inhibits specific members of the caspase family of cysteine proteases, including caspase-3, -7, and -9. It promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. The ubiquitin-protein ligase (E3) activity of XIAP also exhibits in the ubiquitination of second mitochondria-derived activator of caspases (Smac). The mitochondrial proteins, Smac/DIABLO and Omi/HtrA2, can inhibit the antiapoptotic activity of XIAP. XIAP has also been implicated in several intracellular signaling cascades involved in the cellular response to stress, such as the c-Jun N-terminal kinase (JNK), the nuclear factor-kappaB (NF-kappaB), and the transforming growth factor-beta (TGF-beta) pathways. Moreover, XIAP can regulate copper homeostasis by interacting with MURR1. BIRC8, also known as inhibitor of apoptosis-like protein 2, IAP-like protein 2, ILP-2, or testis-specific inhibitor of apoptosis, is a tissue-specific homolog of E3 ubiquitin-protein ligase XIAP. It has been implicated in the control of apoptosis in the testis by direct inhibition of caspase 9. Both XIAP and BIRC8 contain three N-terminal baculoviral IAP repeat (BIR) domains, a ubiquitin-association (UBA) domain and a C3HC4-type RING-HC finger at the carboxyl terminus
EISTEEKLRRLQEEKLCKICMDRNISIVFIPCGHLVTCKQCAEALDKCPICCTVITFKQKIFMS
>gnl|CDD|438375 cd16715, vRING-HC_IRF2BP1, variant of RING finger, HC subclass, found in interferon regulatory factor 2-binding protein 1 (IRF-2BP1). IRF-2BP1, also known as IRF-2-binding protein 1, is a nuclear protein that binds to the C-terminal repression domain of IRF-2 and acts as an IRF-2-dependent transcriptional corepressor, both enhancer-activated and basal transcription. It binds to Jun-dimerization protein 2 (JDP2), a member of the activating protein-1 (AP-1) family of transcription factors, and enhances the polyubiquitination of JDP2. It also represses activating transcription factor-2 (ATF2)-mediated transcriptional activation from a cyclic AMP-responsive element (CRE)-containing promoter. IRF-2BP1 contains an N-terminal C4-type zinc finger and a C-terminal variant C3HC4-type RING-HC finger
PLCCTICHERLEDTHFVQCPSVPGHKFCFPCSRDFIKAQGPAGEVYCPSGDKCPLVGSNVPW
>gnl|CDD|438376 cd16716, vRING-HC_IRF2BP2, variant of RING finger, HC subclass, found in interferon regulatory factor 2 (IRF2)-binding protein 2 (IRF-2BP2). IRF-2BP2, also known as IRF-2-binding protein 2 or DIF-1, is a nuclear protein that binds to the C-terminal repression domain of IRF-2 and acts as an IRF-2-dependent transcriptional corepressor, both enhancer-activated and basal transcription. IRF-2BP2 also specifically interacts with the C-terminal domain of the nuclear factor of activated T cells NFAT1 transcription factor, and negatively regulates the NFAT1-dependent transactivation of NFAT-responsive promoters. Moreover, IRF2BP2 suppresses the transactivation activity of p53 on both Bax and p21 promoters. It also shows anti-apoptotic activity through the modulation of the death domain in NRIF3. In addition, IRF2BP2 functions as a cofactor of VGLL4 and plays a critical role controlling gene expression in skeletal, cardiac, and smooth muscle cells. It is a muscle-enriched transcription factor required to activate vascular endothelial growth factor-A (VEGF-A) expression. IRF-2BP2 contains an N-terminal C4-type zinc finger and a C-terminal variant C3HC4-type RING-HC finger. The zinc finger is responsible for the homo- and hetero-dimerization between different members of the IRF-2BP2 family. The RING-HC finger interacts with IRF2 and also with nuclear receptor interacting factor 3 (NRIF3)
PLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRESIKQQGATGEVYCPSGEKCPLVGSNVPWAFMQG
>gnl|CDD|438377 cd16717, vRING-HC_IRF2BPL, variant of RING finger, HC subclass, found in interferon regulatory factor 2-binding protein-like (IRF-2BPL). IRF-2BPL, also known as C14orf4 or enhanced at puberty protein 1(EAP1), is a homolog of interferon regulatory factor 2-binding proteins, IRF-2BP1 and IRF-2BP2. It is expressed in the mediobasal hypothalamus and plays a critical function in regulating the female reproductive neuroendocrine axis. IRF-2BPL is a proline-rich protein with polyglutamine and polyalanine tracks at the N-terminus and a C3HC4-type RING-HC finger domain with a partially new pattern at the C-terminus
ANSGPLCCTICHERLEDTHFVQCPSVPSHKFCFPCSRESIKAQGATGEVYCPSGEKCPLVGSNVPW
>gnl|CDD|438378 cd16718, RING-HC_LNX3, RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3). LNX3, also known as PDZ domain-containing RING finger protein 3 (PDZRN3), or Semaphorin cytoplasmic domain-associated protein 3 (SEMACAP3), is an E3 ubiquitin-protein ligase that was first identified as a Semaphorin-binding partner. It is also responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX3 acts as a negative regulator of osteoblast differentiation by inhibiting Wnt-beta-catenin signaling. LNX3 also plays an important role in neuromuscular junction formation. It interacts with and ubiquitinates the muscle specific tyrosine kinase (MuSK), thus promoting its endocytosis and negatively regulating the cell surface expression of this key regulator of postsynaptic assembly. LNX3 contains an N-terminal C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain
VDPDFKCNLCNKVLEDPLTTPCGHVFCAGCVLPWVVQQGSCPVKCQR
>gnl|CDD|438379 cd16719, RING-HC_LNX4, RING finger, HC subclass, found in ligand of numb protein X 4 (LNX4). LNX4, also known as PDZ domain-containing RING finger protein 4 (PDZRN4), or SEMACAP3-like protein (SEMCAP3L), is an E3 ubiquitin-protein ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX4 contains an N-terminal C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain
VDPDLKCKLCGKVLEEPLSTPCGHVFCAGCLLPWAVQRRLCPLQCQPIAAKEL
>gnl|CDD|438380 cd16720, RING-HC_MEX3A, RING finger, HC subclass, found in RNA-binding protein MEX3A. MEX3A, also known as RING finger and KH domain-containing protein 4 (RKHD4), is an RNA-binding phosphoprotein that localizes in P-bodies and stress granules, which are two structures involved in the storage and turnover of mRNAs. It has been implicated in the regulation of tumorigenesis. It controls the polarity and stemness of intestinal epithelial cells through the post-transcriptional regulation of the homeobox transcription factor CDX2, which plays a crucial role in intestinal cell fate specification, both during normal development and in tumorigenic processes involving intestinal reprogramming. Moreover, it exhibits a transforming activity when overexpressed in gastric epithelial cells. MEX3A contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3A shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway
GGRDCMVCFESEVTAALVPCGHNLFCMECAVRICERNEPECPVCHALATQAIRIFS
>gnl|CDD|438381 cd16721, RING-HC_MEX3B, RING finger, HC subclass, found in RNA-binding protein MEX3B. MEX3B, also known as RING finger and KH domain-containing protein 3 (RKHD3), or RING finger protein 195 (RNF195), is an RNA-binding phosphoprotein that localizes in P-bodies and stress granules, which are two structures involved in the storage and turnover of mRNAs. It regulates the spatial organization of the Rap1 pathway that orchestrates Sertoli cell functions. It has a 3' long conserved untranslated region (3'LCU)-mediated fine-tuning system for mRNA regulation in early vertebrate development such as anteroposterior (AP) patterning and signal transduction. MEX3B contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3B shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway
RKGSRDCSICFESEVIAALVPCGHNLFCMECANRICEKNEPQCPVCHAAVTQAIRIFS
>gnl|CDD|438382 cd16722, RING-HC_MEX3C, RING finger, HC subclass, found in RNA-binding protein MEX3C. MEX3C, also known as RING finger and KH domain-containing protein 2 (RKHD2), or RING finger protein 194 (RNF194), is an RNA-binding phosphoprotein that acts as a suppressor of chromosomal instability. It functions as an ubiquitin E3 ligase responsible for the post-transcriptional, HLA-A allotype-specific regulation of MHC class I molecules (MHC-I). It also modifies retinoic acid inducible gene-1 (RIG-I) in stress granules and plays a critical role in eliciting antiviral immune responses. Moreover, MEX3C plays an essential role in normal postnatal growth via enhancing the local expression of insulin-like growth factor 1 (IGF1) in bone. It may also be involved in metabolic regulation of energy balance. MEX3C contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3C shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway
KHDCVICFENEVIAALVPCGHNLFCMECANKICEKETPSCPVCQTAVTQAIQIHS
>gnl|CDD|438383 cd16723, RING-HC_MEX3D, RING finger, HC subclass, found in RNA-binding protein MEX3D. MEX3D, also known as RING finger and KH domain-containing protein 1 (RKHD1), RING finger protein 193 (RNF193), or TINO, is an RNA-binding phosphoprotein that controls the stability of the transcripts coding for the anti-apoptotic protein BCL-2, and negatively regulates BCL-2 in HeLa cells. MEX3D contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3D shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway
SSSDGARKSARECVVCFESEVIAALVPCGHNLFCMECAIRICGKSEPECPACHTPATQAIHIFS
>gnl|CDD|438384 cd16724, RING-HC_MIB1_rpt1, first RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins. MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the first RING-HC finger
EECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK
>gnl|CDD|438385 cd16725, RING-HC_MIB1_rpt2, second RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins. MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the second RING-HC finger
EECVVCSDKKASVLFKPCGHMCACEGCAALMKKCVQCR
>gnl|CDD|438386 cd16726, RING-HC_MIB2_rpt1, first RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins. MIB2, also known as novel zinc finger protein (Novelzin), putative NF-kappa-B-activating protein 002N, skeletrophin, or zinc finger ZZ type with ankyrin repeat domain protein 1, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands. It promotes Delta ubiquitylation and endocytosis in Notch activation. Overexpression of MIB2 activates NF-kappaB and interferon-stimulated response element (ISRE) reporter activity. Moreover, MIB2 acts as a novel component of the activated B-cell CLL/lymphoma 10 (BCL10) complex and controls BCL10-dependent NF-kappaB activation. It also functions as a founder myoblast-specific protein that regulates myoblast fusion and muscle stability. MIB2 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of two C3HC4-type RING-HC fingers. This model corresponds to the first RING-HC finger
SECLVCSELAALVRFEPCQHSIVCEECARRMKKCIKCQ
>gnl|CDD|438387 cd16727, RING-HC_MIB1_rpt3, third RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins. MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the third RING-HC finger
TMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIEKRILLY
>gnl|CDD|438388 cd16728, RING-HC_MIB2_rpt2, second RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins. MIB2, also known as novel zinc finger protein (Novelzin), putative NF-kappa-B-activating protein 002N, skeletrophin, or zinc finger ZZ type with ankyrin repeat domain protein 1, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands. Especially, it promotes Delta ubiquitylation and endocytosis in Notch activation. Overexpression of MIB2, activates NF-kappaB and interferon-stimulated response element (ISRE) reporter activity. Moreover, MIB2 acts as a novel component of the activated B-cell CLL/lymphoma 10 (BCL10) complex and controls BCL10-dependent NF-kappaB activation. It also functions as a founder myoblast-specific protein that regulates myoblast fusion and muscle stability. MIB2 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of two C3HC4-type RING-HC fingers. This model corresponds to the second RING-HC finger
MEERITCPICIDNHIKLVFQCGHGSCIECSSALKACPICRQAIRERIQIFV
>gnl|CDD|438389 cd16729, RING-HC_RGLG_plant, RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from plant. RGLG1 is a ubiquitously expressed E3 ubiquitin-protein ligase that interacts with UBC13 and, together with UBC13, catalyzes the formation of K63-linked polyubiquitin chains, which is involved in DNA damage repair. RGLG1 mediates the formation of canonical, K48-linked polyubiquitin chains that target proteins for degradation. It also regulates apical dominance by acting on the auxin transport proteins abundance. RGLG1 has overlapping functions with its closest sequelog, RGLG2. They both function as RING E3 ligases that interact with ethylene response factor 53 (ERF53) in the nucleus and negatively regulate the plant drought stress response. Members of this subfamily contain a Von Willebrand factor type A (vWA) domain and a C3HC4-type RING-HC finger
DDQLCPICLSNPKDMAFGCGHQTCCECGQSLTHCPICRQPITTRIKLY
>gnl|CDD|319644 cd16730, RING-HC_MKRN1_3, RING finger, HC subclass, found in makorin-1 (MKRN1), makorin-3 (MKRN3), and similar proteins. MKRN1, also known as makorin RING finger protein 1 or RING finger protein 61 (RNF61), is an E3 ubiquitin-protein ligase targeting the telomerase catalytic subunit (TERT) for proteasome processing. It regulates the ubiquitination and degradation of peroxisome-proliferator-activated receptor gamma (PPARgamma), a nuclear receptor that is linked to obesity and metabolic diseases. It also mediates the posttranslational regulation of p14ARF, and thus potentially regulates cellular senescence and tumorigenesis in gastric cancer. Moreover, MKRN1 functions as a differentially negative regulator of p53 and p21, and controls cell cycle arrest and apoptosis. It induces degradation of West Nile virus (WNV) capsid protein to protect cells from WNV. It is a RNA-binding protein involved in the modulation of cellular stress and apoptosis. It predominantly associates with proteins involved in mRNA metabolism including regulators of mRNA turnover, transport, and/or translation, and acts as a component of a ribonucleoprotein complex in embryonic stem cells (ESCs) that is recruited to stress granules upon exposure to environmental stress. MKRN1 interacts with poly(A)-binding protein (PABP), a key component of different ribonucleoprotein complexes, in an RNA-independent manner, and stimulates translation in nerve cells. In addition, MKRN1 is a novel SEREX (serological identification of antigens by recombinant cDNA expression cloning) antigen of esophageal squamous cell carcinoma (SCC). It may be involved in carcinogenesis of the well-differentiated type of tumors possibly via ubiquitination of filamin A interacting protein 1 (L-FILIP). Human MKRN1 contains three N-terminal C3H1-type zinc fingers, a motif rich in Cys and His residues (CH), a C3HC4-type RING-HC finger, and another C3H1-type zinc finger at the C-terminus. MKRN3, also known as makorin RING finger protein 3, RING finger protein 63 (RNF63), or zinc finger protein 127 (ZNF127), is a therian mammal-specific retrocopy of MKRN1. It acts as a putative E3 ubiquitin-protein ligase involved in ubiquitination and cell signaling. MKRN3 shows a potential inhibitory effect on hypothalamic gonadotropin-releasing hormone (GnRH) secretion. Its defects represent the most frequent known genetic cause of familial central precocious puberty (CPP). In contrast to human MKRN1, human MKRN3 lacks the second C3H1-type zinc finger at the N-terminal region. The RING-HC finger of mammalian MKRN4 shows high sequence similarity with that of MKRN3, and is also included in this model
DKVCGICMEVVYEKANPSERRFGILSNCNHTYCLKCIRKWRSAKQFESKIIKSCPECRITS
>gnl|CDD|319645 cd16731, RING-HC_MKRN2, RING finger, HC subclass, found in makorin-2 (MKRN2) and similar proteins. MKRN2, also known as makorin RING finger protein 2, RING finger protein 62 (RNF62), or HSPC070, is a putative ribonucleoprotein that acts as a neurogenesis inhibitor acting upstream of glycogen synthase kinase-3beta (GSK-3beta) in the phosphatidylinositol 3-kinase (PI3K)/Akt pathway. It also functions in promoting cell proliferation of primary CD34+ progenitor cells and K562 cells, indicating its possible involvement in normal and malignant hematopoiesis. Mammalian MKRN2 contains three N-terminal C3H1-type zinc fingers, a motif rich in Cys and His residues (CH), a C3HC4-type RING-HC finger, and another C3H1-type zinc finger at the C-terminus. The third C3H1-type zinc finger, the CH motif, as well as the RING zinc finger are necessary for its anti-neurogenic activity
DKVCSICMEVVYEKASASERRFGILSNCNHTYCLSCIRQWRCAKQFENPIIKSCPECR
>gnl|CDD|438390 cd16732, RING-HC_MKRN4, RING finger, HC subclass, found in makorin-4 (MKRN4) and similar proteins. MKRN4, also known as makorin RING finger protein pseudogene 4, makorin RING finger protein pseudogene 5, RING finger protein 64 (RNF64), zinc finger protein 127-Xp (ZNF127-Xp), or zinc finger protein 127-like 1, is a new divergent member of the makorin protein family in vertebrates. It may have an ancestral gonad-specific function and maternal embryonic expression before duplication in vertebrates. MKRN4 contains typical arrays of one to four C3H1-type zinc fingers, a motif rich in Cys and His residues (CH) and a C3HC4-type RING-HC finger. The RING-HC finger of mammalian MKRN4 shows high sequence similarity with that of MKRN3, and is not included in this model
DVACGICMDKVYEKAHAKERVFGILPNCNHAFCVGCIKKWRKSKDFQNEVIKACPQCRVKS
>gnl|CDD|438391 cd16733, RING-HC_PCGF1, RING finger, HC subclass, found in polycomb group RING finger protein 1 (PCGF1) and similar proteins. PCGF1, also known as nervous system Polycomb-1 (NSPc1) or RING finger protein 68 (RNF68), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a noncanonical Polycomb repressive complex 1 (PRC1)-like BCOR complex that also contains RING1, RNF2, RYBP, SKP1, as well as the BCL6 co-repressor BCOR and the histone demethylase KDM2B, and is required to maintain the transcriptionally repressive state of some genes, such as Hox genes, BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. PCGF1 promotes cell cycle progression and enhances cell proliferation as well. It is a cell growth regulator that acts as a transcriptional repressor of p21Waf1/Cip1 via the retinoid acid response element (RARE element). Moreover, PCGF1 functions as an epigenetic regulator involved in hematopoietic cell differentiation. It cooperates with the transcription factor runt-related transcription factor 1 (Runx1) in regulating differentiation and self-renewal of hematopoietic cells. Furthermore, PCGF1 represents a physical and functional link between Polycomb function and pluripotency. PCGF1 contains a C3HC4-type RING-HC finger
VKIKDLNEHIVCYLCAGYFIDATTITECLHTFCKSCIVKYLQTSKYCPMCNIKIHETQPLLNLKLDRVMQ
D
>gnl|CDD|438392 cd16734, RING-HC_PCGF2, RING finger found in polycomb group RING finger protein 2 (PCGF2) and similar proteins. PCGF2, also known as DNA-binding protein Mel-18, RING finger protein 110 (RNF110), or zinc finger protein 144 (ZNF144), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a canonical Polycomb repressive complex 1 (PRC1), which is composed of a chromodomain-containing protein (CBX2, CBX4, CBX6, CBX7 or CBX8) and a Polyhomeotic protein (PHC1, PHC2, or PHC3). Like other PCGF homologs, PCGF2 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF2 uniquely regulates PRC1 to specify mesoderm cell fate in embryonic stem cells. It is required for PRC1 stability and maintenance of gene repression in embryonic stem cells (ESCs) and essential for ESC differentiation into early cardiac-mesoderm precursors. PCGF2 also plays a significant role in the angiogenic function of endothelial cells (ECs) by regulating endothelial gene expression. Furthermore, PCGF2 is a SUMO-dependent regulator of hormone receptors. It facilitates the deSUMOylation process by inhibiting PCGF4/BMI1-mediated ubiquitin-proteasomal degradation of SUMO1/sentrin-specific protease 1 (SENP1). It is also a novel negative regulator of breast cancer stem cells (CSCs) that inhibits the stem cell population and in vitro and in vivo self-renewal through the inactivation of Wnt-mediated Notch signaling. PCGF2 contains a C3HC4-type RING-HC finger
HRTTRIKITELNPHLMCALCGGYFIDAATIVECLHSFCKTCIVRYLETNKYCPMCDVQVHKTRPLLSIRS
DKTLQDIVYK
>gnl|CDD|438393 cd16735, RING-HC_PCGF3, RING finger found in polycomb group RING finger protein 3 (PCGF3) and similar proteins. PCGF3, also known as RING finger protein 3A (RNF3A), is one of six PcG RING finger (PCGF) homologs (PCGF1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6) and serves as the core component of a Polycomb repressive complex 1 (PRC1). Like other PCGF homologs, PCGF3 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. PCGF3 contains a C3HC4-type RING-HC finger
RKIRLKDLNAHITCRLCKGYLIDATTITECLHTFCKSCLVKYLEENNTCPTCGIVIHQSHPLQYIG
>gnl|CDD|438394 cd16736, RING-HC_PCGF4, RING finger found in polycomb group RING finger protein 4 (PCGF4) and similar proteins. PCGF4, also known as polycomb complex protein BMI-1 (B cell-specific Moloney murine leukemia virus integration site 1) or RING finger protein 51 (RNF51), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a canonical Polycomb repressive complex 1 (PRC1), which is composed of a chromodomain-containing protein (CBX2, CBX4, CBX6, CBX7 or CBX8) and a Polyhomeotic protein (PHC1, PHC2, or PHC3), and plays important roles in chromatin compaction and H2AK119 monoubiquitination. PCGF4 associates with the Runx1/CBFbeta transcription factor complex to silence target genes in a PRC2-independent manner. Moreover, PCGF4 is expressed in the hair cells and supporting cells. It can regulate cell survival by controlling mitochondrial function and reactive oxygen species (ROS) level in thymocytes and neurons, thus having an important role in the survival and sensitivity to ototoxic drug of auditory hair cells. Furthermore, PCGF4 controls memory CD4 T-cell survival through direct repression of Noxa gene in an Ink4a- and Arf-independent manner. It is required in neurons to suppress p53-induced apoptosis via regulating the antioxidant defensive response, and also involved in the tumorigenesis of various cancer types. PCGF4 contains a C3HC4-type RING-HC finger
TRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKT
LQDIVYKLVPGLFKNEMKRRRDFYAAH
>gnl|CDD|438395 cd16737, RING-HC_PCGF5, RING finger found in polycomb group RING finger protein 5 (PCGF5) and similar proteins. PCGF5, also known as RING finger protein 159 (RNF159), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) and serves as the core component of a Polycomb repressive complex 1 (PRC1). Like other PCGF homologs, PCGF5 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. PCGF5 contains a C3HC4-type RING-HC finger
KHLVRDFNPYITCRICKGYLIKPTTVTECLHTFCKSCIVQHFEDSNDCPECGIQVHETNPLEMLRLDNTL
EEIIFKLVPGLRERELQREAEFWEK
>gnl|CDD|438396 cd16738, RING-HC_PCGF6, RING finger found in polycomb group RING finger protein 6 (PCGF6) and similar proteins. PCGF6, also known as Mel18 and Bmi1-like RING finger (MBLR), or RING finger protein 134 (RNF134), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a noncanonical Polycomb repressive complex 1 (PRC1)-like L3MBTL2 complex, which is composed of some canonical components, such as RNF2, CBX3, CXB4, CXB6, CXB7, and CXB8, as well as some noncanonical components, such as L3MBTL2, E2F6, WDR5, HDAC1, and RYBP, and plays a critical role in epigenetic transcriptional silencing in higher eukaryotes. Like other PCGF homologs, PCGF6 possesses the transcriptional repression activity, and also associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF6 can regulate the enzymatic activity of JARID1d/KDM5D, a trimethyl H3K4 demethylase, through direct interaction. Furthermore, PCGF6 is expressed predominantly in meiotic and post-meiotic male germ cells and may play important roles in mammalian male germ cell development. It also regulates mesodermal lineage differentiation in mammalian embryonic stem cells (ESCs) and functions in induced pluripotent stem (iPS) reprogramming. The activity of PCGF6 is found to be regulated by cell cycle dependent phosphorylation. PCGF6 contains a C3HC4-type RING-HC finger
LAELNPYILCSICKGYFIDATTITECLHTFCKSCIVRHFYYSNRCPKCNIVVHQTQPLY
>gnl|CDD|438397 cd16739, RING-HC_RING1, RING finger, HC subclass, found in really interesting new gene 1 protein (RING1) and similar proteins. RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), was identified as a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. It is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase that transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING1 interacts with multiple PcG proteins and displays tumorigenic activity. It also shows zinc-dependent DNA binding activity. Moreover, RING1 inhibits transactivation of the DNA-binding protein recombination signal binding protein-Jkappa (RBP-J) by Notch through interaction with the LIM domains of KyoT2. RING1 contains a C3HC4-type RING-HC finger
HSELMCPICLDMLKNTMTTKECLHRFCSDCIVTALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYP
>gnl|CDD|438398 cd16740, RING-HC_RING2, RING finger, HC subclass, found in really interesting new gene 2 protein (RING2) and similar proteins. RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. RING2 is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. The enzymatic activity of RING2 is enhanced by the interaction with BMI1/PCGF4, and it is dispensable for early embryonic development and much of the gene repression activity of PRC1. Moreover, RING2 plays a key role in terminating neural precursor cell (NPC)-mediated production of subcerebral projection neurons (SCPNs) during neocortical development. It also plays a critical role in nonhomologous end-joining (NHEJ)-mediated end-to-end chromosome fusions. Furthermore, RING2 is essential for expansion of hepatic stem/progenitor cells. It promotes hepatic stem/progenitor cell expansion through simultaneous suppression of cyclin-dependent kinase inhibitors (CDKIs) Cdkn1a and Cdkn2a, known negative regulators of cell proliferation. RING2 also negatively regulates p53 expression through directly binding with both p53 and MDM2 and promoting MDM2-mediated p53 ubiquitination in selective cancer cell types to stimulate tumor development. RING2 contains a C3HC4-type RING-HC finger
EIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNF
DALISKI
>gnl|CDD|438399 cd16741, RING-HC_RNFT1, RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 (RNFT1). RNFT1, also known as protein PTD016, is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear
YGIAASKRQCSEADDICAICQAEFRKPILLICQHVFCEECISLWFNREKTCPLCRTVI
>gnl|CDD|438400 cd16742, RING-HC_RNFT2, RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2(RNFT2). RNFT2, also known as transmembrane protein 118 (TMEM118), is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear
GVRATSQQCSEAGDICAICQAEFREPLILICQHVFCEECLCLWFDRERTCPLCRSVVVETLRCWKDG
>gnl|CDD|438401 cd16743, RING-HC_RNF5, RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins. RNF5, also known as protein G16 or Ram1, is an E3 ubiquitin-protein ligase anchored to the outer membrane of the endoplasmic reticulum (ER). It acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. It also regulates the turnover of specific G protein-coupled receptors by ubiquitinating JNK-associated membrane protein (JAMP) and preventing proteasome recruitment. RNF5 limits basal levels of autophagy and influences susceptibility to bacterial infection through the regulation of ATG4B stability. It is also involved in the degradation of Pendrin, a transmembrane chloride/anion exchanger highly expressed in thyroid, kidney, and inner ear. RNF5 plays an important role in cell adhesion and migration. It can modulate cell migration by ubiquitinating paxillin. Furthermore, RNF5 interacts with virus-induced signaling adaptor (VISA) at mitochondria in a viral infection-dependent manner, and further targets VISA at K362 and K461 for K48-linked ubiquitination and degradation after viral infection. It also negatively regulates virus-triggered signaling by targeting MITA, also known as STING, for ubiquitination and degradation at the mitochondria. In addition, RNF5 determines breast cancer response to ER stress-inducing chemotherapies through the regulation of the L-glutamine carrier proteins SLC1A5 and SLC38A2 (SLC1A5/38A2). It also has been implicated in muscle organization and in recognition and processing of misfolded proteins. RNF5 contains a C3HC4-type RING-HC finger
FECNICLETARDAVVSLCGHLFCWPCLHQWLETRPERQECPVCKAGISRDKVIP
>gnl|CDD|438402 cd16744, RING-HC_RNF185, RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins. RNF185 is an E3 ubiquitin-protein ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR). It controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical ERAD model substrates. It also negatively regulates osteogenic differentiation by targeting dishevelled2 (Dvl2), a key mediator of the Wnt signaling pathway, for degradation. Moreover, RNF185 regulates selective mitochondrial autophagy through interaction with the Bcl-2 family protein BNIP1. It also plays an important role in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. RNF185 contains a C3HC4-type RING-HC finger
FECNICLDTAKDAVVSLCGHLFCWPCLHQWLETRPNRQVCPVCKAGISRDKVIPLYG
>gnl|CDD|438403 cd16745, RING-HC_AtRMA-like, RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) and similar proteins. AtRMAs, including AtRma1, AtRma2, and AtRma3, are endoplasmic reticulum (ER)-localized Arabidopsis homologs of human outer membrane of the ER-anchor E3 ubiquitin-protein ligase, RING finger protein 5 (RNF5). AtRMAs possess E3 ubiquitin ligase activity, and may play a role in the growth and development of Arabidopsis. The AtRMA1 and AtRMA3 genes are predominantly expressed in major tissues, such as cotyledons, leaves, shoot-root junction, roots, and anthers, while AtRMA2 expression is restricted to the root tips and leaf hydathodes. AtRma1 probably functions with the Ubc4/5 subfamily of E2. AtRma2 is likely involved in the cellular regulation of ABP1 expression levels through interacting with auxin binding protein 1 (ABP1). AtRMA proteins contain an N-terminal C3HC4-type RING-HC finger and a trans-membrane-anchoring domain in their extreme C-terminal region
FECNICLDLAQDPVVTLCGHLFCWPCLHKWLRRQSSQPECPVCKA
>gnl|CDD|438404 cd16746, RING-HC_RNF212, RING finger, HC subclass, found in RING finger protein 212 (RNF212) and similar proteins. RNF212 is a dosage-sensitive regulator of crossing-over during mammalian meiosis. It plays a central role in designating crossover sites and coupling chromosome synapsis to the formation of crossover-specific recombination complexes. It also functions as an E3 ligase for SUMO modification. RNF212 contains an N-terminal C3HC4-type RING-HC finger
RVFCNFCFQQPRPNCPSFILTNCGHVVCEACLQKGKKNECLVCKAPCR
>gnl|CDD|438405 cd16747, RING-HC_RNF212B, RING finger, HC subclass, found in RING finger protein 212B (RNF212B) and similar proteins. RNF212B is an uncharacterized protein with high sequence similarity with RNF212, a dosage-sensitive regulator of crossing-over during mammalian meiosis. RNF212B contains an N-terminal C3HC4-type RING-HC finger
FHCNKCFRRDGASFFITSCGHIFCEKCIKAEKCTVCG
>gnl|CDD|438406 cd16748, RING-HC_SH3RF1, RING finger, HC subclass, found in SH3 domain-containing RING finger protein 1 (SH3RF1) and similar proteins. SH3RF1, also known as plenty of SH3s (POSH), RING finger protein 142 (RNF142), or SH3 multiple domains protein 2 (SH3MD2), is a trans-Golgi network-associated pro-apoptotic scaffold protein with E3 ubiquitin-protein ligase activity. It also plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and c-Jun N-terminal kinase (JNK) mediated apoptosis, linking Rac1 to downstream components. SH3RF1 also enhances the ubiquitination of ROMK1 potassium channel resulting in its increased endocytosis. Moreover, SH3RF1 assembles an inhibitory complex with the actomyosin regulatory protein Shroom3, which links to the actin-myosin network to regulate neuronal process outgrowth. It also forms a complex with apoptosis-linked gene-2 (ALG-2) and ALG-2-interacting protein (ALIX/AIP1) in a calcium-dependent manner to play a role in the regulation of the JNK pathway. Furthermore, direct interaction of SH3RF1 and another molecular scaffold JNK-interacting protein (JIP) is required for apoptotic activation of JNKs. Interaction of SH3RF1 and E3 ubiquitin-protein isopeptide ligases, Siah proteins, further promotes JNK activation and apoptosis. In addition, SH3RF1 binds to and degrades TAK1, a crucial activator of both the JNK and the Relish signaling pathways. SH3RF1 contains an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs
DLLECPVCLERLDATAKVLPCQHTFCRRCLLGIVGSRSELRCPECRTL
>gnl|CDD|438407 cd16749, RING-HC_SH3RF2, RING finger, HC subclass, found in SH3 domain-containing RING finger protein 2 (SH3RF2) and similar proteins. SH3RF2, also known as heart protein phosphatase 1-binding protein (HEPP1), plenty of SH3s (POSH)-eliminating RING protein (POSHER), protein phosphatase 1 regulatory subunit 39, or RING finger protein 158 (RNF158), is a putative E3 ubiquitin-protein ligase that acts as an anti-apoptotic regulator for the c-Jun N-terminal kinase (JNK) pathway by binding to and promoting the proteasomal degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs
LECPVCFEKLDVTAKVLPCQHTFCKPCLQRIFKARKELRCPECRTP
>gnl|CDD|438408 cd16750, RING-HC_SH3RF3, RING finger, HC subclass, found in SH3 domain-containing RING finger protein 3 (SH3RF3) and similar proteins. SH3RF3, also known as plenty of SH3s 2 (POSH2) or SH3 multiple domains protein 4 (SH3MD4), is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in a screen for interacting partners of p21-activated kinase 2 (PAK2). It may play a role in regulating c-Jun N-terminal kinase (JNK) mediated apoptosis in certain conditions. It also interacts with GTP-loaded Rac1. SH3RF3 is highly homologous to SH3RF1. Both contain an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs
DLLECSVCLERLDTTSKVLPCQHTFCRRCLESIVSSRKELRCPECR
>gnl|CDD|438409 cd16751, RING-HC_SIAH1, RING finger, HC subclass, found in seven in absentia homolog 1 (SIAH1) and similar proteins. SIAH1, also known as Siah-1a, is an inducible E3 ubiquitin-protein ligase that contributes to proteasome-mediated degradation of multiple targets in numerous cellular processes including apoptosis, tumor suppression, cell cycle, axon guidance, transcription regulation, and tumor necrosis factor signaling. SIAH1 functions as a scaffolding protein and interacts with a variety of different substrates for ubiquitination and subsequent degradation. It regulates the oncoprotein p34SEI-1 polyubiquitination and its subsequent degradation in a p53-dependent manner, which mediates p53 preferential vitamin C cytotoxicity. It targets the nonreceptor tyrosine kinase activated Cdc42-associated kinase 1 (ACK1), a valid target in cancer therapy, for ubiquitinylation and proteasomal degradation. It also interacts with KLF10 and targets it for degradation. The CDK2 phosphorylation-mediated KLF10 dissociation from SIAH1 is linked to cell cycle progression. Moreover, SIAH1 is downregulated and associated with apoptosis and invasion in human breast cancer. It targets TAp73, a homolog of the tumor suppressor p53, for degradation. It is suppressed by hypoxia-inducible factor 1-alpha (HIF-1alpha) under hypoxic conditions to regulate TAp73 levels. It also promotes the migration and invasion of human glioma cells by regulating HIF-1alpha signaling under hypoxia. Furthermore, SIAH1 forms a protein complex with glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The apoptosis signal-regulating kinase 1 (ASK1) functions as an activator of the GAPDH-Siah1 stress-signaling cascade. It also plays an important role in ethanol-induced apoptosis in neural crest cells (NCCs). SIAH1 contains an N-terminal C3HC4-type RING-HC finger, two zinc-finger subdomains, and a C-terminal tumor necrosis factor (TNF) receptor associated factor (TRAF)-like substrate-binding domain (SBD) responsible for dimer formation
DLASLFECPVCFDYVLPPILQCQSGHLVCSNCRPKLTCCPTCRGP
>gnl|CDD|438410 cd16752, RING-HC_SIAH2, RING finger, HC subclass, found in seven in absentia homolog 2 (SIAH2) and similar proteins. SIAH2 is an E3 ubiquitin-protein ligase that contributes to proteasome-mediated degradation of multiple targets in numerous cellular processes. It targets the ubiquitylation and degradation of tumor necrosis factor receptor-associated factor 2 (TRAF2) under stress conditions, which is required for the cell to commit to undergoing apoptosis. It is, therefore, a key regulator of TRAF2-dependent signaling in response to tumor necrosis factor-alpha (TNF-alpha) treatment and UV irradiation. SIAH2 modulates the polyubiquitination of G protein pathway suppressor 2 (GPS2), and targets it for proteasomal degradation. It is also a regulator of NF-E2-related factor 2 (Nrf2), a key regulator of cellular oxidative response, and contributes to the degradation of Nrf2 irrespective of its phosphorylation status. Moreover, SIAH2 contributes to castration-resistant prostate cancer (CRPC) by regulation of androgen receptor (AR) transcriptional activity. It enhances AR transcriptional activity and prostate cancer cell growth. Its stability can be regulated by AKR1C3. SIAH2 also inhibits tyrosine kinase-2 (TYK2)-STAT3 signaling in lung carcinoma cells. Furthermore, SIAH2 regulates obesity-induced adipose tissue inflammation by altering peroxisome proliferator-activated receptor gamma (PPAR gamma) protein levels and selectively regulating PPAR gamma activity. It also functions as a regulator of the nuclear hormone receptor RevErbalpha (Nr1d1) stability and rhythmicity, and overall circadian oscillator function. In addition, SIAH2 is an essential component of the hypoxia response Hippo signaling pathway and has been implicated in normal development and tumorigenesis. It modulates the hypoxia pathway upstream of hypoxia-induced transcription factor subunit HIF-1alpha, and therefore may play an important role in angiogenesis in response to hypoxic stress in endothelial cells. It also stimulates transcriptional coactivator YAP1 by destabilizing serine/threonine-protein kinase LATS2, a critical component of the Hippo pathway, in response to hypoxia. Meanwhile, SIAH2 is involved in regulation of tight junction integrity and cell polarity under hypoxia, through its regulation of apoptosis-stimulating proteins of p53 subunit 2 (ASPP2) stability. SIAH2 contains an N-terminal C3HC4-type RING-HC finger, two zinc-finger subdomains, and a C-terminal tumor necrosis factor (TNF) receptor associated factor (TRAF)-like substrate-binding domain (SBD) responsible for dimer formation
TSLFECPVCFDYVLPPILQCQAGHLVCNQCRQKLSCCPTCRGPLTPSIRNL
>gnl|CDD|438411 cd16753, RING-HC_MID1, RING finger, HC subclass, found in midline-1 (MID1) and similar proteins. MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. It monoubiquinates the alpha4 subunit of protein phosphatase 2A (PP2A), promoting proteosomal degradation of the catalytic subunit of PP2A (PP2Ac) and preventing the A and B subunits from forming an active complex. It promotes allergen and rhinovirus-induced asthma through the inhibition of PP2A activity. It is strongly upregulated in cytotoxic lymphocytes (CTLs) and directs lytic granule exocytosis and cytotoxicity of killer T cells. Loss-of-function mutations in MID1 lead to the human X-linked Opitz G/BBB (XLOS) syndrome characterized by defective midline development during embryogenesis. MID1 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. MID1 hetero-dimerizes in vitro with its paralog MID2
TLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCASNESVESITAFQCPTCRYVITLNQRGLEG
LK
>gnl|CDD|438412 cd16754, RING-HC_MID2, RING finger, HC subclass, found in midline-2 (MID2) and similar proteins. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is a probable E3 ubiquitin-protein ligase and is highly related to MID1 that associates with cytoplasmic microtubules along their length and throughout the cell cycle. Like MID1, MID2 associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. MID2 can also substitute for MID1 to control exocytosis of lytic granules in cytotoxic T cells. Loss-of-function mutations in MID2 lead to the human X-linked intellectual disability (XLID). MID2 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxy-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. MID2 hetero-dimerizes in vitro with its paralog MID1
METLESELTCPICLELFEDPLLLPCAHSLCFSCAHRILTSGCASGESIEPPSAFQCPTCRYVISLNHRGL
>gnl|CDD|438413 cd16755, RING-HC_TRIM9, RING finger, HC subclass, found in tripartite motif-containing protein 9 (TRIM9) and similar proteins. TRIM9, human ortholog of rat Spring, also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in the neurodegenerative disorders through its ligase activity. It interacts with the WD repeat region of beta-transducin repeat-containing protein (beta-TrCP) through its N-terminal degron motif depending on the phosphorylation status, and thus negatively regulates nuclear factor-kappaB (NF-kappaB) activation in the NF-kappaB pro-inflammatory signaling pathway. Moreover, TRIM9 acts as a critical catalytic link between Netrin-1 and the exocytic soluble NSF attachment receptor protein (SNARE) machinery in murine cortical neurons. It promotes SNARE-mediated vesicle fusion and axon branching in a Netrin-dependent manner. TRIM9 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
EEELKCPVCGSFYREPIILPCSHNLCLACARNILVQTPEAESPQSCLTCPQCHRS
>gnl|CDD|438414 cd16756, RING-HC_TRIM36_C-I, RING finger, HC subclass, found in tripartite motif-containing protein 36 (TRIM36) and similar proteins. TRIM36, the human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequently dorsal axis formation. It is also potentially associated with chromosome segregation by interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM36 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
ERELICPSCKELFTHPLILPCQHSVCHKCVKELLTTFPCPGCQHDVDLG
>gnl|CDD|438415 cd16757, RING-HC_TRIM46_C-I, RING finger, HC subclass, found in tripartite motif-containing protein 46 (TRIM46) and similar proteins. TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that specifically localizes to the proximal axon, partly overlaps with the axon initial segment (AIS) at later stages, and organizes uniform microtubule orientation in axons. It controls neuronal polarity and axon specification by driving the formation of parallel microtubule arrays. TRIM46 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins, which are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
MERELLCPVCKEMYKQPLVLPCMHNVCQVCASEVLFPCPPCQR
>gnl|CDD|438416 cd16758, RING-HC_TRIM67, RING finger, HC subclass, found in tripartite motif-containing protein 67 (TRIM67) and similar proteins. TRIM67, also known as TRIM9-like protein (TNL), is selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis. TRIM67 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain
EEELKCPVCGSLFREPIILPCSHNVCLPCARTIAVQTPESEQHLPHSSSITCPQCHR
>gnl|CDD|319673 cd16759, RING-HC_MuRF1, RING finger, HC subclass, found in muscle-specific RING finger protein 1 (MuRF-1) and similar proteins. MuRF-1, also known as tripartite motif-containing protein 63 (TRIM63), RING finger protein 28 (RNF28), iris RING finger protein, or striated muscle RING zinc finger, is an E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover. It is predominantly fast (type II) fibre-associated in skeletal muscle and can bind to many myofibrillar proteins, including titin, nebulin, the nebulin-related protein NRAP, troponin-I (TnI), troponin-T (TnT), myosin light chain 2 (MLC-2), myotilin, and T-cap. The early and robust upregulation of MuRF-1 is triggered by disuse, denervation, starvation, sepsis, or steroid administration resulting in skeletal muscle atrophy. It also plays a role in maintaining titin M-line integrity. It associates with the periphery of the M-line lattice and may be involved in the regulation of the titin kinase domain. It also participates in muscle stress response pathways and gene expression. MuRF-1 belongs to the C-II subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains
EKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWQSRGTSMLGSGGRFRCPSCRH
>gnl|CDD|438417 cd16760, RING-HC_MuRF2, RING finger, HC subclass, found in muscle-specific RING finger protein 2 (MuRF-2) and similar proteins. MuRF-2, also known as tripartite motif-containing protein 55 (TRIM55) or RING finger protein 29 (RNF29), is a muscle-specific E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover and is also a ligand of the transactivation domain of the serum response transcription factor (SRF). It is predominantly slow-fibre associated and highly expressed in embryonic skeletal muscle. MuRF-2 associates transiently with microtubules, myosin, and titin during sarcomere assembly. It has been implicated in microtubule, intermediate filament, and sarcomeric M-line maintenance in striated muscle development, as well as in signaling from the sarcomere to the nucleus. It plays an important role in the earliest stages of skeletal muscle differentiation and myofibrillogenesis. It is developmentally downregulated and is assembled at the M-line region of the sarcomere and with microtubules. MuRF-2 belongs to the C-II subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains
EKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQASNPYLPTRGGTTVASGGRFRCPSCRHE
>gnl|CDD|319675 cd16761, RING-HC_MuRF3, RING finger, HC subclass, found in muscle-specific RING finger protein 3 (MuRF-3) and similar proteins. MuRF-3, also known as tripartite motif-containing protein 54 (TRIM54), or RING finger protein 30 (RNF30), is an E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover. It is ubiquitously detected in all fibre types, is developmentally upregulated, associates with microtubules, the sarcomeric M-line and Z-line, and is required for microtubule stability and myogenesis. It associates with glutamylated microtubules during skeletal muscle development, and is required for skeletal myoblast differentiation and development of cellular microtubular networks. MuRF-3 controls the degradation of four-and-a-half LIM domain (FHL2) and gamma-filamin and is required for maintenance of ventricular integrity after myocardial infarction (MI). MuRF-3 belongs to the C-II subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains
LICPICLEMFTKPVVILPCQHNLCRKCANDVFQASNPLWQSRGSSTVSSGGRFRCPSCR
>gnl|CDD|438418 cd16762, RING-HC_TRIM13_C-V, RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar proteins. TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). It also targets the known ER proteolytic substrate CD3-delta, but not the N-end rule substrate Ub-R-YFP (yellow fluorescent protein) for degradation. Moreover, TRIM13 regulates ubiquitination and degradation of NEMO to suppress tumor necrosis factor (TNF) induced nuclear factor-kappaB (NF- kappa B) activation. It is also involved in NF-kappaB p65 activation and nuclear factor of activated T-cells (NFAT)-dependent activation of c-Rel upon T-cell receptor engagement. Furthermore, TRIM13 negatively regulates melanoma differentiation-associated gene 5 (MDA5)-mediated type I interferon production. It also regulates caspase-8 ubiquitination, translocation to autophagosomes, and activation during ER stress induced cell death. Meanwhile, TRIM13 enhances ionizing radiation-induced apoptosis by increasing p53 stability and decreasing AKT kinase activity through MDM2 and AKT degradation. TRIM13 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region. In addition, TRIM13 contains a C-terminal transmembrane domain
EEDLTCPICCCLFDDPRVLPCSHNFCKKCLEGILEGNVRTMLWRPPFKCPTCRKET
>gnl|CDD|438419 cd16763, RING-HC_TRIM59_C-V, RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar proteins. TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis. It is upregulated in gastric cancer and promotes gastric carcinogenesis by interacting with and targeting the P53 tumor suppressor for its ubiquitination and degradation. It also acts as a novel accessory molecule involved in cytotoxicity of BCG-activated macrophages (BAM). Moreover, TRIM59 may serve as a multifunctional regulator for innate immune signaling pathways. It interacts with ECSIT and negatively regulates nuclear factor-kappaB (NF- kappa B) and interferon regulatory factor (IRF)-3/7-mediated signal pathways. TRIM59 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region. In addition, TRIM59 contains a C-terminal transmembrane domain
EEDLTCSVCYSLFEDPRVLPCSHTFCRNCLENILQVSGNFSIWRPLRPPLKCPNCR
>gnl|CDD|438420 cd16764, RING-HC_TIF1alpha, RING finger, HC subclass, found in transcription inknown asiary factor 1-alpha (TIF1-alpha). TIF1-alpha, also known as tripartite motif-containing protein 24 (TRIM24), E3 ubiquitin-protein ligase TRIM24, or RING finger protein 82, belongs to the C-VI subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. It interacts specifically and in a ligand-dependent manner with the ligand binding domain (LBD) of several nuclear receptors (NRs), including retinoid X (RXR), retinoic acid (RAR), vitamin D3 (VDR), estrogen (ER), and progesterone (PR) receptors. It also associates with heterochromatin-associated factors HP1alpha, MOD1 (HP1beta), and MOD2 (HP1gamma), as well as the vertebrate Kruppel-type (C2H2) zinc finger proteins that contain the transcriptional silencing domain KRAB. TIF1-alpha is a ligand-dependent co-repressor of RAR that interacts with multiple nuclear receptors in vitro via an LXXLL motif and further acts as a gatekeeper of liver carcinogenesis. It also functions as an E3-ubiquitin ligase targeting p53, and is broadly associated with chromatin silencing. Moreover, it is a chromatin regulator that recognizes specific, combinatorial histone modifications through its C-terminal PHD-Bromo region. In addition, it interacts with chromatin and estrogen receptor to activate estrogen-dependent genes associated with cellular proliferation and tumor development
LDTCGVCKQHIQSREPRLLPCLHSFCQRCLPQPERYLMLPAPFSPSPGPRATSSANRQVGVVRCPVCSQE
C
>gnl|CDD|438421 cd16765, RING-HC_TIF1beta, RING finger, HC subclass, found in transcription inknown asiary factor 1-beta (TIF1-beta). TIF1-beta, also known as Kruppel-associated Box (KRAB)-associated protein 1 (KAP-1), KRAB-interacting protein 1 (KRIP-1), nuclear co-repressor KAP-1, RING finger protein 96, tripartite motif-containing protein 28 (TRIM28), or E3 SUMO-protein ligase TRIM28, belongs to the C-VI subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. It acts as a nuclear co-repressor that plays a role in transcription and in the DNA damage response. Upon DNA damage, the phosphorylation of KAP-1 on serine 824 by the ataxia telangiectasia-mutated (ATM) kinase enhances cell survival and facilitates chromatin relaxation and heterochromatic DNA repair. It also regulates CHD3 nucleosome remodeling during the DNA double-strand break (DSB) response. Meanwhile, KAP-1 can be dephosphorylated by protein phosphatase PP4C in the DNA damage response. Moreover, KAP-1 is a co-activator of the orphan nuclear receptor NGFI-B (or Nur77) and is involved in NGFI-B-dependent transcription. It is also a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase. The N-terminal RBCC domain of TIF1-beta is responsible for the interaction with KRAB zinc finger proteins (KRAB-ZFPs), MDM2, MM1, C/EBPbeta, and the regulation of homo- and heterodimerization. The C-terminal PHD/Bromo domains are involved in interacting with SETDB1, Mi-2alpha and other proteins to form complexes with histone deacetylase or methyltransferase activity
LEHCGVCRERLRPEREPRLLPCLHSVCSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCKQQC
>gnl|CDD|438422 cd16766, RING-HC_TIF1gamma, RING finger, HC subclass, found in transcriptional inknown asiary factor 1 gamma (TIF1gamma). TIF1gamma, also known as tripartite motif-containing 33 (TRIM33), ectodermin, RFG7, or PTC7, belongs to the C-VI subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. It is an E3-ubiquitin ligase that functions as a regulator of transforming growth factor beta (TGFbeta) signaling, inhibiting the Smad4-mediated TGFbeta response by interaction with Smad2/3 or ubiquitylation of Smad4. Moreover, TIF1gamma is an important regulator of transcription during hematopoiesis, as well as a key actor of tumorigenesis. Like other TIF1 proteins, TIF1gamma also contains an intrinsic transcriptional silencing function. It can control erythroid cell fate by regulating transcription elongation. It can bind to the anaphase-promoting complex/cyclosome (APC/C) and promotes mitosis
LLDTCAVCKQSLQSRDAEPKLLPCLHSFCRRCLPEPERQLSVPVPGGSNGDIQQVGVIRCPVCRQEC
>gnl|CDD|438423 cd16767, RING-HC_TRIM2, RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2). TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM2 also plays a role in mediating the p42/p44 MAPK-dependent ubiquitination of the cell death-promoting protein Bcl-2-interacting mediator of cell death (Bim) in rapid ischemic tolerance. TRIM2 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain
QIDKQFLICSICLDRYKNPKVLPCLHTFCERCLQNYIPAHSLTLSCPVCRQ
>gnl|CDD|438424 cd16768, RING-HC_TRIM3, RING finger, HC subclass, found in tripartite motif-containing protein 3 (TRIM3). TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It functions as a tumor suppressor that regulates asymmetric cell division in glioblastoma. It binds to the cdk inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclin D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It is encoded by the gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of postsynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendritic spine morphology. In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain
DKQFLVCSICLDRYHNPKVLPCLHTFCERCLQNYIPPQSLTLSCPVCR
>gnl|CDD|438425 cd16769, RING-HC_UHRF1, RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1). UHRF1, also known as inverted CCAAT box-binding protein of 90 kDa, nuclear protein 95, nuclear zinc finger protein Np95 (Np95), RING finger protein 106, transcription factor ICBP90, or E3 ubiquitin-protein ligase UHRF1, is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 can acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also a N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF1 contains an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) domain, a SET and RING finger associated (SRA) domain, and a C-terminal C3HC4-type RING-HC finger. It specifically binds to hemimethylated DNA, double-stranded CpG dinucleotides, and recruits the maintenance methyltransferase DNMT1 to its hemimethylated DNA substrate through its SRA domain. UHRF1-dependent H3K23 ubiquitylation has an essential role in maintenance DNA methylation and replication. The tandem Tudor domain directs UHRF1 binding to the heterochromatin mark histone H3K9me3 and the PHD domain targets UHRF1 to unmodified histone H3 in euchromatic regions. The RING-HC finger exhibits both autocatalytic E3 ubiquitin (Ub) ligase activity and activity against histone H3 and DNMT1
PFQLFLSKVEETFQCICCQELVFRPITTVCQHNVCKDCLDRSFRAQVFSCPACRYDLGRSYAMQVNQPLQ
TVLNQLFPGYGNGR
>gnl|CDD|438426 cd16770, RING-HC_UHRF2, RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2). UHRF2, also known as Np95/ICBP90-like RING finger protein (NIRF), Np95-like RING finger protein, nuclear protein 97, nuclear zinc finger protein Np97, RING finger protein 107, or E3 ubiquitin-protein ligase UHRF2, was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation, but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) through interacting with HBV core protein and promoting its degradation. UHRF2 contains an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) domain, a SET- and RING-associated (SRA) domain, and a C-terminal C3HC4-type RING-HC finger
EESFLCICCQELVYQPVTTECQHNVCKSCLQRSFKAEVYTCPACRHDLGKNYSMVPNKILQTLLD
>gnl|CDD|438427 cd16771, RING-HC_UNK, RING finger, HC subclass, found in RING finger protein unkempt (UNK) and similar proteins. UNK, also known as zinc finger CCCH domain-containing protein 5, is a metazoan-specific zinc finger protein enriched in embryonic brains. It may play a broad regulatory role during the formation of the central nervous system (CNS). It is a sequence-specific RNA-binding protein required for early neuronal morphology. UNK is a neurogenic component of the mTOR pathway, and functions as a negative regulator of the timing of photoreceptor differentiation. It also specifically binds to Brg/Brm-associated factor BAF60b and promotes its ubiquitination in a Rac1-dependent manner. UNK contains six tandem CCCH-type zinc fingers at the N-terminus, and a C3HC4-type RING-HC finger at its C-terminus
QSVKCLKCQELKRVTLPCQHALLCETCATSEECPICHPHRPH
>gnl|CDD|438428 cd16772, RING-HC_UNKL, RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar proteins. UNKL, also known as zinc finger CCCH domain-containing protein 5-like, is a putative E3 ubiquitin-protein ligase that may participate in a protein complex showing an E3 ligase activity regulated by RAC1. It shows high sequence similarity with RING finger protein unkempt (UNK), which is a metazoan-specific zinc finger protein enriched in embryonic brains, and may play a broad regulatory role during the formation of the central nervous system (CNS). UNKL contains several CCCH-type zinc fingers at the N-terminus, and a C3HC4-type RING-HC finger at its C-terminus
KKCIVCQERDRSIVLQPCQHYVLCEHCAASKPECPYCKTKILKW
>gnl|CDD|438429 cd16773, RING-HC_RBR_TRIAD1, RING finger, HC subclass, found in two RING fingers and DRIL [double RING finger linked] 1 (TRIAD1). TRIAD1, also known as ariadne-2 (ARI-2), protein ariadne-2 homolog, Ariadne RBR E3 ubiquitin protein ligase 2 (ARIH2), or UbcM4-interacting protein 48, is an RBR-type E3 ubiquitin-protein ligase that catalyzes the formation of polyubiquitin chains linked via lysine-48, as well as lysine-63 residues. Its auto-ubiquitylation can be catalyzed by the E2 conjugating enzyme UBCH7. TRIAD1 has been implicated in hematopoiesis, specifically in myelopoiesis, as well as in embryogenesis. It functions as a regulator of endosomal transport and is required for the proper function of multivesicular bodies. It also acts as a novel ubiquitination target for proteasome-dependent degradation by murine double minute 2 (MDM2). As a proapoptotic protein, TRIAD1 promotes p53 activation, and inhibits MDM2-mediated p53 ubiquitination and degradation. Furthermore, TRIAD1 can inhibit the ubiquitination and proteasomal degradation of growth factor independence 1 (Gfi1), a transcriptional repressor essential for the function and development of many different hematopoietic lineages. TRIAD1 contains an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination
VTCGVCCEDVPKDELFSLACGHYFCNDCWKQYLTVKIKDGVSTGIECMAPDCKV
>gnl|CDD|438430 cd16774, RING-HC_RBR_ANKIB1, RING finger, HC subclass, found in ankyrin repeat and IBR domain-containing protein 1 (ANKIB1) and similar proteins. ANKIB1 is an RBR-type E3 ubiquitin-protein ligase that may function as part of an E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. It contains an N-terminal ankyrin repeat domain and an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination
PLCDICMCSISVFEDPVDMPCGHEFCRACWEGYLNLKIQEGEAHNIFCPAYDCFQLVP
>gnl|CDD|438431 cd16775, RING-HC_RBR_RNF19A, RING finger, HC subclass, found in RING finger protein 19A (RNF19A) and similar proteins. RNF19A, also known as double ring-finger protein (Dorfin) or p38, is a transmembrane (TM) domain-containing RBR-type E3 ubiquitin-protein ligase that localizes to the ubiquitylated inclusions in Parkinson's disease (PD), dementia with Lewy bodies, multiple system atrophy, and amyotrophic lateral sclerosis (ALS). It interacts with Psmc3, a protein component of the 19S regulatory cap of the 26S proteasome, and further participates in the ubiquitin-proteasome system in acrosome biogenesis, spermatid head shaping, and development of the head-tail coupling apparatus and tail. It modulates the ubiquitination and degradation of calcium-sensing receptor (CaR), which may contribute to a general mechanism for CaR quality control during biosynthesis. Moreover, RNF19A can also ubiquitylate mutant superoxide dismutase 1 (SOD1), the causative gene of familial ALS. It may associate with endoplasmic reticulum-associated degradation (ERAD) pathway, which is related to the pathogenesis of neurodegenerative disorders, such as PD or Alzheimer's disease. RNF19A contains an RBR domain followed by three TMs. The RBR domain was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination
MECPLCLLRHSKDRFPDIMTCHHRSCADCLRQYLRIEISESRVNISCPECSERFNP
>gnl|CDD|438432 cd16776, RING-HC_RBR_RNF19B, RING finger, HC subclass, found in RING finger protein 19B (RNF19B) and similar proteins. RNF19B, also known as IBR domain-containing protein 3 or natural killer lytic-associated molecule (NKLAM), is a transmembrane (TM) domain-containing RBR-type E3 ubiquitin-protein ligase that plays a role in controlling tumor dissemination and metastasis. It is involved in the cytolytic function of natural killer (NK) cells and cytotoxic T lymphocytes (CTLs). It interacts with ubiquitin conjugates UbcH7 and UbcH8, and ubiquitinates uridine kinase like-1 (URKL-1) protein, targeting it for degradation. Moreover, RNF19B is a novel component of macrophage phagosomes and plays a role in macrophage anti-bacterial activity. It functions as a novel modulator of macrophage inducible nitric oxide synthase (iNOS) expression. RNF19B contains an RBR domain followed by three TMs. The RBR domain was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination
LVECPLCLVRQPPENFPRLLSCSHRSCRDCLRQYLRIEITESRVNIACPECSERLAPNDVRAIL
>gnl|CDD|438433 cd16777, mRING-HC-C4C4_RBR_RNF144A, Modified RING finger, HC subclass (C4C4-type), found in RING finger protein 144A (RNF144A). RNF144A, also known as UbcM4-interacting protein 4 (UIP4) or ubiquitin-conjugating enzyme 7-interacting protein 4, is a transmembrane (TM) domain-containing RBR-type E3 ubiquitin-protein ligase that targets DNA-dependent protein kinase catalytic subunit (DNA-PKcs) and thus promotes DNA damage-induced cell apoptosis. It is transcriptionally repressed by metastasis-associated protein 1 (MTA1) and inhibits MTA1-driven cancer cell migration and invasion. RNF144A contains an RBR domain followed by a potential single-TM domain. The RBR domain was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C4C4-type RING finger whose overall folding is similar to that of the C3HC4-type RING-HC finger. It is responsible for the interaction of E2-conjugating enzymes UbcH7 and UbcH8
VSCKLCLGEYPVEQMTTIAQCQCIFCTLCLKQYVELLIKEGLETAISCPDAACPK
>gnl|CDD|438434 cd16778, mRING-HC-C4C4_RBR_RNF144B, Modified RING finger, HC subclass (C4C4-type), found in RING finger protein 144B (RNF144B). RNF144B, also known as PIR2, IBR domain-containing protein 2 (IBRDC2), or p53-inducible RING finger protein (p53RFP), is a transmembrane (TM) domain-containing RBR (RING1-IBR-RING2) E3 ubiquitin-protein ligase that induces p53-dependent, but caspase-independent apoptosis. It interacts with E2 ubiquitin-conjugating enzymes UbcH7 and UbcH8, but not with UbcH5. It is involved in ubiquitination and degradation of p21, a p53 downstream protein promoting growth arrest and antagonizing apoptosis, suggesting a role in switching a cell from p53-mediated growth arrest to apoptosis. Moreover, RNF144B regulates the levels of Bax, a pro-apoptotic protein from the Bcl-2 family, and protects cells from unprompted Bax activation and cell death. It also regulates epithelial homeostasis by mediating degradation of p21WAF1 and p63. RNF144B contains an RBR domain followed by a potential single-TM domain. The RBR domain was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C4C4-type RING finger whose overall folding is similar to that of the C3HC4-type RING-HC finger. It is required for RBR-mediated ubiquitination
VTCKLCLCEHPFDAMTTLQECDCVFCTPCLKQYVQLAIREGCGSPITCPDMACTKTG
>gnl|CDD|438435 cd16779, mRING-HC-C3HC3D_LNX1, Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 1 (LNX1). LNX1, also known as numb-binding protein 1 or PDZ domain-containing RING finger protein 2, is a PDZ domain-containing RING-type E3 ubiquitin ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX1 contains an N-terminal modified C3HC3D-type RING-HC finger, a NPAY motif for Numb-LNX interaction, and four PDZ domains necessary for the binding of substrates, including CAR, ErbB2, SKIP, JAM4, CAST, c-Src, Claudins, RhoC, KCNA4, PAK6, PLEKHG5, PKC-alpha1, TYK2, PDZ-binding kinase (PBK), LNX2, and itself
DLICHICLQALIQPLDTPCGHTYCTLCLTNFLVEKDFCPMDR
>gnl|CDD|319694 cd16780, mRING-HC-C3HC3D_LNX2, Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 2 (LNX2). LNX2, also known as numb-binding protein 2, or PDZ domain-containing RING finger protein 1 (PDZRN1), is a PDZ domain-containing RING-type E3 ubiquitin ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. It interacts with contactin-associated protein 4 (Caspr4, also known as CNTNAP4) in a PDZ domain-dependent manner, which modulates the proliferation and neuronal differentiation of neural progenitor cells (NPCs). LNX2 contains an N-terminal modified C3HC3D-type RING-HC finger, a NPAF motif for Numb/ Numblike-LNX interaction, and four PDZ domains necessary for the binding of substrates, including ErbB2, RhoC, the presynaptic protein CAST, the melanoma/cancer-testis antigen MAGEB18 and several proteins associated with cell junctions, such as JAM4 and the Coxsackievirus and adenovirus receptor (CAR)
DDDLVCHICLQPLLQPLDTPCGHTFCFKCLRNFLQEKDFCPLDRK
>gnl|CDD|438436 cd16781, mRING-HC-C3HC3D_Roquin1, Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1. Roquin-1, also known as RING finger and C3H zinc finger protein 1 (RC3H1), or RING finger protein 198 (RNF198), is a ubiquitously expressed RNA-binding protein essential for degradation of inflammation-related mRNAs and maintenance of immune homeostasis. It is localized in cytoplasmic granules and binds to the 3' untranslated region (3'UTR) of inducible costimulator (Icos) mRNA to post-transcriptionally repress its expression. Roquin-1 interacts with the 3'UTR of tumor necrosis factor receptor superfamily member 4 (TNFRSF4) and tumor-necrosis factor-alpha (TNFalpha), and post-transcriptionally regulates A20 mRNA and modulates the activity of the IKK/NF-kappaB pathway. Moreover, Roquin-1 shares functions with its paralog Roquin-2 in the repression of mRNAs controlling T follicular helper cells and systemic inflammation. Roquin-1 contains an N-terminal modified C3HC3D-type RING-HC finger with a potential E3 ubiquitin-ligase function, a highly conserved ROQ domain required for RNA binding and localization to stress granules, and a CCCH-type zinc finger that is involved in RNA recognition, typically contacting AU-rich elements. In addition, both N- and C-terminal to the ROQ domain are combined to form a HEPN (higher eukaryotes and prokaryotes nucleotide-binding) domain that is highly likely to function as an RNA-binding domain
PQWTDFLSCPICTQTFDETIRKPISLGCGHTVCKMCLNKLHRKACPFDQ
>gnl|CDD|438437 cd16782, mRING-HC-C3HC3D_Roquin2, Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-2. Roquin-2, also known as membrane-associated nucleic acid-binding protein (MNAB), RING finger and CCCH-type zinc finger domain-containing protein 2 (RC3H2), or RING finger protein 164 (RNF164), is an E3 ubiquitin ligase that is localized to the cytoplasm and upon stress, is concentrated in stress granules. It is required for reactive oxygen species (ROS)-induced ubiquitination and degradation of apoptosis signal-regulating kinase 1 (ASK1, also known as MAP3K5). Roquin-2 interacts with the 3'UTR of tumor necrosis factor receptor superfamily member 4 (TNFRSF4) and tumor-necrosis factor-alpha (TNFalpha), and modulates immune responses. Moreover, Roquin-2 shares functions with its paralog Roquin-1 in the repression of mRNAs controlling T follicular helper cells and systemic inflammation. Roquin-2 contains an N-terminal modified C3HC3D-type RING-HC finger with a potential E3 ubiquitin-ligase function, a highly conserved ROQ domain required for RNA binding and localization to stress granules, a coiled-coil (CC1), and a CCCH-type zinc finger that is involved in RNA recognition
QWTEFLSCPICYNEFDENVHKPISLGCSHTVCKTCLNKLHRKACPFDQT
>gnl|CDD|438438 cd16783, mRING-HC-C2H2C4_MDM2, Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2 and similar proteins. MDM2, also known as double minute 2 protein (Hdm2), oncoprotein MDM2, or p53-binding protein, exerts its oncogenic activity predominantly by binding p53 tumor suppressor and blocking its transcriptional activity. It forms homo-oligomers and displays E3 ubiquitin ligase activity that catalyzes the attachment of ubiquitin to p53 as an essential step in the regulation of its levels in cells. Moreover, in response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through its interaction with ribosomal proteins L5, L11, and L23. MDM2 can be phosphorylated in the DNA damage. Meanwhile, MDM2 has a p53-independent role in tumorigenesis and cell growth regulation. In addition, it binds interferon (IFN) regulatory factor-2 (IRF-2), an IFN-regulated transcription factor, and mediates its ubiquitination. MDM2 contains an N-terminal p53-binding domain, and a C-terminal modified C2H2C4-type RING-HC finger conferring E3 ligase activity that is required for ubiquitination and nuclear export of p53. It is also responsible for the hetero-oligomerization of MDM2, which is crucial for the suppression of P53 activity during embryonic development, and the recruitment of E2 ubiquitin-conjugating enzymes. MDM2 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain, as well as a nuclear localization signal (NLS) and a nuclear export signal (NES), near the central acidic region. The zf-RanBP2 domain plays an important role in mediating MDM2 binding to ribosomal proteins and thus is involved in MDM2-mediated p53 suppression
IEPCVICQTRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP
>gnl|CDD|319698 cd16784, mRING-HC-C2H2C4_MDM4, Modified RING finger, HC subclass (C2H2C4-type), found in protein MDM4 and similar proteins. MDM4, also known as double minute 4 protein (Hdm4), MDM2-like p53-binding protein, protein MDMX, HDMX, or p53-binding protein MDM4, exerts its oncogenic activity predominantly by binding p53 tumor suppressor and blocking its transcriptional activity. MDM4 is phosphorylated and destabilized in response to DNA damage stress. It can also be specifically dephosphorylated by directly interacting with protein phosphatase 1 (PP1), which may increase its stability and thus inhibit p53 activity. Meanwhile, MDM4 has a p53-independent role in tumorigenesis and cell growth regulation. MDM4 contains an N-terminal p53-binding domain and a C-terminal modified C2H2C4-type RING-HC finger responsible for its hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. MDM4 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region
NLLEPCSLCQKRPRNGNIVHGRTAHLVTCFHCARRLKKAGAPCPVCKKEIQMVIKIFIA
>gnl|CDD|438439 cd16785, mRING-HC-C3HC5_NEU1A, Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) and similar proteins. NEURL1A, also known as NEURL1, NEU, neuralized 1, or RING finger protein 67 (RNF67), is a mammalian homolog of the Drosophila neuralized (D-neu) protein. It functions as an E3 ubiquitin-protein ligase that directly interacts with and monoubiquitinates cytoplasmic polyadenylation element-binding protein 3 (CPEB3), an RNA binding protein and a translational regulator of local protein synthesis, which facilitates hippocampal plasticity and hippocampal-dependent memory storage. It also acts as a potential tumor suppressor that causes apoptosis and downregulates Notch target genes in the medulloblastoma. NEURL1A contains two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain
GSWSDECTICYENAVDTVIYTCGHMCLCYACGLRLKKMLNACCPICRRAIKDIIKTYRS
>gnl|CDD|438440 cd16786, mRING-HC-C3HC5_NEU1B, Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1B (NEURL1B). NEURL1B, also known as neuralized-2 (NEUR2) or neuralized-like protein 3, is a mammalian homolog of the Drosophila neuralized (D-neu) protein. It functions as an E3 ubiquitin-protein ligase that interacts with and ubiquitinates Delta. Thus, it plays a role in the endocytic pathways for Notch signaling through working cooperatively with another E3 ligase, Mind bomb-1 (Mib1), in Delta endocytosis to hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)-positive vesicles. NEURL1B contains two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain
KNGECTVCFDSEVDTVIYTCGHMCLCNSCGLKLKRQINACCPICRRVIKDVIKIYRP
>gnl|CDD|438441 cd16787, mRING-HC-C3HC5_CGRF1, Modified RING finger, HC subclass (C3HC5-type), found in cell growth regulator with RING finger domain protein 1 (CGRRF1) and similar proteins. CGRRF1, also known as cell growth regulatory gene 19 protein (CGR19) or RING finger protein 197 (RNF197), functions as a novel biomarker to monitor endometrial sensitivity and response to insulin-sensitizing drugs, such as metformin, in the context of obesity. CGRRF1 contains a C-terminal modified C3HC5-type RING-HC finger, which is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain
KDCVVCQNAPVNRVLLPCRHACVCDECFKRLQRCPMCR
>gnl|CDD|438442 cd16788, mRING-HC-C3HC5_RNF26, Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and similar proteins. RNF26 is an E3 ubiquitin ligase that temporally regulates virus-triggered type I interferon induction by increasing the stability of Mediator of IRF3 activation, MITA, also known as STING, through K11-linked polyubiquitination of MITA after viral infection, and promoting the degradation of IRF3, another important component required for virus-triggered interferon induction. Although RNF26 substrates of ubiquitination remain unclear at present, RNF26 upregulation in gastric cancer might be implicated in carcinogenesis through dysregulation of growth regulators. RNF26 contains an N-terminal leucine zipper domain and a C-terminal modified C3HC5-type RING-HC finger, which is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain
EERDKKKCVICQDQSKTVLILPCRHMCLCRQCANILLQQPVYRRNCPLCRTMILQTLDVY
>gnl|CDD|438443 cd16789, mRING-HC-C3HC5_MGRN1-like, Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 (MGRN1), RING finger protein 157 (RNF157) and similar proteins. MGRN1, also known as RING finger protein 156 (RNF156), is a cytosolic E3 ubiquitin-protein ligase that inhibits signaling through the G protein-coupled melanocortin receptors-1 (MC1R), -2 (MC2R) and -4 (MC4R) via ubiquitylation-dependent and -independent processes. It suppresses chaperone-associated misfolded protein aggregation and toxicity. MGRN1 interacts with cytosolic prion proteins (PrPs) that are linked with neurodegeneration. It also interacts with expanded polyglutamine proteins, and suppresses misfolded polyglutamine aggregation and cytotoxicity. Moreover, MGRN1 inhibits melanocortin receptor signaling by competition with Galphas, suggesting a novel pathway for melanocortin signaling from the cell surface to the nucleus. MGRN1 also interacts with and ubiquitylates TSG101, a key component of the endosomal sorting complex required for transport (ESCRT)-I, and regulates endosomal trafficking. A null mutation in the gene encoding MGRN1 causes spongiform neurodegeneration, suggesting a link between dysregulation of endosomal trafficking and spongiform neurodegeneration. RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in the brain. It is a homolog of the E3 ligase mahogunin ring finger-1 (MGRN1). In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis. Both MGRN1 and RNF157 contain a modified C3HC5-type RING-HC finger, and a functionally uncharacterized region, known as domain associated with RING2 (DAR2), N-terminal to the RING finger. The C3HC5-type RING-HC finger is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain
SECVICLSDPRDTAVLPCRHLCLCSDCAEVLRYQSNKCPICR
>gnl|CDD|438444 cd16790, SP-RING_PIAS, SP-RING finger found in protein inhibitor of activated signal transducer and activator of transcription (PIAS) proteins. The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. It consists of four members: PIAS1, PIAS2 (also known as PIASx), PIAS3, and PIAS4 (also known as PIASy). PIAS proteins were initially identified as inhibitors of activated STAT only, but are now known to interact with and modulate several other proteins, including androgen receptor (AR), tumor suppressor p53, and the transforming growth factor-beta (TGF-beta) signaling protein SMAD. They interact with STATs in a cytokine-dependent manner. PIAS1, PIAS2, and PIAS3 interact with STAT1, STAT3, and STAT4, respectively. In addition, PIAS4 is associated with STAT1. PIAS proteins have SUMO E3-ligase activity and interaction of PIAS proteins with transcription factors often results in sumoylation of that protein. PIAS proteins contain an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, which is required for the trans-repression of STAT1 activity by PIAS2, a PINT motif, which is essential for nuclear retention of PIAS3L (the long form of PIAS3), a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, which is essential for SUMO ligase activity, and the acidic C-terminal domain, which is involved in binding of PIAS3 to the nuclear coactivator TIF2. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers
SLMCPLGKMRLTIPCRALTCSHLQCFDAALYLQMNEKKPTWICPVCDK
>gnl|CDD|438445 cd16791, SP-RING_ZMIZ, SP-RING finger found in zinc finger MIZ domain-containing protein Zmiz1, Zmiz2, and similar proteins. This subfamily includes Zmiz1 (Zimp10) and its homolog Zmiz2 (Zimp7), both initially identified in humans as androgen receptor (AR) interacting proteins which function as transcriptional co-activators. They interact with BRG1, the catalytic subunit of the SWI-SNF remodeling complex. They also associate with other hormone nuclear receptors and transcription factors, such as p53 and Smad3/Smad4, and regulate transcription of specific target genes by altering their chromatin structure. This subfamily also includes tonalli (Tna), an ortholog identified in Drosophila. It genetically interacts with the ATP-dependent SWI/SNF and Mediator complexes, suggesting a potential role for the Zmiz proteins in chromatin remodeling. Zmiz proteins contain a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a strong transactivation domain within the C-terminus. The SP-RING/Miz domain is highly conserved in members of the PIAS family and confers SUMO-conjugating activity. It is a variant of the RING finger, and lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers. The strong intrinsic transactivation domain facilitates Zmiz proteins to augment the transcriptional activity of nuclear hormone receptors and other transcriptional factors. They may act as transcriptional co-regulators
SLKCPITFRRITLPARGHDCKHIQCFDLESYLQLNCERGTWRCPVCNK
>gnl|CDD|438446 cd16792, SP-RING_Siz-like, SP-RING finger found in Arabidopsis thaliana E3 SUMO-protein ligase SIZ1 (AtSIZ1) and similar proteins. SIZ1-mediated conjugation of SUMO1 and SUMO2 to other intracellular proteins is essential in Arabidopsis. AtSIZ1 negatively regulates abscisic acid (ABA) signaling through the sumoylation of bZIP transcripton factor ABI5. It also mediates sumoylation of bromodomain GTE proteins. Moreover, AtSIZ1 regulates flowering by controlling a salicylic acid-mediated floral promotion pathway and through affecting on FLOWERING LOCUS C (FLC) chromatin structure. It also plays a role in drought stress response likely through the regulation of gene expression. Members of this subfamily contain an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box, a plant homeodomain (PHD) finger, and a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers
SLKCPLSYSRIKVPCRSIKCTHIQCFDLDSFLQLNEQTPSWQCPICNKNI
>gnl|CDD|438447 cd16793, SP-RING_ScSiz-like, SP-RING finger found in Saccharomyces cerevisiae E3 SUMO-protein ligase SIZ1, SIZ2, and similar proteins. Saccharomyces cerevisiae SIZ proteins, also known as SAP and Miz-finger domain-containing proteins, are Siz/PIAS RING (SP-RING) family SUMO E3 ligases, and may be involved in a novel pathway of chromosome maintenance. They enhance SUMO modification with many substrates in vivo, but also exhibit unique substrate specificity. SIZ1, also known as ubiquitin-like protein ligase 1 (Ull1), modifies both cytoplasmic and nuclear proteins. It functions as an E3 factor specific for septin components. SIZ1-dependent substrates include Cdc3 and Cdc11 (septin subunits), Prp45 (a splicing factor), and the proliferating cell nuclear antigen (PCNA). SIZ2, also known as NFI1, interacts with Smt3, SUMO/Smt3 conjugating enzyme Ubc9, and a septin component Cdc3. Members of this subfamily contain an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers
STIMSLQCPISYTRMKYPSKSINCKHLQCFDALWFLHSQLQIPTWQCPVCQIDIAL
>gnl|CDD|438448 cd16794, dRING_RMD5A, Degenerated RING finger found in protein RMD5 homolog A (RMD5A). RMD5A is one of the vertebrate homologs of yeast Rmd5p. The biological function of RMD5A remains unclear. RMD5A contains a Lissencephaly type-1-like homology motif (LisH), a C-terminal to LisH motif (CTLH) domain, and a degenerated RING finger that is characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers
SIFACPILRQQTTENNPPMKLVCGHIISRDALNKMFNGSKLKCPYCPMEQSPGDAKQIFF
>gnl|CDD|438449 cd16795, dRING_RMD5B, Degenerated RING finger found in protein RMD5 homolog B (RMD5B). RMD5B is one of the vertebrate homologs of yeast Rmd5p. The biological function of RMD5B remains unclear. RMD5B contains a Lissencephaly type-1-like homology motif (LisH), a C-terminal to LisH motif (CTLH) domain, and a degenerated RING finger that is characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers
VFACPILRQQTTDSNPPMKLICGHVISRDALNKLINGGKLKCPYCPMEQNPADAKRIYF
>gnl|CDD|438450 cd16796, RING-H2_RNF13, RING finger, H2 subclass, found in RING finger protein 13 (RNF13) and similar proteins. RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that is functionally significant in the regulation of cancer development, muscle cell growth, and neuronal development. Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. It functions as an important regulator of inositol-requiring transmembrane kinase/endonuclease IRE1alpha, mediating endoplasmic reticulum (ER) stress-induced apoptosis through the activation of the IRE1alpha-TRAF2-JNK signaling pathway. Moreover, RNF13 is involved in the regulation of the soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) complex via the ubiquitination of snapin, a SNAP25-interacting protein, which thereby controls synaptic function. In addition, RNF13 participates in regulating the function of satellite cells by modulating cytokine composition. RNF13 is evolutionarily conserved among many metazoans and contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence
KFKKGDEYDVCAICLDEYEEGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPS
>gnl|CDD|319711 cd16797, RING-H2_RNF167, RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins. RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) ubiquitination. It ubiquitinates AMPA-type glutamate receptor subunit GluA2 and regulates its surface expression, and thus acts as a selective regulator of AMPAR-mediated neurotransmission. It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA, also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. RNF167 is widely conserved in metazoans and contains an N-terminal signal peptide, a protease-associated (PA) domain, two transmembrane domains (TM1 and TM2), and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence
DVCAICLDEYEEGDKLRVLPCSHAYHSKCVDPWLTQTKKTCPVCKQ
>gnl|CDD|438451 cd16798, RING-H2_RNF43, RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins. RNF43 is a transmembrane E3 ubiquitin-protein ligase that plays an important role in frizzled (FZD)-dependent regulation of the Wnt/beta-catenin pathway. It functions as a tumor suppressor that inhibits Wnt/beta-catenin signaling by ubiquitinating FZD receptor and targeting it to the lysosomal pathway for degradation. miR-550a-5p directly targeted the 3'-UTR of gene RNF43 and regulated its expression. Moreover, RNF43 interacts with NEDD-4-like ubiquitin-protein ligase-1 (NEDL1) and regulates p53-mediated transcription. It may also be involved in cell growth control through the interaction with HAP95, a chromatin-associated protein interfacing the nuclear envelope. Mutations of RNF43 have been identified in various tumors, including colorectal cancer (CRC), endometrial cancer, mucinous ovarian tumors, gastric adenocarcinoma, pancreatic ductal adenocarcinoma, liver fluke-associated cholangiocarcinoma, hepatocellular carcinoma, and glioma. RNF43 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger followed by a long C-terminal region
SSAPVCAICLEEFSEGQELRIISCSHEFHRECVDPWLHQHRTCPLCMFNIIEG
>gnl|CDD|319713 cd16799, RING-H2_ZNRF3, RING finger, H2 subclass, found in zinc/RING finger protein 3 (ZNRF3) and similar proteins. ZNRF3, also known as RING finger protein 203 (RNF203), is a homolog of Ring finger protein 43 (RNF43). It is a transmembrane E3 ubiquitin-protein ligase that is associated with the Wnt receptor complex, and negatively regulates Wnt signaling by promoting the turnover of frizzled and lipoprotein receptor-related protein LRP6 in an R-spondin-sensitive manner. It inhibits gastric cancer cell growth and promotes cell apoptosis by affecting the Wnt/beta-catenin/TCF signaling pathway. ZNRF3 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger followed by a long C-terminal region
DCAICLEKYIDGEELRVIPCTHRFHKKCVDPWLLQHHTCPHCRHN
>gnl|CDD|438452 cd16800, RING-H2_RNF115, RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins. RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation and its inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a co-factor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. Furthermore, RNF115 and the related protein, RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF115 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger
LECPVCKEDYTVGEQVRQLPCNHFFHSDCIVPWLELHDTCPVCRKSLNGE
>gnl|CDD|438453 cd16801, RING-H2_RNF126, RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins. RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). Moreover, RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. In addition, RNF126 and the related protein, RNF115 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF126 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger
ECPVCKEDYTVGENVRQLPCNHLFHNDCIVPWLEQHDTCPVCRK
>gnl|CDD|438454 cd16802, RING-H2_RNF128-like, RING finger, H2 subclass, found in RING finger protein 128 (RNF128) and similar proteins. This subfamily includes RING finger proteins RNF128, RNF133, RNF148, and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger followed by a putative PEST sequence. RNF128, also known as gene related to anergy in lymphocytes protein (GRAIL), is a type 1 transmembrane E3 ubiquitin-protein ligase that is a critical regulator of adaptive immunity and development. It inhibits cytokine gene transcription, is expressed in anergic CD4+ T cells, and has been implicated in primary T cell activation, survival, and differentiation, as well as in T cell anergy and oral tolerance. It induces T cell anergy through the ubiquitination activity of its cytosolic RING finger. It regulates expression of the costimulatory molecule CD40L on CD4 T cells, and ubiquitinates the costimulatory molecule CD40 ligand (CD40L) during the induction of T cell anergy. Moreover, RNF128 interacts with the luminal/extracellular portion of both CD151 and the related tetraspanin CD81 via its PA domain, which promoted ubiquitination of cytosolic lysine residues. It also down-modulates the expression of CD83 (previously described as a cell surface marker for mature dendritic cells) on CD4 T cells. Furthermore, Rho guanine dissociation inhibitor (RhoGDI) has been identified as a potential substrate of RNF128, suggesting a role for Rho effector molecules in T cell anergy. In addition, RNF128 plays a role in environmental stress responses. It promotes environmental salinity tolerance in euryhaline tilapia. RNF133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase that is mainly present in the cytoplasm of elongated spermatids. It may play a role in sperm maturation through an ER-associated degradation (ERAD) pathway. RNF148 is a testis-specific E3 ubiquitin ligase that is abundantly expressed in testes and slightly expressed in pancreas. Its expression is regulated by histone deacetylases
DSCAVCIEPYKPNDVVRILTCNHLFHKNCIDPWLLEHRTCPMCKCDILK
>gnl|CDD|319717 cd16803, RING-H2_RNF130, RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins. RNF130, also known as Goliath homolog (H-Goliath), is a paralog of RNF128, also known as gene related to anergy in lymphocytes protein (GRAIL). It is a transmembrane E3 ubiquitin-protein ligase expressed in leukocytes. It has a self-ubiquitination property, and controls the development of T cell clonal anergy by ubiquitination. RNF130 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence
DHCAVCIEGYKQNDVVRILPCKHVFHKSCVDPWLNEHCTCPMCKLNILK
>gnl|CDD|438455 cd16804, RING-H2_RNF149, RING finger, H2 subclass, found in RING finger protein 149 (RNF149) and similar proteins. RNF149, also known as DNA polymerase-transactivated protein 2, is an E3 ubiquitin-protein ligase that interacts with wild-type v-Raf murine sarcoma viral oncogene homolog B1 (BRAF), a RING domain-containing E3 ubiquitin ligase involved in control of gene transcription, translation, cytoskeletal organization, cell adhesion, and epithelial development. RNF149 induces the ubiquitination of wild-type BRAF and promotes its proteasome-dependent degradation. Mutated RNF149 has been found in some human breast, ovarian, and colorectal cancers. RNF149 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence
NCAVCIENYKSKDVVRILPCKHVFHRICIDPWLLEHRTCPMCKLDVIK
>gnl|CDD|438456 cd16805, RING-H2_RNF150, RING finger, H2 subclass, found in RING finger protein 150 (RNF150) and similar proteins. RNF150 is a RING finger protein and its polymorphisms may be associated with chronic obstructive pulmonary disease (COPD) risk in the Chinese population. Further studies with larger numbers of participants worldwide are needed for validation of the relationships between RNF150 genetic variants and the pathogenesis of COPD. RNF150 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence
ETESDFDNCAVCIEGYKPNDVVRILPCRHLFHKSCVDPWLLDHRTCPMCKMNILK
>gnl|CDD|438457 cd16806, RING_CH-C4HC3_MARCH1, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING-CH1 (MARCH1). MARCH1, also known as membrane-associated RING finger protein 1, membrane-associated RING-CH protein I (MARCH-I), or RING finger protein 171 (RNF171), is a membrane-anchored E3 ubiquitin ligase that is mainly expressed in cells of the immune system. It regulates antigen presentation and T-cell costimulatory functions of dendritic cells by down-regulating the cell surface expression of major histocompatibility complex class II (MHCII) and CD86 molecules. It mediates ubiquitination of MHCII and CD86 in dendritic cells (DCs). This ubiquitination induces MHCII and CD86 endocytosis, lysosomal transport, and degradation. MARCH1 also plays a regulatory role in T cell activation during immune responses, as well as in splenic DC homeostasis. Moreover, MARCH1 may regulate its own expression through dimerization and autoubiquitination. MARCH1 contains an N-terminal cytoplasmic C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger and two transmembrane domains
PSTQDICRICHCEGDEESPLITPCRCTGTLRFVHQACLHQWIKSSDTRCCELCKYDFIMETKLKPLRKWE
>gnl|CDD|438458 cd16807, RING_CH-C4HC3_MARCH8, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING-CH8 (MARCH8). MARCH8, also known as membrane-associated RING finger protein 8, membrane-associated RING-CH protein VIII (MARCH-VIII), RING finger protein 178 (RNF178), or cellular modulator of immune recognition (c-MIR), is a membrane-anchored E3 ubiquitin ligase that is broadly expressed. It is a functional homolog of Kaposi"s sarcoma associated-herpes virus encoded proteins, modulator of immune recognition (MIR) 1 and 2, which are involved in the evasion of host immunity. MARCH8 mediates the ubiquitination and down-regulation of immune regulatory cell surface molecules, including major histocompatibility complex class II (MHCII), CD86, transferrin receptor, HLA-DM, and Fas in immune cells. Moreover, MARCH8 controls cell surface expression of some additional proteins. It regulates the ubiquitination and lysosomal degradation of the transferrin receptor (TfR). Tumor necrosis factor-related apoptosis inducing ligand receptor 1 (TRAIL-R1) is also a physiological substrate of the endogenous MARCH8, which regulates the steady-state cell surface expression of TRAIL-R1. Meanwhile, it negatively regulates interleukin-1 (IL-1) beta-induced NF-kappaB activation by targeting the IL-1 receptor accessory protein (IL1RAP) coreceptor for ubiquitination and degradation. Furthermore, MARCH8 functions in the embryo to modulate the strength of cell adhesion by regulating the localization of E-cadherin. In addition, MARCH8 plays a role in the inhibition of inflammatory cytokine production, suggesting a new therapeutic approach to the treatment of rheumatoid arthritis (RA). MARCH8 contains an N-terminal cytoplasmic C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger and two transmembrane domains
TPSNQDICRICHCEGDDESPLITPCHCTGSLRFVHQACLQQWIKSSDTRCCELCKYEFIMETKL
>gnl|CDD|319722 cd16808, RING_CH-C4HC3_MARCH2, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING-CH2 (MARCH2). MARCH2, also known as membrane-associated RING finger protein 2, membrane-associated RING-CH protein II (MARCH-II), or RING finger protein 172 (RNF172), is a Golgi-localized, membrane-associated E3 ubiquitin-protein ligase that is involved in endosomal trafficking through the binding of syntaxin 6 (STX6). It is involved in the cystic fibrosis transmembrane conductance regulator (CFTR)-associated ligand (CAL)-mediated ubiquitination and lysosomal degradation of mature CFTR through the association with adaptor proteins CAL and STX6. It also reduces the surface expression of CD86 and the transferrin receptor TFRC and regulates cell surface carvedilol-bound beta2-adrenergic receptor (beta2AR) expression. Moreover, MARCH2 interacts with and ubiquitinates PDZ domains polarity determining scaffold protein DLG1 through its PDZ-binding motif, suggesting it may function as a molecular bridge with ubiquitin ligase activity connecting endocytic tumor suppressor proteins such as syntaxins to DLG1. MARCH2 contains a C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, in the N-terminal cytoplasmic region, two transmembrane domains in the middle region, and a PDZ-binding motif at the C-terminus
PICRICHEGGNGESLLSPCDCTGTLGTVHKSCLEKWLSSSNTSYCELCHTEF
>gnl|CDD|438459 cd16809, RING_CH-C4HC3_MARCH3, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING-CH3 (MARCH3). MARCH3, also known as membrane-associated RING finger protein 3, or membrane-associated RING-CH protein III (MARCH-III), or RING finger protein 173 (RNF173), is an E3 ubiquitin-protein ligase that is broadly expressed and is found at relatively high levels in spleen, colon, and lung. It is localized to early endosomes, binds to MARCH2 and syntaxin 6, and is involved in the regulation of vesicular trafficking and fusion of the transport vesicles in endosomes. MARCH3 is the closest homolog of MARCH2 and it is also a functional homolog of K3 and K5 viral ubiquitin E3 ligases related to immune-evasion strategies used by Kaposi's sarcoma-associated herpesvirus (KSHV). Its E2 specificity significantly overlaps that of MARCH2. MARCH3 contains a C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, in the N-terminal cytoplasmic region, two transmembrane domains in the middle region, and a PDZ-binding motif at the C-terminus. The RING-CH finger and PDZ-binding motif are essential for the subcellular localization of MARCH3 and the inhibitory effect on transferrin uptake
FNDRPMCRICHEGSSQEDLLSPCECTGTLGTIHRSCLEHWLSSSNTSYCELCHFRF
>gnl|CDD|438460 cd16810, RING_CH-C4HC3_MARCH11, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING-CH11 (MARCH11). MARCH11, also known as membrane-associated RING finger protein 11, or membrane-associated RING-CH protein XI (MARCH-XI), is a transmembrane RING-finger ubiquitin ligase that is predominantly expressed in developing spermatids in a stage-specific manner and is localized to trans-Golgi network (TGN) vesicles and multivesicular bodies (MVBs). It mediates selective protein sorting via the TGN-MVB transport pathway through its ubiquitin ligase activity. SAMT family proteins have been identified as substrates of MARCH11 in mouse spermatids, suggesting that MARCH11 plays a role in mammalian spermiogenesis. Moreover, MARCH11 targets CD4 for ubiquitination. It also forms complexes with the adaptor protein complex-1 and with fucose-containing glycoproteins including ubiquitinated forms. MARCH11 contains an N-terminal C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, and two transmembrane domains. In addition, it harbors a proline-rich region, a tyrosine-based motif, and a PDZ binding motif
PICKICFQGPEQGELLNPCRCDGSVRYTHQLCLLKWISERGSWTCELCCYRYHVIAIKMK
>gnl|CDD|319725 cd16811, RING_CH-C4HC3_MARCH4_9, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING finger protein MARCH4, MARCH9, and similar proteins. This subfamily includes the closely related MARCH4 and MARCH9, both belonging to the family of MARCH E3 ligases. They downregulate major histocompatibility complex-I (MHC-I). In the presence of MARCH4 or MARCH9, MHC-I can be ubiquitinated and rapidly internalized by endocytosis, whereas MHC-I molecules lacking lysines in their cytoplasmic tail are resistant to downregulation. Moreover, MARCH4 and MARCH9, but not other MARCH proteins, can associate with Mult1 and prevent Mult1 expression at the cell surface in a lysine-dependent manner that can be reversed by heat shocking the cells. Both MARCH4 and MARCH9 contain an N-terminal C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, followed by two transmembrane regions
LCRICFQGPEQGELLSPCRCDGSVRCTHQPCLIKWISERGSWSCELCYYKY
>gnl|CDD|438461 cd16812, RING_CH-C4HC3_MARCH7, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING-CH7 (MARCH7). MARCH7, also known as membrane-associated RING finger protein 7, membrane-associated RING-CH protein VII (MARCH-VII), RING finger protein 177 (RNF177), or axotrophin, is a ubiquitin E3 ligase expressed in multiple types of cells and tissues, including stem cells and precursor cells, and is predominantly localized on the plasma membrane and cytoplasm. MARCH7 is involved in T cell proliferation and neuronal development. It also participates in the regulation of cytoskeleton re-organization, cellular migration and invasion, cell proliferation, and tumorigenesis in ovarian carcinoma cells. Moreover, MARCH7 modulates nuclear factor kappaB (NF-kappaB) and Wnt/beta-catenin pathways. It has been identified as an authentic target of miR-101. Furthermore, it ubiquitinates tau protein in vitro, impairing microtubule binding. Unlike other MARCH proteins, MARCH7 is predicted to have no transmembrane spanning region. It harbors a C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, that is responsible for its E3 activity
EEEGDLCRICQMGMTSSSNPLIEPCKCTGSLQYVHQECMKKWLQAKINSGSSLEAVTTCELCKEK
>gnl|CDD|438462 cd16813, RING_CH-C4HC3_MARCH10, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING-CH10 (MARCH10). MARCH10, also known as membrane-associated RING finger protein 10, membrane-associated RING-CH protein X (MARCH-X), or RING finger protein 190 (RNF190), is a microtubule-associated E3 ubiquitin ligase in developing spermatids and is involved in spermiogenesis by regulating the formation and maintenance of the flagella. It is localized to the principal piece of elongating spermatids. Unlike other MARCH proteins, MARCH10 is predicted to have no transmembrane spanning region. It harbors a C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, that is responsible for its E3 activity
EDSEEEGDLCRICQIAGGSPSNPLLEPCGCVGSLQFVHQECLKKWLKVKITSGADLGAVKTCEMCKQGLL
VDLGDF
>gnl|CDD|438463 cd16814, RING-HC_RNF20, RING finger, HC subclass, found in RING finger protein 20 (RNF20). RNF20, also known as BRE1A or BRE1, is an E3 ubiquitin-protein ligase that forms a heterodimeric complex together with BRE1B, also known as RNF40, to facilitate the K120 monoubiquitination of histone H2B (H2Bub1), a DNA damage-induced histone modification that is crucial for recruitment of the chromatin remodeler SNF2h to DNA double-strand break (DSB) damage sites. It regulates the cell cycle and differentiation of neural precursor cells (NPCs), and links histone H2B ubiquitylation with inflammation and inflammation-associated cancer. Moreover, RNF20 promotes the polyubiquitination and proteasome-dependent degradation of transcription factor activator protein 2alpha (AP-2alpha), a negative regulator of adipogenesis by repressing the transcription of CCAAT/enhancer binding protein (C/EBPalpha) gene. Furthermore, RNF20 functions as an additional chromatin regulator that is necessary for mixed-lineage leukemia (MLL)-fusion-mediated leukemogenesis. It also inhibits TFIIS-facilitated transcriptional elongation to suppress pro-oncogenic gene expression. TFIIS is a factor capable of relieving stalled RNA polymerase II. RNF20 contains a C3HC4-type RING-HC finger at its C-terminus
LVPNCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFH
RIYIG
>gnl|CDD|438464 cd16815, RING-HC_RNF40, RING finger, HC subclass, found in RING finger protein 40 (RNF40). RNF40, also known as BRE1B or 95 kDa retinoblastoma-associated protein (RBP95), was identified as a novel leucine zipper retinoblastoma protein (pRb)-associated protein that may function as a regulation factor in RNA polymerase II-mediated transcription and/or transcriptional processing. RNF40 also functions as an E3 ubiquitin-protein ligase that forms a heterodimeric complex with BRE1B, also known as RNF40, to facilitate the K120 monoubiquitination of histone H2B (H2Bub1), a DNA damage-induced histone modification that is crucial for recruitment of the chromatin remodeler SNF2h to DNA double-strand break (DSB) damage sites. It cooperates with SUPT16H to induce dynamic changes in chromatin structure during DSB repair. RNF40 contains a C3HC4-type RING-HC finger at the C-terminus
KKVEVYADADEILQEEIKEYKARLTCPCCNTRKKDAVLTKCFHVFCFECVKTRYESRQRKCPKCNAAFGA
HDFHRIYI
>gnl|CDD|438465 cd16816, mRING-HC-C3HC5_MGRN1, Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 (MGRN1) and similar proteins. MGRN1, also known as RING finger protein 156 (RNF156), is a cytosolic E3 ubiquitin-protein ligase that inhibits signaling through the G protein-coupled melanocortin receptors-1 (MC1R), -2 (MC2R) and -4 (MC4R) via ubiquitylation-dependent and -independent processes. It suppresses chaperone-associated misfolded protein aggregation and toxicity. MGRN1 interacts with cytosolic prion proteins (PrPs) that are linked with neurodegeneration. It also interacts with expanded polyglutamine proteins, and suppresses misfolded polyglutamine aggregation and cytotoxicity. Moreover, MGRN1 inhibits melanocortin receptor signaling by competition with Galphas, suggesting a novel pathway for melanocortin signaling from the cell surface to the nucleus. Furthermore, MGRN1 interacts with and ubiquitylates TSG101, a key component of the endosomal sorting complex required for transport (ESCRT)-I, and regulates endosomal trafficking. A null mutation in the gene encoding MGRN1 causes spongiform neurodegeneration, suggesting a link between dysregulation of endosomal trafficking and spongiform neurodegeneration. MGRN1 contains a modified C3HC5-type RING-HC finger, a conserved PSAP motif necessary for interaction between MGRN1 and TSG101. In addition, MGRN1 harbors a functionally uncharacterized region, as known as the domain associated with RING2 (DAR2), N-terminal to the RING finger. The C3HC5-type RING-HC finger is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain
DDENSDNSNECVVCLSDLRDTLILPCRHLCLCNSCADTLRYQANNCPICRLPFRALLQ
>gnl|CDD|438466 cd16817, mRING-HC-C3HC5_RNF157, Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 157 (RNF157) and similar proteins. RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in brain. It is a homolog of the E3 ligase mahogunin ring finger-1 (MGRN1). In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis. RNF157 contains a modified C3HC5-type RING-HC finger, and a functionally uncharacterized region, known as domain associated with RING2 (DAR2), N-terminal to the RING finger. The C3HC5-type RING-HC finger is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain
SDNSAECVVCLSDVRDTLILPCRHLCLCNACADTLRYQANNCPICRLPFRALLQIRAMRK
>gnl|CDD|438467 cd16818, SP-RING_PIAS1, SP-RING finger found in protein inhibitor of activated STAT protein 1 (PIAS1) and similar proteins. PIAS1, also known as DEAD/H box-binding protein 1, Gu-binding protein (GBP), or RNA helicase II-binding protein, was initially identified as an inhibitor of STAT1 that blocks the DNA-binding activity of STAT1 and specifically inhibits STAT1-mediated gene transcription in response to cytokine stimulation. It selectively inhibits interferon-inducible gene expression and plays an important role in the IFN-gamma- or IFN-beta-mediated innate immune response through negative regulation of STAT1. It also regulates the activity of other transcription factors to regulate immune response, such as NF-kappaB and Smad4. Moreover, PIAS1 functions as an E3 small ubiquitin-like modifier (SUMO)-protein ligase specifying target proteins for SUMO conjugation by Ubc9. The sumoylation activity of PIAS1 can suppress cytokine transforming growth factor beta (TGFbeta)-induced epithelial mesenchymal transition (EMT) in non-transformed epithelial cells to promote activation of the matrix metalloproteinase 2 (MMP2). It thus regulates TGFbeta-induced cancer cell invasion and metastasis. PIAS1 may also be involved in spatial learning and memory formation through its SUMOylation of cAMP-responsive element binding protein (CREB). In addition, PIAS1 is the E3 ligase responsible for SUMOylation of High mobility group nucleosomal binding domain 2 (HMGN2), which is a small and unique non-histone protein that has many functions in a variety of cellular processes, including regulation of chromatin structure, transcription, and DNA repair, as well as antimicrobial activity, cell homing, and regulating cytokine release. Furthermore, PIAS1 is a genuine chromatin-bound androgen receptor (AR) co-regulator that functions in a target gene selective fashion to regulate prostate cancer cell growth. It also mediates the SUMOylation of c-Myc, which is the most frequently overexpressed oncogene in tumors, including breast cancer, colon cancer, and lung cancer. Necdin, a pleiotropic protein that promotes differentiation and survival of mammalian neurons, can suppress PIAS1 both by inhibiting SUMO E3 ligase activity and by promoting ubiquitin-dependent degradation. PIAS1 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and the acidic C-terminal domain. The SP-RING finger mediates the interaction of PIAS1 with the SUMO E2 conjugating enzyme Ubc9. It binds a single Zn ion, instead of two ions bound by typical RING fingers
TSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHL
>gnl|CDD|438468 cd16819, SP-RING_PIAS2, SP-RING finger found in protein inhibitor of activated STAT protein 2 (PIAS2) and similar proteins. PIAS2, also known as androgen receptor-interacting protein 3 (ARIP3), DAB2-interacting protein (DIP), Msx-interacting zinc finger protein (Miz1), PIAS-NY protein, protein inhibitor of activated STAT x, protein inhibitor of activated STAT2, is an E3 SUMO-protein ligase highly expressed in the testis. It functions as a transcriptional activator of BCL2 and is essential for blocking c-MYC-induced apoptosis. It also acts as a negative regulator of cell proliferation, induces expression of the cell-cycle inhibitors p15(Ink4b) and p21(Cip1), and activates transcription of the p21(Cip1) gene in response to UV irradiation. Moreover, PIAS2 associates with topoisomerase II binding protein 1 (TopBP1), an essential activator of the Atr kinase. It thus affects the activity of the Atr checkpoint. Receptor of activated C kinase 1 (RACK1), glucocorticoid receptor (GR)-interacting protein 1 (GRIP1), friend leukemia integration-I (FLI-1), and ubiquitously expressed transcript (UXT) are binding partners of PIAS2. The interaction between UXT and PIAS2 may be important for the transcriptional activation of androgen receptor (AR). PIAS2 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus, and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers
TSLRVSLMCPLGKMRLTIPCRAVTCSHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESL
>gnl|CDD|438469 cd16820, SP-RING_PIAS3, SP-RING finger found in protein inhibitor of activated STAT protein 3 (PIAS3) and similar proteins. PIAS3 is an E3 SUMO-protein ligase that was initially identified as an interleukin-6 (IL-6)-dependent repressor of signal transducer and activator of transcription 3 (STAT3) and has anti-proliferative properties. It binds specifically to phosphorylated STAT3 and inhibits its transcriptional activity by blocking its binding to DNA. It regulates STAT3-mediated induction of Snail expression, as well as suppresses acute graft-versus-host disease (GVHD) by modulating effector T and B cell subsets through inhibition of STAT3 activation. It activates the intrinsic apoptotic pathway in non-small cell lung cancer cells independent of p53 status. When overexpressed, it can interact with STAT5 to regulate prolactin-induced STAT5-mediated gene expression. Moreover, PIAS3 binds to and activates Smad3 transcriptional activity, resulting in the enhancement of transforming growth factor-beta (TGF-beta) signaling. It functions as a transcriptional corepressor of Erythroid Kruppel-like factor (EKLF or KLF1) and thus plays an important role in erythropoiesis. It also plays a significant role in the DNA damage response (DDR) pathway by promoting homologous recombination (HR)- and non-homologous end joining (NHEJ)-mediated DNA double-strand break (DSB) repair. Furthermore, PIAS3 preferentially interacts with and enhances the SUMOylation of TAK1-binding protein 2 (TAB2), an upstream adaptor protein in the IL-1 signaling pathway. It also promotes SUMOylation and nuclear sequestration of ErbB4 receptor tyrosine kinase. In addition, PIAS3 may form a complex with microphthalmia-associated transcription factor, nuclear factor-kappaB, Smad, and estrogen receptor. Its other transcription factor binding partners include: ETS, EGR1, NR1I2, and GATA1. PIAS3 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers
TSLRVSLMCPLGKMRLTVPCRAITCTHLQCFDAALYLQMNEKKPTWTCPVCDKKAPYESLII
>gnl|CDD|438470 cd16821, SP-RING_PIAS4, SP-RING finger found in protein inhibitor of activated STAT protein 4 (PIAS4) and similar proteins. PIAS4, also known as PIASy or protein inhibitor of activated STAT protein gamma (PIAS-gamma), is an E3 SUMO-protein ligase that interacts with the androgen receptor (AR) and is involved in ubiquitin signaling pathways. It is associated with macro/microcephaly in the novel interstitial 19p13.3 microdeletion/microduplication syndrome. It also regulates the hypoxia signalling pathway by interacting with the tumor suppressor von Hippel-Lindau (VHL), which leads to VHL sumoylation, oligomerization, and impaired function during growth of pancreatic cancer cells. Moreover, PIAS4 acts as a direct binding partner for vitamin D receptor (VDR) and facilitates its modification with SUMO2. The process of SUMOylation modulates VDR-mediated signaling. As components of the DNA-damage response (DDR), PIAS4 together with PIAS1 promote responses to DNA double-strand breaks (DSBs). They are required for effective ubiquitin-adduct formation mediated by RNF8, RNF168, and BRCA1 at sites of DNA damage. PIAS4 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers
TGVRVSLICPLVKMRLSVPCRAETCAHLQCFDAVFYLQMNEKKPTWTCPVCDKPAPYD
>gnl|CDD|438471 cd16822, SP-RING_ZMIZ1, SP-RING finger found in zinc finger MIZ domain-containing protein 1 (Zmiz1) and similar proteins. Zmiz1, also known as PIAS-like protein Zimp10 (zinc finger-containing, Miz1, PIAS-like protein on chromosome 10) or retinoic acid-induced protein 17, is a novel PIAS-like protein that was initially identified as an androgen receptor (AR) interacting protein and functions as a transcriptional co-activator. It co-localizes with AR and small ubiquitin-like modifier SUMO-1, forms a protein complex at replication foci in the nucleus, and augments AR-mediated transcription. It also functions as a transcriptional co-activator of the p53 tumor suppressor that plays a critical role in cell cycle progression, DNA repair, and apoptosis. Moreover, Zmiz1 dysfunction may be associated with multiple autoimmune diseases and it has been implicated in the development, function, and survival of melanocytes. Zmiz1 also interacts with Smad3/4 proteins and augments Smad-mediated transcription, suggesting it is important in the regulation of the transforming growth factor beta (TGF-beta)/Smad signaling pathway and may have an inhibitory effect on the immune system. Zmiz1 is overexpressed in a significant percentage of human cutaneous squamous cell carcinoma (SCC), breast, ovarian, and colon cancers, suggesting it may play a broader role in epithelial cancers. It functionally interacts with NOTCH1 to promote C-MYC transcription and activity, and thus is involved in a variety of C-MYC-driven cancers. Zmiz1 contains a PAT domain, a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a putative nuclear localization sequence (NLS), as well as a strong intrinsic transactivation domain within the C-terminus. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers
KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMW
>gnl|CDD|438472 cd16823, SP-RING_ZMIZ2, SP-RING finger found in zinc finger MIZ domain-containing protein 2 (Zmiz2) and similar proteins. Zmiz2, also known as PIAS-like protein Zimp7 (zinc finger-containing, Miz1, PIAS-like protein on chromosome 7), is a novel PIAS-like protein that was initially identified as an androgen receptor (AR) interacting protein and functions as a transcriptional co-activator. It interacts with beta-catenin and enhances Wnt/beta-catenin-mediated transcription. It also associates with BRG1 and BAF57, components of the ATP-dependent mammalian SWI/SNF-like BAF chromatin-remodeling complexes, and thus plays a potential role in modulation of AR and/or other nuclear receptor-mediated transcription. For instance, it can increase the effects of BRG1 on AR-mediated transcriptional activity. Moreover, Zmiz2 physically interacts with PIAS proteins, especially PIAS3. Through this interaction, PIAS3 augments Zmiz2-mediated transcription, suggesting PIAS proteins may play a regulatory role in Zmiz-mediated transcription. Furthermore, Zmiz2 is involved in transcriptional regulation of factors essential for patterning in the dorsoventral axis. It is required for the restriction of the zebrafish organizer and mesoderm development. Zmiz2 contains a PAT domain, a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a strong intrinsic transactivation domain within the C-terminus. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers
EQTAIKVSLKCPITFRRIQLPARGHDCRHIQCFDLESYLQLNCERGTWRCPVCNKTALLEG
>gnl|CDD|438473 cd16824, RING_CH-C4HC3_MARCH4, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING-CH4 (MARCH4). MARCH4, also known as membrane-associated RING finger protein 4, membrane-associated RING-CH protein IV (MARCH-IV), or RING finger protein 174 (RNF174), is a transmembrane E3 ubiquitin-protein ligase that down-regulates the tetraspanin CD81 and major histocompatibility complex-I (MHC). It also associates with Mult1, suppressing Mult1 expression at the cell surface in a lysine-dependent manner that can be reversed by heat shocking the cells. MARCH4 contains an N-terminal C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, followed by two transmembrane regions
GMRTPLCRICFQGPEQGELLSPCRCDGSVRCTHQPCLIKWISERGSWSCELCYYKY
>gnl|CDD|438474 cd16825, RING_CH-C4HC3_MARCH9, RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING-CH9 (MARCH9). MARCH9, also known as membrane-associated RING finger protein 9, membrane-associated RING-CH protein IX (MARCH-IX), or RING finger protein 179 (RNF179), is a transmembrane E3 ubiquitin-protein ligase that down-regulates Mult1, CD4, major histocompatibility complex-I (MHC), and intercellular adhesion molecule (ICAM-1). It may also interact with receptor-type protein-tyrosine phosphatases (e.g. PTPRJ/CD148) as well as Fc gamma receptor IIB (CD32B), HLA-DQ, signaling lymphocytic activation molecule (CD150), and polio virus receptor (CD155). MARCH9 contains an N-terminal C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, followed by two transmembrane regions
RTPQCRICFQGPEQGELLSPCRCDGSVRCTHQPCLIRWISERGSWSCELCYFKY
>gnl|CDD|319356 cd16827, ChuX-like, heme utilization protein ChuX and similar proteins. This family contains ChuX, a member of the conserved heme utilization operon from pathogenic E. coli, and similar proteins, which include ChuS, HutX, HuvX, HugX, and ShuX in proteobacteria, among others. It forms a dimer which displays a very similar fold and organization to the monomeric structure of other heme utilization proteins such as HemS, ChuS, HmuS, PhuS; these latter occurring as duplicated domains. They all bind heme via a key conserved histidine. The genes encoded within these heme utilization operons enable the effective uptake and utilization of heme as an iron source in pathogenic microorganisms to enable multiplication and survival within hosts they invade
AEDLAGQYNITEAEVVRALPTDQATKVPGDRFDEILEALEAWGEVTVIVRNRDAVLEFVGTFPKGFHRHG
WFNIRGDRTLDGHILAESCASIFAIEKPFHGGETASIQFFDHDGDAAFKIFLGRDEDEQLLAEQVEAFAT
L
>gnl|CDD|319357 cd16828, HemS-like, N- and C-terminal domains of heme degrading enzyme HemS, and similar proteins. This family contains the N- and C-terminal domains of heme degrading enzyme HemS, and similar proteins, including PhuS, ChuS, ShuS, and HmuS in proteobacteria. Despite low sequence identity between the N- and C-terminal halves, these segments represent a structural duplication, with each terminal half having similar fold to single domains of ChuX. HemS shares homology with both heme degrading enzymes and heme trafficking enzymes. Heme is an iron source for pathogenic microorganisms to enable multiplication and survival within hosts they invade and therefore heme degrading enzyme activity is required for the release of iron from heme after its transportation into the cytoplasm. N- and C-terminal halves of ChuS are each a functional heme oxygenase (HO). The mode of heme coordination by ChuS has been shown to be distinct, whereby the heme is stabilized mostly by residues from the C-terminal domain, assisted by a distant arginine from the N-terminal domain. ChuS can use ascorbic acid or cytochrome P450 reductase-NADPH as electron sources for heme oxygenation. Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicity by physically sequestering DNA. PhuS in Pseudomonas aeruginosa has been reported as a heme chaperone and as a heme degrading enzyme, and is unique among this family since it contains three histidines in the heme-binding pocket, compared with only one in ChuX. Heme transporter protein PhuS in Pseudomonas aeruginosa is unique among this family since it contains three histidines in the heme-binding pocket, compared with only one in ChuX
LYTRWLALKDQHPGKYARDLAKLHNIREAELAFLRVGHDAWRLHNDLAEILEALEEVGEIMVFVRNEHCV
HEQTGPVTNVHLNGHWGLILNPRFDLRLFLNGWAEVFHIREPTARGEVTSIQFFDHQGDAILKVYGARNT
DEAAWRELLARL
>gnl|CDD|319358 cd16829, ChuX_HutX-like, heme iron utilization protein ChuX and similar proteins. This family contains proteins similar to ChuX, a member of the conserved heme utilization operon from pathogenic E. coli, and includes ChuS, HutX, HuvX, HugX, and ShuX in proteobacteria, among others. It forms a dimer which displays a very similar fold and organization to the monomeric structure of other heme utilization proteins such as HemS, ChuS, HmuS, PhuS; these latter occurring as duplicated domains. They all bind heme via a key conserved histidine. The genes encoded within these heme utilization operons enable the effective uptake and utilization of heme as an iron source in pathogenic microorganisms to enable multiplication and survival within hosts they invade. ChuX, a member of the conserved heme utilization operon from pathogenic E. coli O157:H7, forms a dimer with a very similar fold to the monomer structure of two other heme utilization proteins, ChuS and HemS, despite low sequence homology. ChuX has been shown to bind heme in a 1:1 manner, inferring that the ChuX homodimer could coordinate two heme molecules in contrast to only one heme molecule bound in ChuS and HemS. Similarly, cytoplasmic heme-binding protein HutX in Vibrio cholera, an intracellular heme transport protein for the heme-degrading enzyme HutZ, forms a dimer, each domain binding heme that is transferred from HutX to HutZ via a specific protein-protein interaction. This family also includes AGR_C_4470p from Agrobacterium tumefaciens and found to be a dimer, with each subunit having strong structural homology and organization to the heme utilization protein ChuS from Escherichia coli and HemS from Yersinia enterocolitica. However, the heme binding site is not conserved in AGR_C_4470p, suggesting a possible different function
VLEELAAELGVSELEVVRALPEEMATFVPGEHFDEVWQELASWGEVTFIVHTPGSIFEFKGPLPKGKHGH
GYYNLHGKSGLGGHLKADNCAAIAFVSRPFMGKESHSVQFFNADGEAMFKIYVGRDEKRQLLPEQVEAFE
ALK
>gnl|CDD|319359 cd16830, HemS-like_N, N-terminal domain of heme degrading enzyme HemS, and similar proteins. This family contains the N-terminal domain of heme degrading enzyme HemS, and similar proteins, including PhuS, ChuS, ShuS, and HmuS in proteobacteria. Despite low sequence identity between the N- and C-terminal halves, these segments represent a structural duplication, with each terminal half having similar fold to single domains of ChuX. HemS shares homology with both heme degrading enzymes and heme trafficking enzymes. Heme is an iron source for pathogenic microorganisms to enable multiplication and survival within hosts they invade and therefore heme degrading enzyme activity is required for the release of iron from heme after its transportation into the cytoplasm. N- and C-terminal halves of ChuS are each a functional heme oxygenase (HO). The mode of heme coordination by ChuS has been shown to be distinct, whereby the heme is stabilized mostly by residues from the C-terminal domain, assisted by a distant arginine from the N-terminal domain. ChuS can use ascorbic acid or cytochrome P450 reductase-NADPH as electron sources for heme oxygenation. Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicity by physically sequestering DNA. Heme transporter protein PhuS in Pseudomonas aeruginosa is unique among this family since it contains three histidines in the heme-binding pocket, compared with only one in ChuX
LKQRWQALKAENPKLRARDAAARLGVSEAELLAARVGEGVTRLRPDWRALLKALESLGEVMALTRNESAV
HEKKGVYENVSLGGHMGLVLGPDIDLRLFLSHWHHAFAVEEETRGGPRRSLQFFDAAGDAVHKIYLTEES
DLAAWEALVARF
>gnl|CDD|319360 cd16831, HemS-like_C, C-terminal domain of heme degrading enzyme HemS, and similar proteins. This family contains the C-terminal domain of heme degrading enzyme HemS, and similar proteins, including PhuS, ChuS, ShuS, and HmuS in proteobacteria. Despite low sequence identity between the N- and C-terminal halves, these segments represent a structural duplication, with each terminal half having similar fold to single domains of ChuX. HemS shares homology with both, heme degrading enzymes and heme trafficking enzymes. Heme is an iron source for pathogenic microorganisms to enable multiplication and survival within hosts they invade and therefore heme degrading enzyme activity is required for the release of iron from heme after its transportation into the cytoplasm. N- and C-terminal halves of ChuS are each a functional heme oxygenase (HO). The mode of heme coordination by ChuS has been shown to be distinct, whereby the heme is stabilized mostly by residues from the C-terminal domain, assisted by a distant arginine from the N-terminal domain. ChuS can use ascorbic acid or cytochrome P450 reductase-NADPH as electron sources for heme oxygenation. Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicity by physically sequestering DNA. Heme transporter protein PhuS in Pseudomonas aeruginosa is unique among this family since it contains three histidines in the heme-binding pocket, compared with only one in ChuX
ALRADWRALTDVHDFFGLLRKFGVSRLQALRLAGEDFARQVDPDALEQLLEAAAEQGLPIMVFVGNRGCI
QIHTGPVKKIKRMGPWLNVLDPGFNLHLREDAIAEAWVVRKPTKDGIVTSLELFDADGELIAQFFGKRKP
GQPELAAWRELVASL
>gnl|CDD|319353 cd16832, CNF1_CheD_YfiH-like, cytotoxic necrotizing factor 1 (CNF1), chemotaxis protein CheD and YfiH (DUF152) are distant homologs. This family contains distant homologs that include cytotoxic necrotizing factor 1 (CNF1), chemotaxis protein CheD and a protein of unknown function YfiH. CNF-1 along with dermonecrotic toxin (DNT) from Bordetella species, and Burkholderia Lethal Factor 1 (BLF1, also known as BPSL1549) are Rho-activating toxins. The bacterial chemotaxis protein CheD stimulates methylation of methyl-accepting chemotaxis proteins (MCPs). YfiH, a domain of unknown function, also included in this family reveals a structure with a distant homology between to the CNF1, and CheD, all having an invariant Cys-His pair forming a catalytic dyad that is required by the CNF-1 toxins for deamidation activity
IIVVSNSARGANGIVIKLKPVIITSGNLSGCTTVVARDPGAKYIAKAHTGTTKSLAGFTSTTGVDKAVEV
LVLLTKEPGASENFEDSLITYSSSEKKPDSMNIGARNVEAVKKHLITIGRDNVSVFPYFLDNIPEHGFGT
SATVL
>gnl|CDD|319354 cd16833, YfiH, protein of unknown function YfiH. This subfamily contains YfiH, a protein of unknown function from Shigella flexneri, E. coli, and many similar proteins which collectively are often called DUF152. The structure of YfiH reveals a distant homology to Rho-activating toxins cytotoxic necrotizing factor 1 (CNF1) as well as chemotaxis protein CheD that stimulates methylation of methyl-accepting chemotaxis proteins (MCPs), all having an invariant Cys-His pair forming a catalytic dyad, and is required by the CNF-1 toxins for deamidation activity
RLVFLKQVHGVRVVDVDDAGGGTAIPEADALITNEPGVALAVLTADCVPVLLYDPKGGVIAAAHAGWRGT
VAGIVEKTVEAMKELGSDPEDILAAIGPSIGPCCYEVGEEVAEAFPAAFPEAAAFFKPGKYYLDLWAANR
LQLLEAGVPEENIEVSGLCTYCNDDRFFSYRRDGGKTGRMAAVIG
>gnl|CDD|319355 cd16834, CNF1-like, cytotoxic necrotizing factor 1 (CNF1) and similar proteins. This subfamily contains Rho-activating toxins cytotoxic necrotizing factor 1 (CNF1) and dermonecrotic toxin (DNT) from Bordetella species, as well as Burkholderia Lethal Factor 1 (BLF1, also known as BPSL1549), and similar proteins. CNF1 causes alteration of the host cell actin cytoskeleton and promotes bacterial invasion of blood-brain barrier endothelial cells. E. coli CNF1 constitutively activates host small G proteins such as RhoA and Cdc42 by deamidating a glutamine residue essential for GTP hydrolysis. DNT stimulates the assembly of actin stress fibers and focal adhesions by deamidation/polyamination of a specific glutamine of the small GTPase Rho. CNF1 and DNT are A-B toxins composed of an N-terminal receptor-binding (B) domain and a C-terminal enzymatically active (A) domain; their homology is restricted to the catalytic domains at the C termini of the toxins, suggesting that they share a similar molecular mechanism. BLF1, a toxin that inhibits helicase activity of translation factor eIF4A, is similar to the catalytic domain of Escherichia coli CNF1 (CNF1-C); although CNF1-C and BLF1 show little sequence identity, the active sites have the conserved LSGC (Leu, Ser, Gly, Cys) motif
VKVIEVPNGNSGTVGIKIPLDDIKEGKPILITSGALSGCTMVYAVKGGYFYAYHAGQPTNDDKWKTGVDG
VASIYRAHLALTGEDPPDSGPVNNNDLLVYLSETFDQATITYSGQGGKGTKITRNSENVSVFDYNKDKAN
YNPRVGNAYALLTKDGGNVKISTLSEDM
>gnl|CDD|319351 cd16837, BldD_C_like, C-terminal domain of BldD and similar transcription factors. The Streptomyces transcription factor BldD dimerizes via an unusual mechanism that inolves a tetrameric c-di-GMP assembly. BdlD is involved in controlling multicellular differentiation in sporulating actinomycetes
AGKLVLDLERLRSAPDPEAEPLRRYARSIQRQRGDWNGRVLTIRADDLRALALLLGTTPEELIERLEEWG
LLA
>gnl|CDD|319350 cd16839, PCSK9_C-CRD, proprotein convertase subtilisin/kexin type 9, C-terminal cysteine-rich domain (CRD). PCSK9 post-translationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. Other known PSCK9 targets include very-low-density lipoprotein receptor (VLDLR), apoE receptor2, lipoprotein receptor-related protein 1, etc. This PCSK9 C-terminal CRD may play an analogous role to the P (processing) domains of Furin and Kex2 (i.e. be required for the correct functioning/folding of the protein). Structural similarity has been noted between PCSK9 C-terminal CRD and the resistin homotrimer. This alignment model represents a three-fold repeat
GEQLFCRSVWSARSGPTRMATAVARCAGDEEMLSCSSFSRSGKRRGERMEAQGGQKVCVAHNAFGGEGVY
AIARCCLWPQANCQVHTSPPAEASMGTGAHCSQQGHVLTGCSSHSEVGDLGDHKRPVLRPRGQPNQCVGK
REVTSHASCCHAPSLECKVKEHGSPAPQEQVTVSCEEGWTLTGCSALSGTSHTLGAYAVDNTCVVRSRDV
SKGATAVAICCRSRH
>gnl|CDD|411037 cd16840, toxin_MLD, toxin effector region membrane localization domain. This MLD domain functions as a membrane-targeting domain for toxin effectors such as the Rho-inactivation domain of Vibrio MARTX, Pasteurella mitogenic toxin (PMT), where it has been termed PMT C1 domain, and clostridial glycosylating cytotoxins including Clostridium difficile toxins A (TcdA) and B (TcdB), Clostridium novyi alpha-toxin (TcnA), and Clostridium sordellii lethal toxin (TcsL). During infection, the C. difficile homologous exotoxins, TcdA and TcdB, target and disrupt the colonic epithelium, leading to diarrhea and colitis. They disrupt host cell function through a multistep process involving receptor binding, endocytosis, low pH-induced pore formation, and the translocation and delivery of a C-terminal glucosyltransferase domain (GTD) that inactivates host GTPases. Their N-terminal MLD domains confer membrane localization of adjacent effector domains via the 4-helix-bundle motif
MSRDELKKAASVFGKPIGESYQAILDALDRYHNTSGDEKIEKLFELNNQIDGYLEKHPDSGRNPALKKLK
QQLNSALF
>gnl|CDD|319245 cd16841, RraA_family, ribonuclease activity regulator RraA family. RraA protein family is named after the regulator of ribonuclease activity A (RraA), a protein that binds to RNase E and inhibits RNase E endonucleolytic cleavages. Members also include proteins with other functions, like a 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate (HMG/CHA) aldolase from Pseudomonas putida, which catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway and the uncharacterized YER010Cp protein from yeast, an organism lacking RNAse E
ADLSDALDRLGGVLPGIIRPLGGGARFVGPAVTVKCFPDDNLLVREALDEAGPGDVLVVDGGGSLRCALW
GDLLATLAKARGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKKVGPGEVNVPVTIGGVTVNPGDII
VADEDGVVVI
>gnl|CDD|409517 cd16842, Ig_SLAM-like_N, N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family. The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family and similar proteins. The SLAM family is a group of immune-cell specific receptors that can regulate both adaptive and innate immune responses. Members of this group include proteins such as CD84, SLAM (CD150), Ly-9 (CD229), NTB-A (ly-108, SLAM6), 19A (CRACC), and SLAMF9. The genes coding for the SLAM family are nested on chromosome 1, in humans at 1q23, and in mice at 1H2. The SLAM family is a subset of the CD2 family, which also includes CD2 and CD58 located on chromosome 1 at 1p13 in humans. In mice, CD2 is located on chromosome 3, and there is no CD58 homolog. The SLAM family proteins are organized as an extracellular domain with either two or four Ig-like domains, a single transmembrane segment, and a cytoplasmic region having Tyr-based motifs. The extracellular domain is organized as a membrane-distal Ig variable (IgV) domain that is responsible for ligand recognition and a membrane-proximal truncated Ig constant-2 (IgC2) domain
KEVNGILGGSVTFPLNISDGQEIENITWSFKTSLAVIAPGEGGAPEIIITDKSYKERLNISQNDYSLQIS
NLTMEDAGSYRARINTKNSRVTITKEFTLHIY
>gnl|CDD|409518 cd16843, IgC2_D1_D2_LILR_KIR_like, Immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors, Natural killer inhibitory receptors (KIRs) and similar domains; member of Immunoglobulin Constant-2 set of IgSF domains. The members here are composed of the first and second immunoglobulin (Ig)-like domains found in Leukocyte Ig-like receptors (LILRs), Natural killer inhibitory receptors (KIRs, also known as also known as cluster of differentiation (CD) 158), and similar proteins. This group includes LILRB1 (also known as LIR-1), LILRA5 (also known as LIR9), an activating natural cytotoxicity receptor NKp46, the immune-type receptor glycoprotein VI (GPVI), and the IgA-specific receptor Fc-alphaRI (also known as cluster of differentiation (CD) 89). LILRs are a family of immunoreceptors expressed on expressed on T and B cells, on monocytes, dendritic cells, and subgroups of natural killer (NK) cells. The human LILR family contains nine proteins (LILRA1-3, and 5, and LILRB1-5). From functional assays, and as the cytoplasmic domains of various LILRs, for example LILRB1, LILRB2 (also known as LIR-2), and LILRB3 (also known as LIR-3) contain immunoreceptor tyrosine-based inhibitory motifs (ITIMs), it is thought that LIR proteins are inhibitory receptors. Of the eight LIR family proteins, only LILRB1, and LILRB2, show detectable binding to class I MHC molecules; ligands for the other members have yet to be determined. The extracellular portions of the different LIR proteins contain different numbers of Ig-like domains for example, four in the case of LILRB1, and LILRB2, and two in the case of LILRB4 (also known as LIR-5). The activating natural cytotoxicity receptor NKp46 is expressed in natural killer cells, and is organized as an extracellular portion having two Ig-like extracellular domains, a transmembrane domain, and a small cytoplasmic portion. GPVI, which also contains two Ig-like domains, participates in the processes of collagen-mediated platelet activation and arterial thrombus formation. Fc-alphaRI is expressed on monocytes, eosinophils, neutrophils, and macrophages; it mediates IgA-induced immune effector responses such as phagocytosis, antibody-dependent cell-mediated cytotoxicity and respiratory burst. Killer cell immunoglobulin-like receptors (KIRs; also known as CD158 for human KIR) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. KIRs are a family of highly polymorphic activating and inhibitory receptors that serve as key regulators of human NK cell function. The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The major ligands for KIR are MHC class I (HLA-A, -B or -C) molecules
KPFLSAEPSSVVPLGENVTIRCQGPPEAVLFQLYKEGNSLSQGTVREKEPQNKAEFYIPHMDRNHAGRYR
CRYRSGTLWSEPSDPLELVV
>gnl|CDD|319272 cd16844, ParB_N_like_MT, ParB N-terminal-like domain, some attached to C-terminal S-adenosylmethionine-dependent methyltransferase domain. This family represents domains related to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system, fused to a variety of C-terminal domains, including S-adenosylmethionine-dependent methyltransferase-like domains and DUF4417. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci
KNDAQIERVAASIREFGFRVPVLIDKDGEIVDGHLRLEAARRLGLETVPVIRVD
>gnl|CDD|341083 cd16845, STAT1_DBD, DNA-binding domain of Signal Transducer and Activator of Transcription 1 (STAT1). This family consists of the DNA-binding domain (DBD) of the STAT1 proteins (Signal Transducer and Activator of Transcription 1, or Signal Transduction And Transcription 1). The DNA binding domain has an Ig-like fold. STAT1 plays an essential role in mediating responses to all types of interferons (IFN), transducing signals from cytoplasmic domains of transmembrane receptors into the nucleus where it regulates gene expression. Thus STAT1 is involved in modulating diverse cellular processes, such as antimicrobial activities, cell proliferation and cell death. STAT1 function is crucial in the innate and adaptive arm of immunity and protects from pathogen infections; phosphorylation of a critical tyrosine by Janus kinases (JAKs) leads to its activation and nuclear translocation, while phosphorylation of a critical serine is required for full transcriptional activation upon IFN stimulation and in response to cellular stress. Transcription of protein-encoding genes (including Stat1 itself) as well as expression of microRNAs (miRNAs) is regulated by activated STAT1. Animal studies have shown that STAT1 is generally considered a tumor suppressor but it can also act as a tumor promoter; its functions are not restricted to tumor cells, but extend to parts of the tumor microenvironment such as immune cells, endothelial cells. STAT1 abundance is a reliable marker for good prognosis in selected tumor types, but it can also correlate with disease progression. In head and neck cancer (HNC) patients, upregulation of STAT1-induced HLA class I enhances immunogenicity and clinical response to anti-EGFR mAb cetuximab therapy. In systemic juvenile idiopathic arthritis (sJIA) characterized by systemic inflammation and arthritis, STAT1 phosphorylation downstream of IFNs is impaired. It exerts anti-oncogenic activities through interferon-gamma and interferon-alpha. STAT1 may inhibit hepatocellular carcinoma cell growth by regulating p53-related cell cycling and apoptosis. Studies also show a significant correlation of high STAT1 activity with longer colorectal cancer patient overall survival. Recent studies have shown that STAT1 suppresses mouse mammary gland tumorigenesis by immune regulatory as well as tumor cell-specific functions of STAT1
FVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQELNYQLKVKVLFDKDVTEKNTVKGFRKFNILGTN
TKVMNMEESTNGSLAAEFRHLQLKEQKNAGTRTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPIV
VISNVSQLPSGWASILWYNML
>gnl|CDD|341084 cd16846, STAT2_DBD, DNA-binding domain of Signal Transducer and Activator of Transcription 2 (STAT2). This family consists of the DNA-binding domain (DBD) of the STAT2 proteins (Signal Transducer and Activator of Transcription 2, or Signal Transduction And Transcription 2). The DNA binding domain has an Ig-like fold. STAT2 activation is driven predominantly by only two classes of cell surface receptors: Type I and III interferon receptors, making it a unique STAT family of transcription factors. Thus, STAT2 plays a critical role in host defenses against viral infections since type I interferon (IFN-I) response inhibits viral replication, and sets the stage for the development of adaptive immunity; viruses target STAT2 by either inhibiting its expression, blocking its activity, or by targeting it for degradation, thus triggering remarkable divergence in the STAT2 gene across species compared to other STAT family members. STAT2 function is regulated by tyrosine phosphorylation which enables STAT dimerization, and subsequent nuclear translocation and transcriptional activation of IFN stimulated genes. Dengue virus (DENV)-mediated degradation of STAT2 has emerged as an important determinant of DENV pathogenesis and host tropism. This vector-borne flavivirus suppresses IFN1 signaling to replicate and cause disease in vertebrates via proteasome-dependent STAT2 degradation mediated by the nonstructural protein NS5 and its interaction partner UBR4, an E3 ubiquitin ligase. The mechanism of Zika virus (ZIKV) NS5 resembles DENV NS5 but through different mechanism - ZIKV does not require the UBR4 to induce STAT2 degradation. It has also been shown that the STAT2 and STAT4 genes are direct targets for transcription factor Oct-1 protein which is involved in the regulation of expression of genes of the JAK-STAT signaling pathway in the Namalwa Burkitt's lymphoma cell line
FVVETQPCMPQPPRRPLVLKTNTQFSVRVRLLVKLPELNHSLKVEVSVDKNPPNSKGFRRFNILGTNNKT
LNMDEGQSGGLVADFRHLTLKEQKVGGGGKGSNEGSLSVTEELHLITFTTDYKYQGLKVKLETSTLPVVV
ISNMSQLSSAWASVLWFNLL
>gnl|CDD|341085 cd16847, STAT3_DBD, DNA-binding domain of Signal Transducer and Activator of Transcription 3 (STAT3). This family consists of the DNA-binding domain (DBD) of the STAT3 proteins (Signal Transducer and Activator of Transcription 3, or Signal Transduction And Transcription 3). The DNA binding domain has an Ig-like fold. STAT3 plays key roles in vertebrate development and mature tissue function including control of inflammation and immunity. Mutations in human STAT3, especially in the DNA-binding and SH2 domains, are associated with diseases such as autoimmunity, immunodeficiency and cancer. STAT3 regulation is tightly controlled since either inactivation or hyperactivation results in disease. STAT3 activation is stimulated by several cytokines and growth factors, via diverse receptors. For example, IL-6 receptors depend on the tyrosine kinases JAK1 or JAK2, which associate with the cytoplasmic tail of gp130, and results in STAT3 phosphorylation, dimerization, and translocation to the nucleus; this leads to further IL-6 production and up-regulation of anti-apoptotic genes, thus promoting various cellular processes required for cancer progression. Other activators of STAT3 include IL-10, IL-23, and LPS activation of Toll-like receptors TLR4 and TLR9. STAT3 is constitutively activated in numerous cancer types, including over 40% of breast cancers. It has been shown to play a significant role in promoting acute myeloid leukemia (AML) through three mechanisms: promoting proliferation and survival, preventing AML differentiation to functional dendritic cells (DCs), and blocking T-cell function through other pathways. STAT3 also regulates mitochondrion functions, as well as gene expression through epigenetic mechanisms; its activation is induced by overexpression of Bcl-2 via an increase in mitochondrial superoxide. Thus, many of the regulators and functions of JAK-STAT3 in tumors are important therapeutic targets for cancer treatment
FVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTN
TKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLP
VVVISNICQMPNAWASILWYNMLT
>gnl|CDD|341086 cd16848, STAT4_DBD, DNA-binding domain of Signal Transducer and Activator of Transcription 4 (STAT4). This family consists of the DNA-binding domain (DBD) of the STAT4 proteins (Signal Transducer and Activator of Transcription 4, or Signal Transduction And Transcription 4). The DNA binding domain has an Ig-like fold. STAT4 acts as the major signaling transducing STATs in response to interleukin-12 (IL-12) by inducing interferon-gamma (IFNg), and is a central mediator in generating inflammation during protective immune responses and immune-mediated diseases. STAT4 is a critical regulator of Th1 differentiation and inflammatory disease. It is essential for the differentiation and function of many immune cells, including natural killer cells, dendritic cells, mast cells and T helper cells. STAT4-mediated signaling promotes the production of autoimmune-associated components, which are implicated in the pathogenesis of autoimmune diseases, such as rheumatoid arthritis, systemic lupus erythematosus, systemic sclerosis and psoriasis, making STAT4 a promising therapeutic target for autoimmune diseases. Variations in STAT4 gene are linked to the development of systemic lupus erythematosus (SLE) in humans. STAT4 activation is detected in chronic liver diseases; polymorphism in STAT4 gene has been shown to be associated with the antiviral response in primary biliary cirrhosis (PBC), HCV-associated liver fibrosis, hepatocellular carcinoma (HCC), chronic hepatitis C and in drug-induced liver injury (DILI). STAT4 may inhibit HCC development by modulating HCC cell proliferation. Studies show that increased expression of STAT4 is positively correlated with the depth of invasion in colorectal cancer (CRC) patients, and the growth and invasion of CRC cells are repressed by inhibition of STAT4 expression, making STAT4 a promising therapeutic target for the treatment of CRC
FVVERQPCMPTHPQRPMVLKTLIQFTVKLRLLIKLPELNYQIRVKATIDNNRRFVLCGTHVKAMNLEESV
NGSLSVEFRHLQPKEMKPSGGSKGNEGPHMVTEELHSISFETQFSLYGLTIDLETSSLPVVMISNVSQLP
NAWASIIWYNLL
>gnl|CDD|341087 cd16849, STAT5_DBD, DNA-binding domain of Signal Transducer and Activator of Transcription 5 (STAT5). This family consists of the DNA-binding domain (DBD) of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 4), which include STAT5A and STAT5B, both of which are _90% identical despite being encoded by separate genes. The DNA binding domain has an Ig-like fold. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency
FIIEKQPPQVLKTQTRFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKALLKNENITRNETSGEILNNC
GVMEYHQATGQLSVSFRNMSLKRIKRADKRGAESVTEEKFTILFQSQFSVGGNELVFQVWTLSLPVVVIV
HGNQESNATATVLWDNAFA
>gnl|CDD|341088 cd16850, STAT6_DBD, DNA-binding domain of Signal Transducer and Activator of Transcription 6 (STAT6). This family consists of the DNA-binding domain (DBD) of the STAT6 proteins (Signal Transducer and Activator of Transcription 6, or Signal Transduction And Transcription 6). The DNA binding domain has an Ig-like fold. STAT6 is essential for the functional responses of T helper 2 (Th2) lymphocyte mediated by interleukins IL-4 and IL-13. STAT6 almost exclusively mediates the expression of genes activated by these cytokines; IL-4 signaling regulates the expression of genes involved in immune and anti-inflammatory responses. Abnormal production of IL-4 and IL-13 play important roles in the pathogenesis of asthma where upregulation of the Th2 response mediated by IL-4/IL-13 is a main characteristic. STAT6 has a unique extended transactivation domain, not found in other STATs, through which it recruits p300/CBP and NCoA-1, two coactivators needed for transcriptional activation by IL-4. STAT6 activation is linked to Kaposi's sarcoma-associated herpesvirus (KSHV)-associated cancers such as primary effusion lymphoma, a cancerous proliferation of B cells. Studies show that Meningeal solitary fibrous tumor (SFT) and hemangiopericytoma (HPC) represent a histopathologic spectrum linked by STAT6 nuclear expression and recurrent somatic fusions of the two genes, NGFI-A-binding protein 2 (NAB2) and STAT6 (NAB2-STAT6), similar to their soft tissue counterparts. It is associated with local recurrence and late distance metastasis of brain tumors to extracranial sites
FLVEKQPPQVLKTQTKFQAGVRFLLGLRFLGAPAKPPLVRADMVTEKQARELSQPQGPGAGNENTGEIIN
NTVPLENNITSKCCCATFKNLLLKKIKRCERKGSESVTEEKCAVLFSADFTLGPGKLPIQLQALSLPVVV
IVHGNQDNNAKATILWDNAF
>gnl|CDD|341076 cd16851, STAT1_CCD, Coiled-coil domain of Signal Transducer and Activator of Transcription 1 (STAT1). This family consists of the coiled-coil (alpha) domain of the STAT1 proteins (Signal Transducer and Activator of Transcription 1, or Signal Transduction And Transcription 1). STAT1 plays an essential role in mediating responses to all types of interferons (IFN), transducing signals from cytoplasmic domains of transmembrane receptors into the nucleus where it regulates gene expression. Thus STAT1 is involved in modulating diverse cellular processes, such as antimicrobial activities, cell proliferation and cell death. STAT1 function is crucial in the innate and adaptive arm of immunity and protects from pathogen infections; phosphorylation of a critical tyrosine by Janus kinases (JAKs) leads to its activation and nuclear translocation, while phosphorylation of a critical serine is required for full transcriptional activation upon IFN stimulation and in response to cellular stress. Transcription of protein-encoding genes (including Stat1 itself) as well as expression of microRNAs (miRNAs) is regulated by activated STAT1. Animal studies have shown that STAT1 is generally considered a tumor suppressor but it can also act as a tumor promoter; its functions are not restricted to tumor cells, but extend to parts of the tumor microenvironment such as immune cells, endothelial cells. STAT1 abundance is a reliable marker for good prognosis in selected tumor types, but it can also correlate with disease progression. In head and neck cancer (HNC) patients, upregulation of STAT1-induced HLA class I enhances immunogenicity and clinical response to anti-EGFR mAb cetuximab therapy. In systemic juvenile idiopathic arthritis (sJIA) characterized by systemic inflammation and arthritis, STAT1 phosphorylation downstream of IFNs is impaired. It exerts anti-oncogenic activities through interferon-gamma and interferon-alpha. STAT1 may inhibit hepatocellular carcinoma cell growth by regulating p53-related cell cycling and apoptosis. Studies also show a significant correlation of high STAT1 activity with longer colorectal cancer patient overall survival. Recent studies have shown that STAT1 suppresses mouse mammary gland tumorigenesis by immune regulatory as well as tumor cell-specific functions of STAT1
KQKELDAKVKDLKNSVQDAEQDIKSLEDLQDEYDFKRKTLQSREEETNGVAKEELKKEKLKLRKMFIKLK
DKRKEVVHKIIELLNVTELTQFALINDELVEWKRRQQMACIGGPPNACLDQLQNWFTIVAESLQQVRQQL
KKLQELEQKLTYENDPITKNKQALEERALSLFKNLI
>gnl|CDD|341077 cd16852, STAT2_CCD, Coiled-coil domain of Signal Transducer and Activator of Transcription 2 (STAT2). This family consists of the coiled-coil (alpha) domain of the STAT2 proteins (Signal Transducer and Activator of Transcription 2, or Signal Transduction And Transcription 2). STAT2 activation is driven predominantly by only two classes of cell surface receptors: Type I and III interferon receptors, making it a unique STAT family of transcription factors. It differs from other STAT family members in that it associates constitutively with a non-STAT protein, the interferon regulatory factor 9 (IRF9). The coiled-coil domain of STAT2 is necessary for binding the carboxyl terminus of IRF9, an association required for the constitutive nuclear import of unphosphorylated STAT2. STAT2 plays a critical role in host defenses against viral infections since type I interferon (IFN-I) response inhibits viral replication, and sets the stage for the development of adaptive immunity; viruses target STAT2 by either inhibiting its expression, blocking its activity, or by targeting it for degradation, thus triggering remarkable divergence in the STAT2 gene across species compared to other STAT family members. STAT2 function is regulated by tyrosine phosphorylation which enables STAT dimerization, and subsequent nuclear translocation and transcriptional activation of IFN stimulated genes. Dengue virus (DENV)-mediated degradation of STAT2 has emerged as an important determinant of DENV pathogenesis and host tropism. This vector-borne flavivirus suppresses IFN1 signaling to replicate and cause disease in vertebrates via proteasome-dependent STAT2 degradation mediated by the nonstructural protein NS5 and its interaction partner UBR4, an E3 ubiquitin ligase. The mechanism of Zika virus (ZIKV) NS5 resembles DENV NS5 but through different mechanism - ZIKV does not require the UBR4 to induce STAT2 degradation. It has also been shown that the STAT2 and STAT4 genes are direct targets for transcription factor Oct-1 protein which is involved in the regulation of expression of genes of the JAK-STAT signaling pathway in the Namalwa Burkitt's lymphoma cell line
RQHEIEKRINDLKTRIQCLEHSIRQLEDLQDTFDFKYKTHTMDKSTSPDDKQTKQQQILQGMLNELDRFR
KEVLSKMKVLLGRRDTLRELLLEELVEWKRRQQKACIGAPDDTSLEQLEKWFTKVAECLFQLRKFLKKLE
ELMGKVSYEHDPLKKQKPLLQQRVDELLTSLL
>gnl|CDD|341078 cd16853, STAT3_CCD, Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3). This family consists of the coiled-coil (alpha) domain of the STAT3 proteins (Signal Transducer and Activator of Transcription 3, or Signal Transduction And Transcription 3). STAT3 continuously shuttles between nuclear and cytoplasmic compartments. The coiled-coil domain (CCD) of STAT3 appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the STAT3 CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 in the testis, and importin-alpha6 NLS adapters in most cells. STAT3 plays key roles in vertebrate development and mature tissue function including control of inflammation and immunity. Mutations in human STAT3, especially in the DNA-binding and SH2 domains, are associated with diseases such as autoimmunity, immunodeficiency and cancer. STAT3 regulation is tightly controlled since either inactivation or hyperactivation results in disease. STAT3 activation is stimulated by several cytokines and growth factors, via diverse receptors. For example, IL-6 receptors depend on the tyrosine kinases JAK1 or JAK2, which associate with the cytoplasmic tail of gp130, and results in STAT3 phosphorylation, dimerization, and translocation to the nucleus; this leads to further IL-6 production and up-regulation of anti-apoptotic genes, thus promoting various cellular processes required for cancer progression. Other activators of STAT3 include IL-10, IL-23, and LPS activation of Toll-like receptors TLR4 and TLR9. STAT3 is constitutively activated in numerous cancer types, including over 40% of breast cancers. It has been shown to play a significant role in promoting acute myeloid leukemia (AML) through three mechanisms: promoting proliferation and survival, preventing AML differentiation to functional dendritic cells (DCs), and blocking T-cell function through other pathways. STAT3 also regulates mitochondrion functions, as well as gene expression through epigenetic mechanisms; its activation is induced by overexpression of Bcl-2 via an increase in mitochondrial superoxide. Thus, many of the regulators and functions of JAK-STAT3 in tumors are important therapeutic targets for cancer treatment
EKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLT
ALDQMRRQIVSELAGLLSAMEYVQKNLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTR
QQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMK
>gnl|CDD|341079 cd16854, STAT4_CCD, Coiled-coil domain of Signal Transducer and Activator of Transcription 4 (STAT4). This family consists of the coiled-coil (alpha) domain of the STAT4 proteins (Signal Transducer and Activator of Transcription 4, or Signal Transduction And Transcription 4). STAT4 expression is restricted to spermatozoa, myeloid cells, and T lymphocytes, making it distinct from other STATs. It acts as the major signaling transducing STATs in response to interleukin-12 (IL-12) by inducing interferon-gamma (IFNgamma), and is a central mediator in generating inflammation during protective immune responses and immune-mediated diseases. STAT4 is a critical regulator of Th1 differentiation and inflammatory disease. It is essential for the differentiation and function of many immune cells, including natural killer cells, dendritic cells, mast cells and T helper cells. STAT4-mediated signaling promotes the production of autoimmune-associated components, which are implicated in the pathogenesis of autoimmune diseases, such as rheumatoid arthritis, systemic lupus erythematosus, systemic sclerosis and psoriasis, making STAT4 a promising therapeutic target for autoimmune diseases. Variations in STAT4 gene are linked to the development of systemic lupus erythematosus (SLE) in humans. STAT4 activation is detected in chronic liver diseases; polymorphism in STAT4 gene has been shown to be associated with the antiviral response in primary biliary cirrhosis (PBC), HCV-associated liver fibrosis, hepatocellular carcinoma (HCC), chronic hepatitis C and in drug-induced liver injury (DILI). STAT4 may inhibit HCC development by modulating HCC cell proliferation. Studies show that increased expression of STAT4 is positively correlated with the depth of invasion in colorectal cancer (CRC) patients, and the growth and invasion of CRC cells are repressed by inhibition of STAT4 expression, making STAT4 a promising therapeutic target for the treatment of CRC
QRNVEHKVSAIKNSVQMTDQDTKYLEDLQDEFDFRYKTIQTMDQGDKNSILMKQEVTTLQEMLNSLDFKR
KEALSKMTQIINEIDLLMSSMLTEELKDWKRRQQIACIGGPLHGGLDQLQNWFTLLAESLFQLRRQLEKL
DELSTKVTYEGDPIPLQRPQLLERVTFLIYNLF
>gnl|CDD|341080 cd16855, STAT5_CCD, Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5). This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are _90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency
DSHLEIRQQLEELRQRTQETENDLRNLQQKQESFVIQYQESQKIQAQLQQLQQQPQNERIELEQQLQQQK
EQLEQLLNAKAQELLQLRMELADKFKKTIQLLSKLQSRVLDEELIQWKRQQQLAGNGAPFESNLDTIQEW
CESLAEIIWQNRQQIKRAERLKQKLPIPLPPEQKDMLPILNKQITDLLSSLVTS
>gnl|CDD|341081 cd16856, STAT6_CCD, Coiled-coil domain of Signal Transducer and Activator of Transcription 6 (STAT6). This family consists of the coiled-coil (alpha) domain of the STAT6 proteins (Signal Transducer and Activator of Transcription 6, or Signal Transduction And Transcription 6). SImilar to STAT3 and STAT5. the coiled-coil domain (CCD) of STAT6 is required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells.STAT6 is essential for the functional responses of T helper 2 (Th2) lymphocyte mediated by interleukins IL-4 and IL-13. STAT6 almost exclusively mediates the expression of genes activated by these cytokines; IL-4 signaling regulates the expression of genes involved in immune and anti-inflammatory responses. Abnormal production of IL-4 and IL-13 play important roles in the pathogenesis of asthma where upregulation of the Th2 response mediated by IL-4/IL-13 is a main characteristic. STAT6 has a unique extended transactivation domain, not found in other STATs, through which it recruits p300/CBP and NCoA-1, two coactivators needed for transcriptional activation by IL-4. STAT6 activation is linked to Kaposi's sarcoma-associated herpesvirus (KSHV)-associated cancers such as primary effusion lymphoma, a cancerous proliferation of B cells. Studies show that Meningeal solitary fibrous tumor (SFT) and hemangiopericytoma (HPC) represent a histopathologic spectrum linked by STAT6 nuclear expression and recurrent somatic fusions of the two genes, NGFI-A-binding protein 2 (NAB2) and STAT6 (NAB2-STAT6), similar to their soft tissue counterparts. It is associated with local recurrence and late distance metastasis of brain tumors to extracranial sites
GEKAAVLLRPQHLPLSIHQLQEELKFDVENLELQHRVGQIHRLQLSLQQEKKSERIQQQEANGTSPLQER
AQLLQEAVGELEQAQSQVLKRIQIWKRQQQLAGNGAPFDENLSPLQTRCEQLVDVNFQLRQEVMLAGGEL
GSELLSTLQERLNSLLQTLIQSSLVVE
>gnl|CDD|341090 cd16857, ING_ING1_2, Inhibitor of growth (ING) domain of inhibitor of growth protein ING1, ING2, and similar proteins. ING1 is an epigenetic regulator and a type II tumor suppressor that impacts cell growth, aging, apoptosis, and DNA repair, by affecting chromatin conformation and gene expression. It acts as a reader of the active chromatin mark, the trimethylation of histone H3 lysine 4 (H3K4me3). It binds and directs growth arrest and DNA damage inducible protein 45 a (Gadd45a) to target sites, thus linking the histone code with DNA demethylation. It interacts with the proliferating cell nuclear antigen (PCNA) via the PCNA-interacting protein (PIP) domain in a UV-inducible manner. It also interacts with a PCNA-interacting protein, p15 (PAF). Moreover, ING1 associates with members of the 14-3-3 family, which is necessary for cytoplasmic relocalization. Endogenous ING1 protein specifically interacts with the pro-apoptotic BCL2 family member BAX and colocalizes with BAX in a UV-inducible manner. It stabilizes the p53 tumor suppressor by inhibiting polyubiquitination of multi-monoubiquitinated forms via interaction with and colocalization of the herpesvirus-associated ubiquitin-specific protease (HAUSP)-deubiquitinase with p53. It is also involved in trichostatin A-induced apoptosis and caspase 3 signaling in p53-deficient glioblastoma cells. In addition, tyrosine kinase Src can bind and phosphorylate ING1 and further regulates its activity. ING2, also termed inhibitor of growth 1-like protein (ING1Lp), or p32, or p33ING2, is a core component of a multi-factor chromatin-modifying complex containing the transcriptional co-repressor SIN3A and histone deacetylase 1 (HDAC1). It has been implicated in the control of cell cycle, in genome stability, and in muscle differentiation. ING2 independently interacts with H3K4me3 (Histone H3 trimethylated on lysine 4) and PtdIns(5)P, and modulates crosstalk between lysine methylation and lysine acetylation on histone proteins through association with chromatin in the presence of DNA damage. It collaborates with SnoN to mediate transforming growth factor (TGF)-beta-induced Smad-dependent transcription and cellular responses. It is upregulated in colon cancer and increases invasion by enhanced MMP13 expression. It also acts as a cofactor of p300 for p53 acetylation and plays a positive regulatory role during p53-mediated replicative senescence. Both ING1 and ING2 contain an N-terminal leucine zipper-like (LZL) motif-containing ING domain, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain
LDCVENLPGDVQRNLSLMRELDKRYQEILNELEELYEEYLREDDESHAKKRLLARIQKLLIRSQELGDEK
LQIVSQILDLIENRNRQLE
>gnl|CDD|341091 cd16858, ING_ING3_Yng2p, Inhibitor of growth (ING) domain of inhibitor of growth protein 3 (ING3), Yng2p and similar proteins. ING3, also termed p47ING3, is a member of the inhibitor of growth (ING) family of type II tumor suppressors. It is ubiquitously expressed and has been implicated in transcription modulation, cell cycle control, and the induction of apoptosis. It is an important subunit of human NuA4 histone acetyltransferase complex, which regulates the acetylation of histones H2A and H4. Moreover, ING3 promotes ultraviolet (UV)-induced apoptosis through the Fas/caspase-8-dependent pathway in melanoma cells. It physically interacts with subunits of E3 ligase Skp1-Cullin-F-boxprotein complex (SCF complex) and is degraded by the SCF (F-box protein S-phase kinase-associated protein 2, Skp2)-mediated ubiquitin-proteasome system. It also acts as a suppression factor during tumorigenesis and progression of hepatocellular carcinoma (HCC). Yeast chromatin modification-related protein Yng2p, also termed ESA1-associated factor 4 or ING1 homolog 2, is a subunit of the NuA4 histone acetyltransferase (HAT) complex. It plays a critical role in intra-S-phase DNA damage response. Members of this family contain an N-terminal leucine zipper-like (LZL) motif-containing ING domain, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain
LENLPSELRHLLTEIREKDLQVQELLDRIQQRDAKLFKHIKKNGSLTPNPKEEELYEKIREDYDKALELA
DEKVELANRLLDLVDRHLRRLD
>gnl|CDD|341092 cd16859, ING_ING4_5, Inhibitor of growth (ING) domain of inhibitor of growth protein ING4, ING5, and similar proteins. ING4, also termed p29ING4, and ING5, also termed p28ING5, belong to the inhibitor of growth (ING) family of type II tumor suppressors. ING4 acts as an E3 ubiquitin ligase to induce ubiquitination of the p65 subunit of NF-kappaB and inhibit the transactivation of NF-kappaB target genes. It also induces apoptosis through a p53 dependent pathway, including increasing p53 acetylation, inhibiting Mdm2-mediated degradation of p53, and enhancing the expression of p53 responsive genes both at the transcriptional and post-translational levels. Moreover, ING4 can inhibit the translation of proto-oncogene MYC by interacting with AUF1. It also regulates other transcription factors, such as hypoxia-inducible factor (HIF). ING5 is a Tip60 cofactor that acetylates p53 at K120 and subsequently activates the expression of p53-dependent apoptotic genes in response to DNA damage. Aberrant ING5 expression may contribute to pathogenesis, growth, and invasion of gastric carcinomas and colorectal cancer. ING5 can physically interact with p300 and p53 in vivo, and its overexpression induces apoptosis in colorectal cancer cells. It also associates with Inhibitor of cyclin A1 (INCA1) and functions as a growth suppressor with suppressed expression in Acute Myeloid Leukemia (AML). Moreover, ING5 translocation from the nucleus to the cytoplasm might be a critical event for carcinogenesis and tumor progression in human head and neck squamous cell carcinoma. Both ING4 and ING5 contain an N-terminal leucine zipper-like (LZL) motif-containing ING domain, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain. They associate with histone acetyltransferase (HAT) complexes containing MOZ (monocytic leukemia zinc finger protein)/MORF (MOZ-related factor) and HBO1, and further direct the MOZ/MORF and HBO1 complexes to chromatin
LESLPLELQRNFSLMRELDARVQDLLAEIEKLLREYLKTVKSLSKEERRELLKEIQDLFAKAKELSEEKV
QLATQTYETVDKHIRRLDADL
>gnl|CDD|341093 cd16860, ING_ING1, Inhibitor of growth (ING) domain of inhibitor of growth protein 1 (ING1). ING1 is an epigenetic regulator and a type II tumor suppressor that impacts cell growth, aging, apoptosis, and DNA repair, by affecting chromatin conformation and gene expression. It acts as a reader of the active chromatin mark, the trimethylation of histone H3 lysine 4 (H3K4me3). It binds and directs growth arrest and DNA damage inducible protein 45 a (Gadd45a) to target sites, thus linking the histone code with DNA demethylation. It interacts with the proliferating cell nuclear antigen (PCNA) via the PCNA-interacting protein (PIP) domain in a UV-inducible manner. It also interacts with a PCNA-interacting protein, p15 (PAF). Moreover, ING1 associates with members of the 14-3-3 family, which is necessary for the cytoplasmic relocalization. Endogenous ING1 protein specifically interacts with the pro-apoptotic BCL2 family member BAX and colocalizes with BAX in a UV-inducible manner. It stabilizes the p53 tumor suppressor by inhibiting polyubiquitination of multi-monoubiquitinated forms via interaction with and colocalization of the herpesvirus-associated ubiquitin-specific protease (HAUSP)-deubiquitinase with p53. It is also involved in trichostatin A-induced apoptosis and caspase 3 signaling in p53-deficient glioblastoma cells. In addition, tyrosine kinase Src can bind phosphorylate ING1 and further regulates its activity. ING1 contains an N-terminal leucine zipper-like (LZL) motif-containing ING domain, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain
LDSIESLPFDLQRNVSLMREIDAKYQEILKELDEYYEKFKRETDAVQKRRLLHCIQRALIRSQELGDEKI
QIVSQMVELVENRTRQVD
>gnl|CDD|341094 cd16861, ING_ING2, Inhibitor of growth (ING) domain of inhibitor of growth protein 2 (ING2). ING2, also termed inhibitor of growth 1-like protein (ING1Lp), or p32, or p33ING2, is a core component of a multi-factor chromatin-modifying complex containing the transcriptional co-repressor SIN3A and histone deacetylase 1 (HDAC1). It has been implicated in the control of cell cycle, in genome stability, and in muscle differentiation. ING2 independently interacts with H3K4me3 (Histone H3 trimethylated on lysine 4) and PtdIns(5)P, and modulates crosstalk between lysine methylation and lysine acetylation on histone proteins through association with chromatin in the presence of DNA damage. It collaborates with SnoN to mediate transforming growth factor (TGF)-beta-induced Smad-dependent transcription and cellular responses. It is upregulated in colon cancer and increases invasion by enhanced MMP13 expression. It also acts as a cofactor of p300 for p53 acetylation and plays a positive regulatory role during p53-mediated replicative senescence. ING2 contains an N-terminal leucine zipper-like (LZL) motif-containing ING domain, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain
LECVESLPLEIQRNVSLLREIDTKYQEALKEVDEVYEKYKKETDPSQKKRLQQQLQRALINSQELGDEKI
QIVTQMLELVENRARQME
>gnl|CDD|341095 cd16862, ING_ING4, Inhibitor of growth (ING) domain of inhibitor of growth protein 4 (ING4). ING4, also termed p29ING4, is a member of the inhibitor of growth (ING) family of type II tumor suppressors. It acts as an E3 ubiquitin ligase to induce ubiquitination of the p65 subunit of NF-kappaB and inhibit the transactivation of NF-kappaB target genes. It also induces apoptosis through a p53 dependent pathway, including increasing p53 acetylation, inhibiting Mdm2-mediated degradation of p53 and enhancing the expression of p53 responsive genes both at the transcriptional and post-translational levels. Moreover, ING4 can inhibit the translation of proto-oncogene MYC by interacting with AUF1. It also regulates other transcription factors, such as hypoxia-inducible factor (HIF). In addition, ING4 associates with histone acetyltransferase (HAT) complexes containing MOZ (monocytic leukemia zinc finger protein)/MORF (MOZ-related factor) and HBO1, and further directs the MOZ/MORF and HBO1 complexes to chromatin. ING4 contains an N-terminal leucine zipper-like (LZL) motif-containing ING domain, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain
LDSIENLPFELQRNFQLMRDLDQRTEDLKVEIDKLATEYVSNARSLSSEEKLKLLKQIQEAYGKCKEFGD
DKVQLAMQTYEMVDKHIRRLDTDL
>gnl|CDD|341096 cd16863, ING_ING5, Inhibitor of growth (ING) domain of inhibitor of growth protein 5 (ING5). ING5, also termed p28ING5, is a member of the inhibitor of growth (ING) family of type II tumor suppressors. It acts as a Tip60 cofactor that acetylates p53 at K120 and subsequently activates the expression of p53-dependent apoptotic genes in response to DNA damage. Aberrant ING5 expression may contribute to pathogenesis, growth, and invasion of gastric carcinomas and colorectal cancer. ING5 can physically interact with p300 and p53 in vivo, and its overexpression induces apoptosis in colorectal cancer cells. It also associates with Inhibitor of cyclin A1 (INCA1) and functions as a growth suppressor with suppressed expression in Acute Myeloid Leukemia (AML). Moreover, ING5 translocation from the nucleus to the cytoplasm might be a critical event for carcinogenesis and tumor progression in human head and neck squamous cell carcinoma. In addition, ING5 associates with histone acetyltransferase (HAT) complexes containing MOZ (monocytic leukemia zinc finger protein)/MORF (MOZ-related factor) and HBO1, and further directs the MOZ/MORF and HBO1 complexes to chromatin. ING5 contains an N-terminal leucine zipper-like (LZL) motif-containing ING domain, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain
DSIENLPCELQRNFQLMRDLDQRTEDKKAEIDKLASEYIANVKNLSPEQRVEHLKKIQSAYSKCKEYSDD
KVQLAMQTYEMVDKHIRRLDADL
>gnl|CDD|350628 cd16864, ARID_JARID, ARID/BRIGHT DNA binding domain of JARID proteins. The JARID subfamily within the JmjC protein family includes lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and a Drosophila homolog, protein little imaginal discs (Lid). KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. KDM5C is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me3 and H3K4me2), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. The family also includes Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members of this subfamily contain the catalytic JmjC domain, JmjN, the AT-rich domain interacting domain (ARID)/BRIGHT domain, a C5HC2 zinc finger, as well as two or three plant homeodomain (PHD) fingers
TRVKLNFLDQIAKFWELQGSSLKIPNVERKALDLFTLHKIVQEEGGFEEVTKERKWSKVARRLGYPPGKG
VGSLLRGHYERILYPYD
>gnl|CDD|350629 cd16865, ARID_ARID1A-like, ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ARID1B and similar proteins. This subfamily contains ARID1A and its paralog ARID1B. They are mutually exclusive components of human SWItch/Sucrose NonFermentable (SWI/SNF) chromatin remodeling protein complexes, but display different functions in development and cell-cycle control. SWI/SNF complexes containing ARID1A have an antiproliferative function, whereas the one harboring ARID1B shows a pro-proliferative function. ARID1A functions as an important tumor suppressor in various tumor types. It has been implicated in cell-cycle arrest, as well as in the interactions with p53 and BRG1/BRM and with topoisomerase II alpha. ARID1B may be considered as a potential therapeutic target for ARID1A-mutant cancers. Moreover, mutations in the ARID1B gene cause Coffin-Siris syndrome, exhibiting developmental defects, and haplo-insufficiency of ARID1B is a frequent cause of intellectual disability. Mutations in the ARID1B gene also have been found in many cancers. Both ARID1A and ARID1B contain an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), which binds DNA in a non-sequence-specific manner
PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAEVTKNKKWKEICTELNIGASSS
AAFTLRKNYIKYLLAYECRFDRG
>gnl|CDD|350630 cd16866, ARID_ARID2, ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 2 (ARID2) and similar proteins. ARID2, also called BRG1-associated factor 200 (BAF200) or zinc finger protein with activation potential (Zipzap/p200), is a novel serum response factor (SRF)-binding protein with multiple conserved domains, including an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), RFX DNA-binding domain, a glutamine-rich domain, and two C2H2 zinc fingers. It binds DNA without sequence specificity. ARID2 is an intrinsic subunit of PBAF (SWI/SNF-B) remodeling complex, which needs ARID2 to play an essential role in promoting osteoblast differentiation, maintaining cellular identity and activating tissue-specific gene expression. Moreover, ARID2 may function as a tumor suppressor in many cancers. It may also serve as a transcription co-activator for the regulation of cardiac gene expression, and is required for heart morphogenesis and coronary artery development
EYDAFLNELRQFHASRGTPFKKIPVVGGKELDLYLLYSKVTALGGWAKVTDKNKWEEILEDFNFPRGCSN
AAFALKQIYLRYLEAYEK
>gnl|CDD|350631 cd16867, ARID_ARID3, ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID3A, ARID3B, ARID3C, dead ringer (Dri) from Drosophila melanogaster, and similar proteins. The ARID3 subfamily includes AT-rich interactive domain (ARID, also known as BRIGHT)-containing proteins ARID3A, ARID3B and ARID3C, which are the most direct mammalian counterparts of the Drosophila "dead ringer" protein Dri. They consist of an acidic N-terminal region of unknown function, the central ARID matrix association (or attachment) region (MAR)-DNA binding domain, a SUMO-I conjugation (SUMO) motif, and a multifunctional homomerization/nuclear export REKLES domain in the C-terminal third of the molecule. The ARID domain in this subfamily has been described as the "extended" or e-ARID due to additional conserved sequences at both the N and C termini of the core ARID region. The REKLES domain is found only in the ARID3 subfamily. It has co-evolved with and regulates functional properties of the ARID DNA-binding domain
FKQLYELSDDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYELYRLVVEKGGLVEVINKKIWREIT
KGLNLPSSITSAAFTLRTQYMKYLYPYECEKEKLSSPSELQAAIDGNR
>gnl|CDD|350632 cd16868, ARID_ARID4, ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID4A, ARID4B and similar proteins. This subfamily contains ARID4A and its paralog ARID4B, both of which are retinoblastoma (Rb)-binding proteins that function as coactivators to enhance the androgen receptor (AR) and Rb transcriptional activity, and play important roles in the AR and Rb pathways to control male fertility. They also act as the leukemia and tumor suppressors involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndrome. Moreover, they associate with the mSIN3A histone deacetylase (HDAC) chromatin remodeling complex through the interaction with each other, as well as with the breast cancer associated tumor suppressor ING1 and the breast cancer metastasis suppressor BRMS1. Both ARID4A and ARID4B contain a Tudor domain, a PWWP domain (also known as HATH domain or RBB1NT domain), an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a chromobarrel domain, and a C-terminal R2 domain
EKENFLEQLYKFMEDRGTPINKPPVLGYKDLDLFKLYKLVQELGGMERVSQGAKWRSIYQQLGIPVLNSA
ASHNIKQAYKKYLYAFE
>gnl|CDD|350633 cd16869, ARID_ARID5, ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID5A, ARID5B, and similar proteins. This subfamily contains ARID5A and its paralog ARID5B. ARID5A, also called modulator recognition factor 1 (MRF-1), is an estrogen receptor alpha (ER alpha)-interacting protein that is expressed abundantly in cardiovascular tissues and suppresses ER alpha-induced transactivation. It also plays an important role in the promotion of inflammatory processes and autoimmune diseases. ARID5B, also called MRF1-like protein or modulator recognition factor 2 (MRF-2), is a DNA-binding protein that directly interacts with plant homeodomain (PHD) finger 2 (PHF2) to form a protein kinase A (PKA)-dependent PHF2-ARID5B histone H3K9Me2 demethylase complex. It also functions as a transcriptional co-regulator for the transcription factor sex determining region Y (SRY)-box protein 9 (Sox9) and promotes chondrogenesis through histone modification. Moreover, ARID5B is highly expressed in the cardiovascular system and may play essential roles in the phenotypic change of smooth muscle cells (SMCs) through its regulation of SMC differentiation. Both ARID5A and ARID5B contain an AT-rich DNA-interacting domain (ARID, also known as BRIGHT)
EEQAFLKLLYKFMKDRGTPIERIPHLGFKQIDLYTFFKLVQKLGGYEQVTAKRLWKHVYDELGGNPSSTS
AATCTRRHYEKLLLPYE
>gnl|CDD|350634 cd16870, ARID_JARD2, ARID/BRIGHT DNA binding domain of Jumonji/ARID domain-containing protein 2 (JARID2) and similar proteins. JARID2, also called protein Jumonji, is a DNA-binding protein that contains both the Jumonji C (JmjC) domain and AT-rich DNA-interacting domain (ARID, also known as BRIGHT). It is an interacting component of Polycomb repressive complex-2 (PRC2) that catalyzes methylation of lysine 27 of histone H3 (H3K27) and regulates important gene expression patterns during development. It exhibits nucleosome-binding activity that contributes to PRC2 stimulation. However, unlike other JmjC domain-containing proteins, JARID2 is catalytically inactive due to the lack of conserved residues essential for histone demethylase activity. JARID2 is also involved in transforming growth factor-beta (TGF-beta)-induced epithelial-mesenchymal transition (EMT) of lung and colon cancer cell lines through the modulation of histone H3K27 methylation. Moreover, JARID2 is a part of GLP- and G9a-containing protein complex that promotes lysine 9 on histone H3 (H3K9) methylation on the cyclin D1 promoter and silences the expression of cyclin D1 and other cell cycle genes. It functions as a transcriptional repressor that plays critical roles in embryonic development including heart development in mice, and regulates cardiomyocyte proliferation via interaction with retinoblastoma protein (Rb), one of the master regulatory genes of the cell cycle. Furthermore, JARID2 acts as a transcriptional repressor of target genes, including Notch1. It directly binds to SETDB1 (SET domain, bifurcated 1) to form a complex that plays an important role in a novel process involving the modification of H3K9 methylation during heart development. Meanwhile, JARID2 is a key transcriptional repressor that plays a role in invariant natural killer T (iNKT) cell maturation. It regulates promyelocytic leukemia zinc finger (PLZF) expression by linking T-cell receptor (TCR) signaling to H3K9me3. JARID2 polymorphisms are associated with non-syndromic orofacial clefts (NSOC) susceptibility
RWGPNVQKLACIKKHLESQGINLTPPPLIGGCELDLPRLYHLVQELGGMQQVTDKKKWNKVADHLNIPKT
AQDRPSKLQDAYCKYLLSYDTLSDEEKQKLEEEVRAEREKKE
>gnl|CDD|350635 cd16871, ARID_Swi1p-like, ARID/BRIGHT DNA binding domain of yeast SWI/SNF chromatin-remodeling complex subunit Swi1p and similar proteins. Saccharomyces cerevisiae Swi1p, also called SWI/SNF chromatin-remodeling complex subunit SWI1, regulatory protein GAM3, or transcription regulatory protein ADR6, is a transcription regulatory protein that is a subunit of the SWI/SNF complex, which plays critical roles in the regulation of gene transcription and expression. It can exist as a prion [SWI(+)], which demonstrates a link between prionogenesis and global transcriptional regulation. Swi1p contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT) that binds DNA nonspecifically. This subfamily also includes Schizosaccharomyces pombe SWI/SNF chromatin-remodeling complex subunit sol1 (sol1p, also known as switch one-like protein). sol1p is a homolog of S. cerevisiae Swi1p and is also a part of SWI/SNF chromatin-remodeling complex
AQPEQFMKSLREFMAKRGTPIEQQPVIGGRPVNLFRLYQLVQKLGGSRQVTQNNQWPRVAQKLGFPPEQN
PQVAQQLAQIYQRYLLPYEE
>gnl|CDD|350636 cd16872, ARID_HMGB9-like, ARID/BRIGHT DNA binding domain of Arabidopsis thaliana high mobility group B proteins HMGB9, HMGB10, HMGB11, HMGB15 and similar proteins. This subfamily includes a group of conserved plant DNA-binding proteins, including HMGB9 (or ARID-HMG1), HMGB10 (or ARID-HMG2), HMGB11, and HMGB15. They have been termed ARID-HMG proteins, due to containing two DNA-binding domains, an N-terminal AT-rich DNA-interacting domain (ARID, also known as BRIGHT), and a C-terminal high mobility group (HMG)-box domain. They are widely expressed in Arabidopsis and localize primarily to the nucleus. HMGB9/ARID-HMG1 binds specifically to A/T-rich DNA. HMGB15 is a transcription factor predominantly expressed in mature pollen grains and pollen tubes. It may work in the form of a homodimer, or interact with HMGB9, HMGB10 and HMGB11 to form heteromultimers in plant cells. HMGB15 is required for pollen tube growth in Arabidopsis and is involved in transcriptional regulation through the interaction with AGL66 and AGL104
DPDLFWETLRKFHESLGTKFRIPIVGGKELDLHRLYKEVTSRGGLEKVIKDRKWKEVAAVFNFPPTITNA
SFVLRKYYLSLLHHYE
>gnl|CDD|350637 cd16873, ARID_KDM5A, ARID/BRIGHT DNA binding domain of lysine-specific demethylase 5A (KDM5A). KDM5A, also called histone demethylase JARID1A, Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2), was originally identified as a retinoblastoma protein (Rb)-binding partner; its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as the trimethylated histone H3 lysine 4 (H3K4me3) demethylase that belongs to the JARID subfamily within the JmjC proteins. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5A contains the catalytic JmjC domain, a JmjN domain, an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a C5HC2 zinc finger, as well as three plant homeodomain (PHD) fingers
TRVKLDFLDQLAKFWELQGSTLKIPVVERKILDLYALSKIVASEGGFEMVTKEKKWSKVGSRMGYLPGKG
TGSLLKSHYERILYPYELFQSG
>gnl|CDD|350638 cd16874, ARID_KDM5B, ARID/BRIGHT DNA binding domain of lysine-specific demethylase 5B (KDM5B). KDM5B, also called cancer/testis antigen 31 (CT31), histone demethylase JARID1B, Jumonji/ARID domain-containing protein 1B (JARID1B), PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), is a member of the JARID subfamily within the JmjC proteins. It has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well as TIEG1/KLF10 (transforming growth factor-beta inducible earlygene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. KDM5B contains the catalytic JmjC domain, a JmjN domain, an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a C5HC2 zinc finger, as well as three plant homeodomain (PHD) fingers
EAQTRVKLNFLDQIAKFWELQGCTLKIPHVERKILDLFQLNKLVAEEGGFDLVCKERKWTKIATKMGFAP
GKAVGSHIRAHYERILYPYN
>gnl|CDD|350639 cd16875, ARID_KDM5C_5D, ARID/BRIGHT DNA binding domain of lysine-specific demethylase KDM5C and KDM5D. This group includes KDM5C and KDM5D, both of which belong to the JARID subfamily within the JmjC proteins. KDM5C, also called histone demethylase JARID1C, Jumonji/ARID domain-containing protein 1C, protein SmcX, or protein Xe169, is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D, also called histocompatibility Y antigen (H-Y), histone demethylase JARID1D, Jumonji/ARID domain-containing protein 1D, or protein SmcY, is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me3 and H3K4me2), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. Both KDM5C and KDM5D contain the catalytic JmjC domain, a JmjN domain, an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a C5HC2 zinc finger, as well as two plant homeodomain (PHD) fingers
TRVKLNYLDQIAKFWEIQGSSLKIPNVERRILDLYSLSKIVQEEGGYEAICKDRRWARVAQRLGYPPGKN
IGSLLRSHYERIIYPYEMYQSG
>gnl|CDD|350640 cd16876, ARID_ARID1A, ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1A (ARID1A) and similar proteins. ARID1A, also called B120, BRG1-associated factor 250a (BAF250A), Osa homolog 1(OSA1), SWI-like protein, SWI/SNF complex protein p270, or SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1 (SWI1), has been identified as a novel tumor suppressor in various tumor types. It interacts with BRG1 adenosine triphosphatase to form a SWItch/Sucrose NonFermentable (SWI/SNF) chromatin remodeling protein complex, which plays a critical role in transcriptional control and gene expression. ARID1A contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), and Eld/Osa homology domains (EHD) 1 and 2 within the C-terminus. The ARID in ARID1A binds nonspecific DNA in general and plays an important role in targeting SWI/SNF to chromatin. The EHD1 may be capable of mediating an intramolecular association with EHD2, and/or an intermolecular association resulting in homo- or hetero-dimerization. The EHD2 binds Swi2/Brahma homologue Brahma-related gene 1 (BRG1, also known as Snf2b), a human homologue of yeast Swi2
PERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVKEIGGLTQVNKNKKWRELATNLNVGTSSS
AASSLKKQYIQCLYAFECKIERG
>gnl|CDD|350641 cd16877, ARID_ARID1B, ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1B (ARID1B) and similar proteins. ARID1B, also called BRG1-associated factor 250b (BAF250B), BRG1-binding protein ELD/OSA1, Osa homolog 2 (Osa2), or p250R, is the largest subunit of ATP-dependent SWItch/sucrose nonfermentable (SWI/SNF) chromatin remodeling complex, which plays a critical role in transcriptional control and gene expression. ARID1B exhibits tumour-suppressor activities in pancreatic cancer cell lines. Mutations in the ARID1B gene cause Coffin-Siris syndrome, exhibiting developmental defects, and haplo-insufficiency of ARID1B is a frequent cause of intellectual disability. Moreover, mutations in the ARID1B gene have been found in many cancers. ARID1B contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), which binds DNA in a non-sequence-specific manner similar to ARID1A
PERKLWVDRYLTFMEERGTPVASLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSS
AASSLKKQYIQYLFAFECKIERG
>gnl|CDD|350642 cd16878, ARID_ARID3A, ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3A (ARID3A) and similar proteins. ARID3A, also called B-cell regulator of IgH transcription (Bright), dead ringer-like protein 1 (Dril1), or E2F-binding protein 1 (E2FBP1), is an ubiquitously expressed DNA-binding protein that has been implicated in embryonic patterning, cell lineage gene regulation, and cell cycle control, chromatin remodeling and transcriptional regulation. It was originally identified as a B cell-specific trans-activator of immunoglobulin heavy-chain (IgH) transcription, which increases immunoglobulin transcription in antigen-activated B cells and plays regulatory roles in hematopoiesis. It also functions as an E2F transcription regulator, inducing promyelocytic leukemia protein (PML) reduction and suppressing the formation of PML-nuclear bodies. It antagonizes the p16(INK4A)-Rb tumor suppressor machinery by regulating PML stability. ARID3A transcriptional activity can be modulated by SUMO (Small Ubiquitin-related Modifier) modification through the interaction with the SUMO-conjugating enzyme Ubc9. ARID3A also plays an important role in marginal zone B lymphocyte development and autoantibody production. Furthermore, ARID3A is a direct p53 target gene. It controls cell growth in a p53-dependent manner. ARID3A contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a SUMO-I conjugation (SUMO) motif and a multifunctional homomerization/nuclear export REKLES domain, which consists of two subdomains: a modestly conserved N-terminal REKLES alpha and a highly conserved (among ARID3 orthologous proteins) C-terminal REKLES beta
DHGDWTYEEQFKQLYELDGDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYMLYVLVTEKGGLVEV
INKKLWREITKGLNLPTSITSAAFTLRTQYMKYLYPYECEKRGLSNPNELQAAIDSNRREGRR
>gnl|CDD|350643 cd16879, ARID_ARID3B, ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3B (ARID3B) and similar proteins. ARID3B, also called Bright and dead ringer protein, or Bright-Dri-like protein (Bdp), is a DNA binding protein involved in cellular immortalization, epithelial-mesenchymal transition (EMT), and tumorigenesis. Its expression is differentially regulated in normal and malignant tissues. It is required for heart development by regulating the motility and differentiation of heart progenitors. ARID3B is overexpressed in neuroblastoma and ovarian cancer. It acts as a novel target with roles in cell motility in breast cancer cells, promotes migration of mouse embryo fibroblasts (MEFs) and breast cancer cells, and induces tumor necrosis factor alpha (TNFalpha)-mediated apoptosis. ARID3B contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a SUMO-I conjugation (SUMO) motif and a multifunctional homomerization/nuclear export REKLES domain, which consists of two subdomains: a modestly conserved N-terminal REKLES alpha and a highly conserved (among ARID3 orthologous proteins) C-terminal REKLES beta
RDFAKLYELDNDPKRKEFLDDLFAFMQKRGTPINRIPIMAKQVLDLYMLYKLVTEKGGLVEVINKKIWRE
ITKGLNLPTSITSAAFTLRTQYMKYLYPYECEKKSLSSPAELQAAIDGNRREGRRP
>gnl|CDD|350644 cd16880, ARID_ARID3C, ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3C (ARID3C) and similar proteins. ARID3C, also called Brightlike, is a new ARID3 family transcription factor that co-activates ARID3A-mediated immunoglobulin gene transcription. It also functions as a potential regulator of early events in B cell antigen receptor (BCR) signaling. ARID3C contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a SUMO-I conjugation (SUMO) motif and a multifunctional homomerization/nuclear export REKLES domain, which consists of two subdomains: a modestly conserved N-terminal REKLES alpha and a highly conserved (among ARID3 orthologous proteins) C-terminal REKLES beta
EEQFKQLYELDDDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYTLYRLVTDKGGLVEVINKKIWR
EITKGLSLPTSITSAAFTLRTQYMKYLYPYECEKRALSSPGELQAAIDSNRREGRRQ
>gnl|CDD|350645 cd16881, ARID_Dri-like, ARID/BRIGHT DNA binding domain of dead ringer (Dri) from Drosophila melanogaster and similar proteins. Dri, also termed retained (retn), is a nuclear protein with a sequence-specific DNA-binding domain termed AT-rich DNA-interacting domain (ARID, also known as BRIGHT). It is a founding member of the ARID family. Sequence comparison shows that DRI belongs to the "extended" or e-ARID subfamily, which exhibits an extended region of similarity either side of the ARID. Dri plays an important role in embryogenesis. It functions as an essential transcription factor involved in aspects of dorsal/ventral and anterior/posterior axis patterning, as well as myogenesis and hindgut development
FWEFFEQFKQLYEISDDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYELYNLVVARGGLVEVINK
KLWREITKGLHLPSSITSAAFTLRTQYMKYLYPYECEKLKLSTPAELQAAIDGNR
>gnl|CDD|350646 cd16882, ARID_ARID4A, ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 4A (ARID4A) and similar proteins. ARID4A, also called retinoblastoma-binding protein 1 (RBBP1, or RBP1), is a leukemia and tumor suppressor involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndrome. It associates with the mSIN3A histone deacetylase (HDAC) chromatin remodeling complex through the interaction with the breast cancer associated tumor suppressor ING1, the breast cancer metastasis suppressor BRMS1, and the ARID4 family homolog ARID4B (also known as RBP1L1). ARID4A specifically interacts with retinoblastoma protein (pRb) and shows both HDAC-dependent and -independent repression activities. It is also involved in the pocket domain of pRb-mediated repression of E2F-dependent transcription and cellular proliferation. Moreover, it acts as a Runx2 coactivator and is involved in the regulation of osteoblastic differentiation in Runx2-osterix transcriptional cascade. ARID4A contains a Tudor domain, a PWWP domain (also known as HATH domain or RBB1NT domain), an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a chromobarrel domain, and a C-terminal R2 domain. The ARID and R2 domains are responsible for the repression activities. The Tudor, PWWP, and chromobarrel domains are all Royal Family domains, but only chromobarrel domain of ARID4A is responsible for recognizing both dsDNA and methylated histone tails, particularly H4K20me3, in chromatin remodeling and epigenetic regulation
ERDNFLQQLYKFMEDRGTPINKPPVLGYKDLNLFKLFRLVYQQGGCDNIESGSVWKQIYMDLGIPILNSA
ASYNVKTAYRKYLYGFE
>gnl|CDD|350647 cd16883, ARID_ARID4B, ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 4B (ARID4B) and similar proteins. ARID4B, also called 180 kDa Sin3-associated polypeptide (p180), breast cancer-associated antigen BRCAA1, histone deacetylase complex subunit SAP180, or retinoblastoma-binding protein 1-like 1 (RBP1L1, or RBBP1L1), is a tumor suppressor involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndrome. It associates with the mSIN3A histone deacetylase (HDAC) chromatin remodeling complex through the interaction with the breast cancer associated tumor suppressor ING1, the breast cancer metastasis suppressor BRMS1, and the ARID4 family homolog ARID4A (also known as RBP1). ARID4B plays a causative role in metastatic progression of breast cancer. It may also be associated with regulating cell cycle. ARID4B contains a Tudor domain, a PWWP domain (also known as HATH domain or RBB1NT domain), an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a chromobarrel domain, and a C-terminal R2 domain
ERENFLQQLYKFMEDRGTPINKRPVLGYRNLNLFKLFRLVHKLGGFDNIESGAVWKQVYQDLGIPVLNSA
AGYNVKCAYRKYLYGFEEYCTS
>gnl|CDD|350648 cd16884, ARID_ARID5A, ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 5A (ARID5A) and similar proteins. ARID5A, also called modulator recognition factor 1 (MRF-1), is an estrogen receptor alpha (ER alpha)-interacting protein that is expressed abundantly in cardiovascular tissues and suppresses ER alpha-induced transactivation. It also associates with thyroid receptor alpha (TR alpha) and retinoid X receptor alpha (RXR alpha) in a ligand-dependent manner, and with ER beta, androgen receptor (AR), and the retinoic acid receptor (RAR) in a ligand-independent manner. ARID5A functions as a negative regulator of RORgamma-induced Th17 cell differentiation and may be involved in the pathogenesis of rheumatoid arthritis (RA). Moreover, it is an important transcriptional partner of the transcription factor sex determining region Y (SRY)-box protein 9 (Sox9) in stimulation of chondrocyte-specific transcription. Meanwhile, ARID5A plays an important role in promotion of inflammatory processes and autoimmune diseases. It works as a unique RNA binding protein, which stabilizes interleukin-6 (IL-6) but not tumor necrosis factor-alpha (TNF-alpha) mRNA through binding to the 3' untranslated region (UTR) of IL-6 mRNA, and inhibits the destabilizing effect of regnase-1 on IL-6 mRNA. ARID5A contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT)
EEQAFLVNLYKFMKERNTPIERIPHLGFKQINLWKIYKAVEKLGGYELVTARRLWKNVYDELGGSPGSTS
AATCTRRHYERLVLPYV
>gnl|CDD|350649 cd16885, ARID_ARID5B, ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 5B (ARID5B) and similar proteins. ARID5B, also called MRF1-like protein or modulator recognition factor 2 (MRF-2), is a DNA-binding protein that directly interacts with plant homeodomain (PHD) finger 2 (PHF2) to form a protein kinase A (PKA)-dependent PHF2-ARID5B histone H3K9Me2 demethylase complex, which is a signal-sensing modulator of histone methylation and gene transcription. It also functions as a transcriptional co-regulator for the transcription factor sex determining region Y (SRY)-box protein 9 (Sox9) and promotes chondrogenesis through histone modification. Moreover, ARID5B is highly expressed in the cardiovascular system and may play essential roles in the phenotypic change of smooth muscle cells (SMCs) through its regulation of SMC differentiation. Its polymorphism has been associated with risk for pediatric acute lymphoblastic leukemia (ALL). ARID5B contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), which can bind both the major and minor grooves of its target sequences
DEQAFLVALYKYMKERKTPIERIPYLGFKQINLWTMFQAAQKLGGYETITARRQWKHIYDELGGNPGSTS
AATCTRRHYERLILPYERFIKGEED
>gnl|CDD|341123 cd16887, YEATS, YEATS domain family, chromatin reader proteins. The YEATS family is named for several family members: 'YNK7', 'ENL', 'AF-9', and 'TFIIF small subunit', and also contains the GAS41 protein, YEATS2, Drosophila D12, and others. DNA regulation by chromatin through histone post-translational modification and other mechanisms involves complexes with write, eraser and reader functions. YEATS domains act as readers of the chromatin state and stimulates transcriptional activity through preferential interactions with crotonylated lysines on histones
KPIVIGNVAEKIPKPEPDDNTHKWTVYVRSPTNEDLSSFIKKVTFKLHPSFPNPVRVVTDPPFEVEEVGW
GEFPIEIKIYFKDSNEKPVTLSHFLKLHPDGSPLKKPVVVSEKYDEIVFR
>gnl|CDD|381609 cd16888, lyz_G-like_1, lysozyme G-like protein 1. Eukaryotic goose-type or G-type lysozymes (goose egg-white lysozyme; GEWL) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). Mammals have two lysozyme G-like proteins, and this family corresponds to human and mouse lysozyme G-like protein 1. In humans and some other species, the canonical catalytic glutamate residue is absent, suggesting a loss of muramidase activity
CRIGRRHGLNYCGVRASERLAEIDMPYLLRYQPMMRTVGQKYCMDPAVIAGVLSRESPGGNYLVDLGNVG
DGLGMVQDTGFYAPTSWISESQVSQKTEVLTSRIKEIQRRFPTWTPDQCLRGGLCAYSGGPGYVRSNQDL
SCDFCNDVLARAKYFKRHGF
>gnl|CDD|381610 cd16889, chitinase-like, chitinase-like domain. This family includes proteins such as chitinases, chitosanase, pesticin, and endolysin, which are involved in the degradation of 1,4-N-acetyl D-glucosamine linkages in chitin polymers and related activities. Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Chitosanase enzymes hydrolyze chitosan, a biopolymer of beta (1,4)-linked-D-glucosamine (GlcN) residues produced by partial or full deacetylation of chitin. Pesticin (Pst) is a anti-bacterial toxin produced by Yersinia pestis that acts through uptake by the target related bacteria and the hydrolysis of peptidoglycan in the periplasm. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division
WFLLITSLETKGLGPTAVYGDGKDPRGYTRGIGVTHGMLRGSTSRFPGVDTSNQTNNGASTDSQLAKLAM
EGFDPAYRALMRTIAHRDDLSPHVNGCAVIFAGFN
>gnl|CDD|381611 cd16890, lyz_i, I-type lysozyme. Invertebrate type (I-type) lysozyme, initially identified in starfish and marine bivalves, are found in various invertebrate phyla and are apparently ubiquitous in insects. Lysozymes cleave the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, the major bacterial cell wall polymer. I-type enzymes share structural similarity and the conserved glutamate catalytic residue of the lysozyme family
DCLGCLCEAASGCNPTAGCSMGGVCGPFRISKPYWQDAGKPVLPGDDPNRGGAFERCANDPYCAARTVRN
YMARYGQDCNGDGVIDCEDYARIHYLGPNGCKNQETLGYWNRRFKGC
>gnl|CDD|381612 cd16891, CwlT-like, CwlT-like N-terminal lysozyme domain and similar domains. CwlT is a bifunctional cell wall hydrolase containing an N-terminal lysozyme domain and a C-terminal NlpC/P60 endopeptidase domain (gamma-d-D-glutamyl-L-diamino acid endopeptidase), and has been implicated in the spread of transposons. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL)
YRPLVEKEAKKYGIPEYVPLILAIIMQESGGKGPDIMQSSESAGLPPNTITDPEESIEQGVKYFADVLKK
AKGKGVDIWTAVQAYNFGGGYIDYVAKNGGKYTLELAKAYSREVVAPSLGNYTGSALYNGGYLYYNYGDF
FYVELVMRYLA
>gnl|CDD|381613 cd16892, LT_VirB1-like, VirB1-like subfamily. This subfamily includes VirB1 protein, one of twelve proteins making up type IV secretion systems (T4SS). T4SS are macromolecular assemblies generally composed of VirB1-11 and VirD4 proteins, and are used by bacteria to transport material across their membranes. VirB1 acts as a lytic transglycosylase (LT), and is important with respect to piercing the peptidoglycan layer in the periplasm. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL)
LAAQCAPGVHPETLAAIVQVESGGNPYAIGVNGGKLSRQPKTKAEAIATARQLIAAGHNFDVGLGQINSR
NLARLGLTVEDVFDPCTNLKAGATILTECYARAKKTGGDGQAALRAALSCYNTGNFTRGFSNGYVQKVVA
AAG
>gnl|CDD|381614 cd16893, LT_MltC_MltE, membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins. MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda
PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRLLGGKGGLPSKSYLFD
PENNIDIGTAYLHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSDRKKAISKINRLSPDEVYQH
LTKKLPAAETRNYLKKVLKAKK
>gnl|CDD|381615 cd16894, MltD-like, Membrane-bound lytic murein transglycosylase D and similar proteins. Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL)
LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLK
DLYKRFGDWLLALAAYNAGEGRVRRAIKRAGTDKWEDYYRLYLPAETRRYVPKFLAAKI
>gnl|CDD|381616 cd16895, TraH-like, conjugal transfer protein H and similar proteins. This subfamily consists of several TraH proteins, putative conjugal transfer proteins of uncharacterized function, apparently found only in alphaproteobacteria. They have similarity to lysozyme and preserve the critical glutamate residue which has catalytic activity in lysozyme-like proteins
IDAALIQQCADPSLKPAIVEQFVAAVGSPDPLAVTVKAGDRTILVPKPKTPDEAMALIRRYVGQAVVRVG
LTQYPAGLGVKDASDLKPDLFDPCENLRMGTALFAKVYRIVTKWYGNPAPQAFDDAIYAWKTGYFEGESV
FQAQDPGGVIVAPPNVGASGTPESAGDATPPRQPSEPPLEPQDPNKAGMRIDLSGIGG
>gnl|CDD|381617 cd16896, LT_Slt70-like, uncharacterized lytic transglycosylase subfamily with similarity to Slt70. Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue
PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWIAEKLGLEDFSEDDL
YDPETNIRLGTWYLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWSGDGKTLDQIPFPETRHYVKKV
LKNYKI
>gnl|CDD|340383 cd16897, LYZ_C, C-type lysozyme. C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase). In humans, lysozyme is found in a wide variety of tissue types and body fluids. It has bacteriolytic properties through the hydolysis of beta-1,4, glyocosidic linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan, as well as between N-acetyl-D-glucosamine residues in chitodextrins. This family also includes digestive stomach lysozyme, which allow ruminants to digest bacteria in the foregut. The mammalian enzyme is related to lysozyme found hen egg-whites and related species
KIFSRCELARILKRGGLDGYRGYSLANWVCLAYYESGFNTRATNENPDGSTDYGIFQINSRYWCNDGKTP
SKNLCHISCSDLLNDDITDDIKCAKKIVKDPQGMGAWVAWRLHCEGRDLSRWLDGC
>gnl|CDD|340384 cd16898, LYZ_LA, alpha lactalbumin. alpha-lactalbumin (lactose synthase B protein, LA) is a calcium-binding metalloprotein that is expressed exclusively in the mammary gland during lactation. LA is the regulatory subunit of the enzyme lactose synthase. The association of LA with the catalytic component of lactose synthase, galactosyltransferase, alters the acceptor substrate specificity of this glycosyltransferase, facilitating biosynthesis of lactose
IIFTKCELSQILKEHGLDGFNGISLPEWICVTFHTSGYDTQALVYNNGSTEYGLFQISNKGWCDDSQEPV
SRNICGISCSKLLDDDITDDIACAKKILAIPKGIDYWKAHKPFCREDLDQWRC
>gnl|CDD|381618 cd16899, LYZ_C_invert, C-type invertebrate lysozyme. C-type lysozyme proteins of invertebrates, including digestive lysozymes 1 and 2 from Musca domestica, which aid in the use of bacteria as a food source. These lysozymes have high expression in the gut and optimal lytic activity at a lower pH. Other lysozymes in this subfamily have immunological roles. e.g. Anopheles gambiae has eight lysozymes, most of which seem to have immunological roles, those some may function as digestive enzymes in larvae. C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase) has bacteriolytic properties through the hydolysis of beta-1,4, glyocosidic linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan, as well as between N-acetyl-D-glucosamine residues in chitodextrins
KIFTRCELARELRKLGVPRSQLANWVCLAEHESSFNTTAVGGPNSDGSGDYGLFQINDKYWCSPGGGSGN
GCNVKCEDLLDDDISDDVKCAKKIYKEQGFNAWVGWKNKCKGKNLPSYSDC
>gnl|CDD|381619 cd16900, endolysin_R21-like, endolysin R21-like proteins. Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan
AGALALAAAALVGPWEGLRLTAYRDPVGVWTVCYGHTGGDVKPGMRYTPAECDALLAKDLQEAAAAVDRC
VKVPLPDPQRAALASFAYNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERAL
CL
>gnl|CDD|381620 cd16901, lyz_P1, P1 lysozyme Lyz-like proteins. Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan
RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTHGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNG
VPLPQGEFDAYVSFAFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL
>gnl|CDD|381621 cd16902, pesticin_lyz, lysozyme-like C-terminal domain of pesticin. Pesticin (Pst) is an anti-bacterial toxin produced by Yersinia pestis that acts through uptake by the target related bacteria and the hydrolysis of peptidoglycan in the periplasm. Pst contains an N-terminal translocation domain, an intermediate receptor binding domain, and a phage-lysozyme like C-terminal activity domain. Bacteriocins such as pesticin are produced by gram-negative bacteria to attack related bacterial stains. Pst is transported to the periplasm via FyuA, an outer-membrane receptor of Y. pestis and E. coli, where it hydrolyzes peptidoglycan via the cleavage of N-acetylmuramic acid and C4 of N-acetylglucosamine. Disruption of the peptidoglycan layer renders the bacteria vulnerable to lysis via osmotic pressure. The pesticin C-terminal domain resembles the lysozyme-like family, which includes soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, and chitosanases. All the members are involved in the hydrolysis of beta-1,4- linked polysaccharides
IVDKDFISKLEGGRRKGYVPDPNGGGNSGVTIGTGVDLGQRDEADLRELGVPESLIDKLRPYLGLKGQEA
VDKLAKNPLTLSEEEADLLDDAVKDKFTERIARLYNRASAGLKRFEDLPPEQQTVIASVAYQYGSNSSRR
TPKFWGQVTEQDWQGAINELRNFGDKYPTRRNKEADLL
>gnl|CDD|340389 cd16903, pesticin_lyz-like, pesticin C-terminal-like domain of uncharacterized proteins. This subfamily is composed of uncharacterized proteins containing a lysozyme-like domain similar to the C-terminal domain of pesticin. Some members also contain an EF hand domain. Pesticin (Pst) is an anti-bacterial toxin produced by Yersinia pestis that acts through uptake by the target related bacteria and the hydrolysis of peptidoglycan in the periplasm. Pst contains an N-terminal translocation domain, an intermediate receptor binding domain, and a phage-lysozyme like C-terminal activity domain. Bacteriocins such as pesticin are produced by gram-negative bacteria to attack related bacterial stains. Pst is transported to the periplasm via FyuA, an outer-membrane receptor of Y. pestis and E. coli, where it hydrolyzes peptidoglycan via the cleavage of N-acetylmuramic acid and C4 of N-acetylglucosamine. Disruption of the peptidoglycan layer renders the bacteria vulnerable to lysis via osmotic pressure. The pesticin C-terminal domain resembles the lysozyme-like family, which includes soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, and chitosanases. All the members are involved in the hydrolysis of beta-1,4- linked polysaccharides
LTVPKGQLTFDAEGNDIEGSPYFSRKIHWPGNSGSGVTIGRGYDLGQRSKGEIYNDLTSAGVPEEQAKLI
SKGAGLKGCAAKDFVKDNRDSIGEITRKQQIKLFNIIYPEYEARAKRIYNKWTTVEAYGSVDWDSLDPKI
KDVLVDLVYR
>gnl|CDD|340390 cd16904, pesticin_lyz-like, pesticin C-terminal-like domain of uncharacterized proteins. This subfamily is composed of uncharacterized proteins containing a lysozyme-like domain similar to the C-terminal domain of pesticin. Pesticin (Pst) is an anti-bacterial toxin produced by Yersinia pestis that acts through uptake by the target related bacteria and the hydrolysis of peptidoglycan in the periplasm. Pst contains an N-terminal translocation domain, an intermediate receptor binding domain, and a phage-lysozyme like C-terminal activity domain. Bacteriocins such as pesticin are produced by gram-negative bacteria to attack related bacterial stains. Pst is transported to the periplasm via FyuA, an outer-membrane receptor of Y. pestis and E. coli, where it hydrolyzes peptidoglycan via the cleavage of N-acetylmuramic acid and C4 of N-acetylglucosamine. Disruption of the peptidoglycan layer renders the bacteria vulnerable to lysis via osmotic pressure. The pesticin C-terminal domain resembles the lysozyme-like family, which includes soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, and chitosanases. All the members are involved in the hydrolysis of beta-1,4- linked polysaccharides
ISTTAIDLIVSFEVGGRAYYEKKYQHPIWPGGASGVTIGIGYDLGYQTKAQFRSDWQGLLPEADLERLAT
ACGKKGDAAAAALASLSDITIPWDAALTQFAARTLPKYAAQTEDALPNVDLLPPDCQGALVSLVYNRG
>gnl|CDD|341124 cd16905, YEATS_Taf14_like, YEATS domain found in Taf14 and similar proteins. Taf14 has been identified as a component of TFIIF and TFIID transcription factor complexes, various chromatin-remodeling complexes (such as SWI/SNF, INO80, and RSC) and the NuA3 histone acetyltransferase complex. DNA regulation by chromatin thru histone post-translational modification and other mechanism involves complexes with write, eraser and reader functions. YEATS domains act as readers of the chromatin state, and stimulate transcriptional activity, thru preferential interactions with crotonylated lysines on histones. Specifically, Taf14 has been show to be a reader of lysine crotonylation, associated with active gene promoters and enhancers and binding acetyllysine on in histone H3. The YEATS family is named for several family members: 'YNK7', 'ENL', 'AF-9', and 'TFIIF small subunit', and also contains the GAS41 protein
VKRTIRIKTQQHILPDVPPVEGFPLRKWSIELVLLDPNGEEVPADIFDKVTYHLHPTFENPIRTFKKPPF
RLEEKGWGEFDMKIVLHFLDNGGEFTITHDLNFQQEKYEVDHSITFPN
>gnl|CDD|341125 cd16906, YEATS_AF-9_like, YEATS domain found in ENL and AF-9-like proteins. Yeast AFF9 is a YEATS domain protein that binds to modified histones, with a preference for crotonyllysine over acetyllysine. Histone crotonylation upregulates gene expression in an AF9-dependent manner. Sub-family also includes eleven-nineteen-leukemia protein ENL, which binds histones H3 and H1. DNA regulation by chromatin through histone post-translational modification and other mechanisms involves complexes with write, eraser and reader functions. YEATS domains act as readers of the chromatin state and stimulates transcriptional activity through preferential interactions with crotonylated lysines on histones. The YEATS family is named for several family members: 'YNK7', 'ENL', 'AF-9', and 'TFIIF small subunit', and also contains the GAS41 protein
VKLEIGHSATLRKKPTPEGHTHDWTVFVRGANGSDISHFVEKVVFHLHESFPKPKRVVKEPPFEVTESGY
AGFTLPIEIYFKNKEEPKKVRFEYDLFLHLGPPVNHLRTEKLTFKNPSEEFRRKLLK
>gnl|CDD|341126 cd16907, YEATS_YEATS2_like, YEATS domain found in YEATS2 and Drosophila D12. YEATS2 is a YEATS domain reader protein with a preference for recognition of histone H3 crotonylation on lysine 27 (H3K27crHistone crotonylation upregulates gene expression in an AF9-dependent manner. DNA regulation by chromatin thru histone post-translational modification and other mechanism involves complexes with write, eraser and reader functions. YEATS domains act as readers of the chromatin state, and stimulate transcriptional activity, thru preferential interactions with crotonylated lysines on histones. The YEATS family is named for several family members: 'YNK7', 'ENL', 'AF-9', and 'TFIIF small subunit', and also contains the GAS41 protein
KRIIVGNVSKYIPPDEREDDKSTHKWMVYVRGPPEDPDIDHFVKKVRFFLHPSYAPNDVVEVTKPPFHLT
RRGWGEFPVRVQLHFKDPRNKPVDIIHNLKLDRTYTGLQTLGAETVVDVELDR
>gnl|CDD|341127 cd16908, YEATS_Yaf9_like, YEATS domain found in Yaf9 and similar proteins. Yaf9 is a YEATS domain family protein essential in the function the NuA4 histone acetyltransferase complex and the SWR1-C ATP-dependent chromatin remodeling complex. Yaf9 shares structural similarity with histone chaperone Asf1, both exhibit histone H3 and H4 binding in vitro, and evidence supports both play a role in the same histone acetylation mechanism. DNA regulation by chromatin thru histone post-translational modification and other mechanism involves complexes with write, eraser and reader functions. YEATS domains act as readers of the chromatin state, and stimulate transcriptional activity, thru preferential interactions with crotonylated lysines on histones. The YEATS family is named for several family members: `YNK7', `ENL', `AF-9', and `TFIIF small subunit', and also contains the GAS41 protein
QVSRPIVYGNTARPLTPEEKPKAPPDHTHKWTVFVRGPDGEDLSYFIKKVVFKLHESYPNPNRTIEKPPF
EVTETGWGEFEIQIKIYFVPEANEKPITLYHMLKLHPYEDTAENDDLASGGPVVSVQYDEIVFNEPTEEF
YDILM
>gnl|CDD|341128 cd16909, YEATS_GAS41_like, YEATS domain found in YEATS domain-containing protein 4 and similar proteins. glioma amplified sequence 41 (GAS41, also known as, YEATS domain-containing protein 4, NuMA-binding protein 1) is a YEATS domain family protein that is amplified and acts as an oncogene in human glioma. GAS41 is a YEATS domain family protein and has been shown to interact with the general transcription factor TFIIF via the YEATS domain. DNA regulation by chromatin thru histone post-translational modification and other mechanism involves complexes with write, eraser and reader functions. YEATS domains act as readers of the chromatin state, and stimulate transcriptional activity, thru preferential interactions with crotonylated lysines on histones. The YEATS family is named for several family members: 'YNK7', 'ENL', 'AF-9', and 'TFIIF small subunit', and also contains the GAS41 protein
VTIVKPIVYGNIARYFGKKREEDGHTHQWTVYVKPYFNEDMSTYVKKVQFKLHESYANPLRVVTKPPYEV
TETGWGEFEIIIKIFFIDPNERPVTLYHLLKLFQSDTNLMLGKKTLVSEFYDELIFQDPTAMMYQLL
>gnl|CDD|341129 cd16910, YEATS_TFIID14_like, YEATS domain found in transcription initiation factor TFIID subunit 14 and similar proteins. YEATS domain containing proteins, which include Transcription initiation factor TFIID subunits 14 and 14b of Arabidopsis, shown to be part of the TFIID general transcriptional regulator complex in a two-hybrid screen. DNA regulation by chromatin thru histone post-translational modification and other mechanism involves complexes with write, eraser and reader functions. YEATS domains act as readers of the chromatin state, and stimulate transcriptional activity, thru preferential interactions with crotonylated lysines on histones. The YEATS family is named for several family members: 'YNK7', 'ENL', 'AF-9', and 'TFIIF small subunit', and also contains the GAS41 protein
VSVPIVYGSIAFWLGKKADETHTHKWTVYVRGANNEDLSYFIKKVVFVLHPSFANPTRVVTEPPFEVTET
GWGEFEIGITIHFKDDAEKPVELTHPLKLYPPPGSGPPSTKKPVVSEFYDEIVFVEPTEEF
>gnl|CDD|350650 cd16911, AfaD_SafA-like, AfaD-like family of invasins. This family consists of Escherichia coli AfaD, Salmonella SafA and SafD, Yersinia pestis PsaA, Yersinia enterocolitica MyfA, and similar proteins. The afa gene clusters encode an afimbrial adhesive sheath produced by Escherichia coli. The adhesive sheath is composed of two proteins, AfaD and AfaE, which are independently exposed at the bacterial cell surface. AfaE is required for bacterial adhesion to HeLa cells and AfaD for the uptake of adherent bacteria into these cells. Saf-pilin pilus formation proteins SafA and SafD are the major and minor subunits, respectively, of Saf pili, which are often found in clinical isolates of Salmonella and are assembled by the chaperone-usher secretion pathway. PsaA and MyfA are the major subunits of pH 6 antigen (Psa) and Myf fimbrial homopolymers. Also included is the enteroaggregative Escherichia coli AAF/IV pilus tip protein, which is implicated in adhesion as well. During fimbria/pili assembly, polymerization occurs when the N-terminal extension (NTE) of one AfaD-like family monomer is inserted into an adjacent monomer, providing the final beta strand or G-strand, to complete the Ig-like fold, in a mechanism called the donor-strand complementation (DSC) or donor-strand exchange (DSE)
FSATLTPVTGLGAGTQPDGTKIATLSVTNTGSHGGWRVYTNPNSVDGVGGAKGYTVRSKDGSKKVGVRIG
GDGYSGVKGGGGNWVGTGPTTKYITFDIVTDGGQQVKAGTYLFTVSVAEY
>gnl|CDD|341130 cd16913, YkuD_like, L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD. Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue
YIVVDLSEQRLYLYENGKLVKTYPVSTGKPGTPTPTGTFRITRKVKNPTWTGPPSIPPGPYNPLGPYALR
LSGPGSGIGIHGTPWPSSIGRPASHGCIRLSNEDAKELYDWVPVGTPVVIY
>gnl|CDD|410987 cd16914, EcfT, T component of ECF-type transporters. The transmembrane component (T component) of the energy coupling-factor (ECF)-type transporter is a transmembrane protein important for vitamin uptake in prokaryotes. In addition to the T component, energy-coupling factor (ECF) transporters contain an energy-coupling module that consists of two ATP-binding proteins (known as the A and A' components) and a substrate-binding (S) component. ECF transporters comprise a subgroup of ATP-binding cassette (ABC) transporters that do not make use of water-soluble substrate binding proteins or domains, but instead employ integral membrane proteins for substrate binding, the S component, in contrast to classical ABC importers. The T component links the S component to the ATP-binding subcomplex that is composed of the A and A' components
LDPRTKLLLLLLLLILVLLLPSLLLLLLLLLLLLLLLLLAGLPLRLLRLLKRLLFLLLFLLLILLLLPLG
GGGGVFGLGGLGITLEGLLYALLLALRLLAIVLAALLLLLTTPPSELLAALRRLGVPPKLALLLSLALRF
IPLLLEEARRIRDAQRARGGDFSGGGLRRLRSLGPLLGPLLVRSLRRAEELALAMEARGFGGGKRRTSYR
ELKFRRRDYLFLALLLLLLALLL
>gnl|CDD|340392 cd16915, HATPase_DpiB-CitA-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL. This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain
LITIVGNLIDNALDALAATGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQGERG
IGLALVRQSVERLGGSITVESEPGGGTTFSIRIP
>gnl|CDD|340393 cd16916, HATPase_CheA-like, Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases. This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain
VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEG
TITLRAEHQGNQVVIEVSDDGRGIDREKIREKAIERGLITADEAATLSDDEVLNLIFAPGFSTAEQVTDV
SGRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRLP
>gnl|CDD|340394 cd16917, HATPase_UhpB-NarQ-NarX-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ. This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains
LYRIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPAPPGGGGFGLLGMRERAELLGGTL
TIGSRPGGGTRVTARLP
>gnl|CDD|340395 cd16918, HATPase_Glnl-NtrB-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII). This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s)
LIQVFLNLVRNAAQALAGSGGEIILRTRTQRQVTLGHPRHRLALRVSVIDNGPGIPPDLQDTIFYPMVSG
RENGTGLGLAIAQNIVSQHGGVIECDSQPGHTVFSVSLP
>gnl|CDD|340396 cd16919, HATPase_CckA-like, Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s)
LELAILNLAVNARDAMPEGGRLTIETSNQRVDADYALNYRDLIPGNYVCLEVSDTGSGMPAEVLRRAFEP
FFTTKEVGKGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP
>gnl|CDD|340397 cd16920, HATPase_TmoS-FixL-DctS-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS. This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain
IQQVLINLVRNGIEAMSEGGCERRELTIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTKSEGLG
MGLSICRSIIEAHGGRLSVESPAGGGATFQFTLP
>gnl|CDD|340398 cd16921, HATPase_FilI-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases. This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain
LGQVLTNLLGNAIKFRRPRRPPRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHSREEYEGT
GVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP
>gnl|CDD|340399 cd16922, HATPase_EvgS-ArcB-TorS-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC. This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain
LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRK
YGGTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL
>gnl|CDD|340400 cd16923, HATPase_VanS-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain
LQRVFSNLLSNAIKYSPENTRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNSRNTEGAGL
GLSIAKAIIELHGGSASAEYDDNHDLFKVRLP
>gnl|CDD|340401 cd16924, HATPase_YpdA-YehU-LytS-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA, YehU, Bacillus subtilis LytS, and some hybrid sensor histidine kinases. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. It also includes the HATPase domains of Escherichia coli YpdA and YehU, HKs of YpdA-YpdB and YehU-YehTCSs, which are involved together in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), some having accessory sensor domain(s) such as Cache, HAMP or GAF; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain
IPPFTLQPLVENAIQHGLSPLTDKGVVTISALKEDNHVMIEVEDNGRGIDPKVLNILGKKPKEGNGIGLY
NVHQRLILLFGEDYGIHIASEPDKGTRITFTIP
>gnl|CDD|340402 cd16925, HATPase_TutC-TodS-like, Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain
DAEKYERVVLNLLSNAFKFTPDGGRIRCILEKFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTR
AHGGTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP
>gnl|CDD|340403 cd16926, HATPase_MutL-MLH-PMS-like, Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains. This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease
VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSK
ISSFEDLFSITTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDGGGIIEEVKPAAAPVGTTVTVRD
LFYNTPARRKFLKSPKTELSKILDLVQRLALAHPDVSFSLTHDGKLVL
>gnl|CDD|340404 cd16927, HATPase_Hsp90-like, Histidine kinase-like ATPase domain of human cytosolic Hsp90 and its homologs including Escherichia coli HtpG, and related domains. This family includes the histidine kinase-like ATPase (HATPase) domains of 90 kilodalton heat-shock protein (Hsp90) eukaryotic homologs including cytosolic Hsp90, mitochondrial TRAP1 (tumor necrosis factor receptor-associated protein 1), GRP94 (94 kDa glucose-regulated protein) of the endoplasmic reticulum (ER), and chloroplast Hsp90C. It also includes the bacterial homologs of Hsp90, known as HtpG (High temperature protein G). Hsp90 family of chaperones assist other proteins to fold correctly, stabilizes them against heat stress, and aids in protein degradation
NQLLDLIIHSLYSNKEIFLRELISNASDALDKLRYLSLTDPSLLDDDPELEIRISPDKENRTLTISDTGI
GMTKEELINNLGTIARSGTKAFLEALQEGAKDSDLIGQFGVGFYSAFMVADKVTVTTKSAGDDEGYRWES
DGGGSYTIEEAEGELGRGTKITLHLKEDAKEFLEEARIKELVKKYSDFI
>gnl|CDD|340405 cd16928, HATPase_GyrB-like, Histidine kinase-like ATPase domain of the B subunit of DNA gyrase. This family includes histidine kinase-like ATPase domain of the B subunit of DNA gyrase. Bacterial DNA gyrase is a type II topoisomerase (type II as it transiently cleaves both strands of DNA) which catalyzes the introduction of negative supercoils into DNA, possibly by a mechanism in which one segment of the double-stranded DNA substrate is passed through a transient break in a second segment. It consists of GyrA and GyrB subunits in an A2B2 stoichiometry; GyrA subunits catalyze strand-breakage and reunion reactions, and GyrB subunits hydrolyze ATP. DNA gyrase is found in bacteria, plants and archaea, but as it is absent in humans it is a possible drug target for the treatment of bacterial and parasite infections
LHHLVWEIVDNSIDEALAGYATEIEVTLHEDNSITVEDNGRGIPVDIHPKTGKSAVEVVLTVLHAGGKFD
GGSYKVSGGLHGVGVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTPLEVIGETKKTGTTVRFWPDPEI
FEKTEFDFDTLKRRLRELAFLNKGLKIVLEDERTGKEEVF
>gnl|CDD|340406 cd16929, HATPase_PDK-like, Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains. This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids
SPKKVVEDASEEARVLCDDYYLSSPELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDDSDDL
PPIKVTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDFSDLISGTQPSPLAGFGYGLPM
SRLYAEYFGGDLDLQSMEGYGTDVYIYLK
>gnl|CDD|340407 cd16930, HATPase_TopII-like, Histidine kinase-like ATPase domain of eukaryotic topoisomerase II. This family includes the histidine kinase-like ATPase (HATpase) domains of human topoisomerase IIA (TopIIA) and TopIIB, Saccharomyces cerevisae TOP2p, and related proteins. These proteins catalyze the passage of DNA double strands through a transient double-strand break in the presence of ATP
YVPGLYKIFDEILVNAADNKQRDKSMTCIKVTIDPENNEISVWNNGKGIPVVIHKEEKIYVPEMIFGHLL
TSSNYDDDEKKVTGGRNGYGAKLCNIFSTEFTVETADSESKKKFKQTWTNNMGKASEPKITPYEKGKDYT
KVTFKPD
>gnl|CDD|340408 cd16931, HATPase_MORC-like, Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains. This family includes the histidine kinase-like ATPase (HATPase) domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains. In addition to the HATPase domain, MORC family proteins have a CW-type zinc finger domain containing four conserved cysteines and two conserved tryptophans, and coiled-coil domains at the carboxy-terminus. MORC1 has cross-species differential methylation in association with early life stress, and genome-wide association with major depressive disorder (MDD). MORC2 is involved in several nuclear processes, including transcription modulation and DNA damage repair, and exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY. MORC3 regulates p53, and is an antiviral factor which plays an important role during HSV-1 and HCMV infection, and is a positive regulator of influenza virus transcription. MORC4 is highly expressed in a subset of diffuse large B-cell lymphomas and has potential as a lymphoma biomarker
FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDINLLRGGFMLSFLDDGNGMTPEEAHHMISFGFS
DKRSDDHDHIGRYGNGFKSGSMRLGRDVIVFTKKDESQSCGLLSQTFL
>gnl|CDD|340409 cd16932, HATPase_Phy-like, Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E. This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events
YGDQIRLQQVLADFLLNAVRFTPSPGGWVEIKVSPTKKQIGDGVHVIHLEFRITHPGQGLPEELVQEMFE
ENQWTTQEGLGLSISRKLVKLMNGDVRYLREAGRSYFLITLEL
>gnl|CDD|340410 cd16933, HATPase_TopVIB-like, Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B. This family includes the histidine kinase-like ATPase (HATPase) domain of the B subunit of topoisomerase VI (Topo VIB). Topo VI is a heterotetrameric complex composed of two TopVIA and two TopVIB subunits and is categorized as a type II B DNA topoisomerase. It is found in archaea and also in plants. Type II enzymes cleave both strands of a DNA duplex and pass a second duplex through the resulting break in an ATP-dependent mechanism. DNA cleavage by Topo VI generates two-nucleotide 5'-protruding ends
AEFFRKNKEMLGFDNPIRSLYTTVRELVENSLDATEEAGILPDIKVEIEEIGKDHYKVIVEDNGPGIPEE
QIPKVFGKVLYGSKYHNKQSRGQQGLGISAAVLYSQMTTGKPVEIISSTKDSNYAYVVKLMIDTDKNEPE
ILEKEEVENRYKWHGTRVELELEGNWVAARSQILEYYKRTAVIAPYAEIIFIVPDGETEVFRR
>gnl|CDD|340411 cd16934, HATPase_RsbT-like, Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains. This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B
DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEILAVDQGPGI
ADVDEALRDGFSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVVARK
>gnl|CDD|340412 cd16935, HATPase_AgrC-ComD-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Staphylococcus aureus AgrC and Streptococcus pneumoniae ComD which are involved in quorum sensing. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Staphylococcus aureus AgrC which is an HK of the accessory gene regulator (agr) quorum sensing two-component regulatory system (TCS) AgrC-AgrA. The agr system plays a part in the transition from persistent to virulent phenotype. This family also includes Streptococcus pneumoniae ComD HK of the ComD-ComE TCS, involved in quorum sensing and genetic competence
ALDSLLSEKLELAREKGIEFTIEIDIPILLPISPLDLCIIFGNLLDNAIEACAKIDKENRFIHLKIRQKK
GFLIISIENSYEGELKKKNGLFLSTKKDKNHGIGLKSIREIVKKYNGNLSIEYENGIFTLSILL
>gnl|CDD|340413 cd16936, HATPase_RsbW-like, Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains. This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B
VELAVSEAVTNAVRHAYRHDGPGPVRLELDLDPDRLRVEVTDSGPGFDPLRPADPDAGLREGGRGLALIR
ALMDEVGYRRTPGGKTVWLEL
>gnl|CDD|340414 cd16937, HATPase_SMCHD1-like, Histidine kinase-like ATPase domain of structural maintenance of chromosomes flexible hinge domain containing 1 (SMCHD1) protein. This family includes histidine kinase-like ATPase (HATPase) domain of structural maintenance of chromosomes flexible hinge domain containing 1 (SMCHD1) protein, which is involved in gene silencing and in DNA damage. It has critical roles in X-chromosome inactivation and is also an important regulator of autosomal gene clusters. Upon DNA damage, SMCHD1 promotes non-homologous end joining and inhibits homologous recombination repair. SMCHD1 is implicated in the pathogenesis of facioscapulohumeral muscular dystrophy
GMYEYYASEGQNPLPFALAELIDNSLSATRRNTDIRRIQIKLLFDEAQGKPAVAVIDNGRGMTSKQLNNW
AVYRLSKFTRQGDFESDHSGYVRPDPVPRSLNSDISYFGVGGKQAVFFV
>gnl|CDD|340415 cd16938, HATPase_ETR2_ERS2-EIN4-like, Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains. This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain
LPDVVVGDERRVFQVLLHMLGNLLKMRNGGGNITFRVFLEGGSEDRSDRDWGPWRPSMSDESVEIRFEVE
INDSGSPSIESASMRNSLNRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL
>gnl|CDD|340416 cd16939, HATPase_RstB-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain
MARALDNLLRNALRYAHRTVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGL
GLAIVHRVALWHGGHVECDDSELGGACFRLTWPR
>gnl|CDD|340417 cd16940, HATPase_BasS-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain
SAADIQVQGDALLLFLLLRNLVDNAVRYSPQGSRVEIKLSADDGAVIRVEDNGPGIDEEELEALFERFYR
SDGQNYGGSGLGLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL
>gnl|CDD|340418 cd16942, HATPase_SpoIIAB-like, Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains. This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F
RNEMHLQFSARSENESFARVTVAAFVAQLDPTIDELTEIKTVVSEAVTNAIIHGYNNDPNGIVSISVIIE
DGVVHLTVRDEGVGIPDIEEARQPLFTTKPELERSGMGFTIMENFMDEVIVESEVNKGTTVYLKK
>gnl|CDD|340419 cd16943, HATPase_AtoS-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS. This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains
PSQLNQVLLNLLVNAAQAMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTKPVGEGTG
LGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI
>gnl|CDD|340420 cd16944, HATPase_NtrY-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY. This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains
DTTQISQVLTNILKNAAEAIEGRPSDVGEVRIRVEADQDGRIVLIVCDNGKGFPREMRHRATEPYVTTRP
KGTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP
>gnl|CDD|340421 cd16945, HATPase_CreC-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS
DPFLLRQAINNLLDNAIDFSPEGGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSLPRPHSGQ
KSTGLGLAFVQEVAQLHGGRITLRNRPDGVLAFLTL
>gnl|CDD|340422 cd16946, HATPase_BaeS-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain
DRDRLQQLFVNLLENSLRYTDTGGKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRA
SGGSGLGLAICHNIALAHGGTISAEHSPLGGLRLVLTLP
>gnl|CDD|340423 cd16947, HATPase_YcbM-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA)
FQVEINIPDRPIYANANTEALQRILKNLISNAIKYGSDGKFLGMTLREDEKHVYIDIWDKGKGISETEKD
HVFERLYTLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTLK
>gnl|CDD|340424 cd16948, HATPase_BceS-YxdK-YvcQ-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds
TDAKWLSFIIGQIVSNALKYSKQGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGENGRNF
QESTGMGLYLVKKLCDKLGHKIDVESEVGEGTTFTITFP
>gnl|CDD|340425 cd16949, HATPase_CpxA-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA. This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain
LARALENVLRNALRYSPSKILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGL
GLAIAERAIEQHGGKIKASNRKPGGLRVRIWLPA
>gnl|CDD|340426 cd16950, HATPase_EnvZ-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain
LKRVLSNLVDNALRYGGGWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARGTSGTGLGL
AIVQRISDAHGGSLTLANRAGGGLCARIELP
>gnl|CDD|340427 cd16951, HATPase_EL346-LOV-HK-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2. This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain
LGEYINRIASAINAIHAVGDIRINITGDTGPVSSEVATAIGLVVNELLQNALKHAFSDREGGTITIRSVV
DGDYLRITVIDDGVGLPQDEDWPNKGSLGLQIVRSLVEGELKAFLEVQSAENGTRVNIDIP
>gnl|CDD|340428 cd16952, HATPase_EcPhoR-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR. This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism
LRSAFSNLVSNAVKYTPPSDTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGT
GLGLAIVKHVMSRHDARLLIASELGKGSRFTCLFPSSR
>gnl|CDD|340429 cd16953, HATPase_BvrS-ChvG-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain
LGQVLRNLIGNAISFSPPDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAFGQH
SGLGLSISRQIIEAHGGISVAENHNQPGQVIGARFTVQLP
>gnl|CDD|340430 cd16954, HATPase_PhoQ-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain
PLLDSLCSALNKVYQRKGVSISLDISPELRFPGERNDLMELLGNLLDNACKWCLEFVEVTARQTDGGLHL
IVDDDGPGVPESQRSKIFQRGQRLDEQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF
>gnl|CDD|340431 cd16955, HATPase_YpdA-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli YpdA, a HK of the two-component system (TCS) YpdA-YpdB which is involved in a nutrient sensing regulatory network with YehU-YehT. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and some have a GAF sensor domain; some contain a DUF3816 domain; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain
IPKLMIQPLVENAIVHGIQEKKGKGVVKISVKKQLKNRLHIAVEDNGIGISPKVIERVEQDEMPGNKIGL
LNVHQRLKLGYGEGLHIRSRPDPGTLIAFYIP
>gnl|CDD|340432 cd16956, HATPase_YehU-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YehU. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Escherichia coli YehU, a HK of the two-component system (TCS) YehU-YehT which is involved in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase); some have a GAF sensor domain while some have a cupin domain
LPFLTLQPIVENAVKHGLSGLLDGGRVEITARLDGQHLLLEVEDNGGGMDPDTLARILIRSSNGLGLNLV
DKRLRQAFGNDYGLDIECAPGEGTRITIRLP
>gnl|CDD|340433 cd16957, HATPase_LytS-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis LytS and Staphylococcus aureus LytS. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and a GAF sensor domain; most contain a DUF3816 domain
VPPFALQVLVENAIRHAFPKRKENNEVRVVVKKDQHKVHVSVSDNGQGIPEERLDLLGKTTVTSEKGTGT
ALENLNRRLIGLFGSEACLHIESEVHGGTEVWFVIP
>gnl|CDD|341131 cd16961, RMtype1_S_TRD-CR_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR) and similar domains. The restriction-modification (RM) system S subunit generally consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This superfamily represents a single TRD-CR unit; in addition to type I TRD-CR units, it includes RMtype1_S_TRD-CR_like domains of various putative Helicobacter type II restriction enzymes and methyltransferases, such as Hci611ORFHP and HfeORF12890P, as well as TRD-CR-like sequence-recognition domains of the M subunit of putative type I DNA methyltransferase such as M2.CinURNWORF2828P and M.Mae7806ORF3969P
KKLGEIAEIISGKTPSSSSEYWDNGIIPWIRISDINNGGIILTDEKITEEGAEKLKKKILPKGDILISRS
GTIGKVAIVKENDKALLNQAVIVIRPKDEVDSEFLYYFLKSPFGKKLIEGSAGSTQPNLNKSDLKNLKIP
LPPLEEQKKIANILDKLDALIELLEQKLEKLEQLKQAL
>gnl|CDD|438562 cd16962, RuvC, Crossover junction endodeoxyribonuclease RuvC. Crossover junction endodeoxyribonuclease RuvC is also called Holliday junction resolvase RuvC. It is part of the RuvABC pathway in Escherichia coli and other Gram-negative bacteria that is involved in processing Holliday junctions, which are formed by the reciprocal exchange of strands between two DNA duplexes. Holliday junction resolvases (HJRs) are endonucleases that specifically resolve Holliday junction DNA intermediates during homologous recombination. RuvC is thought to bind either on the open, DNA exposed face of a single RuvA tetramer, or to replace one of the two tetramers. Binding is proposed to be mediated by an unstructured loop on RuvC, which becomes structured on binding RuvA. RuvC can be bound to the complex in either orientation, therefore resolving Holliday junctions in either a horizontal or vertical manner. HJRs occur in archaea, bacteria, and in the mitochondria of certain fungi. These are referred to as the RuvC family of Holliday junction resolvases, RuvC being the Escherichia coli HJR. RuvC and its orthologs are homodimers and display structural similarity to RNase H and Hsp70
ILGIDPGLRRTGYGVIEVEGNKLRLLDYGVIRTPSKLSLPERLKEIYDGLSELIEKYKPDEVAIEKLFFN
KNPKSALKLGQARGVILLAAAQAGLPVVEYTPRQVKQAVTGYGRADKEQVQYMVKRLLGLKEIPKPDDAA
DALAIALCHAHS
>gnl|CDD|438563 cd16963, CCE1, fungal mitochondrial Holliday junction resolvases similar to Saccharomyces cerevisiae CCE1. Saccharomyces cerevisiae Cruciform cutting endonuclease 1 (CCE1) is a Holliday junction resolvase specific for 4-way junctions. CCE1 is involved in the maintenance of mitochondrial DNA. Holliday junction resolvases (HJRs) are endonucleases that specifically resolve Holliday junction DNA intermediates during homologous recombination. Holliday junctions are formed by the reciprocal exchange of strands between two DNA duplexes. HJRs occur in archaea, bacteria, and in the mitochondria of certain fungi; they may form homodimers and display structural similarity to RNase H and Hsp70
LAQLKSLAILCGLPSSGTKAELIARLEDQLKELASLSKKLPGPLSILSIDMGIRNLAYCHLSLPKTSPHR
RKPTLVDWNKLDLEEKFGVSGADKLSFSPSYYARLAYQLVNELLLPPNPDLILIERQRFRSGGSSAVLEW
TLRVNMLEAMLYAVLYTRRQQGKSKSKADVISSSPQRMVRYWLSRLDRKSSRPDVKKKKKKSYKNSKKAR
IDLVKNWLSDSNVSPFLLLLPELSSRLRKLFNKKKSLKKTSTSDDAAGVKKLDDLADSLLQGLAWLEWQQ
NREELKEL
>gnl|CDD|438564 cd16964, YqgF, putative pre-16S rRNA nuclease YqgF and RuvX family. Escherichia coli YqgF has been shown to act as a pre-16S rRNA nuclease, presumably as a monomer. It is involved in the processing of pre-16S rRNA during ribosome maturation. The RuvX gene product from Mycobacterium tuberculosis was shown to act, in a dimeric form, as a Holliday junction resolvase (HJR). HJRs endonucleases specifically resolve Holliday junction DNA intermediates during homologous recombination. Holliday junctions are formed by the reciprocal exchange of strands between two DNA duplexes. HJRs occur in archaea, bacteria, and in the mitochondria of certain fungi; they may form homodimers and display structural similarity to RNase H and Hsp70
ILGIDYGTKRIGLAISDPLGIIASPLETIERKNLEKLLEELKKIIKEEKIEKIVVGLPLNMDGTESEQAE
KVRKFAEKLKKRFGLPVVLVDERLTTKEAERILREAGKKRKKRKKKIDALAAAIILQSYLDS
>gnl|CDD|341215 cd16965, Alpha_kinase_ChaK, Alpha-kinase domain of channel kinases. This group is composed of channel kinases 1 (ChaK1) and 2 (ChaK2), and similar proteins. ChaK1 and ChaK2 are also called transient receptor potential cation channel subfamily M members 7 (TRMP7) and 6 (TRMP6), respectively. They are fusion proteins containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. They are both cation-selective channels that preferentially permeate Zn2+, Mg2+, and Ca2+ ions. They are central regulators of Mg2+ and Ca2+ homeostasis. TRMP7 is ubiquitously expressed while TRMP6 is highly expressed in specific tissues such as the kidney and intestine. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions
EEVTVYRLEESSPDPLSSSMSSWSQNGRTAVIQPLSQEEMDGGLRRATKVVCTWSEGDILKLGSVYIVKS
FLPEVVRTWQKIFPESTVLHLCLREIQQQRAAQKLMQRFNQVKPSSIPYSPRFLEVFLLYCHSAGQWLTV
ENNMTGEFRKYNNNNGDEILPTNTLEETMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKVEDKSSG
EMVFGPANLGEDAIQNFVAKHHCNSCCRK
>gnl|CDD|341216 cd16966, Alpha_kinase_ALPK2_3, Alpha-kinase domain of alpha-protein kinases 2 and 3. Alpha-protein kinases 2 (ALPK2) and 3 (ALPK3) are also called heart alpha-protein kinase (HAK) and muscle alpha-protein kinase (MAK), respectively. They both contain a C-terminal alpha-kinase domain and two immunoglobulin (Ig)-like domains. Loss of function mutations in ALPK3 can cause early-onset and familial cardiomyopathy in humans. The ALPK2 gene may also be a novel candidate gene for inherited hypertension in Dahl rats. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions
TEVGEEIEMSPLIFAKDLLDSGYWGDKLFGRIATEELHFGEGVLRKASRSKVIYGLMPIFKSGHTCIIKV
HNAIAYGTRNEDSLIQRNYKLTAQECKVQNTAREYAKIFAAEARPLEGFGEVPEIIPLFLIYRPANNIPY
ATVEEELIGPFVKYSIRDGKEINFLRSESEAGQKCCTFQHWVYQWTNGCLLVTDLQGVGMKLTDVGIATL
AKGYQGLKGNCSMTFIDQFAALHQCNKYC
>gnl|CDD|341217 cd16967, Alpha_kinase_eEF2K, Alpha-kinase domain of eukaryotic elongation factor-2 kinase. Eukaryotic elongation factor-2 kinase (eEF2K) is also called calcium/calmodulin (CaM)-dependent eEF2K. It phosphorylates eukaryotic elongation factor-2 (EEF2) at a single site, leading to its inactivation and inability to bind ribosomes, and slowing down the elongation stage of protein synthesis. It has been linked to many human diseases including cardiovascular conditions (atherosclerosis) and pulmonary arterial hypertension, as well as solid tumors and neurological disorders. eEF2K is an atypical protein kinase containing a CaM binding region, an alpha-kinase catalytic domain, and TPR-like Sel1 repeats at the C-terminus. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions
HLEDLPTERAVRHRYNAATKKWTKDEVLVKMESKPFARGAMRECYRAKKLSNFSHNQDWKHASNYVAKRY
IEPVDREVYFEDVRLQMDAKLWGEEYNRHNPPKKVDIMQMCVLEFVDRPGSPLYHLEHFIEGDYIKYNSN
SGFVRDDDIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTADGEGYGDGNLGLRGMALFFHSH
RCNPIC
>gnl|CDD|341218 cd16968, Alpha_kinase_MHCK_like, Alpha-kinase domain of myosin heavy chain kinase and similar domains. This group is composed of alpha-kinase domains of Dictyostelium discoideum myosin heavy chain kinases A-D (MHCKA, MHCKB, MHCKC, MHCKD), alpha-protein kinase 1 (AK1), and similar proteins. The myosin heavy chain kinases are involved in regulating myosin II filament assembly in Dictyostelium discoideum. They phosphorylate target threonine residues located in the carboxyl-terminal portion of the myosin II heavy chain (MHC) tail, resulting in filament disassembly. The different MHCK isoforms display different spatial regulation, indicating specific roles for each isoform in fine tuning the Dictyostelium actomyosin cytoskeleton. They all contain an alpha-kinase domain as well as WD40 repeats at the C-terminus. AK1 contains an N-terminal Arf-GAP domain and a central alpha-kinase domain. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions
RAIKHEFDPETGKWTSTATKVKIDPKPFAEGALREAYHLKDLSAPGPSTLFVAKLSKDPNESRETYFEDV
EMQMVCKKWAEKFNAKNPPKKVEFLPAWVLELVDRPPPPLCGVEPFIEGEYVKHNNNFGYVDEDERNTPQ
AFSHFTYEASGHQLLVVDIQGVGDLYTDPQIHTIDGKGFGKGNLGQKGIEKFLETHKCNAIC
>gnl|CDD|341219 cd16969, Alpha_kinase_ALPK1, Alpha-kinase domain of alpha-protein kinase 1. Alpha-protein kinase 1 is also called chromosome 4 kinase or lymphocyte alpha-protein kinase (LAK). ALPK1 is implicated in epithelial cell polarity and exocytic vesicular transport towards the apical plasma membrane. It resides on Golgi-derived vesicles where it phosphorylates myosin IA, a motor protein that regulates the delivery of vesicles to the plasma-membrane. It may be associated with inflammation-related diseases such as gout and type 2 diabetes mellitus. ALPK1 contains a C-terminal alpha-kinase domain, an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions
PDQLKRAHDALLLKYSKKSGLWTAQETMVYIGDNLQVGKQGKQRNAFWVHFLHQEETLGRYVGKEYKKPK
ELQYHFNDVERQMTAQHYVTEFNKRLYEQNIPTQIFFIPSVILLILEDKGIKGCVSVEPYMLGEFVKLTN
NTTVKKEEYKATDYGLAYGHFTYEFSNHQDVVVDLQGWVTANGKGLTYLTDPQIHSVVKKSGTTNFGKKG
IEYFFNNQHTECNEICR
>gnl|CDD|341220 cd16970, Alpha_kinase_VwkA_like, Alpha-kinase domain of Dictyostelium discoideum VwkA and similar domains. Dictyostelium discoideum alpha-protein kinase VwkA is also called von Willebrand factor A alpha-kinase or vWF kinase. It influences myosin II abundance and assembly behavior as vWKA gene disruption leads to significant myosin II overassembly. VwkA also serves a critical conserved role in the periodic contractions of the contractile vacuole through its regulation of the myosin II cortical cytoskeleton. It contains a vWFa domain (named after its homology to von Willebrand factor A, a plasma glycoprotein essential for proper blood clotting) and a C-terminal alpha-kinase domain. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions
LPEIKGRQIKFTLPRLLDDCLFALEEMSIREITVKIAPPPFAKGAERWAYYALDTTSDSTKKVVLKEFKT
PGSAQRNSRERYLESMEVQTVAAKLAFEFNKLLARAGINKKITFLEAKVLRVANGDSPQYYTMESFLEGE
YKKFNNNVGVVNEDEVEILQAFSHWTYEASKGYLMVVDLQGVRTDDDGFLLTDPAIHCTDVLRFGRTNLG
KEGIDKFFATHKCNQHC
>gnl|CDD|341221 cd16971, Alpha_kinase_ChaK1_TRMP7, Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation channel subfamily M member 7. Channel kinase 1 (ChaK1), also called transient receptor potential cation channel subfamily M member 7 (TRMP7) or long transient receptor potential channel 7 (LTrpC7), is a fusion protein containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. It is ubiquitously expressed and is a cation-selective channel that preferentially permeates Zn2+, Mg2+, and Ca2+ ions. It is a central regulator of Mg2+ and Ca2+ homeostasis. TRPM7 plays a role in cancer proliferation, stroke, hydrogen peroxide dependent neurodegeneration, and heavy metal toxicity. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions
EPVTVYRLEESSPNILNNSMSSWSQLGLCAKIEFLSKEEMGGGLRRALKVVCTWSENDILKSGHLYIIKS
FLPEVVNTWSSIYKEDTVLHLCLREIQQQRAAQKLTFAFNQMKPKSIPYSPRFLEVFLLYCHSAGQWFAV
EECMTGEFRKYNNNNGDEIIPTNMLEETMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKAGEKRSY
DMVFGPANLGEDAIKNFRAKHHCNSCCRK
>gnl|CDD|341222 cd16972, Alpha_kinase_ChaK2_TRPM6, Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation channel subfamily M member 6. Channel kinase 2 (ChaK2), also called transient receptor potential cation channel subfamily M member 6 (TRMP6) or melastatin-related TRP cation channel 6, is a fusion protein containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. It is highly expressed in the kidney and instestine. It is a cation-selective channel that preferentially permeates Zn2+, Mg2+, and Ca2+ ions. It is a central regulator of Mg2+ and Ca2+ homeostasis. TRPM6 is considered to be the Mg2+ entry pathway in the distal convoluted tubule of the kidney, where it functions as a gatekeeper for controlling the body's Mg2+ balance. Mutations in the TRPM6 gene cause the autosomal recessive disorder hypomagnesemia with secondary hypocalcemia, which often results in severe muscular and neurologic complications from early infancy that can lead to neurologic damage or cardiac arrest if left untreated. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions
EEITVYRLEESSPTNLDKSMSSWSQRGMAAMIQVLSREEMDGGLRRAMKVVCTWSEDDVLKPGQVFIVKS
FLPEVVQTWQKIFNNSTVLHLCLREIQQQRAAQKLIYTFNQVKPHSIPYTPRFLEVFLIYCHSANQWLTI
EKYLTGEFRKYNNNNGDEITPTSLLEETLLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKPEDKQSR
GMVFGPANLGEDAIRNFIAKHHCNSCCRK
>gnl|CDD|341223 cd16973, Alpha_kinase_ALPK3, Alpha-kinase domain of alpha-protein kinase 3. Alpha-protein kinase 3 (ALPK3) is also called muscle alpha-protein kinase (MAK) or myocytic induction/differentiation originator (Midori). Its expression is restricted to fetal and adult heart and adult skeletal muscle, and is localized in the nucleus. It is thought to act as a transcriptional regulator implicated in early cardiac development. Loss of function mutations in ALPK3 can cause early-onset and familial cardiomyopathy in humans. ALPK3 contains a C-terminal alpha-kinase domain and two immunoglobulin (Ig)-like domains. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions
IEVGEEIEMTPMVFAKGLADSGYWGDKFFGRVMTEEAHIGEGCLRKACRAKVIYGLEPVFESGSTCIIKV
RNPIAYGTKNESSLAERNYEITIQECKIQNMAREYCKIFAAEARAVPNFGAVLEIIPLYLIYRPANNIPY
ATVEEDLKGVFQKYCVLDRTGSLVARTKSEVEQKCCTFQHWIYQWTNGNMLVTDLEGVDWKITNVGIATK
SKGYQGLKESCSPKVFEQFISHHQCNYYC
>gnl|CDD|341224 cd16974, Alpha_kinase_ALPK2, Alpha-kinase domain of alpha-protein kinase 2. Alpha-protein kinase 2 (ALPK2) is also called heart alpha-protein kinase (HAK). Little functional information is known about ALPK2. In a three-dimensional colonic-crypt model, it has been identified as crucial for luminal apoptosis and expression of DNA repair-related genes, possibly in the transition of normal colonic crypt to adenoma. The ALPK2 gene may also be a novel candidate gene for inherited hypertension in Dahl rats. ALPK2 contains a C-terminal alpha-kinase domain and two immunoglobulin (Ig)-like domains. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions
EKGGEEIEFSQLMFKEDFLSDSYFGGNLHGRIATEKLHFGEGMHRKAFRSKVMCGLLPVFLPGHACVLKV
HNAIAYGTKNNDELIQKNYKLAVQECYVQNTAREYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPANNIPY
ATVEEELIGDFVKYSVRDGKEINVLRRDSEAGQKCCTFQHWVYQKTDGNLLVTDMQGVGMKLTDVGIATC
SKGYKGFKGNCSVSFIDQFKALHQCNKYC
>gnl|CDD|340434 cd16975, HATPase_SpaK_NisK-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals
DTLLLSRALINIISNACQYAPEGGTVSISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSG
GHYGMGLYIAKNLVEKHGGSLIIENSQKGGAEVTVKI
>gnl|CDD|340435 cd16976, HATPase_HupT_MifS-like, Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS. This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain
IQQVLMNLLQNALDAMGKVENPRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKPVGKGTGL
GLSISYGIVEEHGGRLSVANEEGAGARFTFDL
>gnl|CDD|340774 cd16977, VHS_GGA, VHS (Vps27/Hrs/STAM) domain of GGA (Golgi-localized, Gamma-ear-containing, Arf-binding) subfamily. GGA (Golgi-localized, Gamma-ear-containing, Arf-binding) comprises a subfamily of ubiquitously expressed, monomeric, motif-binding cargo/clathrin adaptor proteins involved in membrane trafficking between the Trans-Golgi Network (TGN) and endosomes. The VHS domain has a superhelical structure similar to the structure of the ARM (Armadillo) repeats and is present at the N-termini of proteins. GGA proteins have a multidomain structure consisting of an N-terminal VHS domain linked by a short proline-rich linker to a GAT (GGA and TOM) domain, which is followed by a long flexible linker to the C-terminal appendage, GAE (Gamma-Adaptin Ear) domain. The VHS domain of GGA proteins binds to the acidic-cluster dileucine (DxxLL) motif found on the cytoplasmic tails of cargo proteins trafficked between the Trans-Golgi Network and the endosomal system
LERWINRATNPSNAEPDWALILGFCDQINEDGEGPRDAARLLAHKIQSPQEWEAIQALTVLEVCMKNCGY
RFHLEVGKFRFLNELIKVVSPKYLGSRRSEKVKRKILELLYSWTVTLPEEGKIRDAYQMLKKQ
>gnl|CDD|340775 cd16978, VHS_HSE1, VHS (Vps27/Hrs/STAM) domain of Class E vacuolar protein-sorting machinery protein HSE1. Class E vacuolar protein-sorting machinery protein HSE1, together with Vps27, comprise the ESCRT-0 complex, the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB). The complex directly binds to ubiquitinated transmembrane proteins and recruits both ubiquitin ligases and deubiquitinating enzymes. It is also required the efficient recycling of late Golgi proteins including the carboxypeptidase Y (CPY) sorting receptor, Vps10. Similar to metazoan STAMs, HSE1 contain: an N-terminal VHS domain, which is involved in cytokine-mediated intracellular signal transduction and has a superhelical structure similar to the structure of ARM (Armadillo) repeats; a Ubiquitin-Interacting Motif (UIM); a SH3 (Src Homology 3) domain, a well-established protein-protein interaction domain; and a GAT (GGA and TOM) domain, which is essential for the normal sorting function of HSE1
IDELIIKATDETLTSENWQYILDVCDKVNSDPEDGAREAIAAIQKRLQHRNANVQLRSLSLADALAKNCG
SRLHQEISSRSFTQTLLRLINDRTTHATVKKRILELIKQLSDSFKSDPSLGLMSDTYDQLKSKY
>gnl|CDD|340776 cd16979, VHS_Vps27, VHS (Vps27/Hrs/STAM) domain of Vacuolar protein sorting-associated protein 27. Vacuolar protein sorting-associated protein 27 (Vps27 or Vps27p) is also called Golgi retention defective protein 11, and is the yeast homolog of Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate). Together with class E vacuolar protein-sorting machinery protein HSE1, it comprises the ESCRT-0 complex, the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB). The complex directly binds to ubiquitinated transmembrane proteins and recruits both ubiquitin ligases and deubiquitinating enzymes. It is also required the efficient recycling of late Golgi proteins including the carboxypeptidase Y (CPY) sorting receptor, Vps10. Vps27 contain similar domains and motifs to Hrs; it contains an N-terminal VHS domain, which has a superhelical structure similar to the structure of ARM (Armadillo) repeats, a FYVE (Fab1p, YOTB, Vac1p, and EEA1) zinc finger domain, two Ubiquitin-Interacting Motifs (UIMs), a GAT (GGA and TOM) domain, two a P(S/T)XP motifs that recruit ESCRT-I, and a short peptide motif near the C-terminus that recruits clathrin
SEFDELIEKATSESIPNGEEDLALALEISDLIRSKSVPPKDAMRSLKKRILHKNPNVQLLALKLTDVCVK
NGGDHFLVEIASREFMDNLVSLIRSTGVNPEVKEKILRLIQEWALAFKSKSQLSYVVEVYKKLKSEGIEF
P
>gnl|CDD|340777 cd16980, VHS_Lsb5, VHS (Vps27/Hrs/STAM) domain of LAS seventeen-binding protein 5. LAS seventeen-binding protein 5 (LAS17-binding protein 5, Lsb5, or Lsb5p) localizes to the plasma membrane and plays a role in endocytosis in yeast. It interacts with actin regulators Sla1p and Las17p, ubiquitin, and Arf3p, coupling actin dynamics to membrane trafficking processes. Lsb5p contains an N-terminal VHS domain and a GAT (GGA and TOM) domain. The VHS domain has a superhelical structure similar to the structure of ARM (Armadillo) repeats. It is a right-handed superhelix of eight alpha helices. The VHS domain has been found in a number of proteins, some of which have been implicated in intracellular trafficking and sorting
ITDTIERLTSSEYEEEDWSLVLELCELINLIESGAKEAARALRKKLKYGNPHQQLRALTLLDLLVENGGK
KFQAQFASDKKLEDLLRLIASDPSTDPKVRKKLLELLGGWAYEFKGDPGLSGIASLYKKVKP
>gnl|CDD|340778 cd16981, CID_RPRD_like, CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing proteins. This family is composed of Regulation of nuclear pre-mRNA domain-containing proteins 1A (RPRD1A), 1B (RPRD1B), 2 (RPRD2), yeast Rtt103, and similar proteins. RPRD1A, RPRD1B, and RPRD2 are CID (CTD-Interacting Domain) containing proteins that co-purify with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. Yeast transcription termination factor Rtt103 is a CID containing protein that functions in DNA damage response. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices
EEALEKKLRSLNNTQQSIQTLSLWCLFHKKHAKQIVKIWLKELKKAKPERKLTLLYLANDVLQNSRRKGA
PEFVEAFKKVLPEALALVRSEGDESVRKKVLRVLNIWEERNVFGSEFLAELRAIL
>gnl|CDD|340779 cd16982, CID_Pcf11, CID (CTD-Interacting Domain) of Pcf11. Pcf11 is conserved across eukaryotes. The best studied protein is Saccharomyces cerevisiae Pcf11, also called protein 1 of CF I, an essential subunit of the cleavage factor IA (CFIA) complex which is required for polyadenylation-dependent pre-mRNA 3'-end processing and RNA polymerase (Pol) II (RNAP II) transcription termination. Human Pcf11, also referred to as pre-mRNA cleavage complex 2 protein Pcf11, has been shown to enhance degradation of RNAP II-associated nascent RNA and transcriptional termination. The family also includes plant PCFS4 (Pcf11-similar-4 protein or Polyadenylation and cleavage factor homolog 4) and Caenorhabditis elegans Polyadenylation and cleavage factor homolog 11. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. Pcf11 CID preferentially interacts with CTD phosphorylated at Ser2. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices
VEEYRSALAELTFNSKPIINNLTMLAEENIQAAQAIVEAIEERIRKVPPEQKLPALYLLDSIVKNVGGPY
TSLFSPNLVDLFLDAYRLVDEKTRKKLEKLLNTWKTVFPNGKLLFPDEVLNKIERAL
>gnl|CDD|340780 cd16983, CID_SCAF8_like, CID (CTD-Interacting Domain) of SR-related and CTD-associated factor 8 and similar proteins. This subfamily includes SR-related and CTD-associated factors 8 (SCAF8) and 4 (SCAF4), and similar proteins. SCAF4 is also called Splicing factor arginine serine rich 15 (SFRS15). Members may play roles in mRNA processing. Both SCAF4 and SCAF8 contains a CTD-interacting domain (CID) at the amino terminus and a Ser/Arg-rich domain followed by an RNA recognition motif. CID binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase (Pol) II (RNAP II). During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices
EEFNKELSSLLDSKPPVSKSKINAITKLAIKAIKFYKHVVQSVEKFIQKCKPEYKLPGLYVIDSIIRQSR
HQYGKEKDVYAPRFAKNLSKTFLNLLKCPEKDKPKVKRVLNLWQKNGVFPKEIIQPLLDAA
>gnl|CDD|340781 cd16984, CID_Nrd1_like, CID (CTD-Interacting Domain) of Nrd1 and similar proteins. This subfamily includes Saccharomyces cerevisiae protein Nrd1, Schizosaccharomyces pombe Rpb7-binding protein Seb1, and similar proteins. Nrd1 cooperates with Nab3 and Sen1, also called the Nrd1-Nab3-Sen1 (NNS) complex, to terminate the transcription by RNA polymerase (Pol) II (RNAPII) of many noncoding RNAs (ncRNAs), including small nuclear RNAs (snRNAs), small nucleolar RNAs (snoRNAs), and cryptic unstable transcripts (CUTs). Schizosaccharomyces pombe Seb1 does not function in an NNS-like termination pathway but promotes polyadenylation site selection of coding and noncoding genes. It cotranscriptionally controls alternative polyadenylation. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. Nrd1 CID preferentially interacts with CTD phosphorylated at Ser5. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices
EEFEATLKSLQALKPPGVSGSKIKKLTDIAVDNVQSESQIVSKLYRYFKKAPPTHKLGVLYVVDSVVRAW
IDQAKKNGQSIDSSAPDGTFAAGVYKITELIESLMNDAIQSAPEDQKEKIKKLVDIWEKGNTFPAEMLNS
IKQKL
>gnl|CDD|340782 cd16985, ANTH_N_AP180, ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) subfamily. The Adaptor Protein 180 (AP180) subfamily members are phosphatidylinositol-binding clathrin assembly proteins, including mammalian clathrin coat assembly protein AP180 and Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), Drosophila LAP (also called Like-AP180 or AP180), and Caenorhabditis elegans Uncoordinated protein 11 (unc-11, also called AP180-like adaptor protein). They are components of the adaptor complexes which link clathrin to receptors in coated vesicles. AP180 and CALM play important roles in clathrin-mediated endocytosis. AP180, also called 91 kDa synaptosomal-associated protein (SNAP91) or phosphoprotein F1-20, is a brain-specific clathrin-binding protein which stimulates clathrin assembly during the recycling of synaptic vesicles. CALM, also called phosphatidylinositol binding clathrin assembly protein (PICALM), is ubiquitously expressed. Members of this subfamily contain ANTH domains, which bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of the Adaptor Protein 180 (AP180) subfamily
LAKAVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNE
RFIQYLASRNSLFNLSNFLDKSGSQGYDMSTFIRRYAKYLNEKAISY
>gnl|CDD|340783 cd16986, ANTH_N_Sla2p_HIP1_like, ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily. Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily
FEKAVNKATNKTDSPPKPKHVRTIIVKSWTHQKGPQFYEELSKRLLLNNPVVQFKALVTLHKVLRDGPPE
LSLLGGYLDAWLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVFH
>gnl|CDD|340784 cd16987, ANTH_N_AP180_plant, ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly protein AP180 and similar proteins. This subfamily is composed of plant clathrin coat assembly protein AP180 and other ANTH domain containing proteins that are yet to be characterized. Arabidopsis thaliana AP180 (At-AP180) is a binding partner of plant alphaC-adaptin; it functions as a clathrin assembly protein that promotes the formation of cages with an almost uniform size distribution. In addition to At-AP180, Arabidopsis thaliana contains many ANTH domain containing proteins labelled as putative clathrin assembly proteins included in this subfamily such as At4g02650, At5g10410, At2g25430, and At1g33340, among others. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of plant clathrin coat assembly protein AP180 and similar proteins
LEVAVVKATSHDDAPPDEKYVREILSLGSSSRAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGS
PILEQELSLAPSGGRNPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDERLIFS
>gnl|CDD|340785 cd16988, ANTH_N_YAP180, ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins. This subfamily includes yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins. There are two YAP180 proteins in Saccharomyces cerevisiae, AP180A (yAP180A or YAP1801) and AP180B (yAP180B or YAP1802). They are involved in endocytosis and clathrin cage assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of plant clathrin coat assembly protein AP180 and similar proteins
YEKLVKGATKIKLAPPKAKYLDPILLATYSSDASFGEIVRALSRRLRDNSWTVVFKSLIVLHLMIREGET
DDVLLYYLSRPDFLDLRKIRNGSSAGSGQLQNIQRYAAYLKERVKEY
>gnl|CDD|340786 cd16989, ENTH_EpsinR, Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein. Epsin-related protein (EpsinR) is also called clathrin interactor 1 (Clint), enthoprotin, or epsin-4. It is a clathrin-coated vesicle (CCV) protein that binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), clathrin, and the gamma appendage domain of the adaptor protein complex 1 (AP1). It contains an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. The ENTH domain of human epsinR binds directly to the helical bundle domain of the mouse SNARE Vti1b; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding
IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRMLKDNKKNWRRVYKSLLLLDYLLKNG
SERVVTSAREHIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREERKKAK
>gnl|CDD|340787 cd16990, ENTH_Epsin, Epsin N-Terminal Homology (ENTH) domain of Epsin family. Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. They are important factors in clathrin-coated vesicle (CCV) generation. They contribute to membrane deformation and play a key function as adaptor proteins, coupling various components of clathrin-mediated uptake. They also have an important role in selecting and recognizing cargo. Three isoforms have been identified in mammals, epsin-1 to -3, and these are conserved in vertebrates. Epsin-1 is highly enriched and represents the dominant isoform in the brain. It is required for proper synaptic vesicle retrieval and modulates the endocytic capacity of synaptic vesicles. Epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of CCVs. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding
EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTG
SERVAQQCKENIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN
>gnl|CDD|340788 cd16991, ENTH_Ent1_Ent2, Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins. This subfamily is composed of the two orthologs of epsin in Saccharomyces cerevisiae, Epsin-1 (Ent1 or Ent1p) and Epsin-2 (Ent2 or Ent2p), and similar proteins. Yeast single epsin knockouts, either Ent1 and Ent2, are viable while the double knockout is not. Yeast epsins are required for endocytosis and localization of actin. Ent2 also plays a signaling role during cell division. The ENTH domain of Ent2 interacts with the septin organizing, Cdc42 GTPase activating protein, Bem3, leading to increased cytokinesis failure when overexpressed. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding
GYSSTQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLNDKGKNWRHVAKALTVLDYLL
HFGSENVVLWAKENIYIIKTLREFQYIDDEGKDQGQNVRVKAKELTSLLLDDERLREERSMR
>gnl|CDD|340789 cd16992, ENTH_Ent3, Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins. This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-3 (Ent3 or Ent3p), and similar proteins. Ent3 is an adaptor proteins at the Trans-Golgi Network (TGN); it cooperates with yeast SNARE Vti1p to regulate transport from the TGN to the prevacuolar endosome. Ent3 facilitates the interaction between Gga2p with both the endosomal syntaxin Pep12p and clathrin in the GGA-dependent transport to the late endosome. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. Similar to mammalian epsinR, The ENTH domain of Ent3 binds to the yeast SNARE Vti1p; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding
MESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEKAGSEWRQIYKALQLLEYLIKNG
SERVVDDARGHLTLIKMLRSFHYIDDKGKDQGINVRNRAKELIELLSDDEK
>gnl|CDD|340790 cd16993, ENTH_Ent5, Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins. This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-5 (Ent5 or Ent5p), and similar proteins. Ent5 is required, together with Ent3 and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. It is also required for protein transport from the Trans-Golgi Network (TGN) to the vacuole. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding
YQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLYLMTEYTLKRLVDHIATRPKNLYEKARKDYVNYGSEW
RVVLKCLIVIEFLLLNVDTGDELNQVLSCLLNHKHIFTREIAQYKVKFSNDGKMEIHERGIQKKCELILQ
LIEDSDFLRQERAKNKKN
>gnl|CDD|340791 cd16994, ENTH_Ent4, Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins. Yeast Epsin-4 (Ent4 or Ent4p) has been reported to be involved in the Trans-Golgi Network (TGN)-to-vacuole sorting of Arn1p, a transporter for the uptake of ferrichrome, an important nutritional source of iron. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding
TELKVKQATDDNETSGATGTLMNEISVLTYSPKTLKEITQVLKKRLSGNSKKSSHKNCVHILKTLTLISY
LINNGSNEFIAWLRSNLYLIERLKDFEVQDNRDLPMANQIRSLSQDICELINDDEL
>gnl|CDD|340792 cd16995, VHS_Tom1, VHS (Vps27/Hrs/STAM) domain of Target of Myb protein 1. Tom1 (Target of myb1 - retroviral oncogene) is a novel negative regulator of interleukin-1 and tumor necrosis factor-induced signaling pathways. It also plays important roles in protein-degradation systems in Alzheimer's disease pathogenesis. Tom1 contains VHS and GAT domains in the N-terminal and central region, respectively. The VHS domain has a superhelical structure similar to the structure of the ARM repeats and is present at the very N-termini of proteins. It is a right-handed superhelix of eight alpha helices. The VHS domain has been found in a number of proteins, some of which have been implicated in intracellular trafficking and sorting. The VHS domain of Tom1 is essential for its function as a negative regulator
PVGQRIEKATDGSLQSEDWGLNMEICDIINETEEGPKDAIRAIKKRIVGNKNFREVMLALTVLETCVKNC
GHRFHVLVASQDFVEGVLVKTILPKNNPPAIVHDKVLNLIQAWADAFRSSPDLTGVVTVYEDLRRKG
>gnl|CDD|340793 cd16996, VHS_Tom1L2, VHS (Vps27/Hrs/STAM) domain of TOM1-like protein 2. TOM1-like protein 2 (Tom1L2) is a member of the Tom1 (Target of myb1) subfamily, characterized by the presence of a VHS (Vps27p/Hrs/Stam) domain in the N-terminal portion followed by a GAT (GGA and Tom) domain. They are novel regulators for post-Golgi trafficking and signaling. Studies in Tom1L2 hypomorphic mice suggest that Tom1L2 may play roles in immune responses and tumor suppression. The VHS domain has a superhelical structure similar to the structure of the ARM repeats and is present at the very N-termini of proteins. It is a right-handed superhelix of eight alpha helices. The VHS domain has been found in a number of proteins, some of which have been implicated in intracellular trafficking and sorting
PVGQCIEKATDGSLQSEDWTLNMEICDIINETEEGPKDAIRALKKRLNGNKNYREVMLALTVLETCVKNC
GHRFHVLVASRDFIDGVLVKIISPKNNPPTIVQDKVLALIQAWADAFRSSPDLTGVVHIYEELKRKG
>gnl|CDD|340794 cd16997, VHS_Tom1L1, VHS (Vps27/Hrs/STAM) domain of TOM1-like protein 1. TOM1-like protein 1 (Tom1L1) is also called Src-activating and signaling molecule protein (Srcasm). It is a member of the Tom1 (Target of myb1) subfamily, characterized by the presence of a VHS (Vps27p/Hrs/Stam) domain in the N-terminal portion followed by a GAT (GGA and Tom) domain. They are novel regulators for post-Golgi trafficking and signaling. Tom1L1 has been implicated in multivesicular body (MVB) formation, viral egress from the cell, and cytokinesis. Its amplification enhances the metastatic progression of ERBB2-positive breast cancers. The VHS domain has a superhelical structure similar to the structure of the ARM repeats and is present at the very N-termini of proteins. It is a right-handed superhelix of eight alpha helices. The VHS domain has been found in a number of proteins, some of which have been implicated in intracellular trafficking and sorting
SVGHLIEKATFGTVQTEDWGQFMHICDIINTTEDGPKDAVKALKKRISKNYNHKEIRLTLSLLDMCMQNC
GPSFQSLVVKKEFVKDVLVKLLNPRYNLPVDLQNKILNFIMTWAQGFQGGVDVSEVKEVYLDLVKKG
>gnl|CDD|340795 cd16998, VHS_GGA_fungi, VHS (Vps27/Hrs/STAM) domain of fungal GGA (Golgi-localized, Gamma-ear-containing, Arf-binding) proteins. GGA (Golgi-localized, Gamma-ear-containing, Arf-binding) comprises a subfamily of ubiquitously expressed, monomeric, motif-binding cargo/clathrin adaptor proteins involved in membrane trafficking between the Trans-Golgi Network (TGN) and endosomes. Yeast GGAs facilitate the specific and direct delivery of vacuolar sorting receptor Vps10p and the processing protease Kex2p from the TGN to the late endosome/prevacuolar compartment (PVC). The VHS domain has a superhelical structure similar to the structure of the ARM (Armadillo) repeats and is present at the N-termini of proteins. GGA proteins have a multidomain structure consisting of an N-terminal VHS domain linked by a short proline-rich linker to a GAT (GGA and TOM) domain, which is followed by a long flexible linker to the C-terminal appendage, GAE (Gamma-Adaptin Ear) domain. The VHS domain of GGA proteins binds to the acidic-cluster dileucine (DxxLL) motif found on the cytoplasmic tails of cargo proteins trafficked between the Trans-Golgi Network and the endosomal system
LQRYIERACDPSLEEPNLALNLEIADLINEKQGNTPREAAFAIVRLVNSRNPTVALLALHLLDVCVKNCG
YPFHLQIASKEFLNELVRRFPERPPSRLNPVQHKILELIEEWKQTLCKTSRYKEDLGHIRDMHRLLSYK
>gnl|CDD|340796 cd16999, VHS_STAM2, VHS (Vps27/Hrs/STAM) domain of Signal Transducing Adapter Molecule 2. Signal Transducing Adapter Molecule 2 (STAM2) is also called EAST (EGFR-Associated protein with SH3 and TAM domain) and Hbp (Hrs-binding protein). It is highly expressed in neurons, where it is localized in the nucleus. STAM (Signal Transducing Adaptor Molecule) subfamily members have at their N-termini a VHS domain, which is involved in cytokine-mediated intracellular signal transduction and has a superhelical structure similar to the structure of ARM (Armadillo) repeats, followed by a Ubiquitin-Interacting Motif (UIM) and a SH3 (Src Homology 3) domain, which is a well-established protein-protein interaction domain, and a GAT (GGA and TOM) domain. At the C-termini of most vertebrate STAMS, an Immunoreceptor Tyrosine-based Activation Motif (ITAM) is present, which mediates the binding of HRS (hepatocyte growth factor-regulated tyrosine kinase substrate) in endocytic and exocytic machineries. STAM is a component of the ESCRT (Endosomal Sorting Complex Required for Transport)-0 machinery and together with Hrs, functions to bind and sequester cargoes for downstream sorting into intralumenal vesicles
FEQDVEKATNEYNTSEDWSLIMDICDKVGSTPNGAKDCLKAIMKRVNHKVPHVALQALTLLGACVSNCGK
IFHLEVCSRDFATEVRAVIKNKAHPKVCEKLKALMVEWSEEFQKDPQFSLISATIKSLKEEGITFPPAG
>gnl|CDD|340797 cd17000, VHS_STAM1, VHS (Vps27/Hrs/STAM) domain of Signal Transducing Adapter Molecule 1. Signal Transducing Adapter Molecule 1 (STAM1) is part of a crucial regulatory axis for the ventral axonal trajectory of developing spinal motor neurons. It forms a complex with beta-arrestin, which regulates lysosomal trafficking of the chemokine receptor CXCR4 and also mediates CXCR4-dependent chemotaxis. STAM (Signal Transducing Adaptor Molecule) subfamily members have at their N-termini a VHS domain, which is involved in cytokine-mediated intracellular signal transduction and has a superhelical structure similar to the structure of ARM (Armadillo) repeats, followed by a Ubiquitin-Interacting Motif (UIM) and a SH3 (Src Homology 3) domain, which is a well-established protein-protein interaction domain, and a GAT (GGA and TOM) domain. At the C-termini of most vertebrate STAMS, an Immunoreceptor Tyrosine-based Activation Motif (ITAM) is present, which mediates the binding of HRS (hepatocyte growth factor-regulated tyrosine kinase substrate) in endocytic and exocytic machineries. STAM is a component of the ESCRT (Endosomal Sorting Complex Required for Transport)-0 machinery and together with Hrs, functions to bind and sequester cargoes for downstream sorting into intralumenal vesicles
FDQDVEKATSEMNTAEDWGLILDICDKVGQSRTGPKDCLRSIMRRVNHKDPHVAMQALTLLGACVSNCGK
IFHLEVCSRDFASEVSNVLNKGHPKVCEKLKALMVEWTEEFKNDPQLSLISAMIKNLKEQG
>gnl|CDD|340798 cd17001, CID_RPRD2, CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 2. Regulation of nuclear pre-mRNA domain-containing protein 2 (RPRD2) is a CID (CTD-Interacting Domain) domain containing protein that co-purifies with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices
ALESSLDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRK
NAIVFRESFAEVLPEAAALVKDASVSKSVERIFKIWEERNVYPEETIAALKEALS
>gnl|CDD|340799 cd17002, CID_RPRD1, CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 1 and similar proteins. This subfamily contains Regulation of nuclear pre-mRNA domain-containing proteins 1A (RPRD1A) and 1B (RPRD1B) from jawed vertebrates, CID domain-containing protein 1 (CIDS1 or cids-1) from Caenorhabditis elegans, and similar proteins. RPRD1A and RPRD1B are CID (CTD-Interacting Domain) containing proteins that co-purify with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. RPRD1A and RPRD1B form homodimers and heterodimers through their coiled-coil domains. Both associate directly with RPAP2 phosphatase and serve as CTD scaffolds to coordinate the dephosphorylation of phospho-S5 by RPAP2. The function of CIDS1 is not yet known. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices
FSEAALEKKLAELSNSQQSIQTLSLWLIHHRKHAKTIVRVWLKELRKEKPSKKLTLLYLANDVIQNSRKK
GPEFTKEFAPVLEDAFKHVAKLTDSEVLKALERILNIWKERQVYEKDFIEQLRAALRK
>gnl|CDD|340800 cd17003, CID_Rtt103, CID (CTD-Interacting Domain) of yeast transcription termination factor Rtt103 and similar proteins. Yeast transcription termination factor Rtt103 is a CID (CTD-Interacting Domain) containing protein that functions in DNA damage response. It associates with sites of DNA breaks and is essential for recovery from DNA double strand breaks in the chromosome. CID binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase (Pol) II (RNAP II). Rtt103 CID preferentially interacts with CTD phosphorylated at Ser2. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices
EEQFISKLNALNETQESIVSISQWVLFHYRHADEIAEIWSDYLLKSSVNSRRKLLLIYLANDVVQQAKAK
KKTEFIDAFSKVLPEVLEKIYPSLPSDIKKKIKRVVNVWKQRQIFSKDVIDDIEERL
>gnl|CDD|340801 cd17004, CID_SCAF8, CID (CTD-Interacting Domain) of SR-related and CTD-associated factor 8. SR-related and CTD-associated factor 8 (SCAF8) is also called CDC5L complex-associated protein 7 (CCAP7) or RNA-binding motif protein 16 (RBM16). It may play a role in mRNA processing. SCAF8 contains a CTD-interacting domain (CID) at the amino terminus and a Ser/Arg-rich domain followed by an RNA recognition motif. CID binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase (Pol) II (RNAP II). During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices
KTFNSELYSLNDYKPPISKAKMTQITKAAIKAIKFYKHVVQSVEKFIQKCKPEYKVPGLYVIDSIVRQSR
HQFGQEKDVFAPRFSNNIISTFQNLYRCPGDDKSKIVRVLNLWQKNNVFKSEIIQPLLDMA
>gnl|CDD|340802 cd17005, CID_SFRS15_SCAF4, CID (CTD-Interacting Domain) of Splicing factor arginine serine rich 15. Splicing factor arginine serine rich 15 (SFRS15) is also called CTD-binding SR-like protein RA4 or SR-related and CTD-associated factor 4 (SCAF4). It may act to physically and functionally link transcription and pre-mRNA processing. SFRS15/SCAF4 contains a CTD-interacting domain (CID) at the amino terminus and a Ser/Arg-rich domain followed by an RNA recognition motif. CID binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase (Pol) II (RNAP II). During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices
NAFNQELFSLMDMKPPISRAKMILITKAAIKAIKLYKHVVQIVEKFIKKCKPEYKVPGLYVIDSIVRQSR
HQFGADKDVFGPRFSKNITATFQYLYLCPSEDKSKIVRVLNLWQKNGVFKIEIIQPLLDMA
>gnl|CDD|340803 cd17006, ANTH_N_HIP1_like, ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins. This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins
QAISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPS
VLRDSQRYRSRLKELGKLWGHLKDGYGKLIAQYCKLLITKLEFH
>gnl|CDD|340804 cd17007, ANTH_N_Sla2p, ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins. This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domains f Sla2p and similar proteins
LQVAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPS
ALKEAIRNIEWLESLGRQSSGSGAKGYGRLIKEYVRYLLDKLAFH
>gnl|CDD|340805 cd17008, VHS_GGA3, VHS (Vps27/Hrs/STAM) domain of ADP-ribosylation factor-binding protein GGA3. ADP-ribosylation factor-binding protein GGA3 (Golgi-localized, Gamma-ear-containing, Arf-binding 3) regulates the trafficking and is required for the lysosomal degradation of BACE (beta-site APP-cleaving enzyme), the protease that initiates the production of beta-amyloid, which causes Alzheimer's disease. It also plays a key role in GABA (+) transmission, which is important in the regulation of anxiety-like behaviors. GGA3 is a member of the GGA subfamily, which is comprised of ubiquitously expressed, monomeric, motif-binding cargo/clathrin adaptor proteins involved in membrane trafficking between the Trans-Golgi Network (TGN) and endosomes. The VHS domain has a superhelical structure similar to the structure of the ARM (Armadillo) repeats and is present at the N-termini of proteins. GGA proteins have a multidomain structure consisting of an N-terminal VHS domain linked by a short proline-rich linker to a GAT (GGA and TOM) domain, which is followed by a long flexible linker to the C-terminal appendage, GAE (Gamma-Adaptin Ear) domain. The VHS domain of GGA proteins binds to the acidic-cluster dileucine (DxxLL) motif found on the cytoplasmic tails of cargo proteins trafficked between the Trans-Golgi Network and the endosomal system
GESLESWLNKATNPSNRQEDWEYIIGFCDQINKELEGPQIAVRLLAHKIQSPQEWEALQALTVLEACMKN
CGRRFHNEVGKFRFLNELIKVVSPKYLGDRVSEKVKTKVIELLYSWTVALPEEAKIKDAYHMLKRQGIVQ
S
>gnl|CDD|340806 cd17009, VHS_GGA1, VHS (Vps27/Hrs/STAM) domain of ADP-ribosylation factor-binding protein GGA1. ADP-ribosylation factor-binding protein GGA1 (Golgi-localized, Gamma-ear-containing, Arf-binding 1) is also called Gamma-adaptin-related protein 1. It is expressed in human brain and affects the generation of amyloid beta-peptide, and may be involved in the pathogenesis of Alzheimer disease. It is a member of the GGA subfamily, which is comprised of ubiquitously expressed, monomeric, motif-binding cargo/clathrin adaptor proteins involved in membrane trafficking between the Trans-Golgi Network (TGN) and endosomes. The VHS domain has a superhelical structure similar to the structure of the ARM (Armadillo) repeats and is present at the N-termini of proteins. GGA proteins have a multidomain structure consisting of an N-terminal VHS domain linked by a short proline-rich linker to a GAT (GGA and TOM) domain, which is followed by a long flexible linker to the C-terminal appendage, GAE (Gamma-Adaptin Ear) domain. The VHS domain of GGA proteins binds to the acidic-cluster dileucine (DxxLL) motif found on the cytoplasmic tails of cargo proteins trafficked between the Trans-Golgi Network and the endosomal system
TLEARINRATNPLNKELDWASINGFCEQLNEEFEGPPLATRLLAHKIQSPQEWEAIQALTVLETCMKSCG
KRFHDEVGKFRFLNELIKVVSPKYLGSRTPEKVKNKILELLYSWTVGLPEEVKIAEAYQMLKKQGIVKS
>gnl|CDD|340807 cd17010, VHS_GGA2, VHS (Vps27/Hrs/STAM) domain of ADP-ribosylation factor-binding protein GGA2. ADP-ribosylation factor-binding protein GGA2 (Golgi-localized, Gamma-ear-containing, Arf-binding 2) is also called Gamma-adaptin-related protein 2 and VHS domain and ear domain of gamma-adaptin (Vear). It is a member of the GGA subfamily, which is comprised of ubiquitously expressed, monomeric, motif-binding cargo/clathrin adaptor proteins involved in membrane trafficking between the Trans-Golgi Network (TGN) and endosomes. The VHS domain has a superhelical structure similar to the structure of the ARM (Armadillo) repeats and is present at the N-termini of proteins. GGA proteins have a multidomain structure consisting of an N-terminal VHS domain linked by a short proline-rich linker to a GAT (GGA and TOM) domain, which is followed by a long flexible linker to the C-terminal appendage, GAE (Gamma-Adaptin Ear) domain. The VHS domain of GGA proteins binds to the acidic-cluster dileucine (DxxLL) motif found on the cytoplasmic tails of cargo proteins trafficked between the Trans-Golgi Network and the endosomal system
SLESWLNKATDPSNSEEDWECIQGFCEQVNKEPEGPQIATRLLAHKIQSPQEREALHALTVLEMCMNNCG
ERFHSEVAKFRFLNELIKVLSPKYLGTWSSEKVKSRVIEVLFSWTVWLPEEVKIRDAYQMLKKQGIIKQ
>gnl|CDD|340808 cd17011, CID_RPRD1A, CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 1A. Regulation of nuclear pre-mRNA domain-containing protein 1A (RPRD1A) is also called Cyclin-dependent kinase inhibitor 2B-related protein or p15INK4B-related protein (P15RS). RPRD1A is a CID (CTD-Interacting Domain) containing protein that co-purifies with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. RPRD1A form homodimers and heterodimers with RPRD1B through their coiled-coil domains. Both RPRD1A and RPRD1B associate directly with RPAP2 phosphatase and serve as CTD scaffolds to coordinate the dephosphorylation of phospho-S5 by RPAP2. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices
FSEAALEKKLSELSNSQQSVQTLSLWLIHHRKHSRPIVTVWERELRKAKPNRKLTFLYLANDVIQNSKRK
GPEFTKDFAPVIVEAFKHVSSETDESCKKHLGRVLSIWEERSVYENDVLEQLKQALYG
>gnl|CDD|340809 cd17012, CID_RPRD1B, CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 1B. Regulation of nuclear pre-mRNA domain-containing protein 1B (RPRD1B) is also called Cell cycle-related and expression-elevated protein in tumor (CREPT). RPRD1B is a CID (CTD-Interacting Domain) containing protein that co-purifies with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. RPRD1B form homodimers and heterodimers with RPRD1A through their coiled-coil domains. Both RPRD1A and RPRD1B associate directly with RPAP2 phosphatase and serve as CTD scaffolds to coordinate the dephosphorylation of phospho-S5 by RPAP2. RPRD1B is highly expressed during tumorigenesis and in endometrial cancer, has been shown to promote tumor growth by accelerating the cell cycle. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices
SFSESALEKKLSELSNSQQSVQTLSLWLIHHRKHAGPIVSVWHRELRKAKSSRKLTFLYLANDVIQNSKR
KGPEFTREFESVLVDAFSHVAREADEGCKKPLERLLNIWQERSVYGGDFIQQLKLSIED
>gnl|CDD|340810 cd17013, ANTH_N_HIP1, ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1. Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1
QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPN
VLKDSLRYKNELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH
>gnl|CDD|340811 cd17014, ANTH_N_HIP1R, ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1-related protein. Huntingtin-interacting protein 1-related protein (HIP1R), also called HIP12, promotes clathrin assembly in vitro. It is an endocytic protein involved in receptor trafficking, including regulating cell surface expression of receptor tyrosine kinases. Low HIP1R protein expression is associated with worse survival in diffuse large B-cell lymphoma (DLBCL) patients; it is preferentially expressed in germinal center B-cell (GCB)-like DLBCL, and may be potentially useful in subtyping DLBCL cases. HIP1R contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1R was found to preferentially bind PtdIns(3,5)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1-related protein
QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPN
VLQDCQRYRSNIRETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH
>gnl|CDD|341097 cd17015, ING_plant, Inhibitor of growth (ING) domain of plant inhibitor of growth proteins. This subfamily is composed of mainly plant inhibitor of growth proteins such as Arabidopsis thaliana ING1 (AtING1 or PHD finger protein ING1) and ING2 (AtING2 or PHD finger protein ING2). They are histone-binding components that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes. The related mammalian ING proteins act as readers and writers of the histone epigenetic code, affecting DNA damage response, chromatin remodeling, cellular senescence, differentiation, cell cycle regulation, and apoptosis. They may have a general role in mediating the cellular response to genotoxic stress through binding to and regulating the activities of histone acetyltransferase (HAT) and histone deacetylase (HDAC) chromatin remodeling complexes. All ING proteins contain an N-terminal leucine zipper-like (LZL) motif-containing ING domain that binds unmodified H3 tails, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain, which binds lysine 4-tri-methylated histone H3 (H3K4me3). Although these two regions can bind histones independently, together they increase the apparent association of the ING domain for the H3 tail
VASLPAELQRNLSLIRDLDERSQALQDQVEQKCERCLEEPSQSSESASSSDDTAAAALREEIESAQKDCL
QLADEKVALAQQAYDLVDGHIQRLDKDL
>gnl|CDD|341098 cd17016, ING_Pho23p_like, Inhibitor of growth (ING) domain of yeast Pho23p and similar proteins. This family is composed of Saccharomyces cerevisiae transcriptional regulatory protein PHO23 (Pho23p), Schizosaccharomyces pombe chromatin modification-related protein png2 (also called ING1 homolog 2), and similar proteins. Pho23p is part of Rpd3/Sin3 histone deacetylase (HDAC) complex. It is required for the normal function of Rpd3 in the silencing of rDNA, telomeric, and mating-type loci. Pho23p inhibits p53-dependent transcription. The related mammalian ING proteins act as readers and writers of the histone epigenetic code, affecting DNA damage response, chromatin remodeling, cellular senescence, differentiation, cell cycle regulation and apoptosis. They may have a general role in mediating the cellular response to genotoxic stress through binding to and regulating the activities of histone acetyltransferase (HAT) and histone deacetylase (HDAC) chromatin remodeling complexes. All ING proteins contain an N-terminal leucine zipper-like (LZL) motif-containing ING domain that binds unmodified H3 tails, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain, binding with lysine 4-tri-methylated histone H3 (H3K4me3). Although these two regions can bind histones independently, together they increase the apparent association of the ING for the H3 tail
IEALPLEVMRYFTLLKEVDAKCRNPEPELNDLIDEFLKNPVEEQDKLERRELLSRLRKKLQEILPSLDEK
MHVASDANDNLDKQLKRID
>gnl|CDD|341099 cd17017, ING_Yng1p, Inhibitor of growth (ING) domain of yeast Yng1p and similar proteins. The ING family includes three yeast orthologs, chromatin modification-related protein YNG1 (Yng1p), YNG2 (Yng2p), and transcriptional regulatory protein PHO23 (Pho23p). Yng1p, also termed ING1 homolog 1, is one of the components of the NuA3 histone acetyltransferase (HAT) complex. Yng2p, also termed ESA1-associated factor 4, or ING1 homolog 2, is a subunit of the NuA4 HAT complex. It plays acritical role in intra-S-phase DNA damage response. Pho23p is part of Rpd3/Sin3 histone deacetylase (HDAC) complex. It is required for the normal function of Rpd3 in the silencing of rDNA, telomeric, and mating-type loci. Yng1p and Pho23p inhibit p53-dependent transcription. In contrast, Yng2p has the opposite effect. The related mammalian ING proteins act as readers and writers of the histone epigenetic code, affecting DNA damage response, chromatin remodeling, cellular senescence, differentiation, cell cycle regulation and apoptosis. They may have a general role in mediating the cellular response to genotoxic stress through binding to and regulating the activities of histone acetyltransferase (HAT) and histone deacetylase (HDAC) chromatin remodeling complexes. All ING proteins contain an N-terminal leucine zipper-like (LZL) motif-containing ING domain that binds unmodified H3 tails, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain, binding with lysine 4-tri-methylated histone H3 (H3K4me3). Although these two regions can bind histones independently, together they increase the apparent association of the ING for the H3 tail
TEHLPSDILRSLQLIQELDKKSDDHINELDELATTYSTLPKLTPKESHDEVELRRNISRALDDAEHARRM
AKAEAERLDETVKRHHSRIEAIKQKLKAVP
>gnl|CDD|409302 cd17018, T3SC_IA_ExsC-like, Class IA type III secretion system chaperone protein, similar to Pseudomonas aeruginosa exoenzyme S synthesis protein C (ExsC). This family includes type III secretion system (T3SS) chaperone proteins similar to Pseudomonas aeruginosa and Aeromonas hydrophila ExsC (also known as exoenzyme S synthesis protein C). P. aeruginosa ExsC, a member of the type IA family of T3SS chaperones, is unique because, as part of the signaling process, it binds small secreted protein ExsE as well as the non-secreted anti-activator protein ExsD; it relieves repression of the transcriptional activator ExsA (which activates expression of T3SS genes) by ExsD. However, in Aeromonas, although ExsA is likely the master regulator of the T3SS, there is little evidence of ExsC and ExsE involvement in the regulation of the T3SS
NEILDEFGTLLGLTGLALDDEGVAALAFDDKLKVAFILLEEEEELVLVAYIAPLPEVDEGLLRQLLKFNY
HWSETGGGTFGIDEETGQLCLSLLIDLPSLDLAEFEEILAELLGAAEFWRELLQSHV
>gnl|CDD|409303 cd17019, T3SC_IA_ShcA-like, Class IA type III secretion system chaperone protein, similar to Pseudomonas syringae chaperone protein ShcA. This family includes type III secretion system (T3SS) chaperone proteins similar to Pseudomonas syringae ShcA and similar proteins. In P. syringae, which is a plant pathogen that can infect a wide range of species, the T3SS allows injection of the effector HopA1 (previously known as HopPsyA or HrmA), a protein that has unknown functions in the host cell but possesses close homologs that trigger the plant hypersensitive response in resistant strains. Chaperone ShcA binding to Hop1A shows that interactions in animal pathogens are preserved in the Gram-negative pathogens of plants
YDRLLAEFASQLGIPPLSFDEDGLCQLLIDEDLAIALRRDEAERLTLIGELDDPLPDALDDDLLRLLLEA
ALNPLRGDGPGIGWHPESGGLIAYRHLPLTKLSAERLSEELGEFIEWMKHWR
>gnl|CDD|409304 cd17020, T3SC_IA_ShcM-like, Class IA type III secretion system chaperone protein, similar to Pseudomonas syringae chaperone protein ShcM. This family includes type III secretion system (T3SS) chaperone proteins similar to Pseudomonas syringae ShcM and similar proteins. In P. syringae, which is a plant pathogen that can infect a wide range of species, the T3SS allows injection of the effector protein HopPtoM (previously known as CEL ORF3), among known plant pathogen effectors, that makes a major contribution to the elicitation of lesion symptoms but not growth in host tomato leaves. Chaperone ShcM is required for efficient translocation and function of HopPtoM in the plant cell, consistent with the presence of customized chaperones in plant pathogenic bacteria
FRQLIDELCELAGLPDPEALAEGGPLTVDGVDFSLIHDEEDDPDALLVYCDFGPLPAEDRAAVLRRLLEL
NLLLFGGGGPVFSLNPETGHVVLSVRLPLDDLTAEDLLDLLARLAAQAKEWR
>gnl|CDD|409305 cd17021, T3SC_IA_SicP-like, Class IA type III secretion system chaperone protein, similar to Salmonella enterica chaperone protein SicP. This family includes type III secretion system (T3SS) chaperone proteins similar to Salmonella enterica SicP and similar proteins. In S. enterica, many of its serovars being serious human pathogens, the T3SS allows injection of the effector SptP, a virulence protein that is involved in bacterial invasion into a host cell. Chaperone SicP forms a complex with SptP at an early stage of the effector protein secretion process in order to avoid premature degradation; also, the complex is dissociated at a late stage to secrete only SptP with the help of the ATPase InvC which is part of the related T3SS injectisome
HEKILAELGQKLGIPLLLDENGQCTLLLDDGLFISIRANDDRWYLYAMLATLPDGDDNALWKKILELNLS
LAETGGGVLGYSESADALLYLLRIPVPLNLDALEAQLERFVNQVEALRQEL
>gnl|CDD|409306 cd17022, T3SC_IA_SigE-like, Class IA type III secretion system chaperone protein, similar to Salmonella enterica SigE. This family includes type III secretion system (T3SS) chaperone proteins similar to Salmonella enterica chaperone SigE and similar proteins. In S. enterica, many of its serovars being serious human pathogens, the T3SS allows injection of the effector SigD (also known as SopB) which is an inositol phosphatase. Chaperone SigE binds to SigD, which, upon translocation into the host cell, preferentially dephosphorylates specific inositol phospholipids that are thought to be crucial for subsequent activation of the host cell Ser-Thr kinase Akt
MENLLLTLYDALGLEVIDEEDPCLVIDDDLPVYFEESGDSLEIICPLYPLPQDKDTLQQLLELNYSSKVI
LSTDAENTLLLALLRLPDESEYEELEAQLELFISKVRELKQQL
>gnl|CDD|409307 cd17023, T3SC_IA_CesT-like, Class IA type III secretion system chaperone protein, similar to Escherichia coli CesT. This family includes type III secretion system (T3SS) chaperone proteins similar to Escherichia coli CesT and also contains Stm2138, a novel virulence chaperone in Salmonella enterica subsp. enterica serovar Typhimurium. In E. coli, the T3SS allows injection of the effector Tir (translocated intimin receptor), which plays a key role in enterohemorrhagic Escherichia coli (EHEC) infection, attaching and effacing (A/E) lesions, and intracellular signal transduction. CesT binds to Tir, which interacts with intimin and anchors the infected cell membrane inside the host cytoplasm for signaling
SRSELLLKQFGEKIGIRSISFDENRLCSFAIDNDYYIILNDVNDEYLMIYGVCGKFPTDNSNLAFELLNA
NLWFAENNGPYLCYEPGAQSLLLALRFPLDEATPEKLENEIEVVLKSMENLYLILQEKGITLD
>gnl|CDD|409308 cd17024, T3SC_IA_DspF-like, Class IA type III secretion system chaperone protein, similar to Erwinia amylovora DspF (DspF/AvrF family protein). This family includes type III secretion system (T3SS) chaperone proteins similar to Erwinia amylovora DspF, Pantoea stewartii WtsE, Pseudomonas viridiflava AvrF, and similar proteins, all of which bind AvrE family type III effector proteins. In E. amylovora, a gram-negative enterobacterium that causes a devastating blight disease of apple and pear trees, the T3SS allows injection of effector DspE via the chaperone DspF. DspE has been shown to interact with several apple proteins, suppress salicylic acid-mediated host defenses and cause necrotic cell death in host and non-host plants. In Pectobacterium carotovorum, DspE is required early in solanum tuberosum leaf infection to cause cell death. Effector WtsE in P. stewartii causes disease-associated cell death in corn and requires the chaperone protein WtsF for stability
IEQLLAELGQRLGLDLSLDNGACALTDNDGEEWVLEVPDDSDLLLLHTPLGRLPDVRAEDLSKLLELNFE
PDLMRGAWLALDEGTRSLRLCAQLPLESLDAGLLENLLTNFIELRKELRER
>gnl|CDD|409309 cd17025, T3SC_IA_ShcF-like, Class IA type III secretion system chaperone protein, similar to Pseudomonas syringae ShcF. This family includes type III secretion system (T3SS) chaperone proteins similar to Pseudomonas syringae ShcF and similar proteins. In P. syringae, which is a plant pathogen that can infect a wide range of species, the T3SS allows injection of the effector protein AvrPphF into genetically susceptible host cells. Chaperone ShcF (originally known as AvrPphF ORD1) binds AvrPphF in a similar manner to type III chaperones from bacterial pathogens of animals, indicating structural conservation of these specialized chaperones, despite high sequence divergence
EFHRLIRPLLKQYGIPAPELEDNEVYELTFDDGLSIHLLGNPRGYLTLSCLLGVPDERSDEELLLELLQA
NLFSLEHPPIIIGLDAEQDKLVLWTRQPLAELDEAELIELFERFVDKAEALKRW
>gnl|CDD|409310 cd17026, T3SC_IA_SpcU-like, Class IA type III secretion system chaperone protein, similar to Pseudomonas aeruginosa SpcU. This family includes type III secretion system (T3SS) chaperone proteins similar to Pseudomonas aeruginosa SpcU and similar proteins. In P. aeruginosa, a multidrug resistant pathogen associated with serious illnesses such as ventilator-associated pneumonia and various sepsis syndromes, the T3SS allows injection of effector protein ExoU, one of the most aggressive toxins injected by a T3SS, into the cytosol of target eukaryotic cells, leading to rapid cell necrosis. Chaperone SpcU binds the cytotoxin ExoU, which is a broad-specificity phospholipase A2 (PLA2) and lysophospholipase, and maintains the N-terminus of ExoU in an unfolded state which is required for secretion
MLDEWLAQWGLSLPASNDETLRLQSADGPELVLERLQGGWLLAVRLGPVPSKLLLGVVLQLLQANSPFSA
LAPVRLAADGAGDLVLWLELRDGADDVDALNSACDKLREGHARLSPLLEP
>gnl|CDD|409311 cd17027, T3SC_IA_YscB_AscB-like, Class IA type III secretion system chaperone protein, similar to Yersinia pestis YscB. This family includes type III secretion system (T3SS) chaperone proteins similar to Yersinia pestis YscB and its homologs, Aeromonas hydrophila AscB and Photorhabdus luminescens LscB. In Yersinia pestis, which causes the deadly bubonic plague, the T3SS allows injection of effector proteins, termed Yersinia outer proteins (Yops) into macrophages and other immune cells, forming pores in the host cell membrane. The secretion of Yops is regulated by the activity of the YopN/SycN/YscB/TyeA complex. YscB acts, along with SycN, as a chaperone for YopN, a key part of a complex that regulates type III secretion so that it responds to contact with the eukaryotic target cell
LDNLLASLAARLGIGPLVADQDGRYTLRFDGRLEVRLFQAGGWLLLEAQLAALPTDDGQREELLKKLLQK
ALALLRTQRSSLSLDPDEDALLLYRRLALEGLSPDDFEEALEEFLNALERWREELGQ
>gnl|CDD|409312 cd17028, T3SC_IA_SycE_Scc1-like, Class IA type III secretion system chaperone protein, similar to Chlamydia SycE/Scc1. This family includes type III secretion system (T3SS) chaperone proteins similar to Chlamydia SycE (also known as Scc1) and similar proteins. Chlamydia SycE is homologous to that of the SycE chaperone protein of Yersinia, which is involved in promoting translocation of Yersinia outer protein E (YopE). In Chlamydia, two T3SS chaperones, Scc1 and Scc4, work together to promote secretion of the important effector and plug protein, CopN, whereas, the Scc3 chaperone represses its secretion
DQFESLLKDLGELLNIPLHPDKNNACVILFDEEVTIQLELDKTEEFLLIGTKLGELPPGRFRENVFREAL
KANGLPYPRKGIFAYSEKSNQLILFDYLPLNTLNGEKLAEILGLFSEKAKAWKEALESGEVPPL
>gnl|CDD|409313 cd17029, T3SC_IA_SycE_SpcS-like, Class IA type III secretion system chaperone protein, similar to Yersinia SycE. This family includes type III secretion system (T3SS) chaperone proteins similar to Yersinia SycE and its homolog Pseudomonas aeruginosa SpcS. Involvement of Yersinia chaperone SycE (also known as YerA) in promoting translocation of Yersinia outer protein E (YopE), a selective activator of mammalian Rho-family GTPases, into host macrophages is essential to Yersinia pathogenesis. In P. aeruginosa, which is an opportunistic pathogen that harbors multiple virulence factors that widely manipulate host cell signaling and immune response, the effector toxin proteins of T3SS are ExoT, ExoS, ExoU and ExoY. Chaperone SpcS (formerly known as Orf1) binds to ExoT as well as its homolog, ExoS, both known to be the actual virulence determinants due to the presence of bifunctional GTPase-activating (GAP) and ADP-ribosyltransferase (ADPRT) domains which are essential for inhibition of bacterial internalization and epithelial cell migration by altering the actin cytoskeleton
FEAAITLLFQKLGLPAPENIEGVFSLKVGEFAIHITEYPVGHLLMFSLLDNEDSDEIETLLQQNLFSDDL
LKPVLAWDEDGGHWVLWNRQPLNSLDENSLYHQLEDLVQGAEQLQ
>gnl|CDD|409314 cd17030, T3SC_IA_SycH-like, Class IA type III secretion system chaperone protein, similar to Yersinia pestis SycH. This family includes type III secretion system (T3SS) chaperone proteins similar to Yersinia pestis SycH and similar proteins. In Yersinia pestis, the causative agent of bubonic and pneumonic plague, the T3SS allows injection of effector proteins, termed Yersinia outer proteins (Yops) into macrophages and other immune cells, forming pores in the host cell membrane and have been linked to cytolysis. The secretion of Yops is regulated by the activity of the YopN/SycN/YscB/TyeA complex. SycH is the chaperone for YopH, a potent eukaryotic-like protein tyrosine phosphatase that is essential for virulence. SycH also binds two negative regulators of type III secretion, YscM1 and YscM2, both sharing significant sequence homology with the chaperone-binding domain of YopH
MERFKAVLEELATLLGLELTETDEGIASLTIDGRWVVHLAPLGEEQLVLFMRAGPLTGEQQAVTLLQQNL
FSPNPGMPRVGLDQDNHLILWSQHSINETDGTALYQALTSLLDKAVTLSS
>gnl|CDD|409315 cd17031, T3SC_IA_SycN-like, Class IA type III secretion system chaperone protein, similar to Yersinia pestis SycN. This family includes type III secretion system (T3SS) chaperone proteins similar to Yersinia pestis SycN and similar proteins. In Yersinia pestis, the causative agent of bubonic and pneumonic plague, the T3SS allows injection of effector proteins, termed Yersinia outer proteins (Yops) into macrophages and other immune cells, forming pores in the host cell membrane and have been linked to cytolysis. The secretion of Yops is regulated by the activity of the YopN/SycN/YscB/TyeA complex; SycN-YscB forms a heterodimeric secretion chaperone and binds YopN, a key part of a complex that regulates type III secretion, in response to calcium levels, so that secretion occurs only after contact with the targeted eukaryotic cell. Negative regulation is mediated by the complex by blocking the entrance to the secretion apparatus prior to contact with mammalian cells
IDDAIAEFGRSMGVPGLELSGSGIIALEFERGGTLFLERQGDGLLLYLAREIPEHHDAEAAAKALRLCHY
DQSLPFPVQAGLLGDNQLVLLARLDEREVTLPTLEQALQLLTRLHDEV
>gnl|CDD|409316 cd17032, T3SC_IA_SycT-like, Class IA type III secretion system chaperone protein, similar to Yersinia enterocolitica SycT. This family includes type III secretion system (T3SS) chaperone proteins similar to Yersinia enterocolitica SycT and similar proteins. In Y. enterocolitica, a food-borne pathogen causing gastroenteritis and mesenteric lymphadenitis, chaperone SycT promotes translocation of effector YopT (Yersinia outer protein T), a cysteine protease that inactivates the small GTPase RhoA of targeted host cells by cleaving its C-terminal, prenylated cysteine, thereby releasing the GTPase into the host cytosol
TTTFDELLQQLFLKLGLNHQTNEDGIYTLEVDGHIQVLIACYHDQWLQLFSELGSELPTNDNLFGEHWPA
HVQGRLDGKAILWSQQPLAGLDVAELQAWLERFIDDIEQRKEPQNTKEPPN
>gnl|CDD|409317 cd17033, DR1245-like, possible type III secretion system (T3SS) chaperone protein DR1245 found in Deinococcus radiodurans. This family includes a possible type III secretion system (T3SS) chaperone protein DR1245 found in Deinococcus radiodurans, a bacterium that is exceptionally resistant to the lethal effects of ionizing radiation (IR), ultraviolet light and other DNA-damaging agents. DR1245, a protein of unknown function conserved only in the Deinococcaceae, and with strong structural homology to YbjN proteins and T3SS chaperones, may display some chaperone activity towards DdrB, a protein found to be highly up-regulated following irradiation; DR1245 may also bind to other substrates
PLDLLEQYLQALDWDFERDSDGEIALTIPGQWGDYRLLFAWREEDEALQLVCAFDMKVPEARRPEVAELL
NRLNERLWIGHFELDPDDGVVRYRYVLDLPGGELDEEQLENLLGNAVEACERFYPAFQFVVWGGKSPE
>gnl|CDD|409318 cd17034, T3SC_IA_ShcO1-like, Class IA type III secretion system chaperone proteins, similar to Pseudomonas syringae ShcO1, ShcS1, and ShcS2. This family includes type III secretion system (T3SS) chaperone proteins similar to Pseudomonas syringae ShcO1 and similar proteins. In P. syringae, which is a plant pathogen that can infect a wide range of species, the T3SS allows injection of effector Hrp-dependent outer proteins (HOPs) HopO1-1, HopS1, and HopS2. Three homologous chaperones ShcO1, ShcS1, and ShcS2 facilitate the translocation of their cognate effectors HopO1-1, HopS1, and HopS2, respectively. Interestingly, ShcS1 and ShcS2 are capable of substituting for ShcO1 in facilitating HopO1-1 secretion and translocation. ShcS1 and ShcO1 are exceptional class IA T3SS chaperones because they can bind more than one target effector
NLLNEWLKELGSDKGTTLSLDDDGVCTLVAGEGNELLLMLPEDSDELYLYSPLMELPPADDGALLALALA
LNLFQLETRGAAIALDPESNQLVLCYSHELEGLDEQTFGNTLNNFIELASKLR
>gnl|CDD|409319 cd17035, T3SC_IB_Spa15-like, Class IB type III secretion system chaperone protein, similar to Shigella flexneri Spa15. This family includes type III secretion system (T3SS) chaperone proteins similar to Shigella flexneri Spa15, Salmonella enterica InvB, and similar proteins. In S. flexineri, which is a facultative intracellular pathogen that invades the colonic epithelium and causes bacillary dysentery, the T3SS allows injection of a number of effectors to ensure their stabilization prior to secretion. Spa15 is the chaperone for several TTS effectors, including IpaA, IpgB1, OspC3, OspB and OspD1. Effector IpgB that chaperone Spa15 is a mimic of the human Ras-like Rho guanosine triphosphatase RhoG, thus activating Rac1 guanosine triphosphatase and setting off membrane ruffling of the cell, assisting the internalization of Shigella. Also, Spa15 is a chaperone for secreted anti-activator OspD1 which is involved in the control of transcription by the type III secretion apparatus (T3SA) activity in Shigella flexneri
DLAELVREALKELGCDDSIIGDLDNHSTITLDLKDLPSINISTVDDRVWLWSQLPELTENLLSQNAARLL
ELLMEPVEFFRTGQLQLGEGDGGLELKALLNPDALEDEEKFAEALEGFYERLEALSEAL
>gnl|CDD|409320 cd17036, T3SC_YbjN-like_1, T110839 is structurally similar to type III secretion system chaperones and YbjN family proteins. This family includes protein T110839 from Synechococcus elongatus that is structurally similar to type III secretion system (T3SS) chaperones (T3SC) that bind effector proteins, and is homologous to YbjN, a putative sensory transduction regulator protein found in Proteobacteria
TIELIEQYLRSLGIDPELAERDQDGLWSFKRGSAEVFIQVFENPEDDYLQVFSPLMELPAKNIEALYRRL
LELNSTTLGAAFSLSGDQVYLSAERPLEGLDPEEVSAAIDRLAFYADEYDDILKE
>gnl|CDD|409321 cd17037, T3SC_IA_ShcV-like, Class IA type III secretion system chaperone protein, similar to Pseudomonas syringae ShcV. This family includes type III secretion system (T3SS) chaperone protein similar to Pseudomonas syringae ShcV. In P. syringae, which is a plant pathogen that can infect a wide range of species, the T3SS allows injection of effector HopPtoV which may play a subtle role in pathogenesis. Chaperone ShcV facilitates secretion of HopProV into plant cells via the amino-terminal third of the effector
TINELLRYLGRRNGLPWLQLDAENVCGVQTDAGIKITLYVPGASPSLLFLAEIVSLPERPQDDLLLRKLL
TYAFPGLRLRGGALSINPGENSLVLSYEQEIETLTAIRFENLLANFSETAAELRERIQTLK
>gnl|CDD|341208 cd17038, Flavi_M, Flavivirus envelope glycoprotein M. Flaviviruses are small enveloped viruses with a membrane-anchored envelope comprised of 3 proteins called C, M and E. The envelope glycoprotein M is translated as a precursor, called prM. The precursor portion of the protein is the signal peptide for the protein's entry into the membrane. prM is cleaved to form M by the proprotein convertase furin in a late-stage cleavage event. Associated with this cleavage is a change in the infectivity and fusion activity of the virus
SVAIPPHGTGGLTTRKETWLSTSNGKEHLTRVERWVLRNPGYALAAVALAWMLGSSTTQRVIIIVLLLLV
APAYA
>gnl|CDD|340559 cd17039, Ubl_ubiquitin_like, ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins. Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation
ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTLSDYGIKDGSTIHLV
>gnl|CDD|340560 cd17040, Ubl_MoaD_like, ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins. Ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins This family includes ThiS, MoaD, CysO, QbsE, and their homologs, which are structurally homologous to ubiquitin (Ub) and may function as the sulfide donor for the biosynthesis of thiamin, molybdopterin, cysteine, thioquinolobactin, and other sulfur-containing natural products. Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of Ub and the epsilon-amino group of a substrate lysine. Like Ub, small sulfide carrier proteins in this family are adenylated at a diglycyl C-terminus by specific activating proteins. The adenylated C-terminus is subsequently converted to a thiocarboxylate, serving as the sulfide source. Those activating proteins are diverse and show little sequence similarity. This family also includes the small archaeal modifier protein (SAMP), including SAMP1, SAMP2 and SAMP3, which are Ub-like proteins that function as protein modifiers and are required for the production of sulfur-containing biomolecules in the archaeon Haloferax volcanii. SAMP1 and SAMP2 are involved in sulfur transfer during molybdenum cofactor biosynthesis and tRNA thiolation much like MoaD and Urm1, respectively. They can form covalent conjugates with their protein targets through an isopeptide linkage via their C-terminal diglycine motif in a streamlined archaeal E1-dependent pathway. SAMP2 also forms homo-conjugates through the intermolecular isopeptide bond between the C-terminal Gly and the Lys58 side chain, a feature that likely resembles polyubiquitination. SAMP3 conjugates are dependent on the Ub-activating E1 enzyme homolog of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease HvJAMM1
VKVRLFGALREAGAGEEEIEVEGGTTVRDLLDALSERYPGLFEALDEDGELRPFILVFVNGRDVRLDDGL
TPLKDGDEVDILPPVAGG
>gnl|CDD|340561 cd17041, Ubl_WDR48, Ubiquitin-like (Ubl) domain found in WD repeat-containing protein 48 (WDR48) and similar proteins. WDR48, also termed USP1-associated factor 1 (UAF1), or WD repeat endosomal protein, or p80, is required for the histone deubiquitination activity. It stimulates activity of ubiquitin-specific proteases USP1, USP12, and USP46.As potential tumor suppressor, WDR48 in complex with deubiquitinase USP12 suppresses Akt-dependent cell survival signaling by stabilizing PH domain leucine-rich repeat protein phosphatase 1 (PHLPP1). WDR48 also functions as a novel interaction partner of E1 helicase from anogenital human papillomavirus (HPV) types, and plays an essential role in anogenital HPV DNA replication. WDR48 contains a WD40 domain and a ubiquitin-like domain that shows high sequence and structural similarity with RING finger- and WD40-associated ubiquitin-like (RAWUL) domain
EFPKISFFLQPHPSSGLPPKTLKNDKLSASRMLRVRKVMEYVAEKLLGQEPESQDASNPEEKLELLCNDQ
VLDPNMTLATVKHFIWKSGGDLVLHYR
>gnl|CDD|340562 cd17042, Ubl_TmoB, Ubiquitin-like (Ubl) domain found in toluene-4-monooxygenase system protein B (TmoB). TmoB is a component of the multicomponent toluene-4-monooxygenase (T4MO) system that metabolizes toluene as a carbon source. The T4MO complex is composed of a diiron hydroxylase (T4MOH), a Rieske-type ferredoxin (T4MOC), an effector protein (T4MOD), and an NADH oxidoreductase (T4MOF). The T4MOH component consists of TmoA, TmoB, and TmoE. TmoB adopts a beta-grasp ubiquitin-like fold but its precise role remains unclear
LFPLVARFEGDFVVQLVAVDTEDTMDQVAEKVAYHSVGRRVAPRGAPLRVRHHGDEVLPRHMTVAEAGLR
PMDWIDVVF
>gnl|CDD|340563 cd17043, RA, Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon
VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLEEDPEDYSLYEVSEKQETERVLHDDECPLLI
QLEWGPQGTEFRFVLKR
>gnl|CDD|340564 cd17044, Ubl_TBCE, ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins. TBCE, also termed tubulin-specific chaperone E, is a tubulin polymerizing protein involved in the second step of the tubulin folding pathway through cooperating in tubulin heterodimer dissociation both in vivo and in vitro. It may also be implicated in the maintenance of the neuronal microtubule network. Mutations in TBCE gene cause hypoparathyroidism, mental retardation and facial dysmorphism. TBCE contains an N-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain, a leucine-rich repeat protein-protein interaction domain followed by leucine-rich repeat (LRR) domains, and a C-terminal ubiquitin-like (Ubl) domain. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes
SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLS
FYSVEDGDTILVR
>gnl|CDD|340565 cd17045, Ubl_TBCEL, ubiquitin-like (Ubl) domain found in tubulin-specific chaperone cofactor E-like protein (TBCEL) and similar proteins. TBCEL, also termed leucine-rich repeat-containing protein 35 (LRRC35), or E-like (EL), is a novel regulator of tubulin stability, suggesting a link between tubulin turnover and vesicle transport. TBCEL is abundantly expressed in testis, but is also present in several tissues at a much lower level. It is required for the synchronous movement of the investment cones and is important for normal male fertility. TBCEL shows high sequence similarity to tubulin-specific chaperone cofactor E (TBCE), a component of the multimolecular complex required for tubulin heterodimer formation in all eukaryotic cells. It contains a leucine-rich repeat protein-protein interaction domain and a C-terminal ubiquitin-like (Ubl) domain, but does not harbor the cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain found in TBCE
DLTPPKSAKVTVHFEDQVESMDIDLDQTVAELKKQLKNLVGLPPSKMRLYYIDIEMSIFGPEELRFPSRA
LYSYNIRDGDEILVEPK
>gnl|CDD|340566 cd17046, Ubl_IKKA_like, ubiquitin-like (Ubl) domain found in inhibitor of nuclear factor kappa-B kinases, IKK-alpha and IKK-beta, and similar proteins. IKK, also termed IkappaB kinase, is an enzyme complex involved in propagating the cellular response to inflammation. It is part of the upstream nuclear factor kappa-B kinase (NF-kappaB) signal transduction cascade, and plays an important role in regulating the NF-kappaB transcription factor. IKK is composed of three subunits, IKK-alpha/CHUK, IKK-beta/IKBKB, and IKK-gamma/NEMO. The IKK-alpha and IKK-beta subunits together are catalytically active whereas the IKK-gamma subunit serves a regulatory function. IKK-alpha and IKK-beta phosphorylate the IkappaB proteins, marking them for degradation via ubiquitination and allowing NF-kappaB transcription factors to go into the nucleus. IKK-alpha, also known as IKK-A, or IkappaB kinase A (IkBKA), or conserved helix-loop-helix ubiquitous kinase (CHUK), or I-kappa-B kinase 1 (IKK1), or nuclear factor NF-kappa-B inhibitor kinase alpha (NFKBIKA), or transcription factor 16 (TCF-16), belongs to the serine/threonine protein kinase family. In addition to NF-kappaB response, it has many additional cellular targets in an NF-kappaB-independent manner. For instance, it plays a role in epidermal differentiation, as well as in the regulation of the cell cycle protein cyclin D1. IKK-beta, also known as IKK-B, or IkappaB kinase B (IkBKB), or I-kappa-B kinase 2 (IKK2), or nuclear factor NF-kappa-B inhibitor kinase beta (NFKBIKB), belongs to the serine/threonine protein kinase family as well. It interacts with many different protein partners and has been implicated in the treatment of many inflammatory diseases and cancers. Both IKK-alpha and IKK-beta contain an N-terminal catalytic domain followed by a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions
KIVHIFNVTTYRILSYEVTEDTSLSTLQSWIERDTGIPVEDQELLLPTGVSLDPEKPASQCWLVRGEDDY
LVFLF
>gnl|CDD|340567 cd17047, Ubl_UBFD1, ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar proteins. UBFD1, also termed ubiquitin-binding protein homolog (UBPH), is a polyubiquitin binding protein containing a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. It may play a role as nuclear factor-kappaB (NF-kappaB) regulator
VDFKVIWNKEKYDVKFPLDSTIAELKEHIETLTGVPPAMQKLMYKGLLKDDKTLRELKVTKGAKVMVVGS
>gnl|CDD|340568 cd17048, Ubl_UBL3, ubiquitin-like (Ubl) domain found in ubiquitin-like protein 3 (UBL3) and similar proteins. UBL3, also termed membrane-anchored ubiquitin-fold protein (MUB), or protein HCG-1, belongs to a newly described MUB protein family with structural homology with ubiquitin. MUB proteins have a beta-grasp ubiquitin-like (Ubl) domain with longer N- and C-termini and extended loops. The Ubl domain contains a C-terminal CAAX-box, a canonical motif for protein prenylation, which is modified through protein lipidation with a hydrophobic membrane anchor. The lipidation and membrane localization inhibit attachment of MUBs to target proteins
INLRLILVSGKTKEFLFSPNDSAADIAQHVFDNWPEDWEEEQVSSANILRLIYQGRFLHGNVTLGALQLP
LGKTTVMHLVAR
>gnl|CDD|340569 cd17049, Ubl_Sacsin, ubiquitin-like (Ubl) domain found in Sacsin and similar proteins. Sacsin, also termed DnaJ homolog subfamily C member 29 (DNAJC29), is encoded by SACS gene that is highly expressed in the brain. Mutations in SACS can cause the neurodegenerative disease autosomal recessive spastic ataxia of Charlevoix Saguenay (ARSACS) which is characterized by early-onset spastic ataxia. Sacsin is a modular protein that is localized on the mitochondrial surface and possibaly required for normal mitochondrial network organization. Sacsin knockdown resulted in a reduction in cells expressing plyglutamine-expanded ataxin-1, which correlated with a loss of cells with large nuclear ataxin-1 incusions. At the N-terminus, sacsin contains a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which can interact with the proteasome. At the C-terminus, sacsin harbors a protein-protein interaction J-domain followed by an higher eukaryotes and prokaryotes nucleotide-binding (HEPN) domain. The J-domain is typically associated with DnaJ-like co-chaperones involved in regulation of the Hsp70 heat shock system
RLPRVTVLHEYIGCRTFEVPPSAAVRDIKELIYEETDFPVSEQQLWHNGKELSDWVKIGGLVPSGSHEIF
LTL
>gnl|CDD|340570 cd17050, Ubl1_ANKUB1, ubiquitin-like (Ubl) domain 1 found in Ankyrin repeat and ubiquitin domain-containing 1 (ANKUB1) and similar proteins. ANKUB1 is an uncharacterized protein with two tandem ubiquitin-like (Ubl) domains located at the N-terminal of Ankyrin repeats (ANK). The Ubl domain may have an adaptor role in ubiquitin (Ub)-signaling by mediating protein-protein interaction. Ubl proteins have a beta-grasp Ubl fold and attach to other proteins in a Ubl manner with biochemically distinct roles. The ankyrin repeats have been identified in numerous proteins with diverse functions. The family corresponds to the first Ubl domain
MRIFVAFEGEREPLDVSPGQTVGDVKEMIRDKFHIDLSDGKQGRKFLVLTYAGADLQDSWVLSDIGIPPG
STIRCLLRE
>gnl|CDD|340571 cd17051, Ubl2_ANKUB1, ubiquitin-like (Ubl) domain 2 found in Ankyrin repeat and ubiquitin domain-containing 1 (ANKUB1) and similar proteins. ANKUB1 is an uncharacterized protein with two tandem ubiquitin-like (Ubl) domains located at the N-terminal of Ankyrin repeats (ANK). The Ubl domain may have an adaptor role in ubiquitin(Ub)-signaling by mediating protein-protein interaction. Ubl proteins have a beta-grasp Ubl fold and attach to other proteins in a Ubl manner with biochemically distinct roles. The ankyrin repeats have been identified in numerous proteins with diverse functions. The family corresponds to the second Ubl domain
EIKPVLYVYCVFNQETIPIMEKINVLTTTVSQLRSIISRKTGLPVSVFRLVTPDGTEMYDCNLLDDYGID
IGTTLRLETWDGW
>gnl|CDD|340572 cd17052, Ubl1_FAT10, ubiquitin-like (Ubl) domain 1 found in leukocyte antigen F (HLA-F) adjacent transcript 10 (FAT10) and similar proteins. FAT10, also termed ubiquitin D (UBD), or diubiquitin, is a cytokine-inducible ubiquitin-like (Ubl) modifer that is highly expressed in the thymus, and targets substrates covalently for 26S proteasomal degradation. It is also associated with cancer development, antigen processing and antimicrobial defense, chromosomal stability and cell cycle regulation. FAT10 is presented on immune cells and under the inflammatory conditions, is synergistically induced by interferon gamma (IFNgamma) and tumor necrosis factor (TNFalpha) in the non-immune (liver parenchymal) cells. FAT10 contains two Ubl domains. The family corresponds to the first Ubl domain of FAT10. Some family members contain only one Ubl domain
VVHVQSEEWDLMTFDANPQDSVKKINEHVRSKTKVPVQDQVLLLGSKILKPRRRLSSYGIDKEKTIHLTL
KVVK
>gnl|CDD|340573 cd17053, Ubl2_FAT10, ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 (FAT10) and similar proteins. FAT10, also termed ubiquitin D (UBD), or diubiquitin, is a cytokine-inducible ubiquitin-like (Ubl) modifer that is highly expressed in the thymus, and targets substrates covalently for 26S proteasomal degradation. It is also associated with cancer development, antigen processing and antimicrobial defense, chromosomal stability and cell cycle regulation. FAT10 is presented on immune cells and under the inflammatory conditions, is synergistically induced by interferon gamma (IFNgamma) and tumor necrosis factor (TNFalpha) in the non-immune (liver parenchymal) cells. FAT10 contains two Ubl domains. The family corresponds to the second Ubl domain of FAT10. Some family members contain only one Ubl domain
LTVNSKLLTGTVHTLQVSRSTTVAQVKAMIEDQSGVPPNEQILVYNGKRLEDGDKTLGEYGIKTGDTLYL
L
>gnl|CDD|340574 cd17054, Ubl_AtBAG1_like, ubiquitin-like (Ubl) domain found in Arabidopsis thaliana Bcl-2-associated athanogenes AtBAG1, AtBAG2, AtBAG3, AtBAG4, and similar proteins. The family includes four Arabidopsis BAG family proteins (AtBAG1, AtBAG2, AtBAG3, AtBAG4) that have very similar domain organizations with a ubiquitin-like (Ubl) domain in the N-terminus and a BAG domain in the C-terminus. They may function as co-chaperones that regulate diverse cellular pathways, such as programmed cell death and stress responses. AtBAG1, AtBAG3, and AtBAG4 are predicted to localize in the cytoplasm, but the localization of AtBAG2 is the microbody. AtBAG4 can interact with Hsc70. The overexpression of AtBAG4 in tobacco plants confers tolerance to a wide range of abiotic stresses such as UV light, cold, oxidants, and salt treatments
TIKIKVSHGAVYHEVTVSAQATFGDLKKLLVQDTGLQPQEQKLLFRGKEKDDKDFLDLAGVKDKAKVVLV
>gnl|CDD|340575 cd17055, Ubl_AtNPL4_like, ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, and similar proteins. The family includes a group of uncharacterized plant ubiquitin-like (Ubl) domain-containing proteins, including Arabidopsis thaliana NPL4-like protein 1 and NPL4-like protein 2
MLLRVRSRDGTERVEVPDDATVGDLKEKIAEQLSVPVSDQTLSLDPGPDLLTAKSSATLSQLGLKHGDMV
FLS
>gnl|CDD|340576 cd17056, Ubl_FAF1, ubiquitin-like (Ubl) domain found in FAS-associated factor 1 (FAF1) and similar proteins. FAF1, also termed UBX domain-containing protein 12 (UBXD12), or UBX domain-containing protein 3A (UBXN3A), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like (Ubl) fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, FAF1 contains two tandem Ubl domains, which show high structural similarity with UBX domain. FAF1 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The FAF1-p97 complex inhibits the proteasomal protein degradation in which p97 acts as a co-chaperone. Moreover, FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF1 is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kappaB (NF-kappaB) by interfering with the nuclear translocation of the p65 subunit. Although the precise role of FAF1 in the ubiquitination pathway remains unclear, FAF1 interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway. This family corresponds to Ubl domains
DFRVEYRDRNVDVVLEDTCTVGEIKQILENELQIPVSKMLLKGWKTGDVEDSTVLKSLHLPKNNSLYVLT
P
>gnl|CDD|340577 cd17057, Ubl_TMUB1_like, ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing proteins TMUB1, TMUB2, and similar proteins. TMUB1, also termed dendritic cell-derived ubiquitin-like protein (DULP), or hepatocyte odd protein shuttling protein, or ubiquitin-like protein SB144, or HOPS, is highly expressed in the nervous system. It is involved in the termination of liver regeneration and plays a negative role in interleukin-6-induced hepatocyte proliferation. The overexpression of Tmub1 has been shown to play a role in the inhibition of cell proliferation. TMUB1 has been implicated in the regulation of locomotor activity and wakefulness in mice, perhaps acting through its interaction with CAMLG. It also facilitates the recycling of AMPA receptors into synaptic membrane in cultured primary neurons. TMUB1 contains transmembrane domains and a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold. TMUB2 is an uncharacterized transmembrane domain and Ubl domain-containing protein that shows high sequence similarity to TMUB1
TITIRLKFLNETERVVYARPEDTVGDFKRRHFPDELAQGKRVRLIYQGQLLRDDSRTLSSYGIQDGSVIH
CHIS
>gnl|CDD|340578 cd17058, Ubl_SNRNP25, ubiquitin-like (Ubl) domain found in small nuclear ribonucleoprotein U11/U12 subunit 25 (SNRNP25) and similar proteins. SNRNP25, also termed U11/U12 small nuclear ribonucleoprotein 25 kDa protein, U11/U12 snRNP 25 kDa protein (U11/U12-25K), or minus-99 protein, is a component of the U11/U12 snRNPs that are part of the U12-type spliceosome. It contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions
AITLSVLRLDGESLPVVVPQNATVLDLKKAIERYFTLKLKREGGTKKISWKYVWKTYCLCFDGQKLTDDK
AKLKDYGIRNGDELTFVKR
>gnl|CDD|340579 cd17059, Ubl_OTU1, ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins. OTU1 (EC 3.4.19.12), also termed YOD1, or DUBA-8, or HIV-1-induced protease 7 (HIN-7), or OTU domain-containing protein 2 (OTUD2), is a p97-associated deubiquitinylase that functions as a key player in endoplasmic reticulum-associated degradation (ERAD). Its deubiquitinylase activity is also required for negatively regulating cholera toxin A1 (CTA1) retro-translocation. OTU1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU domain
MRLRVRSKGGQHVLSLLTDTSTVGELQDRIAALTGIPPSSQKILYGFPPKPLDLSDEEASLESLGIQSGD
TLIVE
>gnl|CDD|340580 cd17060, Ubl_RB1CC1, ubiquitin-like (Ubl) domain found in retinoblastoma 1-inducible coiled-coil protein 1 (RB1CC1) and similar proteins. RB1CC1, also termed FAK family kinase-interacting protein of 200 kDa (FIP200), is the mammalian counterpart of the yeast Atg17 gene and functions as a component of the ULK1/Atg13/RB1CC1/Atg101 complex essential for induction of autophagy. RB1CC1 is a key signaling node to regulate cellular proliferation and differentiation. As a DNA-binding transcription factor, RB1CC1 has been implicated in the regulation of retinoblastoma 1 (RB1) expression. RB1CC1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, as well as a nuclear localization signal (KPRK), a leucine zipper motif and a coiled-coil structure
MLYVFLVNTGTMLTFDMSLAVQSVSDLKEAIEEKTKIPVEKQVLLVSGGESLDPDKRVSSYSAGTDTNPI
FLFNK
>gnl|CDD|340581 cd17061, Ubl_IQUB, ubiquitin-like (Ubl) domain found in IQ and ubiquitin-like domain-containing protein (IQUB) and similar proteins. IQUB is an IQ motif and ubiquitin domain-containing protein that may play roles in cilia formation and/or maintenance. It contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions
ATATVKFVLMPSGQVITLAFTLGQTIGELKEHFSSELKIPPDVLQIMFDGKLVEDNTTLVDLGVRPNGTI
QLEMSSLDP
>gnl|CDD|340582 cd17062, Ubl_NUB1, ubiquitin-like (Ubl) domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins. NUB1, also termed negative regulator of ubiquitin-like proteins 1, or renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1), which may function in the regulation of cell cycle progression. NUB1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif
GVATLRVRLPGQGSKKKKITLETSLDITGSELREKIAEELGVPEDRIKLISNGKVLKDEKTLAEQGVKNN
SQVMVLVL
>gnl|CDD|340583 cd17063, Ubl_ANKRD60, ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and similar proteins. ANKRD60 is an uncharacterized ankyrin repeat domain-containing protein which also harbors a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions
RLFSLKLRLPETEETFTVPNCYPGMKVKELKSRLELVTGIPSHLQRLSYLDEGDLMDDSTLKYNDIVPGA
TITLRVW
>gnl|CDD|340584 cd17064, Ubl_TAFs_like, ubiquitin-like (Ubl) domain found in plant TBP-associated factors (TAFs) and similar proteins. TAFs, also termed transcription initiation factor TFIID subunits, or TAFII250 subunits, are components of the TFIID complex, a multisubunit protein complex involved in promoter recognition and essential for mediating regulation of RNA polymerase transcription. TAFs is the core scaffold of the TFIID complex, which is comprised of the TATA binding protein (TBP) and 12-15 TAFs. TAFs contain a ubiquitin-like (Ubl) domain and a Bromo domain
MKVIVKSLGGKGSLLRVDASETLESLKGKASKKLDDKPSEKVKLFYSGKELEDGKSLAEQNVPPNSLVHL
VR
>gnl|CDD|340585 cd17065, Ubl_UBP24, ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins. UBP24 (EC 3.4.19.12), also termed deubiquitinating enzyme 24, or ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24 (USP24), is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain, a ubiquitin-like (Ubl) domain, and a C-terminal peptidase C19 domain
FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGF
TDEQILTVK
>gnl|CDD|340586 cd17066, Ubl_KPC2, ubiquitin-like (Ubl) domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins. KPC2, also termed ubiquitin-associated domain-containing protein 1 or UBA domain containing 1 (UBAC1), or glialblastoma cell differentiation-related protein 1 (GBDR1), is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains an ubiquitin-like (Ubl) domain and two ubiquitin-associated (UBA) domains
FAGKVLRLHICTMEGAEWLEEVTEDTTIEKLKEKCLKHCVHGSLEDPKTLTHHKLIHAASERVLSDTKTV
LEENLQDKDVLLLIKKR
>gnl|CDD|340587 cd17067, RBD2_RGS12_like, Ras-binding domain (RBD) 2 of regulator of G protein signaling 12 (RGS12) and similar proteins. Regulator of G-protein signaling (RGS) proteins belong to a large family of GTPase-accelerating proteins (GAPs) which act as key inhibitors of G-protein-mediated cell responses in eukaryotes. The RGS12-like subfamily is composed of RGS12 and RGS14, with multidomain architectures including a RGS domain, two tandem Ras-binding domains (RBDs), and a second Galpha interacting domain, the GoLoco motif. The RBD is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes
RVLFRLDLPNKKIIGVKAKPTKTLAEVLRPILAKYGYKLDQVVVHLAGTQVPLDLGIPVSSIDNQRLVVE
TK
>gnl|CDD|340588 cd17068, RBD_PLEKHG5, Ras-binding domain (RBD) found in pleckstrin homology (PH) and RhoGEF domain containing G5 (PLEKHG5) and similar proteins. PLEKHG5, is also termed PH domain-containing family G member 5, or guanine nucleotide exchange factor 720 (GEF720), Syx, or Tech, is a novel Dbl-like protein related to p115Rho-GEF. It functions as a Rho guanine nucleotide exchange factor directly activating RhoA in vivo and potentially involved in the control of neuronal cell differentiation. It also regulates the balance of the RhoA downstream effector Dia and ROCK activities to promote polarized-cancer-cell migration. Moreover, PLEKHG5 activates the nuclear factor kappaB (NFkappaB) signaling pathway. Mutations in the PLEKHG5 gene are relevant with autosomal recessive intermediate Charcot-Marie-Tooth disease (CMT) and lower motor neuron disease (LMND)
KECFTVKFDDDDDDDVEIVPAVKGKTLRDVLEPLLERRGLDLDRVNVFLDSSNTPLPLEFDTYFLGGHTL
RVKAK
>gnl|CDD|340589 cd17069, DCX2, Dublecortin-like domain 2. Members in doublecortin (DCX) gene family are microtubule-associated proteins (MAPs). Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its protein domains can occur in double tandem or as a single repeat. The first repeat of DCX domain has a stable ubiquitin-like tertiary fold. Proteins with DCX double tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK)
FIKPKLVTVIRNGTKPRKAVRILLNKKTAHSFEQVLTDITEAIKLDSGAVRKLFTLDGRQVTCLQDFFGD
DDVFIAYGPEKFSH
>gnl|CDD|340590 cd17070, DCX2_RP_like, Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein. RP-like protein family is part of doublecortin (DCX) superfamily with double tandem DCX repeats that are associated with retinitis pigmentosa. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. RP-like proteins are colocalized to the photoreceptor and share a function in outer segment disc morphogenesis
KVITVISNGDPHSRHTILLNRRTTQSFEQVLQDLSELLKGPVRKLYTTDGKKVESLSALFHGPDEYVAA
>gnl|CDD|340591 cd17071, DCX1_DCDC2_like, Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2) and similar proteins. DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with
KIIVVYKNGDPFFPGKKFVVNERQVRTFDAFLNEVTSGIKAPFGAVRSIYTPTGGHRVKDLDSLQNGGVY
VAAGSERFKK
>gnl|CDD|340592 cd17072, DCX_DCDC5_like, Doublecortin-like domain found in doublecortin domain-containing protein 5 (DCDC5) and similar proteins. DCDC5 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC5 is expressed during mitosis and involved in coordinating late cytokinesis. DCDC5 interacts with cytoplasmic dynein and Rab8 as well as with the Rab8 nucleotide exchange factor Rabin8. This family also includes DCDC1, which is a hydrophilic intracellular protein that contains only one DCX repeat. Therefore, DCDC1 might only bind to microtubules without microtubule polymerization properties. DCDC1 is mainly expressed in adult testis
VRLRVLKNGERDLERAVYVVGPDLELQLFLDRCTERLNLPFAARRLFDENGKEIFTLRDLERDQLVYVSC
G
>gnl|CDD|340593 cd17073, KHA, KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found in potassium channel tetramerization domain containing 9 (KCTD9) and similar proteins. This family corresponds to KHA, the tetramerization domain of eukaryotic voltage-dependent potassium ion-channel proteins, mainly found in vertebrates KCTD9 and plants AKT proteins. In plants the domain lies at the C-terminus whereas in many chordates it lies at the N-terminus. KHA shows high sequence similarity with doublecortin-like domain, which has a stable ubiquitin-like tertiary fold. KCTD9, also termed BTB/POZ domain-containing protein 9, belongs to the KCTD protein family, which corresponds to potassium channel tetramerization domain proteins, a class of BTB-domain-containing proteins. It is involved in potassium channel formation. Moreover, KCTD9 contributes to liver injury through NK cell activation during hepatitis B virus (HBV)-induced acute-on-chronic liver failure. AKT proteins play crucial roles in K+ uptake and translocation in plant cells
KRVTVFVNGSSSGGKVIALPSTLSELLKIASEKLGIPAKRLYTGSGGEIDDIALIRDDDVLYVSE
>gnl|CDD|340594 cd17074, Ubl_CysO_like, ubiquitin-like (Ubl) domain found in Mycobacterium tuberculosis CysO and similar proteins. CysO, also termed 9.5 kDa culture filtrate antigen cfp10A, together with CysM (Cysteine synthase M), forms a protein complex CysM-CysO that represents a new cysteine biosynthetic pathway in Mycobacterium tuberculosis. The replacement of the acetyl group of O-acetylserine by CysO thiocarboxylate to generate a protein-bound cysteine is catalyzed by CysM in a pyridoxal 5?-phosphate (PLP)-dependent manner. The family also includes QbsE that functions as the sulfide donor for the biosynthesis of thioquinolobactin in Pseudomonas fluorescens. A JAMM motif protein QbsD catalyzes removal of the carboxy-terminal dipeptide from QbsE. Both CysO and QbsE are similar to prokaryotic sulfur carrier proteins such as ThiS and MoaD, containing the beta-grasp ubiquitin-like fold
VTVLIPTPLRKFTGGQKEVEVEGATVGELIDDLEAQYPGIKARLVDDGGKLRRFINIYVNDEDIRFLQGL
DTALKDGDEISIVPAIAGG
>gnl|CDD|340595 cd17075, UBX1_UBXN9, Ubiquitin regulatory domain X (UBX) 1 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) and similar proteins. UBXN9, also termed tether containing UBX domain for GLUT4 (TUG), or alveolar soft part sarcoma chromosomal region candidate gene 1 protein (ASPSCR1), or alveolar soft part sarcoma locus (ASPL), or renal papillary cell carcinoma protein 17 (RCC17), belongs to the UBXD family of proteins that contains two ubiquitin regulatory domains X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, UBXN9 contains an N-terminal ubiquitin-like (Ubl) domain. UBXN9 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. UBXN9 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4, assembly of the Golgi apparatus. In addition to GLUT4, UBXN9 also controls vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. UBXN9 and its budding yeast ortholog, Ubx4p, are multifunctional proteins that share some, but not all functions. Yeast Ubx4p is important for endoplasmic reticulum-associated protein degradation (ERAD) but UBXN9 appears not to share this function
SLVTIALQLEDGSRLQKSFPPSTTLWDILEHFEQESNVNLNLTEDGYLEPVCIYMRREISGEEALKKTTL
KSLGLTSGSALIRLV
>gnl|CDD|340596 cd17076, UBX_UBXN10, Ubiquitin regulatory domain X (UBX) found in UBX domain protein 10 (UBXN10) and similar proteins. UBXN10, also termed UBX domain-containing protein 3 (UBXD3), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN10 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. UBXN10 localizes to cilia in a p97-dependent manner, and both p97 and UBXN10 are required for ciliogenesis. Additionally, UBXN10 interacts with the intraflagellar transport B (IFT-B) and regulates anterograde transport into cilia
PRILLAIRLPDGQRFQRFFRPSDTLQDVLAFAESQSGLDLSNCIIETNEVPRRVFSDLSKTIAECGIQDK
TVLYIE
>gnl|CDD|340597 cd17077, UBX_UBXN11, Ubiquitin regulatory domain X (UBX) found in UBX domain protein 11 (UBXN11) and similar proteins. UBXN11, also termed colorectal tumor-associated antigen COA-1, or socius, or UBX domain-containing protein 5 (UBXD5), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN11 may function as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. UBXN11 also acts as a novel interacting partner of Rnd proteins (Rnd1, Rnd2, and Rnd3/RhoE), new members of Rho family of small GTPases. It directly binds to Rnd GTPases through its C-terminal region, and further participates in disassembly of actin stress fibers. UBXN11 also binds directly to Galpha12 and Galpha13 through its N-terminal region. As a novel activator of the Galpha12 family, UBXN11 promotes the Galpha12-induced RhoA activation
DVTTLRIKSENGEQTYILKMRFSDTIGDLRRYLDKHRSKDAASYEIVTTFPNKVYDDDSATLEELGLVPN
ATLHLR
>gnl|CDD|340598 cd17078, Ubl_SLD1_NFATC2ip, SUMO-like domain 1 (SLD1), structurally similar to a beta-grasp ubiquitin-like fold, found in nuclear factor of activated T-cells 2 interacting protein (NFATC2ip) and similar proteins. NFATC2ip, also termed nuclear factor of activated T cells (NFAT), cytoplasmic, calcineurin dependent 2 interacting protein, or 45 kDa NF-AT-interacting protein, or 45 kDa NFAT-interacting protein (Nip45), or nuclear factor of activated T-cells, or cytoplasmic 2-interacting protein, belongs to the eukaryotic-specific Rad60-Esc2-Nip45 (RENi) protein family. The family members may act as factors in transcriptional regulation, chromatin silencing and genomic stability, and typically contain an N-terminal polar/charged low-complexity segment and two C-terminal consecutive unique small ubiquitin-related modifier (SUMO)-like domains (SLD1 and SLD2) with beta-grasp fold. NFATC2ip was firstly identified as a co-regulator with NFAT and the T helper 2 (Th2)-specific transcription factor, c-Maf, to induce IL-4 production. NFATC2ip has also been involved in cellular differentiation and coordination of the immune response in humans and mice
RTITVKVRCRSGIKRIPLKPTDPFEKIFETLARLLGVPPSRILLLLNDQLLHLDDTPKSLNLGIADIIDC
VVVK
>gnl|CDD|340599 cd17079, Ubl_SLD2_NFATC2ip, SUMO-like domain 2 (SLD2), structurally similar to a beta-grasp ubiquitin-like fold, found in nuclear factor of activated T-cells 2 interacting protein (NFATC2ip) and similar proteins. NFATC2ip, also termed nuclear factor of activated T cells (NFAT), cytoplasmic, calcineurin dependent 2 interacting protein, or 45 kDa NF-AT-interacting protein, or 45 kDa NFAT-interacting protein (Nip45), or nuclear factor of activated T-cells, or cytoplasmic 2-interacting protein, belongs to the eukaryotic-specific Rad60-Esc2-Nip45 (RENi) protein family. The family members may act as factors in transcriptional regulation, chromatin silencing and genomic stability, and typically contain an N-terminal polar/charged low-complexity segment and two C-terminal consecutive unique small ubiquitin-related modifier (SUMO)-like domains (SLD1 and SLD2) with beta-grasp fold. NFATC2ip was firstly identified as a co-regulator with NFAT and the T helper 2 (Th2)-specific transcription factor, c-Maf, to induce IL-4 production. NFATC2ip has also been involved in cellular differentiation and coordination of the immune response in humans and mice. NFATC2ip SLD2 domain binds to E2 SUMOylation enzyme, Ubc9, in an almost identical manner to that of SUMO and thereby inhibits elongation of poly-SUMO chains
DEICLRVQGKEKHSQLEVSVSKTAPLKSLMSQYEEAMGLSGRKLSFFFDGTKLSGKETPADLGMESGDVI
EVW
>gnl|CDD|340600 cd17080, Ubl_SLD2_Esc2_like, SUMO-like domain 2 (SLD2), structurally similar to a beta-grasp ubiquitin-like fold, found in Saccharomyces cerevisiae establishes silent chromatin protein 2 (Esc2p) and similar proteins. Protein Esc2p belongs to the eukaryotic-specific Rad60-Esc2-Nip45 (RENi) protein family, whose members may act as factors in transcriptional regulation, chromatin silencing and genomic stability, and typically contain an N-terminal polar/charged low-complexity segment and two C-terminal consecutive unique small ubiquitin-related modifier (SUMO)-like domains (SLD1 and SLD2) with beta-grasp fold. Yeast Esc2p was identified as a factor promoting gene silencing. It is also required for genome integrity during DNA replication and sister chromatid cohesion in Saccharomyces cerevisiae. Esc2p promotes Mus81p complex-activity via its SUMO-like and DNA binding domains. It also acts as a novel structure-specific DNA-binding factor implicated in the local regulation of the Srs2p helicase through promoting recombination at sites of stalled replication. In addition, Esc2p specifically promotes the accumulation of SUMOylated Mms21-specific substrates and functions with Mms21p to suppress gross chromosomal rearrangements (GCRs). This family also includes DNA repair protein Rad60p from Schizosaccharomyces pombe. It is a SUMO mimetic and SUMO-targeted ubiquitin ligase (STUbL)-interacting protein that is required for the repair of DNA double strand breaks, recovery from S phase replication arrest, and plays an essential role in cell viability. Like other RENi family members, Rad60p has two SLD domains
ELIKLKLRGKDNKRLSLKVKPSTTLSDLVEAYKIKKKLSLAAAKVKLEFDGEPLDLSETVEDLDLEDEDM
LEVV
>gnl|CDD|340601 cd17081, RAWUL_PCGF1, RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in polycomb group RING finger protein 1 (PCGF1) and similar proteins. PCGF1, also termed nervous system Polycomb-1 (NSPc1), or RING finger protein 68 (RNF68), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) and serves as the core component of a noncanonical Polycomb repressive complex 1 (PRC1)-like BCOR complex that also contains RING1, RNF2, RYBP, SKP1, as well as the BCL6 co-repressor BCOR and the histone demethylase KDM2B, and is required to maintain the transcriptionally repressive state of some genes, such as Hox genes, BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. PCGF1 promotes cell cycle progression and enhances cell proliferation as well. It is a cell growth regulator that acts as a transcriptional repressor of p21Waf1/Cip1 via the retinoid acid response element (RARE element). Moreover, PCGF1 functions as an epigenetic regulator involved in hematopoietic cell differentiation. It cooperates with the transcription factor runt-related transcription factor 1 (Runx1) in regulating differentiation and self-renewal of hematopoietic cells. Furthermore, PCGF1 represents a physical and functional link between Polycomb function and pluripotency. PCGF1 contains a C3HC4-type RING-HC finger and a RAWUL domain
DEQVSLCLERLSSGKSSKDKNKKPLQRKYVRCSVRAEVRHLKKLLRKKLAVPPLQQVQILCNNEVLPDHM
TMKQIWLSHWFGKAPPLVLHYS
>gnl|CDD|340602 cd17082, RAWUL_PCGF2_like, RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in polycomb group RING finger proteins PCGF2, PCGF4, and similar proteins. This family includes polycomb group RING finger proteins, PCGF2 (also known as Mel-18, or RNF110, or ZNF144) and PCGF4 (also known as BMI-1, or RNF51), both serving as the core component of a canonical polycomb repressive complex 1 (PRC1). PRC1 is composed of a chromodomain-containing protein (CBX2, CBX4, CBX6, CBX7 or CBX8) and a polyhomeotic protein (PHC1, PHC2, or PHC3). Like other PCGF homologs, PCGF2 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. PCGF4 associates with the Runx1/CBFbeta transcription factor complex to silence the target gene in a PRC2-independent manner. Both, PCGF2 and PCGF4, contain a C3HC4-type RING-HC finger and a RAWUL domain
LISLSLEYYSPLRNQRKSEPESAKEPNVSLKELEKEEVQVPDKRYLRCPAAVTVGHLKKFIRMKFDLPPS
YEVEIMYSDEVLPDDYTLMDVAYIYTWRRKSPLRLYYR
>gnl|CDD|340603 cd17083, RAWUL_PCGF3, RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in polycomb group RING finger protein 3 (PCGF3) and similar proteins. PCGF3, also termed RING finger protein 3A (RNF3A), is one of six PcG RING finger (PCGF) homologs (PCGF1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6) and serves as the core component of a Polycomb repressive complex 1 (PRC1). Like other PCGF homologs, PCGF3 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. PCGF3 contains a C3HC4-type RING-HC finger, and a RAWUL domain
QVNICLECNSNNLKPLKRKYIRCSSQATITHLKKFIAKKLFLDIFRYNEVDILCNEEILGKDHTLKFVTV
TRWRFKETPLLLHYR
>gnl|CDD|340604 cd17084, RAWUL_PCGF5, RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in polycomb group RING finger protein 5 (PCGF5) and similar proteins. PCGF5, also termed RING finger protein 159 (RNF159), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) and serves as the core component of a Polycomb repressive complex 1 (PRC1). Like other PCGF homologs, PCGF5 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. PCGF5 contains a C3HC4-type RING-HC finger, and a RAWUL domain
DPQIAICLDCLRNNGQSGDNVVKGLMKKFIRCSSRVTVGTIKKFLSLKLKLPSSYELDVLCNGEIMGKDH
TLEFIYMTRWRLRGENSYPMVLQYRPRIDFG
>gnl|CDD|340605 cd17085, RAWUL_PCGF6, RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in polycomb group RING finger protein 6 (PCGF6) and similar proteins. PCGF6, also termed Mel18 and Bmi1-like RING finger (MBLR), or RING finger protein 134 (RNF134), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5 and PCGF6/MBLR), and serves as the core component of a noncanonical Polycomb repressive complex 1 (PRC1)-like L3MBTL2 complex, which is composed of some canonical components, such as RNF2, CBX3, CXB4, CXB6, CXB7 and CXB8, as well as some noncanonical components, such as L3MBTL2, E2F6, WDR5, HDAC1 and RYBP, and plays critical roles in epigenetic transcriptional silencing in higher eukaryotes. Like other PCGF homologs, PCGF6 possesses the transcriptional repression activity, and also associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF6 can regulate the enzymatic activity of JARID1d/KDM5D, a trimethyl H3K4 demethylase, through the direct interaction with it. Furthermore, PCGF6 is expressed predominantly in meiotic and post-meiotic male germ cells and may play important roles in mammalian male germ cell development. It also regulates mesodermal lineage differentiation in mammalian embryonic stem cells (ESCs) and functions in induced pluripotent stem (iPS) reprogramming. The activity of PCGF6 is found to be regulated by cell cycle dependent phosphorylation. PCGF6 contains a C3HC4-type RING-HC finger, and a RAWUL domain
DVSLLLEFIGAQEGSDNFKPLEKKYIRVSGEATVGHVEKFLRKKLNLDSTCEVDILCGEHILENYQTLRE
IRDQFGDGAQDGLLVLHYG
>gnl|CDD|340606 cd17086, RAWUL_RING1_like, RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in really interesting new gene proteins RING1, RING2 and similar proteins. RING1, also termed polycomb complex protein RING1, or RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), has been identified as a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. RING2, also termed huntingtin-interacting protein 2-interacting protein 3, or HIP2-interacting protein 3, or protein DinG, or RING finger protein 1B (RING1B), or RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. Both, RING1 and RING2, are core components of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING2 acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Members in this family contain a C3HC4-type RING-HC finger, and a RAWUL domain
EIELVFKPHPDEEEKDLDENQTRYIKTSANATVDHLSKYLAMRLALERQNEEGESDGNTADESERQYTIY
IATGPGQYVLLDGSMTLEQVNEKYWKVNKPLELYYA
>gnl|CDD|340607 cd17087, RAWUL_DRIP_like, RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in DREB2A-interacting protein (DRIP) and similar proteins. Dehydration-Responsive Element-Binding Protein 2A (DREB2A) regulates the expression of stress-inducible genes via the dehydration-responsive elements and requires posttranslational modification for its activation. DREB2A-Interacting Protein (DRIP) contains a RING finger, and a RING finger- and WD40-associated ubiquitin-like (RAWUL) domain. DRIP interacts with DREB2A and functions as a E3 ubiquitin ligases that negatively regulates DREB2A expression
GVWFSLKASANQSGESALPQITAPYLRIKDGNMTVSLVKKYLVTKLNLESETEVEITCRGQPVVSSLTLE
NLVDIWLQKSRDDQRSTPSVGSSAADFLMVLTYK
>gnl|CDD|340608 cd17088, FERM_F1_FRMPD1_like, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing proteins FRMPD1, FRMPD3, FRMPD4, and similar proteins. This family includes FERM and PDZ domain-containing proteins FRMPD1, FRMPD3, and FRMPD4, which all contain a PDZ domain and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). FRMPD1, also termed FERM domain-containing protein 2, is an activator of G-protein signaling 3 (AGS3)-binding protein that regulates the subcellular location of AGS3 and its interaction with G-proteins. FRMPD4, also termed PDZ domain-containing protein 10, or PSD-95-interacting regulator of spine morphogenesis (Preso), is a multiscaffolding protein that modulates both Homer1 and post-synaptic density protein 95 activity. Both FRMPD1 and FRMPD4 can associate with the tetratricopeptide repeat (TPR) motif-containing adaptor protein LGN. The biological role of FRMPD3 remains unclear
MPNVLKVYLENGQTKSFKYDQSTTVKDVLLSLQEKLGIKSMEHFSLVLEYVKSPRTNKLSLLQPDESLAQ
VAARPGSHHLRCLFRISFVP
>gnl|CDD|340609 cd17089, FERM_F0_TLN, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin and similar proteins. Talin is a cytoskeletal protein that activates integrins and couples them to cytoskeletal actin. Talin consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F0 domain that is joined to the F1 domain in a novel fixed orientation by an extensive charged interface. It is required for maximal integrin-activation, by interacting with other FA components; no binding partner has yet been found for it
LSLKIHIVKSGIVKTMQFDPSMTVYDACRLIREKIPEAAQGQASDYGLFLPDEDPKKGRWLEPDRTLEYY
DLRNGDELEYKKKH
>gnl|CDD|340610 cd17090, FERM_F1_TLN, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin and similar proteins. Talin is a cytoskeletal protein that activates integrins and couples them to cytoskeletal actin. Talin consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F0 domain that is joined to the F1 domain in a novel fixed orientation by an extensive charged interface. It is required for maximal integrin-activation, by interacting with other FA components; no binding partner has yet been found for it
RPLRVRTLDGSVKTVLVDDSQTVSQLVETICTKIGITNPEEFSLVREEEEEEKENKATLRKSTSRLRDDK
KMESLKKKLHTDDELNWLDHDQTLREQGVDEDETLLLRRKF
>gnl|CDD|340611 cd17091, FERM_F0_SHANK, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ankyrin repeat domains proteins, SHANK1, SHANK2, and SHANK3. SHANK proteins (SHANK1, SHANK2, and SHANK3) are core components of the postsynaptic density (PSD) of excitatory synapses. They act as scaffolding molecules that cluster neurotransmitter receptors as well as cell adhesion molecules attaching them to the actin cytoskeleton. They play important roles in proper excitatory synapse and circuit function. Mutations in SHANK genes, especially in SHANK3 and SHANK2, may lead to neuropsychiatric disorders, such as autism spectrum disorder (ASD). SHANK proteins contain an N-terminal F0 domain of FERM (Band 4.1, ezrin, radixin, moesin), six ankyrin (ANK) repeats, one SH3 (Src homology 3) domain, one PDZ (PSD-95, Dlg, and ZO-1/2, also termed DHR or GLGF) domain, and a C-terminal SAM (sterile alpha motif) domain. This family corresponds to the F0 domain that adopts a ubiquitin-like fold
IVLRISIPDLNLQKCLKFNPDDTVWDAKQQVLEKLAKDLKDALNYGLFLPPTNGKAGKFLDEERLLREYP
LDGPVGYLEFKYKR
>gnl|CDD|340612 cd17092, FERM1_F1_Myosin-VII, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins. This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGTDHVMDAISQC
EQYAKEKGAQEREAPWRLYFRKEIFAPWH
>gnl|CDD|340613 cd17093, FERM2_F1_Myosin-VII, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins. This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEGDFFFDFIRHLT
DWIKKARPTKDGPKPSLTYQVFFMRKLW
>gnl|CDD|340614 cd17094, FERM_F1_Max1_like, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Caenorhabditis elegans max-1 and its homologs PLEKHH1 and PLEKHH2. Caenorhabditis elegans max-1 is expressed and functions in motor neurons. MAX-1 protein plays a possible role in netrin-induced axon repulsion by modulating the UNC-5 receptor signaling pathway. PLEKHH1 is critically required in vascular patterning in vertebrate species through acting upstream of the ephrin pathway. PLEKHH2 is highly enriched in renal glomerular podocytes, and acts as a novel, important component of the podocyte foot processes. It is involved in matrix adhesion and actin dynamics. Members in this family all contain two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
PISIPVHLPNGTYQVVGFDGSTTVEEFLQTLNLELGIRPPSQSGFALFSDDPIGKDIEHCLQPSVKICDV
ISKWERASREAHSGKVDSSRVIRLTYKNRLYF
>gnl|CDD|340615 cd17095, FERM_F0_kindlins, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in the kindlin family. The kindlin family is composed of kindlin-1, 2 and 3, which are FERM domain-containing adaptor molecules that interact with the cytoplasmic component of integrins and regulate cell-matrix connections. Kindlins belong to the 4.1- ezrin-ridixin-moesin (FERM) domain containing protein family. They contain F1, F2 and F3 subdomains that typify FERM family members, and these subdomains are preceded by an N-terminal F0 subdomain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F0 domain. In addition, a distinctive feature of kindlins is the insertion of a pleckstrin homology (PH) subdomain into the F2 subdomain
SWELSITVTDLQIERKLRVTGDLHIGGVMLKLVETLGVAQDWSDHALWWPQKRVWLLKTRSTLDQYGVQA
DAELHFTPMH
>gnl|CDD|340616 cd17096, FERM_F1_kindlins, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the kindlin family. The kindlin family is composed of Kindlin-1, 2 and 3, which are FERM domain-containing adaptor molecules that interact with the cytoplasmic component of integrins and regulate cell-matrix connections. Kindlins belong to the 4.1- ezrin-ridixin-moesin (FERM) domain containing protein family. They contain F1, F2 and F3 subdomains that typify FERM family members, and these subdomains are preceded by an N-terminal F0 subdomain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F1 domain. In addition, a distinctive feature of kindlins is the insertion of a pleckstrin homology (PH) subdomain into the F2 subdomain
KTLRIQLPDLQYLDLRVDFSVKVFNAVVDLCKELGIRHPEELSLLRPPLYRPKSLVDKARLNSGWLDSSR
SLMEQGVRENDTLLLRFKYY
>gnl|CDD|340617 cd17097, FERM_F1_ERM_like, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family proteins. The ezrin-radixin-moesin (ERM) family includes a group of closely related cytoskeletal proteins that play an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. They exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Merlin, which is highly related to the members of the ezrin, radixin, and moesin (ERM) protein family that are directly attached to and functionally linked with NHE1, is included in this family
INVRVTTMDAELEFSIKPKAKGRELFDLVCRTIGLRETWYFGLQYENKKGRVAWLKPDKKVLTQDVSKNN
TLKFFFLVKFYPE
>gnl|CDD|340618 cd17098, FERM_F1_FARP1_like, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and pleckstrin domain-containing protein 1 (FARP1) and similar proteins. This family includes the F1 sub-domain of FERM, RhoGEF and pleckstrin domain-containing proteins FARP1, FARP2, and FERM domain-containing protein 7 (FRMD7). FARP1, also termed chondrocyte-derived ezrin-like protein (CDEP), or pleckstrin homology (PH) domain-containing family C member 2 (PLEKHC2), is a neuronal activator of the RhoA GTPase. It promotes outgrowth of developing motor neuron dendrites. It also regulates excitatory synapse formation and morphology, as well as activates the GTPase Rac1 to promote F-actin assembly. FARP2, also termed FERM domain including RhoGEF (FIR), or Pleckstrin homology (PH) domain-containing family C member 3, is a Dbl-family guanine nucleotide exchange factor (GEF) that activates Rac1 or Cdc42 in response to upstream signals, suggesting roles in regulating processes such as neuronal axon guidance and bone homeostasis. It is also a key molecule involved in the response of neuronal growth cones to class-3 semaphorins. FRMD7 plays an important role in neuronal development and is involved in the regulation of F-actin, neurofilament, and microtubule dynamics. All family members contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
LHVKVQMLDDTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTDPEGNKCWLDPEKPILRQVKRPK
DVVFKFVVKFYTPDP
>gnl|CDD|340619 cd17099, FERM_F1_PTPN14_like, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptors PTPN14, PTPN21, and similar proteins. This family includes tyrosine-protein phosphatase non-receptors PTPN14 and PTPN21, both of which are protein-tyrosine phosphatase (PTP). They belong to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation
KNSFVVRIQLLDNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLRWVDLEKPLKKQLD
KHAHEPLLYFGVMFY
>gnl|CDD|340620 cd17100, FERM_F1_PTPN3_like, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and similar proteins. This family includes two tyrosine-protein phosphatase non-receptors, PTPN3 and PTPN4, both of which belong to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
EVRCIVHFLDDTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFSDDSPATDSMRWLDPLKPIRKQI
KGGPPYYLNFRVKFYV
>gnl|CDD|340621 cd17101, FERM_F1_PTPN13_like, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 13 (PTPN13) and similar proteins. This family includes tyrosine-protein phosphatase non-receptor type 13 (PTPN13), FERM and PDZ domain-containing protein 2 (FRMPD2), and FERM domain-containing proteins FRMD1 and FRMD6. All family members contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
RRYVNVVLLNGQRLQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAVLKDGEYFFLDPDTKLSKYAPKGW
KSEAKKGLKGGKPVFTLYFRVKFYVDN
>gnl|CDD|340622 cd17102, FERM_F1_FRMD3, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 3 (FRMD3) and similar proteins. FRMD3, also termed band 4.1-like protein 4O, or ovary type protein 4.1 (4.1O), belongs to the 4.1 protein superfamily, which share the highly conserved membrane-association FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). FRMD3 is involved in maintaining cell shape and integrity. It also functions as a tumour suppressor in non-small cell lung carcinoma (NSCLC). Some single nucleotide polymorphisms (SNPs) located in FRMD3 have been associated with diabetic kidney disease (DKD) in different ethnicities
YKCTIRLLDDSEVICCEFKKDTKGQFLLDYVCNYLNLLEKDYFGLRYVDTEKQRHWLDPNKSIYKQLKGV
PPYVLCFRVKFY
>gnl|CDD|340623 cd17103, FERM_F1_FRMD4, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing proteins FRMD4A, FRMD4B, and similar proteins. This family includes FERM domain-containing proteins FRMD4A and FRMD4B, both of which contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). FRMD4A is a cytohesin adaptor involved in cell structure, transport and signaling. It promotes the growth of cancer cells in tongue, head and neck squamous cell carcinomas. FRMD4B, also termed GRP1-binding protein GRSP1, interacts with the coil-coil domain of ARF exchange factor GRP1 to form the Grsp1-Grp1 complex that co-localizes with cortical actin rich regions in response to stimulation of CHO-T cells with insulin or epidermal growth factor (EGF)
EGRRCQVVLLDDRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYEDETGHYNWLQLDKRVLDHEFP
KKWSSGPLVLHFAVKFYVESI
>gnl|CDD|340624 cd17104, FERM_F1_MYLIP, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ubiquitin-protein ligase MYLIP and similar proteins. MYLIP, also termed inducible degrader of the LDL-receptor (Idol), or myosin regulatory light chain interacting protein (MIR), is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Its activity depends on E2 ubiquitin-conjugating enzymes of the UBE2D family, including UBE2D1, UBE2D2, UBE2D3, and UBE2D4. MYLIP stimulates clathrin-independent endocytosis and acts as a sterol-dependent inhibitor of cellular cholesterol uptake by binding directly to the cytoplasmic tail of the LDLR and promoting its ubiquitination via the UBE2D1/E1 complex. The ubiquitinated LDLR then enters the multivesicular body (MVB) protein-sorting pathway and is shuttled to the lysosome for degradation. Moreover, MYLIP has been identified as a novel ERM-like protein that affects cytoskeleton interactions regulating cell motility, such as neurite outgrowth. The ERM proteins includes ezrin, radixin, and moesin, which are cytoskeletal effector proteins linking actin to membrane-bound proteins at the cell surface. MYLIP contains a FERM-domain and a C-terminal C3HC4-type RING-HC finger. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
MLCLVSQPDSVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTGPKGERLWLNLRNRISRQLPGPP
PYRLRLRVKFF
>gnl|CDD|340625 cd17105, FERM_F1_EPB41, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1 (EPB41) and similar proteins. EPB41, also termed protein 4.1 (P4.1), or 4.1R, or Band 4.1, or EPB4.1, belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41 is a widely expressed cytoskeletal phosphoprotein that stabilizes the spectrin-actin cytoskeleton and anchors the cytoskeleton to the cell membrane. EPB41 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
MHCKVSLLDDTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGLAIWDSPTSKTWLDPAKEIKKQVHGGP
WEFTFNVKFYPPD
>gnl|CDD|340626 cd17106, FERM_F1_EPB41L, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like proteins. The family includes erythrocyte membrane protein band 4.1-like proteins EPB41L1/4.1N, EPB41L2/4.1G, and EPB41L3/4.1B. They belong to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L1 is a cytoskeleton-associated protein that may serve as a tumor suppressor in solid tumors. EPB41L2 is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L3 also acts as a tumor suppressor implicated in a variety of meningiomas and carcinomas. Members in this family contain a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
SQQCKVLLLDGTEYTCEVEKRAKGQVLFDKVCEHLNLLEKDYFGLTYRDAQDQKNWLDPAKEIKKQIRSG
PWLFSFNVKFYPPD
>gnl|CDD|340627 cd17107, FERM_F1_EPB41L4A, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band 4.1-like protein 4A (EPB41L4A) and similar proteins. EPB41L4A, also termed protein NBL4, is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). EPB41L4A is an important component of the beta-catenin/Tcf pathway. It may be related to determination of cell polarity or proliferation
EEFYCEIVLLDESELILTIQQDGIKSSKGSVVLDVVFQHLNLLETDYFGLRYIDRQHQTHWLDPAKTLSE
QLKLIGPPYTLYFGVKFYAED
>gnl|CDD|340628 cd17108, FERM_F1_EPB41L5_like, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like 5 (EPB41L5) and similar proteins. This family includes FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like proteins, EPB41L5 and EPB41L4B. EPB41L5 is a mesenchymal-specific protein that is an integral component of the ARF6-based pathway. EPB41L4B is a positive regulator of keratinocyte adhesion and motility, suggesting a role in wound healing. It also promotes cancer metastasis in melanoma, prostate cancer and breast cancer. Both EPB41L5 and EPB41L4B contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
IQCKVILLDGTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQFMDAAQVQHWLDPTKKIKKQVKIGP
PYTLRFRVKFY
>gnl|CDD|340629 cd17109, FERM_F1_SNX17_like, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in PX-FERM family sorting nexin proteins. This family includes three endosome-associated PX (Phox homology) and FERM (Band 4.1, ezrin, radixin, moesin) domain-containing proteins called sorting nexin (SNX) 17, SNX27, and SNX31, which are modular peripheral membrane proteins acting as central scaffolds mediating protein-lipid interactions, cargo binding, and regulatory protein recruitment. They are key regulators of endosomal recycling and bind conserved NPX(Y/F) peptide sorting motifs in transmembrane cargos via an atypical FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
SDVELRVALPNGQTVTVRVKTSDTTEQVLEAVAAKVGLDSTLVGYFALFLVRSHSEGKLSFVRKLAPFEL
PYVSYISNYTPGTKLTLRKWYFT
>gnl|CDD|340630 cd17110, FERM_F1_Myo10_like, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional myosin-X and similar proteins. Myosin-X, also termed myosin-10 (Myo10), is an untraditional member of myosin superfamily. It is an actin-based motor protein that plays a critical role in diverse cellular motile events, such as filopodia formation/extension, phagocytosis, cell migration, and mitotic spindle maintenance, as well as a number of disease states including cancer metastasis and pathogen infection. Myosin-X functions as an important regulator of cytoskeleton that modulates cell motilities in many different cellular contexts. It regulates neuronal radial migration through interacting with N-cadherin. Like other unconventional myosins, Myosin-X is composed of a conserved motor head, a neck region and a variable tail. The neck region consists of three IQ motifs (light chain-binding sites), and a predicted stalk of coiled coil. The tail contains three PEST regions, three PH domains, a MyTH4 domain, and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Amoebozoan Dictyostelium discoideum myosin VII (DdMyo7) and uncharacterized pleckstrin homology domain-containing family H member 3 (PLEKHH3) are also included in this family. Like metazoan Myo10, DdMyo7 is essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin
LQELTVTVTCQGGRTCKVAIDSWTTCGEVSKDLARRLGLERSRNGFALFETSGDIERALEAKTRVVDVLS
KWEKLAATGSSPGDDGWKLLFKLYLFL
>gnl|CDD|340631 cd17111, RA1_DAGK-theta, Ras-associating (RA) domain 1 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins. DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Ten mammalian isoforms of DAGK have been identified to date which are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the first RA domain of DAGK-theta
KEIVKVFDGNASLKRNQFRLITVPRNASVEQVLEAALRAFHIPDDPENYYLTDAYESSLGDERELEDPGP
LRNLVRREGKRPAIFLRYKEK
>gnl|CDD|340632 cd17112, RA_MRL_like, Ras-associating (RA) domain found in Mig10/RIAM/Lpd (MRL) family and growth factor receptor-bound (Grb) protein 7/10/14. MRL proteins share a common structural architecture, including a central structural unit consisting of a Ras-associating (RA) domain and a pleckstrin homology (PH) domain, an upstream coiled-coil region, and a number of polyproline motifs. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. RA and PH form a tandem domain pair (RA-PH), and serve tightly coordinated functions in both Ras GTPase signaling via the RA domain and membrane translocalization via the PH domain. MRL proteins have distinct functions in cell migration and adhesion, signaling, and in cell growth. Grb7/10/14 are multi-domain cytoplasmic adaptor proteins that are recruited to activated receptor tyrosine kinases. Grb7 and its related family members Grb10 and Grb14 share a conserved domain architecture that includes an amino-terminal proline-rich region, a central segment termed the GM region (for Grb and Mig) which includes the RA, PIR, and pleckstrin homology (PH) domains, and a carboxyl-terminal SH2 domain. The tandem RA and PH domains of Grb7/10/14 are also found in a second adaptor family, Rap1-interacting adaptor molecule (RIAM) and lamellipodin, which is involved in actin-cytoskeleton rearrangement. Grb7/10/14 family proteins are phosphorylated on serine/threonine as well as tyrosine residues and are mainly localized to the cytoplasm
VVKVYNEDGSSKTVAVDENMTARDVCQILVEKNHVDPDKSWSLVEELPELGLERTLEDHELVVDVYSKWP
SDSNNKFLFRK
>gnl|CDD|340633 cd17113, RA_ARAPs, Ras-associating (RA) domain found in Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing proteins ARAP1, ARAP2, ARAP3, and similar proteins. ARAPs are phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P(3))-dependent Arf Rap-activated guanosine triphosphatase (GTPase)-activating proteins (GAPs). They contain multiple functional domains, including ArfGAP and RhoGAP domains, as well as a sterile alpha motif (Sam) domain, five PH domains, and a RA domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes
SGDFLIPVYIEEKEGTSVNIKVTPTMTAEEVVEQALNKKNLGGPEGNWALFEVIEDGGLERPLHESEKVL
DVVLRWSQWPRKSNYLCVKKNPLLE
>gnl|CDD|340634 cd17114, RA_PLC-epsilon, Ras-associating (RA) domain found in Phosphatidylinositide-specific phospholipase C (PLC)-epsilon. PLC is a signaling enzyme that hydrolyzes membrane phospholipids to generate inositol triphosphate. PLC-epsilon represents a novel forth class of PLC that has a PLC catalytic core domain, a CDC25 guanine nucleotide exchange factor domain and two RA (Ras-association) domains. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Although PLC RA1 and RA2 have homologous ubiquitin-like folds only RA2 can bind Ras and activate it. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction
RRMFFVTVHGVVPEEPYTVLKITQDTTAREVIAQALGKAGKSLERVTDYVLVEEVQKGWDRKETEKPGSQ
RILDMDEKILQAQSKWKGSGRFILKKL
>gnl|CDD|340635 cd17115, RA_RHG20, Ras-associating (RA) domain found in Rho GTPase-activating protein 20 (RHG20) and similar proteins. RHG20, also termed ARHGAP20, is one of GTPase activating proteins for Rho family proteins (RhoGAPs). It contains a PH-like domain, an RA domain, a RhoGap domain, and two Annexin-like (ANXL) repeats. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin that is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes
KSIPLKVLNRDVGSCAYSKTLTVSNTDTAKDVIKMALQQFGITGDPSDYQLWVKSGKEESPYPLIGHEYP
FSIKMSHLRDAARQSDGDNLNILDLDHLSSMENLPPEAQCQFILRPS
>gnl|CDD|340636 cd17116, RA_Radil_like, Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein (Radil) and similar proteins. Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation.This family also includes Ras-interacting protein 1 (Rain, also termed Rasip1), which is a novel Ras-interacting protein with a unique subcellular localization. It interacts with Ras in a GTP-dependent manner, and may serve as an effector for endomembrane-associated Ras. Radil contains RA, DIL, and PDZ domains. In contrast, Rain contains a myosin5-like cargo binding domain, a RA domain and a PDZ domain. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes
DDPAELSTQASAPGVLKIFGDSICPGANYKSVLATPRSSAQELVKEALERYGLARSEAKQYVLCDVIGRF
TGAEKDQSRSSSSERWRTECLRVIGDNEKPLLLQSLWKPKEGFSRRFELRR
>gnl|CDD|340637 cd17117, RA_ANKFN1_like, Ras-associating (RA) domain found in Ankyrin repeat and fibronectin type-III domain-containing protein 1 (ANKFN1) and similar proteins. ANKFN1 is a multi-domain protein, with unknown function, that contains two ankyrin repeats and one fibronectin type-III domain. Except for the mammalian homologs, most metazon ANKFN1 harbor a RA domain at the C-terminus. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin
ILRVYAAYETGLPKGTSVKLHVTPKTTAREVVNLVVQQLNKAVRSKGKGGPVYSEDQLDDFCLVAVVGAR
ERCLRDDFQPLQLQNPWTKGRLYVRLK
>gnl|CDD|340638 cd17118, Ubl_HERP1, ubiquitin-like (Ubl) domain found in homocysteine-inducible endoplasmic reticulum stress protein HERP1 and similar proteins. HERP1, also termed homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein (HERPUD1), or methyl methanesulfonate (MMF)-inducible fragment protein 1 (MIF1), is an endoplasmic reticulum (ER) integral membrane protein containing an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold. HERP1 is a component of the ER quality control (ERQC) system, also called ER-associated degradation (ERAD), which is involved in ubiquitin-dependent degradation of misfolded ER proteins. It promotes the degradation of ER-resident Ca2+ channels. It is also involved in ubiquitin ligase HRD1-dependent protein degradation at the ER. Moreover, HERP1 plays a role in regulating the cell cycle, apoptosis and steroid hormone biosynthesis in mouse granulosa cells
EVTLLIKSPSQRHEDLELRGDRGWTVRRLKTQLRREYPDHPPEQEQRLIYSGKLLLDHLYLREVLPKDEE
RHVLHLVC
>gnl|CDD|340639 cd17119, Ubl_HERP2, ubiquitin-like (Ubl) domain found in homocysteine-inducible endoplasmic reticulum stress protein HERP2 and similar proteins. HERP2, also termed homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 2 protein (HERPUD2), is an endoplasmic reticulum (ER) integral membrane protein containing an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold. It is homologous to HERP1, and could be involved in the unfolded protein response (UPR) pathway. It regulates the ubiquitin ligase HRD1-dependent protein degradation at the ER
PVTLVIKAPNQKYDDQTINCFLNWTVEKLKSHLSKVYPSKPSTKDQRLVYSGRLLPDHLQLKDILRKQDE
YHMVHLV
>gnl|CDD|340640 cd17120, Ubl_UBTD1, ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein 1 (UBTD1). UBTD1 is the mammalian homolog of the mitochondrial Dc-UbP/UBTD2 protein, both of which contain an N-terminal ubiquitin binding domain (UBD) and a C-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. UBTD1 stably interacts with the UBE2D family of E2 ubiquitin conjugating enzymes. As a tumor suppressor, UBTD1 plays a pivotal role in in regulating cellular senescence that mediates p53 function. It is also involved in MDM2 ubiquitination and degradation
LKVRLSTGKDVRLSASMSDTIGQLKKQLHAQEGIEPSWQRWFFSGKLLTDKTRLQETKIQKDFVIQVIV
>gnl|CDD|340641 cd17121, Ubl_UBTD2, ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein 2 (UBTD2). UBTD2, also termed dendritic cell-derived ubiquitin-like protein (DC-UbP), or ubiquitin-like protein SB72, is a potential ubiquitin shuttle protein firstly identified in dendritic cells and implicated in apoptosis. It binds proteins involved in the ubiquitination pathway and may play an important role in regulating protein ubiquitination and delivery of ubiquitinated substrates in eukaryotic cells. UBTD2 is expressed in tumor cells but not in normal human adult tissue suggesting a role in tumorogenesis. It can potentially regulate the stability of proteins involved in various physiological processes relevant to many disease phenotypes, such as ageing and cancer. UBTD2 reconciles protein ubiquitination and deubiquitination via linking UbE1 and USP5 enzymes
ECQLRLRLSTGKDLKLAVRSTDTVYHMKRRLHTAEGVEPGSQRWFFSGRPLTDKMKLEELKIPKDYVVQV
IVSQP
>gnl|CDD|340642 cd17122, Ubl_UHRF1, ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing protein 1(UHRF1). UHRF1, also termed inverted CCAAT box-binding protein of 90 kDa, or nuclear protein 95, or nuclear zinc finger protein Np95 (Np95), or RING finger protein 106, or transcription factor ICBP90, or E3 ubiquitin-protein ligase UHRF1, is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma, gastric cancer, esophageal squamous cell carcinoma, colorectal cancer, prostate cancer, and breast cancer. UHRF1 can acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21.Moreover, UHRF1-dependent repression of factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination ofTIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF1 contains an N-terminal ubiquitin-like domain (Ubl), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET and RING finger associated (SRA) domain, and a C-terminal RING-finger domain. It specifically binds to hemimethylated DNA, double-stranded CpG dinucleotides, and recruits the maintenance methyltransferase DNMT1 to its hemimethylated DNA substrate through its SRA domain. UHRF1-dependent H3K23 ubiquitination has an essential role in maintenance DNA methylation and replication. The tandem Tudor domain directs UHRF1 binding to the heterochromatin mark histone H3K9me3 and the PHD finger targets UHRF1 to unmodified histone H3 in euchromatic regions. The RING-finger domain exhibits both autocatalytic E3 ubiquitin (Ub) ligase activity and activity against histone H3 and DNMT1
MWIQVRTMDGKETHRIDSLSKLTKVEELRQKIQELFGVEPERQRLFYRGKQMEDGHTLFDYSVGLNDIVQ
LLVR
>gnl|CDD|340643 cd17123, Ubl_UHRF2, ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2). UHRF2, also termed Np95/ICBP90-like RING finger protein (NIRF), or Np95-likeRING finger protein, or nuclear protein 97, or nuclear zinc finger protein Np97, or RING finger protein 107, or E3 ubiquitin-protein ligase UHRF2, was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131(ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) through interacting with HBV core protein and promoting its degradation. UHRF2 contains an N-terminal ubiquitin-like domain (Ubl), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a set- and ring-associated (SRA) domain, and a C-terminal RING finger
MWIQVRTIDGTETQTIDDLSRLTKIESLREKIQELFNVRPERQRLFYRGKQLEDGHTLFDYNVGLNDIVQ
LLIR
>gnl|CDD|340644 cd17124, Ubl_TECR, ubiquitin-like (Ubl) domain found in trans-2,3-enoyl-CoA reductase (TECR). TECR, also termed very-long-chain enoyl-CoA reductase, or synaptic glycoprotein SC2, or TER, or GPSN2, is a synaptic glycoprotein that catalyzes the fourth reaction in the synthesis of very long-chain fatty acids (VLCFA) which is the reduction step of the microsomal fatty acyl-elongation process. Diseases involving perturbations to normal synthesis and degradation of VLCFA (e.g. adrenoleukodystrophy and Zellweger syndrome) have significant neurological consequences. The mammalian TECR P182L mutation causes nonsyndromic mental retardation. Deletion of the yeast TECR homolog (TSC13p) is lethal. TECR contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions, as well as a C-terminal catalytic domain
FFEVEILDAKTKEKLCFLDKVEPNATIGEIKNLFHKSHPQWYPARQSLRLDPKGKSLKDEDILQNLPVGT
TATFYFRDL
>gnl|CDD|340645 cd17125, Ubl_TECRL, ubiquitin-like (Ubl) domain found in trans-2,3-enoyl-CoA reductase-like (TECRL). TECRL, also termed steroid 5-alpha-reductase 2-like 2 protein (SRD5A2L2), is associated with life?threatening inherited arrhythmias displaying features of both long QT syndrome (LQTS) and catecholaminergic polymorphic ventricular tachycardia (CPVT). TECRL contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions, as well as a C-terminal catalytic domain
FEVEILDAQTRKQICVVDKVHPSSTILDVKIKFHKTCPQWYPSRVGLQLERNGPFLKDSCEIQSIAVSSI
VTLYFTDL
>gnl|CDD|340646 cd17126, Ubl_HR23A, ubiquitin-like (Ubl) domain found in UV excision repair protein RAD23 homolog A (HR23A). HR23A, also termed RAD23A, is a DNA repair protein that binds to 19S subunit of the 26S proteasome and shuttles ubiquitinated proteins to the proteasome for degradation, which is required for efficient nucleotide excision repair (NER), a primary mechanism for removing UV-induced DNA lesions. HR23A also plays a critical role in the interaction of HIV-1 viral protein R (Vpr) with the proteasome, especially facilitating Vpr to promote protein poly-ubiquitination. HR23A contains an N-terminal ubiquitin-like (Ubl) domain that binds proteasomes and two C-terminal ubiquitin-associated (UBA) domains that bind ubiquitin or multi-ubiquitinated substrates. In addition, it has a XPC protein-binding domain that might be necessary for its efficient NER function
VTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFV
VVMVTK
>gnl|CDD|340647 cd17127, Ubl_TBK1, ubiquitin-like (Ubl) domain found in TRAF family member-associated NF-kappaB activator (TANK)-binding kinase 1 (TBK1). TBK1, also termed NF-kappa-B-activating kinase, or T2K, or TANK-binding kinase 1, is an interferon regulatory factor-activating kinase that is a non-canonical member of IKK family. It plays a role in regulating innate immunity, inflammation and oncogenic signaling. TBK1 is involved in the regulation of type I interferons and of nuclear factor-kappaB (NF-kappaB) signal transduction. It regulates factors such as IRF3 and IRF7, promoting antiviral activity in the interferon signaling pathways. It modulates inflammatory hyperalgesia by regulating MAP kinases and NF-kappaB dependent genes. Moreover, TBK1 acts as a central player in the intracellular nucleic acid-sensing pathways involved in antiviral signaling. Dysregulation of TBK1 activity is often associated with autoimmune diseases and cancer. TBK1 contains an N-terminal protein kinase domain followed a ubiquitin-like (Ubl) domain, and a C-terminal elongated helical domain. The Ubl domain acts as a protein-protein interaction domain, and has been implicated in regulating kinase activity, which modulates interactions in the interferon pathway
RMVIHVFSLQQMTAHKIYIHSYNTATIFHELVYKQTKIISSNQELIYEGRRLVLEPGRLAQHFPKTTEEN
PIFVVSRE
>gnl|CDD|340648 cd17128, Ubl_IKKE, ubiquitin-like (Ubl) domain found in inhibitor of nuclear factor kappa-B kinase subunit epsilon (IKK-E). IKK-E (EC 2.7.11.10), also termed I-kappa-B kinase epsilon (IKKepsilon), or IKK-epsilon, or IkBKE, or inducible I kappa-B kinase (IKK-i), is an interferon regulatory factor-activating kinase that is a non-canonical member of IKK family. It is involved in the cellular innate immunity by inducing type I interferons. It is induced by the activation of nuclear factor-kappaB (NF-kappaB). IKK-E has also been implicated in antiviral immune response in higher vertebrates. It acts as a crucial pro-survival factor in human T cell leukemia virus type 1 (HTLV-1)-transformed T lymphocytes. Moreover, IKK-E plays an essential role in tumor initiation and progression. It inhibits protein kinase C (PKC) to promote Fascin-dependent actin bundling. IKK-E contains an N-terminal protein kinase domain followed a ubiquitin-like (Ubl) domain, and a C-terminal elongated helical domain. The Ubl domain acts as a protein-protein interaction domain, and has been implicated in regulating kinase activity, which modulates interactions in the interferon pathway
RIVIHVFSLQQATMHHIYIHSYNTTTIFLEDVFKQTSIAPAHQEYLFEGHLYELEPNLQAQHFPKTTENK
PLILISTE
>gnl|CDD|340649 cd17129, Ubl1_FAF1, ubiquitin-like (Ubl) domain 1 found in FAS-associated factor 1 (FAF1) and similar proteins. FAF1, also termed UBX domain-containing protein 12 (UBXD12), or UBX domain-containing protein 3A (UBXN3A), belongs to the UBXD family of proteins that contains the ubiquitin (Ub) regulatory domain X (UBX) with a beta-grasp ubiquitin-like (Ubl) fold, but without the C-terminal double glycine motif. The UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, FAF1 contains two tandem Ubl domains, which show high structural similarity with the UBX domain. FAF1 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The FAF1-p97 complex inhibits the proteasomal protein degradation in which p97 acts as a co-chaperone. Moreover, FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF1 is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kappaB (NF-kappaB) by interfering with the nuclear translocation of the p65 subunit. Although the precise role of FAF1 in the ubiquitination pathway remains unclear, FAF1 interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway. The family corresponds to the first Ubl domain
MLTFNVEYRDRTIDVVLPDTETVGDIKQILENELGIPPCKQILKGWKARTVSDSTVLRSLHLPKENSLYL
LTP
>gnl|CDD|340650 cd17130, Ubl2_FAF1, ubiquitin-like (Ubl) domain 2 found in FAS-associated factor 1 (FAF1) and similar proteins. FAF1, also termed UBX domain-containing protein 12 (UBXD12), or UBX domain-containing protein 3A (UBXN3A), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like (Ubl) fold, but without the C-terminal double glycine motif. The UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, FAF1 contains two tandem Ubl domains, which show high structural similarity with the UBX domain. FAF1 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The FAF1-p97 complex inhibits the proteasomal protein degradation in which p97 acts as a co-chaperone. Moreover, FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF1 is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kappaB (NF-kappaB) by interfering with the nuclear translocation of the p65 subunit. Although the precise role of FAF1 in the ubiquitination pathway remains unclear, FAF1 interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway. The family corresponds to the second Ubl domain
NYTLNITDTTSQREYNLNFPGSKTIQEVKQDVSDLTSIPVRHQRWTGWPSGASDDTMLLALGLDFPCHRL
TVSRR
>gnl|CDD|340651 cd17131, Ubl_TMUB1, ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing protein 1 (TMUB1). TMUB1, also termed dendritic cell-derived ubiquitin-like protein (DULP), or hepatocyte odd protein shuttling protein, or ubiquitin-like protein SB144, or HOPS, is highly expressed in the nervous system. It is involved in the termination of liver regeneration and plays a negative role in interleukin-6-induced hepatocyte proliferation. The overexpression of Tmub1 has been shown to play a role in the inhibition of cell proliferation. TMUB1 has also been implicated in the regulation of locomotor activity and wakefulness in mice, perhaps acting through its interaction with CAMLG. It also facilitates the recycling of AMPA receptors into synaptic membrane in cultured primary neurons. TMUB1 contains transmembrane domains and a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold
PIVLRLKFLNDTERLARVKPEDTIGSLKRTYFPGQEHQVRLIYQGQLLGDDSQTLASLHLTDNCVLHCHI
S
>gnl|CDD|340652 cd17132, Ubl_TMUB2, ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing protein 2 (TMUB2). TMUB2 is composed of an uncharacterized transmembrane domain and a ubiquitin-like (Ubl) domain-containing protein that shows high sequence similarity to TMUB1; the latter is highly expressed in the nervous system and is involved in the termination of liver regeneration
LITVRLKFLNDTEEVAVVRPEDTIGFLKSKYFPGQEQQMKLIYQGQLLQDPARTLRSLNITDNCVIHCHR
S
>gnl|CDD|340653 cd17133, RBD_ARAF, Ras-binding domain (RBD) found in serine/threonine-protein kinase ARAF. ARAF, also termed proto-oncogene ARAF, or proto-oncogene ARAF1, or proto-oncogene PKS2, belongs to the RAF protein family. The RAF family includes three RAF kinases ARAF, BRAF, and RAF1/CRAF, encoded by proto-oncogenes, which activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. ARAF is predominantly found in urogenital tissue with a low basal kinase activity. It directly cross-talks with NODAL/SMAD2 signaling in a MAPK-independent manner. It also promotes MAPK pathway activation and cell migration in a cell type-dependent manner. Moreover, ARAF acts as a scaffold to stabilize BRAF-CRAF heterodimers. Mice deleted for ARAF are viable but die perinatally
GTIKVYLPNKQRTVVNVRPGMTVYDSLDKALKVRGLNQDCCAVYRLIKGRKTLTDWETDITPLVGEELLV
EVL
>gnl|CDD|340654 cd17134, RBD_BRAF, Ras-binding domain (RBD) found in serine/threonine-protein kinase BRAF. BRAF, also termed proto-oncogene B-Raf, or p94, or v-Raf murine sarcoma viral oncogene homolog B1, belongs to the RAF family. The RAF family includes three RAF kinases ARAF, BRAF, and RAF1/CRAF, encoded by proto-oncogenes, which activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. BRAF is the most effective RAF kinase in terms of induction of MEK/ERK activity. It is somatically mutated in a number of human cancers
KPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELH
VEVLENVPL
>gnl|CDD|340655 cd17135, RBD_CRAF, Ras-binding domain (RBD) found in RAF proto-oncogene serine/threonine-protein kinase RAF1/CRAF. RAF1/CRAF, also termed proto-oncogene c-RAF (cRaf), or Raf-1, belongs to the RAF family. The RAF family includes three RAF kinases ARAF, BRAF, and RAF1/CRAF, encoded by proto-oncogenes, which activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. RAF1/CRAF is an important effector of Ras-mediated signaling and is a critical regulator of the MAPK/ERK pathway
SNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGE
ELQVDFL
>gnl|CDD|340656 cd17136, RBD1_RGS12, Ras-binding domain (RBD) 1 of regulator of G protein signaling 12 (RGS12). RGS12 (regulator of G protein signaling 12) is a multidomain RGS protein with numerous signaling regulatory elements. In addition to a central RGS domain which is responsible for GAP activity, the long RGS12 splice variant contains a PDZ (PSD-95/Discs-large/ZO-1 homology) domain capable of binding the interleukin-8 receptor B (CXCR2) or its own C-terminal, a phosphotyrosine-binding (PTB) domain that associates with tyrosine-phosphorylated N-type calcium channel, two tandem Ras-binding domains (RBDs) that may integrate signaling pathways involving both heterotrimeric and monomeric G-proteins, and a GoLoco (G-alpha-i/o-Loco) interaction motif which has guanine nucleotide dissociation inhibitor (GDI) activity toward G-alpha-i subunits. RBD is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. RGS proteins belong to a large family of GTpase-accelerating proteins (GAPs) which act as key inhibitors of G-protein-mediated cell responses in eukaryotes
KHCCVNLPDGSSCAVAIKPGVSIREMLSGLCEKLGINLAAVDLFLVGGDKPLVLDQDSSTLESRDLRLEK
>gnl|CDD|340657 cd17137, RBD1_RGS14, Ras-binding domain (RBD) 1 of regulator of G protein signaling 14 (RGS14). RGS12 (regulator of G protein signaling 14) is a RGS protein with a multidomain structure that allows it to interact with binding partners from multiple signaling pathways. RGS proteins belong to a large family of GTPase-accelerating proteins (GAPs) which act as key inhibitors of G-protein-mediated cell responses in eukaryotes. RGS14 contains an N-terminal RGS domain, two tandem Ras-binding domains (RBDs) and a G protein regulatory (GPR, also referred to as a GoLoco) motif. RGS14 binds activated H-Ras-GTP through its first RBD and interacts with Rap2-GTP and RAF kinases by the second tandem RBD. RBD is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. RGS14 modulates neuronal physiology and all of its binding partners have roles in synaptic plasticity
KYCCVYLPDGTASLASVRPGLTIRDMLSGICEKRGISLPDVKVYLVGNEKKPLVLDQDCSVLTDQEVRLE
N
>gnl|CDD|340658 cd17138, RBD2_RGS12, Ras-binding domain (RBD) 2 of regulator of G protein signaling 12 (RGS12). RGS12 (regulator of G-protein signaling 12) is a multidomain RGS protein with numerous signaling regulatory elements. In addition to a central RGS domain which is responsible for GAP activity, the long RGS12 splice variant contains a PDZ (PSD-95/Discs-large/ZO-1 homology) domain capable of binding the interleukin-8 receptor B (CXCR2) or its own C-terminal, a phosphotyrosine-binding (PTB) domain that associates with tyrosine-phosphorylated N-type calcium channel, two tandem Ras-binding domains (RBDs) that may integrate signaling pathways involving both heterotrimeric and monomeric G-proteins, and a GoLoco (G-alpha-i/o-Loco) interaction motif which has guanine nucleotide dissociation inhibitor (GDI) activity toward G-alpha-i subunits. RBD is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. RGS proteins belong to a large family of GTpase-accelerating proteins (GAPs) which act as key inhibitors of G-protein-mediated cell responses in eukaryotes
RTLFRLDLVPINRSVGLKAKPTKPVTEVLRPVVAKYGLNLNELVARISGEKEPLDLGLPISNLDGQRVVL
EEK
>gnl|CDD|340659 cd17139, RBD2_RGS14, Ras-binding domain (RBD) 2 of regulator of G protein signaling 14 (RGS14). RGS14 (regulator of G protein signaling 14) is a RGS protein with a multidomain structure that allows it to interact with binding partners from multiple signaling pathways. RGS proteins belong to a large family of GTPase-accelerating proteins (GAPs) which act as key inhibitors of G-protein-mediated cell responses in eukaryotes. RGS14 contains an N-terminal RGS domain, two tandem Ras-binding domains (RBDs) and a G protein regulatory (GPR, also referred to as a GoLoco) motif. RGS14 binds activated H-Ras-GTP through its first RBD and interacts with RAP2-GTP and RAF kinases by the second tandem RBD. RBD is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. RGS14 modulates neuronal physiology and all of its binding partners have roles in synaptic plasticity
RITFELEIAFLGKTVRIVAKSSKTLQEALQPILQKYGLRPQEVVLTMSGEKQALDMNTPVSSLANKTLVL
DRV
>gnl|CDD|340660 cd17140, DCX1_DCLK1, Dublecortin-like domain 1 found in doublecortin-like kinase 1 (DCLK1). DCLK1 is a member of doublecortin (DCX) protein superfamily that functions as a microtubule-associated protein (MAP), and contains two conserved tubulin binding domains. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule-binding domains, DCLK encodes a serine/threonine kinase domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases. DCLK1 appears to regulate cyclic AMP signaling and is involved in neuronal migration, retrograde transport, neuronal apoptosis and neurogenesis. Unlike DCX, this DCLK has varying levels of expression throughout embryonic and adult life
KAKKVRFYRNGDRYFKGIVYAISPDRFRSFEALLADLTRTLSDNVNLPQGVRTIYTIDGLKKISSLDQLV
EGESYVCGSIEPFKKLEYT
>gnl|CDD|340661 cd17141, DCX1_DCLK2, Dublecortin-like domain 1 found in doublecortin-like kinase 2 (DCLK2). DCLK2 is a member of doublecortin (DCX) protein superfamily that functions as a microtubule-associated protein (MAP), and contains two conserved tubulin binding domains, which typically occur in tandem. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier (Ubiquitination) in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule binding domains, DCLK encodes a serine/threonine kinase-domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases. Molecular actions of DCX members are less well characterized and it shows that DCLK2 members regulate cyclic AMP signaling. Unlike DCX, this DCLK has varying levels of expression throughout embryonic and adult life
KAKKVRFYRNGDRYFKGLVYAVSSDRFRSFDALLMELTRSLSDNVNLPQGVRTIYTIDGSKKITSLDELL
EGESYVCASNEPFRK
>gnl|CDD|340662 cd17142, DCX2_DCX, Dublecortin-like domain 2 found in neuronal migration protein doublecortin (DCX). DCX, also termed doublin or lissencephalin-X (Lis-XDCX), is a microtubule-associated protein (MAP). It belongs to the doublecortin (DCX) family, has double tandem DCX repeats, and is expressed in migrating neurons. Structure studies show that the N-terminal DCX domain has a stable ubiquitin-like fold. DCX is not only a unique MAP in terms of its structure, but also interacts with multiple additional proteins. Mutations in the human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation
FVRPKLVTIIRSGVKPRKAVRVLLNKKTAHSFEQVLTDITEAIKLETGVVKKLYTLDGKQVTCLHDFFGD
DDVFIACGPEKFRY
>gnl|CDD|340663 cd17143, DCX2_DCLK1, Dublecortin-like domain 2 found in doublecortin-like kinase 1 (DCLK1). DCLK1 is a member of doublecortin (DCX) protein family that functions as a microtubule-associated protein (MAP), and contains two conserved tubulin binding domains. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule binding domains, DCLK encodes a serine/threonine kinase-domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases. DCLK1 appears to regulate cyclic AMP signaling and is involved in neuronal migration, retrograde transport, neuronal apoptosis and neurogenesis. Unlike DCX, the DCLK has varying levels of expression throughout embryonic and adult life
FIRPKLVTIIRSGVKPRKAVRILLNKKTAHSFEQVLTDITDAIKLDSGVVKRLYTLDGKQVMCLQDFFGD
DDIFIACGPEKFRY
>gnl|CDD|340664 cd17144, DCX2_DCLK2, Dublecortin-like domain 2 found in doublecortin-like kinase 2 (DCLK2). DCLK2 is a member of doublecortin (DCX) protein family that functions as a microtubule-associated protein (MAP), and contains two conserved tubulin binding domains, which typically occur in double tandem. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule binding domains, DCLK encodes a serine/threonine kinase-domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases. DCLK2 members regulate cyclic AMP signaling. Unlike DCX, the DCLK has varying levels of expression throughout embryonic and adult life
FIKPKLVTVIRSGVKPRKAVRILLNKKTAHSFEQVLTDITEAIKLDSGVVKRLCTLDGKQVTCLQDFFGD
DDVFIACGPEKYRY
>gnl|CDD|340665 cd17145, DCX1_RP1, Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein. RP1, also termed oxygen-regulated protein 1, is a member of the doublecortin (DCX) family. Its DCX domains occur in double tandem repeats. RP1 is associated with retinitis pigmentosa, which is a type of inherited blindness. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The RP1 protein is expressed in photoreceptors and is required for correct stacking of outer segment discs. It interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with
KRVCFYKSGDPQFGGLRMVVNSRSFKTFDALLDNLSKKVPLPFGVRNITTPRGVHHITSLEDLEDGKSYI
CSHQKKVKP
>gnl|CDD|340666 cd17146, DCX1_RP1L1, Doublecortin-like domain 1 found in retinitis pigmentosa 1-like 1 (RP1L1) protein. RP1L1 is a member of the doublecortin (DCX) family. Its DCX domains occur in double tandem repeats. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX-domain of RP1L1 localizes to the photoreceptor and is genetically associated with retinitis pigmentosa
KKITFYKSGDPQFGGVKMAVNKRTFKSFSALLDDLSQRVPLPFGVRTITTPRGTHSISRLEQLEDGGCYL
CSDKKYVKP
>gnl|CDD|340667 cd17147, DCX2_RP1, Dublecortin-like domain 2 found in retinitis pigmentosa 1 (RP1)-like protein. RP1, also termed oxygen-regulated protein 1, is a member of doublecortin (DCX) superfamily that contains double tandem repeats of the DCX domains. RP1 is associated with retinitis pigmentosa, which is a type of inherited blindness. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The RP1 protein is expressed in photoreceptors that is required for correct stacking of outer segment discs. RP1 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with
RKLIVFKNGDPGFKHTLILNKKTTQSFEALLDHVSELMQFPVVKLYTTDGRRVDSLQALILSSGAVVAAG
REPFKP
>gnl|CDD|340668 cd17148, DCX2_RP1L1, Dublecortin-like domain 2 found in retinitis pigmentosa 1-like 1 (RP1L1) protein. RP1L1 is a member of doublecortin (DCX) family. Its protein domains occur in tandem repeats. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX-domain of RP1L1 localizes to the photoreceptor and is genetically associated with retinitis pigmentosa
KKITLVKNGDPDVRRSIILNRRNARNLRTFLDEISDLLQFPVKKLYTLEGRKIDSIQALLHCPSVLVCVG
REPFKP
>gnl|CDD|340669 cd17149, DCX1_DCDC2, Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2). DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with
KNVLVYRNGDPFYAGRRLVINEKRVSSFEVFLKEVTGGVQAPFGAVRNIYTPRGGHRVRSLEQLQSGEQY
VAAGRERFKK
>gnl|CDD|340670 cd17150, DCX1_DCDC2B, Dublecortin-like domain 1 found in doublecortin domain-containing protein 2B (DCDC2B). DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with
KNVVVYRNGDPFFTGRKFVVNQRQFLTFEAFLNEVTSNIQAPVAVRNLYTPREGHRVTELGDLQNGGHYV
AAGFERFKK
>gnl|CDD|340671 cd17151, DCX1_DCDC2C, Dublecortin-like domain 1 found in doublecortin domain-containing protein 2C (DCDC2C). DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with
KTILVYRNGDPFYQAHKVVIHRRRVKTFDALLRQLTETVKVPFGVRCLYTPRNGHRVKGLDDLQGGGKYV
AAGRERFKK
>gnl|CDD|340672 cd17152, DCX2_DCDC2, Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2). DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with
PCTIFVVANGDLLNPAVRLLIPRKTLNQWEKILEMITEKVTLRTGAVRRLYTLDGKLINDGSELENGQFY
VAVGREKFKK
>gnl|CDD|340673 cd17153, DCX2_DCDC2B, Doublecortin-like domain 2 found in doublecortin domain-containing protein 2B (DCDC2B). DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of a ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with
PCIIHVFRNGDLLSPPFRLLIPKHMLQDWETILSLLTEKANLRTGAVRKLCTLDGVPLSSGKELVSGQYY
VAVGSEKFKD
>gnl|CDD|340674 cd17154, DCX2_DCDC2C, Doublecortin-like domain 2 found in doublecortin domain-containing protein 2C (DCDC2C). DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of a ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with
SRTINVFTNGEVLVPPAKIIIPKFTLRSWENVLAMITEKAFLRTGGVFRLCTLNGHPVSDSTELEDNHYY
VAVGSEKFKA
>gnl|CDD|340675 cd17155, DCX_DCDC1, Doublecortin-like domain found in doublecortin domain-containing protein 1 (DCDC1). Doublecortin (DCX) is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCX gene family consists of eleven paralogs in human and mouse, such that its protein domains can occur in tandem or single repeats. Proteins with DCX tandem domains in general have roles in microtubule (MT) regulation and signal transduction while single DCX repeat proteins are normally localized to actin-rich subcellular structures or to the nucleus. DCDC1 is a hydrophilic intracellular protein that contains only one DCX repeat. Therefore, DCDC1 might only bind to microtubules without microtubule polymerization properties. DCDC1 is mainly expressed in adult testis
IKVTAFKNGTRDVFAKVTAPNIKILLEECTEKLGLNSAARRVFLADGTEVFEPKDIPRDADVYISTGEPF
KD
>gnl|CDD|340676 cd17156, DCX1_DCDC5, Doublecortin-like domain 1 found in doublecortin domain-containing protein 5 (DCDC5). DCDC5 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC5 is expressed during mitosis and is involved in coordinating late cytokinesis. DCDC5 interacts with cytoplasmic dynein and Rab8, as well as with the Rab8 nucleotide exchange factor Rabin8
LRLRVLRNGEKDKNKAVTVVGEFQLFLERCTTALNLPFAARRLFDEKGKEHFTLKDLKRDQLVYVSCGEA
WIDPKL
>gnl|CDD|340677 cd17157, DCX2_DCDC5, Doublecortin-like domain 2 found in doublecortin domain-containing protein 5 (DCDC5). DCDC5 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC5 is expressed during mitosis and involved in coordinating late cytokinesis. DCDC5 interacts with cytoplasmic dynein and Rab8, as well as with the Rab8 nucleotide exchange factor Rabin8
RRILVFKNGDGSEGYEIVADLDEFEQFLDACTSKLNLGSPARVLYDWEGKEIKDLSEAPKLDKCLQNSST
PVLGPLWVSKGEGFSP
>gnl|CDD|340678 cd17158, DCX3_DCDC5, Doublecortin-like domain 3 found in doublecortin domain-containing protein 5 (DCDC5). DCDC5 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC5 is expressed during mitosis and involved in coordinating late cytokinesis. DCDC5 interacts with cytoplasmic dynein and Rab8, as well as with the Rab8 nucleotide exchange factor Rabin8
VKILAYKNGEGRLRDGVLIIGSTFPGLLDQCTHRLGLARAARRLYTADGTLILTLILRYPIEVWVSCGEP
FIP
>gnl|CDD|340679 cd17159, DCX4_DCDC5, Doublecortin-like domain 4 found in doublecortin domain-containing protein 5 (DCDC5). DCDC5 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC5 is expressed during mitosis and involved in coordinating late cytokinesis. DCDC5 interacts with cytoplasmic dynein and Rab8, as well as with the Rab8 nucleotide exchange factor Rabin8
KRVLVYPNGGSPERAVYAWGKSIEELLDSCTERLGLRKPAKYLYTPDGEQIQSWDDIERDMLLCVSTGEP
FLT
>gnl|CDD|340680 cd17160, UBX_UBXN2A, Ubiquitin regulatory domain X (UBX) found in UBX domain protein 2A (UBXN2A) and similar proteins. UBXN2A, also termed UBX domain-containing protein 4 (UBXD4), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN2A functions as a p97 (also known as VCP or Cdc48) adaptor protein facilitating the regulation of the cell surface number and stability of alpha3-containing neuronal nicotinic acetylcholine receptors (nAChRs). It also regulates nicotinic receptor degradation by modulating the E3 ligase activity of carboxyl terminus of Hsc70 interacting protein (CHIP) that is involved in the degradation of several disease-related proteins. In addition, UBXN2A is an important anticancer factor that contributes to p53 localization and activation as a host defense mechanism against cancerous growth. It acts as a potential mortalin inhibitor, as well as a potential chemotherapy sensitizer for clinical application. It binds to the oncoprotein mortalin-2 (mot-2), and further unsequesters p53 from mot-2 in the cytoplasm, resulting in translocation of p53 to the nucleus where p53 proteins activate their downstream biological effects, including apoptosis
LNELEPITNIQIWLADGRRIVQKFNLSHRISHVRDFVEKIQGSSMSVPFTLATSLPFRELLDETLTLQEA
DLQNAVIVQRLQKT
>gnl|CDD|340681 cd17161, UBX_UBXN2B, Ubiquitin regulatory domain X (UBX) found in UBX domain protein 2B (UBXN2B) and similar proteins. UBXN2B, also termed NSFL1 cofactor p37, or p97 cofactor p37, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN2B is an adaptor protein of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. UBXN2B forms a tight complex with p97 in the cytosol and localizes to the Golgi and endoplasmic reticulum (ER)
IDDSVPTTKIQIRLADGSRLIQRFNQSHRIHDIRQFIVQSRPVFAASDFLLVTTFPNKELTDESQTLQEA
DILNTVILQRLK
>gnl|CDD|340682 cd17162, UBX_UBXN2C, Ubiquitin regulatory domain X (UBX) found in NSFL1 cofactor (also known as UBX domain-containing protein 2C (UBXN2C) and similar proteins. UBXN2C, also termed NSFL1C, or NSFL1 cofactor p47, or p97 cofactor p47, UBX1, or UBXD10, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN2C is a major adaptor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The main role of the UBXN2C/p97 complex is in regulation of membrane fusion events. It plays an essential role in the reassembly of Golgi stacks at the end of mitosis. UBXN2C also functions as an essential factor for Golgi membrane fusion, which associates with the nuclear factor-kappaB essential modulator (NEMO) subunit of the IkappaB kinase (IKK) complex upon tumor necrosis factor (TNF)-alpha or interleukin (IL)-1 stimulation, induces the lysosome-dependent degradation of polyubiquitinated NEMO without p97, and thus inhibits IKK activation. Moreover, UBXN2C regulates a membrane fusion process, which is required by the maintenance of the endoplasmic reticulum (ER) network, through phosphorylation by Cdc2 kinase
INDSEPVTNIQIRLADGGRLVQKFNHSHRIRDIRLFIVDARPAMAATSFVLMTTFPNKELTDENQTLKEA
NLLNAVIVQRLK
>gnl|CDD|340683 cd17163, Ubl_ATG8_GABARAPL2, ubiquitin-like (Ubl) domain found in GABA type A receptor associated protein like 2 (GABARAPL2, also known as GATE16). Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. GABARAPL2 (GABA type A receptor associated protein like 2), also known as GATE-16 (golgi-associated adenosine triphosphatase enhancer of 16 kDa), has a ubiquitin-like (Ubl) domain and is a sub-family of the autophagy-related 8 (ATG8) protein family. GABARAPL2 participates to the autophagosome maturation, and seems to be involved in constitutive transport under normal conditions and in autophagic processes during stress. GABARAPL2 is characterized as a membrane transport modulator that controls intra-Golgi transport by interacting with NSF and Golgi v-SNARE GOS-28
FKEEHSLEQRCAESAKIRAKYPDRIPVIVEKVPKSQIPDIDKRKFLVPSDITVAQFMWIIRKRIQLPSEK
AIFLFVGKVLPQSSATMGQLYEEHKDEDGFLYVAYSGENTFG
>gnl|CDD|340684 cd17164, RAWUL_PCGF2, RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in polycomb group RING finger protein 2 (PCGF2). PCGF2, also termed DNA-binding protein Mel-18, or RING finger protein 110 (RNF110), or zinc finger protein 144 (ZNF144), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) and serves as the core component of a canonical polycomb repressive complex 1 (PRC1), which is composed of a chromodomain-containing protein (CBX2, CBX4, CBX6, CBX7 or CBX8) and a polyhomeotic protein (PHC1, PHC2, or PHC3). Like other PCGF homologs, PCGF2 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF2 uniquely regulates PRC1 to specify mesoderm cell fate in embryonic stem cells. It is required for PRC1 stability and maintenance of gene repression in embryonic stem cells (ESCs) and essential for ESC differentiation into early cardiac-mesoderm precursors. PCGF2 also plays a significant role in the angiogenic function of endothelial cells (ECs) by regulating endothelial gene expression. Furthermore, PCGF2 is a SUMO-dependent regulator of hormone receptors. It facilitates the deSUMOylation process by inhibiting PCGF4/BMI1-mediated ubiquitin-proteasomal degradation of SUMO1/sentrin-specific protease 1 (SENP1). It is also a novel negative regulator of breast cancer stem cells (CSCs) that inhibits the stem cell population, and in vitro and in vivo self-renewal through the inactivation of Wnt-mediated Notch signaling. PCGF2 contains a C3HC4-type RING-HC finger, and a RAWUL domain
IVSLSIEFYEGARDEKKQRPASPGDPFKEQRNGKRFLRCPAAMTVMHLAKFLRNKMDVPSKYRVEVLYED
EPLKDYYTLMDIAYIYPWRRNGPLPLKYR
>gnl|CDD|340685 cd17165, RAWUL_PCGF4, RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in polycomb group RING finger protein 4 (PCGF4). PCGF4, also termed polycomb complex protein BMI-1 (B cell-specific Moloney murine leukemia virus integration site 1), or RING finger protein 51 (RNF51), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) and serves as the core component of a canonical Polycomb repressive complex 1 (PRC1), which is composed of a chromodomain-containing protein (CBX2, CBX4, CBX6, CBX7 or CBX8) and a Polyhomeotic protein (PHC1, PHC2, or PHC3), and plays important roles in chromatin compaction and H2AK119 monoubiquitination. PCGF4 associates with the Runx1/CBFbeta transcription factor complex to silence target gene in a PRC2-independent manner. Moreover, PCGF4 is expressed in the hair cells and supporting cells. It can regulate cell survival by controlling mitochondrial function and reactive oxygen species (ROS) level in thymocytes and neurons, thus having an important role in the survival and sensitivity to ototoxic drug of auditory hair cells. Furthermore, PCGF4 controls memory CD4 T-cell survival through direct repression of Noxa gene in an Ink4a- and Arf-independent manner. It is required in neurons to suppress p53-induced apoptosis via regulating the antioxidant defensive response, and also involved in the tumorigenesis of various cancer types. PCGF4 contains a C3HC4-type RING-HC finger, and a RAWUL domain
IISLSIEFFDQNKLERKGNKDKEKSKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPSTFQIDVMYEEEP
LKDYYTLMDIAYIYTWRRNGPLPLKYR
>gnl|CDD|340686 cd17166, RAWUL_RING1, RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in really interesting new gene 1 protein (RING1). RING1, also termed polycomb complex protein RING1, or RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), has been identified as a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. It is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase that transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING1 interacts with multiple PcG proteins and displays tumorigenic activity. It also shows zinc-dependent DNA binding activity. Moreover, RING1 inhibits transactivation of the DNA-binding protein recombination signal binding protein-Jkappa (RBP-J) by Notch through interaction with the LIM domains of KyoT2. RING1 contains a C3HC4-type RING-HC finger, and a RAWUL domain
EIELVFRPHPLLVEKERYSQTRYVKTTANATVDHLSKYLALRIALEERQTDQPAEEPGVGETASGGEGSR
AGPPGRLLDVSEKQYTIYITTGSGQFTTLNGSLTLELVNEKYWKVSKPLELYYA
>gnl|CDD|340687 cd17167, RAWUL_RING2, RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in really interesting new gene 2 protein (RING2). RING2, also termed huntingtin-interacting protein 2-interacting protein 3, or HIP2-interacting protein 3, or protein DinG, or RING finger protein 1B (RING1B), or RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. RING2 is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. The enzymatic activity of RING2 is enhanced by the interaction with BMI1/PCGF4, and it is dispensable for early embryonic development and much of the gene repression activity of PRC1. Moreover, RING2 plays a key role in terminating neural precursor cell (NPC)-mediated production of subcerebral projection neurons (SCPNs) during neocortical development. It also plays a critical role in nonhomologous end-joining (NHEJ)-mediated end-to-end chromosome fusions. Furthermore, RING2 is essential for expansion of hepatic stem/progenitor cells. It promotes hepatic stem/progenitor cell expansion through simultaneous suppression of cyclin-dependent kinase inhibitors (CDKIs) Cdkn1a and Cdkn2a, known negative regulators of cell proliferation. RING2 also negatively regulates p53 expression through directly binding with both p53 and MDM2 and promoting MDM2-mediated p53 ubiquitination in selective cancer cell types to stimulate tumor development. RING2 contains a C3HC4-type RING-HC finger, and a RAWUL domain
EIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLETASEKQYTIY
IATASGQFTVLNGSFSLELVSEKYWKVNKPMELYYA
>gnl|CDD|340688 cd17168, FERM_F1_FRMPD1, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 1 (FRMPD1). FRMPD1, also termed FERM domain-containing protein 2, is an activator of G-protein signaling 3 (AGS3)-binding protein that regulates the subcellular location of AGS3 and its interaction with G-proteins. It also binds to the tetratricopeptide repeat (TPR) motif-containing adaptor protein LGN. FRMPD1 contains a PDZ domain and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
MPNVLKVYLENGQTKAFKFESNTTVKDIILTLKEKLSIRSIEHFALVLEEQYSISKLYLLHEEELIEQVV
EKRESHDYRCLFRVCFVPKD
>gnl|CDD|340689 cd17169, FERM_F1_FRMPD3, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 3 (FRMPD3). FRMPD3 is an uncharacterized FERM and PDZ domain-containing protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
IPNVLKVFLENGQIKSFTFDGRTTVKDVMLTLQDRLSLRHIEHFALVLEYGGPEQNHKFLLLQDKQPLAH
VVQRTHYQGMKCLFRICFFPKDP
>gnl|CDD|340690 cd17170, FERM_F1_FRMPD4, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 4 (FRMPD4). FRMPD4, also termed PDZ domain-containing protein 10, or PSD-95-interacting regulator of spine morphogenesis (Preso), is a multiscaffolding protein that modulates both Homer1 and postsynaptic density protein 95 activity. It can associate with the tetratricopeptide repeat (TPR) motif-containing adaptor protein LGN. Moreover, FRMPD4 is asymmetrically distributed in the cytosol and nuclei of neural stem/progenitor cells in the adult brain, suggesting a significant role in cell differentiation via association with cell polarity machinery. FRMPD4 contains a WW domain, a PDZ domain, and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
FMPNVLKVYLENGQTKSFRFDCSTSIKDVILTLQEKLSIKCIEHFSLMLEQRTEGSGTKLLLLHEQETLT
QVTQRPGSHKMRCLFRISFVPKDP
>gnl|CDD|340691 cd17171, FERM_F0_TLN1, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-1 (TLN1). TLN1 is a cytoskeletal protein that plays a pivotal role in regulating the activity of the integrin family of cell adhesion proteins by coupling them to F-actin. It functions as a focal adhesion protein involved in the attachment of the bacterium. It binds to multiple adhesion molecules, including integrins, vinculin, focal adhesion kinase (FAK), and actin. TLN1 also plays an essential role in integrin activation. TLN1 interacts with the hepatitis B virus (HBV) accessory protein X (HBx), which induces the degradation of TLN1. It also acts as an adaptor protein that regulates leukocyte function-associated antigen-1 (LFA-1) affinity. In addition, TLN1 is required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions. TLN1 consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F0 domain
VALSLKISIGNVVKTMQFEPSTMVYDACRMIRERVPEAQAGQPNDFGLFLSDDDPKKGIWLEAGKALDYY
MLRNGDTMEYRKKQ
>gnl|CDD|340692 cd17172, FERM_F0_TLN2, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin-2 (TLN2). TLN2 is a cytoskeletal protein that plays an important role in cell adhesion and recycling of synaptic vesicles. TLN2 is required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions. TLN2 consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F0 domain
LSLKICVRQCNVVKTMQFEPSTAVYDACRIIRERVPEAQTGQASDYGLFLSDEDPRKGIWLEAGRTLDYY
MLRNGDVLEYKKKQ
>gnl|CDD|340693 cd17173, FERM_F1_TLN1, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-1 (TLN1). TLN1 is a cytoskeletal protein that plays a pivotal role in regulating the activity of the integrin family of cell adhesion proteins by coupling them to F-actin. It functions as a focal adhesion protein involved in the attachment of the bacterium. It binds to multiple adhesion molecules, including integrins, vinculin, focal adhesion kinase (FAK), and actin. TLN1 also plays an essential role in integrin activation. TLN1 interacts with the hepatitis B virus (HBV) accessory protein X (HBx), which induces the degradation of TLN1. It also acts as an adaptor protein that regulates leukocyte function-associated antigen-1 (LFA-1) affinity. In addition, TLN1 is required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions. TLN1 consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F1 domain
RPLKIRMLDGTVKTVMVDDSKTVTDMLMTICARIGITNHDEYSLVREIMEEKKEEVTGTLKKDKTLLRDD
KKMEKLKQKLHTDDELNWLDHGRTLREQGVEEHETLLLRRKF
>gnl|CDD|340694 cd17174, FERM_F1_TLN2, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin-2 (TLN2). TLN2 is a cytoskeletal protein that plays an important role in cell adhesion and recycling of synaptic vesicles. TLN2 is required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions. TLN2 consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F1 domain
RPQKIRMLDGAVKTIMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDE
RKMEKLKAKLHTDDDLNWLDHSRTFREQGVDENETLLLRRKF
>gnl|CDD|340695 cd17175, FERM_F0_SHANK1, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ankyrin repeat domains protein 1 (SHANK1). SHANK1, also termed somatostatin receptor-interacting protein, or SSTR-interacting protein (SSTRIP), is a postsynaptic density (PSD)-associated scaffolding proteins at the excitatory synapse that interconnects neurotransmitter receptors and cell adhesion molecules by direct and indirect interactions with numerous other PSD-associated proteins. Mutations in the SHANK1 synaptic scaffolding gene may lead to autism spectrum disorder and mental retardation. SHANK1 contains an N-terminal F0 domain of FERM (Band 4.1, ezrin, radixin, moesin), six ankyrin (ANK) repeats, one SH3 (Src homology 3) domain, one PDZ (PSD-95, Dlg, and ZO-1/2, also termed DHR or GLGF) domain, and a C-terminal SAM (sterile alpha motif) domain. This family corresponds to the F0 domain that adopts a ubiquitin-like fold
FSMMVFRIGIPDLHQTKCLRFNPDATIWVAKQQVLCTLNESLKDVLNYGLFQPATNGRDAKFLEEERLLR
EYPQSFEKGVPYLEFRYKT
>gnl|CDD|340696 cd17176, FERM_F0_SHANK2, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ankyrin repeat domains protein 2 (SHANK2). SHANK2, also termed cortactin-binding protein 1 (CortBP1), or proline-rich synapse-associated protein 1, is a postsynaptic density (PSD)-associated scaffolding proteins at the excitatory synapse that interconnects neurotransmitter receptors and cell adhesion molecules by direct and indirect interactions with numerous other PSD-associated proteins. It is strongly expressed in the cerebellum. Moreover, SHANK2 acts as a component of the albumin endocytic pathway in podocytes, and regulates renal albumin endocytosis. It also associates with and regulates Na+/H+ exchanger 3 (NHE3) and is involved in the fine regulation of transepithelial salt and water transport through affecting NHE3 expression and activity. Mutations in the SHANK2 synaptic scaffolding gene may lead to autism spectrum disorder and mental retardation. SHANK2 contains an N-terminal F0 domain of FERM (Band 4.1, ezrin, radixin, moesin), six ankyrin (ANK) repeats, one SH3 (Src homology 3) domain, one PDZ (PSD-95, Dlg, and ZO-1/2, also termed DHR or GLGF) domain, and a C-terminal SAM (sterile alpha motif) domain. This family corresponds to the F0 domain that adopts a ubiquitin-like fold
NTLVIRIIIPDLQQTKCIRFNPDATVWVAKQRILCTLNQSLKDVLNYGLFQPASNGRDGKFLDEERLLRE
YPQPVNKGVPSLEFRYKK
>gnl|CDD|340697 cd17177, FERM_F0_SHANK3, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ankyrin repeat domains protein 3 (SHANK3). SHANK3, also termed proline-rich synapse-associated protein 2 (ProSAP2), is a postsynaptic density (PSD)-associated scaffolding protein at the excitatory synapse that interconnects neurotransmitter receptors and cell adhesion molecules by direct and indirect interactions with numerous other PSD-associated proteins. It is critical for synaptic plasticity and the trans-synaptic coupling between the reliability of presynaptic neurotransmitter release and postsynaptic responsiveness. It is a key component of a zinc-sensitive signaling system that regulates excitatory synaptic strength. Mutations in the SHANK3 synaptic scaffolding gene may lead to autism spectrum disorder and mental retardation, and the cause of human Phelan-McDermid syndrome (22q13.3 deletion syndrome) has been isolated to loss of function of one copy of the SHANK3 gene. SHANK3 contains an N-terminal F0 domain of FERM (Band 4.1, ezrin, radixin, moesin), six ankyrin (ANK) repeats, one SH3 (Src homology 3) domain, one PDZ (PSD-95, Dlg, and ZO-1/2, also known as DHR or GLGF) domain, and a C-terminal SAM (sterile alpha motif) domain. This family corresponds to the F0 domain that adopts a ubiquitin-like fold
ALVVRIGIPDLQQTKCLRLNPDAPVWASKQRILCTLNHSLKDVLNYGLFQPAFNGRAGKFLDEERLLREY
PLPLDTPVPYLEFRYKR
>gnl|CDD|340698 cd17178, FERM_F1_PLEKHH1, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin homology domain-containing family H member 1 (PLEKHH1). PLEKHH1 is a homolog of Caenorhabditis elegans MAX-1 that has been implicated in motor neuron axon guidance. PLEKHH1 is critical in vascular patterning in vertebrate species through acting upstream of the ephrin pathway. PLEKHH1 contains a putative alpha-helical coiled-coil segment within the N-terminal half, and two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
PFSIPVHFMNGTYQVVGFDGSTTVDEFLQTLNQETGMRKPSHSGFALFTDDPSGKDLEHCLQGSVKICDV
ISKWEQALKELHPGKYEGTRTVRLTYKSRLYFRAQA
>gnl|CDD|340699 cd17179, FERM_F1_PLEKHH2, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin homology domain-containing family H member 2 (PLEKHH2). PLEKHH2 is a novel podocyte protein downregulated in human focal segmental glomerulosclerosis. It is highly enriched in renal glomerular podocytes, and acts as a novel, important component of the podocyte foot processes. PLEKHH2 contains a putative alpha-helical coiled-coil segment within the N-terminal half, and two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PLEKHH2 is involved in matrix adhesion and actin dynamics. It directly interacts through its FERM domain with the focal adhesion protein Hic-5 and actin
PFSIPVHFMNGTYQVVGFDASTTVEEFLNTLNQDTGMRKPGQSGFALFTDDPSGKDLEHCLQGNIKICDI
ISKWEQASKEQHPGKCEGTRTVRLTYKNRLYFS
>gnl|CDD|340700 cd17180, FERM_F0_KIND1, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in kindlin-1 (KIND1). KIND1, also termed Kindlerin, or Kindler syndrome protein, or fermitin family homolog 1 (FERMT1), or Unc-112-related protein 1 (URP1), is an integrin-interacting protein that has been implicated in cell adhesion, proliferation, polarity, and motility. It is essential for maintaining the structure of cell-matrix adhesion, such as focal adhesions and podosomes. KIND1 is expressed primarily in epithelial cells. Loss or mutations of KIND1 gene may cause the Kindler syndrome (KS), an autosomal recessive skin disorder with an intriguing progressive phenotype comprising skin blistering, photosensitivity, progressive poikiloderma with extensive skin atrophy, and propensity to skin cancer. KIND1 forms a molecular complex with the key transforming growth factor (TGF)-beta/Smad3 signaling components including type I TGFbeta receptor (TbetaRI), Smad3 and Smad anchor for receptor activation (SARA) to control the activation of TGF-beta/Smad3 signaling pathway. KIND1 consists of an atypical FERM domain that is made up of F1, F2 and F3 domains, as well as an N-terminal region, which precedes the FERM domain and has been referred to as the F0 domain. This family corresponds to the F0 domain
SWELSVRVDHQNGEEQKEFTLRVSGDLHIGGVMLKLVEQINVAQDWSDYALWWEQKNCWLLKTHWTLDKY
GVQADAKLLFTPQH
>gnl|CDD|340701 cd17181, FERM_F0_KIND2, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in kindlin-2 (KIND2). KIND2, also termed fermitin family homolog 2 (FERMT2), or mitogen-inducible gene 2 protein (MIG-2), or Pleckstrin homology (PH) domain-containing family C member 1, is an adaptor protein that is widely distributed and is particularly abundant in adherent cells. It binds to the integrin beta cytoplasmic tail to promote integrin activation. It promotes carcinogenesis through regulation of cell-cell and cell-extracellular matrix adhesion. In additon, KIND2 plays an important role in cardiac development. KIND2 consists of an atypical FERM domain that is made up of F1, F2 and F3 domains, as well as an N-terminal region, which precedes the FERM domain and has been referred to as the F0 domain. This family corresponds to the F0 domain
TWELNVHVTDLNRDVTLRVTGEVHIGGVMLKLVEKLDVKKDWSDHALWWEKKKTWLLKTHWTLDKYGIQA
DAKLQFTPQH
>gnl|CDD|340702 cd17182, FERM_F0_KIND3, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in kindlin-3 (KIND3). KIND3, also termed fermitin family homolog 3 (FERMT3), or MIG2-like protein, or Unc-112-related protein 2, is an adaptor protein that expressed primarily in hematopoietic cells. It plays a central role in cell adhesion in hematopoietic cells, and also promotes integrin activation, clustering and outside-in signaling. KIND3, together with talin-1, contributes essentially to the activation of beta2-integrins in neutrophils. In addition, KIND3 interacts with the ribosome and regulates c-Myc expression required for proliferation of chronic myeloid leukemia cells. Mutations in the KIND3 gene cause leukocyte adhesion deficiency type III (LAD III), which is characterized by high susceptibility to infections, spontaneous and episodic bleedings, and osteopetrosis. KIND3 consists of an atypical FERM domain that is made up of F1, F2 and F3 domains, as well as an N-terminal region, which precedes the FERM domain and has been referred to as the F0 domain. This family corresponds to the F0 domain
SWELRVTVEELGPEAEPVTLRVTGDTHIGGVILKIVEKIMIKQDWSDHALWWEQKRQWLLKTNWTLDKYG
VLADARLVFTPQH
>gnl|CDD|340703 cd17183, FERM_F1_KIND1, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-1 (KIND1). KIND1, also termed Kindlerin, or Kindler syndrome protein, or fermitin family homolog 1 (FERMT1), or Unc-112-related protein 1 (URP1), is an integrin-interacting protein that has been implicated in cell adhesion, proliferation, polarity, and motility. It is essential for maintaining the structure of cell-matrix adhesion, such as focal adhesions and podosomes. KIND1 is expressed primarily in epithelial cells. Loss or mutations of KIND1 gene may cause the Kindler syndrome (KS), an autosomal recessive skin disorder with an intriguing progressive phenotype comprising skin blistering, photosensitivity, progressive poikiloderma with extensive skin atrophy, and propensity to skin cancer. KIND1 forms a molecular complex with the key transforming growth factor (TGF)-beta/Smad3 signaling components including type I TGFbeta receptor (TbetaRI), Smad3 and Smad anchor for receptor activation (SARA) to control the activation of TGF-beta/Smad3 signaling pathway. KIND1 consists of an atypical FERM domain that is made up of F1, F2 and F3 domains, as well as an N-terminal region, which precedes the FERM domain and has been referred to as the F0 domain. This family corresponds to the F1 domain
KLLRLQLPNMKTVRLKVSFSAVVFKAVSDICKTLNIRRSEELSLLKPSLAKMYQPRTLLDKAKLNAGWLD
SSRSLMEQGIQEDDQLLLRFKYY
>gnl|CDD|340704 cd17184, FERM_F1_KIND2, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-2 (KIND2). KIND2, also termed fermitin family homolog 2 (FERMT2), or mitogen-inducible gene 2 protein (MIG-2), or Pleckstrin homology (PH) domain-containing family C member 1, is an adaptor protein that is widely distributed and is particularly abundant in adherent cells. It binds to the integrin beta cytoplasmic tail to promote integrin activation. It promotes carcinogenesis through regulation of cell-cell and cell-extracellular matrix adhesion. KIND2 also plays an important role in cardiac development. KIND2 consists of an atypical FERM domain that is made up of F1, F2 and F3 domains, as well as an N-terminal region, which precedes the FERM domain and has been referred to as the F0 domain. This family corresponds to the F1 domain
KLLRLQLPNMKYVKVKVNFSDRVFKAVSDICKTFNIRHPEELSLLRKPRDPTKKKKLAKMYKPQSLLDKA
KINQGWLDSSRSLMEQDVKENEALLLRFKYY
>gnl|CDD|340705 cd17185, FERM_F1_KIND3, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-3 (KIND3). KIND3, also termed fermitin family homolog 3 (FERMT3), or MIG2-like protein, or Unc-112-related protein 2, is an adaptor protein that expressed primarily in hematopoietic cells. It plays a central role in cell adhesion in hematopoietic cells, and also promotes integrin activation, clustering and outside-in signaling. KIND3, together with talin-1, contributes essentially to the activation of beta2-integrins in neutrophils. In addition, KIND3 interacts with the ribosome and regulates c-Myc expression required for proliferation of chronic myeloid leukemia cells. Mutations in the KIND3 gene cause leukocyte adhesion deficiency type III (LAD III), which is characterized by high susceptibility to infections, spontaneous and episodic bleedings, and osteopetrosis. KIND3 consists of an atypical FERM domain that is made up of F1, F2 and F3 domains, as well as an N-terminal region, which precedes the FERM domain and has been referred to as the F0 domain. This family corresponds to the F1 domain
KPVILSLPNRRSLRIRACFSSPVFRAVAGICRVLSIRHPEELSLLRAPKLYRPSSVTDKTQIHSRWLDSS
RSLMQQGVQEGDRLWLRFKYY
>gnl|CDD|340706 cd17186, FERM_F1_Merlin, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and similar proteins. Merlin, also termed moesin-ezrin-radixin-like protein, or neurofibromin-2 (NF2), or Schwannomerlin, or Schwannomin, is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif, merlin however lacks the typical actin-binding motif in the C-tail. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Merlin plays vital roles in controlling proper development of organ sizes by specifically binding to a large number of target proteins localized both in cytoplasm and nuclei. Merlin may function as a tumor suppressor that functions upstream of the core Hippo pathway kinases Lats1/2 (Wts in Drosophila) and Mst1/2 (Hpo in Drosophila), as well as the nuclear E3 ubiquitin ligase DDB1-and-Cullin 4-associated Factor 1 (DCAF1)-associated cullin 4-Roc1 ligase, CRL4(DCAF1). Merlin may also has a tumor suppressor function in melanoma cells, the inhibition of the proto-oncogenic Na(+)/H(+) exchanger isoform 1 (NHE1) activity
KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDSKGTVAWLKMDKKVLDQDVPK
EEPVTFHFLAKFYPE
>gnl|CDD|340707 cd17187, FERM_F1_ERM, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family proteins, Ezrin, Radixin, and Moesin. The ezrin-radixin-moesin (ERM) family includes a group of closely related cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. They exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
VNVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVDSKGYSTWLKLNKKVLSQDVKKEN
PLQFKFRAKFYPE
>gnl|CDD|340708 cd17188, FERM_F1_FRMD7, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 7 (FRMD7). FRMD7 plays an important role in neuronal development and is involved in the regulation of F-actin, neurofilament, and microtubule dynamics. It interacts with the Rho GTPase regulator, RhoGDIalpha, and activates the Rho subfamily member Rac1, which regulates reorganization of actin filaments and controls neuronal outgrowth. Mutations in the FRMD7 gene are responsible for the X-linked idiopathic congenital nystagmus (ICN), a disease which affects ocular motor control. FRMD7 contains a FERM domain, and a pleckstrin homology (PH) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
MLHLKVQFLDDSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLEFRNHAGNNVWLELLKPITKQIKNP
KELIFKFTVKFFPVDP
>gnl|CDD|340709 cd17189, FERM_F1_FARP1, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF and pleckstrin domain-containing protein 1 (FARP1). FARP1, also termed chondrocyte-derived ezrin-like protein (CDEP), or pleckstrin homology (PH) domain-containing family C member 2 (PLEKHC2), is a neuronal activator of the RhoA GTPase. It promotes outgrowth of developing motor neuron dendrites. It also regulates excitatory synapse formation and morphology, as well as activates the GTPase Rac1 to promote F-actin assembly. As a novel downstream signaling partner of Rif, FARP1 is involved in the regulation of semaphorin signaling in neurons. FARP1 contains a FERM domain, a Dbl-homology (DH) domain and two pleckstrin homology (PH) domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
VPIKVQMLDDTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDHRKVMVWLDLLKPIVKQIRRPK
HVVLRFVVKFFPPDH
>gnl|CDD|340710 cd17190, FERM_F1_FARP2, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF and pleckstrin domain-containing protein 2 (FARP2) and similar proteins. FARP2, also termed FERM domain including RhoGEF (FIR), or Pleckstrin homology (PH) domain-containing family C member 3, is a Dbl-family guanine nucleotide exchange factor (GEF) that activates Rac1 or Cdc42 in response to upstream signals, suggesting roles in regulating processes such as neuronal axon guidance and bone homeostasis. It is also a key molecule involved in the response of neuronal growth cones to class-3 semaphorins. FARP2 contains a FERM domain, a Dbl-homology (DH) domain and two pleckstrin homology (PH) domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
LQLRVKLLDNTTEPLEIEPKADGQALLSQVFKRLNLVESDYFGLEFQNSQSNWIWLEPMKLIVKQVRRPK
NTKLRLAVKFFPPDP
>gnl|CDD|340711 cd17191, FERM_F1_PTPN14, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 14 (PTPN14) and similar proteins. PTPN14, also termed protein-tyrosine phosphatase pez, or PTPD2, or PTP36, is a widely expressed non-transmembrane cytosolic protein tyrosine phosphatase (PTP). It belongs to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. It forms a complex with Kibra and LATS1 proteins and negatively regulates the key Hippo pathway protein Yes-associated protein (YAP) oncogenic function by controlling its localization. It specifically regulates p130 Crk-associated substrate (p130Cas) phosphorylation at tyrosine residue 128 (Y128) in colorectal cancer (CRC) cells. Moreover, PTPN14 may be a critical enzyme in regulating endothelial cell function. It plays a crucial role in organogenesis by inducing transforming growth factor beta (TGFbeta) and epithelial-mesenchymal transition (EMT). It also acts as a modifier of angiogenesis and hereditary haemorrhagic telangiectasia. It regulates the lymphatic function and choanal development through the interaction with the vascular endothelial growth factor receptor 3 (VEGFR3), a receptor tyrosine kinase essential for lymphangiogenesis. Furthermore, PTPN14 functions as a regulator of cell motility through its action on cell-cell adhesion. Beta-Catenin, a central component of adherens junctions, has been identified as a PTPN14 substrate. PTPN14 works as a novel sperm-motility biomarker and a potential mitochondrial protein
KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKQLD
KFANEPLLFFGVMFYVP
>gnl|CDD|340712 cd17192, FERM_F1_PTPN21, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and similar proteins. PTPN21, also termed protein-tyrosine phosphatase D1 (PTPD1), is a cytosolic non-receptor protein-tyrosine phosphatase (PTP) that belongs to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation. It also associates with and activates Src tyrosine kinase, and directs epidermal growth factor (EGF)/Src signaling to the nucleus through activating ERK1/2- and Elk1-dependent gene transcription. PTPD1-Src complex interacts a protein kinase A-anchoring protein AKAP121 to forms a PTPD1-Src-AKAP121 complex, which is required for efficient maintenance of mitochondrial membrane potential and ATP oxidative synthesis. As a novel component of the endocytic pathway, PTPN21 supports EGF receptor stability and mitogenic signaling in bladder cancer cells. Moreover, PTPD1 regulates focal adhesion kinase (FAK) autophosphorylation and cell migration through modulating Src-FAK signaling at adhesion sites
KSCLVARIQLLNNEFVEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQNQQRWVDLEKPLKKQLD
KYALEPTVYFGVVFYVP
>gnl|CDD|340713 cd17193, FERM_F1_PTPN3, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 3 (PTPN3). PTPN3, also termed protein-tyrosine phosphatase H1 (PTP-H1), belongs to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN3 associates with the mitogen-activated protein kinase p38gamma (also known as MAPK12) to form a PTPN3-p38gamma complex that promotes Ras-induced oncogenesis. It may also act as a tumor suppressor in lung cancer through its modulation of epidermal growth factor receptor (EGFR) signaling. Moreover, PTPN3 shows sensitizing effect to anti-estrogens. It dephosphorylates the tyrosine kinase EGFR, disrupts its interaction with the nuclear estrogen receptor, and increases breast cancer sensitivity to small molecule tyrosine kinase inhibitors (TKIs). It also cooperates with vitamin D receptor to stimulate breast cancer growth through their mutual stabilization
EVICNVHFLDGSVQSFKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSVDSPRWLEPSKPIRKQLKG
GFPCSLHFRVRFFI
>gnl|CDD|340714 cd17194, FERM_F1_PTPN4, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 4 (PTPN4). PTPN4, also termed protein-tyrosine phosphatase MEG1 (MEG) or PTPase-MEG1, belongs to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN4 protects cells against apoptosis. It associates with the mitogen-activated protein kinase p38gamma (also known as MAPK12) to form a PTPN4-p38gamma complex that promotes cellular signaling, preventing cell death induction. It also inhibits tyrosine phosphorylation and subsequent cytoplasm translocation of TRIF-related adaptor molecule (TRAM, also known as TICAM2), resulting in the disturbance of TRAM-TRIF interaction. Moreover, PTPN4 negatively regulates cell proliferation and motility through dephosphorylation of CrkI
EVVCNILLLDNTVQAFKVNKHDQGQVLLDLVFKHLDLTERDYFGLQLADDSTDNPRWLDPNKPIRKQLKR
GSPHNLNFRVKFFV
>gnl|CDD|340715 cd17195, FERM_F1_PTPN13, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 13 (PTPN13). PTPN13, also termed Fas-associated protein-tyrosine phosphatase 1 (FAP-1), or PTP-BAS, or protein-tyrosine phosphatase 1E (PTP-E1 or PTPE1), or protein-tyrosine phosphatase PTPL1, belongs to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a KIND domain, a FERM domain, five PDZ domains, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN13 interacts with a variety of ligands, suggests an important role as a scaffolding protein. It is also involved in the regulation of apoptosis, cytokinesis and cell cycle progression
RRKVNIMLLSGQRLELTCDTKSTCKDVFDMVVAHIGLVEHHLFALAYLKDNEFFFVDPDLKLSKVAPEGW
KEEPKKKNKMTVNFTLFFRIKFFVDD
>gnl|CDD|340716 cd17196, FERM_F1_FRMPD2, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 2 (FRMPD2). FRMPD2, also termed PDZ domain-containing protein 4 (PDZK4), or PDZ domain-containing protein 5C (PDZD5C), is a potential scaffold protein involved in basolateral membrane targeting in epithelial cells. It interacts with nucleotide-binding oligomerization domain-2 (NOD2) through leucine-rich repeats and forms a complex with the membrane-associated protein ERBB2IP. FRMPD2 contains an N-terminal KIND domain, a FERM domain and three PDZ domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
QRELNVIMPNGQCLEVKCDIKSRVRDVFNMVVAFANLVEHFYFGLAYMKGKEFFFLDHETKLHKVAPEGW
KDQSKKKTSIVNFTLFLRIKFFVDN
>gnl|CDD|340717 cd17197, FERM_F1_FRMD1, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 1 (FRMD1). FRMD1 is an uncharacterized FERM domain-containing protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
HRSICVLLPNKEQLSLTVGVKATGQELFQQVCELLKIKEAHFFGLSVVKNNEHIFMDLEQKLSKYFPKEW
KKETGKGTEKFSIPFVACFRVQYYVENG
>gnl|CDD|340718 cd17198, FERM_F1_FRMD6, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 6 (FRMD6). FRMD6, also termed willin, expanded or expanded homolog, is a FERM domain-containing protein that plays a critical role in regulating both cell proliferation and apoptosis. It acts as a tumor suppressor of human breast cancer cells independently of the Hippo pathway. It also inhibits human glioblastoma growth and progression by negatively regulating activity of receptor tyrosine kinases. As an upstream component of the hippo signaling pathway, FRMD6 orchestrates mammalian peripheral nerve fibroblasts. FRMD6 contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
RRSVCVFLPNDETLNIIVNVKTLCQELLVQVCDLLRLKDCHLFGLSVIQNNEHVYMELSQKLYKYCPKEW
KKEASKGIDQFGPPMIVHFRVQYYVENG
>gnl|CDD|340719 cd17199, FERM_F1_FRMD4A, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 4A (FRMD4A). FRMD4A is a cytohesin adaptor involved in cell structure, transport and signaling. It promotes the growth of cancer cells in tongue, head and neck squamous cell carcinomas. It also regulates tau secretion by activating cytohesin-Arf6 signaling through connecting cytohesin family Arf6-specific guanine-nucleotide exchange factors (GEFs) and Par-3 at primordial adherens junctions during epithelial polarization. As a genetic risk factor for late-onset Alzheimer's disease (AD), FRMD4A may play a role in amyloidogenic and tau-related pathways in AD. FRMD4A contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
EGRRCQVHLLDDRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGHLNWLQLDRRVLEHDFP
KKSGPVVLYFCVRFYIESI
>gnl|CDD|340720 cd17200, FERM_F1_FRMD4B, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 4B (FRMD4B). FRMD4B, also termed GRP1-binding protein GRSP1, interacts with the coil-coil domain of ARF exchange factor GRP1 to form the Grsp1-Grp1 complex that co-localizes with cortical actin rich regions in response to stimulation of CHO-T cells with insulin or epidermal growth factor (EGF). FRMD4B contains a FERM protein interaction domain as well as two coiled coil domains and may therefore function as a scaffolding protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
EGRHCQVHLLDDRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQSNWLQLDHRVLDHDLP
KKSGPVTLYFAVRFYIESI
>gnl|CDD|340721 cd17201, FERM_F1_EPB41L1, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 1 (EPB41L1) and similar proteins. EPB41L1, also termed neuronal protein 4.1 (4.1N), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. It is a cytoskeleton-associated protein that may serve as a tumor suppressor in solid tumors. It suppresses hypoxia-induced epithelial-mesenchymal transition in epithelial ovarian cancer (EOC) cells. The down-regulation of EPB41L1 expression is a critical step for non-small cell lung cancer (NSCLC) development. Moreover, EPB41L1 functions as a linker protein between inositol 1,4,5-trisphosphate receptor type1 (IP3R1) and actin filaments in neurons. EPB41L1 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
SAICKVTLLDGSEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKNWLDPSKEIKKQIRSG
PWHFAFTVKFYPPD
>gnl|CDD|340722 cd17202, FERM_F1_EPB41L2, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 2 (EPB41L2) and similar proteins. EPB41L2, also termed generally expressed protein 4.1 (4.1G), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L2 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
TVLCKVTLLDGTEYSCDLEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSANQKNWLDSTKEIKRQIRRL
PWLFTFNVKFYPPD
>gnl|CDD|340723 cd17203, FERM_F1_EPB41L3, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 3 (EPB41L3) and similar proteins. EPB41L3, also termed 4.1B, or differentially expressed in adenocarcinoma of the lung protein 1 (DAL-1), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L3 is a tumor suppressor that has been implicated in a variety of meningiomas and carcinomas. EPB41L3 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
NMQCKVTLLDGSEYTCEVEKRSKGQVLFDKVCEHLNLLEKDYFGLTYRDSENQKNWLDPAKEIKKQIRSG
AWQFSFNVKFYPPD
>gnl|CDD|340724 cd17204, FERM_F1_EPB41L4B, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band 4.1-like protein 4B (EPB41L4B). EPB41L4B, also termed FERM-containing protein CG1, or expressed in high metastatic cells (Ehm2), or Lulu2, is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). EPB41L4B is a positive regulator of keratinocyte adhesion and motility, suggesting a role in wound healing. It also promotes cancer metastasis in melanoma, prostate cancer and breast cancer
LTCRVLLLDGTDVSVELPKHAKGQDLFDQIVYHLDLVETDYFGLQFMDAAQVAHWLDHTKPIKKQIKIGP
PYTLHFRIKYYSSE
>gnl|CDD|340725 cd17205, FERM_F1_EPB41L5, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like 5 (EPB41L5). EPB41L5 is a mesenchymal-specific protein that is an integral component of the ARF6-based pathway. It is normally induced during epithelial-mesenchymal transition (EMT) by an EMT-related transcriptional factor, ZEB1, which drives ARF6-based invasion, metastasis and drug resistance. EPB41L5 also binds to paxillin to enhance integrin/paxillin association, and thus promotes focal adhesion dynamics. Moreover, EPB41L5 acts as a substrate for the E3 ubiquitin ligase Mind bomb 1 (Mib1), which is essential for activation of Notch signaling. EPB41L5 is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
SIITCRVSLLDGTDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDSAQVAHWLDVTKSIKKQVKI
GPPYCLHLRVKFYSSE
>gnl|CDD|340726 cd17206, FERM_F1_Myosin-X, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional myosin-X. Myosin-X, also termed myosin-10 (Myo10), is an untraditional member of myosin superfamily. It is an actin-based motor protein that plays a critical role in diverse cellular motile events, such as filopodia formation/extension, phagocytosis, cell migration, and mitotic spindle maintenance, as well as a number of disease states including cancer metastasis and pathogen infection. Myosin-X functions as an important regulator of cytoskeleton that modulates cell motilities in many different cellular contexts. It regulates neuronal radial migration through interacting with N-cadherin. Like other unconventional myosins, Myosin-X is composed of a conserved motor head, a neck region and a variable tail. The neck region consists of three IQ motifs (light chain-binding sites), and a predicted stalk of coiled coil. The tail contains three PEST regions, three PH domains, a MyTH4 domain, and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
RREMTATVYCYGGGSCKITINSHTTAGEVVEKLIRGLALEDSRNMFALFEHNGTTDKAIESRTVVADVLA
KFEKLAAEGEMEGGLPWKLYFKLFCFL
>gnl|CDD|340727 cd17207, FERM_F1_PLEKHH3, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin homology domain-containing family H member 3 (PLEKHH3). PLEKHH3 is an uncharacterized Pleckstrin homology (PH) domain-containing protein that shows high sequence similarity with unconventional myosin-X, an actin-based motor protein that plays a critical role in diverse cellular motile events, such as filopodia formation/extension, phagocytosis, cell migration, and mitotic spindle maintenance, as well as a number of disease states including cancer metastasis and pathogen infection. In addition to two PH domains, PLEKHH3 harbors a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
RQELLCTVHCPGAGACSIAITSHTTAEEVVRELVGRLGLSDSRNIFALYEQNGQEEQAIGSSTIVADVLT
RFENLAAEEKEPDPQWRLCFKLYCFL
>gnl|CDD|340728 cd17208, FERM_F1_DdMyo7_like, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium discoideum Myosin-VIIa (DdMyo7) and similar proteins. DdMyo7, also termed Myosin-I heavy chain, or class VII unconventional myosin, or M7, plays a role in adhesion in Dictyostelium where it is a component of a complex of proteins that serve to link membrane receptors to the underlying actin cytoskeleton. It interacts with talinA, an actin-binding protein with a known role in cell-substrate adhesion. DdMyo7 is required for phagocytosis. It is also essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin. Members in this family contain a myosin motor domain, two MyTH4 domains, two FERM (Band 4.1, ezrin, radixin, moesin) domains, and two Pleckstrin homology (PH) domains. Some family members contain an extra SH3 domain. Each FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N)
RRPIVARFYFLDGQFKALEFDSAATAAEVLEQLKQKIGLRSTADGFALYEVFGGIERAILPEEKVADVLS
KWEKLQRTMASCAAQQAVKFVFKKRLFF
>gnl|CDD|340729 cd17209, RA_RalGDS, Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) and similar proteins. RalGDS, also termed Ral guanine nucleotide exchange factor (RalGEF), is a guanine exchange factor (GEF) for the Ral family of small GTPases. It is the prototype of RalGDS family proteins that are involved in Ras and Ral signaling pathways as downstream effector proteins. RalGDS stimulates the dissociation of GDP from the Ras-related RalA and RalB GTPases which allows GTP binding and activation of the GTPases. It interacts and acts as an effector molecule for R-Ras, H-Ras, K-Ras, and Rap. Moreover, RalGDS functions as a novel interacting partner for Rab7-interacting lysosomal protein (RILP), a key regulator for late endosomal/lysosomal trafficking. RILP suppresses invasion of breast cancer cells by inhibiting the GEF activity for RalA of RalGDS. RalGDS also plays a vital role in the regulation of Ral-dependent Weibel-Palade bodies (WPB) exocytosis from endothelial cells. In addition, RalGDS couples growth factor signaling to Akt activation by promoting PDK1-induced Akt phosphorylation. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair
DCCIIRVSLDVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDEEEPEDYELLQILSEDRELKIPDNANVF
YAMNSTANYDFVLKKR
>gnl|CDD|340730 cd17210, RA_RGL, Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 1 (RalGDS-like 1) and similar proteins. RalGDS-like 1 (RGL) is a Ral-specific guanine nucleotide exchange factor that belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. RGL has been identified as a possible effector protein of Ras. It also regulates c-fos promoter and the GDP/GTP exchange of Ral. Members in this family have similar structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair
EDTCIIRVSVEDNNGNMYKSIMLTSQDKTPAVIQRAMSKHNLESDPAEDYELVQVISEDRELVIPDNANV
FYAMNSSVNFDFILRKK
>gnl|CDD|340731 cd17211, RA_RGL2, Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 (RalGDS-like 2) and similar proteins. RalGDS-like 2 (RGL2), also termed RalGDS-like factor (RLF), or Ras-associated protein RAB2L, is a novel Ras and Rap 1A-associating protein that belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. RGL2 exhibits guanine nucleotide exchange activity towards the small GTPase Ral. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The RA domain of RGL2 is phosphorylated by protein kinase A and the phosphorylation affects the ability of RGL2 to bind both Ras and Rap1
SDCRIIRVRMELHDGSVYKSILVTSQDKTPAVISRALEKHNQSSQAASPYELVQLLPEGKELTIPPTANV
FYAMSSASLDFILRPR
>gnl|CDD|340732 cd17212, RA_RGL3, Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 3 (RalGDS-like 3) and similar proteins. RalGDS-like 3 (RGL3), also termed Ras pathway modulator (RPM), interacts in a GTP- and effector loop-dependent manner with Rit and Ras. As a novel potential effector of both p21 Ras and M-Ras, RGL3 negatively regulates Elk-1-dependent gene induction downstream of p21 Ras or mitogen activated protein/extracellular signal regulated kinase Kinase 1 (MEKK1). It also functions as a potential binding partner for Rap-family small G-proteins and profilin II. RGL3 belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier (Ubiquitination) in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair
SEARVIRVSIDNDHGNLYRSILLTSQDKAPSVVQRALQKHNVPQPWARDYQLFQVLPGDRELLIPDNANV
FYAMSPAAPGDFMLRRK
>gnl|CDD|340733 cd17213, RA_PHLPP, Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein phosphatase PHLPP1, PHLPP2, and similar proteins. PHLPP represents a novel family of Ser/Thr protein phosphatases, which is involved in two key signaling pathways, the phosphatidylinositol 3-kinase and diacylglycerol signaling pathways, by directly dephosphorylating and inactivating Akt serine-threonine kinases (Akt1, Akt2, Akt3) and protein kinase C (PKC) isoforms. PHLPP targets oncogenic kinases and may act as a tumor suppressor in several types of cancers. Two PHLPP isoforms are included in this family, PHLPP1 and PHLPP2. They regulate Akt activation together when both phosphatases are expressed. PHLPP1 is also termed pleckstrin homology domain-containing family E member 1, or PH domain-containing family E member 1, or suprachiasmatic nucleus circadian oscillatory protein (SCOP). It plays a suppression role in inflammatory response of glioma. Its loss contributes to gliomas development and progression. Loss of PHLPP1 also protects against colitis by inhibiting intestinal epithelial cell apoptosis. The overexpression of PHLPP1 impairs hippocampus-dependent learning, suggesting a role for PHLPP1 in learning and memory. PHLPP2 is also termed PH domain leucine-rich repeat-containing protein phosphatase-like (PHLPP-like). Both PHLPP1 and PHLPP2 contain a putative Ras-associating (RA) domain followed by a pleckstrin homology (PH) domain, a series of leucine-rich repeats and a protein phosphatase 2C (PP2C) domain
GFIRVYDPDSPSDRSKLVPCTLETTAEDICKKLGISSLYLYVQLGGDHIRRLEPDERPLQIQNEFLASLG
YSDPSRIQREGTDPDLGHLIRFYAGRP
>gnl|CDD|340734 cd17214, RA_CYR1_like, Ras-associating (RA) domain found in Saccharomyces cerevisiae adenylate cyclase and similar proteins. CYR1, also termed ATP pyrophosphate-lyase, or adenylyl cyclase, is a fungal adenylate cyclase that regulates developmental processes such as hyphal growth, biofilm formation, and phenotypic switching. CYR1 plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP. It acts as a scaffold protein keeping Ras2 available for its regulatory factors, the Ira proteins. CYR1 has at least four domains, including an N-terminal adenylate cyclase G-alpha binding domain, a Ras-associating (RA) domain, a middle leucine-rich repeat region, and a catalytic domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The RA domain of CYR1 post-translationally modifies a small GTPase called Ras, which is involved in cellular signal transduction. CYR1 activity is stimulated directly by regulatory proteins (Ras1 and Gpa2), peptidoglycan fragments and carbon dioxide
YRIRVYRPDGTFHTLSCPLNTTTSELLSMLAKKFFLPDSANYRLYLRERGLERILRSNEKPLLIQKRLLL
QAGYTELDGLEEIGREDNSYLCRFIFRPP
>gnl|CDD|340735 cd17215, RA_Rin1, Ras-associating (RA) domain found in Ras and Rab interactor 1 (Rin1). Rin1, also termed Ras inhibitor JC99, or Ras interaction/interference protein 1, is a downstream Ras effector that represents a unique class of Ras effector connected to two independent signaling pathways. The first effector pathway is the direct activation of RAB5-mediated endocytosis and the second pathway involves direct activation of ABL tyrosine kinase activity. Rin1 functions as a guanine nucleotide exchange factor (GEF) for RAB5 GTPases. The RAB5 GEF activity of Rin1 promotes early endosome fusion, an early event in transit to the lysosome. Rin1 binds the SH3 and SH2 domains of ABL proteins, ABL1 and ABL2, and activates their tyrosine kinase activity. Rin1 contains SH2 and proline-rich domains in the N-terminal region, and RH, VPS9, and RA domains in the C-terminal region. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair
QNFLRVAYQDPSSGCTSKTLAVPPSATVADLNQLCATKFKVTQPETYGIFLYKEQGYQRLPPDALPQRIK
AQLKEKGSTFYFVYQRAE
>gnl|CDD|340736 cd17216, RA_Myosin-IXa, Ras-associating (RA) domain found in Myosin-IXa. Myosin-IXa, also termed myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Its RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function
EFTLRIYPGNIAEGTIYCPVPARKNTTAAEVIESLINKLQLDKTKCYVLAEVKEFGGEEWILNPTDCPVQ
RMMLWPRMALENRFSGEDYRFLLREK
>gnl|CDD|340737 cd17217, RA_Myosin-IXb, Ras-associating (RA) domain found in Myosin-IXb. Myosin-IXb, also termed myosin-9b (Myo9b), is a motor protein with a Rho GTPase activating domain (RhoGAP); it is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen and in several immune cells including dendritic cells, macrophages and CD4+ T. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a RhoGAP domain. Its RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells
VYALQIYPQLSAESSTCCIVLATKEATASDVIKDAVATLGLDSSKPYVLAEVKESGGEEWVLDANDSPVQ
RVLLWPRKAQDDHPQSDGYYFLLQER
>gnl|CDD|340738 cd17218, RA_RASSF1, Ras-associating (RA) domain found in Ras-association domain-containing protein 1 (RASSF1). RASSF1 is a member of a family of six related RASSF1-6 proteins (the classical RASSF proteins). RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. With the exception of some minor splice variants (RASSF1F and RASSF1G), RASSF1 contains an RA domain and a C-terminal SARAH protein-protein interaction motif. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases, and the SARAH domain mediates protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF1A and 1C are the most extensively studied RASSF1 with both localized to microtubules and involved in regulation of growth and migration
LSQAEIEQKIKEYNAQINSNLFMSLNKDGSYTGFIKVQLKLVRPVSVPANKKPSSIQDSRKGSGRSQPVK
RRTSFYLPKDTVKHLHISSKTRASEVIEALLKKFTVVDNPRKFALFERTEKDDQVYLRKLSDDEQPLYLR
LLAGPNEKTLSFVLKEN
>gnl|CDD|340739 cd17219, RA_RASSF3, Ras-associating (RA) domain found in Ras-association domain-containing protein 3 (RASSF3). RASSF3 is a member of a family of six related classical RASSF1-6 proteins (the classical RASSF proteins). RASSF3 has three transcripts (A-C) due to alternative splicing of the exons. The RASSF3B and 3C isoforms are shorter than RASSF3A, and unlike RASSF3A do not contain the RA or SARAH domains. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases, and the SARAH domain mediates protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF3A regulates apoptosis and cell cycle via p53 stabilization and possibly is involved in DNA repair
KEEIKQKIQLYNLAVTDKLKMTLNSSGIYTGFIKVQMDLRRPITVRGGAAGNNNNETAFYLPKGSVNTLH
ISSTNTVREVIEALLKKFLVADNPAKFALYKRCHKEDQVYACKLSDREHPLYLRLVAGPNTDTLSFVLRE
H
>gnl|CDD|340740 cd17220, RA_RASSF5, Ras-associating (RA) domain of Ras-association domain family 5 (RASSF5). RASSF5, also called New ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is a member of a family of six related RASSF1-6 proteins (the classical RASSF proteins) and is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. All transcripts variants of RASSF5 contain the RA or SARAH domains. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases, and the SARAH domain mediates protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion
TVEEIKQKIESYNTKVKNCLGMKLSPDGTYTGFIKVHLKLRRPVTVPAGIRPQSIYEVNPADTTDKRTSF
YLPLDAIKQLHISSTTTVSEVIQGLLKKFMVVDNPQKFALFKRMRKDGQVLFQKLPLTEYPLYLRLLAGP
DTDVLSFVLKEN
>gnl|CDD|340741 cd17221, RA_RASSF2, Ras-associating (RA) domain found in Ras-association domain-containing protein 2 (RASSF2). RASSF2 is a member of a family of six related classical RASSF1-6 proteins. The RASSF2 gene is transcribed into two major isoforms (A and C). RASSF2 is structurally related to RASSF1A but unlike RASSF1A It is primarily a nuclear protein. RASSF2 contains the RA and SARAH domains. The RA domain of the classical RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RA domains mediate interactions with Ras and other small GTPases, and SARAH domains mediate protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF2 is inactivated in different cancers and cancer cell lines by promoter methylation and loss of expression, implicating the correlation and significance of RASSF2 in tumorigenesis. In addition to regulating apoptosis and proliferation RASSF2 may have other functions as RASSF2 knockout mice develop normally for the first two weeks but then develop growth retardation and die 4 weeks after birth
NHKTSVFTPAYGSVTNVRINSTMTTPQVLKLLLNKFKIENSAEEFALYIVHTSGEKQKLKATDYPLIARI
LQGPCEQVSKVFLMEKD
>gnl|CDD|340742 cd17222, RA_RASSF4, Ras-associating (RA) domain found in Ras-association domain-containing protein 4 (RASSF4). RASSF4 is a member of a family of six related classical RASSF1-6 proteins and is broadly expressed in normal tissues. RASSF4 expression is reduced in tumor cell lines and primary tumors by promoter specific hypermethylation. RASSF4 contains the RA and SARAH domains. The RA domain of the classical RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RA domains mediate interactions with Ras and other small GTPases, and SARAH domains mediate protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF4 inhibits lung cancer cell proliferation and invasion
NHKTSVFTPAYGSVTNVRVNSTMTTPQVLKLLLNKFRVENSPDEFALYLVHESGERTKLKDTEYPLISRI
LHGPCEKIARIFLMETD
>gnl|CDD|340743 cd17223, RA_RASSF6, Ras-associating (RA) domain found in Ras-association domain-containing protein 6 (RASSF6). RASSF6 is a member of a family of six related classical RASSF1-6 proteins and is expressed as four transcripts via alternative splicing. All transcripts variant of RASSF6 contain the RA and SARAH domains. The RA domain of the classical RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RA domains mediate interactions with Ras and other small GTPases, SARAH domains mediate protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF6 is ubiquitiated and degraded by interacting with MDM2 to stabilize P53 and regulates apoptosis and cell cycle. RASSF6 is a tumor suppressor protein and is epigenetically silenced in childhood leukemia and neuroblastomas. Overexpression of RASSF6 causes apoptosis in HeLa cells
NYKTSVFTPAFGSETKVRINSNMTTQEVIKQLLQKFKIENSPNEFALYIIHATGEKKRLKNTDFPLWERL
LQGPSGKIAKMFLMDKD
>gnl|CDD|340744 cd17224, RA_ASPP1, Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 protein 1 (ASPP1). ASPP1 is a member of the ASPP protein family (Apoptosi-Stimulating Protein of p53) that activates the p53-mediated apoptotic response. ASSP1 functions as a tumor suppressor and coordinates with p53 to protect hematopoietic stem cell (HSC) pool integrity, guarding against hematological malignancies. ASSP1 contains a RA domain at the N-terminus. The RA domain is a ubiquitin-like domain and RA domain-containing proteins are involved in several different functions ranging from tumor suppression to being oncoproteins
MPMILTVFLSNNEQILTEVPITPETTCRDVVEFCKEPGETGCHLAEVWRGNERPIPYDHMMYEHLQKWGP
RREEVKFFLRHEDSP
>gnl|CDD|340745 cd17225, RA_ASPP2, Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 protein 2 (ASPP2). ASPP2, also termed Bcl2-binding protein (Bbp), or renal carcinoma antigen NY-REN-51, or tumor suppressor p53-binding protein 2 (53BP2), or p53-binding protein 2 (p53BP2), is a member of ASPP protein family and it functions as a tumor suppressor. ASPP2 binds to p53 and enhances p53-mediated transcription of proapoptotic genes. ASSP2 contains a RA domain at the N-terminus. The RA domain is a ubiquitin-like domain and RA domain-containing proteins are involved in several different functions ranging from tumor suppression to being oncoproteins. All p53 amino acids that are important for ASPP2 binding are mutated in human cancer, and ASPP2 is frequently downregulated in these tumor cells
MFLTVYLSNNEQHFTEVPITPETTCRDVVELCKEPGETDCHLAEVWRGSERPVADNERMLDVLQQWGAQR
NEVRFFLRHE
>gnl|CDD|340746 cd17226, RA_ARAP1, Ras-associating (RA) domain found in Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1 (ARAP1). ARAP1, also termed Centaurin-delta-2 (Cnt-d2), is a phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P(3))-dependent Arf Rap-activated guanosine triphosphatase (GTPase)-activating protein (GAP) that inhibits the trafficking of epidermal growth factor receptor (EGFR) to the early endosome. It associates with the Cbl-interacting protein of 85 kDa (CIN85), regulates endocytic trafficking of the EGFR, and thus affects ubiquitination of EGFR. It also regulates the ring size of circular dorsal ruffles through Arf1 and Arf5. ARAP1 contains multiple functional domains, including ArfGAP and RhoGAP domains, as well as a sterile alpha motif (Sam) domain, five PH domains, and a RA domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes
SPDFICTVYLEEKKEGSEQHVQVPASMTAEELTFEILDRRNIHTREKDYWSCFEVNEREEAERPLHFSEK
VLPIFHSLGSDSHLVVKKHCSME
>gnl|CDD|340747 cd17227, RA_ARAP2, Ras-associating (RA) domain found in Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 2 (ARAP2). ARAP2, also termed Centaurin-delta-1 (Cnt-d1), or Protein PARX, is a phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P(3))-dependent Arf Rap-activated guanosine triphosphatase (GTPase)-activating protein (GAP), which promotes GLUT1-mediated basal glucose uptake by modifying sphingolipid metabolism through glucosylceramide synthase (GCS). ARAP2 signals through Arf6 and Rac1 to control focal adhesion morphology. ARAP2 contains multiple functional domains, including ArfGAP and RhoGAP domains, as well as a sterile alpha motif (Sam) domain, five PH domains, and a RA domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes
AGDLLIEVYLEKKEPDCSIIIRVSPTMEAEELTNDVLEIKNIIPDKKDIWATFEVIENGELERPLHYKEN
VLEQVLQWSSLSEPGSAYLIVKRFQAAD
>gnl|CDD|340748 cd17228, RA_ARAP3, Ras-associating (RA) domain found in Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3 (ARAP3). ARAP3, also termed Centaurin-delta-3 (Cnt-d3), is a phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P(3))-dependent Arf Rap-activated guanosine triphosphatase (GTPase)-activating protein (GAP) that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members, ADP-ribosylation factor 6 (Arf6) and Ras homolog gene family member A (RhoA). It is regulated by phosphatidylinositol 3,4,5-trisphosphate and a small GTPase Rap1-GTP, and has been implicated in the regulation of cell shape and adhesion. ARAP3 contains multiple functional domains, including ArfGAP and RhoGAP domains, as well as a sterile alpha motif (Sam) domain, five PH domains, and a RA domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes
AGDLIIEVYLEQKLPDCCVTLKVSPTMTAEELTNQVLDMRNIAAASKDVWLTFEVIENGELERPLHPKEK
VLEQALQWCKLPEPSSAYLLVKKVPIGEG
>gnl|CDD|340749 cd17229, RA1_PLC-epsilon, Ras-associating (RA) domain 1 found in Phosphatidylinositide-specific phospholipase C (PLC)-epsilon. PLC is a signaling enzyme that hydrolyzes membrane phospholipids to generate inositol triphosphate. PLC-epsilon represents a novel forth class of PLC that has a PLC catalytic core domain, a CDC25 guanine nucleotide exchange factor domain and two RA (Ras-association) domains. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. Although PLC RA1 and RA2 have homologous ubiquitin-like folds only RA2 can bind Ras and activate it. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and involve in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. This family corresponds to the first RA domain of PLC-epsilon
ERKALQTHKVTVHGVPGPEPFTVFTISEGTTAKQLLQQILATEQGIEPDTTDYFLMEEKYFISKEKNECR
KPPFQRVIGPEEEILQILNSWFPEEGYVGRIILKTREE
>gnl|CDD|340750 cd17230, TGS_DRG1, TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 1 (DRG-1). DRG-1 is a potassium-dependent GTPase that belongs to the DRG family GTP-binding proteins. It plays an important role in regulating cell growth. It functions as a potential oncogene in lung adenocarcinoma and promotes tumor progression via spindle checkpoint signaling regulation. It also plays an important role in melanoma cell growth and transformation, indicating a novel role in CD4(+) T cell-mediated immunotherapy in melanoma. In addition, DRG-1 is regulated by ZC3H15 (zinc finger CCCH-type containing 15, also known as Lerepo4), and displays a high temperature optimum of activity at 42C, suggesting the ability of being active under possible heat stress conditions. DRG-1 contains a domain of characteristic Obg-type G-motifs that may be the core of GTPase activity, as well as this C-terminal TGS (ThrRS, GTPase and SpoT) domain that has a predominantly beta-grasp ubiquitin-like fold and may be related to RNA binding
YLNLVRIYTKPKGQLPDYEEPVVLRSGKSTVEDFCNKIHKSLIKEFKYALVWGSSVKHNPQRVGKDHVLE
DEDVVQIVKK
>gnl|CDD|340751 cd17231, TGS_DRG2, TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 (DRG-2). DRG-2 is a member of the DRG family GTP-binding proteins. It has been implicated in cell growth, differentiation and death. DRG-2 plays a critical role in control of the cell cycle and apoptosis in Jurkat T cells. It regulates G2/M progression via the cyclin B1-Cdk1 complex. Moreover, DRG-2 is an endosomal protein and a key regulator of the small GTPase Rab5 deactivation and transferrin recycling. It enhances experimental autoimmune encephalomyelitis (EAE) by suppressing the development of TH17 cells. It is also associated with survival and cytoskeleton organization of osteoclasts under influence of macrophage colony-stimulating factor, and its overexpression leads to elevated bone resorptive activity of osteoclasts, resulting in bone loss. DRG-2 contains a domain of characteristic Obg-type G-motifs that may be the core of GTPase activity, as well as this C-terminal TGS (ThrRS, GTPase and SpoT) domain that has a predominantly beta-grasp ubiquitin-like fold and may be involved in RNA binding
YLALIRVYTKKRGERPDFGDAIILRRGATVEHVCHRIHRTLASQFKYALVWGTSTKYSPQRVGLTHVMED
EDVIQIVKK
>gnl|CDD|340752 cd17232, Ubl_ATG8_GABARAP, ubiquitin-like (Ubl) domain found in gamma-aminobutyric acid receptor-associated protein (GABARAP). GABARAP (also termed GABA(A) receptor-associated protein, ATG8A, or MM46) has been implicated in intracellular protein trafficking. It is a cytosolic protein that is localized to transport vesicles, the Golgi network and the endoplasmic reticulum. It interacts with the intracellular domain of the gamma2 subunit of GABA(A) receptors, and thus functions as a trafficking modulator implicated in the intracellular trafficking of GABA(A) receptor. GABARAP also acts as a Ubl modifier belonging to the ATG8 (autophagy-related 8) protein family, which is essential for autophagosome biogenesis and maturation. GABARAP recruits phosphatidylinositol 4-kinase II alpha (PI4KIIalpha) as a specific downstream effector, and regulates phosphatidylinositol 4-phosphate (PI4P)-dependent autophagosome lysosome fusion
KFVYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLR
AEDALFFFVNNVIPPTSATMGQLYQEHHEEDFFLYIAYSDESVYG
>gnl|CDD|340753 cd17233, Ubl_ATG8_GABARAPL1_like, ubiquitin-like (Ubl) domain found in gamma-aminobutyric acid receptor-associated protein-like 1 (GABARAPL1) and similar proteins. GABARAPL1, also termed GEC1, or GABA(A) receptor-associated protein-like, belongs to the small family of GABARAP proteins which includes GABARAP, GABARAPL1, GABARAPL2/GATE-16, and GABARAPL3. GABARAPL1 has been involved in the intracellular transport of receptors via interactions with tubulin and GABA(A) or kappa opioid receptors. It is also a Ubl modifier that functions as a mediator involved in androgen-regulated autophagy process. It is transcriptionally modulated by androgen receptor (AR) and has a repressive role in autophagy. In addition, GABARAPL1 is required for increased membrane expression of epidermal growth factor receptor (EGFR) during hypoxia, suggesting a possible role in the trafficking of these membrane proteins. GABARAPL1 may also play a key role in several important biological processes such as cancer or neurodegenerative diseases. Low expression of GABARAPL1 is associated with poor prognosis of patients with hepatocellular carcinoma. This family also includes GABARAPL3, a paralog of GABARAPL1
YKEDHPFEYRKKEGEKIRKKYPDRVPVIVEKAPKARVPDLDKRKYLVPSDLTVGQFYFLIRKRIHLRPED
ALFFFVNNTIPPTSATMGQLYEDNHEEDYFLYVAYSD
>gnl|CDD|340754 cd17234, Ubl_ATG8_MAP1LC3A, ubiquitin-like (Ubl) domain found in microtubule associate protein 1 light chain 3A (MAP1LC3A). Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. MAP1LC3A is belong to MAP1LC3 (short name LC3) family proteins. MAP1LC3 has a ubiquitin-like fold (Ubl) that belongs to the autophagy-related 8 (ATG8) protein family. A Ubl conjugation of MAP1LC3 by the phospholipid phosphatidylethanolamine (PE) is an essential process for the formation of autophagosomes. MAP1LC3 is cleaved by cysteine protease ATG4 and then conjugated with PE by E1-like enzyme ATG7 and ATG3, an E2-like enzyme. The Ubl conversion of MAPLC3 is known as a marker of autophagy-induction. MAP1LC3A staining patterns are used for different cancer diagnostic
DRPFKQRRSFADRCKEVQQIRDQHPSKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELVKIIRRRLQL
NPTQAFFLLVNQHSMVSVSTPIADIYEQEKDEDGFLYMVYASQETFG
>gnl|CDD|340755 cd17235, Ubl_ATG8_MAP1LC3B, ubiquitin-like (Ubl) domain found in microtubule associate protein 1 light chain 3B (MAP1LC3B). Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. MAPLC3B belongs to the MAP1LC3 (short name LC3) family proteins. MAP1LC3 has a ubiquitin-like (Ubl) fold and belongs to the autophagy-related 8 (ATG8) protein family. A Ubl conjugation of MAPLC3 by the phospholipid phosphatidylethanolamine (PE) is an essential process for the formation of autophagosomes. MAP1LC3 is cleaved by cysteine protease ATG4 and then conjugated with PE by E1-like enzyme ATG7 and ATG3, an E2-like enzyme. The Ubl conversion of MAP1LC3 is known as a marker of autophagy-induction. All MAP1LC3 proteins are dispensable for basal autophagy; however, it has been shown that MAP1LC3B is responsible for selective degradation of p62 through autophagy
KTFKQRRTFEQRVEDVRLIREQHPTKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLN
ANQAFFLLVNGHSMVSVSTPISEVYESEKDEDGFLYMVYASQETF
>gnl|CDD|340756 cd17236, Ubl_ATG8_MAP1LC3C, ubiquitin-like (Ubl) domain found in microtubule associate protein 1 light chain 3C (MAPLC3C). Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. MAP1LC3C belongs to the MAP1LC3 (short name LC3) family proteins. MAP1LC3 has a ubiquitin-like (Ubl) fold that belongs to the autophagy-related 8 (ATG8) protein family. A Ubl conjugation of MAP1LC3 by the phospholipid phosphatidylethanolamine (PE) is an essential process for the formation of autophagosomes. MAP1LC3 is cleaved by cysteine protease ATG4 and then conjugated with PE by E1-like enzyme ATG7 and ATG3, a E2-like enzyme. The Ubl conversion of MAP1LC3 is known as a marker of autophagy-induction. ATG8 proteins are ubiquitously expressed, although some subfamily members are expressed at increased levels in certain tissues, e.g. MAP1LC3C is transcribed at lower levels than other members of MAP1LC3 subfamily and expressed predominantly in the lung
FKQRKSLASRKEEVAGIRAKFPNKIPVIVERYYKEKNLPILDKTKFLVPQELTMSQFVTIIRNRMSLTAT
QAFYLLVNNKSLASMSTTMAEVYRDEKDEDGFLYMTYASQEMF
>gnl|CDD|340757 cd17237, FERM_F1_Moesin, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and similar proteins. Moesin, also termed membrane-organizing extension spike protein, is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. The C-terminal domain can fold back to bind to the FERM domain forming an autoinhibited conformation. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Moesin is involved in mitotic spindle function through stabilizing cell shape and microtubules at the cell cortex. It is required for the formation of F-actin networks that mediate endosome biogenesis or maturation and transport through the degradative pathway
TISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKE
SPLLFKFRAKFYPE
>gnl|CDD|340758 cd17238, FERM_F1_Radixin, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and similar proteins. Radixin is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. The C-terminal domain can fold back to bind to the FERM domain forming an autoinhibited conformation. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Radixin plays important roles in cell polarity, cell motility, invasion and tumor progression. It mediates the binding of F-actin to the plasma membrane after a conformational activation through Akt2-dependent phosphorylation at Thr564. It is also involved in reversal learning and short-term memory by regulating synaptic GABAA receptor density
INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKEN
PLQFKFRAKFFPE
>gnl|CDD|340759 cd17239, FERM_F1_Ezrin, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and similar proteins. Ezrin, also termed cytovillin, or villin-2, or p81, is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. The C-terminal domain can fold back to bind to the FERM domain forming an autoinhibited conformation. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Ezrin is a tyrosine kinase substrate that functions as a cross-linker between actin cytoskeleton and plasma membrane. It has been implicated in the regulation of the proliferation, apoptosis, adhesion, invasion, metastasis and angiogenesis of cancer cells
KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRK
ENPLQFKFRAKFYPE
>gnl|CDD|340760 cd17240, RA_PHLPP1, Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein phosphatase 1 (PHLPP1). PHLPP1, also termed pleckstrin homology domain-containing family E member 1, or PH domain-containing family E member 1, or suprachiasmatic nucleus circadian oscillatory protein (SCOP), is involved in two key signaling pathways, the phosphatidylinositol 3-kinase and diacylglycerol signaling pathways, by directly dephosphorylating and inactivating Akt serine-threonine kinases (Akt1, Akt2, Akt3) and protein kinase C (PKC) isoforms. PHLPP1 also plays critical roles in many cancers, such as gastric cancer, sacral chordoma, gallbladder cancer, hypopharyngeal squamous cell carcinomas, and non-small cell lung cancer. It plays a suppression role in inflammatory response of glioma. Its loss contributes to gliomas development and progression. Loss of PHLPP1 also protects against colitis by inhibiting intestinal epithelial cell apoptosis. The overexpression of PHLPP1 impairs hippocampus-dependent learning, suggesting a role in learning and memory. PHLPP1 contains a Ras-associating (RA) domain followed by a pleckstrin homology (PH) domain, a series of leucine-rich repeats and a protein phosphatase 2C (PP2C) domain
GCIHVYDRHMSSYLRPVLCTLDTTASEVAARLLQLQLHGETVRRLEPHEKPLQIQNDYLFQLGFGDLWRV
QEEGMDPEIGCLIRFYAGKP
>gnl|CDD|340761 cd17241, RA_PHLPP2, Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein phosphatase 2 (PHLPP2). PHLPP2, also termed PH domain leucine-rich repeat-containing protein phosphatase-like (PHLPP-like), is involved in two key signaling pathways, the phosphatidylinositol 3-kinase and diacylglycerol signaling pathways, by directly dephosphorylating and inactivating Akt serine-threonine kinases (Akt1, Akt2, Akt3) and protein kinase C (PKC) isoforms. PHLPP2 also plays critical roles in many cancers, such as glioma, hypopharyngeal squamous cell carcinomas, and non-small cell lung cancer. PHLPP2 contains a Ras-associating (RA) domain followed by a PH domain, leucine-rich repeats and protein phosphatase 2C (PP2C) domain
GCVYIYGADTSTPPPTGSQSSSSSSPDLHLVLCTTETTASELCAQEGRESLYLQLHGDLVRRLDPTERPL
QIVYDYLSGLGFEDPVRIQEEAANSDLSCMIRFYSEKP
>gnl|CDD|410988 cd17242, MobM_relaxase, relaxase domain of MobM and similar proteins. With some plasmids, recombination can occur in a site-specific manner that is independent of RecA. In such cases, the recombination event requires another protein called Pre (plasmid recombination enzyme), also known as Mob (conjugative mobilization). The best characterized member of this family is encoded by the streptococcal plasmid pMV158 that recognizes the plasmid origin of transfer. MobM converts supercoiled plasmid DNA into relaxed DNA by cleaving a phosphodiester bond of a specific dinucleotide and remains bound to the 5'-end of the nick site
ILRVEKLKSGALGGALRHNERERETENPNIDPSRTHLNYELVGPGKKDYAEAIKERLEELGKKKKIRKDA
VLAVEFILTASPEFFEGLDPEEIEEFFKDALEFLKERFGEENIVSAVVHLDETTPHLHAVVVPITEDGRL
SAKELFGGRKKLRELQDDYAEAVAKKGGLERGIKGSKAKHKTKEKELKAKHEELKE
>gnl|CDD|341132 cd17243, RMtype1_S_AchA6I-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Arthrobacter chlorophenolicus A6 S subunit (S.AchA6I) TRD2-CR2. The S.AchA6I S subunit recognizes 5'... TGAANNNNNTCG ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.AchA6I-TRD1 recognizes TGAA/TTCA, and TRD2 recognizes CGA/TCG. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
EVKSLSDVVDIIGGGTPKTSVPEYWNGDIPWFSVKDVNNDSRFVLDTEKKITELGLKNSSTKLLPKGTTI
ISARGTVGKLALLGIPMAMNQSCYGLRGKDGLSNYFLYYLLKNLIEELKQKAHGSVFDTITRKTFDEIKV
PLPPEELQKSFENIVSPLFDKILNNLKENQTLAQLRDTLLPK
>gnl|CDD|341133 cd17244, RMtype1_S_Apa101655I-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Acetobacter pasteurianus S subunit (S.Apa101655I) TRD2-CR2. The S. Apa101655I S subunit recognizes 5'... TTAGNNNNNNTTC... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VKLGDIFDIKIGKTPPRKEPEYWSGDNIPWVSISDMGKGKYISDTKEYITDEAVKKFNVKLVPKGTLLMS
FKLTIGRVAIAGKDLYTNEAIAHFIPKDKKIDTEYLYYYLKSFDYSSLGSTASKGKTLNSKKIKEIPIPL
PPLEEQKRIAPILDKIDALIDQLETLIELLDELLPKLMSG
>gnl|CDD|341134 cd17245, RMtype1_S_TteMORF1547P-TRD2-CR2_Aco12261I-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Thermoanaerobacter tengcongensis S subunit (S.TteMORF1547P) TRD2-CR2 and Aminobacterium colombiense DSM 12261 S subunit (S.Aco12261I) TRD1-CR1. The S.Aco12261I S subunit recognizes 5'... GCANNNNNNTGT ... 3', while the recognition sequence is undetermined for S.TteMORF1547P TRD2-CR2. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. S.TteMORF1547P TRD1-CR1 and S.Aco12261I TRD2-CR2 do not belong to this family. This family may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VKLGEVAEIIMGQSPPSSTYNEEGEGLPFLQGKADFGEIYPTPRVWCTKPTKIAEKGDILISVRAPVGDV
NIADEKCCIGRGLAAIRANKDIDNLFLYYYLKYNKPELEKLGTGSTFKAINKKDLEELKIPLPPLEEQQK
IAEILSTVDEAIEKTKALIEKLDELKKGLMQELF
>gnl|CDD|341135 cd17246, RMtype1_S_SonII-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Shewanella oneidensis MR-1 S subunit (S.SonII) TRD2-CR2. This model contains Shewanella oneidensis MR-1 S subunit (S.SonII) TRD2-CR2 and similar TRD-CR's. S.SonII recognizes 5'... GTCANNNNNNRTCA ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases. S.SonII TRD1-CR1 does not belong to this subfamily
WEWVKLGEISSDITDGTHPTPKYVESGIPFITSKNIKNGKIDFSDVKYISEEDHNEILKRSKLKKGDILF
SIIGTIGRVAIVPEDLPANINQAVALIRPKKEKIDPKYLLYYLNSPIIQKQIEKNAVGGTQKNLSLGDLK
NLKIPLPPLEEQKRIAAILDSLDALIDKLEQKLEKLEDLKKGLMQDLLT
>gnl|CDD|341136 cd17247, RMtype1_S_Eco2747I-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Escherichia coli ST2747 S subunit (S.Eco2747I) TRD2-CR2. The S. Eco2747I S subunit recognizes 5'... CACNNNNNNNGTTG ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This CD contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
PEHWEVVRLGDVARVGNGSTPSRKNPDYWNGGTIPWVSSGEVNDNRITEADEFITELALKECSLPLVPPG
SVLVAMIGQGKTRGQAAILAIEATINQNLAAIRPNEERVLPEYLHYYLESQYDELRRIGSGGGQGALNCG
ILKAFPIPLPPLDEQREIVAELEALLAKIDLLEEKIARLIELLKELRQAL
>gnl|CDD|341137 cd17248, RMtype1_S_AmiI-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Actinosynnema mirum DSM 43827 S subunit (S. AmiI) TRD2-CR2. The S. AmiI S subunit recognizes 5'... CAGNNNNNNNTCGA ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S. AmiI -TRD1 recognizes CAG/CTG, and TRD2 recognizes TCGA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
PAHWEVVPLTDVAKLESGHTPSRSRPEYWNGCIPWISLADVKQLRGDYIYETKEKISELGIANSSARLLP
AGTVVLSRTASVGKSAIMGRPMATSQDFANWVCGPELDPEYLLYVLRAMKPEFERLAMGSTHKTIYMPDF
KALRIALPPLEEQRKIVDRLEALDAKIDALERKLERLIELLKELRQALLTAAVTGK
>gnl|CDD|341138 cd17249, RMtype1_S_EcoR124I-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.EcoR124I TRD2-CR2, S.Eco540I TRD2-CR2, S.Eco540AI TRD2-CR2, and S.Eco540ANI TRD2-CR2. Escherichia coli (R124) S subunit (S.EcoR124I), E. coli ST540 S subunit (S.Eco540I), E. coli ST540A S subunit (S.Eco540AI), and Escherichia coli ST540AN S subunit (S.Eco540ANI) recognize the sequence 5'... GAANNNNNNRTCG ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.EcoR124I -TRD1 recognizes GAA/TTC, and -TRD2 recognizes CGAY/RTCG. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VRLGDLGKFLSGGTPSKSNPEYWGGDIPWVSPKDMKSDYISDSEDHITELAVEESGTKLVPAGSVLIVVR
GMILAHTFPVAITTRPVAFNQDIKALIPKEGIDPEFLLYALKANEDRILSLVDKAGHGTGSLDTDDLKNL
PIPLPPLEEQRRIAAILDALDALIDLLERKLAKLEELLKALMQAL
>gnl|CDD|341139 cd17250, RMtype1_S_Eco4255II_TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Escherichia coli O118:H16 07-4255 S subunit (S.Eco4255II) TRD2-CR2 and Shewanella oneidensis MR-1 S subunit (S.SonIV) TRD1-CR1. Escherichia coli O118:H16 07-4255 S subunit (S.Eco4255II) recognizes 5'... TACNNNNNNNRTRTC ... 3 while Shewanella oneidensis MR-1 S subunit (S.SonIV) recognizes 5'... TACNNNNNNGTNGT ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.SonIV-TRD1 recognizes TAC/GTA and S.SonIV-TRD2 recognizes ACNAC/GTNGT. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VRLGDVCDFKAGSGFPEKYQGKEDGEYPFYKVGDMNNSGNEKYLSTAENYISEEIVKELKAKLFPKGTII
FAKIGEAIKLNRRAILSKDSCIDNNVMGLIPNEGIDSEYLYYWLKKVDLYKYSQATTVPSIRKSTLESIP
IPLPPLEEQKRIAAKLDELFEKLDKLKQALEAAKEQLKGLRQSLL
>gnl|CDD|341140 cd17251, RMtype1_S_HinAWORF1578P-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to S.HinAWORF1578P TRD2-CR2. Haemophilus influenzae RdAW S subunit (S.HinAWORF1578P) recognizes 5'... CTANNNNNGTTY ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains mostly TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WEVKTLKDFGKIITGKTPSTKNKEYYGGDIPFIKIPDMHGNVFITKTEDYLSEEGANSQKNKTLPKNSIC
VSCIATVGLVSITTEESQTNQQINSIIPKKENYRYYLYFALKSLKELLEALGSGGSTTLNLNKGKFSKIK
ILLPSEDLLKKFHKIVSPLFDKILNNQKENQKLSQLRDTLLPKLM
>gnl|CDD|341141 cd17252, RMtype1_S_EcoKI-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.EcoKI TRD1-CR1, S.StySPI TRD1-CR1, S.Ara36733II TRD1-CR1, and S.Eco3722I TRD1-CR1. Escherichia coli str. K-12 substr. MG1655 S subunit (S.EcoKI) and Escherichia coli NCM3722 S subunit (S.Eco3722I) recognize 5'... AACNNNNNNGTGC ... 3', Salmonella enterica subsp. enterica serovar Potsdam S subunit (S.StySPI) recognizes 5'... AACNNNNNNGTRC ... 3', and Actinomyces radicidentis S subunit (S.Ara36733II) recognizes 5'... CATCNNNNNNCTC ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.EcoKI-TRD1 and S.StySPI-TRD1 recognize AAC/GTT, S.EcoKI-TRD2 recognizes GCAC/GTGC, and S.StySPI-TRD2 recognizes GYAC/GTRC. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It also includes TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases such as Treponema pedis T A4 putative Type IIG restriction enzyme/N6-adenine DNA methyltransferase RM.TpeTA4ORF2695P. It may also include type I DNA methyltransferases
WEWVRLGEIAEIIRGVTYKKSDASEEPSEGGIPVLRANNIQNGGLDFDDLVYVPKSKVKEEQKLKKGDIL
ICMSSGSKELVGKAAFIDEDTDYTFGAFCGVIRPKKEIDPRYLFYFLQSPSYREYIRSLASGTNINNLSN
EHLENLKIPLPPLAEQKRIVAKLDKLDALIDKLKQALEKLDELLKSLFQ
>gnl|CDD|341142 cd17253, RMtype1_S_Eco933I-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Escherichia coli O157:H7 EDL933 S subunit (S.Eco933I), Escherichia coli O104:H4 2009EL-2071 S subunit (S.Eco2071ORF3585P) TRD2-CR2, and Streptomyces species SirexAA-E S subunit (S.SspAAEORF2129P) TRD1-CR1 and TRD2-CR2. Escherichia coli O157:H7 EDL933 S subunit (S.Eco933I) recognizes 5'... CACNNNNNNNCTGG ... 3' and Escherichia coli O104:H4 2009EL-2071 S subunit (S.Eco2071ORF3585P) recognizes 5'... RTCANNNNNNNNGTGG ... 3'. The recognition sequence of Streptomyces species SirexAA-E S subunit (S.SspAAEORF2129P) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.Eco2071ORF3585P TRD1 recognizes RTCA/TGAY and S.Eco2071ORF3585P TRD2 recognizes CCAC/GTGG. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
GWEWVRLGDVAEVQSGITKGKKRRGGELEVPYLRVANVQDGYLDLSEVKEIEVTEEELERYRLRKGDLLV
TEGGDSDKLGRGAIWRGEIPPCLHQNHLFRVRPKDDLLLPEFLSYWLNSAYGRGYFLRAAKQTTNLASIN
STKLKALPVPLPPLEEQRRIVERLDELLALIDALEASLAKLEELLKALRQALL
>gnl|CDD|341143 cd17254, RMtype1_S_FclI-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.FclI TRD1-CR1. The recognition sequence of Flavobacterium columnare G4 S subunit (S.FclI) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It also contains TRD-CR-like sequence-recognition domains of type I DNA methyltransferases, such as putative Type I N6-adenine DNA methyltransferases from Microbacterium ketosireducens (M.Msp12510ORF408P) and Treponema primitia ZAS-2 (M.TprZAS2ORF3630P). It may also include various type II restriction enzymes and methyltransferases
VKLGDLATFINGRAFKPSEWSDSGLPIIRIQNLNGGNAPFNYYSGLLDEKYYVEKGDLLFSWSASFGPFI
WNGGKAILNQHIFKVVPDEEIDKDYLYYLLKALTEEIESQAHGSTMVHITKGDLENIKVPLPPLEEQKRI
AAILDELDALIDALEEQLKKLEELRKALLQSLL
>gnl|CDD|341144 cd17255, RMtype1_S_Fco49512ORF2615P-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Flavobacterium columnare S subunit (S.Fco49512ORF2615P) TRD2-CR2. The recognition sequence of Flavobacterium columnare S subunit (S.Fco49512ORF2615P) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KKLGDLFEIGRGRVISKKYISENPGDYPVYSSQTKNNGIMGYINTYDFDGEYITWTTDGANAGTVFYRNG
KFSVTNVCGVLKVKNKNINNKFLYYALNLIAKKYVSFDGNPKLMNNVMAKIKIPLPPLEEQEKIANILDK
LDELINLLIAKLKKLIELRKKQLEYY
>gnl|CDD|341145 cd17256, RMtype1_S_EcoJA65PI-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.EcoJA65PI TRD1-CR1, S.Fco49512ORF2615P TRD1-CR1, and S.SonIV TRD2-CR2. Escherichia coli UCD_JA65_pb S subunit (S.EcoJA65PI) recognizes 5'... AGCANNNNNNTGA ... 3' while Shewanella oneidensis MR-1 S subunit (S.SonIV) recognizes 5'... TACNNNNNNGTNGT ... 3'. The recognition sequence of Flavobacterium columnare S subunit (S.Fco49512ORF2615P) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.EcoJA65PI TRD1 recognizes AGCA/TGCT and S.EcoJA65PI TRD2 recognizes TCA/TGA; S.SonIV TRD1 recognizes TAC/GTA and S.SonIV TRD2 recognizes ACNAC/GTNGT. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
LGEIARVKGGGRLPKGESLSDGPTGVPYIRVTDIKNGGIDLDNLKYISPEIHEKIKRYTLSKGDILISIV
GTIGRVGIVPKELDGANLTENAARIRPKDSISPRYLYYYLRSPFGQSQIESETKGAAQPKLNLKRIRELP
IPLPPLEEQKRIVAILDSLDAKIDALEKQLAKLEELKKALMQ
>gnl|CDD|341146 cd17257, RMtype1_S_EcoBI-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.EcoBI TRD1-CR1, S.EcoSanI TRD1-CR1, and S.EcoVR50I TRD1-CR1. Escherichia coli B S subunit (S.EcoBI) and Escherichia coli VR50 S subunit (S.EcoVR50I) recognize 5'... TGANNNNNNNNTGCT ... 3', while Escherichia coli Sanji S subunit (S.EcoSanI) recognizes 5'... TGANNNNNNCTTC ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WEVVRLGDVADVQNGFPFKSKLFNDEGGGLPLIRIRDLKSGDTETYYTGEYDEKYLVKNGDILIGMDGDF
NAAIWKGGDALLNQRVCRIRPKSEELDKRFLYYALPPPLKAIEDTTSSTTVKHLSSKDIDEIELPLPPLE
EQRRIAEILDELDALIDKLIAKLEKLRDLLLPLLQS
>gnl|CDD|341147 cd17258, RMtype1_S_Sau13435ORF2165P-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.Sau13435ORF2165P TRD1-CR1 and S.SauL3067ORFAP TRD1-CR1. Staphylococcus aureus NCTC 13435 S subunit (S.Sau13435ORF2165P) recognizes 5'... TCTANNNNNNRTTC ... 3'; the recognition sequence of Staphylococcus aureus 3067 S.Sau3067ORFAP S subunit is as yet undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.Sau13435ORF2165P TRD1 recognizes TCTA/TAGA, and S.Sau13435ORF2165P TRD2 recognizes GAAY/RTTC. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains mostly TRD1-CR1. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
LTHGPNKDPELFCNGNIKLVCIKNELINSLKVKIVEPDYKIGLKQSKIFKKGDVLITRHGTIGRVSIILS
EEACLSSHVAGFNSKEGISDNKFIKYLFNSKKIKNRLMSYGASSTQPALNLSRLLKIKFPNPPLEEQQKI
GKILSTWDRAIELTEQKLELLQQQKKGLMQQLF
>gnl|CDD|341148 cd17259, RMtype1_S_StySKI-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to TRD2-CR2's of StySKI, S.EcoAI, S.EcoJA17PI, and S.EcoJA23PI. Salmonella kaduna CDC-388 S subunit (StySKI) recognizes 5'... CGATNNNNNNNGTTA ... 3' while Escherichia coli Type-1 restriction enzyme EcoAI specificity protein (S.EcoAI), Escherichia coli UCD_JA17_pb S subunit (S.EcoJA17PI) and Escherichia coli UCD_JA23_pb S subunit (S.EcoJA23PI) recognize 5'... GAGNNNNNNNGTCA ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WEWVKLGDVADILSGYAFKSSEFSESGIRLLRGANVGVGEIRWDDTVYLPEEYLEEYEKYLLKEGDIVIA
LDRPIISGGLKVARIPKSDLPALLVQRVARIRPKDELNSDFLYYLLQSDFFLNYVEPVLTGTDVPHISTK
QIKNFKIPLPPLEEQKKIAEFLSSLDALIDLLEQKLEKLQQLKKGLMQS
>gnl|CDD|341149 cd17260, RMtype1_S_EcoEI-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.EcoEI TRD1-CR1, S.EcoJA17PI TRD1-CR1, S.EcoJA23PI TRD1-CR1, and S.StyLTIII TRD1-CR1. Escherichia coli A58 S subunit (S.EcoEI) recognizes 5'... GAGNNNNNNNATGC ... 3', Escherichia coli UCD_JA17_pb S subunit (S.EcoJA17PI) and Escherichia coli UCD_JA23_pb S subunit (S.EcoJA23PI) recognize 5'... GAGNNNNNNNGTCA ... 3', and Salmonella typhimurium LT7 S subunit (S.StyLTIII) recognizes 5'... GAGNNNNNNRTAYG ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example: S.EcoEI TRD1 and S.StyLTIII TRD1 recognize GAG/CTC, S.EcoEI TRD2 recognizes GCAT/ATGC, and S.StyLTIII TRD2 recognizes CRTAY/RTAYG. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It also includes TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases, such as Pseudomonas putida Jo 4-731 Type IIG restriction enzyme/N6-adenine DNA methyltransferas RM.PpiI and Porphyromonas macacae COT-192 OH2631 RM.Pma2631ORF8845P, as well as type I DNA methyltransferases such as Chlorobium limicola M.Cli245ORF128P. RM.PpiI recognizes the sequence 5' ... GAACNNNNNCTC ... 3'
TEVSFVPMAAVSEGGGIDLSETRPLKEVKKGYTYFRNGDVLLAKITPCFENGKTAIVDGLPNGIGFGSTE
FHVLRPKEGILPEFLYYLLRSPSFRKEAIKSMTGSSGRQRVPKDFLENYKIPLPPLEEQKRIAAILDSLD
AKIDALEAEIETLEELLDALLPKLL
>gnl|CDD|341150 cd17261, RMtype1_S_EcoKI-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Escherichia coli str. K-12 substr. MG1655 S subunit (S.EcoKI) TRD2-CR2, Escherichia coli A58 S subunit (S.EcoEI) TRD2-CR2, and Aminomonas paucivorans S subunit (S.Apa12260I) TRD2-CR2. Escherichia coli str. K-12 substr. MG1655 S subunit (S.EcoKI) recognizes 5'... AACNNNNNNGTGC ... 3', Escherichia coli A58 S subunit (S.EcoEI) recognizes 5'... GAGNNNNNNNATGC ... 3', and Aminomonas paucivorans S subunit (S.Apa12260I) recognizes 5'... GCCNNNNNCTCC ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.EcoKI-TRD1 recognizes AAC/GTT and S.EcoKI-TRD2 recognizes GCAC/GTGC, S.EcoEI TRD1 recognizes GAG/CTC and S.EcoEI TRD2 recognizes GCAT/ATGC, and S.Apa12260I TRD1 recognizes GCC/GGC and S.Apa12260I TRD2 recognizes GGAG/CTCC. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WEWVRLGDLIEGIRNGWSPKPPDDETGWPVLKLSAVTSGKFDPSENKYLPESLEPASEYWLKPGDLLISR
ANTSELVGRAALVDGDPDNLIYPDKLIRLRVNEELLLPEYLALALNSPSARRQIESRATGTAGSMPKISQ
SDLKSLPIPLPPLAEQKRIVARVDELLALIDRLEAQLAAALQLLDRLRQAL
>gnl|CDD|341151 cd17262, RMtype1_S_Aco12261I-TRD2-CR2, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Aminobacterium colombiense DSM 12261 S subunit (S.Aco12261I) TRD2-CR2 and Moraxella catarrhalis S subunit (S.Mca353ORF290P) TRD2-CR2. Aminobacterium colombiense DSM 12261 S subunit (S.Aco12261I) recognizes 5'... GCANNNNNNTGT ... 3', and Moraxella catarrhalis S subunit (S.Mca353ORF290P) recognizes 5'... CAAGNNNNNNTGT ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WEVKKLGEVVENLDSKRIPLSSEERERRQGNYPYYGASGIVDYVDDYIFDGEYVLIGEDGANLLSRGTPI
AFYVSGKFWVNNHAHVLKGKNGISTEFLYYYLNSIDISPYVTGAAQPKLNQANLNSIPIPLPPLEEQKKI
VAILDKLDALIDLLEEELEKLIELKKALLQKL
>gnl|CDD|341152 cd17263, RMtype1_S_AbaB8300I-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Acinetobacter baumannii B8300 S subunit (S.AbaB8300I) TRD1-CR1. Acinetobacter baumannii B8300 S subunit (S.AbaB8300I) recognizes 5'... GAYNNNNNNNTCYC ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VKLGEVCKFSKGKQPPISERFDEPKEGSVRYIQIEDLRNNNEKKYIENPKKSVICNEDDILIVRDGANAG
EVGTGLEGAIASTLFKIIPDKNIIDKDYLYYFLKSKEIQLNILTKAGSTIPHVNKKDLENLKIPLPSLEE
QKKIAEILDKLDALIDKLKELIEKLIELKKGLFQELL
>gnl|CDD|341153 cd17264, RMtype1_S_Eco3763I-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Escherichia coli O69:H11 07-3763 S subunit (S.Eco3763I) TRD2-CR2. Escherichia coli O69:H11 07-3763 S subunit (S.Eco3763I) recognizes 5'... TACNNNNNNNRTRTC ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
RLGDIAEFINGDRGKNYPSKSEFVDEGIPFINAGHLEDGTIDLSNMNFISEEKYNSLGSGKLQKGDILYC
LRGSLGKCAIVDNYDEGAIASSLVIIRPFAKVDVRYLYYYLNSPLGKSQIKKYDNGSAQPNLSAKSLKKF
LIPLPPLEEQKRIVAKLDELDALIDKLKQALEKLEELLQSLFQS
>gnl|CDD|341154 cd17265, RMtype1_S_Eco4255III-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Escherichia coli O118:H16 07-4255 S subunit (S.Eco4255III) TRD2-CR2 and Escherichia coli ECONIH1 S subunit (S.EcoNIH1II) TRD2-CR2. Escherichia coli O118:H16 07-4255 S subunit (S.Eco4255III) recognizes 5'... GAGNNNNNGTTY ... 3', and Escherichia coli ECONIH1 S subunit (S.EcoNIH1II) recognizes 5'... YTCANNNNNNGTTY ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.Eco4255III-TRD1 recognizes GAG/CTC and S.EcoNIH1II-TRD1 recognizes YTCA/TGAR, while both S.EcoNIH1II-TRD2 and S.Eco4255III-TRD2 recognize RAAC/GTTY. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KKLKEIGEAIIGLTYSPEDVSDEGTLVLRSSNIQNGKLDFDDNVYVNSKIPEKLIVKEGDILICVRNGSR
ALIGKNALIDKEAEGMTFGAFMTVFRSEYNDYLFHLFNSDLFKKQIGSFLTATINQITNGNLNNFKIPLP
PLEEQEKIAEFLSSLDAKIDKLIKKIEKLIELKKELMQQLI
>gnl|CDD|341155 cd17266, RMtype1_S_Sau1132ORF3780P-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Staphylococcus aureus subsp. aureus MSHR1132 S subunit (S.Sau1132ORF3780P) TRD2-CR2. Staphylococcus aureus subsp. aureus MSHR1132 S subunit (S.Sau1132ORF3780P) recognizes 5'... CAAGNNNNNRTC ... 3'. The RM system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example S.Sau1132ORF3780P-TRD1 recognizes CAAG/CTTG and S.Sau1132ORF3780P-TRD2 recognizes GAY/RTC. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VKLGELCKIKSGKSITASKISEEGDYPVYGGNGIIGYTDEYNHEGEYILIGRVGALCGNVHYVEGKFWVT
DNALVVTPKKENNIKFLYYLLKSLNLNQYATGSAQPLITVSKLKKLKIPLPPLEEQKKIAAILDSLDAKI
DLLEKKLEKLIELKKELMQ
>gnl|CDD|341156 cd17267, RMtype1_S_EcoAO83I-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.EcoAO83I TRD1-CR1 and S.AbaB8342I TRD2-CR2. Escherichia coli strain A0 34/86 S subunit (S.EcoAO83I) recognizes 5'... GGANNNNNNNNATGC ... 3, and Acinetobacter baumannii B8342 S subunit (S.AbaB8342I) recognizes 5'... TTCANNNNNNTCC ... 3. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example S.AbaB8342I-TRD1 recognizes TTCA/TGAA and S.AbaB8342I-TRD2 recognizes GGA/TCC. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It also includes TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases such as Type IIG restriction enzyme/N6-adenine DNA methyltransferases from Thermus scotoductus RFL1 (RM.TstI) and Acinetobacter lwoffi Ks 4-8 (RM.AloI), as well as type I DNA methyltransferases such as Sideroxydans lithotrophicus ES-1 Type I N6-adenine DNA methyltransferase (M.SliESORF1090P). RM.TstI recognizes 5' ... CACNNNNNNTCC ... 3' and RM.AloI recognizes 5' ... GAACNNNNNNTCC ... 3'
VKLGDVIELQYGKDLPKSRRIPGPYPVYGSNGIVGYHNEALVKGPGIVVGRKGSIGKVHYSEEDFWPIDT
TLYVKDFKGNDPRFLYYLLKTLDLERLNSGSAVPGLNRNDVYSLKVPLPPLEEQKAIAAILDALDDKIEL
NRRQNQTLEELADALLPK
>gnl|CDD|341157 cd17268, RMtype1_S_Ara36733I_TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.Ara36733I TRD1-CR1 AND S.Ara36733I TRD2-CR2. Actinomyces radicidentis S subunit (S.Ara36733I) recognizes 5'... CGAGNNNNNCTG ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VEWKTLGEIGEFIRGKGITKKDFVESGVPCIHYGEIYTKYGIYTTKTKSFISEELAKKLRKAKPGDLLIA
GTGETIEDIGKAVAWLGDEEVAAGGDIIIFRHSQNPKYLSYLLNSPAFQKQKRKLGTGTKVVHISASDLA
KIKIPVPPLEEQERIVEILDKFDALIAGLPAEIEARRKQYEYYRD
>gnl|CDD|341158 cd17269, RMtype1_S_PluTORF4319P-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Photorhabdus luminescens S subunit (S.PluTORF4319P) TRD2-CR2. The recognition sequence of Photorhabdus luminescens S subunit (S.PluTORF4319P) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KTLGEVAEIKTGKLDANAANENGKYPFFTCSKEPLRIDTYAFDEEAILIAGNGSGVGNVKYYNGKFNAYQ
RTYVIHPFKEEIDPKFLYYYLKSYFKKYIEKNSVGSSVPYIRLPMLENFKIPLPPLEEQKRIVRILDKFD
ALTAELPAELEARKKQYEYYRDALLSFA
>gnl|CDD|341159 cd17270, RMtype1_S_Sba223ORF3470P-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.Sba223ORF3470P TRD1-CR1. The recognition sequence of Shewanella baltica OS223 S subunit (S.Sba223ORF3470P) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KTLGEVAKFRRGSFPQPYGNSEWYDGEGSMPFVQVADVGDNFKLVEKTKQKISKLAQPKSVFVPKGTVIV
TLQGSIGRVAITQYDAYVDRTLLIFESYKININKKFFAYQLKLKFEIEKEKAPGGTIKTITKEELSKFEI
PIPSLEEQKEIVNILDKFDELITELQLRKKQLEYYKKALLSFM
>gnl|CDD|341160 cd17271, RMtype1_S_NmaSCMORF606P_TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Nitrosopumilus maritimus SCM1 S subunit (S2.NmaSCMORF606P) TRD2-CR2, Corynebacterium jeikeium K411 S subunit (S.CjeKORF1254P) TRD2-CR2 and Porphyromonas canoris COT-108 OH2762 S subunit (S2.Pca2762ORF8685P) TRD1-CR1. The recognition sequences of Nitrosopumilus maritimus SCM1 S subunit (S2.NmaSCMORF606P), Corynebacterium jeikeium K411 S subunit (S.CjeKORF1254P), and Porphyromonas canoris COT-108 OH2762 S subunit (S2.Pca2762ORF8685P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
LGEVLKGLSSGATPSRGNPEYFNGDIPWITSGELNYNYITDTNEKITEEAVKNTNLKIHPKGTFLIAITG
LEAAGTRGKCAITGIPATTNQSCMAFYPTKKLTTEFLFYWYKKYGNYLGFKYAQGTKQQSYTADIVKKLP
ILLPTLKEQKKIANFLSDIDELIATLEKKIEKLKKIKKGLMQKLLT
>gnl|CDD|341161 cd17272, RMtype1_S_Eco2747II-TRD2-CR2-like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.Eco2747II TRD2-CR2 and S.Eco2747AII TRD2-CR2. Escherichia coli ST2747 S subunit (S.Eco2747II) and Escherichia coli ST2747A s SUBUNIT (S.Eco2747AII) recognize 5'... GAANNNNNNNTAAA ... 3'. Generally The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains mainly TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VEEKTLGDIAVDGFQNGPAPNFDEKGEIPVITSKNISNGKIDFEYVKYDFLSISKNRKINKGDILITMIG
TIGETAIVKCLDPKFYTLNLYLIRLKKEKLLPSYLKYFLDSEKFLNKSISATSGQGYLKANQIDKLEIPL
PPLEEQQRIVKILDKFDTLCNDITEGLPAEIEARQKQYEYYRDLLLSFP
>gnl|CDD|341162 cd17273, RMtype1_S_EcoJA69PI-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.EcoJA69PI TRD1-CR1, MjaXIP/S.MjaORF132P TRD2-CR2, and S.HspDL1ORF16625P TRD2-CR2. Escherichia coli UCD_JA69_pb S subunit (S.EcoJA69PI) recognizes 5'... CCANNNNNNNCTTC ... 3'. The recognition sequences of Methanococcus jannaschii MjaXIP/S.MjaORF132P TRD2-CR2 and Halobacterium species DL1 S subunit (S.HspDL1ORF16625P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It also includes TRD-CR-like sequence-recognition domains of various putative type II restriction enzymes and methyltransferases and may also include type I DNA methyltransferases
WEVVKLGDVAEIVGGGTPSTKNPEYWNGDIPWITPTDLTKLKGKYISDTERKITELGLKNSSAKLLPAGS
VLLSSRAPIGYVAIATNPLATNQGFKSIIPNEEIDNEFLYYLLKNNKPEIESLASGSTFKEISKSTFKKI
EIPLPPLEEQKKIAAILSKLDELIELLEKENEKLKELRDGLLPKLF
>gnl|CDD|341163 cd17274, RMtype1_S_Eco540ANI-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.Eco540ANI TRD1-CR1, S.Eco2747AII TRD1-CR1, S.Eco540AI TRD1-CR1, S.Eco2747II TRD1-CR1, and S.Eco540I TRD1-CR1. Escherichia coli ST540AN S subunit (S.Eco540ANI), Escherichia coli ST540A S subunit (S.Eco540AI), and Escherichia coli ST540 S subunit (S.Eco540I) recognize 5'... GAANNNNNNRTCG ... 3'. Escherichia coli ST2747A S subunit (S.Eco2747AII) and Escherichia coli ST2747 S subunit (S.Eco2747II) recognize 5'... GAANNNNNNNTAAA ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
EWEEKELGELLDYEQPTKYIVKSTNYNDNYKTPVLTAGKTFILGYTNETDGIYKASPSPVIIFDDFTTAS
KWVDFPFKVKSSAMKILTPKNNNVNLKFVYEALQTIKYVPGDHKRHWISEYSKFKIPLPPLEEQNKIVRI
LDKFDELIAELEAKLELLKKQKKYYLQKLFT
>gnl|CDD|341164 cd17275, RMtype1_S_MjaORF132P-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to MjaXIP/S.MjaORF132P TRD1-CR1. The recognition sequence of Methanococcus jannaschii S subunit (MjaXIP/S.MjaORF132P) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
EQVKLGELCEKMKSGGTPSTSNKEYYGGDIPFVKISDMTKSGKYIYSTEKYITEEGLKNSSAWIVPKGTI
LYAMYASVGKVAINKIDVATNQAILGIIPKDEKLDFEFLYYWLLSLKNELKRLIRTGTQANLNAEIVKNL
PIPLPPLEEQKKIAEILDKIDAEIDKLEEKIEKLRELKKGLLQKMF
>gnl|CDD|341165 cd17276, RMtype1_S_Sau1132ORF3780P-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to S.Sau1132ORF3780P TRD1-CR1, and S.Mca353ORF290P TRD1-CR1. The Staphylococcus aureus subsp. aureus MSHR1132 S subunit (S.Sau1132ORF3780P) recognizes 5'... CAAGNNNNNRTC ... 3', and Moraxella catarrhalis S subunit (S.Mca353ORF290P) recognizes 5'... CAAGNNNNNNTGT ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.Sau1132ORF3780P-TRD1 recognizes CAAG/CTTG, and S.Sau1132ORF3780P-TRD2 recognizes GAY/RTC. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KKIGDIAKTSSGGTPLRSNQEYYFNGGTIPWVKTTDLNNGVIYETEEKITEKALKETSCKLLPKGTVLVA
MYGGFGQIGRTGLLGIPAAINQAICAILPNEKKVNPEFLLRYLNFNRPYWMRVAASSRKDPNITKDDVRN
FPIPLPPLDEQRAIVEFLSDVDALIDSLEALIEKLRELKKGLMQQLL
>gnl|CDD|341166 cd17277, RMtype1_M_Cni19672ORF1405P_RMtype11G_Hci611ORFHP_TRD1-CR1_like, Restriction modification N6-adenine DNA methyltransferase TRD-CR, similar to RMtype1 Calditerrivibrio nitroreducens M.Cni19672ORF1405P TRD1-CR1 and RMtype11G Helicobacter cinaedi PAGU611 RM.Hci611ORFHP TRD1-CR1. The recognition sequence of Calditerrivibrio nitroreducens M.Cni19672ORF1405P is undetermined, and the predicted recognition sequence of RM.Hci611ORFHP is 5'... GAGNNNNNGT ... 3'. M.Cni19672ORF1405P is a putative type I N6-adenine DNA methyltransferase. RM.Hci611ORFHP is a type II subtype gamma (also called type IIG and type IIC) N6-adenine DNA methyltransferase. Both are DNA methyltransferase-specificity subunit fusion proteins, they each have a domain corresponding to a HsdM methylation (M) subunit followed by a C-terminal, TRD-CR-like domain for sequence-recognition, which corresponds to the HsdS specificty (S) subunit. The latter consists of two variable TRDs, and two CRs which separate the TRDs; the TRDs each bind to different specific sequences in the DNA. RM.Hci611ORFHP has an additional N-terminal HSDR_N domain. Restriction-modification (RM) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit, two modification (M) subunits, and two restriction (R) subunits
WPIVKLGEVCEIINGSTPSKKNEEYWNNGTIKWLTIPDIDERGLIISSTKQFITEKALEEKKVKLVPKNS
VLLSCTATIGKVAIAKIELTTNQQINALICKDSKILPEYLFYALKHIKQVLERLTTNPGVKHVNLSMLSN
LQIPLPPLEVQKKIVAEIEKVEKVIQGLRQKIDEYQPLINAILD
>gnl|CDD|341167 cd17278, RMtype1_S_LdeBORF1052P-TRD2-CR2, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Lactobacillus delbrueckii subsp. bulgaricus S subunit (S2.LdeBORF1052P) TRD2-CR2. The recognition sequence of Lactobacillus delbrueckii subsp. bulgaricus S subunit (S2.LdeBORF1052P) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WEVVKLGDIADIQNGYAFKSSDFSDEGIPVIRIGNIKNGGIDLDDNSKYPEEPLEKYEKFLLKKGDILIA
MTGGTVGKVAIVPEDDEPALLNQRVGKFRPKDKIDKEFLYYLLRSDSFRNQIKSSATGTAQPNISPKDIE
SIKIPLPPLEEQKKIAEILDSLDAKIDKLEQKLEKLRDLLKPLLQSLFT
>gnl|CDD|341168 cd17279, RMtype1_S_BmuCF2ORF3362P_TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Burkholderia multivorans CF2 S subunit (S.BmuCF2ORF3362P) TRD1-CR1 and and Halomonas campaniensis LS21 S subunit (S.HcaLS21ORF9970P) TRD1-CR1. The recognition sequences of Burkholderia multivorans CF2 S subunit (S.BmuCF2ORF3362P) and Halomonas campaniensis LS21 S subunit (S.HcaLS21ORF9970P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VPLKRIFRIVNGSTPKSGEEDYWDGDIPWVTPADLSKLDGKYISSSQRKITEAGLESCGTSLVPAGSIIL
STRAPIGYVAIATVELCTNQGCKALVPNSDVDSRFLYYLLLAAKEELNSLGRGTTFLELSTDELANFKIP
LPPLSEQRAIADFLDRETAKIDALIAKKQQLIELLKEKRQALIT
>gnl|CDD|341169 cd17280, RMtype1_S_MspEN3ORF6650P_TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Marinobacter species EN3 S subunit (S.MspEN3ORF6650P) TRD1-CR1, Methanothermobacter marburgensis str. Marburg S subunit (S.Mma2133ORF14720P) TRD2-CR2 and Nostoc species NIES-3756 S subunit (S.Nsp3756ORF27100P) TRD1-CR1. The recognition sequences of Marinobacter species EN3 S subunit (S.MspEN3ORF6650P), Methanothermobacter marburgensis str. Marburg S subunit (S.Mma2133ORF14720P), and Nostoc species NIES-3756 S subunit (S.Nsp3756ORF27100P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WKISHLFGLIGSGTTPKSDNEDYYDGGIPWVTTGDLRDGIITETSKKITDKALDDYSALKIYPAGSLVIA
MYGATIGRLGILGIDATTNQACCVLSGSNKIDIKFLFYWLLANRDELISLASGGGQPNISQELIKSLRIP
VPPLEEQKQIAAFLDKKTAKIDSLIEKKERLIELLKERRQALISEAV
>gnl|CDD|341170 cd17281, RMtype1_S_HpyAXIII_TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Helicobacter pylori 26695 S subunit (S.HpyAXIII/Prototype S.Hpy26695ORF4050P) TRD1-CR1, Neisseria meningitidis 510612 S subunit (S.Nme510612ORF1157P) TRD1-CR1 and Streptococcus mitis SVGS_061 S subunit (S2.Smi61ORF7905P) TRD1-CR1. Helicobacter pylori 26695 S subunit (S.HpyAXIII/Prototype S.Hpy26695ORF4050P) recognizes 5'... CTANNNNNNNNTGT ... 3', and the recognition sequences of Neisseria meningitidis 510612 S subunit (S.Nme510612ORF1157P) and Streptococcus mitis SVGS_061 S subunit (S2.Smi61ORF7905P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, Helicobacter pylori 26695 S subunit (S.HpyAXIII/Prototype S.Hpy26695ORF4050P) TRD1 recognizes CTA/TAG, and TRD2 recognizes ACA/TGT. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
GVEWKKLGEIFDIRNGYTPSKSNKEYWENGTIPWFRMEDIRENGRILSDSIQHITPSAVKGGKLFPANSI
ILSTTATIGEHALITVDSLANQRFTNFSLKKSYKNKLDIKFLFYYFFVLGEWCKKNINIGGFPSVDMNKL
KKFKIPIPPLEEQEKIVEILDKFTKLTADLTAELPAELEARKKQYEYYRDKLLSFE
>gnl|CDD|341171 cd17282, RMtype1_S_Eco16444ORF1681_TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Escherichia coli G4/9 S subunit (S.Eco16444ORF1681P) TRD1-CR1 and Zobellia galactanivorans DsiJT S subunit (S.ZgaJTORF2697P)TRD2-CR2. The recognition sequences of Escherichia coli G4/9 S subunit (S.Eco16444ORF1681P) and Zobellia galactanivorans DsiJT S subunit (S.ZgaJTORF2697P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It also includes TRD-CR-like sequence-recognition domains of various putative type II restriction enzymes and methyltransferases and may also include type I DNA methyltransferases
WEVKKLSDLGSLERGKFKHRPRNDPRLYGGDYPFIQTGDVARANGYITSYSQTLNEKGLAQSKLFPKGTL
CITIAANIGDTAILGFDACFPDSVVGFIPNEEKIDVEFLEYYLRTLKKELEAIAPQSAQKNINLEILRPL
KIPVPPLEEQKKIVEILDALDDLIDNLEKRIAKLEELKQSLLQEAF
>gnl|CDD|341172 cd17283, RMtype1_S_Hpy180ORF7835P_TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Helicobacter pylori SJM180 S subunit (S.Hpy180ORF7835P) TRD2-CR2 and Haemophilus influenzae PittGG S subunit (S.HinGGORF3080P) TRD2-CR2. The recognition sequences of Helicobacter pylori SJM180 S subunit (S.Hpy180ORF7835P) and Haemophilus influenzae PittGG S subunit (S.HinGGORF3080P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KKLGDISEIVRGASPRPIGDPITFDGDGIPWIKIGDVTKDGKYITKTKEKITEEGAKKSRLVKPGDLILS
NSMSFGRPYILKIDGCIHDGWLVFSDLKKKLDKDFLYYLLSSITVQLQFSAQAGGGTKNLNTDIVKNLKI
PLPPLEEQKRIAEILDSLDALIDALEEKLEKLEELKKGLMQ
>gnl|CDD|341173 cd17284, RMtype1_S_Cbo7060ORF11580P_TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Clostridium botulinum CFSAN024410 S subunit (S.Cbo7060ORF11580P) TRD2-CR2 and Shewanella xiamenensis BC01 S subunit (S.SxiBC01ORF77P) TRD1-CR1. The recognition sequences of Clostridium botulinum CFSAN024410 S subunit (S.Cbo7060ORF11580P) and Shewanella xiamenensis BC01 S subunit (S.SxiBC01ORF77P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
PEGWEVKRVGDVCDCIVPGRDKPKSFDGNIPWITIEDIKGKYISSSKSGLGVSEEEIKEMNLKVIPKGSV
IMSCVGDFGIVAIATNELVINQQLHAFVPSKKINPEYLMYLLSLQKKYMEKIATGTTIPYLNKTNCESIP
IPLPPIEEQNKIAKILDSIDKKIDLLIAKLEKLQQLKKGLMQQLF
>gnl|CDD|341174 cd17285, RMtype1_S_Csp16704I_TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Campylobacter species RM1670 S subunit (S.Csp16704I) TRD2-CR2, Aeromonas media WS S subunit (S.AmeWSORF2351P) TRD1-CR1, and Clostridium carboxidivorans P7 S subunit (S.CcaPORF573P) TRD2-CR2. Campylobacter species RM16704 S subunit (S.Csp16704I) recognizes 5'... ACANNNNNNNNTCG ... 3', and the recognition sequences of Aeromonas media WS TRD1-CR1 S subunit (S.AmeWSORF2351P) and Clostridium carboxidivorans P7 S subunit (S.CcaPORF573P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KKLGDLVEKIVGGGTPSKSNPEYWNGDIPWASVKDLKGKYLTSTEDKITEEGLKNSSSNLIPKGTVIIAT
RMGLGKVAINKIDVAINQDLKALFPKDELDPEYLLYWFLSIEETIESLGTGTTVKGITLEDLKSLKIPLP
PLEEQKRIVAILDELDELIDKLEAKLEKLKQLKKGLMQSLL
>gnl|CDD|341175 cd17286, RMtype1_S_Lla161ORF747P_TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Lactococcus lactis subsp. lactis Dephy 1 S subunit (S.Lla161ORF747P) TRD1-CR1, and Lactococcus lactis IO-1 S subunit (S2.LlaIO1ORF1141P) TRD2-CR2. The recognition sequences of Lactococcus lactis subsp. lactis Dephy 1 S subunit (S.Lla161ORF747P) and Lactococcus lactis IO-1 S subunit (S2.LlaIO1ORF1141P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KKLGDLGEIVTGNTPSTKNSEYYGGEILFVTPTDIDGNKYIYKTEKKLSEKGFKKARILPKGSILVTCIG
SIGKNAIATEDCATNQQINAIIPNKNYDPEFLYYALENWSKKIKSLAGKQAVPIINKTEFSKIKILVPPL
EEQQKIANFLSKLDELIELQQQKIEKLEELKKGLLQKLF
>gnl|CDD|341176 cd17287, RMtype1_S_EcoN10ORF171P_TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Escherichia coli N10-0505 S subunit (S.EcoN10ORF171P) TRD2-CR2, and Herpetosiphon aurantiacus S subunit (S.HauORF5277P) TRD2-CR2. The recognition sequences of Escherichia coli N10-0505 S subunit (S.EcoN10ORF171P) and Herpetosiphon aurantiacus S subunit (S.HauORF5277P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KKLGEIAKVSSGGTPSRSNPEYWNGGIPWVKTGEVNFNEITDTEEKITEEGLKNSSAKLFPKGTLLMAMY
GQGKTRGRVAILGIEAATNQACAAILPNDGINPDFLFYYLQSSYEELRDLSNGGGQPNLNAGLIKSIEIP
VPPLDEQQKIAAFLSAIDAKIDALEQKLELLQELKKSLMQQLFT
>gnl|CDD|341177 cd17288, RMtype1_S_LlaAI06ORF1089P_TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Lactococcus lactis S subunit (S.LlaAI06ORF1089P) TRD1-CR1 and Bacillus subtilis B4071 S subunit (S2.BsuCC16ORF609P) TRD2-CR2. The recognition sequences of Lactococcus lactis S subunit (S.LlaAI06ORF1089P) and Bacillus subtilis B4071 S subunit (S2.BsuCC16ORF609P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WEVKKLGDLLKIKNGKDYKHLEDGNYPVYGSGGIMGYVNDYLYDGESVLIGRKGTIDKPLYVNGPFWTVD
TMFYTEIKKNNDPKFLYYLLKTIDFKKYNEATGVPSLTQTTLNKIKIPIPPLEEQQKIASILDKLDAKDA
LIELQEKLLEKLKQYKLALMQEL
>gnl|CDD|341178 cd17289, RMtype1_S_BamJRS5ORF1993P-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Bacillus amyloliquefaciens JRS5 S subunit (S.BamJRS5ORF1993P) TRD1-CR1 and Bacillus pumilus Jo2 S subunit (S.BpuJo2I) TRD1-CR1. The recognition sequences of Bacillus amyloliquefaciens JRS5 S subunit (S.BamJRS5ORF1993P) and Bacillus pumilus Jo2 S subunit (S.BpuJo2I) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WEWKKLGDIAEITSSKRIFKSEYVDSGIPFYRSKEIIELFNGEEISTELFISEERYEEIKSKYGVPKKGD
ILITSVGTIGIPYLVKNDDPFYFKDGNLTWFKNIKDINSKFLYYWFQSSIFKNQINSITIGSTQKALTIE
KLKKTKIPLPPLEEQKKIVSILSALDEKIDLNKKQLQKLEELAKTLFQYWF
>gnl|CDD|341179 cd17290, RMtype1_S_AleSS8ORF2795P_TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Algibacter lectus S subunit (S.AleSS8ORF2795P) TRD1-CR1 and Vibrio parahaemolyticus O1:K33 CDC_K4557 S subunit (S.Vpa4557ORF22590P) TRD2-CR2. The recognition sequences of Algibacter lectus S subunit (S.AleSS8ORF2795P) and Vibrio parahaemolyticus O1:K33 CDC_K4557 S subunit (S.Vpa4557ORF22590P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KKLKRLAKSIKTGTTPPSENEEYYDGGIIPWFTPGDFNGDLILSESKRKLSELAIEDGEARLFPKNSVLV
VGIGATIGKVGYSDKESSSNQQITGIIFNKDINPKFLFYWLSSSKEELENLANGATLPILNQEKLKNIKL
PVPPLNEQQKIVEFLDKKTAKIDALIAKKEQLIELLKEYRQALI
>gnl|CDD|341180 cd17291, RMtype1_S_MgeORF438P-TRD-CR_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.MgeORF438P TRD1-CR1 and TRD2-CR2, and to Escherichia coli G5 S subunit (S.Eco16445ORF5013P) TRD2-CR2 and Acetobacter pasteurianus IFO 3283-01 S subunit (S2.Apa3283ORF14230P) TRD1-CR1. The recognition sequences of Mycoplasma genitalium G-37 S subunit (S.MgeORF438P), Escherichia coli G5 S subunit (S.Eco16445ORF5013P), and Acetobacter pasteurianus IFO 3283-01 S subunit (S2.Apa3283ORF14230P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KKLGEIAEIKKGKQITKKELIENGKYPVIAGGIEPSGYHNEYNREGNTITISASGASAGYVNYWKEPFWA
SDCCYILSSKNELVNKFLYYFLKNKQEEIYSLQRGAGQPHIYKKDIEKLKIPIPPLEEQQKIVEILDKFT
ELTAELPAELEARKKQYEYYR
>gnl|CDD|341181 cd17292, RMtype1_S_LlaA17I_TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to the S subunit TRD2-CR2 regions of Lactococcus lactis subsp. cremoris A17 (S.LlaA17I), Haemophilus influenzae Rd (S.HindORF215P) and Clostridium species ASF502 (S.Csp502ORF478P). Lactococcus lactis subsp. cremoris A17 S subunit (S.LlaA17I) recognizes 5'... CAANNNNNNNNTAYG... 3', while the recognition sequences of Clostridium species ASF502 S subunit (S.Csp502ORF478P) and Haemophilus influenzae Rd S subunit (S.HindORF215P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It also includes TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases, such as Porphyromonas species COT-108 OH1349 Type IIG restriction enzyme/N6-adenine DNA methyltransferase (RM.Psp1349ORF730P) of unknown recognition sequence. It may also include type I DNA methyltransferases
YKIGTFGKEPDAYISRELFEEYKSKYSYPKKGDILISASGTIGRTVIYDGEDAYFQDSNIVWLDNDESKV
LNKFLYYFYQIIKWKKTEGSTIKRLYNDNLLNTKIPVPSLDEQRKIAEFLSLLDALIALLQKKLEKLIAL
KKGLMQYLF
>gnl|CDD|341182 cd17293, RMtype1_S_Ppo21ORF8840P_TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Paenibacillus polymyxa SQR-21 SQR21 S subunit (S.Ppo21ORF8840P) TRD1-CR1, Nitrosococcus halophilus Nc4 S subunit (S.NhaNc4ORF3964P) TRD1-CR1. The recognition sequences of Paenibacillus polymyxa SQR-21 SQR21 S subunit (S.Ppo21ORF8840P) and Nitrosococcus halophilus Nc4 S subunit (S.NhaNc4ORF3964P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This superfamily contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VKLGELGEVVTGNTPSKKNPEYYGGDIPFIKPDDLNNGGIILTSEEYLSEEGAKKARIVPKGSILVTCIG
GSIGKVGIADREVAFNQQINAIIPNKSVDPKFLYYQLLSSKFQLQAIASSTTLPIINKSKFEKIEIPLPP
LEEQKRIVAKLDKLFALIDKLEESLEELDELLKSLFQSAF
>gnl|CDD|341183 cd17294, RMtype1_S_MmaC7ORF19P_TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Methanococcus maripaludis C7 S subunit (S.MmaC7ORF19P) TRD1-CR1 and Mycoplasma gallinaceum S subunit (S3.Mme68BORF1125P) TRD2-CR2. The recognition sequences of Methanococcus maripaludis C7 S subunit (S.MmaC7ORF19P) and Mycoplasma gallinaceum S subunit (S3.Mme68BORF1125P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WEWKTLGEIAKIFSGGTPSTSNPEYWDGGTIPWLSSGEVNFKEIYETEKRITEEGLKNSSAKWIPKNSVL
IALAGQGKTRGTVAILKIPLTTNQSLAAIEPDEEIANSRFLYYNLSSRYEELRSLSGGGGRGGLNLKIIK
SLPIPLPPLEEQKKIVAILDKFDALINDLKEGLPALLELRQKQYEYLR
>gnl|CDD|341184 cd17296, RMtype1_S_MmaC5ORF1169P_TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Methanococcus maripaludis C5 S subunit (S.MmaC5ORF1169P) TRD1-CR1, and Methanobacterium formicicum S subunit (S.Mfo3637ORF3708P) TRD2-CR2. The recognition sequences of Methanococcus maripaludis C5 S subunit (S.MmaC5ORF1169P) and Methanobacterium formicicum S subunit (S.Mfo3637ORF3708P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KKLGEICSIQSGGTPSRSKKEYWNNGTIPWVKISDCKNKYVDETEEFITEEGLNNSSAKLLKKGTILIAI
FATIGKVGILKIEATTNQAIAGIKPKNKSINPKYLYYYLKSLYEKFLSLGRGVAQNNINLSILKNLKIPL
PPLEEQQRIVAILDKFEKLINKRQEGLQLLDELVKSLFEEMF
>gnl|CDD|341209 cd17297, AldB-like, proteins similar to alpha-acetolactate dehydrogenase. The structure of this domain displays an alpha-beta-beta-alpha four layer topology, with an H(x)H(x)nH motif (x could be any residue, n could be 9 or 10) that coordinates a zinc ion. The proteins are homologous to bacterial alpha-acetolactate decarboxylase (AldB, E.C. 4.1.1.5), which converts acetolactate into acetoin
NNTLYQVSTIGALLPGVYDGTYTLKELLKHGDFGLGTFDGLDGELIILDGKAYQAKADGSVEKVPDDETT
PFANVTFFEPDLTVTLKGRTGLEDLEAALDKLLPSKNVFYAIRIDGTFGKVKTRSVPKQEKPYPPLAEVA
KWQKEFEFENVPGTLVGFYTPEYPGGINVPGYHLHFLSDDRKFGGHVLDFTTVEGEVYIQVAEKLYLIL
>gnl|CDD|341210 cd17298, DUF1907, proteins similar to putative ester hydrolase C11orf54/PTD012. The structure of this domain displays an alpha-beta-beta-alpha four layer topology, with an HxHxxxxxxxxxH motif (x could be any residue) that coordinates a zinc ion, and an acetate anion at a site that may support the enzymatic activity of a ester. In vitro hydrolytic activity towards para-nitrophenylacetate for the human enzyme was reported. The proteins are homologous to bacterial alpha-acetolactate decarboxylase (AldB, E.C. 4.1.1.5), which converts acetolactate into acetoin
EELAAVLQDGLKKNFEEVSVSVVDCPDLTQEPFNLAAPGLCGSPRIADVGGVPYLLPLPQLDKVYDLKDI
AKLMGLPDGFIIGAGAGPFPVVGVNCELMPNLSISGGGVVTNGSRIAKVDPDNGSCELEKLPDSETRFAL
LGNLFASEGKPGKVLKVKAKKRTGEDNFITCIRKALAEHYGDKPVGLGGVFLIKKGKAKLHVMPDFSKTP
LNSDEDVNNWLKFFEMSAPLVCLGVLVSHDPGLDLRLEHTHCFSDHGEGGHYHYDTTPDTVEYEGYFNVA
EKLYRID
>gnl|CDD|341211 cd17299, acetolactate_decarboxylase, alpha-acetolactate decarboxylase. alpha-acetolactate decarboxylase (AldB, E.C. 4.1.1.5) converts acetolactate ((2S)-2-hydroxy-2-methyl-3-oxobutanoate) into acetoin ((3R)-3-hydroxybutan-2-one) and CO(2). Acetoin may be secreted by the cells, perhaps in order to control the internal pH. AldB may function as a regulator in valine and leucine biosynthesis and in catalyzing the second step of the 2,3-butanediol pathway. The structure of this domain displays an alpha-beta-beta-alpha four layer topology, with an HxHxxxxxxxxxxH motif (x could be any residue) that coordinates a zinc ion
MNTLYQYSTIGALMAGVYDGTLTVGELLKHGDFGLGTFDGLDGEMIVLDGVAYQARADGSVREVDDDETT
PFAVVTFFEPDKTFTLENVTSLEELEALLDELLPSKNLFYAIRIDGTFKSVKTRSVPKQEKPYPPLAEVA
KNQPEFTFENVEGTLVGFYTPEYFQGINVPGYHLHFLSDDRKFGGHVLDFELEEGTVEIQVLDNFELHLP
TTEEFLAADLSDDLAEEIEKVE
>gnl|CDD|340437 cd17300, PIPKc_PIKfyve, Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in 1-phosphatidylinositol-3-phosphate 5-kinase and similar proteins. 1-phosphatidylinositol-3-phosphate 5-kinase (EC 2.7.1.150) is also called FYVE finger-containing phosphoinositide kinase, PIKfyve, phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase). It forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] by catalyzing the phosphorylation of phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) on the fifth hydroxyl of the myo-inositol ring. Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. PIKfyve is vital in early embryonic development. It forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, playing a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human Ether-a-go-go-Related Gene (hERG) channels. This family also includes the yeast ortholog of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal catalytic lipid kinase domain related to PtdInsP kinases (or the PIPKc domain)
TKFTCTIYFAEQFHALRSLYCGGEDDFIRSLSRCVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFL
DFAPAYFEYMAKALFHKRPSLLAKILGVYRISVKNSTTNKTSKQDLLVMENLFYGRNISQVYDLKGSLRN
RYVNVAEDEDSVLLDENFLEYTKGSPLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGIDEEKKELV
VGIIDYIRTYTWDKKLESWVKSLGILGGGGEPTVISPELYKKRFREAMDKYF
>gnl|CDD|340438 cd17301, PIPKc_PIP5KI, Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I phosphatidylinositol 4-phosphate (PtdIns(4)P) 5-kinases (PIP5KI) and similar proteins. PIP5KIs, also known as PIPKIs, or PI4P5KIs, phosphorylate the head group of phosphatidylinositol 4-phosphate (PtdIns4P) to generate phosphatidylinositol 4,5-bisphosphate (PtdIns4,5P2), an essential lipid molecule in various cellular processes. Three distinct PIP5KIs have been characterized in erythrocytes, PIP5K1alpha, PIP5K1beta, and PIP5K1gamma isoforms
SELMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRE
LFGIKPDDYLLSLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTL
LPKFYGLYCYQSGGKNIRFVVMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPE
GILLEPDTYDALLKTIQRDCRVLESFKIMDYSLLLGVHNLGGIPARNSKGERLLLFIGIIDILQSYRLKK
KLEHTWKSVVHDGDTVSVHRPSFYAERFQNFMANTVFKKI
>gnl|CDD|340439 cd17302, PIPKc_AtPIP5K_like, Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana phosphatidylinositol 4-phosphate 5-kinases (PIP5Ks) and similar proteins. PIP5K (EC 2.7.1.68), also known as PtdIns(4)P-5-kinase, or diphosphoinositide kinase, phosphorylates phosphatidylinositol-4-phosphate to produce phosphatidylinositol-4,5-bisphosphate as a precursor of two second messengers, inositol-1,4,5-triphosphate and diacylglycerol, and as a regulator of many cellular proteins involved in signal transduction and cytoskeletal organization. The family includes several PIP5Ks from Arabidopsis thaliana. AtPIP5K1 is involved in water-stress signal transduction. AtPIP5K2 acts as an interactor of all five Arabidopsis RAB-E proteins but not with other Rab subclasses residing at the Golgi or trans-Golgi network. AtPIP5K3 is a key regulator of root hair tip growth. AtPIP5K4 and AtPIP5K5 are type B PI4P 5-kinases expressed in pollen and have important functions in pollen germination and in pollen tube growth. AtPIP5K6 regulates clathrin-dependent endocytosis in pollen tubes. AtPIP5K9 interacts with a cytosolic invertase to negatively regulate sugar-mediated root growth
SYDLMLNLQLGIRYSVGKIAPVARRDLKPSDFDPKAKQWFPFPGSGSTPPPHQSSDFKWKDYCPMVFRNL
RELFGIDAADYMLSLCGDDALRELSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKHVKAYE
NTLLTKFFGVHRVKPVGGRKVRFVVMGNLFCTELRIHRRFDLKGSTHGRTTGKPESEIDPNTTLKDLDLD
FKFRLEKGWRDALMRQIDADCAFLEALRIMDYSLLLGVHFRAGDSTGEPYDVVLYFGIIDILQEYNISKK
LEHAYKSLQYDPASISAVDPKLYSRRFRDFIRKV
>gnl|CDD|340440 cd17303, PIPKc_PIP5K_yeast_like, Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast phosphatidylinositol 4-phosphate 5-kinases (PIP5Ks) and similar proteins. PIP5K (EC 2.7.1.68), also known as PtdIns(4)P-5-kinase, or diphosphoinositide kinase, phosphorylates phosphatidylinositol-4-phosphate to produce phosphatidylinositol-4,5-bisphosphate as a precursor of two second messengers, inositol-1,4,5-triphosphate and diacylglycerol, and as a regulator of many cellular proteins involved in signal transduction and cytoskeletal organization. The family includes Saccharomyces cerevisiae PIP5K MSS4, Schizosaccharomyces pombe PIP5K Its3. MSS4 is required for organization of the actin cytoskeleton in budding yeast. Its3 is involved, together with the calcineurin ppb1, in cytokinesis of fission yeast
YVLMYNMLTGIRVAVSRCAAKVDRELTDADFKAVHKFSFDITGNELTPSSKYDFKFKDYAPWVFRFLREL
FGIDPADYLMSLTGKYILSELGSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPNTL
LSQFYGLHRVKMPRGRKIHFVVMNNLFPPHRDIHQTFDLKGSTVGRETPEDKLAKGPRATLKDLNWLRRK
RKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGIHDLDGGFQATDENNEPGDEIYYLGIIDILTPY
NAKKKLEHFFKSLRHDRHTISAVPPKEYARRFLKFIED
>gnl|CDD|340441 cd17304, PIPKc_PIP5KL1, Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol 4-phosphate 5-kinase-like protein 1 (PIP5KL1) and similar proteins. PIP5KL1 (EC 2.7.1.68), also known as PI(4)P 5-kinase-like protein 1, or PtdIns(4)P-5-kinase-like protein 1, may act as a scaffold to localize and regulate type I PI(4)P 5-kinases to specific compartments within the cell, where they generate PI(4,5)P2 for actin nucleation, signaling and scaffold protein recruitment, and conversion to PI(3,4,5)P3
HEFYSLTCMMKEGLRAAIQNSIDVPPKESLSDDDYTEVLTQVIPKHKGFEFRTYAGPVFATLRQSLGISE
KEYQNSLSPDEPYLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHLENYPHSLLVKFL
GVHSIKLPGKKKKYFIVMQSVFYPDERINERYDIKGCQVSRYTDPEPEGSQIIVVLKDLNFEGNSINLGQ
QRSWFLRQVEIDTEFLKGLNVLDYSLLVGFQPLHSDENRRLLPNYKNALHVVDGPEYRYFVGIIDIFTVY
GLRKRLEHLWKSLRYPGQSFSTVSPEKYARRFCQWVEDH
>gnl|CDD|340442 cd17305, PIPKc_PIP5KII, Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II phosphatidylinositol 5-phosphate 4-kinase (PIP5KII) and similar proteins. PIP5KIIs, also known as PIPKIIs, or PI4P5KIIs, are responsible for the synthesis of phosphatidylinositol-4,5-bisphosphate (PtdIns4,5P2), an essential lipid molecule in various cellular processes, from phosphatidylinositol-5-phosphate (PtdIns5P). Three distinct PIP5KIs have been characterized in erythrocytes, PIP5K2A, PIP5K2B, and PIP5K2C isoforms
PLLSVFMWGINHSINELSHVPIPVMLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERF
GIDDDDYLNSLTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIVERHGKTLL
PQYLGMYRITVNGVETYLVVMRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKI
YIGDEAKAKLLETLKRDVEFLAKLNLMDYSLLVGIHDCIYFMAIIDILTHYGAKKRAAHAAKTVKHGAGA
EISTVKPEQYAKRFLEFISK
>gnl|CDD|340443 cd17306, PIPKc_PIP5K1A_like, Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol 4-phosphate 5-kinase type-1 alpha (PIP5K1alpha) and similar proteins. PIP5K1alpha (EC 2.7.1.68), also termed PIP5K1A, or PtdIns(4)P-5-kinase 1 alpha, or 68 kDa type I phosphatidylinositol 4-phosphate 5-kinase alpha, or PIPKI-alpha, catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). It mediates extracellular calcium-induced keratinocyte differentiation. Unlike other type I phosphatidylinositol-4-phosphate 5-kinase (PIPKI) isoforms, PIP5K1alpha regulates directed cell migration by modulating Rac1 plasma membrane targeting and activation. This function is independent of its catalytic activity, and requires physical interaction of PIP5K1alpha with the Rac1 polybasic domain. The family also includes testis-specific PIP5K1A and PSMD4-like protein, also known as PIP5K1A-PSMD4 or PIPSL. It has negligeable PIP5 kinase activity and binds to ubiquitinated proteins
TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRY
FRELFGIRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNP
RTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQD
IPDGLFLDSDMYNALCKTLQRDCLVLQSFKIMDYSLLVGIHNIDARRGGTIETDDQMGGIPARNSKGERL
LLYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPL
>gnl|CDD|340444 cd17307, PIPKc_PIP5K1B, Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol 4-phosphate 5-kinase type-1 beta (PIP5K1beta) and similar proteins. PIP5K1beta (EC 2.7.1.68), also known as PtdIns(4)P-5-kinase 1 beta, or protein STM-7, or PIP5K1B, is encoded by the Friedreich's ataxia (FRDA) gene, STM7. FRDA is a progressive neurodegenerative disease characterized by ataxia, variously associating heart disease, diabetes mellitus, and/or glucose intolerance. PIP5K1beta is an enzyme functionally linked to actin cytoskeleton dynamics and it phosphorylates phosphatidylinositol 4-phosphate (PtdIns4P) to generate phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)
SAIKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRE
LFGIKPDDYLYSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTL
LPKFYGLYCMQSGGINIRIVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHD
GLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGIHVLGGIPAKNHKGEKLLLFMGIIDILQSYRLMK
KLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKVQ
>gnl|CDD|340445 cd17308, PIPKc_PIP5K1C, Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (PIP5K1gamma) and similar proteins. PIP5K1gamma(EC 2.7.1.68), also known as PtdIns(4)P-5-kinase 1 gamma, or PIP5K1gamma, or PIPKIgamma, or PtdInsPKI gamma, is a phosphatidylinositol-4-phosphate 5-kinase that catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), which is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. PIP5K1gamma is required for epidermal growth factor (EGF)-stimulated directional cell migration. It also modulates adherens junction and E-cadherin trafficking via a direct interaction with mu 1B adaptin
SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYPDFRFKTYAPVAFRYFR
ELFGIRPDDYLYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRT
LLPKFYGLYCVQSGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDMP
EGLMLDADTFSALVKTLQRDCLVLESFKIMDYSLLLGVHNIGGIPAVNGKGERLLLYIGIIDILQSYRLI
KKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSNTVFRKSSS
>gnl|CDD|340446 cd17309, PIPKc_PIP5K2A, Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (PIP5K2A) and similar proteins. PIP5K2A (EC 2.7.1.149), also known as PIP4K2A, or 1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha, or diphosphoinositide kinase 2-alpha, or PIP5KIII, or phosphatidylinositol 5-phosphate 4-kinase type II alpha, or PI(5)P 4-kinase type II alpha, or PIP4KII-alpha, or PtdIns(4)P-5-kinase C isoform, or PtdIns(5)P-4-kinase isoform 2-alpha, catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), one of the key metabolic crossroads in phosphoinositide signaling. It is possibly involved in a mechanism protecting against tardive dyskinesia-inducing neurotoxicity. PIP5K2A is associated with schizophrenia. It controls the function of KCNQ channels via phosphatidylinositol-4,5-bisphosphate (PIP2) synthesis, and plays a potential role in the regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptors
KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPM
VFRNLRERFGIDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYI
VECHGNTLLPQFLGMYRLTVDGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDN
DFINDGQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIHDVVYFMAIIDILTHYDAKKKAAHAA
KTVKHGAGAEISTVNPEQYSKRFLDFITS
>gnl|CDD|340447 cd17310, PIPKc_PIP5K2B, Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol 5-phosphate 4-kinase type-2 beta (PIP5K2B) and similar proteins. PIP5K2B (EC 2.7.1.149), also known as 1-phosphatidylinositol 5-phosphate 4-kinase 2-beta, or diphosphoinositide kinase 2-beta, or phosphatidylinositol 5-phosphate 4-kinase type II beta, or PI(5)P 4-kinase type II beta, or PIP4KII-beta, or PtdIns(5)P-4-kinase isoform 2-beta, or PIP5KIIbeta, or PIP4K2B, participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. It directly regulates the levels of two important phosphoinositide second messengers, PtdIns5P and phosphatidylinositol-(4,5)-bisphosphate (PtdIns(4,5)P2), one of the key metabolic crossroads in phosphoinositide signaling. It regulates the levels of nuclear PtdIns5P, which in turn modulates the acetylation of the tumour suppressor p53. It also interacts with and modulates nuclear localization of the high-activity PtdIns5P-4-kinase isoform PIP4Kalpha. Moreover, PIP5K2B is a molecular sensor that transduces changes in GTP into changes in the levels of the phosphoinositide PtdIns5P to modulate tumour cell growth
CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYC
PMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQ
FIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFK
DNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVVYFMAIIDILTPYDAKKKAAH
AAKTVKHGAGAEISTVNPEQYSKRFNEFMSN
>gnl|CDD|340448 cd17311, PIPKc_PIP5K2C, Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma (PIP5K2C) and similar proteins. PIP5K2C (EC 2.7.1.149), also known as 1-phosphatidylinositol 5-phosphate 4-kinase 2-gamma, or PI5P4Kgamma, or diphosphoinositide kinase 2-gamma, or phosphatidylinositol 5-phosphate 4-kinase type II gamma, or PI(5)P 4-kinase type II gamma, or PIP4KII-gamma, or PIP4K2C, may play an important role in the production of phosphatidylinositol bisphosphate (PIP2) in the endoplasmic reticulum. It contributes to the development and maintenance of epithelial cell functional polarity. It also plays a role in the regulation of the immune system via mTORC1 signaling. Moreover, PIP5K2C is involved in arsenic trioxide (ATO) cytotoxicity. It mediates PIP2 generation required for positioning and assembly of bipolar spindles and alteration of PIP5K2C function by ATO may thus lead to spindle abnormalities
PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERF
GIDDQDYQVSLTRSPPYSESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQ
FLGMYRLSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYV
GEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIHDVVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEI
STVHPEQYAKRFLDFITN
>gnl|CDD|340870 cd17312, MFS_OPA_SLC37, Organophosphate:Pi antiporter/Solute Carrier family 37 of the Major Facilitator Superfamily of transporters. Organophosphate:Pi antiporters (OPA) are integral membrane proteins responsible for the transport of specific organophosphates or sugar phosphates across biological membranes with the simultaneous translocation of inorganic phosphate into the opposite direction. The OPA family is also called solute carrier family 37 (SLC37) in vertebrates. Members include glucose-6-phosphate (Glc6P) transporter (also called translocase or exchanger), glycerol-3-phosphate permease, 2-phosphonopropionate transporter, phosphoglycerate transporter, as well as membrane sensor protein UhpC from Escherichia coli. UhpC is both a sensor and a transport protein; it recognizes external Glc6P and induces transport by UhpT, and it can also transport Glc6P. Vertebrates contain four SLC37 or sugar-phosphate exchange (SPX) proteins: SLC37A1 (SPX1), SLC37A2 (SPX2), SLC37A3 (SPX3), and SLC37AA4 (SPX4). The OPA/SLC37 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RWRIFLGVFLGYAAYYVCRKNFSVAKPPIVEEIGLSKDDLGIIGSAFLIAYAVGKFISGFLSDRSNIRRF
MSAGLLLSALANIFMGFSTSLWFFAVLWGLNGLFQSMGWPPCVKLLGNWFSKKERGTVYGIWSTSHNFGG
ILAPILAASLASYYGWRAAFLVPGIVGLVVAIILFFFLRDSPPYVWVLSLAYAFVYIVRYACLDWGPLYL
YEVKGYSLIDAGWFSSLYEVGGIAGTILAGLLSDKLFGGRRAPIAVIYMLLMTLSLALFWFFPHNKLLSI
VLLFLIGFFVGGPINLIGGAAAQDIGRKEAAGTATGFVGLFGYLGASLAGLPLGYIIDHYGWSTVFYFLI
SAALLSVLLLLSLW
>gnl|CDD|340871 cd17313, MFS_SLC45_SUC, Solute carrier family 45 and similar sugar transporters of the Major Facilitator Superfamily of transporters. This group includes the solute carrier 45 (SLC45) family as well as plant sucrose transporters (SUCs or SUTs) and similar proteins such as Schizosaccharomyces pombe general alpha-glucoside permease. the SLC45 family is composed of four (A1-A4) vertebrate proteins as well as related insect proteins such as Drosophila sucrose transporter SCRT or Slc45-1. Members of this group transport sucrose and other sugars like maltose into the cell, with the concomitant uptake of protons (symport system). Plant sucrose transporters are crucial to carbon partitioning, playing a key role in phloem loading/unloading. They play a key role in loading and unloading of sucrose into the phloem and as a result, they control sucrose distribution throughout the whole plant and drive the osmotic flow system in the phloem. They also play a role in the exchange of sucrose between beneficial symbionts (mycorrhiza and Rhizobium) as well as pathogens such as nematodes and parasitic fungi. There are nine sucrose transporter genes in Arabidopsis and five in rice. Vertebrate SLC45 family proteins have been implicated in the regulation of glucose homoeostasis in the brain (SLC45A1), with skin and hair pigmentation (SLC45A2), and with prostate cancer and myelination (SLC45A3). Mutations in SLC45A2, also called MATP (membrane-associated transporter protein) or melanoma antigen AIM1, cause oculocutaneous albinism type 4 (OCA4), an autosomal recessive disorder of melanin biosynthesis that results in congenital hypopigmentation of ocular and cutaneous tissues. The SLC45 family and related sugar transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LFLLGFGFFGIEFGWALENSYVPPILQTLGLSHALIGFVWTLGPILGLFVQPLVGSLSDRCNSRIGRRRP
FILVGAPLAALGLILIPNAADIGLALGDGPRTWALVLFVLGIVLLDFAMNVCQGPVRALLPDLVPPEQRS
KANGIINFMGGLGGVLGYLLGAILWDHNWFGFALGGNLKVPFYIGAIILLVCVLVTLFFVKEPPLSPEAG
EHSENPSLGEVLKSLLKLLKIMPRSLLRLLLVIFFWWIAFFPFELFFTDYMGEEVYHGTSAASSHYGAGV
RMGAWGLLIFSLAFLIFSLPIGKLGKKIGRKKVYLIGLVLFAVGMALMALVHNVTVALVLFALGGIGWAT
ININPYPLVSDYHSESGRGQGTDTGLLNLAISLAQILVSLLAGPIIDVKGYGTVFPVAAVASFLSLVGAL
F
>gnl|CDD|340872 cd17314, MFS_MCT_like, Monocarboxylate transporter (MCT) family and similar transporters of the Major Facilitator Superfamily. The group is composed of the Monocarboxylate transporter (MCT) family in animals and similar transporters from fungi, plants, archaea, and bacteria. MCT is also called Solute carrier family 16 (SLC16 or SLC16A). It is composed of 14 members, MCT1-14. MCTs play an integral role in cellular metabolism via lactate transport and have been implicated in metabolic synergy in tumors. MCTs have been found to facilitate the transport across the plasma membrane not only of monocarboxylates (MCT1-4), but also thyroid hormones (MCT8/10), and aromatic acids (MCT10). Yeast MCT homologous (Mch) proteins are not involved in the uptake of monocarboxylates; their substrates are not known. The MCT-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RWFVLYVSFLLSAMSTGFILSWSLFYQPWQDAFGYSSSQIATAASLSNLGMLLTQPILGFIADSFGPRPL
MALAGIMVLAGYTYLSYVFNSFPLSYACFVFIGAGTGILYGSAVLVTTQYFPDTKGLALGLPTTGYSLGL
VLGSPLLRILWVFYGLALVYTILGILAAIVLSVVSLLGFKEPPDNQARLHVQKKKTQTMGEIFRDKVFWI
LFIAIFLVLIGGFLFIANMASLVRSLQLDAPSFVTKLMSIYGLFNAFGRLLWGIVADFFGGRLSTLSILL
TILGLGLCAFLFLLKMTPVGLVLTGSLLGFSYGGLFTVYPATVSTVFGTESFATLYGILLFAPAIGSILG
PMLGAKFYDRTPSYISAVYIYAVIVFLASAILLAV
>gnl|CDD|340873 cd17315, MFS_GLUT_like, Glucose transporters (GLUTs) and other similar sugar transporters of the Major Facilitator Superfamily. This family is composed of glucose transporters (GLUTs) and other sugar transporters including fungal hexose transporters (HXT), bacterial xylose transporter (XylE), plant sugar transport proteins (STP) and polyol transporters (PLT), H(+)-myo-inositol cotransporter (HMIT), and similar proteins. GLUTs, also called Solute carrier family 2, facilitated glucose transporters (SLC2A), are a family of proteins that facilitate the transport of hexoses such as glucose and fructose. There are fourteen GLUTs found in humans; they display different substrate specificities and tissue expression. They have been categorized into three classes based on sequence similarity: Class 1 (GLUTs 1-4, 14); Class 2 (GLUTs 5, 7, 9, and 11); and Class 3 (GLUTs 6, 8, 10, 12, and HMIT). GLUT proteins are comprised of about 500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 transmembrane segments. The GLUT-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VAALGGLLFGYDLGVINGALLYIAKDLGFGLSTSLQGLVVSSLLLGAAIGSLFGGPLADRFGRRKSLLIA
AVLYVIGALLSALAPNVWVLIVGRFLLGLGVGLASVLVPLYISEIAPAKIRGALGTLNQLMITFGILLAY
LLGLALSLSPPGWWRLMFALAAVPALLQLLLMFFLPESRALLVGVGLQLLQQLTGINAVMYYAPTIFKSA
GGGTASILASIIVGVVNLLATLVAIRLVDKVGRRPLLLIGFAGMAASLLLLAIAFLLPALAKAAGWLALL
GILLYIAAFAMGAGPVPWLLLSEIFPLRIRGKGMAIATLVNWIFNFIVGLTFLIMVSTIGLAGVFIFFAA
VCLLALVFVFFFVPE
>gnl|CDD|340874 cd17316, MFS_SV2_like, Metazoan Synaptic vesicle glycoprotein 2 (SV2) and related small molecule transporters of the Major Facilitator Superfamily. This family is composed of metazoan synaptic vesicle glycoprotein 2 (SV2) and related small molecule transporters including those that transport inorganic phosphate (Pht), aromatic compounds (PcaK and related proteins), proline/betaine (ProP), alpha-ketoglutarate (KgtP), citrate (CitA), shikimate (ShiA), and cis,cis-muconate (MucK), among others. SV2 is a transporter-like protein that serves as the receptor for botulinum neurotoxin A (BoNT/A), one of seven neurotoxins produced by the bacterium Clostridium botulinum. BoNT/A blocks neurotransmitter release by cleaving synaptosome-associated protein of 25 kD (SNAP-25) within presynaptic nerve terminals. Also included in this family is synaptic vesicle 2 (SV2)-related protein (SVOP) and similar proteins. SVOP is a transporter-like nucleotide binding protein that localizes to neurotransmitter-containing vesicles. The SV2-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLLAGLGWFFDAYDFFLIGFVAPVLAAEFSLGLSLLQTGLLFAAGFLGRPIGALLFGYLGDRIGRKKALI
LTLLLFGLATLLIGLLPTPILLLVLRFLQGIGIGGEYPGASTYVAEFAPSKRRGFALGLLQSGWALGALL
AALVASLLIPLLSGDWGWRILFLIGALPALLALLLRRRTLLLILLWFFISFGYYGLTTFLPTYLQTVLGL
SPATSSLYLLLISLGALVGALIAGLLSDRIGRKKTLVIGLILSGILALPLFYLLSGSPTLLLLLLFILSF
FVGGVWGALYAYLAELFPTEVRATGVGLSYNLGRLGGGGAPPLIALLLASTGGTGVPALILALLAIVALI
VAL
>gnl|CDD|340875 cd17317, MFS_SLC22, Solute carrier 22 (SLC22) family of organic cation/anion/zwitterion transporters of the Major Facilitator Superfamily. The Solute carrier 22 (SLC22) family of organic cation/anion/zwitterion transporters includes organic cation transporters (OCTs), organic zwitterion/cation transporters (OCTNs), and organic anion transporters (OATs). SLC22 transporters interact with a variety of compounds that include drugs of abuse, environmental toxins, opioid analgesics, antidepressant and anxiolytic agents, and neurotransmitters and their metabolites. The SLC22 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWEFDYSVSESTIVTEWDLVCDRDWLVALVQTIFFLGVLIGSLLFGYLADRFGRRPVLLLGLVLQIVCGV
LSAFSPSYELFLVLRFLVGVTSAGIFTVGFVLGMEIVGPKYRSFVGILFGLFWALGYMLLALLAYLIRDW
RWLQLAISLPGLLFLLLLWWLPRRTIIVGLIWFVTSLVYYGLSLNSSNLGGNLYLNFFLSGLVEIPAYFL
ALLLLDRLGRRWTLSGSLLLAGLACLVTALLPDDENTLALTLALVGKFAISAAFSVIYLYTAELYPTVVR
NTGVGLCSTVARVGAILAPFIVLLGKIGPLLPLIIFGVLALLGGLLTLLLP
>gnl|CDD|340876 cd17318, MFS_SLC17, Solute carrier 17 (SLC17) family of the Major Facilitator Superfamily of transporters. The Solute carrier 17 (SLC17) family is primarily involved in the transport of organic anions. There are nime human proteins belonging to this family including: the type I phosphate transporters (SLC17A1-4) that were initially identified as sodium-dependent inorganic phosphate (Pi) transporters but are now known to be involved in tha transport of organic anions; lysosomal acidic sugar transporter (SLC17A5 or sialin), vesicular glutamate transporters (VGluT1#3 or SLC17A7, SLC17A6, and SLC17A8, respectively), and a vesicular nucleotide transporter (VNUT or SLC17A9). SLC17A1 and SLC17A3 have roles in the transport of urate and para-aminohippurate, respectively. The SLC17 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
AILLFLGFAVVYAMRVNLSVAIVAMVNSTATHDNNNTSTDKDTLPVEAPEFDWSEKTQGIILSSFFYGYI
LTQIPGGYLAEKYGAKRVLGYSILITALLTLLTPLAARGGYGALIVLRILQGLAQGVTFPAMHALWAKWA
PPLERSRLTSIAYSGSQFGTVIAMPLSGFLCESLGWPSIFYIFGGLGLLWCLLWFFLVLPVWAIVVAHFG
HNWGFYTLLTELPTYMSDVLHFNIKSNGFLSSLPYLAMWICSIVGGYLADWLRSRGILSTTTVRKLFTSI
GFLGPGVFLIALGYLGSNATLAVVFLTLSVGLSGACYSGFLVNHLDLAPNYAGTLMGITNTAATIAGIIS
PLIVGAIVKNDQTIGQWRIVFFISAAIYILGAIFYLIFG
>gnl|CDD|340877 cd17319, MFS_ExuT_GudP_like, Hexuronate transporter, Glucarate transporter, and similar transporters of the Major Facilitator Superfamily. This family is composed of predominantly bacterial transporters for hexuronate (ExuT), glucarate (GudP), galactarate (GarP), and galactonate (DgoT). They mediate the uptake of these compounds into the cell. They belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RWRIIPLLFLAYVINYLDRVNISVAAPTIMKDLGLSPTQYGLIASAFFLGYALFQVPGGWLLDRFGARKV
LAVSMLLWSLFTALTGFATSLTSLYVLRFLLGVAEAGFFPGAIKALAEWFPARERGRATGLFNSGAPLGA
AIGPPLSGWLLLLFGWRWAFIIEGLLGLLLAVLWWFYLRQVWGLALGYFGINYALYGLLTWLPTYLKQAR
GFSLKQVGLLAAIPFLAGAIGMILGGRLSDRLLRGARRLVIIIGLLLAAVGLLLAYLTTSPVVAVILLSL
AGFGIGAASPVFWSLPADLLPGEAAATAGGLINSGGNLGGFVAPLLIGYLVDATGSYTAAFLFLAAVALL
AALLVLLL
>gnl|CDD|340878 cd17320, MFS_MdfA_MDR_like, Multidrug transporter MdfA and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily. This family is composed of bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as MdfA (also called chloramphenicol resistance pump Cmr), EmrD, MdtM, MdtL, bicyclomycin resistance protein (also called sulfonamide resistance protein), and the uncharacterized inner membrane transport protein YdhC. EmrD is a proton-dependent secondary transporter, first identified as an efflux pump for uncouplers of oxidative phosphorylation. It expels a range of drug molecules and amphipathic compounds across the inner membrane of E. coli. Similarly, MdfA is a secondary multidrug transporter that exports a broad spectrum of structurally and electrically dissimilar toxic compounds. These MDR transporters are drug/H+ antiporters (DHA) belonging to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLLLALLVALGPLAIDMYLPALPAIARDLGASASAVQLTLSAYLLGFALGQLLYGPLSDRFGRRPVLLAG
LLLFILASLLCALASSIEQLLIARFLQGLGAAAGSVVARAIVRDLYSGAELAKIFSLLMMILAIAPALAP
LLGGLLLLFFGWRAIFVFLALLGLLLLLLVLLFLPETLPEEKRKPLLSSLLRAYKRVLKNRRFLGYALAL
GLSFAGLFAYLAAAPFIYIEQLGLSPAQFGLLFALNAIALILGSLLNGRLVRRFGPRRLLRLGLLLLLAA
ALVLLLAALLGGLSLWPLVAPLFLIFFGFGLIFPNATSLALEPFPHVAGTASALLGFLQFLIGALAGALV
GLLPNGTALPMGLLILVLGLLALLLLILL
>gnl|CDD|340879 cd17321, MFS_MMR_MDR_like, Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily. This family is composed of bacterial, fungal, and archaeal multidrug resistance (MDR) transporters including several proteins from Bacilli such as methylenomycin A resistance protein (also called MMR peptide), tetracycline resistance protein (TetB), and lincomycin resistance protein LmrB, as well as fungal proteins such as vacuolar basic amino acid transporters, which are involved in the transport into vacuoles of the basic amino acids histidine, lysine, and arginine in Saccharomyces cerevisiae, and aminotriazole/azole resistance proteins. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. For example, MMR confers resistance to the epoxide antibiotic methylenomycin while TetB resistance to tetracycline by an active tetracycline efflux. MMR-like MDR transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLLAVFLAALDVTIVNVALPTIARDLGASPSQLQWVVNAYLLAFAALLLLAGRLGDRFGRKRVFLIGLAL
FGLASLLCALAPSLAFLIAARALQGIGAAAIMPASLALIAATFPGERRGRALGLWGAVVGIGAALGPLLG
GLLLELFGWRWIFLINVPIGLVALLLARTFSGAVLAAFLLGAALGGLLFLLPLYLQGVLGYSPLQAGLAL
LPLALAMLVAAPLAGRLADRFGPRLVLVAGLLLTAVGLLLLALLGADSSVWLLLPGLVLLGLGLGLFATP
LTNAALSSVPKEKAGAASGILNTARQLGGALGVALLGALLTAGLSANLGDSGVAALLSAAAAAFAAGFHL
AFLVAAALALLAALLALLLP
>gnl|CDD|340880 cd17322, MFS_ARN_like, Yeast ARN family of Siderophore iron transporters and similar proteins of the Major Facilitator Superfamily. The ARN family of siderophore iron transporters includes ARN1 (or ferrichrome permease), ARN2 (or triacetylfusarinine C transporter 1 or TAF1), ARN3 (or siderophore iron transporter 1 or SIT1 or ferrioxamine B permease) and ARN4 (or Enterobactin permease or ENB1). They specifically recognize siderophore-iron chelates are expressed under conditions of iron deprivation. They facilitate the uptake of both hydroxamate- and catecholate-type siderophores. This group also includes glutathione exchanger 1 (Gex1p) and Gex2p, which are proton/glutathione antiporters that import glutathione from the vacuole and exports it through the plasma membrane. The ARN family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LIILFFSLFLCGFAIGLDGQIRYSYQAYATSSFSKHSLLSTINVVNNIVSAVSQPPYAKLSDVFGRLELF
LVSLLLYVVGTIIMAASTNVQTYAAGSVFYNAGYTGLNLLLTLILADFSSLKNRGFASAIPSLPYIITTW
IGGNIAQAALPNSNWRWGYGMWAIILPLSSLPLVLCLLYMQRKARKDGEIKELKNQETEEQTGGLSQNLV
KLFWKLDIFGVILLTAGLGLILVPLTLAGGAKSKWKNSSIIAMIVLGGVLLVAFLLWEAKFAKYPFLPFR
LLKDRTILAACLIDFFYFFSYYIFSDYLYTVLQVAVGESITSATRITNLYSFVSTVAGIFVGFLIRKTRR
YKVLVIIGVPLYIVGMGLLIRYRGGSGSHGGIIGALILIGIGGGLFTYPVQVSVQASVSHQEMAVVTALL
LTVYSIGGAVGAAISGAIWTQTLPKKLLKNLPDSLKATAAYIFPSTFVILSYPWGTPERDAIIESYRYVQ
RILLIVALVFSAPMFALMFFLRNP
>gnl|CDD|340881 cd17323, MFS_Tpo1_MDR_like, Yeast Polyamine transporter 1 (Tpo1) and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily. This family is composed of fungal multidrug resistance (MDR) transporters including several proteins from Saccharomyces cerevisiae such as polyamine transporters 1-4 (Tpo1-4), quinidine resistance proteins 1-3 (Qdr1-3), dityrosine transporter 1 (Dtr1), fluconazole resistance protein 1 (Flr1), and protein HOL1. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. For example, Flr1 confers resistance to the azole derivative fluconazole while Tpo1 confers resistance and adaptation to quinidine and ketoconazole. The polyamine transporters are involved in the detoxification of excess polyamines in the cytoplasm. Tpo1-like MDR transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VFIISFLTFVVTFGSSIYSPALPQIAEDFHVSEEVANLGVSLFVLGFGLGPLIWAPLSELYGRRPVYLVS
LFIFVIFQIGCALAPNIAMLIILRFLQGFFGSSPLAIGAGTIADLFTPEERGKAMGVYSLGPLLGPALGP
IIGGFITQSLGWRWIFWFLAIISGFCLILIFLFLPIVLLLGLYVGLVYAILYLFLTAFPYVFGEVYGFSP
GEVGLMYLPIGIGALIGSIIGGRLSDYYYRRLKKKNGGKPEPEARLPPAFIGAFLFPIGLFIFGWTIYPH
IHWIVPIIGSAFFGFGLMLIFQSSLTYLVDSYPKYAASALAANTLVRSIFAAIFPLFAQPMFNNLGVGWA
FTLLAFISLAMIPIPFIFYKYGKKIR
>gnl|CDD|340882 cd17324, MFS_NepI_like, Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator Superfamily. This family is composed of purine efflux pumps such as Escherichia coli NepI and Bacillus subtilis PbuE, sugar efflux transporters such as Corynebacterium glutamicum arabinose efflux permease, multidrug resistance (MDR) transporters such as Streptomyces lividans chloramphenicol resistance protein (CmlR), and similar proteins. NepI and PbuE are involved in the efflux of purine ribonucleosides such as guanosine, adenosine and inosine, as well as purine bases like guanine, adenine, and hypoxanthine, and purine base analogs. They play a role in the maintenance of cellular purine base pools, as well as in protecting the cells and conferring resistance against toxic purine base analogs such as 6-mercaptopurine. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The NepI-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLALALAAFAIGTTEYVIQGLLPDIARDFGVSVAQAGLLVSAYALGYALGALLLGPLSDRIERRRLLLVL
LLLFILGNLLAALAPSFALLLLARALAGLAHGGFWAIAAAYAADLVPPEKRGRAIGLVFSGLTLGLVLGR
PLGGLLGQLLGWRAAFLAIAVLALLAALLLWRLLPSLPPKKPGSLGLLSSLLLLLRNPRLRLAYLITFLL
FGGFFALYTYLAPFLTDVPGFSSSAIIGLLLLFGVAGVVGSPLAGRLADRGGRRALLIALLLLAAALLLL
TLLGPSPLLLLVGLVLWGLGFFAAHSALQTRVLRLAPEARGLASSLYLAAYNLGGALGAALGGLVLDHGG
WAGVGWVGAALLLLALLLAL
>gnl|CDD|340883 cd17325, MFS_MdtG_SLC18_like, bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily of transporters. This family is composed of eukaryotic solute carrier 18 (SLC18) family transporters and related bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as multidrug resistance protein MdtG, from Bacillus subtilis such as multidrug resistance proteins 1 (Bmr1) and 2 (Bmr2), and from Staphylococcus aureus such as quinolone resistance protein NorA. The family also includes Escherichia coli arabinose efflux transporters YfcJ and YhhS. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The SLC18 transporter family includes vesicular monoamine transporters (VAT1 and VAT2), vesicular acetylcholine transporter (VAChT), and SLC18B1, which is proposed to be a vesicular polyamine transporter (VPAT). The MdtG/SLC18 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LSLALFLDMLGYGIIIPILPLYAESLGASVAQIGLIVAAYALAQLLFSPPAGRLSDRFGRKRLLLLGLLL
LAVSTLLFAFATSYWQLLLARFLQGLASAAVWPAAMALIADIAPPEERGRAMGIFSSAIGLGFLIGPLLG
GLLADALGYRAPFLVCAALALLALVLALLLLPEPRPPPNKRAVSAARLRSGLRLLLRDRRLLALFLAIFV
LAFAFGALEPFLPLYAAELGGLSPAQIGLLFGAQGLASALSQPPAGKLSDRIGRKPLILIGLLLSAVALL
LLPLATSFWLLLLLLALLGLGLGLVFPATLALLADIVPPEGRGTAMGLFNTAFSLGMVLGPLLGGFLYDA
FGFATPFLAAAALLLLAAVLFLLLR
>gnl|CDD|340884 cd17326, MFS_MFSD8, Major facilitator superfamily domain-containing protein 8. Major facilitator superfamily (MFS) domain-containing protein 8 (MFSD8) is also called ceroid-lipofuscinosis neuronal protein 7 (CLN7). It is a polytopic lysosomal membrane protein that may transport small solutes by using chemiosmotic ion gradients. Mutations in MFSD8/CLN7 cause a variant of late-infantile neuronal ceroid lipofuscinoses (vLINCL), a neurodegenerative lysosomal storage disorder. Some variants are associated with nonsyndromic autosomal recessive macular dystrophy. MFSD8/CLN7 belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance -like (SLC46/TetA-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
IYVMYLTMFLSSLQFSIVLTSIWPYLQKIDPTATASFFGWVVAAYSLGQLVFSPVFGYWSNKTSSVKEPL
IVSILIAIVGNILYALAEYFPSNRKYVMLVARFLIGVGAGNVAVLRAYVAAASTLKDRTRAMAVISAAQA
LGFIVGPALQAAFTPIGYPGYVIGIKLRFNMYTAPAWLMAILGIINIILILFFFKEVVCIFLFFVVLFIF
ANLETIGTPLTMDMYGWTREEAVLYNGIILAVSGVLSVLVFLLFKFLSLGLIDERKILLGGLILFFLGFV
VTLPWGITGVILFGLGYPIGNVMLYTLYSKILGPKPQGTMQGVLTASGSLARTLGPIFVTAIYTHFGPRW
TWIITLGLLLLAIILLIVFYKRLV
>gnl|CDD|340885 cd17327, MFS_FEN2_like, Pantothenate transporter FEN2 and similar transporters of the Major Facilitator Superfamily. This family is composed of Saccharomyces cerevisiae pantothenate transporter FEN2 (or fenpropimorph resistance protein 2) and similar proteins from fungi and bacteria including fungal vitamin H transporter, allantoate permease, and high-affinity nicotinic acid transporter, as well as Pseudomonas putida phthalate transporter and nicotinate degradation protein T (nicT). These proteins are involved in the uptake into the cell of specific substrates such as pathothenate, biotin, allantoate, and nicotinic acid, among others. The FEN2-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
KLDLFILPLLCILYFLQYLDKSNISNAAVMGMKEDLKLVGNQYNWGNTVFYVGYIIFELPGNLLLQRFPP
SKWLSVFIVLWGLLTLLTAAVKNFGGLIALRFFLGLFESGVFPGFILYLGMWYKREEQAKRIAFFYAAAG
LGSIFGGLLAYGVFKILGVGGLAGWRWLFIIEGLITIIIGLVIFFWLPDNPSKAWFLTEEEKELAVERLR
ANQTGKGDQKFKWKQIKEAFKDPRTWLLFLFFFCSQITNNGISNFLPLILKSLGFYSLQTNLLSVPIGAL
GAVSLLIAALLSDRFKKRGLFAIFACVLALVGSIILLAAPNPPGAYFAAYILGGGSYAGFPILLSWISSN
CAGYTKRATVLAIMLIFYNVGNIVAPQIFRAGDAPRYIPGNIALLVCACVSIVLSV
>gnl|CDD|340886 cd17328, MFS_spinster_like, Protein spinster and spinster homologs of the Major Facilitator Superfamily of transporters. The protein spinster family includes Drosophila protein spinster, its vertebrate homologs, and similar proteins. Humans contain three homologs called protein spinster homologs 1 (SPNS1), 2 (SPNS2), and 3 (SPNS3). Protein spinster and its homologs may be sphingolipid transporters that play central roles in endosomes and/or lysosomes storage. SPNS2 is also called sphingosine 1-phosphate (S1P) transporter and is required for migration of myocardial precursors. S1P is a secreted lipid mediator that plays critical roles in cardiovascular, immunological, and neural development and function. The spinster-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VAVLFLINLLNYMDRFTIAGVLPDIQSDFLIDDSLAGLLQTVFIISYMVLSPIFGYLGDRYNRKWILAVG
ILIWSAATLLSSFAPNFWQLLLFRALVGIGEASYSPIAPTIIADLFPKEKRTRALGVFYFAIPLGSGLGY
VVGGLVAQATGGWRWAFRVTGVLGVLLAILLLLFVREPPRGAAEGGVMAKSTATSFLADLKALAKNPSFI
LSTLGFTAVSFVTGALAFWAPTFFLRAFGVGDLSSADVGLIFGAITCIAGVLGVLLGGILADRLRRKTPR
ADPLVCAVGLLAAAPFLFLALVLALSNLLLAWVLLFLGEFLLSLNWAPVFAILLYVVIPTRRSTASAIQI
LLSHLLGDAGSPYLIGLISDLLRQNKDSPLAEAASLQYALLLCSFVLVLGGFFFL
>gnl|CDD|340887 cd17329, MFS_MdtH_MDR_like, Multidrug resistance protein MdtH and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily. This family is composed of Escherichia coli MdtH and similar multidrug resistance (MDR) transporters from bacteria and archaea, many of which remain uncharacterized. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. MdtH confers resistance to norfloxacin and enoxacin. MdtH-like MDR transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LWVLLIGSFLNRLGFFMVWPFMAIYLHQQLGLSASIVGLVLALSAVAGIVASLIGGRLADRFGRKPVMLA
GLLLRALGFALLGFAHSPWLFAIALVLTGFGGGLFEPASEAMIADVTTPENRTRAFSLLYWAINLGVAIG
PLLGGLLLLYSFRLLFLAAAVLFLLAALVLLFLLPETRPKRRAAEKTEILRGYKIVLRDRAFLLFLLASF
LISLIYFQLESTLPVYVVEILGLGESLLGLLLALNALLIVLLQFPVARLVERFRLRKILMIGILLFAIGF
AVLAFANTLAVLILAMIVLTLGEMLVFPAVQTLVAALAPPDKRGSYMGFYALAWGLGRAIGPLVGGLLLD
LLGPGLPWLILAALGLIAAALLLGLQ
>gnl|CDD|340888 cd17330, MFS_SLC46_TetA_like, Eukaryotic Solute carrier 46 (SLC46) family, Bacterial Tetracycline resistance proteins, and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of the eukaryotic proteins MFSD9, MFSD10, MFSD14, and SLC46 family proteins, as well as bacterial multidrug resistance (MDR) transporters such as tetracycline resistance protein TetA and multidrug resistance protein MdtG. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. TetA proteins confer resistance to tetracycline while MdtG confers resistance to fosfomycin and deoxycholate. The Solute carrier 46 (SLC46) family is composed of three vertebrate members (SLC46A1, SLC46A2, and SLC46A3), the best-studied of which is SLC46A1, which functions both as an intestinal proton-coupled high-affinity folate transporter involved in the absorption of folates and as an intestinal heme transporter which mediates heme uptake. MFSD10 facilitates the uptake of organic anions such as some non-steroidal anti-inflammatory drugs (NSAIDs) and confers resistance to such NSAIDs. The SLC46/TetA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LFLVVFLDALGFGIVFPVLPFYVREFNKLGASGYYVGLLQSSYSLGQFLASPLWGRLSDRYGRKPVLLLS
LAGSAVSYVLLGLSRNLWLLFLARFLDGLTGGNVSVAQAYIADITDEEERAKAFGIISAAFGLGFILGPA
LGGFLSTPYGYALPFLVAAALALLNLVLVLFFLPPLRRLLLVYFLIALAFAGLESVFSLFLKDRFGFSPS
QIGLLLALVGIAGILAQLLLIPRLAKRLGERKLLRLGLLLAIIGLLLLPFASSVPLLVLAAAILAFGTGI
VFPALSALLSKSVPSKEQGKAQGIIQSLQSLARIIGPLLAGPLYSFLGPGVPFLLAAGLLLIALFLLSL
>gnl|CDD|340889 cd17331, MFS_SLC22A18, Solute carrier family 22 member 18 of the Major Facilitator Superfamily of transporters. Solute carrier family 22 member 18 (SLC22A18) is also called Beckwith-Wiedemann syndrome chromosomal region 1 candidate gene A protein (BWR1A or BWSCR1A), efflux transporter-like protein, imprinted multi-membrane-spanning polyspecific transporter-related protein 1 (IMPT1), organic cation transporter-like protein 2 (ORCTL2), or tumor-suppressing subchromosomal transferable fragment candidate gene 5 protein (TSSC5). It is localized at the apical membrane surface of renal proximal tubules and may act as an organic cation/proton antiporter. It functions as a tumor suppressor in several cancer types including glioblastoma and colorectal cancer. SLC22A18 belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance (TetA) -like (SLC46/TetA-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VLLIVHLNIVLYATCYWLQQPVLPYLTKKLGVDSVVFGYLQTTFSVLQLVGGPLFGRFGDLFGPRAALVL
SFLSSALSYLLLAFASSVPMLFLSRLPSVFMHAMQAAQMVVTDLTDPGERAAALGRLGLSYGIGMVVGSF
LGGLLTKKFGEQAAALVAAVGSLLSIVLVILLIPSNTKSKREKEAKESASPPSVFNLKEILRLLRLPGVA
FLLLVKLLSGLPIGMFQSMFSLVAMDFFGLTPEENGYLMSYAGVLGMVVQGLLVGPLTKRFGERSLLKLS
VALLAIGYLLLAFVTTVWQLLVLLLPLVIGGSVLYTVITSLLTKAVPPEDTGTALGLSHALFSLVRTVSP
TIGGALLQAYGFPSFGLLGAAINGLLTVYLLL
>gnl|CDD|340890 cd17332, MFS_MelB_like, Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major Facilitator Superfamily. This family is composed of Salmonella enterica Na+/melibiose symporter MelB, Major Facilitator Superfamily domain-containing proteins, MFSD2 and MFSD12, and other sugar transporters. MelB catalyzes the electrogenic symport of galactosides with Na+, Li+ or H+. The MFSD2 subfamily is composed of two vertebrate members, MFSD2A and MFSD2B. MFSD2A is more commonly called sodium-dependent lysophosphatidylcholine symporter 1 (NLS1). It is an LPC symporter that plays an essential role for blood-brain barrier formation and function. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. MFSD2B is a potential risk or protect factor in the prognosis of lung adenocarcinoma. MelB-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
KIGYGLGDFGNNLIFQIVSTYLLFFYTDVLGLSAAAAGTIFLVARIIDAINDPLMGYLIDRTRSRWGRFR
PWLLWGAIPLALLFVLLFTTPDGSGTGKLIYALITYILLDLLYTLVNIPYTALIPELTDDPEERTSLTSW
RMFFATIGGLLVTVLPPPLVAYFGGGNASRGYFLTALIIGIIGIILLLICFFGTRERVVPPEEEKSKLPL
LKSLKALLKNRPFLILLLAYLLYFLAFNIVNTVLVYYFKYVLGGRAELVLLLLLILSGALLALLPWPPLK
KRFGKKKAFFIGLLLAILGLLLLFFLPPGNLVLILVLAVLAGIGYGGANLLPWAMLADVIDYGELKTGKR
REGIFYSVMTFFRKLGLALAGALVGLILSLAGYVANAAAQSASALNGIRLLIAVLPAVLLLLALILMSFY
PLDK
>gnl|CDD|340891 cd17333, MFS_FucP_MFSD4_like, Bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4, and similar proteins. This family is composed of bacterial L-fucose permease (FucP), eukaryotic Major facilitator superfamily domain-containing protein 4 (MFSD4) proteins, and similar proteins. L-fucose permease facilitates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell; it can also transport L-galactose and D-arabinose. The MFSD4 subfamily consists of two vertebrate members: MFSD4A and MFSD4B. The function of MFSD4A is unknown. MFSD4B is more commonly know as Sodium-dependent glucose transporter 1 (NaGLT1), a primary fructose transporter in rat renal brush-border membranes that also facilitates sodium-independent urea uptake. The FucP/MFSD4 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LYISFFSNGLTDALLGILGPSLEEAFNLNVADVSVIFSSQNAGYLIGSLLAGFLMKRLGRRRTLILGLLL
ISLALALIFATPSIYLFVVLMFLAGLGAGILDTGANTFVGALFEESSATRLNVLHGFFGLGALIGPLIAT
SLLTSELSWSWAYLIIGLIYLLLAILILLTLFPELPSARNPQQSVGAFSASASRLLRNPSIILGALALFL
YVGAETAFSSWVPSYLVEKKHVSDGLAGYLLSGFWVGITIGRLLGGPISRRIKPHTLLVLSGSGALLGLL
ILLLAPTLVVGLVATALLGLFMAALFPTILSLGISNLPYAKGKGTSVLLAAGSIGGAIIPFIMGFIAEAV
GIQTAMLLITILYAIIFVLALL
>gnl|CDD|340892 cd17334, MFS_SLC49, Solute carrier 49 (SLC49) family of the Major Facilitator Superfamily of transporters. The Solute carrier 49 (SLC49) family is composed of four members: feline leukemia virus subgroup C receptor 1 (FLVCR1, SLC49A1); FLVCR2 (SLC49A2); major facilitator superfamily domain-containing protein 7 (MFSD7, SLC49A3); and disrupted in renal carcinoma protein 2 (DIRC2, SLC49A4). FLVCR1 and FLVCR2 are heme transporters. In addition, FLVCR2 also functions as a transporter for a calcium-chelator complex that is important for growth and calcium metabolism. The function of MFSD7 is unknown. DIRC2 is an electrogenic lysosomal metabolite transporter that is regulated by limited proteolytic processing by cathepsin L. The SLC49 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RRWVVLLLFSLLSFSNAMQWITFSPIADEARTFFDLSASQINWLSLVYPIVYVPGVFAFCWLLDKVGLRI
GVLIGAALNALGSVLKCIPLGQQPKFALLVLGQVLNALAQVLVLSLPPLIAAVWFPPKERTTATAIASLA
NFLGCAIGFLLPPVVVPPPKGTKKEFGAVFYGEFGFACLLLALVLALFPPKPKYPPSAASARQQNSEHVI
LELQKSISELLRNEPFVLLAVAFSIMMGVFAGFSSVLAQILLPFGVSQTSAGWLGFFGIVAGMVGGLLLG
LFVDRTRMFKLIGLIILALGTVVCTFFMLLVDRYGLPYVTLAFYLLCGLLGFFQNSMVPIMFELAVELTY
PVPESVSTGVLTALANLFSFLLMLVFSELLGPTPTESKYLLWFILCTVGSCLGALFF
>gnl|CDD|340893 cd17335, MFS_MFSD6, Major facilitator superfamily domain-containing protein 6. Human Major facilitator superfamily domain-containing protein 6 (MFSD6) is also called macrophage MHC class I receptor 2 homolog (MMR2). It has been postulated as a possible receptor for human leukocyte antigen (HLA)-B62. MFSD6 is conserved through evolution and appeared before bilateral animals. It belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RLKLFYFFFFAALGSLLPFLSVYLKQLGLSPTQIGILIGIRPFVRFLSAPLWGALADRFGKRKALLLLSL
LAAVLFFLSLFFVAQIFWLLLLLVILGAFFSAPVVPLVDSITLQYLGEERERYGKQRLWGSIGFGIAALL
VGILIDRSSTYKNYTIAFYVFAVLMLLALLLALKFPFRPKHPEPNENTGGLLALLRNPRVLAFLLVAFLM
GFGHGLIYSFLFWHLQDLGGSKTLIGLLWTVGVVSEIPFFFFSSRLIQRFGHVGLLYLGLLAYVVRWLLY
SFLENPWLVLPIELLHGLTFALVWAAAVSYASAAAPPGLRATAQGLLQGLYFGLGGGLGSLIGGYLYEAF
GARTTFRFFAIAALAGLLAFFLIQR
>gnl|CDD|340894 cd17336, MFS_SLCO_OATP, Solute carrier organic anion transporters of the Major Facilitator Superfamily of transporters. Solute carrier organic anion transporters (SLCOs) are also called organic anion transporting polypeptides (OATPs) or SLC21 (Solute carrier family 21) proteins. They are sodium-independent transporters that mediate the transport of a broad range of endo- as well as xenobiotics. Their substrates are mainly amphipathic organic anions with a molecular weight of more than 300Da, although there are a few known neutral or positively charged substrates. These include drugs including statins, angiotensin-converting enzyme inhibitors, angiotensin receptor blockers, antibiotics, antihistaminics, antihypertensives, and anticancer drugs. SLCOs/OATPs can be classified into 6 families (SLCO1-6 or OATP1-6) and each family may have subfamilies (e.g. OATP1A, OATP1B, OATP1C). Within the subfamilies, individual members are numbered according to the chronology of their identification and if there is already an ortholog known, they are given the same number. For example, the first SLCO identified, is rat OATP1A1 (encoded by the Slco1a1 gene). The second SLCO identified is the first human SLCO from the same subfamily and is called OATP1A2 (encoded by the SLCO1A2 gene). There are 11 human SLCOs/OATPs. SLCOs belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
PKVFVVLLCLLGLLQGAVVSYFVSTITTIEKRFGLSSSQSGLILSANDIGQLLAVLLVSYFGGRGHRPRW
IGIGSILMGLGCFLLALPHFLFVGQFLLGIGSSPLYTLGITYIDDNVSKKNSPLYIGILYAMRVLGPALG
FLLGSFLLRIYVDFSRVPLGITPDDPRWIGAWWLGFLILGILLLIVSIPLFFFPPIFILLLLAIVFESFA
ISGFSTFLPKYLETQFRLSASLASLLTGLILVPGAALGILLGGLIIKKFKLTARGLAKFVLILSLLSVIL
YISLFFLGCDNPPIAGVTTPYGSSSSPITSSCNSDCNCSDSSFSPVCGSDGITYFSPCHAGCTSSDAGNG
TKTYSNCSCINSGTATSSGCPPDCSVAPNCCSKLIPFLAVLFLSSFLLSLSIVPSTMITLR
>gnl|CDD|340895 cd17337, MFS_CsbX, CsbX family of the Major Facilitator Superfamily of transporters. The CsbX family is composed of Bacillus subtilis CsbX protein (also named alpha-ketoglutarate permease), Klebsiella pneumoniae D-arabinitol transporter (DalT), and similar proteins. The csbX gene is a sigmaB-controlled gene that is expressed during the stationary phase of cell growth. DalT is a pentose-specific ion symporter for D-arabinitol uptake. Most members of this family remain uncharacterized. The CsbX family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
WGYIGVLLFMIGDGVEQGFLSPYLVDLGFSEAQAALLFTVYGLTVAIASWLSGVLAELFGPRRVMLIGLI
IWLVFEVLFLAFGLPSHNYPLMLLTYGLRGFGYPLFAYSFLVWITYRTPAERLGSAVGWFWFAFTGGLPV
LGSYLASFTIPVIGEIGTLWLSLVFVALGGLIALFLVRDRTGEQPLANPSEEPLKELLSGITILFRNPKI
AIGGIVRIINTLSQFGFPVFMPLYFTDTGGFSTSQWLQIWGIIFLVNIFFNLIFGILGDKIGWRRTVRWF
GGVGCAISTLLFYYVPQLFGHNYWAALIAAILFGIGLAGFVPLSALMPSLAPEHKGAAMSILNLGAGLSN
FVGPAIVTLFLGSFGAGGVVWIFAGLYLLSAVLTLFLK
>gnl|CDD|340896 cd17338, MFS_unc93_like, Unc-93 family of the Major Facilitator Superfamily of transporters. The Unc-93 family is composed of Caenorhabditis elegans uncoordinated protein 93 (also called putative potassium channel regulatory protein unc-93) and similar proteins including three vertebrate members: protein unc-93 homolog A (UNC93A), protein unc-93 homolog B1 (UNC93B1), and UNC93-like protein MFSD11 (also called major facilitator superfamily domain-containing protein 11 or protein ET). Unc-93 acts as a regulatory subunit of a multi-subunit potassium channel complex that may function in coordinating muscle contraction in C. elegans. The human UNC93A gene is located in a region of the genome that is frequently associated with ovarian cancer, however, there is no evidence that UNC93A has a tumor suppressor function. UNC93B1 controls intracellular trafficking and transport of a subset of Toll-like receptors (TLRs), including TLR3, TLR7 and TLR9, from the endoplasmic reticulum to endolysosomes where they can engage pathogen nucleotides and activate signaling cascades. MFSD11 is ubiquitously expressed in the periphery and the central nervous system of mice, where it is expressed in excitatory and inhibitory mouse brain neurons. The unc93-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VIILSFGFLLIFLAYSALQNLQTSLHENGLGSISLGILYSSFAVSSFIAPLLVKLLGEKITLVLGGLGYA
IFIASNIFPIWGTLVPASIILGFAAAILWTAQGTYITRISDESNIGRNFGIFWSIFQLSQVFGNLISLAL
LNHSKGSSGTTILFIVFMAIMLVGIILLFFLRGPDNEVITEIESSSVGESMEKKNLFKLPFTLLKDKRFL
LLIPLLIYSGLEQTFFSGVFTLIIGTPTTGIARVGYVMAVYGFGDALGSLVAGLLSDWRFGRIVLAVIGA
FVHIASLILLFLSGNVTPYGLGGSWLAYVSAILWGLGDAIFNTQIYALLGSLYENDSESAFAVYKLWQSI
ATAIAYFLSPYLPLFVKLFVLLALLILLAIFFLFVELK
>gnl|CDD|340897 cd17339, MFS_NIMT_CynX_like, 2-nitroimidazole and cyanate transporters and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of Escherichia coli 2-nitroimidazole transporter (NIMT) and cyanate transport protein CynX, and similar proteins. NIMT, also called YeaN, confers resistance to 2-nitroimidazole, the antibacterial and antifungal antibiotic, by mediating the active efflux of this compound. CynX is part of an active transport system that transports exogenous cyanate into E. coli cells. The NIMT/CynX-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
ILGIVLIAFNLRPAITSVGPLLPEIRDDLGLSASQAGLLTTLPLLCFAVFSPLAPRLARRFGLERTLLLA
LLLLAAGILLRSLGGIALLFLGTALAGAGIAVGNVLLPSLIKRDFPRRVGLMTGLYTTSMNLGAALASGL
SVPLAQALGGGWRGALAIWALPALLALLIWLPQLRRRKRAAAAAAPLTKISVWRSPLAWQVTLFMGLQSL
LFYTLMAWLPTILIDAGLSAATAGWLLSLFQLVGIPASLLVPILATRLKNQRPIVVLLAVLFIIGVLGLL
FAPTALALLWAVLLGLGGGAAFSLALTLISLRSSDPAEAAALSGMAQSVGYLLAALGPLLFGVLHDLTGS
WTAPLVLLLALTVLQLVAGLGAGR
>gnl|CDD|340898 cd17340, MFS_MFSD1, Major facilitator superfamily domain-containing protein 1. Human major facilitator superfamily domain-containing protein 1 (MFSD1) is also called smooth muscle cell-associated protein 4 (SMAP-4). The function of MFSD1 is still unknown. Its expression is affected by altered nutrient intake. During starvation, expression of MFSD1 is downregulated in anterior brain sections in mice while it is upregulated in the brainstem. In mice raised on high-fat diet, MFSD1 is specifically downregulated in brainstem and hypothalamus. MFSD1 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LFLMCFLGFGSYFCYDNPAALQKQFIEDMDINTSQFMLLYSVYSWPNVVLCFFGGFLIDRVFGIRLGTII
FSLLVLIGQLIFALGALTNLFWLMLVGRFIFGIGGESLAVAQNTYAVSWFKGKELNLVFGLQLSFARIGS
TVNFNVMPPIYKRISDFYSGYKSLGVALWIGAITCLFSLICAIILGLLDKRAERILKKESNKTGEVIKLS
DVKDFPLSFWLICIICVFYYVAVFPFIGLGTVFFEEKYGFSPSEAAAVNSIVYIISAAASPVFGFLVDKV
GRNILWVLIALVITLLGHLLLAFTFVNPLIAMVIMGIGYSMLACALWPMVPLVVPEHQLGTAYGFMQSIQ
NLGLAVFPIIAGSILDKKGYLLLEVFFIACLCVSLIALIILYLV
>gnl|CDD|340899 cd17341, MFS_NRT2_like, Plant Nitrate transporter NRT2 family and Bacterial Nitrate/Nitrite transporters of the Major Facilitator Superfamily. This family is composed of plant NRT2 family high-affinity nitrate transporters as well as nitrate and nitrite transporters from bacteria including Bacillus subtilis nitrate transporter NasA and nitrite extrusion protein NarK, Staphylococcus aureus NarT, Synechococcus sp. nitrate permease NapA, Mycobacterium tuberculosis NarK2 and nitrite extrusion protein NarU. NRT2 family proteins are involved in the uptake of nitrate by plant roots from the soil through the high-affinity transport system (HATS). There are seven Arabidopsis thaliana NRT2 proteins, called AtNRT2:1 to AtNRT2:7. The NRT2-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LHLSWLSFFLGFMVWFLFAPLGPVIRDDLGLSTSQIGLLVAIPVLAGALLRLPYGFLCDRFGGRRVFIAS
LLLLLIPLLALALAVSSYWGLLVLGFLLGFAGANFASGQPWASFWFPKEKIGGAAGGIAGAGNMGVAVSQ
LLAPLIAGAIVFDGGFVGWRNAFFVPGILLAIAAVLVLLFGDDLPTGKASALEFLKVQLAVLKNYRTWIL
SLLYGVTFGSFVGFSNVLPTYFKTRFGLPLVTAGILAALFPLAGALARPAGGWLSDRFGGRRRLWWLFIV
MTIGAALLSLSLPTSGTNLVLFLALFVALGLGAGAGNGSVFRMVPFIFRRELGAVTGLVGAIGGLGGFFL
PLLFGSSALMTGSGVGAFSLFGVLAVACTLLVWL
>gnl|CDD|340900 cd17342, MFS_SLC37A3, Solute carrier family 37 member 3 of the Major Facilitator Superfamily of transporters. Solute carrier family 37 member 3 (SLC37A3) is also called sugar phosphate exchanger 3 (SPX3), and is one of four SLC37 family proteins in vertebrates. It's function and activity is unknown. The best characterized SLC37 family member is SLC37A4, also called the glucose-6-phosphate transporter (G6PT), a phosphate (Pi)-linked G6P antiporter. SLC37A3 is a member of the Organophosphate:Pi antiporter (OPA)/SLC37 family, whose members are integral membrane proteins responsible for the transport of specific organophosphates or sugar phosphates across biological membranes with the simultaneous translocation of inorganic phosphate into the opposite direction. The OPA/SLC37 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
HVVVFILTFFSYALLHATRKTFSNVKPSISAEWTPSNSNTSIELHEETWNANPLFPSQDDAALFLGVLDT
IFLFSYAIGLFISGWLGDRLNLRLVLAFGMCSSAITVFLFGVLTEWLHFYNKYLYCILWVLNGLLQSTGW
PCVVAIMGNWFGKSSRGFVLGLWSACASVGNIIGALLASSVLDYGYEYAFLVTSSLLFAGAIVVFFGLLS
SPPGVIPYSLAYACLKLVNYSFFFWLPFYLSNNFHWKESEADQLSIWYDVGGIIGGIVAGYISDRMGSRS
PVVVVMLLLAIPSLFVYSHSPSDKVLNAFVMTITGFFIGGPANLISSAISADLGRQPQLRGSSEALATVT
GIIDGTGSIGAAIGQVLVPLIQNRLGWMWVFYFFIIMTILTIVCILPLL
>gnl|CDD|340901 cd17343, MFS_SLC37A4, Solute carrier family 37 member 4 of the Major Facilitator Superfamily of transporters. Solute carrier family 37 member 4 (SLC37A4), one of four SLC37 family proteins in vertebrates, is better known as glucose-6-phosphate transporter (G6PT). It is also called sugar phosphate exchanger 4 (SPX4), G6P translocase, or transformation-related gene 19 protein (TRG-19). G6PT is a phosphate (Pi)-linked G6P antiporter, catalyzing G6P:Pi and Pi:Pi exchanges. Deficiencies in human G6PT lead to glycogen storage disease type Ib (GSD-Ib), which is a metabolic and immune disorder. G6PT is a member of the Organophosphate:Pi antiporter (OPA)/SLC37 family, whose members are integral membrane proteins responsible for the transport of specific organophosphates or sugar phosphates across biological membranes with the simultaneous translocation of inorganic phosphate into the opposite direction. The OPA/SLC37 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
QLTIFASMFVGYTLYYFNRKSFSFVLPSLMNELGLDKSDLGLITSSQSLAYAISKFIGGVLSDQISARWL
FSSGLVLSGLTTVAFSGSSSVWVFSILWFLNGLAQGLGWPPCAKILRKWFSPSQFGTWWSVLSTSMNLAG
SLGPILATLLALSYGWRSTLSISGTVAVVMSVVCLLFIKNEPSDVGLNNIEEEESKGKKKKSPRGESTLK
ELLLSPFLWLLSLGYLVVFGVKTAVTDWGQLFLIQDKGQSALTGSSFMSSLEVGGFVGSIAAGYLSDWAV
AKHGSSSRGNPRMPLALVFMAGLTVSLHLFRVHITSDSSELFILLLGFLIGFSLYGPIAIFGVIANESAP
SHLCGTSHAIVALAANVGGVLAGLPFSYIAKHYDWRTAFLLLEILCAITVVILFLLRNI
>gnl|CDD|340902 cd17344, MFS_SLC37A1_2, Solute carrier family 37 members 1 and 2 of the Major Facilitator Superfamily of transporters. Solute carrier family 37 members 1 (SLC37A1) and 2 (SLC37A2) are also called sugar phosphate exchangers 1 (SPX1) and 2 (SPX2). SLC37A1 and SLC37A2 are ER-associated, Pi-linked antiporters that can transport glucose-6-phosphate (G6P) but are insensitive to chlorogenic acid, a competitive inhibitor of physiological ER G6P transport, unlike SLC37A4, the best characterized SLC37 family member and is the physiological G6P transporter (G6PT). SLC37A1 and SLC37A2 belong to the Organophosphate:Pi antiporter (OPA)/SLC37 family, whose members are integral membrane proteins responsible for the transport of specific organophosphates or sugar phosphates across biological membranes with the simultaneous translocation of inorganic phosphate into the opposite direction. The OPA/SLC37 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RGFILVLTFLAYACYHLSRKPISIVKSVLHPNCSALIPPPNIVLNNTTWCGWAPFDGKNGTELLGALDSA
FLFAYAIGMFFSGHIGERLPLRYFLSFGMLLSGLFTALFGLGYYWNIHSLWYFVVVQILAGLFQSTGWPS
VVACVGNWFGKGKRGLIMGIWNSHTSVGNILGSLIAGIFVSSAWGLSFIVPGIIIAAMGVLVFLFLVEHP
PGVIEFSLCLFFAKLVSYTFLYWLPLYISNTAILSAKKAGDLSTLFDVGGIVGGILAGYISDYTGGRATT
CAAMLILAAPMLFIYNYFGQVSMTTNIVLLIVCGLLVNGPYALITTAVSADLGTHKSLKGNARALATVTA
IIDGTGSIGAALGPLLAGLISSRGWNNVFYMLIAADVCAGLLLTRLVYKE
>gnl|CDD|340903 cd17345, MFS_GlpT, Glycerol-3-Phosphate Transporter of the Major Facilitator Superfamily of transporters. Glycerol-3-Phosphate Transporter (also called GlpT or G-3-P permease) is responsible for glycerol-3-phosphate uptake. It is part of the Organophosphate:Pi antiporter (OPA) family of integral membrane proteins responsible for the transport of specific organophosphates or sugar phosphates across biological membranes with the simultaneous translocation of inorganic phosphate into the opposite direction. The GlpT group belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RWQVFLGIFIGYAGYYLVRNNFSLAQPYLIEQYGLSKTEIGLIGSALSIAYGLSKFVMGNLSDRSNPKRF
LAIGLILSAIINILIGFVPSATSSVGLMFILLFLNGWFQGMGWPPSGRTMVHWFSKKERGTWTSIWNISH
NVGGGLVGPLAGLGLAIFGDGWWRGAFIFPAIIAIIVAVIVLFLGKDTPESEGLPPIEEYKGDYPEEADG
EEEEQELSAWEIFVKYVLKNKLLWYIAIANVFVYLVRYGILDWAPTYLSEVKGFSKAQAMWAFSLFEWAA
IPGTLLAGWLSDKLFKGRRAPTGIIFMILVIVALIVYWLAPNVLVDLIALIALGFLIYGPVMLIGLQALE
LVPKKAAGTAAGLTGLFGYLGGSVLATALIGIIVDHFGWNGGFIVLLASCILAIIFLALVA
>gnl|CDD|340904 cd17346, MFS_DtpA_like, Dipeptide and tripeptide permease A (DtpA)-like subfamily of the Major Facilitator Superfamily of transporters. The DtpA-like subfamily includes four Escherichia coli proteins: dipeptide and tripeptide permeases A (DtpA, TppB or YdgR), B (DtpB or YhiP), C (DtpC or YjdL), and D (DtpD or YbgH). They are proton-dependent permeases that transport di- and tripeptides. DtpA and DtpB display a preference for di- and tripeptides composed of L-amino acids. DtpC shows higher specificity for dipeptides compared to tripeptides, and prefers dipeptides containing a C-terminal lysine residue. The DtpA-like subfamily belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
PKGLYTLFFTEMWERFSYYGMRAILILYLTAQLGDGFSEADAASIYGAYTALVYLTPIIGGWLADKVLGA
RRTVFIGGILMALGYLLLALSPFSVSMLYLGLALIIVGNGLFKPNISSLVGKLYDENDPRRDSGFSIFYM
GINLGAFLAPLLCGTLGDNYGYHYGFGLAAVGMLLGLLIFLLGRKKLLERKKMLAIIILFLFAVVFWAIY
EQAGTSLALFADENVDRLLGGFTIPPSWFQSLNPLFIILLAPILAALWTKLGKRGKDPSIPTKFALGLLL
LGLSFLLMVLAASFAGGSGKVSALWLVLSYFLQTLGELCLSPVGLSMITKLAPAKFAGFMMGLWFLASAL
GNILAGYLAGFYAQPKDPLASALVYTDYFGLIGVIALVAGIILLLLAKK
>gnl|CDD|340905 cd17347, MFS_SLC15A1_2_like, Solute carrier family 15 members 1 and 2, and similar Major Facilitator Superfamily transporters. Solute carrier family 15 member 1 (SLC15A1) and SLC15A2 are members of the proton-coupled oligopeptide transporter (POT) family of integral membrane proteins that mediate the cellular uptake of di/tripeptides and peptide-like drugs. They mediate the proton-coupled active transport of a broad range of dipeptides and tripeptides, including zwitterionic, anionic and cationic peptides, as well as a variety of peptide-like drugs such as cefadroxil, enalapril, and valacyclovir. SLC15A1, or peptide transporter 1 (PepT1), is primarily expressed in the brush border membranes of enterocytes of the small intestine and is also known as the intestinal isoform. SLC15A2, or peptide transporter 2 (PepT2), is abundantly expressed in the apical membrane of kidney proximal tubules and is also referred to as the renal isoform. Both proteins transport di/tripeptides, but not tetrapeptides or free amino acids, using the energy generated by an inwardly directed transmembrane proton gradient. The SLC15A1/SLC15A2-like group belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
PRAVPFIVGNEFCERFSYYGMRAILVLYLTDFLGFSEAEATAIYHSFVMLCYFFPLLGAIIADSYLGKYR
TILYLSLVYCLGHIVLAVTAIPPLGPPHVWGLLIGLLLIAIGTGGIKPCVSAFGGDQFGADQQHLLARFF
SWFYFAINAGSLLSTFLTPILRADVQFGGHDCYPLAFGVPGVLMAVATLVFWLGRKHYKDVKALLRVLVL
FIPLPVFWALFDQQGSRWTLQAEQMDGLVGGFTILPDQMQALNPILILILIPLFDYVIYPLLERCGIPLT
PLRKMGVGMILAALAFVIAGFLQLRIDGGLPGQPDPGEVTTFEDIEPNSVSILWQLPQYVVLTAGEVLFS
ITGLEFAYTQAPKSMKSVVQAAWLLTVALGNLIVVIVAELIQFSSQAAEYFFFAGLMLVVAVVFALLARF
YKYVTYE
>gnl|CDD|340906 cd17348, MFS_SLC15A3_4, Solute Carrier family 15 members 3 and 4 of the Major Facilitator Superfamily of transporters. Solute carrier family 15 members 3 (SLC15A3) and 4 (SLC15A4) are members of the proton-coupled oligopeptide transporter (POT) family of integral membrane proteins that mediate the cellular uptake of di/tripeptides and peptide-like drugs. They are peptide/histidine transporters (PHTs) that transport free histidine in addition to di/tripeptides. SLC15A4, also called peptide transporter 4 or peptide/histidine transporter 1 (PHT1), is expressed in the human brain, retina, placenta, and immune cells. It is required for Toll-like receptor 7 (TLR7)- and TLR9-mediated type I interferon production in plasmacytoid dendritic cells (pDCs) and is involved in the pathogenesis of lupus-like autoimmunity. SLC15A3, also called osteoclast transporter, peptide transporter 3, or peptide/histidine transporter 2 (PHT2), is expressed in immune tissues including the spleen and thymus. The SLC15A3/SLC15A4 group belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RAACAAVLLVELLERAAFYGITSNLVLFLNGSPFNWEGTQASQALLLFMGATYLLSPFGGWLADAYLGRF
WTILLSLLLYLLGMLLFPATAAPALYAGLLLVGLGVGSVKANITPFGADQVKDRGPEATRRFFNWFYWSI
NLGAILSLGGVAYIQQNVSFLIGYSIPAVCVGLAFLVFLCGQPVFIDVKALVKILPVFLALIPYWTVYFQ
MQTTYVLQSLHLKIPNIFISNIAGITNSSHTFPAAWLTMFDAVLILILIPLKDKLVDPFLKRRGLLPSSL
KRIAVGMFFVMCSAIAAGILESKRLEIVKHNTTIQQQIGNVTYYAADLPIWWQIPQYLLIGISEIFASIA
GLEFAYSAAPKSMQSAIMGLFFFFSGVGSFVGSGLLALVSIKEIGWMSSHKDFGNINGCRLNYYFFLLAG
IQGVTLLLFLIISVK
>gnl|CDD|340907 cd17349, MFS_SLC15A5, Solute Carrier family 15 member 5 of the Major Facilitator Superfamily of transporters. Solute carrier family 15 member 5 (SLC15A5) is a member of the proton-coupled oligopeptide transporter (POT) family of integral membrane proteins that mediate the cellular uptake of di/tripeptides and peptide-like drugs. The specific function of SLC15A5 is unknown. SLC15A5 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LQVVICLLLVELCERFTFFGIVCNMILFCTIKLGYRNHQAAIVNLCFVGTSTLTPVFVGWLAEECMGRNK
LVYICLFLHFLGTALLPVVAFPFEDFYIDTHHIIHTLAKREQTLLFYVALLTASLGTGGIRAIVCPLSAY
GLQDYGSRKLMSFFNWFYWLVNLNSAVVFVGISYIQQSVAKNLGFLIPFMSVLMALITLHMVRNDLINTK
NLVRLFPLFAFQILYRTCIMQIPSGYYLQTMNSNLNLGGFLLPIAAMNVISIIPLLILAPFLEYFSSCLF
SSKRYGPFLSACIIAGHLCAALSVMVAGFSEIHRKRFPLVEQTLSGKVLLVSSMPCFQLAPQYVLLGVAE
ALVTPACSLITFRLVPSSIRGISMHFLTLFNGAGCFMGALLIQLVYLISEGNWFPNTLNKGNLERFFFFL
ASLMLLNALGFWRISHR
>gnl|CDD|340908 cd17350, MFS_PTR2, Peptide transporter PTR2 of the Major Facilitator Superfamily of transporters. Fungal peptide transporter or permease PTR2 is a member of the proton-coupled oligopeptide transporter (POT) family of integral membrane proteins that mediate the cellular uptake of di/tripeptides and peptide-like drugs. It is a 12-transmembrane domain (TMD) integral membrane protein that translocates di-/tripeptides. As with other POT family proteins, it displays characteristic substrate multispecificity. PTR2 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
PWSAFLIAIVELCERFSYYGLTGPFQNYMQFGPDDSTPGALGLGEQGATGLSNFFTFWCYVTPVIGAYVA
DQFLGRYNTIVCGAVIYFVGILILTCTSIPSVIDAGAGLGGFVVAIIIIGLGTGGIKSNVSPLIADQLPK
IKPYVKTLKNGERVIVDPVVTLSRIYMIFYWAINVGSLSLLATTYLERTKGFWYAYLLPLCVFVIPLIIL
AFGKKFYKIRPDLFIDELKRALRACKVFLFYPIYWVCYGQMTSNFISQAGQMQLHGVPNDLFQAFDSIAL
IIFIPILENIIYPLLRKYNIPFKPITRITLGFMFASFSMIYAAVLQAKIYQAGPCYANPTGTCSPNDIHV
WIQIPAYVLIAFSEIFASITGLEYAYTKAPPSMKSFITALFLLTNAFGAALSIAISPAAVDPKLTWMFTG
IAVAAFIAGIMFWLCFHH
>gnl|CDD|340909 cd17351, MFS_NPF, Plant NRT1/PTR family (NPF) of the Major Facilitator Superfamily of transporters. The plant Nitrate transporter/Peptide transporter (NRT1/PTR) family (NPF) is related to the POT (proton-coupled oligopeptide transporter), Peptide transporter (PepT/PTR), or Solute Carrier 15 (SLC15) family in animals. In contrast to related animal and bacterial counterparts, the plant proteins transport a wide variety of substrates including nitrate, peptides, amino acids, dicarboxylates, glucosinolates, as well as the plant hormones indole-3-acetic acid (IAA) and abscisic acid (ABA). A recent study identified eight subfamilies within this family, named NPF1-NPF8. NPF belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
APFILGNEFAERLAFYGIAVNLVTYLTKVMHLSNAKAANTVTNFSGTSYLTPLLGAFLADAYLGRYWTIA
IFSVIYLVGLILLTLSASVPSLRPPPCNPDSPCEPASSTQLTVLYVGLYLIALGTGGIKPCVSAFGADQF
DETDPKEKKQKPSFFNWFYFSINLGSLLAVTLVVYIQDNVSWGWGFGIPAAAMALAVIVFVAGTPFYREV
KCLLRLLPIWATTILLSTVYAQMQTFFVQQGLTMDRRLGGSFEIPAASLSVFSTLFVLLFIPLYDRVFVP
FARRYTGNPRGITPLQRIGIGLVLSILAMAVAALVEVKRLRVARAHGLLDSPTGVVPMSVFWLLPQYFLL
GLAEVFTYIGQLEFFYDEAPDGMRSLGTALFLLTIALGNFLSSALVTIVNKITGKGGGPGWLPNNLNKGR
LDYFYWLLAVLSAVNFLVFLVCAKW
>gnl|CDD|340910 cd17352, MFS_MCT_SLC16, Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily of transporters. The animal Monocarboxylate transporter (MCT) family is also called Solute carrier family 16 (SLC16 or SLC16A). It is composed of 14 members, MCT1-14. MCTs play an integral role in cellular metabolism via lactate transport and have been implicated in metabolic synergy in tumors. MCT1-4 are proton-coupled transporters that facilitate the transport across the plasma membrane of monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and ketone bodies such as acetoacetate, beta-hydroxybutyrate and acetate. MCT8 and MCT10 are transporters which stimulate the cellular uptake of thyroid hormones such as thyroxine (T4), triiodothyronine (T3), reverse triiodothyronine (rT3) and diidothyronine (T2). MCT10 also functions as a sodium-independent transporter that mediates the uptake or efflux of aromatic acids. Many members are orphan transporters whose substrates are yet to be determined. The MCT family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWVVVFASFLVNFFTDGILNSFGVLFVELLEEFGESTSDIAWIGSLLLGVSLFSGPLSSALVNRFGCRPV
AIAGGLLAALGLLLSSFATSLWQLYLTYGVLGGLGLGLIYSPAIVIVGQYFEKKRGLATGIAVAGSGVGT
FVFPPLLRYLLDNYGWRGALLILGGLCLNLCVCGLLLRLLKDPTFVLLALGVSFAMLGFFVPFVYLPSYA
KSLGIDESDAAFLLSIIGISDIVGRILLGLLADKPRIGRLYLYIFTLLILGLSLLAFPLATTYVGLIVFS
VLFGFCSGSYSSLTPVILADLVGLEKLSNAYGLVLLFQGLAALVGPPIAGLLRDYTGDYDAAFYFCGACL
LLSGVLLFLLP
>gnl|CDD|340911 cd17353, MFS_OFA_like, Oxalate:formate antiporter (OFA) and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of Oxalobacter formigenes oxalate:formate antiporter (OFA or OxlT) and similar proteins. O. formigenes, a commensal found in the gut of animals and humans, plays an important role in clearing dietary oxalate from the intestinal tract, which is carried out by OFA/OxlT, an anion transporter that facilitates the exchange of divalent oxalate with monovalent formate, the product of oxalate decarboxylation. This exchange generates an electrochemical proton gradient and is the source of energy for ATP synthesis in this cell. The OFA-like subfamily belongs to the Monocarboxylate transporter -like (MCT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RRWLVLLGAVLMHLILGYQYAWSVFNPPLSSALGWSLASVALAFTLTIVFLAISAPFAGRLVDRGGPRKA
ILIGGILFGLGFILSAFAISLPLLFLGYGVLGGIGAGIGYITPVSTAVKWFPDKRGLATGIVIAGFGLGS
LIFSPLIAYLINTVGVPTTFLILGIIFLIIIVIGAFLIRDPPKGWVPPGVDPLANNAENSPRDYTPREML
RTPTFWLLWLMFFLNATAGLMLIGQAKPIGQEFAGLDAGIAALAVSILSIFNGGGRPFWGWLSDKIGRKN
TLSIAFLIQGVAMFLLPFIGSVAVLFVLGVALIGFCYGGGFALFPALTADFFGTKNAGTNYGLLYTAKGV
GGLIGPIIAAYVLYTGGYNAAFIIAAALSLVALALALLL
>gnl|CDD|340912 cd17354, MFS_Mch1p_like, Monocarboxylate transporter-homologous (Mch) 1 protein and similar transporters of the Major Facilitator Superfamily of transporters. Yeast monocarboxylate transporter-homologous (Mch) proteins are putative transporters that do not transport monocarboxylic acids across the plasma membrane, and may play roles distinct from their mammalian counterparts. Their function has not been determined. The Mch1p-like group belongs to the Monocarboxylate transporter -like (MCT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LRWLSFVAALWSQLSAGSIYLFSLYSPPLKSTLGYSQQQNNLLSVAKDLGYLVGPLLGLLSDRLGPWLLL
LIGAILFFPGYGVLWLVVTGLISDLSFWLMCLCFFLIGNSTSSLYTAALVTCAKNFPESRGLAIGIPKGC
YGLSGAIGSQLYKALFFHDSARVFLFLAVLPAVVGLLAWFSVRIVSIEEGEFLKDIDFWLLFISLFLGVG
PGEMFINNLGQIGQSLTGPSNTSTLVSLFSIFSFLGRLLSGLLSDLFVRKFRLPRPSRMVLLLLILSLGH
LLQAFGLPSGALYVASALIGFGYGGLFSIAPTIVSELFGLKNFGTNYGFLMLAPAIGSLIFSVIYAGVYY
DNGGEGAGSDDLSCIGPHCFSLTFLIMAAVCLLAV
>gnl|CDD|340913 cd17355, MFS_YcxA_like, MFS-type transporter YcxA and similar proteins of the Major Facilitator Superfamily of transporters. This group is composed of uncharacterized bacterial MFS-type transporters including Bacillus subtilis YcxA and YbfB. YcxA has been shown to facilitate the export of surfactin in B. subtilis. The YcxA-like group belongs to the Monocarboxylate transporter -like (MCT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWVVLAVTFLILILSWGIRYYFGVFIIPIIAEFGWSRAVISLAFTVGLLAFGLAQPFVGRLLDRFGPRRV
MLLGLLLLAAGLVLLALATSLWQLYLLWGLLGGGGAGTLAAVAFATVAAWWFERRRGLALGILTAGGGLG
SLVFLPLGAALIEAFGWRTALLVLALLALLVLVPVLLLLRRRPADLALRAYDDASPASPGSTLKEALRSA
SFWLLALAFFLCGFAVVGLIVHLVPYLADRGISPAAAAVALALIGLFNIVGRLLSGWLGDRYSPRRLLAA
SYALRALGLALLLLLPFPPLALLLFAALFGLGWGATVPLTAALAARYFGARSYGTLFGLVFAPHQLGSAL
GPWLGGLLYDRTGSYTAAWALAVALGLIAALLVLPI
>gnl|CDD|340914 cd17356, MFS_HXT, Fungal Hexose transporter subfamily of the Major Facilitator Superfamily of transporters and similar proteins. The fungal hexose transporter (HXT) subfamily is comprised of functionally redundant proteins that function mainly in the transport of glucose, as well as other sugars such as galactose and fructose. Saccharomyces cerevisiae has 20 genes that encode proteins in this family (HXT1 to HXT17, GAL2, SNF3, and RGT2). Seven of these (HXT1-7) encode functional glucose transporters. Gal2p is a galactose transporter, while Rgt2p and Snf3p act as cell surface glucose receptors that initiate signal transduction in response to glucose, functioning in an induction pathway responsible for glucose uptake. Rgt2p is activated by high levels of glucose and stimulates expression of low affinity glucose transporters such as Hxt1p and Hxt3p, while Snf3p generates a glucose signal in response to low levels of glucose, stimulating the expression of high affinity glucose transporters such as Hxt2p and Hxt4p. Schizosaccharomyces pombe contains eight GHT genes (GHT1-8) belonging to this family. Ght1, Ght2, and Ght5 are high-affinity glucose transporters; Ght3 is a high-affinity gluconate transporter; and Ght6 high-affinity fructose transporter. The substrate specificities for Ght4, Ght7, and Ght8 remain undetermined. The HXT subfamily belongs to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLCAFVSLGGFLFGYDTGSISGILNMKSFQKYFADNTGTYYPSSSRQGLIVSIVNLGSFFGALISSFLSD
RIGRKKSIQIGCVIYIIGAIIQVAAIGKWYQLIVGRIIAGLGVGFASVLVPVYQSEVAPKHIRGTLVSLY
QLAITIGILVAYCINYGTHKLDGSAQWRIPLGLQIVWGLLLLIGMFFLPESPRWLYRTILGIMLQLFQQL
TGINYFFYYGTTIFQSTGLTGSSPLLTSIILYIVNFVSTIPGLFFVDKFGRRTCLLIGAAGMSICLFIYA
AVGVRYLIPNPQSGTSNKSAGNGMIVFICLFIFSFATTWGPIAWVYVAEVFPLRVRSKGMALATAFNWLW
NFLISFFTPFIIGSIGFKYYYIFAGCNLLAFIVVFFFVPETKGLTLEEIDELF
>gnl|CDD|340915 cd17357, MFS_GLUT_Class1_2_like, Class 1 and Class 2 Glucose transporters (GLUTs) of the Major Facilitator Superfamily. This subfamily includes Class 1 and Class 2 glucose transporters (GLUTs) including Solute carrier family 2, facilitated glucose transporter member 1 (SLC2A1, also called glucose transporter type 1 or GLUT1), SLC2A2-5 (GLUT2-5), SLC2A7 (GLUT7), SLC2A9 (GLUT9), SLC2A11 (GLUT11), SLC2A14 (GLUT14), and similar proteins. GLUTs are a family of proteins that facilitate the transport of hexoses such as glucose and fructose. There are fourteen GLUTs found in humans; they display different substrate specificities and tissue expression. They have been categorized into three classes based on sequence similarity: Class 1 (GLUTs 1-4, 14); Class 2 (GLUTs 5, 7, 9, and 11); and Class 3 (GLUTs 6, 8, 10, 12, and HMIT). GLUTs 1-5 are the most thoroughly studied and are well-established as glucose and/or fructose transporters in various tissues and cell types. GLUT proteins are comprised of about 500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 transmembrane segments. They belong to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
AVIVAFGGSFQFGYNIGVVNAPQEVFKEFINDTLVDRYGLNLSDSELDLLWSLIVSIFFIGGAIGSFISA
FLANRFGRKNGLLISNALLVVSSLLMFLSKSAKSPELLIFGRFLVGIACGLSTGFVPMYLQEISPSELRG
ALGSLTQIGVTLGILLGQVFGLPSVLGTETLWPYLLFFPGIPALLQLAALPFFPESPKFLLISKGDEEEA
EKSLKFLRGIEDDVDQELEEIKKESEQMGDQKQVSLMQLLRDPSLRLPLLLVLVVSASQQFSGINAIFFY
STFIFENAGFSPQLAEWANLGIGIVNVLSTIVGPFLIEKVGRRPLLLISLSVCAVALLLMSVFLFLSEQN
SWMSYGCIVAIFLFIFFFAIGLGPIPWFIGAELFPQAPRSAAQSLGSSVNWTSNFIVGMAFPPLQSIGGG
FVFIIFAIPCALFLLYLYRYLPETKGR
>gnl|CDD|340916 cd17358, MFS_GLUT6_8_Class3_like, Glucose transporter (GLUT) types 6 and 8, Class 3 GLUTs, and similar transporters of the Major Facilitator Superfamily. This subfamily is composed of glucose transporter type 6 (GLUT6), GLUT8, plant early dehydration-induced gene ERD6-like proteins, and similar insect proteins including facilitated trehalose transporter Tret1-1. GLUTs, also called Solute carrier family 2, facilitated glucose transporters (SLC2A), are a family of proteins that facilitate the transport of hexoses such as glucose and fructose. There are fourteen GLUTs found in humans; they display different substrate specificities and tissue expression. They have been categorized into three classes based on sequence similarity: Class 1 (GLUTs 1-4, 14); Class 2 (GLUTs 5, 7, 9, and 11); and Class 3 (GLUTs 6, 8, 10, 12, and HMIT). Insect Tret1-1 is a low-capacity facilitative transporter for trehalose that mediates the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source. GLUT proteins are comprised of about 500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 transmembrane segments. They belong to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLATFVANLGSFSFGIAVGWSSPALPSLMSDNSLSLPLTVAQFSWFGSLLTLGALIGALLSGKLADRIGR
KRTLLISAIPCILGWLLIAFAKDVWMLYLGRFLAGFGGGAASVVVPVYIAEIAPKNVRGALGSLNQLLVN
IGILLGYVLGSFLPWRTLALIGAIPPVVFLILLFFIPESPRWLAKKGREEEAEKSLQFLRGKDADISKEA
AEIQEELAELEKEAKESSFSDLFQRKYLKPLVIGLGLMLFQQLSGINAVIFYASSIFDEAGSGLDPNTAT
IIIGVVQVVGTLVATLLVDRLGRRPLLLVSAIGMGIGLLALGLYFYLQEHGALLSSVSWLPLVGLVIYII
SFSIGLGPLPWVIMSEIFPAKIKGLAGSLVTLVNWLFAFIVTKTFPFLTLAWGASGTFWIFAGICGLALV
FVLLFVPETKGKSLEE
>gnl|CDD|340917 cd17359, MFS_XylE_like, D-xylose-proton symporter and similar transporters of the Major Facilitator Superfamily. This subfamily includes bacterial transporters such as D-xylose-proton symporter (XylE or XylT), arabinose-proton symporter (AraE), galactose-proton symporter (GalP), major myo-inositol transporter IolT, glucose transport protein, putative metabolite transport proteins YfiG, YncC, and YwtG, and similar proteins. The symporters XylE, AraE, and GalP facilitate the uptake of D-xylose, arabinose, and galactose, respectively, across the boundary membrane with the concomitant transport of protons into the cell. IolT is involved in polyol metabolism and myo-inositol degradation into acetyl-CoA. The XylE-like subfamily belongs to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LISLVAALGGLLFGYDTGVINGALPFLQTDFNLTPFLEGLVVSSALLGAAIGALFAGRLADRFGRRKTLL
ISAVLFFISALGSAFSPNFTIFIIARIIGGLAVGGASALVPMYIAEVAPAEIRGRLVSLNQLMIVFGQLL
AYIVNYLIANAGGADWLGAEGWRWMLGLEAIPAILFLLGMLFIPESPRWLVSKGKPILIIGIGLAIFQQF
VGINVIFYYGPEIFQNAGFSENAALLQTIGIGVVNVIFTIIAILLVDKVGRKPLLLIGSIGMAISLLLIG
TAFYFAPGSQASGIVALVLILLFVAFFAMSWGPVTWVLLSEIFPNRIRGLAMGIAVFFLWIANFLVSLTF
PILLAAFGLAFTFLIFAVICVLAFLFVWKFVPE
>gnl|CDD|340918 cd17360, MFS_HMIT_like, H(+)-myo-inositol cotransporter and similar transporters of the Major Facilitator Superfamily. This subfamily is composed of myo-inositol/inositol transporters and similar transporters from vertebrates, plant, and fungi. The human protein is called H(+)-myo-inositol cotransporter/Proton myo-inositol cotransporter (HMIT), or H(+)-myo-inositol symporter, or Solute carrier family 2 member 13 (SLC2A13). HMIT is classified as a Class 3 GLUT (glucose transporter) based on sequence similarity with GLUTs, but it does not transport glucose. It specifically transports myo-inositol and is expressed predominantly in the brain, with high expression in the hippocampus, hypothalamus, cerebellum and brainstem. HMIT may be involved in regulating processes that require high levels of myo-inositol or its phosphorylated derivatives, such as membrane recycling, growth cone dynamics, and synaptic vesicle exocytosis. Arabidopsis Inositol transporter 4 (AtINT4) mediates high-affinity H+ symport of myo-inositol across the plasma membrane. The HMIT-like subfamily belongs to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
FAGIGGFLFGYDTGVISGALLYIKDDLGEVVLSTGWQELIVSSTVAGAAVGAAIGGWLNDRFGRRPCILL
ADALFTIGAIVMAAAPNKEVLIVGRVLVGLGVGIASMTVPLYIAEAAPPRIRGRLVTINVLFITGGQFVA
YVINGAFSYLPGGWRWMLGLAAVPAVLQFIGLLFLPESPRWPSTRRALIVGCGLQAFQQFSGINTVMYYS
ATILQMAGFKDNQNAIWLSLIVAGTNFIFTIVGMYLIDKFGRRKLLLISLFGVIVALVVLAVWLALVGLI
LYLAFFAPGMGPVPWTVNSEIYPLWARGTGGGCAAAVNWVFNLLVSQTFLTLTQAIGPYGTFLLFAGLAV
LGLIFIYFCVPE
>gnl|CDD|340919 cd17361, MFS_STP, Plant Sugar transport protein subfamily of the Major Facilitator Superfamily of transporters. The plant Sugar transport protein (STP) subfamily includes STP1-STP14; they are also called hexose transporters. They mediate the active uptake of hexoses such as glucose, 3-O-methylglucose, fructose, xylose, mannose, galactose, fucose, 2-deoxyglucose and arabinose, by sugar/hydrogen symport. Several STP family transporters are expressed in a tissue-specific manner, or at specific developmental stages. STP1 is the member with the highest expression level of all members and high expression is detected in photosynthetic tissues, such as leaves and stems, while roots, siliques, and flowers show lower expression levels. It plays a major role in the uptake and response of Arabidopsis seeds and seedlings to sugars. The STP subfamily belongs to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VAALGGLIFGYDIGISGGVTSMDPFLEKFFPSVYEKKKGASENNYCKYDDQLLQLFTSSLYLAGLVASLL
ASYVTRKWGRKPSMLIGGVLFLVGAALNAAAQNIAMLIVGRILLGFGVGFGNQAVPLYLSEMAPAKLRGA
LNIGFQLAITIGILIANLINYGTSKIKPNGWRLSLGLAAVPALILLLGSLFLPETPNSPQLVIAILIPFF
QQLTGINVIMFYAPVLFQTLGFGSDASLISAVITGAVNVVSTLVSIYLVDRFGRRFLLLEGGVQMLASQV
AIGILLAVKFGDGGELPKAYAIAVVVLICLYVAAFAWSWGPLGWLVPSEIFPLETRSAGQSLTVAVNFLF
TFVIAQAFLSMLCAMKFGIFLFFAGWVVVMSLFVYFLLPE
>gnl|CDD|340920 cd17362, MFS_GLUT10_12_Class3_like, Glucose transporter (GLUT) types 10 and 12, Class 3 GLUTs, and similar transporters of the Major Facilitator Superfamily. This subfamily is composed of glucose transporter type 10, GLUT12, plant polyol transporters (PLTs), and similar proteins. GLUTs, also called Solute carrier family 2, facilitated glucose transporters (SLC2A), are a family of proteins that facilitate the transport of hexoses such as glucose and fructose. There are fourteen GLUTs found in humans; they display different substrate specificities and tissue expression. They have been categorized into three classes based on sequence similarity: Class 1 (GLUTs 1-4, 14); Class 2 (GLUTs 5, 7, 9, and 11); and Class 3 (GLUTs 6, 8, 10, 12, and HMIT). GLUT proteins are comprised of about 500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 transmembrane segments. They belong to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
FPALGGLLFGYDIGATSGALLSITSPALSGTDWYNLSSLQSGLVVSGSLLGALLGSLVAGALIDRLGRRK
ELILAALLYLVGSLVTGLAPSYPVLLVGRLIYGVGIGLAMHAAPVYIAETSPSHIRGLLVSLKELFIVLG
ILLGYVSGYAFADVVGGWRYMYGLAAPPALLLGIGMWFLPPSPRWQGNYRKPLIIGLGLVLFQQITGQPS
VLYYAATIFKSAGFSAASDATLVSVGLGVFKLLMTIVAVLLVDKLGRRPLLLGGVSGMVVSLFLLAAYNL
FVQMGPAGLAWLSLVALLLYVGAYQISFGPISWLMVSEIFPLRVRGRAIALAVLVNFGSNALVSLAFLPL
QELIGLPGTFLGFGVIGVLALLFIYFTVPETKGLSLEEI
>gnl|CDD|340921 cd17363, MFS_SV2, Synaptic vesicle glycoprotein 2 of the Major Facilitator Superfamily of transporters. Synaptic vesicle glycoprotein 2 (SV2) is a transporter-like integral membrane glycoprotein, with 12 transmembrane regions, expressed in vertebrates and is localized to synaptic and endocrine secretory vesicles. Three isoforms have been identified, SV2A, SV2B, and SV2C. SV2A and SV2B are widely expressed in the brain, while SV2C is more restricted to evolutionarily older brain. SV2 isoforms have been shown to be critical for the proper function of the central nervous system. SV2 serves as the receptor for botulinum neurotoxin A (BoNT/A), one of seven neurotoxins produced by the bacterium Clostridium botulinum. BoNT/A blocks neurotransmitter release by cleaving synaptosome-associated protein of 25 kD (SNAP-25) within presynaptic nerve terminals. The SV2 family belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
FFVLGLALMADGVEVFVVGFVLPSAEKDMCLSNSNKGMLGLIVYLGMMVGAFVWGGLADKLGRKQCLLIA
LSVNGVFAFLSSFVQGYGFFLFCRLLSGIGIGGSIPIVFSYFAEFLAREKRGEHLSWLCMFWMIGGLYAS
AMAWAIIPHYGWGFSMGTAYQFHSWRVFVIVCALPSVASVVALTFMPESPRFLLEVGKHDEAWMILKQVH
DTNMRAKGHPERVFTVSHIKRMNTLFLAIVWFTMSFSYYGLTVWFPDMIKYLQFEDSLFEECYFEDVTST
NTFFENCTFINTVFYNTDLFEYKFIDSRFLNSTFFLKEKCGCHLNDDEENAYLIYLVSFLGSLSVLPGNI
VSALLMDKIGRLKMIGGSMLLSAVCCFFLFFGNSESAMIGLQCLFCGVSIAAWNALDVVTVELYPTDKRA
TAFGFLNGLCKLAAILGNSIFGSFVGITKVIPILLASAALVCGGLLALKLPETR
>gnl|CDD|340922 cd17364, MFS_PhT, Inorganic Phosphate Transporter of the Major Facilitator Superfamily of transporters. This subfamily is composed of predominantly fungal and plant high-affinity inorganic phosphate transporters (PhT or PiPT), which are involved in the uptake, translocation, and internal transport of inorganic phosphate. They also function in sensing external phosphate levels as transceptors. Phosphate is crucial for structural and metabolic needs, including nucleotide and lipid synthesis, signalling and chemical energy storage. The Pht subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
IIIAGMGFFTDAYDLFSISLVTKILGRLYYGGKGSLPSGVSGLVNAAALVGTIIGQLFFGFLGDRFGRKR
VYGVELIIMIIGTILSALSPGSTPLGVMGWLIFFRFLLGIGIGGDYPLSATIMSEYANKKRRGALIAAVF
AMQGFGILAGAIVTLILSAIFEHPLPAGTYHHADLVWRIVLGLGAIPALSVLYFRKHLLGTAGTWFLLDI
AFYGQNLFQSTIISAIGFSKTMNAYQELFNIAVGQLIIALAGTVPGYWFTVFLIDRIGRKKIQMMGFFGM
TIFLLILAGPYDHWKISTIGFFVLYGLTFFFSNFGPNTTTFIVPAEVFPARVRSTCHGISAASGKIGAIV
GSFLFLSLTQNIGVRNVLIILAGVALLGIILTLLFPEEK
>gnl|CDD|340923 cd17365, MFS_PcaK_like, 4-hydroxybenzoate transporter PcaK and similar transporters of the Major Facilitator Superfamily. This aromatic acid:H(+) symporter subfamily includes Acinetobacter sp. 4-hydroxybenzoate transporter PcaK, Pseudomonas putida gallate transporter (GalT), Corynebacterium glutamicum gentisate transporter (GenK), Nocardioides sp. 1-hydroxy-2-naphthoate transporter (PhdT), Escherichia coli 3-(3-hydroxy-phenyl)propionate (3HPP) transporter (MhpT), and similar proteins. These transporters are involved in the uptake across the cytoplasmic membrane of specific aromatic compounds such as 4-hydroxybenzoate, gallate, gentisate (2,5-dihydroxybenzoate), 1-hydroxy-2-naphthoate, and 3HPP, respectively. The PcaK-like aromatic acid:H(+) symporter subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LALCFLIIVLDGFDLAVMGFVAPALAQDWGLSPAQLGPVGSAALFGMAIGALLAGPLADRFGRKRVLLVS
VALFGLFTLLTAFAQSVLQLALLRFLTGLGLGAAMPNAITLVSEYAPARRRSLAVTLMFCGYPLGAALGG
FLAAALIPAFGWRSVFLLGGVPPLILLPLLRGTLLLWVTFFMGLLLVYLLNSWLPKLMVEAGYSLSQALT
ITLLLNIGGVIGSLLLGWLADRFGPKRVLALFFALGAVSLALLGVSPASLVLLYVLVFLAGACVNGAQVG
LYALAARFYPTEVRATGVGWALGVGRLGAILGPLLGGLLLAAGLGPESVFLALAIPAALGALAVLLLRLR
R
>gnl|CDD|340924 cd17366, MFS_ProP, Proline/betaine transporter of the Major Facilitator Superfamily of transporters. This subfamily is composed of Escherichia coli proline/betaine transporter, also called proline porter II (PPII), and similar proteins. ProP is a proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response. The ProP subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VKAAALGNAMEWFDFGVYGYLAVTIGKVFFPGGDPTAQLLATFATFAVAFLVRPLGGLVFGPLGDKYGRQ
KVLAITIILMAASTFCIGLLPTYATIGVWAPILLLLARMVQGFSTGGEYGGAATFVAEYAPDRKRGFLGS
WLEFGTLAGFILGAGLVTLLTLLLTEAQMLDWGWRIPFLIAAPLGLVGLYLRRPLLICIGLVLVFNVTNY
MLLSYMPSYLEETLGYSETHGLLVIIIIMVTMLVLQPFLGRLSDRVGRKPVYAAGLAGLLVLAVPAFLLM
NSGSIAAIFIGLLVLGLLLSCYTATMASTLPALFPTHVRYSALAIAFNISVSLFGGTTPLVASWLVSATG
NPLMPAYYLMVAAVVGLVAVLFLTETA
>gnl|CDD|340925 cd17367, MFS_KgtP, Alpha-ketoglutarate permease of the Major Facilitator Superfamily of transporters. This subfamily includes Escherichia coli alpha-ketoglutarate permease (KgtP) and similar proteins. KgtP is a constitutively expressed proton symporter that functions in the uptake of alpha-ketoglutarate across the boundary membrane. Also included is a putative transporter from Pseudomonas aeruginosa named dicarboxylic acid transporter PcaT. The KgtP subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
ILGGSVGNLVEWYDWYVYAAFALYFAPQFFPSGDPTVALLSTAAVFAVGFLMRPIGGWLFGRLADRIGRR
AALTLSVSLMAAGSLVIAVTPTYATIGIWAPIILLLARLLQGLSVGGEYGTSATYLSEVAPPGRRGFYSS
FQYVTLIGGQLLALGVLLVLQHTLGEDQMAAWGWRIPFLLGGVLAVVVLWLRRGLEETESFEAIAESNEA
SAGTLRELRRHPRELLLVVGLTAGGTLAFYTWTTYLQKFLVNTAGFSKGDATWITTAALLVFMLLQPLGG
RLSDRIGRRPLLLFFGIGGTLATVPLLSALDHTDSPYTAFALVLVGLVFLSGYTSINAVVKAELFPTHVR
ALGVGLPYALAVAIFGGTAPYVALWLKSIGHEWVFFWYVAGLIAISLVVYLRMPETR
>gnl|CDD|340926 cd17368, MFS_CitA, Citrate-proton symporter of the Major Facilitator Superfamily of transporters. Citrate-proton symporter, also called citrate carrier protein or citrate transporter or citrate utilization protein A (CitA), is a proton symporter that functions in the uptake of citrate across the boundary membrane. It allows the utilization of citrate as a sole source of carbon and energy. In Klebsiella pneumoniae, the gene encoding this protein is called citH, instead of citA, which is the case for Escherichia coli and other organisms. CitA belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
ILAATSGNALEFFDFGVYGFFAVYIGRLFFPSGSEFASLLLTFATFGVGFFMRPIGAIVLGAYADRIGRK
PAMTLTLAIMALGTLLIALAPTYATIGIAAPLLVLLARLLQGFAAGGEVGGVTAYLVEAAPPGRRGFYTS
WQSASQQVAIVAGALVGYLLSLTLTAEALAEWGWRIPFFIGLLIIPLGLWLRRSLEETEAFLERKARPTR
RELFALLANNRRIILLGMLLVAGSTVTFYFTTVYTPTYAKTVLGLSARDSFLVTLLAGVANFIWAPLGGA
LSDRIGRRPVLLVITLAALVTLYPVFAWLTAAPSFGRLLLVLLVLSFFFGMYGGAMVVALVELFPVRVRS
TGFSLVYALAVAIFGGFAQFIVTWLIELTGSPLAPAWYLMGAALLGLLATLMLRETA
>gnl|CDD|340927 cd17369, MFS_ShiA_like, Shikimate transporter and similar proteins of the Major Facilitator Superfamily. This subfamily is composed of Escherichia coli shikimate transporter (ShiA), inner membrane metabolite transport protein YhjE, and other putative metabolite transporters. ShiA is involved in the uptake of shikimate, an aromatic compound involved in siderophore biosynthesis. It has been suggested that YhjE may mediate the uptake of osmoprotectants. The ShiA-like subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RRVALASLVGTAIEWYDFFIYGTAAALVFNKLFFPAVDPAAGTLAAFATFGVGFLARPLGGVVFGHFGDR
IGRKKTLVLTLLLMGIATFLIGLLPTYAQIGILAPILLVLLRLLQGLALGGEWGGAVLMAVEHAPPKRRG
FYGSFPQLGAPVGLLLATGVFLLLSALLSDEAFLSWGWRIPFLLSAVLVAVGLYIRLRLEETPVFRRAKE
AGQVVRAPLVEVLRRHWRALLLAIGLRLAENVLFYLFTTFALSYATQTLGVDRSTVLLAVLIASVVAAIT
IPLFGWLSDRVGRRPVYLAGALLAALFAFPFFWLLDTGSTWLIVLAAVVVLGVLHGMMYGPQAAFLAELF
PTRVRYTGASLGYQLGAILGGGFAPLIATALVAATGSWWPVALYLAALAVISLVAALF
>gnl|CDD|340928 cd17370, MFS_MJ1317_like, MJ1317 and similar transporters of the Major Facilitator Superfamily. This family is composed of Methanocaldococcus jannaschii MFS-type transporter MJ1317, Mycobacterium bovis protein Mb2288, and similar proteins. They are uncharacterized transporters belonging to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VWLLGLVSLFADISYEMARSILPLFLVVLGASAAAVGLIEGLAEALGSLLRLFSGYLSDRTGKRKPLVIL
GYGLSALAKPLLALAGSWQLVLLLRILERLGKGIRTPPRDALLADATPPSGRGKAFGLHRALDTLGAVLG
PLLAALLLYLLGGNYRTIFLLAAIPALLALLILLFVVKEYPRPPKLRKKSKKTSLKKLPKAFWLYLLAVA
LFALGNFSFAFLILRAQELGLSAALIPLLYALFNLVYALAAYPAGRLSDRIGRKKLLILGYLSLALAYLG
FALGSSLWLLLLGFILWGLYMGAQESIERAAVADLVPAELRGTAYGLFNTVVGIGWLLASLIAGYLWDLI
SPSAAFLFSAVLALIALLLLL
>gnl|CDD|340929 cd17371, MFS_MucK, Cis,cis-muconate transport protein and similar proteins of the Major Facilitator Superfamily. This subfamily is composed of Acinetobacter sp. Cis,cis-muconate transport protein (MucK), Escherichia coli putative sialic acid transporter 1, and similar proteins. MucK functions in the uptake of muconate and allows Acinetobacter calcoaceticus ADP1 (BD413) to grow on exogenous cis,cis-muconate as the sole carbon source. The MucK subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
FWAAFLGWALDGFDLLLLGLVLPALIAEFGLDEAEAGLLGTVTLAGGAIGGILGGILADRFGRVRVLVIT
ILLFAVFTLLCGFAQNYWQLLILRALAGLGFGGEWAAGAALMAEYVPARHRGKALGYVQSGWAVGWLLAT
LLAALLFPLLPPEIAWRVLFLLGALPALLVLFIRRFVKEPPQWQAARAARRHFADRPSLRELFSPPLLRT
TLLASLLATGALGGYYGITTWLPSYLTGERGLSFEGSAGYLVVTILGGFLGYLAGGFLADRIGRRNNFAL
FALGSAISILLYFFLPLSPTLILILGFPLGFFASGPFSGMGAYLTELFPTAVRATAQGFCYNVGRIIGAL
FPFLVGFLATSGSLGTAIAVFAAVYYIAGLVLALLLPET
>gnl|CDD|340930 cd17372, MFS_SVOP_like, Synaptic vesicle 2-related protein (SVOP) and related proteins of the Major Facilitator Superfamily. This subfamily is composed of synaptic vesicle 2 (SV2)-related protein (SVOP), SVOP-like protein (SVOPL), and similar proteins. SVOP is a transporter-like nucleotide binding protein that localizes to neurotransmitter-containing vesicles. Like SV2, SVOP is expressed in all brain regions, with highest levels in cerebellum, hindbrain and pineal gland. Studies with knockout mice suggets that SVOP may perform a subtle function that is not necessary for survival under normal conditions, since mice lacking SVOP are viable, fertile, and phenotypically normal. SVOP and SVOPL share structural similarity to the solute carrier family 22 (SLC22), a large family of organic cation and anion transporters. The SVOP-like subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LAYAGMGWVAEAMEMMLLSFVGPAVQCEWNLSAWQVALITSVVFAGMMIGSYLWGIVSDKYGRRKGLIIS
ALWTFYAGFLSAFAPNYMWLIILRCLVGLGLGGGPQLASWYLEFLPAKSRGTWMVLFSVFWTVGTIFEAS
LAWLVMPRLGWRWLLAFSSVPSSLLLVFYRWTPKTTLLLWVIWFGNAFAYYGVVLLTTELNNSHNVCGSK
SDSDSGESPTEKQCRNSNDVDYRDVFIATFAEFPGLLISAAMIDRLGRKASMASMLFTCCIFLLLLLICQ
SPFILTVLLFGGRACISAAFTVVYIYTPEVYPTAVRALGVGTGSSVGRIGAILCPFIAQVLVHGSQTIAL
LLFSVVCLVSAICVCLL
>gnl|CDD|340931 cd17373, MFS_SLC22A17_like, Solute carrier family 22, member 17 and similar proteins of the Major Facilitator Superfamily. This group is composed of Solute carrier family 22, members 17, 23, and 31. They are members of the SLC22 family of organic cation/anion/zwitterion transporters, which includes organic cation transporters (OCTs/OCTNs) and organic anion transporters (OATs). SLC22A17 functions as a cell surface receptor for lipocalin-2 (LCN2), also called NGAL or 24p3, which plays a key role in iron homeostasis and transport. SLC22A23 and SLC22A31 are orphan members of the SLC22 family. SLC22 transporters interact with a variety of compounds that include drugs of abuse, environmental toxins, opioid analgesics, antidepressant and anxiolytic agents, and neurotransmitters and their metabolites. The SLC22A17-like group belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
WDYGIRAGLVQNAVSKWDLVCDNGWKVHLEQFSLLLGLIFGYLILGCIADRFGRRPVLLFSLILILIFGL
TVALAVSVTMFSTLRFLEGFCLAGIILTLYLLRLELCDPGKRLMITMVASLVAVAGQFLMPGLAALCRDW
RVLQALIICPFLLMLLYWSIFPKNILILGFNSLTGYGIRHCFARSMMGHEPENFYLDYYLTAGIAAVACV
FLCVTVDFLGRRGGLLLFMILTGLASLLLLGLLNLIGKYSQHPDSGMSDSVKDKFSIAFSVLGLFASHAV
GSLSVLFAAEVTPTVIRGGGLGLVLASGGLGMLTGPIIELHNQKGYFLQHVVFACCALLCILCILLLP
>gnl|CDD|340932 cd17374, MFS_OAT, Organic anion transporters of the Major Facilitator Superfamily of transporters. Organic anion transporters (OATs) generally display broad substrate specificity and they facilitate the exchange of extracellular with intracellular organic anions (OAs). Several OATs have been characterized including OAT1-10 and urate anion exchanger 1 (URAT1, also called SLC22A12). Many OATs occur in renal proximal tubules, the site of active drug secretion. OATs mediate the absorption, distribution, and excretion of a diverse array of environmental toxins, and clinically important drugs, including anti-HIV therapeutics, anti-tumor drugs, antibiotics, anti-hypertensives, and anti-inflammatories, and therefore is critical for the survival of the mammalian species. OAT falls into the SLC22 (solute carrier 22) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
SEADTEPCVDGWVYDRSKFTSTIVTEWDLVCESQSLKSVAQSIFMAGLLVGALIFGHLSDRFGRKFILLL
SLLQLAIFGTCAAFAPTFPVYCVLRFLAGFAVSGISINTLILGTEWTTPRHRALAITLTSCFFSIGQMLL
AGLAYAIRDWRLLQLVVSVPFFLFFLYSWWLPKRTLILSFVWFANSFSYYGLSLDLQHLGLNVFLLQFLF
GAVEVPARCLALFLLNHMGRRISQAVLLLLAGLCILANIFVPQEMQTLRTVLAVLGKGSSAAAFTISYVY
TAELFPTVLRQTGMGLNSMFARIGGILAPLIMLLGVYSPLLPMIIYGVLPILAGLLALLLP
>gnl|CDD|340933 cd17375, MFS_SLC22A16_CT2, Solute carrier family 22 member 16 (also called Carnitine transporter 2) of the Major Facilitator Superfamily of transporters. Solute carrier family 22 member 16 (SLC22A16) is also called carnitine transporter 2 (CT2), fly-like putative transporter 2 (FLIPT2), organic cation transporter OKB1, or organic cation/carnitine transporter 6 (OCT6). It is a partially sodium-ion dependent high affinity carnitine transporter. It also transports organic cations such as tetraethylammonium (TEA) and doxorubicin. It is one of several organic cation transporters (OCTs) that falls into the SLC22 (solute carrier 22) family. OCTs are broad-specificity transporters that play a critical role in the excretion and distribution of endogeneous organic cations and for the uptake, elimination and distribution of cationic drugs, toxins, and environmental waste products. SLC22A16 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GNKTRFSCSDGFVYDQSKWESSIVTDWDLVCDREWLAKLIQPIFMLGVLLGAVIFGDIADRIGRRPVLWF
TSTGQFVFGIAVAFTFDYYSFVIVRFLLAMVSSGYLVVVFVYVTEFTGIKARTWASMHVHAFFAVGIMVV
ALVGYLVRTWWIYQIILSLVTIPFILCCWMLPKRTITVWLIWFTGSLGYYVFSLGSVNLGGNEYLNLFLV
GAVEIPSYIIACIGMDKLGRRNTLAPFLLLSALACMLIMVIPQDYEVLTIVLSMTGKFAIAIAFGLIYLY
TAELYPTIVRSLAVGSGSMMCRVGSVVAPFCVYLSDVWIFLPQLLVGIMAFLSGILTLMLP
>gnl|CDD|340934 cd17376, MFS_SLC22A4_5_OCTN1_2, Solute carrier family 22 members 4 and 5 (also called Organic cation/carnitine transporters 1 and 2) of the Major Facilitator Superfamily of transporters. This subfamily is composed of solute carrier family 22 members 4 (SLC22A4) and 5 (SLC22A5), and similar proteins. SLC22A4 is also called ergothioneine transporter (ETT) or organic cation/carnitine transporter 1 (OCTN1). It is a sodium-ion dependent, low affinity carnitine transporter, and a highly specific transporter for the uptake of ergothioneine (ET), a thiolated derivative of histidine with antioxidant properties. ET is a natural compound produced only by certain fungi and bacteria and must be absorbed from the diet by humans and other vetebrates. SLC22A5, also called organic cation/carnitine transporter 2 (OCTN2), is a sodium-ion dependent, high affinity carnitine transporter involved in the active cellular uptake of carnitine. SLC22A4/5 belongs to the Solute carrier 22 (SLC22) family of organic cation/anion/zwitterion transporters of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
TQIEQEPCLDGWEYSQDVYLSTIVTEWNLVCEDDWKVPLTTSLFFVGVLLGSFISGQLSDRFGRKKVLFA
TMAVQTGFSFLQIFSPSWEMFTVLFVIVGMGQISNYVVAFVLGTEILGKSVRILFSTLGVCIFYAIGYML
LPLFAYFIRDWRMLLLALTLPGVLCVPLWWFIPITTIMSLLLWMAISVGYFGLSLNTPNLHGDPYLNCFL
SAVIEVPAYIIAWLLLRSLPRRYSIAATLVLGGGVLLFIQLVPTDLQVLATALVMLGKFGITAAFSMVYV
YTAELYPTVVRNMGVGVCSTASRIGSIISPYFVYLGAYDRYLPYILMGSLTVLIGILTLFLP
>gnl|CDD|340935 cd17377, MFS_SLC22A15, Solute carrier family 22 member 15 of the Major Facilitator Superfamily of transporters. Solute carrier family 22 member 15 (SLC22A15) is also called fly-like putative transporter 1 (FLIPT1). It is expressed at the highest levels in the kidney and brain. It is a member of the SLC22 family of transporters, which includes organic cation transporters (OCTs), organic zwitterion/cation transporters (OCTNs), and organic anion transporters (OATs). SLC22 transporters interact with a variety of compounds that include drugs of abuse, environmental toxins, opioid analgesics, antidepressant and anxiolytic agents, and neurotransmitters and their metabolites. SLC22A15 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
AFGEWLLTANDSEVHKHVHFSSSFTSIVSEWFLVGNAAYKVSLASSFFFAGVLIGVVSFGQLSDRFGRKP
VYLTGLALDILFAYFNALAPSYEFFAVSRFLVGVMNGGMSLVAFVLLNECVGKSYWALAGSLGGLFFAVG
IAQYALLGYFIRSWRTLAVVVNLQGTLVFLLSLFIPGRTLILMYVWFVCSLVYYGLTLNAGDLGGNIYLN
LALSGLVELPAYPLCIYLINQKWSGRRRTLAGFLFLGGIACLLVMFVPEKKDSGVFAVVNSTSLSLLGKL
TISAAFNIVYIYTSELYPTVVRNAGLGVCSMFSRVGGIIAPFIPSLKSVQWSLPFIVFGASGLSAGLLSL
LLP
>gnl|CDD|340936 cd17378, MFS_OCT_plant, Plant organic cation/carnitine transporters of the Major Facilitator Superfamily of transporters. Plant organic cation/carnitine transporters (OCTs) are sequence-similar to their animal counterparts, which are broad-specificity transporters that play a critical role in the excretion and distribution of endogeneous organic cations and for the uptake, elimination and distribution of cationic drugs, toxins, and environmental waste products. Little is know about plant OCTs. In Arabidopsis, there are six genes belonging to this family that show distinct, organ-specific expression pattern of the individual genes. AtOCT1 has been found to affect root development and carnitine-related responses in Arabidopsis. AtOCT4, 5 and 6 are up-regulated during drought stress, AtOCT3 and 5 during cold stress and AtOCT5 and 6 during salt stress treatments. Plant OCTs belongs to the Solute carrier 22 (SLC22) family of organic cation/anion/zwitterion transporters of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
SDICKLPRSSWEWDGGSKVSIVSEWGLICAGSFLVGLPQSSFFVGCLIGSGVLGHLADSSLGRKNLLFLS
CLLMALSGIATAFSPNYWVYAFLRFLTGFGRSGIGTCALVLATEPVGPKWRGQVGMSTFFFFVLGFMSLP
GIAYLNGSSWRVLYFWTSIPALIYCILVYLFARRLLAVMVIGFGIGMVYYGIPLAVGNLKFNIYLSVALN
ALSELPAFVITAFLLDRFGRRPSLLGFTLLSGASCLLCFVLSIGGTTSLQIALELVGFFGAAGAFNLLYI
YTVELFPTCVRNAALGMLRQALVVGGIFAPFIVSLGRKNAALSFGVFGVAILLLGLFALGLP
>gnl|CDD|340937 cd17379, MFS_SLC22A1_2_3, Solute carrier family 22 members 1, 2, and 3 (also called Organic cation transporters 1, 2, and 3) of the Major Facilitator Superfamily of transporters. This sufamily includes solute carrier family 22 member 1 (SLC22A1, also called organic cation transporter 1 or OCT1), SLC22A2 (or OCT2), SLC22A3 (or OCT3), and similar proteins. OCT1-3 have similar basic functional properties: they are able to translocate a variety of structurally different organic cations in both directions across the plasma membrane; to translocate organic cations independently from sodium, chloride or proton gradients; and to function as electrogenic uniporters for cations or as electroneutral cation exchangers. They show overlapping but distinct substrate and inhibitor specificities, and different tissue expression pattern. In humans, OCT1 is strongly expressed in the liver, OCT2 is highly expressed in the kidney where it is localized at the basolateral membrane of renal proximal tubules, and OCT3 is most strongly expressed in skeletal muscle. OCTs are broad-specificity transporters that play a critical role in the excretion and distribution of endogeneous organic cations and for the uptake, elimination and distribution of cationic drugs, toxins, and environmental waste products. The SLC22A1-3 subfamily belongs to the Solute carrier 22 (SLC22) family of organic cation/anion/zwitterion transporters of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
SMLPLSPCQDGWVYNTPRSSIVTEFNLVCEDAWKLDLFQSSLNLGFLIGSIVIGYLADRFGRKVCFLISI
LGNGVSGVLMAFSPNYPWFLIFRFLQGLFGKGGWMTGYVLVTEFVGSKYRRTVGIVYQMFFTLGLLILPG
IAYFIPHWRWLQLAVTLPNFLFLLYYWFIPKHTFILMYAWFTSAVVYQGLIMRLGITGGNLYLDFFISAL
VELPAAFIILLTIDRIGRRLPFAASNIVAGAACLITAFIPPDLHWLKTTIACVGRLGITMAFEIVCLVNT
ELYPTFLRNLGVSVCSSLCDIGGIIAPFLLYRLAEIWLELPLIVFGVLALVAGGLVLLLP
>gnl|CDD|340938 cd17380, MFS_SLC17A9_like, Solute carrier family 17 member 9 and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily includes solute carrier family 17 member 9 (SLC17A9) and similar proteins including plant inorganic phosphate transporters (PHT4) that are also probably anion transporters. SLC17A9, also called vesicular nucleotide transporter (VNUT), is involved in vesicular storage and exocytosis of ATP. It facilitates the accumulation of ATP and other nucleotides in secretory vesicles such as adrenal chromaffin granules and synaptic vesicles. It also functions as a lysosomal ATP transporter and regulates cell viability. Plant PHT4 family transporters mediate the transport of inorganic phosphate and may also transport organic anions. The Arabidopsis protein AtPHT4;4 is a chloroplast-localized ascorbate transporter. PHT4 proteins show differential expression that suggests specialized functions. The SLC17A9-like subfamily belongs to the Solute carrier 17 (SLC17) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VILLFLATCICYADRVNMPIAIVPMAKEFGWSKTDQGLVLSSFFWGYALTQVLGGYLADRFGGKKVLLLA
VALWSLATLLTPLLAYSSLPLLILSRILLGLGEGVHFPSMTSLFSRWVPVSERSRAVSIVTAGSYLGTLL
GGLIGPLLLEYYGWPSVFYFFGLLGLLWALVWLIYLPPVWAIIVAHFCMNWGFYILLSWLPTYFHEVLVP
LAKGWVFNVVPWLVMFPSSNVAGWLADHLISRGWTVTSVRKLMQSIGFLGPALFLLLLSHTDSFSLALLC
MSVALGLSAFSSSGVLVNHQDIAPNYAGIVFGISNTAGTIPGIVGVYLTGYILEATGSWSLVFVLAAVVN
LVGAVVFLLFG
>gnl|CDD|340939 cd17381, MFS_SLC17A5, Solute carrier family 17 member 5 (also called sialin) of the Major Facilitator Superfamily of transporters. Solute carrier family 17 member 5 (SLC17A5) is also called sialin, H(+)/nitrate cotransporter, H(+)/sialic acid cotransporter (AST), membrane glycoprotein HP59, or vesicular H(+)/aspartate-glutamate cotransporter. It transports glucuronic acid and free sialic acid out of the lysosome after its cleavage from sialoglycoconjugates, which is required for normal CNS myelination. It also mediates the membrane potential-dependent uptake of aspartate and glutamate into synaptic vesicles and synaptic-like microvesicles. In the plasma membrane, it functions as a nitrate transporter. Recessive mutations in the SLC17A5 gene cause the allelic disorders, Infantile sialic acid storage disease (ISSD) and Salla disease (a predominantly neurological disorder). SLC17A5 belongs to the Solute carrier 17 (SLC17) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LALLAFFGFFVVYALRVNLSVALVDMVNSNSTLPSNNSSNACPEHSSSPSVEHNETGKKYDWDAETQGWI
LGSFFYGYIITQIPGGYLASKIGGKLLLGFGILGTAVFTLLTPLAADLGAGYLIAVRALEGLGEGVTFPA
MHAMWASWAPPLERSRLLTISYAGAQLGTVVSLPLSGLICYYLDWTYVFYIFGAVGLLWFFLWIWLVMPL
WAIVVAHFSYNWTFYTLLTLLPTYMKEILRFDIQENGFLSALPYLGCWLFMILSGQIADNLREKQNFSTV
CVRKIFTLIGMIGPAVFLLAAGFTGCNYSLAVAFLTISSTLGGFSASGFNINHLDIAPSYAGILLGITNT
FATIPGMVGPVIAKSLTHNNTVEEWQTVFYISAAINVFGAIFFTIFG
>gnl|CDD|340940 cd17382, MFS_SLC17A6_7_8_VGluT, Solute carrier family 17 members 6, 7, and 8 (also called Vesicular glutamate transporters) of the Major Facilitator Superfamily of transporters. This subfamily is composed of solute carrier family 17 member 6 (SLC17A6), SLC17A7, SLC17A8, and similar proteins. SLC17A6 is also called vesicular glutamate transporter 2 (VGluT2), differentiation-associated BNPI, or differentiation-associated Na(+)-dependent inorganic phosphate cotransporter. SLC17A7 is also called VGluT1 or brain-specific Na(+)-dependent inorganic phosphate cotransporter. SLC17A8 is also called VGluT3. They mediate the uptake of glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells, and may also mediate the transport of inorganic phosphate. VGluTs are also expressed and localized in various secretory vesicles in non-neuronal peripheral organelles such as hormone-containing secretory granules in endocrine cells, and thus, also act as metabolic regulators. The VGluT subfamily belongs to the Solute carrier 17 (SLC17) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
AIMAGLGFCISFGIRCNLGVAIVRMVNNFTDAYGGKVIVHKAEFNWTPETVGLIESSFFWGYLVTQIPGG
FIAAKFAANRVFGLAIFVTSTLNMLIPIAARVHYGCVIFVRILQGLVEGVTYPACHGIWRKWAPPLERSR
LATTAFCGSYAGAVVGMPLSGILVQYVGWSSPFYVYGVFGIIWYMFWMLVSMPVYAIIVANFCRSWTFYL
LLISQPAYFKEVFGFDISKVGILSALPHLVMTIIVPIGGQLADYLRSRGILSTTAVRKIFNCGGFGMEAT
FLLVVAFSHSPTVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGIGTLSGMVCPVIVGALT
KHKTREEWQYVFLIASLVHFFGVIFYAIFA
>gnl|CDD|340941 cd17383, MFS_SLC18A3_VAChT, Vesicular acetylcholine transporter (VAChT) and similar transporters of the Major Facilitator Superfamily. Vesicular acetylcholine transporter (VAChT) is also called solute carrier family 18 member 3 (SLC18A3) in vertebrates and uncoordinated protein 17 (unc-17) in Caenorhabditis elegans. It is a glycoprotein involved in acetylcholine transport into synaptic vesicles and is responsible for the accumulation of acetylcholine into pre-synaptic vesicules of cholinergic neurons. Variants in SLC18A3 are associated with congenital myasthenic syndrome in humans. VAChT belongs to the bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LVIVCIALLLDNMLYMVIVPIIPDYLNEDIAIGVLFASKAIVQLLVNPFSGTLIDRVGYDIPMMIGLTVM
FLSTAVFAFGESYAVLFFARSLQGVGSAFADTAGLAMIADRFTEEAERSKALGIALAFISFGCLVAPPFG
GILYEFAGKEVPFLILAFVCLLDGLLLLLVMKPVRRETRANMPEPVGTPIHRLLMDPYIAVCAGALTMAN
VSLAFLEPTIANWMKDTMNASEWQMGLVWLPAFFPHVLGVYLTVKLAAKYPHYQWLMAAVGLAIEGASCF
IVPFCTNFGVLIIPLCGICFGIALVDTALLPTLGFLVDVRHVSVYGSVYAIADISYSLAYALGPIVAGQI
VHSIGFTQLNIGIGLANLLYAPVLLLLR
>gnl|CDD|340942 cd17384, MFS_SLC18A1_2_VAT1_2, Vesicular amine transporters 1 (VAT1) and 2 (VAT2), and similar transporters of the Major Facilitator Superfamily. Vesicular amine transporter 1 (VAT1 or VMAT1) is also called solute carrier family 18 member 1 (SLC18A1) or chromaffin granule amine transporter, while VAT2 (or VMAT2) is also called SLC18A2, synaptic vesicular amine transporter, or monoamine transporter. VATs (or VMATs) are responsible for the uptake of cytosolic monoamines into synaptic vesicles in monoaminergic neurons. VAT1 and VAT2 distinct pharmacological properties and tissue distributions. VAT1 is preferentially expressed in neuroendocrine cells and endocrine cells, where it transports biogenic monoamines, such as serotonin, from the cytoplasm into the secretory vesicles. VAT2 is primarily expressed in the CNS and is involved in the ATP-dependent vesicular transport of biogenic amine neurotransmitters including dopamine, norepinephrine, serotonin, and histamine into synaptic vesicles. VATs belong to the bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VLVIVYVALLLDNMLLTVVVPIIPDYLNENVRVGLLFASKALVQLITNPIVGPLTNRIGYSLPMFVGFVI
MFISTLLFAFGESYGVLFLARALQGVGSACSSVAGMGMLASLYPDDKERGKAMGIALGGLALGVLVGPPF
GGVMYEFVGKSAPFLILAFLALLDGALQLFILQPSVKSEESEEGTPWKTLLKDPYILIAAGAICFSNSGI
AILEPCLPIWMMETMCPPKWQLGTAFLPDSIGYLIGTNLFGPLAHKIGRWLCSLLGMLLVGISLILIPLA
KNIYGLIIPHFGLGLGIGMVDSSMMPLLAYLVDLRHSSVYGSVYAIADVAFCLAFALGPSLGGAIVKSIG
FPWLMRIIGIINILYAPLLFFLR
>gnl|CDD|340943 cd17385, MFS_SLC18B1, Solute carrier family 18 member B1 of the Major Facilitator Superfamily of transporters. Solute carrier family 18 member B1 (SLC18B1) is the fourth member of the SLC18 transporter family, which includes vesicular monoamine transporters and vesicular acetylcholine transporter. It is predominantly expressed in the hippocampus and is associated with vesicles in astrocytes. It actively transports spermine and spermidine by exchange of H(+), and has been suggested to be a vesicular polyamine transporter (VPAT). SLC18B1 belongs to the bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LISLALANFSSMICYSILAPFFPREAEKKGVSDTIIGLVFGCFALVIFLTSPIFGKYLVKIGAKFMFVAG
MFVSGGCTILFGFLDRVPDGTVFIALCFLVRIVEAVGFAAFITASFAIIAKEFPNNIATVLGTLETFSGL
GLMLGPPLGGFLYQAGGYELPFLVLGCLLLLTVPLNMFILPRYDDDPSPKSGSMLKLLKIPSVLLLCLSI
VSGSVSLGFLDPTLSPHLRQFKLSPGQVGLMFLILAGSYAISAPLWGWLSDKKKIPKWLMVIGSIITGVG
FLLLGPAPLLPIKSELWMVIIGLVLLGLSLGAALVPTFPELLNCAREYGFPDNLSTYGLVSGLFNAAFSL
GAFIGPTLGGFLLERLGFEWAATIQAGLAFVVGILMSIYY
>gnl|CDD|340944 cd17386, MFS_SLC46, Solute carrier 46 (SLC46) family of the Major Facilitator Superfamily of transporters. The solute carrier 46 (SLC46) family is composed of three vertebrate members (SLC46A1, SLC46A2, and SLC46A3) and similar proteins from insects and nematodes. The best-studied member is SLC46A1, also called proton-coupled folate transporter (PCFT), which functions both as an intestinal proton-coupled high-affinity folate transporter involved in the absorption of folates and as an intestinal heme transporter which mediates heme uptake. SLC46A2, also called thymic stromal cotransporter protein (TSCOT), is a putative 12-transmembrane protein mainly expressed in the thymic cortex in a specific thymic epithelial cell (TEC) subpopulation. SLC46A3 is a lysosomal membrane protein that functions as a direct transporter of noncleavable antibody maytansine-based catabolites from the lysosome to the cytoplasm. The SLC46 family belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance (TetA) -like (SLC46/TetA-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
MLNVEPIVFLYMFASVLSGPVTQNFVYAANFYLYMNLMGSIPPLFSSLFLGSWSDRYGRKPPLLMSLVGL
LLSSLILVLIVYFTTVPSVWWFYLSAIPLALFGGFTAFLSASFAYISDISSEKKRTYRMAILEVALGLGG
FLGSLLSGHLFKALGYAWSFSISAALLLIALLYILFFLTLLILLLLAAFLTIFVLSGESDVLYLFVLEKF
AWNVKDFSYFSTLGSLIYLTGMLGGVLLLRCLLKMSDSTLAMLGLASHILSSLLFAFATNTWMMYLAAVV
GMFNGIVGPMIRSILSKLVPKSEQGKIFSLLSVLESLSPLVASPIYNNIYKATLTTFPGFFFLLSAGLLL
IPVILIGVVY
>gnl|CDD|340945 cd17387, MFS_MFSD14, Major facilitator superfamily domain-containing 14A and 14B. This subfamily is composed of major facilitator superfamily domain-containing 14A (MFSD14A) and MFSD14B, and similar proteins. MFSD14A and MFSD14B are also called hippocampus abundant transcript 1 protein (HIAT1) and hippocampus abundant transcript-like protein 1 (HIATL1), respectively. They are both ubiquitously expressed with HIAT1 highly expressed intestis and HIATL1 most abundantly expressed in skeletal muscle. Gene disruption of MFSD14A causes globozoospermia and infertility in male mice. It has bee suggested that MFSD14A may transport a solute from the bloodstream that is required for spermiogenesis. The function of MFSD14B is unknown. The MFSD14 subfamily belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance (TetA) -like (SLC46/TetA-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VYHAVVVIFLEFFAWGLLTTPMITVLHETFPQHTFLMNGLVQGVKGILSFLSAPLIGALSDVWGRKSFLL
LTVFFTCAPIPLMRISPWWYFAMISVSGIFSVTFSVIFAYVADITTEEERSTAYGLVSATFAASLVTSPA
LGAYLSESYGDNLVVLVATIVALLDICFILLAVPESLPEKMRPASWGAPISWEQADPFASLRKVGKDKTV
LLICITVFLSYLPEAGQYSSFFVYLKQVMGFEYEEVAAFIAVVGILSITAQTLLLSILMRSIGAKNTILL
GLGFQMLQLAWYGFGSQHWMMWAAGAVAAMSSITFPAISALVSRYADPDQQGAVQGMITGIRGLCNGLGP
ALFGFVFYLFHVDLNEIKPVQSSKQRMQNPSLEGAIIPGPPFLFGAISVLLAILVASFIP
>gnl|CDD|340946 cd17388, MFS_TetA, Tetracycline resistance protein TetA and related proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of tetracycline resistance proteins similar to Escherichia coli TetA(A), TetA(B), and TetA(E), which are metal-tetracycline/H(+) antiporters that confer resistance to tetracycline by an active tetracycline efflux, which is an energy-dependent process that decreases the accumulation of the antibiotic in cells. TetA-like tetracycline resistance proteins belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance (TetA) -like (SLC46/TetA-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LIFILVTVLLDAMGIGLIMPVLPTLLREFVGDSADAATHYGVLLALYALMQFIFAPILGALSDRFGRRPV
LLLSLAGAALDYLLMAFAPTLWWLYLGRIIAGITGATGAVAAAYIADVTPPEQRARNFGLLGAAFGLGFI
AGPALGGLLGEISPRAPFLVAAGLNGLNFLLGLFVLPESLPPERRRAFRWRRANPFGSLRWLTGFPGLLG
LLAVFFLIQLIGQVPATTWVLFTEDRFDWSPTMVGLSLAVFGLLHALFQAFVTGPIAKRLGEKRAILLGL
AADALGFLLLAFATQGWMVFPILILLALGGIAGPALQGLLSRQVPENEQGELQGVLTSLTSLTSIIGPLL
FTGIFAASPATWPGLAWIIGAALYLICLVLAYRFF
>gnl|CDD|340947 cd17389, MFS_MFSD10, Major facilitator superfamily domain-containing protein 10. Major facilitator superfamily domain-containing protein 10 (MFSD10) is also called tetracycline transporter-like protein (TETRAN). It is expressed in various human tissues, including the kidney. In cultured cells, its overexpression facilitated the uptake of organic anions such as some non-steroidal anti-inflammatory drugs (NSAIDs). MFSD10/TETRAN overexpression cause resistance to some NSAIDs, suggesting that it may be an organic anion transporter that serves as an efflux pump for some NSAIDs and various other organic anions at the final excretion step. MFSD10 belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance (TetA) -like (SLC46/TetA-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
ITIVFLALLLDLLAFTIILPLFPSLLDYYGQNDDSGLYSLQISSVDWFRDAIGAPDERRYNSVLFGGLIG
SLFSLLQFLSSPITGAASDVYGRKPVLLLTMIGLAISYALWAVSRSFTIFLLSRIVGGISKGNVSLSTAI
VADVTSPKKRSKGMALIGVAFSLGFIIGPMIGAYFASFTRSLGEVFFSMPALFALVLALADLLFIFFFLP
ETLPSNLRRLGLVYFLYLFLFSGLEFTLTFLTHQRFQYTSMQQGKMFFFIGIIMALVQGGYVRRIKPGKE
KKAVLQGLILLIPAFLLIGWASSVTVLYAGLFLYSFAAATVVPCLTTLVSGYGSDDQKGTVMGIFRSLGA
LARALGPIVACTVYWLAGSEACYTIGALLFLLPLLLLARLK
>gnl|CDD|340948 cd17390, MFS_MFSD9, Major facilitator superfamily domain-containing protein 9. Major facilitator superfamily domain-containing protein 9 (MFSD9) is expressed in the central nervous system (CNS) and in most peripheral tissues but at very low expression levels. The function of MFSD9 is unknown. MFSD9 belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance (TetA) -like (SLC46/TetA-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LYLVGFLDLFGVSMILPLLSTHIRSLGASPTVIGLIGSVYGALQLFSSPLVGSWSDVVGRRPVLLICLLL
TALGYVLLGFSTSLALLFLSRIPLGIFKHTQSLCKAYLSDLVSEQERSRVLGRFNAASSLGFILGPVVGG
HLAETDGGFYYVALLCSAIFILNAGLVWFLLSKLWDLLLVRFLMGFSVLLFRSNFSLYLEERFDLSPKTI
GYLISYSGVLGALSGFLVGRILKLYKNNEYLLLLHSFILLALSLLGLALAPSIWLLVLCLTPLSISSAVL
RTCSTSLLLSRGKSKERGTLLGVGQSVTSLARILAPLLSGLLQEFSVSGPGLLGAVLALAAILLMLARQR
>gnl|CDD|340949 cd17391, MFS_MdtG_MDR_like, Multidrug resistance protein MdtG and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily. This subfamily is composed of Escherichia coli multidrug resistance protein MdtG, Streptococcus pneumoniae multidrug resistance efflux pump PmrA, and similar multidrug resistance (MDR) transporters from bacteria. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. MdtG confers resistance to fosfomycin and deoxycholate. PmrA serves as an efflux pump for various substrates and is associated with fluoroquinolone resistance. MdtG-like MDR transporters belong to the bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
CWLGNFFTGIGFSLIAPFLPLYIEQLGVTSGGLVELWSGLAFSSTFLVSAIFSPIWGRLADRYGRKPMLL
RASLGMAIVIGLMAFVTNVWQLLILRLLQGVFSGYVPNATALIASQTPKEKSGWALGTLSTGVVAGTLIG
PLLGGFLADLFGIRNVFFITGGLLFLAFLLTLFFVKEDFKPVEKKKMVSTKEVWNSVPNPSLLISLFVTT
FIIQLANQSIEPILTLYIRQLMGDASNLAFISGLVFSATGVSSLLSAPRLGKLGDRIGHHRILLGALLAS
ALLYIPQAFVQTPWQLGILRFLLGLATGGLLPAINSLLAKITPKEVAGRIFGYNQSFQYLGNVAGPLLGS
AIAAHFGYRAVFVVTALLVLLNAIWSFIFL
>gnl|CDD|340950 cd17392, MFS_MFSD2, Major facilitator superfamily domain-containing protein 2 subfamily. The major facilitator superfamily domain-containing protein 2 (MFSD2) subfamily is composed of two vertebrate members, MFSD2A amd MFSD2B. MFSD2A is more commonly called sodium-dependent lysophosphatidylcholine symporter 1 (NLS1). It is an LPC symporter that plays an essential role for blood-brain barrier formation and function. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. MFSD2B is a potential risk or protect factor in the prognosis of lung adenocarcinoma. The MFSD2 subfamily belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
KLCYAIGGAPYQMTSSATGFFLQIFLLDVAQMGAFSVSLILFVGRVWDAVTDPLVGYFISRSQRTGIGRL
MPWIVFSTPLIILAYFFLWFLPPFTSLSGLWYLTFYCLFETFMTCFHVPYSALTMFLGGCQRERDSATAY
RMTVEVFGTLMGATIQGQIVGVAHRPRRQDCTATPGTSDHPVTVLPNTRRAYLIAALVVVVLYFVCCSIL
FLGVKEQPDPLSPASGPGLSYLAGLKLVTGHPPYLKLVIGFLFSSLAFQMEQGNFVLFCTHAAGLGDHFQ
HLVLAILVSATLSIPLWQWVLQRRGKKTTSFIGISAMVPFLILLALVPSNLPVAYVVAVVSGVSLAALFL
LPWSMLPDVVDDFQLKNPHCPGLEPIFYSCYVFFTKLGGGLSLGISTLSLHFSGYKAGACKQPEEVVVTL
KVLIAPVPICLILAGLVLFYVYPINE
>gnl|CDD|340951 cd17393, MFS_MosC_like, Membrane protein MosC and similar proteins of the Major Facilitator Superfamily of transporters. The gene encoding Sinorhizobium meliloti membrane protein MosC is part of the mos locus, which encodes the biosynthesis of the rhizopine 3-O-methyl-scyllo-inosamine. MosC belongs to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RLAVAAFFFINGILMASWATRIPAIKDRLGLSDAALGLLLLALGVGALVAMPLAGRLVARFGSRRVTRLG
ALLLLLALLLLGLAPSVPALALALFLFGAANGALDVAMNAQGVAVERAYGRPIMSSLHAMWSLGGLAGAL
LGAAAIGAGVSPGVHLLAAAVLLLLAALVAIRALLPGTGEAAEDRPDGAGKPGFLLPNRLLLLLGLLALA
AALAEGAAADWSALYLRDVLGASAALAALGYAVFSLAMTVGRLFGDRLVDRFGDVAVLRAGALLAALGLL
LALLAPSVWVALAGFALMGLGLSVVVPLAFSAAGALPGLAAGIAVARVATLGYLGFLVGPPLIGFLADAT
GLRTAFLVVALLALLVALLARAV
>gnl|CDD|340952 cd17394, MFS_FucP_like, Fucose permease and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of L-fucose permease (also called L-fucose-proton symporter) and similar proteins such as glucose/galactose transporter and N-acetyl glucosamine transporter NagP. L-fucose permease facilitates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell; it can also transport L-galactose and D-arabinose. Glucose/galactose transporter functions in the uptake of of glucose and galactose. The FucP-like subfamily belongs to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LALVTSLFFLWGFATNLNDILIPQFKNIFDLSNFQASLVQFAFFGAYFIMAIPAGMLIKRYGYKKGILLG
LGLYAIGALLFIPAASLRTYGLFLIALFVLASGLALLQTAANPYVTVLGPEETAARRLNLAQAFNSLGST
IAPLFGSYLILSGIPSTATALAAMSAAELQAYKTAELASVQLPYLGIALVLLLLAVLILLSKLPEIEAAE
AEALGSKGTLLRLLKNPHLRLGVLAIFFYVGAEVAIWSFLINYLMEYIAGLTETSAATFVSYYWGGFMVG
RFLGTALLKKISPKKLLAVFALLGLLLLLGAIFTGGMVALYALVLVGFFNSIMFPTIFSLALKGLGKHTK
TGSGLLVMAIVGGAVVPLIQGAVADDAAGLRIAFLVPLLCFAYILFYGLRG
>gnl|CDD|340953 cd17395, MFS_MFSD4, Major facilitator superfamily domain-containing protein 4. The Major facilitator superfamily domain-containing protein 4 (MFSD4) subfamily consists of two vertebrate members: MFSD4A and MFSD4B. The function of MFSD4A is unknown. MFSD4B is more commonly know as sodium-dependent glucose transporter 1 (NaGLT1), a primary fructose transporter in rat renal brush-border membranes that also facilitates sodium-independent urea uptake. The MFSD4 subfamily belongs to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
TYWSVFFSFGLSIAFLGPTLLDLACNTNSSLPQISWVFFSRQLGYLLGSALGGVFKRTLNSLWALFTSSL
LIALVLAVIPFCKDVKVLASVMAIAGLAMGCLDTGANMQIVRMWQKDSAPFLQVLHFSFGFGAFLAPLIA
DPFLSYAYWIMALINLPVPMAVLMLLSKERLLTCCSQRRRKNLRRAPYSFFAIHITGALFLFMYVGLEGA
YGAFVYSYAVEKPGVGHKVAAYLPSLFWGTFTLGRLLSIPISSRMKPATMVVLNVVGVVVTSLVLLLFSK
SVVFLWIGTASLGLFLASTFPSMLSYTEDSLQYTGCSTTVLVTGAGLGEMVLPMLVGSIQPFQAQGSYSF
LVCGVLFGCLAFTFYIL
>gnl|CDD|340954 cd17396, MFS_YdiM_like, Inner membrane transport protein YdiM and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily contains Escherichia coli inner membrane transport proteins YdiM and YdiN, which belong to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
TALGLYFNYFVHGMGVIILAQNMSSLSEKWHTDVAGVAYVISGIGIGRLLTILFAGVLSDKFGRKPSVLL
GMVLYALFFVGILFSPNLIIAYVFALLAGAANSFLDTGTYPALMEAFPKASGSANILVKAFVSFGQFLLP
FIIAFLAANNLWYGWSFIVPAAVLVLNALLLLKLSFPPQTVTAANTKQKEIPVKREKPKFLIEGIALILI
GFTSTATFYLFSQWMPKYGSAVAGMGEAESLKLISYYSMGSLVCVFITAVLLKRYVRPIWILVLYPIISL
LALFVLYLVPSPDVCILGAFVIGFFAAGGVLQLGLTLMAEFFPKGKGKVTGIYMIASSLANFVIPLITGI
IASAIGIAYIFLFDFGIALLGLLLAIFVFIRYRK
>gnl|CDD|340955 cd17397, MFS_DIRC2, Disrupted in renal carcinoma protein 2 of the Major Facilitator Superfamily of transporters. Disrupted in renal carcinoma protein 2 or disrupted in renal cancer protein 2 (DIRC2), encoded by the SLC49A4 gene, was initially identified as a breakpoint-spanning gene in a chromosomal translocation associated with the development of renal cancer. It is an electrogenic lysosomal metabolite transporter that is regulated by limited proteolytic processing by cathepsin L. DIRC2 belongs to the Solute carrier 49 (SLC49) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RRWYILLVFSLLAFTQGAVWNTWGPIADSAKPAFGWSDSDIALLANWGPIGFVPTFFFMAWLMDVKGLRI
AVLSSAFLVAAGTGLRCIPVPNHLATWLIHIGQFLNGLAGPVAMAAAPFLSATWFPPNQRATATAIASIF
NYLGGAASFLIGPLVLMYLEFGWSALIFLAMLIYFPSKPPTPPSVSASTQRLSYKSGILSLLKNKRFWLI
ALAYGIPTGVYAGWSGVLDVNLTPFGVSQVEAGWIGFYSTVAGCVGGIIVGRFADRFGGRMKLILLLLFS
GATGSFLWFTLICLKLLPFSTVSLYTSCILLGVFLNGSVPLFYELAVEAAYPVPEGITSGVLTFLNNVFG
LVFLLILIIPNIGTSWMNWCLLGSCLLSVPL
>gnl|CDD|340956 cd17398, MFS_FLVCR_like, Feline leukemia virus subgroup C receptor subfamily of the Major Facilitator Superfamily of transporters. The Feline leukemia virus subgroup C receptor (FLVCR) subfamily is conserved in metazoans and is composed of two vertebrate members, FLVCR1 and FLVCR2. FLVCR1 is a heme transporter and it has two isoforms: 1 (or FLVCR1a), which exports cytoplasmic heme as well as coproporphyrin and protoporphyrin IX; and 2 (FLVCR1b), which promotes heme efflux from the mitochondrion to the cytoplasm. FLVCR2 functions as a heme importer as well as a transporter for a calcium-chelator complex that is important for growth and calcium metabolism. The FLVCR subfamily belongs to the Solute carrier 49 (SLC49) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RRWIMLFLFCLYSMSNAFQWIQYAIISNIIVDYYGVSDTAVDWTSMIYMLTYIPLIFPATWLLEKYGLRV
TVLLGSFLNCLGAWLKLFSSSPDLFWVAMAGQTICALAQVFILGIPPRLAAVWFGPDEVSTATAIGVFGN
QLGVALGFVLPPLLVPNSENKDEIGKGLSILFYGVAGICTALFILVIIFFKEKPPIPPSRAQAAAQELRS
EDQSYLGSLKRLFKNKGFLLLLITYGINTGVYYAISTLLNQMVLEYFPNEEVNAGWIGLTLVIAGLVGSV
VAGIWLDKTKKYKETTIIVYILSFIGMVAFTFTLDLGSIWVVFLTAGALGFFMTGYLPVGFEFAAELTYP
EPEGTSSGLLNASAQIFGIIFTLVMGALLDKVGALASNIVLSVALLLGTILTAFIK
>gnl|CDD|340957 cd17399, MFS_MFSD7, Major facilitator superfamily domain-containing protein 7. Major facilitator superfamily domain-containing protein 7 (MFSD7) is also called myosin light polypeptide 5 regulatory protein (MYL5). It's function is unknown. It is encoded by the a SLC49A3 gene and is a member of the Solute carrier 49 (SLC49) family, which also includes feline leukemia virus subgroup C receptor 1 (FLVCR1, SLC49A1), FLVCR2 (SLC49A2), as well as disrupted in renal carcinoma protein 2 (DIRC2, SLC49A4). FLVCR1 and FLVCR2 are heme transporters. DIRC2 is an electrogenic lysosomal metabolite transporter that is regulated by limited proteolytic processing by cathepsin L. MFSD7 belongs to the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RRWFVLLVVCLLNCSNAMIWISFAPVADYTAEYYNVSLDAVNWLSLIYMIVSIPVGFVAMWLLDTLGLRT
AIILGAWLNFIGAVIRVISSLPFVDPSFRFPVLMTGQTLAAFAQPFILFLPTKLAALWFPDNQRAIANML
ASMSNPLGVLLANLLSPLIVKSSEDIFLLLSIYTIPALIAVVLATFGVRSSVPPTPPSASAAHESEPFFV
GLKQLFKNKQYLILMLCFGGGIGLFNALSTLLEQILCPSGYSNNFAGICGALMIGVGLIGAFVAGLIVDK
TKKFIEVTKVCFCLAVIFLVAFLVVSRFPNQSVLLAVLCGLFGFFGFAIYPVGLELAVECTYPVAEATST
GLIFMSGQIQGIILVFIMQALATPLSVYDLPIQCASSASGNITPLDWTVPLLVMAGLAAVLAIIFVVFF
>gnl|CDD|340958 cd17400, MFS_SLCO1_OATP1, Solute carrier organic anion transporter 1 family of the Major Facilitator Superfamily of transporters. The Solute carrier organic anion transporter 1 (SLCO1) or Organic anion transporting polypeptide 1 (OATP1) family contains three subfamilies: OATP1A, OATP1B, and OATP1C. OATP1A contains one human member, OATP1A2, which shows a broad spectrum of substrates including endogenous compounds (such as bile acids, steroid hormones and their conjugates, thyroid hormones) and various drugs (such as fexofenadine, ouabain and the cyanobacterial toxin microcystin). OATP1B contains two human proteins, OATP1B1 and OATP1B3, which can both accept a wide variety of structurally-unrelated compounds as substrates including clinically-important drugs such as hydroxymethylglutaryl (HMG)-CoA reductase inhibitors (statins), angiotensin II receptor blockers (sartans), angiotensin converting enzyme (ACE) inhibitors, and anti-diabetes drugs (glinides). OATP1C contains one mammalian member, OATP1C1, which is also called thyroxine transporter. It mediates the high affinity transport of the thyroid hormones, T4 (3,5,3',5'tetraiodo-L-thyronine or thyroxine), rT3 (3,3'5'-triiodo-L-thyronine), and T3 (3,5,3'tri-iodo-L-thyronine or triiodothyronine). The SLCO1/OATP1 family belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LKMFLLALSCAFVAKTLSGSYMKSMITQIERRFNIPSSLVGFIDGSFEIGNLLVIIFVSYFGTKLHRPKM
IGIGCVIMGLGCFLKALPHFFMNQYEYSLMWIYVFVGNILRGIGETPILPLGISYIDDFAKEENSPLYIG
LVETGAIIGPIIGFLLGSLCAKVYVDIGFVNLDDIIITPTDTRWVGAWWLGFLICGGVSVLTAIPFFFLP
PIYMLFILVSVIQFNSFVGMITYMPKYLEQQYGQSSSDANFLMGIINIPPIAIGYFIGGLIMKKFKITVK
GAAKIGCWLSVLEYLLYLLSFLMTCENSSVAGLTTSYEGIPPVLYHENDIFSDCNSDCNCPEKIWEPVCG
NNGITYLSACLAGCETSIGTGKNIVFYNCSCIQTSGNSSANLSLCDGGCPRDPDCSLMFQYFLIISVMSS
FIYSLGGIPGYMLLLR
>gnl|CDD|340959 cd17401, MFS_SLCO2_OATP2, Solute carrier organic anion transporter 2 family of the Major Facilitator Superfamily of transporters. The Solute carrier organic anion transporter 2 (SLCO2) or Organic anion transporting polypeptide 2 (OATP2) family contains two subfamilies: OATP2A and OATP2B, each containing one mammalian member, OATP2A1 and OATP2B1, respectively. OATP2A1 (encoded by SLCO2A1) is a lactate/prostaglandin anion exchanger that mediates the release of newly synthesized prostaglandins (PGD2, PGE1, PGE2, PGF2A and PGI2) from cells, the transepithelial transport of prostaglandins, and the clearance of prostaglandins from the circulation. OATP2B1 (encoded by SLCO2B1) mediates the Na(+)-independent transport of various organic anions such as taurocholate, the prostaglandins PGD2, PGE1, PGE2, leukotriene C4, thromboxane B2 and iloprost, as well as endogenous sex steroid conjugates such as dehydroepiandrosterone sulfate (DHEAS). The SLCO2/OATP2 family belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
IKVFVLCHGLLQLCQLLYSGYLKSSITTIEKRFGLSSSSSGLLASFNEVGNTILIVFVSYFGSRVHRPRL
IGIGGLFLAAGAFLLTLPHFISEPYQYGIMVVAQLLLGIGGVPIQPFGISYIDDFAEPSNSPLYLGILFA
VTVFGPAFGYLLGSVMLRLYVDIGRMNTAAVNLVPGDPRWIGAWWLGFLIAAALLVLTSFPYFFFPRFIK
RFPCIFLRTLRNPIFLLVVLAQVTLSSMIAGLATFLNKFLEKQFGTTASYANFLIGAVNLPSAALGILFG
GVLMKRLVLSLQAIPAICTTIITISMIFCVPLFFIGCSTPTIAGVYPPSSSSSIHPQSPACRRDCSCPDS
IFNPVCGDNGVEYLSPCHAGCSNINMSTSATSKQVIYTNCSCVTGGSASAKTGSCPSPCSHLLLPFIFLI
SLVSLIACLSHTPSFMMILR
>gnl|CDD|340960 cd17402, MFS_SLCO3_OATP3, Solute carrier organic anion transporter 3 family of the Major Facilitator Superfamily of transporters. The Solute carrier organic anion transporter 3 (SLCO3) or Organic anion transporting polypeptide 3 (OATP3) family contains only one subfamily, OATP3A, which contains only one mammalian member OATP3A1 (encoded by SLCO3A1). It mediates the Na(+)-independent transport of organic anions such as estrone-3-sulfate, prostaglandins (PG) E1 and E2, thyroxine (T4), deltorphin II, BQ-123, and vasopressin. SLCO3A1 has been identified as a Crohn's disease (CD)-associated gene, which mediates inflammatory processes in intestinal epithelial cells through NF-kappaB transcription activation, resulting in a higher incidence of bowel perforation in CD patients. The SLCO3/OATP3 family belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
IKIFLVSECALMLAQGTVGAYLVSVLTTLERRFNLQSADVGVIASSFEIGNLALILFVSYFGARGHRPRL
IGCGGIVMALGALLSALPEFLTHQYKTNMMYLLLIGAQVLLGIGATPVQPLGVSYIDDHVRRKDSSLYIG
ILFTMLVFGPACGFILGSFCTKIYVDAVFIDTSKLDITPDDPRWIGAWWGGFLLCGALLFFSALLMFGFP
QSLQQLRVIPKVTKHLLSNPVFTCIVLAACMEIAVVAGFAAFLGKYLEQQFNLTTSSANQLLGMTAIPCA
CLGIFLGGLLVKKLSLSALGAIRMAMLVNLVSTACYVSFLFLGCDTGPVAGVTVPYGNDTAPGSSLDPYA
PCNSNCECQTDSFSPVCGADGITYLSACFAGCSSTNLSGCACLSSVPAENATVVPGKCPSPGCQEAFLTF
LCVMCVCSMIGAMAQTPSVIILIR
>gnl|CDD|340961 cd17403, MFS_SLCO4_OATP4, Solute carrier organic anion transporter 4 family of the Major Facilitator Superfamily of transporters. The Solute carrier organic anion transporter 4 (SLCO4) or Organic anion transporting polypeptide 4 (OATP4) family contains two families: OATP4A and OATP4C, each containing one mammalian member, OATP4A1 and OATP4C1, respectively. OATP4A1 (encoded by SLCO4A1), is ubiquitously expressed and mediates the Na(+)-independent transport of the thyroid hormones T3 (triiodo-L-thyronine), T4 (thyroxine) and rT3, and other organic anions such as estrone sulfate and taurocholate. OATP4C1 (encoded by SLCO4C1) is capable of transporting pharmacological substances such as digoxin, ouabain, thyroxine, methotrexate, cAMP, and uremic toxins, which accumulate in patients with chronic kidney diseases (CKDs). The SLCO4/OATP4 family belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
PKGFLFFLCIFAFLQGMVVNGFVNVSITTIEKRFGLTSTQTGLIASSYDIASVLLLLFVSYFGGRGHKPR
WLGIGAFIMGIGSLVFALPHFTVFILAQLLHGAGATPLYTLGVTYLDENVSTKMSPLYIGIFYAMAILGP
AIGYVLGGFLLNLYTDIDQVDSELGLTPDDPRWVGAWWLGFLISGALALIIAFPLLGFPPTFMFLNLAGA
SEGMLLAGFATFLPKLIESQFSLSASLAALLVGVVVVPGGILGTFLGGLIVKKLKLKCKGILKFCIVCSI
VAFLFSFILLIYCPNAPFAGVTVPYGNSPLEGTSNLTSTCNADCHCSEDFYDPVCGSDGVTYYSPCHAGC
TTSHGDDGQKVYSNCSCIQSNSSKTSTAATGKACPCETCCQKLYLFLAVFFLLIVFTFMSSTPALSATLR
>gnl|CDD|340962 cd17404, MFS_SLCO5_OATP5, Solute carrier organic anion transporter 5 family of the Major Facilitator Superfamily of transporters. The Solute carrier organic anion transporter 5 (SLCO5) or Organic anion transporting polypeptide 5 (OATP5) family contains only one subfamily, OATP5A, which contains only one mammalian member OATP5A1 (encoded by SLCO5A1). Deletion of the SLCO5A1 gene has been implicated in the pathogenesis of Mesomelia-synostoses syndrome (MSS), a rare autosomal-dominant disorder characterized by mesomelic limb shortening, acral synostoses, and multiple congenital malformations. OATP5A1 may be a non-classical OATP which is involved in biological processes that require the reorganization of the cell shape, such as differentiation and migration. It seems to affect intracellular transport of drugs and may participate in chemoresistance of small cell lung cancer (SCLC by sequestration), rather than mediating cellular uptake. The SLCO5/OATP5 family belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
KAFLVCMCLLIFIQSALSSGYLNSVITTIEKRYSLKSSESGLIVSSYEIGSLLTVVFVSYFGGRGHRPRW
IAVGGVLIALGSFLFSLPHFFILAQILIGMGGTPIFTLGTTYLDDHVKKESSSLYLAIMYVMGALGPAAG
FLLGGLLINFYVDPLSTPPDISPGDPRWIGAWWGGFLLCGIALLLVAFPFFTFPKMTFLVVSLGYCMELA
IVSGFITFLPKYLETQFGIPASNANIFTGVIAVPGAGIGIVLGGYILKRFKLGPKGAAKLALICNFLSLL
LFLTLFFLGCESIKLAGITIPYTTGPSLSSTHGRNLTSECNVNCGCSINEYEPVCGSDGITYFSPCLAGC
TSVGNTSTGIRNYTNCACLQSRSSISPPTVGQGSQLQAGPCSRTCNTLIPFLILLFIVTLITACAQMPAL
MITLR
>gnl|CDD|340963 cd17405, MFS_SLCO6_OATP6, Solute carrier organic anion transporter 6 family of the Major Facilitator Superfamily of transporters. The Solute carrier organic anion transporter 6 (SLCO6) or Organic anion transporting polypeptide 6 (OATP6) family contains only one subfamily, OATP6A, which contains only one human member OATP6A1 (encoded by SLCO6A1). The OATP6 family is the most diverged of the OATPs. OATP6A1 is also called cancer/testis antigen 48 (CT48) or gonad-specific transporter. It is strongly expressed only in normal testis, and weakly in spleen, brain, fetal brain, and placenta. It is found in tumor samples (lung, bladder, and esophageal) and cancer cell lines (lung), and may be of potential use as a target for therapy for a variety of tumor types. The SLCO6/OATP6 family belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
IDGFMILYCILVLIQGAVFGLVDMSIGIFQVQFSLTRTEKYLLDFSYDISSFLVAIIIAHYGSRGNRTRW
IAASCFLMGLGSMLFAFPFFTFHIAGQCIQGIAGMPIYILGITFIFDNIPTSSAGIYLGIAHSAYLIGYL
LGYVGGLPNFQPPPNEKSVEIEVNKVYQLWQSGWWKTFLIAAAIAWCTSFPLVCFPTSLPGLLKNPLLLC
QAICKATEYLTFIGALEFLPHYLENQFLLTPGIASLLTGAFLIPGGAIGHFLGGLIVSRLEMSCKNKMRF
ILVTSVISLGLFVLIFFVECQTVTFAGINEDYDGYGQLGNLTAPCNEYCDCTSSLYTSICGRDEIEYFSP
CFAGCKASKVSNTEKTYYNCSCIKEGLAAADDEGDFIDAIAGKCDSKCYKLPLFFAFYFSATVFSNMCSI
PIILIILR
>gnl|CDD|340964 cd17406, MFS_unc93A_like, Protein unc-93 homolog A and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of Caenorhabditis elegans Uncoordinated protein 93 (also called putative potassium channel regulatory protein unc-93), human protein unc-93 homolog A (HmUnc-93A or UNC93A), and similar proteins. Unc-93 acts as a regulatory subunit of a multi-subunit potassium channel complex that may function in coordinating muscle contraction in C. elegans. The human UNC93A gene is located in a region of the genome that is frequently associated with ovarian cancer, however, there is no evidence that UNC93A has a tumor suppressor function. This unc93A-like subfamily belongs to the Unc-93 family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLVISFAFLLLFTAFQGLQNLQSSLNSDDGLGVVSLSVIYASLIVSCMFLPPLLIKKLGCKWTIVLSMFC
YVLYIAANFYPSWYTLIPASIILGFGAAPLWSAKCTYLTESGNRYAKLTGKSGDDVINRFFGIFFMIFQS
SQIWGNLISSLVFSQSLIYTLLGIYLGCGILAVIIVAVFLDPLKRDKEKRKQETKFSVLSLLLATFKHLK
DPRQLLLIPLTIYSGLEQAFLSGDFTKSYVTCALGIWNVGYVMICFGVVNALCSFLFGRLVKYTGRIPLF
ALGALVNLGLIIALLLWEPDPDQLAIFFVFAGLWGMADAVWQTQINALYGVLFPKNKEAAFSNYRLWESL
GFVIAFAYSNFLCVYVKLYILLAVLLLGMVGYGVVEYIER
>gnl|CDD|340965 cd17407, MFS_MFSD11, UNC93-like Major facilitator superfamily domain-containing protein 11. This group is composed of UNC93-like protein MFSD11 (also called major facilitator superfamily domain-containing protein 11 or protein ET) and similar proteins, most of which are uncharacterized. MFSD11 is ubiquitously expressed in the periphery and the central nervous system of mice, where it is expressed in excitatory and inhibitory mouse brain neurons. Its expression is affected by altered energy homeostasis, suggesting plausible involvement in the energy regulation. MFSD11 belongs to the Unc-93 family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VIILGVAFMFIFTAFQTCGNIEQTVIKSLNQGNTTFHGSGYTSLAIIYGVFAASNWIAPSVVAVIGPKWS
MVVGGLTYSLFIASFIQPMTWSLYTASVLLGIGAAVLWTGQGNFLTINSDSETIGRNSGIFWALLQCSLL
FGNLYVYFAFQGKTTISDHDRRTVFIVLTVISLVGVVLLFLLRKPPSEPKEMLLLSVTFAYTGLELTFFS
GVYGTCIGNTNKFGEDAKSLIGLSGIFIGIGEILGGGLFGILGKKTNRFGRDPIVLLGFVVHLIAFYLIF
LNIPSDAPIAEGTNDSAYIEPSAYVALFCSFLLGFGDSCFNTQIYSILGFMYPEDSAPAFALFKFVQSIA
AAIAFFYSNYLLLQWQLLILVVFGFLGTISFFLVEWK
>gnl|CDD|340966 cd17408, MFS_unc93B1, Protein unc-93 homolog B1 of the Major Facilitator Superfamily of transporters. Protein unc-93 homolog B1 (UNC93B1) controls intracellular trafficking and transport of a subset of Toll-like receptors (TLRs), including TLR3, TLR7 and TLR9, from the endoplasmic reticulum to endolysosomes where they can engage pathogen nucleotides and activate signaling cascades. It regulates differential transport of TLR7 and TLR9 into signaling endosomes to prevent autoimmunity. UNC93B1 belongs to the Unc-93 family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VVAASLGGMLTYGVYLGLLQMQLILHYDETYREVKYGNMGLQDIDSKMLMGINVTPIVALLYTPVLIRFF
GTKWMMFLAVGIYALFVSTNYWERYYTLVPSAVAIGVAIVPLWASMGNYITRMAQKYYEYVNYKEEDVQE
QKRPPRGAYHKYIIIFQSVFYAIFHLSFVCAQLPMIFFLNNYLYDYNHTLYNVKHCGAQSKGILEGFNKT
VLITLPRSLNLIIVESALMGAAFLSMLLVLLLCGAAYRPTEEIDLRSIGWGNIFQLPFKHLRDYRLRLLI
PFFIYSGFEVLFACTGFALSYGVCSLGLERLAYLLMAYGLSASLCSLLALSLLRLPRPVPLVAGAFLHLT
LLITLFFWAPTPRLTSQMPLLYVVAALWGLGSALNKTGLSTLLGILYEDKERQDFIFTIYHWWQALAIFI
VYLWSNLPMKAKLGILLATLVIALLSYLWMERKLAR
>gnl|CDD|340967 cd17409, MFS_NIMT_like, 2-nitroimidazole transporter and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of Escherichia coli 2-nitroimidazole transporter (NIMT), also called YeaN, and similar proteins. NIMT confers resistance to 2-nitroimidazole, the antibacterial and antifungal antibiotic, by mediating the active efflux of this compound. The NIMT-like subfamily belongs to the 2-nitroimidazole and cyanate transporters like (NIMT/CynX-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
IAGILLIAANLRAPFTGVAPLLDTIRESFGLSTAQAGLLTTLPLLAFALFSPLAAKLARRYGLERSLFAA
LLLIAAGIALRSTGSVWALYLGTAIIGAGIAIGNVLLPSLLKRDFPARVATLTGAYALTMGVGAALGSAL
VVPLAQVLAFGWQLALGAFLVFPLVAALIWLPQLRRHTSPAADTAKPPHGGSVWRSPLAWQVTLFLGLNS
FIYYVLVGWLPSILTDAGYSAAQAGSLHGLLQLATAVPGLLLIPVLARMKDQRLLAVLVSLLGAVGLIGL
LLAPSLAILWVILFGFGSGAGFILGLAFIGLRTSSAHQAAALSGMAQCVGYLLAATGPMLVGALHDLTGS
WSVPLLLCAALALLMAIFGLLAGR
>gnl|CDD|340968 cd17410, MFS_CynX_like, Cyanate transport protein CynX and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of Escherichia coli cyanate transport protein CynX and similar proteins. CynX is part of an active transport system that transports exogenous cyanate into E. coli cells. The gene encoding CynX is part of the cyn operon that also includes cynS, encoding cynase, which catalyzes the reaction of cyanate with bicarbonate to give ammonia and carbon dioxide, and cynT, which encodes a carbonic anhydrase. The CynX-like subfamily belongs to the 2-nitroimidazole and cyanate transporters like (NIMT/CynX-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLVIVLLGLNLRPILTSVGPLLNEIRAATGLSFQVASLLTVLPVLCMGLVALLGPWLARRVGERRGVALS
LLAIAAACLWRLWSGTGPTLIASALLGGLGIAIIQALVPGLIKRRFPARVPLAMGLYSASLMAGGGLAAS
LSPRLAQHSAGWQLGLGIWAVPALVALVLWWRQPPREVAPSDTAGPGVRFFRNRRAWLLALYFGLINAGY
TSMIAWLPAYYLELGWSAQDSGSLLGFMTIFQVLGALVMPALARRSADRRPLLMGALAAQLAGFLGLILM
PQSLPLLWVALIGLGLGACFSLGLILALDHLRKPRAAGQLAAFVQGIGFIITGISPWIAGWLRDSTGSFQ
AAWLLLAASVVAMLLLTLRFAP
>gnl|CDD|340969 cd17411, MFS_SLC15A2, Solute carrier family 15 member 2 of the Major Facilitator Superfamily of transporters. Solute carrier family 15 member 2 (SLC15A2), also called peptide transporter 2 (PepT2), is a member of the proton-coupled oligopeptide transporter (POT) family of integral membrane proteins that mediate the cellular uptake of di/tripeptides and peptide-like drugs. SLC15A2, as well as SLC15A1, mediate the proton-coupled active transport of a broad range of dipeptides and tripeptides, including zwitterionic, anionic and cationic peptides, as well as a variety of peptide-like drugs such as cefadroxil, enalapril, and valacyclovir. SLC15A2 is a high-affinity transporter and is abundantly expressed in the apical membrane of kidney proximal tubules and choroid plexus epithelial cells. It is the major transporter involved in the reclamation of peptide-bound amino acids and peptide-like drugs in the kidney, and is also called the renal isoform. In choroid plexus and the brain, it acts as an efflux transporter and plays a role in regulating peptide/neuropeptide homeostasis. SLC15A2/PepT2 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
PLSIAFIVVNEFCERFSYYGMKAVLTLYFLSFLHWDENLSTAIYHAFSGLCYFTPVLGALIADSWLGKFK
TIIYLSIVYVVGHVIKSVGAIPTVGDQQVHVVLSMIGLFLIALGTGGIKPCVAAFGGDQFEEEHARERSK
FFSIFYLSINAGSLISTFVTPILRGDVQCFGGDCYALAFGVPAALMVVALVVFIAGSGMYKEVKMVTRVL
FLYIPLPMFWALFDQQGSRWTLQATRMNDFGGGFVLQPDQMQTLNPLLILVFIPIFDLGIYPLVSKCKIN
FTSLRKMATGMILAALAFAVAAAVEIKIAWQLPQYVLLSAGEVMFSITGLEFSYSQAPASMKSVLQAGWL
LTVAFGNVIVLIVAQAAGMAQWAEFLLFAALLLAVCIIFSIMGYFYVYVDPED
>gnl|CDD|340970 cd17412, MFS_SLC15A1, Solute Carrier family 15 member 1 of the Major Facilitator Superfamily of transporters. Solute carrier family 15 member 1 (SLC15A1), also called peptide transporter 1 (PepT1), is a member of the proton-coupled oligopeptide transporter (POT) family of integral membrane proteins that mediate the cellular uptake of di/tripeptides and peptide-like drugs. SLC15A1, as well as SLC15A2, mediate the proton-coupled active transport of a broad range of dipeptides and tripeptides, including zwitterionic, anionic and cationic peptides, as well as a variety of peptide-like drugs such as cefadroxil, enalapril, and valacyclovir. SLC15A1 is primarily expressed in the brush border membranes of enterocytes of the small intestine and is also known as the intestinal isoform. It is a high-capacity/low-affinity transporter that drives the transport of di-and tripeptides for metabolic purposes. It's expression is upregulated in the colon during chronic inflammation associated with inflammatory bowel disease. SLC15A1/PepT1 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
PLSIFFIVVNEFCERFSYYGMRAVLVLYFKYFLRWDDDLSTAIYHTFVALCYLTPILGAIIADSWLGKFK
TIVYLSIVYTIGQAVMAVSAIHDLTDANRDGTPDNLTLHVALSMIGLLLIALGTGGIKPCVAAFGGDQFE
EHQEKQRSRFFSIFYLSINAGSLLSTIITPILRSQECGIHSKQKCYPLAFGVPAALMVVALIVFILGSKM
YKQIKMVLKVLFLYIPLPMFWALFDQQGSRWTLQATTMDGNFGAIQIQPDQMQTVNPILIIIMVPIFDAV
IYPLIKKCKINFTPLRKMTVGMFLAALAFVAAALLQIQMAWQIPQYFLLTCGEVVFSVTGLEFSYSQAPS
NMKSVLQAGWLLTVAVGNIIVLIVAEAGSISEQWAEYVLFAALLVAVCIIFAIMAYFYTYVDPAE
>gnl|CDD|340971 cd17413, MFS_NPF6, NRT1/PTR family (NPF), subfamily 6 of the Major Facilitator Superfamily of transporters. The plant Nitrate transporter 1/Peptide transporter (NRT1/PTR) family (NPF) is related to the POT (proton-coupled oligopeptide transporter), Peptide transporter (PepT/PTR), or Solute Carrier 15 (SLC15) family in animals. In contrast to related animal and bacterial counterparts, the plant proteins transport a wide variety of substrates including nitrate, peptides, amino acids, dicarboxylates, glucosinolates, as well as the plant hormones indole-3-acetic acid (IAA) and abscisic acid (ABA). A recent study identified eight subfamilies within this family, named NPF1-NPF8. NPF6 includes the first identified member of the NRT1/PTR family: Arabidopsis thaliana NRT1.1, now called AtNPF6.3. It is a dual affinity nitrate influx transporter and a nitrate sensor. It also transports auxin and has nitrate efflux activity. NPF6 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
WKSAALILGIEMCERLTTLGIGVNLVTYLTGTMHLPSATSANIVTNFLGTSFLLCLLGGFIADTFLGRYL
TIAIFASIQALGVLVLTLSTTLPSLRPPPCNHTTSHHCEPASGIQLTVLYLALYLIALGTGGIKSSVSGF
GSDQFDENDPKERKLMSYFFNRFFFCISVGSLLAVTVLVYIQDNVGRGWGYGICAAAMVLAIVVFLAGTK
RYRFKKSIGSTQVEEVKMVVRMLPIWATTILFWTVYAQMTTFSVEQAETMDRNIGSFEIPPASMAVFLVA
TILLTTAVYDRVIVPLCRKLTGHPQGLTTLQRIGVGLVFSCLAMAVAALVELKRLRIAHAHGKPVKTVPM
SVFWLVPQYFLVGAGEAFIYTGQLDFFIRESPKGMKSMSTGLFLSTLSLGFFVSSFLVSIVNRVTGKSHP
HGWLADNLNKGRLDYFYWLLAVLSALNFVIFLVFAKW
>gnl|CDD|340972 cd17414, MFS_NPF4, NRT1/PTR family (NPF), subfamily 4 of the Major Facilitator Superfamily of transporters. The plant Nitrate transporter/Peptide transporter (NRT1/PTR) family (NPF) is related to the POT (proton-coupled oligopeptide transporter), Peptide transporter (PepT/PTR), or Solute Carrier 15 (SLC15) family in animals. In contrast to related animal and bacterial counterparts, the plant proteins transport a wide variety of substrates including nitrate, peptides, amino acids, dicarboxylates, glucosinolates, as well as the plant hormones indole-3-acetic acid (IAA) and abscisic acid (ABA). A recent study identified eight subfamilies within this family, named NPF1-NPF8. Members of the NPF4 subfamily have been shown to transport ABA. NPF4 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
MRAAFFVLVVEALENMAYLANANNLVTYLINNMHYSLAKSANIVTNFVGTAFLLALLGGFLSDSFLSSFK
TIIIFGSIELLGLILLTVQAHIPSLQPPSCNSLGDLTCKEPSGSQAAILFVGLYLVALGVGCIKPNLPSH
GADQFDENDPKGRRQLSSFFNWYYFSFSLGALIAVTLVVWVEENKGWDWGFGVSAAVIAVGILVFVAGTP
FYRNKTQVEEVKIVLKMLPIFACTIILNCILAQLQTFSVQQGSTMNRTKIGSFNIPPASLQAIPVIFMLI
LVPLYDHLLVPFARKITGHESGITHLQRIGIGLVLSTLSMVVAALVETKRKKVAVENGLLNSKENLPISI
FWIALQFLILGISDMFTAVGLLEFFYTESPSSMRSLGTALTWCSYSFGFYLSSVLVSVVNKVTGSGGHGG
WLLGENLNRDRLDLFYWLLCVLSTINFLNYLFWARR
>gnl|CDD|340973 cd17415, MFS_NPF3, NRT1/PTR family (NPF), subfamily 3 of the Major Facilitator Superfamily of transporters. The plant Nitrate transporter/Peptide transporter (NRT1/PTR) family (NPF) is related to the POT (proton-coupled oligopeptide transporter), Peptide transporter (PepT/PTR), or Solute Carrier 15 (SLC15) family in animals. In contrast to related animal and bacterial counterparts, the plant proteins transport a wide variety of substrates including nitrate, peptides, amino acids, dicarboxylates, glucosinolates, as well as the plant hormones indole-3-acetic acid (IAA) and abscisic acid (ABA). A recent study identified eight subfamilies within this family, named NPF1-NPF8. NPF3 is the smallest NPF subfamily and it includes Cucumis sativus nitrite transporter (CsNitr1), now named CsNPF3.2. It functions as a chloroplast nitrite uptake transporter to remove toxic nitrite from the cytosol. NPF3 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
WKTMPFIFGNEICERLASVGFHTNLITYLTLQLHMPLVKAANILTNFNGTASLTPLLGAFIADSFAGRFW
TITIGSIIYQLGMVLLTISAILPSLRPPPCNGHEVCACQASSAQLSILYLSLLLTALGSGGIRPCVVAFG
ADQFDESDPKQAKQTWNFFNWYYFCMGIAILLAVTVIVYIQDNVGWGWGFGIPTIAMAISVIAFVVGSPL
YRELKSIIRMLPIWAAGILLVTASSQQHTFSIQQARTMNRHLTPSFQIPPASMSVFGILSLLTTVPLYDR
VLMPVARKFTGNERGITFLQRMGIGLFISILATVVAAFVEVKRKSVAANHGLLDRPHATVPISVFWLVPQ
YILHGIAEAFMSIGHLEFFYDQSPESMRSTATALFWSTISLGSYLSTLLVTLVHKETSRGGRWWLPNNLN
RGRLDYFYWLVAVLQAVNLVYFLICARW
>gnl|CDD|340974 cd17416, MFS_NPF1_2, NRT1/PTR family (NPF), subfamily 1 and 2 of the Major Facilitator Superfamily of transporters. The plant Nitrate transporter/Peptide transporter (NRT1/PTR) family (NPF) is related to the POT (proton-coupled oligopeptide transporter), Peptide transporter (PepT/PTR), or Solute Carrier 15 (SLC15) family in animals. In contrast to related animal and bacterial counterparts, the plant proteins transport a wide variety of substrates including nitrate, peptides, amino acids, dicarboxylates, glucosinolates, as well as the plant hormones indole-3-acetic acid (IAA) and abscisic acid (ABA). A recent study identified eight subfamilies within this family, named NPF1-NPF8. NPF1 includes Medicago truncatula LATD/NIP, now named MtNPF1.7, which is a high-affinity nitrate transporter and is involved in nodulation and root architecture. NPF2 members are well-established nitrate and glucosinolate transporters, including Arabidopsis nitrate influx and efflux transporters with varied tissue and developmental specificity. Examples are AtNPF2.7, which is expressed in the cortex of mature roots, and AtNPF2.9, which is expressed in root companion cells where it is involved in phloem loading. NPF1/2 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
MPFIIGNETGEKLASYGLLANLIVYLIEEYNMKSIAAANIINIWSGTTNFLPVVGAFLSDSYFGRFPTIS
VGSFASLLGMVLLTLTAAIPSLRPPPCETASSLCQSPSKLQLAVLYSALALLSIGAGGIRPCSLAFGADQ
FDKKTESGKRGLESFFNWYYFTFTVAQIISLTAIVYIQDNVSWKIGFGIPAALMLLSFILFLAGSRLYVV
EDLKSLIRVIPIWSTGIILSLAMAQQMSLTVLQALVMDRHLGPSFQIPAGSITVFLLITLTIFIPLYDRV
LVPLLRKITGRGRGLTLLQRVGIGIVFSILSMAVAAIVERKRRKTALTQGNGTSPMSVLWLVPQLVLMGI
AEAFHFIGQIEFFYQEFPESMRSTATSLFSLGMGVASYLSSALISAVHRTTGRGGGGSWLPDDINKGRLD
YVYWLLAGLGALNLGYFLVCSWRY
>gnl|CDD|340975 cd17417, MFS_NPF5, NRT1/PTR family (NPF), subfamily 5 of the Major Facilitator Superfamily of transporters. The plant Nitrate transporter/Peptide transporter (NRT1/PTR) family (NPF) is related to the POT (proton-coupled oligopeptide transporter), Peptide transporter (PepT/PTR), or Solute Carrier 15 (SLC15) family in animals. In contrast to related animal and bacterial counterparts, the plant proteins transport a wide variety of substrates including nitrate, peptides, amino acids, dicarboxylates, glucosinolates, as well as the plant hormones indole-3-acetic acid (IAA) and abscisic acid (ABA). A recent study identified eight subfamilies within this family, named NPF1-NPF8. NPF5 includes Arabidopsis thaliana PTR3 (AtPTR3, now named AtNPF5.2), which is a wound-induced peptide transporter that is necessary for defense against virulent bacterial pathogens. NPF5 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
WKACSFIIGIEVAERFAYYGIASNLVTYLTTPLHQSTARAAKNVNNWSGTATLLPLLGAFVADAYLGRYR
TILISSLIYLLGLVLLTLSASLPSLKPPECNGTCSKASTLQVAFFFFSLYLVAIGQGGHKPCVQAFGADQ
FDEDDPKEKKQKSSFFNWWYFSICAGSLTAVTVLVYIQDNVGWALGFGIPTIVMALALFVFLLGTPLYRY
KVEEVKLVLRLIPIWFTTLVFTVVFAQSPTFFTKQGVTMDRTIGPNFKIPPASLQSFITLSILISIPIYD
RVFVPIARKITGNPRGITLLQRIGIGMFLSILAMVIAALVEMKRLKVAKEHGLISPKATVPMSIFWLLPQ
YILLGIADVFTMVGMQEFFYDQVPDEMRSLGTALYLSVFGVGSFLSSFLISIVDKITSSSGGQSWFNNNL
NRAHLDYFYWLLAVLSAVNFVLFLFVAKSYVY
>gnl|CDD|340976 cd17418, MFS_NPF8, NRT1/PTR family (NPF), subfamily 8 of the Major Facilitator Superfamily of transporters. The plant Nitrate transporter/Peptide transporter (NRT1/PTR) family (NPF) is related to the POT (proton-coupled oligopeptide transporter), Peptide transporter (PepT/PTR), or Solute Carrier 15 (SLC15) family in animals. In contrast to related animal and bacterial counterparts, the plant proteins transport a wide variety of substrates including nitrate, peptides, amino acids, dicarboxylates, glucosinolates, as well as the plant hormones indole-3-acetic acid (IAA) and abscisic acid (ABA). A recent study identified eight subfamilies within this family, named NPF1-NPF8. NPF8 contains the Arabidopsis dipeptide transporters AtNPF8.1 (PTR1), AtNPF8.2 (PTR5), and AtNPF8.3 (PTR2), as well as tonoplast-localized transporters AtNPF8.4 (PTR4) and AtNPF8.5 (PTR6). Oryza sativa NRT1 (now called OsNPF8.9) is a low-affinity nitrate transporter. NPF8 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
WKACPFILGNECCERLAYYGIATNLITYLTKELHQGNVSAANNVTNWSGTCYITPLIGAFIADAYWGRYW
TIASFSAIYFIGMVLLTLSASVPGLKPASCIGSLCPPATSVQYAVFFLGLYLIALGTGGIKPCVSSFGAD
QFDDTDPKEKVRKSSFFNWFYFSINIGALISSSVLVWIQENVGWGWGFGIPTVFMGIAIVSFFFGTPLYR
EVKILIRLLPIWASGIVFATVYSQMSTMFVQQGRTMDRMGGNFEIPPASLSLFDTLSVLIWVPIYDRFIV
PLVRKFTGHERGFTQLQRMGIGLFISVLSMVAAAIVEIVRLQLARTHNLVESGPPVPMSIFWQIPQYFLI
GAAEVFTFIGQLEFFYDQSPDAMRSLCSALSLLTTALGNYLSSLIVTLVTYVTTKGGKPGWIPDNLNNGH
LDYFFWLLASLSFLNILVYLWIAKRYT
>gnl|CDD|340977 cd17419, MFS_NPF7, NRT1/PTR family (NPF), subfamily 7 of the Major Facilitator Superfamily of transporters. The plant Nitrate transporter/Peptide transporter (NRT1/PTR) family (NPF) is related to the POT (proton-coupled oligopeptide transporter), Peptide transporter (PepT/PTR), or Solute Carrier 15 (SLC15) family in animals. In contrast to related animal and bacterial counterparts, the plant proteins transport a wide variety of substrates including nitrate, peptides, amino acids, dicarboxylates, glucosinolates, as well as the plant hormones indole-3-acetic acid (IAA) and abscisic acid (ABA). A recent study identified eight subfamilies within this family, named NPF1-NPF8. NPF7 includes the nitrate transporters AtNPF7.2 and AtNPF7.3, as well as the dipeptide transporter OsNPF7.3. AtNPF7.3 is a bidirectional transporter involved in nitrate influx and efflux. NPF7 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
WKSAIFILVNQGLATLAYFGVGVNLVLYLTRVMHQSNASAANNVSNWTGTVYITPLIGAFLSDSYWGRYW
TSTLFQAIFVIGLLLLTLSSALPSLRPPQCGDGDLKCPPASAAQTTFLYFSLYLIALGYGGYQPCIATLG
ADQFDDEDPIEKASKSAFFSYFYQALNLGSLFSNTILVYFEDNGSWGLGFGISAGAAFIGLVLFLAGTPF
YREVKCILRLLPIWLSTIIYSVVYTQMATLFVEQGAAMDTSFGNFKIPPASMSVFEILSVAVGTVLYRKF
LVPLLRKVTGHPKGITELQRMGIGLVIGILAMVVAALVEIQRLKVARPSNLDDPTSPSPLSIFWQIPQYV
LVGASEVFTYVGQLEFFYDQAPDGLRSLGSALCMASVALGNYLSSLLVTIVNKVTTKDGSPGWIPDNLNK
GHLDRFYWLLAALSGIDFVVFLICAKW
>gnl|CDD|340978 cd17420, MFS_MCT8_10, Monocarboxylate transporters 8 and 10, and similar proteins of the Major Facilitator Superfamily of transporters. Monocarboxylate transporters 8 (MCT8) and 10 (MCT10) are transporters which stimulate the cellular uptake of thyroid hormones such as thyroxine (T4), triiodothyronine (T3), reverse triiodothyronine (rT3) and diidothyronine (T2). MCT has a preference for T3 and is also a sodium-independent transporter that mediates the uptake or efflux of aromatic acids such as Phe, Tyr, and Trp, as well as L-3,4-di-hydroxy-phenylalanine. MCT8/10 and similar proteins belong to the Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWLVMVAAFWCNGSIFGIINTYGVLHSLLLERLTKLGDPEASFKAAWVGALAMGMIFFCSPIVSCFTDKI
GCRLTAFAGAAVSFGGLLLSSFCSSIGALYFTYGIMFGCGCSFAYQPSLVILGHYFKRRLGLVNGFVTAG
SSVFTVILPPLLRKLLDSYGLEGTLRVLSLFMFVLILCSFTYRPLHPSPEDPKSKPGRRTLHSRINLFLR
KIFNVEIFKRKRYVIWALGIPLALFGYFVPYVHLMKFVKEEFFPGKDVNVPLMCIGITSGIGRLIFGVIA
DMPPGVKKMYLQVLSFVSIGLMSMMIPLCNSFGILISVCLVMGLFDGCFISIMAPIAFELVGPSGASQAI
GFLLGLMSIPMTVGPPIAGLLRDSTGSYTVAFYLAGVPPLIGSSLLFFIP
>gnl|CDD|340979 cd17421, MFS_MCT5, Monocarboxylate transporter 5 of the Major Facilitator Superfamily of transporters. Monocarboxylate transporter 5 (MCT5) is also called Solute carrier family 16 member 4 (SLC16A4). It is an orphan transporter expressed in the brain, muscle, liver, kidney, lung, ovary, placenta, and heart. It is a member of the monocarboxylate transporter (MCT) family, whose members include MCT1-4, which are proton-coupled transporters that facilitate the transport across the plasma membrane of monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and ketone bodies such as acetoacetate, beta-hydroxybutyrate and acetate. MCT5 belongs to the Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWMIVLHFFLVNVLVMGTLKTFGIFFVAFQEEFGGSSEQISWIGSIMSSLRLSAGPLASVACGRLGERWT
SILGAFLVSAGFLISIFATSVPFLYVSMGLLVGLGFAFLYQAAAVMTAKYFKKRLATAYAIARSGMGLTF
ALAPFTQLLLDEYDWQGALLIFGGIMLNLVASGMLLRPIDFSLLKDPFFCIYTWSFVFSQLAYFIPYFHL
VARARTLGIDPMDASFIISVAGITETVAQLASGWIADQNWIKKYHYHKAYLILCGVTNLLAPLATTYPLL
MTYAVFFAIFCGGYLALLLPVLVDLVGVTKVNSSLGFSMFFAGIGCLTGPPLAGWLYDYTQTYDCSFYLA
GGCYLLSSVSFFLEPLARR
>gnl|CDD|340980 cd17422, MFS_MCT7, Monocarboxylate transporter 7 of the Major Facilitator Superfamily of transporters. Monocarboxylate transporter 7 (MCT7) is also called Solute carrier family 16 member 6 (SLC16A6). Zebrafish MCT7 is required for hepatocyte secretion of ketone bodies during fasting; it has been shown to be a selective transporter of the major ketone body beta-hydroxybutyrate, whose abundance is increased during fasting. MCT7 is expressed in the brain, pancreas, muscle, and prostate. It belongs to the Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWAVAVAFFFVEVFTYGVIKSFGVFFNDLMSYFNETNSRVSWIISICVFVMTFTAPLSTVLSNRFGHRPV
VMVGGLLISLGMITASFASSIVEMYLTIGIISGLGYCFTFLPTVTILSQYFKKRRSLVTAIASTGECFAV
FAFAPAFTALKESIGWRYCLLVVGALQLNIVVCGALLRVLKEPGFICYALFGLFATLGFFAPQLYIIPLS
LSLGIDQDWAAYMLSAMAIAELFGRISAGWVLNKCPIRKIYIELICVILLCVVLLLFPFAYGFWSLLVCS
IFYGFMFGTVAGTHIPLLAEDDVVGIEKMSSALGVYVFIQSIAGLAGPPLGGVLVDWTQNYGSAFYSCAA
GMALGAVFLALVR
>gnl|CDD|340981 cd17423, MFS_MCT11_13, Monocarboxylate transporters 11 and 13 of the Major Facilitator Superfamily of transporters. Monocarboxylate transporters 11 (MCT11) and 13 (MCT13) are also called Solute carrier family 16 members 11 (SLC16A11) and 13 (SLC16A13), respectively. They are orphan transporters whose substrates are yet to be determined. MCT11 is expressed in skin, lung, ovary, breast, lung, pancreas, retinal pigment epithelium, and choroid plexus. Genetic variants in SLC16A11, the gene encoding MCT11, are associated with type 2 diabetes in Mexican and other Latin American populations. MCT13 is expressed in breast and bone marrow stem cells. MCT11/13 belongs to the Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWVVVLAAFLQNALVFGVLRSFGVFFVEFVEYFEESAQRVSWITSIGLAVQQLASPVGSALSTRYGARPV
VMLGGLLSSLGFLLASFATSLLHLYLCIGLLSGLGWALVFAPTMATVSRYFSRRRSLATGLALTGVGLSS
FALSPLFQLLLDTYAWRGALLLLSALSLHLVPCGALLRPLALPGDPPAPPRSLSAAFGLSLLTHRAFLRY
ALATTLINTGYFIPYVHLVAHARALGLGEYQAAFVVSVAAVADAVGRLFSGWLADLGPLRLLHLLVLWTA
LTGLSLLLLPLAKVYGSLLALAVAYGFCAGALAPLVFSVLPELVGVERVLNATGLLQMIESVGGLLGPPL
SGWLRDITGDYTASFLVAGSFLLLGSLILLTLP
>gnl|CDD|340982 cd17424, MFS_MCT12, Monocarboxylate transporter 12 of the of the Major Facilitator Superfamily of transporters. Monocarboxylate transporter 12 (MCT12) is also called Solute carrier family 16 member 12 (SLC16A12). It is a creatine transporter encoded by the cataract and glucosuria associated gene SLC16A12. A heterozygous mutation of the gene causes a syndrome with juvenile cataracts, microcornea, and glucosuria. MCT12 may function in a basolateral exit pathway for creatine in the proximal tubule. It belongs to the Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWMIVAGCFLVTVCTRAVTRCISIFFVEFQNYFAQDYARTAWIHSIVDCTTMLCAPLGSLISNHLSCQVG
IILGGLLASTGLILSSFATSLEYLYLTLGVLTGLGFALCYSPAIAMVGKYFHKRKALAYGIAMSGSGIGT
FILAPVVQLLIEQFSWRGALLILGGFVLNLCVCGALMRFLLMPDFLVLAVSVLFLAYGCSPPFVYLVPYA
LSVGVSHQQAAFLMSILGVIDIIGNITFGWLTDRRCLKKYRYFCYLFAVGMDGLCCLFLPILKTFPLLVP
FSFTFGYFDGAYVALIPVVTSDVVGTSSLSSALGVVYFLHAVPYLVSPPIAGWLVDTTGTYTAAFLLSGF
SMIFSSLLLGSAR
>gnl|CDD|340983 cd17425, MFS_MCT6, Monocarboxylate transporter 6 of the Major Facilitator Superfamily of transporters. Monocarboxylate transporter 6 (MCT6) is also called Solute carrier family 16 member 5 (SLC16A5). MCT6 has been shown to transport bumetanide, nateglinide, probenecid, and prostaglandin F2a, but not L-lactic acid, in a pH- and membrane potential-dependent manner. It may be involved in the disposition and absorption of various drugs. MCT6 is expressed in the kidney, muscle, brain, heart, pancreas, prostate, lung, and placenta. It belongs to the Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
AWVVLLATMIVQGLTLGFPSCIGIFFTDLQKEFQASNSETSWFPSIMTAVLHAGGPLCSILVERFGCRVT
VMLGGLLSGVGMVASSFSHSIVQLYFTAGFITGLGFCFSFQSSVTVLGFYFVRRRALANALASTGTSIGL
TLWPLLSQYLLEEMGWRGSFLVFGGVLLNCCVCGAVMRPFCSNTRYQIYTLGVTWMVLGFVLPLIYLVPY
ATSNGMDESKAALLLSILGFINIFMRPLAGLLSGLPVFKGRRIYLFSLALLLNGLSNLICAISASFPVLL
VYCLLYSISMSGIGSLIFQVLMDTVEMDRFPSALGLFTILESVTILIGPPLAGLLVDITQQYSYVFYASS
IFVVSAALFMGLSF
>gnl|CDD|340984 cd17426, MFS_MCT1, Monocarboxylate transporter 1 of the Major Facilitator Superfamily of transporters. Monocarboxylate transporter 1 (MCT1) is also called Solute carrier family 16 member 1 (SLC16A1). It is a proton-coupled transporter that facilitates the transport across the plasma membrane of monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and ketone bodies such as acetoacetate, beta-hydroxybutyrate and acetate. It is widely expressed in many tissues its main function is to transport lactate into the cell. MCT1 deficiency has been identified as a cause of profound ketoacidosis, a potentially lethal condition caused by the imbalance between hepatic production and extrahepatic utilization of ketone bodies. This suggests that MCT1-mediated ketone-body transport is crucial in maintaining acid-base balance. MCT1 belongs to the Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWAVVLGAFISIGFSYAFPKSITVFFKEIEVIFNATSSEVSWISSIMLAVMYAGGPISSILVNKYGSRPI
MIAGGCLSGAGLIAASFCNTVEGLYFCVGVVGGLGLAFNLNPALTMIGKYFYKKRPLANGLAMAGSPVFL
STLAPLNQWFFDIFGWRGSFLILGGLLLNCCVAGSLMRPIGPKPFLDLTLFTHRGFLLYLSGNVIMFFGL
FAPLVFLSNYAKSKQISNESAAFLLSILAFVDMVARPSMGIVANTKWVRPRIQYFFAASVLYNGVCHLLA
PLSTSYVGFCIYAIFFGFAFGWLSSVLFETLMDLVGAQRFSSAVGLVTIVECCPVLLGPPLLGRLNDIYG
DYKYTYWACGIVLIISSIYLFIGM
>gnl|CDD|340985 cd17427, MFS_MCT2, Monocarboxylate transporter 2 of the Major Facilitator Superfamily of transporters. Monocarboxylate transporter 2 (MCT2) is also called Solute carrier family 16 member 7 (SLC16A7). It is a proton-coupled transporter that facilitates the transport across the plasma membrane of monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and ketone bodies such as acetoacetate, beta-hydroxybutyrate and acetate. It transports pyruvate and lactate outside and inside of sperm and plays roles in the regulation of spermatogenesis. Genetic variation in MCT2 has functional and clinical relevance with male infertility. MCT2 is consistently overexpressed in prostate cancer (PCa) cells and its location at peroxisomes is associated with malignant transformation. MCT2 belongs to the Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWAVVFGAFISIGFSYAFPKAITVFFKEIQEIFHTSYSEIAWISSIMLAVMYAGGPISSILVNKYGSRPV
VIAGGLLCSLGMISASFCNSVMQLYLCIGVIGGLGLAFNLQPALTIIGKYFYKKRPIANGLAMAGSPVFL
STLAPLNQFLFNQFGWRGSFLILGGLLLNCCVAGSLMRPLGPLFKHRGFLIYLSGNVIMFLGFFAPIVFL
APYAKHMGIDEYSAAFLLSILAFVDMFARPSMGLVANSKWIRPRIQYFFSFAVMYNGVCHLLCPLAEDYT
GLVIYAVFFGFAFGMVSSVLFETLMDLVGAQRFSSAVGLVTIVECCPVLIGPPLGGKLVDVTGNYKYMYF
VCGAIVIVASIWLFIGN
>gnl|CDD|340986 cd17428, MFS_MCT9, Monocarboxylate transporter 9 of the Major Facilitator Superfamily of transporters. Monocarboxylate transporter 9 (MCT9) is also called Solute carrier family 16 member 9 (SLC16A9). It is an orphan transporter that is expressed in a number of tissues including intestine and kidney. A missense variant of MCT9 (K258T) is associated with significant increase in susceptibility to renal overload (ROL) gout with intestinal urate underexcretion. This suggests that MCT9 may have a role in intestinal urate excretion; it is possible that it transports urate. MCT9 belongs to the Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWVIVFVSFLAQFLCYGSPLAVGVLYPEWLDAFGEGKGMTAWVGSLASGVGLIASPVCSACVSSFGARPV
TIFSGFMVAGGLMLSAFAPNIYFLIFSYGIVVGLGCGLVYAATVTITCQYFDKRRGLALGLISTGSSVGL
FIYAALQRELIELYGLDGCLLIVGALALNLLACGSLMRLFKNRVFSALFIAILLFDIGAFPPSLLMEDVA
RSENIIEEIALIPLVSIIGITTAIGKLILGVLADFKWVNSLYLYVLTLIGMGAALLAIPFAKSYLTLAVL
SAILGFLSGNWSIFPYVTTKTVGIEKLGHAYGILMFFAGLGNSLGPPIVGWFYDWTQTYDIAFYFSGFCV
LLGGFLLLLAA
>gnl|CDD|340987 cd17429, MFS_MCT14, Monocarboxylate transporter 14 of the Major Facilitator Superfamily of transporters. Monocarboxylate transporter 14 (MCT14) is also called Solute carrier family 16 member 14 (SLC16A14). It is an orphan transporter expressed in the brain, heart, muscle, ovary, prostate, breast, lung, pancreas, liver, spleen, and thymus. It may function as a neuronal aromatic-amino-acid transporter. MCT14 belongs to the Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
AWMVVLSSFIVHILVMGSQMALGILNMEWLEEFQQSRGLTAWISSLSMGITLIVGPFIGLFINTCGCRKT
AIIGGILTSLGWVLSAYATNVHYLFISFGVTAGIGSGMAYLPAVVMVGQYFQKRRALAQGLSTTGTGFGT
FLMTILLKYLCAEFGWRNAMFIQGAVSLNLCVCGALMRLFTNKVFVAFIFWALFAYCSFVIPFIHLPEIV
KLYGLSEQNDKFPLTSIIAIVHIFGKVILGIICDLPCISVWNVFILANFTLGVCILILPLMHTYTGLAIV
CALIGFSSGYFSLMPVVTEDLVGIKNLANAYGIIICANGISALLGPPFAGWIYDITQKYDFSFYVCGLLY
MVGIICLLLKP
>gnl|CDD|340988 cd17430, MFS_MCT3_4, Monocarboxylate transporters 9 and 14, and similar proteins of the Major Facilitator Superfamily of transporters. Monocarboxylate transporters 3 (MCT3) and 4 (MCT4) are also called Solute carrier family 16 members 8 (SLC16A8) and 3 (SLC16A3), respectively. They are proton-coupled transporters that facilitate the transport across the plasma membrane of monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and ketone bodies such as acetoacetate, beta-hydroxybutyrate and acetate. MCT3 is preferentially expressed in the basolateral membrane of the retinal pigment epithelium and plays a role in pH and ion homeostasis of the outer retina by facilitating the transport of lactate and H(+) out of the retina. Mice deficient with MCT3 display altered visual function. MCT4 is highly expressed in tissues dependent on glycolysis, and it plays an important role in lactate efflux from cells. MCT4 is expressed in neurons and astrocytes; it has been found to play a role in neuroprotective mechanism of ischemic preconditioning in animals (in the gerbil) with transient cerebral ischemia. Increased MCT4 expression has also been correlated with worse prognosis across many cancer types. MCT3/4 belongs to the Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWAVLFGCFVITGFSYAFPKAVSVFFKELMREFGVGYSDTAWISSILLAMLYGTGPLCSILVNRFGCRPV
MLVGGLLASLGMILASFCTSIIQLYLTAGVITGLGLALNFQPSLIMLGRYFDKRRPLANGLAAAGSPVFL
SALSPLGQILLEEYGWRGGFLILGGLLLNCCTCGAVMRPLDFSVFRDRGFVIYTIAKFIMVLGLFVPPIF
VVNYAKDIGVPDTEAAFLLSILGFIDIFARPACGVVAGLKWVRPRVVYLFSFAMLFNGLTDLCSATAADY
GGLVVFCVFFGISYGMVGALQFEVLMAIVGTQKFSSAIGLVLLVEAVAVLIGPPSAGRLVDATKNYELIF
YLAGSEVVLSALFLALGN
>gnl|CDD|340989 cd17431, MFS_GLUT_Class1, Class 1 Glucose transporters (GLUTs) of the Major Facilitator Superfamily. GLUTs, also called Solute carrier family 2, facilitated glucose transporters (SLC2A), are a family of proteins that facilitate the transport of hexoses such as glucose and fructose. There are fourteen GLUTs found in humans; they display different substrate specificities and tissue expression. They have been categorized into three classes based on sequence similarity: Class 1 (GLUTs 1-4, 14); Class 2 (GLUTs 5, 7, 9, and 11); and Class 3 (GLUTs 6, 8, 10, 12, and HMIT). GLUTs 1-4 are well-established as glucose and/or fructose transporters in various tissues and cell types. GLUT1, also called solute carrier family 2, facilitated glucose transporter member 1 (SLC2A1), displays broad substrate specificity and can transport a wide range of pentoses and hexoses including glucose, galactose, mannose, and glucosamine. It is found in the brain, erythrocytes, and in many fetal tissues. GLUT2 (or SLC2A2) is found in the liver, islet of Langerhans, intestine, and kidney, and is the isoform that likely mediates the bidirectional transfer of glucose across the plasma membrane of hepatocytes and is responsible for uptake of glucose by beta cells. GLUT3 (or SLC2A3) is found in the brain and can mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and dehydroascorbate. GLUT4 (or SLC2A4) is an insulin-regulated facilitative glucose transporter found in adipose tissues, and in skeletal and cardiac muscle. GLUT14 (or SLC2A14) is an orphan transporter expressed mainly in the testis. GLUT proteins are comprised of about 500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 transmembrane segments. They belong to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
FAVFVAVLGSLQFGYNTGVINAPQKVIEEFYNKTLGDRYGEPISPETLTTLWSLSVAIFSVGGMIGSFSV
GLFVNRFGRRNSMLYNNLLAFAGAALMGLSKLAKSYEMLILGRFIIGLYCGLTTGLVPMYIGEISPTALR
GALGTLHQLGIVVGILISQIFGLEFILGTEELWPLLLGFTIVPAILQLALLPFCPESPRYLLINRNEEEE
AKSVLKKLRGTTDVSEDIQEMKEESRQMMREKKVTILELFRSSSYRQPIIIAIVLQLSQQLSGINAVFYY
STSIFEKAGVQQPVYATIGAGVVNTIFTVVSLFLVERAGRRTLHLIGLGGMAICAILMTIALLLLEGYPW
MSYVSIVAIFGFVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGFSNWTSNFIVGMCFQYIANLCGPYV
FIIFTVFLLTFFIFTYFKVPETKGK
>gnl|CDD|340990 cd17432, MFS_GLUT_Class2, Class 2 Glucose transporters (GLUTs) of the Major Facilitator Superfamily. GLUTs, also called Solute carrier family 2, facilitated glucose transporters (SLC2A), are a family of proteins that facilitate the transport of hexoses such as glucose and fructose. There are fourteen GLUTs found in humans; they display different substrate specificities and tissue expression. They have been categorized into three classes based on sequence similarity: Class 1 (GLUTs 1-4, 14); Class 2 (GLUTs 5, 7, 9, and 11); and Class 3 (GLUTs 6, 8, 10, 12, and HMIT). GLUT5, also called Solute carrier family 2, facilitated glucose transporter member 5 (SLC2A5), is a well-established fructose transporter found in the small intestine. GLUT7 (or SLC2A7) is a high-affinity glucose and fructose transporter expressed in the small intestine and colon. GLUT9 (or SLC2A9) transports urate and fructose, and is most strongly expressed in the basolateral membranes of proximal renal tubular cells, liver and placenta. It may play a role in urate reabsorption by proximal tubules. GLUT11 (or SLC2A11) is a facilitative glucose transporter expressed in heart and skeletal muscle. GLUT proteins are comprised of about 500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 transmembrane segments. They belong to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
ATLAAAFGSSFQYGYNLSVVNSPTPYIQNFYNETWTERYGTPLEESTLTLLWSLTVSIFPLGGLFGSLLV
GPLVIRLGRKGTLLLNNIFAIVAAILMGLSKIAKSFEMIIVGRFLVGINAGISLNVVPMYLGESAPKNLR
GAVGLVPAIFITLGILLGQVLGLRELLGNEEGWPLLLALTGVPALLQLLTLPFFPESPRYLLIEKGDEEA
ARKALQRLRGKEDVDDEMEEMLEEQRAEKGVGTVSVLELFRDRSVRWQLISIIVLMAGQQLCGINAIYFY
ADSIFLEAGIPEDKIQYVTVGTGACEVLATITCVLVIERLGRRPLLIGGFGLMAVWCAVLTVALSLQNTV
SWMPYLSIVCIFAYIASFGIGPAGVPFILTTEIFDQSSRPAAFMVAGSLNWLSNFLVGLLFPFIQEGLGA
YCFLVFAVICLLTAIYIFFVLPETKGKTFLEI
>gnl|CDD|340991 cd17433, MFS_GLUT8_Class3, Glucose transporter type 8, a Class 3 GLUT, of the Major Facilitator Superfamily of transporters. Glucose transporter type 8 (GLUT8) is also called Solute carrier family 2, facilitated glucose transporter member 8 (SLC2A8) or glucose transporter type X1 (GLUTX1). It is classified as a Class 3 GLUT protein and is an insulin-regulated facilitative glucose transporter predominantly expressed in testis and brain. It can also transport fructose and galactose. SLC2A8 knockout mice were viable, developed normally, and display only a very mild phenotype, including mild alterations in the brain (increased proliferation of hippocampal neurons), heart (impaired transmission of electrical wave through the atrium), and sperm cells (reduced number of motile sperm cells). GLUT proteins are comprised of about 500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 transmembrane segments. They belong to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
FLATFAAVLGPLSFGFVLGYSSPAIPSLQRIADPALRLDDAAASWFGSVVTLGAAAGGVLGGWIVDRAGR
KLSLMLCSVPFIAGFTVITAAQNVWMLYVGRLLTGLASGVTSLVVPVYISEIAHPRVRGTLGSCVQLMVV
IGIMGAYLAGLVLDWRWLAVLGSIPPTLMLLLMCFMPETPRFLLTQHRRQEAMAALRFLRGPDQGWEWEC
IGIEQSFHLEEQSFSLALLKQPGIYKPLIIGVSLMAFQQLTGINAVMFYAETIFEEAKFKDSSVASVIVA
AIQVLFTAVAALIMDRAGRKVLLVLSGVVMVFSTAAFGWLAVGSMGFFIAGFAVGWGPIPWLVMSEIFPL
HVRGVASGICVLTNWLMAFLVTKEFSSLMEVLSSYGTFWLFSAFCAFSVLFTLFCVPETKGKTLEQ
>gnl|CDD|340992 cd17434, MFS_GLUT6_Class3, Glucose transporter type 6, a Class 3 GLUT, of the Major Facilitator Superfamily of transporters. Glucose transporter type 6 (GLUT6) is also called Solute carrier family 2, facilitated glucose transporter member 6 (SLC2A6). It is classified as a Class 3 GLUT protein, and is a facilitative glucose transporter that binds cytochalasin B with low affinity. It is found in the brain, spleen, and leucocytes. GLUT6 may function in oxalate secretion. SLC2A6 has been identified as an oxalate nephrolithiasis gene in mice; its deletion causes spontaneous calcium oxalate nephrolithiasis in the setting of hyperoxalaemia, hyperoxaluria, and nephrocalcinosis. GLUT proteins are comprised of about 500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 transmembrane segments. They belong to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
FLAVFSAVLGNFSFGYALVYTSPVIPALEQGDDPRLHLNVHQISWFGSVFTLGAAAGGLSAMFLNDRLGR
KLSIMFSAVPSALGYLLMGSAQGIWMLLLGRFLTGFAGGITAASIPVYVSEISHPGVRGALGACPQIMAV
FGSLALYALGLLLPWRWLAVAGEVPVVIMILLLCFMPNSPRFLISKGKDEKALKALAWLRGPNTDYMTEF
EQIKDNIRKQSSRLSWAELKTPSYYKPILIAVVMRFLQQLTGITPILVYLEPIFHLTAVILEPKYDAALV
GAVRLLSVAIAASLMDKAGRKILLFTSAFLMFAANLSMGLIPLIAAMLFIMGYAMGWGPITWLLMSEILP
LKARGVASGLCVVVSWITAFVLTQLFLPVVVTFGLQVPFLFFAAVCAVSIIFTACCVPETKGRTLEQ
>gnl|CDD|340993 cd17435, MFS_GLUT12_Class3, Glucose transporter type 12 (GLUT12), a Class 3 GLUT, of the Major Facilitator Superfamily of transporters. Glucose transporter type 12 (GLUT12) is also called Solute carrier family 2, facilitated glucose transporter member 12 (SLC2A12). It is a facilitative glucose transporter, classified as a Class 3 GLUT, and is expressed in the heart, skeletal muscle, prostate, and small intestine, and is highly upregulated in breast ductal cell carcinoma. It plays a role as a secondary insulin-sensitive glucose transporter in insulin-dependent tissues. The GLUT12 subfamily belongs to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LSSVTAAVSGLLVGYELGIISGALLQLRTLLALSCHEQEMVVSSLLIGALLASLTGGVLIDRYGRRTAII
LTSCLLVLGSLLLVCSVSYTVLIVGRIAIGVSISLSSIATCVYIAEIAPQHRRGLLVSLNELMIVIGILL
AYISNYAFANVSNGWKYMFGLVIPLAALQAIAMYFLPPSPRFLVMKDNMRARLLIGLTLVFFVQITGQPN
ILFYASTVLKSVGFQSNEAASLASTGVGVVKVVSTIPAIFLVDKVGSKTFLCIGSSVMAVSLVTMGLWLS
LASLLVYVAAFSIGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGINLLISLTFLTVTELIGLPWVCFIY
TAMSLASLVFVIMFVPETKGCSLEQI
>gnl|CDD|340994 cd17436, MFS_GLUT10_Class3, Glucose transporter type 10 (GLUT10), a Class 3 GLUT, of the Major Facilitator Superfamily of transporters. Glucose transporter type 10 (GLUT10) is also called Solute carrier family 2, facilitated glucose transporter member 10 (SLC2A10). It is classified as a Class 3 GLUT and is a facilitative glucose transporter that exhibits a wide tissue distribution. It is expressed in pancreas, placenta, heart, lung, liver, brain, fat, muscle, and kidney. GLUT10 facilitates the transport of dehydroascorbic acid (DHA), the oxidized form of vitamin C, into mitochondria, and also increases cellular uptake of DHA, which in turn protects cells against oxidative stress. Loss-of-function mutations in SLC2A10 cause arterial tortuosity syndrome (ATS), an autosomal recessive connective tissue disorder characterized by twisting and lengthening of the major arteries, hypermobility of the joints, and laxity of skin. The GLUT10 subfamily belongs to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LTATVSLLGGLTFGYELGIISGALLQLQTDFSLSCFEQEALVSALLIGALLASLIGGFLIDRHGRRTSIL
GSNLVLLAGSLILTLAGSFFWLVIGRAVVGFAISVSSMACCIYVSEMVTPHQRGLLVSLYEAGITVGILI
SYALNYFFSNVLTGWRYMFGLAIIPAAIQFASILLLPKKPEVLNIKDNMRRRTLVGLGLVLFQQFTGQPN
VLCYASTIFRSVGFQSNSSAVLASVGLGVVKVIATLLAMLFADRAGRRSLLIAGCSVMAVSVSGIGLWIT
LLCLMAFVSAFSIGFGPMTWLVLSEIYPADIRGRAFSFCNSFNWAANLLITLSFLDLIDVIGLSWTFLLY
GVVGVAGVVFIYLFVPETKGQSLEEI
>gnl|CDD|340995 cd17437, MFS_PLT, Plant Polyol transporter family of the Major Facilitator Superfamily of transporters. The plant Polyol transporter (PLT) subfamily includes PLT1-6 from Arabidopsis thaliana and similar transporters. The best characterized member of the group is Polyol transporter 5, also called Sugar-proton symporter PLT5, which mediates the H+-symport of numerous substrates including linear polyols (such as sorbitol, xylitol, erythritol or glycerol), cyclic polyol myo-inositol, and different hexoses, pentoses (including ribose), tetroses, and sugar alcohols. It functions to transport a wide range of substrates into specific sink tissues in the plant. The PLT subfamily belongs to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LASLNSILLGYDIGVMSGAVIFIKEDLKISDVQEEVLIGSLNIISLVGSLAAGRTSDWIGRRYTIALAAL
IFFVGALLMGVAPNYPVLMVGRFVAGIGVGFALMIAPVYTAEVAPASSRGFLTSFPEIFINIGILLGYVS
NYAFSGLPLHVGWRLMLGVGAVPSLFLAIGVLAMPESPRWTPAVRRMLIAALGIHFFQQASGIDAVVLYS
PRIFKKAGIKSKDKLLLATVAVGVTKTLFILVATFLLDKVGRRPLLLTSTGGMTLSLTALATSLTFIDRN
GGGLTWALVLAITAVCSFVAFFSIGAGPITWVYSSEIFPLRLRAQGASLGVVVNRLMSGTVSMTFLSMSK
AITTGGTFFLFAGVAAAAWVFFYFFLPETKGKSLEEI
>gnl|CDD|340996 cd17438, MFS_SV2B, Synaptic vesicle glycoprotein 2B of the Major Facilitator Superfamily of transporters. Synaptic vesicle glycoprotein 2 (SV2) is a transporter-like integral membrane glycoprotein, with 12 transmembrane regions, expressed in vertebrates and is localized to synaptic and endocrine secretory vesicles. Three isoforms have been identified, SV2A, SV2B, and SV2C. SV2A and SV2B are widely expressed in the brain, while SV2C is more restricted to evolutionarily older brain. SV2 isoforms have been shown to be critical for the proper function of the central nervous system. SV2 serves as the receptor for botulinum neurotoxin A (BoNT/A), one of seven neurotoxins produced by the bacterium Clostridium botulinum. BoNT/A blocks neurotransmitter release by cleaving synaptosome-associated protein of 25 kD (SNAP-25) within presynaptic nerve terminals. SV2B is a key modulator of amyloid toxicity at the synaptic site and also has an essential role in the formation and maintenance of the glomerular capillary wall. SV2B belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
FFVLGLALMADGVEVFVVGFVLPSAEKDMCLSSSNKGMLGLIVYLGMMAGAFIWGGLADKLGRKRCLIIS
LAINASFAFLSSFVQGYGAFLFCRLISGFGIGGSLPIVFAYFSEFLAREKRGEHLSWLCMFWMIGGLYAS
AMAWSIIPHYGWGFSMGTNYHFHSWRVFVIICALPCIASIIALKFMPESPRFLLEMGKHDEAWMILKNIH
DTNMRAKGTPEKVFTVSNIKRKNTLFLAVVWFTMAFSYYGLTVWFPDMIRYLQKHVTFEDSLFDECYFED
VTSTDTYFKNCTIESTIFYNTDLYEHKFIDCRFINSTFLEQKEGCHMDFEEDNDFLIYLVSFLGSLSVLP
GNIISALLMDKIGRIKMIGGSMLISAVCCFFLFFGNSESAMIGWQCLFCGTSIAAWNALDVITVELYPTN
KRATAFGILNGLCKFAAILGNSIFASFVGITKVIPILLASTALVGGGLISLRLPETR
>gnl|CDD|340997 cd17439, MFS_SV2A, Synaptic vesicle glycoprotein 2A of the Major Facilitator Superfamily of transporters. Synaptic vesicle glycoprotein 2 (SV2) is a transporter-like integral membrane glycoprotein, with 12 transmembrane regions, expressed in vertebrates and is localized to synaptic and endocrine secretory vesicles. Three isoforms have been identified, SV2A, SV2B, and SV2C. SV2A and SV2B are widely expressed in the brain, while SV2C is more restricted to evolutionarily older brain. SV2 isoforms have been shown to be critical for the proper function of the central nervous system. SV2 serves as the receptor for botulinum neurotoxin A (BoNT/A), one of seven neurotoxins produced by the bacterium Clostridium botulinum. BoNT/A blocks neurotransmitter release by cleaving synaptosome-associated protein of 25 kD (SNAP-25) within presynaptic nerve terminals. It is unclear how SV2A is involved in correct SV function, but it has been suggested to either act as a transporter or a regulator of exocytosis by mediating Ca2+ dynamics. SV2A has been identified as the molecular target of the antiepileptic drug levetiracetam (LEV). Its expression is decreased in patients with epilepsy and in epileptic animal models. SV2A belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
YFVLGLALMADGVEVFVVGFVLPSAEKDMCLSDSNKGMLGLIVYLGMMVGAFLWGGLADRIGRRQCLLIS
LSVNSVFAFFSSFVQGYGTFLFCRLLSGVGIGGSIPIVFSYFSEFLAQEKRGEHLSWLCMFWMIGGIYAS
AMAWAIIPHYGWSFQMGSAYQFHSWRVFVLVCAFPSVFAIGALTTMPESPRFFLENGKHDEAWMVLKQVH
DTNMRAKGHPERVFSVTHIKRRITLMMMAVWFTMSFSYYGLTVWFPDMIKHLQKSVVFEDSLFEECYFED
ITSSNTFFKNCTFISTLFYNTDLFEYKFINSKLINSTFLHNKEGCLLDFSDENNAYMIYFVSFLGTLAVL
PGNIVSALLMDKIGRLRMLAGSSVMSCVSCFFLSFGNSESAMIALLCLFGGVSIASWNALDVLTVELYPS
DKRTTAFGFLNALCKLAAVLGISIFTSFVGITKAVPILLASAALAAGSSLALKLPETR
>gnl|CDD|340998 cd17440, MFS_SV2C, Synaptic vesicle glycoprotein 2C of the Major Facilitator Superfamily of transporters. Synaptic vesicle glycoprotein 2 (SV2) is a transporter-like integral membrane glycoprotein, with 12 transmembrane regions, expressed in vertebrates and is localized to synaptic and endocrine secretory vesicles. Three isoforms have been identified, SV2A, SV2B, and SV2C. SV2A and SV2B are widely expressed in the brain, while SV2C is more restricted to evolutionarily older brain. SV2 isoforms have been shown to be critical for the proper function of the central nervous system. SV2 serves as the receptor for botulinum neurotoxin A (BoNT/A), one of seven neurotoxins produced by the bacterium Clostridium botulinum. BoNT/A blocks neurotransmitter release by cleaving synaptosome-associated protein of 25 kD (SNAP-25) within presynaptic nerve terminals. SV2C exhibits enriched expression in several basal ganglia nuclei, and has been found to be involved in normal operation of the basal ganglia network and could be also be involved in system adaptation in basal ganglia pathological conditions. SV2C belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
FFVLGMALMADGVEVFVVGFVLPSAETDMCIPNSGSGWLGSIVYLGMMVGAFFWGGLADKVGRRQSLLIC
MSVNGFFAFLSSFVQGYGLFLFCRLLSGFGIGGAVPTVFSYFAEVLAREKRGEHLSWLCMFWMIGGIYAS
AMAWAIIPHYGWSFSMGSAYQFHSWRVFVIVCALPCVSSVVALTFMPESPRFLLEVGKHDEAWMILKQIH
DTNMRARGQPEKVFTVNRIKKDNTIKLTIVWLTLSFGYYGLSVWFPDVIKHLQFKSVTFEDSLFKSCFFE
DVTSVNTYFRNCTFIETVFYNTDLEDYKFIDSDFINCTFFHNKTGCQITFDDDYSAYWIYFVNFLGTLAV
LPGNIVSALLMDRIGRLTMLGGSMVLSGISCFFLWFGTSESMMIGMLCLYNGLTISAWNSLDVVTVELYP
TDRRATGFGFLNALCKAAAVLGNLIFGSLVGITKAIPILLASTVLVCGGLVGLRLPDTR
>gnl|CDD|340999 cd17441, MFS_SVOP, Synaptic vesicle 2-related protein (SVOP) of the Major Facilitator Superfamily. Synaptic vesicle 2 (SV2)-related protein (SVOP) is a transporter-like nucleotide binding protein that localizes to neurotransmitter-containing vesicles. Like SV2, SVOP is expressed in all brain regions, with highest levels in cerebellum, hindbrain and pineal gland. Studies with knockout mice suggets that SVOP may perform a subtle function that is not necessary for survival under normal conditions, since mice lacking SVOP are viable, fertile, and phenotypically normal. SVOP shares structural similarity to the solute carrier family 22 (SLC22), a large family of organic cation and anion transporters. This SVOP subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
SILTGLAWMADAMEMMILSILAPQLHCEWRLPSWQVALLTSVVFIGMMLSSSLWGNISDQYGRKTGLKIS
VLWTLYYGILSAFAPIYSWILVLRGLVGFGIGGVPQSVTLYAEFLPMKSRAKCILLIEVFWALGTVFEVL
LAVFVMPTLGWRWLLILSALPLLIFAVLCFWLPESARYWTTILLWFIWFSNAFSYYGLVLLTTELFQAGD
VCSGSSGKKVEGKCSLECEYLTTSDYMDLLWTTLSEFPGLLVTLWIIDRFGRKKTMALCFFVFSFCTLLL
FSCVGRFSLTVLLFIARAFISGGFQAAYVYTPEVYPTATRALGLGTCSGMARVGALITPFIAQVMLESSV
YLTLSVYSGCCLLAAIASCFLP
>gnl|CDD|341000 cd17442, MFS_SVOPL, Synaptic vesicle 2 (SV2)-related protein-like (SVOPL) of the Major Facilitator Superfamily. Synaptic vesicle 2 (SV2)-related protein-like (SVOPL) or SVOP-like protein is a transporter-like protein that shares structural similarity to the solute carrier family 22 (SLC22), a large family of organic cation and anion transporters. It belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLFLIMGSTGVAEAMEIMLLAVVSPEIRCEWHLEDWQVALVTTMVFFGYMVFSILLGLLADRYGRWKILL
LSFVWGAYFSLLTSFAPSYIWFVFLRCMVGCGVSGHSQGLIIKTEFLPTKYRGYMLPLSQIFWLAGSLLI
IGLASVVIPTLGWRWLIRFASIPGIILIVVFKFIPRTTLQIWVIWLGISFAYYGVILASSELLERNLLCG
SDPSDEEAGIKHIESESPCYCHMFNPSDYQTMIISTLGEIALNPLNILGINFLGRRLSLVITMGLTAIFF
LLLNICTSSAGLTIFLFMLRALVSANFNTVYIYTAEVYPTTMRALGMGTSGSLCRIGAMVAPFISQVLMS
ASVLGALCLFSSVCIVCAISAFTLP
>gnl|CDD|341001 cd17443, MFS_SLC22A31, Solute carrier family 22, member 31 of the Major Facilitator Superfamily. Solute carrier family 22, member 31 (SLC22A31) is an uncharacterized member of the SLC22 family of transporters, which includes organic cation transporters (OCTs), organic zwitterion/cation transporters (OCTNs), and organic anion transporters (OATs). SLC22 transporters interact with a variety of compounds that include drugs of abuse, environmental toxins, opioid analgesics, antidepressant and anxiolytic agents, and neurotransmitters and their metabolites. SLC22A31 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
PSNLAVLCTGGWPFSAAAGLGSNLVTEWNLVCDDGWKVPLEKISYLLGWLLGYIILGAGCDRLGRRAAFV
LSLVLATLLGVSVALSASPPTFLVLRLLQGGTLAGVFLSLYIARLELCDPSHRLMVSMGAGFFSVAGELL
LPGLAVLCRDWRVLQGVGTLPLLLLLLYWCFPSRNGLILGFTAFIGGGIRYCFARNLAPFVPTFYLPYFL
QAGLEALACIFLCLTVDRCGRRGVLLLGTIVTGLSSLLLLALTQYLHGGLVLVLSVVGLLASHAVSMLSM
FFAAEVLPTVIRGAGLGLIMGAGFLGRAAGPLMELQNKQGYFLHHVVFASFAVLSVLCILLLP
>gnl|CDD|341002 cd17444, MFS_SLC22A23, Solute carrier family 22, member 23 of the Major Facilitator Superfamily. Solute carrier family 22, member 23 (SLC22A23) is an orphan member of the SLC22 family of organic cation/anion/zwitterion transporters, which includes organic cation transporters (OCTs/OCTNs) and organic anion transporters (OATs). It is abundantly expressed in brain and is also found in liver. Single-nucleotide polymorphisms in SLC22A23 are associated with inflammatory bowel disease (IBD) in a Canadian white population. SLC22 transporters interact with a variety of compounds that include drugs of abuse, environmental toxins, opioid analgesics, antidepressant and anxiolytic agents, and neurotransmitters and their metabolites. SLC22A23 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
TENASSCQCTERDYRIRAGLVQNIVSKWDLVCDSSWKVHIAKFSLLVGLIFGYLITGCLADWFGRRPVLL
FSVVFILIFGLTVALSVNVTMFSTLRFFEGFCLAGIILSLYALRIELCPPGHRFMITMVASFIAMAGQFL
MPGLAALCRDWQVLQAVIICPFLLMLSYWCIFPKNIVVLCVNSLTGYGIHHCFAKSMMDHEMKGSFLHNF
YAEYYTMAVIALASCLAMCPVVGFLGRRGGLLLFMILTALASLLQLGLLNLIGKYSQHPDSGMSDEVKDK
FSVTFSIVGMFSSHAVGSLSVFFCAEITPTVIRGGGLGLVLASAGFGMLTAPIMELHNQKGYFLHHIIFA
CCTLICIICILLLP
>gnl|CDD|341003 cd17445, MFS_SLC22A17, Solute carrier family 22, member 17 of the Major Facilitator Superfamily. Solute carrier family 22, member 17 (SLC22A17) is also called 24p3 receptor (24p3R), lipocalin-2 receptor, or neutrophil gelatinase-associated lipocalin (NGAL) receptor (NGALR). It functions as a cell surface receptor for lipocalin-2 (LCN2), also called NGAL or 24p3, which plays a key role in iron homeostasis and transport. LCN2 is a secreted protein of the lipocalin family that induces apoptosis in some types of cells and inhibits bacterial growth by sequestration of the iron-laden bacterial siderophore. Over-expressions of NGAL and NGALR have been found to be correlated with unfavorable clinicopathologic features and poor prognosis of patients with hepatocellular carcinoma. SLC22A17 is a member of the SLC22 family of organic cation/anion/zwitterion transporters, which includes organic cation transporters (OCTs/OCTNs) and organic anion transporters (OATs). It belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
TQTGVRHCDAGWNYTGLPGLTNNIVTEWDLVCSRYWLVPLEQVCFILGFASGYLCLGYTADRLGRRRTLL
LSLTLAVPFGVLVAVAASPSLFMAMRFLLGAALAGVYLTLYLTRLELCDPPQRLLVAMAGGLTMVGGHFL
LLGLALGCGSWRVLQGTITAPLSLFLCYGCPGVKNLLILGFTTFIAHAISHCYQSFSDDVRGTPSTFYLS
YLLSTGTAGLACLFLCATVDRFGRRGILLLAMTLTGIASLILLGLMDYLNDAAIKTFSILGLFSSQAAAS
LSILFAAEVIPTVIRGSGLGLIMALGSLGGLSSPLMRLRNQHGYFLHHVVLASLALLAILSIMLLP
>gnl|CDD|341004 cd17446, MFS_SLC22A6_OAT1_like, Solute carrier family 22 member 6 (also called Organic anion transporter 1) and similar transporters of the Major Facilitator Superfamily. This subfamily includes solute carrier family 22 member 6 (SLC22A6, also called organic anion transporter 1 or OAT1 or para-aminohippurate (PAH) transporter), SLC22A8 (or OAT3), and SLC22A20 (or OAT6). OAT1 and OAT3 are involved in the renal elimination of endogenous and exogenous organic anions (OAs). They function as OA exchangers, coupling the uptake of OAs against an electrochemical gradient with the efflux of intracellular dicarboxylates. SLC22A20 is an OA transporter that mediates the uptake of estrone sulfate. The OAT1-like subfamily belongs to the Solute carrier 22 (SLC22) family of organic cation/anion/zwitterion transporters of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LATEPCTDGWVYDKSEFPSTIITEWDLVCNHRALRQLAQSIYMAGVLVGAIVFGGLSDRFGRRPLLIWSY
LQMAVSGTCAAFSPSFPIYCVFRFLTGMALSGIVLNSVSLNVEWMPTRVRAVVGTLLGYCYTLGQLILAG
VAYAIRDWRWLQLAVSLPFFIFFLYSWWFPRITFCLSLVWFSTSFAYYGLAMDLQKFGVSIYLIQIIFGA
VDIPAKFISTLTMSYLGRRPTQAAALILAGIMILANIFVPQDLQTVRTALAVFGKGCLAASFNCVYLYTG
ELYPTVIRQTGMGLGSTMARLGGIVAPLVKMLGEYYPFLPLIIYGAAPILSGIAACFLP
>gnl|CDD|341005 cd17447, MFS_SLC22A7_OAT2, Solute carrier family 22 member 7 (also called Organic anion transporter 2) of the Major Facilitator Superfamily of transporters. Solute carrier family 22 member 7 (SLC22A7), also called organic anion transporter 2 (OAT2) mediates sodium-independent transport of a variety of organic anions including prostaglandin E2, prostaglandin F2, tetracycline, bumetanide, estrone sulfate, glutarate, dehydroepiandrosterone sulfate, allopurinol, 5-fluorouracil, paclitaxel, L-ascorbic acid, salicylate, ethotrexate, and alpha-ketoglutarate. It also plays a role in renal uric acid uptake from blood as a first step of tubular secretion. OAT2 belongs to the Solute carrier 22 (SLC22) family of organic cation/anion/zwitterion transporters of the Major Facilitator Superfamily (MFS)of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
SDLPVVPCQNGWVYDHSTFSSTIATEWDLVCDRKGLNQATATFFFAGVTMGAVAFGYLSDRFGRKRMLLV
AYVLSLVFGLASAFSVSYVMFAITRTLTGFALTGFSIISMVLCVEWVDIEHRTVAGVLISLFWTVGNMLL
ALVAYLIRDWRWLILAVTLPCAPGIITWWWVPKISLCTGIVWFGVAFTYYGISFNISGFGLNVYLTQFIY
GAIELPAKLLAYLLLDRIGRRLTQAGSLILTGLSIGINILIPSEFTVVRTVIAVLGKGFSEAAFTTVFLY
TSELYPTVLRQNGMGYTSFIARLGGSLAPLVILLDDVWLSLPQVIFCGVALLAGGVAFLLP
>gnl|CDD|341006 cd17448, MFS_SLC46A3, Solute carrier family 46 member 3 of the Major Facilitator Superfamily of transporters. Solute carrier family 46 member 3 (SLC46A3) is a lysosomal membrane protein that functions as a direct transporter of noncleavable antibody maytansine-based catabolites from the lysosome to the cytoplasm. SLC46A3 belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance (TetA) -like (SLC46/TetA-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LYLVEPVVALYAFASFMTYPLIQQYVYRRLWEETSNSTYISSSNISHCEKNKSSPAFVFQEEVQKKTSLF
NMQMDLSGLIPSLIVTLILVSYSDRHGRKFSIILPSIGALLTSLSYCLVSYFSFPLNLLIASSFISGLFG
GFTTFIGGCFAYVADLCKDHKQKTIRMAVVDMILGVLTGLAGLSSGYFIRALGFNWPFLTIALLHVVNLL
YILFFLVVLCLLLFAFSTYLLANFGGASIFILYELNAPLCWNEVLVGYGSAASTAIFLTSFVGVALFSRC
LPDIYIVFIGIFSVAGGMIMTAFAKTTLLMFLVRLPLLFAIMPFPVLRSMMSKVVLPSEQGALFACVAFL
ETLSGVLSVTIFNSIYAATVAWFPGFSFLLSAGLCLIPASLLCVLL
>gnl|CDD|341007 cd17449, MFS_SLC46A1_PCFT, Solute carrier family 46 member 1, also called Proton-coupled folate transporter, of the Major Facilitator Superfamily of transporters. Solute carrier family 46 member 1 (SLC46A1) is also called proton-coupled folate transporter (PCFT), G21, or heme carrier protein 1 (HCP1). It functions in two ways: as an intestinal proton-coupled high-affinity folate transporter that facilitates the absorption of folates across the brush-border membrane of the small intestine; and as an intestinal heme transporter which mediates heme uptake from the gut lumen into duodenal epithelial cells. It displays a higher affinity for folate than heme. It is also expressed in the choroid plexus and is required for transport of folates into the cerebrospinal fluid. Loss of function mutations in the SLC46A1 gene results in the autosomal recessive disorder "hereditary folate malabsorption" (HFM), characterized by severe systemic and cerebral folate deficiency. SLC46A1 belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance (TetA) -like (SLC46/TetA-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
SVTVEPVLFLAMFALVLQGPLTTQYLWDRLSADLGYNGTRTRGCASNASTSADPLQQEVETLTAHWNLYI
NLGGFLVGLFSVTLLGPWSDSVGRRPVLILPSLGLALQAAVYLLVMYLQLHVAYFLIGRILSGLLGDFNG
ILAGCFAYVADVSDRRSRTFRVAVLEACLGLAGMLASIIGGQWRKAQGYINPFWLVLALNLAAALYAAFC
VGESVKEPKSARLFTTRHHQSVVRLYVAPAPNGSRRKLALYSLALFVVVTVHFGAKDLLVLYELSSPLCW
DSDLIGYGSAAEHLTYLSSLLGLRLLQLCLEDTWVAEIGLISNISGLVVISVATTTPLMFTGYGLLFLSM
ATTPVIRAKLSKLVRETEQGALFASVACVEGLCSLVATGIFNSLYPATLHFMKGFPFLFGAALLLIPAGI
IGLLE
>gnl|CDD|341008 cd17450, MFS_SLC46A2_TSCOT, Solute carrier family 46 member 2, also called Thymic stromal cotransporter protein, of the Major Facilitator Superfamily of transporters. Solute carrier family 46 member 2 (SLC46A2) is also called thymic stromal cotransporter protein (TSCOT). It is a putative 12-transmembrane protein mainly expressed in the thymic cortex in a specific thymic epithelial cell (TEC) subpopulation. Polymorphisms in TSCOT are linked to cervical cancer in affected sib-pairs with high mean age at diagnosis. TSCOT belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance (TetA) -like (SLC46/TetA-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RTWIEPVVASAQVASSFYDTGLLMVVKEYYNNTSSSSNRGLEDAQQKAISNFYMIYNLVAGLSPLLPAYL
LAKLGDRRHRKITICVPLLGYLLSRALLLLVILLDWPLEVMYGAAALNGLTGGFTAYWAGVMALASLASS
EGRRSVRLITIELVYGLAGFLGSLASGHIFVHYTINHHQGAILAACSLVLYVLCLLYSVFVLKITIALLF
VGAILYDLAVAGGMDVLSVFVLKEPLSWGAVEVGYGNAAGYMIFITSFLGVFVFSRCLRDTTMIMIGMVS
FSSGILIMAFVKWTFMFYIARAVMLFALIPLPTIRSLISKQVQGSSYGKVFVMLQLSLKLTGVATSTIYN
KIYQATLDWFPGFCFILSSILGFLSIIPISIVA
>gnl|CDD|341009 cd17451, MFS_NLS1_MFSD2A, Sodium-dependent lysophosphatidylcholine symporter 1 of the Major Facilitator Superfamily of transporters. Sodium-dependent lysophosphatidylcholine (LPC) symporter 1 (NLS1) is also called major facilitator superfamily domain-containing protein 2A (MFSD2A). NLS1/MFSD2A is an LPC symporter that plays an essential role for blood-brain barrier formation and function. It also transports the essential omega-3 fatty acid docosahexaenoic acid (DHA), which is essential for normal brain growth and cognitive function, in the form of LPC into the brain across the blood-brain barrier. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. NLS1/MFSD2A belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
KLCYAIGGAPYQITGCALGFFLQIYLLDVAQLDPFYASIILFVGRAWDAITDPTVGFFVSKSPWTRFGRL
MPWIIFSTPFAVLSYFLIWFVPDFSQGKVMWYLLFYCLFQTLQTCFHVPYSALTMFISTEQKERDSATAY
RMTVEVLGTVLGTAIQGQIVGMAAYMIAAGVICAIYVLCAIILFLGVREQREPCELKSQKPVSFFKGLKL
VMSHGPYIKLITGFLFTSLAFMLLEGNFALFCTYTLGFRNDFQNILLVIMLSATLTIPFWQWFLTRFGKK
TAVYIGISSAVPFLILVVLVESNLIVTYVVSVAAGVSVAAAFLLPWSMLPDVVDDFKLKNPDSQGHEAIF
YSFYVFFTKFASGVSLGISTLSLDFAGYQTRGCSQPEEVNLTLKMLVSAAPVVLILLGLLLFKLYPIDE
>gnl|CDD|341010 cd17452, MFS_MFSD2B, Major facilitator superfamily domain-containing protein 2B. Major facilitator superfamily domain-containing protein 2B (MFSD2B) is closely related to MFSD2A, and their conserved genomic structure suggests that they are derived from the duplication of an ancestral gene. Variations of chromosome 2 gene expressions among patients with lung cancer or non-cancer identified MFSD2B as a potential risk or protect factor in the prognosis of lung adenocarcinoma. MFSD2B belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
KLCYAIGGAPNQVAGSATAFFLQIYLLDIAQITPFQASLVLFVGKAWGAATDPVVGFFISKSKWTKIGRL
MPWMLGCTPFIVVSYFFLWFVPPFTTGRFLWYLTFYCLFQALATCFHVPYSALTMFLSTDQRERDSATAY
RMTVEVLGTLVGAAVQGQIVASAYMIAAGVIGGLYLLCISVLFLGVKERDDPYAPKSGKAIPFFKGLSLT
MRHGPYLKLTASFLFISAAVQLEQSNFVLFCTHAVDLHDHFQNLVLTILVSAVVSIPFWQWFLQRFGKKA
AACGISWMIPFAIMLVTIPNLIVAYVVAFVSGLSIAASLLLPWSMLPDVVDDFRLQNPHGKGLETIFYSS
YVFFTKLSAGIALGISTLSLEFAGYETGACKQPESVVLTLKLLIGAAPTCMILIGLCILMFYPITE
>gnl|CDD|341011 cd17453, MFS_MFSD4A, Major facilitator superfamily domain-containing protein 4A. Major facilitator superfamily domain-containing protein 4A (MFSD4A) belongs to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
TLTYWSVFFSFGLCIAFLGPTLLDLRCQTQSSLQQITWVFFSQQFCLLLGSTLGGVFKRTLAQSLFALFV
SSLAISVVFAIIPFCRNVGVLAFVMAVAGLAMGCIDTISNMQLVKIYQKDSAVFLQALHFFVGFGALLSP
LIADPFLSDTNCVSYAFWIMAIINLPVPIAVFVLLYKERMVPCCSDPSRPLLSADELAMEARPEEKLDES
TGKAHTSNGHADLFSCCQSKNFRGAPFSFFAIHVTGALVLFMTDGIVGEYSGFVYSYAVEPPLNLPHKVA
GYLPSLFWGFITLGRLISIPISYRMKPATMVFINLVGVIVTFLLLLIFSNSTVFLFVGTASLGLFLSSTF
PSMLAYTEDILQYKGCATTVLVTGAGMGEMVLQMLVGSIMHSQGSYSFLVCGMIFGCLAFTFYTF
>gnl|CDD|341012 cd17454, MFS_NaGLT1_MFSD4B, Sodium-dependent glucose transporter 1, also called Major facilitator superfamily domain-containing protein 4B. Sodium-dependent glucose transporter 1 (NaGLT1) is also called major facilitator superfamily domain-containing protein 4B (MFSD4B). NaGLT1 is a primary fructose transporter in rat renal brush-border membranes. It also facilitates sodium-independent urea uptake in assays performed on Xenopus oocytes. NaGLT1/MFSD4B belongs to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
ALCASFLGLGMSIAVLGPTFQDLATNVNKNISNISYIFVGRSLGYLGGSVLGGILFDCMNHHLLLGFSML
ITAAGLFAIPWCKKALLLTALMSLIGVSMGVLDTGGNVLILNTWGDQAGPHMQALHFSFALGAFVAPILA
KLAFLWAYIVIGTYVLLVSLFFFILYSKSSSNREKSKASAQKTRFAKYHNALIILLFLFFFFYVGAEVTY
GSYIFTYAKTYVHMEESEAAGLNSLFWGTFAACRGLAIFFAACLYPGTMILLSLIGSTVSSLFLVLFSKN
PISLWVGTAVYGASMATTFPSGISWIEQYTTITGKSAALFVVGAALGEMVIPAVVGYLQGHVPDYPVLMY
TALGTSTMTAILFPVMYKL
>gnl|CDD|341013 cd17455, MFS_FLVCR1, Feline leukemia virus subgroup C receptor-related protein 1 of the Major Facilitator Superfamily of transporters. Feline leukemia virus subgroup C receptor-related protein 1 (FLVCR1) is also called feline leukemia virus subgroup C receptor (FLVCR). FLVCR1 is a heme transporter and it has two isoforms: 1 (or FLVCR1a), which exports cytoplasmic heme as well as coproporphyrin and protoporphyrin IX; and 2 (FLVCR1b), which promotes heme efflux from the mitochondrion to the cytoplasm. Mutations in the FLVCR1 gene have been linked to vision impairment, posterior column ataxia, and sensory neurodegeneration with loss of pain perception. FLVCR1 belongs to the Solute carrier 49 (SLC49) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RRFAVLAVFSLYSLVNAFQWIQYSIITNIFTEFYGVSSGAIDWLSVVYMVAYVPLIFPATWLLDLKGLRV
TALLGAGLNCLGAWVKCASVRPDLFGVTMLAQVLCSVAQVFILGLPSRIASVWFGPREVSTACAVAVLGN
QLGTAIGFLLPPVLVPNTVDDIDLMGHNISIMFYGTAAVSTLLFILTIIVFKEKPPLPPSQAQAVLQGIP
SEDYSYKQSIINLFKNVPFVLLLISYGIMTGTFYSVSTLLNQMIITHYEGEEVNAGRIGLTLVVAGMVGS
ILCGLWLDYTKTYKQTTLIVYILSFIGMVVFTFTLDLGYLIVVFVTGGVLGFFMTGYLPLGFEFAVEITY
PESEGTSSGLLNASAQIFGIIFTLIQGKLTTDYGPQAGNIFLCAWIFVGIILTALIK
>gnl|CDD|341014 cd17456, MFS_FLVCR2, Feline leukemia virus subgroup C receptor-related protein 2 of the Major Facilitator Superfamily of transporters. Feline leukemia virus subgroup C receptor-related protein 2 (FLVCR2) is also called calcium-chelate transporter (CCT). It functions as a heme importer as well as a transporter for a calcium-chelator complex that is important for growth and calcium metabolism. Mutations in the FLVCR2 gene cause Proliferative vasculopathy and hydranencephaly-hydrocephaly syndrome (PVHH), also known as Fowler syndrome, a rare autosomal recessive disorder characterized by glomerular vasculopathy in the central nervous system, severe hydrocephaly, hypokinesia and arthrogryphosis. FLVCR2 belongs to the Solute carrier 49 (SLC49) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RRWVIVLLFSSYSLCNAFQWIQYGIINNIFMHFYGVSSFAIDWLSMSYMLTYIPLIFPVAWLLDKRGLRV
IALVGSALNCLGAWIKTGSARPDLFPVTVLGQLVCSVAQVFILGMPSRIASVWFGSSEVSTACSIGVFGN
QLGVAIGFLLPPVLVPNIDDLDELAYHISIMFYGTAAVATLLFILVIIVFQEKPKIPPSQAQAAIQSIPS
QDYSYLQSILRLLKNVNFILLVVSYGLNTGCFYALSTLLNRMVIFHYPGEEVNAGRIGLTIVVAGMVGAL
ISGIWLDRTKTYKQTTLAVYIMSLVGMVVYTFTLNLGHLWVVFITAGTLGFFMTGYLPLGFEFAAELTYP
ESEGTSSGLLNVSAQVFGIIFTISQGQIIDNFGTKAGNIFLCAFLLVGTILTALIK
>gnl|CDD|341015 cd17457, MFS_SLCO1B_OATP1B, Solute carrier organic anion transporter 1B subfamily of the Major Facilitator Superfamily of transporters. The Solute carrier organic anion transporter 1B (SLCO1B), also called organic anion-transporting polypeptide 1B (OATP1B), subfamily is composed of two human proteins, OATP1B1 (encoded by SLCO1B1) and OATP1B3 (encoded by SLCO1B3), and one rodent member, OATP1B2 (encoded by Slco1b2). OATP1B1 and OATP1B3 are almost exclusively expressed on the basal side of hepatocytes in normal human organs. They both can accept a wide variety of structurally-unrelated compounds as substrates including clinically-important drugs such as hydroxymethylglutaryl (HMG)-CoA reductase inhibitors (statins), angiotensin II receptor blockers (sartans), angiotensin converting enzyme (ACE) inhibitors, and anti-diabetes drugs (glinides). Loss-of-function mutations in both SLCO1B1 and SLCO1B3 genes result in the Rotor syndrome, a hereditary hyperbilirubinemia. The SLCO1B/OATP1B subfamily belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LKMFLAALSFSYFAKALSGIIMKSSITQIERRFDISSSTVGFIDGSFEIGNLLVIAFVSYFGAKLHRPKL
IAAGCFIMGLGSVLTALPHFFMGYYKYGCLKESGSYMWVYVLMGNMLRGIGETPIVPLGISYLDDFAKEE
NSPLYLACLHTIAMIGPMIGFTLGSLFAKLYVDIGFVDLSTIRITPQDSRWVGAWWLGFLVSGLFSIISA
IPFFFLPGFFQSLKSILTNRLYVMFVCLTLLQVSSFIGFFTYKPKYMEQQYGQSSSKANFLLGVITLPIF
ASGMFLGGYIMKKYKLNTVGAAKFACFTSVMALSFYLLYFFIGCENKSVAGITMTYDGNNPVTSHRDVIL
SYCNSDCNCDESQWDPVCGNNGITYISACLAGCKSSSGNGKPIVFHNCSCLEVTGSQNRNYSAHLGECPR
DDDCSRMFYFYVVIQVLNLFFSALGGTSAYMLIVK
>gnl|CDD|341016 cd17458, MFS_SLCO1A_OATP1A, Solute carrier organic anion transporter 1A subfamily of the Major Facilitator Superfamily of transporters. The Solute carrier organic anion transporter 1A (SLCO1A), also called Organic anion-transporting polypeptide 1A (OATP1A), subfamily is composed of one human member OATP1A2 (encoded by SLCO1A2) and several rodent proteins encoded by the Slco1a1, Slco1a3, Slco1a4, Slco1a5, and Slco1a6 genes. OATP1A2, also known as human OATP-A or OATP1, shows a broad spectrum of substrates including endogenous compounds (such as bile acids, steroid hormones and their conjugates, thyroid hormones) and various drugs (such as fexofenadine, ouabain and the cyanobacterial toxin microcystin). It is expressed in the brain, kidney, intestine, liver, lung, testes, and the eye (ciliary body). The SLCO1A/OATP1A subfamily belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
KLKIFLLALSYAYVAKTLSGAYMNSMITQIERRFNIPSSLVGIINGSFEIGNLLVIAFVSYFGAKLHRPK
VIGLGCLIMSLGCFLASLPHFLMGRYEYESTVSTTSNSSSRVPLCLANQSLSHNVTQLPSECEKESMSLM
WIFVLVGNLLRGIGETPVMPLGISYIDDFSKKENSPFYIGCLHTATIVGPLLGLLLASFCAQLYVDLGSV
NADDLTITPTDIRWVGAWWLGFLICAGVNFLAGLPFWFLPKSLPKEGEENETEPSKTLTVELEENKGQET
KQEMYEIAKDFLPFLKSLFRNPIYMLFIIVTVLQFNAFSGMISFMPKYLEQQYGKSASDAIFLIGVYNLP
IICLGYFFGGLYMKKFKINTYQAAHIGFWVSLLEYLLYFSAFWMGCDNSPVAGLTVSYEGIDQDSYYENT
LLADCNRDCDCPLKVWDPVCGNNGLTYVSACLAGCKASVGTGKNMVFQNCSCVAASGFPSQNSSAVGQCD
KGETCDKMLQYFLILSLVCSFIFSLAAMPGYMVLIRS
>gnl|CDD|341017 cd17459, MFS_SLCO1C_OATP1C, Solute carrier organic anion transporter 1C subfamily of the Major Facilitator Superfamily of transporters. The Solute carrier organic anion transporter 1C (SLCO1C), also called Organic anion-transporting polypeptide 1C (OATP1C), subfamily contains one mammalian member, OATP1C1 (encoded by SLCO1C1), which is also called thyroxine transporter. It mediates the high affinity transport of the thyroid hormones, T4 (3,5,3',5'tetraiodo-L-thyronine or thyroxine), rT3 (3,3'5'-triiodo-L-thyronine), and T3 (3,5,3'tri-iodo-L-thyronine or triiodothyronine), as well as organic anions such as 17-beta-glucuronosyl estradiol, estrone-3-sulfate, and sulfobromophthalein (BSP), which are transported with much lower efficiency. The SLCO1C/OATP1C subfamily belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LKIFLAALSFAYFAKALSGSYMKSTITQIERRFDIPSSLIGVIDGSFEMGNLLVIAFVSYFGAKLHRPRI
IGAGCLLMAIGTFLIALPHFFMGRYKYETAIQSSSNSTVSISPCSLEPSPQLHSIESSDSKTGTGCEKEP
GSSMWIYVFLGNLLRGIGETPVQPLGISYIDDFAKEENAAFYIGCVQTIAIIGPVFGFLLGSLCAKLYVD
IGFVNLDSITITPKDARWVGAWWLGYLIAGVITLLSAVPFWFLPKSLPKDFLPSLKNLLGNPVYFLYLCT
SILQFNSLIGMVTYKPKYIEQQYGQSASKANFLIGLINIPAVAIGIFSGGLLMKKFKLSVIGAAKLSFGT
SFFGYLLLLSFFAMGCENSDVAGLTVSYNGTKQVSYADRSLFSQCNADCKCSQKDWDPVCGENGITYVSP
CLAGCKASNGSGKNTVFHNCSCIGIPSSASGSSSAILGQCPKGNACARMFLYFLAISVISSFTLSLGGTP
GYILLIRC
>gnl|CDD|341018 cd17460, MFS_SLCO2B_OATP2B, Solute carrier organic anion transporter 2B subfamily of the Major Facilitator Superfamily of transporters. The Solute carrier organic anion transporter 2B (SLCO2B), also called Organic anion-transporting polypeptide 2B (OATP2B), subfamily has one mammalian member, OATP2B1 (encoded by SLCO2B1). It mediates the Na(+)-independent transport of various organic anions such as taurocholate, the prostaglandins PGD2, PGE1, PGE2, leukotriene C4, thromboxane B2 and iloprost. It also mediates the transport of endogenous sex steroid conjugates such as dehydroepiandrosterone sulfate (DHEAS). SLCO2B1 variations result in differential expression and uptake of DHEAS, which impacts subsequent resistance to androgen-deprivation therapy (ADT), the primary treatment of metastatic prostate cancer. The SLCO2B/OATP2B subfamily belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
IKFFVLCHGLLQLSQLLVSGYLKSSISTIEKRFGLSSQTSGLLASFNEVGNTVLIVFVSYFGSRVHRPRF
IGCGAILVSLAGFLMALPHFISEPYEYGILFLGQLLLGIGGVPIQPFGISYIDDFASESNSPLYLGILFA
VTVLGPGFGFMLGSAMLRFYVDIDKMSEDEISLEIGDPRWVGAWWLGFLIAATLVALSAVPYFFFPREMP
KEVVELQPREKKLAKTMLKKLKSLSDILQNLSLLQFIKKFPRILLRTLRNPIYLLVVLAQVNLSAMVAGL
ATFMGKFLERQFSITASFANLMIGGLNIPSAMVGIVVGGVILKRLQLTVRGCGAMCVLGMLLCLFFALPL
LFIGCSTQKIAGITHRTSSSPGLELSSQCSEACSCPPEAFNPVCGSDGVEYISPCHAGCKSVNVQALDNS
VVNYTDCSCVSEGGPVGAASPGTCGSGCSHLLVPFMLLVSLGGFLASLSHTPSFMLILR
>gnl|CDD|341019 cd17461, MFS_SLCO2A_OATP2A, Solute carrier organic anion transporter 2A subfamily of the Major Facilitator Superfamily of transporters. The Solute carrier organic anion transporter 2A (SLCO2A), also called Organic anion-transporting polypeptide 2A (OATP2A), subfamily has one mammalian member, OATP2A1 (encoded by SLCO2A1), which is also called prostaglandin transporter. It is a lactate/prostaglandin anion exchanger that mediates the release of newly synthesized prostaglandins (PGD2, PGE1, PGE2, PGF2A and PGI2) from cells, the transepithelial transport of prostaglandins, and the clearance of prostaglandins from the circulation. Mutations in SLCO2A1 can cause primary hypertrophic osteoarthropathy (PHO), a rare multi-organic disease characterized by digital clubbing, pachydermia and periosteal reaction. The SLCO2A/OATP2A subfamily belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
NIKVFVLCHGLLQLSQLLYSAYFKSSLTTIEKRFGLSSLSSGLISSLHEIGNAVLIIFVSYFGSRVHRPR
LIGIGGLLLALGAFLLTLPHFLSEPYQYSMWVLMVVAQLLAGIGTVPIQPFGISYVDDFAEPSNSPLYIA
ILFAISVFGPAFGYLLGSVVLRIFVDIGRVNTATVELTPADPRWIGAWWLGLLISSGLLVLTSLPYFFFP
REMLVGKKPSPEGDMLRKKEDEKKEEGSLLDFIKRFPKMFVKLLLNPLFMLLVLAQCTFSSVIAGLSTFL
NKFLEKQYGASASYANFLIGAVNLPAAALGMLLGGIIMKRFGFSLRAIPRFSVVILSISIMLCVPLFFMG
CSTQDVAGVYPKTSNSSDGPHLSCSANCSCPESAFNPVCGENGIEYISPCHAGCTNSNMDSSTYRQQIYS
NCSCIPDLSGEKPAKTGSCPNSCSHLLLPVMFLISFAGLIACLTHNPLYMMVLR
>gnl|CDD|341020 cd17462, MFS_SLCO4A_OATP4A, Solute carrier organic anion transporter 4A subfamily of the Major Facilitator Superfamily of transporters. The Solute carrier organic anion transporter 4A (SLCO4A), also called Organic anion-transporting polypeptide 4A (OATP4A), subfamily has one mammalian member, OATP4A1 (encoded by SLCO4A1). It is ubiquitously expressed and it mediates the Na(+)-independent transport of the thyroid hormones T3 (triiodo-L-thyronine), T4 (thyroxine) and rT3, and other organic anions such as estrone sulfate and taurocholate. OATP4A1 is the most abundantly expressed transporter colorectal cancer (CRC) and its role in the transport of estrone sulfate, which is used in hormone replacement therapy (HRT), affects the outcome of the treatment. The SLCO4A/OATP4A subfamily belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
PKGVLFFLCAASFLQGMTVNGFINTVITSIERRFDLRSYQSGLIASSYDIAACLCLTFVSYFGGSGHKPR
WLGWGVLIMGLGSLVFALPHFTVFMLGQFLHGIGATPLYTLGVTYLDENVKSNYSPVYIGIFYTAAIVGP
AAGYLLGGFFLNIYTEIGRQTELTPENPLWVGAWWIGFLGAGAAALLIALPILGYPRQLPGLLKNPTFIF
LCLAGATEATLIAGMSTFGPKFLESQFSLSASEAATLFGYLVVPAGGGGTFLGGFIVNKLKLRCSGIIKF
CLICTVVSLLAIFIFSLHCPNVPMAGVTASYRGSVLPEGSLNLTALCNADCRCLEEIYSPVCGADGLMYY
SPCHAGCSEAYSDIRNGQKVYQDCSCVAGNLSVGFGEASAGKCTSNCNHMPLLLAFVFLVILFTFLCSIP
ALTATLR
>gnl|CDD|341021 cd17463, MFS_SLCO4C_OATP4C, Solute carrier organic anion transporter 4C subfamily of the Major Facilitator Superfamily of transporters. The Solute carrier organic anion transporter 4C (SLCO4C), also called Organic anion-transporting polypeptide 4C (OATP4C), subfamily has one mammalian member, OATP4C1 (encoded by SLCO4C1). It is capable of transporting pharmacological substances such as digoxin, ouabain, thyroxine, methotrexate and cAMP. It is the only OATP expressed at the basolateral side of proximal tubular cells in human kidney and it mediates the excretion of uremic toxins, which accumulate in patients with chronic kidney diseases (CKDs) and cause further progression of renal damage and cardiovascular diseases. Overexpression of human SLCO4C1 in rat kidney promotes the renal excretion of uremic toxins and reduces hypertension, cardiomegaly, and renal inflammation in renal failure. The SLCO4C/OATP4C subfamily belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
PKGYLLFYSLLAVVQGIVVNGLVNISISTIEKRYELSSSLTGLISSSYDISFCLLSLFVSFYGERGHKPR
WLAFSAFMIGLGSLVFSLPHFFVFILGQLLLGVGGTPLYTLGTAYIDDSVPTHKSSLYIGIGYGMSVLGP
AIGYLLGGQLLNIYIDVNKGQSVDLTEEDPRWLGAWWIGFLMCWLIAWCLIAPFSCFPKHLPGLLKNPVF
MCLTISSCSEALITTGFATFLPKFIENQFGQTSSFAAILGGLVLIPGAAIGQILGGIIVSKFKLKCKNMI
KFAIITTTVSLLLLSVFIFAKCGNDPFAGVSETYNGTGKIGNLTAPCNANCSCLSSFYYPVCGADGVQYF
SPCFAGCTNENLHDKKKVYYNCSCIGNFTEEFSANTTKCEEGKKCETTCKNLPIFLCFFFFVVIFTFMTS
TPITVAILR
>gnl|CDD|341022 cd17464, MFS_MCT10, Monocarboxylate transporter 10 of the Major Facilitator Superfamily of transporters. Monocarboxylate transporter 10 (MCT10) is also called Solute carrier family 16 member 10 (SLC16A10). In addition, human MCT10 is also called T-type amino acid transporter 1 (TAT1). MCT10 is a sodium-independent transporter that mediates the uptake or efflux of aromatic acids such as Phe, Tyr, and Trp, as well as L-3,4-di-hydroxy-phenylalanine. It is also a thyroid hormone transporter with preference for triiodothyronine (T3). MCT10 is expressed in intestine, kidney, liver, muscle, and placenta, and appears predominantly localized in the basolateral membrane. It belongs to the Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWVVMLAAMWCNGSVFGIQNAFGVLFVSLLEEFGSKDDAQMRFKTAWVGSLSMGMIFFCSPIVSVFTDLF
GCRKTATGGAAVGFVGLLASSFVSSIEPLYFTYGIIFACGCSFAYQPSLVILGHYFKKRLGLVNGIVTAG
SSVFTITLPFLLRVLLDSVGLFNTLRVLCIFMFVLFLAGFTYKPLVPMKKDKEGKKRKFKCPPLKKIFNF
NIWKSTGYRIWAFGIPAALFGYFVPYVHLMNHVKERFGEDVNKEVLLMCIGITSGIGRLIFGRVADYIPG
VKKVYLQVSSFFFIGLMSMMIPLCHVFGGLIAVCLFMGLFDGCFISIMAPIAFELVGAQNVSQAIGFLLG
LMSIPMTVGPPIAGFLRDRLGSYDVAFYLAGVPPIIGGIILCFIP
>gnl|CDD|341023 cd17465, MFS_MCT8, Monocarboxylate transporter 8 of the Major Facilitator Superfamily of transporters. Monocarboxylate transporter 8 (MCT8) is also called Solute carrier family 16 member 2 (SLC16A2) or X-linked PEST-containing transporter. MCT8 is a very active and specific thyroid hormone transporter which stimulates the cellular uptake of thyroxine (T4), triiodothyronine (T3), reverse triiodothyronine (rT3) and diidothyronine (T2). Inactivating mutations in SLC16A2, the gene that encodes MCT8, lead to an X-linked syndrome with severe neurological impairment known as Allan-Herndon-Dudley syndrome (AHDS). AHDS is characterized by congenital hypotonia that progresses to spasticity with severe psychomotor delays, spastic paraplegia and dystonic movements, global developmental delay, and profound intellectual disability. MCT8 belongs to the Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
GWVVVFAATWCNGSIFGIQNSFGILYVMLLNEQEDQKDQAVQFKTAWVGALAMGMIFFCSPVVSIFTDRF
GCRKTAMGGAAVAFIGLLSSSFTKSLGLRYFTYGILFGCGSSFAFQPSLVILGHYFRRRLGLANGVVTAG
SSLFSMLLPFLLKMVGDAIGLAHTFQVLSLFMFIQIFLSLTYKVFRRKTYRIWAFGIATAVLGYFVPYVH
LMKYVEEEFKENKREWVLLVCIGASSGIGRLMSGKIGDLIPGLKKIYLQVASFLLLGIMSMMIPLCQVFE
GVIVVCLFLGLCDGCFITIMAPIAFELVGPMQASQAIGYLLGLMAIPMTAGPPIAGLLHDYFGSYHVAFY
LAGVPPIIGGTVLFFVP
>gnl|CDD|350654 cd17466, T3SS_Flik_C_like, C-terminal domain of type III secretion proteins FliK, HrpP, YscP, and similar domains. Type III secretion systems (T3SS) are essential components of two complex bacterial machineries: the flagellum, which drives cell motility, and the non-flagellar T3SS, which delivers effectors into eukaryotic cells. This model represents the C-terminal domain of T3SS proteins such as the flagellar hook-length control protein FliK, and non-flagellar Yop proteins translocation protein P (YscP) and HrpP. FliK is responsible for switching secretion from the hook protein to that of the filament protein, by interacting with FlhB, the switchable secretion gate. HrpP is a type III secretion system substrate specificity switch-domain protein that is required for the export of pathogenicity factors into plant cells by pathogens. YscP is a needle-length sensing protein that controls the needle length of the injectisome, which is used by pathogenic bacteria to inject effector proteins across eukaryotic cell membranes. FliK, YscP, and HrpP contain a C-terminal globular domain that is necessary for the hierarchical switching of substrates during T3SS assembly and subsequent virulence effector secretion and is also referred to as the substrate-switching (SS) domain or the type III secretion substrate specificity switch (T3S4) domain
EQVPTQLIDEVAQRLPDQPDGPLSFQLRLPSLGSVRVNANKTENQWQVQLGFARRDVLKRLAAHTGLCRL
SLSQALGQDVQLDMHED
>gnl|CDD|350655 cd17467, T3SS_YscP_C, C-terminal substrate-switching domain of ruler proteins from the Ysc family, such as YscP and PscP. This subfamily includes needle-length sensing proteins, also called ruler proteins, in type 3 secretion systems (T3SS), such as Yersinia pestis Yop proteins translocation protein P (YscP) and Pseudomonas aeruginosa PscP. T3SS ruler proteins contain an N-terminal helical region that dictates needle length and is referred to as the length-sensing (LS) domain, and a C-terminal globular domain that is necessary for the hierarchical switching of substrates during T3SS assembly and subsequent virulence effector secretion and is also referred to as the substrate-switching (SS) domain or the type III secretion substrate specificity switch (T3S4) domain. The C-terminal SS domain is highly stable and sits on the extracellular side prior to needle assembly
ARDLNQLLEKLVERILVSLPSGGKEVRLQLNLPQLGGTEIRIKQDNGQLQVEIRASNASLLILQQARQDL
LERLQRLNPDQPVRLTFSNQQQSEQQGSRQRRHVYEEWEEE
>gnl|CDD|350656 cd17468, T3SS_HrpP_C, C-terminal domain of type III secretion protein HrpP and similar domains. This subfamily contains Pseudomonas syringae HrpP, a type III secretion system (T3SS) substrate specificity switch-domain protein that has has an atypical T3SS translocation signal. HrpP is required for the export of pathogenicity factors into plant cells. HrpP contains a C-terminal domain similar to the globular C-terminal substrate-switching (SS) domain, also called the type III secretion substrate specificity switch (T3S4) domain, of Yersinia pestis YscP
AAAALWQALIEQLAPRLPAQAQWPLQFTLLLPRLGRVDVRARRRPGGWDIELRFERADTLQWLRGQRQRC
QRRLSRALGQPVRLRLEQE
>gnl|CDD|350657 cd17470, T3SS_Flik_C, C-terminal domain of flagellar hook-length control protein FliK and similar domains. The flagellar hook-length control protein FliK is a soluble cytoplasmic protein that is secreted during flagellar formation. It controls hook elongation by two successive events: by determining hook length and by stopping the supply of hook protein. It contains an N-terminal domain that determines hook length and a C-terminal domain that is responsible for switching secretion from the hook protein to that of the filament protein, by interacting with FlhB, the switchable secretion gate
AELAQQLAEQIRQLARQGVQEAEIRLDPEELGKVDIKLSVEGGQVSAQITAENPEARELLESNLPQLRQA
LAQQGLQLAQVDVSVG
>gnl|CDD|341024 cd17471, MFS_Set, Sugar efflux transporter (Set) family of the Major Facilitator Superfamily of transporters. This family is composed of sugar transporters such as Escherichia coli Sugar efflux transporter SetA, SetB, SetC and other sugar transporters. SetA, SetB, and SetC are involved in the efflux of sugars such as lactose, glucose, IPTG, and substituted glucosides or galactosides. They may be involved in the detoxification of non-metabolizable sugar analogs. The Set family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLLATLLTGLAGAFVLPYLSLFLTEELGASPLQIGIFMTLSALSGIVVSQWLGRLSDRGGDRKPLILLAL
LAGALGYLLFAFLRNYWVLLLVGVVLLSLGAAAFPQLFALAREYADRSSGRDATLFNSVLRAAFSLAWVI
GPPLAFLLLDVLGFTGLFLLAALLYLVVALLVLFLLPSVKPPAQKATPASSLVKAPVNRRLLLLFAAFTL
LFAANSMYIIAMPLYVTNELGGSESWVGLLFGLAAALEIPIMLLAGLLAKRFGKRRLLLAGFLAGVLFYL
GLALATSLWQLIALQLLNAIFIGITAGLGISYFQDLMPGQPGLATTLYSNASRIGSLLGGLLAGVIAQYF
GYRAVFLVCAVLALLALVLLL
>gnl|CDD|341025 cd17472, MFS_YajR_like, Escherichia coli inner membrane transport protein YajR and similar multidrug-efflux transporters of the Major Facilitator Superfamily. This family is composed of Escherichia coli inner membrane transport protein YajR and some uncharacterized multidrug-efflux transporters. YajR is a putative proton-driven major facilitator superfamily (MFS) transporter found in many gram-negative bacteria. Unlike most MFS transporters, YajR contains a C-terminal, cytosolic YAM domain, which may play an essential role for the proper functioning of the transporter. YajR-like transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LSLIFSLRMLGMFLVLPVLSVYAKSLPGATPTLIGLALGIYGLTQAIFQIPFGLLSDRIGRKPVILFGLL
LFIAGSLLAAYATSIYGLILGRALQGSGAISSVVMALLADLTREENRTKAMALIGASIGIAFAISMVLGP
LLAAHLGVSGLFLITAILSLVSLLILLFFVPDPPKIVQISEKEKKKLKKLLKNKRLLRLDFSIFILHFVL
MAFFYILPLLLTQLGGGKGQLWKVYLPAILIGFILMVPFVIYAEKKGKMKQVFVSSILLIAVGFLLLLFA
ATSLWLLIIGLIIFFIGFNLLEALLPSLVSKIAPKEYRGTAMGIYNTSQFLGSFLGGALGGLLWGLLGYS
SVFLTILILALLWLLVSFLLP
>gnl|CDD|341026 cd17473, MFS_arabinose_efflux_permease_like, Putative arabinose efflux permease family transporters of the Major Facilitator Superfamily. This family includes a group of putative arabinose efflux permease family transporters, such as alpha proteobacterium quinolone resistance protein NorA (characterized Staphylococcus aureus Quinolone resistance protein NorA belongs to a different group), Desulfovibrio dechloracetivorans bacillibactin exporter, Vibrio aerogenes antiseptic resistance protein. The biological function of those transporters remain unclear. They belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LITLLLASTLTVMAGAAIAPALPAIAQHFVPNSELLVPLLLTLPALFIALFAPLAGWLADRFGRKRLLIA
GLLLYGIGGVAGLFLDSLYALLASRALLGIGVAGIMTLATALIGDYFEGEERAKMLGLQSAAMSLGGVVF
LLLGGALAEIGWRAPFLVYLLALPVLILVLLFLPEPARKSKSAASPGAATAAALPWKRVLPIYFLAFLAM
LLFYVIPIQLPFLLQERGGGSAALIGLALAIASLAGAIGALLFGRLKRRLGKRRLLAIGFALMALGFLLL
ALASGLWVVLLGAILAGLGFGLLLPTLNSWAMSLVPPELRGRAMGIVTSAFFLGQFLSPLVLGPLVNLTG
GLSGAFLILGVLALVLAIVLLLLR
>gnl|CDD|341027 cd17474, MFS_YfmO_like, Bacillus subtilis multidrug efflux protein YfmO and similar transporters of the Major Facilitator Superfamily. This family is composed of Bacillus subtilis multidrug efflux protein YfmO, bacillibactin exporter YmfD/YmfE, uncharacterized MFS-type transporter YvmA, and similar proteins. YfmO acts to efflux copper or a copper complex, and could contribute to copper resistance. YmfD/YmfE is involved in secretion of bacillibactin. The YfmO-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LYAVFFATLLAVLGVSIVDPILPAIAEALGASPAQVGLLITAFTLPAAVLMPVAGVLADRFGRKKVLLPG
LLLFGIGGLLCGLSDSFALLLAGRALQGIGAAGLGPLALTLIGDLFEGGERAKAMGLYEAALGLGIAVGP
LLGGLLAAISWRYPFFLLAALIPVAFLAILFLLPEPKEKAKSSSATKLRDLKKALRGRGLLTFLVSAFLY
FFLYFAFLTYLPFLLELLYGISPIIIGLLFAGWSVLLALGSLFVGRLLKKRFGARRILVIGLLLYALSLL
LLGFVPSLALLLIAIVLFGLGLGLNLPLLTTLVTELAPEEERGTASSLYNFVRFLGQAVGPLLFGLLLEI
FGLSAPFLVGAAIALAAAVLLALL
>gnl|CDD|341028 cd17475, MFS_MT3072_like, Mycobacterium tuberculosis uncharacterized MFS-type transporter MT3072 and similar transporters of the Major Facilitator Superfamily. This family includes the Mycobacterium tuberculosis uncharacterized MFS-type transporter MT3072. It belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
ATLAQAAASLVAQGIPALAPFLQEDLHLSLAQVGLLLSALNLGVAVSMLPAGWLLDRFGERRVLAVGLLL
MGAAALLMALVGSYPVLLVLLFLVGAGYGSVQPGGGRAIMRWFPPRERGLAMGIRQTGVPLGGALAAALL
PPLALHYGWRAAFVVAGLVSILAAVLFWLFYREPPAASAATESASTLLRSLKEVLRNRDVWLIAIAGALL
VAPQFALLTFLLLFLHDHLGLSVVAAGALLAVAQLGGALGRIGLGRVSDRVFGGRRRPVLVITAAIAAAA
LLVLSLLSPGTPLWLLVLLLILLGLFAIGWNGLYLTLVAESAGPEQAGTALGLANTINFIGIAIGPPLFG
LLVDATHSYAPAWLALALLLVLAALLLL
>gnl|CDD|341029 cd17476, MFS_Amf1_MDR_like, Saccharomyces cerevisiae low affinity ammonium transporter Amf1p/YOR378W, aminotriazole resistance protein Atr1p, and similar transporters of the Major Facilitator Superfamily. Saccharomyces cerevisiae Amf1p/Ammonium Facilitator 1/YOR378W functions as a low affinity NH4+ transporter. S. cerevisiae aminotriazole resistance protein (Atr1p) is required for controlling sensitivity to aminotriazole; it is a putative component of the machinery responsible for pumping aminotriazole (and possibly other toxic compounds) out of the cell. This subfamily also includes S. cerevisiae YMR279C, a putative boron transporter involved in boron efflux and resistance, and Kluyveromyces lactis Knq1p which is involved in oxidative stress response and iron homeostasis. Amf1p, Atr1p, and YMR279C have been classified as group 1 members of the DHA2 (Drug:H+ Antiporter family 2) family, K. lactis Knq1 as group 2. This subfamily also includes two Aspergillus terreus terrein biosynthesis cluster proteins, efflux pump TerG and TerJ which may be required for efficient secretion of terrein or other secondary metabolites produced by the terrein gene cluster. The Amf1p-like subfamily belongs to the Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance (MDR) transporters (MMR-like MDR transporter) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
ATISGAQLLNQAGLGSVIVILPIIGDSFGTSPNQLSWLAASYSLTVGTFILIFGRLGDIYGHKKMFVIGS
FWFAIWSLIAGFSPNFIFFIICRALQGLGPAFLLPNAMALLGRTYPPGPRKNIVFSLFGATAPLGFALGG
VFGGLFAQLAWWPWIFWFLAILAAIVAVAAIFWTSPSFIAVLLAVFLGWASFGIWVFYATQYFQNVRGYS
PLLTSARFIPMAIGGVLAAITVGFLIARLPPSYIMAISMVAFLVGPILFATMPVHQTYWAQAFPAMIVAP
FGMDFSFPAATIIASNAVPREYQGLAGSLVNTVVNYGISIGLGIAGTVETSVNEDGADLLKGYRAAWYLG
IGLAALGLLISV
>gnl|CDD|341030 cd17477, MFS_YcaD_like, YcaD and similar transporters of the Major Facilitator Superfamily. This family is composed of Escherichia coli MFS-type transporter YcaD, Bacillus subtilis MFS-type transporter YfkF, and similar proteins. They are uncharacterized transporters belonging to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLLSVALLGLGSGLLLPLLSLRLEREGVSTALIGLVASAYYLGILLGSPLVPRLIRRVGHIRAFAAGAAI
TAVSVLLLALTDSPWVWFLLRFVMGIGLAGLFVVSESWLNALATNENRGRVLGLYSTVLGLGFALGPLLL
ALVGTAGALPFLIAAVLLLLALVPLLLTRRAAPEIEEAESISLRRLLRIAPLALLGAFVAGFLEGAFYSL
LPLYGLRLGLSVAQAALLLAAFVLGGLLLQWPLGWLADRFDRRRVLLGCALLGALAALLLPLVPGLPLAL
LVLLFLWGGAAGPLYTLALALAGDRLPGDELVAANAALLLLYGLGSVIGPLLAGALMDAFGPHGLFLFLA
AVALLFLLFL
>gnl|CDD|341031 cd17478, MFS_FsR, Fosmidomycin resistance protein of the Major Facilitator Superfamily of transporters. Fosmidomycin resistance protein (FsR) confers resistance against fosmidomycin. It shows sequence similarity with the bacterial drug-export proteins that mediate resistance to tetracycline and chloramphenicol. This FsR family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LSLGHFLNDFYQGFLPALLPLLIAKLGLSYAQAGLLVSVFSITSSLLQPLFGYLADRKPRRYLLPLGPLL
TGLGLSLLGFAPNYWLLLLLVALAGIGSAAFHPEGARLASQAAGGRRGLAMSIFSVGGNLGFALGPLIAA
ALVALFGGLGLLILLIIPGLAVALLLLRLRPLKKPEAKKAAAKSSARSTLKGVWRALLLLLIIVFLRSWV
LSSLTTFLPFYLVQRGYSLVFAGLLLSLFLFAGAIGTLIGGPLSDRFGRRRVIIASLLLAAPFLLLFLLT
PGIWSYILLVLAGFLLFASFPVTVVLAQELLPGNVGLASGLMMGLSFGLGGIGAPVLGALADAFGLESVL
LILALLPLLGALLAF
>gnl|CDD|341032 cd17479, MFS_MFSD6L, Major facilitator superfamily domain-containing protein 6-like and similar transporters of the Major Facilitator Superfamily. Major facilitator superfamily domain-containing protein 6-like (MFSD6L) protein family includes a group uncharacterized proteins similar to human major facilitator superfamily domain-containing protein 6 (MFSD6). MFSD6 is also called Macrophage MHC class I receptor 2 homolog (MMR2). It has been postulated as a possible receptor for human leukocyte antigen (HLA)-B62. The MFSD6L family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
ASLFHFFHSAGKACLLPFLTLYFRQLGLTAPQVGIIIGSKHLISLLWAPFWSFLAKSYRKRRFVILFSLL
ISLGTYLLYHQIFLLVLLVIIIWELLSAPLEKVADDSLYEYLDFVDATERYGKLKVWSALGAAFGPCGIT
LLVDNLDCFLPPKISRILLHFYTYGGFMILTFLLSFFYPIPVPKKEEHSSKVVKGLRLLGGDGRAILYAL
TVFLVGFVGSTVQNFLFWLMQDKGGSELHMGLSIALALLSEILMSFFGNWLLRKLGHAGCVVLGLLGLGA
QLLYYSFLWTPWAVLPIELLHAFSNGALWWAVNSQVEFLASPGMERSLQLVLRALYYGIGFALGSFVSGF
IYDRFGLAILYQACCVVLGLWLIIFA
>gnl|CDD|341033 cd17480, MFS_SLC40A1_like, Solute carrier family 40 member 1 of the Major Facilitator Superfamily of transporters. Solute carrier family 40 member 1 (SLC40A1 or SLC11A3) is also called ferroportin-1 (FPN1) or iron-regulated transporter 1 (IREG1). In the presence of a ferroxidase (hephaestin and/or ceruloplasmin), SLC40A1 acts as an iron exporter ferroportin releases Fe(2+) from cells into plasma, thereby maintaining iron homeostasis. Specially, it is involved in iron export from duodenal epithelial cell and also in the transfer of iron between maternal and fetal circulation. The transport activity of SLC40A1 is suppressed by the peptide hormone hepcidin. This family also includes a bacterial homologue of SLC40A1 (Bdellovibrio bacteriovorus ferroportin). It adopts the major facilitator superfamily fold, but undergoes an intra-domain conformational rearrangement during the transport cycle. SLC40A1 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLYLSHFLSTWGDRMWEFAVPLFLIELFPGSLLPTAVYGLVTALSVIILGPIIGKWVDKTPRLKVVRISL
VLQNISVILSAVLFGLLLLVKSAAASAEGWLLTPLFILLVFFGAIERLASLATNIAVERDWVVVIAGGDS
SALANLNATLRRIDLVCKLLAPLLVGLLMSFVSPVAGALFIAGWNLLSFPPEYFLLRRVYQLQPVFLASL
ALALLYFTVLSFGGILTAYLLSQGGSESVIGLFRGLGAVFGLLGTFVFPWLVKRLGLLRTGLWSIWFQAS
LLLLAVASFFSPSSPFYASVILLLGGIILSRLGLWSFDLAVTQLLQEGVPESERGVINGVQSSLNSLFDL
LSFLLGIIASDPEQFGILVIVSVAAVVLAAILYTRW
>gnl|CDD|341034 cd17481, MFS_MFSD13A, Major facilitator superfamily domain containing 13A. Human major facilitator superfamily domain containing 13A (MFSD1A) protein is also called transmembrane protein 180. Its function is still unknown. MFSD13A belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
VAYGSLAFFLSILHNVFLLYYVDVFVSVYKIDKASFWIGETIFLIWNSLNDPLFGWLSDRKFLSSSSSGA
HISSPAVVLKRLRALSINGPLFALSFLAFWVPWAPPGLQFVVCLCLYDGFLTMVDLNHNALLADLAVSAE
DRTRLNSYCSVFSAIGSLSVFLSYAVWDKENLGSFRIFCACLAIISAVGFFLSSALLNFLWFVVMNLVQV
FHCHFNSNFFPLFLEHLLGDHISPSTGSVLLGISFVAPHLNNLYFLSLCRRYGVYNVVRGLFLIKLGLSL
AMLLAGPDLLWLLCLFIASNRVFTEGTCKLLNLVISDLVDEDYVLNHRKQAISALVFGTAALLSKPGQTL
APLIGTWLLCVQTGSDLFQTGAEPGSIKQQQSSADEASTQTLRQGCFYLLVYVPIVCALIQLLAWSQFTL
HGRRLQYVK
>gnl|CDD|341035 cd17482, MFS_YxiO_like, Bacillus subtilis YxiO, Listeria monocytogenes BtlA, and similar transporters of the Major Facilitator Superfamily. This family is composed of Bacillus subtilis MFS-type transporter YxiO, and similar proteins including Listeria monocytogenes BtlA. The function of B. subtilis YxiO is still unknown, and L. monocytogenes BtlA is a putative secondary transporter involved in bile tolerance and general stress resistance. This family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
WALYDWANSAFATTVTTAVFPVYFKAVAAQGASPVTSTALWGYANSIASLVIALLAPILGAIADYSGRKK
RFLAFFCLIGVVSTALLFFVTPGQWLLALLLFILANIGFSGANVFYDAFLPDVASPERMDRVSSLGYALG
YIGGGLLFAVNLVLILGPDAFGLDTAEAVRLSFLSVALWWALFSIPLKQLLLFLIAYFFYIDGVQTIIRM
ATIYGAEEGKLGSSALILALLLTQFVAFPGALLFGWLAERFGAKRAILVSLVIYILICIYAYFMLTAWDF
WILAALIGLVQGGIQALSRSLFGRLIPKGKSAEFFGFYNISGKFAAIIGPLLFGLITQLTGSSRYGILSL
IVLFVIGGILLA
>gnl|CDD|341036 cd17483, MFS_Atg22_like, Autophagy-related protein 22 and similar proteins; member of the Major Facilitator Superfamily of transporters. Atg22 (also known as Aut4) protein functions as a vacuolar effluxer which mediates the efflux of amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation. Members of this family belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
WYSYGFAAEGFAVVAVGSYLPLLLQQLARDNGVLLSDHSTPCDTSVGSSANDKCVLPIGGGYIDTSSFAL
YVFSISVLLQAVLFISLGSLADYGNYRKRLLLTFTIIGSISSILFLFVPSPSLWWLAALLYIVSNICYGA
SLVFYNSFLPILARNHPDVRAARDKGSSLSAEATEEEISLEEKVSSRISSLGFASGYVGGIIVQIISIII
LFVLGNSIVSLRIAIAVVGVWWLIFSVPTFLWLKPRPGPPLPGGSHPIFYSWKSLFRTLKHARKLPETFI
FLLAWFFLSDGINTISSTAVLFAKSQLHMSTLQLILIGLLTPITAILGAFFFPRIQRRFNLSTKTMLMLI
VVLTALIPLYGLLGFFTGKFGLKHPWEMYVLAVWFGFFLGGLQSYSRSLFSELIPPGHEAEFFSLFSITD
KGSSWIGPLVVGAIIDATGNIRYGFIFLFALFVLPLPLLWFVNVEKG
>gnl|CDD|341037 cd17484, MFS_FBT, Folate-biopterin transporter of the Major Facilitator Superfamily of transporters. The Folate-biopterin transporter (FBT) family includes folate carriers related to those of trypanosomatids in higher plant plastids and cyanobacteria. FBT mediates folate monoglutamate transport involved in tetrahydrofolate biosynthesis. It also mediates transport of antifolates, such as methotrexate and aminopterin. The FBT family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
SVIAVVYFSQGVAGLSWLAVSYYYKDDLHLGPASVQALTSIASLPWAIKPLYGLLSDSVPIFGYRRKPYL
ILAGALGALSWLALALVSNSSLALALLLLLLASLGVAFSDVVIDALVVEASRGAPQSLAGDLQSLCWGSS
AIGGIVGSYFSGYLLELLGPRTVFAVTSFFPLLLLIVAFFVKEERVPPHRTKENFDEQLKALWETVKQPS
IWLPALFIFLYQATPSSGSAMFYFMTNELGFSPEFLGRLRVIGSIASLLGVLLYNRFLKHVPFRKIFFWT
TVLLVLLGLTDLILVTRWNLKLGIPDHAFVLGDDAVVTVIGEILFMPILVLAARLCPPGIEGTVFALLMS
ISNLGSLTSSFLGALLTKALGVTSTNFDNLWLLILICNLSRLLPLLFLF
>gnl|CDD|341038 cd17485, MFS_MFSD3, Major facilitator superfamily domain containing 3 protein. Major facilitator superfamily domain containing 3 protein (MFSD3) is a predicted acetyl-CoA transporter. As an atypical putative membrane-bound solute carrier (SLC), MFSD3 is most likely to be functionally active in the plasma membrane and not in any intracellular organelles. MFSD3 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLFGLYLAQGLPYGFQSQALPVLLRSAGVSLTAIGLLKLLYLPWVLKFLWAPLVDRYGLPRLGRRRSWLL
PTQLGLALLLLALAFLPPTTNLLAFLGLLFLLNLFSATQDIATDGLAVELLTPEERGLGNAAQVVGYKLG
SLLGGGGLLWLYDLIGWQSLLLSLAALYLLLLLPVLFLRELELPQQPPASERGAALKASLRAFLRRPGTR
WLLLFLLLYKLGEQGALAMLPPFLVDRGFSLSQIGLLSGVGGSLVSIAGSLLGGYLLKRRGRRRLLLLGG
LLRLLLLGLYTLLALGGSGLNWVLLLASLALLHLVGGMITTALFTLMMDCSQQAQAGTDYTLLATVEVLG
KLLFGSLAGFLADHLGYAAAFLLFAILSALSVLLLL
>gnl|CDD|341039 cd17486, MFS_AmpG_like, AmpG and similar transporters of the Major Facilitator Superfamily. AmpG acts as an inner membrane permease in the beta-lactamase induction system and in peptidoglycan recycling. It transports meuropeptide from the periplasm into the cytosol in gram-negative bacteria, which is essential for the induction of the ampC encoding beta-lactamase. The AmpG family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
ILLLGFASGLPYLLTGTTLQAWLKEAGVDLDTIGLFSLVGLPYSLKFLWAPLVDRYSTPFLGRRRGWILL
TQILLMAALIALAFLDPFTNLVLSALLFLLVAFFSATQDIAIDAYRIEALEDKEQGAGAGVRVNGYRIGM
LVAGAGALYLADSLSWSAVYLIMAALMGPGILATLFAPEPPRTDPPANSLSETVVAFFAPFKDFFGQPGA
LLILAFILLYKLGDAMLGAMATPFLLDLGFTKTEIGAVYKTVGLIATIVGGLLGGFLMSRLGLKRSLWLF
GILQALSNLGFIYLAHAGPNLTLLVAAVAVENFGGGLGTTAFVAYLMSLCNGEFTATQYALLSSLMALGR
MVLGAPSGWLAEALGWTGFFLLTTLAAIPGLLLLLKV
>gnl|CDD|341040 cd17487, MFS_MFSD5_like, Major facilitator superfamily domain containing 5 protein. Human major facilitator superfamily domain containing 5 protein (MFSD5) is also called molybdate-anion transporter, or molybdate transporter 2 homolog (MOT2). It acts as an atypical solute carrier (SLC) that mediates high-affinity intracellular uptake of the rare oligo-element molybdenum. It may also play a role in maintaining the glucose homeostasis and pancreatic beta-cell proliferation, as well as in altered energy homeostasis. MFSD5 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
FRKFQRRYLVVYLLAMFADWLQGPYLYALYESYGFSEEQIAILFVTGFGSSVVFGTFVGSLADKFGRKRA
CLLFCVLYSLSCLTKHSPNFGVLLLGRVLGGISTSLLFSAFESWMVHEHNKRGFFPKEWLSTTFSKATLG
NGLVAILAGLVANFAEALGFGPVAPFDAAIPFLVLAGVLIMRTWTENYGDPSSPSRLGCQEEALRAILSD
KKVLLLGAIQSLFESAMYIFVFLWTPALDPAQSGGVPLGIIFACFMVAMMIGSSLFRLLLSKRVSPEHLL
VIVLLVASVSLFLPVVSTITSSPKILLLAFLVFEACVGLYFPSMGTLRSKYIPEEHRATVMNLFRVPLNL
LVCVVLLNLHEESFGNRSVFGMCSGLLLVALLLQV
>gnl|CDD|341041 cd17488, MFS_UhpC, Membrane sensor protein UhpC of the Major Facilitator Superfamily of transporters. Membrane sensor protein UhpC acts as both a sensor and a transport protein. It is part of the UhpABC signaling cascade that controls the expression of the hexose phosphate transporter UhpT. UhpC recognizes external glucose-6-phosphate (Glc6P) and induces transport by UhpT. It can also transport and sense Glc6P, and interacts with the histidine kinase UhpB, leading to the stimulation of the autokinase activity of UhpB. This group also includes the hexose phosphate transport protein UhpT from Chlamydia pneumoniae; it is a transport protein for sugar phosphate uptake. It is part of the Organophosphate:Pi antiporter (OPA) family of integral membrane proteins responsible for the transport of specific organophosphates or sugar phosphates across biological membranes with the simultaneous translocation of inorganic phosphate into the opposite direction. The UhpC group belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RIHILASMFIGYAVFYLTRKSFNAAMPAMLADLGLDKSDIGILGSLFYITYGVSKFVSGLMSDRSNPRYF
MGIGLIATGIINILFGFSSSLWAFAVLWTLNAFFQGWGWPPCARLLTHWYSRNERGFWWSIWNTSHNIGG
ALIPILTGFAALTYGWRAGMYVPGIIAILMGIVLCWRLRDRPPYIWLLAFCYVLVYVVRTAINDWGNLYL
SETHGYSLVKANSAVSLFEVGGLIGALVAGWGSDKLFKGNRGPMNLIFALGLLVSVGALWLVPVHSYWLL
ATCFFTIGFFVFGPQMLIGMAAAECSHKDAAGSATGFVGLFAYLGAALAGYPLAKVIESWGWSGFFIVIS
IAAAISGLLLLPLL
>gnl|CDD|341042 cd17489, MFS_YfcJ_like, Escherichia coli YfcJ, YhhS, and similar transporters of the Major Facilitator Superfamily. This subfamily is composed of Escherichia coli membrane proteins, YfcJ and YhhS, Bacillus subtilis uncharacterized MFS-type transporter YwoG, and similar proteins. YfcJ and YhhS are putative arabinose efflux transporters. YhhS has been implicated glyphosate resistance. YfcJ-like arabinose efflux transporters belong to the bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
ILLANFFFFLSFYLLLPVLPLYAHDLGGSEAVAGLVVGLFTLAALLARPFAGRLLDRFGRKRLLLIGLLI
FALATLLYLLATSVALLLVLRLIHGIGWGAFTTAAATLVADIIPPSRRGEGIGYYGLATTLAMALGPALG
LFLYQHLGFAVLFIVAAVLALLALLLVFLVKDPPPVAAEEAEAGTRAFRRLVEKKVLPPALILFLASIAY
GAISTFLPLYAAERGISNAGLFFTVYAIALLLSRPFSGKLSDRKGPKTVIIPGLLLLALGLLLLSFAGSP
WMLLLAAVLYGLGFGLLFPALQALAVDLVPPHRRGAANGTFFIFFDLGIGLGGLLLGLVAELFGYRAMFL
LAAVVVLLALVLYIFLL
>gnl|CDD|341043 cd17490, MFS_YxlH_like, Bacillus subtilis YxlH and similar transporters of the Major Facilitator Superfamily. This subfamily is composed of Bacillus subtilis YxlH uncharacterized MFS-type transporter YxlH and similar proteins. The biological function of YxlH remains unclear. The YxlH-like subfamily belongs to the bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
FLIIVFLFWFSQYVYVPFLSPYAESLGASLSMIGIILGAYGISQMLLRIPLGILSDRIGKRKLFIIIGLL
FTVLASLIMILFPSPWGLLIARFLSGIAAATWVSFTVLYASYFPPDEAAKAMGLINLVNNLGQLIAFLIG
GLIAEHFGMRAPFLLAALAGVLGFILSLFIKEERREKKPVLTELKELLSVLKDKKLLFFSLLAILQQMIT
FSTTFGFTPLIAKQLGASSFQLGLLSIIYLLPNALASLLSGTLFYKKLGERNTIIIGFLLLGAYCFLIPF
APNLTLLYLLQALNGFGTGILFPLLMSLSIEGVPAEQRSTAMGFFQAIYALGMFLGPVLVGIISEAFGLQ
TGFFVIGVIALLAAILSLAYY
>gnl|CDD|341044 cd17491, MFS_MFSD12, Major facilitator superfamily domain-containing protein 12. Major facilitator superfamily domain-containing protein 12 (MFSD12) protein subfamily includes a group of uncharacterized proteins similar to human MFSD2. MFSD2 is composed of two vertebrate members, MFSD2A and MFSD2B. MFSD2A is an LPC symporter that plays an essential role for blood-brain barrier formation and function. MFSD2B is a potential risk or protect factor in the prognosis of lung adenocarcinoma. The MFSD12 subfamily belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
RIAYGVGHVLNDLCASMWFTYLLVYFHLVLGFSSALAGILLLIGQVADAISTPLVGYESDRTNGCGKYGR
RKSWHLIGTICVLLSFPFIFNPCLGCSDSTSEWAKLVYYGPFIIIFQFGWAAVQISHLSLIPELTSDEHE
RVELTALRYAFTVIANITVYLIAWLLLQQSSGDSVNPTSAQDLPIFRNLSLIVVGIGFLFSLLFHLGTKE
PRPPTDLSTTTNEGEEVTAPEEPRLTWKEWLREPQFYQVALLYMCTRLIVNLSQVYIPLYLTETLQLPKE
SIAIVPLVMYVSGFLTSLVMKPINKKIGRKITYLLGLLFVLGFCIWVWFQSGSSRTYEIYGAAVLLGVGS
ATLLVTSLSMTADLIGTNTESGAFVYGAMSFTDKLSNGIAVLIIQSLHPCNTELDECISYYYRVMVVVAG
GVAILAGLLLLAFLLLPK
>gnl|CDD|341212 cd17492, toxin_CptN, type III toxin-antitoxin system toxin CptN and similar proteins. CptN-like toxin component of a type III toxin-antitoxin (TA) system, which consists of a ribonuclease (RNase) toxin that processes its structured and specific cognate RNA antitoxin, which in turn then directly inhibits the toxin. TA systems have been associated with many important phenotypes, like phage resistance, maintenance of genomic islands, and formation of bacterial persister cells
EEGGFYFIKDEFFDKFPDKGLMQNKEKGHKRPCYYAFKDKENKDIYWMIPISSKVEKYKKIYEKKIKKYG
RCDTIHFGKVLGKKSAFLIQNMFPITEKYIDREYTINGNPVVIKKKLIKEIEKKAKKILALEKRGKKLFF
TPDIKKILL
>gnl|CDD|341213 cd17493, toxin_TenpN, type III toxin-antitoxin system toxin TenpN and similar proteins. TenpN-like toxin component of a type III toxin-antitoxin (TA) system, which consists of a ribonuclease (RNase) toxin that processes its structured and specific cognate RNA antitoxin, which in turn then directly inhibits the toxin. TA systems have been associated with many important phenotypes, like phage resistance, maintenance of genomic islands, and formation of bacterial persister cells
MKIVKLTEKFYEDYPHLKEPEILKKKNRPYGVLLIEINGLTFAIPLRSNINHKYGYKFKNTPRSKKKKSG
LDYSKAVIIKDDEYISDENALIDQDEYKKIKKNEKKIVKEFEKYVKKYIKA
>gnl|CDD|341185 cd17494, RMtype1_S_Sma198ORF994P-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Streptococcus macedonicus ACA-DC 198 S subunit (S1.Sma198ORF994P) TRD2-CR2 and Lactobacillus amylovorus GRL 1112 S subunit (S1.LamGRLORF5415P) TRD2-CR2. The recognition sequences of Streptococcus macedonicus ACA-DC 198 S subunit (S1.Sma198ORF994P) and Lactobacillus amylovorus GRL 1112 S subunit (S1.LamGRLORF5415P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. This subfamily of TRD-CR's shows similarity to TRD1-CR1 of Aminobacterium colombiense DSM 12261 S subunit (S.Aco12261I), which recognizes 5'... GCANNNNNNTGT ... 3'. This subfamily may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KKLGEIAEITMGQSPSSKNYNDNPNGLPLVQGNADIKNGKVIPRIWTSEITKTANKGDIILSVRAPVGEV
AKTNFDACIGRGVCAIKGNEFIFLYLYLLNIEGYWSKISQGSTFESINSNDIKNLKISIPSLEEQQKIAT
FLSTLDAEITLLEKKLEKLKQLKKGLLQKLF
>gnl|CDD|341186 cd17495, RMtype1_S_Cep9333ORF4827P-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Crinalium epipsammum S subunit (S.Cep9333ORF4827P) TRD2-CR2 and Corynebacterium genitalium sp. nov. S subunit (S.CgeORF10704P) TRD2-CR2. The recognition sequences for Crinalium epipsammum S subunit (S.Cep9333ORF4827P) and Corynebacterium genitalium sp. nov. S subunit (S.CgeORF10704P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. This subfamily of TRD-CR's shows similarity to TRD1-CR1 of Aminobacterium colombiense DSM 12261 S subunit (S.Aco12261I), which recognizes 5'... GCANNNNNNTGT ... 3'. This subfamily may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
GTLGDIANITMGQSPKGESYNEDGEGLPFYQGVTDFGFRFPTNRVYTTAPTRFAEAGDILFSVRAPVGDI
NIANEKCCIGRGLAAIRSKSGSQSFLFYQLKSLFKEFDIFNGEGTVFGSINKKDLENLPIIIPSDEIIEA
FEKLVSPIDQKIENNEKENRTLAKLRDTLLPKLM
>gnl|CDD|341187 cd17496, RMtype1_S_BliBORF2384P-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Bacillus licheniformis S subunit (S1.BliBORF2384P) TRD1-CR1 and Chlorobium tepidum TLS S subunit (S.CteTORF675P) TRD1-CR1. The recognition sequences for Bacillus licheniformis S subunit (S1.BliBORF2384P) and Chlorobium tepidum TLS S subunit (S.CteTORF675P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. This subfamily of TRD-CR's shows similarity to TRD1-CR1 of Aminobacterium colombiense DSM 12261 S subunit (S.Aco12261I), which recognizes 5'... GCANNNNNNTGT ... 3'. This subfamily may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VKLGDIAEIIMGQSPKGESYNTEGIGIPLLNGPADFGDGYPIPKKWTTKPTKLCKKGDILFCVRGSTTGR
LNIADDEYCIGRGVAAIRPKNGIDTEFLYYLLESNLDYLLAAATGSTFPNISRDDLLNLKIPLPPLEEQK
RIVAILDPLDEKIDKNKQEIEKLEELRDTLLPKLL
>gnl|CDD|341188 cd17497, RMtype1_S_TteMORF1547P-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Thermoanaerobacter tengcongensis S subunit (S.TteMORF1547P) TRD2-CR2. The recognition sequence is undetermined for Thermoanaerobacter tengcongensis S subunit (S.TteMORF1547P). The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This CD contains both TRD1-CR1 and TRD2-CR2. This subfamily of TRD-CR's shows similarity to TRD1-CR1 of Aminobacterium colombiense DSM 12261 S subunit (S.Aco12261I), which recognizes 5'... GCANNNNNNTGT ... 3'. This subfamily may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases. S.TteMORF1547P TRD1-CR1 does not belong to this subfamily
KKLKYVADIIMGQSPPSSTYNTEGIGLPFLQGKAEFGKLYPTPRKWCSAPKKIAEKGDILLSVRAPVGPT
NIADQEYCIGRGLAAIRPKKGLDKKYLLYYLKSIENELSSLGTGSTFKAISKEDLENLLIPLPPLAEQKR
IAAFLDELTAKIDQLIALLEKAIELLKEYRQAVL
>gnl|CDD|341189 cd17498, RMtype1_S_Aco12261I-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Aminobacterium colombiense DSM 12261 S subunit (S.Aco12261I) TRD1-CR1. The S.Aco12261I S subunit recognizes 5'... GCANNNNNNTGT ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. This subfamily may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases. S.Aco12261I TRD2-CR2 does not belong to this subfamily
VKLGEIAEITMGQSPKSEFYNEDGIGLPFLQGNRTFGDKYPYIDTYTTDIKKIAKKGDILMSVRAPVGDL
NIANKDICIGRGLCSIRMKNGNNSFLYYLLKNNIKNLINKSSGTVFGSINKDDIENLEVDIPEDEEQKRI
ANILSKIDDKIEINNQINKNLEELAQAIFKHWF
>gnl|CDD|341190 cd17499, RMtype1_S_CloLW9ORF3270P-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Cecembia lonarensis LW9 S subunit (S.CloLW9ORF3270P) TRD1-CR1 and Bacillus licheniformis 9945A S subunit (S.Bli9945ORF10320P) TRD1-CR1. The recognition sequences for Cecembia lonarensis LW9 S subunit (S.CloLW9ORF3270P) and Bacillus licheniformis 9945A S subunit (S.Bli9945ORF10320P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. This subfamily of TRD-CR's shows similarity to TRD1-CR1 of Aminobacterium colombiense DSM 12261 S subunit (S.Aco12261I), which recognizes 5'... GCANNNNNNTGT ... 3'. This subfamily also includes TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases such as Helicobacter bizzozeronii CIII-1 putative Type IIG restriction enzyme/N6-adenine DNA methyltransferase RM.HbiCORF8670P, and may also contain type I DNA methyltransferases
VRLGDVAEIIMGQSPEGKSYNTNKEGLPFYQGKKEFGDKYIKEPNTWTTSPTKIAEKNDILMSVRAPVGD
VNITTRKICIGRGLAAIRAKKNIDKKYLFYFLLSNKDYFKGKSGGSTFKSINKNQIKNIKIPLPPLEEQK
RIVSELDKLFKLIFEAKNNIEEALANAQQLFKSIL
>gnl|CDD|341191 cd17500, RMtype1_S_MmaGORF2198P_TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Methanosarcina mazei Goe1 S subunit (S.MmaGORF2198P) TRD1-CR1, and Flavobacterium psychrophilum FPG3 S subunit (S.FpsFPG3ORF6820P) TRD1-CR1. The recognition sequences of Methanosarcina mazei Goe1 S subunit (S.MmaGORF2198P) and Flavobacterium psychrophilum FPG3 S subunit (S.FpsFPG3ORF6820P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains TRD1-CR1. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KLEDICIKITSGGTPSRSNKEYYNGGNIPWLKTKELNFKRIYDTEEKITEEGLKNSSAKLIPENTVIIAM
YGAGKTAGRVAINKIPLTTNQACCNLIIDNKKADYRFVYYSLKTQYEELVNLASGAAQQNLNSKLIKNFE
IPLPPLPEQKRIASILSSLDDKIELNNRQNETLEAMAETLFKEWFV
>gnl|CDD|341192 cd17501, RMtype1_S_Vch69ORF1407P_TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Vibrio cholerae 1311-69 S subunit (S.Vch69ORF1407P) TRD2-CR2, and Methanococcoides methylutens MM1 S subunit (S.MmeMM1ORF456P) TRD2-CR2. The recognition sequences of Vibrio cholerae 1311-69 S subunit (S.Vch69ORF1407P) and Methanococcoides methylutens MM1 S subunit (S.MmeMM1ORF456P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VPEGWEVGTILDLCYKTQSGGTPSRKNPEYWDGGIIPWLKTGELRDNIILDTEEKITEEGLKNSSAKLFP
KGTVLVAMYGATAGKLGILAKEATTNQACCALIPKEEYSPFFLYLYLLNSRDYLANLASGSAQQNISQQI
IKNTKVLIPPEDLLEIFNKLVEPLFDKIINNLKENQKLAKLRDTLLPKLMS
>gnl|CDD|341045 cd17502, MFS_Azr1_MDR_like, Saccharomyces cerevisiae Azole resistance protein 1 (Azr1p), and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily. This subfamily is composed of multidrug resistance (MDR) transporters including various Saccharomyces cerevisiae proteins such as azole resistance protein 1 (Azr1p), vacuolar basic amino acid transporter 1 (Vba1p), vacuolar basic amino acid transporter 5 (Vba5p), and Sge1p (also known as Nor1p, 10-N-nonyl acridine orange resistance protein, and crystal violet resistance protein). MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. This subfamily belongs to the Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance (MDR) transporters (MMR-like MDR transporter) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LMLALFLAALDQTIVATALPTIVAEFGGLSLVSWVGTAYLLTSTAFQPIYGKLSDLFGRKWVLLIAIVIF
ELGSLLCGLAPNMTMLIVGRAIQGIGGGGLMSLAFIIIADLVPPRERGKYQGYIGAVFGIASVAGPLIGG
AFTDHLSWRWCFYINLPIGGLALALLRTILLSSIFGFLFGGALFGLIYYLPLYFQLVLGDSATKSGVRLL
PLIIGLVIGSIISGALISKTGRYKPLIVIGTILMSVGAGLLTTLTLDTSKWLLIGYLILLGLGLGIGFQQ
PLVAVQNAVPPADVGVATATNTFFRSLGGTLGVAITDVFLVALALAALAFLLSLFLP
>gnl|CDD|341046 cd17503, MFS_LmrB_MDR_like, Bacillus subtilis lincomycin resistance protein (LmrB) and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily. This subfamily is composed of multidrug resistance (MDR) transporters including Bacillus subtilis lincomycin resistance protein LmrB, and several proteins from Escherichia coli such as the putative MDR transporters EmrB, MdtD, and YieQ. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. For example, MMR confers resistance to the epoxide antibiotic methylenomycin. This subfamily belongs to the Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance (MDR) transporters (MMR-like MDR transporter) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LLLGAFMAILDTTIVNVALPTIMGDLGASLDTVQWVITSYLLALAIMIPLSGWLADRFGTRRLFLTALAL
FTLGSLLCGLAPNLASLIIFRILQGFGGGVLIPLAQTILLRIYPPEKRGAAMGLVGLVILLAPAIGPTLG
GWLTDNLSWRWIFYINLPIGILALLLAPLLDLRLFKDRNFTLGLLLSFLLGLGLFGAMFLLPLYLQNVLG
YSAFESGLVLAPGGLASAILSPLVGRLLDKFGPRLLLLAGLLLLALGTLLLAFLTPDTSLWLIILPLFIR
GLGMGLVFMPLNTLALNSLPPEQIGDATALFNTIRQLGGSIGTALLATLLTNRTQFHHSRLSELLAQQVQ
KQALIIAFNDAFLVSAILLLVGLLLALFLR
>gnl|CDD|341047 cd17504, MFS_MMR_MDR_like, Methylenomycin A resistance protein (also called MMR peptide)-like multidrug resistance (MDR) transporters of the Major Facilitator Superfamily. This subfamily is composed of putative multidrug resistance (MDR) transporters including Chlamydia trachomatis antiseptic resistance protein QacA_2, and Serratia sp. DD3 Bmr3. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. This subfamily belongs to the Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance (MDR) transporters (MMR-like MDR transporter) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement
LALAALAVMLVETMLSPALPTIQREFGTSAAAVSWVLTAYLLVGAVSTPILGRLGDLYGRKKVLLIVLAI
YTAGSLLAAFAPNLPVLIAGRALQGIGGAVFPLAFALVREEFPPERVPVAQGILSATFGIGAGIGLPLGG
WIVQHLGWRWIFWTAAPVAVLLAALVPLIDLRLLRRRNVLLANITALLAGFGMFMVFQLLPQLLQLPTPT
GFGLGITEAGLLLLPGALVMLIAGPLAGRLIARVGPRRVLLIGLVISAVGLLLLALLHSSLWALVVALLL
IGIGLGLAFASLPNIVVESVPPDRTGIATGMNTVLRTIGSAIGPAIAGAILTTYTVSITSGGVPTEGAYV
LAFLIGAALALAALLLSLLIP
>gnl|CDD|340762 cd17505, Ubl_SAMP1_like, ubiquitin-like (Ubl) domain found in small archaeal modifier protein 1 (SAMP1). Ubiquitin-like small archaeal modifier protein 1 (SAMP1) shows a beta-grasp fold of Ub, suggesting that this archaeal Ubl molecule is more closely related to eukaryotic Ub and Ubls than to its prokaryotic counterpart. Several Ub-like structural features such as an N-terminal single lysine residue and di-glycine motif at the C-terminus, spatially isolated, implicate formation of a poly-SAMPylated chainpoly-SAMPylation. SAMP1 can form covalent conjugates with its protein targets through an isopeptide linkage via their C-terminal diglycine motif in a streamlined archaeal E1-dependent pathway. It is involved in sulfur transfer during molybdenum cofactor biosynthesis much like MoaD. This family also includes proteins such as Thermoplasma acidophilum TA0895 and others, all closely related to proteins MoaD
VEVKLYATLREVAGSKEVELDVDGATVGEVLDSLVALYPALEGRLITEDGELAEHVIVLVNGRNIRHLEG
LETPLKDGDTIDLFPPVAGG
>gnl|CDD|340763 cd17506, Ubl_SAMP2_like, ubiquitin-like (Ubl) domain found in small archaeal modifier protein (SAMP2). Ubiquitin-like small archaeal modifier protein 2 (SAMP2) shows a beta-grasp fold of Ub, suggesting that this archaeal Ubl molecule is more closely related to eukaryotic Ub and Ubls than to its prokaryotic counterpart. Several Ub-like structural features such as an N-terminal single lysine residue and di-glycine motif at the C-terminus, spatially isolated, implicate formation of a poly-SAMPylated chainpoly-SAMPylation. SAMP2 can form covalent conjugates with its protein targets through an isopeptide linkage via their C-terminal diglycine motif in a streamlined archaeal E1-dependent pathway. It also forms homo-conjugates through the intermolecular isopeptide bond between the C-terminal Gly and the Lys58 side chain, a feature that likely resembles polyubiquitination. SAMP2 is involved in sulfur transfer during tRNA thiolation much like Urm1. This family also includes uncharacterized proteins such as Methanothermococcus thermolithotrophicus Mth1743, Pyrococcus furiosus PF1061 and others, all closely related to proteins MoaD
ITVILVGAGRMVEIELPEGGATVRDLLRTLSLPPEEVIVVVNGEVVPEDDPLKDGDIIRLIPVVSGG
>gnl|CDD|340861 cd17507, GT28_Beta-DGS-like, beta-diglucosyldiacylglycerol synthase and similar proteins. beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility
VLILTASTGGGHIQAAQALKEAFREKFDNYEVIIEDLLKYSNPVVNKILKRGEKLYKKAPTLYKLFYNLT
SDRLNSISNKAARLGLKKLKELLREEQPDVIISTFPLMSALVELFKRKGLLPIPVYTVITDYVLHSTWIH
PEVDRYFVASEEVKRELVERGVTPSQIKVTGIPVRPSFAEVRDKDEARNELNLSPDKPTVLLMGGGGGMG
PVKETVEALLDSLRAGQVLVVCGKNKKLYEKLSGLEEDYINVRVLGYVDDMNELMAASDLVITKPGGLTI
SEALARGLPVIIYDPIPGQEEENADFLENNGAGIIARDPEELLEIVARLIDPPSLLRMMSEAAKELKPPA
AAKVIADILSLLID
>gnl|CDD|341225 cd17508, Alpha_kinase, Alpha kinase family; uncharacterized subgroup. The alpha kinase family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional serine/threonine protein kinases. The family contains myosin heavy chain kinases, elongation factor-2 kinases, and bifunctional ion channel kinases. These kinases are implicated in a large variety of cellular processes such as protein translation, Mg2+/Ca2+ homeostasis, intracellular transport, cell migration, adhesion, and proliferation. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions
SKLERARIYKFLPPGAFGIAVRKLPFGEGAERNVFRCTEISKEGGTKTATKIGPRLVAKESRHAEDESFD
IKFHKKFCKTQSTAQELAERFNKRLRALPGGPAPRVKFLPCHVYKTKDVSYRGRAWVLVEKELEGKFTKW
NTNAGGVKKSIESVGEGRGESNSSRLRVDDVPQAFSHFTYEHSGGRFLVCDLQGVWNATPDGFLLTDPVI
HHVSGKRHRFGATDKGLEGIRNFLRTHKCSPLC
>gnl|CDD|341226 cd17509, Alpha_kinase, Alpha kinase family; uncharacterized subgroup. The alpha kinase family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional serine/threonine protein kinases. The family contains myosin heavy chain kinases, elongation factor-2 kinases, and bifunctional ion channel kinases. These kinases are implicated in a large variety of cellular processes such as protein translation, Mg2+/Ca2+ homeostasis, intracellular transport, cell migration, adhesion, and proliferation. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions
CVSCANGTNEDMKTTKGRYNDSTEASISVQQLENPFASGTFRWVYKGFYTSGERKGQACVVKWFKSGHVF
EDDYFDGDIKAVDKALEIVNAFNALNRIDKKIKINVPEVWKFGDGLTLWWLGRRVLIEPFIENYEKFNSN
SGWNDDSKGWGEVMQALSHFSYHISGGKYLLCDLQGGVYKNEYVLTDPVILSRTGREYGVTDLGPEGIWN
FFANHKCNKYC
>gnl|CDD|409322 cd17510, T3SC_YbjN-like_2, Uncharacterized protein is structurally similar to type III secretion system chaperones and YbjN family proteins. This family includes an uncharacterized protein from Methanothermobacter Thermautotrophicus that is structurally similar to type III secretion system (T3SS) chaperones (T3SC) that bind effector proteins, and is homologous to YbjN, a putative sensory transduction regulator protein found in Proteobacteria
VKELIKEWLKEEGLKVKEPPDANAEFHFVVKPPPGGPVISVIQPKDKRDRVIIASGIKISPDHQKALSSL
PPEEREEFIWELRKELLFLGVDFRILPPPQEPPQSIQVSKEIYFDGLTKNRFFDSLRKVRNAALLVIWKL
NE
>gnl|CDD|409323 cd17511, YbjN_AmyR-like, YbjN protein family is structurally similar to type III secretion system chaperones. This YbjN protein family includes Escherichia coli YbjN, Erwinia amylovora AmyR, and similar proteins. YbjN proteins share a class I type III secretion chaperone (T3SC)-like fold with type III secretion system (T3SS) chaperone proteins but appear to function independently of the T3SS. YbjN is an enterobacteria-specific protein. In E. coli, it acts as a sensory transduction regulator that may play important roles in regulating bacterial multicellular behavior, metabolism, and survival under stress conditions. E. amylovora AmyR, a functionally conserved ortholog of E. coli YbjN, is a stress and virulence associated protein that regulates the ams operon. Ams proteins are required for amylovoran biosynthesis. AmyR may also regulate the Rcs phosphorelay system, an atypical two-component signal transduction (TCST) system present only in Enterobacteriaceae and positively regulates amylovoran biosynthesis by activating the ams operon transcription
LTLDRLAEILTAAGYTYETKDSDGDPIIRSEGARFRVYFFVCGNGDCESLQFRARFRGPPDVTLELVNRW
NRERRFVKAYLDVDGDVVVEMDVVLDGGVTREQLDDFLRLFLSALLQFFDEL
>gnl|CDD|341193 cd17512, RMtype1_S_BceB55ORF5615P-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Bacillus cereus HuB5-5 S subunit (S.BceB55ORF5615P) TRD2-CR2. The recognition sequence of Bacillus cereus HuB5-5 S subunit (S.BceB55ORF5615P) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WEEIRLGDIIDYQKGYAFKSKDYQDSGIRIVRVSDFTDDSIDINNLVYISEEKANKYKKYELKENDIIIT
TVGSWPSNPDSVVGKVVRVPKEADGALLNQNAVKIRPKKGILDQSFLFYNLKSERFKNYIESIARGNANQ
ASITLGDIKKFKFLLPPLEEQKKIASILSAYDDLIENNEKRIKLLEQMKQALYQE
>gnl|CDD|341194 cd17513, RMtype1_S_AveSPN6ORF1907P_TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Archaeoglobus veneficus SNP6 S subunit (S.AveSPN6ORF1907P) TRD2-CR2 and Bacillus subtilis JRS2 S subunit (S.BsuJRS7ORF3308P) TRD1-CR1. The recognition sequences of Archaeoglobus veneficus SNP6 S subunit (S.AveSPN6ORF1907P) and Bacillus subtilis JRS2 S subunit (S.BsuJRS7ORF3308P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VKLGELGKFIGGGTPSTKNPEYWNGNIPWITSSDLSEDDIFKINIRKFITEEAIKNSATKIIPANSILIV
TRVGVGKVAINPFDICTSQDFTSLIPIKEVNPLFLAYLLYSLLQKLKSQLQGTSIKGITKDDLKNLKIPL
PPLEEQQKIAAILSKLDKLIEAHEKKLEKLKQLKKGLMQKLF
>gnl|CDD|341195 cd17514, RMtype1_S_Eco2747I_MmaC7ORF19P-TRD-CR_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Escherichia coli ST2747 S subunit (S.Eco2747I) TRD2-CR2, Methanococcus maripaludis C7 S subunit (S.MmaC7ORF19P) TRD1-CR1, and related domains. The S. Eco2747I S subunit recognizes 5'... CACNNNNNNNGTTG ... 3'. The recognition sequence of Methanococcus maripaludis C7 S subunit (S.MmaC7ORF19P) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This CD contains both TRD1-CR1 and TRD2-CR2. It also includes the TRD-CR-like domains of putative type II restriction enzymes and methyltransferases, such as Helicobacter cinaedi PAGU611 Hci611ORFHP which may recognize 5'... GAGNNNNNGT ... 3', and type I N6-adenine DNA methyltransferases, such as Calditerrivibrio nitroreducens M.Cni19672ORF1405P whose recognition sequence is undetermined
VKIQDIAFEIINGGTPSRNEPEYWNNGDIPWLTSGETDDNFINNTSEKITTKNGLEDSSIRIVPKGTILI
ACTGQGYTRGQVAVLQIDASTNQAIAAIRCKENVNPKYLYYYLKTQKNNLRNLTSGVAQKNLNIEMLRNL
QIPLPPKEEQQKIVNILETLEFFEKDSLRKIKETAQDINLMIN
>gnl|CDD|341196 cd17515, RMtype1_S_MjaORF132P_Sau1132ORF3780P-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to MjaXIP/S.MjaORF132P TRD1-CR1, S.Sau1132ORF3780P TRD1-CR1, S.Mca353ORF290P TRD1-CR1, and other TRD-CR's. The Staphylococcus aureus subsp. aureus MSHR1132 S subunit (S.Sau1132ORF3780P) recognizes 5'... CAAGNNNNNRTC ... 3', and Moraxella catarrhalis S subunit (S.Mca353ORF290P) recognizes 5'... CAAGNNNNNNTGT ... 3'. The recognition sequence of Methanococcus jannaschii S subunit (MjaXIP/S.MjaORF132P) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.Sau1132ORF3780P-TRD1 recognizes CAAG/CTTG, and S.Sau1132ORF3780P-TRD2 recognizes GAY/RTC. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VKLGDIGKWGSGGTPSRSNPEYYGGGIPWIKSGELNDGYITSTEEKITEEGLKNSSAKLFPKGSVLIAMY
GATAGKVGILGIDAATNQAICAILPNEEIDNEFLFYFLKSQKEYLISLGKGGAQPNISQGIIKNIEIPLP
PLAEQKRIVAKLDKLDKLIEKLEKALEKLEELKKALMQKLL
>gnl|CDD|341197 cd17516, RMtype1_S_HinAWORF1578P-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.HinAWORF1578P TRD2-CR2. Haemophilus influenzae RdAW S subunit (S.HinAWORF1578P) recognizes 5'... CTANNNNNGTTY ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
VKIGDLGKVVTGKTPSTKNPEYFGGDIPFITPSDMKGGKYIIKTERRLSSKGLEKVKNKLIPANSICVTC
IGSDMGKVAITKEPSVTNQQINSIIVNKNKFDPDFVYYLLKNNSKYLKSIAGGSTATPIINKSTFSNIEI
PLPPLPEQKKIAAILSSLDDKIENNRRINKTLEEMAQALFKEWF
>gnl|CDD|341198 cd17517, RMtype1_S_EcoKI_StySPI-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR),similar to Escherichia coli str. K-12 substr. MG1655 S subunit (S.EcoKI) TRD2-CR2, Salmonella enterica subsp. enterica serovar Potsdam S subunit (S.StySPI) TRD2-CR2, and other TRD-CR's. Escherichia coli str. K-12 substr. MG1655 S subunit (S.EcoKI) recognizes 5'... AACNNNNNNGTGC ... 3' and Salmonella enterica subsp. enterica serovar Potsdam S subunit (S.StySPI) recognizes 5'... AACNNNNNNGTRC ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.EcoKI-TRD1 and S.StySPI-TRD1 both recognize AAC/GTT, S.EcoKI-TRD2 recognizes GCAC/GTGC and S.StySPI-TRD2 recognizes GYAC/GTRC. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2.It also includes TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases, such as Pseudomonas putida Jo 4-731 Type IIG restriction enzyme/N6-adenine DNA methyltransferase (RM.PpiI), and type I DNA methyltransferases such as Bacillus cereus BDRD-ST24 M subunit of Type I N6-adenine DNA methyltransferase (M.Bce24ORF51270P). RM.PpiI recognizes 5' ... GAACNNNNNCTC ... 3'
WEVVKLGDLLEDPRYGTSKKSSYDGSGTPVLRIPNIYDGGIDLDDLKKRVDLSEKELEKYLLKKGDILFN
RSNGSPELVGKCALVDEEDEPAIFASYLIRLRLDKKKILPEFLYYYLNSPLGRKQIEKIAKSAAGQANIN
QKDLKKLPIPLPPLEEQKEIVEILESLDSKIDLLEKKLEKLEQLFKSLMQSL
>gnl|CDD|341199 cd17518, RMtype1_S_Asp27244ORF1181P-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Acinetobacter sp. S subunit (S.Asp27244ORF1181P) TRD1-CR1. The recognition sequence of Acinetobacter sp. S subunit (S.Asp27244ORF1181P) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
KKLSDVCFFQEGPGLRNWQFTDEGIKLLNVTNIVNGSLDLDKTDRYISTEEYNGKYKHFLIDEGDILIAS
SGNSWGKVAIVEKDHLPLMLNTSTIRFKFIDGLLDNNFLKYFLNSDYFKEQLDLLITGGAQPNFGPSHLK
KIKIPLPPLEEQKRIAEILDDADDAIEAALEALRKKKQAA
>gnl|CDD|341200 cd17519, RMtype1_S_HpyCR35ORFAP-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Helicobacter pylori CR35 S subunit (S.HpyCR35ORFAP) TRD1-CR1 and Mycoplasma haemofelis str. Langford 1 S subunit (S2.Mha1ORF7190P) TRD1-CR1. The recognition sequences of Helicobacter pylori CR35 S subunit (S.HpyCR35ORFAP) and Mycoplasma haemofelis str. Langford 1 S subunit (S2.Mha1ORF7190P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
EYKTLGEVCKFQNGFAFKSSKYRESGFPIIRITNIQNGKIDTDNLKYFDLNDYKENLDKYIVRPGDIVIA
MSGATTGKVGINLTDQEFYLNQRVGKFIPNEEILNNRYLYHFLLSKQNEKYILAGGSQPNLSSEKLKKIK
IPIPSLEVQEEIVSILDKFRELTNELESELNLRLKQYEYYRDY
>gnl|CDD|341201 cd17520, RMtype1_S_HmoORF3075P-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Heliobacterium modesticaldum Ice1 S subunit (S1.HmoORF3075P) TRD1-CR1. The recognition sequence of Heliobacterium modesticaldum Ice1 S subunit (S1.HmoORF3075P) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This subfamily also includes the TRD-CR-like sequence-recognition domain of type I N6-adenine DNA methyltransferase (M) subunit of Clostridium intestinale URNW (M2.CinURNWORF2828P). The recognition sequence of M2.CinURNWORF2828P is undetermined. Type I methyltransferases included in this group include two domains: one for methylation, and another (TRD-CR-like) for sequence-recognition
VKLKEVAEVFRGKSILKKDIKPGSISVLNISNIEDGEIDYSGMDTIEEEERKVKRYELRDGDLVLSCRGT
AIKVAVFREQKKIVIASANIIVIRPNEKVLSEYLKIFLESPVGTALIKSFQRGTTVMNINHSDIAEMEIP
LLPLEEQKKIAEEYRKERSLYRETVRKAEKRWTEEKEKIY
>gnl|CDD|341202 cd17521, RMtype1_S_Sau13435ORF2165P_TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Staphylococcus aureus NCTC 13435 S subunit (S.Sau13435ORF2165P) TRD2-CR2, Escherichia coli E24377A S subunit (S.EcoE24377ORF286P) TRD1-CR1 and Pseudoalteromonas species P1-13-1a S. subunit (S.Psp1bORF2093P) TRD2-CR2. Staphylococcus aureus NCTC 13435 S subunit (S.Sau13435ORF2165P) recognizes 5'... TCTANNNNNNRTTC ... 3', and the recognition sequences of Escherichia coli E24377A S subunit (S.EcoE24377ORF286P) and Pseudoalteromonas species P1-13-1a S subunit (S.Psp1bORF2093P) are undetermined. The restriction-modification (RM) system S subunit generally consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, Staphylococcus aureus NCTC 13435 S subunit (S.Sau13435ORF2165P) TRD1 recognizes TCTA/TAGA, and -TRD2 recognizes GAAY/RTTC. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. In addition, this family includes RMtype1_S_TRD-CR_like domains of various putative Helicobacter type II restriction enzymes and methyltransferases, such as Hci611ORFHP and HfeORF12890P
WEVKKLGELSEKIQYGYTASAAYEDGGPRYLRITDIQDDGVLWDTVPYCSISEEDAEKYLLKDGDILFAR
TGATVGKSYLYKEDDGKAVFASYLIRFRPNKKKVLPKYLFYFTQSSLYWKQIKSISSGSAQPNINAEKLK
SLKIPLPPLEEQKRIVAILDALDAKIDALEELLEKLEELLKELLQSL
>gnl|CDD|341203 cd17522, RMtype1_S_MjaORF1531P-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Methanocaldococcus jannaschii DSM 2661 S subunit (S.MjaORF1531P/MjaXIIP) TRD1-CR1. The recognition sequence of Methanocaldococcus jannaschii DSM 2661 S subunit (S.MjaORF1531P, also called MjaXIIP) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WKVVKLGDVLEEIRNGTTVKQNKEGGGYPVTRIETISNGTIDLNRVGYAITNEEKIEKYKLQKGDILFSH
INSIEHIGKTAIYDGDPEPLIHGMNLLRLRPNKNIVDPKYLYYLLKSDRFRNQFRSIAKKAVNQASINQT
ELKKIKIPLPPLEEQQKIASILEKLDKKIEKRKEKIEKLKELKKGLFQKL
>gnl|CDD|341204 cd17523, RMtype1_S_StySPI-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Salmonella enterica subsp. enterica serovar Potsdam S subunit (S.StySPI) TRD2-CR2. Salmonella enterica subsp. enterica serovar Potsdam S subunit (S.StySPI) recognizes 5'... AACNNNNNNGTRC ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.StySPI-TRD1 recognizes AAC/GTT and S.StySPI-TRD2 recognizes GYAC/GTRC. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WEWVRLGDLIPEFQNGLSKRGGSDGEPIIVLRLADIKNNKISFENLRRIKLTEKEIEKYSLSKGDLLIIR
VNGSPDLVGRFILFKGYEDVAYCDHFIRMRLDQEKIDPEFLSYIFNSPLIRRKIERNFVTSAGQKTVNQG
HIKSLPIPLPPLKEQKKIVARVEELFALIDQLESSLDLAQQLQNKLAQSI
>gnl|CDD|341205 cd17524, RMtype1_S_EcoUTORF5051P-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Escherichia coli UTI89 S subunit (S.EcoUTORF5051P) TRD2-CR2 and Archaeoglobus fulgidus VC-16 S subunit (S.AfuORF1715P) TRD2-CR2. Escherichia coli UTI89 S subunit (S.EcoUTORF5051P) recognizes 5'... CCANNNNNNNCTTC ... 3' and the recognition sequence of Archaeoglobus fulgidus VC-16 S subunit (S.AfuORF1715P) is undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It also includes TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases, such as Pseudomonas putida Jo 4-731 Type IIG restriction enzyme/N6-adenine DNA methyltransferase (RM.PpiI), and type I DNA methyltransferases such as Bacillus cereus BDRD-ST24 M subunit of Type I N6-adenine DNA methyltransferase (M.Bce24ORF51270P). RM.PpiI recognizes 5' ... GAACNNNNNCTC ... 3'
WEWVTIGDLVTSVQYGTSEKKSEDEGGYPVLRMGNIQDGGIDDDDLKYVDLDEKEFEKYLLKKGDVLFNR
TNSPELVGKTAIFRGDGPATFASYLIRIRLNEEKILPEYLNYFLNSPYGRKQIKSVATQGVGQANINATK
LKAIPIPLPPLEEQKEIVEKLDELDALIDRLEALLEEAEELLESLLQSL
>gnl|CDD|341206 cd17525, RMtype1_S_Eco15ORF14057P-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Escherichia coli 541-15 S subunit (S.Eco15ORF14057P) TRD1-CR1 and Desulfotignum phosphitoxidans S subunit (S.Dph13687ORF2110P) TRD2-CR2. The recognition sequences of Escherichia coli 541-15 S subunit (S.Eco15ORF14057P) and Desulfotignum phosphitoxidans S subunit (S.Dph13687ORF2110P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases
WEWVKLGDILSSTQLGLVRSNSEDPNGYPYIKMGNIGRGGINLLKVETYVDATELEVEKYLLEDGDLLFN
TRNTLELVGKVAIWRGELPKALFNNNILRIRFDDIVLPYFINYYLNSPDGKKQLESIASGTTSVAAIYQK
DLKKLKLPLPPLDEQREIVSFLSELDAKIDQLEQKLEKLLQIKKALMQQL
>gnl|CDD|341207 cd17526, RMtype1_S_Cje2232P-TRD2-CR2_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Campylobacter jejuni RM 2232 S subunit (S.Cje2232P) TRD2-CR2 and Shewanella baltica OS223 S subunit (S.Sba223ORF389P) TRD1-CR1. The recognition sequences of Campylobacter jejuni RM 2232 S subunit (S.Cje2232P) and Shewanella baltica OS223 S subunit (S.Sba223ORF389P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. Also included in this subfamily is the C-terminal TRD-CR-like sequence-recognition domain of Microcystis aeruginosa putative type I N6-adenine DNA methyltransferase M subunit (M.Mae7806ORF3969P). The recognition sequence of M.Mae7806ORF3969P is undetermined
WEVVRLGDIILDIQSGFASGKQNEDEDGVPQLRPHNITTDGELDLDKLIKIVPSPKERKRYLLQKGDVLF
NNTNSQELVGKTALFDGEEPYVFSNHMTRIRVKKSKINPEFLARYLHLLWRSGYFKKLCTNWVNQAGINS
DTLANLKIPLPPLPEQKRIAEILDQIDRLAKALRAEAEALLELAKSLFEDLL
>gnl|CDD|381744 cd17527, HAMP_II, second HAMP domain of aerotaxis transducer Aer2 and similar domains. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established
KSLIAEMQRMSAEHDAGDIDVRIDADKFQGSYREMAEGVNDMVAGH
>gnl|CDD|381745 cd17528, HAMP_III, third HAMP domain of aerotaxis transducer Aer2 and similar domains. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established
IAVKKKAMACVTAFGEGNFDAPLEKFPGKKAFINETIEQVRANL
>gnl|CDD|381746 cd17529, HAMP_I, first HAMP domain of aerotaxis transducer Aer2 and similar domains. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established
GGEPADLAVLAKRFAAGDLDTKIGLPAPDKTSLMASMRRLQRTL
>gnl|CDD|381086 cd17530, REC_RocR, phosphoacceptor receiver (REC) domain of response regulator RocR. The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
LRVLVLDDDPFQCMMAATILEDLGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAES
HSNAAVILMSGLDGGILESAETLAGANGLNLLGTLSKPFSPEELTELLTKYTA
>gnl|CDD|381087 cd17532, REC_LytTR_AlgR-like, phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR. Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ALIVDDEPLAREELRYLLEEHPDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLA
KPPLIVFVTAYDEYAVEAFELNAVDYLLKPFSEERLAEALAKLRKRLS
>gnl|CDD|381088 cd17533, REC_LytTR_AgrA-like, phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA. Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
MNIFILEDDKIQRVRLEEIIENILKIENIEYVIELTGKTEELLEKIKERGKNGIYFLDIDIKMEEKNGLE
VAQKIRKYDPYAIIIFVTTHSEFAPLTFEYKVAALDFILKPLKLEEFKKRIEECIKYAQKN
>gnl|CDD|381089 cd17534, REC_DC-like, phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains. This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
KKILIVEDEAIIALDLKEILESLGYEVVGIADSGEEAIELAEENKPDLILMDINLKGDMDGIEAAREIRE
KFDIPVIFLTAYSDEETLERAKETNPYGYLVKPFNERELKAAIELAL
>gnl|CDD|381090 cd17535, REC_NarL-like, phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators. The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLIVDDHPLVREGLRRLLESEPDIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRY
PDLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA
>gnl|CDD|381091 cd17536, REC_YesN-like, phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators. This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLIVDDEPLIREGLKKLIDWEELGFEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIREL
YPDIKIIILSGYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEELD
>gnl|CDD|381092 cd17537, REC_FixJ, phosphoacceptor receiver (REC) domain of FixJ family response regulators. FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ATVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARG
SNIPIIFITGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL
>gnl|CDD|381093 cd17538, REC_D1_PleD-like, first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains. PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPE
TRHIPVIMITALDDREDRIRGLEAGADDFLSKPI
>gnl|CDD|381094 cd17539, psREC-like_D2_PleD, REC-like adaptor domain (D2) of response regulator PleD. PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain
VLLVDDRPSSAERIAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTR
QLPILAVADPGDRGRLIRALEIGVNDYLVRPIDPNELLARVRTQIRRKRYTDYL
>gnl|CDD|381095 cd17540, REC_PhyR, phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins. PhyR is a hybrid stress regulator that contains an N-terminal sigma-like (SL) domain and a C-terminal REC domain. Phosphorylation of the REC domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. It is involved in the general stress response. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
TRVLIIEDEPLIAMDLEQIVEDLGHQVVGIARTRDEAVALARRERPDLILADIQLADGSSGIDAVNEILT
THDVPVIFVTAYPERLLTGERPEPTFLITKPFDPEMVKAAISQALFF
>gnl|CDD|381096 cd17541, REC_CheB-like, phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins. Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
IRVLIVDDSAVMRKLLSRILESDPDIEVVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMA
ERPTPVVMVSSLTEEGAEITLEALELGAVDFIAKPSGGISLDLEEIAEELIEKIK
>gnl|CDD|381097 cd17542, REC_CheY, phosphoacceptor receiver (REC) domain of chemotaxis protein CheY. The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
KKVLIVDDAAFMRMMLKDILTKAGYEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKI
DPNAKVIMCSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL
>gnl|CDD|381098 cd17544, REC_2_GGDEF, second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins. This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
IKVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIKLVITDYNMPEMDGFELVREIRKK
YSRDQLAIIGISASGDNALSARFIKAGANDFLTKPFLPEEFYCRVTQNLETL
>gnl|CDD|381099 cd17546, REC_hyHK_CKI1_RcsC-like, phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC. This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGG
GRRTPIIALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL
>gnl|CDD|381100 cd17548, REC_DivK-like, phosphoacceptor receiver (REC) domain of DivK and similar proteins. Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPA
TRDIPVIALTAYAMKGDREKILEAGCDGYISKPIDTREFLETVAK
>gnl|CDD|381101 cd17549, REC_DctD-like, phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins. C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPD
LPVILITGHGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL
>gnl|CDD|381102 cd17550, REC_NtrX-like, phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins. NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPD
LPVIMISGHGTIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE
>gnl|CDD|381103 cd17551, REC_RpfG-like, phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins. Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
MRILIVDDNPTNLLLLEALLRSAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRAL
PGLEDVPIVMITADTDREVRLRALEAGATDFLTKPFDPVELLARVRNL
>gnl|CDD|381104 cd17552, REC_RR468-like, phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains. Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
SKRILVIDDEEDIREVVQACLEKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQA
NPETQSIPVILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLLG
>gnl|CDD|381105 cd17553, REC_Spo0F-like, phosphoacceptor receiver (REC) domain of Spo0F and similar domains. Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVID
ENIRVIIMTAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYLP
>gnl|CDD|381106 cd17554, REC_TrrA-like, phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains. Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKK
PDLPVIICTAYSEYKSDFSSWAADAYVVKSSDLTELKETIKRL
>gnl|CDD|381107 cd17555, REC_RssB-like, phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains. Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKES
PDTPVIVVSGAGVMSDAVEALRLGAWDYLTKPIEDLAVLEHAVRRA
>gnl|CDD|381108 cd17557, REC_Rcp-like, phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains. This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
TILLVEDNPGDAELIQEAFKEAGVPNELHVVRDGEEALDFLRGEGEYADAPRPDLILLDLNMPRMDGFEV
LREIKADPDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLGEYW
>gnl|CDD|381109 cd17561, REC_Spo0A, phosphoacceptor receiver (REC) domain of Spo0A. Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
KIKVLIADDNREFVQLLEEYLNSQPDMEVVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLR
RMRLEKRPKIIMLTAFGQEDITQRAVELGASYYILKPF
>gnl|CDD|381110 cd17562, REC_CheY4-like, phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins. CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLP
AYKFTPILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL
>gnl|CDD|381111 cd17563, REC_RegA-like, phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA. Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQ
PDARIVVLTGYASIATAVEAIKLGADDYLAKPADADEILAAL
>gnl|CDD|381112 cd17565, REC_GlnL-like, phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar proteins. Bacillus subtilis GlnL is part of the GlnK-GlnL (formerly YcbA-YcbB) two-component system that positively regulates the expression of the glsA-glnT (formerly ybgJ-ybgH) operon in response to glutamine. It contains a REC domain and a DNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
FYIVDDDKNIIKILSDIIEDDDLGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTG
SNGKFIMISQVSDKEMIGKAYQAGIEFFINKPI
>gnl|CDD|381113 cd17569, REC_HupR-like, phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains. This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERY
PDTVRILLTGYADLDAAIEAINEGEIYRFLTKPWDDEELKETIRQALE
>gnl|CDD|381114 cd17572, REC_NtrC1-like, phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators. NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLP
TSVIVITAHGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKLTK
>gnl|CDD|381115 cd17573, REC_HP-RR-like, phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins. Helicobacter pylori response regulator hp1043 (HP-RR) is an orphan response regulator which is phosphorylation-independent and is essential for growth. HP-RR functions as a cell growth-associated regulator in the absence of post-translational modification. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPS
IVVIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI
>gnl|CDD|381116 cd17574, REC_OmpR, phosphoacceptor receiver (REC) domain of OmpR family response regulators. OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDI
PIIMLTAKDEEEDKVLGLELGADDYITKP
>gnl|CDD|381117 cd17575, REC_WspR-like, phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins. The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
IMVLLVDDQAIIGEAVRRALADEEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRAN
PATRDIPIIVLSTKEEPEVKSEAFALGANDYLVKLPDKIELVARIRYHSRSYINLLQR
>gnl|CDD|381118 cd17580, REC_2_DhkD-like, second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains. Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWL
ANTPAIALTGYGQPEDRERALEAGFDAHLVKPVDPDELIELI
>gnl|CDD|381119 cd17581, REC_typeA_ARR, phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and similar proteins. Type-A response regulators of Arabidopsis (ARRs) are involved in cytokinin signaling, which involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Type-A ARRs function downstream of and are regulated by type-B ARRs, which are a class of MYB-type transcription factors. As primary cytokinin response genes, type-A ARRs act as redundant negative feedback regulators of cytokinin signaling by inactivating the phosphorelay. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-A ARRs are similar in domain structure to CheY, in that they lack a typical output domain and only contain a stand-alone receiver (REC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEEDSSNFNEPKVNMIITDYCMPGMTGYD
LLKKVKESSALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLADVKRL
>gnl|CDD|381120 cd17582, psREC_PRR, pseudo receiver domain of pseudo-response regulators. In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions
VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEIDLILTEVDLPVSSGFKLLSYIMRHK
ICKNIPVIMMSSQDSVGVVFKCLSKGAADYLVKP
>gnl|CDD|381121 cd17584, REC_typeB_ARR-like, phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains. Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDEFDLVITDVHMPDMDGFEFLELIRLEM
DLPVIMMSADGSTSTVMKGLAHGACDYLLKPVSIEDLKNIWQHVV
>gnl|CDD|381122 cd17586, REC_PFxFATGY, phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response regulators. This subfamily is composed of stand-alone response regulators (RRs) containing the PFxFATG[G/Y] motif; RRs with such a motif are also called ''FAT GUY'' response regulators. Included in this subfamily are Sphingomonas melonis SdrG, Sinorhizobium meliloti Sma0114, and Erythrobacter litoralis EL_LovR. SdrG is involved in the control of the general stress response. Sma0114 is part of the Sma0113/Sma0114 two-component system (TCS) that is involved in catabolite repression and polyhydroxy butyrate synthesis. EL_LovR is involved in a light-regulated TCS. PFxFATG[G/Y] RRs are typically associated with histidine-tryptophan-glutamate (HWE) histidine kinases that constitute a subclass of the larger histidine kinase superfamily characterized by an altered ATP binding site, which lacks the F-box that is normally an integral component of the ATP lid. The PFxFATG[G/Y] motif is involved in conformational changes after phosphorylation that results in the activation of the RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLVLEDEPLIAMNLEDALEDLGGKEVVTAATCAEALRSLADGPIDIAILDVNLGGETSIPVADALKRRAI
PFIFATGYGDSHGIDSRLIDVPVLRKPFDADSALAALAMLL
>gnl|CDD|381123 cd17589, REC_TPR, phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR)-containing response regulators. Response regulators share the common phosphoacceptor REC domain and different output domains. This subfamily contains uncharacterized response regulators with TPR repeats as the effector or output domain, which might contain between 3 to 16 TPR repeats (each about 34 amino acids). TPR-containing proteins occur in all domains of life and the abundance of TPR-containing proteins in a bacterial proteome is not indicative of virulence. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members in this subfamily may contain inactive REC domains lacking canonical metal-binding and active site residues
FLIVDDQPTFRSMLKSMLRSLGVTRIDTASSGEEALRMCENKTYDIVLCDYNLGKGKNGQQLLEELRHKK
LISPSTVFIMVTGESSRAMVLSALELEPDDYLLKPFTVSELRERL
>gnl|CDD|381124 cd17593, REC_CheC-like, phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain. This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
MKVLICDDSSMARKQLARALPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVE
QLETKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEELG
>gnl|CDD|381125 cd17594, REC_OmpR_VirG, phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators. VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSD
VPIIIISGDRRDEIDRVVGLELGADDYLAKPFGLRELLARVRA
>gnl|CDD|381126 cd17595, REC_TrxB, phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase output domain. This family is composed of uncharacterized fusion proteins containing a REC domain and a thioredoxin reductase domain. Thioredoxin reductase catalyzes the reduction of thioredoxin and is thus a central component in the thioredoxin system. Fusion proteins containing REC and thioredoxin reductase domains could play an important role in the environmental regulation of the cellular dithiol-disulfide ratio. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
PIILTVDDDPQVLRAVARDLRRQYGKDYRVLRADSGAEALDALKELKLRGEAVALFLVDQRMPEMDGVEF
LEKAMELFPEAKRVLLTAYADTDAAIRAINDVQLDYYLLKPWDPPEEKLYPVLDDLLDDWQASYR
>gnl|CDD|381127 cd17596, REC_HupR, phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR). Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
PTILVVDDEVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWP
EVVRIIISGYTDSEDIIAGINEAGIYQYLTKPWHPDQLLLTVRNAARLFELQRENERLSLELR
>gnl|CDD|381128 cd17598, REC_hyHK, phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators. Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase/response regulators contain all the elements of a classical TCS in a single polypeptide chain. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDL
KDIPVILLTTLSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYILVN
>gnl|CDD|381129 cd17602, REC_PatA-like, phosphoacceptor receiver (REC) domain of PatA and similar domains. Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues
VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSAL
KDTPIIMLTGKDGLVDRIRAKMAGASGYLTKP
>gnl|CDD|381130 cd17614, REC_OmpR_YycF-like, phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators. YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNV
PIIMLTAKDSEVDKVLGLELGADDYVTKPFSNRELLARVKANLRR
>gnl|CDD|381131 cd17615, REC_OmpR_MtPhoP-like, phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators. Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGP
DVPVLFLTAKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALLRRS
>gnl|CDD|381132 cd17616, REC_OmpR_CtrA, phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators. CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVK
TPILILSGLADIEDKVKGLGFGADDYMTKPFHKDELVARIHAIV
>gnl|CDD|381133 cd17618, REC_OmpR_PhoB, phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family. The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDE
MTRDIPIIMLTARGEEEDKVRGLEAGADDYITKPFSPRELVARIKAVL
>gnl|CDD|381134 cd17619, REC_OmpR_ArcA_TorR-like, phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators. This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQS
EVGIILVTGRDDEVDRIVGLEIGADDYVTKPFNPRELLVRAKN
>gnl|CDD|381135 cd17620, REC_OmpR_KdpE-like, phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators. KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSAV
PVIVLSARDEESDKIAALDAGADDYLTKP
>gnl|CDD|381136 cd17621, REC_OmpR_RegX3-like, phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators. RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSNV
PVIMVTAKDSEIDKVVGLELGADDYVTKP
>gnl|CDD|381137 cd17622, REC_OmpR_kpRstA-like, phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators. Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
TRILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKY
QGPILLLTALDSDIDHILGLELGADDYVVKPVEPAVLLARLRALLR
>gnl|CDD|381138 cd17623, REC_OmpR_CpxR, phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators. CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQV
PVLMLTARGDDIDRILGLELGADDYLPKPFNPRELVARIRAILRR
>gnl|CDD|381139 cd17624, REC_OmpR_PmrA-like, phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators. This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQS
LPVLILTARDGVDDRVAGLDAGADDYLVKPFALEELLARLRALLR
>gnl|CDD|381140 cd17625, REC_OmpR_DrrD-like, phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators. DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIET
PVLLLTALDAVEDRVKGLDLGADDYLPKPFSLAELLARIRALLRR
>gnl|CDD|381141 cd17626, REC_OmpR_MtrA-like, phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators. MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAES
GVPIVMLTAKSDTVDVVLGLESGADDYVAKPFKPKELVARIRARL
>gnl|CDD|381142 cd17627, REC_OmpR_PrrA-like, phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators. The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGND
LPILVLTARDSVSDRVAGLDAGADDYLVKPFALEELLARVRALLRR
>gnl|CDD|341285 cd17630, OSB_MenE-like, O-succinylbenzoic acid-CoA ligase. This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors
RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELV
LLERNQALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYT
TYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVEDGEIWVGGASLAMGYLRGQLVPEFNEDGWFTTK
DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA
DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL
>gnl|CDD|341286 cd17631, FACL_FadD13-like, fatty acyl-CoA synthetase, including FadD13. This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway
LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGA
VFVPLNFRLTPPEVAYILADSGAKVLFDDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDD
VLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATT
DLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIV
DPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGG
ENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVE
FVDALPRNATGKILK
>gnl|CDD|341287 cd17632, AFD_CAR-like, adenylation domain of carboxylic acid reductase (CAR). This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids
DPQFAAAAPLEAVTEAIRRPGLRLAQIIATVMTGYADRPALGQRATELVTDPATGRTTLRLLPRFETITY
AELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETE
PRLLAVSAEHLDLAVEAVLEGGTPPRLVVFDHRPEVDAHRAALESARERLAAVGIPVTTLTLIAVRGRDL
PPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLNFMPMSHIAGR
ISLYGTLARGGTAYFAAASDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAER
VKAELRERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGAVILDGVIVRPPVLDYKLVD
VPELGYFRTDRPHPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVL
KLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDTARLRAALAESLQRIARE
AGLQSYEIPRDFLIETEPFTIANGLLSG
>gnl|CDD|341288 cd17633, AFD_YhfT-like, fatty acid-CoA ligase VraA. This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFI
GQRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLI
EFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGGFSNPDGWM
SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD
KLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR
>gnl|CDD|341289 cd17634, ACS-like, acetate-CoA ligase. This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
YETKYRQSINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLRENGDRT
AIIYEGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIF
GGFAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQEGRD
LWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCT
ADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEG
TDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGV
QPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITG
RSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVR
KEIGPLATPDVVHWVDSLPKTRSGKIM
>gnl|CDD|341290 cd17635, FADD10, adenylate forming domain, fatty acid CoA ligase (FadD10). This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A
EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGL
CVTGGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEAT
GLTNTAQVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGY
WNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEI
SDEEFGELVGLAVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR
>gnl|CDD|341291 cd17636, PtmA, long-chain fatty acid CoA ligase (FadD). This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions
DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNV
FVRRVDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKP
GGYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVN
ARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQ
SVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD
>gnl|CDD|341292 cd17637, ACLS-CaiC, acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II. This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions
DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANV
VMEKFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAPETIQRFEETTGATFW
SLYGQTETSGLVTLSPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTA
YTFRNGWHHTGDLGRFDEDGYLWYAGRKPEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWG
EGIKAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR
>gnl|CDD|341293 cd17638, FadD3, acyl-CoA synthetase FadD3 and similar proteins. This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used
DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATV
VPVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELG
FETVLTAYGLTEAGVATMCRPGDDAETVATTCGRACPGFEVRIADDGEVLVRGYNVMQGYLDDPEATAEA
IDADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVG
KAFVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK
>gnl|CDD|341294 cd17639, LC_FACS_euk1, Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins. The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate
GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALI
HSLNETECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPDDRYLAYLPL
AHIFELAAENVCLYRGGTIGYGSPRTLTDKSKRGCKGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGG
LKRTLFWTAYQSKLKALKEGPGTPLLDELVFKKVRAALGGRLRYMLSGGAPLSADTQEFLNIVLCPVIQG
YGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPPRGEILIRGPNVFKGYYKNPEK
TKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKS
YPVAIVVPNEKHLTKLAEKHGVINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEWT
PENGLVTAAQKLKRKEI
>gnl|CDD|341295 cd17640, LC_FACS_like, Long-chain fatty acid CoA synthetase. This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions
KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELL
YILNHSESVALVVENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWH
SYERSAEYFIFACGCSQAYTSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFL
SGGIFKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDP
EGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSN
GENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGALIVPNFEELEKWAKESGVKLANDRSQLLASKKVLKL
YKNEIKDEISNRPGFKSFEQIAPFALLEEPFIENGEMTQTMKIKRNVV
>gnl|CDD|341296 cd17641, LC_FACS_bac1, bacterial long-chain fatty acid CoA synthetase. The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions
LREKDFGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDS
MAEEVAYLLNYTGARVVIAEDEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPRLISFEDVVALGRAL
DRRDPGLYEREVAAGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPW
IGEQMYSVGQALVCGFIVNFPEEPETMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFEL
GMKLGLRALDRGKRGRPVSLWLRLASWLADALLFRPLRDRLGFSRLRSAATGGAALGPDTFRFFHAIGVP
LKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEVGEILVRSPGVFVGYYKNPEATAEDFDEDG
WLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRPYLTAFICIDY
AIVGKWAEQRGIAFTTYTDLASRPEVYELIRKEVEKVNASLPEAQRIRRFLLLYKELDADDGELTRTRKV
RRGVIAEKY
>gnl|CDD|341297 cd17642, Firefly_Luc, insect luciferase, similar to plant 4-coumarate: CoA ligases. This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light
IIVGPGPFYPLEDGTAGEQLHKAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQND
RIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKII
KTIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIV
ARFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSAL
LVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTETTSAILITPEGD
DKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYY
DEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEK
EVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI
>gnl|CDD|341298 cd17643, A_NRPS_Cytc1-like, similar to adenylation domain of cytotrienin synthetase CytC1. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPA
YPVERIAFILADSGPSLLLTDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTLF
HSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPL
ALRYVIFGGEALEAAMLRPWAGRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLR
VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEY
LGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKE
LLPDYMVPARYVPLDALPLTVNGKLDRAAL
>gnl|CDD|341299 cd17644, A_NRPS_ApnA-like, similar to adenylation domain of anabaenopeptin synthetase (ApnA). This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAI
LKAGGAYVPLDPNYPQERLTYILEDAQISVLLTQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIK
EYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHL
LVLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNI
TSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSESERLYKT
GDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYE
ESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRALP
>gnl|CDD|341300 cd17645, A_NRPS_LgrA-like, adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin
HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLK
AGGAYVPIDPDYPGERIAYMLADSSAKILLTNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYF
GVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAEQFM
QLDNQSLRVLLTGGDKLKKIERKGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEAL
QLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVK
IRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYF
VHLKALPLTANGKVDRKALP
>gnl|CDD|341301 cd17646, A_NRPS_AB3403-like, Peptide Synthetase. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLK
AGAAYLPLDPGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNL
AYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVA
RPGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAE
LHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLG
RPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHA
VVVARAAPAGAARLVGYVVPAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL
>gnl|CDD|341302 cd17647, A_NRPS_alphaAR, Alpha-aminoadipate reductase. This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate
FPERTCVVETPSLNSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGA
TFSVIDPAYPPARQNIYLGVAKPRGLIVIRAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPW
MAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAM
GQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVPSRSSDPTFL
KNLKDVMPAGRGMLNVQLLVVNRNDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDH
WNYLDKDNNEPWRQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLV
RENITLVRRDKDEEPTLVSYIVPRFDKPDDESFAQEDVPKEVSTDPIVKGLIGYRKLIKDIREFLKKRLA
SYAIPSLIVVLDKLPLNPNGKVDKPKLQFP
>gnl|CDD|341303 cd17648, A_NRPS_ACVS-like, N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase. This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase
PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDP
SYPDERIQFILEDTGARVVITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAV
LFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLARLPHLK
RVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMK
RVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQERARGRNARLYKTGDLVRWLPSGELEYLG
RNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQKYLVGYYLPEPGHVPESDLLSFL
RAKLPRYMVPARLVRLEGIPVTINGKLDVRALP
>gnl|CDD|341304 cd17649, A_NRPS_PvdJ-like, non-ribosomal peptide synthetase. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPE
YPAERLRYMLEDSGAGLLLTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQ
FASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGR
PPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAY
ILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLG
RVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRTALRAS
LPDYMVPAHLVFLARLPLTPNGKLDRKALP
>gnl|CDD|341305 cd17650, A_NRPS_PpsD_like, similar to adenylation domain of plipastatin synthase (PpsD). This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPD
YPAERLQYMLEDSGAKLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQ
MASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDL
SAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTA
MYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELL
GRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELP
SYMIPSYYVQLDALPLTPNGKVDRRAL
>gnl|CDD|341306 cd17651, A_NRPS_VisG_like, similar to adenylation domain of virginiamycin S synthetase. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGA
AYVPLDPAYPAERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAY
VIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPE
EVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGLPG
LRLHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARG
YLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGV
REAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL
P
>gnl|CDD|341307 cd17652, A_NRPS_CmdD_like, similar to adenylation domain of chondramide synthase cmdD. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid)
PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPA
YPAERIAYMLADARPALLLTTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQF
ASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLPDLRTLV
VAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGV
PGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRI
ELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLD
ALPLTPNGKLDRRALP
>gnl|CDD|341308 cd17653, A_NRPS_GliP_like, nonribosomal peptide synthase GliP-like. This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKA
GAAYVPLDAKLPSARIQAILRTSGATLLLTTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPAR
LDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHVARTVDALMSTPSILSTLSPQDFPN
LKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPV
PEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRG
FRINLEEIEEVVLQSQPEVTQAAAIVVNGRLVAFVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPL
TANGKVDRKALRE
>gnl|CDD|341309 cd17654, A_NRPS_acs4, acyl-CoA synthetase family member 4. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
PDRPALIIDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAP
IDPASPEQRSLTVMKKCHVSYLLQNKELDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPH
KCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRHR
ITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILSSWRGKGNRTRIFNIYGITEVSCW
ALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLNRVCILDDEVTVPKGTMRATGDFVTVK
DGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIVGESSSSRIHKELQLTL
LSSHAIPDTFVQIDKLPLTSHGKVDKSEL
>gnl|CDD|341310 cd17655, A_NRPS_Bac, bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKA
GGAYLPIDPDYPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLA
YVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVR
KETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPT
ITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYL
NRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKE
AVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEPD
>gnl|CDD|341311 cd17656, A_NRPS_ProA, gramicidin S synthase 2, also known as ATP-dependent proline adenylase. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions
TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDP
EYPEERRIYIMLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTT
GKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQ
LFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGP
SETHVVTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAE
KFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKAD
DKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP
>gnl|CDD|350495 cd17657, CDC14_N, N-terminal domain pseudophosphatase domain of CDC14 family proteins. The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif. The N-terminal pseudophosphatase domain lacks the catalytic residues
SAIEIIPDRLYFASLRGPPKSTDNTHYFSIDDELVYEPFFADFGPLNLAQIYRFCCKLNKKLKSPSLASK
KIVHYTSLDPKKRANAAFLIGAYAVIYLGKTPEEAYRPLESGEPPFLPFRDASYGPCTYELTVLDCLKGL
EKAL
>gnl|CDD|350496 cd17658, PTPc_plant_PTP1, protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs. Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response
YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAKCADYFPAEENES
REFGRISVTNKKLKHSQHSITLRVLEVQYIESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIP
PSAGPIVVHCSAGIGRTGAYCTIHNTIRRILEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA
>gnl|CDD|350497 cd17659, PTP_paladin_1, protein tyrosine phosphatase-like domain of paladin, repeat 1. Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 1
EHYLIQGKYFLVKDVFSGIDILGTLKKYGAPNFRQAGGGYPVYGMGQPSLDGLKRVLEKLQTRGHKEIIF
FNLREEPVLFLSLEEDFVPYSPRAYRYHRLPLPEDGAPLEIQFDAFVNVLRENPSLSDAIGLLPALLFSC
QPGVGRTNLAMVLGTLVLGHKHGTTSEATNASDYENGEPKIIFQVIQVFINKLLPALIFNCHVPQGRTTV
EEVDRAIILC
>gnl|CDD|350498 cd17660, PTP_paladin_2, protein tyrosine phosphatase-like domain of paladin, repeat 2. Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 2
GDLITKGTRVLVEDERLSPDVLSTYKEMKVANFRRVPKMPIYGMAQPSSEALGVVLAYLTDAKRKHSKVL
WVNLREELVLEANGQTFSPREPGNLEQLIPVGLTYRRIPIPDFCAPREEDFDRLLEAMKSALAEDSGTAF
VFNCLDGKGRTTTAMVIAVLTLWHFNGFPEGTEDEIVSVPDAKYTKGEFEVVMKVVRLLPDGHRMKREVD
AALDSV
>gnl|CDD|350499 cd17661, PFA-DSP_Oca2, atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 2. Oxidant-induced cell-cycle arrest protein 2 (Oca2) is an atypical dual specificity phosphatase of unknown function. It has been identified as a putative negative regulator acting on cell wall integrity and mating MAPK pathways in yeast. It belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs). Oca2 may be an inactive DSP-like protein as it lacks the CxxxxxR catalytic motif
VPPLNFSLVADGIYRSGHPMPINYPFLKQLNLKTIIYLGDKDPYRQDYLDFLQSQGIELYYFDFSSSSEP
FTEEDQERMEQALKLLLDKRNYPILVHSNKGKHRVGVLVGIMRKLLQGWCLAGIFDEYGRFAGGKGETDL
EFIETF
>gnl|CDD|350500 cd17662, PFA-DSP_Oca4, atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 4. Oxidant-induced cell-cycle arrest protein 4 (Oca4) is an atypical dual specificity phosphatase of unknown function. It belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs). Oca4 may be an inactive DSP-like protein as it lacks the CxxxxxR catalytic motif
LVPPANFGIVEPGIYRCSKLSTLNFSFLETLNLKTIVFVGGQEPSKFFKEFFERNNIELIVLRDADFSNH
HHPGKNSSSGKLQGNTDVNDLEPINTNYHLWKNDLDMLIKSTLLQRIFEKNLPVLNHNKLLVDKTSTVIG
CLRRIQKWNFSSIINEYRRFAGKSSNYFAETFLELFD
>gnl|CDD|350501 cd17663, PFA-DSP_Oca6, atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 6. Oxidant-induced cell-cycle arrest protein 6 (Oca6) is an atypical dual specificity phosphatase of unknown function. It belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs). Oca6 may be an inactive DSP-like protein as it lacks the CxxxxxR catalytic motif
IPPFRFATVEPGLYRGAYPRLKNFRFLRRLKLKTIVSLTPEPPTEDLANFCEAENITLIHISAEKFKKGK
VPLSYSTVIQILQLLIDKDNLPVYIHCLDGRHVTGLVVACLRKLQFWSSIAIFAEFLRFARTISSEERAF
IENFKGEIEVPANKPKWLWGGV
>gnl|CDD|350502 cd17664, Mce1_N, N-terminal triphosphatase domain of mRNA capping enzyme. mRNA capping enzyme, also known as RNA guanylyltransferase and 5'-phosphatase (RNGTT) or mammalian mRNA capping enzyme (Mce1) in mammals, is a bifunctional enzyme that catalyzes the first two steps of cap formation: (1) by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end using the polynucleotide 5'-phosphatase activity (EC 3.1.3.33) of the N-terminal triphosphatase domain; and (2) by transferring the GMP moiety of GTP to the 5'-diphosphate terminus through the C-terminal mRNA guanylyltransferase domain (EC 2.7.7.50). The enzyme is also referred to as CEL-1 in Caenorhabditis elegans
RWLNCPRKGQPVAGKFLPFKTPLGPRYDDQVPEENRFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNE
VEKEGCKYIKLQCKGHGECPSPEQTETFIRLCENFIEKNPLELIGVHCTHGFNRTGFLICAYLVEKMDWS
VEAAVATFAQARPPGIYKGDYLKELFR
>gnl|CDD|350503 cd17665, DSP_DUSP11, dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins. dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus
RWIDYLPVGQRIPGTRFIAFKVPLRKSFFANLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPR
DLTNHGVYYKKITCPGHQVPDDKTIQSFKDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLICRYLIDVDG
MSPDDAIEAFEQARGHPIERENYLEDLLK
>gnl|CDD|350504 cd17666, PTP-MTM-like_fungal, protein tyrosine phosphatase-like domain of fungal myotubularins. Myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. Not all members are catalytically active proteins, some function as adaptors for the active members
QRIPVLTYLHKANGCSITRSSQPLVGLKQNRSIQDEKLVSEIFNTSINEIYISPQKNLIVDARPTTNAMA
QVALGAGTENMDNYKYKTAKKIYLGIDNIHVMRDSLNKVTEALKDGDDSNPSYPPLINALKKSNWLKYLA
IILQGADLIAKSIHFNHSHVLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFAER
SGHKETSPVFHQFLDCVYQ
>gnl|CDD|350505 cd17667, R-PTPc-G-1, catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1. Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1)
FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNK
AKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHA
CYTVRRFSIRNTKVKKGQKGNPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVL
VHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL
>gnl|CDD|350506 cd17668, R-PTPc-Z-1, catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1. Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1)
YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGN
FLVTQKSVQVLAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYA
KRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV
>gnl|CDD|350507 cd17669, R-PTP-Z-2, catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2. Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2)
YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCET
FKVTLIAEEHKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRD
GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL
>gnl|CDD|350508 cd17670, R-PTP-G-2, PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2. Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2)
YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEA
FTVTLISKDRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRD
GPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS
>gnl|CDD|439038 cd17671, RUN, RUN domain. RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways
KAVKELLESFADNGEADDSAALTLTDDDPVVGRLCAALEAILSHGLKPKRFGGGKVSFWDFLEALEKLLP
APSLKQAIRDINSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRDPEEAELF
LSLLVGLSSLDFNL
>gnl|CDD|349491 cd17672, MDM2, p53-binding domain found in E3 ubiquitin-protein ligase MDM2 and similar proteins. MDM2, also known as double minute 2 protein (Hdm2), or oncoprotein MDM2, or p53-binding protein, exerts its oncogenic activity predominantly by binding the p53 tumor suppressor and blocking its transcriptional activity. It forms homo-oligomers and displays E3 ubiquitin ligase activity, catalyzing the attachment of ubiquitin to p53 as an essential step in the regulation of its expression levels in cells. Moreover, in response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through the interaction with ribosomal proteins L5, L11, and L23. MDM2 also has a p53-independent role in tumorigenesis and cell growth regulation. In addition, it binds interferon (IFN) regulatory factor-2 (IRF-2), an IFN-regulated transcription factor, and mediates its ubiquitination. MDM2 contains an N-terminal p53-binding domain and a C-terminal zinc RING-finger domain conferring E3 ligase activity that is required for ubiquitination and nuclear export of p53. It is also responsible for the hetero-oligomerization of MDM2, which is crucial for the suppression of P53 activity during embryonic development, and the recruitment of E2 ubiquitin-conjugating enzymes. MDM2 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain, as well as a nuclear localization signal (NLS) and a nuclear export signal (NES), near the central acidic region
EKLVRPKPLLLKLLKSAGAQKDTFTMKEVLFYLGQYIMAKQLYDEKQQHIVHCSNDPLGDLFGVQSFSVK
EHRRIYAMISRNL
>gnl|CDD|349492 cd17673, MDM4, p53-binding domain found in MDM4 and similar proteins. MDM4, also known as double minute 4 protein, MDM2-like p53-binding protein, protein MDMX, HDMX, or p53-binding protein MDM4, exerts its oncogenic activity predominantly by binding the p53 tumor suppressor and blocking its transcriptional activity. MDM4 is phosphorylated and destabilized in response to DNA damage stress. It can also be specifically dephosphorylated through directly interacting with protein phosphatase 1 (PP1), which may increase its stability and thus inhibit p53 activity. MDM4 also has a p53-independent role in tumorigenesis and cell growth regulation. MDM4 contains an N-terminal p53-binding domain and a C-terminal zinc RING-finger domain responsible for its hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. MDM4 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region
PKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDKQQQHIVYCGGDPLGELLGVQSFSVKDPSPL
YDMLKRNLV
>gnl|CDD|349493 cd17674, SWIB_BAF60A, SWIB domain found in BRG1-associated factor 60A (BAF60A) and similar proteins. BAF60A, also termed SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1 (SMARCD1), or 60 kDa BRG-1/Brm-associated factor subunit A, or SWI/SNF complex 60 kDa subunit, is a core subunit of the SWI/SNF chromatin-remodeling complex that activates the transcription of fatty acid oxidation genes during fasting. BAF60A is involved in chromatin remodeling and hepatic lipid metabolism. It mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation. It is also a key component of the transcriptional control in cardiac progenitors. Moreover, BAF60A interacts with p53 to recruit the SWI/SNF complex, suggesting that the SWI/SNF chromatin remodeling complex is involved in the suppression of tumors
QFKLDPRLARLLGIHTQTRPVIINALWQYIKTHKLQDPHEREYINCDKYLQQIFECQRMKFSEIPQRLHP
LLMPPDP
>gnl|CDD|349494 cd17675, SWIB_BAF60B, SWIB domain found in BRG1-associated factor 60B (BAF60B) and similar proteins. BAF60B, also termed SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2 (SMARCD2), or 60 kDa BRG-1/Brm-associated factor subunit B, is a component of the BAF complex. It is involved in transcriptional activation and repression of select genes by chromatin remodeling. It plays a role in the ATM-p53 pathway in sensing chromatin opening by facilitating ATM recruitment to the SWI/SNF complex, as well as ATM activation. It also regulates transcriptional networks controlling differentiation of neutrophil granulocytes. Thus, it acts as a key factor controlling myelopoiesis and is a potential tumor suppressor in leukemia
QPPQYKLDPRLARLLGVHTQTRANIMQALWLYIKHNKLQDSHEKEYINCNRYFRQIFNCLRMRFSEIPMK
LAGLLQHPDP
>gnl|CDD|349495 cd17676, SWIB_BAF60C, SWIB domain found in BRG1-associated factor 60C (BAF60C) and similar proteins. BAF60C, also termed SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3 (SMARCD3), or 60 kDa BRG-1/Brm-associated factor subunit C, is a core subunit of the SWI/SNF chromatin-remodeling complex that activates the transcription of fatty acid oxidation genes during fasting. It is involved in chromatin remodeling and hepatic lipid metabolism. It is also essential for cardiomyocyte differentiation at the early heart development. Moreover, BAF60C drives glycolytic metabolism in the muscle and improves systemic glucose homeostasis through Deptor-mediated Akt activation. Furthermore, BAF60C epigenetically regulates epithelial-mesenchymal transition (EMT) by activating WNT signaling pathways
LDPRLARLLGIHTQTRSAIIQALWQYIKTNKLQDSHDKEYINCDKYFQQIFDCPRLKFSEIPQRLTNLLL
PPDP
>gnl|CDD|439039 cd17677, RUN1_DENND5, RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins. DENND5 has been characterized as Rab6-interacting protein which is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. It functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. DENND5 has two isoforms, DENND5A and DENND5B. This model represents the first RUN domain of DENND5
VIAQTNWKFVEGLLKECKMKTKRMLVEKMGQEAVELGHGEVNITGVEENTLIASLCDLLERIWSHGLQTK
QGKSALWSHLLAYQENEERLKPLPESLLFDMKNVQNMKEIKTDVGYARAWIRLALEKKLLSKHLKTLLSN
QDLLRSLYKRYAFLRCEDEREQFLYHLLSLNAVDYFCFTNTFT
>gnl|CDD|439040 cd17678, RUN2_DENND5, RUN2 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins. DENND5 has been characterized as Rab6-interacting protein which is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. It functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. DENND5 has two isoforms, DENND5A and DENND5B. This model represents the second RUN domain of DENND5
EIQELLGDAVNNIVKYFYKPEKERGSLTLLLCGESGLVSCLEQVFLYGFKSSRLFRRNLYIWDFIEKVKE
YFESLLKQEESDKDYELSKEDRSAMRSFCRLVQKINNASSSIGKDGKFQLFICLGLRDHLLHRWLPLLAS
SPVTLQMYEENSFLRDPDLLSFLVQLLESLNEFNITLENSLT
>gnl|CDD|439041 cd17679, RUN_PLEKHM1, RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and similar proteins. PLEKHM1, also called PH domain-containing family M member 1, or 162 kDa adapter protein (AP162), may act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. This model represents the RUN domain of PLEKHM1
KKSLTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKFISKVSSVFSGDVDKLPEP
NFWPLLLKFSHRDVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRD
PEQLDILKSLLQGLESFQFELPYNSSLLNTW
>gnl|CDD|439042 cd17680, RUN_PLEKHM2, RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and similar proteins. PLEKHM2, also called PH domain-containing family M member 2, or Salmonella-induced filaments A (SifA) and Kinesin-Interacting Protein (SKIP), is the lysosome, melanosome and lytic granule cargo adaptor that controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain. In addition to kinesin-1, it also interacts with several Rabs to affect endosomal trafficking. This model represents the RUN domain of PLEKHM2
RILRNISEAIKSLQSYSSSQEEEDVLITNENRELQRLCEALDHALLHGLRRGNRGYWPFVKEFTHKETIK
QIENLPNVTTDLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALLRDSQRLELLLTLLSGLEF
VQFDL
>gnl|CDD|439043 cd17681, RUN_RUFY1_like, RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar proteins. This family includes RUN and FYVE domain-containing protein RUFY1, RUFY2, and RUFY3. RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. RUFY1, RUFY2, and RUFY3 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain
ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVE
KLVPEANEITASVRDLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFYEPGALMMSEEAVV
IAGLLVGLNVIDCNL
>gnl|CDD|439044 cd17682, RUN_RUFY4_like, RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil domain-containing protein 1 (FYCO1), and similar proteins. The family includes RUFY4 and FYCO1. RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. Both RUFY4 and FYCO1 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain
DLKGCVLDLKSEFGEITDPDNPYLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEELLKKLNKIPKSL
SDAVKFVKSCKKVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEILSEILLSLL
YQLNEINFDL
>gnl|CDD|439045 cd17683, RUN_RUNDC1, RUN domain found in RUN domain-containing protein 1 (RUNDC1) and similar proteins. RUN domain-containing protein 1 (RUNDC1) is thought to a role as p53/TP53 inhibitor and as such may have oncogenic activity. This model contains the RUN domain
KEQLVDQLKTQISDLERFINFLQHWGDLRARLEIAVNRVIELAETQQRLDEEDSSSYTDSSDDPVVRSED
ELTTAVRKELAPALRDLLQHGLMSPSSSSSLVPAILACCPSSSSSSPQAMHAWDLFLKYYELKNGREFNE
SPARKLSQSFQLDIVGGKAITPKQSLLTAIGNIISSHEPLKRSPDSHFKAFVCAALNEKRLVSWLRLILR
SPTLVDEHYQPWSYVARTGFEDALQSLEKLSSLKFDLP
>gnl|CDD|439046 cd17684, RUN_RUNDC3, RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins. RUNDC3 contains two isoforms, RUNDC3A and RUNDC3B. RUNDC3A, also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. RUNDC3B, also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. Both RUNDC3A and RUNDC3B contain a RUN domain
NLVTVCRLSVKSLIDKACLETIDDSSEELINFAAILEQILSHRLKPVKPWYGSEEPRTFWDYIRVACKKV
PQNCIASIEQMENIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSEDATVLCGML
IGLNAIDFSF
>gnl|CDD|439047 cd17685, RUN_RUSC, RUN domain found in RUN and SH3 domain-containing proteins, RUSC1, RUSC2 and similar proteins. RUSC1, also called new molecule containing SH3 at the carboxy-terminus (NESCA), may acts as a signaling adapter that translocates to the nuclear envelope and regulates neurotrophin-induced neurite outgrowth. RUSC2, also called iporin, or interacting protein of Rab1, is a novel interacting molecule for the active GTP-bound conformation of Rab1. It may function as a link between the targeting of endoplasmic reticulum derived vesicles, triggered by the Rab1 GTPase and a signaling pathway regulated by molecules containing SH3 and/or poly-proline regions. This model contains the RUN domain of RUSC1 and RUSC2
QKRGLVKAVIAAVDKIVAHFSQSRDPSDKAKLGNSAVSPEVGHLVLKYLCPALYALLSDGLKPYVLTLFG
QVKNSVWSVVEASTQPGPSTKALNELVNKLNSEEKLTSGTLKFNAFIFGLLNLRSLDAWLSYLVTKENLL
SKHYNPNAFLLLASSAYRPLFDELLLALQPLSVLPFDL
>gnl|CDD|439048 cd17686, RUN_RUBCN, RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (RUBCN) and similar proteins. RUBCN, also called rubicon, or beclin-1 associated RUN domain containing protein (Baron), is part of a Beclin-1-Vps34-containing autophagy complex. It negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. It is also an important negative regulator of the innate immune response, enhances viral replication and may play a role in viral immune evasion. This model contains the RUN domain of RUBCN
STVEGLLLSRSSNVWSTYGGLQRLCRAVENILQHGLKEFQGLNKEIDDWEFVQGLRWLQPTLAPSIEQQS
RSSPSESEVSDKGRLWLRQSLQQHCLSSQLQWLVSDKELLRKYYEDEAFLRQEGYATALLICLTAVELNQ
PSLLAQIDPSL
>gnl|CDD|439049 cd17687, RUN_SGSM1_like, RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins. SGSM1, also called RUN and TBC1 domain-containing protein 2 (RUTBC2), interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. It is a Rab9A effector and GTPase-activating protein for Rab36, and links Rab9A function to Rab36 function in the endosomal system. SGSM2, also called RUN and TBC1 domain-containing protein 1 (RUTBC1), is a GTPase-activating protein for Rab32/38, and regulates melanogenic enzyme trafficking in melanocytes. It also acts as a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins. This model contains the RUN domain of SGSM1 and SGSM2
KEVKQLMEEAVTRKFIHEDSSSVTSLCGAVDACLLHGLRKRALGLFRSSSTFSLLQKVAKSCPPAADILR
KVQEIENLSENKRSSSSSGSNSSNSHGNSSSNRKILWIRIALFEKVLDKIVDYLVENASKYYEKEALMAD
PVDGPLLASLLVGPCALDYTK
>gnl|CDD|439050 cd17688, RUN_SGSM3, RUN domain found in small G protein signaling modulator 3 (SGSM3) and similar proteins. SGSM3, also called RUN and TBC1 domain-containing protein 3 (RUTBC3), or Merlin-Associated Protein (MAP), or Rab-GTPase-activating protein-like protein (RabGAPLP), may play a cooperative role in NF2-mediated growth suppression of cells. This model contains the RUN domain of SGSM3
DEHCWVGELNGLRGWFPAKFVELLDERSKEYSIAGDDSVTETITDLVRGRLCPALKAIFEHGLKKPSLLG
GACHPWLFIEEAASKEVEKDFNSVYSRLVLCKTFRLDEDGKVLTPEELLYRSVQAVNMSHDAAHAQMDVK
LRSLICVGLNEQVLHLWLEVLCSSVQIVEKWYHPWSFLRSPGWVQIKCELRVLSQFSFNLSLDWELPKKR
TKKS
>gnl|CDD|439051 cd17689, RUN_SNX29, RUN domain found in sorting nexin-29 (SNX29) and similar proteins. SNX29, also called RUN domain-containing protein 2A (RUNDC2A), belongs to the sorting nexin family. Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain, a phospholipid-binding motif, or through protein-protein interactions with membrane-associated protein complexes. Some sorting nexin family members have been shown to facilitate protein sorting. This model contains the RUN domain of SNX29
RLLDAVKQCQIRFGGKTELATESDSRVSCLCAQLEAVLQHGLKTSRSPNLVSSAVTQVSGLAGSLGSAET
EPTFWPFVKEHLTKHELERFELLKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFL
RDEERSSMLPNMAAGLGSILFALSID
>gnl|CDD|439052 cd17690, RUN1_DENND5A, RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins. DENND5A, also called Rab6-interacting protein 1 (Rab6IP1), is present predominantly in developing neuronal tissue, and functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5A
VIAQTNWKFVEGLLKECRNKTKRMLVEKMGREAVELGHGEVNITGVEENTLIASLCDLLERIWSHGLQVK
QGKSALWSHLLHYQENRERKTTSSGLSTSGIILDSERRKSDASLAMPPLKISLIQDMRHIQNIGEIKTDV
GKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAFLRCDDEKEQFLYHLLSFNAVDYFCFTNVFT
>gnl|CDD|439053 cd17691, RUN1_DENND5B, RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins. DENND5B, also called Rab6-interacting protein 1 (Rab6IP1)-like protein, functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5B
VIAQTNWKFVEGLLKECRMKTKRMLVEKMGHEAVELGHGEANITGLEENTLIASLCDLLERIWSHGLQVK
QGKSALWSHLLHFQEREEKQEHVAESPVANGLERRKSETGVNLPTLRVSLIQDMRHIQNMSEIKTDVGRA
RAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAFLRCEEEKEQFLYHLLSLNAVDYFCFTSVFT
>gnl|CDD|439054 cd17692, RUN2_DENND5A, RUN2 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins. DENND5A, also called Rab6-interacting protein 1 (Rab6IP1), is present predominantly in developing neuronal tissue, and functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the second RUN domain of DENND5A
QIQEAVGEAINGIVKHFHKPEKERGSLTLLLCGENGLVSALEQVFQHGFKSPRLFKNVFIWDFLEKAQAY
YESLEQNELVPEENWQTRARNFCRFVNAINSTPRNIGKDGKFQMLVCLGARDHLLHHWIALLADCPITAQ
MYEDTALIKDHTLVNSLIRVLQTLQEFNITLEASLV
>gnl|CDD|439055 cd17693, RUN2_DENND5B, RUN2 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins. DENND5B, also called Rab6-interacting protein 1 (Rab6IP1)-like protein, functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the second RUN domain of DENND5B
QIQEGIGEAVNNIVKHFHKPEKERGSLTVLLCGENGLVAALEQVFHHGFKSARIFQKNVFIWDFIEKAVA
YFETTDQIGDLEEDLLILKSSCKTFCHYVNAINTAPRNIGKDGKFQLLVCLGARDHLLPQWIPLLAECPV
ITRMYEENALLRDRMTVNSLIRVLQTLQDFNITLEGSLI
>gnl|CDD|439056 cd17694, RUN_RUFY1, RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins. RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain
ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVE
KLCPEASDIATSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAV
IVGLLVGLNVIDANLC
>gnl|CDD|439057 cd17695, RUN_RUFY2, RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins. RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. This model represents the RUN domain of RUFY2
ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVE
KLCPEAEEIAASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAV
IVGLLVGLNVIDANLC
>gnl|CDD|439058 cd17696, RUN_RUFY3, RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins. RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3
ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVE
KLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAI
IAGLLVGLNVIDANFC
>gnl|CDD|439059 cd17697, RUN_RUFY4, RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins. RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain; this model represents the RUN domain of RUFY4
KDLQASIAELQKDQEEQQLPITDGSPELHRLCARLEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGG
TEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNPELTGEWYYARSPFLSPELRSDILDSL
YELNGVNFDL
>gnl|CDD|439060 cd17698, RUN_FYCO1, RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins. FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and Phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. This model represents the RUN domain of FYCO1
ESQLQKIIRDLQDCVTELKKEFEETGEPITDDSTTLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCE
CLAKVKGLNDGIRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPRSVFLNHKY
SSDIINSLYDLNEVQFDL
>gnl|CDD|439061 cd17699, RUN_RUNDC3A, RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins. RUN domain-containing protein 3A (RUNDC3A), also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. It contains a RUN domain
NLITVCRFSVKTLLEKYTAEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFSSDGQRGFWDYIRLACSKV
PNNCISSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTVLTGML
IGLSAIDFSFC
>gnl|CDD|439062 cd17700, RUN_RUNDC3B, RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins. RUN domain-containing protein 3B (RUNDC3B), also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. RUNDC3B contains a RUN domain
NLITVCRFSVKTLIDRSCFETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYESPRSFWDYIRVACSKV
PHNCICSIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGML
LGLNAIDFSFC
>gnl|CDD|439063 cd17701, RUN_RUSC1, RUN domain found in RUN and SH3 domain-containing protein 1 (RUSC1) and similar proteins. RUSC1, also called new molecule containing SH3 at the carboxy-terminus (NESCA), may acts as a signaling adapter that translocates to the nuclear envelope and regulates neurotrophin-induced neurite outgrowth. This model contains the RUN domain of RUSC1
QKKGLLNAVSVSVDKIISHFSSARNLVQKAQLGDSRLSPDVGHLVLQTLCPALYALVADGLKPFQKDLIT
GRRRSSPWSVVEASVKPGPSTRSLHSLYCQVSRLAQLRSSRSRFNAFIFGLLNTKQLDLWLSHLQKCSDV
LSLFYLPTGFFSLARGSCPSLFEELLLLLQPLSVLTFHLDLLF
>gnl|CDD|439064 cd17702, RUN_RUSC2, RUN domain found in RUN and SH3 domain-containing protein 2 (RUSC2) and similar proteins. RUSC2, also called iporin, or interacting protein of Rab1, is a novel interacting molecule for the active GTP-bound conformation of Rab1. It may function as a link between the targeting of endoplasmic reticulum derived vesicles, triggered by the Rab1 GTPase and a signaling pathway regulated by molecules containing SH3 and/or poly-proline regions. This model contains the RUN domain of RUSC2
QKKGLVKAVNIAVDLIVAHFGTSRDPGVKAKLGNSSVSPNVGHLILKYLCPAVRNILQDGLKAYVLDVII
GQRRNKPWSVVEASTQLGPSTKLLHSLVSKVSQYSELTSHSMRFNAFIFGLLNIRSLEFWFNHLYNHEDI
ITEHYQPWGFLALAHGVCQPLFEELLLLLQPLSLLPFDLDLLF
>gnl|CDD|439065 cd17703, RUN_SGSM1, RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins. SGSM1, also called RUN and TBC1 domain-containing protein 2 (RUTBC2), interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. It is a Rab9A effector and GTPase-activating protein for Rab36, and links Rab9A function to Rab36 function in the endosomal system. This model contains the RUN domain of SGSM1
KEVKQIMEEAVTRKFVHEDSSHIISFCAAVEACVLHGLKRRAAGFLRSNKIAALFMKVGKSFPPAEELCR
KVQELEQLLENKRNQMQGLQENVRKMPKLPNLSPQAIKHLWIRTALFEKVLDKIVHYLVENSSKYYEKEA
LLMDPVDGPILASLLVGPCALEYTKMKTADHFWTDPS
>gnl|CDD|439066 cd17704, RUN_SGSM2, RUN domain found in small G protein signaling modulator 2 (SGSM2) and similar proteins. SGSM2, also called RUN and TBC1 domain-containing protein 1 (RUTBC1), is a GTPase-activating protein for Rab32/38, and regulates melanogenic enzyme trafficking in melanocytes. It also acts as a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins. This model contains the RUN domain of SGSM2
KEVKQIMEEAVTRKFVHEDSSHIIALCGVVEACLLHLLKRRAAGFLRSDKVAALFTKVGKTYPTAGDICK
KVQELQQQVEGRKNTQSTQEELRRQSSTTSKTPPLTPQAIKHIWVRTALIEKVLDKIVQYIVDNCSKYYE
KEALMSDPVCGPILASLLVGPCALEYTKLKTADHYWTDPS
>gnl|CDD|350658 cd17706, MCM, MCM helicase family. MCM helicases are a family of helicases that play an important role in replication and homologous recombination repair. The heterohexameric ring-shaped Mcm2-7 complex is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases. Mcm8 and Mcm9, form a complex required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs)
ILADSIAPSIYGHEDVKKAVLLQLFGGVQKILEDGTRIRGDIHILLVGDPGTAKSQILKYVLKIAPRGVY
TSGKGSSGAGLTAAVVRDSETGEWYLEAGALVLADGGVCCIDEFDKMKELDRTALHEAMEQQTISIAKAG
IVTTLNARCSILAAANPKGGRYNPKLSPIENINLPSPLLSRFDLIFVIRDDPDEERDEELAEHIIDLHRG
SDPEEQVKPEEDGIPIDIELLRKYILYARQIHPKISEEAREKLVRWYVELRKESERRSTIPITARQLESV
IRLAEAHAKMRLSEVVTEEDVEEAIRLVRHS
>gnl|CDD|349340 cd17707, BRCT_XRCC1_rpt2, Second (C-terminal) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar proteins. XRCC1 is a DNA repair protein that corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. It forms homodimers and interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB), DNA ligase III (LIG3), APTX, APLF, and APEX1. XRCC1 contains an N-terminal XRCC1-specific domain and two BRCT domains. This model corresponds to the second BRCT domain
ELPDFFSGKHFFLYGDFPADERRLLKRYITAFNGEVEDYMSDKVTFVVTNQEWDDNFDEALAENPSLAFV
RPRWIYACHEKQKLLPCQPYLVVP
>gnl|CDD|349341 cd17709, BRCT_pescadillo_like, BRCT domain of pescadillo and related proteins. Pescadillo has been characterized in zebrafish as a protein involved in the control of cell proliferation, specifically in the developing embryo. Mammalian homologs have been linked to ribosome biogenesis and nucleologenesis, and yeast homologs have been shown to be required for synthesis of the 60S ribosomal subunit. Pescadillo contains a BRCT domain
LFKGLKFFLSREVPRESLEFIIRSFGGEVSWDGSDSPGADEDDESITHQIVDRPVQNKQYLSREYVQPQW
VFDCVNARILLPVEDY
>gnl|CDD|349342 cd17710, BRCT_PAXIP1_rpt2, second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins. PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the second BRCT domain
LFSGVVVCPSQISAEDRLKLWAMVTFHGGKCQLNLDKKCTHLVTGKASGAKYECALKHEGIKIVTPDWVT
DCIKAKTLLDE
>gnl|CDD|349343 cd17711, BRCT_PAXIP1_rpt3, third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins. PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the third BRCT domain
GCVFFIADYPEQMGDQEIATWKKVIEEHGGEVVDEYSPRVTHVICESQDSPEYQQALRDGKRVVTAYWLN
DVLKRGKLLPP
>gnl|CDD|349344 cd17712, BRCT_PAXIP1_rpt5, fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins. PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the fifth BRCT domain
TPRVLFTGFDPVQVRKLTKKVTILGGEVVESPQECTHLVAPKVSRTVKFLTAISVCKHIVTPEWLEESFK
QGKFL
>gnl|CDD|349345 cd17713, BRCT_polymerase_mu_like, BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu), DNA nucleotidylexotransferase and similar proteins. The family includes DNA-directed DNA/RNA polymerase mu (polymerase mu) and DNA nucleotidylexotransferase. Polymerase mu (EC 2.7.7.7), also termed Pol mu, or terminal transferase, is a Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). It participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination. DNA nucleotidylexotransferase (EC 2.7.7.31), also termed terminal addition enzyme, or terminal deoxynucleotidyltransferase, or terminal transferase, is a template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. It is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. All family members contains a BRCT domain
KFPDVVIFLVERKMGSSRRAFLTELARSKGFRVEDELSDSVTHVVAENNSAEEVLEWLERQKLQGSSSPE
LLDISWFTESMGAGKPV
>gnl|CDD|349346 cd17714, BRCT_PAXIP1_rpt1, first (N-terminal) BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins. PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the first BRCT domain
FKDVKYFVVGNLDEKVEQLLKNGGAKEVSYLSDMATHVIVDDNDNPEVGEARDLFELPVVTSSWVILSIK
AGKLLP
>gnl|CDD|349347 cd17715, BRCT_polymerase_lambda, BRCT domain of DNA polymerase lambda and similar proteins. DNA polymerase lambda, also termed Pol Lambda, or DNA polymerase beta-2 (Pol beta2), or DNA polymerase kappa, is involved in base excision repair (BER) and is responsible for repair of lesions that give rise to abasic (AP) sites in DNA. It also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. DNA polymerase lambda has both template-dependent and template-independent (terminal transferase) DNA polymerase activities, as well as a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity. DNA polymerase lambda contains one BRCT domain
FEGLTIHLVRTGIGRARAELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAERKVDRDPPGAQLVKSGWL
SACIQEKRLV
>gnl|CDD|349348 cd17716, BRCT_microcephalin_rpt1, first (N-terminal) BRCT domain of microcephalin and similar proteins. Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the first repeat
GVVAYVDVRSGDGADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEA
CKETGKRV
>gnl|CDD|349349 cd17717, BRCT_DNA_ligase_IV_rpt2, second BRCT domain of DNA ligase 4 (LIG4) and similar proteins. LIG4 (EC 6.5.1.1), also termed DNA ligase IV, or polydeoxyribonucleotide synthase [ATP] 4, is involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. It is a component of the LIG4-XRCC4 complex that is responsible for the NHEJ ligation step. LIG4 contains two BRCT domains. The family corresponds to the second one
FRGCTVYFDSYAVINDPSTEIEGTGLDIRALELRFHGGKVVSELAEGISHVVVDSDHSRVVDFKELRRLL
KKKFKIVSESWVTDSIKR
>gnl|CDD|349350 cd17718, BRCT_TopBP1_rpt3, third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins. TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the third BRCT domain
EKAGDFLDGCKIYLSGFSGAELDKLRRIINAGGGTRFNQLNESVTHVVVGESSEELLKELAKLAGRPHVV
TPSWLLECFKQGK
>gnl|CDD|349351 cd17719, BRCT_Rev1, BRCT domain of DNA repair protein Rev1 and similar proteins. REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light
IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKKARNYKVVRPEWI
VDSIKAGRLLPEAPYLL
>gnl|CDD|349352 cd17720, BRCT_Bard1_rpt2, second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins. Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the second BRCT domain
LFDGCHFYFHGTFKPPTTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAYARPDSDLANCTHYIIYD
KLNDKKPAKVRQGKVRVVPVSWLLDCISQFK
>gnl|CDD|349353 cd17721, BRCT_BRCA1_rpt2, second (C-terminal) BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins. BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT repeats at the C-terminus. The family corresponds to the second BRCT domain
KLLFRGFEICCYGPFTNMTKDQLEWLLELCGATVVKEPSLFTAKPGKKRLIVVQPDAWTEDNDYNAIYRR
YKALVVTREWVLDSVALYKVQPLDAYLL
>gnl|CDD|349354 cd17722, BRCT_DNA_ligase_IV_rpt1, first BRCT domain of DNA ligase 4 (LIG4) and similar proteins. LIG4 (EC 6.5.1.1), also termed DNA ligase IV, or polydeoxyribonucleotide synthase [ATP] 4, is involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. It is a component of the LIG4-XRCC4 complex that is responsible for the NHEJ ligation step. LIG4 contains two BRCT domains. The family corresponds to the first one
IFEGVEFCVMSDMSSPKSKAELEKLIKENGGKVVQNPGAPDTICVIAGREVVKVKNLIKSGGHDVVKPSW
LLDCIARKELLPLEPKYMIH
>gnl|CDD|349355 cd17723, BRCT_Rad4_rpt4, fourth BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins. Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system, which couples S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the fourth one
GLSISLTGFSGVDLLHISKLIKLLGAKYHESLTKDRSLLIVNSTEKKSDKINFAKKWGIPVVSVEWLWDC
LKEG
>gnl|CDD|349356 cd17724, BRCT_p53bp1_rpt2, Second (C-terminal) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins. p53BP1, also termed 53BP1, or TP53-binding protein 1 (TP53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. TP53BP1 contains two tandem BRCT repeats. This family corresponds to the second BRCT domain
LFKGLKILVVSKKKKPFRETWSFILKAAGATSVKKLPSTSAASSSDIGKIDVVVTDGSCPSTVLKKARQL
GIPVVSTEWVIQCLING
>gnl|CDD|349357 cd17725, BRCT_XRCC1_rpt1, First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar proteins. XRCC1 is a DNA repair protein that corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. It forms homodimers and interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB), DNA ligase III (LIG3), APTX, APLF, and APEX1. XRCC1 contains an N-terminal XRCC1-specific domain and two BRCT domains. This family corresponds to the first one
GVVFVLSGFQNPFRGELRDKALEMGAKYRPDWTADCTHLICAFANTPKYKQVKGAGGIIVSKEWILDCYK
KKKRLPWKRY
>gnl|CDD|349358 cd17726, BRCT_PARP4_like, BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins. PARP-4, also termed 193 kDa vault protein, or ADP-ribosyltransferase diphtheria toxin-like 4 (ARTD4), or PARP-related/IalphaI-related H5/proline-rich (PH5P), or vault poly(ADP-ribose) polymerase (VPARP), shows poly(ADP-ribosyl)ation activity that catalyzes the formation of ADP-ribose polymers in response to DNA damage. PARP-4 is a component of the vault ribonucleoprotein particle, at least composed of MVP, PARP4 and one or more vault RNAs (vRNAs). The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group
VFSGCQIVLDLKTLPGFKEKKKLKKKITENGGIISYIINKKCTHVVVNNAKALSSYKCRMAQKYGIPVVS
LDYIWKCVEAGKLLD
>gnl|CDD|349359 cd17727, BRCT_TopBP1_rpt6, sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins. TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the sixth BRCT domain
LKGVVICVSKKLSKRQGELNKIAASLGAEYRWTYDESCTHFIYQGKANDTNREYKSAKEQGKFIVSPHWL
YACKE
>gnl|CDD|349360 cd17728, BRCT_TopBP1_rpt8, eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1. TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the eighth BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group
GWKVLLVVDIAKEDGFKRLLEAGGAKVIPSSPPYSLKLKDATHAFVDLTKDTSVDLISLLAKAGVPCLKP
EYIAEYLMKD
>gnl|CDD|349361 cd17729, BRCT_CTDP1, BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar proteins. CTDP1 (EC 3.1.3.16), also termed TFIIF-associating CTD phosphatase, or TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1), promotes the activity of RNA polymerase II through processively dephosphorylating 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. It plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation
DVKDILPELRSKVLKGCVIVFSGVIPTGIDPERSRLWKLAESLGAKVVTDLSPRTTHLVAAKLGTEKVKQ
ALKMPGIHVVHPDWLWACAERWERVDE
>gnl|CDD|349362 cd17730, BRCT_PAXIP1_rpt4, fourth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins. PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the fourth BRCT domain
QVISVTGFDGSEREDIKRMIELMGAKYTGYLTRSNTHLICKRPEGEKYEKAKEWRIPVVNAQWLEDILLG
GRL
>gnl|CDD|349363 cd17731, BRCT_TopBP1_rpt2_like, second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins. TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain
PPFKGLVICVTGFDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPSGQKYEFARKWNSIHIVTPEWL
YDSIEAG
>gnl|CDD|349364 cd17732, BRCT_Ect2_rpt2, second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar proteins. ECT2 is a guanine nucleotide exchange factor (GEF) for Rho GTPases, phosphorylated in G2/M phases, and is involved in the regulation of cytokinesis. It contains two tandem BRCT domains. The family corresponds to the second BRCT domain
PFEGCTLSFLGFSDEEKTHMEELTEENGGKVTPLGDPSCTHLVVDESTVKELPFEPSSKLHVVKQEWFWA
SIQMDACADE
>gnl|CDD|349365 cd17733, BRCT_Ect2_rpt1, first BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar proteins. ECT2 is a guanine nucleotide exchange factor (GEF) for Rho GTPases, phosphorylated in G2/M phases, and is involved in the regulation of cytokinesis. It contains two tandem BRCT domains. The family corresponds to the first BRCT domain
MENLVLCFTGFRKKEELSRLVNLVHHMGGSIRKDFSSKVTHLVANSTQGEKYRVAVSLGTPIMTEDWIYK
AWEKRN
>gnl|CDD|349366 cd17734, BRCT_Bard1_rpt1, first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins. Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain
LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADERGVCPRTMKYLMGILAGKWIVSFEWV
EACLKAKKLV
>gnl|CDD|349367 cd17735, BRCT_BRCA1_rpt1, first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins. BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain
MSMVASGLTPEELMLVQKFARKTGSTLTSQFTEETTHVIMKTDAELVCERTLKYFLGIAGRKWVVSYQWI
TQSIKEGKILPEHDFEVRGDVVNGRNH
>gnl|CDD|349368 cd17736, BRCT_microcephalin_rpt2, second BRCT domain of microcephalin and similar proteins. Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat
RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESL
EAGKWL
>gnl|CDD|349369 cd17737, BRCT_TopBP1_rpt1, first BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins. TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the first BRCT domain
DVTISCTSLEKEEREEVHKYVQLMGGRVSRDLTVSVTHLIAGEVGSKKYLVAASLKKPIMLPSWVKTLWE
KS
>gnl|CDD|349370 cd17738, BRCT_TopBP1_rpt7, seventh BRCT domain of DNA topoisomerase 2-binding protein 1. TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the seventh BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group
KPVFLLSGFSEDEKKELISIIEKLGGKVLDSDEFDPKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEA
SAKAG
>gnl|CDD|349371 cd17740, BRCT_Rad4_rpt1, first BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins. Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system which couples the S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the first one
KPLSGIVLCCTSIPAEQRTEIATKASKMGAAYTADLTSDVTHLVAGQVNTTKYKFAARSRPDIKVMTVEW
VEHLYESWQQGE
>gnl|CDD|349372 cd17741, BRCT_nibrin, BRCT domain of nibrin and similar proteins. Nibrin (NBN), also termed Nijmegen breakage syndrome protein 1 (NBS1), or cell cycle regulatory protein p95, is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The BRCT (Breast Cancer Suppressor Protein BRCA1, carboxy-terminal) domain is found within many DNA damage repair and cell cycle checkpoint proteins. The unique diversity of this domain superfamily allows BRCT modules to interact forming homo/hetero BRCT multimers, BRCT-non-BRCT interactions, and interactions within DNA strand breaks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is absent in this group
EPLVVCSSCLDSEEKKKLKQIIAKLGGKVVNEWTEECTHLVMSKIKVTVKVICALISGKPIVTPEYLDAL
LEAI
>gnl|CDD|349373 cd17742, BRCT_CHS5_like, BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins. CHS5, also termed protein CAL3, is a component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. It is also involved in targeting FUS1 to sites of polarized growth
SGITVCLGPLDPPESVDELEQCLERIGAKPTDRVAIDTTHFVCTVPSGPEYEKAKEMNIPIVRPEWLRAC
EVEKKIV
>gnl|CDD|349374 cd17743, BRCT_BRC1_like_rpt5, fifth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar proteins. Schizosaccharomyces pombe BRC1 is required for mitotic fidelity, specifically in the G2 phase of the cell cycle. It plays a role in chromatin organization. The family also includes Cryptococcus neoformans DNA ligase 4 (LIG4, also known as DNA ligase IV or polydeoxyribonucleotide synthase [ATP] 4), which is involved in dsDNA break repair, and plays a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologus end-joining. Members in this family contain six BRCT domains. This family corresponds to the fifth one
VRLLFTGYKLWTEKEIKKLKKLGISIVEDPDECTHLVAPKIVRTEKFLCALAYAPVIVTTDWLEACLKAG
>gnl|CDD|349375 cd17744, BRCT_MDC1_rpt1, first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins. MDC1, also termed nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The family corresponds to the first BRCT domain
PRVLFTGVSDKEEGEKIIKKLGGSVVDSVEDCTHLVTDKVRRTVKFLCALARGIPIVSPDWLEASIKANK
FL
>gnl|CDD|349376 cd17745, BRCT_p53bp1_rpt1, first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins. p53BP1, also termed 53BP1, or TP53-binding protein 1 (TP53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis. TP53BP1 contains two tandem BRCT repeats. This family also includes Schizosaccharomyces pombe Crb2, which is a checkpoint mediator required for the cellular response to DNA damage. This model corresponds to the first BRCT domain
IFSGCAFLLTGAEETDKPFDKERLESQIEANGGTVLEDFDEELFNDGRSSTRKSRSKDLRFVFLIADSPS
RTPKYLQALALGIPCVSHKWILDCIEAGK
>gnl|CDD|349377 cd17746, BRCT_Rad4_rpt2, second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins. Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system which couples S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the second one
KHILPTLFKCRVCLTNIGQPERSRIENYVLKHGGTFCPDLTRDVTHLIAGTSSGRKYEYALKWKINVVCV
EWLWQSIQRNAVLEPQYFQLD
>gnl|CDD|349378 cd17747, BRCT_PARP1, BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins. PARP-1 (EC 2.4.2.30), also termed ADP-ribosyltransferase diphtheria toxin-like 1 (ARTD1), or NAD(+) ADP-ribosyltransferase 1 (ADPRT 1), or poly[ADP-ribose] synthase 1, is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism
LTGMKFALIGKLSKSKDELKKLIEKLGGKVASKVTKKVTLCISTKAEVEKMSKKMKEAKEAGVPVVSEDF
LEDCIK
>gnl|CDD|349379 cd17748, BRCT_DNA_ligase_like, BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins. LigA, also called NAD(+)-dependent polydeoxyribonucleotide synthase, catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family
LAGKTFVFTGTLSSMSRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLKKGEELKAKGLGIKIISE
EEFLDL
>gnl|CDD|349380 cd17749, BRCT_TopBP1_rpt4, fourth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins. TopBP1, also called DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the fourth BRCT domain
FNGKRFLILGFDEEQEAQLAELIEENGGKVLKDNSRAVADYAIVPLLGCPVEATVGEVVTNCWLQMCIEQ
EELLDPDSNPLFTP
>gnl|CDD|349381 cd17750, BRCT_SLF1, BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins. SLF1, also termed Smc5/6 localization factor 1, or ankyrin repeat domain-containing protein 32 (ANKRD32), or BRCT domain-containing protein 1 (BRCTD1), plays a role in the DNA damage response (DDR) pathway by regulating post replication repair of UV-damaged DNA and genomic stability maintenance. It is a component of the SLF1-SLF2 complex that acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand break (DSB) sites on chromatin during DNA repair in response to stalled replication forks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group
VQKHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYII
NSAKSGRWLDE
>gnl|CDD|349382 cd17751, BRCT_microcephalin_rpt3, third BRCT domain of microcephalin and similar proteins. Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the third repeat
SRYRQNLFADGGPIYVSSNSVPPKDKLEELVLLCGGKVVKSSRKADICIGKTPPNPDKPSVSEKWLLDSI
TNHKL
>gnl|CDD|349383 cd17752, BRCT_RFC1, BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins. RFC1, also termed activator 1 140 kDa subunit, or A1 140 kDa subunit, or activator 1 large subunit, or activator 1 subunit 1, or replication factor C 140 kDa subunit, or RF-C 140 kDa subunit, or RFC140, is the large subunit of replication factor C (RFC), which is a heteropentameric protein essential for DNA replication and repair. RFC1 can bind single- or double-stranded DNA. It could play a role in DNA transcription regulation as well as DNA replication and/or repair. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family
GAPNCLEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGPSKLEKAKELGTKIID
EDGLFDLIR
>gnl|CDD|350659 cd17753, MCM2, DNA replication licensing factor Mcm2. Mcm2 is a helicase that play an important role in replication. It is part of the heterohexameric ring-shaped Mcm2-7 complex, which is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases
RIINSIAPSIYGHDDIKTAIALALFGGVAKNPGGKHRIRGDINVLLLGDPGTAKSQFLKYVEKTAHRAVF
TTGQGASAVGLTASVRKDPVTKEWTLEGGALVLADKGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAG
IVTSLQARCSVIAAANPIGGRYNPTLTFAQNVNLTEPILSRFDILCVVRDTVDPEEDERLAKFVVGSHVR
SHPENDEDREGEEEKNQRQRPKETKVEPIPQELLRKYIHYAREKVRPKLNQMDMDKVSRVYADLRKESMA
TGSLPITVRHLESIIRISEAHAKMHLREYVSEEDVDMAIRVMLDS
>gnl|CDD|350660 cd17754, MCM3, DNA replication licensing factor Mcm3. Mcm3 is a helicase that play an important role in replication. It is part of the heterohexameric ring-shaped Mcm2-7 complex, which is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases
LLSKSLAPSIYGHEYIKKAILLMLLGGVEKNLENGSHLRGDINILLVGDPSVAKSQLLRYVLNTAPLAIA
TTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDIDRVAIHEVMEQQTVTIAKAG
IHASLNARCSVLAAANPVYGRYDVYKTPMENIGLPDSLLSRFDLLFIVLDDIDEERDRSISEHVLRMHRY
IKFLRKYIHYAKERIKPKLTQEAAEYIAEEYADLRNDDNTKTDKARTSPITARTLETLIRLATAHAKARL
SKTVDKVDAEVALNLLRFA
>gnl|CDD|350661 cd17755, MCM4, DNA replication licensing factor Mcm4. Mcm4 is a helicase that play an important role in replication. It is part of the heterohexameric ring-shaped Mcm2-7 complex, which is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases
RLARSIAPSIYELEDVKKGILLQLFGGTRKDFTKTGGKYRGDINILLCGDPGTSKSQLLQYVHKISPRGV
YTSGKGSSAVGLTAYVTRDPDTKQLVLESGALVLSDGGICCIDEFDKMSDSTRSVLHEVMEQQTLSIAKA
GIITTLNARTSILASANPIGSRYNPKLTVVENIDLPPTLLSRFDLIYLVLDKVDEKYDRRLAKHLVSLYL
EDTPEHIQDEVLDVEVLTDYISYAREHIHPKLSEEAAQELVQAYVDMRKMGSDARKRITATPRQLESLIR
LAEAHAKMRLSNVVEAEDVEEAVRLIREA
>gnl|CDD|350662 cd17756, MCM5, DNA replication licensing factor Mcm5. Mcm5 is a helicase that play an important role in replication. It is part of the heterohexameric ring-shaped Mcm2-7 complex, which is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases
IISKSIAPSIYGNEDIKKAIACLLFGGSRKRLPDGMRLRGDINVLLLGDPGTAKSQLLKFVEKVAPIGVY
TSGKGSSAAGLTASVMRDPSTREFYLEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAG
ITTTLNSRTSVLAAANPVFGRYDDLKTPGDNIDFQTTILSRFDMIFIVKDKHDEERDITIAKHVINIHAS
ARKASQSQENEGEIPISKLKRYIAYCRAKCAPRLSEEAAEKLSNHYVTIRKDVRQNELESDNRSSIPITV
RQLEAIIRISESLAKMELSPIATEKHVEEAIRLFQVS
>gnl|CDD|350663 cd17757, MCM6, DNA replication licensing factor Mcm6. Mcm6 is a helicase that play an important role in replication. It is part of the heterohexameric ring-shaped Mcm2-7 complex, which is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases
NLVRSIAPSIYGHEEVKKGILLMLLGGVHKITREGISLRGDINVCIVGDPSTAKSQFLKYVEEFSPRAVY
TSGKASSAAGLTAAVVRDEETGDFVIEAGALMLADNGICCIDEFDKMDIKDQVAIHEAMEQQTISITKAG
IQATLNARTSILAAANPVGGRYDRSKSLKQNINISAPIMSRFDLFFVLLDECNEVTDYAIASHIVDLHSK
REEAIEPPFTAEQLKRYIAYARTFKPKLTKEAKDELVEQYKELRQDDASGSTRSSYRITVRQLESLIRLS
EAIARLHCSDEVTPEHVEEAARLLKKS
>gnl|CDD|350664 cd17758, MCM7, DNA replication licensing factor Mcm7. Mcm7 is a helicase that play an important role in replication. It is part of the heterohexameric ring-shaped Mcm2-7 complex, which is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases
KLAASIAPEIYGHEDVKKALLLLLVGGVDKRGDGMKIRGDINICLMGDPGVAKSQLLKYICRIAPRSVYT
TGRGSSGVGLTAAVMKDPVTGEMTLEGGALVLADQGICCIDEFDKMDESDRTAIHEVMEQQTISIAKAGI
TTTLNARTSILAAANPAYGRYNPRRSPEQNINLPAALLSRFDLLFLILDKPDRDNDLRLAEHVTYVHQHN
KQPDSDFEPLDPKLLRAYIALAKRKRPTVPPALADYIVQAYVEMRQEAKRSKDFTFTTPRTLLAILRLSQ
ALARLRLSDSVEIDDVEEALRLMEMS
>gnl|CDD|350665 cd17759, MCM8, DNA helicase Mcm8. Mcm8 plays an important role homologous recombination repair. It forms a complex with Mcm9 that is required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs)
LIVNSLCPAIYGHELVKAGLLLSLFGGKQKYADDKNRIPIRGDPHVLIVGDPGLGKSQMLQAACNIAPRG
VYVCGNTTTTSGLTVTLTKDGRSGDFALEAGALVLGDQGICGIDEFDKMGSQHQALLEAMEQQSVSLAKA
GVVCSLPARTSVIAAANPVGGHYNKGKTVSENLKMGPALLSRFDLVFILLDTPSEEHDHLLSEHHQLLRK
YISYARQYVNPVLSKDASEALQEFYLELRKQNQLADSSPITTRQLESLIRLTEARARLELREEATKEDAE
DVIEIMKES
>gnl|CDD|350666 cd17760, MCM9, DNA helicase Mcm9. Mcm9 plays an important role homologous recombination repair. It forms a complex with Mcm8 that is required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs)
EILASLCPQVFGLYNVKLAVAMVLAGGVQRIDASGTRVRGESHLLLVGDPGTGKSQFLKYAAKITPRSVL
TAGIGSTSAGLTVTAVKDGGEWNLEAGALVLADGGLCCIDEFNSLKEHDRTSIHEAMEQQTISVAKAGLV
CKLNTRTTILAATNPKGQYDPNESISVNIALASPLLSRFDLVLVLLDTKNEDWDRIISSFILENKGEPSK
SSKLWSMEKMRTYFCLIKNLRPVLSDEANAILLRYYQLQRQSDCRNAARTTIRMLESLIRLAEAHARLMF
RETVTEEDAITVVSVMESS
>gnl|CDD|350667 cd17761, MCM_arch, archaeal MCM protein. archaeal MCM proteins form a homohexameric ring homologous to the eukaryotic Mcm2-7 helicase and also function as the replicative helicase at the replication fork
EKIISSIAPSIYGHEDVKEAIALQLFGGVPKVLPDGTRIRGDIHILLVGDPGTAKSQLLKYVSKVAPRAV
YTTGKGSTAAGLTAAVVRDEGTGEWYLEAGALVLADKGIAVVDEIDKMRKEDRSALHEAMEQQTISIAKA
GIVATLNARAAVLAAANPKFGRFDSYRPVAEQIDLPPTLLSRFDLIFVLKDTPNEEKDRRLANHILDTHS
GGEMREIKPEIDPDLLRKYIAYARKNVRPVLTEEAKQLIKDFYVEMRKSGQETPSPVPITARQLEALVRL
SEASARMRLSQEVTLEDAERAIRIMLNC
>gnl|CDD|350162 cd17762, AMN, AMP nucleosidase. AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate and adenine. It is a prokaryotic enzyme which plays a role in purine nucleoside salvage and intracellular AMP level regulation. AMN is active as a homohexamer; each monomer is comprised of a catalytic domain and a putative regulatory domain. This model represents the catalytic domain. AMN belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
REEIALNRLERYTGTPLEDFQRYILLTNFDMYVDEFAERTGVPIRGGSVQMPAAHLKKEGITIINFGVGS
PNAATITDLLAVLRPKAVLMLGHCGGLRNSQEIGDFVLPIAAIRGEGTSDDYLPPEVPALPSFELQRALS
DALREVGLDYRTGTVYTTDRRNWEFDEAFKEYLRESRAIAIDMESATIFAVGFANRVPYGALLLVSDKPL
HPEGKKTKESAQEVYEKYKEEHLEIGIEALEE
>gnl|CDD|350163 cd17763, UP_hUPP-like, uridine phosphorylases similar to a human UPP1 and UPP2. Uridine phosphorylase (UP) catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose 1-phosphate. Human UPP1 has a role in the activation of pyrimidine nucleoside analogues used in chemotherapy, such as 5-fluorouracil. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPAGAALVNLSKTTDRYSMYK
VGPVLSVSHGMGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQ
VILGKVVKRPAVLDAQLAEELLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKL
YDAGVRNIEMESLCFAAFCHRAGIKAAVVCVTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK
>gnl|CDD|350164 cd17764, MTAP_SsMTAPI_like, 5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI. 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP) catalyzes the reversible phosphorolysis of 5'-deoxy-5'-methylthioadenosine (MTA) to adenine and 5-methylthio-D-ribose-1-phosphate. Sulfolobus solfataricus MTAPI will utilize inosine, guanosine, and adenosine as substrates, in addition to MTA. Two MTAPs have been isolated from S. solfataricus: SsMTAP1 and SsMTAPII, SsMTAPII belongs to a different subfamily of the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-I family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
ERVIAVGDPGRVELLSTLLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIMLGAKVI
IRLGTAGGLVPELRVGDIVVATGASYYPGGGLGQYFPDVCPPASPDPELTLELVESLSKRGLKYYVGPVF
SSDAFYAEDEEFAERWSSLGFIAVEMECATLFTLGWLRGVKAGAVLVVSDNLVKGGKLMLTKEELEEKVM
KAAKAVLEAL
>gnl|CDD|350165 cd17765, PNP_ThPNP_like, purine nucleoside phosphorylases similar to Thermus thermophiles PNP. Purine nucleoside phosphorylase (PNP) catalyzes the reversible phosphorolysis of purine nucleosides. Thermus thermophiles PNP catalyzes the phosphorolysis of guanosine but not adenosine. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
MPIHIRAEPGDVAEAVLLPGDPGRATYIAETFFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAA
IVVEELAQLGVKRLIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRALLGGEPYAPAADFELVEALYRAA
RAAGMPVHVGPVATSDLFYDPTPDGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVSDLIGDPER
RIDDEELRAGVDRMTEVALEAVVA
>gnl|CDD|350166 cd17766, futalosine_nucleosidase_MqnB, futalosine nucleosidase which catalyzes the hydrolysis of futalosine to dehypoxanthinylfutalosine and a hypoxanthine base; similar to Thermus thermophiles MqnB. Futalosine nucleosidase (MqnB, EC 3.2.2.26, also known as futalosine hydrolase) functions in an alternative menaquinone biosynthetic pathway (the futalosine pathway) which operates in some bacteria, including Streptomyces coelicolor and Thermus thermophiles. This domain model belongs to the PNP_UDP_1 superfamily which includes members which accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. PNP_UDP_1 includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Superfamily members have different physiologically relevant quaternary structures: hexameric such as the trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP, homotrimeric such as human PNP and Escherichia coli PNPII (XapA), homohexomeric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD), or homodimeric such as human and Trypanosoma brucei UP. The PNP_UDP_2 (nucleoside phosphorylase-II family) is a different structural family
MILIVTAVPLETNLERVEAEREAVLRGLLGDQRVDVLVAGVGPVNAAAATALLLERHPPDLVINAGIAGA
FPGSGLSVGDLVVASEEIAADLGVETPEGFLSLDELGFGLLRIGTDPYLNRFPLSALLLAAGLQVKTGPF
LTVSTVTGTAERAAELQRRFPAIAENMEGAAVAHAALLYGVPFLEIRGISNPVGPRDRSAWDIPEALEAL
QRAVLAL
>gnl|CDD|350167 cd17767, UP_EcUdp-like, uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases. Uridine phosphorylase (UP) is specific for pyrimidines, and is involved in pyrimidine salvage and in the maintenance of uridine homeostasis. In addition to E. coli Udp, this subfamily includes Shewanella oneidensis MR-1 UP and Plasmodium falciparum purine nucleoside phosphorylase (PfPNP). PfPNP is an outlier in terms of genetic distance from the other families of PNPs. PfPNP is catalytically active for inosine and guanosine, and in addition, has a weak UP activity. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
YHIGLKPGDVAPYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAV
EELAQLGAKTFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELG
VPYHVGITASKDSFYGGQGRPGPGLPPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVG
NRVTDEAPDEEDVAAGEERAIRVALEALK
>gnl|CDD|350168 cd17768, adenosylhopane_nucleosidase_HpnG-like, adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; similar to Burkholderia cenocepacia HpnG. adenosylhopane nucleosidase HpnG, catalyzes the second step in hopanoid side-chain biosynthesis. Hopanoids are bacterial membrane lipids. This CD belongs to the PNP_UDP_1 superfamily which includes members which accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. PNP_UDP_1 includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Superfamily members have different physiologically relevant quaternary structures: hexameric such as the trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP, homotrimeric such as human PNP and Escherichia coli PNPII (XapA), homohexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD), or homodimeric such as human and Trypanosoma brucei UP. The PNP_UDP_2 (nucleoside phosphorylase-II family) is a different structural family
AEARCLTVTGLKFEARIAIGDGLLVILSGAGPERARRAAERLLAAGARALISFGVAGGLDPALKPGDLVL
PEAVVADGERYPTDPAWRRRLLRALPAGLRVVAGPLAGSDAPVLSVADKAALHAATGAVAVDMESGAVAA
VAAEAGLPFAAIRAIADPADRSLPPAALKALDPDGSVDLLALLRALLR
>gnl|CDD|350169 cd17769, NP_TgUP-like, nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase. This subfamily is composed of mostly uncharacterized proteins with similarity to Toxoplasma gondii uridine phosphorylase (TgUPase). Toxoplasma gondii appears to have a single non-specific uridine phosphorylase which catalyzes the reversible phosphorolysis of uridine, deoxyuridine and thymidine, rather than the two distinct enzymes of mammalian cells: uridine phosphorylase (nucleoside phosphorylase-I family) and thymidine phosphorylase (nucleoside phosphorylase-II family). TgUPase is a potential target for intervention against toxoplasmosis. It belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
NRIITVGDPARARLIAKLLDKEPKVFELTSERGFLTITGRYKGVPVSIVAIGMGAPMMDFFVREARAVVD
GPMAIIRLGSCGSLDPDVPVGSVVVPSASVAVTRNYDDDDFAGPSTSSEKPYLISKPVPADPELSELLES
ELKASLGGEVVVEGLNASADSFYSSQGRQDPNFPDHNENLIDKLLKRYPGAASLEMETFHLFHLARCSRP
AQGKIRAAAAHMVFANRTSNDFISPERVHELERWAGRACLDALVA
>gnl|CDD|341407 cd17771, CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc, CBS domain protein. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
LIRREPVTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQIDLDAPISEVMTPD
PVRLPPSASAFEAALLMAEHGFRHVCVVDNGRLVGVVSERDLFSL
>gnl|CDD|341408 cd17772, CBS_pair_DHH_polyA_Pol_assoc, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
SSPVISVEPDTTIAEAAELMTRYNINALPVVDGGTGRLVGIITRQVAEKAIYHGLGDLPVSEYMTTEFAT
VTPDAPLSEIQEIIVEQRQRLVPVVEDGRLVGVITRTDLLNL
>gnl|CDD|341409 cd17773, CBS_pair_NeuB, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase. This CD contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase NeuB. NeuB catalyzes the condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine, directly forming N-acetylneuraminic acid (or sialic acid). The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
IIERNITPYVVFAEDSILNALQKISDNKSRIVFCVDEHGVLEGVLTDGDFRRWLLENPNADLSQPVSHVA
NTNFVSAPEGESPEKIEALFSSRISYIPLVDERGRLVAVARKRAAEIR
>gnl|CDD|341410 cd17774, CBS_two-component_sensor_histidine_kinase_repeat2, 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 2. This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
EVMTTRVIHAPPTASVLELAQLMAEHRVSCVVIVEEDEQQEKNKLIPVGIVTERDIVQFQALGLDLSQTQ
AQTVMSSPLFSLRPDDSLWTAHQLMQQRRIRRLVVVGEQGELLGIVTQTSLLQALDPLEMYHVIELL
>gnl|CDD|341411 cd17775, CBS_pair_bact_arch, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
CRREVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIVVEVVAKGLDPKDVTVGDIMSAD
LITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL
>gnl|CDD|341412 cd17776, CBS_pair_arch, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
MTTDVVTVDADASLEDAAERMLRNRVGSVVVTDDGTPAGILTETDALHAGYATDDPFSEIPVRAVASRPL
VTISPTATLREAAERMVDEGVKKLPVVDGLDLVGILTATDIIRAY
>gnl|CDD|341413 cd17777, CBS_arch_repeat1, CBS pair domains found in archeal proteins, repeat 1. CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here
EKELMIIASPPVLSISPSAPILSAFEKMNRRGIRRLVVVDENKLEGILSARDLVSYLGGGCLFKIVESRH
QGDLYSALNREVVETIMTPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLVLYL
>gnl|CDD|341414 cd17778, CBS_arch_repeat2, CBS pair domains found in archeal proteins, repeat 2. CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here
KVKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAMDIVKYFGSHEAKKRLTTGDID
EAYSTPVEEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVLIAL
>gnl|CDD|341415 cd17779, CBS_archAMPK_gamma-repeat1, signal transduction protein with CBS domains. Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here
SIMAIATKDVITIPPTTTIIGAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVDFLGGGSKYNLVEKKH
NGNLLAAINEPVREIMTRDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLKFL
>gnl|CDD|341416 cd17780, CBS_pair_arch1_repeat1, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
TTEFVEVDADTRLGKVRGLFEDENPKGVVVTDDGEYEGVVTERQLLQSHVEDDAKVGALVRAAPKVDRTE
DVREVARLLVEGGTKVAPVFEGGSLWGVVTADAILE
>gnl|CDD|341417 cd17781, CBS_pair_MUG70_1, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1. Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
PSPALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNP
LCVTMDTSATDALDLMVEGKFRHLPVVDDDGDVVGVLDITKCLYDAIE
>gnl|CDD|341418 cd17782, CBS_pair_MUG70_2, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2. Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
GTPPPLVSPKTTVREAARLMKENRTTAVLVMDNSGKVIGIFTSKDVVLRVLAAGLDPATTSVVRVMTPNP
ETAPPSTTILDALHKMHEGKFLNLPVVDDEGEIVGLVDVLQLTYATLQ
>gnl|CDD|341419 cd17783, CBS_pair_bac, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
NPMIPPLKPTDSVEKALDWMEEFRVSQLPVVDNGQYLGLISEDDLLELNDPEAPLSNLPLSLKDVFVYED
QHFYDVIRLASEYKLEVVPVLDEENEYLGVITVNDLLA
>gnl|CDD|341420 cd17784, CBS_pair_Euryarchaeota, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
TKNVITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHNLILDKYELGTTVEEVMVKDVA
TVHPDETLLEAIKKMDSNAPDEEIINQLPVVDDGKLVGIISDGDIIRAIK
>gnl|CDD|341421 cd17785, CBS_pair_bac_arch, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
VGDIYNLITKKPSVVHENTSIRDVIDKMIEDPKTRSVYVVDDDEKLLGIITLMELLKYIGYRFGVTIYKG
VSFGLLLRISLKEKAKDIMLSPIYVKKEDTLEEALELMVKNRLQELPVVDENGKVIGDLNSLELLK
>gnl|CDD|341422 cd17786, CBS_pair_Thermoplasmatales, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Thermoplasmatales. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
NKNFKTINWNATVFDAVKIMNENHLYGLVVKDDDGNYVGLISERSIIKRFIPRNVKPDEVPVKLVMRKPI
PKVKSDYDVKDVAAFLSENGLERCAVVDDNGRVVGIVTITDLSR
>gnl|CDD|341423 cd17787, CBS_pair_ACT, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Thermatoga in combination with an ACT domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
NRDFPTFEESATVGEVLHEMRKYETDYCIVVDEEGKFAGMVRKSKIMDEDLDKKVKEYVVEPDFYCHEED
YIEDAALLLIESHEFVLPVVNSDMKVKGVLTVFEILEALME
>gnl|CDD|341424 cd17788, CBS_pair_bac, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
AEPYPTVSLDDDALDAARLLAEERLPGLVVVDDDGRPYAVLPGSQVLRFLVPRYVRDDPALARVIDERHA
DQLCARLAGRTVADLLPAERVRLPVVGPDATLLEIAALMARLRSPLVAVVDRKGRLLGVVTASRLLE
>gnl|CDD|341425 cd17789, CBS_pair_plant_CBSX, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase)
PKGKLHVVKPNTTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLLALDSISGRSQTDNNFPPADSTW
KTFNEVQKLLSKTNGKVVGDVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVVR
A
>gnl|CDD|341356 cd17790, 7tmA_mAChR_M1, muscarinic acetylcholine receptor subtype M1, member of the class A family of seven-transmembrane G protein-coupled receptors. Muscarinic acetylcholine receptors (mAChRs) regulate the activity of many fundamental central and peripheral functions. The mAChR family consists of 5 subtypes M1-M5, which can be further divided into two major groups according to their G-protein coupling preference. The M1, M3 and M5 receptors selectively interact with G proteins of the G(q/11) family, whereas the M2 and M4 receptors preferentially link to the G(i/o) types of G proteins. Activation of mAChRs by agonist (acetylcholine) leads to a variety of biochemical and electrophysiological responses. M1 is the dominant mAChR subtype involved in learning and memory. It is linked to synaptic plasticity, neuronal excitability, and neuronal differentiation during early development. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes
VLIVITTGILSLVTVTGNLLVLISFKVNSELKTVNNYFLLSLACADLIIGAFSMNLYTTYILMGHWALGT
VACDLWLALDYVASNASVMNLLIISFDRYFSITRPLTYRAKRTPRRAAIMIGLAWLISFVLWAPAILFWQ
YLVGERTVLAGQCYIQFLSQPIITFGTAIAAFYLPVTIMIILYWRIYRETIKEKKAARTLSAILLAFILT
WTPYNIMVLVSTFCKDCVPKTLWELGYWLCYVNSTVNPMCYALCNKSFRDTF
>gnl|CDD|341490 cd17791, HipA-like, serine/threonine-protein kinases similar to HipA and CtkA. This family contains serine/threonine-protein kinases similar to Escherichia coli HipA, a type II toxin-antitoxin (TA) system HipA family toxin that phosphorylates Glu-tRNA-ligase (GltX), preventing it from being charged, leading to an increase in uncharged tRNA(Glu), and is the toxin component of the HipA-HipB TA module, as well as similar to the Helicobacter pylori serine/threonine-protein kinase CtkA (proinflammatory kinase), which has been shown to be secreted by the bacteria and to induce cytokines in gastric epithelial cells relevant to chronic gastric inflammation
SVAGAQGKISLFYNGNDWCIPKGITPETHIVKFPPKPSTHKEMSYTNGVFNEYVACHLAKSLGLNVQETL
IGTYGNKIALAVERFDRRWNAERTVLLRYELVDFCQLKGTMISLKYKSGKGTNLNRVLYAIDHFIEPKVL
KCDFWDMFVFDTLLGNFDRHNKNWSFFRASNKEYQITPIYDCGSCLYPQELNARIYNFPQLAMKDDNDKK
INYYDIYTQTNLATAKVLRFPNKDCLDALLRIARRIPMALDKVHSILPNTEIHKEFLVTMLDERKLKIID
RAHT
>gnl|CDD|341491 cd17792, CtkA, serine/threonine-protein kinase CtkA and similar proteins. The Helicobacter pylori serine/threonine-protein kinase CtkA (proinflammatory kinase), encoded by the jhp940 gene, has been shown to be secreted by the bacterium and to induce cytokines in gastric epithelial cells. It may play a role in chronic gastric inflammation. CtkA autophosphorylates itself at a threonine residue near the N-terminus and it translocates into cultured human cells. It also enhances phosphorylation of the NF-kappaB p65 subunit at Ser276 in human epithelial cancer cells; phosphorylation at this position is known to activate the transcriptional activity of NF-kappaB
ESSRFYGGAAGKKIGILYNGELYMLKFPKSTKELKGDISYTNSPLSEYIGSHIYESLGIPVQETILGTYK
GKIVVACKDFTEDNERLYEFSQLKNSILDESSSSGYGTELSDILEVIEEQPLLINIEGLKERFWDMFVVD
ALIGNFDRHNGNWGFLVNEDTGEVELAPVYDNGSSLYPKLSDEKIKKILKDEEEIEKRIYNFPTSAIKLN
GKKINYFEFITSLENEDCNKALKRIVPKIDMDKIDEIIDSIPEISEIRKEFYKKMLKERYEKILLPAYEK
L
>gnl|CDD|341492 cd17793, HipA, type II toxin-antitoxin sytem toxin HipA and similar proteins. This family contains type II toxin-antitoxin (TA) system HipA family toxins similar to Escherichia coli and Shewanella oneidensis HipA, which is a serine/threonine-protein kinase that phosphorylates Glu-tRNA-ligase (GltX), preventing it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to persistence and multidrug resistance. HipA is the toxin component of the HipA-HipB TA module that is a major factor in persistence and bioflim formation; its toxic effect is neutralized by its cognate antitoxin HipB. HipA, with HipB, acts as a a corepressor for transcription of the hipBA promoter. Structures of HipAB:DNA complexes from both Escherichia coli and Shewanella oneidensis reveal distinct complex assembly
DADGTLSFRYAPDWLANPGAFPLSLSLPLRAEPFGDDEVRPFFANLLPEGDVRRLIARRLGVSRSDDFAL
LEAIGGDCAGAVSILPEGLRLSLAGAQDKLPVLIDDGRIALPLGGAPSTHILKPDIRRLPDSVENEAFCM
RLARACGLDVPEVEILSAGDVPALLVERYDRVIDEDGVVRRLHQEDFCQALGLPPELKYERDGGPSLADC
FALLREHSRNPARDRQALLRWVIFNLLIGNADAHAKNLSLLYRPGGPRLAPFYDLVSTRVYPDLSRKLAM
AIGGERRPDEITPRHWEAFAEELGLRPRLVRRRLAELAKRLPAALESVAEELSSLGAEVPLLDRIAELIL
KRCRRLLA
>gnl|CDD|341493 cd17808, HipA_Ec_like, type II toxin-antitoxin sytem toxin HipA from Escherichia coli and similar proteins. This family contains type II toxin-antitoxin (TA) system HipA family toxins similar to Escherichia coli HipA, a serine/threonine-protein kinase that phosphorylates Glu-tRNA-ligase (GltX), preventing it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to persistence and multidrug resistance. HipA is the toxin component of the HipA-HipB TA module that is a major factor in persistence and bioflim formation; its toxic effect is neutralized by its cognate antitoxin HipB. HipA, with HipB, acts as a a corepressor for transcription of the hipBA promoter. In the Escherichia coli HipAB:DNA promoter complex, HipA forms a dimer and each HipA monomer interacts with a HipB homodimer which binds DNA. The HipAB component of the complex is composed of two HipA and four HipB subunits
RSNGKIRFTYDDEWLASPDATPLSLSLPLTRGRHRGDAVRAFLDNLLPDNDEVRRRWARRFGVSSTNPFS
LLAHIGRDCAGAVQFLPPDELPAPERAGELRPLSDAEIAERLRALRADPGGGSWDDDDGRFSLAGAQEKT
ALLRHDGRWFEPTGATPTTHILKPGIGRLPDSDLNEHLCLRAARALGLPVARTEILEFGGERALVVERFD
RRRDDDGTVLRLHQEDLCQALGVPPSRKYESDGGPGAADIARLLRGSSDAEADRLRFFRALAFNWLIGAT
DAHAKNYSLLLDPGGRVRLAPLYDVASALPYPGRGPPRKLKLAMSIGGEYRFGEITPRHWRRFARRAGLD
PDRVLARVREIAERLPDAFEAALAELPAGFPAALADRLVDGVASRCRRLLR
>gnl|CDD|341494 cd17809, HipA_So_like, type II toxin-antitoxin sytem toxin HipA from Shewanella oneidensis and similar proteins. This family contains type II toxin-antitoxin (TA) system HipA family toxins similar to Shewanella oneidensis HipA, a serine/threonine-protein kinase that phosphorylates Glu-tRNA-ligase (GltX), preventing it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to persistence and multidrug resistance. HipA is the toxin component of the HipA-HipB TA module that is a major factor in persistence and bioflim formation; its toxic effect is neutralized by its cognate antitoxin HipB. HipA, with HipB, acts as a a corepressor for transcription of the hipBA promoter. In the Shewanella oneidensis HipAB:DNA promoter complex, HipB forms a dimer that binds the duplex operator DNA, with each HipB monomer interacting with separate HipA monomers. The HipAB component of the complex is composed of two HipA and two HipB subunits
AETDQWSFRYTPDWLADGFPLSPHLPLTEEEDGATSRPVRWFFENLLPEGDALDDLAASLRISKANIFAL
LRAIGAETAGALTFLPPGAEAPPTGLRPLKEEELEERIRRRRPRPFAVWDGKKRLSLAGVQDKLAVYIDD
GELFLAEGSLASTHILKPEPASADYPHLVINEFFCMRLAKRVGLPVAEVQLRHVPEPVLLVERFDRRIAA
GGRVRRLHIIDACQALGLPPSFKYERNFGSGRDVKNIREGVSFEKLFSLLEQCRNPAAARLQLLRWALFN
LLIGNSDAHGKNISFFVGPSGIELAPAYDLVSVDAYAGWIDQELAMAIGDAFDPDEVTAYQLAAFAEECG
LPPRLLQRLLSRMAKRLERAAAEVIDELALLTEVERSFVAELKASVLKRASRFLA
>gnl|CDD|341489 cd17814, Fe-ADH-like, iron-containing alcohol dehydrogenases (Fe-ADH)-like. This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized
KFVAPEFIFGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDF
EVMEGAELYREEGCDGIVAVGGGSPIDCAKGIGIVVSNGGHILDYEGVDKVRRPLPPLICIPTTAGSSAD
VSQFAIITDTERRVKMAIISKTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLH
ALEAIRLISENLPKAVADPDDLEAREKMMLASLQAGLAFSNASLGAVHAMAHSLGGLLDLPHGECNALLL
PHVIRFNFPAAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAK
RAMKDPCLVTNPRRPTREDIEEIY
>gnl|CDD|349777 cd17868, GPN, GPN-loop GTPase. GPN-loop GTPases are deeply evolutionarily conserved family of three small GTPases, Gpn1, 2, and 3. They form heterodimers, interact with RNA polymerase II and may function in nuclear import of RNA polymerase II
YAILVIGPAGSGKTTFCKNMKEHLRARKRNPYVINLDPGNINEPLDYDIDIRDLIKYDDIMEELDLGPNG
SIVYSLEYFEKNFDWFEKKLENEDKNPHYILFDCPGQIELFTHSDSLPKIIERFASWFISVVIVNLIDSQ
FLSDKSKFLSNLLIALSSMFRLELPQINVISKMDLLDFIPLNYSDEESIKLLLQNIDK
>gnl|CDD|349778 cd17869, TadZ-like, pilus assembly protein TadZ. Pilus assembly protein TadZ is involved in the production of a variant of type IV pili. It is part of the SIMIBI superfamily which contains a variety of proteins which share a common ATP-binding domain. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion
DATSVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQSTDVFFGASGRYLMSDHLYTLKSRKA
NLADKLESCVKQHESGVYYFSPFKSALDILEIKKDDILHMITKLVEAHAYDYIIMDLSFEFSSTVCKLLQ
ASHNNVVIALQDANSSYKLNKFLRALEDLFQENFSYIYNKYSNNVEDSLSTNIEKKIIGGAPRYEHALDV
RQIIEALAK
>gnl|CDD|349779 cd17870, GPN1, GPN-loop GTPase 1. GPN-loop GTPase 1 (GPN1, also kown as MBD2-interacting protein or MBDin, RNAPII-associated protein 4, and XPA-binding protein 1) is a GTPase is required for nuclear targeting of RNA polymerase II. It forms heterodimers with GPN3
VVIIVVGMAGSGKTTFVQRLNAYLHDNKKPPYVINLDPAVKSLPYPPNIDIRDTVNYKEVMKQYGLGPNG
AIVTSLNLFATKFDQVINLIEKRASELDYVIIDTPGQIEVFTWSASGSIITEALASSFPTVVVYVVDTPR
CTSPITFMSNMLYACSILYKTKLPFILVFNKTDVVSHDFAIEWMEDFESFQDALKEDSSYMSSLSRSMSL
VLDEFYNNLRVVGVSAKTGEGFEELLEAIDE
>gnl|CDD|349780 cd17871, GPN2, GPN-loop GTPase 2. GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). It forms heterodimers with GPN1 or GPN3
FGQVVIGPPGSGKTTYCKGMQQFLSALGRKVAVVNLDPANEFLPYPCDVDIRELITVEDVMEELKLGPNG
GLLYCMEYLEKNIDWLIDKLKKLKDSYLIFDCPGQVELYTHHNSLRNILDKLQKWLYRLVAVHLVDSHYC
SDPSKFISALLLSLSTMLRLELPHVNVLSKIDLVSFIPLDVQDKESMLRLLKAIDK
>gnl|CDD|349781 cd17872, GPN3, GPN-loop GTPase 3. GPN-loop GTPase 3 (GPN3) is a small GTPase that is required for nuclear targeting of RNA polymerase II. It forms heterodimers with GPN1
YAQLVMGPAGSGKSTYCSTLQEHCETLGRSVHVVNLDPAAEEFEYPVSIDIRDLISLEDVMEELGLGPNG
GLVYCMEYLLENLDWLEEQLGDYEDDYLIFDCPGQIELYTHLPVMKRLVDALQRWGFRLCAVYLLDSQFI
SDASKFISGVLSALSAMIQLELPHVNVLTKMDLVSFLPLDITDEESINNVLSQIDN
>gnl|CDD|349782 cd17873, FlhF, signal-recognition particle GTPase FlhF. FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR)
RVIALVGPTGVGKTTTLAKLAARYVLKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEVAEDPEDLAD
ALERLSDRDLILIDTAGRSPRDKEQLEELKELLGAGEDIEVHLVLSATTKAKDLKEIIERFSPLGYRGLI
LTKLDETTSLGSVLSVLAESQLPVSYVTTGQRVPEDIEVASPLRLARLL
>gnl|CDD|349783 cd17874, FtsY, signal recognition particle receptor FtsY. FtsY, the bacterial signal-recognition particle (SRP) receptor (SR), is homologous to the SRP receptor alpha-subunit (SRalpha) of the eukaryotic SR. It interacts with the signal-recognition particle (SRP) and is required for the co-translational membrane targeting of proteins
FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAV
AFDAIQAAKARGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKE
FNEAVGLTGIILTKLDGTAKGGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL
>gnl|CDD|349784 cd17875, SRP54_G, GTPase domain of the signal recognition 54 kDa subunit. The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain
NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKI
AKEGVEKFKKEKFDIIIVDTSGRHKQEEELFEEMKQISDAVKPDEVILVIDASIGQAAEDQAKAFKEAVD
IGSVIITKLDGHAKGGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL
>gnl|CDD|349785 cd17876, SRalpha_C, C-terminal domain of signal recognition particle receptor alpha subunit. The signal-recognition particle (SRP) receptor (SR) alpha-subunit (SRalpha) of the eukaryotic SR interacts with the signal-recognition particle (SRP) and is essential for the co-translational membrane targeting of proteins
YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAV
AKEAIKYARDQGFDVVLIDTAGRMQNNEPLMRALAKLIKENNPDLVLFVGEALVGNDAVDQLKKFNQALA
DYSPSDNPRLIDGIVLTKFDTIDDKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL
>gnl|CDD|350170 cd17877, NP_MTAN-like, nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases. This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs), as well as futalosine nucleosidase and adenosylhopane nucleosidase. Bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family
IGIIAAMPEEISPLLRRIEVLQKVRLGGFRFYRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLII
STGFAGGLDPGLAVGDLVIADRVLYHDGDVPAGLEADEKLVALAEELAAGLNLKVHRGTIITVDAIVRKS
AEKAALAARFPALAVDMESAAIAQVAAARGIPFLAIRAISDPADEELPFSIEEFLDEEGAVRPGAVLLTL
>gnl|CDD|350625 cd17880, D-Ala-D-Ala_dipeptidase, D-Ala-D-Ala_dipeptidase. This family contains D-Ala-D-Ala dipeptidase enzymes which include D-alanyl-D-alanine dipeptidase vanX and Aad, among others. VanX is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. It fasmily includes Lactobacillus Aad peptidase and belongs in the MEROPS peptidase family M15, subfamily D
TGVLKRLDKARLTAADIGWELLVFDAYRPIAAQQFMVQHTFAPIVARDGLQGQHQVYQIWAVPNNNVLTP
SPHSRGAAIDLTLRRELLNTIMESGGFLRHSGEWWHFSLG
>gnl|CDD|467615 cd17892, GAPDH_N_E4PDH, N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins. E4PDH (EC 1.2.1.72), also called E4P dehydrogenase, catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate (E4P) to 4-phosphoerythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase (GADPH), whose substrate differs only in the lack of one carbon relative to E4P. E4PDH proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal GADPH-like catalytic domain and are members of the GAPDH family of proteins
YRVAINGYGRIGRNVLRALYESGRRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNG
DKIRVLHEPDPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVDATIVYGINQDL
LRAEHRIVSNASDNEWGFANRMLDTALHM
>gnl|CDD|467520 cd17894, ASADH_USG1_N, N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins. The family includes Escherichia coli USG-1 protein, Pseudomonas aeruginosa USG-1 homolog proteins and similar proteins. Although their biological function remains unknown, they are homologs to aspartate beta-semialdehyde dehydrogenase (ASADH) which contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain. However, USG-1 proteins lack the conserved active site residues of the ASADH protein C-terminal domain
YRIAVVGATGLVGKELLELLEERGFPVGRLRLLDSEESAGELVEFGGEPLDVQDLDEFDFSDVDLVFFAG
PAEVARAYAPRARAAGCLVIDLSGALRSDPDVPLVVPGVNPEALAAAAERRVVAVPNNRRGAALNAVEIA
ELLL
>gnl|CDD|467521 cd17895, AGPR_1_N, N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins. AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate; the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both the arginine and lysine biosynthetic pathways
IKVGIIGASGYTGAELLRLLLNHPEVEIVALTSRSYAGKPVSEVFPHLRGLTDLTFEPDDDEEIAEDADV
VFLALPHGVSMELAPKLLEAGVKVIDLSADFRLKDPETYEKWYGFEHAAPELLKEAVYGLPELNREEIKK
ARLVANPNLVKGAAGQAVQNMNLMFGLDET
>gnl|CDD|467522 cd17896, AGPR_2_N, N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and similar proteins. AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate; the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 2 AGPR family
PKVFIDGEAGTTGLQIRERLAGRSDIELLSIPEDKRKDPAARAELLNAADIAILCLPDDAAREAVALVTN
PRTRIIDASTAHRTAPGWAYGFPELSPEQREKIATSKRVANPGNLGKGASGAAVQNMNLMLG
>gnl|CDD|350087 cd17900, ArfGap_ASAP3, ArfGAP domain of ASAP3 (ArfGAP with ANK repeat and PH domain-containing protein 3). The ArfGAPs are a family of multidomain proteins with a common catalytic domain that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. ASAP-subfamily GAPs include three members: ASAP1, ASAP2, ASAP3. The ASAP subfamily comprises Arf GAP, SH3, ANK repeat and PH domains. From the N-terminus, each member has a BAR, PH, Arf GAP, ANK repeat, and proline rich domains. Unlike ASAP1 and ASAP2, ASAP3 do not have an SH3 domain at the C-terminus. ASAP1 and ASAP2 show strong GTPase-activating protein (GAP) activity toward Arf1 and Arf5 and weak activity toward Arf6. ASAP1 is a target of Src and FAK signaling that regulates focal adhesions, circular dorsal ruffles (CDR), invadopodia, and podosomes. ASAP1 GAP activity is synergistically stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. ASAP2 is believed to function as an ArfGAP that controls ARF-mediated vesicle budding when recruited to Golgi membranes. It also functions as a substrate and downstream target for protein tyrosine kinases Pyk2 and Src, a pathway that may be involved in the regulation of vesicular transport. ASAP3 is a focal adhesion-associated ArfGAP that functions in cell migration and invasion. Similar to ASAP1, the GAP activity of ASAP3 is strongly enhanced by PIP2 via PH domain. Like ASAP1, ASAP3 associates with focal adhesions and circular dorsal ruffles. However, unlike ASAP1, ASAP3 does not localize to invadopodia or podosomes. ASAP 1 and 3 have been implicated in oncogenesis, as ASAP1 is highly expressed in metastatic breast cancer and ASAP3 in hepatocellular carcinoma
LTKLLIAEVKSRPGNSQCCDCGAPDPTWLSTNLGILTCIECSGIHRELGVRYSRIQSLTLDLLSTSELLL
AVSMGNTRFNEVMEATLPAHGGPKPSAESDMGTRKDYIMAKYVEHRFVRKRCTP
>gnl|CDD|350088 cd17901, ArfGap_ARAP1, ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing protein 1. The ARAP subfamily includes three members, ARAP1-3, and belongs to the ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) family of proteins that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. The function of Arfs is dependent on GAPs and guanine nucleotide exchange factors (GEFs), which allow Arfs to cycle between the GDP-bound and GTP-bound forms. In addition to the Arf GAP domain, ARAPs contain the SAM (sterile-alpha motif) domain, 5 pleckstrin homology (PH) domains, the Rho-GAP domain, the Ras-association domain, and ANK repeats. ARAPs show phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3)-dependent GAP activity toward Arf6. ARAPs play important roles in endocytic trafficking, cytoskeleton reorganization in response to growth factors stimulation, and focal adhesion dynamics. ARAP1 localizes to the plasma membrane, the Golgi complex, and endosomal compartments. It displays PI(3,4,5)P3-dependent ArfGAP activity that regulates Arf-, RhoA-, and Cdc42-dependent cellular events. For example, ARAP1 inhibits the trafficking of epidermal growth factor receptor (EGFR) to the early endosome
SEVAEKIWSVESNRFCADCGSPKPDWASVNLCVVICKRCAGEHRGLGPSVSKVRSLKMDRKVWTEELIEL
FLLLGNGKANQFWAANVPPSEALCPSSSSEERRHFITAKYKEGKYR
>gnl|CDD|350089 cd17902, ArfGap_ARAP3, ArfGap with Rho-Gap domain, ANK repeat and PH domain-containing protein 3. The ARAP subfamily includes three members, ARAP1-3, and belongs to the ADP-ribosylation factor GTPase-activating proteins (Arf GAPs) family of proteins that promotes the hydrolysis of GTP bound to Arf, thereby inactivating Arf signaling. The function of Arfs is dependent on GAPs and guanine nucleotide exchange factors (GEFs), which allow Arfs to cycle between the GDP-bound and GTP-bound forms. In addition to the Arf GAP domain, ARAPs contain the SAM (sterile-alpha motif) domain, 5 pleckstrin homology (PH) domains, the Rho-GAP domain, the Ras-association domain, and ANK repeats. ARAPs show phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3)-dependent GAP activity toward Arf6. ARAPs play important roles in endocytic trafficking, cytoskeleton reorganization in response to growth factors stimulation, and focal adhesion dynamics. ARAP3 possesses a unique dual-specificity GAP activity for Arf6 and RhoA regulated by PI(3,4,5)P3 and a small GTPase Rap1-GTP. The RhoGAP activity of ARAP3 is enhanced by direct binding of Rap1-GTP to the Ras-association (RA) domain. ARAP3 is involved in regulation of cell shape and adhesion
YEVAEKIWSNKANRFCADCHASSPDWASINLCVVICKQCAGQHRSLGSGISKVQSLKLDTSVWSNEIVQL
FIVLGNDRANRFWAARLPASEALHPDATPEQRREFISRKYREGRFR
>gnl|CDD|350090 cd17903, ArfGap_AGFG2, ArfGAP domain of AGFG2 (ArfGAP domain and FG repeat-containing protein 2). The ArfGAP domain and FG repeat-containing proteins (AFGF) subfamily of Arf GTPase-activating proteins consists of the two structurally-related members: AGFG1 and AGFG2. AGFG2 is a member of the HIV-1 Rev binding protein (HRB) family and contains one Arf-GAP zinc finger domain, several Phe-Gly (FG) motifs, and four Asn-Pro-Phe (NPF) motifs. AGFG2 interacts with Eps15 homology (EH) domains and plays a role in the Rev export pathway, which mediates the nucleocytoplasmic transfer of proteins and RNAs. In humans, the presence of the FG repeat motifs (11 in AGFG1 and 7 in AGFG2) are thought to be required for these proteins to act as HIV-1 Rev cofactors. Hence, AGFG promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm, which is an essential step for HIV-1 replication
CRRVRELGGCSAANRHCFECAQRGVTYVDITVGSFVCTTCSGLLRGLNPPHRVKSISMTTFTEPEVLFLQ
ARGNEVCRKIWLGLFDARTSLIPDSRDPQKVKEFLQEKYEKKRWYV
>gnl|CDD|380783 cd17904, PFM_monalysin-like, pore-forming module of Pseudomonas entomophila monalysin and similar aerolysin-type beta-barrel pore-forming proteins. Monalysin plays a role in Pseudomonas entomophila virulence against Drosophila, contributing to host intestinal damage and lethality. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin)
PVKKGSYEIDRYLFGGDVPKPGCWVEGLTVYGDIRIGGQNWATYTRPVFAYLEYVDTIRVPSNVEQTYEV
TKKKGFSKSFTSSVEVKYSVGAGIGGVNVSSEITTGFSYSETWSSPSTTTQTLELKGPGTYYVYQVHLVY
AHCATSAGDLCANKFFNYGKRYKRGGREDLYFLSSVATDQLVTVPYENSVDPLSWDELQQYVLNEG
>gnl|CDD|381733 cd17905, CheC-like, chemotaxis protein CheC; includes CheC classes I, II, and III. This family contains chemotaxis protein CheC that acts as a weak CheY-P phosphatase but shows increased activity in the presence of CheD. This CheC family includes three classes: class I containing Bacillus subtilis CheC which might function as a regulator of CheD; class II CheCs that likely function as phosphatases in systems other than chemotaxis; and class III CheCs that are found chiefly in the archaeal class Halobacteria and might function similarly as class I CheCs. Class I CheCs contain two active sites with the consensus sequence ([DS]xxxExxNx(22)P), with four conserved residues thought to form the phosphatase active site; class II and class III CheCs have only one actve site
EIIANIGADNAARALSKLLGEEVEISLPSVRLVPLEEIPELLGGPEDEVVGVYLRVEGDINGQLLLVFPE
ESALELADLLLGRPPGTTKELDELERSALGEVGNILGSAFLNALADLLGLELRPSPPAVVVDMAGAILEF
AVAEQAAESDEVLLIETEFEVEDSELDGHFLLL
>gnl|CDD|381734 cd17906, CheX, chemotaxis phosphatase CheX. This family contains CheX CheY-P phosphatase which is very closely related to CheC chemotaxis phosphatase; both dephosphorylate CheY, although CheC requires binding of CheD to achieve the level of activity of CheX. CheX has been shown to be the most powerful CheY-P phosphatase of the CheC-FliY-CheX (CXY) family. Structural and functional data of CheX and its CheY3 substrate in Borrelia burgdorferi (the causative agent of Lyme disease) bound to the phosphoryl analog BeF3(-) and Mg2+ reveal a unique mode of binding, but a catalytic mechanism which is virtually identical to that used by the structurally unrelated CheZ, providing a striking example of convergent evolution. Thus, CheX is quite divergent from the rest of the CXY family; it forms a dimer and some may function outside chemotaxis. The data also suggest a possible CheX regulatory mechanism through dissociation of the CheX homodimer
VEYINPFIEATKEVFKTMLGLEVEPGKPYLKKDPFLSGDVSGIIGITGDLKGSVIISFSEETALKIASAM
LGEEVTELDEMVKDAIGELANMIAGNAKTKLSEKGIDIDISPPTVITGKNHKISSPKGPTIVIPFETEGG
EFEVEIAL
>gnl|CDD|381735 cd17907, FliY_FliN-Y, flagellar motor switch protein FliY. This family contains the flagellar rotor protein FliY, a highly conserved and essential member of the CheC phosphatase family, that distinguishes flagellar architecture and function in different types of bacteria. Unlike CheC and CheX, FliY is localized in the flagellar switch complex, which also contains the stator-coupling protein FliG and the target of CheY-P, FliM, all present in many copies, and together corresponding structurally to the C-ring of the flagellar basal body. FliY structure resembles that of the rotor protein FliM but contains two active centers for CheY dephosphorylation. In bacteria such as Thermotogae and Bacilli, FliY is fused to FliN. It incorporates properties of the FliM/FliN rotor proteins and the CheC/CheX phosphatases to serve multiple functions in the flagellar switch. FliY seems to act on CheY-P constitutively, as compared to CheC and CheX that appear to be primarily involved in restoring normal CheY-P levels
LSDEEKDALGEIGNISMGSAATALSTLLNKKVTITTPRVSVVTIEELLEEFPEPYVVVKVDYTEGLEGSN
VLILKQEDAAVIADLMMGGDGTNPDEELDELHLSAVSEAMNQMMGSAATSLSEMLGKKVDISPPEVELVD
FEEELELPPLEDEDKVVKVSFRLKIEDLIDSEIMQLMPIDFAKELVSKLLG
>gnl|CDD|381736 cd17908, FliM, flagellar protein FliM. This family contains bacterial flagellar protein FliM which is localized in the flagellar switch complex along with FliG and FliY; all are present in many copies, and together they correspond structurally to the C-ring of the flagellar basal body. FliM does not contain the CheC consensus sequence of the phosphatase active site ([DS]xxxExxNx(22)P) and is not a CheY-P phosphatase. FliM sits in the center of the rotor with the N-terminal region interacting with the signaling protein, phosphorylated CheY (CheY-P). The activated form of CheY destabilizes the parallel arrangement of FliM molecules, and perturbs FliG alignment in a process that may reflect the onset of rotation switching. This suggests a model of C-ring assembly in which intermolecular contacts among FliG domains provide a template for FliM assembly. Recent data show that binding of FliM to spermine synthase, SpeE, contributes to flagellar motility, an association that is unique to Helicobacter species
REQLRTLEVIHERFARLLSTSLSALLRTPVEVSLESVEQLTYGEFLASLPNPTSLAVFSLEPLKGRALLE
IDPSLVFALVDRLLGGSGEAPKIEGREFTEIELRLLRRLLERLLEDLEEAWSPVLPLEFELERIETNPQF
AQIAPPNEPVVVVTFEVKIGEREGTINLCIPYSALEPILEK
>gnl|CDD|381737 cd17909, CheC_ClassI, chemotaxis protein CheC, Class I. This subfamily contains Class I CheC proteins with phosphatase activity. The Class I cheC genes are generally found in firmicute and archaeal chemotaxis operons with cheD, usually translationally coupled. Class I CheCs interact with the CheD protein which is responsible for deamidation of certain glutamine residues to glutamates on the chemotaxis receptor proteins. This family contains two active sites with the consensus sequence ([DS]xxxExxNx(22)P), with four conserved residues thought to form the phosphatase active site. The C-terminal helix of CheC acts as a mimic of the natural enzymatic target of CheD, the alpha-helical receptors, and serves as the binding site for CheD. The CheC/CheD heterodimerization increases CheY-P phosphatase activity five-fold. Class I CheCs are involved in adaptation of the chemotaxis system
QLDALKEIGNIGAGNAATALSQLLGKKVDMSVPEVKILPFEEVPELLGGPEEVVAGVLLRIEGDISGSIL
FIFPEESALKLVDLLLGREPGSTEELDEMELSALKEIGNILAGSYLNALSDFLGLTLLPSVPSLAVDMAG
AILSSVLIELGQESDEALLIETEFSIEEEKIEGHFLLLPDPESLEKLLK
>gnl|CDD|381738 cd17910, CheC_ClassII, chemotaxis protein CheC, Class II. This family contains class II CheC proteins found in proteobacteria, which diverge from class I CheCs in sequence conservation and lack critical well-conserved residues for CheD binding. These proteins are likely to be dedicated phosphatases. The class II cheC genes are not found in chemotaxis operons, but in operons containing more archetypical two-component signaling components, non-signaling operons, or as orphans. Thus, class II CheCs appear to be involved in non-chemotactic two component systems. Class II CheCs lack the first of the two phosphatase active sites of class I CheCs, and retain the second active site of class I CheCs
DQRDALQELFNIGMGRAAASLSELLGEFVTLSVPEVELLSPSELAMALGADGDERVSAVSQGFSGSFSGE
ALLLFPEDSSLELVALLLGEEEPLEDLDELEQEALLEVGNILLNACLGSLANQLDLELSYSLPVVLEGSL
EELLLLNGSDEWDYVLLIEIDFTIEDRDIEGDLLLLLDEDSLDALLE
>gnl|CDD|381739 cd17911, CheC_ClassIII, chemotactic protein CheC, Class III. This family contains class III CheC proteins, present chiefly in the archaeal class Halobacteria. Sequence analysis shows that class III CheC proteins are structurally and functionally similar to class I CheCs, and not to CheX, despite the fact that both class III CheCs and CheX lack the first of the two phosphatase active sites of class I CheCs, and retain the second active site. Mutation analysis shows that the second active site is more important for function that the first one, suggesting that class III proteins arose by loss of the unnecessary first active site through mutational shift. All chemotactic archaea have a CheC homologue
DIDKLETFNELAREGAERAADSLSQMTGIETTVEVTKVSFVPIEDIPEEFGDEEYVGVRVELEGGLSGYT
LLLFDEESARRLAEALLPGMGDDELSEMAESAIEELGNIMTSGFIDGWANVLGTTIDISPPTYVEDMGSA
ILDPVLADLGDDDLAFVFDSRIEAVDTEIDFRIYLLPDPESLVELLD
>gnl|CDD|350670 cd17912, DEAD-like_helicase_N, N-terminal helicase domain of the DEAD-box helicase superfamily. The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region
NILHLGPTGSGKTLVAIQKIASAMSSGKSVLVVTPTKLLAHEILIVIDEIQXILDPAAGWAWATRALLGL
KAEKVIGVGAT
>gnl|CDD|350671 cd17913, DEXQc_Suv3, DEXQ-box helicase domain of Suv3. Suppressor of var1 3-like protein (Suv3) is a DNA/RNA unwinding enzyme belonging to the class of DexH-box helicases. It localizes predominantly in the mitochondria, where it forms an RNA-degrading complex called mitochondrial degradosome (mtEXO) with exonuclease PNP (polynucleotide phosphorylase), that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Suv3 plays a role in the RNA surveillance system in mitochondria; it regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. It also confers salinity and drought stress tolerance by maintaining both photosynthesis and antioxidant machinery, probably via an increase in plant hormone levels such as gibberellic acid (GA3), the cytokinin zeatin (Z), and indole-3-acetic acid (IAA). Suv3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
RKIIFHAGPTNSGKTYHALQRLKSAKSGVYCGPLRLLAWEVYERLNAEGVPCDLVTGQERREVEGATHVS
CTVEMASISEPYDVAVIDEIQMIGDPQRGWAWTRALLGLPAEEIHLCGDPSALPLVRKLAETTGDELEVR
EY
>gnl|CDD|438706 cd17914, DExxQc_SF1-N, DEXQ-box helicase domain of superfamily 1 helicase. The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LSLIQGPPGTGKTRVLVKIVAALMQNKNGEPGRILLVTPTNKAAAQLDNILVDEAAQILEPETSRLIDLA
LDQGRVILVGDHDQLGPVWRGAVLAKICNEQSLFTRLVRLGVSLIRLQVQY
>gnl|CDD|350673 cd17915, DEAHc_XPD-like, DEAH-box helicase domain of XPD family DEAD-like helicases. The xeroderma pigmentosum group D (XPD)-like family members are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
GGHVALESPTGSGKTLSLLCSALSYQREFHKTKVLYCSRTHSQIEQIIRELRKLLEKRKIRALALSSRDA
DIVVLPYPYLLDARIREFIGIDLREQVVIIDEAHNLDERSVIITSGTLSPLDIYSKILGIRNMLVLAV
>gnl|CDD|350674 cd17916, DEXHc_UvrB, DEXH-box helicase domain of excinuclease ABC subunit B. Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II) and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA, but its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a member of the DEAD-like helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
FKLVSPFKPAGDQPQAIAKLVEGLKRGVKFQTLLGVTGSGKTFTIANVIAQVNKPTLVIAHNKTLAAQLY
SEFKEFFPENAVEYFVSYYDYYQPEAYVPQTDTYIEKDASINDEIDRLRHSATRSLLERRDVIVVASVSC
IYERAIKSIEEELEERLKYFRAQGKLLEAQRLEQRTRYDLEMLREMGFCSGIENYSRHLSGRKPGEPPYT
LLDYFPDDFLLVIDESHVTVPQLRGMYNGDRSRKQSLVDYGFRLPSALDNRPLKFEEFEEKVNQVIYVSA
TPGDYELEHSGQVVEQIIR
>gnl|CDD|438707 cd17917, DEXHc_RHA-like, DEXH-box helicase domain of DEAD-like helicase RHA family proteins. The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRF
ESKTSSKTRIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSA
TLDAEKFSSYFGGAPVIHI
>gnl|CDD|350676 cd17918, DEXHc_RecG, DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins. The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
DRALIQELCKSLPFSLTKDQAQAIKDIEKDLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAIL
VPTEILAHQHYEEARKFLPFINVELVTGGTKAQILSGISLLVGTHALLHLDVKFKNLDLVIVDEQHRFGV
AQREALYNLGATHFLEATATPIPRTLALALSGLLDLSVID
>gnl|CDD|350677 cd17919, DEXHc_Snf, DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins. Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFE
KWTPDLRVVVYHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQL
SKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDPPFLLRR
>gnl|CDD|350678 cd17920, DEXHc_RecQ, DEXH-box helicase domain of RecQ family proteins. The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region
EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVD
RLQQLGIRAAALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPERKRLALIVVDEAH
CVSQWGHDFRPDYLRLGRLRRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD
>gnl|CDD|350679 cd17921, DEXHc_Ski2, DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins. Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVYIAPTRALVNQKEADLRERF
GPLGKNVGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHLIGDGERGVVLE
LLLSRLLRINKNARFVGLSATLPNAEDLAEWLGVEDLIRFD
>gnl|CDD|350680 cd17922, DEXHc_LHR-like, DEXH-box helicase domain of LHR. Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVRH
GDTSQSEKAKQLKNPPGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHALLGSKRGVQLELLLERLR
KLTGRPLRRIGLSATLGNLEEAAAFL
>gnl|CDD|350681 cd17923, DEXHc_Hrq1-like, DEAH-box helicase domain of Hrq1 and similar proteins. Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LYSHQAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAQDQLRSLRELLE
QLGLGIRVATYDGDTPREERRAIIRNPPRILLTNPDMLHYALLPHHDRWARFLRNLRYVVLDEAHTYRGV
FGSHVALLLRRLRRLCRRYGADPQFILTSATIGNPAEHARTL
>gnl|CDD|350682 cd17924, DDXDc_reverse_gyrase, DDXD-box helicase domain of reverse gyrase. Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
KEYEDFEEFFKKKTGFPPWGAQRTWAKRLLRGKSFAIIAPTGVGKTTFGLATSLYLASKGKRSYLIFPTK
SLVKQAYERLSKYAEKAGVEVKILVYHSRLKKKEKEELLEKIEKGDFDILVTTNQFLSKNFDLLSNKKFD
FVFVDDVDAVLKSSKNIDRLLKLLGFGQLVVSSATGRPRGIRPLLFREL
>gnl|CDD|350683 cd17925, DEXDc_ComFA, DEXD-box helicase domain of ComFA. ATP-dependent helicase ComFA (also called ComF operon protein 1) is part of the complex mediating the binding and uptake of single-stranded DNA. ComFA is required for DNA uptake but not for binding. It belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
GQQKASNALVETIDAKEDLLVWAVTGAGKTEMLFPAIAQALRQGGRVAIASPRIDVCLELAPRLKAAFPG
AAIVLLHGGSEDQYQRSPLVIATTHQLLRFYRAFDLLIIDEVDAFPYAGDPMLYYAVEKARKEEGSLIYL
TAT
>gnl|CDD|350684 cd17926, DEXHc_RE, DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins. This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LRPYQEEALEAWLAHKNNRRGILVLPTGSGKTLTALALIAYLKELRTLIVVPTDALLDQWKERFEDFLGD
SSIGLIGGGKKKDFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFSEILKELNAKYRL
GLTATP
>gnl|CDD|350685 cd17927, DEXHc_RIG-I, DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins. Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
FKPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVF
RKHFERPGYKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHNTTKN
HPYNEIMFRYLDQKLGSSGPLPQILGLTASPGVGGAKNTEEALEHICKLCANLDISVIATV
>gnl|CDD|350686 cd17928, DEXDc_SecA, DEXD-box helicase domain of SecA. SecA is a part of the Sec translocase that transports the vast majority of bacterial and ER-exported proteins. SecA binds both the signal sequence and the mature domain of the preprotein emerging from the ribosome. SecA belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
ELRAKTDELRERLAKGETLDDLLPEAFALVREAARRVLGMRPFDVQLIGGLVLHEGKIAEMKTGEGKTLT
ATLPAYLNALTGKGVHVVTVNDYLARRDAEWMGPLYEFLGLTVGVILSDMSPDERREAYAADITYGTNNE
LGFDYLRDNMVTSKEDLVQRGLNFAIVDEVDSILIDEARTPLIISGTLATITFQNYFRLYPKLAGMTGTA
KTEAEEFREIYNLDVVVIPT
>gnl|CDD|350687 cd17929, DEXHc_priA, DEXH-box helicase domain of PriA. PriA, also known as replication factor Y or primosomal protein N', is a 3'--_5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
QRKAYEAIVSSLGGFKTFLLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTPQLIKRFKKRFGDK
VAVLHSKLSDKERADEWRKIKRGEAKVVIGARSALFAPFKNLGLIIVDEEHDSSYKQDSGPRYHARDVAI
YRAKLENAPVVLGSATPSLESYYNAQQGKYRLLQLTER
>gnl|CDD|350688 cd17930, DEXHc_cas3, DEXH/Q-box helicase domain of Cas3. CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
PGLVILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATINQMYERIREILGRLDDEDKVLLLHSK
AALELLESDEEPDDDPVEAVDWALLLKRSWLAPIVVTTIDQLLESLLKYKHFERRLHGLANSVVVLDEVQ
AYDPEYMALLLKALLELLGELGGPVVLMTATLPALLRDELLEALLK
>gnl|CDD|350689 cd17931, DEXHc_viral_Ns3, DEXH-box helicase domain of NS3 protease-helicase. NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
GQLTVLDLHPGAGKTTRVLPQIIREAIKKRLRTLVLAPTRVVAAEMYEALRGLPIRYRTGAVKEEHGGNE
IVDYMCHGTFTCRLLSPKRVPNYNLIIMDEAHFTDPASIAARGYIHTRVEMGEAAVIFMTATPPGTVTPF
PQSNHPIEDFE
>gnl|CDD|350690 cd17932, DEXQc_UvrD, DEXQD-box helicase domain of UvrD. UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
NPEQREAVTHPDGPLLVLAGAGSGKTRVLTHRIAYLILEGGVPPERILAVTFTNKAAKEMRERLRKLLGE
QLASGVWIGTFHSFALRILRRYGDFDDLLLYALELLEENPDVREKLQSRFRYILVDEYQDTNPLQYELLK
LLAGDGKNLFVVGDDDQSIYGFRGADPENILDFEKDFPDAKVIKLEENY
>gnl|CDD|350691 cd17933, DEXSc_RecD-like, DEXS-box helicase domain of RecD and similar proteins. RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
EQKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAPTGKAAKRLSESTGIEASTIHRL
LGINPGGGGFYYNEENPLDADLLIVDEASMVDTRLMAALLSAIPAGARLILVGDPDQLPSVGAGNVLRDL
IASKGVPTVELTEVF
>gnl|CDD|438708 cd17934, DEXXQc_Upf1-like, DEXXQ-box helicase domain of Upf1-like helicase. The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
ISLIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAVDNVDVVIIDEASQITEPELLIALIRAKK
VVLVGDPKQLPPVVQEDHAALLGLSFILSLLLLFRLLLPGSPKVMLDTQYR
>gnl|CDD|350693 cd17935, EEXXQc_AQR, EEXXQ-box helicase domain of AQR. Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
QNTVKFTPTQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQLFEKI
MALDIDERHLLRLGHGAKIIAMTCTHAALKRGELVELGFKYDNILMEEAAQILEIETFIPLLLQNPEDGP
NRLKRLIMIGDHHQLPPVIKNMAFQKYSNMEQSLFTRLVRLGVPTVDLDAQGRARASISSLYNWRYK
>gnl|CDD|350694 cd17936, EEXXEc_NFX1, EEXXE-box helicase domain of NFX1. Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
TLDPSQLEALKHALTSELALIQGPPGTGKTFLGVKLVRALLQNQDLSITGPILVVCYTNHALDQFLEGLL
DFGPTKIVRLGARVIGMTTTGAAKYRELLQALGPKVVIVEEAAEVLEAHILAALTPSTEHLILIGDHKQL
RPKVNVYELTAKKYNLDVSLFERLVKNGLPFVTLNVQR
>gnl|CDD|350695 cd17937, DEXXYc_viral_SF1-N, DEXXY-box helicase domain of viral superfamily 1 helicase. Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. The members here contain arterivirus equine arteritis virus (EAV) non-structural protein (nsp)10. Nsp10 is composed of two domains, ZBD (ATPase) and HEL1 (helicase) along with 2 additional non-enzymatic domains that are thought to regulate HEL1 function. The helicase activity depends on the extensive relay of interactions between the ZBD and HEL1 domains. The arterivirus helicase structurally resembles the cellular Upf1 helicase, suggesting that nidoviruses may also use their helicases for post-transcriptional quality control of their large RNA genomes. The proteins here are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
AASTYIEGPPGCGKTFWLKKLVQPNDVLYVPTHATMLDMIKSLGPCRFVVPFGAPDLDFPTPSSSGPTVR
LLAVGYTPGGKAFVDEACYCNPVDLARLLTQTPVTAFGDPNQLGPVGFASVFFLVDLMQREQLNVIY
>gnl|CDD|350696 cd17938, DEADc_DDX1, DEAD-box helicase domain of DEAD box protein 1. DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVVALILEPSR
ELAEQTYNCIENFKKYLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRF
FVLDEADRLLSQGNLETINRIYNRIPKITSDGKRLQVIVCSATLHSFEVKKLADKIMHFPTWVD
>gnl|CDD|350697 cd17939, DEADc_EIF4A, DEAD-box helicase domain of eukaryotic initiation factor 4A. The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALV
LAPTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKI
KMFVLDEADEMLSRGFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL
>gnl|CDD|350698 cd17940, DEADc_DDX6, DEAD-box helicase domain of DEAD box protein 6. DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQA
LILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLS
HCKTLVLDEADKLLSQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN
>gnl|CDD|350699 cd17941, DEADc_DDX10, DEAD-box helicase domain of DEAD box protein 10. Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGALIISP
TRELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQML
VLDEADRILDMGFKETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH
>gnl|CDD|350700 cd17942, DEADc_DDX18, DEAD-box helicase domain of DEAD box protein 18. This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISP
TRELALQIYGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQC
LIIDEADRILEIGFEEEMRQIIKLLPKRRQTMLFSATQTRKVEDLARISLKKKPLYVG
>gnl|CDD|350701 cd17943, DEADc_DDX20, DEAD-box helicase domain of DEAD box protein 20. DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREI
AVQIHDVFKKIGKKLEGLKCEVFIGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDE
ADKLMEGSFQKDVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR
>gnl|CDD|350702 cd17944, DEADc_DDX21_DDX50, DEAD-box helicase domain of DEAD box proteins 21 and 50. DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region
TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVL
APTRELANQVTKDFKDITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHV
VLDEVDQMLDMGFAEQVEEILSVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYEQVD
>gnl|CDD|350703 cd17945, DEADc_DDX23, DEAD-box helicase domain of DEAD box protein 23. DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKDDGPYAL
ILAPTRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQ
CTYVVLDEADRMIDMGFEPQVTKILDAMPVSNKKPDTEEAEKLAASGKHRYRQTMMFTATMPPAVEKIAK
GYLRRPVVVT
>gnl|CDD|350704 cd17946, DEADc_DDX24, DEAD-box helicase domain of DEAD box protein 24. The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region
ILRALADLGFSEPTPIQALALPAAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLR
ALILTPTRELAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHL
ANLKSLRFLVLDEADRMLEKGHFAELEKILELLNKDRAGKKRKRQTFVFSATLTLDHQLPLKLNSKKKKK
KKEKKQKLELLIEKVGFRKKPKVID
>gnl|CDD|350705 cd17947, DEADc_DDX27, DEAD-box helicase domain of DEAD box protein 27. DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPT
RELAMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEIL
VLDEADRMLEEGFADELKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF
>gnl|CDD|350706 cd17948, DEADc_DDX28, DEAD-box helicase domain of DEAD box protein 28. DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNAPRGLV
ITPSRELAEQIGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQL
RHLVLDEADTLLDDSFNEKLSHFLRRFPLASRRSENTDGLDPGTQLVLVSATMPSGVGEVLSKVIDVDSI
ETVTSDKLHRLMPHVKQKFLR
>gnl|CDD|350707 cd17949, DEADc_DDX31, DEAD-box helicase domain of DEAD box protein 31. DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
LVSHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDGTLALV
LVPTRELALQIYEVLEKLLKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVS
NLRWLVLDEADRLLDMGFEKDITKILELLDDKRSKAGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDP
VYID
>gnl|CDD|350708 cd17950, DEADc_DDX39, DEAD-box helicase domain of DEAD box protein 39. DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQ
VSVLVICHTRELAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKNKCPHIVVGTPGRILALVREK
KLKLSHVKHFVLDECDKMLEQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV
>gnl|CDD|350709 cd17951, DEADc_DDX41, DEAD-box helicase domain of DEAD box protein 41. DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLPFIKGEGPYGL
IVCPSRELARQTHEVIEYYCKALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKK
KINLDICRYLCLDEADRMIDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN
>gnl|CDD|350710 cd17952, DEADc_DDX42, DEAD-box helicase domain of DEAD box protein 42. DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVA
PTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTY
LVLDEADRMFDMGFEYQVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV
>gnl|CDD|350711 cd17953, DEADc_DDX46, DEAD-box helicase domain of DEAD box protein 46. DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPM
FRHIKDQRPVKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVV
CTPGRMIDILTANNGRVTNLRRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEAL
ARKVLHKPIEIT
>gnl|CDD|350712 cd17954, DEADc_DDX47, DEAD-box helicase domain of DEAD box protein 47. DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFF
ALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFS
LKSLKFLVMDEADRLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE
>gnl|CDD|350713 cd17955, DEADc_DDX49, DEAD-box helicase domain of DEAD box protein 49. DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFA
LVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTK
VLSRVKFLVLDEADRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE
>gnl|CDD|350714 cd17956, DEADc_DDX51, DEAD-box helicase domain of DEAD box protein 51. DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
LLKNLQNNGITSAFPVQAAVIPWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLR
ALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGRYLSRVDILVATPGRLVDH
LNSTPGFTLKHLRFLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLGSFGDANLLERSVRPLQKLLFSA
TLTRDPEKLSSLKLHRPRLFT
>gnl|CDD|350715 cd17957, DEADc_DDX52, DEAD-box helicase domain of DEAD box protein 52. DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRALILAPTR
ELASQIYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLV
LDEADKLFEPGFREQTDEILAACTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG
>gnl|CDD|350716 cd17958, DEADc_DDX43_DDX53, DEAD-box helicase domain of DEAD box proteins 43 and 53. DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNGPGVLVL
TPTRELALQIEAECSKYSYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITY
LVLDEADRMLDMGFEPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY
>gnl|CDD|350717 cd17959, DEADc_DDX54, DEAD-box helicase domain of DEAD box protein 54. DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTV
GARALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMN
LKLSSVEYVVFDEADRLFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR
>gnl|CDD|350718 cd17960, DEADc_DDX55, DEAD-box helicase domain of DEAD box protein 55. DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIIS
PTRELATQIYEVLQSFLEHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKADKVKV
KSLEVLVLDEADRLLDLGFEADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV
>gnl|CDD|350719 cd17961, DEADc_DDX56, DEAD-box helicase domain of DEAD box protein 56. DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQGTR
ALILVPTRELAQQVSKVLEQLTAYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSL
LLLSTLKYLVIDEADLVLSYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL
>gnl|CDD|350720 cd17962, DEADc_DDX59, DEAD-box helicase domain of DEAD box protein 59. DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTREL
AVQIEDQAKELMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVD
EADTMLKMGFQQQVLDILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRIT
>gnl|CDD|350721 cd17963, DEADc_DDX19_DDX25, DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25. DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
LKPELLKGLYAMGFNKPSKIQETALPLILSDPPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCL
APTRELARQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILV
LDEADVMLDTQGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK
>gnl|CDD|350722 cd17964, DEADc_MSS116, DEAD-box helicase domain of DEAD-box helicase Mss116. Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
LDPSLLKALTRMGFETMTPVQQKTLKPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVS
ALIISPTRELALQIAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHLENPGV
AKAFTDLDYLVLDEADRLLDMGFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFI
D
>gnl|CDD|350723 cd17965, DEADc_MRH4, DEAD-box helicase domain of ATP-dependent RNA helicase MRH4. Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
FDQLKLLPSVREAIIKEILKGSNKTDEEIKPSPIQTLAIKKLLKTLMRKVTKQTSNEEPKLEVFLLAAET
GSGKTLAYLAPLLDYLKRQEQEPFEEAEEEYESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGI
KTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSII
KRAPKLKHLILCSATIPKEFDKTLRKLFPDVVRIATPRLHA
>gnl|CDD|350724 cd17966, DEADc_DDX5_DDX17, DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17. DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLA
PTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTY
LVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN
>gnl|CDD|350725 cd17967, DEADc_DDX3_DDX4, DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4. This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSV
GRGRRKAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLV
DFIERGRISLSSIKFLVLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK
NYIFLTVGRVG
>gnl|CDD|350726 cd17968, DEAHc_DDX11_starthere, DEAH-box helicase domain of ATP-dependent DNA helicase DDX11. DDX11 (also called ChlR1) encodes a protein of the conserved family of Iron-Sulfur (Fe-S) cluster DNA helicases and is thought to function in maintaining chromosome transmission fidelity and genome stability. Mutations in the Chl1 human homologs ChlR1/DDX11 and BACH1/BRIP1/FANCJ collectively result in Warsaw Breakage Syndrome, Fanconi anemia, cell aneuploidy and breast and ovarian cancers. DDX11 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
GKVGIFESPTGTGKSLSLICGALTWLTKIYYCSRTHSQLAQFVHEVQKSPFGKDVRLVSLGSRQPAAQVV
VLPYQMLLHAATRKASGIKLKDQVVIIDEAHNLICRAVIIAGGTMQPVADFKEQLLFSAGVTPE
>gnl|CDD|350727 cd17969, DEAHc_XPD, DEAH-box helicase domain of TFIIH basal transcription factor complex helicase XPD subunit. TFIIH can be resolved biochemically into a seven subunit core complex containing XPD/Rad3, XPB/Ssl2, p62/Tfb1, p52/Tfb2, p44/Ssl1, p34/Tfb4, and p8/Tfb5 and a three subunit Cdk Activating Kinase (CAK) complex containing CDK7/Kin28, cyclin H/Ccl1, and MAT1/Tfb3. XPD interacts directly with p44, which stimulates XPD helicase activity. XPD/Rad3 also interacts directly with the CAK via its MAT1/Tfb3 subunit inhibiting the helicase activity of XPD. XPD is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
LELKRTLDAKGHCVLEMPSGTGKTVSLLSLIVAYQKAYPLEVTKLIYCSRTVPEIEKVVEELRKLMDYYE
KQTGEKPNFLGLALSSRHANVVVYSYHYLLDPKIAELVSKELSKKSVVVFDEAHNIDFQSVVITSGTLSP
LDMYPKILDFRPVTMAS
>gnl|CDD|350728 cd17970, DEAHc_FancJ, DEAH-box helicase domain of Fanconi anemia group J protein and similar proteins. Fanconi anemia group J protein (FACJ or FANCJ, also known as BRIP1) is a DNA helicase required for the maintenance of chromosomal stability. It plays a role in the repair of DNA double-strand breaks by homologous recombination dependent on its interaction with BRCA1. FANCJ belongs to the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
GQNALLESPTGTGKTLSLLCSTLAWRQSLKGKATSEGSDGGGSGKIPKIIYASRTHSQLAQVVRELKRTA
YKRPRMTILGSRDHLCIHPVINKLSNQNANEACMALLSGKNEADLVFCPYNYLLDPNIRRSMGLNLKGSV
VIFDEAHNIEVRTIILTSGTLSPLDSFASELGTKFPIRLEN
>gnl|CDD|350729 cd17971, DEXHc_DHX8, DEXH-box helicase domain of DEAH-box helicase 8. DEAH-box helicase 8 (DHX8, also known as pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22) acts late in the splicing of pre-mRNA and mediates the release of the spliced mRNA from spliceosomes. DHX8 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKR
VAEEFGCCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFG
LLKKTVQKRPDLKLIVTSATLDAVKFSQYFYEAPIFTIP
>gnl|CDD|350730 cd17972, DEXHc_DHX9, DEXH-box helicase domain of DEAH-box helicase 9. DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
VPWSPPQSNWNPWTSSNIDEGPLAFATPEQISMDLKNELMYQREQDHNLQQILQERELLPVKKFREEILE
AISNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAVSVAERVAFERGEEVGKSC
GYSVRFESVLPRPHASILFCTVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRV
ILMSATIDTSMFCEYFFNCPVIEV
>gnl|CDD|438709 cd17973, DEXHc_DHX15, DEXH-box helicase domain of DEAH-box helicase 15. DEAH-box helicase 15 (DHX15) is a pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. DHX15 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
QRYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKLVACTQPRR
VAAMSVAQRVAEEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHER
TLATDILMGLLKEVVRRRPDLKLIVMSATLDAGKFQKYFDNAPLLKV
>gnl|CDD|350732 cd17974, DEXHc_DHX16, DEXH-box helicase domain of DEAH-box helicase 16. DEAH-box helicase 16 (DHX16) is probably involved in pre-mRNA splicing. DHX16 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGKIGCTQPRRVAAMSVAARVAEE
MGVKLGNEVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKD
IARFRPDLKLLISSATMDAEKFSAFFDDAPIFRI
>gnl|CDD|350733 cd17975, DEXHc_DHX29, DEXH-box helicase domain of DEAH-box helicase 29. DEAH-box helicase 29 (DHX29) is a part of the 43S pre-initiation complex involved in translation initiation of mRNAs with structured 5'-UTRs. DHX29 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLLNGGTAQKCNIVCTQPRRISAMSLATR
VCEELGCESGPGGKNSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQS
DFLLIILKEILHKRSDLHLILMSATVDCEKFSSYFTHCPILRI
>gnl|CDD|350734 cd17976, DEXHc_DHX30, DEXH-box helicase domain of DEAH-box helicase 30. DEAH-box helicase 30 (DHX30) plays an important role in the assembly of the mitochondrial large ribosomal subunit. DHX30 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRV
AHELGPNLRRNVGYQVRLESRPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLI
LLKGVLQLNPELRVVLMSATGDNQRLSRYFGGCPVVRV
>gnl|CDD|350735 cd17977, DEXHc_DHX32, DEXH-box helicase domain of DEAH-box helicase 32. DEAH-box helicase 32 (DHX32) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSAHYQHGVVVCTQVHKQTAVWLALRVA
DEMDVNIGHEVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLL
KDVLLSRPELKLVIITCPHLSSKLLSYYGNVPLIEV
>gnl|CDD|438710 cd17978, DEXHc_DHX33, DEXH-box helicase domain of DEAH-box helicase 33. DEAH-box helicase 33 (DHX33) stimulates RNA polymerase I transcription of the 47S precursor rRNA. DHX33 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGMIGITQPRRVAAVSVAKRVAEEM
GVELGQLVGYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSA
QRRRKEQKLSPLKVIIMSATLDADLFSEYFNGAPVLYI
>gnl|CDD|350737 cd17979, DEXHc_DHX34, DEXH-box helicase domain of DEAH-box helicase 34. DEAH-box helicase 34 (DHX34) plays a role in the nonsense-mediated decay (NMD), a surveillance mechanism that degrades aberrant mRNAs. DHX34 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRHIACTQPRRIACISLAKRVAFESLNQ
YGSKVAYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRL
RPDLKLILMSATINIELFSGYFEGAPVVQV
>gnl|CDD|350738 cd17980, DEXHc_DHX35, DEXH-box helicase domain of DEAH-box helicase 35. DHX35 plays a role in colorectal cancers and seems to be associated with risk to thyroid cancers. It also has been shown to positively regulate poxviruses, such as Myxoma virus. DEAH-box helicase 35 (DHX35) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRVVGCTQPRRVAAVTVAGRVAEE
MGAVLGHEVGYCIRFDDCTDPQATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLK
KIQKKRGDLRLIVASATLDAEKFRDFFNQNETNDPSKDTATILSV
>gnl|CDD|350739 cd17981, DEXHc_DHX36, DEXH-box helicase domain of DEAH-box helicase 36. DEAH-box helicase 36 (DHX36, also known as G4-resolvase 1 or G4R1, MLE-like protein 1 and RNA helicase associated with AU-rich element or RHAU) unwinds a G4-quadruplex in human telomerase RNA. DHX36 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERV
AAERAESCGLGNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVL
MGIVKDLLPFRSDLKVILMSATLNAEKFSDYFNNCPMIHI
>gnl|CDD|350740 cd17982, DEXHc_DHX37, DEXH-box helicase domain of DEAH-box helicase 37. DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPESDNPGMIGITQPRRVAAVSMAKR
VAEELNVFGKEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGM
LSRIVPLRAKLYLQDQTVKPLKLVIMSATLRVEDFTENKLLFPRPPPVIKV
>gnl|CDD|350741 cd17983, DEXHc_DHX38, DEXH-box helicase domain of DEAH-box helicase 38. DEAH-box helicase 38 (DHX38, also known as PRP16) is involved in pre-mRNA splicing. DHX38 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEM
GVELGEEVGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREV
VARRRDLKLIVTSATMDADKFADFFGNVPIFTI
>gnl|CDD|350742 cd17984, DEXHc_DHX40, DEXH-box helicase domain of DEAH-box helicase 40. DEAH-box helicase 40 (DHX40) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRRVAAISVAQRVAEEM
KCTLGSKVGYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKL
FQEKSPNRKEHLKVVVMSATLELAKLSAFFGNCPVFDI
>gnl|CDD|350743 cd17985, DEXHc_DHX57, DEXH-box helicase domain of DEAH-box helicase 57. DEAH-box helicase 57 (DHX57) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERV
AQERAERVGQSVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLV
LKDLMVQRPDLKVILMSATLNAELFSDYFNSCPVIHI
>gnl|CDD|350744 cd17986, DEXQc_DQX1, DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1. DEAQ-box RNA dependent ATPase 1 (DQX1) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPIWAAKFTFLEQLESPSGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQKGQVTVTQPHPLAARSLALRV
ADEMDLNLGHEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGL
LKDVRLQRPELRVVVVTSPALEPKLRAFWGNPPVVHV
>gnl|CDD|350745 cd17987, DEXHc_YTHDC2, DEXH-box helicase domain of YTH domain containing 2. YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCRIFCTQPRRLAAIAVAERVAA
ERGEKIGQTVGYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSALSTVTHVIVDEVHERDRFSDFLLTKL
RDILQKHPNLKLILSSAALDVNLFIRYFGSCPVIYI
>gnl|CDD|350746 cd17988, DEXHc_TDRD9, DEXH-box helicase domain of tudor domain containing 9. Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQ
EREWTLGSLVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVR
RLLRTNSRHVKIILMSATISCKEFADYFTTPNNPAYVFEV
>gnl|CDD|350747 cd17989, DEXHc_HrpA, DEXH-box helicase domain of ATP-dependent RNA helicase HrpA. HrpA is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpA belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGLIGHTQPRRLAARSVAERIAEEL
KTELGGAVGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQL
LPRRPDLKVIITSATIDAERFSRHFNNAPIIEV
>gnl|CDD|438711 cd17990, DEXHc_HrpB, DEXH-box helicase domain of ATP-dependent helicase HrpB. HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGGKIIVLEPRRVAARAAARRLATLL
GEAPGETVGYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEV
QQLLRDDLRLLAMSATLDGDGLAALLPEAPVVES
>gnl|CDD|350749 cd17991, DEXHc_TRCF, DEXH/Q-box helicase domain of the transcription-repair coupling factor. Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
DGEEQEEFEASFPYEETPDQLKAIEEILKDMESGKPMDRLICGDVGFGKTEVAMRAAFKAVLSGKQVAVL
VPTTLLAQQHYETFKERFANFPVNVELLSRFTTAAEQREILEGLKEGKVDIVIGTHRLLSKDVEFKNLGL
LIIDEEQRFGVKQKEKLKELRPNVDVLTLSATPIPRTLHMALSGIRDLSVIAT
>gnl|CDD|350750 cd17992, DEXHc_RecG, DEXH/Q-box helicase domain of RecG. ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LAFEELFALQLALLLRRRKIEELKGIILEISGELLKKFLEALPFELTGAQKRVIDEILRDLASEKPMNRL
LQGDVGSGKTVVAALAMLAAVENGYQVALMAPTEILAEQHYDSLKKLLEPLGIRVALLTGSTKAKEKREI
LEKIASGEIDIVIGTHALIQEDVEFHNLGLVIIDEQHRFGVEQRLKLREKGETPHVLVMTATPIPRTLAL
TLYGDLDVSIIDELP
>gnl|CDD|350751 cd17993, DEXHc_CHD1_2, DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins. Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREF
AKWAPDMNVIVYLGDIKSRDTIREYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRL
KNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQEKGIADLHKE
LEPFILRR
>gnl|CDD|350752 cd17994, DEXHc_CHD3_4_5, DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5. Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFE
MWAPDFYVVTYVGDHVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLT
GTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR
>gnl|CDD|350753 cd17995, DEXHc_CHD6_7_8_9, DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9. Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFE
TWTDMNVVVYHGSGESRQIIQQYEMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDE
AHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVE
KLQALLKPYMLRR
>gnl|CDD|350754 cd17996, DEXHc_SMARCA2_SMARCA4, DEXH-box helicase domain of SMARCA2 and SMARCA4. SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, members 2 and 4 (SMARCA2 and SMARCA4) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVS
EFEKWAPSVSKIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQ
SKLTQTLNTYYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNE
EETLLIIRRLHKVLRPFLLRRLK
>gnl|CDD|350755 cd17997, DEXHc_SMARCA1_SMARCA5, DEAH-box helicase domain of SMARCA1 and SMARCA5. SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMR
EFKRWCPSLRVVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNE
KSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEVVQRLH
KVLRPFLLRRIK
>gnl|CDD|350756 cd17998, DEXHc_SMARCAD1, DEXH-box helicase domain of SMARCAD1. SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1, also known as ATP-dependent helicase 1 or Hel1) possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for both DNA repair and heterochromatin organization. SMARCAD1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKR
WCPSLKVEPYYGSQEERKHLRYDILKGLEDFDVIVTTYNLATSNPDDRSFFKRLKLNYVVYDEGHMLKNM
TSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPFILRR
>gnl|CDD|350757 cd17999, DEXHc_Mot1, DEXH-box helicase domain of Mot1. Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSFNSENLPSLVVCPPTLVGHW
VAEIKKYFPNAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKN
SKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKE
QEAGALALEALHKQVLPFLLRR
>gnl|CDD|350758 cd18000, DEXHc_ERCC6, DEXH-box helicase domain of ERCC6. ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFH
RWWPPFRVVVLHSSGSGTGSEEKLGSIERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDE
GHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYLLRR
>gnl|CDD|350759 cd18001, DEXHc_ERCC6L, DEXH-box helicase domain of ERCC6L. ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAK
WTPGLRVKVFHGTSKKERERNLERIQRGGGVLLTTYGMVLSNTEQLSADDHDEFKWDYVILDEGHKIKNS
KTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNGSLLGTRKTFKMEFENPITRGRDKDATQGE
KALGSEVAENLRQIIKPYFLRR
>gnl|CDD|350760 cd18002, DEXQc_INO80, DEAQ-box helicase domain of INO80. INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEIS
RFVPQFKVLPYWGNPKDRKVLRKFWDRKNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAI
KSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGL
NEHQLKRLHMILKPFMLRR
>gnl|CDD|350761 cd18003, DEXQc_SRCAP, DEXH/Q-box helicase domain of SRCAP. Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFK
RWCPGFKILTYYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQ
RWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTAMSEGSQEENEELVR
RLHKVLRPFLLRR
>gnl|CDD|350762 cd18004, DEXHc_RAD54, DEXH-box helicase domain of RAD54. RAD54 proteins play a role in recombination. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LRPHQREGVQFLYDCLTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPTAKKALIVCPSSL
VGNWKAEFDKWLGLRRIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKISIDLLIC
DEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSR
DPDASEEDKELGAERSQELSELTSRFILRR
>gnl|CDD|350763 cd18005, DEXHc_ERCC6L2, DEXH-box helicase domain of ERCC6L2. ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRFKKKPPASSAK
KPVLIVAPLSVLYNWKDELDTWGHFEVGVYHGSRKDDELEGRLKAGRLEVVVTTYDTLRRCIDSLNSINW
SAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEP
IKRGQRHTATARELRLGRKRKQELAVKLSKFFLRR
>gnl|CDD|350764 cd18006, DEXHc_CHD1L, DEAH/Q-box helicase domain of CHD1L. Chromodomain helicase DNA binding protein 1 like (CHD1L, also known as ALC1) is involved in DNA repair by regulating chromatin relaxation following DNA damage. CHD1L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELN
RFAPDLSVITYMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSL
LHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESETVEELHLLLQ
PFLLRR
>gnl|CDD|350765 cd18007, DEXHc_ATRX-like, DEXH-box helicase domain of ATRX-like proteins. This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LKPHQVEGVRFLWSNLVGTDVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLY
NWEDEFKKWLPPDLRPLLVLVSLSASKRADARLRKINKWHKEGGVLLIGYELFRNLASNATTDPRLKQEF
IAALLDPGPDLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLK
EFKKKFVKPIEAGQCVDSTEEDVRLMLKR
>gnl|CDD|350766 cd18008, DEXDc_SHPRH-like, DEXH-box helicase domain of SHPRH-like proteins. The SHPRH-like subgroup belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LLPYQKQGLAWMLPRGGILADEMGLGKTIQALALILATRPQDPKIPEELEENSSDPKKLYLSKTTLIVVP
LSLLSQWKDEIEKHTKPGSLKVYVYHGSKRIKSIEELSDYDIVITTYGTLASEFPKNKKGGGRDSKEKEA
SPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPW
FNSDISKPFSKNDRKALERLQALLKPILLRR
>gnl|CDD|350767 cd18009, DEXHc_HELLS_SMARCA6, DEXH-box helicase domain of HELLS. HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNE
FARFTPSVPVLLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRL
KNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISN
LSEEREQNIVHMLHAILKPFLLRRLK
>gnl|CDD|350768 cd18010, DEXHc_HARP_SMARCAL1, DEXH-box helicase domain of SMARCAL1. SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLP
PDDIQVIVKSKDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRA
KRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYSGSSNLEELHLLLLATIM
IRR
>gnl|CDD|350769 cd18011, DEXDc_RapA, DEXH-box helicase domain of RapA. In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
PLPHQIDAVLRALRKPPVRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKF
GLPFLILDRETAAQLRRLIGNPFEEFPIVIVSLDLLKRSEERRGLLLSEEWDLVVVDEAHKLRNSGGGKE
TKRYKLGRLLAKRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLRLDGLREVLAKVLLRR
>gnl|CDD|350770 cd18012, DEXQc_arch_SWI2_SNF2, DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins. Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEE
EAAKFAPELKVLVIHGTKRKREKLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKT
AKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEALEELKKLIS
PFILRRLK
>gnl|CDD|350771 cd18013, DEXQc_bact_SNF2, DEXQ-box helicase domain of bacterial SNF2 family proteins. Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
PHPYQKVAINFIIEHPYCGLFLDMGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARSTWPDEVEKWNH
LRNLTVSVAVGTERQRSKAANTPADLYVINRENLKWLVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALR
KVRPVIKRLIGLTGTPSPNGLMDLWAQIALLDQGERLGRSITAYRERWFDPDKRNGQQVFKYKPKPGAEE
EIYRAISD
>gnl|CDD|350772 cd18014, DEXHc_RecQ5, DEAH-box helicase domain of RecQ5. ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
RSTLKKVFGHSDFKSPLQEKATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQ
VDHLKTLKIRVDSLNSKLSAQERKRIIADLESEKPQTKFLYITPEMAATSSFQPLLSSLVSRNLLSYLVV
DEAHCVSQWGHDFRPDYLRLGALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKPVAIFKTPCF
>gnl|CDD|350773 cd18015, DEXHc_RecQ1, DEXH-box helicase domain of RecQ1. ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
PWSGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISL
MEDQLMALKKLGISATMLNASSSKEHVKWVHAALTDKNSELKLLYVTPEKIAKSKRFMSKLEKAYNAGRL
ARIAIDEVHCCSQWGHDFRPDYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN
>gnl|CDD|350774 cd18016, DEXHc_RecQ2_BLM, DEAH-box helicase domain of RecQ2. ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome
HSKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLI
VDQVQKLTSLDIPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEKISASNRLISTLENLYERKLLA
RFVIDEAHCVSQWGHDFRPDYKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN
>gnl|CDD|350775 cd18017, DEXHc_RecQ3, DEAH-box helicase domain of RecQ3. DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Werner's syndrome
LNALNEYFGHSSFRPVQWKVIRSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQV
LQLVMSNIPACFLGSAQSQNVLDDIKMGKIRVIYVTPEFVSKGLELLQQLRNGITLIAIDEAHCVSQWGH
DFRSSYRHLGSIRNRLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD
>gnl|CDD|350776 cd18018, DEXHc_RecQ4-like, DEAH-box helicase domain of RecQ4 and similar proteins. ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome
LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLTLVVSPLIALMK
DQVDALPRAIKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPPISLLVVDEAH
CISEWSHNFRPDYLRLCRVLRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPLY
>gnl|CDD|350777 cd18019, DEXHc_Brr2_1, N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase. Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGTINL
DAFKIVYIAPMKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDR
TYTQLVRLIIIDEIHLLHDDRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGL
FYFD
>gnl|CDD|350778 cd18020, DEXHc_ASCC3_1, N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3. Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQGGVIKKDDFKIVYIAPMKALAA
EMVEKFSKRLAPLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVH
LLHDDRGPVIESLVARTLRQVESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD
>gnl|CDD|350779 cd18021, DEXHc_Brr2_2, C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase. Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWR
AKFGPLLGKKVVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENG
PVYEVVVSRMRYISSQLEKPIRIVGLSSSLANARDVGEWLGASKSTIFNFH
>gnl|CDD|350780 cd18022, DEXHc_ASCC3_2, C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3. Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKR
FEEKLGKKVVELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPV
LEVIVSRMNYISSQTEKPVRLVGLSTALANAGDLANWLGIKKMGLFNFR
>gnl|CDD|350781 cd18023, DEXHc_HFM1, DEXH-box helicase domain of ATP-dependent DNA helicase HFM1. HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGNRKVVYIAPIKALCSEKYD
DWKEKFGPLGLSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNGNLVQLVALVLIDEVHIIK
ENRGATLEVVVSRMKTLSSSSELRGSTVRPMRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP
>gnl|CDD|350782 cd18024, DEXHc_Mtr4-like, DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4. Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
CTHEVALPPDYDYTPISAHKPPGNPARTYPFTLDPFQKTAIACIERNESVLVSAHTSAGKTVVAEYAIAQ
SLRDKQRVIYTSPIKALSNQKYRELQEEFGDVGLMTGDVTINPNASCLVMTTEILRSMLYRGSEIMREVA
WVIFDEIHYMRDKERGVVWEETIILLPDKVRYVFLSATIPNARQFAEWICKIHKQPCHVVYTDYR
>gnl|CDD|350783 cd18025, DEXHc_DDX60, DEXH-box helicase domain of DEAD box protein 60. DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
NPDAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARF
SKKYPPSGKSLWGVFTRDYRHNNPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDG
AVWEQLLLLIPCPFLALSATIGNPQKFHEWLQSVQRARKAELKKIEHNHRDS
>gnl|CDD|350784 cd18026, DEXHc_POLQ-like, DEXH-box helicase domain of DNA polymerase theta. DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region
LPDAVREAYAKKGIKKLYDWQKECLSLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRLLERRKKALFVLP
YVSIVQEKVDALSPLFEELGFRVEGYAGNKGRSPPKRRKSLSVAVCTIEKANSLVNSLIEEGRLDELGLV
VVDELHMLGDGHRGALLELLLTKLLYAAQKNIQIVGMSATLPNLEELASWLRAELYTTNFRP
>gnl|CDD|350785 cd18027, DEXHc_SKIV2L, DEXH-box helicase domain of SKIV2L. Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
PAFKWPFELDVFQKQAILHLEAGDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRD
FKNTFGDVGLITGDVQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLI
MLPDHVSIILLSATVPNTVEFADWIGRIKKKNIYVISTP
>gnl|CDD|350786 cd18028, DEXHc_archSki2, DEXH-box helicase domain of archaeal Ski2-type helicase. Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKKLEE
IGLKVGISTGDYDEDDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIV
ARLRRLNPNTQIIGLSATIGNPDELAEWLNAELVESD
>gnl|CDD|350787 cd18029, DEXHc_XPB, DEXH-box helicase domain of TFIIH XPB subunit and similar proteins. TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
IDLKPSTQLRPYQEKALSKMFGNGRARSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRRQ
FLDWTTIDDEQIGRFTSDKKEIFPEAGVTVSTYSMLANTRKRSPESEKFMEFITEREWGLIILDEVHVVP
APMFRRVLTLQKAHCKLGLTATLVREDDK
>gnl|CDD|350788 cd18030, DEXHc_RE_I_HsdR, DEXH-box helicase domain of type I restriction enzyme HdsR subunit. The HdsR motor subunit of type I restriction-modification enzymes contains the DNA cleavage and ATP-dependent DNA translocation activities of the heteromeric complex. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LLDVLRNFIVFDEDDDKTKKVARYYQYYAVEAALERIKTATNKDGDKKGGYIWHTQGSGKSLTMFKAAKL
LIEDPKNPKVVFVVDRKDLDYQTSSTFSRFAAEDVVRANSTKELKELLKNLSGGIIVTTIQKFNNAVKEE
SKPVLIYRKNIVVIVDEAHRSQFGELAKALKKALPNATFIGFTGTPIFKEGDKTTEKVFGDYLHKYTI
>gnl|CDD|350789 cd18031, DEXHc_UvsW, DEXH-box helicase domain of bacteriophage UvsW. Bacteriophage UvsW is part of the WXY system that repairs DNA damage by a process that involves homologous recombination. UvsW is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
PHWYQKDAVFEGLVNRRRILNLPTSAGRSLIQALLARYYLENYEGKILIIVPTTALTTQMADDFVDYRLF
SHAMIKKIGGGASKDDKYKNDAPVVVGTWQTVVKQPKEWFSQFGMMMNDECHLATGKSISSIISGLNNCM
FKFGLSGSLRDGKANIMQYVG
>gnl|CDD|350790 cd18032, DEXHc_RE_I_III_res, DEXH-box helicase domain of type III restriction enzyme res subunit. Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
PRYYQQEAIEALEEAREKGQRRALLVMATGTGKTYTAAFLIKRLLEANRKKRILFLAHREELLEQAERSF
KEVLPDGSFGNLKGGKKKPDDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHHAIASSYRKILEYFE
PAFLLGLTATPERTDGLDTYELF
>gnl|CDD|350791 cd18033, DEXDc_FANCM, DEAH-box helicase domain of FANCM. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
VPLRDYQFTIVQKALFQNTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACYKIT
GIPSSQTAELTGSVPPTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHRATGNYAYCQV
VRELMRYNSHFRILALTATPGSKLEAVQQVIDNLLISHIEIR
>gnl|CDD|350792 cd18034, DEXHc_dicer, DEXH-box helicase domain of endoribonuclease Dicer. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
FTPRSYQLELFEAALKRNTIVVLPTGSGKTLIAVMLIKEMGELNRKEKNPKKRAVFLVPTVPLVAQQAEA
IRSHTDLKVGEYSGEMGVDKWTKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDECHHATG
DHPYARIMKEFYHLEGRTSRPRILGLTASPVNGKGDPKSVEKKIQQLEELLNSTIKTVSD
>gnl|CDD|350793 cd18035, DEXHc_Hef, DEXH-box helicase domain of Hef. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
EERRLYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLTKKGGKVLILAPSRPLVEQHAENLKRVLN
IPDKITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHHAVGNYAYVYIAH
RYKREANNPLILGLTASPGSDKEKIMEICENLGIEHIEIKT
>gnl|CDD|350794 cd18036, DEXHc_RLR, DEXH-box helicase domain of RIG-I-like receptors. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQQLEK
FFKYFRKGYKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEERVYLSDFSLLIFDECHHT
QKEHPYNKIMRMYLDKKLSSQGPLPQILGLTASPGVGGARSFEEALEHILKLCANLDASVIATV
>gnl|CDD|350795 cd18037, DEXSc_Pif1_like, DEAD-box helicase domain of Pif1. Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
EQRRVLDLVLDGKNVFFTGSAGTGKSYLLRRIIRALPSRPKRVAVTASTGIAACNIGGTTLHSFAGIGLG
SEPAEDLLERVKRSPYLVQRWRKCDVLIIDEISMLDADLFDKLDRVAREVRGSDKPFGGIQLILCGDFLQ
LPPVTKNSERQAFFFRGDQQFCFEAKSWERCIFLTVELTKVFR
>gnl|CDD|350796 cd18038, DEXXQc_Helz-like, DEXXQ/H-box helicase domain of Helz-like helicase. This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
ELNDEQKLAVRNIVTGTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERL
LNALVTKREILRLNAPSRDRASVPPELLPYCNSKAEGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPN
GHFTHIFIDEAGQATEPEALIPLSELASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLY
YKDGEYNPSYITKLLKNYR
>gnl|CDD|350797 cd18039, DEXXQc_UPF1, DEXXQ-box helicase domain of UPF1. UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
ELNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGL
KVVRLCAKSREAVESPVSFLALHNQVRNLDSAEKLELLKLLKLETGELSSADEKRYRKLKRKAERELLRN
ADVICCTCVGAGDPRLSKMKFRTVLIDEATQATEPECLIPLVHGAKQVILVGDHCQLGPVVMCKKAAKAG
LSQSLFERLVQLGIRPIRLQVQYR
>gnl|CDD|350798 cd18040, DEXXc_HELZ2-C, C-terminal DEXX-box helicase domain of HELZ2. Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
KLNPSQNHAVRTALTKPFTLIQGPPGTGKTVTGVHIAYWFAKQNREIQSVSGEGDGGPCVLYCGPSNKSV
DVVAELLLKVPGLKILRVYSEQIETTEYPIPNEPRHPNKKSERESKPNSELSSITLHHRIRQPSNPHSQQ
IKAFEARFERTQEKITEEDIKTYKILIWEARFEELETVDVILCTCSEAASQKMRTHANVKQCIVDECGMC
TEPESLIPIVSAPRAEQVVLIGDHKQLRPVVQNKEAQKLGLGRSLFERYAEKACMLDTQYR
>gnl|CDD|350799 cd18041, DEXXQc_DNA2, DEXXQ-box helicase domain of DNA2. DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGV
NFLRLGRLKKIHPDVQEFTLEAILKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQ
ITLPICLGPLRLAKKFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHPDAVVQLTIQYR
>gnl|CDD|438712 cd18042, DEXXQc_SETX, DEXXQ-box helicase domain of SETX. The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LNESQLEAIASALQNSPGITLIQGPPGTGKTKTIVGILSVLLAGKYRKYYEKVKKKLRKLQRNLNNKKKK
NRILVCAPSNAAVDEIVLRLLSEGFLDGDGRSYKPNVVRVGRQELRASILNEADIVCTTLSSSGSDLLES
LPRGFDTVIIDEAAQAVELSTLIPLRLGCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQLAGYPV
LMLTTQYR
>gnl|CDD|350801 cd18043, DEXXQc_SF1, DEXXQ-box helicase domain of Superfamily 1 helicases. Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
DSSQEAAIISARNGKNVVIQGPPGTGKSQTIANIIANALARGKRVLFVSEKKAALDVVRFPCWIMSPLSV
SQYLPLNRNLFDLVIFDEASQIPIEEALPALFRGKQVVVVGDDKQLPPSILLREHYR
>gnl|CDD|350802 cd18044, DEXXQc_SMUBP2, DEXXQ-box helicase domain of SMUBP2. SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
NLNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKV
KVVRIGHPARLLESVLDHSLDALVAAQVVLATNTGAGSRQLLPNELFDVVVIDEAAQALEASCWIPLLKA
RRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGESVVRMLTVQYR
>gnl|CDD|350803 cd18045, DEADc_EIF4AIII_DDX48, DEAD-box helicase domain of eukaryotic initiation factor 4A-III. Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQA
LILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTR
HIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL
>gnl|CDD|350804 cd18046, DEADc_EIF4AII_EIF4AI_DDX2, DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II. Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQA
LVLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTD
YIKMFVLDEADEMLSRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL
>gnl|CDD|350805 cd18047, DEADc_DDX19, DEAD-box helicase domain of DEAD box protein 19. DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANK
YPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFI
DPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK
>gnl|CDD|350806 cd18048, DEADc_DDX25, DEAD-box helicase domain of DEAD box protein 25. DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGK
TAAFVLAMLSRVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIV
IGTPGTVLDWCFKLRLIDVTNISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAF
AERIVPDPNIIKLKKEELT
>gnl|CDD|350807 cd18049, DEADc_DDX5, DEAD-box helicase domain of DEAD box protein 5. DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
QEVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQT
GSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQ
IRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSA
TWPKEVRQLAEDFLKDYIHINIGA
>gnl|CDD|350808 cd18050, DEADc_DDX17, DEAD-box helicase domain of DEAD box protein 17. DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
KFGNPGERLRKKKWDLSELPKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFP
QYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLV
LAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRC
TYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG
>gnl|CDD|350809 cd18051, DEADc_DDX3, DEAD-box helicase domain of DEAD box protein 3. DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSG
KTAAFLLPILSQIYEQGPGESLPSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVY
GGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMP
PTGERQTLMFSATFPKEIQMLARDFLDNYIFLAVGRVGS
>gnl|CDD|350810 cd18052, DEADc_DDX4, DEAD-box helicase domain of DEAD box protein 4. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region
YIPPPPPEDEDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQ
KYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEA
RKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMG
FGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFLKEDYLFLTVGRVG
>gnl|CDD|350811 cd18053, DEXHc_CHD1, DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1. Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
PRFVALKKQPSYIGGHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLY
GPFLLVVPLSTLTSWQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQTKRLKFNILLTTYEILLKDK
SFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWED
FEEEHGKGREYGYASLHKELEPFLLRR
>gnl|CDD|350812 cd18054, DEXHc_CHD2, DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
RPRFVALKKQPSYIGGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLY
GPFLLVVPLSTLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDK
TVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWED
FEEDHGKGRENGYQSLHKVLEPFLLRR
>gnl|CDD|350813 cd18055, DEXHc_CHD3, DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3. Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQ
MWAPDFYVVTYTGDKDSRAIIRENEFSFDDNAVKGGKKAFKMKREAQVKFHVLLTSYELVTIDQAALGSI
RWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA
DISKEDQIKKLHDLLGPHMLRR
>gnl|CDD|350814 cd18056, DEXHc_CHD4, DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFE
MWAPDMYVVTYVGDKDSRAIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSI
DWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFA
DIAKEDQIKKLHDMLGPHMLRR
>gnl|CDD|350815 cd18057, DEXHc_CHD5, DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFE
MWAPDFYVVTYTGDKESRSVIRENEFSFEDNAIRSGKKVFRMKKEAQIKFHVLLTSYELITIDQAILGSI
EWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA
DISKEDQIKKLHDLLGPHMLRR
>gnl|CDD|350816 cd18058, DEXHc_CHD6, DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6. Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRT
WTEMNAIVYHGSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEA
HRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKK
LQSILKPMMLRR
>gnl|CDD|350817 cd18059, DEXHc_CHD7, DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7. Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRT
WTELNVVVYHGSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEA
HRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQK
LQAILKPMMLRR
>gnl|CDD|350818 cd18060, DEXHc_CHD8, DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8. Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNT
WTEMNTIVYHGSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEA
HRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQK
LQAILKPMMLRR
>gnl|CDD|350819 cd18061, DEXHc_CHD9, DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9. Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRT
WTDLNVVVYHGSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEA
HRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQK
LQAILKPMMLRR
>gnl|CDD|350820 cd18062, DEXHc_SMARCA4, DEXH-box helicase domain of SMARCA4. SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHK
RINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQIL
AKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFE
QWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLK
>gnl|CDD|350821 cd18063, DEXHc_SMARCA2, DEXH-box helicase domain of SMARCA2. SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHK
RLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHIL
AKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFE
QWFNAPFAMTGERVDLNEEETILIIRRLHKVLRPFLLRRLK
>gnl|CDD|350822 cd18064, DEXHc_SMARCA5, DEAH-box helicase domain of SMARCA5. SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
CTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMV
LVPKSTLHNWMAEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRY
LVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNC
LGDQKLVERLHMVLRPFLLRRIKADVEKSLPPKK
>gnl|CDD|350823 cd18065, DEXHc_SMARCA1, DEAH-box helicase domain of SMARCA1. SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
CVRFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMV
LVPKSTLHNWMNEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRY
LVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNC
LGDQKLVERLHAVLKPFLLRRIK
>gnl|CDD|350824 cd18066, DEXHc_RAD54B, DEXH-box helicase domain of RAD54B. DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LRPHQREGIEFLYECVMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGKPVIKRALIVTPGS
LVKNWKKEFQKWLGSERIKVFTVDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHR
LKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTAT
PEEKKLGEARAAELTRLTGLFILRR
>gnl|CDD|350825 cd18067, DEXHc_RAD54A, DEXH-box helicase domain of RAD54A. DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LRPHQREGVKFLYRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIDKAIVVSPSSL
VKNWANELGKWLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGL
VICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPIL
KGRDADASEKERQLGEEKLQELISIVNRCIIRR
>gnl|CDD|350826 cd18068, DEXHc_ATRX, DEXH-box helicase domain of ATRX. Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSRVLVVCPL
NTVLNWLNEFEKWQEGLKDEEKIEVNELATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERNVKSR
EKLKEIFNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKP
NLLGTIKEFRNRFVNPIQNGQCADSTLVDVRVMKKR
>gnl|CDD|350827 cd18069, DEXHc_ARIP4, DEXH-box helicase domain of ARIP4. Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTL
QNWLSEFNKWLPPPEALPNVRPRPFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRLRPGPDVV
ICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILN
GQCVDSTPQDVKLMRYR
>gnl|CDD|350828 cd18070, DEXQc_SHPRH, DEXQ-box helicase domain of SHPRH. E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LLPYQRRAVNWMLVPGGILADEMGLGKTVEVLALILLHPRPDNDLDAADDDSDEMVCCPDCLVAETPVSS
KATLIVCPSAILAQWLDEINRHVPSSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDVLRTELHYAE
ANRSNRRRRRQKRYEAPPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDD
LFGLLSFLGVEPFCDSDWWARVLIRPQGRNKAREPLAALLKELLWRS
>gnl|CDD|350829 cd18071, DEXHc_HLTF1_SMARC3, DEXH-box helicase domain of HLTF1. Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LLPHQKQALAWMVSRENSQDLPPFWEEAVGLFLNTITNFSQKKRPELVRGGILADDMGLGKTLTTISLIL
ANFTLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRDPKLLSKYDIVLTTYNTLASDFGAKGDSP
LHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWR
RLIQRPLTMGDPTGLKRLQVLMKQITLRR
>gnl|CDD|350830 cd18072, DEXHc_TTF2, DEAH-box helicase domain of TTF2. Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEEKEKALTEWESKKDSTL
VPSAGTLVVCPASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKE
ESRSSPLFRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFD
DLKVWKKQVDNKSRKGGERLNILTKSLLLRR
>gnl|CDD|350831 cd18073, DEXHc_RIG-I_DDX58, DEXH-box helicase domain of RIG-I. RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFATKVPVYEQQKSVF
SKYFERHGYRVTGISGATAENVPVEQIIENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSGN
HPYNMIMFRYLDQKLGGSSGPLPQIIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATV
>gnl|CDD|350832 cd18074, DEXHc_RLR-2, DEXH-box helicase domain of RLR-2. RIG-I-like receptor 2 (RLR-2, also known as melanoma differentiation-associated protein 5 or Mda5 and IFIH1) is a viral double-stranded RNA (dsRNA) receptor that shares sequence similarity and signaling pathways with RIG-I, yet plays essential functions in antiviral immunity through distinct specificity for viral RNA. RLR-2 recognizes the internal duplex structure, whereas RIG-I recognizes the terminus of dsRNA. RLR-2 uses direct protein-protein contacts to stack along dsRNA in a head-to-tail arrangement. The signaling domain (tandem CARD), which decorates the outside of the core RLR-2 filament, also has an intrinsic propensity to oligomerize into an elongated structure that activates the signaling adaptor, MAVS. RLR-2 uses long dsRNA as a signaling platform to cooperatively assemble the core filament, which in turn promotes stochastic assembly of the tandem CARD oligomers for signaling. LGP2 appears to positively and negatively regulate RLR-2 and RIG-I signaling, respectively. RLR-2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
LTLRDYQMEVAKPALEGKNIIICLPTGSGKTRVAVYITKDHLDKKRKASEPGKVIVLVNKVPLVEQHYRK
EFNPFLKHWYQVIGLSGDSQLKISFPEVVKRYDVIICTAQILENSLLNATEEEDEGVQLSDFSLIIIDEC
HHTQKEAVYNNIMRRYLKQKIKNRKQKKENKPLIPLPQILGLTASPGVGGAKNNKKAEEHILKICANLDA
FRIMTV
>gnl|CDD|350833 cd18075, DEXHc_RLR-3, DEXH-box helicase domain of RLR-3. RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
MELHGYQWEVVAPALRGKNSIIWLPTGAGKTRAAVYVARRHLETKRGAKVAVLVNKVHLVDQHLEKEFHV
LLDKYTVTAISGDSSHKCFFGQLARGSDVVICTAQILQNALLSGEEEAHVELTDFSLLVIDECHHTHKEA
VYNKIMLSYLEKKLSRQGDLPQILGLTASPGTGGATSFDGAVEHILQICANLDTWVIMSA
>gnl|CDD|350834 cd18076, DEXXQc_HELZ2-N, N-terminal DEXXQ-box helicase domain of HELZ2. Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
AGNNKQQLAFNFIAGKPSEARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADIYIR
EYFHPYVDKGHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAFNL
HVLSGFFTHIFIDEAAQMLECEALIPLSYAGPKTRVVLAGDHMQMTPKLFSVADYNRANHTLLNRLFHYY
QGEKHEVAVKSRVIFSENYR
>gnl|CDD|350835 cd18077, DEXXQc_HELZ, DEXXQ-box helicase domain of HELZ. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEY
LHPYVETGNPRARPLRVYYRNRWVKTVHPVVQKYCLIDEHGTFRMPTREDVMRHRVVVVTLSTSQYLCQL
DLEPGFFTHILLDEAAQAMECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEH
YPSEHPCRILLCENYR
>gnl|CDD|350836 cd18078, DEXXQc_Mov10L1, DEXXQ-box helicase domain of Mov10L1. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
DLNELQKEAVKRILGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRL
HESKVLKPGDMVRLNAVNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHV
FVDEAGQATEPESLIPLGLISSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNR
FGESGGYNPLLVTKLVDNYR
>gnl|CDD|350837 cd18079, S-AdoMet_synt, S-adenosylmethionine synthetase. S-adenosylmethionine synthetase (EC 2.5.1.6), also known as methionine adenosyltransferase, catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP in two steps, the formation of AdoMet and hydrolysis of the tripolyphosphate, which occurs prior to release of the product from the enzyme, which consists of three structural domains that have a similar alpha+beta fold
LFTSESVTEGHPDKICDQISDAILDACLAQDPNSRVACETLVTTGLVIIAGEITTKAYVDIEKIVREVIK
EIGYDDSDFGFDAKTCGVLVSIHEQSPDIAQGVDEGLELEEIGAGDQGIMFGYATDETPELMPLPIVLAH
KLARRLAEVRKNGTLPWLRPDGKTQVTVEYEDGKPVRVDTIVVSTQHDEDVSLEELREDIIEKVIKPVIP
EELLDEDTKYLINPTGRFVIGGPAGDTGLTGRKIIVDTYGGYARHGGGAFSGKDPTKVDRSAAYAARYIA
KNIVAAGLAKRCEVQLSYAIGVAEPVSIYVDTFGTGKISDEKIEEIIKKNFDLRPAGIIEDLDLRRPIYR
KTAAYGHFGREDEDFPWEKTD
>gnl|CDD|349953 cd18080, TrmD-like, tRNA-M1G37-methyltransferase TrmD. The bacterial tRNA-(N(1)G37) methyltransferase (TrmD) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the N1 position of G37 in the anticodon loop of a subset of tRNA that contains a G at position 36. The presence of the modification prevents Watson-Crick base-pairing of this guanosine with cytosine in mRNA and translational frame-shifting. This family of proteins contains members of the SPOUT methyltransferases. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
KIDVLTLFPEMFEGFLNDSILGRALEKGLIEIEVINLRDFATDKHKTVDDYPYGGGAGMVMKPEPLVKAL
ESIKKKRKKSKVIYLSPQGKPFNQKLAKELAKEDHLVLICGRYEGIDERVIEYYVDEEISIGDYVLTGGE
LAAMVLIDAVVRLLPGVLGNEESAEEESFSDGLLEYPQYTRPAEFRGLKVPEVLLSGNHAKIAKWRREQS
LERTKKRRP
>gnl|CDD|349954 cd18081, RlmH-like, 23S-rRNA-pseudouridine1915-N3-methyltransferase RlmH. 23S rRNA (pseudouridine1915-N3)-methyltransferase RlmH catalyzes the addition of a methyl group at the N-3 position of pseudouridine Psi1915 in 23S rRNA to form m(3)Psi1915. This family of proteins belongs to the SPOUT methyltransferases. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
IRIIAVGKLKEKWLKELIEEYLKRLSRYAKLELIELKDEKIPKSIEQIKEKEGERILKALPKGDYVIALD
ERGKQLDSEEFAKLLEKWRDSGGSRIVFVIGGADGLSEEVRKRADLLLSLSKLTFPHQLARVVLLEQLYR
AFTILNGHPYHK
>gnl|CDD|349955 cd18082, SpoU-like_family, SAM-dependent rRNA or tRNA methylase related to SpoU. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
HLVLDNIRSPGNIGSIFRTADAFGVEKIYLVGPTADIFDPKAKRTSRGTHFSVPYERVDNFEEYLKSLKE
EGYPLIGLELTDGSIPLSEFKFKKPKKIALIFGNERSGLSPELLALCDYTVHIPMSGKNSSLNVSVATGI
ALYEF
>gnl|CDD|349956 cd18083, aTrm56-like, archaeal tRNA (cytidine(56)-2'-O)-methyltransferase Trm56. Archaeal tRNA (cytidine(56)-2'-O)-methyltransferase Trm56 catalyzes the 2'-O-ribose methylation of cytidine at position 56 in tRNAs. Trm56 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
IYVLRLGHRPERDKRITTHVGLTARAFGADGIILSGEDEKVKESLRDVVERWGGDFEVEYGVNWKRYIRE
WKEEGGVVVHLTMYGLNIDDVIEEIRRAGKDILIVVGAEKVPGEVYELADYNVSVGNQPHSEVAALAVFL
DRLYEGKELEREFEDARLRIIPSERGKKV
>gnl|CDD|349957 cd18084, RsmE-like, SPOUT superfamily RNA methyltransferase RsmE-like. 16S rRNA m3U1498 methyltransferase RsmE modifies nucleotides during ribosomal RNA maturation in a site-specific manner. The Escherichia coli member is specific for U1498 methylation. RsmE is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
ITLAQALPKGDRMEWILEKATELGVTRIIPVISERSVVKYDKKAEKKLERWQKIAIEAAEQSGRTRLPEI
EPPISLKELLLLLPDDDLRLVAHEGEEQSLLLLLLLLKSSKRILLLIGPEGGFSEEEIELLKEAGFKPVS
LGPRILRTETAAIAALSLL
>gnl|CDD|349958 cd18085, TM1570-like, SPOUT superfamily RNA methyltransferase TM1570-like. DUF2168; This domain, found in various hypothetical prokaryotic proteins, has no known function. It is also found in a few prokaryotic tRNA (guanine-N(1)-)-methyltransferases. Proteins of this family are members of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
LYVALVHYPVLNKRGEIVTTSVTNLDLHDIARSSRTYGVKGYYIVTPLEDQQELAERILGHWTEGYGGKY
NPDRKEALSLVRVVESLEEAIAEIEEKEGKRPLVVATSARPYANAISYAELRRMLLEDRPVLLVFGTGWG
LAPEVLERADYVLEPIRGAGDYNHLSVRSAAAIILDRL
>gnl|CDD|349959 cd18086, HsC9orf114-like, SPOUT superfamily RNA methyltransferase HsC9orf114-like. Human C9orf114 (also known as centromere protein 32 or CENP-32) is required for association of the centrosomes with the poles of the bipolar mitotic spindle during metaphase. CENP-32 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
TLSIAIPSSILSNAQSLELKTYKAGQIARAAAIFRVDEIVVYDDSSASEDTKEKSDDAEFLARLLQYLET
PPYLRKRLFPKYWGYSVRVAKSLSEVFTSPYKGGYDLVIGTSRRGEDISSVLLESILLPSFKHLLLVFGG
PDKGLEEALEADGDPKELFDHYVNTIPGQGSRTIRTEEALLITLALL
>gnl|CDD|349960 cd18087, TrmY-like, tRNA (pseudouridine(54)-N(1))-methyltransferase TrmY. tRNA (pseudouridine(54)-N(1))-methyltransferase TrmY catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs. TrmY is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
RSFVVIGHKARTDPDFSLNDLPGSAGRLDVLCRCVNAALFLSHGIRRDVRVHLVLLGPPDPPKTIRFDGS
RLRYLNPDERSIAALIKKALKKGVGASEAEVSPGIYVRRRGFEELLDELAERKPIYYLDEDGEDIRNVAF
EPNPVFVLGDHIGLTEEEEKLLERDGAKKISLGPRSLHADHCIVIVHNELDRR
>gnl|CDD|349961 cd18088, Nep1-like, 18S rRNA (pseudouridine(1248)-N1)-methyltransferase Nep1. 18S rRNA (pseudouridine(1248)-N1)-methyltransferase Nep1 (also known as EMG1) methylates pseudouridine at position1248 (Psi1248) in 18S rRNA and is required for small subunit (SSU) ribosomal RNA (rRNA) maturation. Mutations on human cause in Bowen-Conradi Syndrome. Nep1 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
LIVVLEEASLELVPVEIWKKPKYELLNSDDHHNAMKKLKRDPKRGRPDIVHQCLLALLDSPLNKAGLLQV
YIHTYNNVLIEVNPQTRIPRTYKRFCGLMVQLLHKGKIRAANGGEKLLKVIKNPLTDHLPEGCRKIGLSE
KGELVNPKELVANLPDDEPIVFVIGAFAHGDFSEDTSYADEKISISNYPLSAATVCSRICSAFE
>gnl|CDD|349962 cd18089, SPOUT_Trm10-like, tRNA methyltransferase Trm10-like. Family of tRNA methyltransferase Trm10-like proteins catalyzes the N(1) methylation of guanine at position 9 (m(1)G9) of tRNA (eukaryotes) or N(1) methylation of guanine or adenine at position 9 (m1G9/m1A9) of tRNA (archaea), which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
PRIVIDLSFDDLMTEKEIRSLAKQLSRCYGANRRSEKPLRLHLTSFSGDLKQRLLKKSGAENWKIITHEE
SLLEEEAFPKEKLVYLTADAEEVLEELDPDKVYIIGGIVDRNRHKGLTLNKAEELGIRTARLPIREYIKL
KGRKVLTVNHVFEILLRYLEGGDWKEALEEV
>gnl|CDD|349963 cd18090, Arginine_MT_Sfm1, SAM-dependent arginine methyltransferase related to yeast Sfm1. Arginine methyltransferase Sfm1 methylates R146 of 40S ribosomal protein S3 (Rps3), which contacts 18S RNA. Sfm1 is part of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent mainly RNA MTases which are structurally characterized by a deep trefoil knot
PKYIIEHLEEELSEWLLLEYSHMAKIVGRERLIFTNVPEEDVELLSEKLLKKLEVSITDLVLELLFPKER
VCLLDPRAEEELSPEDAEKFDYFVFGGILGDHPPRDRTKELRTKGGFPSRNLGPIQMTTDTAVLVAKLIL
>gnl|CDD|349964 cd18091, SpoU-like_TRM3-like, SAM-dependent tRNA methylase related to TRM3. Yeast tRNA (guanosine(18)-2'-O)-methyltransferase TRM3 catalyzes the formation of 2'-O-methylguanosine at position 18 (Gm18) in various tRNAs. TRM3 is similar to C-terminal domain of TAR (HIV-1) RNA binding protein 1 (TARBP1), a protein binding to TAR, which functions as a RNA regulatory signal by forming a stable stem-loop structure to which transactivator protein Tat binds. The role of TARBP1 is believed to be to disengage RNA polymerase II from TAR during transcriptional elongation. TRM3 and the C-terminal methyltransferase domain of TARBP1 are members of the SPOUT methyltransferase superfamily
LIVVASLIDKPPNLGGLCRTCEIFGVSKLVLPNLAVVEDKQFKALSVSAEKWLPIEEVKPEDLLPYLKEK
KQEGYTIVGLEQTANSVSLHDFQFPKKTVLVLGNEKEGIPAELLSLLDVCVEIPQLGVIRSLNVHVSGAI
AIYEY
>gnl|CDD|349965 cd18092, SpoU-like_TrmH, SAM-dependent tRNA methylase related to TrmH. TrmH catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of the ribose of the universally conserved guanosine 18 (G18) position in tRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
ERLERIEEVLARRTRDLTVVLENVHDPHNASAVLRTCDAFGVQDVHVIEPKNKFKKNRGVAMGADKWLDV
HRHDSTEECLAALKEQGYRIVATSLSPDAVPLDELDYTRPTALVFGNEKDGVSEEALAAADERVYIPMYG
FVESLNVSVAAAIILYELQRQR
>gnl|CDD|349966 cd18093, SpoU-like_TrmJ, SAM-dependent tRNA methylase related to TrmJ. tRNA methyltransferase TrmJ catalyzes the methyl transfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH at position 32 in both tRNASer1 and tRNAGln2. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
IRVVLVEPQHPGNIGAVARAMKNFGLSDLRLVNPRCDDPEEAARALASGAEDVLENAKVYDTLEEALADC
DLVVATTARPRGLRRPLLTPRELAELLKEHAAGGKVALVFGREDSGLTNEELALCDLLVTIPTNPEYPSL
NLAQAVAIVLYEL
>gnl|CDD|349967 cd18094, SpoU-like_TrmL, SAM-dependent tRNA methylase related to TrmL. tRNA (Um34/Cm34) methyltransferase TrmL catalyzes the methyl transfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH at position 34 in both tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
NIVLYEPEIPQNTGNIARTCAATGARLHLIEPLGFSLDDKRLKRAGLDYWDHVDLTVHDSWEAFLEALPP
GRLFLFTTKGTKPYTDFDFKPGDYLVFGRESTGLPEEILDAFPDRRLRIPMRPKVRSLNLSNSVAIVLYE
ALRQL
>gnl|CDD|349968 cd18095, SpoU-like_rRNA-MTase, SAM-dependent rRNA methylase related to SpoU-TrmH. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
LVLVLDGVQDPGNLGTIIRTAAAFGVDGVILSKGTVDPYNPKVVRASMGALFRLPIIRVDDLEELLEELK
EAGYKVVAADLDGGSSLYDLDLPKPVALVLGNEGNGLSDELLELCDKRVTIPMSGGVESLNVAVAAAILL
YEL
>gnl|CDD|349969 cd18096, SpoU-like, SAM-dependent rRNA or tRNA methylase related to SpoU. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
LYLVLHNVAKRHNIGTIVRSANAFGVKEVHLVGRRKFNPFGAMGTDRHVKFRHFDTLAEAKEYLKERGIR
LVGVEIVPGAEPIETHPFPGDTAFVLGNEGTGLSDEQLAICDGFVYIPQYGSGTASLNVSVAASIVLHHF
>gnl|CDD|349970 cd18097, SpoU-like, SAM-dependent rRNA or tRNA methylase related to SpoU. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
LVVVLDNLRSAHNVGSIFRTADAAGVEKIYLCGYTPTPPHPKVAKTALGAEESVPWEHFEDTLEAVRALK
ARGYTIIALETTENSVPLHEARLPRPLALVLGNEVRGVSPEVLALCDAVVEIPMFGRKNSLNVAVAAAVA
LYEL
>gnl|CDD|349971 cd18098, SpoU-like, SAM-dependent rRNA or tRNA methylase related to SpoU. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
FAIGIENPKTPKNVGTLWRAAGCLGASFVFTIGARYKRRKQSTDTSKAWRHIPLFHYDDLEDLAEPLPFG
AVLVAVELTEGATPLPDFKHPDRAVYLLGPEDGGLPQEVLARCHHVVYLPTRGSLNVAVAGSIVLYDR
>gnl|CDD|349972 cd18099, Trm10arch, archaeal tRNA(m1G9/m1A9)-methyltransferase Trm10. Archaeal tRNA(m1G9/m1A9)-methyltransferase Trm10 catalyzes the N(1) methylation of guanine or adenine at position 9 (m1G9/m1A9) of tRNA, which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
PYFIIDLSLWDLHTEKEKKKLVLQVLLSIGVIRKYLWDGNLVLTWANSMFLEMLNKVESLSLYTVGLKEK
GEDNAVLLDPYAEEVATEDIIRDTKAFIIGGIVDKGGNKKGATTELGELLGGAIEVPRRKIVLRGSIVGV
PDRINKILEIILRVIEGDQSLEEAIIAVQS
>gnl|CDD|349973 cd18100, Trm10euk_B, eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B. Eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B (TM10B) catalyzes the N(1) methylation of guanine at Position 9 (m(1)G9) of tRNA, which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
LRVCIDLSLEHKMSEKEISKLAQQLRRLYGSNRKAEKPLHIYLTSFDKEGLLYKECVRKNDGFENYLIDM
TEESHSELFPKEEIVYLSPDSENVLESIDPNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYMV
KADGKGNYSTVLAINQVFDILLKYYETGDWREALSAGVPQRK
>gnl|CDD|349974 cd18101, Trm10euk_A, eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A. Eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A (TM10A) catalyzes the N(1) methylation of guanine at Position 9 (m(1)G9) of tRNA, which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
IRVAIDCSFDDLMTEKDIKKLVKQIQRCYAENRRADNPVQLYLTSLGGKTKENMEKDKGYENWDVNFKEE
HYLEVFKKEDIVYLTSDSPNVLEDLDEDKVYIIGGLVDHNHHKGLCYKRAVELGIQHARLPIDEYVKMKT
RKVLTINHVFEILLRYTEGKDWKEAFFKVIPQRK
>gnl|CDD|349975 cd18102, Trm10_MRRP1, Mitochondrial ribonuclease P protein 1. Mitochondrial ribonuclease P protein 1 (or tRNA methyltransferase 10 homolog C) functions in mitochondrial tRNA maturation and is part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/RG9MTD1, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. MRRP1 is related to Trm10, a tRNA m1G9 methyltransferase and is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
QPLVIDMSYEDLMSPREIKNTARQLLEAYSANRRSTEPFHLHFCNLDPDGESIKRLLRLIPKLSLDKFPI
TVTEKSYLDLFPKEKLVYLSPDAPEVLKEFDPDKVYIIGGLVDKSTKKPLSLAKAKKEGIRMARLPLDRY
LKWGGGSKSLTLNQVVSILLDLKDTGDWKEALKHVPPRK
>gnl|CDD|349976 cd18103, SpoU-like_RlmB, SAM-dependent rRNA methylase related to RlmB. 23S rRNA-M2G2251-MTase RlmB catalyzes the methylation of guanosine 2251, a modification conserved in the peptidyltransferase domain of 23S rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
LLLILDGITDPHNLGAIIRSAEAFGVDGVIIPKRRSAPLTPTVAKASAGALEHLPIARVTNLARALEELK
EAGFWIYGADGEAEKSLYDVDLTGPLALVLGSEGKGLRRLVLKNCDFLVKIPMAGKVDSLNVSVAAGIIL
YEI
>gnl|CDD|349977 cd18104, SpoU-like_RNA-MTase, SAM-dependent RNA methylase related to SpoU-TrmH. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
LILVLEGLEKPGNLGAILRSADAAGADAVILCDPKTDLFNPNVIRASLGAVFTLPVAEASSEETLAWLKE
NKIRILATTPKAEKLYYEADLRGPIAIVVGSESEGLSEFWLKAADERVRIPMAGQADSLNVSVAAAILLY
EALRQR
>gnl|CDD|349978 cd18105, SpoU-like_MRM1, SAM-dependent rRNA methylase related to MRM1. MRM1 catalyzes the methylation of 2'-O-ribose residues G1145 to GmG residue of the mitochondrial 16S rRNA. MRM1 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
LWLLLDEITDPQNLGAILRSAYFLGVDGVVVSSKNSAPLSPVVSKASAGALELMPIYSVDNLASFLKSSK
ENGWKVVGTSAPPSASSDKKTIPANELSELLLEKPTILVLGNEGRGLRTNIKNLCDYLVSIPGGRSAENP
GVDSLNVSVAAGILLHSL
>gnl|CDD|349979 cd18106, SpoU-like_RNMTL1, SAM-dependent rRNA methylase related to RNMTL1. RNMTL1 (also known as HC90, MRM3 and RMTL1) catalyzes the methylation of 2'-O-ribose residues G1370 to GmG residue of the mitochondrial 16S rRNA. RNMTL1 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
LTVICDNIRDPGNLGSILRSAAAAGCSKVLLTKGCVDPWEPKVLRAGAGAHFRLPIYGNLSWDDIPNYLP
DDSKVFLADNNLPVQPYDSIDYCSGPIVLVIGGETHGVSPEAYKLAHSTGGSRVHIPLANGVDSLNSAVA
ASILLFEM
>gnl|CDD|349980 cd18107, SpoU-like_AviRb, SAM-dependent rRNA methylase related to AviRb. AviRb from Streptomyces viridochromogenes methylates the 2'-O atom of U2479 of the 23S ribosomal RNA. AviRb is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
LVVLFDRPTSPGNLGTIIRSADALGAHGLVVTGHAADVYDPKTIRASTGSLFSLPIVRVPSNRELEDWVE
ARKARGTPLQLVGTDEHGDHQIADHDFTRPTLLLIGNETAGLSAAWRELCDETVSIPMAGSASSLNAACA
ASIFLYEA
>gnl|CDD|349981 cd18108, SpoU-like_NHR, Nosiheptide-resistance methyltransferase (NHR). Nosiheptide-resistance methyltransferase (NHR) confers resistance to the thiazole antibiotic nosiheptide via catalyzing 2'O-methylation of 23S rRNA at the nucleotide A1067. NHR is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
DVVVLDGVRIVGNIGAIVRTSLALGAAGIVLVDSDLATVADRRLLRASRGYVFSLPVVLADREEAVAFLR
DNDIPLMTLDADGDVPVKELGDRPDRLALVFGSEKGGPSGLFEEAAAGTVSIPMSSSTESLNVSVSAGIA
LHER
>gnl|CDD|349982 cd18109, SpoU-like_RNA-MTase, SAM-dependent RNA methylase related to SpoU-TrmH. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot
LTLALDGIQDPGNLGTIIRTADWFGIRQIICSPDTVDPYNPKVVQASMGSIFRVQIHYTDLPALLAELKK
AFPVYGADLDGENLYEFTLPEKGILVMGNEGHGISPEVLKLLTHRLTIPRYGKGAESLNVAVATAILLSE
F
>gnl|CDD|349745 cd18110, ATP-synt_F1_beta_C, F1-ATP synthase beta (B) subunit, C-terminal domain. The beta (B) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic
IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKY
VPLKDTIKGFKEILDGEYDDLPEQAFYMVGTIDEAVEK
>gnl|CDD|349746 cd18111, ATP-synt_V_A-type_alpha_C, V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain. The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes
WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQYKML
KLILTFYDKALEALEKGVPLSKILELPVREKIARM
>gnl|CDD|349747 cd18112, ATP-synt_V_A-type_beta_C, V/A-type ATP synthase beta (B) subunit, C-terminal domain. The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit
GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLD
LGWELLSILPKEELKRISEEYIDKY
>gnl|CDD|349748 cd18113, ATP-synt_F1_alpha_C, F1-ATP synthase alpha (A) subunit, C-terminal domain. The alpha (A) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic
MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGY
LDDIPVEKIKEFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF
>gnl|CDD|349749 cd18114, ATP-synt_flagellum-secretory_path_III_C, Flagellum-specific ATP synthase, C-terminal domain. The C-terminal domain of the flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The flagellum-specific ATPase FliI is the soluble export component that drives flagellar protein export, and it shows extensive similarity to the alpha and beta subunits of FoF1-ATP synthase. Although they both are proton driven rotary molecular devices, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway
HYLAARKFRELMSTYQENEDLIRIGAYKKGSDPEVDEAIRLKPQIEAFLKQGLNEKAPLEESLQQLEEIF
G
>gnl|CDD|349739 cd18115, ATP-synt_F1_beta_N, F1-ATP synthase beta (B) subunit, N-terminal domain. The beta (B) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic
NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVI
DTGAPI
>gnl|CDD|349740 cd18116, ATP-synt_F1_alpha_N, F1-ATP synthase alpha (A) subunit, N-terminal domain. The alpha (A) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, in mitochondrial inner membranes, and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic
EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR
>gnl|CDD|349741 cd18117, ATP-synt_flagellum-secretory_path_III_N, Flagellum-specific ATP synthase, N-terminal domain. The N-terminal domain of the flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The FliI ATPase is the soluble export component that drives flagellar protein export, and it shows extensive similarity to the alpha and beta subunits of F1-ATP synthase. Although they both are proton driven rotary molecular devices, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens, such as Salmonella and Chlamydia, also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway
VYGRVVRVVGLLLEAVGPQAPIGELCLIETADGLSILAEVVGFSGEKVLLMPLGELSGLSPGARVVPLGR
>gnl|CDD|349742 cd18118, ATP-synt_V_A-type_beta_N, V/A-type ATP synthase beta (B) subunit, N-terminal domain. The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core, that is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex which forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit
EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFT
GE
>gnl|CDD|349743 cd18119, ATP-synt_V_A-type_alpha_N, V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain. The alpha (A) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes
KGKIYRVSGPVVVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTGK
>gnl|CDD|349413 cd18120, ATP-synt_Vo_Ao_c, Membrane-bound Vo/Ao complexes of V/A-type ATP synthases, subunit c. Vo/Ao-ATP synthase subunit c. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPases) is exclusively found in archaea and functions like the F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. The V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. The V1 complex consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The Vo complex consists of five different subunits: a, c, c', c'', and d. The Ao/A1 complexes are composed of nine subunits in a stoichiometry of A(3):B(3):C:D:E:F:H(2):a:c(x). ATP is synthesized on the A3:B3 hexamer and the energy released during that process is transferred to the Ao complex, which consists of the C-terminal segment of subunit a and subunit c
AYLGAALAVGLSCLGAGIAVGMVGAAAIGAIAEKPELFGKALIFVGLAEGLAIYGLIVAILI
>gnl|CDD|349414 cd18121, ATP-synt_Fo_c, membrane-bound Fo complex of F-ATP synthase, subunit c. Subunit c (also called subunit 9, or proteolipid) of the Fo complex of F-ATP synthase. The F-ATP synthase (also called FoF1-ATPase) consists of two structural domains: the F1 (factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons though the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Methanosarcina acetivorans
ALGAGLAIGLGAIGPGIGIGLAAAKALEGIARQPEAAGKIRTTMIIGLALIESLAIYALVIALIL
>gnl|CDD|467672 cd18122, GAPDH_like_C, C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins. GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins
CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSEVRAIIPNIPKNETKHAPETGKVLGE
IGKPIKVDGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVY
GVPVGRQREFAFDDNKLKVFSAVDNE
>gnl|CDD|467673 cd18123, GAPDH_C, C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). GADPH family members include the ubiquitous NAD+ or NADP+ utilizing type I, type II NADP+ utilizing mainly from archaea, and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose
CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVL
PELNGKLTGMAVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEGKGRLGYTEAEDVSSDFRGDIFES
VFDAESIIAVNDNEVKLMQWYDNE
>gnl|CDD|467674 cd18124, ASADH_C_like, C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 protein and similar proteins. The family includes aspartate beta-semialdehyde dehydrogenase (ASADH), NADP-dependent malonyl-CoA reductase (MCR), and USG-1 protein. These proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain and are members of the GAPDH superfamily of proteins. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. NADP-dependent MCR (EC 1.2.1.75) is mainly found in Archaea. It catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA. Sequence comparison suggests that the archaeal MCR gene (mcr) has evolved from the duplication of a common ancestral ASADH gene (asd). The biological function of USG-1 protein and homologs remains unclear. They are homologs to ASADH but lack the conserved active site residues of the ASADH protein C-terminal catalytic domain
CTVSLLVMALKPLFAKFLVEWVSVATXQAVSGAGYENMRELLSQMGELMRAGPLPTGVFSXAIADNLIPW
IDKVLDNGQSKEEWKIQAEANKILGTLDSPIPISVTCNRVPVLDGHSQSFTLKLKEDVPLEEVEEVLDAH
KPWVKVIPNDYAIRPQPRLDRKVTGGLSTPVGRIRKDAMDPFDVNAFAVSDNT
>gnl|CDD|467675 cd18125, AGPR_C, C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar proteins. N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC), while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase (EC 2.7.2.8) domain and a C-terminal AGPR domain. There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. This family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase, EC 1.2.1.103/EC 1.2.1.106), which is involved in both the arginine and lysine biosynthetic pathways
CYATAALLALYPLLKAGLLKPTPITVTGVSGTSGAGRAASPASLHPEVAGSLRPYALSGHRHTPEIAQNL
GGKHNVHFTPHVGPWVRGILMTIQCFTQKGWSLRQLHEAYREAYAGEPFVRVMPQGKGPDPKFVQGTNYA
DIGVELEEDTGRLVVMSAIDNLVKGA
>gnl|CDD|467676 cd18126, GAPDH_I_C, C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose
CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIP
ELKGKLTGMAFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHS
SIFDATATIVLGGNLVKVVAWYDNE
>gnl|CDD|467677 cd18127, GAPDH_II_C, C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to type II NADP+ utilizing GAPDHs, mainly from archaea
SCNTTGLSRVLKALDRAFGLKRVRATIVRRAADPGKHKKGVINAIVPEPKDPSHHAPDVKTVFPDLDITT
SAVKVPTTLMHLHTINVELKRKVSREEVLEALASNPRIALVDKEDGTSTNQVFELARDLGRPRGDIYEVA
VWEDSIVVDGNELYLFYAVPQE
>gnl|CDD|467678 cd18128, ASADH_C, C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins. Aspartate beta-semialdehyde dehydrogenase (ASADH; EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins
CTVSLMLMALGGLFQKFLVEWVSVATYQAVSGAGXPIAGNLIPWIDVFLDNGQTKEEWKGQAETNKILGD
LDSPIPISGTCVRVGVLRCHSQAFTIKLKEDAPIEEVEEAIAAHNXWIKVIPNVDRITPRTPANVTGTLS
TPVGRIRKDAMGPFDLQAFTVGDNL
>gnl|CDD|467679 cd18129, ASADH_C_USG1_like, C-terminal domain of USG-1 protein and similar proteins. The family includes Escherichia coli USG-1 protein, Pseudomonas aeruginosa USG-1 homolog proteins and similar proteins. Although its biological function remains unknown, it is found to be homologous to aspartate beta-semialdehyde dehydrogenase (ASADH) which contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain. However, USG-1 proteins lack the conserved active site residues of the ASADH protein C-terminal domain
PAAIALARVLAPLHDAAGLERVVVTVLQPVSEAGQAGVDELARQTARLLNGQPVEPEVFPRQLAFNLLPQ
VGDFDADGLSDEERRIAAELRRLLGGPDLPVSVTCVQVPVFYGHSASVHVELAEPVDLEEVRAALAAAPG
LELADDAEAPPYPVDAAGSDDVLVGRVRQDPGNPRGLWLWAVADNL
>gnl|CDD|467680 cd18130, ASADH_C_arch_fung_like, C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins. The family corresponds to a new branch of aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share very little sequence homology with the typical bacterial ASADHs. They are mainly from archaea and fungi. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. This family also includes NADP-dependent malonyl-CoA reductase (MCR, EC 1.2.1.75), which catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA
CSTAGLALPLKPLHDFFGIEAVIVTTMQAISGAGYPGVPSLDILDNVIPYIGGEEEKIESETKKILGTLN
EDKIEPADFKVSATCNRVPVIDGHTESVSVKFKERPDPEEVKEALENYEPEPQVLGPPSAPKPIIVVEDE
PRRPQPRLDRDAGDGMAVTVGRIRKDDDFDLKFVLLSHNT
>gnl|CDD|467681 cd18131, ASADH_C_bac_euk_like, C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins. The family corresponds to a new branch of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share less sequence homology with the other bacterial ASADHs. The second isoform of ASADH in Vibrio cholerae is one of the prototypes of this family. It also includes ASADHs from Streptococcus pneumoniae, Mycobacterium tuberculosis, Thermus thermophilus, as well as from eukaryotes. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins
CSTIQMVVALKPLHDAFGLKRVVVSTYQAVSGAGAAAMEELEEQTRGLLNGKEAEPKVFPYQIAFNVIPH
IDVFLDNGYTKEEMKMVNETRKILGDPDLRVSATCVRVPVFRGHSESVNIEFEKPISVEEAREALAKAPG
VVVVDDPANNVYPTPLDAAGKDDVFVGRIRKDISVPNGLNLWVVGDNL
>gnl|CDD|350838 cd18133, HLD_clamp, helical lid domain of clamp loader-like AAA+ proteins. Clamp loader complexes are multisubunit complexes that play an important role in DNA replication. They open sliding clamps for assembly and close them around DNA, specifically targeting them to sites where DNA synthesis is initiated and orienting them correctly for replication. The subunits belong to the clamp loader clade of AAA+ superfamily
LDQEQLKRRLAAIAEQEKLKLDDAALQALAYISEGDLRKALNALQRAAALGDDGKISLDRVYQAV
>gnl|CDD|350839 cd18137, HLD_clamp_pol_III_gamma_tau, helical lid domain of DNA polymerase III subunits gamma and tau. DNA polymerase III subunit gamma/tau is part of the DNA polymerase III holoenzyme. Gamma and tau subunits are isoforms, both containing the helical lid domain. Gamma interacts with the delta subunit to transfer the beta subunit on the DNA while tau serves as a scaffold to help in the dimerization of the core complex. Both are members of the clamp-loader clade of the AAA+ superfamily
ISVEDIVGRLAHILEKEGIEIEDEALELIARAAEGSMRDALSLLDQAIAFGGGRVTLDDVREMLG
>gnl|CDD|350840 cd18138, HLD_clamp_pol_III_delta, helical lid domain of DNA polymerase III subunits delta. DNA polymerase III subunit delta is part of the DNA polymerase III holoenzyme. the delta subunit id required for ring opening and binds the beta subunit. It is a member of the clamp-loader clade of the AAA+ superfamily
PEGQQLPQWIQQRAKQAGLQLDPDALQLLAERVEGNLLAAAQEIEKLALLYPDGPITAEQVEAAV
>gnl|CDD|350841 cd18139, HLD_clamp_RarA, helical lid domain of recombination factor protein RarA. Recombination factor RarA (Replication associated recombination gene/protein A, also known as MgsA (Maintenance of genome stability A) or Mgs1 in yeast and WRNIP1 in mammals) is a member of the clamp-loader clade of the AAA+ superfamily. It functions as a tetramer. RarA co-localize with the replication fork throughout the cell cycle and may play a role in the rescue of stalled replication forks
LSEEDLEKLLKRALEDKERGGDRKVTIDDEALELLAEAADGDARSALNLLELAVLSAEEDGGIVITLEDL
EEVLQ
>gnl|CDD|350842 cd18140, HLD_clamp_RFC, helical lid domain of replication factor C subunit. Replication factor C (RFC) is five-protein clamp loader complex that forms a stable ATP-dependent complex with the sliding clamp, PCNA, which binds specifically to primed DNA. RFC subunits belong to the clamp loader clade of the AAA+ superfamily
LSKEQIVKRLREICKKEGVKIDEEALEAIAEKSEGDMRKAINDLQAAAAGGGVITEEDVYEVA
>gnl|CDD|381143 cd18159, REC_OmpR_NsrR-like, phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators. Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISNV
PIIFISSRDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL
>gnl|CDD|381144 cd18160, REC_CpdR_CckA-like, phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains. Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDIDIVVTDIVMPEMDGIELAREARKID
PDVKILFISGGAAAAPELLSDAVGDNATLKKPF
>gnl|CDD|381145 cd18161, REC_hyHK_blue-like, phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase. Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIDLLVTDVIMPGGMNGSQLAEEARRRR
PDLKVLLTSGYAENAIEGGDLAPGVDVLSKPF
>gnl|CDD|349482 cd18172, M14_CP_plant, Zinc carboxypeptidase, including SOL1, a carboxypeptidase D in plant. This family includes only plant members of the carboxypeptidase (CP) N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs). It includes Arabidopsis thaliana SOL1 carboxypeptidase D which is known to possess enzymatic activity to remove the C-terminal arginine residue of CLE19 proprotein in vitro, and SOL1-dependent cleavage of the C-terminal arginine residue is necessary for CLE19 activity in vivo. The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes eight members, of which five (CPN, CPE, CPM, CPD, CPZ) are considered enzymatically active, while the other three are non-active (CPX1, PCX2, ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily, enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form; rather, they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition, all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation
YHSNAELEDALKAFTRRCGAISRLIVIGSSVNGFPLWALEISDGPGEDETEPAFKFVGNMHGDEPVGREL
LLRLADWLCANYKAKDPLAAKIVENAHLHLVPTMNPDGFARRRRNNANNVDLNRDFPDQFFPKNLRNDLA
ARQPETLAVMNWSRSVRFTASANLHEGALVANYPWDGNADGRTKYSASPDDATFRRLASVYAQAHPNMAK
SKEFPGGITNGAQWYPLYGGMQDWNYLHTGCMDLTLEVNDNKWPPEDRLVQIWAEHRKAMLALAAA
>gnl|CDD|349483 cd18173, M14_CP_bacteria, bacterial peptidase M14 carboxypeptidase, uncharacterized. This family contains only bacterial carboxypeptidase (CP) members of the M14 family of metallocarboxypeptidases (MCPs), mostly of which have yet to be characterized. The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes eight members, of which five (CPN, CPE, CPM, CPD, CPZ) are considered enzymatically active, while the other three are non-active (CPX1, PCX2, ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily, enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form; rather, they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition, all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation
WDSYPTYEEYEAMMQSFAANYPNICRLVSIGTSVQGRKLLALKISDNVNTEEAEPEFKYTSTMHGDETTG
YELMLRLIDYLLTNYGTDPRITNLVDNTEIWINPLANPDGTYAGGNNTVSGATRYNANGVDLNRNFPDPV
DGDHPDGNGWQPETQAMMNFADEHNFVLSANFHGGAEVVNYPWDTWYSRHPDDDWFQDISREYADTNQAN
SPPMYMSEFNNGITNGYDWYEVYGGRQDYMYYWHGCREVTIELSNTKWPPASQLPTYWNYNRESLLNYIE
Q
>gnl|CDD|349484 cd18174, M14_ASTE_ASPA_like, Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup. A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD
LLVTAGVHGYEYASIEALQRLIKELDPAKLSGTVIVVPIANIPAFEGRSIYVNPLDGKNLNRSFPGDPDG
TPTERLAHWLTTNVIARADYYIDLHGGDLNEDLRPFVYYYETGNAALDAASREMAEAFGLDHIVFYKARL
KASRGSLYTQAAALLRGIPAILVEAGGLGSRDEEDVARHVEGVLNVL
>gnl|CDD|349415 cd18175, ATP-synt_Vo_c_ATP6C_rpt1, V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar proteins. ATP6C (also called the V-ATPase 16 kDa proteolipid subunit, or vacuolar proton pump 16 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells
FFGYMGAAAALVFSNLGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGILGIYGLVVAVLISNNI
>gnl|CDD|349416 cd18176, ATP-synt_Vo_c_ATP6C_rpt2, V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar proteins. ATP6C (also called V-ATPase 16 kDa proteolipid subunit, or vacuolar proton pump 16 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells
LFKGFAHLGAGLSVGLSGLAAGFAIGIVGDAGVRATAQQPKLFVGMILILIFAEALGLYGLIVALILS
>gnl|CDD|349417 cd18177, ATP-synt_Vo_c_ATP6F_rpt1, V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins. ATP6F (also called V-ATPase 21 kDa proteolipid subunit, or vacuolar proton pump 21 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells
WAALGIGLSIGLSVVGAAWGIFITGSSIVGAGVKAPRIRTKNLISIIFCEAVAIYGIIMAIVL
>gnl|CDD|349418 cd18178, ATP-synt_Vo_c_ATP6F_rpt2, V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins. ATP6F (also called V-ATPase 21 kDa proteolipid subunit, or vacuolar proton pump 21 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells
AGYALFGAGLTVGFSNLACGISVGIIGSGAALADAKNPSLFVKILIVEIFASAIGLFGLIVGILM
>gnl|CDD|349419 cd18179, ATP-synt_Vo_Ao_c_NTPK_rpt1, V-type sodium ATPase subunit K (NTPK) and similar proteins. NTPK (also called Na(+)-translocating ATPase subunit K, or sodium ATPase proteolipid component) is involved in ATP-driven sodium extrusion
LALIGAALAVGLAGIGSAIGVGIAGQAAAGVLAEKPEKFGKLLVLQALPGTQGIYGFVIAFLI
>gnl|CDD|349420 cd18180, ATP-synt_Vo_Ao_c_NTPK_rpt2, V-type sodium ATPase subunit K (NTPK) and similar proteins. NTPK (also called Na(+)-translocating ATPase subunit K, or sodium ATPase proteolipid component) is involved in ATP-driven sodium extrusion
GLAILGAGLPVGIVGLFSAIYQGKVAAAGIGAVAKRPEEFGKAIILAAMVETYAILGLLISILI
>gnl|CDD|349421 cd18181, ATP-synt_Vo_Ao_c_TtATPase_like, Thermus thermophilus V/A-ATPase and similar proteins. This family includes a group of uncharacterized ATPase similar to Thermus thermophilus V/A-ATPase, which is homologous to the eukaryotic V-ATPase, but has a simpler subunit composition and functions in vivo to synthesize ATP rather than pump protons
IAIGAGLAIGLAAIGTGWAQSRIGAAAVGAIAEKPELFGTALILTAIPETLVILGFVIAFLL
>gnl|CDD|349422 cd18182, ATP-synt_Fo_c_ATP5G3, ATP synthase F(0) complex subunit C3 (ATP5G3) and similar proteins. ATP5G3 (also called ATP synthase lipid-binding protein, ATP synthase proteolipid P3, ATP synthase proton-transporting mitochondrial F(o) complex subunit C3, ATPase protein 9, or ATPase subunit c) transports protons across the inner mitochondrial membrane to the F1-ATPase protruding on the matrix side, resulting in the generation of ATP
KYIGAGLATIGLAGAGIGIGNVFGSLINGVARNPSAKQQLFTYAILGFALTEAIGLFALMVAFLI
>gnl|CDD|349423 cd18183, ATP-synt_Fo_c_ATPH, F-type proton-translocating ATP synthase (ATPH) and similar proteins. This family includes subunit c of chloroplast F-ATP synthase (F1Fo-ATP synthase), also known as ATP synthase F(o) sector subunit c (also called ATPase subunit III, F-type ATPase subunit c, or F-ATPase subunit c)and similar proteins. It is a proton-translocating subunit of the ATP synthase encoded by gene atpH
LISAASVIAAGLAVGLAAIGPGIGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALA
LLFAN
>gnl|CDD|349424 cd18184, ATP-synt_Fo_c_NaATPase, F-type sodium ion-translocating ATP synthase and similar proteins. This family includes F-type Na(+)-coupled ATP synthase and similar proteins
AAIGAGLAMIAGIGPGIGQGYAAGKAVEAVGRNPEAEGKIRSTMILGAAVAETTAIYGLIIALLL
>gnl|CDD|349425 cd18185, ATP-synt_Fo_c_ATPE, F-type proton-translocating ATPase subunit c (ATPE) and similar proteins. This family includes subunit c of F-ATP synthase (also called ATP synthase F(o) sector subunit c, F-type ATPase subunit c, or F-ATPase subunit c) and similar proteins. It is a proton-translocating subunit of the ATP synthase encoded by gene atpE
LIAAGLAIGLAAIGAAIGDGLVGSKFIEGIARQPELRGKLRTNMFIGVGLVEAVPIIAVVIALLL
>gnl|CDD|349497 cd18186, BTB_POZ_ZBTB_KLHL-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing (ZBTB) proteins, Kelch-like (KLHL) proteins, and similar proteins. This family includes a variety of BTB/POZ domain-containing proteins, such as zinc finger and BTB domain-containing (ZBTB) proteins and Kelch-like (KLHL) proteins. They have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
LCDVTLVVGGREFPAHRAVLAARSPYFRAMFSSGMKESSSSEIELDDVSPEAFEALLDYIYTGELELSEE
NVEELLAAADKL
>gnl|CDD|349498 cd18187, BTB_POZ_Kv_KCTD, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in voltage-gated potassium (Kv) channels and potassium channel tetramerization domain-containing (KCTD) proteins. This family includes two protein groups: voltage-gated potassium (Kv) channels and potassium channel tetramerization domain-containing (KCTD) proteins. Kv channels are membrane proteins with fundamental physiological roles. They are responsible for a variety of electrical phenomena, such as the repolarization of the action potential, spike frequency adaptation, synaptic repolarization, and smooth muscle contraction. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels, and others. All family members contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization
VVLNVSGTRFVTNRQTLTRHPDTLLGRMFKPGREFTFPNETGEYFIDRDPTVFRTILNYYRTGKLNCPDG
ISIPDLREECDFY
>gnl|CDD|349499 cd18190, BTB_POZ_ETO1-like, BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Arabidopsis thaliana ethylene-overproduction protein 1 (ETO1) and similar proteins. ETO1, also called protein ethylene overproducer 1, is an essential regulator of the ethylene pathway, which acts by regulating the stability of 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes. It may act as a substrate-specific adaptor that connects ACS enzymes, such as ACS5, to ubiquitin ligase complexes, leading to proteasomal degradation of ACS enzymes. The family also includes ETO1-like proteins 1 (EOL1) and 2 (EOL2). ETO1, EOL1, and EOL2 contain a BTB domain and tetratricopeptide (TPR) repeats. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
DLVFCVGGEKFCCVRKKIASLSRPFKAMLYGNFRESTSDCIDFEENGISIEAMRAVIDFSVTGRLDLFSV
ENVHEVLELASKF
>gnl|CDD|349500 cd18191, BTB_POZ_ARMC5, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in armadillo repeat-containing protein 5 (ARMC5). ARMC5 plays a role in steroidogenesis, and modulates the expression and cortisol production of steroidogenic enzymes. It negatively regulates adrenal cells survival. It contains armadillo (ARM) repeats and a BTB domain, which is a common protein-protein interaction motif of about 100 amino acids
AHDLRFLLDGGTQLPASRAALTGASEVFRAMLEGGFAEAQQDLVPLRQVPSGAFLPVLHYLHGCRGCDAN
EDDEKSDQSPEGDLMKSSLGQTLEVAGRFL
>gnl|CDD|349501 cd18192, BTB_POZ_ZBTB1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 1 (ZBTB1). ZBTB1 acts as a transcriptional repressor that represses cAMP-responsive element (CRE)-mediated transcriptional activation. It also has a role in translesion DNA synthesis, and is essential for lymphocyte development. ZBTB1 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
RPSHSSYVLQQLNNQREWGFLCDCCIAIDDIYFQAHKAVLAACSSYFRMMFINHQHTTAQLNLSNMKISA
ECFDLILQFMYLGKIMTAPSDFEQLKVAMNYLQLYYIPECLEDI
>gnl|CDD|349502 cd18193, BTB_POZ_ZBTB2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 2 (ZBTB2). ZBTB2 is a POZ domain Kruppel-like zinc finger (POK) family transcription factor acting as a potent repressor of the ARF-HDM2-p53-p21 pathway, which is important in cell cycle regulation. It represses transcription of the ARF, p53, and p21 genes, but activates the HDM2 gene. ZBTB2 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
LANHGLILLQQLNAQREFGFLCDCTVAIGDVYFKAHKSVLASFSNYFKMLFVHQTSECVRLKPTDIQPDI
FSYLLHLMYTGKMAPQLIDPVRLEQGIKFLHAYPLIQEASLASHG
>gnl|CDD|349503 cd18194, BTB_POZ_ZBTB3-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing proteins, ZBTB3, ZBTB18, ZBTB42 and similar proteins. The family includes zinc finger and BTB domain-containing proteins, ZBTB3, ZBTB18 and ZBTB42. ZBTB3 is a transcription factor essential for cancer cell growth via the regulation of the reactive oxygen species (ROS) detoxification pathway. ZBTB18 is a sequence-specific transrepressor associated with heterochromatin. ZBTB42 is a transcriptional repressor that specifically binds DNA and probably acts by recruiting chromatin remodeling multiprotein complexes. Members of this family contain a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
MEFPEHSRQLLQCLREQRSQGFLCDCTVLVGSAQFPAHRAVLASCSMYFHLFYRDRLDKRDLVRLNSDIV
TAPAFGLLLDFMYEGRLALRDLPVEDVLAAASYLHMYDIVKVCKGRLQEKALAEADST
>gnl|CDD|349504 cd18195, BTB_POZ_ZBTB4, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 4 (ZBTB4). ZBTB4, also called KAISO-like zinc finger protein 1 (KAISO-L1), is a transcriptional repressor with bimodal DNA-binding specificity. It binds with a higher affinity to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' but can also bind to the non-methylated consensus sequence 5'-CTGCNA-3', also known as the consensus kaiso binding site (KBS). It can also bind specifically to a single methyl-CpG pair and can bind hemimethylated DNA but with a lower affinity compared to methylated DNA. ZBTB4 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
HAGALLLQLNEQRLRGLFCDVTLIAGDTKFRAHRSVLAASSPYFRELLSSPLPLGAAAVAAAPGATQSPE
RVLELPGVKAGVFSDVLNFIYSSRVALPGSAAAKELGAAGKRLGIPFLQGLEGG
>gnl|CDD|349505 cd18196, BTB_POZ_ZBTB5, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 5 (ZBTB5). ZBTB5 is a POZ domain Kruppel-like zinc finger (POK) family transcription repressor of cell cycle arrest gene p21 and a potential proto-oncogene stimulating cell proliferation. ZBTB5 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
FPGHFEQIFQQLNYQRLHGQLCDCVIVVGNRHFKAHRSVLAACSTHFRALFTVAEGDQTMNMIQLDSEVV
TAEAFAALIDMMYTSTLMLGESNVMDVLLAASHLHLNSVVKACKHYLTTRTLPMSP
>gnl|CDD|349506 cd18197, BTB_POZ_ZBTB6, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 6 (ZBTB6). ZBTB6, also called zinc finger protein 482 (ZNF482) or zinc finger protein with interaction domain, may be involved in transcriptional regulation. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
LHFKFEQQGDAVLQKMNLLRQQNLFCDVSIYINDTEFHGHKVILAACSTFMRDQFLLNQSKQVRITILQS
AEVGRKLLLSCYTGALEVKKKELLKYLTAASYLQMVHIVEKCTEAL
>gnl|CDD|349507 cd18198, BTB_POZ_ZBTB7, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 7 (ZBTB7). There are three ZBTB7 isoforms: ZBTB7A, ZBTB7B, and ZBTB7C. ZBTB7A is a transcription repressor of key glycolytic genes, including GLUT3, PFKP, and PKM, and its downregulation in human cancer contributes to tumor metabolism. ZBTB7B is a transcriptional regulator of extracellular matrix gene expression. ZBTB7C is a transcriptional repressor with a pro-oncogenic role that relies upon binding to p53 and inhibition of its transactivation function. ZBTB7 isoforms contain a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
IGIPFPDHSSEILSGLNEQRTQGLLCDVVILVQGREYRTHRSVLAACSQYFKKLFTSGAVVDQQNVYEID
FVSPEALTALLEFAYTATLTVSTANVGDILSAARLLEIPCVSHVCAEILD
>gnl|CDD|349508 cd18199, BTB_POZ_ZBTB8, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 8 (ZBTB8). There are two ZBTB8 isoforms: ZBTB8A and ZBTB8B. ZBTB8A is a novel proto-oncoprotein that stimulates cell proliferation. ZBTB8B may be involved in transcriptional regulation. They both contain a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
HQSRLLGQLNEQRKQDFFCDCSIIVEGRIFKAHRNVLFASSGYFRMLLSHYIQDTGRPSTASFDVFSSDA
FSIILDFVYSGKLSLTSQNVIEVMSAASYLQMTDVINVCKTFI
>gnl|CDD|349509 cd18200, BTB_POZ_ZBTB9, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 9 (ZBTB9). ZBTB9 may be involved in transcriptional regulation. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
YSSALLETLNKHRLEGKFCDLSVHVQGRVFRAHKAVLAASSPYFHDKLLLNDTNCLVLPSVIEAAAFENL
LQLIYSGRLTLCMDALPSHLLVASGLQMWQVVDRCSELLKE
>gnl|CDD|349510 cd18201, BTB_POZ_ZBTB10, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 10 (ZBTB10). ZBTB10, also called zinc finger protein RIN ZF, is an mRNA target of miR-27a and a transcriptional repressor of Specificity protein (Sp) expression. The microRNA-27a:ZBTB10-specificity protein pathway is involved in follicle stimulating hormone-induced VEGF, Cox2, and survivin expression in ovarian epithelial cancer cells. ZBTB10 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
ENSYCYQLLQELNEQRKKGILCDVNIVVSGKVFRAHKNILVAGSRFFKTLYCFTNKESCDQTTVTHLDVV
AVQGFSVILDFMYSGNLVLTSQNAIEVMSVASYLQMTEVVQSCRNFIKDALN
>gnl|CDD|349511 cd18202, BTB_POZ_ZBTB11, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 11 (ZBTB11). ZBTB11 is a transcriptional repressor of TP53. It is critical for basal and emergency granulopoiesis. It regulates neutrophil development through its integrase-like zinc finger domain. ZBTB11 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
KHGQTVLDQLNQQRLNNQFCDVTLLIEGEEYKAHKSVLAANSEYFRELFIEKGAVSSHEAVVDLSGFCKS
SFLPLLEFAYTSELTFDFCSMAEVAMLARHLFMNEVLEICESVHKQME
>gnl|CDD|349512 cd18203, BTB_POZ_ZBTB12, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 12 (ZBTB12). ZBTB12, also called protein G10, may be involved in transcriptional regulation. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
LRFQLPGHEAATLRNMNQLRSEERFCDVTIVADSLKFRGHKVVLAACSPFLRDQFLLNPSSELQVSLMHS
SRVVADLLLSCYTGALEFSVRDIVNYLTAASYLQMEHVVEKCRGALSQFIEP
>gnl|CDD|349513 cd18204, BTB_POZ_ZBTB14, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 14 (ZBTB14). ZBTB14 is also called zinc finger protein 161 (Zfp-161), zinc finger protein 478, zinc finger protein 5 (ZF5), or Zfp-5. It is a novel transcriptional activator of the dopamine transporter, binding it's promoter at the consensus sequence 5'-CCTGCACAGTTCACGGA-3'. It also binds to 5'-d(GCC)(n)-3' trinucleotide repeats in promoter regions and acts as a repressor of the FMR1 gene. ZBTB14 acts as a transcriptional repressor of MYC and thymidine kinase promoters. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
HKTVFLKTLNEQRLEGEFCDIAIVVEDVKFRAHRCVLAACSTYFKKLFKKLEVDSSSVIEIDFLRSDIFE
EVLNYMYTAKISVKKEDVNLMMSSGQILGIRFLDKLCSQKRDVS
>gnl|CDD|349514 cd18205, BTB_POZ_ZBTB16_PLZF, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 16 (ZBTB16). ZBTB16 is also called promyelocytic leukemia zinc finger protein, zinc finger protein 145, or zinc finger protein PLZF. It is a DNA-binding transcription factor essential for undifferentiated cell maintenance. ZBTB16 also acts as a downstream transcriptional regulator of Osterix and can be useful as a late marker of osteoblastic differentiation. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
HPTGLLHKANQMRLAGTLCDVVIMVDSQEFHAHRTVLACTSKMFEILFHRNSQHYTLDFLSPKTFQQILE
YAYTATLQAKVEDLDDLLYAAEILEIEYLEEQCLKIL
>gnl|CDD|349515 cd18206, BTB_POZ_ZBTB17_MIZ1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 17 (ZBTB17). ZBTB1 is also called c-Myc-interacting zinc finger protein 1 (Miz-1), zinc finger protein 151, or zinc finger protein 60. It is a poly-Cys2His2 zinc finger (ZF) transcription factor that can function as an activator or repressor depending on its binding partners, and by targeting negative regulators of cell cycle progression. ZBTB17 has been implicated in cardiomyopathy and is important in cardiac stress response. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
DFPQHSQHVLEQLNQQRQLGLLCDCTFVVDGVDFKAHKAVLAACSEYFRMLFVDQKDVVHLDISNAAGLG
QVLEFMYTAKLSLSPENVDDVLAVATFLQMQDIVTACHALKS
>gnl|CDD|349516 cd18207, BTB_POZ_ZBTB19_PATZ1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in POZ-, AT hook-, and zinc finger-containing protein 1 (PATZ1). PATZ1 is also called zinc finger and BTB domain-containing protein 19 (ZBTB19), BTB/POZ domain zinc finger transcription factor, protein kinase A RI subunit alpha-associated protein, zinc finger protein 278, or zinc finger sarcoma gene protein. It is an important transcriptional regulatory factor that regulates divergent pathways depending on the cellular context. For instance, it acts as a transcriptional suppressor that functions in T lymphocytes. It is also a DNA damage-responsive transcription factor that inhibits p53 function. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
SYTYQVSQHSADMLHNLNQQRKSGGRFCDVLLRVGEESFPAHRAVLAACSEYFESVFSAQEGDGGTPREL
EMHTISSKVFGDILDFAYTSRIVVRLESFPELMTAAKFLLMRSVIDICQEVIKQSNVQ
>gnl|CDD|349517 cd18208, BTB_POZ_ZBTB20_DPZF, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 20 (ZBTB20). ZBTB20, also called dendritic-derived BTB/POZ zinc finger protein (DPZF) or zinc finger protein 288, may be a transcription factor involved in hematopoiesis, oncogenesis, and immune responses. It is an essential regulator of hepatic lipogenesis and may be a therapeutic target for the treatment of fatty liver disease. It also functions as a critical regulator of anterior pituitary development and lactotrope specification. Moreover, it promotes astrocytogenesis during neocortical development. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
HSINLHNFSNSVLETLNEQRNRGHFCDVTVRIHGSMLRAHRCVLAAGSPFFQDKLLLGYSDIEIPSVVSV
QSVQKLIDFMYSGVLRVSQSEALQILTAASILQIKTVIDECTRIVSQ
>gnl|CDD|349518 cd18209, BTB_POZ_ZBTB21_ZNF295, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 21 (ZBTB21). ZBTB21, also called zinc finger protein 295 (ZNF295), is a transcription repressor that acts in a selective manner on different promoters. It may be involved in the bi-directional control of gene expression in concert with another transcription factor ZFP161. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
HAISLLSALNEERLKGQLCDVLLIVGDQKFRAHKNVLAASSEYFQSLFTEKENESQSVFQLDFCEPDAFE
NVLNYIYSSSLFVEKSSLAAVQELGYSLGISFLTNIVSKTPQ
>gnl|CDD|349519 cd18210, BTB_POZ_ZBTB22_BING1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 22 (ZBTB22). ZBTB22, also called protein BING1 or zinc finger protein 297, may be involved in transcriptional regulation. Its gene, together with BING 3-5, TAPASIN, DAXX, RGL2, and HKE2, form a dense cluster at the centromeric end of the major histocompatibility complex class I region. ZBTB22 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
FPEITSSLLESLNQQRMEGKLCDISIHVQGRVFRAHRAVLAASSPYFHDQVLLKNMSSISLPGVMDPGAF
ESVLASAYTGKLTMLADEIVNYLTVGSVLQMWHIVDKCTELL
>gnl|CDD|349520 cd18211, BTB_POZ_ZBTB23_GZF1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in glial cell line-derived neurotrophic factor-inducible zinc finger protein 1 (GZF1). GZF1 is also called GDNF-inducible zinc finger protein 1, zinc finger and BTB domain-containing protein 23 (ZBTB23), or zinc finger protein 336 (ZNF336). It is a sequence-specific transcriptional repressor that binds the GZF1 responsive element (GRE), with the consensus sequence of 5'-TGCGCN[TG][CA]TATA-3'. It may play a role in renal branching morphogenesis. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
VLLESKSAPSNLLNEMHKLRLLGHLCDVTVQVEHQGSKEEFSAHKAVLAASSKYFKEVFLNEKISDGKNT
NVMLNEIYTADFASFLEFVYTAKVEVEEDRVQRMLEIAEKLKCLDLSETCFQLKKQML
>gnl|CDD|349521 cd18212, BTB_POZ_ZBTB24_ZNF450, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 24 (ZBTB24). ZBTB24, also called zinc finger protein 450, functions as a transcription factor essentially involved in B-cell functions in humans. The loss-of-function mutations in ZBTB24 can cause ICF2 (immunodeficiency, centromeric instability and facial anomalies syndrome 2) with immunological characteristics of greatly reduced serum antibodies and circulating memory B cells. ZBTB24 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
IHSKTHKDTVLTNFEEQRKKDFLCDITLIVENVQFRAHKALLAASSEYFSMMFADEGEVGQSIYMLEGMV
AETFGALLEFIYTGCLQVGEKSLEQILATAQFLKVNDLVKAYSDYQNN
>gnl|CDD|349522 cd18213, BTB_POZ_ZBTB25_ZNF46_KUP, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 25 (ZBTB25). ZBTB25, also called zinc finger protein 46 (ZNF46) or zinc finger protein KUP, is a transcription repressor that facilitates viral RNA transcription and replication. It interacts with viral RNA-dependent RNA polymerase (RdRp) proteins and modulates their transcription activity. It also functions as a viral RNA-binding protein, binding preferentially to the U-rich sequence within 5' UTR of vRNA. ZBTB25 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
VSSHSLVLLQQLNMQREFGFLCDCTVAIGDVYFKAHRAVLAAFSNYFKMIFIHQSSECIKIQPTDIQPDI
FSYLLHIMYTGKGPKQSVDHSRLEEGIRFLHANYLSRIATEMNQDFSPETMQSSNLYG
>gnl|CDD|349523 cd18214, BTB_POZ_ZBTB26_Bioref, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 26 (ZBTB26). ZBTB26, also called zinc finger protein 481 (ZNF481) or zinc finger protein Bioref, may be involved in transcriptional regulation. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
LHFRFENYGDSMLQKMNKLREQNKFCDVTVHIDDLEVPGHKVVFAAGSPFLRDQFLLNDSREVQISILQN
SEVGRQLLLSCYTGVLEFPEMELVNYLTAASFLQMSHIVERCTQALWKFIKP
>gnl|CDD|349524 cd18215, BTB_POZ_ZBTB27-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in B-cell lymphoma 6 proteins, BCL-6 and BCL-6B. This family includes B-cell lymphoma 6 proteins, BCL-6 and BCL-6B. BCL-6 is a transcriptional repressor mainly required for germinal center (GC) formation and antibody affinity maturation, which have different mechanisms of action specific to the lineage and biological functions. BCL-6B is a sequence-specific transcriptional repressor in association with BCL-6. It may function in a narrow stage or be related to some events in the early B-cell development. Family members contain a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
RHASDVLLNLNRLRSRDILTDVVLVVGREQFRAHKTVLMACSGLFYSIFTDQLKNNVSVINLDPEIEPEG
FRILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFI
>gnl|CDD|349525 cd18216, BTB_POZ_ZBTB29-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in hypermethylated in cancer proteins, Hic-1 and Hic-2. The family includes hypermethylated in cancer proteins, Hic-1 and Hic-2. Hic-1 is a sequence-specific transcriptional repressor that recognizes and binds to the consensus sequence '5-[CG]NG[CG]GGGCA[CA]CC-3'. Hic-2 is a homolog of tumor suppressor Hic-1 that functions as a transcriptional regulator. Family members contain a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
PSHATQLLLQLNNQRTKGFLCDVIIVVENSLFRAHKNVLAASSGYFKSLVLHDNLIHLDQDMVSPTVFQQ
ILDFIYTGKLLDSLFEEPNLSEVLAAANYLQLPDLAALCRSKLKRGGK
>gnl|CDD|349526 cd18217, BTB_POZ_ZBTB31_myoneurin, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in myoneurin. Myoneurin, also called zinc finger and BTB domain-containing protein 31 (ZBTB31), is a novel member of the BTB/POZ-zinc finger family highly expressed in the neuromuscular system and is associated with neuromuscular junctions during the late embryonic period. It may function as a synaptic gene regulator. Myoneurin contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
HCEQLLERLNKQREAGFLCDCTIVIGQFQFKAHRNVLAAFSEYFGAQYKDTEDNIVFLDQSQVSADGFQK
LLEFIYTGNLNLDSWNVAEIHQAASYLGMEEVVAKCKIKME
>gnl|CDD|349527 cd18218, BTB_POZ_ZBTB32_FAZF_TZFP, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 32 (ZBTB32). ZBTB32 is also called FANCC-interacting protein, fanconi anemia zinc finger protein (FAZF), testis zinc finger protein (TZFP), or zinc finger protein 538 (ZNF538). It is a DNA-binding transcription factor that binds to the 5'-TGTACAGTGT-3' core sequence. It acts as a transcription suppressor that controls T cell-mediated autoimmunity. ZBTB32 is essential for down-regulation of GATA3 via ZPO2; this promotes aggressive breast cancer development. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
HSDRLLHLAARLRPAGALCDTLITVGSQEFPAHSLVLAGASQQLGRQLTNPNPGQWCLGEGISPSTFKQL
LDFVYGESVEVQPGELRPLLEAARALEVESLEEACWRALG
>gnl|CDD|349528 cd18219, BTB_POZ_ZBTB33_KAISO, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kaiso. Kaiso, also called zinc finger and BTB domain-containing protein 33 (ZBTB33), is a DNA methylation-dependent transcriptional repressor that binds to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3'. It also binds to the non-methylated consensus sequence 5'-CTGCNA-3', also known as the consensus kaiso binding site (KBS). It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
DTQYSGSLLKSLNEQRGHGLFCDVTVIVEDRKFRAHKNILSASSTYFHQLFSVAGQVVELNFIRADIFAE
ILNYIYSSKIVRVRSDLLEELIKSGQLLGVKFIAEL
>gnl|CDD|349529 cd18220, BTB_POZ_ZBTB34, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 34 (ZBTB34). ZBTB34 acts as a transcriptional regulator. It downregulates specificity protein (Sp) transcription factors Sp1, Sp3, and Sp4 in pancreatic cancer cells. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
IQFDVPEYSNTVLSQLNELRLQGKLCDIIVHIQGQPFRAHKAVLAASSPYFRDHSALSTMSGLSISVIKN
PNVFEQLLSFCYTGRMSLQLKDVVSFLTAASFLQMQCVIDKCTQILESIH
>gnl|CDD|349530 cd18221, BTB_POZ_ZBTB35_ZNF131, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger protein 131 (ZNF131). ZNF131, also called zinc finger and BTB domain-containing protein 35 (ZBTB35), is a transcriptional activator implicated as a regulator of Kaiso-mediated biological processes. It regulates cell growth of developing and mature T cells. It inhibits estrogen signaling by suppressing estrogen receptor alpha homo-dimerization, and plays a role in breast cancer cell proliferation. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
HYKVMLDRLNEQRELDQFTDITLIVDGHQFKAHKAVLAACSQFFYKFFQDFTQEPLVEIEGVSNMAFRHL
IEFTYTAKLMVQGEEEANDVWKAAEYLQMQEAIKALEFRNKES
>gnl|CDD|349531 cd18222, BTB_POZ_ZBTB37, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 37 (ZBTB37). ZBTB37 may be involved in transcriptional regulation. It is differentially expressed in aryl hydrocarbon receptor (AhR)-KO mice compared with WT mice, and may potentially contribute to the aging phenotype of AhR-KO mice. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
IQLEIPDFSNSVLSHLNQLRMQGRLCDIVVNVQGQSFRAHKVVLAASSPYFRDHMSLNEMSTVSISVIKN
PTVFEQLLSFCYTGRICLQLADIISYLTAASFLQMQHIIDKCTQILEGIHFKI
>gnl|CDD|349532 cd18223, BTB_POZ_ZBTB38_CIBZ, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 38 (ZBTB38). ZBTB38, also termed CIBZ, is a transcriptional regulator with bimodal DNA-binding specificity. It binds with a higher affinity to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3', as well as E-box elements (5'-CACGTG-3'). It can also bind specifically to a single methyl-CpG pair. ZBTB38 represses transcription in a methyl-CpG-dependent manner. It is a negative regulator of endoplasmic reticulum stress-associated apoptosis. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
HSDTVLSCLNEQRIQGILCDVTIVVEDTKFKAHKNVLAASSLYFKNAFSSQEIWISSHVLELPDLKAEVF
AEILNFIYSSKVVVKRQETVTDLVAAGKKLGITFLENLTDQNFS
>gnl|CDD|349533 cd18224, BTB_POZ_ZBTB39, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 39 (ZBTB39). ZBTB39 may be involved in transcriptional regulation. Its specific function is as yet unknown. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
RIKLHSSDHPNNLLKELNKCRLSETMCDVTIVVGNRSFAAHKAVLACAAGYFQKLFLSTELDVARTYVVD
FITPANFEKVLSFIYTSELFTDLINVGVIYEVAEKLGMEDLLKACHSTFPDLE
>gnl|CDD|349534 cd18225, BTB_POZ_ZBTB40, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 40 (ZBTB40). ZBTB40 may be involved in transcriptional regulation. Single-nucleotide polymorphisms of ZBTB40 are associated with bone mineral density in European and East-Asian populations. ZBTB40 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
MELPNYSRQLLQQLHTLRKEQQFCDCTIFIGTFHFRAHKLVLAASSLLFKSLLDSTDTISIDASVVSPEE
FALLLEMVYTGKLPPGKHNFTKIISVADSLQMFDVAVSCKNLLTSL
>gnl|CDD|349535 cd18226, BTB_POZ_ZBTB41, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 41 (ZBTB41). ZBTB41, also called FRBZ1, may be involved in transcriptional regulation. Its specific function is as yet unknown. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
SLQYNKNLLKYLNDDRQKQSSFCDLVITVEGKEFSAHKVVVAVGSSYFHACLSKNPNTDAVTLDHVSYSV
FQHLLEFLYTSEFFVYENEIPLVLEAAKFLDIIDAVKLLTNEAV
>gnl|CDD|349536 cd18227, BTB_POZ_ZBTB43, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 43 (ZBTB43). ZBTB43, also called zinc finger and BTB domain-containing protein 22B (ZBTB22b), zinc finger protein 297B (ZNF297B), or ZnF-x, may be involved in transcriptional regulation. It interacts with BDP1, a subunit of transcription factor IIIB (TFIIIB). Since BDP1 is essential in Pol III transcription, ZBTB43 may also regulate these transcriptional pathways. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
FRVEFPDFSSTILQKLNQQRQQGQLCDISVVVQGHLFRAHKAVLAASSPYFCDQVLLKNSRRIVLPDVMN
PRVFENILLSCYTGRLVLPAPEIVSYLTAASFLQMWHVVDKCTELLEGNPT
>gnl|CDD|349537 cd18228, BTB_POZ_ZBTB44, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 44 (ZBTB44). ZBTB44, also called BTB/POZ domain-containing protein 15 (BTBD15) or zinc finger protein 851 (ZNF851), may be involved in transcriptional regulation. Single-nucleotide polymorphisms of ZBTB44 showed a suggestive association with disease progression of Crohn's disease. ZBTB44 has also preferentially been recognized by sera of patients with peripheral T-cell lymphoma (PTCL). It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
SHSQELLGKLNSLRNEGHFCDVTIRVQDKIFRAHKVVLAACSDFFRSKLVGQASPRLVLVSPAGKCVLDL
HHVTVTGFAPLLEYAYTSTLSINTENIIDVLAAASYMQMFNVANTCSEFMKSSILW
>gnl|CDD|349538 cd18229, BTB_POZ_ZBTB45, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 45 (ZBTB45). ZBTB45, also called zinc finger protein 499 (ZNF499), may act as a transcriptional regulator that is essential for proper glial differentiation of neural and oligodendrocyte progenitor cells. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
FSKSLLETLNAQRLGGHFCDVTVRIHDASLRAHRCVLAAGSPFFHDKLLLGHSEIEVPPVVPAQTVRQLV
EFMYSGSLVVAQSEALQILTAASILQIKTVIDECTQIISQSR
>gnl|CDD|349539 cd18230, BTB_POZ_ZBTB46, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 46 (ZBTB46). ZBTB46 is also called BTB-ZF protein expressed in effector lymphocytes (BZEL), BTB/POZ domain-containing protein 4 (BTBD4), or zinc finger protein 340 (ZNF340). It is a conventional dendritic cell (cDC) lineage specific transcription factor that acts as a negative regulator required to prevent activation of classical dendritic cells in the steady state. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
ITSHYRHLLRELNEQRQHGILCDVCIIVEGKIFKAHKNVLLGSSRYFKTLYCQVQKTSDQATVTHLDIVT
AQGFKAIIDFMYSAHLALTSKNVIEVMSAASYLQMTDIVQACHNFIKAALDISIK
>gnl|CDD|349540 cd18231, BTB_POZ_ZBTB47_ZNF651, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 47 (ZBTB47). ZBTB47, also called zinc finger protein 651 (ZNF651), is a paralog of ZNF652, a novel zinc-finger transcriptional repressor. It interacts with CBFA2T3 via its carboxy-terminal proline-rich region. CBFA2T3-ZNF651 functions as a transcriptional co-repressor complex. ZBTB47 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
MDRLNEQRLFQPDLCDVDIVLVRQRSTFPAHKGVLAAYSQFFHSLFTQNKQLQRVELSLEALTSQGLQQI
LNFIYTSKLLVNSCNVQDVLNAAAVLQMNDIAASCQELIDSRSLS
>gnl|CDD|349541 cd18232, BTB_POZ_ZBTB48_TZAP_KR3, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in telomere zinc finger-associated protein (TZAP). TZAP is also called Krueppel-related zinc finger protein 3 (KR3), zinc finger and BTB domain-containing protein 48 (ZBTB48), or zinc finger protein 855 (ZNF855). It is a vertebrate telomere-binding protein involved in telomere length control. It directly binds the telomeric double-stranded 5'-TTAGGG-3' repeat. TZAP also acts as a transcription regulator that binds to promoter regions. It is a transcriptional activator of alternate reading frame (ARF) gene. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
HSVKVLQALNKQREEGQYCDATLDVGGRVFKAHWSVLACCSHFFQSLYGDGTSGSVVLPESFAEVFGLLL
DFFYTGELALTRENRDRVLLAAKELRVPEAVELCQRFQ
>gnl|CDD|349542 cd18233, BTB_POZ_ZBTB49, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 49 (ZBTB49). ZBTB49, also called zinc finger protein 509 (ZNF509), is a transcription factor that inhibits cell proliferation by activating either CDKN1A/p21 transcription or RB1 transcription. There are four ZNF509 isoforms generated by alternative splicing. Short ZNF509 (ZNF509S1, -S2 and -S3) isoforms contain one or two out of the seven zinc-fingers contained in long ZNF509 (ZNF509L). ZBTB49 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
HSCHLLQQLHEQRIQGLLCDCMLVVKGVCFKAHKNVLAAFSQYFRSLFQNSSSQKNDVFHLDIKNVGGIG
QILDFMYTSHLDLNQDNVQVMLDIAQCLQVQNVLNMCYTFLK
>gnl|CDD|349543 cd18234, BTB_POZ_KLHL1-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins KLHL1, KLHL4 and KLHL5. This family contains the Kelch-like proteins: KLHL1, KLHL4 and KLHL5, all of which share high identity and similarity with the Drosophila kelch protein, a component of ring canals. KLHL1 is a neuronal actin-binding protein that modulates voltage-gated CaV2.1 (P/Q-type) and CaV3.2 (alpha1H T-type) calcium channels. Family members contain a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
LCDVILIAGDRRIPAHRLVLSAVSDYFAAMFTNDVREATEEEIKLKDVDPDALWTLVQYCYTGRLELKED
NVESLLATACLLQLSEVVEACCGFLMKQLHPSNCL
>gnl|CDD|349544 cd18235, BTB_POZ_KLHL2-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins, KLHL2 and KLHL3. The family includes Kelch-like proteins, KLHL2 and KLHL3. KLHL2 is a novel actin-binding protein predominantly expressed in brain. It plays a role in the reorganization of the actin cytoskeleton, and promotes growth of cell projections in oligodendrocyte precursors. KLHL2 and KLHL3 each functions as a component of an E3 ubiquitin ligase complex that mediates the ubiquitination of target proteins. They contain a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
NPQHTQKAFDVMNELRKQNLLCDVILVADGVEIPAHRVVLASCSPYFHAMFTGDLSESRANRVTLQDVDG
KALLLLIDYVYTAEIQVTEENVQVLLPAANLLQLTDVRDACCDFLQSQLHP
>gnl|CDD|349545 cd18236, BTB_POZ_KLHL6, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 6 (KLHL6). KLHL6 is a BTB-kelch protein with a lymphoid tissue-restricted expression pattern. It is involved in B-lymphocyte antigen receptor signaling and germinal center formation. It belongs to the KLHL gene family, which is composed of an N-terminal BTB-POZ domain and four to six Kelch motifs in tandem. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
KFDDTGLSLVLQNGLENLRLENSLTDVILCVDSQEFSCHRVVLAAASNYFRAMFCNDLKEKYEEKIIIKG
VDAETMQILLDYTYTSKVLITKQNVQRVLEAASLFQFLRMVDACASFLTEALHPENCVG
>gnl|CDD|349546 cd18237, BTB_POZ_KLHL7, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 7 (KLHL7). KLHL7 is a component of a Cul3-based E3 ubiquitin ligase complex and is involved in the ubiquitination of target proteins for proteasome-mediated degradation. Mutations in KLHL7 causes autosomal-dominant retinitis pigmentosa. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
EAKLLADFMGVMNNMRKQKTLCDVILIVEGREIKAHRVVLAAASHFFHLMFTSNMTESKSSEVELKDAEP
DIIELLVEFAYTARISVNSNNVQSLLDAANQYQIEPVKKMCVDFLKEQLDASNCLG
>gnl|CDD|349547 cd18238, BTB_POZ_KLHL8, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 8 (KLHL8). KLHL8 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for the ubiquitination and degradation of rapsyn, a postsynaptic protein required for clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
DSFKVLHQFYENGELCDVTLKVGEKSIHCHRLVLACVSPYFRAMFTSEMAESKQDSITIKDIDEEAVELL
VDFAYTGKLTLTVDNVQSLLYAASLLQVEEVAKACCEFMKDHLHPSNCLG
>gnl|CDD|349548 cd18239, BTB_POZ_KLHL9_13, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins KLHL9 and KLHL13. KLHL9 and KLHL13 (also called BTB and kelch domain-containing protein 2, or BKLHD2) are substrate-specific adaptors of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates the ubiquitination of AURKB and controls the dynamic behavior of AURKB on mitotic chromosomes, thereby coordinating faithful mitotic progression and completion of cytokinesis. They contain a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
FTSNTHSSVVLQGFDQLRGEGLLCDVTLVPGDGDETFPVHRAMMASASDYFKAMFTGGMKEQELMCIKLH
GVSKIGLKNIIDFIYTAKLSLNMDNLQDTLEAASFLQILPVLDFCKVLLISGVTLENC
>gnl|CDD|349549 cd18240, BTB_POZ_KLHL10, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 10 (KLHL10). KLHL10 is a substrate-specific adaptor of a CUL3-based E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins specifically in the testis during spermatogenesis. Haploinsufficiency of Klhl10 causes infertility in male mice. KLHL10 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
SAMACNVFNELRLEGKLCDVVIRVNGVEFPAHRNILCACSPYFRALFTNGWNETEKKVYKIPGVSPEMME
LIIEYAYTRTVPITAENVEELLPAADQFNIMGIVKACCDFLEDQLCPENC
>gnl|CDD|349550 cd18241, BTB_POZ_KLHL11, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 11 (KLHL11). KLHL11 is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
FECSSHCSELSWRQNEQRKQGLFCDITLAFGGAGGREFRAHRSVLAAATEYFTPLLSGQFSESRSGRVEM
RKWSSEPGPDPDTVEAVIQYMYTGRIRVSTGNVHEVLELADRFLLIRLKEFCGEFLKKKLNLSNC
>gnl|CDD|349551 cd18242, BTB_POZ_KLHL12_C3IP1_DKIR, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 12 (KLHL12). KLHL12, also called CUL3-interacting protein 1 (C3IP1) or DKIR homolog, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a negative regulator of the Wnt signaling pathway and ER-Golgi transport. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
TNSHAKSILNTMNSLRKSNTLCDVTLRVEGKEFPAHRIVLAACSDYFCAMFTSEMSEKGKSEVELQGLTA
STMEILLDFVYTETVHVTVENVQELLPAACLLQLKGVKQACCEFLESQLDPSNC
>gnl|CDD|349552 cd18243, BTB_POZ_KLHL14_printor, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 14 (KLHL14). KLHL14 is also called protein interactor of Torsin-1A (TOR1A), protein interactor of torsinA, or Printor. It is a novel torsinA-interacting protein that preferentially interacts with ATP-free form of TOR1A and is implicated in dystonia pathogenesis. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
MSRSGDRTSTFDPSHSDNLLHGLNLLWRKQLFCDVTLTAQGQQFHCHKAVLASCSQYFRSLFSINNLVLQ
GCSSIGLRLVLEYLYTANVTLSLDTVEEVLSVSKILHIPQVTKLCVQFLNDQISVQNYKQ
>gnl|CDD|349553 cd18244, BTB_POZ_KLHL15, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 15 (KLHL15). KLHL15 is a substrate-specific adaptor for the Cullin3 E3 ubiquitin-protein ligase complex that targets the serine/threonine-protein phosphatase 2A (PP2A) subunit PPP2R5B for ubiquitination and subsequent proteasomal degradation, thus promoting exchange with other regulatory subunits. It also plays a key role in DNA damage response, favoring DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR), by targeting the DNA-end resection factor RBBP8/CtIP for ubiquitination and subsequent proteasomal degradation. KLHL15 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
MAGDVEVYNSSIHDTSVSAGFRALYEEGLLLDVTLVIEDHQFQAHKALLATQSDYFRIMFTADMRERDQD
KIHLKGLTATGFSHVLQFMYYGTIELSMLTVHEILQAAMYVQLTEVVKFCCSFLLAKICLDNCAEIM
>gnl|CDD|349554 cd18245, BTB_POZ_KLHL16_gigaxonin, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in gigaxonin. Gigaxonin, also called Kelch-like protein 16 (KLHL16), may be a cytoskeletal component that directly or indirectly plays an important role in neurofilament architecture. It may also act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, including tubulin folding cofactor B (TBCB), microtubule-associated protein MAP1B, and glial fibrillary acidic protein (GFAP). Gigaxonin is mutated in giant axonal neuropathy. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
LLRALNSFREEPHLCDATLVVGGEEIPVQKNVLAAASPYFRAKLNYNPPKDDGSTYKIELEGISVEVMEE
ILDYIYTGQIKLSEDNIQDIVQAADLLLMTDLKDLCCEFLE
>gnl|CDD|349555 cd18246, BTB_POZ_KLHL17_actinfilin, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 17 (KLHL17). KLHL17, also called actinfilin, is a substrate-recognition component of some cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes. It acts as a Cullin 3 (Cul3) substrate adaptor that links GLUR6 to the E3 ubiquitin-ligase complex, and mediates the ubiquitination and subsequent degradation of GLUR6. It may play a role in actin-based neuronal function. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
MEGGVQLLNRDGHSISHNSKRHYHDAFVSMNRMRQRGLLCDIVLHVGTKEIKAHKVVLASCSPYFHAMFT
NEMSESRQTHVTLHDIDPQALEQLVQYAYTAEIVVGEGNVQTLLPAASLLQLNGVRDACCKFLLSQLDP
>gnl|CDD|349556 cd18247, BTB_POZ_KLHL18, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 18 (KLHL18). KLHL18 acts as a substrate-specific adaptor for a Cullin3 E3 ubiquitin-protein ligase complex that regulates mitotic entry and ubiquitylates Aurora-A. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
DLPSSGFPVMEEIRRQGKLCDVTLKVGDQKFSAHRIVLAATIPYFHAMFTHDMVESKQDEITMQGIEPSA
LEALINFAYSGRIAIDTSNVQSLLVGASFLQLQSVKDACCEFLKER
>gnl|CDD|349557 cd18248, BTB_POZ_KLHL19_KEAP1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like ECH-associated protein 1 (KEAP1). KEAP1, also called cytosolic inhibitor of Nrf2 (INrf2) or Kelch-like protein 19 (KLHL19), is a redox-regulated substrate adaptor protein for a Cullin3-dependent ubiquitin ligase complex that targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
LEDHTKEAFQIMNELRLSQQLCDVTLKVKYQDPKEEFMAHKVVLASSSPYFKAMFTSGLRECGMEVVPIE
GVHPCVMSRLIEFAYTASISVGEKCVLHVLPGAVMYQMDSVVKACCDFLEQQLD
>gnl|CDD|349558 cd18249, BTB_POZ_KLHL20_KLEIP, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 20 (KLHL20). KLHL20, also called Kelch-like ECT2-interacting protein (KLEIP) or Kelch-like protein X, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. KLHL20 plays a role in actin assembly at cell-cell contact sites of Madin-Darby canine kidney cells. It also controls endothelial migration and sprouting angiogenesis. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
YTSDKHPRQTLEAINLLRKHRELCDVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVTIRDI
DERAMELLIDFAYTSQITVEEGNVQTLLPAACLLQLAEIQEVCCEFLKRQLDPSNCLG
>gnl|CDD|349559 cd18250, BTB_POZ_KLHL21, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 21 (KLHL21). KLHL21 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for efficient chromosome alignment and cytokinesis. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of aurora B. KLHL21 also targets IkappaB kinase-beta to regulate nuclear factor kappa-light chain enhancer of activated B cells (NF-kappaB) signaling negatively. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
DPAHALHLLRGLSELRAERKFFDVTLCAGGREFPCHRTVLAAASSYFRAMFAGELRESRADRVVLHGVSA
EILGLLLDFSYTGRVTVTQDNVEALLRAADLFQFPSVKEACCAYLQQRLDVSNC
>gnl|CDD|349560 cd18251, BTB_POZ_KLHL22, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 22 (KLHL22). KLHL22 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of polo-like kinase 1 (PLK1) at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates mono-ubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
YRSVAHSQALLDGLVALRDSGILFDVVLVVEGKPIEAHRILLAASCDYFRGMFAGGLREMQQTEVLIHGV
SYNAMCKILDFIYTSELELSLDNVQETLTAACQLQIPEVIGFCCDFLMSWVDNEN
>gnl|CDD|349561 cd18252, BTB_POZ_KLHL23, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 23 (KLHL23). KLHL23 overexpression is associated with increased cell proliferation and invasion in gastric cancer. Downregulation of KLHL23 is associated with invasion, metastasis, and poor prognosis of hepatocellular carcinoma and pancreatic cancer. KLHL23 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
DSSHPADFLDAFRTFYLDGLFTDITLQCASGQIFHCHKAALAACSSYFKVMFTADMKEKSNNVIKLSGID
HDILEALVNYVYTSQICITERNVQSLLEAADLLQFISVKKACEQFLVRHLDIDNCLG
>gnl|CDD|349562 cd18253, BTB_POZ_KLHL24_KRIP6, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 24 (KLHL24). KLHL24, also called kainate receptor-interacting protein for GluR6 (KRIP6) or protein DRE1, is necessary to maintain the balance between intermediate filament stability and degradation, a process that is essential for skin integrity. KLHL24 is a component of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that mediates ubiquitination of KRT14 and controls its levels during keratinocyte differentiation. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
HSESILQVFNEFRDSRLFTDVIICVEGREFPCHRAILSACSSYFRAMFCNDHRESREMLVEINGILAEAM
DCFLQYVYTGKVKITTENVQYLFETSSLFQISPLRDACAKFLEEQLDPCNC
>gnl|CDD|349563 cd18254, BTB_POZ_KLHL25, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 25 (KLHL25). KLHL25, also called ectoderm-neural cortex protein 2 (ENC-2), is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that is required for translational homeostasis. The BCR(KLHL25) ubiquitin ligase complex acts by mediating ubiquitination of hypophosphorylated EIF4EBP1 (4E-BP1). Cullin3-KLHL25 ubiquitin ligase also targets ATP-citrate lyase (ACLY), a key enzyme for lipid synthesis, for degradation to inhibit lipid synthesis and tumor progression. KLHL25 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
HKPSHPDCVLTHLNTLRKQCMFTDVTLWAGNRSFPCHRAVLAACSRYFEAMFSNGLRESLDSTVNFHDSL
HPEVLELLLDFAYSSRIIINEENAESLLEAGDMLQFHDVRDAAAEFLEKNLYPSNCLG
>gnl|CDD|349564 cd18255, BTB_POZ_KLHL26, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 26 (KLHL26). KLHL26 is encoded by the klhl26 gene, which is regulated by p53 via fuzzy tandem repeats. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
HSVTLLQGLNALRAKGQLLDVTLIADGQRFQAHKVVLASCSDYFRAMFTGGMRESSQDEIELKGVSAKGL
KHILDFAYTSELTLDLDCIQDVLGAAVHLQMLPVVELCEEFLKSAMSVENC
>gnl|CDD|349565 cd18256, BTB_POZ_KLHL27_IPP, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in intracisternal A particle-promoted polypeptide (IPP). IPP, also called Kelch-like protein 27 (KLHL27) or actin-binding protein IPP, is an actin-binding protein that may play a role in organizing the actin cytoskeleton. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
DKHASLILAQLNKLRGQHEFCDVQLQVGMELFSVHRLVLAASSPYFAALFAGGMSESSKDVVQIHGVEPD
IFHILLDFIYTGVVEVTVSNVQELLVAADMLQLTEVVEICCEFLKGQLHPSNCIG
>gnl|CDD|349566 cd18257, BTB_POZ_KLHL28_BTBD5, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 28 (KLHL28). KLHL28, also called BTB/POZ domain-containing protein 5 (BTBD5), contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
HSEQLLQGLNLLRQHHELCDVVLRVGDVKIHAHKVVLASCSPYFKAMFTGNLSEKENSEVEFQCIDETAL
QAIVEYAYTGTVFISQATVESLLPAANLLQIKLVLKECCDFLESQLDP
>gnl|CDD|349567 cd18258, BTB_POZ_KLHL29_KBTBD9, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 29 (KLHL29). KLHL29 is also called Kelch repeat and BTB domain-containing protein 9 (KBTBD9). A novel fusion transcript NR5A2-KLHL29FT, resulting from transchromosomal insertion, may influence the origin or progression of colon cancer. KLHL29 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
PKEMLKELNQQRRAKEFTDLKIIVEGKEFEVHQNVLASCSLYFKDLIKRSSRDSGGGEKLELTMSNINAD
VLELLLEFVYTGSLIIDSANAKTLLEAANKFQFHTFCKVCVSFLEKQLTASNCLG
>gnl|CDD|349568 cd18259, BTB_POZ_KLHL30, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 30 (KLHL30). KLHL30 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
MVRNIDDLDFCLPSHPQSILDGLQTLRSNPKLSDVTLLVGGREFPCHRSVLALCSHYFNAMFTGDFVESI
SARVEIKDVDPAVMESLIDFAYTGKLTINQGNVEALIRTSNRLQFPTVRKVCSRYLQQQIDATNCLG
>gnl|CDD|349569 cd18260, BTB_POZ_KLHL31_KBTBD1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 31 (KLHL31). KLHL31 is also called BTB and kelch domain-containing protein 6 (BKLHD6), Kelch repeat and BTB domain-containing protein 1 (KBTBD1), or Kelch-like protein KLHL. It is a transcriptional repressor in the MAPK/JNK signaling pathway to regulate cellular functions. Overexpression inhibits the transcriptional activities of both the TPA-response element (TRE) and serum response element (SRE). It is also a novel modulator of canonical Wnt signaling, which is important for vertebrate myogenesis. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
YGANLLEGLNRMRQERFLCDLTIATKTKSFDVHKVVMASCSEYFRNILKKDPSLQRVELNDISPLGLATV
ITYAYTGKLTLSLYTIGSTISAASYLQIHALVKMCCDFLMQEMNVENCMY
>gnl|CDD|349570 cd18261, BTB_POZ_KLHL32, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 32 (KLHL32). KLHL32, also called BTB and kelch domain-containing protein 5 (BKLHD5), contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. Deletion of KLHL32 may be ssociated with Tourette syndrome and obsessive-compulsive disorder. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
TGQRLCQSKSHKDAVLAALNQQRNDGILCDITLVAEEQKFHAHKAVLAACSDYFRAMFSLCMVESEADEV
NLHGVTSLGLKQALDFAYTGQILLEPGVIQDVLAAGSHLQLLELLSLCSHYLIQELNSFNYLD
>gnl|CDD|349571 cd18262, BTB1_POZ_KLHL33, first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 33 (KLHL33). KLHL33 contains BTB domains and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. KLHL33 gene expression in normal and tumor tissue suggest a significant association with prostate cancer risk. KLHL33 contains two BTB domains. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
HPSQFFGEAQRLREQRLLLDETVSVGGRSYGVHSVILAAVSSLFRERLLGSNGPLPPLSLEVTPVGWEAV
LTFAYTGVLGRNPATVGDILVAAEALGAPRV
>gnl|CDD|349572 cd18263, BTB2_POZ_KLHL33, second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 33 (KLHL33). KLHL33 contains BTB domains and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. KLHL33 gene expression in normal and tumor tissue suggest a significant association with prostate cancer risk. KLHL33 contains two BTB domains. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
LQSIEGLWEKGVGCDVQLEADGSIFRVHRVILAAGSDYFRAMFTSGMKESTQSVVQLPTIPAKDLRLLIS
FAYSGILHLSWENLFEATCTALQLQISGALALCLDFLQREISPARCLD
>gnl|CDD|349573 cd18264, BTB_POZ_KLHL34, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 34 (KLHL34). KLHL34 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The methylation status of KLHL34 cg14232291 appears to be predictive of pathologic response to preoperative chemoradiation therapy in rectal cancer patients. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
MSYFLAYSKSHGEAVLSQYQSLRAEGFLCDVVLEAEGNEFPAHRSLLACSSDYFRALFKDYTQESKARVI
HLPVVSAAGLQRVLDFIYTSWLSLSLDTLEDTLEAASYLQVTEAIGLCSQYLINNLAPENCCFSAN
>gnl|CDD|349574 cd18265, BTB_POZ_KLHL35, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 35 (KLHL35). KLHL35 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. Significant differences in DNA methylation of the KLHL35 gene in abdominal aortic aneurysm (AAA) patients compared to non-AAA controls suggest a potential role in AAA pathology. Hypermethylation of the KLHL35 gene has also been associated with the development of hepatocellular carcinoma. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
CSGPCHAERILQVLNAYRRSGTFTDVVLLVDGKDFPCHRATLSANSAYFRAMFGGHLKESRQAVVEIQKV
SAAAMEVLLDYMYGGGLRIQEDNVESVLEASDLLQVSKLREACVRFLEGQLHPCNCLG
>gnl|CDD|349575 cd18266, BTB_POZ_KLHL36, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 36 (KLHL36). KLHL36 may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
KVYRWADHSNLVLQGLNEQRQRGLFCDVVLVADEQRVPAHRNLLAVCSDYFNSMFTIGMREAHQKEVELV
GASYIGLKAVIDFLYSSELPLDGGNIDYVLETAHLLQIWKVVDFCCEYLENEVSEENYLYLQELA
>gnl|CDD|349576 cd18267, BTB_POZ_KLHL37_ENC1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ectoderm-neural cortex protein 1 (ENC-1). ENC-1 is also called Kelch-like protein 37 (KLHL37), nuclear matrix protein NRP/B, or p53-induced gene 10 protein. It is an actin-binding nuclear matrix protein that associates with p110(RB), and is involved in the regulation of neuronal process formation and in differentiation of neural crest cells. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
HENRKSRASSGSMNIYLFHKSSYADSVLTHLNLLRQQRLFTDVLLHAGNRSFPCHRAVLAACSRYFEAMF
SGGLKESQDSEVNFHDSIHPEVLELLLDYAYSSRVIINEENAESLLEAGDMLEFQDIRDACAEFLEKNLH
PTNCLGM
>gnl|CDD|349577 cd18268, BTB_POZ_KLHL38, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 38 (KLHL38). KLHL38 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The KLHL38 gene is significantly up-regulated during diapause, a temporary arrest of development during early ontogeny. It may also function in preadipocyte differentiation in the chicken. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
FKDQDLSSELLRQLNSLRQERILTDVILCTGDKEIPCHRNVLASSSPYFRAMFCNNFRESSQAKVDLKGI
DSDVLDQIVDYVYTGEILITRDNVLPLMEAASMLQYPKLFEACSLYLQDQLTPENCLSM
>gnl|CDD|349578 cd18269, BTB_POZ_KLHL40-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins, KLHL40 and KLHL41. This family includes Kelch-like proteins, KLHL40 and KLHL41. KLHL40 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development. KLHL41 is a novel kelch related protein that is involved in pseudopod elongation in transformed cells. They both contain a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
EQKEELRLYQQTLLQDGLKDLLDENKFVDCVLKIGDKEFPCHRLVLAACSPYFRAMFLSDLEESKKKEVV
LEDVDPDVMGMILKYLYTSEIDLNDQNVQDIFALASRFQIPSIFTVCVSYLQKRLSLSNCLAI
>gnl|CDD|349579 cd18270, BTB_POZ_KBTBD2_BKLHD1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 2 (KBTBD2). KBTBD2, also called BTB and kelch domain-containing protein 1 (BKLHD1), plays an essential role in the regulation of insulin-signaling pathway. It is a BTB-Kelch family substrate recognition subunit of the Cullin-3-based E3 ubiquitin ligase, which targets p85alpha, the regulatory subunit of the phosphoinositol-3-kinase (PI3K) heterodimer, causing p85alpha ubiquitination and proteasome-mediated degradation. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
DERQINTEYAVSLLEQLKFFYEQQLLTDIVLIVEGTEFPCHKMVLATCSSYFRAMFMSGLSESKQTHVHL
RNVDAATLQIIITYAYTGNLAINDSTVEQLYETACFLQVEDVLQRCREYLIKKINAENCVRLL
>gnl|CDD|349580 cd18271, BTB_POZ_KBTBD3_BKLHD3, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 3 (KBTBD3). KBTBD3, also called BTB and kelch domain-containing protein 3 (BKLHD3), contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
SLVAECHGQQILSVLQNFREQNAFFDFNIIVKDETIPCHRCVLAACSDFFRAMFEVNMKERDDGSVTISN
LSPKAVKAFLDYAYTGKAEITDDNVEMFFQMSSFLQVSLLSKACSDFLIKSIDLTNCLQL
>gnl|CDD|349581 cd18272, BTB_POZ_KBTBD4, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 4 (KBTBD4). KBTBD4, also called BTB and kelch domain-containing protein 4 (BKLHD4), is a BTB-BACK-Kelch domain protein belonging to a large family of cullin-RING ubiquitin ligase adaptors that facilitate the ubiquitination of target substrates. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
ENYFVSYTFTDRSHSSRVAQSIMDLCLEDGLFADVTISVEGKEFQLHRLVLSAQSCFFRSMFTSNLKEAR
NRVIELKDVSESVFQLLVDYIYHGTVKLRVEELQETYEVADMYQLTALFEECSRFLARTVQVRNCLQVMW
>gnl|CDD|349582 cd18273, BTB_POZ_KBTBD6_7, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing proteins KBTBD6 and KBTBD7. KBTBD6 and KBTBD7 are substrate adaptors of a cullin-3 RING ubiquitin ligase complex that mediates ubiquitylation and proteasomal degradation of T-lymphoma and metastasis gene 1 (TIAM1), a RAC1-specific guanine exchange factor (GEF), by cooperating with gamma-aminobutyric acid receptor-associated proteins (GABARAP). KBTBD7 may also act as a new transcriptional activator in mitogen-activated protein kinase (MAPK) signaling. They both contain a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
PEELEDAAHARALLAQLKSFYDARLLTDVTIEVNGPGSGPGSGRLFPCNRNVLAAASPYFKSMFTGGLYE
SKQETVTIHDVDSESMALIIDYCYTGRVTLSEANVQRLYAAANMLQLEYVREACASFLARRLDLSNCVGI
LK
>gnl|CDD|349583 cd18274, BTB_POZ_KBTBD8, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 8 (KBTBD8). KBTBD8, also called T-cell activation kelch repeat protein (TA-KRP), is a BTB-kelch family protein that is located in the Golgi apparatus and translocates to the spindle apparatus during mitosis. It acts as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of neural crest specification. The BCR(KBTBD8) complex monoubiquitylates NOLC1 and its paralog TCOF1, the mutation of which underlies the neurocristopathy Treacher Collins syndrome. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
MDPLHACSILQQLKAMYDEGQLTDIVVEVDHGKTFSCHRNVLAAISPYFRSMFTSGLTESTQKEVRIVGV
EAESMHLVLDYAYTSRVTLTEANVQALFTAASIFQIPSLQDQCAQFMISRLDPQNSIGV
>gnl|CDD|349584 cd18275, BTB_POZ_KBTBD11, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 11 (KBTBD11). KBTBD11 is also called chronic myelogenous leukemia-associated protein (CMLAP) or Kelch domain-containing protein 7B, or KLHDC7C. It is a BTB-Kelch family protein whose function remains unclear. A novel polymorphism rs11777210 in KBTBD11 is significantly associated with colorectal cancer risk. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
PLGEPDLVIEVSGQRIRAHKSVLAAKSDYFRARLSRDILKVKGLSYATLRLLVDYVYSGRMAVSKDNVVE
VVAGARFLQMPCAAQCAVDAVRAQLCLGNCYEVL
>gnl|CDD|349585 cd18276, BTB_POZ_KBTBD12, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 12 (KBTBD12). KBTBD12, also called Kelch domain-containing protein 6 (KLHDC6), contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
RQKHSLTLLDQLNRMKELAELTDVVLVAEGEKFPCHRLVLAAFSPYFKAMFTCGLMECSQREVVLHDITA
ESVSIILNYMYSSDLHLTNSNVQGVATAAFFLQMEDIFSVCQKYMMDHMDASNCLGI
>gnl|CDD|349586 cd18277, BTB_POZ_BACH1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB and CNC homolog 1 (BACH1). BACH1, also called BTB-basic leucine zipper transcription factor 1, belongs to the cap 'n' collar (CNC) and basic leucine zipper (bZIP) factor family. It can act as repressor or activator. BACH1 is a heme-responsive transcriptional repressor of heme oxygenase (HO)-1. It represses genes involved in heme metabolism and oxidative stress response. It is also a negative regulator of nuclear factor erythroid 2-related factor 2 (Nrf2) that controls antioxidant response elements (ARE)-dependent gene expressions. BACH1 binds to NF-E2 binding sites in vitro, and plays important roles in coordinating transcription activation and repression by MafK. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
SVFAYESSVHSTNVLLSLNDQRKKDVLCDVTILVEGQRFRAHRSVLAACSSYFHSRIVGQADAELNITLP
EEVTVKGFEPLIQFAYTAKLILSKDNVDEVCKCVEFLSVHNIEESCFQFL
>gnl|CDD|349587 cd18278, BTB_POZ_BACH2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB and CNC homolog 2 (BACH2). BACH2, also called BTB-basic leucine zipper transcription factor 2, belongs to the cap 'n' collar (CNC) and basic leucine zipper (bZIP) factor family. BACH2 is a lymphoid-specific transcription factor with a prominent role in B-cell development. It is transcriptionally regulated by the BCR/ABL oncogene. It represses the anti-apoptotic factor heme oxygenase-1 (HO-1). It is also a potent general repressor of effector differentiation in naive T cells. Moreover, BACH2 is required for pulmonary surfactant homeostasis and alveolar macrophage function. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
KTESPMYVYESTVHCTNILLCLNDQRKQDILCDVTLIVEGKEFRAHRAVLAACSEYFLQALVGQTENDLV
VSLPEEVTARGFGPLLQFAYTAKLLLSRENIQEVIRCAEFLRMHNLEDSCFRFL
>gnl|CDD|349588 cd18279, BTB_POZ_SPOP-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein (SPOP) and similar proteins. This family includes speckle-type POZ protein (SPOP), speckle-type POZ protein-like (SPOPL), TD and POZ domain-containing proteins (TDPOZ), Drosophila melanogaster protein roadkill and similar proteins. Both, SPOP and SPOPL, serve as adaptors of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that mediate the ubiquitination and proteasomal degradation of target proteins. TDPOZ is a family of bipartite animal and plant proteins that contain a tumor necrosis factor receptor-associated factor (TRAF) domain (TD) and a POZ/BTB domains. TDPOZ proteins may be nuclear scaffold proteins probably involved in transcription regulation in early development and other cellular processes. Drosophila melanogaster protein roadkill, also called Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
PECRLAEDLGNLWENSRFTDCCLCVGGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVDPEVF
KEMMRFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEDALCSNLSVEN
>gnl|CDD|349589 cd18280, BTB_POZ_BPM_plant, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in plant BTB/POZ-MATH (BPM) protein family. The BPM protein family includes Arabidopsis thaliana BTB/POZ and MATH domain-containing proteins, AtBPM1-6, and similar proteins from other plants. BPM protein, also called protein BTB-POZ and MATH domain, may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
LGQHFGALLESEEGADVTFNVDGEKFRAHKLVLAARSPVFRSMLFGPMREENEGEIVIEDVEPPVFKALL
HFIYKDELPDDVEPAGSDSSSLDTTMAQHLLAAADRYALERLRLLCESRLC
>gnl|CDD|349590 cd18281, BTB_POZ_BTBD1_2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing proteins, BTBD1 and BTBD2. This family includes BTB/POZ domain-containing proteins BTBD1 and BTBD2, both of which are BTB-domain-containing Kelch-like proteins that interact with DNA topoisomerase 1 (Topo1), a key enzyme of cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
NWQASKTTVKERFAFLFNNETLSDVHFIVGKGDNEQRIPAHKFVLSIGSAVFDAMFNGGMATTSAEIELP
DVEPAAFLALLRFLYSDEVQIGPETVMTTLYTAKKYAVPALESACVEFLKKNLSSDN
>gnl|CDD|349591 cd18282, BTB_POZ_BTBD3_6, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing proteins, BTBD3 and BTBD6. This family includes BTB/POZ domain-containing proteins BTBD3 and BTBD6, both of which are BTB-domain-containing Kelch-like proteins. BTBD3 controls dendrite orientation toward active axons in mammalian neocortex. BTBD6 is required for proper embryogenesis and plays an essential evolutionary conserved role during neuronal development. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
MFNNELMADVHFIVGPPGGTQRIPAHKYVLATGSSVFYAMFYGGLAENKNEIEIPDVEPAAFLNLLRYLY
CDEIDLEPDTVLATLYAAKKYLVPHLARACVQFLETSL
>gnl|CDD|349592 cd18283, BTB1_POZ_BTBD7, first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 7 (BTBD7). BTBD7 is a crucial regulator that is essential for region-specific epithelial cell dynamics and branching morphogenesis. It has been implicated in various cancers. BTBD7 contains two BTB domains. This model corresponds to the first domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
YCTDVDLVFQGTCFPVHRAILSARCPFFRDLLSSSPGYGAEIPVDLPTAGIDVPMFSALLRYLYTGEFGS
EDSRSQNLDVLIQLSEEFGTPN
>gnl|CDD|349593 cd18284, BTB2_POZ_BTBD7, second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 7 (BTBD7). BTBD7 is a crucial regulator that is essential for region-specific epithelial cell dynamics and branching morphogenesis. It has been implicated in various cancers. BTBD7 contains two BTB domains. This model corresponds to the second domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
DYGDAVLVFASDKETVESSSGKVNEPDFELRCHKAILSARSPFFRNLLQRRIRTGEDRTLSTPTRIVLDE
SIIPRRYARVLLHAMYTDSVDLSLILRSSPSESSLSEVQAIVAGKGPETRLEEAMELYHIARFLEFDILA
QGCEDI
>gnl|CDD|349594 cd18285, BTB1_POZ_BTBD8, first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 8 (BTBD8). BTBD8 is a BTB-domain-containing Kelch-like protein that may play a role in developmental processes. It may also act as a protein-protein adaptor in a transcription complex and thus be involved in brain development. BTBD8 contains two BTB domains. This model corresponds to the first domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
HLSQDLLRLLREELHTDVTFYVGSTLFKAHKAILLARVPEFFSHIIGKLSSLEDQEPINIENLEASEFKT
FLRQVYTSDKNIKMLEEEILKGKVLDQKVDKEND
>gnl|CDD|349595 cd18286, BTB2_POZ_BTBD8, second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 8 (BTBD8). BTBD8 is a BTB-domain-containing Kelch-like protein that may play a role in developmental processes. It may also act as a protein-protein adaptor in a transcription complex and thus be involved in brain development. BTBD8 contains two BTB domains. This model corresponds to the second domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
CSRLGKDLLQLFLNGEDSDITIKVDGKTFKAHRCILCARSSYFAAMLSGSWAESNSSEITLTGVSHAAVS
FVLLFIYGGVLDLPDDVNLGELLSLADMYGLDGLKDVVAYTLRRDYCHFFH
>gnl|CDD|349596 cd18287, BTB_POZ_BTBD9, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 9 (BTBD9). BTBD9 is a risk factor for Restless Legs Syndrome (RLS) encoding a Cullin-3 substrate adaptor. The BTBD9 gene may be associated with antipsychotic-induced RLS in schizophrenia. Mutations in BTBD9 lead to reduced dopamine, increased locomotion and sleep fragmentation. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
GEIDHVHFLSEDIGALFLNEEYSDVTFVVEEKRFPAHRVILAARSEYFRALLYGGMRESQQSEIELKDTN
AEAFKALLKYIYTGRLTLTDLKEDVLLDVLGLAHQYGFEELEAAISDYL
>gnl|CDD|349597 cd18288, BTB_POZ_BTBD12_SLX4, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Structure-specific endonuclease subunit SLX4. SLX4, also called BTB/POZ domain-containing protein 12 (BTBD12), is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases and is required for DNA repair. Mutations of the SLX4 gene are found in Fanconi anemia. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
SLGKLAADFSAMVNNPHLSDVQFQTDSGEVLYAHSFVLYARCPLLIQMVHSEGFSVEEEGGVTTRRVLLG
DVSGEAARCFLQYLYTADTGLPPGLSPHVSELADRFGVSELVHLCE
>gnl|CDD|349598 cd18289, BTB_POZ_BTBD14A_NAC2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in nucleus accumbens-associated protein 2 (NAC-2). NAC-2, also called BTB/POZ domain-containing protein 14A (BTBD14A) or repressor with BTB domain and BEN domain (RBB), is a novel transcription repressor through its association with the NuRD complex. It recruits the NuRD complex to the promoter of MDM2, leading to the repression of MDM2 transcription and subsequent stability of p53/TP53. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
MSQMLHIEIPNFGNTVLGCLNEQRLMGLYCDVSIVVKGQAFKAHRAVLAASSLYFRDLFSGNSKSAFELP
ATVPPACFQQILSFCYTGKLTMAASEQLVVMYTAGFLQIQHIVERGTDLMFKVSSPHCDSQ
>gnl|CDD|349599 cd18290, BTB_POZ_BTBD14B_NAC1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in nucleus accumbens-associated protein 1 (NAC-1). NAC-1, also called BTB/POZ domain-containing protein 14B (BTBD14B), is a transcriptional repressor that contributes to tumor progression, tumor cell proliferation, and survival. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
QTLQMEIPNFGNSILECLNEQRLQGLYCDVSVVVKGHAFKAHRAVLAASSSYFRDLFNSSRSAVVELPAA
VQPQSFQQILSFCYTGRLSMNVGDQFLLMYTAGFLQIQEIMEKGTEFFLKVSS
>gnl|CDD|349600 cd18291, BTB_POZ_BTBD16, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 16 (BTBD16). BTBD16 is a BTB domain-containing protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
YYHSQKVARSACPDVVLECLGSFWELHSPYLCKSETLAELLKPVTISLNINDPLVTKEAFAVALGNLYNS
EVEVNVEDAVGVLAAAALLRFPTLFQKCVKVMISSISSSTVCKF
>gnl|CDD|349601 cd18292, BTB_POZ_BTBD17, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 17 (BTBD17). BTBD17, also called galectin-3-binding protein-like, is a BTB domain-containing protein. Its function remains unclear. It may be associated with hepatocellular carcinoma. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
SREFLQDIAQLYNNEELSDIVLRVGGKVFHAHRLILAKSSDVFRVMLSNDWWSESKQSEIELVEDPECAA
VFEKFLRYLYTGQISVNLETALPLLMLADKYNVTDLKQLCVDFM
>gnl|CDD|349602 cd18293, BTB_POZ_BTBD18, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 18 (BTBD18). BTBD18 acts as a specific controller for transcription activation through RNA polymerase II elongation at a subset of genomic PIWI-interacting RNA (piRNA) loci. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
TAFLQLHRQQNSGVFCDVLLQAEGESVPAHCCVLSACSPYLTERLSSEPPPAGQKVVLELQGLKAHTLLK
LVDFLYTSELEVSSEEAQDVLAAARRLQISELESLCLEGGKLVKAPPGRR
>gnl|CDD|349603 cd18294, BTB_POZ_BTBD19, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 19 (BTBD19). BTBD19 is a BTB domain-containing protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
FAADMKSLINNPEFSDVKFLVGPERQEIFAHKCILAARCEVFRAMFLTGPQKESTQSPLVLSDIEPEVFR
AVLEFIYTNCVTLSNHTVIEVLAAAVEYGLDELRKLCERFI
>gnl|CDD|349604 cd18295, BTB1_POZ_ABTB1_BPOZ1, first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 1 (ABTB1). ABTB1, also called elongation factor 1A-binding protein or bood POZ containing gene type 1 (BPOZ-1), is an anti-proliferative factor that may act as a mediator of the phosphatase and tensin homolog (PTEN) growth-suppressive signaling pathway. It may play a role in developmental processes. ABTB1 contains an ankyrin repeat and two BTB domains. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
MRRDYYDEFLRRLLEQGSYSDVTFNVHGESFPAHRCILSARSPYFAEMFETKWKDKREINLKHPLVNPDA
FRALLQYLYTGRLEIHVDDVEDCKRLAKQCRLEELIEELEAKCKKVREF
>gnl|CDD|349605 cd18296, BTB2_POZ_ABTB1_BPOZ1, second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 1 (ABTB1). ABTB1, also called elongation factor 1A-binding protein or bood POZ containing gene type 1 (BPOZ-1), is an anti-proliferative factor that may act as a mediator of the phosphatase and tensin homolog (PTEN) growth-suppressive signaling pathway. It may play a role in developmental processes. ABTB1 contains an ankyrin repeat and two BTB domains. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
RVDLDELPFPPEQELSFPDVCFQVEGHRFPCHKAFFCGRSDYFKALLRDHFAESEENNGSIPVVTLHDVS
PEVFAIVLYYIYTDDTDLPPENAYDVLYVADMYLLPGLKRLCGTVLAQSLD
>gnl|CDD|349606 cd18297, BTB_POZ_ABTB2-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) and similar proteins. This family includes ABTB2, BTBD11, plant ARM repeat protein interacting with ABF2 (ARIA), and similar proteins. ABTB2, also called bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation, and prevent translation. The BTBD11 gene has been recently identified as an all-trans retinoic acid (atRA)-responsive gene that lies downstream of atRA and its receptors in the regulation of neurite outgrowth and cell adhesion in neural as well as non-neural tissues. ARIA is an armadillo (ARM) repeat and BTB domain-containing protein that acts as a positive regulator of ABA response via the modulation of the transcriptional activity of ABF2. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
RIDPHYVNNPEMSDVTFLVEGRPFYAHKIVLVTASDRFKSMLSSGSTEAQTPVIEIPDIRYDIFQLMMQY
LYTGGVESLDVAQDDALELLRAASFFQLDGLKRHCEILLSQQIDLDN
>gnl|CDD|349607 cd18298, BTB_POZ_RCBTB1_2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in RCC1 and BTB domain-containing proteins, RCBTB1 and RCBTB2. The RCC1-related guanine nucleotide exchange factor (GEF) family includes RCC1 and BTB domain-containing proteins, RCBTB1 and RCBTB2, both of which are chromosome condensation regulator-like guanine nucleotide exchange factors. They contain an RCC1 repeat, a BTB domain, and a BACK domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
DSLRKAFNDPRTSDLKFRVDGKYIYVHKAILKIRCEYFRSMFQSHWNEDDKNVIEIDQYSYPVYYAFLRY
LYTDQVDLPPEDAIGLLDLANSYCEERLKKLCEDIIKQ
>gnl|CDD|349608 cd18299, BTB1_POZ_RhoBTB, first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing proteins (RhoBTB). RhoBTB proteins constitute a subfamily of atypical members within the Rho family of small guanosine triphosphatases (GTPases), which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. In vertebrates, the RhoBTB subfamily consists of 3 isoforms: RhoBTB1, RhoBTB2, and RhoBTB3. Orthologs are present in several other eukaryotes, such as Drosophila and Dictyostelium, but have been lost in plants and fungi. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
EDLRNLLHSPSCADVVFILQGGVRIFAHRIVLAAASSVFADLFLMMTVVTLDSDITPEAFRRVLEFLYTG
VLDENEDDLKELKDAAELLELFDLVMMCTNVLN
>gnl|CDD|349609 cd18300, BTB2_POZ_RhoBTB, second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing proteins (RhoBTB). RhoBTB proteins constitute a subfamily of atypical members within the Rho family of small guanosine triphosphatases (GTPases), which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, a tandem of 2 BTB domains, and a conserved C-terminal region. In humans, the RhoBTB subfamily consists of 3 isoforms: RhoBTB1, RhoBTB2, and RhoBTB3. Orthologs are present in several other eukaryotes, such as Drosophila and Dictyostelium, but have been lost in plants and fungi. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
KLFLNKGLFSDVTFIVEDGTIPAHKALLVARCDVMAAMFGGNFRESSAKEVELPGVSKETFLALLEYLYT
DQAPILEDGDCVGLIVLANRLCLPRLVALCEQYIVKEL
>gnl|CDD|349610 cd18301, BTB1_POZ_IBtk, first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in inhibitor of Bruton tyrosine kinase (IBtk). IBtk is an inhibitor or negative regulator of Bruton tyrosine kinase (Btk), which is required for B-cell differentiation and development. IBtk binds to the PH domain of Btk and down-regulates the Btk kinase activity. It contains two BTB domains. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
FQEDFKKLLDEADEGDNIHDVVFQVGGKTFPAHKFILASRSDYFRKLFLSSLLTSEDAVGCDVVHIEKVP
PEIFEQLLQFIYTDTCDLLTDGYKPKLQR
>gnl|CDD|349611 cd18302, BTB2_POZ_IBtk, second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in inhibitor of Bruton tyrosine kinase (IBtk). IBtk is an inhibitor or negative regulator of Bruton tyrosine kinase (Btk), which is required for B-cell differentiation and development. IBtk binds to the PH domain of Btk and down-regulates the Btk kinase activity. It contains two BTB domains. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
KHSDLYDVTIVSEDGKEFPCHKCVLVARLEYFHSMLSSSWIEASSCSALTMPIPSDILEIILDYLYTDEA
SAVKESQNVEFLCNVLVIADQLLITRLKEICEVALVELLSLKN
>gnl|CDD|349612 cd18303, BTB_POZ_Rank-5, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in rabankyrin-5 (Rank-5). Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1) or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms. It contains an N-terminal BTB domain, followed by a BACK domain, several ankyrin (ANK) repeats and a C-terminal FYVE domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
FISRLLKTVASLFDKELYSDITIKLADKSIPAHKFVLAARSEKWSNENLASTNELDLSDISYEVVLALLR
WLYTDELDLTLDDEFLLELMKAAKRFQLTDLVERCERALMSSVNVDNCIR
>gnl|CDD|349613 cd18304, BTB_POZ_M2BP, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Mac-2-binding protein (MAC2BP/M2BP). M2BP is also called galectin-3-binding protein, basement membrane autoantigen p105, lectin galactoside-binding soluble 3-binding protein (LGALS3BP), or tumor-associated antigen 90K. It promotes integrin-mediated cell adhesion and may stimulate host defense against viruses and tumor cells. It contains a scavenger receptor cysteine-rich domain, followed by BTB and BACK domains. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
SMELSEDLGLLYDSQQGCDFNISVLTAGGEEEELTFCAHRVILMLSPEANFLHKTGSSNITLDVDEECLP
HVPDFLRYFYTRQIDITLTSVKCFHKLASIYGVRKLREYCGQLF
>gnl|CDD|349614 cd18305, BTB_POZ_GCL, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster protein germ cell-less (GCL) and similar proteins. GCL proteins are nuclear envelope proteins highly conserved between the mammalian and Drosophila orthologs. Drosophila melanogaster GCL is a key regulator required for the specification of pole cells and primordial germ cell formation in embryos. Both, human germ cell-less protein-like 1 (GMCL1) and germ cell-less protein-like 2 (GMCL2), also called germ cell-less protein-like 1-like (GMCL1P1 or GMCL1L), may function in spermatogenesis. They may also be substrate-specific adaptors of E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. They contain BTB and BACK domains. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
TSKYIYQTLFLNGENSDITICALGREWKLHKIYLCQSGYFASMFSGSWKESKETVINLEIPDDNITVEAL
NVVFGSLYRDEIEIKPSRVVSILAAATLLQLDGLIQQCSEVMKET
>gnl|CDD|349615 cd18306, BTB_POZ_NS1BP, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Influenza virus NS1A-binding protein (NS1-BP). NS1-BP is also called NS1-binding protein, aryl hydrocarbon receptor-associated protein 3 (ARA3), or IVNS1ABP. It is a novel protein that interacts with the influenza A virus nonstructural NS1 protein, which is relocalized in the nuclei of infected cells. It plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through its kelch repeats. It also interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control. NS1-BP contains BTB and BACK domains at the N-terminal region and kelch repeats at the C-terminal region. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
HPESVLAKLNALRKNRQFCDVILQVGGHEIPAHRAVLACASPYLFELFSSDSDGESILTVKLDGLDPDAV
EVLVNYAYTSRLEVPADLVKSVYSAAKKLKMDRVKKACGDFLLEKLTPQNCIGI
>gnl|CDD|349616 cd18307, BTB_POZ_calicin, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in calicin. Calicin is a basic cytoskeletal protein involved in the formation and maintenance of the highly regular organization of the postacrosomal perinuclear theca, the calyx of mammalian spermatozoa. It contains BTB and BACK domains at the N-terminal region and kelch repeats at the C-terminal region. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
FCDVVISVDNHSFAAHRNVLAAVSPFVKSLISSNDMKATDELSITIDCDYLSPETVEQLLDYFYTGKIVI
SEKNVEDLLKGAKYFNIPRLKDHCVDF
>gnl|CDD|349617 cd18308, BTB1_POZ_LZTR1, first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1). LZTR-1 is a golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas. LZTR-1 contains two BTB domains. This model corresponds to the first domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
QFSSYPKCTLHDDFGRLLESRQFCDVEFIVGEEEERIPAHIAFVAARSKWLRNKILQARERQKQKAEQEV
EDEGSEADSSSASKNDSPMLEVRLPEADPEAFELILSFIYTDKIDPTRKGQDPGSNEVVLLMMDVYRLAL
QFQMSRLEQLCVQYLE
>gnl|CDD|349618 cd18309, BTB2_POZ_LZTR1, second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1). LZTR-1 is a golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas. LZTR-1 contains two BTB domains. This model corresponds to the second domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
IGTTLEQDMEAFLESVGGDFCDITLLLDGHPIPAHKAILAARCSYFEAMFRSFMPEDNTVNISIGEMVPS
RQAFDSLLRYIYYGDVTMPPEDSLYLFSAPYFYGFTNNRLQAYCKQNLEMNVSFEN
>gnl|CDD|349619 cd18310, BTB_POZ_NPR_plant, BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in plant regulatory proteins, NPR1-4, and similar proteins. NPR1 and NPR2 are essential for pathogenicity and the utilization of many nitrogen sources. NPR1 is also called nitrogen pathogenicity regulation protein NPR1, non-inducible immunity protein 1 (Nim1), nonexpresser of PR genes 1, or salicylic acid insensitive 1 (Sai1). It acts as a transcription coactivator that plays dual roles in regulating plant immunity. NPR3 and NPR4 are involved in negative regulation of defense responses against pathogens in plant. NPR proteins contain a BTB domain, DUF3420, ankyrin (ANK) repeats, and a conserved C-terminal domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
KKLSSDLENLLDSPDLFYSDAEIIVEGGRPVPVHRCILAARSPFFRDIFASAKAEGANTKPKLELRELIP
GGIVGYDAFMLVLSYLYSGRLRLVPKEGSACVDSDCWHVACRPAVDFALEVLYAASVFQIPELVSLFQRR
LLDFV
>gnl|CDD|349620 cd18311, BTB_POZ_CP190-like, BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster centrosomal protein 190kD (CP190) and similar proteins. CP190 is a large, multi-domain protein, first identified as a centrosome protein with oscillatory localization over the course of the cell cycle. It has an essential function in the nucleus as a chromatin insulator. It is known to associate with the nuclear matrix, components of the RNAi machinery, active promoters and borders of the repressive chromatin domains. CP190 contains an N-terminal BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
FLQRLQNLFNKTEYCDLTLQFRDNEQLKVHRLVLSACTDYFNVLEQTCEIVDDTLIMPNELQADAVVPVI
NFMYTGQLEFEEKSYGKLLRTAKELNMTVLLKLLEAHRRT
>gnl|CDD|349621 cd18312, BTB_POZ_NPY3-like, BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Arabidopsis thaliana protein naked pins in YUC mutants 3 (NPY3), Root phototropism protein 3 (RPT3), and similar proteins. NPY3 may play an essential role in auxin-mediated organogenesis and in root gravitropic responses in Arabidopsis. RPT3 is a signal transducer of the phototropic response and photo-induced movements. It is necessary for root and hypocotyl phototropisms, but not for the regulation of stomata opening. Proteins in this subfamily contain an N-terminal BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
SWFRDTGEPSDITVRVGNTTFHLHKFPLCSKSGYFKRLASSSSESDPSEIELNDFPGGAEAFELVAKFCY
GMPINLTATNVVGLRCAAEYLEMTESGNLGNLIDK
>gnl|CDD|349622 cd18313, BTB_POZ_BT, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Arabidopsis thaliana BTB/POZ and TAZ domain-containing proteins, BT1-5. BT1-5 may act as substrate-specific adaptors of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. They contain a BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
GADVEIETDNNSHIPAHSNVLASASPVIAGMLKQPRRKSSKKVIKILGVPCDAVRVFIRFLYSSCYEEEE
MEKFGIHLLVLSHVYVVPQLKRVCEKGLEQGL
>gnl|CDD|349623 cd18314, BTB_POZ_trishanku-like, BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Dictyostelium discoideum trishanku and similar proteins. Trishanku is a novel regulator required for normal morphogenesis and cell-type stability in Dictyostelium discoideum. It contains a BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
YNDSEFSDVVLCVGDRKFFAHRIVLCARSPVFRSMLTGSMIESNLKEVTLEDVEPEIFETVLKYMYTGQV
TLSEENVLDLLMLASKYQVPDLEKLC
>gnl|CDD|349624 cd18315, BTB_POZ_BAB-like, BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster proteins bric-a-brac 1 (BAB1), bric-a-brac 2 (BAB2), modifier of mdg4 (doom), and similar proteins. BAB1 and BAB2 probably act as transcriptional regulators that are required for specification of the tarsal segment and are involved in antenna development. Doom is a product of the Drosophila mod(mdg4) gene. It induces apoptosis and binds to baculovirus inhibitor-of-apoptosis proteins. This subfamily also includes Drosophila melanogaster sex determination protein fruitless (FRU), protein jim lovell (LOV), zinc finger protein chinmo, transcription factor GAGA, transcription factor Ken, and longitudinals lacking proteins (LOLA). FRU probably acts as a transcriptional regulator that plays a role in male courtship behavior and sexual orientation, and enhances male-specific expression of takeout in brain-associated fat body. LOV, also called tyrosine kinase-related (TKR), has a regulatory role during midline cell development. Chinmo is a functional effector of the JAK/STAT pathway that regulates eye development, tumor formation, and stem cell self-renewal in Drosophila. GAGA is a transcriptional activator that functions by regulating chromatin structure. Ken, also termed protein Ken and Barbie, is a transcription factor required for Terminalia development. LOLA proteins are putative transcription factors required for axon growth and guidance in the central and peripheral nervous systems. Proteins in this subfamily contain a BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
LVDVTLACEGGSLKAHKLVLAAASPYFAALLKETPPDEHPVIILPDVPYSELKALLDFIYTGEVNVSQEQ
LESLLKLAELLQIKG
>gnl|CDD|349625 cd18316, BTB_POZ_KCTD-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins. The potassium channel tetramerization domain (KCTD) family proteins contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. Some others show Cullin-independent functions including binding and regulation of GABA (gamma-aminobutyric acid) receptors (KCTD8, KCTD12 and KCTD16) and inhibition of AP-2 function (KCTD15). KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
VKLNVGGTLFTTSRSTLLKDPDSLLAALFSGRWPLPRDEDGSIFIDRDPELFRHILNFLRTGKLPLPSDF
VELEELLAEAEFY
>gnl|CDD|349626 cd18317, BTB_POZ_Kv, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in voltage-gated potassium (Kv) channels. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. This family includes several groups of alpha subunits such as KCNA/Kv1 family of Shaker-type Kv channels, KCNB/Kv2 family of Shab-type Kv channels, KCNC/Kv3 family of Shaw-type Kv channels, KCND/Kv4 family of Shal-type Kv channels, KCNF/Kv5 subfamily of Kv channels, KCNG/Kv6 subfamily of Kv channels, KCNV/Kv8 subfamily of Kv channels, and KCNS/Kv9 subfamily of Kv channels. Kv alpha subunits form functional homo- or hetero-tetrameric channels (typically with other alpha subunits from the same subfamily) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. KCNQ/Kv7 channels are not included in this family, since they do not contain a BTB/POZ domain
VVLNVGGTRFELSRSTLLRFPDTRLGKLAKESHAYDESTNEYFFDRNPEVFEAILDYYRTGELHLPSNVC
PASFKEELEFWG
>gnl|CDD|349627 cd18318, BTB_POZ_KCTD20-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 20 (KCTD20) and BTB/POZ domain-containing protein 10 (BTBD10). KCTD20, also termed potassium channel tetramerization domain containing 20, is a positive regulator of Akt signaling. It may play an important role in regulating the death and growth of some non-nervous and nervous cells. BTBD10, also termed glucose metabolism-related protein 1 (GMRP1), plays a major role as an activator of AKT family members. It binds to Akt and protein phosphatase 2A (PP2A) and inhibits the PP2A-mediated dephosphorylation of Akt, thereby keeping Akt activated. It also plays a role in preventing motor neuronal death and accelerating the growth of pancreatic beta cells
EKVTLVVDGTRFVVDPSLFTAHPDTMLGRMFGSGLENNFTRPNERGEYEVADGISATVFRAILDYYKTGI
IRCPPSVSVAELREACDYLLIP
>gnl|CDD|349628 cd18319, BTB_POZ_KLHL42, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 42 (KLHL42). KLHL42, also called Cullin-3-binding protein 9 (Ctb9) or Kelch domain-containing protein 5, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL42) E3 ubiquitin ligase complex mediates the ubiquitination and subsequent degradation of katanin (KATNA1). KLHL42 is involved in microtubule dynamics throughout mitosis. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
EETVQIRLEDRCYNVSKRKLIEQSDYFRALYRSGMRESGEEVVQLRGLSAPGLELVLDFINTSKVHESQG
DSTDTLEENELLEDLVEAASFLQ
>gnl|CDD|349629 cd18320, BTB_POZ_KBTBD13, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 13 (KBTBD13). KBTBD13 is a muscle specific protein. Its autosomal dominant mutations may cause Nemaline Myopathy (NEM). KBTBD13 may act as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that functions as a muscle specific ubiquitin ligase, and thereby implicating the ubiquitin proteasome pathway in the pathogenesis of KBTBD13-associated NEM. KBTBD13 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
MQKVKVWVEEQLFTVDKALLVENSEYFRALFRSGMRECTQDEIRLQGLSARGFRIMLRVLAGERPILNGE
EILQAIECAAFLQ
>gnl|CDD|349630 cd18321, BTB_POZ_EloC, BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Elongin-C (EloC) and similar proteins. Elongin-C is also called elongin 15 kDa subunit, RNA polymerase II transcription factor SIII subunit C, SIII p15, or transcription elongation factor B polypeptide 1 (TCEB1). It is a component of SIII (also known as elongin), which is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. It forms a regulatory complex with subunit B or elongin-B (BC) that enhances the activity of the transcriptionally active subunit A. The BC complex also functions as an adaptor protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC (VHL) and the suppressors of cytokine signaling (SOCS) box ubiquitin ligase family. Elongin-C belongs to the BTB/POZ domain family; the domain is a common protein-protein interaction motif of about 100 amino acids
YVKLISSDGHEFIVDREAAMVSGTIKAMLSGPGQFAENETNEVRFPEISSHILEKVCEYFYYKVRYTNSS
TEIPEFPIPPEIALELLMAANFLDC
>gnl|CDD|349631 cd18322, BTB_POZ_SKP1, BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in S-phase kinase-associated protein 1 (SKP1) and similar proteins. SKP1 is also called cyclin-A/CDK2-associated protein p19 (p19A), organ of Corti protein 2 (OCP-2), organ of Corti protein II (OCP-II), RNA polymerase II elongation factor-like protein, transcription elongation factor B polypeptide 1-like, or p19skp1. It is an essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. SKP1 serves as an adaptor protein that links the F-box protein to CUL1. SKP1 and CUL1 are invariant components of all SCF complexes, while F-box proteins are variable substrate binding modules that determine specificity. SKP1 belongs to the BTB/POZ domain family; the domain is a common protein-protein interaction motif of about 100 amino acids
KIKLQSSDGEIFEVDEEVARQSVTIKNMLEDLGYDDDPIPLPNVTSKILKKVIEWCEHHKDDPPPEIDLD
SEKRTDDIPEWDAEFLKVDQDTLFELILAANYLDIKGLLDLTCKTVANMI
>gnl|CDD|349632 cd18323, BTB_POZ_ZBTB3, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 3 (ZBTB3). ZBTB3 is a transcription factor essential for cancer cell growth via the regulation of the reactive oxygen species (ROS) detoxification pathway. ZBTB3 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
MEFPDHSRHLLQSLREQRHQGFLCDCTVLVGSTQFLAHRAVLASCSPFFHMFYKEQLDKRDLVCINNEIV
TAPAFSLLLEFMYEGRLSFNDTPVEDVLAAASYLHMNDIVKVCKKRLQARALAEADST
>gnl|CDD|349633 cd18324, BTB_POZ_ZBTB18_RP58, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 18 (ZBTB18). ZBTB18 is also called 58 kDa repressor protein (RP58), transcriptional repressor RP58, translin-associated zinc finger protein 1 (TAZ-1), zinc finger protein 238 (ZNF238), or zinc finger protein C2H2-171. It is a sequence-specific transrepressor associated with heterochromatin. It plays a role in various developmental processes such as myogenesis and brain development. It specifically binds the consensus DNA sequence 5'-[AC]ACATCTG[GT][AC]-3' which contains the E box core, and acts by recruiting chromatin remodeling multiprotein complexes. ZBTB18 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
MEFPDHSRHLLQCLSEQRHQGFLCDCTVLVGDAQFRAHRAVLASCSMYFHLFYKDQLDKRDIVHLNSDIV
TAPAFALLLEFMYEGKLQFKDLPIEDVLAAASYLHMYDIVKVCKKKLKEKATTEADSTKKEEDASSCSDK
VESFSSG
>gnl|CDD|349634 cd18325, BTB_POZ_ZBTB18_2-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 18.2 and similar proteins. This subfamily is composed of Xenopus laevis zinc finger and BTB domain-containing protein 18.2, encoded by the znf238.2.L gene, and similar proteins. Many proteins in this group are annotated as zinc finger and BTB domain-containing protein 42 (ZBTB42). However, characterized mammalian ZBTB42 does not belong to this subfamily. ZBTB18.2, like ZBTB18, functions as a transcriptional repressor that plays a role in various developmental processes. Members of this family contain a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
MEFPDHSRQLLQCLSQQRHQGFLCDCTVLVGEAQFRAHRAVLASCSMYFHLFYRDQLDKRDIVHLNSDIV
TAPAFSLLLEFMYEGKLEFSSLPVEDVLAAASYLHMYDIVKVCKGKLKDKELCSEEKI
>gnl|CDD|349635 cd18326, BTB_POZ_ZBTB7A, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 7A (ZBTB7A). ZBTB7A is also called factor binding IST protein 1 (FBI-1), factor that binds to inducer of short transcripts protein 1, HIV-1 1st-binding protein 1, Leukemia/lymphoma-related factor (LRF), POZ and Krueppel erythroid myeloid ontogenic factor, POK erythroid myeloid ontogenic factor, Pokemon, TTF-I-interacting peptide 21 (TIP21), or zinc finger protein 857A (ZNF857A). It is a transcription repressor of key glycolytic genes, including GLUT3, PFKP, and PKM, and its downregulation in human cancer contributes to tumor metabolism. It has been implicated in carcinogenesis and cell differentiation and development. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
IGIPFPDHSSDILSSLNEQRTQGLLCDVVILVEGREFPTHRSVLAACSQYFKKLFTSGAVVDQQNVYEID
FVSAEALTALLDFAYTATLTVSTSNVGDILSAARLLEIPAVSHVCADLLD
>gnl|CDD|349636 cd18327, BTB_POZ_ZBTB7B_ZBTB15, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 7B (ZBTB7B). ZBTB7B is also called Krueppel-related zinc finger protein cKrox, T-helper-inducing POZ/Krueppel-like factor, zinc finger and BTB domain-containing protein 15 (ZBTB15), zinc finger protein 67 (ZNF67), Zfp67, zinc finger protein 857B (ZNF857B), or zinc finger protein Th-POK. It is a transcriptional regulator of extracellular matrix gene expression. It plays widespread and critical roles in T-cell development, particularly as the master regulator of CD4 commitment. It also plays a role as a potent driver of brown fat development and thermogenesis, as well as cold-induced beige fat formation. ZBTB7B contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
IGIPFPEHSSELLSCLNEQRRAGLLCDLTIKTRGLEYRTHRAVLAACSLYFRKLFTGGGGGSGDLGAGGG
QDVCELDFVGPEALGALLEFAYTATLTISSSNMREVLRAARLLEIPCVADACADILQ
>gnl|CDD|349637 cd18328, BTB_POZ_ZBTB7C_ZBTB36, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 7C (ZBTB7C). ZBTB7C is also called affected by papillomavirus DNA integration in ME180 cells protein 1 (APM-1), zinc finger and BTB domain-containing protein 36 (ZBTB36), zinc finger protein 857C (ZNF857C), or kidney cancer-related POZ domain and Kruppel-like protein (Kr-POK). It is a transcriptional repressor with a pro-oncogenic role that relies upon binding to p53 and inhibition of its transactivation function. It may act as an important regulator of fatty acid synthesis and may induce rapid cancer cell proliferation by increasing palmitate synthesis. The ZBTB7C gene has been identified as a susceptibility gene to ischemic injury. ZBTB7C contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
IGIPFPNHSSEVLCSLNEQRHDGLLCDVVLIVQDQEYRTHRSVLAACSKYFKKLFTAGTLADQPYVYEID
FVTPEALSAILEFAYTSTLTITTSNVKHILNAAQMLEIQCIINVCLEIMD
>gnl|CDD|349638 cd18329, BTB_POZ_ZBTB8A_BOZF1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 8A (ZBTB8A). ZBTB8A, also called BTB/POZ and zinc-finger domain-containing factor or BTB/POZ and zinc-finger domains factor on chromosome 1 (BOZ-F1), is a novel proto-oncoprotein that stimulates cell proliferation. It binds to all the proximal GC boxes to repress transcription, and it inhibits p53 acetylation without affecting p53 stability. It may be involved in gastric adenocarcinoma cell differentiation, cancer invasion, and metastasis. ZBTB8A contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
ISSHQSRLLQQLDEQRKQELFCDCSILVEGQVFKAHRNVLFASSGYFKMLLSQNAKETGQPTVATFDVFS
PDTFTIILDFVYSGKLSLTSQNVIEVMSAASYLQMTDVISVCKTFI
>gnl|CDD|349639 cd18330, BTB_POZ_ZBTB8B, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 8B (ZBTB8B). ZBTB8B may be involved in transcriptional regulation. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
YYTKLLGELNEQRKRDFFCDCSIIVEGRIFKAHRNILFANSGYFRALLIHYIQDSGRHSTASLDIVTSEA
FSIILDFLYSGKLDLCSENVIEVMSAASYLQMTDVVNFCKGYI
>gnl|CDD|349640 cd18331, BTB_POZ_ZBTB27_BCL6, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in B-cell lymphoma 6 protein (BCL-6). BCL-6 is also called B-cell lymphoma 5 protein (BCL-5), zinc finger and BTB domain-containing protein 27 (ZBTB27), protein LAZ-3, or zinc finger protein 51 (ZNF51). It is a transcriptional repressor mainly required for germinal center (GC) formation and antibody affinity maturation, which have different mechanisms of action specific to the lineage and biological functions. It represses its target genes by binding directly to the DNA sequence 5'-TTCCTAGAA-3' or indirectly by repressing the transcriptional activity of transcription factors. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
CIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPE
INPEGFNILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFI
>gnl|CDD|349641 cd18332, BTB_POZ_ZBTB28_BCL6B, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in B-cell CLL/lymphoma 6 member B protein (BCL6B). BCL6B is also called Bcl6-associated zinc finger protein, zinc finger protein 62, or zinc finger and BTB domain-containing protein 28 (ZBTB28). It is a sequence-specific transcriptional repressor in association with BCL-6. It may function in a narrow stage or be related to some events in the early B-cell development. BCL6B plays an important role as a potential tumor suppressor in gastric cancer; it is found preferentially methylated in gastric cancer. It also inhibits both colorectal cancer growth and hepatocellular carcinoma metastases. BCL6B contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
RHSSDVLLNLNELRKRDILTDVTLLVGGTPLRAHKAVLIACSGFFYSIFSGRVGEGVSVLTLPSGLEARG
FQLLLDFMYTSRLPLTPRTVPAVLAAATYLQMEHVVETCRRFIQ
>gnl|CDD|349642 cd18333, BTB_POZ_ZBTB29_HIC1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in hypermethylated in cancer 1 protein (Hic-1). Hic-1, also called zinc finger and BTB domain-containing protein 29 (ZBTB29), is a sequence-specific transcriptional repressor that recognizes and binds to the consensus sequence '5-[CG]NG[CG]GGGCA[CA]CC-3'. It may act as a tumor suppressor, and is involved in regulatory loops modulating P53-dependent and E2F1-dependent cell survival, growth control, and stress responses. It also regulates intestinal immunity and homeostasis. Hic-1 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
VPSHSRQLLLQLNTQRTKGFLCDVIIVVQNALFRAHKNILAASSVYLKSLVVHDNLINLDHEMVSPGIFR
LILDYIYTGRLSEGDPGSEQNLGAVLAAASYLQIPDLVALCKKKLKRNGKY
>gnl|CDD|349643 cd18334, BTB_POZ_ZBTB30_HIC2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in hypermethylated in cancer 2 protein (Hic-2). Hic-2 is also called HIC1-related gene on chromosome 22 protein (HRG22), Hic-3, or zinc finger and BTB domain-containing protein 30 (ZBTB30). It is a homolog of tumor suppressor Hic-1. It functions as a transcriptional regulator. It is a dosage-dependent regulator of cardiac development located within the distal 22q11 deletion syndrome region. Hic-2 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
LPNHAKQLLLQLNQQRAKGFLCDVIIVVENALFRAHKNILAASSMYFKSLVLHDNLINLDTDMVNPTVFR
QILDFIYTGKLLTSDQPGEQNFNALLTAASYLQLHDLAALCRKKLKRNGK
>gnl|CDD|349644 cd18335, BTB_POZ_KLHL1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 1 (KLHL1). KLHL1 is a neuronal actin-binding protein that modulates voltage-gated CaV2.1 (P/Q-type) and CaV3.2 (alpha1H T-type) calcium channels. It may play a role in organizing the actin cytoskeleton the brain cells. KLHL1 contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
HHAEQTFRKMESYLKQQQLCDVILIAGNRKIPAHRLVLSAVSDYFAAMFTSDVCEAKQEEIKMEGIDPNA
LWDLVQFAYTGCLELKEDTIENLLAAACLLQLSQVVEVCCHFLMKLLHPSNCLGIR
>gnl|CDD|349645 cd18336, BTB_POZ_KLHL4, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 4 (KLHL4). KLHL4 shares high identity and similarity with the Drosophila kelch protein, a component of ring canals. It may be associated with X-linked cleft palate (CPX) and is also a candidate gene in the impairment of mullerian duct development. In addition, it has been identified as a target of insulin-like growth factor binding protein 5 (IGFBP5). KLHL4 contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
NHAEQTFRKMENYLQHKQLCDVLLIAGNLKIPAHRLVLSAVSDYFAAMFTNDVREAKQEEIKMEGVDPDA
LKALVHYAYTGVLELKEDTIESLLAAACLLQLSQVIDVCCNFLMKQLHPSNCLGIR
>gnl|CDD|349646 cd18337, BTB_POZ_KLHL5, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 5 (KLHL5). KLHL5 shares high identity and similarity with the Drosophila kelch protein, a component of ring canals. It is abundantly expressed in the ovary, adrenal gland, and thymus. It contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
FQALNHAEQTFKKMENYLRHKQLCDVVLVAGDRRIPAHRLVLSSVSDYFAAMFTNDVREAKQEEIKMEGV
EPNALWALVQYAYTGRLELKEDNIECLLSTACLLQLSQVVEACCKFLMKQLHPSNCLGIR
>gnl|CDD|349647 cd18338, BTB_POZ_KLHL2_Mayven, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 2 (KLHL2). KLHL2, also called actin-binding protein Mayven, is a novel actin-binding protein predominantly expressed in the brain. It plays a role in the reorganization of the actin cytoskeleton, and promotes growth of cell projections in oligodendrocyte precursors. KLHL2 is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, such as NPTXR, leading most often to their proteasomal degradation. It contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
NPRHMKKAFKVMNELRSQNLLCDVTIVAEDVEIAAHRVVLAACSPYFHAMFTGEMSESRAKRVRIKEVDG
WTLKMLIDYVYTAEIQVTEENVQVLLPAAGLLQLQDVKKTCCEFLESQLHP
>gnl|CDD|349648 cd18339, BTB_POZ_KLHL3, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 3 (KLHL3). KLHL3 is a component of an E3 ubiquitin ligase complex that regulates blood pressure by targeting With-No-Lysine (WNK) kinases for degradation. It contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
NPAHMKKAFKVMNELRSKQLLCDVTIVAEDVEIEAHRVVLAACSPYFCAMFTGDMSESKAKKIEIKDVDG
QTLSKLIDYIYTAEIEVTEENVQVLLPAASLLQLMDVRQNCCDFLQSQLHP
>gnl|CDD|349649 cd18340, BTB_POZ_KLHL40_KBTBD5, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 40 (KLHL40). KLHL40, also called Kelch repeat and BTB domain-containing protein 5 (KBTBD5) or sarcosynapsin, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development. Mutations in KLHL40 may cause severe autosomal-recessive nemaline myopathy. KLHL40 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
DQVEELRLYQQTLLQDGLKDLLDHNKFVDCVLKIKEKEFPCHRLVLAACSPYFRAMFLSDLEESKKREIV
LEDVDPDVMGKILHYIYTSEIEITEQNVQDIFAAANMFQIPSIFTVCVSFLQKRLCLSNCLAIF
>gnl|CDD|349650 cd18341, BTB_POZ_KLHL41_KBTBD10, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 41 (KLHL41). KLHL41 is also called Kel-like protein 23, Kelch repeat and BTB domain-containing protein 10 (KBTBD10), Kelch-related protein 1 (Krp1), or sarcosine. It is a novel kelch-related protein that is involved in pseudopod elongation in transformed cells. It is also involved in skeletal muscle development and differentiation. It regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
EIKEELRLYQSTLLQDGLKELLDENKFVDCTLKAGDKSLPCHRLILAACSPYFREYFLSEESEEKKKEVV
LDNVDPNIMDMILKYLYSAEIDLNDGNVQDIFALASRFQIPSVFTVCVTYLQKRLSPANCLAI
>gnl|CDD|349651 cd18342, BTB_POZ_SPOP, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein (SPOP). SPOP, also called HIB homolog 1 or Roadkill homolog 1, is a novel nuclear speckle-type protein which serves as an adaptor of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and proteasomal degradation of target proteins, such as BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
MVKVPECRLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVE
PEVFKEMMCFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEDALCSNLSVENA
>gnl|CDD|349652 cd18343, BTB_POZ_SPOPL, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein-like (SPOPL). SPOPL, also called HIB homolog 2 or Roadkill homolog 2, is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The complexes may contain homodimeric SPOPL or the heterodimers formed by speckle-type POZ protein (SPOP) and SPOPL, which are less efficient than ubiquitin ligase complexes containing only SPOP. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
LKVPECRLAEDLGNLWENSRFTDCSLFVGGQEFKAHKSILAARSPVFNAMFEHEMEESKKNRVEINDVDP
EVFKEMMRFIYTGKAPNLDKMADNLLAAADKYALERLKVMCEEALCNNLSVEN
>gnl|CDD|349653 cd18344, BTB_POZ_TDPOZ, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in TD and POZ domain-containing proteins (TDPOZ). TDPOZ is a family of bipartite animal and plant proteins that contains a tumor necrosis factor receptor-associated factor (TRAF) domain (TD) and a POZ/BTB domain. TDPOZ proteins may be nuclear scaffold proteins probably involved in transcription regulation in early development and other cellular processes. This subfamily contains only mammalian members. Plant TDPOZ proteins contain a MATH domain at the N-terminal region and are named "BTB/POZ and MATH domain-containing proteins (BPM)", not included in this subfamily. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
PAIKDPRHMLTDDLGELWENSLFTDCCLLVAGHEFRAHKAILAARSPVFRAMFEHEMEERLKNPIEIHDL
DPQVFKEMMGFIYTGKAPHLHSHSMACDVLAAADKYGLEGLKVLCEDALCRNLSVENA
>gnl|CDD|349654 cd18345, BTB_POZ_roadkill-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster protein roadkill and similar proteins. Drosophila melanogaster protein roadkill, also called Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
PECRLSDDLGLLFERSAFSDVTLCVGGREFQAHKAILAARSPVFNAMFEHEMEERKQNRVEITDVDHEVM
REMLRFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEEALCSNLSVENV
>gnl|CDD|349655 cd18346, BTB_POZ_BTBD1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 1 (BTBD1). BTBD1, also called Hepatitis C virus NS5A-transactivated protein 8 or HCV NS5A-transactivated protein 8, is a BTB-domain-containing Kelch-like protein that is expressed in skeletal muscle and interacts with DNA topoisomerase 1 (Topo1), a key enzyme of cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. BTBD1 may serve as substrate-specific adaptor of an E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
NWQATKSSLKERFAFLFNNELLSDVRFVVGKGRPRGPGPGAQRIPAHRFVLAAGSAVFDAMFNGGMATTS
AEIELPDVEPAAFLALLRFLYSDEVQIGPETVMTTLYTAKKYAVPALEAHCVEFLTKHLRADN
>gnl|CDD|349656 cd18347, BTB_POZ_BTBD2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 2 (BTBD2). BTBD2 is a BTB-domain-containing Kelch-like protein that interacts with DNA topoisomerase 1 (Topo1), a key enzyme of cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
NWQATKPTVQERFAFLFNNEVLSDVHFLVGKGLGSQRIPAHRFVLAVGSAVFDAMFNGGMATTSTEIELP
DVEPAAFLALLKFLYSDEVQIGPETVMTTLYTAKKYAVPALEAHCVEFLKKNLRADN
>gnl|CDD|349657 cd18348, BTB_POZ_BTBD3, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 3 (BTBD3). BTBD3 is a BTB-domain-containing Kelch-like protein that controls dendrite orientation toward active axons in the mammalian neocortex. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
WQGLYPTIRERNAVMFNNDLMADIHFVVGPPGGTQRLPGHKYVLAVGSSVFHAMFYGELAEDKDEIRIPD
VEPAAFLAMLKYIYCDEIDLAADTVLATLYAAKKYIVPHLARACVNFLETSLSAKNACVLL
>gnl|CDD|349658 cd18349, BTB_POZ_BTBD6, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 6 (BTBD6). BTBD6, also termed lens BTB domain protein, is a BTB-domain-containing Kelch-like protein required for proper embryogenesis and plays an essential evolutionary conserved role during neuronal development. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
LMFNNELMADVHFIVGPPGASQRVPAHKYVLAVGSSVFYAMFYGDLAEVKSEIHIPDVEPAAFLILLKYM
YSDEIDLEADTVLATLYAAKKYIVPALAKACVNFLETSL
>gnl|CDD|349659 cd18350, BTB_POZ_ABTB2_BPOZ2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2). ABTB2, also called bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins with various functions ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, with implications for Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation, and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homolog (PTEN). It contains an ankyrin repeat, BTB/POZ, and BACK domains. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKSLLTNKSEQESQGSKTIEI
SDIKYHIFQMLMQYLYYGGTESMEIPIADVLELLSAASLFQLDALQRHCEILCSQTINLENAVN
>gnl|CDD|349660 cd18351, BTB_POZ_BTBD11, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 11 (BTBD11). BTBD11, also called ankyrin repeat and BTB/POZ domain-containing protein BTBD11, is a BTB-domain-containing protein. The BTBD11 gene has been recently identified as an all-trans retinoic acid (atRA)-responsive gene that lies downstream of atRA and its receptors in the regulation of neurite outgrowth and cell adhesion in neural as well as non-neural tissues. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
PKLTEIKRKQTSRLDPHFLNNKEMSDVTFLVEGRPFYAHKVLLFTASPRFKALLSNKPSAENTCIEISYV
KYHIFQLVMQYLYCGGTESLLIKNNEIMELLSAAKFFQLEALQRHCEIICAKSINTENCVD
>gnl|CDD|349661 cd18352, BTB_POZ_ARIA_plant, BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in plant ARM repeat protein interacting with ABF2 (ARIA) and similar proteins. ARIA is an armadillo (ARM) repeat and BTB domain-containing protein that acts as a positive regulator of ABA response via the modulation of the transcriptional activity of ABF2, a transcription factor which controls ABA-dependent gene expression via the G-box-type ABA-responsive elements. ARIA is a novel abscisic acid signaling component. It negatively regulates seed germination and young seedling growth. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
VYLGEQYVNNATLSDVTFLVEGRRFYAHRIALLASSDAFRAMFDGGYREKEARDIEIPNIRWEVFELMMR
FIYTGSVDITNDIAKDLLRAADQYLLEGLKRLCEYTIAQDLTLENI
>gnl|CDD|349662 cd18353, BTB_POZ_RCBTB1_CLLD7, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in RCC1 and BTB domain-containing protein 1 (RCBTB1). RCBTB1 is also called chronic lymphocytic leukemia deletion region gene 7 protein (CLLD7), CLL deletion region gene 7 protein, regulator of chromosome condensation and BTB domain-containing protein 1, or E4.5. It is a novel chromosome condensation regulator-like guanine nucleotide exchange factor that may be involved in cell cycle regulation by chromatin remodeling. It may also function as a tumor suppressor that regulates pathways of DNA damage/repair and apoptosis. RCBTB1 may also be a substrate adaptor for a cullin3 (CUL3) E3 ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Biallelic mutations in RCBTB1 may cause isolated and syndromic retinal dystrophy. It contains an RCC1 repeat, a BTB domain, and a BACK domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
HDDFLTVAESLKKEFDSPETSDLKFRVDGKYIHVHKAVLKIRCEHFRTMFQSHWNEDMKEVIEIDQFSYP
VYRAFLEYLYTDSVDLPPEDAIGLLDLATSYCENRLKKLCQHIIKRG
>gnl|CDD|349663 cd18354, BTB_POZ_RCBTB2_CHC1L, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in RCC1 and BTB domain-containing protein 2 (RCBTB2). RCBTB2 is also called chromosome condensation 1-like (CHC1-L), RCC1-like G exchanging factor, or regulator of chromosome condensation and BTB domain-containing protein 2. It is a chromosome condensation regulator-like guanine nucleotide exchange factor (GEF) protein for the Ras-related GTPase Ran. It contains an RCC1 repeat, a BTB domain, and a BACK domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
PDDHLTVAESLKREFDNPDTADLKFLVDGKYIYVHKVLLKIRCEHFRSLLNENEEEIIEMSQFSYPVYRA
FLEYLYTDSISLSPEDAIGLLDLATFYRENRLKKLCQQTIKQGICEE
>gnl|CDD|349664 cd18355, BTB1_POZ_RHOBTB1, first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1). RhoBTB1 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB1 functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
CPSKSRNEAGQLLDNPLCADVMFILQEQVHIFAHRIYLATSSSKFYDLFLMECEESLSSWSKGFYSMHKE
MQVNPVSNRPCPMTVVKMDSSIQHGPFKTVLRFLYTGQLDEKEKDLMRLAQIAEILEVFDLRMMVENIMN
KEAFMN
>gnl|CDD|349665 cd18356, BTB1_POZ_RHOBTB2, first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 2 (RhoBTB2). RhoBTB2, also called Deleted in breast cancer 2 gene protein (DBC2) or p83, is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB2 functions as a tumor suppressor that regulates the expression of the methyltransferase METTL7A. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
PDPPTKSEEHPAHLLEDPLCADVILVLQERIRIYAHKIYLSTSSSKFYDLFLMDRGRDLSSWSRAFVSIQ
EEVAEDPLTYKSRLMVVVKMDSSIQPGPFRAVLKYLYTGELDENERDLMHIAHIAELLEVFDLRMMVANI
LNNEAFMN
>gnl|CDD|349666 cd18357, BTB1_POZ_RHOBTB3, first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 3 (RhoBTB3). RhoBTB3 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB3 is a Golgi-associated Rho-related ATPase that regulates the S/G2 transition of the cell cycle by targeting cyclin E for ubiquitylation. It is involved in vesicle trafficking and in targeting proteins for degradation in the proteasome. It binds directly to Rab9 GTPase and functions with Rab9 in protein transport from endosomes to the trans Golgi network. It also promotes proteasomal degradation of Hypoxia-inducible factor alpha (HIFalpha) through facilitating hydroxylation and suppresses the Warburg effect. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
EASHYNSDLLNLLYSCQCADVAFCTEDLKEVGEAHRVVLCSVSQVFMLLFGVKSTREIQDSSIGRTAQSL
FAVDGDDIFPAPSHDLHTAGPPVRVIVKDSLLCACLPEILKFIYSGASQWEELEEDLRKKLKDSEKVEHV
LEKVKCLLKTPGKLRCLRD
>gnl|CDD|349667 cd18358, BTB2_POZ_RHOBTB1, second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1). RhoBTB1 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB1 functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
KAFHVRKANRIKECLSKGTFSDVTFKLDDGTINAHKPLLICSCEWMAAMFGGSFIESANSEVVLPNISKV
SMQAVLDYLYTKQLSPTADLDPLELIALANRFCLPHLVALTEQHAVQELTKASKSG
>gnl|CDD|349668 cd18359, BTB2_POZ_RHOBTB2, second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 2 (RhoBTB2). RhoBTB2, also called Deleted in breast cancer 2 gene protein (DBC2) or p83, is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB2 functions as a tumor suppressor that regulates the expression of the methyltransferase METTL7A. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
KAFHVRRTNRVKECLAKGTFSDVTFMLDDGTISAHKPLLISSCDWMAAMFGGPFVESSTTEVVFPYTSRS
SMRAVLEYLYTGQFSSSPDLDDMKLIILANRLCLPHLVALTEQYTVTVLMEAAQ
>gnl|CDD|349669 cd18360, BTB2_POZ_RHOBTB3, second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 3 (RhoBTB3). RhoBTB3 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB3 is a Golgi-associated Rho-related ATPase that regulates the S/G2 transition of the cell cycle by targeting cyclin E for ubiquitylation. It is involved in vesicle trafficking and in targeting proteins for degradation in the proteasome. It binds directly to Rab9 GTPase and functions with Rab9 in protein transport from endosomes to the trans Golgi network. It also promotes proteasomal degradation of Hypoxia-inducible factor alpha (HIFalpha) through facilitating hydroxylation and suppresses the Warburg effect. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
LGLFFNSPLLADVVFKIQGTTVPAHRAVLVARCEVMAAMFNGNYAEAKSFLVPIYGVSKDTFLSFLEYLY
TDSCCPASILQAMALLICAEMYQVSRLQHICELYIITQLQ
>gnl|CDD|349670 cd18361, BTB_POZ_KCTD1-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins, KCTD1 and KCTD15. This subfamily of KCTD proteins includes KCTD1 and KCTD15. KCTD1 is a nuclear BTB/POZ domain-containing protein that acts as a transcriptional repressor and mediates protein-protein interactions through a BTB domain. It represses the transcriptional activity of AP-2 family members, including TFAP2A, TFAP2B and TFAP2C. It also functions as a novel inhibitor of the Wnt signaling pathway. Mutations in KCTD1 cause scalp-ear-nipple (SEN) syndrome. KCTD15 is a BTB/POZ domain-containing protein that plays a role in the regulation of neural crest (NC) formation and other steps in embryonic development. It inhibits AP2 transcriptional activity by interaction with its activation domain. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD1 BTB domains form pentamers
VHIDVGGHIYTSSLETLTKYPESRLGKLFNGSIPIVLDSLKQHYFIDRDGKMFRHILNFLRTSKLLLPDD
FTEFDLLYEEARYYELQPMVKQLE
>gnl|CDD|349671 cd18362, BTB_POZ_KCTD2-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins KCTD2, KCTD5, and KCTD17, and similar proteins. This subfamily includes potassium channel tetramerization domain-containing proteins KCTD2, KCTD5, and KCTD17, all of which function as adaptors of Cullin3 based ubiquitin E3 ubiquitin ligases. KCTD2 suppresses gliomagenesis by destabilizing c-Myc. KCTD5 is a negative regulator of the AKT pathway, a key signaling cascade frequently deregulated in cancer. KCTD5 does not impact the operation of Kv4.2, Kv3.4, Kv2.1, or Kv1.2 channels. KCTD17 polyubiquitylates trichoplein, a protein involved in ciliogenesis down-regulation. It is a positive regulator of ciliogenesis, playing a crucial role in the initial steps of axoneme extension. A missense mutation in KCTD17 causes autosomal dominant myoclonus-dystonia (M-D). The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. KCTD5 and KCTD17 BTB domains form pentamer structures
WVKLNVGGTYFLTTRTTLCRDPKSFLCRLCQEDPDLPSDKDETGAYLIDRDPTYFGPILNYLRHGKLIID
KDLAEEGVLEEAEFY
>gnl|CDD|349672 cd18363, BTB_POZ_KCTD3-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 3 (KCTD3) and SH3KBP1-binding protein 1 (SHKBP1). The group of KCTD proteins includes KCTD3 and SHKBP1. KCTD3, also called renal carcinoma antigen NY-REN-45, is a BTB/POZ domain-containing protein that is an accessory subunit of potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3 (HCN3), upregulating its cell-surface expression and current density without affecting its voltage dependence and kinetics. SHKBP1, also called SETA-binding protein 1, interacts with cathepsin B and participates in tumor necrosis factor (TNF)-induced apoptosis in ovarian cancer cells. It can promote epidermal growth factor receptor (EGFR) signaling by interrupting c-Cbl-CIN85 complex and inhibiting EGFR degradation. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
GDIINLNVGGKRFSTSRQTLTWIPDSFFTSLLSGRISSLKDETGAIFIDRDPKLFSIILNYLRTKEIDLR
NVDISSLRHEAEFYGI
>gnl|CDD|349673 cd18364, BTB_POZ_KCTD4, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 4 (KCTD4). KCTD4 is a BTB/POZ domain-containing protein with an unknown biological function. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
LVTLNVGGYLYITQRQTLTKYPDSFLEGMVNGKIQCTVDADGNYFIDRDGLLFRHVLNFLRNGELLLPEG
FQENQLLALEADFYQL
>gnl|CDD|349674 cd18365, BTB_POZ_KCTD6_like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins, KCTD6, KCTD21 and similar proteins. KCTD6, also called KCASH3 (KCTD containing, Cullin3 adaptor, suppressor of Hedgehog 3), is a substrate-specific adaptor of cullin-3, effectively regulating protein levels of the muscle small ankyrin-1 isoform 5 (sAnk1.5). KCTD21, also called KCASH2, functions as a substrate-specific adaptor of cullin-3, promoting the ubiquitination and degradation of histone deacetylase HDAC1, thereby inhibiting the deacetylation-mediated transcriptional activation of the Hedgehog effectors Gli1 and Gli2. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
DIVNLNVGGVHYTTTLATLTRFPDSMLGAMFSGSMPTTRDDQGNYFIDRDGTLFRYILNFLRSSQLSLPE
DFKEYDLLLREADFYQIEPLIEAL
>gnl|CDD|349675 cd18366, BTB_POZ_KCTD7, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 7 (KCTD7). KCTD7 is a BTB/POZ domain-containing protein that has an impact on K+ fluxes, neurotransmitter synthesis, and neuronal function. It functions as a regulator of potassium conductance in neurons, and is involved in the control of excitability of cortical neurons. Mutations in KCTD7 may cause progressive myoclonus epilepsy (PME). The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
QFPEVVPLNVGGMHFTTRLSTLRKYEDSMLAAMFSGRHHIPKDSEGRYFIDRDGSYFGYILNFLRDGDLP
PRERARAVYKEAQYYGIGPLIE
>gnl|CDD|349676 cd18367, BTB_POZ_KCTD8-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins, KCTD8, KCTD12, KCTD16 and similar proteins. This subfamily of KCTD proteins includes KCTD8, KCTD12 (also called predominantly fetal expressed T1 domain/Pfetin), and KCTD16. They act as auxiliary subunits of GABAB receptors associated with mood disorders. KCTD8 interacts as a tetramer with GABRB1 and GABRB2. KCTD12 regulates agonist potency and kinetics of GABAB receptor signaling. It promotes tumorigenesis by facilitating CDC25B/CDK1/Aurora A-dependent G2/M transition. KCTD16 interacts with amyloid beta precursor protein (APP), a type I transmembrane protein involved in a variety of cellular processes such as cell adhesion, and axon guidance. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
FPEIVELNVGGQVYTTSLSTLIKDPDSLLGRMFSGKNRQELARDSKGRYFLDRDGVLFRYILDYLRNQKL
VLPENFPERERLKREAEYFQLPELVKALRA
>gnl|CDD|349677 cd18368, BTB_POZ_KCTD9, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 9 (KCTD9). KCTD9 is a BTB/POZ domain-containing protein that contributes to liver injury through NK cell activation during hepatitis B virus-induced acute-on-chronic liver failure. It functions as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of target proteins, leading to their degradation by the proteasome. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD9 BTB domain forms a pentameric structure
DWIKLNVGGRIFTTTRSTLVKKEPDSMLARMFSDDSTWPSSRDENGAYLIDRSPEYFEPILNYLRHGQLI
LNDGLNPLGVLEEAKFFGIQSLIEILEQLI
>gnl|CDD|349678 cd18369, BTB_POZ_KCTD10-like_BACURD, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins, KCTD10 (BACURD3), KCTD13 (BACURD1), and TNFAIP1 (BACURD2). This subfamily of KCTD proteins, also called the BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein (BACURD) subfamily, includes KCTD10 (BACURD3), KCTD13 (BACURD1), and TNFAIP1 (BACURD2). KCTD10 is a BTB/POZ domain-containing protein that interacts with proliferating cell nuclear antigen (PCNA) and polymerase delta, and participates in DNA repair, DNA replication, and cell-cycle control. Its down-regulation could inhibit cell proliferation. KCTD10 also plays crucial roles in embryonic angiogenesis and heart development in mammals by negatively regulating the Notch signaling pathway. KCTD13 is a BTB/POZ domain-containing protein that may function as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of RhoA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. TNFAIP1, also called protein B12, is a BTB/POZ domain-containing protein that is involved in DNA replication, DNA damage repair, cell apoptosis, and is implicated in human diseases including cancer, Alzheimer's disease (AD) and type 2 diabetic nephropathy. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. KCTD10 and KCTD13 BTB domains form a novel two-fold symmetric tetramer that is distinct from the tetramer formed by voltage-gated potassium (Kv) channels
VKLNVGGSLHYTTIGTLTKQDTMLRAMFSGRMEVLTDSEGWILIDRCGKHFGTILNYLRDGSVPLPESRR
ELAELLAEAKYYLVQGLVEQC
>gnl|CDD|349679 cd18370, BTB_POZ_KCTD11, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein KCTD11. KCTD11 may function as an antagonist of the Hedgehog pathway of cell proliferation and differentiation by affecting the nuclear transfer of transcription factor GLI1, thus maintaining cerebellar granule cells in the undifferentiated state. It is a probable substrate-specific adapter for a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex towards HDAC1. It contains a BTB/POZ domain; in some cases the domain may be truncated. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. Variants of the human/mouse KCTD11 appear to contain truncated BTB/POZ domains
VTLNVGGTLYSTTLETLTRFPDSMLGAMFRAGTPIPPNLNMQGGGHYFIDRDGKAFRHILNFLRLGRLDL
PRGYGETALLRAEADFYQ
>gnl|CDD|349680 cd18371, BTB_POZ_KCTD14, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 14 (KCTD14). KCTD14 is a BTB/POZ domain-containing protein with unknown biological function. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
SQVVSLNVGGHIYTTTLSTLRKFPGSKLAELFNGQPKLRTDSEGRYFIDRDGTYFRYILEYLRTNQVPTQ
HIQEVYKEALFYDIEPLVKLLEESPQIFG
>gnl|CDD|349681 cd18372, BTB_POZ_KCTD18, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 18 (KCTD18). KCTD18 is a BTB/POZ domain-containing protein with with unknown biological function. A duplication of the KCTD18 gene has been found in a patient with epilepsy, developmental delay, and autistic behavior, which may contribute to the phenotype. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
DVLRLNVGGCIYTARRESLCRFKDSMLSSMFSGRFPLKLDESGACVIDRDGRLFKYLLDYLHGELQIPED
EQTRLALQEEADYFGIPYPYSLTDHLANEME
>gnl|CDD|349682 cd18373, BTB1_POZ_KCTD19, first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 19 (KCTD19). KCTD19 is a BTB/POZ domain-containing protein with unclear biological function. It may be a host factor involved in Nef-induced downregulation of MHC-I. Nef is a HIV-1-encoded protein that plays a key role in the development of AIDS. KCTD19 contains two BTB domains. This model corresponds to the first domain. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
FYFNVGGWIFSVPKSKLAQFPDSLLWKEASSLSESENTRLFIDRDGFTFRHVHYYLQTSKLSSSSCSELN
LLYEQAAGLQLTSLLQALDNLKEGKHHL
>gnl|CDD|349683 cd18374, BTB2_POZ_KCTD19, second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 19 (KCTD19). KCTD19 is a BTB/POZ domain-containing protein with unclear biological function. It may be a host factor involved in Nef-induced downregulation of MHC-I. Nef is a HIV-1-encoded protein that plays a key role in the development of AIDS. KCTD19 contains two BTB domains. This model corresponds to the second domain. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
QIVKVYVGSHWYATYLKTLLKYPELLSNSKKVRWITYGQTLLISGDGQMFRHILNFLRLGKLLLPSEFKE
WPLLCQEVEEYQIPALSEALRQCEAYRLW
>gnl|CDD|349684 cd18375, BTB_POZ_KCNRG, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel regulatory protein (KCNRG). KCNRG, also called potassium channel regulator or protein CLLD4, is an endoplasmic reticulum (ER)-associated tumor suppressor that regulates Kv1 family potassium channel proteins by retaining a fraction of the channels in endomembranes. It contains a BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization
ELVTLNVGGKKFTTRPSTLRRFPDSRLARMLDGKDQDFKVVNGQFFVDRDGSLFSYILDYLRTGQLTLPT
EFSDYNRLAREAEFYGLYSLADLLSQN
>gnl|CDD|349685 cd18376, BTB_POZ_FIP2-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Arabidopsis thaliana FH protein interacting protein FIP2 and similar proteins. FIP2 may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It contains a BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization
VKLNVGGQKFTTTLDTLTKDPDSMLAAMFSGRHSLKKDEDGSYFIDRDGTHFRHILNYLRDGEVKIPTED
RSVLKELLEEAEYYQLRGL
>gnl|CDD|349686 cd18377, BTB_POZ_Kv1_KCNA, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCNA/Kv1 subfamily of Shaker-type voltage-dependent potassium channels. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv1, also known as subfamily A, contains eight alpha subunit members, Kv1.1 (KCNA1), Kv1.2 (KCNA2), Kv1.3 (KCNA3), Kv1.4 (KCNA4), Kv1.5 (KCNA5), Kv1.6 (KCNA6), Kv1.7 (KCNA7), and Kv1.8 (KCNA10), which are orthologs of the Shaker gene in Drosophila. They are delayed rectifiers except for Kv1.4 (KCNA4), which is an A-type potassium channel. Delayed rectifiers are slow opening and closing voltage-gated potassium channels. Because of their delayed activation kinetics, they play an important role in controlling action potential duration. A-type channels are fast/rapidly inactivating potassium channels. Kv1/KCNA subfamily alpha subunits form functional homo- or hetero-tetrameric channels (with other Kv1/KCNA alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
ERVVINVSGLRFETQLKTLAQFPNTLLGDPNKRMRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPV
NVPLDIFLEEIRFYE
>gnl|CDD|349687 cd18378, BTB_POZ_Kv2_KCNB, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCNB/Kv2 subfamily of Shab-type voltage-dependent potassium channels. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv3, also known as subfamily C, contains two alpha subunit members, Kv2.1 (KCNB1) and Kv2.2 (KCNB2), which are orthologs of the Shab gene in Drosophila. They are delayed-rectifier potassium currents in various neurons, although their physiological roles often remain elusive. Kv2/KCNB subfamily alpha subunits form functional homo- or hetero-tetrameric channels (with other alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
SRRVLLNVGGVRHEVLWRTLDRLPRTRLGRLRECNTHESLLELCDDYDLEDNEYFFDRHPGAFTSILNFY
RTGKLHMPEEMCVLSFSQELEYWGIDEIYLESCCQHRYH
>gnl|CDD|349688 cd18379, BTB_POZ_Kv3_KCNC, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCNC/Kv3 subfamily of Shaw-type voltage-dependent potassium channels. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv3, also known as subfamily C, contains four alpha subunit members, Kv3.1 (KCNC1), Kv3.2 (KCNC2), Kv3.3 (KCNC3), and Kv3.4 (KCNC4), which are orthologs of the Shaw gene in Drosophila. Unlike other Kv subfamilies, Kv3 channels typically open only at positive potentials and both, activation and deactivation, in response to changes in voltage are very rapid. They are uniquely associated with the ability of certain neurons to fire action potentials and to release neurotransmitter at high rates of up to 1,000 Hz. Kv3/KCNC subfamily alpha subunits form functional homo- or hetero-tetrameric channels (with other alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
IVINVGGVRHETYKSTLRNLPDTRLAWLTETEASAFDYDPVTGEFFFDRHPGVFAQILNYYRTGKLHCPA
DVCGPLFEEELAFWGIDETQIEPCCWMTYRQHRDAQETL
>gnl|CDD|349689 cd18380, BTB_POZ_Kv4_KCND, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCND/Kv4 subfamily of Shal-type voltage-dependent potassium channels. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv4, also known as subfamily D, contains three alpha subunit members, Kv4.1 (KCND1), Kv4.2 (KCND2), and Kv4.3 (KCND3), which are orthologs of the Shal gene in Drosophila. They are A-type potassium channels that mediate the native, fast inactivating (A-type) K+ current (IA) described both in the nervous system (A currents) and the heart (transient outward current). Kv4/KCND subfamily alpha subunits form functional homo- or hetero-tetrameric channels through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. They are modulated by cytoplasmic KChIPs/KCNIPs (Kv-channel interacting proteins), which are small calcium binding proteins with EF-hand-like domains
RIVINVSGRRFETWKNTLEKYPDTLLGSTEKEFFYDDDTKEYFFDRDPEIFRHILNFYRTGKLHYPRHEC
ISAYDDELAFFGILPEIIGDCCYEDYRDRKRE
>gnl|CDD|349690 cd18381, BTB_POZ_Kv5_KCNF1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCNF/Kv5 subfamily of potassium voltage-gated channels. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv5, also known as subfamily F, only contains KCNF1 (also known as Kv5.1 or kH1), which functions as a regulatory alpha-subunit of voltage-gated potassium channel that when coassembled with Kv2.1 can modulate gating in a physiologically relevant manner. It forms hetero-tetrameric channels (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
TEIVVNVGGVRQVLYGDVLNRYPETRLAELLNCLSGGYDAIFSLCDDYDPGKREFYFDRDPDAFKCIIEV
YYYGEIHMKKGICPICFKNEMDFWRVDLDFLDECCKCHLSEKREEL
>gnl|CDD|349691 cd18382, BTB_POZ_Kv6_KCNG, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCNG/Kv6 subfamily of potassium voltage-gated channels. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv6, also known as subfamily G, includes KCNG1 (Kv6.1), KCNG2 (Kv6.2 or KCNF2), KCNG3 (Kv6.3) and KCNG4 (Kv6.4), which are regulatory alpha subunits and do not form functional channels on their own. KCNG1 can form functional heterotetrameric channels with KCNB1 (also known as Kv2.1), and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1. KCNG2, also called cardiac potassium channel subunit, can form functional heterodimeric channels with KCNB1, and further modulates channel activity by shifting the threshold and the half-maximal activation to more negative values. KCNG3, also called voltage-gated potassium channel subunit Kv10.1, is an electrically silent modulatory subunit that can form functional heterotetrameric channels with KCNB1, and further promotes a reduction in the rate of activation and inactivation of the delayed rectifier voltage-gated potassium channel KCNB1. KCNG4 is a silent voltage-gated potassium (KvS) channel subunit that can form functional heterotetrameric channels with KCNB1, and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1
VIINVGGARYSLPWSTLDRFPLTRLSRLKACRSEDDILRVCDDYDVERNEFFFDRSPEAFGVILLFLRAG
KLRLLREMCALSFQEELAYWGIEEAHLERCCKRRLLRRL
>gnl|CDD|349692 cd18384, BTB_POZ_Kv9_KCNS, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCNS/Kv9 subfamily of potassium voltage-gated channels. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv9, also known as subfamily S, includes KCNS1 (Kv9.1), KCNS2 (Kv9.2) and KCNS3 (Kv9.3). They are regulatory alpha subunits that cannot form functional homo-tetrameric channels. Both KCNS1 and KCNS2 are delayed-rectifier K(+) channel alpha subunits that can form functional heterotetrameric channels with KCNB1 (also known as Kv2.1) and KCNB2 (also known as Kv2.2), and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2. KCNS3 is a delayed-rectifier K(+) channel alpha subunit linked to tissue oxygenation responses. It can form functional heterotetrameric channels with KCNB1, and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1
IRINVGGFRRRLSASALLRFPGTRLGRLLACHSEEAILELCDDYDVAAREFYFDRNPGFFLYVLHFYRTG
KLHVMDELCVFSFSQEIEYWGINEFFLDSCCSYRYH
>gnl|CDD|349693 cd18385, BTB_POZ_BTBD10_GMRP1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 10 (BTBD10). BTBD10, also called glucose metabolism-related protein 1 (GMRP1), plays a major role as an activator of AKT family members. It binds to Akt and protein phosphatase 2A (PP2A) and inhibits the PP2A-mediated dephosphorylation of Akt, thereby keeping Akt activated. It also plays a role in preventing motor neuronal death and accelerating the growth of pancreatic beta cells. BTBD10 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
TSERVTLIVDNTRFVVDPSIFTAQPNTMLGRMFGSGREHNFTRPNEKGEYEVAEGISSTVFRAILDYYKT
GIIRCPDGISIPELREACDYLCISFDYSTIKCRDLSALMH
>gnl|CDD|349694 cd18386, BTB_POZ_KCTD20, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 20 (KCTD20). KCTD20, also called potassium channel tetramerization domain containing 20, is a positive regulator of Akt signaling. It may play an important role in regulating the death and growth of some non-nervous and nervous cells. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
APEKVTLIVDGTRFVVNPQIFTAHPDTMLGRMFGPGREYNFTRPNEKGEYEIAEGISCTVFRTVLDYYKT
GIINCPDGISIPDLRDTCDYLCINFDFNTIKCQD
>gnl|CDD|349695 cd18387, BTB_POZ_KCTD1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 1 (KCTD1). KCTD1 is a nuclear BTB/POZ domain-containing protein that acts as a transcriptional repressor and mediates protein-protein interactions through a BTB domain. It represses the transcriptional activity of AP-2 family members, including TFAP2A, TFAP2B and TFAP2C to various extent. It also functions as a novel inhibitor of the Wnt signaling pathway. Mutations in KCTD1 cause scalp-ear-nipple (SEN) syndrome. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD1 BTB domains form pentamers
SNAPVHIDVGGHMYTSSLATLTKYPESRIGRLFDGTEPIVLDSLKQHYFIDRDGQMFRYILNFLRTSKLL
IPDDFKDYSLLYEEAKYFQLQPMLLELERWKQDRE
>gnl|CDD|349696 cd18388, BTB_POZ_KCTD15, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 15 (KCTD15). KCTD15 is a BTB/POZ domain-containing protein that plays a role in the regulation of neural crest (NC) formation and other steps in embryonic development. It inhibits AP2 transcriptional activity by interaction with its activation domain. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD1 BTB domains, closely related to KCTD15, form pentamers
NAPVHIDVGGHMYTSSLATLTKYPDSRISRLFNGTEPIVLDSLKQHYFIDRDGEIFRYILSFLRTSKLLL
PEDFKDFNLLYEEAKYYQLQPMVKELERW
>gnl|CDD|349697 cd18389, BTB_POZ_KCTD2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 2 (KCTD2). KCTD2 is a BTB/POZ domain-containing protein that functions as an adaptor of Cullin3 E3 ubiquitin ligase. It suppresses gliomagenesis by destabilizing c-Myc. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. KCTD5 and KCTD17 BTB domain, highly similar to KCTD2, form pentamer structures
KWVRLNVGGTYFVSTKQTLCRDPKSFLYRLCQEDPDLDSDKDETGAYLIDRDPTYFGPILNYLRHGKLII
NKELAEEGVLEEAEFYNIASLVRLVKERIRDNENR
>gnl|CDD|349698 cd18390, BTB_POZ_KCTD5, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 5 (KCTD5). KCTD5 is a BTB/POZ domain-containing protein that functions as a substrate adaptor for cullin3 based ubiquitin E3 ligases. It is a negative regulator of the AKT pathway, a key signaling cascade frequently deregulated in cancer. KCTD5 does not impact the operation of Kv4.2, Kv3.4, Kv2.1, or Kv1.2 channels. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. KCTD5 forms pentamers mediated by its BTB domain
GGVSKWVRLNVGGTYFLTTRQTLCRDPKSFLYRLCQADPDLDSDKDETGAYLIDRDPTYFGPVLNYLRHG
KLVINKDLAEEGVLEEAEFYNITSLIKLVKDKIRERDSKTSQ
>gnl|CDD|349699 cd18391, BTB_POZ_KCTD17, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 17 (KCTD17). KCTD17 is a BTB/POZ domain-containing protein that functions as a substrate-adaptor for cullin3-RING ubiquitin ligases that polyubiquitylates trichoplein, a protein involved in ciliogenesis down-regulation. It is a positive regulator of ciliogenesis, playing a crucial role in the initial steps of axoneme extension. A missense mutation in KCTD17 causes autosomal dominant myoclonus-dystonia (M-D). The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD17 BTB domains form pentamers
KWVRLNVGGTVFLTTRQTLCREQKSFLSRLCQGEELQSDRDETGAYLIDRDPTYFGPILNFLRHGKLVLD
KDMAEEGVLEEAEFYNIGPLIRIIKDRMEEK
>gnl|CDD|349700 cd18392, BTB_POZ_KCTD3, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 3 (KCTD3). KCTD3, also called renal carcinoma antigen NY-REN-45, is a BTB/POZ domain-containing protein that is an accessory subunit of potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3 (HCN3), upregulating its cell-surface expression and current density without affecting its voltage dependence and kinetics. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
GEIIQLNVGGTRFSTSRQTLMWIPDSFFSSLLSGRISSLKDETGAIFIDRDPTAFVPILNFLRTKELDLR
GVNINVLRHEAEFYGITP
>gnl|CDD|349701 cd18393, BTB_POZ_SHKBP1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in SH3KBP1-binding protein 1 (SHKBP1). SHKBP1, also called SETA-binding protein 1, interacts with cathepsin B and participates in tumor necrosis factor (TNF)-induced apoptosis in ovarian cancer cells. It can promote epidermal growth factor receptor (EGFR) signaling by interrupting c-Cbl-CIN85 complex and inhibiting EGFR degradation. It contains a BTB/POZ domain, also known as tetramerization (T1) domain, a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
GEVIHLNVGGKRFSTSRQTLTWIPDSFFSSLLSGRISTLKDETGAIFIDRDPTVFAPILNFLRTKELDPR
GIHVSLLLHEAQFYGITPLVRRLQLCEELDRSS
>gnl|CDD|349702 cd18394, BTB_POZ_KCTD6, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 6 (KCTD6). KCTD6, also called KCTD containing, Cullin3 adaptor, suppressor of Hedgehog 3 (KCASH3), is a BTB/POZ domain-containing protein that functions as a substrate-specific adaptor of cullin-3, regulating protein levels of the muscle small ankyrin-1 isoform 5 (sAnk1.5) as well as suppressing histone deacetylase and Hedgehog activity in medulloblastoma. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
MTDPVTLNVGGHLYTTSLSTLTRYPDSMLGAMFRGDFPTARDSQGNYFIDRDGPLFRYILNFLRTSELTL
PVDFKEFDLLRKEADFYQIEPLIQCLNDPKPLYP
>gnl|CDD|349703 cd18395, BTB_POZ_KCTD21, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 21 (KCTD21). KCTD21, also calledz KCTD containing, Cullin3 adaptor, suppressor of Hedgehog 2 (KCASH2), is a BTB/POZ domain-containing protein that functions as a substrate-specific adaptor of cullin-3, promoting the ubiquitination and degradation of histone deacetylase HDAC1, thereby inhibiting the deacetylation-mediated transcriptional activation of the Hedgehog effectors Gli1 and Gli2. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
DPITLNVGGKLYTTSLATLTRYPDSMLGAMFSGKFPTKKDSQGNCFIDRDGKIFRYILNFLRTSHLDLPE
DFQEMGLLKREADFYQIQPLIEALQEKE
>gnl|CDD|349704 cd18396, BTB_POZ_KCTD8, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein KCTD8. KCTD8, a BTB/POZ domain-containing protein, is an auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. It interacts as a tetramer with GABRB1 and GABRB2. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
PFPEVVELNVGGQVYVTKHSTLLSVPDSTLASMFSRRAARELPRDNRGRFFIDRDGFLFRYVLDYLRDKQ
LALPDHFPEKERLLREAEYFQLGDLVKLLTPKV
>gnl|CDD|349705 cd18397, BTB_POZ_KCTD12_Pfetin, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 12 (KCTD12). KCTD12, also called predominantly fetal expressed T1 domain (Pfetin), is a BTB/POZ domain-containing protein that is an auxiliary subunit of GABAB receptors associated with mood disorders. It regulates agonist potency and kinetics of GABAB receptor signaling. It promotes tumorigenesis by facilitating CDC25B/CDK1/Aurora A-dependent G2/M transition. It also regulates colorectal cancer cell stemness through the ERK pathway. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
FPEIVELNVGGQVYVTRHTTLVSVPDSLLWHMFSQQKPGELARDSKGRFFLDRDGFLFRYILDYLRDLQL
VLPDYFPERSRLQREAEFFQLPELVKRLNP
>gnl|CDD|349706 cd18398, BTB_POZ_KCTD16, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 16 (KCTD16). KCTD16 is a BTB/POZ domain-containing protein that is an auxiliary subunit of GABAB receptors associated with mood disorders. It interacts with amyloid beta precursor protein (APP), a type I transmembrane protein involved in a variety of cellular processes such as cell adhesion and axon guidance. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization
FPEVVELNVGGQVYFTRHATLVSIPHSLLWKMFSPKRDTANDLAKDSKGRFFIDRDGFLFRYILDYLRDR
QVVLPDHFPEKGRLKREAEYFQLPDLVKLLTPD
>gnl|CDD|349707 cd18399, BTB_POZ_KCTD10_BACURD3, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 10 (KCTD10). KCTD10, also called BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3 (BACURD3), is a BTB/POZ domain-containing protein that interacts with proliferating cell nuclear antigen (PCNA) and polymerase delta, and participates in DNA repair, DNA replication, and cell-cycle control. Its down-regulation could inhibit cell proliferation. KCTD10 also plays crucial roles in embryonic angiogenesis and heart development in mammals by negatively regulating the Notch signaling pathway. Furthermore, KCTD10 may function as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of target proteins, leading to their degradation by the proteasome. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD10 BTB domain forms a novel two-fold symmetric tetramer that is distinct from the tetramer formed by voltage-gated potassium (Kv) channels
GTSPSSKYVKLNVGGALYYTTMQTLTKQDTMLKAMFSGRMEVLTDSEGWILIDRCGKHFGTILNYLRDGA
VPLPESRREIEELLAEAKYYLVQGLVEECQAALQNKDTYE
>gnl|CDD|349708 cd18400, BTB_POZ_KCTD13_BACURD1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 13 (KCTD13). KCTD13, also called BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1 (BACURD1), or TNFAIP1-like protein, is a BTB/POZ domain-containing protein that may function as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of RhoA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD13 BTB domain forms a novel two-fold symmetric tetramer that is distinct from the tetramer formed by voltage-gated potassium (Kv) channels
SKYVKLNVGGSLHYTTVQTLTKQDTMLKAMFSGRVEVLTDSEGWVLIDRSGRHFGTILNYLRDGSVPLPE
STRELEELLGEARYYLVQGLVEDCQLALQQKRD
>gnl|CDD|349709 cd18401, BTB_POZ_TNFAIP1_BACURD2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in tumor necrosis factor, alpha-induced protein 1, endothelial (TNFAIP1). TNFAIP1, also called BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2 (BACURD2), or protein B12, is a BTB/POZ domain-containing protein that is involved in DNA replication, DNA damage repair and cell apoptosis, and is implicated in human diseases including cancer, Alzheimer's disease (AD) and type 2 diabetic nephropathy. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The BTB domains of other BACURD subfamily members, KCTD10 and KCTD13, form a novel two-fold symmetric tetramer that is distinct from the tetramer formed by voltage-gated potassium (Kv) channels
GNKYVRLNVGGSLYYTTVQVLTRHDTMLKAMFSGRMEVLTDKEGWILIDRCGKHFGTILNYLRDDTVALP
KSRQEIKELMAEAKYYLIQGLVDMCQAALQDKKD
>gnl|CDD|349710 cd18402, BTB_POZ_KCNA1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily A member 1 (KCNA1). KCNA1 is also called voltage-gated K(+) channel HuKI, voltage-gated potassium channel HBK1, or voltage-gated potassium channel subunit Kv1.1. It mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the kidney. It is involved in the regulation of the membrane potential and nerve signaling, and prevents neuronal hyperexcitability. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNA1 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv1/KCNA alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
DHDDHECCERVVINIAGLRFETQLKTLAQFPNTLLGNPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQS
GGRLRRPVNVPLDMFSEEIKFYELGEEA
>gnl|CDD|349711 cd18403, BTB_POZ_KCNA2_KCNA3, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily A members 2 (KCNA2) and 3 (KCNA3). KCNA2 is also called NGK1, voltage-gated K(+) channel HuKIV, voltage-gated potassium channel HBK5, or voltage-gated potassium channel subunit Kv1.2. KCNA3 is also called HGK5, HLK3, HPCN3, voltage-gated K(+) channel HuKIII, or voltage-gated potassium channel subunit Kv1.3. KCNA2 and KCNA3 mediate transmembrane potassium transport in excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. KCNA2 primarily functions in the brain and the central nervous system, but also in the cardiovascular system. It prevents aberrant action potential firing and regulates neuronal output. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNA2 and KCNA3 are alpha subunits that form functional homo- or hetero-tetrameric channels (with other Kv1/KCNA alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
ERVVINISGLRFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPV
NVPLDIFSEEIRFYELGEEAMEMFREDEG
>gnl|CDD|349712 cd18405, BTB_POZ_KCNA4, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily A member 4 (KCNA4). KCNA4 is also called HPCN2, or voltage-gated K(+) channel HuKII, voltage-gated potassium channel HBK4, voltage-gated potassium channel HK1, or voltage-gated potassium channel subunit Kv1.4. It mediates transmembrane potassium transport in excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNA4 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv1/KCNA alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
ERVVINVSGLRFETQLKTLAQFPETLLGDPEKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLKRPV
NVPFDIFSEEVKFYELGEEALLKFRED
>gnl|CDD|349713 cd18406, BTB_POZ_KCNA5, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily A member 5 (KCNA5). KCNA5, also called HPCN1, voltage-gated potassium channel HK2, or voltage-gated potassium channel subunit Kv1.5, mediates transmembrane potassium transport in excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. KCNA5 may play a role in regulating the secretion of insulin in normal pancreatic islets. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNA5 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv1/KCNA alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
ERVIINIAGLRFETQLGTLNQFPDTLLGDPDKRMRYFDPLRNEYFFDRNRPSFDGILYFYQSGGKIRRPV
NVSIDVFADEIRFYQLGEEAMERFRED
>gnl|CDD|349714 cd18407, BTB_POZ_KCNA6, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily A member 6 (KCNA6). KCNA6, also called voltage-gated potassium channel HBK2 or voltage-gated potassium channel subunit Kv1.6, mediates transmembrane potassium transport in excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. KCNA6 is distributed primarily in neurons of central and peripheral nervous systems. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNA6 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv1/KCNA alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
ERLVINISGLRFETQLRTLSIFPDTLLGDPSRRVRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPV
HVPLDIFLEEIRFYQLGQEAIETFREDEGFIPEEEKPLPSHHFQRQVWLLFEYPESS
>gnl|CDD|349715 cd18408, BTB_POZ_KCNA7, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily A member 7 (KCNA7). KCNA7, also called voltage-gated potassium channel subunit Kv1.7, mediates transmembrane potassium transport in excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. KCNA7 plays an important role in the repolarization of cell membranes. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNA7 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv1/KCNA alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
PCGCCERVVLNVAGLRFETRARTLGRFPDTLLGDPARRGRFYDDRRREYFFDRHRPSFDAVLYYYQSGGR
LRRPAHVPLDVFLEEVAFYGLGAAALARLREDEGCPVPPERPLPR
>gnl|CDD|349716 cd18409, BTB_POZ_KCNA10, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily A member 10 (KCNA10). KCNA10, also called voltage-gated potassium channel subunit Kv1.8, is a cyclic nucleotide-gated, voltage-activated potassium channel that mediates transmembrane potassium transport in excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. KCNA10 is expressed in proximal tubular cells, glomerular and vascular endothelial cells, as well as in vascular smooth muscle cells. It may facilitate proximal tubular sodium absorption by stabilizing cell membrane voltage. The channel activity is up-regulated by cAMP. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNA10 is an alpha subunit that forms functional homotetrameric channels through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
QKVIINIAGLRFETQLKTLDQFPDTLLGDPEKRMKYFDSMRNEYFFDRNRPSFDGILYYYQSGGKIRRPA
NVPLDVFADEIIFYELG
>gnl|CDD|349717 cd18410, BTB_POZ_Shaker-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster potassium voltage-gated channel protein Shaker and similar proteins. Shaker, also termed protein minisleep, represents a family of putative potassium channel proteins in the nervous system of Drosophila. It is a voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Shaker plays a role in the regulation of sleep need or efficiency. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. Shaker is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
ERVVINVSGLRFETQLKTLNQFPDTLLGDPQRRNRYYDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPV
NVPLDVFSEEIKFYELGENAFEKYREDEGF
>gnl|CDD|349718 cd18411, BTB_POZ_KCNB1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily B member 1 (KCNB1). KCNB1, also called delayed rectifier potassium channel 1 (DRK1) or voltage-gated potassium channel subunit Kv2.1, mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. KCNB1 is involved in the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNB1 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
EIIRSKACSRRVKLNVGGLAHEVLWRTLDRLPRTRLGKLRDCNTHESLMEICDDYNLEENEYFFDRHPGA
FTSILNFYRTGKLHMMEEMCALSFSQELDYWGIDEIYLESCCQARYH
>gnl|CDD|349719 cd18412, BTB_POZ_KCNB2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily B member 2 (KCNB2). KCNB2, also called voltage-gated potassium channel subunit Kv2.2, mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. KCNB2 contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNB2 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
SLPPEPVEIIRSKACSRRVKINVGGLNHEVLWRTLDRLPRTRLGKLRDCNTHESLLEVCDDYNLNENEYF
FDRHPGAFTSILNFYRTGKLHMMEEMCALSFGQELDYWGIDEIYLESCCQARYHQKK
>gnl|CDD|349720 cd18413, BTB_POZ_Shab-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster potassium voltage-gated channel protein Shab and similar proteins. Shab is a slow delayed rectifier voltage-gated potassium channel in Drosophila. It mediates transmembrane potassium transport in excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. Shab is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
NRRVVINVGGVKHEVLWRTLDRMPHTRLGKLRDSNTHEAIVELCDDYSLADNEYFFDRHPRSFASILNFY
RTGKLHLVEEMCVLAFSDDLEYWGVDELYLESCCQHKYH
>gnl|CDD|349721 cd18414, BTB_KCNC1_3, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily C members KCNC1 and KCNC3. KCNC1 (also called NGK2, voltage-gated potassium channel subunit Kv3.1, or voltage-gated potassium channel subunit Kv4) and KCNC3 (also called KSHIIID or voltage-gated potassium channel subunit Kv3.3) play important roles in the rapid repolarization of fast-firing brain neurons. Assuming opened or closed conformations in response to the voltage difference across the membrane, the proteins form tetrameric potassium-selective channels through which potassium ions may pass in accordance with their electrochemical gradient. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNC1 and KCNC3 are alpha subunit that form functional homo- or hetero-tetrameric channels (with other alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
ESDRIVINVGGTRHETYRSTLRTLPGTRLAWLAEPDAHSNFDYDPRADEFFFDRHPGVFAHILNYYRTGK
LHCPADVCGPLYEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDSF
>gnl|CDD|349722 cd18415, BTB_KCNC2_4, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily C members KCNC2 and KCNC4. KCNC2, also called Shaw-like potassium channel or voltage-gated potassium channel Kv3.2, is a delayed rectifier voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. It contributes to the regulation of the fast action potential repolarization and in sustained high-frequency firing in neurons of the central nervous system. KCNC4, also called KSHIIIC or voltage-gated potassium channel subunit Kv3.4, is a novel high-voltage-activating, tetraethylammonium (TEA)-sensitive, type-A potassium channel that mediates the voltage-dependent potassium ion permeability of excitable membranes. It plays a pivotal role in oxidative stress-related neural cell damage as an oxidation-sensitive channel. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNC2 and KCNC4 are alpha subunit that form functional homo- or hetero-tetrameric channels (with other alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
NERIILNVGGTRHETYRSTLKTLPGTRLALLASSDPQGDCLTQCSQVGGSDGSPGGGNEFFFDRHPGVFA
YVLNYYRTGKLHCPADVCGPLFEEELAFWGIDETDVEPCCWMTYRQHRDAEEAL
>gnl|CDD|349723 cd18416, BTB_Shaw-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel protein Shaw. Shaw, also called Shaw2, is a voltage-gated potassium channel in Drosophila. It mediates transmembrane potassium transport in excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. Shaw is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
ENRVVLNVGGIRHETYKATLKKIPATRLSRLTEALANYDPVLNEYFFDRHPGVFAQILNYYRTGKLHYPT
DVCGPLFEEELEFWGLDANQVEPCCWMTYTAHRDTQETLAVL
>gnl|CDD|349724 cd18417, BTB_POZ_KCND1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily D member 1 (KCND1). KCND1, also called voltage-gated potassium channel subunit Kv4.1, is a pore-forming subunit of voltage-gated rapidly inactivating A-type potassium channels. It may contribute to I (To) current in heart and I (Sa) current in neurons. Its properties are modulated by interactions with other alpha subunits and with regulatory subunits. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCND1 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv4/KCND alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. It is modulated by cytoplasmic KChIPs/KCNIPs (Kv-channel interacting proteins), which are small calcium binding proteins with EF-hand-like domains
ATWLPFARAAAVGWLPLAKKPMPKPPSDKKRRNDEILVVNVSGRRFQTWKNTLDRYPDTLLGSSEKEFFY
NEDTQEYFFDRDPEMFRHILNFYRTGRLHYPRHECIQAFDEELSFYGIIPEIIGDCCLEEYRDRKKEN
>gnl|CDD|349725 cd18418, BTB_POZ_KCND2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily D member 2 (KCND2). KCND2, also called voltage-gated potassium channel subunit Kv4.2, is a major pore-forming subunit in somatodendritic subthreshold A-type potassium current I(SA) channels. It mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCND2 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv4/KCND alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. It is modulated by cytoplasmic KChIPs/KCNIPs (Kv-channel interacting proteins), which are small calcium binding proteins with EF-hand-like domains
LIVLNVSGTRFQTWRNTLERYPDTLLGSSERDFFYHEETQEYFFDRDPDIFRHILNFYRTGKLHYPRHEC
ISAYDEELAFFGIIPEIIGDCCYEEYKDRRREN
>gnl|CDD|349726 cd18419, BTB_POZ_KCND3, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily D member 3 (KCND3). KCND3, also called voltage-gated potassium channel subunit Kv4.3, is a pore-forming subunit of voltage-gated rapidly inactivating A-type potassium channels. Mutations in KCND3 cause spinocerebellar ataxia. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCND3 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv4/KCND alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. It is modulated by cytoplasmic KChIPs/KCNIPs (Kv-channel interacting proteins), which are small calcium binding proteins with EF-hand-like domains
AAWLPFARAAAIGWMPVANCPMPLAPADKNKRQDELIVLNVSGRRFQTWRTTLERYPDTLLGSTEKEFFF
NEDTKEYFFDRDPEVFRCVLNFYRTGKLHYPRYECISAYDEELAFYGILPEIIGDCCYEEYKDRKREN
>gnl|CDD|349727 cd18420, BTB_POZ_Shal-like, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster potassium voltage-gated channel protein Shal and similar proteins. Drosophila melanogaster Shal, also called Shaker cognate l or Shal2, is a transient potassium current (I(A)) channel, which is required for maintaining excitability during repetitive firing and normal locomotion in Drosophila. It may play a role in the nervous system and in the regulation of beating frequency in pacemaker cells. Shal mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. Shal is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
AWLPFARAAAIGWVPIANNPLPPPPVDQERRRTDDEKLIINVSGRRFETWRNTLEKYPDTLLGSNEREFF
YDEETKEYFFDRDPDIFRHILNYYRTGKLHYPKHECLTAYDEELAFFGIMPDIIGDCCYEDYRDRKREN
>gnl|CDD|349728 cd18421, BTB_POZ_KCNG1_2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily G members, KCNG1 and KCNG2. KCNG1, also called voltage-gated potassium channel subunit Kv6.1 or kH2, functions as a regulatory alpha-subunit of voltage-gated potassium channel that can form functional heterotetrameric channels with KCNB1 (also known as Kv2.1), and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1. KCNG2, also called cardiac potassium channel subunit or voltage-gated potassium channel subunit Kv6.2, is a new gamma-subunit of voltage-gated potassium channels that can form functional heterodimeric channels with KCNB1, and further modulates channel activity by shifting the threshold and the half-maximal activation to more negative values. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNG1 and KCNG2 are regulatory alpha subunits and do not form homomultimers. They form heteromultimers (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
DRTRHVIINVGGIKYRIPWTTLEEFPLTRLGQLKSCNNFDEIMDICDDYDVTCNEFFFDRNPCAFRTILT
FLRAGKLRLLREMCALSFQEELLYWGIEEENLEWCCRRRLLQKE
>gnl|CDD|349729 cd18422, BTB_POZ_KCNG3, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily G member 3 (KCNG3). KCNG3, also called voltage-gated potassium channel subunit Kv6.3 or voltage-gated potassium channel subunit Kv10.1, is an electrically silent modulatory subunit that can form functional heterotetrameric channels with KCNB1 (also known as Kv2.1), and further promotes a reduction in the rate of activation and inactivation of the delayed rectifier voltage-gated potassium channel KCNB1. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNG3 is a regulatory alpha subunit that cannot form a functional homo-tetrameric channel. It forms hetero-tetrameric channels (with other functional alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
VTLNVGGTRYSFSREVIKDFPLRRVSRLHGCLSEQDVLEVCDDYDRERNEYFFDRHSEAFGFIMLYVKYG
KLRFVPQMCELSFYNEMIYWGLERSHLEYCCQRRLDDRMSD
>gnl|CDD|349730 cd18423, BTB_POZ_KCNG4, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily G member 4 (KCNG4). KCNG4, also called voltage-gated potassium channel subunit Kv6.4, is a silent voltage-gated potassium (KvS) channel subunit that can form functional heterotetrameric channels with KCNB1 (also known as Kv2.1), and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNG4 is a regulatory alpha subunit that cannot form a functional homo-tetrameric channel. It forms hetero-tetrameric channels (with other functional alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
KREIIINVGGIKYLMPWSTLDEFPLTRLGKLKFCSSYEEIVQICDDYDEDTNEFFFDRNPCAFRMIVSFL
AAGKLRLLREMCALSFQEELTYWGIEEANLERCCLRKLFQKL
>gnl|CDD|349731 cd18424, BTB_POZ_KCNV1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily V member 1 (KCNV1). KCNV1, also called neuronal potassium channel alpha subunit HNKA or voltage-gated potassium channel subunit Kv8.1, is a new neuronal voltage-gated potassium channel alpha subunit with specific inhibitory properties towards Shab and Shaw channels. It modulates KCNB1 (also known as Kv2.1) and KCNB2 (also known as Kv2.2) channel activity by shifting the threshold for inactivation to more negative values and by slowing the rate of inactivation. It can also down-regulate the channel activity of KCNB1, KCNB2, KCNC4 (also known as Kv3.4) and KCND1 (also known as Kv4.1), possibly by trapping them in intracellular membranes. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNV1 is a regulatory alpha subunit that cannot form a functional homo-tetrameric channel. It forms hetero-tetrameric channels (with other functional alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
FTINVGGSRFVLSQQVLSSHPETRLGKLAVSVRDSVLELCDDANFVDNEYFFDRSSQAFKYIMNYYKTGH
LHVMEELCAISFLQEIEYWGIDELSIDSCCRERYYRRKE
>gnl|CDD|349732 cd18425, BTB_POZ_KCNV2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily V member 2 (KCNV2). KCNV2, also called voltage-gated potassium channel subunit Kv8.2, is a modulatory voltage-gated potassium channel alpha subunit that modulates channel activity by shifting the threshold and the half-maximal activation to more negative values. KCNV2 is essential for visual function and cone survival. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNV2 is a regulatory alpha subunit that cannot form a functional homo-tetrameric channel. It forms hetero-tetrameric channels (with other functional alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
LNINVGGTSYQISYRVAASYPKTRIGRLATYTDRSRKLDLCDDYNVQNDEYFFDRDPAVFHHIYNFYRTG
VLWVKDELCPRNFLEEINYWGVRIKNTPRCCRISFEER
>gnl|CDD|349733 cd18426, BTB_POZ_KCNS1, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily S member 1 (KCNS1). KCNS1, also called delayed-rectifier K(+) channel alpha subunit 1 or voltage-gated potassium channel subunit Kv9.1, is a modulatory alpha subunit of voltage-gated potassium channel that mediates neuropathic pain following nerve injury. It can form functional heterotetrameric channels with KCNB1 (also known as Kv2.1) and KCNB2 (also known as Kv2.2), and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNS1 is a regulatory alpha subunit that cannot form a functional homo-tetrameric channel. It forms hetero-tetrameric channels (with other functional alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
ININVGGLKRRLSSSTLSKFPDTRLGRLLSCDSEESILQICDDYDVSAKEFYFDRNPGLFPYVLHFYQTG
KLHIMEELCVFSFSQEIEYWGINEFFLDSCCSYRYH
>gnl|CDD|349734 cd18427, BTB_POZ_KCNS2, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily S member 2 (KCNS2). KCNS2, also called delayed-rectifier K(+) channel alpha subunit 2 or voltage-gated potassium channel subunit Kv9.2, is a modulatory alpha subunit of voltage-gated potassium channel that can form functional heterotetrameric channels with KCNB1 (also known as Kv2.1) and KCNB2 (also known as Kv2.2), and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNS2 is a regulatory alpha subunit that cannot form a functional homo-tetrameric channel. It forms hetero-tetrameric channels (with other functional alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
EISINVGGFKKRLRSHTLLRFPETRLGRLLSCRSKESILELCDDYDDTKNEFYFDRNPELFPYVLHFYNT
GKLHVMGELCVFSFSQEIEYWGINEFFIDSCCSYSYH
>gnl|CDD|349735 cd18428, BTB_POZ_KCNS3, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily S member 3 (KCNS3). KCNS3, also called delayed-rectifier K(+) channel alpha subunit 3 or voltage-gated potassium channel subunit Kv9.3, is an alpha subunit of voltage-gated potassium channel linked to tissue oxygenation responses. It can form functional heterotetrameric channels with KCNB1 (also known as Kv2.1), and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNS3 is a regulatory alpha subunit that cannot form a functional homo-tetrameric channel. It forms hetero-tetrameric channels (with other functional alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif
ELINLNVGGFKQSVDQSTLLRFPHTRLGKLLNCHSEEAILELCDDYSVADKEYYFDRNPSLFRYVLNFYY
TGKLHVMEELCVFSFCQEIEYWGINELFIDSCCSNRYQ
>gnl|CDD|349485 cd18429, M14_Nna1-like, Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; uncharacterized bacterial subgroup. A bacterial subgroup of the Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP),-like proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins (such as alpha-tubulin in eukaryotes) to remove a C-terminal tyrosine. Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain
DLDRLLAKIRKNPLVEITTIGKTVEGRPLEIIRIGNESAPHRVFLRARAHPWEAGGNWVVEGLVERLLQN
DEEAKRFLKRYCVYILPMANKDGVARGRTRFNANGKDLNREWDKPADPVLAPENFALEKWLEEMIKAGKK
PDLAIELHNDGGGNLHVSRPPVDGLERYLARMARLEALLRRHTWFTEGSTKAEFRNPGTLGEGWLERFGI
DAAVYELNYNWIAGLNKAPSAKHWELLGSQLAKVFYVYFDKFK
>gnl|CDD|349486 cd18430, M14_ASTE_ASPA_like, Succinylglutamate desuccinylase/aspartoacylase; uncharacterized. A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD
LAVLGAVHGNETCGTRAVERLLAELPSGALQKGPVTLVPANERAYAEGVRFCEEDLNRVFPGDPDPDTYE
RRLANRLCPELEGHDVVLDLHSTHSGGQPFAILDYGDKASRRLARSVGIPKGWRVVYGRDLGYAHGGGKT
EVTGVTVECGYHDSEEAAEVAYRAILNT
>gnl|CDD|349384 cd18431, BRCT_DNA_ligase_III, BRCT domain of DNA ligase 3 (LIG3) and similar proteins. LIG3 (EC 6.5.1.1), also termed DNA ligase III, or polydeoxyribonucleotide synthase [ATP] 3, functions as heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents
LPDIFTGVKVYLPGSVEDDYKKLKRYFIAYDGDVVEEYDEEDATHVVVDRDDKLGNPSAKVVSPEWLWDC
IKKQKLVP
>gnl|CDD|349385 cd18432, BRCT_PAXIP1_rpt6_like, sixth BRCT domain of PAX-interacting protein 1 (PAXIP1), second BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins. PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. MDC1, also termed nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The family corresponds to the sixth BRCT domain of PAXIP1 and the second BRCT domain of MDC1
LFEGYTFYVTPNVKPPPEELKEIIEAAGGKVLKKLPTKRIEDDDPDTIVISCEEDRKLWKPLKKKGIPIY
SVEFILTGILRQKLD
>gnl|CDD|349386 cd18433, BRCT_Rad4_rpt3, third BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins. Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system which couples S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the third repeat
IFSGCTFYIHGFDDKKIQILRKHLLSNGGQVVSSLSELEADESKHRYVIVPHTNPPDELPPVSENAPLVT
EWWIERCLHSKRL
>gnl|CDD|349387 cd18434, BRCT_TopBP1_rpt5, fifth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins. TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the fifth BRCT domain
PLNGCVISVSQFTGTERDCLTHLAELLGAKVQDYFVRKANPSKGLLASTHLVLKEPEGSKYEAAKKWNLP
AVTKSWLFECARTGKKVPE
>gnl|CDD|349388 cd18435, BRCT_BRC1_like_rpt1, first (N-terminal) BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar proteins. Schizosaccharomyces pombe BRC1 is required for mitotic fidelity, specifically in the G2 phase of the cell cycle. It plays a role in chromatin organization. Members in this family contains six BRCT domains. This family corresponds to the fourth repeat
IFKHLAFYLDSPANAQRHGMARPKYEAAITKSFEEVEKLFIDNGGKILDLPYDPKLTHVILDDFDSPRVV
ELMKRTGKPRRLHLVKTKWIEDCVDENTLLDEEEYSP
>gnl|CDD|349389 cd18436, BRCT_BRC1_like_rpt2, second BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar proteins. Schizosaccharomyces pombe BRC1 is required for mitotic fidelity, specifically in the G2 phase of the cell cycle. It plays a role in chromatin organization. The family also includes Cryptococcus neoformans DNA ligase 4 (LIG4, also known as DNA ligase IV or polydeoxyribonucleotide synthase [ATP] 4), which is involved in dsDNA break repair, and plays a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologus end-joining. Members in this family contains six BRCT domains. This family corresponds to the second repeat
FSGVVITCSDLPSGDKEAIYGGVLALGGQYSDELTRDVTHLIALSPDGDKYKTALKRPELNIKIVLPHWF
DDCFK
>gnl|CDD|349390 cd18437, BRCT_BRC1_like_rpt3, third BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar proteins. Schizosaccharomyces pombe BRC1 is required for mitotic fidelity, specifically in the G2 phase of the cell cycle. It plays a role in chromatin organization. The family also includes Cryptococcus neoformans DNA ligase 4 (LIG4, also known as DNA ligase IV or polydeoxyribonucleotide synthase [ATP] 4), which is involved in dsDNA break repair, and plays a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologus end-joining. Members in this family contains six BRCT domains. This family corresponds to the third repeat. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group; it contains a conserved Trp, but not the Cys/Ser residue
KRFYLSADLNLGARRRKTISALIKGGGGKIVDTLADADIFIGRYRDGDEYLAASRSNKIVGNLSWLYHVL
ATGEWSSP
>gnl|CDD|349391 cd18438, BRCT_BRC1_like_rpt4, fourth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar proteins. Schizosaccharomyces pombe BRC1 is required for mitotic fidelity, specifically in the G2 phase of the cell cycle. It plays a role in chromatin organization. Members in this family contains six BRCT domains. This family corresponds to the fourth repeat
YKITITNYTGAARQYLEKLILALGATYTKNLKPDNTHLITASPEGEKYEAAKEWNIPIVNHLWLYDSY
>gnl|CDD|349392 cd18439, BRCT_BRC1_like_rpt6, sixth (C-terminal) BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar proteins. Schizosaccharomyces pombe BRC1 is required for mitotic fidelity, specifically in the G2 phase of the cell cycle. It plays a role in chromatin organization. The family also includes Cryptococcus neoformans DNA ligase 4 (LIG4, also known as DNA ligase IV or polydeoxyribonucleotide synthase [ATP] 4), which is involved in dsDNA break repair, and plays a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologus end-joining. Members in this family contains six BRCT domains. This family corresponds to the sixth repeat
EKKYGCTLAESLARAKANKGKLLKGYTVYLTPKVKGGVETFKSIVEANGGICNLLRAAKGKLGDGIAEKG
PVVLISTTKEKKLWPKFLKNAREGGKEPRVYSTDWLLDVVLRQELV
>gnl|CDD|349393 cd18440, BRCT_PAXIP1_rpt6, sixth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins. PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the sixth BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family
LFKGKYFYITPGVKPSPSVLKEIIESAGGKVEKKRPSLKKIMEKNNQGPPSYIIITCENDLHLCRDLFRK
NIDVYNAEFILTGVLRQKLD
>gnl|CDD|349394 cd18441, BRCT_MDC1_rpt2, second BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins. MDC1, also termed nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The family corresponds to the second BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family
LLEGYEIHVTPGVKPEPPQMKDIITCAGGTFLPSMPKTYKPQTVVISCPEDFPHCSPALKAGLPVVSAEF
LLTGILRQEAD
>gnl|CDD|349395 cd18442, BRCT_polymerase_mu, BRCT domain of DNA-directed DNA/RNA polymerase mu (polymerase mu) and similar proteins. Polymerase Mu (EC 2.7.7.7), also termed Pol mu, or terminal transferase, is a Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). It participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination. Polymerase Mu contains a BRCT domain
RFPGVCIFLVERRMGASRRAFLTGLARSKGFRVLDAYSSEVTHVVSEQNSAEEVVSWLERQMAAAPPACT
PPALLDISWFTESMGAGQPVPVECRHRL
>gnl|CDD|349396 cd18443, BRCT_DNTT, BRCT domain of DNA nucleotidylexotransferase (DNTT) and similar proteins. DNTT (EC 2.7.7.31), also termed terminal addition enzyme, or terminal deoxynucleotidyltransferase, or terminal transferase, is a template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. It is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. DNA nucleotidylexotransferase contains a BRCT domain
KFKDLVIFIVERKMGSTRRTFLMELARKKGFRVEDELSDSVTHIVAENNSGAEVLEWLQGQKLRDSSRLE
LLDISWFTECMGAGKPVEIEKRHRL
>gnl|CDD|350519 cd18444, BACK_KLHL1_like, BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins KLHL1, KLHL4 and KLHL5. This subfamily contains Kelch-like proteins: KLHL1, KLHL4 and KLHL5, all of which share high identity and similarity with the Drosophila kelch protein, a component of ring canals. Members of this subfamily contain a BTB domain and kelch repeat domains, characteristics of a kelch family protein. KLHL1 is a neuronal actin-binding protein that modulates voltage-gated CaV2.1 (P/Q-type) and CaV3.2 (alpha1H T-type) calcium channels
QLHPSNCLGIRSFADAQGCTDLLKVAHNYTMEHFMEVIQNQEFLLLPAEEVAKLLASDDLNVPSEETIFH
ALLLWVKHDLPERKKHLAKLLALIRLPLLTPQFLAD
>gnl|CDD|350520 cd18445, BACK_KLHL2_like, BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins, KLHL2 and KLHL3. This subfamily includes Kelch-like proteins, KLHL2 and KLHL3. KLHL2 is a novel actin-binding protein predominantly expressed in the brain. It plays a role in the reorganization of the actin cytoskeleton, and promotes growth of cell projections in oligodendrocyte precursors. Both KLHL2 and KLHL3 function as a component of an E3 ubiquitin ligase complex that mediates the ubiquitination of target proteins
LHPSNCLGIRAFADLHSCTDLLKYAQTYTEQHFSEVVKGEEFLLLSKEQVCELISSDDLTVPSEEKVFEA
VMSWVNHDPENRKEHLAELLEHVRLPLLSPEYLVQRVEEEELIK
>gnl|CDD|350521 cd18446, BACK_KLHL6, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 6 (KLHL6). KLHL6 is a BTB-kelch protein with a lymphoid tissue-restricted expression pattern. It belongs to the KLHL gene family, which is composed of an N-terminal BTB-POZ domain and four to six Kelch motifs in tandem. It is involved in B-lymphocyte antigen receptor signaling and germinal center formation
LHPENCVGILRLADAHSLESLKKQVQNYIIQNFSQVLNHEEFLELPVDILCHILKSDDLYVTEEEQVFET
VMRWVRYKESERLPLLPRVLENVRLPLLDPWYFVETVE
>gnl|CDD|350522 cd18447, BACK_KLHL7, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 7 (KLHL7). KLHL7 is a BTB-Kelch protein that constitutes a Cul3-based E3 ubiquitin ligase complex and is involved in the ubiquitination of target proteins for proteasome-mediated degradation. Mutations in KLHL7 cause autosomal-dominant retinitis pigmentosa
QVDASNCLGISVLAECLDCPELKATADDFIHQHFTEVYKTDEFLQLDVKRVTHLLNQDTLTVRAEDQVYD
AAVRWLKYDEPNRQPYMVDILAKVRFPL
>gnl|CDD|350523 cd18448, BACK_KLHL8, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 8 (KLHL8). KLHL8 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL8) ubiquitin ligase complex mediates ubiquitination and degradation of RAPSN
HLHPSNCLGVRTFAEQHNRVDLMKMADKYACDHFNEVVECEEFVSISAQHLEKLISSSDLNVESESQVYE
AVMKWVKHDPQHRKRHLDDLLSQVRLP
>gnl|CDD|350524 cd18449, BACK_KLHL9_13, BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins, KLHL9 and KLHL13. KLHL9 and KLHL13 (also termed BTB and kelch domain-containing protein 2, or BKLHD2) are substrate-specific adaptors of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates the ubiquitination of AURKB and controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis
VSLENCVEIGRIANTYHLTEVDKYVNDFILKNFPALLSTGDFVKLPFERLAFVLSSNSLKGCTELELFKA
ACRWLRHEDDRMQFAAKLMENIRFP
>gnl|CDD|350525 cd18450, BACK_KLHL10, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 10 (KLHL10). KLHL10 may be a substrate-specific adapter of a CUL3-based E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins during spermatogenesis
LTPENCIGIRKFARYYFCPELERKAYRYILRNFEEVAKDSEEFLELSCEELEDIIEDDELNVKEEEVVFE
AIVKWIDHDP
>gnl|CDD|350526 cd18451, BACK_KLHL11, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 11 (KLHL11). KLHL11 is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation
LNLSNCVAIHSLAHMYSLDQLALKAADMIRRNFHKVIQDEEFYTLPFHLVRDWLSDAEITVDSEEVLFEA
VLKWVQRNAEERERYFEE
>gnl|CDD|350527 cd18452, BACK_KLHL12, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 12 (KLHL12). KLHL12, also termed CUL3-interacting protein 1 (C3IP1), or DKIR, is a substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a negative regulator of Wnt signaling pathway and ER-Golgi transport
LDPSNCLGIRDFAETHNCVDLMQAAEVFSQKHFPEVVQHEEFMLLSQEEVEKLIKSDEIQVDSEEPVFEA
VLNWVKHDKEEREDYLPELLQYVRLPLLSPRYITDVVDAEPLIRCSLECRDLVDEAKKFHLRPELR
>gnl|CDD|350528 cd18453, BACK_KLHL14, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 14 (KLHL14). KLHL14, also termed protein interactor of Torsin-1A, or Printor, or protein interactor of torsinA, is a novel ATP-free form of torsinA-interacting protein implicated in dystonia pathogenesis
ISVQNYKQVCKIAALHGLEETKKLANKYLVEDVLLLNFEEMRAMLDSLPPPVESELALFQMSVLWLEHDR
ETRMQYAPDLMKRLRFALIPAPELVERVQSVD
>gnl|CDD|350529 cd18454, BACK_KLHL15, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 15 (KLHL15). KLHL15 is a substrate-specific adaptor for Cullin3 E3 ubiquitin-protein ligase complex that target the serine/threonine-protein phosphatase 2A (PP2A) subunit PPP2R5B for ubiquitination and subsequent proteasomal degradation, thus promoting exchange with other regulatory subunits. It also plays a key role in DNA damage response, favoring DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR), by targeting the DNA-end resection factor RBBP8/CtIP for ubiquitination and subsequent proteasomal degradation
ICLDNCAEIMRLLDDFSVNIEGVREKLDSFLLENFVPLMSRPDFLSYLSFEKLMSYLDNDHLSRFPEIEL
YEAVQAWLRHDRRRWRHTDTIIQNIRFCLMTPTNVFEK
>gnl|CDD|350530 cd18455, BACK_KLHL16_gigaxonin, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 16 (KLHL16). Gigaxonin, also termed Kelch-like protein 16 (KLHL16), may be a cytoskeletal component that directly or indirectly plays an important role in neurofilament architecture. It may also act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as tubulin folding cofactor B (TBCB), microtubule-associated protein MAP1B and glial fibrillary acidic protein (GFAP). Gigaxonin is mutated in giant axonal neuropathy
SAENCIGIRDFAERFSCPHVHYVATEYLETHFRDVSSTEEFLELSPEKLKELLSRDKLNVGNEEYIFEAV
LRWVRHDPEERKVHLKDLMSSCWRSGL
>gnl|CDD|350531 cd18456, BACK_KLHL17, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 17 (KLHL17). KLHL17, also termed actinfilin, is a substrate-recognition component of some cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes. It acts as a Cullin 3 (Cul3) substrate adaptor that links GluR6 to the E3 ubiquitin-ligase complex, and mediates the ubiquitination and subsequent degradation of GLUR6. It may play a role in the actin-based neuronal function
LDPSNCLGIRGFADTHSCSDLLKSAHKYVLQHFVEVSKTEEFMLLPLKQVLDLISSDSLNVPSEEEVYRA
VLSWVKHDVDGRRQHVPRLMKCVRLPLLSRDF
>gnl|CDD|350532 cd18457, BACK_KLHL18, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 18 (KLHL18). KLHL18 acts as a substrate-specific adaptor for the Cullin3 E3 ubiquitin-protein ligase complex that regulates mitotic entry and ubiquitylates Aurora-A
LHPNNCLGIRQFAETMMCSSLVDAANKYIQQHFIEVSKSEEFLALSKEEVLEILSRDELNVKSEEQVFEA
ALAWVKYDRENREEYLPELLSKVRLPLLRPQFLTDRV
>gnl|CDD|350533 cd18458, BACK_KLHL19_KEAP1, BACK (BTB and C-terminal Kelch) domain found in Kelch-like ECH-associated protein 1 (KEAP1). KEAP1, also termed cytosolic inhibitor of Nrf2 (INrf2), or Kelch-like protein 19 (KLHL19), is a redox-regulated substrate adaptor protein for a Cullin3-dependent ubiquitin ligase complex that targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression
QLDPSNCIGIANFAEQHGCTELHKKAREYIYMHFSEVSQSEEFFNLSPCQLVALISRDELNVRCESEVYN
AVIRWVKYDEENRRQYLEALL
>gnl|CDD|350534 cd18459, BACK_KLHL20, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 20 (KLHL20). KLHL20, also termed Kelch-like ECT2-interacting protein (KLEIP), or Kelch-like protein X, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. KLHL20 plays a role in actin assembly at cell-cell contact sites of Madin-Darby canine kidney cells. It also controls endothelial migration and sprouting angiogenesis
QLDPSNCLGIRAFADTHACRELLRIADKFTQHNFQEVMESEEFMLLPVNQLIDIISSDELNVRSEEQVFN
AVMAWVKYNIQERRPHLPQVLQHVRLPLLS
>gnl|CDD|350535 cd18460, BACK_KLHL21, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 21 (KLHL21). KLHL21 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for efficient chromosome alignment and cytokinesis. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of aurora B. KLHL21 targets IkappaB kinase-beta to regulate nuclear factor kappa-light chain enhancer of activated B cells (NF-kappaB) signaling negatively
LDVSNCLEMQDFAEAFACRGLAEAAKRFILRHIVELAKGEQFERLPLKRLLEYLSDDGLCVDKEETAYQI
ALRWVKADPKHRQHFWPELLQHVRLPFVRRF
>gnl|CDD|350536 cd18461, BACK_KLHL22, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 22 (KLHL22). KLHL22 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of Polo-like kinase 1 (PLK1) at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation
VDEENILDVYKLADLFHLTHLSEQLDSYILKNFPTFSRTETYRQLPLEKVYSLLSSNRLEVDSENEVYEG
ALLYHYTPEQVEKDQVSLQEPPKLLEAVRFPLME
>gnl|CDD|350537 cd18462, BACK_KLHL23, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 23 (KLHL23). KLHL23 is involved in tumorigenesis and resistance to anticancer drug treatment. It also associates with cone-rod dystrophy
LDIDNCLGMHSFAEFHVCPELEKESRRIILSRFEEVWQQEEFLELSKEKLLYILSRENLNVWKEEVLIEA
VVKWVAHDVEKRIECAYDLLSSIKLDLDEIYL
>gnl|CDD|350538 cd18463, BACK_KLHL24, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 24 (KLHL24). KLHL24, also called kainate receptor-interacting protein for GluR6 (KRIP6), or protein DRE1, is necessary to maintain the balance between intermediate filament stability and degradation, a process that is essential for skin integrity. KLHL24 is a component of the BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that mediates ubiquitination of KRT14 and controls its levels during keratinocyte differentiation
QLDPCNCLGIQKFADTHSLKQLFEKCKKFALENFVEVSQHEEFLELCKDELIEYISNDELVVPKEEEVFE
AVMRWVYH
>gnl|CDD|350539 cd18464, BACK_KLHL25_like, BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins, KLHL25 and KLHL37. The family includes KLHL25 and KLHL37. KLHL25, also called ectoderm-neural cortex protein 2 (ENC-2), is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for translational homeostasis. The BCR(KLHL25) ubiquitin ligase complex acts by mediating ubiquitination of hypophosphorylated EIF4EBP1 (4E-BP1). KLHL37, also called ectoderm-neural cortex protein 1 (ENC-1), or nuclear matrix protein NRP/B, or p53-induced gene 10 protein, is an actin-binding nuclear matrix protein that associates with p110(RB), and is involved in the regulation of neuronal process formation and in differentiation of neural crest cells
HPSNCLGMLLLSDAHQCQRLYELSWRMCLANFTTLRKTEDFLSLPKDKLLELVSSEELEVEDERLVYEAV
IGWIRYDLPRRHEVLPELLRSVRLALLP
>gnl|CDD|350540 cd18465, BACK_KLHL26, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 26 (KLHL26). KLHL26 is a kelch family protein encoded by gene klhl26, which is regulated by p53 via fuzzy tandem repeats
MSVETCLNIGQMATTFSLASLKESVDAFTFRHFLQIAEEEDFLHLPLERLVFFLQSNKLKNCSEIDLFRA
AIRWLQHDPSRRASASHVLCHIRFPLM
>gnl|CDD|350541 cd18466, BACK_KLHL27_IPP, BACK (BTB and C-terminal Kelch) domain found in intracisternal A particle-promoted polypeptide (IPP). IPP, also termed Kelch-like protein 27 (KLHL27), is an actin-binding protein that may play a role in organizing the actin cytoskeleton
IDPANCIGIFQFSEQIACHDLLEFTENYIHVHFLEVQSGEEFLGLTKDQLVKILRSEELSIEDEYQVFTA
AMEWILKDVGKRKKHVVEVLEPVRFPLLPPQRL
>gnl|CDD|350542 cd18467, BACK_KLHL28_BTBD5, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 28 (KLHL28). KLHL28, also termed BTB/POZ domain-containing protein 5 (BTBD5), belongs to the KLHL family. Its function remains unclear
LDPGNCIGISRFAETYGCHDLYLAANKYICQNFEDVCQTEEFFELTHAELDEIVSNDCLNVVTEETVFYA
LESWIKYDVQERQKYLAQLLHCVRLPLLS
>gnl|CDD|350543 cd18468, BACK_KLHL29_KBTBD9, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 29 (KLHL29). KLHL29, also termed Kelch repeat and BTB domain-containing protein 9 (KBTBD9), belongs to the KLHL family. Its function remains unclear. A nuclear receptor subfamily 5, group A, member 2 (NR5A2)-Kelch-like family member 29 (KLHL29) fusion transcript may participate in the origin or progression of some colon cancers
TPSNCLGIWALAEALQCTELHNMAKAYALQNFPDVARQEEILSISKDDIVEYLSHDSLNTKAEELVFETA
IKWLKKDPKNRKQHIAELLAVVRLPFIHPSYL
>gnl|CDD|350544 cd18469, BACK_KLHL30, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 30 (KLHL30). KLHL30 belongs to the KLHL family. Its function remains unclear. Differential expression of the KLHL30 gene has been observed in glioblastoma multiforme versus normal brain
QQIDATNCLGICEFGETHGCPEVAAKAWSFLLENFEAVSQEEEFLQLEKERLVACLGDDLLQVRDEQSRL
EAVLRWVGHDPQARAAHLPELLSLVHLSLLTDQY
>gnl|CDD|350545 cd18470, BACK_KLHL31_KBTBD1, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 31 (KLHL31). KLHL31, also termed BTB and kelch domain-containing protein 6, or Kelch repeat and BTB domain-containing protein 1, or Kelch-like protein KLHL, is a transcriptional repressor in MAPK/JNK signaling pathway that regulates cellular functions. Overexpression inhibits the transcriptional activities of both the TPA-response element (TRE) and serum response element (SRE)
INVENCMYVVNIAETYGLKNTKEAAQKFIRDNFIEFSETDQFLKLTFEQINEFLIDDDLQLPSEITAFQI
AMKWLDFDQKRVKYAADLLSNIRFGTIS
>gnl|CDD|350546 cd18471, BACK_KLHL32_BKLHD5, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 32 (KLHL32). KLHL32, also termed BTB and kelch domain-containing protein 5 (BKLHD5), belongs to the KLHL family. Its function remains unclear. KLHL32 SNPs may be associated with body mass index in individuals of African ancestry
LNSFNYLDLYKLADLFNLTLLEEAVVDFLVKHLSELLKSHPEEVLALPYRLLREVLKSDRLTSLSEEQIW
QLAVRWLEHNCRYQYMDELLQYVRFGLM
>gnl|CDD|350547 cd18472, BACK_KLHL33, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 33 (KLHL33). KLHL33 belongs to the KLHL family. Its function remains unclear. KLHL33 SNPs may be associated with prostate cancer risk
LSPANCLELWAFADAATLPRLAAAARAFALKHFAEVAASAAFLSLPLARLLELLRSDELEVAEEEAVFEA
AVRWL
>gnl|CDD|350548 cd18473, BACK_KLHL34, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 34 (KLHL34). KLHL34 belongs to the KLHL family. Its function remains unclear. The methylation status of KLHL34 cg14232291 may be a predictive candidate of sensitivity to preoperative chemoradiation therapy
LSPENCCFSANIAARFGLPDALKAAEKYIISNLWRLLASDADDAGLLELNLESLQAVLEADDIPRVKESR
LLTLVLEWLNQDESRLAYANALLSRIRYGLVPVEEL
>gnl|CDD|350549 cd18474, BACK_KLHL35, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 35 (KLHL35). KLHL35 belongs to the KLHL family. Its function remains unclear. Hypermethylation of KLHL35 is associated with hepatocellular carcinoma and abdominal aortic aneurysm
IGANNCLALLAAADALHCAPLQEHCIRVLLRDFAQAARHPSFLKLELQLVLELLADDSLAVRSEEVVLEA
ALRWVDADP
>gnl|CDD|350550 cd18475, BACK_KLHL36, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 36 (KLHL36). KLHL36 may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins
VSEENYLYLQELASIYSLERLDSFIDSFILQNFGTLSFTPDFLQNVSMQKLCQYLSSNQVQHECEHDLLQ
AALQWLTQSPERENEAYQVLSNIHFPLIPK
>gnl|CDD|350551 cd18476, BACK_KLHL38, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 38 (KLHL38). KLHL38 belongs to the KLHL family. Its function remains unclear. The klhl38 gene has recently been identified as a possible diapause (a temporary arrest of development during early ontogeny) gene, as it is significantly up-regulated during diapause. It may also be involved in chicken preadipocyte differentiation
LTPSNCLSMIRLSEILNCETLKKKAKDMALQCFPDVAASEDLKELCASELLDYLGDDELCGEEEQVFETL
MVWIRHDPKARKGYIHDLFKKVRLQYVHP
>gnl|CDD|350552 cd18477, BACK_KLHL40_like, BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins, KLHL40 and KLHL41. The family includes Kelch-like proteins, KLHL40 and KLHL41. KLHL40 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development. KLHL41 is a novel kelch related protein that is involved in pseudopod elongation in transformed cells
LCLGNCLAIFRLGLLLDCPRLAVSARDFICAHFTLVAKDEDFLGLSADELIAIISSDGLNVEKEEAVFEA
VMKWVREAKENRQKALPTVFESIRFRLLP
>gnl|CDD|350553 cd18478, BACK_KLHL42_KLHDC5, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 42 (KLHL42). KLHL42, also called Cullin-3-binding protein 9 (Ctb9), or Kelch domain-containing protein 5, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL42) E3 ubiquitin ligase complex mediates the ubiquitination and subsequent degradation of KATNA1. KLHL42 is involved in microtubule dynamics throughout mitosis
IRLPNCLELYRLAQVYGLRDLAEACLKFMATHYHPMLRRPEFRPLPSSLKQQLRERRLRGTPALVALGDF
LGTPLDPYQDEPWSMLRYDEVEQRWLPLANELP
>gnl|CDD|350554 cd18479, BACK_KBTBD2, BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing protein 2 (KBTBD2). KBTBD2, also called BTB and kelch domain-containing protein 1 (BKLHD1), plays an essential role in the regulating the insulin-signaling pathway. It is a BTB-Kelch family substrate recognition subunit of the Cullin-3-based E3 ubiquitin ligase, which targets p85alpha, the regulatory subunit of the phosphoinositol-3-kinase (PI3K) heterodimer, causing p85alpha ubiquitination and proteasome-mediated degradation
INAENCVRLLSFADLFSCEELKQSAKRMVEHKFTAVYHQEAFMQLSHDLLIDILSSDNLNVEKEETVREA
AMLWLEYNTESRSQYLSSVLSQIRID
>gnl|CDD|350555 cd18480, BACK_KBTBD3, BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing protein 3 (KBTBD3). KBTBD3, also termed BTB and kelch domain-containing protein 3 (BKLHD3), is a BTB-Kelch family protein. Its function remains unclear
LDLSNCLQLLSFAESYGSTRLLDHALEFVMQHFSLLSQSQEFLELNFEVLEKILEADELNVPDEEAVLKA
VLRWTKHDLEAR
>gnl|CDD|350556 cd18481, BACK_KBTBD4, BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing protein 4 (KBTBD4). KBTBD4, also termed BTB and kelch domain-containing protein 4 (BKLHD4), is a BTB-BACK-Kelch domain protein belonging to a large family of cullin-RING ubiquitin ligase adaptors that facilitate the ubiquitination of target substrates
VQVRNCLQVMWLADQHSDQELYTAAKHCAKTHLSQLHQTEEFLNLPLRLLTDIIKDGVPCSQNPTAAIEA
WINHNKEEREGFSETLTS
>gnl|CDD|350557 cd18482, BACK_KBTBD6_7, BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing proteins, KBTBD6 and KBTBD7. KBTBD6 and KBTBD7 are substrate adaptors of a cullin-3 RING ubiquitin ligase complex that mediates ubiquitylation and proteasomal degradation of T-lymphoma and metastasis gene 1 (TIAM1), a RAC1-specific guanine exchange factor (GEF), by cooperating with gamma-aminobutyric acid receptor-associated proteins (GABARAP). KBTBD7 may also act as a new transcriptional activator in mitogen-activated protein kinase (MAPK) signaling
LDLSNCAGILKFADAFDNRELKSKALAFIARNFQQLLAKEEELCELSLAQLKEVLMLDSLDVDSERKVCS
VAVQWIEANLKERAASAAEVLKCVRWQHF
>gnl|CDD|350558 cd18483, BACK_KBTBD8, BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing protein 8 (KBTBD8). KBTBD8, also called T-cell activation kelch repeat protein (TA-KRP), is a BTB-kelch family protein that is located in the Golgi apparatus and translocates to the spindle apparatus during mitosis. It acts as a substrate-specific adaptor for a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of neural crest specification. The BCR(KBTBD8) complex monoubiquitylates NOLC1 and its paralogue TCOF1, the mutation of which underlies the neurocristopathy Treacher Collins syndrome
LDPQNSIGVFIFADHYGHQELKERSQDYIRKKFLSVTKEQEFLHLTKDQLISILNSDDLNVEKEEHVYES
IIHWFEHEQSKREMHLPEIFAKCIRMP
>gnl|CDD|350559 cd18484, BACK_KBTBD11_CMLAP, BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing protein 11 (KBTBD11). KBTBD11, also termed chronic myelogenous leukemia-associated protein (CMLAP), or Kelch domain-containing protein 7B, or KLHDC7C, is a BTB-Kelch family protein. Its function remains unclear. A novel polymorphism rs11777210 in KBTBD11 is significantly associated with colorectal cancer risk; KBTBD11 may function as a tumor suppressor. KBTBD11 hypomethylation may also be a potential target for differentiating between the mostly fatal TCF3-HLF and curable TCF3-PBX1 pediatric acute lymphoblastic leukemia subtypes
LDLGNCYEVLTLAKKQRLNELREAAYKFMSDNYLQVLREPAVYGRLSGAERELILRRRLEAGRACLVVAE
LNDVFER
>gnl|CDD|350560 cd18485, BACK_KBTBD12, BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing protein 12 (KBTBD12). KBTBD12, also termed Kelch domain-containing protein 6 (KLHDC6), is a BTB-Kelch family protein. Its function remains unclear
MDASNCLGIYYFAKQIGAEDLSDRARKYLYQHFTEVCLHEEVLEIEAHQLLTLIKSDDLNVSREESILDL
VLRWVNHNRKSRVQHLVELLKQVRLELVSP
>gnl|CDD|350561 cd18486, BACK_KBTBD13, BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing protein 13 (KBTBD13). KBTBD13 is a muscle-specific protein. Autosomal dominant mutations may cause nemaline myopathy (NEM); these disease-associated mutations are located in conserved Kelch repeats and are predicted to disrupt the beta-propeller structure. KBTBD13 may act as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that functions as a muscle specific ubiquitin ligase, and thereby implicate the ubiquitin proteasome pathway in the pathogenesis of KBTBD13-associated NEM
INSDNCVLMYQAAATFGLLDLFHSAALFIRDIYSELREDLDCLPEDLLDYVESLVPSTYVAVGTHTPAPG
FLEDASRTVCYLDEEENTW
>gnl|CDD|350562 cd18487, BACK_BTBD1_like, BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing proteins, BTBD1 and BTBD2. This subfamily includes BTB/POZ domain-containing proteins BTBD1 and BTBD2, both of which are BTB-domain-containing Kelch-like proteins that interact with DNA topoisomerase 1 (Topo1), a key enzyme in cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta
LSSDNAFMLLTQARLFDEPQLASLCLETIDKNTAEALAAEGFTDIDLDTLCVVLERDTLGIRECKLFQAV
LRWAEAECQRQGLSVTPENQRKVLG
>gnl|CDD|350563 cd18488, BACK_BTBD3_like, BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing proteins, BTBD3 and BTBD6. This subfamily includes BTB/POZ domain-containing proteins BTBD3 and BTBD6, both of which are BTB-domain-containing Kelch-like proteins. BTBD3 controls dendrite orientation toward active axons in mammalian neocortex. BTBD6 is required for proper embryogenesis and plays an essential evolutionarily-conserved role during neuronal development
LSARNACVLLSQSRLFEEPELMQRCWEVIDAQAELALKSEGFTEIDYKTLESILRRETLNAKESVVFEAA
LRWAEAECQRRGLEPTPENKRKVLG
>gnl|CDD|350564 cd18489, BACK_BTBD7, BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 7 (BTBD7). BTBD7 is a crucial regulator that is essential for region-specific epithelial cell dynamics and branching morphogenesis. It has been implicated in various cancers. BTBD7 contains two BTB domains and a BACK domain
LSLDTLVGILRWSSQPHGSQWVHRQALHFLREEFSQIAQSPVLFELTKEYLIEALQSDFLQASELDILKA
VLKWGEHQLIKRMEEREPNLLSHTAHSV
>gnl|CDD|350565 cd18490, BACK_BTBD8, BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 8 (BTBD8). BTBD8 is a BTB-domain-containing Kelch-like protein that may play a role in developmental process. It may also act as a protein-protein adaptor in a transcription complex and thus may be involved in brain development
CLAGVLECLPLAHTFGLEDLYEKCLRWIAKHFAKVWSTKSFASLPPELQEKCYEALVSSLTIEN
>gnl|CDD|350566 cd18491, BACK_ABTB2_like, BACK (BTB and C-terminal Kelch) domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) and similar proteins. ABTB2, also called Bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins involved in a range of functions from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, with implications in Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homologue (PTEN). This subfamily also includes BTB/POZ domain-containing protein 11 (BTBD11), whose function is unclear
LDLDNVVAIYKHAKLYNAPELLAYCEGYFLQNMVQLLLENDSFRKLLFGKKLHGHDVLQGLQATLTQRIQ
SR
>gnl|CDD|350567 cd18492, BACK_BTBD16, BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 16 (BTBD16). BTBD16 is a BTB-domain-containing Kelch-like protein. Its function remains unclear. BTBD16 SNPs may be bipolar disorder (BD) genetic susceptibility variants exhibiting genetic background-dependent effects
IKSSTVCKFHRAACKYKQESLATACERWLELNLVPQLSSQIYLRDLPLELLHKILKSPRLFTFNEYSLYK
TLCYWVFLQLNPKVQLMPSHSTILTYF
>gnl|CDD|350568 cd18493, BACK_BTBD17, BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 17 (BTBD17). BTBD17, also termed galectin-3-binding protein-like, is a BTB-domain-containing Kelch-like protein. Its function remains unclear. It may be involved in hepatocellular carcinoma development and progression
SVNHAVSWLQYAKMCGHKELAEACLEFIAWNFEKVLKSPDWLNLDLDLLVSLLQSSDLVVEDEYTLFQAV
EKWL
>gnl|CDD|350569 cd18494, BACK_BTBD19, BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 19 (BTBD19). BTBD19 is a BTB-domain-containing Kelch-like protein. Its function remains unclear
SVETACEALQAAVTYGQDELKERCLAFIEEHTEEVFKTKGFHELSDEALSVILRSDKLRIDELDILKAVR
EWA
>gnl|CDD|350570 cd18495, BACK_GCL, BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster protein germ cell-less (GCL) and similar proteins. The GCL protein is a nuclear envelope protein highly conserved between the mammalian and Drosophila orthologs. Drosophila melanogaster GCL is a key regulator required for the specification of pole cells and primordial germ cell formation in Drosophila embryos. Both human germ cell-less protein-like 1 (GMCL1) and germ cell-less protein-like 1-like (GMCL1P1 or GMCL1L) may function in spermatogenesis. They may also be substrate-specific adaptors of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins
ISAKTVCSYYEAACMYGLTEVKKKCLEWLLRNLMTSQNVTLLRELSIELMEQLIASPNLFVMQVEMDVYT
LLKKWLFL
>gnl|CDD|350571 cd18496, BACK_LGALS3BP, BACK (BTB and C-terminal Kelch) domain found in lectin galactoside-binding soluble 3-binding protein (LGALS3BP). LGALS3BP, also called galectin-3-binding protein, or basement membrane autoantigen p105, or Mac-2-binding protein (MAC2BP/M2BP), or tumor-associated antigen 90K, promotes integrin-mediated cell adhesion. It may stimulate host defense against viruses and tumor cells
SFQTQLSLYEYALSTGDALLRGLCLQYLAWNCEALISSEAWLDLPWDQLKALLTRSDLVVPDELVLLKAL
EAWA
>gnl|CDD|350572 cd18497, BACK_ABTB1_BPOZ, BACK (BTB and C-terminal Kelch) domain found in ankyrin repeat and BTB/POZ domain-containing protein 1 (ABTB1). ABTB1, also called elongation factor 1A-binding protein, or Bood POZ containing gene type 1 (BPOZ-1), is an anti-proliferative factor that may act as a mediator of the phosphatase and tensin homologue (PTEN) growth-suppressive signaling pathway. It may play a role in developmental processes
LDEDNVIDVLRTARLFNLPRLEDQCTEFMAKNLEELVDDEEFAELVREDAASVKNRQETDSIPIIDDIRY
HL
>gnl|CDD|350573 cd18498, BACK_RCBTB1_2, BACK (BTB and C-terminal Kelch) domain found in RCC1 and BTB domain-containing proteins, RCBTB1 and RCBTB2. The RCC1-related guanine nucleotide exchange factor (GEF) family includes RCC1 and BTB domain-containing proteins, RCBTB1 and RCBTB2, both of which are chromosome condensation regulator-like guanine nucleotide exchange factors
ITVENAAFLYAAAIKYNAKELEEFCFKFAVNHLTAVVQTEAFSKLDESTLKDFIVKAAEAGAFK
>gnl|CDD|350574 cd18499, BACK_RHOBTB, BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing proteins (RhoBTB). RhoBTB proteins constitute a subfamily of atypical members within the Rho family of small guanosine triphosphatases (GTPases), which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline rich region, a tandem of 2 BTB domains, and a C-terminal BACK domain. In humans, the RhoBTB subfamily consists of 3 isoforms: RhoBTB1, RhoBTB2, and RhoBTB3. Orthologs are present in several other eukaryotes, such as Drosophila and Dictyostelium, but have been lost in plants and fungi
IDEDVIDLLELAQLHNADQLAAWCLHFISTNYNAFCKHRKEFKLLSPENQEYIEEHRWPPVWYLKELDEY
EKKLKE
>gnl|CDD|350575 cd18500, BACK_IBtk, BACK (BTB and C-terminal Kelch) domain found in inhibitor of Bruton tyrosine kinase (IBtk). IBtk is an inhibitor of Bruton's tyrosine kinase (Btk), thereby playing a role in B-cell development
ITLRNVAELLEFADIYNADQLKESCLQFICLNLETLLESRLLDNLDEDLLKELSKYYREM
>gnl|CDD|350576 cd18501, BACK_ANKFY1_Rank5, BACK (BTB and C-terminal Kelch) domain found in rabankyrin-5 (Rank-5). Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1), or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms
VNVRNCIRFYQTAEEIGASTLREYCSEIISTHWDDLTPEDFAKMSAPLLYRMFKSKTKHPLHAAIRLKRE
DVVFLYLIEFDSQLPGKLN
>gnl|CDD|350577 cd18502, BACK_NS1BP_IVNS1ABP, BACK (BTB and C-terminal Kelch) domain found in influenza virus NS1A-binding protein (NS1-BP). NS1-BP, also called NS1-binding protein, or Aryl hydrocarbon receptor-associated protein 3, or IVNS1ABP, is a novel protein that interacts with the influenza A virus nonstructural NS1 protein, which is relocalized in the nuclei of infected cells. It plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats. It also interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control
LTPENCIGIRSFAGRMNDSELLQKVDSYIQENIEEVAESKEFLKLPRLQIEVILESNQELESINERKLCQ
LVLEWVQRSIEEGGLDLDDLTEKVHMLYL
>gnl|CDD|350578 cd18503, BACK_calicin, BACK (BTB and C-terminal Kelch) domain found in calicin. Calicin is a basic cytoskeletal protein involved in the formation and maintenance of the highly regular organization of the postacrosomal perinuclear theca, the calyx of mammalian spermatozoa
LDRDNCLTALCLATTAGLKDLSDEIYDYIRDNFFDVSGTREFLQCPYDIFSRLLKDENLHVNNEDQVLLA
LLNWTEHN
>gnl|CDD|350579 cd18504, BACK_ARIA_like, BACK (BTB and C-terminal Kelch) domain found in plant ARM repeat protein interacting with ABF2 (ARIA) and similar proteins. ARIA is an ARM repeat protein that acts as a positive regulator of ABA response via the modulation of the transcriptional activity of ABF2, a transcription factor which controls ABA-dependent gene expression via the G-box-type ABA-responsive elements. ARIA is a novel abscisic acid signaling component. It negatively regulates seed germination and young seedling growth
DITLENVGEMYELSEAFHAMSLRHACILFILEHFEKLSSMPWFNSLVHRIIPEIREYFCRILTK
>gnl|CDD|350580 cd18505, BACK1_LZTR1, first BACK (BTB and C-terminal Kelch) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1). LZTR-1 is a Golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas
NVRNVLVALENASKLNLDQLKEHCLNFIVKESNYNQIVMSKEFEHLDQPLMVEIVRRRQ
>gnl|CDD|350581 cd18506, BACK2_LZTR1, second BACK (BTB and C-terminal Kelch) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1). LZTR-1 is a Golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas
VSFENVLQILEAADKIQALDMKKHALHIIVHHFPKVARLPKLRSLSRELLLDIIDALADHM
>gnl|CDD|350582 cd18507, BACK_GPRS_like, BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster serine-enriched protein (GPRS) and similar proteins. The family includes uncharacterized Drosophila melanogaster serine-enriched protein (GPRS) and similar proteins
NVDTVCALLASAERYDQYKCTKTLVQKVLEFVDKHGTDVLNLPEFLLLPEHVVRLILSRDSLGADEMTKF
QAALAWSRKY
>gnl|CDD|350583 cd18508, BACK_KEL_like, BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster ring canal kelch protein (KEL) and similar proteins. KEL, also termed kelch short protein, is a component of ring canals that regulates the flow of cytoplasm between cells. It binds actin and may be involved in the regulation of cytoplasm flow from nurse cells to the oocyte during oogenesis
DATNCLGIHEFADAHSCVELEEAAQNYIYQHFNEVIQGEEFLSLDHESLTELISSDRLNVPSEERVYEAA
VAWLKHD
>gnl|CDD|350584 cd18509, BACK_KLHL1, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 1 (KLHL1). KLHL1 is a neuronal actin-binding protein that modulates voltage-gated CaV2.1 (P/Q-type) and CaV3.2 (alpha1H T-type) calcium channels. It may play a role in organizing the actin cytoskeleton in brain cells. KLHL1 contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein
LLHPSNCLGIRAFADAQGCIELMKVAHSYTMENIMEVIRNQEFLLLPAEELHKLLASDDVNVPDEETIFH
ALMMWVKYDMQRRCSDLSMLLAYIRLPLLPPQLLAD
>gnl|CDD|350585 cd18510, BACK_KLHL4, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 4 (KLHL4). KLHL4 shares high identity and similarity with the Drosophila kelch protein, a component of ring canals. It contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein
QLHPSNCLGIRSFGDAQGCTELLKVAHSYTMEHFLEVIKNQEFLLLPASEIVKLLASDDINVPDEETIFQ
ALMMWVRHDLQNRQKDLGMLLSYIRLPLLPPQLLAD
>gnl|CDD|350586 cd18511, BACK_KLHL5, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 5 (KLHL5). KLHL5 shares high identity and similarity with the Drosophila kelch protein, a component of ring canals. It contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein. It is abundantly expressed in ovary, adrenal gland, and thymus
QLHPSNCLGIRSFADAQGCTDLHKVAHNYTMEHFMEVIRNQEFLLLPASEIAKLLASDDMNIPNEETILN
ALLSWVRHDVEQRRKDLSKLLAYIRLPLLAPQFLAD
>gnl|CDD|350587 cd18512, BACK_KLHL2_Mayven, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 2 (KLHL2). KLHL2, also called actin-binding protein Mayven, is a novel actin-binding protein predominantly expressed in the brain. It plays a role in the reorganization of the actin cytoskeleton, and promotes growth of cell projections in oligodendrocyte precursors. KLHL2 is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, such as NPTXR, leading most often to their proteasomal degradation
LHPTNCLGIRAFADMHACTELLNQANTYAEQHFSDVVLSEEFLNLGIEQVCSLIASDKLTISSEEKVFEA
VIAWVNHDKEVRQEHMAHLMEHVRLPLLSREYLVQRVEEETLVKNSSACKDYLIEAMKYH
>gnl|CDD|350588 cd18513, BACK_KLHL3, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 3 (KLHL3). KLHL3 serves as a substrate adapter in Cullin3 (Cul3) E3 ubiquitin ligase complexes. It is a component of an E3 ubiquitin ligase complex that regulates blood pressure by targeting With-No-Lysine (WNK) kinases for degradation
LHPTNCLGIRAFADVHTCTELLQQANAYAEQHFPEVMLGEEFLSLSLDQVCSLISSDKLTVSSEEKVFEA
VISWIKYDKEARLEHMAKLMEHVRLPLLPRDYLVQTVEEEALIKNNNTCKDFLIEAMKYH
>gnl|CDD|350589 cd18514, BACK_KLHL25_ENC2, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 25 (KLHL25). KLHL25, also called ectoderm-neural cortex protein 2 (ENC-2), is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for translational homeostasis. The BCR(KLHL25) ubiquitin ligase complex acts by mediating ubiquitination of hypophosphorylated EIF4EBP1 (4E-BP1)
LHPSNCLGMMLLSDAHQCRRLYELSWRMCLVHFETVRESEDFYSLSKDKLLDLISSDELEIEDEQVVFNA
VLQWVKYDLEKRKDYLPELLRNVRLALLP
>gnl|CDD|350590 cd18515, BACK_KLHL37_ENC1, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 37 (KLHL37). KLHL37, also called ectoderm-neural cortex protein 1 (ENC-1), or nuclear matrix protein NRP/B, or p53-induced gene 10 protein, is an actin-binding nuclear matrix protein that associates with p110(RB), and is involved in the regulation of neuronal process formation and in differentiation of neural crest cells
HPTNCLGMLLLSDAHQCTKLYELSWRMCLSNFQTICKTEDFLQLPKDMVVQLLSSEELETEDERLVYEAA
INWVNYDLKKRHCYLSELLQTVRLALLP
>gnl|CDD|350591 cd18516, BACK_KLHL40_KBTBD5, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 40 (KLHL40). KLHL40, also called Kelch repeat and BTB domain-containing protein 5, or sarcosynapsin, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development. Mutations in KLHL40 may cause severe autosomal-recessive nemaline myopathy
LCLSNCLAIFRLGLLLDCPRLAVAARDFICDRFQLIARDEDFLQLSPDELIAIISSDSLNVEKEEDVFEA
VMKWVGKDQEERTKALPVLLESIRFRLMP
>gnl|CDD|350592 cd18517, BACK_KLHL41_KBTBD10, BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 41 (KLHL41). KLHL41, also called Kel-like protein 23, or Kelch repeat and BTB domain-containing protein 10, or Kelch-related protein 1 (Krp1), or sarcosine, is a novel kelch related protein that is involved in pseudopod elongation in transformed cells. It is also involved in skeletal muscle development and differentiation. It regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils
LSVGNCLAIFRLGLLLDCPRLAVSARDFVSDRFEQISKEEDFLQLAPHELIAIISSDSLNVEKEELVFEA
VMKWVRTDKENRVKSLGEIFDCIRFRLMP
>gnl|CDD|350593 cd18518, BACK_SPOP, BACK (BTB and C-terminal Kelch) domain found in speckle-type POZ protein (SPOP). SPOP, also termed HIB homolog 1, or Roadkill homolog 1, is a novel nuclear speckle-type protein which serves as an adaptor of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and proteasomal degradation of target proteins, such as BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3
LSVENAAEILILADLHSADQLKTQAVDFINYHASDVMETSGWKSMVVSHPHLVAEAYRSLASAQCPFLGP
P
>gnl|CDD|350594 cd18519, BACK_SPOPL, BACK (BTB and C-terminal Kelch) domain found in speckle-type POZ protein-like (SPOPL). SPOPL, also termed HIB homolog 2, or Roadkill homolog 2, is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The complexes containing homodimeric SPOPL or the heterodimer formed by speckle-type POZ protein (SPOP) and SPOPL are less efficient than ubiquitin ligase complexes containing only SPOP
LSVENVADTLILADLHSAEQLKAQAIDFINRCSVLRQLGCKDGKNWNSNHATDIMETAGWKSMIHSHPHL
VAEAFRALASAQCPPFGIPRKRLKQS
>gnl|CDD|350595 cd18520, BACK_roadkill_like, BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster protein roadkill and similar proteins. Drosophila melanogaster protein roadkill, also termed Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor
LSVETAAEVLILADLHSADQLKAQAIDFINTHATDVMETAGWKSMIRTHPHLLAEAFRALATQQIPPIGP
PRKR
>gnl|CDD|350596 cd18521, BACK_Tdpoz, BACK (BTB and C-terminal Kelch) domain found in TD and POZ domain-containing proteins, Tdpoz1-4. TDPOZ is a family of bipartite animal and plant proteins that contain a tumor necrosis factor receptor-associated factor (TRAF) domain (TD) and a POZ/BTB domain. TDPOZ proteins may be nuclear scaffold proteins probably involved in transcription regulation in early development and other cellular processes. This subfamily contains only mammalian members. Plant TDPOZ proteins contain a MATH domain at the N-terminal region and are named "BTB/POZ and MATH domain-containing proteins (BPM)", and are not inlcuded in this subfamily
LSVKNAAHTLILADLHSTEKLKTQALDFIAVHASEVSETSEWKSMVESHPHLVAEAFHSLASAQCSF
>gnl|CDD|350597 cd18522, BACK_BTBD1, BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 1 (BTBD1). BTBD1, also called Hepatitis C virus NS5A-transactivated protein 8 or HCV NS5A-transactivated protein 8, is a BTB-domain-containing Kelch-like protein specifically expressed in skeletal muscle. It interacts with DNA topoisomerase 1 (Topo1), a key enzyme in cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. It may serve as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins
LRADNAFMLLTQARLFDEPQLASLCLDTIDKSTMDAISAEGFTDIDLDTLCAVLERDTLSIRESRLFGAV
VRWAEAECQRQQLPVTSENKQKVLGKALSLIRFPLMT
>gnl|CDD|350598 cd18523, BACK_BTBD2, BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 2 (BTBD2). BTBD2 is a BTB-domain-containing Kelch-like protein that interacts with DNA topoisomerase 1 (Topo1), a key enzyme in cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta
LRADNAFMLLTQARLFDEPQLASLCLENIDKNTSDAINAEGFTDIDLDTLVAVLERDTLGIREVRLFNAV
VRWAEAECQRQQLQVTPENKRKVLGKALSLIRFPLM
>gnl|CDD|350599 cd18524, BACK_BTBD3, BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 3 (BTBD3). BTBD3 is a BTB-domain-containing Kelch-like protein that controls dendrite orientation toward active axons in mammalian neocortex
LSAKNACVLLSQSCLFEEPDLTQRCWEVIDAQAELALKSEGFCDIDFQTLESILRRETLNAKEIVVFEAA
LNWAEVECQRQELQPTIENKRKVLG
>gnl|CDD|350600 cd18525, BACK_BTBD6, BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 6 (BTBD6). BTBD6, also called lens BTB domain protein, is a BTB-domain-containing Kelch-like protein that is required for proper embryogenesis and plays an essential evolutionarily-conserved role during neuronal development
LEAKNACVLLSQSRLFEEPELTQRCWEVIDAQAELALKSEGFCEIDQQTLEIILTRETLNTKEVVVFEAV
LNWAEAECKRQGLPPTARNKRNVLG
>gnl|CDD|350601 cd18526, BACK_ABTB2, BACK (BTB and C-terminal Kelch) domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2). ABTB2, also called Bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins with functions ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, with implications in Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homologue (PTEN)
INLENSVSIYKYAKIHNAPELASFCEGFFLKNMKALLEQDSFRQLIYGRNSKVQGLDPLQDLQVTLAKRM
HSIYITSRV
>gnl|CDD|350602 cd18527, BACK_BTBD11, BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 11 (BTBD11). BTBD11, also termed ankyrin repeat and BTB/POZ domain-containing protein BTBD11, is a BTB-domain-containing Kelch-like protein. Its function remains unclear. The BTBD11 gene has been identified as an all-trans retinoic acid-responsive gene that may play a role in neural development
INTENCVDIYNHAKFLGATELSSYCEGYFLKNMVLLIENEAFKQLLYDKNGESPGQDVLQDLERTLATRI
QSIHLSSSKGSIV
>gnl|CDD|350603 cd18528, BACK_RCBTB1, BACK (BTB and C-terminal Kelch) domain found in RCC1 and BTB domain-containing protein 1 (RCBTB1). RCBTB1, also called chronic lymphocytic leukemia deletion region gene 7 protein (CLLD7), or CLL deletion region gene 7 protein, or regulator of chromosome condensation and BTB domain-containing protein 1, or E4.5, is a novel chromosome condensation regulator-like guanine nucleotide exchange factor (GEF) that may be involved in cell cycle regulation by chromatin remodeling. It may also function as a tumor suppressor that regulates pathways of DNA damage/repair and apoptosis. Moreover, RCBTB1 acts as a putative substrate adaptor for a cullin3 (CUL3) E3 ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Biallelic mutations in RCBTB1 may cause isolated and syndromic retinal dystrophy
GITVENAFSLLSAAVRYDAEDLEEFCFKFCVNHLTEVTQTAAFWQMDGNLLKEFIAKASKCGAFKN
>gnl|CDD|350604 cd18529, BACK_RCBTB2, BACK (BTB and C-terminal Kelch) domain found in RCC1 and BTB domain-containing protein 2 (RCBTB2). RCBTB2, also called chromosome condensation 1-like (CHC1-L), or RCC1-like G exchanging factor, or regulator of chromosome condensation and BTB domain-containing protein 2, is a chromosome condensation regulator-like guanine nucleotide exchange factor (GEF) protein for the Ras-related GTPase Ran
ISEENAIALLSAAVKYEAQDLEEFCFKFCINHMTVVTQTQAFADMDHDLLKNFISKASKVGAFKN
>gnl|CDD|350605 cd18530, BACK_RHOBTB1, BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1). RhoBTB1 is an atypical member of the Rho GTPase family of signaling proteins, which is characterized by containing a carboxyl terminal extension that harbors two BTB domains and a BACK domain and is capable of assembling cullin 3-dependent ubiquitin ligase complexes. It functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. RhoBTB1 also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex
IDGEVLTYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSPENQEYFERHRWPPVWYLKEEDH
YQRVKKEREKEDVALHKHHSKRKWCFWNSS
>gnl|CDD|350606 cd18531, BACK_RHOBTB2, BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 2 (RhoBTB2). RhoBTB2, also called Deleted in breast cancer 2 gene protein (DBC2), or p83, is an atypical member of the Rho GTPase family of signaling proteins, which is characterized by containing a carboxyl terminal extension that harbors two BTB domains and a BACK domain and is capable of assembling cullin 3-dependent ubiquitin ligase complexes. It functions as a tumor suppressor that regulates the expression of the methyltransferase METTL7A. RhoBTB2 also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex
IDGQVLVYLELAQFHNAKQLADWCLHHICTNYNSVCRKFPRDMKAMSPENQEHFEKHRWPPVWYLKEEDR
YLRSKKEREKEEELLRKQHPKRKWCFW
>gnl|CDD|350607 cd18532, BACK_RHOBTB3, BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 3 (RhoBTB3). RhoBTB3 is an atypical member of the Rho GTPase family of signaling proteins, which is characterized by containing a carboxyl terminal extension that harbors two BTB domains and a BACK domain and is capable of assembling cullin 3-dependent ubiquitin ligase complexes. It is a Golgi-associated Rho-related ATPase that regulates the S/G2 transition of the cell cycle by targeting cyclin E for ubiquitylation. RhoBTB3 is involved in vesicle trafficking and in targeting proteins for degradation in the proteasome. It binds directly to Rab9 GTPase and functions with Rab9 in protein transport from endosomes to the trans Golgi network. It also promotes proteasomal degradation of Hypoxia-inducible factor alpha (HIFalpha) by facilitating hydroxylation and ubiquitination
TSLSVVSLLRKAKFHNADQLSTWLLHFIASNYLIFSQKPEFQDLSAEERDFVETHRWPSSMYLQELAEYR
QHIHSRKSRCSVM
>gnl|CDD|350509 cd18533, PTP_fungal, fungal protein tyrosine phosphatases. This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization
YINASYITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEY
GDLTVELVSEEENDDGGFIVREFELSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSAS
LDPPIIVHCSAGVGRTGTFIALDSLLDELKRGLSDSQDLEDSEDPVYEIVNQLRKQRMSMVQTLRQYIFL
YD
>gnl|CDD|350510 cd18534, DSP_plant_IBR5-like, dual specificity phosphatase domain of plant IBR5-like protein phosphatases. This subfamily is composed of Arabidopsis thaliana INDOLE-3-BUTYRIC ACID (IBA) RESPONSE 5 (IBR5) and similar plant proteins. IBR5 protein is also called SKP1-interacting partner 33. The IBR5 gene encodes a dual-specificity phosphatase (DUSP) which acts as a positive regulator of plant responses to auxin and abscisic acid. DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. IBR5 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs. It has been shown to target MPK12, which is a negative regulator of auxin signaling
PTEILPGFLYLGSYDNASRAELLKAQGITRILNTVPDCQNLYKNSFTYHVLSEEKTVPFAEAVDFIEQCR
KDKARVLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRPSINLSPAVAKQLQEF
>gnl|CDD|350511 cd18535, PTP-IVa3, protein tyrosine phosphatase type IVA 3. Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), also known as protein-tyrosine phosphatase of regenerating liver 3 (PRL-3), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It exerts its oncogenic functions through activation of PI3K/Akt, which is a key regulator of the rapamycin-sensitive mTOR complex 1. PRL-3 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation
NRPAPVEVCYKNMRFLITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGA
PPPGKVVEDWLSLLKTKFCEDPGCCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSK
QLTYLEKYRPKQRL
>gnl|CDD|350512 cd18536, PTP-IVa2, protein tyrosine phosphatase type IVA 2. Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), also known as protein-tyrosine phosphatase of regenerating liver 2 (PRL-2), stimulates progression from G1 into S phase during mitosis and promotes tumors. It regulates tumor cell migration and invasion through an ERK-dependent signaling pathway. Its overexpression correlates with breast tumor formation and progression. PRL-2 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation
MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIQVLDWPFDDG
APPPNQIVDDWLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNS
KQLLYLEKYRPKMRL
>gnl|CDD|350513 cd18537, PTP-IVa1, protein tyrosine phosphatase type IVA 1. Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation
MARMNRPAPVEITYKNMRFLITHNPTNATLNKFIEELKKYGVTTVVRVCEATYDTTLVEKEGIQVLDWPF
DDGAPPSNQIVDDWLNLLKVKFREEPGCCIAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGA
FNSKQLLYLEKYRPKMRLRFKDSNGHR
>gnl|CDD|350514 cd18538, PFA-DSP_unk, unknown subfamily of atypical dual-specificity phosphatases from fungi. This uncharacterized subfamily belongs to the plant and fungi atypical dual-specificity phosphatases (PFA-DSPs) group of atypical DSPs that present in plants, fungi, kinetoplastids, and slime molds. They share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The PFA-DSP group is composed of active as well as inactive phosphatases. This unknown subgroup contains the conserved the CxxxxxR catalytic motif present in active cysteine phosphatases
GLPPNFGVVVPGVYRSSFPKPENFGFLKSLGLRTILTLVQEEYSPEFLNFLRENGIQHFHIAMLGNKDPK
VSIPDHTMNRILRIILDKENHPILVHCNKGKHRTGCVIACFRKLQGWDVENVLEEYLSYAHPKSRDLDEE
YIENF
>gnl|CDD|349786 cd18539, SRP_G, GTPase domain of signal recognition particle protein. The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain
TVILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDI
AKRALEKAKEEGFDVVIVDTAGRLHIDEELMDELKEIKEVLNPDEVLLVVDAMTGQDAVNVAKAFNERLG
LTGVVLTKLDGDARGGAALSIRHVTGKPIKFIGVGEKIEDLEPFHPDRMASRI
>gnl|CDD|349984 cd18540, ABC_6TM_exporter_like, Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins. This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIE
MGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLIL
NWKLALIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKEL
TEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLAR
VLAELQSAQASAERV
>gnl|CDD|349985 cd18541, ABC_6TM_TmrB_like, Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins. This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRR
IEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISP
KLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNE
EYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVI
NLIQRGAASLKRI
>gnl|CDD|349986 cd18542, ABC_6TM_YknU_like, Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKV
AYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWK
LTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEE
YRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLIN
DMSRASASAERI
>gnl|CDD|349987 cd18543, ABC_6TM_Rv0194_D1_like, Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins. This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGV
EHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVVMLVLSPPL
ALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRL
RATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAM
AQRARAAAERV
>gnl|CDD|349988 cd18544, ABC_6TM_TmrA_like, Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins. This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQ
RIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLN
WRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEIN
QEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEK
FNILQSAMASAERI
>gnl|CDD|349989 cd18545, ABC_6TM_YknV_like, Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQR
ILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNV
RLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNR
ENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFY
NQLQSAMASAERI
>gnl|CDD|349990 cd18546, ABC_6TM_Rv0194_D2_like, Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins. This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERL
LYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPR
LALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDD
YRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFD
SYQQARAALEKI
>gnl|CDD|349991 cd18547, ABC_6TM_Tm288_like, Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMA
RVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMM
LYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEF
DEINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQ
ISQQINSLQSALAGAERV
>gnl|CDD|349992 cd18548, ABC_6TM_Tm287_like, Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGF
GRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPK
LALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDD
LTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFV
MLPRASASAKRI
>gnl|CDD|349993 cd18549, ABC_6TM_YwjA_like, Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins. This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
KKLFFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMG
ARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTI
NVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEG
NDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVN
FTEQYQKGMAGFERF
>gnl|CDD|349994 cd18550, ABC_6TM_exporter_like, Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins. This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGV
MYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWR
LALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVSGALLVKLFGREDDEAARFARRS
RELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNI
QVDLMTSLALFERI
>gnl|CDD|349995 cd18551, ABC_6TM_LmrA_like, Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins. This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLD
LRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTL
VTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYR
AGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQ
KALGALERI
>gnl|CDD|349996 cd18552, ABC_6TM_MsbA_like, Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins. The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRV
VRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWK
LTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANER
LRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNA
NLQRGLAAAERI
>gnl|CDD|349997 cd18553, ABC_6TM_PglK_like, Six-transmembrane helical domain of the ABC transporter PglK and similar proteins. This group represents the transmembrane (TM) domain of an active lipid-linked oligosaccharides flippase PglK (protein glycosylation K), which is a homodimeric ABC transporter that flips a lipid-linked oligosaccharide that serves as a glycan donor in N-linked protein glycosylation. Pglk mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. This TM subunit exhibits the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter
LLFSIFVSLIETIGISAIMPFISVASNFSLILSNKYYKFIYNFFGFSSPVNFVIFFGIILIGFYIFRSLY
NIFYTYLLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNLSQVIQSFLFILSEIFV
ILFIYSLLLYVNWKITLVLTLFLGLNVFFITKIVSKKIKKQGKKREESQKKFYKILSETFGNFKIIKLKS
NEKEILKNFSQASLKFAKANIINQTLQTVPRLILETIGFSLLILIVLYILYKYSDASAVLPIISMYALAL
YRLLPSVNRILSSYNQILYY
>gnl|CDD|349998 cd18554, ABC_6TM_Sav1866_like, Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins. This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs
IIITIVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTLDEKVYKLFTIIGIMFFIFLILRPPVEYYRQYFA
QWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICI
MLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQ
FDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLR
RLVNSFTTLTQSFASMDRV
>gnl|CDD|349999 cd18555, ABC_6TM_T1SS_like, Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins. This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides
KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQ
TKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYS
PLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLF
KKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINS
YNQFILLKSYLERL
>gnl|CDD|350000 cd18556, ABC_6TM_McjD_like, Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins. This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter
KLLFFSILFISLLSSILISISPVILAKITDLLTSSSSDSYNYIVVLAALYVITISATKLLGFLSLYLQSS
LRVELIISISSSYFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIVVIL
SSGDYFVAALFLLYAVLFVINNTIFTKKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRY
EATLTNDRNSQKRYWKLTFKMLILNSLLNVILFGLSFFYSLYGVVNGQVSIGHFVLITSYILLLSTPIES
LGNMLSELRQSVHSLAGF
>gnl|CDD|350001 cd18557, ABC_6TM_TAP_ABCB8_10_like, Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10. This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins
GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVAR
LRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTL
VLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYR
LARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIM
KALGASERV
>gnl|CDD|350002 cd18558, ABC_6TM_Pgp_ABCB1, Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins. P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells
MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLNSSAGPFEKLEEEMTLYAYYYLIIGA
IVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVI
FQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRT
VIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLT
VFFSVLIGAFSAGQQVPSIEAFANARGAAYHI
>gnl|CDD|350003 cd18559, ABC_6TM_ABCC, Six-transmembrane helical domain of the ABC transporters, subfamily C. This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides
SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFAS
RAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMA
AVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNEL
AYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNI
VAAEVSLERS
>gnl|CDD|350004 cd18560, ABC_6TM_ATM1_ABCB7_HMT1_ABCB6, Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily. This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster
SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAY
RELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAW
LALIVFLSVLLYGVFTIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKE
YQKSSVKVQASLSLLNVGQQLIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYR
MIIQSLTDMENL
>gnl|CDD|350005 cd18561, ABC_6TM_AarD_CydDC_like, Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs)
SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQH
LRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVAL
ILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQ
ATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGY
QGISAADSI
>gnl|CDD|350006 cd18562, ABC_6TM_NdvA_beta-glucan_exporter_like, Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins. This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs
ALGLALANVALAGVQFAEPVLFGRVVDALSSGGDAFPLLALWAALGLFSILAGVLVALLADRLAHRRRLA
VMASYFEHVITLPLSFHSQRGSGRLLRIMLRGTDALFGLWLGFFREHLAALVSLIVLLPVALWMNWRLAL
LLVVLAAVYAALNRLVMRRTKAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRLLA
AQYPVLNWWALASVLTRAASTLTMVAIFALGAWLVQRGELTVGEIVSFVGFATLLIGRLDQLSGFINRLF
MQAPKLQEF
>gnl|CDD|350007 cd18563, ABC_6TM_exporter_like, Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins. This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARL
GERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFS
LNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDE
ANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLS
RLNNWITRALTSAERI
>gnl|CDD|350008 cd18564, ABC_6TM_exporter_like, Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins. This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLGLAPLLGPDPLALLLLAAAALVGIALLRGLA
SYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLL
TLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFG
REEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYL
KNLYKPVRDLAKLTGRIAKASASAERV
>gnl|CDD|350009 cd18565, ABC_6TM_exporter_like, Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins. This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFLPLVPASLGPADPRGQLWLLGGLTVAAFLLESLF
QYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVV
TVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFT
AEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGPPLFTGTLTVGTLV
TFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV
>gnl|CDD|350010 cd18566, ABC_6TM_PrtD_LapB_HlyB_like, Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins. This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion
RPLLPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIG
ARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLG
GKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQ
ANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGL
WTRFQQVRVAVRRL
>gnl|CDD|350011 cd18567, ABC_6TM_CvaB_RaxB_like, Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins. This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium
KRALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLS
TSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYS
PKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLL
VDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDK
LFELRMLRLHLERL
>gnl|CDD|350012 cd18568, ABC_6TM_HetC_like, Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins. This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion
RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFA
NRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYN
LQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKF
AKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGL
WDELQETRISVERL
>gnl|CDD|350013 cd18569, ABC_6TM_NHLM_bacteriocin, Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters. This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion
RSALLFVVLAGLLLVIPGLVIPVFSRIFIDDILVGGLPDWLRPLLLGMALTALLQGLLTWLQQYYLLRLE
TKLALSSSSRFFWHVLRLPVEFFSQRYAGDIASRVQSNDRVANLLSGQLATTVLNLVMAVFYALLMLQYD
VPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESDFFSRWAGYQ
AKVLNAQQELGRTNQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGL
GGTLQEMRGDMERL
>gnl|CDD|350014 cd18570, ABC_6TM_PCAT1_LagD_like, Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters. This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins
KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLS
QKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYN
WKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKF
SKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINL
QPKIQEAKVAADRL
>gnl|CDD|350015 cd18571, ABC_6TM_peptidase_like, Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins. This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion
KKLILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNFIYLILIAQLVLFLGSTSIEFIRSWILLHIS
SRINISIISDFLIKLMRLPISFFDTKMTGDILQRINDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYN
LTIFLIFLIGSVLYILWILLFLKKRKKLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQ
AKLFKINIKSLKLDQYQQIGALFINQLKNILITFLAAKLVIDGEITLGMMLAIQYIIGQLNSPIEQLIGF
IQSLQDAKISLERL
>gnl|CDD|350016 cd18572, ABC_6TM_TAP, Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing. This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation
AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRR
LRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTL
LAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALK
LSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLM
QAVGAAEKV
>gnl|CDD|350017 cd18573, ABC_6TM_ABCB10_like, Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins. This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane
ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGE
RIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYIS
PKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKV
DEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSF
YSELMKGLGASSRL
>gnl|CDD|350018 cd18574, ABC_6TM_ABCB8_like, Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins. This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter
AVLSALAAALVNIQIPLLLGDLVNVISRSLKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVG
ERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLI
SPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEE
VEKAAKLNEKLGLGIGIFQGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSV
LFGQYVKGKSAGARV
>gnl|CDD|350019 cd18575, ABC_6TM_bac_exporter_ABCB8_10_like, Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10. This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs
ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVAD
LRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTL
LVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFA
AALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQ
RAAGAAERL
>gnl|CDD|350020 cd18576, ABC_6TM_bac_exporter_ABCB8_10_like, Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10. This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs
GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVAD
LRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTL
LMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVK
LALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQ
KALGASERV
>gnl|CDD|350021 cd18577, ABC_6TM_Pgp_ABCB1_D1_like, Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins. P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells
LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTAC
WTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFI
IAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIK
RYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSL
GQIAPNLQAFAKARAAAAKI
>gnl|CDD|350022 cd18578, ABC_6TM_Pgp_ABCB1_D2_like, Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins. P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells
LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYF
LQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIV
TLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLT
LEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMAL
IFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI
>gnl|CDD|350023 cd18579, ABC_6TM_ABCC_D1, Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C. This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs
LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRV
RSALSSLIYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWA
ALAGLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKE
LKALRKFGYLRALNSFLFFSTPVLVSLATFATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLI
EALVSLKRI
>gnl|CDD|350024 cd18580, ABC_6TM_ABCC_D2, Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C. This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs
VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRA
SRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPY
FLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDA
SQRAFYLLLAVQRWLGLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTEL
ETSMVSVERILEYT
>gnl|CDD|350025 cd18581, ABC_6TM_ABCB6, Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial. This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia
CLLLLAAGRVVNVLVPILYKKIVDSLTPDSADSPLAFPWALILLYVFLKFLQGGGSGSVGLLSNLRSFLW
IPVQQFTTREISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIY
FAIAFNPWFGLIVFVTMALYLILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVE
RYRRAIDDYQVAEWKSNASLNLLNTAQNLIITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPL
NFFGTYYRMIQQSFIDMENM
>gnl|CDD|350026 cd18582, ABC_6TM_ATM1_ABCB7, Six-transmembrane helical domain of the Atm1/ABC7 transporters. This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia
ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAV
RRLALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWS
YALITLVTVALYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAK
YEKAAVKSQTSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYR
EIRQSLIDMEKL
>gnl|CDD|350027 cd18583, ABC_6TM_HMT1, Six-transmembrane helical domain of the heavy metal tolerance protein. This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria
CFLCLLAERVLNVLVPRQLGIIVDSLSGGSGKSPWKEIGLYVLLRFLQSGGGLGLLRSWLWIPVEQYSYR
ALSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQGSSINDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMG
LIVAVVMVLYVWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQ
KAERKYLFSLNLLNAVQSLILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSI
QSDLIDAERL
>gnl|CDD|350028 cd18584, ABC_6TM_AarD_CydD, Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs)
AVLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKA
ELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSA
LILLVTAPLIPLFMILIGKAAQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYR
RRTMKVLRVAFLSSAVLEFFATLSIALVAVYIGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHAR
ADGLAAAERL
>gnl|CDD|350029 cd18585, ABC_6TM_CydC, Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter. The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs)
GLLTLLASIGLLALSGWFISAAALAGLAAPTFNYFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNL
RVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALI
LLAGLLLAGVVIPLLFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIK
EQRRLARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLG
ETRAAARRLF
>gnl|CDD|350030 cd18586, ABC_6TM_PrtD_like, Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins. This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
RRVFVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVG
LRLDVELGRRVFRAVLELPLESRPSGYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPL
GWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAET
LELQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELTIGALIAASILSGRALAPIDQLVGAWKQ
LSAARQAYERL
>gnl|CDD|350031 cd18587, ABC_6TM_LapB_like, Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins. This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein
RRIYRDVLLAALLINLFALASPLFVMNVYDRVVPNNAIETLWVLAIGVLIALLFDFILKLLRAYFIDVAG
KRADVILSSRLFERVLGLRLEARPASVGSFANNLREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGG
PLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVA
ALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLL
TRYQQARTALKSL
>gnl|CDD|350032 cd18588, ABC_6TM_CyaB_HlyB_like, Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins. This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein)
KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTT
NRIDAELGARLFRHLLRLPLSYFESRQVGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYS
PTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELL
ARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQL
WQDFQQAKVSVERL
>gnl|CDD|350033 cd18589, ABC_6TM_TAP1, Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1). This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation
VLGLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSR
LQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLAL
LTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYR
LNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVM
KAVGSSEKI
>gnl|CDD|350034 cd18590, ABC_6TM_TAP2, Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2). This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation
AFLFLTLAVICETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLR
LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTL
LTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYN
LKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDML
SNVGAAAKV
>gnl|CDD|350035 cd18591, ABC_6TM_SUR1_D1_like, Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2. This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion
LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVSYVTVEEFFSNGYVLAVILFLALLLQA
TFSQASYHIVIREGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWA
IPLKIIVGLILLYLKLGVSALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLK
LYAWENIFLDKIQEARRKELKLLLKDAVYWSLMTFLTQASPILVTLVTFGLYPYLEGEPLTAAKAFSSLA
LFNQLTVPLFIFPVVIPILINAVVSTRRL
>gnl|CDD|350036 cd18592, ABC_6TM_MRP5_8_9_D1, Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9. This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0)
FSILLLLISLIFGFIGPTILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRL
RGAVLGLLYKKILRLRSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWAL
LGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERK
ILEKAGYLQSISISLAPIVPVIASVVTFLAHVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEA
KVALQRI
>gnl|CDD|350037 cd18593, ABC_6TM_MRP4_D1_like, Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins. This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0)
LLGIFLFLEEAIRVVQPIFLGKLIRYFEGNGSSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMR
LRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGW
SCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRK
EIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILTAERVFVTMALYNAVRLTMTLFFPFAIQF
GSELSVSIRRI
>gnl|CDD|350038 cd18594, ABC_6TM_CFTR_D1, Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator. This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent
LLGILLFLEESLKIVQPLLLGRLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQL
RIALSSLIYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPS
SLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKE
LKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTARKVFTVISLLNALRMTITRFFPESIQTL
SESRVSLKRIQ
>gnl|CDD|350039 cd18595, ABC_6TM_MRP1_2_3_6_D1_like, Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6. This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0)
LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIR
TALTSAIYRKALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSV
LAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKEL
KLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNL
VQASVSLKRL
>gnl|CDD|350040 cd18596, ABC_6TM_VMR1_D1_like, Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily. This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification
LQALLAVLSSVLSFAPPFFLNRLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRL
RAILTQLIFEKALRRRDKSGSSKSSESKKKDKEEDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVS
APLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIK
FFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLA
LFNMLRGPLNVLPELITQLLQAKVSLDRI
>gnl|CDD|350041 cd18597, ABC_6TM_YOR1_D1_like, Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily. This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane
LAGLLKLLADVLQVLSPLLLKYLINFVEDAYLGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLT
GAQVRAALTKAIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVN
LGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEI
RKKELKYVRKLQILRSILTAVAFSLPVLASMLSFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLAL
SSLADALVALKRI
>gnl|CDD|350042 cd18598, ABC_6TM_MRP7_D1_like, Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins. This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0)
PLGLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVR
AALVTAVYRKALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAF
LAGLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKEL
KALKGRKYLDALCVYFWATTPVLISILTFATYVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVE
AWVSLKRL
>gnl|CDD|350043 cd18599, ABC_6TM_MRP5_8_9_D2, Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9. This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0)
GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILV
ILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFL
QNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTI
HAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALS
YALQLSGLFQFTVRLASETEARFTSVERILEYI
>gnl|CDD|350044 cd18600, ABC_6TM_CFTR_D2, Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator. This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs
TTWNTYLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTSSY
YVFYIYVGVADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAIL
DDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFA
HLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTG
DGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRIFKFI
>gnl|CDD|350045 cd18601, ABC_6TM_MRP4_D2_like, Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins. This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0)
GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTA
ATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDF
LQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWT
IRAYSAQERFQEEFDAHQDLHSEAWFLFLATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSL
SYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS
>gnl|CDD|350046 cd18602, ABC_6TM_SUR1_D2_like, Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2. This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion
VALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVT
NLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLS
AIIVNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQAR
FTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVP
IYLNWVVRNLADVEMQMNSVERVLEYT
>gnl|CDD|350047 cd18603, ABC_6TM_MRP1_2_3_6_D2_like, Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6. This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0)
SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCV
RASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISIST
PIFLVVIIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRV
DENQRAYYPSIVSNRWLAVRLEFLGNLIVLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTS
ELETNIVSVERIKEYS
>gnl|CDD|350048 cd18604, ABC_6TM_VMR1_D2_like, Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily. This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification
WALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFG
SLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVV
VSPAFLLPAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLR
RIDRYSRAFRYLWNLNRWLSVRIDLLGALFSFATAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSY
NELELDMNSVERIQEYL
>gnl|CDD|350049 cd18605, ABC_6TM_MRP7_D2_like, Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins. This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0)
LILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGG
LRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQ
LPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEK
LENNQRAQLASQAASQWLSIRLQLLGVLIVTFVALTAVVQHFFGLSIDAGLIGLALSYALPITGLLSGLL
NSFTETEKEMVSVERVRQYF
>gnl|CDD|350050 cd18606, ABC_6TM_YOR1_D2_like, Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily. This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane
LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRL
HNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIA
LPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRA
YFLTIANQRWLAIRLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNM
NSVERLLHYA
>gnl|CDD|350119 cd18607, GH130, Glycoside hydrolase family 130. Members of the glycosyl hydrolase family 130, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor
WESAAVFNPGAILHDGKYHLLYRAVGKGTRRSSIGYARSKDGIHFERLDEPPLYPPPENPYEKGGCEDPR
ITKIDDTYYMTYTAYDGFGPRLALATTKDLKNWERHGLAFPPAPENKNGVIFPEKINGKYAMLHRPDGPD
IWLATSDDLIHWGDHKPLLKPRKGTWDSAKVGAGPPPIKTKKGWLLLYHGVNETAAGNRYRLGAALLDLN
DPTRVLYRSDKPILEPEEDYEKSGYVPNVVFPCGAVAIDGDELKLYYGAADTKVAVATV
>gnl|CDD|350120 cd18608, GH43_F5-8_typeC-like, Glycosyl hydrolase family 43 protein most having a F5/8 type C domain C-terminal to the GH43 domain. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as having beta-xylosidase (EC 3.2.1.37), xylanase (EC 3.2.1.8), and beta-galactosidase (EC 3.2.1.145) activities, and some as F5/8 type C domain (also known as the discoidin (DS) domain)-containing proteins. Most contain a F5/8 type C domain C-terminal to the GH43 domain. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. Characterized enzymes belonging to this subgroup include Lactobacillus brevis (LbAraf43) and Weissella sp (WAraf43) which show activity with similar catalytic efficiency on 1,5-alpha-L-arabinooligosaccharides with a degree of polymerization (DP) of 2-3; size is limited by an extended loop at the entrance to the active site. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
FADPSIVKFGGTYYLYATTDGWGGFNSGEPVVWKSKDFVNWKFEGLNWPTKAASGDSKVWAPSVVKGKDG
KYYMYVSVGSEIYVGVADSPLGPWKNANGDGPPIIPGDGKPNYHMIDAEPFIDDDGKAYLYWGSGLHVNG
HCFAAKLNPDMVTFDGSEPTIVTPRDYFEAPFMFKRNGIYYLMYSGGGCWDETYNVRYAVSDNPLGPFEE
GENSPILQTDEAKGIFGPGHHSVFEEGGQYYILYHRQGYPFSPGGTLRQVCVDELNFNADGTIKPV
>gnl|CDD|350121 cd18609, GH32-like, Glycosyl hydrolase family 32 family protein. The GH32 family contains glycosyl hydrolase family GH32 proteins that cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
MLALPDHWVWDFWLADDGGTYHLFYLQAPRSLGDPELRHRNARIGHAVSTDLVHWERLGDALGPGDPGAW
DDLATWTGSVIRDPDGLWRMFYTGTSRAEDGLVQRIGLATSDDLITWTKHPGNPLLAADPRWYETLGDSG
WHDEAWRDPWVFRDPDGGGWHMLITARANEGPPDGRGVIGHATSPDLEHWEVLPPLSAPGVFGHLEVPQV
FEIDGRWYLLFSCGADHLSRERRAAGGGGGTWYVPADSPLGPYDVVRARLLLPDGLYAGRLVRDPDGRWV
LLGFRNTGEDGGFVGGISDPIPL
>gnl|CDD|350122 cd18610, GH130_BT3780-like, Glycosyl hydrolase family 130, such as beta-mammosidase BT3780 and BACOVA_03624. This subfamily contains glycosyl hydrolase family 130, as classified by the carbohydrate-active enzymes database (CAZY), and includes Bacteroides enzymes, BT3780 and BACOVA_03624. Members of this family possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. GH130 enzymes have also been shown to target beta-1,2- and beta-1,4-mannosidic linkages where these phosphorylases mediate bond cleavage by a single displacement reaction in which phosphate functions as the catalytic nucleophile. However, some lack the conserved basic residues that bind the phosphate nucleophile, as observed for the Bacteroides enzymes, BT3780 and BACOVA_03624, which are indeed beta-mannosidases that hydrolyze beta-1,2-mannosidic linkages through an inverting mechanism
CPLRPKEVAWESKDVFNPAAIVRDGKVYLLYRAEDASGNGNGTSRIGLAVSDDGLHFTRLPEPVLYPEED
YEWPGGCEDPRIVEIEDGTYYMTYTAYDGKTARLCLATSTDLVHWTKHGPAFPDADGGKYRDLWSKSGAI
VPELKGAAKINGKYWMYWGESNIYLATSDDLIHWTPVEDDGSLRPVLSPRPGKFDSDLVEPGPPPILTDG
GILLIYNGANDGGGGPGYPKGTYSAGQALFDANDPTKLLARLDKPFLEPETPYEKEGQVNNVVFVEGLVY
FKGKWLLYYGTADSKIGVATA
>gnl|CDD|350123 cd18611, GH130, Glycosyl hydrolase family 130; uncharacterized. This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor
WEAEAVFNGSVIKDGGKYHLLYRALSSPQEIDGPKLGLSTIGYAESKDGVHFENRRQLIKPEEEWEKYGC
EDPRVTKIDGKYYIFYTALSGYPFGPEGIKVAVAITKDFKTIEEKHLVTPFNAKAMALFPEKINGKYAAL
LTVNTDNPPAKIALAYFDKIEDLWSPEYWDKWYANLDDHALPLRRSEHDHVEVGAPPIKTKDGWLLIYSY
IQNYFSGERVFGIEAALLDLNDPRKIIGRTKGPLLVPEEEYELYGLVPNIVFPSGALIEGDKLHIYYGAA
DTVCCLASV
>gnl|CDD|350124 cd18612, GH130_Lin0857-like, Glycoside hydrolase family 130 such as Listeria innocua beta-1,2-mannobiose phosphorylase. This subfamily contains the glycosyl hydrolase family 130 (GH130), as classified by the carbohydrate-active enzymes database (CAZY), enzymes that are phosphorylases and hydrolases for beta-mannosides, and includes Listeria innocua beta-1,2-mannobiose phosphorylase (Lin0857). hey possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Structure of Lin0857 shows beta-1,2-mannotriose bound in a U-shape, interacting with a phosphate analog at both ends. Lin0857 has a unique dimer structure connected by a loop, with a significant open-close loop displacement observed for substrate entry. A long loop, which is exclusively present in Lin0857, covers the active site to limit the pocket size
LEVIGVFNPGAARYGDEIILLLRVAEHLRLARSRDGIHFTVDEKPALFPEGPYEAFGIEDPRITRIDDTY
YITYTAVSEYGIATALASTKDFKTFERHGVIFPPENKDVVIFPEKINGKYYALHRPVPSGFGKPEIWIAE
SPDLLHWGNHRHLAGPRPGMWDSGRIGAGAVPIKTEKGWLEIYHGADENNRYCLGALLLDLEDPSKVIAR
SEEPILEPEAPYEKEGFFGNVVFTCGAVVEGDTLLIYYGAADTSIAVAEFS
>gnl|CDD|350125 cd18613, GH130, Glycosyl hydrolase family 130; uncharacterized. This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor
EYAIEAAALFNPSIVPHPDQSGLPPGELRFILSLRAVGEGHISSIEFRTGVIDPGGEIRLIRWLADSNYE
LRFPADVDLSERVLFPVTPAESNGIEDARFVRFTDDDGSVTYYATYTAYDGRAIRPQLLETRDFRTFKVR
PLTGPAARNKGMALFPRKIGGRYAMLSRQDGENIYLMFSDDLYFWDEAELILKPRYPWEFVQIGNCGSPI
ETDEGWLVLTHGVGPMRRYSIGAILLDLDDPTKVIGRLREPLLSPDEEEREGYVPNVVYSCGALVHGDRL
ILPYGMSDSATGFATVDLDELL
>gnl|CDD|350126 cd18614, GH130, Glycosyl hydrolase family 130; uncharacterized. This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor
WESKAVFNPAAIYEDGKVHLLYRAVGEDNISRLGYASSKDGIHFDERLDEPVYVPKKSGGENGGCEDPRI
TKIDDTYYMTYTAYDGWPPPRVALTSISTKDFLNFKWNWVIPPLISPPGVDDKDAVLFPEKINGKYALLH
RIGPDIWIDYSDDLDFGKNWIDSKIILEPRPGMWDSRKIGAGAPPIKTKKGWLLIYHGVDDDDRVYRLGA
ALLDLEDPTKVIARSPEPILEPEEDYEKEGLVPNVVFPCGAVVKDDTLFVYYGGADKVIGVATAPL
>gnl|CDD|350127 cd18615, GH130, Glycosyl hydrolase family 130; uncharacterized. This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor
WPYPANAVFNPGAAKLGGETLLLVRVEDRRGFSHLTVARSADGVTNWKIDPKPTLEPDPEDYPEEMWGIE
DPRITWLEELGRYAITYTAYSPAGPGVSLATTKDFKTFERLGLVMPPEDKDAALFPRRINGRWALLHRPV
SAGRAHIWISFSPDLKHWGDHRPVLPARRGPWWDAVKVGLGPPPIETPEGWLIIYHGVKETASGSIYRVG
LALLDLEDPTKVIRRSDEWVLGPEEPYERIGDVPNVVFPCGAILDEDGDELRLYYGAADTCIALATA
>gnl|CDD|350128 cd18616, GH43_ABN-like, Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activity. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
NPVFEPTFADPTVIRGDDGYFYAYATEDPWGDGGGFRLVPILRSKDLVNWEYVGDAFTSKPRWKWDPGGG
LWAPDIRYIDGKYVLYYSLSDWGADPNPGIGVATADSPAGPFTDQGKLFDSNEIGVRNSIDPFVFEDDGK
KYLFWGSFYGIYAVELTADGLALKPGEKVQIAGDRYEGPYIVKRDGYYYLFGSAGSCCEGPNSTYRVVVG
RSESLLGPYVDRDGRSLLDSGGGGTPVVLQNGNRFVGPGHNAVITDDAGQDWMLYHAYDRNDPYLPGGYN
RRPLLLDRLDW
>gnl|CDD|350129 cd18617, GH43_XynB-like, Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
NPILPGFYPDPSICRVGDDYYLVTSSFEYFPGLPIYHSKDLVNWELIGHALDRPSQLDLRGVPSSGGIFA
PTIRYHDGRFYIITTNVSTDGRGNFIVTADDPAGPWSDPVWLDGPGIDPSLFFDDDGKVYLTGTGPPPDP
YEGHGGIWQQEIDLETGKLLGEPKVLWNGGTGGRWPEGPHLYKIDGWYYLLIAEGGTEEGHSETIARSRS
PWGPYEPCPNNPILTHRHLGSNPVQNTGHADLVEDPDGSWWAVFLGVRPYGGGFHNLGRETFLAPVEWED
GWPVV
>gnl|CDD|350130 cd18618, GH43_Xsa43E-like, Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase Xsa43E. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. This subgroup includes Cellvibrio japonicus arabinan-specific alpha-1,2-arabinofuranosidase, CjAbf43A, which confers its specificity by a surface cleft that is complementary to the helical backbone of the polysaccharide, and Butyrivibrio proteoclasticus GH43 enzyme Xsa43E, also an arabinofuranosidase, which has been shown to cleave arabinose side chains from short segments of xylan. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
YTADPAALVHGDTVYLYTGHDEAPPGGTFFVMNDWRVFSTTDMVNWTDHGAVLSLKDFSWAKGDAWAGQV
IERNGKFYWYVPVHHKTNGGFAIGVAVSDSPTGPFKDALGKPLITNDMTGTTNHSWDDIDPTVFIDDDGQ
AYLYWGNPELYYVKLKEDMISLDGEIGTIDISGLPDFTEAPWVHKRNGLYYLSYAAGFPEKIAYATSDSP
TGPWTYKGVIMDPAGNSFTNHPAIIEFKGQSYFFYHNGALPGGGGFRRSVCVDELYYNEDGTIKK
>gnl|CDD|350131 cd18619, GH43_CoXyl43_like, Glycosyl hydrolase family 43 protein such as metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. Included in this subfamily is the metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43, which shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
PLITHIYTADPSAHVFDGKLYIYPSHDIEADIPFNDNGDQYDMKDYHVFSMDSLGGEVVDHGVALHVKDV
PWASRQMWAPDAAEKDGKYYLYFPAKDKDGIFRIGVAVSDKPEGPFKPEPEPIKGSYSIDPAVFVDDDGS
YYLYFGGIWGGQLQRWQTGSYVSGDGDEPQDDEPALGPRIAKLSPDMLSFAEPPREIVILDEDGKPLLAG
DHDRRFFEGPWMHKYNGKYYLSYSTGDTHLLVYATSDNPYGPFTYQGVILEPVLGWTTHHSIVEFKGKWY
LFYHDASLSGGKDHLRSVKVTELTYDADGTIQT
>gnl|CDD|350132 cd18620, GH43_XylA-like, Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium alpha-L-arabinofuranosidase XylA. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. The GH43_XylA-like subgroup includes Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and enzymes that have been annotated as having beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), endo-alpha-L-arabinanase (EC 3.2.1.-) as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan
PDGEPRVFGGRVYLYGSHDEFGGDEYCSNDYVVWSAPDDDLSNWRYHGVIFRSDQDPDEVPPGKGLLYAP
DVVKGPGRYYLYYCLSKGSVEGVAVSDSPAGPFEYLGPVKYPRKGDIFQIDPAVLVDDDGRVYLYWGQGG
SKGAELDPDMLTIKPETIVDVPAGITFEGHGFFEGSSIRKINGIYYLVYSSISRGRPTELCYATSKSPLG
PFTYGGVIIDNGGCDPPSGNNHGSIVEINGQWYIFYHRSTNNSEFSRQACAEPIEFDEDGTIPQ
>gnl|CDD|350133 cd18621, GH32_XdINV-like, glycoside hydrolase family 32 protein such as Xanthophyllomyces dendrorhous beta-fructofuranosidase (Inv;Xd-INV;XdINV). This subfamily of glycosyl hydrolase family GH32 includes fructan:fructan 1-fructosyltransferase (FT, EC 2.4.1.100) and beta-fructofuranosidase (invertase or Inv, EC 3.2.1.26), among others. These enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Xanthophyllomyces dendrorhous beta-fructofuranosidase (XdINV) also catalyzes the synthesis of fructooligosaccharides (FOS, a beneficial prebiotic), producing neo-FOS, making it an interesting biotechnology target. Structural studies show plasticity of its active site, having a flexible loop that is essential in binding sucrose and beta(2-1)-linked oligosaccharide, making it a valuable biocatalyst to produce novel bioconjugates. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
GWMNDPCAPGYDPSTGLYHLFYQWNPNGVEWGNISWGHATSKDLVTWTDSGEDPPALGPDGPYDSLGVFT
GCVIPNGLNGQDGTLTLFYTSVSHLPIHWTLPYTRGSETQSLATSSDGGRTWQKYEGNPILPGPPEGLNV
TGWRDPFVFPWPALDKLLGDSGPTLYGLISGGIRGVGPRVFLYRIDDSDLTDWTYLGPLEPPVNSNFGPS
RWSGDYGYNFEVANFFTLTDEGNGNGHDFLIMGAEGGREPPHRSGHWQLWMAGSLSKTENGSVTFEPTMG
GVLDWGLLYAANSFWDPKTDRRILWGWITEDDLPQALVEAQGWSGALSLPRELFVQT
>gnl|CDD|350134 cd18622, GH32_Inu-like, glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2). This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), among others. These enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
KGWMNDPNGLVYYDGEYHLFYQYNPDGNVWGNMHWGHAVSKDLVHWEELPIALPPPDELGDIFSGSAVVD
KNNTSGLGGFGKGALVAIYTSAGPDGGQTQSLAYSTDGGRTFTKYEGNPVLPNPGSTDFRDPKVFWHEPS
GKWVMVLAEGDKIGFYTSPDLKNWTYLSEFGPEGADGGVWECPDLFELPVDGDNETKWVLFVSANGGAPG
GGSGTQYFVGDFDGTTFTPDDEAPKWLDFGPDFYAAQTFSNTPDGRRIAIGWMSNWDYANQVPTEPFRGQ
MSLPRELTL
>gnl|CDD|350135 cd18623, GH32_ScrB-like, glycoside hydrolase family 32 sucrose 6 phosphate hydrolase (sucrase). Glycosyl hydrolase family GH32 subgroup contains sucrose-6-phosphate hydrolase (sucrase, EC:3.2.1.26) among others. The enzyme cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose. These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
GLLNDPNGLCYFNGKYHIFYQWNPFGPVHGLKYWGHVTSKDLVHWEDEGVALKPDTPYDKHGVYSGSALV
EDDKLYLFYTGNVKDEGGGREPYQCLATSDDGGKFKKKEVLLIEDPPEGYTEHFRDPKVFKKDGKYYMLL
GAQTKDDKGRILLYRSDDLLDWTYLGELLTGLEDFGYMWECPDLFELDGKDVLIFCPQGLDKEGDRYQNI
YQSGYLIGDLDFENLFFNHGDFQELDYGFDFYAPQTFEDPDGRRILIGWMGLPDTDYPPTDEEGWQHCLT
LPRELTLKN
>gnl|CDD|350136 cd18624, GH32_Fruct1-like, glycoside hydrolase family 32 protein such as Arabidopsis thaliana cell-wall invertase 1 (AtBFruct1;Fruct1;AtcwINV1;At3g13790). This subfamily of glycosyl hydrolase family GH32 includes fructan beta-(2,1)-fructosidase and fructan 1-exohydrolase IIa (1-FEH IIa, EC 3.2.1.153), cell-wall invertase 1 (EC 3.2.1.26), sucrose:fructan 6-fructosyltransferase (6-Sst/6-Dft, EC 2.4.1.10), and levan fructosyltransferases (EC 2.4.1.-) among others. This enzyme cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase. These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
NWMNDPNGPMYYKGLYHLFYQYNPHGAVWGNIVWGHAVSRDLVNWQHLPIALDPDEWYDINGVWSGSATI
LPDGTPVILYTGVDANSVQVQNLAFPANPSDPLLREWVKPPGNPVIAPPPGINPDNFRDPTTAWLGPDGL
WRIVVGARIGGRGIALLYRSKDFKTWELNPAPLHSVDGTGMWECPDFFPVSRKGSEGLGGPVKHVLKASL
DDEGHDYYAIGTYDAASNTFTPDNTDDDVGIGLRYDYGKFYASKSFFDPVKQRRVLWGWVNEEDSQAADI
AKGWAGVQSIPRTVSL
>gnl|CDD|350137 cd18625, GH32_BfrA-like, glycoside hydrolase family 32 protein such as Thermotoga maritima invertase (BfrA or Tm1414). This subfamily of glycosyl hydrolase family GH32 includes beta-fructosidase (invertase, EC 3.2.1.26) that cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase. These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
GWMNDPNGLCYFKGYYHLFYQYNPHGQEWGNMHWGHAVSKDLVHWTHLPVALYPQPELLLDRELTGGAFS
GSAVVKDDKMRLFYTRHFDPRDLRSGEIEWQKTAVSKDGIHFEKEETIIEIRPEGVSHDFRDPKVFREED
GKWKMVLGSGLDGIPAVLLYESDDLEHWTYEGVLYTEEEEGGRCIECPDLFPLDGKWVLIYSIVGYRPET
GRTNLVYYYIGTFKGGKFTPEKKGLLDFGTDFYAVQTFEHEGRRIAIGWLANWLDEHVTKENGANGSMSL
PRELHV
>gnl|CDD|349276 cd18626, CD_eEF3, chromodomain-like insertion in an ATPase domain of elongation factor eEF3. Eukaryotic elongation factor eEF3 (also known as EF-3, YEF3, and TEF3), a member of the ATP-binding cassette (ABC) family of proteins, is a ribosomal binding ATPase essential for fungal translation machinery. Until recently it was considered fungal-specific and therefore an attractive target for antifungal therapy; however, recent bioinformatics analysis indicates it may be more widely distributed among other unicellular eukaryotes, and translation elongation factor 3 activity has been demonstrated from a non-fungal species, Phytophthora infestans. eEF3 is a soluble factor lacking a transmembrane domain and having two ABC domains arranged in tandem, with a unique chromodomain inserted within the ABC2 domain. Chromodomain mutations in the ABC2 domain of eEF3 have been shown to reduce ATPase activity, but not ribosome binding. Thus, the chromodomain-like insertion is critical to eEF3 function. In addition to its elongation function, eEF3 has been shown to interact with mRNA in a translation independent manner, suggesting an additional, non-elongation function for this factor
KRVIEKIVGRRKLKKSYEYEVKWKGMSSKDNSWIPREELEEMGFEKLVQEVDDKEA
>gnl|CDD|349277 cd18627, CD_polycomb_like, chromodomain of polycomb and chromobox family proteins. CHRomatin Organization Modifier (chromo) domain of Polycomb and Polycomb-group (PcG) chromobox (CBX) family proteins such as CBX2, CBX4, CBX6, CBX7, and CBX8. These CBX proteins are components of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells
FAAECILKKRIRKGKVEYLVKWKGWSQKYNTWEPEENILDPRLLAAFES
>gnl|CDD|349278 cd18628, CD3_cpSRP43_like, chromodomain 3 of chloroplast signal recognition particle 43 kDa protein, and similar proteins. This subgroup includes the chromodomain 3 of chloroplast SRP43 (cpSRP43), and similar proteins. CpSRP43 is a component of the chloroplast signal recognition particle (SRP) pathway. It forms a stable complex with cpSRP54 (cpSRP complex) which is required for the efficient posttranslational transport of members of the nuclearly encoded light harvesting chlorophyll-a/b-binding proteins (LHCPs) to the thylakoid membrane. Chromatin organization modifier (chromo) domain is a conserved region of around 50 amino acids found in a variety of chromosomal proteins, which appear to play a role in the functional organization of the eukaryotic nucleus. Experimental evidence implicates the chromodomain in the binding activity of these proteins to methylated histone tails and maybe RNA. May occur as single instance, in a tandem arrangement or followed by a related chromo shadow domain
LEYAVAESVIGKRVGDDGKTIEYLVKWTDMSDATWEPQDNVDSTLVLLYQQ
>gnl|CDD|349279 cd18629, CD2_cpSRP43_like, chromodomain 2 of chloroplast signal recognition particle 43 kDa protein, and similar proteins. This subgroup includes the chromodomain 2 of chloroplast SRP43 (cpSRP43), and similar proteins. CpSRP43 is a component of the chloroplast signal recognition particle (SRP) pathway. It forms a stable complex with cpSRP54 (cpSRP complex) which is required for the efficient posttranslational transport of members of the nuclearly encoded light harvesting chlorophyll-a/b-binding proteins (LHCPs) to the thylakoid membrane. Chromatin organization modifier (chromo) domain is a conserved region of around 50 amino acids found in a variety of chromosomal proteins, which appear to play a role in the functional organization of the eukaryotic nucleus. Experimental evidence implicates the chromodomain in the binding activity of these proteins to methylated histone tails and maybe RNA. May occur as single instance, in a tandem arrangement or followed by a related chromo shadow domain
EYAEVNEILESRGKGKDMEYLIEWKDGGDCEWVKGVHVAEDVASDYET
>gnl|CDD|349280 cd18630, CD_Rhino, chromodomain of Drosophila melanogaster Rhino, and similar proteins. N-terminal CHRomatin Organization Modifier (chromo) domain of Drosophila melanogaster Rhino (also known as heterochromatin protein 1-like), and similar proteins. Rhino is a female-specific protein that affects chromosome structure and egg polarity that is required for germline PIWI-interacting RNA (piRNA) production. In Drosophila the RDC (rhino, deadlock, and cutoff) complex, composed of rhino, the protein deadlock (Del) and the Rai1-like transcription termination cofactor cutoff (Cuff) binds to chromatin of dual-strand piRNA clusters, special genomic regions, which encode piRNA precursors. The RDC complex is anchored to H3K9me3-marked chromatin in part via the H3K9me3-binding activity of Rhino, and is required for transcription of piRNA precursors. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
EYVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENLGNCMKLVADYEA
>gnl|CDD|349281 cd18631, CD_HP1_like, chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma. CHRomatin Organization Modifier (chromo) domain of mammalian HP1alpha (Cbx5), HP1beta (Cbx1), HP1gamma (Cbx5), and similar proteins. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3)
EYVVEKVLDRRVVKGKVEYLLKWKGYPDEDNTWEPEENLDCPDLIAEFEE
>gnl|CDD|349282 cd18632, CD_Clr4_like, N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar proteins. N-terminal CHRomatin Organization Modifier (chromo) domain of cryptic loci regulator 4 (Clr4), a histone H3 lysine methyltransferase which targets H3K9. Clr4 regulates silencing and switching at the mating-type loci and affects chromatin structure at centromeres. Clr4 is a catalytic component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
EYEVEKIVDEKTDRNTAEPLYLVRWKNYSKNHDTWEPAENLSGCQAVLEKWKRKK
>gnl|CDD|349283 cd18633, CD_MMP8, chromodomain of M-phase phosphoprotein 8. The chromodomain of M-phase phosphoprotein 8 (MPP8), a component of the RanBPM-containing large protein complex, binds methylated H3K9. This may in turn recruit the H3K9 methyltransferases GLP and ESET, and DNA methyltransferase 3A to the promoter of the E-cadherin gene, mediating the E-cadherin gene silencing and promoting tumor cell motility and invasion. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK
>gnl|CDD|349284 cd18634, CD_CDY, chromodomain of the Chromodomain Y-like protein family. This group includes the chromodomain found in the mammalian chromodomain Y-like (CDY) protein family, and similar proteins. The human CDY family includes 6 proteins: the genes encoding four of these: two copies of CDY1 (CDY1a, CDY1a) and two copies of CDY2(CDY2a and CDY2b), are located on chromosome Y, and the genes encoding the other two members (CDYL and CDYL2) are located on autosomes. The chromosomal genes are only present in primates, whereas the CDYL and CDYL2 genes exist in most mammalian species. The CDY family proteins contain two functional domains: a chromodomain involved in chromatin binding and a catalytic domain found in many coenzyme A (CoA)- dependent acylation enzymes. CDYL is ubiquitously expressed, whereas CDYL2 shows selective expression in tissues of testis, prostate, spleen, and leukocyte. The CDYL genes are ubiquitously expressed, the CDY genes are only expressed in the testis. Deletion of the CDY1b gene has been shown to be a risk factor for male infertility. Impairments in CDY2 expression could be implicated in the pathogenesis of maturation arrest (a failure of germ cell development)
LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR
>gnl|CDD|349285 cd18635, CD_CMT3_like, chromodomain of chromomethylase 3, and similar proteins. CHRomatin Organization Modifier (chromo) domain of DNA (cytosine-5)-methyltransferase chromomethylase 3 (CMT3, EC:2.1.1.37), and similar proteins. CMT3 is primarily a CHG (where H is either A, T or C) methyltransferase and is predominantly expressed in actively replicating cells. The protein is involved in preferentially methylating transposon-related sequences, reducing their mobility. Studies suggest that in order to target DNA methylation, CMT3 associates with H3K9me2-containing nucleosomes through binding of its BAH- and chromo-domains to H3K9me2. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
EFEVEKLVGICYGDPKKTGERGLYFKVRWKGYGPEEDTWEPIEGLSNCPEKIKEFVQ
>gnl|CDD|349286 cd18636, CD_Chp1_like, chromodomain of chromodomain-containing protein 1, and similar proteins. CHRomatin Organization Modifier (chromo) domain of chromodomain-containing protein 1 (CHp1), and similar proteins. Chp1 is needed for RNA interference-dependent heterochromatin formation in fission yeast. Chp1 is a member of the RNA-induced transcriptional silencing (RITS) complex which maintains the heterochromatin regions. The chromodomain of the Chp1 component binds the histone H3 lysine 9 methylated tail (H3K9me) and the core of the nucleosome. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
VYEVEDILADRVNKNGINEYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKWKK
>gnl|CDD|349287 cd18637, CD_Swi6_like, chromodomain of fission yeast Swi6, and similar proteins. Fission yeast Swi6 protein is a structural and functional homolog of mammalian HP1 (heterochromatin protein 1) and is involved in the chromatin structure by binding to centromeres, telomeres, and the silent mating-type locus. Swi6 contains a N-terminal chromo (CHRromatin Organization MOdifier) domain and a C-terminal chromo shadow domain (CSD). Swi6 binds histone H3 tails methylated at Lys- and the cohesion subunit Psc3, leading to silencing the genes and sister chromatid cohesion. It is also involved in the repression of the silent mating-type loci MAT2 and MAT3. Swi6 may compact MAT2/3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes. chromodomains mediate the interaction of the heterochromatin with other heterochromatin proteins, thereby affecting chromatin structure (e.g. Drosophila and human heterochromatin protein (HP1) and mammalian modifier 1 and modifier 2). CSDs have only been found in proteins that also possess a chromodomain
EYVVEKILKHRMARKGGGYEYLLKWEGYDDPSDNTWSSEADCAGCKDLIEAYWE
>gnl|CDD|349288 cd18638, CD_EhHp1_like, chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins. This subgroup includes the N-terminal CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 (HP1)-like protein from Entamoeba histolytica, and similar proteins. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
TFEVEKIVKKKTVKGGTEYFVKWKGYSAKENTWETEDNLEKSYKEMIDEFEK
>gnl|CDD|349289 cd18639, CD_SUV39H1_like, chromodomain of histone methyltransferase SUV39H1, and similar proteins. CHRomatin Organization Modifier (chromo) domain of human SUV39H1, a histone lysine methyltransferase (HMT) which catalyzes di- and tri-methylation of lysine 9 of histone H3 (H3K9me2/3), leading to heterochromatin formation and gene silencing. H3K9me2/3 represents a specific mark for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3, and/or CBX5) proteins to methylated histones. SUV39H1 mainly functions in heterochromatin regions. The human SUV39H1/2, histone H3K9 methyltransferases, are the mammalian homologs of Drosophila Su(var)3-9 and Schizosaccharomyces pombe Clr4. SUV39H1 contains a chromodomain at its N-terminus and a SET domain at its C-terminus. Although the SET domain performs the catalytic activity, the chromodomain of SUV39H1 is essential for the catalytic activity of SUV39H1. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
YEVEYLCDYKKIREQEYYLVKWKGYPDSENTWEPRQNLKCSRLLKQFHK
>gnl|CDD|349290 cd18640, CD_Chro-like, chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins. This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in chromodomain of Drosophila melanogaster chromator (also known as Chriz/Chro) chromodomain protein, and similar proteins. Chromator is a nuclear protein that plays a role in proper spindle dynamics during mitosis. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
EPVEKIVAKRFNPRKKTWEYLVKWENRSHHENTWEPMANLERCKYLLQMFEK
>gnl|CDD|350843 cd18641, CBD_RBP1_like, chromo barrel domain of retinoblastoma binding protein 1, and similar proteins. Retinoblastoma-binding protein 1 (RBP1), also termed AT-rich interaction domain 4A, is a ubiquitously expressed nuclear protein. RBP1 is a tumor and leukemia suppressor that binds both methylated histone tails and DNA, and is involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndromes. The chromo barrel domain of RBP1 has been reported to recognize histone H4K20me3 weakly, and this binding is enhanced by the simultaneous binding of DNA. RBP1 binds directly, with several other proteins, to retinoblastoma protein (pRB) which regulates cell proliferation; pRB represses transcription by recruiting RBP1. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain
TKVKVKYGRGKTQKIYEASIKSTEIDDGEVLYLVHYYGWNVRYDEWVKADRIIWPLDKG
>gnl|CDD|350844 cd18642, CBD_MOF_like, chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar proteins. This subgroup includes the chromo barrel domains found in human Tat-interactive protein 60 (TIP60, (also known as KAT5 or HTATIP), Drosophila melanogaster males-absent on the first (MOF) protein, and Saccharomyces ESA1. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. The MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites
IKCRCWVQRNDEEHLAEVLSRRTRKHAPPEFYVHYVELNRRLDEWITTDRIDLDLKECELPKKKATK
>gnl|CDD|350845 cd18643, CBD, chromo barrel domain of MOF acetyltransferase, and similar proteins. This group includes the chromo barrel domains found in human Tat-interactive protein 60 (TIP60, (also known as KAT5 or HTATIP), Drosophila melanogaster males-absent on the first (MOF) protein, human male-specific lethal (MSL) complex subunit 3 (MSL3), and retinoblastoma binding protein 1. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. The chromobarrel domains include a MOF-like subgroup which may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites
EKVLVFEPDPKARVLYDAKILSVITGKDGRAPPEYLVHYVGWNRRLDEWVAEDRVLPDLDE
>gnl|CDD|349291 cd18644, CD_polycomb, chromodomain of polycomb. CHRomatin Organization Modifier (chromo) domain of the PcG (polycomb-group) chromodomain protein Polycomb (Pc) from Drosophila melanogaster, anthropod, worm, and sea cucumber, and similar proteins. Pc is a component of the Polycomb-group (PcG) multiprotein PRC1 complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. The core subunits of PRC1 are polycomb (Pc), polyhomeotic (Ph), posterior sex combs (Psc), and sex comb extra (Sce, also known as dRing). Polycomb (Pc) plays a role in modulating life span in flies, it negatively regulates longevity
DLVYAAEKILKKRVRKGKVEYLVKWKGWSNKHNTWEPEENILDRRLIEIFERTN
>gnl|CDD|349292 cd18645, CD_Cbx4, chromodomain of chromobox homolog 4. CHRomatin Organization Modifier (chromo) domain of chromobox homolog 4 (CBX4), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. In addition to a chromodomain with H3K27me3-binding activity, Cbx4 contains two SUMO-interacting motifs responsible for its small ubiquitin-related modifier (SUMO) E3 ligase activity. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, for example CBX8 promotes proliferation while suppressing metastasis, in colorectal carcinoma progression. CBX4 may serve as a tumor suppressor in colorectal carcinoma, and has been shown to be an oncogene in osteosarcoma and breast cancer
EHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRER
>gnl|CDD|349293 cd18646, CD_Cbx7, chromodomain of chromobox homolog 7. CHRomatin Organization Modifier (chromo) domain of chromobox homolog 7 (CBX7), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, for example CBX8 promotes proliferation while suppressing metastasis, in colorectal carcinoma progression. CBX7 has been shown to function as a tumor suppressor in lung carcinoma and an oncogene in gastric cancer and lymphoma
GEQVFAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHILDPRLVMAYEEKEE
>gnl|CDD|349294 cd18647, CD_Cbx2, chromodomain of chromobox homolog 2. CHRomatin Organization Modifier (chromo) domain of chromobox homolog 2 (CBX2), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells
EQVFAAECILSKRLRKGKLEYLVKWRGWSSKHNSWEPEENILDPRLLLAFQKK
>gnl|CDD|349295 cd18648, CD_Cbx6, chromodomain of chromobox homolog 6. CHRomatin Organization Modifier (chromo) domain of chromobox homolog 6 (CBX6), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells
ERVFAAESIIKRRIRKGRIEYLVKWKGWAIKYSTWEPEENILDSRLIAAFEQKERERE
>gnl|CDD|349296 cd18649, CD_Cbx8, chromodomain of chromobox homolog 8. CHRomatin Organization Modifier (chromo) domain of chromobox homolog 8 (CBX8), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, CBX8 for example promotes proliferation while suppressing metastasis, in colorectal carcinoma progression
GERVFAAEALLKRRIRKGRMEYLVKWKGWSQKYSTWEPEENILDARLLAAFEERE
>gnl|CDD|349297 cd18650, CD_HP1beta_Cbx1, chromodomain of heterochromatin protein 1 homolog beta. CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog beta (also known as HP1beta, CBX1, and chromobox 1), and related proteins. HP1beta is a highly conserved non-histone protein, which is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta, and HP1gamma (also known as Cbx3)
EYVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENLDCPDLIAEFLQ
>gnl|CDD|349298 cd18651, CD_HP1alpha_Cbx5, chromodomain of heterochromatin protein 1 homolog alpha. CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog alpha (also known as HP1alpha, Cbx5, and Chromobox 5), and related proteins. HP1alpha has diverse functions in heterochromatin formation, gene regulation, and mitotic progression, and forms complex networks of gene, RNA, and protein interactions. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha, HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3)
EYVVEKVLDRRVVKGQVEYLLKWKGFSEEHNTWEPEKNLDCPELISEFMK
>gnl|CDD|349299 cd18652, CD_HP1gamma_Cbx3, chromodomain of heterochromatin protein 1 homolog gamma. CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog gamma (also known as HP1gamma, Cbx3, and Chromobox 3), and related proteins. HP1gamma is a highly conserved non-histone protein, which is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. In addition to being involved in transcriptional silencing in heterochromatin-like complexes, HP1gamma also binds lamin B receptor, an integral membrane protein found in the inner nuclear membrane. The dual binding functions of the protein may explain the association of heterochromatin with the inner nuclear membrane. HP1gamma is also recruited to sites of ultraviolet-induced DNA damage and double-strand breaks. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma
EFVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENLDCPELIEAFLN
>gnl|CDD|349300 cd18653, CD_HP1a_insect, chromodomain of insect HP1a. CHRomatin Organization Modifier (chromo) domain of insect HP1a. HP1a is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. In Drosophila, there are at least five HP1 family proteins, this subgroup includes the CD of Drosophila melanogaster HP1a
EYAVEKICDRRVRKGKVEYYLKWKGYPETENTWEPEENLDCQDLIQQYEA
>gnl|CDD|349301 cd18654, CSD_HP1beta_Cbx1, chromo shadow domain of heterochromatin protein 1 homolog beta. heterochromatin protein 1 homolog beta (also known as HP1beta, Cbx1, chromobox 1) is a highly conserved non-histone protein, which is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1beta has a single N-terminal chromodomain which can bind to histone proteins via methylated lysine residues, and a C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1beta may play an important role in the epigenetic control of chromatin structure and gene expression. CSD domains have only been found in proteins that also possess a related chromodomain, while chromodomains can exist in isolation. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. The HP1 CSD, in addition to interacting with various proteins bearing the PXVXL motif, also interacts with a region of histone H3 that bears the similar PXXVXL motif. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta, and HP1gamma (also known as Cbx3). The CSD domains of all three human HP1 homologs have similar affinities to the PXXVXL motif of histone H3
GFARGLEPERIIGATDSSGELMFLMKWKNSDEADLVPAKEANVKCPQVVISFYEERLT
>gnl|CDD|349302 cd18655, CSD_HP1alpha_Cbx5, chromo shadow domain of heterochromatin protein 1 homolog alpha. Chromo shadow domain (CSD) of heterochromatin protein 1 homolog alpha (also known as HP1alpha, Cbx5, and Chromobox 5), and related proteins. HP1alpha has diverse functions in heterochromatin formation, gene regulation, and mitotic progression, and forms complex networks of gene, RNA, and protein interactions. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. CSD domains have only been found in proteins that also possess a related chromodomain, while chromodomains can exist in isolation. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. The HP1 CSD, in addition to interacting with various proteins bearing the PXVXL motif, also interacts with a region of histone H3 that bears the similar PXXVXL motif. There are three human homologs of HP1 proteins: HP1alpha, HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3). The CSD domains of all three human HP1 homologs have similar affinities to the PXXVXL motif of histone H3
GFERGLEPEKIIGATDSCGDLMFLMKWKDSDEADLVLAKEANVKCPQIVIAFYEERLT
>gnl|CDD|349303 cd18656, CSD_HP1gamma_Cbx3, chromo shadow domain of heterochromatin protein 1 gamma homolog gamma. Chromo shadow domain (CSD) of heterochromatin protein 1 gamma homolog gamma (also known as HP1gamma, Cbx3, Chromobox 3), and related proteins. HP1gamma appears to be involved in transcriptional silencing in heterochromatin-like complexes. It binds histone H3 tails methylated at Lys-9, leading to epigenetic repression, and also binds lamin B receptor, an integral membrane protein found in the inner nuclear membrane. The dual binding functions of the protein may explain the association of heterochromatin with the inner nuclear membrane. HP1gamma is also recruited to sites of ultraviolet-induced DNA damage and double-strand breaks. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal CSD which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. CSD domains have only been found in proteins that also possess a related chromodomain, while chromodomains can exist in isolation. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. The HP1 CSD, in addition to interacting with various proteins bearing the PXVXL motif, also interacts with a region of histone H3 that bears the similar PXXVXL motif. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma. The CSD domains of all three human HP1 homologs have similar affinities to the PXXVXL motif of histone H3
GFARGLDPERIIGATDSSGELMFLMKWKDSDEADLVLAKEANMKCPQIVIAFYEERLT
>gnl|CDD|349304 cd18657, CSD_Swi6, chromo shadow domain of chromatin-associated protein Swi6. Chromo shadow domain (CSD) of fission yeast Swi6 protein. Swi6 is a structural and functional homolog of mammalian HP1 (heterochromatin protein 1) and is involved in the chromatin structure by binding to centromere, telomere and silent mating-type locus. Swi6 contains a N-terminal chromo (CHRromatin Organization MOdifier) domain and a C-terminal chromo shadow domain (CSD). Swi6 binds histone H3 tails methylated at Lys- and the cohesion subunit Psc3, leading to silencing the genes and sister chromatid cohesion. It is also involved in the repression of the silent mating-type loci MAT2 and MAT3. Swi6 may compact MAT2/3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes. The chromo shadow domain (CSD) is always found in association with a related N-terminal chromo (CHRromatin Organization MOdifier) domain. CSD domains have only been found in proteins that also possess a chromodomain, while chromodomains can exist in isolation
SWEDLVDSIETVERDKDGKLLVYLTWKNGKKSQHPSSVVYKKCPQKMLQFYESHL
>gnl|CDD|349305 cd18658, CSD_HP1a_insect, chromo shadow domain of insect heterochromatin protein 1a. The chromo shadow domain (CSD) is always found in association with a related N-terminal chromo (CHRromatin Organization MOdifier) domain. CSD domains have only been found in proteins that also possess a chromodomain, while chromodomains can exist in isolation. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal CSD which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. The HP1 CSD, in addition to interacting with various proteins bearing the PXVXL motif, also interacts with a region of histone H3 that bears the similar PXXVXL motif. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3). The CSD domains of all three human HP1 homologs have similar affinities to the PXXVXL motif of histone H3. In Drosophila, there are at least five HP1 family proteins, this subgroup includes the CSD of Drosophila melanogaster HP1a
GLEAEKILGASDSNGGLTFLIQFKGVDQAEMVPASVANVKIPQMVIKFYEERL
>gnl|CDD|349306 cd18659, CD2_tandem, repeat 2 of paired tandem chromodomains. Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
EYTIVERIIAHREDDEGVTEYLVKWKGLPYDECTWESEEDISDIFQEAIDEYKK
>gnl|CDD|349307 cd18660, CD1_tandem, repeat 1 of paired tandem chromodomains. Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
DEDKIEKILDHRPKGPVEEASLDLTDPDEPWDEREFLVKWKGKSYLHCTWVTEETLEQLRGKKKLKNYIK
>gnl|CDD|349308 cd18661, CD2_tandem_CHD1-2_like, repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins. Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
QYQIVERIIAHSPQKSAASGYPDYLCKWQGLPYSECTWEDGALISKKFQACIDEYHSR
>gnl|CDD|349309 cd18662, CD2_tandem_CHD3-4_like, repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and 4, and similar proteins. Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD3 and CHD4, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. Human CHD3 (also named Mi-2 alpha) and CHD4 (also named Mi-2 beta) are coexpressed in many cell lines and tissues and may act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). The proteins form distinct CHD3- and CHD4-NuRD complexes that repress, as well as activate gene transcription of overlapping and specific target genes. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
PEWLQIHRIINHRVDKDGNTWYLVKWRDLPYDQSTWESEDDDIPDYEKHIQEYWD
>gnl|CDD|349310 cd18663, CD2_tandem_CHD5-9_like, repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins. Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR
>gnl|CDD|349311 cd18664, CD2_tandem_ScCHD1_like, repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins. Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
EFHVVERIIASQRASLEDGTSQLQYLVKWRRLNYDECTWEDATLIAKLAPEQVDHFQNR
>gnl|CDD|349312 cd18665, CD1_tandem_CHD1_yeast_like, repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins. Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
DEHGIDIVLDHRLKEGLEEGELDDPKENYEFLIKWTDESHLHNTWETYESLKQVRGLKKVDNYIK
>gnl|CDD|349313 cd18666, CD1_tandem_CHD1-2_like, repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins. Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
EFETIERVLDHRIGRKGATGASTTIYAVEADGDPNAGFDPEDEETEIQYLIKWKGWSHIHNTWESEESLK
DQNVKGMKKLENYKK
>gnl|CDD|349314 cd18667, CD1_tandem_CHD3-4_like, repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and 4, and similar proteins. Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD3 and CHD4. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. Human CHD3 (also named Mi-2 alpha) and CHD4 (also named Mi-2 beta) are coexpressed in many cell lines and tissues and may act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). The proteins form distinct CHD3- and CHD4-NuRD complexes that repress, as well as activate gene transcription of overlapping and specific target genes. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
LKGKVEKILTWRWAEPPYPEPLPEKPDEDPYPPPPRKLQPRPEREFFVKWHGMSYWHCEWVSELQLEVHH
PAMYRNYQR
>gnl|CDD|349315 cd18668, CD1_tandem_CHD5-9_like, repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins. Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
EEDTMIIEKILASRKKKKEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKGDKRIKQKIKRFKQ
>gnl|CDD|349948 cd18669, M20_18_42, M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases. This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues)
NVIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKE
NGFKLKGTVVVAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTPLVDALSEAAR
KVFGKPQHAEGTGGGTDGRYLQELGIPGVTLGAGGGKGAHSPNERVNLEDLESALAVL
>gnl|CDD|350850 cd18670, PIN_Mut7-C-like, PIN domain at the C-terminus of Caenorhabditis elegans exonuclease Mut-7 and related domains. The Mut7-C-like family of the PIN domain superfamily includes the C-terminal domain of Caenorhabditis elegans Mut-7 (also known as exonuclease 3'-5' domain-containing protein 3 homolog). Mut-7 is involved in RNA interference (RNAi) and transposon silencing in C. elegans. The Mut7-C PIN domain family is recognized as a genuine PIN domain, however it is not included it in the CDD PIN domain superfamily hierarchical model as it is lacks a core strand and helix (H3 and S3). The PIN (PilT N terminus) domain belongs to a large nuclease superfamily, and were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Other PIN domain families are: the FEN-like PIN domain family which includes the PIN domains of Flap endonuclease-1 (FEN1), Exonuclease-1 (EXO1), Mkt1, Gap Endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease, 5'-3' exonucleases of DNA polymerase I and bacteriophage T4- and T5-5' nucleases; the VapC-like PIN domain family which includes toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and, rRNA-processing protein Fcf1; the LabA-like PIN domain family which includes the PIN domains of Synechococcus elongatus LabA (low-amplitude and bright); the PRORP-Zc3h12a-like PIN domain family which includes the PIN domains of of RNase P (PRORP), ribonuclease Zc3h12a; and Bacillus subtilis YacP/Rae1-like PIN domains. Matelska et al. recently classified PIN-like domains into distinct groups, this family includes some sequences belonging to two of these, PIN _10 and PIN_16
VLLDENLPRFGANLRRAGIDVIVPKLVSDFEKYAKAIEEKSYEVLTMDYDNELIAIPGLFFGLFN
>gnl|CDD|350238 cd18671, PIN_PRORP-Zc3h12a-like, PIN domain of protein-only RNase P (PRORP), ribonuclease Zc3h12a, and related proteins. PRORPs catalyze the maturation of the 5' end of precursor tRNAs in eukaryotes. This family includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3, PRORP1 localizes to the chloroplast and the mitochondria, and PRORP2 and PRORP3 localize to the nucleus. Zc3h12a (zinc finger CCCH-type containing 12A, also known as MCPIP1/MCP induced protein 1 and Regnase-1) is a critical regulator of inflammatory response, with additional roles in defense against viruses and various stresses, cellular differentiation, and apoptosis. This PIN_PRORP-Zc3h12a-like family also includes Caenorhabditis elegans REGE-1 (REGnasE-1), which also functions as a cytoplasmic endonuclease. Additionally, it includes three less-studied mammalian homologs: Zc3h12b-d/Regnase-2-4, as well as N4BP1 (NEDD4-binding partner-1), NYNRIN (NYN domain and retroviral integrase containing, also known as CGIN1/Cousin of GIN1), and KHNYN (KH and NYN domain containing) protein. N4BP1, CGIN1, and KHNYN proteins are probably of retroviral origin. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
AVIDGANVGLSHQNKESFSCRQLLLAVNWFLERSHNNTDPLVFLHKWRVEQPRPVPPTDRHLLEEWEKKG
ILYATPPGSNDDWYWLYAAYESKCLLVTNDEMRDHQFELLGRQFFKRWKEEHQVRY
>gnl|CDD|350239 cd18672, PIN_FAM120B-like, FEN-like PIN domains of FAM120B (family with sequence similarity 120B) and related proteins. FAM120B (also known as CCPG, "constitutive coactivator of PPAR-gamma", PGCC1, "PPARgamma constitutive coactivator 1") is a constitutive coactivator of peroxisome proliferator-activated receptor (PPARgamma) that promotes adipogenesis in a PPARgamma-dependent manner. This subfamily belongs to the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), the helical arch/clamp region is involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
GLQSFVESHCPNACVQVNLKKLAREHRRKPPGSTPVLVVDAMCCLRYLYGGYLDWVCGGQWNEMLRNLSN
FVSAFQAAGIQLVFFFDGVVESQKRDEWVKRRLKNNKKVSKVFNHIKKKGTQPPKNLFFLPSGLATFTRF
ALRSLGVEVICSMDEADQEVASYCRQNNCFGILGQDSDYLIFDTPPYLSISKLKLTSLKTVLESRERLCD
>gnl|CDD|350240 cd18673, PIN_XRN1-2-like, FEN-like PIN domains of XRN1, XRN2, and related proteins. XRN1 (5'-3' exoribonuclease 1, also known as SEP1) is a processive 5'-3' exoribonuclease that degrades the body of transcripts in the major pathway of RNA decay; XRN2 (5'-3' exoribonuclease 2) is predominantly localized in the nucleus and recognizes single-stranded RNAs with a 5'-terminal monophosphate to degrade them possessively to mononucleotides. XRN2 has a critical function to process maturation of 5.8S and 25S/28S rRNAs as well as degradation of some spacer fragments that are excised during rRNA maturation. Both XRN1 and XRN2 preferentially cleave 5'-monophosphorylated RNA. XRN2 is also known as Rat1p in yeast. This subfamily belongs to the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), the helical arch/clamp region is involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LYLDMNGIIHPCTHPEDRPAPKSEEEMFQNIFKYIDRLFNIVRPRKLLYIAVDGVAPRAKMNQQRSRRFR
SAKEAEEKEAKEEELESEGKELGEEEEKERFDSNCITPGTEFMERLSKALRYYIAKKLNTDPGWKNLKVI
LSDSNVPGEGEHKIMDFIRSQRAQPGYDPNTRHCIYGLDADLIMLGLATHEPNFSILREEVFFGKPKPKK
LCCGEKSEKKTRAKEKKFQFLHISVLREYL
>gnl|CDD|350241 cd18674, PIN_Pox_G5, FEN-like PIN domain of vaccinia virus G5 protein and related proteins. Poxvirus G5 nuclease is involved in DNA replication and double-strand break repair by homologous recombination. This subfamily belongs to the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), the helical arch/clamp region is involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
GIFVDTMSIYIAIAYSVRNLEELTTVFIEYVQGWVKKGGHVTLFIDRGSIKIKQSLRDKKIDKLTFHIFL
SDSDNLKRSLEEILAHFNDNVEIVYCDGVDAEFVMCLRAKALAATTGEWPLIISTDQDTLLFASVDNHPK
IIKTLTQLYKF
>gnl|CDD|350242 cd18675, PIN_SpAst1-like, FEN-like PIN domain of Schizosaccharomyces pombe asteroid homolog 1 and related proteins. Schizosaccharomyces pombe Ast1 is a homologue of Drosophila Asteroid and human ASTE1. Ast1 appears to be involved in mounting a checkpoint response to endogenous damage in cells lacking Rad2 and Exo1. This subfamily belongs to the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), the helical arch/clamp region is involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
VVIDGPSLVYHVYNRLLAWSSVSPNLVAAQPSYDEISQAVMQFLLQLETLGVKIEAIYFDGGLPASKRET
RLERMENLQRQQLERYAKGHFKVPIVWADLVQVVPGEADKYCAIAAKESGAAILTNDSDLLVHDLGPEGS
VILLHSIETKKYRSLEPKEHFSL
>gnl|CDD|350243 cd18676, PIN_asteroid-like, FEN-like PIN domain of Drosophila melanogaster asteroid and related proteins. This subfamily includes Drosophila melanogaster asteroid protein which may function in EGF receptor signaling, and may play a role in compound eye morphogenesis. This subfamily belongs to the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), the helical arch/clamp region is involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LVIDGNNLCYQLYFDSNLDNSAFGGDYDKYARVVREFFELLSKCNVTPYVILDGGYEDRKLKTVTSRLRA
KIKIAKAKTPSTGGSGSILPLLLKEVFVDVLKELNVKVVQCDFEADDEIAALARKLNCPVLSYDSDFYIF
DVLYIPFSTVQWNVVLKPKENFYL
>gnl|CDD|350244 cd18677, PIN_MjVapC2-VapC6_like, VapC-like PIN domain of Methanocaldococcus jannaschii VapC2, and VapC6, and related proteins. This subfamily includes Methanocaldococcus jannaschii VapC2 and VapC6. It belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
FIDSNVFIEYLKGNELAKELLEKLENEFELFINPIVFSEVLYVYLRLKTGKSPYTLKKKPEIIEKLELED
VLELLELFKILEINEEILELALELIEKYGLLPNDALILATCKYYGIKKIATFDSDFKRVDFLEVIE
>gnl|CDD|350245 cd18678, PIN_MtVapC25_VapC33-like, VapC-like PIN domain of Mycobacterium tuberculosis VapC25, VapC33, and related proteins. This subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC25, VapC29, VapC33, VapC37, and VapC39 toxins. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LPDVNVLIYAVRTDHPHHRAAAAWLDAMVSGDDRFGLTPLVLSGFVRIVTNPRVFAAPSPRADAIAQVEA
WRAQPNCVLVGPGPRHWDILLRLCDEVGAKHRLVTDAYLAALAVEHGCELVTLDRDFARFAGVRWRHPPA
>gnl|CDD|350246 cd18679, PIN_VapC-Af1683-like, VapC-like PIN domain of VapC ribonuclease similar to Archaeoglobus fulgidus uncharacterized Af1683 protein. Uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LIDTGIFFGFYSLKDVHHMDSVAIVVHAVEGKWGRLFVTNHILDETLTLLKYYKLPADKFLEGFVESGVL
NIIYTDKEVEEKALEVFKARVYEKGFSYTDAISEVVAEELKLTLISYDSRFSLPTI
>gnl|CDD|350247 cd18680, PIN_MtVapC20-like, VapC-like PIN domain of Mycobacterium tuberculosis VapC20 and related proteins. M. tuberculosis VapC20 inhibits translation by site-specific cleavage of the universally conserved Sarcin-Ricin loop in 23S rRNA. This subfamily belongs to the VapC (virulence-associated protein C)-like nuclease family of the PIN domain-like superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1
YIDTSALIALFNKRDKNHETAVSYFESAVTGGIRFVVSRPVLMETLNGLSKRYGKRAAVELYDIILSSRF
VIIENETEEDWEKAWEIFEKYDDQRGMDFVDALSFAIMERLGIRKAFTFDSDFEVYGFYRV
>gnl|CDD|350248 cd18681, PIN_MtVapC27-VapC40_like, VapC-like PIN domain of Mycobacterium tuberculosis VapC27, and VapC40, and related proteins. This subfamily includes Mycobacterium tuberculosis VapC27 and VapC40. It belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
IAVDTSVAVALLVSWHEAHEAARAALRGRRLGLAGHAAFETYSVLTRLPPPHRVAPADAARLLAANFPES
LTLSATAYAALLPELAAAGISGGAVYDALVGAAAAEHGAELLTRDRRAAPTYEALGVEV
>gnl|CDD|350249 cd18682, PIN_VapC-like, Uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
VVLDASALLALLNGEPGAERVEAALPGAVISAVNLAEVVAKLADRGVDPEEIREALAALGLEVVPFDEEQ
ALLAARLRPLTRPLGLSLGDRACLALAIRLGLPVLTADRAWAKLDLGV
>gnl|CDD|350250 cd18683, PIN_VapC-like, Uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
IAVDTNVLVRYLVNDDPEQAARARALLEEAEPVFVPLTVLLELEWVLRSAYKFSRAEIAAALRALLGLPN
VVVEDPEAVEAALDWYRAGADFADALHLAAARRAGCETFVTFDRKAARRAGALGL
>gnl|CDD|350251 cd18684, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
AVVDTNVLIYDTVEDSEYHKEARELLDSLEKWVIPTIVVHELVWFLRKLGLSPDDAKEKVEEYLEDPRFE
VVCEDREDIKSALELLLEEGLSLSRYNDYVILAVAKRLKLPLATFDKKLRKLAKKLGVEVL
>gnl|CDD|350252 cd18685, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains and included distant subgroups, this subgroup includes some sequences belonging to one of these, PIN_14
LLISDANILIDLEEGGLLAAMFQLPYQFAVPDILFFEELEEQHPHLLDLGLQLLELSGESVAYAEELAQK
YRRPSRNDLFALALAKQEQCPLLTGDKALRKAAKKEGVEV
>gnl|CDD|350253 cd18686, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
VVDSSGWIEYFADGPLADEFAPAIEDPEELIVPTIVLYEVYKKILRERGEEAALEAVALMQQGRVVPLDE
SLALAAADLSLEHKLPMADSIIYATARRHGATLWTQDAHFKGLPGVRYF
>gnl|CDD|350254 cd18687, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_3
ARPSRDLIVAAHQQITREWWENRRGRFELYISELVLDEISAGDPEAAQRRLELLADIPVLEITEEVEELA
EAYLAEGALPEKAADDALHIAIATVHGMDYLLTWNCKHIANAEKRPKI
>gnl|CDD|350255 cd18688, PIN_VapC-like, uncharacterized subfamily of the VapC-like nuclease family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LRVLLDTSFLLPTLGIEVGERVAKALERLAGHELYYSSFSILECLWVVARLKKKPKFDIERVELGLSIIE
GGRYRAEEDAEVVKEALRLYRMGHKDMIDNILYASSLSHNLKLLTLDRELKEFIRKKGLEDVFI
>gnl|CDD|350256 cd18689, PIN_VapC-like, uncharacterized subfamily of the VapC-like nuclease family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
VLDSGALLAYFEGEPHKVAKKLIELIKEGKAELYISAINLGEVYYITARKKGEEKAEEVLSLLLALPIEV
VEADEELVEAAAKIKAKYGLSYADCFALATAKELNAALVTGDPEFKKVKEIEIII
>gnl|CDD|350257 cd18690, PIN_VapC-like, uncharacterized subfamily of the VapC-like nuclease family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_12
TLDTSIFDENGLKLESGLLGQLEQFRDSEIRLLIPDVVANEVKSHLKKRLDDFLKRTGAEVIDAEDYVSV
GELMDRYFAGEPPFAETGKKKNEFPDAIALLALEGWAEENDTKILAVSKDNDWQRFCAQSDRLV
>gnl|CDD|350258 cd18691, PIN_VapC-like, uncharacterized subfamily of the VapC-like nuclease family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LFFGDEEELIKKLLTWITIKSPDRYEIKIPASVFYELIEEMRERINRGLRVAEEAVREAAEDGEEKKAET
IGEIIKRLREKYREALREGILDSKEDLDLLLLAKELDAALVSADEGVIKWAEKLGVKEID
>gnl|CDD|350259 cd18692, PIN_VapC-like, uncharacterized subfamily of the VapC-like nuclease family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
FLDTNILVYAFDDDEPEKQARALELLREEAGGGVISTQVLNEFYNVLTRKLKLPLSEIRARLEVLRLLCW
VVVLTPETILEAIRLAERYQLSFWDALIVAAALEAGCSILYSEDLQHGQVIGGLTIVNP
>gnl|CDD|350260 cd18693, PIN_VapC-like, uncharacterized subfamily of the VapC-like nuclease family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_22
LLDSNIIIGLWKQYPFVIDKLIKDKKIKILKEISEELVVKEMRKYKGQRILSQRFCSLLSFIIEIDKKKI
SEFYSIINYKYSNYYATNKLSENDLLLLYACYLNNDLILVTEDKYLFNTSKFLLGEHRV
>gnl|CDD|350261 cd18694, PIN_VapC-like, uncharacterized subfamily of the VapC-like nuclease family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_24
FLDTNIYIIGDLDKNSPESKILEALGYRNKNPILNVEIIFSDELIDQIRRVGKRLYGKDWAGEILSRIWQ
WLDVFYVPVTIEWVQEKEKLGAEKLIPREDVEIYLTAKYGQADCFISGNRELIKAIADFECLT
>gnl|CDD|350262 cd18695, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_13
VLDHTALAALAEGDPFLTGLYIEASRGTGRIVVPSLAVAAAERERPGAGRHAASLRFATFLDFTAAHAVD
TMGWPHTDWPIAHAAAIAWHAIKAGEPLTLLSLDPDLYAGTGITPLNP
>gnl|CDD|350263 cd18696, PIN_MtVapC26-like, VapC-like PIN domain of Mycobacterium tuberculosis VapC26 and related proteins. Mycobacterium tuberculosis VapC26 cleaves 23S rRNA in the Sarcin-Ricin Loop, it is inhibited by the cognate VapB26 antitoxin. This subfamily belongs to the VapC (virulence-associated protein C)-like nuclease family of the PIN domain-like superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
IIDTGALLALFDAADPDHAAVRECIQRSADALVVSPYVVTELDYLLATRVGNDAELAVLQELAGGAFELA
NCGAAEIEQAARIVKKYQDQRIGLADAANVVLADNYGTATILTLDRRHFSALRPIDGSRFTV
>gnl|CDD|350264 cd18697, PIN_VapC_N-like, VapC-like N-terminal PIN (DUF4935) domain of DUF4935 domain-containing proteins and related proteins. This subgroup the includes N-terminal PIN domain of DUF4935 domain-containing proteins, and is an uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
MLDTCVWLDISSQKAELPMLTALEHLVSDGVIKILIPDLVRTEYERNKDRVAEATRKRLASEFKVVKGVI
ESFGGEGKDTALETLDDVNHRLPILSEANYGTVNRVEKLFDSAVEVPISDAAKIKAAERAIAKKAPFHKQ
KNSVADAVLIETFQEFRLENASEYESFRFVTHNVNDFSGKDHR
>gnl|CDD|350265 cd18698, PIN_VapC_C-like, VapC-like C-terminus of DUF1308 domain in DUF1308 domain-containing proteins and related proteins. This subfamily includes the C-terminus of DUF1308 domain in DUF1308 domain-containing proteins, and is an uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDQAVILTMCSNLSCGLSDSYYESTKENINKDTVITSKNEIDEYLNNKQLLVCQSVYDQTKVKMEFTAG
PQETIRFLELLTKITIVPDCQNDRFLKMKTKENEIICISVAEREGATIVTNNKHIYKKISLFYQEIPC
>gnl|CDD|350266 cd18699, PIN_VapC_like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_15
LLDTNIIIHREDDKIVNPDIGILFRWLDKLHYEKCIHPLSIEEIRKDKDPKRREAILSKLESYPILKTPA
PPNEDVLKISVGTDKNSNDIIDNKLLNEVYKNRVDFLITEDKKIHKKAIRLGISDRVFS
>gnl|CDD|350267 cd18700, PIN_GNAT-like, VapC-like PIN domain of uncharacterized GNAT family proteins. This subfamily includes uncharacterized GNAT family proteins having an N-terminal GNAT family N-acetyltransferase domain. This subgroup belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_17
ALDANIFADLRDSTDRNGAEESKALLADWLVDLVELYYTPELYNEINRLDDTAERRHQTRALLGYFTLEP
CQAAVDERVARLIRKGIILGITPNDISDLRQLAEAIASGVQFFVTRDPGLLNLRDVAEEVFGVRILR
>gnl|CDD|350268 cd18701, PIN_VapC_like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_18
VADADVLAADLLVDGPARAALDHLRRHSWTTLVASDPLLDDAEAVISSLADADLAADWREKVDDWAELVD
HPDGDHPALASAYRGGAMHLLTFDDRLRSAQAGAALGGRFPVSVRHPKAFASLFAPESLYAEVEDGPYPG
PDRD
>gnl|CDD|350269 cd18702, PIN_VapC_like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_19
LIDTNLLLLLLVGLYDRGYIEKHKRTSEYTSEDFDLLLELLSQFSKIITTPNILTEVSNLLNQLGEPARS
EIFEVLAELIENLEEHYIPSKDIAASPEFFRLGLTDAGILELAKSGYLLLTDDLDLYLYAQKLGIDAIN
>gnl|CDD|350270 cd18703, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_20
ILDAGPALNFFATNKERLLIAALGPISVPETVRFEILRKPKRDPRFRAAEKVWKKLPPRFLEVLSDDPTP
ELDRAVNRVSGLPLEERYAHAKDLGETMVIAHAVVRAEAGEDVVVLIDDGGGAALAKKEIRRLDRLRSQG
PGVGSIAL
>gnl|CDD|350271 cd18704, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_21
CPDTNVLYHRFLSSSGIIDPYEVVLVDTVKEEIEAALNFKYSPKQISEIKRSAKYQPFLLDEFVNRRMKK
SRKAAYLALAEYRLRDLAREIEGVEESTDDSEENDRIIVKSLRRFEKERPSLPVLLTADIQMADLCEAEG
VEYFL
>gnl|CDD|350272 cd18705, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_23
VFDTSVLTTDVIAATLRMTPSSIVAGMRAGTLRGFIPHHVWAEVPRVLADRKREGGAFDLEAAERLWWDE
YLPLLHVVTTTGLPMTPAADKLAVEDLSDVPTAQLAGLLGPVVLFAEDTDLVDPGIAPGD
>gnl|CDD|350273 cd18706, PIN_STKc_like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily; includes the PIN domains of uncharacterized serine/threonine kinases. This subfamily includes the PIN domains of some uncharacterized proteins having serine/threonine kinase catalytic domains and annotated as serine/threonine kinases. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_25
YIDTCSLLNEYSEAFMELLLPYLRKFGQKVIVPPSVLAELRKLLQKDPRKALARKAQRVLCLLQSEGLLV
LIGEAEDRFADQDFISLFVRFMTKYDLLLITQDKGLAADLLALNDFRSVKGKRLWV
>gnl|CDD|350274 cd18707, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_26
SLDTNVIIHLYRAGCQNLLFEFLEGVFIVEQIRSIELKNHGKDILDKVDEDIKDGKIELYSDYDLVLLGL
FRVFEEVEENRDLYFPGDLGEVYAIALAQTLGAFSLVTDDTKQGGPYMSLLQFIDEVMPFL
>gnl|CDD|350275 cd18708, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_28
VADTNVYINLGNRLGRLTYSEYGRRLLPSRSVYNELDNKTTTTQKDENLYKFILGMESYRSLHKPPISSK
NRSSGDVELIEETKRLKSYLPDKVVLITADQGLGNSARSKGIRVIL
>gnl|CDD|350276 cd18709, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_4-1
VLDTNFLIQCASKNLPLEHFYPHIRKQYPHLEGKSLITVVVPFTTVREAYQIIWSPSTHLKRSVRLLLWS
RVTSLLRQPSVYVLSIASEFPCSSLSIITRMAYHSRLNEPASENDPDLRILNVCLALQYALRQRKAASLQ
GGSQISEGTMLFSFLKYHVRRHHNDVKGVATDQLLLCTLDKRLSRAADELGVQTFP
>gnl|CDD|350277 cd18710, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_4-2
VFDLSALLSTDTREWQEFSRLGECYLPQVVYEEIEFLADRASEPEQEKTAREFLRFFPESGWQVTDASAT
HPALEPAEGQNLSKRARLDLAIAECAYGLALENPHSLVVLVTNDQPLLQRIQQLGQPNLC
>gnl|CDD|350278 cd18711, PIN_VapC-like_DUF411, VapC-like PIN (DUF411) domain in DUF411 domain-containing proteins and related proteins. This subfamily includes the DUF411 PIN domain in proteins annotated as DUF411 domain-containing proteins. It is an uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
VFDTSSFSDLFHYYPDVFPSLWEKFDELVSNGKIISTREVLRELEDGNKDDELLAWAKDNKAIFTTPTAE
ELRFVAEIFAVPHFQALIEEKKRLKGGPVADPFVIAKAKVKGGTVVTEEKLKPNAAKIPNVCEHFGIPCI
NLEEFM
>gnl|CDD|350279 cd18712, PIN_VapC-like_DUF411, CapC-like PIN (DUF411) domain in DUF411 domain-containing proteins and related proteins. This subfamily includes the DUF411 PIN domain in proteins annotated as DUF411 domain-containing proteins. It is an uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTNVFRYKANPRAHKSYKKAAKRFWKNVLQEIRNGESILYIPKEVIRELEVQSYTLSPKENQRIAQLL
EPIEEVLPDLATPEIEHQIRKISAYVRSEYKSDINAARKMEYPSVSDARILLAAYQNDCILVTANIKDFM
LYPLLFPQ
>gnl|CDD|350280 cd18713, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_27
LVEGLINEDFKAKFYTSNLVLAEMTRVLYDELISEKMRSEGIPLIYWSKYRKKFLLTDEEFFEFKEAVIK
LSNLIRERLNVIVNEVFDVEYYPKLILRYGLMTQDAILLTTAIKSGCNYFITMDRDFHELIRDKRLRKVK
>gnl|CDD|350281 cd18714, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_8
VFDTNCLLNLYRCEEHTREDILEVMEALSSRTWIPFQVGYEYQRNRRKVIEDSINSLEKIKKELQKIYTQ
NILSSGSIKKHLYSSLSDELSDLQSEIKKPIEEFIESKIDPRISSKKKISNHDFIRDEIDKIIEDNIGSL
PTQEKIDKINKEGEKRYKNKIPPGFKDAKKKSNSFFSGIELQDKYGDLYLWMEIIEKAKSEEIKNVIFVC
DDAKEDWWYIHNGKTHGP
>gnl|CDD|350282 cd18715, PIN_VapC-like, uncharacterized subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
RVVLDTNILISALISPHSPPDLIYRAWRAGRFELVTSEEQLDELRRVSRYPKLQARLQPAEAGTMVNNLR
RLAVMLERLPIVEESPDPDDNFLLAMALAGDADYLVTGDKRDGLLLRGHIGRTRI
>gnl|CDD|350283 cd18716, PIN_SSO1118-like, VapC-like PIN domain of Sulfolobus solfataricus SSO1118 and related proteins. This subfamily includes the functionally uncharacterized protein SSO1118 from the hyperthermophilic archaeon Sulfolobus solfataricus P2. This subfamily belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
YAVISPSAFGKLKEILGSLKGYKFVITTLGVSYALKNGIDIDFALDRGVIVRAFSHKPPKIGGLPIYESE
AIMVALELNALLVASDEDVKKKAEKLGVKVVS
>gnl|CDD|350284 cd18717, PIN_ScNmd4p-like, VapC-like PIN domain of Saccharomyces cerevisiae Nmd4p and related proteins. Saccharomyces cerevisiae Nmd4p may be involved in nonsense-mediated mRNA decay. This subfamily belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
ILDASAFEKGLGNIKRWCDDNTKQNKVTLNLYIPTYTLQELDFLQYKRKSFNAKEALKFIDELTNSQNFK
LIIEFPEILDAILWSDVLRFSEGSLGKDSINKLPRRFKNLLKSCVYKCHLEENDDKKWILVTEDPKVREI
ADQCNIPWCS
>gnl|CDD|350285 cd18718, PIN_PRORP, PIN domain of protein-only RNase P (PRORP) and related proteins. PRORPs catalyze the maturation of the 5' end of precursor tRNAs in eukaryotes. This family includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3, PRORP1 localizes to the chloroplast and the mitochondria, and PRORP2 and PRORP3 localize to the nucleus. This subfamily belongs to the PRORP-Zc3h12a-like PIN family which in addition includes Zc3h12a (also known as MCPIP1/MCP induced protein 1 and Regnase-1), Caenorhabditis elegans REGE-1 (REGnasE-1), Zc3h12b-d (also known as Regnase-2-4), N4BP1, and NYNRIN (also known as CGIN1). The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
VVIDGLNVAYYGQNFPGGFNAQQLLAVVEHLQKQNKKVLVLGRKHMLKWSRWSPSAMKLIEKNASLFFTP
NGSNDDPFWLYAALKSGPKTLFVSNDLMRDHKFQLLDELQRLFKKWQERHQVRF
>gnl|CDD|350286 cd18719, PIN_Zc3h12a-N4BP1-like, PRORP-like PIN domain of ribonuclease Zc3h12a, NEDD4-binding partner-1, and related proteins. Zc3h12a (zinc finger CCCH-type containing 12A, also known as MCPIP1/MCP induced protein 1 and Regnase-1) is a critical regulator of inflammatory response, with additional roles in defense against viruses and various stresses, cellular differentiation, and apoptosis. This subfamily also includes Caenorhabditis elegans REGE-1 (REGnasE-1), which also functions as a cytoplasmic endonuclease. Additionally, it includes three less-studied mammalian homologs: Zc3h12b-d/Regnase-2-4, as well as N4BP1 (NEDD4-binding partner-1), NYNRIN (NYN domain and retroviral integrase containing, also known as CGIN1/Cousin of GIN1), and KHNYN (KH and NYN domain containing) protein. N4BP1, CGIN1, and KHNYN proteins are probably of retroviral origin. This subfamily belongs to the PRORP-Zc3h12a-like PIN family which in addition includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
VVIDGSNVAMSHGNGKVFSCKGIQICVRYFLERGHEVTAFVPQFRLESPNPNSTDQDILEELERLGILVF
TPSRRVPGKRISSYDDRFILQLAEETDGVIVSNDNFRDLLNENPDWREIIEERLLPF
>gnl|CDD|350287 cd18720, PIN_YqxD-like, LabA-like PIN domain of uncharacterized Bacillus subtilis YqxD and related proteins. This subfamily includes the PIN domain of uncharacterized Bacillus subtilis YqxD (also known as YqfM) and Escherichia coli YaiI. Firmicute, such as Bacillus and Listeria, YqxD proteins are encoded within RNA polymerase major sigma43 operons, whereas E. coli YaiL is transcribed as a mono cistron. This subfamily belongs to LabA-like PIN domain family which includes Synechococcus elongatus PCC 7942 LabA, human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
KIWVDADACPVKIKEILFRAAERLQIPVIFVANQPLRLPPSPLIRWIVVDSGFDAADDYIVEHVEPGDLV
ITADIPLAALVVEKGAYVLNPRGELY
>gnl|CDD|350288 cd18721, PIN_ZNF451-like, LabA-like PIN domain of human zinc finger protein 451 and related proteins. Human ZNF451 (also known as COASTER) functions as a transcriptional cofactor in promyelocytic leukemia bodies in the nucleus, it acts as a coactivator or corepressor, depending on the factors with which it interacts. ZNF451 interacts with p300 by the PIN-like domain and down regulates TGF-beta signaling in a p300-dependent and sumoylation-independent manner. This subfamily belongs to LabA-like PIN domain family which includes Synechococcus elongatus PCC 7942 LabA, human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_11
HIVFVDLDNWSGFFKHLPGHLPQGTFVWGFQGGNTNWKPPKSCKIYNYLNRIGCFFLHPRCGKTKDAADF
AICMHAGKLDERLPKQIPFTILSGDKGFLELENQFKKTQRPAHILNP
>gnl|CDD|350289 cd18722, PIN_NicB-like, LabA-like PIN domain of Pseudomonas putida S16 NicB and related proteins. Curiously NicB from Pseudomonas putida S16 is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine. This subfamily also includes the uncharacterized CPP15 (plasmid) protein from Campylobacter jejuni. This subfamily belongs to LabA-like PIN domain family which includes Synechococcus elongatus PCC 7942 LabA, human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
RTAVYVDGFNLYYGLKAREELKLYRYYWLDLPPLAKNLLLPDPSQELLERVKYFTARVNSSPKEEKGVDV
NIALDILSDAYKKQVDQAVLVSGDSDFVPAVKLARREPGIRVGLAFP
>gnl|CDD|350290 cd18723, PIN_LabA-like, uncharacterized subfamily of the LabA-like PIN domain of Synechococcus elongatus LabA (low-amplitude and bright) and related proteins. The LabA-like PIN domain family includes Synechococcus elongatus PCC 7942 LabA which participates in cyanobacterial circadian timing, it is required for negative feedback regulation of the autokinase/autophosphatase KaiC, a central component of the circadian clock system, and appears to be necessary for KaiC-dependent repression of gene expression. It also includes the N-terminal domain of limkain b1, a human autoantigen localized to a subset of ABCD3 and PXF marked peroxisomes, human ZNF451, uncharacterized Bacillus subtilis YqxD, uncharacterized Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously Pseudomonas putida S16 NicB, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into this family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_7
RIALIDYENCCNLRNISLADYTDLILFAGPLQQTVVLPADTWPDNIRVSIRQIDNISKNNVDFHLVMELG
RMTCCSAGNNTWHIISNDKGYDGIIHTLQKRGFRCERIAP
>gnl|CDD|350291 cd18724, PIN_LabA-like, uncharacterized subfamily of the LabA-like PIN domain of Synechococcus elongatus LabA (low-amplitude and bright) and related proteins. The LabA-like PIN domain family includes Synechococcus elongatus PCC 7942 LabA which participates in cyanobacterial circadian timing, it is required for negative feedback regulation of the autokinase/autophosphatase KaiC, a central component of the circadian clock system, and appears to be necessary for KaiC-dependent repression of gene expression. It also includes the N-terminal domain of limkain b1, a human autoantigen localized to a subset of ABCD3 and PXF marked peroxisomes, human ZNF451, uncharacterized Bacillus subtilis YqxD, uncharacterized Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously Pseudomonas putida S16 NicB, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into this family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
VHVFVDNSNIFIGFQDALKVARGLPPSRRVRILLSFGNLALILERGRPVARRVLVGSSPPYNDAAWAVRL
GYEVSILERVPKEGDSTKRSDSSSSPGRERGKEQGVDEILHLKILESILDYDTPGTIVLATGDGNEAEFS
DGFPAVVERALKRGWKVELYSWKSGLSRAWKD
>gnl|CDD|350292 cd18725, PIN_LabA-like, uncharacterized subfamily of the LabA-like PIN domain of Synechococcus elongatus LabA (low-amplitude and bright) and related proteins. The LabA-like PIN domain family includes Synechococcus elongatus PCC 7942 LabA which participates in cyanobacterial circadian timing, it is required for negative feedback regulation of the autokinase/autophosphatase KaiC, a central component of the circadian clock system, and appears to be necessary for KaiC-dependent repression of gene expression. It also includes the N-terminal domain of limkain b1, a human autoantigen localized to a subset of ABCD3 and PXF marked peroxisomes, human ZNF451, uncharacterized Bacillus subtilis YqxD, uncharacterized Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously Pseudomonas putida S16 NicB, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into this family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
KTNAKLKKHFKQLHERERQKRLNRLESLKGKKRKKFRAKLKEKEEKYRAAARQVLVPKVGYGLATELRRA
GVYVRTVEDKPQAADKALKSHIMAVINKGVDCLCLVSDDSDFGDILRRARRRNLRTVVVGD
>gnl|CDD|350293 cd18726, PIN_LabA-like, uncharacterized subfamily of the LabA-like PIN domain of Synechococcus elongatus LabA (low-amplitude and bright) and related proteins. The LabA-like PIN domain family includes Synechococcus elongatus PCC 7942 LabA which participates in cyanobacterial circadian timing, it is required for negative feedback regulation of the autokinase/autophosphatase KaiC, a central component of the circadian clock system, and appears to be necessary for KaiC-dependent repression of gene expression. It also includes the N-terminal domain of limkain b1, a human autoantigen localized to a subset of ABCD3 and PXF marked peroxisomes, human ZNF451, uncharacterized Bacillus subtilis YqxD, uncharacterized Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously Pseudomonas putida S16 NicB, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into this family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
IALIVDGPNMLRKEFNLDLEEIREALEELGRIRVGKVVLNQYASEKLIEAVINSGFEPIISSGDVDVALA
VEAMELIYNPKIDVIALATRDADFLPLLMKAKEMGKETIVIGA
>gnl|CDD|350294 cd18727, PIN_Swt1-like, VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins. Saccharomyces cerevisiae mRNA-processing endoribonuclease Swt1p plays an important role in quality control of nuclear mRNPs in eukaryotes. Human transcriptional protein SWT1 (RNA endoribonuclease homolog, also known as HsSwt1, C1orf26, and chromosome 1 open reading frame 26) is an RNA endonuclease that participates in quality control of nuclear mRNPs and can associate with the nuclear pore complex (NPC). This subfamily belongs to the Smg5 and Smg6-like PIN domain family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo
VLDTNVLISHLDLLKQLVEDVEKLSLPVVIVIPWVVLQELDGLKKSKRKSSLGWLARRASTWLLEKLRSK
HPRVRGQALSETLRASGDPGESNDDAILDCCLYFQEKYGAPVVLLSNDKNLCNKALINGIPTISPEEGMT
A
>gnl|CDD|350295 cd18728, PIN_N4BP1-like, PRORP-like PIN domain of NEDD4 binding protein 1 and related proteins. NEDD4-binding partner-1 (N4BP1) interacts with and is a substrate of NEDD4 ubiquitin ligase (neural precursor cell expressed, developmentally down-regulated 4, E3 ubiquitin protein ligase). It is also an inhibitor of the E3 ubiquitin-protein ligase ITCH, a NEDD4 structurally related E3. This subfamily additionally includes NYNRIN (NYN domain and retroviral integrase containing, also known as CGIN1/Cousin of GIN1), and KHNYN (KH and NYN domain containing) protein. N4BP1, CGIN1, and KHNYN proteins are probably of retroviral origin. This subfamily belongs to the Zc3h12a-N4BP1-like PIN subfamily of the PRORP-Zc3h12a-like PIN family, the latter of which additionally includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
IVIDGSNVAMVHGLQHFFSCRGIAIAVEYFWKRGHRNITVFVPQWRTKRDPNVTEQHFLTQLQELGILSL
TPSRMVLGKRIASHDDRFLLHLAEKTGGIIVTNDNFREFVNESPSWREIIKERLLQY
>gnl|CDD|350296 cd18729, PIN_Zc3h12-like, PRORP-like PIN domain of ribonuclease Zc3h12a and related proteins. Zc3h12a (zinc finger CCCH-type containing 12A, also known as MCPIP1/MCP induced protein 1 and Regnase-1) is a critical regulator of inflammatory response, with additional roles in defense against viruses and various stresses, cellular differentiation, and apoptosis. This subfamily also includes three less-studied mammalian homologs: Zc3h12b-d/Regnase-2-4. It belongs to the Zc3h12a-N4BP1-like PIN subfamily of the PRORP-Zc3h12a-like PIN family, the latter of which additionally includes human PRORP, also known as proteinaceous RNase P and mitochondrial RNase P protein subunit 3 (MRPP3), and Arabidopsis thaliana PRORP1-3. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
IVIDGSNVAMSHGNKEVFSCRGIQLAVDWFRERGHRDITVFVPSWRKEQPRPDAPITDQEILRELEKEKI
LVFTPSRRVGGKRVVCYDDRFILKLAYESDGIVVSNDNYRDLQNEKPEWKKFIEERLLMYS
>gnl|CDD|350297 cd18730, PIN_PH0500-like, VapC-like PIN-domain of Pyrococcus horikoshii protein PH0500 and related proteins. This subfamily includes Pyrococcus horikoshii protein PH0500, a protein with possible exonuclease activity and involvement in DNA or RNA editing. This subfamily belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
ITFDSSALIKMHTKQNKRLLEFTLAKFEVFVPIISVYAYLLTKAYLGKNPEEELKILKEIYNIVPLDDEI
IVKAAEIEASLLKKGVFLDLEDLLTAVTAIVTNSLLVTDDPERYEPLRKYGLDVIP
>gnl|CDD|350298 cd18731, PIN_NgFitB-like, VapC-like PIN domain of Neisseria gonorrhoeae FitB and related proteins. This subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Neisseria gonorrhoeae FitB toxin of the FitAB toxin/antitoxin (TA) system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. In N. gonorrhoeae, FitA and FitB form a heterodimer: FitA is the DNA binding subunit and FitB contains a ribonuclease activity that is blocked by the presence of FitA. A tetramer of FitAB heterodimers binds DNA from the fitAB upstream promoter region with high affinity. This results in both sequestration of FitAB and repression of fitAB transcription. It is thought that FitAB release from the DNA and subsequent dissociation both slows N. gonorrhoeae replication and transcytosis by an as yet undefined mechanism. The toxin M. tuberculosis VapC is a structural homolog of N. gonorrhoeae FitB, but their antitoxin partners, VapB and FitA, respectively, differ structurally. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
IVLDTNVVSELMRPAPDPAVLAWLDAQPAEDLYLTAITVAELLYGIALLPDGRRRDALEAAAEALLAEDF
AGRILPFDAAAAEAYAEIVAARRRAGRPISVADAQIAAIARAHGATLATRNVKDFEGLGLELINPW
>gnl|CDD|350299 cd18732, PIN_MtVapC4-C5_like, VapC-like PIN domain of Mycobacterium tuberculosis VapC4, VapC5, and related proteins. This subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 toxin of the VapBC toxin/antitoxin (TA) system. This family belongs to the PIN_VapC4-5_FitB-like subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. M. tuberculosis VapC4 interacts with, and cleaves tRNA44Cys-GCA. M. tuberculosis VapC5 has endonucleolytic activity with RNA, this activity is low with dsRNA, and no activity has been demonstrated on dsDNA. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTSVVIDLERGDPADLPDEVAISAITLAELAFGVLAADTRAERAQRLQRLLQAEDFDPLPFDAEAARA
YGRLAAAVRAAGRKPRPRANDLLIAATAIAHGLPLLTRNPDDFAGLDGLVRVVT
>gnl|CDD|350300 cd18733, PIN_RfVapC1-like, VapC-like PIN domain of Rickettsia felis VapC1 and related proteins. This subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Rickettsia felis VapC1, a ribonuclease toxin of the VapBC toxin/antitoxin (TA) system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC TA systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
GLIIDTSVFIAAERGRLDLEALQQERPDEDVYISAITASELLHGVHRAKTPERRARREAFVEAILEAFPV
LDFDLEVARTHARLWAELAKRGITIGAHDLLIAATALAHGYSVLTANVRDFKRIPGLEVEE
>gnl|CDD|350301 cd18734, PIN_RfVapC2-like, VapC-like PIN domain of Rickettsia felis VapC2 and related proteins. This subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Rickettsia felis VapC2, a ribonuclease toxin of the VapBC toxin/antitoxin (TA) system. Rickettsia felis VapC2 cleaves single-stranded RNA. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC TA systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
MLDTNICVYLIKKKPDSYYARLEKLQKNNDIAISSIVLAELQYGVSKSQYKEQNQAALNMFLMKLEVLPF
EEKATFYYGEIRAELEKSGQVIGGNDLLIAAHALAENATLVTNNIKEFARVPNLILENW
>gnl|CDD|350302 cd18735, PIN_HiVapC1-like, VapC-like PIN domain of Haemophilus influenzae VapC1 and related proteins. Haemophilus influenzae VapC1 has endonucleolytic activity with RNA, it cleaves initiator tRNA between the anticodon stem and loop, but does not cleave mRNA, rRNA or tmRNA, and has no activity on ssDNA or dsDNA. This subfamily belongs to the PIN_VapC4-5_FitB-like subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC TA systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. FitB is a toxin of the FitAB TA system. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTNICIYIRKQRPPSVLERFAQLQPGEVAMSVITYGELLYGAEKSQRRAKALEALERLAELIPVLPLP
EEVAEHYGEIRADLEKKGTPIGNNDLWIAAHALALGLTLVTNNTREFQRVPGLKVENW
>gnl|CDD|350303 cd18736, PIN_CcVapC1-like, VapC-like PIN domain of Caulobacter Crescentus VapC1-like and related proteins. This subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Caulobacter Crescentus VapC1, a ribonuclease toxin of the VapBC toxin/antitoxin (TA) system. This subfamily belongs to the PIN_VapC4-5_FitB-like subfamily of the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC TA systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. FitB is a toxin of the FitAB TA system. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTNICIYLLKGQPPALARRVAACEPGEVVISAITLAELAYGVRRSAPPRRAALDALLEVIPVLPFDEA
AAAAYARIRAAFPFRRASFDRLIAAHALALGLTLVTNNEADFADIPGLRVENW
>gnl|CDD|350304 cd18737, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LFDTNILIDYLNGVPQARAELERYEQPAISVITWMEVLVGAPPEEEEATRAFLSSFEIIPLDQAIAERAV
ALRRQSRLKLPDAIILATAQVHGLILVTRNTKDFPASMPGVRVPY
>gnl|CDD|350305 cd18738, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTNIIIYYLKGELPESLEELLEELNEPAISVITKIELLGWPKLTPEEEEEIEDFLSLAEVIPLDDEIA
RKTIELRKQYKIKLPDAIIAATALVHGLTLVTRNVKDFKKIPGLKLLN
>gnl|CDD|350306 cd18739, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
CLDSSFLIDYLDGVDAAQAFLESQEDEPLVTPTIALYEVYVGAVRSAGETDLDGVREDLDWVEPLDFDEE
VAREAAQIQAELLEAGEPINPPDLMIAATARSLGATLVTRDGDFERIDGLEVEN
>gnl|CDD|350307 cd18740, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
MLDTNTVSHIIKGRPPAVRERLRAVPMASICISSITEAELLYGLAKRPEAKRLHAAVREFLLRVDVLPWD
SSVARTYGDLRAALEAQGKTLGPLDMMIAAHALALGATLVTNDRAFRRVPGLAVED
>gnl|CDD|350308 cd18741, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTDILIDFLRGNPSAAEKLLELLGGNLAISVITVAELYAGARNKKELEKLEKLLSLFEVIPVDEEIAE
LAGELRRKYRKSHGLGLPDALIAATALEHGLTLVTLNVKHFPMIEGLKLP
>gnl|CDD|350309 cd18742, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTDICIYWLKGNESVKEKFLEVGNEPLSISVITYAELYYGAYNSQRVEKNLARVERFKELLPVLPLSE
AIAETFGKIKADLRKKGNPIDDFDLLIASTALANNLILVTNNTKHFKRIPGLKIENW
>gnl|CDD|350310 cd18743, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTNICIFLLRGKYGVAEKIEEVGLENCFISEITIAELLYGAENSARPEKNRKLVDDFLSLFTVLPISD
ALEEYAKEKARLRRQGKLIDDFDLLIGATAIANNLTLVTENVKHFARIPGIKLENWI
>gnl|CDD|350311 cd18744, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTDILSALLKGNPKVVEKFREYLKEYGKITISIITYYEILRGLLAKNATKQLEVFEEFCSNNEVLPLD
DESADIAAEIYADLRKKGTLIDDADILIAATAIANNLVLVTNNTKHFQRIEGLKLENW
>gnl|CDD|350312 cd18745, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
YLLDTNTVIALFRGRGPVLRARLRAAAPSDLALSSIVLYELEYGAAKSARPERNRARLEELLSLIEVLPF
DEEDARAAAEIRADLERAGTPIGPYDTLIAGQALARGATLVTHNVREFSRVPGLKVEDWY
>gnl|CDD|350313 cd18746, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTNVISELRKPRPDPGVVAWLAAVDEDDLFLSVITIGEIRKGIERLRRRDPARAARLEAWLDGLLLRF
AGRILPVDAEVARRWGRLHAPAPAPLPVADALIAATALVHGLTLVTRNVRDFEGTGVPLLNPW
>gnl|CDD|350314 cd18747, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTNILSEPLKPEPNANVLARLERHEGEIAIAAVVWHELLYGCYRLPEGKRKRILEYYLEDVVSGLPIL
PYDEAAAEWHAEERARLTAIGKTPPFADGQIAAIAVANNLILVTRNTKDFQGFEGLRLENWF
>gnl|CDD|350315 cd18748, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTNIISDLIRNPRGKVARRIREVGEDAVCTSIIVASELRFGAAKKGSERLARRVEAVLSRIPVLPLEP
PADEHYARIRADLERQGTPIGPNDLLIAAHALALDLTLVTDNTREFSRVPGLKVENWL
>gnl|CDD|350316 cd18749, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
VLDTDVASYLFKGRLLAALYAPRLVGKILVISFVTVAELYFWAEKRGWGEKRLQQLEAWLSRYVVLPYDE
EIARTWGRLRAEAQRRGRPRPTNDAWIAATALTHGLPLATHNVKDFEDFPGLQLIS
>gnl|CDD|350317 cd18750, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTCTISDFVRGNPNTLERLKSTSPSLIAISSITVMEIEYGLRLNPQRAKKLRPILEAFLSSITILPFD
EEDAIAAAAIRAALKKQGTPIGAYDVLIAGTALAHGLILVTSNTKEFQRVDGLVIEN
>gnl|CDD|350318 cd18751, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTDILSEILKGKNPQVVARARAYLAAFGRYTISVITVMEVVRGLQKVQRAERLQQFLEMIESAEVLPL
DRTAAELAGRIYADLERTGQPIGRADPMIAAIALRHGLVLVTGNTAHYQRIQELGYPLVLENW
>gnl|CDD|350319 cd18752, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LFDTDAISELLKKRPSPPLLERLNSIPREDQFTSAITVGELYYGAYRSDRRLRLLEELLEPVISRVTILP
FDRESARVYGRLRAELEKKGTPLGEADLQIAAIALAHNLTLVTGNIRHFERIPGLRVENW
>gnl|CDD|350320 cd18753, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LLDTNAYSALLRGDPAVLEALARADEIYLPVIVLGELLFGFRKGSREEENRERLEEFLSSPRVEVLPIDE
ETAEIYAEIKSALKKKGTPIPENDIWIAALALEHGLPLVTRDAHFDKIPGLKL
>gnl|CDD|350321 cd18754, PIN_VapC4-5_FitB-like, uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily. The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
ILDTSFLIDLMRGDEAAIEKARELESESVPQRVSSPTVFELYVGVGLSAAPEEERERIESVLESKPILPL
DGESARKAGRIDGQLRREGEPIDPGDAMIAATALVHDEPVLTRNVKHFERIDGLEVES
>gnl|CDD|350322 cd18755, PIN_MtVapC3_VapC21-like, VapC-like PIN domain of Mycobacterium tuberculosis VapC3, VapC21 and related proteins. This subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC3 and VapC21 toxins. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LIDTSALVRLLRPAVAARWEPLIERGLVAICGPTELEILYSARSAADRDRLLRLLRAFPWLPVPDEAWRR
ALEVQRLLARRGQHRAASIPDLLIAATAELHGLTVLHYDRDFDTIAAVTGQPVEWVV
>gnl|CDD|350323 cd18756, PIN_MtVapC15-VapC11-like, VapC-like PIN domain of Mycobacterium tuberculosis VapC11, VapC15, and related proteins. This subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC11 and VapC15 toxins. M. tuberculosis VapC11 and VapC15 cleave tRNA3 Leu-CAG, VapC11 may additionally cleave tRNA13Leu-GAG and tRNA10Gln-CTG. This subgroup belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LVDTSAWIEYLRATGSPADREVRELLGEGGPVATTEPVAMELLAGARDEAHLARLRRLLNGLRLLPLDPA
LDFEAAAAIYRACRRGGHTVRSLIDCLIAAVAIRHGATLLHRDRDFDVIARVTPLRLVS
>gnl|CDD|350324 cd18757, PIN_MtVapC3-like, uncharacterized subgroup of the VapC3-like nuclease subfamily of the PIN domain superfamily. The VapC3-like nuclease subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of various Mycobacterium tuberculosis VapC toxins including VapC3, VapC11, VapC15, VapC21, VapC25, VapC28, VapC29, VapC30, VapC32, VapC33, VapC37, and VapC39. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LVDTSVWSLALRRKAPDESKIVQELRELIEDGRVVMIGPIRQELLSGIRDAAQFERLKNKLRAFPDLPLT
TEDYEKAAEFFNICRSKGIQGSNTDFLICAVAVRHDLPIFTTDKDFEHYAKHLPIRLHR
>gnl|CDD|350325 cd18758, PIN_MtVapC3-like, uncharacterized subgroup of the VapC3-like nuclease subfamily of the PIN domain superfamily. The VapC3-like nuclease subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of various Mycobacterium tuberculosis VapC toxins including VapC3, VapC11, VapC15, VapC21, VapC25, VapC28, VapC29, VapC30, VapC32, VapC33, VapC37, and VapC39. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LIDTSVWIEALRPRGSPKVKEKVREALSEDRVATTGIIILELLRGAKTEKEYEELKEDLEALPYLPIEEE
VWERAAKLGFDLRRKGLRVPLTDLLIAAVALKHNCELLHADRHFDLIAKHSPLKVES
>gnl|CDD|350326 cd18759, PIN_MtVapC3-like, uncharacterized subgroup of the VapC3-like nuclease subfamily of the PIN domain superfamily. The VapC3-like nuclease subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of various Mycobacterium tuberculosis VapC toxins including VapC3, VapC11, VapC15, VapC21, VapC25, VapC28, VapC29, VapC30, VapC32, VapC33, VapC37, and VapC39. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LVDTSVWIEFFRGKSSPVSEVVDELLDEDEVCTCGIVLAELLQGAKSEKELSLLEDFLSALPYLPITDEL
WIKAGELSFSLRKKGITIPLSDLYIAALAIENNLELFTLDKHFEIIPKHTGLKLYG
>gnl|CDD|350327 cd18760, PIN_MtVapC3-like, uncharacterized subgroup of the VapC3-like nuclease subfamily of the PIN domain superfamily. The VapC3-like nuclease subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of various Mycobacterium tuberculosis VapC toxins including VapC3, VapC11, VapC15, VapC21, VapC25, VapC28, VapC29, VapC30, VapC32, VapC33, VapC37, and VapC39. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LVDSSVWIDYFNGRPTPQTDRLDALLGREPILIGDLILTEVLQGFRDDRDFRQARRLLLSLPVVEMLGPE
LAIKAARNYRALRKKGITIRKTIDVIIATFCIENGHPLLHNDRDFDPFEEHLGLKV
>gnl|CDD|350328 cd18761, PIN_MtVapC3-like, uncharacterized subgroup of the VapC3-like nuclease subfamily of the PIN domain superfamily. The VapC3-like nuclease subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of various Mycobacterium tuberculosis VapC toxins including VapC3, VapC11, VapC15, VapC21, VapC25, VapC28, VapC29, VapC30, VapC32, VapC33, VapC37, and VapC39. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LIDTSVWISVLRDKTGRVRQQLETLIGGRDVVLTRFTQLELLQGARDEREWQLLSDYLETQDYLEATPST
WSAAARIYFDLRRQGLTVRSPIDCCIAQLALENDLTLLHDDRDFETIAQVRPLQQLR
>gnl|CDD|350329 cd18762, PIN_MtVapC3-like, uncharacterized subgroup of the VapC3-like nuclease subfamily of the PIN domain superfamily. The VapC3-like nuclease subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of various Mycobacterium tuberculosis VapC toxins including VapC3, VapC11, VapC15, VapC21, VapC25, VapC28, VapC29, VapC30, VapC32, VapC33, VapC37, and VapC39. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LVDTSVLIDYLKGKDNKPTEKFDEILDRDIPFGINSYIYQEVLQGAKTEKEFNLLKEYLSTQRFYHLKDG
IESYEEAAKIYFRCRRKGITIRSTIDCLIAQTAIENNLYLLHNDRDFDNIAKVIPLLKCY
>gnl|CDD|350330 cd18763, PIN_MtVapC3-like, uncharacterized subgroup of the VapC3-like nuclease subfamily of the PIN domain superfamily. The VapC3-like nuclease subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of various Mycobacterium tuberculosis VapC toxins including VapC3, VapC11, VapC15, VapC21, VapC25, VapC28, VapC29, VapC30, VapC32, VapC33, VapC37, and VapC39. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LVDTSVWIDFFRGRDTPQVALLEELIEQREDLCICGVILTEVLQGIRDDKEYAKTKELLESLLFLPMTQS
TFIRAADIYRTLRKKGITIRKPVDCMIAAVALEHDVSLLHNDRDFDPIARHYPLKVVN
>gnl|CDD|350331 cd18764, PIN_MtVapC3-like, uncharacterized subgroup of the VapC3-like nuclease subfamily of the PIN domain superfamily. The VapC3-like nuclease subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of various Mycobacterium tuberculosis VapC toxins including VapC3, VapC11, VapC15, VapC21, VapC25, VapC28, VapC29, VapC30, VapC32, VapC33, VapC37, and VapC39. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LFDTSVWIDFFNGKETPQTDLLQELLLEDQPVYICPTIVQEILQGIRDDNEFKKIKDLLSALPILELDPY
EAAIGAADLYRSLRKKGVTIRKSNDCLIAHYAIKFDLPLVHNDRDFDLIAKYSKLKVYK
>gnl|CDD|350332 cd18765, PIN_MtVapC3-like, uncharacterized subgroup of the VapC3-like nuclease subfamily of the PIN domain superfamily. The VapC3-like nuclease subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of various Mycobacterium tuberculosis VapC toxins including VapC3, VapC11, VapC15, VapC21, VapC25, VapC28, VapC29, VapC30, VapC32, VapC33, VapC37, and VapC39. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LVDTSVWIDLLRGTGTPAVRRLRRLLQSEEPVALAPVILQELLQGARSPEHFVRLQAHFDALPMLKPKDA
RATHRAAAALYARCRWAGITPRSPNDCLIAQCAIEHGVPLLHDDRDFETIARVEPKLKLLP
>gnl|CDD|350333 cd18766, PIN_MtVapC3-like, uncharacterized subgroup of the VapC3-like nuclease subfamily of the PIN domain superfamily. The VapC3-like nuclease subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of various Mycobacterium tuberculosis VapC toxins including VapC3, VapC11, VapC15, VapC21, VapC25, VapC28, VapC29, VapC30, VapC32, VapC33, VapC37, and VapC39. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LVDTSVWSLALRRPKHAVNREATLLKQIIEKGEPIALTGIILQELLQGIRNDKLFDQLKEHLEAFPLILP
TREDHIEAARLRNDCRRKGVQVSAIDALIAQMCISHDLTLFTTDKDFKHIATHSSLKLFS
>gnl|CDD|350334 cd18767, PIN_MtVapC3-like, uncharacterized subgroup of the VapC3-like nuclease subfamily of the PIN domain superfamily. The VapC3-like nuclease subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of various Mycobacterium tuberculosis VapC toxins including VapC3, VapC11, VapC15, VapC21, VapC25, VapC28, VapC29, VapC30, VapC32, VapC33, VapC37, and VapC39. It belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is a PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LVDTSVWINLFRRPSRFRLADLNLPDEVVTCLPVVQEVLQGIRDDHAFRRIREAMLALPIVESPLSLDVF
LSAAQLYRLARRKGLTVRSSVDCLIAAIAIRHDLTVLHHDRDFDALARISPLKIQK
>gnl|CDD|350335 cd18768, PIN_MtVapC4-C5-like, VapC-like PIN domain of Mycobacterium tuberculosis VapC4, VapC5, and related proteins. This subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 toxin of the VapBC toxin/antitoxin (TA) system. This family belongs to the PIN_VapC4-5_FitB-like subfamily of the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. M. tuberculosis VapC4 interacts with, and cleaves tRNA44Cys-GCA. M. tuberculosis VapC5 has endonucleolytic activity with RNA, this activity is low with dsRNA, and no activity has been demonstrated on dsDNA. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons
LADTSVFIAQESGRALDGDLLPDEIAVSVVTLAELRAGVLAARDLATRARRLATLQLAADLEPLPIDDAV
AAAWARLRLELRESGRRMRVNDSWIAATALAHDLPVVTQDADFDALPDLEVIR
>gnl|CDD|350851 cd18769, PIN_Mut7-C-like, uncharacterized subgroup of the Mut7-C-like family of the PIN domain superfamily. The Mut7-C-like family of the PIN domain superfamily includes the C-terminal domain of Caenorhabditis elegans Mut-7 (also known as exonuclease 3'-5' domain-containing protein 3 homolog). Mut-7 is involved in RNA interference (RNAi) and transposon silencing in C. elegans. The Mut7-C PIN domain family is recognized as a genuine PIN domain, however it not included it in the CDD PIN domain superfamily hierarchical model as it is lacks a core strand and helix (H3 and S3). The PIN (PilT N terminus) domain belongs to a large nuclease superfamily, and were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Other PIN domain families are: the FEN-like PIN domain family which includes the PIN domains of Flap endonuclease-1 (FEN1), Exonuclease-1 (EXO1), Mkt1, Gap endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease, 5'-3' exonucleases of DNA polymerase I and bacteriophage T4- and T5-5' nucleases; the VapC-like PIN domain family which includes toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and, rRNA-processing protein Fcf1; the LabA-like PIN domain family which includes the PIN domains of Synechococcus elongatus LabA (low-amplitude and bright); the PRORP-Zc3h12a-like PIN domain family which includes the PIN domains of of RNase P (PRORP), ribonuclease Zc3h12a; and Bacillus subtilis YacP/Rae1-like PIN domains. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_10
IYIDENMPPHLAHGFNTLQSPEGLKTGELIEVKSLPDAFGYGAKDEDWIPKVGKENACVITQDINISRRK
HELELYQKNGVGMFF
>gnl|CDD|350852 cd18770, PIN_Mut7-C-like, uncharacterized subgroup of the Mut7-C-like family of the PIN domain superfamily. The Mut7-C-like family of the PIN domain superfamily includes the C-terminal domain of Caenorhabditis elegans Mut-7 (also known as exonuclease 3'-5' domain-containing protein 3 homolog) Mut-7 is involved in RNA interference (RNAi) and transposon silencing in C. elegans. The Mut7-C PIN domain family is recognized as a genuine PIN domain, however it is not included it in the CDD PIN domain superfamily hierarchical model as it is lacks a core strand and helix (H3 and S3). The PIN (PilT N terminus) domain belongs to a large nuclease superfamily, and were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Other PIN domain families are: the FEN-like PIN domain family which includes the PIN domains of Flap endonuclease-1 (FEN1), Exonuclease-1 (EXO1), Mkt1, Gap endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease, 5'-3' exonucleases of DNA polymerase I and bacteriophage T4- and T5-5' nucleases; the VapC-like PIN domain family which includes toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and, rRNA-processing protein Fcf1; the LabA-like PIN domain family which includes the PIN domains of Synechococcus elongatus LabA (low-amplitude and bright); the PRORP-Zc3h12a-like PIN domain family which includes the PIN domains of of RNase P (PRORP), ribonuclease Zc3h12a; and Bacillus subtilis YacP/Rae1-like PIN domains. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_16
LLLDENVPRPMARIVRILLKDHQVRHVAELGGWAGTKDIELYAKATAAGFTIVLTNDTKQLSRNLEVAAI
AESGLHRIEY
>gnl|CDD|350853 cd18771, PIN_Mut7-C-like, uncharacterized subgroup of the Mut7-C-like family of the PIN domain superfamily. The Mut7-C-like family of the PIN domain superfamily includes the C-terminal domain of Caenorhabditis elegans Mut-7 (also known as exonuclease 3'-5' domain-containing protein 3 homolog). Mut-7 is involved in RNA interference (RNAi) and transposon silencing in C. elegans. The Mut7-C PIN domain family is recognized as a genuine PIN domain, however it is not included it in the CDD PIN domain superfamily hierarchical model as it is lacks a core strand and helix (H3 and S3). The PIN (PilT N terminus) domain belongs to a large nuclease superfamily, and were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Other PIN domain families are: the FEN-like PIN domain family which includes the PIN domains of Flap endonuclease-1 (FEN1), Exonuclease-1 (EXO1), Mkt1, Gap endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease, 5'-3' exonucleases of DNA polymerase I and bacteriophage T4- and T5-5' nucleases; the VapC-like PIN domain family which includes toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and, rRNA-processing protein Fcf1; the LabA-like PIN domain family which includes the PIN domains of Synechococcus elongatus LabA (low-amplitude and bright); the PRORP-Zc3h12a-like PIN domain family which includes the PIN domains of of RNase P (PRORP), ribonuclease Zc3h12a; and Bacillus subtilis YacP/Rae1-like PIN domains
FLLDVHLGTLARLLRLLGFDTAYDNTYADATLAALADAEDRILLSRDRGLLKRRGIRRGAFV
>gnl|CDD|350854 cd18772, PIN_Mut7-C-like, Mut7-C-like family of the PIN domain superfamily similar to the PIN domain found at the C-terminus of Caenorhabditis elegans exonuclease Mut-7 and related proteins. This Mut7-C-like subgroup of the PIN domain superfamily includes the C-terminal domain of Caenorhabditis elegans Mut-7 (also known as exonuclease 3'-5' domain-containing protein 3 homolog). Mut-7 is involved in RNA interference (RNAi) and transposon silencing in C. elegans. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily, and were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Other PIN domain families are: the FEN-like PIN domain family which includes the PIN domains of Flap endonuclease-1 (FEN1), Exonuclease-1 (EXO1), Mkt1, Gap endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease, 5'-3' exonucleases of DNA polymerase I and bacteriophage T4- and T5-5' nucleases; the VapC-like PIN domain family which includes toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and, rRNA-processing protein Fcf1; the LabA-like PIN domain family which includes the PIN domains of Synechococcus elongatus LabA (low-amplitude and bright); the PRORP-Zc3h12a-like PIN domain family which includes the PIN domains of of RNase P (PRORP), ribonuclease Zc3h12a; and Bacillus subtilis YacP/Rae1-like PIN domains
FIVDEHLPPAFVKALRGEGYDVIEINDTVDDRILEYAIEQRAISIRDERILITKDRVVLSEDLTIFRPAD
STLITTLDLEN
>gnl|CDD|350341 cd18773, PDC1_HK_sensor, first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains. Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution
LEEADLLLRSLASALEALAALGSADREELQALLRRLLERNPEISGIYVVDADGRVVASSDRDPGGGDDDD
DRDRFWYQAAKATGKLVISEPYISRVTGKPVITLSRPIRDADGRFIGVVGADIDL
>gnl|CDD|350342 cd18774, PDC2_HK_sensor, second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains. Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution
YLSDLLSSIKLGETGYAFLVDSDGTILAHPPKELVGKGKSLDDLALLAALLLAGESGTFEYTSDDGVERL
VAYRPVPGTPWVVVVGVPE
>gnl|CDD|350651 cd18775, SafA-like, Saf-pilin pilus formation protein SafA. This subfamily is composed of Saf-pilin pilus formation protein SafA from Salmonella enterica and similar proteins. SafA is the major subunit of Saf pili, which are often found in clinical isolates of Salmonella and are assembled by the chaperone-usher secretion pathway. In addition to safA, the saf operon is also composed of safB (periplasmic chaperone), safC (outer membrane usher), and safD (minor subunit). SafA and SafD subunits are transported from the cytoplasm into the periplasm via the SEC machinery, and the periplasmic chaperone SafB donates its G1 strand to complete the correct folding of SafA or SafD. In Saf pili assembly, the N-terminal extension (NTE) of an incoming SafA replaces the G1 strand (in SafB) via a zip-in-zip-out mechanism (also called donor-strand complementation or exchange) to form the polymer of SafD-(SafA)n (n _ 100)
LTVSLTPVSGLVAGKHADNTVIAKGTVTSTDAKRFAVRGTAGTGEDSNGSAWTITGKNDGNKLKVKLSPD
STSGSTVKWNGGTWFVFNINAPTDTYDIKLDGDQNVPADTYPITLDAAAYQA
>gnl|CDD|350652 cd18776, AfaD-like, AfaD and similar proteins. This subfamily consists of Escherichia coli AfaD, Salmonella SafD, and similar proteins. The afa gene clusters encode an afimbrial adhesive sheath produced by Escherichia coli. The adhesive sheath is composed of two proteins, AfaD and AfaE, which are independently exposed at the bacterial cell surface. AfaE is required for bacterial adhesion to HeLa cells and AfaD for the uptake of adherent bacteria into these cells. SafD is the minor subunit of Saf pili, which are often found in clinical isolates of Salmonella and are assembled by the chaperone-usher secretion pathway. In addition to safD, the saf operon is also composed of safA (major subunit), safB (periplasmic chaperone), and safC (outer membrane usher). Also included is the enteroaggregative Escherichia coli AAF/IV pilus tip protein, which is implicated in adhesion as well. During fimbria/pili assembly, polymerization occurs when the N-terminal extension (NTE) of one monomer is inserted into an adjacent monomer, providing the final beta strand or G-strand, to complete the Ig-like fold, in a mechanism called the donor-strand complementation (DSC) or donor-strand exchange (DSE)
LELSLQPKTGLGAGLVRDGTLIATGRISCRGAHSGFRVWSNAEKVGGRPGRYILTGKNNPRNKLRVRLEG
EGWQPDTQGGKGIILTTSEESATFDIVADGNQNVPPDTYTISLSAACL
>gnl|CDD|350653 cd18777, PsaA_MyfA, Fimbrial subunit PsaA, MyfA, and similar proteins. This subfamily is composed of Yersinia pestis PsaA, Yersinia enterocolitica MyfA, and similar proteins. PsaA and MyfA are the major subunits of pH 6 antigen (Psa) and Myf fimbrial homopolymers. Psa and Myf specifically recognize beta1-3- or beta1-4-linked galactose in glycosphingolipids, but while Psa also binds phosphatidylcholine, Myf does not. Psa has acquired a tyrosine-rich surface that enables it to bind to phosphatidylcholine and mediate adhesion of Y. pestis/pseudotuberculosis to alveolar cells. Myf has specialized as a carbohydrate-binding adhesin, facilitating the attachment of Y. enterocolitica to intestinal cells. During fimbria/pili assembly, polymerization occurs when the N-terminal extension (NTE) of one monomer is inserted into an adjacent monomer, providing the final beta strand or G-strand, to complete the Ig-like fold, in a mechanism called the donor-strand complementation (DSC) or donor-strand exchange (DSE)
FKVEFKASPNEIFSGKQAADTTVFTLKMSDTAEHGGWRVIPTGSSKGGYMVDADGDKVGLHSNNMTWDGG
DDHWYINDSSSEDLEEHLYVAKGTVVKAGEYHFTGRVEEY
>gnl|CDD|350051 cd18778, ABC_6TM_exporter_like, Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins. This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis
LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQK
VVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINP
KLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSR
RYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLN
EMLQRALAGAERV
>gnl|CDD|350052 cd18779, ABC_6TM_T1SS_like, uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins. uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides
PGLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLR
TRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQS
PLLGLVVLGLAALQVALLLATRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLF
VDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGT
AQQLQLLGSHLERL
>gnl|CDD|350053 cd18780, ABC_6TM_AtABCB27_like, Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins. This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family
GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAG
ERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTT
SWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEK
INESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSS
LYGDFMQAVGASVRV
>gnl|CDD|350054 cd18781, ABC_6TM_AarD_CydDC_like, uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins. This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family
TVLLQWISLLANIAFVFSIANLLQKLLEGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKK
TLREKIYDKLLRLGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAA
LVLLICVPLIPISIIAVQKIAKKLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFR
KITMKVLTMQLNSITVMDLVAYGGAALGIILALLQFANGSISLAGALFIILLSAEFFLPLRLLGSFFHIA
MNGMAASDKI
>gnl|CDD|350055 cd18782, ABC_6TM_PrtD_LapB_HlyB_like, uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins. Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion
RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTA
NRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYS
PLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRY
ARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTL
WQQFQELRVSLERL
>gnl|CDD|350056 cd18783, ABC_6TM_PrtD_LapB_HlyB_like, uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins. Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion
KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVAT
TRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYS
PTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERV
ARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGL
VQEYQEARLSVRML
>gnl|CDD|350057 cd18784, ABC_6TM_ABCB9_like, Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins. ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit
AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIR
IRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSL
VTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYK
LKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLM
QAVGAAEKV
>gnl|CDD|350172 cd18785, SF2_C, C-terminal helicase domain of superfamily 2 DEAD/H-box helicases. Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
VMVVKIIVFTNSIEHAEEIASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE
GEVILFV
>gnl|CDD|350173 cd18786, SF1_C, C-terminal helicase domain of superfamily 1 DEAD/H-box helicases. Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
PAIVNAANGLYKGVVLTPYHRDRAYLNQYLQGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTANSLT
PRRLYVALTRARKRLVIYD
>gnl|CDD|350174 cd18787, SF2_C_DEAD, C-terminal helicase domain of the DEAD box helicases. DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERAL
KKFRSGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV
>gnl|CDD|350175 cd18788, SF2_C_XPD, C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases. The xeroderma pigmentosum group D (XPD)-like family members are DEAD-box helicases belonging to superfamily (SF)2. This family includes DDX11 (also called ChlR1), a protein involved in maintaining chromosome transmission fidelity and genome stability, the TFIIH basal transcription factor complex XPD subunit, and FANCJ (also known as BRIP1), a DNA helicase required for the maintenance of chromosomal stability. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
DQVCPGIVGRGPDQQALNSKFQTREDEAVMDELGNLLLELCAVVPDGVLVFFPSYSYMERVVSRGALLLA
VCRGKVSEGIDFSDDLGRAVIMVGIPYPNTKDPILKLKMDDLEYLRDKGLLTGEDWYTFQAMRAVNQAIG
RAIRHKNDYGAIVLLDKRF
>gnl|CDD|350176 cd18789, SF2_C_XPB, C-terminal helicase domain of XPB-like helicases. TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
CAEIRCPMTPEFYREYLGLGAHRKRRLLAAMNPNKLRALEELLKRHEQGDKIIVFTDNVEALYRYAKRLL
KPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQISGHGGSRRQEAQRLGRILRPK
KGGGKNAFFYSLV
>gnl|CDD|350177 cd18790, SF2_C_UvrB, C-terminal helicase domain of the UvrB family helicases. Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
DPEIEVRPTEGQVDDLLGEIRKRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEII
RDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSETSLIQTIGRAARNVNGKVILYADKITD
SMQKAIEETERRREIQMEYNEEHGITPKTII
>gnl|CDD|350178 cd18791, SF2_C_RHA, C-terminal helicase domain of the RNA helicase A (RHA) family helicases. The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
FPVEVYYLEDILELLGISSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSP
DLGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLS
SLVTVWISKASAEQRAGRAGRTRPGKCYRLY
>gnl|CDD|350179 cd18792, SF2_C_RecG_TRCF, C-terminal helicase domain of the RecG family helicases. The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
PIRTYVIPHDDLDLVYEAIERELARGGQVYYVYPRIEESEKLDLKSIEALAEELKELVPEARVALLHGKM
TEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLL
YPDPKKLTETAKKRLRAIAE
>gnl|CDD|350180 cd18793, SF2_C_SNF, C-terminal helicase domain of the SNF family helicases. The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
LPPKIEEVVSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLV
DRFNEDPDIRVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI
>gnl|CDD|350181 cd18794, SF2_C_RecQ, C-terminal helicase domain of the RecQ family helicases. The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRR
DVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY
>gnl|CDD|350182 cd18795, SF2_C_Ski2, C-terminal helicase domain of the Ski2 family helicases. Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
RPVPLEEYVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLAGIAFHH
AGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELSPLEYLQMIGRAGR
PGFDTRGEAIIMTK
>gnl|CDD|350183 cd18796, SF2_C_LHR, C-terminal helicase domain of LHR family helicases. Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
KKKLDIKVILPVAPEIFPWAGESGADAYAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRVPPDF
IALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG
AASKGRLVPT
>gnl|CDD|350184 cd18797, SF2_C_Hrq, C-terminal helicase domain of HrQ family helicases. Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
HFVLWNPPLLDRKDGERGSARREAARLFADLVRAGVKTIVFCRSRKLAELLLRYLKARLVEEGPLASKVA
SYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDS
LVILVA
>gnl|CDD|350185 cd18798, SF2_C_reverse_gyrase, C-terminal helicase domain of the reverse gyrase. Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
NIVDVYIEDSDSLEKLLELVKKLGDGGLIFVSIDYGKEYAEELKEFLERHGIKAELALSSTEKNLEKFEE
GEIDVLIGVASYYGVLVRGIDLPERIKYAIFYGVPVTTYIQASGRTSRLYAGGLTKGLSVVLVDDPELFE
ALKKRLKLILDEFIFKELEEVDLEELLSEIDESR
>gnl|CDD|350186 cd18799, SF2_C_EcoAI-like, C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases. This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
PYKYVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEALILLFFGELKPPILVTVDLLT
TGVDIPEVDNVVFLRPTESRTLFLQMLGRGLRLHEGKDFFTILDFI
>gnl|CDD|350187 cd18800, SF2_C_EcoR124I-like, C-terminal helicase domain of EcoR124I HsdR-like restriction enzyme family helicases. This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoR124I R protein. EcoR124I recognizes the sequence, 5'-GAAN(6)RTCG-3', and cleaves at random sites. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
PFNVEYRKAMVVTSSRRAAVRYYKALDLLIVVDMLLTGFDAPSLNTLYVDKPLKYHGLIQAIARVNRVYK
DEKEFGLIVDYR
>gnl|CDD|350188 cd18801, SF2_C_FANCM_Hef, C-terminal helicase domain of Fanconi anemia group M family helicases. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
KRKVEKIHPKLEKLEEIVKEHFKKKQEGSDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATRFIGQASGKS
SKGMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQGRVV
VLL
>gnl|CDD|350189 cd18802, SF2_C_dicer, C-terminal helicase domain of the endoribonuclease Dicer. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
EEIVVIPKLQKLIEILREYFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGFLIGRGNSSQRK
RSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSKYIL
MV
>gnl|CDD|350190 cd18803, SF2_C_secA, C-terminal helicase domain of the protein translocase subunit secA. SecA is a component of the Sec translocase that transports the vast majority of bacterial and ER-exported proteins. SecA binds both the signal sequence and the mature domain of the preprotein emerging from the ribosome. SecA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
RKDLPDLVYKTEEEKWKAIVEEVKELHAKGQPVLVGTRSVEKSELLSALLKEEGIPHNVLNAKNHAREAE
IIAEAGQKGAVTIATNMAGRGTDIKLGGNVEELGGLHVIGTERHESRRIDNQLRGRAGRQGDPGSSRFYL
S
>gnl|CDD|350191 cd18804, SF2_C_priA, C-terminal helicase domain of ATP-dependent helicase PriA. PriA, also known as replication factor Y or primosomal protein N', is a 3'--_5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
IEIVDMKEEELKSGFSPKLLDAIKETLEKGEQVILFLNRRGYSPSVLCRDCGYVPECPNCDVSMTYHKST
NKLKCHYCGYQEPIPKQCPECGSEDLVFKGIGTERVEEELKTLFPEARIARIDRDTTRKKGALEKLLDQF
ERGEIDILIGTQMIAKGLDFPNVTLVGILNADSGLNSPDFRASERAFQLLTQVSGRAGRGDKPGKVIIQT
YNPEHPLIQAAKEEDYEAFYEEELAERK
>gnl|CDD|350192 cd18805, SF2_C_suv3, C-terminal helicase domain of ATP-dependent RNA helicase. The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
TPLSVESKPLGSLRNLRPGDCVVAFSRKDIFSLKREIEKRTGLKCAVIYGALPPETRRQQARLFNDPESG
YDVLVASDAIGMGLNLNIRRVIFSSLSKFDGNEMRPLSPSEVKQIAGRAGRFGSHFPEGEVTTLR
>gnl|CDD|350193 cd18806, SF2_C_viral, C-terminal helicase domain of viral helicase. Viral helicases in this family here are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
IEDVALEIPGRIWFYGKAWITIYGGKTVWFVHSKKKGNEIAACLSGLGKNVIQLYRKLDDTEYPKIKTID
WDFVVTTDISEMGANFDADRVIDCRTCVKPTILFSGDFRVILTGPVPQTAASAAQRRGRTGRNPAQERDI
YRFVG
>gnl|CDD|350194 cd18807, SF1_C_UvrD, C-terminal helicase domain of UvrD family helicases. UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
STKNILDAANSLIKQNKNRPKKPLKAGNKSGGPVELLLAKDEADEAKAIADEIKRLIESGPVQYSDIAIL
VRTNRQARVIEEALRVTLMTIHASKGLEFPVVFIVGLGEGFIPSDASYHAAKEDEERLEEERRLLYVALT
RAKKELYLVG
>gnl|CDD|350195 cd18808, SF1_C_Upf1, C-terminal helicase domain of Upf1-like family helicases. The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
MHPEISEFPSKLFYEGKLKAGVSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVEL
VKYLLKSGVKPSSIGVITPYRAQVALIRELLRKRGGLLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS
IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE
>gnl|CDD|350196 cd18809, SF1_C_RecD, C-terminal helicase domain of RecD family helicases. RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
SGIAELAEAIRDIQVLAPTRKGGVDALNERLQAYAMTIHKSQGSEFDRVIVVLPTSHPMLSRGLLYTALT
RARKLLTLVG
>gnl|CDD|350197 cd18810, SF2_C_TRCF, C-terminal helicase domain of the transcription-repair coupling factor. Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
PVRTYVMPYDDELIREAIERELLRGGQVFYVHNRIESIEKLATQLRQLVPEARIAIAHGQMTENELEEVM
LEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKERAYAYFLYPDQKKLTE
DALKRLEAIQE
>gnl|CDD|350198 cd18811, SF2_C_RecG, C-terminal helicase domain of DNA helicase RecG. ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC
PITTYLIFHTRLDKVYEFVREEIAKGRQAYVIYPLIEESEKLDLKAAVAMYEYLKERFRPELNVGLLHGR
LKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLL
VYKDPLTETAKQRLRVMTE
>gnl|CDD|349406 cd18812, CAP_PI15-like, CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor 15 and similar proteins. This family is composed of peptidase inhibitor 15 (PI15), peptidase inhibitor R3HDML, cysteine-rich secretory protein LCCL domain-containing 1 (CRISPLD1), and cysteine-rich secretory protein LCCL domain-containing 2 (CRISPLD2). PI15 is a serine protease inhibitor which displays weak inhibitory activity against trypsin and may play a role in facial patterning during embryonic development. The PI15 gene is a candidate gene for abdominal aortic internal elastic lamina ruptures in the rat. R3HDML is a putative serine protease inhibitor, whose gene may be associated with clinical dimensions of schizophrenia. CRISPLD1 may play a role in NSCLP (nonsyndromic cleft lip with or without cleft palate) through the interaction with CRISPLD2 and folate pathway genes. plays a role in the etiology of NSCLP and is required for neural crest cell migration and cell viability during craniofacial development. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others
MNAILDYHNKLRGQVYPPAANMEYMVWDKELARSAEAWATQCIWEHGPSSLLRSIGQNLSAHWGRYRSPV
FLVKSWYDEVKDYLFPYPRDCNPHCPWRCSGPMCTHYTQMVWATSNRIGCAIHTCSNMNVWGNVWHRAVY
LVCNYA
>gnl|CDD|349407 cd18813, CAP_CRISPLD1, CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory protein LCCL domain-containing 1. Cysteine-rich secretory protein LCCL domain-containing 1 (CRISPLD1) is also called cysteine-rich secretory protein 10 (CRISP-10), CocoaCrisp, LCCL domain-containing cysteine-rich secretory protein 1 (LCRISP1), or CAP and LCCL domain containing protein 1 (CAPLD1). CRISPLD1 is clearly distinct from CRISPs because they do not contain the 10 absolutely conserved cysteines or the ICR (ion channel regulator) domain of the CRISPs. It may play a role in NSCLP (nonsyndromic cleft lip with or without cleft palate) through the interaction with CRISPLD2 and folate pathway genes. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others
MQLILDLHNKLRGQVYPPASNMEYMTWDVELERSAEAWAETCLWEHGPAHLLPSIGQNLGAHWGRYRPPT
FHVQAWYDEVRDFSYPYPQECNPYCPFRCSGPVCTHYTQVVWATSNRIGCAINLCHNMNVWGQIWPKAIY
LVCNYS
>gnl|CDD|349408 cd18814, CAP_PI15, CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor 15. Peptidase inhibitor 15 (PI15) is also called 25 kDa trypsin inhibitor (p25TI), cysteine-rich secretory protein 8 (CRISP-8), or SugarCrisp. It is a serine protease inhibitor which displays weak inhibitory activity against trypsin and may play a role in facial patterning during embryonic development. The PI15 gene is a candidate gene for abdominal aortic internal elastic lamina ruptures in the rat. PI15 may also participate in the regulation of drug resistance in ovarian cancer and serve as a potential target in targeted therapies. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others
MIAILDYHNQVRGKVFPPAANMEYMVWDENLAKSAEAWAATCIWDHGPSYLLRFLGQNLSVRTGRYRSIL
QLVKPWYDEVKDYAFPYPQDCNPRCPLRCYGPMCTHYTQMVWATSNRIGCAIHTCHNMNVWGSVWRRAVY
LVCNYS
>gnl|CDD|349409 cd18815, CAP_R3HDML, CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor R3HDML. Peptidase inhibitor R3HDML, also called cysteine-rich secretory protein R3HDML, is a putative serine protease inhibitor. The R3HDML gene may be associated with clinical dimensions of schizophrenia. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others
MNALLDYHNRVRSQVFPPAANMEYMVWDERLAKSAEAWAAQCVWEHGPPQLMRYIGQNLSIHSGRYRSIV
DLVKSWYDERQHYSFPHPRECNPRCPSKCSGAVCSHYTQMVWASSNRIGCAVHTCSNINVWGSTWRRATY
LVCNYA
>gnl|CDD|349410 cd18816, CAP_CRISPLD2, CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory protein LCCL domain-containing 2. Cysteine-rich secretory protein LCCL domain-containing 2 (CRISPLD2) is also called cysteine-rich secretory protein 11 (CRSIP-11), LCCL domain-containing cysteine-rich secretory protein 2 (LCRISP2), or CAP and LCCL domain containing protein 2 (CAPLD2). It plays a role in the etiology of NSCLP (non-syndromic cleft lip with or without cleft palate). It is required for neural crest cell migration and cell viability during craniofacial development. The CRISPLD2 gene has been identified a glucocorticoid responsive gene that modulates cytokine function in airway smooth muscle cells. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others
KEEILQLHNKLRGQVYPSASNMEYMTWDDELERSAEAWAQQCIWEHGPTSLLPSIGQNLAVHWGRYRSPA
FHVQSWYDEVKDYTYPYPHECNPWCPERCSGPMCTHYTQIVWATTNKVGCAVNVCRRMNVWGEIWENAVY
LVCNYS
>gnl|CDD|350138 cd18817, GH43f_LbAraf43-like, Glycosyl hydrolase family 43 such as Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with alpha-L-arabinofuranosidase (EC 3.2.1.55) activity. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. Characterized enzymes belonging to this subgroup include Lactobacillus brevis (LbAraf43) and Weissella sp (WAraf43) which show activity with similar catalytic efficiency on 1,5-alpha-L-arabinooligosaccharides with a degree of polymerization (DP) of 2-3; size is limited by an extended loop at the entrance to the active site. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
ADPHIYKHTDGYYYFTASVPEYDRIELRRAKTIQGLADAPEVVIWRKHDSGPMSAHIWAPEIHFIDGKWY
IYFAAGPTENDVWQIRMYVLECDAADPLTGTWTEKGQIKTAWDSFSLDATTFEHNGKRYYVWAQKDPEIE
GNSNLYIAEMENPWTLKGKPVMLSKPEYDWETRGFWVNEGPAVLKRNGKIFLTYSASATDANYCMGMLTA
DENADLLDPASWTKSPEPVFQTSEENGQYGPGHNSFTVSEDGRTDVLVYHAR
>gnl|CDD|350139 cd18818, GH43_GbtXyl43B-like, Glycosyl hydrolase family 43 such as Geobacillus thermoleovorans IT-08 beta-xylosidase/exo-xylanase (GbtXyl43B). This glycosyl hydrolase family 43 (GH43) subgroup includes the characterized enzymes Geobacillus thermoleovorans IT-08 beta-xylosidase (EC 3.2.1.37) / exo-xylanase (GbtXyl43B), and Paenibacillus sp. strain E18 alpha-L-arabinofuranosidase (EC 3.2.1.55) Abf43B. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
ADPCILRWNGKYYFIATDDNDGQHGLYIREADTIEGLADAPEHLILNVDLSGDISGCLWAPEFHVIGGDL
YIFFAASGNDWWGVQSHVMKLKGGGDPTNPADWETPIRVVKKDGSDLAEKGITLDMTYFEDGGRSYVVWS
QRKIIGTSGDGGADLYIATVDPSKPWRLTSDPVLLSRPDYGWERNHTFVAEGPYALRRGDKVYLTYSGSA
VDYTYAVGLLTADAGADLLDPASWTKSNYPLLTSESVPGEYGPGHNSFVTDEDGNLLNVYHAK
>gnl|CDD|350140 cd18819, GH43_LbAraf43-like, Glycosyl hydrolase family 43 proteins similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans GbtXyl43B. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes enzymes with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities, similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans IT-08 beta-xylosidase / exo-xylanase (GbtXyl43B). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
ADPYIVYDEDDGYYYFTASYPAYGNDDDEGYDRIVLRRAKTIEGLADAEEVTIWKESESGGLHRYIWAPE
IHKIGGKWYVLFTASRSGNVWDIRPYVLVCDGDDDPMDPDSWTEEGRYVESQVGDTDAFSTFSLDMTYFE
ANGTHYVIWAEKPGISKLYIATIDPDDPWKLTSKPVILSTPDYAWERNRGQKINEGPAVLKHDGKIFLAF
SASTVDSEYCVGMLTADEDADLMDPDSWTKNPYPLLSTADVDGQCGPGHNSFTVDENGNPVIVYHAR
>gnl|CDD|350141 cd18820, GH43_LbAraf43-like, Glycosyl hydrolase family 43 proteins similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans GbtXyl43B. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes enzymes with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities, similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans IT-08 beta-xylosidase / exo-xylanase (GbtXyl43B). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
ADPWVVYHDGYYYLTFTTGDRITIWKSKTLTGLGTAEPKVVWTPPDPSRSCNIWAPELHFIDGRWYIYYA
ADDGDNANHRMYVLESASDDPPLGPYTFKGRLADPTDKWAIDGTVLEHNGKLYFVWSGWEGDTNGPQNLY
IAPMSNPWTLSGERVLISTPTYDWERQGPPGVNEGPQVLYHGGRTFLVYSASGSWTPDYCLGLLTLTGGD
DPLDPASWTKSPGPVFQSNDANGVYGPGHNSFFKSPDGTEDWIVYHAK
>gnl|CDD|350142 cd18821, GH43_Pc3Gal43A-like, Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1,3-galactanase (Pc1, 3Gal43A, 1,3Gal43A). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), Fusarium oxysporum 12S Fo/1 (3Gal), and Streptomyces sp. 19(2012) SGalase1 and SGalase2. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
IQAHGGGILKVGDTYYWFGEDKTDGSNLFQGVSCYSSTDLVNWTFEGLALPPQESGDLGPNRVVERPKVI
YNPSTGKYVMWMHIDSSNYGDARVGVATSDTVTGPYTYVGSFRPLGYESRDIGVFQDDDGTAYLLFEDRD
NGLRIYRLSDDYLSVVELVYTFIAAGLEAPAMFKVDGTYYLLGSHLTGWRPNDNVYFTATSLSGPWSEPG
LIAPEGTNTYNSQSTFVLPVGGSKKTTYIYMGDRWDSPDLSASTYVWLPLTI
>gnl|CDD|350143 cd18822, GH43_CtGH43-like, Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43), Streptomyces avermitilis MA-4680 = NBRC 14893 (Sa1,3Gal43A;SAV2109) (1,3Gal43A), and Ruminiclostridium thermocellum ATCC 27405 (Ct1,3Gal43A;CtGH43;Cthe_0661) (1,3Gal43A). It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
IQAHGGGILKVGGTYYWYGENRDNNNGFNGVSLYSSTDLVNWEFRNTVLTRDTCSASELASCKIERPKVI
YNPKTGKFVMWAHWENGKDYGLARAAVATSDTPDGDYTFHGSFRPLGYDSRDMTLFVDDDGTAYLISAAN
DNADLNIYRLTPDYLSVDSLVATLFKGQHREAPALVKRNGYYYLFTSGASGWYPNQGQYASATSLAGPWS
SLRNIGNNTTFGSQSTFILPVGGSGGTSYLYMGDRWNSPWGGDLGDSRYVWLPLSF
>gnl|CDD|350144 cd18823, GH43_RcAra43A-like, Glycosyl hydrolase family 43 such as Ruminococcus champanellensis arabinanase Ara43A. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis arabinanase Ara43A and Fibrobacter succinogenes subsp. succinogenes S85 Fisuc_1994 / FSU_2517. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
IYSQGGGVFKVGDTYYWYGVKYSGAVTYAANTKKNSDTSFKSVTLYSSTDLVNWTFEGNVLTASGAVDTA
GDFAGAGWVGRPGVAYNSATGKYVLLIQWGSTGNGRNGVLFATSDSPTGPFTYQRVQPMIDNVGTNNTGD
QTSFFDDDGKAYLVYSNDRGRGSLYIAKLRSDYLGIEPAVRIDNYVGPGREGNALFKYGGTYYLCASDLH
GWNASQTYYMVATSLTGPYSPSNVLETTGPESDNSHVTQTGFFIPVHGSKGTTYVYCGDRWSDFAGNGIG
YNQWYPLTF
>gnl|CDD|350145 cd18824, GH43_CtGH43-like, Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
IDAHDGKIYFFGGAYYWYGTPYGCGCGSCGFTLFCGFVVYSSVDLVNWTYRGVLFDPNTCAGSPGVCFRP
HVVYNARTGRYVLWYNAYDGSSGYAVATSSTPTGPFVTVPDPVLAPAGLQAGDFSLFVDDDGTGYLAYTT
IDFPQSIVVEQLTDDYLNTTGEYVRDLIDQEAEAPSIFKRNGIYYILASNTCCGCCQGTGARVYRATSPL
GPWTRQIDINSCAGALFPPSDSAYTCGGQPTAVLPLPSPGGETLYLYMGDRWRTAPDGRKGHDGHYWQPL
SF
>gnl|CDD|350146 cd18825, GH43_CtGH43-like, Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
IQAHGGGILKHNGTYYWYGEDKTGGTYRRVDVIGVSCYSSKDLYNWKDEGIVLDAVDDAPASDLYPNNVV
ERPKVIYNKKTKKYVMWFHLDGPGADYSRARAGVAVSDSPTGPFKYLGSFRPNAGEKNRDFSNGQMSRDM
TLFVDDDGKAYLIYSSEENKTLYIAKLTDDYTGVTGDYARILIGQSREAPAVFKHDGKYYMITSGCTGWA
PNAARYAVADSIFGPWKEIGNPCRGPNDDADTTFGSQSTFVLPVDGENGKFIYMGDRWNPKDLADSRYVW
LPITF
>gnl|CDD|350147 cd18826, GH43_CtGH43-like, Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
IQAHGGSVIYVDGVYYWYGENKEHTDGESGIWHWGVRCYSSTDLYNWEDEGLIIPPDPDDPSSPLHPTRI
MDRPHIIYNEKTGKYVCWLKLYPGGDVQYFGVLTADSPTGPYTYVHKFLGPLGMGAGDFDLVVDPDGKAY
LYFERVHKEVVCADLTDDYTDVTGEYSTHFPGLGPPFAREAPAVFKRGGKHYLLTSGTTGYFPNPSEVAV
ADSYHGPWTVLGNPHVGDGSETSFNSQISSVFKVPGKKDLYIAMADRWISRYVWLPIRF
>gnl|CDD|350148 cd18827, GH43_XlnD-like, Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); includes mostly xylanases. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have mostly been annotated as xylanases (endo-alpha-L-arabinanase, EC 3.2.1.8). It belongs to the GH43_bXyl-like subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_bXyl-like subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidases (EC 3.2.1.37) and xylanases, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
ADPEIRIFDGQYWIYPTYSAPYEEQTFFDAFSSPDLVHWTKHERILDMADVPWANRAVWAPSVIEKNGKY
YLYFAANDIQSDDEGGGIGVAVADRPEGPFKDALGKPLIGEFHNGAQPIDQHVFKDDDGQAYLYYGGWGH
CNVAKLNDDMTSLVPFDDGETFKEITPEGYVEGPFMFKRNGKYYFMWSEGGWTGPDYSVAYAVADSPLGP
FKRIGKILQQDPAIATGAGHHSVVNVPGTDDWYIVYHRRPLGETDGNHRVVCIDRMEFNEDGTIKPV
>gnl|CDD|350149 cd18828, GH43_BT3675-like, Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675). This glycosyl hydrolase family 43 (GH43) subgroup includes the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the GH43_bXyl subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_bXyl subgroup also includes enzymes annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
ADPDIAYFDGKYYIYPTTDGFPGWSGTQFHVFSSDDLVTWKDEGVILDLKNDQVVPWATGNAWAPTIEER
DGKYYFYFCGKNPDGRSQIGVAVADSPTGPFTAQGSPLITHEMARVTMGQAIDPSVFTDPVDGKYYLYWG
NGYAAIAELNDDMISIKPGTLVNLDGLTDFREAVTVLYRDGLYHFTWSCDDTGSENYHVNYGTSDSPYGP
ITYRGVILQKDPSKGILGTGHHSILQVPGTDEWYIAYHRFATPLGIYGSGLGYHRETCIDRLTFDADGLI
LPV
>gnl|CDD|350150 cd18829, GH43_BsArb43A-like, Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase Arb43A. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes annotated as having endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities, and includes Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase (AbnA;BSU28810) (Arb43A). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the arabinofuranosidase (ABF; EC 3.2.1.55) enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
THDPSIIKEGSTWWTFSTGDGIPVKYSSDGLNWTQGPPIFGSPLSWWKTYVPANTTNDVWAPDVHYYNGK
YWLYYAISTFGSNTSAIGLASASSIAAGNWTDEGLVLRSTSADNYNAIDPNLVIDASGNPWLVFGSFWSG
IKITRLDKATMKPTGSIYSIASRPSGGIEGPFIVYRDGYYYLFVSIDKCCRGVNSTYKIAYGRSTSITGP
YLDKNGKDMLNGGGTVLDSGNSRWKGPGGQDIYATGKNVIARHAYDANNNGAPKLLISDLYWD
>gnl|CDD|350151 cd18830, GH43_CjArb43A-like, Glycosyl hydrolase family 43 protein such as Cellvibrio japonicus Ueda107 endo-alpha-1,5-L-arabinanase / exo-alpha-1,5-L-arabinanase 43A (ArbA;CJA_0805) (Arb43A). This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes annotated with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities, and includes the bifunctional Cellvibrio japonicus Ueda107 endo-alpha-1,5-L-arabinanase / exo-alpha-1,5-L-arabinanase 43A (ArbA;CJA_0805) (Arb43A). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
VHDPVMAREGGTYYLFSTGPGISVMSSKDLKNWTQERPVFDEPPQWAKEAVPGFNGHIWAPDISFHNGRY
YLYYSCSAFGKNTSAIGVATNKTLDPDSPDYKWEDHGMVVQSVPGRDLWNAIDPNVIVDEKGTPWLSFGS
FWGGIKLVKLDPDLKSLAEPQEWHTIARRERTFKLTDSEAGPGAIEAPFIFKKGGYYYLFVSWDYCCRGV
NSTYKVVVGRSKNVTGPYLDKDGKSMLQGGGTLVVGGNKRWAGVGHNSVYTFDGKDYLVFHAYDAADNGA
SKLVIREIRWD
>gnl|CDD|350152 cd18831, GH43_AnAbnA-like, Glycosyl hydrolase family 43 protein such as Aspergillus niger endo-alpha-L-arabinanase (AbnA). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities such as Aspergillus niger AbnA, Aspergillus niveus AbnA, and Chrysosporium lucknowense Abn1. It belongs to the GH43_Arb43a subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_Arb43a subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. The GH43_Arb43a subgroup includes many enzymes such as Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, and are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
THDPSIIRREDGTYFRFSTGGGIRIATAPSLTGPWTYVGSVLPGGSSIDLAGNDDLWAPDVHYVNGTYYC
YYSVSTFGSQDSAIGVATSPTMEPGSWTDHGAVIRSSSGDPYNAIDPNLIVDDDGTPYLTFGSYWQGIFQ
VPLTDPLLSPAAGPPPTHLAYNPSGNHPEEGSFMYKHGGYYYLFFSSGICCGYDPSLPAPGEEYKIRVCR
STSPTGPFVDKDGRDCLEGGGTTVLLASHGNVYAPGGQGVYDDPVGGDVLYYHYVNTTIGYADGDAQFGW
NYLDFS
>gnl|CDD|350153 cd18832, GH43_GsAbnA-like, Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1,5-L-arabinanase AbnA. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. It includes Geobacillus stearothermophilus T-6 NCIMB 40222 AbnA, Bacillus subtilis subsp. subtilis str. 168 (Abn2;YxiA;J3A;BSU39330) (Arb43B), and Thermotoga petrophila RKU-1 (AbnA;TpABN;Tpet_0637). These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
VHDPSIVKDDGTYYVFGSHLAAAKSTDLMNWTQFTNGVTTDNPLLFNLFDSTAWELAEDFNWAGGGNLWA
PDVIYNKAMGKYCMYYSVSGDDSPSAIGLATADNIEGPYTYKGTVLKSGFTGSTSADADVYLTGGKYNNN
YHPNAIDPCVFYDKDGKLWMVYGSWSGGIFLLELDPKTGLRDYSVETDGNLPDQYYGKKIAGGYHASGEG
PYILYDKDTGYYYLFVSYGGLDANGGYNIRVFRSKNPDGPYVDAAGNDAIYTSGNDNLGLKDGGIIELMG
NYKLPGLGTGYVSPGHNSAYYDEDGKYYLVYHTRFPGGGEYHEVRVHQMFMN
>gnl|CDD|350154 cd18833, GH43_PcXyl-like, Glycosyl hydrolase family 43 protein such as the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). This glycosyl hydrolase family 43 (GH43) subgroup includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a characterized bifunctional enzyme with beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37)/ alpha-L-arabinofuranosidase (EC 3.2.1.55) activities. This subgroup belongs to the GH43_XybB subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_XybB subgroup includes enzymes having beta-1,4-xylosidase and alpha-L-arabinofuranosidase activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43_XybB subgroup includes Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller
NPIIPGFHPDPSCIFVPEWDGTFFCVTSSFLAFPGIPIYASKDLINWKLISNVLSRPSQLPELATTGTGQ
QGGIWAPTLRYHDGTFYVITTLVFPDKTDASRWDNLLFTTTDPYSDSAWSDPIRFDFPGYDPDLFWDDDG
TAYVQGAHYWRVRPEIQQQEIDLKTGESLSPSPIWNGTGGSAPEGPHMYKKDGWYYLLIAEGGTGLGHSV
TIARSRSIWGPYESYPSNPVLTNANTSEYFQTVGHADLFQDANGNWWGVALATRSGPEYEIYPMGRETVL
YPVTWEEGEWPV
>gnl|CDD|467581 cd18869, NUDIX_U8_SnoRNA_DE_Nudt16, nucleoside diphosphate-linked moiety X)) motif 16. U8 SnoRNA-decapping enzyme, also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 16/Nudt16, is encoded by the human NUDT16 gene and a RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
GYRHACHAMLYAPNPGKLFGRYPIRATLLMQMRFDGLLGFPGGFVDTGESLEEGLNRELREELGLAHAVF
PVTEDDYRSSHVREGPKRLVLHFYAKELSLEELDEIEIAAVNAKDHGLEVLGLIRVPLYTLRDGYGGLPT
FLANSFIGNAREQLLEALISLNLLPEEEITEALIA
>gnl|CDD|467582 cd18870, NUDIX_AcylCoAdiphos_Nudt19, Nucleoside diphosphate-linked moiety X)) motif 19. Acyl CoA diphosphohydrolase (also known as NUDIX (nucleoside diphosphate linked moiety X))-type motif 10; Nudt19; testosterone-regulated protein rp2) has activity towards CoA, oxidized CoA and a wide range of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA esters. CoA is the major acyl carrier in mammals and a key cofactor in energy metabolism. Dynamic regulation of CoA in different tissues and organs supports metabolic flexibility. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
PAATVILLRDGADGLEVLLLRRSSTMSFMPGAYVFPGGRVDPADRDAPWAGLLPPDVASASRPGKSDPEA
RALRIAAIRETFEETGLLLAWARWITPPGMPRRFDTRFFLAPLPAGQEPVHDGGETVEARWVTPREALEA
AEAGEIPLPPPTFYELTRL
>gnl|CDD|467583 cd18871, NUDIX_Cfim25_Nudt21, 25 kDa subunit of cleavage factor Im. Precursor mRNA (pre-mRNA) cleavage factor I(m) (also called NUDIX (nucleoside diphosphate linked moiety X))-type motif 21) is a oligomer composed of a small 25 kDa subunit (CF I(m)25) and a variable larger subunit of either 59, 68 or 72 kDa and plays an important role in pre-mRNA 3'-end cleavage and the selection of poly(A) sites in a 3'-untranslated region (3'-UTR) of mRNA, producing mRNAs with variable 3' ends. The small subunit also interacts with RNA, poly(A) polymerase, and the nuclear poly(A)-binding protein and belongs to the NUDIX hydrolase superfamily. NUDIX hydrolases are found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes
IYPLTNYTFGTKEAKVEKDSSVAARLQRLKEEYEKDGMRRTVEGVLLVHEHGHPHVLLLQLGNSFFKLPG
GRLRPGEDEVEGLKRKLTEKLSPEDSEVLNDWEIGDCLGVWWRPNFETPMYPYLPAHITKPKECKKLYLV
QLPEKCLFAVPKNYKLLAVPLFELYDNAARYGPIISSLPQLLSR
>gnl|CDD|467584 cd18872, NUDIX_eIF-2B, translation initiation factor IF-2B alpha subunit. Eukaryotic translation initiation factor 2B subunit alpha (EIF2B1) is one of five subunits of eukaryotic translation initiation factor 2B (EIF2B), a GTP exchange factor for eukaryotic initiation factor 2 and an essential regulator for protein synthesis. Mutations in this gene and the genes encoding other EIF2B subunits have been associated with leukoencephalopathy with vanishing white matter. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
SVVTSFLFHDGKVLLFRRSDKVGTYQGRWAGISGSIESDDPPLAAAWREIREETGLTPEDVELLRQGKPF
EFTDESLGREWTVHPFLFRLKDDRAIKLDWEHTEWEWVDPTDILDYETVPRLWESLRRV
>gnl|CDD|467585 cd18873, NUDIX_NadM_like, bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins. Bacterial NadM-Nudix is a bifunctional enzyme containing a nicotinamide mononucleotide (NMN) adenylyltransferase (NMNAT) and an ADP-ribose pyrophosphatase (ADPRase) domain. NMNAT was initially identified as an NAD+ synthase that catalyzes the reversible conversion of NMN to NAD+ in the final step of both the de novo biosynthesis and salvage pathways in most organisms across all three kingdoms of life ADPRase is a member of the NUDIX family proteins, catalyzes the metal-induced and concerted general acid-base hydrolysis of ADP ribose (ADPR) into AMP and ribose-5'-phosphate (R5P). Additional members in this cd include bacterial transcriptional regulator, NrtR, which represses the transcription of NAD biosynthetic genes in vitro and adenosine diphosphate ribose (ADPR), as well as NadQ, a NUDIX-like ATP-responsive regulator of NAD biosynthesis. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belong to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, U=I, L or V) which functions as metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
PSVTVDCVIFGFDDGELKVLLIKRKNEPFKGGWALPGGFVREDETLEDAARRELREETGLKDIYLEQLGT
FGDPDRDPRGRVISVAYLALVPEEDLAPKAGDDAAEARWFPVDELLPPLAFDHAEIIADALE
>gnl|CDD|467586 cd18874, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
PEPTVGALIFNPDGKVLLVRSHKWNDLYGIPGGKVEWGETLEEALKREVKEETGLDITDIRFILVQESIN
SEEFHKPAHFVFVDYLARTDSSEVVLNEEAVEYLWVEPEEALKYPLNSFTRLLLE
>gnl|CDD|467587 cd18875, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
VELTNMCMIYDGEDRVLVLDRVKKDWGGYTFPGGHVEPGESFVDSVIREVKEETGLTIKNPELCGIKQWI
NPDGERYIVFLYKTDHFSGELLSSEEGELFWIPIEELKKLPLATDFDEMLRVFESDDLSEFFYYREGDDW
NKKL
>gnl|CDD|467588 cd18876, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
AAAGALFTDAAGRVLLVKPTYKDGWELPGGVVEAGESPLQAARREVREELGLDVPVGRLLAVDWVPPAGG
GDDAVLFVFDGGVLTPEQAAAIRLQDEELSAYRFVTPEEAAELLPPRLARR
>gnl|CDD|467589 cd18877, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
DGWVICACGSRHWGRHGAAGLLLFAPAEDGGPHVLLQHRAWWTHQGGTWALPGGARDSGETPEAAALRET
EEETGLDADTLRVVGTHVDDHGGWSYTTVLASAPEPLPVRPANEESVELRWVPLDEVESLPLHPGFAASW
P
>gnl|CDD|467590 cd18879, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
PDFILELREHIGHDPLWLPGVTAVVLRDAGRVLLVRRADNGRWTPVTGIVEPGEQPADAAVREVLEETGV
DVEVERLASVGASPPVTYPNGDQCQYLDLTFRCRPVGGEARVNDDESLEVGWFPVDALPPMLPRFRRRIA
LA
>gnl|CDD|467591 cd18880, NUDIX_ADPRase, ADP-ribose pyrophosphatase and similar proteins. ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). ADPRase-m is also known as NUDT9. It can be distinugished from the cytosolic ADPRase by a N-terminal target sequence unique to mitochondrial ADPRase. NUDT9 functions as a monomer
RIRAKAIIIEDGKLLLVKHRDEGGIFYILPGGGQEHGETLPEALKRECLEETGLDVEVGDLLFVREYIGP
NKPVHQVELFFLCTLEGGELTLGSDPDLNQVGVEWIPLEELDSIRLYPAILRELII
>gnl|CDD|467592 cd18881, NUDIX_Tm1382, uncharacterized NUDIX hydrolase subfamily Tm1382 found in Thermotoga maritima, and similar proteins. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
ERVLVVKTEVFPALFGFQGSLIPLEAELLRRVEQEGFFVERPEAEYDETHRQIIPYAVVRHRDRYLLMRR
TKKQAEARLHNLYTLGVGGHINPEDGGGPREAFLKGLRRELLEEVDVRAYSLQYVGLINMADTPVSRVHA
GVVFIAEVKFEGRVEKEKFEGRLAKLEELQEVYEGMEGWSKVVADYL
>gnl|CDD|467593 cd18882, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
HEVAIAILYDDRGKVLLQLRDDKPGIPYPGYWGLFGGHLEPGETPEEAIRRELEEEIGYEPGEFRFFLLY
TEDDGEDRIRHVFHAPLDVDLSDLVLNEGQALRLFSPEEILQGPLYSNLAGILRPLLAIH
>gnl|CDD|467594 cd18883, NUDIX_MutT_Nudt1, MutT homolog-1 and similar proteins. MutT homolog-1 (MTH1), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 1/Nudt1, is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases
YTARGVIISDEHLLLARVKGDDKTFLPGGHIEIGESAEIALVRELREELGLSCKVGRYLGAVENQWQDKE
VIHVELNHLFEVELQDLHTSDTPESQEPHLEFYWIPYNDLELHNLQPMPLRNLLLNRKLSDGLFWC
>gnl|CDD|467595 cd18884, NUDIX_Hydrolase, uncharacterized NUDIX hydrolase subfamily. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase
GFVHWNNPIPVVAAIVEHDGHIVLARNKAWPEGWYGLVTGFLEAGESPEEAVLREVKEELGLDGHEAKFI
GHYAFPERNQLIIAYHVRARGNVKLNEELDDYKIVPIDKLRPWPFGTGYAVRDWL
>gnl|CDD|467596 cd18886, NUDIX_MutT_Nudt1, MutT homolog-1 and similar proteins. MutT homolog-1 (MTH1), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 1/Nudt1, is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases
KYTLCFIIRDDEVLLLNRNKKPNMGKWNGVGGKLEPGESPEECAIREVFEETGLELEDLQLRGIVTFPSF
DGGEDWLMYVFLAEAFSGELVESDREGILAWVPIDWLLNLPLWEGDRYFLPLLFDNEPPFEGKFHYDGGR
LLDYEVN
>gnl|CDD|467597 cd18887, NUDIX_UGPPase_Nudt14, UDP-glucose pyrophosphatase. UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 14; Nudt14) hydrolyzes the pyrophosphate of the nucleoside diphosphate sugar to generate glucose-1-P and UMP. In mammals, UDP-glucose is the glucosyl donor for the synthesis of the storage polysaccharide glycogen. UGPPase, as a regulator of UDP-glucose, could play a regulatory role, but it has been shown to prefer ADP-ribose over UDP-glucose. Like other members of the NUDIX hydrolase superfamily, it requires a divalent cation, such as Mg2+, for its activity. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site
YKQNGKKKTWDFVKSHDSVAILLYNKTRDAFVLVKQFRPAVYASQVRAAERNGGKDTEKYPPELGYTYEL
CAGLVDKDKSLEEIAQEEILEECGYDVPLEDLEKITSFRSGVGTSGSRQTLFYAEVTDDMKVSEGGGVEE
EGEMIEVVELPVEEAKEFIFDEEIPKPPGLLFALLWFLQNK
>gnl|CDD|467598 cd18888, NUDIX_ADPRase_Nudt5, ADP-ribose pyrophosphatase. ADP-ribose pyrophosphatase (ADPRase) (also known as NUDIX (Nucleoside diphosphate-linked moiety X)) motif 5; Nudt5) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity
DVDAVAIIAILKRKLKPPELVLVKQYRPPVNAYTIEFPAGLVDPGESPEQAALRELKEETGYTGEKVLSV
SPPLALDPGLSNANMKLVTVEVDGDDPENQNPKQELEDGEFIEVILVPLNELLERLQELAKEEGYAIDAR
LYSFALGLS
>gnl|CDD|467599 cd18889, NUDIX_ADPRase, ADP-ribose pyrophosphatase. ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). ADPRase-m is also known as NUDT9. It can be distinugished from the cytosolic ADPRase by a N-terminal target sequence unique to mitochondrial ADPRase. NUDT9 functions as a monomer
PKIDTRAAIFKDDKILLVQEKDGRWSLPGGWVDVNQSIKENTIKEAKEEAGLDVEPKRIIAVLDRNKHNK
PPYAYGIYKIFVLCELLGGEFQPNIETIESGYFSLDELPPLSEEKNTKEQIEMCFEA
>gnl|CDD|467600 cd18890, NUDIX_CDP-Chase, CDP-choline pyrophosphatase. CDP-choline pyrophosphatase catalyzes the hydrolysis of CDP-choline to produce CMP and phosphocholine. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
PKVDIRAVVFNDKEEILLVKEKEDGKWTLPGGWADVGYTPTEVAAKEVEEETGLEVSPKKLLAILDKRKH
PHPPQPTYVYKLFILCEIEGGELKPSFETGEVRFFSENELPELSTDRVTEEQIKELFAY
>gnl|CDD|467601 cd18891, NUDIX_UDP-X_diphosphatase, UDP-X diphosphatase. UDP-X diphosphatase hydrolyzes UDP-N-acetylmuramic acid and UDP-N-acetylmuramoyl-L-alanine, the last step of the Mur pathway of peptidoglycan biosynthesis. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required
PKVDVRAFIQNENKVLLVQDKHTKEWALPGGFAEVGLSPKENILKEVKEETGLHVEVERLLAVFDTDLRQ
DIPQSFQYYKFIFACKILDGEFQENSETSDLQYFSLDQLPNLSLKRTTKEQLQQLFKV
>gnl|CDD|380671 cd18892, TET, oxygenase domain of ten-eleven translocation (TET)1, TET2, and TET3 methylcytosine dioxygenases and similar proteins. TET proteins are involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. Alterations in TET protein function have been linked to cancer, and TETs influence many cell differentiation processes. TET family genes have been implicated as tumor suppressors, for example mutations/deletions of the TET2 gene frequently occur in multiple spectra of myeloid malignancies. TET3 acts as a suppressor of ovarian cancer by demethylating the miR-30d precursor gene promoter to block TGF-beta1 induced epithelial-mesenchymal transition (EMT). TET3 (and TET2) promoters are silenced in melanoma cells by mechanisms triggered by TGF-beta and mediated by DNA methyltransferase 3 alpha (DNMT3A). TET genes are downregulated in endometriosis. TET proteins belong to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity
CGCFPPDESPPEPGPYYTHLGAGPSLAALRELLEKRTGVTGKAIRIEKVIYTGKEGKTSQGCPIAKWIIR
RSSLEEKYLVLVKHRPGHFCHSAFIVICIVAWEGVPQSNADELYSLLTDKLNKFGLPTKRRCGTNEERTC
ACQGLDPETCGASFSFGCSWSMYYNGCKFARSKTVRKFRLSDKSEEEELEDKLQNLATHLAPLYKSLAPD
SYKNQVQFEEEALDCRLGLKPGRPFSGVTACVDFCAHAHKDLHNMNNGCTVVVTLTKHRNLTKPEPEQLH
VLPLYLYDMTDEDEFGSVEGQEEKVRNGSIEVLTKYPCEVREYWSDSEECFLDPDIGGVAIALSHGSVLF
ECAKRELHATTPLKNPNRQHPTRISLVFYQHKNLNYSRHGLAEYEAKM
>gnl|CDD|380672 cd18893, TET-like, oxygenase domain of ten-eleven translocation (TET)-like proteins such as Naegleria gruberi Tet-like protein (NgTet1) and similar proteins. Naegleria gruberi Tet1 can catalyze the iterative oxidation of both 5-methylcytosine (5mC) and thymidine (T) on various DNA forms. Like mammalian TETs, it catalyzes the oxidation of 5mC to 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC) in three consecutive, Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate, 2-OG)-dependent oxidation reactions. Like JBP1 and JBP2, NgTet1 can perform T-oxidation to form 5-hydroxymethyluridine (5hmU), but in addition it can catalyze the formation of 5-formyluridine (5fU) and 5-carboxyluridine (5caU). This family belongs to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity
KKSLEQNLLKKCNTTFQSFTNANITLVYGKDDKWLKNVRTNYFVVDKEGSVELALLPNVLPKELVEEFTE
KFESIQTGLKTEKDIDKSGWWTMNKPMGYSCIDDNSMPFNYTKVIADLLQDLGQYLLEIVNPQINYKISK
LLECVCLYPSTCFNSLKPSNEGHRIRKPHKDNLDIGPSSLFYFGNFQEGYLELTDKNEKCKVFVQPGDVV
FLRGNEYKHVVANITPQSSGWRIGLVYFAHKGS
>gnl|CDD|380673 cd18894, JBP-like, oxygenase domain of J-binding protein (JBP) 1 and JBP2 thymidine hydroxylases and similar proteins, including uncharacterized bacterial and phage proteins. J binding protein (JBP) 1 and JBP2 catalyze the first step of base J biosynthesis: the hydroxylation of thymine in DNA to form 5-hydroxymethyluracil (hmU). Base J (beta-d-glucopyranosyloxymethyluracil) is a hyper-modified DNA base found in the DNA of kinetoplastids (Trypanosoma brucei, Trypanosoma cruzi, and Leishmania). JBP1 and JBP2 each contain a J-DNA binding domain and this oxygenase domain. They belong to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity
TESRESDETLVPFEGNFEGEDDFNILDTGDTKVREPNGRLLAVYLKNALPKKITRKAAAVLEPAATRKTL
RRGIASGGLPPRSGIVGYGDYDRNPTELKCRKTAFTRRNWPKWPAVIPLLQYISKLYKEHAPERYKAQKE
AIPDTYVIFGTVFSTVTVNKNFRTAVHTDAGDFKGGGGLLAVLDGEYEGGYLALPKYRVAFDMQPGDVLL
FDTHLWHGNTEVHCKCEDWERISVVFYYRTGLGECGCEEE
>gnl|CDD|380674 cd18895, TET1, oxygenase domain of ten-eleven translocation (TET)1 methylcytosine dioxygenase and similar proteins. TET1 is involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). Human TET1 (and TET2) are more active on 5mC-DNA than 5hmC/5fC-DNA substrates. TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. TET1 plays multiple roles in in tumor development and progression. TET1 serves as a tumor suppressor gene; loss of TET1 is associated with tumorigenesis and can be used as a potential biomarker for cancer therapy. In addition to its dioxygenase activity, it can induce epithelial-mesenchymal transition and act as a coactivator to regulate gene transcription. The regulation of TET1 is also correlated with microRNA in a posttranscriptional modification process. TET1 belongs to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity
CDCVEQIIEKDEGPYYTHLGAGPSVAAVREIMENRYGEKGNAIRIEVVVYTGKEGKSSQGCPIAKWVIRR
SSDEEKLLCLVRQRAGHHCQTAVIVILILAWEGIPRLLADRLYQELTQTLKKYGSPTSRRCALNEDRTCA
CQGLDPETCGASFSFGCSWSMYFNGCKFARSKYPRKFRLLTDDPKEEENLESNLQNLATDVAPVYKKLAP
EAFQNQVENENVAPDCRLGSKEGRPFSGVTACIDFCAHAHKDTHNMHNGSTVVCTLTKEDNRSVGVIPED
EQLHVLPLYKISDTDEFGSEEGQEAKIKNGAIQVLSAFPREVREVWSDSEHNFLDEDIGGVAVAPSHGSI
LIECARRELHATTPIKKPNRNHPTRISLVFYQHKNLNEPKHGLALWEAKMAEKAKEKEKE
>gnl|CDD|380675 cd18896, TET2, oxygenase domain of ten-eleven translocation (TET)2 methylcytosine dioxygenase and similar proteins. TET2 is involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). Human TET2 (and TET1) have been shown to be more active on 5mC-DNA than 5hmC/5fC-DNA substrates. TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. TET2 acts as a tumor suppressor in hematopoiesis; mutations/deletions of the TET2 gene frequently occur in multiple spectra of myeloid malignancies. TET2 (and TET3) promoters are silenced in melanoma cells by mechanisms triggered by TGF-beta and mediated by DNA methyltransferase 3 alpha (DNMT3A), which play a functional role in the epithelial-mesenchymal transition process and metastasis. In addition, TET2 (and TET3) may be guardians of regulatory T cell stability and immune homeostasis. TET2 belongs to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity
DFPSCSCVEQIIEKDEGPYYTHLGAGPNVAAIREIMEERFGQKGKAIRIERVIYTGKEGKSSQGCPIAKW
VIRRSSEEEKLLCLVRERAGHSCETAVIVILILVWEGIPISLADKLYSELTDTLRKYGTLTNRRCALNEE
RTCACQGLDPETCGASFSFGCSWSMYYNGCKFARSKIPRKFKLLGDDPKEEEKLESNLQNLSTLMAPTYK
KLAPDAYNNQIEYEHRAPDCRLGLKEGRPFSGVTACLDFCAHAHRDLHNMQNGSTLVCTLTREDNREIGK
IPEDEQLHVLPLYKVSDVDEFGSTEAQEEKKRNGAIQVLSSFRRKVRMLAEPVKTCRQRKLEDEVWSDSE
QSFLDPDIGGVAVAPSHGSILIECAKRELHATTPLKNPNRNHPTRISLVFYQHKSMNEPKHGLALWEAKM
AEKAREKEEECEKY
>gnl|CDD|380676 cd18897, TET3, oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar proteins. TET3 is involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. TET3 serves as a tumor suppressor; it acts as a suppressor of ovarian cancer by demethylating the miR-30d precursor gene promoter to block TGF-beta1 induced epithelial-mesenchymal transition (EMT). TET3 (and TET2) promoters are silenced in melanoma cells by mechanisms triggered by TGF-beta and mediated by DNA methyltransferase 3 alpha (DNMT3A), which play a functional role in the EMT process and metastasis. In addition, TET3 (and TET2) may be guardians of regulatory T cell stability and immune homeostasis. TET3 has been shown to prevent terminal differentiation of adult neural stem cells by a mechanism involving direct binding and repression of TET3 to the imprinted gene Snrpn. TET3 has also been shown to mediate the activation of hepatic stellate cells via modulation of the long non-coding RNA HIF1A-AS1 expression. TET1 belongs to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity
CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRR
SSEEEKLLCLVRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCA
CQGKDPNTCGASFSFGCSWSMYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAP
QAYQNQVTNEDIAIDCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTVGKIPED
EQLHVLPLYKMSTTDEFGSEENQNEKIGSGAIQVLTSFPREVREVWSDSEHNFLDENIGGVAVAPAHGSI
LIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKLLAERARARQEEAARLGLQ
QEIKPYGKKRKWGGAPAAEPQPKEKKDKIPTR
>gnl|CDD|381478 cd18908, bHLH_SOHLH1_2, basic helix-loop-helix (bHLH) domain found in the spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein (SOHLH) family. The SOHLH family includes two bHLH transcription factors, SOHLH1 and SOHLH2. They are specifically in spermatogonia and oocytes and essential for early spermatogonial and oocyte differentiation
SDASSHSLKERLRRERIKSSCDQLRDLLPYIKGRKLDMASVLEMTVKYIRYIQERIPPE
>gnl|CDD|381479 cd18909, bHLH_TCFL5, basic helix-loop-helix (bHLH) domain found in transcription factor-like 5 protein (TCFL5) and similar proteins. TCFL5, also termed Cha transcription factor, or HPV-16 E2-binding protein 1 (E2BP-1), is a bHLH transcription factor that plays a crucial role in spermatogenesis. It regulates cell proliferation or differentiation of cells through binding to a specific DNA sequence like other bHLH molecules
QRRERHNRMERDRRRRIRICCDELNLLVPFCNAETDKATTLQWTTAFLKYIQEKHGDSLK
>gnl|CDD|381480 cd18910, bHLHzip_USF3, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in basic helix-loop-helix domain-containing protein USF3 and similar proteins. USF3, also termed upstream transcription factor 3, is a bHLHzip protein that is involved in the negative regulation of epithelial-mesenchymal transition, the process by which epithelial cells lose their polarity and adhesion properties to become mesenchymal cells with enhanced migration and invasive properties
RREKKRESHNEVERRRKDKINAGINKIGELLPDRDAKKQSKNMILEQAYKYIVELKKKNDKLLLN
>gnl|CDD|381481 cd18911, bHLHzip_MGA, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) and similar proteins. MGA, also termed MAX dimerization protein 5 (MAD5), is a dual specificity T-box/ bHLHzip transcription factor that regulates the expression of both Max-network and T-box family target genes. It contains a Myc-like bHLHZip motif and requires heterodimerization with Max for binding to the preferred Myc-Max-binding site CACGTG. In addition to the bHLHZip domain, MGA harbors a second DNA-binding domain, the T-box or T-domain. It thus binds the preferred Brachyury-binding sequence and represses transcription of reporter genes containing promoter-proximal Brachyury-binding sites
RRTHTANERRRRNEMRDLFEKLKRTLGLHNLPKVSKYYILKQAFEEIQGLTDQADRLIGQKTLLT
>gnl|CDD|381482 cd18912, bHLH_TS_bHLHa9, basic helix-loop-helix (bHLH) domain found in Class A basic helix-loop-helix protein 9 (bHLHa9) and similar proteins. bHLHa9, also termed Class F basic helix-loop-helix factor 42 (bHLHf42), is a bHLH transcription factor that plays an essential role in limb development
RPVRSKARRVAANVRERKRILDYNQAFNALRLALKHDLGGKRLSKIATLRRAINRISALSLFL
>gnl|CDD|381483 cd18913, bHLH-O_hairy_like, basic helix-loop-helix-orange (bHLH-O) domain found in Drosophila melanogaster protein hairy, protein deadpan and similar proteins. Protein hairy is a bHLH transcriptional repressor of genes that require a bHLH-O protein for their transcription. It acts as a pair-rule protein that regulates embryonic segmentation and adult bristle patterning. Protein deadpan is closely related to the product of the segmentation gene hairy. It is a direct target of Notch signaling and regulates neuroblast self-renewal in Drosophila
ESRKSSKPIMEKRRRARINASLNELKSLLLDALKKDGTRHSKLEKADILEMTVKHLRQVQRQQLAVA
>gnl|CDD|381484 cd18914, bHLH_AtORG2_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana OBP3-responsive gene 2 (ORG2), 3 (ORG3) and similar proteins. The family includes ORG2 (also termed AtbHLH38, or EN 8) and ORG3 (also termed AtbHLH39, or EN 9), both of which act as bHLH transcription factors
KKLLHNDVERQRRQEMASLFSSLRSLLPLQYIKGKLSVSDHVDEAVNYIKELQEKIKELSEKRDELLKLI
SGVRSEE
>gnl|CDD|381485 cd18915, bHLH_AtLHW_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein LONESOME HIGHWAY (LHW) and similar proteins. The family includes several bHLH transcription factors from Arabidopsis thaliana, such as LHW, and EMB1444. LHW, also termed AtbHLH156, or bHLH delta, is a bHLH transcription activator that regulates root development and promotes the production of stele cells in roots. It coordinately controls the number of all vascular cell types by regulating the size of the pool of cells from which they arise. EMB1444, also termed AtbHLH169, or lonesome highway-like protein 1, or protein embryo defective 1444, may regulate root development
ESPRPRPKDRQMIQDRIKELREIVPNGAKCSIDALLERTIKHMLFLQSVSKHADKLKQSGESKMQKEEEG
T
>gnl|CDD|381486 cd18916, bHLH-O_ESM5_like, basic helix-loop-helix-orange (bHLH-O) domain found in Drosophila melanogaster Enhancer of split proteins, E(spl)m5, E(spl)m8 and similar proteins. The family includes two bHLH-O transcriptional repressors, E(spl)m5 and E(spl)m8, which participate in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo. They bind DNA on N-box motifs, 5'-CACNAG-3'
KSKKPMLERQRRARINKCLSELKTLVAECSGDDGCLRMDKAEMLETAVAFMRQQQTAKN
>gnl|CDD|381487 cd18917, bHLH_AtSAC51_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana suppressor of acaulis 51 (SAC51) and similar proteins. SAC51, also termed AtbHLH142, or EN 128, is a bHLH transcription factor that is involved in stem elongation, probably by regulating a subset of genes involved in this process
GLSNEKSRKEKIKKAVKLLRSIVPGGESMDTALVLDEAIDYLKSLKMELQSLE
>gnl|CDD|381488 cd18918, bHLH_AtMYC1_like, basic Helix-Loop-Helix (bHLH) domain found in Arabidopsis thaliana MYC1 and similar proteins. MYC1, also termed AtbHLH12, or EN 58, acts as a transcription activator, when associated with MYB75/PAP1 or MYB90/PAP2
LFATERERREKLNEKFSDLRNLIPNPTKNDRASILSDAIKYINELQRTVEELKSLVEKKRCGERDRKTTE
>gnl|CDD|381489 cd18919, bHLH_AtBPE_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana BIG PETAL (BPE) and similar proteins. The family includes several bHLH transcription factors from Arabidopsis thaliana, such as BPE, HBI1 and BEE proteins (BEE1-3). BPE, also termed AtbHLH31, or EN 88, is involved in the control of Arabidopsis petal size, by interfering with postmitotic cell expansion to limit final petal cell size. HBI1, also termed AtbHLH64, or homolog of bee2 interacting with IBH1, or EN 79, is an atypical bHLH transcription factor that acts as positive regulator of cell elongation downstream of multiple external and endogenous signals by direct binding to the promoters and activation of the two expansin genes EXPA1 and EXPA8, encoding cell wall loosening enzymes. BEEs, also termed protein Brassinosteroid enhanced expression, are positive regulators of brassinosteroid signaling
DYIHVRARRGQATDSHSLAERVRREKISERMKLLQDLVPGCNKVTGKALMLDEIINYVQSLQRQVEFLSM
KLAAVNPRLDFNSEDL
>gnl|CDD|381490 cd18920, bHLH-O_HEY2, basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with YRPW motif protein 2 (HEY2) and similar proteins. HEY2, also termed cardiovascular helix-loop-helix factor 1 (CHF-1), or Class B basic helix-loop-helix protein 32 (bHLHb32), or HES-related repressor protein 2, or hairy and enhancer of split-related protein 2 (HESR-2), or hairy-related transcription factor 2 (HRT-2), or protein gridlock homolog, is a bHLH-O transcriptional repressor expressed preferentially in the developing and adult cardiovascular system. As a downstream effector of Notch signaling, HEY2 may be required for cardiovascular development. It also plays an important role in neurologic development, as well as in the progression of human cancers
PTTTSQIMARKKRRGIIEKRRRDRINNSLSELRRLVPTAFEKQGSAKLEKAEILQMTVDHLKMLQATGGK
GYFDAHALAMDF
>gnl|CDD|381491 cd18921, bHLHzip_SREBP1, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein 1 (SREBP1) and similar proteins. SREBP1, also termed Class D basic helix-loop-helix protein 1 (bHLHd1), or sterol regulatory element-binding transcription factor 1 (SREBF1), is a member of a family of bHLHzip transcription factors that recognize sterol regulatory element 1 (SRE-1). It acts as a transcriptional activator required for lipid homeostasis. It may control transcription of the low-density lipoprotein receptor gene as well as the fatty acid. SREBP1 has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3')
PSKGEKRTAHNAIEKRYRSSINDKIIELKDLVVGTEAKLNKSAVLRKAIDYIRFLQQSNQKLKQENMALK
MAVQK
>gnl|CDD|381492 cd18922, bHLHzip_SREBP2, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein 2 (SREBP2) and similar proteins. SREBP2, also termed Class D basic helix-loop-helix protein 2 (bHLHd2), or sterol regulatory element-binding transcription factor 2 (SREBF2), is a member of a family of bHLHzip transcription factors that recognize sterol regulatory element 1 (SRE-1). It acts as a transcription activator of cholesterol biosynthesis
PKEGERRTTHNIIEKRYRSSINDKIIELKDLVMGTDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENMALK
LANQKNK
>gnl|CDD|381493 cd18923, bHLHzip_USF2, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in upstream stimulatory factor 2 (USF2) and similar proteins. USF2, also termed Class B basic helix-loop-helix protein 12 (bHLHb12), or major late transcription factor 2, or FOS-interacting protein (FIP), or upstream transcription factor 2, is a bHLHzip transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters
RTPRDERRRAQHNEVERRRRDKINNWIVQLSKIIPDCNTDNSKTGASKGGILSKACDYIRELRQTNQRMQ
ETYKEAERLQ
>gnl|CDD|381494 cd18924, bHLHzip_USF1, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in upstream stimulatory factor 1 (USF1) and similar proteins. USF1, also termed Class B basic helix-loop-helix protein 11 (bHLHb11), or major late transcription factor 1, is a bHLHzip transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters. It is ubiquitously expressed and involved in the transcription activation of various functional genes implicated in lipid and glucose metabolism, stress response, immune response, cell cycle control and tumour suppression. USF-1 recruits chromatin remodeling enzymes and interact with co-activators and the members of the transcription pre-initiation complex. Genetic polymorphisms of USF1 are associated with some metabolic and cardiovascular diseases, like diabetes, atherosclerosis, coronary artery calcifications and familial combined hyperlipidaemia (FCHL)
RDEKRRAQHNEVERRRRDKINNWIVQLSKIIPDCSMESTKSGQSKGGILSKACDYIQELRQSNHR
>gnl|CDD|381495 cd18925, bHLHzip_TFEC, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor EC (TFEC) and similar proteins. TFEC, also termed Class E basic helix-loop-helix protein 34 (bHLHe34), or transcription factor EC-like (TFEC-L), is a bHLHzip transcriptional regulator that acts as a repressor or an activator and regulates gene expression in macrophages. It plays an important role in the niche to expand hematopoietic progenitors through the modulation of several cytokines
KERQKKDNHNLIERRRRYNINYRIKELGTLIPKSNDPDMRWNKGTILKASVEYIKWLQKEQQRARELEHR
QKKLEQANRRLLLRI
>gnl|CDD|381496 cd18926, bHLHzip_MITF, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in microphthalmia-associated transcription factor (MITF) and similar proteins. MITF, also termed Class E basic helix-loop-helix protein 32 (bHLHe32), is a bHLHzip transcription factor that is involved in neural crest melanocytes development as well as the pigmented retinal epithelium. It regulates the expression of genes with essential roles in cell differentiation, proliferation and survival. It binds to M-boxes (5'-TCATGTG-3') and symmetrical DNA sequences (E-boxes) (5'-CACGTG-3') found in the promoters of target genes, such as BCL2 and tyrosinase (TYR)
ESEARALAKERQKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPDMRWNKGTILKASVDYIRKLQREQQ
RAKELENRQKKLEHANRHLLLRIQELEMQARAHG
>gnl|CDD|381497 cd18927, bHLHzip_TFEB, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor EB (TFEB) and similar proteins. TFEB, also termed Class E basic helix-loop-helix protein 35 (bHLHe35), is a bHLHzip transcription factor that is required for vascularization of the mouse placenta. It specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Its efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFE3 or MITF
EARALAKERQKKDNHNLIERRRRFNINDRIKELGTLIPKTNDLDVRWNKGTILKASVDYIKRMQKDLQRS
RELENHSRRLEMTNKQLWLRI
>gnl|CDD|381498 cd18928, bHLHzip_TFE3, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor E3 (TFE3) and similar proteins. TFE3, also termed Class E basic helix-loop-helix protein 33 (bHLHe33), is a bHLHzip transcription factor that is involved in B cell function. It specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Its efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFEB or MITF
EAKAFLKERQKKDNHNLIERRRRFNINDRIKELGTLIPKSTDPEMRWNKGTILKASVDYIRKLQKEQQRS
KEIEMRQRKLEQANRSLQLRI
>gnl|CDD|381499 cd18929, bHLHzip_Mad4, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 4 (Mad4) and similar proteins. Mad4, also termed Max dimerization protein 4, or Max dimerizer 4 (MXD4), or Class C basic helix-loop-helix protein 12 (bHLHc12), or Max-interacting transcriptional repressor MAD4, is a bHLHZip Max-interacting transcriptional repressor that suppresses c-myc dependent transformation and is expressed during neural and epidermal differentiation. It is regulated by a transcriptional repressor complex that contains Miz-1 and c-Myc
NNRSSHNELEKHRRAKLRLYLEQLKQLVPLGPDSTRHTTLSLLKRAKMHIKKLEEQDRKALNIKEQLQRE
HRYLKRRLEQLSVQGMER
>gnl|CDD|381500 cd18930, bHLHzip_MXI1, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-interacting protein 1 (MXI1) and similar proteins. MXI1, also termed Max interactor 1, or Class C basic helix-loop-helix protein 11 (bHLHc11), is a bHLHZip transcriptional repressor that binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. It thus antagonizes MYC transcriptional activity by competing for MAX. It plays an important role in the regulation of cell proliferation
NRSTHNELEKNRRAHLRLCLERLKVLIPLGPDCTRHTTLGLLNKAKAHIKKLEEADRKSQHQLENLEREQ
RFLKRRLEQL
>gnl|CDD|381501 cd18931, bHLHzip_Mad1, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max-associated protein 1 (Mad1) and similar proteins. Mad1, also termed Max dimerization protein 1 (MXD1), or Max dimerizer 1, or protein MAD, is a bHLHZip transcriptional repressor that binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. It thus antagonizes MYC transcriptional activity by competing for MAX
SRSTHNEMEKNRRAHLRLCLEKLKMLVPLGPESNRHTTLSLLMKAKLHIKKLEDSDRKAVHQIDQLQREQ
RHLKRQLEKL
>gnl|CDD|381502 cd18932, bHLHzip_Mad3, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 3 (Mad3) and similar proteins. Mad3, also termed Max dimerization protein 3, or Max dimerizer 3 (MXD3), or Class C basic helix-loop-helix protein 13 (bHLHc13), or Max-interacting transcriptional repressor MAD3, or Myx, is a bHLHZip Max-interacting transcriptional repressor that plays an important role in cellular proliferation. It suppresses c-myc dependent transformation and is expressed during neural and epidermal differentiation
GAPDSGRSVHNELEKHRRAQLRRCLEQLKQQVPLGADCSRYTTLSLLRRARLHIQKLEEQEQRAQQLKER
LRWEQQKLRRRLESL
>gnl|CDD|381503 cd18933, bHLH-O_HES3, basic helix-loop-helix-orange (bHLH-O) domain found in transcription factor HES-3 and similar proteins. HES-3, also termed Class B basic helix-loop-helix protein 43 (bHLHb43), or hairy and enhancer of split 3, is a bHLH-O transcription factor expressed in neural stem and progenitor cells that is involved in tissue regeneration. It regulates gene expression, cell growth, and insulin release. HES-3 is one mammalian counterpart of the Hairy and Enhancer of split proteins that play a critical role in many physiological processes including cellular differentiation, cell cycle arrest, apoptosis and self-renewal ability
MEKKRRARINVSLEQLKSLLEKHYSNNIRKRKLEKADILELTVKYLRSLQNSIQG
>gnl|CDD|381504 cd18934, bHLH_TS_MRF4_Myf6, basic helix-loop-helix (bHLH) domain found in muscle-specific regulatory factor 4 (MRF4) and similar proteins. MRF4, also termed Class C basic helix-loop-helix protein 4 (bHLHc4), or myogenic factor 6 (Myf-6), is a bHLH transcription factor associated with myogenesis. It plays a role in skeletal muscle differentiation
DRRKAATLRERRRLKKINEAFEALKRRTVPNPNQRLPKVEILRSAINYIEKLQDLLHSLDQQEK
>gnl|CDD|381505 cd18935, bHLH_TS_MYOG_Myf4, basic helix-loop-helix (bHLH) domain found in myogenin (MYOG) and similar proteins. MYOG, also termed Class C basic helix-loop-helix protein 3 (bHLHc3), or myogenic factor 4 (Myf-4), is a bHLH transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation, cell cycle exit and muscle atrophy
DRRRAATLREKRRLKKVNEAFEALKRSTLLNPNQRLPKVEILRSAIQYIERLQALLSSL
>gnl|CDD|381506 cd18936, bHLH_TS_MYOD1_Myf3, basic helix-loop-helix (bHLH) domain found in myoblast determination protein 1 (MYOD1) and similar proteins. MYOD1, also termed Class C basic helix-loop-helix protein 1 (bHLHc1), or myogenic factor 3 (Myf-3), is a bHLH transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Together with Myf-5 and MYOG, MYOD1 co-occupies muscle-specific gene promoter core region during myogenesis
TTNADRRKAATMRERRRLSKVNEAFETLKRCTSTNPNQRLPKVEILRNAIRYIESLQALLR
>gnl|CDD|381507 cd18937, bHLH_TS_Myf5, basic helix-loop-helix (bHLH) domain found in myogenic factor 5 (Myf-5) and similar proteins. Myf-5, also termed Class C basic helix-loop-helix protein 2 (bHLHc2), is a nuclear bHLH transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle specification and differentiation. It also acts as an RNA-binding protein which enhances Ccnd1/Cyclin D1 mRNA translation during myogenesis
DRRKAATMRERRRLKKVNQAFETLKRCTTSNPNQRLPKVEILRNAIRYIESLQDLLREQVENYY
>gnl|CDD|381508 cd18938, bHLH_TS_Mesp, basic helix-loop-helix (bHLH) domain found in the mesoderm posterior protein (Mesp) family. Mesp, a bHLH tissue specific transcription factor, acts as a key regulator of the cardiovascular transcriptional network by inducing directly and/or indirectly the expression of the majority of key cardiovascular transcription factors. The Mesp family includes two bHLH transcription factors, Mesp1 and Mesp2. Mesp1, also termed Class C basic helix-loop-helix protein 5 (bHLHc5), promotes cardiovascular differentiation during embryonic development and embryonic stem cell differentiation. Mesp2, also termed Class C basic helix-loop-helix protein 6 (bHLHc6), plays an important role in somitogenesis
QRQSASEREKLRMRDLAKALHNLRRYLPPSVAPAGQSLTKIETLRLTIRYISHLSAQLGLSEESL
>gnl|CDD|381509 cd18939, bHLH_TS_Msgn1, basic helix-loop-helix (bHLH) domain found in mesogenin-1 (Msgn1) and similar proteins. Msgn1, also termed paraxial mesoderm-specific mesogenin1, or pMesogenin1 (pMsgn1), is a bHLH transcription factor required for maturation and segmentation of paraxial mesoderm. It may regulate the expression of T-box transcription factors essential for mesoderm formation and differentiation
KVKMSAQRRRKASEREKLRMRTLAEALHTLRNYLPPVYSQRGQPLTKIQTLKCTIQYISELSGLLN
>gnl|CDD|381510 cd18940, bHLH_TS_OLIG2, basic helix-loop-helix (bHLH) domain found in oligodendrocyte transcription factor 2 (Oligo2) and similar proteins. Oligo2, also termed Class B basic helix-loop-helix protein 1 (bHLHb1), or Class E basic helix-loop-helix protein 19 (bHLHe19), or protein kinase C-binding protein 2, or protein kinase C-binding protein RACK17, is a bHLH transcription factor that is required for oligodendrocyte and motor neuron specification in the spinal cord, as well as for the development of somatic motor neurons in the hindbrain. It cooperates with OLIG1 to establish the MN progenitors (pMN) domain of the embryonic neural tube
KKDKKQMSEPELQQLRLKINSRERKRMHDLNIAMDGLREVMPYAHGPSVRKLSKIATLLLARNYILMLTN
SLEEMKRLVSEIYGG
>gnl|CDD|381511 cd18941, bHLH_TS_OLIG3, basic helix-loop-helix (bHLH) domain found in oligodendrocyte transcription factor 3 (Oligo3) and similar proteins. Oligo3, also termed Class B basic helix-loop-helix protein 7 (bHLHb7), or Class E basic helix-loop-helix protein 20 (bHLHe20), is a bHLH transcription factor that is expressed in the ventricular zone of the dorsal alar plate of the hindbrain and involved in regulating the development of dorsal and ventral spinal cord. It may determine the distinct specification program of class A neurons in the dorsal part of the spinal cord and suppress specification of class B neurons
KYKIKKQLSEQDLQQLRLKINGRERKRMHDLNLAMDGLREVMPYAHGPSVRKLSKIATLLLARNYILMLT
SSLEEMKRLVG
>gnl|CDD|381512 cd18942, bHLH_TS_OLIG1, basic helix-loop-helix (bHLH) domain found in oligodendrocyte transcription factor 1 (Oligo1) and similar proteins. Oligo1, also termed Class B basic helix-loop-helix protein 6 (bHLHb6), or Class E basic helix-loop-helix protein 21 (bHLHe21), is a bHLH transcription factor that promotes formation and maturation of oligodendrocytes, especially within the brain
EEQQQLRRKINSRERKRMQDLNLAMDALREVILPYSAAHCQSSPGRKLSKIATLLLARNYILLLGSSLQE
LRRLL
>gnl|CDD|381513 cd18943, bHLH_E-protein_E47-like, basic helix-loop-helix (bHLH) domain found in transcription factor E47 and similar proteins. E47 is a class I bHLH transcriptional regulator that forms heterodimers with class II bHLH proteins to regulate distinct differentiation pathways. Its homodimers regulate B lymphocytes development
EEKDLRDRERRMANNARERVRVRDINEAFKELGRMCQMHLKSDKAQTKLIILQQAVQVILGLEQQVRERN
LNPK
>gnl|CDD|381514 cd18944, bHLH_E-protein_E2A_TCF3, basic helix-loop-helix (bHLH) domain found in transcription factor E2-alpha (E2A) and similar proteins. E2A, also termed Class B basic helix-loop-helix protein 21 (bHLHb21), or immunoglobulin enhancer-binding factor E12/E47, or immunoglobulin transcription factor 1, or Kappa-E2-binding factor, or transcription factor 3 (TCF-3), or transcription factor ITF-1, is a bHLH transcriptional regulator involved in the initiation of neuronal differentiation
ERRVANNARERLRVRDINEAFKELGRMCQLHLNSEKPQTKLLILHQAVSVILNLEQQVRERNLNPKAACL
KRRE
>gnl|CDD|381515 cd18945, bHLH_E-protein_TCF4_E2-2, basic helix-loop-helix (bHLH) domain found in transcription factor 4 (TCF-4) and similar proteins. TCF-4, also termed E2-2, or Class B basic helix-loop-helix protein 19 (bHLHb19), or immunoglobulin transcription factor 2 (ITF-2), or SL3-3 enhancer factor 2 (SEF-2), is a bHLH transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. It is involved in the initiation of neuronal differentiation
KAEREKERRMANNARERLRVRDINEAFKELGRMVQLHLKSDKPQTKLLILHQAVAVILSLEQQVRERNLN
PKAACLKRREEEKVS
>gnl|CDD|381516 cd18946, bHLH_E-protein_TCF12_HEB, basic helix-loop-helix (bHLH) domain found in transcription factor 12 (TCF-12) and similar proteins. TCF-12, also termed HEB, or Class B basic helix-loop-helix protein 20 (bHLHb20), or DNA-binding protein HTF4, or E-box-binding protein, or transcription factor HTF-4, is a bHLH transcription factor that is involved in the initiation of neuronal differentiation
RRMANNARERLRVRDINEAFKELGRMCQLHLKSEKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLK
RREEEKVSAVSAE
>gnl|CDD|381517 cd18947, bHLH-PAS_ARNT, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator (ARNT) and similar proteins. ARNT, also termed Class E basic helix-loop-helix protein 2 (bHLHe2), or Dioxin receptor, nuclear translocator, or hypoxia-inducible factor 1-beta (HIF1b), or HIF-1-beta, or HIF1-beta, is a member of bHLH-PAS transcription regulators that acts as the heterodimeric partner for bHLH-PAS proteins such as aryl hydrocarbon receptor (AhR), hypoxia-inducible factor (HIF), and single-minded (SIM). These bHLH-PAS transcription complexes are involved in transcriptional responses to xenobiotic, hypoxia, and developmental pathways. Heterodimerization of bHLH-PAS proteins with ARNT is mediated by contacts between both the bHLH and the tandem PAS domains. ARNT use bHLH and/or PAS domains to interact with several transcriptional coactivators. It is required for activity of the aryl hydrocarbon (dioxin) receptor
KERFARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTST
>gnl|CDD|381518 cd18948, bHLH-PAS_NCoA1_SRC1, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in nuclear receptor coactivator 1 (NCoA-1) and similar proteins. NCoA-1, also termed Class E basic helix-loop-helix protein 74 (bHLHe74), or protein Hin-2, or RIP160, or renal carcinoma antigen NY-REN-52, or steroid receptor coactivator 1 (SRC-1), is a bHLH-PAS nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion
TAQSTEKRRREQENKYLEELAELLSANIGDIDSLSVKPDKCKILKKTVDQIQQMKRLEQEK
>gnl|CDD|381519 cd18949, bHLH-PAS_NCoA3_SRC3, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in nuclear receptor coactivator 3 (NCoA-3) and similar proteins. NCoA-3, also termed ACTR, or amplified in breast cancer 1 protein (AIB-1), or CBP-interacting protein (pCIP), or Class E basic helix-loop-helix protein 42 (bHLHe42), or receptor-associated coactivator 3 (RAC-3), or steroid receptor coactivator protein 3 (SRC-3), or thyroid hormone receptor activator molecule 1 (TRAM-1), is a bHLH-PAS steroid/nuclear receptor-associated coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. It also plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin
LNCSGEKRRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKSSSNDDDVQKA
DVS
>gnl|CDD|381520 cd18950, bHLH-PAS_NCoA2_SRC2, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in nuclear receptor coactivator 2 (NCoA-2) and similar proteins. NCoA-2, also termed Class E basic helix-loop-helix protein 75 (bHLHe75), or transcriptional intermediary factor 2 (TIF2), or steroid receptor coactivator 2 (SRC-2), or glucocorticoid receptor interacting protein-1 (GRIP1), is a bHLH-PAS transcriptional coactivator for steroid receptors and nuclear receptors. It is required with NCoA-1 to control energy balance between white and brown adipose tissues
PSPKRSTEKRNREQENKYIEELAELIFANFNDIDNFNVKPDKCAILKETVKQIRQIKEQEKAAA
>gnl|CDD|381521 cd18951, bHLH_TS_scleraxis, basic helix-loop-helix (bHLH) domain found in scleraxis and similar proteins. Scleraxis, also termed SCX, or Class A basic helix-loop-helix protein 41 (bHLHa41), or Class A basic helix-loop-helix protein 48 (bHLHa48), is a bHLH transcription factor that is expressed in sclerotome limb bud cranial and body wall mesenchyme, pericardium and heart valves, ligaments and tendons. It is required for tendon formation ligaments, connective tissue, the diaphragm, and testis development. Scleraxis plays a central role in promoting fibroblast proliferation and matrix synthesis during the embryonic development of tendons
EPRQRHTANARERDRTNSVNTAFTALRTLIPTEPADRKLSKIETLRLASSYISHLGNVLLVGEACGDG
>gnl|CDD|381522 cd18952, bHLH_TS_HAND1, basic helix-loop-helix (bHLH) domain found in heart- and neural crest derivatives-expressed protein 1 (HAND1) and similar proteins. HAND1, also termed Class A basic helix-loop-helix protein 27 (bHLHa27), or extraembryonic tissues, heart, autonomic nervous system and neural crest derivatives-expressed protein 1 (eHAND), is a bHLH transcription factor that plays an essential role in both trophoblast-giant cells differentiation and in cardiac morphogenesis
RRKGAGPKKERRRTESINSAFAELRECIPNVPADTKLSKIKTLRLATSYIAYLMDVLAKD
>gnl|CDD|381523 cd18953, bHLH_TS_bHLHe23_bHLHb4, basic helix-loop-helix (bHLH) domain found in Class E basic helix-loop-helix protein 23 (bHLHe23) and similar proteins. bHLHe23, also termed Class B basic helix-loop-helix protein 4 (bHLHb4), is an OLIG-related bHLH transcription factor that is expressed in rod bipolar cells and is required for rod bipolar cell maturation. bHLHe23 have roles in spinal interneuron differentiation by mechanisms linked to the Notch signaling pathway. It modulates the expression of genes required for the differentiation and/or maintenance of pancreatic and neuronal cell types
PKEQRSLRLSINARERRRMHDLNDALDGLRSVIPYAHSPSVRKLSKIATLLLAKNYILMQAQALEEMRRL
VAYLNQGQTLS
>gnl|CDD|381524 cd18954, bHLH_TS_bHLHe22_bHLHb5, basic helix-loop-helix (bHLH) domain found in Class E basic helix-loop-helix protein 22 (bHLHe22) and similar proteins. bHLHe22, also termed Class B basic helix-loop-helix protein 5 (bHLHb5), or trinucleotide repeat-containing gene 20 protein, is an OLIG-related bHLH neural-specific transcriptional repressor that is expressed in both excitatory (unipolar brush cells) and inhibitory neurons (cartwheel cells) of the dorsal cochlear nucleus (DCN) during development. It is important for the proper development and/or survival of a number of neural cell types
VRLNINARERRRMHDLNDALDELRAVIPYAHSPSVRKLSKIATLLLAKNYILMQANALEEMRRLVAYLNQ
>gnl|CDD|349736 cd18955, BTB_POZ_BACH, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB and CNC homolog (BACH) proteins. This subfamily includes BACH1 (also called BTB-basic leucine zipper transcription factor 1), BACH2 (also called BTB-basic leucine zipper transcription factor 2), and similar proteins. They belong to the cap 'n' collar (CNC) and basic leucine zipper (bZIP) factor family. BACH1 is a heme-responsive transcriptional repressor of heme oxygenase (HO)-1. It represses genes involved in heme metabolism and oxidative stress response. BACH2 is a lymphoid-specific transcription factor with a prominent role in B-cell development. It is transcriptionally regulated by the BCR/ABL oncogene. It represses the anti-apoptotic factor heme oxygenase-1 (HO-1). Subfamily members contain a BTB domain and a basic leucine zipper (bZIP) domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids
LCDVTIVVEDQRFRAHRAVLAACSDYFLSRVVGQTDGDLVITLPEEVTVKGFEPLLQFAYTAKLLLSKEN
VLEVCRCAEFLGVHNIEKACFDFL
>gnl|CDD|349737 cd18956, BTB_POZ_ZBTB42, BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 42 (ZBTB42). ZBTB42 is a transcriptional repressor that specifically binds DNA and probably acts by recruiting chromatin remodeling multiprotein complexes. It is enriched in skeletal muscles, especially at the neuromuscular junction. A ZBTB42 mutation has been identified to define a novel lethal congenital contracture syndrome (LCCS6), a lethal autosomal recessive form of arthrogryposis multiplex congenita (AMC). ZBTB42 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids
MEFPEHGGRLLGRLRQQRELGFLCDCTVLVGDARFPAHRAVLAACSVYFHLFYRDRPAGGRDTVRLNGDI
VTAPAFGRLLDFMYEGRLDLRSLPVEDVLAAASYLHMYDIVKVCKGRLREKDPALPRGA
>gnl|CDD|349316 cd18960, CD_HP1_like, chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; uncharacterized subgroup. CHRomatin Organization Modifier (chromo) domain of mammalian HP1alpha (Cbx5), HP1beta (Cbx1), HP1gamma (Cbx5), and similar proteins. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3)
VFVVERILDKRLGRNGGEEFLIKWQGFPESDSSWEPRENLQCDEMLEEFEK
>gnl|CDD|349317 cd18961, CD_CEC-4_like, chromodomain of Caenorhabditis elegans chromodomain protein 4, and similar proteins. CHRomatin Organization Modifier (chromo) domain of Caenorhabditis elegans CEC-4, and similar proteins. CEC-4 is a perinuclear heterochromatin anchor, it mediates the anchoring of H3K9 methylation-bearing chromatin at the nuclear periphery in early to mid-stage embryos. It is necessary for anchoring, but does not affect transcriptional repression. CEC-4 contributes to the efficiency with which muscle differentiation is induced following ectopic expression of the master regulator, HLH-1 (MyoD in mammals). A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
YEVEKILSHRIVNGKPLYLVMWVGYPGPVENSEMWEEDLKNCGELLKAYKD
>gnl|CDD|349318 cd18962, CD_MT_like, chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins. This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Coemansia reversa NRRL 1564 SET (Su(var)3-9, enhancer-of-zeste, trithorax) domain-containing protein, and similar proteins. The SU(VAR)3-9 protein is the main chromocenter-specific histone H3-K9 methyltransferase (HMTase) in Drosophila where it plays a role in heterochromatic gene silencing. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
EGHYVVEAIVNDVLIDGKHMYEVKWEGYPSDHNNWVAEWDLNDKEILRKYNK
>gnl|CDD|349319 cd18963, chromodomain, CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain
ERVFAAECIIKRRVRKGRIEYLVKWKGWASKERERELYGPKKRGPKPKKFLLKARAQ
>gnl|CDD|349320 cd18964, chromodomain, CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain
FFVERIIGRRPSARDGPGKFLWLVKWDGYPIEDATWEPPENLGEHAKLIEDFEK
>gnl|CDD|349321 cd18965, chromodomain, CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain
YIIEALLKKRQFNRKLEYLVKWHGLPESENTWEREKDIKHVSHWKQLLKDLRA
>gnl|CDD|349322 cd18966, chromodomain, CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain
YEVERILAERRDDGGKRYLVKWEGYPLEEATWEPEENIGDEELLKEWEE
>gnl|CDD|349323 cd18967, chromodomain, CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain
WEIEAILAHHMSDPRTHPGKPATMLYLTKWEGFPDETWEPAESFDDRKILHDYRR
>gnl|CDD|349324 cd18968, chromodomain, CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain
EYEVEVILAARVVKDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDDLLERFWE
>gnl|CDD|349325 cd18969, chromodomain, CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members of this subgroup, the chromodomain is followed by a chromo shadow domain. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. For the majority of members of this subgroup, the chromodomain is followed by a chromo shadow domain (CSD)
EEEYEIEEILDVKKGGFEDGKLAYFVKWKGYPSSENSWVTEEDAANAQEMIEEYWK
>gnl|CDD|349326 cd18970, CD_POL_like, chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins. This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Hypsizygus marmoreus TY3B-I_0 protein, a putative TY3/gypsy retrotransposon polyprotein, and similar proteins. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
FFVERILDERRRGRGWQYLVRWLGYGPSDDSWLPRRELEECEALDDWLR
>gnl|CDD|349327 cd18971, CD_POL_like, chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar proteins. This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Magnaporthe grisea putative retrotransposon polyprotein which includes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
YEVEEILAARRRRIRGKGREVLVKWVGYAEPTWEPLDNLADTAALDRFEA
>gnl|CDD|349328 cd18972, CD_POL_like, chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and similar proteins. This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Moniliophthora perniciosa FA553 putative retrotelement polyprotein, which includes domains in the following order: a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related "chromo shadow" domain
YEVEAIVGHKPKKKPRQFLVSWLGYDSSHNEWKQKEELENARELLQDYLK
>gnl|CDD|349329 cd18973, CD_Tf2-1_POL_like, chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type 1, and similar proteins. This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type 1 (Tf2-1), and similar proteins. It belongs to the Ty3/gypsy family of long terminal repeat (LTR) retrotransposons. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
YVVEAILDNKRRKGKWLYLVKWKGYGPEHNTWEPRENLEHAQKLLKKYYQ
>gnl|CDD|349330 cd18974, CD_POL_like, chromodomain of Penicillium solitum protein PENSOL_c198G03123. This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Penicillium solitum protein PENSOL_c198G03123 a putative polyprotein from a Ty3/Gypsy long terminal repeat (LTR) retroelement. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
WEVEEIVDEKMIDDELHYLVKWKGWPAEYNQWEPEDDMENAPKAIQSYEK
>gnl|CDD|349331 cd18975, CD_MarY1_POL_like, chromodomain of Tricholoma matsutake polyprotein, and similar proteins. This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in the polyprotein from the MarY1 Ty3/Gypsy long terminal repeat (LTR) retroelement from the from the Ectomycorrhizal Basidiomycete Tricholoma matsutake. The pol gene in TY3/gypsy elements generally encodes domains in the following order: prt-reverse transcriptase-RNase H-integrase, in marY1 POL the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
YEVESILNSRLHRGKLQYLIQWKGYPLEEASWELEDNIKNPRLIEEFHK
>gnl|CDD|349332 cd18976, CD_POL_like, chromodomain of uncharacterized putative retroelement polyprotein proteins. This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in uncharacterized putative retrotransposon proteins, and similar proteins. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
YIVESLLDRRKVRGQVQYLVKWRGFPRSEATWEPREELMRRCAELVAAYDA
>gnl|CDD|349333 cd18977, CD_POL_like, chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins. This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Rhizoctonia solani AG-3 Rhs1AP, a putative Ty3/Gypsy polyprotein/retrotransposon which includes a protease, a reverse transcriptase, a ribonuclease H, and an integrase domain, in that order, with a chromodomain at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
LPEYEVEKIVGEKWKKRKNRRVKLYKVRFKGYGPEEDEWLTKEELKNAPEILAEWKL
>gnl|CDD|349334 cd18978, CD_DDE_transposase_like, chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins. This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Rhizopus microsporus putative DDE transposases, and similar proteins. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
DESYEVEKIINHRGEKNRRKYLVKWKGYDDTDNSWVTQEDFNDKDMIDEYEN
>gnl|CDD|349335 cd18979, CD_POL_like, chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins (Z195D10.9), and similar proteins. This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Zea maize Z195D10.9 protein, and other putative TY3/gypsy retrotransposon polyproteins. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
LFPEKVLDIRQRDKGNKEFLVQWQGLSVEEATWEPYKDLVQQFPDFKL
>gnl|CDD|349336 cd18980, CD_NC-like, chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and similar proteins. This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Trichosporon asahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and similar proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain
QPEYEVEAILDHKVDRRYRDPNFYLVRWRGYGPSHDSWEPTSALENAQDLLREFWE
>gnl|CDD|349337 cd18981, CSD_HP1e_insect, chromo shadow domain of insect heterochromatin protein 1E. The chromo shadow domain (CSD) is always found in association with a related N-terminal chromo (CHRromatin Organization MOdifier) domain. CSD domains have only been found in proteins that also possess a chromodomain, while chromodomains can exist in isolation. CSDs are found for example in Drosophila and human heterochromatin protein (HP1) and mammalian modifier 1 and modifier 2. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. The HP1 CSD, in addition to interacting with various proteins bearing the PXVXL motif, also interacts with a region of histone H3 that bears the similar PXXVXL motif. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3). The CSD domains of all three human HP1 homologs have similar affinities to the PXXVXL motif of histone H3
GFTAQEILKGINNNGEISFLIRFKHLDQPQVVPSDMAYVEIPQMVLKFYENHC
>gnl|CDD|349338 cd18982, CSD, chromo shadow domain; uncharacterized subgroup. The chromo shadow domain (CSD) is always found in association with a related N-terminal chromo (CHRromatin Organization MOdifier) domain. CSD domains have only been found in proteins that also possess a chromodomain, while chromodomains can exist in isolation. CSDs are found for example in Drosophila and human heterochromatin protein (HP1) and mammalian modifier 1 and modifier 2. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. The HP1 CSD, in addition to interacting with various proteins bearing the PXVXL motif, also interacts with a region of histone H3 that bears the similar PXXVXL motif. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3). The CSD domains of all three human HP1 homologs have similar affinities to the PXXVXL motif of histone H3
SYKASVSNDVQDVSVTFLALRSDGKEVLVDNKFLKANNPLLLINFYEQHL
>gnl|CDD|350846 cd18983, CBD_MSL3_like, chromo barrel domain of human male-specific lethal complex subunit 3, and similar proteins. This subgroup includes human male-specific lethal (MSL) complex subunit 3 (MSL3, also known as MSL3L1). The MSL3 chromodomain specifically recognizes the H4K20 monomethyl mark, in a DNA-dependent manner, and may be involved in chromosomal targeting of the MSL complex. Also included is MORF-related gene on chromosome 15 (MRG15, also known as MORF4L1) which specifically binds to Lys36-methylated histone H3 and plays a role in transcriptional regulation and in DNA repair. This subgroup also includes Arabidopsis thaliana Morf Related Gene 2 (MRG2) which acts as a H3K4me3/H3K36me3 reader involved in the regulation of Arabidopsis flowering. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain
ERVLCFHGPLLYEAKILDVIPDKKEWKYFIHYNGWNKSWDEWVPEDRVLKYTDENLR
>gnl|CDD|350847 cd18984, CBD_MOF_like, chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar proteins. This subgroup includes the chromo barrel domain of Drosophila melanogaster males-absent on the first (MOF) protein. The histone H4 lysine 16 (H4K16)-specific acetyltransferase MOF is part of two distinct complexes involved in X chromosome dosage compensation and autosomal transcription regulation. Its chromobarrel domain is essential for H4K16 acetylation throughout the Drosophila genome and controls spreading of the male-specific lethal (MSL) complex on the X chromosome. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. The MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites
GSTYYCRRSDDTVHRAEVIQSRTTKQAGREEYYVHYVGLNRRLDEWVDKSRLSLNDLGKIVKTPAPPNAE
>gnl|CDD|350848 cd18985, CBD_TIP60_like, chromo barrel domain of human tat-interactive protein 60, and similar proteins. Tat-interactive protein 60 (also known as KAT5 or HTATIP) catalyzes the acetylation of lysine side chains in various histone and nonhistone proteins, and in itself. It plays roles in multiple cellular processes including remodeling, transcription, DNA double-strand break repair, apoptosis, embryonic stem cell identity, and embryonic development. The TIP60 chromo barrel domain recognizes trimethylated lysine at site 9 of histone H3 (H3K9me3) which triggers TIP60 to acetylate and activate ataxia telangiectasia-mutated kinase, thereby promoting the DSB repair pathway. In a different study, the TIP60 chromo barrel domain was shown to bind H3K4me1, which stabilizes TIP60 recruitment to a subset of estrogen receptor alpha target genes, facilitating regulation of the associated gene transcription. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. This subgroup belongs to the MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites
CRLRVRMHKTDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKT
>gnl|CDD|350849 cd18986, CBD_ESA1_like, chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, and similar proteins. The subgroup includes the chromo barrel domain of NuA4 histone acetyltransferase (HAT) complex catalytic subunit Esa1 (also known as Tas1 and Kat5). Yeast Esa1p acetylates specific histones nonrandomly in H4, H3, and H2A. Esa1 also plays roles in cell cycle progression. In addition, its chromo barrel domain plays a role in the yeast Piccolo NuA4 complex's ability to distinguish between histones and nucleosomes; however, the chromodomain is not required for the Piccolo to bind to nucleosomes. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. This subgroup belongs to the MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites
IGCKCWVQKDGEERLAEILSINTRKAPPKFYVHYEDFNKRLDEWITADRINLSKEVLYPKPKATE
>gnl|CDD|349788 cd18987, LGIC_ECD_anion, extracellular domain (ECD) of anionic Cys-loop neurotransmitter-gated ion channels. This family contains the extracellular domain (ECD) of anionic Cys-loop neurotransmitter-gated ion channels which include type-A gamma-aminobutyric acid receptor (GABAAR), glycine receptor (GlyR), invertebrate glutamate-gated chloride channel (GluCl), and histimine-gated chloride channel (HisCl). These neurotransmitter receptors directly mediate chloride permeability and constitute one half of the Cys-loop receptor family. Receptors in this family are composed of five either identical or homologous subunits, which generate diversity in functional profiles and pharmacological preferences. GABAAR and GlyR, both mediate fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR receptor pore, resulting in hyperpolarization of the neuron. GluCl channels are found only in protostomia, but are closely related to mammalian glycine receptors (GlyRs). They have several roles in these invertebrates, including controlling locomotion and feeding, and mediating sensory inputs into behavior. Ligand-gated chloride channels are critical not only for maintaining appropriate neuronal activity, but have long been important therapeutic targets: benzodiazepines, barbiturates, some intravenous and volatile anaesthetics, alcohol, strychnine, picrotoxin, and ivermectin all derive their biological activity from acting on this inhibitory half of the Cys-loop receptor family. Many of the therapeutically useful compounds acting at Cys-loop receptors target an allosteric site. The sites in Cys-loop receptors at which these allosteric ligands bind and their structure-based mechanisms of action are largely unresolved
TNVKVSIYIESISSIDEQTMDFTVDMYLRQRWTDPRLAYPDRNGTDPILLPSDKFDKIWLPDLYFRNEKS
SSFHDVTTPNVLVRIFPNGTVLYSQRLTLTLSCPMNLQKFPFDTQVCTLRLESYGYTTDQVVLHWDDDPP
IVVNESSLLLPEFSLVKITTSDCTGNYSTTGNYSCLEATFKLKRE
>gnl|CDD|349789 cd18988, LGIC_ECD_bact, extracellular domain of prokaryotic pentameric ligand-gated ion channels (pLGIC). This family contains extracellular domain (ECD) of bacterial pentameric ligand-gated ion channels (pLGICs), including ones from Gloebacter violaceus (GLIC) and Erwinia chrysanthemi (ELIC). These prokaryotic homologs of Cys-loop receptors have been useful in understanding their eukaryotic counterparts. The largely beta-sheet ECD in this family is similar to other pLGICs, but lacks the cysteine loop and an intracellular domain. While most pLGICs undergo desensitization on prolonged exposure to the agonist, GLIC is activated by protons, but does not desensitize, even at proton concentrations eliciting maximal electrophysiological response (pH 4.5). Studies show that GLIC activation is inhibited by most general anaesthetics at clinical concentrations, including xenon which has been used in clinical practice as a potent gaseous anesthetic for decades. Xenon binding sites have been identified in three distinct regions of the TMD: in a large intra-subunit cavity, in the pore, and at the interface between adjacent subunits
PTEVSVGIYLIDIYGIDEVNETFEADGYLRLRWQDPRLAFDPAAGKEYRLGEAEKQLDEIWNPQIEFINQ
RGLRDTLNRRLRVFPDGTVTYRQRFTGTFSTPMDLRRFPFDRQTLTIELESFSYDPDEVVLVVDQDDTGL
SDDLSLPEWSIGDVSAEVSSYKGSNGGEEFSRFTFEIDVKRK
>gnl|CDD|349790 cd18989, LGIC_ECD_cation, extracellular domain (LBD) of cationic Cys-loop neurotransmitter-gated ion channels. This superfamily contains the extracellular domain (ECD) of cationic Cys-loop neurotransmitter-gated ion channels, which include nicotinic acetylcholine receptor (nAChR), serotonin 5-hydroxytryptamine receptor (5-HT3), and zinc-activated ligand-gated ion channel (ZAC) receptor. These ligand-gated ion channels (LGICs) are found across metazoans and have close homologs in bacteria. They are vital for communication throughout the nervous system. nAChR is a non-selective cation channel that is permeable to Na+ and K+, and some subunit combinations are also permeable to Ca2+. Na+ enters and K+ exits to allow net flow of positively charged ions inward. 5-HT3, a cation-selective channel, binds serotonin and is permeable to Na+, K+, and Ca2+. It mediates neuronal depolarization and excitation within the central and peripheral nervous systems. ZAC forms an ion channel gated by Zn2+, Cu2+, and H+ and is non-selectively permeable to monovalent cations. However, the role of ZAC in Zn2+, Cu2+, and H+ signaling require is as yet unknown
VNVNVSFSLYSILDLDEVEQTLTLSGWLTLTWTDERLTWNPSDYGGITSIVVPSSEIWTPDIVLYNSVDS
LDLLGDSNTLVRVSSDGTVTWVPPGVLTTSCDIDVTYFPFDTQTCSLRFGSWSYTTDEINLTPSSNGVDL
EDYEENGEWELLSTSVSREEDKYCNETYSELTFTITLKRR
>gnl|CDD|349791 cd18990, LGIC_ECD_GABAAR, gamma-aminobutyric acid receptor extracellular domain. This family contains extracellular domain (ECD) of type-A gamma-aminobutyric acid receptor (GABAAR), a member of the pentameric "Cys-loop" superfamily of transmitter-gated ion channels. This family includes 19 isoforms in human; six alpha, 3 beta, 3 gamma, one of delta, epsilon, pi, and theta, known to form heteropentameric GABAARs, and 3 rho subunits that only form homopentameric channels (also known as GABAA rho or GABAC receptor) or pseudoheteromeric if consisting of different rho subunits. The majority of GABAA receptor pentamers contain two alpha subunits, two beta subunits, and a gamma subunit, with different isoforms affecting potency of the neurotransmitter. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to its site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. Benzodiazepine and barbiturates each bind to their own distinct sites on the ECD. The channels have to contain the gamma subunit and alpha subunits in order to respond to benzodiazepines. Specific combinations of alpha, beta, and gamma subunits exhibit ethanol sensitivity. All these major classes of drugs favor channel-opening. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy
VVVTVEIWVQSIGSISEINMDFTLDIYFRQYWRDPRLAFDHNGCNKNLTLSGEMLSKIWTPDTFFVNSKK
AKFHDVTTPNILLRIYPNGTVLYSYRLTVTAPCSMDLRKFPMDTQTCSLVFESYGYTTDDVVYKWKEGDT
PVTILEKIELPQFDLTGVTTSEKTEVYPAGNYSRLTVTFTFKRR
>gnl|CDD|349792 cd18991, LGIC_ECD_GlyR, extracellular domain of glycine receptor (GlyR). This subfamily contains extracellular domain of glycine receptor (GlyR or GLR) of the amino acid neurotransmitter glycine. GlyR has four known isoforms of the alpha-subunit (alpha1-4, encoded by GLRA1, GLRA2, GLRA3, GLRA4) that are essential to bind ligands and a single beta-subunit (encoded by GLRB), all of which have been described to have a regionally and temporally controlled expression during development and maturation of the central nervous system (CNS). Functional chloride-permeable GlyR ion channels are formed by 5 alpha subunit homopentamers or by alpha and beta subunit heteropentamers, which form complexes with either a 2alpha-3beta or 3alpha-2beta stoichiometry. The receptor can be activated by glycine as well as beta-alanine and taurine, and can be selectively blocked by the high-affinity competitive antagonist strychnine. Caffeine is also a competitive antagonist of GlyR. In human, glycine receptor alpha1 and beta subunits are the major targets of mutations that cause disruption of GlyR surface expression or reduced ability of expressed GlyRs to conduct chloride ions, leading to hyperekplexia, a rare neurological disorder characterized by neonatal hypertonia and exaggerated startle responses to unexpected stimuli. Mutations in GlyR alpha2 are known to cause cortical neuronal migration/autism spectrum disorder and in GlyR alpha3 to cause inflammatory pain sensitization/rhythmic breathing
PTNVSVQIYINSIDSINEATMDYSVNIFLRQRWNDPRLNFTKLSNIDYLELDPKMIDKIWVPDLFFPNEK
KANFHDVTVPNKLLRIYPNGTVYYSMRLSLTLSCPMDLHKYPLDTQTCPIQIESFGYTTENLIFKWNDDK
PVQLNDGLELPQFELKGVSTSDCTKTYTETGNFSCLEAKFHLQRN
>gnl|CDD|349793 cd18992, LGIC_ECD_HisCl, extracellular domain of histimine-gated chloride channel (HisCl or HGCC). This family contains extracellular domain (ECD) of histamine-gated chloride channel (HisCl), a member of the Cys-loop receptor superfamily of ligand-gated ion channels and is closely related to the mammalian GABAA receptor and glycine receptor (GlyR). Histamine (HA) is a neurotransmitter that activates GPCRs in vertebrates, but in arthropods, it is a photoreceptor neurotransmitter, directly gating chloride channels on large monopolar cells (LMCs), postsynaptic to photoreceptors in the lamina. It has also been reported to play important roles in mechanosensory reception, temperature preference, and sleep in insects. HA activates its receptor channels to cause an inward chloride flux in the insect nervous system. In Drosophila, HA acts on two histamine-gated chloride channel (HGCC) subunits called HisCl1 (HisClalpha2, HCLB) and HisCl2 (HisClalpha1, Ort, HCLA). HisCl1 (HCLB) and HisCl2 (HCLA) are expressed predominantly in the insect eye, sharing 60% sequence identity, and forming homomeric and heteromeric HGCCs. HCLA homomers are involved in synaptic transmission in the lamina, while HCLB homomers, localized in the glia cells, have a role in shaping the transmission. HCLB channels, but not HCLA channels, are also responsible for the activation and maintenance of wake state in D. melanogaster. In Manduca sexta, HCLB channels in the flight sensory-motor have been shown to be involved in olfactory processing circuit. Studies show that HCLB channels are more sensitive to agonists when compared with HCLA channels, but insensitive to known LGCC insecticides
QPTVVYFHVTVMGLDSIDEESMTYVADIFFAQSWRDHRLRLPENMTSEYRLLDVDWLKNIWRPDSFFKNA
KSVTFHTMTIPNHYLWLYKDKTILYMVKLTLVLSCAMNFEIYPHDTQECKLQIESLSHTTDDLVFQWDPD
VPLVVDENIELPQLQLSNNYTADCTQVYSTGNFTCLEVVFVLKRR
>gnl|CDD|349794 cd18993, LGIC_ECD_GluCl, glutamate-gated chloride channel (GluCl) extracellular domain. This subfamily contains extracellular domain of glutamate-gated chloride channel (GluCl) found only in protostomia, but are closely related to mammalian glycine receptors. They have several roles in these invertebrates, including controlling locomotion and feeding, and mediating sensory inputs into behavior. Comparison of the GluCl gene families between organisms shows that insect gene family is relatively simple, while that found in nematodes tends to be larger and more diverse. Glutamate is an inhibitory neurotransmitter that shapes the responses of projection neurons to olfactory stimuli in the Drosophila. GluCls are targeted by the macrocyclic lactone family of anthelmintics and pesticides in arthropods and nematodes, thus making the GluCls of considerable medical and economic importance. In Drosophila melanogaster, GluCl mediates sensitivity to the antiparasitic agents ivermectin and nodulisporic acid, suggesting that their drug target is the same throughout the Ecdysozoa
PVIVKVNIYVRSISKIDDVKMEYSVQLTFRQEWYDPRLRYDDTGGKPEYLTLTDDSKIWKPDTFFQNEKE
GHFHNIDKPNVYLRIYPDGKVLYSVRISLTLSCPMDLQYYPFDKQTCSIDLASYGYTTDDIVYLWKEEDP
VQLPKGLSLPNFTLTNFKTGYCTSKTNTGEYSCLRVDFILRRE
>gnl|CDD|349795 cd18994, LGIC_ECD_ZAC, extracellular domain of zinc-activated ligand-gated ion channel. This family is the extracellular domain of zinc-activated ligand-gated ion channel (ZAC), a cationic ion channel belonging to the superfamily of Cys-loop receptors, which consists of pentameric ligand-gated ion channels. ZAC displays low sequence similarity to other members in the superfamily, with closest matches to the human serotonin 5-HT3 receptor (5-HT3R) subunits 5-HT3A and 5-HT3B, and nAChR alpha7 subunits that exhibit approximately 15% amino acid sequence identity to ZAC. Expression of ZAC has been detected in human fetal whole brain, spinal cord, pancreas, placenta, prostate, thyroid, trachea, and stomach, as well as in adult hippocampus, striatum, amygdala, and thalamus. ZAC forms an ion channel gated by Zn2+, Cu2+, and H+, and is non-selectively permeable to monovalent cations. However, the role of ZAC in Zn2+, Cu2+, and H+ signaling is as yet unknown
LLVDVTVFVSNVFNVDILEYTMSSRLLLNLSWLDPRLAWNENISPMSAVTLPWDSLWTPGLTIQEALWVT
WRPQSPDARVTRDGHVELYLALTTETNCDFELFHFPRDTSDCPLSFFALSNTVLELEFSNHIVNEIVSVK
REYVVRVLITQVPPFQLVPCFQVTLSLKNT
>gnl|CDD|349796 cd18995, LGIC_AChBP, acetylcholine binding protein (AChBP). This family contains acetylcholine binding protein (AChBP) which is a soluble extracellular domain homolog secreted by protostomia, and has been widely recognized as a surrogate for the ligand binding domain of nicotinic acetylcholine receptors (nAChRs). AChBP forms a pentameric structure where the interfaces between the subunits provide an acetylcholine (ACh) binding pocket homologous to the binding pocket of nAChRs. Thus far, AChBPs have been characterized only in aquatic mollusks, which have shown low sensitivity to neonicotinoids, the insecticides targeting insect nAChRs. Lymnaea stagnalis acetylcholine binding protein (Ls-AChBP) which has been found in glial cells as a water-soluble protein modulating synaptic ACh concentration has its the binding pocket show better resemblance as it contains all the five aromatic residues fully conserved in nAChR. Five AChBP subunits have been characterized in Pardosa pseudoannulata, a predator enemy against rice insect pests, and share higher sequence similarities with nAChR subunits of both insects and mammals compared with mollusk AChBP subunits
VKVSLSLTLQDILSVDEETNEVDLVGWLQMTWKDPRLTWDPAEYGNLKNLRLPSSKIWTPDIAVYNSIGA
PSVLFSPQLVLVSSDGTVLWVPPIRIRFSCDLDNVDPEDGATCRLKIGSWTYSGREIDLNTGTDVDLDSY
YNQSSKWELLSATQKREVKTYSCCPEPYPDIEFVFTFKKR
>gnl|CDD|349797 cd18996, LGIC_ECD_5-HT3, extracellular domain of serotonin 5-HT3 receptor. This family contains extracellular domain of serotonin 5-HT3 receptor which belongs to the Cys-loop superfamily of ligand-gated ion channels (LGICs). This ion channel is cation-selective and mediates neuronal depolarization and excitation within the central and peripheral nervous systems. Like other ligand gated ion channels, the 5-HT3 receptor consists of five subunits arranged around a central ion conducting pore, which is permeable to Na+, K+, and Ca2+ ions. Binding of the neurotransmitter 5-hydroxytryptamine (serotonin) to the 5-HT3 receptor opens the channel, which then leads to an excitatory response in neurons, and the rapidly activating, desensitizing, inward current is predominantly carried by Na+ and K+ ions. This receptor is most closely related by homology to the nicotinic acetylcholine receptor (nAChR). Five subunits have been identified for this family: 5-HT3A, 5-HT3B, 5-HT3C, 5-HT3D, and 5-HT3E, encoded by HTR3A-E genes. Only 5-HT3A subunits are able to form functional homomeric receptors, whereas the 5-HT3B, C, D, and E subunits form heteromeric receptors with 5-HT3A. Different receptor subtypes are important mediators of nausea and vomiting during chemotherapy, pregnancy, and following surgery, while some contribute to neuro-gastroenterologic disorders such irritable bowel syndrome (IBS) and eating disorders as well as co-morbid psychiatric conditions. 5-HT3 receptor antagonists are established treatments for emesis and IBS, and are beneficial in the treatment of psychiatric diseases
NCSYYDVLKALNKTFNSLHLTYTRPVKNWTPPTTVYLDLTLYAILDVDEKLQTLTTYIWLEMVWFNEFLS
WNPEQFCGISKVSVPEDTLWKPDILIYEMTDKDKSPKIPYVYVSNNGTVRNYKPLQVVSTCSLDIYKFPF
DTQNCNLTFSSFLHTVNDIILNPGSNSEEITSESKEIFQTQGEWELLNIKVSDEKLSLLGNSFDQIVYQI
TIKRR
>gnl|CDD|349798 cd18997, LGIC_ECD_nAChR, extracellular domain of nicotinic acetylcholine receptor. This family contains the extracellular domain of nicotinic acetylcholine receptor (nAChR), a member of the pentameric "Cys-loop" superfamily of transmitter-gated ion channels. nAChR is found in high concentrations at the nerve-muscle synapse, where it mediates fast chemical transmission of electrical signals in response to the endogenous neurotransmitter acetylcholine (ACh) released from the nerve terminal into the synaptic cleft. Thus far, seventeen nAChR subunits have been identified, including ten alpha subunits, four beta subunits, and one gamma, delta, and epsilon subunit each, all found on the cell membrane that non-selectively conducts cations (Na+, K+, Ca++). These nAChR subunits combine in several different ways to form functional nAChR subtypes which are broadly categorized as either muscle subtype located at the neuromuscular junction or neuronal subtype that are found on neurons and on other cell types throughout the body. The muscle type of nAChRs are formed by the alpha1, beta1, gamma, delta, and epsilon subunits while the neuronal type are composed of nine alpha subunits and three beta subunits, which combine in various permutations and combinations to form functional receptors. Among various subtypes of neuronal nAChRs, the homomeric alpha7 and the heteromeric alpha4beta2 receptors are the main subtypes widely distributed in the brain and implicated in the pathophysiology of neurodevelopmental disorders such as schizophrenia and autism and neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease. Among subtypes of muscle nAChRs, the heteromeric subunits (alpha1)2, beta, gamma, and delta in fetal muscle, and the gamma subunit replaced by epsilon in adult muscle have been implicated in congenital myasthenic syndromes and multiple pterygium syndromes due to various mutations. This family also includes alpha- and beta-like nAChRs found in protostomia
VNVTFGLTLRQIIDVDEKNQVLTTNVWLRQEWNDERLTWNPSDYGGITSIRVPSDKIWLPDIVLYNNADG
DFDSSYKTNVIVYSDGTVTWLPPAIFKSSCKIDVTYFPFDEQNCTLKFGSWTYDGSELDLQLKSDTVDLS
DYIENGEWDLLGAPAKRNVVKYSCCPEPYPDVTFTIHIRRK
>gnl|CDD|349799 cd18998, LGIC_ECD_GABAAR_A, extracellular domain of gamma-aminobutyric acid receptor subunit alpha. This family contains extracellular domain (ECD) of type-A gamma-aminobutyric acid receptor (GABAAR), a member of the pentameric "Cys-loop" superfamily of transmitter-gated ion channels. This family includes 19 isoforms in human; six alpha, 3 beta, 3 gamma, one of delta, epsilon, pi, and theta, known to form heteromeric GABAARs, and 3 rho subunits that only form homomeric channels (also known as GABAA rho or GABAC receptor) or pseudoheteromeric if consisting of different rho subunits. GABAAR is assembled from a variety of different subunit subtypes which determines their pharmacology and physiology; the most abundant being 2alpha2beta1gamma stoichiometry. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to its site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. Benzodiazepine and barbiturates each bind to their own distinct sites on the ECD. The channels have to contain the gamma subunit and alpha subunits in order to respond to benzodiazepines. All these major classes of drugs favor channel-opening. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. GABRA1, GABRA3, GABRB3, GABRG2, and GABRD, encoding the alpha1-, alpha3-, beta2-, gamma3-, and delta-subunits have been directly associated with epilepsy. Specific combinations of alpha, beta, and gamma subunits exhibit ethanol sensitivity
TEVKTDIYVTSFGPVSDVDMEYTIDVFFRQTWKDERLKFKGPMKILRLNNLMASKIWTPDTFFHNGKKSV
AHNMTTPNKLLRIQDDGTLLYTMRLTIHAECPMHLEDFPMDAHSCPLKFGSYAYPKSEVVYTWTYGPKKS
VEVAEDGSRLNQYDLIGQTVGSETIKSSTGEYVVMTVHFHLKRK
>gnl|CDD|349800 cd18999, LGIC_ECD_GABAAR_B, extracellular domain of gamma-aminobutyric acid receptor subunit beta (GABAAR-B or GABRB). This family contains extracellular domain (ECD) of beta subunits of type-A gamma-aminobutyric acid receptor (GABAAR), which include beta1-beta4 in vertebrates. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. Benzodiazepine and barbiturates each bind to their own distinct sites on the LBD. The channels must contain the gamma subunit and alpha subunits in order to respond to benzodiazepines. Specific combinations of alpha, beta, and gamma subunits exhibit ethanol sensitivity. All these major classes of drugs favor channel-opening. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. Mutations or genetic variations of the genes encoding the GABRB2 and GABRB3 have been associated with human epilepsy, both with and without febrile seizures. Mutations in GABRB2, and GABRB3 have been associated with infantile spasms and Lennox-Gastaut syndrome. A de novo missense mutation of GABRB2 causes early myoclonic encephalopathy, a disease with a devastating prognosis, characterized by neonatal onset of seizures. Another de novo heterozygous missense variant in exon 4 of GABRB2 is associated with intellectual disability and epilepsy. Mutations in the GABRB1 gene promote alcohol consumption through increased tonic inhibition
VTVGMSIDIASIDMVSEVNMDYTLTMYFQQSWRDKRLAYNGIPLNLTLDNRVADQLWVPDTYFLNDKKSF
VHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWQGGDNAV
TGVEKIELPQFSIVEYRLVSREVVFTTGSYPRLSLSFRLKRN
>gnl|CDD|349801 cd19000, LGIC_ECD_GABAAR_G, extracellular domain of gamma-aminobutyric acid receptor subunit gamma. This family contains extracellular domain (ECD) of the theta subunit of type-A gamma-aminobutyric acid receptor (GABAAR). GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. GABA stimulates human hepatocellular carcinoma growth through overexpressed GABAA receptor theta subunit. Also, two autism spectrum disorder (ASD)-associated protein truncation variants have been identified in alpha 3 (GABRA3) and theta (GABRQ) genes
TVIHTDMYVNSIGPVNAINMEYTIDIFFAQTWYDSRLKFNSTMKVLRLNSNMVGKIWIPDTFFRNSKKAD
AHWITTPNRLLRIWNDGRVLYTLRLTINAECQLQLHNFPMDEHSCPLEFSSYGYPKEEIIYKWKKSSVEV
ADQKSWRLYQFSFVGLRNTTEIVKTTSGDYVVMTIYFDLSRR
>gnl|CDD|349802 cd19001, LGIC_ECD_GABAAR_delta, extracellular domain of gamma-aminobutyric acid receptor subunit delta. This family contains extracellular domain of delta subunit of type-A gamma-aminobutyric acid receptor (GABAAR). GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. Receptors containing the delta subunit (GABRD) are expressed exclusively extra-synaptically (in the cortex, hippocampus, thalamus, striatum, and cerebellum) and mediate tonic inhibition. Studies suggest that delta subunits form heteropentamers in similar stoichiometry and arrangement as alpha/beta/gamma receptors, with the delta subunit replacing the gamma subunit (2alpha:2beta:1delta), although other stoichiometries have also been detected. The delta subunit is flexible in its positioning in the pentameric complex, producing receptors with diverse pharmacological properties. Mutations in GABRD have been associated with susceptibility to generalized epilepsy with febrile seizures, type 5. GABRD gene may also be associated with childhood-onset mood disorders
PVNVALAIEVASIDHISEVNMEYTMTVFLHQSWRDERLSYNHTNETLGLDSRFVDKLWLPDTFIVNAKSA
WFHDVTVENKLIRLQPDGVILYSSRITSTVACDMDLTKYPMDEQECMLDLESYGYSSEDIVYHWSENQEH
IHGLDKLELAQFTITNYRFTTEMMNFKSAGQFPRLSLHFHLRRN
>gnl|CDD|349803 cd19002, LGIC_ECD_GABAAR_E, extracellular domain of gamma-aminobutyric acid receptor subunit epsilon (GABRE). This family contains extracellular domain of epsilon subunit of type-A gamma-aminobutyric acid receptor (GABAAR), a protein that is encoded by the GABRE gene in humans. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. The epsilon subunits form heteropentamers with other GABAAR subunits, possibly with alpha3, beta4, and theta subunits since their genes are clustered on the same human chromosome. Various combinations of alpha3-, theta-, and epsilon-subunits may be assembled at a regional and developmental level in the brain. Brainstem expression of epsilon subunit-containing GABAA receptors is upregulated during pregnancy, particularly in the ventral respiratory neurons, thus protecting breathing, despite increased neurosteroid levels during pregnancy
TVVTVEISVNSLGPLSILDMEYTIDIIFSQTWYDERLRYNDTFESLVLNGNVVSQLWIPDTFFRNSKRTH
EHEITMPNQMVRIHKDGKVLYTIRMTIDAGCSLHMLRFPMDSHSCPLSFSSFSYPENEMIYKWENFKLEI
NEKNSWKLFQFDFTGVSNKTEIITTPVGDFMVMTIFFNVSRR
>gnl|CDD|349804 cd19003, LGIC_ECD_GABAAR_theta, extracellular domain of gamma-aminobutyric acid receptor subunit theta (GABRQ). This family contains extracellular domain (ECD) of the theta subunit of type-A gamma-aminobutyric acid receptor (GABAAR), and encoded by the GABRQ gene, which is mapped to chromosome Xq28 in a cluster of genes that also that encode the alpha 3 and epsilon subunits. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. GABA stimulates human hepatocellular carcinoma growth through overexpressed GABAAR theta subunit. Also, two autism spectrum disorder (ASD)-associated protein truncation variants have been identified in alpha 3 (GABRA3) and theta (GABRQ) genes
PVPVRISIYVSSIEQISEMNMDYTITMFFHQTWKDSRLAYYETTLNLTLDYRMHEKLWVPDCYFLNSKDA
FVHDVTVENRVFQLHPDGTVRYGIRLTTTAACSLDLHKFPMDKQACKLEVESYGYTVEDIILFWEDNGNA
IHMTEELHIPQFTFLGRTITSKEVYFYTGSYIRLILKFQVQRE
>gnl|CDD|349805 cd19004, LGIC_ECD_GABAAR_pi, extracellular domain of gamma-aminobutyric acid receptor subunit pi (GABRP). This family contains extracellular domain of pi subunit of type-A gamma-aminobutyric acid receptor (GABAAR). GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. GABRP is expressed mainly in non-neuronal tissues such as the mammary gland, prostate gland, lung, thymus, and uterus. It is also highly expressed in certain types of cancer such as basal-like breast cancer and pancreatic ductal adenocarcinoma. GABRP is involved in inhibitory synaptic transmission in the central nervous system. Its assembly with other GABAAR subunits alters the sensitivity of recombinant receptors to modulatory agents such as pregnanolone. Studies suggest that polymorphisms in the GABRP gene may be associated with the susceptibility to systematic lupus erythematosus (SLE)
PVTVGMSLDIASIDTISEINMDYTATIFLRQRWTDERLCFEGNKSLSLDGRLVELLWVPDTFIVDSKKSF
LHDITVENRLIRIFPNGTVLYALRITTTVACSMDLTKYPMDKQTCTLQLESWGYNINDVMFYWTRGNDSV
RGLDHLRLAQYTVEDYFTSVSEAVYETGNYPKLVFHFELKRN
>gnl|CDD|349806 cd19005, LGIC_ECD_GABAAR_rho, extracellular domain of gamma-aminobutyric acid receptor subunit rho. This family contains extracellular domain of rho subunits (rho1, rho2, and rho3, encoded by GABRR1, GABRR2, and GABRR3, respectively) of type-A gamma-aminobutyric acid receptor (GABAAR). These subunits homo-oligomerize to form GABAA-rho receptors (formerly classified as GABA-rho or GABAC receptor), but do not co-assemble with any of the classical GABAA subunits. They are especially high expression in the retina and their distinctive pharmacological properties are unique; they are not modulated by many GABAA receptor modulators such as barbiturates, benzodiazepines, and neuroactive steroids. In humans, mutations in the GABRR1 and GABRR2 genes may be responsible for some cases of autosomal recessive retinitis pigmentosa. Variation in GABRR1 is also associated with susceptibility to bipolar schizoaffective disorder while a SNP in GABRR2 has been reported to show association with autism
AIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLSFPSTANKSMTFDGRLVKKIWVPDVFFVHSKR
SFIHDTTTDNIMLRVFPDGHVLYSLRITVTAMCNMDFSRFPLDTQTCSLELESYAYTEDDLMLYWKNGNE
SLKTDEKISLSQFLIQKFHTTSRLAFYSSTGWYNRLYINFTLRRHI
>gnl|CDD|349807 cd19006, LGIC_ECD_GABAAR_LCCH3-like, gamma-aminobutyric acid receptor subunit beta-like extracellular domain in protostomia, such as LCCH3 (ligand-gated chloride channel homolog 3). This family contains extracellular domain of beta-like subunits of type-A gamma-aminobutyric acid receptor (GABAAR) found in protostomia, similar to Drosophila melanogaster ligand-gated chloride channel homolog 3 (LCCH3) subunits. Drosophila melanogaster expresses three GABA-receptor subunit orthologs: (RDL, resistant to dieldrin; GRD, GABA/glycine-like receptor of Drosophila; LCCH3, ligand-gated chloride channel homolog 3), and may possibly form homo- and/or heteropentameric associations. LCCH3 has been shown to combine with subunit GRD to form cation-selective GABA-gated ion channels when coexpressed in Xenopus laevis oocytes. GABAARs are known to be the molecular targets of a class of insecticides. The resulting pentameric receptors in this family have been shown to be activated by insect GABA-receptor agonists muscimol and CACA, and blocked by antagonists fipronil, dieldrin, and picrotoxin, but not bicuculline. GABAARs are abundant in the CNS, where their physiological role is to mediate fast inhibitory neurotransmission. In insects, this inhibitory transmission plays a crucial role in olfactory information processing
PLLVGMDLTIASFDSISEVNMDYTITMYLNQYWKDERLAFSIDNESDVLTLSGDFAEKIWVPDTFFANDK
NSFLHDVTERNKMVRLNGDGSITYGMRFTTTLACMMDLHYYPLDSQNCTVEIESYGYTVSDVVMYWKNTP
VRGVEDAELPQFTIIGYETNDRKEKLATGSYQRLSLSFKLQRN
>gnl|CDD|349808 cd19007, LGIC_ECD_GABAR_GRD-like, gamma-aminobutyric acid receptor subunit alpha-like extracellular domain in protostomia, such as GRD (GABA/glycine-like receptor of Drosophila). This family contains extracellular domain of alpha-like subunits of type-A gamma-aminobutyric acid receptor (GABAAR) found in protostomia, similar to Drosophila melanogaster GABA/ glycine-like receptor of Drosophila (GRD) subunits. Drosophila melanogaster expresses three GABA-receptor subunit orthologs: (RDL, resistant to dieldrin; GRD, GABA/glycine-like receptor of Drosophila; LCCH3, ligand-gated chloride channel homolog 3), and may possibly form homo- and/or heteropentameric associations. LCCH3 has been shown to combine with subunit GRD to form cation-selective GABA-gated ion channels when co-expressed in Xenopus laevis oocytes. GABAARs are known to be the molecular targets of a class of insecticides. The resulting pentameric receptors in this family have been shown to be activated by insect GABA-receptor agonists muscimol and CACA, and blocked by antagonists fipronil, dieldrin, and picrotoxin, but not bicuculline. GABAARs are abundant in the CNS, where their physiological role is to mediate fast inhibitory neurotransmission. In insects, this inhibitory transmission plays a crucial role in olfactory information processing
PTTVETDILIRSMGPISELDMTYSMDCYFRQSWQDRRLAFNGPSIDTLSLSIKMLDRIWKPDTYFYNGKK
SYLHTITTPNKLVRLRQDGRILYSMRLTIKASCPMNLEKFPMDTQSCPLIIGSYGYTTKDVIYKWKDGRD
VVIAPDMTLSQFDLVGFPAGNVTDIRRGGNYSMLSVNFHLQRH
>gnl|CDD|349809 cd19008, LGIC_ECD_GABAR_RDL-like, gamma-aminobutyric acid receptor subunit beta-like extracellular domain in protostomia, such as RDL (resistant to dieldrin). This family contains extracellular domain of beta-like subunits of type-A gamma-aminobutyric acid receptor (GABAAR) found in protostomia, similar to Drosophila melanogaster resistant to dieldrin (RDL) subunits. Drosophila melanogaster expresses three GABA-receptor subunit orthologs: (RDL, resistant to dieldrin; GRD, GABA/glycine-like receptor of Drosophila; LCCH3, ligand-gated chloride channel homolog 3), and may possibly form homo- and/or heteropentameric associations. GABAARs are known to be the molecular targets of a class of insecticides. The resulting pentameric receptors in this family have been shown to be activated by insect GABA-receptor agonists muscimol and CACA, and blocked by antagonists fipronil, dieldrin, and picrotoxin, but not bicuculline. GABAARs are abundant in the CNS, where their physiological role is to mediate fast inhibitory neurotransmission. In insects, this inhibitory transmission plays a crucial role in olfactory information processing. Bombyx mori includes three RDL (RD1, RD2, RD3), one LCCH3, and one GRD subunits. Its RDL1 gene has RNA-editing sites, and the RDL1 and RDL3 genes possess alternative splicing, enhancing the diversity of its GABA-receptor gene family. The three RDL subunits may have arisen from two duplication events
VEVGVTMYVLSISSVSEVDMDFTLDFYFRQFWTDPRLAFKKSPGVESLTVGSEFIKNIWVPDTFFPNEKQ
SYFHIATTSNEFLRIHHSGSITRSIRLTITASCPMNLQYFPMDRQLCHIEIESFGYTMRDIRYKWNGGPN
SVGISPEVELPQFKVLGHRQRAREISLTTGNYSRLACEIQFVRS
>gnl|CDD|349810 cd19009, LGIC_ECD_GlyR_alpha, extracellular domain of glycine receptor alpha subunit. This subfamily contains extracellular domain of glycine receptor (GlyR or GLR) alpha subunits of the amino acid neurotransmitter glycine. GlyR has four known isoforms of alpha-subunit (alpha1-4, encoded by GLRA1, GLRA2, GLRA3, GLRA4) that are essential to bind ligands, and, along with the GlyR beta subunit, have been described to have a regionally and temporally controlled expression during development and maturation of the central nervous system (CNS). These alpha subunits are highly homologous, but differ in their kinetic properties, temporal and regional expression and physiological functions. They can form functional chloride-permeable GlyR ion channels by forming homopentamers with 5 alpha subunits or heteropentamers with a combination of alpha and beta subunits, either a 2alpha-3beta or 3alpha-2beta stoichiometry. In human, mutations in glycine receptor alpha subunits cause disruption of GlyR surface expression or reduced ability of expressed GlyRs to conduct chloride ions. Mutations in GlyR alpha1 subunit leads to hyperekplexia, a rare neurological disorder characterized by neonatal hypertonia and exaggerated startle responses to unexpected stimuli, while mutations in GlyR alpha2 are known to cause cortical neuronal migration/autism spectrum disorder and in GlyR alpha3 to cause inflammatory pain sensitization/rhythmic breathing. GlyR alpha1 and alpha2 subunits have an important role in regulation of the excitatory-inhibitory balance, control of motor actions, modulation of sedative ethanol effects and probably regulation ethanol preference and consumption
PVNVTCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPSMLDSIWKPDLFFANEKG
ANFHEVTTDNKLLRISKNGNVLYSIRLTLTLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQEKGP
VQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEVRFHLERQ
>gnl|CDD|349811 cd19010, LGIC_ECD_GlyR_beta, extracellular domain of glycine receptor beta subunit. This subfamily contains extracellular domain of glycine receptor (GlyR or GLR) beta subunit of the amino acid neurotransmitter glycine encoded by GLRB gene. These subunits form heteropentamers with a combination of alpha and beta subunits, either a 2alpha-3beta or 3alpha-2beta stoichiometry. While the alpha subunits contain binding sites for agonists and antagonists and are responsible for ion channel formation, the beta subunit displays structural and regulatory functions, such as GlyR clustering in synaptic locations by interaction between intracellular loop domains with the scaffolding protein gephyrin, and control of pharmacologic responses to agonist or allosteric modulators due in part to the presence of interfaces alpha/beta and beta/beta. GLRB gene mutations are associated with the neurological disorder hyperekplexia, a rare neurological disorder characterized by neonatal hypertonia and exaggerated startle responses to unexpected stimuli, as well as agoraphobic cognitions
PVDVVVNIFINSFGSIQETTMDYRVNIFLRQKWNDPRLKLPNDFRGSDALTVDPTMFKCLWKPDLFFANE
KSANFHDVTQENILLFIFRDGDVLVSMRLSITLSCPLDLTLFPMDTQRCKMQLESFGYTTDDLRFIWQSG
DPVQLEKIALPQFDIKKEDIEYGNCTKYYKGTGYYTCVEVIFTLRRQ
>gnl|CDD|349812 cd19011, LGIC_ECD_5-HT3A, extracellular domain of serotonin 5-hydroxytryptamine receptor (5-HT3) receptor subunit A (5HT3A). This subfamily contains extracellular domain of subunit A of serotonin 5-HT3 receptor (5-HT3AR), encoded by the HTR3A gene. 5-HT3A subunit forms a homopentameric complex or a heterologous combination with other subunits (B-E). Heteromeric combination of A and B subunits provides the full functional features of this receptor, since either subunit alone results in receptors with very low conductance and response amplitude. 5-HT3A receptors are located in the dorsal vagal complex of the brainstem and in the gastrointestinal (GI) tract, and form a channel circuit that controls gut motility, secretion, visceral perception, and the emesis reflex. These receptors are implicated in several GI and psychiatric disorder conditions including anxiety, depression, bipolar disorder, and irritable bowel syndrome (IBS). Several 5-HT3AR antagonists, such as the isoquinoline Palonosetron, are in clinical use to control emetic reflexes associated with gastrointestinal pathologies and cancer therapies. SNPs in the 5-HT3A serotonin receptor gene are associated with psychiatric disorders
LLRLSDHLLEGYKKGVRPVRDWRKPTTVSIDVMVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFD
NVTQLSIPTDSIWVPDILINEFVDVGKSPEIPYVYVNHEGEVQNYKPIQVVTACSLDIYNFPFDVQNCSL
TFTSWLHTIQDINISLWRSPEEVKSDKSVFMNQGEWELLGVLPQYREFSIDISDSYAEMKFYVVIRRR
>gnl|CDD|349813 cd19012, LGIC_ECD_5-HT3B, extracellular domain of serotonin 5-hydroxytryptamine receptor (5-HT3) receptor subunit B (5HT3B). This subfamily contains extracellular domain of subunit B of serotonin 5-HT3 receptor (5-HT3BR), encoded by the HTR3B gene. 5-HT3B is not functional as a homopentameric complex and is co-expression with the 5-HT3A subunit, resulting in heteromeric 5-HT3AB receptors that are functionally distinct from homomeric 5-HT3A receptors. This receptor causes fast, depolarizing responses in neurons after activation, with affinities of competitive ligands at the two receptor subtypes extracellular domains mostly similar. HTR3B gene variants may contribute to variability in severity of and response to anti-emetic therapy for nausea and vomiting in pregnancy, as well as efficacy of ondansetron in cancer chemotherapy, radiation therapy, or surgery. 5-HT3B subunit affects high-potency inhibition of 5-HT3 receptors by morphine by reducing its affinity at its high-affinity, non-competitive site
RSTLNQLTRTLLRKYDKGVRPVLNWTDATTVYIDLFVHAVLDVDGQNQKLTTSIWYRQIWKDEFLVWNSS
DFDGINEISLPLSAIWVPDIVINEFVDVGRYPDLPYVYVNSSGTIKNYKPIQVVSACDLETYAFPFDRQN
CSLTFRSWLHTVGDVDLALWRSPEEIANDKREFLNDGEWELLSVPSRYRILHMEDQDFAQIQFNVVIRRR
>gnl|CDD|349814 cd19013, LGIC_ECD_5-HT3C_E, extracellular domain of serotonin 5-hydroxytryptamine receptor (5-HT3) receptor subunit E (5HT3E); may include subunits C and D (5-HT3C,D). This subfamily contains extracellular domain of subunit E of serotonin 5-HT3 receptor (5-HT3ER), encoded by the HTR3E gene, and may also contain subunits C and D, all three encoding genes forming a cluster on chromosome 3. Data show that 5-HT3C, 5-HT3D, and 5-HT3E subunits are co-expressed with 5-HT3A in cell bodies of myenteric neurons, and that 5-HT3A and 5-HT3D are expressed in submucosal plexus of the human large intestine while HTR3E is restricted to the colon, intestine, and stomach. None of these subunits can form functional homopentamers, but, upon co-expression with the 5-HT3A subunit, they give rise to functional receptors that differ in maximal responses to 5-HT, and thus modulate 5-HT3 receptor's pharmacological profile. HTR3A and HTR3E polymorphisms have been shown to remarkably up-regulate the expression of 5-HT3 receptors, which have been proved to cause the gastric functional disorders including emesis, eating disorders and IBS-D
NCSGPTTPSLLSALEVEFDRKAFRPVMNLSTPTNVNISFTLYAILGVNEKAQLLTTFLWLRLVWDNEFLS
WDPEECEGVTKISVPRENLWVPDIFINEFMDEDKSPKVPYVYVSHTGRVRDDKPVRVVSSCNLDIFTFPF
DIQNCTLTFGSYLHTVDDIKLFLLLSVEEILKNSRKVLTTQGEWELVDIKAAKAKLSFGEELYDEITFYV
IIRRR
>gnl|CDD|349815 cd19014, LGIC_ECD_nAChR_A1, extracellular domain of nicotinic acetylcholine receptor subunit alpha 1 (CHRNA1). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit alpha 1 (alpha1), encoded by the CHRNA1 gene. These muscle type nicotinic subunits form heteropentamers with other nAChR subunits, most broadly expressed as combination of two alpha1, beta1, delta, and epsilon subunits in mature muscles, and of two alpha1, beta1, delta, and gamma in embryonic cells. The alpha1 subunit in human nAChR is the primary target of Myasthenia gravis antibodies that disrupt communication between the nervous system and the muscle, causing chronic muscle weakness
EHETRLVADLFKNYNKVVRPVEHHKDFVVVTVGLQLIQLINVDEVNQIVTTNVRLKQQWIDVNLKWNPDD
YGGIKKIRIPSSDIWRPDLVLYNNADGDFAIVKETKVLLEYTGKITWTPPAIFKSYCEIIVTHFPFDQQN
CSMKLGTWTYDGTLVVINPESDRPDLSNFMESGEWVMKDYRGWKHWVYYTCCPDTPYLDITYHFLLQRLP
>gnl|CDD|349816 cd19015, LGIC_ECD_nAChR_A2, extracellular domain of nicotinic acetylcholine receptor subunit alpha 2 (CHRNA2). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit alpha 2 (alpha2), encoded by the CHRNA2 gene. It is specifically expressed in medial subpallium-derived amygdalar nuclei from early developmental stages to adult. This subunit is incorporated in heteropentameric neuronal nAChRs mainly with beta2 or beta4 subunits and, along with the alpha4 and alpha7, is one of the main nAChR subunits expressed in primate brain. In Xenopus laevis oocytes, when alpha2 is co-expressed with the beta2 subunit, two subtypes of alpha2beta2 nAChR are formed with either low or high ACh sensitivity. Mouse mutation studies show that alpha2 subunits in the nAChRs influence hippocampus-dependent learning and memory as well as CA1 synaptic plasticity in adolescent mice
EDRLFKHLFTGYNRWSRPVPNTSDVVIVKFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFD
NVTSIRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGKVKWVPPAIYKSSCSIDVTFFPFDQQNCK
MKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCTEIYPDITYYFVIRRLP
>gnl|CDD|349817 cd19016, LGIC_ECD_nAChR_A3, extracellular domain of nicotinic acetylcholine receptor subunit alpha 3 (CHRNA3). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit alpha 3 (alpha3), encoded by the CHRNA3 gene, and likely plays a role in neurotransmission. The alpha3 subunit is expressed in the aorta and macrophages, and may play a regulatory role in the process of vascular inflammation. One of the most broadly expressed subtype is the alpha3beta4 nAChR, also known as the ganglion-type nicotinic receptor, located in the autonomic ganglia and adrenal medulla, where activation yields post- and/or presynaptic excitation, mainly by increased Na+ and K+ permeability. The exact pentameric stochiometry of alpha3beta4 receptor is not known and functional assemblies with varying subunit stoichiometries are possible. Alpha4 plays a pivotal role in regulating the inflammatory responses in endothelial cells and macrophages, via mechanisms involving the modulations of multiple cell signaling pathways. Polymorphisms in this gene (CHRNA3) have been associated with an increased risk of smoking initiation and an increased susceptibility to lung cancer
EHRLFERLFEDYNEIIRPVANVSDPVIIQFEVSMSQLVKVDEVNQIMETNLWLKHIWNDYKLKWNPSDYG
GAEFMRVPAEKIWKPDIVLYNNAVGDFQVDDKTKALLKYTGEVTWIPPAIFKSSCKIDVTYFPFDYQNCT
MKFGSWSYDKAKIDLVLIGSSMNLKDYWESGEWAIIKAPGYKHDIKYNCCEEIYPDITYSLYIRRLP
>gnl|CDD|349818 cd19017, LGIC_ECD_nAChR_A4, extracellular domain of neuronal acetylcholine receptor subunit alpha 4 (CHRNA4). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit alpha 4 (alpha4), encoded by the CHRNA4 gene. Alpha4 forms a functional nAChR by interacting with either nAChR beta2 or beta4 subunits. Alpha4beta2, the major heteropentameric nAChR in the brain, exists in two isoforms, (alpha4)3(beta2)2 and (alpha4)2(beta2)3, with the latter believed to constitute the majority of alpha4beta2 nAChR in the cortex. Both isoforms contain two canonical alpha4:beta2 ACh-binding sites with either low or high ACh sensitivity. This protein is an integral membrane receptor subunit that can interact with either nAChR beta-2 or nAChR beta-4 to form a functional receptor. Mutations in this gene (CHRNA4) cause nocturnal frontal lobe epilepsy type 1. Polymorphisms in this gene may provide protection against nicotine addiction
VLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPADYENVTSIRIPSELIWRPDIVLYNNADG
DFAVTHLTKAHLFHDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMKFGSWTYDKAKIDLVSMHSRVDQL
DFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFIIRRL
>gnl|CDD|349819 cd19018, LGIC_ECD_nAChR_A5, extracellular domain of nicotinic acetylcholine receptor subunit alpha 5 (CHRNA5). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit alpha 5 (alpha5), encoded by the CHRNA5 gene, which is part of the CHRNA5/A3/B4 gene cluster. Polymorphisms in this gene cluster have been identified as risk factors for nicotine dependence, lung cancer, chronic obstructive pulmonary disease, alcoholism, and peripheral arterial disease. A loss-of-function polymorphism in CHRNA5 is strongly linked to nicotine abuse and schizophrenia; the alpha5 nAChR subunit is strategically situated in the prefrontal cortex (PFC), where a loss-of-function in this subunit may contribute to cognitive disruptions in both disorders. Alpha5 forms heteropentamers with alpha3beta2 or alpha3beta4 nAChRs which increases the calcium permeability of the resulting receptors possibly playing significant roles in the initiation of ACh-induced signaling cascades under normal and pathological condition. Acetylcholine (ACh) release and signaling via alpha4/beta2 nAChR subunits plays a central role in the control of attention, but a subset of these oligomers also contains alpha5 subunit. A strong association is seen between a CHRNA5 polymorphism and the risk of lung cancer, especially in smokers
KSEDRLFKHLFQDYQRWVRPVEHLNDTIKIKFGLAISQLVDVDEKNQLMTTNVWLKQEWIDVKLRWNPDD
YAGITSIRVPSDSIWIPDIVLYDNADGRFEGTSTKTVVRYDGTITWTPPANYKSSCTIDVTFFPFDLQNC
SMKFGSWTYDGSQVDIILEDYDVDKRDFFDNGEWEIVSATGSKGNRTDGCCWYPFITYSFIIRRLPL
>gnl|CDD|349820 cd19019, LGIC_ECD_nAChR_A6, extracellular domain of nicotinic acetylcholine receptor subunit alpha 6 (CHRNA6). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit alpha 6 (alpha6), encoded by the CHRNA6 gene. Human (alpha6beta2)(alpha4beta2)3 nicotinic acetylcholine receptors (AChRs) are essential for addiction to nicotine and a target for drug development for smoking cessation. In xenopus oocytes, data show efficient expression of (alpha6beta2)2beta3 AChR subunits with only small changes in alpha6 subunits, while not altering AChR pharmacology or channel structure. Alternatively spliced transcript variants have been observed for this gene. Single nucleotide polymorphisms in this gene have been associated with both nicotine and alcohol dependence. CHRNA6 has a cellular expression signature for retinal ganglion cells with high correlation to Thy1, a known marker, and is preferentially expressed by retinal ganglion cells (RGCs) in the young and adult mouse retina and expression is reduced in glaucoma. A genetic variant in CHRNB3#CHRNA6 cluster is associated with esophageal adenocarcinoma
VTVHFEVAITQLVNVDEVNQIMETNLWLRHIWNDYKLRWDPREYDGIEFMRVPADKIWKPDIVLYNNAVG
DFQVEGKTKALLKYNGMITWTPPAIFKSSCPMDITFFPFDHQNCSLKFGSWTYDKAKIDLLIIGSKVDMN
DFWENSEWEIVDASGYKHDIKYNCCEEIYTDITYSFYIRRL
>gnl|CDD|349821 cd19020, LGIC_ECD_nAChR_A7, extracellular domain of neuronal acetylcholine receptor subunit alpha 7 (CHRNA7). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit alpha 7 (alpha7), encoded by the CHRNA7 gene. Alpha7 subunits form a homo-pentameric channel, displays marked permeability to calcium ions and is a major component of brain nicotinic receptors that are blocked by, and highly sensitive to, alpha-bungarotoxin. This protein is ubiquitously expressed in both the central nervous system and in the periphery, in several tissues, including adrenal, small intestine, testis, and stomach. CHRNA7 is located in a region identified as a major susceptibility locus for juvenile myoclonic epilepsy and a chromosomal location involved in the genetic transmission of schizophrenia. It is also genetically linked to other disorders with cognitive deficits, including bipolar disorder, ADHD, Alzheimer's disease, and Rett syndrome. An evolutionarily recent partial duplication of CHRNA7 on chromosome 15 forms a new gene, CHRFAM7A or FAM7A, which encodes the protein dup-alpha7. This protein assembles with alpha7 subunits, results in fewer binding sites and is a dominant negative regulator of alpha7 nAChR function
PLTVYFSLSLMQIMDVDEKNQVLTTNIWLQMYWTDHYLQWNASEYPGVKNVRFPDGQIWKPDILLYNSAD
ERFDATFHTNVLVNSSGHCQYLPPGIFKSSCYIDVRWFPFDVQKCNLKFGSWTYGGWSLDLQMQEADISG
YISNGEWDLVGVPGKRNEKFYECCKEPYPDVTFTVTMRRR
>gnl|CDD|349822 cd19021, LGIC_ECD_nAChR_A7L, extracellular domain of neuronal acetylcholine receptor subunit alpha-7-like. This family contains the extracellular domain of nicotinic acetylcholine receptor (nAChR), a member of the pentameric "Cys-loop" superfamily of transmitter-gated ion channels. nAChR is found in high concentrations at the nerve-muscle synapse, where it mediates fast chemical transmission of electrical signals in response to the endogenous neurotransmitter acetylcholine (ACh) released from the nerve terminal into the synaptic cleft. Thus far, seventeen nAChR subunits have been identified, including ten alpha subunits, four beta subunits and one gamma, delta, and epsilon subunit each, all found on the cell membrane that non-selectively conducts cations (Na+, K+, Ca++). These nAChR subunits combine in several different ways to form functional nAChR subtypes which are broadly categorized as either muscle subtype located at the neuromuscular junction or neuronal subtype that are found on neurons and on other cell types throughout the body. The muscle type of nAChRs are formed by the alpha1, beta1, gamma, delta, and epsilon subunits while the neuronal type are composed of nine alpha subunits and three beta subunits, which combine in various permutations and combinations to form functional receptors. Among various subtypes of neuronal nAChRs, the homomeric alpha7 and the heteromeric alpha4beta2 receptors are the main subtypes widely distributed in the brain and implicated in the pathophysiology of neurodevelopmental disorders such as schizophrenia and autism and neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease
IVVELQLSLLQIIDVDEKNQVLITNAWLQMYWVDIYLSWDQYEYPGVQNLRFPSDQIWVPDILLYNSADE
RFDATFHTNVLVNYSGSCQYIPPGILKSTCYIDVRWFPFDVQKCDLKFGSWTHSGWLIDLQMLEADISNY
ISNGEWDLVGVPGKRNELYYECCKEPYPDVTYTITMRRR
>gnl|CDD|349823 cd19022, LGIC_ECD_nAChR_A9, extracellular domain of neuronal acetylcholine receptor subunit alpha 9 (CHRNA9). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit alpha 9 (alpha9), encoded by the CHRNA9 gene. This protein is involved in cochlea hair cell development and is also expressed in the outer hair cells (OHCs) of the adult cochlea as well as in keratinocytes, the pituitary gland, B-cells, and T-cells. Mammalian alpha9 subunits can form functional homomeric alpha9 receptors as well as the heteromeric alpha9alpha10 receptors, the latter being atypical since the heteromeric alpha9alpha10 receptor is composed only of alpha subunits compared to nAChRs typically assembled from alpha and beta subunits. A stoichiometry of (alpha9)2(alpha10)3 has been determined for the rat recombinant receptor. The alpha9alpha10 nAChR is an important therapeutic target for pain; selective block of alpha9alpha10 nicotinic acetylcholine receptors by the conotoxin RgIA has been shown to be analgesic in an animal model of nerve injury pain, and accelerates recovery of nerve function after injury, possibly through immune/inflammatory-mediated mechanisms. CHRNA9 polymorphisms are associated with non-small cell lung cancer, and effect of a particular SNP (rs73229797) and passive smoking exposure on risk of breast malignancy has been observed
AQKLFNDLFEDYSNALRPVEDTDKVLNVTLQITLSQIKDMDERNQILTAYLWIRQSWYDAYLKWDRDEYD
GLDSIRIPSNLVWRPDIVLYNKADDEFSEPVNTNVVLRYDGKITWDAPAITKSSCVVDVSYFPFDNQQCN
LTFGSWTYNGNQVDIINALDSGDLSDFVEDVEWEVHGMPAVKNVITYGCCSEPYPDVTFTLILKRRS
>gnl|CDD|349824 cd19023, LGIC_ECD_nAChR_A10, extracellular domain of neuronal acetylcholine receptor subunit alpha 10 (CHRNA10). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit alpha 10 (alpha10), encoded by the CHRNA10 gene. This protein is involved in cochlea hair cell development and is also expressed in the outer hair cells (OHCs) of the adult cochlea as well as in keratinocytes, the pituitary gland, B-cells, and T-cells. Unlike alpha9 nAChR subunits, alpha10 subunits do not generate functional channels when expressed heterologously, suggesting that alpha10 might serve as a structural subunit, much like a beta subunit of heteromeric receptors, providing only complementary components to the agonist binding site. Mammalian alpha10 subunits can form functional heteromeric alpha9alpha10 receptors, an atypical heteromeric receptor since it is composed only of alpha subunits compared to nAChRs typically assembled from alpha and beta subunits. A stoichiometry of (alpha9)2(alpha10)3 has been determined for the rat recombinant receptor. The alpha9alpha10 nAChR is an important therapeutic target for pain; selective block of alpha9alpha10 nicotinic acetylcholine receptors by the conotoxin RgIA has been shown to be analgesic in an animal model of nerve injury pain, and accelerates recovery of nerve function after injury, possibly through immune/inflammatory-mediated mechanisms
LNVTLQITLSQIIDMDERNQILTAYLWIRQVWLDAYLAWNKEAYDGLDTIRIPSSYVWRPDIVLYNNADD
RFTGSMETNVVIRSDGQIMWDSPAITKSSCKVDVSFFPFDGQQCRLTFGSWTYNGNQIDILNLLDTGDLT
DFVENVEWEVLGMPAKRNVITYGCCSEPYPDVTYTLLLKRR
>gnl|CDD|349825 cd19024, LGIC_ECD_nAChR_B1, extracellular domain of nicotinic acetylcholine receptor subunit beta 1 (CHRNB1). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit beta 1 (beta1), encoded by the CHRNB1 gene. It is a muscle type subunit found predominantly in the neuromuscular junction (NMJ), but also in other tissues and cell lines such as adrenal glands, carcinomas, brain, and lung. Simultaneous mRNA and protein expression of beta1 nAChR subunit is present in human placenta and skeletal muscle. The beta1 nAChR subunit forms a heteropentamer with either (alpha1)2, gamma and delta subunits in embryonic type or (alpha1)2, epsilon and delta subunits in adult type receptors. nAChRs containing beta1 subunits have been attributed to efficient clustering and anchoring of the receptors to the cytoskeleton which is important for formation of synapses in the NMJ. Mutations in the transmembrane domain region of this gene are associated with slow-channel congenital myasthenic syndrome (CMS)
EGQLLEKLFENYNPKVRPARTVGDRVVVSVGLTLAQLISLNEKNEEMTTKVYLDLEWTDYRLSWDPAEYD
GIDSLRITSDSVWLPDIVLMNNNDGNFDVALDVNVLVSSDGSVRWHPPAIYRSSCSIEVTYFPFDWQNCS
MVFRSYTYDSSEVSLQHGLDPDGKELQEIVIHENTFIENGQWSIEHKPSRKNQLPGDPLYEDITFYLIIR
RKP
>gnl|CDD|349826 cd19025, LGIC_ECD_nAChR_B2, extracellular domain of nicotinic acetylcholine receptor subunit beta 2 (CHRNB2). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit beta 2 (beta2), encoded by the CHRNB2 gene. The most abundant nicotinic subtype in the human brain is alpha4beta2 receptor which is known to assemble in two functional subunit stoichiometries, (alpha4)3(beta2)2 and (alpha4)2(beta2)3, the latter having a much higher affinity for both acetylcholine and nicotine. This subtype is implicated in the pathophysiology of neurodevelopmental disorders such as schizophrenia and autism, and neurodegenerative disorders such as Parkinson's disease and Alzheimer's disease. Thus, pharmacological ligands targeting this subtype have been researched and developed as a treatment approach implicated in these diseases. They include agonists such as varenicline and cytisine used as smoking cessation aids, as well as positive allosteric modulators (PAMs) such as desformylflustrabromine (dFBr), which are ligands that bind to nicotinic receptors at sites other than the orthosteric site where acetylcholine binds, and are not able to act as agonists on nAChR
RLVEHLLGPSRYNKLIRPATNGSQLVTVQLMVSLAQLISVHEREQIMTTNVWLTQEWEDYRLTWDPAEFD
NMKKVRLPSKHIWLPDVVLYNNADGMYEVSFYSNAVVSYDGSIFWLPPAIYKSACKIEVKHFPFDQQNCT
LKFRSWTYDRTEIDLVLRSDVASLDDFTPSGEWDIVALPGRRNENPNDSTYVDITYDFIIRRKP
>gnl|CDD|349827 cd19026, LGIC_ECD_nAChR_B3, extracellular domain of nicotinic acetylcholine receptor subunit beta 3 (CHRNB3). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit beta 3 (beta3), encoded by the CHRNB3 gene. CHRNB3 polymorphisms have been reported to potentially affect nicotine-induced upregulation of nicotinic and to be associated with disorders such as schizophrenia, autism, and cancer. Beta3 subunit is depleted in the striatum of Parkinson's disease patients. Rare variants in CHRNB3 are also implicated in risk for alcohol and cocaine dependence and independently associated with bipolar disorder. Human alpha6beta2beta3* (* indicating possible additional assembly partners) nAChRs on dopaminergic neurons are important targets for drugs to treat nicotine addiction and Parkinson's disease; (alpha6beta2)(alpha4beta2)beta3 nAChR is essential for addiction to nicotine and a target for drug development for smoking cessation
IKVLFGLKISQLVDVDEKNQLMTTNVWLKQEWMDHKLRWNPEDYGGITSIRVPSESLWLPDIVLFENADG
RFEGSLMTKAIVKYNGTVTWTPPASYKSSCTMDVTFFPFDRQNCSMKFGSWTYDGNMVDLILIDENVDRK
DFFDNGEWEILNAKGMKGNRKDGLYSYPFITYSFVLRRL
>gnl|CDD|349828 cd19027, LGIC_ECD_nAChR_B4, extracellular domain of nicotinic acetylcholine receptor subunit beta 4 (CHRNB4). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit beta 4 (beta4), encoded by the CHRNB4 gene and ubiquitously expressed on lung epithelial cells. The cluster of human neuronal nicotinic receptor gene CHRNA5-CHRNA3-CHRNB4 is related to drug-related behaviors and the development of lung cancer. One of the most broadly expressed subtype is the alpha-3 beta-4 nAChR, also known as the ganglion-type nicotinic receptor, located in the autonomic ganglia and adrenal medulla, where activation yields post- and/or pre-synaptic excitation, mainly by increased Na+ and K+ permeability. Beta4 forms heteromeric nAchRs to modulate receptor affinity for nicotine, but the exact pentameric stochiometry of alpha3beta4 receptor is not known; functional assemblies with varying subunit stoichiometries are possible
VSIKLQLSLAQLISVNEREQIMTTNVWLNQEWTDYRLTWNPSDYEGINKLRIPAKHIWLPDIVLYNNADG
TYEVSVYTNAIVQNNGSVAWLPPAIYKSACKIEVKHFPFDQQNCTLKFRSWTYDHTEIDMVLKTPTASMD
DFTPSGEWDIVALPGRRTVNPLDPTYVDVTYDFIIKRK
>gnl|CDD|349829 cd19028, LGIC_ECD_nAChR_D, extracellular domain of nicotinic acetylcholine receptor subunit delta (CHRND). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit delta (delta), encoded by the CHRND gene and found in the muscle. Delta nAChR subunit forms a heteropentamer with either (alpha1)2, beta and gamma subunits in embryonic type or (alpha1)2, beta and epsilon subunits in adult type receptors. Defects in this gene are a cause of multiple pterygium syndrome lethal type (MUPSL), congenital myasthenic syndrome slow-channel type (SCCMS), and congenital myasthenic syndrome fast-channel type (FCCMS). The slow-channel congenital myasthenic syndromes (SCCMS) are caused by prolonged opening episodes of AChR due to dominant gain-of-function mutations in the transmembrane regions of the heteropentamer. These mutations produce an increase in the channel opening rate, a decrease in the channel closing rate, or an increase in the affinity of ACh for the AChR, resulting in the stabilization of the open state or the destabilization of the closed state of the AChR
ERLINHLFIERGYNKELRPVAHKDEVVNVALALTLSNLISLKEVDETLTTNVWVEHGWYDHRLTWNASEY
GNISILRLPPEMVWLPEIVLENNNDGQFEVAYYCNVLVYSDGFVYWLPPAIFRSSCPINVNYFPFDWQNC
SLKFSSLNYNAKEINLDLKTDTDDGKTYPVEWIIIDPEGFTENGEWEIVHKPAKKNIDPSKPPESTKYQD
ITFYLIIKRKP
>gnl|CDD|349830 cd19029, LGIC_ECD_nAChR_G, extracellular domain of nicotinic acetylcholine receptor subunit gamma (CHRNG). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit gamma (gamma), encoded by the CHRNG gene expressed during early fetal development, and replaced by the epsilon subunit in the adult. The gamma subunit forms a heteropentamer with (alpha1)2, beta, and delta and plays a role in neuromuscular organogenesis and ligand binding. Disruption of gamma subunit expression prevents the correct localization of the receptor in cell membranes. Mutations in CHRNG may cause the non-lethal Escobar variant (EVMPS) and lethal form (LMPS) of multiple pterygium syndrome (MPS), a condition characterized by prenatal growth failure with pterygium and akinesia leading to muscle weakness and severe congenital contractures, as well as scoliosis. Muscle-type acetylcholine receptor is the major antigen in the autoimmune disease myasthenia gravis
DVVDVTLKLTLTNLISLNEKEEALTTNVWIEIQWNDYRLRWNPSEYEGIWVLRVPSTMVWLPDIVLENNI
DGQFEVAYYANVLVYPDGSMYWLPPAIYRSTCPIEVTYFPFDWQNCSLVFQSQTYSANEINLQLSVEEGT
TIEWIDIDPEAFTENGEWAIRHRPAKKILNPQLPKDDLGYQEIVFYLIIQRKP
>gnl|CDD|349831 cd19030, LGIC_ECD_nAChR_E, extracellular domain of nicotinic acetylcholine receptor subunit epsilon (CHRNE). This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit epsilon (epsilon), encoded by the CHRNE gene and found in adult skeletal muscle. Epsilon subunit forms a heteropentamer with (alpha1)2, beta and delta after birth, replacing the gamma subunit seen in embryonic receptors. The adult-type epsilon-AChR has a higher conductance and a shorter open time compared to embryonic gamma-AChR and the open channel is non-selectively cation permeable. Mutations of the CHRNE gene are the most common causes of congenital myasthenic syndrome (CMS), most of which are autosomal recessive loss-of-function mutations, resulting in endplate AChR deficiency. A highly fatal fast-channel syndrome is caused by AChR epsilon subunit mutation (Trp to Arg; changing environment from anionic to cationic) at the agonist binding site at the alpha/epsilon interface of the receptor, thus disrupting agonist binding affinity and gating efficiency
VTISLKVTLTNLISLNEKEETLTTSVWIGIDWQDYRLNYSKDDFGGVETLRVPSELVWLPEIVLENNIDG
QFGVAYDANVLVYEGGSVSWLPPAIYRSTCAVEVTYFPFDWQNCSLIFRSQTYNAEEVEFTFAVDDDGKT
INKIDIDTEAYTENGEWAIDFCPGVIRRHHGGSTDGPGETDVIYSLIIRRK
>gnl|CDD|349832 cd19031, LGIC_ECD_nAChR_proto_alpha-like, extracellular domain of nicotinic acetylcholine receptor subunit alpha-like found in protostomia. This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit alpha-like in organisms that include arthropods, mollusks, annelid worms, and flat worms, and have their cholinergic system limited to the central nervous system. C. elegans genome encodes 29 acetylcholine receptor subunits, of which the levamisole-sensitive receptor (L-AChR) alpha-subunits, UNC-38, UNC-63, and LEV-8, included in this subfamily, form heteromers with the two non-alpha (also known as beta-like) subunits, UNC-29 and LEV-1. This receptor functions as the main excitatory postsynaptic receptor at neuromuscular junctions, indicating that many are expressed in neurons. Also included is the nicotinic alpha subunit MARA1 (Manduca ACh Receptor Alpha 1) which is expressed in Ca2+ responding neurons and contributes to the nicotinic responses in the neurons. In insects, the receptors supply fast synaptic excitatory transmission and represent a major target for several insecticides. In Drosophila, ten exclusively neuronal nAChRs have been identified, Dalpha1-Dalpha7 and Dbeta1-Dbeta3, and various combinations of these subunits and mutations are key to nAChR function. Alpha5 subunit is involved in alpha-bungarotoxin sensitivity while the alpha6 subunit is essential for the insecticidal effect of spinosad. nAChR agonists acetylcholine, nicotine, and neonicotinoids stimulate dopamine release in Drosophila larval ventral nerve cord and mutations in nAChR subunits affect how insecticides stimulate dopamine release
DAKRLYDDLLSNYNYNRRPRVTNDSDTLTVKLGLKLSQLIDVDEKNQIMTTNVWLEQEWYDYKLVWDPAE
YGGVEMLYVPSEDIWLPDIVLYNNADGNYEVTLMTKATLHYNGTVRWEPPAIYKSSCEIDVEYFPFDEQT
CFMKFGSWTYDGFEVDLRHVDQKYGSEDEVIDVGIDLSEFYPSVEWDLLEVPARRNEKYYPCCDEPYPDI
TFNITLRRKTLF
>gnl|CDD|349833 cd19032, LGIC_ECD_nAChR_proto_beta-like, extracellular domain of nicotinic acetylcholine receptor subunit beta-like found in protostomia. This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit beta-like in organisms that include arthropods, mollusks, annelid worms, and flat worms, and have their cholinergic system limited to the central nervous system. C. elegans genome encodes 29 acetylcholine receptor subunits, of which the levamisole-sensitive receptor alpha-subunits (L-AChR), UNC-38, UNC-63, and LEV-8, form heteromers with the two non-alpha (also known as beta-like) subunits, UNC-29 and LEV-1 found in this subfamily. This receptor functions as the main excitatory postsynaptic receptor at neuromuscular junctions, indicating that many are expressed in neurons. In insects, the receptors supply fast synaptic excitatory transmission and represent a major target for several insecticides. In Drosophila, ten exclusively neuronal nAChR subunits have been identified, Dalpha1-Dalpha7 and Dbeta1-Dbeta3, and various combinations of these subunits and mutations are key to nAChR function. Dbeta1 subunits in dopaminergic neurons play a role in acute locomotor hyperactivity caused by nicotine in male Drosophila. Mutations of Dbeta2 or Dalpha1 nAChR subunits in Drosophila strains have significantly lower neonicotinoid-stimulated release, but no changes in nicotine-stimulated release; they are highly resistant to the neonicotinoids nitenpyram and imidacloprid. This family also includes a novel nAChR found in Aplysia bag cell neurons (neuroendocrine cells that control reproduction) which is a cholinergic ionotropic receptor that is both, nicotine insensitive and acetylcholine sensitive
DEERLVRDLFRGYNYLIRPVRNMSEPVEVNFGLALIQLINVDEKNQIMKTNVWLTMYWNDYQLKWDPADY
GGIKVIRVPPDKVWKPDIVLFNNADGNYEVSYKSNVLIYSTGEVLWVPPAIYKSSCTIDVEYFPFDQQEC
EMKFGSWTFNGDEVSLDLYNNKKFVDLSDYWKSGTWDIIDVPGQLVNKDDAGPTETDIIFKIKIRRKT
>gnl|CDD|349834 cd19033, LGIC_ECD_nAChR_proto-like, nicotinic acetylcholine receptor (nAChR) subunit extracellular domain in molluscs and annelids. This subfamily contains the extracellular domain of nicotinic acetylcholine receptor subunit found in molluscs, including several Lymnaea nAChRs, and annelids that are mostly uncharacterized. To date, 12 Lymnaea nAChRs have been identified which can be subdivided in two subtypes according to the residues that may be contributing to the selectivity of ion conductance. Phylogenetic analysis of the nAChR gene sequences suggests that anionic nAChRs in molluscs probably evolved from cationic ancestors through amino acid substitutions in the ion channel pore which is a mechanism different from acetylcholine-gated channels in other invertebrates
VTVEFGLQLIQILDLDENNQVLTTNVWSRYRWTDYHLRWNPEDYGGVTHVRIPPDKIWTPDIKLYNYADE
RLEERREAMVVVYSTGTVLWMPQAIYKSTCEIDIKYFPFDTQTCYLKFGSWTYDGTRLDITFYDNEEEID
LTDYIESNEWEILAYPAVKNVKYYPCCPEPYPDLTFFLVIKRR
>gnl|CDD|349835 cd19034, LGIC_ECD_GABAAR_A1, extracellular domain of gamma-aminobutyric acid receptor subunit alpha-1 (GABAAR-A1 or GABRA1). This family contains extracellular domain of gamma-aminobutyric acid receptor subunit alpha-1 (GABAAR-A1), a protein that is encoded by the GABRA1 gene in humans. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. The alpha-1 subunits form heteropentamers with other GABAAR subunits, most broadly expressed as combination of two alpha1, beta1, gamma. Alpha1, beta2, and gamma2 subunits are clustered on the same human chromosome and may be why alpha1beta2gamma2 receptors are one of the most abundant GABAA receptor isoforms in CNS neurons. Mutations in this gene cause familial juvenile myoclonic epilepsy, sporadic childhood absence epilepsy type 4, and idiopathic familial generalized epilepsy. Polymorphisms in GABRA1 are also significantly associated with schizophrenia. GABRA1 has also been associated with methamphetamine abuse. The GABRA1 receptor is the specific target of the z-drug class of nonbenzodiazepine hypnotic agents and is responsible for their hypnotic and hallucinogenic effects
RLRPGLGERVTEVKTDIFVTSFGPVSDHDMEYTIDVFFRQSWKDERLKFKGPMTVLRLNNLMASKIWTPD
TFFHNGKKSVAHNMTMPNKLLRITEDGTLLYTMRLTVRAECPMHLEDFPMDAHACPLKFGSYAYTRAEVV
YEWTREPARSVVVAEDGSRLNQYDLLGQTVDSGIVQSSTGEYVVMTTHFHLKRK
>gnl|CDD|349836 cd19035, LGIC_ECD_GABAAR_A2, extracellular domain of gamma-aminobutyric acid receptor subunit alpha-2 (GABAAR-A2 or GABRA2). This family contains extracellular domain of gamma-aminobutyric acid receptor subunit alpha-2 (GABAAR-A2), a protein that is encoded by the GABRA2 gene in humans. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. The alpha-2 subunit forms heteropentamers with other GABAAR subunits, most broadly expressed as combination of alpha2beta3gamma2. The alpha-2 (GABRA2) subunit is found primarily in the forebrain and hippocampus, and is more confined to areas of the brain compared to other alpha subunits. GABRA2 increases the risk of anxiety, making it a target for treating behavioral disorders including alcohol dependence, and drug use. GABRA2 is a binding site for benzodiazepines (psychoactive drugs known to reduce anxiety), causing chloride channels to open, leading to the hyper-polarization of the membrane. Other anxiolytic drugs such as Diazepam bind this subunit to induce inhibitory effects. GABRA2 is associated with reward behavior when it activates the insula, the part of the cerebral cortex responsible for emotions. GABA alpha2 and/or alpha3 receptor subtypes are also involved in GABAergic modulation of prolactin secretion
DRLLDGYDNRLRPGLGDSITEVFTNIYVTSFGPVSDTDMEYTIDVFFRQRWKDERLKFKGPMNILRLNNL
MASKIWTPDTFFHNGKKSVAHNMTMPNKLLRIQDDGTLLYTMRLTVQAECPMHLEDFPMDAHSCPLKFGS
YAYTTSEVTYIWTYNASDSVQVAPDGSRLNQYDLLGQTIGKETIKSSTGEYTVMTAHFHLKRK
>gnl|CDD|349837 cd19036, LGIC_ECD_GABAAR_A3, extracellular domain of gamma-aminobutyric acid receptor subunit alpha-3 (GABAAR-A3 or GABRA3). This family contains extracellular domain of gamma-aminobutyric acid receptor subunit alpha-3 (GABAAR-A3), a protein that is encoded by the GABRA3 gene in humans. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. The alpha-3 subunit forms heteropentamers with other GABAAR subunits, most broadly expressed as combination of alpha3betagamma2, typically found post-synaptically. Rare loss-of-function variants in GABRA3 have been shown to increase the risk for a varying combination of epilepsy, intellectual disability/developmental delay, and dysmorphic features. GABRA3, normally exclusively expressed in adult brain, is also expressed in breast cancer, with high expression being inversely correlated with breast cancer survival. It activates the AKT pathway to promote breast cancer cell migration, invasion, and metastasis. GABRA3 promotes lymphatic metastasis in lung adenocarcinoma by mediating upregulation of matrix metalloproteinases, MMP-2 and MMP-9, through activation of the JNK/AP-1 signaling pathway. GABRA3 is overexpressed in human hepatocellular carcinoma growth and, with GABA, promotes the proliferation of cancer cells
LDGYDNRLRPGLGDSVTEVKTDIYVTSFGPVSDTDMEYTIDVFFRQSWRDERLKFDGPMKILPLNNLLAS
KIWTPDTFFHNGKKSVAHNMTTPNKLLRLVDNGTLLYTMRLTIHAECPMHLEDFPMDVHACPLKFGSYAY
TKTEVVYSWTLGKNKSVEVAPDGSRLNQYDLLGHVVGTETIRSSTGEYVVMTTHFHLKRK
>gnl|CDD|349838 cd19037, LGIC_ECD_GABAAR_A4, extracellular domain of gamma-aminobutyric acid receptor subunit alpha-4 (GABAAR-A4 or GABRA4). This family contains extracellular domain of gamma-aminobutyric acid receptor subunit alpha-4 (GABAAR-A4), a protein that is encoded by the GABRA4 gene in humans, with biased expression in the brain and heart. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. The alpha-4 subunit forms heteropentamers with other GABAAR subunits, most broadly expressed as combination of alpha2alpha4beta1gamma1, all four subunits existing on the same gene cluster. Alpha-4 is involved in the etiology of autism and eventually increases autism risk through interaction with the beta-1 (GABRB1) subunit. Polymorphism in GABRA4 may trigger migraine by ethanol, while another is associated to faster reaction times and with lower ethanol effects. A rare variant in GABRA4 may have modest physiological effect in autism spectrum disorder etiology
DGYDNRLRPGFGGPVTEVKTDIYVTSFGPVSDVEMEYTMDVFFRQTWVDKRLKYDGPIEILRLNNLMVTK
VWTPDTFFRNGKKSVAHNMTAPNKLFRIMRNGTILYTMRLTISAECPMRLVDFPMDGHACPLKFGSYAYP
KSEMIYTWTKGPEKSVEVPPESSSLVQYDLIGQTVSSETIKSITGEYIVMTVYFHLRRK
>gnl|CDD|349839 cd19038, LGIC_ECD_GABAAR_A5, extracellular domain of gamma-aminobutyric acid receptor subunit alpha-5 (GABAAR-A5 or GABRA5). This family contains extracellular domain of gamma-aminobutyric acid receptor subunit alpha-5 (GABAAR-A5), a protein that is encoded by the GABRA5 gene in humans, with biased expression in the brain and heart. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. The alpha-5 subunit forms heteropentamers with other GABAAR subunits, most broadly expressed as alpha5-beta-gamma2, and probably alpha5-beta3-gamma2, predominantly expressed in the hippocampus and localized extrasynaptically. These receptors have been demonstrated to play an important modulatory role in learning and memory processes, thus making them suitable targets for pharmacological intervention. Studies show that alpha5-containing GABAARs play an important part in tonic inhibition in hippocampal pyramidal neurons, and that these can also contribute to synaptic inhibition. Studies strongly suggest that amnesia is primarily mediated by alpha5-beta-gamma2. Polymorphisms in GABRA5 (and GABRA3) are linked to the susceptibility to panic disorder. A genetic association also exists between GABRA5 and bipolar affective disorder
DGYDNRLRPGLGERITQVRTDIYVTSFGPVSDTEMEYTIDVFFRQSWKDERLRFKGPMQRLPLNNLLASK
IWTPDTFFHNGKKSIAHNMTTPNKLLRLEDDGTLLYTMRLTISAECPMQLEDFPMDAHACPLKFGSYAYP
NSEVVYVWTNGTTKSVVVAEDGSRLNQYHLMGQTVGTENISTSTGEYTIMTAHFHLKRK
>gnl|CDD|349840 cd19039, LGIC_ECD_GABAAR_A6, extracellular domain of gamma-aminobutyric acid receptor subunit alpha-6 (GABAAR-A6 or GABRA6). This family contains extracellular domain of gamma-aminobutyric acid receptor subunit alpha-6 (GABAAR-A6), a protein that is encoded by the GABRA6 gene in humans. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. The alpha-6 subunit forms heteropentamers with other GABAAR subunits, most broadly expressed as alpha6-beta-gamma2 found extrasynaptically, alpha6-beta2/3-delta in the cerebellar granule cells and likely also forms alpha1-alpha6-beta-gamma/alpha1-alpha6-beta-delta. A GABRA6 mutation from Arg to Trp, has been identified as a susceptibility gene that may contribute to the pathogenesis of childhood absence epilepsy and cause neuronal disinhibition and increase in seizures via a reduction of alphabetagamma and alphabetadelta receptor function and expression. Polymorphism in the GABRA6 gene is associated with specific personality characteristics as well as a marked attenuation in hormonal and blood pressure responses to psychological stress. Alpha6-containing receptors lack high sensitivity to diazepam
GYDNRLRPGFGGPVTEVKTDIYVTSFGPVSDVEMEYTMDVFFRQTWIDERLKFGGPTEILRLNNLMVSKI
WTPDTFFRNGKKSISHNMTTPNKLFRIMQNGTILYTMRLTINAECPMRLVNFPMDGHACPLKFGSYAYPK
SEIVYTWKKGPLYSVEVPEESSSLLQYDLIGQTVSSETLKSNTGEYVVMTVYFHLQRK
>gnl|CDD|349841 cd19040, LGIC_ECD_GABAAR_B1, extracellular domain of gamma-aminobutyric acid receptor subunit beta-1 (GABAAR-B1 or GABRB1). This family contains extracellular domain (ECD) of gamma-aminobutyric acid receptor beta-1 subunit, a protein that is encoded by the GABRB1 gene. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. The beta-1 subunit forms heteropentamers with other GABAAR subunits, likely expressed as alpha-beta1-gamma/delta, mainly found in the brain. It is clustered on the chromosome with genes encoding alpha 4, alpha 2, and gamma 1 subunits of the GABAAR. GABRB1 expression is altered significantly in the lateral cerebellum of subjects with schizophrenia, major depression, and bipolar disorder. Mutations in the GABRB1 gene promote alcohol consumption through increased tonic inhibition. Epigenetic control of gene expression may affect the expression of GABRB1 and disrupt inhibitory synaptic transmission during embryonic development. The GABRB1 gene is also associated with thalamus volume and modulates the association between thalamus volume and intelligence
VDVGMRIDVASIDMVSEVNMDYTLTMYFQQSWRDKRLSYSGIPLNLTLDNRVADQLWVPDTYFLNDKKSF
VHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWNGGEGAV
TGVNKIELPQFSIIDYKMVSKKVEFTTGAYPRLSLSFRLKRN
>gnl|CDD|349842 cd19041, LGIC_ECD_GABAAR_B2, extracellular domain of gamma-aminobutyric acid receptor subunit beta-2 (GABAAR-B2 or GABRB2). This family contains extracellular domain (ECD) of gamma-aminobutyric acid receptor beta-2 subunit, a protein that is encoded by the GABRB2 gene. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. The beta-2 subunit forms heteropentamers with other GABAAR subunits, with alpha1-beta2-gamma2 subtype being the most prevalent isoform (approximately 50%-60% of all GABAARs), and are expressed in almost all regions of the brain. It also assembles less abundantly as alpha4beta2/3delta and alpha6beta2/3delta. Mutations or genetic variations of the genes encoding the GABRB2 and GABRB3 have been associated with human epilepsy, both with and without febrile seizures. Mutations in GABRB2, and GABRB3 have been associated with infantile spasms and Lennox-Gastaut syndrome. A de novo missense mutation of GABRB2 causes early myoclonic encephalopathy, a disease with a devastating prognosis, characterized by neonatal onset of seizures. Another de novo heterozygous missense variant in exon 4 of GABRB2 is associated with intellectual disability and epilepsy. GABRB2 plays important tumorigenic functions and acts as a novel oncogene in papillary thyroid carcinoma (PTC)
VAVGMNIDIASIDMVSEVNMDYTLTMYFQQAWRDKRLSYNVIPLNLTLDNRVADQLWVPDTYFLNDKKSF
VHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGGDNAV
TGVTKIELPQFSIVDYKLITKNVVFSTGSYPRLSLSFKLKRN
>gnl|CDD|349843 cd19042, LGIC_ECD_GABAAR_B3, extracellular domain of gamma-aminobutyric acid receptor subunit beta-3 (GABAAR-B3 or GABRB3). This family contains extracellular domain (ECD) of gamma-aminobutyric acid receptor beta-3 subunit, a protein that is encoded by the GABRB3 gene. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. The beta-3 subunit forms heteropentamers with other GABAAR subunits, with alpha2-beta3-gamma2 and alpha3-beta3-gamma2 subtypes highly enriched in hippocampal pyramidal neurons and cholinergic neurons of the basal forebrain, respectively. Other heteromers include alpha1-beta3-gamma2 and alpha5-beta3-gamma2. GABRB3 mutations are likely associated with a broad phenotypic spectrum of epilepsies and that reduced receptor function causing GABAergic disinhibition represents the relevant disease mechanism. GABRB3 might be associated with heroin dependence, and increased expression possibly contributing to the pathogenesis of heroin dependence. This gene may also be associated with the pathogenesis of other disorders such as Angelman syndrome, Prader-Willi syndrome, nonsyndromic orofacial clefts, schizophrenia, and autism
PVCVGMNIDIASIDMVSEVNMDYTLTMYFQQYWRDKRLAYSGIPLNLTLDNRVADQLWVPDTYFLNDKKS
FVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGGDKA
VTGVERIELPQFSIVEHRLVSRNVVFATGAYPRLSLSFRLKRN
>gnl|CDD|349844 cd19043, LGIC_ECD_GABAAR_G1, extracellular domain of gamma-aminobutyric acid receptor subunit gamma-1 (GABAAR-G1 or GABRG1). This family contains extracellular domain of gamma-aminobutyric acid receptor subunit gamma-1 (GABAAR-G1), a protein that is encoded by the GABRG1 gene in humans, clustered with the alpha2 gene GABRA2, which is associated with alcohol dependence. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. The gamma-1 subunit forms heteropentamers with other GABAAR subunits, likely expressed as combination of alpha1/2-beta-gamma1 subunits. A variant in GABRG1 shows the strongest statistical evidence of association of recovery from eating disorders. Studies show that upregulating or preserving GABAA gamma1/3 and gamma2 receptors may protect neurons against neurofibrillary pathology in Alzheimer's disease
TVIETDVYVNSIGPVDPINMEYTIDIIFAQTWFDSRLKFNSTMKVLMLNSNMVGKIWIPDTFFRNSRKSD
AHWITTPNRLLRIWSDGRVLYTLRLTINAECYLQLHNFPMDEHSCPLEFSSYGYPKNEIEYKWKKPSVEV
ADPKYWRLYQFAFVGLRNSTEISHTISGDYIIMTIFFDLSRR
>gnl|CDD|349845 cd19044, LGIC_ECD_GABAAR_G2, extracellular domain of gamma-aminobutyric acid receptor subunit gamma-2 (GABAAR-G2 or GABRG2). This family contains extracellular domain of gamma-aminobutyric acid receptor subunit gamma-2 (GABAAR-G2), a protein that is encoded by the GABRG2 gene in humans. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. The gamma-2 subunit forms heteropentamers with other GABAAR subunits, most prevalently expressed as alpha1-beta2-gamma2. The gamma2 subunit also coassembles with other alpha and beta variants in the brain, but these receptors are found in considerably less abundance and are restricted in their regional, e.g. the alpha2-beta3-gamma2 and alpha3-beta3-gamma2 subtypes are highly enriched in hippocampal pyramidal neurons and cholinergic neurons of the basal forebrain, respectively. Pathogenic missense and truncating variants in this gene have been associated with spectrum of epilepsies, from Dravet syndrome to milder simple febrile seizures, while a recurrent GABRG2 missense variant is associated with early-onset seizures, significant motor and speech delays, intellectual disability, hypotonia, movement disorder, dysmorphic features, and vision/ocular issues
KPTVIHTDMYVNSIGPVNAINMEYTIDIFFAQTWYDRRLKFNSTIKVLRLNSNMVGKIWIPDTFFRNSKK
ADAHWITTPNRMLRIWNDGRVLYTLRLTIDAECQLQLHNFPMDEHSCPLEFSSYGYPREEIVYQWKRSSV
EVGDTRSWRLYQFSFVGLRNTTEVVKTTSGDYVVMSVYFDLSRR
>gnl|CDD|349846 cd19045, LGIC_ECD_GABAAR_G3, extracellular domain of gamma-aminobutyric acid receptor subunit gamma-3 (GABAAR-G3 or GABRG3). This family contains extracellular domain of gamma-aminobutyric acid receptor subunit gamma-3 (GABAAR-G3), a protein that is encoded by the GABRG3 gene in humans. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on the ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. The gamma-3 subunit forms heteropentamers with other GABAAR subunits, likely expressed as alpha1-beta3-gamma3. This subunit contains the benzodiazepine binding site. Polymorphisms in GABG3 show consistent evidence of alcohol dependence
TVIDVDIYVNSIGPVSSINMEYQIDIFFAQTWTDSRLRFNSTMKILTLNSNMVGLIWIPDTIFRNSKTAE
AHWITTPNQLLRIWNDGKILYTLRLTINAECQLQLHNFPMDEHSCPLIFSSYGYPKEEMIYRWRKNSVEA
ADQKSWRLYQFDFMGLRNTTEIVTTSAGDYVVMTIYFELSRR
>gnl|CDD|349847 cd19046, LGIC_ECD_GABAAR_rho1, extracellular domain of gamma-aminobutyric acid receptor subunit rho-1 (GABA-rho1 or GABRR1). This family contains extracellular domain (ECD) of the rho subunit 1 of type-A gamma-aminobutyric acid receptor (GABAAR), encoded by the GABRR1 gene, expressed in many areas of the brain, but especially high in the retina. GABRR1 exists next to GABRR2 (encoding rho subunit 2) on the chromosome region thought to be associated with susceptibility for psychiatric disorders and epilepsy. Close proximity of the rho1 and rho2 subunit genes suggests that they emerged via a local duplication event. This subunit homo-oligomerizes to form GABAA-rho receptors (formerly classified as GABA-rho or GABAc receptor), but does not co-assemble with any of the classical GABAAR subunits. In humans, mutations in the GABRR1 gene may be responsible for some cases of autosomal recessive retinitis pigmentosa. Variation in GABRR1 is also associated with susceptibility to bipolar schizoaffective disorder, and may be associated with alcohol dependency
AIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLSFPSTNNQSMTFDGRLVKKIWVPDMFFVHSKR
SFIHDTTTDNVMLRVQPDGKVLYSLRVTVTAMCNMDFSRFPLDTQTCSLEIESYAYTEDDLMLYWKNGND
SLKTDERISLSQFLIQEFHTTTKLAFYSSTGWYNRLYINFTLRRHI
>gnl|CDD|349848 cd19047, LGIC_ECD_GABAAR_rho2, extracellular domain of gamma-aminobutyric acid receptor subunit rho-2 (GABA-rho2 or GABRR2). This family contains extracellular domain (ECD) of the rho subunit 2 of type-A gamma-aminobutyric acid receptor (GABAAR), encoded by the GABRR2 gene which exists next to GABRR1 (encoding rho subunit 1) on the chromosome region thought to be associated with susceptibility for psychiatric disorders and epilepsy. Close proximity of the rho1 and rho2 subunit genes suggests that they emerged via a local duplication event. Rho1 is expressed in many areas of the brain, but especially high in the retina. This subunit homo-oligomerizes to form GABAA-rho receptors (formerly classified as GABA-rho or GABAc receptor), but does not co-assemble with any of the classical GABAAR subunits. In humans, mutations in the GABRR2 gene may be responsible for some cases of autosomal recessive retinitis pigmentosa. Variation in GABRR2 is also associated with susceptibility to bipolar schizoaffective disorder, as well as alcohol dependence and general cognitive ability. GABA-rho2 receptors expressed pre-synaptically in the spinal dorsal horn have been implicated in pain perception and identified as a novel target for analgesia
AIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLSFPSTTNKSMTFDGRLVKKIWVPDVFFVHSKR
SFIHDTTTDNIMLRVFPDGHVLYSMRITVTAMCNMDFSRFPLDSQTCSLELESYAYTDEDLMLYWKNGNE
SLKTDEKISLSQFLIQKFHTTSRLAFYSSTGWYNRLYINFTLRRHI
>gnl|CDD|349849 cd19048, LGIC_ECD_GABAAR_rho3, extracellular domain of gamma-aminobutyric acid receptor subunit rho-3 (GABAA-rho3). This family contains extracellular domain (ECD) of the rho subunit 3 of type-A gamma-aminobutyric acid receptor (GABAAR), encoded by the GABRR3 gene which maps to a different chromosome to that of GABRR1 and GABRR2. While close proximity of the rho1 and rho2 subunit genes suggests that they emerged via a local duplication event, GABRR3 may have arisen by duplication of a GABRR1/GABRR2 progenitor. This subunit homo-oligomerizes to form GABAA-rho receptors (formerly classified as GABA-rho or GABAc receptor), but does not co-assemble with any of the classical GABAAR subunits. In humans, some individuals contain a variant that is predicted to inactivate this gene product
PIPVGIDVQVESIDSISEVDMDFTMTLYLRHYWKDERLSFPSTKNKSMTFDGRLIKKIWVPDVFFVHSKR
SFIHDTTMENVMLRVYPDGNVLFSLRITVSAMCFMDFSRFPLDTQNCSLELESYAYNEDDLMLYWKHGNE
SLSTDEHISLSQFFIEEFSASSGLAFYSSTGWYNRLFINFALRRHI
>gnl|CDD|349851 cd19049, LGIC_TM_anion, transmembrane domain of anionic Cys-loop neurotransmitter-gated ion channels, includes GABAAR, GlyR and GluCl. This family contains transmembrane domain of type-A gamma-aminobutyric acid receptor (GABAAR) as well as glycine receptor (GlyR) subunits. Thus far, there are 18 vertebrate receptor subunits categorized in 7 families: alpha1-6, beta1-4, gamma1-4, delta, epsilon, theta, rho, and pi. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. GlyR, with a similar structure as GABAAR, is concentrated in the brain stem and spinal cord in the CNS and can be activated by glycine, beta-alanine, or taurine. It is selectively blocked by the high-affinity competitive antagonist strychnine, which causes death by asphyxiation. An autosomal dominant R271Q mutation in GLRA1 causes hyperekplexia (Startle disease or Stiff Baby Syndrome) by decreasing glycine sensitivity
YYLIQTYIPSILIVILSWVSFWIDPEAVPARVSLGITTVLTMTTQSSGVRSSLPKVSYVKAIDVWLGVCF
VFVFAALLEYAVVNYLKASKIDRISRILFPLAFLIFNIIYW
>gnl|CDD|349852 cd19050, LGIC_TM_bact, transmembrane domain of prokaryotic pentameric ligand-gated ion channels (pLGIC). This family contains transmembrane (TM) domain of bacterial pentameric ligand-gated ion channels (pLGICs) including ones from Gloeobacter violaceus (GLIC) and Erwinia chrysanthemi (ELIC). The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. Studies show that GLIC activation is inhibited by most general anaesthetics at clinical concentrations, including xenon which has been used in clinical practice as a potent gaseous anesthetic for decades. Xenon binding sites have been identified in three distinct regions of the TMD: in a large intra-subunit cavity, in the pore, and at the interface between adjacent subunits. Propofol, the drug used for induction and maintenance of general anesthesia, and desflurane, a negative allosteric modulator of GLIC bind at the entrance in the intra-subunit cavity. Alzheimer's drug memantine, which blocks ion conduction at vertebrate pLGICs by plugging the channel pore, has been shown to have similar potency in ELIC
YYIWKVILPLLLIVAMSWSVFWIDPESFGPQIGISVTSMLTLIAFNFLISNSLPRLPYLTFMDAFILASY
LLVFLALIEVIVTHYLARNGKEALALRIDRISRWAFPLAFLLVNLILAL
>gnl|CDD|349853 cd19051, LGIC_TM_cation, transmembrane domain of Cys-loop neurotransmitter-gated ion channels, includes 5HT3, nAChR, and ZAC. This superfamily contains the transmembrane (TM) domain of cationic Cys-loop neurotransmitter-gated ion channels, which include nicotinic acetylcholine receptor (nAChR), serotonin 5-hydroxytryptamine receptor (5-HT3), and zinc-activated ligand-gated ion channel (ZAC) receptor. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. The ligand-gated ion channels (LGICs) in this family are found across metazoans and have close homologs in bacteria. They are vital for communication throughout the nervous system. nAChR is a non-selective cation channel that is permeable to Na+ and K+, and some subunit combinations are also permeable to Ca2+. Na+ enters and K+ exits to allow net flow of positively charged ions inward. 5-HT3, a cation-selective channel, binds serotonin and is permeable to Na+, K+, and Ca2+. It mediates neuronal depolarization and excitation within the central and peripheral nervous systems. ZAC forms an ion channel gated by Zn2+, Cu2+, and H+ and is non-selectively permeable to monovalent cations. However, the role of ZAC in Zn2+, Cu2+, and H+ signaling require is as yet unknown
LFYVFNLILPCVLLSVLALLVFLLPPDSGEKVSLGITVLLSLTVFLLLVSESLPPTSDSVPLIGIYLLAT
MVLSALSTVLTVIVLNLHHVLDRLFFWLFLLVTVITTLVLFL
>gnl|CDD|349854 cd19052, LGIC_TM_GABAAR_alpha, transmembrane domain of alpha subunits of type-A gamma-aminobutyric acid receptor (GABAAR). This family contains transmembrane domain of type-A gamma-aminobutyric acid receptor (GABAAR) as well as glycine receptor (GlyR) subunits. Thus far, there are 18 vertebrate receptor subunits categorized in 7 families: alpha1-6, beta1-4, gamma1-4, delta, epsilon, theta, rho, and pi. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. GlyR, with a similar structure as GABAAR, is concentrated in the brain stem and spinal cord in the CNS and can be activated by glycine, beta-alanine or taurine. It is selectively blocked by the high-affinity competitive antagonist strychnine, which causes death by asphyxiation. An autosomal dominant R271Q mutation in GLRA1 causes hyperekplexia (Startle disease or Stiff Baby Syndrome) by decreasing glycine sensitivity
YFVIQTYLPCIMTVILSQVSFWLNKESVPARTVFGVTTVLTMTTLSISARNSLPKVSYATAMDWFIAVCF
AFVFSALIEFATVNYFGTSKIDKYSRILFPVLFGIFNLVYW
>gnl|CDD|349855 cd19053, LGIC_TM_GABAAR_beta, transmembrane domain of beta subunits of type-A gamma-aminobutyric acid receptor (GABAAR). This family contains transmembrane (TM) domain of the beta subunit of type-A beta-aminobutyric acid receptor (GABAAR), which includes beta1-beta4 in vertebrates. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. Mutations or genetic variations of the genes encoding beta2 (GABRB2) and beta3 (GABRB3) have been associated with human epilepsy, both with and without febrile seizures. Mutations in GABRB2, and GABRB3 have been associated with infantile spasms and Lennox-Gastaut syndrome. A de novo missense mutation of GABRB2 causes early myoclonic encephalopathy, a disease with a devastating prognosis, characterized by neonatal onset of seizures. Another de novo heterozygous missense variant in exon 4 of GABRB2 is associated with intellectual disability and epilepsy. Mutations in the GABRB1 gene encoding beta1 promote alcohol consumption through increased tonic inhibition
YFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCF
VFVFLALLEYAFVNYIDVNAIDRWSRIIFPITFSFFNLVYW
>gnl|CDD|349856 cd19054, LGIC_TM_GABAAR_gamma, transmembrane domain of gamma subunits of type-A gamma-aminobutyric acid receptor (GABAAR). This family contains transmembrane (TM) domain of the gamma subunit of type-A beta-aminobutyric acid receptor (GABAAR), which includes gamma1-gamma3 in vertebrates. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. Studies show upregulating or preserving GABAA gamma1/3 and gamma2 receptors may protect neurons against neurofibrillary pathology in Alzheimer's disease. Pathogenic missense and truncating variants in GABRG2 have been associated with spectrum of epilepsies, from Dravet syndrome to milder simple febrile seizures. Polymorphisms in GABG3 show consistent evidence of alcohol dependence
YFTIQTYIPCILTVVLSWVSFWINKDAVPARTSLGITTVLTMTTLSTIARKSLPKVSYVTAMDLFVSVCF
IFVFAALMEYGTLHYFRIAKIDSYSRIFFPTAFLLFNLVYW
>gnl|CDD|349857 cd19055, LGIC_TM_GABAAR_delta, transmembrane domain of delta subunits of type-A gamma-aminobutyric acid receptor (GABAAR). This family contains transmembrane (TM) domain of the delta subunit of type-A gamma-aminobutyric acid receptor (GABAAR), encoded by the gene GABRD. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. Receptors containing the delta subunit (GABRD) are expressed exclusively extra-synaptically (in the cortex, hippocampus, thalamus, striatum, and cerebellum) and mediate tonic inhibition. Studies suggest that delta subunits form heteropentamers in similar stoichiometry and arrangement as alpha/beta/gamma receptors, with the delta subunit replacing the gamma subunit (2alpha:2beta:1delta), although other stoichiometries have also been detected. The delta subunit is flexible in its positioning in the pentameric complex, producing receptors with diverse pharmacological properties. Mutations in GABRD have been associated with susceptibility to generalized epilepsy with febrile seizures, type 5. GABRD gene may also be associated with childhood-onset mood disorders
VYIIQSYMPSILLVAMSWVSFWISQAAVPARVSLGITTVLTMTTLMVSARSSLPRASAIKALDVYFWICY
VFVFAALVEYAFAHYNADYRRPIDADTIDVYARAVFPAAFAAVNIIYWVAY
>gnl|CDD|349858 cd19056, LGIC_TM_GABAAR_theta, transmembrane domain of theta subunits of type-A gamma-aminobutyric acid receptor (GABAAR). This family contains transmembrane (TM) domain of the theta subunit of type-A gamma-aminobutyric acid receptor (GABAAR). The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. GABA stimulates human hepatocellular carcinoma growth through overexpressed GABAA receptor theta subunit. Also, two autism spectrum disorder (ASD)-associated protein truncation variants have been identified in alpha 3 (GABRA3) and theta (GABRQ) genes
SYLVQVYWPTVLTTIASWISFWMNYDSSAARVTIGLTSMLILTTIDSHLRDKLPEISCIKAIDIYILVCL
FFVFLSLLEYVYINYLFYSDYVPKVDKWSRFLFPLAFGLFNIVYWPYH
>gnl|CDD|349859 cd19057, LGIC_TM_GABAAR_epsilon, transmembrane domain of epsilon subunits of type-A gamma-aminobutyric acid receptor (GABAAR). This family contains transmembrane (TM) domain of type-A gamma-aminobutyric acid receptor (GABAAR) subunits as well as glycine receptor (GlyR). Thus far, there are 18 vertebrate receptor subunits categorized in 7 families: alpha1-6, beta1-4, gamma1-4, delta, epsilon, theta, rho, and pi. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. GlyR, with a similar structure as GABAAR, is concentrated in the brain stem and spinal cord in the CNS and can be activated by glycine, beta-alanine, or taurine. It is selectively blocked by the high-affinity competitive antagonist strychnine, which causes death by asphyxiation. An autosomal dominant R271Q mutation in GLRA1 causes hyperekplexia (Startle disease or Stiff Baby Syndrome) by decreasing glycine sensitivity
FNAFQNYVPSSVTTMLSWVSFWIKKESAPARTSLGITSVLTMTTLGTFSRKNFPRVSYITALDFYIAICF
VFCFCALLEFAVLNFLIHVYRLDNYSRVIFPVTFFFFNVLYWVIC
>gnl|CDD|349860 cd19058, LGIC_TM_GABAAR_pi, transmembrane domain of pi subunits of type-A gamma-aminobutyric acid receptor (GABAAR). This family contains transmembrane (TM) domain of the pi subunit of type-A gamma-aminobutyric acid receptor (GABAAR), encoded my the gene GABRP. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. GABRP is expressed mainly in non-neuronal tissues such as the mammary gland, prostate gland, lung, thymus, and uterus. It is also highly expressed in certain types of cancer such as basal-like breast cancer and pancreatic ductal adenocarcinoma. GABRP is involved in inhibitory synaptic transmission in the central nervous system. Its assembly with other GABAAR subunits alters the sensitivity of recombinant receptors to modulatory agents such as pregnanolone. Studies suggest that polymorphisms in the GABRP gene may be associated with the susceptibility to systematic lupus erythematosus (SLE)
LYFILETYVPSTLLVVLSWVSFWISLSSVPARTCIGVTTVLSMTTLMMGSRTSLPNANCFIKAIDVYLGI
CFSFIFGALLEYAVAHYCSLVQNPSNVDNYSRLLFPLIFMLINVFYWAYYLYF
>gnl|CDD|349861 cd19059, LGIC_TM_GABAAR_rho, transmembrane domain of rho subunits of type-A gamma-aminobutyric acid receptor (GABAAR). This family contains transmembrane (TM) domain of the rho subunit of type-A gamma-aminobutyric acid receptor (GABAAR), which includes rho1-3. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. These rho subunits homo-oligomerize to form GABAA-rho receptors (formerly classified as GABA-rho or GABAC receptor) but do not co-assemble with any of the classical GABAA subunits. They are especially high expression in the retina and their distinctive pharmacological properties are unique; they are not modulated by many GABAA receptor modulators such as barbiturates, benzodiazepines, and neuroactive steroids. In humans, mutations in the rho-1 and rho genes, GABRR1 and GABRR2, may be responsible for some cases of autosomal recessive retinitis pigmentosa. Variation in GABRR1 is also associated with susceptibility to bipolar schizoaffective disorder while a SNP in GABRR2 has been reported to show association with autism
FFFLLQTYFPATLMVMLSWVSFWIDRRAVPARVSLGITTVLTMSTIITGVNASMPRVSYVKAVDIYLWVS
FVFVFLSVLEYAAVNYLNTHAIDKYSRIIFPGAYILFNLIYWS
>gnl|CDD|349862 cd19060, LGIC_TM_GlyR_alpha, transmembrane domain of alpha subunits of glycine receptor (GlyR). This family contains transmembrane (TM) domain of the alpha subunit of glycine receptor (GlyR or GLR) of the amino acid neurotransmitter glycine. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. GlyR has four known isoforms of the alpha-subunit (alpha1-4, encoded by GLRA1, GLRA2, GLRA3, GLRA4) that are essential to bind ligands and, along with the GlyR beta subunit, have been described to have a regionally and temporally controlled expression during development and maturation of the central nervous system (CNS). These alpha subunits are highly homologous but differ in their kinetic properties, temporal and regional expression and physiological functions. They can form functional chloride-permeable GlyR ion channels by forming homopentamers with 5 alpha subunits or heteropentamers with a combination of alpha and beta subunits, either a 2alpha-3beta or 3alpha-2beta stoichiometry. In human, mutations in glycine receptor alpha subunits cause disruption of GlyR surface expression or reduced ability of expressed GlyRs to conduct chloride ions. Mutations in GlyR alpha1 subunit leads to hyperekplexia, a rare neurological disorder characterized by neonatal hypertonia and exaggerated startle responses to unexpected stimuli, while mutations in GlyR alpha2 are known to cause cortical neuronal migration/autism spectrum disorder and in GlyR alpha3 to cause inflammatory pain sensitization/rhythmic breathing. GlyR alpha1 and alpha2 subunits have an important role in regulation of the excitatory-inhibitory balance, control of motor actions, modulation of sedative ethanol effects and probably regulation of ethanol preference and consumption
GYYLIQMYIPSLLIVILSWVSFWINMDAAPARVALGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVC
LLFVFSALLEYAAVNFVSRQDRAKRIDTISRAAFPLAFLIFNIFYWITYK
>gnl|CDD|349863 cd19061, LGIC_TM_GlyR_beta, transmembrane domain of beta subunits of glycine receptor (GlyR). This family contains transmembrane (TM) domain of the beta subunit of glycine receptor (GlyR or GLR) of the amino acid neurotransmitter glycine, encoded by GLRB gene. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. These subunits form heteropentamers with a combination of alpha and beta subunits, either a 2alpha-3beta or 3alpha-2beta stoichiometry. While the alpha subunits contain binding sites for agonists and antagonists and are responsible for ion channel formation, the beta subunit displays structural and regulatory functions, such as GlyR clustering in synaptic locations by interaction between intracellular loop domains with the scaffolding protein gephyrin, and control of pharmacologic responses to agonist or allosteric modulators due in part to the presence of interfaces alpha/beta and beta/beta. GLRB gene mutations are associated with the neurological disorder hyperekplexia, a rare neurological disorder characterized by neonatal hypertonia and exaggerated startle responses to unexpected stimuli, as well as agoraphobic cognitions
FYMMGVYAPTLLIVVLSWLSFWINPDASAARVPLGIFSVLSLASECTTLAAELPKVSYVKAIDVWLIACL
LFGFASLVEYAVVQVMAAKRIDLYARALFPFCFLFFNVIYWSVY
>gnl|CDD|349864 cd19062, LGIC_TM_GluCl, transmembrane domain of glutamate gated chloride channel (GluCl). This family contains transmembrane (TM) domain of the glutamate-gated chloride channel (GluCl) found only in protostomia but are closely related to mammalian glycine receptors. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. These GluCl channels have several roles in these invertebrates, including controlling locomotion and feeding, and mediating sensory inputs into behavior. Comparison of the GluCl gene families between organisms shows that insect gene family is relatively simple, while that found in nematodes tends to be larger and more diverse. Glutamate is an inhibitory neurotransmitter that shapes the responses of projection neurons to olfactory stimuli in the Drosophila. GluCls are targeted by the macrocyclic lactone family of anthelmintics and pesticides in arthropods and nematodes, thus making the GluCls of considerable medical and economic importance. In Drosophila melanogaster, GluCl mediates sensitivity to the antiparasitic agents ivermectin and nodulisporic acid, suggesting that their drug target is the same throughout the Ecdysozoa
FYLLQLYIPSCMLVIVSWVSFWIDWTAVPGRVTLGVTTLLTMTTQSAGINAKLPPVSYIKAIDVWIGACV
TFVFGALLEFAFVNYAGNRAKRIDLISRILFPLLFLVFNIVYWSTY
>gnl|CDD|349865 cd19063, LGIC_TM_5-HT3, transmembrane domain of 5-hydroxytryptamine 3 (5-HT3) receptor. This family contains transmembrane (TM) domain of the serotonin 5-HT3 receptors. The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. The 5-HT3 channel is cation-selective and mediates neuronal depolarization and excitation within the central and peripheral nervous systems. Like other ligand gated ion channels, the 5-HT3 receptor consists of five subunits arranged around a central ion conducting pore, which is permeable to Na+, K+, and Ca2+ ions. Binding of the neurotransmitter 5-hydroxytryptamine (serotonin) to the 5-HT3 receptor opens the channel, which then leads to an excitatory response in neurons, and the rapidly activating, desensitizing, inward current is predominantly carried by Na+ and K+ ions. This receptor is most closely related by homology to the nicotinic acetylcholine receptor (nAChR). Five subunits have been identified for this family: 5-HT3A, 5-HT3B, 5-HT3C, 5-HT3D, and 5-HT3E, encoded by HTR3A-E genes. Only 5-HT3A subunits are able to form functional homomeric receptors, whereas the 5-HT3B, C, D, and E subunits form heteromeric receptors with 5-HT3A. Different receptor subtypes are important mediators of nausea and vomiting during chemotherapy, pregnancy, and following surgery, while some contribute to neuro-gastroenterologic disorders such irritable bowel syndrome (IBS) and eating disorders as well as co-morbid psychiatric conditions. 5-HT3 receptor antagonists are established treatments for emesis and IBS, and are beneficial in the treatment of psychiatric diseases
LLYVVNLLIPSIFLMLVDLASFYLPPNSGERLGFKVTLLLGYSVFLLILNDLLPATAIGTPLIGVYFVVC
LALMVLSLLETILIVKLLHWLRVAYVLDRLLFRLYLLTVLAYAITLGLLWA
>gnl|CDD|349866 cd19064, LGIC_TM_nAChR, transmembrane domain of nicotinic acetylcholine receptor (nAChR). This family contains transmembrane (TM) domain of the nicotinic acetylcholine receptor (nAChR). The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. nAChR is found in high concentrations at the nerve-muscle synapse, where it mediates fast chemical transmission of electrical signals in response to the endogenous neurotransmitter acetylcholine (ACh) released from the nerve terminal into the synaptic cleft. Thus far, seventeen nAChR subunits have been identified, including ten alpha subunits, four beta subunits and one gamma, delta, and epsilon subunit each, all found on the cell membrane that non-selectively conducts cations (Na+, K+, Ca++). These nAChR subunits combine in several different ways to form functional nAChR subtypes which are broadly categorized as either muscle subtype located at the neuromuscular junction or neuronal subtype that are found on neurons and on other cell types throughout the body. The muscle type of nAChRs are formed by the alpha1, beta1, gamma, delta, and epsilon subunits while the neuronal type are composed of nine alpha subunits and three beta subunits, which combine in various permutations and combinations to form functional receptors. Among various subtypes of neuronal nAChRs, the homomeric alpha7 and the heteromeric alpha4beta2 receptors are the main subtypes widely distributed in the brain and implicated in the pathophysiology of neurodevelopmental disorders such as schizophrenia and autism and neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease. Among subtypes of muscle nAChRs, the heteromeric subunits (alpha1)2, beta, gamma, and delta in fetal muscle, and the gamma subunit replaced by epsilon in adult muscle have been implicated in congenital myasthenic syndromes and multiple pterygium syndromes due to various mutations. This family also includes alpha- and beta-like nAChRs found in protostomia
LFYTVNLIIPCVLISFLTVLVFYLPADSGEKITLSISVLLALTVFLLLIAEIIPPTSLVVPLIGKYLLFT
MILVTLSIIVTVIVLNVHHRVIDRLFLWIFLLVCVIGTLGIFL
>gnl|CDD|349867 cd19065, LGIC_TM_ZAC, transmembrane domain of zinc-activated ligand-gated ion channel. This family contains transmembrane (TM) domain of zinc-activated ligand-gated ion channel (ZAC). The transmembrane region consists of four transmembrane-spanning alpha-helical segments (M1-M4) that are linked by loops. The intracellular loop that links M1 and M2 determines the ion selectivity of the channel. ZAC displays low sequence similarity to other members in the superfamily, with closest matches to the human serotonin 5-HT3 receptor (5-HT3R) subunits 5-HT3A and 5-HT3B, and nAChR alpha7 subunits that exhibit approximately 15% amino acid sequence identity to ZAC. Expression of ZAC has been detected in human fetal whole brain, spinal cord, pancreas, placenta, prostate, thyroid, trachea, and stomach, as well as in adult hippocampus, striatum, amygdala, and thalamus. ZAC forms an ion channel gated by Zn2+, Cu2+, and H+, and is non-selectively permeable to monovalent cations. However, the role of ZAC in Zn2+, Cu2+, and H+ signaling is as yet unknown
LKAIIALLVPGEALLLADVCGGLLPLRATERIAYKVTLLLSYLVFHSSLVQALPSSSSCNPLLIYYFTVL
LLLLFLSTIETVLLAGLLARGNLGAKSSPSPAPRGEQREHGNPGPHPEEAPGRGKGSQRSWAEAADRIFF
LVYVVGVLCSQFVFIGIWMWATCKSDPAPGEAAPHG
>gnl|CDD|380453 cd19066, C_NRPS-like, Condensation domain of nonribosomal peptide synthetases (NRPSs). Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity
KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVV
LDKTVRFRIEIIDLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGG
SFQILFEDISSVYDAAERQKPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAK
RPSQVASYEVLTLEFFLRSEETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEA
VEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFT
FKNNQQQLGKTGGFIFTTPVYTSSEGTVFDLDLEASEDPDGDLLLRLEYSRGVYDERTIDRFAERYMTAL
RQLIENP
>gnl|CDD|410989 cd19067, PfuEndoQ-like, lesion-specific endonuclease similar to Pyrococcus furiosus EndoQ. Pyrococcus furiosus EndoQ is a lesion-specific endonuclease which is assumed to be involved in DNA repair pathways in Thermococcales. It recognizes a deaminated base and hydrolyzes the phosphodiester bond 5' to the site of the lesion. Initially identified as a hypoxanthine-specific endonuclease, it has now been shown that EndoQ also recognizes uracil, xanthine, and apurinic/apyrimidinic (AP) sites in DNA, and that a homolog in Bacillus pumilus shares functional properties of the archaeal EndoQs
IADLHIHSGYSRATSKVLTLENIAEWAKLKGIDLVGTGDFTHPEWLKELKEKLEEGELGLLKLGGGRGVR
FILTTEISIIYTKGGKGRRVHHLIFFPSLEAAEKFNKWLSKRGNLISDGRPILGLSARELLEIVLEIDPD
GLIIPAHIWTPWFSLYGSKSGFDSLEECFGDLTKHIDAIETGLSSDPAMAWRISELDRYTFLSNSDAHSP
PKIGREANVFELEEPSYKEIKKALKRKDGRKILATIEFFPEEGKYHRTGHRKCGVSLSPEETKKLNGICP
VCGKPLTKGVLDRVEELADRPEGFHPPNRPPYIHLVPLEEIIAEALGVGPNSKKVKKTYEKLLERFGTEM
NILLDAPEEELAKVVGEKIAEAIIRAREGKLKIEPGGDGVYGKVK
>gnl|CDD|381297 cd19071, AKR_AKR1-5-like, AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins
MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGY
ERVREALEESLKDLGLDYLDLYLIHWPVPGKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEE
LLAAARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRPLLDDPVLKEIAKKYGKTPAQVL
LRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID
>gnl|CDD|381298 cd19072, AKR_AKR3F1-like, Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins. Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor
GEEVPVLGLGTWGIGGGMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDREDL
FITTKVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNF
SLEELEEAQSYLKKGPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPLLDEIA
KKYGKTPAQIALNWLISKPNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD
>gnl|CDD|381299 cd19073, AKR_AKR3F2_3, Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins. Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase
IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRP
EDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP
LPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKG
IVVIPKASSEDHLKENLAIFDWELTSEDVAKID
>gnl|CDD|381300 cd19074, Aldo_ket_red_shaker-like, Shaker potassium channel beta subunit family and similar proteins. This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit
GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRESYVIST
KVFWPTGPGPNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWG
TSEWSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRD
GIPPPSRSRATDEDNRDKKRRLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPE
QLEENVKASGVKLSPEV
>gnl|CDD|381301 cd19075, AKR_AKR7A1-5, AKR7A family of aldo-keto reductase (AKR). Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol
PKIILGTMTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGERGFKIDTKANP
GVGGGLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEV
AEIVEICKENGWVLPTVYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDKAGGGR
FDPNNALGKLYRDRYWKPSYFEALEKVEEAAEKEGISLAEAALRWLYHHSALDGEKGDGVILGASSLEQL
EENLAALEKGPLPEEVVKAIDEAW
>gnl|CDD|381302 cd19076, AKR_AKR13A_13D, AKR13A and AKR13D families of aldo-keto reductase (AKR). Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6
PTRKLGTQGLEVSALGLGCMGMSAFYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD
RRDEVVIATKFGIVRDPGSGFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAE
LVEEGKVRYIGLSEASADTIRRAHAVHPITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLT
GAIKSPEDLPEDDFRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKR
IKYLEENVGALDVVLTPEELAEI
>gnl|CDD|381303 cd19077, AKR_AKR8A1-2, AKR8A family of aldo-keto reductase (AKR). Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+)
NGKLVGPIGLGLMGLTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHANLKLLARFFRKYPEY
ADKVVLSVKGGLDPDTLRPDGSPEAVRKSIENILRALGGTKKIDIFEPARVDPNVPIEETIKALKELVKE
GKIRGIGLSEVSAETIRRAHAVHPIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRI
KSLADIPEGDFRRHLDRFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIPIPGSTTLE
RVEENLKAANVELTDEELKEIN
>gnl|CDD|381304 cd19078, AKR_AKR13C1_2, AKR13C family of aldo-keto reductase (AKR). The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides
GLEVSAIGLGCMGMSHGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRDQVVI
ATKFGFKIDGGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGK
IRHWGLSEAGVETIRRAHAVCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDEN
TKFDEGDDRASLPRFTPEALEANQALVDLLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEE
NIGAADIELTPEELREIEDAL
>gnl|CDD|381305 cd19079, AKR_EcYajO-like, Escherichia coli YajO and similar proteins. Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase
EYVRLGNSGLKVSRLCLGCMSFGDPKWRPWVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRA
LKEFAPRDEVVIATKVYFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEA
LHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPW
SPLARGRLARPWGDTTERRRSTTDTAKLKYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVT
APIVGATKLEHLEDAVAALDIKLSEEEIKYLE
>gnl|CDD|381306 cd19080, AKR_AKR9A_9B, AKR9A and AKR9B families of aldo-keto reductase (AKR). The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively
RLLGRSGLRVSPLALGTMTFGTEWGWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGN
RDRIVLATKYTMNRRPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLV
RAGKVLYVGISDTPAWVVARANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGG
GLLTGKYQRGEEGRAGEAKGVTVGFGKLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIG
ARTLEQLKDNLGALDLTLSPEQLARLD
>gnl|CDD|381307 cd19081, AKR_AKR9C1, AKR9C family of aldo-keto reductase (AKR). Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1)
PLGRTGLSVSPLCLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSAWVPGNAGGESETIIGRWLK
SRGKRDRVVIATKVGFPMGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDL
IRQGKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPL
AGGFLTGKYRSEADLPGSTRRGEAAKRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIA
GARTVEQLEDLLAAAGLRLTDEEVARLD
>gnl|CDD|381308 cd19082, AKR_AKR10A1_2, AKR10A family of aldo-keto reductase (AKR). Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR
SRIVLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGASERVIGEWLKSRGNRDKVVIAT
KGGHPDLEDMSRSRLSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFG
ASNWSTERIAEANAYAKAHGLPGFAASSPQWSLARPNEPPWPGPTLVAMDEEMRAWHEENQLPVFAYSSQ
ARGFFSKRAAGGAEDDSELRRVYYSEENFERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTP
EQLRDSLAAAD
>gnl|CDD|381309 cd19083, AKR_AKR11A1_11D1, AKR11A and AKR11D families of aldo-keto reductase (AKR). Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1)
KVKLGKSDIDVNPIGLGTNAVGGHNLYPNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK
EYNRNEVVIATKGAHKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQE
LKDEGKIRAIGVSNFSLEQLKEANKDGYVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLA
GKYTKDTKFPDNDLRNDKPLFKGERFSENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKR
AEQVIDNLKALDVTLTEEEIAFIDALF
>gnl|CDD|381310 cd19084, AKR_AKR11B1-like, AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR). Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization
DLKVSRIGLGTWAIGGTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDDVVI
ATKCGLRWDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIR
YIGVSNFSVEQLEEARKYGPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPT
FPPDDRRSRFPFFRGENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENA
GALDWELTEEELKEID
>gnl|CDD|381311 cd19085, AKR_AKR11B3, Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins. Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification
VSRLGLGCWQFGGGYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRDDVVIAT
KVSPDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQ
LEEALDAGRIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGDARTRLF
RHFEPGAEEETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPS
VLERLDEISDPL
>gnl|CDD|381312 cd19086, AKR_AKR11C1, AKR11C family of aldo-keto reductase (AKR). Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase
LEVSEIGFGTWGLGGDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGRRDKVVIA
TKFGNRFDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEVLDNDELFEALEKLKQEGKIR
AYGVSVGDPEEALAALRRGGIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGKLAQAAL
RFILSHPAVSTVIPGARSPEQVEENAAA
>gnl|CDD|381313 cd19087, AKR_AKR12A1_B1_C1, AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR). Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase
MEYRTLGRTGLKVSRLCLGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRR
DDIVLATKVFGPMGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQ
GKIRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGL
LTGKYGKGKRPESGRLVERARYQARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGP
RTLEQLEDSLAALEITLTPELLAEIDELFP
>gnl|CDD|381314 cd19088, AKR_AKR13B1, AKR13B family of aldo-keto reductase (AKR). Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid
VSRLGYGAMRLTGPGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYPDDVVIA
TKGGLVRTGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRH
IGLSNVTVAQIEEARAIVRIVSVQNRYNLANRDDEGVLDYCEAAGIAFIPWFPLGGGDLAQPGGLLAEVA
ARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS
>gnl|CDD|381315 cd19089, AKR_AKR14A1_2, AKR14A family of aldo-keto reductase (AKR). Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor
YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPPPGSAEENFGRILKRD
LRPYRDELVISTKAGYGMWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALA
DAVRSGKALYVGISNYPGAKARRAIALLRELGVPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPL
AQGLLTDKYLNGIPPDSRRAAESKFLTEEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSV
LIGASSPSQLEDNVAALKNLDFSEEELA
>gnl|CDD|381316 cd19090, AKR_AKR15A-like, AKR15A family of aldo-keto reductase and similar proteins. The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+)
SALGLGTAGLGGVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDSEERLGLALAELPREPLVLSTKVGR
LPEDTADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPGGALEALLELKEEGLIKHIGLG
GGPPDLLRRAIETGDFDVVLTANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRYTY
RWLSPELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEELW
>gnl|CDD|381317 cd19091, AKR_PsAKR, Polaromonas Sp. aldo-keto reductase and similar proteins. The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp
MEYRTLGRSGLKVSELALGTMTFGGGGGFFGAWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEI
LGKALKGRRDDVLIATKVRGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETL
RALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLL
VWSPLAGGLLSGKYRRGQPAPEGSRLRRTGFDFPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSR
PTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLDKVS
>gnl|CDD|381318 cd19092, AKR_BsYcsN_EcYdhF-like, Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins. Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases
PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKI
EIQTKCGIRLGDDPRPGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELV
KSGKVRYFGVSNFTPSQIELLQSYLDQPLVTNQIELSLLHTEAIDDGTLDYCQLLDITPMAWSPLGGGRL
FGGFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTREEWY
EIYEAAR
>gnl|CDD|381319 cd19093, AKR_AtPLR-like, Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins. Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway
EVSPLGLGTWQWGDRLWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRDE
VVIATKFAPLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEALMDGLADAVEEGLVRAVG
VSNYSADQLRRAHKALKERGVPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYSP
ENPPPGGRRRLFGRKNLEKVQPLLDALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGAL
GWRLSEEEVAELD
>gnl|CDD|381320 cd19094, AKR_Tas-like, Escherichia coli Tas protein and similar proteins. Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor
VSEICLGTMTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPVPPSPETQGRTEEIIGSWLKKKGNRDKV
VLATKVAGPGEGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLFGGGYYTEPSEE
EDSVSFEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAE
ACHRENVGLLAYSPLAGGVLTGKYLDGAARPEGGRLNLFPGYMARYRSPQALEAVAEYVKLARKHGLSPA
QLALAWVRSRPFVTSTIIGATTLEQLKENIDAFDVPLSDELLAEIDAV
>gnl|CDD|381321 cd19095, AKR_PA4992-like, Pseudomona aeruginosa PA4992 and similar proteins. Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor
SVLGLGTSGIGRVWGVPSEAEAARLLNTALDLGINLIDTAPAYGRSEERLGRALAGLRRDDLFIATKVGT
HGEGGRDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGD
GEELEAAIASGVFDVVQLPYNVLDREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPE
FAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA
>gnl|CDD|381322 cd19096, AKR_Fe-S_oxidoreductase, Fe-S oxidoreductase and similar proteins. The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications
SVLGFGTMRLPESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPREKFYLATK
LPPWSVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNSPEWLEKARKGGLLEFLEKAKKEGLIRHIGFSF
HDSPELLKEILDSYDFDFVQLQYNYLDQENQAGRPGIEYAAKKGMGVIIMEPLKGGGLANNPPEALAILC
GAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAADEFEP
>gnl|CDD|381323 cd19097, AKR_unchar, uncharacterized aldo-keto reductase (AKR) superfamily protein. This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications
SKLALGTAQFGLDYGIANKSGKPSEKEAKKILEYALKAGINTLDTAPAYGDSEKVLGKFLKRLDKFKIIT
KLPPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDLLKHGGKLVEALLELKKEGLIRKIGVSV
YSPEELEKALESFKIDIIQLPFNILDQRFLKSGLLAKLKKKGIEIHARSVFLQGLLLMEPDKLPAKFAPA
KPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKPPL
>gnl|CDD|381324 cd19098, AKR_unchar, uncharacterized aldo-keto reductase (AKR) superfamily protein. This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications
PRLGLGLAALGRPGYINLGHAADLGSGRSVEAMRAHTHAVLDAAWAAGVRYFDAARSYGRAEEFLGSWLR
SRNIAPDAVFVGSKWGYTYTADWQVDAAVHEVKDHSLARLLKQWEETRSLLGKHLDLYQIHSATLESGVL
EDADVLAALAELKAEGVKIGLSLSGPQQAETLRRALEIEIDGARLFDSVQATWNLLEQSAGEALEEAHEA
GMGVIVKEALANGRLTDRNPSPELAPLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLR
SNLRALDVSLDLELLAALADLAEPPEDYWATRSALAWN
>gnl|CDD|381325 cd19099, AKR_unchar, uncharacterized aldo-keto reductase (AKR) superfamily protein. This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications
LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELIEKGGIKRDE
VVIVTKAGYIPGDGDEPLRPLKYLEEKLGRGLIDVADSAGLRHCISPAYLEDQIERSLKRLGLDTIDLYL
LHNPEEQLLELGEEEFYDRLEEAFEALEEAVAEGKIRYYGISTWDGFRAPPALPGHLSLEKLVAAAEEVG
GDNHHFKVIQLPLNLLEPEALTEKNTVKGEALSLLEAAKELGLGVIASRPLNQGQLLGELRLADLLALPG
GATLAQRALQFARSTPGVDSALVGMRRPEHVDENLA
>gnl|CDD|381326 cd19100, AKR_unchar, uncharacterized aldo-keto reductase (AKR) superfamily protein. This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications
YRRLGRTGLKVSRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDSEEKIGKALKGRRDKVFL
ATKTGARDYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVFGPGGALEALLEAKEEGKIRFIGIS
GHSPEVLLRALETGEFDVVLFPINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLDPEQA
LRYALSLPPVDVVIVGMDSPEELDENLA
>gnl|CDD|381327 cd19101, AKR_unchar, uncharacterized aldo-keto reductase (AKR) superfamily protein. This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications
TISRVINGMWQLSGGHGGIRDEDAAVRAMAAYVDAGLTTFDCADIYGPAEELIGEFRKRLRRERDAADDV
QIHTKWVPDPGELTMTRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPGYLDAAKHLAELQEEGKIRHL
GLTNFDTERLREILDAGVPIVSNQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYLGVPEP
TGPALETRSLQKYKLMIDEWGGWDLFQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEH
IDDNVRAFSFRLDDEDRAAIDAVL
>gnl|CDD|381328 cd19102, AKR_unchar, uncharacterized aldo-keto reductase (AKR) superfamily protein. This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications
LTTIGLGTWAIGGGGWGGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRDRPI
VATKCGLLWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKV
RAIGVSNFSVDQMKRCQAIHPIASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPER
VASLPADDWRRRSPFFQEPNLARNLALVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQID
ETVGAADLRLTPEELAEIEALL
>gnl|CDD|381329 cd19103, AKR_unchar, uncharacterized aldo-keto reductase (AKR) superfamily protein. This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications
DKKLPKIALGTWSWGSGGAGGDQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR
YPREDYIISTKFTPQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNPADVERWTPELIPLLKSGKVKHV
GVSNHNLAEIKRANEILAKAGVSLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYD
TKHPLPEGSGRAETYNPLLPQLEELTAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAAR
AASITLTDDEIKELEQLAD
>gnl|CDD|381330 cd19104, AKR_unchar, uncharacterized aldo-keto reductase (AKR) superfamily protein. This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications
KYRRFGRTGLKVSELTFGGGGIGGLMGRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKG
LPAGPYITTKVRLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLHNRIGDERDKPVGGTLSTTDVLGL
GGVADAFERLRSEGKIRFIGITGLGNPPAIRELLDSGKFDAVQVYYNLLNPSAAEARPRGWSAQDYGGII
DAAAEHGVGVMGIRVLAAGALTTSLDRGREAPPTSDSDVAIDFRRAAAFRALAREWGETLAQLAHRFALS
NPGVSTVLVGVKNREELEEAVAAEAAGPLPAENLARLEALW
>gnl|CDD|381331 cd19105, AKR_unchar, uncharacterized aldo-keto reductase (AKR) superfamily protein. This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications
MPYRTLGKTGLKVSRLGFGGGGLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRRDKVF
LATKASPRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLNEELLEALEKLKKEGKVRFIG
FSTHDNMAEVLQAAIESGWFDVIMVAYNFLNQPAELEEALAAAAEKGIGVVAMKTLAGGYLQPALLSVLK
AKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA
>gnl|CDD|381332 cd19106, AKR_AKR1A1-4, AKR1A family of aldo-keto reductase (AKR). The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid
LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKAVPREDLFV
TSKLWNTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAM
EKLVDKGLVKAIGLSNFNSRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPD
RPWAKPDEPVLLEEPKVKALAKKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMK
QLDALNRNWRYIVPMITVDGKRVPR
>gnl|CDD|381333 cd19107, AKR_AKR1B1-19, AKR1B family of aldo-keto reductase (AKR). The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity
GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKL
WCTFHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELV
DEGLVKAIGVSNFNHLQIERILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRP
WAKPEDPSLLEDPKIKEIAAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATI
LSFNRNWRACALLSCSSHKDYPFHAEY
>gnl|CDD|381334 cd19108, AKR_AKR1C1-35, AKR1C family of aldo-keto reductase (AKR). The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus
QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVK
REDIFYTSKLWCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLC
ATWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVA
YSALGSQRDKEWVDQNSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFE
FQLTSEDMKALDGLNRNLRYLPA
>gnl|CDD|381335 cd19109, AKR_AKR1D1-3, AKR1D family of aldo-keto reductase (AKR). The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites
GNSIPIIGLGTYSEPKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFY
CGKLWNTCHPPELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEAL
EACKDAGLVKSIGVSNFNRRQLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGT
CRDPIWVNVSSPPLLEDPLLNSIGKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEE
EMKDIEALNKNVRYVELLMWRDHPEYPF
>gnl|CDD|381336 cd19110, AKR_AKR1E1-2, AKR1E family of aldo-keto reductase (AKR). The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR
MEDIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKL
WCTCHKKSLVKTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLV
IEGLVKNIGVSNFNHEQLERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEG
VDLIDDPVIQRIAKKHGKSPAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRN
LRLATFPITENHKDYPFHIEY
>gnl|CDD|381337 cd19111, AKR_AKR1G1_1I, Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins. CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications
GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKL
PPVYLEFKDTEKSLEKSLENLKLPYVDLYLIHHPCGFVNKKDKGERELASSDVTSVWRAMEALVSEGKVK
SIGLSNFNPRQINKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANQSLWPDQ
PDLLEDPTVLAIAKELDKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRN
MKYFDF
>gnl|CDD|381338 cd19112, AKR_AKR2A1-2, AKR2A family of aldo-keto reductase (AKR). The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis
STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKRED
LFITTKLWNSDHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKHTGVGTTGSALGEDGVLDIDVTISLET
TWHAMEKLVSAGLVRSIGISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTP
LGGAAANAEWFGSVSPLDDPVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLS
KEDMKLIKSLDRKYRTNQPAKFWGIDLY
>gnl|CDD|381339 cd19113, AKR_AKR2B1-10, AKR2B family of aldo-keto reductase (AKR). The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol
PDIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREE
LFLTSKLWNNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFVPIEEKYPPGFYCGDGDNFVYEDV
PILDTWKALEKLVDAGKIKSIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITIT
AYSSFGPQSFVELNQGRALNTPTLFEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNL
SVNDFDLTKEDFEEIAKLDIGLRFNDPWDW
>gnl|CDD|381340 cd19114, AKR_AKR2C1, AKR2C family of aldo-keto reductase (AKR). Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate
GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKL
WNNFHGKDHVREAFDRQLKDYGLDYIDLYLIHFPIPAAYVDPAENYPFLWKDKELKKFPLEQSPMQECWR
EMEKLVDAGLVRNIGIANFNVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGN
AVYTKVTKHLKHFTNLLEHPVVKKLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLD
EEDMEALYELEANARFNDPVVY
>gnl|CDD|381341 cd19115, AKR_AKR2D1, AKR2D family of aldo-keto reductase (AKR). Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner
ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKR
EDLFIVSKLWNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDPAVRYPPGWFYDGKKVEFSN
APIQETWTAMEKLVDKGLARSIGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAV
TAYSSFGPQSFLELDLPGAKDTPPLFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQN
LDVTGFDLEAEEIKAISALDIGLRFNNPLNY
>gnl|CDD|381342 cd19116, AKR_AKR2E1-5, AKR2E family of aldo-keto reductase (AKR). Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively
PTIKLNDGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKRE
DLFITTKLWNSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDSESNGDGSLSDIDYLETWRG
MEDLVKLGLTRSIGVSNFNSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRL
VPRGQTNPPPRLDDPTLVAIAKKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVA
ALNSFNTNQRVY
>gnl|CDD|381343 cd19117, AKR_AKR3A1-2, AKR3A family of aldo-keto reductase (AKR). Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal
PSSKTFKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEI
FITTKLWCTWHRRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKDDGTKDHEPDWDFIKTWE
LMQKLPATGKVKAIGVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPL
GSTNAPLLKEPVIIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFTLSDEEFKEIDELH
KEYG
>gnl|CDD|381344 cd19118, AKR_AKR3B1-3, AKR3B family of aldo-keto reductase (AKR). Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose
LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEPGVKREDLFI
TSKLWNNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLTAVPTNGGEVDLDLSVSLVD
TWKAMVELKKTGKVKSIGVSNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSP
LGNNLAGLPLLVQHPEVKAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVELSDDEFNAV
TAL
>gnl|CDD|381345 cd19119, AKR_AKR3C1, Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins. Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+)
EISFKLNTGASIPALGLGTASPHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIK
REELFITTKVWPTFYDEVERSLDESLKALGLDYVDLLLVHWPVCFEKDSDDSGKPFTPVNDDGKTRYAAS
GDHITTYKQLEKIYLDGRAKAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILV
TAYSPLGSHGAPNLKNPLVKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIVSLTKEDLQ
KLDDIGEKYPVRFI
>gnl|CDD|381346 cd19120, AKR_AKR3C2-3, Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin
GSKIPAIAFGTGTAWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFI
TTKVSPGIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFR
IEDLEELLDTAKIKPAVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPLSPLTRDAGGPLDPVLEKIAE
KYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQKHF
>gnl|CDD|381347 cd19121, AKR_AKR3D1, AKR3D family of aldo-keto reductase (AKR). Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH
MTSFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGGVKRED
LFVTTKLWSTYHRRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPTLPDGSRDLDWDWNHVDT
WKQMEKVLKTGKTKAIGVSNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPL
GSTGSPLISDEPVVEIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLDDEDMNKLNDI
>gnl|CDD|381348 cd19122, AKR_AKR3E1, AKR3E family of aldo-keto reductase (AKR). Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis
FTLNNGVKIPAVGFGTFANEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENPSVKRE
DLFICTKVWNHLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKLGPDGKYVILKDLTEN
PEPTWRAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEA
YSPLGSQNQVPSTGERVSENPTLNEVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELSD
EDFEAINQVAK
>gnl|CDD|381349 cd19123, AKR_AKR3G1, AKR3G family of aldo-keto reductase (AKR). Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols
MKTLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKRE
DLWITSKLWNNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGVGFPESGEDLLSLSPIPLEDTW
RAMEELVDKGLCRHIGVSNFSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLG
SGDRPAAMKAEGEPVLLEDPVINKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELD
ASDMATIAALDRHHRYV
>gnl|CDD|381350 cd19124, AKR_AKR4A_4B, AKR4A and AKR4B families of aldo-keto reductase (AKR). The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis
SGQTMPVIGMGTASDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKSRDELFV
TSKLWCSDAHPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFLPFDIKGVWEAMEEC
QRLGLTKAIGVSNFSCKKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKW
GSNAVMESDVLKEIAAAKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIP
Q
>gnl|CDD|381351 cd19125, AKR_AKR4C1-15, AKR4C family of aldo-keto reductase (AKR). The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops
RFFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKRED
LFITSKLWCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEPEEVLPPDIPSTWKAMEK
LVDSGKVRAIGVSNFSVKKLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTT
WVKKNVLKDPIVTKVAEKLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI
EQQRRVL
>gnl|CDD|381352 cd19126, AKR_AKR5A_5G, AKR5A and AKR5G families of aldo-keto reductase (AKR). The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis
VTLNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTT
KLWNDDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHL
EELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVV
LRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN
>gnl|CDD|381353 cd19127, AKR_AKR5B1, AKR5B family of aldo-keto reductase (AKR). Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine
ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTK
LWISDYGYDKALRGFDASLRRLGLDYVDLYLLHWPVPNDFDRTIQAYKALEKLLAEGRVRAIGVSNFTPE
HLERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASGPTGPGDVLQDPTIT
GLAEKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD
>gnl|CDD|381354 cd19128, AKR_GlAR-like, Giardia lamblia aldose reductase (AR) and similar proteins. Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies
PPRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPT
MHQPENVKEQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEK
LTKNIGVSNYSTKLLTDLLNYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNLTF
LNDSELKALATKYNTTPPQVIIAWHLQKWPKNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL
>gnl|CDD|381355 cd19129, AKR_BaDH-like, Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins. Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family
NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTT
KLWNTNHRPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDGVTLLDTWRAME
RLVDEGRCKAIGLSDVSLEKLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME
PKLLEDPVITAIARRVNKTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDISTLPEDAMREINEGIKTRY
RFNSVVETGVPGFIP
>gnl|CDD|381356 cd19130, AKR_AKR5C1, Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins. Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates
SIVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTT
KLWNDRHDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPP
HLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQ
IVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD
>gnl|CDD|381357 cd19131, AKR_AKR5C2, Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins. Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives
TITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITT
KLWNSDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQDKYVETWKALIELKKEGRVKSIGVSNFTIE
HLQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQ
VVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD
>gnl|CDD|381358 cd19132, AKR_AKR5D1_E1, AKR5D and AKR5E families of aldo-keto reductase (AKR). 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG)
LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLP
GRHHGYEEALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLD
RLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSGLLDEPVIKAIAEKHGKTPAQVV
LRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR
>gnl|CDD|381359 cd19133, AKR_AKR5F1, the AKR5F family of aldo-keto reductase (AKR). Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG)
VTLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITT
KLWIQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFGDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLV
DLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNNLFENPVLTEIAEKYGKSVAQV
ILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD
>gnl|CDD|381360 cd19134, AKR_AKR5H1, AKR5H family of aldo-keto reductase (AKR). Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal
PTVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVT
TKLATPDQGFTASQAACRASLERLGLDYVDLYLIHWPAGREGKYVDSWGGLMKLREEGLARSIGVSNFTA
EHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPA
QVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRFR
>gnl|CDD|381361 cd19135, AKR_CeZK1290-like, Caenorhabditis elegans ZK1290.5 and similar proteins. Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase
GTPTVRLSNGVEMPILGLGTSHSGGYSHEAVVYALKECGYRHIDTAKRYGCEELLGKAIKESGVPREDLF
LTTKLWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKNVKETRAETWRALEELYDEGLCRA
IGVSNFLIEHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELA
KKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSLH
>gnl|CDD|381362 cd19136, AKR_DrGR-like, Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins. Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal)
MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAP
KDQGYEKARAACLGSLERLGTDYLDLYLIHWPGVQGLKPSDPRNAELRRESWRALEDLYKEGKLRAIGVS
NYTVRHLEELLKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLRLLEDPTVLAIAKK
YGRTPAQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL
>gnl|CDD|381363 cd19137, AKR_AKR3F1, Thermotoga maritime Tm1743 and similar proteins. Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase
GEKIPALGLGTWGIGGFLTPDYSRDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPREDL
FIVTKVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNF
NRRLLEEAISKSQTPIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNY
GKTIAQIALAWLIQKPNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD
>gnl|CDD|381364 cd19138, AKR_YeaE, Escherichia coli YeaE and similar proteins. Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor
RTVTLPDGTKVPALGQGTWYMGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGRRD
KVFLVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETVAAMEELKKEGKIRAWGVSN
FDTDDMEELWAVPGGGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRRGLLENPTLK
EIAARHGATPAQVALAWVLRDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD
>gnl|CDD|381365 cd19139, AKR_AKR3F2, Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins. Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG)
IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSK
DKLLPSLEESLEKLRTDYVDLTLIHWPSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAV
VGAGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAM
ARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL
>gnl|CDD|381366 cd19140, AKR_AKR3F3, Sinorhizobium meliloti isatin reductase and similar proteins. Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase
VTVNGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKV
WPDNYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLR
EAVELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVAL
RWLLQQEGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL
>gnl|CDD|381367 cd19141, Aldo_ket_red_shaker, Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR). This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit
PYRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKG
WRRSSYVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVI
NQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLA
CGILSGKYDDGVPEYSRASLKGYQWLKEKILSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGV
SSVLLGASSTEQLYENLQAIQVLPKLTPNI
>gnl|CDD|381368 cd19142, AKR_AKR6B1, AKR6B family of aldo-keto reductase (AKR). Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase
LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKK
GWKRSSYIVSTKIYWSYGSEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLI
DNGLIMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLS
LGLDPGISEETRRLVTKLSFKSSKYKVGSDGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIAWSLKN
ENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEELERILDNKP
>gnl|CDD|381369 cd19143, AKR_AKR6C1_2, AKR6C family of aldo-keto reductase (AKR). Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit
MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKEL
GWPRSDYVVSTKIFWGGGGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMN
DLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWS
PLASGLLTGKYNNGIPEGSRLALPGYEWLKDRKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNP
NVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI
>gnl|CDD|381370 cd19144, AKR_AKR13A1, AKR13A family of aldo-keto reductase (AKR). Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor
IPTRTLGRNGPSVPALGFGAMGLSAFYGPPKPDEERFAVLDAAFELGCTFWDTADIYGDSEELIGRWFKQ
NPGKREKIFLATKFGIEKNVETGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAA
MAELVQEGKIKHIGLSECSAETLRRAHAVHPIAAVQIEYSPFSLDIERPEIGVLDTCRELGVAIVAYSPL
GRGFLTGAIRSPDDFEEGDFRRMAPRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIP
IPGTTKLKRLEENLGALKVKLTEEEEKEIREIAEEAEVVGERY
>gnl|CDD|381371 cd19145, AKR_AKR13D1, AKR13D family of aldo-keto reductase (AKR). Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6
PRVKLGSQGLEVSAQGLGCMGLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALK
DGPREKVQLATKFGIHEIGGSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELK
KLVEEGKIKYIGLSEASADTIRRAHAVHPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFF
AGKAKLEELLENSDVRKSHPRFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTT
KIKNLNQNIGALSVKLTKEDLKEI
>gnl|CDD|381372 cd19146, AKR_AKR9A1-2, Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins. Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis
RQLSPTAGVRVSPLCLGAMSFGEAWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEW
MASRGNRDEMVLATKYTTGYRRGGPIKIKSNYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSI
PELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEG
MALAPWGVLGQGQFRTEEEFKRRGRSGRKGGPQTEKERKVSEKLEKVAEEKGTAITSVALAYVMHKAPYV
FPIVGGRKVEHLKGNIEALGISLSDEEIQEIEDAYPFDVGFPMNFL
>gnl|CDD|381373 cd19147, AKR_AKR9A3_9B1-4, Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins. Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively
VLSKTAGIRVSPLILGAMSIGDAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWM
KSRKNRDQIVIATKFTTDYKAYEVGKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSI
EEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFG
MALAPWDVLGGGKFQSKKAVEERKKNGEGLRSFVGGTEQTPEEVKISEALEKVAEEHGTESVTAIALAYV
RSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE
>gnl|CDD|381374 cd19148, AKR_AKR11B1, Bacillus subtilis aldo-keto reductase YhdN and similar proteins. Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor
DLPVSRIALGTWAIGGWMWGGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGKRDRV
VIATKVGLEWDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGK
IRAIGVSNFSPEQMETFRKVAPLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKD
TKFEGDDLRRTDPKFQEPRFSQYLAAVEELDKLAQERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLD
AVDEVFGWSLNDEDMKEIDAIL
>gnl|CDD|381375 cd19149, AKR_AKR11B2, Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization
YRKLGKSGIEASVIGLGTWAIGGGPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIK
GRRDKVVLATKCGLRWDREGGSFFFVRDGVTVYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETP
IEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQA
YSPLEQGLLTGKITPDREFDAGDARSGIPWFSPENREKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPG
ITSALCGARKPEQAEENAKAGDIRLSAEDIATMRS
>gnl|CDD|381376 cd19150, AKR_AKR14A1, Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins. Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo
QYRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPPPGSAEENFGRILRE
DFAGYRDELIISTKAGYDMWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGAL
DHAVRSGKALYVGISSYSPERTREAAAILRELGTPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFT
PLAQGLLTDKYLNGIPEGSRASKERSLSPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTS
ALIGASRPEQLEENVGALDNLTFSADELA
>gnl|CDD|381377 cd19151, AKR_AKR14A2, Salmonella enterica aldo-keto reductase (AKR) and similar protein. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2)
KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPPPGSAEENFGRILKE
DLKPYRDELIISTKAGYTMWPGPYGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGAL
DQIVRQGKALYVGISNYPPEEAREAAAILKDLGTPCLIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSP
LAQGLLTDRYLNGIPEDSRAAKGSSFLKPEQITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTS
VLIGASKPSQIEDAVGALDNREFSEEELA
>gnl|CDD|381378 cd19152, AKR_AKR15A, AKR15A family of aldo-keto reductase. The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose
PKLGFGTAPLGNLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGREDYVISTKV
GRLLVPLQEVEPTFEPGFWNPLPFDAVFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDE
HFAQAIKGAFRALEELREEGVIKAIGLGVNDWEVILRILEEADLDWVMLAGRYTLLDHSAARELLPECEK
RGVKVVNAGPFNSGFLAGGDNFDYYEYGPAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVA
PGASSPERVEENVALLATEIPAAFWEEL
>gnl|CDD|381379 cd19153, AKR_galDH-like, L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins. L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+)
FGETLEIALGNVSPVGLGTAALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALA
ALQVPRSSYTVATKVGRYRDSEFDYSAERVRASVATSLERLHTTYLDVVYLHDIEFVDYDTLVDEALPAL
RTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSLDAVLSYCHLTLQDARLESDAPGLVRGAGPHVINASP
LSMGLLTSQGPPPWHPASGELRHYAAAADAVCASVEASLPDLALQYSLAAHAGVGTVLLGPSSLAQLRSM
LAAVDAVASLGAAI
>gnl|CDD|381380 cd19154, AKR_AKR1G1_CeAKR, Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins. CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor
SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKRE
DLFITTKLWTHEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDV
WRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATL
GSPGRANFTKSTGVSPAPNLLQDPIVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFD
FSLSEEDMATLEEIEKSLRLFLF
>gnl|CDD|381381 cd19155, AKR_AKR1I_CgAKR1, Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications
RNCVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKRE
ELFIVTKLPPGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSGKLDPTGEHKQDYTTDLL
DIWKAMEAQVDQGLTRSIGLSNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYA
PLGSPGAAHFSPGTGSPSGSSPDLLQDPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENF
QVFDFELTEADMAKLSSLDKNIRGRTF
>gnl|CDD|381382 cd19156, AKR_AKR5A1_2, AKR5A family of aldo-keto reductase (AKR). Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde
VKLANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTT
KLWNSDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHL
EELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVI
IRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRYGPDPDNF
>gnl|CDD|381383 cd19157, AKR_AKR5G1-3, AKR5G family of aldo-keto reductase (AKR). Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis
TVTLNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFIT
SKVWNADQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHH
LEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQV
ILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRVGPDPD
>gnl|CDD|381384 cd19158, AKR_KCAB2B_AKR6A1-like, voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins. KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability
QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKK
GWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHV
INQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPL
ACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEG
VSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILGNKPY
>gnl|CDD|381385 cd19159, AKR_KCAB1B_AKR6A3-like, voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins. KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits
MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKK
GWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHV
INQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPL
ACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEG
VSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP
>gnl|CDD|381386 cd19160, AKR_KCAB3B_AKR6A9-like, voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins. KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5
TGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILK
SKGWRRSSYVVTTKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMT
YVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWS
PLACGLITGKYDGRVPDTCRAAVKGYQWLKEKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRS
EGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDALLGNKP
>gnl|CDD|381387 cd19161, AKR_AKR15A1, Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins. Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal
SELGLGTAGLGNLYTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPRDEFVLSTKV
GRLLKPAREGSVPDPNGFVDPLPFEIVYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKER
HHFAQLMSGGFKALEELKKAGVIKAFGLGVNEVQICLEALDEADLDCFLLAGRYSLLDQSAEEEFLPRCE
QRGTSLVIGGVFNSGILATGTKSGAKFNYGDAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVAS
VLTGARNPAQLRQNVEAFQTDIPEELWQAL
>gnl|CDD|381388 cd19162, AKR_FDH, D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose
PRLGLGAASLGNLARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAEYVVSTKVG
RLLEPGAAGRPAGADRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLQALTDAFPALEELRAE
GVVGAIGVGVTDWAALLRAARRADVDVVMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATD
DPAGDRYDYRPATPEVLARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRT
PIPAEFWAEL
>gnl|CDD|381389 cd19163, AKR_galDH, L-galactose dehydrogenase (L-galDH) and similar proteins. L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+)
MKYRKLGKTGLKVSKLGFGASPLGGVFGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALK
GIPRDSYYLATKVGRYGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHDIEFAPSLDQILNETLP
ALQKLKEEGKVRFIGITGYPLDVLKEVLERSPVKIDTVLSYCHYTLNDTSLLELLPFFKEKGVGVINASP
LSMGLLTERGPPDWHPASPEIKEACAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNL
EAAEEPLDAHLLA
>gnl|CDD|381390 cd19164, AKR_ARA2, D-arabinose 1-dehydrogenase (ARA2) and similar proteins. ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+)
PVPKPVALSLAGLPPLIFGAATFSYQYTTDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIILGRALKA
LRDEFPRDTYFIITKVGRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVYLHDVEFVADEEVLEALKEL
FKLKDEGKIRNVGISGYPLPVLLRLAELARTTAGRPLDAVLSYCHYTLQNTTLLAYIPKFLAAAGVKVVL
NASPLSMGLLRSQGPPEWHPASPELRAAAAKAAEYCQAKGTDLADVALRYALREWGGEGPTVVGCSNVDE
LEEAVEAYWSVLAGASEE
>gnl|CDD|350856 cd19165, HemeO, heme oxygenase in eukaryotes and some bacteria. This subfamily contains heme oxygenase (HO, EC 1.14.14.18) found in eukaryotes as well as some proteobacteria, including cyanobacteria. Heme oxygenase (HO) catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling of iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. In vertebrates, HO plays a role in heme homeostasis and oxidative stress response, and cellular signaling in mammals that include isoforms HO-1, HO-2 and HO-3. HO-1 is ubiquitously expressed after induction while HO-2 expression is constitutive, mostly limited to certain organs, such as the brain, testes, and the vascular system. HO-3 is non-functional in humans, suggesting that the Hmox3 gene is a pseudogene derived from HO-2 transcripts. In higher plants and cyanobacteria, heme oxygenase is required for the synthesis of light-harvesting pigments, which contain tetrapyrrols derived from biliverdin. Candida albicans expresses a heme oxygenase that is required for the utilization of heme as a nutritional iron source, whereas Saccharomyces cerevisiae responds to iron deprivation by increasing Hmx1p transcription, which is controlled by the major iron-dependent transcription factor, Aft1p, and promotes both the re-utilization of heme iron and the regulation of heme-dependent transcription during periods of iron scarcity. In pathogenic bacteria, HO is part of a pathway for iron acquisition from host heme. In Leptospira interrogans, a pathogenic spirochete that causes leptospirosis, HO is required for iron utilization when hemoglobin is the sole iron source, thus making HO an interesting target for novel antimicrobial agents. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology
PLSERLREATRKLHTAAERSIFAKLLLAGPLDREAYARLLVQLYFVYEALEEALDRLADDPVLAAALYDP
ELERSEALEADLAFLLGPDWREPIPPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRKL
AKAYGLFGGEGLSFYDFDGIGDGKDLKDEYRARLDALELTEEEKDAIVEEAKLAFELNIALFEEL
>gnl|CDD|350857 cd19166, HemeO-bac, heme oxygenase found in pathogenic bacteria. This subfamily contains bacterial heme oxygenase (HO, EC 1.14.14.18), where HO is part of a pathway for iron acquisition from host heme and heme products. Most of these proteins have yet to be characterized. HO catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling of iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. This family includes heme oxygenase (pa-HO) from Pseudomonas aeruginosa, an opportunistic pathogen that causes a variety of systemic infections, particularly in those afflicted with cystic fibrosis, as well as cancer and AIDS patients who are immunosuppressed. Pa-HO, expressed by the PigA gene, is critical for the acquisition of host iron since there is essentially no free iron in mammals, and is unusual since it hydroxylates heme predominantly at the delta-meso heme carbon, while all other well-studied HOs hydroxylate the alpha-meso carbon. Also included in this family is Neisseria meningitidis HO which is substantially different from the human HO, with the reaction product being ferric biliverdin IXalpha rather than reduced iron and free biliverdin IXalpha. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology
LRARLRAATRAAHERLEALLGLLDLFLTLADYARFLAAQYGFYAPLEAALAAALLAALLPDLAARRRLPL
LAADLAALGLAPPAPAAAPLPALPSLAAALGALYVLEGSTLGGRVIARRLAKLLGLADFGARFLAGYGEG
TGARWRAFLAALEAAALTPADEDAAVAGARATFALFEAALAA
>gnl|CDD|380944 cd19167, SET_SMYD1_2_3-like, SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, SMYD2, SMYD3 and similar proteins. The family includes SET and MYND domain-containing proteins, SMYD1, SMYD2 and SMYD3. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex
GQVERFCSPGKGRGLRALKPFEPGDLIFSERPYAYVLTPPEHVRLTGRILYKQHIRKTRTSGKLLSVYDL
ESHVEKLDEEKKDGLRSDVATLHQFMSKDLQLPDAAYLVELFGKVNCNGFTISDEELQHVGVGIYPQAAL
LNHSCCPNCIVTFNGPNIEVRAVQEIEPGEEVFHSYIDLLYPTEERRDQLRDQYFFLCQCADCQT
>gnl|CDD|380945 cd19168, SET_EZH-like, SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb repressive complex 2 (PRC2), and similar proteins. The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both EZH1 and EZH2 can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics
KAVVLGKSQLECGLGLFAAEDIKEGEFVIEYTGELISHDEGVRREHRRGDVSYLYLFEEQEGIWVDAAIY
GNLSRYINHATDKVKTGNCMPKIMYVNHEWRIKFTAIKDIKIGEELFFNYGDNF
>gnl|CDD|380946 cd19169, SET_SETD1, SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and similar proteins. This family includes SET domain-containing protein 1A (SETD1A) and SET domain-containing protein 1B (SETD1B). These proteins are histone-lysine N-methyltransferases that specifically methylate 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated
DLLKFNQLKFRKKQLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEAIGIGSSYLF
RVDDDTIIDATKCGNLARFINHSCNPNCYAKIITVESQKKIVIYSKRPIAVNEEITYDYKFPIEDEKIPC
LCGAPQCR
>gnl|CDD|380947 cd19170, SET_KMT2A_2B, SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B) and similar proteins. This family includes KMT2A and KMT2B. Both KMT2A (also termed ALL-1 or CXXC7 or MLL or MLL1 or TRX1 or HRX) and KMT2B (also termed MLL4 or TRX2) act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me)
MAMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMF
RIDDDEVVDATMHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIEDVKIPC
TCGSKKCRKYLN
>gnl|CDD|380948 cd19171, SET_KMT2C_2D, SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), 2D (KMT2D) and similar proteins. This family includes KMT2C and KMT2D. Both, KMT2C (also termed HALR or MLL3) and KMT2D (also termed ALR or MLL2), act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me). They are subunits of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation
KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMF
RIDNDWVIDATMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKI
PCLCGAPNCRKWM
>gnl|CDD|380949 cd19172, SET_SETD2, SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and similar proteins. SETD2 (also termed HIF-1, huntingtin yeast partner B, huntingtin-interacting protein 1 (HIP-1), huntingtin-interacting protein B, lysine N-methyltransferase 3A or protein-lysine N-methyltransferase SETD2) acts as histone-lysine N-methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. It has been shown that methylation is a posttranslational modification of dynamic microtubules and that SETD2 methylates alpha-tubulin at lysine 40, the same lysine that is marked by acetylation on microtubules. Methylation of microtubules occurs during mitosis and cytokinesis and can be ablated by SETD2 deletion, which causes mitotic spindle and cytokinesis defects, micronuclei, and polyploidy
YAKVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYAREGNRHYYFMALKSDEIIDAT
KKGNLSRFINHSCEPNCETQKWTVNGELRVGFFAKRDIPAGEELTFDYQFERYGKEAQKCYCGSPNCRGY
IG
>gnl|CDD|380950 cd19173, SET_NSD, SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, NSD2, NSD3 and similar proteins. The nuclear receptor-binding SET Domain (NSD) family of histone H3 lysine 36 methyltransferases is comprised of NSD1, NSD2, and NSD3, which are primarily known to be involved in chromatin integrity and gene expression through mono-, di-, or tri-methylating lysine 36 of histone H3 (H3K36), respectively. NSD1 (EC 2.1.1.43; also termed histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), androgen receptor-associated protein of 267 kDa, H3-K36-HMTase, H4-K20-HMTase, lysine N-methyltransferase 3B (KMT3B) or NR-binding SET domain-containing protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD2 (EC 2.1.1.43; also termed multiple myeloma SET domain-containing protein (MMSET), protein trithorax-5 (TRX5), or wolf-Hirschhorn syndrome candidate 1 protein (WHSC1)) acts as histone-lysine N-methyltransferase with histone H3 'Lys-27' (H3K27me) methyltransferase activity. NSD3 (EC 2.1.1.43; also termed protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1L1), or WHSC1-like protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-4' and 'Lys-27' of histone H3
YPPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRLKKAHENNITNFYMLTLDKDRIIDAG
PKGNLSRFMNHSCQPNCETQKWTVNGDTRVGLFAVRDIPAGEELTFNYNLDCLGNEKKVCRCGAPNCSGF
LG
>gnl|CDD|380951 cd19174, SET_ASH1L, SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins. ASH1L (EC 2.1.1.43; also termed absent small and homeotic disks protein 1 homolog, KMT2H, or lysine N-methyltransferase 2H) acts as histone-lysine N-methyltransferase that specifically methylates 'Lys-36' of histone H3 (H3K36me). It plays important roles in development; heterozygous mutation of ASH1L is associated with severe intellectual disability (ID) and multiple congenital anomaly (MCA)
GLERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHHYCLNLDSGMVIDGYRMG
NEARFVNHSCDPNCEMQKWSVNGVYRIGLFALKDIPAGEELTYDYNFHSFNVEKQQPCKCGSPNCRGVIG
G
>gnl|CDD|380952 cd19175, SET_ASHR3-like, SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins. This family includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3, also termed protein SET DOMAIN GROUP 4 or protein stamen loss), ASH1 homolog 3 (ASHH3, also termed protein SET DOMAIN GROUP 7) and homolog 4 (ASHH4, also termed protein SET DOMAIN GROUP 24). They all function as histone-lysine N-methyltransferases (EC 2.1.1.43)
KMKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKGEKNFYMCEIDKDMVIDATFK
GNLSRFINHSCDPNCELQKWQVDGETRIGVFAIRDIKKGEELTYDYQFVQFGADQDCHCGSKNCRGKLG
>gnl|CDD|380953 cd19176, SET_SETD3, SET domain found in SET domain-containing protein 3 (SETD3) and similar proteins. SETD3 (EC 2.1.1.43) is a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and H3K36me). It functions as a transcriptional activator that plays an important role in the transcriptional regulation of muscle cell differentiation via interaction with MYOD1
EAFLEWLKDNGVSLSKVEIAFFEEEGYGLRATRDIKAGELLLSIPRKLMITAEAAKSSVLGPLIESDPIL
QAMPNVALALHLLCERSNPNSFWKPYIDILPSSYTTPLYFTPEELLLLKGSPAFEEAINQYRNIARQYAY
FYQLLQTSPLASKLNLRNSFTFDDYRWAVSTVMTRQNQIPTEDGTERSTLALIPLWDMCNHANGKITTDY
NLESDSLECVAMEDFKAGEQVFIFYGPRSNAELLLHSGFVP
>gnl|CDD|380954 cd19177, SET_SETD4, SET domain found in SET domain-containing protein 4 (SETD4) and similar proteins. SETD4 is a cytosolic and nuclear functional lysine methyltransferase that plays a crucial role in breast carcinogenesis. However, its specific substrates and modification sites remain to be disclosed
KSSKLKPAEFPDTGRGLVATKDIKPGELIISIPESLLINTTTVLSSLLGSLIKRVKPKLSSLQLLALFLA
LEKRRGENSFWAPYLDSLPKSFDTHPLYWSLEELSLLPPSLLEAVRKLLDKQKKRFESDWEIISSVLKSL
PSLFDSEIFTLEEFRWAWLCVNTRCVYYKLPLSDYLSSSEDNIALAPFLDLLNHSPDVNVKAGFNKSGKC
YEIRTGTDYKKGEEVFISYGPHSNDFLLLEYGFVL
>gnl|CDD|380955 cd19178, SET_SETD6, SET domain found in SET domain-containing protein 6 (SETD6) and similar proteins. SETD6 is a lysine N-methyltransferase that monomethylates 'Lys-310' of the RELA subunit of NF-kappa-B complex, leading to down-regulate NF-kappa-B transcription factor activity. It also monomethylates 'Lys-8' of H2AZ (H2AZK8me1)
IELSPKVAISKLGSSAGRGMVATEDIKEGEVLFTVPRSALLSPETSSIADLLEEEEDASLQSLSGWVPLL
LALMYEYTNPSSRWRPYLSLLPDFSELHHPMFWDEEEREELLGGTGIAEAVDRDLKEIDEEYNSIVLPFI
KKHPELFSPEKHSLELYKRMVAFVMAYSFTEPDEDEDDDDEDEDDDSPPMMVPMADMLNHIANNNARLEF
DPDCLRMIATRDIKKGEEIFNTYGELANWELLHMYGFVEP
>gnl|CDD|380956 cd19179, SET_RBCMT, SET domain found in chloroplastic ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase (RBCMT) and similar proteins. RBCMT (EC 2.1.1.127; also termed [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase, RuBisCO LSMT, RuBisCO methyltransferase, or rbcMT) methylates 'Lys-14' of the large subunit of RuBisCO
SHGLKADKVTVDEEAGGRGLVAARPIRRGERLLSVPESLWITAETAARSEIGGVLESGLKPWLALALFLL
RERSRGEASFWAPYIAVLPKEEELDSPLLWSEEELAELLGSPLLAATAERKAYVRAEYEALLEAVFEKNP
KVFPPEVFTLEAFKWAFGILFSRAFSLLAGGTLALVPWADLLNHSSGVSSDASYDVRGGSSKAVVLTADR
NYSAGEQVFISYGPKSNAELLLDYGFV
>gnl|CDD|380957 cd19180, SET_SpSET10-like, SET domain found in Schizosaccharomyces pombe SET domain-containing protein 10 (SETD10) and similar proteins. Schizosaccharomyces pombe SETD10 is a ribosomal S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates ribosomal protein L23 (rpl23a and rpl23b)
LEWATENGAKIHPKLEFRYDPDSGISVVATENAIDPGETLLSIPTSLILTPENARKSFLGALSLASAALE
SLLPRRLLLVFLLIERRGLGLGSFWGPYIDLLPKEFSTPLYWSDDELELLRGTNLFGAVQDRREQLEKEY
EVLKEALKSEHPPKEVFTFEDYLWAYTIVSSRSFPSRLVSDSGDTSSESEPVLLPLLDLLNHKPGAKVTW
NTTDTSSAFELVSGDDLAKGEQVFNNYGPKSNEELLLGYGFV
>gnl|CDD|380958 cd19181, SET_SETD5, SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and similar proteins. SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. SETD5 loss-of-function mutations are a likely cause of a familial syndromic intellectual disability with variable phenotypic expression
GSQMQLQLGRVTRVQKHRKILRAARDLALDTLIIEYRGKVMLRQQFEVNGHFFKRPYPFVLFYSKFNGVE
MCVDARTFGNDARFIRRSCTPNAEVRHMIADGMIHLCIYAVAAIAKDAEVTIAFDYEYSNCNYKVDCACH
KGNRNCPVQK
>gnl|CDD|380959 cd19182, SET_KMT2E, SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins. KMT2E (also termed inactive lysine N-methyltransferase 2E, myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. Lack of key residues in the SET domain as well as the presence of an unusually large loop in the SET-I subdomain preclude the interaction of MLL5 SET with its cofactor and substrate thus making MLL5 devoid of any in vitro methyltransferase activity on full-length histones and histone H3 peptide
TSNLLFKPPVESHVQKNKKILKAAKDLPPDTLIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLE
MCVDARTFGNEARFIRRSCTPNAEVRHVIEDGTIHLYIYSIRSIPKGTEITIAFDFDYG
>gnl|CDD|380960 cd19183, SET_SpSET3-like, SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET domain-containing protein 3 (SETD3) and similar proteins. Schizosaccharomyces pombe SETD3 functions as a transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. It is required for both, gene activation and repression
TEISSIGLANASRFGLFADRPIPAGDPIQELLGEIGLQSEYIADPENQYQILGAPKPHVFFHPQSPLYID
TRRSGSVARFIRRSCRPNAELVTVASDSGSVLKFVLYASRDISPGEEITIGWDWDNPHPFRRFALGELVP
SNLDLEQHLLSFLLQTILSNGECACGDGKNCLF
>gnl|CDD|380961 cd19184, SET_KMT5B, SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5B (KMT5B) and similar proteins. KMT5B (also termed lysine N-methyltransferase 5B, lysine-specific methyltransferase 5B, suppressor of variegation 4-20 homolog 1, Su(var)4-20 homolog 1 or Suv4-20h1) is a histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 (H4K20me3). It plays a central role in the establishment of constitutive heterochromatin in pericentric heterochromatin regions
DSGFEILPCNRYSSEQNGAKIVATKEWKRNDKIELLVGCIAELSEIEENMLLRHGENDFSVMYSTRKNCA
QLWLGPAAFINHDCRPNCKFVSTGRDTACVKALRDIEPGEEISCYYGDGFFGENNEFCECYTCERRGTGA
FKSR
>gnl|CDD|380962 cd19185, SET_KMT5C, SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) and similar proteins. KMT5C (also termed lysine N-methyltransferase 5C, lysine-specific methyltransferase 5C, suppressor of variegation 4-20 homolog 2, Su(var)4-20 homolog 2 or Suv4-20h2) is a histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 (H4K20me3). It plays a central role in the establishment of constitutive heterochromatin in pericentric heterochromatin regions
PESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREEDEGLLRAGENDFSIMYSTRKRSA
QLWLGPAAFINHDCKPNCKFVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECHTCERKGEGA
FR
>gnl|CDD|380963 cd19186, SET_Suv4-20, SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of variegation 4-20 (Suv4-20) and similar proteins. Suv4-20 (also termed Su(var)4-20) is a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-20' of histone H4. It acts as a dominant suppressor of position-effect variegation
ESGFEIQPCHRYSLEGQMGAKIVATKKWKKNEKIPLLVGCIAELTEEEEAQLLRPGENDFSVMYSCRKNC
AQLWLGPAAFINHDCRPNCKFVSTGRDTACVQVLRDIEPGEEITCFYGEDFFGDNNCYCECETCERRQTG
AF
>gnl|CDD|380964 cd19187, PR-SET_PRDM1, PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins. PRDM1 (also termed BLIMP-1, beta-interferon gene positive regulatory domain I-binding factor, PR domain-containing protein 1, positive regulatory domain I-binding factor 1, PRDI-BF1, or PRDI-binding factor 1) acts as a transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs
ASLPRNLTLKYSSVGREVLGVWSSDYIPRGTRFGPLVGEIYTNDPVPKGANRKYFWRIYSNGEFYHYIDG
FDPSKSNWMRYVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFARRL
>gnl|CDD|380965 cd19188, PR-SET_PRDM2, PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins. PRDM2 (also termed GATA-3-binding protein G3B, lysine N-methyltransferase 8, MTB-or MTE-binding protein, PR domain-containing protein 2, retinoblastoma protein-interacting zinc finger protein, or zinc finger protein RIZ) is S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. It may function as a DNA-binding transcription factor
LMGLPEELELKPSAVDKTRIGVWAKKSIPKGRKFGPFVGEKKKRSQVKNNVYMWEIYGPKRGWMCVDASD
PTKGNWLRYVNWARSGEEQNLFPLQINRAIYYKTLKPIAPGEELLCWYNGEDN
>gnl|CDD|380966 cd19189, PR-SET_PRDM4, PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins. PRDM4 (also termed PR domain-containing protein 4, or PFM1) may function as a transcription factor involved in cell differentiation
RARLSLPRQLYLRQSETGAEVGVWTKETIPVRTCFGPLIGQQSHSAEVADWTDKAAPHIWKIYHNDVLEF
CIITTDENECNWMMFVRKARTREEQNLVAYPHDGKIYFCTSRDIPPDQELLFYYSRDYARQLG
>gnl|CDD|380967 cd19190, PR-SET_PRDM5, PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins. PRDM5 (also termed PR domain-containing protein 5) is a sequence-specific DNA-binding transcription factor that represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1
LGMYVPDRFSLKSSKVQDGMGLYTARRVKKGEKFGPFAGEKRMPNELDESMDPRLMWEVRGSKGEVLYIL
DASNPRHSNWLRFVHEAPSQEQKNLAAIQEGENIFYLAVDDIETDTELLIGYLDSDM
>gnl|CDD|380968 cd19191, PR-SET_PRDM6, PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins. PRDM6 (also termed PR domain-containing protein 6) is a putative histone-lysine N-methyltransferase that acts as a transcriptional repressor of smooth muscle gene expression. It may specifically methylate 'Lys-20' of histone H4 when associated with other proteins and in vitro
LPDEVCLCTSSIPGLGYGICAAQRIPQGTWIGPFEGVLVSPEKQIGAVRNTQHLWEIYDQEGTLQHFIDG
GDPSKSSWMRYIRCARHCGEQNLTVVQYRGCIFYRACRDIPRGTELLVWYDDSYTSFF
>gnl|CDD|380969 cd19192, PR-SET_PRDM8, PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins. PRDM8 (also termed PR domain-containing protein 8) may function as histone methyltransferase, preferentially acting on 'Lys-9' of histone H3
MSHRSLWRGGSKSVLTDIFTSVVTTTDIPAGTIFGPCVLSFTLGYDIADIALKTTDKRVVPYIFRVDTGA
CNGSSEPSDWLRLVQPARDRHEQNLEAFRKNEGQVYFRTLRRIRKGEELLVWYSDELAELL
>gnl|CDD|380970 cd19193, PR-SET_PRDM7_9, PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar proteins. PRDM7 (also termed PR domain-containing protein 7) is a primate-specific histone methyltransferase that is the result of a recent gene duplication of PRDM9. It selectively catalyzes the trimethylation of H3 lysine 4 (H3K4me3). PRDM9 (also termed PR domain-containing protein 9) is a histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 (H3K4me3) during meiotic prophase and is essential for proper meiotic progression. It also efficiently mono-, di-, and trimethylates H3K36. Aberrant PRDM9 expression is assciated with with genome instability in cancer
RLTLPPGLSIKRSSIPGAGLGVWAEAPIPKGMVFGPYEGEIVEDEEAADSGYSWQIYKGGKLSHYIDAKD
ESKSNWMRYVNCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAKELGIK
>gnl|CDD|380971 cd19194, PR-SET_PRDM10, PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins. PRDM10 (also termed PR domain-containing protein 10, or tristanin) may be involved in transcriptional regulation
RARASLPLILQIFRFGETLGGVFAKRRIPKRTQFGPLEGPLVKKSELKDNKIHPLELEEDDGEDLYFDLS
DENKCNWMMFVRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFLG
>gnl|CDD|380972 cd19195, PR-SET_PRDM11, PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins. PRDM11 (also termed PR domain-containing protein 11) may be involved in transcription regulation
AALTAPQGIEVVKDTSGESDVRCVDEVIPKGHIFGPYEGQICTQDKSSGFFSWLIVDKNNRYKSIDGSDE
TKANWMRYVVISREEREQNLLAFQHSEQIYFRACRDIRPGEKLRVWYSEDYMKRLHS
>gnl|CDD|380973 cd19196, PR-SET_PRDM12, PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins. PRDM12 (also termed PR domain-containing protein 12) acts as a transcription factor that is involved in the positive regulation of histone H3-K9 dimethylation
LPSQVIIAQSSIPGAGLGVFSKTWIKEGTEMGPYTGRIVSPEDVDPCKNNNLMWEVFNEDGTVSHFIDAS
QENHRSWMTFVNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQELLVWYGNSYNTFLGIP
>gnl|CDD|380974 cd19197, PR-SET_PRDM13, PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins. PRDM13 (also termed PR domain-containing protein 13) may be involved in transcriptional regulation. It mediates the balance of inhibitory and excitatory neurons in somatosensory circuits
IPAGLRLGPVPGIFKLGKYLSDRKEPGNKKKVRRVRGDYLVDESGSPATEWIGLVRAARNNQEQNLEAIA
DLPGGQIFYRALRDIQPGEELTVWYSNSLAQWF
>gnl|CDD|380975 cd19198, PR-SET_PRDM14, PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins. PRDM14 (also termed PR domain-containing protein 14) acts as a transcription factor that has both positive and negative roles on transcription. It acts on regulating epigenetic modifications in the cells, playing a key role in the regulation of cell pluripotency, epigenetic reprogramming, differentiation and development. Aberrant PRDM14 expression is associated with tumorigenesis, cell migration and cell chemotherapeutic drugs resistance
LDLPEGLRVLQTSFGGTPHYGVFCKKTIPKGTRFGPFRGRVVNTSEIKTYDDNSFMWEIFEDGKLSHFID
GRGSTGNWMSYVNCARYAEEQNLIAIQCQGQIFYESCKEILQGQELLVWYGDCYLQFMGIPVA
>gnl|CDD|380976 cd19199, PR-SET_PRDM15, PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins. PRDM15 (also termed PR domain-containing protein 15, or zinc finger protein 298 (ZNF298)) may be involved in transcriptional regulation. It plays an essential role as a chromatin factor that modulates the transcription of upstream regulators of WNT and MAPK-ERK signaling to safeguard naive pluripotency
SRARSSLPDNLEIRQLEDGSEGVFALVPLVKRTQFGPFEAKRVARLDGFAVFPLKVFEKDGSVVYLDTSN
EDDCNWMMFVRPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVWYAAFYAKKM
>gnl|CDD|380977 cd19200, PR-SET_PRDM16_PRDM3, PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus protein and similar proteins. PRDM16 (also termed PR domain-containing protein 16, transcription factor MEL1, or MDS1/EVI1-like gene 1) functions as a transcriptional regulator. PRDM16 is preferentially expressed by hematopoietic and neuronal stem cells. It is closely related to paralog of PRDM3 (also termed MDS1 and EVI1 complex locus protein, ecotropic virus integration site 1 protein, EVI-1, myelodysplasia syndrome 1 protein, myelodysplasia syndrome-associated protein 1, or MECOM) which is a nuclear transcription factor essential for the proliferation/maintenance of hematopoietic stem cells (HSCs). PRDM3 and PRDM16 are both directly linked to various aspects of oncogenic transformation
PVYIPEDIPIPPDFELRESAAVGAGLGVWTKVRIEVGEKFGPFVGVQRSSVKDPTYAWEIVDEFGKVKFW
IDASEPGTGNWMKYIRSAPSCEQQNLMACQIDEQIYYKVVRDIQPGEELLLYMKAAVYPHETMPP
>gnl|CDD|380978 cd19201, PR-SET_ZFPM, PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins. ZFPM1 (also termed friend of GATA protein 1, FOG-1, friend of GATA 1, zinc finger protein 89A, or zinc finger protein multitype 1) functions as a transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. ZFPM2 (also termed friend of GATA protein 2, FOG-2, friend of GATA 2, zinc finger protein 89B, or zinc finger protein multitype 2) functions as a transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis
LSLPGELELRKPSQDAGRSGGVWAKQPLPEGTRFGPYPGKLVKEPLDPSYEWKVEAQGSKGGEGLLLLTE
DSGTWLKLVRSADDEDEANLILYFKGGQIWCEVTKDIPPGEELILVLREPLL
>gnl|CDD|380979 cd19202, SET_SMYD2, SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 (SMYD2) and similar proteins. SMYD2 (also termed HSKM-B, lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). It plays a role in myofilament organization in both skeletal and cardiac muscles via Hsp90 methylation. SMYD2 overexpression is associated with tumor cell proliferation and a worse outcome in human papillomavirus-unrelated nonmultiple head and neck carcinomas. It regulates leukemia cell growth such that diminished SMYD2 expression upregulates SET7/9, thereby possibly shifting leukemia cells from growth to quiescence state associated with resistance to DNA damage associated with Acute Myeloid Leukemia (AML)
GGLERFCSPGKGRGLRALRPFQVGDLLFSCPAYAYVLTPSETVRLTARILAKQKIHPERTPSEKLLAVKE
FESHLDKLDNEKKDLIQSDIAALHHFYSKHLEFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVA
LMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYPTEDRNDRLRDSYFFTCECQECTT
>gnl|CDD|380980 cd19203, SET_SMYD3, SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 (SMYD3) and similar proteins. SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. It is overexpressed in colorectal, breast, prostate, and hepatocellular tumors, and has been implicated as an oncogene in human malignancies. Methylation of MEKK2 by SMYD3 is important for regulation of the MEK/ERK pathway, suggesting the possibility of selectively targeting SMYD3 in RAS-driven cancers
SKVEKFETAEKGRGLRAVTPLKPGELVLKADPFAYTVCNPPDSVRLEGRIIFKLLDKAPSESEKLYSFYD
LQSNINKLSEDRKEGLRQLAMVLQHYLREEIQDASQLPPAFDIFELFAKVTCNSFTICDAEMQEVGVGLY
PSASLLNHSCDPNCVIVFNGPHLLLRAIREIEVGEELTISYIDMLMPSEERRKQLRDQYCFECDCFRCQD
>gnl|CDD|380981 cd19204, SET_SETD1A, SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and similar proteins. SETD1A (EC2.1.1.43), also termed lysine N-methyltransferase 2F, or Set1/Ash2 histone methyltransferase complex subunit SET1, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Human SET domain containing protein 1A (hSETD1A) expression occurs at a high rate in hepatocellular carcinoma patients and controls tumor metastasis in breast cancer by activating MMP expression
SDLLKLNQLKFRKKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEGIGSSYL
FRVDHDTIIDATKCGNLARFINHCCTPNCYAKVITIESQKKIVIYSKQPIGVNEEITYDYKFPIEDNKIP
CLCGTENCRGTLN
>gnl|CDD|380982 cd19205, SET_SETD1B, SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and similar proteins. SETD1B (EC2.1.1.43), also termed lysine N-methyltransferase 2G, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Loss of SETD1B occurs in up to half the gastric and colorectal cancers, most commonly via SETD1B mutations, while de novo variants in SETD1B are associated with intellectual disability, epilepsy and autism
SDLLKFNQLKFRKKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSSYM
FRVDHDTIIDATKCGNFARFINHSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIEDVKIP
CLCGSENCRGTLN
>gnl|CDD|380983 cd19206, SET_KMT2A, SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) and similar proteins. KMT2A (EC2.1.1.43; also termed lysine N-methyltransferase 2A, ALL-1, CXXC-type zinc finger protein 7 (CXXC7), myeloid/lymphoid or mixed-lineage leukemia (MLL), myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (TRX1), or zinc finger protein HRX) acts as a histone methyltransferase that plays an essential role in early development and hematopoiesis. It is a catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac)
MPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMF
RIDDSEVVDATMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKL
PCNCGAKKCRKFLN
>gnl|CDD|380984 cd19207, SET_KMT2B, SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) and similar proteins. KMT2B (EC2.1.1.43; also termed lysine N-methyltransferase 2B, myeloid/lymphoid or mixed-lineage leukemia protein 4 (MLL2/MLL4), trithorax homolog 2 (TRX2), or WW domain-binding protein 7 (WBP-7)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that precedes resumption of meiosis, oocyte survival and normal zygotic genome activation
MAMRFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGIGCYMF
RIDDFDVVDATMHGNAARFINHSCEPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEDASNKL
PCNCGAKRCRRFLN
>gnl|CDD|380985 cd19208, SET_KMT2C, SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) and similar proteins. KMT2C (EC2.1.1.43; also termed lysine N-methyltransferase 2C, homologous to ALR protein (HALR) myeloid/lymphoid, or mixed-lineage leukemia protein 3 (MLL3)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me) and may be involved in leukemogenesis and developmental disorder. KMT2C is a catalytic subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. Overexpression of KMT2C is associated with estrogen receptor-positive breast cancer; KMT2C mediates the estrogen dependence of breast cancer through regulation of estrogen receptor alpha (ERalpha) enhancer function. KMT2C is frequently mutated in certain populations with diffuse-type gastric adenocarcinomas (DGA); its loss promotes epithelial-to-mesenchymal transition (EMT) and is associated with worse overall survival
SKSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYM
FRIDNDHVIDATLTGGPARYINHSCAPNCVAEVVTFEKGHKIIISSSRRIQKGEELCYDYKFDFEDDQHK
IPCHCGAVNCRKWM
>gnl|CDD|380986 cd19209, SET_KMT2D, SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) and similar proteins. KMT2D (EC2.1.1.43; also termed lysine N-methyltransferase 2D, ALL1-related protein (ALR), or myeloid/lymphoid or mixed-lineage leukemia protein 2 (MLL2)), acts as histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription. KMT2D is a subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation
HSKSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIY
MFRINNEHVIDATLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQH
KIPCHCGAWNCRKWM
>gnl|CDD|380987 cd19210, SET_NSD1, SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins. NSD1 (EC 2.1.1.43; also termed Histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), androgen receptor-associated protein of 267 kDa, H3-K36-HMTase, H4-K20-HMTase, lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD1 is altered in approximately 10% of head and neck cancer patients with 55% decrease in risk of death in NSD1-mutated versus non-mutated patients; its disruption promotes favorable chemotherapeutic responses linked to hypomethylation
YPEVEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAG
PKGNYARFMNHCCQPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGF
LG
>gnl|CDD|380988 cd19211, SET_NSD2, SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins. NSD2 (EC 2.1.1.43; also termed multiple myeloma SET domain-containing protein (MMSET), protein trithorax-5 (TRX5), or wolf-Hirschhorn syndrome candidate 1 protein (WHSC1)) acts as histone-lysine N-methyltransferase with histone H3 'Lys-36' (H3K36me) methyltransferase activity. NSD2 has been shown to mediate di- and trimethylation of H3K36 and dimethylation of H4K20 in different systems, and has been characterized as a transcriptional repressor interacting with histone deacetylase HDAC1 and histone demethylase LSD1. NSD2 mediates constitutive NF-kappaB signaling for cancer cell proliferation, survival and tumor growth. It is highly overexpressed in several types of human cancers, including small-cell lung cancers, neuroblastoma, carcinomas of stomach and colon, and bladder cancers, and its overexpression tends to be associated with tumor aggressiveness. WHSC1 is frequently deleted in Wolf-Hirschhorn syndrome (WHS)
YPETKIIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAG
PKGNYSRFMNHSCQPNCETQKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGAPNCSGF
LG
>gnl|CDD|380989 cd19212, SET_NSD3, SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 3 (NSD3) and similar proteins. NSD3 (EC 2.1.1.43; also termed protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1L1), or WHSC1-like protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. NSD3 is amplified and overexpressed in multiple cancer types, including acute myeloid leukemia (AML), breast, lung, pancreatic and bladder cancers, as well as squamous cell carcinoma of the head and neck (SCCHN). NSD3 contributes to tumorigenesis by interacting with bromodomain-containing protein 4 (BRD4), the bromodomain and extraterminal (BET) protein, which is a potential therapeutic target in acute myeloid leukemia (AML). NSD3 is amplified in primary tumors and cell lines from breast carcinoma, and can promote the cell viability of small-cell lung cancer and pancreatic ductal adenocarcinoma. High NSD3 expression is implicated in poor grade and heavy smoking history in SCCHN. Thus, NSD3 may serve as a potential druggable target for selective cancer therapy
YPDAEIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSVTNFYMLTVTKDRIIDAG
PKGNYSRFMNHSCNPNCETQKWTVNGDVRVGLFALCDIPAGMELTFNYNLDCLGNGRTECHCGADNCSGF
LG
>gnl|CDD|380990 cd19213, PR-SET_PRDM16, PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins. PRDM16, also termed PR domain-containing protein 16, or transcription factor MEL1, or MDS1/EVI1-like gene 1, functions as a transcriptional regulator. PRDM16 is preferentially expressed by hematopoietic and neuronal stem cells and is closely related to paralog of PRDM3, both of which are directly linked to various aspects of oncogenic transformation
TPKEGSPYEAPVYIPDDIPIPSDFELRESSIPGAGLGVWAKRKIEAGERFGPYTGVQRSTLKDTNFGWEQ
ILNDVEVSSQEGCITKIVDDLGNEKFCVDAGQAGAGSWLKYIRVACSCDEQNLTACQINEQIYYKVIKDI
EPGEELLVYVKDGVYPLGTMPP
>gnl|CDD|380991 cd19214, PR-SET_PRDM3, PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins. PRDM3 (also termed MDS1 and EVI1 complex locus protein, ecotropic virus integration site 1 protein, EVI-1, myelodysplasia syndrome 1 protein, myelodysplasia syndrome-associated protein 1, or MECOM) is a nuclear transcription factor, which is essential for the proliferation/maintenance of hematopoietic stem cells (HSCs). It is closely related to paralog PRDM16, both o fwhich are directly linked to various aspects of oncogenic transformation
SSPATSSEAFTPKEGSPYKAPIYIPDDIPIPSEFELRESNIPGTGLGIWTKRKIEVGEKFGPYVGEQRSN
LKDPSYGWEVLDEFGNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRAVADIDPGEELL
LFMKSEDYSHETMAPDIH
>gnl|CDD|380992 cd19215, PR-SET_ZFPM1, PR-SET domain found in zinc finger protein ZFPM1 and similar proteins. ZFPM1 (also termed friend of GATA protein 1, FOG-1, friend of GATA 1, zinc finger protein 89A, or zinc finger protein multitype 1) functions as a transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation
WNGPDELELVGSSGQRRVRARQSLSEGLSWGPYHGSIQSSASSPGQAEESPAVTLLLVDEDCWLRRLPLV
STEAEANCTIYRKGDAIWCKTTKPVPEGELLSAILVTEPQ
>gnl|CDD|380993 cd19216, PR-SET_ZFPM2, PR-SET domain found in zinc finger protein ZFPM2 and similar proteins. ZFPM2 (also termed friend of GATA protein 2, FOG-2, friend of GATA 2, zinc finger protein 89B, or zinc finger protein multitype 2) functions as a transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis
WDGPGELEVFQKDGERKIHSRQQLPVGTTWGPFPGKIDLNNNSLKTKAPVPLVLTAGPKWLLDVTWQGTE
DNKNNCIVYSKGGQLWCTTTKNISEGEELIAFVVDFDSRLQ
>gnl|CDD|380994 cd19217, SET_EZH1, SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins. EZH1 (EC 2.1.1.43), also termed ENX-2, or histone-lysine N-methyltransferase EZH1, is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively
QRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSSFLFNLNNDFVVD
ATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQQGEELFFDYRYSQADALKYVGIERE
>gnl|CDD|380995 cd19218, SET_EZH2, SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins. EZH2 (EC 2.1.1.43), also termed lysine N-methyltransferase 6, or ENX-1, or histone-lysine N-methyltransferase EZH2, is a catalytic subunit of the polycomb repressive complex 2 (PRC2)/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics
GSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDAT
RKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRY
>gnl|CDD|412037 cd19318, Rev1_UBM2, Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1. This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen
GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ
>gnl|CDD|381707 cd19333, Wnt_Wnt1, Wnt domain found in proto-oncogene Wnt-1 and similar proteins. Wnt-1, also called proto-oncogene Int-1, acts in the canonical Wnt signaling pathway by promoting beta-catenin-dependent transcriptional activation. It plays a role in osteoblast function, bone development and bone homeostasis. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
LTKKQRRLVRQNPGTLHAIARGARMAIKECKWQFRNRRWNCPTTDSRGGPNVFGKILNRGCRETAFIYAI
TSAAVTHSVARACSEGSIESCSCDYRRRGPGGPDWEWGGCSDNIDFGRKFSREFVDAGEKGRDLRYLMNL
HNNEAGRVHVSSEMRQECKCHGMSGSCTVKTCWMRLPTFRTVGDRLKDRFDGASRVAYGNNGNNRGSRRA
KKFLLEPENPNHKPPTSKDLVYFEESPNFCEKNPKLGTLGTRGRECNATSIGLDGCDLMCCGRGYRTETE
EVKERCNCTFHWCCEVKCENCTRTRTVHTCL
>gnl|CDD|381708 cd19334, Wnt_Wnt2_like, Wnt domain found in protein Wnt-2, Wnt-2b and similar proteins. The family includes Wnt-2 and Wnt-2b. Wnt-2, also called Int-1-like protein 1 (INT1L1), or Int-1-related protein (IRP), functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family. It plays an important role in embryonic lung development. Wnt-2b, also called protein Wnt-13, functions in the canonical Wnt/beta-catenin signaling pathway. It plays a redundant role in embryonic lung development. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
GARVICDNIPGLVSKQRQLCRKHPDVMVSIGEGAKLGVKECQYQFRNQRWNCSTVDRDATVFGKVLLKGS
REAAFVYAISSAGVVHAITRACSKGELLNCACDPTKRGKGRDSKGEFDWGGCSDNVKYGINFARKFVDAR
ERRVRDARALMNLHNNRAGRKAVKKNLKLQCKCHGVSGSCTIRTCWRALAEFREVGDYLREKYDGAVQVT
MNQSGTNLLAANKGHKKPTRSDLVYFESSPDYCVPNPETGSLGTAGRVCNKTSTGTDGCDIMCCGRGYDT
TRVRRTTKCNCKFHWCCQVKCKTCTETVDVHTCK
>gnl|CDD|381709 cd19335, Wnt_Wnt3_Wnt3a, Wnt domain found in proto-oncogene Wnt-3 and similar proteins. Wnt-3, also called proto-oncogene Int-4, functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family. It is required for normal embryonic development, and especially for limb development. Wnt-3a functions in the canonical Wnt signaling pathway and plays crucial roles in both proliferation and differentiation processes in several types of stem cells. Wnt3a stimulates the migration and invasion of trophoblasts and induce the survival, proliferation, and migration of human embryonic kidney (HEK) 293 cells. It also up-regulates genes implicated in melanocyte differentiation and increases the expression and nuclear localization of the transcriptional co-activator with PDZ-binding motif (TAZ), a transcriptional modulator involved in activating osteoblastic differentiation. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
PILCGSIPGLVPKQLRFCRNYTELMPSVAEGAKLGIQECQHQFRGRRWNCTTIEGDLSVFGPVLDKASRE
SAFVHAIASAGVAHAVTRACAEGDSTSCGCDSRHKGPPGEGWRWGGCSEDVEFGVRFSREFADARENRPD
ARSAMNRHNNEAGRQAILDNMELKCKCHGLSGSCELKTCWWAQPDFRKIGDYLKDKYDSASEMVVERHRE
SRGWVETLRPKYKLFKPPTERDLIYYEESPNFCEPNPETGSFGTRGRECNVTSHGIDGCDLLCCGRGYNT
RTEKRTEKCHCIFVWCCYVSCQECIRVYDVHTCK
>gnl|CDD|381710 cd19336, Wnt_Wnt4, Wnt domain found in protein Wnt-4 and similar proteins. Wnt-4 may function as a signaling molecule which affects the development of discrete regions of tissues. Its overexpression may be associated with abnormal proliferation in human breast tissue. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
CESLKGLTKRQVQFCKRNLEVMDSVRRGAQLAIEECQFQFRNRRWNCSTLDKEPVFGKVLNQGTREAAFV
HAISSAGVAHAVTRACSSGELEKCGCDRSVRGRSPEGFQWSGCSDNVAYGVAFSKSFVDARERRKGRASS
SRALMNLHNNEAGRKAIEKNMRVECKCHGVSGSCELKTCWRAMPTFREVGNILKEKFDGATEVQQKRIGS
RPVLVPKNPQFKPHTDADLVYLDSSPDFCEPDPKTGSLGTHGRVCNKTSKAIDGCDLLCCGRGYVTRTEE
VVERCSCKFHWCCYVKCKTCRREVEVHTCR
>gnl|CDD|381711 cd19337, Wnt_Wnt5, Wnt domain found in protein Wnt-5a, Wnt-5b and similar proteins. The family includes Wnt-5a and Wnt-5b, both of which are secreted growth factors that belong to the noncanonical members of the Wingless-related MMTV-integration family. Wnt-5a can activate or inhibit canonical Wnt signaling, depending on receptor context. It specifically regulates dendritic spine formation in rodent hippocampal neurons, resulting in postsynaptic development that promotes the clustering of the postsynaptic density protein 95 (PSD-95). The overexpression of Wnt-5b is associated with cancer aggressiveness. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
CDQLRGLSPGQRKLCQLYQDHMPSVGRGAKLAIEECQYQFRYRRWNCSTPDSSSVFGPVTNIGTREAAFT
YAISAAGVVHAIARACREGNLSTCGCSRERRPKDLPRDWLWGGCGDNIEYGYKFAKEFIDARERETNYPR
HSRELARVLMNLHNNEAGRRAVYEKARVACKCHGVSGSCSLKTCWRQLAPFREVGDRLKDKYDGAVKVKL
NRRGTLLRRRNSRFNKPTKDDLVYLDDSPDYCERNPKTGSLGTKGRECNKTSSGTDGCELLCCGRGYNTK
KVEVVERCHCKFHWCCEVKCKTCEKIVDVHICK
>gnl|CDD|381712 cd19338, Wnt_Wnt6, Wnt domain found in protein Wnt-6 and similar proteins. Wnt-6 may function as a signaling molecule which affects the development of discrete regions of tissues. It may promote tumorigenesis in gastrointestinal cancer and cervical cancer. It can compensate for the absence of ectoderm and can induce the formation of muscle cells in the limb. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
MDPNSICRKTRRLKGKQREICRKEPEILEEVAKGAKLGIRECQYQFRNRRWNCSTSRKSFGKILKRDTRE
TAFVYAITSAGVTYSVTRACSMGELLQCGCDKSKRGKSTEGEWEWGGCSDNVRYGYRKSREFMDAKEKNR
SDIRTLMNLHNNEAGRLAVKNNMRKECKCHGLSGSCTLKTCWRKMPPFREVGDRLKERFDGAIKVKGSND
GKSLIPEGKTIKPPTKEDLVYLEESPDFCEPNKKTGSLGTRGRECNRTSMGVDGCDLLCCGRGYQTEVRV
VEENCNCRFHWCCEVKCETCKVRKEIHTCN
>gnl|CDD|381713 cd19339, Wnt_Wnt7, Wnt domain found in protein Wnt-7a, Wnt-7b and similar proteins. The family includes Wnt-7a and Wnt-7b. Wnt-7a acts as a canonical Wnt ligand that modulates the synaptic vesicle cycle and synaptic transmission in hippocampal neurons. It also plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development, and urogenital tract development. Wnt-7b functions in the canonical Wnt/beta-catenin signaling pathway in vascular smooth muscle cells. It is required for normal fusion of the chorion and the allantois during placenta development. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
ICNKIPGLTPRQRAICQSRPDAIVAIGEGAQLGIEECQFQFRNHRWNCTLLGERTVFGQELPVGSREAAF
TYAITSAGVAYAITQACSQGNLSDCGCDKSKKGYGKSDEGWKWGGCSADVKYGLRFSRKFVDAREVKRNA
RSLMNLHNNEAGRKAVEENLKLECKCHGVSGSCTTKTCWTTLPSFREIGDYLKKKYERARRVEPVRGRRR
RRPTFLKLKISRKYKKPRPRDLVYLEKSPNYCEKDPLTGSLGTVGRRCNRTSTGTDGCDLMCCGRGYNTH
QYTKTWQCNCKFHWCCYVKCNTCSERTEEYTCK
>gnl|CDD|381714 cd19340, Wnt_Wnt8, Wnt domain found in protein Wnt-8a, Wnt-8b and similar proteins. The family includes Wnt-8a and Wnt-8b. Wnt-8a, also called protein Wnt-8d, plays a role in embryonic patterning. Wnt-8b may play an important role in the development and differentiation of certain forebrain structures, notably the hippocampus. It acts as a suppressor of early eye and retinal progenitor formation. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
SGPKAYLSLSDSVAAGAQLAMEECQYQFKWDRWNCPESAFFSQKNNPSATRETAFVHAISSAGVMYTLTR
NCSLGHFEGCGCDDSKKGSKGGEGWTWGGCSDNVKFGERVSKKFLDSLETGQDAQALMNLHNNRAGRKAV
RKTMKKTCKCHGVSGSCSTQTCWMQLAPFREIGTDLKRKYDRAVRVDYENGGLRETNGSRAIKLLNIKKN
DLVYLEKSPNYCRANVTLGWPGTLGRQCSRDKKESVSRWERKSCRRLCRACGLKVRKKVVEVTSSCNCKF
HWCCEVKCETCVELVIEYTCV
>gnl|CDD|381715 cd19341, Wnt_Wnt9, Wnt domain found in protein Wnt-9a, Wnt-9b and similar proteins. The family includes Wnt-9a and Wnt-9b, both of which function in the canonical Wnt/beta-catenin signaling pathway. Wnt-9a, also called protein Wnt-14, is required for normal timing of IHH expression during embryonic bone development, normal chondrocyte maturation and for normal bone mineralization during embryonic bone development. Wnt-9a plays a redundant role in maintaining joint integrity. It is a conserved regulator of hematopoietic stem and progenitor cell development. Wnt-9b, also called protein Wnt-14b, or protein Wnt-15, plays a central role in the regulation of mesenchymal to epithelial transitions underlying organogenesis of the mammalian urogenital system. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
LSRRQRRMCRRDPGLAETLLEAIRLSVLECQEQFRYERWNCSLGKYRINLLKKGYKETAFLYAISSAGLT
HSVARACSSGRLDRCTCDESFSLEENRQTWLWGGCGDNIKYGKKFTRRFLQLKKKSGKDLRAEIDRHNSE
VGIRVVREGVKKTCKCHGVSGSCTVKTCWKQLAPFNEIGKILKRKYEKAVKVVSENNAATGGSQLRKGKS
GSVKKKSRPRRKDLVYLEKSPSFCRSTRYSPGTKGRRCLKGDNCDTLCCGRGYNTQSEVVVKPCKCRVVW
CCQVECKTCTEREEIYTCK
>gnl|CDD|381716 cd19342, Wnt_Wnt10, Wnt domain found in protein Wnt-10a, Wnt-10b and similar proteins. The family includes protein Wnt-10a and Wnt-10b. Wnt-10a plays a role in normal ectoderm development. It is required for normal postnatal development and maintenance of tongue papillae and sweat ducts, as well as normal hair follicle function. Wnt-10b, also called protein Wnt-12, specifically activates canonical Wnt/beta-catenin signaling and thus triggers beta-catenin/LEF/TCF-mediated transcriptional programs. It is involved in signaling networks controlling stemness, pluripotency, and cell fate decisions. Wnt-10b is unique and plays an important role in differentiation of epithelial cells in the hair follicle. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
NTVCRTFPGLTREQLELCRRYPDVTASAIQGIQLAVHECQRQFRDHRWNCSSLETKNKNPHTSPILSRGY
RETAFAYAISAAGVAHQVARACSLGKLLSCGCDRSRRGKRSSGNDWKWGGCSHNLDFGEKFSRKFLDSRE
KARDIHSRMNLHNNRAGRLAVSENMERKCKCHGMSGSCELKTCWKAAPDFREVGDILKEKYDHATLVDQS
NLNNGARRRRLTRRKRRRRPPKTDLVYYERSPNFCEADPSLDSPGTRGRVCNKTSTGPDSCDSLCCGRGY
NTVRQTRTERCNCRFHWCCYVVCEKCTETEWVTVCK
>gnl|CDD|381717 cd19343, Wnt_Wnt11, Wnt domain found in protein Wnt-11 and similar proteins. Wnt-11 may be a signaling molecule which has possible roles in the development of skeleton, kidney and lung. It is a positive regulator of the Wnt signaling pathway, which plays a crucial role in carcinogenesis. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
LVGDQVKLCRRNLELMPSVVEAARLTVDTCQEQFADRRWNCSSIELAPNFTPDLTRGTREQAFVYALSSA
ALTHTIARACASGALPGCGCGRLPREPPDGDFKWGGCGDNVRYGLRFAKRFTDAPEKKKKKKKRQARALM
NLHNNRVGRKAVRDSLETQCKCHGVSGSCSVKTCWKALPDLSEVASRLKRKYARAVEVVSRKVGSRRKLV
PKSLKVRPYTKDDLIYLTKSPDYCLPDEKLGSLGTRGRECNKTSVGSDSCDSMCCGRGYRTYTVEVVERC
HCKYHWCCYVKCKTCRRTVEVHVCK
>gnl|CDD|381718 cd19344, Wnt_Wnt16, Wnt domain found in protein Wnt-16 and similar proteins. Wnt-16 is a mixed canonical and noncanonical Wnt ligand involved in the regulation of postnatal bone homeostasis. It promotes bone formation and inhibits bone resorption. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
LVSQQRRLCKKKPEAIPSVSEGARLGIYECQHQFRHERWNCSTTNDQNVFGKTLSRGTKETAFIYAITSA
GVVHAVTRACSAGNLTDCSCDSRRQGQSASEGWKWGGCSDNVDYGIWFARKFVDAPEKSERKRSRDVRSL
MNLHNNEVGRQAIARLMKVKCRCHGVSGSCEVKTCWKTMPSFEEVGDFLKQKYENSIQIATKKSKRRLRR
RERRKRKVPISKDELVYIHKSPNYCVRDPKKGILGTSGRECNRTSTGPDSCDLLCCGRGYNTQVVRHVER
CNCKFVWCCYVKCKTCETMTDVHTCK
>gnl|CDD|381719 cd19345, Wnt_Wnt2, Wnt domain found in protein Wnt-2 and similar proteins. Wnt-2, also called Int-1-like protein 1 (INT1L1), or Int-1-related protein (IRP), functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family. It plays an important role in embryonic lung development. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
GSRVMCDNIPGLVSRQRQLCHRHPEVMQAIGSGVKEWIAECQHQFRNHRWNCNTLDRDHSLFGRLLLRSS
RESAFVYAISSAGVVFAITRACSQGELKSCSCDPKKKGSSKDSKGSFDWGGCSDNIDYGIRFARAFVDAK
ERKGKDARALMNLHNNRAGRKAVKRFMTLECKCHGVSGSCTVRTCWLAMADFRKTGDYLRKKYNGAIQVV
MNQDGTGFTVANKHFKKPTKNDLVYFENSPDYCVRDRDAGSLGTAGRVCNRTSRGMDGCEVMCCGRGYDT
SRVGRMTKCECKFHWCCAVRCKDCHQQVDVHTCK
>gnl|CDD|381720 cd19346, Wnt_Wnt2b, Wnt domain found in protein Wnt-2b and similar proteins. Wnt-2b, also called protein Wnt-13, functions in the canonical Wnt/beta-catenin signaling pathway. It plays a redundant role in embryonic lung development. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
GARVICDNIPGLVNKQRQLCQRHPDIMQSIGEGAKEWIRECQHQFRHHRWNCSTLDRDHTVFGRVMLRSS
REAAFVYAISSAGVVYAITRACSQGELKSCSCDPHKRGRSHDERGEFDWGGCSDNINYGIKFAKAFVDAK
EKKEKDARALMNLHNNRCGRMAVKRFMKLECKCHGVSGSCTLRTCWLAMSDFRKTGDYLRKRYNGAVQVT
MNQDGTGFTVANKNFRKATKTDLVYFENSPDYCVMDKSAGSLGTAGRVCNKSSRGTDGCEVMCCGRGYDT
TRVTRVTKCECKFHWCCAVRCKECEETVDVHTCK
>gnl|CDD|381721 cd19347, Wnt_Wnt5a, Wnt domain found in protein Wnt-5a and similar proteins. Wnt-5a is a secreted growth factor that belongs to the noncanonical members of the Wingless-related MMTV-integration family. It can activate or inhibit canonical Wnt signaling, depending on receptor context. Wnt-5a specifically regulates dendritic spine formation in rodent hippocampal neurons, resulting in postsynaptic development that promotes the clustering of the postsynaptic density protein 95 (PSD-95). Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
CSQLAGLSQGQKKLCQLYQDHMQYIGEGAKTGIKECQYQFRHRRWNCSTVDNTSVFGRVMQIGSRETAFT
YAISAAGVVNAVSRACREGELSTCGCSRAARPKDLPRDWLWGGCGDNLEYGYRFAKEFVDAREREKIYQK
GSYESARTLMNLHNNEAGRRTVYNLADVACKCHGVSGSCSLKTCWLQLADFRKVGDALKEKYDSAAAMKL
NSRGKLVQVNSRFNPPTTLDLVYIDPSPDYCVRNESTGSLGTQGRLCNKTSEGMDGCELMCCGRGYDQFK
TVQTERCHCKFHWCCYVKCKKCTEIVDQFVCK
>gnl|CDD|381722 cd19348, Wnt_Wnt5b, Wnt domain found in protein Wnt-5b and similar proteins. Wnt-5b is a secreted growth factor that belongs to the noncanonical members of the Wingless-related MMTV-integration family. Its overexpression is associated with cancer aggressiveness. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
CSQLTGLSPGQRKLCQLYQDHMVYIGEGAKTGIKECQYQFRQRRWNCSTVDNTSVFGRVMQIGSRETAFT
YAVSAAGVVNAISRACREGELSTCGCSRAARPKDLPRDWLWGGCGDNVEYGYRFAKEFVDAREREKNYPK
GSEEHARTLMNLQNNEAGRRAVYNLADVACKCHGVSGSCSLKTCWLQLADFRKVGDLLKEKYDSAAAMRI
NRKGKLELVNSRFNPPTAEDLVYIDPSPDYCLRNETTGSLGTQGRLCNKTSEGMDGCELMCCGRGYDQFK
TVQVERCHCKFHWCCYVKCKKCTEIVDQFVCK
>gnl|CDD|381723 cd19349, Wnt_Wnt7a, Wnt domain found in protein Wnt-7a and similar proteins. Wnt-7a acts as a canonical Wnt ligand that modulates the synaptic vesicle cycle and synaptic transmission in hippocampal neurons. It also plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
LGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGAQMGINECQFQFRNGRWNCSALGERTVFGKELKVGS
REAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYNQEEGWKWGGCSADIRYGIGFSKVFVDARE
IKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPKFRELGYILKDKYNEAVHVEPV
RASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRMCNKTAQQNNGCDLMCCGR
GYNTHQYSRVWQCNCKFHWCCYVKCNTCSERTEVYTCK
>gnl|CDD|381724 cd19350, wnt_Wnt7b, Wnt domain found in protein Wnt-7b and similar proteins. Wnt-7b functions in the canonical Wnt/beta-catenin signaling pathway in vascular smooth muscle cells. It is required for normal fusion of the chorion and the allantois during placenta development. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
LGANIICNKIPGLAPRQRAICQSRPDAIIVIGEGAQMGINECQYQFRYGRWNCSALGERTVFGQELRVGS
REAAFTYAITAAGVAHAVTAACSQGNLSNCGCDREKQGYYNQEEGWKWGGCSADIKYGIDFSRKFVDARE
IKKNARRLMNLHNNEAGRKVLEERMKLECKCHGVSGSCTTKTCWTTLPKFREIGYVLKEKYNAAVQVEVV
RASRLRQPTFLKIKKRRSYQKPMETDLVYIERSPNYCEEDAATGSVGTQGRLCNRTSPHTDGCDLMCCGR
GYNTHQYTKVWQCNCKFHWCCFVKCNTCSERTEVFTCK
>gnl|CDD|381725 cd19351, Wnt_Wnt8a, Wnt domain found in protein Wnt-8a and similar proteins. Wnt-8a, also called protein Wnt-8d, plays a role in embryonic patterning. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
TGPKAYLTYSSSVAAGAQSGIEECKHQFAWERWNCPESALQLSTHNGLRSATRETSFVHAISSAGVMYTL
TRNCSLGDFENCGCDDSRNGRTGGRGWIWGGCSDNVEFGERISKQFVDALETGQDARALMNLHNNEAGRL
AVKATMKRTCKCHGVSGSCSIQTCWLQLADFREIGNYLKVKHDQALKLEMDKRRMRAGNSADNRGAIAEA
FGSVAETELIYLEDSPDYCTKNASLGLQGTEGRECLQSGKNLSQWERRSCRRLCTECGLRVEERRTEVVS
SCNCKFHWCCTVKCEQCRQVVTKHYCA
>gnl|CDD|381726 cd19352, Wnt_Wnt8b, Wnt domain found in protein Wnt-8b and similar proteins. Wnt-8b may play an important role in the development and differentiation of certain forebrain structures, notably the hippocampus. It acts as a suppressor of early eye and retinal progenitor formation. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
MTGPKAYLIYSSSVAAGAQSGIEECKYQFAWDRWNCPERALQLSSHSGLRSANRETAFVHAISSAGVMYT
LTRNCSLGDFDNCGCDDSRNGQLGGQGWLWGGCSDNVGFGEAISKQFVDALETGQDARAAMNLHNNEAGR
KAVKGTMKRTCKCHGVSGSCTTQTCWLQLPEFREVGNYLKEKYHRALKVDLLQGAGNSAASRGAIAETFR
SISKKELVHLEDSPDYCLENKTLGLLGTEGRECLKRGKALSKWEKRSCRRLCGDCGLAVEERRAEMVSSC
NCKFHWCCAVKCEQCRKTVTKYFCV
>gnl|CDD|381727 cd19353, Wnt_Wnt9a, Wnt domain found in protein Wnt-9a and similar proteins. Wnt-9a, also called protein Wnt-14, functions in the canonical Wnt/beta-catenin signaling pathway. It is required for normal timing of IHH expression during embryonic bone development, normal chondrocyte maturation and for normal bone mineralization during embryonic bone development. Wnt-9a plays a redundant role in maintaining joint integrity. It is a conserved regulator of hematopoietic stem and progenitor cell development. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
LERKQRRMCRRDPGVAETLMEAISMSALECQYQFRFERWNCTLEGRYRASLLKRGFKETAFLYAISSAGL
THAMAKACSAGRMERCTCDEAPDLENREAWQWGGCGDNLKYSNKFVKEFLGRKSSKDLRARVDFHNNLVG
IKVIKAGVETTCKCHGVSGSCTVRTCWRQLSPFHEIGKQLKQKYETSLKVGSTTNEATGEGDISPPKKSG
AGHSDQIPRTTDLVYIDDSPSFCLMSRFSPGTSGRRCYKDKNCESICCGRGHNTQSRVVTRPCQCQVRWC
CYVECKQCTQREEVYTCK
>gnl|CDD|381728 cd19354, Wnt_Wnt9b, Wnt domain found in protein Wnt-9b and similar proteins. Wnt-9b, also called protein Wnt-14b or Wnt-15, functions in the canonical Wnt/beta-catenin signaling pathway. It plays a central role in the regulation of mesenchymal to epithelial transitions underlying organogenesis of the mammalian urogenital system. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
LSRRQKRLCRREPGLAETLRDAVRLGLLECQFQFRSERWNCSLEGRGSLLKRGFKETAFLYAVSSAALTH
SLAKACSSGRMERCTCDDSPGLENREAWQWGVCGDNLKYSTKFLKNFLGQKKGSKDLRARVDAHNTNVGI
KAVKSGLKTTCKCHGVSGSCAVRTCWKQLSPFHETGRLLKLKYENAVKVHSVTNDATGETELWSPERHGH
TLKGHSPRSTDLVYLEDSPSFCRPSKYSPGTAGRTCSRETNCDSLCCGRGYNTQSRLVTFSCHCQVQWCC
YVECQQCVQEEEVYTCK
>gnl|CDD|381729 cd19355, Wnt_Wnt10a, Wnt domain found in protein Wnt-10a and similar proteins. Wnt-10a plays a role in normal ectoderm development. It is required for normal postnatal development and maintenance of tongue papillae and sweat ducts, as well as normal hair follicle function. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
NTVCLTLPGLTRRQLEVCMRHPDVTASAIQGIQIAIHECQHQFRDHRWNCSSLETRNKIPYESVVFSRGF
RESAFAYAIAAAGVVHAVSNACAMGKLKACGCDWEWGGCSPDVEYGERFSKDFLDSRETYRDIHARMRLH
NNRVGRQVVMDNMRRKCKCHGTSGSCQLKTCWQVTPEFRTVGSLLKDRFYVATLIKPHNRNTGQLEPGHA
PHRRRASINDLVYFEKSPDFCEREPRLDSAGTQGRICNKTSPGMDNCESLCCGRGHNILRQTRSERCNCK
FHWCCYVVCEECRITEWVSVCK
>gnl|CDD|381730 cd19356, Wnt_Wnt10b, Wnt domain found in protein Wnt-10b and similar proteins. Wnt-10b, also called protein Wnt-12, specifically activates canonical Wnt/beta-catenin signaling and thus triggers beta-catenin/LEF/TCF-mediated transcriptional programs. It is involved in signaling networks controlling stemness, pluripotency and cell fate decisions. Wnt-10b is unique and plays an important role in differentiation of epithelial cells in the hair follicle. Wnt genes have been identified in vertebrates and invertebrates, but not in plants, unicellular eukaryotes, or prokaryotes. In humans, 19 WNT proteins are known. Because of their insolubility little is known about Wnt protein structure, but all have 23 or 24 Cys residues whose spacing is highly conserved. Signal transduction by Wnt proteins (including the Wnt/beta-catenin, the Wnt/Ca++, and the Wnt/polarity pathway) is mediated by receptors of the Frizzled and LDL-receptor-related protein (LRP) families. The Wnt signaling mediated by Wnt proteins that orchestrate and influence a myriad of cellular processes, such as cell proliferation, differentiation, tumorigenesis, apoptosis, and participation in immune defense during microbe infection
NTVCLTLPGLSKRQMGLCVRSPDVTASALQGIQIAIHECQHQLRDQRWNCSSLEGGGKLPHDSAILKRGF
RESAFSFSLLAAGVMHSVATACSLGKLRGCGCEWEWGGCSHDIEFGEKFSRDFLDSRESPRDIQARMRIH
NNRVGRQVVTENMKRKCKCHGTSGSCQFKTCWHVTPEFRLVGALLREKFQRAIFINSHNKNSGVFLPRLR
PRRLARELVYFEKSPDFCERDPAVDSPGTQGRICNKTSPGMDGCGSLCCGRGHNILKQTRSERCHCRFHW
CCYVLCEECRVTEWVNVCK
>gnl|CDD|381692 cd19357, TenA_E_At3g16990-like, TenA_E proteins similar to Arabidopsis thaliana At3g16990. This family of TenA proteins belongs to the TenA_E class, and lacks the conserved active site Cys residue of the TenA_C class; most have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2; aminopyrimidine aminohydrolase, also known as thiaminase II) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Members of this family include Arabidopsis thaliana At3g16990, Zea mays GRMZM2G080501, and Pyrococcus furiosus PF1337, among others. Arabidopsis thaliana TenA_E hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP, but does not hydrolyze thiamin; nor does it have activity with other thiamine degradation products such as thiamine mono- or diphosphate, oxythiamine, oxothiamine, thiamine disulfide, desthiothiamine or thiochrome as substrates. Structural studies of P. furiosus PF1337 strongly support its enzymatic function in thiamine biosynthesis. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect
TSHLLSLHPALYTAATQHPFLRAAADGTLPKEALSRWLAQDRLYVQAYIRFLGSLLARAPLPSSSLNQRL
LDVLLGALANLRRELAFFEETAAEYGLDLPGLGVPPSPATRAYVDFLASLASEGVSYLEGLVVLWATEKV
YLDAWSYARSFLPSDADGGALYREFIPNWTSPEFAAFVDRLGDLVDEALEQAGEEVLERAEEVWRRVLEL
EEAFWPM
>gnl|CDD|381693 cd19358, TenA_E_Spr0628-like, TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C PET18. This family of TenA proteins belongs to the TenA_E class, and lacks the conserved active site Cys residue of the TenA_C class; most have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2; aminopyrimidine aminohydrolase, also known as thiaminase II) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Arabidopsis thaliana TenA_E (not belonging to this family) hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP. Members of this family include the putative thiaminase Streptococcus pneumoniae Spr0628, and Saccharomyces cerevisiae S288C PET18, a protein of unknown function whose expression is induced in the absence of thiamin. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. Many proteins in this family have yet to be characterized
FSDRLRAANAEDWDAAVTHRFVRELCAGTLPDAVLARYLVQDYQFVETFLRLLGKAVAKAPDLEAKLRLA
RFLGFLANDENDYFERAFAALGVSEADREAPPLLPATRAFIDLMLEAARSGSYAEILTVLLVAEWLYLDW
ASRAAAAAPLRFKHQEWIDLHSGPEFEAWVDFLRDEVDRVGPTEEERERLEAVFARAVELEIAFFDAAY
>gnl|CDD|381694 cd19359, TenA_C_Bt3146-like, uncharacterized TenA_C proteins similar to Bacteroides thetaiotaomicron Bt3146. This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; only one of the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes mostly uncharacterized TenA-like proteins such as Bacteroides thetaiotaomicron Bt3146
IDKLWNDNEDLWDKALNNPFCQGMADGTLDLDGFGYYMVQDYYYCINYVRFKALRAAKAPDPDLLAFLAA
KIKSYLDYAEDFLKTCHIKLGIPDVVDGVKPSPALKAYVDFERSVAESEDWFYLLVAMIPCIYLWYWLAN
QLNEDPSDKNTNFYKTWIEPNLPDPSSAKQLEFFLNANAAWSKIDREKANEIFRQAMQLEINFFNS
>gnl|CDD|381695 cd19360, TenA_C_SaTenA-like, TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA). This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. This family includes Staphylococcus aureus TenA (SaTenA) which plays two essential roles in thiamin metabolism: in the deamination of aminopyrimidine to HMP, and in hydrolyzing thiamin into HMP and 5-(2-hydroxyethyl)4-methylthiazole (THZ). It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. SaTenA is then also a putative transcriptional regulator controlling the secretion of extracellular proteases such as subtilisin-type proteases in bacteria. This family includes mostly uncharacterized TenA like proteins
FSEELREEAQPILEAIYAHPFVQGIAAGELPKEALIHYVQQDYEYLNAFLKVYALAIAKSDTREDMRFFL
EQIGFILNGESHAHQNLCEVAGVDYEELQGAPWAPTADHYIKHMYYAARTGDLGDILAALLPCPWTYVEL
AKRLIEEGKPTPDNPFYEWIDFYADDEMDGLTDQLFARLDRLAEKASEEERERAKQAFLKSCQLEWRFWE
M
>gnl|CDD|381696 cd19361, TenA_C_HP1287-like, TenA_C proteins similar to Helicobacter pylori TenA (HP1287. This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. This family includes Helicobacter pylori TenA (HP1287) protein which is thought to catalyze a salvage reaction in thiamin metabolism, however its pyrimidine substrate has not yet been identified. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. HP1287 may contribute to stomach colonization and persistence
LSERLYEAVEDIWDSYYEHPFVQGIADGTLDIEKFRFYMIQDYLYLLDYAKVFALGVAKAKDEEVMRFFA
DLINAILNEEMDIHRGYMKRLGITEEEIENTKPALDNLSYTSYMLSVAYEGGIAEILAAILSCSWSYEYI
AKKLVERYPAALEHEFYGEWVKGYSSEEYAEANQELIDLLDRLTEDISEEQIEKLEEIFVNCSRYELKFW
DM
>gnl|CDD|381697 cd19362, TenA_C_SsTenA-1-like, uncharacterized TenA_C proteins similar to Sulfolobus solfataricus TenA-1 (Sso2206). This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; only one of the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes mostly uncharacterized TenA like proteins such as Sulfolobus solfataricus putative TenA-like thiaminase (Tena-1, Sso2206)
SENLKNLVGDLWNKYVRHEFVERMRDGTLPLDNFRYYLIQDSKYVEEMLRALLRASSKAPLDKAIKILNS
VFSGRDKGMEVHKFLYSELGITEDEIRRTGYNLVNYAYTRHLYYYSTLGWPQFLAAWAPCMWGYSEIGKY
VLNSPNELYKTWASFYASKDYKKRVEAILEALDSIEDTEDIKNIFRNSVNFEIMFWDAAL
>gnl|CDD|381698 cd19363, TenA_C_PH1161-like, uncharacterized TenA_C proteins similar to Pyrococcus horikoshii PH1161. This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; only one of the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes functionally uncharacterized TenA like proteins such as Pyrococcus horikoshii PH1161 protein
ITGKLRRDADDIWKKILNHPFVVELYSGTLPMEKFKFYLLQDYNYLVGSTKNLSILASKAESLDLMRELL
ELAYGEATTEFANYEELLDELGLSLEDAIKVEPFPTNVAYMNFLLSTSSLGSFYEGLAALLPCFWSYLEI
AEYHKDKLSENPNDIYRDWASVYLSKEYKELVERLRRIVDKYGEGEPFEKLKRIFKTASKYEYMFWDAAY
>gnl|CDD|381699 cd19364, TenA_C_BsTenA-like, TenA_C proteins similar to Bacillus subtilis TenA. This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. This family includes Bacillus subtilis TenA which has been shown to be a thiaminase II, catalyzing the hydrolysis of thiamine into HMP and 5-(2-hydroxyethyl)-4-methylthiazole (THZ), within thiamine metabolism. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect
FTEELREAADPLWQKSFEHPFIQGLADGTLPLETFRYYLIQDAYYLKHFAKLHALAAAKADDPAIKALLL
EGAQGLAEGELALRETFFKELGITEEEIAQTPPAPTAYHYVSHMYRQLNEGSVAEAVAALLPCYWLYQEI
GERLADAGSPVPLYQRWIDTYASDEFTESVQQQIDLVDRLAEEASEEEREKMKQAFLISSYYELQFWEMA
YT
>gnl|CDD|381700 cd19365, TenA_C-like, uncharacterized TenA_C proteins. This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes mostly uncharacterized TenA_C- like proteins
TEALWEAIAPIYAAILAHPFIRELADGTLPREKFRFYLAQDALYLRDYARALALLAARAPDPEEQVFFAR
FAAGAIEVERELHRSFLGEFGIDAAAEPSPVTLAYTSFLLATAATGPYAVAVAAVLPCFWIYAEVGKRLA
AAASPNHPYQDWIDTYSDEEFAEAVRRAIAIVDRLAAEASPEERARMLEAFLRASRLEWMFWDAA
>gnl|CDD|381701 cd19366, TenA_C_BhTenA-like, TenA_C proteins similar to Bacillus halodurans TenA. This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. This family includes Bacillus halodurans TenA which participates in a salvage pathway where the thiamine degradation product 2-methyl-4-formylamino-5-aminomethylpyrimidine (formylamino-HMP) is hydrolyzed first to amino-HMP by the YlmB protein, and the amino-HMP is then hydrolyzed by TenA to produce HMP. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect
FSERLREKAKPIWEAGLEHPFVQGLGDGTLDKEKFKFYLKQDYLYLIDYARVFALGAAKADDLETMGRFA
ELLHGTLNTEMDLHRQYAAEFGITEEELEATEPSPTTLAYTSYMLRTAQTGTLAELLAALLPCAWGYAEI
GKRLAEQGGALEHNPYREWIEMYSSDEFTELADWLIDLLDELAEGKSEAELERLEEIFLTSSRYEYMFWD
MAY
>gnl|CDD|381702 cd19367, TenA_C_ScTHI20-like, TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 protein. This TenA family belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. Saccharomyces cerevisiae THI20 includes a C-terminal tetrameric TenA-like domain fused to an N-terminal HMP kinase/HMP-P kinase (ThiD-like) domain, and participates in thiamin biosynthesis, degradation and salvage; the TenA-like domain catalyzes the production of HMP from thiamin degradation products (salvage). A majority of this family are single-domain TenA_C- like proteins; some however have additional domains such as a ThiD domain. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect
PIWKAYTNHPFVRQLADGTLPLESFRHYLKQDYLYLIHYARAHALAAYKAPTLEDIRAAAAILLAILEEM
ELHVKYCAEWGISEEELEATPESPATLAYTRYVLDVGLSGDLLDLLVALAPCLLGYGEIGLRLAADPATK
LEGNPYWSWIETYASDEYQEAVREGIELLEKLAAERPSPARLEELVKIFATATRLEIGFWDMGL
>gnl|CDD|381703 cd19368, TenA_C_AtTH2-like, TenA_C family similar to the N-terminal TenA_C domain of Arabidopsis thaliana thiamine requiring 2. This TenA family belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. Arabidopsis thaliana TH2 is an orphan enzyme thiamin monophosphate phosphatase which has a haloacid dehalogenase (HAD) family domain fused to its TenA_C domain, it's TenA_C domain has thiamin salvage hydrolase activity against amino-HMP. This family includes mostly uncharacterized single-domain TenA_C- like proteins; some however have additional domains such as a HAD family domain or a kinase domain It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect
LAKRLWKKNRDEALFALYHPFVVGLAAGNLPLDSFRHYISQDAHFLEAFARAYELAEAKADDDEDKKAIR
ELRKGVLEELKLHDSYAEEWGVDLPKEVTPDPATRKYTDFLLATASGKVKVAAYTLAAMAPCMRLYAFLG
QELARALDDTEDHPYKKWIDTYSSQEFEALALQLEDLLDKLSASLTGEELEALEKLYRRAMKLEVEFFAA
>gnl|CDD|381704 cd19369, TenA_C-like, uncharacterized TenA_C proteins. This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes mostly uncharacterized TenA_C- like proteins
PIWEQYLEHPFIKELGEGTLDKEKFKNYLIQDSLYLKEYAKVFAMGIYKSRTMKEMQFFYSSLSFVNEDE
TATRIKYLKEFGLTDEDIEKIEPLPENKAYTDYMLGIAKTGDVKEILMAVLPCMLSYYYIFKELVKKYKD
NLESNPYKDWIEDYASEEYAEYCKEWIDFADRLCENLSEEEKEKLKEIFRKASLYELKFWDM
>gnl|CDD|381705 cd19370, TenA_PqqC, TenA_like proteins, including PqqC and CADD. This family contains proteins with similarity to TenA, and includes bacterial coenzyme pyrroloquinoline quinone (PQQ) synthesis protein C or PQQC proteins. PQQ is the prosthetic group of several bacterial enzymes, including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria. PQQC catalyzes the last step of PQQ biogenesis which involves a ring closure and an eight-electron oxidation of the substrate [3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid (AHQQ)]. The exact molecular function of members of this family is unclear. Also belonging to this family is Chlamydia protein CADD (Chlamydia protein Associating with Death Domains), a redox protein toxin unique to Chlamydia species, which modulates host cell apoptosis; its redox activity and death domain binding ability may be required for this biological activity. CADD may have a role in folate metabolism
PQLFEELRRIKGDRYHNHHPFHVAMHNGTLTKEQLQGYVANRYYYQKTIPKKLSAIMARCDDAQTRRKWL
QNILDEDGGHGEPGHIELWLRLGEALGLTRELLSERHPLPATRFAVDTYLNFARRASWLEAAASSLSEEF
APQRIQSRLDSWLQHYNSPWIKEEGYFFFRSELSQDVRHAREGLALAEAYCDSAEKQNRVLEALQFKLDI
LWSMLDAML
>gnl|CDD|381686 cd19371, UDG-F1-like, Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein D4, Nitratifractor salsuginis UNG and similar proteins. Uracil DNA glycosylase family 1 is the most efficient of all uracil-DNA glycosylases (UDGs, also known as UNGs) and shows a specificity for uracil in DNA. UDG catalyzes the removal of uracil from DNA to initiate the DNA base excision repair pathway. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or deamination of cytosine. Uracil mispaired with guanine in DNA is one of the major pro-mutagenic events, causing G:C-_A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other. More distant members of UDG family 1 include Nitratifractor salsuginis UNG (NsaUNG) and Vaccinia virus (VAVC) protein D4 uracil-DNA glycosylase, a subunit of the VACV DNA polymerase holoenzyme. NsaUNG only exhibits robust enzymatic activity on uracil-containing DNAs, in particular double-stranded uracil-containing substrates; it does not act on hypoxanthine- and xanthine-containing substrates. NsUNG is not inhibited by Ugi protein that specifically inhibits conventional family 1 UDGs. D4, in addition to excising uracil residues from DNA, is part of a heterodimeric processivity factor which potentiates the DNA polymerase activity
VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFLPPGNGTLEFWARQGVLLLNAALT
CESGKPKSHYLLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPADF
>gnl|CDD|381687 cd19372, UDG_F1_VAVC_D4-like, Uracil DNA glycosylase family 1 subfamily, includes Vaccinia virus protein D4 and similar proteins. Vaccinia virus (VAVC) protein D4 uracil-DNA glycosylase, is a subunit of the VACV DNA polymerase holoenzyme, and a more distant member of uracil DNA glycosylase (UDG) family 1. D4, in addition to excising uracil residues from DNA, is part of a heterodimeric processivity factor which potentiates the DNA polymerase activity. UDG catalyzes the removal of uracil from DNA to initiate the DNA base excision repair pathway. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. Uracil mispaired with guanine in DNA is one of the major pro-mutagenic events, causing G:C-_A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other
WEPVINQLVDEYTEVAPWLLRDETSPIPENFFKQLKQPLRDKRVCICGIDPYPTDATGVPFESPDFSKKT
IRAIAEAISRRTGVSLYKGYNFALVEGVLAWNYYLSCREGETKSHAIHWERISKLLLQHIAKYVSVLYCL
GKTDFSNVRARLEVPVTVVVGYHPAARDGQFDKERAFEIVNVLLELNGKPPVNWAQGFLY
>gnl|CDD|381688 cd19373, UDG-F1_NsUNG-like, Uracil DNA glycosylase family 1 subfamily, includes Nitratifractor salsuginis UNG and similar proteins. Uracil DNA glycosylase family 1 is the most efficient of all uracil-DNA glycosylases (UDGs, also known as UNGs) and shows a specificity for uracil in DNA. Nitratifractor salsuginis UNG (NsaUNG) only exhibits robust enzymatic activity on uracil-containing DNAs, in particular double-stranded uracil-containing substrates, and does not act on hypoxanthine- and xanthine-containing substrates. NsUNG is not inhibited by Ugi protein that specifically inhibits conventional family 1 UDGs. UDG catalyzes the removal of uracil from DNA to initiate the DNA base excision repair pathway. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or deamination of cytosine. Uracil mispaired with guanine in DNA is one of the major pro-mutagenic events, causing G:C-_A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other
YILFGQDPYPREKSATGYAFIDGAVKEIFSPKGLSKEVNRATSLRNFIKMALVARGSLDPDDLSQEAIAK
LDKSLLVDTIDELRENFEKSGVLLLNAALLFTSKEESNRHARAWRPFIEKLLEGLEAYGPELILFGAHAK
EIKKLKSARGFPQVELEHPYNHTFIVNEKAWELF
>gnl|CDD|381689 cd19374, UDG-F3_SMUG1-like, Uracil DNA glycosylase family 3 subfamily, includes single-strand-selective monofunctional uracil-DNA glycosylase 1 and similar proteins. Uracil DNA glycosylase family 3 includes Human SMUG1 that can remove uracil and its oxidized pyrimidine derivatives from both, single-stranded DNA and double-stranded DNA, with a preference for single-stranded DNA substrates. The SMUG-targeted mismatched uracil derivatives include 5-hydroxyuracil, 5-hydroxymethyluracil and 5-formyluracil. Also included in this subfamily is Geobacter metallireducens SMUG1 which has dual substrate specificities for DNA with uracil or xanthine. UDG catalyzes the removal of uracil from DNA to initiate the DNA base excision repair pathway. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. Uracil mispaired with guanine in DNA is one of the major pro-mutagenic events, causing G:C-_A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other
EKLLEIARRLSEELDALRFSEPVAHVYNPLEYAWEPHEAYLRRYGNGGKKVLFLGMNPGPWGMAQTGVPF
GEVAAVRDWLGIEGPVGKPEKEHPKRPVEGFECPRSEVSGRRLWGLFRERFGTPEAFFARFFVHNYCPLV
FMEESGRNITPDKLPAAERKALFEACDEALREVVELLQPEWVVGVGKFAEKRARAALKDASDVKVGRILH
PSPASPAANRGWAEKAEAQLEE
>gnl|CDD|381690 cd19375, UDG-F3-like_SMUG2, Uracil DNA glycosylase family 3-like subfamily, includes single-strand-selective monofunctional uracil-DNA glycosylase 2 and similar proteins. Uracil DNA glycosylase family 3-like, which includes Pedobacter heparinus SMUG2, displays catalytic activities towards DNA containing uracil or hypoxanthine/xanthine. UDG catalyzes the removal of uracil from DNA to initiate the DNA base excision repair pathway. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or deamination of cytosine. Uracil mispaired with guanine in DNA is one of the major pro-mutagenic events, causing G:C-_A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other
FADKVLQFYKSLKLPGSLPPGVEVLNPYENPEVREIVEAFYHKYYNDNNKRVLILGINPGRFGAGVTGIP
FTDPKRLEEECGIPNDFPKRHELSSVFIYEVIEAYGGPEAFYSDFYITSVCPLGFVKNGKNYNYYDDKAL
LKALKPFIVESLREQLSFGIDTDVCICLGSGKNYKFLQKLNKEYGFFDEIIPLEHPRFIMQYKRKQKDEY
IEKYLEAL
>gnl|CDD|381646 cd19376, TGF_beta_GDF15, transforming growth factor beta (TGF-beta) like domain found in mammalian growth/differentiation factor 15 (GDF-15) and similar proteins. GDF-15, also termed macrophage inhibitory cytokine 1 (MIC-1), or NSAID-activated gene 1 protein (NAG-1), or NSAID-regulated gene 1 protein (NRG-1), or placental TGF-beta, or placental bone morphogenetic protein, or prostate differentiation factor, regulates food intake, energy expenditure and body weight in response to metabolic and toxin-induced stresses
GRCCRFSLRVSFKEIGWADWVLAPESYNAYYCDGSCPHNYKPANMHAQIKSRLHRLNPGAVPAPCCVPSS
YEPLTLLHYDSDGKLTLTEFDDMIVKDCHCA
>gnl|CDD|381647 cd19377, TGF_beta_INHA_B_like, transforming growth factor beta (TGF-beta) like domain found in inhibin alpha chain (INHA), beta chain (INHB) and similar proteins. INHA is a component of inhibins (inhibin A or inhibin B) that inhibit the secretion of follitropin by the pituitary gland. INHB includes inhibin beta A chain (INHBA), B chain (INHBB), C chain (INHBC), and E chain (INHBE). INHBA, also termed activin beta-A chain, or erythroid differentiation protein (EDF), is a component of inhibin A, activin A, or activin AB. Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. INHBB, also termed activin beta-B chain, is a component of inhibin B, activin A, or activin AB. Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. INHBC, also termed activin beta-C chain, might play important roles in carcinogenesis. It may function as a negative regulator of liver growth. INHBE, also termed activin beta-E chain, is a possible insulin resistance-associated hepatokine with hepatic gene expression that positively correlated with insulin resistance and body mass index in humans. It also acts as a possible new marker for drug-induced endoplasmic reticulum stress
CCRVALFVSFEELGWNRWIIAPPGFNFHFCHGGCALHIVPDLSLPVPSAPPTPARPYSVLPGAQPCCAPT
KVTPLSVLYTSDGGTIKYETIPDLIVQECGC
>gnl|CDD|381648 cd19378, TGF_beta_DAF7, transforming growth factor beta (TGF-beta) like domain found in Caenorhabditis elegans Dauer larva development regulatory growth factor DAF-7 and similar proteins. DAF-7, also termed abnormal dauer formation protein 7, may act as a negative regulator of dauer larva development by transducing chemosensory information from ASI neurons. It is involved in sensitivity to CO2 levels
TSCCLYDLTIDFEEIGWNFIIAPKKYNANMCRGDCKSNHHHRPNSASILLNPITRSESKQEHGSCCHPTE
YDPITVVYFNEDGQLKIKTINGMIAKKCSC
>gnl|CDD|381649 cd19379, TGF_beta_GSDF, transforming growth factor beta (TGF-beta) like domain found in Danio rerio gonadal somatic cell derived factor (GSDF) and similar proteins. GSDF is a new member of transforming growth factor beta (TGF-beta) superfamily. It is a teleost- and gonad-specific growth factor that controls sex determination in some fish and plays an important role in mediating germ cell/soma signaling
LKCCQETSEIFFKDLGWENWVIYPESFTYVQCVGCNAGRNSSESQCRQRLQGRAGARQERCCKPTSQEAV
PFVYIDEDSSLVISPVPLTRECGC
>gnl|CDD|381650 cd19380, TGF_beta_GDNF, transforming growth factor beta (TGF-beta) like domain found in glial cell line-derived neurotrophic factor (GDNF) and similar proteins. GDNF, also termed astrocyte-derived trophic factor (ATF), is a member of the glial cell-line-derived neurotrophic factor (GDNF) family. It acts as a neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake
NRGCVLTEIHLNVTDLGLGYETKEELIFRYCSGSCDAAETTYDKILKNLTRNKKLVSDKVGQACCRPIAF
DDDLSFLDDNLVYHTLKKHSAKKCGC
>gnl|CDD|381651 cd19381, TGF_beta_Artemin, transforming growth factor beta (TGF-beta) like domain found in Artemin and similar proteins. Artemin, also termed Enovin, or Neublastin, is a member of the glial cell-line-derived neurotrophic factor (GDNF) family with growth promoting activity on neuronal cells. It acts as the ligand for the GFR-alpha-3-RET receptor complex but can also activate the GFR-alpha-1-RET receptor complex. It supports peripheral and central neurons and signals through the GFR-alpha-3-RET receptor complex
GCRLRSLRVKVRDLGLGYESDEIVLFKYCSGSCQRARTNYDLTLNSLLKQGAIPPGPHERVSSQPCCRPT
RYENVSFMDVQNVWQTVEKLSAAECSCV
>gnl|CDD|381652 cd19382, TGF_beta_Persephin, transforming growth factor beta (TGF-beta) like domain found in Persephin and similar proteins. Persephin is a member of the glial cell-line-derived neurotrophic factor (GDNF) family with neurotrophic activity on mesencephalic dopaminergic and motor neurons
RPCRLRSLLLRVGDLGLGYDSEETVLFKYCSGGCPRARTNHDLTLSRLLQKGDLPSLGEKIFGGPCCRPT
HYEDVAFLDDNHRWHTVEKLSAAACACVG
>gnl|CDD|381653 cd19383, TGF_beta_Neurturin, transforming growth factor beta (TGF-beta) like domain found in Neurturin and similar proteins. Neurturin is a member of the glial cell-line-derived neurotrophic factor (GDNF) family. It acts as a neurotrophic factor that supports the survival of sympathetic neurons in culture and may regulate the development and maintenance of the CNS. It might control the size of non-neuronal cell population such as haemopoietic cells
RRRSKPCSLRELEVTVSELGLGYESDETVLFRYCSGKCEAARRNYDLTLKHMRGKKSLKKGRKDKVRARP
CCRPTAYEDDVSFLDNNNRYHTIQELSAKECGCV
>gnl|CDD|381654 cd19384, TGF_beta_TGFB1, transforming growth factor beta (TGF-beta) like domain found in transforming growth factor beta-1 (TGF-beta-1) and similar proteins. TGF-beta-1 is a polypeptide member of the transforming growth factor beta superfamily of cytokines. It is a secreted protein that performs many cellular functions, including the control of cell growth, cell proliferation, cell differentiation, and apoptosis
NCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQAL
EPLPIVYYVGRKPKVEQLSNMIVRSCKCS
>gnl|CDD|381655 cd19385, TGF_beta_TGFB2, transforming growth factor beta (TGF-beta) like domain found in transforming growth factor beta-2 (TGF-beta-2) and similar proteins. TGF-beta-2, also termed BSC-1 cell growth inhibitor, or cetermin, or glioblastoma-derived T-cell suppressor factor (G-TSF), or polyergin, is a polypeptide member of the transforming growth factor beta superfamily of cytokines. It is a secreted protein that performs many cellular functions and has a vital role during embryonic development. It can suppress the effects of interleukin-2 dependent T-cell growth
CCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASASPCCVSQDLE
PLTILYYIGKTPKIEQLSNMIVKSCKC
>gnl|CDD|381656 cd19386, TGF_beta_TGFB3, transforming growth factor beta (TGF-beta) like domain found in transforming growth factor beta-3 (TGF-beta-3) and similar proteins. TGF-beta-3 is a polypeptide member of the transforming growth factor beta superfamily of cytokines. It is involved in embryogenesis and cell differentiation. It regulates molecules involved in cellular adhesion and extracellular matrix (ECM) formation during the process of palate development
EENCCVRPLYIDFRQDLGWKWVHEPKGYFANFCSGPCPYLRSADTTHSTVLGLYNTLNPEASASPCCVPQ
DLEPLTILYYVGRTPKVEQLSNMVVKSCKCS
>gnl|CDD|381657 cd19387, TGF_beta_univin, transforming growth factor beta (TGF-beta) like domain found in Strongylocentrotus purpuratus univin and similar proteins. Univin may have a critical role in early developmental decisions in the sea urchin embryo
NICQRHSLYVDFKDVGWSDWIIAPRGYQAYRCAGECPFPLNEHLNGTNHAIIQTLVNSIDPSNVPKACCA
PTKLSSISMLYFDNNDNVVLRQYEDMVVEACGCR
>gnl|CDD|381658 cd19388, TGF_beta_GDF8, transforming growth factor beta (TGF-beta) like domain found in growth/differentiation factor 8 (GDF8) and similar proteins. GDF8, also termed myostatin, acts specifically as a negative regulator of skeletal muscle growth
FGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAG
PCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
>gnl|CDD|381659 cd19389, TGF_beta_GDF11, transforming growth factor beta (TGF-beta) like domain found in growth/differentiation factor 11 (GDF11) and similar proteins. GDF11, also termed bone morphogenetic protein 11 (BMP-11), is a secreted signal that acts globally to specify positional identity along the anterior/posterior axis during development
NLGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGQCEYMFMQKYPHTHLVQQANPRGSA
GPCCTPTKMSPINMLYFNDKQQIIYGKIPGMVVDRCGCS
>gnl|CDD|381660 cd19390, TGF_beta_BMP2, transforming growth factor beta (TGF-beta) like domain found in bone morphogenetic protein 2 (BMP-2) and similar proteins. BMP-2, also termed BMP-2A, induces cartilage and bone formation. It stimulates the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A- ATF4 pathway
SSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVP
TELSAISMLYLDENEKVVLKNYQDMVVEGCGCR
>gnl|CDD|381661 cd19391, TGF_beta_BMP4_BMP2B, transforming growth factor beta (TGF-beta) like domain found in bone morphogenetic protein 4 (BMP-4) and similar proteins. BMP-4, also termed BMP-2B, induces cartilage and bone formation. It also acts in mesoderm induction, tooth development, limb formation and fracture repair
RKNNKNCRRHSLYVDFSDVGWNDWIVAPPGYQAFYCHGDCPFPLADHLNSTNHAIVQTLVNSVNSSIPKA
CCVPTELSAISMLYLDEYDKVVLKNYQEMVVEGCGCR
>gnl|CDD|381662 cd19392, TGF_beta_DPP, transforming growth factor beta (TGF-beta) like domain found in Drosophila melanogaster protein decapentaplegic (Dpp) and similar proteins. decapentaplegic (Dpp) and similar proteins Dpp, also termed as protein DPP-C, is required later in embryogenesis for dorsal closure and patterning of the hindgut. It also functions postembryonically as a long-range morphogen during imaginal disk development and is responsible for the progression of the morphogenetic furrow during eye development
RKGHQNLCRRHPLYVDFSDVGWDDWIVAPLGYDAYYCNGECPFPLADYLNATNHAVVQTLVNSVDPQAVP
KACCVPTELSSIAMLYVDEHDKVVLKNYQDMVVEGCGCR
>gnl|CDD|381663 cd19393, TGF_beta_BMP3, transforming growth factor beta (TGF-beta) like domain found in bone morphogenetic protein 3 (BMP-3) and similar proteins. BMP-3, also termed BMP-3A, or osteogenin, negatively regulates bone density. It antagonizes the ability of certain osteogenic BMPs to induce osteoprogenitor differentitation and ossification
QWNEPRNCARRYLKVDFADIGWSEWIISPKSFDAYYCSGACQFPMPKSLKPSNHATIQSIVRAVGVVPGI
PEPCCVPEKMSSLSILFFDENKNVVLKVYPNMTVESCACR
>gnl|CDD|381664 cd19394, TGF_beta_GDF10, transforming growth factor beta (TGF-beta) like domain found in growth/differentiation factor 10 (GDF10) and similar proteins. GDF10, also termed bone morphogenetic protein 3B (BMP-3B), or bone-inducing protein (BIP), is a growth factor involved in osteogenesis and adipogenesis
RKQWSEPRVCSRRYLKVDFADIGWSEWIISPKSFDAYYCAGACEFPMPKVVRPSNHATIQSIVKAVGIIP
GVPEPCCVPDKMNSLSVLFLDENRNVVLKVYPNMSVETCACR
>gnl|CDD|381665 cd19395, TGF_beta_BMP5, transforming growth factor beta (TGF-beta) like domain found in bone morphogenetic protein 5 (BMP-5) and similar proteins. BMP-5 induces cartilage and bone formation
GDYNTSEQKQACKKHELYVSFRDLGWQDWIIAPEGYAAFYCDGECSFPLNAHMNATNHAIVQTLVHLMFP
DNVPKPCCAPTKLNAISVLYFDDSSNVILKKYRNMVVRSCGCH
>gnl|CDD|381666 cd19396, TGF_beta_BMP6, transforming growth factor beta (TGF-beta) like domain found in bone morphogenetic protein 6 (BMP-6) and similar proteins. BMP-6, also termed VG-1-related protein, or VG-1-R, or VGR-1, induces cartilage and bone formation
ACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAP
TKLNAISVLYFDDNSNVILKKYRNMVVRACGCH
>gnl|CDD|381667 cd19397, TGF_beta_BMP7, transforming growth factor beta (TGF-beta) like domain found in bone morphogenetic protein 7 (BMP-7) and similar proteins. BMP-7, also termed osteogenic protein 1 (OP-1), or eptotermin alfa, induces cartilage and bone formation. It may act as the osteoinductive factor responsible for the phenomenon of epithelial osteogenesis and play a role in calcium regulation and bone homeostasis
DQRQACKKHELYVSFRDLGWQDWIIAPEGYAAYYCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKP
CCAPTQLNAISVLYFDDSSNVILKKYRNMVVRACGCH
>gnl|CDD|381668 cd19398, TGF_beta_BMP8, transforming growth factor beta (TGF-beta) like domain found in bone morphogenetic protein 8A (BMP-8A), 8B (BMP-8B) and similar proteins. BMP-8A plays a role in the maintenance of spermatogenesis and the integrity of the epididymis. BMP-8B, also termed BMP-8, or osteogenic protein 2 (OP-2), may act as secreted factor in cancer progression. It also plays an essential role in bone metabolism and can regulate thermogenesis and energy balance. Like BMP-8A, BMP-8B plays a role in spermatogenesis and placental development. Mutation in either of the genes encoding BMP-8A or BMP-8B causes postnatal depletion of spermatogonia in mice
RQVCKRHELYVSFQDLGWLDWVIAPQGYSAYYCEGECSFPLDSCMNATNHAILQSLVHLMKPEAVPKACC
APTKLSATSVLYYDSNNNVILKKHRNMVVKSCGCH
>gnl|CDD|381669 cd19399, TGF_beta_GDF5, transforming growth factor beta (TGF-beta) like domain found in growth/differentiation factor 5 (GDF5) and similar proteins. GDF5, also termed bone morphogenetic protein 14 (BMP-14), or cartilage-derived morphogenetic protein 1 (CDMP-1), or lipopolysaccharide-associated protein 4 (LAP-4), or LPS-associated protein 4, or radotermin, is a growth factor involved in bone and cartilage formation
RCSRKALHVNFKDMGWDDWIIAPLEYEAFHCEGLCEFPLRSHLEPTNHAVIQTLMNSMDPESTPPTCCVP
TRLSPISILFIDSANNVVYKQYEDMVVESCGCR
>gnl|CDD|381670 cd19400, TGF_beta_BMP9, transforming growth factor beta (TGF-beta) like domain found in bone morphogenetic protein 9 (BMP-9) and similar proteins. BMP-9, also termed growth/differentiation factor 2 (GDF-2), is a potent circulating inhibitor of angiogenesis. It signals through the type I activin receptor ACVRL1 but not other activin receptor-like kinases (ALKs)
NHCRKTSLRVNFKDIGWDSWIIAPKEYDAYECKGGCYFPLTDDVTPTKHAIIQTLVHLKNPKKAGKACCV
PTKLDPISVLYKDDMGVPTLKYHYEGMKVAECGCR
>gnl|CDD|381671 cd19401, TGF_beta_BMP10, transforming growth factor beta (TGF-beta) like domain found in bone morphogenetic protein 10 (BMP-10) and similar proteins. BMP-10 is required for maintaining the proliferative activity of embryonic cardiomyocytes by preventing premature activation of the negative cell cycle regulator CDKN1C/p57KIP and maintaining the required expression levels of cardiogenic factors such as MEF2C and NKX2-5. It inhibits endothelial cell migration and growth. It may reduce cell migration and cell matrix adhesion in breast cancer cell lines
NYCKRSPLYVDFKEIGWDSWIIAPTGYEAYECRGVCYYPLTEHVTPTKHAIVQTLVHLKNPQKASKACCV
PTKLDPISILYLDDAGVVTYKFKYEGMVVAECGCR
>gnl|CDD|381672 cd19402, TGF_beta_GDF9B, transforming growth factor beta (TGF-beta) like domain found in growth/differentiation factor 9B (GDF-9B) and similar proteins. GDF-9B, also termed bone morphogenetic protein 15 (BMP15), acts as oocyte-specific growth/differentiation factor that stimulates folliculogenesis and granulosa cell (GC) growth
NQCSLHSFWVSFHQLGWDHWIIAPHRYNPGYCKGDCPRILHYGYNSPNHAIVQNFINQLVDANVPRPSCV
PYKYGPISVLMIEPNGNILYKEYEDMIAESCTCR
>gnl|CDD|381673 cd19403, TGF_beta_GDF9, transforming growth factor beta (TGF-beta) like domain found in growth/differentiation factor 9 (GDF-9) and similar proteins. GDF-9 is required for ovarian folliculogenesis. It promotes primordial follicle development and stimulates granulosa cell proliferation
PQNECELHDFRLSFSQLKWDHWIIAPHRYNPRYCKGSCPRAVGHRYGSPVHTMVQNIIYEKLDSSIPRPS
CVPSEYNPLSVLTIEPDGSIAYKEYEDMIATKCTCR
>gnl|CDD|381674 cd19404, TGF_beta_INHBA, transforming growth factor beta (TGF-beta) like domain found in inhibin beta A chain (INHBA) and similar proteins. INHBA, also termed activin beta-A chain, or erythroid differentiation protein (EDF), is a component of inhibin A, activin A, or activin AB. Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland
NICCKKQFYVSFKDIGWSDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGYSPFANLK
SCCVPTKLRAMSMLYYDDGQNIIKKDIQNMIVEECGCS
>gnl|CDD|381675 cd19405, TGF_beta_INHBB, transforming growth factor beta (TGF-beta) like domain found in inhibin beta B chain (INHBB) and similar proteins. INHBB, also termed activin beta-B chain, is a component of inhibin B, activin A, or activin AB. Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland
NLCCRQQFYIDFRLIGWNDWIIAPVGYYGNYCEGSCPAYMAGVPGSASSFHTAVVNQYRMRGMNPGTVNS
CCIPTKLSTMSMLYFDDEYNIVKRDVPNMIVEECGCA
>gnl|CDD|381676 cd19406, TGF_beta_INHBC_E, transforming growth factor beta (TGF-beta) like domain found in inhibin beta C chain (INHBC), inhibin beta E chain (INHBE) and similar proteins. The family includes INHBC and INHBE. INHBC, also termed activin beta-C chain, might play important roles in carcinogenesis. It may function as a negative regulator of liver growth. INHBE, also termed activin beta-E chain, is a possible insulin resistance-associated hepatokine with hepatic gene expression that positively correlated with insulin resistance and body mass index in humans. It also acts as a possible new marker for drug-induced endoplasmic reticulum stress
CCRRDFYVDFKDIGWNDWIIKPEGYQMNYCMGQCPLHIAGSPGIAASFHTAVLNLVKANNIATAVHSCCV
PTARRPLSLLYFDRNSNIVKTDIPDMIVEACGCS
>gnl|CDD|438625 cd19407, Tar_Tsr_sensor, ligand binding sensor domain of Tar- and Tsr-related chemoreceptors. Escherichia coli Tar (taxis to aspartate and repellents) and Tsr (taxis to serine and repellents) are homologous transmembrane chemoreceptors that have a high specificity for aspartate and serine, respectively. Both are homodimeric receptors and contain an N-terminal periplasmic ligand binding domain, a transmembrane region, a HAMP domain and a C-terminal cytosolic signaling domain. E. coli Tar mediates bacterial chemotaxis toward attractants, including aspartate (Asp) and maltose, and away from repellents such as nickel and cobalt ions. Tsr has many roles, including sensing of external (serine, leucine) and internal (pH) environments. In Salmonella enterica serovar Typhimurium, Tsr, also called methyl-accepting chemotaxis protein (MCP), is involved in sensing host-derived nitrate in murine intestinal epithelium, thus contributing to invasion of Peyer's patches. This model represents the ligand binding domain of Tar and Tsr
QQLRQQQSALNDSWVALLQARNTLNRAAIRYLLDANNGGGAAVAELLDQAKKSLAQAEKHFAQFKALPKL
PGQDEALAAELEQSYQAYHDALAELIQFLEAGNIDAFLDQPTQGYQDAFEKAYNAYLAQNN
>gnl|CDD|438626 cd19408, NarX_NarQ_sensor, ligand binding sensor domain of NarX and NarQ, and related chemoreceptors. The periplasmic ligand binding sensor domain of NarX and NarQ is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria and similar proteins. It forms a homodimer and binds to ligands such as nitrate via the dimerization interface, a feature that appears to be conserved in this domain superfamily. NarX-NarL sensor-response regulator pair, along with NarQ-NarP, control Escherichia coli gene expression in response to nitrate and nitrite. NarX has been shown to exhibit a clear kinetic preference for NarL over NarP, whereas NarQ exhibits a relatively slight kinetic preference for NarL. There is asymmetry in the Nar cross-regulation network with NarQ shown to interact similarly with both response regulators, while NarX interacts preferentially with NarL
ESTEGDAAAINLAGSLRMQSYRLASLLLQAALEPAEQLAQLIDEFEQRLNSPALTRALPRDSDHPLRQAY
QAVLQHWQQELRPALEAAASGAADREAYLAEVDEFVAQIDQLVKLLQQDTEAKIRL
>gnl|CDD|438627 cd19409, KinB_sensor, ligand binding sensor domain of KinB and related sensor histidine kinases. The ligand binding sensor domain of KinB and related sensor histidine kinases forms a homodimer and binds to an as yet uncharacterized ligand, most likely via the dimerization interface, a feature that appears to be conserved in this domain superfamily. In the human pathogen Pseudomonas aeruginosa, quorum sensing has been shown to repress biofilm formation and virulence by activating expression of genes encoding the KinB-AlgB two-component system. The response regulator phospho-AlgB represses biofilm and virulence genes, while histidine kinase KinB dephosphorylates and thereby inactivates AlgB; the stimulus for KinB is as yet unknown
RHNFATIELGQKLRQNLGDQLVLLLRETPDPAALEASQQHFRQLLDEGIANARDEQDRQGFEQIADAYQQ
FLQALDTPASLRRSLLDDNAFSEAFNALRNRLLDLQQHALDNI
>gnl|CDD|438628 cd19410, HK9-like_sensor, ligand binding sensor domain of Rhodopseudomonas palustris histidine kinase HK9 and similar proteins. The ligand binding sensor domain of Rhodopseudomonas palustris histidine kinase HK9 and similar proteins forms a homodimer and binds to an as yet uncharacterized ligand, most likely via the dimerization interface, a feature that appears to be conserved in this domain superfamily. This domain is similar to the extracellular sensory domain CHASE3, specifically found in histidine kinases, adenylate cyclases, methyl-accepting chemotaxis proteins and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognized by CHASE3 domains are not known at this time
EHTYEVLSELERLLSLLKDAETGQRGYLLTGDESYLEPYNAARARLPALLAELRELTADNPAQQARLDEL
EPLIDEKLAELARTIELRRAGGFEAALALVRSGRGKRLMDEIRALIAEMIAEERR
>gnl|CDD|438629 cd19411, MCP2201-like_sensor, ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar chemoreceptors. This family includes the ligand-binding sensor domain of Comamonas testosteroni transmembrane chemoreceptor CNB-2 MCP2201 and similar chemoreceptors. The C. testosteroni methyl-accepting chemotaxis protein MCP2201 triggers chemotaxis towards tricarboxylic acid cycle intermediates such as citric acid and aromatic compounds. While the apo-form ligand binding domain (LBD) forms a typical four-helix bundle homodimer, similar to other chemoreceptors in the superfamily such as Escherichia coli Tar and Tsr, the citrate-bound LBD reveals a four-helix bundle homotrimer. This type of oligomerization has never been observed in other bacterial chemoreceptor LBD. Site-directed mutations of key amino acid residues have demonstrated the physiological importance of the homotrimer for chemotaxis
IVEDRYPKVRLANEWKDNVNANARRTRNLLLSTDPAERAKELARIAAARARITELLKKLEKLITSPEGKA
LLAAIAEARAAYLAARDKVLELKKAGDREEARALLLGELRPAQAAYLAALDALVDYQEELMDAAAAEA
>gnl|CDD|410990 cd19412, pMMO-AMO_C, subunit C of particulate methane monooxygenase (pMMO, also known as membrane-bound MMO) from methanotrophic bacteria, and of ammonia monooxygenase (AMO) from ammonia-oxidizing bacteria, and related proteins. This family contains subunit C of particulate methane monooxygenase (pMMO; EC 1.14.18.3), an integral membrane metalloenzyme that catalyzes the conversion of methane to methanol. MMO is the first enzyme in the metabolic pathway of methanotrophic bacteria. It also contains subunit C of AMO (EC 1.14.99.39) from ammonia-oxidizing bacteria such as Nitrosomonas europaea (AmoC1-AmoC3). AMO catalyzes the conversion of ammonia to hydroxylamine. pMMO, along with soluble MMO (sMMO; EC 1.14.13.25), and the related enzyme AMO are the only known enzymes capable of methane hydroxylation. pMMO is composed of three subunits, PmoB (B or alpha), PmoA (A or beta), and PmoC (C or gamma), each containing membrane-spanning helices, with three copies each of the subunits forming a cylindrical A3B3C3 oligomer with a hole in the center. This subunit of pMMO has a metal-binding site that is exposed to the center of the pMMO oligomer, the metal being zinc or copper. Although biochemical and mutagenesis data indicate that the active site is located at the dicopper site in subunit B, the metal-binding site in this transmembrane subunit C may also be functionally relevant since all ligands are conserved and best enzymatic activity is obtained from intact pMMO containing all three subunits. Zinc inhibition studies of several respiratory complexes in Methylococcus capsulatus and Methylosinus trichosporium suggest that zinc might inhibit proton transfer in pMMO by either replacing active site copper ions or another copper site that is involved in reducing the active site. Nitrosomonas europaea AMO is composed of three subunits; AmoA, AmoB, and AmoC; it has two nearly identical copies of AmoC encoded by duplicate amoCAB operons and a more divergent AmoC encoded by a monocistronic amoC. The significantly shorter related C subunit of AMO from ammonia-oxidizing archaea are not included in this model
LIGLALLLLLYLAIRWYQQAFAFSAGLDSFSPEFQTYWMNLFYAELILEVLVAAVLWGYLWKTRDRNLDA
LTPREELRRYFVLLGWLAVYAFAVYWGGSFFAEQDASWHQVVIRDTDFTPSHIVLFYLSYPLYIIFGVGA
FLYARTRLPKFAKGKSLPFLLLVAGPFMILPNVGLNEWGHTFWFMEELFAAPLHWGFVVFGWAALGVGGL
LLQILKR
>gnl|CDD|381292 cd19413, RsbR_N-like, globin-like domain of positive regulator of sigma-B activity (RsbRA). The globin-like domain of Bacillus subtilis RsbRA is a non-heme globin presumed to channel sensory input to the C-terminal sulfate transporter/anti-sigma factor antagonist (STAT) domain. RsbRA is a component of the sigma B-activating stressosome, and a regulator of the RNA polymerase sigma factor subunit sigma (B)
VAQFIQENRDEILERWEEELKDLSSERSLQIISDEVYENTSREFIDLILSNISEDNEKFEERLDEFAEKV
VQLGWPLKYLTKGLQEFRKVVYELMNEEELTDQQSLELFYEFDEWIDPIRNEIVNQYSGSWE
>gnl|CDD|381189 cd19414, lipocalin_1_3_4_13-like, lipocalin-1, -3, -4, -13 and similar proteins. Lipocalin-1 (LCN1, also known as tear lipocalin, von ebner's gland protein, or tear specific prealbumin), the main lipid carrier in human tears, is critical to functions involving lipids in protection of the ocular surface. Its large ligand pocket accommodates a range of ligands including alkyl alcohols, glycolipids, phospholipids, cholesterol, steroids, and siderophores. Lipocalin-3 (LCN3, also known as vomeronasal secretory protein 1) and lipocalin-4 (LCN4, also known as vomeronasal secretory protein 2) are involved in transport of lipophilic molecules, and are possibly pheromone-carriers. Lipocalin-13 (LCN13, also known as odorant binding protein 2A) may bind and transport small hydrophobic volatile molecules with a higher affinity for aldehydes and large fatty acids. Another member of this family is late lactation protein B (LLPB), a milk protein produced during the late phase of lactation, which may be involved in transporting a small ligand released during the hydrolysis of milk fat. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
EEEDVSGTWYLKAMVVDKEFPEKRRPRKVSPVTVTALEGGNLEAKFTFMINGRCEEVKIVLEKTDEPGKY
TAFSGKKVVYIQETSVKDHYILYCEGELHGMTFRMAKLVGRDPEENPEALEEFKKFVQRKGLNEENIVIP
EQSETCV
>gnl|CDD|381190 cd19415, lipocalin_ApoM_AGP, apolipoprotein M and alpha1-acid glycoprotein family. Apolipoprotein M (ApoM) is mainly found in high-density lipoproteins (HDL) and is expressed in the liver and in the kidney; it is associated to a lesser extend with low density lipids and triglyceride rich lipoproteins. ApoM is involved in lipid transport and can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid. Alpha1-acid glycoprotein (AGP), also known as orosomucoid, has many important biological roles such as in the acute-phase reaction in response to inflammation, in immune regulation, in drug-binding and drug-transportation, in regulating sphingolipid synthesis and metabolism, and in maintaining the capillary barrier. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
CEELVKPLSLADPSQILGKWVFIAGASDSEEYLAILKLVDSSWVNLTASSDEDTIVLRQGNRLNGKCIYS
TVNATLEGSGTTFTYTNASETSTGLLLTSCPDCLLLNFNSTSGEEKGRSLYLYSRTGTLEKSELEEFKKQ
AECLGFSPPFIYD
>gnl|CDD|381191 cd19416, lipocalin_beta-LG-like, beta-lactoglobulin and similar proteins. Beta-Lactoglobulin (beta-LG) is the major whey protein of ruminant species and present in the milk of many other species, with a notable exception of human. It is the major allergen of bovine milk. Beta-LG has been shown to bind hydrophobic ligands such as curcumin, vitamin E or fatty acids, or hydrophilic such as vitamin B9. This group also includes human glycodelin (also known as placental protein 14, pregnancy-associated endometrial alpha-2 globulin, and progestagen-associated endometrial protein) which is involved in crucial biological processes such as reproduction and immune reaction. Four glycoforms of glycodelin have been identified in reproductive tissue that differ in glycosylation and biological activity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
VTQTMKDLDVQKVAGTWYSLAMAASDISLLDAQSAPLRVYIEELKPTPEGNLEIVLQKWENGRCAEKKLL
AEKTKIPAVFKINALNENKVLVLDTDYDSYLLFCMENSAEPEQSLACQCLVRTLEVDNEAMEKFDKALKT
LPMHIRLLFNPTQLEEQCHV
>gnl|CDD|381192 cd19417, lipocalin_C8gamma, complement protein C8 gamma. Human complement protein C8 gamma, together with C8alpha and C8beta, form one of five components of the cytolytic membrane attack complex (MAC), a pore-like structure that assembles on bacterial membranes. C8alpha and C8gamma form a disulfide-linked heterodimer that is noncovalently associated with C8beta. MAC plays an important role in the defense against gram-negative bacteria and other pathogenic organisms. C8gamma belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
QPAQNFDIQQFSGKWYLVAVASACRYLQESGHKVEATVLTVAPPKTTVAVSTFRKLNGICWEIKQEYGKT
GTLGRFLLKARRPRGNTDIVVGETDYSSYAILYYQRAGKLTMKLYGRSTELSENILDKFEQRAQKAHLGL
DQIFYFPKYGFCESADKFHVLD
>gnl|CDD|381193 cd19418, lipocalin_A1M-like, lipocalin domain of alpha1-microglobulin and similar proteins. Alpha(1)-microglobulin (A1M, also known as protein AMBP, alpha-1 microglycoprotein, and protein HC), has immunosuppressive properties, such as inhibition of antigen induced lymphocyte cell-proliferation, cytokine secretion, and oxidative burst of neutrophils. A1M may participate in the reducing and scavenging of biological pro-oxidants such as heme and heme-proteins. It binds heme strongly, and a C-terminally processed form of the protein degrades the heme. It can reduce cytochrome C, nitroblue tetrazolium, methemoglobin and free iron, using NADH, NADPH or ascorbate as cofactor. Intravenous administration of recombinant A1M in animal models eliminates or significantly reduces the manifestations of preeclampsia. A1M is a useful biomarker in clinical diagnostics for monitoring pre-eclampsia, hepatitis E, renal tubular dysfunction, and renal toxicity. A1M belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
LIQTQENFNLSRIYGKWYDLAVGSTCPWLKRIKDKMAIGTLVLQEGATGAELSMTRTRLRRGTCEEISGE
YEKTDTPGKFLYHKSKWNATVDAYVVHTNYDEYAIFLMKKFKRHGEPTTTLKLYGRTPQLRPTLLQDFRT
LALEQGIPEDSIIIKADKGECVP
>gnl|CDD|381194 cd19419, lipocalin_L-PGDS, lipocalin-type prostaglandin D synthase. Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5.3.99.2) is a secreted enzyme and the second most abundant protein in human cerebrospinal fluid. L-PGDS acts as both, an enzyme and as a lipid transporter, converting prostaglandin H2 to prostaglandin D2 and serving as a carrier for hydrophobic ligands including retinoids, hemoglobin metabolites, thyroid hormones, gangliosides, and fatty acids. L-PGDS belongs to the lipocalin/cytosolic fatty-acid binding protein family which has a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
PQPDFDLDKFAGRWYSVGLASNSNWFVEKKAKLKMCTTVVAPTTDGNLNLTMTFLKKNGCETRTYLYEKT
EQPGRFTYKSPRWGSDHDVRVVETNYDEYALVHTIKTKGNEEFTMVTLYSRTQTLRPELKEKFRQFAKAQ
GFTEENIVTLPQTDECPP
>gnl|CDD|381195 cd19420, lipocalin_VDE, lipocalin domain of violaxanthin deepoxidase and similar proteins. Plant violaxanthin de-epoxidase (VDE, EC 1.23.5.1) participates in the xanthophyll cycle for controlling the concentration of zeaxanthin in chloroplasts. It catalyzes the conversion of violaxanthin to antheraxanthin and zeaxanthin in strong light, and plays a central role in adjusting photosynthetic activity to changing light conditions. In addition, maize VDE has been shown to interact with sugarcane mosaic virus helper component-proteinase, HC-(SCMV), and to attenuate the RNA silencing suppression activity of the latter. VDE belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
DDGEYPVPDPSVLVQSFDMNDFNGKWYITAGLNPTFDTFDCQLHFFHVEGDDKLVGKINWRIKTPDGGFF
TRSAVQRFVQDPNQPGILYNHDNEYLHYQDDWYILSYKIENKPEDYIFVYYRGRNDAWDGYGGAVVYTRS
STLPPSYIPELEKAAKKVGVDFSTFIRTDNSCGPEPP
>gnl|CDD|381196 cd19421, lipocalin_5_8-like, lipocalin similar to human epididymal-specific lipocalin-8, mouse lipocalin-5 and -8, and similar proteins. Lipocalin 5 (LCN5; also known as epididymal retinoic acid binding protein Erabp, mouse epididymal protein 10, MEP10, and E-RABP) and Lipocalin 8 (LCN8; also known as mouse epididymal protein 17, MEP17) are homologous proteins belonging to the epididymis-specific lipocalins; they may play a role in male fertility, and may act as retinoid carrier proteins within the epididymis. In mice, genes encoding the two proteins are contiguous; in humans, there is one gene LCN8 (which has been previously called LCN5). This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
VVKDLDISKILGFWYEVAVASDQGLVLHAEERVEGLFLTLSGNNLTVKTTYNSSGSCVLEKVTGSEGDGP
GKFAFPGKREIHVLDTDYETYAILDITLLWAGRNFRVLKYFTRSLEDDDGEGFWNFREITADTGLYILAR
DGRCAELLKE
>gnl|CDD|381197 cd19422, lipocalin_15-like, lipocalin 15 and similar proteins, such as chicken CALbeta. This subfamily includes uncharacterized human lipocalin 15, and chicken chondrogenesis-associated lipocalin (CAL) beta which is associated with chondrogenesis and inflammation. It belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
KFAGLWHVMAMASDCPVFLGMKDHMTSSTTAIRPTPEGDLTMHTEFPLPDGCKQIEAEFQKSGQAGHFRV
PELGKRDLRVMDTDYSSYAILYIYKELEGESSTMVQLYTRNQDVSPQLLQKFKELYPTLGLTEDMMVILP
KSD
>gnl|CDD|381198 cd19423, lipocalin_LTBP1-like, Triatominae salivary lipocalins such as Rhodnius prolixus LTBP1 and Meccus pallidipennis triabin, and similar proteins. This subfamily includes various insect proteins found in the saliva of Triatominae (kissing bugs), including Rhodnius prolixus leukotriene-binding LTBP1. Rhodnius prolixus, a vector of the pathogen Trypanosoma cruzi, sequesters cysteinyl leukotrienes during feeding to inhibit immediate inflammatory responses; LTBP1 binds leukotrienes C4 (LTC4), D4 (LTD4), and E4 (LTE4). Meccus pallidipennis (syn Triatoma pallidipennis) triabin is a potent and selective thrombin inhibitor. It also includes Triatoma protracta procalin, a major salivary allergen which causes an allergic reaction in humans. It belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
EKCQNVEPMSNFDSTKFFSGTWYVTHAKNGTNSTVCRKYKTSKNDGKITINYGGYYGGKGKNYEVRCSGT
KKSKKGQFSFDCKQKNDRKENTNFQVEFSVIDTDYDNYALVYRCVTYGSGKKKDNYLVLQRD
>gnl|CDD|381199 cd19424, lipocalin_NPs-like, nitrophorins and similar proteins. Nitrophorins (NPs) represent a group of nitric oxide (NO)-carrying heme proteins found in the saliva of Rhodnius prolixus. In its adult phase, R. prolixus expresses at least 4 nitrophorins (designated NP1-4 in order of their increasing abundance in the saliva of adult insects). Two additional nitrophorins, NP5 and NP6, have been detected mainly in the five instar nymphal stages of insect development. NP7 has not been isolated from the insects but was instead recognized in a cDNA library. Besides NO, NPs also show high affinities for histamine (Hm). This group also includes Rhodnius prolixus amine-binding protein (ABP) which plays an important role in biogenic amine binding; it binds serotonin and norepinephrine with high affinity. NPs belong to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
ECSTNKITKTGFDKDKYFSGTWYVTHYLDTDPQTVTDKYCLSFAPRESGGKVKEALYHYNPKNKTYFYDI
SEGKLESNGGKYTAKFKTVDKDGRVIKEADEKYSYTVTVIDADDSSALVHICLQEGSKDLGDLYAVLNRN
KDADPNGKVKSAVAEAGLKLSDFVDTKDLDCQYDD
>gnl|CDD|381200 cd19425, lipocalin_10-like, Epididymal-specific lipocalin-10 and similar proteins. Epididymal-specific lipocalin-10 (LCN10) may play a role in male fertility, and may act as a retinoid carrier protein within the epididymis. It belongs to the lipocalin/cytosolic fatty-acid binding protein family which has a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
NWSKFSGFWYILATATDAQGFLPARDKRKLGASVVKVHKVGQLRVVLAFRRGQGCGRAQLKKPGTSGHLW
ASLKGVKGFHVLSTDYSYGLVYLRLGRATQNYKNLLLFHRQ
>gnl|CDD|381201 cd19426, lipocalin_6, Epididymal-specific lipocalin-6. Epididymal-specific lipocalin-6 (LCN6) may play a role in male fertility. It belongs to the lipocalin/cytosolic fatty-acid binding protein family which has a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
AVWLGRLDPKQLLGPWYVLAVASREKSFAVEKDMKNVAGVVVTLTPENNLRVLSSQHGLGGCSQSVTELL
KRNSGWVFENPSIGVLELRVLGTNFRDYAIVFTQLEFGDEPFNTVELYSRTETASQEAMGLFTKWSRGLG
FLSQ
>gnl|CDD|381202 cd19427, lipocalin_OBP-like, Lipocalin odorant-binding protein and similar proteins. Odorant-binding proteins (OBPs) transport small hydrophobic molecules in the nasal mucosa of vertebrates. This subfamily includes mouse odorant-binding protein 1a (Obp1a), Obp1b, and probasin. Mouse Obp1a and Obp1b, which are expressed in the nasal mucosa, bind the chemical odorant 2-isobutyl-3-methoxypyrazine, and may form a OBPO1a/Opb1B heterodimer. Mouse probasin may play a role in the biology of the prostate gland. This group also includes hamster female-specific lacrimal gland protein (FLP) and aphrodisin. FLP may bind tear lipids or lipid-like pheromones found in hamster tears; aphrodisin is found in hamster vaginal discharge, carries pheromones, and stimulates copulatory behavior in males. This group also includes dog allergen Ca f4 which is expressed by tongue epithelial tissue and found in saliva and dander. Bovine OBP is believed to act as a homodimer, having the C-terminal alpha-helix of each monomer stacking against the beta-barrel of the other monomer; this is possible due to its lack of cysteines and therefore lack of disulfide bonds. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
LSELSGPWRTIYIAADNVEKIEEGGPLRTYFREIECDDECQKIKITFYVKKNGQCQETTVVGYKQEDGTY
VADYEGQNYFKVVSVSEDALVFYNVNVDRAGRKTKLTLLLGKGNSLTPEQKEKFKKLAEEKGIPEENIRN
LLETDNC
>gnl|CDD|381203 cd19428, lipocalin_MUP-like, major urinary proteins (MUPs) and similar proteins. Mouse urine contains major urinary proteins (MUPs) which bind low molecular weight hydrophobic organic compounds such as urinary volatile pheromones such as the male-specific 2-sec-butyl-4,5-dihydrothiazole (SB2HT) which hastens puberty in female mice. The association between MUPs and these volatiles slows the release of the volatiles into the air from urine marks. MUPs may also act as pheromones themselves. MUPs, expressed in the nasal and vomeronasal mucosa, may be important for delivering urinary volatiles to receptors in the vomeronasal organ. This group includes MUPs encoded by central genes in the MUP cluster, as well as those encoded by peripheral genes such as Darcin/Mup20 which binds most of the male pheromone SB2HT in urine and was the first MUP shown to have male pheromonal activity in its own right. This group includes rat MUPs (also called alpha-2U globulins) and other lipocalins such as major horse allergen Equ c 1 and boar salivary lipocalin, a pheromone-binding protein specifically expressed in the submaxillary glands of the boar. It belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
SVTRNFDVSKINGEWYSILLASDKREKIEENGSMRVFVEHIHVLENSLAFKFHTKVNGECTELNLVADKT
EKAGEYSVTYDGYNTFTILETDYDNYIMFHLINFKNGETFQLMELYGREPDVSSDIKERFVKLCEEHGII
KENIIDLTKTDRCLQARG
>gnl|CDD|381204 cd19429, lipocalin_9, lipocalin 9. Lipocalin 9 (LCN9) is specifically expressed in the epididymis. It belongs to the lipocalin/cytosolic fatty-acid binding protein family. Lipocalins are typically small extracellular proteins that bind small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids and form covalent or non-covalent complexes with soluble macromolecules as well as membrane bound-receptors. They are involved in many important functions, like ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior
HTAVRRDYNMARISGVWYSISMASDNMTRIEENGDLRLFIRNIELLNNGSLQFDFHFMLQGECVAVTVVC
EKTKKNGEFSIAYEGENKVLLLETDYSMYIIFYLQNIRNGTETQVLALYGRSILLDKTHQRRFENICNKY
GLGPRNTIDMAKKDFC
>gnl|CDD|381205 cd19430, lipocalin_trichosorin-like, trichosurin and similar proteins. Trichosurin is a protein from the milk whey of the common brushtail possum, Trichosurus Vulpecula, and shows a preference for binding small phenolic ligands. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
SDEKERKWEQLSRHWHTVVLASSDRSLIEEEGPFRNFIQNITVESGNLNGFFLTRKNGQCIPLYLTAFKT
EEARQFKLNYYGTNDVYYESSKPNEYAKFIFYNYHDGKVNVVANLFGRTPNLSNEIKKRFEEDFMNRGFR
RENILDISEVDHC
>gnl|CDD|381206 cd19431, lipocalin_Can_f_2, Minor allergen Can f 2. The minor dog lipocalin allergen Can f 2 is an important cause of allergic sensitization in humans worldwide. It is one of two major allergens present in dog dander extracts, and is produced by tongue and the parotid gland (a major salivary gland). Can f 2 belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
QEGNHEEPQGGLEELSGRWHSVALASNKSDLIKPWGHFRVFIHSMSAKDGNLHGDILIPQDGQCEKVSLT
AFKTATSNKFDLEYWGHNDLYLAEVDPKSYLILYMINQYNDDTSLVAHLMVRDLSRQQDFLPAFESVCED
IGLHKDQIVVLSDDDRCQGSRD
>gnl|CDD|381207 cd19432, lipocalin_2_12-like, lipocalin 2 and 12 and similar proteins. Lipocalin-2 (LCN2, also known as siderocalin, uterocalin, neutrophil gelatinase-associated lipocalin) is expressed in renal, endothelial, liver, smooth muscle cells, cardiomyocytes, in various populations of immune cells and dendritic cells. Roles ascribed to LCN2 include chemotactic and bacteriostatic effects, and iron trafficking. LCN2 can also act as a growth factor. It plays a key role in the pathophysiology of renal and cardiovascular diseases, and is involved in various deleterious processes, such as inflammation and fibrosis. It is used as a renal injury biomarker. Lipocalin 12 (LCN12) is an epididymis-specific protein which binds all-trans retinoic acid. It may act as a retinoid carrier protein within the epididymis and play a role in male reproduction. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
FQDNQFQGKWYVVGLAGNAILREDKDPQKMYATIYELKEDKSYNVTSVLFRKKKCDYWIRTFVPGNQPGE
FTLGNIKSYPGLTSYLVRVVSTNYNQHAMVFFKKVSQNREYFKITLYGRTKELTSELKENFIRFSKSLGL
PENHIVFPVPIDQC
>gnl|CDD|381208 cd19433, lipocalin_CpcS-CpeS, CpcS/CpeS phycobiliprotein lyase family. Phycobilin lyases covalently attach a chromophore to the Cys residue(s) of cyanobacterial phycobiliproteins. They include Synechococcus sp. PCC 7002 phycocyanobilin lyase CpcS which attaches a phycocyanobilin chromophore to C-phycocyanain beta subunit and to allophycocyanin alpha and beta subunits, Synechococcus sp. PCC 7002 phycocyanobilin lyase subunit CpcU which forms a heterodimer with CpcS-I to attach phycocyanobilin to beta-phycocyanin and to allophycocyanin subunits, and Prochlorococcus marinus phycoerythrobilin lyase CpeS which attaches 3Z-phycoerythrobilin to phycoerythrin. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
MDIMEFFQLSAGEWFSQRTYHHLAFREVENGKSEITIELLEADDPEVILLCELHNIDPQEALGGARVTWE
GSLDWDKEKHKGSTVLVFLPDPDNPRQGKLLRDRGYAETVPIVGRYRFDEDGALTLTTEYEGAVSEERIW
FASPNLRLRTSIVKRAGGVLTASFCSEIR
>gnl|CDD|381209 cd19434, lipocalin_YxeF, Lipocalin similar to uncharacterized Bacillus subtilis YxeF. Bacillus subtiuls YxeF lacks the alpha-helix that packs in all lipocalins with known structure against the beta-barrel. It belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
TPFYYGTWDEGRAPGPTDGVKSATVTFTEDEVVETEVMEGRGEVQLPFMAYKVISQSTDGSIEIQYLGPY
YPLKSTLKRGENGTLIWEQNGQRKTMTRIESKTGREEK
>gnl|CDD|381210 cd19435, lipocalin_Bacteroides, bacteroides lipocalin. An uncharacterized Bacteroides subfamily of the lipocalin/cytosolic fatty-acid binding protein family a characterisitc of which is a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
PADLKGIWQLCHYVSESPDVPGALKPSNTFKVLSDDGRIVNFTIIPGADAIITGYGTYKQLTDDSYKESI
EKNIHLPXLDNKDNILEFEIGDNGVXYLKYFIKKDLNGNELNTWFHETWKRVEXPAKFPED
>gnl|CDD|381211 cd19436, lipocalin_crustacyanin, crustacyanin Type I CRTC and Type II CRTA subunits. Alpha crustacyanin bound with the carotenoid astaxanthisn (AXT) is the predominant cartenoprotein generating the slate-grey/blue color of the lobster carapace. Crustacyanin forms heterodimers (beta-crustacyanin) or complexes of 16 subunits (alpha-crustacyanin) assembled from beta-crustacyanin. Beta-crustacyanin is formed from one type I CRTC lipocalin subunit, and one type II CRTA lipocalin subunit (and two bound astaxanthin molecules). Homarus gammarus (European lobster) crustacyanin has of five distinct subunits evident on 6 M urea-PAGE gels: type I CRTC (A1, C1, C2) and type II CRTA (A2, A3). Homarus americanus crustacyanin consists of only two major subunits, namely type I CRTC (H1) and type II CRTA (H2), both of which behave like Ax subunits on a 6 M urea-PAGE gel. This family includes both type I CRTC subunit and type II CRTA subunits and belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
IPDFVVPGKCASVANQDNFDLRRYAGRWYQTHLINNPYQPVTRCVHSNYSYSGSDYGFKVTSAGFNPDNN
YLKRNGKVYPTKEFPAAHMLIDYPSVFAAPYEVIETDYENYSCVYSCIDTDGYKSEFGFVFSRSPQLAGP
AVEKCAAVFKKNGVDFSRFVPVVHTSDCV
>gnl|CDD|381212 cd19437, lipocalin_apoD-like, apolipoprotein D and similar proteins. Human apolipoprotein D (ApoD) is a small glycoprotein associated with high density lipoproteins (HDL) in plasma. It appears promiscuous since it can bind hydrophobic ligands belonging to different lipid groups, with different shapes and biochemical properties; however, it exhibits specificity between very similar lipidic species. Some ligands, such as progesterone and arachidonic acid, bind to the ligand-binding pocket with high affinity, while others may interact with ApoD via its region of surface hydrophobicity. This hydrophobic surface cluster may facilitate its association with HDL particles and facilitate its insertion into cellular lipid membranes. Drosophila NLaz and Schistocerca Laz belong to this group, and share functional properties with human ApoD, including regulation of lifespan, lipid and carbohydrate metabolism control, and protection against oxidative stress or starvation. This group also includes Sandercyanin, a blue protein secreted in the skin mucus of blue forms of walleye, Sander vitreus. Walleye is an important golden yellow commercial and sport fish; the findings of blue walleye are recent. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
LGKCPTVPVQEDFDVDKYLGRWYEIERYPAPFEKGGDCVTANYSLNDDGTVRVVNSGINLTDGSINTIEG
SARCPDPNEPAKLGVSFPGFPPAGPYWVLDTDYDNYAIVYSCTDVLGLFKVEYAWILSRQRTLSAETLTK
AKEILTSYGIDVSKLKKTDQ
>gnl|CDD|381213 cd19438, lipocalin_Blc-like, bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar proteins. Escherichia coli bacterial lipocalin (Blc, also known as YjeL) is an outer membrane lipoprotein involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Blc has a binding preference for lysophospholipids. This group includes eukaryotic lipocalins such as Arabidopsis thaliana temperature-induced lipocalin-1 (TIL) which is involved in thermotolerance, oxidative, salt, drought and high light stress tolerance, and is needed for seed longevity by ensuring polyunsaturated lipids integrity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
VPNVDLDRYMGTWYEIARLPNRFEKGCVNVTATYTLNDDGTISVVNRCRDGDEGKWKEAEGKARVVDPSD
NAKLKVSFFGPPFYGDYWVLALDPDYQWALVGGPSRDYLWILSRTPQLSEETLQRLLEKARELGYDTDKL
IRT
>gnl|CDD|381214 cd19439, lipocalin_Ex-FABP-like, extracellular fatty acid-binding protein. Ex-FABP (also known as siderocalin, lipocalin Q83 or protein Ch21) displays a dual ligand binding mode as it can bind siderophore and fatty acids simultaneously. ExFABP has a cavity which extends through the protein and has two separate ligand specificities, one for bacterial siderophores at one end, and other specifically binding co-purified lysophosphatidic acid (LPA), a potent cell signaling molecule, at the other end. As well as acting as an LPA "sensor", Ex-FABP is bacteriostatic, and tightly binds the 2,3-catechol-type ferric siderophores enterobactin, bacillibactin, and parabactin, associated with enteric bacteria and Gram-positive bacilli. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
RSELAGKWYLVALASNTDFFLREKGKMKMMMARISFLGEDELLVSYAFPSPGGCRKWETTFKKTSDDGEV
YYSEEARKTVEVLDTDYKSYAVIYATRVKDGRTLHMMRLYSRSQEVSPEAEAIFRKLAEERNYTDEMVAI
LP
>gnl|CDD|381215 cd19440, lipocalin_Bla_g_4_Per_a_4, major allergens Bla g 4 and Per a 4. Inhalant allergens from cockroaches are an important cause of asthma. Bla g 4 and Per a 4 are male pheromone transport lipocalins, and both are major allergens. Bla g 4 is produced by Blattella germanica (German cockroach) and has been shown to bind two biogenic amines, tyramine and octopamine which may be its physiological ligands. Per a 4 is produced by Periplaneta americana (American cockroach) and may bind different ligands from Bla g 4 or have different modes for tyramine/octopamine binding. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
CQRGDSLFTGFDYTKYLGVWYEAFRTPNAHEEQYKCWIDRFSLDPEGPIAVTSVAYDSRGKNRVTLTGTV
PVSTGNKFDIDYGDDEAWSSQYWVLGTDYETYAILAGCPAQDSNKHLIWVQSRDTSFDNATKKAVNEVLK
HYNLSLED
>gnl|CDD|381216 cd19441, CRABP, cellular retinoic acid-binding proteins (CRABP1 and CRABP2). Cellular retinoic acid-binding proteins (CRABPs) play a role in the metabolism of vitamin A and retinoic acid. They bind all trans retinoic acid, but not retinol. Retinol, the alcohol form of vitamin A, is an essential dietary nutrient. Within the cell, it gets oxidized into its biologically active acid form, retinoic acid, which interacts with the nuclear receptors (RARs and RXRs). The two CRABPs (CRABP1 AND CRABP2) differ in their pattern of expression across cells and developmental stages. Like other lipid binding proteins, CRABPs serve to solubilize and protect their ligand in the aqueous cytosol and transport retinoic acid between cellular compartments. CRABP1 (also known as CRABP, CRABP-I, CRABPI, RBP5) is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. CRABP1 has been shown to modulate stem cell proliferation to affect learning and memory. It has also been shown to regulate CaMKII, excessive and/or persistent activation of which is detrimental in acute and chronic cardiac injury. CRABP2 (also known as CRABP-II, RBP6) transports retinoic acid to the nucleus, and delivers all-trans-retinoic acid to nuclear retinoic acid receptors. CRABPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and besides CRABPS include the cellular retinol-binding protein (CRBPs) and the fatty acid-binding proteins (FABPs)
NFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEF
EEQTVDGRPCKSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVR
>gnl|CDD|381217 cd19442, CRBP, cellular retinol-binding protein. Cellular retinol-binding proteins (CRBPs) participate in the cellular uptake of vitamin A in the form of free retinol. Retinol achieves a higher chemical stability when bound to CRBPs, and its interaction with retinol-binding proteins allows the solubilization in the aqueous medium of the hydrophobic retinol molecule. There are four human CRBP types (CRBP1, -2, -3, -4) which differ in their tissue-specific expression pattern, as well as in their different ligand affinities. CRBPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and, besides CRBPS, include the cellular retinoic acid-binding proteins (CRABPs) and the fatty acid-binding proteins (FABPs)
DLNGTWEMVSNENFEGYMRALDIDFATRKIANLLKPQKVIEQDGDHFTIKTLSTFRNYTVDFDVGVEFEE
DTKGLDGRKCKTLVTWEGDKLVCVQKGEKENRGWTHWIEGDKLHLELTCEDQVCKQVFKKV
>gnl|CDD|381218 cd19443, FABP3-like, fatty acid-binding protein 3 and similar proteins including FABP4, -5, -7, -8, -9, -11, and -12. This FABP3-like subfamily includes FABP3, -4, -5, -7, -8, -9, -11, -12, and similar proteins and belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
KFLGTWKLVSSDNFDEYMKALGVGFATRKLGNLAKPTVIISVDGDKITIKTESTFKNTEISFKLGEEFDE
TTADGRKTKSTVTLDNGKLVQVQKWDGKETTIVRELKDGKLVVTCTMGDVVCTRTYEK
>gnl|CDD|381219 cd19444, FABP1, fatty acid-binding protein 1. Fatty acid-binding protein 1, FABP1 (also known as fatty acid-binding protein 1, liver FABP, L-FABP) occurs at high cytosolic concentration in liver, intestine, and, in the case of humans, also in kidney. FABP1 binds to two molecules of long-chain fatty acids; the two binding sites appear to be inter-dependent. FABP1 binds to fatty acyl-CoAs, peroxisome proliferators, prostaglandins, bile acids, bilirubin, heme, hydroxyl and hydroperoxyl metabolites of fatty acids, lysophosphatidic acids, selenium, and other hydrophobic ligands. FABP1 is down-regulated in about ten percent of hepatocellular carcinoma (HCC) as well as in colorectal cancer at the adenoma stage, but can also be over-expressed in various cancers. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
SFSGKYQLESQENFEPFMKAIGLPDELIQKGKDIKSVSEIVQNGNDFKLTVTTGSKVLTNEFTVGEECEL
ETLTGEKVKTVVNMEGDNKLVATLKNITSVTELNGDTLTNTMTLGDIVYKRISKRI
>gnl|CDD|381220 cd19445, FABP2, fatty acid-binding protein 2. FABP2 (also known as fatty acid-binding protein 2, intestinal, and I-FABP) is a small cytosolic protein abundantly present in mature enterocytes of small and large intestine and responsible for the absorption and intracellular transport of fatty acids. It is present throughout the small intestine; its highest expression is in the jejunum. It is a sensitive marker for damage to the intestinal epithelium. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
AFDGTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEY
SLADGTELTGTWSLEGNKLVGKFKRKDNGKELTTVREIIGDELVQTYVYEGVEAKRIFKK
>gnl|CDD|381221 cd19446, FABP6, fatty acid-binding protein 6. Human fatty acid-binding protein 6 (also known as gastrotropin, I-15P, I-BABP, I-BALB, I-BAP, ILBP, ILBP3, ileal bile acid-binding protein, ILLBP, "ileal lipid-binding protein) is an intracellular carrier of bile salts in the epithelial cells of the distal small intestine and has a key role in the enterohepatic circulation of bile salts. It recognizes a series of physiological bile salts that vary in the number and position of steroidal hydroxyl groups, and the presence and type of side-chain conjugation. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
AFTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSQHYPGGHTMTNKFTIGKESD
METMGGKKFKATVQMEGGKLVVNFPNYHHTAEIVGGKLVEVSTAGGVTYERVSKK
>gnl|CDD|381222 cd19447, L-BABP-like, liver bile acid-binding protein and similar proteins. Liver bile acid-binding protein (also known as "fatty acid-binding protein, liver", LB-FABP, L-BABP, L-FABP, FABP1) is present in the liver of the vertebrates fish, amphibians, reptiles, and birds but not in mammals. L-BABPs bind free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. The role of L-BABPs may be that of cellular and metabolic trafficking of bile acids; they may be involved in intracellular lipid transport. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
AFNGTWQVYAQENYEEFLRALSLPEDIIKMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAEI
TTMDGKKIKCTVHLEGGKLVCKSEKFSHIQEVKGGEMVETLTVGGVTLIRRSKR
>gnl|CDD|381223 cd19448, FABP_pancrustacea, fatty acid-binding protein similar to Manduca sexta and Eriocheir sinensis fatty acid-binding protein 1. This subfamily includes fatty acid-binding protein found mainly in insects such as Manduca sexta FABP1 (also known as MFB1) and Luciola cerata FABP (LcFABP), and crustacea such as Eriocheir sinensis FABP (Es-FABP). MFB1, which is isolated from midgut cytosol, binds fatty acids in a 1:1 molar ratio. LcFABP, abundantly and specifically expressed in the cytosol as well as the nucleus of cells of the photogenic layer of firefly light organ, binds fatty acids of length C14-C18. Es-FABP plays a role in lipid transport during the period of rapid ovarian growth and is involved in lipid nutrient absorption and utilization processes in the hepatopancreas, ovary, and hemocytes. It is also expressed in gills, muscle, thoracic ganglia, heart, and intestine. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
QFAGKYQLEKNENFEEFLKALGIPADLAKKLLQYKPSLEVSQNGDKYTFKSTSGDKTKTNTFKLGVEFEE
TLPGGREFKSVTTLEGNTLTQTSKFGGKKGTRTYEFSDDGLVVTLTSNKWDGKAKRYYKR
>gnl|CDD|381224 cd19449, ReP1-NCXSQ-like, fatty acid-binding protein ReP1-NCXSQ and similar proteins. Arthropod ReP1-NCXSQ (regulatory protein of the squid nerve sodium calcium exchanger) is required for MgATP stimulation of the squid nerve Na(+)/Ca(2+) exchanger NCXSQ1. ReP1-NCXSQ acts as a carrier of fatty acids; is possible that its biological ligand is palmitic acid, which is abundant in squid axons. The mechanism for fine-tuning of the regulation of NCXSQ1 by ReP1-NCXSQ may then involve the transport of palmitic acid. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
DLAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDE
TTGDGRKIKTTCTIDGNKLIQDQKGSKGKDSILTREFKDGQMHMILKVDDVVCTRIYKR
>gnl|CDD|381225 cd19450, lipocalin_ApoM, Apolipoprotein M. Apolipoprotein M (ApoM) is mainly found in high-density lipoproteins (HDL) and is expressed in the liver and the kidney; it is associated to a lesser extend with low density lipids and triglyceride rich lipoproteins. It is involved in lipid transport and can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid. This subgroup belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
CPPPAPLSTSVLNPDQYLGRWYFVAAAAWDEDDLATFKPLDNIVFNMQKGSNDTLQLTATIRIGGQCVPR
KWTYRLTEHTGSFELRTEGRPDMKWDGFSANCPGCIILQETDQEEYNRFLLYARSPHPPEECIEEFKSKT
SCLGMEDFLLTPLQQGYCKLE
>gnl|CDD|381226 cd19451, lipocalin_AGP-like, alpha1-acid glycoprotein and similar proteins. Alpha1-acid glycoprotein (AGP), also known as orosomucoid, has many important biological roles such as in the acute-phase reaction in response to inflammation, in immune regulation, in drug-binding and drug-transportation, in regulating sphingolipid synthesis and metabolism, and in maintaining the capillary barrier. This subgroup belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
PACANLTAAPITNATLDQLSGKWFYIGSAFRNPEYKKEVQEIQAAFFYLTPNKTEDTILLREYQTIGDQC
VYNSSKLTVQRENGTLSKYEGGVEHVAHLLLLRDPGTFMLAFFPEDEKNVGLSFYADKPEATPEQLKEFY
EALKCLGMDESEIMYTDWKKDKCEPLEKQHEEE
>gnl|CDD|381227 cd19452, lipocalin_ABP, Rhodnius prolixus amine-binding protein and similar proteins. Rhodnius prolixus amine-binding protein (ABP) plays an important role in biogenic amine binding; it binds serotonin and norepinephrine with high affinity. It is a subgroup of the lipocalin NP-like family. Nitrophorins (NPs) represent a group of nitric oxide (NO)-carrying heme proteins found in the saliva of Rhodnius prolixus. The lipocalin NP-like family belongs to the lipocalin/cytosolic fatty-acid binding protein family which has a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
SGCSTVDTVKDFNKDNFFTGSWYITHYKLGDSTLEVGDKNCTKFLHQKTADGKIKEVFSNYNPNAKTYSY
DISFAKVSDFDGNNGKYTAKNVIVEKDGRKIDERTLQVSYIDTDYSKYSVVHVCDPAAPDYYLYAVQSRT
ENVKEDVKSKVEAALGKVGLKLSGLFDATTLGNKCQYDDETLQKLLKQS
>gnl|CDD|381228 cd19453, lipocalin_NP2, nitrophorin 2. Nitrophorins (NPs) represent a group of nitric oxide (NO)-carrying heme proteins found in the saliva of Rhodnius prolixus. In its adult phase R. prolixus expresses at least 4 nitrophorins (designated NP1-4 in order of their increasing abundance in the saliva of adult insects). Two additional nitrophorins, NP5 and NP6, have been detected mainly in the five instar nymphal stages of insect development. NP7 has not been isolated from the insects but was instead recognized in a cDNA library. NPs belong to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
DCSTNISPKQGLDKAKYFSGKWYVTHFLDKDPQVTDQYCSSFTPRESDGTVKEALYHYNANKKTSFYNIG
EGKLESSGLQYTAKYKTVDKKKAVLKEADEKNSYTLTVLEADDSSALVHICLREGSKDLGDLYTVLTHQK
DAEPSAKVKSAVTQAGLQLSQFVGTKDLGCQYDDQFTSL
>gnl|CDD|381229 cd19454, lipocalin_NP3, nitrophorin 3. Nitrophorins (NPs) represent a group of nitric oxide (NO)-carrying heme proteins found in the saliva of Rhodnius prolixus. In its adult phase R. prolixus expresses at least 4 nitrophorins (designated NP1-4 in order of their increasing abundance in the saliva of adult insects). Two additional nitrophorins, NP5 and NP6, have been detected mainly in the five instar nymphal stages of insect development. NP7 has not been isolated from the insects but was instead recognized in a cDNA library. NPs belong to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
CLTSTMGVSGDCSTNISPKKGLDKAKYFSGTWYVTHYLDKDPQVTDPYCSSFTPKESGGTVKEALYHFNS
KKKTSFYNIGEGKLGSAGVQYTAKYNTVDKKRKEIEPADPKDSYTLTVLEADDSSALVHICLREGPKDLG
DLYTVLSHQKTGEPSATVKNAVAQAGLKLNDFVDTKTLSCTYDDQFTSM
>gnl|CDD|381230 cd19455, lipocalin_NP1, nitrophorin 1. Nitrophorins (NPs) represent a group of nitric oxide (NO)-carrying heme proteins found in the saliva of Rhodnius prolixus. In its adult phase R. prolixus expresses at least 4 nitrophorins (designated NP1-4 in order of their increasing abundance in the saliva of adult insects). Two additional nitrophorins, NP5 and NP6, have been detected mainly in the five instar nymphal stages of insect development. NP7 has not been isolated from the insects but was instead recognized in a cDNA library. NPs belong to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
KCTKNALAQTGFNKDKYFNGDVWYVTDYLDLEPDDVPKRYCAALAAGTASGKLKEALYHYDPKTQDTFYD
VSELQEESPGKYTANFKKVEKNGNVKVDVTSGNYYTFTVMYADDSSALIHTCLHKGNKDLGDLYAVLNRN
KDTNAGDKVKGAVTAASLKFSDFISTKDNKCEYDNVSLKSLLTK
>gnl|CDD|381231 cd19456, lipocalin_NP4, nitrophorin 4. Nitrophorins (NPs) represent a group of nitric oxide (NO)-carrying heme proteins found in the saliva of Rhodnius prolixus. In its adult phase R. prolixus expresses at least 4 nitrophorins (designated NP1-4 in order of their increasing abundance in the saliva of adult insects). Two additional nitrophorins, NP5 and NP6, have been detected mainly in the five instar nymphal stages of insect development. NP7 has not been isolated from the insects but was instead recognized in a cDNA library. NPs belong to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
ACTKNAIAQTGFNKDKYFNGDVWYVTDYLDLEPDDVPKRYCAALAAGTASGKLKEALYHYDPKTQDTFYD
VSELQVESLGKYTANFKKVDKNGNVKVAVTAGNYYTFTVMYADDSSALIHTCLHKGNKDLGDLYAVLNRN
KDAAAGDKVKSAVSAATLEFSKFISTKENNCAYDNDSLKSLLTK
>gnl|CDD|381232 cd19457, lipocalin_2-like, lipocalin 2 and similar proteins. Lipocalin-2 (LCN2, also known as siderocalin, uterocalin, oncogene 24p3, and neutrophil gelatinase-associated lipocalin) is expressed in renal, endothelial, liver, smooth muscle cells, cardiomyocytes, in various populations of immune cells and dendritic cells. Roles ascribed to LCN2, include chemotactic and bacteriostatic effects, and iron trafficking. LCN2 can also act as a growth factor. It plays an key role in the pathophysiology of renal and cardiovascular diseases, and is involved in various deleterious processes, such as inflammation and fibrosis. It is used as a renal injury biomarker. This subgroup belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
TPDLIPAPPLSKVPLQPDFQDDQFQGKWYVIGVAGNTIQNESLSQLTMYSTIYELKDDHSYNVTSILFRD
KGCEHWIRTFVPSVQPGQFTLGNITSYPGLQSYTVRVVATDYNQFAMVFFKKTSENRVYFEITLYGRTKE
LSPELKERFIKFSKSLGLPDDNIIFTVPIGQCI
>gnl|CDD|381233 cd19458, lipocalin_12, Lipocalin 12. Lipocalin 12 (LCN12) is an epididymis-specific protein which binds all-trans retinoic acid. It may act as a retinoid carrier protein within the epididymis and play a role in male reproduction. This subgroup belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
PQMTSFQSNQFQGEWFVLGLADNTFRREHRALLNAFTTLFELSDDSRFQVTNSMTRGKHCDTWSYTLIPA
AKPGQFTRDNRGSGPGADRENIQVIETDYTQFALVLSLRQTSRQNITRVSLLGRSWLLPHKTIDQFICLT
RTQNLTKDNILFPDLTDWLPDPSVC
>gnl|CDD|381234 cd19459, lipocalin_C1_moubatin-like, Ornithodoros moubata CI, O. moubata moubatin, and similar proteins. The soft tick Ornithodoros moubata complement inhibitor CI (OmCI, also known as coversin) specifically targets C5, a member of the C3/C4/C5 protein family that orchestrates the assembly of the terminal C multiprotein complexes. O. moubata moubatin is a specific inhibitor of collagen-induced platelet aggregation. This subgroup belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
DCTGSEPVDAFQAFSEGKEAYVLVRSTDPKARDCLKGEPAGEKQDNTLPVMMTFKDGTDWASTDWTFTLD
GAKVTATLGKLTQNREVVYDSQSHHCHVDKVEKEVPDYEMWMLDAGGLEVEVECCRQKLEELASGRNQMY
PHLKDC
>gnl|CDD|381235 cd19460, CRABP1, cellular retinoic acid-binding protein 1. Cellular retinoic acid-binding proteins (CRABPs) play a role in the metabolism of vitamin A and retinoic acid. They bind all trans retinoic acid, but not retinol. Retinol, the alcohol form of vitamin A, is an essential dietary nutrient. Within the cell, it gets oxidized into its biologically active acid form, retinoic acid, which interacts with the nuclear receptors (RARs and RXRs). The two CRABPs (CRABP1 AND CRABP2) differ in their pattern of expression across cells and developmental stages. Like other lipid binding proteins, CRABPs serve to solubilize and protect their ligand in the aqueous cytosol and transport retinoic acid between cellular compartments. This subgroup includes CRABP1 (also known as CRABP, CRABP-I, CRABPI, RBP5), which is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. CRABP1 has been shown to modulate stem cell proliferation to affect learning and memory. It has also been shown to regulate CaMKII, excessive and/or persistent activation of which is detrimental in acute and chronic cardiac injury. CRABPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and besides CRABPS include the cellular retinol-binding protein (CRBPs) and the fatty acid-binding proteins (FABPs)
PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEE
FEEETVDGRKCRSLPTWENENKIYCKQTLVEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE
>gnl|CDD|381236 cd19461, CRABP2, Cellular retinoic acid-binding protein 2. Cellular retinoic acid-binding proteins (CRABPs) play a role in the metabolism of vitamin A and retinoic acid. They bind all trans retinoic acid, but not retinol. Retinol, the alcohol form of vitamin A, is an essential dietary nutrient. Within the cell, it gets oxidized into its biologically active acid form, retinoic acid, which interacts with the nuclear receptors (RARs and RXRs). The two CRABPs (CRABP1 AND CRABP2) differ in their pattern of expression across cells and developmental stages. Like other lipid binding proteins, CRABPs serve to solubilize and protect their ligand in the aqueous cytosol and transport retinoic acid between cellular compartments. This subgroup includes CRABP2 (also known as CRABP-II, RBP6) which transports retinoic acid to the nucleus, and delivers all-trans-retinoic acid to nuclear retinoic acid receptors. CRABPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and besides CRABPS include the cellular retinol-binding protein (CRBPs) and the fatty acid-binding proteins (FABPs)
NFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEF
EEQTVDGRPCKSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE
>gnl|CDD|381237 cd19462, CRBP1, cellular retinol-binding protein 1. Cellular retinol-binding proteins (CRBPs) participate in the cellular uptake of vitamin A in the form of free retinol. Retinol achieves a higher chemical stability when bound to CRBPs, and its interaction with retinol-binding proteins allows the solubilization in the aqueous medium of the hydrophobic retinol molecule. There are four human CRBP types (CRBP1, -2, -3, -4) which differ in their tissue-specific expression pattern, as well as in their different ligand affinities. CRBP1 (also known as Retinol-Binding Protein 1, CRBP, RBPC, CRBP1, CRBPI, CRABP-I) is widely expressed in numerous tissues: it has highest abundance in the liver, kidney, lung, and retinal pigment epithelium cells of the eye. CRBP1 has a high affinity for retinol. It accepts retinol transported from the plasma to cytosol via a cell surface receptor named STRA6, which interacts with serum retinol-binding protein. CRBP1 can bind all-trans-retinol, all trans-retinal and 13-cis-retinol, but not 9-cis-retinol. CRBPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and, besides CRBPS, include the cellular retinoic acid-binding proteins (CRABPs) and the fatty acid-binding proteins (FABPs)
DFNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEE
DLTGIDDRKCMTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKV
>gnl|CDD|381238 cd19463, CRBP2, cellular retinol-binding protein 2. Cellular retinol-binding proteins (CRBPs) participate in the cellular uptake of vitamin A in the form of free retinol. Retinol achieves a higher chemical stability when bound to CRBPs, and its interaction with retinol-binding proteins allows the solubilization in the aqueous medium of the hydrophobic retinol molecule. There are four human CRBP types (CRBP1, -2, -3, -4) which differ in their tissue-specific expression pattern, as well as in their different ligand affinities. CRBP2 is also known as: "retinol-binding protein 2, cellular", CRABP-II, CRBP2, CRBPII, and RBPC2. Expression of CRBP2 is limited to the small intestine. CRBP2 binds both retinol and retinal; rat CRBP2 appears to bind both with equal affinity, human CRBP2 showed a significantly higher affinity for retinol relative to retinal. CRBP2 can bind all-trans-retinol, all trans-retinal and 13-cis-retinol, but not 9-cis-retinol. CRBPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and, besides CRBPS, include the cellular retinoic acid-binding proteins (CRABPs) and the fatty acid-binding proteins (FABPs)
DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDE
YTKSLDNRHVKALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKKK
>gnl|CDD|381239 cd19464, CRBP3, cellular retinol-binding protein 3. Cellular retinol-binding proteins (CRBPs) participate in the cellular uptake of vitamin A in the form of free retinol. Retinol achieves a higher chemical stability when bound to CRBPs, and its interaction with retinol-binding proteins allows the solubilization in the aqueous medium of the hydrophobic retinol molecule. There are four human CRBP types (CRBP1, -2, -3, -4) which differ in their tissue-specific expression pattern, as well as in their different ligand affinities. This group includes human CRBP3 (also known as retinol-binding protein 5, HRBPiso) which is expressed at highest levels in kidney and liver. CRBP3 binds retinol, and may be a human intracellular carrier of retinol in such tissues. CRBPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and, besides CRBPS, include the cellular retinoic acid-binding proteins (CRABPs) and the fatty acid-binding proteins (FABPs)
NLTGYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEE
DLRSVDGRKCQTTVTWEEEKLVCVQKGEVPNRGWRHWLEGEMLHLELTARDAVCKQVFRKV
>gnl|CDD|381240 cd19465, CRBP4, cellular retinol-binding protein 4. Cellular retinol-binding proteins (CRBPs) participate in the cellular uptake of vitamin A in the form of free retinol. Retinol achieves a higher chemical stability when bound to CRBPs, and its interaction with retinol-binding proteins allows the solubilization in the aqueous medium of the hydrophobic retinol molecule. There are four human CRBP types (CRBP1, -2, -3, -4) which differ in their tissue-specific expression pattern, as well as in their different ligand affinities. This group includes human CRBP4 (also known as retinoid-binding protein 7, CRABP4, CRBP4, CRBPIV) which is expressed primarily in kidney, heart, and transverse colon, and mouse CRBP4 which is highly expressed in white adipose tissue and mammary gland. Human CRBP4 binds retinol with an affinity lower than those for CRBP1, -2, -3. CRBPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and, besides CRBPS, include the cellular retinoic acid-binding proteins (CRABPs) and the fatty acid-binding proteins (FABPs)
DLSGTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDE
DNRGLDNRKCKSLVIWDNDRLTCIQKGEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQRA
>gnl|CDD|381241 cd19466, FABP3, fatty acid binding protein 3. FABP3 (also known as heart-type fatty acid binding protein, H-FABP, MDGI, O-FABP) is a cytosolic protein mainly expressed in cardiac and skeletal muscle cells. In these tissues, it plays an important role in fatty acid transportation, cell growth, cell signaling, and gene transcription. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
AFAGTWKLVDSKNFDEYMKALGVGFATRQVGNMTKPTTIIEVDGDKVTLKTQSTFKNTEISFKLGEEFDE
TTADDRKVKSLVTLDGGKLVHVQKWDGKETTLVREVSDGKLILTLTLGDVVSTRTYEK
>gnl|CDD|381242 cd19467, FABP4, fatty acid binding protein 4. FABP4 (also known as A-FABP, adipocyte fatty acid binding protein, aP2) is highly expressed in macrophages and in adipocytes where it regulates fatty acid storage and lipolysis and is an important mediator of inflammation. It binds long chain fatty acids, retinoic acid and eicosanoids. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEF
DEVTADDRKVKSIITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER
>gnl|CDD|381243 cd19468, FABP5, fatty acid binding protein 5. FABP5 (also known as epidermal FABP, E-FABP, cutaneous fatty-acid-binding protein, C-FABP, psoriasis-associated fatty-acid-binding protein, KFABP, PA-FABP) binds a wide array of ligands. It is an intracellular carrier for long-chain fatty acids and related active lipids, and also selectively delivers specific fatty acids from the cytosol to the nucleus. Its ligands include vitamin A metabolite all-trans-retinoic acid, endocannabinoid and numerous synthetic drugs and probes. It may be involved in keratinocyte differentiation. Mouse FABP5 is found only in the monomeric form; however, human FABP5 can exist as a monomer as well as a domain-swapped dimer. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
DLEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEE
TTADGRKTQTVCTFQDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNATCTRVYEK
>gnl|CDD|381244 cd19469, FABP8, fatty acid binding protein 8. FABP8 (also known as peripheral myelin protein 2, PMP2, myelin fatty acid binding protein, M-FABP, myelin P2 protein, MP2) is a fatty acid-binding structural component of the myelin sheath in the peripheral nervous system and may play a role in lipid transport and homeostasis in myelin. It may bind cholesterol which is present in myelin at high concentrations. In addition to binding momomeric ligands, P2 is able to bind membrane surfaces, and to stack lipid bilayers together. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFE
ETTADNRKTKSTVTLARGSLNQVQKWNGKETTIKRKLVDGKMVVECKMKGVVCTRIYEK
>gnl|CDD|381245 cd19470, FABP7, Fatty acid binding protein 7. FABP7 (also known as brain FABP, B-FABP, BLBP, brain lipid binding protein) is highly expressed in glial cells through development of the nervous system. In the developing brain, FABP7 is required for the establishment of the radial glial fiber system, which is involved in the migration of immature neurons. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
VEAFCATWKLVDSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGDKVVIRTLSTFKNTEISFKLGEEF
DETTADDRNCKSVVSLDGDKLVHVQKWDGKETNFVREIKDGKMVMTLTFGDVVAVRHYEK
>gnl|CDD|381246 cd19471, FABP9, fatty acid binding protein 9 and similar proteins. FABP9 (also known as testis-FABP, T-FABP, PERF15) is a major protein found in the inner acrosomal membrane and outer face of the nuclear envelope of mammalian sperm. Its expression is increased in prostate cancer. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
IEPFLGTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTISFNGEMMTIQTGSACRNTKISFKLGEEF
DETTADNRKVKSLITLENGSMIHVQKWLGKETTIKRKIVDGKMVVECTMNNVVSTRIYEK
>gnl|CDD|380996 cd19473, SET_SUV39H_DIM5-like, SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins. This subfamily contains Neurospora crassa DIM-5 (also termed H3-K9-HMTase dim-5, or HKMT) which functions as histone-lysine N-methyltransferase that specifically trimethylates histone H3 to form H3K9me3
PDFRFIEKSILGEGVELADEEFRSGCECTDDEDCMYSGCLCLQDVDPDDDRDPGKKKNAYHSSGAKKGCL
RGHMLNSRLPIYECHEGCACSDDCPNRVVERGRKVPLQIFRTSDGRGWGVRSTVDIKRGQFVDCYVGEII
TPEEAQRRRDAATIAQRKDVYLFALDKFSDPDSLDPRLRGDPYEIDGEFMSGPTRFINHSCDPNLRIFAR
VGDHADKHIHDLAFFAIKDIPRGTELTFDYVDGVTGLDDDAGDEEKEKEMTKCLCGSPKCRGYL
>gnl|CDD|410883 cd19475, FlaH, flagellar accessory protein FlaH. Flagellar accessory protein FlaH is part of the motor of the archaellum membrane-anchored archaeal motility structure, together with FlaX and FlaI. FlaH forms a hexameric ring, and binds ATP which is essential for its interaction with FlaI and for archaellum assembly
ISLGRDDLDKRLGGGIPYPSSIMIEGEESTGKSVLSQRLVYGFLQNDYSGYYISTQQTTKEFLKQMKSLK
YDINKKLLRGKLLYIPVYPLIFDNSLKDKFLKKIVNTRAFYEKDFIIFDSLSILIANDASEVQVLDLMKF
IKRIVNTGKIILFTINPKELDEEVKTKIRTIATVYIKTEAFTFGGRLKNIAKIVKYNGAIGGFQKTIVFR
VDPALGIAVE
>gnl|CDD|410884 cd19476, RecA-like_ion-translocating_ATPases, RecA-like domain of ion-translocating ATPases. RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKI
GIFGGSGVGKTVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGA
RMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKV
KDGGGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV
>gnl|CDD|410885 cd19477, type_II_IV_secretion_ATPases, type II/type IV hexameric secretion ATPases. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
SAIKDGIAIGKNVIVCGGTGSGKTTYIKSILEFIPKEERIISIEDTEEIVFKHHKNYTQLFFGGNITSAD
CLKSCLRQRPDRIILGELRSSEAYDFYNVLCSGHKGTLTTLHAGSSEEAFIRLANXSSSNSAARNIKFES
LIEGFKDLIDGIVHINHHKQCDEFYIKH
>gnl|CDD|410886 cd19478, Csm2, Shu complex subunit Csm2. Csm2, together with Shu1, Shu2, and Psy3, form the Shu complex which is thought to play a role in maintaining genome stability by linking error-free post-replication repair to homologous recombination
DLLTIWVSPKPIDLAQFIAQFLTKEHSDTQLYFIDATNSFPLSQFQKLVPPNEENKRIYENIRINTCLDL
EELSIIVNKILQILSINKIQRQQKKKDQETPPLKILLVINGLEVMFRNTQFKSSQERAHLLLRDILLRLR
VMANTYNDEPLSLKTLLLFPKQELPVSLSKPNHNTKTPGKRMKKRRINNGNSLGEYVSKFYADRLL
>gnl|CDD|410887 cd19479, Elp456, Elongator subcomplex subunits Elp4, 5 and 6. Elongator is a highly conserved multiprotein complex involved in RNA polymerase II-mediated transcriptional elongation and many other processes, including cytoskeleton organization, exocytosis, and tRNA modification. It is composed of two subcomplexes, Elp1-3 and Elp4-6. Elp4-6 forms a heterohexameric RecA-like ring structure, although they lack the key sequence signatures of ATPases
FLITHQSCTQPLWLINAFVEQHVLGSPSSLNESDLPSSTRSHAVLASFIHEQNYFTNSLNKLKIPSNNYN
FIDFTQKILSDVLAQISAAIQNNQPKDTIVIIESLELLLSLVSGLTCSELINKFITPLLSQCKVLIAVSN
SDIFNIDEYDASVHSSNLPNFLKLLFIKSTINLNL
>gnl|CDD|410888 cd19480, Psy3, Shu complex subunit Psy3. Psy3, together with Shu1, Shu2, and Csm2, form the Shu complex which is thought to play a role in maintaining genome stability by linking error-free PRR to homologous recombination (HR)
DVLKNCRIYPLSNFYKPTEQYINLPNLLINNTNELDTSKIGFLHLIEHSFKLSKFKKQLVNTNLGDDDES
ILIIDIISIWKQFLLHKNEQGVHYLNSISILNFEGLINFLSQLNDSPDEALRRCQIIDANLDQQLSGIII
DNLSYLQFDNNLSSFETLIKILKKLRETFGCWIITTSYGLEYYEGVENTTSTKYGRSGSPTRLPISYLKG
MDLILLRE
>gnl|CDD|410889 cd19481, RecA-like_protease, proteases similar to RecA. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGES
EKNLRKIFERARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPD
LLDPALLRPGRFDEVIEF
>gnl|CDD|410890 cd19482, RecA-like_Thep1, RecA-like domain of the nucleoside-triphosphatase THEP1 family. This family represents the THEP1 family ATPase domain. It includes nucleoside-triphosphatase THEP 1 from Aquifex aeolicus (aaTHEP1) a nucleoside-phosphatase, with activity towards ATP, GTP, CTP, TTP and UTP; and which may hydrolyze nucleoside diphosphates with lower efficiency. The catalytic function of aaTHEP1 remains unclear, it may be a DNA/RNA modifying enzyme. Human THEP1 (hsTHEP1) may have a general function in many human tissues, as it is widely expressed in most examined tissues (such as in brain, heart, lymph node, skin, pancreas); it is especially highly expressed in embryonic and various tumor tissues. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
IFITGPPGVGKTTLVLKVAELLKESGLKVGGFYTPEVREGGKRIGFKIVDLASGERGWLARVGAGSPKVG
KYGVDVDELEEIAVPALRRALEEADVIIIDEIGPMELKSPKFREAVEEVLKSDKPLLATVHRRSYPRLAE
IRGLGEVFWLTPENRDALPEEILN
>gnl|CDD|410891 cd19483, RecA-like_Gp4D_helicase, RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase. This family includes the RecA-like domain of the Gp4D fragment of the Gene4 helicase-primase (Gp4) from bacteriophage T7. Gp4D (residues 241-566) is the minimal fragment of the Gp4 that forms hexameric rings, it contains the helicase domain and the linker connecting the helicase and primase domains. Helicases are ring-shaped oligomeric enzymes that unwind DNA at the replication fork; they couple NTP hydrolysis to the unwinding of nucleic acid duplexes into their component strands. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
VTIGAGSGIGKSTIVRELAYHLITEHGEKVGIISLEESVEETAKGLAGKHLGKPEPLELPRDDITEEEED
DAFDNELGSGRFFLYDHFGSLDWDNLKEKIRYMVKVLGCKVIVLDHLTILVSGLDSSDERKELDEIMTEL
AALVKELGVTIILVSHLRRPGGGKGHEEGGEVSESDLRGSSAIAQLSDYVIGLERNKQADDPVERNTTRV
RVLKNRFTGETGIAGTLYYDE
>gnl|CDD|410892 cd19484, KaiC_C, C-terminal domain of Circadian Clock Protein KaiC. KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation
ISTGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLIRNAKSI
GIDLEQMERKGLLKIICARPELYGLEDHLIIIKSEINEFKPSRVIVDPLSALARGGSLNEVKEFVIRLID
YLKSQEITGLFTNLTPDGGSLEITEAGISSLTDTWILLRYVEINGERNRGLYVLKMRGMAHSNQIREFSI
SDKGIDIG
>gnl|CDD|410893 cd19485, KaiC-N, N-terminal domain of Circadian Clock Protein Kaic. KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation
LPTGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQFLVNGIKEFGEPGVFVTFEESPEDIIKNMASF
GWDLPKLVAEGKLLILDASPEPSEEEVTGEYDLEALLIRIEYAIRKIGAKRVSLDSLEAVFSGLSDSAVV
RAELLRLFAWLKQKGVTAIMTGERGEDGPLTRYGVEEYVSDCVVILRNVLEGERRRRTLEILKYRGSSHG
KGEYPFTITENGISIL
>gnl|CDD|410894 cd19486, KaiC_arch, KaiC family protein; uncharacterized subfamily similar to Pyrococcus horikoshii PH0284. KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation
VKTGIPGMDEILHGGIPERNVVLLSGGPGTGKSIFSQQFLWNGLKEGEPGVFVALEEHPVQVRRNMEQFG
WDVREYEREGKFAIVDAFTGGIGEAAEREKYVVKDPDDVRELIDVLRQAIRDIGAKRVVIDSVTTLYITK
PAMARRIVMQLKRVLSGLGCTSIFVSQVSVGERGFGGPGVEHAVDGIIRLDLDEVDGELKRSLIVWKMRG
TKHSMRRHPFEITDKGIIVY
>gnl|CDD|410895 cd19487, KaiC-like_C, C-terminal domain of KaiC family protein; uncharacterized subfamily. KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation
VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTLFERSEALG
IDLRAMVEKGLLSIEQIDPAELSPGEFAQRVRTSVEQEDARVVVIDSLNGYLNAMPDERFLILQMHELLS
YLNNQGVTTLLIVAQHGLLGGDMGTPVDISYLADTVVLLRYFEAEGEVRKAISVLKKRTGDHERTIREFR
ITRSGLKVG
>gnl|CDD|410896 cd19488, KaiC-like_N, N-terminal domain of KaiC family protein; uncharacterized subfamily. KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation
ISTGIPGLDDILRGGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYITLSETEQELRAVALSHG
WSLDGIHIFELSPSESALDAAQQYTILHPSELELSETTRLIFERVERLKPSRVVIDSLSELRLLAQDSLR
YRRQILALKQFFAGRNTTVLLLDDLTSDAADLDLHSIAHGVIRLEQLESDYGAARRRLRVSKMRGSSFRG
GYHDFRITRGGLQVF
>gnl|CDD|410897 cd19489, Rad51D, RAD51D recombinase. RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51D, together with the other RAD51 paralogs, RAD51B, RAD51C, XRCC3, and XRCC2, helps recruit RAD51 to the break site
GGGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVLYIDTKSSFSARRLAQILKSRAQDAEEIDKA
LQRIRVVRVFDPYELLDLLEELRNTLSQQQENLYSRLKLVIIDSLSALISPLLGGSKHSEGHALLASLAR
LLKKLAAEYQIAVLVTNLTVRGGDGGQQGSTKPALGEYWESVPSTRLLLSRDENDPEESGVCTATLLKS
>gnl|CDD|410898 cd19490, XRCC2, XRCC2 recombinase. XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells 2) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC2, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC3, helps recruit RAD51 to the break site
GDVIEITGPSGSGKTELLYHLAARCILPSSWGGVPLGGLEAAVVFIDTDGRFDILRLRSILEARIRAAIQ
AANSSDDEEDVEEIARECLQRLHIFRCHSSLQLLATLLSLENYLLSLSANPELGLLLIDSISAFYWQDRF
SAELARAAPLLQEAALRAILRELRRLRRRFQLVVIATKQALFPGKSASTDNPAANNAVSKASAPSHREYL
PRPWQRLVTHRLVLSR
>gnl|CDD|410899 cd19491, XRCC3, XRCC3 recombinase. XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells 3) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC3, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC2, helps recruit RAD51 to the break site
LDELLGGGIPVGGITEIAGESGAGKTQLCLQLALTVQLPRELGGLGGGAVYICTESSFPSKRLQQLASSL
PKRYHLEKAKNFLDNIFVEHVADLETLEHCLNYQLPALLERGPIRLVVIDSIAALFRSEFDTSRSDLVER
AKYLRRLADHLKRLADKYNLAVVVVNQVTDRFDSSSDASGLGVLDYLSQFSSFSGGVSGNRKVPALGLTW
ANLVNTRLMLSRTPKRITDSSAASISVRRLEVVFSPHLPP
>gnl|CDD|410900 cd19492, Rad51C, RAD51C recombinase. RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51C, together with the other RAD51 paralogs, RAD51B, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site. Additionally, RAD51C acts as a mediator in the early steps of DNA damage signaling
GKITEICGVPGVGKTQLCMQLAVNVQIPKCFGGLAGEAIYIDTEGSFNIHYFRVHDYVELLALINSLPKF
LEDHPKVKLIVVDSIAFPFRHDFDDLAQRTRLLNGLAQLLHSLARQHNLAVVLTNQVTTKISEDGQSQLV
PALGESWSHACTTRLFLTWDEKQRFAHLYKSP
>gnl|CDD|410901 cd19493, Rad51B, RAD51B recombinase. RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site
DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAMPARKGGLDGGVLYIDTESKFSAERLAEIAEARF
PEAFSGFMEENERAEEMLKRVAVVRVTTLAQLLERLPNLEEHILSSGVRLVVIDSIAALVRREFGGSDGE
VTERHNALAREASSLKRLAEEFRIAVLVTNQATTHFGDAGDGSSGVTAALGDAWAHAVNTRLRLERCLLQ
LRRVLEIVKSPL
>gnl|CDD|410902 cd19494, Elp4, Elongator subcomplex subunit Elp4. Elongator is a highly conserved multiprotein complex involved in RNA polymerase II-mediated transcriptional elongation and many other processes, including cytoskeleton organization, exocytosis, and tRNA modification. It is composed of two subcomplexes, Elp1-3 and Elp4-6. Elp4-6 forms a heterohexameric RecA-like ring structure, although they lack the key sequence signatures of ATPases
GTRPSPHNSQLLTSTGIASLDDLLGGGLPLGSLLLIEEDSHSSYAKLLLKYFLAEGLVSGHHVFVASADD
DPFEFLRELPGPVSDSEAAEDDEDDASAAAGNEEDMKIAWRYQNLKKVETSVSSSSSSPDYCHTFDLTKR
MDPEALSASELTCIDPEPLSSASSPYDTLLSQIQELLSASGFGSPKNVLRIAIPSLGSPLWGDDESSSEL
LKFLHALRSLLRSSNAVAMITVPSHLYDSPALVARLRHLADAVIELESF
>gnl|CDD|410903 cd19495, Elp6, Elongator subcomplex subunit Elp6. Elongator is a highly conserved multiprotein complex involved in RNA polymerase II-mediated transcriptional elongation and many other processes, including cytoskeleton organization, exocytosis, and tRNA modification. It is composed of two subcomplexes, Elp1-3 and Elp4-6. Elp4-6 forms a heterohexameric RecA-like ring structure, although they lack the key sequence signatures of ATPases
KLILITDTLGTSGSFLLHSLLENALKGGPEKVCLVVVLQSFSHYDFVGKKLGKNLLDLKKSGNFTFIDGL
SDLVSENIGSQLPKSNSKVLKSLFEQIVSAIENSNSPVVVIIDDPELLLSLGVSLSEELLKFILYLRKLV
CSNSSLVVLTHADSPLIDEEEQTRFLNKLAHKADLVISVRPLDTGRAKDVTGVLTITRGGNSFEKSVHVV
EKEYLYKVKDSGVKLFAR
>gnl|CDD|410904 cd19496, Elp5, Elongator subcomplex subunit Elp5. Elongator is a highly conserved multiprotein complex involved in RNA polymerase II-mediated transcriptional elongation and many other processes, including cytoskeleton organization, exocytosis, and tRNA modification. It is composed of two subcomplexes, Elp1-3 and Elp4-6. Elp4-6 forms a heterohexameric RecA-like ring structure, although they lack the key sequence signatures of ATPases
ILILDSLEQSSRPLLNEFVRRALSRSTNVVYVSFETLNKPSYADHFIDATSKSLQELIKEIKSYLPSPSQ
TKKKVLVIIDSLNYILLHSNSSLAQFLSSLASPGHVSVLGTYHSDLPESSDSNAYYPSPLKLLQFMATTI
LTV
>gnl|CDD|410905 cd19497, RecA-like_ClpX, ATP-dependent Clp protease ATP-binding subunit ClpX. ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQKDDDVELEKSNILLIGPTGSGKTLLAQTL
AKILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDV
SGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFGAE
TSSEKDEKERDELLSKVEPEDLIKFGLIPEFVGRLPVIVTL
>gnl|CDD|410906 cd19498, RecA-like_HslU, ATP-dependent protease ATPase subunit HslU. HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLA
GAPFIKVEATKFTEVGYVGRDVESIIRDLVEGIVFIDEIDKIAKRGGSSGPDVSREGVQRDLLPIVEGST
VSTKYGPVKTDHILFIAAGAFHVAKPSDLIPELQGRFPIRVEL
>gnl|CDD|410907 cd19499, RecA-like_ClpB_Hsp104-like, Chaperone protein ClpB/Hsp104 subfamily. Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDED
NLIRIDMSEYMEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDG
RLTDSHGRTVDFKNTIIIMTSNHFRPEFLNRIDEIVVF
>gnl|CDD|410908 cd19500, RecA-like_Lon, lon protease homolog 2 peroxisomal. Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISL
GGVRDEAEIRGHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTF
SDHYLDVPFDLSKVLFIATANSLDTIPGPLLDRMEIIELSGY
>gnl|CDD|410909 cd19501, RecA-like_FtsH, ATP-dependent zinc metalloprotease FtsH. FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG
SDFVEMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESN
TGVIVIAATNRPDVLDPALLRPGRFDRQVYV
>gnl|CDD|410910 cd19502, RecA-like_PAN_like, proteasome activating nucleotidase PAN and related proteasome subunits. This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVG
SELVQKYIGEGARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPR
GNIKVIMATNRPDILDPALLRPGRFDRKIEF
>gnl|CDD|410911 cd19503, RecA-like_CDC48_NLV2_r1-like, first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains. CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSI
VSKYLGESEKNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVI
AATNRPDAIDPALRRPGRFDREVEI
>gnl|CDD|410912 cd19504, RecA-like_NSF-SEC18_r1-like, first of two ATPase domains of NSF and SEC18, and similar ATPase domains. N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
GIGGLDKEFSDIFRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVNGP
EILNKYVGESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSKI
DGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI
>gnl|CDD|410913 cd19505, RecA-like_Ycf2, ATPase domain of plant YCF2. Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
KPFSLRLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKPDFGNDDWIDGMLILKES
LHRLNLQFELAKAMSPCIIWIPNIHELNVNRSTQNLEEDPKLLLGLLLNYLSRDFEKSSTRNILVIASTH
IPQKVDPALIAPNRLDTCINI
>gnl|CDD|410914 cd19506, RecA-like_IQCA1, ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1). IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
DVRQLLTLYGILPLGSQAVHEKAPLVKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKN
GLQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPKTEKQLDPKRLKKDLPKILKSLKPEDRVLIVGTTS
RPFEADLKSFCKVYNKIILI
>gnl|CDD|410915 cd19507, RecA-like_Ycf46-like, ATPase domain of Ycf46 and similar ATPase domains. Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
DVGGLDNLKDWLKKRKAAFSKQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGG
LVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGDSGTSSRVLGTFLTWLQEKKKPVFVVATAN
NVQSLPPELLRKGRFDEIFFV
>gnl|CDD|410916 cd19508, RecA-like_Pch2-like, ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains. Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
AANHWLLPAAEFHGLWESLIYDSNLKSRLLDYVTTTLLFSDKNVNTNLITWNRLVLLHGPPGTGKTSLCK
ALAQKLSIRLSSRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQELIDDKDALVFVLIDEVESLAAA
RSASSSGTEPSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFVDRADIKQYI
>gnl|CDD|410917 cd19509, RecA-like_VPS4-like, ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains. This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVS
KWVGESEKIVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVL
GATNRPWELDEAFLRRFEKRIYI
>gnl|CDD|410918 cd19510, RecA-like_BCS1, Mitochondrial chaperone BCS1. Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTDDRLNHLL
NTAPKQSIILLEDIDAAFESREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPA
LIRPGRVDMKIYM
>gnl|CDD|410919 cd19511, RecA-like_CDC48_r2-like, second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains. This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGE
SERAVREIFQKARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRP
DMIDPALLRPGRLDKLIYV
>gnl|CDD|410920 cd19512, RecA-like_ATAD3-like, ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains. ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIH
KVFDWANTSRRGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAI
NDRIDEMVEF
>gnl|CDD|410921 cd19513, Rad51, RAD51D recombinase. RAD51 recombinase plays an essential role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51 is recruited to the break site with the help of its paralogs, RAD51D, RAD51B, RAD51C, XRCC3, and XRCC2, where it forms long helical polymers which wrap around the ssDNA tail at the break which leads to pairing and strand invasion
ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLCHTLAVTCQLPIDQGGGEGKALYIDTEGTFRPERL
LAIAERYGLNGEDVLDNVAYARAYNTDHQMQLLIQASAMMAESRYALLIVDSATALYRTDYSGRGELSAR
QMHLAKFLRMLQRLADEFGVAVVITNQVVAQVDGAAMFAGDPKKPIGGNIMAHASTTRLYLRKGRGETRI
CKIYDSPCLPEAEAVFAITEDGIGD
>gnl|CDD|410922 cd19514, DMC1, homologous-pairing protein DMC1. DMC1 has a central role in homologous recombination in meiosis. It assembles at the sites of programmed DNA double-strand breaks and carries out a search for allelic DNA sequences located on homologous chromatids. It forms octameric rings
ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLSHTLCVTAQLPGSMGGGGGKVAYIDTEGTFRPDRI
RPIAERFGVDHDAVLDNILYARAYTSEHQMELLDYVAAKFHEEAVFRLLIIDSIMALFRVDFSGRGELAE
RQQKLAQMLSRLQKISEEYNVAVFITNQVTADPGAAMTFQADPKKPIGGHILAHASTTRISLRKGRGEER
IAKIYDSPDLPENEATFAITAGGIAD
>gnl|CDD|410923 cd19515, archRadA, archaeal recombinase Rad51/RadA. This group includes the archaeal protein RadA which is a homolog of Rad51. RAD51 recombinase plays an essential role in DNA repair by homologous recombination (HR)
ISTGSKELDKLLGGGIETQAITEVFGEFGSGKTQLCHQLAVNVQLPPEEGGLNGKAVYIDTENTFRPERI
MQMAKALGLDPDEVLDNIYVARAYNSNHQMLLVEKAEDLIKEGNNIKLLIVDSLTSHFRAEYVGRGTLAE
RQQKLNKHLHDLHRLADLYNIAVLVTNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRKGKGGKRIAR
LVDSPHLPEGEAVFRITEKGIED
>gnl|CDD|410924 cd19516, DotB_TraJ, dot/icm secretion system protein DotB-like. Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon
PDLVEALFPREGLVYVAGATGSGKSTLLAAIYRYILENDPPDRKIITYEDPIEFVYDGIKSKHSIIVQSQ
IPRHFKSFAKAVREALRRKPSLIGVGELRDQETISAAVEASLTGHPVYSTVHTKSVAETIRRLISLFPPE
ERDAAAYDLLSTLRFIIVQRLVRTTDGKRVAVREYLVFD
>gnl|CDD|410925 cd19517, RecA-like_Yta7-like, ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains. Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSFFMR
KGADCLSKWVGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRG
QVVVIGATNRPDALDPALRRPGRFDREFYF
>gnl|CDD|410926 cd19518, RecA-like_NVL_r1-like, first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains. NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEI
VSGVSGESEEKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTAGGP
VLVIGATNRPDSLDPALRRAGRFDREICL
>gnl|CDD|410927 cd19519, RecA-like_CDC48_r1-like, first of two ATPase domains of CDC48 and similar ATPase domains. CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEI
MSKLAGESESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVM
AATNRPNSIDPALRRFGRFDREIDIG
>gnl|CDD|410928 cd19520, RecA-like_ATAD1, ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains. ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
DIGGLDEVITELKELVILPLQRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSS
LTDKWYGESQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRV
IVMGATNRPQDLDEAILRRMPKRFHI
>gnl|CDD|410929 cd19521, RecA-like_VPS4, ATPase domain of vacuolar protein sorting-associated protein 4. Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFS
VSSSDLVSKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGND
SQGVLVLGATNIPWQLDSAIRRRFEKRIYI
>gnl|CDD|410930 cd19522, RecA-like_KTNA1, Katanin p60 ATPase-containing subunit A1. Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLT
SKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDP
SKMVMVLAATNFPWDIDEALRRRLEKRIYI
>gnl|CDD|410931 cd19523, RecA-like_fidgetin, ATPase domain of fidgetin. Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLV
AKWAGEGEKILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQVELLAQLDGVLGSGEDGVLVV
CTTSKPEEIDESLRRYFSKRLLV
>gnl|CDD|410932 cd19524, RecA-like_spastin, ATPase domain of spastin. Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT
SKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLV
MGATNRPQELDDAVLRRFTKRVYV
>gnl|CDD|410933 cd19525, RecA-like_Figl-1, ATPase domain of Fidgetin-Like 1 (FIGL-1). FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTL
IGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRR
IKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVKRLYI
>gnl|CDD|410934 cd19526, RecA-like_PEX1_r2, second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1). PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGA
SEQNVRDLFSRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPD
LIDPALLRPGRLDKLVYC
>gnl|CDD|410935 cd19527, RecA-like_PEX6_r2, second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6). PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
VKKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGES
EANVREVFQKARDAKPCVIFFDELDSLAPSRGNSGDSGGVMDRVVSQLLAELDGMSSSGQDVFVIGATNR
PDLLDPALLRPGRFDKLLYL
>gnl|CDD|410936 cd19528, RecA-like_CDC48_r2-like, second of two ATPase domains of CDC48 and similar ATPase domains. CDC48 in yeast and p97 or VCP in metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGE
SEANVRDIFDKARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATN
RPDIIDPAILRPGRLDQLIYI
>gnl|CDD|410937 cd19529, RecA-like_VCP_r2, second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains. The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGE
SEKAIREIFRKARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRP
DIIDPALLRAGRFDRLIYI
>gnl|CDD|410938 cd19530, RecA-like_NVL_r2-like, second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains. NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKY
VGESERAVRQVFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATN
RPDIIDPAMLRPGRLDKTLYV
>gnl|CDD|380454 cd19531, LCL_NRPS-like, LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains
PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVI
LPPLPLPLPVVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDG
WSMGVLLRELAALYAAFLAGRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPT
DRPRPAVQSFRGARVRFTLPAELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNR
AELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVM
FVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYNTDLFDAATIERMAGHFQTLL
EAIVADP
>gnl|CDD|380455 cd19532, C_PKS-NRPS, Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs). Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain
TEPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPMQ
GVLASSPLRLEHVQISDEAEVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQ
IFLRDLERAYNGQPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEPLPLLPFAKVKSRPPL
TRYDTHTAERRLDAALAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETI
GFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGV
AESRPFGDCELEGEEFEDARTPYDLSLDIIDNPDGDCLLTLKVQSSLYSEEDAELLLDSYVNLLEAFARD
P
>gnl|CDD|380456 cd19533, starter-C_NRPS, Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs). Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity
RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWI
DPYTPVPIRHIDLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFS
FALFGQRVAEIYTALLKGRPAPPAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARRAP
GRSLAFLRRTAELPPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQT
PGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRHQRYRYEDLRRDLGLTGELHPLFGPTVNYMPFDY
GLDFGGVVGLTHNLSSGPTNDLSIFVYDRDDESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP
>gnl|CDD|380457 cd19534, E_NRPS, Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family. Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity
EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRG
DVEELFRLEVVDLSSLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWR
ILLEDLEAAYEQALAGEPIPLPSKTSFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQTYG
DARTVSFTLDEEETEALLQEANAAYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSR
TVGWFTSMYPVVLDLEASEDLGDTLKRVKEQLRRIPNKGIGYGILRYLTPEGTKRLAFHPQPEISFNYLG
QFDQGERDDALFVSAVGGGGSDIGPDTPRFALLDINAVVEGGQLVITVSYSRNMYHEETIQQLADSYKEA
LEALIEHC
>gnl|CDD|380458 cd19535, Cyc_NRPS, Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family. Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain
PFPLTDVQYAYWIGRQDDQELGGVGCHAYLEFDGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQQILP
EVPWYGITVHDLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADAL
SLQILLRELAALYEDPGEPLPPLELSFRDYLLAEQALRETAYERARAYWQERLPTLPPAPQLPLAKDPEE
IKEPRFTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVN
DVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSYSGVVVVRRLLRRRGGQPVLAPVVFTSNL
GLPLLDEEVREVLGELVYMISQTPQVWLDHQVYEEDGGLLLNWDAVDELFPEGMLDDMFDAYVRLLERLA
DDD
>gnl|CDD|380459 cd19536, DCL_NRPS-like, DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains. Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity
MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQV
VHRQAQVPVTELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLVISDHHSILDG
WSLYLLVKEILAVYNQLLEYKPLSLPPAQPYRDFVAHERASIQQAASERYWREYLAGATLATLPALSEAV
GGGPEQDSELLVSVPLPVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAER
LLGLFLNTLPLRVTLSEETVEDLLKRAQEQELESLSHEQVPLADIQRCSEGEPLFDSIVNFRHFDLDFGL
PEWGSDEGMRRGLLFSEFKSNYDVNLSVLPKQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP
>gnl|CDD|380460 cd19537, C_NRPS-like, Condensation family domain with an atypical active site motif. Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain
DTALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSY
SSSPPRVQRVDTLDVWKEINRPFDLEREDPIRVFISPDTLLVVMSHIICDLTTLQLLLREVSAAYNGKLL
PPVRREYLDSTAWSRPASPEDLDFWSEYLSGLPLLNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSS
GITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPSSSDASAADFLRA
VRRSSQAALAHAIPWHQLLEHLGLPPDSPNHPLFDVMVTFHDDRGVSLALPIPGVEPLYTWAEGAKFPLM
FEFTALSDDSLLLRLEYDTDCFSEEEIDRIESLILAALELLVEGK
>gnl|CDD|380461 cd19538, LCL_NRPS, LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains
EIPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLI
LEEDEATPKLEIKEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAP
LTRDLSKAYRARCKGEAPELAPLPVQYADYALWQQELLGDESDPDSLIARQLAYWKKQLAGLPDEIELPT
DYPRPAESSYEGGTLTFEIDSELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRND
DSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIM
LALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREQYNDGTPNGIEGFIEYRTDLFDHETIEALAQR
YLLLLESAVENP
>gnl|CDD|380462 cd19539, SgcC5_NRPS-like, SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs. SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity
RIPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQE
ILPPGPAPLEVRDLSDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDA
WSLDVFARDLAALYAARRKGPAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEPTALPTD
RPRPAGFPYPGADLRFELDAELVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHP
RFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVF
QVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYATSLFDEETIQGFLADYLQVL
RQLLANP
>gnl|CDD|380463 cd19540, LCL_NRPS-like, LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains
RIPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVV
LPAAEARPDLTVVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAP
LARDLATAYAARRAGRAPDWAPLPVQYADYALWQRELLGDEDDPDSLAARQLAYWRETLAGLPEELELPT
DRPRPAVASYRGGTVEFTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGD
EALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVM
LAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTERRDADGAPAGLTGELEYATDLFDRSTAERLAD
RFVRVLEAVVADP
>gnl|CDD|380464 cd19542, CT_NRPS-like, Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs). Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain
IYPCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVV
LKSLDPPIEEVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILR
DLAAAYNGQLLPPAPPFSDYISYLQSQSQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSSTRRSLAK
LEAFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDW
TVLDLLRQLQQQYLRSLPHQHLSLREIQRALGLWPSGTLFNTLVSYQNFEASPESELSGSSVFELSAAED
PTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLANP
>gnl|CDD|380465 cd19543, DCL_NRPS, DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity
IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQV
VLKDRKLPWRELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLD
GWSLPILLKELFAIYAALGEGQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPA
DADGSYEPGEVSFELSAELTARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPG
IETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELREHEYVPLYEIQAWSEGKQALFDHLLVFENYP
VDESLEEEQDEDGLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVA
ANP
>gnl|CDD|380466 cd19544, E-C_NRPS, Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs). Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain
IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEGLSEPVQV
VWRQAELPVEELTLDPGDDALAQLRARFDPRRYRLDLRQAPLLRAHVAEDPANGRWLLLLLFHHLISDHT
SLELLLEEIQAILAGRAAALPPPVPYRNFVAQARLGASQAEHEAFFREMLGDVDEPTAPFGLLDVQGDGS
DITEARLALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALG
MFINTLPLRVRLGGRSVREAVRQTHARLAELLRHEHASLALAQRCSGVPAPTPLFSALLNYRHSAAAAAA
AALAAWEGIELLGGEERTNYPLTLSVDDLGDGFSLTAQVVAPIDAERVCAYMETALEQLVDAL
>gnl|CDD|380467 cd19545, FUM14_C_NRPS-like, Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein. Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain
IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVV
KESPISWTESTSLDEYLEEDRAAPMGLGGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAA
YQGEPVPQPPPFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLEHSISLPSSAS
SGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQ
TVQKDLLDMIPFEHTGLQNIRRLGPDARAACNFQTLLVVQPALPSSTSESLELGIEEESEDLEDFSSYGL
TLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP
>gnl|CDD|380468 cd19546, X-Domain_NRPS, X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS). The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif
RPDEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVH
QRILDADAARPELPVVPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDES
LDVLVRDLAAAYGARREGRAPERAPLPLQFADYALWERELLAGEDDRDSLIGDQIAYWRDALAGAPDELE
LPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPR
DDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELLALPPSADRHPV
FQVALDVRDDDNDPWDAPELPGLRTSPVPLGTEAMELDLSLALTERRNDDGDPDGLDGSLRYAADLFDRA
TAAALARRLVRVLEQVAADP
>gnl|CDD|380469 cd19547, beta-lac_NRPS, Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis. Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site
VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQY
VRDDLAPPWALLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLD
GWCLSLIWGDVFRVYEELAHGREPQLSPCRPYRDYVRWIRARTAQSEESERFWREYLRDLTPSPFSTAPA
DREGEFDTVVHEFPEQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSE
HMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTAAHGHVPLAQIKSWASGERLSGGRVFDNLVAFEN
YPEDNLPGDDLSIQIIDLHAQEKTEYPIGLIVLPLQKLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCR
RP
>gnl|CDD|381016 cd19548, serpinA_A1AT-like, serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles. The alpha-1-antitrypsin family has a variety of different members of sauropsida belonging to the clade A of the serpin superfamily. This branch includes members from zebra finch, green anole, king cobra, gekko, crocodile, and central bearded dragon. Alpha-1-antitrypsin (also called A1AT, A1A, AAT, alpha1-proteinase inhibitor/A1PI, alpha1-antiproteinase/A1AP, and serum trypsin inhibitor) is a protease inhibitor. Clade A includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
YLKIAPNNADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNLSEIEEKEI
HEGFHHLLHMLNRPDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEAEKQINDYVE
NKTHGKIVDLVKDLDPDTVMVLVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFD
EDLSCTVVQIPYKGDASALFILPDEGKMKQVEAALSKETLSKWAKSLRRQRINLSIPKFSISTSYDLKDL
LQKLGVTDVFTDNADLSGITGERNLKVSKAVHKAVLDVHESGTEAAAATAIEIVPTSLPPEPKFNRPFLV
LIVDKLTNSILFLGKIVNPT
>gnl|CDD|381017 cd19549, serpinA_A1AT-like, serpin family A member, alpha-1-antitrypsin and similar proteins. This group contains proteins similar to alpha-1-antitrypsin (also called A1AT, A1A, AAT, alpha1-proteinase inhibitor/A1PI, alpha1-antiproteinase/A1AP, and serum trypsin inhibitor), a protease inhibitor that belongs to the serpin superfamily. It is encoded in humans by the SERPINA1 gene. When the blood contains inadequate amounts of A1AT or functionally defective A1AT (such as in alpha-1 antitrypsin deficiency), neutrophil elastase is excessively free to break down elastin, degrading the elasticity of the lungs, which results in respiratory complications, such as chronic obstructive pulmonary disease. Normally, A1AT leaves its site of origin, the liver, and joins the systemic circulation; defective A1AT can fail to do so, building up in the liver, which results in cirrhosis. This group belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
ANSDFAFRLYKHLASQPDSQGKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSSQVTQAQVNEAF
EHLLHMLGHSEELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTEAADTINKYVAKKTHG
KIDKLVKDLDPSTVMYLISYIYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEIST
TVLRLPYNGSASMMLLLPDKGMATLEEVICPDHIKKWHKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGM
TDMFGDSADLSGISEEVKLKVSEVVHKATLDVDEAGATAAAATGIEIMPMSFPDAPTLKFNRPFMVLIVE
HTTKSILFMGKITNPTE
>gnl|CDD|381018 cd19550, serpinA2_PIL, serpin family A member 2, protease inhibitor 1-like. Protease inhibitor 1-like (also called serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 2, ARGS, protease inhibitor 1 (alpha-1-antitrypsin)-like)/PIL, and alpha-1-antitrypsin-related protein/ATR) belongs to the serpin superfamily and is encoded by the SERPINA2 gene in humans. SERPINA2 was once thought to be a pseudogene, but recent evidence shows that it produces an active transcript. It is very similar in structure and function to SERPINA1. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
NIANLAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKETPEAEIHKCFQQ
LLNTLHQPDNQLQLTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRK
IVDLVKDLDKDTALALVNYISFHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMINRLGTFYLHRDEELSSW
VLVQHYVGNATAFFILPDPGKMQQLEEGLTYEHLSNILRHIDIRSANLHFPKLSISGTYDLKTILGKLGI
TKVFSNEADLSGITEEAPLKLSKAVHKAVLTIDENGTEVSGATDLEDKAWSRVLTIKFNRPFLIIIKDEN
TNFPLFMGKVVNP
>gnl|CDD|381019 cd19551, serpinA3_A1AC, serpin family A member 3, alpha 1-antichymotrypsin. Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT/AACT) is an alpha globulin glycoprotein that is a member of the serpin superfamily. In humans, it is encoded by the SERPINA3 gene. It inhibits the activity of proteases, such as cathepsin G that is found in neutrophils, and chymases found in mast cells, by cleaving them into a different shape or conformation. This activity protects some tissues, such as the lower respiratory tract, from damage caused by proteolytic enzymes. Deficiency of this protein has been associated with liver disease. Mutations have been identified in patients with Parkinson disease and chronic obstructive pulmonary disease. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
DKGTQVDSLTLASSNTDFAFSLYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFNLT
ETPEADIHQGFQHLLQTLSQPSDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDPTAAKK
LINDYVKNKTQGKIKELISDLDPRTSMVLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMMKIEN
LTTPYFRDEELSCTVVELKYTGNASALFILPDQGKMQQVEASLQPETLKRWRDSLRPRRIDELYLPKFSI
SSDYNLEDILPELGIREVFSQQADLSGITGAKNLSVSQVVHKAVLDVAEEGTEAAAATGVKIVLTSAKLK
PIIVRFNRPFLVAIVDTDTQSILFLGKVTNPK
>gnl|CDD|381020 cd19552, serpinA4_KST, serpin family A member 4, kallistatin. Kallistatin (KST, also called proteinase inhibitor 4/PI4, or kallikrein inhibitor/KAL) is a protein that in humans is encoded by the SERPINA4 gene. Kallistatin inhibits human amidolytic and kininogenase activities of tissue kallikrein. Heparin blocks kallistatin's complex formation with tissue kallikrein and abolishes its inhibitory effect on tissue kallikrein's activity. Kallistatin was found to be expressed in human liver, stomach, pancreas, kidney, aorta, testes, prostate, artery, atrium, ventricle, lung, renal proximal tubular cell, and a colonic carcinoma cell line T84. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
EASPSLQIAPGNTNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFNLTQLS
EPEIHEGFQHLQHTLNHPNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERLIN
DHVREETRGKISDLVSDLSRDVKMVLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMMLQDQEYH
WYLHDRRLPCSVLRMDYKGDATAFFILPDQGKMREVEQVLSPGMLMRWDRLLQNRYFYRKLELHFPKFSI
SGSYELDQILPELGFQDLFSPNADFSGITKQQKLRVSKSFHKATLDVNEVGTEAAAATSLFTVFLSAQKK
TRVLRFNRPFLVAIFSTSTQSLLFLGKVVNPMK
>gnl|CDD|381021 cd19553, serpinA5_PCI, serpin family A member 5, protein C inhibitor. Protein C inhibitor (PCI/PROCI, also called PAI3, plasminogen activator inhibitor-3/PLANH3, plasma serine protease inhibitor) has many biological functions. It acts as a pro-coagulant in blood and in the seminal vesicles, it is required for spermatogenesis. It is a member of the clade A serpin family that includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
SSRDFAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNPQKGSEEQLHRGFQQ
LLQELNQPRDGFQLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFEDPAGAKKQINDYVAKQTKGK
IVDLIKNLDSTTVMVMVNYIFFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLSCR
VVGVPYQGNATALFILPSEGKMEQVENGLSEKTLRKWLKMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGI
RDVFTSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGMVFTFRSARLNSQRIVFNRPFLMFIV
ENSNILFLGKVTRP
>gnl|CDD|381022 cd19554, serpinA6_CBG, serpin family A member 6, corticosteroid-binding globulin. Corticosteroid-binding globulin (CBG, also known as transcortin) is encoded by the SERPINA6 gene in humans which encodes an alpha-globulin with corticosteroid-binding properties. It is produced in the liver. CBG binds several steroid hormones at high rates including cortisol, cortisone, deoxycorticosterone (DOC), corticosterone, aldosterone, progesterone, and 17a-hydroxyprogesterone. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
SSPHRGLAPNNVDFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFNLTEISE
AEIHQGFQHLHHLLRESDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQINE
YVKNKTQGKIVDLFSELDSPATLILVNYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKY
LHDSELPCQLVQLDYVGNGTVFFILPDKGKMDTVIAALSRDTIQRWSKSLTSSQVDLYIPKVSISGAYDL
GDILEDMGIADLFTNQTDFSGITQDAQLKLSKVVHKAVLQLDEKGVEAAAPTGSTLHLRSEPLTLRFNRP
FIIMIFDHFTWSSLFLGKVVNPA
>gnl|CDD|381023 cd19555, serpinA7_TBG, serpin family A member 7, thyroxine-binding globulin. Thyroxine-binding globulin (TBG, also called T4-binding globulin) is a globulin that binds thyroid hormones in circulation. It is one of three transport proteins (along with transthyretin and serum albumin) responsible for carrying the thyroid hormones thyroxine (T4) and triiodothyronine (T3) in the bloodstream. TBG is synthesized primarily in the liver and is a serpin with no inhibitory function like many other members of this class of proteins. There are two forms of inherited thyroxine-binding globulin deficiency: the complete form (TBG-CD), which results in a total loss of thyroxine-binding globulin, and the partial form (TBG-PD), which reduces the amount of this protein or alters its structure. Neither of these conditions causes any problems with thyroid function, but it can be mistaken for more serious thyroid disorders, such as hypothyroidism. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
ATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDTPMV
EIQQGFQHLICSLNFPKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSAAQQEINSH
VEMQTKGKIVGLIQDLKPNTIMVLVNYIHFKAQWANPFDPSKTEESSSFLVDKTTTVQVPMMHQMEQYYH
LVDMELNCTVLQMDYSKNALALFVLPKEGQMEWVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDL
GATLLKMGIQDAFAENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQPENTFLHPIIQ
IDRSFLLLILEKSTRSILFLGKVVDPTEA
>gnl|CDD|381024 cd19556, serpinA9_centerin, serpin family A member 9, centerin. Centerin, also known as germinal center B-cell-expressed transcript 1/GCET1, is a serpin whose expression is restricted to germinal center B-cells and lymphoid malignancies with germinal center B-cell maturation. Expression of centerin, together with bcl-6 and GCET2, constitutes a germinal center B-cell signature, which is associated with a good prognosis in diffuse large B-cell lymphomas. Centerin is thought to function in vivo in the germinal centre as an efficient inhibitor of a trypsin-like protease. It also inhibits the trypsin-like serine proteases trypsin, thrombin and plasmin and is able to bind heparin and DNA. The centerin gene maps to the A clade serpin cluster on chromosome 14q32.1, which also contains a1-antitrypsin and a1-antichymotrypsin together with seven other serpins. The clade A of the serpin superfamily includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
YPRPSSTKKTPASQVYSLNTDFAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLG
FNLTHTPESAIHQGFQHLVHSLTVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPS
IAQARINSHVKKKTQGKVVDIIQGLDLLTAMVLVNHIFFKAKWEKPFHPEYTRKNFPFLVGEQVTVHVPM
MHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFVLPSKGKMRQLEQALSARTLRKWSHSLQKRWIEVFIPR
FSISASYNLETILPKMGIQNAFDKNADFSGIAKRDSLQVSKATHKAVLDVSEEGTEATAATTTKFIVRSK
DGPSYFTVSFNRTFLMMITNKATDGILFLGKVENPTKS
>gnl|CDD|381025 cd19557, serpinA11, serpin family A member 11. Serpin A11, in rats also called liver regeneration-related protein LRRG023, is a serpin encoded by the gene SERPINA11. It maps on chromosome 14, at 14q32.13 and is strongly expressed in the human liver. The function of this protein is unknown. It belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
VTPTITNFALRLYKQLAEEAPGNILFSPVSLSSTLALLSLGAHADTQAQILESLGFNLTETPAADIHRGF
QSLLHTLDLPSPKLELKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQINDLVRKQTY
GQVVGCLPEFSQDTLMVLLNYIFFKAKWKHPFDRYQTRKQESFFVDQRTSLRIPMMRQKEMHRFLYDQEA
SCTVLQIEYSGTALLLLVLPDPGKMQQVEAALQPETLRRWGQRFLPSLLDLHLPRFSISATYNLEEILPL
IGLTNLFDLEADLSGIMGQLNKTVSRVSHKAMVDMNEKGTEAAAASGLLSQPPSLNMTSAPHAHFNRPFL
LLLWEVTTQSLLFLGKVVNPAAG
>gnl|CDD|381026 cd19558, serpinA12_vaspin, serpin family A member 12, visceral adipose tissue-derived serpin. Vaspin, also called visceral adipose tissue-derived serpin or serpinA12, was identified as an adipokine with insulin-sensitizing effects and has been shown to significantly reduce blood glucose concentrations in various mouse models. As such, vaspin may represent a novel treatment tool for diabetes intervention strategies. Human kallikrein 7 (hK7), which cleaves human insulin within A and B chain, was the first protease target of vaspin inhibited by classical serpin mechanism with high specificity in vitro. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
RGRKAAKELARHNMEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRKMPE
KDLHEGFHYLIHELNQKTQDLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQDLEMAQKQIND
YISQKTHGKINNLVKNIDPGTVMLLANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQV
GYDDQLSCTILEIPYKGNITATFILPDEGKLKHLEKGLQKDTFARWKTLLSRRVVDVSVPKLHISGTYDL
KKTLSYLGVSKIFEEHGDLTKIAPHRSLKVGEAVHKAELKMDEKGTEGAAGTGAQTLPMETPLLVKLNKP
FLLIIYDDKMPSVLFLGKIVNP
>gnl|CDD|381027 cd19559, serpinA14_UTMP_UABP-2, serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2. The uteroferrin(Uf)-associated basic proteins-2(UABP-2/UABP/UfAP) are a group of three (Mr = 42K, 48K, and 50K) antigenically related, basic glycoproteins secreted by the porcine uterus under the influence of progesterone (P4), which exist as heterodimers (Mr = 80,000) with the iron-binding acid phosphatase, Uf. This group also contains UTMP (uterine milk protein), encoded by SERPINA14. UTMP binds noncovalently to the iron-containing glycoprotein uteroferrin, which displays phosphatase activity and is thought to be involved with iron transport to the fetus. Synthesis of these serpins is induced by progesterone in the uterus. UTMP is also an activin-binding protein and has been implicated in regulation of uterine immune function. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
NPVSSKRISPLSQKMEADHKAFAQKLFKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLG
FDLKNIRVWDVHQSFQHLVQLLHELVRQKQLKHQDILFIDSNRKINQMFLHEIEKLYKVDIQMIDFRDKE
KAKKQINHFVAEKMHKKIKELITDLDPHTFLCLVNYIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMM
RKTERMIYSRSEELFATMVKMPCKGNVSLVLVLPDAGQFDSALKEMAAKRARLQKSSDFRLVHLILPKFK
ISSKIDLKHLLPKIGIEDIFTTKANFSGITEEAFPAILEAVHEARIEVSEKGLTKDAAKHMDNKLAPPAK
QKAVPVVVKFNRPFLLFVEDEKTQRDLFVGKVFNPK
>gnl|CDD|381028 cd19560, serpinB1_LEI, serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI). Leukocyte elastase inhibitor (LEI, also known as proteinase inhibitor 2/PI2, monocyte neutrophil elastase inhibitor/MNEI, EI, or ELANH2) is a member of the clade B serpins or ov-serpins (ovalbumin related serpins) that in humans is encoded by the SERPINB1 gene. Human SERPINB1 is a potent intracellular inhibitor for granzyme H (GzmH) which is constitutively expressed in NK cells and induces target cell death. GzmH cleaves SERPINB1 at Phe343 in the RCL to mediate suicide inhibition. Equine leukocyte elastase inhibitor (HLEI) in contrast to other serpins contains no carbohydrate and has a blocked amino terminus. HLEI is a thymosin beta4-binding protein suggesting a physiological role for cytoplasmic elastase inhibitors in the thymosin B4-regulated rearrangement of the cytoskeleton of leukocytes. HLEI has been proposed to be involved with the control of intracellular protein turnover or the control of elastinolytic activity during inflammation. Ov-serpins are a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSRF
QSLNAEINKRGASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQT
EGKIPELLASGVVDSMTKLVLVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIP
ELKCRVLELPYVGKELSMVILLPDDIEDESTGLKKLEKQLTLEKLHEWTKPENLMNIDVHVHLPRFKLEE
SYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVHKSFVEVNEEGTEAAAATAGIAMFCMLMPEE
EFTADHPFLFFIRHNPTNSILFFGRYSSP
>gnl|CDD|381029 cd19562, serpinB2_PAI-2, serpin family B member 2, plasminogen activator inhibitor 2. Plasminogen activator inhibitor-2 (PAI-2/PLANH2, also called placental PAI, monocyte arg-serpin, or urokinase inhibitor) is a serine protease inhibitor that belongs to the ovalbumin family of serpins (ov-serpins). It is an effective inhibitor of urinary plasminogen activator (urokinase or uPA) and is involved in cell differentiation, tissue growth and regeneration. Ov-serpins are a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
EDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAYDLTPG
NPENFTGCDFAQQIQRDNYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEY
IRLCQKYYSSEPQAVDFLECAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTP
FEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTGLEL
LESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSILRSMGMEDAFNKGRANFSGMSERNDLFL
SEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITNCILFFGRFSSP
>gnl|CDD|381030 cd19563, serpinB3_B4_SCCA1_2, serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2. Squamous cell carcinoma antigen 1 (SCCA1, also called HsT1196 or protein T4-A) and squamous cell carcinoma antigen 2 (SCCA2, also called PI11 or leupin), which are encoded by the SERPINB3 and SERPINB4 genes, respectively, are members of the serpin family of serine protease inhibitors. SCCA1 is a so called cross-class serpin, inhibiting cysteine proteinases such as cathepsin S, K, L, and papain. SCCA2 inhibits chymotrypsin-like serine proteases including chymase, cathepsin G, and Der p1. Elevated levels of SCCA1 and SCCA2 have been detected in chronic inflammatory conditions involving the skin, especially atopic dermatitis (AD)and psoriasis, as well as in respiratory inflammatory diseases such as asthma, chronic obstructive pulmonary disease (COPD), and tuberculosis. They are both normally co-expressed in squamous epithelial cells of tongue, esophagus, tonsils, epidermal hair follicles, lung and uterus, and become highly up-regulated in squamous carcinomas of these organs. Diseases associated with SERPINB3 include anal cancer and cervical squamous cell carcinoma, whereas SERPINB4 include squamous cell carcinoma and chromosome 18Q deletion syndrome. The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
MNSLSEANTKFMFDLFQQFRKSKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTENTTGKA
ATYHVDRSGNVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAP
EESRKKINSWVESQTNEKIKNLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSI
QMMRQYTSFHFASLEDVQAKVLEIPYKGKDLSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETRV
DLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGSRGLVLSGVLHKAFVEVTEEGAEAAAATAVV
GFGSSPTSTNEEFHCNHPFLFFIRQNKTNSILFYGRFSSP
>gnl|CDD|381031 cd19565, serpinB6_CAP, serpin family B member 6, cytoplasmic antiproteinase. Cytoplasmic antiproteinase (CAP, also called proteinase inhibitor 6/PI6 or placental thrombin inhibitor/PTI) is thought to be involved in the regulation of serine proteinases present in the brain or extravasated from the blood. It may play an important role in the inner ear in the protection against leakage of lysosomal content during stress; loss of this protection results in cell death and sensorineural hearing loss. It is an inhibitor of cathepsin G, kallikrein-8 and thrombin. The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
MDVLAEANGTFALNLLKTLGKDNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKSSGGGGDIH
QGFQSLLTEVNKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVA
EKTEGKIAELLSPGSVNPLTRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKT
YIGEIFTQILVLPYVGKELNMIIMLPDETTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVFLPRFKLEES
YDMESVLYKLGMTDAFELGRADFSGMSSKQGLFLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPR
FCADHPFLFFIQHSKTNGILFCGRFSSP
>gnl|CDD|381032 cd19566, serpinB7_megsin, serpin family B member 7, megsin. Megsin is named as such due to its primary expression in the mesangium, a structure associated with the capillaries in the glomerulus of the kidney. Megsin is thought to play a role in the regulation of a wide variety of processes in mesangial cells, such as matrix metabolism, cell proliferation, and apoptosis. Identification of the exact biological functions and target proteases of megsin will lead to the development of novel therapeutic approaches to glomerular diseases. Expression of this gene is upregulated in IgA nephropathy and mutations have been found to cause palmoplantar keratoderma, Nagashima type. Megsin belongs to the ovalbumin family of serpins (ov-serpins), a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
MASLAAANAEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTASRYGNSS
NNQPGLQSQLKRVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRR
KINKWIENETHGKIKKVIGESSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQ
ERKFNLSTIQDPPMQVLELQYHGGINMYIMLPENDLSEIENKLTFQNLMEWTNRRRMKSQYVEVFLPQFK
IEKNYEMKHHLKSLGLKDIFDESKADLSGIASGGRLYVSKLMHKSFIEVTEEGTEATAATESNIVEKQLP
ESTVFRADHPFLFVIRKNDIILFTGKVSCP
>gnl|CDD|381033 cd19567, serpinB8_CAP-2, serpin family B member 8, cytoplasmic antiproteinase 2. Cytoplasmic antiproteinase 2 (CAP-2 or peptidase inhibitor 8/PI-8) is a member of the ovalbumin family of serpins (ov-serpins). Serpin B8 is produced by platelets and can bind to and inhibit the function of furin, a serine protease involved in platelet functions. In addition, this protein has been found to enhance the mechanical stability of cell-cell adhesion in the skin, and defects in this gene have been associated with an autosomal-recessive form of exfoliative ichthyosis. Diseases associated with SERPINB8 include Peeling Skin Syndrome 5 and Exfoliative Ichthyosis. Among its related pathways are Response to elevated platelet cytosolic Ca2+ and CFTR-dependent regulation of ion channels in Airway Epithelium (norm and CF). The ov-serpins are a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
MDDLCEANGTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNGDVHRGF
QSLLAEVNKTGTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECRKHINDWVSEKT
EGKISEVLSAGTVCPLTKLVLVNAIYFKGKWNEQFDRKYTRGMPFKTNQEKKTVQMMFKHAKFKMGHVDE
VNMQVLELPYVEEELSMVILLPDENTDLAVVEKALTYEKFRAWTNPEKLTESKVQVFLPRLKLEESYDLE
TFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAHKCFVEVNEEGTEAAAATAVVRNSRCCRMEPRFCAD
HPFLFFIRHHKTNSILFCGRFSSP
>gnl|CDD|381034 cd19568, serpinB9_CAP-3, serpin family B member 9, cytoplasmic antiproteinase 3. Cytoplasmic antiproteinase 3 (CAP-3; peptidase inhibitor 9/PI-9, Spi6, or testicular tissue protein Li 180) is an intracellular inhibitor of granzyme B (grB) that protects cytotoxic lymphocytes from grB-mediated death. It is also thought to be expressed in accessory immune cells, including dendritic cells (DCs), although there is some debate about this. Overexpression of serpin B9 may prevent cytotoxic T-lymphocytes from eliminating certain tumor cells. A pseudogene of this gene is found on chromosome 6. Diseases associated with serpin B9 include chronic obstructive pulmonary disease (COPD) and oral squamous cell carcinoma (OSCC). The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
METLSEASGTFAIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTEKDIHRGF
QSLLTEVNKPGAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAAEESRKHINAWVSKKT
EGKIEELLPGNSIDAETRLVLVNAVYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVG
EVRAQVLELPYAGQELSMLVLLPDDGVDLSTVEKSLTFEKFQAWTSPECMKRTEVEVLLPKFKLQEDYDM
VSVLQGLGIVDAFQQGKADLSAMSADRDLCLSKFVHKSVVEVNEEGTEAAAASSCFVVAYCCMESGPRFC
ADHPFLFFIRHNRTNSLLFCGRFSSP
>gnl|CDD|381035 cd19569, serpinB10_bomapin, serpin family B member 10, bomapin. Bomapin (also called proteinase inhibitor 10/PI10) is a hematopoietic- and myeloid leukaemia-specific protease inhibitor which is thought to augment proliferation or apoptosis of leukemia cells, depending on growth factor availability. Bomapin is expressed only in bone marrow, leukocytes of patients with myeloid leukaemia that correspond to myeloid progenitors, and promyelocytic leukaemia cell lines (HL60, THP1, and AML-193), but it is not present in terminally differentiated leukocytes. The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
MDSLATSINQFALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRDQDVKSDP
ESEKKRKMEFNSSKSEEIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQS
VNFVEASDQIRKEINSWVESQTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRIN
KTTSKPVQMMSMKKKLQVFHIEKPQAIGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAD
MMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSKADFSGMSSERNLFLSNVFHKAFVEINEQGTE
AAAGTGSEISVRIKVPSIEFNADHPFLFFIRHNKTNSILFYGRFCSP
>gnl|CDD|381036 cd19570, serpinB11_epipin, serpin family B member 11, epipin. Epipin/SERPINB11 has no serine protease inhibitory activity, probably due to mutations in the scaffold, impairing conformational changes, and may have evolved a non-inhibitory function. The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
MDSLSTANVEFCLDVFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNHFSGSLKPE
LKDSSKCSQAGRIHSEFGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEH
STEETRKTINAWVESKTNGKVTNLFGKGTIDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSV
PVEMMYQSGTFKLASIKEPQMQVLELPYVNNKLSMIILLPVGTANLEQIEKQLNVKTFKEWTSSSNMVER
EVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAKADLSGMSPDKGLYLSKVIHKSYVDVNEEGTEAAAAT
GDSIAVKRLPVRAQFVANHPFLFFIRHISTNTILFAGKFASP
>gnl|CDD|381037 cd19571, serpinB12_yukopin, serpin family B member 12, yukopin. Yukopin, encoded by the SERPINB12 gene, is a member of the serpin superfamily of serine protease inhibitors. It inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator. An important paralog of this gene is SERPINB4. The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
MDSLVAANTKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNELSQNESKE
PDPCSKSKKQEVVAGSPFRQTGAPDLQAGSSKDESELLSCYFGKLLSKLDRIKADYTLSIANRLYGEQEF
PICPEYSDGVTQFYHTTIESVDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFK
AKWEKYFDHENTVDAPFCLNENEKKTVKMMNQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPSCSSD
NLKGLEELEKKITHEKILAWSSSENMSEETVAISFPQFTLEDSYDLNSILQDMGITDIFDETKADLTGIS
KSPNLYLSKIVHKTFVEVDEDGTQAAAASGAVGAESLRSPVTFNANHPFLFFIRHNKTQTILFYGRVCSP
>gnl|CDD|381038 cd19572, serpinB13_headpin, serpin family B member 13, headpin. Headpin (also known as hurpin or proteinase inhibitor 13/P113) maps to chromosome 18q21.3 and is expressed in normal squamous epithelium of the oral mucosa, skin, and cervix. Inhibitory serpins are known to play an important role in tumor invasion, metastasis, tumor suppression and apoptosis. Headpin belongs to the ovalbumin family of serpins (ov-serpins), a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
MDSLGAANTQFGFDLFKELKKTNDGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFYSEKDTESSRIKA
EEKEVIEKTEEIHHQFQKFLTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVNA
ADESRKKINSWVESQTNEKIKDLFPDGSLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKS
VLMMTQCHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIIDKISPEKLVEWTSPGHMEERN
VSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQADYSGMSARSGLHAQKFLHRSFVVVTEEGTEAAAATG
VGFTVSSAPGCENVHCNHPFLFFIRHNESDSVLFFGRFSSP
>gnl|CDD|381039 cd19573, serpinE2_GDN, serpin family E member 2, glia derived nexin (GDN). Serpin glia-derived nexin (GDN; also called peptidase inhibitor 7/PI-7 or protease nexin 1/PN-1) is a specific and extremely efficient inhibitor of thrombin. Unlike other thrombin inhibitors, it is not synthesized in the liver and does not circulate in the blood. It is instead expressed by multiple cell types and is located on the surface of these cells, bound to glycosaminoglycans. GDN plays a role in thrombosis and atherosclerosis and is a clade E serpin. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
QFNPLSLEELGSDLGIQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNGVGK
SLKKINKAIVSKKNKDIVTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQ
TRGMIDNLVSPDLIDGALTRLVLVNAVYFKGLWKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGS
TSTPNGLWYNVIELPYHGESISMLIALPTESSTPLSAIIPHISTKTIQSWMNTMVPKRVQLILPKFTAEA
ETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQKAKIEVNEDGTKASAATTAILIARSSPPWF
IVDRPFLFFIRHNPTGAILFMGQIN
>gnl|CDD|381040 cd19574, serpinE3, serpin family E member 3. The function of serpin E3 is not known. It is a member of clade E, which also includes nexin and plasminogen activator inhibitor type 1, of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
GNGSLQDSLKELHTEFAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYNVHDP
RVQDFLLKVYEDLTNSSQGTRLQLACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNHTASQINQW
VSRQTAGWILSQGSCEGEALWWAPLPQMALVSTMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQT
AEVNFGQFQTPSEQRYTVLELPYLGNSLSLFLVLPSDRKTPLSLIEPHLTARTLALWTTSLRRTKMDIFL
PRFKIQNKFNLKSVLPALGISDAFDPLKADFKGISGQDGLYVSEAIHKAKIEVTEDGTKAAAATAMVLLK
RSRAPVFKADRPFLFFLRQANTGSILFIGRVMNP
>gnl|CDD|381041 cd19575, serpinH2, serpin family H member 2. The function of Danio rerio serpin H2 is not known. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
SPPEISSLGHPSWSLGLRLYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISSNENV
VGETLTTALKSVHEANGTSFILHSSSALFSKQAPELEKSFLKKLQTRFRVQHVALGDADKQADMEKLHYW
AKSGMGGEETAALKTELEVKAGALILANALHFKGLWDRGFYHENQDVRSFLGTKYTKVPMMHRSGVYRHY
EDMENMVQVLELGLWEGKASIVLLLPFHVESLARLDKLLTLELLEKWLGKLNSTSMAISLPRTKLSSALS
LQKQLSALGLTDAWDETSADFSTLSSLGQGKLHLGAVLHWASLELAPESGSKDDVLEDEDIKKPKLFYAD
HSFIILVRDNTTGALLLMGALDHTDGPALHDE
>gnl|CDD|381042 cd19576, serpinI2_pancpin, serpin family I member 2, pancpin. Pancpin (also called proteinase inhibitor 14/PI14 or myoepithelium-derived serine protease inhibitor/MEPI) is an inhibitory member of the serpin superfamily. It is downregulated in pancreatic and breast cancer, and is associated with acinar cell apoptosis and pancreatic insufficiency when absent in mice. Pancpin was found to inhibit pancreatic chymotrypsin and elastase. It is thought that pancpin protects pancreatic cells from the consequences of premature activation of their respective zymogens. This subgroup belongs to clade I of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
GDKITEFAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQGTQAGEEFSVLKT
LSSVISESKKEFTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEAISTWVERQTDGK
IKNMFSSQDFNPLTRMVLVNAIYFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYFSASS
LSYQVLELPYKGDEFSLILILPAEGTDIEEVEKLVTAQLIKTWLSEMSEEDVEISLPRFKVEQKLDLKES
LYSLNITEIFSGGCDLSGITDSSELYISQVFQKVFIEINEEGSEAAASTGMQIPAIMSLPQHRFVANHPF
LFIIRHNLTGSILFMGRVMNP
>gnl|CDD|381043 cd19577, serpinJ_IRS-2-like, serpin family J, Ixodes ricinus serpin-2 (IRS-2). The serpin family J clade contains serpins from the Chelicerates. This model includes serpins from the Japanese horseshoe crab, mites, ticks, and spiders. The Limulus intracellular coagulation inhibitor, designated LICI, was isolated from hemocytes of the Japanese horseshoe crab. It blocks the amidolytic activities of Limulus lipopolysaccharide-sensitive serine protease, factor C and also inhibits human alpha-thrombin, rat salivary kallikrein, bovine plasmin, and trypsin but not Limulus clotting enzyme, Limulus factor B, bovine factor Xa, human factor XIa, human tissue plasminogen activator, human urokinase, chymotrypsin, elastase, and papain. Glycosaminoglycans such as heparin and heparan sulfate had no effect on the inhibitory activity. The castor bean tick, Ixodes ricinus serpin-2 (IRS-2) whose structure has been solved, unlike that of the LICI, is found in the saliva of the tick and primarily targets 2 proinflammatory serine proteases: cathepsin G and mast cell chymase, and in higher molar excess, thrombin. It also blocks cathepsin G- and thrombin-induced platelet aggregation. Thus it has a dual role and can interfere with both inflammation and wound healing during tick feeding. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
KLARANNQFGLNLLKELPSENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAGLTRDDVLSA
FRQLLNLLNSTSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFANDGEKVVDEINEWVKEK
THGKIPKLLEEPLDPSTVLVLLNAVYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDP
DLNVDALELPYKGDDISMVILLPRSRNGLPALEQSLTSDKLDDILSQLRERKVKVTLPKFKLEYSYDLKE
PLKALGLKSAFSESADLSGITGDRDLYVSDVVHKAVIEVNEEGTEAAAVTGVVIVVRSLAPPPEFTADHP
FLFFIRDKRTGLILFLGRVNEL
>gnl|CDD|381044 cd19578, serpinK_insect_SRPN2-like, serpin family K, insect Serpin-2 and similar proteins. Serpin-2 (SRPN2) is a negative regulator of the melanization response in the malaria vector Anopheles gambiae. SRPN2 irreversibly inhibits clip domain serine proteinase 9 (CLIPB9), which functions in a serine proteinase cascade ending in the activation of prophenoloxidase and melanization. Silencing of SRPN2 results in spontaneous melanization and decreased life span of the mosquito and is a promising target for vector control. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
DYVPPQGERFDEFDWKLLKEVAKEENGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGFPDKKDETRD
KYSKILDSLQKENPEYTLNIGTRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTAAAATINSWVSEI
TNGRIKDLVTEDDVEDSVMLLANAIYFKGLWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESP
ELDAKILRLPYKGNKFSMYIILPNAKNGLDQLLKRINPDLLHRALWLMEETEVDVTLPKFKFDFTTSLKE
VLQELGIRDIFSDTASLPGIARGKGLSGRLKVSNILQKAGIEVNEKGTTAYAATEIQLVNKFGGDVEEFN
ANHPFLFFIEDETTGTILFAGKVENP
>gnl|CDD|381045 cd19579, serpin1K-like, Manduca sexta Serpin 1K and similar proteins. Serpin 1K is a chymotrypsin inhibitor and is 1 of 12 serpins found in the hemolymph of the hornworm moth Manduca sexta. Serpins may be involved in the immune response in insect hemolymph. All of these serpins are encoded by the same gene, and the message for each is produced by alternative splicing of the final exon. This exon encodes the RCL and two strands of sheet B. Serpin 1K has a canonical structure at the reactive center, as is observed in a1-antitrypsin, whereas hinge residues (P17-P13) adopt the position and conformation observed in ovalbumin. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
KGLGNGNDKFTLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPNDDEIRSVFP
LLSSNLRSLKGVTLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFSKPQEAAKIINDWVEEQTNGR
IKNLVSPDMLSEDTRLVLVNAIYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELD
AKLLELPYKGDNASMVIVLPNEVDGLPALLEKLKDPKLLNSALDKLSPTEVEVYLPKFKIESEIDLKDIL
KKLGVTKIFDPDASGLSGILVKNESLYVSAAIQKAFIEVNEEGTEAAAANAFIVVLTSLPVPPIEFNADR
PFLYYILYKDNVLFCGVY
>gnl|CDD|381046 cd19580, serpin_silkworm16_18_22, silk gland serpins 16, 18, and 22 from Bombyx mori. Serpins 16, 18, and 22 of the silkworm Bombyx mori are found in the silk gland, a highly specialized organ that functions to synthesize and store silk proteins. These three serpins are mainly distributed in the middle silk gland and contain a signal peptide for secretion. They also share high sequence homology (~87%), implying that they might carry out a similar and specific function in the middle silk gland lumen. They have a canonical serpin fold, but contain a unique reactive center loop, which is shorter than that of typical serpins. It is thought that active proteases in silk glands are restricted by serpins until the wandering stage. Studies show that serpins 16 and 18 act as inhibitor of cysteine protease with serpin 18 acting specifically on fibroinase. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
TEAQLKYYDANTGLCGIGIDQWFQYEPERNQFSTAFPLLFMLSELSLNSKEDTTAELYKNLNLRSEDEVV
NVNQAVNTNLNTKNEVYQSTLILNAYTDIDSPFSETFIQNFAKVFNGTVKNIDYSNDAVATIRDSLQSDS
GNDIEIALKDGDINKDTGIILTAYTNIYFPWGQASDSYRPYKQIDISFTALDGTQSNKQAWYSEGAGKYA
EIENLGIKVFQFSLRPGLSVVLGTSLNDNEDLSGAFNKLRDPATLAYILTQTESKYLKLAVPIELTLRDS
RDYVPEVKRAGLLTELFEKNFDGFDTVYDNKSGYISYMLSHTRIDFEQPTEEQAASVVAEPDFIFDKPYF
FLILDQFNTPAFIGL
>gnl|CDD|381047 cd19581, serpinL_nematode, serpin family L, serpin family proteins from nematodes. The role of nematode serpins remains largely elusive. The only nematode serpin for which experimental evidence indicates an evasive function is Brugia malayi SPN-2 which specifically inhibits two human neutrophil-derived serine proteinases, cathepsin G and elastase. Less is known of Brugia malayi SPN-1, which is present at all stages of the parasite life cycle and could exist to inhibit a cognate proteinase endogenous to the parasite. Schistosoma serpins are hypothesized to play a role in both the physiological control of elastase within the schistosomes, and protection of the parasite from activated neutrophils during inflammation. Caenorhabditis elegans serpins are thought to regulate endogenous serine proteinases as well as inhibit proteinases produced by pathogenic microorganisms. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
SEADFGLNLLRQLPHTESLVFSPLSIALALALVHAGAKGETRTEIRNALLKGATDEQIINHFSNLSKELS
NATNGVEVNIANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNIIT
PESSKDAVALLINAIYFKADWQNKFSKESTSKREFFTSENEKREVDFMHETNADRAYAEDDDFQVLSLPY
KDSSFALYIFLPKERFGLAEALKKLNGSRIQNLLSNCKRTLVNVTIPKFKIETEFNLKEALQALGITEAF
SDSADLSGGIADGLKISEVIHKALIEVNEEGTTAAAATALRMVFKSVRTEEPRDFIADHPFLFALTKDNH
PLFIGVF
>gnl|CDD|381048 cd19582, serpinM_ShSPI, serpin family M, Schistosoma haematobium serpin. ShSPI is a serpin from the trematode Schistosoma haematobium. The protein is exposed on the surface of invading cercaria as well as of adult worms, suggesting its involvement in the parasite-host interaction. It has several distinctive features, mostly concerning the helical subdomain of the protein. It is proposed that these peculiarities are related to the unique biological properties of a small serpin subfamily which is conserved among pathogenic schistosomes. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
ISHNDFTRGFLKASLADGNTGNYVASPIGVLFLLSALLGSGGPQGNTAKEIAQALVLKSDKETCNLDEAQ
KEAKSLYRELRTSLTNEKTEINRSGKKVISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSEA
FEDINEWVNSKTNGLIPQFFKSKDELPPDTLLVLLNVFYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPM
MHIEEQLVYGKFPLDGFEMVSKPFKNTRFSFVIVLPTEKFNLNGIENVLEGNDFLWHYVQKLESTQVSLK
LPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITSHPNLYVNEFKQTNVLKVDEAGVEAAAVTSIIIL
PMSLPPPSVPFHVDHPFICFIYDSQLKMPLFAARIINP
>gnl|CDD|381049 cd19583, serpinN_SPI-1_SPI-2, serpin family N, viral serpin-1 and serpin-2. This group of viral serpins are from the Orthopoxvirus branch (cowpox, ectromelia, vaccinia, variola, and rabbitpox) and corresponding to clade N which contains viral serpin-1 (SPI-1-like) and viral serpin-2 (SPI-2-like) serpins. The other is clade O which contains the viral serpin-3 (SPI-3-like) serpins. SPI-2, also called cytokine response modifier A (crmA), acts to inhibit inflammation and apoptosis. SPI-1, a serpin that is approximately 45% identical to SPI-2, has also been implicated in the inhibition of apoptosis, since certain cells infected with RPV SPI-1 mutants undergo apoptotic cell death. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
RYCLSYAMDIFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQLSKYIIPEDNKDDNNDMDVTFA
TANKIYGRDSIEFKDSFLQKIKDDFQTVDFNNANQTKDLINEWVKTMTNGKINPLLTSPLSINTRMIVIS
AVYFKAMWLYPFSKHLTYTDKFYISKTIVVSVDMMVGTENDFQYVHINELFGGFSIIDIPYEGNTSMVVI
LPDDIDGLYNIEKNLTDENFKKWCNMLSTKSIDLYMPKFKVETESYNLVPILEKLGLTDIFGYYADFSNM
CNETITVEKFLHKTYIDVNEEYTEAAAATGVLMTDCMVYRTKVYINHPFIYMIKDNTGKILFIGRYC
>gnl|CDD|381050 cd19584, serpinO_SPI-3_virus, serpin family O, viral serpin-3. This group of viral serpins are from the Orthopoxvirus branch (cowpox, ectromelia, vaccinia, variola, and rabbitpox) and corresponding to clade O which contains the viral serpin-3 (SPI-3-like) serpins. The other is clade N which contains viral serpin-1 (SPI-1-like) and viral serpin-2 (SPI-2-like) serpins. SPI-3 is an N-glycosylated bifunctional protein that acts as both a proteinase inhibitor and a suppressor of infected cell-cell fusion. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
GFTNAGILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRDLGPAFTELISGL
AKLKTSKYTYTDLTYQSFVDNTVCIKPSYYQQYHRFGLYRLNFRRDAVNKINSIVERRSGMSNVVDSTML
DNNTLWAIINTIYFKGTWQYPFDITKTRNASFTNKYGTKTVPMMNVVTKLQGNTITIDDEEYDMVRLPYK
DANISMYLAIGDNMTHFTDSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNA
SFKHMTRDPLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGK
>gnl|CDD|381051 cd19585, serpin_poxvirus, serpin-like proteins found in poxviruses. These are viral serpins from poxviridae that are not in the Orthopoxvirus branch (cowpox, ectromelia, vaccinia, variola, and rabbitpox) that contains clade N serpins (viral serpin-1/SPI-1-like and viral serpin-2/SPI-2-like) and clade O serpins (viral serpin-3/SPI-3-like). The members here include fowlpox virus, canarypox virus, deerpox virus, tanapox virus, an cotia virus and belong to other poxviridae branches including Leporipoxvirus, Yatapoxvirus, and Avipoxvirus. These viruses have a variety of hosts including humans, birds, and mice. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
NNKIAFILKKFYYSIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPDNHNIDKILLEID
SRTEFNEIFVIRNNKRINKSFKNYFNKTNKTVTFNNIINDYVYDKTNGLNFDVIDIDSIRRDTKMLLLNA
IYFNGLWKHPFPPEDTDDHIFYVDKYTTKTVPMMATKGMFGTFYCPEINKSSVIEIPYKDNTISMLLVFP
DDYKNFIYLESHTPLILTLSKFWKKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFCAS
PDKVSYVSKAVQSQIIFIDERGTTADQKTWILLIPRSYYLNRPFMFLIEYKPTGTILFSGKIKDP
>gnl|CDD|381052 cd19586, serpin_mimivirus, serpin-like proteins found in mimiviruses. These viral serpins are from Mimiviridae (Tupanvirus, Powai, Bandra, Moumouvirus, and Megavirus) and may represent a new clade of viral serpins. Mimiviridae are thought to have a common evolutionary origin with Poxviridae whose viral serpins are classified into clades N and O. N is composed of viral serpin-1 (SPI-1-like) and viral serpin-2 (SPI-2-like) serpins and clade O is made up of viral serpin-3 (SPI-3-like) serpins. Mimiviruses have the only known viral serpins outside of the poxvirus family. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
DDKISQANNTFTIKLFNNFDSASNVFSPLSINYALSLLHLGALGNTNKQLTNLLGYKYTVDDLKVIFKIF
NNDVIKMTNLLIVNKKQKVNKEYLNMVNNLAIVQNDFSNPDLIVQKVNHYIENNTNGLIKDVISPSDINN
DTIMILVNTIYFKAKWKKPFKVNKTKKEKFGSEKKIVDMMNQTNYFNYYENKSLQIIEIPYKNEDFVMGI
ILPKIVPINDTNNVPIFSPQEINELINNLSLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLD
IISKNPYVSNIIHEAVVIVDESGTEAAATTVATGRAMAVMPKKENPKVFRADHPFVYYIRHIPTNTFLFF
GDFQG
>gnl|CDD|381053 cd19587, serpinA16_HongrES1-like, serpin family A member 16, HongrES1 and similar proteins. HongrES1 is an epididymis-specific secretory protein and is encoded by the SERPINA16 gene. It is one of several potential decapacitation factors of rodents, including a 40-kDa glycoprotein, phosphatidylethanolamine-binding protein 1 (PEBP1), a cysteine-rich secretory protein 1, an acrosome-stabilizing factor, SVA, SVS2, and SPINKL. In humans, some potential decapacitation factors that have been reported are glycodelin-S, semenogelin I, a 130-kDa glycoprotein, and some mannosyl glycopeptides. Decapitation factors are removed from the sperm head surface during the capacitation process and are able to reverse sperm capacitation. The clade A of the serpin superfamily includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
STSSPFLNNSHFAFSLYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTLTGVPEDR
AHEHYSQLLSALLPPPGACGTDTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKNYGTARKQMDLAI
RKKTHGKIEKLLQILKPHTVLILANYIFFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQY
FSHLHSYVLQLPFTCNITAVFILPDDGKLKEVEEALMKESFETWTQPFPSSRRRLYFPKFSLPVNLQLDQ
LVPVNSILDIFSYHMDLSGISLQTAPMRVSKAVHRVELTVDEDGEEKEDITDFRFLPKHLIPALHFNRPF
LLLIFEEGSHNLLFMGKVVNPNA
>gnl|CDD|381054 cd19588, serpin_miropin-like, serpin miropin and similar proteins. Miropin, the serpin from Tannerella forsythia, is thought to contribute to the virulence of periodontal pathogens by inhibiting neutrophil serine proteases. Miropin broadly inhibits serine endopeptidases (SEPs) including trypsin, neutrophil elastase, pancreatic elastase, subtilisin, and cathepsin G and cysteine endopeptidases (CEPs) including papain, calpain-like peptidase Tpr, and gingipain K through various reactive-site bonds. This is achieved by offering several target bonds of the RCL for cleavage within a bait region, instead of a single RSB as found in canonical serpins. In addition, promiscuous inhibition is facilitated by the capacity to insert strands deviating from the canonical length into the central sheet A, while keeping the prey peptidase bound and inactivated. The structural adaptation of miropin to provide a relaxed inhibitory specificity, which allows for formation of inhibitory complexes using different sites, is unique among serpins. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
EKELVEANNRFGFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEGLSLEEINE
AYKSLLELLPSLDPKVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFSDPAAVDTINNWVSEKT
NGKIPKILDEIIPDTVMYLINAIYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFPYLENEDF
QAVRLPYGNGRFSMTVFLPKEGKSLDDLLEQLDAENWNEWLESFEEQEVTLKLPRFKLEYETELNDALKA
LGMGIAFDPGAADFSIISDGPLYISEVKHKTFIEVNEEGTEAAAVTSVGMGTTSAPPEPFEFIVDRPFFF
AIRENSTGTILFMGK
>gnl|CDD|381055 cd19589, serpin_tengpin-like, serpin tengpin and similar proteins. Tengpin is an unusual prokaryotic serpin from the extremophile Thermoanaerobacter tengcongensis. In addition to the serpin domain, tengpin contains an N-terminal region that functions to trap the serpin domain in the native metastable state and prevent the spontaneous transition to the latent conformation. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
EFIKALNDFSFKLFKELLDEGENVLISPLSVYLALAMTANGAKGETKAELEKVLGGSDLEELNAYLYAYL
NSLNNSEDTKLKIANSIWLNEDGSLTVKKDFLQTNADYYDAEVYSADFDDDSTVKDINKWVSEKTNGMIP
KILDEIDPDTVMYLINALYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMMNSTESFSYLEDDGATGFIL
PYKGGRYSFVALLPDEGVSVSDYLASLTGEKLLKLLDSAESTKVNLSLPKFKYEYSLELNDALKAMGMED
AFDPGKADFSGMGDSPDGNLYISDVLHKTFIEVDEKGTEAAAVTAVEMKATSAPEPEEPKEVILDRPFVY
AIVDNETGLPLFMGTVN
>gnl|CDD|381056 cd19590, serpin_thermopin-like, serpin thermopin and similar proteins. Thermopin, the serpin from Thermobifida fusca, functions as an irreversible proteinase inhibitor with resistance to polymerization at high temperatures. The crystal structure of the cleaved thermopin was found to adopt the canonical serpin fold, supporting its inclusion as a classical inhibitory member of the serpin superfamily. A detailed structural comparison revealed unique features, including charge-stabilizing interactions, a deleted element of secondary structure (the G helix), and a C-terminal "tail" that interacts with the top of the A beta sheet and plays an important role in the folding/unfolding of the molecule. These unique features provide structural and biophysical evidence as to how this unusual serpin member has adapted to remain functional in an extreme environment. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
RANNAFALDLYRALASPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPLPQDDLHAAFNALDLA
LNSRDGPDPPELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAGDPEGARKTINAWVAEQTNGKI
KDLLPPGSIDPDTRLVLTNAIYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFRYAEGDGWQA
VELPYAGGELSMLVLLPDEGDGLALEASLDAEKLAEWLAALREREVDLSLPKFKFESSFDLKETLKALGM
PDAFTPAADFSGGTGSKDLFISDVVHKAFIEVDEEGTEAAAATAVVMGLTSAPPPPPVEFRADRPFLFLI
RDRETGAILFLGRVVD
>gnl|CDD|381057 cd19591, serpin_like, serpin family proteins. This group includes a variety of serpins in three domains of life eukaryotes, bacteria, and archaea. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
IAAANNAFAFDMYSELKDEDENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFPLNKTVLRKRSKDII
DTINSESDDYELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPEESRDTINEWVEEKTNDKI
KDLIPKGSIDPSTRLVITNAIYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKNFFNYGEDSKAKI
IELPYKGNDLSMYIVLPKENNIEEFENNFTLNYYTELKNNMSSEKEVRIWLPKFKFETKTELSESLIEMG
MTDAFDQAAASFSGISESDLKISEVIHQAFIDVQEKGTEAAAATGVVIEQSESAPPPREFKADHPFMFFI
EDKRTGCILFMGKV
>gnl|CDD|381058 cd19593, serpin_bacteria_crustaceans, serpin family proteins from bacteria and crustaceans. This group includes a variety of serpin family proteins from various bacteria and crustaceans including sea louse and salmon louse. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
VSALAKGNTKFGVDLYRELAKPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPLDVEDLKSAYS
SFTALNKSDENITLETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFTEAALETINQWVRKKTEGK
IEFILESLDPDTVAVLLNAIYFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFAPIEFASLEDLKFTIV
ALPYKGERLSMYILLPDERFGLPELEAKLTSDTLDPLLLELDAAQSQKVELYLPKFKLETGHDLKEPFQS
LGIKDAFDPGSDDSGGGGGPKGELYVSQIVHKAVIEVNEEGTEAAAATAVEMTLRSARMPPPFVVDHPFL
FMIRDNATGLILFMGRVVDP
>gnl|CDD|381059 cd19594, serpin_crustaceans_chelicerates_insects, serpin family proteins from crustaceans, chelicerates, and insects. This group includes a variety of serpins from crustaceans (sea louse, Chinese mitten crab, signal crayfish, red king crab, Asian tiger shrimp), chelicerates (Atlantic horseshoe crab, common house spider), and insects (Asian tiger mosquito, caddisfly, pea aphid, bed bug, fruit fly, Australian sheep blowfly, tobacco hornworm, alfalfa leafcutting bee). SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
LYSGEQDFSLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWALSKADVLRAY
RLEKFLRKTRQNNSSSYEFSSANRLYFSKTLKLRECMLDLFKDELEKVDFRSDPEEARKEINDWVSNQTK
GHIKDLLPPGSITEDTKLVLANAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEE
LGAHVLELPYKGDDISMFILLPPFSGNGLDNLLSRLNPNTLQNALEEMYPREVEVSLPKFKLEQELELVP
ALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHKAKIEVDEEGTEAAAATALFSFRSSRPLEPTKFICN
HPFVFLIYDKKTNTILFMGVYRDP
>gnl|CDD|381060 cd19596, serpin_fungal, cellulosomal serpin precursor. A single fungal serpin has been characterized to date: celpin from Piromyces spp. strain E2. Piromyces is a genus of anaerobic fungi found in the gut of ruminants and is important for digesting plant material. Celpin is predicted to be inhibitory and contains two N-terminal dockerin domains in addition to its serpin domain. Dockerins are commonly found in proteins that localise to the fungal cellulosome, a large extracellular multiprotein complex that breaks down cellulose.[21] It is therefore suggested that celpin may protect the cellulosome against plant proteases. Certain bacterial serpins similarly localize to the cellulosome.[186] SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
SNSDFDFSFLKLENNKENMLYSPLSIKYALNMLKEGADGNTYTEINKVIGNAELTKYTNIDKVLSLANGL
FIRDKFYEYVKTEYIKTLKEKYNAEVIQDEFKSAKNANQWIEDKTLGIIKNMLNDKIVQDPETAMLLINA
LAIDMEWKSQFDSYNTYGEVFYLDDGQRMIATMMNKKEIKSDDLSYYMDDDITAVTMDLEEYNGTQFEFM
AIMPNENLSSFVENITKEQINKIDKKLILSSEEPYGVNIKIPKFKFSYDLNLKKDLMDLGIKDAFNENKA
NFSKISDPYSSEQKLFVSDALHKADIEFTEKGVKAAAVTVFLMYATSARPKPGYPVEVVIDKPFMFIIRD
KNTKDIWFTGT
>gnl|CDD|381061 cd19597, serpin28D-like_insects, insect serpins similar to Drosophila melanogaster Serpin-28D. Serpins in insects function within development, wound healing and immunity. Drosophila melanogaster Serpin-28D is required for pupal viability and plays an essential role in regulating melanization. Insect serpins from mosquitoes, Mediterranean fruit fly, fruit fly, and blowfly are included in this subfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
TDLARKIGLALALQKSKTEIFSPVSIAGALSLLLLGAGGRTREELLQVLGLNTKRLSFEDIHRSFGRLLQ
DLVSNDPSLGPLVQWLNDKCDEYDDEEDDEPRPQPPEQRIVISLANGIFVQRGLPLNPRYRRVARELYGS
EIQRLDFEGNPAAARALINRWVNKSTNGKIREIVSGDIPPETRMILASALYFKAFWETMFIEQATRPRPF
YPDGEGEPSVKVQMMATGGCFPYYESPELDARIIGLPYRGNTSTMYIILPNNSSRQKLRQLQARLTAEKL
EDMISQMKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSIFNPSRSNLSPKLFVSEIVHKVDLDVNEQGTE
GGAVTATLLDRSGPSVNFRVDTPFLILIRHDPTKLPLFYGAVYDP
>gnl|CDD|381062 cd19598, serpin77Ba-like_insects, insect serpins similar to Drosophila melanogaster Serpin 77Ba. Serpins in insects function within development, wound healing and immunity. Drosophila melanogaster Serpin 77Ba plays an essential role in regulating the tracheal melanization immune response to bacterial and fungal infection. Insect serpins from pine beetle, diamondback moth, red flour beetle, mosquito, silkworm, and fruit fly are included in this subfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
LSRGVNNFSLELLQRTSVETESFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPVDNKCLRNFYR
ALSNLLNVKTSGVELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDFSNSTKTANIINEYISNATHG
RIKNAVKPDDLENARMLLLSALYFKGKWKFPFNKSDTKVEPFYDENGNVIGEVNMMYQKGPFPYSNIKEL
KAHVLELPYGKDNRLSMLVILPYKGVKLNTVLNNLKTIGLRSIFDELERSKEEFSDDEVEVYLPRFKISS
DLNLNEPLIDMGIRDIFDPSKANLPGISDYPLYVSSVIQKAEIEVTEEGTVAAAVTGAEFANKILPPRFE
ANRPFAYLIVEKSTNLILFAGVYSNP
>gnl|CDD|381063 cd19599, serpin18-like_insects, insect serpins similar to Anopheles gambiae Serpin 18. Serpins in insects function within development, wound healing and immunity. A. gambiae serpin 18 is categorized as non-inhibitory based on the sequence of its reactive-center loop. It is expressed throughout all life stages in multiple tissues and the hemolymph, and is predicted to be secreted based on the presence of a signal peptide. Insect serpins from mosquitoes are included in this subfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
SSTKFTLDFFRKSYNPSENAIVSPISVQLALSMFYPLAGPAVAPDMQRALGLPADKKKAIDDLRRFLQST
NKQSHLKMLSKVYHSDEELNPEFLPLFQDTFGTEVETADFTDKQKVADSVNSWVDRATNGLIPDFIEASS
LRPDTDLMLLNAVALNARWEIPFNPEETESELFTFHNVNGDVEVMHMTEFVRVSYHNEHDCKAVELPYEE
ATDLSMVVILPKKKGSLQDLVNSLTPALYAKINERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVFE
NDDLDVFARSKSRLSEIRQTAVIKVDEKGTEAAAVTETQAVFRSGPPPFIANRPFIYLIRRRSTKEILFI
GHYS
>gnl|CDD|381064 cd19600, serpin11-like_insects, insect serpins similar to Bombyx mori Serpin-11. Serpins in insects function within development, wound healing and immunity. The specific function of Bombyx mori serpin-11 (SPN19) is unknown. Insect serpins from sawfly, mealworm, riceborer, moth, silkworm, bollworm are included in this subfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
ESRLNFFDIDLLQYVAEEKEGNVMVSPASIKSALAMLLEGARGRTAEEIRSALRLPPDKSDIREQLSRYL
ASLKVNTSGTELENANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGNPVNAANTINDWVRQATHGLIP
SIVEPGSISPDTQLLLTNALYFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAH
AVELPYSDGRYSMLILLPNDREGLQTLSRDLPYVSLSQILDLLEETEVLLSIPKFSIEYKLDLVPALKSL
GIQDLFSSNANLTGIFSGESARVNSILHKVKIEVDEEGTVAAAVTEAMVVPLIGSSVQLRVDRPFVFFIR
DNETGSVLFEGRIEEP
>gnl|CDD|381065 cd19601, serpin42Da-like, serpins similar to Drosophila melanogaster Serpin 42Da. This subfamily is composed mainly of insect serpins, including Drosophila melanogaster serpin 42Da. Serpins in insects function within development, wound healing and immunity. Serpin 42Da, previously serpin 4, is a serine protease inhibitor that is capable of remarkable functional diversity through the alternative splicing of four different reactive center loop exons. Insect serpins from stink bug, alfalfa leafcutting bee, red flour beetle, house fly, and brown planthopper are also included in this subfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
SLNKFSSNLYKALAKSESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLPSDDESIAEGYKSLIDS
LNNVKSVTLKLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLI
SPDDLDEDTRLVLVNAIYFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIE
LPYKNSDLSMVIILPNEIDGLKDLEENLKKLNLSDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMK
DMFSDGANFFSGISDEPLKVSKVIQKAFIEVNEEGTEAAAATGVVVVLRSMPPPPIEFRVDRPFLFAIVD
KDTKTPLFVGR
>gnl|CDD|381066 cd19602, serpin_mollusks, serpin family proteins from mollusks. This group includes a variety of serpins from mollusks (freshwater snail, sea slug, and disk abalone). SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
NEQLALSSASSTFSQNLYQKLSQSESNIVYSPFSIHSALTMTSLGARGDTAREMKRTLGLSSLGDSVHRA
YKELIQSLTYVGDVQLSVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLSAPGGPETPINDWVANETR
NKIQDLLAPGTINDSTALILVNAIYFNGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRYKRDPA
LGADVVELPFKGDRFSMYIALPHAVSSLADLENLLASPDKAETLLTGLETRRVKLKLPKFKIETSLSLKK
ALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKAVIEVNETGTTAAAATAVIISGKSSFLPPPVEFIV
DRPFLFFLRDKVTGAILFQGKFSG
>gnl|CDD|381067 cd19603, serpin_platyhelminthes, serpin family proteins from platyhelminthes. This group includes a variety of serpins from platyhelminthes (lung fluke, tapeworm, flatworm). SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
MEVKQSLINFSSDLYEQIVKKQGGSLENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLPDCLEADEV
HSSIGSLLQEFFKSSEGVELSLANRLFILQPITIKEEYKQILKKYYKADTESVTFMPDNEAKRRHINQWV
SENTKGKIQELLPPGSLTADTVLVLINALYFKGLWKLPFDKEKTKESEFHCLDGSTMKVKMMYVKASFPY
VSLPDLDARAIKLPFKDSKWEMLIVLPNANDGLPKLLKHLKKPGGLESILSSPFFDTELHLYLPKFKLKE
GNPLDLKELLQKCGLKDLFDAGSADLSKISSSSNLCISDVLHKAVLEVDEEGATAAAATGMVMYRRSAPP
PPEFRVDHPFFFAIIWKSTVPVFLGHVVNP
>gnl|CDD|381068 cd19604, serpin_protozoa, serpin family proteins from protozoa. This group includes a variety of serpin clades from various protozoa including Neospora caninum that causes neosporosis, Toxoplasma gondii that causes toxoplasmosis, and Hammondia hammondi. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
MTATPAGTLVRLYSSLVSGQHKSADGDCNFAFSPYAVSAVLAGLYFGARGTSREQLENHYFEGRSAADAA
ACLNEAIPAVSQKEEGVDPDSQSSVVLQAANRLYASKELMEAFLPQFREFRETLEKALHTEALLANFKTN
SNGEREKINEWVCSVTKRKIVDLLPPAAVTPETTLLLVGTLYFKGPWLKPFVPCECSSLSKFYRQGPSGA
TISQEGIRFMESTQVCSGALRYGFKHTDRPGFGLTLLEVPYIDIQSSMVFFMPDKPTDLAELEMMWREQP
DLLNDLVQGMADSSGTELQDVELTIRLPYLKVSGDTISLTSALESLGVTDVFGSSADLSGINGGRNLFVS
DVFHRCLVEIDEEGTDAAAGAAAGVACVSLPFVREHKVINIDRSFLFQTRKLKRVQGLRAGNSPAMRKDD
DILFVGRVVDVGVLQSGGE
>gnl|CDD|381069 cd19605, serpin_protozoa, viral serpin. CrmA is a viral serpin that inhibits both cysteine and serine proteinases involved in the regulation of host inflammatory and apoptosis processes. It differs from other members of the serpin superfamily by having a shorter reactive center loop as well as possessing an additional highly charged antiparallel beta-strand of beta-sheet A, whose sequence and length are unique. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
SDEMASMSTPAAELQRAMAARKRAQGRDGNFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSSLPAIP
KLDQEGFSPEAAPQLAVGSRVYVHQDFEGNPQFRKYASVLKTESAGETEAKTIDFADTAAAVEEINGFVA
DQTHEHIKQLVTAQDVNPNTRLVLVSAMYFKCPWATQFPKHRTDTGTFHALVNGKHVEQQVSMMHTTLKD
SPLAVKVDENVVAIALPYSDPNTAMYIIQPRDSHHLATLFDKKKSAELGVAYIESLIREMRSEATAEAMW
GKQVRLTMPKFKLSAAANREDLIPEFSEVLGIKSMFDVDKADFSKITGNRDLVVSSFVHAADIDVDENGT
VATAATAMGMMLRMAMAPPKIVNVTIDRPFAFQIRYTPPSGKQDGSDDYVLFSGQITDVAAAQ
>gnl|CDD|381624 cd19606, GH113-like, Glycoside hydrolase family 113 beta-mannosidase and similar proteins. Family 113 glycoside hydrolases cleave (1-_4)-beta-glycosidic linkages, such as endo-1,4-beta-mannanase. This family also includes TIM-barrel domains found in gene transfer agent proteins
FIRGVTFGVSWQGGDLITPKAEGSLRAATEAWRNSVGIARAQLERVPARIDDRPVYGGTVADDEVVEAIH
AAKALGLKVLLKPTVNCRQGTWRGRITFSTAPGPRVLYWGAWFWSYRRFILHYAWLARLTGCEMFCVGCE
MRGAEPAEAEWRELIADVRGIYGGLVTYNADWSLEADVNFWDALDPISSSNYYPIDRWPITDADFGEVWV
HRPKPIFFTEYGCPSRSGSSNQPNLFGSSGARDLGEQANYYRAMFEYWQDEAWMDGAHLWAWDARLYPAF
PANYARGYWLNGKPAEQVLSAVV
>gnl|CDD|381625 cd19607, GTA_TIM-barrel-like, Putative glycoside hydrolase TIM-barrel domain in gene transfer agent and similar proteins. This domain is found in the gene transfer agent protein, such as the Rhodobacter capsulatus putative gene transfer agent protein encoded by orfg15. In the purple nonsulfur bacterium Rhodobacter capsulatus, DNA transmission is mediated via an unusual system, a small bacteriophage-like particle called the gene transfer agent (GTA) that transfers random 4.5-kb segments of the producing cell's genome to recipient cells, where allelic replacement occurs
LEDDLPNVEWVSLVVAWFGDDLDAGTCIIGPGVEQDAKDTAPADWQVGGYTRASAGLVSTDVNGRPVYGG
TPSDASVVRAIRELKARGYRVMFYPFLLMDQPAPGKPWRGRITLSAAAGRAGSPDDFADGGTVVSYGGGF
DWGYRRFILHYAHLCAGAGGVDAFLIGSELRGLTSIRDPDGNFPAVTGLRRLAADVRAILGPDVKISYAA
DWSEYEYHGSGGGFFHLDPLWADPNIDFVGIDNYFPLTDWREADRDLQIRSPITDGGEGEGWVYPEKDDR
AWWRPPHWDRPGGVPDGGPTAWVPQSKPIWFTEYGCPAVDKGTNQPNVFLDPKSSESALPYFSNGKRDDA
IQRAAIEATLDYWGDPENNPVSGYGGPMVDVGRCFAWAWDARPYPFFPALTDVWSDGDNWALGHWLTGRI
GAVSLAAVVAEICLRAGL
>gnl|CDD|381626 cd19608, GH113_mannanase-like, Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins. Mannan endo-1,4-beta mannosidase (E.C 3.2.1.78) randomly cleaves (1-_4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans and is also called beta-1,4-mannanase, endo-1,4-beta-mannanase, endo-beta-1,4-mannase, beta-mannanase B, beta-1, 4-mannan 4-mannanohydrolase, endo-beta-mannanase, beta-D-mannanase, 1,4-beta-D-mannan mannanohydrolase, and 4-beta-D-mannan mannanohydrolase. (1-_4)-beta-linked mannans are polysaccharides with a linear polymer backbone of (1-_4)-beta-linked mannose units (in plants and fungi) or alternating mannose and glucose/galactose units (glucomannan in plants and fungi, and galactomannan and galactoglucomannan in plants), such as in the hemicellulose fraction of hard- and softwoods. Complete degradation of mannan requires a series of enzymes, including beta-1,4-mannanase. According to the CAZy database beta-1,4-mannanases are grouped into various glycoside hydrolase (GH) families; GH family 113 beta-1,4-mannanases include mostly bacterial and archaeal sequences
GFQKGVSLTSWGNPGYGSPEAARSLDRLKALGANWVSLVPTWYQDTATSSTISPDPGSTPSDEDLIAAIR
AAHARGLKVMLKPHLDVQDPGSWRGDINPPDDWDAWFASYRRFILHYADLAEENGVELFCIGTELVSLTE
DYEDRWRALIAEVRSVYSGKLTYAANWDSEYESVPFWDALDYIGVDAYFPLTDKPTPSVEELAAGWQPIL
DQLEALADKYGKPVLFTEIGYPSVDGAAAEPWDWPGASGPVDLQEQANAYEAFFRAFWDRPWFAGVFWWG
WDPDPDPGGPGDTGYSPQGKPAEDVIRRWF
>gnl|CDD|410991 cd19609, NTD_TDP-43, N-terminal domain of transactive response DNA-binding protein 43. Transactive response DNA-binding protein of 43 kDa (TDP-43) is a nuclear DNA/RNA-binding protein involved in gene transcription and mRNA processing, transport, and translational regulation. It is vital to pre-mRNA and microRNA processing and regulates stress granule activity through the differential regulation of G3BP and TIA-1. It also forms aggregates implicated in amyotrophic lateral sclerosis. The N-terminal domain of TDP-43 is required for its physiological functions and pathological aggregation
YVRVAEDEGDEPIEVPLEEDGTLLLSTLQAQFPGATGLKYRNPETGRARGVRLVDGKLYPPEGGWGDRVY
YVVF
>gnl|CDD|381622 cd19610, mannanase_GH134, glycosyl hydrolase family 134 inverting endo-beta-1,4-mannanase. glycosyl hydrolase family 134 beta-mannanase (E.C. 3.2.1.78) differs from other mannanases in as it has a hen egg white lysozyme fold and cleaves beta-1,4-mannans with inversion of sterochemistry. Beta-mannosidases are enzymes involved in seed germination and the degradation of the hemicellulose fraction of soft- and hardwoods
ASCGSYTVPGLGARKQQVLNAGGDTLDLAIAMLETEDMDTDYPYGDGKSGDAANFGIFKQNWGMLRTCCS
QFKGQTAGDYNNGAVLNSNLAQDIKCLHESQSYYGGDKWFAGHRNGETGLSNPNTQDIQNYKAGVAWIKD
QLESDPKYLTDDTRFWVEVPAI
>gnl|CDD|381623 cd19611, Ctf13_LRR_LRR-insertion, leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein complex CBF3 subunit C (Ctf13). Ctf13, is an F-box protein of the leucine-rich-repeat superfamily; it is a component of CEN binding factor 3 (CBF3), a complex that recognizes point centromeres found in budding yeast, associating specifically with the third centromere DNA element (CDEIII) DNA. CBF3 is comprised of two homodimers of Cep3 and Ndc10, and a Ctf13-Skp1 heterodimer. The Skp1-Ctf13 heterodimer interacts with Cep3, Ndc10 and CDEIII at a completely conserved G, centrally positioned between the TGC/CCG sites. The eight leucine-rich repeat (LRR) motifs of Ctf13 (LRR 1-8) form a solenoid structure. At the N-terminus of the Ctf13 LRR is an expanded F-box, and at the C-terminal end, an alpha-beta domain formed by insertions within the latter LRRs of Ctf13 (LRR insertion domain). This domain model includes the LLR domain and the LRR insertion domain
TEIEYLRLNLEYLNPNMVKKILKVLEKKELLDLVSEVFFGQDEEESDEEDEDDSSKNDRKKLTDDDVKEK
SYKLNDPSIIRIISSLESMKNLRKLSVRGDNLYERLINFHGVRDNPGKTINYIVKRRIRELELLQISDLT
KTGVADFTRWENLRKLTLSNIGYIDLNKIVLPPNCKSLTLKNIRKLKWWDIEEKIEILLKPLHRKEDDDS
CTSLENLKHVKIKTLDKSSIDQDELFKCKAIVWKSFQPLNYIQLQNVSEIEGDTIVVPRTLYNNKRIQIF
GCTKIEEIIV
>gnl|CDD|381247 cd19614, FABP_Der_p_13-like, mite group 13 allergens similar to Dermatophagoides farinae Der p 13, and related proteins. The minor house dust mite allergen Der p 13 is a fatty acid-binding protein and an activator of a TLR2-mediated innate immune response. This group also contains other mite group 13 allergens, including Tyrophagus putrescentiae Tyr p 13 and Blomia tropicalis mite blo t 13. blo t 13 binds the natural fluorescent fatty acid cis-parinaric acid and oleic acid by competition, but not retinol, retinoic acid, cholesterol, or dansylated or anthroxylated fatty acids. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
QIEGKYKLEKSDNFDAFLDELGVGFMVKTAAKTLKPTVEVIVDGDSYTFRSLSTFKNTEIKFKLGEEFEE
DRADGKKVKTVVTKEGDNKLVQTQFGDKEVKIVREFNGDGVVVTASVDGVTSVRTYKR
>gnl|CDD|381248 cd19615, lipocalin_NP7, nitrophorin 7. Nitrophorins (NPs) represent a group of nitric oxide (NO)-carrying heme proteins found in the saliva of Rhodnius prolixus. In its adult phase R. prolixus expresses at least 4 nitrophorins (designated NP1-4 in order of their increasing abundance in the saliva of adult insects). Two additional nitrophorins, NP5 and NP6, have been detected mainly in the five instar nymphal stages of insect development. NP7 has not been isolated from the insects but was instead recognized in a cDNA library. NP7 displays peculiar properties, such as an abnormally high isoelectric point, the ability to bind negatively charged membranes, and a strong pH sensitivity of NO affinity. In contrast to NP1-4, which show high affinities for histamine (Hm), Np7 does not appear to sequester Hm. NPs belong to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
ECSVNVIPKKNLDKAKFFSGTWYETHYLDMDPQATEKFCFSFAPRESGGTVKEALYHFNVDSKVSFYNTG
TGPLESNGAKYTAKFNTVDKKGKEIKPADEKYSYTVTVIEAAKQSALIHICLQEDGKDIGDLYSVLNRNK
NALPNKKIKKALNKVSLVLTKFVVTKDLDCKYDD
>gnl|CDD|381249 cd19616, FABP11, fatty acid binding protein 11 similar to zebrafish FABP11. This group includes zebrafish FABP11a and FABP11b, Senegalese sole FABP11, and similar proteins. The two copies of the fabp11 gene in the zebrafish genome may have resulted from a fish-specific whole genome duplication event. Fabp11a transcripts have been detected in the liver, brain, heart, testis, muscle, ovary and skin of adult zebrafish while fabp11b transcripts have been found in the brain, heart, ovary and eye in adult tissues. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
QFVGTWKMTTSDNFDEYMKAIGVSFATRQMGNRAKPNLVICVDEQGVICMKSQSTFKTTEIKFKLNEEFD
ETTADDRKTKTTMTLENGKLVQKQTWDGKETTIEREVQDGKLIAKCTMGDVVAVRTYVK
>gnl|CDD|381250 cd19617, FABP12, fatty acid-binding protein 12. FABP12 is expressed in rodent retina and testis, as well as in human retinoblastoma cell lines. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
QLQGTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEE
ITPGGRKSKSTVTLDNDSLVQVQDWDGKEATITRRLVDGKMVVESAVNNVTCTRTYQR
>gnl|CDD|410998 cd19668, TmYidC_peri, periplasmic beta-super sandwich fold domain of membrane protein insertase YidC from Thermotoga maritima and similar domains. This subfamily is composed of Thermotoga maritima YidC (TmYidC) and similar proteins. Membrane protein insertase YidC, also called foldase YidC or membrane integrase YidC, facilitates proper folding, insertion, and assembly of inner membrane proteins and complexes. Depending on the nature of the substrate, YidC functions in a Sec-independent (YidC only) or a Sec-dependent manner as part of a complex containing YidC, the SecYEG channel, and SecDFYajC. YidC belongs to the YidC/Oxa1/Alb3 protein family of insertases that contain a core domain of five transmembrane (TM) segments that is essential to insertase function. In addition to this core transmembrane domain, YidC from Gram-negative bacteria contain an extra transmembrane segment (TM1) at the N-terminus and a large periplasmic domain, located between TM1 and TM2, that adopts a beta-super sandwich fold that is found in sugar-binding proteins such as galactose mutarotase. This periplasmic domain may have a role in protein assembly: a region of YidC that binds to SecF maps to one edge of the beta-super sandwich. The periplasmic domain of TmYidC shows no amino acid sequence identity with that of the prototypical Escherichia coli YidC (EcYidC), yet they adopt a similar fold. However, the periplasmic domain of TmYidC displays shorter beta strands and some differences in connectivity, compared to EcYidC
ITVEERTDTITVTTRFAEYEFDLNGNLKNVYIVVDRRVHIYEYDNDGFDLLDEGTELEPIPFSYNGDEDK
DNYESVEVTFFYENGGKKTFTFKNDPNYTFDVEINSPDPVKVTLPRISYEDNDRVAKNYFVSFAPKKKIV
SIVKFDSKLAIDGNLKFKGGKLKFKVYMGPYKRTFIKEAFPEDYDVIKELLKTIGG
>gnl|CDD|439067 cd19669, UBR-box, UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins. The UBR-box is a 70-residue zinc finger domain present in the UBR family of E3 ubiquitin ligases (UBR1-7, also called N-recognins) that directly binds N-terminal degradation signals (N-degrons) in substrate proteins to facilitate substrate ubiquitination and proteasomal degradation via the ubiquitin-proteasome system (UPS). UBR1 and UBR2 bind all type-1 and type-2 N-degrons. They mediate ubiquitination and proteolysis of short-lived regulators and misfolded proteins. UBR4 binds both type-1 and type-2 N-degrons and is involved in proteome-wide turnover of cell surface proteins. UBR5 preferentially binds type-1 N-degrons and mediates ubiquitination of short-lived proteins. UBR3, UBR6 (also called FBXO11), and UBR7 may not bind efficiently to N-degrons. UBR3 is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. UBR6 is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. It does not bind N-terminal signals. UBR7 is a RING-type E3 ubiquitin ligase that may play an important role in spermiogenesis and fertilization
CTFSITGINQVMYHCLTCSLDDNSGICEECAKKCHEGHDVVYIGSGSGFCDCGDSSAKSGFCKCHS
>gnl|CDD|439068 cd19670, UBR-box_UBR1_2_3, UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 (UBR3) and similar proteins. This family includes UBR1, UBR2, and UBR3 (all belonging to EC 2.3.2.27). Both UBR1 (also called E3alpha-I or N-recognin-1) and UBR2 (also called E3-alpha-II or N-recognin-2), are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Deficiency of UBR1 causes Johanson-Blizzard syndrome. UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both germ cells and somatic cells. It plays an important role in spermatogenesis. UBR3, also called ubiquitin-protein ligase E3-alpha-III (E3alpha-III), or N-recognin-3, or zinc finger protein 650, is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. It negatively regulates the mono-ubiquitination of non-muscle Myosin II, a protein associated with hearing loss in humans. It acts as a positive regulator of Hedgehog (Hh) signaling in Drosophila and vertebrates. It also plays an important role for genome stability by controlling cellular levels of the essential DNA repair protein APE1
CGKSLKKGELYYRCLDCSLDPSSCICEECFLNGNHEGHNYSLRTSSGGGVCDCGDSEAWKPSGFCSKHQ
>gnl|CDD|439069 cd19671, UBR-box_UBR4_5_6_7, UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins. This family includes UBR4 (EC 2.3.2.27), UBR5 (EC 2.3.2.26), UBR6/FBOX11 and UBR7 (EC 2.3.2.27). Both UBR4 (also called 600 kDa retinoblastoma protein-associated factor, or N-recognin-4, or retinoblastoma-associated factor of 600 kDa, or RBAF600, or p600, or zinc finger UBR1-type protein 1) and UBR7 (also called N-recognin-7) are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR5 (also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia. UBR6 (also called FBOX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1)), is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. UBR6 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. UBR6 does not bind N-terminal signals
CTFEKTGRKYIKQPWYHCYTCGLIDGLGVCEACARKCHKGHDLVYIGYSNFYCDCGSSGPGKCKCES
>gnl|CDD|439070 cd19672, UBR-box_UBR1_like, UBR-box found in ubiquitin-protein ligases, E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), and similar proteins. This family includes UBR1 and UBR2 (both EC 2.3.2.27). Both UBR1 (also called E3alpha-I or N-recognin-1) and UBR2 (also called E3-alpha-II or N-recognin-2), are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Deficiency of UBR1 causes Johanson-Blizzard syndrome. UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both germ cells and somatic cells. It plays an important role in spermatogenesis
VCGRVFKPGEPTYSCLDCGVDPTCVLCEDCFLNSEHVNHNYKMSISSGGGCCDCGDPEAWKSHSFCSKHG
>gnl|CDD|439071 cd19673, UBR-box_UBR3, UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins. UBR3 (EC 2.3.2.27), also called ubiquitin-protein ligase E3-alpha-III (E3alpha-III), or N-recognin-3, or zinc finger protein 650, is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. It negatively regulates the mono-ubiquitination of non-muscle Myosin II, a protein associated with hearing loss in humans. It acts as a positive regulator of Hedgehog (Hh) signaling in Drosophila and vertebrates. It also plays an important role for genome stability by controlling cellular levels of the essential DNA repair protein APE1
SGVCGRVWKAGDIAYRCRTCGLDPTCVICADCFQAGDHEGHDYSMYRSSAGGCCDCGDPEAWKPSGFCSR
HR
>gnl|CDD|439072 cd19674, UBR-box_UBR4_like, UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins. UBR4 (EC 2.3.2.27; also called 600 kDa retinoblastoma protein-associated factor, N-recognin-4, retinoblastoma-associated factor of 600 kDa, RBAF600, p600, or zinc finger UBR1-type protein 1) is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR4 acts as a multifunctional protein with roles in anoikis, viral transformation, and protein degradation, as well as in neurogenesis, neuronal migration, neuronal signaling, and survival. The family also includes Arabidopsis thaliana auxin transport protein BIG (also called protein attenuated shade avoidance 1, protein corymbosa1, protein dark over-expression of cab 1, protein low phosphate-resistant root 1, protein transport inhibitor response 3, or protein umbrella 1). It is a calossin-like protein required for auxin efflux and polar auxin transport (PAT) influencing auxin-mediated developmental responses in Arabidopsis
NVCTFASTGKNYARQHWYECYTCFLNGNEGVCEVCARVCHKGHDLVYSKTSSFFCDCGAGGGPSKCKSMR
KS
>gnl|CDD|439073 cd19675, UBR-box_UBR5, UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins. UBR5 (EC 2.3.2.26; also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia
YVLCCNDTCSFTWTGAEHINQDIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKC
KALIAG
>gnl|CDD|439074 cd19676, UBR-box_UBR6_FBXO11, UBR-box found in F-box only protein 11 (FBXO11) and similar proteins. FBXO11 (also called UBR6, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1)) is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. FBXO11 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. FBXO11 does not bind N-terminal signals
CLYKISSYTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHDRFFCDCGAGTLSNDCQLAG
>gnl|CDD|439075 cd19677, UBR-box_UBR7, UBR-box found in RING-type E3 ubiquitin-protein ligase UBR7 and similar proteins. UBR7 (EC 2.3.2.27; also called N-recognin-7) is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR7 may play an important role in spermiogenesis and fertilization
ECTYSKGYIRQAVYACLTCTPAGADQPAGICLACSLSCHEGHELEELYTKRNFRCDCGNSKFPSNPCKLF
P
>gnl|CDD|439076 cd19678, UBR-box_UBR1, UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1) and similar proteins. UBR1 (EC 2.3.2.27), also called ubiquitin-protein ligase E3-alpha-I (E3alpha-I), or N-recognin-1, is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Deficiency of UBR1 causes Johanson-Blizzard syndrome
LCGRVFKGGETTYSCRDCAIDPTCVLCMDCFQNSVHKNHRYKMHSSTGGGFCDCGDTEAWKTGPFCVKHE
P
>gnl|CDD|439077 cd19679, UBR-box_UBR2, UBR-box found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar proteins. UBR2 (EC 2.3.2.27), also called ubiquitin-protein ligase E3-alpha-II (E3alpha-II), or N-recognin-2, is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both germ cells and somatic cells. It plays an important role in spermatogenesis
LCGRVFKVGEPTYSCRDCAVDPTCVLCMECFLGSIHRDHRYRMTTSGGGGFCDCGDTEAWKEGPYCQKHE
>gnl|CDD|439078 cd19680, UBR-box_UBR4, UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins. UBR4 (EC 2.3.2.27; also called 600 kDa retinoblastoma protein-associated factor, N-recognin-4, retinoblastoma-associated factor of 600 kDa, RBAF600, p600, or zinc finger UBR1-type protein 1) is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR4 acts as a multifunctional protein with roles in anoikis, viral transformation, and protein degradation, as well as in neurogenesis, neuronal migration, neuronal signaling, and survival
KLCTFTITQKEFMNQHWYHCHTCKMVDGVGVCSVCAKVCHKDHDLSYAKYGSFFCDCGAKEDGSCQALVK
R
>gnl|CDD|439079 cd19681, UBR-box_BIG_like, UBR-box found in Arabidopsis thaliana auxin transport protein BIG and similar proteins. BIG (also called protein attenuated shade avoidance 1, protein corymbosa1, protein dark over-expression of cab 1, protein low phosphate-resistant root 1, protein transport inhibitor response 3, or protein umbrella 1) is a calossin-like protein required for auxin efflux and polar auxin transport (PAT) influencing auxin-mediated developmental responses in Arabidopsis
KVCTYVSSGSNFMEQHWYFCYTCGLVDSKGCCSVCAKVCHRGHDVVYSRYSRFFCDCGAGGAKRGRPCRC
LKPR
>gnl|CDD|381525 cd19682, bHLHzip_MGA_like, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) family. The MGA family includes MGA, Schizosaccharomyces pombe ESC1 (spESC1) and similar proteins. MGA, also termed MAX dimerization protein 5 (MAD5), is a dual specificity T-box/ bHLHzip transcription factor that regulates the expression of both Max-network and T-box family target genes. It contains a Myc-like bHLHZip motif and requires heterodimerization with Max for binding to the preferred Myc-Max-binding site CACGTG. In addition to the bHLHZip domain, MGA harbors a second DNA-binding domain, the T-box or T-domain. It thus binds the preferred Brachyury-binding sequence and represses transcription of reporter genes containing promoter-proximal Brachyury-binding sites. spESC1 is a bHLHzip protein with homology to human MyoD and Myf-5 myogenic differentiation inducers. It is involved in the sexual differentiation process
RLRHKKRERERRSELRELFDKLKQLLGLDSDEKASKLAVLTEAIEEIQQLKREEDELQKEKARLT
>gnl|CDD|381526 cd19683, bHLH_SOHLH_like, basic helix-loop-helix (bHLH) domain found in the spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein (SOHLH) family and similar proteins. The SOHLH family includes two bHLH transcription factors, SOHLH1 and SOHLH2. They are specifically in spermatogonia and oocytes and essential for early spermatogonial and oocyte differentiation. The family also includes transcription factor-like 5 protein (TCFL5) and similar proteins. TCFL5, also termed Cha transcription factor, or HPV-16 E2-binding protein 1 (E2BP-1), is a bHLH transcription factor that plays a crucial role in spermatogenesis. It regulates cell proliferation or differentiation of cells through binding to a specific DNA sequence like other bHLH molecules
KSRERHNAKERQRRERIKIACDQLRKLVPGCSRKTDKATVFEFTVAYIKFLREKLGDS
>gnl|CDD|381527 cd19684, bHLH_dnHLH_ID, basic helix-loop-helix (bHLH) domain found in the DNA-binding protein inhibitor (ID) family. The ID family includes a dominant negative group of helix-loop-helix (dnHLH) proteins, ID1-4, that are negative regulators of bHLH transcription factors. They contain the HLH-dimerization domain but lack the basic domain necessary for DNA-binding. ID proteins inhibit binding to DNA and transcriptional transactivation by heterodimerization with bHLH proteins. They also interact with many non-bHLH proteins in complex networks. ID proteins have been implicated in regulating gene expression as well as cell-cycle progression. Whereas ID-1, ID-2 and ID-3, are generally considered as tumor promoters, ID4 on the contrary has emerged as a tumor suppressor
NDILNAEMQDCYSKLKELVPTIPQNKKVSKVEILQHVIDYILDLQLA
>gnl|CDD|381528 cd19685, bHLH-O_HERP_HES, basic helix-loop-helix-orange (bHLH-O) domain found in HERP/HES-like family. The HERP/HES-like family includes bHLH-O transcriptional regulators that are related to the Drosophila hairy and Enhancer-of-split (HES) proteins. The HERP (HES-related repressor protein) subfamily proteins contain a basic helix-loop-helix (bHLH) domain with an invariant glycine residue in its basic region, an orange domain in the central region and YXXW sequence motif at its C-terminal region. Hairy and enhancer of split (HES)-related repressor protein (HERP) proteins (HEY1, HEY2 and HEYL) act as downstream effectors of Notch signaling. They are involved in cardiovascular development and have roles in somitogenesis, myogenesis and gliogenesis. Hairy and enhancer of split-related protein HELT is a transcriptional repressor expressed in the developing central nervous system. It binds preferentially to the canonical E box sequence 5'-CACGCG-3' and regulates neuronal differentiation and/or identity. Differentially expressed in chondrocytes proteins, DEC1 and DEC2, are widely expressed in both embryonic and adult tissues and have been implicated in apoptosis, cell proliferation, and circadian rhythms, as well as malignancy in various cancers. Drosophila melanogaster protein clockwork orange (Cwo) is also included in this subfamily. It is involved in the regulation of Drosophila circadian rhythms. It functions as both an activator and a repressor of clock gene expression. The HES subfamily proteins contain a basic helix-loop-helix (bHLH) domain with an invariant proline residue in its basic region, an orange domain in the central region and a conserved tetrapeptide motif, WRPW, at its C-terminal region. They form heterodimers or homodimers via their HLH domain and bind DNA to repress gene transcription that play an essential role in development of both compartment and boundary cells of the central nervous system
SEKRRRQRINDKLNQLKELLPPNLSKQSRSKLSKAEILEMAITELRRLQQEV
>gnl|CDD|381529 cd19686, bHLH_TS_FERD3L_like, basic helix-loop-helix (bHLH) domain found in Fer3-like protein (FERD3L), pancreas transcription factor 1 subunit alpha (PTF1A) and similar proteins. The family corresponds to a group of bHLH transcription factors, including FERD3L and PTF1A. FERD3L, also termed basic helix-loop-helix protein N-twist, or Class A basic helix-loop-helix protein 31 (bHLHa31), or nephew of atonal 3 (NATO3), or Neuronal twist (NTWIST), is expressed in the developing central nervous system (CNS). It regulates floor plate (FP) cells development. FP is a critical organizing center located at the ventral-most midline of the neural tube. FERD3L binds to the E-box and functions as inhibitor of transcription. PTF1A, also termed Class A basic helix-loop-helix protein 29 (bHLHa29), or pancreas-specific transcription factor 1a, or bHLH transcription factor p48, or p48 DNA-binding subunit of transcription factor PTF1 (PTF1-p48), is implicated in the cell fate determination in various organs. It binds to the E-box consensus sequence 5'-CANNTG-3' and plays a role in early and late pancreas development and differentiation
QRQAANIRERKRMRSINDAFDGLRRHIPTFPYEKRLSKVDTLRLAIQYINFLTELL
>gnl|CDD|381530 cd19687, bHLHzip_Mlx, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) and similar proteins. Mlx, also termed Class D basic helix-loop-helix protein 13 (bHLHd13), or Max-like bHLHZip protein, or protein BigMax, or transcription factor-like protein 4, is a Max-like bHLHZip transcription regulator that interacts with the Max network of transcription factors. It forms a sequence-specific DNA-binding protein complex with some member of Mad family (Mad1 and Mad4) and Mondo family but not the Myc family and bind the E-box DNA to control transcription
RRREAHTQAEQKRRDAIKKGYDDLQDIVPTCQQQDDIGSQKLSKATILQRSIDYIQFLHQQKKKQEEELS
ALRKEV
>gnl|CDD|381531 cd19688, bHLHzip_MLXIP, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP) and similar proteins. MLXIP, also termed Class E basic helix-loop-helix protein 36 (bHLHe36), or transcriptional activator MondoA, is a bHLHZip transcriptional activator that binds DNA as a heterodimer with Mlx. It binds to the canonical E box sequence 5'-CACGTG-3' and plays a role in transcriptional activation of glycolytic target genes. MLXIP is most highly expressed in skeletal muscle and functions as an indirect glucose sensor, by sensing glucose 6-phosphate and shuttling between the nucleus and the cytoplasm
KNRRMKHISAEQKRRFNIKICFDTLNSLVSTLKNSKPISNAITLQKTVEYIAKLQQERTQMQEETKRLRE
EI
>gnl|CDD|381532 cd19689, bHLHzip_MLXIPL, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein-like (MLXIPL) and similar proteins. MLXIPL, also termed carbohydrate-responsive element-binding protein (ChREBP), or Class D basic helix-loop-helix protein 14 (bHLHd14), or MLX interactor, or WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), is a bHLHZip transcriptional factor integral to the regulation of glycolysis and lipogenesis in the liver. It forms heterodimers with the bHLHZip protein Mlx to bind the DNA sequence 5'-CACGTG-3'
KTETRRITHISAEQKRRFNIKLGFDTLHSLVTTLSSQPSIKISKATTLQKTAEYISKLQQERAQLQEEAQ
RLRDQI
>gnl|CDD|381533 cd19690, bHLHzip_spESC1_like, basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Schizosaccharomyces pombe ESC1 (spESC1) and similar proteins. spESC1 is a bHLHzip protein with homology to human MyoD and Myf-5 myogenic differentiation inducers. It is involved in the sexual differentiation process
RVSHKLAERKRRKEMKELFEDLRDALPQERGTKASKWEILTKAISYIQQLKRHIRELRSEVNDLR
>gnl|CDD|381534 cd19691, bHLH_dnHLH_ID1, basic helix-loop-helix (bHLH) domain found in DNA-binding protein inhibitor ID1 and similar proteins. ID1, also termed Class B basic helix-loop-helix protein 24 (bHLHb24), or inhibitor of DNA binding 1, or inhibitor of differentiation 1, is a dominant negative helix-loop-helix (dnHLH) transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the bHLH transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. ID1 interferes with centrosomal function. It has been implicated in the regulation of cell proliferation and differentiation in myogenesis, neurogenesis, and/or hematopoiesis
MNMLLYDMNGCYSRLKELVPTLPQNRKVSKVEILQHVIDYIWDLQVELDSGP
>gnl|CDD|381535 cd19692, bHLH_dnHLH_ID2, basic helix-loop-helix (bHLH) domain found in DNA-binding protein inhibitor ID2 and similar proteins. ID2, also termed Class B basic helix-loop-helix protein 26 (bHLHb26), or inhibitor of DNA binding 2, or inhibitor of differentiation 2, is a dominant negative helix-loop-helix (dnHLH) transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the bHLH transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. It has been implicated in the regulation of cell proliferation and differentiation in myogenesis, neurogenesis, and/or hematopoiesis
HSLGISRSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVSKMEILQHVIDYILDLQIALDSHP
>gnl|CDD|381536 cd19693, bHLH_dnHLH_ID3, basic helix-loop-helix (bHLH) domain found in DNA-binding protein inhibitor ID3 and similar proteins. ID3, also termed Class B basic helix-loop-helix protein 25 (bHLHb25), or helix-loop-helix protein HEIR-1, or ID-like protein inhibitor HLH 1R21, or inhibitor of DNA binding 3, or inhibitor of differentiation 3, is a dominant negative helix-loop-helix (dnHLH) transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the bHLH transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. It negatively regulates muscle differentiation by inhibiting the DNA-binding activities of the myogenic regulatory factors
SSRNGSNKGPALEEPVSLLYDMNDCYSRLRELVPGVPQGTKLSQVEILQHVIDYILDLQIV
>gnl|CDD|381537 cd19694, bHLH_dnHLH_ID4, basic helix-loop-helix (bHLH) domain found in DNA-binding protein inhibitor ID4 and similar proteins. ID4, also termed Class B basic helix-loop-helix protein 27 (bHLHb27), or inhibitor of DNA binding 4, or inhibitor of differentiation 4, is a dominant negative helix-loop-helix (dnHLH) transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the bHLH transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. It plays a role in adipose cell differentiation
EEEALCLQYDMNDCYSRLKRLVPTIPPNKKVSKVEILQHVIDYILDLQLALETHPALLRQ
>gnl|CDD|381538 cd19695, bHLH_dnHLH_EMC_like, basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster protein extra-macrochaetae and similar proteins. Extra-macrochaetae is a negative regulator of sensory organ development in Drosophila. It belongs to dominant negative group of helix-loop-helix (dnHLH) proteins, which lack a basic DNA-binding domain but can form heterodimers with other HLH proteins, thereby inhibiting DNA binding
LNQERREMALYLAKLRNLVPTLPKNRKVSKLELLQHVIDYIADLEEQLEDHP
>gnl|CDD|381539 cd19696, bHLH-PAS_AhR_like, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in the aryl hydrocarbon receptor (AhR) family. The AhR family includes AhR, AhR repressor (AhRR) and Drosophila melanogaster protein spineless. AhR, also termed Ah receptor, or Dioxin receptor (DR), or Class E basic helix-loop-helix protein 76 (bHLHe76), is the only member of bHLH-PAS transcription regulators that bind and be activated by small chemical ligands. It is activated by Dioxin to control the expression of certain genes to influence biological processes such as apoptosis, proliferation, cell growth and differentiation. To form active DNA binding complexes AhR dimerizes with a bHLH-PAS factor ARNT (Aryl hydrocarbon Nuclear Receptor Translocator). AhRR, also termed Class E basic helix-loop-helix protein 77 (bHLHe77), is a member of bHLH-PAS transcription factors that acts as a negative regulator of AhR, playing key roles in development and environmental sensing. AhRR functions by competing with AhR for its partner ARNT. AhRR-ARNT complexes are transcriptionally inactive. Spineless is a bHLH-PAS transcription factor that plays an important role in fly morphogenesis. It is both necessary and sufficient for the formation of the ommatidial mosaic
GGVKSNPSKRHRDRLNSELDELASLLPFPEDVISKLDKLSVLRLSVSYLRTKNYFQAVL
>gnl|CDD|381540 cd19697, bHLH-PAS_NPAS4_PASD10, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing protein 4 (NPAS4) and similar proteins. NPAS4, also termed neuronal Per-Arnt-Sim homology (PAS) factor 4, or neuronal PAS4, or Class E basic helix-loop-helix protein 79 (bHLHe79), or HLH-PAS transcription factor NXF, or PAS domain-containing protein 10 (PASD10), is a bHLH-PAS neuronal activity-dependent transcription factor which heterodimerizes with ARNT2 to regulate genes involved in inhibitory synapse formation
GRSTKGASKQRRDLINAEIRELRDLLPLPESTRQRLSQLQIMSLACVYIRKSNFFSQ
>gnl|CDD|381541 cd19698, bHLH_AtMEE8_like, basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein maternal effect embryo arrest 8 (AtMEE8) and similar proteins. AtMEE8, also termed AtbHLH108, or EN 132, is a bHLH transcription factor required during early embryo development, for the endosperm formation
HNLLEKKRRERIKDKIEILKGLTPNCTPKSDIASILSCVIDYIKSLLLQVEKLSMGICDDWRLFTPFGAV
L
>gnl|CDD|381542 cd19699, bHLH_TS_dMYOD_like, basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster myogenic-determination protein (dMYOD) and similar proteins. dMYOD, also termed protein nautilus, or Myd, may play an important role in the early development of muscle in Drosophila
DRRKAATMRERRRLRKVNEAFEVLKRRTCPNPNQRLPKVEILRNAIEYIESLEDLL
>gnl|CDD|381543 cd19700, bHLH_TS_TWIST2, basic helix-loop-helix (bHLH) domain found in twist-related protein 2 (TWIST2) and similar proteins. TWIST2, also termed Class A basic helix-loop-helix protein 39 (bHLHa39), or Dermis-expressed protein 1, or Dermo-1, is a bHLH transcription factor that regulates the development of mesenchymal tissues and plays a critical role in embryogenesis. It binds to the E-box consensus sequence 5'-CANNTG-3' as a heterodimer and inhibits transcriptional activation by MYOD1, MYOG, MEF2A and MEF2C
GKKSSPSSQSYEELQSQRILANVRERQRTQSLNEAFAALRKIIPTLPSDKLSKIQTLKLAARYIDFLYQV
LQSDEMDNKMTS
>gnl|CDD|381544 cd19701, bHLH_TS_HEN1, basic helix-loop-helix (bHLH) domain found in helix-loop-helix protein 1 (HEN-1) and similar proteins. HEN-1, also termed nescient helix-loop-helix 1 (Nhlh1), or Class A basic helix-loop-helix protein 35 (bHLHa35), or nescient helix loop helix 1 (NSCL-1), is a neuron-specific bHLH transcription factor that may serve as DNA-binding protein and may be involved in the control of cell-type determination, possibly within the developing nervous system
LSREERRRRRRATAKYRTAHATRERIRVEAFNVAFAELRKLLPTLPPDKKLSKIEILRLAICYISYLNHV
LD
>gnl|CDD|381545 cd19702, bHLH_TS_HEN2, basic helix-loop-helix (bHLH) domain found in helix-loop-helix protein 2 (HEN-2) and similar proteins. HEN-2, also termed nescient helix-loop-helix 2 (Nhlh2), or Class A basic helix-loop-helix protein 34 (bHLHa34), or nescient helix loop helix 2 (NSCL-2), is a neuron-specific bHLH transcription factor that may serve as DNA-binding protein and may be involved in the control of cell-type determination, possibly within the developing nervous system
LSREEKRRRRRATAKYRSAHATRERIRVEAFNLAFAELRKLLPTLPPDKKLSKIEILRLAICYISYLNHV
LDV
>gnl|CDD|381546 cd19703, bHLH_TS_musculin, basic helix-loop-helix (bHLH) domain found in musculin and similar proteins. Musculin, also termed activated B-cell factor 1 (ABF-1), or Class A basic helix-loop-helix protein 22 (bHLHa22), is a bHLH transcription factor expressed in activated B lymphocytes. It acts as a transcription repressor capable of inhibiting the transactivation capability of TCF3/E47. Musculin may play a role in regulating antigen-dependent B-cell differentiation. The mouse homolog, musculin, is suggested to be a repressor of myogenesis that is expressed in developing muscle and in the spleen. Musculin heterodimerizes with products of the E2A gene
KQSQRNAANARERARMRVLSKAFSRLKTSLPWVPPDTKLSKLDTLRLASSYIAHLRQLLQEDRYEN
>gnl|CDD|381547 cd19704, bHLH_TS_TCF21_capsulin, basic helix-loop-helix (bHLH) domain found in transcription factor 21 (TCF-21) and similar proteins. TCF-21, also termed capsulin, or Class A basic helix-loop-helix protein 23 (bHLHa23), or epicardin, or podocyte-expressed 1 (Pod-1), is a bHLH transcription factor expressed specifically in mesodermally-derived cells that surround the epithelium of the developing gastrointestinal, genitourinary and respiratory systems during mouse embryogenesis. It may play a role in the specification or differentiation of one or more subsets of epicardial cell types
KQVQRNAANARERARMRVLSKAFSRLKTTLPWVPPDTKLSKLDTLRLASSYIAHLRQILANDKY
>gnl|CDD|381548 cd19705, bHLH_TS_LYL1, basic helix-loop-helix (bHLH) domain found in protein lyl-1 and similar proteins. Lyl-1, also termed Class A basic helix-loop-helix protein 18 (bHLHa18), or lymphoblastic leukemia-derived sequence 1, is a proto-oncogenic bHLH transcription factor involved in T-cell acute lymphoblastic leukemia. It plays an important role in hematopoietic stem cell function and is required for the late stages of postnatal angiogenesis to limit the formation of new blood vessels, notably by regulating the activity of the small GTPase Rap1. LYL-1 deficiency induces a stress erythropoiesis
PQKVARRVFTNSRERWRQQNVNGAFAELRKLIPTHPPDKKLSKNEILRLAMKYIDFLVTLLRDQA
>gnl|CDD|381549 cd19706, bHLH_TS_TAL1, basic helix-loop-helix (bHLH) domain found in T-cell acute lymphocytic leukemia protein 1 (TAL-1) and similar proteins. TAL-1, also termed Class A basic helix-loop-helix protein 17 (bHLHa17), or stem cell protein (SCL), or T-cell leukemia/lymphoma protein 5, is a hematopoietic-specific bHLH transcription factor that functions in embryonic and adult hematopoiesis in vertebrates. It is also required for embryonic vascular remodeling. It acts as a regulator of erythroid differentiation and binds to regulatory regions of a large cohort of erythroid genes as part of a complex with GATA-1, LMO2 and Ldb1. TAL-1 has been implicated in T-cell acute lymphoblastic leukemia. In common with other tissue-specific bHLH proteins, Tal heterodimerizes with ubiquitously-expressed members of the E2A family and form a DNA-binding complex with an E-box (CANNTG) to regulate transcription at its recognition site
KVVRRIFTNSRERWRQQNVNGAFAELRKLIPTHPPDKKLSKNEILRLAMKYINFLAKLLNDQEEE
>gnl|CDD|381550 cd19707, bHLH_TS_TAL2, basic helix-loop-helix (bHLH) domain found in T-cell acute lymphocytic leukemia protein 2 (TAL-2) and similar proteins. TAL-2, also termed Class A basic helix-loop-helix protein 19 (bHLHa19), is a bHLH transcription factor essential for the normal brain development. It has been implicated in T-cell acute lymphoblastic leukemia
TRKIFTNTRERWRQQNVNSAFAELRKLIPTHPPDKKLSKNEILRLAMKYINFLVKLLGDQG
>gnl|CDD|381551 cd19708, bHLH_TS_dHLH3B_like, basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster helix loop helix protein 3B (dHLH3B) and similar proteins. Drosophila HLH3B is an uncharacterized bHLH transcription factor that belongs to the T-cell acute lymphocytic leukemia protein/ lymphoblastic leukemia-derived sequence (TAL/LYL) family
RRMFTNSRERWRQQNVNGAFAELRKLVPTHPPDKKLSKNEILRLAIKYIRLLSNVLEWQK
>gnl|CDD|381552 cd19709, bHLH_TS_TCF23_OUT, basic helix-loop-helix (bHLH) domain found in transcription factor 23 (TCF-23) and similar proteins. TCF-23, also termed Class A basic helix-loop-helix protein 24 (bHLHa24), is a bHLH transcription factor that is essential for progesterone-dependent decidualization. The mouse homolog is also called ovary, uterus and testis protein (OUT), which is expressed predominantly in the reproductive organs such as the uterus, ovary and testis. It shows an Id-like inhibitory activity and functions as a negative regulator of bHLH factors through the formation of a functionally inactive heterodimeric complex. OUT inhibits the formation of TCF3 and MYOD1 homodimers and heterodimers, but lacks DNA binding activity. OUT is involved in the regulation or modulation of smooth muscle contraction of the uterus during pregnancy and particularly around the time of delivery. It also plays a role in the inhibition of myogenesis. Unlike typical bHLH factors, OUT proteins do not bind E-box (CANNTG) or N-box DNA sequences and inhibit DNA binding of homo- and heterodimers consisting of E12 and MyoD in gel mobility shift assays
SPENAARERSRVRTLRQAFLALQAALPSVPPDTKLSKLDVLVLATSYIAHLTRTLD
>gnl|CDD|381553 cd19710, bHLH_TS_TCF24, basic helix-loop-helix (bHLH) domain found in transcription factor 24 (TCF-24) and similar proteins. TCF-24 is an uncharacterized bHLH transcription factor that shows high sequence similarity with TCF-23
PAAANAARERSRVQTLRSAFLELQRTLPSVPPDTKLSKLDVLVLATTYIAHLMRTL
>gnl|CDD|381554 cd19711, bHLH_TS_MIST1, basic helix-loop-helix (bHLH) domain found in muscle, intestine and stomach expression 1 (MIST-1) and similar proteins. MIST-1, also termed Class A basic helix-loop-helix protein 15 (bHLHa15), or Class B basic helix-loop-helix protein 8 (bHLHb8), is a bHLH transcription factor expressed in pancreatic acinar cells and other serous exocrine cells. It is essential for cytoskeletal organization and secretory activity. It also functions as a potent endoplasmic reticulum (ER) stress-inducible transcriptional regulator. MIST-1 is capable of binding to E-box (CANNTG) motifs as a homodimer or a heterodimer with E-proteins (E12 and E47) to regulate transcription
RRLESNERERQRMHKLNNAFQALREVIPHVRAEKKLSKIETLTLAKNYIKSLTTTILNMSNG
>gnl|CDD|381555 cd19712, bHLH_TS_dimmed_like, basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster protein dimmed and similar proteins. Dimmed, also termed DIMM, is a bHLH transcription factor that regulates neurosecretory (NS) cell function and neuroendocrine cell fate in Drosophila
RRLESNERERMRMHSLNDAFQGLREVIPHVNAERKLSKIETLTLAKNYIKALTNVICELR
>gnl|CDD|381556 cd19713, bHLH_TS_ATOH1, basic helix-loop-helix (bHLH) domain found in protein atonal homolog 1 (ATOH1) and similar proteins. ATOH1, also termed Class A basic helix-loop-helix protein 14 (bHLHa14), or helix-loop-helix protein hATH-1 (hATH1), or Math1, or Cath1, is a proneural bHLH transcription factor that is essential for inner ear hair cell differentiation. It dimerizes with E47 and activates E-box (CANNTG) dependent transcription. ATOH1 is a mammalian homolog of the Drosophila melanogaster gene atonal and mouse atonal homolog 1 (Math1)
GVQKQRRLAANARERRRMHGLNHAFDQLRNVIPSFNNDKKLSKYETLQMAQIYINALSELLQGP
>gnl|CDD|381557 cd19714, bHLH_TS_ATOH7, basic helix-loop-helix (bHLH) domain found in protein atonal homolog 7 (ATOH7) and similar proteins. ATOH7, also termed Class A basic helix-loop-helix protein 13 (bHLHa13), or helix-loop-helix protein hATH-5 (hATH5), or Math5, is a bHLH transcription factor involved in the differentiation of retinal ganglion cells
RLESAARRRLAANARERRRMQGLNTAFDRLRKVVPQWGQDKKLSKYETLQMALSYIMALTRILAEAERY
>gnl|CDD|381558 cd19715, bHLH_TS_amos_like, basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster protein Amos and similar proteins. Amos, also termed absent MD neurons and olfactory sensilla protein, or reduced olfactory organs protein, or rough eye protein, is a bHLH transcription factor that promotes multiple dendritic neuron formation in the Drosophila peripheral nervous system
GKDVLKKRRLAANARERRRMNSLNVAFDKLRDVVPSLGDDRKLSKYETLQMAQSYITALKELLS
>gnl|CDD|381559 cd19716, bHLH_TS_NGN1_NeuroD3, basic helix-loop-helix (bHLH) domain found in neurogenin-1 (NGN-1) and similar proteins. NGN-1, also termed Class A basic helix-loop-helix protein 6 (bHLHa6), or neurogenic basic-helix-loop-helix protein, or neurogenic differentiation factor 3 (NeuroD3), is a neural-specific bHLH transcription factor involved in the initiation of neuronal differentiation. It activates transcription by binding to the E box (5'-CANNTG-3')
RSRVKNEALLHTIKKSRRVKANDRERNRMHNLNAALDELRSVLPSFPDDTKLTKIETLRFAHNYIWALSE
TLRLADQ
>gnl|CDD|381560 cd19717, bHLH_TS_NGN2_ATOH4, basic helix-loop-helix (bHLH) domain found in neurogenin-2 (NGN-2) and similar proteins. NGN-2, also termed Class A basic helix-loop-helix protein 8 (bHLHa8), or protein atonal homolog 4 (ATOH4), is a neural-specific bHLH transcription factor required for sensory neurogenesis. It activates transcription by binding to the E box (5'-CANNTG-3')
ETVLKIKKTRRVKANNRERNRMHNLNAALDSLREVLPTFPEDAKLTKIETLRFAHNYIWALSETLRLAD
>gnl|CDD|381561 cd19718, bHLH_TS_NGN3_ATOH5, basic helix-loop-helix (bHLH) domain found in neurogenin-3 (NGN-3) and similar proteins. NGN-3, also termed Class A basic helix-loop-helix protein 7 (bHLHa7), or protein atonal homolog 5 (ATOH5), is a neural-specific bHLH transcription factor expressed in the developing central nervous system and the embryonic pancreas. It is involved in neurogenesis and plays an important role in spermatogenesis
VSKQKRNRRMKANDRERNRMHNLNSALDALRSVLPTFPDDAKLTKIETLRFAHNYIWALTETLRMADH
>gnl|CDD|381562 cd19719, bHLH_TS_NeuroD1, basic helix-loop-helix (bHLH) domain found in neurogenic differentiation factor 1 (NeuroD1) and similar proteins. NeuroD1, also termed Class A basic helix-loop-helix protein 3 (bHLHa3), is a neuronal bHLH transcription factor involved in the development and maintenance of the endocrine pancreas and neuronal elements. It acts as an essential regulator of glutamatergic neuronal differentiation. Loss of NeuroD1 causes ataxia, cerebellar hypoplasia, sensorineural deafness, and severe retinal dystrophy in mice
EDDDQKPKRRGPKKKKMTKARLERFKMRRMKANARERNRMHGLNAALDNLRKVVPCYSKTQKLSKIETLR
LAKNYIWALSEILRSG
>gnl|CDD|381563 cd19720, bHLH_TS_NeuroD2, basic helix-loop-helix (bHLH) domain found in neurogenic differentiation factor 2 (NeuroD2) and similar proteins. NeuroD2, also termed Class A basic helix-loop-helix protein 1 (bHLHa1), or NeuroD-related factor (NDRF), is a neuronal calcium-dependent bHLH transcription factor that induces neuronal differentiation and promotes neuronal survival. It plays a central role in thalamocortical synaptic maturation. NeuroD2 mediates calcium-dependent transcription activation by binding to E box-containing promoter
EEEEGLEEADGERPKKRGPKKRKMTKARLERSKLRRQKANARERNRMHDLNSALDNLRKVVPCYSKTQKL
SKIETLRLAKNYIWALSEILRSG
>gnl|CDD|381564 cd19721, bHLH_TS_NeuroD4_ATOH3, basic helix-loop-helix (bHLH) domain found in neurogenic differentiation factor 4 (NeuroD4) and similar proteins. NeuroD4, also termed Class A basic helix-loop-helix protein 4 (bHLHa4), or protein atonal homolog 3 (ATH-3), or Atoh3, or Math-3, is a bHLH transcriptional activator that mediates neuronal differentiation
EEEEDGEKPKRRGPKKKKMTKARLERFRARRVKANARERSRMHGLNDALDNLRRVMPCYSKTQKLSKIET
LRLARNYIWALSEVLET
>gnl|CDD|381565 cd19722, bHLH_TS_NeuroD6_ATOH2, basic helix-loop-helix (bHLH) domain found in neurogenic differentiation factor 6 (NeuroD6) and similar proteins. NeuroD6, also termed Class A basic helix-loop-helix protein 2 (bHLHa2), or protein atonal homolog 2 (ATH-2), or Atoh2, or Math2, or Nex1, is a neurogenic bHLH transcription factor involved in neuronal development, differentiation, and survival in Alzheimer's disease (AD) brains of both cohorts. It plays an integrative role in coordinating increase in mitochondrial mass with cytoskeletal remodeling, suggesting that it may act as a co-regulator of neuronal differentiation and energy metabolism
KKMTKARMERVKVRRQEANARERNRMHGLNDALDSLRKVVPCYSKTQKLSKIETLRLAKNYIWALSEILR
>gnl|CDD|381566 cd19723, bHLH_TS_ASCL1_like, basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster achaete-scute complex (AS-C) proteins, achaete-scute-like proteins, ASCL1-2, and similar proteins. This subfamily includes Drosophila melanogaster AS-C proteins and two ASCL family of transcription factors, ASCL-1 and ASCL-2. Drosophila melanogaster AS-C proteins includes lethal of scute (also known as achaete-scute complex protein T3 or AST3), scute (also known as achaete-scute complex protein T4 or AST4), achaete (also known as achaete-scute complex protein T5 or AST5), and asense (also known as achaete-scute complex protein T8 or AST8). They are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system, as well as in sex determination and dosage compensation. ASCL-1, also termed Class A basic helix-loop-helix protein 46 (bHLHa46), or achaete-scute homolog 1 (ASH-1), or mammalian achaete scute homolog 1 (Mash1), is expressed in subsets of neural progenitors in both the central and peripheral nervous system. It plays a key role in neuronal differentiation and specification in the nervous system. ASCL-2, also termed achaete-scute homolog 2 (ASH-2), or Class A basic helix-loop-helix protein 45 (bHLHa45), or mammalian achaete scute homolog 2 (Mash2), is involved in Schwann cell differentiation and control of proliferation in adult peripheral nerves
AVARRNERERNRVKLVNLGFATLREHVPNGRANKKMSKVETLRSAVEYIRQLQQLL
>gnl|CDD|381567 cd19724, bHLH_TS_ASCL3_like, basic helix-loop-helix (bHLH) domain found in achaete-scute-like proteins, ASCL3-5, and similar proteins. This subfamily includes three ASCL family of transcription factors, ASCL-3, ASCL-4 and ASCL-5. ASCL-3, also termed Class A basic helix-loop-helix protein 42 (bHLHa42), or bHLH transcriptional regulator Sgn-1, or achaete-scute homolog 3 (ASH-3), is specifically localized in the duct cells of the salivary glands. It may act as transcriptional repressor that inhibits myogenesis. ASCL-4, also termed Class A basic helix-loop-helix protein 44 (bHLHa44), or achaete-scute homolog 4 (ASH-4), or Hash4, may be involved in skin development. ASCL-5, also termed Class A basic helix-loop-helix protein 47 (bHLHa47), or achaete-scute homolog 5 (ASH-5), is an uncharacterized bHLH transcription factor that is close related to ASCL-3 and ASCL-4
FIRKRNERERQRVRCVNEGYARLRRHLPLENKDKRLSKVETLRAAIRYIKHLQELL
>gnl|CDD|381568 cd19725, bHLH_TS_OLIG2_like, basic helix-loop-helix (bHLH) domain found in oligodendrocyte transcription factors, Oligo2, Oligo3 and similar proteins. The family includes two bHLH transcription factors, Oligo2 and Oligo3. Oligo2, also termed Class B basic helix-loop-helix protein 1 (bHLHb1), or Class E basic helix-loop-helix protein 19 (bHLHe19), or protein kinase C-binding protein 2, or protein kinase C-binding protein RACK17, is required for oligodendrocyte and motor neuron specification in the spinal cord, as well as for the development of somatic motor neurons in the hindbrain. It cooperates with OLIG1 to establish the MN progenitors (pMN) domain of the embryonic neural tube. Oligo3, also termed Class B basic helix-loop-helix protein 7 (bHLHb7), or Class E basic helix-loop-helix protein 20 (bHLHe20), is expressed in the ventricular zone of the dorsal alar plate of the hindbrain and involved in regulating the development of dorsal and ventral spinal cord. It may determine the distinct specification program of class A neurons in the dorsal part of the spinal cord and suppress specification of class B neurons
LRLKINSRERKRMHDLNSALDGLREVMPYAHGPSVRKLSKIATLLLARNYILMLTNSLEEMKR
>gnl|CDD|381569 cd19726, bHLH-PAS_cycle_like, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein cycle and similar proteins. Protein cycle, also termed brain and muscle ARNT-like 1 (BMAL1), or MOP3, is a putative bHLH-PAS transcription factor involved in the generation of biological rhythms in Drosophila. It activates cycling transcription of Period (PER) and Timeless (TIM) by binding to the E-box (5'-CACGTG-3') present in their promoters
RRQNHSEIEKRRRDKMNTYITELSSMIPMCNAMSRKLDKLTVLRMAVQHMKTLRGSLTSYTE
>gnl|CDD|381570 cd19727, bHLH-PAS_HIF1a_PASD8, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor 1-alpha (HIF1a) and similar proteins. HIF1a, also termed HIF-1-alpha, or HIF1-alpha, or ARNT-interacting protein, or Basic-helix-loop-helix-PAS protein MOP1, or Class E basic helix-loop-helix protein 78 (bHLHe78), or Member of PAS protein 1, or PAS domain-containing protein 8 (PASD8), functions as a master transcriptional regulator of the adaptive response to hypoxia
VSSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASIMRLTISYLRMRKLLDAGELEEEA
D
>gnl|CDD|381571 cd19728, bHLH-PAS_HIF2a_PASD2, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor 2-alpha (HIF2a) and similar proteins. HIF2a, also termed HIF-2-alpha, or HIF2-alpha, or endothelial PAS domain-containing protein 1 (EPAS-1), or Basic-helix-loop-helix-PAS protein MOP2, or Class E basic helix-loop-helix protein 73 (bHLHe73), or Member of PAS protein 2, or PAS domain-containing protein 2 (PASD2), or HIF-1-alpha-like factor (HLF), is a bHLH-PAS transcription factor involved in the induction of oxygen regulated genes
RSSSERRKEKSRDAARCRRSKETEVFYELAHQLPLPHSVSSHLDKASIMRLAISFLRTHKLLSSVC
>gnl|CDD|381572 cd19729, bHLH-PAS_HIF3a_PASD7, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor 3-alpha (HIF3a) and similar proteins. HIF3a, also termed HIF-3-alpha, or HIF3-alpha, or endothelial PAS domain-containing protein 1 (EPAS-1), or Basic-helix-loop-helix-PAS protein MOP7, or Class E basic helix-loop-helix protein 17 (bHLHe17), or Member of PAS protein 7, or PAS domain-containing protein 7 (PASD7), or HIF3-alpha-1, or inhibitory PAS domain protein (IPAS), is a bHLH-PAS transcriptional regulator in adaptive response to low oxygen tension. It plays a role in the regulation of hypoxia-inducible gene expression
TEQRKEKSRDAARCRRSQETEVFYELAHTLPFPRGVSSHLDKASIMRLTISYLRMHRLIASGE
>gnl|CDD|381573 cd19730, bHLH-PAS_spineless_like, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein spineless and similar proteins. Spineless is a bHLH-PAS transcription factor that plays an important role in fly morphogenesis. It is both necessary and sufficient for the formation of the ommatidial mosaic
PKDHPTKSNPSKRHRERLNAELDHLASLLPFEQSVISKLDKLSILRLSVSYLRTKSYFQAVLQK
>gnl|CDD|381574 cd19731, bHLH-PAS_NPAS1_PASD5, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing protein 1 (NPAS1) and similar proteins. NPAS1, also termed neuronal PAS1, or Basic-helix-loop-helix-PAS protein MOP5, or Class E basic helix-loop-helix protein 11 (bHLHe11), or member of PAS protein 5, or PAS domain-containing protein 5 (PASD5), is a bHLH-PAS transcriptional repressor expressed in the central nervous system and involved in neuronal differentiation. It is active during late embryogenesis and postnatal development
QALRKEKSRNAARSRRGKENFEFYELAKMLPLPGAITSQLDKASIVRLTISYLKMRDFASHGDPPWSLRA
EGPP
>gnl|CDD|381575 cd19732, bHLH-PAS_NPAS3_PASD6, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing protein 3 (NPAS3) and similar proteins. NPAS3, also termed neuronal PAS3, or Basic-helix-loop-helix-PAS protein MOP6, or Class E basic helix-loop-helix protein 12 (bHLHe12), or member of PAS protein 6, or PAS domain-containing protein 6 (PASD6), is a bHLH-PAS brain-enriched transcription factor that is involved in central nervous system development and neurogenesis. It is a replicated genetic risk factor for psychiatric disorders. Human chromosomal rearrangements that affect NPAS3 normal expression are associated with schizophrenia and mental retardation
RLQALRKEKSRDAARSRRGKENFEFYELAKLLPLPAAITSQLDKASIIRLTISYLKMRDFANQGDPPWNL
RMEGPPPN
>gnl|CDD|381576 cd19733, bHLH-PAS_trachealess_like, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein trachealess and similar proteins. Protein trachealess is a bHLH-PAS transcription factor that acts as an inducer of tracheal cell fates in Drosophila. It is necessary for the development of the salivary gland duct and the posterior spiracles
ILELRKEKSRDAARSRRGKENYEFYELAKMLPLPAAITSQLDKASIIRLTISYLKLRDFSGHGDPPWNRE
SLSSPPSTS
>gnl|CDD|381577 cd19734, bHLH-PAS_CLOCK, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output cycles protein kaput (CLOCK) and similar proteins. CLOCK, also termed Class E basic helix-loop-helix protein 8 (bHLHe8), is a bHLH-PAS transcriptional activator which forms a core component of the circadian clock. It forms heterodimers with another bHLH-PAS protein, Brain-Muscle-Arnt-Like (also known as BMAL or ARNT3 or mop3), which regulates circadian rhythm. BMAL1-CLOCK heterodimer complex activates transcription from E-box (CANNTG) elements found in the promoter of circadian responsive genes
DDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITA
>gnl|CDD|381578 cd19735, bHLH-PAS_dCLOCK, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster Circadian locomotor output cycles protein kaput (dCLOCK) and similar proteins. dCLOCK, also termed dPAS1, is a bHLH-PAS Circadian regulator that acts as a transcription factor and generates a rhythmic output with a period of about 24 hours
DEEDEKDTIKRKSRNLSEKKRRDQFNVLINELCSMVSTSNRKMDKSTVLKSTIAFLKNHNEVTMQSHQQE
IQEDWKPSFL
>gnl|CDD|381579 cd19736, bHLH-PAS_PASD1, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in circadian clock protein PASD1. PASD1, also termed PAS domain-containing protein 1, is evolutionarily related to Circadian locomotor output cycles protein kaput (CLOCK)and functions as a suppressor of the biological clock that drives the daily circadian rhythms of cells throughout the body. Mammalian PASD1 doesn't harbor the bHLH-PAS domain and is not included in this family
MDEDEKDRAKRASRNKSEKKRRDQFNVLIKELCTMLQGHGHPLKMDKSTILQRTIDFLQKQKEITAQTEA
>gnl|CDD|381580 cd19737, bHLH-PAS_NPAS2_PASD4, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in neuronal PAS domain-containing protein 2 (NPAS2) and similar proteins. NPAS2, also termed neuronal PAS2, or basic-helix-loop-helix-PAS protein MOP4, or Class E basic helix-loop-helix protein 9 (bHLHe9), or member of PAS protein 4, or PAS domain-containing protein 4 (PASD4), is a bHLH-PAS transcriptional activator which forms a core component of the circadian clock
MDEDEKDRAKRASRNKSEKKRRDQFNVLIKELSSMLPGNTRKMDKTTVLEKVIGFLQKHNEVSAQTEICD
IQQDWKP
>gnl|CDD|381581 cd19738, bHLH-PAS_SIM1, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in single-minded homolog 1 (SIM1) and similar proteins. SIM1, also termed Class E basic helix-loop-helix protein 14 (bHLHe14), is a bHLH-PAS transcription factor that may have pleiotropic effects during embryogenesis and in the adult
MKEKSKNAARTRREKENSEFYELAKLLPLPSAITSQLDKASIIRLTTSYLKMRVVFPEGLGEAWGHSSRT
S
>gnl|CDD|381582 cd19739, bHLH-PAS_SIM2, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in single-minded homolog 2 (SIM2) and similar proteins. SIM2, also termed Class E basic helix-loop-helix protein 15 (bHLHe15), is a bHLH-PAS transcription factor that may be a master gene of central nervous system (CNS) development in cooperation with ARNT. It may have pleiotropic effects in the tissues expressed during development
MKEKSKNAAKTRREKENGEFYELAKLLPLPSAITSQLDKASIIRLTTSYLKMRAVFPEGLGDAWGQPSRI
GPLD
>gnl|CDD|381583 cd19740, bHLH-PAS_dSIM_like, basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein single-minded (SIM) and similar proteins. SIM is a nuclear bHLH-PAS transcription factor that functions as a master developmental regulator controlling midline development of the ventral nerve cord in Drosophila
MKEKSKNAARSRREKENAEFLELAKLLPLPAAITSQLDKASIIRLTTSYLKMRQVFPDGLGD
>gnl|CDD|381584 cd19741, bHLH-O_ESMB_like, basic helix-loop-helix-orange (bHLH-O) domain found in Drosophila melanogaster enhancer of split mbeta protein (ESMB) and similar proteins. ESMB, also termed E(spl)mbeta, or HLH-mbeta, or split locus enhancer protein mA, is a bHLH-O transcriptional repressor of genes that require a bHLH protein for their transcription. It is involved in the neural-epidermal lineage decision during early neurogenesis. The family also includes Enhancer of split m7 protein (also known as E(spl)m7), which acts as a transcriptional repressor that participates in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo
MSKTYQYRKVTKPLLERKRRARINKCLDELKDLMVEALATEAENVSKLEKADILELTVRHLKKLRRQKS
>gnl|CDD|381585 cd19742, bHLH_TS_ASCL1_Mash1, basic helix-loop-helix (bHLH) domain found in achaete-scute-like protein 1 (ASCL-1) and similar proteins. ASCL-1, also termed Class A basic helix-loop-helix protein 46 (bHLHa46), or achaete-scute homolog 1 (ASH-1), or mammalian achaete scute homolog 1 (Mash1), is a neural-specific bHLH transcription factor that is expressed in subsets of neural progenitors in both the central and peripheral nervous system. It plays a key role in neuronal differentiation and specification in the nervous system
QQPAAVARRNERERNRVKLVNMGFATLREHVPNGAANKKMSKVETLRSAVEYIRALQQLLDEHDAVSAAF
Q
>gnl|CDD|381586 cd19743, bHLH_TS_ASCL2_Mash2, basic helix-loop-helix (bHLH) domain found in achaete-scute-like protein 2 (ASCL-2) and similar proteins. ASCL-2, also termed achaete-scute homolog 2 (ASH-2), or Class A basic helix-loop-helix protein 45 (bHLHa45), or mammalian achaete scute homolog 2 (Mash2), is a bHLH transcription factor that is involved in Schwann cell differentiation and control of proliferation in adult peripheral nerves
AAAVERRNERERNRVKLVNLGFAALRQHVPQGGASKKMSKVETLRSAVEYIRALQRLLGEHDAE
>gnl|CDD|381587 cd19744, bHLH_TS_dAS-C_like, basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster achaete-scute complex (AS-C) proteins and similar proteins. Drosophila melanogaster AS-C proteins includes lethal of scute (also known as achaete-scute complex protein T3 or AST3), scute (also known as achaete-scute complex protein T4 or AST4), achaete (also known as achaete-scute complex protein T5 or AST5), and asense (also known as achaete-scute complex protein T8 or AST8). They are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system, as well as in sex determination and dosage compensation
SVARRNARERNRVKQVNNGFAILRQHIPQSVIEDLTAGGGRGKSKKLSKVDTLRMAVEYIRRLQKLL
>gnl|CDD|381588 cd19745, bHLH_TS_ASCL3, basic helix-loop-helix (bHLH) domain found in achaete-scute-like protein 3 (ASCL-3) and similar proteins. ASCL-3, also termed Class A basic helix-loop-helix protein 42 (bHLHa42), or bHLH transcriptional regulator Sgn-1, or achaete-scute homolog 3 (ASH-3), is a bHLH transcription factor specifically localized in the duct cells of the salivary glands. It may act as transcriptional repressor that inhibits myogenesis
GPAFIRKRNERERQRVKCVNEGYAKLRRHLPQEYSEKRLSKVETLRAAIKYIKHLQSVL
>gnl|CDD|381589 cd19746, bHLH_TS_ASCL4, basic helix-loop-helix (bHLH) domain found in achaete-scute-like protein 4 (ASCL-4) and similar proteins. ASCL-4, also termed Class A basic helix-loop-helix protein 44 (bHLHa44), or achaete-scute homolog 4 (ASH-4), or Hash4, is a bHLH transcriptional regulator that may be involved in skin development
DYSFEPAFIRKRNERERQRVRCVNEGYARLREHLPQELADKRLSKVETLRAAIDYIKHLQELLE
>gnl|CDD|381590 cd19747, bHLH_TS_ASCL5, basic helix-loop-helix (bHLH) domain found in achaete-scute-like protein 5 (ASCL-5) and similar proteins. ASCL-5, also termed Class A basic helix-loop-helix protein 47 (bHLHa47), or achaete-scute homolog 5 (ASH-5), is an uncharacterized bHLH transcription factor that belongs to AS-C (achaete, scute, lethal of scute, and asense) family
PFEPAFIQKRNERERQRVKCVNEGYARLRDHLPGAMAEKRLSKVETLRAAIRYIKYLQDLL
>gnl|CDD|381591 cd19748, bHLH-O_HEY1, basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with YRPW motif protein 1 (HEY1) and similar proteins. HEY1, also termed cardiovascular helix-loop-helix factor 2 (CHF-2), or Class B basic helix-loop-helix protein 31 (bHLHb31), or HES-related repressor protein 1, or hairy and enhancer of split-related protein 1 (HESR-1), or hairy-related transcription factor 1 (HRT-1), is a bHLH-O transcriptional repressor that acts as an essential downstream effector of the Notch signaling pathway and may play a fundamental role in vascular development. HEY1 also participates several cancer-related pathways. It acts as a positive regulator of the tumor suppressor p53
STSSQVLARKRRRGIIEKRRRDRINNSLSELRRLVPSAFEKQGSAKLEKAEILQMTVDHLKMLHAAGGKG
Y
>gnl|CDD|381592 cd19749, bHLH-O_DEC1, basic helix-loop-helix-orange (bHLH-O) domain found in differentially expressed in chondrocytes protein 1 (DEC1) and similar proteins. DEC1, also termed Class E basic helix-loop-helix protein 40 (bHLHe40), or Class B basic helix-loop-helix protein 2 (bHLHb2), or enhancer-of-split and hairy-related protein 2 (SHARP-2), or stimulated by retinoic acid gene 13 protein (STRA13), is a bHLH-O transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes
RRGLKRSEDSKDTYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTS
LIEQQQQKILALQSGLQIGE
>gnl|CDD|381593 cd19750, bHLH-O_DEC2, basic helix-loop-helix-orange (bHLH-O) domain found in differentially expressed in chondrocytes protein 2 (DEC2) and similar proteins. DEC2, also termed Class E basic helix-loop-helix protein 41 (bHLHe41), or Class B basic helix-loop-helix protein 3 (bHLHb3), or enhancer-of-split and hairy-related protein 1 (SHARP-1), is a bHLH-O transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes
KPKRGLKRDESKEAYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHLKALT
ALTEQQHQKIIALQNGERSLKS
>gnl|CDD|410992 cd19751, 5TM_YidC_Oxa1_Alb3, Five transmembrane core domain of YidC/Oxa1/Alb3 protein family of insertases. The YidC/Oxa1/Alb3 protein family of insertases facilitate the insertion, folding and assembly of proteins of the inner membranes of bacteria and mitochondria, and the thylakoid membrane of plastids. Members include bacterial YidC, mitochondrial Cox18 and Oxa1, and chloroplastic Alb3 and Alb4. Membrane protein insertase YidC, also called foldase YidC or membrane integrase YidC, facilitates proper folding, insertion, and assembly of inner membrane proteins and complexes. Oxa1 and Cox18/Oxa2 mediate the insertion of both mitochondrion-encoded precursors and nuclear-encoded proteins from the matrix into the mitochondrial inner membrane. Alb3 and Alb3-like proteins, including Alb4, are required for the post-translational insertion of the light-harvesting chlorophyll-binding proteins (LHCPs) into the chloroplast thylakoid membrane. YidC/Oxa1/Alb3 family insertases contain a core domain of five transmembrane (5TM) segments that is essential to insertase function
GLSIIIVTILIRLALLPLTLKQQKSMRKMQVIRPEMEAIREKYKEKASKDKVQQEMQKEMLGLYKKHGVN
PMAGCLPLFIQLPIFMAFYFAIMRTEEIRYHTFLWFFDLGQPDYLYILPFVAGITTYFQFKMTMSHQQQM
QMMQMQMKVMLYVMPVMIIIAGLSFPSALSLYWIISNLFMIIQTYFIVR
>gnl|CDD|381391 cd19752, AKR_unchar, uncharacterized aldo-keto reductase (AKR) superfamily protein. This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications
SELCLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAFWTEGGVGGESERLIGRWLKDRGNRDDVV
IATKVGAGPRDPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKA
GKVRAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHSYLRPRPGADFGVQRIVTDELLDYASSRPDLT
LLAYSPLLSGAYTRPDRPLPEQYDGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTV
EQLEENLAALD
>gnl|CDD|381293 cd19753, Mb-like_oxidoreductase, Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain. This subfamily is composed of uncharacterized proteins containing an N-terminal myoglobin-like (M family globin) domain and a C-terminal oxygenase reductase FAD/NADH binding domain belonging to the ferredoxin reductase (FNR) family and is usually part of multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. The domain architecture of this subfamily is similar to flavohemoglobins, which function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses
LRASLAAVEDGPDELARRFYARLFAEAPELRDLFPADMDAQRDRLARALTHVVENLDDPDGLVPFLAQLG
RDHRKYGVAPEHYPAVGAALLAALRHFAGEAWTPELEAAWAEAYTLIAGVM
>gnl|CDD|381294 cd19754, FHb_fungal-globin, Globin domain of fungal flavohemoglobin. FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses. FlavoHb expression affects Aspergillus nidulans sexual development and mycotoxin production, and Dictyostelium discoideum development
LTPAQIKIIKDSVPILESLGVKLTEKFYKYMLKRYPEVKPYFNETNQKLLRQPKILAFALLQYAKNIDDL
TPLSGFVEQIVSKHVGLQVKPEHYPIVGECLIETMKELLPEAVATDEFIEAWTTAYGNLANILIDAEKKE
Y
>gnl|CDD|381295 cd19755, TrHb2_AtGlb3-like_O, nonsymbiotic haemoglobin Ahb3 (GLB3) and similar truncated hemoglobins, group 2 (O). The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). This subfamily includes the dimeric Arabidopsis thaliana TrHb2 AtGLB3. GLB3 is likely to have a function distinct from other plant globins: it exhibits a low O2 affinity, an unusual concentration-independent binding of O2 and CO, and does not respond to any of the treatments that induce plant 3-on-3 globins
YERLGEEGFISLSTEFYNRVYADEEPWFRDIFANSPKEEAIQNQYEFFVQRFGGPPLYSERKGHPALIGR
HAPFPVTPQAAERWLYHMENALDAVEEIDADSRERLLNYFRHTAFFLVV
>gnl|CDD|380814 cd19756, Bbox2, B-box-type 2 zinc finger (Bbox2). The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interaction. Based on different consensus sequence and the spacing of the 7-8 zinc-binding residues, B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). The family corresponds to type 2 B-box (Bbox2)
LCPEHPEEPLKLFCETCQELVCVLCLLSGEHRGHKVVPL
>gnl|CDD|380815 cd19757, Bbox1, B-box-type 1 zinc finger (Bbox1). The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain, in functionally unrelated proteins, most likely mediating protein-protein interactions. Based on different consensus sequences and the spacing of the 7-8 zinc-binding residues, the B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). This family corresponds to the type 1 B-box (Bbox1)
LCDECEEREATVYCLECEEFLCDDCSDAIHRRGKLTRSHKLVPL
>gnl|CDD|380816 cd19758, Bbox2_MID, B-box-type 2 zinc finger found in midline (MID) family. The MID family includes MID1 and MID2. MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is highly related to MID1. It associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. They also play a central role in the regulation of granule exocytosis, and functional redundancy exists between MID1 and MID2 in cytotoxic lymphocytes (CTL). Both MID1 and MID2 belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
LMCSEHEEEKVNMYCLTDDQLICSLCKLVGKHKDHEVAAL
>gnl|CDD|380817 cd19759, Bbox2_TRIM2-like, B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM2, TRIM3, and similar proteins. TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It also plays an important role in the central nervous system (CNS). In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. Both TRIM2 and TRIM3 belong to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
PLVCPNHDGETLEFYCESCETAVCRECTAGEHNEHRTVLLKD
>gnl|CDD|380818 cd19760, Bbox2_TRIM4-like, B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM4, TRIM17, TRIM41, TRIM52 and similar proteins. This family includes a group of tripartite motif-containing proteins, including TRIM4, TRIM17, TRIM41 and TRIM52. TRIM4, also known as RING finger protein 87 (RNF87), is a cytoplasmic E3 ubiquitin-protein ligase that recently evolved and is present only in higher mammals. It transiently interacts with mitochondria, induces mitochondrial aggregation and sensitizes the cells to hydrogen peroxide (H2O2) induced death. Its interaction with peroxiredoxin 1 (PRX1) is critical for the regulation of H2O2 induced cell death. Moreover, TRIM4 functions as a positive regulator of RIG-I-mediated type I interferon induction. It regulates the K63-linked ubiquitination of RIG-1 and assembly of antiviral signaling complex at mitochondria. TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (Terf), is a crucial E3 ubiquitin ligase that is necessary and sufficient for neuronal apoptosis and contributes to Mcl-1 ubiquitination in cerebellar granule neurons (CGNs). It interacts in a SUMO-dependent manner with nuclear factor of activated T cell NFATc3 transcription factor, and thus inhibits the activity of NFATc3 by preventing its nuclear localization. In contrast, it binds to and inhibits NFATc4 transcription factor in a SUMO-independent manner. Moreover, TRIM17 stimulates degradation of kinetochore protein ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for mitotic spindle checkpoint, and negatively regulates cell proliferation. TRIM41, also known as RING finger-interacting protein with C kinase (RINCK), is an E3 ubiquitin-protein ligase that promotes the ubiquitination of protein kinase C (PKC) isozymes in cells. It specifically recognizes the C1 domain of PKC isozymes. It controls the amplitude of PKC signaling by controlling the amount of PKC in the cell. TRIM52, also known as RING finger protein 102 (RNF102), is encoded by a novel, noncanonical antiviral TRIM52 gene in primate genomes with unique specificity determined by the rapidly evolving RING domain. TRIM4, TRIM17 and TRIM41 belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of TRIM family that contains only RBCC domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
GLCEKHQEPLKLFCEEDEALICVICRESRAHRAHTVVPI
>gnl|CDD|380819 cd19761, Bbox2_TRIM5-like, B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM5, TRIM6, TRIM22, TRIM34, TRIM38 and similar proteins. The family includes TRIM5, TRIM6, TRIM22, TRIM34, and TRIM38, all of which belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM5, also termed RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also termed RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also termed 50 kDa-stimulated trans-acting factor (Staf-50), or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also termed interferon-responsive finger protein 1, or RING finger protein 21 (RNF21), may function as an antiviral protein that contributes to the defense against retroviral infections. TRIM38, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is an E3 ubiquitin-protein ligase that promotes K63- and K48-linked ubiquitination of cellular proteins and also catalyzes self-ubiquitination. It negatively regulates tumor necrosis factor alpha (TNF-alpha) and interleukin-1beta-triggered nuclear factor-kappaB (NF-kappaB) activation by mediating lysosomal-dependent degradation of transforming growth factor beta (TGFbeta)-activated kinase 1 (TAK1)-binding protein (TAB)2/3, two critical components of the TAK1 kinase complex. It also inhibits TLR3/4-mediated activation of NF-kappaB and interferon regulatory factor 3 (IRF3) by mediating ubiquitin-proteasomal degradation of TNF receptor-associated factor 6 (Traf6) and NAK-associated protein 1 (Nap1), respectively. Moreover, TRIM38 negatively regulates TLR3-mediated interferon beta (IFN-beta) signaling by targeting ubiquitin-proteasomal degradation of TIR domain-containing adaptor inducing IFN-beta (TRIF). It functions as a valid target for autoantibodies in primary Sjogren's Syndrome
DHCEHHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLLE
>gnl|CDD|380820 cd19762, Bbox2_TRIM7-like, B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM7, TRIM27 and similar proteins. The family includes TRIM7 and TRIM27, both of which belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM27, also termed RING finger protein 76 (RNF76), or RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. It also inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. Furthermore, TRIM27 promotes non-canonical polyubiquitination of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. In addition, TRIM27 forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is also a component of an estrogen receptor 1 (ESR1) regulatory complex, and is involved in estrogen receptor-mediated transcription in MCF-7 cells. Meanwhile, TRIM27 interacts with the hinge region of chromosome 3 protein (SMC3), a component of the multimeric cohesin complex that holds sister chromatids together and prevents their premature separation during mitosis
GVCEKHQEPLKLFCKEDKRPICVVCDRSREHRHHTVLPVEEAAQ
>gnl|CDD|380821 cd19763, Bbox2_TRIM8_C-V, B-box-type 2 zinc finger found in tripartite motif-containing protein 8 (TRIM8) and similar proteins. TRIM8, also known as glioblastoma-expressed RING finger protein (GERP) or RING finger protein 27 (RNF27), is a probable E3 ubiquitin-protein ligase that may promote proteasomal degradation of suppressor of cytokine signaling 1 (SOCS1) and further regulate interferon-gamma signaling. It functions as a new p53 modulator that stabilizes p53, impairing its association with MDM2 and inducing the reduction of cell proliferation. TRIM8 deficit dramatically impairs p53 stabilization and activation in response to chemotherapeutic drugs. TRIM8 also modulates tumor necrosis factor-alpha (TNFalpha) and interleukin-1beta (IL-1beta)-triggered nuclear factor-kappaB (NF-kappa B) activation by targeting transforming growth factor beta (TGFbeta) activated kinase 1 (TAK1) for K63-linked polyubiquitination. Moreover, TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. It also interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation of STAT3. TRIM8 belongs to the C-V subclass of nuclear TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The coiled coil domain is required for homodimerization and the region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
AWSCPQHDAYRLYHCEAEQVAVCEYCCYEGTHQGHSICDLE
>gnl|CDD|380822 cd19764, Bbox2_TRIM9-like, B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM9, TRIM67 and similar proteins. This family includes a group of tripartite motif-containing proteins including TRIM9 and TRIM67, both of which belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, consisting of three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM9 (the human ortholog of rat Spring), also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. It plays an important role in the regulation of neuronal functions and participates in neurodegenerative disorders through its ligase activity. TRIM67, also termed TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis
TCSEHPDEALSMYCLSCKVPVCYLCLEDGRHSNHDVQAL
>gnl|CDD|380823 cd19765, Bbox2_TRIM10-like, B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM10, TRIM15, TRIM26, TRIM31 and similar proteins. This family includes TRIM10, TRIM15, TRIM26 and TRIM31. TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM15, also termed RING finger protein 93 (RNF93), or zinc finger protein 178 (ZNF178), or zinc finger protein B7 (ZNFB7), is a focal adhesion protein that regulates focal adhesion disassembly. It localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. TRIM15 can also associate with coronin 1B, cortactin, filamin binding LIM protein1, and vasodilator-stimulated phosphoprotein, which are involved in actin cytoskeleton dynamics. As an additional component of the integrin adhesome, it regulates focal adhesion turnover and cell migration. TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM31 is an E3 ubiquitin-protein ligase that primarily localizes to the cytoplasm, but is also associated with the mitochondria. It can negatively regulate cell proliferation and may be a potential biomarker of gastric cancer as it is overexpressed from the early stage of gastric carcinogenesis. TRIM31 is downregulated in non-small cell lung cancer and serves as a potential tumor suppressor. It interacts with p52 (Shc) and inhibits Src-induced anchorage-independent growth. TRIM10, TRIM15 and TRIM26 belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM31 belongs to the C-V subclass of TRIM family of proteins. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
TLCEEHGEKIHFFCEDDGKFLCVVCRESREHRTHTVSLL
>gnl|CDD|380824 cd19766, Bbox2_TRIM11_C-IV, B-box-type 2 zinc finger found in tripartite motif-containing protein 11 (TRIM11) and similar proteins. TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) through mediating the degradation of CCHS-associated polyalanine-expanded Phox2b. Trim11 modulates the function of neurogenic transcription factor Pax6 through the ubiquitin-proteosome system, and thus plays an essential role for Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM11 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
GLCGKHREPLKLFCKDHEALLCVVCERSREHWGHRVVPAEEAAQ
>gnl|CDD|380825 cd19767, Bbox2_TRIM13_C-XI, B-box-type 2 zinc finger found in tripartite motif-containing protein 13 (TRIM13) and similar proteins. TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane-anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). It also targets the known ER proteolytic substrate CD3-delta, but not the N-end rule substrate Ub-R-YFP (yellow fluorescent protein) for its degradation. Moreover, TRIM13 regulates ubiquitination and degradation of NEMO to suppress tumor necrosis factor (TNF) induced nuclear factor-kappaB (NF- kappa B) activation. It is also involved in NF-kappaB p65 activation and nuclear factor of activated T-cells (NFAT)-dependent activation of c-Rel upon T-cell receptor engagement. Furthermore, TRIM13 negatively regulates lanoma differentiation-associated gene 5 (MDA5)-mediated type I interferon production. It also regulates caspase-8 ubiquitination, translocation to autophagosomes, and activation during ER stress induced cell death. Meanwhile, TRIM13 enhances ionizing radiation-induced apoptosis by increasing p53 stability and decreasing AKT kinase activity through MDM2 and AKT degradation. TRIM13 belongs to the C-XI subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region. In addition, TRIM13 contains a C-terminal transmembrane domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
PVCKVHSGQPLNIFCSTDLKLICGFCATMGDHKKHVFCSIED
>gnl|CDD|380826 cd19768, Bbox2_TRIM14, B-box-type 2 zinc finger found in tripartite motif-containing protein 14 (TRIM14) and similar proteins. TRIM14 is a mitochondrial adaptor that facilitates innate immune signaling. It also plays a critical role in tumor development. TRIM14 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. It contains a Bbox2 zinc finger as well as a C-terminal SPRY/B30.2 domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
RCCPEHKDRPLELFCKTCKRCVCALCPILGQHRGHDVRLIDEEA
>gnl|CDD|380827 cd19769, Bbox2_TRIM16-like, B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, TRIM47 and similar proteins. This family includes a group of tripartite motif-containing proteins, such as TRIM16, TRIM29 and TRIM47. TRIM16, also termed estrogen-responsive B box protein (EBBP), is a regulator that may play a role in the regulation of keratinocyte differentiation. It may also act as a tumor suppressor through affecting cell proliferation and migration or tumorigenicity in carcinogenesis. TRIM29, also termed ataxia telangiectasia group D-associated protein (ATDC), plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. TRIM16 and TRIM29 belong to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. TRIM47 belongs to the C-IV subclass of TRIM family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
RVCPIHKKPLELFCRTDQMCICELCAKEEHRGHDVVTVEEEREKKE
>gnl|CDD|380828 cd19770, Bbox2_TRIM19_C-V, B-box-type 2 zinc finger found in tripartite motif-containing protein 19, also called promyelocytic leukemia protein (PML), and similar proteins. Protein PML, also known as RING finger protein 71 (RNF71) or tripartite motif-containing protein 19 (TRIM19), is predominantly a nuclear protein with a broad intrinsic antiviral activity. It is the eponymous component of PML nuclear bodies (PML NBs) and has been implicated in a wide variety of cell processes, including DNA damage signaling, apoptosis, and transcription. PML interferes with the replication of many unrelated viruses, including human immunodeficiency virus 1 (HIV-1), human foamy virus (HFV), poliovirus, influenza virus, rabies virus, EMCV, adeno-associated virus (AAV), and vesicular stomatitis virus (VSV). It also selectively interacts with misfolded proteins through distinct substrate recognition sites and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. PML belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
PFCPSPNHETQMISIYCRQCSKSVCCTCALLDSSHKGQHCDIKAEIQRRQ
>gnl|CDD|380829 cd19771, Bbox2_TRIM20, B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM20 and similar proteins. TRIM20, also termed Pyrin, or Marenostrin (MEFV), is involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. TRIM20 belongs to unclassified TRIM family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. It contains a pyrin domain, a Bbox2 zinc finger, and a C-terminal SPRY/B30.2 domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
PQCKLHLEQLKLFCEDHREPICLICQLSQEHQGHRVRPI
>gnl|CDD|380830 cd19772, Bbox2_TRIM21_C-IV, B-box-type 2 zinc finger found in tripartite motif-containing protein 21 (TRIM21) and similar proteins. TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren's syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
ERCAVHGERLHLFCEEDQKALCLVCAQSQKHRDHAMVPIE
>gnl|CDD|380831 cd19773, Bbox2_TRIM23_C-IX_rpt1, first B-box-type 2 zinc finger found in tripartite motif-containing protein 23 (TRIM23) and similar proteins. TRIM23, also known as ADP-ribosylation factor domain-containing protein 1, GTP-binding protein ARD-1, or RING finger protein 46 (RNF46), is an E3 ubiquitin-protein ligase belonging to the C-IX subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, two Bbox2, and a coiled coil region, as well as C-terminal ADP ribosylation factor (ARF) domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM23 is involved in nuclear factor (NF)-kappaB activation. It mediates atypical lysine 27 (K27)-linked polyubiquitin conjugation to NF-kappaB essential modulator NEMO, also known as IKKgamma, which plays an important role in the NF-kappaB pathway, and this conjugation is essential for TLR3- and RIG-I/MDA5-mediated antiviral innate and inflammatory responses. It also regulates adipocyte differentiation via stabilization of the adipogenic activator peroxisome proliferator-activated receptor gamma (PPARgamma) through atypical ubiquitin conjugation to PPARgamma. Moreover, TRIM23 interacts with and polyubiquitinates yellow fever virus (YFV) NS5 to promote its binding to STAT2 and trigger type I interferon (IFN-I) signaling inhibition
PSIPCDENEDHEATLYCTVCSTNLCEECFTSTHSTKTLSKHRRVPLSEKP
>gnl|CDD|380832 cd19774, Bbox2_TRIM23_C-IX_rpt2, second B-box-type 2 zinc finger found in tripartite motif-containing protein 23 (TRIM23) and similar proteins. TRIM23, also known as ADP-ribosylation factor domain-containing protein 1, GTP-binding protein ARD-1, or RING finger protein 46 (RNF46), is an E3 ubiquitin-protein ligase belonging to the C-IX subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, two Bbox2, and a coiled coil region, as well as C-terminal ADP ribosylation factor (ARF) domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM23 is involved in nuclear factor (NF)-kappaB activation. It mediates atypical lysine 27 (K27)-linked polyubiquitin conjugation to NF-kappaB essential modulator NEMO, also known as IKKgamma, which plays an important role in the NF-kappaB pathway, and this conjugation is essential for TLR3- and RIG-I/MDA5-mediated antiviral innate and inflammatory responses. It also regulates adipocyte differentiation via stabilization of the adipogenic activator peroxisome proliferator-activated receptor gamma (PPARgamma) through atypical ubiquitin conjugation to PPARgamma. Moreover, TRIM23 interacts with and polyubiquitinates yellow fever virus (YFV) NS5 to promote its binding to STAT2 and trigger type I interferon (IFN-I) signaling inhibition
EKPKCPIHPDHLIEFVCLEEDCQESPLMCIICKEYGKHQGHKHELLEEEA
>gnl|CDD|380833 cd19775, Bbox2_TIF1_C-VI, B-box-type 2 zinc finger found in transcription intermediary factor 1 (TIF1) family. This family corresponds to the TIF1 family of transcriptional cofactors including TIF1-alpha (TRIM24), TIF1-beta (TRIM28), and TIF1-gamma (TRIM33), which belong to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1alpha and TIF1beta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. They bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. TIF1gamma is structurally closely related to TIF1alpha and TIF1beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatinic proteins HP1alpha, beta and gamma. It cannot bind to nuclear receptors (NRs)
PLFCPVHPQEPLKLFCETCDKLTCRDCQLLEHKDHKYQFAEEA
>gnl|CDD|380834 cd19776, Bbox2_TRIM25_C-IV, B-box-type 2 zinc finger found in tripartite motif-containing protein 25 (TRIM25) and similar proteins. TRIM25, also termed estrogen-responsive finger protein (EFP), or ubiquitin/ISG15-conjugating enzyme TRIM25, or zinc finger protein 147 (ZNF147), or E3 ubiquitin/ISG15 ligase TRIM25, is induced by estrogen and particularly abundant in placenta and uterus. It has been implicated in cell proliferation, protein modification, and the retinoic acid inducible gene I (RIG-I)-mediated antiviral signaling pathway. It functions as an E3-ubiquitin ligase able to transfer ubiquitin and ISG15 to target proteins. It binds to mono-ubiquitinated PCNA and promotes the ISG15 modification (ISGylation) of PCNA, suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. It suppresses p53's transcriptional activity and dampens the response to DNA damage. Upon deubiquitylation by ubiquitin-specific peptidase 15 (USP15), it mediates K63-linked polyubiquitination of RIG-I that is crucial for downstream antiviral interferon signaling. TRIM25 is required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF- kappa B) and interferon production. It is an RNA binding protein acting as RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
RKCTQHGKLLEFYCKSHSLCICSTCLVKEHKRCELVDI
>gnl|CDD|380835 cd19777, Bbox2_TRIM35_C-IV, B-box-type 2 zinc finger found in tripartite motif-containing protein 35 (TRIM35) and similar proteins. TRIM35, also known as hemopoietic lineage switch protein 5 (HLS5), is a putative hepatocellular carcinoma (HCC) suppressor that inhibits phosphorylation of pyruvate kinase isoform M2 (PKM2), which is involved in aerobic glycolysis of cancer cells and further suppresses the Warburg effect and tumorigenicity in HCC. It also negatively regulates Toll-like receptor 7 (TLR7)- and TLR9-mediated type I interferon production by suppressing the stability of interferon regulatory factor 7 (IRF7). Moreover, TRIM35 regulates erythroid differentiation by modulating globin transcription factor 1 (GATA-1) activity. TRIM35 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
NDPALCRLHGETLKLFCLDDKELLCCACQSSKQHQGHRVYPVKE
>gnl|CDD|380836 cd19778, Bbox2_TRIM36_C-I, B-box-type 2 zinc finger found in tripartite motif-containing protein 36 (TRIM36) and similar proteins. TRIM36, human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequently dorsal axis formation. It is also potentially associated with chromosome segregation through interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM36 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
LMCPEHEMEKVNMYCEACRRPVCHLCKLGGSHANHRVTSMSSAYK
>gnl|CDD|380837 cd19779, Bbox2_TRIM37_C-VIII, B-box-type 2 zinc finger found in tripartite motif-containing protein 37 (TRIM37) and similar proteins. TRIM37, also known as Mulibrey nanism protein, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
DKCETHNEKLSVYCWTCKKCICHQCALWGGTHSGHTFKPL
>gnl|CDD|380838 cd19780, Bbox2_TRIM39-like, B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM39, TRIM58 and similar proteins. The family includes TRIM39 and TRIM58, both of which belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM39, also termed RING finger protein 23 (RNF23), or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability and modulates cell cycle progression and DNA damage responses via stabilization of p21. TRIM39 also negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcription, which is induced by inflammatory stimulants such as tumor necrosis factor alpha (TNFalpha). TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM58, also known as protein BIA2, is an erythroid E3 ubiquitin-protein ligase induced during late erythropoiesis. It binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. It may participate in the erythroblast enucleation process through regulation of nuclear polarization
EESLCARHREALSLFCEEDQEAVCLVCEISHDHRAHTLVPLQDA
>gnl|CDD|380839 cd19781, Bbox2_TRIM40_C-V, B-box-type 2 zinc finger found in tripartite motif-containing protein 40 (TRIM40) and similar proteins. TRIM40, also termed probable E3 NEDD8-protein ligase, or RING finger protein 35, may function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway. It promotes neddylation of IKBKG/NEMO, stabilizing NFKBIA, and inhibiting NF-kappaB nuclear translocation and activity. TRIM40 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
AGYLCQLHEKKVEWFCEEDQVLLCEECLKSPEHQSHHVLTIEDA
>gnl|CDD|380840 cd19782, Bbox2_TRIM42_C-III, B-box-type 2 zinc finger found in tripartite motif-containing protein 42 (TRIM42) and similar proteins. TRIM42 belongs to the C-III subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil domain. It also has a novel cysteine-rich motif N-terminal to the RBCC domain, as well as a COS (carboxyl-terminal subgroup one signature) box and a fibronectin type-III (FN3) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM42 can interact with TRIM27, a known cancer-associated protein. Its precise biological function remains unclear
EKNCLIHPNNKLTEYCLDDNELLCEFCKNSQHNGHDTVSL
>gnl|CDD|380841 cd19783, Bbox2_TRIM43-like, B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, TRIM51, TRIM64, TRIM77 and similar proteins. The family includes a group of closely related uncharacterized tripartite motif-containing proteins, TRIM43, TRIM43B, TRIM48/RNF101, TRIM49/RNF18, TRIM49B, TRIM49C/TRIM49L2, TRIM49D/TRIM49L, TRIM51/SPRYD5, TRIM64, TRIM64B, TRIM64C, and TRIM77, whose biological functions remain unclear. TRIM49, also known as testis-specific RING-finger protein, has moderate similarity with SS-A/Ro52 antigen, suggesting it may be one of target proteins of autoantibodies in the sera of patients with these autoimmune disorders. All family members (except for TRIM51) belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM51 belongs to unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
SSEEQICGTHRETKKLFCEADKSLLCLLCSSSQEHRAHRHYPIEWAAEEHREK
>gnl|CDD|380842 cd19784, Bbox2_TRIM44, B-box-type 2 zinc finger found in tripartite motif-containing protein 44 (TRIM44) and similar proteins. TRIM44, also termed protein DIPB, functions as a critical regulator in tumor metastasis and progression. TRIM44 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. It contains a Bbox2 domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
KKCPEHGQELSLYCKEDEKIICVLCAVIGAHRQHQLITL
>gnl|CDD|380843 cd19785, Bbox2_TRIM45_C-X, B-box-type 2 zinc finger found in tripartite motif-containing protein 45 (TRIM45) and similar proteins. TRIM45, also known as RING finger protein 99 (RNF99), is a novel receptor for activated C-kinase (RACK1)-interacting protein that suppresses transcriptional activities of Elk-1 and AP-1 and downregulates mitogen-activated protein kinase (MAPK) signal transduction by inhibiting RACK1/PKC (protein kinase C) complex formation. It also negatively regulates tumor necrosis factor alpha (TNFalpha)-induced nuclear factor-kappaB (NF-kappa B)-mediated transcription and suppresses cell proliferation. TRIM45 belongs to the C-X subclass of TRIM (tripartite motif) family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a filamin-type immunoglobulin (IG-FLMN) domain and NHL repeats positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
PVLCPFHPAEELRLFCETCDKPVCRDCVLVEHRGHQCDFTSDV
>gnl|CDD|380844 cd19786, Bbox2_TRIM46_C-I, B-box-type 2 zinc finger found in tripartite motif-containing protein 46 (TRIM46) and similar proteins. TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that specifically localizes to the proximal axon, partly overlaps with the axon initial segment (AIS) at later stages, and organizes uniform microtubule orientation in axons. It controls neuronal polarity and axon specification by driving the formation of parallel microtubule arrays. TRIM46 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins, which are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
KGLMCPEHKEEVTHYCKTCQRLVCQLCRVRRTHAGHKITPVLSAYQ
>gnl|CDD|380845 cd19787, Bbox2_TRIM50-like, B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 and similar proteins. TRIM50 is a stomach-specific E3 ubiquitin-protein ligase, encoded by the Williams-Beuren syndrome (WBS) TRIM50 gene, which regulates vesicular trafficking for acid secretion in gastric parietal cells. It colocalizes, interacts with, and increases the level of p62/SQSTM1, a multifunctional adaptor protein implicated in various cellular processes including the autophagy clearance of polyubiquitinated protein aggregates. It also promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through the interaction with the histone deacetylase 6 (HDAC6), a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. TRIM50 can be acetylated by PCAF and p300. TRIM50 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. The family also includes two paralogs of TRIM50, tripartite motif-containing protein 73 (TRIM73), also known as tripartite motif-containing protein 50B (TRIM50B), and tripartite motif-containing protein 74 (TRIM74), also known as tripartite motif-containing protein 50C (TRIM50C), both of which are WBS-related genes encoding proteins and may also act as E3 ligases. In contrast with TRIM50, TRIM73 and TRIM74 belong to the C-V subclass of TRIM family of proteins that are defined by the N-terminal RBCC domains only
ESCPHHHNPLSLFCEKDQEVICGLCGLIGSHRQHKITPV
>gnl|CDD|380846 cd19788, Bbox2_MuRF, B-box-type 2 zinc finger found in muscle-specific RING finger protein (MuRF) family. This family corresponds to a group of striated muscle-specific tripartite motif (TRIM) proteins, including TRIM63/MuRF-1, TRIM55/MuRF-2, and TRIM54/MuRF-3, which function as E3 ubiquitin ligases in ubiquitin-mediated muscle protein turnover. They are tightly developmentally regulated in skeletal muscle and associate with different cytoskeleton components, such as microtubules, Z-disks and M-bands, as well as with metabolic enzymes and nuclear proteins. They also cooperate with diverse proteins implicated in selective protein degradation by the proteasome and autophagosome, and target proteins of metabolic regulation, sarcomere assembly and transcriptional regulation. Moreover, MURFs display variable fibre-type preferences. TRIM63/MuRF-1 is predominantly fast (type II) fibre-associated in skeletal muscle. TRIM55/MuRF-2 is predominantly slow-fibre associated. TRIM54/MuRF-3 is ubiquitously present. They play an active role in microtubule-mediated sarcomere assembly. MuRFs belong to the C-II subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain positioned C-terminal to the RBCC domain. They also harbor a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
MCEEHEEEKINIYCLTCEVPTCSMCKVFGAHKDCEVAPL
>gnl|CDD|380847 cd19789, Bbox2_TRIM56_C-V, B-box-type 2 zinc finger found in tripartite motif-containing protein 56 (TRIM56) and similar proteins. TRIM56, also known as RING finger protein 109 (RNF109), is a virus-inducible E3 ubiquitin ligase that restricts pestivirus infection. It positively regulates the Toll-like receptor 3 (TLR3) antiviral signaling pathway, and possesses antiviral activity against bovine viral diarrhea virus (BVDV), a ruminant pestivirus classified within the family Flaviviridae shared by tick-borne encephalitis virus (TBEV). It also possesses antiviral activity against two classical flaviviruses, yellow fever virus (YFV) and dengue virus (DENV), as well as a human coronavirus, HCoV-OC43, which is responsible for a significant share of common cold cases. It may not act on positive-strand RNA viruses indiscriminately. Moreover, TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses. TRIM56 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
QRIMCREHRDERLLLYCTPCEAAVCRECRLRPHLSLTHRCLPLAEAA
>gnl|CDD|380848 cd19790, Bbox2_TRIM59_C-XI, B-box-type 2 zinc finger found in tripartite motif-containing protein 59 (TRIM59) and similar proteins. TRIM59, also known as TRIM57, or RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis. It is upregulated in gastric cancer and promotes gastric carcinogenesis by interacting with and targeting the P53 tumor suppressor for its ubiquitination and degradation. It also acts as a novel accessory molecule involved in cytotoxicity of BCG-activated macrophages (BAM). Moreover, TRIM59 may serve as a multifunctional regulator for innate immune signaling pathways. It interacts with ECSIT and negatively regulates nuclear factor-kappaB (NF- kappa B) and interferon regulatory factor (IRF)-3/7-mediated signal pathways. TRIM59 belongs to the C-XI subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region. In addition, TRIM59 contains a C-terminal transmembrane domain
PTCPEHYRQPLNLFCLLDRKLICGQCLTVGQHQGHPIDDL
>gnl|CDD|380849 cd19791, Bbox2_TRIM60-like, B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM60, TRIM61, TRIM75 and similar proteins. This family includes a group of tripartite motif-containing proteins, including TRIM60, TRIM61 and TRIM75. TRIM60, also known as RING finger protein 129 (RNF129) or RING finger protein 33 (RNF33), is a cytoplasmic protein expressed in the testis. It may play an important role in the spermatogenesis process, the development of the preimplantation embryo, and in testicular functions. TRIM60 interacts with the cytoplasmic kinesin motor proteins KIF3A and KIF3B suggesting possible contribution to cargo movement along the microtubule in the expressed sites. It is also involved in spermatogenesis in Sertoli cells under the regulation of nuclear factor-kappaB (NF-kappaB). TRIM61 is closely related to TRIM60, but its biological function remains unclear. TRIM75 could be the product of a pseudogene. Its biological function remains unclear. TRIM60 and TRIM75 belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM61 belongs to the C-V subclass of TRIM family that contains RBCC domains only. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
TLCEKHNQPLTKFCKKDLEPLCPQCSQSTDHQHHVVVPL
>gnl|CDD|380850 cd19792, Bbox2_TRIM62_C-IV, B-box-type 2 zinc finger found in tripartite motif-containing protein 62 (TRIM62) and similar proteins. TRIM62, also known as Ductal Epithelium Associated Ring Chromosome 1 (DEAR1), is a cytoplasmic E3 ubiquitin-protein ligase that was identified as a dominant regulator of acinar morphogenesis in the mammary gland. It is implicated in the inflammatory response of immune cells by regulating the Toll-like receptor 4 (TLR4) signaling pathway, leading to increased activity of the activator protein 1 (AP-1) transcription factor in primary macrophages. It is also involved in muscular protein homeostasis, especially during inflammation-induced atrophy, and may play a role in the pathogenesis of ICU-acquired weakness (ICUAW) by activating and maintaining inflammation in myocytes. Moreover, TRIM62 facilitates K27-linked poly-ubiquitination of CARD9 and also regulates CARD9-mediated anti-fungal immunity and intestinal inflammation. Furthermore, TRIM62 is involved in the regulation of apical-basal polarity and acinar morphogenesis. It also functions as a chromosome 1p35 tumor suppressor and negatively regulates transforming growth factor beta (TGFbeta)-driven epithelial-mesenchymal transition (EMT) through binding to and promoting the ubiquitination of SMAD3, a major effector of TGFbeta-mediated EMT. TRIM62 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
FPCKDHDKVKLFCLTDRALVCFFCDEPALHEQHQVTNV
>gnl|CDD|380851 cd19793, Bbox2_TRIM65-like, B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65), B box and SPRY domain-containing protein (BSPRY) and similar proteins. The family includes TRIM65 and BSPRY. TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5 enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. BSPRY is a regulatory protein for maintaining calcium homeostasis. It may regulate epithelial calcium transport by inhibiting TRPV5 activity. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
ELCPEHGRELELYCRTEKRCVCAQCASKGECRGHRVTLLEERA
>gnl|CDD|380852 cd19794, Bbox2_TRIM66-like, B-box-type 2 zinc finger found in tripartite motif-containing protein 66 (TRIM66) and similar proteins. TRIM66, also termed transcriptional intermediary factor 1 delta (TIF1delta), is a novel heterochromatin protein 1 (HP1)-interacting member of the transcriptional intermediary factor 1 (TIF1) family expressed by elongating spermatids. Like other TIF1 proteins, TRIM66 displays a potent trichostatin A (TSA)-sensitive repression function; TSA is a specific inhibitor of histone deacetylases. Moreover, TRIM66 plays an important role in heterochromatin-mediated gene silencing during postmeiotic phases of spermatogenesis. It functions as a negative regulator of postmeiotic genes acting through HP1 isotype gamma (HP1gamma) complex formation and centromere association. TRIM66 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
LMCPLHNQEPLKLFCETCDVLVCRSCLLSEHKEHRFKHLDEAL
>gnl|CDD|380853 cd19795, Bbox2_TRIM68_C-IV, B-box-type 2 zinc finger found in tripartite motif-containing protein 68 (TRIM68) and similar proteins. TRIM68, also known as RING finger protein 137 (RNF137) or SSA protein SS-56 (SS-56), is an E3 ubiquitin-protein ligase that negatively regulates Toll-like receptor (TLR)- and RIG-I-like receptor (RLR)-driven type I interferon production by degrading TRK fused gene (TFG), a novel driver of IFN-beta downstream of anti-viral detection systems. It also functions as a cofactor for androgen receptor-mediated transcription by regulating ligand-dependent transcription of androgen receptor in prostate cancer cells. Moreover, TRIM68 is a cellular target of autoantibody responses in Sjogren's syndrome (SS), as well as systemic lupus erythematosus (SLE). It is also an auto-antigen for T cells in SS and SLE. TRIM68 belongs the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
EDLCERHKEKLNLFCEEDQELLCVVCEQSPEHKAHTVVPVEEAA
>gnl|CDD|380854 cd19796, Bbox2_TRIM71_C-VII, B-box-type 2 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar proteins. TRIM71, also known as protein lineage variant 41 (lin-41), is an E3 ubiquitin-protein ligase that may play essential roles in embryonic stem cells, cellular reprogramming, and the timing of embryonic neurogenesis. It was first identified in the nematode Caenorhabditis elegans as a target of the differentiation-associated microRNA (miRNA) let-7 (lethal 7), and therefore part of a heterochronic gene network that controls larval development. In humans, it regulates let-7 microRNA biogenesis via modulation of Lin28B protein polyubiquitination. TRIM71 localizes to cytoplasmic P-bodies and directly interacts with the miRNA pathway proteins Argonaute 2 (AGO2) and DICER. It represses miRNA activity by promoting degradative ubiquitination of AGO2. Moreover, TRIM71 associates with SHCBP1, a novel component of the fibroblast growth factor (FGF) signaling pathway, and regulates its non-degradative polyubiquitination. It is also involved in the post-transcriptional regulation of the CDKN1A, RBL1 and RBL2 or EGR1 mRNAs through mediating RNA-binding in embryonic stem cells. TRIM71 belongs to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
PSYCEIHEHEVLRLYCDTCSVPICRECTMGEHRGHSFIYLQEAVQDSK
>gnl|CDD|380855 cd19797, Bbox2_TRIM72_C-IV, B-box-type 2 zinc finger found in tripartite motif-containing protein 72 (TRIM72) and similar proteins. TRIM72, also known as Mitsugumin-53 (MG53), is a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at muscle injury sites. It is required in repair of alveolar epithelial cells under plasma membrane stress failure. It interacts with dysferlin to regulate sarcolemmal repair. Upregulation of TRIM72 develops obesity, systemic insulin resistance, dyslipidemia, and hyperglycemia, as well as induces diabetic cardiomyopathy through transcriptional activation of peroxisome proliferation-activated receptor alpha (PPAR-alpha) signaling pathway. Compensation for the absence of AKT signaling by ERK signaling during TRIM72 overexpression leads to pathological hypertrophy. Moreover, TRIM72 functions as a novel negative feedback regulator of myogenesis via targeting insulin receptor substrate-1 (IRS-1). It is transcriptionally activated by the synergism of myogenin (MyoD) and myocyte enhancer factor 2 (MEF2). TRIM72 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
GHCEEHLDPLSVYCEQDRALICGVCASLGKHKGHNIITAAEA
>gnl|CDD|380856 cd19798, Bbox2_BRAT-like, B-box-type 2 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and similar proteins. BRAT is a NHL-domain family protein that functions as a translational repressor to inhibit cell proliferation. This family also contains Caenorhabditis elegans B-box type zinc finger protein ncl-1, a C. elegans Brat homolog which functions as a translational repressor that inhibits protein synthesis. BRAT contains Bbox1 and Bbox2 zinc fingers and NHL repeats. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
EKPVFCPKHPNEVLKFFCKTCNIPICKDCTLLDHNKGLHDYEYL
>gnl|CDD|380857 cd19799, Bbox2_MYCBP2, B-box-type 2 zinc finger found in Myc-binding protein 2 (MYCBP2) and similar proteins. MYCBP2, also termed protein associated with Myc (Pam), is an atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues. MYCBP2 harbors a B-box motif that shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs). The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
PTCDNHDDGETAAIIFCCDCGNYLCAECDRFLHLHRKNRSHQRQVFKEEE
>gnl|CDD|380858 cd19800, Bbox2_xNF7-like, B-box-type 2 zinc finger found in Xenopus laevis nuclear factor 7 (xNF7) and similar proteins. xNF7 is a maternally expressed novel zinc finger nuclear phosphoprotein. It acts as a transcription factor that determines dorsal-ventral body axis. xNF7 harbors a B-box motif that shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs). The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
EVCSEHDEPLKLFCKDDKRLICVICRDSRKHRGHRFLPV
>gnl|CDD|380859 cd19801, Bbox1_MID, B-box-type 1 zinc finger found in the midline (MID) family. The MID family includes MID1 and MID2. MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is highly related to MID1. It associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with alpha4, a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. They also play a central role in the regulation of granule exocytosis, and functional redundancy exists between MID1 and MID2 in cytotoxic lymphocytes (CTL). Both MID1 and MID2 belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
LVPCDVCEKEPPRKAVKTCLTCEVSYCKRCLEATHPNRGPFATHRLVEP
>gnl|CDD|380860 cd19802, Bbox1_TRIM8-like, B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM8, TRIM16, TRIM25, TRIM29, TRIM44, TRIM47 and similar proteins. This family includes a group of tripartite motif-containing proteins, including TRIM8, TRIM16, TRIM25, TRIM29, TRIM44 and TRIM47. TRIM8, also known as glioblastoma-expressed RING finger protein (GERP) or RING finger protein 27 (RNF27), is a probable E3 ubiquitin-protein ligase that may promote proteasomal degradation of suppressor of cytokine signaling 1 (SOCS1) and further regulate interferon-gamma signaling. It functions as a new p53 modulator that stabilizes p53, impairing its association with MDM2 and inducing the reduction of cell proliferation. TRIM16, also termed estrogen-responsive B box protein (EBBP), may play a role in the regulation of keratinocyte differentiation. It may also act as a tumor suppressor by affecting cell proliferation and migration or tumorigenicity in carcinogenesis. TRIM25, also termed estrogen-responsive finger protein (EFP), or ubiquitin/ISG15-conjugating enzyme TRIM25, or zinc finger protein 147 (ZNF147), or E3 ubiquitin/ISG15 ligase TRIM25, is induced by estrogen and is particularly abundant in placenta and uterus. It has been implicated in cell proliferation, protein modification, and the retinoic acid inducible gene I (RIG-I)-mediated antiviral signaling pathway. It functions as an E3-ubiquitin ligase able to transfer ubiquitin and ISG15 to target proteins. TRIM29, also termed ataxia telangiectasia group D-associated protein (ATDC), plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. TRIM44, also termed protein DIPB, functions as a critical regulator in tumor metastasis and progression. TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. The TRIM (tripartite motif) family of proteins are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
LCDFCDPGKALKAVKSCLTCEASLCEIHLRPHLESPALKSHQLVEP
>gnl|CDD|380861 cd19803, Bbox1_TRIM9-like_C-I, B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM9, TRIM67 and similar proteins. This family includes a group of tripartite motif-containing proteins, including TRIM9 and TRIM67, both of which belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, consisting of three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TRIM9 (the human ortholog of rat Spring), also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. It plays an important role in the regulation of neuronal functions and participates in the neurodegenerative disorders through its ligase activity. TRIM67, also termed TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis
RCQLCEKSPPKEASVFCEQCEVFYCDSCRESCHPPRGPLAKHTLVSP
>gnl|CDD|380862 cd19804, Bbox1_TRIM19_C-V, B-box-type 1 zinc finger found in promyelocytic leukemia protein (PML) and similar proteins. Protein PML, also known as RING finger protein 71 (RNF71) or tripartite motif-containing protein 19 (TRIM19), is predominantly a nuclear protein with a broad intrinsic antiviral activity. It is the eponymous component of PML nuclear bodies (PML NBs) and has been implicated in a wide variety of cellular processes, including DNA damage signaling, apoptosis, and transcription. PML interferes with the replication of many unrelated viruses, including human immunodeficiency virus 1 (HIV-1), human foamy virus (HFV), poliovirus, influenza virus, rabies virus, EMCV, adeno-associated virus (AAV), and vesicular stomatitis virus (VSV). It also selectively interacts with misfolded proteins through distinct substrate recognition sites, and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. PML belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
ELMCNRCSESEAEFWCSECEEFLCRKCFEAHQRFKKRKKHEALRLAE
>gnl|CDD|380863 cd19805, Bbox1_TIF1, B-box-type 1 zinc finger found in transcription intermediary factor 1 (TIF1) family. This family corresponds to the TIF1 family of transcriptional cofactors including TIF1-alpha (TRIM24), TIF1-beta (TRIM28), and TIF1-gamma (TRIM33), which belongs to the C-VI subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1-alpha and TIF1-beta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. They bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. TIF1-gamma is structurally closely related to TIF1-alpha and TIF1-beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatinic proteins HP1alpha, beta and gamma. It cannot bind to nuclear receptors (NRs)
VCTSCEDNAPATSFCVECSEWLCDTCVQAHQRVKVTKDHTIRSK
>gnl|CDD|380864 cd19806, Bbox1_TRIM32_C-VII, B-box-type 1 zinc finger found in tripartite motif-containing protein 32 (TRIM32) and similar proteins. TRIM32, also known as 72 kDa Tat-interacting protein, or zinc finger protein HT2A, or BBS11, is an E3 ubiquitin-protein ligase that promotes degradation of several targets, including actin, PIASgamma, Abl interactor 2, dysbindin, X-linked inhibitor of apoptosis (XIAP), p73 transcription factor, thin filaments and Z-bands during fasting. It plays important roles in neuronal differentiation of neural progenitor cells, as well as in controlling cell fate in skeletal muscle progenitor cells. It reduces PI3K-Akt-FoxO signaling in muscle atrophy by promoting plakoglobin-PI3K dissociation. It also functions as a pluripotency-reprogramming roadblock that facilitates cellular transition towards differentiation via modulating the levels of Oct4 and cMyc. Moreover, TRIM32 is an intrinsic influenza A virus (IAV) restriction factor which senses and targets the polymerase basic protein 1 (PB1) for ubiquitination and protein degradation. It also plays a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo, binding specifically to the activation domain of HIV-1 Tat; it and can also interact with the HIV-2 and EIAV Tat proteins. Furthermore, TRIM32 regulates myoblast proliferation by controlling turnover of NDRG2 (N-myc downstream-regulated gene). It negatively regulates tumor suppressor p53 to promote tumorigenesis. It also facilitates degradation of MYCN on spindle poles and induces asymmetric cell division in human neuroblastoma cells. In addition, TRIM32 plays important roles in regulation of hyperactivities and positively regulates the development of anxiety and depression disorders induced by chronic stress. It also plays a role in regeneration by affecting satellite cell cycle progression via modulation of the SUMO ligase PIASy (PIAS4). Defects in TRIM32 leads to limb-girdle muscular dystrophy type 2H (LGMD2H), sarcotubular myopathies (STM) and Bardet-Biedl syndrome. TRIM32 belongs to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The NHL domain mediates the interaction with Argonaute proteins and consequently allows TRIM32 to modulate the activity of certain miRNAs. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
LMCKSCKRRLPRHFCKSCALVLCDPCKEEGHQLPGHTVLAI
>gnl|CDD|380865 cd19807, Bbox1_TRIM36-like, B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM36, TRIM46 and similar proteins. The family includes tripartite motif-containing proteins, TRIM36 and TRIM46, both of which belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TRIM36, the human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequent dorsal axis formation. It is also potentially associated with chromosome segregation by interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that specifically localizes to the proximal axon, partly overlaps with the axon initial segment (AIS) at later stages, and organizes uniform microtubule orientation in axons. It controls neuronal polarity and axon specification by driving the formation of parallel microtubule arrays
AIKCQLCKPPPQEATKSCADCVASFCNECFKVVHPWGTPKAQHEYVGPTNNF
>gnl|CDD|380866 cd19808, Bbox1_TRIM42_C-III, B-box-type 1 zinc finger found in tripartite motif-containing protein 42 (TRIM42) and similar proteins. TRIM42 belongs to the C-III subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil domain. It also has a novel cysteine-rich motif N-terminal to the RBCC domain, as well as a COS (carboxyl-terminal subgroup one signature) box and a fibronectin type-III (FN3) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TRIM42 can interact with TRIM27, a known cancer-associated protein. Its precise biological function remains unclear
PIFCQICTQKRESAVKRCITCRLNLCNKCLRKLHGNKAFQDHILTDP
>gnl|CDD|380867 cd19809, Bbox1_TRIM45_C-X, B-box-type 1 zinc finger found in tripartite motif-containing protein 45 (TRIM45) and similar proteins. TRIM45, also known as RING finger protein 99 (RNF99), is a novel receptor for activated C-kinase (RACK1)-interacting protein that suppresses transcriptional activities of Elk-1 and AP-1, and downregulates mitogen-activated protein kinase (MAPK) signal transduction by inhibiting RACK1/PKC (protein kinase C) complex formation. It also negatively regulates tumor necrosis factor alpha (TNFalpha)-induced nuclear factor-kappaB (NF-kappa B)-mediated transcription, and suppresses cell proliferation. TRIM45 belongs to the C-X subclass of the TRIM (tripartite motif) family of proteins that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a filamin-type immunoglobulin (IG-FLMN) domain and NHL repeats positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
LLCDLCTDGNSSAEYRCFDCSENLCEFCKQAHRRQRKTASHRIISL
>gnl|CDD|380868 cd19810, Bbox1_TRIM56_C-V, B-box-type 1 zinc finger found in tripartite motif-containing protein 56 (TRIM56) and similar proteins. TRIM56, also known as RING finger protein 109 (RNF109), is a virus-inducible E3 ubiquitin ligase that restricts pestivirus infection. It positively regulates the Toll-like receptor 3 (TLR3) antiviral signaling pathway, and possesses antiviral activity against bovine viral diarrhea virus (BVDV), a ruminant pestivirus classified within the family Flaviviridae shared by tick-borne encephalitis virus (TBEV). It also possesses antiviral activity against two classical flaviviruses, yellow fever virus (YFV) and dengue virus (DENV), as well as a human coronavirus, HCoV-OC43, which is responsible for a significant share of common cold cases. It may not act on positive-strand RNA viruses indiscriminately. Moreover, TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses. TRIM56 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
PFCAVCPLSGPANVPATSRCLDCADFLCDACASGHRCSRLTHDHRVVDL
>gnl|CDD|380869 cd19811, Bbox1_TRIM66, B-box-type 1 zinc finger found in tripartite motif-containing protein 66 (TRIM66) and similar proteins. TRIM66, also termed transcriptional intermediary factor 1 delta (TIF1delta), is a novel heterochromatin protein 1 (HP1)-interacting member of the transcriptional intermediary factor 1 (TIF1) family, and is expressed by elongating spermatids. Like other TIF1 proteins, TRIM66 displays a potent trichostatin A (TSA)-sensitive repression function; TSA is a specific inhibitor of histone deacetylases. Moreover, TRIM66 plays an important role in heterochromatin-mediated gene silencing during postmeiotic phases of spermatogenesis. It functions as a negative regulator of postmeiotic genes acting through HP1 isotype gamma (HP1gamma) complex formation and centromere association. TRIM66 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
SCSECKEKRPAHSLCTTCNKWLCSSCTEEHRHGKSTS
>gnl|CDD|380870 cd19812, Bbox1_TRIM71_C-VII, B-box-type 1 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar proteins. TRIM71, also known as protein lineage variant 41 (lin-41), is an E3 ubiquitin-protein ligase that may play essential roles in embryonic stem cells, cellular reprogramming, and the timing of embryonic neurogenesis. It was first identified in the nematode Caenorhabditis elegans as a target of the differentiation-associated microRNA (miRNA) let-7 (lethal 7) and therefore part of a heterochronic gene network that controls larval development. In humans, it regulates let-7 microRNA biogenesis via modulation of Lin28B protein polyubiquitination. TRIM71 localizes to cytoplasmic P-bodies and directly interacts with the miRNA pathway proteins Argonaute 2 (AGO2) and DICER. It represses miRNA activity by promoting degradative ubiquitination of AGO2. Moreover, TRIM71 associates with SHCBP1, a novel component of the fibroblast growth factor (FGF) signaling pathway, and regulates its non-degradative polyubiquitination. It is also involved in the post-transcriptional regulation of the CDKN1A, RBL1 and RBL2 or EGR1 mRNAs by mediating RNA-binding in embryonic stem cells. TRIM71 belongs to the C-VII subclass of the TRIM (tripartite motif) family of proteins that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
RCSSCDEGNAATSRCKDCNEYLCDNCVRAHQRVRLTKDHFIVRF
>gnl|CDD|380871 cd19813, Bbox1_BRAT-like, B-box-type 1 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and similar proteins. BRAT is a NHL-domain family protein that functions as a translational repressor to inhibit cell proliferation. The family also contains Caenorhabditis elegans B-box type zinc finger protein ncl-1, a C. elegans Brat homolog which functions as a translational repressor that inhibits protein synthesis. BRAT contains Bbox1 and Bbox2 zinc fingers and NHL repeats. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
HCTGCKSKETAVARCFDCQVLLCANCVTAHQFMHCFKDHRVITL
>gnl|CDD|380872 cd19814, Bbox1_RNF207-like, B-box-type 1 zinc finger found in RING finger protein 207 (RNF207) and similar proteins. RNF207 is a cardiac-specific E3 ubiquitin-protein ligase that plays an important role in the regulation of cardiac repolarization. It regulates action potential duration, likely via effects on human ether-a-go-go-related gene (HERG) trafficking and localization, in a heat shock protein-dependent manner. RNF207 contains a RING finger, a B-box motif and Bbox C-terminal (BBC) domain, as well as a C-terminal non-homologous region (CNHR). The B-box motif shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
QCANCDSECLAMFYCNTCGQPLCDDCREETHRAKMFSKHEVVSLSKRTK
>gnl|CDD|380873 cd19815, Bbox1_HOIP, B-box-type 1 zinc finger found in HOIL-1-interacting protein (HOIP) and similar proteins. HOIP, also termed RING finger protein 31 (RNF31), or zinc in-between-RING-finger ubiquitin-associated domain protein, together with HOIL-1 and SHARPIN, forms the E3-ligase complex (also known as linear-ubiquitin-chain assembly complex LUBAC) that regulates NF-kappaB activity and apoptosis. It also interacts with the atypical mammalian orphan receptor DAX-1, trigger DAX-1 ubiquitination and stabilization, and participate in repressing steroidogenic gene expression. HOIP contains a B-box motif that shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
LCDLCGEAAASVFCASCEDKLCLSCDDLYHKHPARRSHHRQPI
>gnl|CDD|380874 cd19816, Bbox1_CYLD, B-box-type 1 zinc finger found in tumor suppressor cylindromatosis (CYLD) and similar proteins. CYLD, also termed ubiquitin carboxyl-terminal hydrolase CYLD, or deubiquitinating enzyme CYLD, or ubiquitin thioesterase CYLD, or ubiquitin-specific-processing protease CYLD, is a microtubule-associated deubiquitinase that specifically cleaves Lys-63-linked polyubiquitin chains. It plays a pivotal role in a wide range of cellular activities, including innate immunity, cell division, and ciliogenesis. CYLD antagonizes NF-kappaB and JNK signaling by disassembly of Lys63-linked ubiquitin chains synthesized in response to cytokine stimulation. Structural characterization reveals a small zinc-binding B-box inserted within the ubiquitin specific protease (USP) domain of CYLD. The B-box motif shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs) and is responsible for its intermolecular interaction and cytoplasmic localization. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
PRECIICGGLAEYECRDCYLDPGIGGKIKAFCKKCNKQTHLHPKRQNHKPRPLSVP
>gnl|CDD|380875 cd19817, Bbox1_ANCHR-like, B-box-type 1 zinc finger found in Abscission/NoCut checkpoint regulator (ANCHR) and similar proteins. ANCHR, also termed MLL partner containing FYVE domain, or zinc finger FYVE domain-containing protein 19, is a key regulator of the abscission step in cytokinesis: part of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. The family also includes zinc finger B-box domain-containing protein 1 (ZBBX), a B-box motif containing protein with unclear biological function. The B-box motif of this family shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
LPWCCICNEDASLRCHGCDGDLYCKRCFREGHDGFDRRDHRTVPY
>gnl|CDD|380876 cd19818, Bbox1_ZBBX, B-box-type 1 zinc finger found in zinc finger B-box domain-containing protein 1 (ZBBX) and similar proteins. The family corresponds to a group of uncharacterized zinc finger B-box domain-containing proteins. The B-box motif shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
QCGQCEQKAALLVCLECGEDYCSSCFAKFHQKGALKKHRSIPL
>gnl|CDD|380877 cd19819, Bbox1_ZFYVE1_rpt1, first B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) and similar proteins. ZFYVE1 also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYVE1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by Wortmannin, a PI3-kinase inhibitor. ZFYVE1 harbors two B-box motifs, both of which show high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
LMCQESYACSGSDEAVFECDECGSLQCQRCEKELHQQERLRNHERTRI
>gnl|CDD|380878 cd19820, Bbox1_ZFYVE1_rpt2, second B-box-type 1 zinc finger found in zinc finger FYVE domain-containing protein 1 (ZFYVE1) and similar proteins. ZFYVE1 also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYVE1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by Wortmannin, a PI3-kinase inhibitor. ZFYVE1 harbors two B-box motifs, both of which show high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
PYCDSCKGGNGNSMHSSTAGSRQRAAVRCQSCKINLCPECQKRTHSGGNKRKHPVTVYP
>gnl|CDD|380879 cd19821, Bbox1_BBX-like, B-box-type 1 zinc finger found in B-box (BBX) family of plant transcription factors and similar proteins. The BBX family includes a group of zinc finger transcription factors that contain one or two B-box motifs, and sometimes also feature a CCT (CONSTANS, CO-like, and TOC1) domain. They play important roles in plant growth and development, including seedling photomorphogenesis, photoperiodic regulation of flowering, shade avoidance, and responses to biotic and abiotic stresses. Their B-box motifs show high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs) and are involved in mediating transcriptional regulation and protein-protein interaction in plant signaling. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif; this family contains a modified motif, C3XC2H2, where X can be D, E, C or H
LCDSCESAPAVVYCRADRASLCRACDAKVHSANKLASRHQRVPL
>gnl|CDD|380880 cd19822, Bbox2_MID1_C-I, B-box-type 2 zinc finger found in midline-1 (MID1) and similar proteins. MID1, also termed midin, or midline 1 RING finger protein, or putative transcription factor XPRF, or RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRI18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. It monoubiquinates the alpha4 subunit of protein phosphatase 2A (PP2A), promoting proteosomal degradation of the catalytic subunit of PP2A (PP2Ac) and preventing the A and B subunits from forming an active complex. It promotes allergen and rhinovirus-induced asthma through the inhibition of PP2A activity. It is strongly upregulated in cytotoxic lymphocytes (CTLs) and directs lytic granule exocytosis and cytotoxicity of killer T cells. Loss-of-function mutations in MID1 lead to the human X-linked Opitz G/BBB (XLOS) syndrome characterized by defective midline development during embryogenesis. It heterodimerizes in vitro with its paralog MID2. MID1 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
SHIRGLMCLEHEDEKVNMYCVTDDQLICALCKLVGRHRDHQVAALSD
>gnl|CDD|380881 cd19823, Bbox2_MID2_C-I, B-box-type 2 zinc finger found in midline-2 (MID2) and similar proteins. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is a probable E3 ubiquitin-protein ligase that is highly related to MID1 that associate with cytoplasmic microtubules along their length and throughout the cell cycle. Like MID1, MID2 associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. MID2 can also substitute for MID1 to control exocytosis of lytic granules in cytotoxic T cells. It heterodimerizes in vitro with its paralog MID1. Loss-of-function mutations in MID2 lead to the human X-linked intellectual disability (XLID). MID2 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxy-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
LTCLEHENEKVNMYCVVDDQLICALCKLVGRHRDHQVASL
>gnl|CDD|380882 cd19824, Bbox2_TRIM2_C-VII, B-box-type 2 zinc finger found in tripartite motif-containing protein 2 (TRIM2) and similar proteins. TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM2 also plays a role in mediating the p42/p44 Semi-independent ubiquitination of the cell death-promoting protein Bcl-2-interacting mediator of cell death (Aim) in rapid ischemic tolerance. TRIM2 belongs to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
PLSCPNHDGNVMEFYCQSCETAMCQECTEGEHAEHPTVPLKD
>gnl|CDD|380883 cd19825, Bbox2_TRIM3_C-VII, B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3). TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It functions as a tumor suppressor that regulates asymmetric cell division in neuroblastoma. It binds to the ck inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclins D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It corresponds to gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of presynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendrite spine morphology. In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 belongs to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
AVAGKPLSCPNHEGKTMEFYCESCETAMCRECTEGEHREHVTVPLRD
>gnl|CDD|380884 cd19826, Bbox2_TRIM9_C-I, B-box-type 2 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar proteins. TRIM9 (the human ortholog of rat Spring), also termed RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in the neurodegenerative disorders through its ligase activity. It interacts with the WD repeat region of beta-transducer repeat-containing protein (beta-TCP) through its N-terminal degron motif (DSGXXS) depending on the phosphorylation status, and thus negatively regulate nuclear factor-kappaB (NF-kappaB) activation in the NF-kappaB pro-inflammatory signaling pathway. Moreover, TRIM9 acts as a critical catalytic link between Netrin-1 and exocytosis soluble NSF attachment receptor protein (SNARE) machinery in murine cortical neurons. It promotes SNARE-mediated vesicle fusion and axon branching in a Netrin-dependent manner. TRIM9 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
PRKISTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWK
>gnl|CDD|380885 cd19827, Bbox2_TRIM67_C-I, B-box-type 2 zinc finger found in tripartite motif-containing protein 67 (TRIM67) and similar proteins. TRIM67, also termed TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis. TRIM67 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
PTCAEHELENYSMYCASCRTPVCYQCLEEGKHAKHEVKALGAMWK
>gnl|CDD|380886 cd19828, Bbox2_TIF1a_C-VI, B-box-type 2 zinc finger found in transcription intermediary factor 1-alpha (TIF1-alpha). TIF1-alpha, also known as tripartite motif-containing protein 24 (TRIM24), E3 ubiquitin-protein ligase TRIM24, or RING finger protein 82, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TIF1-alpha interacts specifically and in a ligand-dependent manner with the ligand binding domain (LBD) of several nuclear receptors (NRs), including retinoid X (RXR), retinoic acid (RAR), vitamin D3 (VDR), estrogen (ER), and progesterone (PR) receptors. It also associates with heterochromatin-associated factors HP1alpha, MOD1 (HP1beta), and MOD2 (HP1gamma), as well as the vertebrate Kruppel-type (C2H2) zinc finger proteins that contain the transcriptional silencing domain KRAB. TIF1-alpha is a ligand-dependent co-repressor of retinoic acid receptor (RAR) that interacts with multiple nuclear receptors in vitro via an LXXLL motif and further acts as a gatekeeper of liver carcinogenesis. It also functions as an E3-ubiquitin ligase targeting p53, and is broadly associated with chromatin silencing. Moreover, it is a chromatin regulator that recognizes specific, combinatorial histone modifications through its C-terminal PHD-Bromo region. In addition, it interacts with chromatin and estrogen receptor to activate estrogen-dependent genes associated with cellular proliferation and tumor development
QRPVFCPFHKKEQLKLYCETCDKLTCRDCQLLEHKEHRYQFIEEAFQNQKVIIDTLI
>gnl|CDD|380887 cd19829, Bbox2_TIF1b_C-VI, B-box-type 2 zinc finger found in transcription intermediary factor 1-beta (TIF1-beta). TIF1-beta, also known as Kruppel-associated Box (KRAB)-associated protein 1 (KAP-1), KRAB-interacting protein 1 (KRIP-1), nuclear co-repressor KAP-1, RING finger protein 96, tripartite motif-containing protein 28 (TRIM28), or E3 SUMO-protein ligase TRIM28, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD) and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TIF1-beta acts as a nuclear co-repressor that plays a role in transcription and in the DNA damage response. Upon DNA damage, the phosphorylation of KAP-1 on serine 824 by the ataxia telangiectasia-mutated (ATM) kinase enhances cell survival and facilitates chromatin relaxation and heterochromatic DNA repair. It also regulates CHD3 nucleosome remodeling during the DNA double-strand break (DSB) response. Meanwhile, KAP-1 can be dephosphorylated by protein phosphatase PP4C in the DNA damage response. Moreover, KAP-1 is a co-activator of the orphan nuclear receptor NGFI-B (or Nur77) and is involved in NGFI-B-dependent transcription. It is also a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase. The N-terminal RBCC domains of TIF1-beta are responsible for the interaction with KRAB zinc finger proteins (KRAB-ZFPs), MDM2, MM1, C/EBPbeta, and the regulation of homo- and heterodimerization. The C-terminal PHD/Bromo domains are involved in interacting with SETDB1, Mi-2alpha and other proteins to form complexes with histone deacetylase or methyltransferase activity
TVYCSIHKQEPLKLFCETCDTLTCRDCQLNAHKDHQYQFLEDAV
>gnl|CDD|380888 cd19830, Bbox2_TIF1g_C-VI, B-box-type 2 zinc finger found in transcription intermediary factor 1 gamma (TIF1-gamma). TIF1-gamma, also known as tripartite motif-containing 33 (TRIM33), ectodermin, RFG7, or PTC7, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TIF1-gamma is an E3-ubiquitin ligase that functions as a regulator of transforming growth factor beta (TGFbeta) signaling. It inhibits the Smad4-mediated TGFbeta response by interaction with Smad2/3 or ubiquitylation of Smad4. Moreover, TIF1gamma is an important regulator of transcription during hematopoiesis, as well as a key actor of tumorigenesis. Like other TIF1 family members, TIF1-gamma also contains an intrinsic transcriptional silencing function. It can control erythroid cell fate by regulating transcription elongation. It can bind to the anaphase-promoting complex/cyclosome (APC/C) and promotes mitosis
ASGQRPVFCPVHKQEQLKLFCETCDRLTCRDCQLLEHKEHRYQFLEEAFQNQK
>gnl|CDD|380889 cd19831, Bbox2_MuRF1_C-II, B-box-type 2 zinc finger found in muscle-specific RING finger protein 1 (MuRF-1) and similar proteins. MuRF-1, also known as tripartite motif-containing protein 63 (TRIM63), RING finger protein 28 (RNF28), iris RING finger protein, or striated muscle RING zinc finger, is an E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover. It is predominantly fast (type II) fibre-associated in skeletal muscle and can bind to many myofibrillar proteins, including titin, nebulin, the nebulin-related protein NRAP, troponin-I (TnI), troponin-T (TnT), myosin light chain 2 (MLC-2), myotilin, and T-cap. The early and robust upregulation of MuRF-1 is triggered by disuse, denervation, starvation, sepsis, or steroid administration resulting in skeletal muscle atrophy. It also plays a role in maintaining titin M-line integrity. It associates with the periphery of the M-line lattice and may be involved in the regulation of the titin kinase domain. It also participates in muscle stress response pathways and gene expression. MuRF-1 belongs to the C-II subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
GHPMCKEHEDEKINIYCLTCEVPTCSMCKVFGIHKACEVAPLQ
>gnl|CDD|380890 cd19832, Bbox2_MuRF2_C-II, B-box-type 2 zinc finger found in muscle-specific RING finger protein 2 (MuRF-2) and similar proteins. MuRF-2, also known as tripartite motif-containing protein 55 (TRIM55) or RING finger protein 29 (RNF29), is a muscle-specific E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover and also a ligand of the transactivation domain of the serum response transcription factor (SRF). It is predominantly slow-fibre associated and highly expressed in embryonic skeletal muscle. MuRF-2 associates transiently with microtubules, myosin, and titin during sarcomere assembly. It has been implicated in microtubule, intermediate filament, and sarcomeric M-line maintenance in striated muscle development, as well as in signalling from the sarcomere to the nucleus. It plays an important role in the earliest stages of skeletal muscle differentiation and myofibrillogenesis. It is developmentally downregulated and is assembled at the M-line region of the sarcomere and with microtubules. MuRF-2 belongs to the C-II subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
PMCEEHEEERINIYCLNCEVPTCSLCKVFGAHKDCQVAPLTHVFQ
>gnl|CDD|380891 cd19833, Bbox2_MuRF3_C-II, B-box-type 2 zinc finger found in muscle-specific RING finger protein 3 (MuRF-3) and similar proteins. MuRF-3, also known as tripartite motif-containing protein 54 (TRIM54), or RING finger protein 30 (RNF30), is an E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover. It is ubiquitously detected in all fibre types, and is developmentally upregulated, associates with microtubules, the sarcomeric M-line and Z-line, and is required for microtubule stability and myogenesis. It associates with glutamylated microtubules during skeletal muscle development, and is required for skeletal myoblast differentiation and development of cellular microtubular networks. MuRF-3 controls the degradation of four-and-a-half LIM domain (FHL2) and gamma-filamin and is required for maintenance of ventricular integrity after myocardial infarction (MI). MuRF-3 belongs to the C-II subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
LMCEEHEEEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTV
>gnl|CDD|380892 cd19834, Bbox2_BSPRY, B-box-type 2 zinc finger found in B box and SPRY domain-containing protein (BSPRY) and similar proteins. BSPRY is a regulatory protein for maintaining calcium homeostasis. It may regulate epithelial calcium transport by inhibiting TRPV5 activity. BSPRY is composed of a B-box, an alpha-helical coiled coil and a SPRY domain. The B-box motif shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs). The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
DLCPDHELELDWFCSTERRLVCAQCASLGTCRGHRVTPLEERA
>gnl|CDD|380893 cd19835, Bbox2_TRIM65_C-IV, B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65) and similar proteins. TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5 enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
TLCQRHGRPLELYCRTEKRCVCCKCTVKECRNHNRVLLEEER
>gnl|CDD|380894 cd19836, Bbox1_MID1_C-I, B-box-type 1 zinc finger found in midline-1 (MID1) and similar proteins. MID1, also termed midin, or midline 1 RING finger protein, or putative transcription factor XPRF, or RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRI18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. It monoubiquinates the alpha4 subunit of protein phosphatase 2A (PP2A), promoting proteosomal degradation of the catalytic subunit of PP2A (PP2Ac) and preventing the A and B subunits from forming an active complex. It promotes allergen and rhinovirus-induced asthma through the inhibition of PP2A activity. It is strongly upregulated in cytotoxic lymphocytes (CTLs) and directs lytic granule exocytosis and cytotoxicity of killer T cells. Loss-of-function mutations in MID1 lead to the human X-linked Opitz G/BBB (XLOS) syndrome characterized by defective midline development during embryogenesis. MID1 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. MID1 heterodimerizes in vitro with its paralog MID2
EKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP
>gnl|CDD|380895 cd19837, Bbox1_MID2_C-I, B-box-type 1 zinc finger found in midline-2 (MID2) and similar proteins. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is a probable E3 ubiquitin-protein ligase that is highly related to MID1, which associates with cytoplasmic microtubules along their length and throughout the cell cycle. Like MID1, MID2 associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with alpha4, a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. MID2 can also substitute for MID1 to control exocytosis of lytic granules in cytotoxic T cells. Loss-of-function mutations in MID2 lead to human X-linked intellectual disability (XLID). MID2 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxy-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. MID2 heterodimerizes in vitro with its paralog MID1
ERIACQFCEQEPPRDAVKTCITCEVSYCDRCLRATHPNKKPFTSHRLVEPVPD
>gnl|CDD|380896 cd19838, Bbox1_TRIM8_C-V, B-box-type 1 zinc finger found in tripartite motif-containing protein 8 (TRIM8) and similar proteins. TRIM8, also known as glioblastoma-expressed RING finger protein (GERP) or RING finger protein 27 (RNF27), is a probable E3 ubiquitin-protein ligase that may promote proteasomal degradation of suppressor of cytokine signaling 1 (SOCS1) and further regulate interferon-gamma signaling. It functions as a new p53 modulator that stabilizes p53, impairing its association with MDM2 and inducing the reduction of cell proliferation. TRIM8 deficit dramatically impairs p53 stabilization and activation in response to chemotherapeutic drugs. TRIM8 also modulates tumor necrosis factor-alpha (TNFalpha) and interleukin-1beta (IL-1beta)-triggered nuclear factor-kappaB (NF-kappa B) activation by targeting transforming growth factor beta (TGFbeta) activated kinase 1 (TAK1) for K63-linked polyubiquitination. Moreover, TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. It also interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation of STAT3. TRIM8 belongs to the C-V subclass of nuclear TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The coiled coil domain is required for homodimerization and the region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
LHCVFCRRGPPLPAQKICLRCEAPCCQSHVQTHLQQPSTARGHLLVEA
>gnl|CDD|380897 cd19839, Bbox1_TRIM16, B-box-type 1 zinc finger found in tripartite motif-containing protein 16 (TRIM16) and similar proteins. TRIM16, also termed estrogen-responsive B box protein (EBBP), is a regulator that may play a role in the regulation of keratinocyte differentiation. It may also act as a tumor suppressor by affecting cell proliferation and migration or tumorigenicity in carcinogenesis. TRIM16 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
VLCDFCLEAKVKAVKSCLTCMVSYCEGHLRPHLENSKLQAHQLCDP
>gnl|CDD|380898 cd19840, Bbox1_TRIM29, B-box-type 1 zinc finger found in tripartite motif-containing protein 29 (TRIM29) and similar proteins. TRIM29, also termed ataxia telangiectasia group D-associated protein (ATDC), plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. TRIM29 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
VLCDSCIDNKQKAVKSCLVCQASFCELHLKPHLEGAAFRDHQLLEPI
>gnl|CDD|380899 cd19841, Bbox1_TRIM44, B-box-type 1 zinc finger found in tripartite motif-containing protein 44 (TRIM44) and similar proteins. TRIM44, also termed protein DIPB, functions as a critical regulator in tumor metastasis and progression. TRIM44 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif; this family contains a modified motif, C5H3
DGTCDACEPDEAKSALKVCDECAFSFCQSHAEEHRQKFASHTLREY
>gnl|CDD|380900 cd19842, Bbox1_TRIM25-like_C-IV, B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM25, TRIM47 and similar proteins. The family includes tripartite motif-containing proteins, TRIM25 and TRIM47, both of which belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TRIM25, also termed estrogen-responsive finger protein (EFP), or ubiquitin/ISG15-conjugating enzyme TRIM25, or zinc finger protein 147 (ZNF147), or E3 ubiquitin/ISG15 ligase TRIM25, is induced by estrogen and is particularly abundant in placenta and uterus. It has been implicated in cell proliferation, protein modification, and the retinoic acid inducible gene I (RIG-I)-mediated antiviral signaling pathway. It functions as an E3-ubiquitin ligase able to transfer ubiquitin and ISG15 to target proteins. TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis
LCDLCLGRELAAAKTCLTCLASFCPEHLEPHLSSPAFRSHRLCPPERDL
>gnl|CDD|380901 cd19843, Bbox1_TRIM9_C-I, B-box-type 1 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar proteins. TRIM9 (the human ortholog of rat Spring), also termed RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in neurodegenerative disorders through its ligase activity. It interacts with the WD repeat region of beta-transducer repeat-containing protein (beta-TCP) through its N-terminal degron motif depending on the phosphorylation status, and thus negatively regulate nuclear factor-kappaB (NF-kappaB) activation in the NF-kappaB pro-inflammatory signaling pathway. Moreover, TRIM9 acts as a critical catalytic link between Netrin-1 and exocytosis soluble NSF attachment receptor protein (SNARE) machinery in murine cortical neurons. It promotes SNARE-mediated vesicle fusion and axon branching in a Netrin-dependent manner. TRIM9 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
LKCQLCEKSPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP
>gnl|CDD|380902 cd19844, Bbox1_TRIM67_C-I, B-box-type 1 zinc finger found in tripartite motif-containing protein 67 (TRIM67) and similar proteins. TRIM67, also termed TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis. TRIM67 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
NARCQLCDRNPPEPAAVLCEQCDVLYCSACQLKCHPTRGPFAKHRLVPP
>gnl|CDD|380903 cd19845, Bbox1_TIF1a_C-VI, B-box-type 1 zinc finger found in transcription intermediary factor 1-alpha (TIF1-alpha). TIF1-alpha, also known as tripartite motif-containing protein 24 (TRIM24), E3 ubiquitin-protein ligase TRIM24, or RING finger protein 82, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TIF1-alpha interacts specifically and in a ligand-dependent manner with the ligand binding domain (LBD) of several nuclear receptors (NRs), including retinoic X (RXR), retinoic acid (RAR), vitamin D3 (VDR), estrogen (ER), and progesterone (PR) receptors. It also associates with heterochromatin-associated factors HP1alpha, MOD1 (HP1beta), and MOD2 (HP1gamma), as well as the vertebrate Kruppel-type (C2H2) zinc finger proteins that contain the transcriptional silencing domain KRAB. TIF1-alpha is a ligand-dependent co-repressor of retinoic acid receptor (RAR) that interacts with multiple nuclear receptors in vitro via an LXXLL motif and further acts as a gatekeeper of liver carcinogenesis. It also functions as an E3-ubiquitin ligase targeting p53, and is broadly associated with chromatin silencing. Moreover, it is a chromatin regulator that recognizes specific, combinatorial histone modifications through its C-terminal PHD-Bromo region. In addition, it interacts with chromatin and estrogen receptor to activate estrogen-dependent genes associated with cellular proliferation and tumor development
QVCTSCEDNAEANGFCVECVEWLCKTCIEAHQRVKFTKDHTVRQK
>gnl|CDD|380904 cd19846, Bbox1_TIF1b_C-VI, B-box-type 1 zinc finger found in transcription intermediary factor 1-beta (TIF1-beta). TIF1-beta, also known as Kruppel-associated Box (KRAB)-associated protein 1 (KAP-1), KRAB-interacting protein 1 (KRIP-1), nuclear co-repressor KAP-1, RING finger protein 96, tripartite motif-containing protein 28 (TRIM28), or E3 SUMO-protein ligase TRIM28, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TIF1-beta/KAP-1 acts as a nuclear co-repressor that plays a role in transcription and in the DNA damage response. Upon DNA damage, the phosphorylation of KAP-1 on serine 824 by the ataxia telangiectasia-mutated (ATM) kinase enhances cell survival and facilitates chromatin relaxation and heterochromatic DNA repair. It also regulates CHD3 nucleosome remodeling during the DNA double-strand break (DSB) response. Meanwhile, KAP-1 can be dephosphorylated by protein phosphatase PP4C in the DNA damage response. Moreover, KAP-1 is a co-activator of the orphan nuclear receptor NGFI-B (or Nur77) and is involved in NGFI-B-dependent transcription. It is also a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase. The N-terminal RBCC domains of TIF1-beta are responsible for the interaction with KRAB zinc finger proteins (KRAB-ZFPs), MDM2, MM1, C/EBPbeta, and the regulation of homo- and heterodimerization. The C-terminal PHD/Bromo domains are involved in interacting with SETDB1, Mi-2alpha and other proteins to form complexes with histone deacetylase or methyltransferase activity
ETIQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRVKSSSK
>gnl|CDD|380905 cd19847, Bbox1_TIF1g_C-VI, B-box-type 1 zinc finger found in transcriptional intermediary factor 1 gamma (TIF1-gamma). TIF1-gamma, also known as tripartite motif-containing 33 (TRIM33), ectodermin, RFG7, or PTC7, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TIF1-gamma is an E3-ubiquitin ligase that functions as a regulator of transforming growth factor beta (TGFbeta) signaling. It inhibits the Smad4-mediated TGFbeta response by interaction with Smad2/3 or ubiquitylation of Smad4. Moreover, TIF1-gamma is an important regulator of transcription during hematopoiesis, as well as a key actor of tumorigenesis. Like other TIF1 family members, TIF1-gamma also contains an intrinsic transcriptional silencing function. It can control erythroid cell fate by regulating transcription elongation. It can bind to the anaphase-promoting complex/cyclosome (APC/C) and promotes mitosis
DEKSEQVCTSCEDNASAVGFCVECGEWLCKTCIEAHQRVKFTKDHMIRKKEDVS
>gnl|CDD|380906 cd19848, Bbox1_TRIM36_C-I, B-box-type 1 zinc finger found in tripartite motif-containing protein 36 (TRIM36) and similar proteins. TRIM36, the human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequent dorsal axis formation. It is also potentially associated with chromosome segregation by interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM36 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
AATAIMCDLCKPPPQESTKSCMDCKASYCNECFKIHHPWGTPKAQHEYVGPTTNF
>gnl|CDD|380907 cd19849, Bbox1_TRIM46_C-I, B-box-type 1 zinc finger found in tripartite motif-containing protein 46 (TRIM46) and similar proteins. TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that specifically localizes to the proximal axon, partly overlaps with the axon initial segment (AIS) at later stages, and organizes uniform microtubule orientation in axons. It controls neuronal polarity and axon specification by driving the formation of parallel microtubule arrays. TRIM46 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins, which are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
AIMCQFCKPPQLEATKGCTECRASFCNECFKLYHPWGTQKAQHEPTPPTLTF
>gnl|CDD|381251 cd19851, lipocalin_CHL, chloroplastic lipocalin(CHL) similar to Arabidopsis CHL. Chloroplastic lipocalin (CHL) prevents thylakoidal membrane lipids peroxidation and is protective against oxidative stress, especially mediated by singlet oxygen in response to excess light and other stress (e.g. heat shocks). CHL is required for seed longevity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
MRGMTAKNFDPVRYSGRWFEVASLKRGFAGQGQEDCHCTQGVYTFDMKESAIRVDTFCVHGSPDGYITGI
RGKVQCVGAEDLEKSETDLEKQEMIKEKCFLRFPTIPFIPKLPYDVIATDYDNYALVSGAKDKGFVQVYS
R
>gnl|CDD|381252 cd19852, FABP_pancrustacea, fatty acid-binding protein similar to Locusta migratoria FABP (Lm-FABP). This subfamily includes fatty acid-binding protein found mainly in insects such as the migratory locust (Locusta migratoria) FABP (Lm-FABP) and the desert locust (Schistocerca gregaria) FABP (Sg-FABP), having flight muscle tissues that contain unusually high levels FABP, similar to migratory birds. Both Sg- and Lm-FABP are closely related to the mammalian i-LBP subfamily IV, especially to the heart and adipocyte FABP forms. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development
EFLGIKYKLDSSENFDEYMKAIGVGLITRKAGNALTPVVELELEDGTYTLTTSTTFKTTEFKFKLGEEFD
EETLDGRKVKSIITFDGNKLVQEQKGDHPTIIIREFSKEEMKAVLTAGDVVCTRVYKA
>gnl|CDD|380683 cd19854, DSRM_DHX9_rpt1, first double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins. DHX9 (EC 3.6.4.13; also known as ATP-dependent RNA helicase A, DExH-box helicase 9 (DDX9), Leukophysin (LKP), nuclear DNA helicase II (NDH II), NDH2, or RNA helicase A) is a multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation, and RNA-mediated gene silencing. It contains two double-stranded RNA binding motifs (DSRMs) at the N-terminal region. This model corresponds to the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
EIKAFLYAWCGKKKLTPEYDIKEAGNKHRQRFKCEVRVEGFDYVGTGNATNKKDAQTNAARDFLNYLVR
>gnl|CDD|380684 cd19855, DSRM_DHX9_rpt2, second double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins. DHX9 (EC 3.6.4.13; also known as ATP-dependent RNA helicase A, DExH-box helicase 9 (DDX9), Leukophysin (LKP), nuclear DNA helicase II (NDH II), NDH2, or RNA helicase A) is a multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation and RNA-mediated gene silencing. It contains two double-stranded RNA binding motifs (DSRMs) at the N-terminal region. This model corresponds to the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
LDNAKSRLNEFLQKNKIPAEYKYTSVGPDHNRSFIAELSIFVKQLGKTIYARETGSNKKLASQSCALSLV
RQLYH
>gnl|CDD|380685 cd19856, DSRM_Kanadaptin, double-stranded RNA binding motif of Kanadaptin and similar proteins. Kanadaptin (also known as human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP)) is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. The double-stranded RNA binding motif (DSRM) is not sequence specific, but highly specific for dsRNAs of various origin and structure
EAFYLKDPKKALKGFFDREGEELEYEVEEQGSGRTRKYVCRIELPLDDASGGPIVAEASVSGKKKEAVVA
CALEACRILDRHGLLR
>gnl|CDD|380686 cd19857, DSRM_STAU_rpt1, first double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins. Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
TPMCLLNELARFNKIRPQYTLVDEEGPAHKKTFTVKLTLGDEEEYEASGSSIKKAQHAAAEKAL
>gnl|CDD|380687 cd19858, DSRM_STAU_rpt2, second double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins. Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
RQEHPNYNNYGMPQRRGDYRFRYPYPNNPSGPPPPFYVTLTVGEREFIGEGRTRQAARHDAASKALK
>gnl|CDD|380688 cd19859, DSRM_STAU_rpt3, third double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins. Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
EISLVHEIALKRNLTVNFEVLRESGPPHMKNFITRCTVGSFVTEGEGNSKKVSKKRAAEKMLEEL
>gnl|CDD|380689 cd19860, DSRM_STAU_rpt4, fourth double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins. Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the fourth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
NPISRLIQIQQARKEKEPVYSLVAERGTPRRREFVMQVTVGDKTATGTGPNKKLAKRNAAEAMLELLG
>gnl|CDD|380690 cd19861, DSRM_STAU_rpt5, fifth double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins. Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the fifth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
PKEQLEYLAKVLGFSVEFTDFPKGNKSEYLSLVSLGTEPPQVCHGSGSSVEESRDAAALNALKLLKEL
>gnl|CDD|380691 cd19862, DSRM_PRKRA-like_rpt1, first double-stranded RNA binding motif of protein activator of the interferon-induced protein kinase (PRKRA) and similar proteins. This family includes protein activator of the interferon-induced protein kinase (PRKRA) and the RISC-loading complex subunit TARBP2. PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. TARBP2 (also called TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)), participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. This family also includes Drosophila melanogaster Loquacious and similar proteins. Loquacious (Loqs) is a double-stranded RNA-binding domain (dsRBD) protein, a homolog of human TAR RNA binding protein (TRBP) that is a protein first identified as binding the HIV trans-activator RNA (TAR). Loqs interacts with Dicer1 (dmDcr1) to facilitate miRNA processing. PRKRA family proteins contain three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KTPISVLQELCAKRGITPKYELISSEGAVHEPTFTFRVTVGDITATGSGTSKKKAKHAAAENALEQLKGS
>gnl|CDD|380692 cd19863, DSRM_PRKRA-like_rpt2, second double-stranded RNA binding motif of PRKRA, TARBP2 and similar proteins. The family includes protein activator of the interferon-induced protein kinase (PRKRA) and the RISC-loading complex subunit TARBP2. PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. TARBP2 (also called TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)) participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. The family also includes Drosophila melanogaster Loquacious and similar proteins. Loquacious (Loqs) is a double-stranded RNA-binding domain (dsRBD) protein, a homolog of human TAR RNA binding protein (TRBP) that is a protein first identified as binding the HIV trans-activator RNA (TAR). Loqs interacts with Dicer1 (dmDcr1) to facilitate miRNA processing. PRKRA family proteins contain three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
NPVGILQELCVQRRWRLPEYEVEQESGPPHEKEFTIACRVENFSETGSGKSKKLAKRAAAEKMLTRL
>gnl|CDD|380693 cd19864, DSRM_PRKRA-like_rpt3, third double-stranded RNA binding motif of PRKRA, TARBP2 and similar proteins. The family includes protein activator of the interferon-induced protein kinase (PRKRA) and the RISC-loading complex subunit TARBP2. PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. TARBP2 (also called TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)) participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. The family also includes Drosophila melanogaster Loquacious and similar proteins. Loquacious (Loqs) is a double-stranded RNA-binding domain (dsRBD) protein, a homolog of human TAR RNA binding protein (TRBP) that is a protein first identified as binding the HIV trans-activator RNA (TAR). Loqs interacts with Dicer1 (dmDcr1) to facilitate miRNA processing. PRKRA family proteins contain three double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
DDYCELLQELAEEQKFKVTYVDIEELSSSGKYQCLVQLSTLPPTVCHGSGASLEEAKEEAARNALEYLKI
MT
>gnl|CDD|380694 cd19865, DSRM_STRBP_RED-like_rpt1, first double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins. This family includes spermatid perinuclear RNA-binding protein (STRBP) and interleukin enhancer-binding factor 3 (ILF3), as well as two RNA-editing deaminases, RED1 and RED2. STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. RED1 (EC 3.5.4.37; also called double-stranded RNA-specific editase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase, ADARB1, ADAR2, or DRADA2) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. RED2 (also called double-stranded RNA-specific editase B2, RNA-dependent adenosine deaminase 3, RNA-editing enzyme 2, dsRNA adenosine deaminase B2, ADAR3, or ADARB2) prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. It is capable of binding to dsRNA, but also to ssRNA. RED2 lacks editing activity for currently known substrate RNAs. Members of this group contain two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KNALMQLNELRPGLQYKLTSQTGPVHAPVFTMSVEVNGQTFEGTGRSKKKAKLEAAEKALRSF
>gnl|CDD|380695 cd19866, DSRM_STRBP_RED-like_rpt2, second double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins. This family includes spermatid perinuclear RNA-binding protein (STRBP) and interleukin enhancer-binding factor 3 (ILF3), as well as two RNA-editing deaminases, RED1 and RED2. STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. RED1 (EC 3.5.4.37; also called double-stranded RNA-specific editase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase, ADARB1, ADAR2, or DRADA2) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. RED2 (also called double-stranded RNA-specific editase B2, RNA-dependent adenosine deaminase 3, RNA-editing enzyme 2, dsRNA adenosine deaminase B2, ADAR3, or ADARB2) prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. It is capable of binding to dsRNA but also to ssRNA. RED2 lacks editing activity for currently known substrate RNAs. Members of this group contain two double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KNPVMLLNELRPGLKYKCLSESGESHAKSFVMSVTVDGQTFEGTGRSKKLAKAAAAQAALAKL
>gnl|CDD|380696 cd19867, DSRM_DGCR8_rpt1, first double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and similar proteins. DGCR8 is a component of the microprocessor complex that acts as an RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis. Within the microprocessor complex, DGCR8 functions as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11bp away from the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. DGCR8 contains two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
INPDGKSPVCILHEYCQRVLKVQPEYNFTETENAATPFSAEVFINGVEYGSGEASSKKLAKQKAARATLE
ILIP
>gnl|CDD|380697 cd19868, DSRM_DGCR8_rpt2, second double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and similar proteins. DGCR8 is a component of the microprocessor complex that acts as an RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis. Within the microprocessor complex, DGCR8 functions as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11bp away from the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. DGCR8 contains two double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
PSPYQILQECLKRNHGMGDTELKFEVINDKHQKHEYTMTVGKHTVTVICKNKKEGKQLAAQAILKKLHP
>gnl|CDD|380698 cd19869, DSRM_DCL_plant, double-stranded RNA binding motif of plant Dicer-like proteins. The family includes plant Dicer-like (DCL) proteins and other ribonuclease (RNase) III-like (RTL) proteins. DCLs are endoribonucleases involved in RNA-mediated post-transcriptional gene silencing (PTGS). They function in the microRNA (miRNA) biogenesis pathway by cleaving primary miRNAs (pri-miRNAs) and precursor miRNAs (pre-miRNAs). Family members contain a double-stranded RNA binding motif (DSRM) at the C-terminus. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
NEICLKRRWPMPVYRCVEEEGPAHAKRFTYMVRVKIPERGWTIECEGEPMRSKKRAKDSAALLLLEYLKK
>gnl|CDD|380699 cd19870, DSRM_SON-like, double-stranded RNA binding motif of protein SON and similar proteins. Protein SON (also known as Bax antagonist selected in saccharomyces 1 (BASS1), negative regulatory element-binding protein (NRE-binding protein), or protein DBP-5, or SON3) is an RNA-binding protein which acts as an mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. It specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Members of this group contain a double-stranded RNA binding motif (DSRM) at the C-terminus. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
GKHPVSALMELCNKRKWGPPEFRLVEESGPPHRKHFLFKVVVNGVEYQPSVASGNKKDAKAQAATVALQA
LGLVP
>gnl|CDD|380700 cd19871, DSRM_DUS2L, double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins. DUS2L (also known as dihydrouridine synthase 2 (DUS2), up-regulated in lung cancer protein 8 (URLC8), or tRNA-dihydrouridine synthase 2-like) catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. It negatively regulates the activation of EIF2AK2/PKR. DUS2L contains an N-terminal FMN-binding domain and a C-terminal double-stranded RNA binding motif (DSRM) that is not sequence specific, but highly specific for dsRNAs of various origin and structure
TPKMILNEWCRKNKLPQPVYETVQRPSDRLFQSVVTVDGKKYTSSLWEKSKKLAEQAAAIVCLRALGL
>gnl|CDD|380701 cd19872, DSRM_A1CF-like, double-stranded RNA binding motif of APOBEC1 complementation factor (A1CF), RNA-binding protein 46 (RBM46) and similar proteins. The family includes two dsRNA-binding motif-containing proteins, A1CF and RBM46. A1CF (also known as APOBEC1-stimulating protein) is an essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the posttranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. A1CF binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. RBM46 (also called cancer/testis antigen 68 (CT68), or RNA-binding motif protein 46) plays a novel role in the regulation of embryonic stem cell (ESC) differentiation by regulating the degradation of beta-catenin mRNA. It also regulates trophectoderm specification by stabilizing Cdx2 mRNA in early mouse embryos. Members of this family contain three RNA recognition motifs (RRMs) and a C-terminal double-stranded RNA binding motif (DSRM) that is not sequence specific, but highly specific for dsRNAs of various origin and structure
NPVQILEEICQKNGWGEPVYQLLSTSSNNEVQLFIYKVTIPNLPNGRLTFQPDKLCRTPEEAKVLAAEFV
LAQLG
>gnl|CDD|380702 cd19873, DSRM_MRPL3_like, double-stranded RNA binding motif of Saccharomyces cerevisiae mitochondrial 54S ribosomal protein L3 (MRPL3) and similar proteins. MRPL3 (also called mitochondrial large ribosomal subunit protein mL44) is a component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. MRPL3 contains a RNase III-like domain and a double-stranded RNA binding motif (DSRM). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
RPLDISDLIKLENPKRTLSALLKREGLEPPVSRLLKESGRASHTPTFVVGVYSGSQKLGEGAGSSIKMAE
IRAARDALRKHYLY
>gnl|CDD|380703 cd19874, DSRM_MRPL44, double-stranded RNA binding motif of mitochondrial 39S ribosomal protein L44 (MRPL44) and similar proteins. MRPL44 (also known as L44mt, MRP-L44, or mitochondrial large ribosomal subunit protein mL44) is a component of the 39S subunit of mitochondrial ribosome. It may play a role in the assembly/stability of nascent mitochondrial polypeptides exiting the ribosome. MRPL44 contains a RNase III-like domain and a double-stranded RNA binding motif (DSRM). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
VGKDLNEIWTPANPMGLLVEILQKRGLPPPEPRLIRQSGANTVLPVYFVGLYSDKKLIGEGPGESILIAE
EMAARDALRRLFGT
>gnl|CDD|380704 cd19875, DSRM_EIF2AK2-like, double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins. The family includes EIF2AK2 and adenosine deaminase domain-containing proteins, ADAD1 and ADAD2. EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. ADAD1 (also called testis nuclear RNA-binding protein (TENR)) and ADAD2 (also called testis nuclear RNA-binding protein-like (TENRL)) are phylogenetically related to a family of adenosine deaminases involved in RNA editing. ADAD1 plays an essential function in spermatid morphogenesis. It may be involved in testis-specific nuclear post-transcriptional processes such as heterogeneous nuclear RNA (hnRNA) packaging, alternative splicing, or nuclear/cytoplasmic transport of mRNAs. ADAD2 is a double-stranded RNA binding protein with unclear biological function. Members of this group contains varying numbers of double-stranded RNA binding motifs (DSRMs). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KNPVSALNEYCQKRGLSLEFVDVSVGPDHCPGFTASATIDGIVFASATGTSKKEAKRAAAKLALKKL
>gnl|CDD|380705 cd19876, DSRM_RNT1p-like, double-stranded RNA binding motif of Saccharomyces cerevisiae ribonuclease 3 (RNT1p) and similar proteins. RNT1p (EC 3.1.26.3; also known as ribonuclease III (RNase III)) is a dsRNA-specific nuclease that cleaves eukaryotic pre-ribosomal RNA at the U3 snoRNP-dependent A0 site in the 5'-external transcribed spacer (ETS) and in the 3'-ETS. RNT1p contains a double-stranded RNA binding motif (DSRM) at the C-terminus. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
DKFAKQKLYSLIGPASLKPEYVVVKKEGGNDPNYTVACRINGEVLGTGVGRSIKKAGQRAAMSALSNKK
>gnl|CDD|380706 cd19877, DSRM_RNAse_III_meta_like, double-stranded RNA binding motif of metazoan ribonuclease III (RNase III) and similar proteins. RNase III (EC 3.1.26.3; also known as Drosha, or ribonuclease 3) is a double-stranded RNA (dsRNA)-specific endoribonuclease that is involved in the initial step of microRNA (miRNA) biogenesis. It is a component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, RNase III cleaves the 3' and 5' strands of a stem-loop in pri-miRNAs (processing center 11 bp from the dsRNA-ssRNA junction) to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. It is also involved in pre-rRNA processing. Metazoan RNase III is a larger protein than bacterial RNase III. It contains two RNase III domains in the C-terminal half of the protein followed by a double-stranded RNA binding motif (DSRM). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
NDPKSQLQQCCLTLRTEGKKEPDIPEYKVLQKSGPTNTRVYTVAVYFRGERIATGTGSSIQQAEMNAAEK
ALEKL
>gnl|CDD|380707 cd19878, DSRM_AtDRB-like, double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRBs)and similar proteins. This family includes a group of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRB1-5). They bind double-stranded RNA (dsRNA) and may be involved in RNA-mediated silencing. Members of this family contain two to three double-stranded RNA binding motifs (DSRMs). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
YKNLLQEYAQKKKIPLPKYESAKSGPSHQPTFVSTVIVLGVRFSSEGAKNKKQAEQSAAKVALKELG
>gnl|CDD|380708 cd19879, DSRM_STAU1_rpt1, first double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KEKTPMCLVNELARFNKIQPEYKLLSEQGPAHSKVFTVQLTLGDQHWEAEGTSIKKAQHAAAAKAL
>gnl|CDD|380709 cd19880, DSRM_STAU2_rpt1, first double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
NPKEKTPMCLVNELARFNRIQPQYKLLNERGPAHAKIFTVQLTLGEQTWEAEGSSIKKAQHAAASKAL
>gnl|CDD|380710 cd19881, DSRM_STAU1_rpt2, second double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
MKLGKKPIYKPIDPYTGMRSAYNYNMRGNGAYPPRYFYPFPPVGPVLYQVELSIGGQQFHGKGRTRQAAK
HDAAAKALK
>gnl|CDD|380711 cd19882, DSRM_STAU2_rpt2, second double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
VELNGLAMKRGEPAIYRPIDPKPPPNYRPNYNFRGMYNQRYHYPMPKTFYVSLTVGNREFIGEGRTRQAA
RHNAAMKALQAL
>gnl|CDD|380712 cd19883, DSRM_STAU1_rpt3, third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KSEISQVFEIALKRNMPVNFEVTKETGPPHMKSFVTKVSVGEFAGEGEGKSKKISKKNAAIAVLEEL
>gnl|CDD|380713 cd19884, DSRM_STAU2_rpt3, third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KSEISLVFEIALKRNMPVSFEVIKESGPPHMKSFVTRVTVGEFTAEGEGNSKKLSKKRAATSVLQEL
>gnl|CDD|380714 cd19885, DSRM_STAU1_rpt4, fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the fourth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
QTSPEYGQGMNPISRLAQIQQAKKEKEPEYTLITERGLPRRREFVMQVKVGNQTAEGMGPNKKVAKRNAA
EKMLELLGFKVPQPQP
>gnl|CDD|380715 cd19886, DSRM_STAU2_rpt4, fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the fourth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
QGMNPISRLAQIQQAKKEKEPEYVLLSERGMPRRREFVMQVKVGNEVATGTGPNKKIAKRNAAEAMLLQL
GYKASTPLQDQTEKSG
>gnl|CDD|380716 cd19887, DSRM_STAU1_rpt5, fifth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the fifth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
RPSEQLDYLSRVQGLQVEYKDFPKNNKNEFVSLINCSSQPPLISHGIGKDVESCHDMAALNILKLLSELD
>gnl|CDD|380717 cd19888, DSRM_STAU2_rpt5, fifth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the fifth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
VQPSKQLEYLARIQGFQVQYSDRQNGKECMTCLTLSPVQMTFHGIGSSIEASHDQAALSALKQLSEQG
>gnl|CDD|380718 cd19889, DSRM_PRKRA_rpt1, first double-stranded RNA binding motif of protein activator of the interferon-induced protein kinase (PRKRA) and similar proteins. PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. PRKRA contains three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
GKTPIQLLHEYGTKTGNIPVYELEKSEGQAHLPSFTFRVTVGDITCTGEGTSKKLAKHRAAEAALNILKG
N
>gnl|CDD|380719 cd19890, DSRM_TARBP2_rpt1, first double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and similar proteins. TARBP2 (also known as TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)), participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. TARBP2 contains three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
PGKTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDISCTGQGPSKKAAKHKAAEVALKLLK
GG
>gnl|CDD|380720 cd19891, DSRM_PRKRA_rpt2, second double-stranded RNA binding motif of protein activator of the interferon-induced protein kinase (PRKRA) and similar proteins. PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. PRKRA contains three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
NPIGSLQELAVQKGWRLPEYTLAQESGPPHKREFTITCRVETFVETGTGTSKKVAKRNAAEKLLAKF
>gnl|CDD|380721 cd19892, DSRM_PRKRA_rpt3, third double-stranded RNA binding motif of protein activator of the interferon-induced protein kinase (PRKRA) and similar proteins. PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. PRKRA contains three double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
TDYVQMLGEVAEEQGFNVTYLDIDELSVNGQYQCLAELSTSPVTVCHGTGISCGNAHNDAAHNALQYLKI
MA
>gnl|CDD|380722 cd19893, DSRM_TARBP2_rpt3, third double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and similar proteins. TARBP2 (also known as TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)) participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. TARBP2 contains three double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
SNFCRLLRELSEEQAFHISYLDIEELSLSGLCQCLVELSTQPATVCHGSATTRDAARANAAHNALQYLKI
MA
>gnl|CDD|380723 cd19894, DSRM_STRBP-like_rpt1, first double-stranded RNA binding motif of STRBP, ILF3 and similar proteins. This family includes spermatid perinuclear RNA-binding protein (STRBP) and interleukin enhancer-binding factor 3 (ILF3). STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Members of this STRBP/ILF3 group contain an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
MNALMRLNQLRPGLQYKLASQTGPVHAPQFTMSVEVDGVTYEASGPSKKTAKLHVAVKVLQAM
>gnl|CDD|380724 cd19895, DSRM_RED1_rpt1, first double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar proteins. RED1 (EC 3.5.4.37; also known as double-stranded RNA-specific editase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase, ADARB1, ADAR2, or DRADA2) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. It contains two double-stranded RNA binding motifs (DSRMs) and a C-terminal RNA-specific adenosine-deaminase (editase) domain. This model describes the first DSRM. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
GPVLPKNALMQLNEIKPGLQYKLLSQTGPVHAPVFVMSVEVNGQVFEGSGPTKKKAKLHAAEKALRSFVQ
FP
>gnl|CDD|380725 cd19896, DSRM_RED2_rpt1, first double-stranded RNA binding motif of RNA-editing deaminase 2 (RED2) and similar proteins. RED2 (also known as double-stranded RNA-specific editase B2, RNA-dependent adenosine deaminase 3, RNA-editing enzyme 2, dsRNA adenosine deaminase B2, ADAR3, or ADARB2) prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. It is capable of binding to dsRNA but also to ssRNA. RED2 contains two double-stranded RNA binding motifs (DSRMs) and a C-terminal RNA-specific adenosine-deaminase (editase) domain. This model describes the first DSRM. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure. RED2 lacks editing activity for currently known substrate RNAs, and may have an inactive editase domain
WSVTPKNALVQLNELKPGLQYRMVSQTGPVHAPVFAVAVEVNGLTFEGTGPTKKKAKMRAAEMALKSFVQ
FPNA
>gnl|CDD|380726 cd19897, DSRM_STRBP-like_rpt2, second double-stranded RNA binding motif of STRBP, ILF3 and similar proteins. This family includes spermatid perinuclear RNA-binding protein (STRBP) and interleukin enhancer-binding factor 3 (ILF3). STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Members of this STRBP/ILF3 group contain an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGAGSNKKVAKANAALAALEKLF
>gnl|CDD|380727 cd19898, DSRM_RED1_rpt2, second double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar proteins. RED1 (EC 3.5.4.37; also known as double-stranded RNA-specific editase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase, ADARB1, ADAR2, or DRADA2) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. It contains two double-stranded RNA binding motifs (DSRMs) and a C-terminal RNA-specific adenosine-deaminase (editase) domain. This model describes the second DSRM. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
SGKNPVMILNELRPGLKYEFVSESGESHAKNFVMSVTVDGQTFEGSGRNKKLAKARAAQAALAKLFNLQL
>gnl|CDD|380728 cd19899, DSRM_RED2_rpt2, second double-stranded RNA binding motif of RNA-editing deaminase 2 (RED2) and similar proteins. RED2 (also known as double-stranded RNA-specific editase B2, RNA-dependent adenosine deaminase 3, RNA-editing enzyme 2, dsRNA adenosine deaminase B2, ADAR3, or ADARB2) prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. It is capable of binding to dsRNA but also to ssRNA. RED2 contains two double-stranded RNA binding motifs (DSRMs) and a C-terminal RNA-specific adenosine-deaminase (editase) domain. This model describes the second DSRM. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure. RED2 lacks editing activity for currently known substrate RNAs, and may have an inactive editase domain
SPAESEKNPVVLLNELRPGLRYVCLSETAEKQHIKSFVMAVRVDGRTFEGSGRSKKLAKAQAAQAALQAL
FNIR
>gnl|CDD|380729 cd19900, DSRM_A1CF, double-stranded RNA binding motif of APOBEC1 complementation factor (A1CF) and similar proteins. A1CF (also known as APOBEC1-stimulating protein) is an essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the posttranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. A1CF binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. It contains three RNA recognition motifs (RRMs) and a C-terminal double-stranded RNA binding motif (DSRM) that is not sequence specific, but highly specific for dsRNAs of various origin and structure
KSPPQILEEICQKNNWGQPVYQLHSTIGPDQRQLFLYKVTIPALASQYPNITPFQPNKLCRSVEEAKSYA
AEYTLQQLGIP
>gnl|CDD|380730 cd19901, DSRM_RBM46, double-stranded RNA binding motif of RNA-binding protein 46 (RBM46) and similar proteins. RBM46 (also known as cancer/testis antigen 68 (CT68), or RNA-binding motif protein 46) plays a novel role in the regulation of embryonic stem cell (ESC) differentiation by regulating the degradation of beta-catenin mRNA. It also regulates trophectoderm specification by stabilizing Cdx2 mRNA in early mouse embryos. RBM46 contains three RNA recognition motifs (RRMs) and a C-terminal double-stranded RNA binding motif (DSRM) that is not sequence specific, but highly specific for dsRNAs of various origin and structure
SAVMHLDYYCNKNNWSPPEYYLYSTTSQDGKVLLVYKVVIPAIANSSQSYFMPDKLCTTLEDAKELAAQF
TLLHLDYS
>gnl|CDD|380731 cd19902, DSRM_DRADA, double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) and similar proteins. DRADA (EC 3.5.4.37; also known as 136 kDa double-stranded RNA-binding protein (p136), interferon-inducible protein 4 (IFI-4), K88DSRBP, ADAR1, G1P1, or ADAR) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. DRADA family members contain at least one double-stranded RNA binding motifs (DSRM); vertebrate proteins contain three. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KNPVSALMEYAQSRGVTAEIEVLSQSGPPHNPRFKAAVFVGGRRFPSVEASSKKDAKQEAADLALRALIA
E
>gnl|CDD|380732 cd19903, DSRM_EIF2AK2_rpt1, first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins. EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
GNYMGKLNEYCQKQKVVLDYVEVPTSGPSHDPRFTFQVVIDGKEYPEGEGKSKKEAKQAAAKLALEIL
>gnl|CDD|380733 cd19904, DSRM_EIF2AK2_rpt2, second double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins. EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
VNYISLLNQYAQKKRLTVNYEQCASTGVPGPPRFSCKCKIGQKEYGIGTGSTKQEAKQAAAKEAYEQLL
>gnl|CDD|380734 cd19905, DSRM_ADAD1, double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) and similar proteins. ADAD1 (also known as testis nuclear RNA-binding protein (TENR)) is phylogenetically related to a family of adenosine deaminases involved in RNA editing. It plays an essential function in spermatid morphogenesis. It may be involved in testis-specific nuclear post-transcriptional processes such as heterogeneous nuclear RNA (hnRNA) packaging, alternative splicing, or nuclear/cytoplasmic transport of mRNAs. ADAD1 contains a double-stranded RNA binding motif (DSRM) and a C-terminal adenosine-deaminase (editase) domain. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KNPVSALHEYAQMTRLKLSFKETVTTGNVAGPYFAFCAVVDGIEYPTGVGKTKKEAKANAAKIALDELL
>gnl|CDD|380735 cd19906, DSRM_ADAD2, double-stranded RNA binding motif of adenosine deaminase domain-containing protein 2 (ADAD2) and similar proteins. ADAD2 (also known as testis nuclear RNA-binding protein-like (TENRL)) is phylogenetically related to a family of adenosine deaminases involved in RNA editing. It is a double-stranded RNA binding protein with unclear biological function. ADAD2 contains a double-stranded RNA binding motif (DSRM) and a C-terminal adenosine-deaminase (editase) domain. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
PPKTPLSLLHEYAAKLSLEVEFRETQEEGPVGPFTVSARLRSRVQRTGVVCGAGTARAKKDAKQVAAAAA
LEKL
>gnl|CDD|380736 cd19907, DSRM_AtDRB-like_rpt1, first double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRBs)and similar proteins. This family includes a group of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRB1-5). They bind double-stranded RNA (dsRNA) and may be involved in RNA-mediated silencing. Members of this family contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
MYKSQLQEYAQKSCLNLPVYACIREGPDHAPRFRATVTFNGVIFESPPGFPTLKAAEHSAAEVALNSLA
>gnl|CDD|380737 cd19908, DSRM_AtDRB-like_rpt2, second double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRBs)and similar proteins. This family includes a group of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRB1-5). They bind double-stranded RNA (dsRNA) and may be involved in RNA-mediated silencing. Members of this family contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
GLYKNLLQEYAQKAGLPLPLYTTVRSGPGHVPTFTCTVEIAGITFTGEAAKTKKQAEKSAARTAWSSIK
>gnl|CDD|380738 cd19909, DSRM_STRBP_rpt1, first double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) and similar proteins. STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. STRBP contains an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
DANQPMNALMRLNQIRPGLQYKLLSQSGPVHAPVFTMSVDVDGTTYEASGPSKKTAKLHVAVKVLQAMGY
PTGFDTDLECMSSD
>gnl|CDD|380739 cd19910, DSRM_ILF3_rpt1, first double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and similar proteins. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. ILF3 contains an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
EPPQAMNALMRLNQLKPGLQYKLISQTGPVHAPVFTMSVEVDGKTFEASGPSKKTAKLHVAVKVLQDMGL
PTG
>gnl|CDD|380740 cd19911, DSRM_STRBP_rpt2, second double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) and similar proteins. STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. STRBP contains an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFRGAGPNKKVAKASAALAALEKLF
>gnl|CDD|380741 cd19912, DSRM_ILF3_rpt2, second double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and similar proteins. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. ILF3 contains an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
ILTKHGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGAGSNKKVAKAYAALAALEKLF
PD
>gnl|CDD|380742 cd19913, DSRM_DRADA_rpt1, first double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA). DRADA (EC 3.5.4.37; also known as 136 kDa double-stranded RNA-binding protein (p136), interferon-inducible protein 4 (IFI-4), K88DSRBP, ADAR1, G1P1, or ADAR) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. Vertebrate DRADA contains three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KNPVSGLMEYAQFLGQTCEFLLLEQSGPSHDPRFKFQAVIDGRRFPPAEASSKKVAKKDAAAIALKILLR
E
>gnl|CDD|380743 cd19914, DSRM_DRADA_rpt2, second double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) and similar proteins. DRADA (EC 3.5.4.37; also known as 136 kDa double-stranded RNA-binding protein (p136), interferon-inducible protein 4 (IFI-4), K88DSRBP, ADAR1, G1P1, or ADAR) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. Vertebrate DRADA contains three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
KNPISVLMEHSQKSGNMCEFQLLSQEGPPHDPKFTYCVKVGEQTFPSVVANSKKVAKQMAAEEAVKELMG
E
>gnl|CDD|380744 cd19915, DSRM_DRADA_rpt3, third double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) and similar proteins. DRADA (EC 3.5.4.37; also known as 136 kDa double-stranded RNA-binding protein (p136), interferon-inducible protein 4 (IFI-4), K88DSRBP, ADAR1, G1P1, or ADAR) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. Vertebrate DRADA contains three double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure
TNPVSGLLEYARSKGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWFPAVCAHNKKQGKQEAADAALRVLIG
E
>gnl|CDD|381179 cd19916, OphMA_like, tetrapyrrole methylase family protein similar to Omphalotus olearius omphalotin methyltransferase (OphMA) and Dendrothele bispora dbOphMA. OphMA, is the precursor protein of the fungal cyclic peptide Omphalotin A. Omphalotin A is a potent nematicide, having 9 out of 12 of its residues methylated at the backbone amide. Omphalotin A derives from the C-terminus of OphMA (also known as OphA). OphMA catalyzes the automethylation of its own C-terminus using S-adenosyl methionine (SAM); this C terminus is subsequently released and macrocyclized by the protease OphP to give Omphalotin A
GSLVVVGTGIKGIGHLTLEAESAIEQADKVFYLVADPLTEEWLRELNPNAEDLYDLYGEGKPRLDTYREM
AERILEAVRAGKPVCAAFYGHPGVFVSPSHLAIRIARREGYRARMLPGISAEDCLFADLGIDPGRPGCQS
YEATDFLLRRRPLDPSAHLILWQVGVVGDLTFTRFGYDNRGLELLVEYLLKFYPPDHEVILYEAATYPGC
EPRIERIPLSDLAEAELTGISTLYIPP
>gnl|CDD|381180 cd19917, RsmI_like, tetrapyrrole methylase family protein similar to ribosomal RNA small subunit methyltransferase I (RsmI). RsmI, also known as rRNA (cytidine-2'-O-)-methyltransferase, is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress
YLVATPIGNTDDITLRALETLKAVDLIICEDTRNASRLLKHVGIIGKTLEVLNEHNTPEDIQELLDKLAG
GKNVALVSDAGTPAFADPGADLVKLCRDAGIPVVPLPGASSLMTALSASGLKSDRFLFYGFLPAEPGERK
KALKALEQEPRTLIFMETPYRLKKTLEDLAAVFGPNRKVVLARNLTQEEETILTGTLGELLNKIPELPKG
EFVLLLY
>gnl|CDD|381181 cd19918, RsmI_like, uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small subunit methyltransferase I (RsmI). RsmI, also known as rRNA (cytidine-2'-O-)-methyltransferase, is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress
YIVATPIGNYDDITLRALEVLKEVDVIICEEFKEGSRLLKKLIIEKELLLLNEHNEKEDAAELLDLLAQG
KSVALISDCGTPVFADPGALLVKLCIQKGIPVVPVPGASSLMAALSVSGFKIDRFLFAGFLPRKKEERRR
ELKRLKSEKRPIVLMDTPYRLKKLLEDLAKVFGPNRRIVLAYNLTLPDEKILRGTLAEILKKVEEKPLKG
EFVLIIH
>gnl|CDD|381146 cd19919, REC_NtrC, phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC. DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRH
PDLPVIIMTAHSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI
>gnl|CDD|381147 cd19920, REC_PA4781-like, phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains. Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPAT
RHIPVIFLTALTDTEDKVKGFELGAVDYITKPF
>gnl|CDD|381148 cd19921, REC_1_GGDEF, first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins. This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the first REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
KVLIVEDSKTFSKVLKHLIAQELGLEVDVAETLAEAKALLEEGDDYFAALVDLNLPDAPNGEAVDLVLEK
GIPVIVLTGSFDEDKRETLLSKGVVDYVLKDSRYSYDYVVKLVRR
>gnl|CDD|381149 cd19922, REC_RitR-like, receiver (REC) domain of orphan response regulator RitR and similar domains. Streptococcus pneumoniae RitR (Repressor of iron transport Regulator, formerly RR489) is an orphan two-component signal transduction response regulator that is required for lung pathogenicity. It acts to repress iron uptake via binding the pneumococcal iron uptake (Piu) transporter promoter. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. However, members of this family do not contain the phosphorylatable aspartic acid residue and are phosphorylation-independent
ILLLEKERNLAHFLSLELQKEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKLSRIKPA
SVIIVLDHWEDLQEELEEVQRFAVSYVVKPVLISNLVDKI
>gnl|CDD|381150 cd19923, REC_CheY_CheY3, phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins. CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
MKVLVVDDFSTMRRIIKNLLKELGFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRAD
GALSHLPVLMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF
>gnl|CDD|381151 cd19924, REC_CheV-like, phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins. This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEGNDLSKELDLIITDIEMPKMDGYELT
FELRDDPRLANIPVILNSSLSGEFSRARGKKVGADAYLAKF
>gnl|CDD|381152 cd19925, REC_citrate_TCS, phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators. This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
INVLIVEDDPMVAEIHRAYVEQVPGFTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA
AGHDVDVIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERYR
>gnl|CDD|381153 cd19926, REC_PilR, phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR and similar proteins. Pseudomonas aeruginosa PilR is the response regulator of the PilS/PilR two-component regulatory system (PilSR TCS) that acts in conjunction with sigma-54 to regulate the expression of type 4 pilus (T4P) major subunit PilA. In addition, the PilSR TCS regulates flagellum-dependent swimming motility and pilus-dependent twitching motility. PilR contains an N-terminal REC domain, a central sigma-54 interaction domain, and a C-terminal Fis-type helix-turn-helix DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQ
TPVAVITAYGSLDTAIEALKAGAFDFLTKP
>gnl|CDD|381154 cd19927, REC_Ycf29, phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29. Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays
ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADF
DTIPVIFLTAKGMTSDRIKGYNAGCDGYLSKP
>gnl|CDD|381155 cd19928, REC_RcNtrC-like, phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators. NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPD
LPIIVMSAQNTLMTAVKAAERGAFEYLPKP
>gnl|CDD|381156 cd19929, psREC_Atg32, pseudo receiver domain of autophagy receptor Atg32. Autophagy receptor Atg32 is a single-pass outer mitochondrial membrane protein that is required for the selective autophagy of mitochondria, called mitophagy, in yeast. It mediates ubiquitin-independent mitophagy in response to nitrogen deprivation. It recruits the autophagy machinery to mitochondria, facilitating mitochondrial capture in phagophores, the precursors to autophagosomes. Whereas mammals have at least 7 different autophagy receptors, yeast only has one. Little is known about the structure of Atg32; it contains a binding region for the selective autophagy scaffolding protein Atg11 and an Atg8-interacting motif (AIM). Limited proteolysis has identified a structured domain, a pseudo receiver (psREC) domain, within the cytosolic region of Atg32 that is essential for the induction of mitophagy. psREC domains lack the metal-binding, phosphorylatable asp, and active site residues of canonical REC domains and are thought to function in protein-protein interactions
VMPKLSLSQRSQKFKILIVGRPARKFYQTIPKSYQKLFELPKLSDLNEEFQKYTAIMIIFQDLKELVSLL
NRVSQKNPKKPIIPICQKGQQQQVKNVLKSYLRNKLIRLLYPPVVMSNHRELHKLLKHLHSLSNEVESG
>gnl|CDD|381157 cd19930, REC_DesR-like, phosphoacceptor receiver (REC) domain of DesR and similar proteins. This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLIAEDQEMVRGALAALLELEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREEL
PDTKVLIVTTFGRPGYFRRALAAGVDGYVLKDRPIEELADAIRTVHA
>gnl|CDD|381158 cd19931, REC_NarL, phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL). Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VLLIDDHPLLRKGIKQLIELDPDFTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEG
VSARIVILTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAAS
>gnl|CDD|381159 cd19932, REC_PdtaR-like, phosphoacceptor receiver (REC) domain of PdtaR and similar proteins. This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
VRVLIAEDEALIRMDLREMLEEAGYEVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSE
NIAPIVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIAR
>gnl|CDD|381160 cd19933, REC_ETR-like, phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins. Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSFQLVLLDLCMPEMDGFEVALRIRK
LFGRRERPLIVALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL
>gnl|CDD|381161 cd19934, REC_OmpR_EcPhoP-like, phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators. Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRA
TPVLILTARDSWQDKVEGLDAGADDYLTKPFHIEELLARLRALIRRA
>gnl|CDD|381162 cd19935, REC_OmpR_CusR-like, phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators. Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQ
TPVLMLTARDSVEDRVKGLDLGADDYLVKP
>gnl|CDD|381163 cd19936, REC_OmpR_ChvI-like, phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators. Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKSTL
PVIFLTSKDDEIDEVFGLRMGADDYITKP
>gnl|CDD|381164 cd19937, REC_OmpR_BsPhoP-like, phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators. Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTS
SIPIIMLTAKGEEFDKVLGLELGADDYITKPFSPRELLARVKAVLR
>gnl|CDD|381165 cd19938, REC_OmpR_BaeR-like, phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators. BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSD
VPIIMVTARVEEIDRLLGLELGADDYICKPYSPREVVARVKAIL
>gnl|CDD|381166 cd19939, REC_OmpR_BfmR-like, phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators. Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays
RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSH
VPILMLTARTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALLRR
>gnl|CDD|410849 cd19940, XPF_nuclease-like, nuclease domain of XPF/MUS81 family proteins. The XPF/MUS81 family belongs to 3'-flap endonuclease that act upon 3'-flap structures and involved in DNA repair pathways that are necessary for the removal of UV-light-induced DNA lesions and cross-links between DNA strands. Family members exist either as heterodimers or as homodimers in their functionally competent states which consist of a catalytic and a noncatalytic subunit. The catalytic subunits have a DX(n)RKX(3)D motif. This motif is required for metal-dependent endonuclease activity but not for DNA junction binding. The equivalent regions of the noncatalytic subunits (ERCC1, EME1, and FAAP24) have diverged. The noncatalytic subunits have roles such as binding ssDNA or an ability to target the endonuclease to defined DNA structures or sites of DNA damage
SIVVDPRERRSELLSELQRLGVQVEFEDLAVGDYVLSNRTCVERKSLSDLVSSINKGRLREQLQRLTRKF
ERRVLLVEKDRSKFRSMVSSVQALSALTKLQLLTGIRLLIVASPKETADLLEELTQ
>gnl|CDD|410995 cd19941, TIL, trypsin inhibitor-like cysteine rich domain. TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation
CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC
>gnl|CDD|381075 cd19942, Fer2_BFD-like [2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins. The BFD-like [2Fe-2S]-binding domain comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. The Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport. BFD-like [2Fe-2S]-binding domains are found in proteins such as bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, Cu+ chaperone CopZ, anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, nitrogen fixation protein NifU, prokaryotic assimilatory nitrate reductase catalytic subunit NasA, and archaeal proline dehydrogenase PDH1. This superfamily also includes uncharacterized proteins having an N-terminal BFD-like [2Fe-2S]-binding domain and a C-terminal domain belonging to the Ni,Fe-hydrogenase I small subunit family
ALVCECFAVTEKELREAIRKGGLKTVEELLTGTGAGGGCGVCHPHVAQL
>gnl|CDD|381076 cd19943, NirB_Fer2_BFD-like_1, first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large subunit of the NADH-dependent nitrite reductase. The NADH-dependent nitrite reductase (NirBD) complex comprises a large and a small subunit, and is also known as nitrite reductase (reduced nicotinamide adenine dinucleotide), NADH-nitrite oxidoreductase, and assimilatory nitrite reductase. NirBD uses NADH as electron donor, and FAD, iron-sulfur cluster, and siroheme cofactors, all embedded in the large subunit NirB to catalyze the 6-electron reduction of nitrite to ammonium. NirBD plays a role in regulating nitric oxide homeostasis in Streptomyces coelicolor. In addition to NirB, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins including bacterioferritin-associated ferredoxin (BFD) and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport
PDDAEVCGCNGVSKGAIVQAIQEKGLTTLDEVKACTKASTSCGGCTPLVEQLL
>gnl|CDD|381077 cd19944, NirB_Fer2_BFD-like_2, second bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large subunit of the NADH-dependent nitrite reductase. The NADH-dependent nitrite reductase (NirBD) complex comprises a large (NirB) and a small (NirD) subunit, and is also known as nitrite reductase (reduced nicotinamide adenine dinucleotide), NADH-nitrite oxidoreductase, and assimilatory nitrite reductase. NirBD uses NADH as electron donor, and FAD, iron-sulfur cluster, and siroheme cofactors, all embedded in the large subunit NirB to catalyze the 6-electron reduction of nitrite to ammonium. Some of the second [2Fe-2S]-binding domains, have one of the Cys residues replaced by a His residue, they may interact with non-Rieske NirD subunits. NirBD plays a role in regulating nitric oxide homeostasis in Streptomyces coelicolor. In addition to NirB, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins including bacterioferritin-associated ferredoxin (BFD) and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport
KTLCSCTDLSHDEVREAIQEHGLTSFEEVMAALGWKTPDGCEKCRPALNYYL
>gnl|CDD|381078 cd19945, Fer2_BFD, bacterioferritin-associated ferredoxin (BFD) [2Fe-2S]-binding domain. This family includes Escherichia coli and Pseudomonas aeruginosa bacterioferritin-associated ferredoxin BFD which binds an [2Fe-2S] cluster and appears to interact with bacterioferritin (E. coli BFR/YheA and P. aeruginosa BfrB), a dynamic regulator of intracellular iron levels. It has been suggested that BFD and bacterioferritin form an electron transfer complex which may participate in the iron storage or iron immobilization functions of bacterioferritin. For Pseudomonas aeruginosa, it has been shown that mobilization of Fe3+ stored in BfrB requires interaction with BFD, which transfers electrons to reduce Fe3+ in the internal cavity of BfrB for subsequent release of Fe2+. The stability of BFD may be aided by an anion-binding site found within this domain. In addition to BFD, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins such as the large subunit of NADH-dependent nitrite reductase and the Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport
MYVCLCNGITDKQIRQAVAQGATSLRELREQLGVGSQCGKCARMARQVLEEELA
>gnl|CDD|381079 cd19946, GlpA-like_Fer2_BFD-like, bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, and similar proteins. This subgroup includes the BFD-like [2Fe-2S]-binding domains of subunits of various component dehydrogenase/oxidases, including anaerobic glycerol 3-phosphate dehydrogenase subunit A of GlpABC, hydrogen cyanide synthase subunit HcnB of HcnABC, octopine oxidase subunit A of OoxAB, and nopaline oxidase subunit A of NoxAB. GlpABC catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone, and participates in the glycerol degradation by glycerol kinase pathway in step 1 of the sub-pathway that synthesizes glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route). HcnABC oxidizes glycine producing hydrogen cyanide and CO2. In Agrobacterium spp, the first enzymic step in the catabolic utilization of octopine and nopaline is the oxidative cleavage into L-arginine and pyruvate or 2-ketoglutarate, respectively; nopaline oxidase (NoxAB) accepts nopaline and octopine while octopine oxidase (OoaB) has high activity with octopine but barely detectable activity with nopaline, both subunits possibly contributing to the substrate specificity. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport
TIVCRCEEVTEGEIRDAIRRGAARDLDGLKRRTRAGMGRCQGRFCAPRVAELLAR
>gnl|CDD|381080 cd19947, NifU_Fer2_BFD-like, bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of nitrogen fixation protein NifU and similar proteins. This family includes the BFD-like [2Fe-2S]-binding domain of Azotobacter vinelandii and Klebsiella pneumoniae nitrogen fixation protein NifU. NifU binds one Fe cation per subunit and one [2Fe-2S] cluster per subunit, and is involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport
EGAIVCKCFGVTEVMIERAIRENNLTTVEDVTNYTKAGGGCGSCHEKIEDILDRV
>gnl|CDD|381081 cd19948, NasA-like_Fer2_BFD-like, bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit NasA and similar proteins. The BFD-like [2Fe-2S]-binding domain described in this family is found at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit (NasA) such as Rhodobacter capsulatus E1F1 NasA. Nitrate reductase catalyzes the reduction of nitrate to nitrite, the first step of nitrate assimilation. R. capsulatus E1F1 nitrate reductase is composed of this NasA subunit and a small diaphorase subunit with FAD. Note that this [2Fe-2S]-binding domain is not always present; for example, it is absent from the characterized haloaechean Haloferax mediterranei NasA; both, however, have an [4Fe-4S] binding domain at their N-terminus. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport
GRTVCACFSVGENTIRRAIADNGLTSVAQVGTCLKAGTNCGSCVPEIQKLLSE
>gnl|CDD|381082 cd19949, PDH1_Fer2_BFD-like, bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the alpha-subunit of archaeal proline dehydrogenase PDH1. This domain family describes the alpha-subunit of archaeal dye-linked L-proline dehydrogenase PDH1. Dye-linked PDH catalyzes the oxidation of L-proline to 1-pyrroline-5-carboxylate in the presence of artificial electron acceptors. It includes the alpha subunit of Pyrococcus horikoshii PHD1 which has been shown to exist as an (alphabeta)4 heterooctamer and to contain three cofactors: FAD, FMN, and ATP; the alpha subunit contains ATP but exhibits no PDH activity, the beta subunit is the catalytic component contains FAD and exhibits PDH activity, and FMN is located between the alpha and beta subunits. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport
DVQICGCDVSLKKVDDVVRRGITDLQIIKRLTHLAMGFCQGRYCLFNGAVVVSQRT
>gnl|CDD|381083 cd19950, Fer2_BFD-like [2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; uncharacterized subgroup. The BFD-like [2Fe-2S]-binding domain comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. The Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport. BFD-like [2Fe-2S]-binding domains are found in proteins such as bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, Cu+ chaperone CopZ, anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, nitrogen fixation protein NifU, prokaryotic assimilatory nitrate reductase catalytic subunit NasA, and archaeal proline dehydrogenase PDH1
PTLVCTCNDLYIDDIEEAIAEGETEYEEIFAYNDTQPRCGECIDHVQEIVA
>gnl|CDD|381084 cd19951, HyaA_family_Fer2_BFD-like, bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of uncharacterized proteins having a C-terminal Ni,Fe-hydrogenase I small subunit (HyaA) family domain. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport
GRLVCSCEHVYYQDLIDIIVSCAITSFAELKEFSEAGRVCGRCKKDVDDIIAAS
>gnl|CDD|467690 cd19952, GT29, glycosyltransferase family 29. Glycosyltransferase family 29 members (also called sialyltransferases) are enzymes that transfer sialic acid to oligosaccharide, each having specificity for a certain sugar substrate
CAVVGNSGILLGSEYGKEIDSHDAVFRFNQAPTKGFEKDVGSKTTFRVLNSKWAGFYLRGPRCGCHPLPL
EEEVVLILSRAAAADFKRLKRRKKRHDNAVLLLTDPAPDLLSYVRKRLEKLGLKSFFGGNAPSSGLLAVL
LALQLCDSVDLYGFGVDSGHAPKVPYHYYDLVEAEEGTAVHSFDLEAELLRAL
>gnl|CDD|410996 cd19953, PDS5, Sister chromatid cohesion protein PDS5. Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase
LLKRLKALHEELSELDQDEVDLESLEPVAKELVSPKLLKHKDKGVRALVACCLADILRLYAPDAPYTDDQ
LKDIFKLFISQLKGLLDPDSPYFSQYFYLLESLAEVKSIVLLLDLPDADELILELFKTFFDLVRDDHPKN
VENLMLDILVELIDESESVPQEVLDIILAQFLKKNKSENPPAYRLAVEVCERCSDKLQRYVTQFFSEVLV
DASTEEDSEEDSEELEKAHELIYELWRIAPELLLSVIPQLEEELKADDVDVRLLATKLLGKMFAEKGSAG
FAQTYPSLWKEFLGRFNDKSPEVRLAWVESAKHILLNHPDLAEDILEALKKRLLDPDEKVRLAAVKAICD
LAYEDLLHKVPEELLSTLAERLRDKKASVRKEALQGLARLYKVAYGEIEEGDETAIKQFGWIPSKILHLY
YINDPEINLLVERVLFEYLLPLSLDDEERVKRLLLLFSSLDDKAKKAFFAILKRQQRLRKELQKYLDLCE
KYNGGVIEDEEEVEKKLEKLIKWLSASFPDPLKAEEDLQKFAKLNDRRIYKLLKTCLDPETDYKTVRKAR
KELLKRLGDPSKASLLETLKILLYRSSPLIFNKSNVPALLKILKSSDGSDNEKLASAALELLLEISKVFP
>gnl|CDD|381070 cd19954, serpin42Dd-like_insects, insect serpins similar to Drosophila melanogaster Serpin 42Dd. Serpins in insects function within development, wound healing and immunity. Drosophila melanogaster Serpin 42Dd, also called serpin 1 (Spn1), regulates Toll-mediated immune responses, functioning as a repressor of Toll activation upon fungal infection. Insect serpins from house flies, fruit flies, and stable flies are included in this subfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
AVSNLFASELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDKEEVAKKYKEL
LQKLEQREGATLKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIK
DLVTPSDLDPDTKALLVNAIYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDAT
AIELPYANSNLSMLIILPNEVDGLAKLEQKLKELDLNELTERLQMEEVTLKLPKFKIEFDLDLKEPLKKL
GINEIFTDSADFSGLLAKSGLKISKVLHKAFIEVNEAGTEAAAATVSKIVPLSLPKDVKEFTADHPFVFA
IRDEEAIYFAGHVVNP
>gnl|CDD|381071 cd19955, serpin48-like_insects, insect serpins similar to Tenebrio molitor serpin 48. Serpins in insects function within development, wound healing and immunity. Tenebrio molitor serpin 48 (SPN48) is highly specific for Spatzle-processing enzyme, an essential component in insect innate immunity. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
GNNKFTASVYKEIAKTEGGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLPSSKEKIEEAYKSLLPK
LKNSEGYTLHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEKINKWVEEQTNNKIKNLI
SPEALNDRTRLVLVNALYFKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMHLSEQYFNYYESKELNAKFL
ELPFEGQDASMVIVLPNEKDGLAQLEAQIDQVLRPHNFTPERVNVSLPKFRIESTIDFKEILQKLGVKKA
FNDEEADLSGIAGKKGDLYISKVVQKTFINVTEDGVEAAAATAVLVALPSSGPPSSPKEFKADHPFIFYI
KIKGVILFVGR
>gnl|CDD|381072 cd19956, serpinB, serpin B family, ov-serpins. The clade B of the serpin superfamily corresponds to the ovalbumin family of serpins (ov-serpins), a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). Family members are also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
ANTEFALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNKVTESGNQCEKPGGV
HSGFQALLSEINKPSTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPEEARKQINSWV
ESQTEGKIKNLLPPGSIDSSTKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKL
GYIEELNAQVLELPYAGKELSMIILLPDDIEDLSKLEKELTYEKLTEWTSPENMKETEVEVYLPRFKLEE
SYDLKSVLESLGMTDAFDEGKADFSGMSSAGDLVLSKVVHKSFVEVNEEGTEAAAATGAVIVERSLPIPE
EFKADHPFLFFIRHNKTNSILFFGRF
>gnl|CDD|381073 cd19957, serpinA, serpin family A. The clade A of the serpin superfamily includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans
ANSDFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFNLTETPEAEIHEGFQH
LLQTLNQPKKELQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEEAKKQINDYVKKKTHGK
IVDLVKDLDPDTVMVLVNYIFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRELSCT
VLQLPYKGNASMLFILPDEGKMEQVEEALSPETLERWNRSLRKSQVELYLPKFSISGSYKLEDILPQMGI
SDLFTNQADLSGISEQSNLKVSKVVHKAVLDVDEKGTEAAAATGVEITPRSLPPTIKFNRPFLLLIYEET
TGSILFLGKVVNP
>gnl|CDD|410997 cd19958, pyocin_knob, knob domain of R1 and R2 pyocins and similar domains. The knob domain is present as a tandemly repeated structural domain in R-type pyocins, which are high-molecular weight bacteriocins produced by some strains of Pseudomonas aeruginosa to specifically kill other strains of the same species. R-type pyocins are structurally similar to simple contractile tails, such as those of phage P2 and Mu, and they punch a hole in the bacterial envelope to efficiently kill target cells. The second knob domain may contain regions responsible for determining the killing spectrum. Knob-like domains occur in host-recognition and binding proteins of, not only pyocins, but also phages, such as in phage K1F endosialidase (not represented by this model), where it may interact with sialic acid, the cell surface molecule that is recognized during infection
AGTLLGTTDLNTLTTPGFYYQSANANATTALNYPVAGAGYLEVYRYGGGGVTQIYTPYNSGRIYVRTRYN
GTWSAWKEIA
>gnl|CDD|467843 cd19959, paratox, Streptococcus prophage gene product paratox and similar proteins. Paratox (Prx), the product of a Streptococcus prophage gene, binds to the competence regulator ComR and prevents the ComR-XIP complex from interacting with DNA
LTLDEFKEAIDKGFITGDTVMVVRRNGKIFDYVLPGEPVRPNEVVSVESLEDVLKELF
>gnl|CDD|410999 cd19960, YidC_peri, periplasmic beta-super sandwich fold domain of membrane protein insertase YidC from Gram-negative bacteria and similar domains. Membrane protein insertase YidC, also called foldase YidC or membrane integrase YidC, facilitates proper folding, insertion, and assembly of inner membrane proteins and complexes. Depending on the nature of the substrate, YidC functions in a Sec-independent (YidC only) or a Sec-dependent manner as part of a complex containing YidC, the SecYEG channel, and SecDFYajC. YidC belongs to the YidC/Oxa1/Alb3 protein family of insertases that contains a core domain of five transmembrane (TM) segments that is essential to insertase function. In addition to this core transmembrane domain, YidC from Gram-negative bacteria contain an extra transmembrane segment (TM1) at the N-terminus and a large periplasmic domain, located between TM1 and TM2, that adopts a beta-super sandwich fold that is found in sugar-binding proteins such as galactose mutarotase. This periplasmic domain may have a role in protein assembly: a region of YidC that binds to SecF maps to one edge of the beta-super sandwich. Other members of the YidC/Oxa1/Alb3 family include YidC1/YidC2 from gram-positive bacteria as well as eukaryotic members such as mitochondrial Oxa1/Oxa2 (or Cox18) and chloroplastic Alb3/Alb4; they are not part of this hierarchy as they do not possess the periplasmic domain
IIATVKSKDFELTIDTLGRISQFYLKDKKYKNEDGKQLELISPQAPKPLEIRFSDPALNEEAFKTPYTAS
VSEIDLESGPQSVVLTQTLSGLTVTKTITFYPDGHYDVKVKLSKPVDYFITPGQRPNAAVDSYTVHGALV
KTADGTITIIEDGDAEGTESFSNVNIAASFDRYYATLFYNFDKGLNVVVTKDASDNPLVFVKGNGNFSLH
GYIGPKEYKLLKSIDPELTDVIE
>gnl|CDD|411000 cd19961, EcYidC-like_peri, periplasmic beta-super sandwich fold domain of membrane protein insertase YidC from Escherichia coli and similar domains. This subfamily is composed of Escherichia coli YidC and similar proteins. Membrane protein insertase YidC, also called foldase YidC or membrane integrase YidC, facilitates proper folding, insertion, and assembly of inner membrane proteins and complexes. Depending on the nature of the substrate, YidC functions in a Sec-independent (YidC only) or a Sec-dependent manner as part of a complex containing YidC, the SecYEG channel, and SecDFYajC. YidC belongs to the YidC/Oxa1/Alb3 protein family of insertases that contain a core domain of five transmembrane (TM) segments that is essential to insertase function. In addition to this core transmembrane domain, YidC from Gram-negative bacteria contain an extra transmembrane segment (TM1) at the N-terminus and a large periplasmic domain, located between TM1 and TM2, that adopts a beta-super sandwich fold that is found in sugar-binding proteins such as galactose mutarotase. This periplasmic domain may have a role in protein assembly: a region of YidC that binds to SecF maps to one edge of the beta-super sandwich
KRITVETDLLKASISTKGGRIKSVELKKYKETLPDSKPVELLSPDGPYVAQLGLIGADGPLIPTADLLFT
ADSGSYEGGDSLTVTLTWTNGDGLTIEKTYTFDPDSYLIDVEVRVENNSSAPLSLSLYLQLQRKGGEPEG
SGSTITYEGPAGTEDGKLEKLSFKDLEEEKLSSGKVGWVAFKQKYFLSALIPDQGFFYSAKLSGKDDGDG
VKLLSAALTLPPGGSGTFSFRLYAGPKDYDILKAYGPGLELAVDF
>gnl|CDD|380617 cd19962, PBP1_ABC_RfuA-like, periplasmic riboflavin-binding component (RfuA) of ABC transporter (RfuABCD) from Treponema pallidum and its close homologs in other bacteria. This group includes the basic membrane lipoprotein (BMP) family ABC transporter substrate-binding protein RfuA from Treponema pallidum and its close homologs in other bacteria. RfuA is the riboflavin-binding component of ABC transporter (RfuABCD) in spirochetes. The members of this group are highly similar to that of the periplasmic binding domain of basic membrane lipoprotein (BMP), PnrA. The PnrA lipoprotein, also known as Tp0319 or TmpC, represents a novel family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC) transport system (pnrABCDE). It shows a striking structural similarity to another basic membrane lipoprotein Med which regulates the competence transcription factor gene, comK, in Bacillus subtilis. PnrA-like proteins are likely to have similar nucleoside-binding functions and a similar type 1 periplasmic sugar-binding protein-like fold
KVAVFVPGNVGDSPYYEMLVLGVTRAAEKYGLSLQVIEAGNNPAKWAPTLDDLAATGGYDLIVSSNPQLP
ELVEQAARQFPEQKFLLLDAYYDGGCENVYSITYRQTEQAYLAGYLAGLVTKSAGERANADKRIGLLAGQ
DYPVMTQEIRPGYLAGARAVDPQIEVDFRVVGSWYDPAKGKDLAAGMFDQGVDIILTIAGGTNQGVIEAA
AAGNAYVIGNDSNGYDRAPGLIVGSTLETQETAAYEETLRLISGELLVGSTRSLGVKEGINRFVESDEYK
LYVPEDIRQEIAGILQAIQAGTLTI
>gnl|CDD|380618 cd19963, PBP1_BMP-like, periplasmic binding component of a basic membrane lipoprotein (BMP) from Brucella abortus and its close homologs in other bacteria. Periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and various putative lipoproteins from other bacteria. These outer membrane proteins include Med, a cell-surface localized protein regulating the competence transcription factor gene comK in Bacillus subtilis, and PnrA, a periplasmic purine nucleoside binding protein of an ATP-binding cassette (ABC) transport system in Treponema pallidum. All contain the type 1 periplasmic sugar-binding protein-like fold
KVGFIYVGPVGDGGWTQAHDEGRLAVEKEGDKVETIYVENVPEGADAERVIEELIAQGAKLIFGTSFGYM
DPMLKVAKKYPDVAFEHASGYKTAPNLGTYFGRIYEARYLAGIAAGLMTKSNKIGYVAAFPIPEVIRGIN
AFALGARSVNPDATVKVVWTNSWFDPAKEREAANALIDQGADVITQHQDSPAVVQVAEERGVYSIGYNSD
MSKFAPKAYLTSVVWNWGPYYTDIVKAVLDGTWKPGDYWGGLKEGAVDLAPLGPAVPAEVKAAVEAAKA
>gnl|CDD|380619 cd19964, PBP1_BMP-like, periplasmic binding component of a basic membrane lipoprotein (BMP) from Aeropyrum pernix K1 and its close homologs in other bacteria. Periplasmic binding component of a family of basic membrane lipoproteins from Aeropyrum pernix K1 and various putative lipoproteins from other bacteria. These outer membrane proteins include Med, a cell-surface localized protein regulating the competence transcription factor gene comK in Bacillus subtilis, and PnrA, a periplasmic purine nucleoside binding protein of an ATP-binding cassette (ABC) transport system in Treponema pallidum. All contain the type 1 periplasmic sugar-binding protein-like fold
KVALVTPGPLGDKSFNDSAAAGLKKLAEELGVEIKVIEAGDASKYEEQLRAAAEAGYDVIVATGDDLADA
LEKVAPEYPDQKFILLDTDIDEKLPNVASVSFDQNEGSYLAGVVAALMTKTGVVGFVGGMDIPVINDFLA
GYEAGAKYVNPDIKVIVSYVGSFTDPAKGKELALALYNQGADVIFQVAGGSGLGVIEAAAEAGKYAIGVD
SDQNDIYPGVILTSALKDVDNAVYDAVKDVLDGTFKGGVVSLGLKEGGVGLAI
>gnl|CDD|380620 cd19965, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
KFVFVTHVTTNPFFQPVKKGMDDACELLGAECQFTGPQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAF
DEVIKRALDAGIPVVAFNVDAPGGENARLAFVGQDLYPAGYVLGKRIAEKFKPGGGHVLLGISTPGQSAL
EQRLDGIKQALKEYGRGITYDVIDTGTDLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLK
GKVLVGGFDLVPEVLQGIKAGYIDFTIDQQPYLQGFYPVMQLFLYKKFGLSPFDIDTGAAVV
>gnl|CDD|380621 cd19966, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
KIYFIPGGAPGDPFWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGA
YTPLIEAAKKAGIIVTSFNTDLPKLEYGDCGLGYVGADLYAAGYTLAKELVKRGGLKTGDRVFVPGLLPG
QPYRVLRTKGVIDALKEAGIKVDYLEISLEPNKPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLK
AAGKKPGEIPVAGFDLSPATVQAIKSGYVNATIDQQPYLQGYLPVLQIYLTKKYGFSGLDIDTGGGYV
>gnl|CDD|380622 cd19967, PBP1_TmRBP-like, D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP). Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability
LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASI
AAVKKAKDAGIPVFLIDREINAEGVAVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVELLGKESDTNAQLR
SQGFHSVIDQYPELKMVAQQSADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRAGDV
IIVGFDGSNDVRDAIKEGKISATVLQPAKLIARLAVEQADQYLKGGSTGKEEKQLFDCVLIT
>gnl|CDD|380623 cd19968, PBP1_ABC_IbpA-like, periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins. The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge
KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALV
PAIEAAIKAGIPVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRT
KGFHEELAAGPKIKVVFEQTGNFERDEGLTVMENILTSLPGPPDAIICANDDMALGAIEAMRAAGLDLKK
VKVIGFDAVPDALQAIKDGELYATVEQPPGGQARTALRILVDYLKDKKAPKKVNLKPKLIT
>gnl|CDD|380624 cd19969, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate binding protein. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
YYVMVTFKSGHPYWDDVKEGFEDAGAELGVKTEYTGPATADVNEQITAIEQAIAKNPDGIAVSAIDPEAL
TPTINKAVDAGIPVVTFDSDAPESKRISYVGTDNYEAGYAAAEKLAELLGGKGKVAVLTGPGQPNHEERV
EGFKEAFAEYPGIEVVAVGDDNDDPEKAAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTGKVK
IVAFDDDPETLDLIKDGVIDASIAQRPWMMGYWSLQFLYDLANGLVKDAWQTAGVNPLPPYVDTGITI
>gnl|CDD|380625 cd19970, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate-binding protein. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
KVALVMKSLANEFFIEMEKGARKHAKEANGYELLVKGIKQETDIEQQIAIVENLIAQKVDAIVIAPADSK
ALVPVLKKAVDAGIAVINIDNRLDADALKEGGINVPFVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEGIP
GADNAQQRKAGFLKAFEEAGMKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDA
AGKAGKVLVVGFDNIPAVRPLLKDGKMLATIDQHPAKQAVYGIEYALKMLNGEEVPGWVKTPVEL
>gnl|CDD|380626 cd19971, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate-binding protein. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIR
PALEAAKEAGIPVINVDTPVKDTDLVDSTIASDNYNAGKLCGEDMVKKLPEGAKIAVLDHPTAESCVDRI
DGFLDAIKKNPKFEVVAQQDGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKLGDIL
VYGVDGSPDAKAAIKDGKMTATAAQSPIEIGKKAVETAYKILNGEKVEKEIVVPTFL
>gnl|CDD|380627 cd19972, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate-binding protein. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAA
VPVKAARAAGIPVIAVDRNPEDAPGDTFIATDSVAAAKELGEWVIKQTGGKGEIAILHGQLGTTPEVDRT
KGFQEALAEAPGIKVVAEQTADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDHKIW
VVGFDGDVAGLKAVKDGVLDATMTQQTQKMGRLAVDSAIDLLNGKAVPKEQLQDAVLTT
>gnl|CDD|380628 cd19973, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate-binding protein. Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins
TIGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKA
IVPAVKKARDAGVLVIALDTPTDPIDAADATFATDNFKAGVLIGEWAKAALGAKDAKIATLDLTPGHTVG
VLRHQGFLKGFGIDEKDPESNEDEDDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGA
YQALKAAGKEKGVLIVSVDGGCPGVKDVKDGIIGATSQQYPLRMAALGVEAIAAFAKTGGTKGSGFTDTG
VTLVT
>gnl|CDD|380629 cd19974, PBP1_LacI-like, ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
NIAVLIPERFFGDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILGEISK
EYLEKLKELGIPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFVGDINYTSSFMDRYLGY
RKALLEAGLPPEKEEWLLEDRDDGYGLTEEIELPLKLMLPTAFVCANDSIAIQLIKALKEKGYRVPEDIS
VVGFDNIELAELSTPPLTTVEVDKEAMGRRAVEQLLWRIENPDRPFEKILVSGKLIERDS
>gnl|CDD|380630 cd19975, PBP1_CcpA-like, ligand-binding domain of putative DNA transcription regulators highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation. This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators
TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEEN
KQLLKNMNIPVVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDDPNAGYPRYEGYK
KALKDAGLPIKENLIVEGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISV
IGFDNTEIAEMSIPPLTTVSQPFYEMGKKAVELLLDLIKNEKKEEKSIVLPHQIIERES
>gnl|CDD|380631 cd19976, PBP1_DegA_Like, ligand-binding domain of putative DNA transcription regulators highly similar to that of the transcription regulator DegA. This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the transcription regulator DegA, which is involved in the control of degradation of Bacillus subtilis amidophosphoribosyltransferase (purF). This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding
TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEA
IIKLLKEEKIPVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYK
NALQDHNLPIDESWIYSGESSLEGGYKAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVI
GFDNIILSEYITPALTTIAQPIFEMGQEAAKLLLKIIKNPAKKKEEIVLPPELIKRDS
>gnl|CDD|380632 cd19977, PBP1_EndR-like, periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its close homologs. This group includes the ligand-binding domain of putative repressor of the endoglucanase operon from Paenibacillus polymyxa and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding
TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDL
IEKLVKSGIPVVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKA
ALADHGLPVDEELIKHVDRQDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIG
FDDIPWADLFNPPLTVIAQPTYEIGRKAAELLLDRIENKPKGPPRQIVLPTELI
>gnl|CDD|380633 cd19978, PBP1_ABC_ligand_binding-like, periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally, however
IRLGMSAALSGPAAELGNEMKRGIEAAFNEVNAQGGVNGRKIKLIALDDGYEPDRTVKNTKKLIEEDKVF
ALIGYVGTPTALAALPLANEKKIPLFGPFTGAEFLRTPFLPYVFNLRASYADETEALVDYLVKTLGPKRI
AIFYQNDAFGLAGLEGAKKALKKRGLTPVAEGSYTRNTLDVEEALAKILKAKPEAIILVGTYAPAAEFIR
LARAAGLNPLFANVSFVGSEALALELGDYGEGVIVSQVVPDPNDSSLPIVKEYREAMKKYGPNAPPDFVS
LEGYLAARLLVEALKKAGPPLTREKLLALEESLKNDLGKGLTLTFSPNDHQGSDKVWLTTL
>gnl|CDD|380634 cd19979, PBP1_ABC_ligand_binding-like, amino acid amide ABC transporter substrate binding protein haat family. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters, such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally
VIGLDADLSGGSAASGEAIKRGIQLAIDEINAAGGLLGRKLELVAKDHRGNPARGVDNLREFAADPDVLA
VFGGLHSPVLLAELDFIHELKIPYLVPWAAATPITRNGYSPNYIFRLSVDDSLAGPFLVEYALKKGCKRP
ALLLENTGWGRSNLKAMTKALAKKGLQPVGVEWFNWGDTDAKPQLRALKAAGADAILLVANAPEGAAIVK
ALAALPERLPIISHWGITGGDFPELPREALSKIDLRFIQTFSFFDANQSPRGKQVLARYKRRYPVEDPES
DIPAPVGFAHAYDLTHLLALAIEQAGSTDRAAVRAALELLPPHEGLIKTYKPPFTPERHEALNESDFCMA
>gnl|CDD|380635 cd19980, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally
KIGVIAPLSGPVAALGQQVLNGAKLAVEEINAKGGVLGRKLELVVEDDKCPPAEGVAAAKKLITDDKVPA
IIGAWCSSVTLAVMPVAERAKVPLVVEISSAPKITEGGNPYVFRLNPTNSMLAKAFAKYLADKGKPKKVA
FLAENDDYGRGAAEAFKKALKAKGVKVVATEYFDQGQTDFTTQLTKLKAANPDAIFVVAETEDGALILKQ
ARELGLKQQLVGTGGTTSPDLIKLAGDAAEGVYGASIYAPTADNPANKAFVAAYKKKYGEPPDKFAALGY
DAVMVIAEAIKKAGSTDPEKIRAAALKKVDYKGPGGTIKFDEKGQAHKNVVLVQ
>gnl|CDD|380636 cd19981, PBP1_ABC_HAAT-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally
KIGFFAPLTGPAAADGKSALHGAELAVEQINAAGGINGKKVELVVYDDQASPKQAVNIAQKLIEQDKVVA
VVSGSYSGPTRAAAPIFQEAKVPMVSAYAVHPDITKAGDYVFRVAFLGPVQGRAGAEYAVKDLGAKKVAI
LTIDNDFGKSLAAGFKEEAKKLGAEIVSEYAYALGDRDFRPILTKIKSANPDAIYASGYYAEAAPIVKQA
RELGIKVPIIGQEGYDSPKFIEIAGSAAEGVIITTSLNRDSDRPITQKFIKEYRKRYGIDPDMVAASTYD
AVMVLAGEVQKPVQVQI
>gnl|CDD|380637 cd19982, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, their ligand specificity has not been determined experimentally
KIGAILSLTGPFAPFGEMFKNGYEMALEEINAAGGIKGKKLELVIEDDQSKPQTALAAAEKLVSQDKVPL
IVGGYSSGITLPVAAVAERQKIPLLVPTAADDDITKPGYKYVFRLNPPASIYAKALFDFFKELVKPKTIA
ILYENTAFGTSVAKAARRFAKKRGIEVVADESYDKGATDFKPLLNKVKAANPDVVYMVSYLNDAILLMRQ
AKELGLNPKLFAGGGAGFTIPEFLKQAGPLAEYVVTATLWSPDVKYPGAKEFYEKYKAKYGVEPSYHEAE
AYAALYVAANQNPHPTLVLQVQ
>gnl|CDD|380638 cd19983, PBP1_ABC_HAAT-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of hydrophobic amino acids or peptides. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of hydrophobic amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally
RIGFVGGLTGRYSDLGVQGRNGAQLAVEEINAAGGINGRPVELIIRDDQQDPEAAKAADRELIAGGVVAI
IGHMTSAMTVAVLPVINEAKVLMISPTVSTPELSGKDDYFFRVTPTTRESAQALARYAYNRGGLRRVAVI
YDLSNRAYSESWLDNFRSEFEALGGRIVAEIPFSSGADVDFSDLARRLLASKPDGLLLVASAVDTAMLAQ
QIRKLGSKIPLFSSAWAATEELLELGGKAVEGMLFSQAYDRNSSNPRYLAFKEAYEERFGREPSFAAAYA
YEAAMVLAGDVSRPVFIVTVRNG
>gnl|CDD|380639 cd19984, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally
KIGVILPLTGDAASYGEDMKNGIELAVEEINAAGGINGKKIELIYEDSKCDPKKAVSAANKLINVDKVKA
IIGGVCSSETLAIAPIAEQNKVVLISPGASSPEITKAGDYIFRNYPSDAYQGKVLAEFAYNKLYKKVAIL
YENNDYGVGLKDVFKKEFEELGGKIVASESFEQGETDFRTQLTKIKAANPDAIFLPGYPKEGGLILKQAK
ELGIKAPILGSDGFEDPELLEIAGEAAEGVIFTYPAFDDSSEKKQKFFFYRYKEKYGKEPDIYAALAYDA
VMILAGDVVKPYVIKT
>gnl|CDD|380640 cd19985, PBP1_ABC_HAAT-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of hydrophobic amino acids or peptides. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of hydrophobic amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally
HIAVVGPMSGKSASKGKSMLRGAELYIDQINAAGGINGKKVKLDVFDDQNDPDAARKAAQIIVSDKALAV
IGHYYSSASIAAGKIYKKAGIPAITPSATADAVTRDNPWYFRVIFNDSLQGRFLANYAKKVLKKDKVSII
YEEDSYGKSLASVFEATARALGLKVLKKWSFDTDSSQLDQNLDQIVDELKKAPDEPGVIFLATHADEGAK
LIKKLRDAGLKAPIIGPDSLASESFAQGFAEYPEEKEEPGYYTDGIYATSPFIFDIANEKAQKFRDTYQK
RYGEEPSWIAAFAYDAAMLAIGNIYFDSNGDAVKPVAIGVY
>gnl|CDD|380641 cd19986, PBP1_ABC_HAAT-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally
KIGVVAPLTGPAALNGEYQKNGAQLALEEINAAGGVLGRPLELVVEDDQGTNTGAVNAVNKLISDDKVVA
VIGPHYSTQVLAVSPLVKEAKIPVITGGTSPKLTEQGNPYMFRIRPSDSVSAKALAKYAVEELGAKKIAI
LYDNDDFGTGGADVVTAALKALGLEPVAVESYNTGDKDFTAQLLKLKNSGADVIIAWGHDAEAALIARQI
RQLGLDVPVIGSSSFATPTVLLLAGEALEGIYSVTDFVPSDPDPKVQAFVKKYKAKYGEDPDLYSAWYYD
AMYLLAGDGVHEVNIVQ
>gnl|CDD|380642 cd19987, PBP1_SBP-like, periplasmic substrate-binding domain of active transport proteins. Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids
TIGLNVPLSGPYAPQGEDQRRGFELAVDHLNNGGGLVDKDSRLSGDGILGKKVELVTADTETKADTAVDN
AKRLIEQDGAVMITGGSSSAVAVAAQKLAQKEGVLYFAGLSHSNDTTGKDCHRYGFRECFNAHMSAKALA
PYLVEKFGKDRKYFYLTADYTWGHSTEQSMREYTEAHGWKTVGNPATPLGETDFSAALLNAADSGADVLV
LVLFGRDMVNALKQAKQFGLLKKMDIVVPLLTAFMAESVGPEIMEGVLGTVNWHWSLPDDYSYAFGKAEA
FEKEYGAYPSQAAASAYVQVLQYAAAVERAGSFDPPAVIRALEGHEYTLLKGEQYWRACDHQSVRPVYVV
RGK
>gnl|CDD|380643 cd19988, PBP1_ABC_HAAT-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally
KIGVFGPLSGDAAPYGQAMLQGAELAVEEINAAGGILGIPIELVVEDDEGLPAASVSAAKKLIYQDKVWA
IIGSINSSCTLAAIRVALKAGVPQINPGSSAPTITESGNPWVFRCTPDDRQQAYALVDYAFEKLKVTKIA
VLYVNDDYGRGGIDAFKDAAKKYGIEVVVEESYNRGDKDFSPQLEKIKDSGAQAIVMWGQYTEGALIAKQ
ARELGLKQPLFGSDGLVTPKFIELAGDAAEGAIATTPFLPDSDDPKVSAFVEKYKKRYGEEPDVFAAQAY
DAMNILAGDNVGPVVLAKVENG
>gnl|CDD|380644 cd19989, PBP1_SBP-like, periplasmic substrate-binding domain of active transport proteins. Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids
KIGVLTPLSGPYAALGEEARRGAQLAVEEINAAGGILGRPVELVVEDTEGKPATAVQKARKLVEQDGVDF
LTGAVSSAVALAVAPKAAELKVPYLVTVAADDELTGENCNRYTFRVNTSDRMIARALAPWLAENGGKKWY
IVYADYAWGQSSAEAFKEAIEELGGEVVGTLFAPLGTTDFSSYITQISDSGADGLLLALAGSDAVNFLKQ
AGQFGLGKKYKIVGGILSIEPLALPALGDAAEGVYGGVRYPPTLDTPANRAFVEAYEKEYGEAPDNFAGE
AYEAMQALAHQAVQPGYIG
>gnl|CDD|380645 cd19990, PBP1_GABAb_receptor_plant, periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close homologs in other plants. This group includes the ligand-binding domain of Arabidopsis thaliana glutamate receptors, which have sequence similarity with animal ionotropic glutamate receptor and its close homologs in other plants. The ligand-binding domain of GABAb receptors are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb receptor or GABAbR). GABAa receptors are members of the ionotropic receptor superfamily which includes alpha-adrenergic and glycine receptors. The GABAb receptor is a member of a receptor superfamily which includes the mGlu receptors. The GABAb receptor is coupled to G alpha-i proteins, and activation causes a decrease in calcium, an increase in potassium membrane conductance, and inhibition of cAMP formation. The response is thus inhibitory and leads to hyperpolarization and decreased neurotransmitter release, for example
KIGAILDLNSRVGKEAKVAIEMAVSDFNSDSSSYGTKLVLHVRDSKGDPLQAASAALDLIKNKKVEAIIG
PQTSEEASFVAELGNKAQVPIISFSATSPTLSSLRWPFFIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYE
DDDYGSGIIPYLSDALQEVGSRIEYRVALPPSSPEDSIEEELIKLKSMQSRVFVVHMSSLLASRLFQEAK
KLGMMEKGYVWIVTDGITNLLDSLDSSTISSMQGVIGIKTYIPESSEFQDFKARFRKKFRSEYPEEENAE
PNIYALRAYDAIWALAHAVEKLNSSGGNISVSDSGKKLLEEILSTKFKGLSGEVQFVDGQLAPPPAFEIV
NVIGKGYRELGFWSPGSGFSEVL
>gnl|CDD|380646 cd19991, PBP1_ABC_xylose_binding, D-xylose binding periplasmic protein. Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR
KIGFSMDSLRVERWQRDRDYFVKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALA
PIVKEAKKAGVPVLAYDRLILNADVDLYVSFDNEKVGELQAEALVKAKPKGNYVLLGGSPTDNNAKLFRE
GQMKVLQPLIDSGDIKVVGDQWVDDWDPEEALKIMENALTANNNKIDAVIASNDGTAGGAIQALAEQGLA
GKVAVSGQDADLAACQRIVEGTQTMTIYKPIKELAEKAAELAVALAKGEKNEANRTINNGKKEVPSILLD
PIAV
>gnl|CDD|380647 cd19992, PBP1_ABC_xylose_binding-like, periplasmic xylose-like sugar-binding component of the ABC-type transport systems. Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR
KIGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAA
NIVDKAKAAGVPVISYDRLILNADVDLYVGRDNYKVGQLQAEYALEAVPKGNYVILSGDPGDNNAQLITA
GAMDVLQPAIDSGDIKIVLDQYVKGWSPDEAMKLVENALTANNNNIDAVLAPNDGMAGGAIQALKAQGLA
GKVFVTGQDAELAALKRIVEGTQTMTVWKDLKELARAAADAAVKLAKGEKPQTTDETINNGGKDVPAILI
PGVL
>gnl|CDD|380648 cd19993, PBP1_ABC_xylose_binding-like, periplasmic xylose-like sugar-binding component of the ABC-type transport systems. Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR
VVGVSWSNFQEERWKTDEAAMKKALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAIL
PAVEKAAAEGIPVIAYDRLIENPIAFYISFDNVEVGRMQARGVLKAKPEGNYVFIKGSPTDPNADFLRAG
QMEVLQPAIDSGKIKIVGEQYTDGWKPANAQKNMEQILTANNNKVDAVVASNDGTAGGAVAALAAQGLAG
KVPVSGQDADKAALNRIALGTQTVTVWKDARELGKEAAEIAVELAKGTKIEAIKGAALTNDGPKKVAVPS
IFLKPIA
>gnl|CDD|380649 cd19994, PBP1_ChvE, periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling system. Periplasmic aldose-monosaccharides binding protein ChvE that belongs to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR
KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALG
DVLEEAKDAGIPVIAYDRLIMNTDAVDYYVTFDNEKVGELQGQYLVDKLGLKDGKGPFNIELFAGSPDDN
NAQLFFKGAMEVLQPYIDDGTLVVRSGQTTFEQVATPDWDTETAQARMETLLSAYYTGGKKLDAVLSPND
GIARGVIEALKAAGYDTGPWPVVTGQDAEDASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEVE
VNDTKTYDNGVKVVPSYLLDPVIV
>gnl|CDD|380650 cd19995, PBP1_ABC_xylose_binding-like, periplasmic xylose-like sugar-binding component of the ABC-type transport systems. Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR
KVAFLLPDTTSARWEQQDAPGFEKAMKKLCPDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSN
AAAGIVAKAAQAGVPVIAYDRLILGGPADYYVSFDNVAVGEAQAQSLVDHLKAIGKKGVNIVMINGSPTD
NNAGLFKKGAHEVLDPLGDSGELKLVCEYDTPDWDPANAQTAMEQALTKLGNNIDGVLSANDGLAGGAIA
ALKAQGLAGKVPVTGQDATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVAVALLKGETPPSDLVTGTVTN
GGDKVPAVLLPPVV
>gnl|CDD|380651 cd19996, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate binding protein such as CUT2. Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail
TIGFSNAGLGNSWRVQMIAEFEAEAAKLKKLIKELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPT
ALLPAIEKAAAAGIPVVLFDSGVGSDKYTAFVGVDDAAFGRVGAEWLVKQLGGKGNIIALRGIAGVSVSE
DRWAGAKEVFKEYPGIKIVGEVYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPL
VPMTGEDNNGFLKAWKELPGFKSIAPSYPPWLGATALDAALAALEGEPVPKYVYIPLPVITDENLDQYVK
PDLDDPWWPDTLLSDELLKKLG
>gnl|CDD|380652 cd19997, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate binding protein such as CUT2. Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail
VIALSNSYAGNTWRQQMVDAFEEAAKKAKADGLIADYIVVNADGSATTQISQIQNLILQGVDAIVIDAAS
PTALNGAIQQACDAGIKVVVFDSGVTEPCAYILNNDFEDYGAASVEYVADRLGGKGNVLEVRGVAGTSPD
EEIYAGQVEALKKYPDLKVVAEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGGDGYGAAQAFEAAGRPL
PIIIGGNRGEFLKWWQEEYAKNGYETVSVSTDPGQGSAAFWVALDILNGKDVPKEMILPVVTITEDDLDA
WLAVTPDGIVAPTYYTEWVVSNLID
>gnl|CDD|380653 cd19998, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate binding protein such as CUT2. Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail
KIALSNSYSGNDWRQEMINIAKAAAKQPPYADKVELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISP
TALNPVIKRACDAGIVVVAFDNVVDEPCAYNVNTDQAKAGEQTAQWLVDKLGGKGNILMVRGVPGTSVDR
DRYEGAKEVFKKYPDIKVVAEYYGNWDDGTAQKAVADALAAHPDVDGVWTQGGETGVIKALQAAGHPLVP
VGGEAENGFRKAMLEPLANGLPGISAGSPPALSAVALKLAVAVLEGEKEPKTIELPLPWVTTDDVKLCQG
GFPDLPKNGFTVNDFPSCFPGF
>gnl|CDD|380654 cd19999, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate binding protein such as CUT2. Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail
VIGVSNGYVGNEWRAQMIADFEEVAAEYKEEGVISDLIVQNADADATGQISQIRNMINEGVDAILIDPVS
ATALNPVIEKAQAAGILVVSFDQPVSSPDAINVVIDQYKWAAIQAQWLAEQLGGKGNIVAINGVAGNPAN
EARVKAADDVFAKYPGIKVLASVPGGWDQATAQQVMATLLATYPDIDGVLTQDGMAEGVLRAFQAAGKDP
PVMTGDYRKGFLRKWKELDLPDFESIGVVNPPGIGATALRIAVRLLQGKELKEDALNPLDPYLVNTLYVP
EPLVVTLENLQPAWWMEGLPPDYSFDLLLELEQ
>gnl|CDD|380655 cd20000, PBP1_ABC_rhamnose, rhamnose ABC transporter substrate-binding protein. Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling
RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGPTTATAEAQIPFINTLIQQGVDAIAISANDPDAL
APALKKARAAGIKVVTFDSDVAPEARDLFVNQADADGIGRAQVDMMAELIGGEGEFAILSATPTATNQNA
WIDAMKKELASPEYAGMKLVKVAYGDDDAQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGLK
GKVKVTGLGLPSEMAKYVKDGTVPAFALWNPIDLGYLAAYAAAALAQGEITGKEGETFTAGRLGEYTVGE
GGEVVLGPPFVFTADNID
>gnl|CDD|380656 cd20001, PBP1_LsrB_Quorum_Sensing-like, ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein. Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling
TIAVVVKVTGIAWFDRMETGVEQFAKDTGVNVYQIGPATADAAQQVQIIEDLIAQGVDAICVVPNDPEAL
EPVLKKARDAGIVVITHEASNLKNVDYDVEAFDNAAYGAFIMDKLAEAMGGKGKYVTFVGSLTSTSHMEW
ANAAVAYQKANYPDMLLVTDRVETNDDSETAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQG
KIAVVGTGLPSVAGEYLEDGTIDYIQFWDPADAGYAMNALAVMVLEGEKITDGTDLGVPGYEKVTVGKGK
VLYGNAWLIVTKDNVD
>gnl|CDD|380657 cd20002, PBP1_LsrB_Quorum_Sensing-like, ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein. Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling
TIVTVVKLAGIPWFNRMEQGVKKAGKEFGVNAYQVGPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVL
EPVFKKAREKGIVVITHESPGQKGADWDVELIDNEKFGEAQMELLAKEMGGKGEYAIFVGSLTVPLHNLW
ADAAVEYQKEKYPNMKQVTDRIPGGEDVDVSRQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGLKG
KVAVVGTVIPSQAAAYLKEGSITEGYLWDPADAGYAMVYIAKMLLDGKRKEIGDGFEIPGKGTPDIDGNV
IIFDAPLEITKENAD
>gnl|CDD|380658 cd20003, PBP1_LsrB_Quorum_Sensing, ligand-binding protein LsrB of ABC transporter periplasmic binding protein. Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling
TIAMIPKLVGVPYFTAAGQGAQEAAKELGVDVTYDGPTEASVSKQVEVINNFINQGYDVIAVSANDPDAL
APALKKAMKKGIKVVTWDSDVNPDARDFFVNQATPEGIGKTLVDMVAEQTGEKGKVAIVTSSPTATNQNA
WIKAMKAYIAEKYPDMKIVTTQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTG
KVAVTGLSTPNVMRPYVKDGTVKSVVLWDVVDLGYLAVYVARALADGTLLKVGDFFVAGRLGTFTVVPKG
NGIILLGEPLIFTKENID
>gnl|CDD|380659 cd20004, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate-binding protein such as CUT2. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRGPSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKA
LVAPVERARAQGIPVVIIDSDLGGDAVISFVATDNYAAGRLAAKRMAKLLNGKGKVALLRLAKGSASTTD
RERGFLEALKKLAPGLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGLAG
KVKFIGFDASDLLLDALRAGEISALVVQDPYRMGYLGVKTAVAALRGKPVPKRIDTGVVLVTK
>gnl|CDD|380660 cd20005, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate-binding protein such as CUT2. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
YIAVISKGFQHQFWKAVKKGAEQAAKELGVKITFEGPDTESDVDKQIEMLDNAIAKKPDAIALAALDTNA
LLPQLEKAKEKGIPVVTFDSGVPSDLPLATVATDNYAAGALAADHLAELIGGKGKVAIVAHDATSETGID
RRDGFKDEIKEKYPDIKVVNVQYGVGDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKLG
KIKVVGFDSGEAQIDAIKNGVIAGSVTQNPYGMGYKTVKAAVKALKGEEVEKLIDTGAKWYDKD
>gnl|CDD|380661 cd20006, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate-binding protein such as CUT2. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
KIALILKSSDPNSDFWQTVKSGAEAAAKEYGVDLEFLGPESEEDIDGQIELIEEAIAQKPDAIVLAASDY
DRLVEAVERAKKAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLLGEKGKVAIVSFVKGSSTA
IEREEGFKQALAEYPNIKIVETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGLG
GKVKVVGFDSSVEEIQLLEEGIIDALVVQNPFNMGYLSVQAAVDLLNGKKIPKRIDTGSVVITK
>gnl|CDD|380662 cd20007, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate-binding protein such as CUT2. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVQGPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQAL
IAPLKRAADAGIKVVTVDTTLGDPSFVLSQIASDNVAGGALAAEALAELIGGKGKVLVINSTPGVSTTDA
RVKGFAEEMKKYPGIKVLGVQYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGK
VKVVGFDASPAQVEQLKAGTIDALIAQKPAEIGYLAVEQAVAALTGKPVPKDILTPFVVIT
>gnl|CDD|380663 cd20008, PBP1_ABC_sugar_binding-like, monosaccharide ABC transporter substrate-binding protein such as CUT2. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis
KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPATEADIAGQVNLVENAISRKPDAIVLAPNDTAA
LVPAVEAADAGIPVVLVDSGANTDDYDAFLATDNVAAGALAADELAELLKASGGGKGKVAIISFQAGSQT
LVDREEGFRDYIKEKYPDIEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAG
KAGKIVLVGFDSSPDEVALLKSGVIKALVVQDPYQMGYEGVKTAVKALKGEEIVEKNVDTGVTVVTK
>gnl|CDD|380664 cd20009, PBP1_RafR-like, Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar proteins. Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
VIALVLPTEDEIDGFTSQLISGISEALRGTPYHLVVTPEFPGDDPLEPVRYIVENRLADGIIISHTEPQD
PRVRYLLERGFPFVTHGRTELSTPHAYFDFDNEAFAYEAVRRLAARGRRRIALVAPPRELTYAQHRLRGF
RRALAEAGLEVEPLLIVTLDSSAEAIRAAARRLLRQPPRPDGIICASEIAALGALAGLEDAGLVVGRDVD
VVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEGEPAEPLQTLERPELI
>gnl|CDD|380665 cd20010, PBP1_AglR-like, Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and similar proteins. Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
AIGLVLPLDPGDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILARTRV
NDPRIAYLLERGIPFVVHGRSESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRD
GYRAALAEAGLPVDPALVREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKD
VSVIGHDDLLPALEYFSPPLTTTRSSLRDAGRRLAEMLLALIDGEPAAELQELWPPELI
>gnl|CDD|380666 cd20013, PBP1_RPA0985_benzoate-like, type 1 periplasmic binding-protein component of an ABC system (RPA0985), involved in the active transport of lignin-derived benzoate derivative compounds, and its close homologs. This group includes RPA0985 from Rhodopseudomonas palustris and its close homologs in other bacteria. Rpa0985 is the periplasmic binding-protein component of an ABC system that is involved in the active transport of lignin-derived benzoate derivative compounds. Members of this group has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP)
KVGVIGPFSGPFADYGKQFDRGIDLYLKLHGDKVGGRKVEVIYRDDGGPNPAVAKRLAQELIVRDKVQIL
IGFGFTPNALAVAPVATEAKTPTVIMNAATSSITRKSPYFVRTSFTMWQVAYPMGKWAAKNGIKKAYTAV
ADYAPGHDAETAFKKAFEAAGGKIVGSIRVPLATPDFAPFMQRIKDAKPDAVFVFVPAGAPSIGFLKAYA
ERGLKEAGIKLLGTGDATDDDDLPAMGDAALGLITAGHYSAALDSPENKAFVAAYQKAYGPDARPDFMAV
AAYDGMALIYKMIKATGGKFDGDKAMAAVKGLKWESPRGPISIDPETRDIVQNVYIRRVEKVDGKLQNVE
FDTFEA
>gnl|CDD|380667 cd20014, PBP1_RPA0668_benzoate-like, type 1 periplasmic binding-protein component of an ABC system (RPA0668), involved in in the active transport of lignin-derived benzoate derivative compounds, and its close homologs. This group includes RPA0668 from Rhodopseudomonas palustris and its close homologs in other bacteria. Rpa0668 is the periplasmic binding-protein component of an ABC system that is involved in the active transport of lignin-derived benzoate derivative compounds. Members of this group has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP)
KIGLLLPYSGVYAALGEDIRNGFQLYLDEHGGKLGGRPIELVKEDDEADPDVALQKARKLIEQDKVDVLV
GPVSSGVALAIRDVVEQAKVPLIVANAGANALTRAACSPYIFRTSFSNWQLGYALGKYAAENVGKTVVTI
ASDYAAGREVVAGFKEGFEAAGGKVVGEIWTPLGTTTDFSPYLTQIAASGPDAVYAFFAGADAVRFVKQY
AEFGLKGKIPLYGPGFLTDEDVLPALGEAAEGIITVLHYAPTLDNPANRAFVAAYQAKYGRLPDVYAVQG
YDAAQVIDAALEAVGGDTSDKDILAAALELGSIDSPRGPFRFDPTTHNPIQNIYLREVVKGGGGLT
>gnl|CDD|410789 cd20015, FH_FOXA, Forkhead (FH) domain found in the Forkhead box protein A (FOXA) subfamily. The FOXA subfamily includes three winged helix transcription factors, FOXA1 (also called hepatocyte nuclear factor 3-alpha or transcription factor 3A), FOXA2 (also called hepatocyte nuclear factor 3-beta or transcription factor 3B), and FOXA3 (also called hepatocyte nuclear factor 3-gamma or transcription factor 3G). FOXA1 is essential for epithelial lineage differentiation and has been found to be upregulated in numerous cancers. FOXA2 controls cell differentiation. It is a key transcriptional regulator that maintains airway mucus homeostasis and may also have an important role in bone metabolism. FOXA3 acts as an essential transcriptional regulator engaged in adipogenesis and energy metabolism. This subfamily also includes Xenopus tropicalis FOXA4, Drosophila melanogaster protein fork head (dFKH), and similar proteins. FOXA4 is only present in amphibians, where it is required for the correct regionalization and maintenance of the central nervous system. dFKH promotes terminal as opposed to segmental development. In the absence of dFKH, this developmental switch does not occur. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSYISLITMAIQQSPSKMLTLSEIYQWIMDLFPYYRQNQQRWQNSIRHSLSFNDCFVKVPRSPDKPG
KGSYWTLHPDSGNMFENGCYLRRQKRF
>gnl|CDD|410790 cd20016, FH_FOXB, Forkhead (FH) domain found in the Forkhead box protein B (FOXB) subfamily. The FOXB subfamily includes two winged helix transcription factors, FOXB1 (also called transcription factor FKH-5) and FOXB2 (also called transcription factor FKH-4). FOXB1 controls development of mammary glands and regions of the central nervous system (CNS) that regulate the milk-ejection reflex. It is essential for access of mammillothalamic axons to the thalamus. FOXB2 may act as a tumor suppressor; it has been found to inhibit the malignant characteristics of the pancreatic cancer cell line Panc-1 in vitro. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSYISLTAMAIQSSPEKMLPLSDIYKFIMDRFPYYRKNTQRWQNSLRHNLSFNDCFIKIPRRPDRPG
KGSYWALHP
>gnl|CDD|410791 cd20017, FH_FOXC, Forkhead (FH) domain found in the Forkhead box protein C (FOXC) subfamily. The FOXC subfamily includes two winged helix transcription factors, FOXC1 (also called Forkhead-related protein FKHL7, or Forkhead-related transcription factor 3) and FOXC2 (also called Forkhead-related protein FKHL14, or Mesenchyme fork head protein 1). FOXC1 is a DNA-binding transcriptional factor that plays a role in a broad range of cellular and developmental processes such as the development of the eyes, bones, cardiovascular system, kidneys, and skin. FOXC2 acts as a transcriptional activator that might be involved in the formation of special mesenchymal tissues. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSYIALIAMAIQNAPDKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNECFVKVPRDDKKPG
KGSYWTL
>gnl|CDD|410792 cd20018, FH_FOXD, Forkhead (FH) domain found in the Forkhead box protein D (FOXD) subfamily. The FOXD subfamily includes four winged helix transcription factors, FOXD1-4. FOXD1, also called Forkhead-related protein FKHL8 or Forkhead-related transcription factor 4 (FREAC-4), is involved in transcriptional activation of Placental Growth Factor (PGF) and the complement component (C3) genes. It plays an important role in early embryonic development and organogenesis, and functions as an oncogene in several cancers. FOXD2, also called Forkhead-related protein FKHL17 or Forkhead-related transcription factor 9 (FREAC-9), is a probable transcription factor involved in embryogenesis and somatogenesis. FOXD3, also called HNF3/FH transcription factor genesis, acts as a transcriptional repressor that binds to the consensus sequence 5'-A[AT]T[AG]TTTGTTT-3'. It also acts as a transcriptional activator. It promotes development of neural crest cells from neural tube progenitors and restricts neural progenitor cells to the neural crest lineage while suppressing interneuron differentiation. FOXD3 is required for maintenance of pluripotent cells in the pre-implantation and peri-implantation stages of embryogenesis. FOXD4, also called Forkhead-related protein FKHL9 or Forkhead-related transcription factor 5 (FREAC-5), is essential for establishing neural cell fate and for neuronal differentiation. The family also includes Forkhead box protein D4-like proteins, FOXD4L1-6. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSYIALITMAILQSPQKKLTLSGICEFIMNRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNPG
KGNYWTLD
>gnl|CDD|410793 cd20019, FH_FOXE, Forkhead (FH) domain found in the Forkhead box protein E (FOXE) subfamily. The FOXE subfamily includes two winged helix transcription factors, FOXE1 (also known as FOXE2) and FOXE3. FOXE1, also called Forkhead-related protein FKHL15, HFKH4, HNF-3/fork head-like protein 5 (HFKL5), or thyroid transcription factor 2 (TTF-2), is a transcription factor that binds consensus sites on a variety of gene promoters and activate their transcription. FOXE3, also called Forkhead-related protein FKHL12 or Forkhead-related transcription factor 8 (FREAC-8), is a transcription factor that controls lens epithelial cell growth through regulation of proliferation, apoptosis, and the cell cycle. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSYIALIAMAIANSPERKLTLGGIYKFIMERFPFYRDNSKKWQNSIRHNLTLNDCFVKIPREPGRPG
KGNYWTLDPAAEDMFDNGSFLRRR
>gnl|CDD|410794 cd20020, FH_FOXF, Forkhead (FH) domain found in the Forkhead box protein F (FOXF) subfamily. The FOXF subfamily includes two winged helix transcription factors, FOXF1 and FOXF2, both of which are probable transcription activators for a number of lung-specific genes. FOXF1 mutations in sporadic and familial cases of alveolar capillary dysplasia with misaligned pulmonary veins (ACD/MPV) suggest its involvement in ACD/MPV and lung organogenesis. FOXF2 is involved in programming organogenesis and regulating epithelial-to-mesenchymal transition (EMT) and cell proliferation. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
PPYSYIALIVMAIQASPTKRLTLSEIYQFLQQRFPFFRGPYQGWKNSVRHNLSLNECFIKLPKGLGRPGK
GHYWTIDP
>gnl|CDD|410795 cd20021, FH_FOXG, Forkhead (FH) domain found in the Forkhead box protein G (FOXG) subfamily. The FOXG subfamily includes a winged helix transcription factor FOXG1, which is also called brain factor 1 (BF-1), brain factor 2 (BF-2), Forkhead box protein G1A, Forkhead box protein G1B, Forkhead box protein G1C, Forkhead-related protein FKHL1, Forkhead-related protein FKHL2, or Forkhead-related protein FKHL3. FOXG1 acts as a transcription repression factor which plays an important role in the establishment of the regional subdivision of the developing brain and in the development of the telencephalon. It is repetitively used in the sequential events of telencephalic development to control multi-steps of brain circuit formation ranging from cell cycle control to neuronal differentiation in a clade- and species-specific manner. Individuals with mutations in FOXG1 harbor "FOXG1-related encephalopathy", characterized by two clinical phenotypes/syndromes including microcephaly, developmental delay, severe cognitive disabilities, early-onset dyskinesia and hyperkinetic movements, stereotypies, epilepsy, and cerebral malformation for those with deletions or intragenic mutations of FOXG1. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPFSYNALIMMAIRQSPEKRLTLNGIYEFIMKNFPYYRENKQGWQNSIRHNLSLNKCFVKVPRHYDDPG
KGNYWMLDP
>gnl|CDD|410796 cd20022, FH_FOXH, Forkhead (FH) domain found in the Forkhead box protein H (FOXH) subfamily. The FOXH subfamily includes a winged helix transcription factor, FOXH1, which is also called Forkhead activin signal transducer 1 (Fast-1), or Forkhead activin signal transducer 2 (Fast-2). FOXH1 acts as a transcriptional activator that recognizes and binds to the DNA sequence 5'-TGT[GT][GT]ATT-3'. It is required for induction of the goosecoid (GSC) promoter by TGF-beta or activin signaling. FOXH1 forms a transcriptionally active complex containing FOXH1/SMAD2/SMAD4 on a site on the GSC promoter called TARE (TGF-beta/activin response element). The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSYLAMIALAIQNSPEKRLTLSEIIKALSTMFPFFKGEYKGWKDSVRHNLSSNDCFVKVLKDPGKPQ
AKGNYWTVD
>gnl|CDD|410797 cd20023, FH_FOXJ1, Forkhead (FH) domain found in Forkhead box protein J1 (FOXJ1) and similar proteins. FOXJ1, also called Forkhead-related protein FKHL13 or hepatocyte nuclear factor 3 Forkhead homolog 4 (HFH-4), acts as a transcription factor specifically required for the formation of motile cilia. It acts by activating transcription of genes that mediate assembly of motile cilia, such as CFAP157. FOXJ1 binds the DNA consensus sequences 5'-HWDTGTTTGTTTA-3' or 5'-KTTTGTTGTTKTW-3' (where H is not G, W is A or T, D is not C, and K is G or T). It activates the transcription of a variety of ciliary proteins in the developing brain and lung. The FH domain is a winged helix DNA-binding domain
KPPYSYATLICMAMQASKKTKITLSAIYKWITDNFMYYRVADPTWQNSIRHNLSLNKCFIKVPRSKDEPG
KGGFWRIDP
>gnl|CDD|410798 cd20024, FH_FOXJ2-like, Forkhead (FH) domain found in Forkhead box proteins, FOXJ2, FOXJ3 and similar proteins. The FOXJ2-like subfamily includes two winged helix transcription factors, FOXJ2 and FOXJ3. FOXJ2, also called Forkhead homologous X (FHX), plays an important role in tumorigenesis, progression, and metastasis of certain cancers. It acts as a transcriptional activator that can bind to two different type of DNA binding sites. FOXJ3 is a transcription factor which regulates sperm function. It transcriptionally activates Mef2c and regulates adult skeletal muscle fiber type identity. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSYATLITFAINSSPKKKMTLSEIYTWICENFPYYREAGTGWKNSIRHNLSLNKCFKKVPRSKDDPG
KGSYWTL
>gnl|CDD|410799 cd20025, FH_FOXI, Forkhead (FH) domain found in the Forkhead box protein I (FOXI) subfamily. The FOXI subfamily includes three human winged helix transcription factors, FOXI1-3, Xenopus laevis FoxI1c, and similar proteins. FOXI1 acts as a transcriptional activator required for the development of normal hearing, sense of balance, and kidney function. FOXI2 may act as a transcriptional activator that plays a possible role in controlling cellular identity. Loss of function mutations in the FOXI2 gene may contribute to ectodermal dysplasia. FOXI3 plays a critical role in the development of the inner ear and jaw. It is a regulator of ectodermal development. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
PPYSYSALIAMAIQSAPEKKLTLSQIYQYVAENFPFYKRSKAGWQNSIRHNLSLNDCFKKVPRDEDDPGK
GNYWTLD
>gnl|CDD|410800 cd20026, FH_FOXK, Forkhead (FH) domain found in the Forkhead box protein K (FOXK) subfamily. The FOXK subfamily includes two winged helix transcription factors, FOXK1 and FOXK2. FOXK1, also called myocyte nuclear factor (MNF), acts as a transcriptional regulator that binds to the upstream enhancer region (CCAC box) of myoglobin genes. It positively regulates Wnt/beta-catenin signaling by translocating dishevelled (DVL) proteins into the nucleus. It also reduces virus replication, probably by binding the interferon stimulated response element (ISRE) to promote antiviral gene expression. In addition, FOXK1 plays important roles in multiple human cancers. FOXK2, also called cellular transcription factor ILF-1 or interleukin enhancer-binding factor 1, is a transcriptional regulator that recognizes the core sequence 5'-TAAACA-3'. It binds to NFAT-like motifs (purine-rich) in the IL2 promoter. It also binds to the HIV-1 long terminal repeat. FOXK2 may be involved in both, positive and negative regulation of important viral and cellular promoter elements. In addition, FOXK2 plays a critical role in suppressing tumorigenesis. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSYAQLIVQAISSAPDKQLTLSGIYAYITKNYPYYRTADKGWQNSIRHNLSLNRYFIKVPRSQEEPG
KGSFWRID
>gnl|CDD|410801 cd20027, FH_FOXL1, Forkhead (FH) domain found in Forkhead box protein L1 (FOXL1) and similar proteins. FOXL1, also called Forkhead-related protein FKHL11 or Forkhead-related transcription factor 7 (FREAC-7), acts as a transcription factor required for proper proliferation and differentiation in the gastrointestinal epithelium. It may play a critical role in suppressing tumorigenesis. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
PQKPPYSYIALIAMAIKSAPDQKVTLNGIYQFIMDRFPYYHDNKQGWQNSIRHNLSLNDCFVKVPREKGR
PGKGNYWTLDPDCEEMFENGNYRRRKRR
>gnl|CDD|410802 cd20028, FH_FOXL2, Forkhead (FH) domain found in Forkhead box protein L2 (FOXL2) and similar proteins. FOXL2 is a transcriptional regulator that is essential for ovary differentiation and maintenance, and repression of the genetic program for somatic testis determination. Mutations in the FOXL2 gene cause blepharophimosis-ptosis-epicanthus inversus syndrome (BPES) types I and II, a rare genetic disorder. In BPES type I, a complex eyelid malformation is associated with premature ovarian failure (POF), whereas in BPES type II, the eyelid defect occurs as an isolated entity. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSYVALIAMAIRESPEKRLTLSGIYQYIIAKFPYYEKNKKGWQNSIRHNLSLNECFVKVPREGGGER
KGNYWTLDPACEDMFEKGN
>gnl|CDD|410803 cd20029, FH_FOXM, Forkhead (FH) domain found in the Forkhead box protein M (FOXM) subfamily. The FOXM subfamily includes a winged helix transcription factor, FOXM1, which is also called Forkhead-related protein FKHL16, Hepatocyte nuclear factor 3 Forkhead homolog 11 (HFH-11), HNF-3/fork-head homolog 11, M-phase phosphoprotein 2, MPM-2 reactive phosphoprotein 2, transcription factor Trident, or Winged-helix factor from INS-1 cells. FOXM1 acts as a transcriptional factor regulating the expression of cell cycle genes essential for DNA replication and mitosis. It plays a role in the control of cell proliferation. It is also involved in DNA break repair, participating in the DNA damage checkpoint response. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
RPPYSYMALIQFAINSTEDKRMTLKEIYTWIEDHFPYFKHTAKPGWKNSIRHNLSLHDIFVRETSANGKG
SFWTLRP
>gnl|CDD|410804 cd20030, FH_FOXN1-like, Forkhead (FH) domain found in Forkhead box protein N1 (FOXN1) and similar proteins. The FOXN1-like group includes two FOXN subfamily winged helix transcription factors, FOXN1 and FOXN4. FOXN1, also called winged helix transcription factor nude, acts as a transcriptional regulator which regulates the development, differentiation, and function of thymic epithelial cells (TECs), both in the prenatal and postnatal thymus. FOXN4 acts as a transcription factor essential for neural and some non-neural tissue development, such as retina and lung, respectively. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPAYSYSCLIAMALKNSRTGCLPVSEIYSFMCENFPYFKTAPDGWKNSVRHNLSLNKCFEKIERPDGNGS
SRKGCLWALNP
>gnl|CDD|410805 cd20031, FH_FOXN2-like, Forkhead (FH) domain found in Forkhead box protein N2 (FOXN2) and similar proteins. The FOXN2-like group includes two FOXN subfamily winged helix transcription factors, FOXN2 and FOXN3. FOXN2, also called human T-cell leukemia virus enhancer factor (HTLF), is a potential tumor suppressor that can facilitate replication fork reversal. It acts as a transcription factor that binds to the purine-rich region in human T-cell leukemia virus long terminal repeat (HTLV-I LTR). It may be a potential therapeutic and radiosensitization target for lung cancer. FOXN3, also called checkpoint suppressor 1, acts as a transcriptional repressor that may be involved in DNA damage-inducible cell cycle arrests (checkpoints). The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSFSCLIFMAIESSPEKALPVKDIYSWIEKHFPYYRNAPSGWKNSIRHNLSLNKCFKKVEKEKNKGK
GSLWCV
>gnl|CDD|410806 cd20032, FH_FOXO, Forkhead (FH) domain found in the Forkhead box protein O (FOXO) subfamily. The FOXO subfamily includes several winged helix transcription factors: FOXO1, FOXO3, FOXO4 and FOXO6. FOXO transcription factors are involved in the regulation of longevity phenomenon via insulin and insulin-like growth factor signaling. All FOXOs bind to the consensus sequence 5'-GTAAACAA-3', known as the DAF-16 family member-binding element, which includes the core sequence 5'-(A/C)AA(C/T)A-3' recognized by all FOX family members. FOXO1, also called Forkhead box protein O1A or Forkhead in rhabdomyosarcoma (FKHR), is a transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. FOXO3, also called AF6q21 protein or Forkhead in rhabdomyosarcoma-like 1 (FKHRL1), is a transcriptional activator which triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress. It recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3'. FOXO4, also called Fork head domain transcription factor AFX1, is a transcription factor involved in the regulation of the insulin signaling pathway. It binds to insulin-response elements (IREs) and can activate transcription of IGFBP1. FOXO6 acts as a transcriptional activator that may play an important role on tumor invasion, metastasis, and prognosis. The FH domain is a winged helix DNA-binding domain
GNMSYADLITKAIESSPDKRLTLQQIYDWMVRNVPYFKDKGDSNSSAGWKNSIRHNLSLHSRFVRVQNEG
TGKSSWWTLN
>gnl|CDD|410807 cd20033, FH_FOXP, Forkhead (FH) domain found in the Forkhead box protein P (FOXP) subfamily. The FOXP subfamily includes four winged helix transcription factors, FOXP1-4. They are involved in the development of the central nervous system. Mutations in FOXP1, also called Mac-1-regulated Forkhead (MFH), leads to developmental delay, intellectual disability, autism spectrum disorder, speech delay, and dysmorphic features. FOXP2, also called CAG repeat protein 44 or Trinucleotide repeat-containing gene 10 protein, is a transcriptional repressor that may play a role in the specification and differentiation of lung epithelium. It may also play a role in developing neural, gastrointestinal and cardiovascular tissues. FOXP3, also called Scurfin, is a transcriptional regulator which is crucial for the development and inhibitory function of regulatory T-cells (Treg). FOXP4, also called Forkhead-related protein-like A, is a transcriptional repressor that represses lung-specific expression. It is necessary for normal T cell cytokine recall responses to antigen following pathogenic infection. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
RPPFTYASLIRQAILESPNKQLTLNEIYNWFQKTFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKGAVW
TVD
>gnl|CDD|410808 cd20034, FH_FOXQ1-like, Forkhead (FH) domain found in Forkhead box protein Q1 (FOXQ1) and similar proteins. FOXQ1, also called HNF-3/Forkhead-like protein 1 (HFH-1), or hepatocyte nuclear factor 3 Forkhead homolog 1, plays a role in hair follicle differentiation. It has also been reported to promote epithelial differentiation, inhibit smooth muscle differentiation, activate T cells and autoimmunity, and control mucin gene expression and granule content in stomach surface mucous cells. FOXQ1 is significantly associated with the pathogenesis of various tumor types including gastric, breast, colorectal, pancreatic, bladder and ovarian cancer, and glioma. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSYIALIAMAIRDSPSGRLTLAEINEYLMKKFPFFRGSYTGWRNSVRHNLSLNDCFVKVLRDPSRPW
GKDNYWTIN
>gnl|CDD|410809 cd20035, FH_FOXQ2-like, Forkhead (FH) domain found in Forkhead box protein Q2 (FOXQ2) and similar proteins. FOXQ2 is the neurogenic ectoderm specification transcription factor that controls aboral development in cnidarians and anterior identity in bilaterians. It plays essential roles in epidermal development and central brain patterning. The foxQ2 gene is absent in placental mammals. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPSHSYVALIAKAILSSPEKKLVLSDIYQYIEENYPYFKSRGSSWKNSVRHNLSLNECFVKAGRAENGKG
NYWTIHPACLEDFEKGDFRRRRARR
>gnl|CDD|410810 cd20036, FH_FOXR, Forkhead (FH) domain found in the Forkhead box protein R (FOXR) subfamily. The FOXR subfamily includes two winged helix transcription factors, FOXR1-2. FOXR1, also called Forkhead box protein N5 (FOXN5), is required for proper cell division and survival possibly via the p21 and mTOR pathways. FOXR2, also called Forkhead box protein N6 (FOXN6), is an important player in a wide range of cellular processes such as proliferation, migration, differentiation, and apoptosis. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
WPKPPLSYPNLIALALRNSETGSLNVQEIYDFIRFHFPFFRTAPDGWKNSVRHNLSFSDSFEKVPTSVSG
YGGRRSCLWKLTPEGER
>gnl|CDD|410811 cd20037, FH_FOXS1, Forkhead (FH) domain found in Forkhead box protein S1 (FOXS1). FOXS1, also called Forkhead-like 18 protein or Forkhead-related transcription factor 10 (FREAC-10), is a transcriptional repressor that suppresses transcription from the FASLG, FOXO3, and FOXO4 promoters. It may have a role in the organization of the testicular vasculature. It has also been implicated in energy turnover, motor function, and body weight. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
TKPPYSYIALIAMAIQSSPGQRATLSGIYRYIMGRFAFYRHNRPGWQNSIRHNLSLNECFVKVPRDDRKP
GKGSYWTLDPDCHDMFEHGSFLRRRRRFTR
>gnl|CDD|410812 cd20038, FH_FOXA1, Forkhead (FH) domain found in Forkhead box protein A1 (FOXA1) and similar proteins. FOXA1, also called hepatocyte nuclear factor 3-alpha (HNF-3-alpha or HNF-3A) or transcription factor 3A (TCF-3A), acts as a transcription factor that is essential for epithelial lineage differentiation. It has been found to be upregulated in numerous cancers. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
RDTKTFRRSYPHAKPPYSYISLITMAIQQAPSKMLTLSEIYQWIMDLFPYYRQNQQRWQNSIRHSLSFND
CFVKVARSPDKPGKGSYWTLHPDSGNMFENGCYLRRQKRFKC
>gnl|CDD|410813 cd20039, FH_FOXA2, Forkhead (FH) domain found in Forkhead box protein A2 (FOXA2) and similar proteins. FOXA2, also called hepatocyte nuclear factor 3-beta (HNF-3-beta or HNF-3B) or transcription factor 3B (TCF-3B), acts as a core transcription factor that controls cell differentiation. It is a key transcriptional regulator that maintains airway mucus homeostasis. It may also have an important role in bone metabolism. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
YTHAKPPYSYISLITMAIQQSPNKMLTLSEIYQWIMDLFPFYRQNQQRWQNSIRHSLSFNDCFLKVPRSP
DKPGKGSFWTLHPDSGNMFENGCYLRRQKRFKCE
>gnl|CDD|410814 cd20040, FH_FOXA3, Forkhead (FH) domain found in Forkhead box protein A3 (FOXA3) and similar proteins. FOXA3, also called hepatocyte nuclear factor 3-gamma (HNF-3-gamma or HNF-3G), fork head-related protein FKH H3, or transcription factor 3G (TCF-3G), acts as an essential transcriptional regulator engaged in adipogenesis and energy metabolism. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
HAKPPYSYISLITMAIQQAPSKMLTLNEIYQWIMDLFPYYRENQQRWQNSIRHSLSFNDCFVKVARSPDK
PGKGSYWALHPNSGNMFENGCYLRRQKRFKLE
>gnl|CDD|410815 cd20041, FH_dFKH, Forkhead (FH) domain found in Drosophila melanogaster protein fork head (dFKH) and similar proteins. dFKH promotes terminal as opposed to segmental development. In the absence of dFKH, this developmental switch does not occur. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSYISLITMAIQNSPNKMVTLSEIYQFIMDLFPFYRQNQQRWQNSIRHSLSFNDCFVKVPRTPDKPG
KGSFWTLHPDSGNMFENGCYLRRQKRFK
>gnl|CDD|410816 cd20042, FH_FOXB1, Forkhead (FH) domain found in Forkhead box protein B1 (FOXB1) and similar proteins. FOXB1, also called transcription factor FKH-5, is a winged helix transcription factor that controls development of mammary glands and regions of the central nervous system (CNS) that regulate the milk-ejection reflex. It is essential for access of mammillothalamic axons to the thalamus. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
TYSDQKPPYSYISLTAMAIQSSPEKMLPLSEIYKFIMDRFPYYRENTQRWQNSLRHNLSFNDCFIKIPRR
PDQPGKGSFWALHPSCGDMFEN
>gnl|CDD|410817 cd20043, FH_FOXB2, Forkhead (FH) domain found in Forkhead box protein B2 (FOXB2) and similar proteins. FOXB2, also called transcription factor FKH-4, may act as a transcription factor. It may also act as a tumor suppressor; it has been found to inhibit the malignant characteristics of the pancreatic cancer cell line Panc-1 in vitro. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
MPRPGKNSYSDQKPPYSYISLTAMAIQSSQEKMLPLSDIYKFIMDRFPYYRENTQRWQNSLRHNLSFNDC
FIKIPRRPDQPGKGSFWALHPDCGDMFENGSFLRRRKRFK
>gnl|CDD|410818 cd20044, FH_FOXC1, Forkhead (FH) domain found in Forkhead box protein C1 (FOXC1) and similar proteins. FOXC1, also called Forkhead-related protein FKHL7, or Forkhead-related transcription factor 3 (FREAC-3), is a DNA-binding transcriptional factor that plays a role in a broad range of cellular and developmental processes such as the development of the eyes, bones, cardiovascular system, kidneys, and skin. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
PKDMVKPPYSYIALITMAIQNAPDKKITLNGIYQFIMERFPFYRDNKQGWQNSIRHNLSLNECFVKVPRD
DKKPGKGSYWTLDPDSYNMFENG
>gnl|CDD|410819 cd20045, FH_FOXC2, Forkhead (FH) domain found in Forkhead box protein C2 (FOXC2) and similar proteins. FOXC2, also called Forkhead-related protein FKHL14, Mesenchyme fork head protein 1 (MFH-1 protein), or transcription factor FKH-14, acts as a transcriptional activator that might be involved in the formation of special mesenchymal tissues. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
LVKPPYSYIALITMAIQNAPDKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNECFVKVPRDDKK
PGKGSYWTLDPDSYNMFENG
>gnl|CDD|410820 cd20046, FH_FOXD1_D2-like, Forkhead (FH) domain found in Forkhead box proteins FOXD1, FOXD2 and similar proteins. FOXD1, also called Forkhead-related protein FKHL8, or Forkhead-related transcription factor 4 (FREAC-4), is involved in transcriptional activation of Placental Growth Factor (PGF) and the complement component (C3) genes. It plays an important role in early embryonic development and organogenesis, and functions as an oncogene in several cancers. FOXD2, also called Forkhead-related protein FKHL17, or Forkhead-related transcription factor 9 (FREAC-9), is a probable transcription factor involved in embryogenesis and somatogenesis. It has been found that long noncoding RNA FOXD2 adjacent opposite strand RNA1 (lncRNA FOXD2-AS1) expression is upregulated in various human malignancies, including gastric, lung, bladder, colorectal, nasopharyngeal, esophageal, hepatocellular, thyroid and skin cancer. It is a promising candidate as a new biomarker and therapeutic target for cancer diagnosis/prognostication due to high tissue specificity and elevated efficiency. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSYIALITMAILQSPKKRLTLSEICEFISNRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNPG
KGNYWTLDPESADMFDNGSFLRRRKRFKR
>gnl|CDD|410821 cd20047, FH_FOXD3, Forkhead (FH) domain found in Forkhead box protein D3 (FOXD3) and similar proteins. FOXD3, also called HNF3/FH transcription factor genesis, acts as a transcriptional repressor that binds to the consensus sequence 5'-A[AT]T[AG]TTTGTTT-3'. It also acts as a transcriptional activator. It promotes development of neural crest cells from neural tube progenitors and restricts neural progenitor cells to the neural crest lineage while suppressing interneuron differentiation. FOXD3 is required for maintenance of pluripotent cells in the pre-implantation and peri-implantation stages of embryogenesis. The FH domain is a winged helix DNA-binding domain
VKPPYSYIALITMAILQSPQKKLTLSGICEFISNRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNP
GKGNYWTLDPQSEDMFDNGSFLRRRKR
>gnl|CDD|410822 cd20048, FH_FOXD4-like, Forkhead (FH) domain found in Forkhead box protein D4 (FOXD4) and similar proteins. FOXD4, also called Forkhead-related protein FKHL9, Forkhead-related transcription factor 5 (FREAC-5), or myeloid factor-alpha, is essential for establishing neural cell fate and for neuronal differentiation. The family also includes Forkhead box protein D4-like proteins, FOXD4L1-6. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSYIALITMAILQSPHKRLTLSGICAFISGRFPYYRRKFPAWQNSIRHNLSLNDCFVKIPREPGHPG
KGNYWSLDPASQDMFDNGSFLRRRKR
>gnl|CDD|410823 cd20049, FH_FOXF1, Forkhead (FH) domain found in Forkhead box protein F1 (FOXF1) and similar proteins. FOXF1, also called Forkhead-related activator 1 (FREAC-1), Forkhead-related protein FKHL5, or Forkhead-related transcription factor 1, is a probable transcription activator for a number of lung-specific genes. FOXF1 mutations in sporadic and familial cases of alveolar capillary dysplasia with misaligned pulmonary veins (ACD/MPV) suggest its involvement in ACD/MPV and lung organogenesis. The role of FOXF1 in cancer is conflicting; its loss in some cancers suggests a tumor suppressive function, but its abundance in others is associated with protumorigenic and metastatic traits. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
PPYSYIALIVMAIQSSPTKRLTLSEIYQFLQSRFPFFRGSYQGWKNSVRHNLSLNECFIKLPKGLGRPGK
GHYWTIDPASEFMFEEGSFRRRPRGFRRK
>gnl|CDD|410824 cd20050, FH_FOXF2, Forkhead (FH) domain found in Forkhead box protein F2 (FOXF2) and similar proteins. FOXF2, also called Forkhead-related activator 2 (FREAC-2), Forkhead-related protein FKHL6, or Forkhead-related transcription factor 2, is a probable transcription activator for a number of lung-specific genes. It is involved in programming organogenesis and regulating epithelial-to-mesenchymal transition (EMT) and cell proliferation. FOXF2 dysregulation is critical for tumorigenesis of various tissue types. Its expression correlates with good prognosis in patients with early non-invasive stages of breast cancer, but with poor prognosis in advanced breast cancer. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
PPYSYIALIVMAIQSSPSKKLTLSEIYQFLQARFPFFRGAYQGWKNSVRHNLSLNECFIKLPKGLGRPGK
GHYWTIDPASEFMFEEGSFRRRP
>gnl|CDD|410825 cd20051, FH_FOXJ2, Forkhead (FH) domain found in Forkhead box protein J2 (FOXJ2) and similar proteins. FOXJ2, also called Fork head homologous X (FHX), plays an important role in tumorigenesis, progression, and metastasis of certain cancers. It acts as a transcriptional activator that can bind to two different type of DNA binding sites. It is specifically expressed in meiotic spermatocytes in adult mouse testes and appears to promote meiotic progression during spermatogenesis. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
GKPPYSYATLITYAINSSPAKKMTLSEIYRWICDNFPYYRNAGVGWKNSIRHNLSLNKCFRKVPRPRDDP
GKGSYWMIDSCP
>gnl|CDD|410826 cd20052, FH_FOXJ3, Forkhead (FH) domain found in Forkhead box protein J3 (FOXJ3) and similar proteins. FOXJ3 is a transcription factor which regulates sperm function. It transcriptionally activates Mef2c and regulates adult skeletal muscle fiber type identity. Polymorphisms in the FOXJ3 gene may be associated with the development of rheumatoid arthritis. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
GKPPYSYANLITFAINSSPKKKMTLSEIYQWICDNFPYYREAGNGWKNSIRHNLSLNKCFLKVPRSKDDP
GKGSYWAID
>gnl|CDD|410827 cd20053, FH_FOXI1, Forkhead (FH) domain found in Forkhead box protein I1 (FOXI1) and similar proteins. FOXI1 is also called Forkhead-related protein FKHL10, Forkhead-related transcription factor 6 (FREAC-6), Hepatocyte nuclear factor 3 Forkhead homolog 3 (HFH-3), or HNF-3/fork-head homolog 3. It is a master regulator of vacuolar H-ATPase proton pump subunits in the inner ear, kidney, and epididymis, and is required for the development of normal hearing, sense of balance, and kidney function. Its epididymal expression is required for male fertility. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KLVRPPYSYSALIAMAIHGAPDKRLTLSQIYQYVADNFPFYNKSKAGWQNSIRHNLSLNDCFKKVPRDED
DPGKGNYWTLDPNCEKMFDNGNFRRKRKRK
>gnl|CDD|410828 cd20054, FH_FOXK1, Forkhead (FH) domain found in Forkhead box protein K1 (FOXK1) and similar proteins. FOXK1, also called myocyte nuclear factor (MNF), acts as a transcriptional regulator that binds to the upstream enhancer region (CCAC box) of myoglobin genes. It positively regulates Wnt/beta-catenin signaling by translocating dishevelled (DVL) proteins into the nucleus. It also reduces virus replication, probably by binding the interferon stimulated response element (ISRE) to promote antiviral gene expression. In addition, FOXK1 plays important roles in multiple human cancers. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
ESKPPYSYAQLIVQAISSAQDRQLTLSGIYAHITKHYPYYRTADKGWQNSIRHNLSLNRYFIKVPRSQEE
PGKGSFWRIDPASEAKLVEQAFRKRRQRGVS
>gnl|CDD|410829 cd20055, FH_FOXK2, Forkhead (FH) domain found in Forkhead box protein K2 (FOXK2) and similar proteins. FOXK2, also called cellular transcription factor ILF-1 or interleukin enhancer-binding factor 1, is a transcriptional regulator that recognizes the core sequence 5'-TAAACA-3'. It binds to NFAT-like motifs (purine-rich) in the IL2 promoter. It also binds to the HIV-1 long terminal repeat. FOXK2 may be involved in both, positive and negative regulation of important viral and cellular promoter elements. In addition, FOXK2 plays a critical role in suppressing tumorigenesis. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
DSKPPYSYAQLIVQAITMAPDKQLTLNGIYTHITKNYPYYRTADKGWQNSIRHNLSLNRYFIKVPRSQEE
PGKGSFWRIDPASESKLIEQAFRKRRPR
>gnl|CDD|410830 cd20056, FH_FOXN1, Forkhead (FH) domain found in Forkhead box protein N1 (FOXN1). FOXN1, also called winged helix transcription factor nude, acts as a transcriptional regulator which regulates the development, differentiation, and function of thymic epithelial cells (TECs), both in the prenatal and postnatal thymus. It is also an important factor in controlling the skin wound healing process, as it actively participates in re-epithelialization and is responsible for scar formation. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
PKPIYSYSILIFMALKNSKTGSLPVSEIYNFMTEHFPYFKTAPDGWKNSVRHNLSLNKCFEKVENKSGSS
SRKGCLWALNPAKIDKMQEELQKWKRK
>gnl|CDD|410831 cd20057, FH_FOXN4, Forkhead (FH) domain found in Forkhead box protein N4 (FOXN4). FOXN4 acts as a transcription factor essential for neural and some non-neural tissue development, such as retina and lung, respectively. During development of the central nervous system, FOXN4 is required in specifying the amacrine and horizontal cell fates from multipotent retinal progenitors, while suppressing alternative photoreceptor cell fates. In non-neural tissues, it plays an essential role in specifying the atrioventricular canal and is indirectly required for patterning the distal airway during lung development. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
PKHYPKPIYSYSCLIAMALKNSKTGSLPVSEIYSFMKEHFPYFKTAPDGWKNSVRHNLSLNKCFEKVENK
MSGSSRKGCLWALNPAKIDKMEEEMQKWKRKDLPAI
>gnl|CDD|410832 cd20058, FH_FOXN2, Forkhead (FH) domain found in Forkhead box protein N2 (FOXN2). FOXN2, also called human T-cell leukemia virus enhancer factor (HTLF), is a potential tumor suppressor that can facilitate replication fork reversal. It acts as a transcription factor that binds to the purine-rich region in human T-cell leukemia virus long terminal repeat (HTLV-I LTR). It may be a potential therapeutic and radiosensitization target for lung cancer. FOXN2 has also been found to be down-regulated in breast cancer, where it regulates migration, invasion, and epithelial-mesenchymal transition. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
SKPPYSFSLLIYMAIEHSPNKCLPVKEIYSWILEHFPYFSTAPTGWKNSVRHNLSLNKCFRKVERSHGKV
NGKGSLWCVDPE
>gnl|CDD|410833 cd20059, FH_FOXN3, Forkhead (FH) domain found in Forkhead box protein N3 (FOXN3). FOXN3, also called checkpoint suppressor 1 (CHES1), acts as a transcriptional repressor that may be involved in DNA damage-inducible cell cycle arrests (checkpoints). It displays transcriptional inhibitory activity, and is involved in cell cycle regulation and tumorigenesis. Alterations in FOXN3 are found in of a variety of cancers including melanoma, osteosarcoma, and hepatocellular carcinoma. FOXN3 also regulates hepatic glucose utilization/metabolism by regulating gluconeogenic substrate selection. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
KPPYSFSCLIFMAIEDSPTKRLPVKDIYNWILEHFPYFANAPTGWKNSVRHNLSLNKCFKKVDKEKGQSI
GKGSLWCIDPEYRPNLLQAL
>gnl|CDD|410834 cd20060, FH_FOXO1, Forkhead (FH) domain found in Forkhead box protein O1 (FOXO1). FOXO1, also called Forkhead box protein O1A or Forkhead in rhabdomyosarcoma (FKHR), is a transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. It binds to the insulin response element (IRE) with the consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with the consensus sequence 5'-TT[G/A]TTTAC-3'. The FH domain is a winged helix DNA-binding domain
KSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLH
SKFIRVQNEGTGKSSWWMLNPEGGKSGKS
>gnl|CDD|410835 cd20061, FH_FOXO3, Forkhead (FH) domain found in Forkhead box protein O3 (FOXO3). FOXO3, also called AF6q21 protein or Forkhead in rhabdomyosarcoma-like 1 (FKHRL1), is a transcriptional activator which triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress. It recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3'. The FH domain is a winged helix DNA-binding domain. All FOXOs bind to the consensus sequence 5'-GTAAACAA-3', known as the DAF-16 family member-binding element, which includes the core sequence 5'-(A/C)AA(C/T)A-3' recognized by all FOX family members
WGNLSYADLITRAIESSPDKRLTLSQIYDWMVRCVPYFKDKGDSNSSAGWKNSIRHNLSLHSRFIRVQNE
GTGKSSWWMINPD
>gnl|CDD|410836 cd20062, FH_FOXO4, Forkhead (FH) domain found in Forkhead box protein O4 (FOXO4) and similar proteins. FOXO4, also called Fork head domain transcription factor AFX1, is a transcription factor involved in the regulation of the insulin signaling pathway. It binds to insulin-response elements (IREs) and can activate transcription of IGFBP1. The FH domain is a winged helix DNA-binding domain. All FOXOs bind to the consensus sequence 5'-GTAAACAA-3', known as the DAF-16 family member-binding element, which includes the core sequence 5'-(A/C)AA(C/T)A-3' recognized by all FOX family members
RNAWGNQSYAELISQAIESSPEKRLTLAQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIKV
HNEATGKSSWWMLNPE
>gnl|CDD|410837 cd20063, FH_FOXO6, Forkhead (FH) domain found in Forkhead box protein O6 (FOXO6) and similar proteins. FOXO6 acts as a transcriptional activator that may play an important role on tumor invasion, metastasis and prognosis. The FH domain is a winged helix DNA-binding domain. All FOXOs bind to the consensus sequence 5'-GTAAACAA-3', known as the DAF-16 family member-binding element, which includes the core sequence 5'-(A/C)AA(C/T)A-3' recognized by all FOX family members
GNLSYADLITKAIESSPDKRLTLSQIYDWMVRYVPYFKDKGDSNSSAGWKNSIRHNLSLHTRFIRVQNEG
TGKSSWWMLNPEGGKTGK
>gnl|CDD|410838 cd20064, FH_FOXP1, Forkhead (FH) domain found in Forkhead box protein P1 (FOXP1). FOXP1, also called Mac-1-regulated Forkhead (MFH), is a transcription factor that is widely expressed and has a broad range of functions. It has been shown to have a role in cardiac, lung, and lymphocyte development. Deregulation of FOXP1 is an important contributor to the pathogenesis of diffuse large B-cell lymphoma (DLBCL), suggesting it may function as an oncogene. Loss of FOXP1 expression in breast cancer is associated with a worse outcome, suggesting that FOXP1 may function as a tumor suppressor in some tissues. Haploinsufficiency of the FOXP1 gene leads to a neurodevelopmental disorder termed FOXP1 syndrome, characterized by developmental delay, intellectual disability, autism spectrum disorder, speech delay, and dysmorphic features. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
AEVRPPFTYASLIRQAILESPEKQLTLNEIYNWFTRMFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKG
AVWTVDEIEFQKRRPQK
>gnl|CDD|410839 cd20065, FH_FOXP2, Forkhead (FH) domain found in Forkhead box protein P2 (FOXP2). FOXP2, also called CAG repeat protein 44, or Trinucleotide repeat-containing gene 10 protein, is a transcriptional repressor that may play a role in the specification and differentiation of lung epithelium. It may also play a role in developing neural, gastrointestinal, and cardiovascular tissues. An arginine-to-histidine missense mutation (R553H) in the FOXP2 Forkhead domain has been linked to a severe speech and language disorder. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
VRPPFTYATLIRQAIMESSDRQLTLNEIYSWFTRTFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKGAV
WTVDEVEYQKRR
>gnl|CDD|410840 cd20066, FH_FOXP3, Forkhead (FH) domain found in Forkhead box protein P3 (FOXP3) and similar proteins. FOXP3, also called Scurfin, is a transcriptional regulator which is crucial for the development and inhibitory function of regulatory T-cells (Treg), which are required for maintaining self-tolerance. It may also have intrinsic regulatory function in conventional T (Tconv) cells. A deletion of the Forkhead domain arising from a frame-shift mutation in mouse FOXP3 is linked to the autoimmune disorder scurfy, and a similar congenital disease in humans is known as IPEX (immune dysregulation, polyendocrinopathy, enteropathy, X-linked syndrome). The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
RPPFTYASLIRWAILESPEKQLTLNEIYHWFTRMFAFFRNNTATWKNAVRHNLSLHKCFVRVENEKGAVW
TVDELEFQRRR
>gnl|CDD|410841 cd20067, FH_FOXP4, Forkhead (FH) domain found in Forkhead box protein P4 (FOXP4) and similar proteins. FOXP4, also called Forkhead-related protein-like A, is a transcriptional repressor that represses lung-specific expression. It is not required for T cell development, but is necessary for normal T cell cytokine recall responses to antigen following pathogenic infection. The FH domain is a winged helix DNA-binding domain. FOX transcription factors recognize the core sequence 5'-(A/C)AA(C/T)A-3'
RPPFTYASLIRQAILETPDRQLTLNEIYNWFTRMFAYFRRNTATWKNAVRHNLSLHKCFVRVENVKGAVW
TVDELEYQKRRPPKMTG
>gnl|CDD|410993 cd20069, 5TM_Oxa1-like, Five transmembrane core domain of mitochondrial inner membrane protein Oxa1 and similar proteins. This group is composed mostly of the mitochondrial members of the YidC/Oxa1/Alb3 protein family of insertases, including mitochondrial inner membrane proteins Oxa1, Oxa1-like (Oxa1L), cytochrome c oxidase assembly protein 18 (Cox18, also called Oxa2), and Arabidopsis thaliana mitochondrial ALBINO3-like protein 3 (ALB33). It also includes Arabidopsis thaliana chloroplastic ALBINO3-like protein 2 (ALB32). Members of this group mediate the insertion of both mitochondrion-encoded precursors and nuclear-encoded proteins from the matrix into the mitochondrial inner membrane. Oxa1 and Cox18/Oxa2 are essential for the activity and assembly of cytochrome c oxidase, playing central roles in the translocation and export of the N-terminal and C-terminal parts, respectively, of the COX2 protein into the mitochondrial intermembrane space. ALB32 may be involved in the insertion of integral membrane proteins into the chloroplast thylakoid membranes. YidC/Oxa1/Alb3 family insertases contain a core domain of five transmembrane (5TM) segments that is essential to insertase function
GLPWWATIAATTVALRLLLLPLVIKSQRNAARMANLQPELQKLQEKLKEARASGDQLEAAEARKELKELM
KKHNVNPLKSLLLPLVQAPVFISFFFALRKMANLPVPSFKTGGLLWFTDLTVPDPYYILPILTSLTFLAT
IELGAETGTSGSPQSKTMKNVFRGLPVLMIPFTANFPSAVFLYWITSNLFSLAQNLLLRIP
>gnl|CDD|410994 cd20070, 5TM_YidC_Alb3, Five transmembrane core domain of membrane protein insertase YidC, Alb3, and similar proteins. This group is composed of the bacterial and chloroplastic members of the YidC/Oxa1/Alb3 protein family of insertases, including bacterial YidC, and chloroplastic ALBINO3 (Alb3) and Alb3-like proteins such as ALBINO3-like protein 1 (also called Alb4). Membrane protein insertase YidC, also called foldase YidC or membrane integrase YidC, facilitates proper folding, insertion, and assembly of inner membrane proteins and complexes. Depending on the nature of the substrate, YidC functions in a Sec-independent (YidC only) or a Sec-dependent manner as part of a complex containing YidC, the SecYEG channel, and SecDFYajC. YidC from Gram-negative bacteria contains an extra transmembrane segment (TM1) at the N-terminus and a large periplasmic domain, located between TM1 and TM2, that adopts a beta-super sandwich fold that is found in sugar-binding proteins such as galactose mutarotase. Alb3 and Alb3-like proteins are required for the post-translational insertion of the light-harvesting chlorophyll-binding proteins (LHCPs) into the chloroplast thylakoid membrane. Alb3 acts independently and may also function cooperatively with the thylakoid cpSecYE translocase to insert proteins co-translationally into the thylakoid membrane, similar to bacterial YidC that can function with the SecYEG translocase. YidC/Oxa1/Alb3 family insertases contain a core domain of five transmembrane (5TM) segments that is essential to insertase function
GLAIILLTILIRLLLLPLTLKQYKSMKKMQELQPKIKEIQEKYKDDKQKLQQEMMKLYKEHGVNPLGGCL
PLLIQMPIFIALYQVLRNSIELRGAPFLWWILDLSAPDPYYILPILMGVTMFLQQKLTPTPTDDQAPQQK
MMMYFMPVMFTFIFLSFPSGLVLYWLVSNLFSIIQQLIINK
>gnl|CDD|380997 cd20071, SET_SMYD, SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing protein, and similar proteins. The family includes SET and MYND domain-containing proteins, SMYD1-SYMD5. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions
EVRESEGSKGRGLVATRDIEPGELILVEKPLVSVPSNSFSLTDGLNEIGVGLFPLASLLNHSCDPNAVVV
FDGNGTLRVRALRDIKAGEELTISYIDPLLPRTERRRELLEKYGFTCSCPRC
>gnl|CDD|380998 cd20072, SET_SET1, SET domain (including post-SET domain) found in catalytic component of the Saccharomyces cerevisiae COMPASS complex and similar proteins. The family contains mostly fungal SET domains, including SET1 found in the catalytic component of the Saccharomyces cerevisiae COMPASS (complex of proteins associated with Set1). SET1 is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex. The activity of this catalytic domain is established through forming a complex with a set of core proteins; it is extensively contacted by Cps60 (Bre2), Cps50 (Swd1), and Cps30 (Swd3)
DLLRFNQLKKRKKQLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGIGSSYLF
RIDDDTVVDATKKGNIARFINHCCDPNCTAKIIKVEGEKRIVIYAKRDIAAGEELTYDYKFPREEDKIPC
LCGAPNCR
>gnl|CDD|380999 cd20073, SET_SUV39H_Clr4-like, SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 methyltransferase Clr4, and similar proteins. This subfamily contains fission yeast Schizosaccharomyces pombe H3K9 methyltransferase Clr4 (also known as Suv39h), the sole homolog of the mammalian SUV39H1 and SUV39H2 enzymes, that has a critical role in preventing aberrant heterochromatin formation. It is known to di- and tri-methylate Lys-9 of histone H3, a central heterochromatic histone modification, with its specificity profile most similar to that of the human SUV39H2 homolog
IDFEFITSYRYGLGIEPPDPLFISGCSCSKLGGCDLNNPGSCQCLEDSNEKSFAYDEYGRVRANTGSIIY
ECNENCDCGINCPNRVVQRGRKLPLEIFKTKHKGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYD
NVGVTYLFDLDLFEDQVDEYYTVDAQYCGDVTRFINHSCDPNLAIYSVLRDKSDSKIYDLAFFAIKDIPA
LEELTFDYSGRNNFDQLGFIGNRSNSKYINLKNKRPCYCGSANCRGWLF
>gnl|CDD|410850 cd20074, XPF_nuclease_Mus81, XPF-like nuclease domain of Mus81. Mus81 is a crossover junction endonuclease that interacts with Eme1 and Eme2 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. The typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. Mus81 may be required in mitosis for the processing of stalled or collapsed replication forks. Mus81 consists of the active nuclease domain with the GDX(n)ERKX(3)D motif which is required for metal-dependent endonuclease activity and two helix-hairpin-helix (HhH2) domains
SYEVVLLVDNREVKGKKDRDYFQRELEKLGVKVETRSLPVGDFLWVARHKSDTGEELVLDYIVERKRLDD
LASSIKDGRYHEQKFRLKRSGIKNVIYLVEGDGSAQSGGLPEEALKTALANTQVVDGFFVKRTKSLDETV
RYLARLTRAL
>gnl|CDD|410851 cd20075, XPF_nuclease_XPF_arch, nuclease domain of XPF found in archaea. XPF, also called DNA excision repair protein ERCC-4, or DNA repair protein complementing XP-F cells, or Xeroderma pigmentosum group F-complementing protein, is a 3'-flap repair endonuclease that cleaves 5' of ds/ssDNA interfaces in 3' flap structures, although it also cuts bubble, Y-DNA structures and mobile and immobile Holliday junctions. XPF cuts preferentially after pyrimidines, may continue to progressively cleave substrate upstream of the initial cleavage, at least in vitro. It may be involved in nucleotide excision repair. The nuclease domains of the catalytic subunits XPF have the GDX(n)ERKX(3)D motif which is required for metal-dependent endonuclease activity but not for DNA junction binding. XPF-ERRC1 and its yeast homolog Rad1-Rad10 play key roles in the excision of DNA lesions and are required for certain types of homologous recombination events and for the repair of DNA cross-links
RIIVDSREKNSGVVRELKELGVEVEFKQLEVGDYIVSDRVAIERKTVDDFVSSIIDGRLFDQAKRLKEAY
EKPILIIEGDLLYLKRRIHPNAIRGALASIALDFGIPIIFTKDPEETAELLYSLAKR
>gnl|CDD|410852 cd20076, XPF_nuclease_FAAP24, XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24). FAAP24, also called Fanconi anemia core complex-associated protein 24, plays a role in DNA repair through recruitment of the Fanconi anemia (FA) core complex to damaged DNA. It regulates FANCD2 monoubiquitination upon DNA damage and induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed. FAAP24 may possess a high affinity toward single-stranded DNA (ssDNA). The nuclease domain of FAAP24 lacks the catalytic motif. The FANCM/FAAP24 complex is related to XPF/MUS81 endonucleases but lacks endonucleolytic activity. It binds branched DNA structures containing ssDNA regions, such as splayed-arm and 3'-flap DNA structures, and anchors the FA core complex to chromatin in repairing DNA interstrand crosslinks
GHILVNEKWRGSELVKSLQGKVKVIFEDGLGVVDFYPSNDCAVIYISEADLVAGNGYKRKLVKLRKANYL
RGIVIAEKTPMSEQYFPALQKFVVLELGLVLLPVTSQSEAAQLLIQMVNEETK
>gnl|CDD|410853 cd20077, XPF_nuclease_FANCM, XPF-like nuclease domain of Fanconi anemia group M protein (FANCM). FANCM (EC 3.6.4.13), also called Fanconi anemia-associated polypeptide of 250 kDa (FAAP250), or protein Hef ortholog, or ATP-dependent RNA helicase FANCM, is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA) and Holliday junction substrates. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, FANCM strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA
LVILVDSREISSGQEVISSLRIKHGIKVEVCQLGGCDYIVSNRMGVERKSLSEFANGSNRSKLVERIQHL
CDLYDRPCLIIEKDRVKPGETSRIFHRTKYYDSTLAALAQAGVRVLFSDSQEETARLLADLAQLEQRKN
>gnl|CDD|410854 cd20078, XPF_nuclease_XPF_euk, nuclease domain of XPF found in eukaryotes. XPF, also called DNA excision repair protein ERCC-4, or DNA repair protein complementing XP-F cells, or Xeroderma pigmentosum group F-complementing protein, is a DNA repair endonuclease that is a catalytic component of a structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. It is involved in homologous recombination that assists in removing interstrand cross-link. The nuclease domains of the catalytic subunits XPF have the GDX(n)ERKX(3)D motif which is required for metal-dependent endonuclease activity but not for DNA junction binding. XPF-ERRC1 and its yeast homolog Rad1-Rad10 play key roles in the excision of DNA lesions and are required for certain types of homologous recombination events and for the repair of DNA cross-links
KVIVDMREFRSSLPFLLHKAGIDLIPVTLEVGDYILSPDICVERKSISDLISSLNSGRLYTQLEAMCRYY
KHPILLIEFDENKPFSLQSKSSLSSEISSNSLISKLVLLLLHFPKLRIIWSRSPHFTAELFRELKK
>gnl|CDD|410855 cd20079, XPF_nuclease_ERCC1, XPF-like nuclease domain of DNA excision repair protein ERCC1. ERCC1 is a non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. In conjunction with SLX4, ERCC1 is responsible for the first step in the repair of interstrand cross-links (ICL), as well as for homology-directed repair (HDR) of DNA double-strand breaks. ERCC1 participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. ERCC1 also plays a critical role in targeting the XPF-ERCC1 complex to DNA. XPF-ERRC1 and its yeast homolog Rad1-Rad10 play key roles in the excision of DNA lesions and are required for certain types of homologous recombination events and for the repair of DNA cross-links. The critical motif, DX(n)ERKX(3)D, for endonuclease activity is absent in the nuclease domain of ERCC1
SILVNPRQRGNPILKFVRNVPWEFGDIVPDYVLGQTTCALFLSLRYHNLHPDYIHERLKQLGKSYELRVL
LVQVDVKDPHHALKELAKICILADCTLILAWSPEEAGRYLETYKA
>gnl|CDD|410856 cd20080, XPF_nuclease_EME-like, XPF-like nuclease domain of the family of Essential Meiotic Endonucleases (EMEs) and similar proteins. The family of EMEs includes EME1 and EME2. EME1, also called MMS4 homolog (hMMS4), interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Its typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. EME1 may be required in mitosis for the processing of stalled or collapsed replication forks. EME2 interacts with MUS81 to form a DNA structure-specific endonuclease which cleaves substrates such as 3'-flap structures. MUS81-EME2 is responsible for fork cleavage and restart in human cells. The MUS81-EME2 protein, whose actions are restricted to S phase, is also responsible for telomere maintenance in telomerase-negative ALT (Alternative Lengthening of Telomeres) cells. The nuclease domain of EMEs is a nuclease-like domain which is involved in targeting the MUS81-EME heterodimer complex to DNA. The family also includes budding yeast Mms4 (also known as Eme1 in other organisms), a putative transcriptional (co)activator that protects Saccharomyces cerevisiae cells from endogenous and environmental DNA damage. It interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. The nuclease domain of Mms4 lacks the catalytic motif
HIIVVLDPVLLQLEGGGQLLGALQTAECRCVIEAQAVPCSVTWRRRAGPSEDREDWVEEPTVLVLLRAEA
FVSYIDNGKQGSLDSTMKGKETLQGFVTDITAKTAGKALSLVIVDQEKIRVDAEEALVDLQLHTEAQAQI
VQSWKELADFTCAFTKAVAEAPFK
>gnl|CDD|410857 cd20081, XPF_nuclease_EME1, XPF-like nuclease domain of crossover junction endonuclease EME1. EME1, also called MMS4 homolog (hMMS4), interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Its typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. EME1 may be required in mitosis for the processing of stalled or collapsed replication forks. The nuclease domain of EME1 is a nuclease-like domain which is involved in targeting the MUS81-EME1 heterodimer complex to DNA
RPEECLKHIVVVLDPGLLQMEGGGQLLSALQAMECSCVIEAQAIPRSVTWRRRAAPSQVDEEDWVEEPTV
LVLLPAEEFVSMVHNYKQESLGSTTEGKETLQSFVTDITAKTAGKALSLVVVDMEKYFRVSRVDVEEALV
DLQLHTGVQVQFLETWKEFADFICMFTKAVAEAPFKKLR
>gnl|CDD|410858 cd20082, XPF_nuclease_EME2, XPF-like nuclease domain of crossover junction endonuclease EME2. EME2 interacts with MUS81 to form a DNA structure-specific endonuclease which cleaves substrates such as 3'-flap structures. MUS81-EME2 is responsible for fork cleavage and restart in human cells. The MUS81-EME2 protein, whose actions are restricted to S phase, is also responsible for telomere maintenance in telomerase-negative ALT (Alternative Lengthening of Telomeres) cells. The nuclease domain of EME2 is a nuclease-like domain which is involved in targeting the MUS81-EME2 heterodimer complex to DNA
RPEQCLKSLTVCVDPALLQDAGSDVLLEALSSLEWRYSIEPQSLPHSITWRRELPQDEPCCEAGTVEEDQ
VLMVLEPNEFLDMVASLKQVPNGDGSSGEMESLLGPLFEYLNKDPTKVVTLLVIGLDAYSWSNQLSGQKQ
KQLGSELGMTDLDIEEALVFLQLHKNVSVLFLESWQELTDHVCAVTKALSKRPFK
>gnl|CDD|410859 cd20083, XPF_nuclease_EME, XPF-like nuclease domain of crossover junction endonucleases, EME1, EME2 and similar proteins. The Mus81-EME1 complex is a structure-selective endonuclease with a critical role in the resolution of recombination intermediates during DNA repair after interstrand cross-links, replication fork collapse, or double-strand breaks. ERCC4 domain of Eme1 is a nuclease-like domain which is involved in targeting the MUS81-EME1 heterodimer complex to DNA
FIRVVIDPKILEESYGGELLSALQEKGLKYEIESQPIPNSITWTRNVPEDTVADNEVALEESEEDEPYVL
LILSAEEFVKMVKNGTLLDHISSVKSLFPNYPITLVIYGLNKYKRYHKKKEQSKKKKKNLKNVSRPPVEE
ALIELQLHAKCSSRLCETEAELALHVAQLTKAIAEAPYK
>gnl|CDD|410860 cd20085, XPF_nuclease_Mms4, XPF-like nuclease domain of Saccharomyces cerevisiae crossover junction endonuclease Mms4 and similar proteins. Budding yeast Mms4, also known as Eme1 in other organisms, is a putative transcriptional (co)activator that protects Saccharomyces cerevisiae cells from endogenous and environmental DNA damage. It interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks with regressed leading strands and nicked Holliday junctions. The nuclease domain of Mms4 lacks the catalytic motif
LAEVNKLKRDKEESTPEMIVDIPSSLLSSSLGSQLEELLKPLGVEHSTWDSPVPNIIRWRRKVTAEYDDE
LDHWEPIPERIEEEKHVLLYLTAKEFVELALGGNDLDSHVSKIKSLFPGKKVIYLIEGLTAWLRKNKNLR
NRQFAAAVRSQLSGSETSSRSAKSKKKALSAEYIDEDDIEDALLRLQVEHNVLIHHTNSPLETAEWIANF
TQHISTIPYK
>gnl|CDD|439080 cd20088, MBT, malignant brain tumor (MBT) repeat. The MBT repeat is a protein module that recognizes methylated lysine residues on histones and are thought to affect a variety of chromatin processes, including transcription. It exists as tandem repeats and is found in a number of nuclear proteins such as Drosophila sex comb on midleg protein. In the human genome, there are at least 9 MBT repeat proteins, each containing two, three or four MBT repeats. MBT repeat proteins use a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine (monomethyllysine and/or dimethyllysine)
FKVGMKLEAVDPLNPSEICVATVVKVVGGRLLLHFDGWDPSRYDFWCDVDSPDIHPVGWCE
>gnl|CDD|438853 cd20090, F-box_FBXW4, F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins. FBXW4, also called dactylin, or F-box and WD-40 domain-containing protein 4, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is likely to be involved in key signaling pathways crucial for normal limb development. It may participate in Wnt signaling and act as a novel tumor suppressor that regulates important cellular processes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression
PLLDLPDDLLFLIFSYLDPASLGRLSQVCRRLYRLISRDAVWRRIAR
>gnl|CDD|439081 cd20091, MBT_dScm-like_rpt1, first malignant brain tumor (MBT) repeat found in the sex comb on midleg family. The sex comb on midleg (Scm) family of Polycomb proteins includes Drosophila melanogaster Scm protein, as well as two vertebrate homologs of Scm, sex comb on midleg homolog 1 (SCMH1) and sex comb on midleg-like protein 2 (SCML2). Scm is a putative zinc finger protein that functions as a transcriptional regulator which represses multiple homeotic genes during embryonic stages. It coordinates Polycomb group (PcG) complexes, PRC1 (PcG-repressive complex 1) or PRC2 (PcG-repressive complex 2), and polymerizes to produce broad domains of PcG silencing. Both SCMH1 and SCML2 are components of PRC1, which acts as an E3 ubiquitin ligase both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. SCML2 is a germline-specific Polycomb protein that acts as a critical regulator of heterochromatin organization in spermatogenesis. Members of this family contain two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues
QSPIPPVNEFKVGMKLEAQDPRNLTSTCIATVVGIQGPRLRLRLDGSDNKNDFWRLVDSSDIHPVGWCEK
NGGLLQPPLGFRMNPSSWPMFLQKTLN
>gnl|CDD|439082 cd20092, MBT_dScm-like_rpt2, second malignant brain tumor (MBT) repeat found in the Polycomb protein sex comb on midleg family. The Sex comb on midleg (Scm) family of Polycomb proteins includes Drosophila melanogaster Scm protein, as well as two vertebrate homologs of Scm, Polycomb protein sex comb on midleg homolog 1 (SCMH1) and sex comb on midleg-like protein 2 (SCML2). Scm is a putative zinc finger protein that functions as a transcriptional regulator which represses multiple homeotic genes during embryonic stages. It coordinates Polycomb group (PcG) complexes, PRC1 (PcG-repressive complex 1) or PRC2 (PcG-repressive complex 2), and polymerizes to produce broad domains of PcG silencing. Both SCMH1 and SCML2 are components of PRC1, which acts as an E3 ubiquitin ligase both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. SCML2 is a germline-specific Polycomb protein that acts as a critical regulator of heterochromatin organization in spermatogenesis. Members of this family contain two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
PEKNMFKVGMKLEAVDRKNPQLICPATVGDVDGDEIHISFDGWRGAFDYWCRYDSRDIFPVGWCKKTGHP
LQPPG
>gnl|CDD|439083 cd20093, MBT_SFMBT_rpt1, first malignant brain tumor (MBT) repeat found in the Scm-like with four MBT domains protein (SFMBT) family. The SFMBT family includes SFMBT1 and SFMBT2. SFMBT1, also called renal ubiquitous protein 1, is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3 and functions as a chromatin reader in regulating epigenetic silencing and the myogenic gene program. It mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. SFMBT2, also called Scm-like with 4 MBT domains protein 2, is a transcriptional repressor of the HOXB13 gene. It is required for trophoblast maintenance and placenta development. It also negatively regulates cell migration and invasion in prostate cancer cells. Members of this family contain four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that contains a partially conserved semi-aromatic cage
QSGFKPGMKLEVPNKNNPDTYWVATVVMTCGPLLRLRYVGYEDDRSADFWCDLSSGDVHPIGWCAQNGKP
LQPPADIKEKELDWAEFLIKELTG
>gnl|CDD|439084 cd20094, MBT_SFMBT_rpt2, second malignant brain tumor (MBT) repeat found in the Scm-like with four MBT domains protein (SFMBT) family. The SFMBT family includes SFMBT1 and SFMBT2. SFMBT1, also called renal ubiquitous protein 1, is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3 and functions as a chromatin reader in regulating epigenetic silencing and the myogenic gene program. It mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. SFMBT2, also called Scm-like with 4 MBT domains protein 2, is a transcriptional repressor of the HOXB13 gene. It is required for trophoblast maintenance and placenta development. It also negatively regulates cell migration and invasion in prostate cancer cells. Members of this family contain four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains a partially conserved semi-aromatic cage
ADRIKVGMYLEVQDELNPYSVWIAKVLENVGGRLLLRYDGPEDSDSPDFWLFYLSPRLHPLGWAKSNGYT
YRPPKSLEKLHATEEWKAILQ
>gnl|CDD|439085 cd20095, MBT_SFMBT_rpt3, third malignant brain tumor (MBT) repeat found in the Scm-like with four MBT domains protein (SFMBT) family. The SFMBT family includes SFMBT1 and SFMBT2. SFMBT1, also called renal ubiquitous protein 1, is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3 and functions as a chromatin reader in regulating epigenetic silencing and the myogenic gene program. It mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. SFMBT2, also called Scm-like with 4 MBT domains protein 2, is a transcriptional repressor of the HOXB13 gene. It is required for trophoblast maintenance and placenta development. It also negatively regulates cell migration and invasion in prostate cancer cells. Members of this family contain four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues
FKVGMKLEALHPKNPSTICPATVTKVFNEYYFLVEIDDLRPEESEKITFVCHANSPGIFPVGWCAKNGLR
LTPPPGYPKSEFDWDSYLKLCG
>gnl|CDD|439086 cd20096, MBT_SFMBT_rpt4, fourth malignant brain tumor (MBT) repeat found in the Scm-like with four MBT domains protein (SFMBT) family. The SFMBT family includes SFMBT1 and SFMBT2. SFMBT1, also called renal ubiquitous protein 1, is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3 and functions as a chromatin reader in regulating epigenetic silencing and the myogenic gene program. It mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. SFMBT2, also called Scm-like with 4 MBT domains protein 2, is a transcriptional repressor of the HOXB13 gene. It is required for trophoblast maintenance and placenta development. It also negatively regulates cell migration and invasion in prostate cancer cells. Members of this family contain four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the fourth MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues
FERGMKLEAVNPENPNQICVATITKVVGPLLWLHLDSEKKLSPNIIVDVESTDIFPVGWCESNGYPLVTP
RKY
>gnl|CDD|439087 cd20097, MBT_dSfmbt-like_rpt1, first malignant brain tumor (MBT) repeat found in the Drosophila melanogaster Polycomb protein Sfmbt (dSfmbt)-like family. The dSfmbt-like family includes Drosophila melanogaster Scm-like with four MBT domain-containing protein 1 (dSfmbt), as well as its two vertebrate homologs, MBT domain-containing protein 1 (MBTD1) and Lethal(3)malignant brain tumor-like protein 2 (L3MBTL2). dSfmbt is a Polycomb group (PcG) repressor involved in epigenetic regulation of gene expression. MBTD1 and L3MBTL2, also called L(3)mbt-like protein 2, are putative PcG proteins that specifically bind to monomethylated and dimethylated 'Lys-20' on histone H4. L3MBTL2 also binds histone H3 peptides which are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. Members of this family contain four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that contains a partially conserved semi-aromatic cage
WEKVKIGVKVEVANRDDDKPTDNVKVYWFARIIKVAGYRVLLRYEGYDEDSSHDFWINLCSNEIHPIGYA
AENGKILVPPKSIEDKENDWKEYIMKRLHGKRTIP
>gnl|CDD|439088 cd20098, MBT_dSfmbt-like_rpt2, second malignant brain tumor (MBT) repeat found in the Drosophila melanogaster Polycomb protein Sfmbt (dSfmbt)-like family. The dSfmbt-like family includes Drosophila melanogaster Scm-like with four MBT domain-containing protein 1 (dSfmbt), as well as its two vertebrate homologs, MBT domain-containing protein 1 (MBTD1) and Lethal(3)malignant brain tumor-like protein 2 (L3MBTL2). dSfmbt is a Polycomb group (PcG) repressor involved in epigenetic regulation of gene expression. MBTD1 and L3MBTL2, also called L(3)mbt-like protein 2, are putative PcG proteins that specifically bind to monomethylated and dimethylated 'Lys-20' on histone H4. L3MBTL2 also binds histone H3 peptides which are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. Members of this family contain four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that does not seem to contain a semi-aromatic cage and may not bind methylated lysine residues
DFHEKVLESLKSTPFKVGMRLEVVDKMCISRTRVAVVEEVVGGRLRLQYVDSEDDDDDFWCHMKSPLIHP
VGWSQAVGHKIRA
>gnl|CDD|439089 cd20099, MBT_dSfmbt-like_rpt3, third malignant brain tumor (MBT) repeat found in the Drosophila melanogaster Polycomb protein Sfmbt (dSfmbt)-like family. The dSfmbt-like family includes Drosophila melanogaster Scm-like with four MBT domain-containing protein 1 (dSfmbt), as well as its two vertebrate homologs, MBT domain-containing protein 1 (MBTD1) and Lethal(3)malignant brain tumor-like protein 2 (L3MBTL2). dSfmbt is a Polycomb group (PcG) repressor involved in epigenetic regulation of gene expression. MBTD1 and L3MBTL2, also called L(3)mbt-like protein 2, are putative PcG proteins that specifically bind to monomethylated and dimethylated 'Lys-20' on histone H4. L3MBTL2 also binds histone H3 peptides which are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. Members of this family contain four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that does not seem to contain a semi-aromatic cage and may not bind methylated lysine residues
FKVGMKLEAVDPLNLSSICVATVRKVLRFGYLVIGIDGPSADDGSDWFCCHASSPFIFPVGFAEKNGIEL
TPPRGYESKPFDWEEYLEETG
>gnl|CDD|439090 cd20100, MBT_dSfmbt-like_rpt4, fourth malignant brain tumor (MBT) repeat found in the Drosophila melanogaster Polycomb protein Sfmbt (dSfmbt)-like family. The dSfmbt-like family includes Drosophila melanogaster Scm-like with four MBT domain-containing protein 1 (dSfmbt), as well as its two vertebrate homologs, MBT domain-containing protein 1 (MBTD1) and Lethal(3)malignant brain tumor-like protein 2 (L3MBTL2). dSfmbt is a Polycomb group (PcG) repressor involved in epigenetic regulation of gene expression. MBTD1 and L3MBTL2, also called L(3)mbt-like protein 2, are putative PcG proteins that specifically bind to monomethylated and dimethylated 'Lys-20' on histone H4. L3MBTL2 also binds histone H3 peptides which are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. Members of this family contain four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the fourth MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
HGFKVGMKLEAVDLMEPRLICVATVTRVVGRLLRVHFDGWDDEFDQWVDCDSPDIYPVGWCELVGYPLQP
P
>gnl|CDD|439091 cd20101, MBT_L3MBTL1-like_rpt1, first malignant brain tumor (MBT) repeat found in the Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1)-like family. The L3MBTL1-like family includes L3MBTL1, L3MBTL3, and L3MBTL4. L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a PcG protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a PcG protein that may act as a tumor suppressor. Members of this family contain three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that contains the semi-aromatic cage and may bind methylated lysine residues
FNKNGFKVGMKLEGIDPKHPSLFCVLSVAEVRGYRLRLHFDGYSECYDFWVNADSPDIFPVGWCEKTGHK
LQPPKGYTSETFSWSAYLKLTKAQAAPKHLF
>gnl|CDD|439092 cd20102, MBT_L3MBTL1-like_rpt2, second malignant brain tumor (MBT) repeat found in the Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1)-like family. The L3MBTL1-like family includes L3MBTL1, L3MBTL3, and L3MBTL4. L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a PcG protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a PcG protein that may act as a tumor suppressor. Members of this family contain three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
PHGFRVGMKLEAVDRKNPSLICVATVTDVIGNRFLVHFDGWDDSYDYWCDPDSPYIHPVGWCEENGKTLQ
PPKGYSPGNFSWDKYLEETN
>gnl|CDD|439093 cd20103, MBT_L3MBTL1-like_rpt3, third malignant brain tumor (MBT) repeat found in the Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1)-like family. The L3MBTL1-like family includes L3MBTL1, L3MBTL3, and L3MBTL4. L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a PcG protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a PcG protein that may act as a tumor suppressor. Members of this family contain three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues
PPHGFEVGMKLEAVDKRNPRLIRVATVADVEDYRVKLHFDGWPDIYDFWVDDDSPDIHPPGWCSKTGHPL
EPP
>gnl|CDD|439094 cd20104, MBT_PHF20L1-like, malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and similar domains. PHF20L1 associates with SOX2, antagonizes SOX2 ubiquitination and the sequential degradation induced by MLL1/WDR5 complexes. It binds both monomethylated Lys-42 and Lys-117 in SOX2 and thereby prevents SOX2 proteolysis. PHF20L1 also reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 degradation. PHF20L1 contains one MBT (malignant brain tumor) repeat. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the MBT repeat of PHF20L1 and similar domains that contains the semi-aromatic cage that may bind methylated lysine residues
FKVGDRVDALDGEGKWYEAKIVEVDEEENKVLVHYDGWSSRYDEWIDRDSERLRPLHTPT
>gnl|CDD|439095 cd20105, MBT_SCMH1_rpt1, first malignant brain tumor (MBT) repeat found in Polycomb protein sex comb on midleg homolog 1. Sex comb on midleg homolog 1 (SCMH1) is a homolog of Drosophila Sex comb on midleg (Scm). It is a component of PRC1 (Polycomb repressive complex 1), which acts as an E3 ubiquitin ligase, both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. It contains two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues
HFSWDKYLKETGAVPAPVHCFKQSYTPPVNEFKIGMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSD
NKNDFWRLVDSSEIQPIGNCEKNGGMLQPPLGFRLNASSWPMFLLKTLNGAEMAPVRIFHK
>gnl|CDD|439096 cd20106, MBT_SCML2_rpt1, first malignant brain tumor (MBT) repeat found in sex comb on midleg-like protein 2. Sex comb on midleg-like protein 2 (SCML2) is a homolog of Drosophila Sex comb on midleg (Scm). It is a component of PRC1 (Polycomb repressive complex 1), which acts as an E3 ubiquitin ligase, both for histone H2A to silence transcription and for geminin to regulate its stability. SCML2 is a germline-specific Polycomb protein that acts as a critical regulator of heterochromatin organization in spermatogenesis. SCML2 contains two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues
QSRIPPVNDFKVGMKLEARDPRNATSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPIGTCEK
EGDMLQPPLGFQMNASSWPMFLLRTLNG
>gnl|CDD|439097 cd20107, MBT_dScm_rpt1, first malignant brain tumor (MBT) repeat found in Drosophila melanogaster Polycomb protein sex comb on midleg and similar proteins. Sex comb on midleg (Scm) is a putative zinc finger protein that functions as a transcriptional regulator which represses multiple homeotic genes during embryonic stages. It coordinates Polycomb group (PcG) complexes, PRC1 (PcG-repressive complex 1) or PRC2 (PcG-repressive complex 2), and polymerizes to produce broad domains of PcG silencing. Scm contains two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues
QAQNPPKNEFKIGMKLEALDPRNVTSTCIATVVGVLGPRLRLRLDGSDNKNDFWRLVDSTEIHPIGHCEK
NGGMLQPPLGFRMNASSWPMFLLKTLNNA
>gnl|CDD|439098 cd20108, MBT_SCMH1_rpt2, second malignant brain tumor (MBT) repeat found in Polycomb protein sex comb on midleg homolog 1 (SCMH1) and similar proteins. SCMH1 is a homolog of Drosophila Sex comb on midleg (Scm). It is a component of PRC1 (Polycomb repressive complex 1), which acts as an E3 ubiquitin ligase, both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. It contains two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
PSQNFFKTGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRYDSRDIFPVGWCSLTGDN
LQPPG
>gnl|CDD|439099 cd20109, MBT_SCML2_rpt2, second malignant brain tumor (MBT) repeat found in sex comb on midleg-like protein 2 (SCML2) and similar proteins. SCML2 is a homolog of Drosophila Sex comb on midleg (Scm). It is a component of PRC1 (Polycomb repressive complex 1), which acts as an E3 ubiquitin ligase, both for histone H2A to silence transcription and for geminin to regulate its stability. SCML2 is a germline-specific Polycomb protein that acts as a critical regulator of heterochromatin organization in spermatogenesis. SCML2 contains two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
PPLNNFKVGMKLEAIDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCRLTGDV
LQPPGNS
>gnl|CDD|439100 cd20110, MBT_dScm_rpt2, second malignant brain tumor (MBT) repeat found in Drosophila melanogaster Polycomb protein sex comb on midleg (Scm) and similar proteins. Scm is a putative zinc finger protein that functions as a transcriptional regulator which represses multiple homeotic genes during embryonic stages. It coordinates Polycomb group (PcG) complexes, PRC1 (PcG-repressive complex 1) or PRC2 (PcG-repressive complex 2), and polymerizes to produce broad domains of PcG silencing. Scm contains two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
PESNLFKVGMKLEAVDRKNPHLICPATVGAVKDDQIFVTFDGWRGAFDYWCRYDSRDIFPVGWCARSGHP
LQPPG
>gnl|CDD|439101 cd20111, MBT_SFMBT1_rpt1, first malignant brain tumor (MBT) repeat found in Scm-like with four MBT domains protein 1 (SFMBT1). SFMBT1, also called renal ubiquitous protein 1, is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3 and functions as a chromatin reader in regulating epigenetic silencing and the myogenic gene program. It mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. SFMBT1 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that contains a partially conserved semi-aromatic cage
QNGFSPGMKLEVAVRTDPNTYWVATIITTCGQLLLLRYDGYGEDRRADFWCDIMTADLHPIGWCEQNGKT
LRPPEGIRDKLSDWEEFLAQTLTG
>gnl|CDD|439102 cd20112, MBT_SFMBT2_rpt1, first malignant brain tumor (MBT) repeat found in Scm-like with four MBT domains protein 2 (SFMBT2). SFMBT2, also called Scm-like with 4 MBT domains protein 2, is a transcriptional repressor of the HOXB13 gene. It is required for trophoblast maintenance and placenta development. It also negatively regulates cell migration and invasion in prostate cancer cells. SFMBT2 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that contains a partially conserved semi-aromatic cage
QSSFQPGMKLEVANKSNPDTYWVATIITTCGQLLLLRYCGYGDDRRADFWCDVMTADLHPVGWCTQNNKV
LMPPDAIKEKYTDWTEFLIHDLTG
>gnl|CDD|439103 cd20113, MBT_SFMBT1_rpt2, second malignant brain tumor (MBT) repeat found in Scm-like with four MBT domains protein 1 (SFMBT1). SFMBT1, also called renal ubiquitous protein 1, is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3 and functions as a chromatin reader in regulating epigenetic silencing and the myogenic gene program. It mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. SFMBT1 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains a partially conserved semi-aromatic cage
LDLIGPGSRLELQDFQDSLVAWIVVVVENIGGRLKLRYEGLEGSDKSDTWLFYLDPFLHQVGWAAQHGYT
LQPPAAIRHLKSEAEWQEILKKVKEEEEE
>gnl|CDD|439104 cd20114, MBT_SFMBT2_rpt2, second malignant brain tumor (MBT) repeat found in Scm-like with four MBT domains protein 2 (SFMBT2). SFMBT2, also called Scm-like with 4 MBT domains protein 2, is a transcriptional repressor of the HOXB13 gene. It is required for trophoblast maintenance and placenta development. It also negatively regulates cell migration and invasion in prostate cancer cells. SFMBT2 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains a partially conserved semi-aromatic cage
VDLITVGSLIELQDSQNPFQYWIVRVIENVGGRLRLRYVGLEDESHDQWLFYLDTRLRPVGWCQENNLRM
EPPTEICDLKSASEWKEALEKSLAEAAN
>gnl|CDD|439105 cd20115, MBT_SFMBT1_rpt3, third malignant brain tumor (MBT) repeat found in Scm-like with four MBT domains protein 1 (SFMBT1). SFMBT1, also called renal ubiquitous protein 1, is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3 and functions as a chromatin reader in regulating epigenetic silencing and the myogenic gene program. It mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. SFMBT1 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues
HCFSEGMKLEAVDPAAPFTISPATVAKVFNEKFFLVEMDDLRPEEAGAHSFVCHRDSPGIFPVQWSLKNG
LHLSPPPGYPGQDFDWADYLKQCG
>gnl|CDD|439106 cd20116, MBT_SFMBT2_rpt3, three malignant brain tumor (MBT) repeat found in Scm-like with four MBT domains protein 2 (SFMBT2). SFMBT2, also called Scm-like with 4 MBT domains protein 2, is a transcriptional repressor of the HOXB13 gene. It is required for trophoblast maintenance and placenta development. It also negatively regulates cell migration and invasion in prostate cancer cells. SFMBT2 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues
HSFTVGMKLEVVDPREPFHICPASVTKVFNNHYFQVTVDDLRPEASENSMLCHADSLGILPVQWCLKNGV
NLTPPKGYSGQDFDWADYQKQCG
>gnl|CDD|439107 cd20117, MBT_SFMBT1_rpt4, fourth malignant brain tumor (MBT) repeat found in Scm-like with four MBT domains protein 1 (SFMBT1). SFMBT1, also called renal ubiquitous protein 1, is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3 and functions as a chromatin reader in regulating epigenetic silencing and the myogenic gene program. It mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. SFMBT1 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the fourth MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues
HCFKENMKLEAVNPICPEEICVATVTKVKGSYLWLQLEGSKKPIPECIVHVESMDIFPVGWCETNGYPLL
HPRKARVNKQRKIAVVQPEK
>gnl|CDD|439108 cd20118, MBT_SFMBT2_rpt4, fourth malignant brain tumor (MBT) repeat found in Scm-like with four MBT domains protein 2 (SFMBT2). SFMBT2, also called Scm-like with 4 MBT domains protein 2, is a transcriptional repressor of the HOXB13 gene. It is required for trophoblast maintenance and placenta development. It also negatively regulates cell migration and invasion in prostate cancer cells. SFMBT2 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the fourth MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues
GFTKNMKLEAVNPRNPAEICVASITSVKGRLLWLHLEGLQNPVPEYIVDVESMDIFPVGWCEANGYPLTP
PHKAVCKKKRKIAVVQPEKQL
>gnl|CDD|439109 cd20119, MBT_dSfmbt_rpt1, first malignant brain tumor (MBT) repeat found in Drosophila melanogaster Polycomb protein Sfmbt (dSfmbt) and similar proteins. dSfmbt, also called Scm-like with four MBT domain-containing protein 1, is a Polycomb group repressor involved in epigenetic regulation of gene expression. dSfmbt contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that contains a partially conserved semi-aromatic cage
WDNITVGMKVEVENTDTDLIEDPTSFWIATVLKIAGYKALMRYEGFGTDDSKDFWVNLCSEDVHPVGWCA
TRGKPLIPPRTIEHKYSDWKEFLVKRLTGARTLP
>gnl|CDD|439110 cd20120, MBT_MBTD1_rpt1, first malignant brain tumor (MBT) repeat found in MBT domain-containing protein 1 (MBTD1). MBTD1 is a putative Polycomb group (PcG) protein that specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4. MBTD1 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that contains a partially conserved semi-aromatic cage
WGDIAEGVRVEVPNTDCNLPTKVFWIAGIVKLAGYKALLRYEGFENDSSLDFWCNICGSDIHPVGWCATS
GKPLVPPKTIQHKYTNWKAFLVKRLTGAKTLPP
>gnl|CDD|439111 cd20121, MBT_L3MBTL2_rpt1, first malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 2 (L3MBTL2) and similar proteins. L3MBTL2, also called L(3)mbt-like protein 2, is a putative Polycomb group (PcG) protein that binds to monomethylated and dimethylated 'Lys-20' on histone H4 and also binds histone H3 peptides which are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. L3MBTL2 orchestrates ubiquitin signalling by dictating the sequential recruitment of RNF8 and RNF168 after DNA damage. It is an integral component of the polycomb repressive complex 1.6 (PRC1.6) and has been implicated in transcriptional repression and chromatin compaction. L3MBTL2 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that contains a partially conserved semi-aromatic cage
WEDVMEGMKVEVLNTDAVLPSRVYWIASVIQLAGYKALLRYEGFENDSSHDFWCNLGTVDVHPIGWCAIN
SKILVPPQTIHAKFTDWRGYLMKRLVGSRTIP
>gnl|CDD|439112 cd20122, MBT_dSfmbt_rpt2, second malignant brain tumor (MBT) repeat found in Drosophila melanogaster Polycomb protein Sfmbt (dSfmbt) and similar proteins. dSfmbt, also called Scm-like with four MBT domain-containing protein 1, is a Polycomb group repressor involved in epigenetic regulation of gene expression. dSfmbt contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that does not seem to contain a semi-aromatic cage and may not bind methylated lysine residues
NFHNKVNESLRSRFRLGLNLECVDKNRISQVRVATVTKIVGKRLHLRYEGSEPDDDGFWCHEDSPLIHPV
GWAQTVGHNLAAS
>gnl|CDD|439113 cd20123, MBT_MBTD1_rpt2, second malignant brain tumor (MBT) repeat found in MBT domain-containing protein 1 (MBTD1). MBTD1 is a putative Polycomb group (PcG) protein that specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4. MBTD1 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that does not seem to contain a semi-aromatic cage and may not bind methylated lysine residues
DFSQKVSESMQYPFKPCMRVEVVDKTHLCRTRVAVVESVIGGRLRLVYEESEDGTDDFWCHMYSPLIHHI
GWSRSIGHRFKRSDI
>gnl|CDD|439114 cd20124, MBT_L3MBTL2_rpt2, second malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 2 (L3MBTL2). L3MBTL2, also called L(3)mbt-like protein 2, is a putative Polycomb group (PcG) protein that binds to monomethylated and dimethylated 'Lys-20' on histone H4 and also binds histone H3 peptides which are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. L3MBTL2 orchestrates ubiquitin signalling by dictating the sequential recruitment of RNF8 and RNF168 after DNA damage. It is an integral component of the polycomb repressive complex 1.6 (PRC1.6) and has been implicated in transcriptional repression and chromatin compaction. L3MBTL2 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that does not seem to contain a semi-aromatic cage and may not bind methylated lysine residues
DFHIKMAESMKYPFRQGMRVEVVDKSQVSRTRMAVVDTVIGGRLRLLYEDGDSDDDFWCHMWSPLIHPVG
WSRRVGHSIKMSDR
>gnl|CDD|439115 cd20125, MBT_dSfmbt_rpt3, third malignant brain tumor (MBT) repeat found in Drosophila melanogaster Polycomb protein Sfmbt (dSfmbt) and similar proteins. dSfmbt, also called Scm-like with four MBT domain-containing protein 1, is a Polycomb group repressor involved in epigenetic regulation of gene expression. dSfmbt contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that does not seem to contain a semi-aromatic cage and may not bind methylated lysine residues
FKEGMKLEAVDPLNLSAICVATVMKVLRFGYLMIRIDSYEPDASGSDWFCYHESSPCIFPAGFCEVNNIT
LTPPNGYDGRTFTWEGYLRQTGATAAPQHLFHRIIPD
>gnl|CDD|439116 cd20126, MBT_MBTD1_rpt3, third malignant brain tumor (MBT) repeat found in MBT domain-containing protein 1 (MBTD1). MBTD1 is a putative Polycomb group (PcG) protein that specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4. MBTD1 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that does not seem to contain a semi-aromatic cage and may not bind methylated lysine residues
FKEGMKLEAIDPLNLSTICVATVRKVLANGYLMIGIDGSEAADGSDWFCYHATSPSIFPVGFCEINMIEL
TPPRGYKKPFKWFDYLRETG
>gnl|CDD|439117 cd20127, MBT_L3MBTL2_rpt3, third malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 2 (L3MBTL2). L3MBTL2, also called L(3)mbt-like protein 2, is a putative Polycomb group (PcG) protein that binds to monomethylated and dimethylated 'Lys-20' on histone H4 and also binds histone H3 peptides which are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. L3MBTL2 orchestrates ubiquitin signalling by dictating the sequential recruitment of RNF8 and RNF168 after DNA damage. It is an integral component of the polycomb repressive complex 1.6 (PRC1.6) and has been implicated in transcriptional repression and chromatin compaction. L3MBTL2 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that does not seem to contain a semi-aromatic cage and may not bind methylated lysine residues
FEEGMKLEAIDPLNLGNICVATVCKVLLDGYLMIGIDGGPSTDGSDWFCYHASSHAIFPVGFCQKNDIEL
TPPKGYDAQTFNWENYLEKTK
>gnl|CDD|439118 cd20128, MBT_dSfmbt_rpt4, fourth malignant brain tumor (MBT) repeat found in Drosophila melanogaster Polycomb protein Sfmbt (dSfmbt). dSfmbt, also called Scm-like with four MBT domain-containing protein 1, is a Polycomb group repressor involved in epigenetic regulation of gene expression. dSfmbt contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the fourth MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
HGFEVGMSLECADLMDPRLVCVATVARVVGRLLKVHFDGWTDEYDQWLDCESADIYPVGWCVLVNHKLEG
PP
>gnl|CDD|439119 cd20129, MBT_MBTD1_rpt4, fourth malignant brain tumor (MBT) repeat found in MBT domain-containing protein 1 (MBTD1). MBTD1 is a putative Polycomb group (PcG) protein that specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4. MBTD1 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the fourth MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
HGFRVGMKLEAVDLMEPRLVCVATVTRIIHRLLRIHFDGWEDEYDQWVDCESPDLYPVGWCQLTGYQLQP
P
>gnl|CDD|439120 cd20130, MBT_L3MBTL2_rpt4, fourth malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 2 (L3MBTL2). L3MBTL2, also called L(3)mbt-like protein 2, is a putative Polycomb group (PcG) protein that binds to monomethylated and dimethylated 'Lys-20' on histone H4 and also binds histone H3 peptides which are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. L3MBTL2 orchestrates ubiquitin signalling by dictating the sequential recruitment of RNF8 and RNF168 after DNA damage. It is an integral component of the polycomb repressive complex 1.6 (PRC1.6) and has been implicated in transcriptional repression and chromatin compaction. L3MBTL2 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the fourth MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
CPNHGFKVGMKLEAVDLMEPRLICVATVKRVVHRLLSIHFDGWDSEYDQWVDCESPDIYPVGWCELTGYQ
LQPPV
>gnl|CDD|439121 cd20131, MBT_L3MBTL1_rpt1, first malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1). L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL1 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that contains the semi-aromatic cage and may bind methylated lysine residues
FQDSQAVTHNKNGFKLGMKLEGIDPQHPSMYFILTVAEVCGYRLRLHFDGYSECHDFWVNANSPDIHPAG
WFEKTGHKLQPPKGYKEEEFSWSQYLRSTRAQAAPKHLF
>gnl|CDD|439122 cd20132, MBT_L3MBTL3_rpt1, first malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 3 (L3MBTL3). L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a Polycomb group (PcG) protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL3 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
YNKNGFKVGMKLEGVDPEHQSMYCVLTVAEVCGYRIRLHFDGYSDCYDFWVNADSPDIHPVGWCEKTGHK
LHPPKGYKEEEFNWQSYLKTCKAQAAPKSLF
>gnl|CDD|439123 cd20133, MBT_L3MBTL4_rpt1, first malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 4 (L3MBTL4). L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a Polycomb group (PcG) protein that may act as a tumor suppressor. L3MBTL4 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
QSRNGFKVGMRLEGIDPEHPSLFCVLSVAEVQGYRLRLHFDGYSECYDFWVNADSPDIHPVGWCEKTGHK
LLPPKGYKDGEFNWSSYLKTCKAQAAPKNLF
>gnl|CDD|439124 cd20134, MBT_L3MBTL1_rpt2, second malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1). L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL1 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
PPPLGFQVGMKLEAVDRMNPSLVCVASVTDVVDSRFLVHFDNWDDTYDYWCDPSSPYIHPVGWCQKQGKP
LTPPQDYPDPDNFSWEKYLEETG
>gnl|CDD|439125 cd20135, MBT_L3MBTL3_rpt2, second malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 3 (L3MBTL3). L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a Polycomb group (PcG) protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL3 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
VTPSGFRVGMKLEAVDKKNPSFICVATITDMVDNRLLIHFDNWDESYDYWCDASSPYIHPVGYCQEHGRT
LTTPPGYKDPKHFSWEKYLEETN
>gnl|CDD|439126 cd20136, MBT_L3MBTL4_rpt2, second malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 4 (L3MBTL4). L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a Polycomb group (PcG) protein that may act as a tumor suppressor. L3MBTL4 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues
MPKEFQVGMKLEAVDRKNPSLVCVATIADIVEDRLLVHFDNWDDSYDYWCDVNSPYIQPVGWCQENGRTL
VAPQGYPNPEKFSWTEYLEATQ
>gnl|CDD|439127 cd20137, MBT_L3MBTL1_rpt3, third malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1). L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL1 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues
PPHGFQVNMKLEAVDRRNPALIRVASVEDVEDHRIKIHFDGWSHGYDFWIDADHPDIHPAGWCSKTGHPL
QPPLG
>gnl|CDD|439128 cd20138, MBT_L3MBTL3_rpt3, third malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 3 (L3MBTL3). L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a Polycomb group (PcG) protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL3 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues
FKVKPPHGFQKNMKLEVVDKRNPMLIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPAGWCAKT
GHPLQPPL
>gnl|CDD|439129 cd20139, MBT_L3MBTL4_rpt3, fourth malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 4 (L3MBTL4). L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a Polycomb group (PcG) protein that may act as a tumor suppressor. L3MBTL4 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues
FKLRPPHGFQVNMKLEAVDKRNPILIRVATIVDKDDHRIKLHFDGWDHNYDFWVDADSPDIHPVGWCDKT
GHALQVPLGASD
>gnl|CDD|438968 cd20140, PWWP_PWWP2, PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family. The PWWP2 family includes PWWP2A and its paralog PWWP2B. PWWP2A is a H2A.Z-specific chromatin binding protein which may play an important role in the neural crest stem cell migration and differentiation during early development. It is also required for proper mitosis progression. PWWP2A and PWWP2B form a stable complex with NuRD subunits MTA1/2/3:HDAC1/2:RBBP4/7, but not with MBD2/3, p66alpha/beta, and CHD3/4. The PWWP domain specifically recognizes DNA and histone methylated lysines
GRTLRVGDIVWGKIHGFPWWPGRILSITVSRDDNGELSTQEAHVSWFGSSTTSYMPCSQLYPFLEDFKLR
YNKKKRGPYKEAVRQALEAAKQ
>gnl|CDD|438969 cd20141, PWWP_MBD5, PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins. MBD5, is a methyl-CpG-binding protein that binds to heterochromatin. It does not interact with either methylated or unmethylated DNA. MBD5 acts as a transcriptional regulator responsible for 2q23.1 deletion syndrome. It belongs to the MBD family proteins, which play central roles in transcriptional regulation and development. The PWWP domain specifically recognizes DNA and histone methylated lysines
FNVGDLVWGQIRGFPSWPGKLVSENDVGKTNEGKVWVSWFGDHSFGQVEPDKLKTLSEGLEAHHRARKRT
RKGRKLNNHLEAAIQEAMSELD
>gnl|CDD|438970 cd20142, PWWP_AtATX1-like, PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like proteins ATX1, ATX2, and similar proteins. This family includes A. thaliana ATX1 and ATX2, which are sister paralogs originating from a segmental chromosomal duplication. They are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1 regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain containing proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. The PWWP domain specifically recognizes DNA and histone methylated lysines
SPGDVVWAKVKGYPMWPALVIDEEHAERCGLEANRPGKKGTVPVQFFGTYEVARLNPKKVVGFSKGLDLK
YHSKCKAPVFRQALEEAERYLKEGKLP
>gnl|CDD|438971 cd20143, PWWP_AtATX3-like, PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like protein ATX3, ATX4, ATX5, and similar proteins. The family includes A. thaliana ATX3 (also called protein SET domain group 14, or trithorax-homolog protein 3), ATX4 (also called protein SET domain group 16, or trithorax-homolog protein 4) and ATX5 (also called protein SET domain group 29, or trithorax-homolog protein 5), which belong to the histone-lysine methyltransferase family. They show distinct phylogenetic origins from the family of ATX1 and ATX2. They are multi-domain containing protein that consists of an N-terminal PWWP domain, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. The PWWP domain specifically recognizes DNA and histone methylated lysines
VEGDLVWAKVGTHPFWPARVVEPAEQAEEVRRRCVPGSLCVYFFGPGGSRDYGWVRRSMIFPFTDDLARF
QTQKIKNKKRPQEFQEALEEAKLADAGFEE
>gnl|CDD|438972 cd20144, PWWP_NSD_rpt1, first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins. The nuclear receptor binding SET domain (NSD) protein family consists of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1 that are critical in maintaining the chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising in suppressing cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and play nonredundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, through mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). This model corresponds to the first PWWP domain. This family also includes Drosophila melanogaster maternal-effect sterile 4 (dMes4) that may act as a histone-lysine N-methyltransferase required for wing morphogenesis. The PWWP domain specifically recognizes DNA and histone methylated lysines
VGDLVWAKVSGHPWWPCMVTYDPESGLYTKIKGSGGRTYRQYHVQFFGDNGERGWVSEKSLMPFEGKEKF
EELVKELKKKAKKKSKKAKLEKKVKPSRRKKWEIAVEEAEEALP
>gnl|CDD|438973 cd20145, PWWP_ZCWPW1, PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins. ZCWPW1 is a histone H3K4me3 reader. It is associated with late-onset Alzheimer's disease (LOAD). In addition to the PWWP domain, ZCWPW1 contains a zinc finger CW (zf-CW) domain that is a histone modification reader for the histone H3 tail with trimethylated K4. The PWWP domain specifically recognizes DNA and histone methylated lysines
LIYTKYTPGSLVWAKMPGYPWWPAMVEDDPDTEEFFWLDEESDIPTKYHVTFFDKPVSRAWVRASSIKPF
TDNSNEPNLTKKKGKKYKKRLNEAVEMAREALKLSIKERLKKFGF
>gnl|CDD|438974 cd20146, PWWP_ZCWPW2, PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins. ZCWPW2 is a histone H3K4me3 reader. In addition to the PWWP domain, ZCWPW2 contains a zinc finger CW (zf-CW) domain that is a histone modification reader for the histone H3 tail with trimethylated K4. The PWWP domain specifically recognizes DNA and histone methylated lysines
GLKYVYSQLPLGSLVWAKMTGYPRWPAILTPDPICGEYVDYDEDGEVEKYHVEFLGKPHSHAWISAKSVE
PYNSNTKTPKCKTKKSKKRKKSYESALEEAERLLKLTCEERLE
>gnl|CDD|438975 cd20147, PWWP_HULK, PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family. The HULK family includes HUA2-like proteins 1-3 (HULK1-3), which are probable transcription factors that act with partial redundancy with each other. They may play diverse and essential roles in the control of plant development, physiology and flowering time. The PWWP domain specifically recognizes DNA and histone methylated lysines
GDLVLAKVKGFPAWPAQVSEPEDWGSAPDPKKVFVHFFGTQQIGFCNPGELSEFTEEIKQSLLARTLKKK
KGSDFSRAVKEICELYEERKGQ
>gnl|CDD|438976 cd20148, PWWP_HDGF, PWWP domain found in Hepatoma-derived growth factor (HDGF). HDGF, also called high mobility group protein 1-like 2 (HMG-1L2), is a heparin-binding protein that acts as a transcriptional repressor with mitogenic activity for fibroblasts. It contains a PWWP domain, which is necessary for DNA binding
YKCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKR
KGFSEGLWEIENNPTVK
>gnl|CDD|438977 cd20149, PWWP_HDGFL2, PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2). HDGFL2, also called HDGF-related protein 2 (HRP-2), or Hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. It contains a PWWP domain, which is necessary for DNA binding
FKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKYKDKYGKPNKR
KGFNEGLWEIQNNP
>gnl|CDD|438978 cd20150, PWWP_HDGFL3, PWWP domain found in Hepatoma-derived growth factor-related protein 3 (HDGFL3). HDGFL3, also called HDGF-related protein 3 (HRP-3), is the only hepatoma-derived growth factor (HDGF)-related protein (HRP) family member whose expression is almost restricted to the nervous tissue. It enhances DNA synthesis and may play a role in cell proliferation. It contains a PWWP domain, which is necessary for DNA binding
PRPREYKAGDLVFAKMKGYPHWPARIDELPEGAVKPPANKYPIFFFGTHETAFLGPKDLFPYKEYKDKFG
KSNKRKGFNEGLWEIENNPGVKF
>gnl|CDD|438979 cd20151, PWWP_PSIP, PWWP domain found in PC4 and SFRS1-interacting protein (PSIP). PSIP, also called CLL-associated antigen KW-7, dense fine speckles 70 kDa protein (DFS 70), lens epithelium-derived growth factor (LEDGF), or transcriptional coactivator p75/p52, acts as a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. It contains a PWWP domain, which is necessary for DNA binding
FKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKR
KGFNEGLWEIDNNPKVKF
>gnl|CDD|438980 cd20152, PWWP_PWWP2A, PWWP domain found in PWWP domain-containing protein 2A (PWWP2A). PWWP2A is a H2A.Z-specific chromatin binding protein which may play an important role in the neural crest stem cell migration and differentiation during early development. It is also required for proper mitosis progression. PWWP2A and its paralog PWWP2B form a stable complex with NuRD subunits MTA1/2/3:HDAC1/2:RBBP4/7, but not with MBD2/3, p66alpha/beta, and CHD3/4. The PWWP domain specifically recognizes DNA and histone methylated lysines
KGKVFSKNVSKCVTPDGRTICVGDIVWAKIYGFPWWPARILAITVSRKDNGLLVRQEARISWFGSPTTSF
LALSQLAPFLENFQSRFNKKRKGLYRKAITEAAKAAKQLTPEVRALLTQFET
>gnl|CDD|438981 cd20153, PWWP_PWWP2B, PWWP domain found in PWWP domain-containing protein 2B (PWWP2B). PWWP2B is a paralog of PWWP2A, a H2A.Z-specific chromatin binding protein which may play an important role in the neural crest stem cell migration and differentiation during early development. PWWP2A and PWWP2B form a stable complex with NuRD subunits MTA1/2/3:HDAC1/2:RBBP4/7, but not with MBD2/3, p66alpha/beta, and CHD3/4. The PWWP domain specifically recognizes DNA and histone methylated lysines
KSVSKCVTEEGRTVSVGDIVWGKIHGFPWWPARVLSISLSQKEDGEPSWQEAKVSWFGSPTTSLLSVSKL
SPFSEFFKLRFNRKKKGMYRKAITEAAKAAEHLTPEIRELLTQFET
>gnl|CDD|438982 cd20154, PWWP_DNMT3A, PWWP domain found in DNA (cytosine-5)-methyltransferase 3A (DNMT3A). DNMT3A, also called DNA methyltransferase HsaIIIA, DNA MTase HsaIIIA, or M.HsaIIIA, is required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. It modifies DNA in a non-processive manner and also methylates non-CpG sites. It may preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. DNMT3A is recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. It contains a PWWP domain that binds methylated histone
EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFSSAF
HQATYNKQPMYRKAIYEVLQVASSRAGKLFPVCPESDESDTSKAVEVQNKQMIEWALGGFQPSG
>gnl|CDD|438983 cd20155, PWWP_DNMT3B, PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B). DNMT3B, also called DNA methyltransferase HsaIIIB, DNA MTase HsaIIIB, or M.HsaIIIB, is required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. It may preferentially methylate nucleosomal DNA within the nucleosome core region. DNMT3B may function as a transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. In tumorigenesis, DNA methylation by DNMT3B is known to play a role in the inactivation of tumor suppressor genes. In addition, a point mutation in the PWWP domain of DNMT3B has been identified in patients with ICF (immunodeficiency, centromeric instability, and facial anomalies) syndrome, a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA
GIGELVWGKIKGFSWWPAMVVSWRATGKRQASSGMRWLQWFGDGKFSEVSADKLVSLTAFSQHFNLSTYN
KLVSYRKAMYHALEVARVRAGKTFPSSPGESLEDQLKPMLDWAHGGF
>gnl|CDD|438984 cd20156, PWWP_BRPF1, PWWP domain found in bromodomain and PHD finger-containing protein 1 (BRPF1). BRPF1, also called peregrin, or protein Br140, is a multi-domain protein that binds histones, mediates monocytic leukemic zinc-finger protein (MOZ)-dependent histone acetylation, and is required for Hox gene expression and segmental identity. It is a close partner of the MOZ histone acetyltransferase (HAT) complex and a novel Trithorax group (TrxG) member with a central role during development. BRPF1 is primarily a nuclear protein that has a broad tissue distribution and is abundant in testes and spermatogonia. It may be involved in chromatin remodeling. It contains a plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, C2HC5HC2H, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PHD finger binds to methylated lysine 4 of histone H3 (K4H3), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties
LDALDLVWAKCRGYPSYPALIIDPKMPREGMFHHGVPIPVPPLEVLKLGEQMTQEAREHLYLVLFFDNKR
TWQWLPRTKLVPLGVNQDLDKEKMLEGRKSNIRKSVQIAYHRAMQHRNKV
>gnl|CDD|438985 cd20157, PWWP_BRPF2, PWWP domain found in bromodomain and PHD finger-containing protein 2 (BRPF2). BRPF2, also called bromodomain-containing protein 1 (BRD1), or BR140-likeprotein, is encoded by BRL (BR140 Like gene). It is responsible for the bulk of the acetylation of H3K14 and forms a novel monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with HBO1 and ING4. The complex is required for full transcriptional activation of the erythroid-specific regulator genes essential for terminal differentiation and survival of erythroblasts in fetal liver. BRPF2 shows widespread expression and localizes to the nucleus within spermatocytes. It contains a cysteine rich region harboring a plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, C2HC5HC2H, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PHD finger binds to lysine 4 of histone H3 (K4H3), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties
LEPLKVVWAKCSGYPSYPALIIDPKMPRVGCHHNGVTIPVPPLDVLKIGEQMQTKSDEKLFLVLFFDNKR
SWQWLPKSKMVPLGIDETIDKLKMMEGRNSSIRKAVRIAFDRAMNHLSRV
>gnl|CDD|438986 cd20158, PWWP_BRPF3, PWWP domain found in bromodomain and PHD finger-containing protein 3 (BRPF3). BRPF3 is a homolog of BRPF1 and BRPF2. It is a scaffold protein that forms a novel monocytic leukemic zinc finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with other regulatory subunits. BRPF3 contains a plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, C2HC5HC2H, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PHD finger binds to lysine 4 of histone H3 (K4H3), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties
LEPLELVWAKCRGYPSYPALIIDPKMPREGLLHNGVPIPVPPLDVLKLGEQKQAEAGEKLFLVLFFDNKR
TWQWLPRDKVLPLGVDDTVDKLKMMEGRKTSIRKSVQVAYDRAMIHLS
>gnl|CDD|438987 cd20159, PWWP_BS69, PWWP domain found in protein BS69 and similar proteins. Protein BS69, also called zinc finger MYND domain-containing protein 11 (ZMYND11 or ZMY11), is a ubiquitously expressed nuclear protein acting as a transcriptional co-repressor in association with various transcription factors. It was originally identified as an adenovirus 5 E1A-binding protein that inhibits E1A transactivation, as well as c-Myb transcription. It also mediates repression, at least in part, through interaction with the co-repressor N-CoR. Moreover, it interacts with Toll-interleukin 1 receptor domain (TIR)-containing adaptor molecule-1 (TICAM-1, also named TRIF) to facilitate NF-kappaB activation and type I IFN induction. It associates with PIAS1, a SUMO E3 enzyme, and Ubc9, a SUMO E2 enzyme, and plays an inhibitory role in muscle and neuronal differentiation. Moreover, BS69 regulates Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1)/C-terminal activation region 2 (CTAR2)-mediated NF-kappaB activation by interfering with the complex formation between TNFR-associated death domain protein (TRADD) and LMP1/CTAR2. It also cooperates with tumor necrosis factor receptor (TNFR)-associated factor 3 (TRAF3) in the regulation of EBV-derived LMP1/CTAR1-induced NF-kappaB activation. Furthermore, BS69 is involved in the p53-p21Cip1-mediated senescence pathway. BS69 contains a plant homeodomain (PHD) finger, a bromodomain, a proline-tryptophan-tryptophan-proline (PWWP) domain, and a MYeloid translocation protein 8, Nervy and DEAF-1 (MYND) domain. The PWWP domain specifically recognizes DNA and histone methylated lysines
KPCRPPHELVWAKQKGFPYWPAKVIQKEDNQYDVRFFGGHHQRAWIPKENIKPITTSPKQLKVKRTAGWN
KACEELKKHQELLEE
>gnl|CDD|438988 cd20160, PWWP_PRKCBP1, PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins. PRKCBP1, also called cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor. They form a RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a plant homeodomain (PHD) finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PWWP domain specifically recognizes DNA and histone methylated lysines
EPCRKPHLLVWAKLKGFPFWPAKALRVNNGQVDVRFFGAHDRAWVPVKDCYLYSKEPPTSVKKKKSGLDE
AMEELEIHIEKLREKFGKFNY
>gnl|CDD|438989 cd20161, PWWP_NSD1_rpt1, first PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins. NSD1, also called H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, androgen receptor coactivator 267 kDa protein, androgen receptor-associated protein of 267 kDa, H3-K36-HMTase H4-K20-HMTase, Lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein, is a lysine methyltransferase that preferentially methylates H3 on Lysine36 (H3-K36) and H4 on Lysine20 (H4-K20), which is primarily associated with active transcription. It plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. It can alter transcription by interacting with the protein NSD1-interacting zinc finger protein 1 (NIZP1). It also mitigates caspase-1 activation by listeriolysin o (LLO) in macrophages, and requires functional LLO for the regulation of IL-1beta secretion. Moreover, NSD1 regulates RNA polymerase II (RNAP II) recruitment to bone morphogenetic protein 4 (BMP4). NSD1 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD domains are involved in protein-protein interactions. The model corresponds to the first PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines
PVKYEVGDLVWAKFSRRPWWPCRICADPLLDTHSKMKVPSRRPCRQYYVETLGELTEKAWVAAKAVVPFE
GRHQFEELPVLRRRGKQKEKDYKHKIPQKLLSLWEASVAHAEDFLS
>gnl|CDD|438990 cd20162, PWWP_NSD2_rpt1, first PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins. NSD2, also called histone-lysine N-methyltransferase NSD2, multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, through mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). NSD2 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, a high mobility group (HMG) box, five PHD (plant-homeodomain) zinc finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD domains mediate chromatin interaction and recognition of histone marks. This model corresponds to the first PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines
YNVGDLVWSKVSGYPWWPCMVSADPLLHSHTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVPFEGEGQ
FEQLCQESAKQAPTKAEKIKLLKPISGKLRAQWDMGIVQAEEAASMTVEERKAKFTFL
>gnl|CDD|438991 cd20163, PWWP_NSD3_rpt1, first PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins. NSD3, also called histone-lysine N-methyltransferase NSD3, protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant-homeodomain (PHD) zinc finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD domains are involved in protein-protein interactions. This model corresponds to the first PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines
FQVGDLVWSKVGTYPWWPCMVSSDPQLEVHTKINTRGAREYHVQFFSSQPERAWVHEKRVREYKGHKQYE
ELLAEATKQASNHSEKQKIRKPRPQRERAQWDIGIAHAEKALKMTREERIEQYTFIYIDK
>gnl|CDD|438992 cd20164, PWWP_NSD1_rpt2, second PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins. NSD1, also called H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, androgen receptor coactivator 267 kDa protein, androgen receptor-associated protein of 267 kDa, H3-K36-HMTase H4-K20-HMTase, Lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein, is a lysine methyltransferase that preferentially methylates H3 on Lysine36 (H3-K36) and H4 on Lysine20 (H4-K20), which is primarily associated with active transcription. It plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. It can alter transcription by interacting with the protein NSD1-interacting zinc finger protein 1 (NIZP1). It also mitigates caspase-1 activation by listeriolysin o (LLO) in macrophages, and requires functional LLO for the regulation of IL-1beta secretion. Moreover, NSD1 regulates RNA polymerase II (RNAP II) recruitment to bone morphogenetic protein 4 (BMP4). NSD1 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD domains are involved in protein-protein interactions. This model corresponds to the second PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines
HYKEVVWVKVGRYRWWPAEVCHPKSIPTNIQKMKHDIGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKD
KMGKGVDGTYKKALQEAAVRFEELKA
>gnl|CDD|438993 cd20165, PWWP_NSD2_rpt2, second PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins. NSD2, also called histone-lysine N-methyltransferase NSD2, multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, through mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). NSD2 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, an high mobility group (HMG) box, five PHD (plant-homeodomain) zinc finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD domains mediate chromatin interaction and recognition of histone marks. This model corresponds to the second PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines
RFQDIIWVKLGNYRWWPAEVCHPKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEGDRGSKY
QGGKGIGKVFKNALQEAEARFREIKL
>gnl|CDD|438994 cd20166, PWWP_NSD3_rpt2, second PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins. NSD3, also called histone-lysine N-methyltransferase NSD3, protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant-homeodomain (PHD) zinc finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD domains are involved in protein-protein interactions. This model corresponds to the second PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines
HYKQIVWVKLGNYRWWPAEICNPRSVPLNIQGLKHDIGDFPVFFFGSHDYYWVHQGRVFPYVEGDKSFAE
GQTSINKTFKKALEEAAKRFQELKA
>gnl|CDD|380911 cd20167, Peptidase_M90-like, M90 peptidase is a zinc-metallopeptidase. The M90 peptidase family includes the MtfA (Mlc Titration Factor A) peptidase from Escherichia coli, also known as the YeeI gene product, which is involved in the control of the glucose-phosphotransferase sensory and regulatory system by inactivation of the repressor Mlc (making large colonies). E. coli MtfA has been shown to have aminopeptidase activity with the presence of a single zinc ion in the active site ligated by two histidines in a HEXXH motif. This family also includes uncharacterized proteins similar to MtfA peptidase
EQHKLTQXAARFLQQKRLVALQGLELTPLHQARIAXLFCLPVLELGIEWLDGFHEVLIYPAPFIVDDEWE
DDIGLVHNQRVVQSGQSWQQGPVVLNWLDIQDSFDASGFNLVVHEVAHKLDTRNGDRASGVPLIPLREVA
GWEHDLHAAXNNIQDEIDLVGESAASIDAYAATDPAECFAVLSEYFFSAPELFAPRFPALWQRFCHFY
>gnl|CDD|380912 cd20169, Peptidase_M90_mtfA, Mlc titration factor A (MtfA) is a zinc metallopeptidase (M90 peptidase). This subfamily includes the Mlc Titration Factor A (MtfA; also known as YeeI or DgsA anti-repressor MtfA) which is involved in the control of the glucose-phosphotransferase sensory and regulatory system by inactivation of the repressor Mlc (making large colonies). It can cleave synthetic substrates of both carboxypeptidases and aminopeptidases, with strongest activity towards the latter. Its biologically relevant substrate has yet to be identified. Although it interacts with the transcription repressor Mlc, it does not cleave it. However, Mlc seems to activate the peptidase activity of MtfA. MtfA is related to the catalytic domain of the anthrax lethal factor which is a zinc-dependent metalloprotease, targeting mitogen-activated protein kinase kinases (MAPKKs), and resulting in apoptosis, as well as the Mop (modulation of pathogenesis) protein involved in the virulence of Vibrio cholerae; although sequence similarity is low, conservation is observed in the overall structure as well as in the residues around the active site
ERARLERLAQLFLAEKRFEGAGGLELTDEMRLLIAAQACLLVLGLGLDWYDGLREILVYPDAFVARREEE
DEAGVVHEGRGVLGGEAWEQGPVVLSWPDVEAGFRNPGDGHNVVIHEFAHKLDMLDGDADGVPPLLSGMD
ARRWARVFQAAYERLRRGVSRGRETLIDPYAATNPAEFFAVASEYFFERPALLRREHPELYALLARFY
>gnl|CDD|380913 cd20170, Peptidase_M90-like, uncharacterized M90 peptidase family-like proteins. This subfamily contains uncharacterized M90 peptidase-like domains, similar to the Mlc Titration Factor A (MtfA) peptidase from Escherichia coli, also known as the YeeI gene product, which is involved in the control of the glucose-phosphotransferase sensory and regulatory system by inactivation of the repressor Mlc (making large colonies). E. coli MtfA has been shown to have aminopeptidase activity with the presence of a single zinc ion in the active site ligated by two histidines in an HEXXH motif. MtfA is related to the catalytic domain of the anthrax lethal factor and the Mop protein involved in the virulence of Vibrio cholerae; although sequence similarity is low, conservation is observed in the overall structure as well as in the residues around the active site
ILEKYFPYYNKLSPKQKKRFEHRVARFINSKKFIGREGLEVTEEMKVLIAATAVQLTFGLRNYLLSHFDT
ILIYPDAYYSTINKQYHKGEVNPRLKAIVLSWKDFLEGYAIPNDGLNLGLHEMAHALHLENLISNDESAF
FFRKGFKKFKKLAKDEFEKIKLGESSYFRDYAFTNIHEFFAVAVENFFETPEEFKAEFPELYEALKKLLN
>gnl|CDD|380332 cd20171, M34_peptidase, Peptidase family M34 includes the C-terminal catalytic domain of anthrax lethal factor (ATLF), the protective antigen-binding domains of ATLF and edema factor, and Pro-Pro endopeptidase. Peptidase family M34 (also known as the anthrax lethal factor family) includes the C-terminal catalytic domain of anthrax lethal factor (ATLF, EC 3.4.24.83), and the N-terminal protective antigen-binding domains (PABDs) of ATLF and edema factor (EF). ATLF and EF are enzyme components of anthrax toxin and are carried into the cell by a third component, the protective antigen (PA). ATLF is a highly selective protease whose major substrates are mitogen-activated protein kinase kinases (MKKs). At its N-terminus, ATLF has a PABD domain which lacks the hallmark metalloprotease motif HEXXH, and, at its C-terminus, the related catalytic domain has the HEXXH motif where the two His residues bind a single zinc atom, and the Glu has a catalytic role. EF acts as a Ca2+- and calmodulin-dependent adenylyl cyclase that can cause edema when associated with PA. EF is comprised of the PABD and an adenylyl cyclase domain. This family also includes Pro-Pro endopeptidase (PPEP-1; EC 3.4.24.89, also known as Zmp1) which is an extracellular metalloprotease that shows a unique specificity for hydrolyzing a Pro-Pro bond and is involved in bacterial adhesion
DVLNALKAIGGKIYITDGDITNHIELEALSEDKIKDIYGKDALLHEHYGYAKEGYPVIVVRSSEDYVENT
NKALNVYHEIGHAVDRDALSKINQPYQKFIDIFNKEKSASTSDGLGYNSNNPQEYFAEAFALYIEPDHRS
VLQLYAPLTFNYMDKF
>gnl|CDD|380910 cd20174, GH18_LinChi78-like_UFR, an unknown function domain of Listeria innocua LinChi78 GH18 chitinase that is essential for its catalytic activity; found in similar chitinase-like proteins. This domain is referred to as an unknown-function region (UFR) and shown to be necessary for the hydrolytic activity of LinChi78 glycosyl hydrolase family 18 (GH18) chitinase (a product of the lin0153gene) from the nonpathogenic bacterium Listeria innocua. The catalytic domain (CatD) of GH18 chitinases folds into a TIM barrel and has a conserved DXXDXDXE motif, in which the Glu residue functions as a catalytic residue; these chitinases contain additional domains such as a chitin-binding domain (ChBD) and/or a fibronectin type III-like (FnIII) domain. LinChi78 consists of a CatD, a FnIII, and a ChBD domain, and has this UFR region located between the CatD and the FnIII domain. Its catalytic site is composed of a typical CatD and a portion of this UFR, in particular the key Gln and Ile residues which are indispensable for LinChi78 to exhibit full catalytic activity. This UFR domain is also found in proteins where it is located between a CatD domain and DUF5011 and ChBD(s) domains. LinChi78 exhibits chitinase activity towards artificial and natural substrates, including colloidal chitin and chitin oligosaccharides of various lengths, and hydrolyzes these in a processive manner. Members of this family include some uncharacterized chitinase-like proteins from pathogenic bacteria such as Listeria monocytogenes and Clostridium botulinum
LNVSATVTPYTESGGEGYEITITNNEKLEESGEVLSAVEKAAKTIKNPKLYIKTKDGETLTSGDYKAGTV
TTENGYTVVDLSTVYDGKFIKPGASYTFKLKTDAGAADLSNIESIELSQRIVSSGPELGRQTIYGD
>gnl|CDD|412038 cd20175, ThyX, FAD-dependent thymidylate synthase (ThyX), mechanistically and structurally unrelated to thymidylate synthase (ThyA). This family contains FAD-dependent thymidylate synthase (also known as ThyX, Thy1, FDTS or thymidylate synthase complementing protein), found in many microbial genomes including several human pathogens, but absent in humans. This protein is mechanistically and structurally unrelated to thymidylate synthase (TS or ThyA) found in mammals. ThyA and ThyX both produce de novo thymidylate or deoxythymidine 5'-monophosphate (dTMP), an essential DNA precursor. The classic ThyA catalyzes the reductive methylation of deoxyuridine 5'-monophosphate (dUMP) to form dTMP, with methylenetetrahydrofolate (CH2H4folate) serving as a one-carbon donor and as the source of reductive power. On the other hand, ThyX contains FAD, tightly bound by a novel fold, that mediates hydride transfer from NADPH during catalysis. Consequently, CH2H4folate serves only as a carbon donor and tetrahydrofolate (and not dihydrofolate as in the case of ThyA) is produced. The differences between the ThyX and ThyA is used for mechanism-based drugs to selectively inhibit FDTS and not have much effect on human and other eukaryotic TS. ThyX has been pursued for the development of new antibacterial agents against Mycobacterium tuberculosis, the causative agent of the widespread infectious disease tuberculosis (TB). It is also an attractive target for designing specific antibiotic drugs against many diseases such as ulcers, periodontal disease, and Lyme's disease, as well as biological warfare agents such as anthrax, botulism, and typhus
ELIDYTPDPEEKPEELIAAAARVSYSSEGEEKAEEEDEKLIKRLLKRDGHGSVLEHASFTFEIEGVSAAT
HQLVRHRIASFTQESQRYVDLSGFKYPPPPPEIEDEELEELYEEAMEEAEELYEKLLEAGIAKEDARYVL
PNATKTRIVVTMNLRELLHFLELRTCPHAQWEIRELAEEMLEELKK
>gnl|CDD|439130 cd20177, Dpy19, C-mannosyltransferase Dpy19. Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant
KILLGLLLALLVGVLYSLHLSTLFENDRHFSHLSELEREMTFRTEMGLYYSYYKQLIEAPSFLEGLYKLT
HDNVTEYPHTINTLKRFNLYPEVILAILYRVFPSIANYFGIPTKQCWQVRGEDLPPVESCEGLGEPAYFY
IYVVFGLNGLVAGLLFLYGWLLSGSILGGLLTVAFFFFNHGEATRVQWTPPLRESFAYPFLLLQILLITI
YLRSNIGKRFHLLAISISTFLFMLMWQFSQFALLTQILSLFALYVLGYIPSSKVQTIILSHLISLLLAFV
LLFGNEMLLTSLYLSSLLAFLIILYLQLRLKKSFKFKLIIWLLQLILVFLGTLGLKLLLSKLLNVEDDAH
IFKILKSKFGDYRDFDTRLYTCAAEFDFLSLETFLRLSKTLLLPLYIVVLVVIAFLFLRVRLLTLNDSTL
KESVNFTDSRLILNPEIVYNVLQLLAFGLLAILIMRLKLFWTPHMCILASLLLSKKLLWKLLLKKIFRLA
VLFALLASMSYPGIPNLQEELSILGEFSNPDTEELMEWIKDNTPPDAVFAGSMPLMANVKLSTGRPIVNH
PHYEDAGLRERTKQVYSMYSRRPAEEVYNILKKLGVNYIILEDSICLSRRRDGCSLPDIWDLEDPHNRGK
PPLCIRLLLEDYVPYFKLVFSNKTYRV
>gnl|CDD|439131 cd20178, Dpy19L1, C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1). Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. Dpy19L1 (also called protein Dpy-19 homolog 1) regulates neurite extension during development
KIWVTLLLAALAGVLHWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIIEAPSFLNGVWMIM
NDRLTEYPLVINTLKRFNLYPEVVLASWYRIYTGIMDFFGIQTKTCWTVNRGEGLSPVESCEGLGDPAYF
YVAVIFLLNGLMMSLFFIYGTYLSGSRLGGVVTVLCFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVT
YILRAPNLGRGSLIALCISNVLFMLPWQFAQFVLLTQIASLFAVYVVGYIDSCKLQKILYAHMISLVVCF
VLMFGNSMLLTSYYASSLVIIWGILALRPKFLKVNKSEVSLWVIQGCAWLFGTVILKYLTSKVFGIADDA
HIGNLLKSKFTSYKDFDTLMYTCAAEFDFMEKETPLRYTKTLLLPVVLVVFAAIARKTIKDLWGVLAKKA
THTRKEQFAHGELVYHALQLLAYAVLAILIMRLKLFLTPHMCVMASLVCSRQLFGWLFCKVHPQAVVFAI
LAAMAIQGSANLQTQWNIIGEFSNLPQEELLEWIKYNTKPDAVFAGAMPTMASVKLSALRPIVNHPHYED
AGLRARTKIVYSMYSRKPAEEVKRELMKLGVNYYILEESWCVRRSKPGCSMPEIWDVEDPDNAGKTPLCT
LMSKDSRPHFTTVFENSVYKVL
>gnl|CDD|439132 cd20179, Dpy19L2, C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2). Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. Dpy19L2 (also called protein Dpy-19 homolog 2) deletion is a major cause of globozoospermia
RFSSRTTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWM
IMNDRLTEYPLIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGDPA
CFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCI
LTLILRTSSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTL
SFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSD
HIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDISYVLAT
NIYLRKQLLEHSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKVIFG
ILTVMSIQGYANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYE
DADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLC
SVLLEDARPYFTTVFQNSVYRV
>gnl|CDD|439133 cd20180, Dpy19L4, C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4). Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. The function of Dpy19L4 (also called protein Dpy-19 homolog 4) is unknown
KIFFGCLAAVTSGMMYAVYLSTYHERKFWFSNRQELEREITFQGDSAIYYSYYKDMLKAPSFERGVYELT
HNNKTVSLKTINAVQQMSLYPELIASVLYQATGSNEVIEPVYFYIGIVFGLQGIYVTALFVTSWLMSGTW
LAGMLTVAWFIINRVDTTRIEYSIPLRENWALPYFACQVAALTGYLKSNLNTYAERFCYLLMSASTYTFM
MMWEYSHYVLFLQAISLFLLDSFSLEQSDKVYEVYKVYLFSLFLGYLLQFENPALLVSPLLSLVAALMLA
KCLQLNMKKGPFVAKMIKVLHFYLVCTLTITLNFIMKMFVPHKENEHLLKFLEVKFGLNTTKNFTMNWLL
CQESLQAPSQDFFLRLTQSSLLPFYILVLIICLLSMLQVIFRRLSGKPLKETVTLEDGRIGERPEIVYHV
IHTILLGSLAMLFEGMKYLWTPYVCMLAAFGVCSPELWMTLFKWLRLRTVHPILLALILSMAVPTIIGFS
LWKEFFPRLMTELSELQEFYDPDTVELMTWIKRQAPVAAVFAGSPQLMGTIKLCTGWMVTSLPLYNDDDL
LKRNENIYQIYSKRSAEDIYKILTSYKANYLIIEDAICNEVGPVRGCRVKDLLDIANGHVVCEEGDKYTY
SKYGRFCHEIKINYSPYVNYFTRVYWNRSYFVYK
>gnl|CDD|439134 cd20181, Dpy19L3, C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3). Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. In humans Dpy19L3 (also called protein Dpy-19 homolog 3) is a C-mannosyltransferase of R-spondin
STTVGGTVALCIGLLTSVYVATLHENDLWFSNIKEVEREISFRTECGLYYSYYKQMLQAPSIQQGFHGLI
YDNKTESMRTINLLQRMNIYQEVFLSVLYRVLPIQKYLEPVYFYIYTLFGLQAVYVIALYITSWLLSGTW
LSGLLAAVWYITNRIDTTRVEFTIPLRENWALPFFAIQIAAITYFLRPNLQPLQERLTLLAIFISTFLFS
LTWQFNQFMMLIQALVLFTLDCLDMLPTAKVTWLYGIQISGLLLVCILQFFNSMILGSLLLSFNLSVLIV
RKLQKNLKTGSFLNRLGKLLLHLALVLCLTLFLNNIIKKILNLKSDEHIFKFLKAKFGFGATRDFDANLY
LCEEAFGLLPFNTFERLSDTLLFYAYIFVLLLTVIVAAVVAFHNLSDSTNQQSMGKMEKGTVDLKPEVAY
NLIHTILFGFLALSTMRMKYLWTSHMCVFASFGLCSTELWELLLKSVHLYNPKRIRVMRYSVPILTLLYL
CYKFWPGLMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTNHPHYEDKSLR
ERTRQVYQIYAKRSPEEVHALLRSFGTDYVILEDSICYERRHRRGCRLRDLLDIANGHIMDGPGENDPDL
KPADHPRFCEEIKRNLPSYAAYFTRVFQNKTFHVYKL
>gnl|CDD|380333 cd20183, M34_PPEP, Pro-Pro endopeptidase (PPEP) and similar proteins; belongs to peptidase family M34. This subfamily includes the enzyme Pro-Pro endopeptidase (PPEP-1, EC 3.4.24.89, also known as Zmp1 (Clostridium difficile-type)), an extracellular metalloprotease showing a unique specificity for hydrolyzing a Pro-Pro bond. It belongs to peptidase family M34 and has the hallmark metalloprotease motif HEXXH, where the two His residues bind a single zinc atom, and the Glu has a catalytic role. PPEP-1 cleaves two C. difficile cell surface proteins (CD2831 and CD3246) involved in adhesion, one of which is encoded by the gene adjacent to the ppep-1 gene. There are multiple PPEP-1 cleavage sites located just above the site of attachment to the peptidoglycan layer. PPEP-1 may play a role in switching from an adhesive to a motile phenotype. Also included in this subfamily is Paenibacillus alvei PPEP-2, a secreted Pro-Pro endopeptidase. The cleavage motif of PPEP-2, PLP PVP, is distinct from that of PPEP-1 (VNP PVP). PPEP-2 cleavage sites in a cell-surface protein, with putative extracellular matrix-binding domains, and encoded by the adjacent gene, suggests a similar role of PPEP-2 in controlling bacterial adhesion
LLEQIIILPEGSYDEEEAAKMINRLSKIPPSILEKLKENGIKIKLFNGKLTDEPEAAHLKGVVPRGWEGT
GKTWDDVPGIGGSKTVLVKIGYSEKGKGHGSVNLELHELAHSIDRYVFNNISSSEEFLQIWKEEAPKLFP
GNSYFLNYPEEYFAETFAMYYYSEETREKLKEKAPLTYEFIKKL
>gnl|CDD|380334 cd20184, M34_peptidase_like, uncharacterized subfamily of peptidase family M34. Peptidase family M34 (also known as the anthrax lethal factor family) includes the C-terminal catalytic domain of anthrax lethal factor (ATLF, EC 3.4.24.83), and the N-terminal protective antigen-binding domains (PABDs) of ATLF and edema factor (EF). ATLF and EF are enzyme components of anthrax toxin and are carried into the cell by a third component, the protective antigen (PA). ATLF is a highly selective protease whose major substrates are mitogen-activated protein kinase kinases (MKKs). At its N-terminus, ATLF has a PABD domain which lacks the hallmark metalloprotease motif HEXXH, and, at its C-terminus, the related catalytic domain has the HEXXH motif where the two His residues bind a single zinc atom, and the Glu has a catalytic role. EF acts as a Ca2+- and calmodulin-dependent adenylyl cyclase that can cause edema when associated with PA; it is comprised of the PABD and an adenylyl cyclase domain. Pro-Pro endopeptidase (PPEP-1; EC 3.4.24.89, also known as Zmp1) is an extracellular metalloprotease that shows a unique specificity for hydrolyzing a Pro-Pro bond and is involved in bacterial adhesion. This uncharacterized subfamily includes proteins which have an N-terminal SLH domain, and proteins which may have an N-terminal IG-like domain; these proteins have the hallmark metalloprotease motif HEXXH motif
IPEKILNAFESNGWKIVIDPKYIAETSEGSGGSYAGLTSYSEKKIYLSAEIASALLHEFGHFLDYILGNP
SQSSEFKAIYNAEKSKFKGFNKNYATTNAREYFAESFREYILNPSRLKKNAPKTYAYIEKL
>gnl|CDD|380335 cd20185, M34_PABD, N-terminal protective antigen-binding domain (PABD) of Anthrax Toxin Lethal Factor (ATLF) and Edema Factor (EF), and similar domains; belongs to peptidase family M34. This subfamily includes the functional N-terminal protective antigen-binding domain (PABD) of the anthrax edema factor (EF), as well as the likely inactive N-terminal PABD of anthrax toxin lethal factor (ATLF), both secreted by Bacillus anthracis. ATLF and EF are enzyme components of anthrax toxin and are carried into the cell by a third component, the protective antigen (PA). ATLF-PABD resembles the C-terminal catalytic domain of ATLF (EC 3.4.24.83) but lacks the hallmark metalloprotease motif HEXXH. This subfamily belongs to the peptidase family M34 (also known as the anthrax lethal factor family), which also includes the C-terminal catalytic domain of ATLF, and Pro-Pro endopeptidase (PPEP-1; EC 3.4.24.89, also known as Zmp1), which is an extracellular metalloprotease that shows a unique specificity for hydrolyzing a Pro-Pro bond and is involved in bacterial adhesion
EENKTQEERMKEIIKHIVKIEVKNEEVAKKEATEKLLKKLPSEVLEMYKEVGGKIYIVDGDLTEHPELKD
LSEKQIKDSEGNEVSLAEHYVYAKEGEEPVLVIQASEDYEENIEKSKNVYYEIGKSLVRDVLKKETQPNP
AFLDALNQIKADEDSSDLLFSQALKEHTGSFDEEFVKEHLEEFQEVFAKAFAYYFEPHYRDVLKLYAPEM
FNYMDKLNW
>gnl|CDD|410313 cd20187, T-box_TBX1_10-like, DNA-binding domain of T-box transcription factor 1 and 10, and related T-box proteifactors. This subfamily includes TBX1 and TBX10. TBX1 is a T-box transcription factor which plays an important role in heart development and has been implicated in DiGeorge or 22q11.2 deletion syndrome. This syndrome is associated with various types of cardiac outflow tract (OFT) and vascular defects. Wnt5a is regulated by TBX1 in the second heart field (SHF). TBX1 is required to maintain the integrity of extracellular matrix-cell interactions in the SHF and this interaction is critical for cardiac (OFT) development. TBX10 is a putative T-box transcription factor. Diseases associated with TBX10 include Isolated Cleft Lip and Cleft Lip/cleft lip with or without cleft palate. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
NVTVQLEMKALWDEFNQLGTEMIVTKAGRRMFPTFQVKIFGMDPMADYMLMMDFVPVDDKRYRYAFHSSS
WLVAGKADPAMPGRIHVHPDSPAKGAQWMKQIVSFDKLKLTNNLLDDNGHIILNSMHRYQPRFHVVYVDP
RKDSENSAEENFKTFIFPETKFTAVTAYQNHRITQLKIASNPFAKGFRD
>gnl|CDD|410314 cd20188, T-box_TBX2_3-like, DNA-binding domain of T-box transcription factor 2 and 3, and related T-box proteins. This subfamily includes the T-box transcription factors TBX2 and TBX3 and similar proteins. TBX2 is an oncogenic transcription factor implicated in developmental processes, including coordinating cell fate, patterning and morphogenesis of a wide range of tissues and organs. It is overexpressed in several cancers, including melanoma and breast, and plays a key role during cardiac development. TBX2 is a negative regulator of promyelocytic leukemia protein (PML) function in cellular senescence, and it interacts with HP1 to recruit a repression complex to EGR1-responsive promoters to drive the proliferation of breast cancer cells. TBX3 has also been implicated in oncogenesis in breast cancer and melanoma. The tbx3 gene is downregulated by PML. TBX3 directly represses TBX2 under the control of the PRC2 complex in skeletal muscle and rhabdomyosarcoma. Also included in this family is the Drosophila melanogaster optomotor-blind protein (Omb, also known as lethal(1)optomotor-blind, or L(1)omb, or protein bifid) which controls many developmental processes such as wing, eye, and abdominal tergites and optic lobes, and induces epithelial cell migration and extrusion in vivo. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
DDPKVELEAKDLWDQFHKLGTEMVITKSGRRMFPPFKVRVSGLDKKAKYILLMDIVAADDCRYKFHNSRW
MVAGKADPEMPKRMYIHPDSPSTGEQWMQKVVSFHKLKLTNNISDKHGFTILNSMHKYQPRFHIVRANDI
LKLPYSTFRTYVFKETEFIAVTAYQNEKITQLKIDNNPFAKGFRD
>gnl|CDD|410315 cd20189, T-box_TBX4_5-like, DNA-binding domain of T-box transcription factor 4 and 5, and related T-box proteins. This subfamily includes the T-box transcription factors TBX4 and TBX5 which play important roles in vertebrate limb and heart development, and in lung and trachea development. TBX4 is needed for normal skeletal and muscular hindlimb development and is involved in super-enhancer-driven transcriptional programs underlying features specific to lung fibroblasts. TBX5 plays a role in regulating cardiac conduction system function, and in coordinating forelimb muscle pattern. Mutations in human TBX5 and TBX4 are associated with Holt-Oram syndrome and Small Patella syndrome, respectively. Both syndromes are characterized by limb defects in addition to other abnormalities. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
IKVFLENRELWQKFHEVGTEMIITKAGRRMFPSIKVKVTGLNPKTKYILLMDIVPADDHRYKFHDSEWVV
AGKAEPAMPGRLYVHPDSPATGAHWMRQLVSFQKLKLTNNHLDQFGHIILNSMHKYQPRIHIVQADDNNA
FGSKNTAFSTHVFPETAFIAVTAYQNHQITQLKIENNPFAKGFRG
>gnl|CDD|410316 cd20190, T-box_TBX6_VegT-like, DNA-binding domain of T-box transcription factor 6, VegT and related T-box proteins. This subfamily includes the transcriptional regulators TBX6 and VegT. TBX6 plays an essential role in the fate determination of axial stem to become either neural or mesodermal. It also plays an essential role in the regulation of left/right patterning in mouse embryos through effects on nodal cilia and perinodal signaling. VegT (also known as Antipodean, Brat and Xombi) is required in early Xenopus embryos for the formation of both the mesoderm and endoderm germ layers. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved 1DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
VSLSLEDRELWKEFSSVGTEMIITKSGRRMFPACKVSVTGLDPEAKYLFLLDVVPVDNARYKWNKRRWEP
SGKAEPHLPDRVYIHPDSPAPGAHWMRQPISFHKLKLTNNTLDPHGHLILHSMHKYQPRIHLVQSADLCS
QHWGGMASFRFPETTFIAVTAYQNPQITKLKIAANPFAKGFRE
>gnl|CDD|410317 cd20191, T-box_TBX15_18_22-like, DNA-binding domain of T-box transcription factor 15, 18 and 22, and related T-box proteins. This subfamily includes the transcriptional regulators TBX15, TBX18 and TBX22 which are involved in various developmental processes. TBX15 (also known as TBX14) plays an important role in the development of the skeleton of the limb, vertebral column and head, possibly through its control of the number of mesenchymal precursor cells and chondrocytes; it also plays a role in the differentiation of brown and brite adipocytes. TBX18 is involved in the developmental processes of a variety of tissues and organs, including the ureter, vertebral column. epicardium and coronary vessels; it is important for the development of the head portion of the sino atrial node (SAN). Mutations in the T-box transcription factor gene TBX22 are found in X-linked Cleft Palate with or without Ankyloglossia syndrome (CPX syndrome), and associated with cleft lip and palate, and tooth agenesis. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
KEIQVELQGSELWKRFHDIGTEMIITKAGRRMFPAIRVKVSGLDPHAQYIVAMDIVPVDNKRYRYVYHSS
KWMVAGNADAPVPPRVYIHPDSPASGETWMRQVVSFDKLKLTNNEMDDQGHIILHSMHKYQPRVHVIRKD
SSTDLSPKKPVPPGEGVKTFSFPETVFTTVTAYQNQQITRLKIDRNPFAKGFRD
>gnl|CDD|410318 cd20192, T-box_TBXT_TBX19-like, DNA-binding domain of T-box transcription factor T, T-box transcription factor 19 and related T-box proteins. Tbx19 (also known as Tpit) is a T-box factor restricted to two pituitary (pro-opiomelanocortin) POMC-expressing lineages, the corticotrophs and melanotrophs; it controls terminal differentiation of these lineages. TBX19 activates POMC gene transcription with the cooperation of another transcription factor Pitx1. TBXT, also known as Brachyury protein, or protein T, is a transcription factor needed for posterior mesoderm formation and differentiation as well as for the notochord development during embryogenesis. It binds to a 24 base-pair (bp) palindromic site (called the T site) and activates gene transcription when bound to such a site. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. TBXT is the founding member of the T-box family, members of which share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
IRVTLEDRELWKKFHSLTNEMIVTKSGRRMFPVLKVSVSGLDPNAMYSVLLDFVQVDNHRWKYVNGEWVP
GGKAEPPPPSSVYVHPDSPNFGAHWMKGPVSFSKVKLTNKPNGEGQIMLNSLHKYEPRVHIVRVGSNNHE
RLVSTFSFPETQFIAVTAYQNEEITALKIKYNPFAKAFLD
>gnl|CDD|410319 cd20193, T-box_TBX20-like, DNA-binding domain of T-box transcription factor 20 and related T-box proteins. TBX20 is a T-box transcriptional factor which functions in embryonic development and its deficiency is associated with congenital heart disease. It acts both as a transcriptional activator and a repressor required for cardiac development, and has key roles in maintaining the functional and structural phenotypes in the adult heart. The TBX20-cardiac transcription factor CASZ1 protein complex is protective against dilated cardiomyopathy and is essential for maintaining cardiac homeostasis. TBX20 has also been shown to regulate angiogenesis through the PROK2-PROKR1 (prokineticin receptor 1) pathway and is involved in both, pathological and developmental, angiogenesis. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
VQCHLETKELWDKFHELGTEMIITKSGRRMFPTVRVSFSGVDPDAKYIVLMDIVPVDNKRYRYAYHRSSW
LVAGKADPPLPARLYVHPDSPFTGEQLLKQMVSFEKVKLTNNELDKHGHIILNSMHKYQPRVHIVKKKDH
TASLVNLKSEEFRTFIFPETVFTAVTAYQNQLITKLKIDSNPFAKGFRDS
>gnl|CDD|410320 cd20194, T-box_TBR1_2_21-like, DNA-binding domain of T-box brain protein 1 and 2, T-box transcription factor 21 and related T-box proteins. TBX21 (also known as T-cell-specific T-box transcription factor T-bet or transcription factor TBLYM) is a lineage-defining transcription factor which directs T helper type 1 (Th1) cell differentiation. This subfamily includes TBR1 (also known as T-brain-1, or TES-56), which is a neuron-specific transcription factor involved in forebrain development, and TBR2 (also known as Eomesodermin, Eomes, or T-brain-2), which is associated with neurogenesis, cardiogenesis and tumor immune response. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
KASVYLCNRDLWLKFHQHQTEMIITKQGRRMFPTLSFNLSGLDPTAHYNVFVDMVLADPNHWKFQSGKWV
PCGKAEGLPQGNRVYVHPDSPNTGAHWMKQEISFSKLKLTNNKGADQGMIVLNSMHKYQPRIHVIEVGGN
GPNEQRNLQTHSFPETQFIAVTAYQNTDITQLKIDHNPFAKGFRD
>gnl|CDD|410321 cd20195, T-box_MGA-like, DNA-binding domain of MAX gene-associated protein and related T-box proteins. MGA (also known as MGAP, MAX dimerization protein, MAD5, MXD5) is a dual-specificity transcription factor that regulates the expression of both, MAX-network and T-box family target genes. MGA functions as a repressor or an activator; it binds to 5'-AATTTCACACCTAGGTGTGAAATT-3' core sequence. Its function is activated by heterodimerization with MAX. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
ITVTLENNSMWNEFYRCGTEMILTKQGRRMFPYCRFRISGLDPDRNYILVMDISPVDNFRYRWNGRWWEP
SGKAEPHVLGRVFIHPESPATGRHWMDQPVSFYKLKLTNNTLDQEGHIILHSMHRYLPRLHVVPADKEVD
VIQLNGPDVHTFTFPQTEFFAVTAYQNKQITQLKIDYNPFAKGFRE
>gnl|CDD|410322 cd20196, T-box_TBX6, DNA-binding domain of T-box transcription factor 6, and related T-box proteins. TBX6 is a T-box transcription factor which plays an essential role in the fate determination of axial stem to become either neural or mesodermal. It also plays an essential role in the regulation of left/right patterning in mouse embryos, through effects on nodal cilia and perinodal signaling. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
VRMSLENAELWKQFSSVGTEMIITKAGRRMFPQLRVSVSGLDPEARYLLLLDVVPVDGSRYRWQGNSWEA
SGKAEPRLPDRVYIHPDSPATGAHWMRQPISFHRAKLTNNTLDPHGHIILHSMHRYQPRVHVVRARDVLS
WGGGCASFTFPETQFITVTAYQNPKITQLKINSNPFAKGFRE
>gnl|CDD|410323 cd20197, T-box_VegT-like, DNA-binding domain of Xenopus VegT and related T-box proteins. VegT, (also known as Antipodean, Brat and Xombi), is a T-box transcription factor required in early Xenopus embryos for the formation of both, the mesoderm and endoderm germ layers. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
VRASLEDQDLWKKFHQIGTEMIITKSGRRMFPQCKIRVSGLLPYAKYVMLVDFVPVDNFRYKWNKDQWEV
AGKAEPQPPCRTYVHPDSPAPGSHWMKQPISFQKLKLTNNTLDQHGHIILHSMHRYQPRFHIVQADDLFN
VRWSLFQVFSFPETVFTAVTAYQNEKITKLKIDNNPFAKGFRE
>gnl|CDD|410324 cd20198, T-box_TBX15-like, DNA-binding domain of T-box transcription factor 15 and related T-box proteins. TBX15 (also known as TBX14) plays an important role in the development of the skeleton of the limb, vertebral column and head, possibly through its control of the number of mesenchymal precursor cells and chondrocytes. TBX15 also plays a role in the differentiation of brown and brite adipocytes. This subgroup belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
TSSMEEIQVELQCADLWKRFHDIGTEMIITKAGRRMFPAMRVKITGLDPHQQYYIAMDIVPVDNKRYRYV
YHSSKWMVAGNADSPVPPRVYIHPDSLASGDTWMRQVVSFDKLKLTNNELDDQGHIILHSMHKYQPRVHV
IRKDFSSDLSPTKPVPTGDGVKTFSFPETVFTTVTAYQNQQITRLKIDRNPFAKGFRD
>gnl|CDD|410325 cd20199, T-box_TBX18_like, DNA-binding domain of T-box transcription factor 18 and related T-box proteins. TBX18 acts as a transcription repressor involved in the developmental processes of a variety of tissues and organs, including the ureter, vertebral column. epicardium and coronary vessels. TBX18 is important for the development of the head portion of the sino atrial node (SAN); SAN is the pacemaker region of the heart that initiates each heartbeat. This subgroup belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
GEEVRVDLQGADLWKRFHEIGTEMIITKAGRRMFPAMRVKITGLDPHQQYYIAMDIVPVDNKRYRYVYHS
SKWMVAGNADSPVPPRVYIHPDSPASGETWMRQVISFDKLKLTNNELDDQGHIILHSMHKYQPRVHVIRK
ECGEELSPVKPIPSGEGVKAFSFPETVFTTVTAYQNQQITRLKIDRNPFAKGFRD
>gnl|CDD|410326 cd20200, T-box_TBX22-like, DNA-binding domain of T-box transcription factor 22 and related T-box proteins. TBX22 is a transcriptional regulator involved in developmental processes. Mutations in the T-Box transcription factor gene TBX22 are found in X-linked Cleft Palate with or without Ankyloglossia syndrome (CPX syndrome). TBX22 mutation is also associated with cleft lip and palate, and tooth agenesis. This subgroup belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
RKVQVELQGSELWKRFHEIGTEMIITKAGRRMFPSVRVKVKGLDPLKQYYIAMDVVPVDSKRYRYVYHSS
QWMVAGNTDHSCITPRLYVHPDSPCSGETWMRQIISFDRVKLTNNEMDDKGHIILQSMHKYKPRVHVILQ
DSRFDLSQIQSLPAEGVKTFSFPETEFTTVTAYQNQQITKLKIDRNPFAKGFRD
>gnl|CDD|410327 cd20201, T-box_TBX19-like, DNA-binding domain of T-box transcription factor 19 and related T-box proteins. Tbx19 (also known as Tpit) is a T-box factor restricted to two pituitary (pro-opiomelanocortin) POMC-expressing lineages, the corticotrophs and melanotrophs; it controls terminal differentiation of these lineages. TBX19 activates POMC gene transcription with the cooperation of another transcription factor Pitx1. Mutations of the human TPIT gene cause early onset pituitary adrenocorticotrophic hormone (ACTH) deficiency. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
PTEKQLQVSLEDAELWQRFKEVTNEMIVTKNGRRMFPVLKISVSGLDPNAMYSFLLDFAPADGHRWKYVN
GEWVPAGKPEPHSHSCVYIHPDSPNFGAHWMKAPISFSKVKLTNKLNGGGQIMLNSLHKYEPQIHIVRVG
GPHRMVTNCSFPETQFIAVTAYQNEEITALKIKYNPFAKAFLD
>gnl|CDD|410328 cd20202, T-box_TBXT, DNA-binding domain of T-box transcription factor T and related T-box proteins. TBXT, also known as Brachyury protein, or protein T, is a transcription factor needed for posterior mesoderm formation and differentiation as well as for the notochord development during embryogenesis. It binds to a 24 base-pair (bp) palindromic site (called the T site) and activates gene transcription when bound to such a site. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. TBXT is the founding member of the T-box family, members of which share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
ELKVSLEESELWLRFKELTNEMIVTKNGRRMFPVLKVNVSGLDPNAMYSFLLDFVAADNHRWKYVNGEWV
PGGKPEPQAPSCVYIHPDSPNFGAHWMKAPVSFSKVKLTNKLNGGGQIMLNSLHKYEPRIHIVRVGGPQR
MITSHSFPETQFIAVTAYQNEEITALKIKYNPFAKAFLD
>gnl|CDD|410329 cd20203, T-box_TBX21, DNA-binding domain of T-box transcription factor 21 and related T-box proteins. TBX21 (also known as T-cell-specific T-box transcription factor T-bet or transcription factor TBLYM) is a lineage-defining transcription factor which directs T helper type 1 (Th1) cell differentiation. It initiates Th1 lineage development from naive T helper precursor cells both by initiating the Th1 genetic programs and by inhibiting the opposing Th2 and Th17 lineage-commitment programs. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
KLQVLLNNHPLWSKFHKHQTEMIITKQGRRMFPFLSFNLTGLDPTAHYNVYVDVVLADQHHWRYQGGKWV
QCGKAEGNMPGNRLYVHPDSPNTGAHWMRQEVSFGKLKLTNNKGASNNVTQMIVLQSLHKYQPRLHIVEV
KEGETEEAYSSSKTHTFTFPETQFIAVTAYQNAEITQLKIDHNPFAKGFRD
>gnl|CDD|410330 cd20204, T-box_TBR1, DNA-binding domain of T-box brain protein 1 and related T-box proteins. TBR1 (also known as T-brain-1 or TES-56) is a neuron-specific transcription factor of the T-box family and involved in forebrain development. It has been recognized as a high-confidence risk gene for autism spectrum disorders (ASD); it regulates the expression of ASD-related genes that are critical for cortical development. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
KAQVYLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNISGLDPTAHYNIFVDVILADPNHWRFQGGKWV
PCGKADTNVQGNRVYMHPDSPNTGAHWMRQEISFGKLKLTNNKGASNNNGQMVVLQSLHKYQPRLHVVEV
NEDGTEDTSQPGRVQTFTFPETQFIAVTAYQNTDITQLKIDHNPFAKGFRD
>gnl|CDD|410331 cd20205, T-box_TBR2, DNA-binding domain of T-box brain protein 2 and related T-box proteins. TBR2 (also known as Eomesodermin, Eomes, or T-brain-2) is a member of the T-box family of transcription factors and is associated with neurogenesis, cardiogenesis and tumor immune response. This subfamily belongs to the T-box family of transcription factors which plays a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns
RAQVYLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNITGLNPTAHYNVFVEVVLADPNHWRFQGGKWV
TCGKADNNMQGNKVYVHPESPNTGAHWMRQEISFGKLKLTNNKGANNNNTQMIVLQSLHKYQPRLHIVEV
SEDGVEDLNDSSKTQTFTFPENQFIAVTAYQNTDITQLKIDHNPFAKGFRD
>gnl|CDD|411001 cd20206, YbbR, YbbR domain. YbbR domains occur as tandem repeats or in architectures together with other domains. Putative roles in cell growth, cell division, and/or virulence have been suggested for this domain
PLEVRNLPEGLVVTGEPETVRVRVRGPRSLLANLSPDDIKAYVDLSGAKEGEHTLPVQVDLPPGVEVVSV
SPSTVTVTL
>gnl|CDD|380908 cd20207, Bbox2_GefO-like, B-box-type 2 zinc finger found in Ras guanine nucleotide exchange factor O (GefO) and similar proteins. Ras guanine-nucleotide exchange factors (RasGEFs) activate Ras by catalyzing the replacement of GDP with GTP, and thus lie near the top of many signaling pathways. They are important for signaling in development and chemotaxis in many organisms. Ras guanine nucleotide exchange factor O (GefO), also known as RasGEF domain-containing protein O, is faintly expressed during development of Dictyostelium discoideum. It contains a C3HC4-type RING finger, a B-box motif that shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs), a REM (Ras exchanger motif) domain, and a # RasGEF domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif
VVCSKHNEHMLDKFCKDCSAPVCENCVLTTHAGHNVEPIT
>gnl|CDD|380909 cd20208, Bbox1_DUF2009, B-box-type 1 zinc finger found in DUF2009 domain-containing proteins and similar proteins. This group is composed of uncharacterized proteins containing a zinc finger B-box domain and a DUF2009 domain, and similar zinc finger B-box domain-containing proteins. The B-box motif shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif
MCIECEDQPAEVRCEECGDEFCEVCFQSQHRKGKRRLHSFRPV
>gnl|CDD|380784 cd20214, PFM_CEL-III-like, pore-forming module of hemolytic lectin Cucumaria echinate CEL-III and similar aerolysin-type beta-barrel pore-forming proteins. Cucumaria echinate CEL-III is a Ca(2+)-dependent and galactose-specific lectin, which is cytotoxic to some cultured cell lines, has strong hemolytic activity toward human and rabbit erythrocytes, and anti-malarial activity. Hemolysis results from ion-permeable pores formed from CEL-III oligomers in the target cell membrane. Members of this group includes CEL-III isoforms: CEL-III-L1, CEL-III-L2, CEL-III-S1, CEL-III-S2, and CEL-III-LS1. Many proteins belonging to this group have two N-terminal ricin-type carbohydrate-binding domains which adopt beta-trefoil folds. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). The CEL-III oligomer in the membrane may be composed of six monomers
DDWEVPTATWNMVGCNQNGKVSQQISNTISFSSTVTAGVAVEVSSTIEKGVIFAKASVSVKVSASLSKAW
TNSQSGTTAITYTCDNYDSDEEFTRGCMWQLAIETTEVKSGDLLVWNPQIVKCT
>gnl|CDD|380785 cd20215, PFM_LSL-like, pore-forming module of Laetiporus sulphureus LSL lectin and similar aerolysin-type beta-barrel pore-forming proteins. LSL is a lectin, produced by the parasitic mushroom Laetiporus sulphureus, which exhibits hemolytic and hemagglutinating activities. Members of this family belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin)
EDMEIVSVEYDLDKGKILSSTPLVLARQTLRNDTDVEQTMSFTLTETETHTSTFEYTAGFTITVGTSFKA
GIPGVAEGKIKVDTTVSNEWKWGESTTFTKTYTATFPVKAPPGSTVRAVATVTKSNLEVPFTMTLKSKST
GYEVETKGIYRGVSTWNLRTAIRE
>gnl|CDD|380786 cd20216, PFM_HFR-2-like, pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel pore-forming proteins. HFR-2 is a wheat cytolytic toxin which may normally function in defense against certain insects or pathogens. The Hfr-2 gene is upregulated in virulent Hessian fly larval feedingdouble dagger. The HFR-2 protein may insert in plant cell membranes at the feeding sites and by forming pores provide water, ions and other small nutritive molecules to the developing larvae. This group also contains FEM32, a flower-specific lectin-like protein from the dioecious plant Rumex acetosa, which alters flower development and induces male sterility in transgenic tobacco. It has been suggested that the FEM32 gene activates some form of programmed cell death (PCD), a process that could be mediated by the action of its lectin domains for binding to specific glycoproteins on the cell membrane and facilitated by the formation of pore structures in the membranes and the subsequent leakage of the cytosolic content through its pore-forming aerolysin domain. Most proteins belonging to this group have N-terminal agglutatin (also known as amaranthin) lectin domains; most have two agglutatin domains, in combination with one aerolysin domain. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin)
IYDEKVLTLATGEATNNTSEPQTVTLKLSYTDTKTSTWNSSVSLKLGVKTTISAGVPFIVDGKIEISAEF
SGSYEWGETKTETTEVETTYTVTVPPMTKVTVTLIATRGSCDVPFSYTQRDTLTNGTTVTYEKDDGLYTG
VNSYNFKYETKE
>gnl|CDD|380787 cd20217, PFM_agglutinin-like, pore-forming module (PFM) of uncharacterized proteins which have agglutatin domain(s), and similar aerolysin-type beta-barrel pore-forming proteins. Most proteins belonging to this group have an N-terminal agglutatin (also known as amaranthin) lectin domain; some have fascin-like domains which adopt a beta-trefoil topology. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin)
PLVVGQGSATNNGSEPADMQVQVTLTETVSTSRTWSNSFTFSQSISTTFTAGVPEIASAETTITIGAEQT
FGTEWGETTEEAVQFQSTYLVKDVPPGEEATVTVECSTGKCRVPFTYKTRDTRLDGVDRPTVDEIDGVFE
GVSAYNTRAV
>gnl|CDD|380788 cd20218, PFM_aerolysin, pore-forming module of aerolysin and similar aerolysin-type beta-barrel pore-forming proteins. Aerolysin is a cytosolic bacterial toxin that forms pores in the host membrane, leading to destruction of the membrane permeability barrier and host cell death. Another member of this family is alpha-toxin from Clostridium septicum, the main virulence factor of this bacterium, known for causing non-traumatic gas gangrene. Many proteins belonging to this group have an N-terminal APT domain; an APT domain is the N-terminal domain of aerolysin and pertussis toxin and has a type-C lectin-like fold. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding 
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